LOCUS       NP_001423335             778 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423335 XP_063122300
VERSION     NP_001423335.1
DBSOURCE    REFSEQ: accession NM_001436406.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_063122300.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.35513.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..778
                     /product="transducin-like enhancer protein 3 isoform 5"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=83908
     Region          18..142
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          139..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          141..208
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          193..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          209..277
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          234..237
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <260..478
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            284
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          490..528
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <491..776
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          495..534
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          536..575
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          542..580
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          580..619
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          585..621
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          622..661
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          628..663
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          663..702
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          668..701
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          704..743
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          709..743
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          745..777
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          750..774
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..778
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436406.1:1076..3412"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqlqaq hlshathgpp vqlpphpsgl qppgippvtg sssgllalga
      181 lgsqahlavk deknhheldh reresstnns vspseslras ekhrgsadys meakkrkaee
      241 kdslsrydsd gdksddlvvd vsnedpatpr vspahsppen gldkarglkk daptspasva
      301 sssstpsskt kdlghndkss tpglksntpt prndaptpgt sttpglrsmp gkppgmdpia
      361 salrtpislt ssyaapfamm shhemngslt spsayaglhn ipsqmsaaaa aaaaaygrsp
      421 mvsfgavgfd phppmratgl psslasipgg kpaysfhvsa dgqmqpvpfp hdalagpgip
      481 rharqintls hgevvcavti snptrhvytg gkgcvkiwdi sqpgskspis qldclnrdny
      541 irsckllpdg rtlivggeas tltiwdlasp tprikaelts sapacyalai spdakvcfsc
      601 csdgniavwd lhnqtlvrqf qghtdgasci dishdgtklw tggldntvrs wdlregrqlq
      661 qhdftsqifs lgycptgewl avgmessnve vlhhtkpdky qlhlhescvl slkfaycgkw
      721 fvstgkdnll nawrtpygas ifqskesssv lscdisaddk yivtgsgdkk atvyeviy
//
LOCUS       NP_001423322             211 aa            linear   ROD 11-MAR-2025
DEFINITION  platelet-derived growth factor subunit A isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001423322
VERSION     NP_001423322.1
DBSOURCE    REFSEQ: accession NM_001436393.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Rashid,F.N., Clayton,Z.E., Ogawa,M., Perdomo,J., Hume,R.D.,
            Kizana,E. and Chong,J.J.H.
  TITLE     Platelet derived growth factor-A (Pdgf-a) gene transfer modulates
            scar composition and improves left ventricular function after
            myocardial infarction
  JOURNAL   Int J Cardiol 341, 24-30 (2021)
   PUBMED   34265313
  REMARK    GeneRIF: Platelet derived growth factor-A (Pdgf-a) gene transfer
            modulates scar composition and improves left ventricular function
            after myocardial infarction.
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Connolly,N.P., Stokum,J.A., Schneider,C.S., Ozawa,T., Xu,S.,
            Galisteo,R., Castellani,R.J., Kim,A.J., Simard,J.M., Winkles,J.A.,
            Holland,E.C. and Woodworth,G.F.
  TITLE     Genetically engineered rat gliomas: PDGF-driven tumor initiation
            and progression in tv-a transgenic rats recreate key features of
            human brain cancer
  JOURNAL   PLoS One 12 (3), e0174557 (2017)
   PUBMED   28358926
  REMARK    GeneRIF: an Ntv-a transgenic rat colony was established and used to
            study glial brain tumors driven by two well-characterized oncogenic
            gene transformations, PDGFA overexpression and p53 depletion.
            Combined PDGFA and p53 alterations resulted in large, heterogeneous
            tumors in all affected animals
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Shepherd,J.A., Stamper,E., Matheson,P.J., Galganski,L.,
            Garrison,R.N., Madden,K. and Downard,C.D.
  TITLE     Alterations in platelet-derived growth factor expression in the
            pathophysiology of necrotizing enterocolitis
  JOURNAL   J Surg Res 198 (2), 377-383 (2015)
   PUBMED   25899145
  REMARK    GeneRIF: expression altered in experimental Necrotizing
            enterocolitis
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Ha,J.M., Yun,S.J., Kim,Y.W., Jin,S.Y., Lee,H.S., Song,S.H.,
            Shin,H.K. and Bae,S.S.
  TITLE     Platelet-derived growth factor regulates vascular smooth muscle
            phenotype via mammalian target of rapamycin complex 1
  JOURNAL   Biochem Biophys Res Commun 464 (1), 57-62 (2015)
   PUBMED   26032503
  REMARK    GeneRIF: PDGF regulates vascular smooth muscle phenotype via
            mammalian target of rapamycin complex 1.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Bryckaert,M.C., Rendu,F., Tobelem,G. and Wasteson,A.
  TITLE     Collagen-induced binding to human platelets of platelet-derived
            growth factor leading to inhibition of P43 and P20 phosphorylation
  JOURNAL   J Biol Chem 264 (8), 4336-4341 (1989)
   PUBMED   2538439
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Matsui,T., Heidaran,M., Miki,T., Popescu,N., La Rochelle,W.,
            Kraus,M., Pierce,J. and Aaronson,S.
  TITLE     Isolation of a novel receptor cDNA establishes the existence of two
            PDGF receptor genes
  JOURNAL   Science 243 (4892), 800-804 (1989)
   PUBMED   2536956
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Escobedo,J.A., Navankasatussas,S., Cousens,L.S., Coughlin,S.R.,
            Bell,G.I. and Williams,L.T.
  TITLE     A common PDGF receptor is activated by homodimeric A and B forms of
            PDGF
  JOURNAL   Science 240 (4858), 1532-1534 (1988)
   PUBMED   2836953
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Womer,R.B., Frick,K., Mitchell,C.D., Ross,A.H., Bishayee,S. and
            Scher,C.D.
  TITLE     PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma
            cells but does not stimulate cell replication
  JOURNAL   J Cell Physiol 132 (1), 65-72 (1987)
   PUBMED   2439522
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Heldin,C.H., Westermark,B. and Wasteson,A.
  TITLE     Platelet-derived growth factor: purification and partial
            characterization
  JOURNAL   Proc Natl Acad Sci U S A 76 (8), 3722-3726 (1979)
   PUBMED   291037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061731.1, SRR26643291.32143.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..211
                     /product="platelet-derived growth factor subunit A isoform
                     1 precursor"
                     /note="PDGF subunit A; Platelet-derived growth factor A
                     chain; platelet derived growth factor, alpha;
                     platelet-derived growth factor alpha polypeptide"
                     /calculated_mol_wt=22029
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2177
     Region          21..95
                     /region_name="PDGF_N"
                     /note="Platelet-derived growth factor, N terminal region;
                     pfam04692"
                     /db_xref="CDD:461394"
     mat_peptide     86..204
                     /product="Platelet-derived growth factor subunit A.
                     /id=PRO_0000023363"
                     /note="propagated from UniProtKB/Swiss-Prot (P28576.2)"
                     /calculated_mol_wt=13656
     Region          94..181
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(94..97,133,135..138,153..156)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(96,129,133,140,177,179)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(123,132)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28576.2)"
     Region          158..162
                     /region_name="Receptor binding site.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P28576.2)"
     CDS             1..211
                     /gene="Pdgfa"
                     /gene_synonym="PDGF-1; PDGFACP"
                     /coded_by="NM_001436393.1:174..809"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25266"
                     /db_xref="RGD:3282"
ORIGIN      
        1 mrtwacllll gcgylahala eeaeipreli erlarsqihs irdlqrllei dsvgaedale
       61 tnlrahgsht vkhvpekrpv pirrkrsiee aipavcktrt viyeiprsqv dptsanfliw
      121 ppcvevkrct gccntssvkc qpsrvhhrsv kvakveyvrk kpklkevqvr leehlecaca
      181 tsnlnpdhre eetgrrresg kkrkrkrlkp t
//
LOCUS       NP_001423336             777 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423336 XP_006243276
VERSION     NP_001423336.1
DBSOURCE    REFSEQ: accession NM_001436407.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243276.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.29582.1,
                                           SRR26643288.34034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..777
                     /product="transducin-like enhancer protein 3 isoform 6"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=83876
     Region          18..143
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          140..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          142..209
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          194..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          210..278
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          235..238
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <261..477
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            285
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          489..527
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <490..775
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          494..533
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          535..574
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          541..579
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          579..618
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          584..620
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          621..660
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          627..662
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          662..701
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          667..700
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          703..742
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          708..742
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          744..776
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          749..773
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..777
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436407.1:1076..3409"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg
      181 algsqahlav kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae
      241 ekdslsryds dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv
      301 asssstpssk tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi
      361 gimasalrtp isltssyaap fammshhemn gsltspsaya glhnipsqms aaaaaaaaay
      421 grspmvgfdp hppmratglp sslasipggk paysfhvsad gqmqpvpfph dalagpgipr
      481 harqintlsh gevvcavtis nptrhvytgg kgcvkiwdis qpgskspisq ldclnrdnyi
      541 rsckllpdgr tlivggeast ltiwdlaspt prikaeltss apacyalais pdakvcfscc
      601 sdgniavwdl hnqtlvrqfq ghtdgascid ishdgtklwt ggldntvrsw dlregrqlqq
      661 hdftsqifsl gycptgewla vgmessnvev lhhtkpdkyq lhlhescvls lkfaycgkwf
      721 vstgkdnlln awrtpygasi fqskesssvl scdisaddky ivtgsgdkka tvyeviy
//
LOCUS       NP_001423343             763 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 12 [Rattus norvegicus].
ACCESSION   NP_001423343 XP_006243283
VERSION     NP_001423343.1
DBSOURCE    REFSEQ: accession NM_001436414.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243283.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.33957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..763
                     /product="transducin-like enhancer protein 3 isoform 12"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82385
     Region          18..132
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          129..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          131..198
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          183..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          199..267
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          224..227
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <250..463
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          268..443
                     /region_name="SP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            274
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          475..513
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <476..761
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          480..519
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          521..560
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          527..565
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          565..604
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          570..606
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          607..646
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          613..648
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          648..687
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          653..686
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          689..728
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          694..728
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          730..762
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          735..759
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..763
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436414.1:1076..3367"
                     /note="isoform 12 is encoded by transcript variant 13"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqlqaq hlshathgpp vqlpphpsgl qppgippvtg sssgllalga lgsqahlavk
      181 deknhheldh reresstnns vspseslras ekhrgsadys meakkrkaee kdslsrydsd
      241 gdksddlvvd vsnedpatpr vspahsppen gldkarglkk daptspasva sssstpsskt
      301 kdlghndkss tpglksntpt prndaptpgt sttpglrsmp gkppgmdpia salrtpislt
      361 ssyaapfamm shhemngslt spsayaglhn ipsqmsaaaa aaaaaygrsp mvgfdphppm
      421 ratglpssla sipggkpays fhvsadgqmq pvpfphdala gpgiprharq intlshgevv
      481 cavtisnptr hvytggkgcv kiwdisqpgs kspisqldcl nrdnyirsck llpdgrtliv
      541 ggeastltiw dlasptprik aeltssapac yalaispdak vcfsccsdgn iavwdlhnqt
      601 lvrqfqghtd gascidishd gtklwtggld ntvrswdlre grqlqqhdft sqifslgycp
      661 tgewlavgme ssnvevlhht kpdkyqlhlh escvlslkfa ycgkwfvstg kdnllnawrt
      721 pygasifqsk esssvlscdi saddkyivtg sgdkkatvye viy
//
LOCUS       NP_001423334             779 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423334 XP_006243275
VERSION     NP_001423334.1
DBSOURCE    REFSEQ: accession NM_001436405.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 779)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 779)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243275.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.28649.1,
                                           SRR26643294.32979.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..779
                     /product="transducin-like enhancer protein 3 isoform 4"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=84036
     Region          18..143
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          140..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          142..209
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          194..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          210..278
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          235..238
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <261..479
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            285
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          491..529
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <492..777
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          496..535
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          537..576
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          543..581
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          581..620
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          586..622
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          623..662
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          629..664
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          664..703
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          669..702
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          705..744
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          710..744
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          746..778
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          751..775
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..779
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436405.1:1076..3415"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg
      181 algsqahlav kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae
      241 ekdslsryds dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv
      301 asssstpssk tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi
      361 asalrtpisl tssyaapfam mshhemngsl tspsayaglh nipsqmsaaa aaaaaaygrs
      421 pmvsfgavgf dphppmratg lpsslasipg gkpaysfhvs adgqmqpvpf phdalagpgi
      481 prharqintl shgevvcavt isnptrhvyt ggkgcvkiwd isqpgskspi sqldclnrdn
      541 yirsckllpd grtlivggea stltiwdlas ptprikaelt ssapacyala ispdakvcfs
      601 ccsdgniavw dlhnqtlvrq fqghtdgasc idishdgtkl wtggldntvr swdlregrql
      661 qqhdftsqif slgycptgew lavgmessnv evlhhtkpdk yqlhlhescv lslkfaycgk
      721 wfvstgkdnl lnawrtpyga sifqskesss vlscdisadd kyivtgsgdk katvyeviy
//
LOCUS       NP_001423341             767 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001423341 XP_006243281
VERSION     NP_001423341.1
DBSOURCE    REFSEQ: accession NM_001436412.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243281.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.31486.1,
                                           SRR26643297.28653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..767
                     /product="transducin-like enhancer protein 3 isoform 11"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82814
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..467
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          479..517
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <480..765
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          484..523
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          525..564
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          531..569
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          569..608
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          574..610
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          611..650
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          617..652
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          652..691
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          657..690
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          693..732
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          698..732
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          734..766
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          739..763
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..767
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436412.1:1076..3379"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi gimasalrtp
      361 isltssyaap fammshhemn gsltspsaya glhnipsqms aaaaaaaaay grspmvgfdp
      421 hppmratglp sslasipggk paysfhvsad gqmqpvpfph dalagpgipr harqintlsh
      481 gevvcavtis nptrhvytgg kgcvkiwdis qpgskspisq ldclnrdnyi rsckllpdgr
      541 tlivggeast ltiwdlaspt prikaeltss apacyalais pdakvcfscc sdgniavwdl
      601 hnqtlvrqfq ghtdgascid ishdgtklwt ggldntvrsw dlregrqlqq hdftsqifsl
      661 gycptgewla vgmessnvev lhhtkpdkyq lhlhescvls lkfaycgkwf vstgkdnlln
      721 awrtpygasi fqskesssvl scdisaddky ivtgsgdkka tvyeviy
//
LOCUS       NP_445852                764 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_445852
VERSION     NP_445852.1
DBSOURCE    REFSEQ: accession NM_053400.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF186092.1, SRR26643299.35512.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..764
                     /product="transducin-like enhancer protein 3 isoform 2"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82513
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..464
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          269..444
                     /region_name="SP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          476..514
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <477..762
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          481..520
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          522..561
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          528..566
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          566..605
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          571..607
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          608..647
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          614..649
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          649..688
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          654..687
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          690..729
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          695..729
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          731..763
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          736..760
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..764
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_053400.3:1076..3370"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi asalrtpisl
      361 tssyaapfam mshhemngsl tspsayaglh nipsqmsaaa aaaaaaygrs pmvgfdphpp
      421 mratglpssl asipggkpay sfhvsadgqm qpvpfphdal agpgiprhar qintlshgev
      481 vcavtisnpt rhvytggkgc vkiwdisqpg skspisqldc lnrdnyirsc kllpdgrtli
      541 vggeastlti wdlasptpri kaeltssapa cyalaispda kvcfsccsdg niavwdlhnq
      601 tlvrqfqght dgascidish dgtklwtggl dntvrswdlr egrqlqqhdf tsqifslgyc
      661 ptgewlavgm essnvevlhh tkpdkyqlhl hescvlslkf aycgkwfvst gkdnllnawr
      721 tpygasifqs kesssvlscd isaddkyivt gsgdkkatvy eviy
//
LOCUS       NP_001423340             769 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423340 XP_063122302
VERSION     NP_001423340.1
DBSOURCE    REFSEQ: accession NM_001436411.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_063122302.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.28652.1,
                                           SRR26643299.35515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..769
                     /product="transducin-like enhancer protein 3 isoform 1"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82974
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..469
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          481..519
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <482..767
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          486..525
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          527..566
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          533..571
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          571..610
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          576..612
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          613..652
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          619..654
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          654..693
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          659..692
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          695..734
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          700..734
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          736..768
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          741..765
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..769
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436411.1:901..3210"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi asalrtpisl
      361 tssyaapfam mshhemngsl tspsayaglh nipsqmsaaa aaaaaaygrs pmvsfgavgf
      421 dphppmratg lpsslasipg gkpaysfhvs adgqmqpvpf phdalagpgi prharqintl
      481 shgevvcavt isnptrhvyt ggkgcvkiwd isqpgskspi sqldclnrdn yirsckllpd
      541 grtlivggea stltiwdlas ptprikaelt ssapacyala ispdakvcfs ccsdgniavw
      601 dlhnqtlvrq fqghtdgasc idishdgtkl wtggldntvr swdlregrql qqhdftsqif
      661 slgycptgew lavgmessnv evlhhtkpdk yqlhlhescv lslkfaycgk wfvstgkdnl
      721 lnawrtpyga sifqskesss vlscdisadd kyivtgsgdk katvyeviy
//
LOCUS       NP_001423342             767 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001423342 XP_063122304
VERSION     NP_001423342.1
DBSOURCE    REFSEQ: accession NM_001436413.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_063122304.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.45730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..767
                     /product="transducin-like enhancer protein 3 isoform 11"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82814
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..467
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          479..517
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <480..765
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          484..523
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          525..564
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          531..569
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          569..608
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          574..610
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          611..650
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          617..652
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          652..691
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          657..690
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          693..732
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          698..732
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          734..766
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          739..763
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..767
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436413.1:901..3204"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi gimasalrtp
      361 isltssyaap fammshhemn gsltspsaya glhnipsqms aaaaaaaaay grspmvgfdp
      421 hppmratglp sslasipggk paysfhvsad gqmqpvpfph dalagpgipr harqintlsh
      481 gevvcavtis nptrhvytgg kgcvkiwdis qpgskspisq ldclnrdnyi rsckllpdgr
      541 tlivggeast ltiwdlaspt prikaeltss apacyalais pdakvcfscc sdgniavwdl
      601 hnqtlvrqfq ghtdgascid ishdgtklwt ggldntvrsw dlregrqlqq hdftsqifsl
      661 gycptgewla vgmessnvev lhhtkpdkyq lhlhescvls lkfaycgkwf vstgkdnlln
      721 awrtpygasi fqskesssvl scdisaddky ivtgsgdkka tvyeviy
//
LOCUS       NP_036933                196 aa            linear   ROD 11-MAR-2025
DEFINITION  platelet-derived growth factor subunit A isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_036933
VERSION     NP_036933.2
DBSOURCE    REFSEQ: accession NM_012801.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Rashid,F.N., Clayton,Z.E., Ogawa,M., Perdomo,J., Hume,R.D.,
            Kizana,E. and Chong,J.J.H.
  TITLE     Platelet derived growth factor-A (Pdgf-a) gene transfer modulates
            scar composition and improves left ventricular function after
            myocardial infarction
  JOURNAL   Int J Cardiol 341, 24-30 (2021)
   PUBMED   34265313
  REMARK    GeneRIF: Platelet derived growth factor-A (Pdgf-a) gene transfer
            modulates scar composition and improves left ventricular function
            after myocardial infarction.
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Connolly,N.P., Stokum,J.A., Schneider,C.S., Ozawa,T., Xu,S.,
            Galisteo,R., Castellani,R.J., Kim,A.J., Simard,J.M., Winkles,J.A.,
            Holland,E.C. and Woodworth,G.F.
  TITLE     Genetically engineered rat gliomas: PDGF-driven tumor initiation
            and progression in tv-a transgenic rats recreate key features of
            human brain cancer
  JOURNAL   PLoS One 12 (3), e0174557 (2017)
   PUBMED   28358926
  REMARK    GeneRIF: an Ntv-a transgenic rat colony was established and used to
            study glial brain tumors driven by two well-characterized oncogenic
            gene transformations, PDGFA overexpression and p53 depletion.
            Combined PDGFA and p53 alterations resulted in large, heterogeneous
            tumors in all affected animals
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Shepherd,J.A., Stamper,E., Matheson,P.J., Galganski,L.,
            Garrison,R.N., Madden,K. and Downard,C.D.
  TITLE     Alterations in platelet-derived growth factor expression in the
            pathophysiology of necrotizing enterocolitis
  JOURNAL   J Surg Res 198 (2), 377-383 (2015)
   PUBMED   25899145
  REMARK    GeneRIF: expression altered in experimental Necrotizing
            enterocolitis
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Ha,J.M., Yun,S.J., Kim,Y.W., Jin,S.Y., Lee,H.S., Song,S.H.,
            Shin,H.K. and Bae,S.S.
  TITLE     Platelet-derived growth factor regulates vascular smooth muscle
            phenotype via mammalian target of rapamycin complex 1
  JOURNAL   Biochem Biophys Res Commun 464 (1), 57-62 (2015)
   PUBMED   26032503
  REMARK    GeneRIF: PDGF regulates vascular smooth muscle phenotype via
            mammalian target of rapamycin complex 1.
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Bryckaert,M.C., Rendu,F., Tobelem,G. and Wasteson,A.
  TITLE     Collagen-induced binding to human platelets of platelet-derived
            growth factor leading to inhibition of P43 and P20 phosphorylation
  JOURNAL   J Biol Chem 264 (8), 4336-4341 (1989)
   PUBMED   2538439
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Matsui,T., Heidaran,M., Miki,T., Popescu,N., La Rochelle,W.,
            Kraus,M., Pierce,J. and Aaronson,S.
  TITLE     Isolation of a novel receptor cDNA establishes the existence of two
            PDGF receptor genes
  JOURNAL   Science 243 (4892), 800-804 (1989)
   PUBMED   2536956
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Escobedo,J.A., Navankasatussas,S., Cousens,L.S., Coughlin,S.R.,
            Bell,G.I. and Williams,L.T.
  TITLE     A common PDGF receptor is activated by homodimeric A and B forms of
            PDGF
  JOURNAL   Science 240 (4858), 1532-1534 (1988)
   PUBMED   2836953
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Womer,R.B., Frick,K., Mitchell,C.D., Ross,A.H., Bishayee,S. and
            Scher,C.D.
  TITLE     PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma
            cells but does not stimulate cell replication
  JOURNAL   J Cell Physiol 132 (1), 65-72 (1987)
   PUBMED   2439522
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Heldin,C.H., Westermark,B. and Wasteson,A.
  TITLE     Platelet-derived growth factor: purification and partial
            characterization
  JOURNAL   Proc Natl Acad Sci U S A 76 (8), 3722-3726 (1979)
   PUBMED   291037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Nov 27, 2020 this sequence version replaced NP_036933.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L06238.1, SRR22582419.1725151.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..196
                     /product="platelet-derived growth factor subunit A isoform
                     2 precursor"
                     /note="PDGF subunit A; Platelet-derived growth factor A
                     chain; platelet derived growth factor, alpha;
                     platelet-derived growth factor alpha polypeptide"
                     /calculated_mol_wt=20179
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2177
     Region          21..95
                     /region_name="PDGF_N"
                     /note="Platelet-derived growth factor, N terminal region;
                     pfam04692"
                     /db_xref="CDD:461394"
     Region          94..181
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(94..97,133,135..138,153..156)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(96,129,133,140,177,179)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(123,132)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28576.2)"
     Region          158..162
                     /region_name="Receptor binding site.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P28576.2)"
     CDS             1..196
                     /gene="Pdgfa"
                     /gene_synonym="PDGF-1; PDGFACP"
                     /coded_by="NM_012801.3:483..1073"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:25266"
                     /db_xref="RGD:3282"
ORIGIN      
        1 mrtwacllll gcgylahala eeaeipreli erlarsqihs irdlqrllei dsvgaedale
       61 tnlrahgsht vkhvpekrpv pirrkrsiee aipavcktrt viyeiprsqv dptsanfliw
      121 ppcvevkrct gccntssvkc qpsrvhhrsv kvakveyvrk kpklkevqvr leehlecaca
      181 tsnlnpdhre eetdvr
//
LOCUS       NP_001423333             782 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423333 XP_008764569
VERSION     NP_001423333.1
DBSOURCE    REFSEQ: accession NM_001436404.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_008764569.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.32010.1,
                                           SRR26643292.33958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..782
                     /product="transducin-like enhancer protein 3 isoform 3"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=84337
     Region          18..143
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          <261..482
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          <495..780
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          499..538
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          546..584
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          589..625
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          632..667
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          672..705
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          713..747
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          754..778
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..782
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436404.1:1076..3424"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg
      181 algsqahlav kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae
      241 ekdslsryds dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv
      301 asssstpssk tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi
      361 gimasalrtp isltssyaap fammshhemn gsltspsaya glhnipsqms aaaaaaaaay
      421 grspmvsfga vgfdphppmr atglpsslas ipggkpaysf hvsadgqmqp vpfphdalag
      481 pgiprharqi ntlshgevvc avtisnptrh vytggkgcvk iwdisqpgsk spisqldcln
      541 rdnyirsckl lpdgrtlivg geastltiwd lasptprika eltssapacy alaispdakv
      601 cfsccsdgni avwdlhnqtl vrqfqghtdg ascidishdg tklwtggldn tvrswdlreg
      661 rqlqqhdfts qifslgycpt gewlavgmes snvevlhhtk pdkyqlhlhe scvlslkfay
      721 cgkwfvstgk dnllnawrtp ygasifqske sssvlscdis addkyivtgs gdkkatvyev
      781 iy
//
LOCUS       NP_001423338             773 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001423338 XP_063122301
VERSION     NP_001423338.1
DBSOURCE    REFSEQ: accession NM_001436409.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_063122301.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.32012.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..773
                     /product="transducin-like enhancer protein 3 isoform 8"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=83446
     Region          18..142
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          139..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          141..208
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          193..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          209..277
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          234..237
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <260..473
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          278..453
                     /region_name="SP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            284
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          485..523
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <486..771
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          490..529
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          531..570
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          537..575
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          575..614
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          580..616
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          617..656
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          623..658
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          658..697
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          663..696
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          699..738
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          704..738
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          740..772
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          745..769
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..773
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436409.1:1076..3397"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqlqaq hlshathgpp vqlpphpsgl qppgippvtg sssgllalga
      181 lgsqahlavk deknhheldh reresstnns vspseslras ekhrgsadys meakkrkaee
      241 kdslsrydsd gdksddlvvd vsnedpatpr vspahsppen gldkarglkk daptspasva
      301 sssstpsskt kdlghndkss tpglksntpt prndaptpgt sttpglrsmp gkppgmdpia
      361 salrtpislt ssyaapfamm shhemngslt spsayaglhn ipsqmsaaaa aaaaaygrsp
      421 mvgfdphppm ratglpssla sipggkpays fhvsadgqmq pvpfphdala gpgiprharq
      481 intlshgevv cavtisnptr hvytggkgcv kiwdisqpgs kspisqldcl nrdnyirsck
      541 llpdgrtliv ggeastltiw dlasptprik aeltssapac yalaispdak vcfsccsdgn
      601 iavwdlhnqt lvrqfqghtd gascidishd gtklwtggld ntvrswdlre grqlqqhdft
      661 sqifslgycp tgewlavgme ssnvevlhht kpdkyqlhlh escvlslkfa ycgkwfvstg
      721 kdnllnawrt pygasifqsk esssvlscdi saddkyivtg sgdkkatvye viy
//
LOCUS       NP_001423339             772 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 9 [Rattus norvegicus].
ACCESSION   NP_001423339 XP_006243278
VERSION     NP_001423339.1
DBSOURCE    REFSEQ: accession NM_001436410.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 772)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 772)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243278.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.28644.1,
                                           SRR26643285.31485.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..772
                     /product="transducin-like enhancer protein 3 isoform 9"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=83276
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..472
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          484..522
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <485..770
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          489..528
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          530..569
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          536..574
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          574..613
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          579..615
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          616..655
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          622..657
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          657..696
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          662..695
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          698..737
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          703..737
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          739..771
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          744..768
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..772
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436410.1:1076..3394"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi gimasalrtp
      361 isltssyaap fammshhemn gsltspsaya glhnipsqms aaaaaaaaay grspmvsfga
      421 vgfdphppmr atglpsslas ipggkpaysf hvsadgqmqp vpfphdalag pgiprharqi
      481 ntlshgevvc avtisnptrh vytggkgcvk iwdisqpgsk spisqldcln rdnyirsckl
      541 lpdgrtlivg geastltiwd lasptprika eltssapacy alaispdakv cfsccsdgni
      601 avwdlhnqtl vrqfqghtdg ascidishdg tklwtggldn tvrswdlreg rqlqqhdfts
      661 qifslgycpt gewlavgmes snvevlhhtk pdkyqlhlhe scvlslkfay cgkwfvstgk
      721 dnllnawrtp ygasifqske sssvlscdis addkyivtgs gdkkatvyev iy
//
LOCUS       NP_001423337             774 aa            linear   ROD 11-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423337 XP_006243277
VERSION     NP_001423337.1
DBSOURCE    REFSEQ: accession NM_001436408.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243277.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.28643.1,
                                           SRR26643294.32980.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..774
                     /product="transducin-like enhancer protein 3 isoform 7"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=83574
     Region          18..143
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          140..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          142..209
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          194..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          210..278
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          235..238
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <261..474
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          279..454
                     /region_name="SP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            285
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          486..524
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <487..772
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          491..530
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          532..571
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          538..576
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          576..615
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          581..617
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          618..657
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          624..659
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          659..698
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          664..697
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          700..739
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          705..739
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          741..773
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          746..770
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..774
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436408.1:1076..3400"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigvrglpn lpltqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg
      181 algsqahlav kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae
      241 ekdslsryds dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv
      301 asssstpssk tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi
      361 asalrtpisl tssyaapfam mshhemngsl tspsayaglh nipsqmsaaa aaaaaaygrs
      421 pmvgfdphpp mratglpssl asipggkpay sfhvsadgqm qpvpfphdal agpgiprhar
      481 qintlshgev vcavtisnpt rhvytggkgc vkiwdisqpg skspisqldc lnrdnyirsc
      541 kllpdgrtli vggeastlti wdlasptpri kaeltssapa cyalaispda kvcfsccsdg
      601 niavwdlhnq tlvrqfqght dgascidish dgtklwtggl dntvrswdlr egrqlqqhdf
      661 tsqifslgyc ptgewlavgm essnvevlhh tkpdkyqlhl hescvlslkf aycgkwfvst
      721 gkdnllnawr tpygasifqs kesssvlscd isaddkyivt gsgdkkatvy eviy
//
LOCUS       NP_071514               1828 aa            linear   ROD 11-MAR-2025
DEFINITION  unconventional myosin-Va isoform 2 [Rattus norvegicus].
ACCESSION   NP_071514
VERSION     NP_071514.2
DBSOURCE    REFSEQ: accession NM_022178.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1828)
  AUTHORS   Canclini,L., Cal,K., Bardier,C., Ruiz,P., Mercer,J.A. and
            Calliari,A.
  TITLE     Calcium triggers the dissociation of myosin-Va from ribosomes in
            ribonucleoprotein complexes
  JOURNAL   FEBS Lett 594 (14), 2311-2321 (2020)
   PUBMED   32412091
  REMARK    GeneRIF: Calcium triggers the dissociation of myosin-Va from
            ribosomes in ribonucleoprotein complexes.
REFERENCE   2  (residues 1 to 1828)
  AUTHORS   Maschi,D., Gramlich,M.W. and Klyachko,V.A.
  TITLE     Myosin V functions as a vesicle tether at the plasma membrane to
            control neurotransmitter release in central synapses
  JOURNAL   Elife 7, e39440 (2018)
   PUBMED   30320552
  REMARK    GeneRIF: myosin V acts as a vesicle tether at the plasma membrane,
            rather than a motor transporting vesicles to the release sites, or
            directly regulating vesicle exocytosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1828)
  AUTHORS   Landrock,K.K., Sullivan,P., Martini-Stoica,H., Goldstein,D.S.,
            Graham,B.H., Yamamoto,S., Bellen,H.J., Gibbs,R.A., Chen,R.,
            D'Amelio,M. and Stoica,G.
  TITLE     Pleiotropic neuropathological and biochemical alterations
            associated with Myo5a mutation in a rat Model
  JOURNAL   Brain Res 1679, 155-170 (2018)
   PUBMED   29217155
  REMARK    GeneRIF: This study identified in vivo neuropathological and
            biochemical alterative changes involved in the pathogenesis of a
            spontaneous autosomal recessive movement disorder in a mutant Myo5a
            juvenile rat model.
REFERENCE   4  (residues 1 to 1828)
  AUTHORS   Guatteo,E., Rizzo,F.R., Federici,M., Cordella,A., Ledonne,A.,
            Latini,L., Nobili,A., Viscomi,M.T., Biamonte,F., Landrock,K.K.,
            Martini,A., Aversa,D., Schepisi,C., D'Amelio,M., Berretta,N. and
            Mercuri,N.B.
  TITLE     Functional alterations of the dopaminergic and glutamatergic
            systems in spontaneous alpha-synuclein overexpressing rats
  JOURNAL   Exp Neurol 287 (Pt 1), 21-33 (2017)
   PUBMED   27771352
REFERENCE   5  (residues 1 to 1828)
  AUTHORS   Ultanir,S.K., Yadav,S., Hertz,N.T., Oses-Prieto,J.A., Claxton,S.,
            Burlingame,A.L., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     MST3 kinase phosphorylates TAO1/2 to enable Myosin Va function in
            promoting spine synapse development
  JOURNAL   Neuron 84 (5), 968-982 (2014)
   PUBMED   25456499
REFERENCE   6  (residues 1 to 1828)
  AUTHORS   Opartkiattikul,N., Funahara,Y., Fucharoen,S. and Talalak,P.
  TITLE     Increase in spontaneous platelet aggregation in
            beta-thalassemia/hemoglobin E disease: a consequence of splenectomy
  JOURNAL   Southeast Asian J Trop Med Public Health 23 Suppl 2, 36-41 (1992)
   PUBMED   1298991
REFERENCE   7  (residues 1 to 1828)
  AUTHORS   Mercer,J.A., Seperack,P.K., Strobel,M.C., Copeland,N.G. and
            Jenkins,N.A.
  TITLE     Novel myosin heavy chain encoded by murine dilute coat colour locus
  JOURNAL   Nature 349 (6311), 709-713 (1991)
   PUBMED   1996138
  REMARK    Erratum:[Nature 1991 Aug 8;352(6335):547]
REFERENCE   8  (residues 1 to 1828)
  AUTHORS   Moore,K.J., Swing,D.A., Copeland,N.G. and Jenkins,N.A.
  TITLE     Interaction of the murine dilute suppressor gene (dsu) with
            fourteen coat color mutations
  JOURNAL   Genetics 125 (2), 421-430 (1990)
   PUBMED   2379821
  REMARK    Erratum:[Genetics 1990 Sep;126(1):285]
REFERENCE   9  (residues 1 to 1828)
  AUTHORS   Moore,K.J., Seperack,P.K., Strobel,M.C., Swing,D.A., Copeland,N.G.
            and Jenkins,N.A.
  TITLE     Dilute suppressor dsu acts semidominantly to suppress the coat
            color phenotype of a deletion mutation, dl20J, of the murine dilute
            locus
  JOURNAL   Proc Natl Acad Sci U S A 85 (21), 8131-8135 (1988)
   PUBMED   3141922
REFERENCE   10 (residues 1 to 1828)
  AUTHORS   Murad,S. and Kishimoto,Y.
  TITLE     Alpha hydroxylation of lignoceric acid to cerebronic acid during
            brain development. Diminished hydroxylase activity in
            myelin-deficient mouse mutants
  JOURNAL   J Biol Chem 250 (15), 5841-5846 (1975)
   PUBMED   1150661
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Nov 27, 2020 this sequence version replaced NP_071514.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB035736.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1828
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1828
                     /product="unconventional myosin-Va isoform 2"
                     /note="dilute-opisthotonus; myosin-Va; dilute myosin heavy
                     chain, non-muscle; myosin 5a; unconventional myosin-Va"
                     /calculated_mol_wt=211990
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4I1; propagated from
                     UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Region          7..1275
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          83..751
                     /region_name="MYSc_Myo5"
                     /note="class V myosin, motor domain; cd01380"
                     /db_xref="CDD:276831"
     Site            order(111..119,163..170,209..219,437..442)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276831"
     Site            111..119
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276831"
     Site            163..170
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276831"
     Site            209..219
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276831"
     Site            437..445
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276831"
     Site            order(466..477,480..489)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276831"
     Region          599..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Region          643..665
                     /region_name="Actin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Site            685..695
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276831"
     Site            order(706..716,736..751)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276831"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Region          1105..1147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Region          <1158..>1436
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Site            1425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Region          1454..1828
                     /region_name="Myo5a_CBD"
                     /note="Cargo binding domain of myosin 5a; cd15478"
                     /db_xref="CDD:271262"
     Site            order(1471..1473,1476..1479,1649..1650,1808,1813,1815,
                     1817..1819)
                     /site_type="other"
                     /note="RILPL2 interface [polypeptide binding]"
                     /db_xref="CDD:271262"
     Site            order(1499,1502..1503,1506..1507,1510..1511,1514,1545,
                     1563..1568,1570..1571,1574)
                     /site_type="other"
                     /note="melanophilin interface [polypeptide binding]"
                     /db_xref="CDD:271262"
     Site            1625
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYF3.1)"
     Site            1733
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9QYF3.1)"
     CDS             1..1828
                     /gene="Myo5a"
                     /gene_synonym="Dop; Myh12"
                     /coded_by="NM_022178.2:34..5520"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25017"
                     /db_xref="RGD:3143"
ORIGIN      
        1 maaselytkf arvwipdpee vwksaellkd ykpgdkvlll hleegkdley rldpktselp
       61 hlrnpdilvg endltalsyl hepavlhnlr vrfidskliy tycgivlvai npyeqlpiyg
      121 ediinaysgq nmgdmdphif avaeeaykqm ardernqsii vsgesgagkt vsakyamryf
      181 atvsgsasea nveekvlasn pimesignak ttrndnssrf gkyieigfdk ryriiganmr
      241 tylleksrvv fqaeeernyh ifyqlcasak lpefkmlrlg nadsfhytkq ggspmiegvd
      301 dakemahtrq actllgises yqmgifrila gilhlgnvgf asrdsdscti ppkhepliif
      361 cdlmgvdyee mchwlchrkl atatetyikp isklqatnar dalakhiyak lfnwivghvn
      421 qalhsavkqh sfigvldiyg fetfeinsfe qfcinyanek lqqqfnmhvf kleqeeymke
      481 qipwtlidfy dnqpcinlie sklgildlld eeckmpkgtd dtwaqklynt hlnkcalfek
      541 prmsnkafii khfadkveyq cegfleknkd tvfeeqikvl ksskfkmlpe lfqddekais
      601 ptsatssgrt pltrvpvkpt kgrpgqtake hkktvglqfr nslhllmetl nattphyvrc
      661 ikpndfkfpf tfdekravqq lracgvleti risaagfpsr wtyqeffsry rvlmkqkdvl
      721 gdrkqtcqnv leklildkdk yqfgktkiff ragqvaylek lradklraac iriqktirgw
      781 llrkrylcmq raaitvqryv rgyqarcyak flrrtkaatt iqkywrmyvv rrkykirraa
      841 tivlqsylrg ylarnryrki lrehkaviiq krvrgwlart hykrtmkaii ylqccfrrmm
      901 akrelkklki earsverykk lhigmenkim qlqrkvdeqn kdykclmekl tnlegvynse
      961 teklrndver lqlseeeakv atgrvlslqe eiaklrkdle qtrsekksie eradkykqet
     1021 eqlvsnlkee ntllkqeket lnhlmveqak emtetmerkl veetkqleld lnderlryqn
     1081 llnefsrlee ryddlkeemt lmlnvpkpgh krtdsthssn eseytfssef aetediaprt
     1141 eeptekkvpl dmslflklqk rvteleqekq lmqdeldrke eqvlrskake eerpqirgae
     1201 leyeslkrqe lesenkklkn elnelrkals eksapevtap gapayrvlme qltavseeld
     1261 vrkeevlilr sqlvsqkeai qpkddkntmt dstilledvq kmkdkgeiaq ayiglketnr
     1321 llesqlqsqk rsheneaeal rgeiqslkee nnrqqqllaq nlqlppeari easlqheitr
     1381 ltnenldlme qlekqdktvr klkkqlkvfa kkigelevgq menispgqii depirpvnip
     1441 rkekdfqgml eykredeqkl vknlilelkp rgvavnlipg lpayilfmcv rhadylnddq
     1501 kvrslltsti nsikkvlkkr gddfetvsfw lsntcrflhc lkqysgeegf mkhntsrqne
     1561 hcltnfdlae yrqvlsdlai qiyqqlvrvl enilqpmivs gmlehetiqg vsgvkptglr
     1621 krtssiadeg tytldsilrq lnsfhsvmcq hgmdpelikq vvkqmfyivg aitlnnlllr
     1681 kdmcswskgm qirynvsqle ewlrdknlmn sgaketlepl iqaaqllqvk kktdddaeai
     1741 csmcnaltta qivkvlnlyt pvnefeervs vsfirtiqvr lrdrkdspql lmdakhifpv
     1801 tfpfnpssla letiqipasl glgfiarv
//
LOCUS       NP_001102896             165 aa            linear   ROD 11-MAR-2025
DEFINITION  transmembrane protein 88B [Rattus norvegicus].
ACCESSION   NP_001102896 XP_001058568
VERSION     NP_001102896.1
DBSOURCE    REFSEQ: accession NM_001109426.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001058568.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132273,
                              SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..165
                     /product="transmembrane protein 88B"
                     /calculated_mol_wt=17922
     CDS             1..165
                     /gene="Tmem278"
                     /gene_synonym="Tmem88b"
                     /coded_by="NM_001109426.1:287..784"
                     /db_xref="GeneID:680723"
                     /db_xref="RGD:1588243"
ORIGIN      
        1 msdqeretee degvtsdtap mlprrrptdy hisvlatqgl rtlmlsaral agfllhlllp
       61 gtvfllvllp aaavvylgfl chsrvhpapg prcrallsdr gsaalivfgf lslppllvla
      121 saarsllvrr lhlvlptpar tpdprrlprg sedladeekh lcawv
//
LOCUS       NP_058928                604 aa            linear   ROD 11-MAR-2025
DEFINITION  prostaglandin G/H synthase 2 precursor [Rattus norvegicus].
ACCESSION   NP_058928
VERSION     NP_058928.3
DBSOURCE    REFSEQ: accession NM_017232.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Toi,M., Toshiya,T., Noguchi,K., Yamanaka,H., Kobayashi,K.,
            Okubo,M., Kishima,K. and Dai,Y.
  TITLE     COX2 expression plays a role in spinal cord injury-induced
            neuropathic pain
  JOURNAL   Neurosci Lett 823, 137663 (2024)
   PUBMED   38286397
  REMARK    GeneRIF: COX2 expression plays a role in spinal cord injury-induced
            neuropathic pain.
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Zhang,X.H., Cui,H., Zheng,S.M., Lu,Y., Yuan,H.W., Zhang,L.,
            Wang,H.H. and Du,R.S.
  TITLE     Electroacupuncture regulates microglial polarization via inhibiting
            NF-kappaB/COX2 pathway following traumatic brain injury
  JOURNAL   Brain Res 1818, 148516 (2023)
   PUBMED   37562566
  REMARK    GeneRIF: Electroacupuncture regulates microglial polarization via
            inhibiting NF-kappaB/COX2 pathway following traumatic brain injury.
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Dourado,T.M.H., Assis,V.O., Awata,W.M.C., de Mello,M.M.B.,
            Carnio,E.C., Castro,M.M. and Tirapelli,C.R.
  TITLE     Mineralocorticoid receptors contribute to ethanol-induced vascular
            hypercontractility through reactive oxygen species generation and
            up-regulation of cyclooxygenase 2
  JOURNAL   Eur J Pharmacol 949, 175723 (2023)
   PUBMED   37059378
  REMARK    GeneRIF: Mineralocorticoid receptors contribute to ethanol-induced
            vascular hypercontractility through reactive oxygen species
            generation and up-regulation of cyclooxygenase 2.
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Abo-El Fetoh,M.E., Abdel-Fattah,M.M., Mohamed,W.R., Ramadan,L.A.A.
            and Afify,H.
  TITLE     Cyclooxygenase-2 activates EGFR-ERK1/2 pathway via PGE2-mediated
            ADAM-17 signaling in testosterone-induced benign prostatic
            hyperplasia
  JOURNAL   Inflammopharmacology 31 (1), 499-516 (2023)
   PUBMED   36586043
  REMARK    GeneRIF: Cyclooxygenase-2 activates EGFR-ERK1/2 pathway via
            PGE2-mediated ADAM-17 signaling in testosterone-induced benign
            prostatic hyperplasia.
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Xu,S., Yang,J., Wan,H., Yu,L. and He,Y.
  TITLE     Combination of Radix Astragali and Safflower Promotes Angiogenesis
            in Rats with Ischemic Stroke via Silencing PTGS2
  JOURNAL   Int J Mol Sci 24 (3), 2126 (2023)
   PUBMED   36768450
  REMARK    GeneRIF: Combination of Radix Astragali and Safflower Promotes
            Angiogenesis in Rats with Ischemic Stroke via Silencing PTGS2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Kulmacz,R.J. and Wang,L.H.
  TITLE     Comparison of hydroperoxide initiator requirements for the
            cyclooxygenase activities of prostaglandin H synthase-1 and -2
  JOURNAL   J Biol Chem 270 (41), 24019-24023 (1995)
   PUBMED   7592599
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Hla,T. and Neilson,K.
  TITLE     Human cyclooxygenase-2 cDNA
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7384-7388 (1992)
   PUBMED   1380156
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Ryseck,R.P., Raynoschek,C., Macdonald-Bravo,H., Dorfman,K.,
            Mattei,M.G. and Bravo,R.
  TITLE     Identification of an immediate early gene, pghs-B, whose protein
            product has prostaglandin synthase/cyclooxygenase activity
  JOURNAL   Cell Growth Differ 3 (7), 443-450 (1992)
   PUBMED   1419907
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Sirois,J. and Richards,J.S.
  TITLE     Purification and characterization of a novel, distinct isoform of
            prostaglandin endoperoxide synthase induced by human chorionic
            gonadotropin in granulosa cells of rat preovulatory follicles
  JOURNAL   J Biol Chem 267 (9), 6382-6388 (1992)
   PUBMED   1556140
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Hobel,W., Dudeck,J., Bockmann,R.D. and Weber,G.
  TITLE     Improvements of the algorithm for defining QRS onset and offset in
            the Pipberger program
  JOURNAL   Adv Cardiol 21, 181-184 (1978)
   PUBMED   619537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Jun 10, 2007 this sequence version replaced NP_058928.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF233596.1, S67722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..604
                     /product="prostaglandin G/H synthase 2 precursor"
                     /EC_number="1.14.99.1"
                     /note="prostaglandin G/H synthase 2; PGH synthase 2;
                     prostaglandin H2 synthase 2; cyclooxygenase-2"
                     /calculated_mol_wt=67382
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1800
     mat_peptide     18..604
                     /product="Prostaglandin G/H synthase 2.
                     /id=PRO_0000023879"
                     /note="propagated from UniProtKB/Swiss-Prot (P35355.1)"
                     /calculated_mol_wt=67382
     Region          21..53
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     Region          75..562
                     /region_name="prostaglandin_endoperoxide_synthase"
                     /note="Animal prostaglandin endoperoxide synthase and
                     related bacterial proteins; cd09816"
                     /db_xref="CDD:188648"
     Site            order(103,191,331,334..335,339,341,367,371,373,504,508,
                     512..513,516..517,520)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:188648"
     Site            order(111,113..115,122..126,128,215,305..309,312..313,316,
                     319..320,323,353..360,523..524,527..531,533..535,537..538)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:188648"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     Site            order(134,185,189,193,196..198,281,368,371..374,377,394,
                     430,432..433,436)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:188648"
     Site            396
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     Site            516
                     /site_type="other"
                     /note="Aspirin-acetylated serine.
                     /evidence=ECO:0000250|UniProtKB:P35354; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     Site            565
                     /site_type="acetylation"
                     /note="O-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q05769; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     Site            580
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35355.1)"
     CDS             1..604
                     /gene="Ptgs2"
                     /gene_synonym="COX-2; Cox2; PGHS-2; Pghs2; PHS II"
                     /coded_by="NM_017232.4:145..1959"
                     /db_xref="GeneID:29527"
                     /db_xref="RGD:620349"
ORIGIN      
        1 mlfravllca alalshaanp ccsnpcqnrg ecmsigfdqy kcdctrtgfy gencttpefl
       61 triklllkpt pntvhyilth fkgvwnivnn ipflrnsimr yvltsrshli dspptynvhy
      121 gyksweafsn lsyytralpp vaddcptpmg vkgnkelpds kevlekvllr refipdpqgt
      181 nmmfaffaqh fthqffktdq krgpgftrgl ghgvdlnhvy getldrqhkl rlfqdgklky
      241 qviggevypp tvkdtqvdmi ypphvpehlr favgqevfgl vpglmmyati wlrehnrvcd
      301 ilkqehpewd derlfqtsrl iligetikiv iedyvqhlsg yhfklkfdpe llfnqqfqyq
      361 nriasefntl yhwhpllpdt fniedqeytf kqflynnsil lehglahfve sftrqiagrv
      421 aggrnvpiav qavakasidq sremkyqsln eyrkrfslkp ytsfeeltge kemaaelkal
      481 yhdidamely pallvekprp daifgetmve lgapfslkgl mgnpicspqy wkpstfggev
      541 gfriintasi qslicnnvkg cpfasfnvqd pqptktatin asashsrldd inptvlikrr
      601 stel
//
LOCUS       NP_001013894             468 aa            linear   ROD 11-MAR-2025
DEFINITION  Mgat4 family, member E-like precursor [Rattus norvegicus].
ACCESSION   NP_001013894 XP_222643
VERSION     NP_001013894.2
DBSOURCE    REFSEQ: accession NM_001013872.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079259.1.
            
            On Sep 15, 2012 this sequence version replaced NP_001013894.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079259.1, CV113050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..468
                     /product="Mgat4 family, member E-like precursor"
                     /note="alpha-1,3-mannosyl-glycoprotein
                     4-beta-N-acetylglucosaminyltransferase MGAT4E-like; Mgat4
                     family, member E-like"
                     /calculated_mol_wt=50448
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3131
     Region          55..319
                     /region_name="PGAP4-like"
                     /note="Post-GPI attachment to proteins factor 4 and
                     similar proteins; cl04660"
                     /db_xref="CDD:471077"
     Region          240..264
                     /region_name="putative TM2 helix"
                     /note="putative TM2 helix [structural motif]"
                     /db_xref="CDD:409189"
     CDS             1..468
                     /gene="Mgat4f"
                     /gene_synonym="Mgat4e-like; Mgat4el"
                     /coded_by="NM_001013872.1:182..1588"
                     /db_xref="GeneID:289035"
                     /db_xref="RGD:1359351"
ORIGIN      
        1 mrgclwrcir vlasliilgf llreniavrv epqfntflse kkkmiqqiaq eeitseiknh
       61 skyfiemqks ssshvlqhat ytvlagsslq pkrlltvgiv smqrsprtyl ldtmtslfqa
      121 sseqdleyml ilvllsdtdp kwlnqtvani sglfmphies grllvvhgll ggsraesrnh
      181 tspcgklysr qkmssvllmn larnlseyfl mlgdkvhsap rflsdifwal sawnqlpwvi
      241 ldfssmtisg kvfhtedlsc lisflllfpk dipthlllse frlllsqnvp irlspsifyr
      301 mdsnsefedt cfpaeqnddl grpdnpaatv ftdmisfwht spqyayilnd dyfwaldpik
      361 gnyllvvldk pqkviqiave tgnnvnklnl lkhgqlllgy spmdypkrca qytlvgplvr
      421 gqldqmvfye edsvkeisci kllvteshdy pikimqikvw tevkeeen
//
LOCUS       NP_001416578             919 aa            linear   ROD 11-MAR-2025
DEFINITION  sarcosine dehydrogenase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001416578 XP_006233795
VERSION     NP_001416578.1
DBSOURCE    REFSEQ: accession NM_001429649.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Tibbetts,A.S. and Appling,D.R.
  TITLE     Compartmentalization of Mammalian folate-mediated one-carbon
            metabolism
  JOURNAL   Annu Rev Nutr 30, 57-81 (2010)
   PUBMED   20645850
  REMARK    Review article
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Bergeron,F., Otto,A., Blache,P., Day,R., Denoroy,L., Brandsch,R.
            and Bataille,D.
  TITLE     Molecular cloning and tissue distribution of rat sarcosine
            dehydrogenase
  JOURNAL   Eur J Biochem 257 (3), 556-561 (1998)
   PUBMED   9839943
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Porter,D.H., Cook,R.J. and Wagner,C.
  TITLE     Enzymatic properties of dimethylglycine dehydrogenase and sarcosine
            dehydrogenase from rat liver
  JOURNAL   Arch Biochem Biophys 243 (2), 396-407 (1985)
   PUBMED   2417560
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Cook,R.J., Misono,K.S. and Wagner,C.
  TITLE     The amino acid sequences of the flavin-peptides of dimethylglycine
            dehydrogenase and sarcosine dehydrogenase from rat liver
            mitochondria
  JOURNAL   J Biol Chem 260 (24), 12998-13002 (1985)
   PUBMED   4055729
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Wittwer,A.J. and Wagner,C.
  TITLE     Identification of the folate-binding proteins of rat liver
            mitochondria as dimethylglycine dehydrogenase and sarcosine
            dehydrogenase. Flavoprotein nature and enzymatic properties of the
            purified proteins
  JOURNAL   J Biol Chem 256 (8), 4109-4115 (1981)
   PUBMED   6163778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 24, 2024 this sequence version replaced XP_006233795.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.7398.1,
                                           SRR26643286.9636.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..919
                     /product="sarcosine dehydrogenase, mitochondrial"
                     /EC_number="1.5.8.3"
                     /calculated_mol_wt=99060
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=2373
     mat_peptide     23..919
                     /product="Sarcosine dehydrogenase, mitochondrial.
                     /id=PRO_0000010772"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=99060
     Region          67..445
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Region          431..486
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          481..917
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL12; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            803
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            885
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            905
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     CDS             1..919
                     /gene="Sardh"
                     /coded_by="NM_001429649.1:138..2897"
                     /db_xref="GeneID:114123"
                     /db_xref="RGD:621125"
ORIGIN      
        1 maslsrvlrv aatcprgrsa rnlglqplar earptteksv pyqctlkeea qgasvvpqgp
       61 sqplpstanv vvigggslgc qtlyhlaklg vggvvllere rltsgttwht agllwqlrps
      121 dvevellaht rqvvshdlee etglhtgwiq ngglfiasnq qrldeykrlm slgkaygies
      181 hvlspaetkd lyplmnvddl ygtlyvprdg tmdpagtctt ltraavarga qviencavtg
      241 irvrtddfgv rrvtavetqh gsiqtpcvvn cagvwassvg rmagvkvplv amhhayvvte
      301 riegiqnmpn vrdhdasvyl rlqgdalsvg gyeanpifwd evsdkfafgl fdldwdvftq
      361 hiegainrvp vlektgikst vcgpesftpd hkplmgeape lrgfflgcgf nsagmmlggg
      421 cgqelahwiv hgrpekdmys ydirrfhhsl tdhprwirer shesyaknys vvfphdepla
      481 grnmrrdplh eellgqgcvf qerqgwerpg wfnpqetaqv ldydyygayg hqahkdyays
      541 rllgdeytfd fpphhcviqk eclacrtaaa vfnmsyfgkf yllgadarka adwlfsadvn
      601 rppgstvytc mlnqrggtes dltvsclapg aqasplapaf egdgyylavg gavaqhnwsh
      661 intvlqdqef rcqlmdcsed lgmlsiqgpa srdilqdvld adlsneafpf sthqlvraag
      721 hlvrairlsf vgelgwelhv pqasclpvyr avmaagakhg lvnagyraid slsiekgyrh
      781 whadlrsdds pleaglaftc klktsvpflg realekqrat glrrrlvclt veeevpmfgl
      841 eaiwrngqvv ghvrradfgf tvnktiaygy irdpsggpvs ldfvkngdya lermgvtyaa
      901 qvhlkspfdp dnkrvkgiy
//
LOCUS       NP_001295194            1109 aa            linear   ROD 11-MAR-2025
DEFINITION  zinc finger E-box-binding homeobox 1 [Rattus norvegicus].
ACCESSION   NP_001295194
VERSION     NP_001295194.1
DBSOURCE    REFSEQ: accession NM_001308265.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Sun,S., Yan,T., Yang,N., Wu,J. and Liu,Z.
  TITLE     Regulation of osteoclast differentiation and inflammatory signaling
            by TCF8 in periodontitis
  JOURNAL   Oral Dis 30 (4), 2580-2591 (2024)
   PUBMED   37246926
  REMARK    GeneRIF: Regulation of osteoclast differentiation and inflammatory
            signaling by TCF8 in periodontitis.
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Souza,C.S., Deluque,A.L., Oliveira,B.M., Maciel,A.L.D.,
            Giovanini,C., Boer,P.A., de Paula,F.J.A., Costa,R.S.,
            Franscecato,H.D.C., de Almeida,L.F. and Coimbra,T.M.
  TITLE     Vitamin D deficiency contributes to the diabetic kidney disease
            progression via increase ZEB1/ZEB2 expressions
  JOURNAL   Nutr Diabetes 13 (1), 9 (2023)
   PUBMED   37391399
  REMARK    GeneRIF: Vitamin D deficiency contributes to the diabetic kidney
            disease progression via increase ZEB1/ZEB2 expressions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Zhu,X., Yan,F., Liu,L. and Huang,Q.
  TITLE     ZEB1 regulates bone metabolism in osteoporotic rats through
            inducing POLDIP2 transcription
  JOURNAL   J Orthop Surg Res 17 (1), 423 (2022)
   PUBMED   36123704
  REMARK    GeneRIF: ZEB1 regulates bone metabolism in osteoporotic rats
            through inducing POLDIP2 transcription.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1109)
  AUTHORS   Chen,Y.Y., Jiang,K.S., Bai,X.H., Liu,M., Lin,S.Y., Xu,T., Wei,J.Y.,
            Li,D., Xiong,Y.C., Xin,W.J. and Li,Z.Y.
  TITLE     ZEB1 Induces Ddr1 Promoter Hypermethylation and Contributes to the
            Chronic Pain in Spinal Cord in Rats Following Oxaliplatin Treatment
  JOURNAL   Neurochem Res 46 (8), 2181-2191 (2021)
   PUBMED   34032956
  REMARK    GeneRIF: ZEB1 Induces Ddr1 Promoter Hypermethylation and
            Contributes to the Chronic Pain in Spinal Cord in Rats Following
            Oxaliplatin Treatment.
REFERENCE   5  (residues 1 to 1109)
  AUTHORS   Sun,D., Liu,X., Zhu,L. and Zhang,B.
  TITLE     Zinc-finger E-box-binding homeobox 1 alleviates acute kidney injury
            by activating autophagy and the AMPK/mTOR pathway
  JOURNAL   Mol Med Rep 23 (6) (2021)
   PUBMED   33846788
  REMARK    GeneRIF: Zincfinger Eboxbinding homeobox 1 alleviates acute kidney
            injury by activating autophagy and the AMPK/mTOR pathway.
REFERENCE   6  (residues 1 to 1109)
  AUTHORS   Gong,S.G. and Eulenberg,R.L.
  TITLE     Palatal development in Twirler mice
  JOURNAL   Cleft Palate Craniofac J 38 (6), 622-628 (2001)
   PUBMED   11681996
REFERENCE   7  (residues 1 to 1109)
  AUTHORS   Cabanillas,A.M., Smith,G.E. and Darling,D.S.
  TITLE     T3-activation of the rat growth hormone gene is inhibited by a zinc
            finger/homeodomain protein
  JOURNAL   Mol Cell Endocrinol 181 (1-2), 131-137 (2001)
   PUBMED   11476947
REFERENCE   8  (residues 1 to 1109)
  AUTHORS   Takagi,T., Moribe,H., Kondoh,H. and Higashi,Y.
  TITLE     DeltaEF1, a zinc finger and homeodomain transcription factor, is
            required for skeleton patterning in multiple lineages
  JOURNAL   Development 125 (1), 21-31 (1998)
   PUBMED   9389660
REFERENCE   9  (residues 1 to 1109)
  AUTHORS   Higashi,Y., Moribe,H., Takagi,T., Sekido,R., Kawakami,K.,
            Kikutani,H. and Kondoh,H.
  TITLE     Impairment of T cell development in deltaEF1 mutant mice
  JOURNAL   J Exp Med 185 (8), 1467-1479 (1997)
   PUBMED   9126927
REFERENCE   10 (residues 1 to 1109)
  AUTHORS   Cabanillas,A.M. and Darling,D.S.
  TITLE     Alternative splicing gives rise to two isoforms of Zfhep, a zinc
            finger/homeodomain protein that binds T3-response elements
  JOURNAL   DNA Cell Biol 15 (8), 643-651 (1996)
   PUBMED   8769566
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U51583.1, SRR26643296.36810.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..1109
                     /product="zinc finger E-box-binding homeobox 1"
                     /note="zfhep; zinc finger homeodomain enhancer-binding
                     protein; TCF-8; transcription factor 8 (represses
                     interleukin 2 expression)"
                     /calculated_mol_wt=121496
     Region          1..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Region          9..>150
                     /region_name="GET2"
                     /note="GET complex subunit GET2; pfam08690"
                     /db_xref="CDD:400847"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Region          123..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Region          152..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          180..202
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          220..242
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          222..242
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          234..257
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          278..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64318; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37275; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Region          468..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Region          525..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Region          560..607
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          614..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37275; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64318; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64318; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P37275; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64318; propagated from
                     UniProtKB/Swiss-Prot (Q62947.2)"
     Region          834..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     Region          883..903
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(888,890,892,894..895,898..899,902,916,918,922..923,
                     926..927,930,944,946,948,950..951,954..955)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          895..920
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          911..931
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          923..948
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          939..956
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          968..1109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62947.2)"
     CDS             1..1109
                     /gene="Zeb1"
                     /gene_synonym="deltaEF1; Tcf8; Zfhx1a"
                     /coded_by="NM_001308265.3:24..3353"
                     /db_xref="GeneID:25705"
                     /db_xref="RGD:3831"
ORIGIN      
        1 madgprckrr kqanprrnnv tnyntvvean sdsddedklh iveeesvtda adceggvpdd
       61 elptdqtvlp ggsdragsak ncwqddvkdd ecdsdaeneq nhdpnveefl qqqdtaviyp
      121 eapeedqrqg tpeasghddn gtpdafsqll tcpycdrgyk rftslkehik yrheknednf
      181 scslcsytfa yrtqlerhmt shksgreqrh vtqsggnrkf kctecgkafk ykhhlkehlr
      241 ihsgekpyec pnckkrfshs gsysshissk kcislmpvng rprsglktsq csspslstsp
      301 gsptrpqirq kienkplqep lsvnqiktep vdyefkpivv asgincstpl qngvfsgggq
      361 lqatsspqgv vqavvlptvg lvspisinls diqnvlkvav dgniirqvle nnqaslaske
      421 qeavsassiq qgghsvisai slplvdqdgt tkiiinysle qpgqlqvvpq nlkkenpapp
      481 kscksekspe dltvksekdk sfdgaadest cllcedcpgd lnalpelkhy dpehpaqppp
      541 papatekpes sassagngdl spsqpplknl lsllkayyal naqpsteelt kiadsvnlpl
      601 dvvkkwfekm qagqipgqsl eppspgpgsg nipakteeqp qpvdgnepqe dstrgqsplk
      661 mtsspvlpvg saingsrsct sspsplnlss arnpqgyscv segtqeepqv epldlslpkq
      721 qgellerstv ssvyqnsvys vqeeplnlsc akkepqkdsc vtdsepvvnv vppsanpini
      781 aiptvtaqlp tivaiadqns vpclralaan kqtilipqva ytysatvspa mqeppvkviq
      841 pngnqderqd tssegvsved qndsdctppk kktrkaengm yacdlcdkif qksssllrhk
      901 yehtgkrphe cgicrkafkh khhliehmrl hsgekpyqcd kcgkrfshsg sysqhmnhry
      961 syckrgaedr dameqedtgp ealpevlpte lvgaraspsq adsdereslt reededseke
     1021 eeeedkemee lqedkecenp qeeeeeeeee eeeeeeeeee eaeeaeheaa aaktggavee
     1081 eaaqqagsfq qkasgseskr lseektnea
//
LOCUS       NP_001002827            1961 aa            linear   ROD 11-MAR-2025
DEFINITION  neurogenic locus notch homolog protein 4 precursor [Rattus
            norvegicus].
ACCESSION   NP_001002827 XP_579090
VERSION     NP_001002827.1
DBSOURCE    REFSEQ: accession NM_001002827.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1961)
  AUTHORS   Guo,M., Zhang,M., Cao,X., Fang,X., Li,K., Qin,L., He,Y., Zhao,J.,
            Xu,Y., Liu,X. and Li,X.
  TITLE     Notch4 mediates vascular remodeling via ERK/JNK/P38 MAPK signaling
            pathways in hypoxic pulmonary hypertension
  JOURNAL   Respir Res 23 (1), 6 (2022)
   PUBMED   35016680
  REMARK    GeneRIF: Notch4 mediates vascular remodeling via ERK/JNK/P38 MAPK
            signaling pathways in hypoxic pulmonary hypertension.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1961)
  AUTHORS   Xia,Z., Wang,J., Yang,S., Liu,C., Qin,S., Li,W., Cheng,Y., Hu,H.,
            Qian,J., Liu,Y. and Deng,C.
  TITLE     Emodin alleviates hypertrophic scar formation by suppressing
            macrophage polarization and inhibiting the Notch and TGF-beta
            pathways in macrophages
  JOURNAL   Braz J Med Biol Res 54 (8), e11184 (2021)
   PUBMED   34320121
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1961)
  AUTHORS   Yang,G.S., Zhou,X.Y., An,X.F., Liu,X.J., Zhang,Y.J. and Yu,D.
  TITLE     Mild hypothermia inhibits the Notch 3 and Notch 4 activation and
            seizure after stroke in the rat model
  JOURNAL   Pathol Res Pract 214 (7), 1008-1016 (2018)
   PUBMED   29754932
  REMARK    GeneRIF: mild hypothermia inhibits Notch 3 and Notch 4 activation
            and seizure after stroke in the rat model
REFERENCE   4  (residues 1 to 1961)
  AUTHORS   Pierscianek,D., Wolf,S., Keyvani,K., El Hindy,N., Stein,K.P.,
            Sandalcioglu,I.E., Sure,U., Mueller,O. and Zhu,Y.
  TITLE     Study of angiogenic signaling pathways in hemangioblastoma
  JOURNAL   Neuropathology 37 (1), 3-11 (2017)
   PUBMED   27388534
REFERENCE   5  (residues 1 to 1961)
  AUTHORS   Pierscianek,D., Michel,A., Hindy,N.E., Keyvani,K., Dammann,P.,
            Oezkan,N., Mueller,O., Sure,U. and Zhu,Y.
  TITLE     Activation of multiple angiogenic signaling pathways in
            hemangiopericytoma
  JOURNAL   Brain Tumor Pathol 33 (3), 200-208 (2016)
   PUBMED   26951238
REFERENCE   6  (residues 1 to 1961)
  AUTHORS   Uyttendaele,H., Ho,J., Rossant,J. and Kitajewski,J.
  TITLE     Vascular patterning defects associated with expression of activated
            Notch4 in embryonic endothelium
  JOURNAL   Proc Natl Acad Sci U S A 98 (10), 5643-5648 (2001)
   PUBMED   11344305
REFERENCE   7  (residues 1 to 1961)
  AUTHORS   Suzuki,T., Aoki,D., Susumu,N., Udagawa,Y. and Nozawa,S.
  TITLE     Imbalanced expression of TAN-1 and human Notch4 in endometrial
            cancers
  JOURNAL   Int J Oncol 17 (6), 1131-1139 (2000)
   PUBMED   11078798
REFERENCE   8  (residues 1 to 1961)
  AUTHORS   Uyttendaele,H., Closson,V., Wu,G., Roux,F., Weinmaster,G. and
            Kitajewski,J.
  TITLE     Notch4 and Jagged-1 induce microvessel differentiation of rat brain
            endothelial cells
  JOURNAL   Microvasc Res 60 (2), 91-103 (2000)
   PUBMED   10964583
REFERENCE   9  (residues 1 to 1961)
  AUTHORS   Uyttendaele,H., Soriano,J.V., Montesano,R. and Kitajewski,J.
  TITLE     Notch4 and Wnt-1 proteins function to regulate branching
            morphogenesis of mammary epithelial cells in an opposing fashion
  JOURNAL   Dev Biol 196 (2), 204-217 (1998)
   PUBMED   9576833
REFERENCE   10 (residues 1 to 1961)
  AUTHORS   Sarkar,N.H., Haga,S., Lehner,A.F., Zhao,W., Imai,S. and Moriwaki,K.
  TITLE     Insertional mutation of int protooncogenes in the mammary tumors of
            a new strain of mice derived from the wild in China: normal- and
            tumor-tissue-specific expression of int-3 transcripts
  JOURNAL   Virology 203 (1), 52-62 (1994)
   PUBMED   8030284
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BX883044.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579090.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132262, SAMD00132264
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1961
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..1961
                     /product="neurogenic locus notch homolog protein 4
                     precursor"
                     /note="neurogenic locus notch homolog protein 4; notch 4"
                     /calculated_mol_wt=203701
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2395
     Region          191..222
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(191,194,210)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          311..349
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(311,314,331)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          352..387
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(352,355,369)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          429..470
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(429,432,451)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          472..508
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(472,475,489)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          511..546
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          548..584
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(548,551,565)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          588..622
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          <696..723
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          765..800
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          <810..839
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          892..924
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          927..961
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          966..1000
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1002..1040
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1002,1005,1021)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1207..1242
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1245..1281
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1291..1340
                     /region_name="NOD"
                     /note="NOTCH protein; pfam06816"
                     /db_xref="CDD:462014"
     Region          1436..1511
                     /region_name="JMTM_Notch4"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in neurogenic locus notch homolog protein 4 (Notch4) and
                     similar proteins; cd21705"
                     /db_xref="CDD:411988"
     Region          <1611..1828
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1626..1656
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1627,1631..1632,1635..1637,1639..1640,1644,1647,
                     1656,1658,1660,1664..1665,1668..1670,1672..1673,1677,1681,
                     1690,1692,1694,1698..1699,1702..1704,1706..1707,1711,1714,
                     1723)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1658..1690
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1692..1723
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1725..1756
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1758..1789
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1791..1827
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..1961
                     /gene="Notch4"
                     /coded_by="NM_001002827.1:164..6049"
                     /db_xref="GeneID:406162"
                     /db_xref="RGD:1303282"
ORIGIN      
        1 mqrqwlllll lplsfpvilt rellcggspe pcanggtclr lsqgqgtcqc apgflgetcq
       61 fpdpcwdtql cenggscqal lptapsshsp tspltphfsc tcpsgftgdr cqspleelcp
      121 psfcsngghc svqvsgrpqc scepgwtgeq cqlrdfcsan pcanggvcla typqiqcrcp
      181 tgfeghicer dvnecflepg pcprgtschn tlgsfqclcp vgqegpqckl rkgaclpgtc
      241 lnggtcqlvp egdttfhlcl cppgftglnc emnpddcvrn qcqngatcqd glgtytclcp
      301 ktwkgwdcse dideceaqgp prcrnggtcq nsaggfhcvc vsgwggegcd enlddcaaat
      361 calgstcidr vgsfsclcpp grtgllchle dmclrqpchv naqcstnplt gstlcicqpg
      421 ysgptchqdl decqmaqqgp spcehggsci ntpgsfnclc lpgytgsrce adhneclsqp
      481 chpgstcldl latfqclcpp glegrlceve inecasnpcl nqaachdqln gflclclpgf
      541 tgarcekdmd ecssapcang ghcqdqpgaf hceclpgfeg prceteadec rsdpcpvgas
      601 cldlpgaflc lcrpgftgql cevplcspil cqpgqqcqdq ehrapclcpd gspgcvpaed
      661 dcpchhghcq rslcvcnegw tgpecetelg gclstpcahg gtchpqpsgy ncsclagytg
      721 ltcseeitac hsgpclnggs csihpegysc tcppshtgph cqtavdhcas asclnggtcm
      781 skpgtffchc atgfqglhce kkihpscadn pcrnkatcqd tprgarclcs pgytgsscqt
      841 lidlcarkpc phtarclqsg psfhclchqg wtgslcdlpl scqaaamsqg veisnlcqng
      901 glcidtgssy fcrcppgfeg klcqdtvnpc tskpclhgat cvpqpngyvc qcapgyegqn
      961 cskvhdacqs gpchnhgtct prpggfhcac ppgfvglrce gdvdecldrp chpsgtasch
     1021 slanafycqc lpghtgqrce vemdlcqsqp csnggscevt tgpppgftcr cpegfegptc
     1081 srkapacgnh hchngglclp spkpgspplc aclsgfggpd cltppappgc gppspcmhng
     1141 sctetpglgn pgfqctcppd spgprcqrpg angcegrggd gacdagcsgp ggdwdggdcs
     1201 lgvpdpwkgc pphsqcwllf rdgrchpqcd seeclfdgyd ceipptctpa ydqycrdhfh
     1261 nghcekgcnn aqcgwdggdc rpegddsegg pslallvvls ppaldqqlla larvlsltlr
     1321 vglwvrkdse grnmvfpypg trakeelsgt rdssswerqa phtqtpgket eslgagfvvv
     1381 mgvdlsrcgp ehpasrcprd sglllrflaa maavgalepl lpgpllaahp qagtgspatr
     1441 lpwpilcspv vgvlllalga llvlqlirrr rrehgalwlp pgfirrpqtq qaphrrrppl
     1501 gedniglkal kpeaevdedg vvmcsgpeeg eaektasasr cqlwplrsgc eglpqavmlt
     1561 ppqeceselp dsdtcgpdgv tplmsavfcg gvqsttvqrl glgnpepwep lldrgacpqa
     1621 htvgtgetpl hlaarfsrpt aarrlleaga npnqpdragr tplhtavaad arevcqllla
     1681 srqtavdart ddgttplmla arlavedlve eliaaradvg ardkrgktal hwaaavnnar
     1741 aarcllqtga dkdaqdsreq tplflaareg avevaqllle igaarglrdq aglapadvar
     1801 qrshwdlltl legagpitqe arsharntpg ggaaprcrtl sagarprggg aclqartwsv
     1861 dlgarrgavy arcrsrsggs ggpsmrgrrl sadsrgrrga rvsqddwprd wvaleacgsa
     1921 csapipppsl tpspergspq vswglpvhqe vplnsggrnq n
//
LOCUS       NP_849197                137 aa            linear   ROD 11-MAR-2025
DEFINITION  insulin-like growth factor 1 isoform b preproprotein [Rattus
            norvegicus].
ACCESSION   NP_849197
VERSION     NP_849197.3
DBSOURCE    REFSEQ: accession NM_178866.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Xiong,J., Wang,Y., Wang,H., Luo,J., Chen,T., Sun,J., Xi,Q. and
            Zhang,Y.
  TITLE     GHRH-stimulated pituitary small extracellular vesicles inhibit
            hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p
  JOURNAL   J Nanobiotechnology 22 (1), 649 (2024)
   PUBMED   39438882
  REMARK    GeneRIF: GHRH-stimulated pituitary small extracellular vesicles
            inhibit hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Maleki,A.H., Azar,J.T., Razi,M. and Tofighi,A.
  TITLE     The Effect of Different Exercise Modalities on Sertoli-germ Cells
            Metabolic Interactions in High-fat Diet-induced Obesity Rat Models:
            Implication on Glucose and Lactate Transport, Igf1, and
            Igf1R-dependent Pathways
  JOURNAL   Reprod Sci 31 (8), 2246-2260 (2024)
   PUBMED   38632221
  REMARK    GeneRIF: The Effect of Different Exercise Modalities on
            Sertoli-germ Cells Metabolic Interactions in High-fat Diet-induced
            Obesity Rat Models: Implication on Glucose and Lactate Transport,
            Igf1, and Igf1R-dependent Pathways.
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Banjac,K., Obradovic,M., Zafirovic,S., Essack,M., Gluvic,Z.,
            Sunderic,M., Nedic,O. and Isenovic,E.R.
  TITLE     The involvement of Akt, mTOR, and S6K in the in vivo effect of
            IGF-1 on the regulation of rat cardiac Na+/K+-ATPase
  JOURNAL   Mol Biol Rep 51 (1), 517 (2024)
   PUBMED   38622478
  REMARK    GeneRIF: The involvement of Akt, mTOR, and S6K in the in vivo
            effect of IGF-1 on the regulation of rat cardiac Na[+]/K[+]-ATPase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Barik,P., Kuo,W.W., Kuo,C.H., Hsieh,D.J., Day,C.H., Daddam,J.,
            Chen,M.Y., Padma,V.V., Shibu,M.A. and Huang,C.Y.
  TITLE     Rewiring of IGF1 secretion and enhanced IGF1R signaling induced by
            co-chaperone carboxyl-terminus of Hsp70 interacting protein in
            adipose-derived stem cells provide augmented cardioprotection in
            aging-hypertensive rats
  JOURNAL   Aging (Albany NY) 15 (23), 14019-14038 (2023)
   PUBMED   38085649
  REMARK    GeneRIF: Rewiring of IGF1 secretion and enhanced IGF1R signaling
            induced by co-chaperone carboxyl-terminus of Hsp70 interacting
            protein in adipose-derived stem cells provide augmented
            cardioprotection in aging-hypertensive rats.
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Zhao,H., Wang,L., Yan,Y., Zhao,Q.H., He,J., Jiang,R., Luo,C.J.,
            Qiu,H.L., Miao,Y.Q., Gong,S.G., Yuan,P. and Wu,W.H.
  TITLE     Identification of the shared gene signatures between pulmonary
            fibrosis and pulmonary hypertension using bioinformatics analysis
  JOURNAL   Front Immunol 14, 1197752 (2023)
   PUBMED   37731513
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Nanto-Salonen,K. and Rosenfeld,R.G.
  TITLE     Insulin-like growth factor binding protein expression in the
            hypothyroid rat is age dependent
  JOURNAL   Endocrinology 131 (3), 1489-1496 (1992)
   PUBMED   1380443
REFERENCE   7  (residues 1 to 137)
  AUTHORS   Hall,L.J., Kajimoto,Y., Bichell,D., Kim,S.W., James,P.L.,
            Counts,D., Nixon,L.J., Tobin,G. and Rotwein,P.
  TITLE     Functional analysis of the rat insulin-like growth factor I gene
            and identification of an IGF-I gene promoter
  JOURNAL   DNA Cell Biol 11 (4), 301-313 (1992)
   PUBMED   1605853
REFERENCE   8  (residues 1 to 137)
  AUTHORS   Bouillon,R.
  TITLE     Diabetic bone disease. Low turnover osteoporosis related to
            decreased IGF-I production
  JOURNAL   Verh K Acad Geneeskd Belg 54 (4), 365-91 (1992)
   PUBMED   1466160
REFERENCE   9  (residues 1 to 137)
  AUTHORS   Nanto-Salonen,K., Glasscock,G.F. and Rosenfeld,R.G.
  TITLE     The effects of thyroid hormone on insulin-like growth factor (IGF)
            and IGF-binding protein (IGFBP) expression in the neonatal rat:
            prolonged high expression of IGFBP-2 in methimazole-induced
            congenital hypothyroidism
  JOURNAL   Endocrinology 129 (5), 2563-2570 (1991)
   PUBMED   1718729
REFERENCE   10 (residues 1 to 137)
  AUTHORS   Kato,H., Okoshi,A., Miura,Y. and Noguchi,T.
  TITLE     A new cDNA clone relating to larger molecular species of rat
            insulin-like growth factor-I mRNA
  JOURNAL   Agric Biol Chem 54 (6), 1599-1601 (1990)
   PUBMED   1368571
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC086374.1 and CB761687.1.
            
            On Dec 20, 2007 this sequence version replaced NP_849197.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and has
            multiple coding region differences which include the absence of an
            alternate frame-shifting exon, compared to variant 3. These
            differences cause translation initiation from a distinct start
            codon and result in an isoform (b) with novel N- and C-termini,
            compared to isoform c. This isoform is also known as IIA.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086374.1, CO383788.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..137
                     /product="insulin-like growth factor 1 isoform b
                     preproprotein"
                     /note="somatomedin; IGF-I; Insulin-like growth factor I"
                     /calculated_mol_wt=11760
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3453
     proprotein      33..137
                     /product="insulin-like growth factor 1 isoform b
                     proprotein"
                     /calculated_mol_wt=11760
     mat_peptide     33..102
                     /product="insulin-like growth factor 1 isoform b"
                     /calculated_mol_wt=7693
     Region          33..100
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(35,44,52..56)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(53,55..56,76)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            order(81..83,87..88)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     CDS             1..137
                     /gene="Igf1"
                     /gene_synonym="IGF"
                     /coded_by="NM_178866.4:32..445"
                     /note="isoform b preproprotein is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:24482"
                     /db_xref="RGD:2868"
ORIGIN      
        1 msappikihi mssshlfyla lclltftssa tagpetlcga elvdalqfvc gprgfyfnkp
       61 tgygssirra pqtgivdecc frscdlrrle mycaplkptk sarsiraqrh tdmpktqkev
      121 hlkntsrgsa gnktyrm
//
LOCUS       NP_001099191            2531 aa            linear   ROD 11-MAR-2025
DEFINITION  neurogenic locus notch homolog protein 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001099191 XP_001078434 XP_342393
VERSION     NP_001099191.1
DBSOURCE    REFSEQ: accession NM_001105721.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2531)
  AUTHORS   Wang,Y.C., Chen,R.F., Liu,K.F., Chen,W.Y., Lee,C.C. and Kuo,Y.R.
  TITLE     Adipose-derived stem cell modulate tolerogenic dendritic
            cell-induced T cell regulation is correlated with activation of
            Notch-NFkappaB signaling
  JOURNAL   Cytotherapy 26 (8), 890-898 (2024)
   PUBMED   38625070
  REMARK    GeneRIF: Adipose-derived stem cell modulate tolerogenic dendritic
            cell-induced T cell regulation is correlated with activation of
            Notch-NFkappaB signaling.
REFERENCE   2  (residues 1 to 2531)
  AUTHORS   Zhang,H., Gu,R., Luo,J., Zhong,C. and Pan,J.
  TITLE     Involvement of NOTCH1-mediated Microglia Activation in
            Neuromodulation of Chronic Prostatitis-related Pain
  JOURNAL   In Vivo 38 (2), 691-698 (2024)
   PUBMED   38418142
  REMARK    GeneRIF: Involvement of NOTCH1-mediated Microglia Activation in
            Neuromodulation of Chronic Prostatitis-related Pain.
REFERENCE   3  (residues 1 to 2531)
  AUTHORS   Li,Y., Ma,L., Deng,Y., Du,Z., Guo,B., Yue,J., Liu,X. and Zhang,Y.
  TITLE     The Notch1/Hes1 signaling pathway affects autophagy by adjusting
            DNA methyltransferases expression in a valproic acid-induced autism
            spectrum disorder model
  JOURNAL   Neuropharmacology 239, 109682 (2023)
   PUBMED   37543138
  REMARK    GeneRIF: The Notch1/Hes1 signaling pathway affects autophagy by
            adjusting DNA methyltransferases expression in a valproic
            acid-induced autism spectrum disorder model.
REFERENCE   4  (residues 1 to 2531)
  AUTHORS   Wang,P., Zhang,S., Hu,C., Ren,L. and Bi,J.
  TITLE     Regulatory role of melatonin in Notch1 signaling pathway in
            cerebral cortex of Abeta1-42-induced Alzheimer's disease rat model
  JOURNAL   Mol Biol Rep 50 (3), 2463-2469 (2023)
   PUBMED   36602704
  REMARK    GeneRIF: Regulatory role of melatonin in Notch1 signaling pathway
            in cerebral cortex of Abeta1-42-induced Alzheimer's disease rat
            model.
REFERENCE   5  (residues 1 to 2531)
  AUTHORS   Yang,C., Pan,J., Luo,X., Li,J. and Jiang,Z.
  TITLE     Hypoxia-induced mesenchymal stem cells inhibit corneal fibroblast
            proliferation by regulating the WWP2/Notch1 axis
  JOURNAL   Regen Med 17 (6), 375-388 (2022)
   PUBMED   35545948
  REMARK    GeneRIF: Hypoxia-induced mesenchymal stem cells inhibit corneal
            fibroblast proliferation by regulating the WWP2/Notch1 axis.
REFERENCE   6  (residues 1 to 2531)
  AUTHORS   de la Pompa,J.L., Wakeham,A., Correia,K.M., Samper,E., Brown,S.,
            Aguilera,R.J., Nakano,T., Honjo,T., Mak,T.W., Rossant,J. and
            Conlon,R.A.
  TITLE     Conservation of the Notch signalling pathway in mammalian
            neurogenesis
  JOURNAL   Development 124 (6), 1139-1148 (1997)
   PUBMED   9102301
REFERENCE   7  (residues 1 to 2531)
  AUTHORS   Conlon,R.A., Reaume,A.G. and Rossant,J.
  TITLE     Notch1 is required for the coordinate segmentation of somites
  JOURNAL   Development 121 (5), 1533-1545 (1995)
   PUBMED   7789282
REFERENCE   8  (residues 1 to 2531)
  AUTHORS   Lindsell,C.E., Shawber,C.J., Boulter,J. and Weinmaster,G.
  TITLE     Jagged: a mammalian ligand that activates Notch1
  JOURNAL   Cell 80 (6), 909-917 (1995)
   PUBMED   7697721
REFERENCE   9  (residues 1 to 2531)
  AUTHORS   Weinmaster,G., Roberts,V.J. and Lemke,G.
  TITLE     Notch2: a second mammalian Notch gene
  JOURNAL   Development 116 (4), 931-941 (1992)
   PUBMED   1295745
REFERENCE   10 (residues 1 to 2531)
  AUTHORS   Weinmaster,G., Roberts,V.J. and Lemke,G.
  TITLE     A homolog of Drosophila Notch expressed during mammalian
            development
  JOURNAL   Development 113 (1), 199-205 (1991)
   PUBMED   1764995
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474001.2.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_342393.3, XP_001078434.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132262, SAMD00132263
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2531
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..2531
                     /product="neurogenic locus notch homolog protein 1
                     precursor"
                     /note="neurogenic locus notch homolog protein 1; Notch
                     gene homolog 1; Drosophila Notch homolog 1 (controlling
                     the the ectodermal and neural cell fate in Drosophila);
                     notch 1"
                     /calculated_mol_wt=268922
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1920
     mat_peptide     19..2531
                     /product="Neurogenic locus notch homolog protein 1.
                     /id=PRO_0000007680"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
                     /calculated_mol_wt=268922
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            65
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            73
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            116
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          142..175
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            146
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          178..216
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(178,181,197)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            194
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            232
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01705; O-linked
                     (GalNAc...) threonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          257..293
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(257,260,274)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          295..332
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(295,298,314)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            311
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          335..370
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(335,338,352)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            341
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            349
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            378
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          412..450
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(412,415,431)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          420..421
                     /region_name="Interaction with DLL4.
                     /evidence=ECO:0000269|PubMed:25700513,
                     ECO:0007744|PDB:4XL1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Site            435
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000269|PubMed:25700513,
                     ECO:0007744|PDB:4XL1; propagated from UniProtKB/Swiss-Prot
                     (Q07008.3)"
     Region          448..452
                     /region_name="Interaction with DLL4.
                     /evidence=ECO:0000269|PubMed:25700513,
                     ECO:0007744|PDB:4XL1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          452..488
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(452,455,469)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            458
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000269|PubMed:25700513; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            466
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000269|PubMed:25700513,
                     ECO:0007744|PDB:4XL1; propagated from UniProtKB/Swiss-Prot
                     (Q07008.3)"
     Site            469
                     /site_type="other"
                     /note="Interaction with DLL4.
                     /evidence=ECO:0000269|PubMed:25700513,
                     ECO:0007744|PDB:4XL1; propagated from UniProtKB/Swiss-Prot
                     (Q07008.3)"
     Region          490..526
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(490,493,507)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            496
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000269|PubMed:25700513; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          528..564
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(528,531,545)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            534
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          566..601
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(566,569,582)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          603..639
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(603,606,620)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            609
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            617
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          641..675
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(641,644,657)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            647
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          678..713
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(678,681,695)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            692
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          717..750
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            722
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          755..789
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            759
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            767
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            784
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          791..827
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(791,794,808)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            797
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            805
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          869..905
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(869,872,886)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            888
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            900
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          907..943
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(907,910,924)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            921
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          945..981
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(945,948,962)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            951
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            959
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          988..1019
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            997
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1021..1057
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1021,1024,1038)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1027
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1035
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1065
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1146..1180
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1159
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1179
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1184..1219
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1189
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1197
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1221..1265
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1221,1224,1246)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1267..1305
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1267,1270,1286)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1273
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1362
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1379
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1402
                     /site_type="glycosylation"
                     /note="O-linked (Fuc...) threonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01705; O-linked
                     (GalNAc...) threonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1442..1479
                     /region_name="NL"
                     /note="Domain found in Notch and Lin-12; smart00004"
                     /db_xref="CDD:197463"
     Region          1449..1489
                     /region_name="LNR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1487..1522
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Site            1489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1490..1531
                     /region_name="LNR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1525..1561
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1532..1571
                     /region_name="LNR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1566..1621
                     /region_name="NOD"
                     /note="NOTCH protein; pfam06816"
                     /db_xref="CDD:462014"
     Site            1587
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1654..1655
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1663..1719
                     /region_name="NODP"
                     /note="NOTCH protein; pfam07684"
                     /db_xref="CDD:462229"
     Region          1710..1789
                     /region_name="JMTM_Notch1"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in neurogenic locus notch homolog protein 1 (Notch1) and
                     similar proteins; cd21702"
                     /db_xref="CDD:411985"
     Site            1710..1711
                     /site_type="cleavage"
                     /note="Cleavage, by ADAM17.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            order(1711..1713,1716..1718,1729..1730,1732,1734..1751)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411985"
     Site            1715
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P46531; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1718..1750
                     /region_name="Interaction with PSEN1.
                     /evidence=ECO:0000250|UniProtKB:P46531"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1726..1746
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1770..1798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01705; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Site            order(1870,1872,1876..1877,1880..1882,1897..1898,1902,
                     1905,1915,1917,1919,1923..1924,1927..1929,1931..1932,1936,
                     1939,1948,1950,1952,1956..1957,1960..1962,1964..1965,1969,
                     1972)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1870..1915
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <1894..2108
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1917..1948
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1917..1946
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1937..1945
                     /region_name="HIF1AN-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Site            1945
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1950..1981
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1950..1980
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          1984..2015
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1984..2013
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2004..2012
                     /region_name="HIF1AN-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Site            2012
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2017..2081
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          2017..2046
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2050..2079
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2141..2185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2146..>2526
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          2382..2428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     Region          2440..2531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07008.3)"
     CDS             1..2531
                     /gene="Notch1"
                     /gene_synonym="NOTCH; TAN1"
                     /coded_by="NM_001105721.1:227..7822"
                     /db_xref="GeneID:25496"
                     /db_xref="RGD:3187"
ORIGIN      
        1 mprllapllc ltllpalaar glrcsqpsgt clnggrceva ngteacvcsg afvgqrcqdp
       61 spclstpckn agtcyvvdhg givdyacscp lgfsgplclt planaclanp crnggtcdll
      121 tlteykcrcp pgwsgkscqq adpcasnpca nggqclpfes syicgcppgf hgptcrqdvn
      181 ecsqnpglcr hggtchneig syrcacrath tgphcelpyv pcspspcqng gtcrptgdtt
      241 hecaclpgfa gqnceenvdd cpgnnckngg acvdgvntyn crcppewtgq yctedvdecq
      301 lmpnacqngg tchnshggyn cvcvngwtge dcseniddca saacfqgatc hdrvasfyce
      361 cphgrtgllc hlndacisnp cnegsncdtn pvngkaictc psgytgpacs qdvdecalga
      421 npcehagkcl ntlgsfecqc lqgytgprce idvnecisnp cqndatcldq igefqcicmp
      481 gyegvycein tdecasspcl hngrcvdkin eflcqcpkgf sghlcqydvd ecastpckng
      541 akcldgpnty tcvctegytg thcevdidec dpdpchyglc kdgvatftcl cqpgytghhc
      601 etninechsq pcrhggtcqd rdnyylclcl kgttgpncei nlddcasnpc dsgtcldkid
      661 gyecacepgy tgsmcnvnid ecagspchng gtcedgiagf tcrcpegyhd ptclsevnec
      721 nsnpcihgac rdglngykcd capgwsgtnc dinnnecesn pcvnggtckd mtsgyvctcr
      781 egfsgpncqt ninecasnpc lnqgtciddv agykcncplp ytgatcevvl apcatspckn
      841 sgvckesedy esfscvcptg wqgqtceidi necvkspcrh gascqntngs yrclcqagyt
      901 grncesdidd crpnpchngg sctdgvnaaf cdclpgfqga fceedineca snpcqnganc
      961 tdcvdsytct cptgfngihc enntpdctes scfnggtcvd ginsftclcp pgftgsycqy
     1021 dvnecdsrpc lhggtcqdsy gtykctcpqg ytglncqnlv rwcdsapckn ggkcwqtntq
     1081 yhcecrsgwt gfncdvlsvs cevaaqkrgi dvtllcqhgg lcvdeedkhy chcqagytgs
     1141 ycedevdecs pnpcqngatc tdylggfsck cvagyhgsnc seeineclsq pcqnggtcid
     1201 ltntykcscp rgtqgvhcei nvddchppld pasrspkcfn ngtcvdqvgg ytctcppgfv
     1261 gercegdvne clsnpcdprg tqncvqrvnd fhcecraght grrcesving crgkpcrngg
     1321 vcavasntar gficrcpagf egatcendar tcgslrclng gtcisgprsp tclclgsftg
     1381 pecqfpassp cvgsnpcynq gtceptsesp fyrclcpakf ngllchildy sftggagrdi
     1441 pppqieeace lpecqedagn kvcnlqcnnh acgwdggdcs lnfndpwknc tqslqcwkyf
     1501 sdghcdsqcn sagclfdgfd cqltegqcnp lydqyckdhf sdghcdqgcn saecewdgld
     1561 caehvperla agtlvlvvll ppdqlrnnsf hflrelshvl htnvvfkrda qgqqmifpyy
     1621 greeelrkhp ikrsavgwat tsllpgtngg rqrreldpmd ihgsivylei dnrqcvqsss
     1681 qcfqsatdva aflgalaslg slnipykiea vksetveppl psqlhlmyva aaafvllffv
     1741 gcgvllsrkr rrqhgqlwfp egfkvseask kkrreplged svglkplkna sdgalmddnq
     1801 newgdedlet kkfrfeepvv lpdlddqtdh rqwtqqhlda adlrvsamap tppqgevdad
     1861 cmdvnvrgpd gftplmiasc sgggletgns eeeedapavi sdfiyqgasl hnqtdrtget
     1921 alhlaarysr sdaakrllea sadaniqdnm grtplhaavs adaqgvfqil lrnratdlda
     1981 rmhdgttpli laarlavegm ledlinshad vnavddlgks alhwaaavnn vdaavvllkn
     2041 gankdmqnnk eetplflaar egsyetakvl ldhfanrdit dhmdrlprdi aqermhhdiv
     2101 rlldeynlvr spqlhgtalg gtptlsptlc spngylgnlk satqgkkark pstkglacss
     2161 keakdlkarr kksqdgkgcl ldsssmlspv dslesphgyl sdvasppllp spfqqspsmp
     2221 lshlpgmpdt hlgishlnva akpemaalag gsrlafeppp prlshlpvas sastvlstng
     2281 tgamnftvga paslngqcew lprlqngmvp sqynplrpgv tpgtlstqaa glqhgmmgpi
     2341 hsslstntls piiyqglpnt rlatqphlvq tqqvqpqnlq iqpqnlqpps qphlsvssaa
     2401 nghlgrsfls gepsqadvqp lgpsslpvht ilpqesqalp tslpssmvpp mtttqfltpp
     2461 sqhsyssspv dntpshqlqv pehpfltpsp espdqwssss phsnisdwse gisspptsmp
     2521 sqithipeaf k
//
LOCUS       NP_001075946             143 aa            linear   ROD 11-MAR-2025
DEFINITION  insulin-like growth factor 1 isoform a preproprotein [Rattus
            norvegicus].
ACCESSION   NP_001075946
VERSION     NP_001075946.2
DBSOURCE    REFSEQ: accession NM_001082477.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Xiong,J., Wang,Y., Wang,H., Luo,J., Chen,T., Sun,J., Xi,Q. and
            Zhang,Y.
  TITLE     GHRH-stimulated pituitary small extracellular vesicles inhibit
            hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p
  JOURNAL   J Nanobiotechnology 22 (1), 649 (2024)
   PUBMED   39438882
  REMARK    GeneRIF: GHRH-stimulated pituitary small extracellular vesicles
            inhibit hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Maleki,A.H., Azar,J.T., Razi,M. and Tofighi,A.
  TITLE     The Effect of Different Exercise Modalities on Sertoli-germ Cells
            Metabolic Interactions in High-fat Diet-induced Obesity Rat Models:
            Implication on Glucose and Lactate Transport, Igf1, and
            Igf1R-dependent Pathways
  JOURNAL   Reprod Sci 31 (8), 2246-2260 (2024)
   PUBMED   38632221
  REMARK    GeneRIF: The Effect of Different Exercise Modalities on
            Sertoli-germ Cells Metabolic Interactions in High-fat Diet-induced
            Obesity Rat Models: Implication on Glucose and Lactate Transport,
            Igf1, and Igf1R-dependent Pathways.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Banjac,K., Obradovic,M., Zafirovic,S., Essack,M., Gluvic,Z.,
            Sunderic,M., Nedic,O. and Isenovic,E.R.
  TITLE     The involvement of Akt, mTOR, and S6K in the in vivo effect of
            IGF-1 on the regulation of rat cardiac Na+/K+-ATPase
  JOURNAL   Mol Biol Rep 51 (1), 517 (2024)
   PUBMED   38622478
  REMARK    GeneRIF: The involvement of Akt, mTOR, and S6K in the in vivo
            effect of IGF-1 on the regulation of rat cardiac Na[+]/K[+]-ATPase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Barik,P., Kuo,W.W., Kuo,C.H., Hsieh,D.J., Day,C.H., Daddam,J.,
            Chen,M.Y., Padma,V.V., Shibu,M.A. and Huang,C.Y.
  TITLE     Rewiring of IGF1 secretion and enhanced IGF1R signaling induced by
            co-chaperone carboxyl-terminus of Hsp70 interacting protein in
            adipose-derived stem cells provide augmented cardioprotection in
            aging-hypertensive rats
  JOURNAL   Aging (Albany NY) 15 (23), 14019-14038 (2023)
   PUBMED   38085649
  REMARK    GeneRIF: Rewiring of IGF1 secretion and enhanced IGF1R signaling
            induced by co-chaperone carboxyl-terminus of Hsp70 interacting
            protein in adipose-derived stem cells provide augmented
            cardioprotection in aging-hypertensive rats.
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Zhao,H., Wang,L., Yan,Y., Zhao,Q.H., He,J., Jiang,R., Luo,C.J.,
            Qiu,H.L., Miao,Y.Q., Gong,S.G., Yuan,P. and Wu,W.H.
  TITLE     Identification of the shared gene signatures between pulmonary
            fibrosis and pulmonary hypertension using bioinformatics analysis
  JOURNAL   Front Immunol 14, 1197752 (2023)
   PUBMED   37731513
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Nanto-Salonen,K. and Rosenfeld,R.G.
  TITLE     Insulin-like growth factor binding protein expression in the
            hypothyroid rat is age dependent
  JOURNAL   Endocrinology 131 (3), 1489-1496 (1992)
   PUBMED   1380443
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Hall,L.J., Kajimoto,Y., Bichell,D., Kim,S.W., James,P.L.,
            Counts,D., Nixon,L.J., Tobin,G. and Rotwein,P.
  TITLE     Functional analysis of the rat insulin-like growth factor I gene
            and identification of an IGF-I gene promoter
  JOURNAL   DNA Cell Biol 11 (4), 301-313 (1992)
   PUBMED   1605853
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Bouillon,R.
  TITLE     Diabetic bone disease. Low turnover osteoporosis related to
            decreased IGF-I production
  JOURNAL   Verh K Acad Geneeskd Belg 54 (4), 365-91 (1992)
   PUBMED   1466160
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Nanto-Salonen,K., Glasscock,G.F. and Rosenfeld,R.G.
  TITLE     The effects of thyroid hormone on insulin-like growth factor (IGF)
            and IGF-binding protein (IGFBP) expression in the neonatal rat:
            prolonged high expression of IGFBP-2 in methimazole-induced
            congenital hypothyroidism
  JOURNAL   Endocrinology 129 (5), 2563-2570 (1991)
   PUBMED   1718729
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Kato,H., Okoshi,A., Miura,Y. and Noguchi,T.
  TITLE     A new cDNA clone relating to larger molecular species of rat
            insulin-like growth factor-I mRNA
  JOURNAL   Agric Biol Chem 54 (6), 1599-1601 (1990)
   PUBMED   1368571
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M17593.1, BC086374.1, M15480.1 and CB761687.1.
            
            On Dec 20, 2007 this sequence version replaced NP_001075946.1.
            
            Transcript Variant: This variant (1) differs in the 5' UTR and 5'
            coding region, compared to variant 3. These differences cause
            translation initiation from a distinct start codon and result in an
            isoform (a) with a novel C-terminus, compared to isoform c. This
            isoform is also known as IIC.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ093477.1, M15480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..143
                     /product="insulin-like growth factor 1 isoform a
                     preproprotein"
                     /note="somatomedin; IGF-I; Insulin-like growth factor I"
                     /calculated_mol_wt=12640
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3453
     proprotein      33..143
                     /product="insulin-like growth factor 1 isoform a
                     proprotein"
                     /calculated_mol_wt=12640
     mat_peptide     33..102
                     /product="insulin-like growth factor 1 isoform a"
                     /calculated_mol_wt=7693
     Region          33..100
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Site            order(35,44,52..56)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(53,55..56,76)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Site            order(81..83,87..88)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     CDS             1..143
                     /gene="Igf1"
                     /gene_synonym="IGF"
                     /coded_by="NM_001082477.2:32..463"
                     /note="isoform a preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:24482"
                     /db_xref="RGD:2868"
ORIGIN      
        1 msappikihi mssshlfyla lclltftssa tagpetlcga elvdalqfvc gprgfyfnkp
       61 tgygssirra pqtgivdecc frscdlrrle mycaplkptk sarsiraqrh tdmpktqksq
      121 plsthkkrkl qrrrkgstle ehk
//
LOCUS       NP_001409929             919 aa            linear   ROD 11-MAR-2025
DEFINITION  sarcosine dehydrogenase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001409929 XP_006233794
VERSION     NP_001409929.1
DBSOURCE    REFSEQ: accession NM_001423000.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Tibbetts,A.S. and Appling,D.R.
  TITLE     Compartmentalization of Mammalian folate-mediated one-carbon
            metabolism
  JOURNAL   Annu Rev Nutr 30, 57-81 (2010)
   PUBMED   20645850
  REMARK    Review article
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Bergeron,F., Otto,A., Blache,P., Day,R., Denoroy,L., Brandsch,R.
            and Bataille,D.
  TITLE     Molecular cloning and tissue distribution of rat sarcosine
            dehydrogenase
  JOURNAL   Eur J Biochem 257 (3), 556-561 (1998)
   PUBMED   9839943
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Porter,D.H., Cook,R.J. and Wagner,C.
  TITLE     Enzymatic properties of dimethylglycine dehydrogenase and sarcosine
            dehydrogenase from rat liver
  JOURNAL   Arch Biochem Biophys 243 (2), 396-407 (1985)
   PUBMED   2417560
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Cook,R.J., Misono,K.S. and Wagner,C.
  TITLE     The amino acid sequences of the flavin-peptides of dimethylglycine
            dehydrogenase and sarcosine dehydrogenase from rat liver
            mitochondria
  JOURNAL   J Biol Chem 260 (24), 12998-13002 (1985)
   PUBMED   4055729
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Wittwer,A.J. and Wagner,C.
  TITLE     Identification of the folate-binding proteins of rat liver
            mitochondria as dimethylglycine dehydrogenase and sarcosine
            dehydrogenase. Flavoprotein nature and enzymatic properties of the
            purified proteins
  JOURNAL   J Biol Chem 256 (8), 4109-4115 (1981)
   PUBMED   6163778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jun 29, 2023 this sequence version replaced XP_006233794.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.12981.1,
                                           SRR26643429.10874.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..919
                     /product="sarcosine dehydrogenase, mitochondrial"
                     /EC_number="1.5.8.3"
                     /calculated_mol_wt=99060
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=2373
     mat_peptide     23..919
                     /product="Sarcosine dehydrogenase, mitochondrial.
                     /id=PRO_0000010772"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=99060
     Region          67..445
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Region          431..486
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          481..917
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL12; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            803
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            885
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            905
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     CDS             1..919
                     /gene="Sardh"
                     /coded_by="NM_001423000.1:539..3298"
                     /db_xref="GeneID:114123"
                     /db_xref="RGD:621125"
ORIGIN      
        1 maslsrvlrv aatcprgrsa rnlglqplar earptteksv pyqctlkeea qgasvvpqgp
       61 sqplpstanv vvigggslgc qtlyhlaklg vggvvllere rltsgttwht agllwqlrps
      121 dvevellaht rqvvshdlee etglhtgwiq ngglfiasnq qrldeykrlm slgkaygies
      181 hvlspaetkd lyplmnvddl ygtlyvprdg tmdpagtctt ltraavarga qviencavtg
      241 irvrtddfgv rrvtavetqh gsiqtpcvvn cagvwassvg rmagvkvplv amhhayvvte
      301 riegiqnmpn vrdhdasvyl rlqgdalsvg gyeanpifwd evsdkfafgl fdldwdvftq
      361 hiegainrvp vlektgikst vcgpesftpd hkplmgeape lrgfflgcgf nsagmmlggg
      421 cgqelahwiv hgrpekdmys ydirrfhhsl tdhprwirer shesyaknys vvfphdepla
      481 grnmrrdplh eellgqgcvf qerqgwerpg wfnpqetaqv ldydyygayg hqahkdyays
      541 rllgdeytfd fpphhcviqk eclacrtaaa vfnmsyfgkf yllgadarka adwlfsadvn
      601 rppgstvytc mlnqrggtes dltvsclapg aqasplapaf egdgyylavg gavaqhnwsh
      661 intvlqdqef rcqlmdcsed lgmlsiqgpa srdilqdvld adlsneafpf sthqlvraag
      721 hlvrairlsf vgelgwelhv pqasclpvyr avmaagakhg lvnagyraid slsiekgyrh
      781 whadlrsdds pleaglaftc klktsvpflg realekqrat glrrrlvclt veeevpmfgl
      841 eaiwrngqvv ghvrradfgf tvnktiaygy irdpsggpvs ldfvkngdya lermgvtyaa
      901 qvhlkspfdp dnkrvkgiy
//
LOCUS       NP_001075947             159 aa            linear   ROD 11-MAR-2025
DEFINITION  insulin-like growth factor 1 isoform c preproprotein [Rattus
            norvegicus].
ACCESSION   NP_001075947
VERSION     NP_001075947.1
DBSOURCE    REFSEQ: accession NM_001082478.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Xiong,J., Wang,Y., Wang,H., Luo,J., Chen,T., Sun,J., Xi,Q. and
            Zhang,Y.
  TITLE     GHRH-stimulated pituitary small extracellular vesicles inhibit
            hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p
  JOURNAL   J Nanobiotechnology 22 (1), 649 (2024)
   PUBMED   39438882
  REMARK    GeneRIF: GHRH-stimulated pituitary small extracellular vesicles
            inhibit hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Maleki,A.H., Azar,J.T., Razi,M. and Tofighi,A.
  TITLE     The Effect of Different Exercise Modalities on Sertoli-germ Cells
            Metabolic Interactions in High-fat Diet-induced Obesity Rat Models:
            Implication on Glucose and Lactate Transport, Igf1, and
            Igf1R-dependent Pathways
  JOURNAL   Reprod Sci 31 (8), 2246-2260 (2024)
   PUBMED   38632221
  REMARK    GeneRIF: The Effect of Different Exercise Modalities on
            Sertoli-germ Cells Metabolic Interactions in High-fat Diet-induced
            Obesity Rat Models: Implication on Glucose and Lactate Transport,
            Igf1, and Igf1R-dependent Pathways.
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Banjac,K., Obradovic,M., Zafirovic,S., Essack,M., Gluvic,Z.,
            Sunderic,M., Nedic,O. and Isenovic,E.R.
  TITLE     The involvement of Akt, mTOR, and S6K in the in vivo effect of
            IGF-1 on the regulation of rat cardiac Na+/K+-ATPase
  JOURNAL   Mol Biol Rep 51 (1), 517 (2024)
   PUBMED   38622478
  REMARK    GeneRIF: The involvement of Akt, mTOR, and S6K in the in vivo
            effect of IGF-1 on the regulation of rat cardiac Na[+]/K[+]-ATPase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Barik,P., Kuo,W.W., Kuo,C.H., Hsieh,D.J., Day,C.H., Daddam,J.,
            Chen,M.Y., Padma,V.V., Shibu,M.A. and Huang,C.Y.
  TITLE     Rewiring of IGF1 secretion and enhanced IGF1R signaling induced by
            co-chaperone carboxyl-terminus of Hsp70 interacting protein in
            adipose-derived stem cells provide augmented cardioprotection in
            aging-hypertensive rats
  JOURNAL   Aging (Albany NY) 15 (23), 14019-14038 (2023)
   PUBMED   38085649
  REMARK    GeneRIF: Rewiring of IGF1 secretion and enhanced IGF1R signaling
            induced by co-chaperone carboxyl-terminus of Hsp70 interacting
            protein in adipose-derived stem cells provide augmented
            cardioprotection in aging-hypertensive rats.
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Zhao,H., Wang,L., Yan,Y., Zhao,Q.H., He,J., Jiang,R., Luo,C.J.,
            Qiu,H.L., Miao,Y.Q., Gong,S.G., Yuan,P. and Wu,W.H.
  TITLE     Identification of the shared gene signatures between pulmonary
            fibrosis and pulmonary hypertension using bioinformatics analysis
  JOURNAL   Front Immunol 14, 1197752 (2023)
   PUBMED   37731513
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Nanto-Salonen,K. and Rosenfeld,R.G.
  TITLE     Insulin-like growth factor binding protein expression in the
            hypothyroid rat is age dependent
  JOURNAL   Endocrinology 131 (3), 1489-1496 (1992)
   PUBMED   1380443
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Hall,L.J., Kajimoto,Y., Bichell,D., Kim,S.W., James,P.L.,
            Counts,D., Nixon,L.J., Tobin,G. and Rotwein,P.
  TITLE     Functional analysis of the rat insulin-like growth factor I gene
            and identification of an IGF-I gene promoter
  JOURNAL   DNA Cell Biol 11 (4), 301-313 (1992)
   PUBMED   1605853
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Bouillon,R.
  TITLE     Diabetic bone disease. Low turnover osteoporosis related to
            decreased IGF-I production
  JOURNAL   Verh K Acad Geneeskd Belg 54 (4), 365-91 (1992)
   PUBMED   1466160
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Nanto-Salonen,K., Glasscock,G.F. and Rosenfeld,R.G.
  TITLE     The effects of thyroid hormone on insulin-like growth factor (IGF)
            and IGF-binding protein (IGFBP) expression in the neonatal rat:
            prolonged high expression of IGFBP-2 in methimazole-induced
            congenital hypothyroidism
  JOURNAL   Endocrinology 129 (5), 2563-2570 (1991)
   PUBMED   1718729
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Kato,H., Okoshi,A., Miura,Y. and Noguchi,T.
  TITLE     A new cDNA clone relating to larger molecular species of rat
            insulin-like growth factor-I mRNA
  JOURNAL   Agric Biol Chem 54 (6), 1599-1601 (1990)
   PUBMED   1368571
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB751206.1, BC086374.1, M15480.1 and CB761687.1.
            
            Transcript Variant: This variant (3) represents the longest variant
            and encodes isoform c. This isoform is also known as IB.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X06107.1, FQ210560.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..159
                     /product="insulin-like growth factor 1 isoform c
                     preproprotein"
                     /note="somatomedin; IGF-I; Insulin-like growth factor I"
                     /calculated_mol_wt=12640
     sig_peptide     1..48
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5338
     proprotein      49..159
                     /product="insulin-like growth factor 1 isoform c
                     proprotein"
                     /calculated_mol_wt=12640
     mat_peptide     49..118
                     /product="insulin-like growth factor 1 isoform c"
                     /calculated_mol_wt=7693
     Region          49..116
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Region          49..77
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Site            order(51,60,68..72)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(69,71..72,92)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Region          78..89
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Region          90..110
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Site            order(97..99,103..104)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          111..118
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     CDS             1..159
                     /gene="Igf1"
                     /gene_synonym="IGF"
                     /coded_by="NM_001082478.1:281..760"
                     /note="isoform c preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:24482"
                     /db_xref="RGD:2868"
ORIGIN      
        1 mgkisslptq lfkiclcdfl kikihimsss hlfylalcll tftssatagp etlcgaelvd
       61 alqfvcgprg fyfnkptgyg ssirrapqtg ivdeccfrsc dlrrlemyca plkptksars
      121 iraqrhtdmp ktqksqplst hkkrklqrrr kgstleehk
//
LOCUS       NP_036744                152 aa            linear   ROD 11-MAR-2025
DEFINITION  natriuretic peptides A precursor [Rattus norvegicus].
ACCESSION   NP_036744
VERSION     NP_036744.1
DBSOURCE    REFSEQ: accession NM_012612.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Huang,Y., Wang,L.L., Liu,Z.B., Chen,C., Ren,X., Luo,A.T., Ma,J.H.,
            Antzelevitch,C., Barajas-Martinez,H. and Hu,D.
  TITLE     Underlying mechanism of atrial fibrillation-associated Nppa-I137T
            mutation and cardiac effect of potential drug therapy
  JOURNAL   Heart Rhythm 21 (2), 184-196 (2024)
   PUBMED   37924963
  REMARK    GeneRIF: Underlying mechanism of atrial fibrillation-associated
            Nppa-I137T mutation and cardiac effect of potential drug therapy.
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Dogra,A., Kour,D., Gour,A., Bhardwaj,M., Bag,S., Dhiman,S.K.,
            Kumar,A., Singh,G. and Nandi,U.
  TITLE     Ameliorating effect of rutin against diclofenac-induced cardiac
            injury in rats with underlying function of FABP3, MYL3, and ANP
  JOURNAL   Drug Chem Toxicol 46 (3), 597-608 (2023)
   PUBMED   35509154
  REMARK    GeneRIF: Ameliorating effect of rutin against diclofenac-induced
            cardiac injury in rats with underlying function of FABP3, MYL3, and
            ANP.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Zhang,Y., Wang,S., Huang,Y., Yang,K., Liu,Y., Bi,X., Liu,C.,
            Xiong,J., Zhang,B., Zhao,J. and Nie,L.
  TITLE     Inhibition of CYP1B1 ameliorates cardiac hypertrophy induced by
            uremic toxin
  JOURNAL   Mol Med Rep 21 (1), 393-404 (2020)
   PUBMED   31746392
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Li,X., Han,Z.N., Liu,Y., Hong,L., Cui,B.R. and Cui,X.
  TITLE     Endogenous ET-1 promotes ANP secretion through activation of
            COX2-L-PGDS-PPARgamma signaling in hypoxic beating rat atria
  JOURNAL   Peptides 122, 170150 (2019)
   PUBMED   31541683
  REMARK    GeneRIF: These results indicate that endogenous ET-1 induced by
            hypoxia promotes hypoxia-induced ANP secretion by activation of
            COX2-L-PGDS-PPARgamma signaling in beating rat atria
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Yu,L., Li,W., Park,B.M., Lee,G.J. and Kim,S.H.
  TITLE     Hypoxia augments NaHS-induced ANP secretion via KATP channel,
            HIF-1alpha and PPAR-gamma pathway
  JOURNAL   Peptides 121, 170123 (2019)
   PUBMED   31386893
  REMARK    GeneRIF: Hypoxia augments NaHS-induced ANP secretion via KATP
            channel, HIF-1A and PPAR-gamma pathway.
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Ramirez,G., Saba,S.R., Dietz,J.R. and Vesely,D.L.
  TITLE     Immunocytochemical localization of proANF 1-30, proANF 31-67 and
            atrial natriuretic factor in the kidney
  JOURNAL   Kidney Int 41 (2), 334-341 (1992)
   PUBMED   1372667
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Bennett,B.D., Bennett,G.L., Vitangcol,R.V., Jewett,J.R.,
            Burnier,J., Henzel,W. and Lowe,D.G.
  TITLE     Extracellular domain-IgG fusion proteins for three human
            natriuretic peptide receptors. Hormone pharmacology and application
            to solid phase screening of synthetic peptide antisera
  JOURNAL   J Biol Chem 266 (34), 23060-23067 (1991)
   PUBMED   1660465
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Levin,E.R. and Frank,H.J.
  TITLE     Natriuretic peptides inhibit rat astroglial proliferation:
            mediation by C receptor
  JOURNAL   Am J Physiol 261 (2 Pt 2), R453-R457 (1991)
   PUBMED   1652217
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Koller,K.J., Lowe,D.G., Bennett,G.L., Minamino,N., Kangawa,K.,
            Matsuo,H. and Goeddel,D.V.
  TITLE     Selective activation of the B natriuretic peptide receptor by
            C-type natriuretic peptide (CNP)
  JOURNAL   Science 252 (5002), 120-123 (1991)
   PUBMED   1672777
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Jin,H., Yang,R.H., Chen,Y.F., Jackson,R.M. and Oparil,S.
  TITLE     Atrial natriuretic peptide attenuates the development of pulmonary
            hypertension in rats adapted to chronic hypoxia
  JOURNAL   J Clin Invest 85 (1), 115-120 (1990)
   PUBMED   2136863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB724799.1, X00665.1 and AI602287.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EV765126.1, BC158590.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..152
                     /product="natriuretic peptides A precursor"
                     /note="Natriuretic peptide precursor A (pronatriodilatin,
                     also Anf, Pnd); natriuretic peptides A;
                     prepronatriodilatin; natriuretic peptide precursor type A;
                     proANF; proANP; preproANF; preproANP; atriopeptigen;
                     cardiodilatin; preproCDD-ANF; atrial natriuretic factor
                     prohormone; atrial natriuretic peptide prohormone"
                     /calculated_mol_wt=13929
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2645
     mat_peptide     25..150
                     /product="Natriuretic peptides A.
                     /evidence=ECO:0000250|UniProtKB:P01160.
                     /id=PRO_0000449770"
                     /note="propagated from UniProtKB/Swiss-Prot (P01161.1)"
                     /calculated_mol_wt=13616
     Region          54..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01161.1)"
     Region          122..145
                     /region_name="NAT_PEP"
                     /note="Natriuretic peptide; smart00183"
                     /db_xref="CDD:128480"
     Site            122..123
                     /site_type="cleavage"
                     /note="Cleavage, by CORIN.
                     /evidence=ECO:0000250|UniProtKB:P01160; propagated from
                     UniProtKB/Swiss-Prot (P01161.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01160; propagated from
                     UniProtKB/Swiss-Prot (P01161.1)"
     Site            129..130
                     /site_type="cleavage"
                     /note="Cleavage, by MME.
                     /evidence=ECO:0000269|PubMed:2966343; propagated from
                     UniProtKB/Swiss-Prot (P01161.1)"
     Region          146..150
                     /region_name="Important for degradation of atrial
                     natriuretic peptide by IDE.
                     /evidence=ECO:0000250|UniProtKB:P01160"
                     /note="propagated from UniProtKB/Swiss-Prot (P01161.1)"
     CDS             1..152
                     /gene="Nppa"
                     /gene_synonym="ANF; ANP; CDD; Pnd; RATANF"
                     /coded_by="NM_012612.2:77..535"
                     /db_xref="GeneID:24602"
                     /db_xref="RGD:3193"
ORIGIN      
        1 mgsfsitkgf flflafwlpg higanpvysa vsntdlmdfk nlldhleekm pvedevmppq
       61 alseqtdeag aalsslsevp pwtgevnpsq rdggalgrgp wdpsdrsall ksklrallag
      121 prslrrsscf ggridrigaq sglgcnsfry rr
//
LOCUS       NP_001416579             919 aa            linear   ROD 11-MAR-2025
DEFINITION  sarcosine dehydrogenase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001416579 XP_006233793
VERSION     NP_001416579.1
DBSOURCE    REFSEQ: accession NM_001429650.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Tibbetts,A.S. and Appling,D.R.
  TITLE     Compartmentalization of Mammalian folate-mediated one-carbon
            metabolism
  JOURNAL   Annu Rev Nutr 30, 57-81 (2010)
   PUBMED   20645850
  REMARK    Review article
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Bergeron,F., Otto,A., Blache,P., Day,R., Denoroy,L., Brandsch,R.
            and Bataille,D.
  TITLE     Molecular cloning and tissue distribution of rat sarcosine
            dehydrogenase
  JOURNAL   Eur J Biochem 257 (3), 556-561 (1998)
   PUBMED   9839943
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Porter,D.H., Cook,R.J. and Wagner,C.
  TITLE     Enzymatic properties of dimethylglycine dehydrogenase and sarcosine
            dehydrogenase from rat liver
  JOURNAL   Arch Biochem Biophys 243 (2), 396-407 (1985)
   PUBMED   2417560
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Cook,R.J., Misono,K.S. and Wagner,C.
  TITLE     The amino acid sequences of the flavin-peptides of dimethylglycine
            dehydrogenase and sarcosine dehydrogenase from rat liver
            mitochondria
  JOURNAL   J Biol Chem 260 (24), 12998-13002 (1985)
   PUBMED   4055729
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Wittwer,A.J. and Wagner,C.
  TITLE     Identification of the folate-binding proteins of rat liver
            mitochondria as dimethylglycine dehydrogenase and sarcosine
            dehydrogenase. Flavoprotein nature and enzymatic properties of the
            purified proteins
  JOURNAL   J Biol Chem 256 (8), 4109-4115 (1981)
   PUBMED   6163778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 24, 2024 this sequence version replaced XP_006233793.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.14641.1,
                                           SRR26643294.12389.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..919
                     /product="sarcosine dehydrogenase, mitochondrial"
                     /EC_number="1.5.8.3"
                     /calculated_mol_wt=99060
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=2373
     mat_peptide     23..919
                     /product="Sarcosine dehydrogenase, mitochondrial.
                     /id=PRO_0000010772"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=99060
     Region          67..445
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Region          431..486
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          481..917
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL12; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            803
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            885
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            905
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     CDS             1..919
                     /gene="Sardh"
                     /coded_by="NM_001429650.1:92..2851"
                     /db_xref="GeneID:114123"
                     /db_xref="RGD:621125"
ORIGIN      
        1 maslsrvlrv aatcprgrsa rnlglqplar earptteksv pyqctlkeea qgasvvpqgp
       61 sqplpstanv vvigggslgc qtlyhlaklg vggvvllere rltsgttwht agllwqlrps
      121 dvevellaht rqvvshdlee etglhtgwiq ngglfiasnq qrldeykrlm slgkaygies
      181 hvlspaetkd lyplmnvddl ygtlyvprdg tmdpagtctt ltraavarga qviencavtg
      241 irvrtddfgv rrvtavetqh gsiqtpcvvn cagvwassvg rmagvkvplv amhhayvvte
      301 riegiqnmpn vrdhdasvyl rlqgdalsvg gyeanpifwd evsdkfafgl fdldwdvftq
      361 hiegainrvp vlektgikst vcgpesftpd hkplmgeape lrgfflgcgf nsagmmlggg
      421 cgqelahwiv hgrpekdmys ydirrfhhsl tdhprwirer shesyaknys vvfphdepla
      481 grnmrrdplh eellgqgcvf qerqgwerpg wfnpqetaqv ldydyygayg hqahkdyays
      541 rllgdeytfd fpphhcviqk eclacrtaaa vfnmsyfgkf yllgadarka adwlfsadvn
      601 rppgstvytc mlnqrggtes dltvsclapg aqasplapaf egdgyylavg gavaqhnwsh
      661 intvlqdqef rcqlmdcsed lgmlsiqgpa srdilqdvld adlsneafpf sthqlvraag
      721 hlvrairlsf vgelgwelhv pqasclpvyr avmaagakhg lvnagyraid slsiekgyrh
      781 whadlrsdds pleaglaftc klktsvpflg realekqrat glrrrlvclt veeevpmfgl
      841 eaiwrngqvv ghvrradfgf tvnktiaygy irdpsggpvs ldfvkngdya lermgvtyaa
      901 qvhlkspfdp dnkrvkgiy
//
LOCUS       NP_112369                735 aa            linear   ROD 11-MAR-2025
DEFINITION  ribosomal protein S6 kinase alpha-1 [Rattus norvegicus].
ACCESSION   NP_112369
VERSION     NP_112369.2
DBSOURCE    REFSEQ: accession NM_031107.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Takegaki,J., Sase,K. and Fujita,S.
  TITLE     Repeated bouts of resistance exercise attenuate mitogen-activated
            protein-kinase signal responses in rat skeletal muscle
  JOURNAL   Biochem Biophys Res Commun 520 (1), 73-78 (2019)
   PUBMED   31582215
  REMARK    GeneRIF: repeated bouts of resistance training desensitized ERK1/2
            and p38 MAPK, subsequently attenuating p90RSK phosphorylation in a
            rat model
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Han,J.H., Kim,S., Kim,S., Lee,H., Park,S.Y. and Woo,C.H.
  TITLE     FMK, an Inhibitor of p90RSK, Inhibits High Glucose-Induced TXNIP
            Expression via Regulation of ChREBP in Pancreatic beta Cells
  JOURNAL   Int J Mol Sci 20 (18), 4424 (2019)
   PUBMED   31505737
  REMARK    GeneRIF: FMK, an Inhibitor of p90RSK, Inhibits High Glucose-Induced
            TXNIP Expression via Regulation of ChREBP in Pancreatic beta Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Dou,X., Menkari,C., Mitsuyama,R., Foroud,T., Wetherill,L.,
            Hammond,P., Suttie,M., Chen,X., Chen,S.Y. and Charness,M.E.
  CONSRTM   Collaborative Initiative on Fetal Alcohol Spectrum Disorders
  TITLE     L1 coupling to ankyrin and the spectrin-actin cytoskeleton
            modulates ethanol inhibition of L1 adhesion and ethanol
            teratogenesis
  JOURNAL   FASEB J 32 (3), 1364-1374 (2018)
   PUBMED   29109170
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Carretero,L., Llavona,P., Lopez-Hernandez,A., Casado,P.,
            Cutillas,P.R., de la Pena,P., Barros,F. and Dominguez,P.
  TITLE     ERK and RSK are necessary for TRH-induced inhibition of r-ERG
            potassium currents in rat pituitary GH3 cells
  JOURNAL   Cell Signal 27 (9), 1720-1730 (2015)
   PUBMED   26022182
  REMARK    GeneRIF: in the native GH3 cell system, ERK and RSK are involved in
            the pathway linking TRH receptor to r-ERG channel inhibition, but
            additional components must participate to cause such inhibition.
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Seow,K.H., Zhou,L., Stephanopoulos,G. and Too,H.P.
  TITLE     c-Jun N-terminal kinase in synergistic neurite outgrowth in PC12
            cells mediated through P90RSK
  JOURNAL   BMC Neurosci 14, 153 (2013)
   PUBMED   24330599
  REMARK    GeneRIF: Our findings demonstrate a hitherto unrecognized mechanism
            of c-Jun N-terminal kinase-P90RSK in mediating synergistic neurite
            outgrowth
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Buck,M., Poli,V., van der Geer,P., Chojkier,M. and Hunter,T.
  TITLE     Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP
            beta is required for hepatocyte proliferation induced by TGF alpha
  JOURNAL   Mol Cell 4 (6), 1087-1092 (1999)
   PUBMED   10635333
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Suzuki,T., Mitake,S. and Murata,S.
  TITLE     Presence of up-stream and downstream components of a
            mitogen-activated protein kinase pathway in the PSD of the rat
            forebrain
  JOURNAL   Brain Res 840 (1-2), 36-44 (1999)
   PUBMED   10517950
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Smith,J.A., Poteet-Smith,C.E., Malarkey,K. and Sturgill,T.W.
  TITLE     Identification of an extracellular signal-regulated kinase (ERK)
            docking site in ribosomal S6 kinase, a sequence critical for
            activation by ERK in vivo
  JOURNAL   J Biol Chem 274 (5), 2893-2898 (1999)
   PUBMED   9915826
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Wong,E.V., Schaefer,A.W., Landreth,G. and Lemmon,V.
  TITLE     Involvement of p90rsk in neurite outgrowth mediated by the cell
            adhesion molecule L1
  JOURNAL   J Biol Chem 271 (30), 18217-18223 (1996)
   PUBMED   8663493
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Grove,J.R., Price,D.J., Banerjee,P., Balasubramanyam,A., Ahmad,M.F.
            and Avruch,J.
  TITLE     Regulation of an epitope-tagged recombinant Rsk-1 S6 kinase by
            phorbol ester and erk/MAP kinase
  JOURNAL   Biochemistry 32 (30), 7727-7738 (1993)
   PUBMED   7688567
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 26, 2020 this sequence version replaced NP_112369.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M99169.1, SRR22582416.149335.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..735
                     /product="ribosomal protein S6 kinase alpha-1"
                     /EC_number="2.7.11.1"
                     /note="RSK-1; p90S6K; pp90RSK1; ribosomal protein S6
                     kinase polypeptide 1; MAPKAPK1A; p90-RSK 1; ribosomal S6
                     kinase 1; ribosomal protein S6 kinase, polypeptide A1; 90
                     kDa ribosomal protein S6 kinase 1; MAP kinase-activated
                     protein kinase 1a; p90RSK1; MAPKAPK-1a; S6K-alpha-1;
                     MAPKAP kinase 1a; MAPK-activated protein kinase 1a; S6
                     protein kinase (Rsk-1)"
                     /calculated_mol_wt=82793
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Region          66..382
                     /region_name="STKc_RSK_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, 90 kDa ribosomal protein S6 kinase; cd05582"
                     /db_xref="CDD:270734"
     Site            order(68..72,76,92,94,125,141..142,144,148,150,187,189,
                     191..192,194,204..205,208,222..227,254,260,263)
                     /site_type="active"
                     /db_xref="CDD:270734"
     Site            order(68..72,76,92,94,125,142..144,148,187,189,191..192,
                     194,204..205)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270734"
     Site            order(72,148,150,187,189,191,208,222..227,254,260,263)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270734"
     Site            order(204..215,217..227)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270734"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDPK1.
                     /evidence=ECO:0000269|PubMed:10480933; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            363
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270734"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            376..381
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270734"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Region          416..706
                     /region_name="STKc_RSK1_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Ribosomal S6 kinase 1 (also called Ribosomal
                     protein S6 kinase alpha-1 or 90kDa ribosomal protein S6
                     kinase 1); cd14175"
                     /db_xref="CDD:271077"
     Site            order(424..428,432,445,447,473,489..492,496,498,534..535,
                     537,539..540,542,556..557,560,575..579,581)
                     /site_type="active"
                     /db_xref="CDD:271077"
     Site            order(424..427,432,445,447,473,489..492,496,539..540,542,
                     556..557)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271077"
     Site            order(428,496,498,534..535,537,539,560,575..579,581)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271077"
     Site            556..579
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271077"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15418; propagated from
                     UniProtKB/Swiss-Prot (Q63531.1)"
     CDS             1..735
                     /gene="Rps6ka1"
                     /gene_synonym="S6K-alpha 1"
                     /coded_by="NM_031107.2:143..2350"
                     /db_xref="GeneID:81771"
                     /db_xref="RGD:620675"
ORIGIN      
        1 mplaqlkepw plmelvpldp engqasgeea glqpskdegi lkeisithhv kagsekadps
       61 hfellkvlgq gsfgkvflvr kvtrpdnghl yamkvlkkat lkvrdrvrtk merdiladvn
      121 hpfvvklhya fqtegklyli ldflrggdlf trlskevmft eedvkfylae lalgldhlhs
      181 lgiiyrdlkp enilldeegh ikltdfglsk eaidhekkay sfcgtveyma pevvnrqght
      241 hsadwwsygv lmfemltgsl pfqgkdrket mtlilkaklg mpqflsteaq sllralfkrn
      301 panrlgsgpd gaeeikrhif ystidwnkly rreikppfkp avaqpddtfy fdteftsrtp
      361 rdspgippsa gahqlfrgfs fvatglmedd skpratqapl hsvvqqlhgk nlvfsdgyiv
      421 ketigvgsys vckrcvhkat nmeyavkvid kskrdpseei eillrygqhp niitlkdvyd
      481 dskhvylvte lmrggelldk ilrqkffser easfvlytis ktveylhsqg vvhrdlkpsn
      541 ilyvdesgnp eclricdfgf akqlraengl lmtpcytanf vapevlkrqg ydegcdiwsl
      601 gvllytmlag ytpfangpsd tpeeiltris sgkftlnggn wntvsetakd lvskmlhvdp
      661 hqrltakqvl qhpwitqkdk lpqsqlshqd lqlvkgamaa tysalssskp tpqlkpiess
      721 ilaqrrvrkl psttl
//
LOCUS       NP_036872                498 aa            linear   ROD 11-MAR-2025
DEFINITION  tyrosine 3-monooxygenase [Rattus norvegicus].
ACCESSION   NP_036872
VERSION     NP_036872.1
DBSOURCE    REFSEQ: accession NM_012740.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Yamaguchi,H., Hara,S., Ichinose,H., Nagasaki,H. and Nakashima,A.
  TITLE     Role of NT5DC2 in tyrosine hydroxylase phosphorylation based on the
            analysis of NT5DC2-binding proteins
  JOURNAL   Biochem Biophys Res Commun 703, 149698 (2024)
   PUBMED   38382359
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Zhang,Y., Tsai,T.H., Ezrokhi,M., Stoelzel,C. and Cincotta,A.H.
  TITLE     Tyrosine Hydroxylase Knockdown at the Hypothalamic Supramammillary
            Nucleus Area Induces Obesity and Glucose Intolerance
  JOURNAL   Neuroendocrinology 114 (5), 483-510 (2024)
   PUBMED   38128505
  REMARK    GeneRIF: Tyrosine Hydroxylase Knockdown at the Hypothalamic
            Supramammillary Nucleus Area Induces Obesity and Glucose
            Intolerance.
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Leem,K.H., Kim,S., Kim,H.W. and Park,H.J.
  TITLE     Downregulation of microRNA-330-5p induces manic-like behaviors in
            REM sleep-deprived rats by enhancing tyrosine hydroxylase
            expression
  JOURNAL   CNS Neurosci Ther 29 (6), 1525-1536 (2023)
   PUBMED   36794530
  REMARK    GeneRIF: Downregulation of microRNA-330-5p induces manic-like
            behaviors in REM sleep-deprived rats by enhancing tyrosine
            hydroxylase expression.
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Cassinotti,L., Guil,M., Bianciotti,L. and Vatta,M.
  TITLE     Role of Brain Endothelin Receptor Type B (ETB) in the Regulation of
            Tyrosine Hydroxylase in the Olfactory Bulb of DOCA-Salt
            Hypertensive Rats
  JOURNAL   Curr Vasc Pharmacol 21 (4), 246-256 (2023)
   PUBMED   37349999
  REMARK    GeneRIF: Role of Brain Endothelin Receptor Type B (ETB) in the
            Regulation of Tyrosine Hydroxylase in the Olfactory Bulb of
            DOCA-Salt Hypertensive Rats.
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Jimenez,A., Herrera-Gonzalez,A., Organista-Juarez,D., Estudillo,E.,
            Velasco,I., Guerrero-Vargas,N.N., Guzman-Ruiz,M.A. and
            Guevara-Guzman,R.
  TITLE     Diabetes Induces Permanent Deleterious Effects in the Olfactory
            Bulb Associated with Increased Tyrosine Hydroxylase Expression and
            ERK1/2 Phosphorylation
  JOURNAL   ACS Chem Neurosci 13 (19), 2821-2828 (2022)
   PUBMED   36122168
  REMARK    GeneRIF: Diabetes Induces Permanent Deleterious Effects in the
            Olfactory Bulb Associated with Increased Tyrosine Hydroxylase
            Expression and ERK1/2 Phosphorylation.
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Haycock,J.W. and Haycock,D.A.
  TITLE     Tyrosine hydroxylase in rat brain dopaminergic nerve terminals.
            Multiple-site phosphorylation in vivo and in synaptosomes
  JOURNAL   J Biol Chem 266 (9), 5650-5657 (1991)
   PUBMED   1672315
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Wolff,J.A., Fisher,L.J., Xu,L., Jinnah,H.A., Langlais,P.J.,
            Iuvone,P.M., O'Malley,K.L., Rosenberg,M.B., Shimohama,S.,
            Friedmann,T. et al.
  TITLE     Grafting fibroblasts genetically modified to produce L-dopa in a
            rat model of Parkinson disease
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 9011-9014 (1989)
   PUBMED   2573072
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Horellou,P., Guibert,B., Leviel,V. and Mallet,J.
  TITLE     A single RNA species injected in Xenopus oocyte directs the
            synthesis of active tyrosine hydroxylase
  JOURNAL   FEBS Lett 205 (1), 6-10 (1986)
   PUBMED   2427363
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Grima,B., Lamouroux,A., Blanot,F., Biguet,N.F. and Mallet,J.
  TITLE     Complete coding sequence of rat tyrosine hydroxylase mRNA
  JOURNAL   Proc Natl Acad Sci U S A 82 (2), 617-621 (1985)
   PUBMED   2857492
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Joh,T.H., Park,D.H. and Reis,D.J.
  TITLE     Direct phosphorylation of brain tyrosine hydroxylase by cyclic
            AMP-dependent protein kinase: mechanism of enzyme activation
  JOURNAL   Proc Natl Acad Sci U S A 75 (10), 4744-4748 (1978)
   PUBMED   33381
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M10244.1, SRR26360194.681303.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..498
                     /product="tyrosine 3-monooxygenase"
                     /EC_number="1.14.16.2"
                     /note="tyrosine 3-hydroxylase"
                     /calculated_mol_wt=55835
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04177.3)"
     Region          2..26
                     /region_name="TOH_N"
                     /note="Tyrosine hydroxylase N terminal; pfam12549"
                     /db_xref="CDD:403668"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000269|PubMed:11502746,
                     ECO:0000269|PubMed:1672315, ECO:0000269|PubMed:21392500,
                     ECO:0000269|PubMed:32778969, ECO:0000269|PubMed:38382359;
                     propagated from UniProtKB/Swiss-Prot (P04177.3)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1672315,
                     ECO:0000269|PubMed:21392500, ECO:0000269|PubMed:32778969,
                     ECO:0000269|PubMed:38382359; propagated from
                     UniProtKB/Swiss-Prot (P04177.3)"
     Region          38..158
                     /region_name="ACT_TH"
                     /note="ACT domain of the nonheme iron-dependent aromatic
                     amino acid hydroxylase, tyrosine hydroxylases (TH);
                     cd04930"
                     /db_xref="CDD:153202"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2 and PKA.
                     /evidence=ECO:0000269|PubMed:11502746,
                     ECO:0000269|PubMed:1672315, ECO:0000269|PubMed:21392500,
                     ECO:0000269|PubMed:32778969, ECO:0000269|PubMed:38382359;
                     propagated from UniProtKB/Swiss-Prot (P04177.3)"
     Site            order(95..98,115..118)
                     /site_type="other"
                     /note="putative amino acid binding site [chemical
                     binding]"
                     /db_xref="CDD:153202"
     Region          165..495
                     /region_name="Biopterin_H"
                     /note="Biopterin-dependent aromatic amino acid
                     hydroxylase; pfam00351"
                     /db_xref="CDD:459776"
     Site            425
                     /site_type="other"
                     /note="Important for substrate specificity.
                     /evidence=ECO:0000269|PubMed:10933781; propagated from
                     UniProtKB/Swiss-Prot (P04177.3)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P24529; propagated from
                     UniProtKB/Swiss-Prot (P04177.3)"
     CDS             1..498
                     /gene="Th"
                     /gene_synonym="The"
                     /coded_by="NM_012740.4:12..1508"
                     /db_xref="GeneID:25085"
                     /db_xref="RGD:3853"
ORIGIN      
        1 mptpsapspq pkgfrravse qdakqaeavt sprfigrrqs liedarkere aaaaaaaaav
       61 assepgnple avvfeerdgn avlnllfslr gtkpsslsra vkvfetfeak ihhletrpaq
      121 rplagsphle yfvrfevpsg dlaallssvr rvsddvrsar edkvpwfprk vseldkchhl
      181 vtkfdpdldl dhpgfsdqvy rqrrkliaei afqykhgepi phveytaeei atwkevyvtl
      241 kglyathacr ehlegfqlle rycgyredsi pqledvsrfl kertgfqlrp vagllsardf
      301 laslafrvfq ctqyirhass pmhspepdcc hellghvpml adrtfaqfsq diglaslgas
      361 deeieklstv ywftvefglc kqngelkayg agllssygel lhslseepev rafdpdtaav
      421 qpyqdqtyqp vyfvsesfnd akdklrnyas riqrpfsvkf dpytlaidvl dsphtiqrsl
      481 egvqdelhtl ahalsais
//
LOCUS       NP_001413962            1373 aa            linear   ROD 11-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 10 [Rattus norvegicus].
ACCESSION   NP_001413962 XP_002728482
VERSION     NP_001413962.1
DBSOURCE    REFSEQ: accession NM_001427033.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1373)
  AUTHORS   Haaland,O.A., Romanowska,J., Gjerdevik,M., Lie,R.T., Gjessing,H.K.
            and Jugessur,A.
  TITLE     A genome-wide scan of cleft lip triads identifies parent-of-origin
            interaction effects between ANK3 and maternal smoking, and between
            ARHGEF10 and alcohol consumption
  JOURNAL   F1000Res 8, 960 (2019)
   PUBMED   31372216
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1373)
  AUTHORS   Matsushita,T., Ashikawa,K., Yonemoto,K., Hirakawa,Y., Hata,J.,
            Amitani,H., Doi,Y., Ninomiya,T., Kitazono,T., Ibayashi,S., Iida,M.,
            Nakamura,Y., Kiyohara,Y. and Kubo,M.
  TITLE     Functional SNP of ARHGEF10 confers risk of atherothrombotic stroke
  JOURNAL   Hum Mol Genet 19 (6), 1137-1146 (2010)
   PUBMED   20042462
REFERENCE   3  (residues 1 to 1373)
  AUTHORS   Aoki,T., Ueda,S., Kataoka,T. and Satoh,T.
  TITLE     Regulation of mitotic spindle formation by the RhoA guanine
            nucleotide exchange factor ARHGEF10
  JOURNAL   BMC Cell Biol 10, 56 (2009)
   PUBMED   19635168
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1373)
  AUTHORS   Mohl,M., Winkler,S., Wieland,T. and Lutz,S.
  TITLE     Gef10--the third member of a Rho-specific guanine nucleotide
            exchange factor subfamily with unusual protein architecture
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 373 (5), 333-341 (2006)
   PUBMED   16896804
REFERENCE   5  (residues 1 to 1373)
  AUTHORS   Verhoeven,K., De Jonghe,P., Van de Putte,T., Nelis,E., Zwijsen,A.,
            Verpoorten,N., De Vriendt,E., Jacobs,A., Van Gerwen,V., Francis,A.,
            Ceuterick,C., Huylebroeck,D. and Timmerman,V.
  TITLE     Slowed conduction and thin myelination of peripheral nerves
            associated with mutant rho Guanine-nucleotide exchange factor 10
  JOURNAL   Am J Hum Genet 73 (4), 926-932 (2003)
   PUBMED   14508709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Jan 9, 2024 this sequence version replaced XP_002728482.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1373
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..1373
                     /product="rho guanine nucleotide exchange factor 10"
                     /note="Rho guanine nucleotide exchange factor (GEF) 10"
                     /calculated_mol_wt=150703
     Region          <2..>114
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          429..613
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(435,439,537,564..565,568..569,571..572,575..576,
                     579..580,583,609,613)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          636..785
                     /region_name="PH_19"
                     /note="PH domain; pfam19057"
                     /db_xref="CDD:465965"
     Region          893..1371
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     CDS             1..1373
                     /gene="Arhgef10"
                     /gene_synonym="RGD1565043"
                     /coded_by="NM_001427033.1:180..4301"
                     /db_xref="GeneID:306618"
                     /db_xref="RGD:1565043"
ORIGIN      
        1 mdqgeasppv paehevkcdt snneeegelf dfesgdevpe adrqaptadd gtgvaeadga
       61 dentspdgtg vaeadgaden tspdgtrvde adgadentsp agngtgaesv peaepeklvv
      121 pikvnpysvi ditpfqedqp pspdanpeee gvglrvpsgy cvpvpcgyav psnlplllpt
      181 yssqiiiraq sveeevaaev agdgqcnsls sedlphsgdq gsqegsalar waadpantaw
      241 menpeeaiyd dvprensdse pdemiyddve nggeggnssl eygwsssefe syeepsdseg
      301 kngiprsflr snhkkqlshd ltrfkahcee kmrglvastv gameaqqrqe wkmqrlmkaa
      361 kegtrdglek tkaavkrgrs firtkslvsq dhryyfeeeq nlfidvdckh peavltpmpe
      421 glsqqqvvrr yilgsivese knyvdalrri leqyekplse meprllsdrk lrmvfyrike
      481 ilqchsmfqi alasrvsewd avetigdvfv asfsksmvld ayseyvnnfs tavavlkktc
      541 atkpaflefl klsqdsspdr vtlhslmmrp iqrfpqfill lqdmlkntak ghpdrlplqm
      601 alteletlae klnerkrdad qrceikqiak ainerylnkl lssgnrylvr sddvietvyn
      661 drgeivktkq rrifmlndvl mcatassrns heshammnqr yllkwsvplg qvdvieysgs
      721 sgtgdhsrhh tahspeslav vanvkphkvy mgpgqlyqdl qnllhdlnvv gqisqlignl
      781 rgsyqnlnqs vahdwtsglq qlilrkedai raadrcriql qlpgkqdksg rptfftavfn
      841 tftpaikesw vsslqmakla leeenhmgwf cvdddgslak kethpllvgh tsvmvakqpe
      901 fkiecaaynp epypsndnqp aspstargfl wigscsnqmg qvaivsfqsa npkviecfnv
      961 esrilcmiyi paeeskpqep adtkdpeata sraphvptic lgteegsisi ykssqgckkv
     1021 rlqhfytpdk stvmslacsp hglyaglvng svasytkapd gswnsepqqv iklgvlpvrs
     1081 lllvegalwa asggqvfmas vethtvenql eahqdegmvi shmavagvgi wiaftsgstl
     1141 rlfhtetlkh lqdvnidapv hsmlpghqrl svtsllvchg llmvgtslgv vvalpvprlq
     1201 gipkvtgrgm vsyhahngpv kfivtatafq nkdrardrpr ssselqdedp kdllcgeegt
     1261 sclgqtdtst avwlgdslgl taqndlssss gslshgsssl ehrsvdsslc dllrdpsafp
     1321 rsraqssrra rassalvvcg gqghrrvhrk arqpsqedlv ssvmvwqipl lgm
//
LOCUS       NP_001075948             153 aa            linear   ROD 11-MAR-2025
DEFINITION  insulin-like growth factor 1 isoform d preproprotein [Rattus
            norvegicus].
ACCESSION   NP_001075948
VERSION     NP_001075948.1
DBSOURCE    REFSEQ: accession NM_001082479.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Xiong,J., Wang,Y., Wang,H., Luo,J., Chen,T., Sun,J., Xi,Q. and
            Zhang,Y.
  TITLE     GHRH-stimulated pituitary small extracellular vesicles inhibit
            hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p
  JOURNAL   J Nanobiotechnology 22 (1), 649 (2024)
   PUBMED   39438882
  REMARK    GeneRIF: GHRH-stimulated pituitary small extracellular vesicles
            inhibit hepatocyte proliferation and IGF-1 expression by its cargo
            miR-375-3p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Maleki,A.H., Azar,J.T., Razi,M. and Tofighi,A.
  TITLE     The Effect of Different Exercise Modalities on Sertoli-germ Cells
            Metabolic Interactions in High-fat Diet-induced Obesity Rat Models:
            Implication on Glucose and Lactate Transport, Igf1, and
            Igf1R-dependent Pathways
  JOURNAL   Reprod Sci 31 (8), 2246-2260 (2024)
   PUBMED   38632221
  REMARK    GeneRIF: The Effect of Different Exercise Modalities on
            Sertoli-germ Cells Metabolic Interactions in High-fat Diet-induced
            Obesity Rat Models: Implication on Glucose and Lactate Transport,
            Igf1, and Igf1R-dependent Pathways.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Banjac,K., Obradovic,M., Zafirovic,S., Essack,M., Gluvic,Z.,
            Sunderic,M., Nedic,O. and Isenovic,E.R.
  TITLE     The involvement of Akt, mTOR, and S6K in the in vivo effect of
            IGF-1 on the regulation of rat cardiac Na+/K+-ATPase
  JOURNAL   Mol Biol Rep 51 (1), 517 (2024)
   PUBMED   38622478
  REMARK    GeneRIF: The involvement of Akt, mTOR, and S6K in the in vivo
            effect of IGF-1 on the regulation of rat cardiac Na[+]/K[+]-ATPase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Barik,P., Kuo,W.W., Kuo,C.H., Hsieh,D.J., Day,C.H., Daddam,J.,
            Chen,M.Y., Padma,V.V., Shibu,M.A. and Huang,C.Y.
  TITLE     Rewiring of IGF1 secretion and enhanced IGF1R signaling induced by
            co-chaperone carboxyl-terminus of Hsp70 interacting protein in
            adipose-derived stem cells provide augmented cardioprotection in
            aging-hypertensive rats
  JOURNAL   Aging (Albany NY) 15 (23), 14019-14038 (2023)
   PUBMED   38085649
  REMARK    GeneRIF: Rewiring of IGF1 secretion and enhanced IGF1R signaling
            induced by co-chaperone carboxyl-terminus of Hsp70 interacting
            protein in adipose-derived stem cells provide augmented
            cardioprotection in aging-hypertensive rats.
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Zhao,H., Wang,L., Yan,Y., Zhao,Q.H., He,J., Jiang,R., Luo,C.J.,
            Qiu,H.L., Miao,Y.Q., Gong,S.G., Yuan,P. and Wu,W.H.
  TITLE     Identification of the shared gene signatures between pulmonary
            fibrosis and pulmonary hypertension using bioinformatics analysis
  JOURNAL   Front Immunol 14, 1197752 (2023)
   PUBMED   37731513
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Nanto-Salonen,K. and Rosenfeld,R.G.
  TITLE     Insulin-like growth factor binding protein expression in the
            hypothyroid rat is age dependent
  JOURNAL   Endocrinology 131 (3), 1489-1496 (1992)
   PUBMED   1380443
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Hall,L.J., Kajimoto,Y., Bichell,D., Kim,S.W., James,P.L.,
            Counts,D., Nixon,L.J., Tobin,G. and Rotwein,P.
  TITLE     Functional analysis of the rat insulin-like growth factor I gene
            and identification of an IGF-I gene promoter
  JOURNAL   DNA Cell Biol 11 (4), 301-313 (1992)
   PUBMED   1605853
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Bouillon,R.
  TITLE     Diabetic bone disease. Low turnover osteoporosis related to
            decreased IGF-I production
  JOURNAL   Verh K Acad Geneeskd Belg 54 (4), 365-91 (1992)
   PUBMED   1466160
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Nanto-Salonen,K., Glasscock,G.F. and Rosenfeld,R.G.
  TITLE     The effects of thyroid hormone on insulin-like growth factor (IGF)
            and IGF-binding protein (IGFBP) expression in the neonatal rat:
            prolonged high expression of IGFBP-2 in methimazole-induced
            congenital hypothyroidism
  JOURNAL   Endocrinology 129 (5), 2563-2570 (1991)
   PUBMED   1718729
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Kato,H., Okoshi,A., Miura,Y. and Noguchi,T.
  TITLE     A new cDNA clone relating to larger molecular species of rat
            insulin-like growth factor-I mRNA
  JOURNAL   Agric Biol Chem 54 (6), 1599-1601 (1990)
   PUBMED   1368571
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB751206.1, BC086374.1 and CB761687.1.
            
            Transcript Variant: This variant (4) lacks an alternate
            frame-shifting exon in the 3' coding region, compared to variant 3,
            resulting in a protein (isoform d) with a novel C-terminus,
            compared to isoform c. This isoform is also known as IA.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M17335.1, CF108511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..153
                     /product="insulin-like growth factor 1 isoform d
                     preproprotein"
                     /note="somatomedin; IGF-I; Insulin-like growth factor I"
                     /calculated_mol_wt=11760
     sig_peptide     1..48
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5338
     proprotein      49..153
                     /product="insulin-like growth factor 1 isoform d
                     proprotein"
                     /calculated_mol_wt=11760
     mat_peptide     49..118
                     /product="insulin-like growth factor 1 isoform d"
                     /calculated_mol_wt=7693
     Region          49..116
                     /region_name="IlGF"
                     /note="insulin_like growth factors; specific to
                     vertebrates. Members include a number of peptides
                     including insulin-like growth factors I and II, which play
                     a variety of roles in controlling processes such as
                     growth, differentiation, and reproduction. On a...;
                     cd04368"
                     /db_xref="CDD:239834"
     Region          49..77
                     /region_name="B"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Site            order(51,60,68..72)
                     /site_type="active"
                     /note="IGFBP binding surface [active]"
                     /db_xref="CDD:239834"
     Site            order(69,71..72,92)
                     /site_type="active"
                     /note="type 1 IGF- and insulin-receptor binding surface
                     [active]"
                     /db_xref="CDD:239834"
     Region          78..89
                     /region_name="C"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Region          90..110
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Site            order(97..99,103..104)
                     /site_type="active"
                     /note="type 2 IGF-receptor binding surface [active]"
                     /db_xref="CDD:239834"
     Region          111..118
                     /region_name="D"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     Region          119..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08025.3)"
     CDS             1..153
                     /gene="Igf1"
                     /gene_synonym="IGF"
                     /coded_by="NM_001082479.1:281..742"
                     /note="isoform d preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:24482"
                     /db_xref="RGD:2868"
ORIGIN      
        1 mgkisslptq lfkiclcdfl kikihimsss hlfylalcll tftssatagp etlcgaelvd
       61 alqfvcgprg fyfnkptgyg ssirrapqtg ivdeccfrsc dlrrlemyca plkptksars
      121 iraqrhtdmp ktqkevhlkn tsrgsagnkt yrm
//
LOCUS       NP_446116                919 aa            linear   ROD 11-MAR-2025
DEFINITION  sarcosine dehydrogenase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_446116
VERSION     NP_446116.2
DBSOURCE    REFSEQ: accession NM_053664.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Tibbetts,A.S. and Appling,D.R.
  TITLE     Compartmentalization of Mammalian folate-mediated one-carbon
            metabolism
  JOURNAL   Annu Rev Nutr 30, 57-81 (2010)
   PUBMED   20645850
  REMARK    Review article
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Bergeron,F., Otto,A., Blache,P., Day,R., Denoroy,L., Brandsch,R.
            and Bataille,D.
  TITLE     Molecular cloning and tissue distribution of rat sarcosine
            dehydrogenase
  JOURNAL   Eur J Biochem 257 (3), 556-561 (1998)
   PUBMED   9839943
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Porter,D.H., Cook,R.J. and Wagner,C.
  TITLE     Enzymatic properties of dimethylglycine dehydrogenase and sarcosine
            dehydrogenase from rat liver
  JOURNAL   Arch Biochem Biophys 243 (2), 396-407 (1985)
   PUBMED   2417560
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Cook,R.J., Misono,K.S. and Wagner,C.
  TITLE     The amino acid sequences of the flavin-peptides of dimethylglycine
            dehydrogenase and sarcosine dehydrogenase from rat liver
            mitochondria
  JOURNAL   J Biol Chem 260 (24), 12998-13002 (1985)
   PUBMED   4055729
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Wittwer,A.J. and Wagner,C.
  TITLE     Identification of the folate-binding proteins of rat liver
            mitochondria as dimethylglycine dehydrogenase and sarcosine
            dehydrogenase. Flavoprotein nature and enzymatic properties of the
            purified proteins
  JOURNAL   J Biol Chem 256 (8), 4109-4115 (1981)
   PUBMED   6163778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jun 29, 2023 this sequence version replaced NP_446116.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF067650.2, SRR26643286.9635.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..919
                     /product="sarcosine dehydrogenase, mitochondrial"
                     /EC_number="1.5.8.3"
                     /calculated_mol_wt=99060
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=2373
     mat_peptide     23..919
                     /product="Sarcosine dehydrogenase, mitochondrial.
                     /id=PRO_0000010772"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64380.2)"
                     /calculated_mol_wt=99060
     Region          67..445
                     /region_name="DadA"
                     /note="Glycine/D-amino acid oxidase (deaminating) [Amino
                     acid transport and metabolism]; COG0665"
                     /db_xref="CDD:440429"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Region          431..486
                     /region_name="FAO_M"
                     /note="FAD dependent oxidoreductase central domain;
                     pfam16350"
                     /db_xref="CDD:465100"
     Region          481..917
                     /region_name="GcvT"
                     /note="Glycine cleavage system protein T
                     (aminomethyltransferase) [Amino acid transport and
                     metabolism]; COG0404"
                     /db_xref="CDD:440173"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL12; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            803
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            885
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     Site            905
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LB7; propagated from
                     UniProtKB/Swiss-Prot (Q64380.2)"
     CDS             1..919
                     /gene="Sardh"
                     /coded_by="NM_053664.3:155..2914"
                     /db_xref="GeneID:114123"
                     /db_xref="RGD:621125"
ORIGIN      
        1 maslsrvlrv aatcprgrsa rnlglqplar earptteksv pyqctlkeea qgasvvpqgp
       61 sqplpstanv vvigggslgc qtlyhlaklg vggvvllere rltsgttwht agllwqlrps
      121 dvevellaht rqvvshdlee etglhtgwiq ngglfiasnq qrldeykrlm slgkaygies
      181 hvlspaetkd lyplmnvddl ygtlyvprdg tmdpagtctt ltraavarga qviencavtg
      241 irvrtddfgv rrvtavetqh gsiqtpcvvn cagvwassvg rmagvkvplv amhhayvvte
      301 riegiqnmpn vrdhdasvyl rlqgdalsvg gyeanpifwd evsdkfafgl fdldwdvftq
      361 hiegainrvp vlektgikst vcgpesftpd hkplmgeape lrgfflgcgf nsagmmlggg
      421 cgqelahwiv hgrpekdmys ydirrfhhsl tdhprwirer shesyaknys vvfphdepla
      481 grnmrrdplh eellgqgcvf qerqgwerpg wfnpqetaqv ldydyygayg hqahkdyays
      541 rllgdeytfd fpphhcviqk eclacrtaaa vfnmsyfgkf yllgadarka adwlfsadvn
      601 rppgstvytc mlnqrggtes dltvsclapg aqasplapaf egdgyylavg gavaqhnwsh
      661 intvlqdqef rcqlmdcsed lgmlsiqgpa srdilqdvld adlsneafpf sthqlvraag
      721 hlvrairlsf vgelgwelhv pqasclpvyr avmaagakhg lvnagyraid slsiekgyrh
      781 whadlrsdds pleaglaftc klktsvpflg realekqrat glrrrlvclt veeevpmfgl
      841 eaiwrngqvv ghvrradfgf tvnktiaygy irdpsggpvs ldfvkngdya lermgvtyaa
      901 qvhlkspfdp dnkrvkgiy
//
LOCUS       NP_071602                347 aa            linear   ROD 11-MAR-2025
DEFINITION  CCN family member 2 precursor [Rattus norvegicus].
ACCESSION   NP_071602
VERSION     NP_071602.1
DBSOURCE    REFSEQ: accession NM_022266.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Yang,Y., Long,J., Yang,J., Zheng,H., Lai,Y., Chen,C., Tang,F.,
            Gao,Y., Chen,L. and He,Z.
  TITLE     METTL3-dependent m6A modification mediates bladder remodeling after
            partial bladder outlet obstruction through CCN2 activation
  JOURNAL   Neurourol Urodyn 42 (7), 1506-1521 (2023)
   PUBMED   37455557
  REMARK    GeneRIF: METTL3-dependent m6A modification mediates bladder
            remodeling after partial bladder outlet obstruction through CCN2
            activation.
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Song,X., Cui,Y. and Zhu,T.
  TITLE     MicroRNA-19 upregulation attenuates cardiac fibrosis via targeting
            connective tissue growth factor
  JOURNAL   Am J Med Sci 365 (4), 375-385 (2023)
   PUBMED   36539014
  REMARK    GeneRIF: MicroRNA-19 upregulation attenuates cardiac fibrosis via
            targeting connective tissue growth factor.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Pi,L., Sun,C., Jn-Simon,N., Basha,S., Thomas,H., Figueroa,V.,
            Zarrinpar,A., Cao,Q. and Petersen,B.
  TITLE     CCN2/CTGF promotes liver fibrosis through crosstalk with the
            Slit2/Robo signaling
  JOURNAL   J Cell Commun Signal 17 (1), 137-150 (2023)
   PUBMED   36469291
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Yanagihara,T., Tsubouchi,K., Gholiof,M., Chong,S.G., Lipson,K.E.,
            Zhou,Q., Scallan,C., Upagupta,C., Tikkanen,J., Keshavjee,S., Ask,K.
            and Kolb,M.R.J.
  TITLE     Connective-Tissue Growth Factor Contributes to TGF-beta1-induced
            Lung Fibrosis
  JOURNAL   Am J Respir Cell Mol Biol 66 (3), 260-270 (2022)
   PUBMED   34797990
  REMARK    GeneRIF: Connective-Tissue Growth Factor Contributes to
            TGF-beta1-induced Lung Fibrosis.
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Zhang,S., Wang,N., Ma,Q., Fan,F. and Ma,X.
  TITLE     LncRNA TUG1 acts as a competing endogenous RNA to mediate CTGF
            expression by sponging miR-133b in myocardial fibrosis after
            myocardial infarction
  JOURNAL   Cell Biol Int 45 (12), 2534-2543 (2021)
   PUBMED   34553456
  REMARK    GeneRIF: LncRNA TUG1 acts as a competing endogenous RNA to mediate
            CTGF expression by sponging miR-133b in myocardial fibrosis after
            myocardial infarction.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Babic,A.M., Chen,C.C. and Lau,L.F.
  TITLE     Fisp12/mouse connective tissue growth factor mediates endothelial
            cell adhesion and migration through integrin alphavbeta3, promotes
            endothelial cell survival, and induces angiogenesis in vivo
  JOURNAL   Mol Cell Biol 19 (4), 2958-2966 (1999)
   PUBMED   10082563
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Murphy,M., Godson,C., Cannon,S., Kato,S., Mackenzie,H.S., Martin,F.
            and Brady,H.R.
  TITLE     Suppression subtractive hybridization identifies high glucose
            levels as a stimulus for expression of connective tissue growth
            factor and other genes in human mesangial cells
  JOURNAL   J Biol Chem 274 (9), 5830-5834 (1999)
   PUBMED   10026205
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Perbal,B., Martinerie,C., Sainson,R., Werner,M., He,B. and
            Roizman,B.
  TITLE     The C-terminal domain of the regulatory protein NOVH is sufficient
            to promote interaction with fibulin 1C: a clue for a role of NOVH
            in cell-adhesion signaling
  JOURNAL   Proc Natl Acad Sci U S A 96 (3), 869-874 (1999)
   PUBMED   9927660
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Kireeva,M.L., Latinkic,B.V., Kolesnikova,T.V., Chen,C.C.,
            Yang,G.P., Abler,A.S. and Lau,L.F.
  TITLE     Cyr61 and Fisp12 are both ECM-associated signaling molecules:
            activities, metabolism, and localization during development
  JOURNAL   Exp Cell Res 233 (1), 63-77 (1997)
   PUBMED   9184077
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Ryseck,R.P., Macdonald-Bravo,H., Mattei,M.G. and Bravo,R.
  TITLE     Structure, mapping, and expression of fisp-12, a growth
            factor-inducible gene encoding a secreted cysteine-rich protein
  JOURNAL   Cell Growth Differ 2 (5), 225-233 (1991)
   PUBMED   1888698
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF120275.1 and AB023068.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF120275.1, AB023068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093042, SAMN16093043
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..347
                     /product="CCN family member 2 precursor"
                     /note="connective tissue growth-related protein; CCN
                     family member 2; connective tissue growth factor"
                     /calculated_mol_wt=35420
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2354
     mat_peptide     25..347
                     /product="CCN family member 2. /id=PRO_0000014405"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1E9.1)"
                     /calculated_mol_wt=35420
     Region          <39..80
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     pfam00219"
                     /db_xref="CDD:459717"
     Region          101..160
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          197..240
                     /region_name="TSP1_CCN"
                     /note="CCN3 Nov like TSP1 domain; pfam19035"
                     /db_xref="CDD:465952"
     Region          245..347
                     /region_name="Heparin-binding.
                     /evidence=ECO:0000250|UniProtKB:P29279"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1E9.1)"
     Region          251..343
                     /region_name="GHB_like"
                     /note="Glycoprotein hormone beta chain homologues;
                     cl21545"
                     /db_xref="CDD:473907"
     CDS             1..347
                     /gene="Ccn2"
                     /gene_synonym="Ctgf; CTGRP"
                     /coded_by="NM_022266.2:225..1268"
                     /db_xref="GeneID:64032"
                     /db_xref="RGD:621392"
ORIGIN      
        1 mlasvagpvs lalvlllctr patgqdcsaq cqcaaeaapr cpagvslvld gcgccrvcak
       61 qlgelcterd pcdphkglfc dfgspanrki gvctakdgap cvfggsvyrs gesfqsscky
      121 qctcldgavg cvplcsmdvr lpspdcpfpr rvklpgkcce ewvcdepkdr tvvgpalaay
      181 rledtfgpdp tmmranclvq ttewsacskt cgmgistrvt ndntfcrlek qsrlcmvrpc
      241 eadleenikk gkkcirtpki akpvkfelsg ctsvktyrak fcgvctdgrc ctphrtttlp
      301 vefkcpdgei mkknmmfikt cachyncpgd ndifeslyyr kmygdma
//
LOCUS       NP_001123962            4545 aa            linear   ROD 11-MAR-2025
DEFINITION  prolow-density lipoprotein receptor-related protein 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001123962
VERSION     NP_001123962.1
DBSOURCE    REFSEQ: accession NM_001130490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 4545)
  AUTHORS   Wang,H., Liang,L., Yang,C., Xiao,L., Wang,H., Wang,G. and Zhu,Z.
  TITLE     The protective role of hippocampal LRP1 knockdown involves synaptic
            plasticity through the promoting microtubule dynamics and
            activation of Akt/GSK-3beta pathway in depressive rats
  JOURNAL   J Affect Disord 322, 63-75 (2023)
   PUBMED   36372121
  REMARK    GeneRIF: The protective role of hippocampal LRP1 knockdown involves
            synaptic plasticity through the promoting microtubule dynamics and
            activation of Akt/GSK-3beta pathway in depressive rats.
REFERENCE   2  (residues 1 to 4545)
  AUTHORS   Haghjoo,S., Hedayati Ch,M., Rostampour,M. and Khakpour-Taleghani,B.
  TITLE     Red-light radiation: does it enhance memory by increasing
            hippocampal LRP-1 and TRPA-1 genes expression?
  JOURNAL   Int J Radiat Biol 99 (2), 329-339 (2023)
   PUBMED   35446172
  REMARK    GeneRIF: Red-light radiation: does it enhance memory by increasing
            hippocampal LRP-1 and TRPA-1 genes expression?
REFERENCE   3  (residues 1 to 4545)
  AUTHORS   Taghadosi,Z., Zarifkar,A., Razban,V. and Aligholi,H.
  TITLE     The effect of chronic stress and its preconditioning on spatial
            memory as well as hippocampal LRP1 and RAGE expression in a
            streptozotocin-induced rat model of Alzheimer's disease
  JOURNAL   Metab Brain Dis 37 (8), 2699-2710 (2022)
   PUBMED   35930096
  REMARK    GeneRIF: The effect of chronic stress and its preconditioning on
            spatial memory as well as hippocampal LRP1 and RAGE expression in a
            streptozotocin-induced rat model of Alzheimer's disease.
REFERENCE   4  (residues 1 to 4545)
  AUTHORS   Garcia,J., Chang,R., Steinberg,R.A., Arce,A., Yang,J., Van Der
            Eb,P., Abdullah,T., Chandrashekar,D.V., Eck,S.M., Meza,P.,
            Liu,Z.X., Cadenas,E., Cribbs,D.H., Kaplowitz,N., Sumbria,R.K. and
            Han,D.
  TITLE     Modulation of hepatic amyloid precursor protein and lipoprotein
            receptor-related protein 1 by chronic alcohol intake: Potential
            link between liver steatosis and amyloid-beta
  JOURNAL   Front Physiol 13, 930402 (2022)
   PUBMED   36187787
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 4545)
  AUTHORS   Mantuano,E., Azmoon,P., Banki,M.A., Lam,M.S., Sigurdson,C.J. and
            Gonias,S.L.
  TITLE     A soluble derivative of PrPC activates cell-signaling and regulates
            cell physiology through LRP1 and the NMDA receptor
  JOURNAL   J Biol Chem 295 (41), 14178-14188 (2020)
   PUBMED   32788217
  REMARK    GeneRIF: A soluble derivative of PrP(C) activates cell-signaling
            and regulates cell physiology through LRP1 and the NMDA receptor.
REFERENCE   6  (residues 1 to 4545)
  AUTHORS   Brown,M.D., Banker,G.A., Hussaini,I.M., Gonias,S.L. and
            VandenBerg,S.R.
  TITLE     Low density lipoprotein receptor-related protein is expressed early
            and becomes restricted to a somatodendritic domain during neuronal
            differentiation in culture
  JOURNAL   Brain Res 747 (2), 313-317 (1997)
   PUBMED   9046007
REFERENCE   7  (residues 1 to 4545)
  AUTHORS   Ishii,M., Osada,T., Gliemann,J. and Ikai,A.
  TITLE     Neurite-promoting effect of alpha 2-macroglobulin in rat cerebral
            cortex is mainly associated with alpha 2-macroglobulin receptor
  JOURNAL   Brain Res 737 (1-2), 269-274 (1996)
   PUBMED   8930375
REFERENCE   8  (residues 1 to 4545)
  AUTHORS   Stefansson,S., Lawrence,D.A. and Argraves,W.S.
  TITLE     Plasminogen activator inhibitor-1 and vitronectin promote the
            cellular clearance of thrombin by low density lipoprotein
            receptor-related proteins 1 and 2
  JOURNAL   J Biol Chem 271 (14), 8215-8220 (1996)
   PUBMED   8626514
REFERENCE   9  (residues 1 to 4545)
  AUTHORS   Beisiegel,U., Weber,W., Ihrke,G., Herz,J. and Stanley,K.K.
  TITLE     The LDL-receptor-related protein, LRP, is an apolipoprotein
            E-binding protein
  JOURNAL   Nature 341 (6238), 162-164 (1989)
   PUBMED   2779654
REFERENCE   10 (residues 1 to 4545)
  AUTHORS   Herz,J., Hamann,U., Rogne,S., Myklebost,O., Gausepohl,H. and
            Stanley,K.K.
  TITLE     Surface location and high affinity for calcium of a 500-kd liver
            membrane protein closely related to the LDL-receptor suggest a
            physiological role as lipoprotein receptor
  JOURNAL   EMBO J 7 (13), 4119-4127 (1988)
   PUBMED   3266596
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473950.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760494
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4545
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..4545
                     /product="prolow-density lipoprotein receptor-related
                     protein 1 precursor"
                     /note="prolow-density lipoprotein receptor-related protein
                     1; low density lipoprotein-related protein 1
                     (alpha-2-macroglobulin receptor); low density lipoprotein
                     receptor-related protein 1"
                     /calculated_mol_wt=502965
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1946
     mat_peptide     20..4545
                     /product="Prolow-density lipoprotein receptor-related
                     protein 1. /evidence=ECO:0000255. /id=PRO_5015091774"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
                     /calculated_mol_wt=502965
     Region          27..60
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(33,42,53..54)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(46,49,53,59..60)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            56..60
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          72..105
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(78,87,98..99)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(91,94,98,104..105)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            101..105
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          120..149
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            137
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          159..189
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          276..315
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          293..335
                     /region_name="LDL-receptor class B 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          317..359
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          336..379
                     /region_name="LDL-receptor class B 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          362..402
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          380..423
                     /region_name="LDL-receptor class B 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            447
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          487..520
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          552..594
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          572..614
                     /region_name="LDL-receptor class B 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          595..634
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          615..660
                     /region_name="LDL-receptor class B 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          639..671
                     /region_name="HAT 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          641..690
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          661..711
                     /region_name="LDL-receptor class B 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          <701..734
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          712..755
                     /region_name="LDL-receptor class B 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            730
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          808..843
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          854..886
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(860,868,879..880)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(872,875,879,885..886)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            882..886
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          896..929
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(901,909,920..921)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(913,916,920,926..927)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            923..927
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            929
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          936..968
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(942,950,961..962)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(954,957,961,967..968)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            964..968
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          979..1012
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(983,991,1002..1003)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(995,998,1002,1008..1009)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1005..1009
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1016..1049
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1021,1029,1040..1041)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1033,1036,1040,1046..1047)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1043..1047
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1051
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1063..1098
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1068,1077,1088..1089)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1081,1084,1088,1094..1095)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1091..1095
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1105..1141
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1111,1120,1131..1132)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1124,1127,1131,1137..1138)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1134..1138
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1146..1179
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1151,1161,1172..1173)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            1156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            order(1165,1168,1172,1178..1179)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1175..1179
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1186..1222
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            1196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1310..1356
                     /region_name="LDL-receptor class B 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1311..>1504
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
     Region          1337..1377
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1357..1399
                     /region_name="LDL-receptor class B 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1380..1413
                     /region_name="HAT 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1381..1424
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1400..1446
                     /region_name="LDL-receptor class B 10.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1447..1491
                     /region_name="LDL-receptor class B 11.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1470..1503
                     /region_name="HAT 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1492..1532
                     /region_name="LDL-receptor class B 12.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1512
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1559
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1614..1650
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            1617
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1628..1670
                     /region_name="LDL-receptor class B 13.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1646
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1651..1694
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1653..1684
                     /region_name="HAT 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1671..1714
                     /region_name="LDL-receptor class B 14.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1698..1735
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1715..1754
                     /region_name="LDL-receptor class B 15.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1724
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1734
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1735..1776
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1755..1799
                     /region_name="LDL-receptor class B 16.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1826
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1851..1887
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1917..1957
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            1934
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1935..1977
                     /region_name="LDL-receptor class B 17.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          1960..2000
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1978..2020
                     /region_name="LDL-receptor class B 18.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            1996
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2001..2044
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            2010
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZX7; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2021..2064
                     /region_name="LDL-receptor class B 19.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2046..2088
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            2049
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2065..2108
                     /region_name="LDL-receptor class B 20.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            2118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            2128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2160..2195
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          2254..2295
                     /region_name="LDL-receptor class B 21.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2276..2316
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          2277..2309
                     /region_name="HAT 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2296..2344
                     /region_name="LDL-receptor class B 22.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2325..2358
                     /region_name="HAT 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2345..2389
                     /region_name="LDL-receptor class B 23.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2345..2387
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          2371..2412
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          2390..2432
                     /region_name="LDL-receptor class B 24.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2411..2444
                     /region_name="HAT 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2433..2474
                     /region_name="LDL-receptor class B 25.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            2473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2483..2515
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            2503
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            2522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2528..2558
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2531,2539,2550..2551)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2543,2546,2550,2556..2557)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2553..2557
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2567..2601
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2572,2580,2591..2592)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2584,2587,2591,2597..2598)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2594..2598
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            2602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2606..2640
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2611,2619,2630..2631)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            2621
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            order(2623,2626,2630,2636..2637)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2633..2637
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            2639
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          <2667..2689
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2672,2675,2679,2685..2686)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2682..2686
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2697..2731
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2702,2710,2721..2722)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2714,2717,2721,2727..2728)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2724..2728
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2735..2766
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(2740,2748,2759..2760)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2752,2755,2759,2765..2766)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2762..2766
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2774..2807
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(2780,2789,2800..2801)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2793,2796,2800,2806..2807)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2803..2807
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            2816
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2818..2850
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(2824,2832,2843..2844)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2836,2839,2843,2849..2850)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2846..2850
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2858..2891
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(2864,2872,2884..2885)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2877,2880,2884,2890..2891)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2887..2891
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            2906
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          2908..2940
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2911,2919,2930..2931)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2923,2926,2930,2936..2937)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2933..2937
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2965..2986
                     /region_name="cEGF"
                     /note="Complement Clr-like EGF-like; pfam12662"
                     /db_xref="CDD:463661"
     Region          2983..>3012
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(2983,2986,2999)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            3049
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3050..3094
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3070..3114
                     /region_name="LDL-receptor class B 26.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            3090
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3095..3137
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3115..3157
                     /region_name="LDL-receptor class B 27.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3128..3171
                     /region_name="HAT 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3139..3181
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3158..3201
                     /region_name="LDL-receptor class B 28.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3183..3224
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3202..3244
                     /region_name="LDL-receptor class B 29.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3224..3256
                     /region_name="HAT 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3225..3265
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3245..3285
                     /region_name="LDL-receptor class B 30.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            3265
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3295..3331
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            3334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3335..3366
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3340,3348,3359..3360)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3352,3355,3359,3365..3366)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3362..3366
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3375..3409
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3380,3388,3399..3400)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3392,3395,3399,3405..3406)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3402..3406
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3414..3449
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3419,3428,3439..3440)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3432,3435,3439,3445..3446)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3442..3446
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3453..3486
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(3459,3468,3479..3480)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3472,3475,3479,3485..3486)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3482..3486
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            3489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3494..3527
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(3500,3509,3520..3521)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3513,3516,3520,3526..3527)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3523..3527
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3537..3571
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3542,3550,3561..3562)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3554,3557,3561,3567..3568)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3564..3568
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3576..3610
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3581,3589,3600..3601)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3593,3596,3600,3606..3607)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3603..3607
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3614..3648
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3619,3627,3638..3639)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3631,3634,3638,3644..3645)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3641..3645
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3654..3686
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(3660,3668,3679..3680)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            3663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            order(3672,3675,3679,3685..3686)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3682..3686
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3696..3732
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3702,3711,3722..3723)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3715,3718,3722,3728..3729)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3725..3729
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          3747..3777
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(3748,3756,3767..3768)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(3760,3763,3767,3773..3774)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            3770..3774
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            3789
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            3840
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3863..4065
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          3913..3925
                     /region_name="LDL-receptor class B 31.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            3954
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3956..3993
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          3971..4013
                     /region_name="LDL-receptor class B 32.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          3995..4027
                     /region_name="HAT 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          4014..4057
                     /region_name="LDL-receptor class B 33.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          4014..4055
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          4038..4079
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          4058..4102
                     /region_name="LDL-receptor class B 34.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00461"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4076
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4425..4445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Region          4446..4545
                     /region_name="Interaction with MAFB.
                     /evidence=ECO:0000250|UniProtKB:Q91ZX7"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4461
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07954; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4508
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07954; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07954; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07954; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     Site            4524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZX7; propagated from
                     UniProtKB/Swiss-Prot (G3V928.1)"
     CDS             1..4545
                     /gene="Lrp1"
                     /gene_synonym="LRP-1"
                     /coded_by="NM_001130490.1:346..13983"
                     /db_xref="GeneID:299858"
                     /db_xref="RGD:1307535"
ORIGIN      
        1 mltpplllll pllsalvaga tmdapktcsp kqfacrdqit ciskgwrcdg erdcpdgsde
       61 apeicpqska qrcppnehsc lgtelcvpms rlcngiqdcm dgsdegahcr elrvncsrmg
      121 cqhhcvptps gptcycnnsf qlqadgktck dfdecsvygt csqlctntdg sftcgcvegy
      181 llqpdnrsck aknepvdrpp vlliansqni latylsgaqv stitptstrq ttamdfsyan
      241 etvcwvhvgd saaqtqlkca rmpslkgfvd ehtinislsl hhveqmaidw ltgnfyfvdd
      301 iddrifvcnr ngdtcvtlld lelynpkgia ldpamgkvff tdygqipkve rcdmdgqnrt
      361 klvdskivfp hgitldlvsr lvywadayld yievvdyegk grqtiiqgil iehlygltvf
      421 enylyatnsd nantqqktsv irvnrfnste yqvvtrvdkg galhiyhqrr qprvrshace
      481 ndqygkpggc sdicllansh kartcrcrsg fslgsdgksc kkpehelflv ygkgrpgiir
      541 gmdmgakvpd ehmipienlm npraldfhae tgfiyfadtt syligrqkid gteretilkd
      601 gihnvegvav dwmgdnlywt ddgpkktisv arlekaaqtr ktliegkmth praivvdpln
      661 gwmywtdwee dpkdsrrgrl erawmdgshr difvtsktvl wpnglsldip agrlywvdaf
      721 ydrietilln gtdrkivyeg pelnhafglc hhgnylfwte yrsgsvyrle rgvagaqptv
      781 tllrserppi feirmydaqq qqvgtnkcrv nnggcsslcl atpgsrqcac aedqvldadg
      841 vtclanpsyv pppqcqpgef acannrciqe rwkcdgdndc ldnsdeapal chqhtcpsdr
      901 fkcennrcip nrwlcdgdnd cgnsedesna tcsartcppn qfscasgrci piswtcdldd
      961 dcgdrsdesa scayptcfpl tqftcnngrc ininwrcdnd ndcgdnsdea gcshscsstq
     1021 fkcnsgrcip ehwtcdgdnd cgdysdetha nctnqatrpp ggchsdefqc rldglciplr
     1081 wrcdgdtdcm dssdekgceg vthvcdpnvk fgckdsarci skawvcdgds dcednsdeen
     1141 cealacrpps hpcanntsvc lspdklcdgk ddcgdgsdeg elcdqcslnn ggcshncsva
     1201 pgegivcscp lgmelgpdnh tcqiqsycak hlkcsqkcdq nkfsvkcscy egwvlepdge
     1261 scrsldpfkp fiifsnrhei rridlhkgdy svlvpglrnt ialdfhlsqs alywtdvved
     1321 kiyrgklldn galtsfevvi qyglatpegl avdwiagniy wvesnldqie vakldgtlrt
     1381 tllagdiehp raialdprdg ilfwtdwdas lprieaasms gagrrtihre tgsggwpngl
     1441 tvdylekril widarsdaiy sarydgsghm evlrghefls hpfavtlygg evywtdwrtn
     1501 tlakankwtg hnvtvvqrtn tqpfdlqvyh psrqpmapnp ceanggrgpc shlclinynr
     1561 tvscacphlm klhndnttcy efkkfllyar qmeirgvdld apyynyiisf tvpdidnvtv
     1621 ldydareqrv ywsdvrtqai krafingtgv etvvsadlpn ahglavdwvs rnlfwtsydt
     1681 nkkqinvarl dgsfknavvq gleqphglvv hplrgklywt dgdnismvnm dgsnrtllfs
     1741 gqkgpvglai dfpesklywi ssgnhtinrc nldgselevi dtmrsqlgka talaimgdkl
     1801 wwadqvsekm gtcnkadgsg svvlrnsttl vmhmkvydes iqlehegtnp csvnngdcsq
     1861 lclptsettr scmctagysl rsgqqacegv gsfllysvhe girgipldpn dksdalvpvs
     1921 gtslavgidf haendtiywv dmglstisra krdqtwredv vtngigrveg iavdwiagni
     1981 ywtdqgfdvi evarlngsfr yvvisqgldk praitvhpek gylfwtewgh ypriersrld
     2041 gtervvlvnv siswpngisv dyqggklywc darmdkieri dletgenrev vlssnnmdmf
     2101 svsvfedfiy wsdrthangs ikrgckdnat dsvplrtgig vqlkdikvfn rdrqkgtnvc
     2161 avanggcqql clyrgggqra cacahgmlae dgascreyag yllysertil ksihlsdern
     2221 lnapvqpfed pehmknvial afdyragtsp gtpnriffsd ihfgniqqin ddgsgrttiv
     2281 envgsvegla yhrgwdtlyw tsyttstitr htvdqtrpga feretvitms gddhprafvl
     2341 decqnlmfwt nwnelhpsim raalsganvl tliekdirtp nglaidhrae klyfsdatld
     2401 kierceydgs hryvilksep vhpfglavyg ehifwtdwvr ravqrankyv gsdmkllrvd
     2461 ipqqpmgiia vandtnscel spcrinnggc qdlcllthqg hvncscrggr ilqedftcra
     2521 mnsscraqde fecangecis fsltcdgvsh ckdksdekps ycnsrrckkt frqcnngrcv
     2581 snmlwcngvd dcgdgsdeip cnktacgvge frcrdgscig nssrcnqfvd cedasdemnc
     2641 satdcssyfr lgvkgvlfqp certslcyap swvcdgandc gdysderdcp gvkrprcpln
     2701 yfacpsgrci pmswtcdked dcengedeth cnkfcseaqf ecqnhrcisk qwlcdgsddc
     2761 gdgsdeaahc egktcgpssf scpgthvcvp erwlcdgdkd cadgadesis agclynstcd
     2821 drefmcqnrl cipkhfvcdh drdcadgsde speceyptcg pnefrcangr clssrqwecd
     2881 gendchdhsd eapknphcts pehkcnassq flcssgrcva eallcngqdd cgdgsdergc
     2941 hvneclsrkl sgcsqdcedl kigfkcrcrp gfrlkddgrt cadvdecstt fpcsqlcint
     3001 hgsykclcve gyaprggdph sckavtdeep flifanryyl rklnldgsny tllkqglnna
     3061 valdfdyrgq miywtdvttq gsmirrmhln gsnvqvlhrt glsnpdglav dwvggnlywc
     3121 dkgrdtievs klngayrtvl vssglrepra lvvdvqngyl ywtdwgdhsl igrigmdgsg
     3181 rsiivdtkit wpngltvdyv teriywadar edyiefasld gsnrhvvlsq diphifaltl
     3241 fedyvywtdw etksinrahk ttganktlli stlhrpmdlh vfhalrqpdv pnhpckvnng
     3301 gcsnlcllsp ggghkcacpt nfylggdgrt cvsnctasqf vckndkcipf wwkcdteddc
     3361 gdhsdeppdc pefkcrpgqf qcstgictnp aficdgdndc qdnsdeancd ihvclpsqfk
     3421 ctntnrcipg ifrcngqdnc gdgederdcp evtcapnqfq csitkrcipr vwvcdrdndc
     3481 vdgsdepanc tqmtcgvdef rckdsgrcip arwkcdgedd cgdgsdepke ecdertcepy
     3541 qfrcknnrcv pgrwqcdydn dcgdnsdees ctprpcsese fscangrcia grwkcdgdhd
     3601 cadgsdekdc tprcdmdqfq cksghciplr wrcdadadcm dgsdeeacgt gvrtcpldef
     3661 qcnntlckpl awkcdgeddc gdnsdenpee ctrfqcppnr pfrckndrvc lwigrqcdgt
     3721 dncgdgtdee dcepptaqnp hckdkkeflc rnqrclsssl rcnmfddcgd gsdeedcsid
     3781 pkltscatna smcgdearcv rtekaaycac rpgfhtvpgq pgcqdinecl rfgtcsqlcn
     3841 ntkgghlcsc arnfmkthnt ckaegseyqv lyiaddneir slfpghphsa yeqafqgdes
     3901 vridamdvhv kagrvywtnw htgtisyrsl ppaappttsn rhrrqidrgv thlnisglkm
     3961 prgiaidwva gnvywtdsgr dvievaqmkg enrktlisgm idephaivvd plrgtmywsd
     4021 wgnhpkieta amdgtlretl vqdniqwptg lavdyhnerl ywadaklsvi gsirlngtdp
     4081 ivavdskrgl shpfsidvfe dyiygvtyin nrvfkihkfg hsplinltgg lshasdvvly
     4141 hqhkqpevtn pcdrkkcewl cllspsgpvc tcpngkrldn gtcvpvpspt pppdaprpgt
     4201 ctlqcfnggs cflnarrqpk crcqprytgd kceldqcwey chnggtcaas psgmptcrcp
     4261 tgftgprctq qvcagycann stctvnqgnq pqcrclpgfl gdrcqyrqcs gfcenfgtcq
     4321 maadgsrqcr ctvyfegtrc evnkcsrclq gacvvnkqtg dvtcnctdgr vapscltcid
     4381 hcsnggsctm nskmmpecqc pphmtgprce eqvvsqqqpg hmtsilipll lllllllvag
     4441 vvfwykrrvr gakgfqhqrm tngamnveig nptykmyegg epddvgglld adfaldpdkp
     4501 tnftnpvyat lymgghgsrh slastdekre llgrgpedei gdpla
//
LOCUS       NP_001423375             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423375 XP_038936642
VERSION     NP_001423375.1
DBSOURCE    REFSEQ: accession NM_001436446.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_038936642.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.24266.1,
                                           SRR26360186.182801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436446.1:321..902"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423360             860 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423360 XP_063122315
VERSION     NP_001423360.1
DBSOURCE    REFSEQ: accession NM_001436431.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122315.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.44138.1,
                                           SRR26360181.1631764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..860
                     /product="interleukin enhancer-binding factor 3 isoform 2"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=91915
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          520..591
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(527,529..530,533,546,549..551,555,571..574)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..860
                     /gene="Ilf3"
                     /coded_by="NM_001436431.1:240..2822"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdatteqgpi ltkhgknpvm elnekrrglk
      541 yelisetggs hdkrfvmeve vdgqkfqgag snkkvakaya alaaleklfp daplaleank
      601 kkrapvpvrg gpkfaakphn pgfgmggpmh neappppnir grgrggnirg rgrgrgfggt
      661 nhgggymnag agygsygyss nsatagysqf ysngghsgna ggggsggggg sssyssyyqg
      721 dsynspvppk hagkkplhgg qqkpsyssgy qshqgqqqpy nqsqyssygt pqdysgsggr
      781 sggnsygssg ssyntgshgg ygagsggsss yqgkqggyss qsnysspgss qsysgpassy
      841 qssqggysrn tehsmnyqyr
//
LOCUS       NP_001423364             909 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001423364 XP_063122309
VERSION     NP_001423364.1
DBSOURCE    REFSEQ: accession NM_001436435.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 909)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 909)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 909)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 909)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 909)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 909)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122309.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.406538.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..909
                     /product="interleukin enhancer-binding factor 3 isoform 6"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=97345
     Region          101..355
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          411..483
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(416,419..420,423..424,426,440..441,443,445,462..464,
                     467)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          532..603
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(539,541..542,545,558,561..563,567,583..586)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..909
                     /gene="Ilf3"
                     /coded_by="NM_001436435.1:240..2969"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrrpmrif vnddrhvmak hssvyptqee leavqnmvsh teralkavsd
       61 wideqekgns elseaenmdt ppddeskega geqkaehmtr tlrgvmrvgl vakglllkgd
      121 ldlelvllck ekpttalldk vadnlaiqlt tvtedkyeil qsvddaaivi kntkepplsl
      181 tihltspvvr eemekvlage tlsvndppdv ldrqkclaal aslrhakwfq aranglkscv
      241 ivirvlrdlc trvptwgplr gwplellcek sigtanrpmg agealrrvle clasgivmpd
      301 gsgiydpcek eatdaighld rqqreditqs aqhalrlaaf gqlhkvlgmd plpskmpkkp
      361 knenpvdytv qippsttyai tpmkrpmeed geekspskkk kkiqkkeeka eppqamnalm
      421 rlnqlkpglq yklisqtgpv hapiftmsve vdgstfeasg pskktaklhv avkvlqdmgl
      481 ptgaegrdss kgedsaeesd gkpavvappp vveavsnpss vfpsdatteg piltkhgknp
      541 vmelnekrrg lkyelisetg gshdkrfvme vevdgqkfqg agsnkkvaka yaalaalekl
      601 fpdaplalea nkkkrapvpv rggpkfaakp hnpgfgmggp mhneappppn irgrgrggni
      661 rgrgrgrgfg gtnhgggymn agagygsygy ssnsatagys qfysngghsg naggggsggg
      721 ggsssyssyy qgdsynspvp pkhagkkplh ggqqkpsyss gyqshqgqqq pynqsqyssy
      781 gtpqgkqkgy ghgqgsyssy snsynspggg ggsdysydsk fnysgsggrs ggnsygssgs
      841 syntgshggy gagsggsssy qgkqggyssq snysspgssq sysgpassyq ssqggysrnt
      901 ehsmnyqyr
//
LOCUS       NP_446182               1256 aa            linear   ROD 12-MAR-2025
DEFINITION  cohesin subunit SA-3 [Rattus norvegicus].
ACCESSION   NP_446182
VERSION     NP_446182.1
DBSOURCE    REFSEQ: accession NM_053730.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Fukuda,T., Fukuda,N., Agostinho,A., Hernandez-Hernandez,A.,
            Kouznetsova,A. and Hoog,C.
  TITLE     STAG3-mediated stabilization of REC8 cohesin complexes promotes
            chromosome synapsis during meiosis
  JOURNAL   EMBO J 33 (11), 1243-1255 (2014)
   PUBMED   24797475
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 1256)
  AUTHORS   Llano,E., Herran,Y., Garcia-Tunon,I., Gutierrez-Caballero,C., de
            Alava,E., Barbero,J.L., Schimenti,J., de Rooij,D.G.,
            Sanchez-Martin,M. and Pendas,A.M.
  TITLE     Meiotic cohesin complexes are essential for the formation of the
            axial element in mice
  JOURNAL   J Cell Biol 197 (7), 877-885 (2012)
   PUBMED   22711701
REFERENCE   4  (residues 1 to 1256)
  AUTHORS   Gutierrez-Caballero,C., Herran,Y., Sanchez-Martin,M., Suja,J.A.,
            Barbero,J.L., Llano,E. and Pendas,A.M.
  TITLE     Identification and molecular characterization of the mammalian
            alpha-kleisin RAD21L
  JOURNAL   Cell Cycle 10 (9), 1477-1487 (2011)
   PUBMED   21527826
REFERENCE   5  (residues 1 to 1256)
  AUTHORS   Lee,J. and Hirano,T.
  TITLE     RAD21L, a novel cohesin subunit implicated in linking homologous
            chromosomes in mammalian meiosis
  JOURNAL   J Cell Biol 192 (2), 263-276 (2011)
   PUBMED   21242291
REFERENCE   6  (residues 1 to 1256)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   7  (residues 1 to 1256)
  AUTHORS   Li,X.C. and Schimenti,J.C.
  TITLE     Mouse pachytene checkpoint 2 (trip13) is required for completing
            meiotic recombination but not synapsis
  JOURNAL   PLoS Genet 3 (8), e130 (2007)
   PUBMED   17696610
  REMARK    Erratum:[PLoS Genet. 2007 Sep 7;3(9):e168. Li, Xin [corrected to
            Li, Xin Chenglin]]
REFERENCE   8  (residues 1 to 1256)
  AUTHORS   Kouznetsova,A., Novak,I., Jessberger,R. and Hoog,C.
  TITLE     SYCP2 and SYCP3 are required for cohesin core integrity at
            diplotene but not for centromere cohesion at the first meiotic
            division
  JOURNAL   J Cell Sci 118 (Pt 10), 2271-2278 (2005)
   PUBMED   15870106
REFERENCE   9  (residues 1 to 1256)
  AUTHORS   Bayes,M., Prieto,I., Noguchi,J., Barbero,J.L. and Perez Jurado,L.A.
  TITLE     Evaluation of the Stag3 gene and the synaptonemal complex in a rat
            model (as/as) for male infertility
  JOURNAL   Mol Reprod Dev 60 (3), 414-417 (2001)
   PUBMED   11599053
REFERENCE   10 (residues 1 to 1256)
  AUTHORS   Pezzi,N., Prieto,I., Kremer,L., Perez Jurado,L.A., Valero,C., Del
            Mazo,J., Martinez-A,C. and Barbero,J.L.
  TITLE     STAG3, a novel gene encoding a protein involved in meiotic
            chromosome pairing and location of STAG3-related genes flanking the
            Williams-Beuren syndrome deletion
  JOURNAL   FASEB J 14 (3), 581-592 (2000)
   PUBMED   10698974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY027880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..1256
                     /product="cohesin subunit SA-3"
                     /note="cohesin subunit SA-3-like; SCC3 homolog 3;
                     stromalin-3; stromal antigen 3"
                     /calculated_mol_wt=141821
     Region          1..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Region          102..>426
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          188..301
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Region          1096..1169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Region          1230..1256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70576; propagated from
                     UniProtKB/Swiss-Prot (Q99M76.1)"
     CDS             1..1256
                     /gene="Stag3"
                     /coded_by="NM_053730.2:160..3930"
                     /db_xref="GeneID:114522"
                     /db_xref="RGD:621333"
ORIGIN      
        1 mptlwspstq hhgsssgsms splrksvrca qmalspcssn iqpcddrdsq gtaewdssst
       61 sedsdfedsl rrnvrkraak rppkaipvak hpkkqshivp ggndknksvp ptsdlfdavk
      121 aarscaqslv dewlenykqd enagflelvn ffiracgcks tvtpemfktm snseiiqhlt
      181 eefnedsgdy pltapgpswk kfqgsfcefv ktlvcqcqys llfdgfpmdd lislliglsd
      241 sqvrafrhts tlaamklmts lvkvalqlsl hkdnnqrqye aernkgpeqr aperleslle
      301 krkefqenqe eiegmmnaif rgvfvhryrd ilpeiravci eeigcwmqsy stsflndsyl
      361 kyigwtlhdk hkevrlkcvk alaglysnqe lssrmelftn rfkdrmvsmv mdresevave
      421 airlltlilk nmegvltsad cekiysivyi snramassag efvywkifhp ecgakavsgr
      481 errrspqaqr tfiylllaff mesehhdhaa ylvdslwdca gsylkdwesl tslllqkdqn
      541 lgdmqermli eilvssarqa aeghppvgri tgkksltake rklqaydkvk laehlipllp
      601 qllakfsada envapllrll syfdlniyct qrlekhlell lqqlqevvvk hvepevleaa
      661 ahalyllckp eftffsrvdf arsqlvdllt drfqqelddl mqssfldede vysltatlkr
      721 lsafynahdl trweisepcs rllrkavdtg evphqvilpa ltlvyfsilw tvthisests
      781 qkqlmslkkr mvafcelcqs clsdvdpeiq eqafvllsdl llifspqmvv ggrdflrplv
      841 ffpeatlqse lasflmdhvf lqpgelgngq sqedhvqiel lhqrrrllag fcklllygvl
      901 eldaasdvfk hynkfyedyg diiketltra rqidrcqcsr illlslkqly teliqeqgpq
      961 dltelpafie mrdlarrfal sfgpqqlhnr dlvvmlhkeg ikfslselpp agssreppni
     1021 aflellsefs prlfhqdkql llsylekclq rvsmapshpw gpvttychsl hlventaeas
     1081 sqgpphskkr cievprrlqe eesssqgesl qlnsgpttpt ltstavkrrq sprtvgkrqk
     1141 ggpgpgpgpg pgpgpgpgpg pgpgpgpeli csqqlsgtqr lkmssapcfq ircdpsgsgl
     1201 gkqmtrlslm eedeeeelrl ldeewqcgdk llhspsspse hgldlldtte lnmedf
//
LOCUS       NP_620268                358 aa            linear   ROD 12-MAR-2025
DEFINITION  2'-5'-oligoadenylate synthase 1A isoform 2 [Rattus norvegicus].
ACCESSION   NP_620268
VERSION     NP_620268.2
DBSOURCE    REFSEQ: accession NM_138913.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Leisching,G., Cole,V., Ali,A.T. and Baker,B.
  TITLE     OAS1, OAS2 and OAS3 restrict intracellular M. tb replication and
            enhance cytokine secretion
  JOURNAL   Int J Infect Dis 80S, S77-S84 (2019)
   PUBMED   30822544
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Sarmiento,L., Frisk,G., Anagandula,M., Hodik,M., Barchetta,I.,
            Netanyah,E., Cabrera-Rode,E. and Cilio,C.M.
  TITLE     Echovirus 6 Infects Human Exocrine and Endocrine Pancreatic Cells
            and Induces Pro-Inflammatory Innate Immune Response
  JOURNAL   Viruses 9 (2), 25 (2017)
   PUBMED   28146100
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Kim,S., Kim,M.J., Park,D.Y., Chung,H.J., Kim,C.H., Yoon,J.H. and
            Kim,H.J.
  TITLE     Mitochondrial reactive oxygen species modulate innate immune
            response to influenza A virus in human nasal epithelium
  JOURNAL   Antiviral Res 119, 78-83 (2015)
   PUBMED   25930096
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Go,M.J., Hwang,J.Y., Kim,Y.J., Hee Oh,J., Kim,Y.J., Heon Kwak,S.,
            Soo Park,K., Lee,J., Kim,B.J., Han,B.G., Cho,M.C., Cho,Y.S. and
            Lee,J.Y.
  TITLE     New susceptibility loci in MYL2, C12orf51 and OAS1 associated with
            1-h plasma glucose as predisposing risk factors for type 2 diabetes
            in the Korean population
  JOURNAL   J Hum Genet 58 (6), 362-365 (2013)
   PUBMED   23575436
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Donovan,J., Dufner,M. and Korennykh,A.
  TITLE     Structural basis for cytosolic double-stranded RNA surveillance by
            human oligoadenylate synthetase 1
  JOURNAL   Proc Natl Acad Sci U S A 110 (5), 1652-1657 (2013)
   PUBMED   23319625
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Hartmann,R., Walko,G. and Justesen,J.
  TITLE     Inhibition of 2'-5' oligoadenylate synthetase by divalent metal
            ions
  JOURNAL   FEBS Lett 507 (1), 54-58 (2001)
   PUBMED   11682059
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Truve,E., Aaspollu,A., Honkanen,J., Puska,R., Mehto,M., Hassi,A.,
            Teeri,T.H., Kelve,M., Seppanen,P. and Saarma,M.
  TITLE     Transgenic potato plants expressing mammalian 2'-5' oligoadenylate
            synthetase are protected from potato virus X infection under field
            conditions
  JOURNAL   Biotechnology (N Y) 11 (9), 1048-1052 (1993)
   PUBMED   7764002
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Shiojiri,S., Fukunaga,R., Ichii,Y. and Sokawa,Y.
  TITLE     Structure and expression of a cloned cDNA for human
            (2'-5')oligoadenylate synthetase
  JOURNAL   J Biochem 99 (5), 1455-1464 (1986)
   PUBMED   3754863
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Wathelet,M., Moutschen,S., Cravador,A., DeWit,L., Defilippi,P.,
            Huez,G. and Content,J.
  TITLE     Full-length sequence and expression of the 42 kDa 2-5A synthetase
            induced by human interferon
  JOURNAL   FEBS Lett 196 (1), 113-120 (1986)
   PUBMED   3753689
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Shimizu,N. and Sokawa,Y.
  TITLE     (2'-5')Oligoadenylate synthetase in pig spleen: isolation and
            characterization
  JOURNAL   J Biochem 94 (5), 1421-1428 (1983)
   PUBMED   6654863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Nov 27, 2020 this sequence version replaced NP_620268.1.
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z18877.1, SRR26643429.43390.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..358
                     /product="2'-5'-oligoadenylate synthase 1A isoform 2"
                     /EC_number="2.7.7.84"
                     /note="2'-5'-oligoadenylate synthetase 1;
                     2'-5'-oligoadenylate synthase 1; 2'-5' oligoadenylate
                     synthetase 1G; 2-5A synthetase 1; (2-5')oligo(A)
                     synthetase 1; 2-5A synthase 1; (2-5')oligo(A) synthase 1;
                     2',5'-oligoadenylate synthetase 1, 40/46kDa; 25
                     oligoadenylate synthetase; 2-5A synthase 1A;
                     (2-5')oligo(A) synthase 1A; 2'-5'-oligoadenylate synthase
                     1A"
                     /calculated_mol_wt=41549
     Region          14..61
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000250|UniProtKB:P00973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05961.1)"
     Region          27..167
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(62..64,67,69..71,76,78,128..129,132,149)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(76,78,149)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          164..349
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     Region          201..211
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000250|UniProtKB:P00973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05961.1)"
     CDS             1..358
                     /gene="Oas1a"
                     /gene_synonym="Oas1; Oas1g"
                     /coded_by="NM_138913.3:69..1145"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:192281"
                     /db_xref="RGD:621760"
ORIGIN      
        1 meqelrstps wkldkfievy llpntsfrdd vksainvlcd flkercfrdt vhpvrvskvv
       61 kggssgkgtt lkgksdadlv vflnnftsfe dqlnrrgefi keikkqlyev qrekhfrvkf
      121 evqsswwpnp ralsfklsap hlqqevefdv lpaydvlghv slysnpdpki ytilisecis
      181 lgkegefstc ftelqrnflk qrptklksli rlvkhwyqlc keklgkplpp qyalelltvy
      241 awergngite fntaqgfrti lelvtkyqql riywtkyydf qhpdvskylh rqlrksrpvi
      301 ldpadptgnv aggnqegwrr lasearlwlq ypcfmnrggs pvsswevpvd eawscill
//
LOCUS       NP_112388                594 aa            linear   ROD 12-MAR-2025
DEFINITION  syntaxin-binding protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_112388
VERSION     NP_112388.2
DBSOURCE    REFSEQ: accession NM_031126.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Wan,L., Chen,X. and Almers,W.
  TITLE     Munc18-dependent and -independent clustering of syntaxin in the
            plasma membrane of cultured endocrine cells
  JOURNAL   Proc Natl Acad Sci U S A 118 (49) (2021)
   PUBMED   34857632
  REMARK    GeneRIF: Munc18-dependent and -independent clustering of syntaxin
            in the plasma membrane of cultured endocrine cells.
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Yu,H., Shen,C., Liu,Y., Menasche,B.L., Ouyang,Y., Stowell,M.H.B.
            and Shen,J.
  TITLE     SNARE zippering requires activation by SNARE-like peptides in
            Sec1/Munc18 proteins
  JOURNAL   Proc Natl Acad Sci U S A 115 (36), E8421-E8429 (2018)
   PUBMED   30127032
  REMARK    GeneRIF: SNARE zippering requires activation by SNARE-like peptides
            in Sec1/Munc18 proteins
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Qin,T., Liang,T., Zhu,D., Kang,Y., Xie,L., Dolai,S., Sugita,S.,
            Takahashi,N., Ostenson,C.G., Banks,K. and Gaisano,H.Y.
  TITLE     Munc18b Increases Insulin Granule Fusion, Restoring Deficient
            Insulin Secretion in Type-2 Diabetes Human and Goto-Kakizaki Rat
            Islets with Improvement in Glucose Homeostasis
  JOURNAL   EBioMedicine 16, 262-274 (2017)
   PUBMED   28163042
  REMARK    GeneRIF: Data show that Munc18b overexpression increased fusion of
            not only newcomer secretory granule (SG), but also predocked SGs in
            type-2 diabetes (T2D) human and Goto-Kakizaki Rat Islets.
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Gandasi,N.R. and Barg,S.
  TITLE     Contact-induced clustering of syntaxin and munc18 docks secretory
            granules at the exocytosis site
  JOURNAL   Nat Commun 5, 3914 (2014)
   PUBMED   24835618
  REMARK    GeneRIF: Secretory vesicles dock by inducing syntaxin1/munc18
            clustering in the target membrane.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Brochetta,C., Suzuki,R., Vita,F., Soranzo,M.R., Claver,J.,
            Madjene,L.C., Attout,T., Vitte,J., Varin-Blank,N., Zabucchi,G.,
            Rivera,J. and Blank,U.
  TITLE     Munc18-2 and syntaxin 3 control distinct essential steps in mast
            cell degranulation
  JOURNAL   J Immunol 192 (1), 41-51 (2014)
   PUBMED   24323579
  REMARK    GeneRIF: Munc18-2 and STX3 perform distinct, but complementary,
            functions to support, respectively, SG translocation and membrane
            fusion in mast cells.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Coppola,T., Frantz,C., Perret-Menoud,V., Gattesco,S., Hirling,H.
            and Regazzi,R.
  TITLE     Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and
            controls exocytosis
  JOURNAL   Mol Biol Cell 13 (6), 1906-1915 (2002)
   PUBMED   12058058
  REMARK    GeneRIF: binds to granuphilin and controls exocytosis of pancreatic
            beta cells
REFERENCE   7  (residues 1 to 594)
  AUTHORS   van Niel,G., Raposo,G., Candalh,C., Boussac,M., Hershberg,R.,
            Cerf-Bensussan,N. and Heyman,M.
  TITLE     Intestinal epithelial cells secrete exosome-like vesicles
  JOURNAL   Gastroenterology 121 (2), 337-349 (2001)
   PUBMED   11487543
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Lehtonen,S., Riento,K., Olkkonen,V.M. and Lehtonen,E.
  TITLE     Syntaxin 3 and Munc-18-2 in epithelial cells during kidney
            development
  JOURNAL   Kidney Int 56 (3), 815-826 (1999)
   PUBMED   10469351
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Katagiri,H., Terasaki,J., Murata,T., Ishihara,H., Ogihara,T.,
            Inukai,K., Fukushima,Y., Anai,M., Kikuchi,M., Miyazaki,J. et al.
  TITLE     A novel isoform of syntaxin-binding protein homologous to yeast
            Sec1 expressed ubiquitously in mammalian cells
  JOURNAL   J Biol Chem 270 (10), 4963-4966 (1995)
   PUBMED   7890599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced NP_112388.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U20283.1, SRR26643293.83416.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..594
                     /product="syntaxin-binding protein 2 isoform 1"
                     /function="syntaxin binding protein"
                     /note="unc-18B; unc18-2; unc-18 homolog 2; unc-18 homolog
                     B; munc18-2; protein unc-18 homolog 2; protein unc-18
                     homolog B; syntaxin binding protein Munc18-2"
                     /calculated_mol_wt=66523
     Region          29..580
                     /region_name="Sec1"
                     /note="Sec1 family; pfam00995"
                     /db_xref="CDD:460020"
     CDS             1..594
                     /gene="Stxbp2"
                     /gene_synonym="Munc18b"
                     /coded_by="NM_031126.2:14..1798"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:81804"
                     /db_xref="RGD:619967"
ORIGIN      
        1 maplglkavv gekilsgvir svkkdgewkv limdhpsmri lsscckmsdi laegitived
       61 inkrrepips leaiyllspt eksvqaliad fqgtptftyk aahifftdtc peplfselgr
      121 srlakvvktl keihlaflpy eaqvfsldap hstynlycpf ragergrqld vlaqqiatlc
      181 atlqeypsir yrkgpedtaq lahavlakln afkadtpslg egpektrsql limdraadpv
      241 spllheltfq amaydllhie qdtyryettg lsesrekavl ldedddlwve lrhmhiadvs
      301 kkvtellktf ceskrlttdk anikdlshil kkmpqyqkel nkysthlhla ddcmkhfkgs
      361 veklcgveqd lamgsdaege kikdtmkliv pvlldasvpp ydkirvllly illrngvsee
      421 nlakliqhan vqsysnlirn leqlggtvtn sagsgtssrl errermepty qlsrwspvik
      481 dvmedvvedr ldrklwpfvs dpapvsssqa avssarfghw hknkagiear agprlivyiv
      541 ggvamsemra ayevtrateg kwevligssh iltptrfldd lrtldqkled ialp
//
LOCUS       NP_001423373             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423373 XP_063120856
VERSION     NP_001423373.1
DBSOURCE    REFSEQ: accession NM_001436444.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063120856.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.654941.1,
                                           SRR26360172.2477151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436444.1:317..898"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423371             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423371 XP_063120858
VERSION     NP_001423371.1
DBSOURCE    REFSEQ: accession NM_001436442.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063120858.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2121260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436442.1:665..1246"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423362             896 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423362 XP_063122314
VERSION     NP_001423362.1
DBSOURCE    REFSEQ: accession NM_001436433.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 896)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 896)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 896)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 896)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 896)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122314.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.485600.1,
                                           SRR26360194.1365682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..896
                     /product="interleukin enhancer-binding factor 3 isoform 4"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=95600
     Region          52..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          363..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          371..389
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          519..590
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(526,528..529,532,545,548..550,554,570..573)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     Region          608..896
                     /region_name="Interaction with PRMT1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          623..661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          719..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     CDS             1..896
                     /gene="Ilf3"
                     /coded_by="NM_001436433.1:240..2930"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdattegpil tkhgknpvme lnekrrglky
      541 elisetggsh dkrfvmevev dgqkfqgags nkkvakayaa laaleklfpd aplaleankk
      601 krapvpvrgg pkfaakphnp gfgmggpmhn eappppnirg rgrggnirgr grgrgfggtn
      661 hgggymnaga gygsygyssn satagysqfy sngghsgnag gggsgggggs ssyssyyqgd
      721 synspvppkh agkkplhggq qkpsyssgyq shqgqqqpyn qsqyssygtp qgkqkgyghg
      781 qgsyssysns ynspgggggs dysydskfny sgsggrsggn sygssgssyn tgshggygag
      841 sggsssyqgk qggyssqsny sspgssqsys gpassyqssq ggysrntehs mnyqyr
//
LOCUS       NP_001423366             703 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 8 [Rattus
            norvegicus].
ACCESSION   NP_001423366 XP_063122319
VERSION     NP_001423366.1
DBSOURCE    REFSEQ: accession NM_001436437.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122319.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.32697.1,
                                           SRR26643293.44135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..703
                     /product="interleukin enhancer-binding factor 3 isoform 8"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=76146
     Region          52..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          363..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          371..389
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          466..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          520..591
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(527,529..530,533,546,549..551,555,571..574)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     Region          624..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     CDS             1..703
                     /gene="Ilf3"
                     /coded_by="NM_001436437.1:240..2351"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdatteqgpi ltkhgknpvm elnekrrglk
      541 yelisetggs hdkrfvmeve vdgqkfqgag snkkvakaya alaaleklfp daplaleank
      601 kkrapvpvrg gpkfaakphn pgfgmggpmh neappppnir grgrggnirg rgrgrgfggt
      661 nhgggymnag agygsygyss nsatagysdf ftdcygyhdf gas
//
LOCUS       NP_001423356             375 aa            linear   ROD 12-MAR-2025
DEFINITION  G-protein coupled estrogen receptor 1 [Rattus norvegicus].
ACCESSION   NP_001423356
VERSION     NP_001423356.1
DBSOURCE    REFSEQ: accession NM_001436427.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,Y.Q., Sun,T., Zhao,Z., Fu,J., Yang,L., Xu,Y., Zhao,J.F.,
            Tang,X.L., Liu,A. and Zhao,M.G.
  TITLE     Activation of GPR30 Ameliorates Cerebral Ischemia-Reperfusion
            Injury by Suppressing Ferroptosis Through Nrf2/GPX4 Signaling
            Pathway
  JOURNAL   Neuromolecular Med 26 (1), 33 (2024)
   PUBMED   39138706
  REMARK    GeneRIF: Activation of GPR30 Ameliorates Cerebral
            Ischemia-Reperfusion Injury by Suppressing Ferroptosis Through
            Nrf2/GPX4 Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Grubic Kezele,T., Omrcen,H., Baticic,L., Sucurovic,S. and Zoricic
            Cvek,S.
  TITLE     Joint Inflammation Correlates with Joint GPR30 Expression in Males
            and Hippocampal GPR30 Expression in Females in a Rat Model of
            Rheumatoid Arthritis
  JOURNAL   Int J Mol Sci 25 (14), 7864 (2024)
   PUBMED   39063107
  REMARK    GeneRIF: Joint Inflammation Correlates with Joint GPR30 Expression
            in Males and Hippocampal GPR30 Expression in Females in a Rat Model
            of Rheumatoid Arthritis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Azizian,H., Farhadi,Z., Bader,M., Alizadeh Ghalenoei,J.,
            Ghafari,M.A. and Mahmoodzadeh,S.
  TITLE     GPER activation attenuates cardiac dysfunction by upregulating the
            SIRT1/3-AMPK-UCP2 pathway in postmenopausal diabetic rats
  JOURNAL   PLoS One 18 (12), e0293630 (2023)
   PUBMED   38134189
  REMARK    GeneRIF: GPER activation attenuates cardiac dysfunction by
            upregulating the SIRT1/3-AMPK-UCP2 pathway in postmenopausal
            diabetic rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hu,J., Huang,Y., Gao,F., Sun,W., Liu,H., Ma,H., Yuan,T., Liu,Z.,
            Tang,L., Ma,Y., Zhang,X., Bai,J. and Wang,R.
  TITLE     Brain-derived estrogen: a critical player in maintaining cognitive
            health of aged female rats, possibly involving GPR30
  JOURNAL   Neurobiol Aging 129, 15-27 (2023)
   PUBMED   37257405
  REMARK    GeneRIF: Brain-derived estrogen: a critical player in maintaining
            cognitive health of aged female rats, possibly involving GPR30.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Xu,X., Wang,J., Guo,X., Chen,Y., Ding,S., Zou,G., Zhu,L., Li,T. and
            Zhang,X.
  TITLE     GPR30-mediated non-classic estrogen pathway in mast cells
            participates in endometriosis pain via the production of FGF2
  JOURNAL   Front Immunol 14, 1106771 (2023)
   PUBMED   36845134
  REMARK    GeneRIF: GPR30-mediated non-classic estrogen pathway in mast cells
            participates in endometriosis pain via the production of FGF2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Sakamoto,H., Matsuda,K., Hosokawa,K., Nishi,M., Morris,J.F.,
            Prossnitz,E.R. and Kawata,M.
  TITLE     Expression of G protein-coupled receptor-30, a G protein-coupled
            membrane estrogen receptor, in oxytocin neurons of the rat
            paraventricular and supraoptic nuclei
  JOURNAL   Endocrinology 148 (12), 5842-5850 (2007)
   PUBMED   17872373
  REMARK    GeneRIF: Results suggest that GPR30 may serve primarily as a
            nongenomic transducer of estrogen actions in the
            hypothalamo-neurohypophyseal system.
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Funakoshi,T., Yanai,A., Shinoda,K., Kawano,M.M. and Mizukami,Y.
  TITLE     G protein-coupled receptor 30 is an estrogen receptor in the plasma
            membrane
  JOURNAL   Biochem Biophys Res Commun 346 (3), 904-910 (2006)
   PUBMED   16780796
  REMARK    GeneRIF: GPR30, a transmembrane receptor for estrogen, is localized
            to the plasma membrane of CA2 pyramidal neuronal cells of the
            hippocampus in rat brain
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Revankar,C.M., Cimino,D.F., Sklar,L.A., Arterburn,J.B. and
            Prossnitz,E.R.
  TITLE     A transmembrane intracellular estrogen receptor mediates rapid cell
            signaling
  JOURNAL   Science 307 (5715), 1625-1630 (2005)
   PUBMED   15705806
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Thomas,P., Pang,Y., Filardo,E.J. and Dong,J.
  TITLE     Identity of an estrogen membrane receptor coupled to a G protein in
            human breast cancer cells
  JOURNAL   Endocrinology 146 (2), 624-632 (2005)
   PUBMED   15539556
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Bonini,J.A., Anderson,S.M. and Steiner,D.F.
  TITLE     Molecular cloning and tissue expression of a novel orphan G
            protein-coupled receptor from rat lung
  JOURNAL   Biochem Biophys Res Commun 234 (1), 190-193 (1997)
   PUBMED   9168987
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.596012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680428,
                                           SAMN11044071 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..375
                     /product="G-protein coupled estrogen receptor 1"
                     /note="mER; chemokine receptor-like 2; membrane estrogen
                     receptor; G-protein coupled receptor 30; G-protein coupled
                     receptor 41; chemoattractant receptor-like 2"
                     /calculated_mol_wt=42156
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99527; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Region          60..335
                     /region_name="7tmA_GPER1"
                     /note="G protein-coupled estrogen receptor 1, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd14989"
                     /db_xref="CDD:320120"
     Region          61..87
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320120"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          94..119
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320120"
     Site            97..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Site            order(115,118..119,130..135,137..138,141,186,188..192,211,
                     214..216,218..220,222..223,272,275..276,278..279,282,
                     302..303,305..307,310,313..314)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320120"
     Region          130..160
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320120"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          173..194
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320120"
     Site            176..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          211..238
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320120"
     Site            221..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          252..282
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320120"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          303..328
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320120"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     CDS             1..375
                     /gene="Gper1"
                     /gene_synonym="Gper; Gpr30; GPR41"
                     /coded_by="NM_001436427.1:588..1715"
                     /db_xref="GeneID:171104"
                     /db_xref="RGD:619845"
ORIGIN      
        1 maattpaqdv gveiylgpvw papsnstpla lnlslalred apgnltgdls ehqqyvialf
       61 lsclytiflf pigfvgnili lvvnisfrek mtipdlyfin laaadlilva dslievfnld
      121 eqyydiavlc tfmslflqin myssvffltw msfdrylala kamrcglfrt khharlscgl
      181 iwmasvsatl vpftavhlrh teeacfcfad vrevqwlevt lgfivpfaii glcyslivra
      241 lirahrhrgl rprrqkalrm ifavvlvffi cwlpenvfis vhllqwaqpg dtpckqsfrh
      301 aypltghivn laafsnscln pliysflget frdklrlyva qktslpalnr fchatlkavi
      361 pdsteqsdvk fssav
//
LOCUS       NP_001423372             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423372 XP_063120857
VERSION     NP_001423372.1
DBSOURCE    REFSEQ: accession NM_001436443.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063120857.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.24258.1,
                                           SRR26360186.2289072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436443.1:351..932"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001100284            2155 aa            linear   ROD 12-MAR-2025
DEFINITION  alpha-tectorin isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001100284 XP_001059588 XP_236124
VERSION     NP_001100284.2
DBSOURCE    REFSEQ: accession NM_001106814.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2155)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 2155)
  AUTHORS   Mustapha,M., Weil,D., Chardenoux,S., Elias,S., El-Zir,E.,
            Beckmann,J.S., Loiselet,J. and Petit,C.
  TITLE     An alpha-tectorin gene defect causes a newly identified autosomal
            recessive form of sensorineural pre-lingual non-syndromic deafness,
            DFNB21
  JOURNAL   Hum Mol Genet 8 (3), 409-412 (1999)
   PUBMED   9949200
REFERENCE   3  (residues 1 to 2155)
  AUTHORS   Verhoeven,K., Van Laer,L., Kirschhofer,K., Legan,P.K., Hughes,D.C.,
            Schatteman,I., Verstreken,M., Van Hauwe,P., Coucke,P., Chen,A.,
            Smith,R.J., Somers,T., Offeciers,F.E., Van de Heyning,P.,
            Richardson,G.P., Wachtler,F., Kimberling,W.J., Willems,P.J.,
            Govaerts,P.J. and Van Camp,G.
  TITLE     Mutations in the human alpha-tectorin gene cause autosomal dominant
            non-syndromic hearing impairment
  JOURNAL   Nat Genet 19 (1), 60-62 (1998)
   PUBMED   9590290
  REMARK    Erratum:[Nat Genet 1999 Apr;21(4):449]
REFERENCE   4  (residues 1 to 2155)
  AUTHORS   Legan,P.K., Rau,A., Keen,J.N. and Richardson,G.P.
  TITLE     The mouse tectorins. Modular matrix proteins of the inner ear
            homologous to components of the sperm-egg adhesion system
  JOURNAL   J Biol Chem 272 (13), 8791-8801 (1997)
   PUBMED   9079715
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced NP_001100284.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2155
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..2155
                     /product="alpha-tectorin isoform 2 precursor"
                     /note="alpha-tectorin"
                     /calculated_mol_wt=236598
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2877
     Region          98..254
                     /region_name="NIDO"
                     /note="Extracellular domain of unknown function in nidogen
                     (entactin) and hypothetical proteins; smart00539"
                     /db_xref="CDD:214712"
     Region          313..477
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          517..591
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          597..650
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(606,610,623,627)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          652..706
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          703..865
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          905..981
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          984..1036
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(993,996,1009,1013)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          1100..1258
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Region          1300..1368
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          1372..1425
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(1381,1385,1398,1402)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          1487..1639
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Region          1685..1757
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          1805..2059
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Region          2089..2121
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     CDS             1..2155
                     /gene="Tecta"
                     /coded_by="NM_001106814.2:286..6753"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:300653"
                     /db_xref="RGD:1309824"
ORIGIN      
        1 mnyssllriw vsfifalvrh qaqprelmyp fwqndtrtpk vddgssseik laipvfffgv
       61 pyrtvyvnnn gvvsfnvlvs qftpesfplt dgrafiapfw advhngirge iyyretmdsa
      121 ilrratkdir kyfkdmttfs atwvfivtwe evtfyggsst tpvntfqavl vsdgsytftl
      181 fnyyeinwtt gtasggdplt glggvmaqag fnggnltnff slpgsrtpei vniqettnvn
      241 vpgrwafkvd gkeidpangc tsrgqflrrg evfwddlnct ikcrcldfnn eiycqeascs
      301 pyevcepkgr ffycspvets tcvvfgephy htfdgflfhf qgscayllar qclqtsslpf
      361 fsveaknehr ggsavswvke lsvevngyki lipkgsygkv kvndlvtslp vtlelgavki
      421 yqsgmstave tdfgllvtfd gqhyasisip gsyinstcgl cgnynknpld dflrpdgrpa
      481 msvldlgesw rvyhtdwkcg sgcidnctqc daatealyfg sdycgflnkt dgplwecgtv
      541 vdatafvhsc vydlcsvrdn gtllcqaiqa yalvcqalgi pigdwriqtg cvstvrcpsf
      601 shysvctssc pdtcsdltas qncatpcteg cecnegfvls tsqcvplhkc gcdfeghyyt
      661 mgeffwatan ctvqclceeg gdvycfnktc rsgevcaved gyqgcfpkre tvcllsqnqv
      721 lhtfdgaaya fpselsytll ktcperpeyl eidinkrkpd agpawlrgvr ilvadqevki
      781 ggvgalevkl ngqdvelpff hpsgrleihr nknsttvesk gvvsvqysdv gllyirlstm
      841 yfnctgglcg ffnanasdef clpngkctdn lavfleswtt feeicngecg dllkacnnds
      901 ellkfyrsrs rcgiindpsn ssflechgvv nvtayyrtcl frlcqsggne selcdsvary
      961 asacknadve vgpwrtydfc plecpenshf eecmtctetc etlalgpicv dscsegcqcd
     1021 egyalqgsqc vtrsecgcnf eghqlatnet fwvdqdcqif cycngtdnsv hcetipcrdd
     1081 dycmeesgly ycqprtdasc ivsgyghylt fdgypfdfqt scplilcttg srsisdsfpk
     1141 fivtaknedr dpslalwvkq vdvtvfgysi vihraykhtv lvnnerlylp lklgqgkini
     1201 fsfgfhvvve tdfglkvvyd wktflsitvp rsmqnstygl cgryngnpgd dlempmglla
     1261 lsinefgqsw vkrdtfcqvg cgdrcpscak vegfskvqql cslipnqnag fakchskvnp
     1321 tffyknclfd scidggavqt acswlqnyas tcqtqgvavt gwrnytscsv tcppnshyes
     1381 cvsvcqprca airlksdcnh ycvegcqcda gyvlngksci lphncgcysd gkyyepkqlf
     1441 wngdctrrcr cfrrnliqcd prqcksdeec alrsgvrgcf stktsyclaa gggvfrtfdg
     1501 aflrfpanca fvlsticqkl pdisfqliin fdkwsspnlt iispvyfyin eeqilindrn
     1561 tvkvngtqvn vpfitglatk iyssegflvi dtspdiqiyy ngfnvikisi serlqnkvcg
     1621 lcgnfngdmt ddyvtlrgkp vvssvvlaqs wktngmqkrp ltpscnelqf sqyaatcdnv
     1681 hiqamqgdgy clkltdmkgf fqpcyglldp lpfyescyld gcynhkkfql cgslaaygea
     1741 crsfgilste wiekencsgv vedpcvgadc pnrtceldng gelcgciepp pygnnshdii
     1801 daevtckaaq mevsiskckl fqlgferegv rindrqcsgi egedfisfqi nntkgncgnv
     1861 vqsngthimy kntiwiesan ntgniitrdr tinvefscay eldikislds vvkpmlsvin
     1921 ltvptqegsf ttkmalykna sykhpyrqge vvlttrdvly vgvfvvgads thliltlnkc
     1981 yatpsrdsnd klryfiiegg cqnikdntig ieengvsltc rfhvtvfkfi gdydevhlhc
     2041 avslcdseky sckincpqns riatdyskeh keqiisvgpi rrkrldwced nggceqvcts
     2101 rvdgplcscv tgslqedgrs crasnssvep qvwtlllimt qislwhfvyq sgats
//
LOCUS       NP_445864                910 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_445864
VERSION     NP_445864.2
DBSOURCE    REFSEQ: accession NM_053412.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Nov 26, 2020 this sequence version replaced NP_445864.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF220102.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..910
                     /product="interleukin enhancer-binding factor 3 isoform 1"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=97473
     Region          101..355
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          411..483
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(416,419..420,423..424,426,440..441,443,445,462..464,
                     467)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          533..604
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(540,542..543,546,559,562..564,568,584..587)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..910
                     /gene="Ilf3"
                     /coded_by="NM_053412.3:193..2925"
                     /note="isoform 1 is encoded by transcript variant 12"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrrpmrif vnddrhvmak hssvyptqee leavqnmvsh teralkavsd
       61 wideqekgns elseaenmdt ppddeskega geqkaehmtr tlrgvmrvgl vakglllkgd
      121 ldlelvllck ekpttalldk vadnlaiqlt tvtedkyeil qsvddaaivi kntkepplsl
      181 tihltspvvr eemekvlage tlsvndppdv ldrqkclaal aslrhakwfq aranglkscv
      241 ivirvlrdlc trvptwgplr gwplellcek sigtanrpmg agealrrvle clasgivmpd
      301 gsgiydpcek eatdaighld rqqreditqs aqhalrlaaf gqlhkvlgmd plpskmpkkp
      361 knenpvdytv qippsttyai tpmkrpmeed geekspskkk kkiqkkeeka eppqamnalm
      421 rlnqlkpglq yklisqtgpv hapiftmsve vdgstfeasg pskktaklhv avkvlqdmgl
      481 ptgaegrdss kgedsaeesd gkpavvappp vveavsnpss vfpsdatteq gpiltkhgkn
      541 pvmelnekrr glkyeliset ggshdkrfvm evevdgqkfq gagsnkkvak ayaalaalek
      601 lfpdaplale ankkkrapvp vrggpkfaak phnpgfgmgg pmhneapppp nirgrgrggn
      661 irgrgrgrgf ggtnhgggym nagagygsyg yssnsatagy sqfysngghs gnaggggsgg
      721 gggsssyssy yqgdsynspv ppkhagkkpl hggqqkpsys sgyqshqgqq qpynqsqyss
      781 ygtpqgkqkg yghgqgsyss ysnsynspgg gggsdysyds kfnysgsggr sggnsygssg
      841 ssyntgshgg ygagsggsss yqgkqggyss qsnysspgss qsysgpassy qssqggysrn
      901 tehsmnyqyr
//
LOCUS       NP_001100273             186 aa            linear   ROD 12-MAR-2025
DEFINITION  methyl-CpG-binding domain protein 3-like 1 [Rattus norvegicus].
ACCESSION   NP_001100273 XP_001075394 XP_235884
VERSION     NP_001100273.1
DBSOURCE    REFSEQ: accession NM_001106803.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_235884.1, XP_001075394.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..186
                     /product="methyl-CpG-binding domain protein 3-like 1"
                     /calculated_mol_wt=20673
     Region          9..74
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Region          78..166
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     CDS             1..186
                     /gene="Mbd3l1"
                     /coded_by="NM_001106803.2:170..730"
                     /db_xref="GeneID:300389"
                     /db_xref="RGD:1308259"
ORIGIN      
        1 mgktsqrkqc dcenpskpcl stsiplrmsn ytfkrpvtki tshlgnevry yqweetlekp
       61 eqacwqkrlq glqayssage ilstsdlska lkdltprdtd aassiiqans mdprplstlg
      121 ssshlakmip eagpqilcke flvteedisi qerkvkiare rlavaliahk lanetekvrg
      181 srkakv
//
LOCUS       NP_001423374             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423374 XP_006243762
VERSION     NP_001423374.1
DBSOURCE    REFSEQ: accession NM_001436445.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006243762.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061732.1, CF111044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436445.1:237..818"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423389             680 aa            linear   ROD 12-MAR-2025
DEFINITION  leucine-rich repeat-containing protein 49 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423389 XP_063121216
VERSION     NP_001423389.1
DBSOURCE    REFSEQ: accession NM_001436460.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063121216.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.883958.1,
                                           SRR26643298.44687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..680
                     /product="leucine-rich repeat-containing protein 49
                     isoform 4"
                     /note="leucine-rich repeat-containing protein 49"
                     /calculated_mol_wt=78268
     Region          88..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          108..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          111..306
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          130..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..173
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          196..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          218..239
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          240..264
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..680
                     /gene="Lrrc49"
                     /gene_synonym="RGD1309466"
                     /coded_by="NM_001436460.1:71..2113"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:300763"
                     /db_xref="RGD:1309466"
ORIGIN      
        1 msglqslryk vncglhlviq tsslsdknkv efklnretps fpgrllqhdl ernyssrqgd
       61 hinlvsssmp sfpilqrsse ektlysdrlt lerqkltvcp iidgeehlrl lnfqhnfitr
      121 iqnisnlqrl ifldlydnqi eeisglstlk slrvlllgkn rikkisnlen lknldvldlh
      181 gnqitkienv nhlcdlrvln larnllshvd nlngldslte lnlrhnqitf vrdvdnlpcl
      241 qrlflsfnni tsfesvscla estslsditf dgnpiaqesw ykhtvlqnmm qlrqldmkri
      301 teeerrvasv vakkeeekkr eshkqsllke kkrltinnva rkwdlqqrva niaiiqdrkd
      361 sesppqescq idggtisafp eeagsldagl ssalqglsvt ethlveldge tlslygsgal
      421 ecldrnwsvq tagmvttvsf tfiefdeivq vlpklkmkfp nslhlkfret nlvmlqqfna
      481 laqlrrvdql tidpqgnpvv nftlwkyyvl frlshfsmqk ingtevtqnd mimaerlfgi
      541 lahvasselp qyrmisilgd arkkqfryll enkckkpgil ceetsdskrl mgentnratl
      601 nyttrefyhe kleeikdkkk fcrlyvedlv keatainmkn ealqklwpqm fielvrdavi
      661 eirskdsymk lclqqitdqk
//
LOCUS       NP_001127941             686 aa            linear   ROD 12-MAR-2025
DEFINITION  leucine-rich repeat-containing protein 49 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001127941 XP_001073479 XP_236333
VERSION     NP_001127941.1
DBSOURCE    REFSEQ: accession NM_001134469.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_236333.3, XP_001073479.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160848.1, SRR26360172.1761484.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..686
                     /product="leucine-rich repeat-containing protein 49
                     isoform 2"
                     /note="leucine-rich repeat-containing protein 49"
                     /calculated_mol_wt=78807
     Region          94..111
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          114..135
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          117..312
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          136..157
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..179
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          180..201
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          202..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          224..245
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          246..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..686
                     /gene="Lrrc49"
                     /gene_synonym="RGD1309466"
                     /coded_by="NM_001134469.2:188..2248"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300763"
                     /db_xref="RGD:1309466"
ORIGIN      
        1 mipgkyrsvs graannvncg lhlviqtssl sdknkvefkl nretpsfpgr llqhdlerny
       61 ssrqgdhinl vsssmpsfpi lqrsseektl ysdrltlerq kltvcpiidg eehlrllnfq
      121 hnfitriqni snlqrlifld lydnqieeis glstlkslrv lllgknrikk isnlenlknl
      181 dvldlhgnqi tkienvnhlc dlrvlnlarn llshvdnlng ldsltelnlr hnqitfvrdv
      241 dnlpclqrlf lsfnnitsfe svsclaests lsditfdgnp iaqeswykht vlqnmmqlrq
      301 ldmkriteee rrvasvvakk eeekkreshk qsllkekkrl tinnvarkwd lqqrvaniai
      361 iqdrkdsesp pqescqidgg tisafpeeag sldaglssal qglsvtethl veldgetlsl
      421 ygsgalecld rnwsvqtagm vttvsftfie fdeivqvlpk lkmkfpnslh lkfretnlvm
      481 lqqfnalaql rrvdqltidp qgnpvvnftl wkyyvlfrls hfsmqkingt evtqndmima
      541 erlfgilahv asselpqyrm isilgdarkk qfryllenkc kkpgilceet sdskrlmgen
      601 tnratlnytt refyheklee ikdkkkfcrl yvedlvkeat ainmknealq klwpqmfiel
      661 vrdavieirs kdsymklclq qitdqk
//
LOCUS       NP_001423391             314 aa            linear   ROD 12-MAR-2025
DEFINITION  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001423391 XP_006243433
VERSION     NP_001423391.1
DBSOURCE    REFSEQ: accession NM_001436462.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cho,B., Choi,S.Y., Park,O.H., Sun,W. and Geum,D.
  TITLE     Differential expression of BNIP family members of BH3-only proteins
            during the development and after axotomy in the rat
  JOURNAL   Mol Cells 33 (6), 605-610 (2012)
   PUBMED   22639046
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Cuadrado,A. and Nebreda,A.R.
  TITLE     Mechanisms and functions of p38 MAPK signalling
  JOURNAL   Biochem J 429 (3), 403-417 (2010)
   PUBMED   20626350
  REMARK    Review article
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Lu,M. and Krauss,R.S.
  TITLE     N-cadherin ligation, but not Sonic hedgehog binding, initiates
            Cdo-dependent p38alpha/beta MAPK signaling in skeletal myoblasts
  JOURNAL   Proc Natl Acad Sci U S A 107 (9), 4212-4217 (2010)
   PUBMED   20160094
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Oh,J.E., Bae,G.U., Yang,Y.J., Yi,M.J., Lee,H.J., Kim,B.G.,
            Krauss,R.S. and Kang,J.S.
  TITLE     Cdo promotes neuronal differentiation via activation of the p38
            mitogen-activated protein kinase pathway
  JOURNAL   FASEB J 23 (7), 2088-2099 (2009)
   PUBMED   19244314
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Sonn,S., Jeong,Y. and Rhee,K.
  TITLE     Nip2/centrobin may be a substrate of Nek2 that is required for
            proper spindle assembly during mitosis in early mouse embryos
  JOURNAL   Mol Reprod Dev 76 (6), 587-592 (2009)
   PUBMED   19117032
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Boyd,J.M., Malstrom,S., Subramanian,T., Venkatesh,L.K.,
            Schaeper,U., Elangovan,B., D'Sa-Eipper,C. and Chinnadurai,G.
  TITLE     Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
            of cellular proteins
  JOURNAL   Cell 79 (2), 341-351 (1994)
   PUBMED   7954800
  REMARK    Erratum:[Cell. 1994 Dec 16;79(6):1121. PMID: 8001138]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006243433.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.34385.1,
                                           SRR26643290.29846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..314
                     /product="BCL2/adenovirus E1B 19 kDa protein-interacting
                     protein 2 isoform 2"
                     /note="Bcl-2 and E1B 19 kDa interacting protein;
                     BCL2/adenovirus E1B 19kDa-interacting protein 1, NIP2;
                     BCL2/adenovirus E1B interacting protein 2; BCL2/adenovirus
                     E1B 19 kDa protein-interacting protein 2"
                     /calculated_mol_wt=36023
     Region          49..163
                     /region_name="BNIP2"
                     /note="Bcl2-/adenovirus E1B nineteen kDa-interacting
                     protein 2; pfam12496"
                     /db_xref="CDD:463609"
     Region          147..295
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     CDS             1..314
                     /gene="Bnip2"
                     /coded_by="NM_001436462.1:247..1191"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300811"
                     /db_xref="RGD:1308944"
ORIGIN      
        1 megvelkeew qdedfpiplp eddsieadil dvtdpdrqpg slevngnkvr kklvapdisl
       61 tldpgedslw sddldeggev dldgldtpse nsdefewedd lpkpkttevi rkgsiteyaa
      121 teekedgrrw rmfrigeqdh rvdmkaiepy kkvishggyy gdglnaivvf avcfmpesgq
      181 pnyrylmdnl fkyvigtlel lvaenymiiy lngattrrkm pslgwlrrcy qqidrrlrkn
      241 lksliivhps wfirtllavt rpfisskfsq kiryvfnlae laelvpmeyv gipecikqvd
      301 qelngkqepp kseq
//
LOCUS       NP_001001504             943 aa            linear   ROD 12-MAR-2025
DEFINITION  general transcription factor II-I repeat domain-containing protein
            1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001001504 XP_341064 XP_347153
VERSION     NP_001001504.1
DBSOURCE    REFSEQ: accession NM_001001504.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Ganaie,I.A., Malik,M.Z., Naqvi,S.H., Jain,S.K. and Wajid,S.
  TITLE     Differential levels of Alpha-1-inhibitor III, Immunoglobulin heavy
            chain variable region, and Hypertrophied skeletal muscle protein
            GTF3 in rat mammary tumorigenesis
  JOURNAL   Biochimie 174, 57-68 (2020)
   PUBMED   32325114
  REMARK    GeneRIF: Differential levels of Alpha-1-inhibitor III,
            Immunoglobulin heavy chain variable region, and Hypertrophied
            skeletal muscle protein GTF3 in rat mammary tumorigenesis.
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Palmer,S.J., Taylor,K.M., Santucci,N., Widagdo,J., Chan,Y.K.,
            Yeo,J.L., Adams,M., Gunning,P.W. and Hardeman,E.C.
  TITLE     GTF2IRD2 from the Williams-Beuren critical region encodes a
            mobile-element-derived fusion protein that antagonizes the action
            of its related family members
  JOURNAL   J Cell Sci 125 (Pt 21), 5040-5050 (2012)
   PUBMED   22899722
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Enkhmandakh,B., Makeyev,A.V., Erdenechimeg,L., Ruddle,F.H.,
            Chimge,N.O., Tussie-Luna,M.I., Roy,A.L. and Bayarsaihan,D.
  TITLE     Essential functions of the Williams-Beuren syndrome-associated
            TFII-I genes in embryonic development
  JOURNAL   Proc Natl Acad Sci U S A 106 (1), 181-186 (2009)
   PUBMED   19109438
REFERENCE   4  (residues 1 to 943)
  AUTHORS   Olofsson,P., Holmberg,J., Tordsson,J., Lu,S., Akerstrom,B. and
            Holmdahl,R.
  TITLE     Positional identification of Ncf1 as a gene that regulates
            arthritis severity in rats
  JOURNAL   Nat Genet 33 (1), 25-32 (2003)
   PUBMED   12461526
REFERENCE   5  (residues 1 to 943)
  AUTHORS   Bayarsaihan,D. and Ruddle,F.H.
  TITLE     Isolation and characterization of BEN, a member of the TFII-I
            family of DNA-binding proteins containing distinct helix-loop-helix
            domains
  JOURNAL   Proc Natl Acad Sci U S A 97 (13), 7342-7347 (2000)
   PUBMED   10861001
REFERENCE   6  (residues 1 to 943)
  AUTHORS   Franke,Y., Peoples,R.J. and Francke,U.
  TITLE     Identification of GTF2IRD1, a putative transcription factor within
            the Williams-Beuren syndrome deletion at 7q11.23
  JOURNAL   Cytogenet Cell Genet 86 (3-4), 296-304 (1999)
   PUBMED   10575229
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_341064.1, XP_347153.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF547389.1, AF547388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..943
                     /product="general transcription factor II-I repeat
                     domain-containing protein 1 isoform 2"
                     /note="general transcription factor II I repeat
                     domain-containing 1; general transcription factor II-I
                     repeat domain-containing protein 1-like"
                     /calculated_mol_wt=105116
     Region          128..202
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          351..425
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          565..639
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          690..764
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          787..859
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     CDS             1..943
                     /gene="Gtf2ird1"
                     /gene_synonym="Gtf3"
                     /coded_by="NM_001001504.3:277..3108"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:246770"
                     /db_xref="RGD:620856"
ORIGIN      
        1 mallgkhcdi ptngcgserw nstfarkdel inslvsalds mcsalsklnt evacvavhne
       61 svfvmgtekg rvflntrkel qsdflrfcrg plwndpeagh pkkvqrcegg grsiprssle
      121 qcsdvyllqk mveevfdvly seamgratvv plpyerllre pgllavqglp eglafrrpae
      181 ydpkalmail ehshrirfkl rrppddggqd tkalvemngi sllpkgsrdc glhgqaskvs
      241 pqdltptatp ssmanflyst smpnhtirel kqevptcplt psdlglgwpv pephvpstqd
      301 fsdccgqapa gpagpliqnv haskrilfsi vhdksekwdp fikemedint lrecvqilfn
      361 sryaealgld hmvpvpyrki acdpeaveiv gipdkipfkr pctygvpklk rileerhsih
      421 fiikrmfder iftgnkftkd pmklepaspp edtatevcrd smldlagtaw sdmssvsedc
      481 gpgtsgeigm lrpikiepee ldiiqvtvsd psptseemtd slpghlpsed sgygmempad
      541 kgpseepwqe erpaeespgd virplrkqve mlfntkyaka igtsepvkvp yskflmhpee
      601 lfvlglpegi slrrpncfgi aklrkileas nsiqfvikrp elltdgvkep vmdtqerdsw
      661 dplvdetpkr qglqenyntr lsridiantl reqvqdlfnk kygealgiky pvqvpykrik
      721 snpgsviieg lppgipfrkp ctfgsqnler ilsvadkikf tvtrpfqgli pkpdeddanr
      781 lgekvilreq vkelfnekyg ealglnrpvl vpyklirdsp davevkglpd dipfrnpnty
      841 dihrlekilk ardhvrmvii nqlqpfgdvc nnakvpakdn ipkrkrkrvs egnsvsssss
      901 sssssssnpe svastnqisl vqwpvymvdy sglnvqlpgp ldy
//
LOCUS       NP_062249                247 aa            linear   ROD 12-MAR-2025
DEFINITION  14-3-3 protein gamma [Rattus norvegicus].
ACCESSION   NP_062249 XP_346431 XP_347354
VERSION     NP_062249.1
DBSOURCE    REFSEQ: accession NM_019376.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Han,L., Tang,J., Zhu,S. and Zhu,J.
  TITLE     LncRNA SNHG7 Knockdown Aggravates Hepatic Ischemia-Reperfusion
            Injury and Promotes Apoptosis in Hemorrhagic Shock Pregnant Rats by
            Modulating miR-34a-5p/YWHAG Axis
  JOURNAL   Mol Biotechnol 65 (6), 983-996 (2023)
   PUBMED   36427097
  REMARK    GeneRIF: LncRNA SNHG7 Knockdown Aggravates Hepatic
            Ischemia-Reperfusion Injury and Promotes Apoptosis in Hemorrhagic
            Shock Pregnant Rats by Modulating miR-34a-5p/YWHAG Axis.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Abu-Rumeileh,S., Baiardi,S., Polischi,B., Mammana,A.,
            Franceschini,A., Green,A., Capellari,S. and Parchi,P.
  TITLE     Diagnostic value of surrogate CSF biomarkers for Creutzfeldt-Jakob
            disease in the era of RT-QuIC
  JOURNAL   J Neurol 266 (12), 3136-3143 (2019)
   PUBMED   31541342
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Otsuka,S., Sakakima,H., Terashi,T., Takada,S., Nakanishi,K. and
            Kikuchi,K.
  TITLE     Preconditioning exercise reduces brain damage and neuronal
            apoptosis through enhanced endogenous 14-3-3gamma after focal brain
            ischemia in rats
  JOURNAL   Brain Struct Funct 224 (2), 727-738 (2019)
   PUBMED   30478609
  REMARK    GeneRIF: Our findings suggest that preconditioning exercise prior
            to ischemia induces neuron- and astrocyte-mediated brain ischemic
            tolerance through increased expression of HIF-1alpha and
            14-3-3gamma, which are intrinsic protective factors; the
            upregulated 14-3-3gamma induced by preconditioning exercise reduces
            ischemic neuronal cell death through the 14-3-3gamma/p-beta-catenin
            Ser37/Bax/caspase 3 anti-apoptotic pathway.
            Erratum:[Brain Struct Funct. 2019 Mar;224(2):739-740. doi:
            10.1007/s00429-018-1815-x. PMID: 30560373]
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Kanata,E., Golanska,E., Villar-Pique,A., Karsanidou,A., Dafou,D.,
            Xanthopoulos,K., Schmitz,M., Ferrer,I., Karch,A., Sikorska,B.,
            Liberski,P.P., Sklaviadis,T., Zerr,I. and Llorens,F.
  TITLE     Cerebrospinal fluid neurofilament light in suspected sporadic
            Creutzfeldt-Jakob disease
  JOURNAL   J Clin Neurosci 60, 124-127 (2019)
   PUBMED   30309804
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Gerber,K.J., Squires,K.E. and Hepler,J.R.
  TITLE     14-3-3gamma binds regulator of G protein signaling 14 (RGS14) at
            distinct sites to inhibit the RGS14:Galphai-AlF4- signaling complex
            and RGS14 nuclear localization
  JOURNAL   J Biol Chem 293 (38), 14616-14631 (2018)
   PUBMED   30093406
  REMARK    GeneRIF: phosphorylation-independent binding of 14-3-3 has no
            effect on RGS14/Galphai interactions but, instead, inhibits
            (directly or indirectly) RGS14 nuclear import and nucleocytoplasmic
            shuttling
            Erratum:[J Biol Chem. 2019 Aug 9;294(32):12262. doi:
            10.1074/jbc.AAC119.101131. PMID: 31399537]
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Peyrl,A., Weitzdoerfer,R., Gulesserian,T., Fountoulakis,M. and
            Lubec,G.
  TITLE     Aberrant expression of signaling-related proteins 14-3-3 gamma and
            RACK1 in fetal Down syndrome brain (trisomy 21)
  JOURNAL   Electrophoresis 23 (1), 152-157 (2002)
   PUBMED   11824616
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Autieri,M.V. and Carbone,C.J.
  TITLE     14-3-3Gamma interacts with and is phosphorylated by multiple
            protein kinase C isoforms in PDGF-stimulated human vascular smooth
            muscle cells
  JOURNAL   DNA Cell Biol 18 (7), 555-564 (1999)
   PUBMED   10433554
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Martin,H., Rostas,J., Patel,Y. and Aitken,A.
  TITLE     Subcellular localisation of 14-3-3 isoforms in rat brain using
            specific antibodies
  JOURNAL   J Neurochem 63 (6), 2259-2265 (1994)
   PUBMED   7964746
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Watanabe,M., Isobe,T., Ichimura,T., Kuwano,R., Takahashi,Y.,
            Kondo,H. and Inoue,Y.
  TITLE     Molecular cloning of rat cDNAs for the zeta and theta subtypes of
            14-3-3 protein and differential distributions of their mRNAs in the
            brain
  JOURNAL   Brain Res Mol Brain Res 25 (1-2), 113-121 (1994)
   PUBMED   7984035
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Watanabe,M., Isobe,T., Ichimura,T., Kuwano,R., Takahashi,Y. and
            Kondo,H.
  TITLE     Molecular cloning of rat cDNAs for beta and gamma subtypes of
            14-3-3 protein and developmental changes in expression of their
            mRNAs in the nervous system
  JOURNAL   Brain Res Mol Brain Res 17 (1-2), 135-146 (1993)
   PUBMED   8381897
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Dec 17, 2003 this sequence version replaced
            XP_346431.1, XP_347354.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127496.1, SRR26360190.3315089.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..247
                     /product="14-3-3 protein gamma"
                     /note="tyrosine 3/tryptophan 5 -monooxygenase activation
                     protein, gamma polypeptide; tyrosine
                     3-monooxgenase/tryptophan 5-monooxgenase activation
                     protein, gamma polypeptide; 14-3-3 protein gamma-subtype;
                     tryosine 3-monooxgenase/tryptophan 5-monooxgenase
                     activation protein gamma polypeptide;
                     3-monooxygenase/tryptophan 5-monooxgenase activation
                     protein gamma polypeptide; tryosine
                     3-monooxgenase/tryptophan 5 monooxgenase activation
                     protein gamma; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, gamma polypeptide"
                     /calculated_mol_wt=28172
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Region          2..247
                     /region_name="14-3-3_gamma"
                     /note="14-3-3 gamma, an isoform of 14-3-3 protein;
                     cd10024"
                     /db_xref="CDD:206760"
     Region          2..247
                     /region_name="Interaction with SPATA18/MIEAP.
                     /evidence=ECO:0000250|UniProtKB:P61981"
                     /note="propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline, in 14-3-3 protein gamma,
                     N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            order(6,9..10,13..14,16..17,19,22,59,62..63,66,77..78,
                     81..82,85,88..89,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206760"
     Site            order(50,57,125,132..133,177..178,181,222,225,229,
                     232..233)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206760"
     Site            57
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P61981;
                     propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            132
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P61981;
                     propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     CDS             1..247
                     /gene="Ywhag"
                     /gene_synonym="14-3-3G"
                     /coded_by="NM_019376.3:191..934"
                     /db_xref="GeneID:56010"
                     /db_xref="RGD:62002"
ORIGIN      
        1 mvdreqlvqk arlaeqaery ddmaaamknv telneplsne ernllsvayk nvvgarrssw
       61 rvissieqkt sadgnekkie mvrayrekie keleavcqdv lslldnylik ncsetqyesk
      121 vfylkmkgdy yrylaevatg ekratvvess ekayseahei skehmqpthp irlglalnys
      181 vfyyeiqnap eqachlakta fddaiaeldt lnedsykdst limqllrdnl tlwtsdqqdd
      241 dggegnn
//
LOCUS       NP_001423376             193 aa            linear   ROD 12-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_001423376 XP_006243763
VERSION     NP_001423376.1
DBSOURCE    REFSEQ: accession NM_001436447.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006243763.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.584314.1,
                                           SRR22399481.296533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_001436447.1:317..898"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423367             702 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 9 [Rattus
            norvegicus].
ACCESSION   NP_001423367 XP_063122322
VERSION     NP_001423367.1
DBSOURCE    REFSEQ: accession NM_001436438.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 702)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 702)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 702)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 702)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122322.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1971005.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..702
                     /product="interleukin enhancer-binding factor 3 isoform 9"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=76018
     Region          52..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          363..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          371..389
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          519..590
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(526,528..529,532,545,548..550,554,570..573)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     Region          623..661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     CDS             1..702
                     /gene="Ilf3"
                     /coded_by="NM_001436438.1:240..2348"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdattegpil tkhgknpvme lnekrrglky
      541 elisetggsh dkrfvmevev dgqkfqgags nkkvakayaa laaleklfpd aplaleankk
      601 krapvpvrgg pkfaakphnp gfgmggpmhn eappppnirg rgrggnirgr grgrgfggtn
      661 hgggymnaga gygsygyssn satagysdff tdcygyhdfg as
//
LOCUS       NP_001423363             915 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423363 XP_008764212
VERSION     NP_001423363.1
DBSOURCE    REFSEQ: accession NM_001436434.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 915)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 915)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 915)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 915)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 915)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 915)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 915)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 915)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 915)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 915)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_008764212.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2028564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..915
                     /product="interleukin enhancer-binding factor 3 isoform 5"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=98120
     Region          106..360
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          416..488
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(421,424..425,428..429,431,445..446,448,450,467..469,
                     472)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          538..609
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(545,547..548,551,564,567..569,573,589..592)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..915
                     /gene="Ilf3"
                     /coded_by="NM_001436434.1:240..2987"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrfshfqr pmrifvnddr hvmakhssvy ptqeeleavq nmvshteral
       61 kavsdwideq ekgnselsea enmdtppdde skegageqka ehmtrtlrgv mrvglvakgl
      121 llkgdldlel vllckekptt alldkvadnl aiqlttvted kyeilqsvdd aaivikntke
      181 pplsltihlt spvvreemek vlagetlsvn dppdvldrqk claalaslrh akwfqarang
      241 lkscvivirv lrdlctrvpt wgplrgwple llceksigta nrpmgageal rrvleclasg
      301 ivmpdgsgiy dpcekeatda ighldrqqre ditqsaqhal rlaafgqlhk vlgmdplpsk
      361 mpkkpknenp vdytvqipps ttyaitpmkr pmeedgeeks pskkkkkiqk keekaeppqa
      421 mnalmrlnql kpglqyklis qtgpvhapif tmsvevdgst feasgpskkt aklhvavkvl
      481 qdmglptgae grdsskgeds aeesdgkpav vapppvveav snpssvfpsd atteqgpilt
      541 khgknpvmel nekrrglkye lisetggshd krfvmevevd gqkfqgagsn kkvakayaal
      601 aaleklfpda plaleankkk rapvpvrggp kfaakphnpg fgmggpmhne appppnirgr
      661 grggnirgrg rgrgfggtnh gggymnagag ygsygyssns atagysqfys ngghsgnagg
      721 ggsgggggss syssyyqgds ynspvppkha gkkplhggqq kpsyssgyqs hqgqqqpynq
      781 sqyssygtpq gkqkgyghgq gsyssysnsy nspgggggsd ysydskfnys gsggrsggns
      841 ygssgssynt gshggygags ggsssyqgkq ggyssqsnys spgssqsysg passyqssqg
      901 gysrntehsm nyqyr
//
LOCUS       NP_001423370             897 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423370 XP_038938140
VERSION     NP_001423370.1
DBSOURCE    REFSEQ: accession NM_001436441.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_038938140.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.765712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..897
                     /product="interleukin enhancer-binding factor 3 isoform 3"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=95728
     Region          52..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          363..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          371..389
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          466..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          520..591
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(527,529..530,533,546,549..551,555,571..574)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     Region          609..897
                     /region_name="Interaction with PRMT1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          624..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          720..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            818
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     CDS             1..897
                     /gene="Ilf3"
                     /coded_by="NM_001436441.1:337..3030"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdatteqgpi ltkhgknpvm elnekrrglk
      541 yelisetggs hdkrfvmeve vdgqkfqgag snkkvakaya alaaleklfp daplaleank
      601 kkrapvpvrg gpkfaakphn pgfgmggpmh neappppnir grgrggnirg rgrgrgfggt
      661 nhgggymnag agygsygyss nsatagysqf ysngghsgna ggggsggggg sssyssyyqg
      721 dsynspvppk hagkkplhgg qqkpsyssgy qshqgqqqpy nqsqyssygt pqgkqkgygh
      781 gqgsyssysn synspggggg sdysydskfn ysgsggrsgg nsygssgssy ntgshggyga
      841 gsggsssyqg kqggyssqsn ysspgssqsy sgpassyqss qggysrnteh smnyqyr
//
LOCUS       NP_001423368             716 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 10 [Rattus
            norvegicus].
ACCESSION   NP_001423368 XP_008764218
VERSION     NP_001423368.1
DBSOURCE    REFSEQ: accession NM_001436439.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_008764218.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.32700.1,
                                           SRR26643297.27536.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..716
                     /product="interleukin enhancer-binding factor 3 isoform
                     10"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=77891
     Region          101..355
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          411..483
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(416,419..420,423..424,426,440..441,443,445,462..464,
                     467)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          533..604
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(540,542..543,546,559,562..564,568,584..587)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..716
                     /gene="Ilf3"
                     /coded_by="NM_001436439.1:240..2390"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrrpmrif vnddrhvmak hssvyptqee leavqnmvsh teralkavsd
       61 wideqekgns elseaenmdt ppddeskega geqkaehmtr tlrgvmrvgl vakglllkgd
      121 ldlelvllck ekpttalldk vadnlaiqlt tvtedkyeil qsvddaaivi kntkepplsl
      181 tihltspvvr eemekvlage tlsvndppdv ldrqkclaal aslrhakwfq aranglkscv
      241 ivirvlrdlc trvptwgplr gwplellcek sigtanrpmg agealrrvle clasgivmpd
      301 gsgiydpcek eatdaighld rqqreditqs aqhalrlaaf gqlhkvlgmd plpskmpkkp
      361 knenpvdytv qippsttyai tpmkrpmeed geekspskkk kkiqkkeeka eppqamnalm
      421 rlnqlkpglq yklisqtgpv hapiftmsve vdgstfeasg pskktaklhv avkvlqdmgl
      481 ptgaegrdss kgedsaeesd gkpavvappp vveavsnpss vfpsdatteq gpiltkhgkn
      541 pvmelnekrr glkyeliset ggshdkrfvm evevdgqkfq gagsnkkvak ayaalaalek
      601 lfpdaplale ankkkrapvp vrggpkfaak phnpgfgmgg pmhneapppp nirgrgrggn
      661 irgrgrgrgf ggtnhgggym nagagygsyg yssnsatagy sdfftdcygy hdfgas
//
LOCUS       NP_001423382             186 aa            linear   ROD 12-MAR-2025
DEFINITION  methyl-CpG-binding domain protein 3-like 1 [Rattus norvegicus].
ACCESSION   NP_001423382 XP_017451015
VERSION     NP_001423382.1
DBSOURCE    REFSEQ: accession NM_001436453.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_017451015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2664997.1,
                                           SRR26360181.1108077.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..186
                     /product="methyl-CpG-binding domain protein 3-like 1"
                     /calculated_mol_wt=20673
     Region          9..74
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Region          78..166
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     CDS             1..186
                     /gene="Mbd3l1"
                     /coded_by="NM_001436453.1:70..630"
                     /db_xref="GeneID:300389"
                     /db_xref="RGD:1308259"
ORIGIN      
        1 mgktsqrkqc dcenpskpcl stsiplrmsn ytfkrpvtki tshlgnevry yqweetlekp
       61 eqacwqkrlq glqayssage ilstsdlska lkdltprdtd aassiiqans mdprplstlg
      121 ssshlakmip eagpqilcke flvteedisi qerkvkiare rlavaliahk lanetekvrg
      181 srkakv
//
LOCUS       NP_001423365             902 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001423365 XP_008764215
VERSION     NP_001423365.1
DBSOURCE    REFSEQ: accession NM_001436436.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_008764215.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1549873.1,
                                           SRR26360194.2114172.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..902
                     /product="interleukin enhancer-binding factor 3 isoform 7"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=96375
     Region          93..347
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          403..475
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(408,411..412,415..416,418,432..433,435,437,454..456,
                     459)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          525..596
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(532,534..535,538,551,554..556,560,576..579)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..902
                     /gene="Ilf3"
                     /coded_by="NM_001436436.1:240..2948"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mfshfqrpmr ifvnddrhvm akhssvyptq eeleavqnmv shteralkav sdwideqekg
       61 nselseaenm dtppddeske gageqkaehm trtlrgvmrv glvakglllk gdldlelvll
      121 ckekpttall dkvadnlaiq lttvtedkye ilqsvddaai vikntkeppl sltihltspv
      181 vreemekvla getlsvndpp dvldrqkcla alaslrhakw fqaranglks cvivirvlrd
      241 lctrvptwgp lrgwplellc eksigtanrp mgagealrrv leclasgivm pdgsgiydpc
      301 ekeatdaigh ldrqqredit qsaqhalrla afgqlhkvlg mdplpskmpk kpknenpvdy
      361 tvqippstty aitpmkrpme edgeekspsk kkkkiqkkee kaeppqamna lmrlnqlkpg
      421 lqyklisqtg pvhapiftms vevdgstfea sgpskktakl hvavkvlqdm glptgaegrd
      481 sskgedsaee sdgkpavvap ppvveavsnp ssvfpsdatt eqgpiltkhg knpvmelnek
      541 rrglkyelis etggshdkrf vmevevdgqk fqgagsnkkv akayaalaal eklfpdapla
      601 leankkkrap vpvrggpkfa akphnpgfgm ggpmhneapp ppnirgrgrg gnirgrgrgr
      661 gfggtnhggg ymnagagygs ygyssnsata gysqfysngg hsgnaggggs gggggsssys
      721 syyqgdsyns pvppkhagkk plhggqqkps yssgyqshqg qqqpynqsqy ssygtpqgkq
      781 kgyghgqgsy ssysnsynsp gggggsdysy dskfnysgsg grsggnsygs sgssyntgsh
      841 ggygagsggs ssyqgkqggy ssqsnysspg ssqsysgpas syqssqggys rntehsmnyq
      901 yr
//
LOCUS       NP_001423388             667 aa            linear   ROD 12-MAR-2025
DEFINITION  leucine-rich repeat-containing protein 49 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423388 XP_063121217
VERSION     NP_001423388.1
DBSOURCE    REFSEQ: accession NM_001436459.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063121217.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.31470.1,
                                           SRR26643293.45708.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..667
                     /product="leucine-rich repeat-containing protein 49
                     isoform 3"
                     /note="leucine-rich repeat-containing protein 49"
                     /calculated_mol_wt=76768
     Region          75..92
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          95..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          98..293
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          117..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          139..160
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          161..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          183..204
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..226
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          227..251
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..667
                     /gene="Lrrc49"
                     /gene_synonym="RGD1309466"
                     /coded_by="NM_001436459.1:188..2191"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300763"
                     /db_xref="RGD:1309466"
ORIGIN      
        1 mipgkyrsvs graannvefk lnretpsfpg rllqhdlern yssrqgdhin lvsssmpsfp
       61 ilqrsseekt lysdrltler qkltvcpiid geehlrllnf qhnfitriqn isnlqrlifl
      121 dlydnqieei sglstlkslr vlllgknrik kisnlenlkn ldvldlhgnq itkienvnhl
      181 cdlrvlnlar nllshvdnln gldsltelnl rhnqitfvrd vdnlpclqrl flsfnnitsf
      241 esvsclaest slsditfdgn piaqeswykh tvlqnmmqlr qldmkritee errvasvvak
      301 keeekkresh kqsllkekkr ltinnvarkw dlqqrvania iiqdrkdses ppqescqidg
      361 gtisafpeea gsldaglssa lqglsvteth lveldgetls lygsgalecl drnwsvqtag
      421 mvttvsftfi efdeivqvlp klkmkfpnsl hlkfretnlv mlqqfnalaq lrrvdqltid
      481 pqgnpvvnft lwkyyvlfrl shfsmqking tevtqndmim aerlfgilah vasselpqyr
      541 misilgdark kqfryllenk ckkpgilcee tsdskrlmge ntnratlnyt trefyhekle
      601 eikdkkkfcr lyvedlvkea tainmkneal qklwpqmfie lvrdavieir skdsymklcl
      661 qqitdqk
//
LOCUS       NP_001423377             490 aa            linear   ROD 12-MAR-2025
DEFINITION  dual specificity protein kinase CLK3 [Rattus norvegicus].
ACCESSION   NP_001423377
VERSION     NP_001423377.1
DBSOURCE    REFSEQ: accession NM_001436448.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Ma,X., Gao,L., Ge,R., Yuan,T., Lin,B. and Zhen,L.
  TITLE     CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 333-342 (2024)
   PUBMED   38438604
  REMARK    GeneRIF: CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Duncan,P.I., Stojdl,D.F., Marius,R.M., Scheit,K.H. and Bell,J.C.
  TITLE     The Clk2 and Clk3 dual-specificity protein kinases regulate the
            intranuclear distribution of SR proteins and influence pre-mRNA
            splicing
  JOURNAL   Exp Cell Res 241 (2), 300-308 (1998)
   PUBMED   9637771
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Nayler,O., Stamm,S. and Ullrich,A.
  TITLE     Characterization and comparison of four serine- and arginine-rich
            (SR) protein kinases
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 693-700 (1997)
   PUBMED   9307018
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Becker,W., Kentrup,H., Heukelbach,J. and Joost,H.G.
  TITLE     cDNA cloning and characterization of rat Clk3, a LAMMER kinase
            predominately expressed in testis
  JOURNAL   Biochim Biophys Acta 1312 (1), 63-67 (1996)
   PUBMED   8679717
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070891.1, SRR22399489.1990478.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..490
                     /product="dual specificity protein kinase CLK3"
                     /EC_number="2.7.12.1"
                     /calculated_mol_wt=58354
     Region          1..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63117.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Region          142..472
                     /region_name="PKc_CLK3"
                     /note="Catalytic domain of the Dual-specificity protein
                     kinase, CDC-like kinase 3; cd14214"
                     /db_xref="CDD:271116"
     Site            order(162..166,170,184,186,200,220,236..239,242,244..245,
                     283,285,287..288,290,320,323,332,334..337,339,376)
                     /site_type="active"
                     /db_xref="CDD:271116"
     Site            order(162..165,170,184,186,220,236..239,242,245,287..288,
                     290,319..320)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271116"
     Site            order(200,244,283,285,323,332,334..337,339,376)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271116"
     Site            319..339
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271116"
     CDS             1..490
                     /gene="Clk3"
                     /coded_by="NM_001436448.1:42..1514"
                     /db_xref="GeneID:171305"
                     /db_xref="RGD:621259"
ORIGIN      
        1 mhhckryrsp epdpylsyrw krrrsysreh egrlrypsrr eppprrsrsr shdripyqrr
       61 yrehrdsdty rceerspsfg edcygssrsr hrrrsrergp yrtrkhahhc hkrrtrscss
      121 assrsqqssk rssrsveddk eghlvcrigd wlqeryeivg nlgegtfgkv vecldhargk
      181 sqvalkiirn vgkyreaarl einvlkkike kdkenkflcv lmsdwfnfhg hmciafellg
      241 kntfeflken nfqpyplphv rhmayqlcha lrflhenqlt htdlkpenil fvnsefetly
      301 nehksceeks vkntsirvad fgsatfdheh httivatrhy rppevilelg waqpcdvwsi
      361 gcilfeyyrg ftlfqthenr ehlvmmekil gpipshmihr trkqkyfykg glvwdenssd
      421 gryvkenckp lksymlqdsl ehvqlfdlmr rmlefdpaqr itlaeallhp ffagltpeer
      481 sfhssrnpsr
//
LOCUS       NP_001423381             186 aa            linear   ROD 12-MAR-2025
DEFINITION  methyl-CpG-binding domain protein 3-like 1 [Rattus norvegicus].
ACCESSION   NP_001423381 XP_038936923
VERSION     NP_001423381.1
DBSOURCE    REFSEQ: accession NM_001436452.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_038936923.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1071000.1,
                                           SRR26360181.1516671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..186
                     /product="methyl-CpG-binding domain protein 3-like 1"
                     /calculated_mol_wt=20673
     Region          9..74
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Region          78..166
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     CDS             1..186
                     /gene="Mbd3l1"
                     /coded_by="NM_001436452.1:63..623"
                     /db_xref="GeneID:300389"
                     /db_xref="RGD:1308259"
ORIGIN      
        1 mgktsqrkqc dcenpskpcl stsiplrmsn ytfkrpvtki tshlgnevry yqweetlekp
       61 eqacwqkrlq glqayssage ilstsdlska lkdltprdtd aassiiqans mdprplstlg
      121 ssshlakmip eagpqilcke flvteedisi qerkvkiare rlavaliahk lanetekvrg
      181 srkakv
//
LOCUS       NP_001423369             715 aa            linear   ROD 12-MAR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 11 [Rattus
            norvegicus].
ACCESSION   NP_001423369 XP_063122318
VERSION     NP_001423369.1
DBSOURCE    REFSEQ: accession NM_001436440.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063122318.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.432067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..715
                     /product="interleukin enhancer-binding factor 3 isoform
                     11"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=77763
     Region          101..355
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          411..483
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(416,419..420,423..424,426,440..441,443,445,462..464,
                     467)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          532..603
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(539,541..542,545,558,561..563,567,583..586)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..715
                     /gene="Ilf3"
                     /coded_by="NM_001436440.1:449..2596"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrrpmrif vnddrhvmak hssvyptqee leavqnmvsh teralkavsd
       61 wideqekgns elseaenmdt ppddeskega geqkaehmtr tlrgvmrvgl vakglllkgd
      121 ldlelvllck ekpttalldk vadnlaiqlt tvtedkyeil qsvddaaivi kntkepplsl
      181 tihltspvvr eemekvlage tlsvndppdv ldrqkclaal aslrhakwfq aranglkscv
      241 ivirvlrdlc trvptwgplr gwplellcek sigtanrpmg agealrrvle clasgivmpd
      301 gsgiydpcek eatdaighld rqqreditqs aqhalrlaaf gqlhkvlgmd plpskmpkkp
      361 knenpvdytv qippsttyai tpmkrpmeed geekspskkk kkiqkkeeka eppqamnalm
      421 rlnqlkpglq yklisqtgpv hapiftmsve vdgstfeasg pskktaklhv avkvlqdmgl
      481 ptgaegrdss kgedsaeesd gkpavvappp vveavsnpss vfpsdatteg piltkhgknp
      541 vmelnekrrg lkyelisetg gshdkrfvme vevdgqkfqg agsnkkvaka yaalaalekl
      601 fpdaplalea nkkkrapvpv rggpkfaakp hnpgfgmggp mhneappppn irgrgrggni
      661 rgrgrgrgfg gtnhgggymn agagygsygy ssnsatagys dfftdcygyh dfgas
//
LOCUS       NP_001423378             490 aa            linear   ROD 12-MAR-2025
DEFINITION  dual specificity protein kinase CLK3 [Rattus norvegicus].
ACCESSION   NP_001423378 XP_063120897
VERSION     NP_001423378.1
DBSOURCE    REFSEQ: accession NM_001436449.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Ma,X., Gao,L., Ge,R., Yuan,T., Lin,B. and Zhen,L.
  TITLE     CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 333-342 (2024)
   PUBMED   38438604
  REMARK    GeneRIF: CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Duncan,P.I., Stojdl,D.F., Marius,R.M., Scheit,K.H. and Bell,J.C.
  TITLE     The Clk2 and Clk3 dual-specificity protein kinases regulate the
            intranuclear distribution of SR proteins and influence pre-mRNA
            splicing
  JOURNAL   Exp Cell Res 241 (2), 300-308 (1998)
   PUBMED   9637771
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Nayler,O., Stamm,S. and Ullrich,A.
  TITLE     Characterization and comparison of four serine- and arginine-rich
            (SR) protein kinases
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 693-700 (1997)
   PUBMED   9307018
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Becker,W., Kentrup,H., Heukelbach,J. and Joost,H.G.
  TITLE     cDNA cloning and characterization of rat Clk3, a LAMMER kinase
            predominately expressed in testis
  JOURNAL   Biochim Biophys Acta 1312 (1), 63-67 (1996)
   PUBMED   8679717
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063120897.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3009444.1,
                                           SRR26360181.1155481.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..490
                     /product="dual specificity protein kinase CLK3"
                     /EC_number="2.7.12.1"
                     /calculated_mol_wt=58354
     Region          1..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63117.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Region          142..472
                     /region_name="PKc_CLK3"
                     /note="Catalytic domain of the Dual-specificity protein
                     kinase, CDC-like kinase 3; cd14214"
                     /db_xref="CDD:271116"
     Site            order(162..166,170,184,186,200,220,236..239,242,244..245,
                     283,285,287..288,290,320,323,332,334..337,339,376)
                     /site_type="active"
                     /db_xref="CDD:271116"
     Site            order(162..165,170,184,186,220,236..239,242,245,287..288,
                     290,319..320)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271116"
     Site            order(200,244,283,285,323,332,334..337,339,376)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271116"
     Site            319..339
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271116"
     CDS             1..490
                     /gene="Clk3"
                     /coded_by="NM_001436449.1:137..1609"
                     /db_xref="GeneID:171305"
                     /db_xref="RGD:621259"
ORIGIN      
        1 mhhckryrsp epdpylsyrw krrrsysreh egrlrypsrr eppprrsrsr shdripyqrr
       61 yrehrdsdty rceerspsfg edcygssrsr hrrrsrergp yrtrkhahhc hkrrtrscss
      121 assrsqqssk rssrsveddk eghlvcrigd wlqeryeivg nlgegtfgkv vecldhargk
      181 sqvalkiirn vgkyreaarl einvlkkike kdkenkflcv lmsdwfnfhg hmciafellg
      241 kntfeflken nfqpyplphv rhmayqlcha lrflhenqlt htdlkpenil fvnsefetly
      301 nehksceeks vkntsirvad fgsatfdheh httivatrhy rppevilelg waqpcdvwsi
      361 gcilfeyyrg ftlfqthenr ehlvmmekil gpipshmihr trkqkyfykg glvwdenssd
      421 gryvkenckp lksymlqdsl ehvqlfdlmr rmlefdpaqr itlaeallhp ffagltpeer
      481 sfhssrnpsr
//
LOCUS       NP_001100291            3064 aa            linear   ROD 12-MAR-2025
DEFINITION  serine-protein kinase ATM [Rattus norvegicus].
ACCESSION   NP_001100291 XP_001068795 XP_236275
VERSION     NP_001100291.1
DBSOURCE    REFSEQ: accession NM_001106821.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3064)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   2  (residues 1 to 3064)
  AUTHORS   Cho,S.O., Lim,J.W. and Kim,H.
  TITLE     Oxidative stress induces apoptosis via calpain- and
            caspase-3-mediated cleavage of ATM in pancreatic acinar cells
  JOURNAL   Free Radic Res 54 (11-12), 799-809 (2020)
   PUBMED   31401888
  REMARK    GeneRIF: Oxidative stress induces apoptosis via calpain- and
            caspase-3-mediated cleavage of ATM in pancreatic acinar cells.
REFERENCE   3  (residues 1 to 3064)
  AUTHORS   Uhlemeyer,C., Muller,N., Griess,K., Wessel,C., Schlegel,C.,
            Kuboth,J. and Belgardt,B.F.
  TITLE     ATM and P53 differentially regulate pancreatic beta cell survival
            in Ins1E cells
  JOURNAL   PLoS One 15 (8), e0237669 (2020)
   PUBMED   32810137
  REMARK    GeneRIF: ATM and P53 differentially regulate pancreatic beta cell
            survival in Ins1E cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3064)
  AUTHORS   Zhao,J., Nguyen,L.N.T., Nguyen,L.N., Dang,X., Cao,D., Khanal,S.,
            Schank,M., Thakuri,B.K.C., Ogbu,S.C., Morrison,Z.D., Wu,X.Y.,
            Li,Z., Zou,Y., El Gazzar,M., Ning,S., Wang,L., Moorman,J.P. and
            Yao,Z.Q.
  TITLE     ATM Deficiency Accelerates DNA Damage, Telomere Erosion, and
            Premature T Cell Aging in HIV-Infected Individuals on
            Antiretroviral Therapy
  JOURNAL   Front Immunol 10, 2531 (2019)
   PUBMED   31781094
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3064)
  AUTHORS   Warren,R., Domm,W., Yee,M., Campbell,A., Malone,J., Wright,T.,
            Mayer-Proschel,M. and O'Reilly,M.A.
  TITLE     Ataxia-telangiectasia mutated is required for the development of
            protective immune memory after influenza A virus infection
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 317 (5), L591-L601 (2019)
   PUBMED   31509427
REFERENCE   6  (residues 1 to 3064)
  AUTHORS   Hirao,A., Kong,Y.Y., Matsuoka,S., Wakeham,A., Ruland,J.,
            Yoshida,H., Liu,D., Elledge,S.J. and Mak,T.W.
  TITLE     DNA damage-induced activation of p53 by the checkpoint kinase Chk2
  JOURNAL   Science 287 (5459), 1824-1827 (2000)
   PUBMED   10710310
REFERENCE   7  (residues 1 to 3064)
  AUTHORS   Chong,M.J., Murray,M.R., Gosink,E.C., Russell,H.R., Srinivasan,A.,
            Kapsetaki,M., Korsmeyer,S.J. and McKinnon,P.J.
  TITLE     Atm and Bax cooperate in ionizing radiation-induced apoptosis in
            the central nervous system
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 889-894 (2000)
   PUBMED   10639175
REFERENCE   8  (residues 1 to 3064)
  AUTHORS   Tibbetts,R.S., Brumbaugh,K.M., Williams,J.M., Sarkaria,J.N.,
            Cliby,W.A., Shieh,S.Y., Taya,Y., Prives,C. and Abraham,R.T.
  TITLE     A role for ATR in the DNA damage-induced phosphorylation of p53
  JOURNAL   Genes Dev 13 (2), 152-157 (1999)
   PUBMED   9925639
REFERENCE   9  (residues 1 to 3064)
  AUTHORS   Canman,C.E., Lim,D.S., Cimprich,K.A., Taya,Y., Tamai,K.,
            Sakaguchi,K., Appella,E., Kastan,M.B. and Siliciano,J.D.
  TITLE     Activation of the ATM kinase by ionizing radiation and
            phosphorylation of p53
  JOURNAL   Science 281 (5383), 1677-1679 (1998)
   PUBMED   9733515
REFERENCE   10 (residues 1 to 3064)
  AUTHORS   Xu,Y., Ashley,T., Brainerd,E.E., Bronson,R.T., Meyn,M.S. and
            Baltimore,D.
  TITLE     Targeted disruption of ATM leads to growth retardation, chromosomal
            fragmentation during meiosis, immune defects, and thymic lymphoma
  JOURNAL   Genes Dev 10 (19), 2411-2422 (1996)
   PUBMED   8843194
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473975.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001068795.1, XP_236275.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132261, SAMD00132262
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3064
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..3064
                     /product="serine-protein kinase ATM"
                     /EC_number="2.7.11.1"
                     /note="Ataxia telangiectasia gene mutated in human beings;
                     ataxia telangiectasia mutated homolog"
                     /calculated_mol_wt=348990
     Region          8..165
                     /region_name="TAN"
                     /note="Telomere-length maintenance and DNA damage repair;
                     pfam11640"
                     /db_xref="CDD:463317"
     Region          2103..2497
                     /region_name="FAT"
                     /note="FAT domain; pfam02259"
                     /db_xref="CDD:396714"
     Region          2691..2970
                     /region_name="PIKKc_ATM"
                     /note="Catalytic domain of Ataxia Telangiectasia Mutated;
                     cd05171"
                     /db_xref="CDD:270715"
     Site            order(2701,2703..2705,2707,2723,2725,2728,2763,2775..2778,
                     2783,2883,2885,2896..2897)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270715"
     Site            2875..2883
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270715"
     Site            2897..2919
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270715"
     Region          3034..3063
                     /region_name="FATC"
                     /note="FATC domain; pfam02260"
                     /db_xref="CDD:460514"
     CDS             1..3064
                     /gene="Atm"
                     /coded_by="NM_001106821.1:225..9419"
                     /db_xref="GeneID:300711"
                     /db_xref="RGD:1593265"
ORIGIN      
        1 mslalndlli ccrqlehdra terrkevdkf krliqdpetv qhldrhsdsk qgkylnwdav
       61 frflqkyiqk eteslrtaks nvsastqtsr qkkmqeissl vrffikcank raprlkcqdl
      121 lnyvmdtvkd ssngatygad csnillkdil svrkywcevs qqqwlelfsl yirlylkpsq
      181 dinrvlvari ihavtrgccs qtdglpskfl dlfskaiqya rqeksspgls hilaalnifl
      241 ktlavnfrkr vceigdeilp tllyiwtqhr lndslkevii elihlqiyih hpqgakapee
      301 gayesmkwkr ilynlydllv neishigsrg kyssgsrnia vkenlidlma dvcyqlfnad
      361 trsveisqsy atqrestdys vpckrrkidi gwevikdylq ksqndfdlvp wlqittrlis
      421 kypsslpnce lsplililyq llpqqrrger iphvlrclte valcqgkksn lessqksdll
      481 klwikiwsit frgisseqtq tenfgllgai iqgslveldr efwklftgsa ckpsspsvrc
      541 ltlalsmcvv pdaikmgteq svcdanrsfs vkesimrwll fyqlegdled saepppilqs
      601 nfphlileki lvsltmknsk aamkffqsap eceqhcedte epsfseaeel flqttfdkmd
      661 fltpvkedtv ekfqsrvgfs vhqnlkesld hyllglseql lsnysseits setlvrcssl
      721 lvgvlgcycy mgvitedeay kselfqkaks lmqcagesis lfknktnees rvgslrsvih
      781 lctsclcrht khtlnkiasg fflrlltskl mndiadicks lasctkkpfd ygeehslrdd
      841 dddgdggdgg eslmetqgss stdlfsdysa stvsdandyg enqnavgaan pltadwlsrq
      901 dhllldmlrf lclsvtacqs rtasfrgadi rrkllmlldp stldltkslh lhmylvllkd
      961 lpgkehllpm edvvellqpl slvcslyrrd qdvcktilsn vlhivtnlgq gsvdtestrn
     1021 aqgqfltvmg afwhltkekk cifsvrmalv kclqtllead pyskwailnv kgqdfpvrea
     1081 fpqfladghh hvrmlaagsi srlfqdmrqg dssrslkalp lkfqqtsfns aymiaeagir
     1141 ellcdsqnpd lldeiynrks vlltviavvl hcspicekqa lfalcksvke nglephlvkk
     1201 vlekvsesfg crcledfmas hldylvlewl nlqdakysls sfpftllnym svedfyrscy
     1261 kiliphlvir khfdevksia nqiqrcwksl lidcfpkmlv hilpyfaceg tgdsssaqkr
     1321 etatevydtl kgedflgkqi dqvfisnlpe ivvellmtlh etadsdsgqs pdlcdfsgdl
     1381 dpapnppyfp shvikatfay isschktkfk sileilskip dsyqkillai ceqaaetnnv
     1441 fkkhrilkiy hlfvslllkd iqsglggawa fvlrdviytl ihyinkrssh ftdvslrsfs
     1501 lccdllsrvc rtavthckda lenhlhvivg tliplvdyqe vqeqvldllk ylvidnkdnk
     1561 nlfvtiklld pfpdhvvfkd lrltqqkiky sggpftllee inhflsvsay nplpltrleg
     1621 lkdlrrqleq hkdqmldlvr asqdnpqdgi vvklvvsllq lskmavnqtg erevleavgr
     1681 clgeigpldf stiavqhskd tpytkayglp edrelqwtli mltalnntlv edsvkirsaa
     1741 atclknilat ktghifwenh ktsadpmlty lqpfrasrkk flelpqfvke daleglddvn
     1801 lwvpqseshd iwiktltcaf ldsggiksei lqllkpmcev ktdfcqmvlp ylihdvllqd
     1861 theswrtlls thvrgfftnc fkhssqasrs atpansdses enflrccldk ksqrtmlavv
     1921 dylrrqkrps sgtafedafw ldlnylevak vaqscaahft allyaeiysd kknmdeqekr
     1981 sptfeegsqg ttisslseks keetgislqd llleiyrsig epdslygcgg gkvlqpltri
     2041 rtyeheatwe kalvtydlet tissstrqsg iiqalqnlgl shilsiylkg ldherrewcg
     2101 elqelhyqaa wrnmqwdlct sanqelegts yheslynalq clrnrefstf ydslrharvk
     2161 eveelskgsl esvyslyptl srlqavgele nsgelfsrsv tdrersevyl kwqkhsqllk
     2221 dsdfsfqepl malrtvilei lvqkemensq ggcskdiltk hlvefsvlar tfkntqlper
     2281 aifkikqynp aicgisewhl eeaqvfwakk eqslalsilk qmikkldssf revcneaglk
     2341 glhaeclrvc gnwlaetcle npavimqtyl ekavkvagsy dgdsrelrng qmkaflslar
     2401 fsdtqyqrie nymkssefen kqallkrake evglirehki qtnrytikvq releldecal
     2461 ralkedrkrf lckavenyis cllsgeehdl wvfrlcslwl ensgvsevng mmkrdgmkis
     2521 sykflplmyq laarmgtkmt gglgfhevln nlisrismdh phhtlfiila lanankdefl
     2581 skpetarrgr itknapkess qldedraeaa sriihtirsa rrtmvkdmea lcdayiilan
     2641 ldasqwrnqr kgisipanqp itklknledv vvptmeikvd ptgeyeklvt iksfktefrl
     2701 agglnlpkii dcvgsdgker rqlvkgrddl rqdavmqqvf qmcnmllqrn tetrkrklti
     2761 ctykvvplsq rsgvlewctg tipigeylvn neegahkryr pndlsanqcq kkmmevqkks
     2821 feekyetfmt icqnfepvfr yfcmekfldp avwfekrlay trsvatssiv gyilglgdrh
     2881 vqnilineqs aelvhidlgv afeqgkilpt petvpfrlsr divdgmgitg vegvfrrcce
     2941 ktmevmrssq ealltivevl lydplfdwtm nplkalylqq rpedetdlqs tpsaddqeck
     3001 rslsdtdqsf nkvaervlmr lqeklkgvee gtvlsvggqv nlliqqamdp knlsrlfpgw
     3061 kawv
//
LOCUS       NP_001423406             294 aa            linear   ROD 13-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423406 XP_063121274
VERSION     NP_001423406.1
DBSOURCE    REFSEQ: accession NM_001436477.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121274.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.11603.1,
                                           SRR26643298.45831.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..294
                     /product="mortality factor 4-like protein 1 isoform 2"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=33530
     Region          15..>51
                     /region_name="CD_CSD"
                     /note="CHROMO (CHRromatin Organization Modifier) domains
                     and chromo shadow domains; cl28914"
                     /db_xref="CDD:475127"
     Region          108..283
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..294
                     /gene="Morf4l1"
                     /coded_by="NM_001436477.1:142..1026"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mapkqdpkpk fqegervlcf hgpllyeakc vkvaikdkqv kyfihysgwn kkeqyaegkm
       61 rgaapgkkts glqqknvevk tkknkqktpg ngdggstset pqpprkkrar vdptveneet
      121 fmnrvevkvk ipeelkpwlv ddwdlitrqk qlfylpakkn vdsiledyan ykksrgntdn
      181 keyavnevva gikeyfnvml gtqllykfer pqyaeiladh pdapmsqvyg aphllrlfvr
      241 igamlaytpl dekslallln ylhdflkyla knsatlfsas dyevappeyh rkav
//
LOCUS       NP_001423444            1203 aa            linear   ROD 13-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 38 [Rattus
            norvegicus].
ACCESSION   NP_001423444 XP_063121654
VERSION     NP_001423444.1
DBSOURCE    REFSEQ: accession NM_001436515.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Miotto,B., Chibi,M., Xie,P., Koundrioukoff,S., Moolman-Smook,H.,
            Pugh,D., Debatisse,M., He,F., Zhang,L. and Defossez,P.A.
  TITLE     The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common
            fragile site stability
  JOURNAL   Cell Rep 7 (2), 575-587 (2014)
   PUBMED   24726359
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Filion,G.J., Zhenilo,S., Salozhin,S., Yamada,D., Prokhortchouk,E.
            and Defossez,P.A.
  TITLE     A family of human zinc finger proteins that bind methylated DNA and
            repress transcription
  JOURNAL   Mol Cell Biol 26 (1), 169-181 (2006)
   PUBMED   16354688
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Kiefer,H., Chatail-Hermitte,F., Ravassard,P., Bayard,E., Brunet,I.
            and Mallet,J.
  TITLE     ZENON, a novel POZ Kruppel-like DNA binding protein associated with
            differentiation and/or survival of late postmitotic neurons
  JOURNAL   Mol Cell Biol 25 (5), 1713-1729 (2005)
   PUBMED   15713629
  REMARK    GeneRIF: ZENON is involved in the maintenance of panneuronal
            features and/or in the survival of mature neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121654.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.2113359.1,
                                           SRR26643285.32338.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..1203
                     /product="zinc finger and BTB domain-containing protein
                     38"
                     /note="zenon; zinc finger protein expressed in neurons;
                     zinc finger transcription factor Kaiso"
                     /calculated_mol_wt=135144
     Region          15..128
                     /region_name="BTB_POZ_ZBTB38_CIBZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 38 (ZBTB38); cd18223"
                     /db_xref="CDD:349532"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3; propagated from
                     UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          230..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          299..522
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          308..401
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(343,346,359,363)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          372..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(461,464,477,481)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(466,468,470,472..473,476..477,480,494,496,500..501,
                     504..505,508,522,524,526,528..529,532..533)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          731..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          857..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          895..914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          1019..1039
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1019,1022,1035,1039)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(1024,1026,1028,1030..1031,1034..1035,1038,1052,1054,
                     1058..1059,1062..1063,1066,1080,1082,1084,1086..1087,
                     1090..1091,1094)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1032..1055
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1045..1067
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1047..1067
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1075..1095
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1088..>1106
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1103..1123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1134..1154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1172..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     CDS             1..1203
                     /gene="Zbtb38"
                     /gene_synonym="RGD1310136"
                     /coded_by="NM_001436515.1:195..3806"
                     /db_xref="GeneID:315936"
                     /db_xref="RGD:1310136"
ORIGIN      
        1 mtvmslsrdl kddfhsdtvl silneqrirg ilcdvtiive dtkfkahsnv laasslyfkn
       61 ifwshticis shvlelddlk aevfteilny iysstvvvrr qetvtdlaaa gkrlgisfle
      121 dlsdrnfsns pgpyvvcite kgvvkeekne krheepavtn gpritnafsi ietensnsmf
      181 spldlrasfk kvsdamrtts lcqerasvcp eaepvrtlae hsyavssite ayrsqplreh
      241 dsssssgktg kengealttk akpcrkpktq tqdsdstten mplplvtcpe vnqerspqpa
      301 pilshsepps segdvhfpre denqpsetpg ppaaevpplv yncsccsksf dsstllgahm
      361 qlhkptqdpf vckycnkqft tlnrldrheq icmrsshmpm pggnqpflen yptigqdggs
      421 ftspdslvpe srigelssag salsdadhmv kfvngqmlys cvvckrsyvt lsslrrhanv
      481 hswrrtypch ycnkvfalae yrtrheiwht gerryqcifc letfmtyyil knhqksfhai
      541 dhrlsiskkt angglkptvy pyklyrllpm rckrapyksy rnssyesaqg nrqrnesppd
      601 tfvipnlpss emptlnfqdg rnsltsspai pvetpswqgt ptsakvknae glkwrkqalk
      661 tdlvdsaevs issignsvst tlqaepvcvs sgehsasvis ysgsvpsviv hssqfssvik
      721 hsnaiaclan snhqspsqpv aspslikdsk peadkaskla srpknskekk ktvpcnrgei
      781 teeakyvadl ggssgkttnv veetskiety iakpalpgts tnsnvaplcq itvkigneai
      841 vkrhilgskl fykrgrkpky qmqeetlpre sdpetrgdsp lglcqadcve mseafdevsd
      901 qdstdkpwrp yynykpkkks kqlrkirkvk wrkergsrsp vgrrrypael draemgrrry
      961 paeldrcaev klppdkasee eenkempklq celcdgdkaa gagaegkphq hltlkpyice
     1021 lcakqfqsss tlkmhmrcht gekpyqcktc grrfsvqgnl qkherihlgv keficqycnk
     1081 aftlnetlki herihtgekr yhcqfcfqgf lylstkrnhe rrhvrehdgk gfacfqcpki
     1141 cktaaalrmh qkkhlfktlt kqeetddlch ensdllesqp ctdsedsdqk ddikkpllkm
     1201 sfe
//
LOCUS       NP_001423426            1297 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423426 XP_063121457
VERSION     NP_001423426.1
DBSOURCE    REFSEQ: accession NM_001436497.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1297)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1297)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1297)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121457.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.44544.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1297
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1297
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 3"
                     /calculated_mol_wt=138683
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          392..478
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <683..887
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <982..>1188
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..1297
                     /gene="Nfrkb"
                     /coded_by="NM_001436497.1:393..4286"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deedlsswlp ssparspspa vplrvvptls
      241 ttdmktadki elgdsdlklm lkkhhekrkh qpdhpdlltg dltlsdimtr vnagrkgsla
      301 alydlavlkk kvkekeekkk kkikliksea edlaeplsnt egvptlsqap splaissike
      361 epledikpcl gineisssff sllleillle sqaslpmled rvldwqsspa sslnswfsaa
      421 pnwaelvlpa lqylagesra vpssfspfve fkektqqwkl lgqsqdneke laalfhlwle
      481 tkdqafckqe nedssdamtp vprvrtdyvv rpstgeekrv fqeqeryrys qphkaftfrm
      541 hgfesvvgpv kgvfdketsl nkarehsllr sdrpayvtil slvrdaaarl pngegtraei
      601 cellkdsqfl apdvtstqvn tvvsgaldrl hyekdpcvky digrklwiyl hrdrseeefe
      661 rihqaqaaaa karkalqqkp kppskvkssn kegsvkglsg psepsqmsls dssmpptpvt
      721 pvtpttpalp tpispppvsa vsrsgsttvs epaksssgvl lvssptmpql gtmlspasiq
      781 tppssqttar vvshsssagl pqvrvvaqps lpavsqqsvg paqplpqmpa gpqirvpvta
      841 tqtkvvpqav vatvpvkgqt taasvqrpgp aqtgltvtsl paavspgskt amsspgssap
      901 sasttaviqn vtgqniikqv sitgqlgvkp qtgnsiplta tnfriqgkdv lrlppssitt
      961 dakgqtvlri tpdmmatlak sqvttvkltq dlfgagsgta gkgisatlhv tsnpvhaads
     1021 pakapsasvp ssapagttvv kvtpdlkpte tsssafrlmp algvsvadqk gkntvassea
     1081 kpaatirivq glgvmppkag qtitvaahak qgasvaggsg tvhsstvslp sinatvsktv
     1141 avasgatstp isigtgaptv rqvpvnttvv stsqsgklpt ritvplsvis qpmkgksvvt
     1201 apiikgnlga nlsglgrnii lttmpagakl iagnkpvsfl taqqlqqlqq qgqatqvriq
     1261 tvpashlqqg tasgsskavs tvvvttapsp kqapeqq
//
LOCUS       NP_001423412             777 aa            linear   ROD 13-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423412 XP_006243807
VERSION     NP_001423412.1
DBSOURCE    REFSEQ: accession NM_001436483.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243807.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.598576.1,
                                           SRR26360190.1731741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436483.1:220..2553"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001423416             777 aa            linear   ROD 13-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423416 XP_006243812
VERSION     NP_001423416.1
DBSOURCE    REFSEQ: accession NM_001436487.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243812.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.485240.1,
                                           SRR26360194.42055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436487.1:379..2712"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001423407             361 aa            linear   ROD 13-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423407 XP_017451068
VERSION     NP_001423407.1
DBSOURCE    REFSEQ: accession NM_001436478.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_017451068.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1249460.1,
                                           SRR22399492.1295932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..361
                     /product="mortality factor 4-like protein 1 isoform 3"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=41230
     Region          15..109
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(21..22,26..29,44,46..49,91,93..96,98..100,103..104)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(26,46,49,91)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(43,45..50,52,91..94)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(43,46,50,52,94)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          175..350
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..361
                     /gene="Morf4l1"
                     /coded_by="NM_001436478.1:142..1227"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mapkqdpkpk fqegervlcf hgpllyeakc vkvaikdkqv kyfihysgwn knavrprrse
       61 kslktrediv alfpvpegap svhhplltss wdewvpesrv lkyvdanlqk qrelqkanqe
      121 qyaegkmrga apgkktsglq qknvevktkk nkqktpgngd ggstsetpqp prkkrarvdp
      181 tveneetfmn rvevkvkipe elkpwlvddw dlitrqkqlf ylpakknvds iledyanykk
      241 srgntdnkey avnevvagik eyfnvmlgtq llykferpqy aeiladhpda pmsqvygaph
      301 llrlfvriga mlaytpldek slalllnylh dflkylakns atlfsasdye vappeyhrka
      361 v
//
LOCUS       NP_001423436             991 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423436 XP_063121511
VERSION     NP_001423436.1
DBSOURCE    REFSEQ: accession NM_001436507.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 991)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121511.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.30086.1,
                                           SRR26360186.2001766.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..991
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     4"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=112636
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          163..594
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,546,564)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Region          712..991
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     CDS             1..991
                     /gene="Usp28"
                     /coded_by="NM_001436507.1:105..3080"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnsn prtksenpmv qlfygtflte
      301 gvregkpfcn netfgqyplq vngyhnldec legamvegdi allpsdrsvk ygqerwftkl
      361 ppvltfelsr fefnqslgqp ekihnklefp qviymdrymy kskelirskr esirklkeei
      421 qvlqqkless spkscsqnae gsfsspedal pnsevmngpf tsphsslemp apppaprtvt
      481 deemnfvktc lqrwrseieq diqdlkncis sttqaieqmy cdpllrqvpy rlhavlvheg
      541 qasaghyway iynqprqiwl kyndisvtes sweelerdsy gglrnvsayc lmyindklph
      601 csaeaahges dqtaeveals velrqyiqed nwrfeqevee weeeqsckip qmesspnsss
      661 qdfstsqess aasshgvrcl ssehaviake qtaqaianta hayeksgvea alseafheey
      721 srlyqlaket ptshsdprlq hvlvyffqne apkrvvertl leqfadrnls ydersisimk
      781 vaqaklmeig pedmnmeeyk rwhedyslfr kvsvylltgl elfqkgkyqe alsylvyayq
      841 snagllvkgp rrgvkesvia lyrrkcllel nakaaslfet nddhsvtegi nvmneliipc
      901 ihliinndis kddldaievm rnhwcsylgk diaenlqlcl geflprlldp saeiivlkep
      961 ptirpnspyd lcsrfaavme siqgvstvtv k
//
LOCUS       NP_001011999             323 aa            linear   ROD 13-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001011999 XP_217222
VERSION     NP_001011999.1
DBSOURCE    REFSEQ: accession NM_001011999.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Feb 11, 2005 this sequence version replaced XP_217222.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078910.1, FQ226047.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..323
                     /product="mortality factor 4-like protein 1 isoform 5"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=37070
     Region          15..71
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(21..22,26..29,44,46..49,53,55..58,60..62,65..66)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(26,46,49,53)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(43,45..50,52..56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(43,46,50,52,56)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          77..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU1.1)"
     Region          94..227
                     /region_name="Sufficient for interaction with SIN3A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU1.1)"
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBU8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYU1.1)"
     Region          125..191
                     /region_name="Interaction with RB1-1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU1.1)"
     Region          137..312
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     Region          149..303
                     /region_name="Sufficient for interaction with PHF12.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU1.1)"
     Region          284..305
                     /region_name="Interaction with RB1-2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU1.1)"
     CDS             1..323
                     /gene="Morf4l1"
                     /coded_by="NM_001011999.3:142..1113"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mapkqdpkpk fqegervlcf hgpllyeakc vkvaikdkqv kyfihysgwn knwdewvpes
       61 rvlkyvdanl qkqrelqkan qeqyaegkmr gaapgkktsg lqqknvevkt kknkqktpgn
      121 gdggstsetp qpprkkrarv dptveneetf mnrvevkvki peelkpwlvd dwdlitrqkq
      181 lfylpakknv dsiledyany kksrgntdnk eyavnevvag ikeyfnvmlg tqllykferp
      241 qyaeiladhp dapmsqvyga phllrlfvri gamlaytpld ekslalllny lhdflkylak
      301 nsatlfsasd yevappeyhr kav
//
LOCUS       NP_001423424            1307 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423424 XP_063121452
VERSION     NP_001423424.1
DBSOURCE    REFSEQ: accession NM_001436495.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1307)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1307)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1307)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121452.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1991327.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1307
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1307
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 5"
                     /calculated_mol_wt=139866
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          404..489
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <693..897
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1005..>1183
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..1307
                     /gene="Nfrkb"
                     /coded_by="NM_001436495.1:108..4031"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deeatldlqe kfsfedlssw lpssparsps
      241 pavplrvvpt lsttdmktad kielgdsdlk lmlkkhhekr khqpdhpdll tgdltlsdim
      301 trvnagrkgs laalydlavl kkkvkekeek kkkkikliks eaedlaepls ntegvptlsq
      361 apsplaissi keepledikp clgineisss ffsllleill lesqaslpml edrvldwqss
      421 passlnswfs aapnwaelvl palqylages rvpssfspfv efkektqqwk llgqsqdnek
      481 elaalfhlwl etkdqafckq enedssdamt pvprvtdyvv rpstgeekrv fqeqeryrys
      541 qphkaftfrm hgfesvvgpv kgvfdketsl nkarehsllr sdrpayvtil slvrdaaarl
      601 pngegtraei cellkdsqfl apdvtstqvn tvvsgaldrl hyekdpcvky digrklwiyl
      661 hrdrseeefe rihqaqaaaa karkalqqkp kppskvkssn kegsvkglsg psepsqmsls
      721 dssmpptpvt pvtpttpalp tpispppvsa vsrsgsttvs epaksssgvl lvssptmpql
      781 gtmlspasiq tppssqttar vvshsssagl pqvrvvaqps lpavsqqsvg paqplpqmpa
      841 gpqirvpvta tqtkvvpqav vatvpvkgqt taasvqrpgp aqtgltvtsl paavspgskt
      901 amsspgssap sasttaviqn vtgqniikqv sitgqlgvkp qtgnsiplta tnfriqgkdv
      961 lrlppssitt dakgqtvlri tpdmmatlak sqvttvkltq dlfgagsgta gkgisatlhv
     1021 tsnpvhaads pakapsasvp ssapagttvv kvtpdlkpte tsssafrlmp algvsvadqk
     1081 gkntvassea kpaatirivq glgvmppkag qtitvaahak qgasvaggsg tvhsstvslp
     1141 sinatvsktv avasgatstp isigtgaptv rqvpvnttvv stsqsgklpt ritvplsvis
     1201 qpmkgksvvt apiikgnlga nlsglgrnii lttmpagakl iagnkpvsfl taqqlqqlqq
     1261 qgqatqvriq tvpashlqqg tasgsskavs tvvvttapsp kqapeqq
//
LOCUS       NP_001423448            1203 aa            linear   ROD 13-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 38 [Rattus
            norvegicus].
ACCESSION   NP_001423448 XP_063121650
VERSION     NP_001423448.1
DBSOURCE    REFSEQ: accession NM_001436519.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Miotto,B., Chibi,M., Xie,P., Koundrioukoff,S., Moolman-Smook,H.,
            Pugh,D., Debatisse,M., He,F., Zhang,L. and Defossez,P.A.
  TITLE     The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common
            fragile site stability
  JOURNAL   Cell Rep 7 (2), 575-587 (2014)
   PUBMED   24726359
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Filion,G.J., Zhenilo,S., Salozhin,S., Yamada,D., Prokhortchouk,E.
            and Defossez,P.A.
  TITLE     A family of human zinc finger proteins that bind methylated DNA and
            repress transcription
  JOURNAL   Mol Cell Biol 26 (1), 169-181 (2006)
   PUBMED   16354688
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Kiefer,H., Chatail-Hermitte,F., Ravassard,P., Bayard,E., Brunet,I.
            and Mallet,J.
  TITLE     ZENON, a novel POZ Kruppel-like DNA binding protein associated with
            differentiation and/or survival of late postmitotic neurons
  JOURNAL   Mol Cell Biol 25 (5), 1713-1729 (2005)
   PUBMED   15713629
  REMARK    GeneRIF: ZENON is involved in the maintenance of panneuronal
            features and/or in the survival of mature neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121650.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.46012.1,
                                           SRR26643296.22667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..1203
                     /product="zinc finger and BTB domain-containing protein
                     38"
                     /note="zenon; zinc finger protein expressed in neurons;
                     zinc finger transcription factor Kaiso"
                     /calculated_mol_wt=135144
     Region          15..128
                     /region_name="BTB_POZ_ZBTB38_CIBZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 38 (ZBTB38); cd18223"
                     /db_xref="CDD:349532"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3; propagated from
                     UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          230..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          299..522
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          308..401
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(343,346,359,363)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          372..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(461,464,477,481)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(466,468,470,472..473,476..477,480,494,496,500..501,
                     504..505,508,522,524,526,528..529,532..533)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          731..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          857..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          895..914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          1019..1039
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1019,1022,1035,1039)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(1024,1026,1028,1030..1031,1034..1035,1038,1052,1054,
                     1058..1059,1062..1063,1066,1080,1082,1084,1086..1087,
                     1090..1091,1094)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1032..1055
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1045..1067
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1047..1067
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1075..1095
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1088..>1106
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1103..1123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1134..1154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1172..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     CDS             1..1203
                     /gene="Zbtb38"
                     /gene_synonym="RGD1310136"
                     /coded_by="NM_001436519.1:182..3793"
                     /db_xref="GeneID:315936"
                     /db_xref="RGD:1310136"
ORIGIN      
        1 mtvmslsrdl kddfhsdtvl silneqrirg ilcdvtiive dtkfkahsnv laasslyfkn
       61 ifwshticis shvlelddlk aevfteilny iysstvvvrr qetvtdlaaa gkrlgisfle
      121 dlsdrnfsns pgpyvvcite kgvvkeekne krheepavtn gpritnafsi ietensnsmf
      181 spldlrasfk kvsdamrtts lcqerasvcp eaepvrtlae hsyavssite ayrsqplreh
      241 dsssssgktg kengealttk akpcrkpktq tqdsdstten mplplvtcpe vnqerspqpa
      301 pilshsepps segdvhfpre denqpsetpg ppaaevpplv yncsccsksf dsstllgahm
      361 qlhkptqdpf vckycnkqft tlnrldrheq icmrsshmpm pggnqpflen yptigqdggs
      421 ftspdslvpe srigelssag salsdadhmv kfvngqmlys cvvckrsyvt lsslrrhanv
      481 hswrrtypch ycnkvfalae yrtrheiwht gerryqcifc letfmtyyil knhqksfhai
      541 dhrlsiskkt angglkptvy pyklyrllpm rckrapyksy rnssyesaqg nrqrnesppd
      601 tfvipnlpss emptlnfqdg rnsltsspai pvetpswqgt ptsakvknae glkwrkqalk
      661 tdlvdsaevs issignsvst tlqaepvcvs sgehsasvis ysgsvpsviv hssqfssvik
      721 hsnaiaclan snhqspsqpv aspslikdsk peadkaskla srpknskekk ktvpcnrgei
      781 teeakyvadl ggssgkttnv veetskiety iakpalpgts tnsnvaplcq itvkigneai
      841 vkrhilgskl fykrgrkpky qmqeetlpre sdpetrgdsp lglcqadcve mseafdevsd
      901 qdstdkpwrp yynykpkkks kqlrkirkvk wrkergsrsp vgrrrypael draemgrrry
      961 paeldrcaev klppdkasee eenkempklq celcdgdkaa gagaegkphq hltlkpyice
     1021 lcakqfqsss tlkmhmrcht gekpyqcktc grrfsvqgnl qkherihlgv keficqycnk
     1081 aftlnetlki herihtgekr yhcqfcfqgf lylstkrnhe rrhvrehdgk gfacfqcpki
     1141 cktaaalrmh qkkhlfktlt kqeetddlch ensdllesqp ctdsedsdqk ddikkpllkm
     1201 sfe
//
LOCUS       NP_001423450             446 aa            linear   ROD 13-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423450 XP_006243008
VERSION     NP_001423450.1
DBSOURCE    REFSEQ: accession NM_001436521.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243008.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.44055.1,
                                           SRR26360176.1340131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..446
                     /product="cell adhesion molecule 1 isoform 2 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=44375
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          399..417
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..446
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001436521.1:22..1362"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydttatt epavhgltql pnsaeeldse
      361 dlsdsragee gaigavdhav iggvvavvvf amlclliilg ryfarhkgty ftheakgadd
      421 aadadtaiin aeggqnnsee kkeyfi
//
LOCUS       NP_001012201             476 aa            linear   ROD 13-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001012201 XP_343386
VERSION     NP_001012201.1
DBSOURCE    REFSEQ: accession NM_001012201.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Feb 11, 2005 this sequence version replaced XP_343386.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2204347.1, BC078966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..476
                     /product="cell adhesion molecule 1 isoform 1 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=47463
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     mat_peptide     48..476
                     /product="Cell adhesion molecule 1. /evidence=ECO:0000255.
                     /id=PRO_5004270763"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP5.1)"
                     /calculated_mol_wt=47463
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            409..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Region          429..447
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5M8; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP5.1)"
     CDS             1..476
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001012201.3:22..1452"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydpptti pppttttttt ttttttttil
      361 tiitdttatt epavhgltql pnsaeeldse dlsdsragee gaigavdhav iggvvavvvf
      421 amlclliilg ryfarhkgty ftheakgadd aadadtaiin aeggqnnsee kkeyfi
//
LOCUS       NP_001014115             322 aa            linear   ROD 13-MAR-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP16 [Rattus norvegicus].
ACCESSION   NP_001014115 XP_236347
VERSION     NP_001014115.1
DBSOURCE    REFSEQ: accession NM_001014093.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Yang,D., Wang,Q., Wei,G., Wu,J., Zhu,Y.C., Zhu,Q., Ni,T., Liu,X.
            and Zhu,Y.Z.
  TITLE     Smyd3-PARP16 axis accelerates unfolded protein response and
            vascular aging
  JOURNAL   Aging (Albany NY) 12 (21), 21423-21445 (2020)
   PUBMED   33144524
  REMARK    GeneRIF: Smyd3-PARP16 axis accelerates unfolded protein response
            and vascular aging.
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Vyas,S., Matic,I., Uchima,L., Rood,J., Zaja,R., Hay,R.T., Ahel,I.
            and Chang,P.
  TITLE     Family-wide analysis of poly(ADP-ribose) polymerase activity
  JOURNAL   Nat Commun 5, 4426 (2014)
   PUBMED   25043379
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Jwa,M. and Chang,P.
  TITLE     PARP16 is a tail-anchored endoplasmic reticulum protein required
            for the PERK- and IRE1alpha-mediated unfolded protein response
  JOURNAL   Nat Cell Biol 14 (11), 1223-1230 (2012)
   PUBMED   23103912
  REMARK    Erratum:[Nat Cell Biol. 2013 Jan;15(1):123]
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Di Paola,S., Micaroni,M., Di Tullio,G., Buccione,R. and Di
            Girolamo,M.
  TITLE     PARP16/ARTD15 is a novel endoplasmic-reticulum-associated
            mono-ADP-ribosyltransferase that interacts with, and modifies
            karyopherin-ss1
  JOURNAL   PLoS One 7 (6), e37352 (2012)
   PUBMED   22701565
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 20, 2005 this sequence version replaced XP_236347.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085908.1, SRR26360186.1131707.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..322
                     /product="protein mono-ADP-ribosyltransferase PARP16"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 16; PARP-16;
                     ADP-ribosyltransferase diphtheria toxin-like 15; mono
                     [ADP-ribose] polymerase PARP16"
                     /calculated_mol_wt=36581
     Region          15..90
                     /region_name="ARTD15_N"
                     /note="ARTD15 N-terminal domain; pfam18084"
                     /db_xref="CDD:465641"
     Region          102..273
                     /region_name="PARP"
                     /note="Poly(ADP-ribose) polymerase catalytic domain;
                     pfam00644"
                     /db_xref="CDD:395519"
     Site            193
                     /site_type="other"
                     /note="Nicotinamide-stacking aromate.
                     /evidence=ECO:0000250|UniProtKB:Q8N5Y8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Q4.1)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Q4.1)"
     CDS             1..322
                     /gene="Parp16"
                     /gene_synonym="ARTD15; LRRGT00109; RGD1306243"
                     /coded_by="NM_001014093.2:121..1089"
                     /db_xref="GeneID:315760"
                     /db_xref="RGD:1306243"
ORIGIN      
        1 mqlsnraaar esvsrdvlaa dlrcslfasa lqsykrdsvl rpfpasyarh dckdfealla
       61 dtgrlpnlke llqssrdtdk qtwdlvswil sskiltihsa ekaefekiqq ltgaphtpvp
      121 ipdflfeiey fdpanarfye tkggrdliya fhgsrlenfh siihnglhch lnktslfgeg
      181 tyltsdlsla liysphgrgw qhsllgqtls cvavcevidh pdvkcqtkkk dskeidrsra
      241 rikhseggdv ppkyfvvtnn qllrvkyllv ysqkqpkras sqlswlcshw fmvamslyll
      301 lllivsvtns safqhfwnrl kr
//
LOCUS       NP_001423401            1074 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423401 XP_063121249
VERSION     NP_001423401.1
DBSOURCE    REFSEQ: accession NM_001436472.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121249.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.45269.1,
                                           SRR26643297.29086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1074
                     /product="atos homolog protein A isoform 2"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119393
     Region          877..934
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1016..1073
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1074
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436472.1:430..3654"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 lrttlkhssv wrkhdfhsld gtstrafhpq tglpllsspv pqrktqsgcf dldtsllhlr
      841 slsskssrpc lnieadpgvh ekpflsssap pitslsllgn feesvlnyrl dplgivdgft
      901 aevgasgtfc pthltlpvev sfysvsddna pspymgvitl eslgkrgyrv ppsgtiqvtl
      961 fnpnktvvkm fvvvydlrsm panhqtflrq rtfsvpvkqe mkrsinkenv qhtaqllryl
     1021 ihlrfqssks gkiylhrdvr llfsrksmev dsgaayelks ytesptnpqf sprc
//
LOCUS       NP_001423434            1051 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423434 XP_006243073
VERSION     NP_001423434.1
DBSOURCE    REFSEQ: accession NM_001436505.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1051)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1051)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1051)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243073.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB240643.1, SRR26643299.35001.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1051
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=119188
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          163..654
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,606,624)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Region          772..1051
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     CDS             1..1051
                     /gene="Usp28"
                     /coded_by="NM_001436505.1:105..3260"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnsn prtksenpmv qlfygtflte
      301 gvregkpfcn netfgqyplq vngyhnldec legamvegdi allpsdrsvk ygqerwftkl
      361 ppvltfelsr fefnqslgqp ekihnklefp qviymdrymy kskelirskr esirklkeei
      421 qvlqqklery vkygsgpsrf plpdmlkyvi efastkpase sclsgsvehm tlplpsvhcp
      481 isdltakess spkscsqnae gsfsspedal pnsevmngpf tsphsslemp apppaprtvt
      541 deemnfvktc lqrwrseieq diqdlkncis sttqaieqmy cdpllrqvpy rlhavlvheg
      601 qasaghyway iynqprqiwl kyndisvtes sweelerdsy gglrnvsayc lmyindklph
      661 csaeaahges dqtaeveals velrqyiqed nwrfeqevee weeeqsckip qmesspnsss
      721 qdfstsqess aasshgvrcl ssehaviake qtaqaianta hayeksgvea alseafheey
      781 srlyqlaket ptshsdprlq hvlvyffqne apkrvvertl leqfadrnls ydersisimk
      841 vaqaklmeig pedmnmeeyk rwhedyslfr kvsvylltgl elfqkgkyqe alsylvyayq
      901 snagllvkgp rrgvkesvia lyrrkcllel nakaaslfet nddhsvtegi nvmneliipc
      961 ihliinndis kddldaievm rnhwcsylgk diaenlqlcl geflprlldp saeiivlkep
     1021 ptirpnspyd lcsrfaavme siqgvstvtv k
//
LOCUS       NP_001423409             235 aa            linear   ROD 13-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423409 XP_063121276
VERSION     NP_001423409.1
DBSOURCE    REFSEQ: accession NM_001436480.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121276.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2330348.1,
                                           SRR26643293.46684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..235
                     /product="mortality factor 4-like protein 1 isoform 6"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=26619
     Region          49..224
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..235
                     /gene="Morf4l1"
                     /coded_by="NM_001436480.1:313..1020"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mrgaapgkkt sglqqknvev ktkknkqktp gngdggstse tpqpprkkra rvdptvenee
       61 tfmnrvevkv kipeelkpwl vddwdlitrq kqlfylpakk nvdsiledya nykksrgntd
      121 nkeyavnevv agikeyfnvm lgtqllykfe rpqyaeilad hpdapmsqvy gaphllrlfv
      181 rigamlaytp ldekslalll nylhdflkyl aknsatlfsa sdyevappey hrkav
//
LOCUS       NP_001423452             417 aa            linear   ROD 13-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001423452 XP_006243010
VERSION     NP_001423452.1
DBSOURCE    REFSEQ: accession NM_001436523.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.346839.1,
                                           SRR26360172.1934189.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..417
                     /product="cell adhesion molecule 1 isoform 4 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=41351
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          370..388
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..417
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001436523.1:22..1275"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydsrage egaigavdha viggvvavvv
      361 famlclliil gryfarhkgt yftheakgad daadadtaii naeggqnnse ekkeyfi
//
LOCUS       NP_001423451             458 aa            linear   ROD 13-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001423451 XP_006243006
VERSION     NP_001423451.1
DBSOURCE    REFSEQ: accession NM_001436522.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243006.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2151422.1,
                                           SRR26360172.682824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..458
                     /product="cell adhesion molecule 1 isoform 3 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=45563
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          411..429
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..458
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001436522.1:22..1398"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydpptti pppttttttt ttttttttil
      361 tiitdttatt epavhdsrag eegaigavdh aviggvvavv vfamlcllii lgryfarhkg
      421 tyftheakga ddaadadtai inaeggqnns eekkeyfi
//
LOCUS       NP_001423408             336 aa            linear   ROD 13-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423408 XP_063121272
VERSION     NP_001423408.1
DBSOURCE    REFSEQ: accession NM_001436479.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121272.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.476268.1,
                                           SRR26643296.22625.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..336
                     /product="mortality factor 4-like protein 1 isoform 4"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=38643
     Region          15..84
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(21..22,26..29,57,59..62,66,68..71,73..75,78..79)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(26,59,62,66)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(56,58..63,65..69)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(56,59,63,65,69)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          150..325
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..336
                     /gene="Morf4l1"
                     /coded_by="NM_001436479.1:142..1152"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mapkqdpkpk fqegervlcf hgpllyeakv wnllsfekvt kkcvkvaikd kqvkyfihys
       61 gwnknwdewv pesrvlkyvd anlqkqrelq kanqeqyaeg kmrgaapgkk tsglqqknve
      121 vktkknkqkt pgngdggsts etpqpprkkr arvdptvene etfmnrvevk vkipeelkpw
      181 lvddwdlitr qkqlfylpak knvdsiledy anykksrgnt dnkeyavnev vagikeyfnv
      241 mlgtqllykf erpqyaeila dhpdapmsqv ygaphllrlf vrigamlayt pldekslall
      301 lnylhdflky laknsatlfs asdyevappe yhrkav
//
LOCUS       NP_001363879            1441 aa            linear   ROD 13-MAR-2025
DEFINITION  protein turtle homolog B isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001363879 XP_006226409 XP_006242801
VERSION     NP_001363879.1
DBSOURCE    REFSEQ: accession NM_001376950.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1441)
  AUTHORS   Woo,J., Kwon,S.K., Nam,J., Choi,S., Takahashi,H., Krueger,D.,
            Park,J., Lee,Y., Bae,J.Y., Lee,D., Ko,J., Kim,H., Kim,M.H.,
            Bae,Y.C., Chang,S., Craig,A.M. and Kim,E.
  TITLE     The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM
            to promote inhibitory synapse development
  JOURNAL   J Cell Biol 201 (6), 929-944 (2013)
   PUBMED   23751499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Dec 5, 2019 this sequence version replaced
            XP_006242801.1, XP_006226409.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1441
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1441
                     /product="protein turtle homolog B isoform 2 precursor"
                     /note="protein turtle homolog B"
                     /calculated_mol_wt=155782
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1881
     Region          41..115
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          59..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          139..225
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          157..161
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          170..174
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          191..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          205..210
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..221
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          228..307
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          336..410
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          342..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          355..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          380..384
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          394..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          407..410
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          429..505
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          438..442
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          451..455
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          471..475
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          485..490
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          <490..>735
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          498..501
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          510..605
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(510,578,593)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(594..595,597..598)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            727..747
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          762..821
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          <898..1246
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          918..1044
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          1111..1332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1140
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9PZ19; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PZ19; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     CDS             1..1441
                     /gene="Igsf9b"
                     /gene_synonym="RGD1564717"
                     /coded_by="NM_001376950.2:229..4554"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:315510"
                     /db_xref="RGD:1564717"
ORIGIN      
        1 miwyvatlia svistrglva qvahglreep efvtarageg vvlrcdvihp vtgqpppyvv
       61 ewfkfgvpip ifikfgyypp hvdpeyagra slhdkaslrl eqvrsedqgw yeckvlmldq
      121 qydtfhngsw vhltinappt ftetppqyie akeggsitmt ctafgnpkpi vtwlkegtll
      181 sasgkyqvsd gsltvtsvsr edrgaytcra ysiqgeavht thllvqgppf ivsppenitv
      241 nisqdalltc raeaypgnlt ytwywqdenv yfqndlklrv rilidgtlii frvkpedagk
      301 ytcvpsnslg rspsasaylt vqyparvlnm ppviyvpvgi hgyircpvda eppatvvkwn
      361 kdgrplqvek nlgwtlmedg sirieeatee algtytcvpy ntlgtmgqsa parlvlkdpp
      421 yftvlpgwey rqeagrelli pcaaagdpfp vitwrkvgkp srskhnalps gslqfralsk
      481 edhgewecva tnvvtsitas thltvigtsp hapgsvrvhv smttanvswe pgydggyeqt
      541 fsvwygplmk raqfgphdwl slsvplgpsw llvdslepet ayqfsvlaqn rlgtsafsev
      601 vtvntlafpv ttpeplvlvt pprcltanrt qqgvllswlp panhsfpidr yimefrvger
      661 wemlddaipg tdgeffakdl sqdtwyefrv lavmqdlise psniagvsst difpqpdltd
      721 dglarpvlag ivaticflaa ailfstlaac fvnkqrkrkl krkkdpplsi thcrkslesp
      781 lssgkvspes irtlrapses sddqgqpaak rmlsptreke lslykktkra issrkysvak
      841 aeaeaeattp ielisrgpdg rfvmgpseme psvkgrrieg fpfaeetdmy pefrqsdeen
      901 edplvptsva alkpqltpms ssqdsylppp aysprfqprg legpsglggr lqatgqarpp
      961 aprpfqhgqy ygylsssspg evepppfymp evgsplssvm sspplhtegp fghptipeen
     1021 genasnstlp ltqtptggrs pepwgrpefp fggletpamm fphqlhpcdv aeslqpkpcl
     1081 prglppaplq vpaaypgmls leapkgwvgk spgrgpipap patkwqerpm qplvsqgqlr
     1141 htsqgmgipv lpypepaepg ghggpstfgl dtrwyepqpr prpsprqarr aepslhqvvl
     1201 qpsrlspltq splssrtgsp elaararprp gllqqaemse itlqppaavs fsrkstpsst
     1261 gspsqssrsg spsyrptmgf ttlatgypsp ppgpappapg dnldvfgqtp sprrmgeepl
     1321 rpeppttlpt sgilppapgn aavperleal ryqrikkpkk sskgsskskk rsdgsasqdq
     1381 qlpnsqvlwp deavclrkkk rhsrpdpfar lsdlchrqlp edqtailnsv dhddpghatl
     1441 l
//
LOCUS       NP_001423402            1081 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423402 XP_038937070
VERSION     NP_001423402.1
DBSOURCE    REFSEQ: accession NM_001436473.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937070.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212313.1, SRR26643287.20622.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1081
                     /product="atos homolog protein A isoform 4"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=120140
     Region          884..941
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1023..1080
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1081
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436473.1:125..3370"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mvfsgnkglr rqdaldeyfe ydaeeflvsl allitegrtp ecsvkgraes fhcppaqsrf
       61 pgaarhecsd klaqcrqarr trsevtllwk nnlpimvevm llpdccysde gpstegtdln
      121 dpaikqdall lerwilepvp rqngdrfiee kalllavrsf vffsqlsawl svshgaiprn
      181 ilyrisaadv dlqwsfsqtp tehvfpvpnv shnvalkvsv qslprqahyp vltcsihtni
      241 glyekriqeq elracqhrgp geveyrcpss sqslcskhtw tmapvsalhv rsgmppeyta
      301 airnvrlcpg tgsksdngtp qasvlgfsgt gevrsqeasv rtfkslsvid ssvsscqssr
      361 qpvgepnpli dsliqdrqev iariaqhlih cdpsssrmse lpfntpests lspklhpvsq
      421 esgysrrcke afsvsfgspe fgspgdskeg kvkekletrq getcashspy prqpageanp
      481 ligslllerq dviariaqhl ehidptahip rpafskhdsn sipskvfrss fhdktmlkkd
      541 renvsvsath tevsllgdrg dgkspkpskc frsfknspqe kslkpeesaq hqnhpddith
      601 tarqellnka aglltssnss lcnesslali grlestsckl qlrkqemshe tekqclhcns
      661 idkqictnkc tekikdensp gslshlqcde srgidpkikv tmlempdyln kyktncsnkd
      721 skrsktceqn iqlgtenyls edtegsksti sdqlkteqee nkdsvagkpp svkhclstse
      781 rlknadmlrt tlkhssvwrk hdfhsldgts trafhpqtgl pllsspvpqr ktqsgcfdld
      841 tsllhlrsls skssrpclni eadpgvhekp flsssappit slsllgnfee svlnyrldpl
      901 givdgftaev gasgtfcpth ltlpvevsfy svsddnapsp ymgvitlesl gkrgyrvpps
      961 gtiqvtlfnp nktvvkmfvv vydlrsmpan hqtflrqrtf svpvkqemkr sinkenvqht
     1021 aqllrylihl rfqssksgki ylhrdvrllf srksmevdsg aayelksyte sptnpqfspr
     1081 c
//
LOCUS       NP_001423437            1083 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423437 XP_006243071
VERSION     NP_001423437.1
DBSOURCE    REFSEQ: accession NM_001436508.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243071.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.22795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1083
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     5"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=122509
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          163..594
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,546,564)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Region          804..1083
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     CDS             1..1083
                     /gene="Usp28"
                     /coded_by="NM_001436508.1:105..3356"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnsn prtksenpmv qlfygtflte
      301 gvregkpfcn netfgqyplq vngyhnldec legamvegdi allpsdrsvk ygqerwftkl
      361 ppvltfelsr fefnqslgqp ekihnklefp qviymdrymy kskelirskr esirklkeei
      421 qvlqqkless spkscsqnae gsfsspedal pnsevmngpf tsphsslemp apppaprtvt
      481 deemnfvktc lqrwrseieq diqdlkncis sttqaieqmy cdpllrqvpy rlhavlvheg
      541 qasaghyway iynqprqiwl kyndisvtes sweelerdsy gglrnvsayc lmyindklph
      601 csaeaahges dqtaeveals velrqyiqed nwrfeqevee weeeqsckip qmesspnsss
      661 qdfstsqess aasshgvrcl ssehaviake qtaqaianta hayeksgvea alsehkeaep
      721 ekpqetnlae qseqaaevkd teaaappnse vseveipsvg rilvrsdadg ydeevmlspa
      781 mqgvllaiak arqtfdrdgs eaglikafhe eysrlyqlak etptshsdpr lqhvlvyffq
      841 neapkrvver tlleqfadrn lsydersisi mkvaqaklme igpedmnmee ykrwhedysl
      901 frkvsvyllt glelfqkgky qealsylvya yqsnagllvk gprrgvkesv ialyrrkcll
      961 elnakaaslf etnddhsvte ginvmnelii pcihliinnd iskddldaie vmrnhwcsyl
     1021 gkdiaenlql clgeflprll dpsaeiivlk epptirpnsp ydlcsrfaav mesiqgvstv
     1081 tvk
//
LOCUS       NP_001423435            1083 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423435 XP_006243070
VERSION     NP_001423435.1
DBSOURCE    REFSEQ: accession NM_001436506.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243070.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.44077.1,
                                           SRR26643290.29169.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1083
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     3"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=122558
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          60..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          163..654
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,606,624)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          483..539
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5I043; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          703..728
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          804..1083
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     Site            1054
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     CDS             1..1083
                     /gene="Usp28"
                     /coded_by="NM_001436506.1:105..3356"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnsn prtksenpmv qlfygtflte
      301 gvregkpfcn netfgqyplq vngyhnldec legamvegdi allpsdrsvk ygqerwftkl
      361 ppvltfelsr fefnqslgqp ekihnklefp qviymdrymy kskelirskr esirklkeei
      421 qvlqqklery vkygsgpsrf plpdmlkyvi efastkpase sclsgsvehm tlplpsvhcp
      481 isdltakess spkscsqnae gsfsspedal pnsevmngpf tsphsslemp apppaprtvt
      541 deemnfvktc lqrwrseieq diqdlkncis sttqaieqmy cdpllrqvpy rlhavlvheg
      601 qasaghyway iynqprqiwl kyndisvtes sweelerdsy gglrnvsayc lmyindklph
      661 csaeaahges dqtaeveals velrqyiqed nwrfeqevee weeeqsckip qmesspnsss
      721 qdfstsqess aasshgvrcl ssehaviake qtaqaianta hayeksgvea alsevmlspa
      781 mqgvllaiak arqtfdrdgs eaglikafhe eysrlyqlak etptshsdpr lqhvlvyffq
      841 neapkrvver tlleqfadrn lsydersisi mkvaqaklme igpedmnmee ykrwhedysl
      901 frkvsvyllt glelfqkgky qealsylvya yqsnagllvk gprrgvkesv ialyrrkcll
      961 elnakaaslf etnddhsvte ginvmnelii pcihliinnd iskddldaie vmrnhwcsyl
     1021 gkdiaenlql clgeflprll dpsaeiivlk epptirpnsp ydlcsrfaav mesiqgvstv
     1081 tvk
//
LOCUS       NP_001423425            1308 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423425 XP_063121449
VERSION     NP_001423425.1
DBSOURCE    REFSEQ: accession NM_001436496.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1308)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1308)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1308)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121449.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2154299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1308
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1308
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 2"
                     /calculated_mol_wt=140022
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          404..489
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <694..898
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1006..>1184
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..1308
                     /gene="Nfrkb"
                     /coded_by="NM_001436496.1:393..4319"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deeatldlqe kfsfedlssw lpssparsps
      241 pavplrvvpt lsttdmktad kielgdsdlk lmlkkhhekr khqpdhpdll tgdltlsdim
      301 trvnagrkgs laalydlavl kkkvkekeek kkkkikliks eaedlaepls ntegvptlsq
      361 apsplaissi keepledikp clgineisss ffsllleill lesqaslpml edrvldwqss
      421 passlnswfs aapnwaelvl palqylages rvpssfspfv efkektqqwk llgqsqdnek
      481 elaalfhlwl etkdqafckq enedssdamt pvprvrtdyv vrpstgeekr vfqeqeryry
      541 sqphkaftfr mhgfesvvgp vkgvfdkets lnkarehsll rsdrpayvti lslvrdaaar
      601 lpngegtrae icellkdsqf lapdvtstqv ntvvsgaldr lhyekdpcvk ydigrklwiy
      661 lhrdrseeef erihqaqaaa akarkalqqk pkppskvkss nkegsvkgls gpsepsqmsl
      721 sdssmpptpv tpvtpttpal ptpispppvs avsrsgsttv sepaksssgv llvssptmpq
      781 lgtmlspasi qtppssqtta rvvshsssag lpqvrvvaqp slpavsqqsv gpaqplpqmp
      841 agpqirvpvt atqtkvvpqa vvatvpvkgq ttaasvqrpg paqtgltvts lpaavspgsk
      901 tamsspgssa psasttaviq nvtgqniikq vsitgqlgvk pqtgnsiplt atnfriqgkd
      961 vlrlppssit tdakgqtvlr itpdmmatla ksqvttvklt qdlfgagsgt agkgisatlh
     1021 vtsnpvhaad spakapsasv pssapagttv vkvtpdlkpt etsssafrlm palgvsvadq
     1081 kgkntvasse akpaatiriv qglgvmppka gqtitvaaha kqgasvaggs gtvhsstvsl
     1141 psinatvskt vavasgatst pisigtgapt vrqvpvnttv vstsqsgklp tritvplsvi
     1201 sqpmkgksvv tapiikgnlg anlsglgrni ilttmpagak liagnkpvsf ltaqqlqqlq
     1261 qqgqatqvri qtvpashlqq gtasgsskav stvvvttaps pkqapeqq
//
LOCUS       NP_001423417             777 aa            linear   ROD 13-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423417 XP_063121320
VERSION     NP_001423417.1
DBSOURCE    REFSEQ: accession NM_001436488.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121320.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1808673.1,
                                           SRR26360176.1190171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436488.1:503..2836"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001030114             453 aa            linear   ROD 13-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 44 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001030114 XP_343367
VERSION     NP_001030114.1
DBSOURCE    REFSEQ: accession NM_001034942.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 21, 2005 this sequence version replaced XP_343367.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.31088.1, BC104680.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..453
                     /product="zinc finger and BTB domain-containing protein 44
                     isoform 1"
                     /note="zinc finger and BTB domain-containing protein 44;
                     BTB/POZ domain-containing protein 15; BTB (POZ) domain
                     containing 15"
                     /calculated_mol_wt=50146
     Region          15..130
                     /region_name="BTB_POZ_ZBTB44"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 44 (ZBTB44); cd18228"
                     /db_xref="CDD:349537"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCP5; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          203..>322
                     /region_name="pgaA"
                     /note="outer membrane protein PgaA; Provisional; PRK10049"
                     /db_xref="CDD:236644"
     Region          241..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          295..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          336..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          399..421
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..438
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..453
                     /gene="Zbtb44"
                     /gene_synonym="Btbd15; RGD1308984"
                     /coded_by="NM_001034942.3:312..1673"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:363035"
                     /db_xref="RGD:1308984"
ORIGIN      
        1 mgvktfthss sshsqemlgk lnmlrndghf cditirvqdr ifrahkvvla acsdffrtkl
       61 vgqtedenkn vldlhhvtvt gfiplleyay tatlsinten iidvlaaasy mqmfsvastc
      121 sefmkssilw ntpnsqpekg ldagqenssn cnftsrdgsi spvssecsav ertipvcres
      181 rrkrksyivm spespvkcst qtnspqvlns sasyaenrnq pvdsslafpw tfpfgidrri
      241 qpekakqaen trtlelpgps eagrrmadyv tcestkttlp lgteedvrvk verlsdeevh
      301 eevsqpvsas qsslsdqqtv pgsepvqedl lispqsssig svdegvtegl ptlqstsstn
      361 ahadeddrle nvqypyqlyi apstssterp spngpdrpfq cptcgvrftr iqnlkqhmli
      421 hsgikpfqcd ccgkkftray slkmhrlkhe vis
//
LOCUS       NP_001423421            1308 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423421 XP_063121448
VERSION     NP_001423421.1
DBSOURCE    REFSEQ: accession NM_001436492.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1308)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1308)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1308)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121448.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2727970.1,
                                           SRR26643295.31140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1308
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1308
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 2"
                     /calculated_mol_wt=140022
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          404..489
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <694..898
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1006..>1184
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..1308
                     /gene="Nfrkb"
                     /coded_by="NM_001436492.1:108..4034"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deeatldlqe kfsfedlssw lpssparsps
      241 pavplrvvpt lsttdmktad kielgdsdlk lmlkkhhekr khqpdhpdll tgdltlsdim
      301 trvnagrkgs laalydlavl kkkvkekeek kkkkikliks eaedlaepls ntegvptlsq
      361 apsplaissi keepledikp clgineisss ffsllleill lesqaslpml edrvldwqss
      421 passlnswfs aapnwaelvl palqylages rvpssfspfv efkektqqwk llgqsqdnek
      481 elaalfhlwl etkdqafckq enedssdamt pvprvrtdyv vrpstgeekr vfqeqeryry
      541 sqphkaftfr mhgfesvvgp vkgvfdkets lnkarehsll rsdrpayvti lslvrdaaar
      601 lpngegtrae icellkdsqf lapdvtstqv ntvvsgaldr lhyekdpcvk ydigrklwiy
      661 lhrdrseeef erihqaqaaa akarkalqqk pkppskvkss nkegsvkgls gpsepsqmsl
      721 sdssmpptpv tpvtpttpal ptpispppvs avsrsgsttv sepaksssgv llvssptmpq
      781 lgtmlspasi qtppssqtta rvvshsssag lpqvrvvaqp slpavsqqsv gpaqplpqmp
      841 agpqirvpvt atqtkvvpqa vvatvpvkgq ttaasvqrpg paqtgltvts lpaavspgsk
      901 tamsspgssa psasttaviq nvtgqniikq vsitgqlgvk pqtgnsiplt atnfriqgkd
      961 vlrlppssit tdakgqtvlr itpdmmatla ksqvttvklt qdlfgagsgt agkgisatlh
     1021 vtsnpvhaad spakapsasv pssapagttv vkvtpdlkpt etsssafrlm palgvsvadq
     1081 kgkntvasse akpaatiriv qglgvmppka gqtitvaaha kqgasvaggs gtvhsstvsl
     1141 psinatvskt vavasgatst pisigtgapt vrqvpvnttv vstsqsgklp tritvplsvi
     1201 sqpmkgksvv tapiikgnlg anlsglgrni ilttmpagak liagnkpvsf ltaqqlqqlq
     1261 qqgqatqvri qtvpashlqq gtasgsskav stvvvttaps pkqapeqq
//
LOCUS       NP_001423395            1057 aa            linear   ROD 13-MAR-2025
DEFINITION  IQ domain-containing protein H isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423395 XP_017451052
VERSION     NP_001423395.1
DBSOURCE    REFSEQ: accession NM_001436466.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_017451052.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1383106.1,
                                           SRR26643293.45839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1057
                     /product="IQ domain-containing protein H isoform 2"
                     /note="IQ domain-containing protein H"
                     /calculated_mol_wt=120475
     Region          420..447
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1057
                     /gene="Iqch"
                     /gene_synonym="RGD1310670"
                     /coded_by="NM_001436466.1:66..3239"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300776"
                     /db_xref="RGD:1310670"
ORIGIN      
        1 maqaqelndp igsiliqvhg dlhqlkekli qfsaeetrdp ldiqnletai qrtetglkih
       61 ierylgivnq evimtpvksl dspinskwai ptvidqksfi fpmapdklwg lqkhrgslpr
      121 gftrakpkve lnkkimqdpe nmhhraavnv sygislprik qrkahdkvrr vrkgstisnl
      181 tvlpsshrtd phfipipvlq kdaskgilsm ierglippaa ritfqnppik pqalplhsfd
      241 ehrkvsitas fpiahkprla sekveesqqk qkakvlthls teehslpvtg kdkrsrgqps
      301 rkstrittps rirrspwdyi lpvyngsvdr aapdfiafkt rykliwgsif sfleqiekfl
      361 kdyaiseakv rgkslvsllp efelnnkltk tdvlavlenp lhiqmllnlp gqrfkgrdgr
      421 teaavkiqat wksykartsf isyrqkkwas gvialawllh chktrlkriv eesrqrhldn
      481 frirakhlaa nwsrirtsrr tiihipsldv nvnviyvcss pmndelklyy kkllslqaav
      541 ksgyygdrsd lqnrfriitp eavniftkhh mclathlmys pkaikriknl iqgeeayivg
      601 gilhrddlav admlnvpila sepelvhlys gksgskrifd nanvpmppgv ydiytyqqli
      661 eqlsqlvtdn lgirrwvfkm nmefggngta fcdipshlqc ykwvvkesnr fgpedwkkkw
      721 aqesalmkis eelagvlaqh vqlvnekqfp twrkflhmfl tqggiieayp padsitnltv
      781 dmliepdgev rvlsmgdqfh adgpfissgt tmpqtsvdpq vlnslclrig nickekdvvg
      841 yfsidlvtfi dpstleqqvw ttglnlsysd qlamtqltly ltngylncsl stlevprfke
      901 daerekkrls iqaelapets ryavmstqlk hdnlslifyy vflqmckahg igydledrqg
      961 tvfilyeslk ryklgmitig vdlqgalmtf arnlfiihqe isapdmqget nfkttiddie
     1021 tilgvteenk mifagekrrk eeeeslyepv eiytktv
//
LOCUS       NP_001423427            1296 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423427 XP_063121460
VERSION     NP_001423427.1
DBSOURCE    REFSEQ: accession NM_001436498.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1296)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1296)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1296)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121460.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1703310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1296
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 4"
                     /calculated_mol_wt=138527
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          392..478
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <682..886
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <981..>1187
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..1296
                     /gene="Nfrkb"
                     /coded_by="NM_001436498.1:393..4283"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deedlsswlp ssparspspa vplrvvptls
      241 ttdmktadki elgdsdlklm lkkhhekrkh qpdhpdlltg dltlsdimtr vnagrkgsla
      301 alydlavlkk kvkekeekkk kkikliksea edlaeplsnt egvptlsqap splaissike
      361 epledikpcl gineisssff sllleillle sqaslpmled rvldwqsspa sslnswfsaa
      421 pnwaelvlpa lqylagesra vpssfspfve fkektqqwkl lgqsqdneke laalfhlwle
      481 tkdqafckqe nedssdamtp vprvtdyvvr pstgeekrvf qeqeryrysq phkaftfrmh
      541 gfesvvgpvk gvfdketsln karehsllrs drpayvtils lvrdaaarlp ngegtraeic
      601 ellkdsqfla pdvtstqvnt vvsgaldrlh yekdpcvkyd igrklwiylh rdrseeefer
      661 ihqaqaaaak arkalqqkpk ppskvkssnk egsvkglsgp sepsqmslsd ssmpptpvtp
      721 vtpttpalpt pispppvsav srsgsttvse paksssgvll vssptmpqlg tmlspasiqt
      781 ppssqttarv vshsssaglp qvrvvaqpsl pavsqqsvgp aqplpqmpag pqirvpvtat
      841 qtkvvpqavv atvpvkgqtt aasvqrpgpa qtgltvtslp aavspgskta msspgssaps
      901 asttaviqnv tgqniikqvs itgqlgvkpq tgnsipltat nfriqgkdvl rlppssittd
      961 akgqtvlrit pdmmatlaks qvttvkltqd lfgagsgtag kgisatlhvt snpvhaadsp
     1021 akapsasvps sapagttvvk vtpdlkptet sssafrlmpa lgvsvadqkg kntvasseak
     1081 paatirivqg lgvmppkagq titvaahakq gasvaggsgt vhsstvslps inatvsktva
     1141 vasgatstpi sigtgaptvr qvpvnttvvs tsqsgklptr itvplsvisq pmkgksvvta
     1201 piikgnlgan lsglgrniil ttmpagakli agnkpvsflt aqqlqqlqqq gqatqvriqt
     1261 vpashlqqgt asgsskavst vvvttapspk qapeqq
//
LOCUS       NP_001423413             777 aa            linear   ROD 13-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423413 XP_006243811
VERSION     NP_001423413.1
DBSOURCE    REFSEQ: accession NM_001436484.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1769952.1,
                                           SRR26643292.35543.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436484.1:172..2505"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001037690             647 aa            linear   ROD 13-MAR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001037690 XP_001056390 XP_001066592 XP_001066806 XP_213729
VERSION     NP_001037690.1
DBSOURCE    REFSEQ: accession NM_001044225.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Louder,R.K., He,Y., Lopez-Blanco,J.R., Fang,J., Chacon,P. and
            Nogales,E.
  TITLE     Structure of promoter-bound TFIID and model of human pre-initiation
            complex assembly
  JOURNAL   Nature 531 (7596), 604-609 (2016)
   PUBMED   27007846
  REMARK    Erratum:[Nature. 2016 Aug 4;536(7614):112. doi:
            10.1038/nature17984. PMID: 27096372]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Malkowska,M., Kokoszynska,K., Rychlewski,L. and Wyrwicz,L.
  TITLE     Structural bioinformatics of the general transcription factor TFIID
  JOURNAL   Biochimie 95 (4), 680-691 (2013)
   PUBMED   23146842
  REMARK    Review article
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Kamileri,I., Karakasilioti,I., Sideri,A., Kosteas,T., Tatarakis,A.,
            Talianidis,I. and Garinis,G.A.
  TITLE     Defective transcription initiation causes postnatal growth failure
            in a mouse model of nucleotide excision repair (NER) progeria
  JOURNAL   Proc Natl Acad Sci U S A 109 (8), 2995-3000 (2012)
   PUBMED   22323595
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Wilhelm,E., Kornete,M., Targat,B., Vigneault-Edwards,J.,
            Frontini,M., Tora,L., Benecke,A. and Bell,B.
  TITLE     TAF6delta orchestrates an apoptotic transcriptome profile and
            interacts functionally with p53
  JOURNAL   BMC Mol Biol 11, 10 (2010)
   PUBMED   20096117
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Tatarakis,A., Margaritis,T., Martinez-Jimenez,C.P., Kouskouti,A.,
            Mohan,W.S. 2nd, Haroniti,A., Kafetzopoulos,D., Tora,L. and
            Talianidis,I.
  TITLE     Dominant and redundant functions of TFIID involved in the
            regulation of hepatic genes
  JOURNAL   Mol Cell 31 (4), 531-543 (2008)
   PUBMED   18722179
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Pointud,J.C., Mengus,G., Brancorsini,S., Monaco,L., Parvinen,M.,
            Sassone-Corsi,P. and Davidson,I.
  TITLE     The intracellular localisation of TAF7L, a paralogue of
            transcription factor TFIID subunit TAF7, is developmentally
            regulated during male germ-cell differentiation
  JOURNAL   J Cell Sci 116 (Pt 9), 1847-1858 (2003)
   PUBMED   12665565
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Kida,S., Umehara,T. and Horikoshi,M.
  TITLE     Three distinct regions in a rat TFIID subunit containing histone H4
            homology
  JOURNAL   Gene 161 (2), 303-304 (1995)
   PUBMED   7665101
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_213729.2, XP_001056390.1, XP_001066806.1, XP_001066592.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100108.1, SRR26643287.27867.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..647
                     /product="transcription initiation factor TFIID subunit 6
                     isoform 2"
                     /note="TAF6 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 80 kDa; transcription initiation
                     factor TFIID subunit 6; TFIID subunit p80; TAFII80;
                     TAFII-70; TAFII-80; TAF(II)70; transcription initiation
                     factor TFIID 70 kDa subunit; transcription initiation
                     factor TFIID 80 kDa subunit"
                     /calculated_mol_wt=71071
     Region          9..408
                     /region_name="TAF6"
                     /note="Transcription initiation factor TFIID, subunit TAF6
                     (also component of histone acetyltransferase SAGA)
                     [Transcription]; COG5095"
                     /db_xref="CDD:227426"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          142..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63801.1)"
     Region          214..430
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(218..220,222..223,226,237..238,241,245,248..249,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          218..249
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          256..291
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          301..344
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          351..383
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          385..429
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            524
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     CDS             1..647
                     /gene="Taf6"
                     /gene_synonym="TAF(II)80; TAFII70"
                     /coded_by="NM_001044225.2:108..2051"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:288533"
                     /db_xref="RGD:1311608"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt devsyrikei aqdalkfmhm
       61 gkrqklttsd idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint
      121 plprvpldvc lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg
      181 kgqgaaaadg kgkekkappl legapfrlkp rsihelsveq qlyykeitea cvgsceakra
      241 ealqsiatdp glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky
      301 vhelipavmt civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft
      361 kswvdektpw ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga
      421 dhvqslllkh capvlaklrp ppdnqdayrg efgslgpllc shvvkaraqa alqaqqvnrt
      481 tltitqprpt ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv
      541 msssssasst qqgkakeall lillqshlhl lhhlhlgavp svggsrklgt aplqlqglqr
      601 lmapslldla lpsllcdivt cadllssads ythkqrvree eercfpq
//
LOCUS       NP_001423400            1074 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423400 XP_063121250
VERSION     NP_001423400.1
DBSOURCE    REFSEQ: accession NM_001436471.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121250.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1006765.1,
                                           SRR26643297.29090.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1074
                     /product="atos homolog protein A isoform 2"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119393
     Region          877..934
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1016..1073
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1074
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436471.1:236..3460"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 lrttlkhssv wrkhdfhsld gtstrafhpq tglpllsspv pqrktqsgcf dldtsllhlr
      841 slsskssrpc lnieadpgvh ekpflsssap pitslsllgn feesvlnyrl dplgivdgft
      901 aevgasgtfc pthltlpvev sfysvsddna pspymgvitl eslgkrgyrv ppsgtiqvtl
      961 fnpnktvvkm fvvvydlrsm panhqtflrq rtfsvpvkqe mkrsinkenv qhtaqllryl
     1021 ihlrfqssks gkiylhrdvr llfsrksmev dsgaayelks ytesptnpqf sprc
//
LOCUS       NP_001100308            1074 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100308 XP_001058484 XP_217194
VERSION     NP_001100308.1
DBSOURCE    REFSEQ: accession NM_001106838.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217194.4, XP_001058484.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.31158.1,
                                           SRR26643297.29085.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1074
                     /product="atos homolog protein A isoform 2"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119393
     Region          877..934
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1016..1073
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1074
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001106838.2:454..3678"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 lrttlkhssv wrkhdfhsld gtstrafhpq tglpllsspv pqrktqsgcf dldtsllhlr
      841 slsskssrpc lnieadpgvh ekpflsssap pitslsllgn feesvlnyrl dplgivdgft
      901 aevgasgtfc pthltlpvev sfysvsddna pspymgvitl eslgkrgyrv ppsgtiqvtl
      961 fnpnktvvkm fvvvydlrsm panhqtflrq rtfsvpvkqe mkrsinkenv qhtaqllryl
     1021 ihlrfqssks gkiylhrdvr llfsrksmev dsgaayelks ytesptnpqf sprc
//
LOCUS       NP_001423396            1056 aa            linear   ROD 13-MAR-2025
DEFINITION  IQ domain-containing protein H isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423396 XP_017451053
VERSION     NP_001423396.1
DBSOURCE    REFSEQ: accession NM_001436467.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_017451053.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.45846.1,
                                           SRR26360181.2259746.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1056
                     /product="IQ domain-containing protein H isoform 3"
                     /note="IQ domain-containing protein H"
                     /calculated_mol_wt=120296
     Region          420..447
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1056
                     /gene="Iqch"
                     /gene_synonym="RGD1310670"
                     /coded_by="NM_001436467.1:66..3236"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300776"
                     /db_xref="RGD:1310670"
ORIGIN      
        1 maqaqelndp igsiliqvhg dlhqlkekli qfsaeetrdp ldiqnletai qrtetglkih
       61 ierylgivnq evimtpvksl dspinskwai ptvidqksfi fpmapdklwg lqkhrgslpr
      121 gftrakpkve lnkkimqdpe nmhhraavnv sygislprik qrkahdkvrr vrkgstisnl
      181 tvlpsshrtd phfipipvlq kdaskgilsm ierglippaa ritfqnppik pqalplhsfd
      241 ehrkvsitas fpiahkprla sekveesqqk qkakvlthls teehslpvtg kdkrsrgqps
      301 rkstrittps rirrspwdyi lpvyngsvdr aapdfiafkt rykliwgsif sfleqiekfl
      361 kdyaiseakv rgkslvsllp efelnnkltk tdvlavlenp lhiqmllnlp gqrfkgrdgr
      421 teaavkiqat wksykartsf isyrqkkwas gvialawllh chktrlkriv eesrqrhldn
      481 frirakhlaa nwsrirtsrr tiihipslgy sqsvrkhisd ldieqnrqlg rlcdildvnv
      541 nviyvcsspm ndelklyykk llslqaavks gyygdrsdlq nrfriitpea vniftkhhmc
      601 lathlmyspk aikriknliq geeayivggi lhrddlavad mlnvpilase pelvhlysgk
      661 sgskrifdna nvpmppgvyd iytyqqlieq lsqlvtdnlg irrwvfkmnm efggngtafc
      721 dipshlqcyk wvvkesnrfg pedwkkkwaq esalmkisee lagvlaqhvq lvnekqfptw
      781 rkflhmfltq ggiieayppa dsitnltvdm liepdgevrv lsmgdqfhad gpfissgttm
      841 pqtsvdpqvl nslclrigni ckekdvvgyf sidlvtfidp stleqqvwtt glnlsysdql
      901 amtqltlylt ngylncslst levprfkeda erekkrlsiq aelmckahgi gydledrqgt
      961 vfilyeslkr yklgmitigv dlqgalmtfa rnlfiihqei sapdmqgetn fkttiddiet
     1021 ilgvteenkm ifagekrrke eeeslyepve iytktv
//
LOCUS       NP_001423398            1079 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423398 XP_038937073
VERSION     NP_001423398.1
DBSOURCE    REFSEQ: accession NM_001436469.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937073.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.29092.1,
                                           SRR26643287.20616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1079
                     /product="atos homolog protein A isoform 1"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119958
     Region          882..939
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1021..1078
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1079
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436469.1:236..3475"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 ldfssqrttl khssvwrkhd fhsldgtstr afhpqtglpl lsspvpqrkt qsgcfdldts
      841 llhlrslssk ssrpclniea dpgvhekpfl sssappitsl sllgnfeesv lnyrldplgi
      901 vdgftaevga sgtfcpthlt lpvevsfysv sddnapspym gvitleslgk rgyrvppsgt
      961 iqvtlfnpnk tvvkmfvvvy dlrsmpanhq tflrqrtfsv pvkqemkrsi nkenvqhtaq
     1021 llrylihlrf qssksgkiyl hrdvrllfsr ksmevdsgaa yelksytesp tnpqfsprc
//
LOCUS       NP_001423445            1203 aa            linear   ROD 13-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 38 [Rattus
            norvegicus].
ACCESSION   NP_001423445 XP_063121653
VERSION     NP_001423445.1
DBSOURCE    REFSEQ: accession NM_001436516.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Miotto,B., Chibi,M., Xie,P., Koundrioukoff,S., Moolman-Smook,H.,
            Pugh,D., Debatisse,M., He,F., Zhang,L. and Defossez,P.A.
  TITLE     The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common
            fragile site stability
  JOURNAL   Cell Rep 7 (2), 575-587 (2014)
   PUBMED   24726359
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Filion,G.J., Zhenilo,S., Salozhin,S., Yamada,D., Prokhortchouk,E.
            and Defossez,P.A.
  TITLE     A family of human zinc finger proteins that bind methylated DNA and
            repress transcription
  JOURNAL   Mol Cell Biol 26 (1), 169-181 (2006)
   PUBMED   16354688
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Kiefer,H., Chatail-Hermitte,F., Ravassard,P., Bayard,E., Brunet,I.
            and Mallet,J.
  TITLE     ZENON, a novel POZ Kruppel-like DNA binding protein associated with
            differentiation and/or survival of late postmitotic neurons
  JOURNAL   Mol Cell Biol 25 (5), 1713-1729 (2005)
   PUBMED   15713629
  REMARK    GeneRIF: ZENON is involved in the maintenance of panneuronal
            features and/or in the survival of mature neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121653.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1264456.1,
                                           SRR26360194.1264612.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..1203
                     /product="zinc finger and BTB domain-containing protein
                     38"
                     /note="zenon; zinc finger protein expressed in neurons;
                     zinc finger transcription factor Kaiso"
                     /calculated_mol_wt=135144
     Region          15..128
                     /region_name="BTB_POZ_ZBTB38_CIBZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 38 (ZBTB38); cd18223"
                     /db_xref="CDD:349532"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3; propagated from
                     UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          230..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          299..522
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          308..401
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(343,346,359,363)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          372..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(461,464,477,481)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(466,468,470,472..473,476..477,480,494,496,500..501,
                     504..505,508,522,524,526,528..529,532..533)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          731..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          857..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          895..914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          1019..1039
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1019,1022,1035,1039)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(1024,1026,1028,1030..1031,1034..1035,1038,1052,1054,
                     1058..1059,1062..1063,1066,1080,1082,1084,1086..1087,
                     1090..1091,1094)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1032..1055
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1045..1067
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1047..1067
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1075..1095
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1088..>1106
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1103..1123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1134..1154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1172..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     CDS             1..1203
                     /gene="Zbtb38"
                     /gene_synonym="RGD1310136"
                     /coded_by="NM_001436516.1:266..3877"
                     /db_xref="GeneID:315936"
                     /db_xref="RGD:1310136"
ORIGIN      
        1 mtvmslsrdl kddfhsdtvl silneqrirg ilcdvtiive dtkfkahsnv laasslyfkn
       61 ifwshticis shvlelddlk aevfteilny iysstvvvrr qetvtdlaaa gkrlgisfle
      121 dlsdrnfsns pgpyvvcite kgvvkeekne krheepavtn gpritnafsi ietensnsmf
      181 spldlrasfk kvsdamrtts lcqerasvcp eaepvrtlae hsyavssite ayrsqplreh
      241 dsssssgktg kengealttk akpcrkpktq tqdsdstten mplplvtcpe vnqerspqpa
      301 pilshsepps segdvhfpre denqpsetpg ppaaevpplv yncsccsksf dsstllgahm
      361 qlhkptqdpf vckycnkqft tlnrldrheq icmrsshmpm pggnqpflen yptigqdggs
      421 ftspdslvpe srigelssag salsdadhmv kfvngqmlys cvvckrsyvt lsslrrhanv
      481 hswrrtypch ycnkvfalae yrtrheiwht gerryqcifc letfmtyyil knhqksfhai
      541 dhrlsiskkt angglkptvy pyklyrllpm rckrapyksy rnssyesaqg nrqrnesppd
      601 tfvipnlpss emptlnfqdg rnsltsspai pvetpswqgt ptsakvknae glkwrkqalk
      661 tdlvdsaevs issignsvst tlqaepvcvs sgehsasvis ysgsvpsviv hssqfssvik
      721 hsnaiaclan snhqspsqpv aspslikdsk peadkaskla srpknskekk ktvpcnrgei
      781 teeakyvadl ggssgkttnv veetskiety iakpalpgts tnsnvaplcq itvkigneai
      841 vkrhilgskl fykrgrkpky qmqeetlpre sdpetrgdsp lglcqadcve mseafdevsd
      901 qdstdkpwrp yynykpkkks kqlrkirkvk wrkergsrsp vgrrrypael draemgrrry
      961 paeldrcaev klppdkasee eenkempklq celcdgdkaa gagaegkphq hltlkpyice
     1021 lcakqfqsss tlkmhmrcht gekpyqcktc grrfsvqgnl qkherihlgv keficqycnk
     1081 aftlnetlki herihtgekr yhcqfcfqgf lylstkrnhe rrhvrehdgk gfacfqcpki
     1141 cktaaalrmh qkkhlfktlt kqeetddlch ensdllesqp ctdsedsdqk ddikkpllkm
     1201 sfe
//
LOCUS       NP_001423399            1079 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423399 XP_038937072
VERSION     NP_001423399.1
DBSOURCE    REFSEQ: accession NM_001436470.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937072.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.45271.1,
                                           SRR26643295.32500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1079
                     /product="atos homolog protein A isoform 1"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119958
     Region          882..939
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1021..1078
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1079
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436470.1:430..3669"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 ldfssqrttl khssvwrkhd fhsldgtstr afhpqtglpl lsspvpqrkt qsgcfdldts
      841 llhlrslssk ssrpclniea dpgvhekpfl sssappitsl sllgnfeesv lnyrldplgi
      901 vdgftaevga sgtfcpthlt lpvevsfysv sddnapspym gvitleslgk rgyrvppsgt
      961 iqvtlfnpnk tvvkmfvvvy dlrsmpanhq tflrqrtfsv pvkqemkrsi nkenvqhtaq
     1021 llrylihlrf qssksgkiyl hrdvrllfsr ksmevdsgaa yelksytesp tnpqfsprc
//
LOCUS       NP_001423438            1142 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001423438 XP_006243069
VERSION     NP_001423438.1
DBSOURCE    REFSEQ: accession NM_001436509.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1142)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1142)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1142)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1142)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1142)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1142)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243069.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.22797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1142
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1142
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     6"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=128974
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          163..653
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,605,623)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Region          863..1142
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     CDS             1..1142
                     /gene="Usp28"
                     /coded_by="NM_001436509.1:105..3533"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnnp rtksenpmvq lfygtflteg
      301 vregkpfcnn etfgqyplqv ngyhnldecl egamvegdia llpsdrsvky gqerwftklp
      361 pvltfelsrf efnqslgqpe kihnklefpq viymdrymyk skelirskre sirklkeeiq
      421 vlqqkleryv kygsgpsrfp lpdmlkyvie fastkpases clsgsvehmt lplpsvhcpi
      481 sdltakesss pkscsqnaeg sfsspedalp nsevmngpft sphsslempa pppaprtvtd
      541 eemnfvktcl qrwrseieqd iqdlknciss ttqaieqmyc dpllrqvpyr lhavlvhegq
      601 asaghywayi ynqprqiwlk yndisvtess weelerdsyg glrnvsaycl myindklphc
      661 saeaahgesd qtaevealsv elrqyiqedn wrfeqeveew eeeqsckipq messpnsssq
      721 dfstsqessa asshgvrcls sehaviakeq taqaiantah ayeksgveaa lsehkeaepe
      781 kpqetnlaeq seqaaevkdt eaaappnsev seveipsvgr ilvrsdadgy deevmlspam
      841 qgvllaiaka rqtfdrdgse aglikafhee ysrlyqlake tptshsdprl qhvlvyffqn
      901 eapkrvvert lleqfadrnl sydersisim kvaqaklmei gpedmnmeey krwhedyslf
      961 rkvsvylltg lelfqkgkyq ealsylvyay qsnagllvkg prrgvkesvi alyrrkclle
     1021 lnakaaslfe tnddhsvteg invmneliip cihliinndi skddldaiev mrnhwcsylg
     1081 kdiaenlqlc lgeflprlld psaeiivlke pptirpnspy dlcsrfaavm esiqgvstvt
     1141 vk
//
LOCUS       NP_001423403            1086 aa            linear   ROD 13-MAR-2025
DEFINITION  atos homolog protein A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423403 XP_038937069
VERSION     NP_001423403.1
DBSOURCE    REFSEQ: accession NM_001436474.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937069.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.216771.1,
                                           SRR26643287.20621.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1086
                     /product="atos homolog protein A isoform 3"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=120705
     Region          889..946
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1028..1085
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1086
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436474.1:125..3385"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mvfsgnkglr rqdaldeyfe ydaeeflvsl allitegrtp ecsvkgraes fhcppaqsrf
       61 pgaarhecsd klaqcrqarr trsevtllwk nnlpimvevm llpdccysde gpstegtdln
      121 dpaikqdall lerwilepvp rqngdrfiee kalllavrsf vffsqlsawl svshgaiprn
      181 ilyrisaadv dlqwsfsqtp tehvfpvpnv shnvalkvsv qslprqahyp vltcsihtni
      241 glyekriqeq elracqhrgp geveyrcpss sqslcskhtw tmapvsalhv rsgmppeyta
      301 airnvrlcpg tgsksdngtp qasvlgfsgt gevrsqeasv rtfkslsvid ssvsscqssr
      361 qpvgepnpli dsliqdrqev iariaqhlih cdpsssrmse lpfntpests lspklhpvsq
      421 esgysrrcke afsvsfgspe fgspgdskeg kvkekletrq getcashspy prqpageanp
      481 ligslllerq dviariaqhl ehidptahip rpafskhdsn sipskvfrss fhdktmlkkd
      541 renvsvsath tevsllgdrg dgkspkpskc frsfknspqe kslkpeesaq hqnhpddith
      601 tarqellnka aglltssnss lcnesslali grlestsckl qlrkqemshe tekqclhcns
      661 idkqictnkc tekikdensp gslshlqcde srgidpkikv tmlempdyln kyktncsnkd
      721 skrsktceqn iqlgtenyls edtegsksti sdqlkteqee nkdsvagkpp svkhclstse
      781 rlknadmldf ssqrttlkhs svwrkhdfhs ldgtstrafh pqtglpllss pvpqrktqsg
      841 cfdldtsllh lrslsskssr pclnieadpg vhekpflsss appitslsll gnfeesvlny
      901 rldplgivdg ftaevgasgt fcpthltlpv evsfysvsdd napspymgvi tleslgkrgy
      961 rvppsgtiqv tlfnpnktvv kmfvvvydlr smpanhqtfl rqrtfsvpvk qemkrsinke
     1021 nvqhtaqllr ylihlrfqss ksgkiylhrd vrllfsrksm evdsgaayel ksytesptnp
     1081 qfsprc
//
LOCUS       NP_001423423            1296 aa            linear   ROD 13-MAR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423423 XP_063121459
VERSION     NP_001423423.1
DBSOURCE    REFSEQ: accession NM_001436494.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1296)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1296)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1296)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.582442.1,
                                           SRR26643287.19721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1296
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 4"
                     /calculated_mol_wt=138527
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          392..478
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <682..886
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <981..>1187
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..1296
                     /gene="Nfrkb"
                     /coded_by="NM_001436494.1:108..3998"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deedlsswlp ssparspspa vplrvvptls
      241 ttdmktadki elgdsdlklm lkkhhekrkh qpdhpdlltg dltlsdimtr vnagrkgsla
      301 alydlavlkk kvkekeekkk kkikliksea edlaeplsnt egvptlsqap splaissike
      361 epledikpcl gineisssff sllleillle sqaslpmled rvldwqsspa sslnswfsaa
      421 pnwaelvlpa lqylagesra vpssfspfve fkektqqwkl lgqsqdneke laalfhlwle
      481 tkdqafckqe nedssdamtp vprvtdyvvr pstgeekrvf qeqeryrysq phkaftfrmh
      541 gfesvvgpvk gvfdketsln karehsllrs drpayvtils lvrdaaarlp ngegtraeic
      601 ellkdsqfla pdvtstqvnt vvsgaldrlh yekdpcvkyd igrklwiylh rdrseeefer
      661 ihqaqaaaak arkalqqkpk ppskvkssnk egsvkglsgp sepsqmslsd ssmpptpvtp
      721 vtpttpalpt pispppvsav srsgsttvse paksssgvll vssptmpqlg tmlspasiqt
      781 ppssqttarv vshsssaglp qvrvvaqpsl pavsqqsvgp aqplpqmpag pqirvpvtat
      841 qtkvvpqavv atvpvkgqtt aasvqrpgpa qtgltvtslp aavspgskta msspgssaps
      901 asttaviqnv tgqniikqvs itgqlgvkpq tgnsipltat nfriqgkdvl rlppssittd
      961 akgqtvlrit pdmmatlaks qvttvkltqd lfgagsgtag kgisatlhvt snpvhaadsp
     1021 akapsasvps sapagttvvk vtpdlkptet sssafrlmpa lgvsvadqkg kntvasseak
     1081 paatirivqg lgvmppkagq titvaahakq gasvaggsgt vhsstvslps inatvsktva
     1141 vasgatstpi sigtgaptvr qvpvnttvvs tsqsgklptr itvplsvisq pmkgksvvta
     1201 piikgnlgan lsglgrniil ttmpagakli agnkpvsflt aqqlqqlqqq gqatqvriqt
     1261 vpashlqqgt asgsskavst vvvttapspk qapeqq
//
LOCUS       NP_001101614            1079 aa            linear   ROD 13-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001101614 XP_001070037 XP_236240
VERSION     NP_001101614.1
DBSOURCE    REFSEQ: accession NM_001108144.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1079)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1079)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1079)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001070037.1, XP_236240.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1079
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     7"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=122082
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          60..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          163..650
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Site            order(166,171,602,620)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          479..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5I043; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          699..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     Region          800..1079
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     Site            1050
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96RU2; propagated from
                     UniProtKB/Swiss-Prot (D3ZJ96.2)"
     CDS             1..1079
                     /gene="Usp28"
                     /coded_by="NM_001108144.2:105..3344"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqlp
      181 efrrlvlsys lpqnilencr shtekrnimf mqelqylfal llgsnrkfvd psaaldllkg
      241 afrsseeqqq dvsefthkll dwledafqla vnvnsnprtk senpmvqlfy gtfltegvre
      301 gkpfcnnetf gqyplqvngy hnldeclega mvegdiallp sdrsvkygqe rwftklppvl
      361 tfelsrfefn qslgqpekih nklefpqviy mdrymykske lirskresir klkeeiqvlq
      421 qkleryvkyg sgpsrfplpd mlkyviefas tkpasescls gsvehmtlpl psvhcpisdl
      481 takessspks csqnaegsfs spedalpnse vmngpftsph sslempappp aprtvtdeem
      541 nfvktclqrw rseieqdiqd lkncissttq aieqmycdpl lrqvpyrlha vlvhegqasa
      601 ghywayiynq prqiwlkynd isvtesswee lerdsygglr nvsayclmyi ndklphcsae
      661 aahgesdqta evealsvelr qyiqednwrf eqeveeweee qsckipqmes spnsssqdfs
      721 tsqessaass hgvrclsseh aviakeqtaq aiantahaye ksgveaalse vmlspamqgv
      781 llaiakarqt fdrdgseagl ikafheeysr lyqlaketpt shsdprlqhv lvyffqneap
      841 krvvertlle qfadrnlsyd ersisimkva qaklmeigpe dmnmeeykrw hedyslfrkv
      901 svylltglel fqkgkyqeal sylvyayqsn agllvkgprr gvkesvialy rrkcllelna
      961 kaaslfetnd dhsvteginv mneliipcih liinndiskd dldaievmrn hwcsylgkdi
     1021 aenlqlclge flprlldpsa eiivlkeppt irpnspydlc srfaavmesi qgvstvtvk
//
LOCUS       NP_001423414             777 aa            linear   ROD 13-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423414 XP_006243806
VERSION     NP_001423414.1
DBSOURCE    REFSEQ: accession NM_001436485.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243806.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2189213.1,
                                           SRR26360172.1064650.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436485.1:439..2772"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001385671             207 aa            linear   ROD 13-MAR-2025
DEFINITION  protein ripply2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001385671 XP_038938480
VERSION     NP_001385671.1
DBSOURCE    REFSEQ: accession NM_001398742.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Takahashi,J., Ohbayashi,A., Oginuma,M., Saito,D., Mochizuki,A.,
            Saga,Y. and Takada,S.
  TITLE     Analysis of Ripply1/2-deficient mouse embryos reveals a mechanism
            underlying the rostro-caudal patterning within a somite
  JOURNAL   Dev Biol 342 (2), 134-145 (2010)
   PUBMED   20346937
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Chan,T., Kondow,A., Hosoya,A., Hitachi,K., Yukita,A.,
            Okabayashi,K., Nakamura,H., Ozawa,H., Kiyonari,H., Michiue,T.,
            Ito,Y. and Asashima,M.
  TITLE     Ripply2 is essential for precise somite formation during mouse
            early development
  JOURNAL   FEBS Lett 581 (14), 2691-2696 (2007)
   PUBMED   17531978
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Kawamura,A., Koshida,S., Hijikata,H., Ohbayashi,A., Kondoh,H. and
            Takada,S.
  TITLE     Groucho-associated transcriptional repressor ripply1 is required
            for proper transition from the presomitic mesoderm to somites
  JOURNAL   Dev Cell 9 (6), 735-744 (2005)
   PUBMED   16326386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 22, 2021 this sequence version replaced XP_038938480.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI145486.1, BF545907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="protein ripply2 isoform 1"
                     /note="ripply2 homolog"
                     /calculated_mol_wt=22942
     Region          112..196
                     /region_name="Ripply"
                     /note="Transcription Regulator; pfam14998"
                     /db_xref="CDD:464433"
     CDS             1..207
                     /gene="Ripply2"
                     /gene_synonym="RGD1308746"
                     /coded_by="NM_001398742.2:9..632"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:363111"
                     /db_xref="RGD:1308746"
ORIGIN      
        1 mdttesaesa hsparspsrs rcpppaqpgy lsawihpraf stlalclptt epedrlapaq
       61 prapstsala pypsplplpv psalakfels rvarltffvr glrllscrse gfwrpwvrtp
      121 gekeelaepr aaevlpsgpg mieasrkllq yqhpvrlfwp kskcydylyq eaetllknfp
      181 iqatisfyed sdseddvegl acenqsn
//
LOCUS       NP_001423453             428 aa            linear   ROD 13-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 5 precursor [Rattus norvegicus].
ACCESSION   NP_001423453 XP_006243009
VERSION     NP_001423453.1
DBSOURCE    REFSEQ: accession NM_001436524.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1653721.1,
                                           SRR26360194.1373194.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..428
                     /product="cell adhesion molecule 1 isoform 5 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=42475
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          381..399
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..428
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001436524.1:22..1308"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydttatt epavhdsrag eegaigavdh
      361 aviggvvavv vfamlcllii lgryfarhkg tyftheakga ddaadadtai inaeggqnns
      421 eekkeyfi
//
LOCUS       NP_001100300            1070 aa            linear   ROD 13-MAR-2025
DEFINITION  IQ domain-containing protein H isoform 4 [Rattus norvegicus].
ACCESSION   NP_001100300 XP_001075872 XP_236331
VERSION     NP_001100300.1
DBSOURCE    REFSEQ: accession NM_001106830.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001075872.1, XP_236331.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1070
                     /product="IQ domain-containing protein H isoform 4"
                     /note="IQ domain-containing protein H"
                     /calculated_mol_wt=122070
     Region          405..432
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1070
                     /gene="Iqch"
                     /gene_synonym="RGD1310670"
                     /coded_by="NM_001106830.2:66..3278"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:300776"
                     /db_xref="RGD:1310670"
ORIGIN      
        1 maqaqelndp igsiliqvhg dlhqlkekli qfsaeetrdp ldiqnletai qrtetglkih
       61 ierylgivnq evimtpvksl dspinskwai ptvidqksfi fpmapdklwg lqkhrgslpr
      121 gftrakpkve lnkkimqdpe nmhhraavnv sygislprik qrkahdkvrr vrkgstisnl
      181 tvlpsshrtd phfipipvlq kdaskgilsm ierglippaa ritfqnppik pqalplhsfd
      241 ehrkvsitas fpiahkprla sekveesqqk qkakgkdkrs rgqpsrkstr ittpsrirrs
      301 pwdyilpvyn gsvdraapdf iafktrykli wgsifsfleq iekflkdyai seakvrgksl
      361 vsllpefeln nkltktdvla vlenplhiqm llnlpgqrfk grdgrteaav kiqatwksyk
      421 artsfisyrq kkwasgvial awllhchktr lkriveesrq rhldnfrira khlaanwsri
      481 rtsrrtiihi pslgysqsvr khisdldieq nrqlgrlcdi ldvnvnviyv csspmndelk
      541 lyykkllslq aavksgyygd rsdlqnrfri itpeavnift khhmclathl myspkaikri
      601 knliqgeeay ivggilhrdd lavadmlnvp ilasepelvh lysgksgskr ifdnanvpmp
      661 pgvydiytyq qlieqlsqlv tdnlgirrwv fkmnmefggn gtafcdipsh lqcykwvvke
      721 snrfgpedwk kkwaqesalm kiseelagvl aqhvqlvnek qfptwrkflh mfltqggiie
      781 ayppadsitn ltvdmliepd gevrvlsmgd qfhadgpfis sgttmpqtsv dpqvlnslcl
      841 rignickekd vvgyfsidlv tfidpstleq qvwttglnls ysdqlamtql tlyltngyln
      901 cslstlevpr fkedaerekk rlsiqaelap etsryavmst qlkhdnlsli fyyvflqmck
      961 ahgigydled rqgtvfilye slkryklgmi tigvdlqgal mtfarnlfii hqeisapdmq
     1021 getnfkttid dietilgvte enkmifagek rrkeeeesly epveiytktv
//
LOCUS       NP_001423392             711 aa            linear   ROD 13-MAR-2025
DEFINITION  RB-associated KRAB zinc finger protein [Rattus norvegicus].
ACCESSION   NP_001423392 XP_006248929
VERSION     NP_001423392.1
DBSOURCE    REFSEQ: accession NM_001436463.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006248929.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.56417.1,
                                           SRR26643429.42461.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..711
                     /product="RB-associated KRAB zinc finger protein"
                     /note="RB-associated KRAB repressor"
                     /calculated_mol_wt=81537
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..336
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(321,323,325,327..328,331..332,335,349,351,355..356,
                     359..360,363,377,379,381,383..384,387..388,391)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          340..699
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          456..476
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          594..614
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          622..642
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(627,629,631,633..634,637..638,641,655,657,661..662,
                     665..666,669,683,685,687,689..690,693..694,697)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          650..670
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          678..698
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..711
                     /gene="Rbak"
                     /gene_synonym="RGD1562875"
                     /coded_by="NM_001436463.1:255..2390"
                     /db_xref="GeneID:288489"
                     /db_xref="RGD:1562875"
ORIGIN      
        1 msiskgplsf kdvavafsqe ewqqldseer ttyrdvmlet ysnlvsvgyd vtkpnviikl
       61 eqgeepwtve gdrhakrhle ikkvddpreg iqengekhlq cgddlhswra ekgdefdeac
      121 tlepplisps sgahscvscg ktlesvteli csdgsyavek pdkcfecgkg yrenpedlnq
      181 segnsserde silqkitile kpfdyeclea ldresvfmah eraymgekpy ewngsgpdfi
      241 qisdfstyhr sqvemkpfec tqcgksfckk skfiihqrah tgekpyacgv cgksfsqkgt
      301 ltvhrrshle ekpykcdecg ktfcqklhlt qhqrthsgek pyecsecgkt fcqkthltlh
      361 qrnhsgerpy pcsecgksfs rksalndhqr thtgeklytc necgksyyrk stlithqrth
      421 tgekpyqcse cgkffsrvsy ltihyrshle ekpyectecg ktfnlnsaft rhrkahaeer
      481 vqecgecgkp srlqylpdha dglgekhhgc necgktflen safsrhqpvp egektyecni
      541 cgkvfsdlsc ytvhyrghse ekpfgcsecg ktfshnsslf rhqrvhtgek pyecyecgkf
      601 fsqksyltih hrihsgekpy ecskcgkvfs rmsnltvhyr shsgekpyec necgkvfsqk
      661 syltvhyrth sgekpyecne cgkkfhhrsa fnshqrihkr gtinvlnven l
//
LOCUS       NP_001423323             196 aa            linear   ROD 13-MAR-2025
DEFINITION  platelet-derived growth factor subunit A isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001423323 XP_038945034
VERSION     NP_001423323.1
DBSOURCE    REFSEQ: accession NM_001436394.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Rashid,F.N., Clayton,Z.E., Ogawa,M., Perdomo,J., Hume,R.D.,
            Kizana,E. and Chong,J.J.H.
  TITLE     Platelet derived growth factor-A (Pdgf-a) gene transfer modulates
            scar composition and improves left ventricular function after
            myocardial infarction
  JOURNAL   Int J Cardiol 341, 24-30 (2021)
   PUBMED   34265313
  REMARK    GeneRIF: Platelet derived growth factor-A (Pdgf-a) gene transfer
            modulates scar composition and improves left ventricular function
            after myocardial infarction.
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Connolly,N.P., Stokum,J.A., Schneider,C.S., Ozawa,T., Xu,S.,
            Galisteo,R., Castellani,R.J., Kim,A.J., Simard,J.M., Winkles,J.A.,
            Holland,E.C. and Woodworth,G.F.
  TITLE     Genetically engineered rat gliomas: PDGF-driven tumor initiation
            and progression in tv-a transgenic rats recreate key features of
            human brain cancer
  JOURNAL   PLoS One 12 (3), e0174557 (2017)
   PUBMED   28358926
  REMARK    GeneRIF: an Ntv-a transgenic rat colony was established and used to
            study glial brain tumors driven by two well-characterized oncogenic
            gene transformations, PDGFA overexpression and p53 depletion.
            Combined PDGFA and p53 alterations resulted in large, heterogeneous
            tumors in all affected animals
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Shepherd,J.A., Stamper,E., Matheson,P.J., Galganski,L.,
            Garrison,R.N., Madden,K. and Downard,C.D.
  TITLE     Alterations in platelet-derived growth factor expression in the
            pathophysiology of necrotizing enterocolitis
  JOURNAL   J Surg Res 198 (2), 377-383 (2015)
   PUBMED   25899145
  REMARK    GeneRIF: expression altered in experimental Necrotizing
            enterocolitis
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Ha,J.M., Yun,S.J., Kim,Y.W., Jin,S.Y., Lee,H.S., Song,S.H.,
            Shin,H.K. and Bae,S.S.
  TITLE     Platelet-derived growth factor regulates vascular smooth muscle
            phenotype via mammalian target of rapamycin complex 1
  JOURNAL   Biochem Biophys Res Commun 464 (1), 57-62 (2015)
   PUBMED   26032503
  REMARK    GeneRIF: PDGF regulates vascular smooth muscle phenotype via
            mammalian target of rapamycin complex 1.
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Bryckaert,M.C., Rendu,F., Tobelem,G. and Wasteson,A.
  TITLE     Collagen-induced binding to human platelets of platelet-derived
            growth factor leading to inhibition of P43 and P20 phosphorylation
  JOURNAL   J Biol Chem 264 (8), 4336-4341 (1989)
   PUBMED   2538439
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Matsui,T., Heidaran,M., Miki,T., Popescu,N., La Rochelle,W.,
            Kraus,M., Pierce,J. and Aaronson,S.
  TITLE     Isolation of a novel receptor cDNA establishes the existence of two
            PDGF receptor genes
  JOURNAL   Science 243 (4892), 800-804 (1989)
   PUBMED   2536956
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Escobedo,J.A., Navankasatussas,S., Cousens,L.S., Coughlin,S.R.,
            Bell,G.I. and Williams,L.T.
  TITLE     A common PDGF receptor is activated by homodimeric A and B forms of
            PDGF
  JOURNAL   Science 240 (4858), 1532-1534 (1988)
   PUBMED   2836953
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Womer,R.B., Frick,K., Mitchell,C.D., Ross,A.H., Bishayee,S. and
            Scher,C.D.
  TITLE     PDGF induces c-myc mRNA expression in MG-63 human osteosarcoma
            cells but does not stimulate cell replication
  JOURNAL   J Cell Physiol 132 (1), 65-72 (1987)
   PUBMED   2439522
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Heldin,C.H., Westermark,B. and Wasteson,A.
  TITLE     Platelet-derived growth factor: purification and partial
            characterization
  JOURNAL   Proc Natl Acad Sci U S A 76 (8), 3722-3726 (1979)
   PUBMED   291037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 11, 2025 this sequence version replaced XP_038945034.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2193893.1, CF111796.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..196
                     /product="platelet-derived growth factor subunit A isoform
                     2 precursor"
                     /note="PDGF subunit A; Platelet-derived growth factor A
                     chain; platelet derived growth factor, alpha;
                     platelet-derived growth factor alpha polypeptide"
                     /calculated_mol_wt=20179
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2177
     Region          21..95
                     /region_name="PDGF_N"
                     /note="Platelet-derived growth factor, N terminal region;
                     pfam04692"
                     /db_xref="CDD:461394"
     Region          94..181
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(94..97,133,135..138,153..156)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(96,129,133,140,177,179)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(123,132)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28576.2)"
     Region          158..162
                     /region_name="Receptor binding site.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P28576.2)"
     CDS             1..196
                     /gene="Pdgfa"
                     /gene_synonym="PDGF-1; PDGFACP"
                     /coded_by="NM_001436394.1:174..764"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:25266"
                     /db_xref="RGD:3282"
ORIGIN      
        1 mrtwacllll gcgylahala eeaeipreli erlarsqihs irdlqrllei dsvgaedale
       61 tnlrahgsht vkhvpekrpv pirrkrsiee aipavcktrt viyeiprsqv dptsanfliw
      121 ppcvevkrct gccntssvkc qpsrvhhrsv kvakveyvrk kpklkevqvr leehlecaca
      181 tsnlnpdhre eetdvr
//
LOCUS       NP_001423326            1877 aa            linear   ROD 13-MAR-2025
DEFINITION  unconventional myosin-Va isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423326 XP_038936775
VERSION     NP_001423326.1
DBSOURCE    REFSEQ: accession NM_001436397.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1877)
  AUTHORS   Canclini,L., Cal,K., Bardier,C., Ruiz,P., Mercer,J.A. and
            Calliari,A.
  TITLE     Calcium triggers the dissociation of myosin-Va from ribosomes in
            ribonucleoprotein complexes
  JOURNAL   FEBS Lett 594 (14), 2311-2321 (2020)
   PUBMED   32412091
  REMARK    GeneRIF: Calcium triggers the dissociation of myosin-Va from
            ribosomes in ribonucleoprotein complexes.
REFERENCE   2  (residues 1 to 1877)
  AUTHORS   Maschi,D., Gramlich,M.W. and Klyachko,V.A.
  TITLE     Myosin V functions as a vesicle tether at the plasma membrane to
            control neurotransmitter release in central synapses
  JOURNAL   Elife 7, e39440 (2018)
   PUBMED   30320552
  REMARK    GeneRIF: myosin V acts as a vesicle tether at the plasma membrane,
            rather than a motor transporting vesicles to the release sites, or
            directly regulating vesicle exocytosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1877)
  AUTHORS   Landrock,K.K., Sullivan,P., Martini-Stoica,H., Goldstein,D.S.,
            Graham,B.H., Yamamoto,S., Bellen,H.J., Gibbs,R.A., Chen,R.,
            D'Amelio,M. and Stoica,G.
  TITLE     Pleiotropic neuropathological and biochemical alterations
            associated with Myo5a mutation in a rat Model
  JOURNAL   Brain Res 1679, 155-170 (2018)
   PUBMED   29217155
  REMARK    GeneRIF: This study identified in vivo neuropathological and
            biochemical alterative changes involved in the pathogenesis of a
            spontaneous autosomal recessive movement disorder in a mutant Myo5a
            juvenile rat model.
REFERENCE   4  (residues 1 to 1877)
  AUTHORS   Guatteo,E., Rizzo,F.R., Federici,M., Cordella,A., Ledonne,A.,
            Latini,L., Nobili,A., Viscomi,M.T., Biamonte,F., Landrock,K.K.,
            Martini,A., Aversa,D., Schepisi,C., D'Amelio,M., Berretta,N. and
            Mercuri,N.B.
  TITLE     Functional alterations of the dopaminergic and glutamatergic
            systems in spontaneous alpha-synuclein overexpressing rats
  JOURNAL   Exp Neurol 287 (Pt 1), 21-33 (2017)
   PUBMED   27771352
REFERENCE   5  (residues 1 to 1877)
  AUTHORS   Ultanir,S.K., Yadav,S., Hertz,N.T., Oses-Prieto,J.A., Claxton,S.,
            Burlingame,A.L., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     MST3 kinase phosphorylates TAO1/2 to enable Myosin Va function in
            promoting spine synapse development
  JOURNAL   Neuron 84 (5), 968-982 (2014)
   PUBMED   25456499
REFERENCE   6  (residues 1 to 1877)
  AUTHORS   Opartkiattikul,N., Funahara,Y., Fucharoen,S. and Talalak,P.
  TITLE     Increase in spontaneous platelet aggregation in
            beta-thalassemia/hemoglobin E disease: a consequence of splenectomy
  JOURNAL   Southeast Asian J Trop Med Public Health 23 Suppl 2, 36-41 (1992)
   PUBMED   1298991
REFERENCE   7  (residues 1 to 1877)
  AUTHORS   Mercer,J.A., Seperack,P.K., Strobel,M.C., Copeland,N.G. and
            Jenkins,N.A.
  TITLE     Novel myosin heavy chain encoded by murine dilute coat colour locus
  JOURNAL   Nature 349 (6311), 709-713 (1991)
   PUBMED   1996138
  REMARK    Erratum:[Nature 1991 Aug 8;352(6335):547]
REFERENCE   8  (residues 1 to 1877)
  AUTHORS   Moore,K.J., Swing,D.A., Copeland,N.G. and Jenkins,N.A.
  TITLE     Interaction of the murine dilute suppressor gene (dsu) with
            fourteen coat color mutations
  JOURNAL   Genetics 125 (2), 421-430 (1990)
   PUBMED   2379821
  REMARK    Erratum:[Genetics 1990 Sep;126(1):285]
REFERENCE   9  (residues 1 to 1877)
  AUTHORS   Moore,K.J., Seperack,P.K., Strobel,M.C., Swing,D.A., Copeland,N.G.
            and Jenkins,N.A.
  TITLE     Dilute suppressor dsu acts semidominantly to suppress the coat
            color phenotype of a deletion mutation, dl20J, of the murine dilute
            locus
  JOURNAL   Proc Natl Acad Sci U S A 85 (21), 8131-8135 (1988)
   PUBMED   3141922
REFERENCE   10 (residues 1 to 1877)
  AUTHORS   Murad,S. and Kishimoto,Y.
  TITLE     Alpha hydroxylation of lignoceric acid to cerebronic acid during
            brain development. Diminished hydroxylase activity in
            myelin-deficient mouse mutants
  JOURNAL   J Biol Chem 250 (15), 5841-5846 (1975)
   PUBMED   1150661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_038936775.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1877
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1877
                     /product="unconventional myosin-Va isoform 1"
                     /note="dilute-opisthotonus; myosin-Va; dilute myosin heavy
                     chain, non-muscle; myosin 5a; unconventional myosin-Va"
                     /calculated_mol_wt=217976
     Region          7..1445
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          83..751
                     /region_name="MYSc_Myo5"
                     /note="class V myosin, motor domain; cd01380"
                     /db_xref="CDD:276831"
     Site            order(111..119,163..170,209..219,437..442)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276831"
     Site            111..119
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276831"
     Site            163..170
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276831"
     Site            209..219
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276831"
     Site            437..445
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276831"
     Site            order(466..477,480..489)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276831"
     Site            685..695
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276831"
     Site            order(706..716,736..751)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276831"
     Region          1503..1877
                     /region_name="Myo5a_CBD"
                     /note="Cargo binding domain of myosin 5a; cd15478"
                     /db_xref="CDD:271262"
     Site            order(1520..1522,1525..1528,1698..1699,1857,1862,1864,
                     1866..1868)
                     /site_type="other"
                     /note="RILPL2 interface [polypeptide binding]"
                     /db_xref="CDD:271262"
     Site            order(1548,1551..1552,1555..1556,1559..1560,1563,1594,
                     1612..1617,1619..1620,1623)
                     /site_type="other"
                     /note="melanophilin interface [polypeptide binding]"
                     /db_xref="CDD:271262"
     CDS             1..1877
                     /gene="Myo5a"
                     /gene_synonym="Dop; Myh12"
                     /coded_by="NM_001436397.1:60..5693"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25017"
                     /db_xref="RGD:3143"
ORIGIN      
        1 maaselytkf arvwipdpee vwksaellkd ykpgdkvlll hleegkdley rldpktselp
       61 hlrnpdilvg endltalsyl hepavlhnlr vrfidskliy tycgivlvai npyeqlpiyg
      121 ediinaysgq nmgdmdphif avaeeaykqm ardernqsii vsgesgagkt vsakyamryf
      181 atvsgsasea nveekvlasn pimesignak ttrndnssrf gkyieigfdk ryriiganmr
      241 tylleksrvv fqaeeernyh ifyqlcasak lpefkmlrlg nadsfhytkq ggspmiegvd
      301 dakemahtrq actllgises yqmgifrila gilhlgnvgf asrdsdscti ppkhepliif
      361 cdlmgvdyee mchwlchrkl atatetyikp isklqatnar dalakhiyak lfnwivghvn
      421 qalhsavkqh sfigvldiyg fetfeinsfe qfcinyanek lqqqfnmhvf kleqeeymke
      481 qipwtlidfy dnqpcinlie sklgildlld eeckmpkgtd dtwaqklynt hlnkcalfek
      541 prmsnkafii khfadkveyq cegfleknkd tvfeeqikvl ksskfkmlpe lfqddekais
      601 ptsatssgrt pltrvpvkpt kgrpgqtake hkktvglqfr nslhllmetl nattphyvrc
      661 ikpndfkfpf tfdekravqq lracgvleti risaagfpsr wtyqeffsry rvlmkqkdvl
      721 gdrkqtcqnv leklildkdk yqfgktkiff ragqvaylek lradklraac iriqktirgw
      781 llrkrylcmq raaitvqryv rgyqarcyak flrrtkaatt iqkywrmyvv rrkykirraa
      841 tivlqsylrg ylarnryrki lrehkaviiq krvrgwlart hykrtmkaii ylqccfrrmm
      901 akrelkklki earsverykk lhigmenkim qlqrkvdeqn kdykclmekl tnlegvynse
      961 teklrndver lqlseeeakv atgrvlslqe eiaklrkdle qtrsekksie eradkykqet
     1021 eqlvsnlkee ntllkqeket lnhlmveqak emtetmerkl veetkqleld lnderlryqn
     1081 llnefsrlee ryddlkeemt lmlnvpkpgh krtdsthssn eseytfssef aetediaprt
     1141 eeptekkvpl dmslflklqk rvteleqekq lmqdeldrke eqvlrskake eerpqirgae
     1201 leyeslkrqe lesenkklkn elnelrkals eksapevtap gapayrvlme qltavseeld
     1261 vrkeevlilr sqlvsqkeai qpkntmtdst illedvqkmk dkgeiaqayi glketnrssa
     1321 mdyqelnedg elwlvyeglk qanrllesql qsqkrshene aealrgeiqs lkeennrqqq
     1381 llaqnlqlpp earieaslqh eitrltnenl yfeelyaddp kkyqsyrisl ykrmidlmeq
     1441 lekqdktvrk lkkqlkvfak kigelevgqm enispgqiid epirpvnipr kekdfqgmle
     1501 ykredeqklv knlilelkpr gvavnlipgl payilfmcvr hadylnddqk vrslltstin
     1561 sikkvlkkrg ddfetvsfwl sntcrflhcl kqysgeegfm khntsrqneh cltnfdlaey
     1621 rqvlsdlaiq iyqqlvrvle nilqpmivsg mlehetiqgv sgvkptglrk rtssiadegt
     1681 ytldsilrql nsfhsvmcqh gmdpelikqv vkqmfyivga itlnnlllrk dmcswskgmq
     1741 irynvsqlee wlrdknlmns gaketlepli qaaqllqvkk ktdddaeaic smcnalttaq
     1801 ivkvlnlytp vnefeervsv sfirtiqvrl rdrkdspqll mdakhifpvt fpfnpsslal
     1861 etiqipaslg lgfiarv
//
LOCUS       NP_001423332             769 aa            linear   ROD 13-MAR-2025
DEFINITION  transducin-like enhancer protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423332 XP_006243280
VERSION     NP_001423332.1
DBSOURCE    REFSEQ: accession NM_001436403.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Villanueva,C.J., Vergnes,L., Wang,J., Drew,B.G., Hong,C., Tu,Y.,
            Hu,Y., Peng,X., Xu,F., Saez,E., Wroblewski,K., Hevener,A.L.,
            Reue,K., Fong,L.G., Young,S.G. and Tontonoz,P.
  TITLE     Adipose subtype-selective recruitment of TLE3 or Prdm16 by
            PPARgamma specifies lipid storage versus thermogenic gene programs
  JOURNAL   Cell Metab 17 (3), 423-435 (2013)
   PUBMED   23473036
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Wang,J.C., Waltner-Law,M., Yamada,K., Osawa,H., Stifani,S. and
            Granner,D.K.
  TITLE     Transducin-like enhancer of split proteins, the human homologs of
            Drosophila groucho, interact with hepatic nuclear factor 3beta
  JOURNAL   J Biol Chem 275 (24), 18418-18423 (2000)
   PUBMED   10748198
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Feldman,J.D., Vician,L., Crispino,M., Hoe,W., Baudry,M. and
            Herschman,H.R.
  TITLE     rTLE3, a newly identified transducin-like enhancer of split, is
            induced by depolarization in brain
  JOURNAL   J Neurochem 74 (5), 1838-1847 (2000)
   PUBMED   10800926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_006243280.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.33954.1,
                                           SRR26643298.44707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..769
                     /product="transducin-like enhancer protein 3 isoform 1"
                     /note="transducin-like enhancer protein 3; rTLE3;
                     transducin-like enhancer of split 3, E(spl) homolog;
                     transducin-like enhancer of split 3, homolog of Drosophila
                     E(spl); transducin-like enhancer of split 3 homolog of
                     Drosophila; transducin-like enhancer of split 3 (E(sp1)
                     homolog, Drosophila)"
                     /calculated_mol_wt=82974
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          130..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          184..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000250|UniProtKB:Q04724"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <251..469
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04727; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04726; propagated from
                     UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          481..519
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          <482..767
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          486..525
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          527..566
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          533..571
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          571..610
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          576..612
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          613..652
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          619..654
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          654..693
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          659..692
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          695..734
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          700..734
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          736..768
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIT3.1)"
     Region          741..765
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..769
                     /gene="Tle3"
                     /gene_synonym="Esp3"
                     /coded_by="NM_001436403.1:1076..3385"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:84424"
                     /db_xref="RGD:620292"
ORIGIN      
        1 mypqgrhpap hqpgqpgfkf tvaescdrik defqflqaqy hslkveydkl anektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntila qimpflsqeh qqqvaqaver akqvtmteln
      121 aiigqqqlqa qhlshathgp pvqlpphpsg lqppgippvt gsssgllalg algsqahlav
      181 kdeknhheld hreresstnn svspseslra sekhrgsady smeakkrkae ekdslsryds
      241 dgdksddlvv dvsnedpatp rvspahsppe ngldkarglk kdaptspasv asssstpssk
      301 tkdlghndks stpglksntp tprndaptpg tsttpglrsm pgkppgmdpi asalrtpisl
      361 tssyaapfam mshhemngsl tspsayaglh nipsqmsaaa aaaaaaygrs pmvsfgavgf
      421 dphppmratg lpsslasipg gkpaysfhvs adgqmqpvpf phdalagpgi prharqintl
      481 shgevvcavt isnptrhvyt ggkgcvkiwd isqpgskspi sqldclnrdn yirsckllpd
      541 grtlivggea stltiwdlas ptprikaelt ssapacyala ispdakvcfs ccsdgniavw
      601 dlhnqtlvrq fqghtdgasc idishdgtkl wtggldntvr swdlregrql qqhdftsqif
      661 slgycptgew lavgmessnv evlhhtkpdk yqlhlhescv lslkfaycgk wfvstgkdnl
      721 lnawrtpyga sifqskesss vlscdisadd kyivtgsgdk katvyeviy
//
LOCUS       NP_001423321            1429 aa            linear   ROD 13-MAR-2025
DEFINITION  nitric oxide synthase 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423321 XP_063127113
VERSION     NP_001423321.1
DBSOURCE    REFSEQ: accession NM_001436392.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1429)
  AUTHORS   Jiang,T., Wan,G., Zhang,H., Gyawali,Y.P., Underbakke,E.S. and
            Feng,C.
  TITLE     Mapping the Intersubunit Interdomain FMN-Heme Interactions in
            Neuronal Nitric Oxide Synthase by Targeted Quantitative
            Cross-Linking Mass Spectrometry
  JOURNAL   Biochemistry 63 (11), 1395-1411 (2024)
   PUBMED   38747545
  REMARK    GeneRIF: Mapping the Intersubunit Interdomain FMN-Heme Interactions
            in Neuronal Nitric Oxide Synthase by Targeted Quantitative
            Cross-Linking Mass Spectrometry.
REFERENCE   2  (residues 1 to 1429)
  AUTHORS   Gyawali,Y.P., Jiang,T., Yang,J., Zheng,H., Liu,R., Zhang,H. and
            Feng,C.
  TITLE     Differential superoxide production in phosphorylated neuronal
            nitric oxide synthase mu and alpha variants
  JOURNAL   J Inorg Biochem 251, 112454 (2024)
   PUBMED   38100901
  REMARK    GeneRIF: Differential superoxide production in phosphorylated
            neuronal nitric oxide synthase mu and alpha variants.
REFERENCE   3  (residues 1 to 1429)
  AUTHORS   Chen,R., Qian,L., Fu,J., Qin,J., Chen,X. and Xu,X.
  TITLE     Downregulation of Preso protects against
            ischemic/reperfusion-mediated neuronal injury through regulating
            PSD95-nNOS/YAP pathways
  JOURNAL   Neurochem Int 169, 105586 (2023)
   PUBMED   37442439
  REMARK    GeneRIF: Downregulation of Preso protects against
            ischemic/reperfusion-mediated neuronal injury through regulating
            PSD95-nNOS/YAP pathways.
REFERENCE   4  (residues 1 to 1429)
  AUTHORS   Yang,Z., Li,P., Yuan,Q., Wang,X., Ma,H.H. and Zhuan,B.
  TITLE     Inhibition of miR-4640-5p alleviates pulmonary hypertension in
            chronic obstructive pulmonary disease patients by regulating nitric
            oxide synthase 1
  JOURNAL   Respir Res 24 (1), 92 (2023)
   PUBMED   36964568
  REMARK    GeneRIF: Inhibition of miR-4640-5p alleviates pulmonary
            hypertension in chronic obstructive pulmonary disease patients by
            regulating nitric oxide synthase 1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1429)
  AUTHORS   Vasu,D., Li,H., Hardy,C.D., Poulos,T.L. and Silverman,R.B.
  TITLE     2-Aminopyridines with a shortened amino sidechain as potent,
            selective, and highly permeable human neuronal nitric oxide
            synthase inhibitors
  JOURNAL   Bioorg Med Chem 69, 116878 (2022)
   PUBMED   35772285
REFERENCE   6  (residues 1 to 1429)
  AUTHORS   Kobzik,L., Reid,M.B., Bredt,D.S. and Stamler,J.S.
  TITLE     Nitric oxide in skeletal muscle
  JOURNAL   Nature 372 (6506), 546-548 (1994)
   PUBMED   7527495
REFERENCE   7  (residues 1 to 1429)
  AUTHORS   Seo,H.G., Tatsumi,H., Fujii,J., Nishikawa,A., Suzuki,K., Kangawa,K.
            and Taniguchi,N.
  TITLE     Nitric oxide synthase from rat colorectum: purification, peptide
            sequencing, partial PCR cloning, and immunohistochemistry
  JOURNAL   J Biochem 115 (3), 602-607 (1994)
   PUBMED   7520037
REFERENCE   8  (residues 1 to 1429)
  AUTHORS   Stuehr,D.J. and Ikeda-Saito,M.
  TITLE     Spectral characterization of brain and macrophage nitric oxide
            synthases. Cytochrome P-450-like hemeproteins that contain a flavin
            semiquinone radical
  JOURNAL   J Biol Chem 267 (29), 20547-20550 (1992)
   PUBMED   1383204
REFERENCE   9  (residues 1 to 1429)
  AUTHORS   Bredt,D.S., Hwang,P.M., Glatt,C.E., Lowenstein,C., Reed,R.R. and
            Snyder,S.H.
  TITLE     Cloned and expressed nitric oxide synthase structurally resembles
            cytochrome P-450 reductase
  JOURNAL   Nature 351 (6329), 714-718 (1991)
   PUBMED   1712077
REFERENCE   10 (residues 1 to 1429)
  AUTHORS   Bredt,D.S. and Snyder,S.H.
  TITLE     Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 682-685 (1990)
   PUBMED   1689048
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 11, 2025 this sequence version replaced XP_063127113.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360194.858313.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1429
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..1429
                     /product="nitric oxide synthase 1 isoform 2"
                     /EC_number="1.14.13.39"
                     /note="nitric oxide synthase, brain; nitric oxidase
                     synthase; nNOS; N-NOS; NC-NOS; NOS type I; neuronal NOS;
                     constitutive NOS; peptidyl-cysteine S-nitrosylase NOS1;
                     nitric oxide synthase 1, neuronal"
                     /calculated_mol_wt=160329
     Region          1..200
                     /region_name="Interaction with NOSIP.
                     /evidence=ECO:0000269|PubMed:15548660"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Region          14..123
                     /region_name="PDZ_nNOS-like"
                     /note="PDZ domain of neuronal nitric oxide synthase
                     (nNOS), and related domains; cd06708"
                     /db_xref="CDD:467192"
     Site            order(27..33,44,47,77,81,84..85)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467192"
     Region          152..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Region          163..240
                     /region_name="Interaction with DYNLL1/PIN.
                     /evidence=ECO:0000269|PubMed:8864115"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Region          214..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Region          271..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0J4; propagated from
                     UniProtKB/Swiss-Prot (P29476.1)"
     Region          300..711
                     /region_name="NOS_oxygenase_euk"
                     /note="Nitric oxide synthase (NOS) eukaryotic oxygenase
                     domain. NOS produces nitric oxide (NO) by catalyzing a
                     five-electron heme-based oxidation of a guanidine nitrogen
                     of L-arginine to L-citrulline via two successive
                     monooxygenation reactions producing N...; cd00795"
                     /db_xref="CDD:238410"
     Site            order(306..307,318,320,324,326..332,334,336,600,602,622,
                     627..628,632,638,651..652,682,684..686,692,694..698)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238410"
     Site            order(415,478,562,584..585,587..588,592,596..597,677..678,
                     706)
                     /site_type="active"
                     /db_xref="CDD:238410"
     Region          725..745
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:1712077"
                     /note="propagated from UniProtKB/Swiss-Prot (P29476.1)"
     Region          757..930
                     /region_name="Flavodoxin_1"
                     /note="pfam00258"
                     /db_xref="CDD:425562"
     Site            847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29476.1)"
     Site            857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0J4; propagated from
                     UniProtKB/Swiss-Prot (P29476.1)"
     Site            858
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29476.1)"
     Region          996..1399
                     /region_name="Nitric_oxide_synthase"
                     /note="The ferredoxin-reductase (FNR) like C-terminal
                     domain of the nitric oxide synthase (NOS) fuses with a
                     heme-containing N-terminal oxidase domain. The reductase
                     portion is similar in structure to NADPH dependent
                     cytochrome-450 reductase (CYPOR), having an...; cd06202"
                     /db_xref="CDD:99799"
     Site            order(1023,1079..1080,1182,1185,1230,1238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:99799"
     Site            order(1032,1173..1176,1191,1193,1209..1212)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99799"
     Site            order(1173,1175..1176)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99799"
     Site            order(1176,1349,1393,1395)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99799"
     Site            order(1193..1196,1249,1251,1283..1284,1313..1314,1322,
                     1324,1354)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99799"
     Site            order(1209,1212,1215)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99799"
     Site            order(1246,1250..1253,1255)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99799"
     CDS             1..1429
                     /gene="Nos1"
                     /gene_synonym="bNOS"
                     /coded_by="NM_001436392.1:499..4788"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24598"
                     /db_xref="RGD:3184"
ORIGIN      
        1 meentfgvqq iqpnvisvrl fkrkvgglgf lvkervskpp viisdlirgg aaeqsgliqa
       61 gdiilavndr plvdlsydsa levlrgiase thvvlilrgp egftthlett ftgdgtpkti
      121 rvtqplgppt kavdlshqps askdqslavd rvtglgngpq haqghgqgag svsqangvai
      181 dptmkstkan lqdigehdel lkeiepvlsi lnsgskatnr ggpakaemkd tgiqvdrdld
      241 gkshkapplg gdndrvfndl wgkdnvpvvl nnpysekeqs ptsgkqsptk ngspsrcprf
      301 lkvknwetdv vltdtlhlks tletgctehi cmgsimlpsq htrkpedvrt kdqlfplake
      361 fldqyyssik rfgskahmdr leevnkeies tstyqlkdte liygakhawr nasrcvgriq
      421 wsklqvfdar dcttahgmfn yicnhvkyat nkgnlrsait ifpqrtdgkh dfrvwnsqli
      481 ryagykqpdg stlgdpanvq fteiciqqgw kaprgrfdvl plllqangnd pelfqippel
      541 vlevpirhpk fdwfkdlglk wyglpavsnm lleigglefs acpfsgwymg teigvrdycd
      601 nsrynileev akkmdldmrk tsslwkdqal veiniavlys fqsdkvtivd hhsatesfik
      661 hmeneyrcrg gcpadwvwiv ppmsgsitpv fhqemlnyrl tpsfeyqpdp wnthvwkgtn
      721 gtptkrraig fkklaeavkf saklmgqama krvkatilya tetgksqaya ktlceifkha
      781 fdakamsmee ydivhlehea lvlvvtstfg ngdppengek fgcalmemrh pnsvqeerks
      841 ykvrfnsvss ysdsrkssgd gpdlrdnfes tgplanvrfs vfglgsrayp hfcafghavd
      901 tlleelgger ilkmregdel cgqeeafrtw akkvfkaacd vfcvgddvni ekannslisn
      961 drswkrnkfr ltyvaeapdl tqglsnvhkk rvsaarllsr qnlqspkssr stifvrlhtn
     1021 gnqelqyqpg dhlgvfpgnh edlvnalier ledappanhv vkvemleern talgvisnwk
     1081 desrlppcti fqafkyyldi ttpptplqlq qfaslatnek ekqrllvlsk glqeyeewkw
     1141 gknptmvevl eefpsiqmpa tllltqlsll qpryysisss pdmypdevhl tvaivsyhtr
     1201 dgegpvhhgv csswlnriqa ddvvpcfvrg apsfhlprnp qvpcilvgpg tgiapfrsfw
     1261 qqrqfdiqhk gmnpcpmvlv fgcrqskidh iyreetlqak nkgvfrelyt aysrepdrpk
     1321 kyvqdvlqeq laesvyralk eqgghiyvcg dvtmaadvlk aiqrimtqqg klseedagvf
     1381 isrlrddnry hedifgvtlr tyevtnrlrs esiafieesk kdadevfss
//
LOCUS       NP_001423460             207 aa            linear   ROD 14-MAR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 [Rattus norvegicus].
ACCESSION   NP_001423460 XP_017451232
VERSION     NP_001423460.1
DBSOURCE    REFSEQ: accession NM_001436531.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Asai,M., Ramachandrappa,S., Joachim,M., Shen,Y., Zhang,R.,
            Nuthalapati,N., Ramanathan,V., Strochlic,D.E., Ferket,P.,
            Linhart,K., Ho,C., Novoselova,T.V., Garg,S., Ridderstrale,M.,
            Marcus,C., Hirschhorn,J.N., Keogh,J.M., O'Rahilly,S., Chan,L.F.,
            Clark,A.J., Farooqi,I.S. and Majzoub,J.A.
  TITLE     Loss of function of the melanocortin 2 receptor accessory protein 2
            is associated with mammalian obesity
  JOURNAL   Science 341 (6143), 275-278 (2013)
   PUBMED   23869016
  REMARK    Erratum:[Science. 2013 Aug 30;341(6149):959]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_017451232.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.7120.1,
                                           SRR26360176.1387325.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN12840120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="melanocortin-2 receptor accessory protein 2"
                     /calculated_mol_wt=23660
     Region          16..101
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     CDS             1..207
                     /gene="Mrap2"
                     /gene_synonym="RGD1309873"
                     /coded_by="NM_001436531.1:176..799"
                     /db_xref="GeneID:363112"
                     /db_xref="RGD:1309873"
ORIGIN      
        1 memsaqrlts nrtspqspsn sdytweyeyy eigpvsfegl kahkysivig fwvglavfvi
       61 fmffvltllt ktgaphqdna essekrfrmn sfvsdfgkpl esdkvfsrqg neesrslfhc
      121 yinevehldr vkvchrttai dsdvhlqeai rssgrpeeel trfmqfdipn fvntdqnsfg
      181 eddllisepp vllenkpvsq tsrtdld
//
LOCUS       NP_001178926             376 aa            linear   ROD 14-MAR-2025
DEFINITION  layilin isoform 6 precursor [Rattus norvegicus].
ACCESSION   NP_001178926 XP_576410
VERSION     NP_001178926.1
DBSOURCE    REFSEQ: accession NM_001191997.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_576410.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN12840108, SAMN12840111
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..376
                     /product="layilin isoform 6 precursor"
                     /calculated_mol_wt=40253
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          37..185
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(147,151,153,169,171..174,177..179)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153065"
     CDS             1..376
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001191997.2:122..1252"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgd ldprggqrfc wegtrrpcyr viyfhdtsqr
       61 rnfeeakeac mkdggqlasi etadeqrlie nfieslqasd gdfwiglkrl eekqhnstac
      121 qdlyawtdgs lsqfrnwymd epscesevcv vmyhqpsapp giggpymfqw nddrcntkkn
      181 fickysddkp sttpslspgg eatepaapil peetleidtk erreaalnla yilipsiplf
      241 lllvvtsavc wvwicrrkre qtdpptkeqh tiwptphqen spdlevynvi rkqseadlae
      301 prpdlknisf rvcsgeampd dtscdydnmv inpsesglvt lasmegrfvt ndiyefspdr
      361 mgrskesgwv eneiyy
//
LOCUS       NP_001423463             581 aa            linear   ROD 14-MAR-2025
DEFINITION  cysteine/serine-rich nuclear protein 1 [Rattus norvegicus].
ACCESSION   NP_001423463 XP_006244182
VERSION     NP_001423463.1
DBSOURCE    REFSEQ: accession NM_001436534.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Ye,X., Lin,J., Lin,Z., Xue,A., Li,L., Zhao,Z., Liu,L., Shen,Y. and
            Cong,B.
  TITLE     Axin1 up-regulated 1 accelerates stress-induced cardiomyocytes
            apoptosis through activating Wnt/beta-catenin signaling
  JOURNAL   Exp Cell Res 359 (2), 441-448 (2017)
   PUBMED   28830684
  REMARK    GeneRIF: Axud1 mediated stress-induced cardiomyocytes apoptosis
            through activating Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Gingras,S., Pelletier,S., Boyd,K. and Ihle,J.N.
  TITLE     Characterization of a family of novel cysteine- serine-rich nuclear
            proteins (CSRNP)
  JOURNAL   PLoS One 2 (8), e808 (2007)
   PUBMED   17726538
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Schmahl,J., Raymond,C.S. and Soriano,P.
  TITLE     PDGF signaling specificity is mediated through multiple immediate
            early genes
  JOURNAL   Nat Genet 39 (1), 52-60 (2007)
   PUBMED   17143286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006244182.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.48264.1,
                                           SRR26360181.3171095.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..581
                     /product="cysteine/serine-rich nuclear protein 1"
                     /note="AXIN1 up-regulated 1"
                     /calculated_mol_wt=62329
     Region          77..301
                     /region_name="CSRNP_N"
                     /note="Cysteine/serine-rich nuclear protein N-terminus;
                     pfam16019"
                     /db_xref="CDD:464977"
     CDS             1..581
                     /gene="Csrnp1"
                     /gene_synonym="Axud1"
                     /coded_by="NM_001436534.1:445..2190"
                     /db_xref="GeneID:363165"
                     /db_xref="RGD:1305999"
ORIGIN      
        1 magiqkrkfd qleeddcsss slssgdlsps ppsssaspaw tseeeglgdq ppqpdqdssg
       61 iqslmppsil kraprerpgh vafdgitvyy fprcqgftsv pshggctlgm asrhstcrlf
      121 slaefkqeqf rarreklrrr lkeeklemlk wklsvsgvpe agadvpltvd aiddasveed
      181 lavavaggrl eeanflqpyp prqrrallra sgvrridree krelqalrqs redcgchcdg
      241 vcdpetcsci lagikcqmdh tsfpcgccse gcenphgrve fnqarvqthf ihtltrlqme
      301 qgaeslgdpe spmedvpveq tvvspfppsk ptmsndlgds scgsdmtdss ttyssggsgs
      361 rseapnhlah pslpgssfrs gidedsleqi lnfsdsdlgi eeeeeeggsv gnldnlscfh
      421 ladifgtgdp gslaswthsq fgsslpsgil denanldasc flssgleglr egslpsssgs
      481 pegeaaqsss ldlslsscds fellqslpdy slgphytsrr vsgsldslet fhpspsfspp
      541 rdasfldsli glsepvtdvl apllesqfed tavvpldpvp v
//
LOCUS       NP_001178947             652 aa            linear   ROD 14-MAR-2025
DEFINITION  beta-galactosidase-1-like protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001178947 XP_578717
VERSION     NP_001178947.1
DBSOURCE    REFSEQ: accession NM_001192018.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_578717.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1978458.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..652
                     /product="beta-galactosidase-1-like protein 2 isoform 2"
                     /EC_number="3.2.1.23"
                     /note="beta-galactosidase-1-like protein 2"
                     /calculated_mol_wt=73849
     Region          69..382
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     CDS             1..652
                     /gene="Glb1l2"
                     /gene_synonym="RGD1564436"
                     /coded_by="NM_001192018.2:43..2001"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:503194"
                     /db_xref="RGD:1564436"
ORIGIN      
        1 mpkwslrrrp grtlglllll vlsflvlrry lnpkvgscdr egalrlnwts vlplwlqrqr
       61 lglrtkgpnf mledstfqil ggsihyfrvp reywrdrllk lkacglntlt tyvpwnlhep
      121 ergkfdfsgn ldleafiwla akiglwvilr pgpyicseid lgglpswllq dpdmklrtty
      181 pgftkavdly fdhlmsrvvp lqykhggpii avqveneygs yngdhaympy ikkaledrgi
      241 iemlltsdnk dglekgvvdg vlatinlqsq qelvalnsil lsiqgiqpkm vmeywtgwfd
      301 swggshnild ssevlqtvsa iikdgssinl ymfhggtnfg fingamhfgd ykadvtsydy
      361 dailteagdy takytklrel fgtfsgvppp pppeltakmv yepvtpsfyl slwdallymd
      421 kpitseipin menlpvnngn gqafgyvlye ttifssgvls glvrdrgqvf lnrvsigfld
      481 ytttkitipl tqgytilril venrgrvnyg nnidsqrkgl ignlylnnkp lknfkiysld
      541 mtkqffqrfd mdkwsvvpke itfpafflgt lsvgiypsdt flklegwvkg vvlvndhnlg
      601 rywnvgpqet lylpgvwldk glnkviifee tmagsmvqst diphlgrnqy vn
//
LOCUS       NP_001102244             207 aa            linear   ROD 14-MAR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 [Rattus norvegicus].
ACCESSION   NP_001102244 XP_001065048
VERSION     NP_001102244.1
DBSOURCE    REFSEQ: accession NM_001108774.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Asai,M., Ramachandrappa,S., Joachim,M., Shen,Y., Zhang,R.,
            Nuthalapati,N., Ramanathan,V., Strochlic,D.E., Ferket,P.,
            Linhart,K., Ho,C., Novoselova,T.V., Garg,S., Ridderstrale,M.,
            Marcus,C., Hirschhorn,J.N., Keogh,J.M., O'Rahilly,S., Chan,L.F.,
            Clark,A.J., Farooqi,I.S. and Majzoub,J.A.
  TITLE     Loss of function of the melanocortin 2 receptor accessory protein 2
            is associated with mammalian obesity
  JOURNAL   Science 341 (6143), 275-278 (2013)
   PUBMED   23869016
  REMARK    Erratum:[Science. 2013 Aug 30;341(6149):959]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001065048.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB720474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984015, SAMN14984024
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="melanocortin-2 receptor accessory protein 2"
                     /calculated_mol_wt=23660
     Region          16..101
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     CDS             1..207
                     /gene="Mrap2"
                     /gene_synonym="RGD1309873"
                     /coded_by="NM_001108774.2:184..807"
                     /db_xref="GeneID:363112"
                     /db_xref="RGD:1309873"
ORIGIN      
        1 memsaqrlts nrtspqspsn sdytweyeyy eigpvsfegl kahkysivig fwvglavfvi
       61 fmffvltllt ktgaphqdna essekrfrmn sfvsdfgkpl esdkvfsrqg neesrslfhc
      121 yinevehldr vkvchrttai dsdvhlqeai rssgrpeeel trfmqfdipn fvntdqnsfg
      181 eddllisepp vllenkpvsq tsrtdld
//
LOCUS       NP_001423483             333 aa            linear   ROD 14-MAR-2025
DEFINITION  layilin isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001423483 XP_038937886
VERSION     NP_001423483.1
DBSOURCE    REFSEQ: accession NM_001436554.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937886.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2147297.1,
                                           SRR21887621.678274.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760494,
                                           SAMN06621351 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..333
                     /product="layilin isoform 3 precursor"
                     /calculated_mol_wt=35726
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          30..178
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(140,144,146,162,164..167,170..172)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153065"
     CDS             1..333
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001436554.1:122..1123"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgq rfcwegtrrp cyrviyfhdt sqrrnfeeak
       61 eacmkdggql asietadeqr lienfieslq asdgdfwigl krleekqhns tacqdlyawt
      121 dgslsqfrnw ymdepscese vcvvmyhqps appgiggpym fqwnddrcnt kknfickysd
      181 eaalnlayil ipsiplflll vvtsavcwvw icrrkreqtd pptkeqhtiw ptphqenspd
      241 levynvirkq seadlaeprp dlknisfrvc sgeampddts cdydnmvinp sesglvtlas
      301 megrfvtndi yefspdrmgr skesgwvene iyy
//
LOCUS       NP_001423488             692 aa            linear   ROD 14-MAR-2025
DEFINITION  beta-galactosidase-1-like protein 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423488 XP_017451348
VERSION     NP_001423488.1
DBSOURCE    REFSEQ: accession NM_001436559.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_017451348.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.27725.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..692
                     /product="beta-galactosidase-1-like protein 2 isoform 3"
                     /EC_number="3.2.1.23"
                     /note="beta-galactosidase-1-like protein 2"
                     /calculated_mol_wt=77864
     Region          109..422
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     CDS             1..692
                     /gene="Glb1l2"
                     /gene_synonym="RGD1564436"
                     /coded_by="NM_001436559.1:43..2121"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:503194"
                     /db_xref="RGD:1564436"
ORIGIN      
        1 mpkwslrrrp grtlglllll vlsflvlrry lnpkvgscdr egalslrvfm lnvlsvlfla
       61 aasacsspav gpspgssnee shlsrlnwts vlplwlqrqr lglrtkgpnf mledstfqil
      121 ggsihyfrvp reywrdrllk lkacglntlt tyvpwnlhep ergkfdfsgn ldleafiwla
      181 akiglwvilr pgpyicseid lgglpswllq dpdmklrtty pgftkavdly fdhlmsrvvp
      241 lqykhggpii avqveneygs yngdhaympy ikkaledrgi iemlltsdnk dglekgvvdg
      301 vlatinlqsq qelvalnsil lsiqgiqpkm vmeywtgwfd swggshnild ssevlqtvsa
      361 iikdgssinl ymfhggtnfg fingamhfgd ykadvtsydy dailteagdy takytklrel
      421 fgtfsgvppp pppeltakmv yepvtpsfyl slwdallymd kpitseipin menlpvnngn
      481 gqafgyvlye ttifssgvls glvrdrgqvf lnrvsigfld ytttkitipl tqgytilril
      541 venrgrvnyg nnidsqrkgl ignlylnnkp lknfkiysld mtkqffqrfd mdkwsvvpke
      601 itfpafflgt lsvgiypsdt flklegwvkg vvlvndhnlg rywnvgpqet lylpgvwldk
      661 glnkviifee tmagsmvqst diphlgrnqy vn
//
LOCUS       NP_001423472             253 aa            linear   ROD 14-MAR-2025
DEFINITION  triosephosphate isomerase 1 like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423472 XP_038937855
VERSION     NP_001423472.1
DBSOURCE    REFSEQ: accession NM_001436543.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937855.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1837491.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418971, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..253
                     /product="triosephosphate isomerase 1 like 1 isoform 1"
                     /EC_number="5.3.1.1"
                     /calculated_mol_wt=27284
     Region          8..251
                     /region_name="PTZ00333"
                     /note="triosephosphate isomerase; Provisional"
                     /db_xref="CDD:240365"
     Site            order(16,18,100,170,176,216,235,237..238)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(16,19,50..52,54,57,69,87,90..91,102..103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(18,100,170)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
     CDS             1..253
                     /gene="Tpi1l1"
                     /coded_by="NM_001436543.1:340..1101"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:500959"
                     /db_xref="RGD:1560534"
ORIGIN      
        1 mtimelnsrk ffvggnwkmn gkkkclgeli ctlnaakmpa dtevvcappt ayidfarqkl
       61 dpkiavaaqn cykvtngaft geispgmikd lgatwvvlgh serrhvfges deligqkvnh
      121 alseglgvia cigekldere agitekvvfe qtkaiadnvk dwskvvlaye pvwaigtgkt
      181 atpqqaqevh eklrgwlkcn vseevaqctr iiyggsvtga tckelasqpd vdgflvggas
      241 lkpefvdiin akq
//
LOCUS       NP_001102760             643 aa            linear   ROD 14-MAR-2025
DEFINITION  zinc finger protein 202 [Rattus norvegicus].
ACCESSION   NP_001102760 XP_001059357 XP_576391
VERSION     NP_001102760.1
DBSOURCE    REFSEQ: accession NM_001109290.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Wagner,S., Hess,M.A., Ormonde-Hanson,P., Malandro,J., Hu,H.,
            Chen,M., Kehrer,R., Frodsham,M., Schumacher,C., Beluch,M.,
            Honer,C., Skolnick,M., Ballinger,D. and Bowen,B.R.
  TITLE     A broad role for the zinc finger protein ZNF202 in human lipid
            metabolism
  JOURNAL   J Biol Chem 275 (21), 15685-15690 (2000)
   PUBMED   10748193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_576391.2, XP_001059357.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.27953.1,
                                           SRR26360186.310913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..643
                     /product="zinc finger protein 202"
                     /calculated_mol_wt=73303
     Region          45..155
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          239..299
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <334..626
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          395..415
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(400,402,404,406..407,410..411,414,428,430,434..435,
                     438..439,442,482,484,486,488..489,492..493,496)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          423..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(566,568,570,572..573,576..577,580,594,596,600..601,
                     604..605,608,622,624,626,628..629,632..633,636)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          617..637
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..643
                     /gene="Zfp202"
                     /gene_synonym="RGD1562294"
                     /coded_by="NM_001109290.2:205..2136"
                     /db_xref="GeneID:500981"
                     /db_xref="RGD:1562294"
ORIGIN      
        1 mataleledq dlweeeeegv lmvkleddft cgpesalqgd dpvletshqn frcfryqeas
       61 sprealirlr elchqwlrpe rrtkeqilel lvleqfltvl pgelqswvrg qrpesgeeav
      121 tlveglqkqp rrprrwvtvh vqgqevlsee tlhlgvepes sneqqeptqt ltaeqpheea
      181 lrstdlgtle qeslqheger lpllesevpv sqhadlpteq gsghpemval ltalsqglvt
      241 fkdvalcfsq dqwsdldptq kefygeyvle edcgivvsls fpiprlddps qireeepqvp
      301 gvhesqepae peilsftytg dmseaeeecv eqqdtnksil anteihqtpd weiviednts
      361 rlnerfgtnv skvnsftnir ktmpvhsqsg rqhhcplcak sftcnshlir hlrthtgekp
      421 ykcmecgksy trsshlarhq kvhkvntphk hppnrktvda sqvqseattr vekpytcddc
      481 gkhfrwtsdl vrhqrthtge kpffcticgk sfsqksvltt hqrihvggkp ytcancgenf
      541 seqkqylahr kthvseenhl csecgrsfnh saafakhlkg hasvrncrcd ecgksfsrrd
      601 hlvrhqrtht gekpftcatc gksfsrgyhl irhqrihtgk tkt
//
LOCUS       NP_001102256             581 aa            linear   ROD 14-MAR-2025
DEFINITION  cysteine/serine-rich nuclear protein 1 [Rattus norvegicus].
ACCESSION   NP_001102256 XP_001077652 XP_343505
VERSION     NP_001102256.1
DBSOURCE    REFSEQ: accession NM_001108786.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Ye,X., Lin,J., Lin,Z., Xue,A., Li,L., Zhao,Z., Liu,L., Shen,Y. and
            Cong,B.
  TITLE     Axin1 up-regulated 1 accelerates stress-induced cardiomyocytes
            apoptosis through activating Wnt/beta-catenin signaling
  JOURNAL   Exp Cell Res 359 (2), 441-448 (2017)
   PUBMED   28830684
  REMARK    GeneRIF: Axud1 mediated stress-induced cardiomyocytes apoptosis
            through activating Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Gingras,S., Pelletier,S., Boyd,K. and Ihle,J.N.
  TITLE     Characterization of a family of novel cysteine- serine-rich nuclear
            proteins (CSRNP)
  JOURNAL   PLoS One 2 (8), e808 (2007)
   PUBMED   17726538
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Schmahl,J., Raymond,C.S. and Soriano,P.
  TITLE     PDGF signaling specificity is mediated through multiple immediate
            early genes
  JOURNAL   Nat Genet 39 (1), 52-60 (2007)
   PUBMED   17143286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001077652.1, XP_343505.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360186.1327846.1, SRR26643299.37802.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN06680413,
                                    SAMN06680414 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..581
                     /product="cysteine/serine-rich nuclear protein 1"
                     /note="AXIN1 up-regulated 1"
                     /calculated_mol_wt=62329
     Region          77..301
                     /region_name="CSRNP_N"
                     /note="Cysteine/serine-rich nuclear protein N-terminus;
                     pfam16019"
                     /db_xref="CDD:464977"
     CDS             1..581
                     /gene="Csrnp1"
                     /gene_synonym="Axud1"
                     /coded_by="NM_001108786.2:111..1856"
                     /db_xref="GeneID:363165"
                     /db_xref="RGD:1305999"
ORIGIN      
        1 magiqkrkfd qleeddcsss slssgdlsps ppsssaspaw tseeeglgdq ppqpdqdssg
       61 iqslmppsil kraprerpgh vafdgitvyy fprcqgftsv pshggctlgm asrhstcrlf
      121 slaefkqeqf rarreklrrr lkeeklemlk wklsvsgvpe agadvpltvd aiddasveed
      181 lavavaggrl eeanflqpyp prqrrallra sgvrridree krelqalrqs redcgchcdg
      241 vcdpetcsci lagikcqmdh tsfpcgccse gcenphgrve fnqarvqthf ihtltrlqme
      301 qgaeslgdpe spmedvpveq tvvspfppsk ptmsndlgds scgsdmtdss ttyssggsgs
      361 rseapnhlah pslpgssfrs gidedsleqi lnfsdsdlgi eeeeeeggsv gnldnlscfh
      421 ladifgtgdp gslaswthsq fgsslpsgil denanldasc flssgleglr egslpsssgs
      481 pegeaaqsss ldlslsscds fellqslpdy slgphytsrr vsgsldslet fhpspsfspp
      541 rdasfldsli glsepvtdvl apllesqfed tavvpldpvp v
//
LOCUS       NP_001423482             345 aa            linear   ROD 14-MAR-2025
DEFINITION  layilin isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423482 XP_063122057
VERSION     NP_001423482.1
DBSOURCE    REFSEQ: accession NM_001436553.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_063122057.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.622379.1,
                                           SRR21887621.972806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345331,
                                           SAMN11044071 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..345
                     /product="layilin isoform 2 precursor"
                     /calculated_mol_wt=36895
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          30..178
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(140,144,146,162,164..167,170..172)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     CDS             1..345
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001436553.1:122..1159"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgq rfcwegtrrp cyrviyfhdt sqrrnfeeak
       61 eacmkdggql asietadeqr lienfieslq asdgdfwigl krleekqhns tacqdlyawt
      121 dgslsqfrnw ymdepscese vcvvmyhqps appgiggpym fqwnddrcnt kknfickysd
      181 dkpsttpsls pgeaalnlay ilipsiplfl llvvtsavcw vwicrrkreq tdpptkeqht
      241 iwptphqens pdlevynvir kqseadlaep rpdlknisfr vcsgeampdd tscdydnmvi
      301 npsesglvtl asmegrfvtn diyefspdrm grskesgwve neiyy
//
LOCUS       NP_001423464             581 aa            linear   ROD 14-MAR-2025
DEFINITION  cysteine/serine-rich nuclear protein 1 [Rattus norvegicus].
ACCESSION   NP_001423464
VERSION     NP_001423464.1
DBSOURCE    REFSEQ: accession NM_001436535.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Ye,X., Lin,J., Lin,Z., Xue,A., Li,L., Zhao,Z., Liu,L., Shen,Y. and
            Cong,B.
  TITLE     Axin1 up-regulated 1 accelerates stress-induced cardiomyocytes
            apoptosis through activating Wnt/beta-catenin signaling
  JOURNAL   Exp Cell Res 359 (2), 441-448 (2017)
   PUBMED   28830684
  REMARK    GeneRIF: Axud1 mediated stress-induced cardiomyocytes apoptosis
            through activating Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Gingras,S., Pelletier,S., Boyd,K. and Ihle,J.N.
  TITLE     Characterization of a family of novel cysteine- serine-rich nuclear
            proteins (CSRNP)
  JOURNAL   PLoS One 2 (8), e808 (2007)
   PUBMED   17726538
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Schmahl,J., Raymond,C.S. and Soriano,P.
  TITLE     PDGF signaling specificity is mediated through multiple immediate
            early genes
  JOURNAL   Nat Genet 39 (1), 52-60 (2007)
   PUBMED   17143286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.32629.1,
                                           SRR26643299.37801.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840115,
                                           SAMN12840117 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..581
                     /product="cysteine/serine-rich nuclear protein 1"
                     /note="AXIN1 up-regulated 1"
                     /calculated_mol_wt=62329
     Region          77..301
                     /region_name="CSRNP_N"
                     /note="Cysteine/serine-rich nuclear protein N-terminus;
                     pfam16019"
                     /db_xref="CDD:464977"
     CDS             1..581
                     /gene="Csrnp1"
                     /gene_synonym="Axud1"
                     /coded_by="NM_001436535.1:164..1909"
                     /db_xref="GeneID:363165"
                     /db_xref="RGD:1305999"
ORIGIN      
        1 magiqkrkfd qleeddcsss slssgdlsps ppsssaspaw tseeeglgdq ppqpdqdssg
       61 iqslmppsil kraprerpgh vafdgitvyy fprcqgftsv pshggctlgm asrhstcrlf
      121 slaefkqeqf rarreklrrr lkeeklemlk wklsvsgvpe agadvpltvd aiddasveed
      181 lavavaggrl eeanflqpyp prqrrallra sgvrridree krelqalrqs redcgchcdg
      241 vcdpetcsci lagikcqmdh tsfpcgccse gcenphgrve fnqarvqthf ihtltrlqme
      301 qgaeslgdpe spmedvpveq tvvspfppsk ptmsndlgds scgsdmtdss ttyssggsgs
      361 rseapnhlah pslpgssfrs gidedsleqi lnfsdsdlgi eeeeeeggsv gnldnlscfh
      421 ladifgtgdp gslaswthsq fgsslpsgil denanldasc flssgleglr egslpsssgs
      481 pegeaaqsss ldlslsscds fellqslpdy slgphytsrr vsgsldslet fhpspsfspp
      541 rdasfldsli glsepvtdvl apllesqfed tavvpldpvp v
//
LOCUS       NP_001423484             357 aa            linear   ROD 14-MAR-2025
DEFINITION  layilin isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001423484 XP_008764550
VERSION     NP_001423484.1
DBSOURCE    REFSEQ: accession NM_001436555.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_008764550.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1633603.1,
                                           SRR26643290.29285.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMN06621351 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..357
                     /product="layilin isoform 4 precursor"
                     /calculated_mol_wt=38374
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          30..178
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(140,144,146,162,164..167,170..172)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     CDS             1..357
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001436555.1:122..1195"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgq rfcwegtrrp cyrviyfhdt sqrrnfeeak
       61 eacmkdggql asietadeqr lienfieslq asdgdfwigl krleekqhns tacqdlyawt
      121 dgslsqfrnw ymdepscese vcvvmyhqps appgiggpym fqwnddrcnt kknfickysd
      181 geatepaapi lpeetleidt kerreaalnl ayilipsipl flllvvtsav cwvwicrrkr
      241 eqtdpptkeq htiwptphqe nspdlevynv irkqseadla eprpdlknis frvcsgeamp
      301 ddtscdydnm vinpsesglv tlasmegrfv tndiyefspd rmgrskesgw veneiyy
//
LOCUS       NP_001423461             207 aa            linear   ROD 14-MAR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 [Rattus norvegicus].
ACCESSION   NP_001423461 XP_063121864
VERSION     NP_001423461.1
DBSOURCE    REFSEQ: accession NM_001436532.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Asai,M., Ramachandrappa,S., Joachim,M., Shen,Y., Zhang,R.,
            Nuthalapati,N., Ramanathan,V., Strochlic,D.E., Ferket,P.,
            Linhart,K., Ho,C., Novoselova,T.V., Garg,S., Ridderstrale,M.,
            Marcus,C., Hirschhorn,J.N., Keogh,J.M., O'Rahilly,S., Chan,L.F.,
            Clark,A.J., Farooqi,I.S. and Majzoub,J.A.
  TITLE     Loss of function of the melanocortin 2 receptor accessory protein 2
            is associated with mammalian obesity
  JOURNAL   Science 341 (6143), 275-278 (2013)
   PUBMED   23869016
  REMARK    Erratum:[Science. 2013 Aug 30;341(6149):959]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_063121864.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1641764.1,
                                           SRR26360176.665737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984027, SAMN16418971
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="melanocortin-2 receptor accessory protein 2"
                     /calculated_mol_wt=23660
     Region          16..101
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     CDS             1..207
                     /gene="Mrap2"
                     /gene_synonym="RGD1309873"
                     /coded_by="NM_001436532.1:75..698"
                     /db_xref="GeneID:363112"
                     /db_xref="RGD:1309873"
ORIGIN      
        1 memsaqrlts nrtspqspsn sdytweyeyy eigpvsfegl kahkysivig fwvglavfvi
       61 fmffvltllt ktgaphqdna essekrfrmn sfvsdfgkpl esdkvfsrqg neesrslfhc
      121 yinevehldr vkvchrttai dsdvhlqeai rssgrpeeel trfmqfdipn fvntdqnsfg
      181 eddllisepp vllenkpvsq tsrtdld
//
LOCUS       NP_001423485             330 aa            linear   ROD 14-MAR-2025
DEFINITION  layilin isoform 5 precursor [Rattus norvegicus].
ACCESSION   NP_001423485 XP_038937887
VERSION     NP_001423485.1
DBSOURCE    REFSEQ: accession NM_001436556.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937887.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.3439546.1,
                                           SRR21887623.3439547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..330
                     /product="layilin isoform 5 precursor"
                     /calculated_mol_wt=34969
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          30..178
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(140,144,146,162,164..167,170..172)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153065"
     CDS             1..330
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001436556.1:122..1114"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgq rfcwegtrrp cyrviyfhdt sqrrnfeeak
       61 eacmkdggql asietadeqr lienfieslq asdgdfwigl krleekqhns tacqdlyawt
      121 dgslsqfrnw ymdepscese vcvvmyhqps appgiggpym fqwnddrcnt kknfickysd
      181 dkpsttpsls pggeatepaa pilpeetlei dtkerreaal nlayilipsi plflllvvts
      241 avcwvwicrr kreqtdpptk eqhtiwptph qenspdlevy nvirkqsead laeprpdlkn
      301 isfrvcsgea mpddtscdyd nmvinpsesg
//
LOCUS       NP_001028244             249 aa            linear   ROD 14-MAR-2025
DEFINITION  triosephosphate isomerase 1 like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001028244 XP_576370
VERSION     NP_001028244.2
DBSOURCE    REFSEQ: accession NM_001033072.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced NP_001028244.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22399489.2845270.1, AY461585.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..249
                     /product="triosephosphate isomerase 1 like 1 isoform 2"
                     /EC_number="5.3.1.1"
                     /calculated_mol_wt=26750
     Region          2..247
                     /region_name="PTZ00333"
                     /note="triosephosphate isomerase; Provisional"
                     /db_xref="CDD:240365"
     Site            order(12,14,96,166,172,212,231,233..234)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(12,15,46..48,50,53,65,83,86..87,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(14,96,166)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
     CDS             1..249
                     /gene="Tpi1l1"
                     /coded_by="NM_001033072.2:28..777"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:500959"
                     /db_xref="RGD:1560534"
ORIGIN      
        1 mapsrkffvg gnwkmngkkk clgelictln aakmpadtev vcapptayid farqkldpki
       61 avaaqncykv tngaftgeis pgmikdlgat wvvlghserr hvfgesdeli gqkvnhalse
      121 glgviacige kldereagit ekvvfeqtka iadnvkdwsk vvlayepvwa igtgktatpq
      181 qaqevheklr gwlkcnvsee vaqctriiyg gsvtgatcke lasqpdvdgf lvggaslkpe
      241 fvdiinakq
//
LOCUS       NP_001423489             695 aa            linear   ROD 14-MAR-2025
DEFINITION  beta-galactosidase-1-like protein 2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423489 XP_038937928
VERSION     NP_001423489.1
DBSOURCE    REFSEQ: accession NM_001436560.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937928.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.27718.1,
                                           SRR22582416.1079335.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..695
                     /product="beta-galactosidase-1-like protein 2 isoform 4"
                     /EC_number="3.2.1.23"
                     /note="beta-galactosidase-1-like protein 2"
                     /calculated_mol_wt=78330
     Region          53..366
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     CDS             1..695
                     /gene="Glb1l2"
                     /gene_synonym="RGD1564436"
                     /coded_by="NM_001436560.1:43..2130"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:503194"
                     /db_xref="RGD:1564436"
ORIGIN      
        1 mpkwslrrrp grtlglllll vlsflvlrrl nwtsvlplwl qrqrlglrtk gpnfmledst
       61 fqilggsihy frvpreywrd rllklkacgl ntlttyvpwn lhepergkfd fsgnldleaf
      121 iwlaakiglw vilrpgpyic seidlgglps wllqdpdmkl rttypgftka vdlyfdhlms
      181 rvvplqykhg gpiiavqven eygsyngdha ympyikkale drgiiemllt sdnkdglekg
      241 vvdgvlatin lqsqqelval nsillsiqgi qpkmvmeywt gwfdswggsh nildssevlq
      301 tvsaiikdgs sinlymfhgg tnfgfingam hfgdykadvt sydydailte agdytakytk
      361 lrelfgtfsg vppppppelt akmvyepvtp sfylslwdal lymdkpitse ipinmenlpv
      421 nngngqafgy vlyettifss gvlsglvrdr gqvflnrvsi gfldytttki tipltqgyti
      481 lrilvenrgr vnygnnidsq rkglignlyl nnkplknfki ysldmtkqff qrfdmdkwsv
      541 vpkeitfpaf flgtlsvgiy psdtflkleg wvkgvvlvnd hnlgrywnvg pqetlylpgv
      601 wldkglnkhv qptlalqhrl vlpgpvnhir dlspsrvlap tpncsetlla ppshfclltv
      661 wdhtcgiltp apssvcpqph grntdswpsl svacm
//
LOCUS       NP_001423491             365 aa            linear   ROD 14-MAR-2025
DEFINITION  transmembrane protein 25 precursor [Rattus norvegicus].
ACCESSION   NP_001423491 XP_006243022
VERSION     NP_001423491.1
DBSOURCE    REFSEQ: accession NM_001436562.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Zhang,H., Tian,X., Lu,X., Xu,D., Guo,Y., Dong,Z., Li,Y., Ma,Y.,
            Chen,C., Yang,Y., Yang,M., Yang,Y., Liu,F., Zhou,R., He,M., Xiao,F.
            and Wang,X.
  TITLE     TMEM25 modulates neuronal excitability and NMDA receptor subunit
            NR2B degradation
  JOURNAL   J Clin Invest 129 (9), 3864-3876 (2019)
   PUBMED   31424425
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243022.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.34799.1,
                                           SRR26643289.22724.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..365
                     /product="transmembrane protein 25 precursor"
                     /calculated_mol_wt=36461
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2760
     Region          27..118
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          48..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..365
                     /gene="Tmem25"
                     /coded_by="NM_001436562.1:89..1186"
                     /db_xref="GeneID:689172"
                     /db_xref="RGD:1596132"
ORIGIN      
        1 melplsqatl rhtllllpal lssgqgelap qidgqtwaer alrenehhaf tcrvaggsat
       61 prlawyldgq lqkattsrll svggdafsgg tstftvtaqr sqhelncslq dpgsgrpana
      121 svilnvqfkp eiaqvgakyq eaqgpgllvv lfalvranpp anvtwidqdg pvtvnasdfl
      181 vldaqnypwl tnhtvqlqlr slahnlsvva tndvgvtsas lpapgllatr ievpllgivv
      241 agglafgtlv gfstlvaclv crkekktkgp srrpslissd snnlklnnvr lprenmslps
      301 nlqlndltpd irgkaterpm aqhssrpell eaepggllts rgfirlpmlg yiyrvssvss
      361 deiwl
//
LOCUS       NP_001423480             571 aa            linear   ROD 14-MAR-2025
DEFINITION  NXPE family member 1 [Rattus norvegicus].
ACCESSION   NP_001423480 XP_006243081
VERSION     NP_001423480.1
DBSOURCE    REFSEQ: accession NM_001436551.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243081.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1210819.1,
                                           SRR26360186.526197.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..571
                     /product="NXPE family member 1"
                     /calculated_mol_wt=64754
     Region          <155..276
                     /region_name="Neurexophilin"
                     /note="pfam06312"
                     /db_xref="CDD:428882"
     CDS             1..571
                     /gene="Nxpe1"
                     /gene_synonym="RGD1566243"
                     /coded_by="NM_001436551.1:60..1775"
                     /db_xref="GeneID:500992"
                     /db_xref="RGD:1566243"
ORIGIN      
        1 mwimfstimr qkrlliftsf lvviwvifvi sqnsaklwtt lntstsfnpw ttstkssppe
       61 ipmnqstlpt etklreeipk mtghqedksp tetelkvrei lekldgqipp rpfahlnntt
      121 sathstatil npqdtycvgd qldvllaakd yfghrkeygg dflrarmssp alkagasgkv
      181 tdfnngtyli sftlfwegqv slsillmhps egvsalwrar nqgygriafk gtfvngtskv
      241 taecglilns sselckylyr ggeevfycvk pqhmpcealt yvctshqdvs yltakeknlf
      301 qksnigvemm khpkyivvsq cnksengrkr ceigmeiptp sgytlqgrwv saqctqrllt
      361 ssqindclkg kliyllgdst lrqwieylpk vaktlrpfdl hgtglykkhl ildaerhtlv
      421 ewkkhshpfi tvqlysvidd gyipqeidrl pgdkdtvivi tvgqhfrpfp melfvhrvin
      481 iqkaigrlfl rspdtkviik menirernld tekfgdfhgy vqylttkeif kdlhvgtida
      541 wdmtiahgtn vlhppaavig nqidvflnyi c
//
LOCUS       NP_001020925             387 aa            linear   ROD 14-MAR-2025
DEFINITION  endonuclease 8-like 1 [Rattus norvegicus].
ACCESSION   NP_001020925 XP_345945
VERSION     NP_001020925.1
DBSOURCE    REFSEQ: accession NM_001025754.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ma,H., Wang,J., Abdel-Rahman,S.Z., Hazra,T.K., Boor,P.J. and
            Khan,M.F.
  TITLE     Induction of NEIL1 and NEIL2 DNA glycosylases in aniline-induced
            splenic toxicity
  JOURNAL   Toxicol Appl Pharmacol 251 (1), 1-7 (2011)
   PUBMED   21145906
  REMARK    GeneRIF: In the spleen aniline-induced oxidative stress is
            associated with an induction of NEIL1/2.
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Das,A., Boldogh,I., Lee,J.W., Harrigan,J.A., Hegde,M.L.,
            Piotrowski,J., de Souza Pinto,N., Ramos,W., Greenberg,M.M.,
            Hazra,T.K., Mitra,S. and Bohr,V.A.
  TITLE     The human Werner syndrome protein stimulates repair of oxidative
            DNA base damage by the DNA glycosylase NEIL1
  JOURNAL   J Biol Chem 282 (36), 26591-26602 (2007)
   PUBMED   17611195
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Takao,M., Kanno,S., Kobayashi,K., Zhang,Q.M., Yonei,S., van der
            Horst,G.T. and Yasui,A.
  TITLE     A back-up glycosylase in Nth1 knock-out mice is a functional Nei
            (endonuclease VIII) homologue
  JOURNAL   J Biol Chem 277 (44), 42205-42213 (2002)
   PUBMED   12200441
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 22, 2005 this sequence version replaced XP_345945.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099125.1, SRR26643296.21860.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..387
                     /product="endonuclease 8-like 1"
                     /EC_number="4.2.99.18"
                     /note="endonuclease VIII-like 1; nei endonuclease
                     VIII-like 1"
                     /calculated_mol_wt=43218
     Region          1..127
                     /region_name="FpgNei_N"
                     /note="N-terminal domain of Fpg (formamidopyrimidine-DNA
                     glycosylase, MutM)_Nei (endonuclease VIII) base-excision
                     repair DNA glycosylases; cl03119"
                     /db_xref="CDD:470740"
     Site            order(2..3,54,78,80..82,95..96)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176801"
     Site            2
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:176801"
     Site            order(3..6,8..9,12,51..55)
                     /site_type="other"
                     /note="H2TH interface [polypeptide binding]"
                     /db_xref="CDD:176801"
     Site            order(3,54)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:176801"
     Region          <52..>206
                     /region_name="fpg"
                     /note="DNA-formamidopyrimidine glycosylase; TIGR00577"
                     /db_xref="CDD:273150"
     Region          252..290
                     /region_name="Neil1-DNA_bind"
                     /note="Endonuclease VIII-like 1, DNA bind; pfam09292"
                     /db_xref="CDD:462745"
     CDS             1..387
                     /gene="Neil1"
                     /coded_by="NM_001025754.2:84..1247"
                     /db_xref="GeneID:367090"
                     /db_xref="RGD:1306077"
ORIGIN      
        1 mpegpelhla shfvneickg lvfggcveks svsrnpevpf essayhisal argkelrltl
       61 splpgshppq kplslvfrfg msgsfqlvpa ealprhahlr fytappaprl alcfvdirrf
      121 ghwdpggewq pgrgpcvlle yerfrenvlr nlsdkafdrp icealldqrf fngignylra
      181 eilyrlkipp fekartvlea lqqcrlspel tlsqkvkakl qnpdllelch lvpkevvqlg
      241 gkgygperge edfaafrawl rcyavpgmss lrdrhgrtiw fqgdpgplap kggrsrkkks
      301 qetqleaedr kedppsksis rtqrarkhcp knvpqqsega slpqnletpa vpekgkrrgr
      361 rastgrhrgp kskpdtqpre ageisas
//
LOCUS       NP_001423459             207 aa            linear   ROD 14-MAR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 [Rattus norvegicus].
ACCESSION   NP_001423459 XP_006243549
VERSION     NP_001423459.1
DBSOURCE    REFSEQ: accession NM_001436530.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Asai,M., Ramachandrappa,S., Joachim,M., Shen,Y., Zhang,R.,
            Nuthalapati,N., Ramanathan,V., Strochlic,D.E., Ferket,P.,
            Linhart,K., Ho,C., Novoselova,T.V., Garg,S., Ridderstrale,M.,
            Marcus,C., Hirschhorn,J.N., Keogh,J.M., O'Rahilly,S., Chan,L.F.,
            Clark,A.J., Farooqi,I.S. and Majzoub,J.A.
  TITLE     Loss of function of the melanocortin 2 receptor accessory protein 2
            is associated with mammalian obesity
  JOURNAL   Science 341 (6143), 275-278 (2013)
   PUBMED   23869016
  REMARK    Erratum:[Science. 2013 Aug 30;341(6149):959]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.55627.1,
                                           SRR26360190.2604982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840109
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="melanocortin-2 receptor accessory protein 2"
                     /calculated_mol_wt=23660
     Region          16..101
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     CDS             1..207
                     /gene="Mrap2"
                     /gene_synonym="RGD1309873"
                     /coded_by="NM_001436530.1:333..956"
                     /db_xref="GeneID:363112"
                     /db_xref="RGD:1309873"
ORIGIN      
        1 memsaqrlts nrtspqspsn sdytweyeyy eigpvsfegl kahkysivig fwvglavfvi
       61 fmffvltllt ktgaphqdna essekrfrmn sfvsdfgkpl esdkvfsrqg neesrslfhc
      121 yinevehldr vkvchrttai dsdvhlqeai rssgrpeeel trfmqfdipn fvntdqnsfg
      181 eddllisepp vllenkpvsq tsrtdld
//
LOCUS       NP_001423466             387 aa            linear   ROD 14-MAR-2025
DEFINITION  endonuclease 8-like 1 [Rattus norvegicus].
ACCESSION   NP_001423466 XP_038937802
VERSION     NP_001423466.1
DBSOURCE    REFSEQ: accession NM_001436537.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ma,H., Wang,J., Abdel-Rahman,S.Z., Hazra,T.K., Boor,P.J. and
            Khan,M.F.
  TITLE     Induction of NEIL1 and NEIL2 DNA glycosylases in aniline-induced
            splenic toxicity
  JOURNAL   Toxicol Appl Pharmacol 251 (1), 1-7 (2011)
   PUBMED   21145906
  REMARK    GeneRIF: In the spleen aniline-induced oxidative stress is
            associated with an induction of NEIL1/2.
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Das,A., Boldogh,I., Lee,J.W., Harrigan,J.A., Hegde,M.L.,
            Piotrowski,J., de Souza Pinto,N., Ramos,W., Greenberg,M.M.,
            Hazra,T.K., Mitra,S. and Bohr,V.A.
  TITLE     The human Werner syndrome protein stimulates repair of oxidative
            DNA base damage by the DNA glycosylase NEIL1
  JOURNAL   J Biol Chem 282 (36), 26591-26602 (2007)
   PUBMED   17611195
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Takao,M., Kanno,S., Kobayashi,K., Zhang,Q.M., Yonei,S., van der
            Horst,G.T. and Yasui,A.
  TITLE     A back-up glycosylase in Nth1 knock-out mice is a functional Nei
            (endonuclease VIII) homologue
  JOURNAL   J Biol Chem 277 (44), 42205-42213 (2002)
   PUBMED   12200441
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937802.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.11283.1,
                                           SRR26643292.33806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..387
                     /product="endonuclease 8-like 1"
                     /EC_number="4.2.99.18"
                     /note="endonuclease VIII-like 1; nei endonuclease
                     VIII-like 1"
                     /calculated_mol_wt=43218
     Region          1..127
                     /region_name="FpgNei_N"
                     /note="N-terminal domain of Fpg (formamidopyrimidine-DNA
                     glycosylase, MutM)_Nei (endonuclease VIII) base-excision
                     repair DNA glycosylases; cl03119"
                     /db_xref="CDD:470740"
     Site            order(2..3,54,78,80..82,95..96)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176801"
     Site            2
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:176801"
     Site            order(3..6,8..9,12,51..55)
                     /site_type="other"
                     /note="H2TH interface [polypeptide binding]"
                     /db_xref="CDD:176801"
     Site            order(3,54)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:176801"
     Region          <52..>206
                     /region_name="fpg"
                     /note="DNA-formamidopyrimidine glycosylase; TIGR00577"
                     /db_xref="CDD:273150"
     Region          252..290
                     /region_name="Neil1-DNA_bind"
                     /note="Endonuclease VIII-like 1, DNA bind; pfam09292"
                     /db_xref="CDD:462745"
     CDS             1..387
                     /gene="Neil1"
                     /coded_by="NM_001436537.1:108..1271"
                     /db_xref="GeneID:367090"
                     /db_xref="RGD:1306077"
ORIGIN      
        1 mpegpelhla shfvneickg lvfggcveks svsrnpevpf essayhisal argkelrltl
       61 splpgshppq kplslvfrfg msgsfqlvpa ealprhahlr fytappaprl alcfvdirrf
      121 ghwdpggewq pgrgpcvlle yerfrenvlr nlsdkafdrp icealldqrf fngignylra
      181 eilyrlkipp fekartvlea lqqcrlspel tlsqkvkakl qnpdllelch lvpkevvqlg
      241 gkgygperge edfaafrawl rcyavpgmss lrdrhgrtiw fqgdpgplap kggrsrkkks
      301 qetqleaedr kedppsksis rtqrarkhcp knvpqqsega slpqnletpa vpekgkrrgr
      361 rastgrhrgp kskpdtqpre ageisas
//
LOCUS       NP_113877                196 aa            linear   ROD 14-MAR-2025
DEFINITION  beta-crystallin A4 [Rattus norvegicus].
ACCESSION   NP_113877
VERSION     NP_113877.1
DBSOURCE    REFSEQ: accession NM_031689.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Li,W., Ji,Q., Wei,Z., Chen,Y.L., Zhang,Z., Yin,X., Aghmiuni,S.K.,
            Liu,M., Chen,W., Shi,L., Chen,Q., Du,X., Yu,L., Cao,M.J., Wang,Z.,
            Huang,S., Jin,T. and Wang,Q.
  TITLE     Biochemical characterization of G64W mutant of acidic
            beta-crystallin 4
  JOURNAL   Exp Eye Res 186, 107712 (2019)
   PUBMED   31254514
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Billingsley,G., Santhiya,S.T., Paterson,A.D., Ogata,K., Wodak,S.,
            Hosseini,S.M., Manisastry,S.M., Vijayalakshmi,P., Gopinath,P.M.,
            Graw,J. and Heon,E.
  TITLE     CRYBA4, a novel human cataract gene, is also involved in
            microphthalmia
  JOURNAL   Am J Hum Genet 79 (4), 702-709 (2006)
   PUBMED   16960806
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Lampi,K.J., Shih,M., Ueda,Y., Shearer,T.R. and David,L.L.
  TITLE     Lens proteomics: analysis of rat crystallin sequences and
            two-dimensional electrophoresis map
  JOURNAL   Invest Ophthalmol Vis Sci 43 (1), 216-224 (2002)
   PUBMED   11773034
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Takeuchi,N. and Kamei,A.
  TITLE     Crystallin proteins in lenses of hereditary cataractous rat, ICR/f
  JOURNAL   Biol Pharm Bull 23 (3), 283-290 (2000)
   PUBMED   10726880
REFERENCE   5  (residues 1 to 196)
  AUTHORS   David,L.L. and Shearer,T.R.
  TITLE     Beta-crystallins insolubilized by calpain II in vitro contain
            cleavage sites similar to beta-crystallins insolubilized during
            cataract
  JOURNAL   FEBS Lett 324 (3), 265-270 (1993)
   PUBMED   8405363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF013247.1, SRR26360194.513503.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093047 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..196
                     /product="beta-crystallin A4"
                     /note="beta-A4 crystallin"
                     /calculated_mol_wt=22251
     Region          2..11
                     /region_name="N-terminal arm"
                     /note="propagated from UniProtKB/Swiss-Prot (P56374.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000269|PubMed:11773034; propagated from
                     UniProtKB/Swiss-Prot (P56374.2)"
     Region          13..97
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     Region          99..104
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P56374.2)"
     Region          106..194
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     CDS             1..196
                     /gene="Cryba4"
                     /coded_by="NM_031689.2:39..629"
                     /db_xref="GeneID:64348"
                     /db_xref="RGD:61962"
ORIGIN      
        1 mtlqctksag hwrvvvwdee gfqgrrheft aecpsvldlg fetvrslkvl sgawvgfeha
       61 gfqgqqyvle rgdypgwdaw ggntaypaer ltsfrpvaca nhrdsrltif eqenflgrkg
      121 elsddypslq amgwdgtevg sfhvqsgawv csqfpgyrgf qyvlesdhhs gdykhfrewg
      181 shahtfqvqs vrriqq
//
LOCUS       NP_001423353            1256 aa            linear   ROD 14-MAR-2025
DEFINITION  cohesin subunit SA-3 [Rattus norvegicus].
ACCESSION   NP_001423353 XP_006249082
VERSION     NP_001423353.1
DBSOURCE    REFSEQ: accession NM_001436424.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Fukuda,T., Fukuda,N., Agostinho,A., Hernandez-Hernandez,A.,
            Kouznetsova,A. and Hoog,C.
  TITLE     STAG3-mediated stabilization of REC8 cohesin complexes promotes
            chromosome synapsis during meiosis
  JOURNAL   EMBO J 33 (11), 1243-1255 (2014)
   PUBMED   24797475
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 1256)
  AUTHORS   Llano,E., Herran,Y., Garcia-Tunon,I., Gutierrez-Caballero,C., de
            Alava,E., Barbero,J.L., Schimenti,J., de Rooij,D.G.,
            Sanchez-Martin,M. and Pendas,A.M.
  TITLE     Meiotic cohesin complexes are essential for the formation of the
            axial element in mice
  JOURNAL   J Cell Biol 197 (7), 877-885 (2012)
   PUBMED   22711701
REFERENCE   4  (residues 1 to 1256)
  AUTHORS   Gutierrez-Caballero,C., Herran,Y., Sanchez-Martin,M., Suja,J.A.,
            Barbero,J.L., Llano,E. and Pendas,A.M.
  TITLE     Identification and molecular characterization of the mammalian
            alpha-kleisin RAD21L
  JOURNAL   Cell Cycle 10 (9), 1477-1487 (2011)
   PUBMED   21527826
REFERENCE   5  (residues 1 to 1256)
  AUTHORS   Lee,J. and Hirano,T.
  TITLE     RAD21L, a novel cohesin subunit implicated in linking homologous
            chromosomes in mammalian meiosis
  JOURNAL   J Cell Biol 192 (2), 263-276 (2011)
   PUBMED   21242291
REFERENCE   6  (residues 1 to 1256)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   7  (residues 1 to 1256)
  AUTHORS   Li,X.C. and Schimenti,J.C.
  TITLE     Mouse pachytene checkpoint 2 (trip13) is required for completing
            meiotic recombination but not synapsis
  JOURNAL   PLoS Genet 3 (8), e130 (2007)
   PUBMED   17696610
  REMARK    Erratum:[PLoS Genet. 2007 Sep 7;3(9):e168. Li, Xin [corrected to
            Li, Xin Chenglin]]
REFERENCE   8  (residues 1 to 1256)
  AUTHORS   Kouznetsova,A., Novak,I., Jessberger,R. and Hoog,C.
  TITLE     SYCP2 and SYCP3 are required for cohesin core integrity at
            diplotene but not for centromere cohesion at the first meiotic
            division
  JOURNAL   J Cell Sci 118 (Pt 10), 2271-2278 (2005)
   PUBMED   15870106
REFERENCE   9  (residues 1 to 1256)
  AUTHORS   Bayes,M., Prieto,I., Noguchi,J., Barbero,J.L. and Perez Jurado,L.A.
  TITLE     Evaluation of the Stag3 gene and the synaptonemal complex in a rat
            model (as/as) for male infertility
  JOURNAL   Mol Reprod Dev 60 (3), 414-417 (2001)
   PUBMED   11599053
REFERENCE   10 (residues 1 to 1256)
  AUTHORS   Pezzi,N., Prieto,I., Kremer,L., Perez Jurado,L.A., Valero,C., Del
            Mazo,J., Martinez-A,C. and Barbero,J.L.
  TITLE     STAG3, a novel gene encoding a protein involved in meiotic
            chromosome pairing and location of STAG3-related genes flanking the
            Williams-Beuren syndrome deletion
  JOURNAL   FASEB J 14 (3), 581-592 (2000)
   PUBMED   10698974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006249082.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression, longest
                                         protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..1256
                     /product="cohesin subunit SA-3"
                     /note="cohesin subunit SA-3-like; SCC3 homolog 3;
                     stromalin-3; stromal antigen 3"
                     /calculated_mol_wt=141821
     Region          1..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Region          102..>426
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          188..301
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Region          1096..1169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Region          1230..1256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99M76.1)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70576; propagated from
                     UniProtKB/Swiss-Prot (Q99M76.1)"
     CDS             1..1256
                     /gene="Stag3"
                     /coded_by="NM_001436424.1:104..3874"
                     /db_xref="GeneID:114522"
                     /db_xref="RGD:621333"
ORIGIN      
        1 mptlwspstq hhgsssgsms splrksvrca qmalspcssn iqpcddrdsq gtaewdssst
       61 sedsdfedsl rrnvrkraak rppkaipvak hpkkqshivp ggndknksvp ptsdlfdavk
      121 aarscaqslv dewlenykqd enagflelvn ffiracgcks tvtpemfktm snseiiqhlt
      181 eefnedsgdy pltapgpswk kfqgsfcefv ktlvcqcqys llfdgfpmdd lislliglsd
      241 sqvrafrhts tlaamklmts lvkvalqlsl hkdnnqrqye aernkgpeqr aperleslle
      301 krkefqenqe eiegmmnaif rgvfvhryrd ilpeiravci eeigcwmqsy stsflndsyl
      361 kyigwtlhdk hkevrlkcvk alaglysnqe lssrmelftn rfkdrmvsmv mdresevave
      421 airlltlilk nmegvltsad cekiysivyi snramassag efvywkifhp ecgakavsgr
      481 errrspqaqr tfiylllaff mesehhdhaa ylvdslwdca gsylkdwesl tslllqkdqn
      541 lgdmqermli eilvssarqa aeghppvgri tgkksltake rklqaydkvk laehlipllp
      601 qllakfsada envapllrll syfdlniyct qrlekhlell lqqlqevvvk hvepevleaa
      661 ahalyllckp eftffsrvdf arsqlvdllt drfqqelddl mqssfldede vysltatlkr
      721 lsafynahdl trweisepcs rllrkavdtg evphqvilpa ltlvyfsilw tvthisests
      781 qkqlmslkkr mvafcelcqs clsdvdpeiq eqafvllsdl llifspqmvv ggrdflrplv
      841 ffpeatlqse lasflmdhvf lqpgelgngq sqedhvqiel lhqrrrllag fcklllygvl
      901 eldaasdvfk hynkfyedyg diiketltra rqidrcqcsr illlslkqly teliqeqgpq
      961 dltelpafie mrdlarrfal sfgpqqlhnr dlvvmlhkeg ikfslselpp agssreppni
     1021 aflellsefs prlfhqdkql llsylekclq rvsmapshpw gpvttychsl hlventaeas
     1081 sqgpphskkr cievprrlqe eesssqgesl qlnsgpttpt ltstavkrrq sprtvgkrqk
     1141 ggpgpgpgpg pgpgpgpgpg pgpgpgpeli csqqlsgtqr lkmssapcfq ircdpsgsgl
     1201 gkqmtrlslm eedeeeelrl ldeewqcgdk llhspsspse hgldlldtte lnmedf
//
LOCUS       NP_001102998             365 aa            linear   ROD 14-MAR-2025
DEFINITION  transmembrane protein 25 precursor [Rattus norvegicus].
ACCESSION   NP_001102998 XP_001060928
VERSION     NP_001102998.1
DBSOURCE    REFSEQ: accession NM_001109528.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Zhang,H., Tian,X., Lu,X., Xu,D., Guo,Y., Dong,Z., Li,Y., Ma,Y.,
            Chen,C., Yang,Y., Yang,M., Yang,Y., Liu,F., Zhou,R., He,M., Xiao,F.
            and Wang,X.
  TITLE     TMEM25 modulates neuronal excitability and NMDA receptor subunit
            NR2B degradation
  JOURNAL   J Clin Invest 129 (9), 3864-3876 (2019)
   PUBMED   31424425
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473975.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001060928.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132308, SAMEA5760393
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..365
                     /product="transmembrane protein 25 precursor"
                     /calculated_mol_wt=36461
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2760
     Region          27..118
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          48..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..365
                     /gene="Tmem25"
                     /coded_by="NM_001109528.1:137..1234"
                     /db_xref="GeneID:689172"
                     /db_xref="RGD:1596132"
ORIGIN      
        1 melplsqatl rhtllllpal lssgqgelap qidgqtwaer alrenehhaf tcrvaggsat
       61 prlawyldgq lqkattsrll svggdafsgg tstftvtaqr sqhelncslq dpgsgrpana
      121 svilnvqfkp eiaqvgakyq eaqgpgllvv lfalvranpp anvtwidqdg pvtvnasdfl
      181 vldaqnypwl tnhtvqlqlr slahnlsvva tndvgvtsas lpapgllatr ievpllgivv
      241 agglafgtlv gfstlvaclv crkekktkgp srrpslissd snnlklnnvr lprenmslps
      301 nlqlndltpd irgkaterpm aqhssrpell eaepggllts rgfirlpmlg yiyrvssvss
      361 deiwl
//
LOCUS       NP_001423390             326 aa            linear   ROD 14-MAR-2025
DEFINITION  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423390 XP_006243432
VERSION     NP_001423390.1
DBSOURCE    REFSEQ: accession NM_001436461.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cho,B., Choi,S.Y., Park,O.H., Sun,W. and Geum,D.
  TITLE     Differential expression of BNIP family members of BH3-only proteins
            during the development and after axotomy in the rat
  JOURNAL   Mol Cells 33 (6), 605-610 (2012)
   PUBMED   22639046
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Cuadrado,A. and Nebreda,A.R.
  TITLE     Mechanisms and functions of p38 MAPK signalling
  JOURNAL   Biochem J 429 (3), 403-417 (2010)
   PUBMED   20626350
  REMARK    Review article
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Lu,M. and Krauss,R.S.
  TITLE     N-cadherin ligation, but not Sonic hedgehog binding, initiates
            Cdo-dependent p38alpha/beta MAPK signaling in skeletal myoblasts
  JOURNAL   Proc Natl Acad Sci U S A 107 (9), 4212-4217 (2010)
   PUBMED   20160094
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Oh,J.E., Bae,G.U., Yang,Y.J., Yi,M.J., Lee,H.J., Kim,B.G.,
            Krauss,R.S. and Kang,J.S.
  TITLE     Cdo promotes neuronal differentiation via activation of the p38
            mitogen-activated protein kinase pathway
  JOURNAL   FASEB J 23 (7), 2088-2099 (2009)
   PUBMED   19244314
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Sonn,S., Jeong,Y. and Rhee,K.
  TITLE     Nip2/centrobin may be a substrate of Nek2 that is required for
            proper spindle assembly during mitosis in early mouse embryos
  JOURNAL   Mol Reprod Dev 76 (6), 587-592 (2009)
   PUBMED   19117032
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Boyd,J.M., Malstrom,S., Subramanian,T., Venkatesh,L.K.,
            Schaeper,U., Elangovan,B., D'Sa-Eipper,C. and Chinnadurai,G.
  TITLE     Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
            of cellular proteins
  JOURNAL   Cell 79 (2), 341-351 (1994)
   PUBMED   7954800
  REMARK    Erratum:[Cell. 1994 Dec 16;79(6):1121. PMID: 8001138]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006243432.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.319268.1,
                                           SRR26643429.30937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..326
                     /product="BCL2/adenovirus E1B 19 kDa protein-interacting
                     protein 2 isoform 1"
                     /note="Bcl-2 and E1B 19 kDa interacting protein;
                     BCL2/adenovirus E1B 19kDa-interacting protein 1, NIP2;
                     BCL2/adenovirus E1B interacting protein 2; BCL2/adenovirus
                     E1B 19 kDa protein-interacting protein 2"
                     /calculated_mol_wt=37674
     Region          49..163
                     /region_name="BNIP2"
                     /note="Bcl2-/adenovirus E1B nineteen kDa-interacting
                     protein 2; pfam12496"
                     /db_xref="CDD:463609"
     Region          147..295
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     CDS             1..326
                     /gene="Bnip2"
                     /coded_by="NM_001436461.1:247..1227"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300811"
                     /db_xref="RGD:1308944"
ORIGIN      
        1 megvelkeew qdedfpiplp eddsieadil dvtdpdrqpg slevngnkvr kklvapdisl
       61 tldpgedslw sddldeggev dldgldtpse nsdefewedd lpkpkttevi rkgsiteyaa
      121 teekedgrrw rmfrigeqdh rvdmkaiepy kkvishggyy gdglnaivvf avcfmpesgq
      181 pnyrylmdnl fkyvigtlel lvaenymiiy lngattrrkm pslgwlrrcy qqidrrlrkn
      241 lksliivhps wfirtllavt rpfisskfsq kiryvfnlae laelvpmeyv gipecikqye
      301 eekfkkrqkr vdqelngkqe ppkseq
//
LOCUS       NP_001423387             752 aa            linear   ROD 14-MAR-2025
DEFINITION  leucine-rich repeat-containing protein 49 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423387 XP_063121213
VERSION     NP_001423387.1
DBSOURCE    REFSEQ: accession NM_001436458.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063121213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.33949.1,
                                           SRR26360172.2019935.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..752
                     /product="leucine-rich repeat-containing protein 49
                     isoform 1"
                     /note="leucine-rich repeat-containing protein 49"
                     /calculated_mol_wt=85612
     Region          160..177
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          180..201
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          183..378
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          202..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          224..245
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          246..267
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          268..289
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          290..311
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          312..336
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..752
                     /gene="Lrrc49"
                     /gene_synonym="RGD1309466"
                     /coded_by="NM_001436458.1:188..2446"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300763"
                     /db_xref="RGD:1309466"
ORIGIN      
        1 mipgkyrsvs graannvncg lhlviqtssl sdknkvefkl nretpsfpgr llqhdlerny
       61 ssrqgdgrvi spsprnkssc issttnvtel cgldmrtatt slsafgdssi qtpskprirq
      121 gchsagpnvs gdhinlvsss mpsfpilqrs seektlysdr ltlerqkltv cpiidgeehl
      181 rllnfqhnfi triqnisnlq rlifldlydn qieeisglst lkslrvlllg knrikkisnl
      241 enlknldvld lhgnqitkie nvnhlcdlrv lnlarnllsh vdnlngldsl telnlrhnqi
      301 tfvrdvdnlp clqrlflsfn nitsfesvsc laestslsdi tfdgnpiaqe swykhtvlqn
      361 mmqlrqldmk riteeerrva svvakkeeek kreshkqsll kekkrltinn varkwdlqqr
      421 vaniaiiqdr kdsesppqes cqidggtisa fpeeagslda glssalqgls vtethlveld
      481 getlslygsg alecldrnws vqtagmvttv sftfiefdei vqvlpklkmk fpnslhlkfr
      541 etnlvmlqqf nalaqlrrvd qltidpqgnp vvnftlwkyy vlfrlshfsm qkingtevtq
      601 ndmimaerlf gilahvasse lpqyrmisil gdarkkqfry llenkckkpg ilceetsdsk
      661 rlmgentnra tlnyttrefy hekleeikdk kkfcrlyved lvkeatainm knealqklwp
      721 qmfielvrda vieirskdsy mklclqqitd qk
//
LOCUS       NP_001094412             141 aa            linear   ROD 14-MAR-2025
DEFINITION  proteasome maturation protein [Rattus norvegicus].
ACCESSION   NP_001094412 XP_001060809 XP_213700
VERSION     NP_001094412.1
DBSOURCE    REFSEQ: accession NM_001100942.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Shin,S.W., Shimizu,N., Tokoro,M., Nishikawa,S., Hatanaka,Y.,
            Anzai,M., Hamazaki,J., Kishigami,S., Saeki,K., Hosoi,Y.,
            Iritani,A., Murata,S. and Matsumoto,K.
  TITLE     Mouse zygote-specific proteasome assembly chaperone important for
            maternal-to-zygotic transition
  JOURNAL   Biol Open 2 (2), 170-182 (2013)
   PUBMED   23429752
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Fricke,B., Heink,S., Steffen,J., Kloetzel,P.M. and Kruger,E.
  TITLE     The proteasome maturation protein POMP facilitates major steps of
            20S proteasome formation at the endoplasmic reticulum
  JOURNAL   EMBO Rep 8 (12), 1170-1175 (2007)
   PUBMED   17948026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Aug 12, 2007 this sequence version replaced
            XP_213700.1, XP_001060809.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161800.1, EV765329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN12840117
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..141
                     /product="proteasome maturation protein"
                     /note="voltage-gated potassium channel beta subunit 4.1"
                     /calculated_mol_wt=15713
     Region          25..138
                     /region_name="UMP1"
                     /note="Proteasome maturation factor UMP1; pfam05348"
                     /db_xref="CDD:461627"
     CDS             1..141
                     /gene="Pomp"
                     /gene_synonym="RGD1305831"
                     /coded_by="NM_001100942.2:63..488"
                     /db_xref="GeneID:288455"
                     /db_xref="RGD:1305831"
ORIGIN      
        1 mnarglgsql kdsipvtels asgpfeshdl lrkgfscvkn ellpshplel seknfqlnqd
       61 kmnfstlrni qglfaplklq mefkavqqvq rlpflpssnl sldilrgnde tigfedilnd
      121 psqselmgep hmmveyklgl l
//
LOCUS       NP_001423384            2150 aa            linear   ROD 14-MAR-2025
DEFINITION  alpha-tectorin isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423384 XP_038936975
VERSION     NP_001423384.1
DBSOURCE    REFSEQ: accession NM_001436455.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2150)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 2150)
  AUTHORS   Mustapha,M., Weil,D., Chardenoux,S., Elias,S., El-Zir,E.,
            Beckmann,J.S., Loiselet,J. and Petit,C.
  TITLE     An alpha-tectorin gene defect causes a newly identified autosomal
            recessive form of sensorineural pre-lingual non-syndromic deafness,
            DFNB21
  JOURNAL   Hum Mol Genet 8 (3), 409-412 (1999)
   PUBMED   9949200
REFERENCE   3  (residues 1 to 2150)
  AUTHORS   Verhoeven,K., Van Laer,L., Kirschhofer,K., Legan,P.K., Hughes,D.C.,
            Schatteman,I., Verstreken,M., Van Hauwe,P., Coucke,P., Chen,A.,
            Smith,R.J., Somers,T., Offeciers,F.E., Van de Heyning,P.,
            Richardson,G.P., Wachtler,F., Kimberling,W.J., Willems,P.J.,
            Govaerts,P.J. and Van Camp,G.
  TITLE     Mutations in the human alpha-tectorin gene cause autosomal dominant
            non-syndromic hearing impairment
  JOURNAL   Nat Genet 19 (1), 60-62 (1998)
   PUBMED   9590290
  REMARK    Erratum:[Nat Genet 1999 Apr;21(4):449]
REFERENCE   4  (residues 1 to 2150)
  AUTHORS   Legan,P.K., Rau,A., Keen,J.N. and Richardson,G.P.
  TITLE     The mouse tectorins. Modular matrix proteins of the inner ear
            homologous to components of the sperm-egg adhesion system
  JOURNAL   J Biol Chem 272 (13), 8791-8801 (1997)
   PUBMED   9079715
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_038936975.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2150
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..2150
                     /product="alpha-tectorin isoform 1 precursor"
                     /note="alpha-tectorin"
                     /calculated_mol_wt=236033
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2877
     Region          98..254
                     /region_name="NIDO"
                     /note="Extracellular domain of unknown function in nidogen
                     (entactin) and hypothetical proteins; smart00539"
                     /db_xref="CDD:214712"
     Region          313..477
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          517..591
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          597..650
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(606,610,623,627)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          652..706
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          703..865
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          905..981
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          984..1036
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(993,996,1009,1013)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          1100..1258
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Region          1300..1368
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          1372..1425
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(1381,1385,1398,1402)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          1487..1639
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Region          1680..1752
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Region          1800..2054
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Region          2084..2116
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     CDS             1..2150
                     /gene="Tecta"
                     /coded_by="NM_001436455.1:286..6738"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:300653"
                     /db_xref="RGD:1309824"
ORIGIN      
        1 mnyssllriw vsfifalvrh qaqprelmyp fwqndtrtpk vddgssseik laipvfffgv
       61 pyrtvyvnnn gvvsfnvlvs qftpesfplt dgrafiapfw advhngirge iyyretmdsa
      121 ilrratkdir kyfkdmttfs atwvfivtwe evtfyggsst tpvntfqavl vsdgsytftl
      181 fnyyeinwtt gtasggdplt glggvmaqag fnggnltnff slpgsrtpei vniqettnvn
      241 vpgrwafkvd gkeidpangc tsrgqflrrg evfwddlnct ikcrcldfnn eiycqeascs
      301 pyevcepkgr ffycspvets tcvvfgephy htfdgflfhf qgscayllar qclqtsslpf
      361 fsveaknehr ggsavswvke lsvevngyki lipkgsygkv kvndlvtslp vtlelgavki
      421 yqsgmstave tdfgllvtfd gqhyasisip gsyinstcgl cgnynknpld dflrpdgrpa
      481 msvldlgesw rvyhtdwkcg sgcidnctqc daatealyfg sdycgflnkt dgplwecgtv
      541 vdatafvhsc vydlcsvrdn gtllcqaiqa yalvcqalgi pigdwriqtg cvstvrcpsf
      601 shysvctssc pdtcsdltas qncatpcteg cecnegfvls tsqcvplhkc gcdfeghyyt
      661 mgeffwatan ctvqclceeg gdvycfnktc rsgevcaved gyqgcfpkre tvcllsqnqv
      721 lhtfdgaaya fpselsytll ktcperpeyl eidinkrkpd agpawlrgvr ilvadqevki
      781 ggvgalevkl ngqdvelpff hpsgrleihr nknsttvesk gvvsvqysdv gllyirlstm
      841 yfnctgglcg ffnanasdef clpngkctdn lavfleswtt feeicngecg dllkacnnds
      901 ellkfyrsrs rcgiindpsn ssflechgvv nvtayyrtcl frlcqsggne selcdsvary
      961 asacknadve vgpwrtydfc plecpenshf eecmtctetc etlalgpicv dscsegcqcd
     1021 egyalqgsqc vtrsecgcnf eghqlatnet fwvdqdcqif cycngtdnsv hcetipcrdd
     1081 dycmeesgly ycqprtdasc ivsgyghylt fdgypfdfqt scplilcttg srsisdsfpk
     1141 fivtaknedr dpslalwvkq vdvtvfgysi vihraykhtv lvnnerlylp lklgqgkini
     1201 fsfgfhvvve tdfglkvvyd wktflsitvp rsmqnstygl cgryngnpgd dlempmglla
     1261 lsinefgqsw vkrdtfcqvg cgdrcpscak vegfskvqql cslipnqnag fakchskvnp
     1321 tffyknclfd scidggavqt acswlqnyas tcqtqgvavt gwrnytscsv tcppnshyes
     1381 cvsvcqprca airlksdcnh ycvegcqcda gyvlngksci lphncgcysd gkyyepkqlf
     1441 wngdctrrcr cfrrnliqcd prqcksdeec alrsgvrgcf stktsyclaa gggvfrtfdg
     1501 aflrfpanca fvlsticqkl pdisfqliin fdkwsspnlt iispvyfyin eeqilindrn
     1561 tvkvngtqvn vpfitglatk iyssegflvi dtspdiqiyy ngfnvikisi serlqnkvcg
     1621 lcgnfngdmt ddyvtlrgkp vvssvvlaqs wktngmqksc nelqfsqyaa tcdnvhiqam
     1681 qgdgyclklt dmkgffqpcy glldplpfye scyldgcynh kkfqlcgsla aygeacrsfg
     1741 ilstewieke ncsgvvedpc vgadcpnrtc eldnggelcg ciepppygnn shdiidaevt
     1801 ckaaqmevsi skcklfqlgf eregvrindr qcsgiegedf isfqinntkg ncgnvvqsng
     1861 thimykntiw iesanntgni itrdrtinve fscayeldik isldsvvkpm lsvinltvpt
     1921 qegsfttkma lyknasykhp yrqgevvltt rdvlyvgvfv vgadsthlil tlnkcyatps
     1981 rdsndklryf iieggcqnik dntigieeng vsltcrfhvt vfkfigdyde vhlhcavslc
     2041 dsekysckin cpqnsriatd yskehkeqii svgpirrkrl dwcednggce qvctsrvdgp
     2101 lcscvtgslq edgrscrasn ssvepqvwtl llimtqislw hfvyqsgats
//
LOCUS       NP_064463                789 aa            linear   ROD 14-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 1
            precursor [Rattus norvegicus].
ACCESSION   NP_064463 XP_346441
VERSION     NP_064463.2
DBSOURCE    REFSEQ: accession NM_020078.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Nishimura,H., Kim,E., Nakanishi,T. and Baba,T.
  TITLE     Possible function of the ADAM1a/ADAM2 Fertilin complex in the
            appearance of ADAM3 on the sperm surface
  JOURNAL   J Biol Chem 279 (33), 34957-34962 (2004)
   PUBMED   15194697
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   3  (residues 1 to 789)
  AUTHORS   McLaughlin,E.A., Frayne,J., Barker,H.L., Jury,J.A., Jones,R.,
            Ford,W.C. and Hall,L.
  TITLE     Cloning and sequence analysis of rat fertilin alpha and
            beta--developmental expression, processing and immunolocalization
  JOURNAL   Mol Hum Reprod 3 (9), 801-809 (1997)
   PUBMED   9358007
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced NP_064463.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: Y08616.1, BC081807.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..789
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 1 precursor"
                     /note="disintegrin and metalloproteinase domain-containing
                     protein 1; a disintegrin and metalloprotease domain 1
                     (fertilin alpha); ADAM 1; fertilin subunit alpha; a
                     disintegrin and metalloproteinase domain 1 (fertilin
                     alpha); PH-30 alpha; a disintegrin and metallopeptidase
                     domain 1a"
                     /calculated_mol_wt=78991
     sig_peptide     1..68
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70505.1)"
                     /calculated_mol_wt=7199
     Region          79..194
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          238..432
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70505.1)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70505.1)"
     Region          450..522
                     /region_name="DISIN"
                     /note="Homologues of snake disintegrins; smart00050"
                     /db_xref="CDD:214490"
     Region          524..660
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70505.1)"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70505.1)"
     Site            743..763
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70505.1)"
     CDS             1..789
                     /gene="Adam1a"
                     /gene_synonym="Adam1; PH-30a"
                     /coded_by="NM_020078.2:345..2714"
                     /db_xref="GeneID:56777"
                     /db_xref="RGD:621467"
ORIGIN      
        1 msvaasasrs astlcspqiq qgalkeakvp phiwaarhwn lglrlvpgha svragilvll
       61 iflpstlcdl gsvydssyet viperlpgqg sddpggkvsy vllmqgqkql lhlevkghys
      121 ernfpvysyh hgilgqevpl lsqachyegh iegvpgsfvs vsicsglrgv likeetaygi
      181 epllfstdfe hilytmahqp vvlcnvtptd slgdssqrqg ssktdellal sdlwshakyv
      241 emfvvvnhqr fqmwgsdvnt tvqavvdiia lansftrgin tevvlvglei wtegdpievp
      301 vdlqatlrnf nlwrqeklmg rvrhdvahli vghrpganeg qafldgacsg gfaaaveafh
      361 hedvllfaal mahelghnlg irhdrpgctc gpkhlclmhe tisktssfsn cssdhflrfl
      421 hdhrgaclld rpwhqshkrr dahcgngvve eseecdcgna cdshpccept ctlkvgaqcs
      481 eglccykctf kkkgtlcrpa edvcdlpeyc ngitgecpan symqdgtqcd riyycsgglc
      541 knpdkqcari ygyparsape ecyisvntka nrfgncghpt sanlkyeacs nedifcgklv
      601 ctdvrylpqv kplhsllqip ygddwcwsmd aynvtdipdy gdvqggtyca pkkvcmesic
      661 tghatlqydc hpqemchgng vcnnfkhchc dagfsppdcs sggnggsvds gpvgkpadrn
      721 lslfgvgesp dsrmedeein lkvvvlvvpi flivllcclm liaylwsevq eavspgssst
      781 tsssesesd
//
LOCUS       NP_001258062             832 aa            linear   ROD 14-MAR-2025
DEFINITION  piwi-like protein 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001258062 XP_001072752
VERSION     NP_001258062.1
DBSOURCE    REFSEQ: accession NM_001271133.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Henaoui,I.S., Jacovetti,C., Guerra Mollet,I., Guay,C., Sobel,J.,
            Eliasson,L. and Regazzi,R.
  TITLE     PIWI-interacting RNAs as novel regulators of pancreatic beta cell
            function
  JOURNAL   Diabetologia 60 (10), 1977-1986 (2017)
   PUBMED   28711973
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Sivagurunathan,S., Palanisamy,K., Arunachalam,J.P. and
            Chidambaram,S.
  TITLE     Possible role of HIWI2 in modulating tight junction proteins in
            retinal pigment epithelial cells through Akt signaling pathway
  JOURNAL   Mol Cell Biochem 427 (1-2), 145-156 (2017)
   PUBMED   28025795
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Yang,Z., Chen,K.M., Pandey,R.R., Homolka,D., Reuter,M.,
            Janeiro,B.K., Sachidanandam,R., Fauvarque,M.O., McCarthy,A.A. and
            Pillai,R.S.
  TITLE     PIWI Slicing and EXD1 Drive Biogenesis of Nuclear piRNAs from
            Cytosolic Targets of the Mouse piRNA Pathway
  JOURNAL   Mol Cell 61 (1), 138-152 (2016)
   PUBMED   26669262
REFERENCE   4  (residues 1 to 832)
  AUTHORS   Pastor,W.A., Stroud,H., Nee,K., Liu,W., Pezic,D., Manakov,S.,
            Lee,S.A., Moissiard,G., Zamudio,N., Bourc'his,D., Aravin,A.A.,
            Clark,A.T. and Jacobsen,S.E.
  TITLE     MORC1 represses transposable elements in the mouse male germline
  JOURNAL   Nat Commun 5, 5795 (2014)
   PUBMED   25503965
  REMARK    Erratum:[Nat Commun. 2015 Jul 10;6:7604. doi: 10.1038/ncomms8604.
            PMID: 26159654]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 832)
  AUTHORS   Keam,S.P., Young,P.E., McCorkindale,A.L., Dang,T.H., Clancy,J.L.,
            Humphreys,D.T., Preiss,T., Hutvagner,G., Martin,D.I., Cropley,J.E.
            and Suter,C.M.
  TITLE     The human Piwi protein Hiwi2 associates with tRNA-derived piRNAs in
            somatic cells
  JOURNAL   Nucleic Acids Res 42 (14), 8984-8995 (2014)
   PUBMED   25038252
REFERENCE   6  (residues 1 to 832)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   7  (residues 1 to 832)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   8  (residues 1 to 832)
  AUTHORS   Aravin,A.A., Sachidanandam,R., Bourc'his,D., Schaefer,C., Pezic,D.,
            Toth,K.F., Bestor,T. and Hannon,G.J.
  TITLE     A piRNA pathway primed by individual transposons is linked to de
            novo DNA methylation in mice
  JOURNAL   Mol Cell 31 (6), 785-799 (2008)
   PUBMED   18922463
REFERENCE   9  (residues 1 to 832)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Totoki,Y., Toyoda,A.,
            Ikawa,M., Asada,N., Kojima,K., Yamaguchi,Y., Ijiri,T.W., Hata,K.,
            Li,E., Matsuda,Y., Kimura,T., Okabe,M., Sakaki,Y., Sasaki,H. and
            Nakano,T.
  TITLE     DNA methylation of retrotransposon genes is regulated by Piwi
            family members MILI and MIWI2 in murine fetal testes
  JOURNAL   Genes Dev 22 (7), 908-917 (2008)
   PUBMED   18381894
REFERENCE   10 (residues 1 to 832)
  AUTHORS   Carmell,M.A., Girard,A., van de Kant,H.J., Bourc'his,D.,
            Bestor,T.H., de Rooij,D.G. and Hannon,G.J.
  TITLE     MIWI2 is essential for spermatogenesis and repression of
            transposons in the mouse male germline
  JOURNAL   Dev Cell 12 (4), 503-514 (2007)
   PUBMED   17395546
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Sep 1, 2012 this sequence version replaced XP_001072752.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760434
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..832
                     /product="piwi-like protein 4 isoform 2"
                     /note="piwi-like protein 4; piwi-like 4"
                     /calculated_mol_wt=94258
     Region          249..365
                     /region_name="PAZ_piwi_like"
                     /note="PAZ domain, Piwi_like subfamily. In multi-cellular
                     organisms, the Piwi protein appears to be essential for
                     the maintenance of germline stem cells. In the Drosophila
                     male germline, Piwi was shown to be involved in the
                     silencing of retrotransposons in the...; cd02845"
                     /db_xref="CDD:239211"
     Site            order(294,307,315,319,337,352,354)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239211"
     Region          373..815
                     /region_name="Piwi_piwi-like_Euk"
                     /note="PIWI domain, Piwi-like subfamily found in
                     eukaryotes. This domain is found in Piwi and closely
                     related proteins, where it is believed to perform a
                     crucial role in germline cells, via RNA silencing. RNA
                     silencing refers to a group of related...; cd04658"
                     /db_xref="CDD:240016"
     Site            order(538,542,554..557,560,570,573,577,581)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240016"
     Site            order(602,604,672,807)
                     /site_type="active"
                     /db_xref="CDD:240016"
     CDS             1..832
                     /gene="Piwil4"
                     /coded_by="NM_001271133.1:1..2499"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:689972"
                     /db_xref="RGD:1311015"
ORIGIN      
        1 msgrarvrar gittghsare veraprdlmv sasvyelgvs sgdgrrtlve krgngrqdfv
       61 dlgvctrekl thvkdsktgs sgipvqlatn lfhldlpqdw qlyqyhvtys pdlasrrlrt
      121 allynhsils dkakafdgts lflsekldhk vteltsetqr getvkitltl tselfpnspm
      181 ciqffnvifr kifkklsmyq igrnyykpse pveipqykls lwpgfaisvs rfeskllfna
      241 dvnykvlrne tvlefmtdlc lrtdmscfte tchkqlvgli vltrynnkty riddidwsvk
      301 pthafqkrdg settyvdyyk qqyditlsdl nqpvlvsllk rrrndnsepq mvhlipelcf
      361 ltgltsqats dfrlmkavae etrlspmgrq qqlarladdi qrnqvtrfel etwglhfgsq
      421 lsltgrvvps ekillqdhtc qpafaadwsk dmrsckvlss eplntwlivc csraehlies
      481 flsclrrvgg stgfsvghpk iikvdenpaa flraiqlhvn pdvqlvmcil psnqknyyds
      541 ikrylssdcp vpsqcvltrt lnkqgmmlsv atkiamqmtc klggelwave iplkslmvvg
      601 idicrdalsk dvavvgfvas insritrwfs rcvlqrtaad iadclkvcmt galnkwykhn
      661 hdlpariiay rdgvgngqlk avleyevpql lssvtecgsd arscrlsvvv vrkrcllrlf
      721 aesghtlqnp plgtvvdsea trpewydfyl tsqtanrgtv sptyynviyd dnalkpdhmq
      781 rltfklchly ynwqgvisvp apcqyahklt flvaqsihke pslelanklf yl
//
LOCUS       NP_599167                490 aa            linear   ROD 14-MAR-2025
DEFINITION  dual specificity protein kinase CLK3 [Rattus norvegicus].
ACCESSION   NP_599167
VERSION     NP_599167.2
DBSOURCE    REFSEQ: accession NM_134340.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Ma,X., Gao,L., Ge,R., Yuan,T., Lin,B. and Zhen,L.
  TITLE     CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 333-342 (2024)
   PUBMED   38438604
  REMARK    GeneRIF: CDC-like kinase 3 deficiency aggravates hypoxia-induced
            cardiomyocyte apoptosis through AKT signaling pathway.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Duncan,P.I., Stojdl,D.F., Marius,R.M., Scheit,K.H. and Bell,J.C.
  TITLE     The Clk2 and Clk3 dual-specificity protein kinases regulate the
            intranuclear distribution of SR proteins and influence pre-mRNA
            splicing
  JOURNAL   Exp Cell Res 241 (2), 300-308 (1998)
   PUBMED   9637771
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Nayler,O., Stamm,S. and Ullrich,A.
  TITLE     Characterization and comparison of four serine- and arginine-rich
            (SR) protein kinases
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 693-700 (1997)
   PUBMED   9307018
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Becker,W., Kentrup,H., Heukelbach,J. and Joost,H.G.
  TITLE     cDNA cloning and characterization of rat Clk3, a LAMMER kinase
            predominately expressed in testis
  JOURNAL   Biochim Biophys Acta 1312 (1), 63-67 (1996)
   PUBMED   8679717
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Nov 26, 2020 this sequence version replaced NP_599167.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X94351.1, SRR26360172.2973633.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..490
                     /product="dual specificity protein kinase CLK3"
                     /EC_number="2.7.12.1"
                     /calculated_mol_wt=58354
     Region          1..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63117.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49761; propagated from
                     UniProtKB/Swiss-Prot (Q63117.2)"
     Region          142..472
                     /region_name="PKc_CLK3"
                     /note="Catalytic domain of the Dual-specificity protein
                     kinase, CDC-like kinase 3; cd14214"
                     /db_xref="CDD:271116"
     Site            order(162..166,170,184,186,200,220,236..239,242,244..245,
                     283,285,287..288,290,320,323,332,334..337,339,376)
                     /site_type="active"
                     /db_xref="CDD:271116"
     Site            order(162..165,170,184,186,220,236..239,242,245,287..288,
                     290,319..320)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271116"
     Site            order(200,244,283,285,323,332,334..337,339,376)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271116"
     Site            319..339
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271116"
     CDS             1..490
                     /gene="Clk3"
                     /coded_by="NM_134340.3:409..1881"
                     /db_xref="GeneID:171305"
                     /db_xref="RGD:621259"
ORIGIN      
        1 mhhckryrsp epdpylsyrw krrrsysreh egrlrypsrr eppprrsrsr shdripyqrr
       61 yrehrdsdty rceerspsfg edcygssrsr hrrrsrergp yrtrkhahhc hkrrtrscss
      121 assrsqqssk rssrsveddk eghlvcrigd wlqeryeivg nlgegtfgkv vecldhargk
      181 sqvalkiirn vgkyreaarl einvlkkike kdkenkflcv lmsdwfnfhg hmciafellg
      241 kntfeflken nfqpyplphv rhmayqlcha lrflhenqlt htdlkpenil fvnsefetly
      301 nehksceeks vkntsirvad fgsatfdheh httivatrhy rppevilelg waqpcdvwsi
      361 gcilfeyyrg ftlfqthenr ehlvmmekil gpipshmihr trkqkyfykg glvwdenssd
      421 gryvkenckp lksymlqdsl ehvqlfdlmr rmlefdpaqr itlaeallhp ffagltpeer
      481 sfhssrnpsr
//
LOCUS       NP_001423349             247 aa            linear   ROD 14-MAR-2025
DEFINITION  14-3-3 protein gamma [Rattus norvegicus].
ACCESSION   NP_001423349 XP_006249246
VERSION     NP_001423349.1
DBSOURCE    REFSEQ: accession NM_001436420.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Han,L., Tang,J., Zhu,S. and Zhu,J.
  TITLE     LncRNA SNHG7 Knockdown Aggravates Hepatic Ischemia-Reperfusion
            Injury and Promotes Apoptosis in Hemorrhagic Shock Pregnant Rats by
            Modulating miR-34a-5p/YWHAG Axis
  JOURNAL   Mol Biotechnol 65 (6), 983-996 (2023)
   PUBMED   36427097
  REMARK    GeneRIF: LncRNA SNHG7 Knockdown Aggravates Hepatic
            Ischemia-Reperfusion Injury and Promotes Apoptosis in Hemorrhagic
            Shock Pregnant Rats by Modulating miR-34a-5p/YWHAG Axis.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Abu-Rumeileh,S., Baiardi,S., Polischi,B., Mammana,A.,
            Franceschini,A., Green,A., Capellari,S. and Parchi,P.
  TITLE     Diagnostic value of surrogate CSF biomarkers for Creutzfeldt-Jakob
            disease in the era of RT-QuIC
  JOURNAL   J Neurol 266 (12), 3136-3143 (2019)
   PUBMED   31541342
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Otsuka,S., Sakakima,H., Terashi,T., Takada,S., Nakanishi,K. and
            Kikuchi,K.
  TITLE     Preconditioning exercise reduces brain damage and neuronal
            apoptosis through enhanced endogenous 14-3-3gamma after focal brain
            ischemia in rats
  JOURNAL   Brain Struct Funct 224 (2), 727-738 (2019)
   PUBMED   30478609
  REMARK    GeneRIF: Our findings suggest that preconditioning exercise prior
            to ischemia induces neuron- and astrocyte-mediated brain ischemic
            tolerance through increased expression of HIF-1alpha and
            14-3-3gamma, which are intrinsic protective factors; the
            upregulated 14-3-3gamma induced by preconditioning exercise reduces
            ischemic neuronal cell death through the 14-3-3gamma/p-beta-catenin
            Ser37/Bax/caspase 3 anti-apoptotic pathway.
            Erratum:[Brain Struct Funct. 2019 Mar;224(2):739-740. doi:
            10.1007/s00429-018-1815-x. PMID: 30560373]
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Kanata,E., Golanska,E., Villar-Pique,A., Karsanidou,A., Dafou,D.,
            Xanthopoulos,K., Schmitz,M., Ferrer,I., Karch,A., Sikorska,B.,
            Liberski,P.P., Sklaviadis,T., Zerr,I. and Llorens,F.
  TITLE     Cerebrospinal fluid neurofilament light in suspected sporadic
            Creutzfeldt-Jakob disease
  JOURNAL   J Clin Neurosci 60, 124-127 (2019)
   PUBMED   30309804
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Gerber,K.J., Squires,K.E. and Hepler,J.R.
  TITLE     14-3-3gamma binds regulator of G protein signaling 14 (RGS14) at
            distinct sites to inhibit the RGS14:Galphai-AlF4- signaling complex
            and RGS14 nuclear localization
  JOURNAL   J Biol Chem 293 (38), 14616-14631 (2018)
   PUBMED   30093406
  REMARK    GeneRIF: phosphorylation-independent binding of 14-3-3 has no
            effect on RGS14/Galphai interactions but, instead, inhibits
            (directly or indirectly) RGS14 nuclear import and nucleocytoplasmic
            shuttling
            Erratum:[J Biol Chem. 2019 Aug 9;294(32):12262. doi:
            10.1074/jbc.AAC119.101131. PMID: 31399537]
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Peyrl,A., Weitzdoerfer,R., Gulesserian,T., Fountoulakis,M. and
            Lubec,G.
  TITLE     Aberrant expression of signaling-related proteins 14-3-3 gamma and
            RACK1 in fetal Down syndrome brain (trisomy 21)
  JOURNAL   Electrophoresis 23 (1), 152-157 (2002)
   PUBMED   11824616
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Autieri,M.V. and Carbone,C.J.
  TITLE     14-3-3Gamma interacts with and is phosphorylated by multiple
            protein kinase C isoforms in PDGF-stimulated human vascular smooth
            muscle cells
  JOURNAL   DNA Cell Biol 18 (7), 555-564 (1999)
   PUBMED   10433554
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Martin,H., Rostas,J., Patel,Y. and Aitken,A.
  TITLE     Subcellular localisation of 14-3-3 isoforms in rat brain using
            specific antibodies
  JOURNAL   J Neurochem 63 (6), 2259-2265 (1994)
   PUBMED   7964746
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Watanabe,M., Isobe,T., Ichimura,T., Kuwano,R., Takahashi,Y.,
            Kondo,H. and Inoue,Y.
  TITLE     Molecular cloning of rat cDNAs for the zeta and theta subtypes of
            14-3-3 protein and differential distributions of their mRNAs in the
            brain
  JOURNAL   Brain Res Mol Brain Res 25 (1-2), 113-121 (1994)
   PUBMED   7984035
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Watanabe,M., Isobe,T., Ichimura,T., Kuwano,R., Takahashi,Y. and
            Kondo,H.
  TITLE     Molecular cloning of rat cDNAs for beta and gamma subtypes of
            14-3-3 protein and developmental changes in expression of their
            mRNAs in the nervous system
  JOURNAL   Brain Res Mol Brain Res 17 (1-2), 135-146 (1993)
   PUBMED   8381897
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006249246.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D17447.1, SRR26360181.315695.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..247
                     /product="14-3-3 protein gamma"
                     /note="tyrosine 3/tryptophan 5 -monooxygenase activation
                     protein, gamma polypeptide; tyrosine
                     3-monooxgenase/tryptophan 5-monooxgenase activation
                     protein, gamma polypeptide; 14-3-3 protein gamma-subtype;
                     tryosine 3-monooxgenase/tryptophan 5-monooxgenase
                     activation protein gamma polypeptide;
                     3-monooxygenase/tryptophan 5-monooxgenase activation
                     protein gamma polypeptide; tryosine
                     3-monooxgenase/tryptophan 5 monooxgenase activation
                     protein gamma; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, gamma polypeptide"
                     /calculated_mol_wt=28172
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Region          2..247
                     /region_name="14-3-3_gamma"
                     /note="14-3-3 gamma, an isoform of 14-3-3 protein;
                     cd10024"
                     /db_xref="CDD:206760"
     Region          2..247
                     /region_name="Interaction with SPATA18/MIEAP.
                     /evidence=ECO:0000250|UniProtKB:P61981"
                     /note="propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline, in 14-3-3 protein gamma,
                     N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            order(6,9..10,13..14,16..17,19,22,59,62..63,66,77..78,
                     81..82,85,88..89,92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206760"
     Site            order(50,57,125,132..133,177..178,181,222,225,229,
                     232..233)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206760"
     Site            57
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P61981;
                     propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            132
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P61981;
                     propagated from UniProtKB/Swiss-Prot (P61983.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61981; propagated from
                     UniProtKB/Swiss-Prot (P61983.2)"
     CDS             1..247
                     /gene="Ywhag"
                     /gene_synonym="14-3-3G"
                     /coded_by="NM_001436420.1:191..934"
                     /db_xref="GeneID:56010"
                     /db_xref="RGD:62002"
ORIGIN      
        1 mvdreqlvqk arlaeqaery ddmaaamknv telneplsne ernllsvayk nvvgarrssw
       61 rvissieqkt sadgnekkie mvrayrekie keleavcqdv lslldnylik ncsetqyesk
      121 vfylkmkgdy yrylaevatg ekratvvess ekayseahei skehmqpthp irlglalnys
      181 vfyyeiqnap eqachlakta fddaiaeldt lnedsykdst limqllrdnl tlwtsdqqdd
      241 dggegnn
//
LOCUS       NP_001423380             186 aa            linear   ROD 14-MAR-2025
DEFINITION  methyl-CpG-binding domain protein 3-like 1 [Rattus norvegicus].
ACCESSION   NP_001423380 XP_006242633
VERSION     NP_001423380.1
DBSOURCE    REFSEQ: accession NM_001436451.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006242633.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.15260.1,
                                           SRR26360181.3002426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..186
                     /product="methyl-CpG-binding domain protein 3-like 1"
                     /calculated_mol_wt=20673
     Region          9..74
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Region          78..166
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     CDS             1..186
                     /gene="Mbd3l1"
                     /coded_by="NM_001436451.1:152..712"
                     /db_xref="GeneID:300389"
                     /db_xref="RGD:1308259"
ORIGIN      
        1 mgktsqrkqc dcenpskpcl stsiplrmsn ytfkrpvtki tshlgnevry yqweetlekp
       61 eqacwqkrlq glqayssage ilstsdlska lkdltprdtd aassiiqans mdprplstlg
      121 ssshlakmip eagpqilcke flvteedisi qerkvkiare rlavaliahk lanetekvrg
      181 srkakv
//
LOCUS       NP_001385635             698 aa            linear   ROD 14-MAR-2025
DEFINITION  protein KRI1 homolog isoform 2 [Rattus norvegicus].
ACCESSION   NP_001385635 XP_038938719
VERSION     NP_001385635.1
DBSOURCE    REFSEQ: accession NM_001398706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 22, 2021 this sequence version replaced XP_038938719.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1211164.1,
                                           SRR26360176.2094334.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..698
                     /product="protein KRI1 homolog isoform 2"
                     /calculated_mol_wt=81186
     Region          318..427
                     /region_name="Kri1"
                     /note="KRI1-like family; pfam05178"
                     /db_xref="CDD:461569"
     Region          494..582
                     /region_name="Kri1_C"
                     /note="KRI1-like family C-terminal; pfam12936"
                     /db_xref="CDD:463756"
     CDS             1..698
                     /gene="Kri1"
                     /coded_by="NM_001398706.1:17..2113"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:687183"
                     /db_xref="RGD:1588903"
ORIGIN      
        1 mpeprapatl kvnaafaary sryrereelq rlkdrygdrd dgsdsssesd ssdehvefdp
       61 qqerdfyrtl sllkkkdpri yqkdatfyqr taeasssese eesaalgkqk kvqpmylkdy
      121 erkvilekeg kyvdednsdg esvdhrlqet atksyieeqr qlkesfrafv edssdedsag
      181 eggsgllqkh tksgeekaqe dvdylewlkg qkeidssesl kelthlkeyw nnpeldegeq
      241 flrdyilnkr yeedeeeete eervlgppvq lavddssdeg elflkkqedf ehkynfrfee
      301 pdsasvktyp rsiassvrrk ddrrkekree trerkkreka kkqeelkqlk nlkrkeilak
      361 leklrqvtgn etlgleeqdl eddfdpaqhd qlmqkcfgda fygtveeekp qfeeeegled
      421 dwnwdtwggp eqngawsqqe lhcedpdfnm dadydpsqpr kklreaptsg krkrkspfaa
      481 avgqekpmfd pgdktfeeyl deyyrldyed iiddlpcrfk yrtvvpcdfg lsteeilsad
      541 dkelnrwcsl kktcmyrseq eemqeqrays qkaqsvwkkr qifkslcqee vempteatgk
      601 spskassqvq lpmpsaaggk kpqaelsgak eeelahtpcp ekpasqkqks kkarllgptv
      661 tlgghkfsrq rlqafglnpk rlhfrqlgrq rkkqqsha
//
LOCUS       NP_001423358            1046 aa            linear   ROD 14-MAR-2025
DEFINITION  general transcription factor II-I repeat domain-containing protein
            1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423358 XP_063127132
VERSION     NP_001423358.1
DBSOURCE    REFSEQ: accession NM_001436429.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Ganaie,I.A., Malik,M.Z., Naqvi,S.H., Jain,S.K. and Wajid,S.
  TITLE     Differential levels of Alpha-1-inhibitor III, Immunoglobulin heavy
            chain variable region, and Hypertrophied skeletal muscle protein
            GTF3 in rat mammary tumorigenesis
  JOURNAL   Biochimie 174, 57-68 (2020)
   PUBMED   32325114
  REMARK    GeneRIF: Differential levels of Alpha-1-inhibitor III,
            Immunoglobulin heavy chain variable region, and Hypertrophied
            skeletal muscle protein GTF3 in rat mammary tumorigenesis.
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Palmer,S.J., Taylor,K.M., Santucci,N., Widagdo,J., Chan,Y.K.,
            Yeo,J.L., Adams,M., Gunning,P.W. and Hardeman,E.C.
  TITLE     GTF2IRD2 from the Williams-Beuren critical region encodes a
            mobile-element-derived fusion protein that antagonizes the action
            of its related family members
  JOURNAL   J Cell Sci 125 (Pt 21), 5040-5050 (2012)
   PUBMED   22899722
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Enkhmandakh,B., Makeyev,A.V., Erdenechimeg,L., Ruddle,F.H.,
            Chimge,N.O., Tussie-Luna,M.I., Roy,A.L. and Bayarsaihan,D.
  TITLE     Essential functions of the Williams-Beuren syndrome-associated
            TFII-I genes in embryonic development
  JOURNAL   Proc Natl Acad Sci U S A 106 (1), 181-186 (2009)
   PUBMED   19109438
REFERENCE   4  (residues 1 to 1046)
  AUTHORS   Olofsson,P., Holmberg,J., Tordsson,J., Lu,S., Akerstrom,B. and
            Holmdahl,R.
  TITLE     Positional identification of Ncf1 as a gene that regulates
            arthritis severity in rats
  JOURNAL   Nat Genet 33 (1), 25-32 (2003)
   PUBMED   12461526
REFERENCE   5  (residues 1 to 1046)
  AUTHORS   Bayarsaihan,D. and Ruddle,F.H.
  TITLE     Isolation and characterization of BEN, a member of the TFII-I
            family of DNA-binding proteins containing distinct helix-loop-helix
            domains
  JOURNAL   Proc Natl Acad Sci U S A 97 (13), 7342-7347 (2000)
   PUBMED   10861001
REFERENCE   6  (residues 1 to 1046)
  AUTHORS   Franke,Y., Peoples,R.J. and Francke,U.
  TITLE     Identification of GTF2IRD1, a putative transcription factor within
            the Williams-Beuren syndrome deletion at 7q11.23
  JOURNAL   Cytogenet Cell Genet 86 (3-4), 296-304 (1999)
   PUBMED   10575229
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced XP_063127132.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.50139.1,
                                           SRR26643298.80234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..1046
                     /product="general transcription factor II-I repeat
                     domain-containing protein 1 isoform 1"
                     /note="general transcription factor II I repeat
                     domain-containing 1; general transcription factor II-I
                     repeat domain-containing protein 1-like"
                     /calculated_mol_wt=117018
     Region          128..202
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          351..425
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          565..639
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          690..764
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          787..859
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     Region          890..962
                     /region_name="GTF2I"
                     /note="GTF2I-like repeat; pfam02946"
                     /db_xref="CDD:460759"
     CDS             1..1046
                     /gene="Gtf2ird1"
                     /gene_synonym="Gtf3"
                     /coded_by="NM_001436429.1:277..3417"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:246770"
                     /db_xref="RGD:620856"
ORIGIN      
        1 mallgkhcdi ptngcgserw nstfarkdel inslvsalds mcsalsklnt evacvavhne
       61 svfvmgtekg rvflntrkel qsdflrfcrg plwndpeagh pkkvqrcegg grsiprssle
      121 qcsdvyllqk mveevfdvly seamgratvv plpyerllre pgllavqglp eglafrrpae
      181 ydpkalmail ehshrirfkl rrppddggqd tkalvemngi sllpkgsrdc glhgqaskvs
      241 pqdltptatp ssmanflyst smpnhtirel kqevptcplt psdlglgwpv pephvpstqd
      301 fsdccgqapa gpagpliqnv haskrilfsi vhdksekwdp fikemedint lrecvqilfn
      361 sryaealgld hmvpvpyrki acdpeaveiv gipdkipfkr pctygvpklk rileerhsih
      421 fiikrmfder iftgnkftkd pmklepaspp edtatevcrd smldlagtaw sdmssvsedc
      481 gpgtsgeigm lrpikiepee ldiiqvtvsd psptseemtd slpghlpsed sgygmempad
      541 kgpseepwqe erpaeespgd virplrkqve mlfntkyaka igtsepvkvp yskflmhpee
      601 lfvlglpegi slrrpncfgi aklrkileas nsiqfvikrp elltdgvkep vmdtqerdsw
      661 dplvdetpkr qglqenyntr lsridiantl reqvqdlfnk kygealgiky pvqvpykrik
      721 snpgsviieg lppgipfrkp ctfgsqnler ilsvadkikf tvtrpfqgli pkpdeddanr
      781 lgekvilreq vkelfnekyg ealglnrpvl vpyklirdsp davevkglpd dipfrnpnty
      841 dihrlekilk ardhvrmvii nqlqpftevc ndpkvpdedd snklgkkvil reqvkelfne
      901 kygealglnr pvlvpyklir dspdavevkg lpddipfrnp ntydihrlek ilkardhvrm
      961 viinqlqpfg dvcnnakvpa kdnipkrkrk rvsegnsvss ssssssssss npesvastnq
     1021 islvqwpvym vdysglnvql pgpldy
//
LOCUS       NP_001423350             593 aa            linear   ROD 14-MAR-2025
DEFINITION  syntaxin-binding protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423350 XP_006248845
VERSION     NP_001423350.1
DBSOURCE    REFSEQ: accession NM_001436421.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Wan,L., Chen,X. and Almers,W.
  TITLE     Munc18-dependent and -independent clustering of syntaxin in the
            plasma membrane of cultured endocrine cells
  JOURNAL   Proc Natl Acad Sci U S A 118 (49) (2021)
   PUBMED   34857632
  REMARK    GeneRIF: Munc18-dependent and -independent clustering of syntaxin
            in the plasma membrane of cultured endocrine cells.
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Yu,H., Shen,C., Liu,Y., Menasche,B.L., Ouyang,Y., Stowell,M.H.B.
            and Shen,J.
  TITLE     SNARE zippering requires activation by SNARE-like peptides in
            Sec1/Munc18 proteins
  JOURNAL   Proc Natl Acad Sci U S A 115 (36), E8421-E8429 (2018)
   PUBMED   30127032
  REMARK    GeneRIF: SNARE zippering requires activation by SNARE-like peptides
            in Sec1/Munc18 proteins
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Qin,T., Liang,T., Zhu,D., Kang,Y., Xie,L., Dolai,S., Sugita,S.,
            Takahashi,N., Ostenson,C.G., Banks,K. and Gaisano,H.Y.
  TITLE     Munc18b Increases Insulin Granule Fusion, Restoring Deficient
            Insulin Secretion in Type-2 Diabetes Human and Goto-Kakizaki Rat
            Islets with Improvement in Glucose Homeostasis
  JOURNAL   EBioMedicine 16, 262-274 (2017)
   PUBMED   28163042
  REMARK    GeneRIF: Data show that Munc18b overexpression increased fusion of
            not only newcomer secretory granule (SG), but also predocked SGs in
            type-2 diabetes (T2D) human and Goto-Kakizaki Rat Islets.
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Gandasi,N.R. and Barg,S.
  TITLE     Contact-induced clustering of syntaxin and munc18 docks secretory
            granules at the exocytosis site
  JOURNAL   Nat Commun 5, 3914 (2014)
   PUBMED   24835618
  REMARK    GeneRIF: Secretory vesicles dock by inducing syntaxin1/munc18
            clustering in the target membrane.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Brochetta,C., Suzuki,R., Vita,F., Soranzo,M.R., Claver,J.,
            Madjene,L.C., Attout,T., Vitte,J., Varin-Blank,N., Zabucchi,G.,
            Rivera,J. and Blank,U.
  TITLE     Munc18-2 and syntaxin 3 control distinct essential steps in mast
            cell degranulation
  JOURNAL   J Immunol 192 (1), 41-51 (2014)
   PUBMED   24323579
  REMARK    GeneRIF: Munc18-2 and STX3 perform distinct, but complementary,
            functions to support, respectively, SG translocation and membrane
            fusion in mast cells.
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Coppola,T., Frantz,C., Perret-Menoud,V., Gattesco,S., Hirling,H.
            and Regazzi,R.
  TITLE     Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and
            controls exocytosis
  JOURNAL   Mol Biol Cell 13 (6), 1906-1915 (2002)
   PUBMED   12058058
  REMARK    GeneRIF: binds to granuphilin and controls exocytosis of pancreatic
            beta cells
REFERENCE   7  (residues 1 to 593)
  AUTHORS   van Niel,G., Raposo,G., Candalh,C., Boussac,M., Hershberg,R.,
            Cerf-Bensussan,N. and Heyman,M.
  TITLE     Intestinal epithelial cells secrete exosome-like vesicles
  JOURNAL   Gastroenterology 121 (2), 337-349 (2001)
   PUBMED   11487543
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Lehtonen,S., Riento,K., Olkkonen,V.M. and Lehtonen,E.
  TITLE     Syntaxin 3 and Munc-18-2 in epithelial cells during kidney
            development
  JOURNAL   Kidney Int 56 (3), 815-826 (1999)
   PUBMED   10469351
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Katagiri,H., Terasaki,J., Murata,T., Ishihara,H., Ogihara,T.,
            Inukai,K., Fukushima,Y., Anai,M., Kikuchi,M., Miyazaki,J. et al.
  TITLE     A novel isoform of syntaxin-binding protein homologous to yeast
            Sec1 expressed ubiquitously in mammalian cells
  JOURNAL   J Biol Chem 270 (10), 4963-4966 (1995)
   PUBMED   7890599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006248845.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.847246.1,
                                           SRR26360186.2080487.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..593
                     /product="syntaxin-binding protein 2 isoform 2"
                     /note="unc-18B; unc18-2; unc-18 homolog 2; unc-18 homolog
                     B; munc18-2; protein unc-18 homolog 2; protein unc-18
                     homolog B; syntaxin binding protein Munc18-2"
                     /calculated_mol_wt=66436
     Region          29..579
                     /region_name="Sec1"
                     /note="Sec1 family; pfam00995"
                     /db_xref="CDD:460020"
     CDS             1..593
                     /gene="Stxbp2"
                     /gene_synonym="Munc18b"
                     /coded_by="NM_001436421.1:14..1795"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:81804"
                     /db_xref="RGD:619967"
ORIGIN      
        1 maplglkavv gekilsgvir svkkdgewkv limdhpsmri lsscckmsdi laegitived
       61 inkrrepips leaiyllspt eksvqaliad fqgtptftyk aahifftdtc peplfselgr
      121 srlakvvktl keihlaflpy eaqvfsldap hstynlycpf ragergrqld vlaqqiatlc
      181 atlqeypsir yrkgpedtaq lahavlakln afkadtpslg egpektrsql limdraadpv
      241 spllheltfq amaydllhie qdtyryettg lsesrekavl ldedddlwve lrhmhiadvs
      301 kkvtellktf ceskrlttdk anikdlshil kkmpqyqkel nkysthlhla ddcmkhfkgs
      361 veklcgveqd lamgsdaege kikdtmkliv pvlldasvpp ydkirvllly illrngvsee
      421 nlakliqhan vqsysnlirn leqlggtvtn sagsgtssrl errermepty qlsrwspvik
      481 dvmedvvedr ldrklwpfvs dpapvsssqa avsarfghwh knkagieara gprlivyivg
      541 gvamsemraa yevtrategk wevligsshi ltptrflddl rtldqkledi alp
//
LOCUS       NP_001423348            1494 aa            linear   ROD 14-MAR-2025
DEFINITION  B-cell CLL/lymphoma 9-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423348 XP_017451040
VERSION     NP_001423348.1
DBSOURCE    REFSEQ: accession NM_001436419.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1494)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1494)
  AUTHORS   Deka,J., Wiedemann,N., Anderle,P., Murphy-Seiler,F., Bultinck,J.,
            Eyckerman,S., Stehle,J.C., Andre,S., Vilain,N., Zilian,O.,
            Robine,S., Delorenzi,M., Basler,K. and Aguet,M.
  TITLE     Bcl9/Bcl9l are critical for Wnt-mediated regulation of stem cell
            traits in colon epithelium and adenocarcinomas
  JOURNAL   Cancer Res 70 (16), 6619-6628 (2010)
   PUBMED   20682801
REFERENCE   3  (residues 1 to 1494)
  AUTHORS   Brack,A.S., Murphy-Seiler,F., Hanifi,J., Deka,J., Eyckerman,S.,
            Keller,C., Aguet,M. and Rando,T.A.
  TITLE     BCL9 is an essential component of canonical Wnt signaling that
            mediates the differentiation of myogenic progenitors during muscle
            regeneration
  JOURNAL   Dev Biol 335 (1), 93-105 (2009)
   PUBMED   19699733
REFERENCE   4  (residues 1 to 1494)
  AUTHORS   Fritzmann,J., Morkel,M., Besser,D., Budczies,J., Kosel,F.,
            Brembeck,F.H., Stein,U., Fichtner,I., Schlag,P.M. and Birchmeier,W.
  TITLE     A colorectal cancer expression profile that includes transforming
            growth factor beta inhibitor BAMBI predicts metastatic potential
  JOURNAL   Gastroenterology 137 (1), 165-175 (2009)
   PUBMED   19328798
REFERENCE   5  (residues 1 to 1494)
  AUTHORS   Adachi,S., Jigami,T., Yasui,T., Nakano,T., Ohwada,S., Omori,Y.,
            Sugano,S., Ohkawara,B., Shibuya,H., Nakamura,T. and Akiyama,T.
  TITLE     Role of a BCL9-related beta-catenin-binding protein, B9L, in
            tumorigenesis induced by aberrant activation of Wnt signaling
  JOURNAL   Cancer Res 64 (23), 8496-8501 (2004)
   PUBMED   15574752
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_017451040.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.848865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1494
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..1494
                     /product="B-cell CLL/lymphoma 9-like protein isoform 1"
                     /note="B-cell CLL/lymphoma 9-like protein"
                     /calculated_mol_wt=156751
     Region          395..431
                     /region_name="BCL9"
                     /note="B-cell lymphoma 9 protein; pfam11502"
                     /db_xref="CDD:431912"
     Region          <888..1351
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1494
                     /gene="Bcl9l"
                     /coded_by="NM_001436419.1:796..5280"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300673"
                     /db_xref="RGD:1309096"
ORIGIN      
        1 mrilanktrl phprrreapg spplsprghc ppapakpmhp enkltnhgkt gnggaqsqhq
       61 nvnqgptcnl gskgvgagsh gakanqisps nsslknpqag vspfsslkgk vkrersvsvd
      121 sgeqreagtp sldseakeva prskrrcvle rkqpysgdew csgpdseedd kpigathncn
      181 vadpamvapq lgpgqtaqlp lsensapgpq hgpppglrpd vpggggggvp gkppsqfvyv
      241 ftthlantaa eavlqgraes ilayhqqnvp rakldqapkv pptpeplpln tpsagtpqsq
      301 ppplpppppa pgsappalpq egppedtsqd lapnsvgaas tgggtggthp ntptaatann
      361 plppggdpgs apgsallgea tptgngqrnl vgseglskeq lehrerslqt lrdierlllr
      421 sgetepflkg ppggaveggp paqapsaaqq ppsapppglk kyeeplqsmi sqtqslggpp
      481 lehevpghpq ggdmgqqmnm mmqrlgqdsl tpeqvawrkl qeeyyeekrr keeqiglhgg
      541 rplqdmvgmg gmmgrgpppp yhskpgdqwp pgmgtqlrgp mdvqdpmqlr pgppfpgprf
      601 pgnqmqrvpg fggmqsipme vpmnamqrpv rpgmawnedl ppiggpsnfa qnavpypggq
      661 geaerfmtpr vreellrhql lekrsmgmqr plgmagsgmg qsmemermiq thrqmdptmf
      721 pgqmtggdgl agtpmgiefg ggrgllsppm gqsglrevdp pmgpgnlnmn mnvnmnmnmn
      781 lnvqmtpqqq mlmsqkmrgp gdmmgpqgls peemarvraq nssgmmagpq kmlmpsqfpn
      841 qgqqgfsggq gpyqampqdm gntpdmfspd qssvpmgavg tarlshmplp pasnppgsvh
      901 sapnrglgrr psdltisinq mgspgmghlk sptlsqvhsp lvtspsanlk spqtpsqmvp
      961 lpsanppgpl kspqvlsssl svrsptgsps rlkspsmavp spgwvaspkt ampspgvsqn
     1021 kqpplninss stlgnleqga lppagprnss sappanppss lmnpslpfts spdptpsqnp
     1081 lslmmsqmsk yampsstply hnaiktiats ddellpdrpl lppppppqgs gpgisnnqpn
     1141 qmhmnpaaaq spmgmnlpgq qplshepppt mlpsptplgs niplhpnaqg tggpsqnsmm
     1201 mapggpdsln tpcgpvpsss qmmsfpprlq qphgamaatg gggpglqqhy psgmalpped
     1261 lpnqppgpip sqqhlmgkgm agrmgdaypp gvlpgvasvl ndpelsevir ptptgipefd
     1321 lsriipsekp sstlqyfpkn enqppkaqpp nlhlmnlqnm maeqapsrpp nlpgqqgvqr
     1381 glsmsmchpg qmsllgrtgv ppqqgmvphg lhqgvmsppq glmtqqnfml mkqrgvggev
     1441 ytqpphmlsp qgslmapppq qnlmvshplr qrsvsldsqm gylptpggma nlpf
//
LOCUS       NP_001423357             367 aa            linear   ROD 14-MAR-2025
DEFINITION  2'-5'-oligoadenylate synthase 1A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423357 XP_006249444
VERSION     NP_001423357.1
DBSOURCE    REFSEQ: accession NM_001436428.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Leisching,G., Cole,V., Ali,A.T. and Baker,B.
  TITLE     OAS1, OAS2 and OAS3 restrict intracellular M. tb replication and
            enhance cytokine secretion
  JOURNAL   Int J Infect Dis 80S, S77-S84 (2019)
   PUBMED   30822544
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Sarmiento,L., Frisk,G., Anagandula,M., Hodik,M., Barchetta,I.,
            Netanyah,E., Cabrera-Rode,E. and Cilio,C.M.
  TITLE     Echovirus 6 Infects Human Exocrine and Endocrine Pancreatic Cells
            and Induces Pro-Inflammatory Innate Immune Response
  JOURNAL   Viruses 9 (2), 25 (2017)
   PUBMED   28146100
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Kim,S., Kim,M.J., Park,D.Y., Chung,H.J., Kim,C.H., Yoon,J.H. and
            Kim,H.J.
  TITLE     Mitochondrial reactive oxygen species modulate innate immune
            response to influenza A virus in human nasal epithelium
  JOURNAL   Antiviral Res 119, 78-83 (2015)
   PUBMED   25930096
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Go,M.J., Hwang,J.Y., Kim,Y.J., Hee Oh,J., Kim,Y.J., Heon Kwak,S.,
            Soo Park,K., Lee,J., Kim,B.J., Han,B.G., Cho,M.C., Cho,Y.S. and
            Lee,J.Y.
  TITLE     New susceptibility loci in MYL2, C12orf51 and OAS1 associated with
            1-h plasma glucose as predisposing risk factors for type 2 diabetes
            in the Korean population
  JOURNAL   J Hum Genet 58 (6), 362-365 (2013)
   PUBMED   23575436
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Donovan,J., Dufner,M. and Korennykh,A.
  TITLE     Structural basis for cytosolic double-stranded RNA surveillance by
            human oligoadenylate synthetase 1
  JOURNAL   Proc Natl Acad Sci U S A 110 (5), 1652-1657 (2013)
   PUBMED   23319625
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Hartmann,R., Walko,G. and Justesen,J.
  TITLE     Inhibition of 2'-5' oligoadenylate synthetase by divalent metal
            ions
  JOURNAL   FEBS Lett 507 (1), 54-58 (2001)
   PUBMED   11682059
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Truve,E., Aaspollu,A., Honkanen,J., Puska,R., Mehto,M., Hassi,A.,
            Teeri,T.H., Kelve,M., Seppanen,P. and Saarma,M.
  TITLE     Transgenic potato plants expressing mammalian 2'-5' oligoadenylate
            synthetase are protected from potato virus X infection under field
            conditions
  JOURNAL   Biotechnology (N Y) 11 (9), 1048-1052 (1993)
   PUBMED   7764002
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Shiojiri,S., Fukunaga,R., Ichii,Y. and Sokawa,Y.
  TITLE     Structure and expression of a cloned cDNA for human
            (2'-5')oligoadenylate synthetase
  JOURNAL   J Biochem 99 (5), 1455-1464 (1986)
   PUBMED   3754863
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Wathelet,M., Moutschen,S., Cravador,A., DeWit,L., Defilippi,P.,
            Huez,G. and Content,J.
  TITLE     Full-length sequence and expression of the 42 kDa 2-5A synthetase
            induced by human interferon
  JOURNAL   FEBS Lett 196 (1), 113-120 (1986)
   PUBMED   3753689
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Shimizu,N. and Sokawa,Y.
  TITLE     (2'-5')Oligoadenylate synthetase in pig spleen: isolation and
            characterization
  JOURNAL   J Biochem 94 (5), 1421-1428 (1983)
   PUBMED   6654863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006249444.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086979.1, FQ231421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..367
                     /product="2'-5'-oligoadenylate synthase 1A isoform 1"
                     /EC_number="2.7.7.84"
                     /note="2'-5'-oligoadenylate synthetase 1;
                     2'-5'-oligoadenylate synthase 1; 2'-5' oligoadenylate
                     synthetase 1G; 2-5A synthetase 1; (2-5')oligo(A)
                     synthetase 1; 2-5A synthase 1; (2-5')oligo(A) synthase 1;
                     2',5'-oligoadenylate synthetase 1, 40/46kDa; 25
                     oligoadenylate synthetase; 2-5A synthase 1A;
                     (2-5')oligo(A) synthase 1A; 2'-5'-oligoadenylate synthase
                     1A"
                     /calculated_mol_wt=42516
     Region          27..167
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(62..64,67,69..71,76,78,128..129,132,149)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(76,78,149)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          164..350
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     CDS             1..367
                     /gene="Oas1a"
                     /gene_synonym="Oas1; Oas1g"
                     /coded_by="NM_001436428.1:69..1172"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:192281"
                     /db_xref="RGD:621760"
ORIGIN      
        1 meqelrstps wkldkfievy llpntsfrdd vksainvlcd flkercfrdt vhpvrvskvv
       61 kggssgkgtt lkgksdadlv vflnnftsfe dqlnrrgefi keikkqlyev qrekhfrvkf
      121 evqsswwpnp ralsfklsap hlqqevefdv lpaydvlghv slysnpdpki ytilisecis
      181 lgkegefstc ftelqrnflk qrptklksli rlvkhwyqlc keklgkplpp qyalelltvy
      241 awergngite fntaqgfrti lelvtkyqql riywtkyydf qhpdvskylh rqlrksrpvi
      301 ldpadptgnv aggnqegwrr lasearlwlq ypcfmnrggs pvsswevpte vpvpseqvde
      361 awscill
//
LOCUS       NP_001004080             780 aa            linear   ROD 15-MAR-2025
DEFINITION  gelsolin precursor [Rattus norvegicus].
ACCESSION   NP_001004080 XP_216043
VERSION     NP_001004080.1
DBSOURCE    REFSEQ: accession NM_001004080.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Benavente-Fernandez,I., Ramos-Rodriguez,J.J., Infante-Garcia,C.,
            Jimenez-Gomez,G., Lechuga-Sancho,A., Lubian-Lopez,S. and
            Garcia-Alloza,M.
  TITLE     Altered plasma-type gelsolin and amyloid-beta in neonates with
            hypoxic-ischaemic encephalopathy under therapeutic hypothermia
  JOURNAL   J Cereb Blood Flow Metab 39 (7), 1349-1354 (2019)
   PUBMED   29466895
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Gupta,A.K., Chopra,B.S., Vaid,B., Sagar,A., Raut,S., Badmalia,M.D.,
            Ashish and Khatri,N.
  TITLE     Protective effects of gelsolin in acute pulmonary thromboembolism
            and thrombosis in the carotid artery of mice
  JOURNAL   PLoS One 14 (4), e0215717 (2019)
   PUBMED   31002695
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Hu,W.S., Ting,W.J., Tamilselvi,S., Day,C.H., Wang,T., Chiang,W.D.,
            Viswanadha,V.P., Yeh,Y.L., Lin,W.T. and Huang,C.Y.
  TITLE     Oral administration of alcalase potato protein hydrolysate-APPH
            attenuates high fat diet-induced cardiac complications via
            TGF-beta/GSN axis in aging rats
  JOURNAL   Environ Toxicol 34 (1), 5-12 (2019)
   PUBMED   30240538
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Gertz,K., Uhlemann,R., Foryst-Ludwig,A., Barrientos,R.M.,
            Kappert,K., Thone-Reineke,C., Djoufack,P., Kirschbaum,C.,
            Fink,K.B., Heinz,A., Kintscher,U., Endres,M. and Kronenberg,G.
  TITLE     The cytoskeleton in 'couch potato-ism': Insights from a murine
            model of impaired actin dynamics
  JOURNAL   Exp Neurol 306, 34-44 (2018)
   PUBMED   29684438
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Segado-Arenas,A., Infante-Garcia,C., Benavente-Fernandez,I.,
            Sanchez-Sotano,D., Ramos-Rodriguez,J.J., Alonso-Ojembarrena,A.,
            Lubian-Lopez,S. and Garcia-Alloza,M.
  TITLE     Cognitive Impairment and Brain and Peripheral Alterations in a
            Murine Model of Intraventricular Hemorrhage in the Preterm Newborn
  JOURNAL   Mol Neurobiol 55 (6), 4896-4910 (2018)
   PUBMED   28755273
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Levy,E., Haltia,M., Fernandez-Madrid,I., Koivunen,O., Ghiso,J.,
            Prelli,F. and Frangione,B.
  TITLE     Mutation in gelsolin gene in Finnish hereditary amyloidosis
  JOURNAL   J Exp Med 172 (6), 1865-1867 (1990)
   PUBMED   2175344
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Chaponnier,C., Kocher,O. and Gabbiani,G.
  TITLE     Modulation of gelsolin content in rat aortic smooth muscle cells
            during development, experimental intimal thickening and culture. An
            immunohistochemical and biochemical study
  JOURNAL   Eur J Biochem 190 (3), 559-565 (1990)
   PUBMED   2164930
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Rabie,A., Ferraz,C., Clavel,M.C. and Legrand,C.
  TITLE     Gelsolin immunoreactivity and development of the tectorial membrane
            in the cochlea of normal and hypothyroid rats
  JOURNAL   Cell Tissue Res 254 (1), 241-245 (1988)
   PUBMED   2848627
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Smith,D.B., Janmey,P.A. and Lind,S.E.
  TITLE     Circulating actin-gelsolin complexes following oleic acid-induced
            lung injury
  JOURNAL   Am J Pathol 130 (2), 261-267 (1988)
   PUBMED   2829631
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Kwiatkowski,D.J., Stossel,T.P., Orkin,S.H., Mole,J.E., Colten,H.R.
            and Yin,H.L.
  TITLE     Plasma and cytoplasmic gelsolins are encoded by a single gene and
            contain a duplicated actin-binding domain
  JOURNAL   Nature 323 (6087), 455-458 (1986)
   PUBMED   3020431
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079472.1.
            
            On Sep 3, 2004 this sequence version replaced XP_216043.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132271, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..780
                     /product="gelsolin precursor"
                     /note="ADF; brevin; actin-depolymerizing factor"
                     /calculated_mol_wt=83511
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2575
     mat_peptide     26..780
                     /product="Gelsolin. /id=PRO_0000288477"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
                     /calculated_mol_wt=83511
     Region          28..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          51..174
                     /region_name="Actin-severing. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          57..169
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Site            order(74..75,114,120..121,123..125,127..129,131..132,143,
                     145)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          121..124
                     /region_name="Actin-actin interfilament contact point.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          184..273
                     /region_name="gelsolin_S2_like"
                     /note="Gelsolin sub-domain 2-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11289"
                     /db_xref="CDD:200445"
     Region          196..268
                     /region_name="Gelsolin-like 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          244..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          296..393
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Region          315..387
                     /region_name="Gelsolin-like 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Site            order(388,393)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          432..780
                     /region_name="Actin-binding, Ca-sensitive.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          437..537
                     /region_name="gelsolin_S4_like"
                     /note="Gelsolin sub-domain 4-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11293"
                     /db_xref="CDD:200449"
     Site            order(453..454,492,498..499,501..503,505..507,509..510,
                     521,523)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200449"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Site            528
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200449"
     Region          559..647
                     /region_name="gelsolin_S5_like"
                     /note="Gelsolin sub-domain 5-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11288"
                     /db_xref="CDD:200444"
     Site            567
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200444"
     Site            582
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P13020; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     Region          664..762
                     /region_name="gelsolin_S6_like"
                     /note="Gelsolin sub-domain 6-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11291"
                     /db_xref="CDD:200447"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P06396; propagated from
                     UniProtKB/Swiss-Prot (Q68FP1.1)"
     CDS             1..780
                     /gene="Gsn"
                     /coded_by="NM_001004080.1:11..2353"
                     /db_xref="GeneID:296654"
                     /db_xref="RGD:1303089"
ORIGIN      
        1 mapycsslrs allvlalcal spshaatasr graqerapqs rvsetrpstm vvehpeflka
       61 gkepglqiwr vekfdlvpvp pnlygdfftg dayvilktvq lrngnlqydl hywlgnecsq
      121 desgaaaift vqlddylngr avqhrevqgf esstfqgyfk sglkykkggv asgfkhvvpn
      181 evvvqrlfqv kgrrvvrate vpvswdsfnn gdcfildlgn niyqwcgsgs nkferlkatq
      241 vskgirdner sgraqvhvse egsepeamlq vlgpkpdlpq gtedtakeda anrrlaklyk
      301 vsnsggsmsv slvadenpfa qsalrsedcf ildhgrdgki fvwkgkqanm derkaalkta
      361 sdfiskmqyp rqtqvsvlpe ggetplfkqf fknwrdpdqt dgpglsylss hianvervpf
      421 daatlhtsta maaqhgmddd gtgqkqiwri egsnkvlvdp atygqfyggd syiilynyrh
      481 ggrqgqiiyn wqgaqstqde vaasailtaq ldeelggtpv qsrvvqgkep ahlmslfggk
      541 pmiiykggts rdggqttpas trlfqvrass sgatravevm pkagalnsnd afvlktpsaa
      601 ylwvgtgasd aektgalell kvlraqhvqv eegsepdgfw ealggktayr tsprlkdkkm
      661 dahpprlfac snrigrfvie evpgelmqed latddvmlld twdqvfvwvg kdsqeeekte
      721 altsakryie tdpanrdrrt pitvvrqgfe ppsfvgwflg wdddywsvdp ldralaelaa
//
LOCUS       NP_001012044             627 aa            linear   ROD 15-MAR-2025
DEFINITION  plastin-2 [Rattus norvegicus].
ACCESSION   NP_001012044 XP_224406
VERSION     NP_001012044.1
DBSOURCE    REFSEQ: accession NM_001012044.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Zhang,W., Xu,L., Yu,Z., Zhang,M., Liu,J. and Zhou,J.
  TITLE     Inhibition of the Glycolysis Prevents the Cerebral Infarction
            Progression Through Decreasing the Lactylation Levels of LCP1
  JOURNAL   Mol Biotechnol 65 (8), 1336-1345 (2023)
   PUBMED   36574182
  REMARK    GeneRIF: Inhibition of the Glycolysis Prevents the Cerebral
            Infarction Progression Through Decreasing the Lactylation Levels of
            LCP1.
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Forster,F., Paster,W., Supper,V., Schatzlmaier,P., Sunzenauer,S.,
            Ostler,N., Saliba,A., Eckerstorfer,P., Britzen-Laurent,N.,
            Schutz,G., Schmid,J.A., Zlabinger,G.J., Naschberger,E., Sturzl,M.
            and Stockinger,H.
  TITLE     Guanylate binding protein 1-mediated interaction of T cell antigen
            receptor signaling with the cytoskeleton
  JOURNAL   J Immunol 192 (2), 771-781 (2014)
   PUBMED   24337748
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Choi,J.H., Lee,M.Y., Ramakrishna,S., Kim,Y., Shim,J.Y., Han,S.M.,
            Kim,J.Y., Lee,D.H., Choi,Y.K. and Baek,K.H.
  TITLE     LCP1 up-regulated by partial pancreatectomy supports cell
            proliferation and differentiation
  JOURNAL   Mol Biosyst 7 (11), 3104-3111 (2011)
   PUBMED   21922118
  REMARK    GeneRIF: the LCP1 may play a critical role in the pancreas
            regeneration.
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Ohsawa,K., Imai,Y., Sasaki,Y. and Kohsaka,S.
  TITLE     Microglia/macrophage-specific protein Iba1 binds to fimbrin and
            enhances its actin-bundling activity
  JOURNAL   J Neurochem 88 (4), 844-856 (2004)
   PUBMED   14756805
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   9  (residues 1 to 627)
  AUTHORS   Chafel,M.M., Shen,W. and Matsudaira,P.
  TITLE     Sequential expression and differential localization of I-, L-, and
            T-fimbrin during differentiation of the mouse intestine and yolk
            sac
  JOURNAL   Dev Dyn 203 (2), 141-151 (1995)
   PUBMED   7655078
REFERENCE   10 (residues 1 to 627)
  AUTHORS   Zu,Y., Kohno,M., Kubota,I., Nishida,E., Hanaoka,M. and Namba,Y.
  TITLE     Characterization of interleukin 2 stimulated 65-kilodalton
            phosphoprotein in human T cells
  JOURNAL   Biochemistry 29 (4), 1055-1062 (1990)
   PUBMED   2111166
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083855.1.
            
            On Feb 11, 2005 this sequence version replaced XP_224406.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132301, SAMD00132303
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..627
                     /product="plastin-2"
                     /calculated_mol_wt=69991
     Region          13..79
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(22,24,26,33,62,64,66,73)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Region          98..242
                     /region_name="CH_PLS_rpt1"
                     /note="first calponin homology (CH) domain found in the
                     plastin family; cd21292"
                     /db_xref="CDD:409141"
     Site            order(122,126,189,191..192,195..196,198,207..215,220,
                     222..223,225..226,229..230,233)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409141"
     Region          251..375
                     /region_name="CH_PLS2_rpt2"
                     /note="second calponin homology (CH) domain found in
                     plastin-2; cd21327"
                     /db_xref="CDD:409176"
     Site            order(266,270,329,331..332,335..336,338,346..354,359,
                     361..362,364..365,368..369,372)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409176"
     Region          374..507
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Site            order(400,455,457..458,461..462,464,478..482,487,489..490,
                     492..493,496..497,500)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409180"
     Region          511..625
                     /region_name="CH_PLS2_rpt4"
                     /note="fourth calponin homology (CH) domain found in
                     plastin-2; cd21333"
                     /db_xref="CDD:409182"
     Site            order(517,521,578,580..581,584..585,587,595..603,608,
                     610..611,613..614,617..618,621)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409182"
     CDS             1..627
                     /gene="Lcp1"
                     /coded_by="NM_001012044.1:46..1929"
                     /db_xref="GeneID:306071"
                     /db_xref="RGD:1308288"
ORIGIN      
        1 margsvsdee mmelreafak vdtdgngyis cnelndlfka aclplpgyrv reitenlmat
       61 gdldqdgkis fdefikvfhg lkstevaktf rkainkkegi caiggtseqs svgtqhsyse
      121 eekyafvnwi nkalendpdc rhvipmnpnt ddlfnavgdg ivlckmvnls vpdtiderti
      181 nkkkltpfti qenlnlalns asaigchvvn igaedlkegk pylvlgllwq vikiglfadi
      241 elsrnealia llregesled lmklspeell lrwanyhlen agctkitnfs tdikdskayy
      301 hlleqvaprg deegipavvi dmsglrekdd iqraecmlqq aerlgcrqfv tatdvvrgnp
      361 klnlafianl fnkypalhkp enqdidwgal egetreertf rnwmnslgvn pgvnhlysdl
      421 sdalvifqly ekikvpvdwn rvnrppypkl ggnmkklenc nyavdlgknq akfslvgiag
      481 qdlnegnrtl tlalvwqlmr rytlniledi gggqkvnddi ivnwvnttlk eaqksssits
      541 fkdpkistsl pvldlidaiq pgsinydllk tenlddeekl nnakyaisma rkigarvyal
      601 pedlvevnpk mvmtvfaclm gkgmkrv
//
LOCUS       NP_001013104             349 aa            linear   ROD 15-MAR-2025
DEFINITION  macrophage-capping protein [Rattus norvegicus].
ACCESSION   NP_001013104 XP_216166
VERSION     NP_001013104.1
DBSOURCE    REFSEQ: accession NM_001013086.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hubert,T., Van Impe,K., Vandekerckhove,J. and Gettemans,J.
  TITLE     The actin-capping protein CapG localizes to microtubule-dependent
            organelles during the cell cycle
  JOURNAL   Biochem Biophys Res Commun 380 (1), 166-170 (2009)
   PUBMED   19166812
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Trost,M., English,L., Lemieux,S., Courcelles,M., Desjardins,M. and
            Thibault,P.
  TITLE     The phagosomal proteome in interferon-gamma-activated macrophages
  JOURNAL   Immunity 30 (1), 143-154 (2009)
   PUBMED   19144319
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Hubert,T., Van Impe,K., Vandekerckhove,J. and Gettemans,J.
  TITLE     The F-actin filament capping protein CapG is a bona fide nucleolar
            protein
  JOURNAL   Biochem Biophys Res Commun 377 (2), 699-704 (2008)
   PUBMED   18938132
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Van Impe,K., Hubert,T., De Corte,V., Vanloo,B., Boucherie,C.,
            Vandekerckhove,J. and Gettemans,J.
  TITLE     A new role for nuclear transport factor 2 and Ran: nuclear import
            of CapG
  JOURNAL   Traffic 9 (5), 695-707 (2008)
   PUBMED   18266911
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Witke,W., Li,W., Kwiatkowski,D.J. and Southwick,F.S.
  TITLE     Comparisons of CapG and gelsolin-null macrophages: demonstration of
            a unique role for CapG in receptor-mediated ruffling, phagocytosis,
            and vesicle rocketing
  JOURNAL   J Cell Biol 154 (4), 775-784 (2001)
   PUBMED   11514591
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079104.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216166.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079104.1, SRR8487230.30007.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMEA5756307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..349
                     /product="macrophage-capping protein"
                     /note="actin regulatory protein CAP-G; capping protein
                     (actin filament), gelsolin-like"
                     /calculated_mol_wt=38668
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P40121; propagated from
                     UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Region          17..120
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Region          28..107
                     /region_name="Gelsolin-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Site            order(29..30,65,71..72,74..76,78..80,82..83,94,96)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Region          138..147
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Region          139..226
                     /region_name="gelsolin_S2_like"
                     /note="Gelsolin sub-domain 2-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11289"
                     /db_xref="CDD:200445"
     Region          147..222
                     /region_name="Gelsolin-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Region          247..347
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Region          264..342
                     /region_name="Gelsolin-like 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYC4.1)"
     Site            order(342,347)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     CDS             1..349
                     /gene="Capg"
                     /coded_by="NM_001013086.1:306..1355"
                     /db_xref="GeneID:297339"
                     /db_xref="RGD:1311724"
ORIGIN      
        1 mytpipqsgs pfpasvqdpg lhiwrveklk pvpiarenhg iffsgdsylv lhngpeeash
       61 lhlwigqqss rdeqgacavl avhlntllge rpvqhrevqg nesdlfmsyf pqglkyregg
      121 vesafhktts gttpaairkl yqvkgkknir ateralswds fntgdcfild lgqnifawcg
      181 gksnilernk ardlalaird serqgkaqve iitdgeepae miqvlgpkpa lkegnpeedi
      241 tadqtnaqaa alykvsdatg qmnltkvads spfasellip ddcfvldngl cgkiyiwkgr
      301 kanekerqaa lqvadgfisr mryspntqve ilpqgrespi fkqffkdwk
//
LOCUS       NP_112316                662 aa            linear   ROD 15-MAR-2025
DEFINITION  72 kDa type IV collagenase precursor [Rattus norvegicus].
ACCESSION   NP_112316
VERSION     NP_112316.2
DBSOURCE    REFSEQ: accession NM_031054.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Wang,C., Xu,Y., Xu,M., Sun,C., Zhang,X., Tao,X. and Song,T.
  TITLE     SPOCK2 modulates neuropathic pain by interacting with MT1-MMP to
            regulate astrocytic MMP-2 activation in rats with chronic
            constriction injury
  JOURNAL   J Neuroinflammation 21 (1), 57 (2024)
   PUBMED   38388415
  REMARK    GeneRIF: SPOCK2 modulates neuropathic pain by interacting with
            MT1-MMP to regulate astrocytic MMP-2 activation in rats with
            chronic constriction injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Hirata,T., Fan,F., Fan,L., Amin,G., White,T., Geurts,A.M.,
            Kojima,N., Takahashi,T., Miyata,N., Williams,J. and Roman,R.J.
  TITLE     Knockout of Matrix Metalloproteinase 2 Opposes Hypertension- and
            Diabetes-induced Nephropathy
  JOURNAL   J Cardiovasc Pharmacol 82 (6), 445-457 (2023)
   PUBMED   37643020
  REMARK    GeneRIF: Knockout of Matrix Metalloproteinase 2 Opposes
            Hypertension- and Diabetes-induced Nephropathy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Zhu,X., Tang,Z., Li,W., Li,X., Iwakiri,Y. and Liu,F.
  TITLE     S-nitrosylation of EMMPRIN influences the migration of HSCs and MMP
            activity in liver fibrosis
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1640-1649 (2023)
   PUBMED   37700592
  REMARK    GeneRIF: S-nitrosylation of EMMPRIN influences the migration of
            HSCs and MMP activity in liver fibrosis.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   de Oliveira Neves,V.G., Blascke de Mello,M.M., Rodrigues,D.,
            Pernomian,L., de Oliveira,I.S., Parente,J.M., Arantes,E.C.,
            Tostes,R.C. and Castro,M.M.
  TITLE     Type I collagen proteolysis by matrix metalloproteinase-2
            contributes to focal adhesion kinase activation and vascular smooth
            muscle cell proliferation in the aorta in early hypertension
  JOURNAL   Vascul Pharmacol 152, 107211 (2023)
   PUBMED   37607602
  REMARK    GeneRIF: Type I collagen proteolysis by matrix metalloproteinase-2
            contributes to focal adhesion kinase activation and vascular smooth
            muscle cell proliferation in the aorta in early hypertension.
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Hu,C., Jing,R., Wen,C., Qi,T., Bai,X., Wang,Y., Shao,Y. and Pei,C.
  TITLE     HNF4A Negatively Regulated Posterior Capsular Opacification via
            Transcriptional Inhibition of MMP2
  JOURNAL   Curr Eye Res 48 (7), 627-638 (2023)
   PUBMED   36988559
  REMARK    GeneRIF: HNF4A Negatively Regulated Posterior Capsular
            Opacification via Transcriptional Inhibition of MMP2.
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Harendza,S., Pollock,A.S., Mertens,P.R. and Lovett,D.H.
  TITLE     Tissue-specific enhancer-promoter interactions regulate high level
            constitutive expression of matrix metalloproteinase 2 by glomerular
            mesangial cells
  JOURNAL   J Biol Chem 270 (32), 18786-18796 (1995)
   PUBMED   7642529
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Lerch,M.M., Friess,H., Buchler,M.
            and Adler,G.
  TITLE     Expression and in-situ localization of genes coding for
            extracellular matrix proteins and extracellular matrix degrading
            proteases in pancreatic cancer
  JOURNAL   Int J Cancer 62 (4), 407-413 (1995)
   PUBMED   7635566
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Nakano,A., Tani,E., Miyazaki,K., Yamamoto,Y. and Furuyama,J.
  TITLE     Matrix metalloproteinases and tissue inhibitors of
            metalloproteinases in human gliomas
  JOURNAL   J Neurosurg 83 (2), 298-307 (1995)
   PUBMED   7616276
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Cleutjens,J.P., Kandala,J.C., Guarda,E., Guntaka,R.V. and
            Weber,K.T.
  TITLE     Regulation of collagen degradation in the rat myocardium after
            infarction
  JOURNAL   J Mol Cell Cardiol 27 (6), 1281-1292 (1995)
   PUBMED   8531210
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Marti,H.P., McNeil,L., Davies,M., Martin,J. and Lovett,D.H.
  TITLE     Homology cloning of rat 72 kDa type IV collagenase: cytokine and
            second-messenger inducibility in glomerular mesangial cells
  JOURNAL   Biochem J 291 (Pt 2) (Pt 2), 441-446 (1993)
   PUBMED   7916617
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U65656.1.
            
            On May 4, 2007 this sequence version replaced NP_112316.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U65656.1, BC074013.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093044, SAMN16093046
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..662
                     /product="72 kDa type IV collagenase precursor"
                     /EC_number="3.4.24.24"
                     /note="72 KDa type IV collagenase; MMP-2; 72 kDa
                     gelatinase; matrix metalloproteinase-2; gelatinase A"
                     /calculated_mol_wt=71062
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3106
     Region          <70..97
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
     Region          100..107
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
     mat_peptide     110..662
                     /product="72 kDa type IV collagenase. /id=PRO_0000028721"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
                     /calculated_mol_wt=62130
     Region          110..221
                     /region_name="Collagenase-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
     Region          118..446
                     /region_name="Peptidase_M10"
                     /note="Matrixin; pfam00413"
                     /db_xref="CDD:425668"
     Region          222..396
                     /region_name="Collagen-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
     Region          226..274
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(237,239,244,258,265,271,273)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          284..332
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(295,297,302,316,323,329,331)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          342..390
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(353,355,360,374,381,387,389)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          397..467
                     /region_name="Collagenase-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
     Region          414..662
                     /region_name="Required for inhibitor TIMP2 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P33436.2)"
     Region          468..662
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Site            order(478,480,523,525,571,573,620,622)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     Site            575
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33436.2)"
     Site            644
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33436.2)"
     CDS             1..662
                     /gene="Mmp2"
                     /coded_by="NM_031054.2:292..2280"
                     /db_xref="GeneID:81686"
                     /db_xref="RGD:621316"
ORIGIN      
        1 mearlvwgvl vgplrvlcvl ccllghaiaa pspiikfpgd vspktdkela vqylntfygc
       61 pkescnlfvl kdtlkkmqkf fglpqtgdld qntietmrkp rcgnpdvany nffprkpkwd
      121 knqityriig ytpdldpetv ddafaralkv wsdvtplrfs rihdgeadim infgrwehgd
      181 gypfdgkdgl lahafapgtg vggdshfddd elwtlgegqv vrvkygnadg eyckfpflfn
      241 greyssctdt grsdgflwcs ttynfekdgk ygfcphealf tmggngdgqp ckfpfrfqgt
      301 synscttegr tdgyrwcgtt edydrdkkyg fcpetamstv ggnsegapcv fpftflgnky
      361 esctsagrsd gkvwcatttn ydddrkwgfc pdqgyslflv aahefghamg lehsqdpgal
      421 mapiytytkn frlsnddikg iqelygpspd adtdtgtgpt ptlgpvtpei ckqdivfdgi
      481 aqirgeifff kdrfiwrtvt prdkptgpll vatfwpelpe kidavyeapq eekavffagn
      541 eywvysastl ergypkplts lglppdvqqv daafnwsknk ktyifsgdkf wrynevkkkm
      601 dpgfpkliad swnaipdnld avvdlqgggh syffkgayyl klenqslksv kfgsiksdwl
      661 gc
//
LOCUS       NP_001100305             326 aa            linear   ROD 16-MAR-2025
DEFINITION  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001100305 XP_001055775 XP_217191
VERSION     NP_001100305.1
DBSOURCE    REFSEQ: accession NM_001106835.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cho,B., Choi,S.Y., Park,O.H., Sun,W. and Geum,D.
  TITLE     Differential expression of BNIP family members of BH3-only proteins
            during the development and after axotomy in the rat
  JOURNAL   Mol Cells 33 (6), 605-610 (2012)
   PUBMED   22639046
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Cuadrado,A. and Nebreda,A.R.
  TITLE     Mechanisms and functions of p38 MAPK signalling
  JOURNAL   Biochem J 429 (3), 403-417 (2010)
   PUBMED   20626350
  REMARK    Review article
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Lu,M. and Krauss,R.S.
  TITLE     N-cadherin ligation, but not Sonic hedgehog binding, initiates
            Cdo-dependent p38alpha/beta MAPK signaling in skeletal myoblasts
  JOURNAL   Proc Natl Acad Sci U S A 107 (9), 4212-4217 (2010)
   PUBMED   20160094
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Oh,J.E., Bae,G.U., Yang,Y.J., Yi,M.J., Lee,H.J., Kim,B.G.,
            Krauss,R.S. and Kang,J.S.
  TITLE     Cdo promotes neuronal differentiation via activation of the p38
            mitogen-activated protein kinase pathway
  JOURNAL   FASEB J 23 (7), 2088-2099 (2009)
   PUBMED   19244314
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Sonn,S., Jeong,Y. and Rhee,K.
  TITLE     Nip2/centrobin may be a substrate of Nek2 that is required for
            proper spindle assembly during mitosis in early mouse embryos
  JOURNAL   Mol Reprod Dev 76 (6), 587-592 (2009)
   PUBMED   19117032
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Boyd,J.M., Malstrom,S., Subramanian,T., Venkatesh,L.K.,
            Schaeper,U., Elangovan,B., D'Sa-Eipper,C. and Chinnadurai,G.
  TITLE     Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
            of cellular proteins
  JOURNAL   Cell 79 (2), 341-351 (1994)
   PUBMED   7954800
  REMARK    Erratum:[Cell. 1994 Dec 16;79(6):1121. PMID: 8001138]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474041.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217191.4, XP_001055775.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..326
                     /product="BCL2/adenovirus E1B 19 kDa protein-interacting
                     protein 2 isoform 3"
                     /note="Bcl-2 and E1B 19 kDa interacting protein;
                     BCL2/adenovirus E1B 19kDa-interacting protein 1, NIP2;
                     BCL2/adenovirus E1B interacting protein 2; BCL2/adenovirus
                     E1B 19 kDa protein-interacting protein 2"
                     /calculated_mol_wt=37308
     Region          49..163
                     /region_name="BNIP2"
                     /note="Bcl2-/adenovirus E1B nineteen kDa-interacting
                     protein 2; pfam12496"
                     /db_xref="CDD:463609"
     Region          147..295
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     CDS             1..326
                     /gene="Bnip2"
                     /coded_by="NM_001106835.1:249..1229"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300811"
                     /db_xref="RGD:1308944"
ORIGIN      
        1 megvelkeew qdedfpiplp eddsieadil dvtdpdrqpg slevngnkvr kklvapdisl
       61 tldpgedslw sddldeggev dldgldtpse nsdefewedd lpkpkttevi rkgsiteyaa
      121 teekedgrrw rmfrigeqdh rvdmkaiepy kkvishggyy gdglnaivvf avcfmpesgq
      181 pnyrylmdnl fkyvigtlel lvaenymiiy lngattrrkm pslgwlrrcy qqidrrlrkn
      241 lksliivhps wfirtllavt rpfisskfsq kiryvfnlae laelvpmeyv gipecikqcv
      301 sllcfsswiw arglllcltv lkntgl
//
LOCUS       NP_001423397            1079 aa            linear   ROD 16-MAR-2025
DEFINITION  atos homolog protein A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423397 XP_038937071
VERSION     NP_001423397.1
DBSOURCE    REFSEQ: accession NM_001436468.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937071.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.30012.1,
                                           SRR26643287.20620.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1079
                     /product="atos homolog protein A isoform 1"
                     /note="family with sequence similarity 214, member A; atos
                     homolog protein A"
                     /calculated_mol_wt=119958
     Region          882..939
                     /region_name="DUF4210"
                     /note="Domain of unknown function (DUF4210); pfam13915"
                     /db_xref="CDD:404751"
     Region          1021..1078
                     /region_name="Chromosome_seg"
                     /note="Chromosome segregation during meiosis; pfam13889"
                     /db_xref="CDD:464021"
     CDS             1..1079
                     /gene="Atosa"
                     /gene_synonym="Fam214a; RGD1310552"
                     /coded_by="NM_001436468.1:454..3693"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300836"
                     /db_xref="RGD:1310552"
ORIGIN      
        1 mkpdrdalde yfeydaeefl vslalliteg rtpecsvkgr aesfhcppaq srfpgaarhe
       61 csdklaqcrq arrtrsevtl lwknnlpimv evmllpdccy sdegpstegt dlndpaikqd
      121 alllerwile pvprqngdrf ieekalllav rsfvffsqls awlsvshgai prnilyrisa
      181 advdlqwsfs qtptehvfpv pnvshnvalk vsvqslprqa hypvltcsih tniglyekri
      241 qeqelracqh rgpgeveyrc psssqslcsk htwtmapvsa lhvrsgmppe ytaairnvrl
      301 cpgtgsksdn gtpqasvlgf sgtgevrsqe asvrtfksls vidssvsscq ssrqpvgepn
      361 plidsliqdr qeviariaqh lihcdpsssr mselpfntpe stslspklhp vsqesgysrr
      421 ckeafsvsfg spefgspgds kegkvkekle trqgetcash spyprqpage anpligslll
      481 erqdviaria qhlehidpta hiprpafskh dsnsipskvf rssfhdktml kkdrenvsvs
      541 athtevsllg drgdgkspkp skcfrsfkns pqekslkpee saqhqnhpdd ithtarqell
      601 nkaaglltss nsslcnessl aligrlests cklqlrkqem shetekqclh cnsidkqict
      661 nkctekikde nspgslshlq cdesrgidpk ikvtmlempd ylnkyktncs nkdskrsktc
      721 eqniqlgten ylsedtegsk stisdqlkte qeenkdsvag kppsvkhcls tserlknadm
      781 ldfssqrttl khssvwrkhd fhsldgtstr afhpqtglpl lsspvpqrkt qsgcfdldts
      841 llhlrslssk ssrpclniea dpgvhekpfl sssappitsl sllgnfeesv lnyrldplgi
      901 vdgftaevga sgtfcpthlt lpvevsfysv sddnapspym gvitleslgk rgyrvppsgt
      961 iqvtlfnpnk tvvkmfvvvy dlrsmpanhq tflrqrtfsv pvkqemkrsi nkenvqhtaq
     1021 llrylihlrf qssksgkiyl hrdvrllfsr ksmevdsgaa yelksytesp tnpqfsprc
//
LOCUS       NP_001423411             777 aa            linear   ROD 16-MAR-2025
DEFINITION  transcriptional regulator QRICH1 [Rattus norvegicus].
ACCESSION   NP_001423411 XP_006243809
VERSION     NP_001423411.1
DBSOURCE    REFSEQ: accession NM_001436482.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243809.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1540116.1,
                                           SRR26360181.1765523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..777
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86384
     Region          <6..48
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          600..760
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..777
                     /gene="Qrich1"
                     /gene_synonym="RGD1311095"
                     /coded_by="NM_001436482.1:160..2493"
                     /db_xref="GeneID:301004"
                     /db_xref="RGD:1311095"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqsat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqql
      121 spqftvhqpa eqpiqvqvqi qgqapqsaap siqtpslqsp spsqlqaaqi qvqhvqaaqq
      181 iqaaeipeeh iphqqiqaql vagqslaggq qiqiqtvgal spppsqqgsp regerrvgta
      241 svlqpvkkrk vdmpitvsya isgqpvatvl aipqgqqqsy vslrpdlltv dsahlysatg
      301 titsptgetw tipvysaqpr gdpqqqsith iaipqeayna vhvsgsptal aavkleddke
      361 kmvgttsvvk nsheevvqtl anslfpaqfm ngnihipvav qavagtyqnt aqtvhiwdpq
      421 qqpqqqtaqe qtppqpqqqq qlqvtcsaqt vqvaevepqs qpqpspelll pnslkpeegl
      481 evwknwaqtk naelekdaqn rlapigrrql lrfqedliss avaelnyglc lmtrearnge
      541 gepydpdvly yiflciqkyl fengrvddif sdlyyvrfte wlhevlkdvq prvtplgyvl
      601 pshvteemlw eckqlgahsp stllttlmff ntkyfllktv dqhmklafsk vlrqtkksps
      661 npkdkstsir ylkalgihqt gqkvtddmya eqtenpenpl rcpiklydfy lfkcpqsvkg
      721 rndtfyltpe pvvapnspiw ysvqpisreq mgqmltrilv ireiqeaiav anattmh
//
LOCUS       NP_001423440             322 aa            linear   ROD 16-MAR-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP16 [Rattus norvegicus].
ACCESSION   NP_001423440 XP_038937432
VERSION     NP_001423440.1
DBSOURCE    REFSEQ: accession NM_001436511.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Yang,D., Wang,Q., Wei,G., Wu,J., Zhu,Y.C., Zhu,Q., Ni,T., Liu,X.
            and Zhu,Y.Z.
  TITLE     Smyd3-PARP16 axis accelerates unfolded protein response and
            vascular aging
  JOURNAL   Aging (Albany NY) 12 (21), 21423-21445 (2020)
   PUBMED   33144524
  REMARK    GeneRIF: Smyd3-PARP16 axis accelerates unfolded protein response
            and vascular aging.
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Vyas,S., Matic,I., Uchima,L., Rood,J., Zaja,R., Hay,R.T., Ahel,I.
            and Chang,P.
  TITLE     Family-wide analysis of poly(ADP-ribose) polymerase activity
  JOURNAL   Nat Commun 5, 4426 (2014)
   PUBMED   25043379
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Jwa,M. and Chang,P.
  TITLE     PARP16 is a tail-anchored endoplasmic reticulum protein required
            for the PERK- and IRE1alpha-mediated unfolded protein response
  JOURNAL   Nat Cell Biol 14 (11), 1223-1230 (2012)
   PUBMED   23103912
  REMARK    Erratum:[Nat Cell Biol. 2013 Jan;15(1):123]
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Di Paola,S., Micaroni,M., Di Tullio,G., Buccione,R. and Di
            Girolamo,M.
  TITLE     PARP16/ARTD15 is a novel endoplasmic-reticulum-associated
            mono-ADP-ribosyltransferase that interacts with, and modifies
            karyopherin-ss1
  JOURNAL   PLoS One 7 (6), e37352 (2012)
   PUBMED   22701565
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937432.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.3239421.1,
                                           SRR26643289.23250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..322
                     /product="protein mono-ADP-ribosyltransferase PARP16"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 16; PARP-16;
                     ADP-ribosyltransferase diphtheria toxin-like 15; mono
                     [ADP-ribose] polymerase PARP16"
                     /calculated_mol_wt=36581
     Region          15..90
                     /region_name="ARTD15_N"
                     /note="ARTD15 N-terminal domain; pfam18084"
                     /db_xref="CDD:465641"
     Region          102..273
                     /region_name="PARP"
                     /note="Poly(ADP-ribose) polymerase catalytic domain;
                     pfam00644"
                     /db_xref="CDD:395519"
     Site            193
                     /site_type="other"
                     /note="Nicotinamide-stacking aromate.
                     /evidence=ECO:0000250|UniProtKB:Q8N5Y8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Q4.1)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Q4.1)"
     CDS             1..322
                     /gene="Parp16"
                     /gene_synonym="ARTD15; LRRGT00109; RGD1306243"
                     /coded_by="NM_001436511.1:282..1250"
                     /db_xref="GeneID:315760"
                     /db_xref="RGD:1306243"
ORIGIN      
        1 mqlsnraaar esvsrdvlaa dlrcslfasa lqsykrdsvl rpfpasyarh dckdfealla
       61 dtgrlpnlke llqssrdtdk qtwdlvswil sskiltihsa ekaefekiqq ltgaphtpvp
      121 ipdflfeiey fdpanarfye tkggrdliya fhgsrlenfh siihnglhch lnktslfgeg
      181 tyltsdlsla liysphgrgw qhsllgqtls cvavcevidh pdvkcqtkkk dskeidrsra
      241 rikhseggdv ppkyfvvtnn qllrvkyllv ysqkqpkras sqlswlcshw fmvamslyll
      301 lllivsvtns safqhfwnrl kr
//
LOCUS       NP_001423393             678 aa            linear   ROD 16-MAR-2025
DEFINITION  transcription initiation factor TFIID subunit 6 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423393 XP_063127214
VERSION     NP_001423393.1
DBSOURCE    REFSEQ: accession NM_001436464.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Louder,R.K., He,Y., Lopez-Blanco,J.R., Fang,J., Chacon,P. and
            Nogales,E.
  TITLE     Structure of promoter-bound TFIID and model of human pre-initiation
            complex assembly
  JOURNAL   Nature 531 (7596), 604-609 (2016)
   PUBMED   27007846
  REMARK    Erratum:[Nature. 2016 Aug 4;536(7614):112. doi:
            10.1038/nature17984. PMID: 27096372]
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Malkowska,M., Kokoszynska,K., Rychlewski,L. and Wyrwicz,L.
  TITLE     Structural bioinformatics of the general transcription factor TFIID
  JOURNAL   Biochimie 95 (4), 680-691 (2013)
   PUBMED   23146842
  REMARK    Review article
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Kamileri,I., Karakasilioti,I., Sideri,A., Kosteas,T., Tatarakis,A.,
            Talianidis,I. and Garinis,G.A.
  TITLE     Defective transcription initiation causes postnatal growth failure
            in a mouse model of nucleotide excision repair (NER) progeria
  JOURNAL   Proc Natl Acad Sci U S A 109 (8), 2995-3000 (2012)
   PUBMED   22323595
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Wilhelm,E., Kornete,M., Targat,B., Vigneault-Edwards,J.,
            Frontini,M., Tora,L., Benecke,A. and Bell,B.
  TITLE     TAF6delta orchestrates an apoptotic transcriptome profile and
            interacts functionally with p53
  JOURNAL   BMC Mol Biol 11, 10 (2010)
   PUBMED   20096117
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Tatarakis,A., Margaritis,T., Martinez-Jimenez,C.P., Kouskouti,A.,
            Mohan,W.S. 2nd, Haroniti,A., Kafetzopoulos,D., Tora,L. and
            Talianidis,I.
  TITLE     Dominant and redundant functions of TFIID involved in the
            regulation of hepatic genes
  JOURNAL   Mol Cell 31 (4), 531-543 (2008)
   PUBMED   18722179
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Pointud,J.C., Mengus,G., Brancorsini,S., Monaco,L., Parvinen,M.,
            Sassone-Corsi,P. and Davidson,I.
  TITLE     The intracellular localisation of TAF7L, a paralogue of
            transcription factor TFIID subunit TAF7, is developmentally
            regulated during male germ-cell differentiation
  JOURNAL   J Cell Sci 116 (Pt 9), 1847-1858 (2003)
   PUBMED   12665565
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Bell,B., Scheer,E. and Tora,L.
  TITLE     Identification of hTAF(II)80 delta links apoptotic signaling
            pathways to transcription factor TFIID function
  JOURNAL   Mol Cell 8 (3), 591-600 (2001)
   PUBMED   11583621
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Kida,S., Umehara,T. and Horikoshi,M.
  TITLE     Three distinct regions in a rat TFIID subunit containing histone H4
            homology
  JOURNAL   Gene 161 (2), 303-304 (1995)
   PUBMED   7665101
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Weinzierl,R.O., Ruppert,S., Dynlacht,B.D., Tanese,N. and Tjian,R.
  TITLE     Cloning and expression of Drosophila TAFII60 and human TAFII70
            reveal conserved interactions with other subunits of TFIID
  JOURNAL   EMBO J 12 (13), 5303-5309 (1993)
   PUBMED   8262073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063127214.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1672889.1,
                                           SRR26360176.2093579.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..678
                     /product="transcription initiation factor TFIID subunit 6
                     isoform 1"
                     /note="TAF6 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 80 kDa; transcription initiation
                     factor TFIID subunit 6; TFIID subunit p80; TAFII80;
                     TAFII-70; TAFII-80; TAF(II)70; transcription initiation
                     factor TFIID 70 kDa subunit; transcription initiation
                     factor TFIID 80 kDa subunit"
                     /calculated_mol_wt=72583
     Region          9..408
                     /region_name="TAF6"
                     /note="Transcription initiation factor TFIID, subunit TAF6
                     (also component of histone acetyltransferase SAGA)
                     [Transcription]; COG5095"
                     /db_xref="CDD:227426"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          142..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63801.1)"
     Region          214..430
                     /region_name="TAF6C"
                     /note="C-terminal domain of TATA Binding Protein (TBP)
                     Associated Factor 6 (TAF6); cd08050"
                     /db_xref="CDD:381749"
     Site            order(218..220,222..223,226,237..238,241,245,248..249,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381749"
     Region          218..249
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          256..291
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          301..344
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          351..383
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          385..429
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:381749"
     Region          524..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63801.1)"
     Site            524
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Region          611..678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63801.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62311; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49848; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63801.1)"
     CDS             1..678
                     /gene="Taf6"
                     /gene_synonym="TAF(II)80; TAFII70"
                     /coded_by="NM_001436464.1:108..2144"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288533"
                     /db_xref="RGD:1311608"
ORIGIN      
        1 maeekklkls ntvlpsesmk vvaesmgiaq iqeetcqllt devsyrikei aqdalkfmhm
       61 gkrqklttsd idyalklknv eplygfhaqe fipfrfasgg grelyfyeek evdlsdiint
      121 plprvpldvc lkahwlsieg cqpaipenpp papkeqqkae ateplksakp gqeedgplkg
      181 kgqgaaaadg kgkekkappl legapfrlkp rsihelsveq qlyykeitea cvgsceakra
      241 ealqsiatdp glyqmlprfs tfisegvrvn vvqnnlalli ylmrmvkalm dnptlyleky
      301 vhelipavmt civsrqlclr pdvdnhwalr dfaarlvaqi ckhfstttnn iqsritktft
      361 kswvdektpw ttrygsiagl aelghdvikt lilprlqqeg erirsvldgp vlsnidriga
      421 dhvqslllkh capvlaklrp ppdnqdayrg efgslgpllc shvvkaraqa alqaqqvnrt
      481 tltitqprpt ltlsqapqpg prtpgllkvp gsialpvqtl vsaraaappq psppptkfiv
      541 msssssasst qqvlslstsa pgsgstttsp vtttvpsvqp ivklvstatt appstapagp
      601 gsvqkyivvs lpptgegkgg ppshpspvpp sssspsplgg salcggkqet gdspppapgt
      661 pkangsqptg psspqpal
//
LOCUS       NP_001423405             362 aa            linear   ROD 16-MAR-2025
DEFINITION  mortality factor 4-like protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423405 XP_008764667
VERSION     NP_001423405.1
DBSOURCE    REFSEQ: accession NM_001436476.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Hayakawa,T., Zhang,F., Hayakawa,N., Ohtani,Y., Shinmyozu,K.,
            Nakayama,J. and Andreassen,P.R.
  TITLE     MRG15 binds directly to PALB2 and stimulates homology-directed
            repair of chromosomal breaks
  JOURNAL   J Cell Sci 123 (Pt 7), 1124-1130 (2010)
   PUBMED   20332121
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Tominaga,K., Kirtane,B., Jackson,J.G., Ikeno,Y., Ikeda,T.,
            Hawks,C., Smith,J.R., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     MRG15 regulates embryonic development and cell proliferation
  JOURNAL   Mol Cell Biol 25 (8), 2924-2937 (2005)
   PUBMED   15798182
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Tominaga,K., Magee,D.M., Matzuk,M.M. and Pereira-Smith,O.M.
  TITLE     PAM14, a novel MRG- and Rb-associated protein, is not required for
            development and T-cell function in mice
  JOURNAL   Mol Cell Biol 24 (19), 8366-8373 (2004)
   PUBMED   15367658
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Doyon,Y., Selleck,W., Lane,W.S., Tan,S. and Cote,J.
  TITLE     Structural and functional conservation of the NuA4 histone
            acetyltransferase complex from yeast to humans
  JOURNAL   Mol Cell Biol 24 (5), 1884-1896 (2004)
   PUBMED   14966270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_008764667.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2807042.1,
                                           SRR26360194.1688690.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..362
                     /product="mortality factor 4-like protein 1 isoform 1"
                     /note="mortality factor 4-like protein 1; MORF-related
                     gene 15 protein; transcription factor-like protein MRG15"
                     /calculated_mol_wt=41332
     Region          15..110
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(21..22,26..29,44,46..49,92,94..97,99..101,104..105)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(26,46,49,92)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(43,45..50,91..95)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(43,46,50,91,95)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          176..351
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..362
                     /gene="Morf4l1"
                     /coded_by="NM_001436476.1:142..1230"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300891"
                     /db_xref="RGD:1307938"
ORIGIN      
        1 mapkqdpkpk fqegervlcf hgpllyeakc vkvaikdkqv kyfihysgwn kksavrprrs
       61 ekslktredi valfpvpega psvhhpllts swdewvpesr vlkyvdanlq kqrelqkanq
      121 eqyaegkmrg aapgkktsgl qqknvevktk knkqktpgng dggstsetpq pprkkrarvd
      181 ptveneetfm nrvevkvkip eelkpwlvdd wdlitrqkql fylpakknvd siledyanyk
      241 ksrgntdnke yavnevvagi keyfnvmlgt qllykferpq yaeiladhpd apmsqvygap
      301 hllrlfvrig amlaytplde kslalllnyl hdflkylakn satlfsasdy evappeyhrk
      361 av
//
LOCUS       NP_001423394            1085 aa            linear   ROD 16-MAR-2025
DEFINITION  IQ domain-containing protein H isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423394 XP_008764459
VERSION     NP_001423394.1
DBSOURCE    REFSEQ: accession NM_001436465.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_008764459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.45840.1,
                                           SRR26360181.1283398.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1085
                     /product="IQ domain-containing protein H isoform 1"
                     /note="IQ domain-containing protein H"
                     /calculated_mol_wt=123714
     Region          420..447
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1085
                     /gene="Iqch"
                     /gene_synonym="RGD1310670"
                     /coded_by="NM_001436465.1:66..3323"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300776"
                     /db_xref="RGD:1310670"
ORIGIN      
        1 maqaqelndp igsiliqvhg dlhqlkekli qfsaeetrdp ldiqnletai qrtetglkih
       61 ierylgivnq evimtpvksl dspinskwai ptvidqksfi fpmapdklwg lqkhrgslpr
      121 gftrakpkve lnkkimqdpe nmhhraavnv sygislprik qrkahdkvrr vrkgstisnl
      181 tvlpsshrtd phfipipvlq kdaskgilsm ierglippaa ritfqnppik pqalplhsfd
      241 ehrkvsitas fpiahkprla sekveesqqk qkakvlthls teehslpvtg kdkrsrgqps
      301 rkstrittps rirrspwdyi lpvyngsvdr aapdfiafkt rykliwgsif sfleqiekfl
      361 kdyaiseakv rgkslvsllp efelnnkltk tdvlavlenp lhiqmllnlp gqrfkgrdgr
      421 teaavkiqat wksykartsf isyrqkkwas gvialawllh chktrlkriv eesrqrhldn
      481 frirakhlaa nwsrirtsrr tiihipslgy sqsvrkhisd ldieqnrqlg rlcdildvnv
      541 nviyvcsspm ndelklyykk llslqaavks gyygdrsdlq nrfriitpea vniftkhhmc
      601 lathlmyspk aikriknliq geeayivggi lhrddlavad mlnvpilase pelvhlysgk
      661 sgskrifdna nvpmppgvyd iytyqqlieq lsqlvtdnlg irrwvfkmnm efggngtafc
      721 dipshlqcyk wvvkesnrfg pedwkkkwaq esalmkisee lagvlaqhvq lvnekqfptw
      781 rkflhmfltq ggiieayppa dsitnltvdm liepdgevrv lsmgdqfhad gpfissgttm
      841 pqtsvdpqvl nslclrigni ckekdvvgyf sidlvtfidp stleqqvwtt glnlsysdql
      901 amtqltlylt ngylncslst levprfkeda erekkrlsiq aelapetsry avmstqlkhd
      961 nlslifyyvf lqmckahgig ydledrqgtv filyeslkry klgmitigvd lqgalmtfar
     1021 nlfiihqeis apdmqgetnf kttiddieti lgvteenkmi fagekrrkee eeslyepvei
     1081 ytktv
//
LOCUS       NP_001100342             356 aa            linear   ROD 16-MAR-2025
DEFINITION  C-C chemokine receptor 1-like protein 1 [Rattus norvegicus].
ACCESSION   NP_001100342 XP_001078798 XP_038937250 XP_236742
VERSION     NP_001100342.1
DBSOURCE    REFSEQ: accession NM_001106872.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Mar 13, 2025 this sequence version replaced
            XP_038937250.1, XP_001078798.1, XP_236742.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680413,
                              SAMN06680416 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..356
                     /product="C-C chemokine receptor 1-like protein 1"
                     /calculated_mol_wt=40626
     Region          36..313
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          38..62
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320311"
     Region          71..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320311"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320311"
     Region          153..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320311"
     Region          198..221
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320311"
     Region          239..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320311"
     Region          281..306
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320311"
     CDS             1..356
                     /gene="Ccr1l1"
                     /coded_by="NM_001106872.2:312..1382"
                     /db_xref="GeneID:301088"
                     /db_xref="RGD:1308007"
ORIGIN      
        1 mespavtess yntvamndff sgfvcfsinv rafgitvltp lyslvfvigv ignvlvvlvl
       61 iqrkrlrnmt siylfnlavs dlvflftlpf wvdyivkgdw vfgnamckfl agfyylglys
      121 dmffitllti drylavvhav falrartvtf giissiitwv latlvsipcl yffktqleft
      181 yqtcravlpk ksliqflrfq altmnilgli lpllamiicy triinvlhrr pnkkkakvmr
      241 lifvitllff llltpyylaa fvsafedvlf tpgcvrsqqv dlalmiteal aythccvnpv
      301 iyvfvgerfr kylrqlfwrr tavslpkwlp fhsvdrvqrs sstspstgei evsadl
//
LOCUS       NP_001423433            1143 aa            linear   ROD 16-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 28 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423433 XP_006243068
VERSION     NP_001423433.1
DBSOURCE    REFSEQ: accession NM_001436504.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Hao,X., Ma,C., Chen,S., Dang,J., Cheng,X. and Zhu,D.
  TITLE     Reverse the down regulation of miR-92b-3p by hypoxia can suppress
            the proliferation of pulmonary artery smooth muscle cells by
            targeting USP28
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3064-3077 (2018)
   PUBMED   30149918
  REMARK    GeneRIF: miR-92b-3p reverse the proliferaton of pulmonary artery
            smooth muscle cells under hypoxia condition. miR-92b-3p regulate
            the protein level of USP28.
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Bassermann,F., Frescas,D., Guardavaccaro,D., Busino,L.,
            Peschiaroli,A. and Pagano,M.
  TITLE     The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
            checkpoint
  JOURNAL   Cell 134 (2), 256-267 (2008)
   PUBMED   18662541
REFERENCE   4  (residues 1 to 1143)
  AUTHORS   Popov,N., Herold,S., Llamazares,M., Schulein,C. and Eilers,M.
  TITLE     Fbw7 and Usp28 regulate myc protein stability in response to DNA
            damage
  JOURNAL   Cell Cycle 6 (19), 2327-2331 (2007)
   PUBMED   17873522
REFERENCE   5  (residues 1 to 1143)
  AUTHORS   Popov,N., Wanzel,M., Madiredjo,M., Zhang,D., Beijersbergen,R.,
            Bernards,R., Moll,R., Elledge,S.J. and Eilers,M.
  TITLE     The ubiquitin-specific protease USP28 is required for MYC stability
  JOURNAL   Nat Cell Biol 9 (7), 765-774 (2007)
   PUBMED   17558397
REFERENCE   6  (residues 1 to 1143)
  AUTHORS   Zhang,D., Zaugg,K., Mak,T.W. and Elledge,S.J.
  TITLE     A role for the deubiquitinating enzyme USP28 in control of the
            DNA-damage response
  JOURNAL   Cell 126 (3), 529-542 (2006)
   PUBMED   16901786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006243068.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.31580.1,
                                           SRR26643296.21683.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..1143
                     /product="ubiquitin carboxyl-terminal hydrolase 28 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thioesterase 28; deubiquitinating enzyme
                     28; ubiquitin-specific-processing protease 28; ubiquitin
                     thiolesterase 28; ubiquitin specific protease 28;
                     ubiquitin carboxyl-terminal hydrolase 28"
                     /calculated_mol_wt=129061
     Region          23..64
                     /region_name="UBA_UBP28"
                     /note="UBA domain found in ubiquitin carboxyl-terminal
                     hydrolase 28 (UBP28) and similar proteins; cd14355"
                     /db_xref="CDD:270540"
     Region          163..654
                     /region_name="Peptidase_C19I"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02665"
                     /db_xref="CDD:239130"
     Region          163..>271
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Site            order(166,171,606,624)
                     /site_type="active"
                     /db_xref="CDD:239130"
     Region          864..1143
                     /region_name="USP28_C"
                     /note="carboxyl-terminal domain of ubiquitin-specific
                     protease 28 (USP28); cd20487"
                     /db_xref="CDD:380452"
     CDS             1..1143
                     /gene="Usp28"
                     /coded_by="NM_001436504.1:105..3536"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315639"
                     /db_xref="RGD:1311555"
ORIGIN      
        1 mtaelqqdda agaadghgss cqmllnqlre itgiqdpsfl healkasngd itqavslltd
       61 qrvkepshdt aatepsevee satskdllak vidlthdnkd dlqaaialsl lespniqtds
      121 rdlnrihean saetkrskrk rcevwgenhn pnnwrrvdgw pvglknvgnt cwfsaviqsl
      181 fqlpefrrlv lsyslpqnil encrshtekr nimfmqelqy lfalllgsnr kfvdpsaald
      241 llkgafrsse eqqqdvseft hklldwleda fqlavnvnsn prtksenpmv qlfygtflte
      301 gvregkpfcn netfgqyplq vngyhnldec legamvegdi allpsdrsvk ygqerwftkl
      361 ppvltfelsr fefnqslgqp ekihnklefp qviymdrymy kskelirskr esirklkeei
      421 qvlqqklery vkygsgpsrf plpdmlkyvi efastkpase sclsgsvehm tlplpsvhcp
      481 isdltakess spkscsqnae gsfsspedal pnsevmngpf tsphsslemp apppaprtvt
      541 deemnfvktc lqrwrseieq diqdlkncis sttqaieqmy cdpllrqvpy rlhavlvheg
      601 qasaghyway iynqprqiwl kyndisvtes sweelerdsy gglrnvsayc lmyindklph
      661 csaeaahges dqtaeveals velrqyiqed nwrfeqevee weeeqsckip qmesspnsss
      721 qdfstsqess aasshgvrcl ssehaviake qtaqaianta hayeksgvea alsehkeaep
      781 ekpqetnlae qseqaaevkd teaaappnse vseveipsvg rilvrsdadg ydeevmlspa
      841 mqgvllaiak arqtfdrdgs eaglikafhe eysrlyqlak etptshsdpr lqhvlvyffq
      901 neapkrvver tlleqfadrn lsydersisi mkvaqaklme igpedmnmee ykrwhedysl
      961 frkvsvyllt glelfqkgky qealsylvya yqsnagllvk gprrgvkesv ialyrrkcll
     1021 elnakaaslf etnddhsvte ginvmnelii pcihliinnd iskddldaie vmrnhwcsyl
     1081 gkdiaenlql clgeflprll dpsaeiivlk epptirpnsp ydlcsrfaav mesiqgvstv
     1141 tvk
//
LOCUS       NP_001423454             447 aa            linear   ROD 16-MAR-2025
DEFINITION  cell adhesion molecule 1 isoform 6 precursor [Rattus norvegicus].
ACCESSION   NP_001423454 XP_038937650
VERSION     NP_001423454.1
DBSOURCE    REFSEQ: accession NM_001436525.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Sun,S., Liu,W. and Li,Y.
  TITLE     CADM1 enhances intestinal barrier function in a rat model of mild
            inflammatory bowel disease by inhibiting the STAT3 signaling
            pathway
  JOURNAL   J Bioenerg Biomembr 52 (5), 343-354 (2020)
   PUBMED   32929607
  REMARK    GeneRIF: CADM1 enhances intestinal barrier function in a rat model
            of mild inflammatory bowel disease by inhibiting the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Cao,W., Shi,P. and Ge,J.J.
  TITLE     miR-21 enhances cardiac fibrotic remodeling and fibroblast
            proliferation via CADM1/STAT3 pathway
  JOURNAL   BMC Cardiovasc Disord 17 (1), 88 (2017)
   PUBMED   28335740
  REMARK    GeneRIF: miR-21 overexpression promotes cardiac fibrosis via STAT3
            signaling pathway by decrease CADM1 expression, indicating miR-21
            as an important signaling molecule for cardiac fibrotic remodeling
            and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    GeneRIF: proteins. Our results highlight a previously unexplored
            role for MPP2 at postsynaptic sites as a scaffold that links
            SynCAM1 cell adhesion molecules to core proteins of the
            postsynaptic density.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Zhang,C., Caldwell,T.A., Mirbolooki,M.R., Duong,D., Park,E.J.,
            Chi,N.W. and Chessler,S.D.
  TITLE     Extracellular CADM1 interactions influence insulin secretion by rat
            and human islet beta-cells and promote clustering of syntaxin-1
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E874-E885 (2016)
   PUBMED   27072493
  REMARK    GeneRIF: Our results suggest that, as in the CNS, CADM1
            interactions drive exocytic site assembly and promote actin network
            formation. These results support the broader hypothesis that the
            effects of cell-cell contact on beta-cell maturation and function
            are mediated by the same extracellular protein interactions that
            drive the formation of the presynaptic exocytic machinery. These
            interactions may be therapeutic targets for re...
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Perez de Arce,K., Schrod,N., Metzbower,S.W.R., Allgeyer,E.,
            Kong,G.K., Tang,A.H., Krupp,A.J., Stein,V., Liu,X., Bewersdorf,J.,
            Blanpied,T.A., Lucic,V. and Biederer,T.
  TITLE     Topographic Mapping of the Synaptic Cleft into Adhesive Nanodomains
  JOURNAL   Neuron 88 (6), 1165-1172 (2015)
   PUBMED   26687224
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Li,J., Zhang,Z., Bidder,M., Funk,M.C., Nguyen,L., Goodfellow,P.J.
            and Rader,J.S.
  TITLE     IGSF4 promoter methylation and expression silencing in human
            cervical cancer
  JOURNAL   Gynecol Oncol 96 (1), 150-158 (2005)
   PUBMED   15589594
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Shingai,T., Ikeda,W., Kakunaga,S., Morimoto,K., Takekuni,K.,
            Itoh,S., Satoh,K., Takeuchi,M., Imai,T., Monden,M. and Takai,Y.
  TITLE     Implications of nectin-like
            molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion
            and transmembrane protein localization in epithelial cells
  JOURNAL   J Biol Chem 278 (37), 35421-35427 (2003)
   PUBMED   12826663
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Biederer,T., Sara,Y., Mozhayeva,M., Atasoy,D., Liu,X.,
            Kavalali,E.T. and Sudhof,T.C.
  TITLE     SynCAM, a synaptic adhesion molecule that drives synapse assembly
  JOURNAL   Science 297 (5586), 1525-1531 (2002)
   PUBMED   12202822
  REMARK    GeneRIF: a brain-specific, immunoglobulin domain-containing protein
            that binds to intracellular PDZ-domain proteins and functions as a
            homophilic cell adhesion molecule at the synapse (SynCAM; Synaptic
            cell adhesion molecule)
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Fukuhara,H., Kuramochi,M., Fukami,T., Kasahara,K., Furuhata,M.,
            Nobukuni,T., Maruyama,T., Isogai,K., Sekiya,T., Shuin,T.,
            Kitamura,T., Reeves,R.H. and Murakami,Y.
  TITLE     Promoter methylation of TSLC1 and tumor suppression by its gene
            product in human prostate cancer
  JOURNAL   Jpn J Cancer Res 93 (6), 605-609 (2002)
   PUBMED   12079507
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_038937650.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.267206.1,
                                           SRR26360186.173844.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..447
                     /product="cell adhesion molecule 1 isoform 6 precursor"
                     /note="nectin-like protein 2; spermatogenic immunoglobulin
                     superfamily; immunoglobulin superfamily, member 4A;
                     synaptic cell adhesion molecule; tumor suppressor in lung
                     cancer 1 homolog"
                     /calculated_mol_wt=44438
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4409
     Region          50..143
                     /region_name="IgV_1_Necl-2"
                     /note="First (N-terminal) immunoglobulin (Ig)-like domain
                     of nectin-like molecule 2; member of the V-set of Ig
                     superfamily (IgSF) domains; cd05881"
                     /db_xref="CDD:409465"
     Region          50..68
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409465"
     Region          50..52
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409465"
     Region          53..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409465"
     Region          61..69
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409465"
     Region          69..74
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409465"
     Site            order(75,78,83..84,86,92,94,130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409465"
     Region          75..82
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          75..81
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409465"
     Region          83..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409465"
     Region          85..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          91..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409465"
     Region          95..130
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          99..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409465"
     Region          109..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409465"
     Region          122..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409465"
     Region          131..134
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409465"
     Region          134..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409465"
     Region          136..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409465"
     Region          144..242
                     /region_name="IgI_2_Necl-2"
                     /note="Second immunoglobulin (Ig)-like domain of
                     nectin-like molecule 2 (Necl-2); member of the I-set of Ig
                     superfamily domains; cd05883"
                     /db_xref="CDD:409466"
     Region          144..147
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409466"
     Region          150..154
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409466"
     Region          163..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409466"
     Region          176..185
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409466"
     Region          186..189
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409466"
     Region          191..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409466"
     Region          201..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409466"
     Region          219..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409466"
     Region          234..241
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409466"
     Region          255..333
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          400..418
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..447
                     /gene="Cadm1"
                     /gene_synonym="Igsf4; Igsf4a; Necl-2; sgigsf; SynCAM;
                     TSLC-1; TSLC1"
                     /coded_by="NM_001436525.1:22..1365"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:363058"
                     /db_xref="RGD:1310999"
ORIGIN      
        1 maspvlpsgs qcaaaaavaa aaappglrlr llllllsaaa liptgdgqnl ftkdvtvieg
       61 evatiscqvn ksddsviqll npnrqtiyfr dfrplkdsrf qllnfsssel kvsltnvsis
      121 degryfcqly tdppqesytt itvlvpprnl midiqkdtav egeeievnct amaskpatti
      181 rwfkgnkelk gkseveewsd mytvtsqlml kvhkeddgvp vicqvehpav tgnlqtqryl
      241 evqykpqvqi qmtyplqglt regdafeltc eatgkpqpvm vtwvrvddem pqhavlsgpn
      301 lfinnlnktd ngtyrceasn tvgkahsdym lyvydpptti pppttttttt ttttttttil
      361 tiitdsrage egaigavdha viggvvavvv famlclliil gryfarhkgt yftheakgad
      421 daadadtaii naeggqnnse ekkeyfi
//
LOCUS       NP_001423419            1437 aa            linear   ROD 16-MAR-2025
DEFINITION  protein turtle homolog B isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423419 XP_235959
VERSION     NP_001423419.1
DBSOURCE    REFSEQ: accession NM_001436490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1437)
  AUTHORS   Woo,J., Kwon,S.K., Nam,J., Choi,S., Takahashi,H., Krueger,D.,
            Park,J., Lee,Y., Bae,J.Y., Lee,D., Ko,J., Kim,H., Kim,M.H.,
            Bae,Y.C., Chang,S., Craig,A.M. and Kim,E.
  TITLE     The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM
            to promote inhibitory synapse development
  JOURNAL   J Cell Biol 201 (6), 929-944 (2013)
   PUBMED   23751499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_235959.6.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1437
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1437
                     /product="protein turtle homolog B isoform 1 precursor"
                     /note="protein turtle homolog B"
                     /calculated_mol_wt=155069
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
                     /calculated_mol_wt=2165
     mat_peptide     21..1328
                     /product="Protein turtle homolog B. /id=PRO_5003052708"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
                     /calculated_mol_wt=142933
     Region          41..115
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          59..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          139..225
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          157..161
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          170..174
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          191..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          205..210
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..221
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          228..307
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          336..410
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          342..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          355..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          380..384
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          394..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          407..410
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          429..505
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          438..442
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          451..455
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          471..475
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Region          485..490
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Region          <490..>731
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          498..501
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          510..601
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(510,574,589)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(590..591,593..594)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            624
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            723..743
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          758..817
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          <894..1242
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          914..1040
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Region          1107..1328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1136
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9PZ19; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     Site            1215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PZ19; propagated from
                     UniProtKB/Swiss-Prot (D3ZB51.1)"
     CDS             1..1437
                     /gene="Igsf9b"
                     /gene_synonym="RGD1564717"
                     /coded_by="NM_001436490.1:229..4542"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:315510"
                     /db_xref="RGD:1564717"
ORIGIN      
        1 miwyvatlia svistrglva qvahglreep efvtarageg vvlrcdvihp vtgqpppyvv
       61 ewfkfgvpip ifikfgyypp hvdpeyagra slhdkaslrl eqvrsedqgw yeckvlmldq
      121 qydtfhngsw vhltinappt ftetppqyie akeggsitmt ctafgnpkpi vtwlkegtll
      181 sasgkyqvsd gsltvtsvsr edrgaytcra ysiqgeavht thllvqgppf ivsppenitv
      241 nisqdalltc raeaypgnlt ytwywqdenv yfqndlklrv rilidgtlii frvkpedagk
      301 ytcvpsnslg rspsasaylt vqyparvlnm ppviyvpvgi hgyircpvda eppatvvkwn
      361 kdgrplqvek nlgwtlmedg sirieeatee algtytcvpy ntlgtmgqsa parlvlkdpp
      421 yftvlpgwey rqeagrelli pcaaagdpfp vitwrkvgkp srskhnalps gslqfralsk
      481 edhgewecva tnvvtsitas thltvigtsp hapgsvrvhv smttanvswe pgydggyeqt
      541 fsvwmkraqf gphdwlslsv plgpswllvd slepetayqf svlaqnrlgt safsevvtvn
      601 tlafpvttpe plvlvtpprc ltanrtqqgv llswlppanh sfpidryime frvgerweml
      661 ddaipgtdge ffakdlsqdt wyefrvlavm qdlisepsni agvsstdifp qpdltddgla
      721 rpvlagivat icflaaailf stlaacfvnk qrkrklkrkk dpplsithcr kslesplssg
      781 kvspesirtl rapsessddq gqpaakrmls ptrekelsly kktkraissr kysvakaeae
      841 aeattpieli srgpdgrfvm gpsemepsvk grriegfpfa eetdmypefr qsdeenedpl
      901 vptsvaalkp qltpmsssqd sylpppaysp rfqprglegp sglggrlqat gqarppaprp
      961 fqhgqyygyl sssspgevep ppfympevgs plssvmsspp lhtegpfghp tipeengena
     1021 snstlpltqt ptggrspepw grpefpfggl etpammfphq lhpcdvaesl qpkpclprgl
     1081 ppaplqvpaa ypgmlsleap kgwvgkspgr gpipappatk wqerpmqplv sqgqlrhtsq
     1141 gmgipvlpyp epaepgghgg pstfgldtrw yepqprprps prqarraeps lhqvvlqpsr
     1201 lspltqspls srtgspelaa rarprpgllq qaemseitlq ppaavsfsrk stpsstgsps
     1261 qssrsgspsy rptmgfttla tgypspppgp appapgdnld vfgqtpsprr mgeeplrpep
     1321 pttlptsgil ppapgnaavp erlealryqr ikkpkksskg sskskkrsdg sasqdqqlpn
     1381 sqvlwpdeav clrkkkrhsr pdpfarlsdl chrqlpedqt ailnsvdhdd pghatll
//
LOCUS       NP_001423455             128 aa            linear   ROD 16-MAR-2025
DEFINITION  protein ripply2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423455 XP_343445
VERSION     NP_001423455.1
DBSOURCE    REFSEQ: accession NM_001436526.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Takahashi,J., Ohbayashi,A., Oginuma,M., Saito,D., Mochizuki,A.,
            Saga,Y. and Takada,S.
  TITLE     Analysis of Ripply1/2-deficient mouse embryos reveals a mechanism
            underlying the rostro-caudal patterning within a somite
  JOURNAL   Dev Biol 342 (2), 134-145 (2010)
   PUBMED   20346937
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Chan,T., Kondow,A., Hosoya,A., Hitachi,K., Yukita,A.,
            Okabayashi,K., Nakamura,H., Ozawa,H., Kiyonari,H., Michiue,T.,
            Ito,Y. and Asashima,M.
  TITLE     Ripply2 is essential for precise somite formation during mouse
            early development
  JOURNAL   FEBS Lett 581 (14), 2691-2696 (2007)
   PUBMED   17531978
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Kawamura,A., Koshida,S., Hijikata,H., Ohbayashi,A., Kondoh,H. and
            Takada,S.
  TITLE     Groucho-associated transcriptional repressor ripply1 is required
            for proper transition from the presomitic mesoderm to somites
  JOURNAL   Dev Cell 9 (6), 735-744 (2005)
   PUBMED   16326386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_343445.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.184625.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..128
                     /product="protein ripply2 isoform 2"
                     /note="ripply2 homolog"
                     /calculated_mol_wt=14288
     Region          33..117
                     /region_name="Ripply"
                     /note="Transcription Regulator; pfam14998"
                     /db_xref="CDD:464433"
     CDS             1..128
                     /gene="Ripply2"
                     /gene_synonym="RGD1308746"
                     /coded_by="NM_001436526.1:9..395"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363111"
                     /db_xref="RGD:1308746"
ORIGIN      
        1 mdttesaesa hsparspsrs rcpppaqpgs egfwrpwvrt pgekeelaep raaevlpsgp
       61 gmieasrkll qyqhpvrlfw pkskcydyly qeaetllknf piqatisfye dsdseddveg
      121 lacenqsn
//
LOCUS       NP_001423449             616 aa            linear   ROD 16-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 44 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423449 XP_006242830
VERSION     NP_001423449.1
DBSOURCE    REFSEQ: accession NM_001436520.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006242830.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.32891.1,
                                           SRR26643285.30517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..616
                     /product="zinc finger and BTB domain-containing protein 44
                     isoform 2"
                     /note="zinc finger and BTB domain-containing protein 44;
                     BTB/POZ domain-containing protein 15; BTB (POZ) domain
                     containing 15"
                     /calculated_mol_wt=68429
     Region          15..130
                     /region_name="BTB_POZ_ZBTB44"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 44 (ZBTB44); cd18228"
                     /db_xref="CDD:349537"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCP5; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0A2; propagated from
                     UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          203..>322
                     /region_name="pgaA"
                     /note="outer membrane protein PgaA; Provisional; PRK10049"
                     /db_xref="CDD:236644"
     Region          241..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          295..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          336..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWU4.1)"
     Region          399..421
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(401,404,417,421)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(406,408,410,412..413,416..417,420,434,436,440..441,
                     444..445,448,462,464,466,468..469,472..473,476)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          413..438
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          457..476
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          489..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..616
                     /gene="Zbtb44"
                     /gene_synonym="Btbd15; RGD1308984"
                     /coded_by="NM_001436520.1:312..2162"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363035"
                     /db_xref="RGD:1308984"
ORIGIN      
        1 mgvktfthss sshsqemlgk lnmlrndghf cditirvqdr ifrahkvvla acsdffrtkl
       61 vgqtedenkn vldlhhvtvt gfiplleyay tatlsinten iidvlaaasy mqmfsvastc
      121 sefmkssilw ntpnsqpekg ldagqenssn cnftsrdgsi spvssecsav ertipvcres
      181 rrkrksyivm spespvkcst qtnspqvlns sasyaenrnq pvdsslafpw tfpfgidrri
      241 qpekakqaen trtlelpgps eagrrmadyv tcestkttlp lgteedvrvk verlsdeevh
      301 eevsqpvsas qsslsdqqtv pgsepvqedl lispqsssig svdegvtegl ptlqstsstn
      361 ahadeddrle nvqypyqlyi apstssterp spngpdrpfq cptcgvrftr iqnlkqhmli
      421 hsgikpfqcd ccgkkftray slkmhrlkhe gkrcfrcqic satftsfgey khhmrvsrhi
      481 irkpriyeck tcgamftnsg nlivhlrsln heaselanyf qssdflvpdy lsqeqeealv
      541 qydlgehtse ssssvqmpvi sqvssthnce stfplgslgg laekeedlqe qpktsahdda
      601 prddppkael ssitie
//
LOCUS       NP_001100287            1443 aa            linear   ROD 16-MAR-2025
DEFINITION  B-cell CLL/lymphoma 9-like protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100287 XP_001062700 XP_217124
VERSION     NP_001100287.1
DBSOURCE    REFSEQ: accession NM_001106817.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1443)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1443)
  AUTHORS   Deka,J., Wiedemann,N., Anderle,P., Murphy-Seiler,F., Bultinck,J.,
            Eyckerman,S., Stehle,J.C., Andre,S., Vilain,N., Zilian,O.,
            Robine,S., Delorenzi,M., Basler,K. and Aguet,M.
  TITLE     Bcl9/Bcl9l are critical for Wnt-mediated regulation of stem cell
            traits in colon epithelium and adenocarcinomas
  JOURNAL   Cancer Res 70 (16), 6619-6628 (2010)
   PUBMED   20682801
REFERENCE   3  (residues 1 to 1443)
  AUTHORS   Brack,A.S., Murphy-Seiler,F., Hanifi,J., Deka,J., Eyckerman,S.,
            Keller,C., Aguet,M. and Rando,T.A.
  TITLE     BCL9 is an essential component of canonical Wnt signaling that
            mediates the differentiation of myogenic progenitors during muscle
            regeneration
  JOURNAL   Dev Biol 335 (1), 93-105 (2009)
   PUBMED   19699733
REFERENCE   4  (residues 1 to 1443)
  AUTHORS   Fritzmann,J., Morkel,M., Besser,D., Budczies,J., Kosel,F.,
            Brembeck,F.H., Stein,U., Fichtner,I., Schlag,P.M. and Birchmeier,W.
  TITLE     A colorectal cancer expression profile that includes transforming
            growth factor beta inhibitor BAMBI predicts metastatic potential
  JOURNAL   Gastroenterology 137 (1), 165-175 (2009)
   PUBMED   19328798
REFERENCE   5  (residues 1 to 1443)
  AUTHORS   Adachi,S., Jigami,T., Yasui,T., Nakano,T., Ohwada,S., Omori,Y.,
            Sugano,S., Ohkawara,B., Shibuya,H., Nakamura,T. and Akiyama,T.
  TITLE     Role of a BCL9-related beta-catenin-binding protein, B9L, in
            tumorigenesis induced by aberrant activation of Wnt signaling
  JOURNAL   Cancer Res 64 (23), 8496-8501 (2004)
   PUBMED   15574752
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473975.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001062700.1, XP_217124.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132261, SAMD00132262
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1443
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..1443
                     /product="B-cell CLL/lymphoma 9-like protein isoform 2"
                     /note="B-cell CLL/lymphoma 9-like protein"
                     /calculated_mol_wt=151219
     Region          395..431
                     /region_name="BCL9"
                     /note="B-cell lymphoma 9 protein; pfam11502"
                     /db_xref="CDD:431912"
     Region          <837..1300
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1443
                     /gene="Bcl9l"
                     /coded_by="NM_001106817.1:796..5127"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300673"
                     /db_xref="RGD:1309096"
ORIGIN      
        1 mrilanktrl phprrreapg spplsprghc ppapakpmhp enkltnhgkt gnggaqsqhq
       61 nvnqgptcnl gskgvgagsh gakanqisps nsslknpqag vspfsslkgk vkrersvsvd
      121 sgeqreagtp sldseakeva prskrrcvle rkqpysgdew csgpdseedd kpigathncn
      181 vadpamvapq lgpgqtaqlp lsensapgpq hgpppglrpd vpggggggvp gkppsqfvyv
      241 ftthlantaa eavlqgraes ilayhqqnvp rakldqapkv pptpeplpln tpsagtpqsq
      301 ppplpppppa pgsappalpq egppedtsqd lapnsvgaas tgggtggthp ntptaatann
      361 plppggdpgs apgsallgea tptgngqrnl vgseglskeq lehrerslqt lrdierlllr
      421 sgetepflkg ppggaveggp paqapsaaqq ppsapppglk kyeeplqsmi sqtqslggpp
      481 lehevpghpq ggdmgqqmnm mmqrlgqdsl tpeqvawrkl qeeyyeekrr keeqiglhgg
      541 rplqdmvgmg gnqmqrvpgf ggmqsipmev pmnamqrpvr pgmawnedlp piggpsnfaq
      601 navpypggqg eaerfmtprv reellrhqll ekrsmgmqrp lgmagsgmgq smemermiqt
      661 hrqmdptmfp gqmtggdgla gtpmgiefgg grgllsppmg qsglrevdpp mgpgnlnmnm
      721 nvnmnmnmnl nvqmtpqqqm lmsqkmrgpg dmmgpqglsp eemarvraqn ssgmmagpqk
      781 mlmpsqfpnq gqqgfsggqg pyqampqdmg ntpdmfspdq ssvpmgavgt arlshmplpp
      841 asnppgsvhs apnrglgrrp sdltisinqm gspgmghlks ptlsqvhspl vtspsanlks
      901 pqtpsqmvpl psanppgplk spqvlsssls vrsptgspsr lkspsmavps pgwvaspkta
      961 mpspgvsqnk qpplninsss tlgnleqgal ppagprnsss appanppssl mnpslpftss
     1021 pdptpsqnpl slmmsqmsky ampsstplyh naiktiatsd dellpdrpll ppppppqgsg
     1081 pgisnnqpnq mhmnpaaaqs pmgmnlpgqq plsheppptm lpsptplgsn iplhpnaqgt
     1141 ggpsqnsmmm apggpdslnt pcgpvpsssq mmsfpprlqq phgamaatgg ggpglqqhyp
     1201 sgmalppedl pnqppgpips qqhlmgkgma grmgdayppg vlpgvasvln dpelsevirp
     1261 tptgipefdl sriipsekps stlqyfpkne nqppkaqppn lhlmnlqnmm aeqapsrppn
     1321 lpgqqgvqrg lsmsmchpgq msllgrtgvp pqqgmvphgl hqgvmsppqg lmtqqnfmlm
     1381 kqrgvggevy tqpphmlspq gslmapppqq nlmvshplrq rsvsldsqmg ylptpggman
     1441 lpf
//
LOCUS       NP_001423479             571 aa            linear   ROD 17-MAR-2025
DEFINITION  NXPE family member 1 [Rattus norvegicus].
ACCESSION   NP_001423479 XP_006243080
VERSION     NP_001423479.1
DBSOURCE    REFSEQ: accession NM_001436550.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243080.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.22782.1,
                                           SRR26643292.33556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..571
                     /product="NXPE family member 1"
                     /calculated_mol_wt=64754
     Region          <155..276
                     /region_name="Neurexophilin"
                     /note="pfam06312"
                     /db_xref="CDD:428882"
     CDS             1..571
                     /gene="Nxpe1"
                     /gene_synonym="RGD1566243"
                     /coded_by="NM_001436550.1:128..1843"
                     /db_xref="GeneID:500992"
                     /db_xref="RGD:1566243"
ORIGIN      
        1 mwimfstimr qkrlliftsf lvviwvifvi sqnsaklwtt lntstsfnpw ttstkssppe
       61 ipmnqstlpt etklreeipk mtghqedksp tetelkvrei lekldgqipp rpfahlnntt
      121 sathstatil npqdtycvgd qldvllaakd yfghrkeygg dflrarmssp alkagasgkv
      181 tdfnngtyli sftlfwegqv slsillmhps egvsalwrar nqgygriafk gtfvngtskv
      241 taecglilns sselckylyr ggeevfycvk pqhmpcealt yvctshqdvs yltakeknlf
      301 qksnigvemm khpkyivvsq cnksengrkr ceigmeiptp sgytlqgrwv saqctqrllt
      361 ssqindclkg kliyllgdst lrqwieylpk vaktlrpfdl hgtglykkhl ildaerhtlv
      421 ewkkhshpfi tvqlysvidd gyipqeidrl pgdkdtvivi tvgqhfrpfp melfvhrvin
      481 iqkaigrlfl rspdtkviik menirernld tekfgdfhgy vqylttkeif kdlhvgtida
      541 wdmtiahgtn vlhppaavig nqidvflnyi c
//
LOCUS       NP_001423471             253 aa            linear   ROD 17-MAR-2025
DEFINITION  triosephosphate isomerase 1 like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423471 XP_063122032
VERSION     NP_001423471.1
DBSOURCE    REFSEQ: accession NM_001436542.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_063122032.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.22446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..253
                     /product="triosephosphate isomerase 1 like 1 isoform 1"
                     /EC_number="5.3.1.1"
                     /calculated_mol_wt=27284
     Region          8..251
                     /region_name="PTZ00333"
                     /note="triosephosphate isomerase; Provisional"
                     /db_xref="CDD:240365"
     Site            order(16,18,100,170,176,216,235,237..238)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(16,19,50..52,54,57,69,87,90..91,102..103)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(18,100,170)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
     CDS             1..253
                     /gene="Tpi1l1"
                     /coded_by="NM_001436542.1:228..989"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500959"
                     /db_xref="RGD:1560534"
ORIGIN      
        1 mtimelnsrk ffvggnwkmn gkkkclgeli ctlnaakmpa dtevvcappt ayidfarqkl
       61 dpkiavaaqn cykvtngaft geispgmikd lgatwvvlgh serrhvfges deligqkvnh
      121 alseglgvia cigekldere agitekvvfe qtkaiadnvk dwskvvlaye pvwaigtgkt
      181 atpqqaqevh eklrgwlkcn vseevaqctr iiyggsvtga tckelasqpd vdgflvggas
      241 lkpefvdiin akq
//
LOCUS       NP_001423486             697 aa            linear   ROD 17-MAR-2025
DEFINITION  protein KRI1 homolog isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423486 XP_038938720
VERSION     NP_001423486.1
DBSOURCE    REFSEQ: accession NM_001436557.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038938720.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.10979.1,
                                           SRR26643289.22298.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..697
                     /product="protein KRI1 homolog isoform 1"
                     /calculated_mol_wt=81115
     Region          317..426
                     /region_name="Kri1"
                     /note="KRI1-like family; pfam05178"
                     /db_xref="CDD:461569"
     Region          493..581
                     /region_name="Kri1_C"
                     /note="KRI1-like family C-terminal; pfam12936"
                     /db_xref="CDD:463756"
     CDS             1..697
                     /gene="Kri1"
                     /coded_by="NM_001436557.1:17..2110"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:687183"
                     /db_xref="RGD:1588903"
ORIGIN      
        1 mpeprapatl kvnaafaary sryrereelq rlkdrygdrd dgsdsssesd ssdehvefdp
       61 qqerdfyrtl sllkkkdpri yqkdatfyqr teasssesee esaalgkqkk vqpmylkdye
      121 rkvilekegk yvdednsdge svdhrlqeta tksyieeqrq lkesfrafve dssdedsage
      181 ggsgllqkht ksgeekaqed vdylewlkgq keidsseslk elthlkeywn npeldegeqf
      241 lrdyilnkry eedeeeetee ervlgppvql avddssdege lflkkqedfe hkynfrfeep
      301 dsasvktypr siassvrrkd drrkekreet rerkkrekak kqeelkqlkn lkrkeilakl
      361 eklrqvtgne tlgleeqdle ddfdpaqhdq lmqkcfgdaf ygtveeekpq feeeegledd
      421 wnwdtwggpe qngawsqqel hcedpdfnmd adydpsqprk klreaptsgk rkrkspfaaa
      481 vgqekpmfdp gdktfeeyld eyyrldyedi iddlpcrfky rtvvpcdfgl steeilsadd
      541 kelnrwcslk ktcmyrseqe emqeqraysq kaqsvwkkrq ifkslcqeev empteatgks
      601 pskassqvql pmpsaaggkk pqaelsgake eelahtpcpe kpasqkqksk karllgptvt
      661 lgghkfsrqr lqafglnpkr lhfrqlgrqr kkqqsha
//
LOCUS       NP_001423490             365 aa            linear   ROD 17-MAR-2025
DEFINITION  transmembrane protein 25 precursor [Rattus norvegicus].
ACCESSION   NP_001423490 XP_006243021
VERSION     NP_001423490.1
DBSOURCE    REFSEQ: accession NM_001436561.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Zhang,H., Tian,X., Lu,X., Xu,D., Guo,Y., Dong,Z., Li,Y., Ma,Y.,
            Chen,C., Yang,Y., Yang,M., Yang,Y., Liu,F., Zhou,R., He,M., Xiao,F.
            and Wang,X.
  TITLE     TMEM25 modulates neuronal excitability and NMDA receptor subunit
            NR2B degradation
  JOURNAL   J Clin Invest 129 (9), 3864-3876 (2019)
   PUBMED   31424425
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1596647.1,
                                           SRR26643429.29968.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..365
                     /product="transmembrane protein 25 precursor"
                     /calculated_mol_wt=36461
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2760
     Region          27..118
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          48..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          62..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..365
                     /gene="Tmem25"
                     /coded_by="NM_001436561.1:92..1189"
                     /db_xref="GeneID:689172"
                     /db_xref="RGD:1596132"
ORIGIN      
        1 melplsqatl rhtllllpal lssgqgelap qidgqtwaer alrenehhaf tcrvaggsat
       61 prlawyldgq lqkattsrll svggdafsgg tstftvtaqr sqhelncslq dpgsgrpana
      121 svilnvqfkp eiaqvgakyq eaqgpgllvv lfalvranpp anvtwidqdg pvtvnasdfl
      181 vldaqnypwl tnhtvqlqlr slahnlsvva tndvgvtsas lpapgllatr ievpllgivv
      241 agglafgtlv gfstlvaclv crkekktkgp srrpslissd snnlklnnvr lprenmslps
      301 nlqlndltpd irgkaterpm aqhssrpell eaepggllts rgfirlpmlg yiyrvssvss
      361 deiwl
//
LOCUS       NP_001423465             387 aa            linear   ROD 17-MAR-2025
DEFINITION  endonuclease 8-like 1 [Rattus norvegicus].
ACCESSION   NP_001423465 XP_038937801
VERSION     NP_001423465.1
DBSOURCE    REFSEQ: accession NM_001436536.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Ma,H., Wang,J., Abdel-Rahman,S.Z., Hazra,T.K., Boor,P.J. and
            Khan,M.F.
  TITLE     Induction of NEIL1 and NEIL2 DNA glycosylases in aniline-induced
            splenic toxicity
  JOURNAL   Toxicol Appl Pharmacol 251 (1), 1-7 (2011)
   PUBMED   21145906
  REMARK    GeneRIF: In the spleen aniline-induced oxidative stress is
            associated with an induction of NEIL1/2.
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Das,A., Boldogh,I., Lee,J.W., Harrigan,J.A., Hegde,M.L.,
            Piotrowski,J., de Souza Pinto,N., Ramos,W., Greenberg,M.M.,
            Hazra,T.K., Mitra,S. and Bohr,V.A.
  TITLE     The human Werner syndrome protein stimulates repair of oxidative
            DNA base damage by the DNA glycosylase NEIL1
  JOURNAL   J Biol Chem 282 (36), 26591-26602 (2007)
   PUBMED   17611195
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Takao,M., Kanno,S., Kobayashi,K., Zhang,Q.M., Yonei,S., van der
            Horst,G.T. and Yasui,A.
  TITLE     A back-up glycosylase in Nth1 knock-out mice is a functional Nei
            (endonuclease VIII) homologue
  JOURNAL   J Biol Chem 277 (44), 42205-42213 (2002)
   PUBMED   12200441
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_038937801.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.33801.1,
                                           SRR26643289.23054.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..387
                     /product="endonuclease 8-like 1"
                     /EC_number="4.2.99.18"
                     /note="endonuclease VIII-like 1; nei endonuclease
                     VIII-like 1"
                     /calculated_mol_wt=43218
     Region          1..127
                     /region_name="FpgNei_N"
                     /note="N-terminal domain of Fpg (formamidopyrimidine-DNA
                     glycosylase, MutM)_Nei (endonuclease VIII) base-excision
                     repair DNA glycosylases; cl03119"
                     /db_xref="CDD:470740"
     Site            order(2..3,54,78,80..82,95..96)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176801"
     Site            2
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:176801"
     Site            order(3..6,8..9,12,51..55)
                     /site_type="other"
                     /note="H2TH interface [polypeptide binding]"
                     /db_xref="CDD:176801"
     Site            order(3,54)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:176801"
     Region          <52..>206
                     /region_name="fpg"
                     /note="DNA-formamidopyrimidine glycosylase; TIGR00577"
                     /db_xref="CDD:273150"
     Region          252..290
                     /region_name="Neil1-DNA_bind"
                     /note="Endonuclease VIII-like 1, DNA bind; pfam09292"
                     /db_xref="CDD:462745"
     CDS             1..387
                     /gene="Neil1"
                     /coded_by="NM_001436536.1:254..1417"
                     /db_xref="GeneID:367090"
                     /db_xref="RGD:1306077"
ORIGIN      
        1 mpegpelhla shfvneickg lvfggcveks svsrnpevpf essayhisal argkelrltl
       61 splpgshppq kplslvfrfg msgsfqlvpa ealprhahlr fytappaprl alcfvdirrf
      121 ghwdpggewq pgrgpcvlle yerfrenvlr nlsdkafdrp icealldqrf fngignylra
      181 eilyrlkipp fekartvlea lqqcrlspel tlsqkvkakl qnpdllelch lvpkevvqlg
      241 gkgygperge edfaafrawl rcyavpgmss lrdrhgrtiw fqgdpgplap kggrsrkkks
      301 qetqleaedr kedppsksis rtqrarkhcp knvpqqsega slpqnletpa vpekgkrrgr
      361 rastgrhrgp kskpdtqpre ageisas
//
LOCUS       NP_001423492             848 aa            linear   ROD 17-MAR-2025
DEFINITION  piwi-like protein 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423492 XP_008764202
VERSION     NP_001423492.1
DBSOURCE    REFSEQ: accession NM_001436563.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Henaoui,I.S., Jacovetti,C., Guerra Mollet,I., Guay,C., Sobel,J.,
            Eliasson,L. and Regazzi,R.
  TITLE     PIWI-interacting RNAs as novel regulators of pancreatic beta cell
            function
  JOURNAL   Diabetologia 60 (10), 1977-1986 (2017)
   PUBMED   28711973
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Sivagurunathan,S., Palanisamy,K., Arunachalam,J.P. and
            Chidambaram,S.
  TITLE     Possible role of HIWI2 in modulating tight junction proteins in
            retinal pigment epithelial cells through Akt signaling pathway
  JOURNAL   Mol Cell Biochem 427 (1-2), 145-156 (2017)
   PUBMED   28025795
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Yang,Z., Chen,K.M., Pandey,R.R., Homolka,D., Reuter,M.,
            Janeiro,B.K., Sachidanandam,R., Fauvarque,M.O., McCarthy,A.A. and
            Pillai,R.S.
  TITLE     PIWI Slicing and EXD1 Drive Biogenesis of Nuclear piRNAs from
            Cytosolic Targets of the Mouse piRNA Pathway
  JOURNAL   Mol Cell 61 (1), 138-152 (2016)
   PUBMED   26669262
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Pastor,W.A., Stroud,H., Nee,K., Liu,W., Pezic,D., Manakov,S.,
            Lee,S.A., Moissiard,G., Zamudio,N., Bourc'his,D., Aravin,A.A.,
            Clark,A.T. and Jacobsen,S.E.
  TITLE     MORC1 represses transposable elements in the mouse male germline
  JOURNAL   Nat Commun 5, 5795 (2014)
   PUBMED   25503965
  REMARK    Erratum:[Nat Commun. 2015 Jul 10;6:7604. doi: 10.1038/ncomms8604.
            PMID: 26159654]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Keam,S.P., Young,P.E., McCorkindale,A.L., Dang,T.H., Clancy,J.L.,
            Humphreys,D.T., Preiss,T., Hutvagner,G., Martin,D.I., Cropley,J.E.
            and Suter,C.M.
  TITLE     The human Piwi protein Hiwi2 associates with tRNA-derived piRNAs in
            somatic cells
  JOURNAL   Nucleic Acids Res 42 (14), 8984-8995 (2014)
   PUBMED   25038252
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Aravin,A.A., Sachidanandam,R., Bourc'his,D., Schaefer,C., Pezic,D.,
            Toth,K.F., Bestor,T. and Hannon,G.J.
  TITLE     A piRNA pathway primed by individual transposons is linked to de
            novo DNA methylation in mice
  JOURNAL   Mol Cell 31 (6), 785-799 (2008)
   PUBMED   18922463
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Totoki,Y., Toyoda,A.,
            Ikawa,M., Asada,N., Kojima,K., Yamaguchi,Y., Ijiri,T.W., Hata,K.,
            Li,E., Matsuda,Y., Kimura,T., Okabe,M., Sakaki,Y., Sasaki,H. and
            Nakano,T.
  TITLE     DNA methylation of retrotransposon genes is regulated by Piwi
            family members MILI and MIWI2 in murine fetal testes
  JOURNAL   Genes Dev 22 (7), 908-917 (2008)
   PUBMED   18381894
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Carmell,M.A., Girard,A., van de Kant,H.J., Bourc'his,D.,
            Bestor,T.H., de Rooij,D.G. and Hannon,G.J.
  TITLE     MIWI2 is essential for spermatogenesis and repression of
            transposons in the mouse male germline
  JOURNAL   Dev Cell 12 (4), 503-514 (2007)
   PUBMED   17395546
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_008764202.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.43905.1,
                                           SRR26643429.29219.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..848
                     /product="piwi-like protein 4 isoform 1"
                     /note="piwi-like protein 4; piwi-like 4"
                     /calculated_mol_wt=95889
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G033.2)"
     Region          265..381
                     /region_name="PAZ_piwi_like"
                     /note="PAZ domain, Piwi_like subfamily. In multi-cellular
                     organisms, the Piwi protein appears to be essential for
                     the maintenance of germline stem cells. In the Drosophila
                     male germline, Piwi was shown to be involved in the
                     silencing of retrotransposons in the...; cd02845"
                     /db_xref="CDD:239211"
     Site            order(310,323,331,335,353,368,370)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239211"
     Region          389..831
                     /region_name="Piwi_piwi-like_Euk"
                     /note="PIWI domain, Piwi-like subfamily found in
                     eukaryotes. This domain is found in Piwi and closely
                     related proteins, where it is believed to perform a
                     crucial role in germline cells, via RNA silencing. RNA
                     silencing refers to a group of related...; cd04658"
                     /db_xref="CDD:240016"
     Site            order(554,558,570..573,576,586,589,593,597)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240016"
     Site            order(618,620,688,823)
                     /site_type="active"
                     /db_xref="CDD:240016"
     CDS             1..848
                     /gene="Piwil4"
                     /coded_by="NM_001436563.1:108..2654"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:689972"
                     /db_xref="RGD:1311015"
ORIGIN      
        1 msgrarvrar gittghsare veraprdlmv tsvspgdnea ssrtsvisqp helgvssgdg
       61 rrtlvekrgn grqdfvdlgv ctreklthvk dsktgssgip vqlatnlfhl dlpqdwqlyq
      121 yhvtyspdla srrlrtally nhsilsdkak afdgtslfls ekldhkvtel tsetqrgetv
      181 kitltltsel fpnspmciqf fnvifrkifk klsmyqigrn yykpsepvei pqyklslwpg
      241 faisvsrfes kllfnadvny kvlrnetvle fmtdlclrtd mscftetchk qlvglivltr
      301 ynnktyridd idwsvkptha fqkrdgsett yvdyykqqyd itlsdlnqpv lvsllkrrrn
      361 dnsepqmvhl ipelcfltgl tsqatsdfrl mkavaeetrl spmgrqqqla rladdiqrnq
      421 vtrfeletwg lhfgsqlslt grvvpsekil lqdhtcqpaf aadwskdmrs ckvlssepln
      481 twlivccsra ehliesflsc lrrvggstgf svghpkiikv denpaaflra iqlhvnpdvq
      541 lvmcilpsnq knyydsikry lssdcpvpsq cvltrtlnkq gmmlsvatki amqmtcklgg
      601 elwaveiplk slmvvgidic rdalskdvav vgfvasinsr itrwfsrcvl qrtaadiadc
      661 lkvcmtgaln kwykhnhdlp ariiayrdgv gngqlkavle yevpqllssv tecgsdarsc
      721 rlsvvvvrkr cllrlfaesg htlqnpplgt vvdseatrpe wydfyltsqt anrgtvspty
      781 ynviyddnal kpdhmqrltf klchlyynwq gvisvpapcq yahkltflva qsihkepsle
      841 lanklfyl
//
LOCUS       NP_001423475             643 aa            linear   ROD 17-MAR-2025
DEFINITION  zinc finger protein 202 [Rattus norvegicus].
ACCESSION   NP_001423475 XP_063122034
VERSION     NP_001423475.1
DBSOURCE    REFSEQ: accession NM_001436546.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Wagner,S., Hess,M.A., Ormonde-Hanson,P., Malandro,J., Hu,H.,
            Chen,M., Kehrer,R., Frodsham,M., Schumacher,C., Beluch,M.,
            Honer,C., Skolnick,M., Ballinger,D. and Bowen,B.R.
  TITLE     A broad role for the zinc finger protein ZNF202 in human lipid
            metabolism
  JOURNAL   J Biol Chem 275 (21), 15685-15690 (2000)
   PUBMED   10748193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_063122034.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.44722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..643
                     /product="zinc finger protein 202"
                     /calculated_mol_wt=73303
     Region          45..155
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          239..299
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <334..626
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          395..415
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(400,402,404,406..407,410..411,414,428,430,434..435,
                     438..439,442,482,484,486,488..489,492..493,496)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          423..443
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(566,568,570,572..573,576..577,580,594,596,600..601,
                     604..605,608,622,624,626,628..629,632..633,636)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          617..637
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..643
                     /gene="Zfp202"
                     /gene_synonym="RGD1562294"
                     /coded_by="NM_001436546.1:435..2366"
                     /db_xref="GeneID:500981"
                     /db_xref="RGD:1562294"
ORIGIN      
        1 mataleledq dlweeeeegv lmvkleddft cgpesalqgd dpvletshqn frcfryqeas
       61 sprealirlr elchqwlrpe rrtkeqilel lvleqfltvl pgelqswvrg qrpesgeeav
      121 tlveglqkqp rrprrwvtvh vqgqevlsee tlhlgvepes sneqqeptqt ltaeqpheea
      181 lrstdlgtle qeslqheger lpllesevpv sqhadlpteq gsghpemval ltalsqglvt
      241 fkdvalcfsq dqwsdldptq kefygeyvle edcgivvsls fpiprlddps qireeepqvp
      301 gvhesqepae peilsftytg dmseaeeecv eqqdtnksil anteihqtpd weiviednts
      361 rlnerfgtnv skvnsftnir ktmpvhsqsg rqhhcplcak sftcnshlir hlrthtgekp
      421 ykcmecgksy trsshlarhq kvhkvntphk hppnrktvda sqvqseattr vekpytcddc
      481 gkhfrwtsdl vrhqrthtge kpffcticgk sfsqksvltt hqrihvggkp ytcancgenf
      541 seqkqylahr kthvseenhl csecgrsfnh saafakhlkg hasvrncrcd ecgksfsrrd
      601 hlvrhqrtht gekpftcatc gksfsrgyhl irhqrihtgk tkt
//
LOCUS       NP_001423487             636 aa            linear   ROD 17-MAR-2025
DEFINITION  beta-galactosidase-1-like protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423487 XP_006242800
VERSION     NP_001423487.1
DBSOURCE    REFSEQ: accession NM_001436558.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006242800.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.31062.1,
                                           SRR26360172.2334858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..636
                     /product="beta-galactosidase-1-like protein 2 isoform 1"
                     /EC_number="3.2.1.23"
                     /note="beta-galactosidase-1-like protein 2"
                     /calculated_mol_wt=72089
     Region          53..366
                     /region_name="Glyco_hydro_35"
                     /note="Glycosyl hydrolases family 35; pfam01301"
                     /db_xref="CDD:396048"
     CDS             1..636
                     /gene="Glb1l2"
                     /gene_synonym="RGD1564436"
                     /coded_by="NM_001436558.1:43..1953"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:503194"
                     /db_xref="RGD:1564436"
ORIGIN      
        1 mpkwslrrrp grtlglllll vlsflvlrrl nwtsvlplwl qrqrlglrtk gpnfmledst
       61 fqilggsihy frvpreywrd rllklkacgl ntlttyvpwn lhepergkfd fsgnldleaf
      121 iwlaakiglw vilrpgpyic seidlgglps wllqdpdmkl rttypgftka vdlyfdhlms
      181 rvvplqykhg gpiiavqven eygsyngdha ympyikkale drgiiemllt sdnkdglekg
      241 vvdgvlatin lqsqqelval nsillsiqgi qpkmvmeywt gwfdswggsh nildssevlq
      301 tvsaiikdgs sinlymfhgg tnfgfingam hfgdykadvt sydydailte agdytakytk
      361 lrelfgtfsg vppppppelt akmvyepvtp sfylslwdal lymdkpitse ipinmenlpv
      421 nngngqafgy vlyettifss gvlsglvrdr gqvflnrvsi gfldytttki tipltqgyti
      481 lrilvenrgr vnygnnidsq rkglignlyl nnkplknfki ysldmtkqff qrfdmdkwsv
      541 vpkeitfpaf flgtlsvgiy psdtflkleg wvkgvvlvnd hnlgrywnvg pqetlylpgv
      601 wldkglnkvi ifeetmagsm vqstdiphlg rnqyvn
//
LOCUS       NP_001423481             369 aa            linear   ROD 17-MAR-2025
DEFINITION  layilin isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423481 XP_006243111
VERSION     NP_001423481.1
DBSOURCE    REFSEQ: accession NM_001436552.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Bono,P., Rubin,K., Higgins,J.M. and Hynes,R.O.
  TITLE     Layilin, a novel integral membrane protein, is a hyaluronan
            receptor
  JOURNAL   Mol Biol Cell 12 (4), 891-900 (2001)
   PUBMED   11294894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243111.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.721013.1,
                                           SRR21887620.721014.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840108,
                                           SAMN12840110 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..369
                     /product="layilin isoform 1 precursor"
                     /calculated_mol_wt=39542
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2480
     Region          30..178
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(140,144,146,162,164..167,170..172)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153065"
     CDS             1..369
                     /gene="Layn"
                     /gene_synonym="RGD1564444"
                     /coded_by="NM_001436552.1:122..1231"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:500996"
                     /db_xref="RGD:1564444"
ORIGIN      
        1 mqpgaalqam llavllakpr dskghllsgq rfcwegtrrp cyrviyfhdt sqrrnfeeak
       61 eacmkdggql asietadeqr lienfieslq asdgdfwigl krleekqhns tacqdlyawt
      121 dgslsqfrnw ymdepscese vcvvmyhqps appgiggpym fqwnddrcnt kknfickysd
      181 dkpsttpsls pggeatepaa pilpeetlei dtkerreaal nlayilipsi plflllvvts
      241 avcwvwicrr kreqtdpptk eqhtiwptph qenspdlevy nvirkqsead laeprpdlkn
      301 isfrvcsgea mpddtscdyd nmvinpsesg lvtlasmegr fvtndiyefs pdrmgrskes
      361 gwveneiyy
//
LOCUS       NP_001423458             207 aa            linear   ROD 17-MAR-2025
DEFINITION  melanocortin-2 receptor accessory protein 2 [Rattus norvegicus].
ACCESSION   NP_001423458 XP_006243550
VERSION     NP_001423458.1
DBSOURCE    REFSEQ: accession NM_001436529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Asai,M., Ramachandrappa,S., Joachim,M., Shen,Y., Zhang,R.,
            Nuthalapati,N., Ramanathan,V., Strochlic,D.E., Ferket,P.,
            Linhart,K., Ho,C., Novoselova,T.V., Garg,S., Ridderstrale,M.,
            Marcus,C., Hirschhorn,J.N., Keogh,J.M., O'Rahilly,S., Chan,L.F.,
            Clark,A.J., Farooqi,I.S. and Majzoub,J.A.
  TITLE     Loss of function of the melanocortin 2 receptor accessory protein 2
            is associated with mammalian obesity
  JOURNAL   Science 341 (6143), 275-278 (2013)
   PUBMED   23869016
  REMARK    Erratum:[Science. 2013 Aug 30;341(6149):959]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Sebag,J.A. and Hinkle,P.M.
  TITLE     Regulation of G protein-coupled receptor signaling: specific
            dominant-negative effects of melanocortin 2 receptor accessory
            protein 2
  JOURNAL   Sci Signal 3 (116), ra28 (2010)
   PUBMED   20371771
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chan,L.F., Webb,T.R., Chung,T.T., Meimaridou,E., Cooray,S.N.,
            Guasti,L., Chapple,J.P., Egertova,M., Elphick,M.R., Cheetham,M.E.,
            Metherell,L.A. and Clark,A.J.
  TITLE     MRAP and MRAP2 are bidirectional regulators of the melanocortin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 106 (15), 6146-6151 (2009)
   PUBMED   19329486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006243550.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.912894.1,
                                           SRR26360176.1861836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..207
                     /product="melanocortin-2 receptor accessory protein 2"
                     /calculated_mol_wt=23660
     Region          16..101
                     /region_name="MRAP"
                     /note="Melanocortin-2 receptor accessory protein family;
                     pfam15183"
                     /db_xref="CDD:464550"
     CDS             1..207
                     /gene="Mrap2"
                     /gene_synonym="RGD1309873"
                     /coded_by="NM_001436529.1:188..811"
                     /db_xref="GeneID:363112"
                     /db_xref="RGD:1309873"
ORIGIN      
        1 memsaqrlts nrtspqspsn sdytweyeyy eigpvsfegl kahkysivig fwvglavfvi
       61 fmffvltllt ktgaphqdna essekrfrmn sfvsdfgkpl esdkvfsrqg neesrslfhc
      121 yinevehldr vkvchrttai dsdvhlqeai rssgrpeeel trfmqfdipn fvntdqnsfg
      181 eddllisepp vllenkpvsq tsrtdld
//
LOCUS       NP_001423467             557 aa            linear   ROD 17-MAR-2025
DEFINITION  copine-4 [Rattus norvegicus].
ACCESSION   NP_001423467 XP_017451280
VERSION     NP_001423467.1
DBSOURCE    REFSEQ: accession NM_001436538.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Takizawa,C., Minematsu,T., Nakagami,G., Kitamura,A., Koudounas,S.,
            Kunimitsu,M. and Sanada,H.
  TITLE     Expression levels of NPPB, ITGB6, CPNE4, EML5, and ITSN1 in fresh
            exudates swabbed from critically colonised and infected
            full-thickness wounds in rats
  JOURNAL   Int Wound J 20 (4), 1088-1097 (2023)
   PUBMED   36307995
  REMARK    GeneRIF: Expression levels of NPPB, ITGB6, CPNE4, EML5, and ITSN1
            in fresh exudates swabbed from critically colonised and infected
            full-thickness wounds in rats.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_017451280.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.676376.1,
                                           SRR26360176.1952537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..557
                     /product="copine-4"
                     /note="copine IV"
                     /calculated_mol_wt=62277
     Region          24..140
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(39,45,97,99,109)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Region          155..267
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(170,176,232,234,240)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          326..539
                     /region_name="Copine"
                     /note="pfam07002"
                     /db_xref="CDD:462064"
     CDS             1..557
                     /gene="Cpne4"
                     /coded_by="NM_001436538.1:438..2111"
                     /db_xref="GeneID:367160"
                     /db_xref="RGD:1308844"
ORIGIN      
        1 mkkmsniyes aantlgifns pcltkvelrv ackgisdrda lskpdpcvil kmqshgqwfe
       61 vdrtevirtc inpvysklft vdfyfeevqr lrfevhdiss nhnglkeadf lggmectlgq
      121 ivsqrklsks llkhgntagk ssitviaeel sgnddyvela fnarklddkd ffsksdpfle
      181 ifrmnddatq qlvhrtevvm nnlspawksf kvsvnslcsg dpdrrlkciv wdwdsngkhd
      241 figeftstfk emrgamegkq vqwecinpky kakkknykns gmvilnqcki hkmhsfldyi
      301 mggcqiqftv aidftasngd prnscslhyi hpyqpneylk alvavgeicq dydsdkmfpa
      361 fgfgarippe ytvshdfain fnednpecag iqgvveayqs clpklqlygp tniapiiqkv
      421 aksaseetnt keasqyfill iltdgvitdm adtreaivha shlpmsviiv gvgnadfsdm
      481 qmldgddgil rspkgepvlr divqfvpfrn fkhaspaala ksvlaevpnq vvdyyngkgi
      541 kpkcssevye ssrtlap
//
LOCUS       NP_001178593             711 aa            linear   ROD 17-MAR-2025
DEFINITION  RB-associated KRAB zinc finger protein [Rattus norvegicus].
ACCESSION   NP_001178593 XP_006248930 XP_221920
VERSION     NP_001178593.1
DBSOURCE    REFSEQ: accession NM_001191664.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Mar 13, 2025 this sequence version replaced
            XP_006248930.1, XP_221920.5.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2531008.1,
                                           SRR26643294.45631.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..711
                     /product="RB-associated KRAB zinc finger protein"
                     /note="RB-associated KRAB repressor"
                     /calculated_mol_wt=81537
     Region          8..68
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..336
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(321,323,325,327..328,331..332,335,349,351,355..356,
                     359..360,363,377,379,381,383..384,387..388,391)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          340..699
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          456..476
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          594..614
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          622..642
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(627,629,631,633..634,637..638,641,655,657,661..662,
                     665..666,669,683,685,687,689..690,693..694,697)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          650..670
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          678..698
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..711
                     /gene="Rbak"
                     /gene_synonym="RGD1562875"
                     /coded_by="NM_001191664.2:252..2387"
                     /db_xref="GeneID:288489"
                     /db_xref="RGD:1562875"
ORIGIN      
        1 msiskgplsf kdvavafsqe ewqqldseer ttyrdvmlet ysnlvsvgyd vtkpnviikl
       61 eqgeepwtve gdrhakrhle ikkvddpreg iqengekhlq cgddlhswra ekgdefdeac
      121 tlepplisps sgahscvscg ktlesvteli csdgsyavek pdkcfecgkg yrenpedlnq
      181 segnsserde silqkitile kpfdyeclea ldresvfmah eraymgekpy ewngsgpdfi
      241 qisdfstyhr sqvemkpfec tqcgksfckk skfiihqrah tgekpyacgv cgksfsqkgt
      301 ltvhrrshle ekpykcdecg ktfcqklhlt qhqrthsgek pyecsecgkt fcqkthltlh
      361 qrnhsgerpy pcsecgksfs rksalndhqr thtgeklytc necgksyyrk stlithqrth
      421 tgekpyqcse cgkffsrvsy ltihyrshle ekpyectecg ktfnlnsaft rhrkahaeer
      481 vqecgecgkp srlqylpdha dglgekhhgc necgktflen safsrhqpvp egektyecni
      541 cgkvfsdlsc ytvhyrghse ekpfgcsecg ktfshnsslf rhqrvhtgek pyecyecgkf
      601 fsqksyltih hrihsgekpy ecskcgkvfs rmsnltvhyr shsgekpyec necgkvfsqk
      661 syltvhyrth sgekpyecne cgkkfhhrsa fnshqrihkr gtinvlnven l
//
LOCUS       NP_001423496             633 aa            linear   ROD 17-MAR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 11 [Rattus
            norvegicus].
ACCESSION   NP_001423496 XP_006253453
VERSION     NP_001423496.1
DBSOURCE    REFSEQ: accession NM_001436567.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253453.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.508413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..633
                     /product="kelch repeat and BTB domain-containing protein
                     11"
                     /note="kelch repeat and BTB (POZ) domain containing 11"
                     /calculated_mol_wt=67718
     Region          144..246
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          237..313
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     Region          341..574
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          356..404
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          496..546
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..633
                     /gene="Kbtbd11"
                     /gene_synonym="RGD1563576"
                     /coded_by="NM_001436567.1:931..2832"
                     /db_xref="GeneID:306617"
                     /db_xref="RGD:1563576"
ORIGIN      
        1 mensvapfvl ypgteprtpg edslplpaee egaaspaqtp cslsaslcfs sgddsppqsr
       61 asaaegseas ppslrsdlrv vetqwdvssa aspespqeca rpeepaspee ppsrreharp
      121 velesldelg epvpvppgvg sehgepdlvi evagrrlrah kavlaarsdy frarasrdvl
      181 rvqgvsftal rllladaysg cmagvrpdnv aevvagarrl qlpgaaqrat eamapqlsld
      241 ncyevlsagk rqrlselrda ayrfmcdhyl evlrepavfg rlsgaerdll lrrrlgtgra
      301 cllaaalgtt gersgsrpqs psgdaesrgd aavycyqaea gewreltrlp egapargcgl
      361 cvlfnylfva ggvapagpdg rarpsdqvfc ynpvtdcwst vrplrqarsq vqllaldghl
      421 yalggeclls verydpradr wtavaplprg afavaheaat cngeiyvsgg slfyrllkyd
      481 prrdewqecp csssrersad mvaldgflyr fdlcgsrgda qaatgsgggv svfryhclak
      541 qwsqcaahlr ppgapaglqp frcvaldgti ycvsragtwr fvpsqdteag sdmgpggsfe
      601 peplgspldv rgvlfpfvln lpekpdrgeq gaa
//
LOCUS       NP_001423510             290 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423510
VERSION     NP_001423510.1
DBSOURCE    REFSEQ: accession NM_001436581.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.616331.1,
                                           SRR22582424.2217263.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..290
                     /product="transcription factor Dp-1 isoform 2"
                     /calculated_mol_wt=32336
     Region          1..73
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(78,82,85..86,88..89,92..93,95..96,99..100,103,
                     106..107,110,113..114,116..117,119..121,124,135..146,148,
                     159..167,169,171,173,179..180,182)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          78..124
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          80..218
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(102,105..106,109,142,151,153,168..175,182)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..290
                     /gene="Tfdp1"
                     /coded_by="NM_001436581.1:474..1346"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
       61 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      121 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      181 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      241 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001171155             550 aa            linear   ROD 17-MAR-2025
DEFINITION  probable cysteine--tRNA ligase, mitochondrial isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001171155 XP_001076059 XP_002728484
VERSION     NP_001171155.1
DBSOURCE    REFSEQ: accession NM_001177684.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_001076059.2, XP_002728484.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166536.1, SRR26643288.56382.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..550
                     /product="probable cysteine--tRNA ligase, mitochondrial
                     isoform 1"
                     /EC_number="6.1.1.16"
                     /note="probable cysteine--tRNA ligase, mitochondrial"
                     /calculated_mol_wt=60787
     Region          23..547
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     CDS             1..550
                     /gene="Cars2"
                     /gene_synonym="RGD1311612"
                     /coded_by="NM_001177684.2:56..1708"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361184"
                     /db_xref="RGD:1311612"
ORIGIN      
        1 mlralrpgpg apllraalvl grrgrawqrp qgqdtgvqvh nsltgkkepl ivgrsdavsw
       61 yscgptvydh ahlghacsyv rfdiirrilt svfgcnvvma msitdvddki ikranemnvs
      121 paslaslfee efkqdmaalk vlpptvylrv tenipqiisf iqgiiahgha yatatgsvyf
      181 dlrargdkyg klvntvpsat aepavdsdkr hssdfalwkg akpqevfwas pwgdgrpgwh
      241 iecsamasev fgsqldihtg gidlafphhe neiaqsevfh qcqqwgnyfl hsghlhvkgk
      301 eekmskslkn yitikdflqt fspdvfrlfc lrtnyrsaid ysdstleear hlllglasfv
      361 edarayvkgq licgpvgedv lwerlastkk avkaalandf dtpravnsil dlvhhanrql
      421 ravskeaggp rsptvfgaiv ayveqffetv gislakrqcv sgdsstvalh cvvdelvrfr
      481 lkvrqyalat pgatgearkq qlqerqplle acdalrqdlm thginvkdrg haastwelld
      541 prtkhqkpgt
//
LOCUS       NP_001423502             179 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423502
VERSION     NP_001423502.1
DBSOURCE    REFSEQ: accession NM_001436573.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1853899.1,
                                           SRR26360194.1520438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..179
                     /product="glutamate-rich protein 1 isoform 6"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=20173
     Region          <59..>162
                     /region_name="Cnd3"
                     /note="Nuclear condensing complex subunits, C-term domain;
                     pfam12719"
                     /db_xref="CDD:463678"
     CDS             1..179
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436573.1:577..1116"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msrnkkrkwr aklrlrrkre aglaarasaa sftyepesse eaevegdvgg eeeedpessv
       61 adpaqedtel assradslls flkstqeiyf ydasredpav steaaeellr llesgrlppa
      121 dvlildhmkt llllqdterl tsalkmfpeh cmmppdhari isaffnywit qilpekrse
//
LOCUS       NP_001423504             601 aa            linear   ROD 17-MAR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase-like 6 [Rattus
            norvegicus].
ACCESSION   NP_001423504
VERSION     NP_001423504.1
DBSOURCE    REFSEQ: accession NM_001436575.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Zhang,S., Wang,X., Chen,G., Tong,L., Dai,T., Wang,L., Zhu,L.,
            Zhang,H. and Du,D.
  TITLE     CircRNA Galntl6 sponges miR-335 to ameliorate stress-induced
            hypertension through upregulating Lig3 in rostral ventrolateral
            medulla
  JOURNAL   Redox Biol 64, 102782 (2023)
   PUBMED   37315345
  REMARK    GeneRIF: CircRNA Galntl6 sponges miR-335 to ameliorate
            stress-induced hypertension through upregulating Lig3 in rostral
            ventrolateral medulla.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Raman,J., Guan,Y., Perrine,C.L., Gerken,T.A. and Tabak,L.A.
  TITLE     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferases: completion of the family tree
  JOURNAL   Glycobiology 22 (6), 768-777 (2012)
   PUBMED   22186971
  REMARK    Erratum:[Glycobiology. 2015 Apr;25(4):465. doi:
            10.1093/glycob/cwv003. PMID: 25715345]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1695777.1,
                                           SRR26360176.61016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p12-p11"
     Protein         1..601
                     /product="polypeptide
                     N-acetylgalactosaminyltransferase-like 6"
                     /EC_number="2.4.1.41"
                     /note="polypeptide N-acetylgalactosaminyltransferase 17;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 6"
                     /calculated_mol_wt=69640
     Region          143..438
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(147..149,151,180,209,212,216,232..234,314..315,
                     337..338,340,365,368,373)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(232,234,365)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          449..594
                     /region_name="beta-trefoil_Ricin_GALNTL6"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide
                     N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and
                     similar proteins; cd23477"
                     /db_xref="CDD:467355"
     Site            order(520,531,534,538..539)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467355"
     CDS             1..601
                     /gene="Galntl6"
                     /gene_synonym="Galnt17; RGD1564773"
                     /coded_by="NM_001436575.1:1820..3625"
                     /db_xref="GeneID:361142"
                     /db_xref="RGD:1564773"
ORIGIN      
        1 mkrkqkrflq mtllftvali flpniglwsl ykdkhlmksa epaehqtfpl glgdgqfysw
       61 tdglrrkdwh dyvsiqkdal rsgkgehgkp yplteedhdd sayrengfni fvsnnialer
      121 slpdirhanc khkmylerlp ntsiiipfhn egwtsllrti hsiinrtpes liaeiilvdd
      181 fsdrehlkdk ledymarfpi vrivrtkkre glirtrllga svargevltf ldshcevnvn
      241 wlppllnqia lnhktivcpm idvidhshfg yeaqagdamr gafdwemyyk ripippelqr
      301 adpsepfesp vmagglfavd rkwfwelggy dpgleiwgge qyeisfkvwm cggemfdvpc
      361 srvghiyrky vpykvpsgts larnlkrvae twmdefaeyi yqrrpeyrhl stgdisaqke
      421 lrkrlkckdf kwfmaavawd vpkyyppvep lpaawgeirn vaanlcvdsk hgamgtelrl
      481 dicvkdgser twsheqlftf gwredirpge plhtrkfcld aishsspvtl ydchgmkgnq
      541 lwgyredrtl fhpvsnscmd cnpaekkvfm arcdplsetq qwmfehinmt vlekishyai
      601 s
//
LOCUS       NP_001423506             410 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423506 XP_038950605
VERSION     NP_001423506.1
DBSOURCE    REFSEQ: accession NM_001436577.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_038950605.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2010387.1,
                                           SRR26360172.1484695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..410
                     /product="transcription factor Dp-1 isoform 1"
                     /calculated_mol_wt=45057
     Region          112..193
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(198,202,205..206,208..209,212..213,215..216,
                     219..220,223,226..227,230,233..234,236..237,239..241,244,
                     255..266,268,279..287,289,291,293,299..300,302)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          198..244
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          200..338
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(222,225..226,229,262,271,273,288..295,302)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..410
                     /gene="Tfdp1"
                     /coded_by="NM_001436577.1:123..1355"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 makdasliea ngelkvfidq nlspgkgvvs lvavhpstvn tlgkqllpkt fgqsnvnitq
       61 qvvigtpqrp aaantivvgs phtpnthfvs qnqtsdsspw sagkrnrkge kngkglrhfs
      121 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
      181 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      241 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      301 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      361 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423507             410 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423507 XP_008769620
VERSION     NP_001423507.1
DBSOURCE    REFSEQ: accession NM_001436578.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_008769620.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.251770.1,
                                           SRR21887622.2734729.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..410
                     /product="transcription factor Dp-1 isoform 1"
                     /calculated_mol_wt=45057
     Region          112..193
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(198,202,205..206,208..209,212..213,215..216,
                     219..220,223,226..227,230,233..234,236..237,239..241,244,
                     255..266,268,279..287,289,291,293,299..300,302)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          198..244
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          200..338
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(222,225..226,229,262,271,273,288..295,302)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..410
                     /gene="Tfdp1"
                     /coded_by="NM_001436578.1:690..1922"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 makdasliea ngelkvfidq nlspgkgvvs lvavhpstvn tlgkqllpkt fgqsnvnitq
       61 qvvigtpqrp aaantivvgs phtpnthfvs qnqtsdsspw sagkrnrkge kngkglrhfs
      121 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
      181 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      241 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      301 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      361 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423500             180 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423500
VERSION     NP_001423500.1
DBSOURCE    REFSEQ: accession NM_001436571.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.743350.1,
                                           SRR26360181.878795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..180
                     /product="glutamate-rich protein 1 isoform 5"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=20302
     CDS             1..180
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436571.1:577..1119"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msrnkkrkwr aklrlrrkre aglaarasaa sftyepesse eaevegdvgg eeeedpessv
       61 adpaqedtel assradslls flkstqeiyf ydeasredpa vsteaaeell rllesgrlpp
      121 advlildhmk tllllqdter ltsalkmfpe hcmmppdhar iisaffnywi tqilpekrse
//
LOCUS       NP_001423494            1004 aa            linear   ROD 17-MAR-2025
DEFINITION  malignant fibrous histiocytoma-amplified sequence 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001423494 XP_006253289
VERSION     NP_001423494.1
DBSOURCE    REFSEQ: accession NM_001436565.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Wang,H.H., Sun,P.F., Chen,W.K., Zhong,J., Shi,Q.Q., Weng,M.L.,
            Ma,D. and Miao,C.H.
  TITLE     High Glucose Stimulates Expression of MFHAS1 to Mitigate
            Inflammation via Akt/HO-1 Pathway in Human Umbilical Vein
            Endothelial Cells
  JOURNAL   Inflammation 41 (2), 400-408 (2018)
   PUBMED   29168081
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Shi,Q., Xiong,B., Zhong,J., Wang,H., Ma,D. and Miao,C.
  TITLE     MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C
            subunit cytoplasm translocation and inhibition of c-Jun
            dephosphorylation at Thr239
  JOURNAL   Mol Immunol 88, 79-88 (2017)
   PUBMED   28609714
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Zhong,J., Wang,H., Chen,W., Sun,Z., Chen,J., Xu,Y., Weng,M.,
            Shi,Q., Ma,D. and Miao,C.
  TITLE     Ubiquitylation of MFHAS1 by the ubiquitin ligase praja2 promotes M1
            macrophage polarization by activating JNK and p38 pathways
  JOURNAL   Cell Death Dis 8 (5), e2763 (2017)
   PUBMED   28471450
  REMARK    Erratum:[Cell Death Dis. 2018 Jul 16;9(8):782. doi:
            10.1038/s41419-018-0828-y. PMID: 30013073]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1004)
  AUTHORS   Zhong,J., Shi,Q.Q., Zhu,M.M., Shen,J., Wang,H.H., Ma,D. and
            Miao,C.H.
  TITLE     MFHAS1 Is Associated with Sepsis and Stimulates TLR2/NF-kappaB
            Signaling Pathway Following Negative Regulation
  JOURNAL   PLoS One 10 (11), e0143662 (2015)
   PUBMED   26599367
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1004)
  AUTHORS   Dihanich,S., Civiero,L., Manzoni,C., Mamais,A., Bandopadhyay,R.,
            Greggio,E. and Lewis,P.A.
  TITLE     GTP binding controls complex formation by the human ROCO protein
            MASL1
  JOURNAL   FEBS J 281 (1), 261-274 (2014)
   PUBMED   24286120
REFERENCE   6  (residues 1 to 1004)
  AUTHORS   Kumkhaek,C., Aerbajinai,W., Liu,W., Zhu,J., Uchida,N.,
            Kurlander,R., Hsieh,M.M., Tisdale,J.F. and Rodgers,G.P.
  TITLE     MASL1 induces erythroid differentiation in human
            erythropoietin-dependent CD34+ cells through the Raf/MEK/ERK
            pathway
  JOURNAL   Blood 121 (16), 3216-3227 (2013)
   PUBMED   23327923
REFERENCE   7  (residues 1 to 1004)
  AUTHORS   Ng,A.C., Eisenberg,J.M., Heath,R.J., Huett,A., Robinson,C.M.,
            Nau,G.J. and Xavier,R.J.
  TITLE     Human leucine-rich repeat proteins: a genome-wide bioinformatic
            categorization and functional analysis in innate immunity
  JOURNAL   Proc Natl Acad Sci U S A 108 Suppl 1 (Suppl 1), 4631-4638 (2011)
   PUBMED   20616063
REFERENCE   8  (residues 1 to 1004)
  AUTHORS   Sakabe,T., Shinomiya,T., Mori,T., Ariyama,Y., Fukuda,Y.,
            Fujiwara,T., Nakamura,Y. and Inazawa,J.
  TITLE     Identification of a novel gene, MASL1, within an amplicon at 8p23.1
            detected in malignant fibrous histiocytomas by comparative genomic
            hybridization
  JOURNAL   Cancer Res 59 (3), 511-515 (1999)
   PUBMED   9973190
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253289.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.52808.1,
                                           SRR26643297.47164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..1004
                     /product="malignant fibrous histiocytoma-amplified
                     sequence 1 isoform 2"
                     /note="malignant fibrous histiocytoma amplified sequence
                     1"
                     /calculated_mol_wt=111772
     Region          61..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <109..>371
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          109..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..155
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          156..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          225..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          248..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          294..316
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          317..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          340..360
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          405..>548
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            412..419
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            451
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            455..457
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            473..476
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(475..476,492..493)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     Site            533..536
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Region          656..902
                     /region_name="COR"
                     /note="C-terminal of Roc, COR, domain; pfam16095"
                     /db_xref="CDD:406489"
     CDS             1..1004
                     /gene="Mfhas1"
                     /coded_by="NM_001436565.1:603..3617"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306508"
                     /db_xref="RGD:1308812"
ORIGIN      
        1 magkdsgnlk tvrlwrdaal rarklrsnlr qltlscpgag gdslespdap qlvlpanigd
       61 ievlnlgnng ledvpeglgs algslrvlvl rrnrfarlpp avaelghhlt eldvshnrlt
      121 ilgaevvsal relrklnlsh nqlpalpaql galahleeld vsfnrlahlp dsfsclnhlr
      181 tldvdhnqlt afpqqllqla aleeldvssn rlrglpedis alralkilwl sgaelgtlps
      241 gfcelasles lmldnnglqa lpdefsrlqr lkmlnlssnl feefpaallp lagleelyls
      301 rnqltsvpsl iaglgrlltl wldnnriryl pdsiveltgl eelvlqgnqi avlpdnfgql
      361 srvglwkikd npliqppyev cmkgipyiaa yqkelahsqp avqprlklll mghkaagktl
      421 lrhcltedkv eggqgggdke ksylpfpplg skgievtswt adasrglrfi vydlagdesy
      481 eviqpfflsp galyvlvvnl atyeprcfpt tvgsflhrvg arvphavvci vgthadlcge
      541 releekcldi hrqialqekh daeglshlak vvdealardf elrsasphaa yygvsdknlr
      601 rrkahfqyll nhrlqilspv lpvscrdplq lqrlrdklls vaehreifpn lhrvlprswq
      661 vleelhfqpp qaqrlwlsww dsarlglqag ltedrlqsal sylhesgkll yfedspalke
      721 hvfhnltrli dilnvffqrd aslllhklll gtngegegeg esfptiavpt pgqdplratq
      781 lhhyvegfll hgllpahiir lllkphvqaq qdlqlllell ekmglcycln kpkgkplngs
      841 aawykfpcyv qnevphaeaw ingtnlagqs fvaeqlqiey sfpftfppgl farysvqins
      901 hvvhrsdgkf qifayrgkvp vvvsyrpakg vlqpdtlsia shaslpniwt awqaitplve
      961 elnvllqewp glhytvhilc skclkrgspn phafpvnprq slrd
//
LOCUS       NP_037120                509 aa            linear   ROD 17-MAR-2025
DEFINITION  nuclear factor 1 A-type isoform 2 [Rattus norvegicus].
ACCESSION   NP_037120 XP_346746
VERSION     NP_037120.1
DBSOURCE    REFSEQ: accession NM_012988.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Ding,B., Wang,W., Selvakumar,T., Xi,H.S., Zhu,H., Chow,C.W.,
            Horton,J.D., Gronostajski,R.M. and Kilpatrick,D.L.
  TITLE     Temporal regulation of nuclear factor one occupancy by
            calcineurin/NFAT governs a voltage-sensitive developmental switch
            in late maturing neurons
  JOURNAL   J Neurosci 33 (7), 2860-2872 (2013)
   PUBMED   23407945
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Riffel,A.K., Schuenemann,E. and Vyhlidal,C.A.
  TITLE     Regulation of the CYP3A4 and CYP3A7 promoters by members of the
            nuclear factor I transcription factor family
  JOURNAL   Mol Pharmacol 76 (5), 1104-1114 (2009)
   PUBMED   19706729
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Royland,J.E. and Kodavanti,P.R.
  TITLE     Gene expression profiles following exposure to a developmental
            neurotoxicant, Aroclor 1254: pathway analysis for possible mode(s)
            of action
  JOURNAL   Toxicol Appl Pharmacol 231 (2), 179-196 (2008)
   PUBMED   18602130
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Lu,W., Quintero-Rivera,F., Fan,Y., Alkuraya,F.S., Donovan,D.J.,
            Xi,Q., Turbe-Doan,A., Li,Q.G., Campbell,C.G., Shanske,A.L.,
            Sherr,E.H., Ahmad,A., Peters,R., Rilliet,B., Parvex,P.,
            Bassuk,A.G., Harris,D.J., Ferguson,H., Kelly,C., Walsh,C.A.,
            Gronostajski,R.M., Devriendt,K., Higgins,A., Ligon,A.H.,
            Quade,B.J., Morton,C.C., Gusella,J.F. and Maas,R.L.
  TITLE     NFIA haploinsufficiency is associated with a CNS malformation
            syndrome and urinary tract defects
  JOURNAL   PLoS Genet 3 (5), e80 (2007)
   PUBMED   17530927
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Lin,Y.L., Wang,Y.H. and Lee,H.J.
  TITLE     Transcriptional regulation of the human TR2 orphan receptor gene by
            nuclear factor 1-A
  JOURNAL   Biochem Biophys Res Commun 350 (2), 430-436 (2006)
   PUBMED   17010934
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Chaudhry,A.Z., Lyons,G.E. and Gronostajski,R.M.
  TITLE     Expression patterns of the four nuclear factor I genes during mouse
            embryogenesis indicate a potential role in development
  JOURNAL   Dev Dyn 208 (3), 313-325 (1997)
   PUBMED   9056636
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Osada,S., Daimon,S., Ikeda,T., Nishihara,T., Yano,K., Yamasaki,M.
            and Imagawa,M.
  TITLE     Nuclear factor 1 family proteins bind to the silencer element in
            the rat glutathione transferase P gene
  JOURNAL   J Biochem 121 (2), 355-363 (1997)
   PUBMED   9089412
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Monaci,P., Nuzzo,M., Stampfli,S., Tollervey,D., De Simone,V. and
            Nicosia,A.
  TITLE     A complex interplay of positive and negative elements is
            responsible for the different transcriptional activity of liver NF1
            variants
  JOURNAL   Mol Biol Rep 21 (3), 147-158 (1995)
   PUBMED   8832903
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Ang,S.L., Wierda,A., Wong,D., Stevens,K.A., Cascio,S., Rossant,J.
            and Zaret,K.S.
  TITLE     The formation and maintenance of the definitive endoderm lineage in
            the mouse: involvement of HNF3/forkhead proteins
  JOURNAL   Development 119 (4), 1301-1315 (1993)
   PUBMED   8306889
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Paonessa,G., Gounari,F., Frank,R. and Cortese,R.
  TITLE     Purification of a NF1-like DNA-binding protein from rat liver and
            cloning of the corresponding cDNA
  JOURNAL   EMBO J 7 (10), 3115-3123 (1988)
   PUBMED   3053160
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346746.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB060652.1, D78017.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..509
                     /product="nuclear factor 1 A-type isoform 2"
                     /note="nuclear factor 1 A-type; CTF; NF1-A; NFI-A; NF-I/A;
                     nuclear factor 1/A; TGGCA-binding protein;
                     CCAAT-box-binding transcription factor"
                     /calculated_mol_wt=55845
     Region          9..46
                     /region_name="NfI_DNAbd_pre-N"
                     /note="Nuclear factor I protein pre-N-terminus; pfam10524"
                     /db_xref="CDD:463134"
     Region          68..172
                     /region_name="MH1"
                     /note="MH1 domain; pfam03165"
                     /db_xref="CDD:460833"
     Region          189..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09414.2)"
     Region          214..501
                     /region_name="CTF_NFI"
                     /note="CTF/NF-I family transcription modulation region;
                     pfam00859"
                     /db_xref="CDD:459967"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Region          259..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09414.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12857; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Region          352..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09414.2)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12857; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            389
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q02780; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Region          394..402
                     /region_name="9aaTAD.
                     /evidence=ECO:0000250|UniProtKB:Q12857"
                     /note="propagated from UniProtKB/Swiss-Prot (P09414.2)"
     Region          437..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09414.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12857; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q12857; propagated from
                     UniProtKB/Swiss-Prot (P09414.2)"
     CDS             1..509
                     /gene="Nfia"
                     /coded_by="NM_012988.3:358..1887"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25492"
                     /db_xref="RGD:3170"
ORIGIN      
        1 mysplcltqd efhpfieall phvrafaytw fnlqarkrky fkkhekrmsk eeeravkdel
       61 lsekpevkqk wasrllaklr kdirpeyred fvltvtgkkp pccvlsnpdq kgkmrridcl
      121 rqadkvwrld lvmvilfkgi plestdgerl vkspqcsnpg lcvqphhigv svkeldlyla
      181 yfvhaadssq sespsqpsda dikdqpengh lgfqdsfvts gvfsvtelvr vsqtpiaagt
      241 gpnfslsdle sssyysmspg amrrslpsts stsstkrlks vedemdspge epfytgqgrs
      301 pgsgsqssgw hevepgmpsp ttlkkseksg fsspspsqts slgtaftqhh rpvitgpras
      361 phatpstlhf ptspiiqqpg pyfshpairy hpqetlkefv qlvcpdagqq agqvgflnpn
      421 gssqgkvhnp flptpmlppp ppppmarpvp lpmpdtkppt tsteggaasp tsptystpst
      481 spanrfvsvg prdpsfvnip qqtqswylg
//
LOCUS       NP_001020889             290 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001020889 XP_038950610 XP_573946
VERSION     NP_001020889.2
DBSOURCE    REFSEQ: accession NM_001025718.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Mar 17, 2025 this sequence version replaced
            XP_038950610.1, NP_001020889.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.245568.1,
                                           SRR26643296.35991.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..290
                     /product="transcription factor Dp-1 isoform 2"
                     /calculated_mol_wt=32336
     Region          1..73
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(78,82,85..86,88..89,92..93,95..96,99..100,103,
                     106..107,110,113..114,116..117,119..121,124,135..146,148,
                     159..167,169,171,173,179..180,182)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          78..124
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          80..218
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(102,105..106,109,142,151,153,168..175,182)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..290
                     /gene="Tfdp1"
                     /coded_by="NM_001025718.2:416..1288"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
       61 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      121 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      181 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      241 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423495             633 aa            linear   ROD 17-MAR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 11 [Rattus
            norvegicus].
ACCESSION   NP_001423495 XP_006253452
VERSION     NP_001423495.1
DBSOURCE    REFSEQ: accession NM_001436566.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253452.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..633
                     /product="kelch repeat and BTB domain-containing protein
                     11"
                     /note="kelch repeat and BTB (POZ) domain containing 11"
                     /calculated_mol_wt=67718
     Region          144..246
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          237..313
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     Region          341..574
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          356..404
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          496..546
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..633
                     /gene="Kbtbd11"
                     /gene_synonym="RGD1563576"
                     /coded_by="NM_001436566.1:936..2837"
                     /db_xref="GeneID:306617"
                     /db_xref="RGD:1563576"
ORIGIN      
        1 mensvapfvl ypgteprtpg edslplpaee egaaspaqtp cslsaslcfs sgddsppqsr
       61 asaaegseas ppslrsdlrv vetqwdvssa aspespqeca rpeepaspee ppsrreharp
      121 velesldelg epvpvppgvg sehgepdlvi evagrrlrah kavlaarsdy frarasrdvl
      181 rvqgvsftal rllladaysg cmagvrpdnv aevvagarrl qlpgaaqrat eamapqlsld
      241 ncyevlsagk rqrlselrda ayrfmcdhyl evlrepavfg rlsgaerdll lrrrlgtgra
      301 cllaaalgtt gersgsrpqs psgdaesrgd aavycyqaea gewreltrlp egapargcgl
      361 cvlfnylfva ggvapagpdg rarpsdqvfc ynpvtdcwst vrplrqarsq vqllaldghl
      421 yalggeclls verydpradr wtavaplprg afavaheaat cngeiyvsgg slfyrllkyd
      481 prrdewqecp csssrersad mvaldgflyr fdlcgsrgda qaatgsgggv svfryhclak
      541 qwsqcaahlr ppgapaglqp frcvaldgti ycvsragtwr fvpsqdteag sdmgpggsfe
      601 peplgspldv rgvlfpfvln lpekpdrgeq gaa
//
LOCUS       NP_001423508             410 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423508 XP_008769619
VERSION     NP_001423508.1
DBSOURCE    REFSEQ: accession NM_001436579.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_008769619.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.75890.1,
                                           SRR26643297.47641.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..410
                     /product="transcription factor Dp-1 isoform 1"
                     /calculated_mol_wt=45057
     Region          112..193
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(198,202,205..206,208..209,212..213,215..216,
                     219..220,223,226..227,230,233..234,236..237,239..241,244,
                     255..266,268,279..287,289,291,293,299..300,302)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          198..244
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          200..338
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(222,225..226,229,262,271,273,288..295,302)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..410
                     /gene="Tfdp1"
                     /coded_by="NM_001436579.1:297..1529"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 makdasliea ngelkvfidq nlspgkgvvs lvavhpstvn tlgkqllpkt fgqsnvnitq
       61 qvvigtpqrp aaantivvgs phtpnthfvs qnqtsdsspw sagkrnrkge kngkglrhfs
      121 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
      181 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      241 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      301 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      361 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423501             180 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423501 XP_038950528
VERSION     NP_001423501.1
DBSOURCE    REFSEQ: accession NM_001436572.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_038950528.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.361824.1,
                                           SRR26360194.1745055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680453, SAMN16093045
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..180
                     /product="glutamate-rich protein 1 isoform 5"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=20302
     CDS             1..180
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436572.1:703..1245"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msrnkkrkwr aklrlrrkre aglaarasaa sftyepesse eaevegdvgg eeeedpessv
       61 adpaqedtel assradslls flkstqeiyf ydeasredpa vsteaaeell rllesgrlpp
      121 advlildhmk tllllqdter ltsalkmfpe hcmmppdhar iisaffnywi tqilpekrse
//
LOCUS       NP_001423499             189 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423499 XP_038950526
VERSION     NP_001423499.1
DBSOURCE    REFSEQ: accession NM_001436570.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_038950526.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2256693.1,
                                           SRR26360181.1637277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..189
                     /product="glutamate-rich protein 1 isoform 4"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=20795
     Region          <104..>172
                     /region_name="Cnd3"
                     /note="Nuclear condensing complex subunits, C-term domain;
                     pfam12719"
                     /db_xref="CDD:463678"
     CDS             1..189
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436570.1:57..626"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msslrkqvft ekvlkrlfpn vssgqekgtp qtpaldtpsk dstpeavqqk pvrgltagdi
       61 kiqperrlyt vslpppgyip clpeptscad senassggdt eeasredpav steaaeellr
      121 llesgrlppa dvlildhmkt llllqdterl tsalkmfpeh cmmppdhari isaffnywit
      181 qilpekrse
//
LOCUS       NP_001121152             331 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001121152 XP_001075018 XP_225035
VERSION     NP_001121152.1
DBSOURCE    REFSEQ: accession NM_001127680.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before May 26, 2008 this sequence version replaced
            XP_225035.4, XP_001075018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.883663.1,
                                           SRR26360176.1259533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..331
                     /product="glutamate-rich protein 1 isoform 2"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=36824
     Region          <211..>314
                     /region_name="Cnd3"
                     /note="Nuclear condensing complex subunits, C-term domain;
                     pfam12719"
                     /db_xref="CDD:463678"
     CDS             1..331
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001127680.2:57..1052"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msslrkqvft ekvlkrlfpn vssgqekgtp qtpaldtpsk dstpeavqqk pvrgltagdi
       61 kiqperrlyt vslpppgyip clpeptscad senassggdt edpglpdqpk rrrirrhksk
      121 ksikslggvt vrqteletqr ekthpphpda pamsrnkkrk wraklrlrrk reaglaaras
      181 aasftyepes seeaevegdv ggeeeedpes svadpaqedt elassradsl lsflkstqei
      241 yfydasredp avsteaaeel lrllesgrlp padvlildhm ktllllqdte rltsalkmfp
      301 ehcmmppdha riisaffnyw itqilpekrs e
//
LOCUS       NP_001423503              94 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423503
VERSION     NP_001423503.1
DBSOURCE    REFSEQ: accession NM_001436574.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3293924.1,
                                           SRR26360172.395533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..94
                     /product="glutamate-rich protein 1 isoform 7"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=10298
     CDS             1..94
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436574.1:57..341"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msslrkqvft ekvlkrlfpn vssgqekgtp qtpaldtpsk dstpeavqqk pvrgltvrpp
       61 rkempssask lrttikhsil fnrsrsssey aqgc
//
LOCUS       NP_001101872             327 aa            linear   ROD 17-MAR-2025
DEFINITION  ATP-dependent (S)-NAD(P)H-hydrate dehydratase isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001101872 XP_001076079 XP_341469
VERSION     NP_001101872.1
DBSOURCE    REFSEQ: accession NM_001108402.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Van Bergen,N.J., Guo,Y., Rankin,J., Paczia,N., Becker-Kettern,J.,
            Kremer,L.S., Pyle,A., Conrotte,J.F., Ellaway,C., Procopis,P.,
            Prelog,K., Homfray,T., Baptista,J., Baple,E., Wakeling,M.,
            Massey,S., Kay,D.P., Shukla,A., Girisha,K.M., Lewis,L.E.S.,
            Santra,S., Power,R., Daubeney,P., Montoya,J., Ruiz-Pesini,E.,
            Kovacs-Nagy,R., Pritsch,M., Ahting,U., Thorburn,D.R., Prokisch,H.,
            Taylor,R.W., Christodoulou,J., Linster,C.L., Ellard,S. and
            Hakonarson,H.
  TITLE     NAD(P)HX dehydratase (NAXD) deficiency: a novel neurodegenerative
            disorder exacerbated by febrile illnesses
  JOURNAL   Brain 142 (1), 50-58 (2019)
   PUBMED   30576410
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Marbaix,A.Y., Tyteca,D., Niehaus,T.D., Hanson,A.D., Linster,C.L.
            and Van Schaftingen,E.
  TITLE     Occurrence and subcellular distribution of the NADPHX repair system
            in mammals
  JOURNAL   Biochem J 460 (1), 49-58 (2014)
   PUBMED   24611804
  REMARK    GeneRIF: The human, mouse, and rat Carkd genes contain a first exon
            with two alternative 3' splice sites and two putative initiator ATG
            codons; the second exon also comprises a highly conserved ATG
            codon.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_341469.2, XP_001076079.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ225763.1, SRR26360181.3174597.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..327
                     /product="ATP-dependent (S)-NAD(P)H-hydrate dehydratase
                     isoform 2"
                     /EC_number="4.2.1.93"
                     /note="carbohydrate kinase domain containing;
                     ATP-dependent NAD(P)HX dehydratase; carbohydrate kinase
                     domain-containing protein; ATP-dependent
                     (S)-NAD(P)H-hydrate dehydratase"
                     /calculated_mol_wt=34831
     Region          49..316
                     /region_name="YXKO-related"
                     /note="B.subtilis YXKO protein of unknown function and
                     related proteins. Based on the conservation of the ATP
                     binding site, the substrate binding site and the
                     Mg2+binding site and structural homology this group is a
                     member of the ribokinase-like superfamily; cd01171"
                     /db_xref="CDD:238576"
     Site            order(71,252,255)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238576"
     Site            order(186,226,253..254,257,294)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238576"
     CDS             1..327
                     /gene="Naxd"
                     /gene_synonym="Carkd; RGD1562691"
                     /coded_by="NM_001108402.2:20..1003"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361185"
                     /db_xref="RGD:1562691"
ORIGIN      
        1 mgircvaira cggvlqrals lhtahatkdm dnlfqlvrni vpaltskkhk gqdgrigivg
       61 gcqeytgapy fagisalkvg adlthvfcar eaapviksys pelivhpvld ssdaveevek
      121 wlprlhalvv gpglgrddll lnnvrgiles tkardipvvi dadglwliaq rpalvhgyqk
      181 avltpnhvef srlwdavlss pmdtsnhsgs vlklsqalgn itivqkgeqd lisngqqvlv
      241 cnqegssrrc ggqgdllsgs lgvmahwalr agpektngss pllvaawgac tltrecnhla
      301 fqkygrsttt tdmiaevgaa fsklftt
//
LOCUS       NP_001423498             283 aa            linear   ROD 17-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423498
VERSION     NP_001423498.1
DBSOURCE    REFSEQ: accession NM_001436569.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.18718.1,
                                           SRR26360194.1570232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..283
                     /product="glutamate-rich protein 1 isoform 3"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=31662
     Region          <162..>266
                     /region_name="Cnd3"
                     /note="Nuclear condensing complex subunits, C-term domain;
                     pfam12719"
                     /db_xref="CDD:463678"
     CDS             1..283
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436569.1:57..908"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msslrkqagd ikiqperrly tvslpppgyi pclpeptsca dsenassggd tedpglpdqp
       61 krrrirrhks kksikslggv tvrqteletq rekthpphpd apamsrnkkr kwraklrlrr
      121 kreaglaara saasftyepe sseeaevegd vggeeeedpe ssvadpaqed telassrads
      181 llsflkstqe iyfydeasre dpavsteaae ellrllesgr lppadvlild hmktllllqd
      241 terltsalkm fpehcmmppd hariisaffn ywitqilpek rse
//
LOCUS       NP_001423509             290 aa            linear   ROD 17-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423509 XP_063131643
VERSION     NP_001423509.1
DBSOURCE    REFSEQ: accession NM_001436580.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_063131643.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099767.1, SRR22582419.1898746.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..290
                     /product="transcription factor Dp-1 isoform 2"
                     /calculated_mol_wt=32336
     Region          1..73
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(78,82,85..86,88..89,92..93,95..96,99..100,103,
                     106..107,110,113..114,116..117,119..121,124,135..146,148,
                     159..167,169,171,173,179..180,182)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          78..124
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          80..218
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(102,105..106,109,142,151,153,168..175,182)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..290
                     /gene="Tfdp1"
                     /coded_by="NM_001436580.1:647..1519"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
       61 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      121 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      181 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      241 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423523             230 aa            linear   ROD 18-MAR-2025
DEFINITION  clathrin light chain A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423523 XP_006238167
VERSION     NP_001423523.1
DBSOURCE    REFSEQ: accession NM_001436594.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Li,H., Alavian,K.N., Lazrove,E., Mehta,N., Jones,A., Zhang,P.,
            Licznerski,P., Graham,M., Uo,T., Guo,J., Rahner,C., Duman,R.S.,
            Morrison,R.S. and Jonas,E.A.
  TITLE     A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
            during endocytosis
  JOURNAL   Nat Cell Biol 15 (7), 773-785 (2013)
   PUBMED   23792689
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Bu,W., Lim,K.B., Yu,Y.H., Chou,A.M., Sudhaharan,T. and Ahmed,S.
  TITLE     Cdc42 interaction with N-WASP and Toca-1 regulates membrane
            tubulation, vesicle formation and vesicle motility: implications
            for endocytosis
  JOURNAL   PLoS One 5 (8), e12153 (2010)
   PUBMED   20730103
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Mettlen,M., Loerke,D., Yarar,D., Danuser,G. and Schmid,S.L.
  TITLE     Cargo- and adaptor-specific mechanisms regulate clathrin-mediated
            endocytosis
  JOURNAL   J Cell Biol 188 (6), 919-933 (2010)
   PUBMED   20231386
  REMARK    GeneRIF: The results underscore the highly dynamic and
            cargo-responsive nature of CCP assembly and suggest that the
            observed heterogeneity is, in part, related to compositional
            differences (e.g., cargo and adaptors) between CCPs.
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Drake,M.T., Downs,M.A. and Traub,L.M.
  TITLE     Epsin binds to clathrin by associating directly with the
            clathrin-terminal domain. Evidence for cooperative binding through
            two discrete sites
  JOURNAL   J Biol Chem 275 (9), 6479-6489 (2000)
   PUBMED   10692452
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Saito,Y., Tsubuki,S., Ito,H., Ohmi-Imajo,S. and Kawashima,S.
  TITLE     Possible involvement of clathrin in neuritogenesis induced by a
            protease inhibitor (benzyloxycarbonyl-Leu-Leu-Leu-aldehyde) in PC12
            cells
  JOURNAL   J Biochem 112 (4), 448-455 (1992)
   PUBMED   1490999
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Maycox,P.R., Link,E., Reetz,A., Morris,S.A. and Jahn,R.
  TITLE     Clathrin-coated vesicles in nervous tissue are involved primarily
            in synaptic vesicle recycling
  JOURNAL   J Cell Biol 118 (6), 1379-1388 (1992)
   PUBMED   1325974
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Kirchhausen,T., Scarmato,P., Harrison,S.C., Monroe,J.J., Chow,E.P.,
            Mattaliano,R.J., Ramachandran,K.L., Smart,J.E., Ahn,A.H. and
            Brosius,J.
  TITLE     Clathrin light chains LCA and LCB are similar, polymorphic, and
            share repeated heptad motifs
  JOURNAL   Science 236 (4799), 320-324 (1987)
   PUBMED   3563513
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Brodsky,F.M.
  TITLE     Clathrin structure characterized with monoclonal antibodies. II.
            Identification of in vivo forms of clathrin
  JOURNAL   J Cell Biol 101 (6), 2055-2062 (1985)
   PUBMED   4066749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238167.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.708277.1,
                                           SRR22399489.2969745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..230
                     /product="clathrin light chain A isoform 4"
                     /note="clathrin, light polypeptide (Lca); clathrin, light
                     chain (Lca); lca"
                     /calculated_mol_wt=24766
     Region          22..230
                     /region_name="Clathrin_lg_ch"
                     /note="Clathrin light chain; pfam01086"
                     /db_xref="CDD:460056"
     CDS             1..230
                     /gene="Clta"
                     /gene_synonym="LCA1; LCA2; LCA3"
                     /coded_by="NM_001436594.1:124..816"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:83800"
                     /db_xref="RGD:70919"
ORIGIN      
        1 maeldpfgap agapggpalg ngvagageed paaaflaqqe seiagiende afaildggap
       61 gpqahgeppg gpdavdgvmn geyyqesngp tdsyaaisev drlqsepesi rkwreeqter
      121 lealdansrk qeaewkekav keleewyarq deqlqktkas nstninhpcy sleqaaeeaf
      181 vndidesspg tewervarlc dfnpksskqa kdvsrmrsvl islkqaplvh
//
LOCUS       NP_001423530             251 aa            linear   ROD 18-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423530
VERSION     NP_001423530.1
DBSOURCE    REFSEQ: accession NM_001436601.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.28164.1,
                                           SRR26643291.15443.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..251
                     /product="single-stranded DNA-binding protein 3 isoform d"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=25382
     Region          <12..228
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..251
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_001436601.1:181..936"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mpggpippgf fqpfmsprya ggprppirmg nqppggvpgt qpllpnsmdp trqqghpnmg
       61 gsmqrmnppr gmgpmgpgpq nygsgmrppp nslgpampgi nmgpgagrpw pnpnsansip
      121 ysssspgtyv gppggggppg tpimpspads tnssdniytm inpvppggsr snfpmgpgsd
      181 gpmggmggme phhmngslgs gdidglpkns pnnisgisnp pgtprddgel ggnflhsfqn
      241 dnyspsmtms v
//
LOCUS       NP_001423544             708 aa            linear   ROD 18-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423544
VERSION     NP_001423544.1
DBSOURCE    REFSEQ: accession NM_001436615.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2478537.1,
                                           SRR26643293.75530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..708
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 4"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=79849
     Region          <3..97
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          140..333
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          354..428
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          432..575
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..708
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436615.1:314..2440"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 maylitinen phfihlkkqs fitstavsyt ydrqdvrhsq slsslkncny ngyvagfpns
       61 ivsltvcsgl rgmiqfenvs ygiepvetls gfihviyent nqqakipdlg enqtyswsde
      121 ldyqfrsnmk ksgfavlrpr yiktdivvdk klfdymgsdt rvvlqkviqi igfintmfsk
      181 lkltvlinsv eiwskenrid fpeapenllv qflhwkhkyr pqhisyllaf vehpastgal
      241 ypgnlckpiy gaaialypkg lslesysviv lqllsigigl tydnadschc tgdvclmtpk
      301 aiysggvkdf stcslddfky lstqdleclq dlpmerqkkk psrprricgn gilemneqcd
      361 cgtlkncthk kccdpmscrl kskavcgsge ccgqdckvkp vnvlcrkskn ecdfeeycng
      421 ndaycvpdtf arngqycdsg qafcysglcm tsnnqcmnll gkyvrgasfa cyeefnsrnd
      481 rfgncirkfc sfenslcgkl vctwpfkrll mkdnmsaayg qirddlcisl ykggrplktt
      541 lstysdmser detfvkdgti cgpdmfclet qcketrflvd fqqcntsrdc ndhgvcnnfn
      601 hchcdkgynp pycesvkgqf gsiddghkyy idegksakqq nrgihpkqql qlilyitlpl
      661 imiisavfik qsklsrlcgr ersegtscit edsvsntkmt tnegstlh
//
LOCUS       NP_001423554             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423554 XP_006237781
VERSION     NP_001423554.1
DBSOURCE    REFSEQ: accession NM_001436625.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237781.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.14495.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436625.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001423555             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423555
VERSION     NP_001423555.1
DBSOURCE    REFSEQ: accession NM_001436626.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20315.1,
                                           SRR26643296.14499.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436626.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001423548            1838 aa            linear   ROD 18-MAR-2025
DEFINITION  CDK5 regulatory subunit-associated protein 2 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423548 XP_038965275
VERSION     NP_001423548.1
DBSOURCE    REFSEQ: accession NM_001436619.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1838)
  AUTHORS   Bouguenina,H., Salaun,D., Mangon,A., Muller,L., Baudelet,E.,
            Camoin,L., Tachibana,T., Cianferani,S., Audebert,S.,
            Verdier-Pinard,P. and Badache,A.
  TITLE     EB1-binding-myomegalin protein complex promotes centrosomal
            microtubules functions
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10687-E10696 (2017)
   PUBMED   29162697
REFERENCE   2  (residues 1 to 1838)
  AUTHORS   Gao,F.J., Shi,L., Hines,T., Hebbar,S., Neufeld,K.L. and Smith,D.S.
  TITLE     Insulin signaling regulates a functional interaction between
            adenomatous polyposis coli and cytoplasmic dynein
  JOURNAL   Mol Biol Cell 28 (5), 587-599 (2017)
   PUBMED   28057765
REFERENCE   3  (residues 1 to 1838)
  AUTHORS   Park,J.S., Lee,M.K., Kang,S., Jin,Y., Fu,S., Rosales,J.L. and
            Lee,K.Y.
  TITLE     Species-Specific Expression of Full-Length and Alternatively
            Spliced Variant Forms of CDK5RAP2
  JOURNAL   PLoS One 10 (11), e0142577 (2015)
   PUBMED   26550838
  REMARK    GeneRIF: mouse expresses only one form of CDK5RAP2 that is
            equivalent to the human and rat alternatively spliced variant forms
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1838)
  AUTHORS   Mori,Y., Inoue,Y., Tanaka,S., Doda,S., Yamanaka,S., Fukuchi,H. and
            Terada,Y.
  TITLE     Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein,
            Binds to CDK5RAP2 and Regulates Microtubule Stability
  JOURNAL   PLoS One 10 (10), e0140968 (2015)
   PUBMED   26485573
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1838)
  AUTHORS   Yigit,G., Brown,K.E., Kayserili,H., Pohl,E., Caliebe,A.,
            Zahnleiter,D., Rosser,E., Bogershausen,N., Uyguner,Z.O.,
            Altunoglu,U., Nurnberg,G., Nurnberg,P., Rauch,A., Li,Y., Thiel,C.T.
            and Wollnik,B.
  TITLE     Mutations in CDK5RAP2 cause Seckel syndrome
  JOURNAL   Mol Genet Genomic Med 3 (5), 467-480 (2015)
   PUBMED   26436113
REFERENCE   6  (residues 1 to 1838)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   7  (residues 1 to 1838)
  AUTHORS   Hassan,M.J., Khurshid,M., Azeem,Z., John,P., Ali,G., Chishti,M.S.
            and Ahmad,W.
  TITLE     Previously described sequence variant in CDK5RAP2 gene in a
            Pakistani family with autosomal recessive primary microcephaly
  JOURNAL   BMC Med Genet 8, 58 (2007)
   PUBMED   17764569
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1838)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
REFERENCE   9  (residues 1 to 1838)
  AUTHORS   Wang,X., Ching,Y.P., Lam,W.H., Qi,Z., Zhang,M. and Wang,J.H.
  TITLE     Identification of a common protein association region in the
            neuronal Cdk5 activator
  JOURNAL   J Biol Chem 275 (41), 31763-31769 (2000)
   PUBMED   10915792
REFERENCE   10 (residues 1 to 1838)
  AUTHORS   Ching,Y.P., Qi,Z. and Wang,J.H.
  TITLE     Cloning of three novel neuronal Cdk5 activator binding proteins
  JOURNAL   Gene 242 (1-2), 285-294 (2000)
   PUBMED   10721722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038965275.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MF541099.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..1838
                     /product="CDK5 regulatory subunit-associated protein 2
                     isoform 3"
                     /note="CDK5 activator-binding protein C48"
                     /calculated_mol_wt=207875
     Region          61..129
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          146..>471
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <1357..>1583
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1838
                     /gene="Cdk5rap2"
                     /coded_by="NM_001436619.1:169..5685"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:286919"
                     /db_xref="RGD:708451"
ORIGIN      
        1 mmdsgmeedv tlpgtlsgcs glhpvlpsdl dvisdttglg ngvlpimsee kvsptrarnm
       61 kdfenqitel kkenfnlklr iyfleeriqq efagptehiy kknielkvev eslkrelqer
      121 dqllvkaska veslaegggs eiqrvkedar kkvqqveell tkrihlleed vkaaqaelek
      181 afagteteka lrlsleskls amkkmqegdl emtlaleekd rlieelklsl kskealiqcl
      241 keeksqmasp denvssgelr glsatlreek erdaeerqke rnhfeeriqa lqedlreker
      301 eiatekknsl krdkaiqglt malkskekee senceaalae keallaklhs envtkntenh
      361 rllrnvkkvt qelndlkkek lrlerdleea hregnrgart ihdlrnevek lrkevcerek
      421 avekhykslp gessskfhsq eqvvkgltes asqedlllqk snekdleaiq qncylmtaee
      481 lkfgsdglit ekcsqqspds klifskekqq seyegltgdl kteqnvyahl aknlqdtdsk
      541 lqaelkrvla lrkqleqdvl ayrnlqtalq eqlseirkre eepfsfysdq tsylsiclee
      601 hsqfqlehfs qeeikkkvid liqlvkdlha dnqhlkktif discmgvqgn drlestkqae
      661 imedyaeggg kdgyvrhmds nildhdgaht pdtsedhsle dellsllatf fskkatpsle
      721 srpdllkalg alllericla eqgspgdhsd skaekaleqv avrlrdelgh sclansfsks
      781 hselksprgt wlvktgdeak velksvsvqt mtiedstrgf kperkreawa gkpeeavfst
      841 elesealgem pglqathlsf psaidkddqk tglliqlktp ellenlynlp asqevvaqlq
      901 gqvlelqkel keykirnkql ldklilaeam megmavpnst pvnvpaaqav vrtafqgkpg
      961 eqeghetths agrdkevdsd qytsfeidse icppddlall packenledf lgppsiatyl
     1021 dsksqlsvkv svvgtdqsen inlpddteal kqkihdlqte legyrniivq lqkhsqcsea
     1081 iitvlcgteg aqdglnkpkg hideeemtfs slhqvryvkh mkilrpltpe iidgkmlesl
     1141 kqqlveqeqe lqkeqdlnle lfgeihnlqn kfrdlspsry dslvqsqare lslqrqqikd
     1201 shdicvvchq hmstmikafe ellqasdvds cvaegfreql tqcaglleql eklflhgksa
     1261 rvephtqtel lrrlrteedn lpyqhllpes pepsashals ddemseksfl srepkpdset
     1321 ekyptiasrf pqdllmehiq eirtlrkhle esiktneklr kqlerqgcet dqgstnvsay
     1381 sselhnslts eiqflrkqne alstmlekgs kekqkenekl reslarktes lehlqleyas
     1441 vreenerlrr disekerqnq qltqevcssl qelsrvqeea ksrqqlllqk dellqslqme
     1501 lkvyeklaee hqklqqesrg eacgggqkgq dpfsnlhgll keiqvlrdqa ersiqtnntl
     1561 ksklekqlsq gskqaqegal tlavqalsvt ewslqldkhd vnkcpeasdn sfdlfestqa
     1621 mapksasetp vlsgtdvdsl scdstssats pscmpclvag rhlwasksgh hmlcliedyd
     1681 alykqiswgq tllakmdiqt qealsptsqk lgpkasfsvp lskflssmnt aklilekasr
     1741 llklfwrvsv ptngqcslhc dqigemkaei tklhkklfeq ekklqntakl lqqskhqeki
     1801 ifdqlvithq vlrkargnle lrpraahpgt sspsrpgs
//
LOCUS       NP_001423570             499 aa            linear   ROD 18-MAR-2025
DEFINITION  zinc finger protein PLAG1 isoform a [Rattus norvegicus].
ACCESSION   NP_001423570 XP_063143345
VERSION     NP_001423570.1
DBSOURCE    REFSEQ: accession NM_001436641.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gu,Q. and Wei,H.F.
  TITLE     PLAG1 Promotes High Glucose-Induced Angiogenesis and Migration of
            Retinal Endothelial Cells by Regulating the Wnt/beta-Catenin
            Signalling Pathway
  JOURNAL   Folia Biol (Praha) 68 (1), 25-32 (2022)
   PUBMED   36201855
  REMARK    GeneRIF: PLAG1 Promotes High Glucose-Induced Angiogenesis and
            Migration of Retinal Endothelial Cells by Regulating the
            Wnt/beta-Catenin Signalling Pathway.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hide,T., Takezaki,T., Nakatani,Y., Nakamura,H., Kuratsu,J. and
            Kondo,T.
  TITLE     Sox11 prevents tumorigenesis of glioma-initiating cells by inducing
            neuronal differentiation
  JOURNAL   Cancer Res 69 (20), 7953-7959 (2009)
   PUBMED   19808959
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hensen,K., Braem,C., Declercq,J., Van Dyck,F., Dewerchin,M.,
            Fiette,L., Denef,C. and Van de Ven,W.J.
  TITLE     Targeted disruption of the murine Plag1 proto-oncogene causes
            growth retardation and reduced fertility
  JOURNAL   Dev Growth Differ 46 (5), 459-470 (2004)
   PUBMED   15606491
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Voz,M.L., Agten,N.S., Van de Ven,W.J. and Kas,K.
  TITLE     PLAG1, the main translocation target in pleomorphic adenoma of the
            salivary glands, is a positive regulator of IGF-II
  JOURNAL   Cancer Res 60 (1), 106-113 (2000)
   PUBMED   10646861
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Astrom,A.K., Voz,M.L., Kas,K., Roijer,E., Wedell,B., Mandahl,N.,
            Van de Ven,W., Mark,J. and Stenman,G.
  TITLE     Conserved mechanism of PLAG1 activation in salivary gland tumors
            with and without chromosome 8q12 abnormalities: identification of
            SII as a new fusion partner gene
  JOURNAL   Cancer Res 59 (4), 918-923 (1999)
   PUBMED   10029085
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063143345.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.213675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..499
                     /product="zinc finger protein PLAG1 isoform a"
                     /note="zinc finger protein PLAG1; pleiomorphic adenoma
                     gene 1 protein"
                     /calculated_mol_wt=55509
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          2..84
                     /region_name="Interaction with KPNA2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          22..25
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          36..56
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          41..242
                     /region_name="Decreased nuclear import with localization
                     in the nucleus but also in the cytoplasm.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Site            order(41,43,45,47..48,51..52,55,71,73,77..78,81..82,85,99,
                     101,103,105..106,109..110,113)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <58..139
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          64..86
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          79..101
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          94..114
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          123..143
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(157,159,161,163..164,167..168,171,192,194,198..199,
                     202..203,206,220,222,224,226..227,230..231)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          215..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..499
                     /region_name="Activates transcription, Inhibition of
                     nuclear import due to lack of NLS and KPNA2 interaction.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          243..383
                     /region_name="Repression domain, contains 3 sumoylation
                     motifs and massively decrease transcription activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          364..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          384..499
                     /region_name="Massively activates transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     CDS             1..499
                     /gene="Plag1"
                     /coded_by="NM_001436641.1:613..2112"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:297804"
                     /db_xref="RGD:1305286"
ORIGIN      
        1 matvipgdls evrdtqkaps gkrkrgeskp rknfpcqlcd kafnsveklk vhsfshtger
       61 pykcthqdct kafvskyklq rhmathspek thkcnycekm fhrkdhlknh lhthdpnket
      121 fkceecgksy ntklgfkrhl alhaatsgdl tckvclqtfe stgvllehlk shagkssggv
      181 kekkhqcehc errfytrkdv rrhmvvhtgr kdflcqycaq rfgrkdhltr hmkkshnqel
      241 lkvktepvdf ldpftcnmsv pikdellpvm slpssellsk pftntlqlnl yntpfqsmqs
      301 sgsthqmitt lplgmtcpid mdtvhpshhl afkcpfssts yaisipekeq plkgeiesyl
      361 melqggapss sqdsqasssk lglepqsgsp ddgagdlsls kssisisdpl ntpaldfsql
      421 fnfiplngpp ynplsvgslg msysqdeahs svsqlptqtq dlqdpantvg lgslhslsaa
      481 ftsslssstt lprfhqafq
//
LOCUS       NP_001423563             506 aa            linear   ROD 18-MAR-2025
DEFINITION  myb-related protein A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423563
VERSION     NP_001423563.1
DBSOURCE    REFSEQ: accession NM_001436634.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Zhang,D., Xie,D., Lin,X., Ma,L., Chen,J., Zhang,D., Wang,Y.,
            Duo,S., Feng,Y., Zheng,C., Jiang,B., Ning,Y. and Han,C.
  TITLE     The transcription factor SOX30 is a key regulator of mouse
            spermiogenesis
  JOURNAL   Development 145 (11) (2018)
   PUBMED   29848638
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Li,X.Z., Roy,C.K., Dong,X., Bolcun-Filas,E., Wang,J., Han,B.W.,
            Xu,J., Moore,M.J., Schimenti,J.C., Weng,Z. and Zamore,P.D.
  TITLE     An ancient transcription factor initiates the burst of piRNA
            production during early meiosis in mouse testes
  JOURNAL   Mol Cell 50 (1), 67-81 (2013)
   PUBMED   23523368
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Bolcun-Filas,E., Bannister,L.A., Barash,A., Schimenti,K.J.,
            Hartford,S.A., Eppig,J.J., Handel,M.A., Shen,L. and Schimenti,J.C.
  TITLE     A-MYB (MYBL1) transcription factor is a master regulator of male
            meiosis
  JOURNAL   Development 138 (15), 3319-3330 (2011)
   PUBMED   21750041
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Ma,X.P. and Calabretta,B.
  TITLE     DNA binding and transactivation activity of A-myb, a c-myb-related
            gene
  JOURNAL   Cancer Res 54 (24), 6512-6516 (1994)
   PUBMED   7987850
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.3324022.1,
                                           SRR21887622.3324023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..506
                     /product="myb-related protein A isoform 4"
                     /note="myb-related protein A; myeloblastosis oncogene-like
                     1"
                     /calculated_mol_wt=57703
     Region          38..98
                     /region_name="Myb_DNA-bind_6"
                     /note="Myb-like DNA-binding domain; pfam13921"
                     /db_xref="CDD:372817"
     Site            order(38,68..69,71..72,74..76,78..80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          84..>192
                     /region_name="PLN03091"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:215570"
     Region          240..285
                     /region_name="LMSTEN"
                     /note="LMSTEN motif; pfam07988"
                     /db_xref="CDD:462332"
     CDS             1..506
                     /gene="Mybl1"
                     /coded_by="NM_001436634.1:372..1892"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:297783"
                     /db_xref="RGD:1306940"
ORIGIN      
        1 makrsrsede dddlqyadhd yevpqqkglk klwnrvkwtr deddklkklv eqhgtddwtl
       61 iashlqnrsd fqcqhrwqkv lnpelikgpw tkeedqrvie lvqkygpkrw sliakhlkgr
      121 igkqcrerwh nhlnpevkks swteeedrii yeahkrlgnr waeiakllpg rtdnsiknhw
      181 nstmrrkveq egylqdgiks ersssklqhk pcatmdhlqt qnqfyipvqi pgyqyvspdg
      241 ncvehvqtsa fiqqpfvded pdkekkikel elllmsaene vrrkrlppqp gsfsswsgsf
      301 lmddsmsntl nnleehttef ysmdenqtvs aqqnsptkfl aveanavlss lqtipefaet
      361 leliesdpva wsdvtsfdls daaaspvkst pvklmriqhn egamecqfnv slvlegkkns
      421 cnggdseaip laspnvvkfs tpptilrkkk rlrvgqsags elgegslseg nnaalkhtpv
      481 ktlpfspsqv lvlyvcqcwq atltdl
//
LOCUS       NP_001423539             270 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform b [Rattus norvegicus].
ACCESSION   NP_001423539
VERSION     NP_001423539.1
DBSOURCE    REFSEQ: accession NM_001436610.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.611775.1,
                                           SRR26360190.1326755.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..270
                     /product="aprataxin isoform b"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=30530
     Region          <1..42
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..268
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="Aptx"
                     /coded_by="NM_001436610.1:368..1180"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mgvnptside vvigkdremk llpgqvlhmv nelypymvef eevaespnvt qrkrkrpdcd
       61 sqemeaeaga spsqcsvspk tgkhgaakee slghwsqglk ismkdpkmqv ykddqvvvik
      121 dkypkarhhw lvlpwasiss lkvvtsehle llkhmhavge kviadftgss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa vikmvqeagr vtvkdgtcel
      241 lklplrchec qqllpsipql kehlrkhwgg
//
LOCUS       NP_683687                329 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform a [Rattus norvegicus].
ACCESSION   NP_683687
VERSION     NP_683687.1
DBSOURCE    REFSEQ: accession NM_148889.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078716.1, SRR26360194.1197592.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..329
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=37589
     Region          1..95
                     /region_name="Interactions with ADPRT/PARP1 and NCL.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          2..101
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(27..28,40..41,43,63..64)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          106..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          111..115
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQC5; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          151..252
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            161
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          180..184
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            238
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          242..243
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            order(245,247,249..251)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Region          245..249
                     /region_name="Histidine triad motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Site            249
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            264
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          270..327
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..329
                     /gene="Aptx"
                     /coded_by="NM_148889.3:386..1375"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mrvcwlvrqd cwhqriklph leavvigrsp etkitdkkcs rqqvqlkaec nkryvnvkqm
       61 gvnptsidev vigkdremkl lpgqvlhmvn elypymvefe evaespnvtq rkrkrpdcds
      121 qemeaeagas psqcsvspkt gkhgaakees lghwsqglki smkdpkmqvy kddqvvvikd
      181 kypkarhhwl vlpwasissl kvvtsehlel lkhmhavgek viadftgssk lrfrlgyhai
      241 psmshvhlhv isqdfdspcl knkkhwnsfn teyflesqav ikmvqeagrv tvkdgtcell
      301 klplrchecq qllpsipqlk ehlrkhwgg
//
LOCUS       NP_001423560             682 aa            linear   ROD 18-MAR-2025
DEFINITION  phospholipase DDHD2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423560 XP_063131790
VERSION     NP_001423560.1
DBSOURCE    REFSEQ: accession NM_001436631.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Araki,M., Ohshima,N., Aso,C., Konishi,A., Obinata,H., Tatei,K. and
            Izumi,T.
  TITLE     Enzymatic characterization of recombinant rat DDHD2: a soluble
            diacylglycerol lipase
  JOURNAL   J Biochem 160 (5), 269-279 (2016)
   PUBMED   27198176
  REMARK    GeneRIF: These results therefore support the idea that DDHD2
            functions as a DG lipase in vivo and produces 2-AG.
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Aso,C., Araki,M., Ohshima,N., Tatei,K., Hirano,T., Obinata,H.,
            Kishi,M., Kishimoto,K., Konishi,A., Goto,F., Sugimoto,H. and
            Izumi,T.
  TITLE     Protein purification and cloning of diacylglycerol lipase from rat
            brain
  JOURNAL   J Biochem 159 (6), 585-597 (2016)
   PUBMED   26790472
  REMARK    GeneRIF: DG lipase activity in the soluble fraction of rat brain is
            derived from DDHD2. DDHD2 is distributed widely in the rat brain.
            Immunohistochemical analysis revealed that DDHD2 is expressed in
            hippocampal neurons, but not in glia.
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Inloes,J.M., Hsu,K.L., Dix,M.M., Viader,A., Masuda,K., Takei,T.,
            Wood,M.R. and Cravatt,B.F.
  TITLE     The hereditary spastic paraplegia-related enzyme DDHD2 is a
            principal brain triglyceride lipase
  JOURNAL   Proc Natl Acad Sci U S A 111 (41), 14924-14929 (2014)
   PUBMED   25267624
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063131790.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.47312.1,
                                           SRR26360176.801048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..682
                     /product="phospholipase DDHD2 isoform 2"
                     /note="phospholipase DDHD2"
                     /calculated_mol_wt=77613
     Region          43..112
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          379..447
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          467..670
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..682
                     /gene="Ddhd2"
                     /coded_by="NM_001436631.1:144..2192"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:680971"
                     /db_xref="RGD:1585818"
ORIGIN      
        1 mssgesyqeq lsqsdpspsp nssssfelld mdvgssyepv sphwfyckvi dskelwipfn
       61 sedsqqleea hgsgkdcner vvptdggryd vhlgermrya vywdelpsev rrctwfykgd
      121 kdnkyvpyse sfsqvledty mlavtldewk kklespnrei ivlhnpklmv hyqpitgsde
      181 wgststeqgr prsvkrgves ipvdihcgep lqidhlvfvv hgigpacdlr frsivqcvnd
      241 frsvslnllq thfkkaqenq qigrveflpv nwhsplhstg vdidlqritl psinrlrhft
      301 ndtildvffy nsptycqtiv dtvasemnri ytlflqrnpd fkggvsiagh slgslilfdi
      361 ltnqkdsigd idsekgslst aedlgdvstl eeelkklqls efvtvfekek vdrealalct
      421 drdlqemgip lgprkkilnh fsatkssvgi nrptmsasev svkyprlnyk peiffafgsp
      481 igmfltvrgl rridpnykfp tckgffniyh pfdpvayrie pmvvpgvefe pmliphhkgr
      541 krmhlelreg ltrmsmdlkn nllgslrmaw ksftrapypa lqasemaedt eaesepssek
      601 psdanteepp vevkeeapin vgmlnggqri dyvlqekpie sfneylfalq shlcywesed
      661 tvllvlkeiy qtqgifldqp lq
//
LOCUS       NP_001423576             530 aa            linear   ROD 18-MAR-2025
DEFINITION  chondroitin sulfate N-acetylgalactosaminyltransferase 1 [Rattus
            norvegicus].
ACCESSION   NP_001423576 XP_038950423
VERSION     NP_001423576.1
DBSOURCE    REFSEQ: accession NM_001436647.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Sato,T., Kudo,T., Ikehara,Y., Ogawa,H., Hirano,T., Kiyohara,K.,
            Hagiwara,K., Togayachi,A., Ema,M., Takahashi,S., Kimata,K.,
            Watanabe,H. and Narimatsu,H.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is
            necessary for normal endochondral ossification and aggrecan
            metabolism
  JOURNAL   J Biol Chem 286 (7), 5803-5812 (2011)
   PUBMED   21148564
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Watanabe,Y., Takeuchi,K., Higa Onaga,S., Sato,M., Tsujita,M.,
            Abe,M., Natsume,R., Li,M., Furuichi,T., Saeki,M., Izumikawa,T.,
            Hasegawa,A., Yokoyama,M., Ikegawa,S., Sakimura,K., Amizuka,N.,
            Kitagawa,H. and Igarashi,M.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required
            for normal cartilage development
  JOURNAL   Biochem J 432 (1), 47-55 (2010)
   PUBMED   20812917
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Gotoh,M., Sato,T., Akashima,T., Iwasaki,H., Kameyama,A.,
            Mochizuki,H., Yada,T., Inaba,N., Zhang,Y., Kikuchi,N., Kwon,Y.D.,
            Togayachi,A., Kudo,T., Nishihara,S., Watanabe,H., Kimata,K. and
            Narimatsu,H.
  TITLE     Enzymatic synthesis of chondroitin with a novel chondroitin sulfate
            N-acetylgalactosaminyltransferase that transfers
            N-acetylgalactosamine to glucuronic acid in initiation and
            elongation of chondroitin sulfate synthesis
  JOURNAL   J Biol Chem 277 (41), 38189-38196 (2002)
   PUBMED   12163485
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Kitagawa,H., Uyama,T. and Sugahara,K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase
  JOURNAL   J Biol Chem 276 (42), 38721-38726 (2001)
   PUBMED   11514575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038950423.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.47978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..530
                     /product="chondroitin sulfate
                     N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.174"
                     /note="chondroitin beta1,4
                     N-acetylgalactosaminyltransferase"
                     /calculated_mol_wt=60770
     Region          68..505
                     /region_name="CHGN"
                     /note="Chondroitin N-acetylgalactosaminyltransferase;
                     pfam05679"
                     /db_xref="CDD:461712"
     CDS             1..530
                     /gene="Csgalnact1"
                     /gene_synonym="Chgn; RGD1307618"
                     /coded_by="NM_001436647.1:573..2165"
                     /db_xref="GeneID:306375"
                     /db_xref="RGD:1307618"
ORIGIN      
        1 mvrrglvgwi srvvillvll ccaisvlyml actpkgdqeq lglprangpt gkdgyqavlq
       61 ereeqhrnyv nslkrqiaql kdelqarseq lrsgqdqasd atslrsgwdp epkaqadila
      121 flrgqvdkae vhagvklate yaavpfdsft lqkvyqletg ltrhpeekpv rkdkrdelve
      181 aiesalesln spvessphqr pytaadfieg iyrterdkgt lyeltfkgdh khefqrlvlf
      241 rpfgpimkvk keklnmantl invivplarr vdkfrhfmqn fremciqqdg rvhltvvyfg
      301 keemnevkgi lentskaanf rnftfiqlng efsrgkgldv garfwkgsnv vlffcdvdiy
      361 ftseflntcr lntqpgkkvf ypvlfsqynp giiyghhdav paleqqlvik ketgfwrdfg
      421 fgmtcqyrsd finiggfdld ikgwggedvh lyrkylhsnl ivirtpvrgl fhlwhekhcm
      481 deltpeqyrm cmqskamnea shgqlgmlvf rheieahlrk qklkasskkt
//
LOCUS       NP_001423545             636 aa            linear   ROD 18-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423545
VERSION     NP_001423545.1
DBSOURCE    REFSEQ: accession NM_001436616.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.457773.1,
                                           SRR26643293.75526.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..636
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 5"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=71809
     Region          68..261
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          282..356
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          360..503
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..636
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436616.1:338..2248"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 miqfenvsyg iepvetlsgf ihviyentnq qakipdlgen qtyswsdeld yqfrsnmkks
       61 gfavlrpryi ktdivvdkkl fdymgsdtrv vlqkviqiig fintmfsklk ltvlinsvei
      121 wskenridfp eapenllvqf lhwkhkyrpq hisyllafve hpastgalyp gnlckpiyga
      181 aialypkgls lesysvivlq llsigiglty dnadschctg dvclmtpkai ysggvkdfst
      241 cslddfkyls tqdleclqdl pmerqkkkps rprricgngi lemneqcdcg tlkncthkkc
      301 cdpmscrlks kavcgsgecc gqdckvkpvn vlcrksknec dfeeycngnd aycvpdtfar
      361 ngqycdsgqa fcysglcmts nnqcmnllgk yvrgasfacy eefnsrndrf gncirkfcsf
      421 enslcgklvc twpfkrllmk dnmsaaygqi rddlcislyk ggrplkttls tysdmserde
      481 tfvkdgticg pdmfcletqc ketrflvdfq qcntsrdcnd hgvcnnfnhc hcdkgynppy
      541 cesvkgqfgs iddghkyyid egksakqqnr gihpkqqlql ilyitlplim iisavfikqs
      601 klsrlcgrer segtscited svsntkmttn egstlh
//
LOCUS       NP_001423527             331 aa            linear   ROD 18-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423527 XP_063144565
VERSION     NP_001423527.1
DBSOURCE    REFSEQ: accession NM_001436598.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063144565.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2315385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..331
                     /product="single-stranded DNA-binding protein 3 isoform c"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=34710
     Region          17..43
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          <90..308
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..331
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_001436598.1:360..1355"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mfakgkgsav psdgqarekl alyvyeyllh vgaqksaqtf lseirwekni tlgeppgflh
       61 swwcvfwdly caaperrdtc ehsseakafh dypfmsprya ggprppirmg nqppggvpgt
      121 qpllpnsmdp trqqghpnmg gsmqrmnppr gmgpmgpgpq nygsgmrppp nslgpampgi
      181 nmgpgagrpw pnpnsansip ysssspgtyv gppggggppg tpimpspads tnssdniytm
      241 inpvppggsr snfpmgpgsd gpmggmggme phhmngslgs gdidglpkns pnnisgisnp
      301 pgtprddgel ggnflhsfqn dnyspsmtms v
//
LOCUS       NP_001423559             682 aa            linear   ROD 18-MAR-2025
DEFINITION  phospholipase DDHD2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423559 XP_008769590
VERSION     NP_001423559.1
DBSOURCE    REFSEQ: accession NM_001436630.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Araki,M., Ohshima,N., Aso,C., Konishi,A., Obinata,H., Tatei,K. and
            Izumi,T.
  TITLE     Enzymatic characterization of recombinant rat DDHD2: a soluble
            diacylglycerol lipase
  JOURNAL   J Biochem 160 (5), 269-279 (2016)
   PUBMED   27198176
  REMARK    GeneRIF: These results therefore support the idea that DDHD2
            functions as a DG lipase in vivo and produces 2-AG.
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Aso,C., Araki,M., Ohshima,N., Tatei,K., Hirano,T., Obinata,H.,
            Kishi,M., Kishimoto,K., Konishi,A., Goto,F., Sugimoto,H. and
            Izumi,T.
  TITLE     Protein purification and cloning of diacylglycerol lipase from rat
            brain
  JOURNAL   J Biochem 159 (6), 585-597 (2016)
   PUBMED   26790472
  REMARK    GeneRIF: DG lipase activity in the soluble fraction of rat brain is
            derived from DDHD2. DDHD2 is distributed widely in the rat brain.
            Immunohistochemical analysis revealed that DDHD2 is expressed in
            hippocampal neurons, but not in glia.
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Inloes,J.M., Hsu,K.L., Dix,M.M., Viader,A., Masuda,K., Takei,T.,
            Wood,M.R. and Cravatt,B.F.
  TITLE     The hereditary spastic paraplegia-related enzyme DDHD2 is a
            principal brain triglyceride lipase
  JOURNAL   Proc Natl Acad Sci U S A 111 (41), 14924-14929 (2014)
   PUBMED   25267624
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_008769590.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1632195.1,
                                           SRR26643295.52948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..682
                     /product="phospholipase DDHD2 isoform 2"
                     /note="phospholipase DDHD2"
                     /calculated_mol_wt=77613
     Region          43..112
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          379..447
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          467..670
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..682
                     /gene="Ddhd2"
                     /coded_by="NM_001436630.1:221..2269"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:680971"
                     /db_xref="RGD:1585818"
ORIGIN      
        1 mssgesyqeq lsqsdpspsp nssssfelld mdvgssyepv sphwfyckvi dskelwipfn
       61 sedsqqleea hgsgkdcner vvptdggryd vhlgermrya vywdelpsev rrctwfykgd
      121 kdnkyvpyse sfsqvledty mlavtldewk kklespnrei ivlhnpklmv hyqpitgsde
      181 wgststeqgr prsvkrgves ipvdihcgep lqidhlvfvv hgigpacdlr frsivqcvnd
      241 frsvslnllq thfkkaqenq qigrveflpv nwhsplhstg vdidlqritl psinrlrhft
      301 ndtildvffy nsptycqtiv dtvasemnri ytlflqrnpd fkggvsiagh slgslilfdi
      361 ltnqkdsigd idsekgslst aedlgdvstl eeelkklqls efvtvfekek vdrealalct
      421 drdlqemgip lgprkkilnh fsatkssvgi nrptmsasev svkyprlnyk peiffafgsp
      481 igmfltvrgl rridpnykfp tckgffniyh pfdpvayrie pmvvpgvefe pmliphhkgr
      541 krmhlelreg ltrmsmdlkn nllgslrmaw ksftrapypa lqasemaedt eaesepssek
      601 psdanteepp vevkeeapin vgmlnggqri dyvlqekpie sfneylfalq shlcywesed
      661 tvllvlkeiy qtqgifldqp lq
//
LOCUS       NP_001305345             699 aa            linear   ROD 18-MAR-2025
DEFINITION  phospholipase DDHD2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001305345 XP_006253401
VERSION     NP_001305345.1
DBSOURCE    REFSEQ: accession NM_001318416.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Araki,M., Ohshima,N., Aso,C., Konishi,A., Obinata,H., Tatei,K. and
            Izumi,T.
  TITLE     Enzymatic characterization of recombinant rat DDHD2: a soluble
            diacylglycerol lipase
  JOURNAL   J Biochem 160 (5), 269-279 (2016)
   PUBMED   27198176
  REMARK    GeneRIF: These results therefore support the idea that DDHD2
            functions as a DG lipase in vivo and produces 2-AG.
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Aso,C., Araki,M., Ohshima,N., Tatei,K., Hirano,T., Obinata,H.,
            Kishi,M., Kishimoto,K., Konishi,A., Goto,F., Sugimoto,H. and
            Izumi,T.
  TITLE     Protein purification and cloning of diacylglycerol lipase from rat
            brain
  JOURNAL   J Biochem 159 (6), 585-597 (2016)
   PUBMED   26790472
  REMARK    GeneRIF: DG lipase activity in the soluble fraction of rat brain is
            derived from DDHD2. DDHD2 is distributed widely in the rat brain.
            Immunohistochemical analysis revealed that DDHD2 is expressed in
            hippocampal neurons, but not in glia.
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Inloes,J.M., Hsu,K.L., Dix,M.M., Viader,A., Masuda,K., Takei,T.,
            Wood,M.R. and Cravatt,B.F.
  TITLE     The hereditary spastic paraplegia-related enzyme DDHD2 is a
            principal brain triglyceride lipase
  JOURNAL   Proc Natl Acad Sci U S A 111 (41), 14924-14929 (2014)
   PUBMED   25267624
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006253401.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2397582.1,
                                           SRR26360190.2084953.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..699
                     /product="phospholipase DDHD2 isoform 1"
                     /function="lipase"
                     /note="phospholipase DDHD2"
                     /calculated_mol_wt=79440
     Region          43..112
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          379..447
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          484..687
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..699
                     /gene="Ddhd2"
                     /coded_by="NM_001318416.2:221..2320"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:680971"
                     /db_xref="RGD:1585818"
ORIGIN      
        1 mssgesyqeq lsqsdpspsp nssssfelld mdvgssyepv sphwfyckvi dskelwipfn
       61 sedsqqleea hgsgkdcner vvptdggryd vhlgermrya vywdelpsev rrctwfykgd
      121 kdnkyvpyse sfsqvledty mlavtldewk kklespnrei ivlhnpklmv hyqpitgsde
      181 wgststeqgr prsvkrgves ipvdihcgep lqidhlvfvv hgigpacdlr frsivqcvnd
      241 frsvslnllq thfkkaqenq qigrveflpv nwhsplhstg vdidlqritl psinrlrhft
      301 ndtildvffy nsptycqtiv dtvasemnri ytlflqrnpd fkggvsiagh slgslilfdi
      361 ltnqkdsigd idsekgslst aedlgdvstl eeelkklqls efvtvfekek vdrealalct
      421 drdlqemgip lgprkkilnh fsatkssvgi nrptmsasev nipkekgdyl dvgigqvsvk
      481 yprlnykpei ffafgspigm fltvrglrri dpnykfptck gffniyhpfd pvayriepmv
      541 vpgvefepml iphhkgrkrm hlelregltr msmdlknnll gslrmawksf trapypalqa
      601 semaedteae sepssekpsd anteeppvev keeapinvgm lnggqridyv lqekpiesfn
      661 eylfalqshl cywesedtvl lvlkeiyqtq gifldqplq
//
LOCUS       NP_001423578             432 aa            linear   ROD 18-MAR-2025
DEFINITION  testican-3 precursor [Rattus norvegicus].
ACCESSION   NP_001423578 XP_063131477
VERSION     NP_001423578.1
DBSOURCE    REFSEQ: accession NM_001436649.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Manabe,R., Tsutsui,K., Yamada,T., Kimura,M., Nakano,I., Shimono,C.,
            Sanzen,N., Furutani,Y., Fukuda,T., Oguri,Y., Shimamoto,K.,
            Kiyozumi,D., Sato,Y., Sado,Y., Senoo,H., Yamashina,S., Fukuda,S.,
            Kawai,J., Sugiura,N., Kimata,K., Hayashizaki,Y. and Sekiguchi,K.
  TITLE     Transcriptome-based systematic identification of extracellular
            matrix proteins
  JOURNAL   Proc Natl Acad Sci U S A 105 (35), 12849-12854 (2008)
   PUBMED   18757743
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Nakada,M., Yamada,A., Takino,T., Miyamori,H., Takahashi,T.,
            Yamashita,J. and Sato,H.
  TITLE     Suppression of membrane-type 1 matrix metalloproteinase
            (MMP)-mediated MMP-2 activation and tumor invasion by testican 3
            and its splicing variant gene product, N-Tes
  JOURNAL   Cancer Res 61 (24), 8896-8902 (2001)
   PUBMED   11751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063131477.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.773027.1,
                                           SRR26360176.2015478.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p13"
     Protein         1..432
                     /product="testican-3 precursor"
                     /note="testican-3; sparc/osteonectin, cwcv and kazal-like
                     domains proteoglycan 3; sparc/osteonectin, cwcv and
                     kazal-like domains proteoglycan (testican) 3"
                     /calculated_mol_wt=46486
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          134..180
                     /region_name="Kazal_2"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam07648"
                     /db_xref="CDD:400135"
     Region          198..310
                     /region_name="EFh_SPARC_TICN3"
                     /note="EF-hand, extracellular calcium-binding (EC) motif,
                     found in testican-3 (TICN3); cd16239"
                     /db_xref="CDD:320018"
     Region          246..277
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320018"
     Site            order(258,262,269)
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:320018"
     Region          278..310
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320018"
     Region          314..377
                     /region_name="Thyroglobulin_1"
                     /note="Thyroglobulin type-1 repeat; pfam00086"
                     /db_xref="CDD:459665"
     Site            order(318,333,351,355)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     CDS             1..432
                     /gene="Spock3"
                     /coded_by="NM_001436649.1:49..1347"
                     /db_xref="GeneID:306404"
                     /db_xref="RGD:1305672"
ORIGIN      
        1 mlkvsallcv caaawcsqtl aaaaavavag grsdggnfld ekqwlttvsq ydkevgqwnk
       61 frdddyfrtw npgkpidqal dpardpclkt kcsrhkvcit qdaqtalcis hrrlthsmke
      121 vggshkqwrg lpsstckqcp iayaspvcgs dghsyssqck leyqacvlgk qisikcegrc
      181 pcpsdksmst grnvkracsd lefrevanrl rdwfkalhes gsqnkrtkal lrpersrfdt
      241 silpickdsl gwmfnrldtn ydllldqsel gsiyldkneh ctkaffnscd tykdslisnn
      301 ewcycfqrqq dppchtelsk iqkrqgikkl lgqylplcde dgfykptqch gsvgqcwcvd
      361 rygnevvgsr ingvadcaid feisgdfasg dfrewtddeg eeddmndkdd iedddedegd
      421 ddddgddhdg yi
//
LOCUS       NP_001423534             329 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform a [Rattus norvegicus].
ACCESSION   NP_001423534 XP_006238090
VERSION     NP_001423534.1
DBSOURCE    REFSEQ: accession NM_001436605.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238090.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.923650.1,
                                           SRR26643429.19114.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..329
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=37589
     Region          1..95
                     /region_name="Interactions with ADPRT/PARP1 and NCL.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          2..101
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(27..28,40..41,43,63..64)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          106..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          111..115
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQC5; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          151..252
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            161
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          180..184
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            238
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          242..243
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            order(245,247,249..251)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Region          245..249
                     /region_name="Histidine triad motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Site            249
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            264
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          270..327
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..329
                     /gene="Aptx"
                     /coded_by="NM_001436605.1:43..1032"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mrvcwlvrqd cwhqriklph leavvigrsp etkitdkkcs rqqvqlkaec nkryvnvkqm
       61 gvnptsidev vigkdremkl lpgqvlhmvn elypymvefe evaespnvtq rkrkrpdcds
      121 qemeaeagas psqcsvspkt gkhgaakees lghwsqglki smkdpkmqvy kddqvvvikd
      181 kypkarhhwl vlpwasissl kvvtsehlel lkhmhavgek viadftgssk lrfrlgyhai
      241 psmshvhlhv isqdfdspcl knkkhwnsfn teyflesqav ikmvqeagrv tvkdgtcell
      301 klplrchecq qllpsipqlk ehlrkhwgg
//
LOCUS       NP_001423528             251 aa            linear   ROD 18-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423528
VERSION     NP_001423528.1
DBSOURCE    REFSEQ: accession NM_001436599.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.19867.1,
                                           SRR26643291.15444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..251
                     /product="single-stranded DNA-binding protein 3 isoform d"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=25382
     Region          <12..228
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..251
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_001436599.1:227..982"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mpggpippgf fqpfmsprya ggprppirmg nqppggvpgt qpllpnsmdp trqqghpnmg
       61 gsmqrmnppr gmgpmgpgpq nygsgmrppp nslgpampgi nmgpgagrpw pnpnsansip
      121 ysssspgtyv gppggggppg tpimpspads tnssdniytm inpvppggsr snfpmgpgsd
      181 gpmggmggme phhmngslgs gdidglpkns pnnisgisnp pgtprddgel ggnflhsfqn
      241 dnyspsmtms v
//
LOCUS       NP_001423537             270 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform b [Rattus norvegicus].
ACCESSION   NP_001423537
VERSION     NP_001423537.1
DBSOURCE    REFSEQ: accession NM_001436608.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.19115.1,
                                           SRR26360172.153336.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..270
                     /product="aprataxin isoform b"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=30530
     Region          <1..42
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..268
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="Aptx"
                     /coded_by="NM_001436608.1:83..895"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mgvnptside vvigkdremk llpgqvlhmv nelypymvef eevaespnvt qrkrkrpdcd
       61 sqemeaeaga spsqcsvspk tgkhgaakee slghwsqglk ismkdpkmqv ykddqvvvik
      121 dkypkarhhw lvlpwasiss lkvvtsehle llkhmhavge kviadftgss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa vikmvqeagr vtvkdgtcel
      241 lklplrchec qqllpsipql kehlrkhwgg
//
LOCUS       NP_001423538             270 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform b [Rattus norvegicus].
ACCESSION   NP_001423538
VERSION     NP_001423538.1
DBSOURCE    REFSEQ: accession NM_001436609.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1030393.1,
                                           SRR26360172.775013.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..270
                     /product="aprataxin isoform b"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=30530
     Region          <1..42
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..268
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="Aptx"
                     /coded_by="NM_001436609.1:215..1027"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mgvnptside vvigkdremk llpgqvlhmv nelypymvef eevaespnvt qrkrkrpdcd
       61 sqemeaeaga spsqcsvspk tgkhgaakee slghwsqglk ismkdpkmqv ykddqvvvik
      121 dkypkarhhw lvlpwasiss lkvvtsehle llkhmhavge kviadftgss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa vikmvqeagr vtvkdgtcel
      241 lklplrchec qqllpsipql kehlrkhwgg
//
LOCUS       NP_001423580             418 aa            linear   ROD 18-MAR-2025
DEFINITION  zinc finger protein 362 isoform a [Rattus norvegicus].
ACCESSION   NP_001423580 XP_063143357
VERSION     NP_001423580.1
DBSOURCE    REFSEQ: accession NM_001436651.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063143357.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..418
                     /product="zinc finger protein 362 isoform a"
                     /calculated_mol_wt=45541
     Region          <27..>131
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          239..264
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          253..275
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(260,262,264,266..267,270..271,274,288,290,294..295,
                     298..299,302,318,320,322,324..325,328..329,332)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          267..292
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <305..357
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          311..333
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..418
                     /gene="Zfp362"
                     /gene_synonym="RGD1306498"
                     /coded_by="NM_001436651.1:691..1947"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:297879"
                     /db_xref="RGD:1306498"
ORIGIN      
        1 msrsspsgkg psrmaeprfn npyfwppppt mpsqldnlvl inkikeqlma ekirpphlpp
       61 tsassqqpll vppapaessq avmslpklqq vpglhpqsvp qpdvalharp atstvtglgl
      121 ssrtpavsts estpgtgtgt stpstpttts qsrliasspt lisgitsppl ldsiktiqgh
      181 gllgppkser grkkikaenp ggppvlvvpy pilasgetak egktyrckvc pltfftksem
      241 qihskshtea kphkcphcsk sfanasylaq hlrihlgvkp yhcsycdksf rqlshlqqht
      301 rihtgdrpyk cphpgcekaf tqlsnlqshq rqhnkdkpyk cpncyraysd saslqihlsa
      361 haikhakayc csmcgrayts etylmkhmsk htvvehlvsh hspqrtespg ipvrisli
//
LOCUS       NP_001100110             425 aa            linear   ROD 18-MAR-2025
DEFINITION  probable G-protein coupled receptor 63 [Rattus norvegicus].
ACCESSION   NP_001100110 XP_001060842 XP_232847
VERSION     NP_001100110.1
DBSOURCE    REFSEQ: accession NM_001106640.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232847.1, XP_001060842.1.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..425
                     /product="probable G-protein coupled receptor 63"
                     /calculated_mol_wt=47887
     Region          88..388
                     /region_name="7tmA_GPR63"
                     /note="G protein-coupled receptor 63, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15404"
                     /db_xref="CDD:320526"
     Region          89..115
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320526"
     Region          122..147
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320526"
     Site            order(144,147..148,160..165,167..168,171,213,215..219,245,
                     248..250,252..254,256..257,333,336..337,339..340,343,
                     355..356,358..360,363,366..367)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320526"
     Region          160..190
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320526"
     Region          199..221
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320526"
     Region          245..274
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320526"
     Region          313..343
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320526"
     Region          356..381
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320526"
     CDS             1..425
                     /gene="Gpr63"
                     /coded_by="NM_001106640.3:418..1695"
                     /db_xref="GeneID:297952"
                     /db_xref="RGD:1306460"
ORIGIN      
        1 mvvsgvltap avlttphtgt snmtfvvyen spmnitaplp fqhpspgpll rysletmtst
       61 gfsslavnst vvtpapavfk slnlalqiil saimifilfv sflgnlvvcl mvyqkaamrs
      121 ainillasma fadmllavln mpfalvtilt trwifgkffc rlsamffwlf viegvailli
      181 isidrfliiv qrqdklnpyr akvliavswa tafsvafpla vgnpdlqips rapqcvfgyt
      241 tnsgyqayvi lislisffip flvilysfmg ilntlrhnal rihsypegic lsqvsklglm
      301 slqrpfqmsi dmsfktraft tililfavfi vcwapfttys lvatfskhfy yqhnffeist
      361 wllwlcylks alnpliyywr ikkfhdacld mmpksfkflp rlpghtrrri rpsavyvcge
      421 hrtvl
//
LOCUS       NP_001423585             598 aa            linear   ROD 18-MAR-2025
DEFINITION  anion exchange transporter isoform c [Rattus norvegicus].
ACCESSION   NP_001423585 XP_038965349
VERSION     NP_001423585.1
DBSOURCE    REFSEQ: accession NM_001436656.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Kiriya,M., Kawashima,A., Fujiwara,Y., Tanimura,Y., Yoshihara,A.,
            Nakamura,Y., Tanigawa,K., Kondo,T. and Suzuki,K.
  TITLE     Thyroglobulin regulates the expression and localization of the
            novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes
  JOURNAL   Endocr J 69 (10), 1217-1225 (2022)
   PUBMED   35644541
  REMARK    GeneRIF: Thyroglobulin regulates the expression and localization of
            the novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes.
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Yin,K., Lei,Y., Wen,X., Lacruz,R.S., Soleimani,M., Kurtz,I.,
            Snead,M.L., White,S.N. and Paine,M.L.
  TITLE     SLC26A Gene Family Participate in pH Regulation during Enamel
            Maturation
  JOURNAL   PLoS One 10 (12), e0144703 (2015)
   PUBMED   26671068
  REMARK    GeneRIF: Slc26a1, Slc26a6 and Slc26a7 are novel participants in the
            extracellular transport of bicarbonate during enamel maturation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Sun,X. and Petrovic,S.
  TITLE     Increased acid load and deletion of AE1 increase Slc26a7 expression
  JOURNAL   Nephron Physiol 109 (3), p29-p35 (2008)
   PUBMED   18663336
  REMARK    GeneRIF: Suggest that the increase in Slc26a7 expression caused by
            acid challenge represents an adaptive response, indicating that
            Slc26a7 contributes to the regulation of acid-base balance by the
            kidney.
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Barone,S., Amlal,H., Kujala,M., Xu,J., Karet,F., Blanchard,A.,
            Kere,J. and Soleimani,M.
  TITLE     Regulation of the basolateral chloride/base exchangers AE1 and
            SLC26A7 in the kidney collecting duct in potassium depletion
  JOURNAL   Nephrol Dial Transplant 22 (12), 3462-3470 (2007)
   PUBMED   17804457
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Kosiek,O., Busque,S.M., Foller,M., Shcheynikov,N., Kirchhoff,P.,
            Bleich,M., Muallem,S. and Geibel,J.P.
  TITLE     SLC26A7 can function as a chloride-loading mechanism in parietal
            cells
  JOURNAL   Pflugers Arch 454 (6), 989-998 (2007)
   PUBMED   17404755
  REMARK    GeneRIF: SLC26A7 is a Cl(-) uptake system under histamine
            stimulation
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Petrovic,S., Amlal,H., Sun,X., Karet,F., Barone,S. and Soleimani,M.
  TITLE     Vasopressin induces expression of the Cl-/HCO3- exchanger SLC26A7
            in kidney medullary collecting ducts of Brattleboro rats
  JOURNAL   Am J Physiol Renal Physiol 290 (5), F1194-F1201 (2006)
   PUBMED   16352747
  REMARK    GeneRIF: vasopressin increases the expression of SLC26A7 protein
            through posttranscriptional mechanisms in the outer medullary
            collecting duct
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Kim,K.H., Shcheynikov,N., Wang,Y. and Muallem,S.
  TITLE     SLC26A7 is a Cl- channel regulated by intracellular pH
  JOURNAL   J Biol Chem 280 (8), 6463-6470 (2005)
   PUBMED   15591059
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Petrovic,S., Ju,X., Barone,S., Seidler,U., Alper,S.L., Lohi,H.,
            Kere,J. and Soleimani,M.
  TITLE     Identification of a basolateral Cl-/HCO3- exchanger specific to
            gastric parietal cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 284 (6), G1093-G1103 (2003)
   PUBMED   12736153
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Lohi,H., Kujala,M., Makela,S., Lehtonen,E., Kestila,M.,
            Saarialho-Kere,U., Markovich,D. and Kere,J.
  TITLE     Functional characterization of three novel tissue-specific anion
            exchangers SLC26A7, -A8, and -A9
  JOURNAL   J Biol Chem 277 (16), 14246-14254 (2002)
   PUBMED   11834742
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Mocellin,R. and Buhlmeyer,K.
  TITLE     Late banding operation in children with ventricular septal defect
            and pulmonary arterial hypertension
  JOURNAL   Eur J Cardiol 3 (3), 205-211 (1975)
   PUBMED   1183472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038965349.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.875782.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..598
                     /product="anion exchange transporter isoform c"
                     /note="anion exchange transporter; solute carrier family
                     26 (anion exchanger), member 7"
                     /calculated_mol_wt=65053
     Region          3..579
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     CDS             1..598
                     /gene="Slc26a7"
                     /coded_by="NM_001436656.1:1519..3315"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:297910"
                     /db_xref="RGD:1310846"
ORIGIN      
        1 mgrhvatgtf altslisana verlvpqsnr nlttqsnssv lglsefelqr igvaaavsfl
       61 ggviqlvmfv lqlgnatfll tepvisamtt gaathvvtsq vkyllgikmp yisgplgffy
      121 iyayvfenik svqleallls llsivvlvlv kelneqfkrk ikvvlpvdlv liiaasfacy
      181 ctnmentygl evvgripkgi ppprappmni lsavlteafg valvgyvasl alaqgsakkf
      241 kysvddnqef lahglsnvip sflfcipsaa amgrtaglys tgaktqvacl iscifvlivi
      301 yaigpllywl pmcvlasiiv vglkgmliqf rdlkkywnvd kidwgiwist yifticfaan
      361 vgllfgvvct iaivlgrfpr aktlsitdmk emelkvktet ydntenwpps kstnvkvfpg
      421 slktgsnvrs lsvtprrmen sqqikiisin nplvflnakk fsadlmkiil ketdgsqald
      481 dvskceqntl lsplpngsct eeasqpcpse kyslvlncsg ltffdytgvs tlvelyldck
      541 srsvdvflan ctaslikamt yygdldtekp iffdsvatai sviqsnknls kdtdhsev
//
LOCUS       NP_001423577             530 aa            linear   ROD 18-MAR-2025
DEFINITION  chondroitin sulfate N-acetylgalactosaminyltransferase 1 [Rattus
            norvegicus].
ACCESSION   NP_001423577 XP_063131449
VERSION     NP_001423577.1
DBSOURCE    REFSEQ: accession NM_001436648.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Sato,T., Kudo,T., Ikehara,Y., Ogawa,H., Hirano,T., Kiyohara,K.,
            Hagiwara,K., Togayachi,A., Ema,M., Takahashi,S., Kimata,K.,
            Watanabe,H. and Narimatsu,H.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is
            necessary for normal endochondral ossification and aggrecan
            metabolism
  JOURNAL   J Biol Chem 286 (7), 5803-5812 (2011)
   PUBMED   21148564
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Watanabe,Y., Takeuchi,K., Higa Onaga,S., Sato,M., Tsujita,M.,
            Abe,M., Natsume,R., Li,M., Furuichi,T., Saeki,M., Izumikawa,T.,
            Hasegawa,A., Yokoyama,M., Ikegawa,S., Sakimura,K., Amizuka,N.,
            Kitagawa,H. and Igarashi,M.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required
            for normal cartilage development
  JOURNAL   Biochem J 432 (1), 47-55 (2010)
   PUBMED   20812917
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Gotoh,M., Sato,T., Akashima,T., Iwasaki,H., Kameyama,A.,
            Mochizuki,H., Yada,T., Inaba,N., Zhang,Y., Kikuchi,N., Kwon,Y.D.,
            Togayachi,A., Kudo,T., Nishihara,S., Watanabe,H., Kimata,K. and
            Narimatsu,H.
  TITLE     Enzymatic synthesis of chondroitin with a novel chondroitin sulfate
            N-acetylgalactosaminyltransferase that transfers
            N-acetylgalactosamine to glucuronic acid in initiation and
            elongation of chondroitin sulfate synthesis
  JOURNAL   J Biol Chem 277 (41), 38189-38196 (2002)
   PUBMED   12163485
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Kitagawa,H., Uyama,T. and Sugahara,K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase
  JOURNAL   J Biol Chem 276 (42), 38721-38726 (2001)
   PUBMED   11514575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063131449.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1353958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..530
                     /product="chondroitin sulfate
                     N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.174"
                     /note="chondroitin beta1,4
                     N-acetylgalactosaminyltransferase"
                     /calculated_mol_wt=60770
     Region          68..505
                     /region_name="CHGN"
                     /note="Chondroitin N-acetylgalactosaminyltransferase;
                     pfam05679"
                     /db_xref="CDD:461712"
     CDS             1..530
                     /gene="Csgalnact1"
                     /gene_synonym="Chgn; RGD1307618"
                     /coded_by="NM_001436648.1:826..2418"
                     /db_xref="GeneID:306375"
                     /db_xref="RGD:1307618"
ORIGIN      
        1 mvrrglvgwi srvvillvll ccaisvlyml actpkgdqeq lglprangpt gkdgyqavlq
       61 ereeqhrnyv nslkrqiaql kdelqarseq lrsgqdqasd atslrsgwdp epkaqadila
      121 flrgqvdkae vhagvklate yaavpfdsft lqkvyqletg ltrhpeekpv rkdkrdelve
      181 aiesalesln spvessphqr pytaadfieg iyrterdkgt lyeltfkgdh khefqrlvlf
      241 rpfgpimkvk keklnmantl invivplarr vdkfrhfmqn fremciqqdg rvhltvvyfg
      301 keemnevkgi lentskaanf rnftfiqlng efsrgkgldv garfwkgsnv vlffcdvdiy
      361 ftseflntcr lntqpgkkvf ypvlfsqynp giiyghhdav paleqqlvik ketgfwrdfg
      421 fgmtcqyrsd finiggfdld ikgwggedvh lyrkylhsnl ivirtpvrgl fhlwhekhcm
      481 deltpeqyrm cmqskamnea shgqlgmlvf rheieahlrk qklkasskkt
//
LOCUS       NP_775157               1820 aa            linear   ROD 18-MAR-2025
DEFINITION  CDK5 regulatory subunit-associated protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_775157 XP_001058949 XP_001059003 XP_001059053
VERSION     NP_775157.2
DBSOURCE    REFSEQ: accession NM_173134.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1820)
  AUTHORS   Bouguenina,H., Salaun,D., Mangon,A., Muller,L., Baudelet,E.,
            Camoin,L., Tachibana,T., Cianferani,S., Audebert,S.,
            Verdier-Pinard,P. and Badache,A.
  TITLE     EB1-binding-myomegalin protein complex promotes centrosomal
            microtubules functions
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10687-E10696 (2017)
   PUBMED   29162697
REFERENCE   2  (residues 1 to 1820)
  AUTHORS   Gao,F.J., Shi,L., Hines,T., Hebbar,S., Neufeld,K.L. and Smith,D.S.
  TITLE     Insulin signaling regulates a functional interaction between
            adenomatous polyposis coli and cytoplasmic dynein
  JOURNAL   Mol Biol Cell 28 (5), 587-599 (2017)
   PUBMED   28057765
REFERENCE   3  (residues 1 to 1820)
  AUTHORS   Park,J.S., Lee,M.K., Kang,S., Jin,Y., Fu,S., Rosales,J.L. and
            Lee,K.Y.
  TITLE     Species-Specific Expression of Full-Length and Alternatively
            Spliced Variant Forms of CDK5RAP2
  JOURNAL   PLoS One 10 (11), e0142577 (2015)
   PUBMED   26550838
  REMARK    GeneRIF: mouse expresses only one form of CDK5RAP2 that is
            equivalent to the human and rat alternatively spliced variant forms
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1820)
  AUTHORS   Mori,Y., Inoue,Y., Tanaka,S., Doda,S., Yamanaka,S., Fukuchi,H. and
            Terada,Y.
  TITLE     Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein,
            Binds to CDK5RAP2 and Regulates Microtubule Stability
  JOURNAL   PLoS One 10 (10), e0140968 (2015)
   PUBMED   26485573
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1820)
  AUTHORS   Yigit,G., Brown,K.E., Kayserili,H., Pohl,E., Caliebe,A.,
            Zahnleiter,D., Rosser,E., Bogershausen,N., Uyguner,Z.O.,
            Altunoglu,U., Nurnberg,G., Nurnberg,P., Rauch,A., Li,Y., Thiel,C.T.
            and Wollnik,B.
  TITLE     Mutations in CDK5RAP2 cause Seckel syndrome
  JOURNAL   Mol Genet Genomic Med 3 (5), 467-480 (2015)
   PUBMED   26436113
REFERENCE   6  (residues 1 to 1820)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   7  (residues 1 to 1820)
  AUTHORS   Hassan,M.J., Khurshid,M., Azeem,Z., John,P., Ali,G., Chishti,M.S.
            and Ahmad,W.
  TITLE     Previously described sequence variant in CDK5RAP2 gene in a
            Pakistani family with autosomal recessive primary microcephaly
  JOURNAL   BMC Med Genet 8, 58 (2007)
   PUBMED   17764569
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1820)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
REFERENCE   9  (residues 1 to 1820)
  AUTHORS   Wang,X., Ching,Y.P., Lam,W.H., Qi,Z., Zhang,M. and Wang,J.H.
  TITLE     Identification of a common protein association region in the
            neuronal Cdk5 activator
  JOURNAL   J Biol Chem 275 (41), 31763-31769 (2000)
   PUBMED   10915792
REFERENCE   10 (residues 1 to 1820)
  AUTHORS   Ching,Y.P., Qi,Z. and Wang,J.H.
  TITLE     Cloning of three novel neuronal Cdk5 activator binding proteins
  JOURNAL   Gene 242 (1-2), 285-294 (2000)
   PUBMED   10721722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Dec 25, 2009 this sequence version replaced
            XP_001058949.1, XP_001059003.1, XP_001059053.1, NP_775157.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1820
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..1820
                     /product="CDK5 regulatory subunit-associated protein 2
                     isoform 2"
                     /note="CDK5 activator-binding protein C48"
                     /calculated_mol_wt=206312
     Region          61..129
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          138..>464
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          1405..>1585
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..1820
                     /gene="Cdk5rap2"
                     /coded_by="NM_173134.3:169..5631"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:286919"
                     /db_xref="RGD:708451"
ORIGIN      
        1 mmdsgmeedv tlpgtlsgcs glhpvlpsdl dvisdttglg ngvlpimsee kvsptrarnm
       61 kdfenqitel kkenfnlklr iyfleeriqq efagptehiy kknielkvev eslkrelqer
      121 dqllvkaska veslaegggs eiqrvkedar kkvqqveell tkrihlleed vkaaqaelek
      181 afagteteka lrlsleskls amkkmqegdl emtlaleekd rlieelklsl kskealiqcl
      241 keeksqmasp denvssgelr glsatlreek erdaeerqke rnhfeeriqa lqedlreker
      301 eiatekknsl krdkaiqglt malkskekev eelnsiikel tadstqsrea plktqvsefe
      361 vresenceaa laekeallak lhsenvtknt enhrllrnvk kvtqelndlk keklrlerdl
      421 eeahregnrg artihdlrne veklrkevce rekavekhyk slpgessskf hsqeqvvkgl
      481 tesasqedll lqksnekdle aiqqncylmt aeelkfgsdg litekcsqqs pdsklifske
      541 kqqseyeglt gdlkteqnvy ahlaknlqdt dsklqaelkr vlalrkqleq dvlayrnlqt
      601 alqeqlseir kreeepfsfy sdqtsylsic leehsqfqle hfsqeeikkk vidliqlvkd
      661 lhadnqhlkk tifdiscmgv qgndrlestk qaelmaskad edtlkfkadd enhfqsdqhl
      721 eqsreimedy aegggkdgyv rhmdsnildh dgahtpdtse dhsledells llatffskka
      781 tpslesrpdl lkalgallle riclaeqgsp gdhsdskaek aleqvavrlr delghsclan
      841 sfskshselk sprgtwlvkt gdeakvelks vsvqtmtied strgfkperk reawagkpee
      901 avfstelese algempglqa thlsfpsaid kddqktglli qlktpellen lynlpasqev
      961 vaqlqgqvle lqkelkeyki rnkqlldkli laeammegma vpnstpvnvp aaqavvrtaf
     1021 qgkpgeqegh etthsagrdk evdsdqytsf eidseicppd dlallpacke nledflgpps
     1081 iatyldsksq lsvkvsvvgt dqseninlpd dtealkqkih dlqtelegyr niivqlqkhs
     1141 qcseaiitvl cgtegaqdgl nkpkghidee emtfsslhqv ryvkhmkilr pltpeiidgk
     1201 mleslkqqlv eqeqelqkeq dlnlelfgei hnlqnkfrdl spsrydslvq sqarelslqr
     1261 qqikdshdic vvchqhmstm ikafeellqa sdvdscvaeg freqltqcag lleqleklfl
     1321 hgksarveph tqtellrrlr teednlpyqh llpespepsa shalsddems eksflsrepk
     1381 pdsetekypt iasrfpqdll mehiqeirtl rkhleesikt neklrkqler qgcetdqgst
     1441 nvsaysselh nsltseiqfl rkqnealstm lekgskekqk eneklresla rkteslehlq
     1501 leyasvreen erlrrdisek erqnqqltqe vcsslqelsr vqeeaksrqq lllqkdellq
     1561 slqmelkvye klaeehqklq qdvnkcpeas dnsfdlfest qamapksase tpvlsgtdvd
     1621 slscdstssa tspscmpclv agrhlwasks ghhmlclied ydalykqisw gqtllakmdi
     1681 qtqealspts qklgpkasfs vplskflssm ntaklileka srllklfwrv svptngqcsl
     1741 hcdqigemka eitklhkklf eqekklqnta kllqqskhqe kiifdqlvit hqvlrkargn
     1801 lelrpraahp gtsspsrpgs
//
LOCUS       NP_001423583             656 aa            linear   ROD 18-MAR-2025
DEFINITION  anion exchange transporter isoform a [Rattus norvegicus].
ACCESSION   NP_001423583 XP_006237973
VERSION     NP_001423583.1
DBSOURCE    REFSEQ: accession NM_001436654.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Kiriya,M., Kawashima,A., Fujiwara,Y., Tanimura,Y., Yoshihara,A.,
            Nakamura,Y., Tanigawa,K., Kondo,T. and Suzuki,K.
  TITLE     Thyroglobulin regulates the expression and localization of the
            novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes
  JOURNAL   Endocr J 69 (10), 1217-1225 (2022)
   PUBMED   35644541
  REMARK    GeneRIF: Thyroglobulin regulates the expression and localization of
            the novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes.
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Yin,K., Lei,Y., Wen,X., Lacruz,R.S., Soleimani,M., Kurtz,I.,
            Snead,M.L., White,S.N. and Paine,M.L.
  TITLE     SLC26A Gene Family Participate in pH Regulation during Enamel
            Maturation
  JOURNAL   PLoS One 10 (12), e0144703 (2015)
   PUBMED   26671068
  REMARK    GeneRIF: Slc26a1, Slc26a6 and Slc26a7 are novel participants in the
            extracellular transport of bicarbonate during enamel maturation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Sun,X. and Petrovic,S.
  TITLE     Increased acid load and deletion of AE1 increase Slc26a7 expression
  JOURNAL   Nephron Physiol 109 (3), p29-p35 (2008)
   PUBMED   18663336
  REMARK    GeneRIF: Suggest that the increase in Slc26a7 expression caused by
            acid challenge represents an adaptive response, indicating that
            Slc26a7 contributes to the regulation of acid-base balance by the
            kidney.
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Barone,S., Amlal,H., Kujala,M., Xu,J., Karet,F., Blanchard,A.,
            Kere,J. and Soleimani,M.
  TITLE     Regulation of the basolateral chloride/base exchangers AE1 and
            SLC26A7 in the kidney collecting duct in potassium depletion
  JOURNAL   Nephrol Dial Transplant 22 (12), 3462-3470 (2007)
   PUBMED   17804457
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Kosiek,O., Busque,S.M., Foller,M., Shcheynikov,N., Kirchhoff,P.,
            Bleich,M., Muallem,S. and Geibel,J.P.
  TITLE     SLC26A7 can function as a chloride-loading mechanism in parietal
            cells
  JOURNAL   Pflugers Arch 454 (6), 989-998 (2007)
   PUBMED   17404755
  REMARK    GeneRIF: SLC26A7 is a Cl(-) uptake system under histamine
            stimulation
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Petrovic,S., Amlal,H., Sun,X., Karet,F., Barone,S. and Soleimani,M.
  TITLE     Vasopressin induces expression of the Cl-/HCO3- exchanger SLC26A7
            in kidney medullary collecting ducts of Brattleboro rats
  JOURNAL   Am J Physiol Renal Physiol 290 (5), F1194-F1201 (2006)
   PUBMED   16352747
  REMARK    GeneRIF: vasopressin increases the expression of SLC26A7 protein
            through posttranscriptional mechanisms in the outer medullary
            collecting duct
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Kim,K.H., Shcheynikov,N., Wang,Y. and Muallem,S.
  TITLE     SLC26A7 is a Cl- channel regulated by intracellular pH
  JOURNAL   J Biol Chem 280 (8), 6463-6470 (2005)
   PUBMED   15591059
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Petrovic,S., Ju,X., Barone,S., Seidler,U., Alper,S.L., Lohi,H.,
            Kere,J. and Soleimani,M.
  TITLE     Identification of a basolateral Cl-/HCO3- exchanger specific to
            gastric parietal cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 284 (6), G1093-G1103 (2003)
   PUBMED   12736153
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Lohi,H., Kujala,M., Makela,S., Lehtonen,E., Kestila,M.,
            Saarialho-Kere,U., Markovich,D. and Kere,J.
  TITLE     Functional characterization of three novel tissue-specific anion
            exchangers SLC26A7, -A8, and -A9
  JOURNAL   J Biol Chem 277 (16), 14246-14254 (2002)
   PUBMED   11834742
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Mocellin,R. and Buhlmeyer,K.
  TITLE     Late banding operation in children with ventricular septal defect
            and pulmonary arterial hypertension
  JOURNAL   Eur J Cardiol 3 (3), 205-211 (1975)
   PUBMED   1183472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237973.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.12743.1,
                                           SRR26643298.26547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..656
                     /product="anion exchange transporter isoform a"
                     /note="anion exchange transporter; solute carrier family
                     26 (anion exchanger), member 7"
                     /calculated_mol_wt=71742
     Region          33..637
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     CDS             1..656
                     /gene="Slc26a7"
                     /coded_by="NM_001436654.1:214..2184"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:297910"
                     /db_xref="RGD:1310846"
ORIGIN      
        1 mtgakrkkrs vlwgkmhtph redikqwckr rlpilewapq ynlkenllpd tvsgvllavq
       61 qvtqglsfai lssvhpvfgl ygslfpaiiy aifgmgrhva tgtfaltsli sanaverlvp
      121 qsnrnlttqs nssvlglsef elqrigvaaa vsflggviql vmfvlqlgna tflltepvis
      181 amttgaathv vtsqvkyllg ikmpyisgpl gffyiyayvf eniksvqlea lllsllsivv
      241 lvlvkelneq fkrkikvvlp vdlvliiaas facyctnmen tyglevvgri pkgippprap
      301 pmnilsavlt eafgvalvgy vaslalaqgs akkfkysvdd nqeflahgls nvipsflfci
      361 psaaamgrta glystgaktq vacliscifv liviyaigpl lywlpmcvla siivvglkgm
      421 liqfrdlkky wnvdkidwgi wistyiftic faanvgllfg vvctiaivlg rfpraktlsi
      481 tdmkemelkv ktetydensq qikiisinnp lvflnakkfs adlmkiilke tdgsqalddv
      541 skceqntlls plpngsctee asqpcpseky slvlncsglt ffdytgvstl velyldcksr
      601 svdvflanct aslikamtyy gdldtekpif fdsvataisv iqsnknlskd tdhsev
//
LOCUS       NP_001423542             753 aa            linear   ROD 18-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423542 XP_063131718
VERSION     NP_001423542.1
DBSOURCE    REFSEQ: accession NM_001436613.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063131718.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.75509.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..753
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 1 precursor"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=83188
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     Region          26..142
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          185..378
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          399..473
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          477..620
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..753
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436613.1:287..2548"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 mflllllvvh lnglqagqhp qktilqttvp ekisspdvet dpenhmayli tinenphfih
       61 lkkqsfitst avsytydrqd vrhsqslssl kncnyngyva gfpnsivslt vcsglrgmiq
      121 fenvsygiep vetlsgfihv iyentnqqak ipdlgenqty swsdeldyqf rsnmkksgfa
      181 vlrpryiktd ivvdkklfdy mgsdtrvvlq kviqiigfin tmfsklkltv linsveiwsk
      241 enridfpeap enllvqflhw khkyrpqhis yllafvehpa stgalypgnl ckpiygaaia
      301 lypkglsles ysvivlqlls igigltydna dschctgdvc lmtpkaiysg gvkdfstcsl
      361 ddfkylstqd leclqdlpme rqkkkpsrpr ricgngilem neqcdcgtlk ncthkkccdp
      421 mscrlkskav cgsgeccgqd ckvkpvnvlc rksknecdfe eycngndayc vpdtfarngq
      481 ycdsgqafcy sglcmtsnnq cmnllgkyvr gasfacyeef nsrndrfgnc irkfcsfens
      541 lcgklvctwp fkrllmkdnm saaygqirdd lcislykggr plkttlstys dmserdetfv
      601 kdgticgpdm fcletqcket rflvdfqqcn tsrdcndhgv cnnfnhchcd kgynppyces
      661 vkgqfgsidd ghkyyidegk sakqqnrgih pkqqlqlily itlplimiis avfikqskls
      721 rlcgrerseg tscitedsvs ntkmttnegs tlh
//
LOCUS       NP_001423558             699 aa            linear   ROD 18-MAR-2025
DEFINITION  phospholipase DDHD2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423558
VERSION     NP_001423558.1
DBSOURCE    REFSEQ: accession NM_001436629.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Araki,M., Ohshima,N., Aso,C., Konishi,A., Obinata,H., Tatei,K. and
            Izumi,T.
  TITLE     Enzymatic characterization of recombinant rat DDHD2: a soluble
            diacylglycerol lipase
  JOURNAL   J Biochem 160 (5), 269-279 (2016)
   PUBMED   27198176
  REMARK    GeneRIF: These results therefore support the idea that DDHD2
            functions as a DG lipase in vivo and produces 2-AG.
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Aso,C., Araki,M., Ohshima,N., Tatei,K., Hirano,T., Obinata,H.,
            Kishi,M., Kishimoto,K., Konishi,A., Goto,F., Sugimoto,H. and
            Izumi,T.
  TITLE     Protein purification and cloning of diacylglycerol lipase from rat
            brain
  JOURNAL   J Biochem 159 (6), 585-597 (2016)
   PUBMED   26790472
  REMARK    GeneRIF: DG lipase activity in the soluble fraction of rat brain is
            derived from DDHD2. DDHD2 is distributed widely in the rat brain.
            Immunohistochemical analysis revealed that DDHD2 is expressed in
            hippocampal neurons, but not in glia.
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Inloes,J.M., Hsu,K.L., Dix,M.M., Viader,A., Masuda,K., Takei,T.,
            Wood,M.R. and Cravatt,B.F.
  TITLE     The hereditary spastic paraplegia-related enzyme DDHD2 is a
            principal brain triglyceride lipase
  JOURNAL   Proc Natl Acad Sci U S A 111 (41), 14924-14929 (2014)
   PUBMED   25267624
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.71943.1,
                                           SRR26360172.501296.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..699
                     /product="phospholipase DDHD2 isoform 1"
                     /note="phospholipase DDHD2"
                     /calculated_mol_wt=79440
     Region          43..112
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          379..447
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          484..687
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..699
                     /gene="Ddhd2"
                     /coded_by="NM_001436629.1:144..2243"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:680971"
                     /db_xref="RGD:1585818"
ORIGIN      
        1 mssgesyqeq lsqsdpspsp nssssfelld mdvgssyepv sphwfyckvi dskelwipfn
       61 sedsqqleea hgsgkdcner vvptdggryd vhlgermrya vywdelpsev rrctwfykgd
      121 kdnkyvpyse sfsqvledty mlavtldewk kklespnrei ivlhnpklmv hyqpitgsde
      181 wgststeqgr prsvkrgves ipvdihcgep lqidhlvfvv hgigpacdlr frsivqcvnd
      241 frsvslnllq thfkkaqenq qigrveflpv nwhsplhstg vdidlqritl psinrlrhft
      301 ndtildvffy nsptycqtiv dtvasemnri ytlflqrnpd fkggvsiagh slgslilfdi
      361 ltnqkdsigd idsekgslst aedlgdvstl eeelkklqls efvtvfekek vdrealalct
      421 drdlqemgip lgprkkilnh fsatkssvgi nrptmsasev nipkekgdyl dvgigqvsvk
      481 yprlnykpei ffafgspigm fltvrglrri dpnykfptck gffniyhpfd pvayriepmv
      541 vpgvefepml iphhkgrkrm hlelregltr msmdlknnll gslrmawksf trapypalqa
      601 semaedteae sepssekpsd anteeppvev keeapinvgm lnggqridyv lqekpiesfn
      661 eylfalqshl cywesedtvl lvlkeiyqtq gifldqplq
//
LOCUS       NP_114180                248 aa            linear   ROD 18-MAR-2025
DEFINITION  clathrin light chain A isoform 2 [Rattus norvegicus].
ACCESSION   NP_114180
VERSION     NP_114180.1
DBSOURCE    REFSEQ: accession NM_031974.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Li,H., Alavian,K.N., Lazrove,E., Mehta,N., Jones,A., Zhang,P.,
            Licznerski,P., Graham,M., Uo,T., Guo,J., Rahner,C., Duman,R.S.,
            Morrison,R.S. and Jonas,E.A.
  TITLE     A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
            during endocytosis
  JOURNAL   Nat Cell Biol 15 (7), 773-785 (2013)
   PUBMED   23792689
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Bu,W., Lim,K.B., Yu,Y.H., Chou,A.M., Sudhaharan,T. and Ahmed,S.
  TITLE     Cdc42 interaction with N-WASP and Toca-1 regulates membrane
            tubulation, vesicle formation and vesicle motility: implications
            for endocytosis
  JOURNAL   PLoS One 5 (8), e12153 (2010)
   PUBMED   20730103
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Mettlen,M., Loerke,D., Yarar,D., Danuser,G. and Schmid,S.L.
  TITLE     Cargo- and adaptor-specific mechanisms regulate clathrin-mediated
            endocytosis
  JOURNAL   J Cell Biol 188 (6), 919-933 (2010)
   PUBMED   20231386
  REMARK    GeneRIF: The results underscore the highly dynamic and
            cargo-responsive nature of CCP assembly and suggest that the
            observed heterogeneity is, in part, related to compositional
            differences (e.g., cargo and adaptors) between CCPs.
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Drake,M.T., Downs,M.A. and Traub,L.M.
  TITLE     Epsin binds to clathrin by associating directly with the
            clathrin-terminal domain. Evidence for cooperative binding through
            two discrete sites
  JOURNAL   J Biol Chem 275 (9), 6479-6489 (2000)
   PUBMED   10692452
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Saito,Y., Tsubuki,S., Ito,H., Ohmi-Imajo,S. and Kawashima,S.
  TITLE     Possible involvement of clathrin in neuritogenesis induced by a
            protease inhibitor (benzyloxycarbonyl-Leu-Leu-Leu-aldehyde) in PC12
            cells
  JOURNAL   J Biochem 112 (4), 448-455 (1992)
   PUBMED   1490999
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Maycox,P.R., Link,E., Reetz,A., Morris,S.A. and Jahn,R.
  TITLE     Clathrin-coated vesicles in nervous tissue are involved primarily
            in synaptic vesicle recycling
  JOURNAL   J Cell Biol 118 (6), 1379-1388 (1992)
   PUBMED   1325974
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Kirchhausen,T., Scarmato,P., Harrison,S.C., Monroe,J.J., Chow,E.P.,
            Mattaliano,R.J., Ramachandran,K.L., Smart,J.E., Ahn,A.H. and
            Brosius,J.
  TITLE     Clathrin light chains LCA and LCB are similar, polymorphic, and
            share repeated heptad motifs
  JOURNAL   Science 236 (4799), 320-324 (1987)
   PUBMED   3563513
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Brodsky,F.M.
  TITLE     Clathrin structure characterized with monoclonal antibodies. II.
            Identification of in vivo forms of clathrin
  JOURNAL   J Cell Biol 101 (6), 2055-2062 (1985)
   PUBMED   4066749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213034.1, M15882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..248
                     /product="clathrin light chain A isoform 2"
                     /note="clathrin, light polypeptide (Lca); clathrin, light
                     chain (Lca); lca"
                     /calculated_mol_wt=26849
     Region          1..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08081.1)"
     Region          22..248
                     /region_name="Clathrin_lg_ch"
                     /note="Clathrin light chain; pfam01086"
                     /db_xref="CDD:460056"
     Region          100..162
                     /region_name="Involved in binding clathrin heavy chain"
                     /note="propagated from UniProtKB/Swiss-Prot (P08081.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09496; propagated from
                     UniProtKB/Swiss-Prot (P08081.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09496; propagated from
                     UniProtKB/Swiss-Prot (P08081.1)"
     Site            223
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6IRU5; propagated from
                     UniProtKB/Swiss-Prot (P08081.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09496; propagated from
                     UniProtKB/Swiss-Prot (P08081.1)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O08585; propagated from
                     UniProtKB/Swiss-Prot (P08081.1)"
     CDS             1..248
                     /gene="Clta"
                     /gene_synonym="LCA1; LCA2; LCA3"
                     /coded_by="NM_031974.2:124..870"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:83800"
                     /db_xref="RGD:70919"
ORIGIN      
        1 maeldpfgap agapggpalg ngvagageed paaaflaqqe seiagiende afaildggap
       61 gpqahgeppg gpdavdgvmn geyyqesngp tdsyaaisev drlqsepesi rkwreeqter
      121 lealdansrk qeaewkekav keleewyarq deqlqktkas nrvadeafyk qpfadvigyv
      181 tninhpcysl eqaaeeafvn didesspgte wervarlcdf npksskqakd vsrmrsvlis
      241 lkqaplvh
//
LOCUS       NP_001423529             251 aa            linear   ROD 18-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423529 XP_038966800
VERSION     NP_001423529.1
DBSOURCE    REFSEQ: accession NM_001436600.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038966800.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1827183.1,
                                           SRR21887622.3843950.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680419, SAMN06680425
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..251
                     /product="single-stranded DNA-binding protein 3 isoform d"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=25382
     Region          <12..228
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..251
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_001436600.1:484..1239"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mpggpippgf fqpfmsprya ggprppirmg nqppggvpgt qpllpnsmdp trqqghpnmg
       61 gsmqrmnppr gmgpmgpgpq nygsgmrppp nslgpampgi nmgpgagrpw pnpnsansip
      121 ysssspgtyv gppggggppg tpimpspads tnssdniytm inpvppggsr snfpmgpgsd
      181 gpmggmggme phhmngslgs gdidglpkns pnnisgisnp pgtprddgel ggnflhsfqn
      241 dnyspsmtms v
//
LOCUS       NP_001423565             691 aa            linear   ROD 18-MAR-2025
DEFINITION  myb-related protein A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423565 XP_006237814
VERSION     NP_001423565.1
DBSOURCE    REFSEQ: accession NM_001436636.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Zhang,D., Xie,D., Lin,X., Ma,L., Chen,J., Zhang,D., Wang,Y.,
            Duo,S., Feng,Y., Zheng,C., Jiang,B., Ning,Y. and Han,C.
  TITLE     The transcription factor SOX30 is a key regulator of mouse
            spermiogenesis
  JOURNAL   Development 145 (11) (2018)
   PUBMED   29848638
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Li,X.Z., Roy,C.K., Dong,X., Bolcun-Filas,E., Wang,J., Han,B.W.,
            Xu,J., Moore,M.J., Schimenti,J.C., Weng,Z. and Zamore,P.D.
  TITLE     An ancient transcription factor initiates the burst of piRNA
            production during early meiosis in mouse testes
  JOURNAL   Mol Cell 50 (1), 67-81 (2013)
   PUBMED   23523368
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Bolcun-Filas,E., Bannister,L.A., Barash,A., Schimenti,K.J.,
            Hartford,S.A., Eppig,J.J., Handel,M.A., Shen,L. and Schimenti,J.C.
  TITLE     A-MYB (MYBL1) transcription factor is a master regulator of male
            meiosis
  JOURNAL   Development 138 (15), 3319-3330 (2011)
   PUBMED   21750041
REFERENCE   4  (residues 1 to 691)
  AUTHORS   Ma,X.P. and Calabretta,B.
  TITLE     DNA binding and transactivation activity of A-myb, a c-myb-related
            gene
  JOURNAL   Cancer Res 54 (24), 6512-6516 (1994)
   PUBMED   7987850
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237814.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.811419.1,
                                           SRR21887622.236336.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..691
                     /product="myb-related protein A isoform 3"
                     /note="myb-related protein A; myeloblastosis oncogene-like
                     1"
                     /calculated_mol_wt=78514
     Region          38..98
                     /region_name="Myb_DNA-bind_6"
                     /note="Myb-like DNA-binding domain; pfam13921"
                     /db_xref="CDD:372817"
     Site            order(38,68..69,71..72,74..76,78..80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          84..>192
                     /region_name="PLN03091"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:215570"
     Region          240..285
                     /region_name="LMSTEN"
                     /note="LMSTEN motif; pfam07988"
                     /db_xref="CDD:462332"
     Region          485..641
                     /region_name="Cmyb_C"
                     /note="C-myb, C-terminal; pfam09316"
                     /db_xref="CDD:462753"
     CDS             1..691
                     /gene="Mybl1"
                     /coded_by="NM_001436636.1:372..2447"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:297783"
                     /db_xref="RGD:1306940"
ORIGIN      
        1 makrsrsede dddlqyadhd yevpqqkglk klwnrvkwtr deddklkklv eqhgtddwtl
       61 iashlqnrsd fqcqhrwqkv lnpelikgpw tkeedqrvie lvqkygpkrw sliakhlkgr
      121 igkqcrerwh nhlnpevkks swteeedrii yeahkrlgnr waeiakllpg rtdnsiknhw
      181 nstmrrkveq egylqdgiks ersssklqhk pcatmdhlqt qnqfyipvqi pgyqyvspdg
      241 ncvehvqtsa fiqqpfvded pdkekkikel elllmsaene vrrkrlppqp gsfsswsgsf
      301 lmddsmsntl nnleehttef ysmdenqtvs aqqnsptkfl aveanavlss lqtipefaet
      361 leliesdpva wsdvtsfdls daaaspvkst pvklmriqhn egamecqfnv slvlegkkns
      421 cnggdseaip laspnvvkfs tpptilrkkk rlrvgqsags elgegslseg nnaalkhtpv
      481 ktlpfspsqf fntcpgseql nienpsftst picgqkvlit tplqkeatpk dqkenvgfrt
      541 ptirrsilgt tprtptpfkn alaaqekkyg plkivsqpla fleedirevl keetgtdifl
      601 keedepayks ckqehsasvk kvrkslales wdkeepgtql ltedisdmqs ncewetvvyg
      661 ktedqlimte qarrylstyt apsstsrali l
//
LOCUS       NP_001423551             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423551 XP_006237784
VERSION     NP_001423551.1
DBSOURCE    REFSEQ: accession NM_001436622.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237784.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20317.1,
                                           SRR26643294.20212.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436622.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001100100             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001100100 XP_001059299 XP_232578
VERSION     NP_001100100.1
DBSOURCE    REFSEQ: accession NM_001106630.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001059299.1, XP_232578.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001106630.2:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001100102             749 aa            linear   ROD 18-MAR-2025
DEFINITION  myb-related protein A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100102 XP_001060705 XP_232620
VERSION     NP_001100102.1
DBSOURCE    REFSEQ: accession NM_001106632.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Zhang,D., Xie,D., Lin,X., Ma,L., Chen,J., Zhang,D., Wang,Y.,
            Duo,S., Feng,Y., Zheng,C., Jiang,B., Ning,Y. and Han,C.
  TITLE     The transcription factor SOX30 is a key regulator of mouse
            spermiogenesis
  JOURNAL   Development 145 (11) (2018)
   PUBMED   29848638
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Li,X.Z., Roy,C.K., Dong,X., Bolcun-Filas,E., Wang,J., Han,B.W.,
            Xu,J., Moore,M.J., Schimenti,J.C., Weng,Z. and Zamore,P.D.
  TITLE     An ancient transcription factor initiates the burst of piRNA
            production during early meiosis in mouse testes
  JOURNAL   Mol Cell 50 (1), 67-81 (2013)
   PUBMED   23523368
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Bolcun-Filas,E., Bannister,L.A., Barash,A., Schimenti,K.J.,
            Hartford,S.A., Eppig,J.J., Handel,M.A., Shen,L. and Schimenti,J.C.
  TITLE     A-MYB (MYBL1) transcription factor is a master regulator of male
            meiosis
  JOURNAL   Development 138 (15), 3319-3330 (2011)
   PUBMED   21750041
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Ma,X.P. and Calabretta,B.
  TITLE     DNA binding and transactivation activity of A-myb, a c-myb-related
            gene
  JOURNAL   Cancer Res 54 (24), 6512-6516 (1994)
   PUBMED   7987850
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232620.3, XP_001060705.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..749
                     /product="myb-related protein A isoform 2"
                     /note="myb-related protein A; myeloblastosis oncogene-like
                     1"
                     /calculated_mol_wt=85092
     Region          38..98
                     /region_name="Myb_DNA-bind_6"
                     /note="Myb-like DNA-binding domain; pfam13921"
                     /db_xref="CDD:372817"
     Site            order(38,68..69,71..72,74..76,78..80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          84..>192
                     /region_name="PLN03091"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:215570"
     Region          238..283
                     /region_name="LMSTEN"
                     /note="LMSTEN motif; pfam07988"
                     /db_xref="CDD:462332"
     Region          483..639
                     /region_name="Cmyb_C"
                     /note="C-myb, C-terminal; pfam09316"
                     /db_xref="CDD:462753"
     CDS             1..749
                     /gene="Mybl1"
                     /coded_by="NM_001106632.2:372..2621"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:297783"
                     /db_xref="RGD:1306940"
ORIGIN      
        1 makrsrsede dddlqyadhd yevpqqkglk klwnrvkwtr deddklkklv eqhgtddwtl
       61 iashlqnrsd fqcqhrwqkv lnpelikgpw tkeedqrvie lvqkygpkrw sliakhlkgr
      121 igkqcrerwh nhlnpevkks swteeedrii yeahkrlgnr waeiakllpg rtdnsiknhw
      181 nstmrrkveq egylqdgiks ersssklqhk pcatmdhlqt qnqfyipipg yqyvspdgnc
      241 vehvqtsafi qqpfvdedpd kekkikelel llmsaenevr rkrlppqpgs fsswsgsflm
      301 ddsmsntlnn leehttefys mdenqtvsaq qnsptkflav eanavlsslq tipefaetle
      361 liesdpvaws dvtsfdlsda aaspvkstpv klmriqhneg amecqfnvsl vlegkknscn
      421 ggdseaipla spnvvkfstp ptilrkkkrl rvgqsagsel gegslsegnn aalkhtpvkt
      481 lpfspsqffn tcpgseqlni enpsftstpi cgqkvlittp lqkeatpkdq kenvgfrtpt
      541 irrsilgttp rtptpfknal aaqekkygpl kivsqplafl eedirevlke etgtdiflke
      601 edepayksck qehsasvkkv rkslaleswd keepgtqllt edisdmqsen ilttsllmip
      661 lleihdnrcn ltpekqdins anktytltkk rpnpntckav klekslqsnc ewetvvygkt
      721 edqlimteqa rrylstytap sstsralil
//
LOCUS       NP_001423526             388 aa            linear   ROD 18-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423526 XP_006238597
VERSION     NP_001423526.1
DBSOURCE    REFSEQ: accession NM_001436597.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY724490.1, SRR26643297.19567.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..388
                     /product="single-stranded DNA-binding protein 3 isoform b"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=40290
     Region          17..43
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          81..365
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..388
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_001436597.1:360..1526"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mfakgkgsav psdgqarekl alyvyeyllh vgaqksaqtf lseirwekni tlgeppgflh
       61 swwcvfwdly caaperrdtc ehsseakafh dysaaaapsp vlgnippndg mpggpippgf
      121 fqgppgsqps phaqppphnp ssmmgphsqp fmspryaggp rppirmgnqp pggvpgtqpl
      181 lpnsmdptrq qghpnmggsm qrmnpprgmg pmgpgpqnyg sgmrpppnsl gpampginmg
      241 pgagrpwpnp nsansipyss sspgtyvgpp ggggppgtpi mpspadstns sdniytminp
      301 vppggsrsnf pmgpgsdgpm ggmggmephh mngslgsgdi dglpknspnn isgisnppgt
      361 prddgelggn flhsfqndny spsmtmsv
//
LOCUS       NP_001423543             773 aa            linear   ROD 18-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423543 XP_006253383
VERSION     NP_001423543.1
DBSOURCE    REFSEQ: accession NM_001436614.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006253383.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1857597.1,
                                           SRR26643293.75522.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..773
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 2 precursor"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=85419
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     Region          26..142
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          185..378
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          399..473
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          477..620
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..773
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436614.1:66..2387"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 mflllllvvh lnglqagqhp qktilqttvp ekisspdvet dpenhmayli tinenphfih
       61 lkkqsfitst avsytydrqd vrhsqslssl kncnyngyva gfpnsivslt vcsglrgmiq
      121 fenvsygiep vetlsgfihv iyentnqqak ipdlgenqty swsdeldyqf rsnmkksgfa
      181 vlrpryiktd ivvdkklfdy mgsdtrvvlq kviqiigfin tmfsklkltv linsveiwsk
      241 enridfpeap enllvqflhw khkyrpqhis yllafvehpa stgalypgnl ckpiygaaia
      301 lypkglsles ysvivlqlls igigltydna dschctgdvc lmtpkaiysg gvkdfstcsl
      361 ddfkylstqd leclqdlpme rqkkkpsrpr ricgngilem neqcdcgtlk ncthkkccdp
      421 mscrlkskav cgsgeccgqd ckvkpvnvlc rksknecdfe eycngndayc vpdtfarngq
      481 ycdsgqafcy sglcmtsnnq cmnllgkyvr gasfacyeef nsrndrfgnc irkfcsfens
      541 lcgklvctwp fkrllmkdnm saaygqirdd lcislykggr plkttlstys dmserdetfv
      601 kdgticgpdm fcletqcket rflvdfqqcn tsrdcndhgv cnnfnhchcd kgynppyces
      661 vkgqfgsidd ghkyyidegk sakqqnrgih pkqqlqlily itlplimiis avfikqskls
      721 rlcgrerseg tscitedsvs ntkmttnegr ssadppitpn perilnvfav kkh
//
LOCUS       NP_001100108             601 aa            linear   ROD 18-MAR-2025
DEFINITION  anion exchange transporter isoform b [Rattus norvegicus].
ACCESSION   NP_001100108 XP_001055767 XP_232793
VERSION     NP_001100108.1
DBSOURCE    REFSEQ: accession NM_001106638.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Kiriya,M., Kawashima,A., Fujiwara,Y., Tanimura,Y., Yoshihara,A.,
            Nakamura,Y., Tanigawa,K., Kondo,T. and Suzuki,K.
  TITLE     Thyroglobulin regulates the expression and localization of the
            novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes
  JOURNAL   Endocr J 69 (10), 1217-1225 (2022)
   PUBMED   35644541
  REMARK    GeneRIF: Thyroglobulin regulates the expression and localization of
            the novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Yin,K., Lei,Y., Wen,X., Lacruz,R.S., Soleimani,M., Kurtz,I.,
            Snead,M.L., White,S.N. and Paine,M.L.
  TITLE     SLC26A Gene Family Participate in pH Regulation during Enamel
            Maturation
  JOURNAL   PLoS One 10 (12), e0144703 (2015)
   PUBMED   26671068
  REMARK    GeneRIF: Slc26a1, Slc26a6 and Slc26a7 are novel participants in the
            extracellular transport of bicarbonate during enamel maturation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Sun,X. and Petrovic,S.
  TITLE     Increased acid load and deletion of AE1 increase Slc26a7 expression
  JOURNAL   Nephron Physiol 109 (3), p29-p35 (2008)
   PUBMED   18663336
  REMARK    GeneRIF: Suggest that the increase in Slc26a7 expression caused by
            acid challenge represents an adaptive response, indicating that
            Slc26a7 contributes to the regulation of acid-base balance by the
            kidney.
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Barone,S., Amlal,H., Kujala,M., Xu,J., Karet,F., Blanchard,A.,
            Kere,J. and Soleimani,M.
  TITLE     Regulation of the basolateral chloride/base exchangers AE1 and
            SLC26A7 in the kidney collecting duct in potassium depletion
  JOURNAL   Nephrol Dial Transplant 22 (12), 3462-3470 (2007)
   PUBMED   17804457
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Kosiek,O., Busque,S.M., Foller,M., Shcheynikov,N., Kirchhoff,P.,
            Bleich,M., Muallem,S. and Geibel,J.P.
  TITLE     SLC26A7 can function as a chloride-loading mechanism in parietal
            cells
  JOURNAL   Pflugers Arch 454 (6), 989-998 (2007)
   PUBMED   17404755
  REMARK    GeneRIF: SLC26A7 is a Cl(-) uptake system under histamine
            stimulation
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Petrovic,S., Amlal,H., Sun,X., Karet,F., Barone,S. and Soleimani,M.
  TITLE     Vasopressin induces expression of the Cl-/HCO3- exchanger SLC26A7
            in kidney medullary collecting ducts of Brattleboro rats
  JOURNAL   Am J Physiol Renal Physiol 290 (5), F1194-F1201 (2006)
   PUBMED   16352747
  REMARK    GeneRIF: vasopressin increases the expression of SLC26A7 protein
            through posttranscriptional mechanisms in the outer medullary
            collecting duct
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Kim,K.H., Shcheynikov,N., Wang,Y. and Muallem,S.
  TITLE     SLC26A7 is a Cl- channel regulated by intracellular pH
  JOURNAL   J Biol Chem 280 (8), 6463-6470 (2005)
   PUBMED   15591059
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Petrovic,S., Ju,X., Barone,S., Seidler,U., Alper,S.L., Lohi,H.,
            Kere,J. and Soleimani,M.
  TITLE     Identification of a basolateral Cl-/HCO3- exchanger specific to
            gastric parietal cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 284 (6), G1093-G1103 (2003)
   PUBMED   12736153
REFERENCE   9  (residues 1 to 601)
  AUTHORS   Lohi,H., Kujala,M., Makela,S., Lehtonen,E., Kestila,M.,
            Saarialho-Kere,U., Markovich,D. and Kere,J.
  TITLE     Functional characterization of three novel tissue-specific anion
            exchangers SLC26A7, -A8, and -A9
  JOURNAL   J Biol Chem 277 (16), 14246-14254 (2002)
   PUBMED   11834742
REFERENCE   10 (residues 1 to 601)
  AUTHORS   Mocellin,R. and Buhlmeyer,K.
  TITLE     Late banding operation in children with ventricular septal defect
            and pulmonary arterial hypertension
  JOURNAL   Eur J Cardiol 3 (3), 205-211 (1975)
   PUBMED   1183472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232793.3, XP_001055767.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..601
                     /product="anion exchange transporter isoform b"
                     /note="anion exchange transporter; solute carrier family
                     26 (anion exchanger), member 7"
                     /calculated_mol_wt=65808
     Region          33..582
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     CDS             1..601
                     /gene="Slc26a7"
                     /coded_by="NM_001106638.2:122..1927"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:297910"
                     /db_xref="RGD:1310846"
ORIGIN      
        1 mtgakrkkrs vlwgkmhtph redikqwckr rlpilewapq ynlkenllpd tvsgvllavq
       61 qvtqglsfai lssvhpvfgl ygslfpaiiy aifgmgrhva tgtfaltsli sanaverlvp
      121 qsnrnlttqs nssvlglsef elqrigvaaa vsflggviqi yayvfeniks vqlealllsl
      181 lsivvlvlvk elneqfkrki kvvlpvdlvl iiaasfacyc tnmentygle vvgripkgip
      241 pprappmnil savlteafgv alvgyvasla laqgsakkfk ysvddnqefl ahglsnvips
      301 flfcipsaaa mgrtaglyst gaktqvacli scifvliviy aigpllywlp mcvlasiivv
      361 glkgmliqfr dlkkywnvdk idwgiwisty ifticfaanv gllfgvvcti aivlgrfpra
      421 ktlsitdmke melkvktety densqqikii sinnplvfln akkfsadlmk iilketdgsq
      481 alddvskceq ntllsplpng scteeasqpc psekyslvln csgltffdyt gvstlvelyl
      541 dcksrsvdvf lanctaslik amtyygdldt ekpiffdsva taisviqsnk nlskdtdhse
      601 v
//
LOCUS       NP_001423553             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423553 XP_038965316
VERSION     NP_001423553.1
DBSOURCE    REFSEQ: accession NM_001436624.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038965316.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.14505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436624.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001423536             270 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform b [Rattus norvegicus].
ACCESSION   NP_001423536 XP_008761829
VERSION     NP_001423536.1
DBSOURCE    REFSEQ: accession NM_001436607.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_008761829.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.26911.1,
                                           SRR26360194.1011728.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..270
                     /product="aprataxin isoform b"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=30530
     Region          <1..42
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..268
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="Aptx"
                     /coded_by="NM_001436607.1:231..1043"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mgvnptside vvigkdremk llpgqvlhmv nelypymvef eevaespnvt qrkrkrpdcd
       61 sqemeaeaga spsqcsvspk tgkhgaakee slghwsqglk ismkdpkmqv ykddqvvvik
      121 dkypkarhhw lvlpwasiss lkvvtsehle llkhmhavge kviadftgss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa vikmvqeagr vtvkdgtcel
      241 lklplrchec qqllpsipql kehlrkhwgg
//
LOCUS       NP_001423584             601 aa            linear   ROD 18-MAR-2025
DEFINITION  anion exchange transporter isoform b [Rattus norvegicus].
ACCESSION   NP_001423584 XP_008761753
VERSION     NP_001423584.1
DBSOURCE    REFSEQ: accession NM_001436655.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Kiriya,M., Kawashima,A., Fujiwara,Y., Tanimura,Y., Yoshihara,A.,
            Nakamura,Y., Tanigawa,K., Kondo,T. and Suzuki,K.
  TITLE     Thyroglobulin regulates the expression and localization of the
            novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes
  JOURNAL   Endocr J 69 (10), 1217-1225 (2022)
   PUBMED   35644541
  REMARK    GeneRIF: Thyroglobulin regulates the expression and localization of
            the novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Yin,K., Lei,Y., Wen,X., Lacruz,R.S., Soleimani,M., Kurtz,I.,
            Snead,M.L., White,S.N. and Paine,M.L.
  TITLE     SLC26A Gene Family Participate in pH Regulation during Enamel
            Maturation
  JOURNAL   PLoS One 10 (12), e0144703 (2015)
   PUBMED   26671068
  REMARK    GeneRIF: Slc26a1, Slc26a6 and Slc26a7 are novel participants in the
            extracellular transport of bicarbonate during enamel maturation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Sun,X. and Petrovic,S.
  TITLE     Increased acid load and deletion of AE1 increase Slc26a7 expression
  JOURNAL   Nephron Physiol 109 (3), p29-p35 (2008)
   PUBMED   18663336
  REMARK    GeneRIF: Suggest that the increase in Slc26a7 expression caused by
            acid challenge represents an adaptive response, indicating that
            Slc26a7 contributes to the regulation of acid-base balance by the
            kidney.
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Barone,S., Amlal,H., Kujala,M., Xu,J., Karet,F., Blanchard,A.,
            Kere,J. and Soleimani,M.
  TITLE     Regulation of the basolateral chloride/base exchangers AE1 and
            SLC26A7 in the kidney collecting duct in potassium depletion
  JOURNAL   Nephrol Dial Transplant 22 (12), 3462-3470 (2007)
   PUBMED   17804457
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Kosiek,O., Busque,S.M., Foller,M., Shcheynikov,N., Kirchhoff,P.,
            Bleich,M., Muallem,S. and Geibel,J.P.
  TITLE     SLC26A7 can function as a chloride-loading mechanism in parietal
            cells
  JOURNAL   Pflugers Arch 454 (6), 989-998 (2007)
   PUBMED   17404755
  REMARK    GeneRIF: SLC26A7 is a Cl(-) uptake system under histamine
            stimulation
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Petrovic,S., Amlal,H., Sun,X., Karet,F., Barone,S. and Soleimani,M.
  TITLE     Vasopressin induces expression of the Cl-/HCO3- exchanger SLC26A7
            in kidney medullary collecting ducts of Brattleboro rats
  JOURNAL   Am J Physiol Renal Physiol 290 (5), F1194-F1201 (2006)
   PUBMED   16352747
  REMARK    GeneRIF: vasopressin increases the expression of SLC26A7 protein
            through posttranscriptional mechanisms in the outer medullary
            collecting duct
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Kim,K.H., Shcheynikov,N., Wang,Y. and Muallem,S.
  TITLE     SLC26A7 is a Cl- channel regulated by intracellular pH
  JOURNAL   J Biol Chem 280 (8), 6463-6470 (2005)
   PUBMED   15591059
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Petrovic,S., Ju,X., Barone,S., Seidler,U., Alper,S.L., Lohi,H.,
            Kere,J. and Soleimani,M.
  TITLE     Identification of a basolateral Cl-/HCO3- exchanger specific to
            gastric parietal cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 284 (6), G1093-G1103 (2003)
   PUBMED   12736153
REFERENCE   9  (residues 1 to 601)
  AUTHORS   Lohi,H., Kujala,M., Makela,S., Lehtonen,E., Kestila,M.,
            Saarialho-Kere,U., Markovich,D. and Kere,J.
  TITLE     Functional characterization of three novel tissue-specific anion
            exchangers SLC26A7, -A8, and -A9
  JOURNAL   J Biol Chem 277 (16), 14246-14254 (2002)
   PUBMED   11834742
REFERENCE   10 (residues 1 to 601)
  AUTHORS   Mocellin,R. and Buhlmeyer,K.
  TITLE     Late banding operation in children with ventricular septal defect
            and pulmonary arterial hypertension
  JOURNAL   Eur J Cardiol 3 (3), 205-211 (1975)
   PUBMED   1183472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_008761753.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1648969.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..601
                     /product="anion exchange transporter isoform b"
                     /note="anion exchange transporter; solute carrier family
                     26 (anion exchanger), member 7"
                     /calculated_mol_wt=65808
     Region          33..582
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     CDS             1..601
                     /gene="Slc26a7"
                     /coded_by="NM_001436655.1:214..2019"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:297910"
                     /db_xref="RGD:1310846"
ORIGIN      
        1 mtgakrkkrs vlwgkmhtph redikqwckr rlpilewapq ynlkenllpd tvsgvllavq
       61 qvtqglsfai lssvhpvfgl ygslfpaiiy aifgmgrhva tgtfaltsli sanaverlvp
      121 qsnrnlttqs nssvlglsef elqrigvaaa vsflggviqi yayvfeniks vqlealllsl
      181 lsivvlvlvk elneqfkrki kvvlpvdlvl iiaasfacyc tnmentygle vvgripkgip
      241 pprappmnil savlteafgv alvgyvasla laqgsakkfk ysvddnqefl ahglsnvips
      301 flfcipsaaa mgrtaglyst gaktqvacli scifvliviy aigpllywlp mcvlasiivv
      361 glkgmliqfr dlkkywnvdk idwgiwisty ifticfaanv gllfgvvcti aivlgrfpra
      421 ktlsitdmke melkvktety densqqikii sinnplvfln akkfsadlmk iilketdgsq
      481 alddvskceq ntllsplpng scteeasqpc psekyslvln csgltffdyt gvstlvelyl
      541 dcksrsvdvf lanctaslik amtyygdldt ekpiffdsva taisviqsnk nlskdtdhse
      601 v
//
LOCUS       NP_001423571             417 aa            linear   ROD 18-MAR-2025
DEFINITION  zinc finger protein PLAG1 isoform b [Rattus norvegicus].
ACCESSION   NP_001423571 XP_017448713
VERSION     NP_001423571.1
DBSOURCE    REFSEQ: accession NM_001436642.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Gu,Q. and Wei,H.F.
  TITLE     PLAG1 Promotes High Glucose-Induced Angiogenesis and Migration of
            Retinal Endothelial Cells by Regulating the Wnt/beta-Catenin
            Signalling Pathway
  JOURNAL   Folia Biol (Praha) 68 (1), 25-32 (2022)
   PUBMED   36201855
  REMARK    GeneRIF: PLAG1 Promotes High Glucose-Induced Angiogenesis and
            Migration of Retinal Endothelial Cells by Regulating the
            Wnt/beta-Catenin Signalling Pathway.
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Hide,T., Takezaki,T., Nakatani,Y., Nakamura,H., Kuratsu,J. and
            Kondo,T.
  TITLE     Sox11 prevents tumorigenesis of glioma-initiating cells by inducing
            neuronal differentiation
  JOURNAL   Cancer Res 69 (20), 7953-7959 (2009)
   PUBMED   19808959
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Hensen,K., Braem,C., Declercq,J., Van Dyck,F., Dewerchin,M.,
            Fiette,L., Denef,C. and Van de Ven,W.J.
  TITLE     Targeted disruption of the murine Plag1 proto-oncogene causes
            growth retardation and reduced fertility
  JOURNAL   Dev Growth Differ 46 (5), 459-470 (2004)
   PUBMED   15606491
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Voz,M.L., Agten,N.S., Van de Ven,W.J. and Kas,K.
  TITLE     PLAG1, the main translocation target in pleomorphic adenoma of the
            salivary glands, is a positive regulator of IGF-II
  JOURNAL   Cancer Res 60 (1), 106-113 (2000)
   PUBMED   10646861
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Astrom,A.K., Voz,M.L., Kas,K., Roijer,E., Wedell,B., Mandahl,N.,
            Van de Ven,W., Mark,J. and Stenman,G.
  TITLE     Conserved mechanism of PLAG1 activation in salivary gland tumors
            with and without chromosome 8q12 abnormalities: identification of
            SII as a new fusion partner gene
  JOURNAL   Cancer Res 59 (4), 918-923 (1999)
   PUBMED   10029085
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_017448713.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.128547.1,
                                           SRR26360172.872299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..417
                     /product="zinc finger protein PLAG1 isoform b"
                     /note="zinc finger protein PLAG1; pleiomorphic adenoma
                     gene 1 protein"
                     /calculated_mol_wt=46134
     Region          10..>58
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          12..38
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          12..32
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(17,27,34,36,40,47)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          41..61
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          41..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          70..90
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(70,73,86,90)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(75,77,79,81..82,85..86,89,110,112,116..117,120..121,
                     124,138,140,142,144..145,148..149)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          105..125
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..151
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..417
                     /gene="Plag1"
                     /coded_by="NM_001436642.1:390..1643"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:297804"
                     /db_xref="RGD:1305286"
ORIGIN      
        1 mathspekth kcnycekmfh rkdhlknhlh thdpnketfk ceecgksynt klgfkrhlal
       61 haatsgdltc kvclqtfest gvllehlksh agkssggvke kkhqcehcer rfytrkdvrr
      121 hmvvhtgrkd flcqycaqrf grkdhltrhm kkshnqellk vktepvdfld pftcnmsvpi
      181 kdellpvmsl pssellskpf tntlqlnlyn tpfqsmqssg sthqmittlp lgmtcpidmd
      241 tvhpshhlaf kcpfsstsya isipekeqpl kgeiesylme lqggapsssq dsqasssklg
      301 lepqsgspdd gagdlslsks sisisdplnt paldfsqlfn fiplngppyn plsvgslgms
      361 ysqdeahssv sqlptqtqdl qdpantvglg slhslsaaft sslsssttlp rfhqafq
//
LOCUS       NP_001423552             660 aa            linear   ROD 18-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423552 XP_006237783
VERSION     NP_001423552.1
DBSOURCE    REFSEQ: accession NM_001436623.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237783.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.14512.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436623.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001008317             499 aa            linear   ROD 18-MAR-2025
DEFINITION  zinc finger protein PLAG1 isoform a [Rattus norvegicus].
ACCESSION   NP_001008317 XP_232651
VERSION     NP_001008317.1
DBSOURCE    REFSEQ: accession NM_001008316.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gu,Q. and Wei,H.F.
  TITLE     PLAG1 Promotes High Glucose-Induced Angiogenesis and Migration of
            Retinal Endothelial Cells by Regulating the Wnt/beta-Catenin
            Signalling Pathway
  JOURNAL   Folia Biol (Praha) 68 (1), 25-32 (2022)
   PUBMED   36201855
  REMARK    GeneRIF: PLAG1 Promotes High Glucose-Induced Angiogenesis and
            Migration of Retinal Endothelial Cells by Regulating the
            Wnt/beta-Catenin Signalling Pathway.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hide,T., Takezaki,T., Nakatani,Y., Nakamura,H., Kuratsu,J. and
            Kondo,T.
  TITLE     Sox11 prevents tumorigenesis of glioma-initiating cells by inducing
            neuronal differentiation
  JOURNAL   Cancer Res 69 (20), 7953-7959 (2009)
   PUBMED   19808959
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hensen,K., Braem,C., Declercq,J., Van Dyck,F., Dewerchin,M.,
            Fiette,L., Denef,C. and Van de Ven,W.J.
  TITLE     Targeted disruption of the murine Plag1 proto-oncogene causes
            growth retardation and reduced fertility
  JOURNAL   Dev Growth Differ 46 (5), 459-470 (2004)
   PUBMED   15606491
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Voz,M.L., Agten,N.S., Van de Ven,W.J. and Kas,K.
  TITLE     PLAG1, the main translocation target in pleomorphic adenoma of the
            salivary glands, is a positive regulator of IGF-II
  JOURNAL   Cancer Res 60 (1), 106-113 (2000)
   PUBMED   10646861
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Astrom,A.K., Voz,M.L., Kas,K., Roijer,E., Wedell,B., Mandahl,N.,
            Van de Ven,W., Mark,J. and Stenman,G.
  TITLE     Conserved mechanism of PLAG1 activation in salivary gland tumors
            with and without chromosome 8q12 abnormalities: identification of
            SII as a new fusion partner gene
  JOURNAL   Cancer Res 59 (4), 918-923 (1999)
   PUBMED   10029085
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Dec 16, 2004 this sequence version replaced XP_232651.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085871.1, CK601489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..499
                     /product="zinc finger protein PLAG1 isoform a"
                     /note="zinc finger protein PLAG1; pleiomorphic adenoma
                     gene 1 protein"
                     /calculated_mol_wt=55509
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          2..84
                     /region_name="Interaction with KPNA2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          22..25
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          36..56
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          41..242
                     /region_name="Decreased nuclear import with localization
                     in the nucleus but also in the cytoplasm.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Site            order(41,43,45,47..48,51..52,55,71,73,77..78,81..82,85,99,
                     101,103,105..106,109..110,113)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <58..139
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          64..86
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          79..101
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          94..114
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          123..143
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(157,159,161,163..164,167..168,171,192,194,198..199,
                     202..203,206,220,222,224,226..227,230..231)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          215..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..499
                     /region_name="Activates transcription, Inhibition of
                     nuclear import due to lack of NLS and KPNA2 interaction.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          243..383
                     /region_name="Repression domain, contains 3 sumoylation
                     motifs and massively decrease transcription activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          364..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          384..499
                     /region_name="Massively activates transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     CDS             1..499
                     /gene="Plag1"
                     /coded_by="NM_001008316.3:385..1884"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:297804"
                     /db_xref="RGD:1305286"
ORIGIN      
        1 matvipgdls evrdtqkaps gkrkrgeskp rknfpcqlcd kafnsveklk vhsfshtger
       61 pykcthqdct kafvskyklq rhmathspek thkcnycekm fhrkdhlknh lhthdpnket
      121 fkceecgksy ntklgfkrhl alhaatsgdl tckvclqtfe stgvllehlk shagkssggv
      181 kekkhqcehc errfytrkdv rrhmvvhtgr kdflcqycaq rfgrkdhltr hmkkshnqel
      241 lkvktepvdf ldpftcnmsv pikdellpvm slpssellsk pftntlqlnl yntpfqsmqs
      301 sgsthqmitt lplgmtcpid mdtvhpshhl afkcpfssts yaisipekeq plkgeiesyl
      361 melqggapss sqdsqasssk lglepqsgsp ddgagdlsls kssisisdpl ntpaldfsql
      421 fnfiplngpp ynplsvgslg msysqdeahs svsqlptqtq dlqdpantvg lgslhslsaa
      481 ftsslssstt lprfhqafq
//
LOCUS       NP_001423535             329 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform a [Rattus norvegicus].
ACCESSION   NP_001423535
VERSION     NP_001423535.1
DBSOURCE    REFSEQ: accession NM_001436606.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2248930.1,
                                           SRR26360181.2645223.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..329
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=37589
     Region          1..95
                     /region_name="Interactions with ADPRT/PARP1 and NCL.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          2..101
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(27..28,40..41,43,63..64)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          106..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          111..115
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQC5; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          151..252
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            161
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          180..184
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            238
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          242..243
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            order(245,247,249..251)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Region          245..249
                     /region_name="Histidine triad motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Site            249
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            264
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          270..327
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..329
                     /gene="Aptx"
                     /coded_by="NM_001436606.1:312..1301"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mrvcwlvrqd cwhqriklph leavvigrsp etkitdkkcs rqqvqlkaec nkryvnvkqm
       61 gvnptsidev vigkdremkl lpgqvlhmvn elypymvefe evaespnvtq rkrkrpdcds
      121 qemeaeagas psqcsvspkt gkhgaakees lghwsqglki smkdpkmqvy kddqvvvikd
      181 kypkarhhwl vlpwasissl kvvtsehlel lkhmhavgek viadftgssk lrfrlgyhai
      241 psmshvhlhv isqdfdspcl knkkhwnsfn teyflesqav ikmvqeagrv tvkdgtcell
      301 klplrchecq qllpsipqlk ehlrkhwgg
//
LOCUS       NP_001423581             405 aa            linear   ROD 18-MAR-2025
DEFINITION  zinc finger protein 362 isoform b [Rattus norvegicus].
ACCESSION   NP_001423581 XP_038965343
VERSION     NP_001423581.1
DBSOURCE    REFSEQ: accession NM_001436652.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038965343.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.30256.1,
                                           SRR26643295.22787.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..405
                     /product="zinc finger protein 362 isoform b"
                     /calculated_mol_wt=44226
     Region          <14..>118
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..251
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          240..262
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(247,249,251,253..254,257..258,261,275,277,281..282,
                     285..286,289,305,307,309,311..312,315..316,319)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          254..279
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <292..344
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          298..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..348
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          360..378
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..405
                     /gene="Zfp362"
                     /gene_synonym="RGD1306498"
                     /coded_by="NM_001436652.1:316..1533"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:297879"
                     /db_xref="RGD:1306498"
ORIGIN      
        1 maeprfnnpy fwpppptmps qldnlvlink ikeqlmaeki rpphlpptsa ssqqpllvpp
       61 apaessqavm slpklqqvpg lhpqsvpqpd valharpats tvtglglssr tpavstsest
      121 pgtgtgtstp stptttsqsr liassptlis gitsppllds iktiqghgll gppksergrk
      181 kikaenpggp pvlvvpypil asgetakegk tyrckvcplt fftksemqih skshteakph
      241 kcphcsksfa nasylaqhlr ihlgvkpyhc sycdksfrql shlqqhtrih tgdrpykcph
      301 pgcekaftql snlqshqrqh nkdkpykcpn cyraysdsas lqihlsahai khakayccsm
      361 cgraytsety lmkhmskhtv vehlvshhsp qrtespgipv risli
//
LOCUS       NP_001423575             530 aa            linear   ROD 18-MAR-2025
DEFINITION  chondroitin sulfate N-acetylgalactosaminyltransferase 1 [Rattus
            norvegicus].
ACCESSION   NP_001423575 XP_008769336
VERSION     NP_001423575.1
DBSOURCE    REFSEQ: accession NM_001436646.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Sato,T., Kudo,T., Ikehara,Y., Ogawa,H., Hirano,T., Kiyohara,K.,
            Hagiwara,K., Togayachi,A., Ema,M., Takahashi,S., Kimata,K.,
            Watanabe,H. and Narimatsu,H.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is
            necessary for normal endochondral ossification and aggrecan
            metabolism
  JOURNAL   J Biol Chem 286 (7), 5803-5812 (2011)
   PUBMED   21148564
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Watanabe,Y., Takeuchi,K., Higa Onaga,S., Sato,M., Tsujita,M.,
            Abe,M., Natsume,R., Li,M., Furuichi,T., Saeki,M., Izumikawa,T.,
            Hasegawa,A., Yokoyama,M., Ikegawa,S., Sakimura,K., Amizuka,N.,
            Kitagawa,H. and Igarashi,M.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required
            for normal cartilage development
  JOURNAL   Biochem J 432 (1), 47-55 (2010)
   PUBMED   20812917
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Gotoh,M., Sato,T., Akashima,T., Iwasaki,H., Kameyama,A.,
            Mochizuki,H., Yada,T., Inaba,N., Zhang,Y., Kikuchi,N., Kwon,Y.D.,
            Togayachi,A., Kudo,T., Nishihara,S., Watanabe,H., Kimata,K. and
            Narimatsu,H.
  TITLE     Enzymatic synthesis of chondroitin with a novel chondroitin sulfate
            N-acetylgalactosaminyltransferase that transfers
            N-acetylgalactosamine to glucuronic acid in initiation and
            elongation of chondroitin sulfate synthesis
  JOURNAL   J Biol Chem 277 (41), 38189-38196 (2002)
   PUBMED   12163485
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Kitagawa,H., Uyama,T. and Sugahara,K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase
  JOURNAL   J Biol Chem 276 (42), 38721-38726 (2001)
   PUBMED   11514575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_008769336.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50404.1,
                                           SRR26643289.38253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..530
                     /product="chondroitin sulfate
                     N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.174"
                     /note="chondroitin beta1,4
                     N-acetylgalactosaminyltransferase"
                     /calculated_mol_wt=60770
     Region          68..505
                     /region_name="CHGN"
                     /note="Chondroitin N-acetylgalactosaminyltransferase;
                     pfam05679"
                     /db_xref="CDD:461712"
     CDS             1..530
                     /gene="Csgalnact1"
                     /gene_synonym="Chgn; RGD1307618"
                     /coded_by="NM_001436646.1:708..2300"
                     /db_xref="GeneID:306375"
                     /db_xref="RGD:1307618"
ORIGIN      
        1 mvrrglvgwi srvvillvll ccaisvlyml actpkgdqeq lglprangpt gkdgyqavlq
       61 ereeqhrnyv nslkrqiaql kdelqarseq lrsgqdqasd atslrsgwdp epkaqadila
      121 flrgqvdkae vhagvklate yaavpfdsft lqkvyqletg ltrhpeekpv rkdkrdelve
      181 aiesalesln spvessphqr pytaadfieg iyrterdkgt lyeltfkgdh khefqrlvlf
      241 rpfgpimkvk keklnmantl invivplarr vdkfrhfmqn fremciqqdg rvhltvvyfg
      301 keemnevkgi lentskaanf rnftfiqlng efsrgkgldv garfwkgsnv vlffcdvdiy
      361 ftseflntcr lntqpgkkvf ypvlfsqynp giiyghhdav paleqqlvik ketgfwrdfg
      421 fgmtcqyrsd finiggfdld ikgwggedvh lyrkylhsnl ivirtpvrgl fhlwhekhcm
      481 deltpeqyrm cmqskamnea shgqlgmlvf rheieahlrk qklkasskkt
//
LOCUS       NP_001423587             425 aa            linear   ROD 18-MAR-2025
DEFINITION  probable G-protein coupled receptor 63 [Rattus norvegicus].
ACCESSION   NP_001423587 XP_038965352
VERSION     NP_001423587.1
DBSOURCE    REFSEQ: accession NM_001436658.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_038965352.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3033962.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN12840122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..425
                     /product="probable G-protein coupled receptor 63"
                     /calculated_mol_wt=47887
     Region          88..388
                     /region_name="7tmA_GPR63"
                     /note="G protein-coupled receptor 63, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15404"
                     /db_xref="CDD:320526"
     Region          89..115
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320526"
     Region          122..147
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320526"
     Site            order(144,147..148,160..165,167..168,171,213,215..219,245,
                     248..250,252..254,256..257,333,336..337,339..340,343,
                     355..356,358..360,363,366..367)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320526"
     Region          160..190
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320526"
     Region          199..221
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320526"
     Region          245..274
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320526"
     Region          313..343
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320526"
     Region          356..381
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320526"
     CDS             1..425
                     /gene="Gpr63"
                     /coded_by="NM_001436658.1:373..1650"
                     /db_xref="GeneID:297952"
                     /db_xref="RGD:1306460"
ORIGIN      
        1 mvvsgvltap avlttphtgt snmtfvvyen spmnitaplp fqhpspgpll rysletmtst
       61 gfsslavnst vvtpapavfk slnlalqiil saimifilfv sflgnlvvcl mvyqkaamrs
      121 ainillasma fadmllavln mpfalvtilt trwifgkffc rlsamffwlf viegvailli
      181 isidrfliiv qrqdklnpyr akvliavswa tafsvafpla vgnpdlqips rapqcvfgyt
      241 tnsgyqayvi lislisffip flvilysfmg ilntlrhnal rihsypegic lsqvsklglm
      301 slqrpfqmsi dmsfktraft tililfavfi vcwapfttys lvatfskhfy yqhnffeist
      361 wllwlcylks alnpliyywr ikkfhdacld mmpksfkflp rlpghtrrri rpsavyvcge
      421 hrtvl
//
LOCUS       NP_001423546             488 aa            linear   ROD 18-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423546
VERSION     NP_001423546.1
DBSOURCE    REFSEQ: accession NM_001436617.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1584371.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..488
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 6"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=54420
     Region          <10..113
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          134..208
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          212..355
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..488
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436617.1:1187..2653"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 mthyinigrf vehpastgal ypgnlckpiy gaaialypkg lslesysviv lqllsigigl
       61 tydnadschc tgdvclmtpk aiysggvkdf stcslddfky lstqdleclq dlpmerqkkk
      121 psrprricgn gilemneqcd cgtlkncthk kccdpmscrl kskavcgsge ccgqdckvkp
      181 vnvlcrkskn ecdfeeycng ndaycvpdtf arngqycdsg qafcysglcm tsnnqcmnll
      241 gkyvrgasfa cyeefnsrnd rfgncirkfc sfenslcgkl vctwpfkrll mkdnmsaayg
      301 qirddlcisl ykggrplktt lstysdmser detfvkdgti cgpdmfclet qcketrflvd
      361 fqqcntsrdc ndhgvcnnfn hchcdkgynp pycesvkgqf gsiddghkyy idegksakqq
      421 nrgihpkqql qlilyitlpl imiisavfik qsklsrlcgr ersegtscit edsvsntkmt
      481 tnegstlh
//
LOCUS       NP_001423522             236 aa            linear   ROD 18-MAR-2025
DEFINITION  clathrin light chain A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423522 XP_006238166
VERSION     NP_001423522.1
DBSOURCE    REFSEQ: accession NM_001436593.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Li,H., Alavian,K.N., Lazrove,E., Mehta,N., Jones,A., Zhang,P.,
            Licznerski,P., Graham,M., Uo,T., Guo,J., Rahner,C., Duman,R.S.,
            Morrison,R.S. and Jonas,E.A.
  TITLE     A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
            during endocytosis
  JOURNAL   Nat Cell Biol 15 (7), 773-785 (2013)
   PUBMED   23792689
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Bu,W., Lim,K.B., Yu,Y.H., Chou,A.M., Sudhaharan,T. and Ahmed,S.
  TITLE     Cdc42 interaction with N-WASP and Toca-1 regulates membrane
            tubulation, vesicle formation and vesicle motility: implications
            for endocytosis
  JOURNAL   PLoS One 5 (8), e12153 (2010)
   PUBMED   20730103
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Mettlen,M., Loerke,D., Yarar,D., Danuser,G. and Schmid,S.L.
  TITLE     Cargo- and adaptor-specific mechanisms regulate clathrin-mediated
            endocytosis
  JOURNAL   J Cell Biol 188 (6), 919-933 (2010)
   PUBMED   20231386
  REMARK    GeneRIF: The results underscore the highly dynamic and
            cargo-responsive nature of CCP assembly and suggest that the
            observed heterogeneity is, in part, related to compositional
            differences (e.g., cargo and adaptors) between CCPs.
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Drake,M.T., Downs,M.A. and Traub,L.M.
  TITLE     Epsin binds to clathrin by associating directly with the
            clathrin-terminal domain. Evidence for cooperative binding through
            two discrete sites
  JOURNAL   J Biol Chem 275 (9), 6479-6489 (2000)
   PUBMED   10692452
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Saito,Y., Tsubuki,S., Ito,H., Ohmi-Imajo,S. and Kawashima,S.
  TITLE     Possible involvement of clathrin in neuritogenesis induced by a
            protease inhibitor (benzyloxycarbonyl-Leu-Leu-Leu-aldehyde) in PC12
            cells
  JOURNAL   J Biochem 112 (4), 448-455 (1992)
   PUBMED   1490999
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Maycox,P.R., Link,E., Reetz,A., Morris,S.A. and Jahn,R.
  TITLE     Clathrin-coated vesicles in nervous tissue are involved primarily
            in synaptic vesicle recycling
  JOURNAL   J Cell Biol 118 (6), 1379-1388 (1992)
   PUBMED   1325974
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Kirchhausen,T., Scarmato,P., Harrison,S.C., Monroe,J.J., Chow,E.P.,
            Mattaliano,R.J., Ramachandran,K.L., Smart,J.E., Ahn,A.H. and
            Brosius,J.
  TITLE     Clathrin light chains LCA and LCB are similar, polymorphic, and
            share repeated heptad motifs
  JOURNAL   Science 236 (4799), 320-324 (1987)
   PUBMED   3563513
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Brodsky,F.M.
  TITLE     Clathrin structure characterized with monoclonal antibodies. II.
            Identification of in vivo forms of clathrin
  JOURNAL   J Cell Biol 101 (6), 2055-2062 (1985)
   PUBMED   4066749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238166.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M19260.1, FQ213766.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..236
                     /product="clathrin light chain A isoform 3"
                     /note="clathrin, light polypeptide (Lca); clathrin, light
                     chain (Lca); lca"
                     /calculated_mol_wt=25449
     Region          22..236
                     /region_name="Clathrin_lg_ch"
                     /note="Clathrin light chain; pfam01086"
                     /db_xref="CDD:460056"
     CDS             1..236
                     /gene="Clta"
                     /gene_synonym="LCA1; LCA2; LCA3"
                     /coded_by="NM_001436593.1:124..834"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:83800"
                     /db_xref="RGD:70919"
ORIGIN      
        1 maeldpfgap agapggpalg ngvagageed paaaflaqqe seiagiende afaildggap
       61 gpqahgeppg gpdavdgvmn geyyqesngp tdsyaaisev drlqsepesi rkwreeqter
      121 lealdansrk qeaewkekav keleewyarq deqlqktkas nrvadeafyk qpfadvigyv
      181 aaeeafvndi desspgtewe rvarlcdfnp ksskqakdvs rmrsvlislk qaplvh
//
LOCUS       NP_001423540             270 aa            linear   ROD 18-MAR-2025
DEFINITION  aprataxin isoform b [Rattus norvegicus].
ACCESSION   NP_001423540
VERSION     NP_001423540.1
DBSOURCE    REFSEQ: accession NM_001436611.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2043703.1,
                                           SRR26360194.2450395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..270
                     /product="aprataxin isoform b"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=30530
     Region          <1..42
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..268
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="Aptx"
                     /coded_by="NM_001436611.1:236..1048"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mgvnptside vvigkdremk llpgqvlhmv nelypymvef eevaespnvt qrkrkrpdcd
       61 sqemeaeaga spsqcsvspk tgkhgaakee slghwsqglk ismkdpkmqv ykddqvvvik
      121 dkypkarhhw lvlpwasiss lkvvtsehle llkhmhavge kviadftgss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa vikmvqeagr vtvkdgtcel
      241 lklplrchec qqllpsipql kehlrkhwgg
//
LOCUS       NP_001100104             309 aa            linear   ROD 18-MAR-2025
DEFINITION  epidermal retinol dehydrogenase 2 [Rattus norvegicus].
ACCESSION   NP_001100104 XP_001069656 XP_216325
VERSION     NP_001100104.1
DBSOURCE    REFSEQ: accession NM_001106634.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Takahashi,Y., Moiseyev,G., Farjo,K. and Ma,J.X.
  TITLE     Characterization of key residues and membrane association domains
            in retinol dehydrogenase 10
  JOURNAL   Biochem J 419 (1), 113-122 (2009)
   PUBMED   19102727
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Lee,S.A., Belyaeva,O.V. and Kedishvili,N.Y.
  TITLE     Biochemical characterization of human epidermal retinol
            dehydrogenase 2
  JOURNAL   Chem Biol Interact 178 (1-3), 182-187 (2009)
   PUBMED   18926804
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Markova,N.G., Pinkas-Sarafova,A. and Simon,M.
  TITLE     A metabolic enzyme of the short-chain dehydrogenase/reductase
            superfamily may moonlight in the nucleus as a repressor of promoter
            activity
  JOURNAL   J Invest Dermatol 126 (9), 2019-2031 (2006)
   PUBMED   16691198
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Matsuzaka,Y., Okamoto,K., Tsuji,H., Mabuchi,T., Ozawa,A., Tamiya,G.
            and Inoko,H.
  TITLE     Identification of the hRDH-E2 gene, a novel member of the SDR
            family, and its increased expression in psoriatic lesion
  JOURNAL   Biochem Biophys Res Commun 297 (5), 1171-1180 (2002)
   PUBMED   12372410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473984.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_216325.3, XP_001069656.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMN06621351
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..309
                     /product="epidermal retinol dehydrogenase 2"
                     /EC_number="1.1.1.105"
                     /note="epidermal retinal dehydrogenase 2; retinal short
                     chain dehydrogenase reductase 2"
                     /calculated_mol_wt=34010
     Region          42..284
                     /region_name="17beta-HSDXI-like_SDR_c"
                     /note="human 17-beta-hydroxysteroid dehydrogenase XI-like,
                     classical (c) SDRs; cd05339"
                     /db_xref="CDD:187598"
     Site            order(47,49..52,71..73,97..99,125..127,148,175..177,190,
                     194,223..226,228..229)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187598"
     Site            order(102,106,138..139,142..143,146,150..151,154..155,158,
                     187..189,191..192,195..196,199..200,202..204,206..207,
                     229..231,273..274,277,281)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187598"
     Site            order(149,177,190,194)
                     /site_type="active"
                     /db_xref="CDD:187598"
     Site            order(158,161,204,207,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187598"
     CDS             1..309
                     /gene="Sdr16c5"
                     /gene_synonym="Rdhe2; RGD1565999"
                     /coded_by="NM_001106634.1:220..1149"
                     /db_xref="GeneID:297805"
                     /db_xref="RGD:1565999"
ORIGIN      
        1 mpcnlesakd llvflgksll sileallshv iskprknvag evvlitgags glgrllalqf
       61 arlgsvlvlw dvnketneet rqiaqeagai rvhaytcdcs qreevyrvad qvkkevgdvs
      121 ilinnagivt grkfldcpdd lmeksldvnf kahlwmykaf lpamiannhg hlvcisssag
      181 ligvnglsdy caskfaalgf aesmfvetla qkqrgiktti vcpffiktgm fegcttkcpn
      241 llpildpeya vrkivdailq eqlylympkf lyfimflksf lpiktgilia dylglfhvmd
      301 gftgqkkks
//
LOCUS       NP_001033688             393 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1B2 [Rattus norvegicus].
ACCESSION   NP_001033688
VERSION     NP_001033688.2
DBSOURCE    REFSEQ: accession NM_001038599.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 20, 2007 this sequence version replaced NP_001033688.1.
            
            Transcript Variant: This variant (MOR-1B2) lacks several exons and
            contains an alternate terminal exon compared to variant MOR-1C2.
            The encoded isoform (1B2) is shorter than isoform 1C2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY309003.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..393
                     /product="mu-type opioid receptor isoform 1B2"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=43855
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..393
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001038599.2:208..1389"
                     /note="isoform 1B2 is encoded by transcript variant
                     MOR-1B2"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqepqs vet
//
LOCUS       NP_777353                708 aa            linear   ROD 18-MAR-2025
DEFINITION  nicastrin precursor [Rattus norvegicus].
ACCESSION   NP_777353
VERSION     NP_777353.1
DBSOURCE    REFSEQ: accession NM_174864.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Dursun,E. and Gezen-Ak,D.
  TITLE     Vitamin D receptor is present on the neuronal plasma membrane and
            is co-localized with amyloid precursor protein, ADAM10 or Nicastrin
  JOURNAL   PLoS One 12 (11), e0188605 (2017)
   PUBMED   29176823
  REMARK    GeneRIF: These results demonstrated the localization of VDR on the
            neuronal plasma membrane and the co-localization of VDR and APP or
            ADAM10 or Nicastrin and limited co-localization of VDR and PS1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Dries,D.R., Zhu,Y., Brooks,M.M., Forero,D.A., Adachi,M., Cenik,B.,
            West,J.M., Han,Y.H., Yu,C., Arbella,J., Nordin,A., Adolfsson,R.,
            Del-Favero,J., Lu,Q.R., Callaerts,P., Birnbaum,S.G. and Yu,G.
  TITLE     Loss of Nicastrin from Oligodendrocytes Results in Hypomyelination
            and Schizophrenia with Compulsive Behavior
  JOURNAL   J Biol Chem 291 (22), 11647-11656 (2016)
   PUBMED   27008863
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Bai,X.C., Yan,C., Yang,G., Lu,P., Ma,D., Sun,L., Zhou,R.,
            Scheres,S.H.W. and Shi,Y.
  TITLE     An atomic structure of human gamma-secretase
  JOURNAL   Nature 525 (7568), 212-217 (2015)
   PUBMED   26280335
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Teranishi,Y., Inoue,M., Yamamoto,N.G., Kihara,T., Wiehager,B.,
            Ishikawa,T., Winblad,B., Schedin-Weiss,S., Frykman,S. and
            Tjernberg,L.O.
  TITLE     Proton myo-inositol cotransporter is a novel gamma-secretase
            associated protein that regulates Abeta production without
            affecting Notch cleavage
  JOURNAL   FEBS J 282 (17), 3438-3451 (2015)
   PUBMED   26094765
  REMARK    Review article
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Kizuka,Y., Kitazume,S., Fujinawa,R., Saito,T., Iwata,N.,
            Saido,T.C., Nakano,M., Yamaguchi,Y., Hashimoto,Y., Staufenbiel,M.,
            Hatsuta,H., Murayama,S., Manya,H., Endo,T. and Taniguchi,N.
  TITLE     An aberrant sugar modification of BACE1 blocks its lysosomal
            targeting in Alzheimer's disease
  JOURNAL   EMBO Mol Med 7 (2), 175-189 (2015)
   PUBMED   25592972
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Pasternak,S.H., Bagshaw,R.D., Guiral,M., Zhang,S., Ackerley,C.A.,
            Pak,B.J., Callahan,J.W. and Mahuran,D.J.
  TITLE     Presenilin-1, nicastrin, amyloid precursor protein, and
            gamma-secretase activity are co-localized in the lysosomal membrane
  JOURNAL   J Biol Chem 278 (29), 26687-26694 (2003)
   PUBMED   12736250
  REMARK    GeneRIF: experiments establish amyloid precursor protein,
            nicastrin, and presenilin-1 as resident lysosomal membrane proteins
            and indicate that gamma-secretase is a lysosomal protease
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Chen,F., Tandon,A., Sanjo,N., Gu,Y.J., Hasegawa,H., Arawaka,S.,
            Lee,F.J., Ruan,X., Mastrangelo,P., Erdebil,S., Wang,L.,
            Westaway,D., Mount,H.T., Yankner,B., Fraser,P.E. and St
            George-Hyslop,P.
  TITLE     Presenilin 1 and presenilin 2 have differential effects on the
            stability and maturation of nicastrin in Mammalian brain
  JOURNAL   J Biol Chem 278 (22), 19974-19979 (2003)
   PUBMED   12646573
REFERENCE   8  (residues 1 to 708)
  AUTHORS   Lee,S.F., Shah,S., Li,H., Yu,C., Han,W. and Yu,G.
  TITLE     Mammalian APH-1 interacts with presenilin and nicastrin and is
            required for intramembrane proteolysis of amyloid-beta precursor
            protein and Notch
  JOURNAL   J Biol Chem 277 (47), 45013-45019 (2002)
   PUBMED   12297508
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Dermaut,B., Theuns,J., Sleegers,K., Hasegawa,H., Van den Broeck,M.,
            Vennekens,K., Corsmit,E., St George-Hyslop,P., Cruts,M., van
            Duijn,C.M. and Van Broeckhoven,C.
  TITLE     The gene encoding nicastrin, a major gamma-secretase component,
            modifies risk for familial early-onset Alzheimer disease in a Dutch
            population-based sample
  JOURNAL   Am J Hum Genet 70 (6), 1568-1574 (2002)
   PUBMED   11992262
REFERENCE   10 (residues 1 to 708)
  AUTHORS   Leem,J.Y., Vijayan,S., Han,P., Cai,D., Machura,M., Lopes,K.O.,
            Veselits,M.L., Xu,H. and Thinakaran,G.
  TITLE     Presenilin 1 is required for maturation and cell surface
            accumulation of nicastrin
  JOURNAL   J Biol Chem 277 (21), 19236-19240 (2002)
   PUBMED   11943765
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC074006.1 and AY101378.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY101378.1, SRR8487231.45426.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..708
                     /product="nicastrin precursor"
                     /calculated_mol_wt=75200
     sig_peptide     1..34
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
                     /calculated_mol_wt=3219
     mat_peptide     35..708
                     /product="Nicastrin. /id=PRO_0000019683"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU6.1)"
                     /calculated_mol_wt=75200
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Region          51..653
                     /region_name="M28_Nicastrin"
                     /note="M28 Zn-peptidase nicastrin, a main component of
                     gamma-secretase complex; cd03881"
                     /db_xref="CDD:349877"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            335..339
                     /site_type="other"
                     /note="DYIGS region"
                     /db_xref="CDD:349877"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            434
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            463
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            529
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            561
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            572
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            579
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            593
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU6.1)"
     Site            669..689
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU6.1)"
     CDS             1..708
                     /gene="Ncstn"
                     /coded_by="NM_174864.3:93..2219"
                     /db_xref="GeneID:289231"
                     /db_xref="RGD:631418"
ORIGIN      
        1 matarggsgp dpgsrgllll sfsvvlaglc ggnsverkiy iplnktapcv rllnathqig
       61 cqssisgdtg vihvvekedd lkwvltdgpn ppymvllegk lftrdimekl kgetsriagl
      121 avtlakpnst ssfspsvqcp ndgfgiysns ygpefahckk tlwnelgngl ayddfsfpif
      181 lledenetkv ikqcyqdhnl gqngsapsfp lcamqlfshm havistatcm rrsfiqstfs
      241 inpeivcdpl sdynvwsmlk pintsgglep dvrvvvaatr ldsrsffwnv apgaesavas
      301 fvtqlaaaea lhkapdvttl prnvmfvffq getfdyigss rmvydmengk fpvrlenids
      361 fvelgqvalr tslelwmhtd pmsqknesvk nqvedllvtl eqsgadtpqv vlsrlvqsqa
      421 lppsslqrfl rarnisgvvl adhsgsfhnr yyqsiydtae ninvtypesq speedlnfvt
      481 dtakaladva tvlaralykl aggtnfnnsi qadpqtvtrl lygflvrann swfqsilrhd
      541 lrsylddgpl qhyiavsspt nttyvvqyal anltgkvtnl tqeqcqdpsk vpneskdlye
      601 yswvqgpwns nkterlprcv rstvrlaral spafelsqws steystwaes rwkdiqarif
      661 liaskelefi tlivgfsilv fslivtycin akadvlfvap repgavsy
//
LOCUS       NP_001291667             398 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_001291667
VERSION     NP_001291667.1
DBSOURCE    REFSEQ: accession NM_001304738.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1i2) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1) is shorter
            than isoform 1C2. Variants MOR-1H1, MOR-1i1, MOR-1i2 and MOR-1i3
            encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU024652.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..398
                     /product="mu-type opioid receptor isoform 1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=44363
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..398
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304738.1:476..1672"
                     /note="isoform 1 is encoded by transcript variant MOR-1i2"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_445933               1070 aa            linear   ROD 18-MAR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform [Rattus norvegicus].
ACCESSION   NP_445933
VERSION     NP_445933.1
DBSOURCE    REFSEQ: accession NM_053481.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Wang,J., Zhan,H., Wang,M., Song,H., Sun,J. and Zhao,G.
  TITLE     Sonic hedgehog signaling promotes angiogenesis of endothelial
            progenitor cells to improve pressure ulcers healing by
            PI3K/AKT/eNOS signaling
  JOURNAL   Aging (Albany NY) 15 (19), 10540-10548 (2023)
   PUBMED   37815888
  REMARK    GeneRIF: Sonic hedgehog signaling promotes angiogenesis of
            endothelial progenitor cells to improve pressure ulcers healing by
            PI3K/AKT/eNOS signaling.
            Erratum:[Aging (Albany NY). 2023 Dec 29;15(24):15703-15704. doi:
            10.18632/aging.205458. PMID: 38157439]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Mukhomedzyanov,A.V., Popov,S.V., Maslov,L.N., Diez,E.R. and
            Azev,V.N.
  TITLE     Role of PI3K, ERK1/2, and JAK2 Kinases in the Cardioprotective
            Effect of Deltorphin II during Cardiac Reperfusion
  JOURNAL   Bull Exp Biol Med 175 (1), 17-19 (2023)
   PUBMED   37338759
  REMARK    GeneRIF: Role of PI3K, ERK1/2, and JAK2 Kinases in the
            Cardioprotective Effect of Deltorphin II during Cardiac
            Reperfusion.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Cheng,Q., Wang,M., Jin,R. and Li,G.
  TITLE     Blocking of PI3-kinase beta protects against cerebral
            ischemia/reperfusion injury by reducing platelet activation and
            downstream microvascular thrombosis in rats
  JOURNAL   Sci Rep 13 (1), 2030 (2023)
   PUBMED   36739310
  REMARK    GeneRIF: Blocking of PI3-kinase beta protects against cerebral
            ischemia/reperfusion injury by reducing platelet activation and
            downstream microvascular thrombosis in rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Zhang,L., Li,B., Li,W., Jiang,J., Chen,W., Yang,H. and Pan,D.
  TITLE     miR-107 Attenuates Sepsis-Induced Myocardial Injury by Targeting
            PTEN and Activating the PI3K/AKT Signaling Pathway
  JOURNAL   Cells Tissues Organs 212 (6), 523-534 (2023)
   PUBMED   35717938
  REMARK    GeneRIF: miR-107 Attenuates Sepsis-Induced Myocardial Injury by
            Targeting PTEN and Activating the PI3K/AKT Signaling Pathway.
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Yang,B., Pan,C.S., Li,Q., Yang,Z., Long,F.X., Fan,J.Y., Wang,C.S.,
            Han,J.Y. and Tang,D.X.
  TITLE     Inhibitory effects of Chanling Gao on the proliferation and liver
            metastasis of transplanted colorectal cancer in nude mice
  JOURNAL   PLoS One 14 (2), e0201504 (2019)
   PUBMED   30789971
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Rajala,R.V., McClellan,M.E., Ash,J.D. and Anderson,R.E.
  TITLE     In vivo regulation of phosphoinositide 3-kinase in retina through
            light-induced tyrosine phosphorylation of the insulin receptor
            beta-subunit
  JOURNAL   J Biol Chem 277 (45), 43319-43326 (2002)
   PUBMED   12213821
  REMARK    GeneRIF: in vivo regulation in retina through light-induced
            tyrosine phosphorylation of the insulin receptor beta-subunit
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Alpini,G., Glaser,S., Alvaro,D., Ueno,Y., Marzioni,M., Francis,H.,
            Baiocchi,L., Stati,T., Barbaro,B., Phinizy,J.L., Mauldin,J. and
            Lesage,G.
  TITLE     Bile acid depletion and repletion regulate cholangiocyte growth and
            secretion by a phosphatidylinositol 3-kinase-dependent pathway in
            rats
  JOURNAL   Gastroenterology 123 (4), 1226-1237 (2002)
   PUBMED   12360484
  REMARK    GeneRIF: Bile acid depletion and repletion regulate cholangiocyte
            growth and secretion by a phosphatidylinositol 3-kinase-dependent
            pathway in rats.
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Crljen,V., Volinia,S. and Banfic,H.
  TITLE     Hepatocyte growth factor activates phosphoinositide 3-kinase C2
            beta in renal brush-border plasma membranes
  JOURNAL   Biochem J 365 (Pt 3), 791-799 (2002)
   PUBMED   11931646
  REMARK    GeneRIF: data show a spatial separation of the inositol lipid
            signalling system between brush border membranes (BBM) and
            basolateral membranes (BLM); hepatocyte growth factor causes
            activation of PLC and PI3K in BLM leading to activation of PI3K-C2
            beta in BBM
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Bi,L., Okabe,I., Bernard,D.J. and Nussbaum,R.L.
  TITLE     Early embryonic lethality in mice deficient in the p110beta
            catalytic subunit of PI 3-kinase
  JOURNAL   Mamm Genome 13 (3), 169-172 (2002)
   PUBMED   11919689
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Kim,Y.B., Ciaraldi,T.P., Kong,A., Kim,D., Chu,N., Mohideen,P.,
            Mudaliar,S., Henry,R.R. and Kahn,B.B.
  TITLE     Troglitazone but not metformin restores insulin-stimulated
            phosphoinositide 3-kinase activity and increases p110beta protein
            levels in skeletal muscle of type 2 diabetic subjects
  JOURNAL   Diabetes 51 (2), 443-448 (2002)
   PUBMED   11812753
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AJ012482.1, CV117575.1, EV762942.1, EV765206.1, BQ202622.1 and
            AW523465.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ012482.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase beta; PI3K;
                     PI3Kbeta; ptdIns-3-kinase p110; PI3-kinase p110 subunit
                     beta; PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 3-kinase, catalytic, beta
                     polypeptide; p110beta; phosphatidylinositol
                     4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta;
                     phosphoinositide-3-kinase, catalytic, beta polypeptide;
                     serine/threonine protein kinase PIK3CB"
                     /calculated_mol_wt=122477
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     Region          410..418
                     /region_name="Nuclear localization signal (NLS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P42338; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1L0.1)"
     CDS             1..1070
                     /gene="Pik3cb"
                     /coded_by="NM_053481.2:1..3213"
                     /db_xref="GeneID:85243"
                     /db_xref="RGD:620917"
ORIGIN      
        1 mcfrsimppa madtldiwav dsqiasdgsi svdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpae
      121 kldskigvli gkglhefdal kdpevnefrr kmrkfsedki qslvglswid wlkhtyppeh
      181 epsvlenled klyggklvva vhfensqdvf sfqvspnlnp ikinelaiqk rltirgkeee
      241 aspcdyvlqv sgrveyvfgd hpliqfqyir ncvmnrtlph filvecckik kmyeqemiai
      301 eaainrnsss lplplppkkt rvishvwgnn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktvvs seisgkndhi wneqlefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrsgdvilh swssfpdele emlnpmgtvq
      481 tnpyaenata lhikfpenkk qpyyyppfdk iiekaaeias gdsanvssrg gkkflavlke
      541 ildrdplsql cenemdliwt lrqdcrenfp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leraldnrri gqflfwhlrs evhtpavsiq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna mklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekcrymd
      781 skmkplwlvy snrafgedav gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aataafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001291665             448 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1H2 [Rattus norvegicus].
ACCESSION   NP_001291665
VERSION     NP_001291665.1
DBSOURCE    REFSEQ: accession NM_001304736.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1H2) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1H2) is shorter
            than isoform 1C2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU024651.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..448
                     /product="mu-type opioid receptor isoform 1H2"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=49578
     Region          119..397
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          120..146
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          153..179
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            order(174,177..178,190..195,197..198,201,246,248..252,279,
                     282..284,286..288,290..291,343,346..347,349..350,353,
                     364..365,367..369,372,375..376)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          190..220
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Region          232..254
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Region          279..308
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Region          323..353
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Region          365..390
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     CDS             1..448
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304736.1:70..1416"
                     /note="isoform 1H2 is encoded by transcript variant
                     MOR-1H2"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mgsgpmlagp cknltepraa vrgrgwgawn pkslsalsys lpspqqafst mdsstgpgnt
       61 sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt gspsmvtait
      121 imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst lpfqsvnylm
      181 gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt prnakivnvc
      241 nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa fimpvliitv
      301 cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv iikalitipe
      361 ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq qnstrvrqnt
      421 rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_001257487             268 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001257487
VERSION     NP_001257487.1
DBSOURCE    REFSEQ: accession NM_001270558.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (3, also known as AQP4b) lacks an
            in-frame coding exon compared to variant 1. The resulting isoform
            (3) is shorter, missing an internal protein segment compared to
            isoform M1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72622.1,
                                           SRR26360194.794453.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21850708
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..268
                     /product="aquaporin-4 isoform 3"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=28637
     Region          23
                     /region_name="alternative AUG translation initiation site"
     Region          31..193
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            order(77,95..97,154..155,158,161)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(97..99,158..160)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..268
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_001270558.2:67..873"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 msdgaaarrw gkcgppcsre simvafkgvw tqafwkavta eflamlifvl lsvgstinwg
       61 gsenplpvdm vlislcfgls iatmvqcfgh isgghinpav tvamvctrki siaksvfyit
      121 aqclgaiiga gilylvtpps vvgglgvtti nytgasmnpa rsfgpavimg nwenhwiywv
      181 gpiigavlag alyeyvfcpd velkrrlkea fskaaqqtkg symevednrs qvetedlilk
      241 pgvvhvidid rgdekkgkds sgevlssv
//
LOCUS       NP_001033686             390 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform IA [Rattus norvegicus].
ACCESSION   NP_001033686
VERSION     NP_001033686.1
DBSOURCE    REFSEQ: accession NM_001038597.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L13069.1 and AY309000.1.
            
            Transcript Variant: This variant (MOR-1A) lacks several exons and
            its 3' terminal exon extends past a splice site that is used in
            variant MOR-1C2. This results in a novel 3' coding region and 3'
            UTR, compared to variant MOR-1B2. It encodes isoform 1A which is
            longer/shorter and has a distinct C-terminus, compared to isoform
            1C2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY309000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..390
                     /product="mu-type opioid receptor isoform IA"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=43505
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..390
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001038597.2:208..1380"
                     /note="isoform IA is encoded by transcript variant MOR-1A"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqvcaf
//
LOCUS       NP_001291669             398 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_001291669
VERSION     NP_001291669.1
DBSOURCE    REFSEQ: accession NM_001304740.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1i3) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1) is shorter
            than isoform 1C2. Variants MOR-1H1, MOR-1i1, MOR-1i2 and MOR-1i3
            encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU340246.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..398
                     /product="mu-type opioid receptor isoform 1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=44363
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..398
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304740.1:734..1930"
                     /note="isoform 1 is encoded by transcript variant MOR-1i3"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_001291666             398 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_001291666
VERSION     NP_001291666.1
DBSOURCE    REFSEQ: accession NM_001304737.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1i1) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1) is shorter
            than isoform 1C2. Variants MOR-1H1, MOR-1i1, MOR-1i2 and MOR-1i3
            encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU340245.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..398
                     /product="mu-type opioid receptor isoform 1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=44363
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..398
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304737.1:548..1744"
                     /note="isoform 1 is encoded by transcript variant MOR-1i1"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_001033690             468 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1C2 [Rattus norvegicus].
ACCESSION   NP_001033690
VERSION     NP_001033690.1
DBSOURCE    REFSEQ: accession NM_001038601.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L13069.1 and AY225403.1.
            
            Transcript Variant: This variant (MOR-1C2) encodes the longest
            isoform (1C2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY225403.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMN12840105 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..468
                     /product="mu-type opioid receptor isoform 1C2"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=52279
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..468
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001038601.2:208..1614"
                     /note="isoform 1C2 is encoded by transcript variant
                     MOR-1C2"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqpala vsvaqiftgy pspthgekpc ksyrdrprpc
      421 grtwslksra esnvehfhcg aaliynnelk igpvswlqmp ahvlvrpw
//
LOCUS       NP_001033689             451 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1C1 [Rattus norvegicus].
ACCESSION   NP_001033689
VERSION     NP_001033689.1
DBSOURCE    REFSEQ: accession NM_001038600.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L13069.1 and AY225402.1.
            
            Transcript Variant: This variant (MOR-1C1) lacks an alternate
            segment in the 3' region, compared to variant MOR-1C2. It encodes
            isoform 1C1 which has is shorter than isoform 1C2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY225402.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMN12840105 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..451
                     /product="mu-type opioid receptor isoform 1C1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=50314
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..451
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001038600.2:208..1563"
                     /note="isoform 1C1 is encoded by transcript variant
                     MOR-1C1"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqpala vsvaqiftgy pspthgekpc ksyrdrprpc
      421 grtwslksra esnvehfhcg aaliynnvnf i
//
LOCUS       NP_062077                501 aa            linear   ROD 18-MAR-2025
DEFINITION  beta-secretase 1 precursor [Rattus norvegicus].
ACCESSION   NP_062077
VERSION     NP_062077.1
DBSOURCE    REFSEQ: accession NM_019204.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Velazquez Toledano,J., Bello,M., Correa Basurto,J., Guerrero
            Gonzalez,I., Pacheco-Yepez,J. and Rosales Hernandez,M.C.
  TITLE     Determining Structural Changes for Ligand Recognition between Human
            and Rat Phosphorylated BACE1 in Silico and Its Phosphorylation by
            GSK3beta at Thr252 by in Vitro Studies
  JOURNAL   ACS Chem Neurosci 15 (3), 629-644 (2024)
   PUBMED   38227464
  REMARK    GeneRIF: Determining Structural Changes for Ligand Recognition
            between Human and Rat Phosphorylated BACE1 in Silico and Its
            Phosphorylation by GSK3beta at Thr252 by in Vitro Studies.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Wang,X., Li,M. and Hu,Y.
  TITLE     miR-29c-3p Attenuates beta-Amyloid-Induced Neurotoxicity in
            Alzheimer's Disease Through Regulating beta-Site Amyloid Precursor
            Protein-Cleaving Enzyme 1
  JOURNAL   Physiol Res 72 (6), 833-841 (2023)
   PUBMED   38215068
  REMARK    GeneRIF: miR-29c-3p Attenuates beta-Amyloid-Induced Neurotoxicity
            in Alzheimer's Disease Through Regulating beta-Site Amyloid
            Precursor Protein-Cleaving Enzyme 1.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Qu,J., Xiong,X., Hujie,G., Ren,J., Yan,L. and Ma,L.
  TITLE     MicroRNA-132-3p alleviates neuron apoptosis and impairments of
            learning and memory abilities in Alzheimer's disease by
            downregulation of HNRNPU stabilized BACE1
  JOURNAL   Cell Cycle 20 (21), 2309-2320 (2021)
   PUBMED   34585626
  REMARK    GeneRIF: MicroRNA-132-3p alleviates neuron apoptosis and
            impairments of learning and memory abilities in Alzheimer's disease
            by downregulation of HNRNPU stabilized BACE1.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Babusikova,E., Dobrota,D., Turner,A.J. and Nalivaeva,N.N.
  TITLE     Effect of Global Brain Ischemia on Amyloid Precursor Protein
            Metabolism and Expression of Amyloid-Degrading Enzymes in Rat
            Cortex: Role in Pathogenesis of Alzheimer's Disease
  JOURNAL   Biochemistry (Mosc) 86 (6), 680-692 (2021)
   PUBMED   34225591
  REMARK    GeneRIF: Effect of Global Brain Ischemia on Amyloid Precursor
            Protein Metabolism and Expression of Amyloid-Degrading Enzymes in
            Rat Cortex: Role in Pathogenesis of Alzheimer's Disease.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   De Pietri Tonelli,D., Mihailovich,M., Di Cesare,A., Codazzi,F.,
            Grohovaz,F. and Zacchetti,D.
  TITLE     Translational regulation of BACE-1 expression in neuronal and
            non-neuronal cells
  JOURNAL   Nucleic Acids Res 32 (5), 1808-1817 (2004)
   PUBMED   15034149
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Rogers,G.W. Jr., Edelman,G.M. and Mauro,V.P.
  TITLE     Differential utilization of upstream AUGs in the beta-secretase
            mRNA suggests that a shunting mechanism regulates translation
  JOURNAL   Proc Natl Acad Sci U S A 101 (9), 2794-2799 (2004)
   PUBMED   14981268
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Yan,R., Han,P., Miao,H., Greengard,P. and Xu,H.
  TITLE     The transmembrane domain of the Alzheimer's beta-secretase (BACE1)
            determines its late Golgi localization and access to beta -amyloid
            precursor protein (APP) substrate
  JOURNAL   J Biol Chem 276 (39), 36788-36796 (2001)
   PUBMED   11466313
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Lin,X., Koelsch,G., Wu,S., Downs,D., Dashti,A. and Tang,J.
  TITLE     Human aspartic protease memapsin 2 cleaves the beta-secretase site
            of beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 97 (4), 1456-1460 (2000)
   PUBMED   10677483
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Vassar,R., Bennett,B.D., Babu-Khan,S., Kahn,S., Mendiaz,E.A.,
            Denis,P., Teplow,D.B., Ross,S., Amarante,P., Loeloff,R., Luo,Y.,
            Fisher,S., Fuller,J., Edenson,S., Lile,J., Jarosinski,M.A.,
            Biere,A.L., Curran,E., Burgess,T., Louis,J.C., Collins,F.,
            Treanor,J., Rogers,G. and Citron,M.
  TITLE     Beta-secretase cleavage of Alzheimer's amyloid precursor protein by
            the transmembrane aspartic protease BACE
  JOURNAL   Science 286 (5440), 735-741 (1999)
   PUBMED   10531052
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Urmoneit,B., Reinsch,C., Turner,J., Czech,C., Beyreuther,K. and
            Dyrks,T.
  TITLE     Inhibition of beta A4 production by specific modulation of
            beta-secretase activity
  JOURNAL   J Mol Neurosci 6 (1), 23-32 (1995)
   PUBMED   8562317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF190727.1 and JAXUCZ010000008.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF190727.1, SRR26643287.19966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            regulatory uORF        :: PMID: 14981268
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..501
                     /product="beta-secretase 1 precursor"
                     /EC_number="3.4.23.46"
                     /note="ASP2; asp 2; memapsin-2; aspartyl protease 2;
                     membrane-associated aspartic protease 2; beta-site amyloid
                     precursor protein cleaving enzyme 1; beta-site APP
                     cleaving enzyme 1"
                     /calculated_mol_wt=53557
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2268
     mat_peptide     46..501
                     /product="Beta-secretase 1. /id=PRO_0000025944"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
                     /calculated_mol_wt=51014
     Region          72..437
                     /region_name="beta_secretase_like"
                     /note="Beta-secretase, aspartic-acid protease important in
                     the pathogenesis of Alzheimer's disease; cd05473"
                     /db_xref="CDD:133140"
     Site            order(72,93,95,132..134,171,189,259,289,291..293,368,382)
                     /site_type="active"
                     /note="inhibitor binding site [active]"
                     /db_xref="CDD:133140"
     Site            order(93..96,289..292)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:133140"
     Site            order(93,289)
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:133140"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            order(129..132,136..139)
                     /site_type="active"
                     /note="Active site flap [active]"
                     /db_xref="CDD:133140"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            285
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            300
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            458..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Region          479..501
                     /region_name="Interaction with RTN3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Region          496..500
                     /region_name="DXXLL.
                     /evidence=ECO:0000250|UniProtKB:P56817"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56818; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     CDS             1..501
                     /gene="Bace1"
                     /gene_synonym="Bace"
                     /coded_by="NM_019204.2:428..1933"
                     /db_xref="GeneID:29392"
                     /db_xref="RGD:2191"
ORIGIN      
        1 mapalrwlll wvgsgmlpaq gthlgirlpl rsglagpplg lrlpretdee peepgrrgsf
       61 vemvdnlrgk sgqgyyvemt vgsppqtlni lvdtgssnfa vgaaphpflh ryyqrqlsst
      121 yrdlrksvyv pytqgkwege lgtdlvsiph gpnvtvrani aaitesdkff ingsnwegil
      181 glayaeiarp ddslepffds lvkqthipni fslqlcgagf plnqtealas vggsmiiggi
      241 dhslytgslw ytpirrewyy eviivrvein gqdlkmdcke ynydksivds gttnlrlpkk
      301 vfeaavksik aasstekfpd gfwlgeqlvc wqagttpwni fpvislylmg evtnqsfrit
      361 ilpqqylrpv edvatsqddc ykfavsqsst gtvmgavime gfyvvfdrar krigfavsac
      421 hvhdefrtaa vegpfvtadm edcgynipqt destlmtiay vmaaicalfm lplclmvcqw
      481 rclrclrhqh ddfaddisll k
//
LOCUS       NP_113889                218 aa            linear   ROD 18-MAR-2025
DEFINITION  claudin-5 [Rattus norvegicus].
ACCESSION   NP_113889 XP_344059
VERSION     NP_113889.1
DBSOURCE    REFSEQ: accession NM_031701.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Hirose,Y., Oda,Y., Yoshino,K., Yano,F., Kimura,M., Kimura,H.,
            Iyo,M. and Shirayama,Y.
  TITLE     Reduction of claudin-5 and aquaporin-4 in the rat hippocampal CA-1
            and CA-3 regions of a learned helplessness model of depression
  JOURNAL   Pharmacol Biochem Behav 234, 173676 (2024)
   PUBMED   37992974
  REMARK    GeneRIF: Reduction of claudin-5 and aquaporin-4 in the rat
            hippocampal CA-1 and CA-3 regions of a learned helplessness model
            of depression.
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Hu,Q., Wu,C., Yu,J., Luo,J. and Peng,X.
  TITLE     Angelica sinensis polysaccharide improves rheumatoid arthritis by
            modifying the expression of intestinal Cldn5, Slit3 and Rgs18
            through gut microbiota
  JOURNAL   Int J Biol Macromol 209 (Pt A), 153-161 (2022)
   PUBMED   35318077
  REMARK    GeneRIF: Angelica sinensis polysaccharide improves rheumatoid
            arthritis by modifying the expression of intestinal Cldn5, Slit3
            and Rgs18 through gut microbiota.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Andersson,E.A., Rocha-Ferreira,E., Hagberg,H., Mallard,C. and
            Ek,C.J.
  TITLE     Function and Biomarkers of the Blood-Brain Barrier in a Neonatal
            Germinal Matrix Haemorrhage Model
  JOURNAL   Cells 10 (7), 1677 (2021)
   PUBMED   34359845
  REMARK    GeneRIF: Function and Biomarkers of the Blood-Brain Barrier in a
            Neonatal Germinal Matrix Haemorrhage Model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Rosas-Martinez,L., Rodriguez-Munoz,R., Namorado-Tonix,M.D.C.,
            Missirlis,F., Del Valle-Mondragon,L., Sanchez-Mendoza,A.,
            Reyes-Sanchez,J.L. and Cervantes-Perez,L.G.
  TITLE     Hyperglycemic levels in early stage of diabetic nephropathy affect
            differentially renal expression of claudins-2 and -5 by oxidative
            stress
  JOURNAL   Life Sci 268, 119003 (2021)
   PUBMED   33417957
  REMARK    GeneRIF: Hyperglycemic levels in early stage of diabetic
            nephropathy affect differentially renal expression of claudins-2
            and -5 by oxidative stress.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Shou,J., Peng,J., Zhao,Z., Huang,X., Li,H., Li,L., Gao,X., Xing,Y.
            and Liu,H.
  TITLE     CCL26 and CCR3 are associated with the acute inflammatory response
            in the CNS in experimental autoimmune encephalomyelitis
  JOURNAL   J Neuroimmunol 333, 576967 (2019)
   PUBMED   31151084
  REMARK    GeneRIF: The expression of claudin-5 in the EAE group was
            negatively correlated with the inflammation scores. Levels of CCL26
            in the serum and brain tissues and the number of CCR3-positive
            cells in the brain tissues were negatively correlated with the
            protein expression of claudin-5.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Sun,Z.Y., Wei,J., Xie,L., Shen,Y., Liu,S.Z., Ju,G.Z., Shi,J.P.,
            Yu,Y.Q., Zhang,X., Xu,Q. and Hemmings,G.P.
  TITLE     The CLDN5 locus may be involved in the vulnerability to
            schizophrenia
  JOURNAL   Eur Psychiatry 19 (6), 354-357 (2004)
   PUBMED   15363474
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Wolburg,H., Wolburg-Buchholz,K., Kraus,J., Rascher-Eggstein,G.,
            Liebner,S., Hamm,S., Duffner,F., Grote,E.H., Risau,W. and
            Engelhardt,B.
  TITLE     Localization of claudin-3 in tight junctions of the blood-brain
            barrier is selectively lost during experimental autoimmune
            encephalomyelitis and human glioblastoma multiforme
  JOURNAL   Acta Neuropathol 105 (6), 586-592 (2003)
   PUBMED   12734665
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Nitta,T., Hata,M., Gotoh,S., Seo,Y., Sasaki,H., Hashimoto,N.,
            Furuse,M. and Tsukita,S.
  TITLE     Size-selective loosening of the blood-brain barrier in
            claudin-5-deficient mice
  JOURNAL   J Cell Biol 161 (3), 653-660 (2003)
   PUBMED   12743111
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Poliak,S., Matlis,S., Ullmer,C., Scherer,S.S. and Peles,E.
  TITLE     Distinct claudins and associated PDZ proteins form different
            autotypic tight junctions in myelinating Schwann cells
  JOURNAL   J Cell Biol 159 (2), 361-372 (2002)
   PUBMED   12403818
  REMARK    GeneRIF: MUPP1 and claudin-5 colocalized in the incisures, and the
            COOH-terminal region of claudin-5 interacts with MUPP1 in a
            PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner in
            tight junctions
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Morita,K., Furuse,M., Fujimoto,K. and Tsukita,S.
  TITLE     Claudin multigene family encoding four-transmembrane domain protein
            components of tight junction strands
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 511-516 (1999)
   PUBMED   9892664
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK479973.1, BC082073.1 and AI029697.1.
            
            On Nov 26, 2004 this sequence version replaced XP_344059.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: FQ212855.1, FQ213419.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..218
                     /product="claudin-5"
                     /calculated_mol_wt=22941
     Region          5..180
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKD6.2)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKD6.2)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKD6.2)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKD6.2)"
     Region          217..218
                     /region_name="Interactions with TJP1, TJP2 and TJP3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKD6.2)"
     CDS             1..218
                     /gene="Cldn5"
                     /coded_by="NM_031701.2:143..799"
                     /db_xref="GeneID:65131"
                     /db_xref="RGD:68431"
ORIGIN      
        1 mgsaaleilg lvlclvgwvg lilacglpmw qvtafldhni vtaqttwkgl wmscvvqstg
       61 hmqckvyesv lalsaevqaa raltvgavll alvalfvtlt gaqcttcvap gpvkarvalt
      121 ggalyalcgl lalvplcwfa nivvrefydp tvpvsqkyel gaalyigwaa sallmcgggl
      181 vccgawvctg rpefsfpvky saprrttang dydkknyv
//
LOCUS       NP_001257488             246 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001257488
VERSION     NP_001257488.1
DBSOURCE    REFSEQ: accession NM_001270559.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (4, also known as AQP4d) contains
            an alternate 5' terminal exon and lacks an in-frame coding exon
            compared to variant 1. These changes result in translation
            initiation from an in-frame, downstream start codon, and an isoform
            (4) with a shorter N-terminus and missing an internal protein
            segment compared to isoform M1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1357710.1,
                                           SRR26360176.146936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..246
                     /product="aquaporin-4 isoform 4"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=26320
     Region          9..171
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            order(55,73..75,132..133,136,139)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(75..77,136..138)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..246
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_001270559.2:141..881"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 mvafkgvwtq afwkavtaef lamlifvlls vgstinwggs enplpvdmvl islcfglsia
       61 tmvqcfghis gghinpavtv amvctrkisi aksvfyitaq clgaiigagi lylvtppsvv
      121 gglgvttiny tgasmnpars fgpavimgnw enhwiywvgp iigavlagal yeyvfcpdve
      181 lkrrlkeafs kaaqqtkgsy mevednrsqv etedlilkpg vvhvididrg dekkgkdssg
      241 evlssv
//
LOCUS       NP_001304678             352 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform M1x [Rattus norvegicus].
ACCESSION   NP_001304678
VERSION     NP_001304678.1
DBSOURCE    REFSEQ: accession NM_001317749.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1, also known as AQP4a)
            represents the predominant transcript and encodes two isoforms,
            which result from the use of alternative in-frame translation
            termination codons. The shorter isoform (M1) results from
            translation termination at the upstream UGA stop codon, while the
            longer isoform (M1x) results from UGA stop codon readthrough to the
            downstream UAA termination codon. This RefSeq represents the
            longer, C-terminally extended isoform (M1x). As the UGA stop codon
            has been reported to specify several alternative amino acids
            (tryptophan, cysteine, arginine and serine), its location in the
            longer isoform is denoted by an 'X'.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72618.1,
                                           SRR26643429.53390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF        :: PMID: 21850708
            stop codon readthrough :: inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..352
                     /product="aquaporin-4 isoform M1x"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=37549
     Region          23
                     /region_name="alternative AUG translation initiation site"
     Region          31..248
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            order(77,95..97,209..210,213,216)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(97..99,213..215)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..352
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_001317749.1:67..1125"
                     /note="isoform M1x is encoded by transcript variant 1"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 msdgaaarrw gkcgppcsre simvafkgvw tqafwkavta eflamlifvl lsvgstinwg
       61 gsenplpvdm vlislcfgls iatmvqcfgh isgghinpav tvamvctrki siaksvfyit
      121 aqclgaiiga gilylvtpps vvgglgvttv hgnltaghgl lveliitfql vftifascds
      181 krtdvtgsva laigfsvaig hlfainytga smnparsfgp avimgnwenh wiywvgpiig
      241 avlagalyey vfcpdvelkr rlkeafskaa qqtkgsymev ednrsqvete dlilkpgvvh
      301 vididrgdek kgkdssgevl ssvxledste nrrdslelas dflppiketd ll
//
LOCUS       NP_036957                323 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform M1 [Rattus norvegicus].
ACCESSION   NP_036957
VERSION     NP_036957.1
DBSOURCE    REFSEQ: accession NM_012825.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1, also known as AQP4a)
            represents the predominant transcript and encodes two isoforms,
            which result from the use of alternative in-frame translation
            termination codons. The shorter isoform (M1) results from
            translation termination at the upstream UGA stop codon, while the
            longer isoform (M1x) results from UGA stop codon readthrough to the
            downstream UAA termination codon. This RefSeq represents the
            shorter isoform (M1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72618.1,
                                           SRR26643429.53390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            regulatory uORF        :: PMID: 21850708
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..323
                     /product="aquaporin-4 isoform M1"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=34349
     Region          23
                     /region_name="alternative AUG translation initiation site"
     Region          31..248
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            70..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            order(77,95..97,209..210,213,216)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(97..99,213..215)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          97..99
                     /region_name="NPA 1.
                     /evidence=ECO:0000305|PubMed:16325200,
                     ECO:0000305|PubMed:19406128"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG.
                     /evidence=ECO:0000250|UniProtKB:P55088; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:19800950; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Region          213..215
                     /region_name="NPA 2.
                     /evidence=ECO:0000305|PubMed:16325200,
                     ECO:0000305|PubMed:19406128"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47863.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12692561,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55088; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P47863.1)"
     CDS             1..323
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_012825.4:67..1038"
                     /note="isoform M1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 msdgaaarrw gkcgppcsre simvafkgvw tqafwkavta eflamlifvl lsvgstinwg
       61 gsenplpvdm vlislcfgls iatmvqcfgh isgghinpav tvamvctrki siaksvfyit
      121 aqclgaiiga gilylvtpps vvgglgvttv hgnltaghgl lveliitfql vftifascds
      181 krtdvtgsva laigfsvaig hlfainytga smnparsfgp avimgnwenh wiywvgpiig
      241 avlagalyey vfcpdvelkr rlkeafskaa qqtkgsymev ednrsqvete dlilkpgvvh
      301 vididrgdek kgkdssgevl ssv
//
LOCUS       NP_001291664             398 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_001291664
VERSION     NP_001291664.1
DBSOURCE    REFSEQ: accession NM_001304735.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1H1) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1) is shorter
            than isoform 1C2. Variants MOR-1H1, MOR-1i1, MOR-1i2 and MOR-1i3
            encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU340244.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..398
                     /product="mu-type opioid receptor isoform 1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=44363
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..398
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304735.1:292..1488"
                     /note="isoform 1 is encoded by transcript variant MOR-1H1"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_037203                398 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_037203
VERSION     NP_037203.1
DBSOURCE    REFSEQ: accession NM_013071.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L13069.1 and L20684.1.
            
            Transcript Variant: This variant (1) lacks several exons and
            contains an alternate terminal exon compared to variant MOR-1C2.
            The encoded isoform (1) is shorter than isoform 1C2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L20684.1, D16349.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..398
                     /product="mu-type opioid receptor isoform 1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=44363
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            67..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          69..347
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          70..96
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320218"
     Region          103..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            order(124,127..128,140..145,147..148,151,196,198..202,229,
                     232..234,236..238,240..241,293,296..297,299..300,303,
                     314..315,317..319,322,325..326)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Site            141..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19959593; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Region          182..204
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          229..258
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Site            229..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          273..303
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Site            278..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            313..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          315..340
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     Region          332..336
                     /region_name="NPxxY, plays a role in stabilizing the
                     activated conformation of the receptor.
                     /evidence=ECO:0000250|UniProtKB:P42866"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Region          361..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33535.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11278523; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:10820022; propagated from
                     UniProtKB/Swiss-Prot (P33535.1)"
     CDS             1..398
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_013071.2:208..1404"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mdsstgpgnt sdcsdplaqa scspapgswl nlshvdgnqs dpcglnrtgl ggndslcpqt
       61 gspsmvtait imalysivcv vglfgnflvm yvivrytkmk tatniyifnl aladalatst
      121 lpfqsvnylm gtwpfgtilc kivisidyyn mftsiftlct msvdryiavc hpvkaldfrt
      181 prnakivnvc nwilssaigl pvmfmattky rqgsidctlt fshptwywen llkicvfifa
      241 fimpvliitv cyglmilrlk svrmlsgske kdrnlrritr mvlvvvavfi vcwtpihiyv
      301 iikalitipe ttfqtvswhf cialgytnsc lnpvlyafld enfkrcfref ciptsstieq
      361 qnstrvrqnt rehpstantv drtnhqlenl eaetaplp
//
LOCUS       NP_001291662             300 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1G1 [Rattus norvegicus].
ACCESSION   NP_001291662
VERSION     NP_001291662.1
DBSOURCE    REFSEQ: accession NM_001304733.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1G1) represents use of an
            alternate promoter and 5' UTR, uses a downstream start codon, and
            uses an alternate 3' exon, compared to variant MOR-1C2. The
            resulting isoform (1G1) is shorter than isoform 1C2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ680043.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..300
                     /product="mu-type opioid receptor isoform 1G1"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=34249
     Region          1..249
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          5..31
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            order(26,29..30,42..47,49..50,53,98,100..104,131,134..136,
                     138..140,142..143,195,198..199,201..202,205,216..217,
                     219..221,224,227..228)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          42..72
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Region          84..106
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Region          131..160
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Region          175..205
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Region          217..242
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     CDS             1..300
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304733.1:172..1074"
                     /note="isoform 1G1 is encoded by transcript variant
                     MOR-1G1"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mktatniyif nlaladalat stlpfqsvny lmgtwpfgti lckivisidy ynmftsiftl
       61 ctmsvdryia vchpvkaldf rtprnakivn vcnwilssai glpvmfmatt kyrqgsidct
      121 ltfshptwyw enllkicvfi fafimpvlii tvcyglmilr lksvrmlsgs kekdrnlrri
      181 trmvlvvvav fivcwtpihi yviikaliti pettfqtvsw hfcialgytn sclnpvlyaf
      241 ldenfkrcfr efciptssti eqqnstrvrq ntrehpstan tvdrtnhqle nleaetaplp
//
LOCUS       NP_001135838             301 aa            linear   ROD 18-MAR-2025
DEFINITION  aquaporin-4 isoform M23 [Rattus norvegicus].
ACCESSION   NP_001135838
VERSION     NP_001135838.1
DBSOURCE    REFSEQ: accession NM_001142366.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Chen,K., Xu,B., Qiu,S., Long,L., Zhao,Q., Xu,J. and Wang,H.
  TITLE     Inhibition of phosphodiesterase 4 attenuates aquaporin 4 expression
            and astrocyte swelling following cerebral ischemia/reperfusion
            injury
  JOURNAL   Glia 72 (9), 1629-1645 (2024)
   PUBMED   38785370
  REMARK    GeneRIF: Inhibition of phosphodiesterase 4 attenuates aquaporin 4
            expression and astrocyte swelling following cerebral
            ischemia/reperfusion injury.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Pisani,F., Rossi,A., Nicchia,G.P., Svelto,M. and Frigeri,A.
  TITLE     Translational regulation mechanisms of aquaporin-4 supramolecular
            organization in astrocytes
  JOURNAL   Glia 59 (12), 1923-1932 (2011)
   PUBMED   21850708
  REMARK    GeneRIF: When transfected in Hela cells, the longer rat AQP4
            isoform, not present in humans, impairs formation of the orthogonal
            array of particles in astrocyte primary cultures.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Hirt,B., Gleiser,C., Eckhard,A., Mack,A.F., Muller,M., Wolburg,H.
            and Lowenheim,H.
  TITLE     All functional aquaporin-4 isoforms are expressed in the rat
            cochlea and contribute to the formation of orthogonal arrays of
            particles
  JOURNAL   Neuroscience 189, 79-92 (2011)
   PUBMED   21621589
  REMARK    GeneRIF: Identified all functional AQP4 isoforms -M1, M23, and Mz-
            and the formation of higher-order complexes in the organ of Corti
            of the rat.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Moe,S.E., Sorbo,J.G., Sogaard,R., Zeuthen,T., Petter Ottersen,O.
            and Holen,T.
  TITLE     New isoforms of rat Aquaporin-4
  JOURNAL   Genomics 91 (4), 367-377 (2008)
   PUBMED   18255256
  REMARK    GeneRIF: rat AQP4 has six cDNA isoforms, formed by alternative
            splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond
            to the two classical M1 and M23 isoforms, respectively
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Jung,J.S., Bhat,R.V., Preston,G.M., Guggino,W.B., Baraban,J.M. and
            Agre,P.
  TITLE     Molecular characterization of an aquaporin cDNA from brain:
            candidate osmoreceptor and regulator of water balance
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 13052-13056 (1994)
   PUBMED   7528931
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000018.1.
            
            Summary: This gene encodes a member of the aquaporin family of
            intrinsic membrane proteins that function as water-selective
            channels in the plasma membranes of many cells. This protein is the
            predominant aquaporin found in brain and has an important role in
            brain water homeostasis. Alternatively spliced transcript variants
            encoding different isoforms have been described for this gene. A
            recent study provided evidence for translational readthrough in
            this gene and expression of an additional C-terminally extended
            isoform via the use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2, also known as AQP4c) contains
            an alternate 5' terminal exon, which causes translation initiation
            from an in-frame, downstream start codon, compared to variant 1.
            The resulting isoform (M23) has a shorter N-terminus compared to
            isoform M1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.746681.1,
                                           SRR26360176.2309478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..301
                     /product="aquaporin-4 isoform M23"
                     /note="mercurial-insensitive water channel"
                     /calculated_mol_wt=32031
     Region          9..226
                     /region_name="MIP"
                     /note="Major intrinsic protein; pfam00230"
                     /db_xref="CDD:395174"
     Site            order(55,73..75,187..188,191,194)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(75..77,191..193)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..301
                     /gene="Aqp4"
                     /gene_synonym="AQP-4; Miwc; WCH4"
                     /coded_by="NM_001142366.2:141..1046"
                     /note="isoform M23 is encoded by transcript variant 2"
                     /db_xref="GeneID:25293"
                     /db_xref="RGD:2143"
ORIGIN      
        1 mvafkgvwtq afwkavtaef lamlifvlls vgstinwggs enplpvdmvl islcfglsia
       61 tmvqcfghis gghinpavtv amvctrkisi aksvfyitaq clgaiigagi lylvtppsvv
      121 gglgvttvhg nltaghgllv eliitfqlvf tifascdskr tdvtgsvala igfsvaighl
      181 fainytgasm nparsfgpav imgnwenhwi ywvgpiigav lagalyeyvf cpdvelkrrl
      241 keafskaaqq tkgsymeved nrsqvetedl ilkpgvvhvi didrgdekkg kdssgevlss
      301 v
//
LOCUS       NP_001291663             310 aa            linear   ROD 18-MAR-2025
DEFINITION  mu-type opioid receptor isoform 1G2 [Rattus norvegicus].
ACCESSION   NP_001291663
VERSION     NP_001291663.1
DBSOURCE    REFSEQ: accession NM_001304734.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bischoff,A.R., Dalle Molle,R., Mucellini,A.B., Pokhvisneva,I.,
            Levitan,R.D., Meaney,M.J. and Silveira,P.P.
  TITLE     Accumbal mu-opioid receptors and salt taste-elicited hedonic
            responses in a rodent model of prenatal adversity, and their
            correlates using human functional genomics
  JOURNAL   Stress 27 (1), 2294954 (2024)
   PUBMED   38140734
  REMARK    GeneRIF: Accumbal mu-opioid receptors and salt taste-elicited
            hedonic responses in a rodent model of prenatal adversity, and
            their correlates using human functional genomics.
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Miyahara,K., Hino,M., Shishido,R., Izumi,R., Nagaoka,A.,
            Hayashi,H., Kakita,A., Yabe,H., Tomita,H. and Kunii,Y.
  TITLE     Ethnicity-dependent effect of rs1799971 polymorphism on OPRM1
            expression in the postmortem brain and responsiveness to
            antipsychotics
  JOURNAL   J Psychiatr Res 166, 10-16 (2023)
   PUBMED   37659266
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Yu,J., Zhang,Y., Xun,Y., Tang,H., Fu,X., Zhang,R., Zhu,F. and
            Zhang,J.
  TITLE     Methylation and expression quantitative trait loci rs1799971 in the
            OPRM1 gene and rs4654327 in the OPRD1 gene are associated with
            opioid use disorder
  JOURNAL   Neurosci Lett 814, 137468 (2023)
   PUBMED   37660978
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Chen,Y., Han,Y., Liu,L., Liu,M., Lin,J., Tang,Y., Guo,S., He,R. and
            Wu,Q.
  TITLE     N6-Methyladenosine methylase METTL3 contributes to neuropathic pain
            by epigenetic silencing of mu opioid receptor
  JOURNAL   Behav Brain Res 452, 114592 (2023)
   PUBMED   37482304
  REMARK    GeneRIF: N[6]-Methyladenosine methylase METTL3 contributes to
            neuropathic pain by epigenetic silencing of mu opioid receptor.
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Danisman,M., Bal,C., Ogur,B.
            and Ispir,G.Z.
  TITLE     OPRD1 rs569356 polymorphism has an effect on plasma
            norbuprenorphine levels and dose/kg-normalized norbuprenorphine
            values in individuals with opioid use disorder
  JOURNAL   Environ Toxicol Pharmacol 100, 104143 (2023)
   PUBMED   37146669
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Sedqi,M., Roy,S., Ramakrishnan,S., Elde,R. and Loh,H.H.
  TITLE     Complementary DNA cloning of a mu-opioid receptor from rat
            peritoneal macrophages
  JOURNAL   Biochem Biophys Res Commun 209 (2), 563-574 (1995)
   PUBMED   7733926
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Zimprich,A., Simon,T. and Hollt,V.
  TITLE     Cloning and expression of an isoform of the rat mu opioid receptor
            (rMOR1B) which differs in agonist induced desensitization from
            rMOR1
  JOURNAL   FEBS Lett 359 (2-3), 142-146 (1995)
   PUBMED   7532594
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Bunzow,J.R., Zhang,G., Bouvier,C., Saez,C., Ronnekleiv,O.K.,
            Kelly,M.J. and Grandy,D.K.
  TITLE     Characterization and distribution of a cloned rat mu-opioid
            receptor
  JOURNAL   J Neurochem 64 (1), 14-24 (1995)
   PUBMED   7798908
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Surratt,C.K., Johnson,P.S., Moriwaki,A., Seidleck,B.K.,
            Blaschak,C.J., Wang,J.B. and Uhl,G.R.
  TITLE     -mu opiate receptor. Charged transmembrane domain amino acids are
            critical for agonist recognition and intrinsic activity
  JOURNAL   J Biol Chem 269 (32), 20548-20553 (1994)
   PUBMED   8051154
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Schroeder,J.E., Fischbach,P.S., Zheng,D. and McCleskey,E.W.
  TITLE     Activation of mu opioid receptors inhibits transient high- and
            low-threshold Ca2+ currents, but spares a sustained current
  JOURNAL   Neuron 6 (1), 13-20 (1991)
   PUBMED   1846076
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (MOR-1G2) represents use of an
            alternate promoter and 5' UTR, and uses an alternate 3' exon,
            compared to variant MOR-1C2. The resulting isoform (1G2) is shorter
            than isoform 1C2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU024650.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..310
                     /product="mu-type opioid receptor isoform 1G2"
                     /note="mu-type opioid receptor; MOR-1; MUOR1; opioid
                     receptor B; M-OR-1"
                     /calculated_mol_wt=35315
     Region          8..259
                     /region_name="7tmA_Mu_opioid_R"
                     /note="opioid receptor subtype mu, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15090"
                     /db_xref="CDD:320218"
     Region          15..41
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320218"
     Site            order(36,39..40,52..57,59..60,63,108,110..114,141,
                     144..146,148..150,152..153,205,208..209,211..212,215,
                     226..227,229..231,234,237..238)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320218"
     Region          52..82
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320218"
     Region          94..116
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320218"
     Region          141..170
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320218"
     Region          185..215
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320218"
     Region          227..252
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320218"
     CDS             1..310
                     /gene="Oprm1"
                     /gene_synonym="MORA; Oprm; Oprrm1"
                     /coded_by="NM_001304734.1:70..1002"
                     /note="isoform 1G2 is encoded by transcript variant
                     MOR-1G2"
                     /db_xref="GeneID:25601"
                     /db_xref="RGD:3234"
ORIGIN      
        1 mgsgpmlytk mktatniyif nlaladalat stlpfqsvny lmgtwpfgti lckivisidy
       61 ynmftsiftl ctmsvdryia vchpvkaldf rtprnakivn vcnwilssai glpvmfmatt
      121 kyrqgsidct ltfshptwyw enllkicvfi fafimpvlii tvcyglmilr lksvrmlsgs
      181 kekdrnlrri trmvlvvvav fivcwtpihi yviikaliti pettfqtvsw hfcialgytn
      241 sclnpvlyaf ldenfkrcfr efciptssti eqqnstrvrq ntrehpstan tvdrtnhqle
      301 nleaetaplp
//
LOCUS       NP_001423632             347 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein CCDC163 isoform a [Rattus norvegicus].
ACCESSION   NP_001423632 XP_063143482
VERSION     NP_001423632.1
DBSOURCE    REFSEQ: accession NM_001436703.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143482.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.22610.1,
                                           SRR26643293.29438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..347
                     /product="transmembrane protein CCDC163 isoform a"
                     /note="transmembrane protein CCDC163"
                     /calculated_mol_wt=39374
     Region          <82..>262
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..347
                     /gene="Ccdc163"
                     /coded_by="NM_001436703.1:230..1273"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:298442"
                     /db_xref="RGD:1564486"
ORIGIN      
        1 msrssswsdq lqavlsstde nmarikqsly plrvsstgdl adtwisphhl ppqpgaqaqq
       61 pwalktpilg eslscteahs sslwdevtkl rsqlqtqtqv tealrhsvqs llkdreqqmf
      121 kisaleaslk llqegpkgra lleqrleglr kelqglrsqv qelvqtqmrt rpgkfstasg
      181 fhqelqnehq llweeseilr eelkllrdql sqhqellleq maegrqvqar swktlehlqs
      241 gqmgkvhtle vtrteahdaq keepyllrss vharqsklpl atifdmslss sssevslpdc
      301 drswellkkl drelqnnsls nlepsssqfh aqdvgqedlf lhgprif
//
LOCUS       NP_001423614             310 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423614 XP_006252686
VERSION     NP_001423614.1
DBSOURCE    REFSEQ: accession NM_001436685.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252686.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.35059.1,
                                           SRR26643298.70568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..310
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 1"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=34716
     Region          68..307
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136,177)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(133,136,139,146)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99778"
     Site            order(172,176..179,181)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99778"
     Site            order(177..178,213..215,282..283)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..310
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436685.1:374..1306"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkctldseva lrvggefffd pqptdaprnl vliaggvgin
      181 pllsilrhsa dlhrdhkekr rgydigtikl fysakntsel lfkknildlv hefpekiacs
      241 fhvtkqttqi sselkpyvtd gritekeire hisaetlfyv cgpppmtdff skhlesshvp
      301 kehicfekww
//
LOCUS       NP_001423622             188 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 5
            [Rattus norvegicus].
ACCESSION   NP_001423622
VERSION     NP_001423622.1
DBSOURCE    REFSEQ: accession NM_001436693.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM085077.1, SRR26360172.2954389.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..188
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 5"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=20767
     Region          68..>141
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
     Site            order(95,107..110,127..129,133..136)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..188
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436693.1:267..833"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkvsnhlkhn flvcvstvpa clfvhhmrvs fpqrwsdsle
      181 leplmvvs
//
LOCUS       NP_001423608             342 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein 268 [Rattus norvegicus].
ACCESSION   NP_001423608 XP_017448741
VERSION     NP_001423608.1
DBSOURCE    REFSEQ: accession NM_001436679.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_017448741.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2276865.1,
                                           SRR22582416.578538.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..342
                     /product="transmembrane protein 268"
                     /note="transmembrane protein C9orf91 homolog"
                     /calculated_mol_wt=37799
     Region          39..328
                     /region_name="DUF4481"
                     /note="Domain of unknown function (DUF4481); pfam14800"
                     /db_xref="CDD:464322"
     CDS             1..342
                     /gene="Tmem268"
                     /gene_synonym="RGD1304595"
                     /coded_by="NM_001436679.1:344..1372"
                     /db_xref="GeneID:298104"
                     /db_xref="RGD:1304595"
ORIGIN      
        1 maceppsdpg gaagplptst lgcstlpqgn ppgwgeelhn gqvlsvlrid ntcapisfdl
       61 rvaeeqlqaw giqvpaeqyr slaesallep qvrryiiyns rpmrlafavv fyvlvwaniy
      121 stsqmfalgn qwagvllatl aavsltltlv lvferqqrka ntntdlrlva angallrhrv
      181 llgvtdtveg cqsviqlwfv yfdlencvqf lsdhvqemkr sqesllrsrl sqlcvvmetg
      241 vspvverped ledspllprt pgpqerpltq telyqlvpea epeemarqll avfggyytrl
      301 lvtsqlpqpm gtrhmdsari pcpcqlievh ilgtgccpfl ar
//
LOCUS       NP_001020827             347 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein CCDC163 isoform a [Rattus norvegicus].
ACCESSION   NP_001020827 XP_216494
VERSION     NP_001020827.1
DBSOURCE    REFSEQ: accession NM_001025656.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 22, 2005 this sequence version replaced XP_216494.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098949.1, SRR26643429.20484.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..347
                     /product="transmembrane protein CCDC163 isoform a"
                     /note="transmembrane protein CCDC163"
                     /calculated_mol_wt=39374
     Region          <82..>262
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..347
                     /gene="Ccdc163"
                     /coded_by="NM_001025656.2:433..1476"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:298442"
                     /db_xref="RGD:1564486"
ORIGIN      
        1 msrssswsdq lqavlsstde nmarikqsly plrvsstgdl adtwisphhl ppqpgaqaqq
       61 pwalktpilg eslscteahs sslwdevtkl rsqlqtqtqv tealrhsvqs llkdreqqmf
      121 kisaleaslk llqegpkgra lleqrleglr kelqglrsqv qelvqtqmrt rpgkfstasg
      181 fhqelqnehq llweeseilr eelkllrdql sqhqellleq maegrqvqar swktlehlqs
      241 gqmgkvhtle vtrteahdaq keepyllrss vharqsklpl atifdmslss sssevslpdc
      301 drswellkkl drelqnnsls nlepsssqfh aqdvgqedlf lhgprif
//
LOCUS       NP_001423649             277 aa            linear   ROD 19-MAR-2025
DEFINITION  mitochondrial fission regulator 1-like isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423649 XP_038965567
VERSION     NP_001423649.1
DBSOURCE    REFSEQ: accession NM_001436720.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_038965567.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2729709.1,
                                           SRR26643429.21257.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMEA5760434 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..277
                     /product="mitochondrial fission regulator 1-like isoform
                     b"
                     /note="protein FAM54B; family with sequence similarity 54,
                     member B"
                     /calculated_mol_wt=30422
     Region          7..238
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     CDS             1..277
                     /gene="Mtfr1l"
                     /gene_synonym="Fam54b; RGD1305453"
                     /coded_by="NM_001436720.1:164..997"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="GeneID:298549"
                     /db_xref="RGD:1305453"
ORIGIN      
        1 meanvtipiw qnkphgaars vvrrigtnlp lkpcprasfe tlpnisdlcl kdvppvptla
       61 diawiaadee etyarvrsdt rplrhtwkps plivmqrnas vpnlrgseer llalkkpalp
      121 alsrttelqd elshlrsqia kivaadagss nvssplpcfg ssfhsttsfv isditeetev
      181 evpelptipl lcsaspecck sehkttcsss eeddcislsk assfadmmgi lkdfhrikqs
      241 qdlsrsllke edpavlisev lrrkfalkee disrkgn
//
LOCUS       NP_001005543             776 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform a [Rattus norvegicus].
ACCESSION   NP_001005543 XP_216505
VERSION     NP_001005543.1
DBSOURCE    REFSEQ: accession NM_001005543.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Oct 8, 2004 this sequence version replaced XP_216505.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081913.1, SRR26643293.29379.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..776
                     /product="nuclear autoantigenic sperm protein isoform a"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=84069
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          115..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          <130..506
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          210..242
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          256..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          345..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          457..500
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          499..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          528..604
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          530..567
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          530..563
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          530..558
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(531,534..535,538..539,541,573,576..577,580..581,
                     583..584,605,608..609,612)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          563..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          572..605
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          685..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          704..710
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     CDS             1..776
                     /gene="Nasp"
                     /coded_by="NM_001005543.2:184..2514"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 matestataa iaaelvsadk vedapapsts adkmesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnvdeear eelreqvyda mgekeakkae gqsltkpetd keqesevekg
      181 gredmdisep aeklqekves tskqltesse eakeaaipgl nedevtsgkt eqeslcteeg
      241 ksisgvyvqn kefreavpqe egeemislek kpketsedqt igapekqdtl mkvveieaei
      301 dsevksvdvg geepkdqgai seselgkavl mqlsgqdvev spvvaaeags evsekpgqei
      361 tvlpnngpvv gqssagdqtp sepqnsaerl setkdgasve evkaelvpeq eeamppvees
      421 eaagdgvetk vaqratekap edkfkiaane etqerdeqmk egeetegsee edkendkaee
      481 ttnesvlekk tlqeneeeei gnlelawdml dlakiifkrq etkeaqlyaa qahlklgevs
      541 vesenyiqav eefqaclslq eqyleahdrl laethyqlgl aygynsqyde avaqfgksid
      601 viekrmavll eqmkeaegsf teyekeieel kellpeirek iedakesqrs gnvaelalka
      661 tlvesstsgf tpsgagasvs miasrkptdg asssncvtdi shlvrkkrkp eeesprkdda
      721 kkakpepevn ggsgdavssg nevsenmeae aenqaesqtt aegtvdsaat vkstac
//
LOCUS       NP_001423621             229 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 4
            [Rattus norvegicus].
ACCESSION   NP_001423621
VERSION     NP_001423621.1
DBSOURCE    REFSEQ: accession NM_001436692.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2101463.1,
                                           SRR26360181.817975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..229
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 4"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=25445
     Region          68..>144
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
     Site            order(95,107..110,127..129,133..136)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..229
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436692.1:267..956"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkrlqrilac vgtsckerke anrsrcyrss rtdacwgtws
      181 ivqqsswesr lsvlaavqls eeksypenqk qaifvasnmp lfwalklan
//
LOCUS       NP_001423645             289 aa            linear   ROD 19-MAR-2025
DEFINITION  mitochondrial fission regulator 1-like isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423645
VERSION     NP_001423645.1
DBSOURCE    REFSEQ: accession NM_001436716.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16497.1,
                                           SRR26643296.16349.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..289
                     /product="mitochondrial fission regulator 1-like isoform
                     a"
                     /note="protein FAM54B; family with sequence similarity 54,
                     member B"
                     /calculated_mol_wt=31599
     Region          7..250
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     CDS             1..289
                     /gene="Mtfr1l"
                     /gene_synonym="Fam54b; RGD1305453"
                     /coded_by="NM_001436716.1:264..1133"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:298549"
                     /db_xref="RGD:1305453"
ORIGIN      
        1 meanvtipiw qnkphgaars vvrrigtnlp lkpcprasfe tlpnisdlcl kdvppvptla
       61 diawiaadee etyarvrsdt rplrhtwkps plivmqrnas vpnlrgseer llalkkpalp
      121 alsrttelqd elshlrsqia kivaadaasa sltpdflssg ssnvssplpc fgssfhstts
      181 fvisditeet evevpelpti pllcsaspec cksehkttcs sseeddcisl skassfadmm
      241 gilkdfhrik qsqdlsrsll keedpavlis evlrrkfalk eedisrkgn
//
LOCUS       NP_001423639             615 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423639 XP_006238863
VERSION     NP_001423639.1
DBSOURCE    REFSEQ: accession NM_001436710.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238863.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.120708.1,
                                           SRR26360181.873338.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..615
                     /product="polyadenylate-binding protein 4 isoform 7"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=67891
     Region          11..595
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..615
                     /gene="Pabpc4"
                     /coded_by="NM_001436710.1:885..2732"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgv ptavpnlapr
      481 atvaaaapra vapykyasnv rsphpaiqpl qapqpavhvq gqepltasml aaappqeqkq
      541 mlgerlfpli qtmhsnlagk itgmlleidn sellhmlesp eslrskvdea vavlqahhak
      601 keaaqkvgtv aaats
//
LOCUS       NP_001423625             776 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform a [Rattus norvegicus].
ACCESSION   NP_001423625 XP_008762215
VERSION     NP_001423625.1
DBSOURCE    REFSEQ: accession NM_001436696.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_008762215.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29399.1,
                                           SRR26360181.1716953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..776
                     /product="nuclear autoantigenic sperm protein isoform a"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=84069
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          115..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          <130..506
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          210..242
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          256..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          345..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          457..500
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          499..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          528..604
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          530..567
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          530..563
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          530..558
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(531,534..535,538..539,541,573,576..577,580..581,
                     583..584,605,608..609,612)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          563..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          572..605
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          685..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          704..710
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     CDS             1..776
                     /gene="Nasp"
                     /coded_by="NM_001436696.1:235..2565"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 matestataa iaaelvsadk vedapapsts adkmesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnvdeear eelreqvyda mgekeakkae gqsltkpetd keqesevekg
      181 gredmdisep aeklqekves tskqltesse eakeaaipgl nedevtsgkt eqeslcteeg
      241 ksisgvyvqn kefreavpqe egeemislek kpketsedqt igapekqdtl mkvveieaei
      301 dsevksvdvg geepkdqgai seselgkavl mqlsgqdvev spvvaaeags evsekpgqei
      361 tvlpnngpvv gqssagdqtp sepqnsaerl setkdgasve evkaelvpeq eeamppvees
      421 eaagdgvetk vaqratekap edkfkiaane etqerdeqmk egeetegsee edkendkaee
      481 ttnesvlekk tlqeneeeei gnlelawdml dlakiifkrq etkeaqlyaa qahlklgevs
      541 vesenyiqav eefqaclslq eqyleahdrl laethyqlgl aygynsqyde avaqfgksid
      601 viekrmavll eqmkeaegsf teyekeieel kellpeirek iedakesqrs gnvaelalka
      661 tlvesstsgf tpsgagasvs miasrkptdg asssncvtdi shlvrkkrkp eeesprkdda
      721 kkakpepevn ggsgdavssg nevsenmeae aenqaesqtt aegtvdsaat vkstac
//
LOCUS       NP_001423643             849 aa            linear   ROD 19-MAR-2025
DEFINITION  granulocyte colony-stimulating factor receptor isoform b precursor
            [Rattus norvegicus].
ACCESSION   NP_001423643 XP_038965551
VERSION     NP_001423643.1
DBSOURCE    REFSEQ: accession NM_001436714.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Zhang,E., Lee,S., Yi,M.H., Nan,Y., Xu,Y., Shin,N., Ko,Y., Lee,Y.H.,
            Lee,W. and Kim,D.W.
  TITLE     Expression of granulocyte colony-stimulating factor 3 receptor in
            the spinal dorsal horn following spinal nerve ligation-induced
            neuropathic pain
  JOURNAL   Mol Med Rep 16 (2), 2009-2015 (2017)
   PUBMED   28656207
  REMARK    GeneRIF: the expression of GCSFR in neurons following peripheral
            nerve injury may be involved in the induction and maintenance of
            neuropathic pain through the STAT3 and TRPV1 signaling pathway.
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Aref,S., El-Ghonemy,M., Abouzeid,T., El-Sabbagh,A. and El-Baiomy,M.
  TITLE     Prevalence and impact of colony stimulating factor 3 receptor
            (CSF3R) mutations among Egyptian acute myeloid leukemia patients
  JOURNAL   Leuk Res 38 (6), 722-725 (2014)
   PUBMED   24746896
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Fleischman,A.G., Maxson,J.E., Luty,S.B., Agarwal,A., Royer,L.R.,
            Abel,M.L., MacManiman,J.D., Loriaux,M.M., Druker,B.J. and
            Tyner,J.W.
  TITLE     The CSF3R T618I mutation causes a lethal neutrophilic neoplasia in
            mice that is responsive to therapeutic JAK inhibition
  JOURNAL   Blood 122 (22), 3628-3631 (2013)
   PUBMED   24081659
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Kosmider,O., Itzykson,R., Chesnais,V., Lasho,T., Laborde,R.,
            Knudson,R., Gauthier,A., Merlevede,J., Ades,L., Morabito,M.,
            Fontenay,M., Tefferi,A., Droin,N. and Solary,E.
  TITLE     Mutation of the colony-stimulating factor-3 receptor gene is a rare
            event with poor prognosis in chronic myelomonocytic leukemia
  JOURNAL   Leukemia 27 (9), 1946-1949 (2013)
   PUBMED   23774674
REFERENCE   5  (residues 1 to 849)
  AUTHORS   Hanumanthu,V.S. and Pirruccello,S.J.
  TITLE     GCSF-R expression in myelodysplastic and myeloproliferative
            disorders and blast dysmaturation in CML
  JOURNAL   Am J Clin Pathol 140 (2), 155-164 (2013)
   PUBMED   23897249
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Semerad,C.L., Poursine-Laurent,J., Liu,F. and Link,D.C.
  TITLE     A role for G-CSF receptor signaling in the regulation of
            hematopoietic cell function but not lineage commitment or
            differentiation
  JOURNAL   Immunity 11 (2), 153-161 (1999)
   PUBMED   10485650
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Otsuji,W., Tanase,S., Yoshida,S. and Bawden,J.W.
  TITLE     The immunohistochemical localization of the interferon-gamma and
            granulocyte colony-stimulating factor receptors during early
            amelogenesis in rat molars
  JOURNAL   Arch Oral Biol 44 (2), 173-181 (1999)
   PUBMED   10206335
REFERENCE   8  (residues 1 to 849)
  AUTHORS   Hermans,M.H., Ward,A.C., Antonissen,C., Karis,A., Lowenberg,B. and
            Touw,I.P.
  TITLE     Perturbed granulopoiesis in mice with a targeted mutation in the
            granulocyte colony-stimulating factor receptor gene associated with
            severe chronic neutropenia
  JOURNAL   Blood 92 (1), 32-39 (1998)
   PUBMED   9639496
REFERENCE   9  (residues 1 to 849)
  AUTHORS   Dong,F., Dale,D.C., Bonilla,M.A., Freedman,M., Fasth,A.,
            Neijens,H.J., Palmblad,J., Briars,G.L., Carlsson,G., Veerman,A.J.,
            Welte,K., Lowenberg,B. and Touw,I.P.
  TITLE     Mutations in the granulocyte colony-stimulating factor receptor
            gene in patients with severe congenital neutropenia
  JOURNAL   Leukemia 11 (1), 120-125 (1997)
   PUBMED   9001427
REFERENCE   10 (residues 1 to 849)
  AUTHORS   Fukunaga,R., Ishizaka-Ikeda,E., Seto,Y. and Nagata,S.
  TITLE     Expression cloning of a receptor for murine granulocyte
            colony-stimulating factor
  JOURNAL   Cell 61 (2), 341-350 (1990)
   PUBMED   2158861
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_038965551.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.7664.1,
                                           SRR26360194.1669309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..849
                     /product="granulocyte colony-stimulating factor receptor
                     isoform b precursor"
                     /note="granulocyte colony-stimulating factor receptor;
                     colony stimulating factor 3 receptor (granulocyte)"
                     /calculated_mol_wt=92409
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2540
     Region          24..111
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Region          123..221
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          444..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(524..525,527..528)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(540,604,619)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          543..620
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     CDS             1..849
                     /gene="Csf3r"
                     /coded_by="NM_001436714.1:350..2899"
                     /note="isoform b precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:298518"
                     /db_xref="RGD:1309114"
ORIGIN      
        1 mvglgacnlt gvtlivlllp rslegcgqir isppivhlgd pvlasctisp ncskldrqpk
       61 ilwrlqdepn qpgdrqhhlp dgsqesiitl phlnytqafl fclvpwnnsf qvldqaelra
      121 gyppaspsnl sclmylttns lvcqwepgpe thlptsfilk sfrsrtgcqy qggtildcmp
      181 kkrhsncsip rkhlllyqnm viwvqaenml gssespklci dpmdvgresl ttpppavkle
      241 ppmlqaldig hdivsrqpgc lwlswkpwkp sefmeqecel ryqpqlegan wtlvshlpss
      301 tdrfelcslh qapvytlqlr cirsslpglw sswspglqlr ptikaptirl dtwwqkkhld
      361 petvrmqlfw kptplqkdsg qiqgyllsws cpdgqgrimh lcnttelsct fhlpseaqnv
      421 tlvaynsagt ssptlvvfle hegpavtslh amaqdlgsiw vdweapsllp qgyliewgpd
      481 shkysnnswr iepngnttgi llednihpfq lyritvaply pgtvgppvnv ytysgekalp
      541 hapelylkhv grtwaqlewv petpwlgmip ltnytifwtd ardhsfsvtl nisfhdfvld
      601 hlkpaslyhv ylmatsrags tnstgltlmt maldssdvni flgilcfvll sitcatawfc
      661 ckqsrktffw pnvpdpahss lsawvptimt eetfqlpsfw gssvpsitki teleedkkpt
      721 hwdpsessgt gslpavvqay vlqgdpreis nqfqppsstn dqvlygqvlg sptspevvgy
      781 lrcdstqpll ggptpspksy eniwfhsrpq etfipqppsq eddcvfgppf dfplfqglqv
      841 hgveeqggf
//
LOCUS       NP_001423590             263 aa            linear   ROD 19-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423590
VERSION     NP_001423590.1
DBSOURCE    REFSEQ: accession NM_001436661.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74640.1,
                                           SRR26360186.619255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..263
                     /product="spermatogenesis-associated protein 4 isoform 3"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=30069
     Region          17..91
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     CDS             1..263
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001436661.1:214..1005"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 mlpgaearqd qviqpllprd fsngylvaei fciyypwdlr lssfengtsl kvkldnwaqi
       61 ekflakkkfk lpkelihgti hckagvpeil iqeiytllth qeirsiqddf anftdysyqm
      121 rlplvprstv sksiknnirl sellsnpnil snelkieflf llqmlqrkls rklnpgwfdi
      181 kptvgeitvg hlpahsykhk ykskvskera vsslsksgnd vqphreihvk qngkpcdata
      241 kpminveetm kdteevalkk sch
//
LOCUS       NP_001423592             144 aa            linear   ROD 19-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423592
VERSION     NP_001423592.1
DBSOURCE    REFSEQ: accession NM_001436663.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.694718.1,
                                           SRR26360181.3359500.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..144
                     /product="spermatogenesis-associated protein 4 isoform 5"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=16221
     CDS             1..144
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001436663.1:441..875"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 mrlplvprst vsksiknnir lsellsnpni lsnelkiefl fllqmlqrkl srklnpgwfd
       61 ikptvgeitv ghlpahsykh kykskvsker avsslsksgn dvqphreihv kqngkpcdat
      121 akpminveet mkdteevalk ksch
//
LOCUS       NP_001423626             776 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform a [Rattus norvegicus].
ACCESSION   NP_001423626 XP_006238708
VERSION     NP_001423626.1
DBSOURCE    REFSEQ: accession NM_001436697.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238708.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29380.1,
                                           SRR26360181.720552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..776
                     /product="nuclear autoantigenic sperm protein isoform a"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=84069
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          115..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          <130..506
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          210..242
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          256..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          345..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          457..500
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          499..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          528..604
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          530..567
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          530..563
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          530..558
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(531,534..535,538..539,541,573,576..577,580..581,
                     583..584,605,608..609,612)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          563..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          572..605
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          685..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          704..710
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     CDS             1..776
                     /gene="Nasp"
                     /coded_by="NM_001436697.1:80..2410"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 matestataa iaaelvsadk vedapapsts adkmesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnvdeear eelreqvyda mgekeakkae gqsltkpetd keqesevekg
      181 gredmdisep aeklqekves tskqltesse eakeaaipgl nedevtsgkt eqeslcteeg
      241 ksisgvyvqn kefreavpqe egeemislek kpketsedqt igapekqdtl mkvveieaei
      301 dsevksvdvg geepkdqgai seselgkavl mqlsgqdvev spvvaaeags evsekpgqei
      361 tvlpnngpvv gqssagdqtp sepqnsaerl setkdgasve evkaelvpeq eeamppvees
      421 eaagdgvetk vaqratekap edkfkiaane etqerdeqmk egeetegsee edkendkaee
      481 ttnesvlekk tlqeneeeei gnlelawdml dlakiifkrq etkeaqlyaa qahlklgevs
      541 vesenyiqav eefqaclslq eqyleahdrl laethyqlgl aygynsqyde avaqfgksid
      601 viekrmavll eqmkeaegsf teyekeieel kellpeirek iedakesqrs gnvaelalka
      661 tlvesstsgf tpsgagasvs miasrkptdg asssncvtdi shlvrkkrkp eeesprkdda
      721 kkakpepevn ggsgdavssg nevsenmeae aenqaesqtt aegtvdsaat vkstac
//
LOCUS       NP_001423609             342 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein 268 [Rattus norvegicus].
ACCESSION   NP_001423609 XP_017448744
VERSION     NP_001423609.1
DBSOURCE    REFSEQ: accession NM_001436680.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_017448744.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1700976.1,
                                           SRR26360194.2152557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..342
                     /product="transmembrane protein 268"
                     /note="transmembrane protein C9orf91 homolog"
                     /calculated_mol_wt=37799
     Region          39..328
                     /region_name="DUF4481"
                     /note="Domain of unknown function (DUF4481); pfam14800"
                     /db_xref="CDD:464322"
     CDS             1..342
                     /gene="Tmem268"
                     /gene_synonym="RGD1304595"
                     /coded_by="NM_001436680.1:319..1347"
                     /db_xref="GeneID:298104"
                     /db_xref="RGD:1304595"
ORIGIN      
        1 maceppsdpg gaagplptst lgcstlpqgn ppgwgeelhn gqvlsvlrid ntcapisfdl
       61 rvaeeqlqaw giqvpaeqyr slaesallep qvrryiiyns rpmrlafavv fyvlvwaniy
      121 stsqmfalgn qwagvllatl aavsltltlv lvferqqrka ntntdlrlva angallrhrv
      181 llgvtdtveg cqsviqlwfv yfdlencvqf lsdhvqemkr sqesllrsrl sqlcvvmetg
      241 vspvverped ledspllprt pgpqerpltq telyqlvpea epeemarqll avfggyytrl
      301 lvtsqlpqpm gtrhmdsari pcpcqlievh ilgtgccpfl ar
//
LOCUS       NP_001423642             838 aa            linear   ROD 19-MAR-2025
DEFINITION  granulocyte colony-stimulating factor receptor isoform a precursor
            [Rattus norvegicus].
ACCESSION   NP_001423642 XP_063143508
VERSION     NP_001423642.1
DBSOURCE    REFSEQ: accession NM_001436713.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Zhang,E., Lee,S., Yi,M.H., Nan,Y., Xu,Y., Shin,N., Ko,Y., Lee,Y.H.,
            Lee,W. and Kim,D.W.
  TITLE     Expression of granulocyte colony-stimulating factor 3 receptor in
            the spinal dorsal horn following spinal nerve ligation-induced
            neuropathic pain
  JOURNAL   Mol Med Rep 16 (2), 2009-2015 (2017)
   PUBMED   28656207
  REMARK    GeneRIF: the expression of GCSFR in neurons following peripheral
            nerve injury may be involved in the induction and maintenance of
            neuropathic pain through the STAT3 and TRPV1 signaling pathway.
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Aref,S., El-Ghonemy,M., Abouzeid,T., El-Sabbagh,A. and El-Baiomy,M.
  TITLE     Prevalence and impact of colony stimulating factor 3 receptor
            (CSF3R) mutations among Egyptian acute myeloid leukemia patients
  JOURNAL   Leuk Res 38 (6), 722-725 (2014)
   PUBMED   24746896
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Fleischman,A.G., Maxson,J.E., Luty,S.B., Agarwal,A., Royer,L.R.,
            Abel,M.L., MacManiman,J.D., Loriaux,M.M., Druker,B.J. and
            Tyner,J.W.
  TITLE     The CSF3R T618I mutation causes a lethal neutrophilic neoplasia in
            mice that is responsive to therapeutic JAK inhibition
  JOURNAL   Blood 122 (22), 3628-3631 (2013)
   PUBMED   24081659
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Kosmider,O., Itzykson,R., Chesnais,V., Lasho,T., Laborde,R.,
            Knudson,R., Gauthier,A., Merlevede,J., Ades,L., Morabito,M.,
            Fontenay,M., Tefferi,A., Droin,N. and Solary,E.
  TITLE     Mutation of the colony-stimulating factor-3 receptor gene is a rare
            event with poor prognosis in chronic myelomonocytic leukemia
  JOURNAL   Leukemia 27 (9), 1946-1949 (2013)
   PUBMED   23774674
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Hanumanthu,V.S. and Pirruccello,S.J.
  TITLE     GCSF-R expression in myelodysplastic and myeloproliferative
            disorders and blast dysmaturation in CML
  JOURNAL   Am J Clin Pathol 140 (2), 155-164 (2013)
   PUBMED   23897249
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Semerad,C.L., Poursine-Laurent,J., Liu,F. and Link,D.C.
  TITLE     A role for G-CSF receptor signaling in the regulation of
            hematopoietic cell function but not lineage commitment or
            differentiation
  JOURNAL   Immunity 11 (2), 153-161 (1999)
   PUBMED   10485650
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Otsuji,W., Tanase,S., Yoshida,S. and Bawden,J.W.
  TITLE     The immunohistochemical localization of the interferon-gamma and
            granulocyte colony-stimulating factor receptors during early
            amelogenesis in rat molars
  JOURNAL   Arch Oral Biol 44 (2), 173-181 (1999)
   PUBMED   10206335
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Hermans,M.H., Ward,A.C., Antonissen,C., Karis,A., Lowenberg,B. and
            Touw,I.P.
  TITLE     Perturbed granulopoiesis in mice with a targeted mutation in the
            granulocyte colony-stimulating factor receptor gene associated with
            severe chronic neutropenia
  JOURNAL   Blood 92 (1), 32-39 (1998)
   PUBMED   9639496
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Dong,F., Dale,D.C., Bonilla,M.A., Freedman,M., Fasth,A.,
            Neijens,H.J., Palmblad,J., Briars,G.L., Carlsson,G., Veerman,A.J.,
            Welte,K., Lowenberg,B. and Touw,I.P.
  TITLE     Mutations in the granulocyte colony-stimulating factor receptor
            gene in patients with severe congenital neutropenia
  JOURNAL   Leukemia 11 (1), 120-125 (1997)
   PUBMED   9001427
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Fukunaga,R., Ishizaka-Ikeda,E., Seto,Y. and Nagata,S.
  TITLE     Expression cloning of a receptor for murine granulocyte
            colony-stimulating factor
  JOURNAL   Cell 61 (2), 341-350 (1990)
   PUBMED   2158861
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143508.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.7666.1,
                                           SRR26360194.4951.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..838
                     /product="granulocyte colony-stimulating factor receptor
                     isoform a precursor"
                     /note="granulocyte colony-stimulating factor receptor;
                     colony stimulating factor 3 receptor (granulocyte)"
                     /calculated_mol_wt=91301
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2540
     Region          24..111
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Region          123..221
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          433..521
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(513..514,516..517)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(529,593,608)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          532..609
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     CDS             1..838
                     /gene="Csf3r"
                     /coded_by="NM_001436713.1:259..2775"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:298518"
                     /db_xref="RGD:1309114"
ORIGIN      
        1 mvglgacnlt gvtlivlllp rslegcgqir isppivhlgd pvlasctisp ncskldrqpk
       61 ilwrlqdepn qpgdrqhhlp dgsqesiitl phlnytqafl fclvpwnnsf qvldqaelra
      121 gyppaspsnl sclmylttns lvcqwepgpe thlptsfilk sfrsrtgcqy qggtildcmp
      181 kkrhsncsip rkhlllyqnm viwvqaenml gssespklci dpmdvvklep pmlqaldigh
      241 divsrqpgcl wlswkpwkps efmeqecelr yqpqleganw tlvshlpsst drfelcslhq
      301 apvytlqlrc irsslpglws swspglqlrp tikaptirld twwqkkhldp etvrmqlfwk
      361 ptplqkdsgq iqgyllswsc pdgqgrimhl cnttelsctf hlpseaqnvt lvaynsagts
      421 sptlvvfleh egpavtslha maqdlgsiwv dweapsllpq gyliewgpds hkysnnswri
      481 epngnttgil lednihpfql yritvaplyp gtvgppvnvy tysgekalph apelylkhvg
      541 rtwaqlewvp etpwlgmipl tnytifwtda rdhsfsvtln isfhdfvldh lkpaslyhvy
      601 lmatsragst nstgltlmtm aldssdvnif lgilcfvlls itcatawfcc kqsrktffwp
      661 nvpdpahssl sawvptimte etfqlpsfwg ssvpsitkit eleedkkpth wdpsessgtg
      721 slpavvqayv lqgdpreisn qfqppsstnd qvlygqvlgs ptspevvgyl rcdstqpllg
      781 gptpspksye niwfhsrpqe tfipqppsqe ddcvfgppfd fplfqglqvh gveeqggf
//
LOCUS       NP_001423607             342 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein 268 [Rattus norvegicus].
ACCESSION   NP_001423607 XP_017448742
VERSION     NP_001423607.1
DBSOURCE    REFSEQ: accession NM_001436678.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_017448742.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1400923.1,
                                           SRR26643298.27566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..342
                     /product="transmembrane protein 268"
                     /note="transmembrane protein C9orf91 homolog"
                     /calculated_mol_wt=37799
     Region          39..328
                     /region_name="DUF4481"
                     /note="Domain of unknown function (DUF4481); pfam14800"
                     /db_xref="CDD:464322"
     CDS             1..342
                     /gene="Tmem268"
                     /gene_synonym="RGD1304595"
                     /coded_by="NM_001436678.1:1212..2240"
                     /db_xref="GeneID:298104"
                     /db_xref="RGD:1304595"
ORIGIN      
        1 maceppsdpg gaagplptst lgcstlpqgn ppgwgeelhn gqvlsvlrid ntcapisfdl
       61 rvaeeqlqaw giqvpaeqyr slaesallep qvrryiiyns rpmrlafavv fyvlvwaniy
      121 stsqmfalgn qwagvllatl aavsltltlv lvferqqrka ntntdlrlva angallrhrv
      181 llgvtdtveg cqsviqlwfv yfdlencvqf lsdhvqemkr sqesllrsrl sqlcvvmetg
      241 vspvverped ledspllprt pgpqerpltq telyqlvpea epeemarqll avfggyytrl
      301 lvtsqlpqpm gtrhmdsari pcpcqlievh ilgtgccpfl ar
//
LOCUS       NP_001423602             648 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423602
VERSION     NP_001423602.1
DBSOURCE    REFSEQ: accession NM_001436673.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.53183.1,
                                           SRR26643287.32186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..648
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 3"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=71082
     Region          <1..154
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Region          562..607
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     CDS             1..648
                     /gene="Bap1"
                     /coded_by="NM_001436673.1:461..2407"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mffahqlipn scathallsv llncsnvdlg ptlsrmkdft kgfspeskgy aignapelak
       61 ahnsharpep rhlpekqngl savrtmeafh fvsyvpitgr lfeldglkvy pidhgpwged
      121 eewtdkarrv imeriglata gepyhdirfn lmavvpdrrv kyearlhvlk gnrqtvleal
      181 qqlirvtqpe liqthksqes qlpeeskpas skspfgleag rtpaasecth tdgaeevags
      241 cpqttthspp sksklvvkps gsslngvppt ptpivqrlpa fldnhnyaks pmqeeedlaa
      301 gvgrsrvpvr pqqysddeed yedeeedvqn tssairykrk gtgkpgslsn ssdgqlsvlq
      361 pntinvltek lqesqkdlsi plsiktssga gspavavpth sqpsptpsne stdtaseigs
      421 afnsplrspi rsanptrpss pvtshiskvl fgeddsllrv dcirynravr dlgpvistgl
      481 lhlaedgvls plalteggkg sspstrssqg sqgsssleek evvevtdsrd ksglnrssep
      541 lsgekyspke llallkcvea eianyeaclk eevekrkkfk iddqrrthny defictfism
      601 laqegmlanl veqnisvrrr qgvsigrlhk qrkpdrrkrs rpykakrq
//
LOCUS       NP_001100131             342 aa            linear   ROD 19-MAR-2025
DEFINITION  transmembrane protein 268 [Rattus norvegicus].
ACCESSION   NP_001100131 XP_001064554 XP_233020
VERSION     NP_001100131.1
DBSOURCE    REFSEQ: accession NM_001106661.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_233020.4, XP_001064554.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360176.2258420.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..342
                     /product="transmembrane protein 268"
                     /note="transmembrane protein C9orf91 homolog"
                     /calculated_mol_wt=37799
     Region          39..328
                     /region_name="DUF4481"
                     /note="Domain of unknown function (DUF4481); pfam14800"
                     /db_xref="CDD:464322"
     CDS             1..342
                     /gene="Tmem268"
                     /gene_synonym="RGD1304595"
                     /coded_by="NM_001106661.2:373..1401"
                     /db_xref="GeneID:298104"
                     /db_xref="RGD:1304595"
ORIGIN      
        1 maceppsdpg gaagplptst lgcstlpqgn ppgwgeelhn gqvlsvlrid ntcapisfdl
       61 rvaeeqlqaw giqvpaeqyr slaesallep qvrryiiyns rpmrlafavv fyvlvwaniy
      121 stsqmfalgn qwagvllatl aavsltltlv lvferqqrka ntntdlrlva angallrhrv
      181 llgvtdtveg cqsviqlwfv yfdlencvqf lsdhvqemkr sqesllrsrl sqlcvvmetg
      241 vspvverped ledspllprt pgpqerpltq telyqlvpea epeemarqll avfggyytrl
      301 lvtsqlpqpm gtrhmdsari pcpcqlievh ilgtgccpfl ar
//
LOCUS       NP_001423627             743 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform b [Rattus norvegicus].
ACCESSION   NP_001423627
VERSION     NP_001423627.1
DBSOURCE    REFSEQ: accession NM_001436698.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 743)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 743)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 743)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 743)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 743)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 743)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 743)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 743)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29401.1,
                                           SRR26360181.1055426.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..743
                     /product="nuclear autoantigenic sperm protein isoform b"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=80867
     Region          <97..473
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          466..489
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          495..571
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          497..534
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          497..525
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(498,501..502,505..506,508,540,543..544,547..548,
                     550..551,572,575..576,579)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          530..568
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..743
                     /gene="Nasp"
                     /coded_by="NM_001436698.1:261..2492"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 mesldvdsea kkllglgqkh lvmgdipaav nafqeaasll gkkygetane cgeafffygk
       61 sllelarmen gvlgnalegv hveeeegekt edeslvennd nvdeeareel reqvydamge
      121 keakkaegqs ltkpetdkeq esevekggre dmdisepaek lqekvestsk qltesseeak
      181 eaaipglned evtsgkteqe slcteegksi sgvyvqnkef reavpqeege emislekkpk
      241 etsedqtiga pekqdtlmkv veieaeidse vksvdvggee pkdqgaises elgkavlmql
      301 sgqdvevspv vaaeagsevs ekpgqeitvl pnngpvvgqs sagdqtpsep qnsaerlset
      361 kdgasveevk aelvpeqeea mppveeseaa gdgvetkvaq ratekapedk fkiaaneetq
      421 erdeqmkege etegseeedk endkaeettn esvlekktlq eneeeeignl elawdmldla
      481 kiifkrqetk eaqlyaaqah lklgevsves enyiqaveef qaclslqeqy leahdrllae
      541 thyqlglayg ynsqydeava qfgksidvie krmavlleqm keaegsftey ekeieelkel
      601 lpeirekied akesqrsgnv aelalkatlv esstsgftps gagasvsmia srkptdgass
      661 sncvtdishl vrkkrkpeee sprkddakka kpepevnggs gdavssgnev senmeaeaen
      721 qaesqttaeg tvdsaatvks tac
//
LOCUS       NP_001013957             289 aa            linear   ROD 19-MAR-2025
DEFINITION  mitochondrial fission regulator 1-like isoform a [Rattus
            norvegicus].
ACCESSION   NP_001013957 XP_216546
VERSION     NP_001013957.1
DBSOURCE    REFSEQ: accession NM_001013935.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216546.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083692.1, SRR26643299.24796.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..289
                     /product="mitochondrial fission regulator 1-like isoform
                     a"
                     /note="protein FAM54B; family with sequence similarity 54,
                     member B"
                     /calculated_mol_wt=31599
     Region          7..250
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     CDS             1..289
                     /gene="Mtfr1l"
                     /gene_synonym="Fam54b; RGD1305453"
                     /coded_by="NM_001013935.2:139..1008"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:298549"
                     /db_xref="RGD:1305453"
ORIGIN      
        1 meanvtipiw qnkphgaars vvrrigtnlp lkpcprasfe tlpnisdlcl kdvppvptla
       61 diawiaadee etyarvrsdt rplrhtwkps plivmqrnas vpnlrgseer llalkkpalp
      121 alsrttelqd elshlrsqia kivaadaasa sltpdflssg ssnvssplpc fgssfhstts
      181 fvisditeet evevpelpti pllcsaspec cksehkttcs sseeddcisl skassfadmm
      241 gilkdfhrik qsqdlsrsll keedpavlis evlrrkfalk eedisrkgn
//
LOCUS       NP_001423638             627 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423638 XP_038965541
VERSION     NP_001423638.1
DBSOURCE    REFSEQ: accession NM_001436709.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_038965541.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.22368.1,
                                           SRR26643295.22559.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..627
                     /product="polyadenylate-binding protein 4 isoform 6"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=69255
     Region          11..611
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..627
                     /gene="Pabpc4"
                     /coded_by="NM_001436709.1:885..2768"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgn apasrglptt
      481 aqrvgvptav pnlapratva aaapravapy kyasnvrsph paiqplqapq pavhvqgqep
      541 ltasmlaaap pqeqkqmlge rlfpliqtmh snlagkitgm lleidnsell hmlespeslr
      601 skvdeavavl qahhakkeaa qkeskak
//
LOCUS       NP_001423619             229 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001423619 XP_063131426
VERSION     NP_001423619.1
DBSOURCE    REFSEQ: accession NM_001436690.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063131426.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32233.1,
                                           SRR26360186.2361760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..229
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 3"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=25694
     Region          68..226
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..229
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436690.1:253..942"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkknildlvh efpekiacsf hvtkqttqis selkpyvtdg
      181 ritekeireh isaetlfyvc gpppmtdffs khlesshvpk ehicfekww
//
LOCUS       NP_001423618             250 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001423618 XP_063131425
VERSION     NP_001423618.1
DBSOURCE    REFSEQ: accession NM_001436689.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063131425.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2476715.1,
                                           SRR26643290.47348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..250
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 2"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=28204
     Region          8..247
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(35,47..50,67..69,73..76,117)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(47,49..50)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(73,76,79,86)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99778"
     Site            order(112,116..119,121)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99778"
     Site            order(117..118,153..155,222..223)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..250
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436689.1:635..1387"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
       61 eriielavky tnhppavwvh nkctldseva lrvggefffd pqptdaprnl vliaggvgin
      121 pllsilrhsa dlhrdhkekr rgydigtikl fysakntsel lfkknildlv hefpekiacs
      181 fhvtkqttqi sselkpyvtd gritekeire hisaetlfyv cgpppmtdff skhlesshvp
      241 kehicfekww
//
LOCUS       NP_001100155             838 aa            linear   ROD 19-MAR-2025
DEFINITION  granulocyte colony-stimulating factor receptor isoform a precursor
            [Rattus norvegicus].
ACCESSION   NP_001100155 XP_001057564 XP_233514
VERSION     NP_001100155.1
DBSOURCE    REFSEQ: accession NM_001106685.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Zhang,E., Lee,S., Yi,M.H., Nan,Y., Xu,Y., Shin,N., Ko,Y., Lee,Y.H.,
            Lee,W. and Kim,D.W.
  TITLE     Expression of granulocyte colony-stimulating factor 3 receptor in
            the spinal dorsal horn following spinal nerve ligation-induced
            neuropathic pain
  JOURNAL   Mol Med Rep 16 (2), 2009-2015 (2017)
   PUBMED   28656207
  REMARK    GeneRIF: the expression of GCSFR in neurons following peripheral
            nerve injury may be involved in the induction and maintenance of
            neuropathic pain through the STAT3 and TRPV1 signaling pathway.
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Aref,S., El-Ghonemy,M., Abouzeid,T., El-Sabbagh,A. and El-Baiomy,M.
  TITLE     Prevalence and impact of colony stimulating factor 3 receptor
            (CSF3R) mutations among Egyptian acute myeloid leukemia patients
  JOURNAL   Leuk Res 38 (6), 722-725 (2014)
   PUBMED   24746896
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Fleischman,A.G., Maxson,J.E., Luty,S.B., Agarwal,A., Royer,L.R.,
            Abel,M.L., MacManiman,J.D., Loriaux,M.M., Druker,B.J. and
            Tyner,J.W.
  TITLE     The CSF3R T618I mutation causes a lethal neutrophilic neoplasia in
            mice that is responsive to therapeutic JAK inhibition
  JOURNAL   Blood 122 (22), 3628-3631 (2013)
   PUBMED   24081659
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Kosmider,O., Itzykson,R., Chesnais,V., Lasho,T., Laborde,R.,
            Knudson,R., Gauthier,A., Merlevede,J., Ades,L., Morabito,M.,
            Fontenay,M., Tefferi,A., Droin,N. and Solary,E.
  TITLE     Mutation of the colony-stimulating factor-3 receptor gene is a rare
            event with poor prognosis in chronic myelomonocytic leukemia
  JOURNAL   Leukemia 27 (9), 1946-1949 (2013)
   PUBMED   23774674
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Hanumanthu,V.S. and Pirruccello,S.J.
  TITLE     GCSF-R expression in myelodysplastic and myeloproliferative
            disorders and blast dysmaturation in CML
  JOURNAL   Am J Clin Pathol 140 (2), 155-164 (2013)
   PUBMED   23897249
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Semerad,C.L., Poursine-Laurent,J., Liu,F. and Link,D.C.
  TITLE     A role for G-CSF receptor signaling in the regulation of
            hematopoietic cell function but not lineage commitment or
            differentiation
  JOURNAL   Immunity 11 (2), 153-161 (1999)
   PUBMED   10485650
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Otsuji,W., Tanase,S., Yoshida,S. and Bawden,J.W.
  TITLE     The immunohistochemical localization of the interferon-gamma and
            granulocyte colony-stimulating factor receptors during early
            amelogenesis in rat molars
  JOURNAL   Arch Oral Biol 44 (2), 173-181 (1999)
   PUBMED   10206335
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Hermans,M.H., Ward,A.C., Antonissen,C., Karis,A., Lowenberg,B. and
            Touw,I.P.
  TITLE     Perturbed granulopoiesis in mice with a targeted mutation in the
            granulocyte colony-stimulating factor receptor gene associated with
            severe chronic neutropenia
  JOURNAL   Blood 92 (1), 32-39 (1998)
   PUBMED   9639496
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Dong,F., Dale,D.C., Bonilla,M.A., Freedman,M., Fasth,A.,
            Neijens,H.J., Palmblad,J., Briars,G.L., Carlsson,G., Veerman,A.J.,
            Welte,K., Lowenberg,B. and Touw,I.P.
  TITLE     Mutations in the granulocyte colony-stimulating factor receptor
            gene in patients with severe congenital neutropenia
  JOURNAL   Leukemia 11 (1), 120-125 (1997)
   PUBMED   9001427
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Fukunaga,R., Ishizaka-Ikeda,E., Seto,Y. and Nagata,S.
  TITLE     Expression cloning of a receptor for murine granulocyte
            colony-stimulating factor
  JOURNAL   Cell 61 (2), 341-350 (1990)
   PUBMED   2158861
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057564.1, XP_233514.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680412,
                              SAMN06680413 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..838
                     /product="granulocyte colony-stimulating factor receptor
                     isoform a precursor"
                     /note="granulocyte colony-stimulating factor receptor;
                     colony stimulating factor 3 receptor (granulocyte)"
                     /calculated_mol_wt=91301
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2540
     Region          24..111
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Region          123..221
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          433..521
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(513..514,516..517)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(529,593,608)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          532..609
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     CDS             1..838
                     /gene="Csf3r"
                     /coded_by="NM_001106685.2:178..2694"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:298518"
                     /db_xref="RGD:1309114"
ORIGIN      
        1 mvglgacnlt gvtlivlllp rslegcgqir isppivhlgd pvlasctisp ncskldrqpk
       61 ilwrlqdepn qpgdrqhhlp dgsqesiitl phlnytqafl fclvpwnnsf qvldqaelra
      121 gyppaspsnl sclmylttns lvcqwepgpe thlptsfilk sfrsrtgcqy qggtildcmp
      181 kkrhsncsip rkhlllyqnm viwvqaenml gssespklci dpmdvvklep pmlqaldigh
      241 divsrqpgcl wlswkpwkps efmeqecelr yqpqleganw tlvshlpsst drfelcslhq
      301 apvytlqlrc irsslpglws swspglqlrp tikaptirld twwqkkhldp etvrmqlfwk
      361 ptplqkdsgq iqgyllswsc pdgqgrimhl cnttelsctf hlpseaqnvt lvaynsagts
      421 sptlvvfleh egpavtslha maqdlgsiwv dweapsllpq gyliewgpds hkysnnswri
      481 epngnttgil lednihpfql yritvaplyp gtvgppvnvy tysgekalph apelylkhvg
      541 rtwaqlewvp etpwlgmipl tnytifwtda rdhsfsvtln isfhdfvldh lkpaslyhvy
      601 lmatsragst nstgltlmtm aldssdvnif lgilcfvlls itcatawfcc kqsrktffwp
      661 nvpdpahssl sawvptimte etfqlpsfwg ssvpsitkit eleedkkpth wdpsessgtg
      721 slpavvqayv lqgdpreisn qfqppsstnd qvlygqvlgs ptspevvgyl rcdstqpllg
      781 gptpspksye niwfhsrpqe tfipqppsqe ddcvfgppfd fplfqglqvh gveeqggf
//
LOCUS       NP_001423589             277 aa            linear   ROD 19-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423589
VERSION     NP_001423589.1
DBSOURCE    REFSEQ: accession NM_001436660.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.681793.1,
                                           SRR26360181.1553161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..277
                     /product="spermatogenesis-associated protein 4 isoform 2"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=31392
     Region          54..144
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     CDS             1..277
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001436660.1:9..842"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 maaagraees lplpaaessk ttlptppavp aarkpkkclv yphpprssrl cpsvlrwlqg
       61 ldlsffprnv trdfsngylv aeifciyypw dlrlssfeng tslkvkldnw aqiekflakk
      121 kfklpkelih gtihckagvp eiliqeiytl lthqeirsiq ddfanftdys yqmrlplvpr
      181 stvsksiknn irlsellsnp nilsnelkie flfllqmlqr klsrklnpak sgndvqphre
      241 ihvkqngkpc datakpminv eetmkdteev alkksch
//
LOCUS       NP_001423637             640 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423637 XP_063143503
VERSION     NP_001423637.1
DBSOURCE    REFSEQ: accession NM_001436708.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143503.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20697.1,
                                           SRR26643290.20304.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..640
                     /product="polyadenylate-binding protein 4 isoform 5"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=70489
     Region          11..624
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..640
                     /gene="Pabpc4"
                     /coded_by="NM_001436708.1:885..2807"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgs ecpdrlamdf
      481 ggagaaqqgl tdscqsggvp tavpnlapra tvaaaaprav apykyasnvr sphpaiqplq
      541 apqpavhvqg qepltasmla aappqeqkqm lgerlfpliq tmhsnlagki tgmlleidns
      601 ellhmlespe slrskvdeav avlqahhakk eaaqkeskak
//
LOCUS       NP_001423640             611 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001423640 XP_063143504
VERSION     NP_001423640.1
DBSOURCE    REFSEQ: accession NM_001436711.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143504.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20003.1,
                                           SRR26643296.15990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..611
                     /product="polyadenylate-binding protein 4 isoform 8"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=67677
     Region          11..595
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..611
                     /gene="Pabpc4"
                     /coded_by="NM_001436711.1:885..2720"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgv ptavpnlapr
      481 atvaaaapra vapykyasnv rsphpaiqpl qapqpavhvq gqepltasml aaappqeqkq
      541 mlgerlfpli qtmhsnlagk itgmlleidn sellhmlesp eslrskvdea vavlqahhak
      601 keaaqkeska k
//
LOCUS       NP_001423603             648 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423603
VERSION     NP_001423603.1
DBSOURCE    REFSEQ: accession NM_001436674.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2805240.1,
                                           SRR26360181.2926274.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..648
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 3"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=71082
     Region          <1..154
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Region          562..607
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     CDS             1..648
                     /gene="Bap1"
                     /coded_by="NM_001436674.1:370..2316"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mffahqlipn scathallsv llncsnvdlg ptlsrmkdft kgfspeskgy aignapelak
       61 ahnsharpep rhlpekqngl savrtmeafh fvsyvpitgr lfeldglkvy pidhgpwged
      121 eewtdkarrv imeriglata gepyhdirfn lmavvpdrrv kyearlhvlk gnrqtvleal
      181 qqlirvtqpe liqthksqes qlpeeskpas skspfgleag rtpaasecth tdgaeevags
      241 cpqttthspp sksklvvkps gsslngvppt ptpivqrlpa fldnhnyaks pmqeeedlaa
      301 gvgrsrvpvr pqqysddeed yedeeedvqn tssairykrk gtgkpgslsn ssdgqlsvlq
      361 pntinvltek lqesqkdlsi plsiktssga gspavavpth sqpsptpsne stdtaseigs
      421 afnsplrspi rsanptrpss pvtshiskvl fgeddsllrv dcirynravr dlgpvistgl
      481 lhlaedgvls plalteggkg sspstrssqg sqgsssleek evvevtdsrd ksglnrssep
      541 lsgekyspke llallkcvea eianyeaclk eevekrkkfk iddqrrthny defictfism
      601 laqegmlanl veqnisvrrr qgvsigrlhk qrkpdrrkrs rpykakrq
//
LOCUS       NP_001423628             449 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform c [Rattus norvegicus].
ACCESSION   NP_001423628 XP_006238709
VERSION     NP_001423628.1
DBSOURCE    REFSEQ: accession NM_001436699.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238709.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1085866.1,
                                           SRR26360194.182772.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..449
                     /product="nuclear autoantigenic sperm protein isoform c"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=48645
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          172..195
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..277
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          203..240
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          203..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(204,207..208,211..212,214,246,249..250,253..254,
                     256..257,278,281..282,285)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          236..274
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..449
                     /gene="Nasp"
                     /coded_by="NM_001436699.1:106..1455"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 matestataa iaaelvsadk vedapapsts adkmesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnvdeteg seeedkendk aeettnesvl ekktlqenee eeignlelaw
      181 dmldlakiif krqetkeaql yaaqahlklg evsvesenyi qaveefqacl slqeqyleah
      241 drllaethyq lglaygynsq ydeavaqfgk sidviekrma vlleqmkeae gsfteyekei
      301 eelkellpei rekiedakes qrsgnvaela lkatlvesst sgftpsgaga svsmiasrkp
      361 tdgasssncv tdishlvrkk rkpeeesprk ddakkakpep evnggsgdav ssgnevsenm
      421 eaeaenqaes qttaegtvds aatvkstac
//
LOCUS       NP_001002852             323 aa            linear   ROD 19-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001002852 XP_224832
VERSION     NP_001002852.1
DBSOURCE    REFSEQ: accession NM_001002852.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Aug 30, 2004 this sequence version replaced XP_224832.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY653229.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..323
                     /product="spermatogenesis-associated protein 4 isoform 6"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=36512
     Region          54..144
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     CDS             1..323
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001002852.2:9..980"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 maaagraees lplpaaessk ttlptppavp aarkpkkclv yphpprssrl cpsvlrwlqg
       61 ldlsffprnv trdfsngylv aeifciyypw dlrlssfeng tslkvkldnw aqiekflakk
      121 kfklpkelih gtihckagvp eiliqeiytl lthqeirsiq ddfanftdys yqmrlplvpr
      181 stvsksiknn irlsellsnp nilsnelkie flfllqmlqr klsrklnpgk pslekgwfdi
      241 kptvgeitvg hlpahsykhk ykskvskera vsslsksgnd vqphreihvk qngkpcdata
      301 kpminveetm kdteevalkk sch
//
LOCUS       NP_001423646             289 aa            linear   ROD 19-MAR-2025
DEFINITION  mitochondrial fission regulator 1-like isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423646
VERSION     NP_001423646.1
DBSOURCE    REFSEQ: accession NM_001436717.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.30775.1,
                                           SRR26643295.23150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..289
                     /product="mitochondrial fission regulator 1-like isoform
                     a"
                     /note="protein FAM54B; family with sequence similarity 54,
                     member B"
                     /calculated_mol_wt=31599
     Region          7..250
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     CDS             1..289
                     /gene="Mtfr1l"
                     /gene_synonym="Fam54b; RGD1305453"
                     /coded_by="NM_001436717.1:271..1140"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:298549"
                     /db_xref="RGD:1305453"
ORIGIN      
        1 meanvtipiw qnkphgaars vvrrigtnlp lkpcprasfe tlpnisdlcl kdvppvptla
       61 diawiaadee etyarvrsdt rplrhtwkps plivmqrnas vpnlrgseer llalkkpalp
      121 alsrttelqd elshlrsqia kivaadaasa sltpdflssg ssnvssplpc fgssfhstts
      181 fvisditeet evevpelpti pllcsaspec cksehkttcs sseeddcisl skassfadmm
      241 gilkdfhrik qsqdlsrsll keedpavlis evlrrkfalk eedisrkgn
//
LOCUS       NP_001423631            1421 aa            linear   ROD 19-MAR-2025
DEFINITION  DNA excision repair protein ERCC-6 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423631 XP_006252799
VERSION     NP_001423631.1
DBSOURCE    REFSEQ: accession NM_001436702.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1421)
  AUTHORS   Xu,Y., Wu,Z., Liu,L., Liu,J. and Wang,Y.
  TITLE     Rat Model of Cockayne Syndrome Neurological Disease
  JOURNAL   Cell Rep 29 (4), 800-809 (2019)
   PUBMED   31644904
  REMARK    GeneRIF: Rat Model of Cockayne Syndrome Neurological Disease.
REFERENCE   2  (residues 1 to 1421)
  AUTHORS   Yang,Z., Liu,C., Wu,H., Xie,Y., Gao,H. and Zhang,X.
  TITLE     CSB affected on the sensitivity of lung cancer cells to
            platinum-based drugs through the global decrease of let-7 and
            miR-29
  JOURNAL   BMC Cancer 19 (1), 948 (2019)
   PUBMED   31615563
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1421)
  AUTHORS   West,H., Coffey,M., Wagner,M.J., McLeod,H.L., Colley,J.P.,
            Adams,R.A., Fleck,O., Maughan,T.S., Fisher,D., Kaplan,R.S.,
            Harris,R. and Cheadle,J.P.
  TITLE     Role for Nucleotide Excision Repair Gene Variants in
            Oxaliplatin-Induced Peripheral Neuropathy
  JOURNAL   JCO Precis Oncol 2, 1-18 (2018)
   PUBMED   35135151
REFERENCE   4  (residues 1 to 1421)
  AUTHORS   Luo,S.S., Liao,X.W. and Zhu,X.D.
  TITLE     Prognostic Value of Excision Repair Cross-Complementing mRNA
            Expression in Gastric Cancer
  JOURNAL   Biomed Res Int 2018, 6204684 (2018)
   PUBMED   30417012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1421)
  AUTHORS   Pascucci,B., Fragale,A., Marabitti,V., Leuzzi,G., Calcagnile,A.S.,
            Parlanti,E., Franchitto,A., Dogliotti,E. and D'Errico,M.
  TITLE     CSA and CSB play a role in the response to DNA breaks
  JOURNAL   Oncotarget 9 (14), 11581-11591 (2018)
   PUBMED   29545921
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1421)
  AUTHORS   Dianov,G., Bischoff,C., Sunesen,M. and Bohr,V.A.
  TITLE     Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome
            group B cells
  JOURNAL   Nucleic Acids Res 27 (5), 1365-1368 (1999)
   PUBMED   9973627
REFERENCE   7  (residues 1 to 1421)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Cockayne syndrome group B protein enhances elongation by RNA
            polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (21), 11205-11209 (1997)
   PUBMED   9326587
REFERENCE   8  (residues 1 to 1421)
  AUTHORS   van der Horst,G.T., van Steeg,H., Berg,R.J., van Gool,A.J., de
            Wit,J., Weeda,G., Morreau,H., Beems,R.B., van Kreijl,C.F., de
            Gruijl,F.R., Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Defective transcription-coupled repair in Cockayne syndrome B mice
            is associated with skin cancer predisposition
  JOURNAL   Cell 89 (3), 425-435 (1997)
   PUBMED   9150142
REFERENCE   9  (residues 1 to 1421)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Human transcription-repair coupling factor CSB/ERCC6 is a
            DNA-stimulated ATPase but is not a helicase and does not disrupt
            the ternary transcription complex of stalled RNA polymerase II
  JOURNAL   J Biol Chem 272 (3), 1885-1890 (1997)
   PUBMED   8999876
REFERENCE   10 (residues 1 to 1421)
  AUTHORS   Henning,K.A., Li,L., Iyer,N., McDaniel,L.D., Reagan,M.S.,
            Legerski,R., Schultz,R.A., Stefanini,M., Lehmann,A.R., Mayne,L.V.
            and Friedberg,E.C.
  TITLE     The Cockayne syndrome group A gene encodes a WD repeat protein that
            interacts with CSB protein and a subunit of RNA polymerase II TFIIH
  JOURNAL   Cell 82 (4), 555-564 (1995)
   PUBMED   7664335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252799.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1421
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..1421
                     /product="DNA excision repair protein ERCC-6 isoform 2"
                     /note="DNA excision repair protein ERCC-6; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 6; excision repair
                     cross-complementation group 6"
                     /calculated_mol_wt=158727
     Region          83..159
                     /region_name="cc_ERCC-6_N"
                     /note="coiled-coil domain located near the N-terminus of
                     human Excision Repair Cross Complementing 6 (ERCC-6) and
                     related proteins; cd21397"
                     /db_xref="CDD:411064"
     Site            order(114,118)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:411064"
     Region          <503..928
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          1349..1420
                     /region_name="CSB_WHD"
                     /note="winged-helix domain (WHD) found in cockayne
                     syndrome group B (CSB) and similar proteins; cd22254"
                     /db_xref="CDD:439329"
     Site            order(1349..1350,1353..1354,1356..1357,1360,1364..1365,
                     1370..1371,1400,1418..1420)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439329"
     CDS             1..1421
                     /gene="Ercc6"
                     /coded_by="NM_001436702.1:72..4337"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:306274"
                     /db_xref="RGD:1311509"
ORIGIN      
        1 mpheeipnst qpqgqdwlpg qhvsadrdip agqetagdse agkclsspsc dhgpstsaea
       61 cvlaatrwgp allhidrhqi pavepsaqal elqglgvdvy dqavleegvl qqvdsamhea
      121 srvaqradae keyqsvlddl mscttslrqi nkiieqlspq aasnrdinrk ldsvkrqkyn
      181 keqqlkkita kqkrlqailg gaevhveldh gsleeedaep gpsclgsmlm paqesaweel
      241 irtgqmtpfg tpapqkqekk prkimlneas gfekyladqa qlsfkrkkqa ankrtakkav
      301 vvsessrgpn etkpnqrsqa lsqtdkrlkk hirklqrral qfqgkvglqr gkrplepeer
      361 pgaegdtege esgssptdge eeeeqeeegv avlssddisy elkplrkgqk yekkvpvqei
      421 dddffpssee edeavegrgg grkvsrrpdd gdedyykqrl rrwnrlrlqd keklkledds
      481 eesdaefdeg fkvpgflfkk lfkfeglgpt livcpttvmh qwvkefhtww ppfrvailhe
      541 tgscahrker lvrdivhchg vlitsysyir lmqddisrhd whyvildegh kirnpnaavt
      601 lackqfrtph riilsgspmq nnlrelwslf dftfpgklgt lpvfmeqfsv pitmggysna
      661 spvqvktayk cacvlrdtin pyllrrmksd vkmslslpdk neqvlfcrlt deqhkvyqnf
      721 idskavyril ngenqifsgl valrkicnhp dlfsggpknt salpedglee eqfgywkrsg
      781 kmivvesllk iwhkqgqrvl lfsqsrqmlh ilevflrahk ysylkmdgtt tiasrqplit
      841 kynedtsifv fllttrvggl gvnltganrv iiydpdwnps tdtqareraw rigqkkqvtv
      901 yrlltagtie ekiyhrqifk qfltnrvlkd pkqrrffksn dlyelftlts pdasqgtets
      961 aifagtgsni qtlkchfkkr tppvlqmdpk rkkplvsdts vngatvmeek sqgsgatgsv
     1021 pstesgplks drhtdgsras svgfgeeada gstlehlsgl sgdspavdht srlsavasts
     1081 ekqgssyege ccqaqtgpvh lseqteghfs khkskrkhda aeeettekcp qpkqkaknsr
     1141 hhrdakfegt rvphlvkkrr yhqqtteqes gakdrssddy vleklfkksv gvhsvvkhda
     1201 iidgsspdyv lveaeanrva qdalkalrls rqqclgatsg vptwtghrgi sgapagvkkr
     1261 fgqkrnsslp vqrpsslter tqnmkkegea htaehfsgke dgasssgaps sssllarmra
     1321 rnhmilperl esdgeqlaga aaaaappcst ehdallvdmr nfiafqaqvd gqastqeilq
     1381 afesklsvaq scvfrellrn lcnfhrtpgg egiwklkpey c
//
LOCUS       NP_001423623             154 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 6
            [Rattus norvegicus].
ACCESSION   NP_001423623
VERSION     NP_001423623.1
DBSOURCE    REFSEQ: accession NM_001436694.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1290851.1,
                                           SRR26360181.1259564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..154
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 6"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=16731
     Region          68..>141
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
     Site            order(95,107..110,127..129,133..136)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..154
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436694.1:267..731"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkvaensclc gnfv
//
LOCUS       NP_001423635             660 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423635 XP_006238860
VERSION     NP_001423635.1
DBSOURCE    REFSEQ: accession NM_001436706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238860.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.1490392.1,
                                           SRR26360181.1768040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..660
                     /product="polyadenylate-binding protein 4 isoform 3"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=72281
     Region          11..640
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..660
                     /gene="Pabpc4"
                     /coded_by="NM_001436706.1:885..2867"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgn apasrglptt
      481 aqrvgsecpd rlamdfggag aaqqgltdsc qsggvptavp nlapratvaa aapravapyk
      541 yasnvrsphp aiqplqapqp avhvqgqepl tasmlaaapp qeqkqmlger lfpliqtmhs
      601 nlagkitgml leidnsellh mlespeslrs kvdeavavlq ahhakkeaaq kvgtvaaats
//
LOCUS       NP_001423605             648 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423605
VERSION     NP_001423605.1
DBSOURCE    REFSEQ: accession NM_001436676.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.55582.1,
                                           SRR26643298.70514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN13663631
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..648
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 3"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=71082
     Region          <1..154
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Region          562..607
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     CDS             1..648
                     /gene="Bap1"
                     /coded_by="NM_001436676.1:264..2210"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mffahqlipn scathallsv llncsnvdlg ptlsrmkdft kgfspeskgy aignapelak
       61 ahnsharpep rhlpekqngl savrtmeafh fvsyvpitgr lfeldglkvy pidhgpwged
      121 eewtdkarrv imeriglata gepyhdirfn lmavvpdrrv kyearlhvlk gnrqtvleal
      181 qqlirvtqpe liqthksqes qlpeeskpas skspfgleag rtpaasecth tdgaeevags
      241 cpqttthspp sksklvvkps gsslngvppt ptpivqrlpa fldnhnyaks pmqeeedlaa
      301 gvgrsrvpvr pqqysddeed yedeeedvqn tssairykrk gtgkpgslsn ssdgqlsvlq
      361 pntinvltek lqesqkdlsi plsiktssga gspavavpth sqpsptpsne stdtaseigs
      421 afnsplrspi rsanptrpss pvtshiskvl fgeddsllrv dcirynravr dlgpvistgl
      481 lhlaedgvls plalteggkg sspstrssqg sqgsssleek evvevtdsrd ksglnrssep
      541 lsgekyspke llallkcvea eianyeaclk eevekrkkfk iddqrrthny defictfism
      601 laqegmlanl veqnisvrrr qgvsigrlhk qrkpdrrkrs rpykakrq
//
LOCUS       NP_001423636             656 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423636 XP_006238861
VERSION     NP_001423636.1
DBSOURCE    REFSEQ: accession NM_001436707.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238861.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.7639.1,
                                           SRR26643298.28796.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..656
                     /product="polyadenylate-binding protein 4 isoform 4"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=72067
     Region          11..640
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..656
                     /gene="Pabpc4"
                     /coded_by="NM_001436707.1:885..2855"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgn apasrglptt
      481 aqrvgsecpd rlamdfggag aaqqgltdsc qsggvptavp nlapratvaa aapravapyk
      541 yasnvrsphp aiqplqapqp avhvqgqepl tasmlaaapp qeqkqmlger lfpliqtmhs
      601 nlagkitgml leidnsellh mlespeslrs kvdeavavlq ahhakkeaaq keskak
//
LOCUS       NP_001423616             310 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423616 XP_006252688
VERSION     NP_001423616.1
DBSOURCE    REFSEQ: accession NM_001436687.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252688.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.41040.1,
                                           SRR26643429.49847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..310
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 1"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=34716
     Region          68..307
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136,177)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(133,136,139,146)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99778"
     Site            order(172,176..179,181)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99778"
     Site            order(177..178,213..215,282..283)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..310
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436687.1:253..1185"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkctldseva lrvggefffd pqptdaprnl vliaggvgin
      181 pllsilrhsa dlhrdhkekr rgydigtikl fysakntsel lfkknildlv hefpekiacs
      241 fhvtkqttqi sselkpyvtd gritekeire hisaetlfyv cgpppmtdff skhlesshvp
      301 kehicfekww
//
LOCUS       NP_001423591             236 aa            linear   ROD 19-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423591 XP_038950433
VERSION     NP_001423591.1
DBSOURCE    REFSEQ: accession NM_001436662.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_038950433.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74643.1,
                                           SRR26360181.1684153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..236
                     /product="spermatogenesis-associated protein 4 isoform 4"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=26526
     CDS             1..236
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001436662.1:119..829"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 msgvstspee lppvsfrpal aagpgsqllp eecyqflakk kfklpkelih gtihckagvp
       61 eiliqeiytl lthqeirsiq ddfanftdys yqmrlplvpr stvsksiknn irlsellsnp
      121 nilsnelkie flfllqmlqr klsrklnpgw fdikptvgei tvghlpahsy khkykskvsk
      181 eravsslsks gndvqphrei hvkqngkpcd atakpminve etmkdteeva lkksch
//
LOCUS       NP_001423615             310 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423615 XP_006252687
VERSION     NP_001423615.1
DBSOURCE    REFSEQ: accession NM_001436686.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252687.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32232.1,
                                           SRR26643295.52009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..310
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 1"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=34716
     Region          68..307
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136,177)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(133,136,139,146)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99778"
     Site            order(172,176..179,181)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99778"
     Site            order(177..178,213..215,282..283)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..310
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436686.1:360..1292"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkctldseva lrvggefffd pqptdaprnl vliaggvgin
      181 pllsilrhsa dlhrdhkekr rgydigtikl fysakntsel lfkknildlv hefpekiacs
      241 fhvtkqttqi sselkpyvtd gritekeire hisaetlfyv cgpppmtdff skhlesshvp
      301 kehicfekww
//
LOCUS       NP_001423630            1474 aa            linear   ROD 19-MAR-2025
DEFINITION  DNA excision repair protein ERCC-6 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423630 XP_006252798
VERSION     NP_001423630.1
DBSOURCE    REFSEQ: accession NM_001436701.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1474)
  AUTHORS   Xu,Y., Wu,Z., Liu,L., Liu,J. and Wang,Y.
  TITLE     Rat Model of Cockayne Syndrome Neurological Disease
  JOURNAL   Cell Rep 29 (4), 800-809 (2019)
   PUBMED   31644904
  REMARK    GeneRIF: Rat Model of Cockayne Syndrome Neurological Disease.
REFERENCE   2  (residues 1 to 1474)
  AUTHORS   Yang,Z., Liu,C., Wu,H., Xie,Y., Gao,H. and Zhang,X.
  TITLE     CSB affected on the sensitivity of lung cancer cells to
            platinum-based drugs through the global decrease of let-7 and
            miR-29
  JOURNAL   BMC Cancer 19 (1), 948 (2019)
   PUBMED   31615563
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1474)
  AUTHORS   West,H., Coffey,M., Wagner,M.J., McLeod,H.L., Colley,J.P.,
            Adams,R.A., Fleck,O., Maughan,T.S., Fisher,D., Kaplan,R.S.,
            Harris,R. and Cheadle,J.P.
  TITLE     Role for Nucleotide Excision Repair Gene Variants in
            Oxaliplatin-Induced Peripheral Neuropathy
  JOURNAL   JCO Precis Oncol 2, 1-18 (2018)
   PUBMED   35135151
REFERENCE   4  (residues 1 to 1474)
  AUTHORS   Luo,S.S., Liao,X.W. and Zhu,X.D.
  TITLE     Prognostic Value of Excision Repair Cross-Complementing mRNA
            Expression in Gastric Cancer
  JOURNAL   Biomed Res Int 2018, 6204684 (2018)
   PUBMED   30417012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1474)
  AUTHORS   Pascucci,B., Fragale,A., Marabitti,V., Leuzzi,G., Calcagnile,A.S.,
            Parlanti,E., Franchitto,A., Dogliotti,E. and D'Errico,M.
  TITLE     CSA and CSB play a role in the response to DNA breaks
  JOURNAL   Oncotarget 9 (14), 11581-11591 (2018)
   PUBMED   29545921
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1474)
  AUTHORS   Dianov,G., Bischoff,C., Sunesen,M. and Bohr,V.A.
  TITLE     Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome
            group B cells
  JOURNAL   Nucleic Acids Res 27 (5), 1365-1368 (1999)
   PUBMED   9973627
REFERENCE   7  (residues 1 to 1474)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Cockayne syndrome group B protein enhances elongation by RNA
            polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (21), 11205-11209 (1997)
   PUBMED   9326587
REFERENCE   8  (residues 1 to 1474)
  AUTHORS   van der Horst,G.T., van Steeg,H., Berg,R.J., van Gool,A.J., de
            Wit,J., Weeda,G., Morreau,H., Beems,R.B., van Kreijl,C.F., de
            Gruijl,F.R., Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Defective transcription-coupled repair in Cockayne syndrome B mice
            is associated with skin cancer predisposition
  JOURNAL   Cell 89 (3), 425-435 (1997)
   PUBMED   9150142
REFERENCE   9  (residues 1 to 1474)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Human transcription-repair coupling factor CSB/ERCC6 is a
            DNA-stimulated ATPase but is not a helicase and does not disrupt
            the ternary transcription complex of stalled RNA polymerase II
  JOURNAL   J Biol Chem 272 (3), 1885-1890 (1997)
   PUBMED   8999876
REFERENCE   10 (residues 1 to 1474)
  AUTHORS   Henning,K.A., Li,L., Iyer,N., McDaniel,L.D., Reagan,M.S.,
            Legerski,R., Schultz,R.A., Stefanini,M., Lehmann,A.R., Mayne,L.V.
            and Friedberg,E.C.
  TITLE     The Cockayne syndrome group A gene encodes a WD repeat protein that
            interacts with CSB protein and a subunit of RNA polymerase II TFIIH
  JOURNAL   Cell 82 (4), 555-564 (1995)
   PUBMED   7664335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252798.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.70603.1,
                                           SRR26360186.2898797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1474
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..1474
                     /product="DNA excision repair protein ERCC-6 isoform 1"
                     /note="DNA excision repair protein ERCC-6; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 6; excision repair
                     cross-complementation group 6"
                     /calculated_mol_wt=164694
     Region          83..159
                     /region_name="cc_ERCC-6_N"
                     /note="coiled-coil domain located near the N-terminus of
                     human Excision Repair Cross Complementing 6 (ERCC-6) and
                     related proteins; cd21397"
                     /db_xref="CDD:411064"
     Site            order(114,118)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:411064"
     Region          316..981
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          1402..1473
                     /region_name="CSB_WHD"
                     /note="winged-helix domain (WHD) found in cockayne
                     syndrome group B (CSB) and similar proteins; cd22254"
                     /db_xref="CDD:439329"
     Site            order(1402..1403,1406..1407,1409..1410,1413,1417..1418,
                     1423..1424,1453,1471..1473)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439329"
     CDS             1..1474
                     /gene="Ercc6"
                     /coded_by="NM_001436701.1:88..4512"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:306274"
                     /db_xref="RGD:1311509"
ORIGIN      
        1 mpheeipnst qpqgqdwlpg qhvsadrdip agqetagdse agkclsspsc dhgpstsaea
       61 cvlaatrwgp allhidrhqi pavepsaqal elqglgvdvy dqavleegvl qqvdsamhea
      121 srvaqradae keyqsvlddl mscttslrqi nkiieqlspq aasnrdinrk ldsvkrqkyn
      181 keqqlkkita kqkrlqailg gaevhveldh gsleeedaep gpsclgsmlm paqesaweel
      241 irtgqmtpfg tpapqkqekk prkimlneas gfekyladqa qlsfkrkkqa ankrtakkav
      301 vvsessrgpn etkpnqrsqa lsqtdkrlkk hirklqrral qfqgkvglqr gkrplepeer
      361 pgaegdtege esgssptdge eeeeqeeegv avlssddisy elkplrkgqk yekkvpvqei
      421 dddffpssee edeavegrgg grkvsrrpdd gdedyykqrl rrwnrlrlqd keklkledds
      481 eesdaefdeg fkvpgflfkk lfkyqqtgvr wlwelhcqqa ggilgdemgl gktiqiiafl
      541 aglsyskirt rgsnyrfegl gptlivcptt vmhqwvkefh twwppfrvai lhetgscahr
      601 kerlvrdivh chgvlitsys yirlmqddis rhdwhyvild eghkirnpna avtlackqfr
      661 tphriilsgs pmqnnlrelw slfdftfpgk lgtlpvfmeq fsvpitmggy snaspvqvkt
      721 aykcacvlrd tinpyllrrm ksdvkmslsl pdkneqvlfc rltdeqhkvy qnfidskavy
      781 rilngenqif sglvalrkic nhpdlfsggp kntsalpedg leeeqfgywk rsgkmivves
      841 llkiwhkqgq rvllfsqsrq mlhilevflr ahkysylkmd gtttiasrqp litkynedts
      901 ifvfllttrv gglgvnltga nrviiydpdw npstdtqare rawrigqkkq vtvyrlltag
      961 tieekiyhrq ifkqfltnrv lkdpkqrrff ksndlyelft ltspdasqgt etsaifagtg
     1021 sniqtlkchf kkrtppvlqm dpkrkkplvs dtsvngatvm eeksqgsgat gsvpstesgp
     1081 lksdrhtdgs rassvgfgee adagstlehl sglsgdspav dhtsrlsava stsekqgssy
     1141 egeccqaqtg pvhlseqteg hfskhkskrk hdaaeeette kcpqpkqkak nsrhhrdakf
     1201 egtrvphlvk krryhqqtte qesgakdrss ddyvleklfk ksvgvhsvvk hdaiidgssp
     1261 dyvlveaean rvaqdalkal rlsrqqclga tsgvptwtgh rgisgapagv kkrfgqkrns
     1321 slpvqrpssl tertqnmkke geahtaehfs gkedgasssg apssssllar mrarnhmilp
     1381 erlesdgeql agaaaaaapp cstehdallv dmrnfiafqa qvdgqastqe ilqafeskls
     1441 vaqscvfrel lrnlcnfhrt pggegiwklk peyc
//
LOCUS       NP_001423601             696 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423601 XP_006252669
VERSION     NP_001423601.1
DBSOURCE    REFSEQ: accession NM_001436672.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 696)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252669.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.47295.1,
                                           SRR26643429.49782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..696
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 2"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=76558
     Region          5..233
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Site            order(85,91,169,184)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(85,91,169,184)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Region          <628..655
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     CDS             1..696
                     /gene="Bap1"
                     /coded_by="NM_001436672.1:129..2219"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mnkgwleles dpglftllve dfgvkgvqve eiydlqskcq gpvygfiflf kwieerrsrr
       61 kvstlvddts vidddivnsm ffahqlipns cathallsvl lncsnvdlgp tlsrmkdftk
      121 gfspeskgya ignapelaka hnsharpepr hlpekqngls avrtmeafhf vsyvpitgrl
      181 feldglkvyp idhgpwgede ewtdkarrvi meriglatag epyhdirfnl mavvpdrrvk
      241 yearlhvlkg nrqtvlealq qlirvtqpel iqthksqesq lpeeskpass kspfgleagr
      301 tpaasectht dgaeevagsc pqttthspps ksklvvkpsg sslngvpptp tpivqrlpaf
      361 ldnhnyaksp mqeeedlaag vgrsrvpvrp qqysddeedy edeeedvqnt ssairykrkg
      421 tgkpgslsns sdgqlsvlqp ntinvltekl qesqkdlsip lsiktssgag spavavpths
      481 qpsptpsnes tdtaseigsa fnsplrspir sanptrpssp vtshiskvlf geddsllrvd
      541 cirynravrd lgpvistgll hlaedgvlsp lalteggkgs spstrssqgs qgsssleeke
      601 vvevtdsrdk sglnrssepl sgekyspkid dqrrthnyde fictfismla qegmlanlve
      661 qnisvrrrqg vsigrlhkqr kpdrrkrsrp ykakrq
//
LOCUS       NP_001094008             644 aa            linear   ROD 19-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001094008 XP_001054606 XP_216517
VERSION     NP_001094008.1
DBSOURCE    REFSEQ: accession NM_001100538.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 10, 2008 this sequence version replaced
            XP_001054606.1, XP_216517.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166452.1, SRR26360186.1552365.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..644
                     /product="polyadenylate-binding protein 4 isoform 2"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=70703
     Region          11..624
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..644
                     /gene="Pabpc4"
                     /coded_by="NM_001100538.2:885..2819"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgs ecpdrlamdf
      481 ggagaaqqgl tdscqsggvp tavpnlapra tvaaaaprav apykyasnvr sphpaiqplq
      541 apqpavhvqg qepltasmla aappqeqkqm lgerlfpliq tmhsnlagki tgmlleidns
      601 ellhmlespe slrskvdeav avlqahhakk eaaqkvgtva aats
//
LOCUS       NP_001100762             740 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001100762 XP_001058224 XP_224614
VERSION     NP_001100762.1
DBSOURCE    REFSEQ: accession NM_001107292.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001058224.1, XP_224614.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.37704.1,
                                           SRR26643299.58128.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..740
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 4"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=81604
     Region          5..246
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Region          69..73
                     /region_name="Arg-finger motif.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            order(98,104,182,197)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(98,104,182,197)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Site            98
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01393; propagated
                     from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            197
                     /site_type="other"
                     /note="Important for enzyme activity.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01393; propagated
                     from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          286..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          376..379
                     /region_name="HBM-like motif.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          385..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          475..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          586..635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          607..732
                     /region_name="Interaction with BRCA1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          653..697
                     /region_name="Interaction with YY1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          654..699
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     Region          710..733
                     /region_name="Classical bipartite Nuclear localization
                     signal (NLS). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          710..712
                     /region_name="Interaction with nucleosomal DNA forming a
                     DNA clamp with ASXL1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          715..740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          724..740
                     /region_name="Positively charged C-terminal extension
                     (CTE). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          728..735
                     /region_name="Non-classical PY-nuclear localization signal
                     (PY-NLS). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          728..733
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     CDS             1..740
                     /gene="Bap1"
                     /coded_by="NM_001107292.2:129..2351"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mnkgwleles dpglftllve dfgknpftpd rralagvkgv qveeiydlqs kcqgpvygfi
       61 flfkwieerr srrkvstlvd dtsvidddiv nsmffahqli pnscathall svllncsnvd
      121 lgptlsrmkd ftkgfspesk gyaignapel akahnsharp eprhlpekqn glsavrtmea
      181 fhfvsyvpit grlfeldglk vypidhgpwg edeewtdkar rvimerigla tagepyhdir
      241 fnlmavvpdr rvkyearlhv lkgnrqtvle alqqlirvtq peliqthksq esqlpeeskp
      301 asskspfgle agrtpaasec thtdgaeeva gscpqttths ppsksklvvk psgsslngvp
      361 ptptpivqrl pafldnhnya kspmqeeedl aagvgrsrvp vrpqqysdde edyedeeedv
      421 qntssairyk rkgtgkpgsl snssdgqlsv lqpntinvlt eklqesqkdl siplsiktss
      481 gagspavavp thsqpsptps nestdtasei gsafnsplrs pirsanptrp sspvtshisk
      541 vlfgeddsll rvdcirynra vrdlgpvist gllhlaedgv lsplaltegg kgsspstrss
      601 qgsqgsssle ekevvevtds rdksglnrss eplsgekysp kellallkcv eaeianyeac
      661 lkeevekrkk fkiddqrrth nydefictfi smlaqegmla nlveqnisvr rrqgvsigrl
      721 hkqrkpdrrk rsrpykakrq
//
LOCUS       NP_001423604             648 aa            linear   ROD 19-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423604
VERSION     NP_001423604.1
DBSOURCE    REFSEQ: accession NM_001436675.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.35012.1,
                                           SRR26360172.634980.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..648
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 3"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=71082
     Region          <1..154
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(6,12,90,105)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Region          562..607
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     CDS             1..648
                     /gene="Bap1"
                     /coded_by="NM_001436675.1:294..2240"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mffahqlipn scathallsv llncsnvdlg ptlsrmkdft kgfspeskgy aignapelak
       61 ahnsharpep rhlpekqngl savrtmeafh fvsyvpitgr lfeldglkvy pidhgpwged
      121 eewtdkarrv imeriglata gepyhdirfn lmavvpdrrv kyearlhvlk gnrqtvleal
      181 qqlirvtqpe liqthksqes qlpeeskpas skspfgleag rtpaasecth tdgaeevags
      241 cpqttthspp sksklvvkps gsslngvppt ptpivqrlpa fldnhnyaks pmqeeedlaa
      301 gvgrsrvpvr pqqysddeed yedeeedvqn tssairykrk gtgkpgslsn ssdgqlsvlq
      361 pntinvltek lqesqkdlsi plsiktssga gspavavpth sqpsptpsne stdtaseigs
      421 afnsplrspi rsanptrpss pvtshiskvl fgeddsllrv dcirynravr dlgpvistgl
      481 lhlaedgvls plalteggkg sspstrssqg sqgsssleek evvevtdsrd ksglnrssep
      541 lsgekyspke llallkcvea eianyeaclk eevekrkkfk iddqrrthny defictfism
      601 laqegmlanl veqnisvrrr qgvsigrlhk qrkpdrrkrs rpykakrq
//
LOCUS       NP_001423620             229 aa            linear   ROD 19-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001423620
VERSION     NP_001423620.1
DBSOURCE    REFSEQ: accession NM_001436691.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.47354.1,
                                           SRR26643299.58188.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..229
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 3"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=25694
     Region          68..226
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..229
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436691.1:267..956"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkknildlvh efpekiacsf hvtkqttqis selkpyvtdg
      181 ritekeireh isaetlfyvc gpppmtdffs khlesshvpk ehicfekww
//
LOCUS       NP_001423520             532 aa            linear   ROD 19-MAR-2025
DEFINITION  nuclear factor 1 A-type isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423520 XP_063143251
VERSION     NP_001423520.1
DBSOURCE    REFSEQ: accession NM_001436591.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Ding,B., Wang,W., Selvakumar,T., Xi,H.S., Zhu,H., Chow,C.W.,
            Horton,J.D., Gronostajski,R.M. and Kilpatrick,D.L.
  TITLE     Temporal regulation of nuclear factor one occupancy by
            calcineurin/NFAT governs a voltage-sensitive developmental switch
            in late maturing neurons
  JOURNAL   J Neurosci 33 (7), 2860-2872 (2013)
   PUBMED   23407945
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Riffel,A.K., Schuenemann,E. and Vyhlidal,C.A.
  TITLE     Regulation of the CYP3A4 and CYP3A7 promoters by members of the
            nuclear factor I transcription factor family
  JOURNAL   Mol Pharmacol 76 (5), 1104-1114 (2009)
   PUBMED   19706729
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Royland,J.E. and Kodavanti,P.R.
  TITLE     Gene expression profiles following exposure to a developmental
            neurotoxicant, Aroclor 1254: pathway analysis for possible mode(s)
            of action
  JOURNAL   Toxicol Appl Pharmacol 231 (2), 179-196 (2008)
   PUBMED   18602130
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Lu,W., Quintero-Rivera,F., Fan,Y., Alkuraya,F.S., Donovan,D.J.,
            Xi,Q., Turbe-Doan,A., Li,Q.G., Campbell,C.G., Shanske,A.L.,
            Sherr,E.H., Ahmad,A., Peters,R., Rilliet,B., Parvex,P.,
            Bassuk,A.G., Harris,D.J., Ferguson,H., Kelly,C., Walsh,C.A.,
            Gronostajski,R.M., Devriendt,K., Higgins,A., Ligon,A.H.,
            Quade,B.J., Morton,C.C., Gusella,J.F. and Maas,R.L.
  TITLE     NFIA haploinsufficiency is associated with a CNS malformation
            syndrome and urinary tract defects
  JOURNAL   PLoS Genet 3 (5), e80 (2007)
   PUBMED   17530927
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Lin,Y.L., Wang,Y.H. and Lee,H.J.
  TITLE     Transcriptional regulation of the human TR2 orphan receptor gene by
            nuclear factor 1-A
  JOURNAL   Biochem Biophys Res Commun 350 (2), 430-436 (2006)
   PUBMED   17010934
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Chaudhry,A.Z., Lyons,G.E. and Gronostajski,R.M.
  TITLE     Expression patterns of the four nuclear factor I genes during mouse
            embryogenesis indicate a potential role in development
  JOURNAL   Dev Dyn 208 (3), 313-325 (1997)
   PUBMED   9056636
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Osada,S., Daimon,S., Ikeda,T., Nishihara,T., Yano,K., Yamasaki,M.
            and Imagawa,M.
  TITLE     Nuclear factor 1 family proteins bind to the silencer element in
            the rat glutathione transferase P gene
  JOURNAL   J Biochem 121 (2), 355-363 (1997)
   PUBMED   9089412
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Monaci,P., Nuzzo,M., Stampfli,S., Tollervey,D., De Simone,V. and
            Nicosia,A.
  TITLE     A complex interplay of positive and negative elements is
            responsible for the different transcriptional activity of liver NF1
            variants
  JOURNAL   Mol Biol Rep 21 (3), 147-158 (1995)
   PUBMED   8832903
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Ang,S.L., Wierda,A., Wong,D., Stevens,K.A., Cascio,S., Rossant,J.
            and Zaret,K.S.
  TITLE     The formation and maintenance of the definitive endoderm lineage in
            the mouse: involvement of HNF3/forkhead proteins
  JOURNAL   Development 119 (4), 1301-1315 (1993)
   PUBMED   8306889
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Paonessa,G., Gounari,F., Frank,R. and Cortese,R.
  TITLE     Purification of a NF1-like DNA-binding protein from rat liver and
            cloning of the corresponding cDNA
  JOURNAL   EMBO J 7 (10), 3115-3123 (1988)
   PUBMED   3053160
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 17, 2025 this sequence version replaced XP_063143251.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF112455.1, SRR26360194.1672187.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..532
                     /product="nuclear factor 1 A-type isoform 1"
                     /note="nuclear factor 1 A-type; CTF; NF1-A; NFI-A; NF-I/A;
                     nuclear factor 1/A; TGGCA-binding protein;
                     CCAAT-box-binding transcription factor"
                     /calculated_mol_wt=58440
     Region          33..69
                     /region_name="NfI_DNAbd_pre-N"
                     /note="Nuclear factor I protein pre-N-terminus; pfam10524"
                     /db_xref="CDD:463134"
     Region          91..195
                     /region_name="MH1"
                     /note="MH1 domain; pfam03165"
                     /db_xref="CDD:460833"
     Region          237..524
                     /region_name="CTF_NFI"
                     /note="CTF/NF-I family transcription modulation region;
                     pfam00859"
                     /db_xref="CDD:459967"
     CDS             1..532
                     /gene="Nfia"
                     /coded_by="NM_001436591.1:35..1633"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25492"
                     /db_xref="RGD:3170"
ORIGIN      
        1 mkladsvmag kasdgsikwq lcydisartw wmdefhpfie allphvrafa ytwfnlqark
       61 rkyfkkhekr mskeeeravk dellsekpev kqkwasrlla klrkdirpey redfvltvtg
      121 kkppccvlsn pdqkgkmrri dclrqadkvw rldlvmvilf kgiplestdg erlvkspqcs
      181 npglcvqphh igvsvkeldl ylayfvhaad ssqsespsqp sdadikdqpe nghlgfqdsf
      241 vtsgvfsvte lvrvsqtpia agtgpnfsls dlesssyysm spgamrrslp stsstsstkr
      301 lksvedemds pgeepfytgq grspgsgsqs sgwhevepgm pspttlkkse ksgfsspsps
      361 qtsslgtaft qhhrpvitgp rasphatpst lhfptspiiq qpgpyfshpa iryhpqetlk
      421 efvqlvcpda gqqagqvgfl npngssqgkv hnpflptpml pppppppmar pvplpmpdtk
      481 ppttstegga asptsptyst pstspanrfv svgprdpsfv nipqqtqswy lg
//
LOCUS       NP_001423505             410 aa            linear   ROD 19-MAR-2025
DEFINITION  transcription factor Dp-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423505 XP_038950604
VERSION     NP_001423505.1
DBSOURCE    REFSEQ: accession NM_001436576.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Okuda,M., Araki,K., Ohtani,K. and Nishimura,Y.
  TITLE     The Interaction Mode of the Acidic Region of the Cell Cycle
            Transcription Factor DP1 with TFIIH
  JOURNAL   J Mol Biol 428 (24 Pt B), 4993-5006 (2016)
   PUBMED   27825926
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Gong,W., Gohla,R.M., Bowlin,K.M., Koyano-Nakagawa,N., Garry,D.J.
            and Shi,X.
  TITLE     Kelch Repeat and BTB Domain Containing Protein 5 (Kbtbd5) Regulates
            Skeletal Muscle Myogenesis through the E2F1-DP1 Complex
  JOURNAL   J Biol Chem 290 (24), 15350-15361 (2015)
   PUBMED   25940086
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Zaragoza,K., Begay,V., Schuetz,A., Heinemann,U. and Leutz,A.
  TITLE     Repression of transcriptional activity of C/EBPalpha by
            E2F-dimerization partner complexes
  JOURNAL   Mol Cell Biol 30 (9), 2293-2304 (2010)
   PUBMED   20176812
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Qiao,H., Di Stefano,L., Tian,C., Li,Y.Y., Yin,Y.H., Qian,X.P.,
            Pang,X.W., Li,Y., McNutt,M.A., Helin,K., Zhang,Y. and Chen,W.F.
  TITLE     Human TFDP3, a novel DP protein, inhibits DNA binding and
            transactivation by E2F
  JOURNAL   J Biol Chem 282 (1), 454-466 (2007)
   PUBMED   17062573
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Illenye,S. and Heintz,N.H.
  TITLE     Functional analysis of bacterial artificial chromosomes in
            mammalian cells: mouse Cdc6 is associated with the mitotic spindle
            apparatus
  JOURNAL   Genomics 83 (1), 66-75 (2004)
   PUBMED   14667810
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Hsu,S.I., Yang,C.M., Sim,K.G., Hentschel,D.M., O'Leary,E. and
            Bonventre,J.V.
  TITLE     TRIP-Br: a novel family of PHD zinc finger- and
            bromodomain-interacting proteins that regulate the transcriptional
            activity of E2F-1/DP-1
  JOURNAL   EMBO J 20 (9), 2273-2285 (2001)
   PUBMED   11331592
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Timchenko,N.A., Wilde,M. and Darlington,G.J.
  TITLE     C/EBPalpha regulates formation of S-phase-specific E2F-p107
            complexes in livers of newborn mice
  JOURNAL   Mol Cell Biol 19 (4), 2936-2945 (1999)
   PUBMED   10082561
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Wu,C.L., Zukerberg,L.R., Ngwu,C., Harlow,E. and Lees,J.A.
  TITLE     In vivo association of E2F and DP family proteins
  JOURNAL   Mol Cell Biol 15 (5), 2536-2546 (1995)
   PUBMED   7739537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_038950604.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.47643.1,
                                           SRR26643291.38606.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..410
                     /product="transcription factor Dp-1 isoform 1"
                     /calculated_mol_wt=45057
     Region          112..193
                     /region_name="E2F_TDP"
                     /note="E2F/DP family winged-helix DNA-binding domain;
                     pfam02319"
                     /db_xref="CDD:460530"
     Site            order(198,202,205..206,208..209,212..213,215..216,
                     219..220,223,226..227,230,233..234,236..237,239..241,244,
                     255..266,268,279..287,289,291,293,299..300,302)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271217"
     Region          198..244
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:271217"
     Region          200..338
                     /region_name="DP"
                     /note="Transcription factor DP; pfam08781"
                     /db_xref="CDD:462601"
     Site            order(222,225..226,229,262,271,273,288..295,302)
                     /site_type="other"
                     /note="RbC binding site [polypeptide binding]"
                     /db_xref="CDD:271217"
     CDS             1..410
                     /gene="Tfdp1"
                     /coded_by="NM_001436576.1:181..1413"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361178"
                     /db_xref="RGD:1560344"
ORIGIN      
        1 makdasliea ngelkvfidq nlspgkgvvs lvavhpstvn tlgkqllpkt fgqsnvnitq
       61 qvvigtpqrp aaantivvgs phtpnthfvs qnqtsdsspw sagkrnrkge kngkglrhfs
      121 mkvcekvqrk gttsynevad elvaefsaad nhilpnesay dqknirrrvy dalnvlmamn
      181 iiskekkeik wiglptnsaq ecqnleverq rrlerikqkq sqlqelilqq iafknlvqrn
      241 rqaeqqarrp pppnsvihlp fiivntsrkt vidcsisndk feylfnfdnt feihddievl
      301 krmgmacgle sgscsaedlk varslvpkal epyvtemaqg siggvfvttt gstsngtrls
      361 asdlsngadg mlatssngsq ysgsrvetpv syvgeddddd ddfnendeed
//
LOCUS       NP_001423497             332 aa            linear   ROD 19-MAR-2025
DEFINITION  glutamate-rich protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423497 XP_006253457
VERSION     NP_001423497.1
DBSOURCE    REFSEQ: accession NM_001436568.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253457.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ227386.1, BC167071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..332
                     /product="glutamate-rich protein 1 isoform 1"
                     /note="glutamate-rich protein 1"
                     /calculated_mol_wt=36953
     Region          <211..>315
                     /region_name="Cnd3"
                     /note="Nuclear condensing complex subunits, C-term domain;
                     pfam12719"
                     /db_xref="CDD:463678"
     CDS             1..332
                     /gene="Erich1"
                     /gene_synonym="RGD1559872"
                     /coded_by="NM_001436568.1:57..1055"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306622"
                     /db_xref="RGD:1559872"
ORIGIN      
        1 msslrkqvft ekvlkrlfpn vssgqekgtp qtpaldtpsk dstpeavqqk pvrgltagdi
       61 kiqperrlyt vslpppgyip clpeptscad senassggdt edpglpdqpk rrrirrhksk
      121 ksikslggvt vrqteletqr ekthpphpda pamsrnkkrk wraklrlrrk reaglaaras
      181 aasftyepes seeaevegdv ggeeeedpes svadpaqedt elassradsl lsflkstqei
      241 yfydeasred pavsteaaee llrllesgrl ppadvlildh mktllllqdt erltsalkmf
      301 pehcmmppdh ariisaffny witqilpekr se
//
LOCUS       NP_001423512             365 aa            linear   ROD 19-MAR-2025
DEFINITION  ATP-dependent (S)-NAD(P)H-hydrate dehydratase isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423512 XP_006253527
VERSION     NP_001423512.1
DBSOURCE    REFSEQ: accession NM_001436583.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Van Bergen,N.J., Guo,Y., Rankin,J., Paczia,N., Becker-Kettern,J.,
            Kremer,L.S., Pyle,A., Conrotte,J.F., Ellaway,C., Procopis,P.,
            Prelog,K., Homfray,T., Baptista,J., Baple,E., Wakeling,M.,
            Massey,S., Kay,D.P., Shukla,A., Girisha,K.M., Lewis,L.E.S.,
            Santra,S., Power,R., Daubeney,P., Montoya,J., Ruiz-Pesini,E.,
            Kovacs-Nagy,R., Pritsch,M., Ahting,U., Thorburn,D.R., Prokisch,H.,
            Taylor,R.W., Christodoulou,J., Linster,C.L., Ellard,S. and
            Hakonarson,H.
  TITLE     NAD(P)HX dehydratase (NAXD) deficiency: a novel neurodegenerative
            disorder exacerbated by febrile illnesses
  JOURNAL   Brain 142 (1), 50-58 (2019)
   PUBMED   30576410
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Marbaix,A.Y., Tyteca,D., Niehaus,T.D., Hanson,A.D., Linster,C.L.
            and Van Schaftingen,E.
  TITLE     Occurrence and subcellular distribution of the NADPHX repair system
            in mammals
  JOURNAL   Biochem J 460 (1), 49-58 (2014)
   PUBMED   24611804
  REMARK    GeneRIF: The human, mouse, and rat Carkd genes contain a first exon
            with two alternative 3' splice sites and two putative initiator ATG
            codons; the second exon also comprises a highly conserved ATG
            codon.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253527.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.633681.1,
                                           SRR26643293.76037.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..365
                     /product="ATP-dependent (S)-NAD(P)H-hydrate dehydratase
                     isoform 1"
                     /EC_number="4.2.1.93"
                     /note="carbohydrate kinase domain containing;
                     ATP-dependent NAD(P)HX dehydratase; carbohydrate kinase
                     domain-containing protein; ATP-dependent
                     (S)-NAD(P)H-hydrate dehydratase"
                     /calculated_mol_wt=38600
     Region          87..354
                     /region_name="YXKO-related"
                     /note="B.subtilis YXKO protein of unknown function and
                     related proteins. Based on the conservation of the ATP
                     binding site, the substrate binding site and the
                     Mg2+binding site and structural homology this group is a
                     member of the ribokinase-like superfamily; cd01171"
                     /db_xref="CDD:238576"
     Site            order(109,290,293)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238576"
     Site            order(224,264,291..292,295,332)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:238576"
     CDS             1..365
                     /gene="Naxd"
                     /gene_synonym="Carkd; RGD1562691"
                     /coded_by="NM_001436583.1:20..1117"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361185"
                     /db_xref="RGD:1562691"
ORIGIN      
        1 mgircvaira cgggkidtgv prmavcpyga aavvmallsa aiafhcspll avlqralslh
       61 tahatkdmdn lfqlvrnivp altskkhkgq dgrigivggc qeytgapyfa gisalkvgad
      121 lthvfcarea apviksyspe livhpvldss daveevekwl prlhalvvgp glgrddllln
      181 nvrgilestk ardipvvida dglwliaqrp alvhgyqkav ltpnhvefsr lwdavlsspm
      241 dtsnhsgsvl klsqalgnit ivqkgeqdli sngqqvlvcn qegssrrcgg qgdllsgslg
      301 vmahwalrag pektngsspl lvaawgactl trecnhlafq kygrsttttd miaevgaafs
      361 klftt
//
LOCUS       NP_001423511             549 aa            linear   ROD 19-MAR-2025
DEFINITION  probable cysteine--tRNA ligase, mitochondrial isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423511 XP_006253524
VERSION     NP_001423511.1
DBSOURCE    REFSEQ: accession NM_001436582.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253524.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.59657.1,
                                           SRR26643298.72345.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..549
                     /product="probable cysteine--tRNA ligase, mitochondrial
                     isoform 2"
                     /EC_number="6.1.1.16"
                     /note="probable cysteine--tRNA ligase, mitochondrial"
                     /calculated_mol_wt=60715
     Region          23..546
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     CDS             1..549
                     /gene="Cars2"
                     /gene_synonym="RGD1311612"
                     /coded_by="NM_001436582.1:56..1705"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361184"
                     /db_xref="RGD:1311612"
ORIGIN      
        1 mlralrpgpg apllraalvl grrgrawqrp qgqdtgvqvh nsltgkkepl ivgrsdavsw
       61 yscgptvydh ahlghacsyv rfdiirrilt svfgcnvvma msitdvddki ikranemnvs
      121 paslaslfee efkqdmaalk vlpptvylrv tenipqiisf iqgiiahgha yatatgsvyf
      181 dlrargdkyg klvntvpsat aepvdsdkrh ssdfalwkga kpqevfwasp wgdgrpgwhi
      241 ecsamasevf gsqldihtgg idlafphhen eiaqsevfhq cqqwgnyflh sghlhvkgke
      301 ekmskslkny itikdflqtf spdvfrlfcl rtnyrsaidy sdstleearh lllglasfve
      361 darayvkgql icgpvgedvl werlastkka vkaalandfd tpravnsild lvhhanrqlr
      421 avskeaggpr sptvfgaiva yveqffetvg islakrqcvs gdsstvalhc vvdelvrfrl
      481 kvrqyalatp gatgearkqq lqerqpllea cdalrqdlmt hginvkdrgh aastwelldp
      541 rtkhqkpgt
//
LOCUS       NP_001423689             329 aa            linear   ROD 20-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform a
            [Rattus norvegicus].
ACCESSION   NP_001423689 XP_038965684
VERSION     NP_001423689.1
DBSOURCE    REFSEQ: accession NM_001436760.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_038965684.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.614409.1,
                                           SRR26360172.941679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMN06680429 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..329
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform a"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=37665
     Region          103..309
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..329
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001436760.1:598..1587"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaektknav
      301 qalidkhqri pgnirsalld rfhkeqkan
//
LOCUS       NP_001423678             551 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423678 XP_006252636
VERSION     NP_001423678.1
DBSOURCE    REFSEQ: accession NM_001436749.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006252636.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.37619.1,
                                           SRR26360186.1357613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..551
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     1"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=63041
     Region          152..328
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          342..474
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..551
                     /gene="Arhgef3"
                     /coded_by="NM_001436749.1:486..2141"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mnqciyrgme ehkerpkrpr qnnfsmfpsp kawnfrgrkr kqsaqdedav slcsldisep
       61 snkrvkplsr vtslanlipp vkttplkrfs qtlqrsisfr nesrpdilap rawsrnatss
      121 stkrrdsklw setfdvcvsq vltakeikrq eaifelsqge edliedlkla kkayhdpmlk
      181 lsimteqeln qifgtldsli plhedllsql rdvrkpdgst ehvgpilvgw lpclssydsy
      241 csnqvaakal ldhkkqdhrv qdflqrcles pfsrkldlwn fldiprsrlv kyplllreil
      301 rhtpndnpdq qhleeainii qgivaeintk tgesecryyk erllyleegq kdslidssrv
      361 lcchgelknn rgvklhvflf qevlvitrav thneqlcyql yrqpipvkdl tledlqdgev
      421 rlggslrgaf snneriknff rvsfkngsqs qthslqandt fnkqqwlnci rqaketvlsa
      481 agqaglldse slsqspgten relrgetkle qmdqsdsesd csmdtsevsl ecermeqtda
      541 scansrpeen v
//
LOCUS       NP_001101368             842 aa            linear   ROD 20-MAR-2025
DEFINITION  solute carrier organic anion transporter family member 5A1 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001101368 XP_001064830 XP_232599
VERSION     NP_001101368.1
DBSOURCE    REFSEQ: accession NM_001107898.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Kindla,J., Rau,T.T., Jung,R., Fasching,P.A., Strick,R., Stoehr,R.,
            Hartmann,A., Fromm,M.F. and Konig,J.
  TITLE     Expression and localization of the uptake transporters OATP2B1,
            OATP3A1 and OATP5A1 in non-malignant and malignant breast tissue
  JOURNAL   Cancer Biol Ther 11 (6), 584-591 (2011)
   PUBMED   21278488
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232599.3, XP_001064830.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760475,
                              SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..842
                     /product="solute carrier organic anion transporter family
                     member 5A1 isoform 2"
                     /calculated_mol_wt=91376
     Region          131..668
                     /region_name="MFS_SLCO5_OATP5"
                     /note="Solute carrier organic anion transporter 5 family
                     of the Major Facilitator Superfamily of transporters;
                     cd17404"
                     /db_xref="CDD:340962"
     Site            order(145..146,149..150,153,185,281..282,284..286,289,309,
                     312..313,316,442,445..446,449..451,454,483,487,528..529,
                     533,537,591,594..595,598..599,602)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340962"
     CDS             1..842
                     /gene="Slco5a1"
                     /coded_by="NM_001107898.2:660..3188"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:312907"
                     /db_xref="RGD:1307132"
ORIGIN      
        1 mdegaaqsra qeqleapslv gavqenfese sfrskslpvl hsascrqnls agnadgklal
       61 gsieasghqe thpgrnlivp spsapstsag tttelmdcnh rrdpsktvsv sstlatlqer
      121 rclyvvltds rcflvcmcfl tfiqalmvsg ylssvittie rryslksses gllvscfdig
      181 nlvvvvfvsy fggrgrrplw lavgglliai gaalfalphf isppyqiqel nasasndglc
      241 qngnstaile pppcpkdsgg nshwiyvalf vcaqvligmg stpiytlgpt ylddnvkkdn
      301 aslylaimyv mgalgpavgy llgglligfy vdprnpvlld qndprfignw wsgfllcaia
      361 mflvifpmft fpkklpprhk kkkkfsadvv sdddiikeks ntseqvnkkv ssmgfgknvr
      421 dlpraavril snmtflfvsl sytaesaivt afitfipkfi esqfgipasn asiytgviiv
      481 psagvgivlg gyiikklklg aresaklami csgvsllcfs tlfivgcesi nlgginipyt
      541 tgnltgscnv ncgckiheye pvcgsdgity fnpclagcin sgnlttgvrn ytectcvqsr
      601 qvitpptvgq rsqlrvvivk tylnengyav sgkckracnt lipflvflfi vtfitacaqp
      661 saiivtlrsv edeerpfalg mqfvllrtla yiptpiyfga vidttcmlwq qecgvqgscw
      721 eynvtsfrfv yfglaaglkf vgfififlaw ysikykedel qrrrcrdfpl stvsehvgrp
      781 skaekysrtt scpafstqge sheetalqkg fpgttltypg pfseaesssa drgldeslda
      841 al
//
LOCUS       NP_001423683             374 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423683
VERSION     NP_001423683.1
DBSOURCE    REFSEQ: accession NM_001436754.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.1987617.1,
                                           SRR26360186.366512.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..374
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     4"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=42567
     Region          7..151
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          165..297
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..374
                     /gene="Arhgef3"
                     /coded_by="NM_001436754.1:990..2114"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mlklsimteq elnqifgtld sliplhedll sqlrdvrkpd gstehvgpil vgwlpclssy
       61 dsycsnqvaa kalldhkkqd hrvqdflqrc lespfsrkld lwnfldiprs rlvkyplllr
      121 eilrhtpndn pdqqhleeai niiqgivaei ntktgesecr yykerllyle egqkdslids
      181 srvlcchgel knnrgvklhv flfqevlvit ravthneqlc yqlyrqpipv kdltledlqd
      241 gevrlggslr gafsnnerik nffrvsfkng sqsqthslqa ndtfnkqqwl ncirqaketv
      301 lsaagqagll dseslsqspg tenrelrget kleqmdqsds esdcsmdtse vslecermeq
      361 tdascansrp eenv
//
LOCUS       NP_001423653             700 aa            linear   ROD 20-MAR-2025
DEFINITION  rho GTPase-activating protein 22 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423653 XP_063131429
VERSION     NP_001423653.1
DBSOURCE    REFSEQ: accession NM_001436724.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Valnegri,P., Montrasio,C., Brambilla,D., Ko,J., Passafaro,M. and
            Sala,C.
  TITLE     The X-linked intellectual disability protein IL1RAPL1 regulates
            excitatory synapse formation by binding PTPdelta and RhoGAP2
  JOURNAL   Hum Mol Genet 20 (24), 4797-4809 (2011)
   PUBMED   21926414
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_063131429.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.46545.1,
                                           SRR26643299.58218.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..700
                     /product="rho GTPase-activating protein 22 isoform 2"
                     /note="rho GTPase-activating protein 22"
                     /calculated_mol_wt=76979
     Region          36..151
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          151..349
                     /region_name="RhoGAP_ARHGAP22_24_25"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP22, 24 and 25-like proteins; longer
                     isoforms of these proteins contain an additional
                     N-terminal pleckstrin homology (PH) domain. ARHGAP25
                     (KIA0053) has been identified as a GAP for...; cd04390"
                     /db_xref="CDD:239855"
     Site            order(195,232,236,307,310..311,335)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239855"
     Site            195
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239855"
     Region          <366..>681
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          <592..>682
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..700
                     /gene="Arhgap22"
                     /coded_by="NM_001436724.1:311..2413"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:306279"
                     /db_xref="RGD:1307237"
ORIGIN      
        1 mlspkirqar rarskslvmg eqsrspgrpl aphklgpvlk agwlrkqksi mknwqqrwfv
       61 lrgdqlfyyk dkdegkpqgf islqgtqvte llpdpddpgk hlfeitpgga aerekvpanp
      121 ealllmassq rdmedwvqai rrviwaplgg gifgqrledt vhherkfgpr lapllveqcv
      181 dfirerglse eglfrmpgqa nlvrdlqdsf dcgekplfds ttdvhtvasl lklylrelpe
      241 pvipfaryed flscaqlltk degegtvela kqvsnlpqan ynllryicrf ldevqahsdv
      301 nkmsvqnlat vfgpnilrpq vedpvtimeg tslvqhlmtv lirkhgqlfa tpsfeepasp
      361 rgtvqgtvew gseevtrdhq gepgssglpt hrtssldgpa aavlsrtspp rlgsqagpaa
      421 tspgkrmhtl pgwkssfrqq gsrsespkgv ssslevpiis sggnwlingl sslrshrras
      481 sgdrlkdtgs aqrlstydnv ppsshlssta svastawsva sssreasigs ctacrasnss
      541 acsslhtewa lepsplpsss eghpspdlgh sldeacvgsg ssepndpgsp sqahvrrcra
      601 lqgqvaelra elchqrieyq rslksieegn sdlrkqmcrl eeeldqekkk yamleiklrn
      661 seraredaer rnqllqreme effatlgslt agtkgarape
//
LOCUS       NP_001423679             551 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423679 XP_017455512
VERSION     NP_001423679.1
DBSOURCE    REFSEQ: accession NM_001436750.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_017455512.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.888507.1,
                                           SRR26643288.54894.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..551
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     1"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=63041
     Region          152..328
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          342..474
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..551
                     /gene="Arhgef3"
                     /coded_by="NM_001436750.1:104..1759"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mnqciyrgme ehkerpkrpr qnnfsmfpsp kawnfrgrkr kqsaqdedav slcsldisep
       61 snkrvkplsr vtslanlipp vkttplkrfs qtlqrsisfr nesrpdilap rawsrnatss
      121 stkrrdsklw setfdvcvsq vltakeikrq eaifelsqge edliedlkla kkayhdpmlk
      181 lsimteqeln qifgtldsli plhedllsql rdvrkpdgst ehvgpilvgw lpclssydsy
      241 csnqvaakal ldhkkqdhrv qdflqrcles pfsrkldlwn fldiprsrlv kyplllreil
      301 rhtpndnpdq qhleeainii qgivaeintk tgesecryyk erllyleegq kdslidssrv
      361 lcchgelknn rgvklhvflf qevlvitrav thneqlcyql yrqpipvkdl tledlqdgev
      421 rlggslrgaf snneriknff rvsfkngsqs qthslqandt fnkqqwlnci rqaketvlsa
      481 agqaglldse slsqspgten relrgetkle qmdqsdsesd csmdtsevsl ecermeqtda
      541 scansrpeen v
//
LOCUS       NP_001423680             531 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423680 XP_006252638
VERSION     NP_001423680.1
DBSOURCE    REFSEQ: accession NM_001436751.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006252638.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.57977.1,
                                           SRR26643287.32108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..531
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     2"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=60633
     Region          132..308
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          322..454
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..531
                     /gene="Arhgef3"
                     /coded_by="NM_001436751.1:94..1689"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mrserpmvwc cfflraqrkr kqsaqdedav slcsldisep snkrvkplsr vtslanlipp
       61 vkttplkrfs qtlqrsisfr nesrpdilap rawsrnatss stkrrdsklw setfdvcvsq
      121 vltakeikrq eaifelsqge edliedlkla kkayhdpmlk lsimteqeln qifgtldsli
      181 plhedllsql rdvrkpdgst ehvgpilvgw lpclssydsy csnqvaakal ldhkkqdhrv
      241 qdflqrcles pfsrkldlwn fldiprsrlv kyplllreil rhtpndnpdq qhleeainii
      301 qgivaeintk tgesecryyk erllyleegq kdslidssrv lcchgelknn rgvklhvflf
      361 qevlvitrav thneqlcyql yrqpipvkdl tledlqdgev rlggslrgaf snneriknff
      421 rvsfkngsqs qthslqandt fnkqqwlnci rqaketvlsa agqaglldse slsqspgten
      481 relrgetkle qmdqsdsesd csmdtsevsl ecermeqtda scansrpeen v
//
LOCUS       NP_001005903             272 aa            linear   ROD 20-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 6 [Rattus norvegicus].
ACCESSION   NP_001005903 XP_216562
VERSION     NP_001005903.1
DBSOURCE    REFSEQ: accession NM_001005903.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Oct 23, 2004 this sequence version replaced XP_216562.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083861.1, SRR26360181.1180647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..272
                     /product="F-actin-capping protein subunit beta isoform 6"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=30498
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P47756; propagated from
                     UniProtKB/Swiss-Prot (Q5XI32.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI32.1)"
     Region          11..239
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P47756; propagated from
                     UniProtKB/Swiss-Prot (Q5XI32.1)"
     CDS             1..272
                     /gene="Capzb"
                     /coded_by="NM_001005903.2:100..918"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 msdqqldcal dlmrrlppqq ieknlsdlid lvpslcedll ssvdqplkia rdkvvgkdyl
       61 lcdynrdgds yrspwsnkyd ppledgamps arlrklevea nnafdqyrdl yfeggvssvy
      121 lwdldhgfag vilikkagdg skkikgcwds ihvvevqeks sgrtahyklt stvmlwlqtn
      181 ksgsgtmnlg gsltrqmekd etvsdcsphi anigrlvedm enkirstlne iyfgktkdiv
      241 nglrsvqtfa dkskqealkn dlvealkrkq qc
//
LOCUS       NP_001423671             576 aa            linear   ROD 20-MAR-2025
DEFINITION  transketolase isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423671
VERSION     NP_001423671.1
DBSOURCE    REFSEQ: accession NM_001436742.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Zhao,Y., Wu,Y., Hu,H., Cai,J., Ning,M., Ni,X. and Zhong,C.
  TITLE     Downregulation of transketolase activity is related to inhibition
            of hippocampal progenitor cell proliferation induced by thiamine
            deficiency
  JOURNAL   Biomed Res Int 2014, 572915 (2014)
   PUBMED   25028661
  REMARK    GeneRIF: results suggest that modulation of transketolase activity
            might be one of the mechanisms by which thiamine regulates the
            proliferation of hippocampal progenitor cells.
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Mitschke,L., Parthier,C., Schroder-Tittmann,K., Coy,J., Ludtke,S.
            and Tittmann,K.
  TITLE     The crystal structure of human transketolase and new insights into
            its mode of action
  JOURNAL   J Biol Chem 285 (41), 31559-31570 (2010)
   PUBMED   20667822
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Wang,J.J., Martin,P.R. and Singleton,C.K.
  TITLE     Aspartate 155 of human transketolase is essential for thiamine
            diphosphate-magnesium binding, and cofactor binding is required for
            dimer formation
  JOURNAL   Biochim Biophys Acta 1341 (2), 165-172 (1997)
   PUBMED   9357955
REFERENCE   7  (residues 1 to 576)
  AUTHORS   McCool,B.A., Plonk,S.G., Martin,P.R. and Singleton,C.K.
  TITLE     Cloning of human transketolase cDNAs and comparison of the
            nucleotide sequence of the coding region in Wernicke-Korsakoff and
            non-Wernicke-Korsakoff individuals
  JOURNAL   J Biol Chem 268 (2), 1397-1404 (1993)
   PUBMED   8419340
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Bublitz,C. and Steavenson,S.
  TITLE     The pentose phosphate pathway in the endoplasmic reticulum
  JOURNAL   J Biol Chem 263 (26), 12849-12853 (1988)
   PUBMED   2843500
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Casazza,J.P. and Veech,R.L.
  TITLE     The interdependence of glycolytic and pentose cycle intermediates
            in ad libitum fed rats
  JOURNAL   J Biol Chem 261 (2), 690-698 (1986)
   PUBMED   3079759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.34986.1,
                                           SRR26643299.58027.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..576
                     /product="transketolase isoform 2"
                     /EC_number="2.2.1.1"
                     /note="TK"
                     /calculated_mol_wt=62516
     Region          1..573
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     CDS             1..576
                     /gene="Tkt"
                     /coded_by="NM_001436742.1:267..1997"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64524"
                     /db_xref="RGD:621036"
ORIGIN      
        1 mavlffhtmr ykaldprnph ndrfvlskgh aapilyavwa eagflpeael lnlrkissdl
       61 dghpvpkqaf tdvatgslgq glgaacgmay tgkyfdkasy rvycmlgdge vsegsvweam
      121 afagiykldn lvaifdinrl gqsdpaplqh qvdvyqkrce afgwhaiivd ghsveelcka
      181 fgqakhqpta iiaktfkgrg itgiedkeaw hgkplpknma eqiiqeiysq vqskkkilat
      241 ppqedapsvd ianirmptpp nykvgdkiat rkayglalak lghasdriia ldgdtknstf
      301 selfkkehpd rfiecyiaeq nmvsiavgca trdrtvpfcs tfaafftraf dqirmaaise
      361 sninlcgshc gvsigedgps qmaledlamf rsvpmstvfy psdgvateka velaantkgi
      421 cfirtsrpen aiiysnnedf qvgqakvvlk skddqvtvig agvtlheala aaemlkkeki
      481 gvrvldpfti kpldkklild caratkgril tvedhyyegg igeavsaavv gepgvtvtrl
      541 avsqvprsgk paellkmfgi dkdaivqavk glvtkg
//
LOCUS       NP_001423688             329 aa            linear   ROD 20-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform a
            [Rattus norvegicus].
ACCESSION   NP_001423688 XP_038965686
VERSION     NP_001423688.1
DBSOURCE    REFSEQ: accession NM_001436759.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_038965686.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.197266.1,
                                           SRR26360172.2658382.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..329
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform a"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=37665
     Region          103..309
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..329
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001436759.1:1095..2084"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaektknav
      301 qalidkhqri pgnirsalld rfhkeqkan
//
LOCUS       NP_001423685             225 aa            linear   ROD 20-MAR-2025
DEFINITION  occludin/ELL domain-containing protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423685
VERSION     NP_001423685.1
DBSOURCE    REFSEQ: accession NM_001436756.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.84895.1,
                                           SRR26360186.322549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..225
                     /product="occludin/ELL domain-containing protein 1 isoform
                     3"
                     /note="occludin/ELL domain-containing protein 1"
                     /calculated_mol_wt=25618
     Region          113..213
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..225
                     /gene="Ocel1"
                     /gene_synonym="RGD1563236; RGD1565407"
                     /coded_by="NM_001436756.1:347..1024"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:290628"
                     /db_xref="RGD:1565407"
ORIGIN      
        1 mqipagpssr rrsrgplacg sqsrrsgpda tcnsrpaagg rqsatapcmp arerpqprag
       61 rphcqprpse lrtrprkivf adelqprapl hpekhprdlg prpnpvpdye lkyppvtsrr
      121 drsryaavfq dqyeeflelq rqvgamqakl qqlealllsl ppprsqevrm aahvrrefek
      181 krvdpgfldk qarcdylkgk lrhlkaqirk fddqrdsnse nsvyf
//
LOCUS       NP_001423682             374 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423682
VERSION     NP_001423682.1
DBSOURCE    REFSEQ: accession NM_001436753.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2429703.1,
                                           SRR26643297.46193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..374
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     4"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=42567
     Region          7..151
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          165..297
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..374
                     /gene="Arhgef3"
                     /coded_by="NM_001436753.1:950..2074"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mlklsimteq elnqifgtld sliplhedll sqlrdvrkpd gstehvgpil vgwlpclssy
       61 dsycsnqvaa kalldhkkqd hrvqdflqrc lespfsrkld lwnfldiprs rlvkyplllr
      121 eilrhtpndn pdqqhleeai niiqgivaei ntktgesecr yykerllyle egqkdslids
      181 srvlcchgel knnrgvklhv flfqevlvit ravthneqlc yqlyrqpipv kdltledlqd
      241 gevrlggslr gafsnnerik nffrvsfkng sqsqthslqa ndtfnkqqwl ncirqaketv
      301 lsaagqagll dseslsqspg tenrelrget kleqmdqsds esdcsmdtse vslecermeq
      361 tdascansrp eenv
//
LOCUS       NP_001423664             294 aa            linear   ROD 20-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423664
VERSION     NP_001423664.1
DBSOURCE    REFSEQ: accession NM_001436735.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.31166.1,
                                           SRR26360181.2145995.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..294
                     /product="F-actin-capping protein subunit beta isoform 5"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=33025
     Region          33..261
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..294
                     /gene="Capzb"
                     /coded_by="NM_001436735.1:250..1134"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 mcinqveqse gftwqdgrse mnssdqqldc aldlmrrlpp qqieknlsdl idlvpslced
       61 llssvdqplk iardkvvgkd yllcdynrdg dsyrspwsnk ydppledgam psarlrklev
      121 eannafdqyr dlyfeggvss vylwdldhgf agvilikkag dgskkikgcw dsihvvevqe
      181 kssgrtahyk ltstvmlwlq tnksgsgtmn lggsltrqme kdetvsdcsp hianigrlve
      241 dmenkirstl neiyfgktkd ivnglrsvqt fadkskqeal kndlvealkr kqqc
//
LOCUS       NP_001101372             423 aa            linear   ROD 20-MAR-2025
DEFINITION  transcription factor SOX-17 [Rattus norvegicus].
ACCESSION   NP_001101372 XP_001068621 XP_232640
VERSION     NP_001101372.1
DBSOURCE    REFSEQ: accession NM_001107902.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Walters,R., Vasilaki,E., Aman,J., Chen,C.N., Wu,Y., Liang,O.D.,
            Ashek,A., Dubois,O., Zhao,L., Sabrin,F., Cebola,I., Ferrer,J.,
            Morrell,N.W., Klinger,J.R., Wilkins,M.R., Zhao,L. and Rhodes,C.J.
  TITLE     SOX17 Enhancer Variants Disrupt Transcription Factor Binding And
            Enhancer Inactivity Drives Pulmonary Hypertension
  JOURNAL   Circulation 147 (21), 1606-1621 (2023)
   PUBMED   37066790
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zou,X., Liu,T., Huang,Z., Zhou,W., Yuan,M., Zhao,H., Pan,Z.,
            Chen,P., Shao,Y., Hu,X., Zhang,S., Zheng,S., Zhang,Y. and Huang,P.
  TITLE     SOX17 is a Critical Factor in Maintaining Endothelial Function in
            Pulmonary Hypertension by an Exosome-Mediated Autocrine Manner
  JOURNAL   Adv Sci (Weinh) 10 (14), e2206139 (2023)
   PUBMED   36919784
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Sangam,S., Sun,X., Schwantes-An,T.H., Yegambaram,M., Lu,Q., Shi,Y.,
            Cook,T., Fisher,A., Frump,A.L., Coleman,A., Sun,Y., Liang,S.,
            Crawford,H., Lutz,K.A., Maun,A.D., Pauciulo,M.W., Karnes,J.H.,
            Chaudhary,K.R., Stewart,D.J., Langlais,P.R., Jain,M., Alotaibi,M.,
            Lahm,T., Jin,Y., Gu,H., Tang,H., Nichols,W.C., Black,S.M. and
            Desai,A.A.
  TITLE     SOX17 Deficiency Mediates Pulmonary Hypertension: At the Crossroads
            of Sex, Metabolism, and Genetics
  JOURNAL   Am J Respir Crit Care Med 207 (8), 1055-1069 (2023)
   PUBMED   36913491
  REMARK    GeneRIF: SOX17 Deficiency Mediates Pulmonary Hypertension: At the
            Crossroads of Sex, Metabolism, and Genetics.
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Wan,Q., Liu,H., Xu,Y., Zhang,Q. and Tao,L.
  TITLE     Upregulated miR-194-5p suppresses retinal microvascular endothelial
            cell dysfunction and mitigates the symptoms of hypertensive
            retinopathy in mice by targeting SOX17 and VEGF signaling
  JOURNAL   Cell Cycle 22 (3), 331-346 (2023)
   PUBMED   36200131
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Park,C.S., Kim,S.H., Yang,H.Y., Kim,J.H., Schermuly,R.T., Cho,Y.S.,
            Kang,H., Park,J.H., Lee,E., Park,H., Yang,J.M., Noh,T.W., Lee,S.P.,
            Bae,S.S., Han,J., Ju,Y.S., Park,J.B. and Kim,I.
  TITLE     Sox17 Deficiency Promotes Pulmonary Arterial Hypertension via
            HGF/c-Met Signaling
  JOURNAL   Circ Res 131 (10), 792-806 (2022)
   PUBMED   36205124
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Park,K.S., Wells,J.M., Zorn,A.M., Wert,S.E. and Whitsett,J.A.
  TITLE     Sox17 influences the differentiation of respiratory epithelial
            cells
  JOURNAL   Dev Biol 294 (1), 192-202 (2006)
   PUBMED   16574095
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Niimi,T., Hayashi,Y., Futaki,S. and Sekiguchi,K.
  TITLE     SOX7 and SOX17 regulate the parietal endoderm-specific enhancer
            activity of mouse laminin alpha1 gene
  JOURNAL   J Biol Chem 279 (36), 38055-38061 (2004)
   PUBMED   15220343
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Murakami,A., Shen,H., Ishida,S. and Dickson,C.
  TITLE     SOX7 and GATA-4 are competitive activators of Fgf-3 transcription
  JOURNAL   J Biol Chem 279 (27), 28564-28573 (2004)
   PUBMED   15082719
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Kanai-Azuma,M., Kanai,Y., Gad,J.M., Tajima,Y., Taya,C.,
            Kurohmaru,M., Sanai,Y., Yonekawa,H., Yazaki,K., Tam,P.P. and
            Hayashi,Y.
  TITLE     Depletion of definitive gut endoderm in Sox17-null mutant mice
  JOURNAL   Development 129 (10), 2367-2379 (2002)
   PUBMED   11973269
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Kanai,Y., Kanai-Azuma,M., Noce,T., Saido,T.C., Shiroishi,T.,
            Hayashi,Y. and Yazaki,K.
  TITLE     Identification of two Sox17 messenger RNA isoforms, with and
            without the high mobility group box region, and their differential
            expression in mouse spermatogenesis
  JOURNAL   J Cell Biol 133 (3), 667-681 (1996)
   PUBMED   8636240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232640.3, XP_001068621.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR22582419.366550.1, FM036904.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..423
                     /product="transcription factor SOX-17"
                     /note="SRY-box containing gene 17; SRY (sex determining
                     region Y)-box 17; SRY box 17"
                     /calculated_mol_wt=44908
     Region          62..142
                     /region_name="HMG-box_SoxF_SOX17"
                     /note="high mobility group (HMG)-box found in sex
                     determining region Y (SRY)-box 17 (SOX17) and similar
                     proteins; cd22047"
                     /db_xref="CDD:438850"
     Site            order(69..70,72..73,75..76,80,83,94..96,99..100,103,106,
                     136..137,139..141)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438850"
     Region          203..253
                     /region_name="Sox17_18_mid"
                     /note="Sox 17/18 central domain; pfam12067"
                     /db_xref="CDD:463454"
     CDS             1..423
                     /gene="Sox17"
                     /coded_by="NM_001107902.2:327..1598"
                     /db_xref="GeneID:312936"
                     /db_xref="RGD:1305371"
ORIGIN      
        1 msspdagyas ddqsqprsaq pavmaglgpc pwaeslsslg dvkvkgevva ssgapagtss
       61 rakaesrirr pmnafmvwak derkrlaqqn pdlhnaelsk mlgkswkalt laekrpfvee
      121 aerlrvqhmq dhpnykyrpr rrkqvkrmkr veggflhala epqagalgpe ggrvamdglg
      181 lpfpepgypa gpplmsphmg ahyrdcqglg apaldgyplp tpdtspldgv eqdpaffaap
      241 lpgdcpaaga ytyaqvsdya vpaepsagpm rvgpdpsgsa mpgilappsa lhlyygamgs
      301 paasagrgfh aqpqqplqpq pppppppppp pqqhpthgpg qpspppealp crdgtepnqp
      361 tellgevdrt efeqylhfvy kpemglpyqg hdcgvnlsds hgaissvvsd assavyycny
      421 pdi
//
LOCUS       NP_001423666             613 aa            linear   ROD 20-MAR-2025
DEFINITION  pleckstrin homology domain-containing family N member 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001423666 XP_006239626
VERSION     NP_001423666.1
DBSOURCE    REFSEQ: accession NM_001436737.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Kuriyama,S., Tsuji,T., Sakuma,T., Yamamoto,T. and Tanaka,M.
  TITLE     PLEKHN1 promotes apoptosis by enhancing Bax-Bak
            hetro-oligomerization through interaction with Bid in human colon
            cancer
  JOURNAL   Cell Death Discov 4, 11 (2018)
   PUBMED   29531808
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Maeda,A., Uchida,M., Nishikawa,S., Nishino,T. and Konishi,H.
  TITLE     Role of N-myristoylation in stability and subcellular localization
            of the CLPABP protein
  JOURNAL   Biochem Biophys Res Commun 495 (1), 1249-1256 (2018)
   PUBMED   29180010
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Nishino,T., Matsunaga,R., Jikihara,H., Uchida,M., Maeda,A., Qi,G.,
            Abe,T., Kiyonari,H., Tashiro,S., Inagaki-Ohara,K., Shimamoto,F. and
            Konishi,H.
  TITLE     Antagonizing effect of CLPABP on the function of HuR as a regulator
            of ARE-containing leptin mRNA stability and the effect of its
            depletion on obesity in old male mouse
  JOURNAL   Biochim Biophys Acta 1861 (11), 1816-1827 (2016)
   PUBMED   27616329
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Sano,E., Shono,S., Tashiro,K., Konishi,H., Yamauchi,E. and
            Taniguchi,H.
  TITLE     Novel tyrosine phosphorylated and cardiolipin-binding protein
            CLPABP functions as mitochondrial RNA granule
  JOURNAL   Biochim Biophys Acta 1783 (6), 1036-1047 (2008)
   PUBMED   18191643
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006239626.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.25942.1,
                                           SRR26643294.24145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..613
                     /product="pleckstrin homology domain-containing family N
                     member 1 isoform 3"
                     /note="pleckstrin homology domain containing, family N
                     member 1"
                     /calculated_mol_wt=67275
     Region          96..188
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          222..341
                     /region_name="PH_PLEKHN1"
                     /note="Pleckstrin homology domain containing family N
                     member 1Pleckstrin homology-like domain; cd13323"
                     /db_xref="CDD:270132"
     CDS             1..613
                     /gene="Plekhn1"
                     /gene_synonym="RGD1311019"
                     /coded_by="NM_001436737.1:43..1884"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:298694"
                     /db_xref="RGD:1311019"
ORIGIN      
        1 mgnshcvpqt prrlrasfsr kpslkgnred sarklaglfg tearpdgdta ankifhyipg
       61 tdilgpenhp enleqpflsv fkkgwrrtpv rnlgkvvhys kvqlrfqhsq disdcylelf
      121 pshlyfqahg segltfqgll pltelsicpi dgsrehafqi tgplpapllv lchseaelsh
      181 wlyhlekqma llglrqchsa ppqgslgdkl pwtqlwrahg cepmnsaica srvklqhlps
      241 qeqwdrllvl ypaslaifse epeglnfkge lplsaihinl eekekeirsf liegrlinti
      301 rvvcasyedy sqwllclrtv shrdgahllp gpesfpglqr ptqvlgrgrg slssngrtsr
      361 klecpvfpts qslpepsvpt tigvpahpvp nqtnsncvst gqtkvelrhs gssqfprgka
      421 qrevsgstap lplhldltkm svlnldsgpe aqdcspdiph splyadpytp paiahhkitd
      481 iqgldeqflc avqtspgpel sspfpsvsvs vpvsdsnsgi sssprplgsh llskkgalqs
      541 rasqrhrgsi ksrapqpsdf pqlvtpareg tpsslppppd eeapiwnkts spshqkwshp
      601 rkpaveggfi qwi
//
LOCUS       NP_001423655             626 aa            linear   ROD 20-MAR-2025
DEFINITION  rho GTPase-activating protein 22 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423655
VERSION     NP_001423655.1
DBSOURCE    REFSEQ: accession NM_001436726.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Valnegri,P., Montrasio,C., Brambilla,D., Ko,J., Passafaro,M. and
            Sala,C.
  TITLE     The X-linked intellectual disability protein IL1RAPL1 regulates
            excitatory synapse formation by binding PTPdelta and RhoGAP2
  JOURNAL   Hum Mol Genet 20 (24), 4797-4809 (2011)
   PUBMED   21926414
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.1942386.1,
                                           SRR21887622.1942385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345331, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..626
                     /product="rho GTPase-activating protein 22 isoform 4"
                     /note="rho GTPase-activating protein 22"
                     /calculated_mol_wt=68260
     Region          <18..61
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          77..275
                     /region_name="RhoGAP_ARHGAP22_24_25"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP22, 24 and 25-like proteins; longer
                     isoforms of these proteins contain an additional
                     N-terminal pleckstrin homology (PH) domain. ARHGAP25
                     (KIA0053) has been identified as a GAP for...; cd04390"
                     /db_xref="CDD:239855"
     Site            order(121,158,162,233,236..237,261)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239855"
     Site            121
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239855"
     Region          <292..>607
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          <518..>608
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..626
                     /gene="Arhgap22"
                     /coded_by="NM_001436726.1:138..2018"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:306279"
                     /db_xref="RGD:1307237"
ORIGIN      
        1 mglccckdwr ghlrapkgga aerekvpanp ealllmassq rdmedwvqai rrviwaplgg
       61 gtsrsshahp veplstgifg qrledtvhhe rkfgprlapl lveqcvdfir erglseeglf
      121 rmpgqanlvr dlqdsfdcge kplfdsttdv htvasllkly lrelpepvip faryedflsc
      181 aqlltkdege gtvelakqvs nlpqanynll ryicrfldev qahsdvnkms vqnlatvfgp
      241 nilrpqvedp vtimegtslv qhlmtvlirk hgqlfatpsf eepasprgtv qgtvewgsee
      301 vtrdhqgepg ssglpthrts sldgpaaavl srtspprlgs qagpaatspg krmhtlpgwk
      361 ssfrqqgsrs espkgvsssl evpiissggn wlinglsslr shrrassgdr lkdtgsaqrl
      421 stydnvppss hlsstasvas tawsvasssr easigsctac rasnssacss lhtewaleps
      481 plpssseghp spdlghslde acvgsgssep ndpgspsqah vrrcralqgq vaelraelch
      541 qrieyqrslk sieegnsdlr kqmcrleeel dqekkkyaml eiklrnsera redaerrnql
      601 lqremeeffa tlgsltagtk garape
//
LOCUS       NP_001423690             300 aa            linear   ROD 20-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform b
            [Rattus norvegicus].
ACCESSION   NP_001423690 XP_006237894
VERSION     NP_001423690.1
DBSOURCE    REFSEQ: accession NM_001436761.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006237894.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1447106.1,
                                           SRR26360176.1380079.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..300
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform b"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=34336
     Region          103..295
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..300
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001436761.1:269..1171"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaekpltrp
//
LOCUS       NP_001423654             610 aa            linear   ROD 20-MAR-2025
DEFINITION  rho GTPase-activating protein 22 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423654
VERSION     NP_001423654.1
DBSOURCE    REFSEQ: accession NM_001436725.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Valnegri,P., Montrasio,C., Brambilla,D., Ko,J., Passafaro,M. and
            Sala,C.
  TITLE     The X-linked intellectual disability protein IL1RAPL1 regulates
            excitatory synapse formation by binding PTPdelta and RhoGAP2
  JOURNAL   Hum Mol Genet 20 (24), 4797-4809 (2011)
   PUBMED   21926414
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.453722.1,
                                           SRR21887622.1965971.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680435, SAMN06680445
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..610
                     /product="rho GTPase-activating protein 22 isoform 3"
                     /note="rho GTPase-activating protein 22"
                     /calculated_mol_wt=66615
     Region          <18..61
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          61..259
                     /region_name="RhoGAP_ARHGAP22_24_25"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP22, 24 and 25-like proteins; longer
                     isoforms of these proteins contain an additional
                     N-terminal pleckstrin homology (PH) domain. ARHGAP25
                     (KIA0053) has been identified as a GAP for...; cd04390"
                     /db_xref="CDD:239855"
     Site            order(105,142,146,217,220..221,245)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239855"
     Site            105
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239855"
     Region          <276..>591
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          <502..>592
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..610
                     /gene="Arhgap22"
                     /coded_by="NM_001436725.1:138..1970"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:306279"
                     /db_xref="RGD:1307237"
ORIGIN      
        1 mglccckdwr ghlrapkgga aerekvpanp ealllmassq rdmedwvqai rrviwaplgg
       61 gifgqrledt vhherkfgpr lapllveqcv dfirerglse eglfrmpgqa nlvrdlqdsf
      121 dcgekplfds ttdvhtvasl lklylrelpe pvipfaryed flscaqlltk degegtvela
      181 kqvsnlpqan ynllryicrf ldevqahsdv nkmsvqnlat vfgpnilrpq vedpvtimeg
      241 tslvqhlmtv lirkhgqlfa tpsfeepasp rgtvqgtvew gseevtrdhq gepgssglpt
      301 hrtssldgpa aavlsrtspp rlgsqagpaa tspgkrmhtl pgwkssfrqq gsrsespkgv
      361 ssslevpiis sggnwlingl sslrshrras sgdrlkdtgs aqrlstydnv ppsshlssta
      421 svastawsva sssreasigs ctacrasnss acsslhtewa lepsplpsss eghpspdlgh
      481 sldeacvgsg ssepndpgsp sqahvrrcra lqgqvaelra elchqrieyq rslksieegn
      541 sdlrkqmcrl eeeldqekkk yamleiklrn seraredaer rnqllqreme effatlgslt
      601 agtkgarape
//
LOCUS       NP_001423662             302 aa            linear   ROD 20-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423662 XP_006239237
VERSION     NP_001423662.1
DBSOURCE    REFSEQ: accession NM_001436733.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006239237.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.23410.1,
                                           SRR26360186.314000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..302
                     /product="F-actin-capping protein subunit beta isoform 3"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=33737
     Region          41..269
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..302
                     /gene="Capzb"
                     /coded_by="NM_001436733.1:10..918"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 mmhpsrrslp fplncqlvrv gtadyggaad qsdqqldcal dlmrrlppqq ieknlsdlid
       61 lvpslcedll ssvdqplkia rdkvvgkdyl lcdynrdgds yrspwsnkyd ppledgamps
      121 arlrklevea nnafdqyrdl yfeggvssvy lwdldhgfag vilikkagdg skkikgcwds
      181 ihvvevqeks sgrtahyklt stvmlwlqtn ksgsgtmnlg gsltrqmekd etvsdcsphi
      241 anigrlvedm enkirstlne iyfgktkdiv nglrsvqtfa dkskqealkn dlvealkrkq
      301 qc
//
LOCUS       NP_001423672             562 aa            linear   ROD 20-MAR-2025
DEFINITION  transketolase isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423672
VERSION     NP_001423672.1
DBSOURCE    REFSEQ: accession NM_001436743.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Zhao,Y., Wu,Y., Hu,H., Cai,J., Ning,M., Ni,X. and Zhong,C.
  TITLE     Downregulation of transketolase activity is related to inhibition
            of hippocampal progenitor cell proliferation induced by thiamine
            deficiency
  JOURNAL   Biomed Res Int 2014, 572915 (2014)
   PUBMED   25028661
  REMARK    GeneRIF: results suggest that modulation of transketolase activity
            might be one of the mechanisms by which thiamine regulates the
            proliferation of hippocampal progenitor cells.
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Mitschke,L., Parthier,C., Schroder-Tittmann,K., Coy,J., Ludtke,S.
            and Tittmann,K.
  TITLE     The crystal structure of human transketolase and new insights into
            its mode of action
  JOURNAL   J Biol Chem 285 (41), 31559-31570 (2010)
   PUBMED   20667822
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Wang,J.J., Martin,P.R. and Singleton,C.K.
  TITLE     Aspartate 155 of human transketolase is essential for thiamine
            diphosphate-magnesium binding, and cofactor binding is required for
            dimer formation
  JOURNAL   Biochim Biophys Acta 1341 (2), 165-172 (1997)
   PUBMED   9357955
REFERENCE   7  (residues 1 to 562)
  AUTHORS   McCool,B.A., Plonk,S.G., Martin,P.R. and Singleton,C.K.
  TITLE     Cloning of human transketolase cDNAs and comparison of the
            nucleotide sequence of the coding region in Wernicke-Korsakoff and
            non-Wernicke-Korsakoff individuals
  JOURNAL   J Biol Chem 268 (2), 1397-1404 (1993)
   PUBMED   8419340
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Bublitz,C. and Steavenson,S.
  TITLE     The pentose phosphate pathway in the endoplasmic reticulum
  JOURNAL   J Biol Chem 263 (26), 12849-12853 (1988)
   PUBMED   2843500
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Casazza,J.P. and Veech,R.L.
  TITLE     The interdependence of glycolytic and pentose cycle intermediates
            in ad libitum fed rats
  JOURNAL   J Biol Chem 261 (2), 690-698 (1986)
   PUBMED   3079759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1950922.1,
                                           SRR26360190.2094273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..562
                     /product="transketolase isoform 3"
                     /EC_number="2.2.1.1"
                     /note="TK"
                     /calculated_mol_wt=61221
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Region          8..536
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            37
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P40142; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            258
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     CDS             1..562
                     /gene="Tkt"
                     /coded_by="NM_001436743.1:84..1772"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:64524"
                     /db_xref="RGD:621036"
ORIGIN      
        1 megyhkpdqq klqalkdtan rlrissiqat taagsghpts ccsaaeimav lffhtmryka
       61 ldprnphndr fvlskghaap ilyavwaeag flpeaellnl rkissdldgh pvpkqaftdv
      121 atgslgqglg aacgmaytgk yfdkasyrvy cmlgdgevse gsvweamafa giykldnlva
      181 ifdinrlgqs dpaplqhqvd vyqkrceafg whaiivdghs veelckafgq akhqptaiia
      241 ktfkgrgitg iedkeawhgk plpknmaeqi iqeiysqvqs kkkilatppq edapsvdian
      301 irmptppnyk vgdkiatrka yglalaklgh asdriialdg dtknstfsel fkkehpdrfi
      361 ecyiaeqnmv siavgcatrd rtvpfcstfa afftrafdqi rmaaisesni nlcgshcgvs
      421 igedgpsqma ledlamfrsv pmstvfypsd gvatekavel aantkgicfi rtsrpenaii
      481 ysnnedfqvg qakvvlkskd dqvtvigagv tlhealaaae mlkkdrrpct gplhhqapgq
      541 kahsrlcqsn qrqdphrggp ll
//
LOCUS       NP_001423669             423 aa            linear   ROD 20-MAR-2025
DEFINITION  transcription factor SOX-17 [Rattus norvegicus].
ACCESSION   NP_001423669
VERSION     NP_001423669.1
DBSOURCE    REFSEQ: accession NM_001436740.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Walters,R., Vasilaki,E., Aman,J., Chen,C.N., Wu,Y., Liang,O.D.,
            Ashek,A., Dubois,O., Zhao,L., Sabrin,F., Cebola,I., Ferrer,J.,
            Morrell,N.W., Klinger,J.R., Wilkins,M.R., Zhao,L. and Rhodes,C.J.
  TITLE     SOX17 Enhancer Variants Disrupt Transcription Factor Binding And
            Enhancer Inactivity Drives Pulmonary Hypertension
  JOURNAL   Circulation 147 (21), 1606-1621 (2023)
   PUBMED   37066790
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zou,X., Liu,T., Huang,Z., Zhou,W., Yuan,M., Zhao,H., Pan,Z.,
            Chen,P., Shao,Y., Hu,X., Zhang,S., Zheng,S., Zhang,Y. and Huang,P.
  TITLE     SOX17 is a Critical Factor in Maintaining Endothelial Function in
            Pulmonary Hypertension by an Exosome-Mediated Autocrine Manner
  JOURNAL   Adv Sci (Weinh) 10 (14), e2206139 (2023)
   PUBMED   36919784
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Sangam,S., Sun,X., Schwantes-An,T.H., Yegambaram,M., Lu,Q., Shi,Y.,
            Cook,T., Fisher,A., Frump,A.L., Coleman,A., Sun,Y., Liang,S.,
            Crawford,H., Lutz,K.A., Maun,A.D., Pauciulo,M.W., Karnes,J.H.,
            Chaudhary,K.R., Stewart,D.J., Langlais,P.R., Jain,M., Alotaibi,M.,
            Lahm,T., Jin,Y., Gu,H., Tang,H., Nichols,W.C., Black,S.M. and
            Desai,A.A.
  TITLE     SOX17 Deficiency Mediates Pulmonary Hypertension: At the Crossroads
            of Sex, Metabolism, and Genetics
  JOURNAL   Am J Respir Crit Care Med 207 (8), 1055-1069 (2023)
   PUBMED   36913491
  REMARK    GeneRIF: SOX17 Deficiency Mediates Pulmonary Hypertension: At the
            Crossroads of Sex, Metabolism, and Genetics.
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Wan,Q., Liu,H., Xu,Y., Zhang,Q. and Tao,L.
  TITLE     Upregulated miR-194-5p suppresses retinal microvascular endothelial
            cell dysfunction and mitigates the symptoms of hypertensive
            retinopathy in mice by targeting SOX17 and VEGF signaling
  JOURNAL   Cell Cycle 22 (3), 331-346 (2023)
   PUBMED   36200131
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Park,C.S., Kim,S.H., Yang,H.Y., Kim,J.H., Schermuly,R.T., Cho,Y.S.,
            Kang,H., Park,J.H., Lee,E., Park,H., Yang,J.M., Noh,T.W., Lee,S.P.,
            Bae,S.S., Han,J., Ju,Y.S., Park,J.B. and Kim,I.
  TITLE     Sox17 Deficiency Promotes Pulmonary Arterial Hypertension via
            HGF/c-Met Signaling
  JOURNAL   Circ Res 131 (10), 792-806 (2022)
   PUBMED   36205124
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Park,K.S., Wells,J.M., Zorn,A.M., Wert,S.E. and Whitsett,J.A.
  TITLE     Sox17 influences the differentiation of respiratory epithelial
            cells
  JOURNAL   Dev Biol 294 (1), 192-202 (2006)
   PUBMED   16574095
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Niimi,T., Hayashi,Y., Futaki,S. and Sekiguchi,K.
  TITLE     SOX7 and SOX17 regulate the parietal endoderm-specific enhancer
            activity of mouse laminin alpha1 gene
  JOURNAL   J Biol Chem 279 (36), 38055-38061 (2004)
   PUBMED   15220343
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Murakami,A., Shen,H., Ishida,S. and Dickson,C.
  TITLE     SOX7 and GATA-4 are competitive activators of Fgf-3 transcription
  JOURNAL   J Biol Chem 279 (27), 28564-28573 (2004)
   PUBMED   15082719
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Kanai-Azuma,M., Kanai,Y., Gad,J.M., Tajima,Y., Taya,C.,
            Kurohmaru,M., Sanai,Y., Yonekawa,H., Yazaki,K., Tam,P.P. and
            Hayashi,Y.
  TITLE     Depletion of definitive gut endoderm in Sox17-null mutant mice
  JOURNAL   Development 129 (10), 2367-2379 (2002)
   PUBMED   11973269
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Kanai,Y., Kanai-Azuma,M., Noce,T., Saido,T.C., Shiroishi,T.,
            Hayashi,Y. and Yazaki,K.
  TITLE     Identification of two Sox17 messenger RNA isoforms, with and
            without the high mobility group box region, and their differential
            expression in mouse spermatogenesis
  JOURNAL   J Cell Biol 133 (3), 667-681 (1996)
   PUBMED   8636240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166978.1, SRR26643294.20369.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..423
                     /product="transcription factor SOX-17"
                     /note="SRY-box containing gene 17; SRY (sex determining
                     region Y)-box 17; SRY box 17"
                     /calculated_mol_wt=44908
     Region          62..142
                     /region_name="HMG-box_SoxF_SOX17"
                     /note="high mobility group (HMG)-box found in sex
                     determining region Y (SRY)-box 17 (SOX17) and similar
                     proteins; cd22047"
                     /db_xref="CDD:438850"
     Site            order(69..70,72..73,75..76,80,83,94..96,99..100,103,106,
                     136..137,139..141)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438850"
     Region          203..253
                     /region_name="Sox17_18_mid"
                     /note="Sox 17/18 central domain; pfam12067"
                     /db_xref="CDD:463454"
     CDS             1..423
                     /gene="Sox17"
                     /coded_by="NM_001436740.1:1047..2318"
                     /db_xref="GeneID:312936"
                     /db_xref="RGD:1305371"
ORIGIN      
        1 msspdagyas ddqsqprsaq pavmaglgpc pwaeslsslg dvkvkgevva ssgapagtss
       61 rakaesrirr pmnafmvwak derkrlaqqn pdlhnaelsk mlgkswkalt laekrpfvee
      121 aerlrvqhmq dhpnykyrpr rrkqvkrmkr veggflhala epqagalgpe ggrvamdglg
      181 lpfpepgypa gpplmsphmg ahyrdcqglg apaldgyplp tpdtspldgv eqdpaffaap
      241 lpgdcpaaga ytyaqvsdya vpaepsagpm rvgpdpsgsa mpgilappsa lhlyygamgs
      301 paasagrgfh aqpqqplqpq pppppppppp pqqhpthgpg qpspppealp crdgtepnqp
      361 tellgevdrt efeqylhfvy kpemglpyqg hdcgvnlsds hgaissvvsd assavyycny
      421 pdi
//
LOCUS       NP_001423652             706 aa            linear   ROD 20-MAR-2025
DEFINITION  rho GTPase-activating protein 22 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423652
VERSION     NP_001423652.1
DBSOURCE    REFSEQ: accession NM_001436723.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Valnegri,P., Montrasio,C., Brambilla,D., Ko,J., Passafaro,M. and
            Sala,C.
  TITLE     The X-linked intellectual disability protein IL1RAPL1 regulates
            excitatory synapse formation by binding PTPdelta and RhoGAP2
  JOURNAL   Hum Mol Genet 20 (24), 4797-4809 (2011)
   PUBMED   21926414
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360194.1993361.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760393, SAMN09345238 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..706
                     /product="rho GTPase-activating protein 22 isoform 1"
                     /note="rho GTPase-activating protein 22"
                     /calculated_mol_wt=77643
     Region          42..157
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          157..355
                     /region_name="RhoGAP_ARHGAP22_24_25"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP22, 24 and 25-like proteins; longer
                     isoforms of these proteins contain an additional
                     N-terminal pleckstrin homology (PH) domain. ARHGAP25
                     (KIA0053) has been identified as a GAP for...; cd04390"
                     /db_xref="CDD:239855"
     Site            order(201,238,242,313,316..317,341)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239855"
     Site            201
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239855"
     Region          <372..>687
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          <598..>688
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..706
                     /gene="Arhgap22"
                     /coded_by="NM_001436723.1:376..2496"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:306279"
                     /db_xref="RGD:1307237"
ORIGIN      
        1 mlpaasskrr tfasryftrs kslvmgeqsr spgrplaphk lgpvlkagwl rkqksimknw
       61 qqrwfvlrgd qlfyykdkde gkpqgfislq gtqvtellpd pddpgkhlfe itpggaaere
      121 kvpanpeall lmassqrdme dwvqairrvi waplgggifg qrledtvhhe rkfgprlapl
      181 lveqcvdfir erglseeglf rmpgqanlvr dlqdsfdcge kplfdsttdv htvasllkly
      241 lrelpepvip faryedflsc aqlltkdege gtvelakqvs nlpqanynll ryicrfldev
      301 qahsdvnkms vqnlatvfgp nilrpqvedp vtimegtslv qhlmtvlirk hgqlfatpsf
      361 eepasprgtv qgtvewgsee vtrdhqgepg ssglpthrts sldgpaaavl srtspprlgs
      421 qagpaatspg krmhtlpgwk ssfrqqgsrs espkgvsssl evpiissggn wlinglsslr
      481 shrrassgdr lkdtgsaqrl stydnvppss hlsstasvas tawsvasssr easigsctac
      541 rasnssacss lhtewaleps plpssseghp spdlghslde acvgsgssep ndpgspsqah
      601 vrrcralqgq vaelraelch qrieyqrslk sieegnsdlr kqmcrleeel dqekkkyaml
      661 eiklrnsera redaerrnql lqremeeffa tlgsltagtk garape
//
LOCUS       NP_001101391            1962 aa            linear   ROD 20-MAR-2025
DEFINITION  CASP8-associated protein 2 [Rattus norvegicus].
ACCESSION   NP_001101391 XP_001063464 XP_232860
VERSION     NP_001101391.1
DBSOURCE    REFSEQ: accession NM_001107921.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1962)
  AUTHORS   Wu,T.Y., Leng,Q. and Tian,L.Q.
  TITLE     The microRNA-210/Casp8ap2 Axis Alleviates Hypoxia-Induced
            Myocardial Injury by Regulating Apoptosis and Autophagy
  JOURNAL   Cytogenet Genome Res 161 (3-4), 132-142 (2021)
   PUBMED   33882492
  REMARK    GeneRIF: The microRNA-210/Casp8ap2 Axis Alleviates Hypoxia-Induced
            Myocardial Injury by Regulating Apoptosis and Autophagy.
REFERENCE   2  (residues 1 to 1962)
  AUTHORS   Li,K., Pan,J., Li,Q., Li,S., Li,K., Cheng,Y., Chai,L., Li,C.,
            Li,J., Fu,Z., Wang,D. and Bai,Y.
  TITLE     The MicroRNA-210/Casp8ap2 Pathway Alleviates Hypoxia-Induced Injury
            in Myocardial Cells by Regulating Apoptosis and Autophagy
  JOURNAL   Heart Surg Forum 23 (6), E797-E802 (2020)
   PUBMED   33234216
  REMARK    GeneRIF: The MicroRNA-210/Casp8ap2 Pathway Alleviates
            Hypoxia-Induced Injury in Myocardial Cells by Regulating Apoptosis
            and Autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1962)
  AUTHORS   Li,T., Song,X., Zhang,J., Zhao,L., Shi,Y., Li,Z., Liu,J., Liu,N.,
            Yan,Y., Xiao,Y., Tian,X., Sun,W., Guan,Y. and Liu,B.
  TITLE     Protection of Human Umbilical Vein Endothelial Cells against
            Oxidative Stress by MicroRNA-210
  JOURNAL   Oxid Med Cell Longev 2017, 3565613 (2017)
   PUBMED   28367268
REFERENCE   4  (residues 1 to 1962)
  AUTHORS   Sun,H. and Hunter,T.
  TITLE     Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins
            identified through a string search
  JOURNAL   J Biol Chem 287 (50), 42071-42083 (2012)
   PUBMED   23086935
REFERENCE   5  (residues 1 to 1962)
  AUTHORS   Kim,H.W., Mallick,F., Durrani,S., Ashraf,M., Jiang,S. and
            Haider,K.H.
  TITLE     Concomitant activation of miR-107/PDCD10 and hypoxamir-210/Casp8ap2
            and their role in cytoprotection during ischemic preconditioning of
            stem cells
  JOURNAL   Antioxid Redox Signal 17 (8), 1053-1065 (2012)
   PUBMED   22482882
  REMARK    GeneRIF: The ischemic preconditioning (IPC) enhances stem cell
            survival via the combined participation of hypoxia responsive miRs
            miR-107 and miR-210 via their respective putative target genes
            Pdcd10 and Casp8ap2.
REFERENCE   6  (residues 1 to 1962)
  AUTHORS   Kim,H.W., Haider,H.K., Jiang,S. and Ashraf,M.
  TITLE     Ischemic preconditioning augments survival of stem cells via
            miR-210 expression by targeting caspase-8-associated protein 2
  JOURNAL   J Biol Chem 284 (48), 33161-33168 (2009)
   PUBMED   19721136
  REMARK    GeneRIF: Data identified FLICE-associated huge protein
            (FLASH)/caspase-8-associated protein-2 (Casp8ap2) in (PC)MSCs as
            the target gene of miR-210.
REFERENCE   7  (residues 1 to 1962)
  AUTHORS   Smith,A.J., Karpova,Y., D'Agostino,R. Jr., Willingham,M. and
            Kulik,G.
  TITLE     Expression of the Bcl-2 protein BAD promotes prostate cancer growth
  JOURNAL   PLoS One 4 (7), e6224 (2009)
   PUBMED   19593445
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1962)
  AUTHORS   Milovic-Holm,K., Krieghoff,E., Jensen,K., Will,H. and Hofmann,T.G.
  TITLE     FLASH links the CD95 signaling pathway to the cell nucleus and
            nuclear bodies
  JOURNAL   EMBO J 26 (2), 391-401 (2007)
   PUBMED   17245429
REFERENCE   9  (residues 1 to 1962)
  AUTHORS   Kino,T. and Chrousos,G.P.
  TITLE     Tumor necrosis factor alpha receptor- and Fas-associated FLASH
            inhibit transcriptional activity of the glucocorticoid receptor by
            binding to and interfering with its interaction with p160 type
            nuclear receptor coactivators
  JOURNAL   J Biol Chem 278 (5), 3023-3029 (2003)
   PUBMED   12477726
REFERENCE   10 (residues 1 to 1962)
  AUTHORS   Imai,Y., Kimura,T., Murakami,A., Yajima,N., Sakamaki,K. and
            Yonehara,S.
  TITLE     The CED-4-homologous protein FLASH is involved in Fas-mediated
            activation of caspase-8 during apoptosis
  JOURNAL   Nature 398 (6730), 777-785 (1999)
   PUBMED   10235259
  REMARK    Erratum:[Nature 1999 Jul 1;400(6739):89]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001063464.1, XP_232860.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760400,
                              SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1962
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..1962
                     /product="CASP8-associated protein 2"
                     /calculated_mol_wt=219560
     Region          <70..142
                     /region_name="ADIP"
                     /note="Afadin- and alpha -actinin-Binding; pfam11559"
                     /db_xref="CDD:463295"
     Region          1896..1960
                     /region_name="CASP8AP2"
                     /note="Caspase 8-associated protein 2 myb-like domain;
                     cd12202"
                     /db_xref="CDD:213401"
     CDS             1..1962
                     /gene="Casp8ap2"
                     /coded_by="NM_001107921.2:310..6198"
                     /db_xref="GeneID:313128"
                     /db_xref="RGD:1305771"
ORIGIN      
        1 maadddngdg tglfdvcpas plknndegsl diyagldstv sdstarscvs frncldlyee
       61 ilteegtake atysdlqiey gkcqqqmkdl mkrfkeiqtq nlnlknenqs lkknisalik
      121 tarveinrkd eeinhlhqrl sefphfrnnh ktartkdsrs ksphldncsk tdhgvksdvq
      181 kdihpntsqp nlekegkshs eaqnslhlst giekhctnnv wsrspyqvse gnsnednrrg
      241 rngvrhsqgs rgtdrtqkdl nsscndgepr dkeaasrlhg npekhgssea raenkiseik
      301 sstglgnkse rsassweket srerphtrve pqndknlerq nerlqnthrk elqsqdkaer
      361 kgdvkfkpag eeqghrgrvd ralpphsknd mkyygfnkyh peerrgredg krdrgmsshg
      421 fqdrrcsssl ssnrnskyph skevsvahqw entpfkaerh rtedrrkrer enkeesrhvk
      481 sdkksppehl qrthkdtkks tangkrqteq khgkgpvsts elskgtdnre ctmkvengpn
      541 eakgkdlkls fmeklnltls pakkqpvcqd nehqiigvpk psgvcdsqsl ektetvaclp
      601 svseqdreep kselpepkea lsatsqprts ipenkvkeen rllfksvent vpcellacgt
      661 eisfpapvei eqarclvqsm eveetcagar aaasvvmrvl pehasedfsq elgtkrhddi
      721 nscdiseggk kkvvlspkaa aaseshlepv veepsispvn csgdnnpkle psleerpkve
      781 nkssplepcl pkemfvpspq ktelidhkid tgesnsvyqd ddnsvlsidf nnlrpipepi
      841 splnspvrpv skvlsmessc tiplydsshk defpsnstls tfksqsdlnk enekpvpkld
      901 kcseaesckn lsvdeleege irsddeesva qkrleksarp rtstevppgk ispgsrrstv
      961 hvhkdngrtv vklprdritw sqrsnesrps nterksktms isslekilpl ilapssvwev
     1021 mhmlrllgkh vrknymkfki kfsltqfhri iesailsfts liryldlski cksvstlqks
     1081 lcdviesnlk qvkkngivdr lfeqqqtdmk kklwkfvdeq ldylfeklkk illkfcdsvk
     1141 hendssegkl gkkykeraqh sncqkkkmdn keirrekvlk sentvnfkss lgcekfeekh
     1201 qdqnktnttt vkhdvkrtfs tctdnntkns eckeqflgmn cpstprpget egnveegtpa
     1261 aqhacvkser gfeilteqqa ssltfnlvsd aqmgeifksl lqgsdlldtg gtekaewelk
     1321 tpekqllesl kcesapactt eelvseaasl cpkvisddnw sllssekgps lssglslpvh
     1381 pdvldencmf evssnlalsk dnvysseksk pcissilled lavsltvpsp lksdghlsfl
     1441 kpevlststp eevisahfse dalleeedas eqdihlales dnsssksscs swtsrsvasg
     1501 fqyhpnlpmh avimeksndh fivkirratp stspglkhgm vaeesltplp rtgkeadgaa
     1561 ekeptlfqst vlnpvqdlen sdksidkskp thedqnsivq tqvpdiyefl kdasnkvvhc
     1621 dqvvddcfkl hqvwepkvse slqelpsmek nahsvddhlp nthidltkdp atetkslelm
     1681 dvtvldidhl ehskpnldqd aqitctslqh davdafidlt hdvsneskne snepvltveg
     1741 vgcqvicidd dnhkegkvgk vnsslectve etcidltses agsfevkrht lkseppsksd
     1801 clelpetlgn ghkkrknspa vshssqkkqr kdmdlssekt krlspnsdrt gdahrkhgsk
     1861 krepavsdts lssevnpevk gstaplatfp gslsaknvik kkgeiivswt rnddreille
     1921 cqkrmpslkt fthlavklnk npnqvserfq qlkklfeksk cr
//
LOCUS       NP_001423661             326 aa            linear   ROD 20-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423661 XP_006239234
VERSION     NP_001423661.1
DBSOURCE    REFSEQ: accession NM_001436732.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006239234.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.31168.1,
                                           SRR26360181.2822609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..326
                     /product="F-actin-capping protein subunit beta isoform 2"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=36497
     Region          65..293
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..326
                     /gene="Capzb"
                     /coded_by="NM_001436732.1:10..990"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 mmhpsrrslp fplncqlvrv gtadyggaad qtmcinqveq segftwqdgr semnssdqql
       61 dcaldlmrrl ppqqieknls dlidlvpslc edllssvdqp lkiardkvvg kdyllcdynr
      121 dgdsyrspws nkydppledg ampsarlrkl eveannafdq yrdlyfeggv ssvylwdldh
      181 gfagvilikk agdgskkikg cwdsihvvev qekssgrtah ykltstvmlw lqtnksgsgt
      241 mnlggsltrq mekdetvsdc sphianigrl vedmenkirs tlneiyfgkt kdivnglrsv
      301 qtfadkskqe alkndlveal krkqqc
//
LOCUS       NP_001423663             296 aa            linear   ROD 20-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423663
VERSION     NP_001423663.1
DBSOURCE    REFSEQ: accession NM_001436734.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.768614.1,
                                           SRR26360181.506442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..296
                     /product="F-actin-capping protein subunit beta isoform 4"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=33258
     Region          35..263
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..296
                     /gene="Capzb"
                     /coded_by="NM_001436734.1:100..990"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 mtmcinqveq segftwqdgr semnssdqql dcaldlmrrl ppqqieknls dlidlvpslc
       61 edllssvdqp lkiardkvvg kdyllcdynr dgdsyrspws nkydppledg ampsarlrkl
      121 eveannafdq yrdlyfeggv ssvylwdldh gfagvilikk agdgskkikg cwdsihvvev
      181 qekssgrtah ykltstvmlw lqtnksgsgt mnlggsltrq mekdetvsdc sphianigrl
      241 vedmenkirs tlneiyfgkt kdivnglrsv qtfadkskqe alkndlveal krkqqc
//
LOCUS       NP_001423677             551 aa            linear   ROD 20-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423677 XP_006252637
VERSION     NP_001423677.1
DBSOURCE    REFSEQ: accession NM_001436748.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006252637.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.57974.1,
                                           SRR26643297.46191.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..551
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     1"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=63041
     Region          152..328
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          342..474
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..551
                     /gene="Arhgef3"
                     /coded_by="NM_001436748.1:353..2008"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mnqciyrgme ehkerpkrpr qnnfsmfpsp kawnfrgrkr kqsaqdedav slcsldisep
       61 snkrvkplsr vtslanlipp vkttplkrfs qtlqrsisfr nesrpdilap rawsrnatss
      121 stkrrdsklw setfdvcvsq vltakeikrq eaifelsqge edliedlkla kkayhdpmlk
      181 lsimteqeln qifgtldsli plhedllsql rdvrkpdgst ehvgpilvgw lpclssydsy
      241 csnqvaakal ldhkkqdhrv qdflqrcles pfsrkldlwn fldiprsrlv kyplllreil
      301 rhtpndnpdq qhleeainii qgivaeintk tgesecryyk erllyleegq kdslidssrv
      361 lcchgelknn rgvklhvflf qevlvitrav thneqlcyql yrqpipvkdl tledlqdgev
      421 rlggslrgaf snneriknff rvsfkngsqs qthslqandt fnkqqwlnci rqaketvlsa
      481 agqaglldse slsqspgten relrgetkle qmdqsdsesd csmdtsevsl ecermeqtda
      541 scansrpeen v
//
LOCUS       NP_001423687             329 aa            linear   ROD 20-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform a
            [Rattus norvegicus].
ACCESSION   NP_001423687 XP_038965687
VERSION     NP_001423687.1
DBSOURCE    REFSEQ: accession NM_001436758.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_038965687.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.902109.1,
                                           SRR26643299.21872.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680435,
                                           SAMN06680443 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..329
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform a"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=37665
     Region          103..309
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..329
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001436758.1:306..1295"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaektknav
      301 qalidkhqri pgnirsalld rfhkeqkan
//
LOCUS       NP_001101373             329 aa            linear   ROD 20-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform a
            [Rattus norvegicus].
ACCESSION   NP_001101373 XP_001068973 XP_232647
VERSION     NP_001101373.1
DBSOURCE    REFSEQ: accession NM_001107903.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232647.3, XP_001068973.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360190.2104970.1, SRR26643299.21876.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMN12840105,
                                    SAMN12840106 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..329
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform a"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=37665
     Region          103..309
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..329
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001107903.2:227..1216"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaektknav
      301 qalidkhqri pgnirsalld rfhkeqkan
//
LOCUS       NP_001101385            1862 aa            linear   ROD 20-MAR-2025
DEFINITION  protein virilizer homolog isoform 2 [Rattus norvegicus].
ACCESSION   NP_001101385 XP_001053130 XP_001053205 XP_232783
VERSION     NP_001101385.1
DBSOURCE    REFSEQ: accession NM_001107915.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1862)
  AUTHORS   Hong,H., Xu,G., Bao,G., Zhang,J., Chen,C., Chen,J., Wu,C.,
            Jiang,J., Huang,J., Huang,H. and Cui,Z.
  TITLE     VIRMA promotes neuron apoptosis via inducing m6A methylation of
            STK10 in spinal cord injury animal models
  JOURNAL   CNS Neurosci Ther 30 (3), e14453 (2024)
   PUBMED   37721438
  REMARK    GeneRIF: VIRMA promotes neuron apoptosis via inducing m6A
            methylation of STK10 in spinal cord injury animal models.
REFERENCE   2  (residues 1 to 1862)
  AUTHORS   Wen,J., Lv,R., Ma,H., Shen,H., He,C., Wang,J., Jiao,F., Liu,H.,
            Yang,P., Tan,L., Lan,F., Shi,Y.G., He,C., Shi,Y. and Diao,J.
  TITLE     Zc3h13 Regulates Nuclear RNA m6A Methylation and Mouse Embryonic
            Stem Cell Self-Renewal
  JOURNAL   Mol Cell 69 (6), 1028-1038 (2018)
   PUBMED   29547716
REFERENCE   3  (residues 1 to 1862)
  AUTHORS   Yue,Y., Liu,J., Cui,X., Cao,J., Luo,G., Zhang,Z., Cheng,T., Gao,M.,
            Shu,X., Ma,H., Wang,F., Wang,X., Shen,B., Wang,Y., Feng,X., He,C.
            and Liu,J.
  TITLE     VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near
            stop codon and associates with alternative polyadenylation
  JOURNAL   Cell Discov 4, 10 (2018)
   PUBMED   29507755
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1862)
  AUTHORS   Schwartz,S., Mumbach,M.R., Jovanovic,M., Wang,T., Maciag,K.,
            Bushkin,G.G., Mertins,P., Ter-Ovanesyan,D., Habib,N.,
            Cacchiarelli,D., Sanjana,N.E., Freinkman,E., Pacold,M.E.,
            Satija,R., Mikkelsen,T.S., Hacohen,N., Zhang,F., Carr,S.A.,
            Lander,E.S. and Regev,A.
  TITLE     Perturbation of m6A writers reveals two distinct classes of mRNA
            methylation at internal and 5' sites
  JOURNAL   Cell Rep 8 (1), 284-296 (2014)
   PUBMED   24981863
REFERENCE   5  (residues 1 to 1862)
  AUTHORS   Horiuchi,K., Kawamura,T., Iwanari,H., Ohashi,R., Naito,M.,
            Kodama,T. and Hamakubo,T.
  TITLE     Identification of Wilms' tumor 1-associating protein complex and
            its role in alternative splicing and the cell cycle
  JOURNAL   J Biol Chem 288 (46), 33292-33302 (2013)
   PUBMED   24100041
REFERENCE   6  (residues 1 to 1862)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001053130.1, XP_232783.4, XP_001053205.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1862
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..1862
                     /product="protein virilizer homolog isoform 2"
                     /calculated_mol_wt=206776
     Region          5..235
                     /region_name="VIR_N"
                     /note="Virilizer, N-terminal; pfam15912"
                     /db_xref="CDD:464938"
     CDS             1..1862
                     /gene="Virma"
                     /gene_synonym="RGD1559904"
                     /coded_by="NM_001107915.2:25..5613"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:313061"
                     /db_xref="RGD:1559904"
ORIGIN      
        1 mavdssmell fldtfkhpsa eqsshidvvr fpcvvyinev rvippgvrah sglpdnrayg
       61 etsphtfqld lffnnvskps apvfdrlgsl eydentsiif rpnskvntdg lvlrgwyncl
      121 tlaiygsvdr vlshdrdspp pppppppppq pqptlkrslk hadgekedqf ngspprpqpr
      181 gprtppgppp pdddeddpms lpvsgdkeed vphredyfep ispdrnsvpq egqysdegev
      241 eeeqqeeged deddvdvdee edededdcht vdsipdddee deeeegeede egegddgyeq
      301 issdedgiad leretfkypn fdveytpedl asvppmtydp ydrelvplly fscpykttfe
      361 ieinrmkdqg pdkensgaie aslkltelld lyhedrgakw vtaleevpsl iikglsylql
      421 kntkqdslgq lvdwtmqaln lqvafrqpia lnvrqlkagt klvtslaecg apgvtellqa
      481 gvisvlfdll fadhvssslk lnafkaldsv ismtegmeaf lrstqseksg yqkllelill
      541 dqtvrvvtag sailqkchfy evlseikrlg dhiaektssv pnpsepdhdt davleranpd
      601 yeneveasmd mdllessnis egeieklinl leevfhlmet aphtmiqppv ksfptiarit
      661 gpperddpyp vlfrgpgfgf ehsnsglqps atpvpdgpma ssglcghcth mvhrhtckqn
      721 thnirylhsh hflelvtlll sipitsahpg vlqatkdvlk flaqsqkgll ffmseyeatn
      781 lliralchly dqdeeeglqs dgvddafalw lqdstqtlqc vtelfshfqr ctaseetdhs
      841 dllgtlhnly litfnpvgrs avghvfsldk nlqslitlme yyskealgds kskksvayny
      901 acililvvvq sssdvqmleq haasllklck adennaklqe lgkwleplkn lrfeincipn
      961 lieyvkqnid nlmtaegvgl ttalrvlcnv acppppvegq qkdlkwnlav iqlfsaegmd
     1021 tfirvlqkln siltqpwrlh vnmgttlhrv ttismarctl tllktmltel lrggsfefkd
     1081 mrvpsalvtl hmllcsipls grldsdeqki qndiidillt ftqgvneklt iseetlannt
     1141 wslmlkevls silkvpegff sglillsell plplpmqttq viephdisva lntrklwsmh
     1201 lhvqakllqe ivrsfsgttc qpiqhmlrri cvqlcdlasp tallimrtvl dlivedlqst
     1261 sedkekqyts qttrllalld alashkackl ailhlingti kgdekyaeif qdllalvrsp
     1321 gdsvirqqcv eyvtsilqsl cdqdialilp spsegpgsel eqlsnslpsk elmaaicdcl
     1381 latlansest ynclltcvrt mmflaehdyg lfhlksslrk nssalhsllk rvvstfskdt
     1441 geltsasldf mrqilnsdam gccgddsglm evesahpprt msinaaelkq llqskeespe
     1501 slfleleklv lehskeddsl eslldnvigl kqmlessgdp lplsdqdvep vlsapeslqn
     1561 lfnnrtayvl advmddqlks mwftpfqaee idtdldlvkv dlielsekcc sdfdlhsele
     1621 rsflsepssp grakttkgfk lgkhkhetfi tssgkseyie pakrahvvpp prgrgrggfg
     1681 qgirphdifr qrkqntsrpp smhvddfvaa eskevvpqdg ipppkrplkv sqkissrggf
     1741 sgnrggrgaf hsqnrfftpp askgnysrre gtrgsswsaq ntprgnynes rggqsnfnrg
     1801 plpplrplss tgyrpsprdr asrgrgglgp swastnsgsg gsrgkfvsgg sgrgrhvrsf
     1861 tr
//
LOCUS       NP_001127995             615 aa            linear   ROD 20-MAR-2025
DEFINITION  pleckstrin homology domain-containing family N member 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001127995 XP_001078287 XP_238442
VERSION     NP_001127995.1
DBSOURCE    REFSEQ: accession NM_001134523.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Kuriyama,S., Tsuji,T., Sakuma,T., Yamamoto,T. and Tanaka,M.
  TITLE     PLEKHN1 promotes apoptosis by enhancing Bax-Bak
            hetro-oligomerization through interaction with Bid in human colon
            cancer
  JOURNAL   Cell Death Discov 4, 11 (2018)
   PUBMED   29531808
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Maeda,A., Uchida,M., Nishikawa,S., Nishino,T. and Konishi,H.
  TITLE     Role of N-myristoylation in stability and subcellular localization
            of the CLPABP protein
  JOURNAL   Biochem Biophys Res Commun 495 (1), 1249-1256 (2018)
   PUBMED   29180010
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Nishino,T., Matsunaga,R., Jikihara,H., Uchida,M., Maeda,A., Qi,G.,
            Abe,T., Kiyonari,H., Tashiro,S., Inagaki-Ohara,K., Shimamoto,F. and
            Konishi,H.
  TITLE     Antagonizing effect of CLPABP on the function of HuR as a regulator
            of ARE-containing leptin mRNA stability and the effect of its
            depletion on obesity in old male mouse
  JOURNAL   Biochim Biophys Acta 1861 (11), 1816-1827 (2016)
   PUBMED   27616329
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Sano,E., Shono,S., Tashiro,K., Konishi,H., Yamauchi,E. and
            Taniguchi,H.
  TITLE     Novel tyrosine phosphorylated and cardiolipin-binding protein
            CLPABP functions as mitochondrial RNA granule
  JOURNAL   Biochim Biophys Acta 1783 (6), 1036-1047 (2008)
   PUBMED   18191643
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_238442.4, XP_001078287.1.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..615
                     /product="pleckstrin homology domain-containing family N
                     member 1 isoform 2"
                     /note="pleckstrin homology domain containing, family N
                     member 1"
                     /calculated_mol_wt=67611
     Region          96..188
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          222..341
                     /region_name="PH_PLEKHN1"
                     /note="Pleckstrin homology domain containing family N
                     member 1Pleckstrin homology-like domain; cd13323"
                     /db_xref="CDD:270132"
     CDS             1..615
                     /gene="Plekhn1"
                     /gene_synonym="RGD1311019"
                     /coded_by="NM_001134523.2:43..1890"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298694"
                     /db_xref="RGD:1311019"
ORIGIN      
        1 mgnshcvpqt prrlrasfsr kpslkgnred sarklaglfg tearpdgdta ankifhyipg
       61 tdilgpenhp enleqpflsv fkkgwrrtpv rnlgkvvhys kvqlrfqhsq disdcylelf
      121 pshlyfqahg segltfqgll pltelsicpi dgsrehafqi tgplpapllv lchseaelsh
      181 wlyhlekqma llglrqchsa ppqgslgdkl pwtqlwrahg cepmnsaica srvklqhlps
      241 qeqwdrllvl ypaslaifse epeglnfkge lplsaihinl eekekeirsf liegrlinti
      301 rvvcasyedy sqwllclrtv shrdgahllp gpesfpglqr ptqvlgrgrg slssngrtsr
      361 klecpvfpts qslpepsvpt tigvpahpvp nqtnsncvst gqtkvelrhs gssqfprgka
      421 qrevsgstap lplhldltkm svlnldsgpe aqdcspdiph splyadpytp paiahhkitd
      481 iqgldeflca vqtspgpels spfpsvsvsv pvsdsnsgis ssprplgshl lskkgalqsr
      541 asqrhrgsik srapqpsdfp qlgkgsyfln lmpessltpl ldeeapiwnk tsspshqkws
      601 hprkpavegg fiqwi
//
LOCUS       NP_001099381             523 aa            linear   ROD 20-MAR-2025
DEFINITION  equilibrative nucleoside transporter 4 [Rattus norvegicus].
ACCESSION   NP_001099381 XP_001072979 XP_038945113 XP_221940
VERSION     NP_001099381.2
DBSOURCE    REFSEQ: accession NM_001105911.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Usui,T., Nakazawa,A., Okura,T., Deguchi,Y., Akanuma,S.I., Kubo,Y.
            and Hosoya,K.I.
  TITLE     Histamine elimination from the cerebrospinal fluid across the
            blood-cerebrospinal fluid barrier: involvement of plasma membrane
            monoamine transporter (PMAT/SLC29A4)
  JOURNAL   J Neurochem 139 (3), 408-418 (2016)
   PUBMED   27501284
  REMARK    GeneRIF: These results suggest the elimination of histamine from
            the CSF via plasma membrane monoamine transporter at the
            blood-brain barrier and blood-CSF barrier
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Wu,K.C., Lu,Y.H., Peng,Y.H., Hsu,L.C. and Lin,C.J.
  TITLE     Effects of lipopolysaccharide on the expression of plasma membrane
            monoamine transporter (PMAT) at the blood-brain barrier and its
            implications to the transport of neurotoxins
  JOURNAL   J Neurochem 135 (6), 1178-1188 (2015)
   PUBMED   26376205
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Gong,L., Goswami,S., Giacomini,K.M., Altman,R.B. and Klein,T.E.
  TITLE     Metformin pathways: pharmacokinetics and pharmacodynamics
  JOURNAL   Pharmacogenet Genomics 22 (11), 820-827 (2012)
   PUBMED   22722338
  REMARK    Review article
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Okura,T., Kato,S., Takano,Y., Sato,T., Yamashita,A., Morimoto,R.,
            Ohtsuki,S., Terasaki,T. and Deguchi,Y.
  TITLE     Functional characterization of rat plasma membrane monoamine
            transporter in the blood-brain and blood-cerebrospinal fluid
            barriers
  JOURNAL   J Pharm Sci 100 (9), 3924-3938 (2011)
   PUBMED   21538354
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Duan,H. and Wang,J.
  TITLE     Selective transport of monoamine neurotransmitters by human plasma
            membrane monoamine transporter and organic cation transporter 3
  JOURNAL   J Pharmacol Exp Ther 335 (3), 743-753 (2010)
   PUBMED   20858707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Mar 13, 2025 this sequence version replaced
            XP_038945113.1, NP_001099381.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.49693.1,
                                           SRR26643298.79705.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..523
                     /product="equilibrative nucleoside transporter 4"
                     /note="solute carrier family 29 (nucleoside transporters),
                     member 4; solute carrier family 29 (equilibrative
                     nucleoside transporter), member 4"
                     /calculated_mol_wt=57590
     Region          73..496
                     /region_name="Nucleoside_tran"
                     /note="Nucleoside transporter; cl15430"
                     /db_xref="CDD:472807"
     CDS             1..523
                     /gene="Slc29a4"
                     /coded_by="NM_001105911.2:195..1766"
                     /db_xref="GeneID:288499"
                     /db_xref="RGD:1310545"
ORIGIN      
        1 mgsigsqrlk epcvaatsgq svvtsfdnfq lettiegaqd pgirvrgvpp ftdsavdepv
       61 pddryhaiyf amllagvgfl lpynsfitdv dylhhkypgt sivfdmslty ilvalaavll
      121 nnvvverlnl htrittgyll algpllfisi fdvwlqlfsh dqayainlaa vgtvafgctv
      181 qqssfygytg llpkrytqgv mtgestagvm islsriltkl llpderasti ifflvsagle
      241 llcfllhllv rrsrfvlyyt trprdsrpvr agyrvhhdva sgdihfehqt palsssrspk
      301 dspahevths nsgvymrfdv prprvkrswp tfralllhry vvarviwadm lsiavtyfit
      361 lclfpglese irhcvlgewl pilvmavfnl sdfvgkilaa lpvdwrgthl lacsclrvvf
      421 iplfilcvyp tgmpalrhpa wpcvfsllmg isngyfgsvp milaagkvsp kqrelagntm
      481 tvsymsgltl gsavayctys ltrdahsscf qtatandsil vgp
//
LOCUS       NP_001423564             751 aa            linear   ROD 20-MAR-2025
DEFINITION  myb-related protein A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423564 XP_006237811
VERSION     NP_001423564.1
DBSOURCE    REFSEQ: accession NM_001436635.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Zhang,D., Xie,D., Lin,X., Ma,L., Chen,J., Zhang,D., Wang,Y.,
            Duo,S., Feng,Y., Zheng,C., Jiang,B., Ning,Y. and Han,C.
  TITLE     The transcription factor SOX30 is a key regulator of mouse
            spermiogenesis
  JOURNAL   Development 145 (11) (2018)
   PUBMED   29848638
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Li,X.Z., Roy,C.K., Dong,X., Bolcun-Filas,E., Wang,J., Han,B.W.,
            Xu,J., Moore,M.J., Schimenti,J.C., Weng,Z. and Zamore,P.D.
  TITLE     An ancient transcription factor initiates the burst of piRNA
            production during early meiosis in mouse testes
  JOURNAL   Mol Cell 50 (1), 67-81 (2013)
   PUBMED   23523368
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Bolcun-Filas,E., Bannister,L.A., Barash,A., Schimenti,K.J.,
            Hartford,S.A., Eppig,J.J., Handel,M.A., Shen,L. and Schimenti,J.C.
  TITLE     A-MYB (MYBL1) transcription factor is a master regulator of male
            meiosis
  JOURNAL   Development 138 (15), 3319-3330 (2011)
   PUBMED   21750041
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Ma,X.P. and Calabretta,B.
  TITLE     DNA binding and transactivation activity of A-myb, a c-myb-related
            gene
  JOURNAL   Cancer Res 54 (24), 6512-6516 (1994)
   PUBMED   7987850
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1781605.1,
                                           SRR21887620.567824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..751
                     /product="myb-related protein A isoform 1"
                     /note="myb-related protein A; myeloblastosis oncogene-like
                     1"
                     /calculated_mol_wt=85320
     Region          38..98
                     /region_name="Myb_DNA-bind_6"
                     /note="Myb-like DNA-binding domain; pfam13921"
                     /db_xref="CDD:372817"
     Site            order(38,68..69,71..72,74..76,78..80)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          84..>192
                     /region_name="PLN03091"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:215570"
     Region          240..285
                     /region_name="LMSTEN"
                     /note="LMSTEN motif; pfam07988"
                     /db_xref="CDD:462332"
     Region          485..641
                     /region_name="Cmyb_C"
                     /note="C-myb, C-terminal; pfam09316"
                     /db_xref="CDD:462753"
     CDS             1..751
                     /gene="Mybl1"
                     /coded_by="NM_001436635.1:372..2627"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:297783"
                     /db_xref="RGD:1306940"
ORIGIN      
        1 makrsrsede dddlqyadhd yevpqqkglk klwnrvkwtr deddklkklv eqhgtddwtl
       61 iashlqnrsd fqcqhrwqkv lnpelikgpw tkeedqrvie lvqkygpkrw sliakhlkgr
      121 igkqcrerwh nhlnpevkks swteeedrii yeahkrlgnr waeiakllpg rtdnsiknhw
      181 nstmrrkveq egylqdgiks ersssklqhk pcatmdhlqt qnqfyipvqi pgyqyvspdg
      241 ncvehvqtsa fiqqpfvded pdkekkikel elllmsaene vrrkrlppqp gsfsswsgsf
      301 lmddsmsntl nnleehttef ysmdenqtvs aqqnsptkfl aveanavlss lqtipefaet
      361 leliesdpva wsdvtsfdls daaaspvkst pvklmriqhn egamecqfnv slvlegkkns
      421 cnggdseaip laspnvvkfs tpptilrkkk rlrvgqsags elgegslseg nnaalkhtpv
      481 ktlpfspsqf fntcpgseql nienpsftst picgqkvlit tplqkeatpk dqkenvgfrt
      541 ptirrsilgt tprtptpfkn alaaqekkyg plkivsqpla fleedirevl keetgtdifl
      601 keedepayks ckqehsasvk kvrkslales wdkeepgtql ltedisdmqs enilttsllm
      661 iplleihdnr cnltpekqdi nsanktytlt kkrpnpntck avklekslqs ncewetvvyg
      721 ktedqlimte qarrylstyt apsstsrali l
//
LOCUS       NP_001423572            1162 aa            linear   ROD 20-MAR-2025
DEFINITION  cartilage intermediate layer protein 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001423572 XP_006252964
VERSION     NP_001423572.1
DBSOURCE    REFSEQ: accession NM_001436643.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Johnson,K., Farley,D., Hu,S.I. and Terkeltaub,R.
  TITLE     One of two chondrocyte-expressed isoforms of cartilage
            intermediate-layer protein functions as an insulin-like growth
            factor 1 antagonist
  JOURNAL   Arthritis Rheum 48 (5), 1302-1314 (2003)
   PUBMED   12746903
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006252964.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06621351,
                              SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..1162
                     /product="cartilage intermediate layer protein 2
                     precursor"
                     /calculated_mol_wt=124251
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2012
     Region          59..143
                     /region_name="Mucin2_WxxW"
                     /note="Mucin-2 protein WxxW repeating region; pfam13330"
                     /db_xref="CDD:463846"
     Region          158..197
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          213..287
                     /region_name="CarboxypepD_reg"
                     /note="Carboxypeptidase regulatory-like domain; pfam13620"
                     /db_xref="CDD:433354"
     Region          292..364
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     CDS             1..1162
                     /gene="Cilp2"
                     /coded_by="NM_001436643.1:42..3530"
                     /db_xref="GeneID:306356"
                     /db_xref="RGD:1311157"
ORIGIN      
        1 mssplpllyl ciaaahlaga rdatpteeht atvrglqgrp pdpgqpspal edweeasewt
       61 swfnvdhpgg dgdfeslaai rfyygparvc prplaleart tdwalpaaig ervhanperg
      121 fwclnreqpr grrcsnyhvr frcpleaawg awgawglcsk scgpgrrlrr rscqsssgdt
      181 cpgspqeaqk cvrsrcpgcs sdtcgcpnhi llgsvvtpsg rplsgarvsl rtrpgtvats
      241 dthgtfrvpg vcagskanvs armngfstgt aqahantsns avvtivleel gkpylvkhpe
      301 srvreagqnv tfcckasgtp mpkkyswfhn gtlldrrqqg sgphlelqgl reeqageyhc
      361 kawneagtvr sraahltvla pgqpacdprp qehliklpdd cgqpgggpty ldvglcadtr
      421 cpgpvgsgpr cgdagsrccs vlrlesrdir csgyvlpvkv vaecgcrkcl prrglvrgrv
      481 vaadsgeplr farillglap igftsyqgdf tievppater lvvtfvdssg efvdsirvlp
      541 fdprgagvyh eirvlrkaaa vlldaeqgge iplggteeap algelvfppr tfhhpdgrpy
      601 sgpvearvtf vdprdlasaa aassdlryld ssgelaplrt ygmfavdlha pgsteqlhva
      661 radvrvdadh vrmpghadal alwsldpetg lweeegaeqg gggfrrekea vrvrreertf
      721 lvgaltvrer rlfnldvper rrcfvkvray gtdrfapseq vqgvvvtlln lepapgftan
      781 prawgrfdsa vtgpngacvp afcdaerpda ytafvtaslg geeleaapsr prataatvgv
      841 aepylerlgy qrtdhddpal krtgfrlnla rprtghesea hgpvypwrrl rdcedapvtd
      901 shfrfsrvea dkyeydvvpf hegapaswtg dllawwpnpq efracflkvr lqgpqeymvr
      961 shnaggthed trghlyglrd trsvrnperp gasaacvefk cggmlfdqrq vdrtlvtvtp
     1021 qgscrrvavn tllqdylarh pplapaddpa tfamlaplda lghnygvytv tdqsprlake
     1081 iaigrcfdgs sdgfsremka dagtavtfqc repparpslf qrllenpasa lgdirremgq
     1141 aardsrvtqt qagdtgpfgs gq
//
LOCUS       NP_001423533             329 aa            linear   ROD 20-MAR-2025
DEFINITION  aprataxin isoform a [Rattus norvegicus].
ACCESSION   NP_001423533 XP_006238089
VERSION     NP_001423533.1
DBSOURCE    REFSEQ: accession NM_001436604.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Castellotti,B., Mariotti,C., Rimoldi,M., Fancellu,R., Plumari,M.,
            Caimi,S., Uziel,G., Nardocci,N., Moroni,I., Zorzi,G., Pareyson,D.,
            Di Bella,D., Di Donato,S., Taroni,F. and Gellera,C.
  TITLE     Ataxia with oculomotor apraxia type1 (AOA1): novel and recurrent
            aprataxin mutations, coenzyme Q10 analyses, and clinical findings
            in Italian patients
  JOURNAL   Neurogenetics 12 (3), 193-201 (2011)
   PUBMED   21465257
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Becherel,O.J., Jakob,B., Cherry,A.L., Gueven,N., Fusser,M.,
            Kijas,A.W., Peng,C., Katyal,S., McKinnon,P.J., Chen,J., Epe,B.,
            Smerdon,S.J., Taucher-Scholz,G. and Lavin,M.F.
  TITLE     CK2 phosphorylation-dependent interaction between aprataxin and
            MDC1 in the DNA damage response
  JOURNAL   Nucleic Acids Res 38 (5), 1489-1503 (2010)
   PUBMED   20008512
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Ferrarini,M., Squintani,G., Cavallaro,T., Ferrari,S., Rizzuto,N.
            and Fabrizi,G.M.
  TITLE     A novel mutation of aprataxin associated with ataxia ocular apraxia
            type 1: phenotypical and genotypical characterization
  JOURNAL   J Neurol Sci 260 (1-2), 219-224 (2007)
   PUBMED   17572444
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Takahashi,T., Tada,M., Igarashi,S., Koyama,A., Date,H.,
            Yokoseki,A., Shiga,A., Yoshida,Y., Tsuji,S., Nishizawa,M. and
            Onodera,O.
  TITLE     Aprataxin, causative gene product for EAOH/AOA1, repairs DNA
            single-strand breaks with damaged 3'-phosphate and
            3'-phosphoglycolate ends
  JOURNAL   Nucleic Acids Res 35 (11), 3797-3809 (2007)
   PUBMED   17519253
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Kijas,A.W., Harris,J.L., Harris,J.M. and Lavin,M.F.
  TITLE     Aprataxin forms a discrete branch in the HIT (histidine triad)
            superfamily of proteins with both DNA/RNA binding and nucleotide
            hydrolase activities
  JOURNAL   J Biol Chem 281 (20), 13939-13948 (2006)
   PUBMED   16547001
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gueven,N., Becherel,O.J., Kijas,A.W., Chen,P., Howe,O.,
            Rudolph,J.H., Gatti,R., Date,H., Onodera,O., Taucher-Scholz,G. and
            Lavin,M.F.
  TITLE     Aprataxin, a novel protein that protects against genotoxic stress
  JOURNAL   Hum Mol Genet 13 (10), 1081-1093 (2004)
   PUBMED   15044383
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Sano,Y., Date,H., Igarashi,S., Onodera,O., Oyake,M., Takahashi,T.,
            Hayashi,S., Morimatsu,M., Takahashi,H., Makifuchi,T., Fukuhara,N.
            and Tsuji,S.
  TITLE     Aprataxin, the causative protein for EAOH is a nuclear protein with
            a potential role as a DNA repair protein
  JOURNAL   Ann Neurol 55 (2), 241-249 (2004)
   PUBMED   14755728
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238089.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1721343.1,
                                           SRR21887623.365850.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..329
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="FHA-HIT; forkhead-associated domain histidine
                     triad-like protein"
                     /calculated_mol_wt=37589
     Region          1..95
                     /region_name="Interactions with ADPRT/PARP1 and NCL.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          2..101
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(27..28,40..41,43,63..64)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          106..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          111..115
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQC5; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          151..252
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            161
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          180..184
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            238
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          242..243
                     /region_name="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            order(245,247,249..251)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Region          245..249
                     /region_name="Histidine triad motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00464"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            247
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Site            249
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Site            264
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250|UniProtKB:Q7Z2E3; propagated from
                     UniProtKB/Swiss-Prot (Q8K4H4.1)"
     Region          270..327
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..329
                     /gene="Aptx"
                     /coded_by="NM_001436604.1:196..1185"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:259271"
                     /db_xref="RGD:628740"
ORIGIN      
        1 mrvcwlvrqd cwhqriklph leavvigrsp etkitdkkcs rqqvqlkaec nkryvnvkqm
       61 gvnptsidev vigkdremkl lpgqvlhmvn elypymvefe evaespnvtq rkrkrpdcds
      121 qemeaeagas psqcsvspkt gkhgaakees lghwsqglki smkdpkmqvy kddqvvvikd
      181 kypkarhhwl vlpwasissl kvvtsehlel lkhmhavgek viadftgssk lrfrlgyhai
      241 psmshvhlhv isqdfdspcl knkkhwnsfn teyflesqav ikmvqeagrv tvkdgtcell
      301 klplrchecq qllpsipqlk ehlrkhwgg
//
LOCUS       NP_001423573             309 aa            linear   ROD 20-MAR-2025
DEFINITION  epidermal retinol dehydrogenase 2 [Rattus norvegicus].
ACCESSION   NP_001423573 XP_006237898
VERSION     NP_001423573.1
DBSOURCE    REFSEQ: accession NM_001436644.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Takahashi,Y., Moiseyev,G., Farjo,K. and Ma,J.X.
  TITLE     Characterization of key residues and membrane association domains
            in retinol dehydrogenase 10
  JOURNAL   Biochem J 419 (1), 113-122 (2009)
   PUBMED   19102727
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Lee,S.A., Belyaeva,O.V. and Kedishvili,N.Y.
  TITLE     Biochemical characterization of human epidermal retinol
            dehydrogenase 2
  JOURNAL   Chem Biol Interact 178 (1-3), 182-187 (2009)
   PUBMED   18926804
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Markova,N.G., Pinkas-Sarafova,A. and Simon,M.
  TITLE     A metabolic enzyme of the short-chain dehydrogenase/reductase
            superfamily may moonlight in the nucleus as a repressor of promoter
            activity
  JOURNAL   J Invest Dermatol 126 (9), 2019-2031 (2006)
   PUBMED   16691198
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Matsuzaka,Y., Okamoto,K., Tsuji,H., Mabuchi,T., Ozawa,A., Tamiya,G.
            and Inoko,H.
  TITLE     Identification of the hRDH-E2 gene, a novel member of the SDR
            family, and its increased expression in psoriatic lesion
  JOURNAL   Biochem Biophys Res Commun 297 (5), 1171-1180 (2002)
   PUBMED   12372410
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237898.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20512.1,
                                           SRR26643294.20378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN17050766 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..309
                     /product="epidermal retinol dehydrogenase 2"
                     /EC_number="1.1.1.105"
                     /note="epidermal retinal dehydrogenase 2; retinal short
                     chain dehydrogenase reductase 2"
                     /calculated_mol_wt=34010
     Region          42..284
                     /region_name="17beta-HSDXI-like_SDR_c"
                     /note="human 17-beta-hydroxysteroid dehydrogenase XI-like,
                     classical (c) SDRs; cd05339"
                     /db_xref="CDD:187598"
     Site            order(47,49..52,71..73,97..99,125..127,148,175..177,190,
                     194,223..226,228..229)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187598"
     Site            order(102,106,138..139,142..143,146,150..151,154..155,158,
                     187..189,191..192,195..196,199..200,202..204,206..207,
                     229..231,273..274,277,281)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187598"
     Site            order(149,177,190,194)
                     /site_type="active"
                     /db_xref="CDD:187598"
     Site            order(158,161,204,207,213)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187598"
     CDS             1..309
                     /gene="Sdr16c5"
                     /gene_synonym="Rdhe2; RGD1565999"
                     /coded_by="NM_001436644.1:222..1151"
                     /db_xref="GeneID:297805"
                     /db_xref="RGD:1565999"
ORIGIN      
        1 mpcnlesakd llvflgksll sileallshv iskprknvag evvlitgags glgrllalqf
       61 arlgsvlvlw dvnketneet rqiaqeagai rvhaytcdcs qreevyrvad qvkkevgdvs
      121 ilinnagivt grkfldcpdd lmeksldvnf kahlwmykaf lpamiannhg hlvcisssag
      181 ligvnglsdy caskfaalgf aesmfvetla qkqrgiktti vcpffiktgm fegcttkcpn
      241 llpildpeya vrkivdailq eqlylympkf lyfimflksf lpiktgilia dylglfhvmd
      301 gftgqkkks
//
LOCUS       NP_001423327             319 aa            linear   ROD 20-MAR-2025
DEFINITION  C-X-C chemokine receptor type 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423327 XP_038936876
VERSION     NP_001423327.1
DBSOURCE    REFSEQ: accession NM_001436398.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Yi,H., Zhu,B., Zheng,C., Ying,Z. and Cheng,M.
  TITLE     CXCL13/CXCR5 promote chronic postsurgical pain and astrocyte
            activation in rats by targeting NLRP3
  JOURNAL   Neuroreport 35 (6), 406-412 (2024)
   PUBMED   38526919
  REMARK    GeneRIF: CXCL13/CXCR5 promote chronic postsurgical pain and
            astrocyte activation in rats by targeting NLRP3.
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Cao,J., Hu,C., Ding,Z., Chen,J., Liu,S. and Li,Q.
  TITLE     Mechanism of IRF5-regulated CXCL13/CXCR5 Signaling Axis in
            CCI-induced Neuropathic Pain in Rats
  JOURNAL   Curr Mol Med 24 (7), 940-949 (2024)
   PUBMED   37622691
  REMARK    GeneRIF: Mechanism of IRF5-regulated CXCL13/CXCR5 Signaling Axis in
            CCI-induced Neuropathic Pain in Rats.
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Wang,X., Sumida,H. and Cyster,J.G.
  TITLE     GPR18 is required for a normal CD8alphaalpha intestinal
            intraepithelial lymphocyte compartment
  JOURNAL   J Exp Med 211 (12), 2351-2359 (2014)
   PUBMED   25348153
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Vogel,K.U., Edelmann,S.L., Jeltsch,K.M., Bertossi,A., Heger,K.,
            Heinz,G.A., Zoller,J., Warth,S.C., Hoefig,K.P., Lohs,C., Neff,F.,
            Kremmer,E., Schick,J., Repsilber,D., Geerlof,A., Blum,H., Wurst,W.,
            Heikenwalder,M., Schmidt-Supprian,M. and Heissmeyer,V.
  TITLE     Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40
            costimulator mRNAs and control follicular helper T cell
            differentiation
  JOURNAL   Immunity 38 (4), 655-668 (2013)
   PUBMED   23583643
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Zhang,X., Bedigian,A.V., Wang,W. and Eggert,U.S.
  TITLE     G protein-coupled receptors participate in cytokinesis
  JOURNAL   Cytoskeleton (Hoboken) 69 (10), 810-818 (2012)
   PUBMED   22888021
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Luther,S.A., Ansel,K.M. and Cyster,J.G.
  TITLE     Overlapping roles of CXCL13, interleukin 7 receptor alpha, and CCR7
            ligands in lymph node development
  JOURNAL   J Exp Med 197 (9), 1191-1198 (2003)
   PUBMED   12732660
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Kouba,M., Vanetti,M., Wang,X., Schafer,M. and Hollt,V.
  TITLE     Cloning of a novel putative G-protein-coupled receptor (NLR) which
            is expressed in neuronal and lymphatic tissue
  JOURNAL   FEBS Lett 321 (2-3), 173-178 (1993)
   PUBMED   8386678
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced XP_038936876.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2118127.1,
                                           SRR26643293.44883.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..319
                     /product="C-X-C chemokine receptor type 5 isoform 2"
                     /note="chemokine (C-X-C motif) receptor 5; C-X-C chemokine
                     receptor type 5; CXC-R5; CXCR-5; neurolymphatic receptor;
                     burkitt lymphoma receptor 1 homolog; chemochine (C-X-C
                     motif) receptor 5"
                     /calculated_mol_wt=35730
     Region          1..280
                     /region_name="7tmA_CXCR5"
                     /note="CXC chemokine receptor type 5, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15181"
                     /db_xref="CDD:341336"
     Region          1..26
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341336"
     Site            order(5,54,57,73,76..77,149..154,162,165..166,222,229,232,
                     244,248,251..252,255)
                     /site_type="other"
                     /note="putative chemokine binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341336"
     Region          33..58
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341336"
     Region          69..99
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341336"
     Region          111..133
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341336"
     Region          162..191
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341336"
     Region          199..229
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341336"
     Region          248..273
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341336"
     CDS             1..319
                     /gene="Cxcr5"
                     /gene_synonym="Blr1; NLR"
                     /coded_by="NM_001436398.1:311..1270"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29363"
                     /db_xref="RGD:62010"
ORIGIN      
        1 mpvayslifl lgmmgnilvl vilerhrhtr sstetflfhl avadlllvfi lpfavaegsv
       61 gwvlgtflck tvialhkinf ycsslllaci avdrylaivh avhayrrrrl lsihitcsti
      121 wlagflfalp ellfakvvqp hnneslpqci fsqeneaetr awfasrflyh tggfllpmlv
      181 mawcyvgvvh rllqaqrrpq rqkavrvail vtsifllcws pyhivifldt lerlkavnss
      241 celsgylsva itlceflgla hcclnpmlyt fagvkfrsdl srlltklgca gpaslcqlfp
      301 gwrksslses enatslttf
//
LOCUS       NP_001423569             499 aa            linear   ROD 20-MAR-2025
DEFINITION  zinc finger protein PLAG1 isoform a [Rattus norvegicus].
ACCESSION   NP_001423569 XP_008761747
VERSION     NP_001423569.1
DBSOURCE    REFSEQ: accession NM_001436640.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gu,Q. and Wei,H.F.
  TITLE     PLAG1 Promotes High Glucose-Induced Angiogenesis and Migration of
            Retinal Endothelial Cells by Regulating the Wnt/beta-Catenin
            Signalling Pathway
  JOURNAL   Folia Biol (Praha) 68 (1), 25-32 (2022)
   PUBMED   36201855
  REMARK    GeneRIF: PLAG1 Promotes High Glucose-Induced Angiogenesis and
            Migration of Retinal Endothelial Cells by Regulating the
            Wnt/beta-Catenin Signalling Pathway.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hide,T., Takezaki,T., Nakatani,Y., Nakamura,H., Kuratsu,J. and
            Kondo,T.
  TITLE     Sox11 prevents tumorigenesis of glioma-initiating cells by inducing
            neuronal differentiation
  JOURNAL   Cancer Res 69 (20), 7953-7959 (2009)
   PUBMED   19808959
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hensen,K., Braem,C., Declercq,J., Van Dyck,F., Dewerchin,M.,
            Fiette,L., Denef,C. and Van de Ven,W.J.
  TITLE     Targeted disruption of the murine Plag1 proto-oncogene causes
            growth retardation and reduced fertility
  JOURNAL   Dev Growth Differ 46 (5), 459-470 (2004)
   PUBMED   15606491
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Voz,M.L., Agten,N.S., Van de Ven,W.J. and Kas,K.
  TITLE     PLAG1, the main translocation target in pleomorphic adenoma of the
            salivary glands, is a positive regulator of IGF-II
  JOURNAL   Cancer Res 60 (1), 106-113 (2000)
   PUBMED   10646861
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Astrom,A.K., Voz,M.L., Kas,K., Roijer,E., Wedell,B., Mandahl,N.,
            Van de Ven,W., Mark,J. and Stenman,G.
  TITLE     Conserved mechanism of PLAG1 activation in salivary gland tumors
            with and without chromosome 8q12 abnormalities: identification of
            SII as a new fusion partner gene
  JOURNAL   Cancer Res 59 (4), 918-923 (1999)
   PUBMED   10029085
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_008761747.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1115764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..499
                     /product="zinc finger protein PLAG1 isoform a"
                     /note="zinc finger protein PLAG1; pleiomorphic adenoma
                     gene 1 protein"
                     /calculated_mol_wt=55509
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          2..84
                     /region_name="Interaction with KPNA2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          22..25
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          36..56
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          41..242
                     /region_name="Decreased nuclear import with localization
                     in the nucleus but also in the cytoplasm.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Site            order(41,43,45,47..48,51..52,55,71,73,77..78,81..82,85,99,
                     101,103,105..106,109..110,113)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <58..139
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          64..86
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          79..101
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          94..114
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          123..143
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(157,159,161,163..164,167..168,171,192,194,198..199,
                     202..203,206,220,222,224,226..227,230..231)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          215..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..499
                     /region_name="Activates transcription, Inhibition of
                     nuclear import due to lack of NLS and KPNA2 interaction.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          243..383
                     /region_name="Repression domain, contains 3 sumoylation
                     motifs and massively decrease transcription activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          364..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     Region          384..499
                     /region_name="Massively activates transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T6.1)"
     CDS             1..499
                     /gene="Plag1"
                     /coded_by="NM_001436640.1:503..2002"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:297804"
                     /db_xref="RGD:1305286"
ORIGIN      
        1 matvipgdls evrdtqkaps gkrkrgeskp rknfpcqlcd kafnsveklk vhsfshtger
       61 pykcthqdct kafvskyklq rhmathspek thkcnycekm fhrkdhlknh lhthdpnket
      121 fkceecgksy ntklgfkrhl alhaatsgdl tckvclqtfe stgvllehlk shagkssggv
      181 kekkhqcehc errfytrkdv rrhmvvhtgr kdflcqycaq rfgrkdhltr hmkkshnqel
      241 lkvktepvdf ldpftcnmsv pikdellpvm slpssellsk pftntlqlnl yntpfqsmqs
      301 sgsthqmitt lplgmtcpid mdtvhpshhl afkcpfssts yaisipekeq plkgeiesyl
      361 melqggapss sqdsqasssk lglepqsgsp ddgagdlsls kssisisdpl ntpaldfsql
      421 fnfiplngpp ynplsvgslg msysqdeahs svsqlptqtq dlqdpantvg lgslhslsaa
      481 ftsslssstt lprfhqafq
//
LOCUS       NP_445755                374 aa            linear   ROD 20-MAR-2025
DEFINITION  C-X-C chemokine receptor type 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_445755
VERSION     NP_445755.2
DBSOURCE    REFSEQ: accession NM_053303.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Yi,H., Zhu,B., Zheng,C., Ying,Z. and Cheng,M.
  TITLE     CXCL13/CXCR5 promote chronic postsurgical pain and astrocyte
            activation in rats by targeting NLRP3
  JOURNAL   Neuroreport 35 (6), 406-412 (2024)
   PUBMED   38526919
  REMARK    GeneRIF: CXCL13/CXCR5 promote chronic postsurgical pain and
            astrocyte activation in rats by targeting NLRP3.
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Cao,J., Hu,C., Ding,Z., Chen,J., Liu,S. and Li,Q.
  TITLE     Mechanism of IRF5-regulated CXCL13/CXCR5 Signaling Axis in
            CCI-induced Neuropathic Pain in Rats
  JOURNAL   Curr Mol Med 24 (7), 940-949 (2024)
   PUBMED   37622691
  REMARK    GeneRIF: Mechanism of IRF5-regulated CXCL13/CXCR5 Signaling Axis in
            CCI-induced Neuropathic Pain in Rats.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Wang,X., Sumida,H. and Cyster,J.G.
  TITLE     GPR18 is required for a normal CD8alphaalpha intestinal
            intraepithelial lymphocyte compartment
  JOURNAL   J Exp Med 211 (12), 2351-2359 (2014)
   PUBMED   25348153
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Vogel,K.U., Edelmann,S.L., Jeltsch,K.M., Bertossi,A., Heger,K.,
            Heinz,G.A., Zoller,J., Warth,S.C., Hoefig,K.P., Lohs,C., Neff,F.,
            Kremmer,E., Schick,J., Repsilber,D., Geerlof,A., Blum,H., Wurst,W.,
            Heikenwalder,M., Schmidt-Supprian,M. and Heissmeyer,V.
  TITLE     Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40
            costimulator mRNAs and control follicular helper T cell
            differentiation
  JOURNAL   Immunity 38 (4), 655-668 (2013)
   PUBMED   23583643
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Zhang,X., Bedigian,A.V., Wang,W. and Eggert,U.S.
  TITLE     G protein-coupled receptors participate in cytokinesis
  JOURNAL   Cytoskeleton (Hoboken) 69 (10), 810-818 (2012)
   PUBMED   22888021
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Luther,S.A., Ansel,K.M. and Cyster,J.G.
  TITLE     Overlapping roles of CXCL13, interleukin 7 receptor alpha, and CCR7
            ligands in lymph node development
  JOURNAL   J Exp Med 197 (9), 1191-1198 (2003)
   PUBMED   12732660
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Kouba,M., Vanetti,M., Wang,X., Schafer,M. and Hollt,V.
  TITLE     Cloning of a novel putative G-protein-coupled receptor (NLR) which
            is expressed in neuronal and lymphatic tissue
  JOURNAL   FEBS Lett 321 (2-3), 173-178 (1993)
   PUBMED   8386678
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 11, 2025 this sequence version replaced NP_445755.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.31383.1,
                                           SRR26643292.33377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..374
                     /product="C-X-C chemokine receptor type 5 isoform 1"
                     /note="chemokine (C-X-C motif) receptor 5; C-X-C chemokine
                     receptor type 5; CXC-R5; CXCR-5; neurolymphatic receptor;
                     burkitt lymphoma receptor 1 homolog; chemochine (C-X-C
                     motif) receptor 5"
                     /calculated_mol_wt=42042
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P34997.1)"
     Region          54..335
                     /region_name="7tmA_CXCR5"
                     /note="CXC chemokine receptor type 5, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15181"
                     /db_xref="CDD:341336"
     Region          54..81
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341336"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Site            order(60,109,112,128,131..132,204..209,217,220..221,277,
                     284,287,299,303,306..307,310)
                     /site_type="other"
                     /note="putative chemokine binding site [polypeptide
                     binding]"
                     /db_xref="CDD:341336"
     Region          88..113
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341336"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Region          124..154
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341336"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Region          166..188
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341336"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P34997.1)"
     Region          217..246
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341336"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Region          254..284
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341336"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     Region          303..328
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341336"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P34997.1)"
     CDS             1..374
                     /gene="Cxcr5"
                     /gene_synonym="Blr1; NLR"
                     /coded_by="NM_053303.2:63..1187"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29363"
                     /db_xref="RGD:62010"
ORIGIN      
        1 mnypltldid sitynmdely kelaiysnst eiplqdsifc steegpllts fktifmpvay
       61 slifllgmmg nilvlviler hrhtrsstet flfhlavadl llvfilpfav aegsvgwvlg
      121 tflcktvial hkinfycssl llaciavdry laivhavhay rrrrllsihi tcstiwlagf
      181 lfalpellfa kvvqphnnes lpqcifsqen eaetrawfas rflyhtggfl lpmlvmawcy
      241 vgvvhrllqa qrrpqrqkav rvailvtsif llcwspyhiv ifldtlerlk avnsscelsg
      301 ylsvaitlce flglahccln pmlytfagvk frsdlsrllt klgcagpasl cqlfpgwrks
      361 slsesenats lttf
//
LOCUS       NP_001423557             699 aa            linear   ROD 20-MAR-2025
DEFINITION  phospholipase DDHD2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423557 XP_001059724
VERSION     NP_001423557.1
DBSOURCE    REFSEQ: accession NM_001436628.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Araki,M., Ohshima,N., Aso,C., Konishi,A., Obinata,H., Tatei,K. and
            Izumi,T.
  TITLE     Enzymatic characterization of recombinant rat DDHD2: a soluble
            diacylglycerol lipase
  JOURNAL   J Biochem 160 (5), 269-279 (2016)
   PUBMED   27198176
  REMARK    GeneRIF: These results therefore support the idea that DDHD2
            functions as a DG lipase in vivo and produces 2-AG.
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Aso,C., Araki,M., Ohshima,N., Tatei,K., Hirano,T., Obinata,H.,
            Kishi,M., Kishimoto,K., Konishi,A., Goto,F., Sugimoto,H. and
            Izumi,T.
  TITLE     Protein purification and cloning of diacylglycerol lipase from rat
            brain
  JOURNAL   J Biochem 159 (6), 585-597 (2016)
   PUBMED   26790472
  REMARK    GeneRIF: DG lipase activity in the soluble fraction of rat brain is
            derived from DDHD2. DDHD2 is distributed widely in the rat brain.
            Immunohistochemical analysis revealed that DDHD2 is expressed in
            hippocampal neurons, but not in glia.
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Inloes,J.M., Hsu,K.L., Dix,M.M., Viader,A., Masuda,K., Takei,T.,
            Wood,M.R. and Cravatt,B.F.
  TITLE     The hereditary spastic paraplegia-related enzyme DDHD2 is a
            principal brain triglyceride lipase
  JOURNAL   Proc Natl Acad Sci U S A 111 (41), 14924-14929 (2014)
   PUBMED   25267624
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_001059724.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32947.1,
                                           SRR26643298.71944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..699
                     /product="phospholipase DDHD2 isoform 1"
                     /note="phospholipase DDHD2"
                     /calculated_mol_wt=79440
     Region          43..112
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          379..447
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          484..687
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..699
                     /gene="Ddhd2"
                     /coded_by="NM_001436628.1:144..2243"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:680971"
                     /db_xref="RGD:1585818"
ORIGIN      
        1 mssgesyqeq lsqsdpspsp nssssfelld mdvgssyepv sphwfyckvi dskelwipfn
       61 sedsqqleea hgsgkdcner vvptdggryd vhlgermrya vywdelpsev rrctwfykgd
      121 kdnkyvpyse sfsqvledty mlavtldewk kklespnrei ivlhnpklmv hyqpitgsde
      181 wgststeqgr prsvkrgves ipvdihcgep lqidhlvfvv hgigpacdlr frsivqcvnd
      241 frsvslnllq thfkkaqenq qigrveflpv nwhsplhstg vdidlqritl psinrlrhft
      301 ndtildvffy nsptycqtiv dtvasemnri ytlflqrnpd fkggvsiagh slgslilfdi
      361 ltnqkdsigd idsekgslst aedlgdvstl eeelkklqls efvtvfekek vdrealalct
      421 drdlqemgip lgprkkilnh fsatkssvgi nrptmsasev nipkekgdyl dvgigqvsvk
      481 yprlnykpei ffafgspigm fltvrglrri dpnykfptck gffniyhpfd pvayriepmv
      541 vpgvefepml iphhkgrkrm hlelregltr msmdlknnll gslrmawksf trapypalqa
      601 semaedteae sepssekpsd anteeppvev keeapinvgm lnggqridyv lqekpiesfn
      661 eylfalqshl cywesedtvl lvlkeiyqtq gifldqplq
//
LOCUS       NP_001423574             530 aa            linear   ROD 20-MAR-2025
DEFINITION  chondroitin sulfate N-acetylgalactosaminyltransferase 1 [Rattus
            norvegicus].
ACCESSION   NP_001423574 XP_017455585
VERSION     NP_001423574.1
DBSOURCE    REFSEQ: accession NM_001436645.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Sato,T., Kudo,T., Ikehara,Y., Ogawa,H., Hirano,T., Kiyohara,K.,
            Hagiwara,K., Togayachi,A., Ema,M., Takahashi,S., Kimata,K.,
            Watanabe,H. and Narimatsu,H.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is
            necessary for normal endochondral ossification and aggrecan
            metabolism
  JOURNAL   J Biol Chem 286 (7), 5803-5812 (2011)
   PUBMED   21148564
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Watanabe,Y., Takeuchi,K., Higa Onaga,S., Sato,M., Tsujita,M.,
            Abe,M., Natsume,R., Li,M., Furuichi,T., Saeki,M., Izumikawa,T.,
            Hasegawa,A., Yokoyama,M., Ikegawa,S., Sakimura,K., Amizuka,N.,
            Kitagawa,H. and Igarashi,M.
  TITLE     Chondroitin sulfate N-acetylgalactosaminyltransferase-1 is required
            for normal cartilage development
  JOURNAL   Biochem J 432 (1), 47-55 (2010)
   PUBMED   20812917
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Gotoh,M., Sato,T., Akashima,T., Iwasaki,H., Kameyama,A.,
            Mochizuki,H., Yada,T., Inaba,N., Zhang,Y., Kikuchi,N., Kwon,Y.D.,
            Togayachi,A., Kudo,T., Nishihara,S., Watanabe,H., Kimata,K. and
            Narimatsu,H.
  TITLE     Enzymatic synthesis of chondroitin with a novel chondroitin sulfate
            N-acetylgalactosaminyltransferase that transfers
            N-acetylgalactosamine to glucuronic acid in initiation and
            elongation of chondroitin sulfate synthesis
  JOURNAL   J Biol Chem 277 (41), 38189-38196 (2002)
   PUBMED   12163485
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Kitagawa,H., Uyama,T. and Sugahara,K.
  TITLE     Molecular cloning and expression of a human chondroitin synthase
  JOURNAL   J Biol Chem 276 (42), 38721-38726 (2001)
   PUBMED   11514575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_017455585.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55942.1,
                                           SRR26643285.50466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..530
                     /product="chondroitin sulfate
                     N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.174"
                     /note="chondroitin beta1,4
                     N-acetylgalactosaminyltransferase"
                     /calculated_mol_wt=60770
     Region          68..505
                     /region_name="CHGN"
                     /note="Chondroitin N-acetylgalactosaminyltransferase;
                     pfam05679"
                     /db_xref="CDD:461712"
     CDS             1..530
                     /gene="Csgalnact1"
                     /gene_synonym="Chgn; RGD1307618"
                     /coded_by="NM_001436645.1:767..2359"
                     /db_xref="GeneID:306375"
                     /db_xref="RGD:1307618"
ORIGIN      
        1 mvrrglvgwi srvvillvll ccaisvlyml actpkgdqeq lglprangpt gkdgyqavlq
       61 ereeqhrnyv nslkrqiaql kdelqarseq lrsgqdqasd atslrsgwdp epkaqadila
      121 flrgqvdkae vhagvklate yaavpfdsft lqkvyqletg ltrhpeekpv rkdkrdelve
      181 aiesalesln spvessphqr pytaadfieg iyrterdkgt lyeltfkgdh khefqrlvlf
      241 rpfgpimkvk keklnmantl invivplarr vdkfrhfmqn fremciqqdg rvhltvvyfg
      301 keemnevkgi lentskaanf rnftfiqlng efsrgkgldv garfwkgsnv vlffcdvdiy
      361 ftseflntcr lntqpgkkvf ypvlfsqynp giiyghhdav paleqqlvik ketgfwrdfg
      421 fgmtcqyrsd finiggfdld ikgwggedvh lyrkylhsnl ivirtpvrgl fhlwhekhcm
      481 deltpeqyrm cmqskamnea shgqlgmlvf rheieahlrk qklkasskkt
//
LOCUS       NP_001423582             656 aa            linear   ROD 20-MAR-2025
DEFINITION  anion exchange transporter isoform a [Rattus norvegicus].
ACCESSION   NP_001423582 XP_063143361
VERSION     NP_001423582.1
DBSOURCE    REFSEQ: accession NM_001436653.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Kiriya,M., Kawashima,A., Fujiwara,Y., Tanimura,Y., Yoshihara,A.,
            Nakamura,Y., Tanigawa,K., Kondo,T. and Suzuki,K.
  TITLE     Thyroglobulin regulates the expression and localization of the
            novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes
  JOURNAL   Endocr J 69 (10), 1217-1225 (2022)
   PUBMED   35644541
  REMARK    GeneRIF: Thyroglobulin regulates the expression and localization of
            the novel iodide transporter solute carrier family 26 member 7
            (SLC26A7) in thyrocytes.
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Yin,K., Lei,Y., Wen,X., Lacruz,R.S., Soleimani,M., Kurtz,I.,
            Snead,M.L., White,S.N. and Paine,M.L.
  TITLE     SLC26A Gene Family Participate in pH Regulation during Enamel
            Maturation
  JOURNAL   PLoS One 10 (12), e0144703 (2015)
   PUBMED   26671068
  REMARK    GeneRIF: Slc26a1, Slc26a6 and Slc26a7 are novel participants in the
            extracellular transport of bicarbonate during enamel maturation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Sun,X. and Petrovic,S.
  TITLE     Increased acid load and deletion of AE1 increase Slc26a7 expression
  JOURNAL   Nephron Physiol 109 (3), p29-p35 (2008)
   PUBMED   18663336
  REMARK    GeneRIF: Suggest that the increase in Slc26a7 expression caused by
            acid challenge represents an adaptive response, indicating that
            Slc26a7 contributes to the regulation of acid-base balance by the
            kidney.
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Barone,S., Amlal,H., Kujala,M., Xu,J., Karet,F., Blanchard,A.,
            Kere,J. and Soleimani,M.
  TITLE     Regulation of the basolateral chloride/base exchangers AE1 and
            SLC26A7 in the kidney collecting duct in potassium depletion
  JOURNAL   Nephrol Dial Transplant 22 (12), 3462-3470 (2007)
   PUBMED   17804457
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Kosiek,O., Busque,S.M., Foller,M., Shcheynikov,N., Kirchhoff,P.,
            Bleich,M., Muallem,S. and Geibel,J.P.
  TITLE     SLC26A7 can function as a chloride-loading mechanism in parietal
            cells
  JOURNAL   Pflugers Arch 454 (6), 989-998 (2007)
   PUBMED   17404755
  REMARK    GeneRIF: SLC26A7 is a Cl(-) uptake system under histamine
            stimulation
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Petrovic,S., Amlal,H., Sun,X., Karet,F., Barone,S. and Soleimani,M.
  TITLE     Vasopressin induces expression of the Cl-/HCO3- exchanger SLC26A7
            in kidney medullary collecting ducts of Brattleboro rats
  JOURNAL   Am J Physiol Renal Physiol 290 (5), F1194-F1201 (2006)
   PUBMED   16352747
  REMARK    GeneRIF: vasopressin increases the expression of SLC26A7 protein
            through posttranscriptional mechanisms in the outer medullary
            collecting duct
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Kim,K.H., Shcheynikov,N., Wang,Y. and Muallem,S.
  TITLE     SLC26A7 is a Cl- channel regulated by intracellular pH
  JOURNAL   J Biol Chem 280 (8), 6463-6470 (2005)
   PUBMED   15591059
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Petrovic,S., Ju,X., Barone,S., Seidler,U., Alper,S.L., Lohi,H.,
            Kere,J. and Soleimani,M.
  TITLE     Identification of a basolateral Cl-/HCO3- exchanger specific to
            gastric parietal cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 284 (6), G1093-G1103 (2003)
   PUBMED   12736153
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Lohi,H., Kujala,M., Makela,S., Lehtonen,E., Kestila,M.,
            Saarialho-Kere,U., Markovich,D. and Kere,J.
  TITLE     Functional characterization of three novel tissue-specific anion
            exchangers SLC26A7, -A8, and -A9
  JOURNAL   J Biol Chem 277 (16), 14246-14254 (2002)
   PUBMED   11834742
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Mocellin,R. and Buhlmeyer,K.
  TITLE     Late banding operation in children with ventricular septal defect
            and pulmonary arterial hypertension
  JOURNAL   Eur J Cardiol 3 (3), 205-211 (1975)
   PUBMED   1183472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063143361.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20671.1,
                                           SRR26643287.12744.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..656
                     /product="anion exchange transporter isoform a"
                     /note="anion exchange transporter; solute carrier family
                     26 (anion exchanger), member 7"
                     /calculated_mol_wt=71742
     Region          33..637
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     CDS             1..656
                     /gene="Slc26a7"
                     /coded_by="NM_001436653.1:122..2092"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:297910"
                     /db_xref="RGD:1310846"
ORIGIN      
        1 mtgakrkkrs vlwgkmhtph redikqwckr rlpilewapq ynlkenllpd tvsgvllavq
       61 qvtqglsfai lssvhpvfgl ygslfpaiiy aifgmgrhva tgtfaltsli sanaverlvp
      121 qsnrnlttqs nssvlglsef elqrigvaaa vsflggviql vmfvlqlgna tflltepvis
      181 amttgaathv vtsqvkyllg ikmpyisgpl gffyiyayvf eniksvqlea lllsllsivv
      241 lvlvkelneq fkrkikvvlp vdlvliiaas facyctnmen tyglevvgri pkgippprap
      301 pmnilsavlt eafgvalvgy vaslalaqgs akkfkysvdd nqeflahgls nvipsflfci
      361 psaaamgrta glystgaktq vacliscifv liviyaigpl lywlpmcvla siivvglkgm
      421 liqfrdlkky wnvdkidwgi wistyiftic faanvgllfg vvctiaivlg rfpraktlsi
      481 tdmkemelkv ktetydensq qikiisinnp lvflnakkfs adlmkiilke tdgsqalddv
      541 skceqntlls plpngsctee asqpcpseky slvlncsglt ffdytgvstl velyldcksr
      601 svdvflanct aslikamtyy gdldtekpif fdsvataisv iqsnknlskd tdhsev
//
LOCUS       NP_001423550             660 aa            linear   ROD 20-MAR-2025
DEFINITION  junctophilin-1 [Rattus norvegicus].
ACCESSION   NP_001423550 XP_006237782
VERSION     NP_001423550.1
DBSOURCE    REFSEQ: accession NM_001436621.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Rossi,D., Scarcella,A.M., Liguori,E., Lorenzini,S., Pierantozzi,E.,
            Kutchukian,C., Jacquemond,V., Messa,M., De Camilli,P. and
            Sorrentino,V.
  TITLE     Molecular determinants of homo- and heteromeric interactions of
            Junctophilin-1 at triads in adult skeletal muscle fibers
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15716-15724 (2019)
   PUBMED   31315980
  REMARK    GeneRIF: Molecular determinants of homo- and heteromeric
            interactions of Junctophilin-1 at triads in adult skeletal muscle
            fibers.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Murphy,R.M., Dutka,T.L., Horvath,D., Bell,J.R., Delbridge,L.M. and
            Lamb,G.D.
  TITLE     Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in
            skeletal and cardiac muscle
  JOURNAL   J Physiol 591 (3), 719-729 (2013)
   PUBMED   23148318
  REMARK    GeneRIF: This study demonstrates that both JP1 and JP2 in skeletal
            muscle undergo Ca2+-dependent proteolysis by endogenous proteases
            when the intracellular Ca2+ is raised within the physiological
            range for a sustained period
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,X.G., Wu,B.W., Zhang,W.C., Zhou,L.M., Zhu,D.Y. and Lou,Y.J.
  TITLE     [Expression of Junctophilin 1 during cardiogenesis of mouse
            embryonic stem cells and rat embryos]
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 41 (4), 359-365 (2012)
   PUBMED   22927069
  REMARK    GeneRIF: JP1 gene is expressed during the whole process of
            cardiogenesis, while JP1 protein only appears during the early
            stage.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Komazaki,S., Nishi,M. and Takeshima,H.
  TITLE     Abnormal junctional membrane structures in cardiac myocytes
            expressing ectopic junctophilin type 1
  JOURNAL   FEBS Lett 542 (1-3), 69-73 (2003)
   PUBMED   12729900
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Komazaki,S., Ito,K., Takeshima,H. and Nakamura,H.
  TITLE     Deficiency of triad formation in developing skeletal muscle cells
            lacking junctophilin type 1
  JOURNAL   FEBS Lett 524 (1-3), 225-229 (2002)
   PUBMED   12135771
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Takeshima,H., Komazaki,S., Nishi,M., Iino,M. and Kangawa,K.
  TITLE     Junctophilins: a novel family of junctional membrane complex
            proteins
  JOURNAL   Mol Cell 6 (1), 11-22 (2000)
   PUBMED   10949023
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006237782.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20316.1,
                                           SRR26643296.14500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..660
                     /product="junctophilin-1"
                     /calculated_mol_wt=71895
     Region          <3..333
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          <410..638
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     CDS             1..660
                     /gene="Jph1"
                     /coded_by="NM_001436621.1:242..2224"
                     /db_xref="GeneID:297748"
                     /db_xref="RGD:1308789"
ORIGIN      
        1 mtggrfdfdd ggtycggwee gkahghgict gpkgqgeysg swshgfevvg gytwpsgnty
       61 qgywaqgkrh glgvetkgkw myrgewshgf kgrygvrqsl ctparyegtw snglqdgygv
      121 etygdggtyq gqwaggmrhg ygvrqsvpyg matvirsplr tslaslrseq sngsvlheaa
      181 aaaadnpagt rggfvlnfha dtelgkkksg lfrrgsllgs mklrksesks sisskrssvr
      241 sdaamsriss sdanstisfg dvdcdfcpve dhvdatttet ymgewkndkr ngfgisersn
      301 gmkyegewan nkrhgygctv fpdgskeegk yknnilvrgi rkqlipirnt ktrekvdrai
      361 egaqraaama rtkveiansr taharakada adqaavaarq ecdiaravar elspdfyqpg
      421 pdyikqrfqe gvdikenpee kvpekppspk esphfyrkgt tpprspeasp kqshspqpss
      481 pksmkkqnps sgarlshdkr ntaeeqvvai vnkplmskap skelgatvsk ysgrhyvpnp
      541 sngelhsqyh gyyvklntpq hppedredds gvgqsssalv prpspnkwsp pksvtkpvak
      601 esktepkakk selaipknta sndtcpplek eansgpnsim ivlvmllnig lailfvhflt
//
LOCUS       NP_001178037             997 aa            linear   ROD 20-MAR-2025
DEFINITION  little elongation complex subunit 2 [Rattus norvegicus].
ACCESSION   NP_001178037 XP_001075498 XP_006243464
VERSION     NP_001178037.1
DBSOURCE    REFSEQ: accession NM_001191108.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Hu,D., Smith,E.R., Garruss,A.S., Mohaghegh,N., Varberg,J.M.,
            Lin,C., Jackson,J., Gao,X., Saraf,A., Florens,L., Washburn,M.P.,
            Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex functions at initiation and
            elongation phases of snRNA gene transcription
  JOURNAL   Mol Cell 51 (4), 493-505 (2013)
   PUBMED   23932780
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Yu,Y., Kranzler,H.R., Panhuysen,C., Weiss,R.D., Poling,J.,
            Farrer,L.A. and Gelernter,J.
  TITLE     Substance dependence low-density whole genome association study in
            two distinct American populations
  JOURNAL   Hum Genet 123 (5), 495-506 (2008)
   PUBMED   18438686
REFERENCE   4  (residues 1 to 997)
  AUTHORS   Sugiura,N., Dadashev,V. and Corriveau,R.A.
  TITLE     NARG2 encodes a novel nuclear protein with (S/T)PXX motifs that is
            expressed during development
  JOURNAL   Eur J Biochem 271 (23-24), 4629-4637 (2004)
   PUBMED   15606750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Mar 14, 2025 this sequence version replaced
            XP_006243464.1, XP_001075498.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2785828.1,
                                           SRR26360172.1461442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..997
                     /product="little elongation complex subunit 2"
                     /note="NMDA receptor-regulated gene 2; NMDA
                     receptor-regulated protein 2; NMDA receptor regulated 2;
                     interactor of little elongator complex ELL subunit 2"
                     /calculated_mol_wt=110675
     Region          735..945
                     /region_name="NARG2_C"
                     /note="NMDA receptor-regulated gene protein 2 C-terminus;
                     pfam10505"
                     /db_xref="CDD:463121"
     CDS             1..997
                     /gene="Ice2"
                     /gene_synonym="Narg2"
                     /coded_by="NM_001191108.2:226..3219"
                     /db_xref="GeneID:691379"
                     /db_xref="RGD:1585038"
ORIGIN      
        1 mssgitmsep rlnwdvtpkn glkvffspen ykdhsmapsl kelyilsnrr igenvsvsan
       61 svenepavss atqakekvgm illpkprvpy prfsrfsqre qrtfvdllvk yakipssskt
      121 vgtntneflq yldmkkhvne evneflkflq nsakkcaqdy nmlsdearlf teqilracie
      181 qvkkypefyt lhevtslmgf fpfkiemglk lektllvlgs akfvktafps mpvklqlske
      241 dmssienpqq qaeamhcdis kdpnaeklvs ryhpqialts qalftllnnh gpsykeqwei
      301 pvcvqmiave gskpvkviyi nsplprkqmt mrernqifhe vplkhifskt tsvpvsavfm
      361 dkpeeytsev disteasecr kietlenldl dfdgdvtele tfgvtttsps rspssesdss
      421 apimtdvhta pkvtaipvap aapvtpaapv apvvapvapv vapvapaapv tpvtpeasai
      481 pnitddsrsl cqilmkqlqk ekqlfsgves gpeacknkdd qglepcaeeg psanaksltq
      541 dsevhrteei snesdvgalc tsderqsvqk nadnpnetat asetadtekg ipcgsdtded
      601 cliidtesks nsdgrtaglg sspnssaqas venqttttvs eescvlkkpi krvykkfdpv
      661 geilkmqdel lkpvsrtipe lpltnseesk qpsaseqpsa tldastwpks swpsafqkpk
      721 grlpyelqdy vedtseyvap qegnfvyklf slqdllllvr csvqrvetrp rskkrkkirr
      781 qfpvyvlpkv eyqgcygvea lteselcrfw tesllhsncs fyvghidaft sklfmleeit
      841 seelkeklaa lkisslfnil qhilkklcsl qegsyllsha aedsslliyk tsdgkvtrta
      901 ynlhkahcdl pgvpsslsvp wvpldpsyll pyhihhgrip ctfppkslrp aaqpkvgatr
      961 mptrnhrnpv sretkssclp vqqvenegva qnkrkim
//
LOCUS       NP_476473                193 aa            linear   ROD 20-MAR-2025
DEFINITION  transforming protein RhoA [Rattus norvegicus].
ACCESSION   NP_476473 XP_006243761
VERSION     NP_476473.1
DBSOURCE    REFSEQ: accession NM_057132.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Liu,Q., Liu,C. and Lei,B.
  TITLE     siRNA Mediated Downregulation of RhoA Expression Reduces Oxidative
            Induced Apoptosis in Retinal Ganglion Cells
  JOURNAL   Curr Mol Med 24 (5), 630-636 (2024)
   PUBMED   37171014
  REMARK    GeneRIF: siRNA Mediated Downregulation of RhoA Expression Reduces
            Oxidative Induced Apoptosis in Retinal Ganglion Cells.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Sun,H.G., Jiang,Q., Fan,W.J., Shen,X.Y., Wang,Z.W. and Wang,X.
  TITLE     TAGAP activates Th17 cell differentiation by promoting RhoA and
            NLRP3 to accelerate rheumatoid arthritis development
  JOURNAL   Clin Exp Immunol 214 (1), 26-35 (2023)
   PUBMED   37458218
  REMARK    GeneRIF: TAGAP activates Th17 cell differentiation by promoting
            RhoA and NLRP3 to accelerate rheumatoid arthritis development.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Shan,S., Su,M., Li,Y., Wang,Z., Liu,D., Zhou,Y., Fu,X., Yang,S.,
            Zhang,J., Qiu,J., Liu,H., Zeng,G., Chen,P., Wang,X., DiSanto,M.E.,
            Guo,Y. and Zhang,X.
  TITLE     Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles
  JOURNAL   Mol Med 29 (1), 139 (2023)
   PUBMED   37864185
  REMARK    GeneRIF: Mechanism of RhoA regulating benign prostatic hyperplasia:
            RhoA-ROCK-beta-catenin signaling axis and static & dynamic dual
            roles.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Zhou,W., Yuan,X., Li,J., Wang,W. and Ye,S.
  TITLE     Retinol binding protein 4 promotes the phenotypic transformation of
            vascular smooth muscle cells under high glucose condition via
            modulating RhoA/ROCK1 pathway
  JOURNAL   Transl Res 259, 13-27 (2023)
   PUBMED   37003483
  REMARK    GeneRIF: Retinol binding protein 4 promotes the phenotypic
            transformation of vascular smooth muscle cells under high glucose
            condition via modulating RhoA/ROCK1 pathway.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Li,L., Wang,Q., Sun,X., Li,Z., Liu,S., Zhang,X., Zhou,J., Zhang,R.,
            Liu,K., Wang,P., Niu,J., Wen,Y. and Zhang,L.
  TITLE     Activation of RhoA pathway participated in the changes of emotion,
            cognitive function and hippocampal synaptic plasticity in juvenile
            chronic stress rats
  JOURNAL   Int J Biol Macromol 233, 123652 (2023)
   PUBMED   36780962
  REMARK    GeneRIF: Activation of RhoA pathway participated in the changes of
            emotion, cognitive function and hippocampal synaptic plasticity in
            juvenile chronic stress rats.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Yoshimura,S., Sakai,H., Nakashima,S., Nozawa,Y., Shinoda,J.,
            Sakai,N. and Yamada,H.
  TITLE     Differential expression of Rho family GTP-binding proteins and
            protein kinase C isozymes during C6 glial cell differentiation
  JOURNAL   Brain Res Mol Brain Res 45 (1), 90-98 (1997)
   PUBMED   9105674
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Ishizaki,T., Maekawa,M., Fujisawa,K., Okawa,K., Iwamatsu,A.,
            Fujita,A., Watanabe,N., Saito,Y., Kakizuka,A., Morii,N. and
            Narumiya,S.
  TITLE     The small GTP-binding protein Rho binds to and activates a 160 kDa
            Ser/Thr protein kinase homologous to myotonic dystrophy kinase
  JOURNAL   EMBO J 15 (8), 1885-1893 (1996)
   PUBMED   8617235
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ridley,A.J. and Hall,A.
  TITLE     The small GTP-binding protein rho regulates the assembly of focal
            adhesions and actin stress fibers in response to growth factors
  JOURNAL   Cell 70 (3), 389-399 (1992)
   PUBMED   1643657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_006243761.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO793437.1, FO815825.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..193
                     /product="transforming protein RhoA"
                     /EC_number="3.6.5.2"
                     /note="plysia ras-related homolog A2; ras homolog gene
                     family, member A"
                     /calculated_mol_wt=21651
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030415"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     binding. /evidence=ECO:0000250|UniProtKB:P61586"
                     /note="propagated from UniProtKB/Swiss-Prot (P61589.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1 and SLK.
                     /evidence=ECO:0000269|PubMed:18420945; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61589.1)"
     CDS             1..193
                     /gene="Rhoa"
                     /gene_synonym="Arha; Arha2"
                     /coded_by="NM_057132.4:233..814"
                     /db_xref="GeneID:117273"
                     /db_xref="RGD:619921"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lil
//
LOCUS       NP_001423579             432 aa            linear   ROD 20-MAR-2025
DEFINITION  testican-3 precursor [Rattus norvegicus].
ACCESSION   NP_001423579 XP_017455594
VERSION     NP_001423579.1
DBSOURCE    REFSEQ: accession NM_001436650.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Manabe,R., Tsutsui,K., Yamada,T., Kimura,M., Nakano,I., Shimono,C.,
            Sanzen,N., Furutani,Y., Fukuda,T., Oguri,Y., Shimamoto,K.,
            Kiyozumi,D., Sato,Y., Sado,Y., Senoo,H., Yamashina,S., Fukuda,S.,
            Kawai,J., Sugiura,N., Kimata,K., Hayashizaki,Y. and Sekiguchi,K.
  TITLE     Transcriptome-based systematic identification of extracellular
            matrix proteins
  JOURNAL   Proc Natl Acad Sci U S A 105 (35), 12849-12854 (2008)
   PUBMED   18757743
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Nakada,M., Yamada,A., Takino,T., Miyamori,H., Takahashi,T.,
            Yamashita,J. and Sato,H.
  TITLE     Suppression of membrane-type 1 matrix metalloproteinase
            (MMP)-mediated MMP-2 activation and tumor invasion by testican 3
            and its splicing variant gene product, N-Tes
  JOURNAL   Cancer Res 61 (24), 8896-8902 (2001)
   PUBMED   11751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_017455594.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.475668.1,
                                           SRR26360194.1486073.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p13"
     Protein         1..432
                     /product="testican-3 precursor"
                     /note="testican-3; sparc/osteonectin, cwcv and kazal-like
                     domains proteoglycan 3; sparc/osteonectin, cwcv and
                     kazal-like domains proteoglycan (testican) 3"
                     /calculated_mol_wt=46486
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          134..180
                     /region_name="Kazal_2"
                     /note="Kazal-type serine protease inhibitor domain;
                     pfam07648"
                     /db_xref="CDD:400135"
     Region          198..310
                     /region_name="EFh_SPARC_TICN3"
                     /note="EF-hand, extracellular calcium-binding (EC) motif,
                     found in testican-3 (TICN3); cd16239"
                     /db_xref="CDD:320018"
     Region          246..277
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320018"
     Site            order(258,262,269)
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:320018"
     Region          278..310
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320018"
     Region          314..377
                     /region_name="Thyroglobulin_1"
                     /note="Thyroglobulin type-1 repeat; pfam00086"
                     /db_xref="CDD:459665"
     Site            order(318,333,351,355)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     CDS             1..432
                     /gene="Spock3"
                     /coded_by="NM_001436650.1:113..1411"
                     /db_xref="GeneID:306404"
                     /db_xref="RGD:1305672"
ORIGIN      
        1 mlkvsallcv caaawcsqtl aaaaavavag grsdggnfld ekqwlttvsq ydkevgqwnk
       61 frdddyfrtw npgkpidqal dpardpclkt kcsrhkvcit qdaqtalcis hrrlthsmke
      121 vggshkqwrg lpsstckqcp iayaspvcgs dghsyssqck leyqacvlgk qisikcegrc
      181 pcpsdksmst grnvkracsd lefrevanrl rdwfkalhes gsqnkrtkal lrpersrfdt
      241 silpickdsl gwmfnrldtn ydllldqsel gsiyldkneh ctkaffnscd tykdslisnn
      301 ewcycfqrqq dppchtelsk iqkrqgikkl lgqylplcde dgfykptqch gsvgqcwcvd
      361 rygnevvgsr ingvadcaid feisgdfasg dfrewtddeg eeddmndkdd iedddedegd
      421 ddddgddhdg yi
//
LOCUS       NP_598257                375 aa            linear   ROD 20-MAR-2025
DEFINITION  G-protein coupled estrogen receptor 1 [Rattus norvegicus].
ACCESSION   NP_598257 XP_006248976
VERSION     NP_598257.2
DBSOURCE    REFSEQ: accession NM_133573.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,Y.Q., Sun,T., Zhao,Z., Fu,J., Yang,L., Xu,Y., Zhao,J.F.,
            Tang,X.L., Liu,A. and Zhao,M.G.
  TITLE     Activation of GPR30 Ameliorates Cerebral Ischemia-Reperfusion
            Injury by Suppressing Ferroptosis Through Nrf2/GPX4 Signaling
            Pathway
  JOURNAL   Neuromolecular Med 26 (1), 33 (2024)
   PUBMED   39138706
  REMARK    GeneRIF: Activation of GPR30 Ameliorates Cerebral
            Ischemia-Reperfusion Injury by Suppressing Ferroptosis Through
            Nrf2/GPX4 Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Grubic Kezele,T., Omrcen,H., Baticic,L., Sucurovic,S. and Zoricic
            Cvek,S.
  TITLE     Joint Inflammation Correlates with Joint GPR30 Expression in Males
            and Hippocampal GPR30 Expression in Females in a Rat Model of
            Rheumatoid Arthritis
  JOURNAL   Int J Mol Sci 25 (14), 7864 (2024)
   PUBMED   39063107
  REMARK    GeneRIF: Joint Inflammation Correlates with Joint GPR30 Expression
            in Males and Hippocampal GPR30 Expression in Females in a Rat Model
            of Rheumatoid Arthritis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Azizian,H., Farhadi,Z., Bader,M., Alizadeh Ghalenoei,J.,
            Ghafari,M.A. and Mahmoodzadeh,S.
  TITLE     GPER activation attenuates cardiac dysfunction by upregulating the
            SIRT1/3-AMPK-UCP2 pathway in postmenopausal diabetic rats
  JOURNAL   PLoS One 18 (12), e0293630 (2023)
   PUBMED   38134189
  REMARK    GeneRIF: GPER activation attenuates cardiac dysfunction by
            upregulating the SIRT1/3-AMPK-UCP2 pathway in postmenopausal
            diabetic rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hu,J., Huang,Y., Gao,F., Sun,W., Liu,H., Ma,H., Yuan,T., Liu,Z.,
            Tang,L., Ma,Y., Zhang,X., Bai,J. and Wang,R.
  TITLE     Brain-derived estrogen: a critical player in maintaining cognitive
            health of aged female rats, possibly involving GPR30
  JOURNAL   Neurobiol Aging 129, 15-27 (2023)
   PUBMED   37257405
  REMARK    GeneRIF: Brain-derived estrogen: a critical player in maintaining
            cognitive health of aged female rats, possibly involving GPR30.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Xu,X., Wang,J., Guo,X., Chen,Y., Ding,S., Zou,G., Zhu,L., Li,T. and
            Zhang,X.
  TITLE     GPR30-mediated non-classic estrogen pathway in mast cells
            participates in endometriosis pain via the production of FGF2
  JOURNAL   Front Immunol 14, 1106771 (2023)
   PUBMED   36845134
  REMARK    GeneRIF: GPR30-mediated non-classic estrogen pathway in mast cells
            participates in endometriosis pain via the production of FGF2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Sakamoto,H., Matsuda,K., Hosokawa,K., Nishi,M., Morris,J.F.,
            Prossnitz,E.R. and Kawata,M.
  TITLE     Expression of G protein-coupled receptor-30, a G protein-coupled
            membrane estrogen receptor, in oxytocin neurons of the rat
            paraventricular and supraoptic nuclei
  JOURNAL   Endocrinology 148 (12), 5842-5850 (2007)
   PUBMED   17872373
  REMARK    GeneRIF: Results suggest that GPR30 may serve primarily as a
            nongenomic transducer of estrogen actions in the
            hypothalamo-neurohypophyseal system.
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Funakoshi,T., Yanai,A., Shinoda,K., Kawano,M.M. and Mizukami,Y.
  TITLE     G protein-coupled receptor 30 is an estrogen receptor in the plasma
            membrane
  JOURNAL   Biochem Biophys Res Commun 346 (3), 904-910 (2006)
   PUBMED   16780796
  REMARK    GeneRIF: GPR30, a transmembrane receptor for estrogen, is localized
            to the plasma membrane of CA2 pyramidal neuronal cells of the
            hippocampus in rat brain
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Revankar,C.M., Cimino,D.F., Sklar,L.A., Arterburn,J.B. and
            Prossnitz,E.R.
  TITLE     A transmembrane intracellular estrogen receptor mediates rapid cell
            signaling
  JOURNAL   Science 307 (5715), 1625-1630 (2005)
   PUBMED   15705806
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Thomas,P., Pang,Y., Filardo,E.J. and Dong,J.
  TITLE     Identity of an estrogen membrane receptor coupled to a G protein in
            human breast cancer cells
  JOURNAL   Endocrinology 146 (2), 624-632 (2005)
   PUBMED   15539556
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Bonini,J.A., Anderson,S.M. and Steiner,D.F.
  TITLE     Molecular cloning and tissue expression of a novel orphan G
            protein-coupled receptor from rat lung
  JOURNAL   Biochem Biophys Res Commun 234 (1), 190-193 (1997)
   PUBMED   9168987
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Mar 12, 2025 this sequence version replaced
            XP_006248976.1, NP_598257.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2159302.1,
                                           SRR26643298.79811.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..375
                     /product="G-protein coupled estrogen receptor 1"
                     /note="mER; chemokine receptor-like 2; membrane estrogen
                     receptor; G-protein coupled receptor 30; G-protein coupled
                     receptor 41; chemoattractant receptor-like 2"
                     /calculated_mol_wt=42156
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99527; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08878.1)"
     Region          60..335
                     /region_name="7tmA_GPER1"
                     /note="G protein-coupled estrogen receptor 1, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd14989"
                     /db_xref="CDD:320120"
     Region          61..87
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320120"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          94..119
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320120"
     Site            97..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Site            order(115,118..119,130..135,137..138,141,186,188..192,211,
                     214..216,218..220,222..223,272,275..276,278..279,282,
                     302..303,305..307,310,313..314)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320120"
     Region          130..160
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320120"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          173..194
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320120"
     Site            176..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          211..238
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320120"
     Site            221..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          252..282
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320120"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     Region          303..328
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320120"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08878.1)"
     CDS             1..375
                     /gene="Gper1"
                     /gene_synonym="Gper; Gpr30; GPR41"
                     /coded_by="NM_133573.3:403..1530"
                     /db_xref="GeneID:171104"
                     /db_xref="RGD:619845"
ORIGIN      
        1 maattpaqdv gveiylgpvw papsnstpla lnlslalred apgnltgdls ehqqyvialf
       61 lsclytiflf pigfvgnili lvvnisfrek mtipdlyfin laaadlilva dslievfnld
      121 eqyydiavlc tfmslflqin myssvffltw msfdrylala kamrcglfrt khharlscgl
      181 iwmasvsatl vpftavhlrh teeacfcfad vrevqwlevt lgfivpfaii glcyslivra
      241 lirahrhrgl rprrqkalrm ifavvlvffi cwlpenvfis vhllqwaqpg dtpckqsfrh
      301 aypltghivn laafsnscln pliysflget frdklrlyva qktslpalnr fchatlkavi
      361 pdsteqsdvk fssav
//
LOCUS       NP_072114                655 aa            linear   ROD 20-MAR-2025
DEFINITION  transketolase isoform 4 [Rattus norvegicus].
ACCESSION   NP_072114
VERSION     NP_072114.2
DBSOURCE    REFSEQ: accession NM_022592.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Zhao,Y., Wu,Y., Hu,H., Cai,J., Ning,M., Ni,X. and Zhong,C.
  TITLE     Downregulation of transketolase activity is related to inhibition
            of hippocampal progenitor cell proliferation induced by thiamine
            deficiency
  JOURNAL   Biomed Res Int 2014, 572915 (2014)
   PUBMED   25028661
  REMARK    GeneRIF: results suggest that modulation of transketolase activity
            might be one of the mechanisms by which thiamine regulates the
            proliferation of hippocampal progenitor cells.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Mitschke,L., Parthier,C., Schroder-Tittmann,K., Coy,J., Ludtke,S.
            and Tittmann,K.
  TITLE     The crystal structure of human transketolase and new insights into
            its mode of action
  JOURNAL   J Biol Chem 285 (41), 31559-31570 (2010)
   PUBMED   20667822
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Wang,J.J., Martin,P.R. and Singleton,C.K.
  TITLE     Aspartate 155 of human transketolase is essential for thiamine
            diphosphate-magnesium binding, and cofactor binding is required for
            dimer formation
  JOURNAL   Biochim Biophys Acta 1341 (2), 165-172 (1997)
   PUBMED   9357955
REFERENCE   7  (residues 1 to 655)
  AUTHORS   McCool,B.A., Plonk,S.G., Martin,P.R. and Singleton,C.K.
  TITLE     Cloning of human transketolase cDNAs and comparison of the
            nucleotide sequence of the coding region in Wernicke-Korsakoff and
            non-Wernicke-Korsakoff individuals
  JOURNAL   J Biol Chem 268 (2), 1397-1404 (1993)
   PUBMED   8419340
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Bublitz,C. and Steavenson,S.
  TITLE     The pentose phosphate pathway in the endoplasmic reticulum
  JOURNAL   J Biol Chem 263 (26), 12849-12853 (1988)
   PUBMED   2843500
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Casazza,J.P. and Veech,R.L.
  TITLE     The interdependence of glycolytic and pentose cycle intermediates
            in ad libitum fed rats
  JOURNAL   J Biol Chem 261 (2), 690-698 (1986)
   PUBMED   3079759
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Nov 26, 2020 this sequence version replaced NP_072114.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09256.1, SRR26643295.51883.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..655
                     /product="transketolase isoform 4"
                     /EC_number="2.2.1.1"
                     /note="TK"
                     /calculated_mol_wt=71028
     Region          40..652
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     CDS             1..655
                     /gene="Tkt"
                     /coded_by="NM_022592.2:8..1975"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64524"
                     /db_xref="RGD:621036"
ORIGIN      
        1 mdpvrqiqcd regkrfpfls appastsspd ramegyhkpd qqklqalkdt anrlrissiq
       61 attaagsghp tsccsaaeim avlffhtmry kaldprnphn drfvlskgha apilyavwae
      121 agflpeaell nlrkissdld ghpvpkqaft dvatgslgqg lgaacgmayt gkyfdkasyr
      181 vycmlgdgev segsvweama fagiykldnl vaifdinrlg qsdpaplqhq vdvyqkrcea
      241 fgwhaiivdg hsveelckaf gqakhqptai iaktfkgrgi tgiedkeawh gkplpknmae
      301 qiiqeiysqv qskkkilatp pqedapsvdi anirmptppn ykvgdkiatr kayglalakl
      361 ghasdriial dgdtknstfs elfkkehpdr fiecyiaeqn mvsiavgcat rdrtvpfcst
      421 faafftrafd qirmaaises ninlcgshcg vsigedgpsq maledlamfr svpmstvfyp
      481 sdgvatekav elaantkgic firtsrpena iiysnnedfq vgqakvvlks kddqvtviga
      541 gvtlhealaa aemlkkekig vrvldpftik pldkklildc aratkgrilt vedhyyeggi
      601 geavsaavvg epgvtvtrla vsqvprsgkp aellkmfgid kdaivqavkg lvtkg
//
LOCUS       NP_001423547            1786 aa            linear   ROD 20-MAR-2025
DEFINITION  CDK5 regulatory subunit-associated protein 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423547 XP_063143294
VERSION     NP_001423547.1
DBSOURCE    REFSEQ: accession NM_001436618.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1786)
  AUTHORS   Bouguenina,H., Salaun,D., Mangon,A., Muller,L., Baudelet,E.,
            Camoin,L., Tachibana,T., Cianferani,S., Audebert,S.,
            Verdier-Pinard,P. and Badache,A.
  TITLE     EB1-binding-myomegalin protein complex promotes centrosomal
            microtubules functions
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10687-E10696 (2017)
   PUBMED   29162697
REFERENCE   2  (residues 1 to 1786)
  AUTHORS   Gao,F.J., Shi,L., Hines,T., Hebbar,S., Neufeld,K.L. and Smith,D.S.
  TITLE     Insulin signaling regulates a functional interaction between
            adenomatous polyposis coli and cytoplasmic dynein
  JOURNAL   Mol Biol Cell 28 (5), 587-599 (2017)
   PUBMED   28057765
REFERENCE   3  (residues 1 to 1786)
  AUTHORS   Park,J.S., Lee,M.K., Kang,S., Jin,Y., Fu,S., Rosales,J.L. and
            Lee,K.Y.
  TITLE     Species-Specific Expression of Full-Length and Alternatively
            Spliced Variant Forms of CDK5RAP2
  JOURNAL   PLoS One 10 (11), e0142577 (2015)
   PUBMED   26550838
  REMARK    GeneRIF: mouse expresses only one form of CDK5RAP2 that is
            equivalent to the human and rat alternatively spliced variant forms
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1786)
  AUTHORS   Mori,Y., Inoue,Y., Tanaka,S., Doda,S., Yamanaka,S., Fukuchi,H. and
            Terada,Y.
  TITLE     Cep169, a Novel Microtubule Plus-End-Tracking Centrosomal Protein,
            Binds to CDK5RAP2 and Regulates Microtubule Stability
  JOURNAL   PLoS One 10 (10), e0140968 (2015)
   PUBMED   26485573
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1786)
  AUTHORS   Yigit,G., Brown,K.E., Kayserili,H., Pohl,E., Caliebe,A.,
            Zahnleiter,D., Rosser,E., Bogershausen,N., Uyguner,Z.O.,
            Altunoglu,U., Nurnberg,G., Nurnberg,P., Rauch,A., Li,Y., Thiel,C.T.
            and Wollnik,B.
  TITLE     Mutations in CDK5RAP2 cause Seckel syndrome
  JOURNAL   Mol Genet Genomic Med 3 (5), 467-480 (2015)
   PUBMED   26436113
REFERENCE   6  (residues 1 to 1786)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   7  (residues 1 to 1786)
  AUTHORS   Hassan,M.J., Khurshid,M., Azeem,Z., John,P., Ali,G., Chishti,M.S.
            and Ahmad,W.
  TITLE     Previously described sequence variant in CDK5RAP2 gene in a
            Pakistani family with autosomal recessive primary microcephaly
  JOURNAL   BMC Med Genet 8, 58 (2007)
   PUBMED   17764569
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1786)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
REFERENCE   9  (residues 1 to 1786)
  AUTHORS   Wang,X., Ching,Y.P., Lam,W.H., Qi,Z., Zhang,M. and Wang,J.H.
  TITLE     Identification of a common protein association region in the
            neuronal Cdk5 activator
  JOURNAL   J Biol Chem 275 (41), 31763-31769 (2000)
   PUBMED   10915792
REFERENCE   10 (residues 1 to 1786)
  AUTHORS   Ching,Y.P., Qi,Z. and Wang,J.H.
  TITLE     Cloning of three novel neuronal Cdk5 activator binding proteins
  JOURNAL   Gene 242 (1-2), 285-294 (2000)
   PUBMED   10721722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_063143294.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.156251.1,
                                           SRR26360181.1307425.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1786
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..1786
                     /product="CDK5 regulatory subunit-associated protein 2
                     isoform 1"
                     /note="CDK5 activator-binding protein C48"
                     /calculated_mol_wt=202310
     Region          61..129
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          146..>455
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1371..>1551
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..1786
                     /gene="Cdk5rap2"
                     /coded_by="NM_001436618.1:169..5529"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:286919"
                     /db_xref="RGD:708451"
ORIGIN      
        1 mmdsgmeedv tlpgtlsgcs glhpvlpsdl dvisdttglg ngvlpimsee kvsptrarnm
       61 kdfenqitel kkenfnlklr iyfleeriqq efagptehiy kknielkvev eslkrelqer
      121 dqllvkaska veslaegggs eiqrvkedar kkvqqveell tkrihlleed vkaaqaelek
      181 afagteteka lrlsleskls amkkmqegdl emtlaleekd rlieelklsl kskealiqcl
      241 keeksqmasp denvssgelr glsatlreek erdaeerqke rnhfeeriqa lqedlreker
      301 eiatekknsl krdkaiqglt malkskekev eelnsiikel tadstqsrea plktqvsefe
      361 esenceaala ekeallaklh senvtknten hrllrnvkkv tqelndlkke klrlerdlee
      421 ahregnrgar tihdlrneve klrkevcere kavekhyksl pgessskfhs qeqvvkglte
      481 sasqedlllq ksnekdleai qqncylmtae elkfgsdgli tekcsqqspd sklifskekq
      541 qseyegltgd lkteqnvyah laknlqdtds klqaelkrvl alrkqleqdv layrnlqtal
      601 qeqlseirkr eeepfsfysd qtsylsicle ehsqfqlehf sqeeikkkvi dliqlvkdlh
      661 adnqhlkkti fdiscmgvqg ndrlestkqa eimedyaegg gkdgyvrhmd snildhdgah
      721 tpdtsedhsl edellsllat ffskkatpsl esrpdllkal galllericl aeqgspgdhs
      781 dskaekaleq vavrlrdelg hsclansfsk shselksprg twlvktgdea kvelksvsvq
      841 tmtiedstrg fkperkreaw agkpeeavfs telesealge mpglqathls fpsaidkddq
      901 ktglliqlkt pellenlynl pasqevvaql qgqvlelqke lkeykirnkq lldklilaea
      961 mmegmavpns tpvnvpaaqa vvrtafqgkp geqeghetth sagrdkevds dqytsfeids
     1021 eicppddlal lpackenled flgppsiaty ldsksqlsvk vsvvgtdqse ninlpddtea
     1081 lkqkihdlqt elegyrniiv qlqkhsqcse aiitvlcgte gaqdglnkpk ghideeemtf
     1141 sslhqvryvk hmkilrpltp eiidgkmles lkqqlveqeq elqkeqdlnl elfgeihnlq
     1201 nkfrdlspsr ydslvqsqar elslqrqqik dshdicvvch qhmstmikaf eellqasdvd
     1261 scvaegfreq ltqcaglleq leklflhgks arvephtqte llrrlrteed nlpyqhllpe
     1321 spepsashal sddemseksf lsrepkpdse tekyptiasr fpqdllmehi qeirtlrkhl
     1381 eesiktnekl rkqlerqgce tdqgstnvsa ysselhnslt seiqflrkqn ealstmlekg
     1441 skekqkenek lreslarkte slehlqleya svreenerlr rdisekerqn qqltqevcss
     1501 lqelsrvqee aksrqqlllq kdellqslqm elkvyeklae ehqklqqdvn kcpeasdnsf
     1561 dlfestqama pksasetpvl sgtdvdslsc dstssatsps cmpclvagrh lwasksghhm
     1621 lcliedydal ykqiswgqtl lakmdiqtqe alsptsqklg pkasfsvpls kflssmntak
     1681 lilekasrll klfwrvsvpt ngqcslhcdq igemkaeitk lhkklfeqek klqntakllq
     1741 qskhqekiif dqlvithqvl rkargnlelr praahpgtss psrpgs
//
LOCUS       NP_001099382             459 aa            linear   ROD 20-MAR-2025
DEFINITION  sorting nexin-8 [Rattus norvegicus].
ACCESSION   NP_001099382 XP_001065004 XP_006248982 XP_221947
VERSION     NP_001099382.2
DBSOURCE    REFSEQ: accession NM_001105912.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   van Weering,J.R., Sessions,R.B., Traer,C.J., Kloer,D.P.,
            Bhatia,V.K., Stamou,D., Carlsson,S.R., Hurley,J.H. and Cullen,P.J.
  TITLE     Molecular basis for SNX-BAR-mediated assembly of distinct endosomal
            sorting tubules
  JOURNAL   EMBO J 31 (23), 4466-4480 (2012)
   PUBMED   23085988
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Dyve,A.B., Bergan,J., Utskarpen,A. and Sandvig,K.
  TITLE     Sorting nexin 8 regulates endosome-to-Golgi transport
  JOURNAL   Biochem Biophys Res Commun 390 (1), 109-114 (2009)
   PUBMED   19782049
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Mar 13, 2025 this sequence version replaced
            XP_006248982.1, NP_001099382.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.45737.1,
                                           SRR26643285.56527.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..459
                     /product="sorting nexin-8"
                     /calculated_mol_wt=52016
     Region          70..173
                     /region_name="PX_SNX8_Mvp1p_like"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 8 and yeast Mvp1p; cd06866"
                     /db_xref="CDD:132776"
     Site            order(104..106,130..131,143)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132776"
     Region          190..434
                     /region_name="BAR_SNX8"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 8; cd07597"
                     /db_xref="CDD:153281"
     Site            order(212,215..216,220,222..223,226..227,229..230,
                     247..248,250..251,254..255,257..258,261,290,293..294,395,
                     398..399,401,406,409..410,412..413,416..417,420..421,
                     423..424,427..428,430..431)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153281"
     Site            order(212,215..216,220,222..223,226,229..230,247..248,
                     250..251,254,257..258,261,290,395,398..399,401,406,
                     409..410,412..414,416..417,420..421,423..424,428,430..431)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153281"
     CDS             1..459
                     /gene="Snx8"
                     /coded_by="NM_001105912.2:21..1400"
                     /db_xref="GeneID:288504"
                     /db_xref="RGD:1305791"
ORIGIN      
        1 mtgramdplp spavaaaaea eadeeadppa tgpqtsqvte wrnldprrmq mpqgnpllls
       61 ytlqellakd tvqvelipek kglflkhvey evssqrfkss vyrryndfvv fhevllhkfp
      121 yrmvpalppk rvlgadrefi egrrralkrf inlvarhppf sedvllklfl sfsgsdvqhk
      181 lkeaaqcvgd eftncklaar akdflpadiq tqfamsreli rnvynsfykl rdraeriasr
      241 aidnaadlli fgkelsalgs dttplpswaa lhlstwgslk qalkglsvef alladkaaqq
      301 gkkeendvve klnlfldllq sykdlcerhe kgvlhkhqra lhkyglmkrq mmsaahgrep
      361 esveqlesri veqenviqtm elrnyfslyc lhqetqlvhv ylpltshilg afvnsqiqgh
      421 kemskvwndl kpklsclfag phsvltpprs pqedgmcph
//
LOCUS       NP_001423443            1203 aa            linear   ROD 20-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 38 [Rattus
            norvegicus].
ACCESSION   NP_001423443 XP_063121646
VERSION     NP_001423443.1
DBSOURCE    REFSEQ: accession NM_001436514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Miotto,B., Chibi,M., Xie,P., Koundrioukoff,S., Moolman-Smook,H.,
            Pugh,D., Debatisse,M., He,F., Zhang,L. and Defossez,P.A.
  TITLE     The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common
            fragile site stability
  JOURNAL   Cell Rep 7 (2), 575-587 (2014)
   PUBMED   24726359
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Filion,G.J., Zhenilo,S., Salozhin,S., Yamada,D., Prokhortchouk,E.
            and Defossez,P.A.
  TITLE     A family of human zinc finger proteins that bind methylated DNA and
            repress transcription
  JOURNAL   Mol Cell Biol 26 (1), 169-181 (2006)
   PUBMED   16354688
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Kiefer,H., Chatail-Hermitte,F., Ravassard,P., Bayard,E., Brunet,I.
            and Mallet,J.
  TITLE     ZENON, a novel POZ Kruppel-like DNA binding protein associated with
            differentiation and/or survival of late postmitotic neurons
  JOURNAL   Mol Cell Biol 25 (5), 1713-1729 (2005)
   PUBMED   15713629
  REMARK    GeneRIF: ZENON is involved in the maintenance of panneuronal
            features and/or in the survival of mature neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_063121646.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1342618.1,
                                           SRR26643287.20999.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676811 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..1203
                     /product="zinc finger and BTB domain-containing protein
                     38"
                     /note="zenon; zinc finger protein expressed in neurons;
                     zinc finger transcription factor Kaiso"
                     /calculated_mol_wt=135144
     Region          15..128
                     /region_name="BTB_POZ_ZBTB38_CIBZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 38 (ZBTB38); cd18223"
                     /db_xref="CDD:349532"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3; propagated from
                     UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          230..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          299..522
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000250|UniProtKB:Q8NAP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          308..401
                     /region_name="zf-C2H2_8"
                     /note="C2H2-type zinc ribbon; pfam15909"
                     /db_xref="CDD:464935"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(343,346,359,363)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          372..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..481
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(461,464,477,481)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(466,468,470,472..473,476..477,480,494,496,500..501,
                     504..505,508,522,524,526,528..529,532..533)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          489..509
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          517..535
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          731..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          857..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          895..914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     Region          1019..1039
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1019,1022,1035,1039)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(1024,1026,1028,1030..1031,1034..1035,1038,1052,1054,
                     1058..1059,1062..1063,1066,1080,1082,1084,1086..1087,
                     1090..1091,1094)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1032..1055
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1045..1067
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1047..1067
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1075..1095
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1088..>1106
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1103..1123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1134..1154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1172..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EXX3.1)"
     CDS             1..1203
                     /gene="Zbtb38"
                     /gene_synonym="RGD1310136"
                     /coded_by="NM_001436514.1:162..3773"
                     /db_xref="GeneID:315936"
                     /db_xref="RGD:1310136"
ORIGIN      
        1 mtvmslsrdl kddfhsdtvl silneqrirg ilcdvtiive dtkfkahsnv laasslyfkn
       61 ifwshticis shvlelddlk aevfteilny iysstvvvrr qetvtdlaaa gkrlgisfle
      121 dlsdrnfsns pgpyvvcite kgvvkeekne krheepavtn gpritnafsi ietensnsmf
      181 spldlrasfk kvsdamrtts lcqerasvcp eaepvrtlae hsyavssite ayrsqplreh
      241 dsssssgktg kengealttk akpcrkpktq tqdsdstten mplplvtcpe vnqerspqpa
      301 pilshsepps segdvhfpre denqpsetpg ppaaevpplv yncsccsksf dsstllgahm
      361 qlhkptqdpf vckycnkqft tlnrldrheq icmrsshmpm pggnqpflen yptigqdggs
      421 ftspdslvpe srigelssag salsdadhmv kfvngqmlys cvvckrsyvt lsslrrhanv
      481 hswrrtypch ycnkvfalae yrtrheiwht gerryqcifc letfmtyyil knhqksfhai
      541 dhrlsiskkt angglkptvy pyklyrllpm rckrapyksy rnssyesaqg nrqrnesppd
      601 tfvipnlpss emptlnfqdg rnsltsspai pvetpswqgt ptsakvknae glkwrkqalk
      661 tdlvdsaevs issignsvst tlqaepvcvs sgehsasvis ysgsvpsviv hssqfssvik
      721 hsnaiaclan snhqspsqpv aspslikdsk peadkaskla srpknskekk ktvpcnrgei
      781 teeakyvadl ggssgkttnv veetskiety iakpalpgts tnsnvaplcq itvkigneai
      841 vkrhilgskl fykrgrkpky qmqeetlpre sdpetrgdsp lglcqadcve mseafdevsd
      901 qdstdkpwrp yynykpkkks kqlrkirkvk wrkergsrsp vgrrrypael draemgrrry
      961 paeldrcaev klppdkasee eenkempklq celcdgdkaa gagaegkphq hltlkpyice
     1021 lcakqfqsss tlkmhmrcht gekpyqcktc grrfsvqgnl qkherihlgv keficqycnk
     1081 aftlnetlki herihtgekr yhcqfcfqgf lylstkrnhe rrhvrehdgk gfacfqcpki
     1141 cktaaalrmh qkkhlfktlt kqeetddlch ensdllesqp ctdsedsdqk ddikkpllkm
     1201 sfe
//
LOCUS       NP_001423462             581 aa            linear   ROD 20-MAR-2025
DEFINITION  cysteine/serine-rich nuclear protein 1 [Rattus norvegicus].
ACCESSION   NP_001423462 XP_006244183
VERSION     NP_001423462.1
DBSOURCE    REFSEQ: accession NM_001436533.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Ye,X., Lin,J., Lin,Z., Xue,A., Li,L., Zhao,Z., Liu,L., Shen,Y. and
            Cong,B.
  TITLE     Axin1 up-regulated 1 accelerates stress-induced cardiomyocytes
            apoptosis through activating Wnt/beta-catenin signaling
  JOURNAL   Exp Cell Res 359 (2), 441-448 (2017)
   PUBMED   28830684
  REMARK    GeneRIF: Axud1 mediated stress-induced cardiomyocytes apoptosis
            through activating Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Gingras,S., Pelletier,S., Boyd,K. and Ihle,J.N.
  TITLE     Characterization of a family of novel cysteine- serine-rich nuclear
            proteins (CSRNP)
  JOURNAL   PLoS One 2 (8), e808 (2007)
   PUBMED   17726538
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Schmahl,J., Raymond,C.S. and Soriano,P.
  TITLE     PDGF signaling specificity is mediated through multiple immediate
            early genes
  JOURNAL   Nat Genet 39 (1), 52-60 (2007)
   PUBMED   17143286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 14, 2025 this sequence version replaced XP_006244183.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.35941.1,
                                           SRR26643284.11898.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680412,
                                           SAMN06680413 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..581
                     /product="cysteine/serine-rich nuclear protein 1"
                     /note="AXIN1 up-regulated 1"
                     /calculated_mol_wt=62329
     Region          77..301
                     /region_name="CSRNP_N"
                     /note="Cysteine/serine-rich nuclear protein N-terminus;
                     pfam16019"
                     /db_xref="CDD:464977"
     CDS             1..581
                     /gene="Csrnp1"
                     /gene_synonym="Axud1"
                     /coded_by="NM_001436533.1:171..1916"
                     /db_xref="GeneID:363165"
                     /db_xref="RGD:1305999"
ORIGIN      
        1 magiqkrkfd qleeddcsss slssgdlsps ppsssaspaw tseeeglgdq ppqpdqdssg
       61 iqslmppsil kraprerpgh vafdgitvyy fprcqgftsv pshggctlgm asrhstcrlf
      121 slaefkqeqf rarreklrrr lkeeklemlk wklsvsgvpe agadvpltvd aiddasveed
      181 lavavaggrl eeanflqpyp prqrrallra sgvrridree krelqalrqs redcgchcdg
      241 vcdpetcsci lagikcqmdh tsfpcgccse gcenphgrve fnqarvqthf ihtltrlqme
      301 qgaeslgdpe spmedvpveq tvvspfppsk ptmsndlgds scgsdmtdss ttyssggsgs
      361 rseapnhlah pslpgssfrs gidedsleqi lnfsdsdlgi eeeeeeggsv gnldnlscfh
      421 ladifgtgdp gslaswthsq fgsslpsgil denanldasc flssgleglr egslpsssgs
      481 pegeaaqsss ldlslsscds fellqslpdy slgphytsrr vsgsldslet fhpspsfspp
      541 rdasfldsli glsepvtdvl apllesqfed tavvpldpvp v
//
LOCUS       NP_001423709             632 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423709 XP_063131265
VERSION     NP_001423709.1
DBSOURCE    REFSEQ: accession NM_001436780.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131265.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.320967.1,
                                           SRR26360181.1153706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..632
                     /product="transcriptional repressor p66-alpha isoform 2"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67625
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..632
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436780.1:250..2148"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq vikprrklaf rsgeardwnn gsvlqtssql srgsattprg
      541 vlhtfsqspk lqnaasatal vsrtgrhser vvgtskgtas nwkktplstg gtlafvspsl
      601 avhksssavd rqreylldmi pprsipqsat wk
//
LOCUS       NP_001423708             632 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423708 XP_038950269
VERSION     NP_001423708.1
DBSOURCE    REFSEQ: accession NM_001436779.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038950269.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50362.1,
                                           SRR26643290.47731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..632
                     /product="transcriptional repressor p66-alpha isoform 2"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67625
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..632
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436779.1:300..2198"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq vikprrklaf rsgeardwnn gsvlqtssql srgsattprg
      541 vlhtfsqspk lqnaasatal vsrtgrhser vvgtskgtas nwkktplstg gtlafvspsl
      601 avhksssavd rqreylldmi pprsipqsat wk
//
LOCUS       NP_001423717             607 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423717 XP_063131274
VERSION     NP_001423717.1
DBSOURCE    REFSEQ: accession NM_001436788.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131274.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.71135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..607
                     /product="transcriptional repressor p66-alpha isoform 5"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=64744
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..607
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436788.1:308..2131"
                     /note="isoform 5 is encoded by transcript variant 15"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq tssqlsrgsa ttprgvlhtf sqspklqnaa satalvsrtg
      541 rhservvgts kgtasnwkkt plstggtlaf vspslavhks ssavdrqrey lldmipprsi
      601 pqsatwk
//
LOCUS       NP_001423700             332 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423700 XP_038965815
VERSION     NP_001423700.1
DBSOURCE    REFSEQ: accession NM_001436771.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038965815.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.254249.1,
                                           SRR22399489.587421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..332
                     /product="PC4 and SFRS1-interacting protein isoform 4"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=37363
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          <109..>324
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..332
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436771.1:283..1281"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekqkrkgg rnfqaahrrn
      301 mlkgqhekea adrkrkqeeq metehqttcn lq
//
LOCUS       NP_001423742             722 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423742
VERSION     NP_001423742.1
DBSOURCE    REFSEQ: accession NM_001436813.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2870990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..722
                     /product="cilia- and flagella-associated protein 97
                     isoform 5"
                     /calculated_mol_wt=81334
     Region          535..637
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..722
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436813.1:186..2354"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mwtrlvwtps eiclpllsey wnqritrlqh lcrkpsqmsk ptaaswlyeq vmpwtagrpw
       61 rspfheppsl lealprscrp ysaglitvtg slgtmddrsa artifgrdsv prsprlspsa
      121 eslprsfrpr srvresplas nawegemwcg cacaertrtr tlgaaresva atvprytfgi
      181 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
      241 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      301 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      361 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      421 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      481 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      541 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      601 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      661 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppnvrta
      721 wl
//
LOCUS       NP_001423769             825 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 10 [Rattus
            norvegicus].
ACCESSION   NP_001423769
VERSION     NP_001423769.1
DBSOURCE    REFSEQ: accession NM_001436840.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20636.1,
                                           SRR26360186.1521925.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..825
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 10"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=92625
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          315..>660
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <527..722
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..825
                     /gene="Srrm1"
                     /coded_by="NM_001436840.1:405..2882"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 lkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkekspel pepsvrmkds svqeatstsd ilkapkpepv pepkepspek
      181 nskkekektr prsrsrsksr srtrsrspsh trprrrhrsr srsysprrrp sprrrpsprr
      241 rtpprrmppp prhrrsrspg rrrrrssasl sgssssssss rsrsppkkpp krtsspprkt
      301 rrlspsaspp rrrhrpsspa tpppktrhsp tpqqsnrark srvsvspgrt sgkvtkhkgt
      361 ekrespspap kprkvelses eedkgskmaa adsvqqrrqy rrqnqqsssd sgssstsede
      421 rpkrshvkng evgrrrrhsp srsaspsprk rqketsprsr rrrspspppa rrrrspspap
      481 pppppppprr rrsptppprr rtpsppprrr spsprryspp iqrryspspp pkrrtasppp
      541 ppkrraspsp ppkrrvshsp ppkqrsppvt krrspslssk hrkgsspgrs trearspqpn
      601 krhspsprpr apqtsspppv rrgasaspqg rqspspstrp irrvsrtpep kkikkaasps
      661 pqsvrrvsss rsvsgspept akkppappsp vqsqspstnw spaapakkak sptpspspar
      721 nsdqegggkk kkkkkdkkhk kdkkhkkhkk hkkekavava tpapaapaav saaatpsaqe
      781 epaaapeprk eteseaeddn lddlerhlre kalrsmrkaq vspqs
//
LOCUS       NP_001423694             606 aa            linear   ROD 21-MAR-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423694 XP_063143669
VERSION     NP_001423694.1
DBSOURCE    REFSEQ: accession NM_001436765.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Loh,K.H., Stawski,P.S., Draycott,A.S., Udeshi,N.D., Lehrman,E.K.,
            Wilton,D.K., Svinkina,T., Deerinck,T.J., Ellisman,M.H., Stevens,B.,
            Carr,S.A. and Ting,A.Y.
  TITLE     Proteomic Analysis of Unbounded Cellular Compartments: Synaptic
            Clefts
  JOURNAL   Cell 166 (5), 1295-1307 (2016)
   PUBMED   27565350
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143669.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.298814.1,
                                           SRR26360172.766690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840109, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21-q22"
     Protein         1..606
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2
                     precursor"
                     /note="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2"
                     /calculated_mol_wt=65220
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2949
     Region          27..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          39..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          48..>340
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          59..82
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          131..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          155..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          203..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          251..274
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          275..298
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          299..322
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          323..343
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          327..>391
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          411..500
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          428..432
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          441..445
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..485
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          493..496
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..606
                     /gene="Lingo2"
                     /gene_synonym="RGD1310773"
                     /coded_by="NM_001436765.1:228..2048"
                     /db_xref="GeneID:313156"
                     /db_xref="RGD:1310773"
ORIGIN      
        1 mlhtaipcwq pflglamvll fmgstigcpa rcecsaqnks vschrrrlia ipegipietk
       61 ildlsknrlk sinpeefisy plleeidlsd niianvepga fnnlfnlrsl rlkgnrlklv
      121 plgvftglsn ltkldisenk ivilldymfq dlhnlkslev gdndlvyish rafsglfsle
      181 qltlekcnlt avptealshl rslitlhlkh lninnmpvya fkrlfhlkql eidywplldm
      241 mpanslygln ltslsitntn lstvpflafk hlvylthlnl synpistiea gmfsdlirlq
      301 elhvvgaqlr tiephsfqgl rflrvlnvsq nlletleenv fsspralevl sinnnplacd
      361 crllwllqrq atlqfggqqp mcagpdtire rsfkdfhsta lsfyftckkp kirekklqhl
      421 lvdegqtvql ecnadgdpqp viswvtprrr fittksngra tvlgdgtlei rfaqdqdsgm
      481 yvciasnaag ndtftasltv kgftsdrfly anrtpmymtd sndtvsngtn antfsldlkt
      541 ilvstamgcf tflgvvlfcf lllfvwsrgk gkhknsidle yvprknngav aegevagprr
      601 fnmkmi
//
LOCUS       NP_001423705             633 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423705 XP_038950267
VERSION     NP_001423705.1
DBSOURCE    REFSEQ: accession NM_001436776.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038950267.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50360.1,
                                           SRR26643285.50322.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..633
                     /product="transcriptional repressor p66-alpha isoform 1"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67753
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          420..453
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..633
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436776.1:410..2311"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qqihnirqhs stgpppllla prasvpsmqi qgqriiqqgl irvanvpnts
      301 llvnipqpta aslkgttvgs aqanstpssv asvvasaesp asrqaaakla lrkqlektll
      361 eipppkppap emnflpsaan nefiylvgle evvqnlletq agrisatsaa avlsrepymc
      421 vqcktdftcr wrekggavmc encmtsnqkk alkvehtsrl kaafvkalqq eqemeqrllq
      481 qgvgtasika etaaphpslk qvikprrkla frsgeardwn ngsvlqtssq lsrgsattpr
      541 gvlhtfsqsp klqnaasata lvsrtgrhse rvvgtskgta snwkktplst ggtlafvsps
      601 lavhksssav drqreylldm ipprsipqsa twk
//
LOCUS       NP_001423706             632 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423706 XP_063131264
VERSION     NP_001423706.1
DBSOURCE    REFSEQ: accession NM_001436777.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131264.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55837.1,
                                           SRR26643298.71134.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..632
                     /product="transcriptional repressor p66-alpha isoform 2"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67625
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..632
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436777.1:410..2308"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq vikprrklaf rsgeardwnn gsvlqtssql srgsattprg
      541 vlhtfsqspk lqnaasatal vsrtgrhser vvgtskgtas nwkktplstg gtlafvspsl
      601 avhksssavd rqreylldmi pprsipqsat wk
//
LOCUS       NP_001423727             529 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423727
VERSION     NP_001423727.1
DBSOURCE    REFSEQ: accession NM_001436798.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.19794.1,
                                           SRR26643290.19817.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..529
                     /product="mesoderm induction early response protein 1
                     isoform b"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=60084
     Region          199..248
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          305..349
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(305,335..336,338..339,341..343,345..347)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          359..>505
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..529
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436798.1:205..1794"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mfmfnwftdc lwilflsnyk psvessspgg saasedhefd psadmlvhdf ddertleeee
       61 mmegetnfss eiedlaregd mpidellsly gygstvqlpe eeeeeeeeee egeddedadn
      121 ddnsgcsgen keenikdssg qedetqssnd dpsqsvtsqd aqeiirprrc kyfdtnseie
      181 eeseededyi psedwkkeim vgsmfqaeip vgvcrykene kvyenddqll wdpeylpedk
      241 vivflkdasr rtgdekgvea ipegshikdn eqalyelvkc sfdteealrr lrfnvkaare
      301 elsvwteeec rnfeqglkay gkdfhliqan kvrtrsvgec vafyymwkks erydffaqqt
      361 rfgkkkynlh pgvtdymdrl ldesesaass rapsppptas nsstsqseke dgtlsnsnqn
      421 gvssngpgei lnkeevkveg lhvngptggn kkplltdvdt ngyeennlat dpklahmtar
      481 nendfdekne rpakrrrins sgkespgsse ffqeavshgk feehentnd
//
LOCUS       NP_001124484             512 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001124484 XP_001058293 XP_233245
VERSION     NP_001124484.2
DBSOURCE    REFSEQ: accession NM_001131012.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced NP_001124484.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168252.1, SRR26360194.741127.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..512
                     /product="mesoderm induction early response protein 1
                     isoform c"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=57813
     Region          182..231
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          288..332
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(288,318..319,321..322,324..326,328..330)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          342..>488
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..512
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001131012.2:114..1652"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 maepsvesss pggsaasedh efdpsadmlv hdfddertle eeemmegetn fsseiedlar
       61 egdmpidell slygygstvq lpeeeeeeee eeeegedded adnddnsgcs genkeenikd
      121 ssgqedetqs snddpsqsvt sqdaqeiirp rrckyfdtns eieeeseede dyipsedwkk
      181 eimvgsmfqa eipvgvcryk enekvyendd qllwdpeylp edkvivflkd asrrtgdekg
      241 veaipegshi kdneqalyel vkcsfdteea lrrlrfnvka areelsvwte eecrnfeqgl
      301 kaygkdfhli qankvrtrsv gecvafyymw kkserydffa qqtrfgkkky nlhpgvtdym
      361 drlldesesa assrapsppp tasnsstsqs ekedgtlsns nqngvssngp geilnkeevk
      421 veglhvngpt ggnkkplltd vdtngyeenn latdpklahm tarnendfde knerpakrrr
      481 inssgkespg sseffqeavs hgkfeehent nd
//
LOCUS       NP_001423703             327 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423703 XP_017448855
VERSION     NP_001423703.1
DBSOURCE    REFSEQ: accession NM_001436774.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017448855.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.15199.1,
                                           SRR22399489.1781504.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..327
                     /product="PC4 and SFRS1-interacting protein isoform 7"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=36777
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Region          <85..284
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..327
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436774.1:283..1266"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekkrkggr nfqaahrrnm
      301 lkgqhekeaa drkrkqeeqm etehfal
//
LOCUS       NP_001423760             289 aa            linear   ROD 21-MAR-2025
DEFINITION  complement C1q tumor necrosis factor-related protein 7 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_001423760 XP_038947870
VERSION     NP_001423760.1
DBSOURCE    REFSEQ: accession NM_001436831.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Bi,J., Duan,Y., Wang,M., He,C., Li,X., Zhang,X., Tao,Y., Du,Y. and
            Liu,H.
  TITLE     Deletion of large-conductance calcium-activated potassium channels
            promotes vascular remodelling through the CTRP7-mediated PI3K/Akt
            signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (12), 1-11 (2022)
   PUBMED   36514218
  REMARK    GeneRIF: Deletion of large-conductance calcium-activated potassium
            channels promotes vascular remodelling through the CTRP7-mediated
            PI3K/Akt signaling pathway.
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Rohrbach,S., Aurich,A.C., Li,L. and Niemann,B.
  TITLE     Age-associated loss in adiponectin-activation by caloric
            restriction: lack of compensation by enhanced inducibility of
            adiponectin paralogs CTRP2 and CTRP7
  JOURNAL   Mol Cell Endocrinol 277 (1-2), 26-34 (2007)
   PUBMED   17716811
  REMARK    GeneRIF: The purpose of the current study was to investigate
            age-dependent effects of caloric restriction on the release of
            adiponectin, expression and activation of adiponectin-related
            signaling and on parameters of altered insulin sensitivity.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Wong,G.W., Wang,J., Hug,C., Tsao,T.S. and Lodish,H.F.
  TITLE     A family of Acrp30/adiponectin structural and functional paralogs
  JOURNAL   Proc Natl Acad Sci U S A 101 (28), 10302-10307 (2004)
   PUBMED   15231994
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038947870.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.35039.1,
                                           SRR26643299.54756.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..289
                     /product="complement C1q tumor necrosis factor-related
                     protein 7 isoform 1 precursor"
                     /note="complement C1q tumor necrosis factor-related
                     protein 7; C1q and tumor necrosis factor related protein
                     7; adiponectin g"
                     /calculated_mol_wt=28867
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1654
     Region          <56..>137
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          149..273
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..289
                     /gene="C1qtnf7"
                     /gene_synonym="Adig; Ctrp7"
                     /coded_by="NM_001436831.1:160..1029"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:305423"
                     /db_xref="RGD:1306978"
ORIGIN      
        1 mivllyvtsl aicasgqprg nqakgesysp ryicsipglp gppgppgang spgphgrigl
       61 pgrdgrdgrk gekgekgtag lkgktgplgl agekgdqget gkkgpigpeg ekgevgpagp
      121 pgpkgdrgdq gdpglpgvcr cgsivlksaf svgittsype erlpiifnkv lfnegehynp
      181 atgkficafp giyyfsydit lankhlaigl vhngqyrirt fdantgnhdv asgstviylq
      241 pedevwleif fndqnglfsd pgwadslfsg fllyvdtdyl dsiseddel
//
LOCUS       NP_001013903             630 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 3 [Rattus norvegicus].
ACCESSION   NP_001013903 XP_214308
VERSION     NP_001013903.2
DBSOURCE    REFSEQ: accession NM_001013881.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Dec 18, 2009 this sequence version replaced NP_001013903.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74318.1,
                                           SRR26643296.35378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..630
                     /product="transcriptional repressor p66-alpha isoform 3"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67438
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          417..450
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..630
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001013881.3:410..2302"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqqi hnirqhsstg ppplllapra svpsmqiqgq riiqqglirv anvpntsllv
      301 nipqptaasl kgttvgsaqa nstpssvasv vasaespasr qaaaklalrk qlektlleip
      361 ppkppapemn flpsaannef iylvgleevv qnlletqagr isatsaaavl srepymcvqc
      421 ktdftcrwre kggavmcenc mtsnqkkalk vehtsrlkaa fvkalqqeqe meqrllqqgv
      481 gtasikaeta aphpslkqvi kprrklafrs geardwnngs vlqtssqlsr gsattprgvl
      541 htfsqspklq naasatalvs rtgrhservv gtskgtasnw kktplstggt lafvspslav
      601 hksssavdrq reylldmipp rsipqsatwk
//
LOCUS       NP_001423713             629 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423713 XP_063131272
VERSION     NP_001423713.1
DBSOURCE    REFSEQ: accession NM_001436784.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131272.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.58574.1,
                                           SRR26643297.46808.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..629
                     /product="transcriptional repressor p66-alpha isoform 4"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67310
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          416..449
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..629
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436784.1:308..2197"
                     /note="isoform 4 is encoded by transcript variant 11"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqih nirqhsstgp pplllapras vpsmqiqgqr iiqqglirva nvpntsllvn
      301 ipqptaaslk gttvgsaqan stpssvasvv asaespasrq aaaklalrkq lektlleipp
      361 pkppapemnf lpsaannefi ylvgleevvq nlletqagri satsaaavls repymcvqck
      421 tdftcrwrek ggavmcencm tsnqkkalkv ehtsrlkaaf vkalqqeqem eqrllqqgvg
      481 tasikaetaa phpslkqvik prrklafrsg eardwnngsv lqtssqlsrg sattprgvlh
      541 tfsqspklqn aasatalvsr tgrhservvg tskgtasnwk ktplstggtl afvspslavh
      601 ksssavdrqr eylldmippr sipqsatwk
//
LOCUS       NP_001423768             891 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 9 [Rattus
            norvegicus].
ACCESSION   NP_001423768 XP_063143837
VERSION     NP_001423768.1
DBSOURCE    REFSEQ: accession NM_001436839.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 891)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 891)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143837.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.29592.1,
                                           SRR26360194.275228.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..891
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 9"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=100143
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          348..>695
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <593..788
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..891
                     /gene="Srrm1"
                     /coded_by="NM_001436839.1:26..2701"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkeks pelpepsvrm kdssvqeats tsdilkapkp epvpepkeps peknskkeke
      241 ktrprsrsrs ksrsrtrsrs pshtrprrrh rsrsrsyspr rrpsprrrps prrrtpprrm
      301 pppprhrrsr spgrrrrrss aslsgsssss sssrsrsppk kppkrtsspp rktrrlspsa
      361 spprrrhrps spatpppktr hsptpqqsnr arksrvsvsp grtsgkvtkh kgtekresps
      421 papkprkvel seseedkgsk maaadsvqqr rqyrrqnqqs ssdsgsssts ederpkrshv
      481 kngevgrrrr hspsrsasps prkrqketsp rmqmgkrwqs pvtksrrrrs psppparrrr
      541 spspappppp pppprrrrsp tppprrrtps ppprrrspsp rrysppiqrr yspspppkrr
      601 taspppppkr raspspppkr rvshspppkq rsppvtkrrs pslsskhrkg sspgrstrea
      661 rspqpnkrhs psprprapqt sspppvrrga saspqgrqsp spstrpirrv srtpepkkik
      721 kaaspspqsv rrvsssrsvs gspeptakkp pappspvqsq spstnwspaa pakkaksptp
      781 spsparnsdq egggkkkkkk kdkkhkkdkk hkkhkkhkke kavavatpap aapaavsaaa
      841 tpsaqeepaa apeprketes eaeddnlddl erhlrekalr smrkaqvspq s
//
LOCUS       NP_001423702             328 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423702 XP_038965816
VERSION     NP_001423702.1
DBSOURCE    REFSEQ: accession NM_001436773.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038965816.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.21683.1,
                                           SRR26643298.27719.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..328
                     /product="PC4 and SFRS1-interacting protein isoform 6"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=36905
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          <109..>324
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..328
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436773.1:283..1269"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekqkrkgg rnfqaahrrn
      301 mlkgqhekea adrkrkqeeq metehfal
//
LOCUS       NP_001423718             605 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423718 XP_063131275
VERSION     NP_001423718.1
DBSOURCE    REFSEQ: accession NM_001436789.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131275.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.71136.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..605
                     /product="transcriptional repressor p66-alpha isoform 6"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=64558
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          417..450
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..605
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436789.1:410..2227"
                     /note="isoform 6 is encoded by transcript variant 16"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqqi hnirqhsstg ppplllapra svpsmqiqgq riiqqglirv anvpntsllv
      301 nipqptaasl kgttvgsaqa nstpssvasv vasaespasr qaaaklalrk qlektlleip
      361 ppkppapemn flpsaannef iylvgleevv qnlletqagr isatsaaavl srepymcvqc
      421 ktdftcrwre kggavmcenc mtsnqkkalk vehtsrlkaa fvkalqqeqe meqrllqqgv
      481 gtasikaeta aphpslkqts sqlsrgsatt prgvlhtfsq spklqnaasa talvsrtgrh
      541 servvgtskg tasnwkktpl stggtlafvs pslavhksss avdrqreyll dmipprsipq
      601 satwk
//
LOCUS       NP_001423707             632 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423707 XP_063131267
VERSION     NP_001423707.1
DBSOURCE    REFSEQ: accession NM_001436778.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131267.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.53660.1,
                                           SRR26643284.18527.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..632
                     /product="transcriptional repressor p66-alpha isoform 2"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67625
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..632
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436778.1:308..2206"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq vikprrklaf rsgeardwnn gsvlqtssql srgsattprg
      541 vlhtfsqspk lqnaasatal vsrtgrhser vvgtskgtas nwkktplstg gtlafvspsl
      601 avhksssavd rqreylldmi pprsipqsat wk
//
LOCUS       NP_001423695             473 aa            linear   ROD 21-MAR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX49 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423695
VERSION     NP_001423695.1
DBSOURCE    REFSEQ: accession NM_001436766.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Awasthi,S., Verma,M., Mahesh,A., K Khan,M.I., Govindaraju,G.,
            Rajavelu,A., Chavali,P.L., Chavali,S. and Dhayalan,A.
  TITLE     DDX49 is an RNA helicase that affects translation by regulating
            mRNA export and the levels of pre-ribosomal RNA
  JOURNAL   Nucleic Acids Res 46 (12), 6304-6317 (2018)
   PUBMED   29618122
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1234396.1,
                                           SRR26360176.227984.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..473
                     /product="probable ATP-dependent RNA helicase DDX49
                     isoform 2"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase DDX49; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 49"
                     /calculated_mol_wt=53228
     Region          1..434
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     CDS             1..473
                     /gene="Ddx49"
                     /coded_by="NM_001436766.1:31..1452"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290660"
                     /db_xref="RGD:1311124"
ORIGIN      
        1 magfaelrls swlveqcrql glkqptpvql gcipailegr dclgcaktgs gktaafvlpi
       61 lqklsedpyg ifclvltptr elayqiaeqf rvlgkplglk dciivggmdm vtqalelsrk
      121 phvviatpgr ladhlrssnt fnmkkirflv ldeadrlleq gctdftadle tilsavparr
      181 qtllfsatlt dtlkelqgla tnqpffweaq atvrtveqld qryllvpekv kdaylvhlvq
      241 tfqdqledcs iiiftntckt cqilcmmlrk fnfptvalhs mmkqkerfaa larfksstyr
      301 iliatdvasr gldiptvqvv inhntpglpk iyihrvgrta ragrqgqait lvtqydihll
      361 haieeeikqq laelaveeaq vlqiltqvnv kleashfdek keinkrkqmi legkdpdlea
      421 krkaelakik qqnrrfkekv eqtlrqqkag stgrrsrppr prpqeparae aqn
//
LOCUS       NP_001013154             284 aa            linear   ROD 21-MAR-2025
DEFINITION  DNA-binding protein RFXANK isoform 2 [Rattus norvegicus].
ACCESSION   NP_001013154 XP_224739
VERSION     NP_001013154.1
DBSOURCE    REFSEQ: accession NM_001013136.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   McKinsey,T.A., Kuwahara,K., Bezprozvannaya,S. and Olson,E.N.
  TITLE     Class II histone deacetylases confer signal responsiveness to the
            ankyrin-repeat proteins ANKRA2 and RFXANK
  JOURNAL   Mol Biol Cell 17 (1), 438-447 (2006)
   PUBMED   16236793
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Louise-Plence,P.,
            Prochnicka-Chalufour,A., Selz,F., Picard,C., Le Deist,F.,
            Eliaou,J.F., Fischer,A. and Lisowska-Grospierre,B.
  TITLE     Novel mutations in the RFXANK gene: RFX complex containing
            in-vitro-generated RFXANK mutant binds the promoter without
            transactivating MHC II
  JOURNAL   Immunogenetics 54 (11), 747-755 (2003)
   PUBMED   12618906
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 20, 2005 this sequence version replaced XP_224739.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087111.1, SRR26360194.2550749.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..284
                     /product="DNA-binding protein RFXANK isoform 2"
                     /note="DNA-binding protein RFXANK"
                     /calculated_mol_wt=30612
     Region          72..273
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          118..145
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(147,149,153..154,157..159,161..162,166,169,178,180,
                     182,186..187,190..192,194..195,199,202,211,213,215,
                     219..220,223..225,227..228,232,235)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          147..178
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          180..211
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          213..241
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..284
                     /gene="Rfxank"
                     /coded_by="NM_001013136.2:214..1068"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:306353"
                     /db_xref="RGD:1311390"
ORIGIN      
        1 meptqvaenl ipnqqslapd ledpedrrde spdssdtvvl slfpctpdav npeadasass
       61 lqvpaasvwt plaqaqtpge qalpllagsf lkhsttltnr qrgnevsalp atldslsihq
      121 laaqgelsql kdhlrkgdnl vnkpdergft pliwasafge ietvrflldw gadphilake
      181 resalslasm ggytdivrll ldrdvdiniy dwnggtplly avrgnhvkcv eallargadl
      241 tteadsgytp mdlavalgyr kvqqvmeshi lklfqgtlgp adpe
//
LOCUS       NP_001423696             470 aa            linear   ROD 21-MAR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX49 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423696
VERSION     NP_001423696.1
DBSOURCE    REFSEQ: accession NM_001436767.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Awasthi,S., Verma,M., Mahesh,A., K Khan,M.I., Govindaraju,G.,
            Rajavelu,A., Chavali,P.L., Chavali,S. and Dhayalan,A.
  TITLE     DDX49 is an RNA helicase that affects translation by regulating
            mRNA export and the levels of pre-ribosomal RNA
  JOURNAL   Nucleic Acids Res 46 (12), 6304-6317 (2018)
   PUBMED   29618122
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.1351704.1,
                                           SRR21887623.2151621.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..470
                     /product="probable ATP-dependent RNA helicase DDX49
                     isoform 3"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase DDX49; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 49"
                     /calculated_mol_wt=52916
     Region          1..431
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     CDS             1..470
                     /gene="Ddx49"
                     /coded_by="NM_001436767.1:31..1443"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:290660"
                     /db_xref="RGD:1311124"
ORIGIN      
        1 magfaelrls swlveqcrql glkqptpvql gcipailegr dclgcaktgs gktaafvlpi
       61 lqklsedpyg ifclvltptr elayqiaeqf rvlgkplglk dciivggmdm vtqalelsrk
      121 phvviatpgr ladhlrssnt fnmkkirflv ldeadrlleq gctdftadle tilsavparr
      181 qtllfsatlt dtlkelqgla tnqpffweaq atvrtveqld qryllvpekv kdaylvhlvq
      241 tfqdqledcs iiiftntckt cqilcmmlrk fnfptvalhs mmkqkerfaa larfksstyr
      301 iliatdvasr gldiptvqvv inhntpglpk iyihrvgrta ragrqgqait lvtqydihll
      361 haieeeikqq laelaveeaq vlqiltqkle ashfdekkei nkrkqmileg kdpdleakrk
      421 aelakikqqn rrfkekveqt lrqqkagstg rrsrpprprp qeparaeaqn
//
LOCUS       NP_001423738             548 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423738 XP_008769486
VERSION     NP_001423738.1
DBSOURCE    REFSEQ: accession NM_001436809.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_008769486.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2795976.1,
                                           SRR26360181.138198.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..548
                     /product="cilia- and flagella-associated protein 97
                     isoform 2"
                     /calculated_mol_wt=61612
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          85..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          355..457
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          497..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     CDS             1..548
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436809.1:164..1810"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
       61 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      121 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      181 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      241 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      301 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      361 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      421 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      481 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppniqcs
      541 nskvlrsh
//
LOCUS       NP_001423710             630 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423710 XP_063131269
VERSION     NP_001423710.1
DBSOURCE    REFSEQ: accession NM_001436781.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131269.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.52413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..630
                     /product="transcriptional repressor p66-alpha isoform 3"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67438
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          417..450
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..630
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436781.1:308..2200"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqqi hnirqhsstg ppplllapra svpsmqiqgq riiqqglirv anvpntsllv
      301 nipqptaasl kgttvgsaqa nstpssvasv vasaespasr qaaaklalrk qlektlleip
      361 ppkppapemn flpsaannef iylvgleevv qnlletqagr isatsaaavl srepymcvqc
      421 ktdftcrwre kggavmcenc mtsnqkkalk vehtsrlkaa fvkalqqeqe meqrllqqgv
      481 gtasikaeta aphpslkqvi kprrklafrs geardwnngs vlqtssqlsr gsattprgvl
      541 htfsqspklq naasatalvs rtgrhservv gtskgtasnw kktplstggt lafvspslav
      601 hksssavdrq reylldmipp rsipqsatwk
//
LOCUS       NP_001423698             529 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423698 XP_006238415
VERSION     NP_001423698.1
DBSOURCE    REFSEQ: accession NM_001436769.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238415.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19296.1,
                                           SRR26643295.21680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..529
                     /product="PC4 and SFRS1-interacting protein isoform 2"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=59613
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          <109..524
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          339..416
                     /region_name="Integrase-binding domain (IBD).
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          348..449
                     /region_name="LEDGF"
                     /note="Lens epithelium-derived growth factor (LEDGF);
                     pfam11467"
                     /db_xref="CDD:463284"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          445..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..529
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436769.1:283..1872"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekqkrkgg rnfqaahrrn
      301 mlkgqhekea adrkrkqeeq meteqqtkde gkkpevkkve kkretsmdsr lqrihaeikn
      361 slkidnldvn rciealdela slqvtmqqaq khtemittlk kirrfkvsqv imekstmlyn
      421 kfknmflvge gdsvitqvln kslaeqrqhe eanktkdqgk kgpnkkleke qtgtkslngg
      481 sdaqesnhpq hngdsaeesk dsreagsktk tpgeereaev slkestldn
//
LOCUS       NP_001423722             652 aa            linear   ROD 21-MAR-2025
DEFINITION  histone-lysine N-methyltransferase NSD3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423722 XP_008769572
VERSION     NP_001423722.1
DBSOURCE    REFSEQ: accession NM_001436793.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Black,J.C., Van Rechem,C. and Whetstine,J.R.
  TITLE     Histone lysine methylation dynamics: establishment, regulation, and
            biological impact
  JOURNAL   Mol Cell 48 (4), 491-507 (2012)
   PUBMED   23200123
  REMARK    Review article
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Rahman,S., Sowa,M.E., Ottinger,M., Smith,J.A., Shi,Y., Harper,J.W.
            and Howley,P.M.
  TITLE     The Brd4 extraterminal domain confers transcription activation
            independent of pTEFb by recruiting multiple proteins, including
            NSD3
  JOURNAL   Mol Cell Biol 31 (13), 2641-2652 (2011)
   PUBMED   21555454
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Kim,S.M., Kee,H.J., Eom,G.H., Choe,N.W., Kim,J.Y., Kim,Y.S.,
            Kim,S.K., Kook,H., Kook,H. and Seo,S.B.
  TITLE     Characterization of a novel WHSC1-associated SET domain protein
            with H3K4 and H3K27 methyltransferase activity
  JOURNAL   Biochem Biophys Res Commun 345 (1), 318-323 (2006)
   PUBMED   16682010
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Rosati,R., La Starza,R., Veronese,A., Aventin,A., Schwienbacher,C.,
            Vallespi,T., Negrini,M., Martelli,M.F. and Mecucci,C.
  TITLE     NUP98 is fused to the NSD3 gene in acute myeloid leukemia
            associated with t(8;11)(p11.2;p15)
  JOURNAL   Blood 99 (10), 3857-3860 (2002)
   PUBMED   11986249
  REMARK    Erratum:[Blood 2002 Aug 15;100(4):1132]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_008769572.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.50999.1,
                                           SRR26643429.50972.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..652
                     /product="histone-lysine N-methyltransferase NSD3 isoform
                     2"
                     /EC_number="2.1.1.354"
                     /note="histone-lysine N-methyltransferase NSD3;
                     Wolf-Hirschhorn syndrome candidate 1-like 1"
                     /calculated_mol_wt=72688
     Region          275..404
                     /region_name="PWWP_NSD3_rpt1"
                     /note="first PWWP domain found in nuclear SET
                     domain-containing protein 3 (NSD3) and similar proteins;
                     cd20163"
                     /db_xref="CDD:438991"
     Site            order(288,291,319)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438991"
     Site            289..292
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438991"
     Site            order(356..358,361..362)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438991"
     CDS             1..652
                     /gene="Nsd3"
                     /gene_synonym="Whsc1l1"
                     /coded_by="NM_001436793.1:525..2483"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:290831"
                     /db_xref="RGD:1308980"
ORIGIN      
        1 mdfsfsfmqg imgntiqqpp qlidsanirq edafdnnsdi vedggptpfe atlqqgfqcp
       61 patedlpplt ngyppsisly etqtkyppys qypngsangf gavrnfsptd yyhseipntr
      121 pheilekpsp pqpppppllp pppppvpqtv ipkktgspei klkitktiqn grelfesslc
      181 gdllnevqas ehlkskhesr kekrkkssrh essrseerks hkvpklepeg qnrpnervdp
      241 apekpreepv lkeavpvqpi lssvpttets tgvkfqvgdl vwskvgtypw wpcmvssdpq
      301 levhtkintr gareyhvqff snqperawvh ekrvreykgh eqyeellaea akqasnhsek
      361 qkirkprpqr eraqwdigia haekalqmtr eerveqytfi yidkqpeesp sqakksvtsk
      421 aevkkprrpr svgnsqpeqt sagevaspqs stdprrqsqr rhtsveedgp ppvkiawrta
      481 aarkslpasi tmhkgsldlh kcnmspvvki eqvfalqnat gdgkfidqfv ystkgignkt
      541 eisvrgqdrl iisspsqrne kstpsasppe atsgsagpve kkqqrrsirt rsesekstev
      601 vskkkikkeq vetspqaslk tglqkgsadr gaqgsvrfsd lsvsaakeet vd
//
LOCUS       NP_001423756             262 aa            linear   ROD 21-MAR-2025
DEFINITION  R-spondin-1 precursor [Rattus norvegicus].
ACCESSION   NP_001423756
VERSION     NP_001423756.1
DBSOURCE    REFSEQ: accession NM_001436827.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Li,J.Y., Wu,X., Lee,A., Zhou,S.Y. and Owyang,C.
  TITLE     Altered R-spondin 1/CART neurocircuit in the hypothalamus
            contributes to hyperphagia in diabetes
  JOURNAL   J Neurophysiol 121 (3), 928-939 (2019)
   PUBMED   30649980
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Szenker-Ravi,E., Altunoglu,U., Leushacke,M., Bosso-Lefevre,C.,
            Khatoo,M., Thi Tran,H., Naert,T., Noelanders,R., Hajamohideen,A.,
            Beneteau,C., de Sousa,S.B., Karaman,B., Latypova,X., Basaran,S.,
            Yucel,E.B., Tan,T.T., Vlaminck,L., Nayak,S.S., Shukla,A.,
            Girisha,K.M., Le Caignec,C., Soshnikova,N., Uyguner,Z.O.,
            Vleminckx,K., Barker,N., Kayserili,H. and Reversade,B.
  TITLE     RSPO2 inhibition of RNF43 and ZNRF3 governs limb development
            independently of LGR4/5/6
  JOURNAL   Nature 557 (7706), 564-569 (2018)
   PUBMED   29769720
  REMARK    Erratum:[Nature. 2018 Sep;561(7722):E7. doi:
            10.1038/s41586-018-0296-7. PMID: 29977062]
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Li,J.Y., Chai,B., Zhang,W., Fritze,D.M., Zhang,C. and
            Mulholland,M.W.
  TITLE     LGR4 and its ligands, R-spondin 1 and R-spondin 3, regulate food
            intake in the hypothalamus of male rats
  JOURNAL   Endocrinology 155 (2), 429-440 (2014)
   PUBMED   24280058
  REMARK    GeneRIF: These data indicate that Rspo1 and Rspo3 and their
            receptor LGR4 form novel circuits in the brain to regulate energy
            homeostasis.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Niehrs,C.
  TITLE     The complex world of WNT receptor signalling
  JOURNAL   Nat Rev Mol Cell Biol 13 (12), 767-779 (2012)
   PUBMED   23151663
  REMARK    Review article
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Ruffner,H., Sprunger,J., Charlat,O., Leighton-Davies,J.,
            Grosshans,B., Salathe,A., Zietzling,S., Beck,V., Therier,M.,
            Isken,A., Xie,Y., Zhang,Y., Hao,H., Shi,X., Liu,D., Song,Q.,
            Clay,I., Hintzen,G., Tchorz,J., Bouchez,L.C., Michaud,G., Finan,P.,
            Myer,V.E., Bouwmeester,T., Porter,J., Hild,M., Bassilana,F.,
            Parker,C.N. and Cong,F.
  TITLE     R-Spondin potentiates Wnt/beta-catenin signaling through orphan
            receptors LGR4 and LGR5
  JOURNAL   PLoS One 7 (7), e40976 (2012)
   PUBMED   22815884
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Carmon,K.S., Gong,X., Lin,Q., Thomas,A. and Liu,Q.
  TITLE     R-spondins function as ligands of the orphan receptors LGR4 and
            LGR5 to regulate Wnt/beta-catenin signaling
  JOURNAL   Proc Natl Acad Sci U S A 108 (28), 11452-11457 (2011)
   PUBMED   21693646
REFERENCE   7  (residues 1 to 262)
  AUTHORS   de Lau,W., Barker,N., Low,T.Y., Koo,B.K., Li,V.S., Teunissen,H.,
            Kujala,P., Haegebarth,A., Peters,P.J., van de Wetering,M.,
            Stange,D.E., van Es,J.E., Guardavaccaro,D., Schasfoort,R.B.,
            Mohri,Y., Nishimori,K., Mohammed,S., Heck,A.J. and Clevers,H.
  TITLE     Lgr5 homologues associate with Wnt receptors and mediate R-spondin
            signalling
  JOURNAL   Nature 476 (7360), 293-297 (2011)
   PUBMED   21727895
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Binnerts,M.E., Kim,K.A., Bright,J.M., Patel,S.M., Tran,K., Zhou,M.,
            Leung,J.M., Liu,Y., Lomas,W.E. 3rd, Dixon,M., Hazell,S.A.,
            Wagle,M., Nie,W.S., Tomasevic,N., Williams,J., Zhan,X., Levy,M.D.,
            Funk,W.D. and Abo,A.
  TITLE     R-Spondin1 regulates Wnt signaling by inhibiting internalization of
            LRP6
  JOURNAL   Proc Natl Acad Sci U S A 104 (37), 14700-14705 (2007)
   PUBMED   17804805
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Nam,J.S., Turcotte,T.J., Smith,P.F., Choi,S. and Yoon,J.K.
  TITLE     Mouse cristin/R-spondin family proteins are novel ligands for the
            Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent
            gene expression
  JOURNAL   J Biol Chem 281 (19), 13247-13257 (2006)
   PUBMED   16543246
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Kamata,T., Katsube,K., Michikawa,M., Yamada,M., Takada,S. and
            Mizusawa,H.
  TITLE     R-spondin, a novel gene with thrombospondin type 1 domain, was
            expressed in the dorsal neural tube and affected in Wnts mutants
  JOURNAL   Biochim Biophys Acta 1676 (1), 51-62 (2004)
   PUBMED   14732490
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.1530093.1,
                                           SRR21887623.3215805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..262
                     /product="R-spondin-1 precursor"
                     /calculated_mol_wt=26749
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2139
     Region          42..142
                     /region_name="Furin-like_2"
                     /note="Furin-like repeat, cysteine-rich; pfam15913"
                     /db_xref="CDD:464939"
     Region          148..203
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     CDS             1..262
                     /gene="Rspo1"
                     /gene_synonym="RGD1565558"
                     /coded_by="NM_001436827.1:830..1618"
                     /db_xref="GeneID:313589"
                     /db_xref="RGD:1565558"
ORIGIN      
        1 mrlglcvval vlswthlavg srgikgkrqr risaegsqsc akgcelcsev ngclkcspkl
       61 fillerndir qvgvclpscp pgyfdarnpd mnkcikckie hceacfshnf ctkcqeglyl
      121 hkgrcypacp egstaanstm ecgspaqcem sewspwgpcs kkrklcgfrk gseertrrvl
      181 hapggdqtnc sdtketrkct vrrtpcpegq krkkasqgrr enanrhptrk nskepgsnsr
      241 rhkgqqqpqp gtagpltsvg pt
//
LOCUS       NP_001423739            1062 aa            linear   ROD 21-MAR-2025
DEFINITION  lysine-specific demethylase 4A isoform a [Rattus norvegicus].
ACCESSION   NP_001423739 XP_006238730
VERSION     NP_001423739.1
DBSOURCE    REFSEQ: accession NM_001436810.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Li,L., Ding,Z., Ma,F., Zhang,K., Lu,D., Wang,H. and Yang,K.
  TITLE     Spinal nerve transection-induced upregulation of KDM4A in the
            dorsal root ganglia contributes to the development and maintenance
            of neuropathic pain via promoting CCL2 expression in rats
  JOURNAL   Eur J Neurosci 60 (6), 5169-5188 (2024)
   PUBMED   39136140
  REMARK    GeneRIF: Spinal nerve transection-induced upregulation of KDM4A in
            the dorsal root ganglia contributes to the development and
            maintenance of neuropathic pain via promoting CCL2 expression in
            rats.
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Li,W., Zhang,Y., Lv,J., Zhang,Y., Bai,J., Zhen,L. and He,X.
  TITLE     MicroRNA-137-mediated lysine demethylase 4A regulates the recovery
            of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis
  JOURNAL   Int J Neurosci 133 (1), 37-50 (2023)
   PUBMED   33499717
  REMARK    GeneRIF: MicroRNA-137-mediated lysine demethylase 4A regulates the
            recovery of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Liu,Y., Zhao,L., Zhang,J., Lv,L., Han,K., Huang,C. and Xu,Z.
  TITLE     Histone Demethylase KDM4A Inhibition Represses Neuroinflammation
            and Improves Functional Recovery in Ischemic Stroke
  JOURNAL   Curr Pharm Des 27 (21), 2528-2536 (2021)
   PUBMED   33402077
  REMARK    GeneRIF: Histone Demethylase KDM4A Inhibition Represses
            Neuroinflammation and Improves Functional Recovery in Ischemic
            Stroke.
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Qin,G., Li,Y., Wang,H., Yang,J., Chen,Q., Tang,H., Wang,Y.,
            Zhang,M., Jiang,T., Lin,S. and Huo,S.
  TITLE     Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation
            via Regulating the Binding Ability of H3K9me3 with the Promoters of
            Runx2, Osterix and Osteocalcin
  JOURNAL   J Biomed Nanotechnol 16 (6), 899-909 (2020)
   PUBMED   33187585
  REMARK    GeneRIF: Lysine-Specific Demethylase 4A Regulates Osteogenic
            Differentiation via Regulating the Binding Ability of H3K9me3 with
            the Promoters of Runx2, Osterix and Osteocalcin.
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Johansson,C., Velupillai,S., Tumber,A., Szykowska,A., Hookway,E.S.,
            Nowak,R.P., Strain-Damerell,C., Gileadi,C., Philpott,M.,
            Burgess-Brown,N., Wu,N., Kopec,J., Nuzzi,A., Steuber,H., Egner,U.,
            Badock,V., Munro,S., LaThangue,N.B., Westaway,S., Brown,J.,
            Athanasou,N., Prinjha,R., Brennan,P.E. and Oppermann,U.
  TITLE     Structural analysis of human KDM5B guides histone demethylase
            inhibitor development
  JOURNAL   Nat Chem Biol 12 (7), 539-545 (2016)
   PUBMED   27214403
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Sohi,G., Marchand,K., Revesz,A., Arany,E. and Hardy,D.B.
  TITLE     Maternal protein restriction elevates cholesterol in adult rat
            offspring due to repressive changes in histone modifications at the
            cholesterol 7alpha-hydroxylase promoter
  JOURNAL   Mol Endocrinol 25 (5), 785-798 (2011)
   PUBMED   21372147
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Trojer,P., Zhang,J., Yonezawa,M., Schmidt,A., Zheng,H., Jenuwein,T.
            and Reinberg,D.
  TITLE     Dynamic Histone H1 Isotype 4 Methylation and Demethylation by
            Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji
            Domain-containing JMJD2/KDM4 Proteins
  JOURNAL   J Biol Chem 284 (13), 8395-8405 (2009)
   PUBMED   19144645
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Fodor,B.D., Kubicek,S., Yonezawa,M., O'Sullivan,R.J., Sengupta,R.,
            Perez-Burgos,L., Opravil,S., Mechtler,K., Schotta,G. and
            Jenuwein,T.
  TITLE     Jmjd2b antagonizes H3K9 trimethylation at pericentric
            heterochromatin in mammalian cells
  JOURNAL   Genes Dev 20 (12), 1557-1562 (2006)
   PUBMED   16738407
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Gray,S.G., Iglesias,A.H., Lizcano,F., Villanueva,R., Camelo,S.,
            Jingu,H., Teh,B.T., Koibuchi,N., Chin,W.W., Kokkotou,E. and
            Dangond,F.
  TITLE     Functional characterization of JMJD2A, a histone deacetylase- and
            retinoblastoma-binding protein
  JOURNAL   J Biol Chem 280 (31), 28507-28518 (2005)
   PUBMED   15927959
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Zhang,D., Yoon,H.G. and Wong,J.
  TITLE     JMJD2A is a novel N-CoR-interacting protein and is involved in
            repression of the human transcription factor achaete scute-like
            homologue 2 (ASCL2/Hash2)
  JOURNAL   Mol Cell Biol 25 (15), 6404-6414 (2005)
   PUBMED   16024779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238730.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.28610.1,
                                           SRR26643295.22389.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1062
                     /product="lysine-specific demethylase 4A isoform a"
                     /EC_number="1.14.11.-"
                     /note="lysine-specific demethylase 4A; jumonji domain
                     containing 2A; lysine (K)-specific demethylase 4A"
                     /calculated_mol_wt=120270
     Region          13..55
                     /region_name="JmjN"
                     /note="Small domain found in the jumonji family of
                     transcription factors; smart00545"
                     /db_xref="CDD:128818"
     Region          175..291
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          665..764
                     /region_name="PHD_JMJD2A"
                     /note="PHD finger found in Jumonji domain-containing
                     protein 2A (JMJD2A); cd15575"
                     /db_xref="CDD:277050"
     Site            order(665,732..736,740,759)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277050"
     Region          773..882
                     /region_name="ePHD_JMJD2A"
                     /note="Extended PHD finger (ePHD) found in Jumonji
                     domain-containing protein 2A (JMJD2A); cd15713"
                     /db_xref="CDD:277183"
     Site            order(827,841..845,851,877)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277183"
     Region          897..951
                     /region_name="Tudor_JMJD2A_rpt1"
                     /note="first Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20463"
                     /db_xref="CDD:410534"
     Site            order(929..930,932..935,937)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410534"
     Region          954..1009
                     /region_name="Tudor_JMJD2A_rpt2"
                     /note="second Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20466"
                     /db_xref="CDD:410537"
     Site            order(965..967,971)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410537"
     CDS             1..1062
                     /gene="Kdm4a"
                     /gene_synonym="Jmjd2a"
                     /coded_by="NM_001436810.1:101..3289"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:313539"
                     /db_xref="RGD:1306378"
ORIGIN      
        1 masesetlnp sarimtfypt meefrnfsry iayiesqgah raglakvvpp kewkprtsyd
       61 diddlvipap iqqlvtgqsg lftqyniqkk amtvrefrki ansdkyctpr ysefeelerk
      121 ywknltfnpp iygadvngtl yeqhvdewni grlktildlv ekesgitieg vntpylyfgm
      181 wktsfawhte dmdlysinyl hfgepkswys vppehgkrle rlakgffpgs aqsceaflrh
      241 kmtlisplml kkygipfdkv tqeagefmit fpygyhagfn hgfncaestn fatrrwieyg
      301 kqavlcscrk dmvkismdvf vrrfqperyk lwkagkdstv idhtlptpea aeflkdsglt
      361 pragneecpe edseaaeqge egdvkrslak hrigtkrhrv cleipqevsq selfpkeels
      421 sgqyemtecq atlapvrpth ssvrqvedsl pfpdysdpte vkfeelknvk leeededeep
      481 eaaaldlsvn pesvegrlvf sgskkkasss lgssssqdsv ssdsettesv scqgqektvl
      541 tvhsysrgdg kaapgepsvk rqrsaprsis eqelaevade ymlsleenkk tkgrrqplsk
      601 lprhhplvlq ecgsddetse qltpeeeaee teawakplsq lwqnrppnfe aekefnelma
      661 qqaphcavcm ifqtyhqvef ggfsqscgna sepaaqpqrt kplipemcft ttgcstdinl
      721 stpyleedgt smlvsckkcs vrvhascygv ppakaseewm csrcsanale edcclcslrg
      781 galqranddr wvhvscavai learfvniae rspvdvskip lprfklkcvf ckkrrkrnag
      841 ccvqcshgrc ptafhvscaq aagvmmqpdd wpfvvfitcf rhkipnlera kgallsitag
      901 qkviskhkng rfyqcevvrl ttetfyevnf ddgsfsdnly pedivsqdcl qlgppaegev
      961 vqvrwtdgqv ygakfvashp iqmyqvefed gsqlvvkrdd vytldeelpk rvksrlsvas
     1021 dmrfneifte kevkqekkrq rvinsryred yiepalyrai me
//
LOCUS       NP_001014023             548 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001014023 XP_224861
VERSION     NP_001014023.1
DBSOURCE    REFSEQ: accession NM_001014001.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 20, 2005 this sequence version replaced XP_224861.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082052.1, SRR26643293.74872.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..548
                     /product="cilia- and flagella-associated protein 97
                     isoform 2"
                     /calculated_mol_wt=61612
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          85..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          355..457
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          497..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     CDS             1..548
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001014001.2:184..1830"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
       61 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      121 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      181 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      241 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      301 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      361 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      421 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      481 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppniqcs
      541 nskvlrsh
//
LOCUS       NP_001423719             604 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423719 XP_063131277
VERSION     NP_001423719.1
DBSOURCE    REFSEQ: accession NM_001436790.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131277.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74317.1,
                                           SRR26643429.50357.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..604
                     /product="transcriptional repressor p66-alpha isoform 7"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=64430
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          416..449
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..604
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436790.1:410..2224"
                     /note="isoform 7 is encoded by transcript variant 17"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqih nirqhsstgp pplllapras vpsmqiqgqr iiqqglirva nvpntsllvn
      301 ipqptaaslk gttvgsaqan stpssvasvv asaespasrq aaaklalrkq lektlleipp
      361 pkppapemnf lpsaannefi ylvgleevvq nlletqagri satsaaavls repymcvqck
      421 tdftcrwrek ggavmcencm tsnqkkalkv ehtsrlkaaf vkalqqeqem eqrllqqgvg
      481 tasikaetaa phpslkqtss qlsrgsattp rgvlhtfsqs pklqnaasat alvsrtgrhs
      541 ervvgtskgt asnwkktpls tggtlafvsp slavhksssa vdrqreylld mipprsipqs
      601 atwk
//
LOCUS       NP_001423721             652 aa            linear   ROD 21-MAR-2025
DEFINITION  histone-lysine N-methyltransferase NSD3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423721
VERSION     NP_001423721.1
DBSOURCE    REFSEQ: accession NM_001436792.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Black,J.C., Van Rechem,C. and Whetstine,J.R.
  TITLE     Histone lysine methylation dynamics: establishment, regulation, and
            biological impact
  JOURNAL   Mol Cell 48 (4), 491-507 (2012)
   PUBMED   23200123
  REMARK    Review article
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Rahman,S., Sowa,M.E., Ottinger,M., Smith,J.A., Shi,Y., Harper,J.W.
            and Howley,P.M.
  TITLE     The Brd4 extraterminal domain confers transcription activation
            independent of pTEFb by recruiting multiple proteins, including
            NSD3
  JOURNAL   Mol Cell Biol 31 (13), 2641-2652 (2011)
   PUBMED   21555454
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Kim,S.M., Kee,H.J., Eom,G.H., Choe,N.W., Kim,J.Y., Kim,Y.S.,
            Kim,S.K., Kook,H., Kook,H. and Seo,S.B.
  TITLE     Characterization of a novel WHSC1-associated SET domain protein
            with H3K4 and H3K27 methyltransferase activity
  JOURNAL   Biochem Biophys Res Commun 345 (1), 318-323 (2006)
   PUBMED   16682010
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Rosati,R., La Starza,R., Veronese,A., Aventin,A., Schwienbacher,C.,
            Vallespi,T., Negrini,M., Martelli,M.F. and Mecucci,C.
  TITLE     NUP98 is fused to the NSD3 gene in acute myeloid leukemia
            associated with t(8;11)(p11.2;p15)
  JOURNAL   Blood 99 (10), 3857-3860 (2002)
   PUBMED   11986249
  REMARK    Erratum:[Blood 2002 Aug 15;100(4):1132]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1488534.1,
                                           SRR26360186.2158604.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..652
                     /product="histone-lysine N-methyltransferase NSD3 isoform
                     2"
                     /EC_number="2.1.1.354"
                     /note="histone-lysine N-methyltransferase NSD3;
                     Wolf-Hirschhorn syndrome candidate 1-like 1"
                     /calculated_mol_wt=72688
     Region          275..404
                     /region_name="PWWP_NSD3_rpt1"
                     /note="first PWWP domain found in nuclear SET
                     domain-containing protein 3 (NSD3) and similar proteins;
                     cd20163"
                     /db_xref="CDD:438991"
     Site            order(288,291,319)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438991"
     Site            289..292
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438991"
     Site            order(356..358,361..362)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438991"
     CDS             1..652
                     /gene="Nsd3"
                     /gene_synonym="Whsc1l1"
                     /coded_by="NM_001436792.1:449..2407"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290831"
                     /db_xref="RGD:1308980"
ORIGIN      
        1 mdfsfsfmqg imgntiqqpp qlidsanirq edafdnnsdi vedggptpfe atlqqgfqcp
       61 patedlpplt ngyppsisly etqtkyppys qypngsangf gavrnfsptd yyhseipntr
      121 pheilekpsp pqpppppllp pppppvpqtv ipkktgspei klkitktiqn grelfesslc
      181 gdllnevqas ehlkskhesr kekrkkssrh essrseerks hkvpklepeg qnrpnervdp
      241 apekpreepv lkeavpvqpi lssvpttets tgvkfqvgdl vwskvgtypw wpcmvssdpq
      301 levhtkintr gareyhvqff snqperawvh ekrvreykgh eqyeellaea akqasnhsek
      361 qkirkprpqr eraqwdigia haekalqmtr eerveqytfi yidkqpeesp sqakksvtsk
      421 aevkkprrpr svgnsqpeqt sagevaspqs stdprrqsqr rhtsveedgp ppvkiawrta
      481 aarkslpasi tmhkgsldlh kcnmspvvki eqvfalqnat gdgkfidqfv ystkgignkt
      541 eisvrgqdrl iisspsqrne kstpsasppe atsgsagpve kkqqrrsirt rsesekstev
      601 vskkkikkeq vetspqaslk tglqkgsadr gaqgsvrfsd lsvsaakeet vd
//
LOCUS       NP_001423732             376 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform h [Rattus
            norvegicus].
ACCESSION   NP_001423732 XP_063143767
VERSION     NP_001423732.1
DBSOURCE    REFSEQ: accession NM_001436803.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143767.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.22222.1,
                                           SRR26360194.1671406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..376
                     /product="mesoderm induction early response protein 1
                     isoform h"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=43175
     Region          181..230
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          287..331
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(287,317..318,320..321,323..325,327..329)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          341..>360
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..376
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436803.1:170..1300"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mlpsvesssp ggsaasedhe fdpsadmlvh dfddertlee eemmegetnf sseiedlare
       61 gdmpidells lygygstvql peeeeeeeee eeegeddeda dnddnsgcsg enkeenikds
      121 sgqedetqss nddpsqsvts qdaqeiirpr rckyfdtnse ieeeseeded yipsedwkke
      181 imvgsmfqae ipvgvcryke nekvyenddq llwdpeylpe dkvivflkda srrtgdekgv
      241 eaipegshik dneqalyelv kcsfdteeal rrlrfnvkaa reelsvwtee ecrnfeqglk
      301 aygkdfhliq ankvrtrsvg ecvafyymwk kserydffaq qtrfgkkkyn lhpgvtmkri
      361 cpccpqplra plqgrd
//
LOCUS       NP_001423704             633 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423704 XP_017455524
VERSION     NP_001423704.1
DBSOURCE    REFSEQ: accession NM_001436775.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017455524.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.55452.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..633
                     /product="transcriptional repressor p66-alpha isoform 1"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67753
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          420..453
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..633
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436775.1:308..2209"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qqihnirqhs stgpppllla prasvpsmqi qgqriiqqgl irvanvpnts
      301 llvnipqpta aslkgttvgs aqanstpssv asvvasaesp asrqaaakla lrkqlektll
      361 eipppkppap emnflpsaan nefiylvgle evvqnlletq agrisatsaa avlsrepymc
      421 vqcktdftcr wrekggavmc encmtsnqkk alkvehtsrl kaafvkalqq eqemeqrllq
      481 qgvgtasika etaaphpslk qvikprrkla frsgeardwn ngsvlqtssq lsrgsattpr
      541 gvlhtfsqsp klqnaasata lvsrtgrhse rvvgtskgta snwkktplst ggtlafvsps
      601 lavhksssav drqreylldm ipprsipqsa twk
//
LOCUS       NP_001101396             606 aa            linear   ROD 21-MAR-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001101396 XP_001057633 XP_001057690
VERSION     NP_001101396.1
DBSOURCE    REFSEQ: accession NM_001107926.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Loh,K.H., Stawski,P.S., Draycott,A.S., Udeshi,N.D., Lehrman,E.K.,
            Wilton,D.K., Svinkina,T., Deerinck,T.J., Ellisman,M.H., Stevens,B.,
            Carr,S.A. and Ting,A.Y.
  TITLE     Proteomic Analysis of Unbounded Cellular Compartments: Synaptic
            Clefts
  JOURNAL   Cell 166 (5), 1295-1307 (2016)
   PUBMED   27565350
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057633.1, XP_001057690.1.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21-q22"
     Protein         1..606
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2
                     precursor"
                     /note="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2"
                     /calculated_mol_wt=65220
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2949
     Region          27..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          39..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          48..>340
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          59..82
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          131..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          155..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          203..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          251..274
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          275..298
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          299..322
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          323..343
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          327..>391
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          411..500
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          428..432
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          441..445
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..485
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          493..496
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..606
                     /gene="Lingo2"
                     /gene_synonym="RGD1310773"
                     /coded_by="NM_001107926.2:335..2155"
                     /db_xref="GeneID:313156"
                     /db_xref="RGD:1310773"
ORIGIN      
        1 mlhtaipcwq pflglamvll fmgstigcpa rcecsaqnks vschrrrlia ipegipietk
       61 ildlsknrlk sinpeefisy plleeidlsd niianvepga fnnlfnlrsl rlkgnrlklv
      121 plgvftglsn ltkldisenk ivilldymfq dlhnlkslev gdndlvyish rafsglfsle
      181 qltlekcnlt avptealshl rslitlhlkh lninnmpvya fkrlfhlkql eidywplldm
      241 mpanslygln ltslsitntn lstvpflafk hlvylthlnl synpistiea gmfsdlirlq
      301 elhvvgaqlr tiephsfqgl rflrvlnvsq nlletleenv fsspralevl sinnnplacd
      361 crllwllqrq atlqfggqqp mcagpdtire rsfkdfhsta lsfyftckkp kirekklqhl
      421 lvdegqtvql ecnadgdpqp viswvtprrr fittksngra tvlgdgtlei rfaqdqdsgm
      481 yvciasnaag ndtftasltv kgftsdrfly anrtpmymtd sndtvsngtn antfsldlkt
      541 ilvstamgcf tflgvvlfcf lllfvwsrgk gkhknsidle yvprknngav aegevagprr
      601 fnmkmi
//
LOCUS       NP_001423711             630 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423711 XP_063131268
VERSION     NP_001423711.1
DBSOURCE    REFSEQ: accession NM_001436782.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131268.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3074312.1,
                                           SRR26360181.594807.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..630
                     /product="transcriptional repressor p66-alpha isoform 3"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67438
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          417..450
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..630
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436782.1:250..2142"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqqi hnirqhsstg ppplllapra svpsmqiqgq riiqqglirv anvpntsllv
      301 nipqptaasl kgttvgsaqa nstpssvasv vasaespasr qaaaklalrk qlektlleip
      361 ppkppapemn flpsaannef iylvgleevv qnlletqagr isatsaaavl srepymcvqc
      421 ktdftcrwre kggavmcenc mtsnqkkalk vehtsrlkaa fvkalqqeqe meqrllqqgv
      481 gtasikaeta aphpslkqvi kprrklafrs geardwnngs vlqtssqlsr gsattprgvl
      541 htfsqspklq naasatalvs rtgrhservv gtskgtasnw kktplstggt lafvspslav
      601 hksssavdrq reylldmipp rsipqsatwk
//
LOCUS       NP_001101399             973 aa            linear   ROD 21-MAR-2025
DEFINITION  E3 ubiquitin-protein ligase BRE1A [Rattus norvegicus].
ACCESSION   NP_001101399 XP_001053340 XP_001053415 XP_001053479 XP_001053543
            XP_001053616 XP_232995
VERSION     NP_001101399.2
DBSOURCE    REFSEQ: accession NM_001107929.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Lai,C.Y., Hsieh,M.C., Ho,Y.C., Wang,H.H., Chou,D., Wen,Y.C.,
            Yang,P.S., Cheng,J.K. and Peng,H.Y.
  TITLE     Spinal RNF20-Mediated Histone H2B Monoubiquitylation Regulates
            mGluR5 Transcription for Neuropathic Allodynia
  JOURNAL   J Neurosci 38 (43), 9160-9174 (2018)
   PUBMED   30201771
  REMARK    GeneRIF: RNF20-drive H2B monoubiquitination, which facilitates
            phosphorylated mGluR5 transcription in the dorsal horn in the
            development of neuropathic allodynia.
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Stracker,T.H., Roig,I., Knobel,P.A. and Marjanovic,M.
  TITLE     The ATM signaling network in development and disease
  JOURNAL   Front Genet 4, 37 (2013)
   PUBMED   23532176
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wang,E., Kawaoka,S., Yu,M., Shi,J., Ni,T., Yang,W., Zhu,J.,
            Roeder,R.G. and Vakoc,C.R.
  TITLE     Histone H2B ubiquitin ligase RNF20 is required for MLL-rearranged
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 110 (10), 3901-3906 (2013)
   PUBMED   23412334
REFERENCE   4  (residues 1 to 973)
  AUTHORS   Vethantham,V., Yang,Y., Bowman,C., Asp,P., Lee,J.H., Skalnik,D.G.
            and Dynlacht,B.D.
  TITLE     Dynamic loss of H2B ubiquitylation without corresponding changes in
            H3K4 trimethylation during myogenic differentiation
  JOURNAL   Mol Cell Biol 32 (6), 1044-1055 (2012)
   PUBMED   22252316
REFERENCE   5  (residues 1 to 973)
  AUTHORS   Liu,Z., Oh,S.M., Okada,M., Liu,X., Cheng,D., Peng,J., Brat,D.J.,
            Sun,S.Y., Zhou,W., Gu,W. and Ye,K.
  TITLE     Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor
  JOURNAL   Mol Biol Cell 20 (3), 757-768 (2009)
   PUBMED   19037095
REFERENCE   6  (residues 1 to 973)
  AUTHORS   Shema,E., Tirosh,I., Aylon,Y., Huang,J., Ye,C., Moskovits,N.,
            Raver-Shapira,N., Minsky,N., Pirngruber,J., Tarcic,G.,
            Hublarova,P., Moyal,L., Gana-Weisz,M., Shiloh,Y., Yarden,Y.,
            Johnsen,S.A., Vojtesek,B., Berger,S.L. and Oren,M.
  TITLE     The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a
            putative tumor suppressor through selective regulation of gene
            expression
  JOURNAL   Genes Dev 22 (19), 2664-2676 (2008)
   PUBMED   18832071
  REMARK    Erratum:[Genes Dev. 2017 Sep 15;31(18):1926. doi:
            10.1101/gad.307207.117. PMID: 29051390]
REFERENCE   7  (residues 1 to 973)
  AUTHORS   Tan,L.B., Chen,K.T., Tyan,Y.C., Liao,P.C. and Guo,H.R.
  TITLE     Proteomic analysis for human urinary proteins associated with
            arsenic intoxication
  JOURNAL   Proteomics Clin Appl 2 (7-8), 1087-1098 (2008)
   PUBMED   21136906
REFERENCE   8  (residues 1 to 973)
  AUTHORS   Pavri,R., Zhu,B., Li,G., Trojer,P., Mandal,S., Shilatifard,A. and
            Reinberg,D.
  TITLE     Histone H2B monoubiquitination functions cooperatively with FACT to
            regulate elongation by RNA polymerase II
  JOURNAL   Cell 125 (4), 703-717 (2006)
   PUBMED   16713563
REFERENCE   9  (residues 1 to 973)
  AUTHORS   Kim,J., Hake,S.B. and Roeder,R.G.
  TITLE     The human homolog of yeast BRE1 functions as a transcriptional
            coactivator through direct activator interactions
  JOURNAL   Mol Cell 20 (5), 759-770 (2005)
   PUBMED   16337599
REFERENCE   10 (residues 1 to 973)
  AUTHORS   Zhu,B., Zheng,Y., Pham,A.D., Mandal,S.S., Erdjument-Bromage,H.,
            Tempst,P. and Reinberg,D.
  TITLE     Monoubiquitination of human histone H2B: the factors involved and
            their roles in HOX gene regulation
  JOURNAL   Mol Cell 20 (4), 601-611 (2005)
   PUBMED   16307923
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 10, 2008 this sequence version replaced NP_001101399.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26643292.21664.1, SRR26643289.15248.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..973
                     /product="E3 ubiquitin-protein ligase BRE1A"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 20, E3 ubiquitin protein
                     ligase"
                     /calculated_mol_wt=113329
     Region          <320..934
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          900..973
                     /region_name="RING-HC_RNF20"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 20 (RNF20); cd16814"
                     /db_xref="CDD:438463"
     CDS             1..973
                     /gene="Rnf20"
                     /coded_by="NM_001107929.3:451..3372"
                     /db_xref="GeneID:313216"
                     /db_xref="RGD:1311936"
ORIGIN      
        1 msgignkraa gepgtsvppe kktavedsgt tvetiklggv ssteeldirt lqsknrklae
       61 mldqrqaied elrehiekle rrqatddasl livnrywsqf deniriilkr ydldqglgdl
      121 lterkalvvp epepdsdsnq erkddrerge gqepafsfla tlasssseem esqlqerves
      181 srravsqivt vydklqekvd llsrklnsgd nlimeeavqe lnsflaqenv rlqeltdllq
      241 ekhhtmsqef cklqgkveta esrvsvlesm iddlqwdidk irkreqrlnr hlaevlervn
      301 skgykvygag sslyggtiti narkfeemna eleenkelaq nrhceleklr qdfeevttqn
      361 eklkvelrsa veevvketpe yrcmqsqfsv lyneslqlka hldeartllh gtrgthqrqv
      421 elierdevsl hkklrteviq ledtlaqvrk eyemlriefe qtlaaneqag pinremrhli
      481 sslqnhnhql kgevlrykrk lreaqsdlnk trlrsgsall qsqsstedak deptelkqds
      541 edlathssal kasqedevks krdeeerere rrekererer erekekerer ekqklkesek
      601 erdpvkdkdk gkhddgrkke aeiikqlkte lkkaqesqke mkllldmyrs apkeqrdkvq
      661 lmaaekkska eledlrqrlk dledkekken kkmadedalr kiraveeqie ylqkklavak
      721 qeeeallsem dvtgqafedm qeqnirlmqq lrekddanfk lmseriksnq ihkllkeeke
      781 eladqvltlk tqvdaqlqvv rkleekehll qsnigtgeke lglrtqalem nkrkameaaq
      841 laddlkaqle laqkklhdfq deivensvtk ekdlfnfkra qedisrlrrk lettkkpdnv
      901 pkcdeilmee ikdykarltc pccnmrkkda vltkcfhvfc fecvktrydt rqrkcpkcna
      961 afgandfhri yig
//
LOCUS       NP_001423747             864 aa            linear   ROD 21-MAR-2025
DEFINITION  storkhead-box protein 2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423747
VERSION     NP_001423747.1
DBSOURCE    REFSEQ: accession NM_001436818.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Fenstad,M.H., Johnson,M.P., Loset,M., Mundal,S.B., Roten,L.T.,
            Eide,I.P., Bjorge,L., Sande,R.K., Johansson,A.K., Dyer,T.D.,
            Forsmo,S., Blangero,J., Moses,E.K. and Austgulen,R.
  TITLE     STOX2 but not STOX1 is differentially expressed in decidua from
            pre-eclamptic women: data from the Second Nord-Trondelag Health
            Study
  JOURNAL   Mol Hum Reprod 16 (12), 960-968 (2010)
   PUBMED   20643876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3091468.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..864
                     /product="storkhead-box protein 2 isoform 4"
                     /note="knockout CG10573-PA related; storkhead-box protein
                     2; spinelinin"
                     /calculated_mol_wt=95495
     Region          1..79
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     CDS             1..864
                     /gene="Stox2"
                     /coded_by="NM_001436818.1:544..3138"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:306459"
                     /db_xref="RGD:708477"
ORIGIN      
        1 mspisqsqfi plgeilclai samnsarkpv tqealmehlt tcfpgvptps qeilrhtlnt
       61 lvrerkiypt pdgyfivtpq tyfitpslir tnskwyhlde rvpdrsqcts pqpgtitpsa
      121 sgcvrertlp rkhcdschcc redmhsmhas tlqrkpakdc kdpycppplc qvpptdksks
      181 tinfsyktet lskpkdgekq skkfglklfr lsfkkdktkq lanfsaqfpp eewplrdedt
      241 pttiprevem eiirrinpdl tvenvmrhta lmkkleeeka hrskagssah hsgrskksrt
      301 hrkshgksrs hsktrvskgd psdgshldip gereyefcdp ltrapregcf iiehkgdnfi
      361 mhsntnvies hfpmtpewdv sgelakrrte mpfpepsrgs shskvhrshs htqdrrsrne
      421 rsnkakersr smdnskgplg asslgtpedl aegcsqddqt asqsyiddst lrpaqtighq
      481 rahipsasyk evcipeivgg skepssacsl lepgkspesm psygelspcp aktavddyfq
      541 cntssetvlt apsplgknke dhdtltlveg vkklspserq tphssrdpvg hkeespkgpg
      601 ggpaasggva eglangrlvq hhsaepsnld krkeifskdt lfkplhstls vnsyhkssls
      661 llkshpkspa dtlpgrcekm epslgtsaaq amppsqrqqe pggnqeasfd yynvsdddds
      721 eegankntee eknrddvgtm qwllereker dlqrkfeknl tllapketds ssnqrathsa
      781 rldsmdsssi tvdsgfnspr treslasnts sivesnrrqn palspahgga gptfnfrast
      841 dpptseaekl qkpsnclqas vtsv
//
LOCUS       NP_001423749             355 aa            linear   ROD 21-MAR-2025
DEFINITION  zinc finger MYND domain-containing protein 12 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423749 XP_017448881
VERSION     NP_001423749.1
DBSOURCE    REFSEQ: accession NM_001436820.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017448881.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29785.1,
                                           SRR26360190.2313279.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..355
                     /product="zinc finger MYND domain-containing protein 12
                     isoform b"
                     /note="zinc finger MYND domain-containing protein 12; zinc
                     finger, MYND domain containing 12"
                     /calculated_mol_wt=39991
     Region          17..54
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          77..>264
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          132..162
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(134..135,138..139,141,173,176..177,180..181,
                     183..184,215,218..219,222..223,226)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          171..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..242
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..355
                     /gene="Zmynd12"
                     /coded_by="NM_001436820.1:26..1093"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:313552"
                     /db_xref="RGD:1307175"
ORIGIN      
        1 mnviyplavp kgrrlccevc eapaermcta ctvtyycgpv hqkadwgsih akicqllipl
       61 rtsmpffnse eerqhglqql qrrqehlief cytvaqkylf egrhedavpa alhslrfrmn
      121 vhglssvelv paylllaeas lglgrivqae eylsqaqwtv lkstdcsnat hsllhrnlgl
      181 lyiakknlee aryhlandiy fascafgted vrtsggyfhl anifyslkkm eladtlytkv
      241 seiwytylss hyqallhart qqtdllgkqf mndtgldeaq eaeairilts iliiqestst
      301 qapqkgilil ktlgilyylm lefskvwacf asalgvsrhq hgpgwkegke tclgg
//
LOCUS       NP_001423736             542 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423736
VERSION     NP_001423736.1
DBSOURCE    REFSEQ: accession NM_001436807.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74882.1,
                                           SRR26360181.148505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..542
                     /product="cilia- and flagella-associated protein 97
                     isoform 1"
                     /calculated_mol_wt=60985
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          85..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          355..457
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     CDS             1..542
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436807.1:185..1813"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
       61 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      121 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      181 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      241 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      301 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      361 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      421 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      481 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppnvrta
      541 wl
//
LOCUS       NP_001423743             728 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001423743
VERSION     NP_001423743.1
DBSOURCE    REFSEQ: accession NM_001436814.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74840.1,
                                           SRR26360181.1778769.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..728
                     /product="cilia- and flagella-associated protein 97
                     isoform 6"
                     /calculated_mol_wt=81960
     Region          535..637
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..728
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436814.1:106..2292"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mwtrlvwtps eiclpllsey wnqritrlqh lcrkpsqmsk ptaaswlyeq vmpwtagrpw
       61 rspfheppsl lealprscrp ysaglitvtg slgtmddrsa artifgrdsv prsprlspsa
      121 eslprsfrpr srvresplas nawegemwcg cacaertrtr tlgaaresva atvprytfgi
      181 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
      241 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      301 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      361 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      421 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      481 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      541 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      601 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      661 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppniqcs
      721 nskvlrsh
//
LOCUS       NP_001423728             511 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423728 XP_038965885
VERSION     NP_001423728.1
DBSOURCE    REFSEQ: accession NM_001436799.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038965885.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.22223.1,
                                           SRR26643297.19507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..511
                     /product="mesoderm induction early response protein 1
                     isoform d"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=57726
     Region          181..230
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          287..331
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(287,317..318,320..321,323..325,327..329)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          341..>487
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..511
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436799.1:170..1705"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mlpsvesssp ggsaasedhe fdpsadmlvh dfddertlee eemmegetnf sseiedlare
       61 gdmpidells lygygstvql peeeeeeeee eeegeddeda dnddnsgcsg enkeenikds
      121 sgqedetqss nddpsqsvts qdaqeiirpr rckyfdtnse ieeeseeded yipsedwkke
      181 imvgsmfqae ipvgvcryke nekvyenddq llwdpeylpe dkvivflkda srrtgdekgv
      241 eaipegshik dneqalyelv kcsfdteeal rrlrfnvkaa reelsvwtee ecrnfeqglk
      301 aygkdfhliq ankvrtrsvg ecvafyymwk kserydffaq qtrfgkkkyn lhpgvtdymd
      361 rlldesesaa ssrapspppt asnsstsqse kedgtlsnsn qngvssngpg eilnkeevkv
      421 eglhvngptg gnkkplltdv dtngyeennl atdpklahmt arnendfdek nerpakrrri
      481 nssgkespgs seffqeavsh gkfeehentn d
//
LOCUS       NP_001423766             899 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001423766 XP_038965979
VERSION     NP_001423766.1
DBSOURCE    REFSEQ: accession NM_001436837.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 899)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 899)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 899)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 899)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038965979.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.20885.1,
                                           SRR26643297.20639.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..899
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 7"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=101506
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          399..>734
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <601..796
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..899
                     /gene="Srrm1"
                     /coded_by="NM_001436837.1:26..2725"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssederpkrs hvkngevgrr rrhspsrsas psprkrqket sprrrrrsps
      541 ppparrrrsp spappppppp pprrrrsptp pprrrtpspp prrrspsprr ysppiqrrys
      601 pspppkrrta spppppkrra spspppkrrv shspppkqrs ppvtkrrsps lsskhrkgss
      661 pgrstrears pqpnkrhsps prprapqtss pppvrrgasa spqgrqspsp strpirrvsr
      721 tpepkkikka aspspqsvrr vsssrsvsgs peptakkppa ppspvqsqsp stnwspaapa
      781 kkaksptpsp sparnsdqeg ggkkkkkkkd kkhkkdkkhk khkkhkkeka vavatpapaa
      841 paavsaaatp saqeepaaap eprketesea eddnlddler hlrekalrsm rkaqvspqs
//
LOCUS       NP_001101456             908 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001101456 XP_001069368 XP_233556
VERSION     NP_001101456.2
DBSOURCE    REFSEQ: accession NM_001107986.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 25, 2008 this sequence version replaced NP_001101456.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166715.1, SRR26643287.14617.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..908
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 4"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=102302
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <389..809
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          610..>806
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..908
                     /gene="Srrm1"
                     /coded_by="NM_001107986.3:26..2752"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssts ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rsrrrrspsp pparrrrsps papppppppp prrrrsptpp prrrtpsppp rrrspsprry
      601 sppiqrrysp spppkrrtas pppppkrras pspppkrrvs hspppkqrsp pvtkrrspsl
      661 sskhrkgssp grstrearsp qpnkrhspsp rprapqtssp ppvrrgasas pqgrqspsps
      721 trpirrvsrt pepkkikkaa spspqsvrrv sssrsvsgsp eptakkppap pspvqsqsps
      781 tnwspaapak kaksptpsps parnsdqegg gkkkkkkkdk khkkdkkhkk hkkhkkekav
      841 avatpapaap aavsaaatps aqeepaaape prketeseae ddnlddlerh lrekalrsmr
      901 kaqvspqs
//
LOCUS       NP_001423741             685 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001423741
VERSION     NP_001423741.1
DBSOURCE    REFSEQ: accession NM_001436812.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2088701.1,
                                           SRR26643293.74877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..685
                     /product="cilia- and flagella-associated protein 97
                     isoform 4"
                     /calculated_mol_wt=76767
     Region          498..600
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..685
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436812.1:209..2266"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mskptaaswl yeqvmpwtag rpwrspfhep psllealprs crpysaglit vtgslgtmdd
       61 rsaartifgr dsvprsprls psaeslprsf rprsrvresp lasnawegem wcgcacaert
      121 rtrtlgaare svaatvpryt fgimdrfgdi segevdhsff dsdfedtkkc esnsifdkqn
      181 dddfkegink diknlnlkfg vqndnlkeki dndtenvnvk lgiqtkenyl tqkgnerkpk
      241 fpskeqhven dpiqtrspsl ltssrskklc dttkgnklhl pvpnripkiv kgeddyytdg
      301 eessddgkky hvrsksakps snlkknntsk kyskassssl sssssrsssd csdigsdmqn
      361 kpdsgssgkr vssvtpsspk qkcksgrkss akqkagdyna esednvtdvt pastpdsspa
      421 qpfelsqsqn qkvkvkrqen vsrdvyedve alkndsrclk sakrkekhgq nfapkssvld
      481 anldrrskqk vlhdtmdlnh llkaflqldk kgpqkhhfeq psiiprknys ftreevrqid
      541 renqrllkel srqaekpgnk stipgrslgh ppklyhsaln rqreqqrier enmallkrle
      601 avkptvgmkr seqlmdyhrn isylnpspsv rrvrstlghy splrgasrts satsglsckt
      661 drsvldtssg fllrpkppnv rtawl
//
LOCUS       NP_001423730             428 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform f [Rattus
            norvegicus].
ACCESSION   NP_001423730 XP_063143768
VERSION     NP_001423730.1
DBSOURCE    REFSEQ: accession NM_001436801.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143768.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.22214.1,
                                           SRR26643294.21731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..428
                     /product="mesoderm induction early response protein 1
                     isoform f"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=48469
     Region          233..282
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          339..383
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(339,369..370,372..373,375..377,379..381)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          393..>412
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..428
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436801.1:29..1315"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mdgaspgggg ssggggsggg ygvvarfsqc laefrtwlrt nwlrfnadkt dvmlpsvess
       61 spggsaased hefdpsadml vhdfddertl eeeemmeget nfsseiedla regdmpidel
      121 lslygygstv qlpeeeeeee eeeeegedde dadnddnsgc sgenkeenik dssgqedetq
      181 ssnddpsqsv tsqdaqeiir prrckyfdtn seieeeseed edyipsedwk keimvgsmfq
      241 aeipvgvcry kenekvyend dqllwdpeyl pedkvivflk dasrrtgdek gveaipegsh
      301 ikdneqalye lvkcsfdtee alrrlrfnvk aareelsvwt eeecrnfeqg lkaygkdfhl
      361 iqankvrtrs vgecvafyym wkkserydff aqqtrfgkkk ynlhpgvtmk ricpccpqpl
      421 raplqgrd
//
LOCUS       NP_001423764             907 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423764 XP_006239247
VERSION     NP_001423764.1
DBSOURCE    REFSEQ: accession NM_001436835.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006239247.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16603.1,
                                           SRR26643298.29591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..907
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 5"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=102215
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <389..802
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <609..804
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..907
                     /gene="Srrm1"
                     /coded_by="NM_001436835.1:26..2749"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssts ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rrrrrspspp parrrrspsp appppppppp rrrrsptppp rrrtpspppr rrspsprrys
      601 ppiqrrysps pppkrrtasp ppppkrrasp spppkrrvsh spppkqrspp vtkrrspsls
      661 skhrkgsspg rstrearspq pnkrhspspr prapqtsspp pvrrgasasp qgrqspspst
      721 rpirrvsrtp epkkikkaas pspqsvrrvs ssrsvsgspe ptakkppapp spvqsqspst
      781 nwspaapakk aksptpspsp arnsdqeggg kkkkkkkdkk hkkdkkhkkh kkhkkekava
      841 vatpapaapa avsaaatpsa qeepaaapep rketeseaed dnlddlerhl rekalrsmrk
      901 aqvspqs
//
LOCUS       NP_001423770             824 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 11 [Rattus
            norvegicus].
ACCESSION   NP_001423770
VERSION     NP_001423770.1
DBSOURCE    REFSEQ: accession NM_001436841.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.163883.1,
                                           SRR26360186.1469989.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..824
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 11"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=92538
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <306..719
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <526..721
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..824
                     /gene="Srrm1"
                     /coded_by="NM_001436841.1:418..2892"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 lkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkekspel pepsvrmkds svqeatstsd ilkapkpepv pepkepspek
      181 nskkekektr prsrsrsksr srtrsrspsh trprrrhrsr srsysprrrp sprrrpsprr
      241 rtpprrmppp prhrrsrspg rrrrrssasl sgssssssss rsrsppkkpp krtsspprkt
      301 rrlspsaspp rrrhrpsspa tpppktrhsp tpqqsnrark srvsvspgrt sgkvtkhkgt
      361 ekrespspap kprkvelses eedkgskmaa adsvqqrrqy rrqnqqsssd sgssstsede
      421 rpkrshvkng evgrrrrhsp srsaspsprk rqketsprrr rrspspppar rrrspspapp
      481 ppppppprrr rsptppprrr tpsppprrrs psprrysppi qrryspsppp krrtaspppp
      541 pkrraspspp pkrrvshspp pkqrsppvtk rrspslsskh rkgsspgrst rearspqpnk
      601 rhspsprpra pqtsspppvr rgasaspqgr qspspstrpi rrvsrtpepk kikkaaspsp
      661 qsvrrvsssr svsgspepta kkppappspv qsqspstnws paapakkaks ptpspsparn
      721 sdqegggkkk kkkkdkkhkk dkkhkkhkkh kkekavavat papaapaavs aaatpsaqee
      781 paaapeprke teseaeddnl ddlerhlrek alrsmrkaqv spqs
//
LOCUS       NP_001423767             892 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 8 [Rattus
            norvegicus].
ACCESSION   NP_001423767 XP_017448895
VERSION     NP_001423767.1
DBSOURCE    REFSEQ: accession NM_001436838.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 892)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 892)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017448895.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.20886.1,
                                           SRR26643296.16389.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..892
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 8"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=100230
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <359..787
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..892
                     /gene="Srrm1"
                     /coded_by="NM_001436838.1:26..2704"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkeks pelpepsvrm kdssvqeats tsdilkapkp epvpepkeps peknskkeke
      241 ktrprsrsrs ksrsrtrsrs pshtrprrrh rsrsrsyspr rrpsprrrps prrrtpprrm
      301 pppprhrrsr spgrrrrrss aslsgsssss sssrsrsppk kppkrtsspp rktrrlspsa
      361 spprrrhrps spatpppktr hsptpqqsnr arksrvsvsp grtsgkvtkh kgtekresps
      421 papkprkvel seseedkgsk maaadsvqqr rqyrrqnqqs ssdsgsssts ederpkrshv
      481 kngevgrrrr hspsrsasps prkrqketsp rmqmgkrwqs pvtkssrrrr spsppparrr
      541 rspspapppp ppppprrrrs ptppprrrtp sppprrrsps prrysppiqr ryspspppkr
      601 rtaspppppk rraspspppk rrvshspppk qrsppvtkrr spslsskhrk gsspgrstre
      661 arspqpnkrh spsprprapq tsspppvrrg asaspqgrqs pspstrpirr vsrtpepkki
      721 kkaaspspqs vrrvsssrsv sgspeptakk ppappspvqs qspstnwspa apakkakspt
      781 pspsparnsd qegggkkkkk kkdkkhkkdk khkkhkkhkk ekavavatpa paapaavsaa
      841 atpsaqeepa aapeprkete seaeddnldd lerhlrekal rsmrkaqvsp qs
//
LOCUS       NP_001128335             926 aa            linear   ROD 21-MAR-2025
DEFINITION  storkhead-box protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001128335 NP_775130 XP_224852
VERSION     NP_001128335.1
DBSOURCE    REFSEQ: accession NM_001134863.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Fenstad,M.H., Johnson,M.P., Loset,M., Mundal,S.B., Roten,L.T.,
            Eide,I.P., Bjorge,L., Sande,R.K., Johansson,A.K., Dyer,T.D.,
            Forsmo,S., Blangero,J., Moses,E.K. and Austgulen,R.
  TITLE     STOX2 but not STOX1 is differentially expressed in decidua from
            pre-eclamptic women: data from the Second Nord-Trondelag Health
            Study
  JOURNAL   Mol Hum Reprod 16 (12), 960-968 (2010)
   PUBMED   20643876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Apr 15, 2014 this sequence version replaced
            NP_775130.2, XP_224852.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2312063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..926
                     /product="storkhead-box protein 2 isoform 2"
                     /note="knockout CG10573-PA related; storkhead-box protein
                     2; spinelinin"
                     /calculated_mol_wt=102617
     Region          63..141
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     CDS             1..926
                     /gene="Stox2"
                     /coded_by="NM_001134863.2:1359..4139"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306459"
                     /db_xref="RGD:708477"
ORIGIN      
        1 mkktrsttlr rawpssdfsd rasdrmrsrs ekdyrlhkrf paafapqasr gymtsgdvsp
       61 ismspisqsq fiplgeilcl aisamnsark pvtqealmeh lttcfpgvpt psqeilrhtl
      121 ntlvrerkiy ptpdgyfivt pqtyfitpsl irtnskwyhl dervpdrsqc tspqpgtitp
      181 sasgcvrert lprkhcdsch ccredmhsmh astlqrkpak dckdpycppp lcqvpptdks
      241 kstinfsykt etlskpkdge kqskkfglkl frlsfkkdkt kqlanfsaqf ppeewplrde
      301 dtpttiprev emeiirrinp dltvenvmrh talmkkleee kahrskagss ahhsgrskks
      361 rthrkshgks rshsktrvsk gdpsdgshld ipgereyefc dpltrapreg cfiiehkgdn
      421 fimhsntnvi eshfpmtpew dvsgelakrr tempfpepsr gsshskvhrs hshtqdrrsr
      481 nersnkaker srsmdnskgp lgasslgtpe dlaegcsqdd qtasqsyidd stlrpaqtig
      541 hqrahipsas ykevcipeiv ggskepssac sllepgkspe smpsygelsp cpaktavddy
      601 fqcntssetv ltapsplgkn kedhdtltlv egvkklspse rqtphssrdp vghkeespkg
      661 pgggpaasgg vaeglangrl vqhhsaepsn ldkrkeifsk dtlfkplhst lsvnsyhkss
      721 lsllkshpks padtlpgrce kmepslgtsa aqamppsqrq qepggnqeas fdyynvsddd
      781 dseeganknt eeeknrddvg tmqwllerek erdlqrkfek nltllapket dsssnqrath
      841 sarldsmdss sitvdsgfns prtreslasn tssivesnrr qnpalspahg gagptfnfra
      901 stdpptseae klqkpsnclq asvtsv
//
LOCUS       NP_001423746             894 aa            linear   ROD 21-MAR-2025
DEFINITION  storkhead-box protein 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423746 XP_038950448
VERSION     NP_001423746.1
DBSOURCE    REFSEQ: accession NM_001436817.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Fenstad,M.H., Johnson,M.P., Loset,M., Mundal,S.B., Roten,L.T.,
            Eide,I.P., Bjorge,L., Sande,R.K., Johansson,A.K., Dyer,T.D.,
            Forsmo,S., Blangero,J., Moses,E.K. and Austgulen,R.
  TITLE     STOX2 but not STOX1 is differentially expressed in decidua from
            pre-eclamptic women: data from the Second Nord-Trondelag Health
            Study
  JOURNAL   Mol Hum Reprod 16 (12), 960-968 (2010)
   PUBMED   20643876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038950448.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1395442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..894
                     /product="storkhead-box protein 2 isoform 3"
                     /note="knockout CG10573-PA related; storkhead-box protein
                     2; spinelinin"
                     /calculated_mol_wt=98869
     Region          31..109
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     CDS             1..894
                     /gene="Stox2"
                     /coded_by="NM_001436817.1:235..2919"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:306459"
                     /db_xref="RGD:708477"
ORIGIN      
        1 mrkelsmywk gnsqpshvlk stkgdvspis mspisqsqfi plgeilclai samnsarkpv
       61 tqealmehlt tcfpgvptps qeilrhtlnt lvrerkiypt pdgyfivtpq tyfitpslir
      121 tnskwyhlde rvpdrsqcts pqpgtitpsa sgcvrertlp rkhcdschcc redmhsmhas
      181 tlqrkpakdc kdpycppplc qvpptdksks tinfsyktet lskpkdgekq skkfglklfr
      241 lsfkkdktkq lanfsaqfpp eewplrdedt pttiprevem eiirrinpdl tvenvmrhta
      301 lmkkleeeka hrskagssah hsgrskksrt hrkshgksrs hsktrvskgd psdgshldip
      361 gereyefcdp ltrapregcf iiehkgdnfi mhsntnvies hfpmtpewdv sgelakrrte
      421 mpfpepsrgs shskvhrshs htqdrrsrne rsnkakersr smdnskgplg asslgtpedl
      481 aegcsqddqt asqsyiddst lrpaqtighq rahipsasyk evcipeivgg skepssacsl
      541 lepgkspesm psygelspcp aktavddyfq cntssetvlt apsplgknke dhdtltlveg
      601 vkklspserq tphssrdpvg hkeespkgpg ggpaasggva eglangrlvq hhsaepsnld
      661 krkeifskdt lfkplhstls vnsyhkssls llkshpkspa dtlpgrcekm epslgtsaaq
      721 amppsqrqqe pggnqeasfd yynvsdddds eegankntee eknrddvgtm qwllereker
      781 dlqrkfeknl tllapketds ssnqrathsa rldsmdsssi tvdsgfnspr treslasnts
      841 sivesnrrqn palspahgga gptfnfrast dpptseaekl qkpsnclqas vtsv
//
LOCUS       NP_001423724             259 aa            linear   ROD 21-MAR-2025
DEFINITION  DNA-binding protein RFXANK isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423724 XP_063131447
VERSION     NP_001423724.1
DBSOURCE    REFSEQ: accession NM_001436795.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   McKinsey,T.A., Kuwahara,K., Bezprozvannaya,S. and Olson,E.N.
  TITLE     Class II histone deacetylases confer signal responsiveness to the
            ankyrin-repeat proteins ANKRA2 and RFXANK
  JOURNAL   Mol Biol Cell 17 (1), 438-447 (2006)
   PUBMED   16236793
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Louise-Plence,P.,
            Prochnicka-Chalufour,A., Selz,F., Picard,C., Le Deist,F.,
            Eliaou,J.F., Fischer,A. and Lisowska-Grospierre,B.
  TITLE     Novel mutations in the RFXANK gene: RFX complex containing
            in-vitro-generated RFXANK mutant binds the promoter without
            transactivating MHC II
  JOURNAL   Immunogenetics 54 (11), 747-755 (2003)
   PUBMED   12618906
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131447.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1261487.1,
                                           SRR26360186.526449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..259
                     /product="DNA-binding protein RFXANK isoform 1"
                     /note="DNA-binding protein RFXANK"
                     /calculated_mol_wt=28101
     Region          <93..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          93..120
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(122,124,128..129,132..134,136..137,141,144,153,155,
                     157,161..162,165..167,169..170,174,177,186,188,190,
                     194..195,198..200,202..203,207,210)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          122..153
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          155..186
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          188..216
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..259
                     /gene="Rfxank"
                     /coded_by="NM_001436795.1:432..1211"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:306353"
                     /db_xref="RGD:1311390"
ORIGIN      
        1 meptqvaenl ipnqqslapd ledpedrrde spdssdtvvl slfpctpdav npeadasass
       61 lqgsflkhst tltnrqrgne vsalpatlds lsihqlaaqg elsqlkdhlr kgdnlvnkpd
      121 ergftpliwa safgeietvr flldwgadph ilakeresal slasmggytd ivrllldrdv
      181 diniydwngg tpllyavrgn hvkcvealla rgadlttead sgytpmdlav algyrkvqqv
      241 meshilklfq gtlgpadpe
//
LOCUS       NP_001423726             529 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423726
VERSION     NP_001423726.1
DBSOURCE    REFSEQ: accession NM_001436797.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.28084.1,
                                           SRR26643289.15646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..529
                     /product="mesoderm induction early response protein 1
                     isoform b"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=60084
     Region          199..248
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          305..349
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(305,335..336,338..339,341..343,345..347)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          359..>505
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..529
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436797.1:208..1797"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mfmfnwftdc lwilflsnyk psvessspgg saasedhefd psadmlvhdf ddertleeee
       61 mmegetnfss eiedlaregd mpidellsly gygstvqlpe eeeeeeeeee egeddedadn
      121 ddnsgcsgen keenikdssg qedetqssnd dpsqsvtsqd aqeiirprrc kyfdtnseie
      181 eeseededyi psedwkkeim vgsmfqaeip vgvcrykene kvyenddqll wdpeylpedk
      241 vivflkdasr rtgdekgvea ipegshikdn eqalyelvkc sfdteealrr lrfnvkaare
      301 elsvwteeec rnfeqglkay gkdfhliqan kvrtrsvgec vafyymwkks erydffaqqt
      361 rfgkkkynlh pgvtdymdrl ldesesaass rapsppptas nsstsqseke dgtlsnsnqn
      421 gvssngpgei lnkeevkveg lhvngptggn kkplltdvdt ngyeennlat dpklahmtar
      481 nendfdekne rpakrrrins sgkespgsse ffqeavshgk feehentnd
//
LOCUS       NP_001423735             542 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423735
VERSION     NP_001423735.1
DBSOURCE    REFSEQ: accession NM_001436806.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.271386.1,
                                           SRR26643293.74850.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..542
                     /product="cilia- and flagella-associated protein 97
                     isoform 1"
                     /calculated_mol_wt=60985
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          85..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          355..457
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     CDS             1..542
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436806.1:164..1792"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
       61 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      121 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      181 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      241 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      301 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      361 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      421 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      481 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppnvrta
      541 wl
//
LOCUS       NP_001423701             331 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423701 XP_008762001
VERSION     NP_001423701.1
DBSOURCE    REFSEQ: accession NM_001436772.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_008762001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093606.1, SRR26643293.28361.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..331
                     /product="PC4 and SFRS1-interacting protein isoform 5"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=37235
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Region          <85..284
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..331
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436772.1:283..1278"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekkrkggr nfqaahrrnm
      301 lkgqhekeaa drkrkqeeqm etehqttcnl q
//
LOCUS       NP_001101435             369 aa            linear   ROD 21-MAR-2025
DEFINITION  beta-1,4-galactosyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_001101435 XP_001072098 XP_242992
VERSION     NP_001101435.1
DBSOURCE    REFSEQ: accession NM_001107965.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Yoshihara,T., Sugihara,K., Kizuka,Y., Oka,S. and Asano,M.
  TITLE     Learning/memory impairment and reduced expression of the HNK-1
            carbohydrate in beta4-galactosyltransferase-II-deficient mice
  JOURNAL   J Biol Chem 284 (18), 12550-12561 (2009)
   PUBMED   19265195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_242992.2, XP_001072098.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360172.16374.1, SRR26360194.270561.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..369
                     /product="beta-1,4-galactosyltransferase 2"
                     /EC_number="2.4.1.38"
                     /note="UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,
                     polypeptide 2"
                     /calculated_mol_wt=41838
     Region          142..358
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(147,149,151,186,213..215)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(213,215,308)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..369
                     /gene="B4galt2"
                     /coded_by="NM_001107965.2:191..1300"
                     /db_xref="GeneID:313536"
                     /db_xref="RGD:1305358"
ORIGIN      
        1 msrllggtle rvckavlllc llhflvavil yfdvyaqhla ffsrfstrsp ahalypaass
       61 stncsrpntt aassglpevp sarpgptapv ippcpdvppg lvgrvvieft spmplervqr
      121 enpgvllggr ysppdctpaq tvaviipfrh rehhlrywlh ylhpmlrrqr lrygvyvinq
      181 hgeetfnrak llnvgfleal kedatydcfi fsdvdlvpmd drnlyrcgdq prhfaiamdk
      241 fgfrlpyasy fggvsglska qflringfpn eywgwggedd difnrisltg mkisrpdvri
      301 gryrmikhdr dkhnepnpqr fnkiqntkms mkwdgigsvr yrvlevsrqp lftnitvdig
      361 qpmswltqg
//
LOCUS       NP_001423750             324 aa            linear   ROD 21-MAR-2025
DEFINITION  zinc finger MYND domain-containing protein 12 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423750 XP_063143811
VERSION     NP_001423750.1
DBSOURCE    REFSEQ: accession NM_001436821.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29786.1,
                                           SRR26360181.3044217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..324
                     /product="zinc finger MYND domain-containing protein 12
                     isoform c"
                     /note="zinc finger MYND domain-containing protein 12; zinc
                     finger, MYND domain containing 12"
                     /calculated_mol_wt=36577
     Region          17..54
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          77..>195
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(89,92..93,96..97,99,131,134..135,138..139,141..142,
                     173,176..177,180..181,184)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          121..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <123..297
                     /region_name="TPR_MalT"
                     /note="MalT-like TPR region; pfam17874"
                     /db_xref="CDD:436107"
     Region          172..195
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..324
                     /gene="Zmynd12"
                     /coded_by="NM_001436821.1:26..1000"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:313552"
                     /db_xref="RGD:1307175"
ORIGIN      
        1 mnviyplavp kgrrlccevc eapaermcta ctvtyycgpv hqkadwgsih akicqllipl
       61 rtsmpffnse eerqhglqql qrrqehlief cytvaqkylf egrhedavpa alhslrfrmn
      121 vhglssvelv paylllaeas lglgrivqae eylsqaqwtv lkstdcsnat hsllhrnlgl
      181 lyiakknlee aryhlandvs eiwytylssh yqallhartq qtdllgkqfm ndtgldeaqe
      241 aeairiltsi liiqeststq apqkgililk tlgilyylml efskakeyat kalslaevyl
      301 seeeqgviqe llsailaeek qltt
//
LOCUS       NP_001101440             298 aa            linear   ROD 21-MAR-2025
DEFINITION  zinc finger MYND domain-containing protein 12 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001101440 XP_001073920 XP_233458
VERSION     NP_001101440.1
DBSOURCE    REFSEQ: accession NM_001107970.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001073920.1, XP_233458.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..298
                     /product="zinc finger MYND domain-containing protein 12
                     isoform 4"
                     /note="zinc finger MYND domain-containing protein 12; zinc
                     finger, MYND domain containing 12"
                     /calculated_mol_wt=32872
     Region          8..>221
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          89..119
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91..92,95..96,98,130,133..134,137..138,140..141,172,
                     175..176,179..180,183)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          128..158
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          171..199
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..298
                     /gene="Zmynd12"
                     /coded_by="NM_001107970.2:184..1080"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:313552"
                     /db_xref="RGD:1307175"
ORIGIN      
        1 mpaadpsahq hallqlrgge aawsaaaaea agkvhisvfp qehliefcyt vaqkylfegr
       61 hedavpaalh slrfrmnvhg lssvelvpay lllaeaslgl grivqaeeyl sqaqwtvlks
      121 tdcsnathsl lhrnlgllyi akknleeary hlandiyfas cafgtedvrt sggyfhlani
      181 fyslkkmela dtlytkvsei wytylsshyq allhartqqt dllgkqfmnd tgldeaqeae
      241 airiltsili iqeststqap qkgililktl gilyylmlef sklltgplac shpslgta
//
LOCUS       NP_001423731             377 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform g [Rattus
            norvegicus].
ACCESSION   NP_001423731 XP_063143773
VERSION     NP_001423731.1
DBSOURCE    REFSEQ: accession NM_001436802.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143773.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.22225.1,
                                           SRR26643294.21734.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..377
                     /product="mesoderm induction early response protein 1
                     isoform g"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=43262
     Region          182..231
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          288..332
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(288,318..319,321..322,324..326,328..330)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          342..>361
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..377
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436802.1:114..1247"
                     /note="isoform g is encoded by transcript variant 8"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 maepsvesss pggsaasedh efdpsadmlv hdfddertle eeemmegetn fsseiedlar
       61 egdmpidell slygygstvq lpeeeeeeee eeeegedded adnddnsgcs genkeenikd
      121 ssgqedetqs snddpsqsvt sqdaqeiirp rrckyfdtns eieeeseede dyipsedwkk
      181 eimvgsmfqa eipvgvcryk enekvyendd qllwdpeylp edkvivflkd asrrtgdekg
      241 veaipegshi kdneqalyel vkcsfdteea lrrlrfnvka areelsvwte eecrnfeqgl
      301 kaygkdfhli qankvrtrsv gecvafyymw kkserydffa qqtrfgkkky nlhpgvtmkr
      361 icpccpqplr aplqgrd
//
LOCUS       NP_001101450             262 aa            linear   ROD 21-MAR-2025
DEFINITION  R-spondin-1 precursor [Rattus norvegicus].
ACCESSION   NP_001101450 XP_001056937 XP_233520
VERSION     NP_001101450.1
DBSOURCE    REFSEQ: accession NM_001107980.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Li,J.Y., Wu,X., Lee,A., Zhou,S.Y. and Owyang,C.
  TITLE     Altered R-spondin 1/CART neurocircuit in the hypothalamus
            contributes to hyperphagia in diabetes
  JOURNAL   J Neurophysiol 121 (3), 928-939 (2019)
   PUBMED   30649980
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Szenker-Ravi,E., Altunoglu,U., Leushacke,M., Bosso-Lefevre,C.,
            Khatoo,M., Thi Tran,H., Naert,T., Noelanders,R., Hajamohideen,A.,
            Beneteau,C., de Sousa,S.B., Karaman,B., Latypova,X., Basaran,S.,
            Yucel,E.B., Tan,T.T., Vlaminck,L., Nayak,S.S., Shukla,A.,
            Girisha,K.M., Le Caignec,C., Soshnikova,N., Uyguner,Z.O.,
            Vleminckx,K., Barker,N., Kayserili,H. and Reversade,B.
  TITLE     RSPO2 inhibition of RNF43 and ZNRF3 governs limb development
            independently of LGR4/5/6
  JOURNAL   Nature 557 (7706), 564-569 (2018)
   PUBMED   29769720
  REMARK    Erratum:[Nature. 2018 Sep;561(7722):E7. doi:
            10.1038/s41586-018-0296-7. PMID: 29977062]
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Li,J.Y., Chai,B., Zhang,W., Fritze,D.M., Zhang,C. and
            Mulholland,M.W.
  TITLE     LGR4 and its ligands, R-spondin 1 and R-spondin 3, regulate food
            intake in the hypothalamus of male rats
  JOURNAL   Endocrinology 155 (2), 429-440 (2014)
   PUBMED   24280058
  REMARK    GeneRIF: These data indicate that Rspo1 and Rspo3 and their
            receptor LGR4 form novel circuits in the brain to regulate energy
            homeostasis.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Niehrs,C.
  TITLE     The complex world of WNT receptor signalling
  JOURNAL   Nat Rev Mol Cell Biol 13 (12), 767-779 (2012)
   PUBMED   23151663
  REMARK    Review article
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Ruffner,H., Sprunger,J., Charlat,O., Leighton-Davies,J.,
            Grosshans,B., Salathe,A., Zietzling,S., Beck,V., Therier,M.,
            Isken,A., Xie,Y., Zhang,Y., Hao,H., Shi,X., Liu,D., Song,Q.,
            Clay,I., Hintzen,G., Tchorz,J., Bouchez,L.C., Michaud,G., Finan,P.,
            Myer,V.E., Bouwmeester,T., Porter,J., Hild,M., Bassilana,F.,
            Parker,C.N. and Cong,F.
  TITLE     R-Spondin potentiates Wnt/beta-catenin signaling through orphan
            receptors LGR4 and LGR5
  JOURNAL   PLoS One 7 (7), e40976 (2012)
   PUBMED   22815884
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Carmon,K.S., Gong,X., Lin,Q., Thomas,A. and Liu,Q.
  TITLE     R-spondins function as ligands of the orphan receptors LGR4 and
            LGR5 to regulate Wnt/beta-catenin signaling
  JOURNAL   Proc Natl Acad Sci U S A 108 (28), 11452-11457 (2011)
   PUBMED   21693646
REFERENCE   7  (residues 1 to 262)
  AUTHORS   de Lau,W., Barker,N., Low,T.Y., Koo,B.K., Li,V.S., Teunissen,H.,
            Kujala,P., Haegebarth,A., Peters,P.J., van de Wetering,M.,
            Stange,D.E., van Es,J.E., Guardavaccaro,D., Schasfoort,R.B.,
            Mohri,Y., Nishimori,K., Mohammed,S., Heck,A.J. and Clevers,H.
  TITLE     Lgr5 homologues associate with Wnt receptors and mediate R-spondin
            signalling
  JOURNAL   Nature 476 (7360), 293-297 (2011)
   PUBMED   21727895
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Binnerts,M.E., Kim,K.A., Bright,J.M., Patel,S.M., Tran,K., Zhou,M.,
            Leung,J.M., Liu,Y., Lomas,W.E. 3rd, Dixon,M., Hazell,S.A.,
            Wagle,M., Nie,W.S., Tomasevic,N., Williams,J., Zhan,X., Levy,M.D.,
            Funk,W.D. and Abo,A.
  TITLE     R-Spondin1 regulates Wnt signaling by inhibiting internalization of
            LRP6
  JOURNAL   Proc Natl Acad Sci U S A 104 (37), 14700-14705 (2007)
   PUBMED   17804805
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Nam,J.S., Turcotte,T.J., Smith,P.F., Choi,S. and Yoon,J.K.
  TITLE     Mouse cristin/R-spondin family proteins are novel ligands for the
            Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent
            gene expression
  JOURNAL   J Biol Chem 281 (19), 13247-13257 (2006)
   PUBMED   16543246
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Kamata,T., Katsube,K., Michikawa,M., Yamada,M., Takada,S. and
            Mizusawa,H.
  TITLE     R-spondin, a novel gene with thrombospondin type 1 domain, was
            expressed in the dorsal neural tube and affected in Wnts mutants
  JOURNAL   Biochim Biophys Acta 1676 (1), 51-62 (2004)
   PUBMED   14732490
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_233520.4, XP_001056937.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: EV779428.1, SRR21887622.4007006.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..262
                     /product="R-spondin-1 precursor"
                     /calculated_mol_wt=26749
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2139
     Region          42..142
                     /region_name="Furin-like_2"
                     /note="Furin-like repeat, cysteine-rich; pfam15913"
                     /db_xref="CDD:464939"
     Region          148..203
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     CDS             1..262
                     /gene="Rspo1"
                     /gene_synonym="RGD1565558"
                     /coded_by="NM_001107980.2:303..1091"
                     /db_xref="GeneID:313589"
                     /db_xref="RGD:1565558"
ORIGIN      
        1 mrlglcvval vlswthlavg srgikgkrqr risaegsqsc akgcelcsev ngclkcspkl
       61 fillerndir qvgvclpscp pgyfdarnpd mnkcikckie hceacfshnf ctkcqeglyl
      121 hkgrcypacp egstaanstm ecgspaqcem sewspwgpcs kkrklcgfrk gseertrrvl
      181 hapggdqtnc sdtketrkct vrrtpcpegq krkkasqgrr enanrhptrk nskepgsnsr
      241 rhkgqqqpqp gtagpltsvg pt
//
LOCUS       NP_001423762             921 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423762 XP_006239245
VERSION     NP_001423762.1
DBSOURCE    REFSEQ: accession NM_001436833.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006239245.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.14616.1,
                                           SRR26643298.29590.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..921
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 2"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=103861
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          378..>725
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <623..818
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..921
                     /gene="Srrm1"
                     /coded_by="NM_001436833.1:26..2791"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssts ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rmqmgkrwqs pvtksrrrrs psppparrrr spspappppp pppprrrrsp tppprrrtps
      601 ppprrrspsp rrysppiqrr yspspppkrr taspppppkr raspspppkr rvshspppkq
      661 rsppvtkrrs pslsskhrkg sspgrstrea rspqpnkrhs psprprapqt sspppvrrga
      721 saspqgrqsp spstrpirrv srtpepkkik kaaspspqsv rrvsssrsvs gspeptakkp
      781 pappspvqsq spstnwspaa pakkaksptp spsparnsdq egggkkkkkk kdkkhkkdkk
      841 hkkhkkhkke kavavatpap aapaavsaaa tpsaqeepaa apeprketes eaeddnlddl
      901 erhlrekalr smrkaqvspq s
//
LOCUS       NP_001423716             607 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423716 XP_063131273
VERSION     NP_001423716.1
DBSOURCE    REFSEQ: accession NM_001436787.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131273.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..607
                     /product="transcriptional repressor p66-alpha isoform 5"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=64744
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          419..452
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..607
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436787.1:410..2233"
                     /note="isoform 5 is encoded by transcript variant 14"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqvs qihnirqhss tgppplllap rasvpsmqiq gqriiqqgli rvanvpntsl
      301 lvnipqptaa slkgttvgsa qanstpssva svvasaespa srqaaaklal rkqlektlle
      361 ipppkppape mnflpsaann efiylvglee vvqnlletqa grisatsaaa vlsrepymcv
      421 qcktdftcrw rekggavmce ncmtsnqkka lkvehtsrlk aafvkalqqe qemeqrllqq
      481 gvgtasikae taaphpslkq tssqlsrgsa ttprgvlhtf sqspklqnaa satalvsrtg
      541 rhservvgts kgtasnwkkt plstggtlaf vspslavhks ssavdrqrey lldmipprsi
      601 pqsatwk
//
LOCUS       NP_001423751             203 aa            linear   ROD 21-MAR-2025
DEFINITION  zinc finger MYND domain-containing protein 12 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001423751
VERSION     NP_001423751.1
DBSOURCE    REFSEQ: accession NM_001436822.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.388059.1,
                                           SRR22399484.1657513.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..203
                     /product="zinc finger MYND domain-containing protein 12
                     isoform 5"
                     /note="zinc finger MYND domain-containing protein 12; zinc
                     finger, MYND domain containing 12"
                     /calculated_mol_wt=22964
     Region          17..54
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          77..>195
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          88..116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(89,92..93,96..97,99,131,134..135,138..139,141..142,
                     173,176..177,180..181,184)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          121..163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          172..195
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..203
                     /gene="Zmynd12"
                     /coded_by="NM_001436822.1:26..637"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:313552"
                     /db_xref="RGD:1307175"
ORIGIN      
        1 mnviyplavp kgrrlccevc eapaermcta ctvtyycgpv hqkadwgsih akicqllipl
       61 rtsmpffnse eerqhglqql qrrqehlief cytvaqkylf egrhedavpa alhslrfrmn
      121 vhglssvelv paylllaeas lglgrivqae eylsqaqwtv lkstdcsnat hsllhrnlgl
      181 lyiakknlee aryhlandvs erp
//
LOCUS       NP_001423729             485 aa            linear   ROD 21-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform e [Rattus
            norvegicus].
ACCESSION   NP_001423729
VERSION     NP_001423729.1
DBSOURCE    REFSEQ: accession NM_001436800.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.23488.1,
                                           SRR26643287.13617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..485
                     /product="mesoderm induction early response protein 1
                     isoform e"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=55138
     Region          155..204
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          261..305
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(261,291..292,294..295,297..299,301..303)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          315..>461
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..485
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436800.1:298..1755"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mlvhdfdder tleeeemmeg etnfsseied laregdmpid ellslygygs tvqlpeeeee
       61 eeeeeeeged dedadnddns gcsgenkeen ikdssgqede tqssnddpsq svtsqdaqei
      121 irprrckyfd tnseieeese ededyipsed wkkeimvgsm fqaeipvgvc rykenekvye
      181 nddqllwdpe ylpedkvivf lkdasrrtgd ekgveaipeg shikdneqal yelvkcsfdt
      241 eealrrlrfn vkaareelsv wteeecrnfe qglkaygkdf hliqankvrt rsvgecvafy
      301 ymwkkseryd ffaqqtrfgk kkynlhpgvt dymdrlldes esaassraps ppptasnsst
      361 sqsekedgtl snsnqngvss ngpgeilnke evkveglhvn gptggnkkpl ltdvdtngye
      421 ennlatdpkl ahmtarnend fdeknerpak rrrinssgke spgsseffqe avshgkfeeh
      481 entnd
//
LOCUS       NP_001423699             349 aa            linear   ROD 21-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423699 XP_017448854
VERSION     NP_001423699.1
DBSOURCE    REFSEQ: accession NM_001436770.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017448854.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.28362.1,
                                           SRR26643290.19595.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..349
                     /product="PC4 and SFRS1-interacting protein isoform 3"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=39340
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Region          <90..>332
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..349
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_001436770.1:283..1332"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekkrkggr nfqaahrrnm
      301 lkgqhekeaa drkrkqeeqm etehinpvte krirvehtsd edletdsld
//
LOCUS       NP_001423715             629 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423715 XP_063131271
VERSION     NP_001423715.1
DBSOURCE    REFSEQ: accession NM_001436786.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131271.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2189179.1,
                                           SRR26643293.74325.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..629
                     /product="transcriptional repressor p66-alpha isoform 4"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67310
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          416..449
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..629
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436786.1:250..2139"
                     /note="isoform 4 is encoded by transcript variant 13"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqih nirqhsstgp pplllapras vpsmqiqgqr iiqqglirva nvpntsllvn
      301 ipqptaaslk gttvgsaqan stpssvasvv asaespasrq aaaklalrkq lektlleipp
      361 pkppapemnf lpsaannefi ylvgleevvq nlletqagri satsaaavls repymcvqck
      421 tdftcrwrek ggavmcencm tsnqkkalkv ehtsrlkaaf vkalqqeqem eqrllqqgvg
      481 tasikaetaa phpslkqvik prrklafrsg eardwnngsv lqtssqlsrg sattprgvlh
      541 tfsqspklqn aasatalvsr tgrhservvg tskgtasnwk ktplstggtl afvspslavh
      601 ksssavdrqr eylldmippr sipqsatwk
//
LOCUS       NP_001423740             571 aa            linear   ROD 21-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423740
VERSION     NP_001423740.1
DBSOURCE    REFSEQ: accession NM_001436811.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.74846.1,
                                           SRR26360181.3385779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..571
                     /product="cilia- and flagella-associated protein 97
                     isoform 3"
                     /calculated_mol_wt=64571
     Region          384..486
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..571
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436811.1:106..1821"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mwtrlvwtps eiclpllsey wnqrytfgim drfgdisege vdhsffdsdf edtkkcesns
       61 ifdkqndddf keginkdikn lnlkfgvqnd nlkekidndt envnvklgiq tkenyltqkg
      121 nerkpkfpsk eqhvendpiq trspslltss rskklcdttk gnklhlpvpn ripkivkged
      181 dyytdgeess ddgkkyhvrs ksakpssnlk knntskkysk asssslssss srsssdcsdi
      241 gsdmqnkpds gssgkrvssv tpsspkqkck sgrkssakqk agdynaesed nvtdvtpast
      301 pdsspaqpfe lsqsqnqkvk vkrqenvsrd vyedvealkn dsrclksakr kekhgqnfap
      361 kssvldanld rrskqkvlhd tmdlnhllka flqldkkgpq khhfeqpsii prknysftre
      421 evrqidrenq rllkelsrqa ekpgnkstip grslghppkl yhsalnrqre qqrierenma
      481 llkrleavkp tvgmkrseql mdyhrnisyl npspsvrrvr stlghysplr gasrtssats
      541 glscktdrsv ldtssgfllr pkppnvrtaw l
//
LOCUS       NP_001423763             913 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423763 XP_063143836
VERSION     NP_001423763.1
DBSOURCE    REFSEQ: accession NM_001436834.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143836.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20647.1,
                                           SRR26360194.2074544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..913
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 3"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=103152
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          378..>717
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          615..>878
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..913
                     /gene="Srrm1"
                     /coded_by="NM_001436834.1:26..2767"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssederpkrs hvkngevgrr rrhspsrsas psprkrqket sprmqmgkrw
      541 qspvtksrrr rspsppparr rrspspappp pppppprrrr sptppprrrt psppprrrsp
      601 sprrysppiq rryspspppk rrtasppppp krraspsppp krrvshsppp kqrsppvtkr
      661 rspslsskhr kgsspgrstr earspqpnkr hspsprprap qtsspppvrr gasaspqgrq
      721 spspstrpir rvsrtpepkk ikkaaspspq svrrvsssrs vsgspeptak kppappspvq
      781 sqspstnwsp aapakkaksp tpspsparns dqegggkkkk kkkdkkhkkd kkhkkhkkhk
      841 kekavavatp apaapaavsa aatpsaqeep aaapeprket eseaeddnld dlerhlreka
      901 lrsmrkaqvs pqs
//
LOCUS       NP_001423714             629 aa            linear   ROD 21-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423714 XP_063131270
VERSION     NP_001423714.1
DBSOURCE    REFSEQ: accession NM_001436785.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131270.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.154926.1,
                                           SRR26360181.2537162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..629
                     /product="transcriptional repressor p66-alpha isoform 4"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67310
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          416..449
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..629
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436785.1:410..2299"
                     /note="isoform 4 is encoded by transcript variant 12"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqih nirqhsstgp pplllapras vpsmqiqgqr iiqqglirva nvpntsllvn
      301 ipqptaaslk gttvgsaqan stpssvasvv asaespasrq aaaklalrkq lektlleipp
      361 pkppapemnf lpsaannefi ylvgleevvq nlletqagri satsaaavls repymcvqck
      421 tdftcrwrek ggavmcencm tsnqkkalkv ehtsrlkaaf vkalqqeqem eqrllqqgvg
      481 tasikaetaa phpslkqvik prrklafrsg eardwnngsv lqtssqlsrg sattprgvlh
      541 tfsqspklqn aasatalvsr tgrhservvg tskgtasnwk ktplstggtl afvspslavh
      601 ksssavdrqr eylldmippr sipqsatwk
//
LOCUS       NP_001101436             971 aa            linear   ROD 21-MAR-2025
DEFINITION  lysine-specific demethylase 4A isoform b [Rattus norvegicus].
ACCESSION   NP_001101436 XP_001072204 XP_233441
VERSION     NP_001101436.1
DBSOURCE    REFSEQ: accession NM_001107966.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Li,L., Ding,Z., Ma,F., Zhang,K., Lu,D., Wang,H. and Yang,K.
  TITLE     Spinal nerve transection-induced upregulation of KDM4A in the
            dorsal root ganglia contributes to the development and maintenance
            of neuropathic pain via promoting CCL2 expression in rats
  JOURNAL   Eur J Neurosci 60 (6), 5169-5188 (2024)
   PUBMED   39136140
  REMARK    GeneRIF: Spinal nerve transection-induced upregulation of KDM4A in
            the dorsal root ganglia contributes to the development and
            maintenance of neuropathic pain via promoting CCL2 expression in
            rats.
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Li,W., Zhang,Y., Lv,J., Zhang,Y., Bai,J., Zhen,L. and He,X.
  TITLE     MicroRNA-137-mediated lysine demethylase 4A regulates the recovery
            of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis
  JOURNAL   Int J Neurosci 133 (1), 37-50 (2023)
   PUBMED   33499717
  REMARK    GeneRIF: MicroRNA-137-mediated lysine demethylase 4A regulates the
            recovery of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis.
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Liu,Y., Zhao,L., Zhang,J., Lv,L., Han,K., Huang,C. and Xu,Z.
  TITLE     Histone Demethylase KDM4A Inhibition Represses Neuroinflammation
            and Improves Functional Recovery in Ischemic Stroke
  JOURNAL   Curr Pharm Des 27 (21), 2528-2536 (2021)
   PUBMED   33402077
  REMARK    GeneRIF: Histone Demethylase KDM4A Inhibition Represses
            Neuroinflammation and Improves Functional Recovery in Ischemic
            Stroke.
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Qin,G., Li,Y., Wang,H., Yang,J., Chen,Q., Tang,H., Wang,Y.,
            Zhang,M., Jiang,T., Lin,S. and Huo,S.
  TITLE     Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation
            via Regulating the Binding Ability of H3K9me3 with the Promoters of
            Runx2, Osterix and Osteocalcin
  JOURNAL   J Biomed Nanotechnol 16 (6), 899-909 (2020)
   PUBMED   33187585
  REMARK    GeneRIF: Lysine-Specific Demethylase 4A Regulates Osteogenic
            Differentiation via Regulating the Binding Ability of H3K9me3 with
            the Promoters of Runx2, Osterix and Osteocalcin.
REFERENCE   5  (residues 1 to 971)
  AUTHORS   Johansson,C., Velupillai,S., Tumber,A., Szykowska,A., Hookway,E.S.,
            Nowak,R.P., Strain-Damerell,C., Gileadi,C., Philpott,M.,
            Burgess-Brown,N., Wu,N., Kopec,J., Nuzzi,A., Steuber,H., Egner,U.,
            Badock,V., Munro,S., LaThangue,N.B., Westaway,S., Brown,J.,
            Athanasou,N., Prinjha,R., Brennan,P.E. and Oppermann,U.
  TITLE     Structural analysis of human KDM5B guides histone demethylase
            inhibitor development
  JOURNAL   Nat Chem Biol 12 (7), 539-545 (2016)
   PUBMED   27214403
REFERENCE   6  (residues 1 to 971)
  AUTHORS   Sohi,G., Marchand,K., Revesz,A., Arany,E. and Hardy,D.B.
  TITLE     Maternal protein restriction elevates cholesterol in adult rat
            offspring due to repressive changes in histone modifications at the
            cholesterol 7alpha-hydroxylase promoter
  JOURNAL   Mol Endocrinol 25 (5), 785-798 (2011)
   PUBMED   21372147
REFERENCE   7  (residues 1 to 971)
  AUTHORS   Trojer,P., Zhang,J., Yonezawa,M., Schmidt,A., Zheng,H., Jenuwein,T.
            and Reinberg,D.
  TITLE     Dynamic Histone H1 Isotype 4 Methylation and Demethylation by
            Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji
            Domain-containing JMJD2/KDM4 Proteins
  JOURNAL   J Biol Chem 284 (13), 8395-8405 (2009)
   PUBMED   19144645
REFERENCE   8  (residues 1 to 971)
  AUTHORS   Fodor,B.D., Kubicek,S., Yonezawa,M., O'Sullivan,R.J., Sengupta,R.,
            Perez-Burgos,L., Opravil,S., Mechtler,K., Schotta,G. and
            Jenuwein,T.
  TITLE     Jmjd2b antagonizes H3K9 trimethylation at pericentric
            heterochromatin in mammalian cells
  JOURNAL   Genes Dev 20 (12), 1557-1562 (2006)
   PUBMED   16738407
REFERENCE   9  (residues 1 to 971)
  AUTHORS   Gray,S.G., Iglesias,A.H., Lizcano,F., Villanueva,R., Camelo,S.,
            Jingu,H., Teh,B.T., Koibuchi,N., Chin,W.W., Kokkotou,E. and
            Dangond,F.
  TITLE     Functional characterization of JMJD2A, a histone deacetylase- and
            retinoblastoma-binding protein
  JOURNAL   J Biol Chem 280 (31), 28507-28518 (2005)
   PUBMED   15927959
REFERENCE   10 (residues 1 to 971)
  AUTHORS   Zhang,D., Yoon,H.G. and Wong,J.
  TITLE     JMJD2A is a novel N-CoR-interacting protein and is involved in
            repression of the human transcription factor achaete scute-like
            homologue 2 (ASCL2/Hash2)
  JOURNAL   Mol Cell Biol 25 (15), 6404-6414 (2005)
   PUBMED   16024779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_233441.4, XP_001072204.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760386, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..971
                     /product="lysine-specific demethylase 4A isoform b"
                     /EC_number="1.14.11.-"
                     /note="lysine-specific demethylase 4A; jumonji domain
                     containing 2A; lysine (K)-specific demethylase 4A"
                     /calculated_mol_wt=109933
     Region          84..200
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          574..673
                     /region_name="PHD_JMJD2A"
                     /note="PHD finger found in Jumonji domain-containing
                     protein 2A (JMJD2A); cd15575"
                     /db_xref="CDD:277050"
     Site            order(574,641..645,649,668)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277050"
     Region          682..791
                     /region_name="ePHD_JMJD2A"
                     /note="Extended PHD finger (ePHD) found in Jumonji
                     domain-containing protein 2A (JMJD2A); cd15713"
                     /db_xref="CDD:277183"
     Site            order(736,750..754,760,786)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277183"
     Region          806..860
                     /region_name="Tudor_JMJD2A_rpt1"
                     /note="first Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20463"
                     /db_xref="CDD:410534"
     Site            order(838..839,841..844,846)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410534"
     Region          863..918
                     /region_name="Tudor_JMJD2A_rpt2"
                     /note="second Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20466"
                     /db_xref="CDD:410537"
     Site            order(874..876,880)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410537"
     CDS             1..971
                     /gene="Kdm4a"
                     /gene_synonym="Jmjd2a"
                     /coded_by="NM_001107966.2:228..3143"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313539"
                     /db_xref="RGD:1306378"
ORIGIN      
        1 mtvrefrkia nsdkyctpry sefeelerky wknltfnppi ygadvngtly eqhvdewnig
       61 rlktildlve kesgitiegv ntpylyfgmw ktsfawhted mdlysinylh fgepkswysv
      121 ppehgkrler lakgffpgsa qsceaflrhk mtlisplmlk kygipfdkvt qeagefmitf
      181 pygyhagfnh gfncaestnf atrrwieygk qavlcscrkd mvkismdvfv rrfqperykl
      241 wkagkdstvi dhtlptpeaa eflkdsgltp ragneecpee dseaaeqgee gdvkrslakh
      301 rigtkrhrvc leipqevsqs elfpkeelss gqyemtecqa tlapvrpths svrqvedslp
      361 fpdysdptev kfeelknvkl eeededeepe aaaldlsvnp esvegrlvfs gskkkasssl
      421 gssssqdsvs sdsettesvs cqgqektvlt vhsysrgdgk aapgepsvkr qrsaprsise
      481 qelaevadey mlsleenkkt kgrrqplskl prhhplvlqe cgsddetseq ltpeeeaeet
      541 eawakplsql wqnrppnfea ekefnelmaq qaphcavcmi fqtyhqvefg gfsqscgnas
      601 epaaqpqrtk plipemcftt tgcstdinls tpyleedgts mlvsckkcsv rvhascygvp
      661 pakaseewmc srcsanalee dcclcslrgg alqranddrw vhvscavail earfvniaer
      721 spvdvskipl prfklkcvfc kkrrkrnagc cvqcshgrcp tafhvscaqa agvmmqpddw
      781 pfvvfitcfr hkipnlerak gallsitagq kviskhkngr fyqcevvrlt tetfyevnfd
      841 dgsfsdnlyp edivsqdclq lgppaegevv qvrwtdgqvy gakfvashpi qmyqvefedg
      901 sqlvvkrddv ytldeelpkr vksrlsvasd mrfneiftek evkqekkrqr vinsryredy
      961 iepalyraim e
//
LOCUS       NP_001423765             900 aa            linear   ROD 21-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001423765 XP_038965978
VERSION     NP_001423765.1
DBSOURCE    REFSEQ: accession NM_001436836.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 900)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 900)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038965978.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.8150.1,
                                           SRR26643295.23231.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..900
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 6"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=101594
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <377..725
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <602..797
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..900
                     /gene="Srrm1"
                     /coded_by="NM_001436836.1:26..2728"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssederpkrs hvkngevgrr rrhspsrsas psprkrqket sprsrrrrsp
      541 sppparrrrs pspapppppp ppprrrrspt ppprrrtpsp pprrrspspr rysppiqrry
      601 spspppkrrt aspppppkrr aspspppkrr vshspppkqr sppvtkrrsp slsskhrkgs
      661 spgrstrear spqpnkrhsp sprprapqts spppvrrgas aspqgrqsps pstrpirrvs
      721 rtpepkkikk aaspspqsvr rvsssrsvsg speptakkpp appspvqsqs pstnwspaap
      781 akkaksptps psparnsdqe gggkkkkkkk dkkhkkdkkh kkhkkhkkek avavatpapa
      841 apaavsaaat psaqeepaaa peprketese aeddnlddle rhlrekalrs mrkaqvspqs
//
LOCUS       NP_001423634             631 aa            linear   ROD 21-MAR-2025
DEFINITION  polyadenylate-binding protein 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423634 XP_006238862
VERSION     NP_001423634.1
DBSOURCE    REFSEQ: accession NM_001436705.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Kini,H.K., Kong,J. and Liebhaber,S.A.
  TITLE     Cytoplasmic poly(A) binding protein C4 serves a critical role in
            erythroid differentiation
  JOURNAL   Mol Cell Biol 34 (7), 1300-1309 (2014)
   PUBMED   24469397
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Burgess,H.M., Richardson,W.A., Anderson,R.C., Salaun,C.,
            Graham,S.V. and Gray,N.K.
  TITLE     Nuclear relocalisation of cytoplasmic poly(A)-binding proteins
            PABP1 and PABP4 in response to UV irradiation reveals
            mRNA-dependent export of metazoan PABPs
  JOURNAL   J Cell Sci 124 (Pt 19), 3344-3355 (2011)
   PUBMED   21940797
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Yang,H., Duckett,C.S. and Lindsten,T.
  TITLE     iPABP, an inducible poly(A)-binding protein detected in activated
            human T cells
  JOURNAL   Mol Cell Biol 15 (12), 6770-6776 (1995)
   PUBMED   8524242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006238862.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19995.1,
                                           SRR26643298.28794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..631
                     /product="polyadenylate-binding protein 4 isoform 1"
                     /note="poly(A) binding protein, cytoplasmic 4 (inducible
                     form); polyadenylate-binding protein 4"
                     /calculated_mol_wt=69469
     Region          11..611
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..631
                     /gene="Pabpc4"
                     /coded_by="NM_001436705.1:885..2780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298510"
                     /db_xref="RGD:1305015"
ORIGIN      
        1 mnaaassypm aslyvgdlhs dvteamlyek fspagpvlsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pirimwsqrd pslrksgvgn vfiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy afvhfetqea ankaiekmng mllndrkvfv grfksrkere
      181 aelgakakef tnvyiknfge evddenlrel fsqfgktlsv kvmrdcsgks kgfgfvsyek
      241 hedankavee mngkemsgks ifvgraqkkv erqaelkrkf eqlkqerisr yqgvnlyikn
      301 lddtiddekl rkefspfgsi tsakvmledg rskgfgfvcf sspeeatkav temngrivgs
      361 kplyvalaqr keerkahltn qymqrvagmr alpanailnq fqpaaggyfv pavpqaqgrp
      421 pyytpnqlaq mrpnprwqqg grpqgfqgmp salrqsgprp alrhlaptgn apasrglptt
      481 aqrvgvptav pnlapratva aaapravapy kyasnvrsph paiqplqapq pavhvqgqep
      541 ltasmlaaap pqeqkqmlge rlfpliqtmh snlagkitgm lleidnsell hmlespeslr
      601 skvdeavavl qahhakkeaa qkvgtvaaat s
//
LOCUS       NP_001423600             727 aa            linear   ROD 21-MAR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase BAP1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423600 XP_006252668
VERSION     NP_001423600.1
DBSOURCE    REFSEQ: accession NM_001436671.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Qin,T., Lv,Y., Xi,X. and Wu,Z.
  TITLE     PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy
  JOURNAL   Biochem Pharmacol 226, 116374 (2024)
   PUBMED   38906226
  REMARK    GeneRIF: PLK-3-mediated phosphorylation of BAP1 prevents diabetic
            retinopathy.
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Liu,Y., Hu,N., Ai,B., Xia,H. and Li,W.
  TITLE     MiR-31-5p alleviates septic cardiomyopathy by targeting BAP1 to
            inhibit SLC7A11 deubiquitination and ferroptosis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 286 (2024)
   PUBMED   38816686
  REMARK    GeneRIF: MiR-31-5p alleviates septic cardiomyopathy by targeting
            BAP1 to inhibit SLC7A11 deubiquitination and ferroptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Misumi,K., Hayashi,A., Shibahara,J., Arita,J., Sakamoto,Y.,
            Hasegawa,K., Kokudo,N. and Fukayama,M.
  TITLE     Intrahepatic cholangiocarcinoma frequently shows loss of BAP1 and
            PBRM1 expression, and demonstrates specific clinicopathological and
            genetic characteristics with BAP1 loss
  JOURNAL   Histopathology 70 (5), 766-774 (2017)
   PUBMED   27864835
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Righi,L., Duregon,E., Vatrano,S., Izzo,S., Giorcelli,J.,
            Rondon-Lagos,M., Ascoli,V., Ruffini,E., Ventura,L., Volante,M.,
            Papotti,M. and Scagliotti,G.V.
  TITLE     BRCA1-Associated Protein 1 (BAP1) Immunohistochemical Expression as
            a Diagnostic Tool in Malignant Pleural Mesothelioma Classification:
            A Large Retrospective Study
  JOURNAL   J Thorac Oncol 11 (11), 2006-2017 (2016)
   PUBMED   27422796
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Napolitano,A., Pellegrini,L., Dey,A., Larson,D., Tanji,M.,
            Flores,E.G., Kendrick,B., Lapid,D., Powers,A., Kanodia,S.,
            Pastorino,S., Pass,H.I., Dixit,V., Yang,H. and Carbone,M.
  TITLE     Minimal asbestos exposure in germline BAP1 heterozygous mice is
            associated with deregulated inflammatory response and increased
            risk of mesothelioma
  JOURNAL   Oncogene 35 (15), 1996-2002 (2016)
   PUBMED   26119930
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Scheuermann,J.C., de Ayala Alonso,A.G., Oktaba,K., Ly-Hartig,N.,
            McGinty,R.K., Fraterman,S., Wilm,M., Muir,T.W. and Muller,J.
  TITLE     Histone H2A deubiquitinase activity of the Polycomb repressive
            complex PR-DUB
  JOURNAL   Nature 465 (7295), 243-247 (2010)
   PUBMED   20436459
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Machida,Y.J., Machida,Y., Vashisht,A.A., Wohlschlegel,J.A. and
            Dutta,A.
  TITLE     The deubiquitinating enzyme BAP1 regulates cell growth via
            interaction with HCF-1
  JOURNAL   J Biol Chem 284 (49), 34179-34188 (2009)
   PUBMED   19815555
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Misaghi,S., Ottosen,S., Izrael-Tomasevic,A., Arnott,D.,
            Lamkanfi,M., Lee,J., Liu,J., O'Rourke,K., Dixit,V.M. and
            Wilson,A.C.
  TITLE     Association of C-terminal ubiquitin hydrolase BRCA1-associated
            protein 1 with cell cycle regulator host cell factor 1
  JOURNAL   Mol Cell Biol 29 (8), 2181-2192 (2009)
   PUBMED   19188440
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Ventii,K.H., Devi,N.S., Friedrich,K.L., Chernova,T.A.,
            Tighiouart,M., Van Meir,E.G. and Wilkinson,K.D.
  TITLE     BRCA1-associated protein-1 is a tumor suppressor that requires
            deubiquitinating activity and nuclear localization
  JOURNAL   Cancer Res 68 (17), 6953-6962 (2008)
   PUBMED   18757409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252668.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.58127.1,
                                           SRR26360172.421545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..727
                     /product="ubiquitin carboxyl-terminal hydrolase BAP1
                     isoform 1"
                     /EC_number="3.4.19.12"
                     /note="BRCA1-associated protein 1; ubiquitin
                     carboxyl-terminal hydrolase BAP1; BRCA1 associated
                     protein-1 (ubiquitin carboxy-terminal hydrolase); Brca1
                     associated protein 1"
                     /calculated_mol_wt=80179
     Region          5..233
                     /region_name="Peptidase_C12_UCH37_BAP1"
                     /note="Cysteine peptidase C12 containing ubiquitin
                     carboxyl-terminal hydrolase (UCH) families UCH37 (UCH-L5)
                     and BAP1; cd09617"
                     /db_xref="CDD:187738"
     Region          56..60
                     /region_name="Arg-finger motif.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            order(85,91,169,184)
                     /site_type="other"
                     /note="cancer-causing mutation sites"
                     /db_xref="CDD:187738"
     Site            order(85,91,169,184)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:187738"
     Site            85
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01393; propagated
                     from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            184
                     /site_type="other"
                     /note="Important for enzyme activity.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01393; propagated
                     from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          273..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          363..366
                     /region_name="HBM-like motif.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          372..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          462..522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          573..622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          594..719
                     /region_name="Interaction with BRCA1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92560; propagated from
                     UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          640..684
                     /region_name="Interaction with YY1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          641..686
                     /region_name="UCH_C"
                     /note="Ubiquitin carboxyl-terminal hydrolases; pfam18031"
                     /db_xref="CDD:465622"
     Region          697..720
                     /region_name="Classical bipartite Nuclear localization
                     signal (NLS). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          697..699
                     /region_name="Interaction with nucleosomal DNA forming a
                     DNA clamp with ASXL1.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          702..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          711..727
                     /region_name="Positively charged C-terminal extension
                     (CTE). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          715..722
                     /region_name="Non-classical PY-nuclear localization signal
                     (PY-NLS). /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     Region          715..720
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q92560"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHS6.2)"
     CDS             1..727
                     /gene="Bap1"
                     /coded_by="NM_001436671.1:129..2312"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306257"
                     /db_xref="RGD:1311938"
ORIGIN      
        1 mnkgwleles dpglftllve dfgvkgvqve eiydlqskcq gpvygfiflf kwieerrsrr
       61 kvstlvddts vidddivnsm ffahqlipns cathallsvl lncsnvdlgp tlsrmkdftk
      121 gfspeskgya ignapelaka hnsharpepr hlpekqngls avrtmeafhf vsyvpitgrl
      181 feldglkvyp idhgpwgede ewtdkarrvi meriglatag epyhdirfnl mavvpdrrvk
      241 yearlhvlkg nrqtvlealq qlirvtqpel iqthksqesq lpeeskpass kspfgleagr
      301 tpaasectht dgaeevagsc pqttthspps ksklvvkpsg sslngvpptp tpivqrlpaf
      361 ldnhnyaksp mqeeedlaag vgrsrvpvrp qqysddeedy edeeedvqnt ssairykrkg
      421 tgkpgslsns sdgqlsvlqp ntinvltekl qesqkdlsip lsiktssgag spavavpths
      481 qpsptpsnes tdtaseigsa fnsplrspir sanptrpssp vtshiskvlf geddsllrvd
      541 cirynravrd lgpvistgll hlaedgvlsp lalteggkgs spstrssqgs qgsssleeke
      601 vvevtdsrdk sglnrssepl sgekyspkel lallkcveae ianyeaclke evekrkkfki
      661 ddqrrthnyd efictfisml aqegmlanlv eqnisvrrrq gvsigrlhkq rkpdrrkrsr
      721 pykakrq
//
LOCUS       NP_001423624             776 aa            linear   ROD 21-MAR-2025
DEFINITION  nuclear autoantigenic sperm protein isoform a [Rattus norvegicus].
ACCESSION   NP_001423624 XP_063143477
VERSION     NP_001423624.1
DBSOURCE    REFSEQ: accession NM_001436695.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhang,M., Liu,H., Gao,Y., Zhu,Z., Chen,Z., Zheng,P., Xue,L., Li,J.,
            Teng,M. and Niu,L.
  TITLE     Structural Insights into the Association of Hif1 with Histones
            H2A-H2B Dimer and H3-H4 Tetramer
  JOURNAL   Structure 24 (10), 1810-1820 (2016)
   PUBMED   27618665
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Kato,D., Osakabe,A., Tachiwana,H., Tanaka,H. and Kurumizaka,H.
  TITLE     Human tNASP promotes in vitro nucleosome assembly with histone H3.3
  JOURNAL   Biochemistry 54 (5), 1171-1179 (2015)
   PUBMED   25615412
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,W., Xie,S., Ni,M., Huang,X., Hu,S., Liu,Q., Liu,A., Zhang,J. and
            Zhang,Y.
  TITLE     MicroRNA-29a inhibited epididymal epithelial cell proliferation by
            targeting nuclear autoantigenic sperm protein (NASP)
  JOURNAL   J Biol Chem 287 (13), 10189-10199 (2012)
   PUBMED   22194605
  REMARK    GeneRIF: an increase of miR-29a, and hence decrease of Nasp, may
            contribute to inhibit cell proliferation during postnatal organ
            development.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Stanton,P.G., Sluka,P., Foo,C.F., Stephens,A.N., Smith,A.I.,
            McLachlan,R.I. and O'Donnell,L.
  TITLE     Proteomic changes in rat spermatogenesis in response to in vivo
            androgen manipulation; impact on meiotic cells
  JOURNAL   PLoS One 7 (7), e41718 (2012)
   PUBMED   22860010
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Wang,M., Shi,J.L., Cheng,G.Y., Hu,Y.Q. and Xu,C.
  TITLE     The antibody against a nuclear autoantigenic sperm protein can
            result in reproductive failure
  JOURNAL   Asian J Androl 11 (2), 183-192 (2009)
   PUBMED   19219058
  REMARK    Erratum:[Asian J Androl. 2009 Jul;11(4):492]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Richardson,R.T., Alekseev,O.M., Grossman,G., Widgren,E.E.,
            Thresher,R., Wagner,E.J., Sullivan,K.D., Marzluff,W.F. and
            O'Rand,M.G.
  TITLE     Nuclear autoantigenic sperm protein (NASP), a linker histone
            chaperone that is required for cell proliferation
  JOURNAL   J Biol Chem 281 (30), 21526-21534 (2006)
   PUBMED   16728391
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143477.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212041.1, SRR26360176.52831.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..776
                     /product="nuclear autoantigenic sperm protein isoform a"
                     /note="nuclear autoantigenic sperm protein
                     (histone-binding)"
                     /calculated_mol_wt=84069
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          115..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          <130..506
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          210..242
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          256..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          345..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          457..500
                     /region_name="Histone-binding.
                     /evidence=ECO:0000250|UniProtKB:P49321"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          499..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          528..604
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          530..567
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          530..563
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          530..558
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(531,534..535,538..539,541,573,576..577,580..581,
                     583..584,605,608..609,612)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          563..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          572..605
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          685..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Region          704..710
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49321; propagated from
                     UniProtKB/Swiss-Prot (Q66HD3.1)"
     CDS             1..776
                     /gene="Nasp"
                     /coded_by="NM_001436695.1:106..2436"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:298441"
                     /db_xref="RGD:1359609"
ORIGIN      
        1 matestataa iaaelvsadk vedapapsts adkmesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnvdeear eelreqvyda mgekeakkae gqsltkpetd keqesevekg
      181 gredmdisep aeklqekves tskqltesse eakeaaipgl nedevtsgkt eqeslcteeg
      241 ksisgvyvqn kefreavpqe egeemislek kpketsedqt igapekqdtl mkvveieaei
      301 dsevksvdvg geepkdqgai seselgkavl mqlsgqdvev spvvaaeags evsekpgqei
      361 tvlpnngpvv gqssagdqtp sepqnsaerl setkdgasve evkaelvpeq eeamppvees
      421 eaagdgvetk vaqratekap edkfkiaane etqerdeqmk egeetegsee edkendkaee
      481 ttnesvlekk tlqeneeeei gnlelawdml dlakiifkrq etkeaqlyaa qahlklgevs
      541 vesenyiqav eefqaclslq eqyleahdrl laethyqlgl aygynsqyde avaqfgksid
      601 viekrmavll eqmkeaegsf teyekeieel kellpeirek iedakesqrs gnvaelalka
      661 tlvesstsgf tpsgagasvs miasrkptdg asssncvtdi shlvrkkrkp eeesprkdda
      721 kkakpepevn ggsgdavssg nevsenmeae aenqaesqtt aegtvdsaat vkstac
//
LOCUS       NP_001423633             323 aa            linear   ROD 21-MAR-2025
DEFINITION  transmembrane protein CCDC163 isoform b [Rattus norvegicus].
ACCESSION   NP_001423633 XP_008762217
VERSION     NP_001423633.1
DBSOURCE    REFSEQ: accession NM_001436704.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_008762217.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.23862.1,
                                           SRR26360186.832014.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..323
                     /product="transmembrane protein CCDC163 isoform b"
                     /note="transmembrane protein CCDC163"
                     /calculated_mol_wt=36773
     Region          <82..>262
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..323
                     /gene="Ccdc163"
                     /coded_by="NM_001436704.1:433..1404"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:298442"
                     /db_xref="RGD:1564486"
ORIGIN      
        1 msrssswsdq lqavlsstde nmarikqsly plrvsstgdl adtwisphhl ppqpgaqaqq
       61 pwalktpilg eslscteahs sslwdevtkl rsqlqtqtqv tealrhsvqs llkdreqqmf
      121 kisaleaslk llqegpkgra lleqrleglr kelqglrsqv qelvqtqmrt rpgkfstasg
      181 fhqelqnehq llweeseilr eelkllrdql sqhqellleq maegrqvqar swktlehlqs
      241 gqmgkvhtle vtrteahdaq keepyllsse vslpdcdrsw ellkkldrel qnnslsnlep
      301 sssqfhaqdv gqedlflhgp rif
//
LOCUS       NP_001423629            1474 aa            linear   ROD 21-MAR-2025
DEFINITION  DNA excision repair protein ERCC-6 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423629 XP_006252796
VERSION     NP_001423629.1
DBSOURCE    REFSEQ: accession NM_001436700.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1474)
  AUTHORS   Xu,Y., Wu,Z., Liu,L., Liu,J. and Wang,Y.
  TITLE     Rat Model of Cockayne Syndrome Neurological Disease
  JOURNAL   Cell Rep 29 (4), 800-809 (2019)
   PUBMED   31644904
  REMARK    GeneRIF: Rat Model of Cockayne Syndrome Neurological Disease.
REFERENCE   2  (residues 1 to 1474)
  AUTHORS   Yang,Z., Liu,C., Wu,H., Xie,Y., Gao,H. and Zhang,X.
  TITLE     CSB affected on the sensitivity of lung cancer cells to
            platinum-based drugs through the global decrease of let-7 and
            miR-29
  JOURNAL   BMC Cancer 19 (1), 948 (2019)
   PUBMED   31615563
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1474)
  AUTHORS   West,H., Coffey,M., Wagner,M.J., McLeod,H.L., Colley,J.P.,
            Adams,R.A., Fleck,O., Maughan,T.S., Fisher,D., Kaplan,R.S.,
            Harris,R. and Cheadle,J.P.
  TITLE     Role for Nucleotide Excision Repair Gene Variants in
            Oxaliplatin-Induced Peripheral Neuropathy
  JOURNAL   JCO Precis Oncol 2, 1-18 (2018)
   PUBMED   35135151
REFERENCE   4  (residues 1 to 1474)
  AUTHORS   Luo,S.S., Liao,X.W. and Zhu,X.D.
  TITLE     Prognostic Value of Excision Repair Cross-Complementing mRNA
            Expression in Gastric Cancer
  JOURNAL   Biomed Res Int 2018, 6204684 (2018)
   PUBMED   30417012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1474)
  AUTHORS   Pascucci,B., Fragale,A., Marabitti,V., Leuzzi,G., Calcagnile,A.S.,
            Parlanti,E., Franchitto,A., Dogliotti,E. and D'Errico,M.
  TITLE     CSA and CSB play a role in the response to DNA breaks
  JOURNAL   Oncotarget 9 (14), 11581-11591 (2018)
   PUBMED   29545921
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1474)
  AUTHORS   Dianov,G., Bischoff,C., Sunesen,M. and Bohr,V.A.
  TITLE     Repair of 8-oxoguanine in DNA is deficient in Cockayne syndrome
            group B cells
  JOURNAL   Nucleic Acids Res 27 (5), 1365-1368 (1999)
   PUBMED   9973627
REFERENCE   7  (residues 1 to 1474)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Cockayne syndrome group B protein enhances elongation by RNA
            polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (21), 11205-11209 (1997)
   PUBMED   9326587
REFERENCE   8  (residues 1 to 1474)
  AUTHORS   van der Horst,G.T., van Steeg,H., Berg,R.J., van Gool,A.J., de
            Wit,J., Weeda,G., Morreau,H., Beems,R.B., van Kreijl,C.F., de
            Gruijl,F.R., Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Defective transcription-coupled repair in Cockayne syndrome B mice
            is associated with skin cancer predisposition
  JOURNAL   Cell 89 (3), 425-435 (1997)
   PUBMED   9150142
REFERENCE   9  (residues 1 to 1474)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Human transcription-repair coupling factor CSB/ERCC6 is a
            DNA-stimulated ATPase but is not a helicase and does not disrupt
            the ternary transcription complex of stalled RNA polymerase II
  JOURNAL   J Biol Chem 272 (3), 1885-1890 (1997)
   PUBMED   8999876
REFERENCE   10 (residues 1 to 1474)
  AUTHORS   Henning,K.A., Li,L., Iyer,N., McDaniel,L.D., Reagan,M.S.,
            Legerski,R., Schultz,R.A., Stefanini,M., Lehmann,A.R., Mayne,L.V.
            and Friedberg,E.C.
  TITLE     The Cockayne syndrome group A gene encodes a WD repeat protein that
            interacts with CSB protein and a subunit of RNA polymerase II TFIIH
  JOURNAL   Cell 82 (4), 555-564 (1995)
   PUBMED   7664335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252796.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.18370.1,
                                           SRR26360186.2394780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1474
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..1474
                     /product="DNA excision repair protein ERCC-6 isoform 1"
                     /note="DNA excision repair protein ERCC-6; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 6; excision repair
                     cross-complementation group 6"
                     /calculated_mol_wt=164694
     Region          83..159
                     /region_name="cc_ERCC-6_N"
                     /note="coiled-coil domain located near the N-terminus of
                     human Excision Repair Cross Complementing 6 (ERCC-6) and
                     related proteins; cd21397"
                     /db_xref="CDD:411064"
     Site            order(114,118)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:411064"
     Region          316..981
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          1402..1473
                     /region_name="CSB_WHD"
                     /note="winged-helix domain (WHD) found in cockayne
                     syndrome group B (CSB) and similar proteins; cd22254"
                     /db_xref="CDD:439329"
     Site            order(1402..1403,1406..1407,1409..1410,1413,1417..1418,
                     1423..1424,1453,1471..1473)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439329"
     CDS             1..1474
                     /gene="Ercc6"
                     /coded_by="NM_001436700.1:72..4496"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306274"
                     /db_xref="RGD:1311509"
ORIGIN      
        1 mpheeipnst qpqgqdwlpg qhvsadrdip agqetagdse agkclsspsc dhgpstsaea
       61 cvlaatrwgp allhidrhqi pavepsaqal elqglgvdvy dqavleegvl qqvdsamhea
      121 srvaqradae keyqsvlddl mscttslrqi nkiieqlspq aasnrdinrk ldsvkrqkyn
      181 keqqlkkita kqkrlqailg gaevhveldh gsleeedaep gpsclgsmlm paqesaweel
      241 irtgqmtpfg tpapqkqekk prkimlneas gfekyladqa qlsfkrkkqa ankrtakkav
      301 vvsessrgpn etkpnqrsqa lsqtdkrlkk hirklqrral qfqgkvglqr gkrplepeer
      361 pgaegdtege esgssptdge eeeeqeeegv avlssddisy elkplrkgqk yekkvpvqei
      421 dddffpssee edeavegrgg grkvsrrpdd gdedyykqrl rrwnrlrlqd keklkledds
      481 eesdaefdeg fkvpgflfkk lfkyqqtgvr wlwelhcqqa ggilgdemgl gktiqiiafl
      541 aglsyskirt rgsnyrfegl gptlivcptt vmhqwvkefh twwppfrvai lhetgscahr
      601 kerlvrdivh chgvlitsys yirlmqddis rhdwhyvild eghkirnpna avtlackqfr
      661 tphriilsgs pmqnnlrelw slfdftfpgk lgtlpvfmeq fsvpitmggy snaspvqvkt
      721 aykcacvlrd tinpyllrrm ksdvkmslsl pdkneqvlfc rltdeqhkvy qnfidskavy
      781 rilngenqif sglvalrkic nhpdlfsggp kntsalpedg leeeqfgywk rsgkmivves
      841 llkiwhkqgq rvllfsqsrq mlhilevflr ahkysylkmd gtttiasrqp litkynedts
      901 ifvfllttrv gglgvnltga nrviiydpdw npstdtqare rawrigqkkq vtvyrlltag
      961 tieekiyhrq ifkqfltnrv lkdpkqrrff ksndlyelft ltspdasqgt etsaifagtg
     1021 sniqtlkchf kkrtppvlqm dpkrkkplvs dtsvngatvm eeksqgsgat gsvpstesgp
     1081 lksdrhtdgs rassvgfgee adagstlehl sglsgdspav dhtsrlsava stsekqgssy
     1141 egeccqaqtg pvhlseqteg hfskhkskrk hdaaeeette kcpqpkqkak nsrhhrdakf
     1201 egtrvphlvk krryhqqtte qesgakdrss ddyvleklfk ksvgvhsvvk hdaiidgssp
     1261 dyvlveaean rvaqdalkal rlsrqqclga tsgvptwtgh rgisgapagv kkrfgqkrns
     1321 slpvqrpssl tertqnmkke geahtaehfs gkedgasssg apssssllar mrarnhmilp
     1381 erlesdgeql agaaaaaapp cstehdallv dmrnfiafqa qvdgqastqe ilqafeskls
     1441 vaqscvfrel lrnlcnfhrt pggegiwklk peyc
//
LOCUS       NP_001423641             838 aa            linear   ROD 21-MAR-2025
DEFINITION  granulocyte colony-stimulating factor receptor isoform a precursor
            [Rattus norvegicus].
ACCESSION   NP_001423641 XP_008762229
VERSION     NP_001423641.1
DBSOURCE    REFSEQ: accession NM_001436712.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Zhang,E., Lee,S., Yi,M.H., Nan,Y., Xu,Y., Shin,N., Ko,Y., Lee,Y.H.,
            Lee,W. and Kim,D.W.
  TITLE     Expression of granulocyte colony-stimulating factor 3 receptor in
            the spinal dorsal horn following spinal nerve ligation-induced
            neuropathic pain
  JOURNAL   Mol Med Rep 16 (2), 2009-2015 (2017)
   PUBMED   28656207
  REMARK    GeneRIF: the expression of GCSFR in neurons following peripheral
            nerve injury may be involved in the induction and maintenance of
            neuropathic pain through the STAT3 and TRPV1 signaling pathway.
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Aref,S., El-Ghonemy,M., Abouzeid,T., El-Sabbagh,A. and El-Baiomy,M.
  TITLE     Prevalence and impact of colony stimulating factor 3 receptor
            (CSF3R) mutations among Egyptian acute myeloid leukemia patients
  JOURNAL   Leuk Res 38 (6), 722-725 (2014)
   PUBMED   24746896
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Fleischman,A.G., Maxson,J.E., Luty,S.B., Agarwal,A., Royer,L.R.,
            Abel,M.L., MacManiman,J.D., Loriaux,M.M., Druker,B.J. and
            Tyner,J.W.
  TITLE     The CSF3R T618I mutation causes a lethal neutrophilic neoplasia in
            mice that is responsive to therapeutic JAK inhibition
  JOURNAL   Blood 122 (22), 3628-3631 (2013)
   PUBMED   24081659
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Kosmider,O., Itzykson,R., Chesnais,V., Lasho,T., Laborde,R.,
            Knudson,R., Gauthier,A., Merlevede,J., Ades,L., Morabito,M.,
            Fontenay,M., Tefferi,A., Droin,N. and Solary,E.
  TITLE     Mutation of the colony-stimulating factor-3 receptor gene is a rare
            event with poor prognosis in chronic myelomonocytic leukemia
  JOURNAL   Leukemia 27 (9), 1946-1949 (2013)
   PUBMED   23774674
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Hanumanthu,V.S. and Pirruccello,S.J.
  TITLE     GCSF-R expression in myelodysplastic and myeloproliferative
            disorders and blast dysmaturation in CML
  JOURNAL   Am J Clin Pathol 140 (2), 155-164 (2013)
   PUBMED   23897249
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Semerad,C.L., Poursine-Laurent,J., Liu,F. and Link,D.C.
  TITLE     A role for G-CSF receptor signaling in the regulation of
            hematopoietic cell function but not lineage commitment or
            differentiation
  JOURNAL   Immunity 11 (2), 153-161 (1999)
   PUBMED   10485650
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Otsuji,W., Tanase,S., Yoshida,S. and Bawden,J.W.
  TITLE     The immunohistochemical localization of the interferon-gamma and
            granulocyte colony-stimulating factor receptors during early
            amelogenesis in rat molars
  JOURNAL   Arch Oral Biol 44 (2), 173-181 (1999)
   PUBMED   10206335
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Hermans,M.H., Ward,A.C., Antonissen,C., Karis,A., Lowenberg,B. and
            Touw,I.P.
  TITLE     Perturbed granulopoiesis in mice with a targeted mutation in the
            granulocyte colony-stimulating factor receptor gene associated with
            severe chronic neutropenia
  JOURNAL   Blood 92 (1), 32-39 (1998)
   PUBMED   9639496
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Dong,F., Dale,D.C., Bonilla,M.A., Freedman,M., Fasth,A.,
            Neijens,H.J., Palmblad,J., Briars,G.L., Carlsson,G., Veerman,A.J.,
            Welte,K., Lowenberg,B. and Touw,I.P.
  TITLE     Mutations in the granulocyte colony-stimulating factor receptor
            gene in patients with severe congenital neutropenia
  JOURNAL   Leukemia 11 (1), 120-125 (1997)
   PUBMED   9001427
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Fukunaga,R., Ishizaka-Ikeda,E., Seto,Y. and Nagata,S.
  TITLE     Expression cloning of a receptor for murine granulocyte
            colony-stimulating factor
  JOURNAL   Cell 61 (2), 341-350 (1990)
   PUBMED   2158861
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_008762229.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.7667.1,
                                           SRR26360194.2138570.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..838
                     /product="granulocyte colony-stimulating factor receptor
                     isoform a precursor"
                     /note="granulocyte colony-stimulating factor receptor;
                     colony stimulating factor 3 receptor (granulocyte)"
                     /calculated_mol_wt=91301
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2540
     Region          24..111
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Region          123..221
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          433..521
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(513..514,516..517)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(529,593,608)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          532..609
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     CDS             1..838
                     /gene="Csf3r"
                     /coded_by="NM_001436712.1:350..2866"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:298518"
                     /db_xref="RGD:1309114"
ORIGIN      
        1 mvglgacnlt gvtlivlllp rslegcgqir isppivhlgd pvlasctisp ncskldrqpk
       61 ilwrlqdepn qpgdrqhhlp dgsqesiitl phlnytqafl fclvpwnnsf qvldqaelra
      121 gyppaspsnl sclmylttns lvcqwepgpe thlptsfilk sfrsrtgcqy qggtildcmp
      181 kkrhsncsip rkhlllyqnm viwvqaenml gssespklci dpmdvvklep pmlqaldigh
      241 divsrqpgcl wlswkpwkps efmeqecelr yqpqleganw tlvshlpsst drfelcslhq
      301 apvytlqlrc irsslpglws swspglqlrp tikaptirld twwqkkhldp etvrmqlfwk
      361 ptplqkdsgq iqgyllswsc pdgqgrimhl cnttelsctf hlpseaqnvt lvaynsagts
      421 sptlvvfleh egpavtslha maqdlgsiwv dweapsllpq gyliewgpds hkysnnswri
      481 epngnttgil lednihpfql yritvaplyp gtvgppvnvy tysgekalph apelylkhvg
      541 rtwaqlewvp etpwlgmipl tnytifwtda rdhsfsvtln isfhdfvldh lkpaslyhvy
      601 lmatsragst nstgltlmtm aldssdvnif lgilcfvlls itcatawfcc kqsrktffwp
      661 nvpdpahssl sawvptimte etfqlpsfwg ssvpsitkit eleedkkpth wdpsessgtg
      721 slpavvqayv lqgdpreisn qfqppsstnd qvlygqvlgs ptspevvgyl rcdstqpllg
      781 gptpspksye niwfhsrpqe tfipqppsqe ddcvfgppfd fplfqglqvh gveeqggf
//
LOCUS       NP_001423588             316 aa            linear   ROD 21-MAR-2025
DEFINITION  spermatogenesis-associated protein 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423588 XP_006253157
VERSION     NP_001423588.1
DBSOURCE    REFSEQ: accession NM_001436659.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Choi,E., Lee,J., Oh,J., Park,I., Han,C., Yi,C., Kim,D.H., Cho,B.N.,
            Eddy,E.M. and Cho,C.
  TITLE     Integrative characterization of germ cell-specific genes from mouse
            spermatocyte UniGene library
  JOURNAL   BMC Genomics 8, 256 (2007)
   PUBMED   17662146
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Liu,S.F., Ai,C., Ge,Z.Q., Liu,H.L., Liu,B.W., He,S. and Wang,Z.
  TITLE     Molecular cloning and bioinformatic analysis of SPATA4 gene
  JOURNAL   J Biochem Mol Biol 38 (6), 739-747 (2005)
   PUBMED   16336790
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Liu,S.F., He,S., Liu,B.W., Zhao,Y. and Wang,Z.
  TITLE     Cloning and characterization of testis-specific spermatogenesis
            associated gene homologous to human SPATA4 in rat
  JOURNAL   Biol Pharm Bull 27 (11), 1867-1870 (2004)
   PUBMED   15516739
  REMARK    GeneRIF: expressed specifically in the testis only; expression
            occurs in a development stage-dependent pattern; cloned
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006253157.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2204439.1,
                                           SRR26360186.2083499.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..316
                     /product="spermatogenesis-associated protein 4 isoform 1"
                     /note="spermatogenesis related gene 2;
                     spermatogenesis-associated protein 4"
                     /calculated_mol_wt=35772
     Region          54..144
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     CDS             1..316
                     /gene="Spata4"
                     /gene_synonym="Srg2; Tsarg2"
                     /coded_by="NM_001436659.1:9..959"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306441"
                     /db_xref="RGD:1303065"
ORIGIN      
        1 maaagraees lplpaaessk ttlptppavp aarkpkkclv yphpprssrl cpsvlrwlqg
       61 ldlsffprnv trdfsngylv aeifciyypw dlrlssfeng tslkvkldnw aqiekflakk
      121 kfklpkelih gtihckagvp eiliqeiytl lthqeirsiq ddfanftdys yqmrlplvpr
      181 stvsksiknn irlsellsnp nilsnelkie flfllqmlqr klsrklnpgw fdikptvgei
      241 tvghlpahsy khkykskvsk eravsslsks gndvqphrei hvkqngkpcd atakpminve
      301 etmkdteeva lkksch
//
LOCUS       NP_001423644             289 aa            linear   ROD 21-MAR-2025
DEFINITION  mitochondrial fission regulator 1-like isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423644
VERSION     NP_001423644.1
DBSOURCE    REFSEQ: accession NM_001436715.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.16348.1,
                                           SRR26643298.29498.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on manual assertion,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..289
                     /product="mitochondrial fission regulator 1-like isoform
                     a"
                     /note="protein FAM54B; family with sequence similarity 54,
                     member B"
                     /calculated_mol_wt=31599
     Region          7..250
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWE0; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H019; propagated from
                     UniProtKB/Swiss-Prot (Q5XII9.1)"
     CDS             1..289
                     /gene="Mtfr1l"
                     /gene_synonym="Fam54b; RGD1305453"
                     /coded_by="NM_001436715.1:164..1033"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:298549"
                     /db_xref="RGD:1305453"
ORIGIN      
        1 meanvtipiw qnkphgaars vvrrigtnlp lkpcprasfe tlpnisdlcl kdvppvptla
       61 diawiaadee etyarvrsdt rplrhtwkps plivmqrnas vpnlrgseer llalkkpalp
      121 alsrttelqd elshlrsqia kivaadaasa sltpdflssg ssnvssplpc fgssfhstts
      181 fvisditeet evevpelpti pllcsaspec cksehkttcs sseeddcisl skassfadmm
      241 gilkdfhrik qsqdlsrsll keedpavlis evlrrkfalk eedisrkgn
//
LOCUS       NP_001100691             289 aa            linear   ROD 21-MAR-2025
DEFINITION  complement C1q tumor necrosis factor-related protein 7 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_001100691 XP_001060132 XP_223507
VERSION     NP_001100691.1
DBSOURCE    REFSEQ: accession NM_001107221.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Bi,J., Duan,Y., Wang,M., He,C., Li,X., Zhang,X., Tao,Y., Du,Y. and
            Liu,H.
  TITLE     Deletion of large-conductance calcium-activated potassium channels
            promotes vascular remodelling through the CTRP7-mediated PI3K/Akt
            signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (12), 1-11 (2022)
   PUBMED   36514218
  REMARK    GeneRIF: Deletion of large-conductance calcium-activated potassium
            channels promotes vascular remodelling through the CTRP7-mediated
            PI3K/Akt signaling pathway.
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Rohrbach,S., Aurich,A.C., Li,L. and Niemann,B.
  TITLE     Age-associated loss in adiponectin-activation by caloric
            restriction: lack of compensation by enhanced inducibility of
            adiponectin paralogs CTRP2 and CTRP7
  JOURNAL   Mol Cell Endocrinol 277 (1-2), 26-34 (2007)
   PUBMED   17716811
  REMARK    GeneRIF: The purpose of the current study was to investigate
            age-dependent effects of caloric restriction on the release of
            adiponectin, expression and activation of adiponectin-related
            signaling and on parameters of altered insulin sensitivity.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Wong,G.W., Wang,J., Hug,C., Tsao,T.S. and Lodish,H.F.
  TITLE     A family of Acrp30/adiponectin structural and functional paralogs
  JOURNAL   Proc Natl Acad Sci U S A 101 (28), 10302-10307 (2004)
   PUBMED   15231994
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473963.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001060132.1, XP_223507.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM031994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..289
                     /product="complement C1q tumor necrosis factor-related
                     protein 7 isoform 1 precursor"
                     /note="complement C1q tumor necrosis factor-related
                     protein 7; C1q and tumor necrosis factor related protein
                     7; adiponectin g"
                     /calculated_mol_wt=28867
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1654
     Region          <56..>137
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          149..273
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..289
                     /gene="C1qtnf7"
                     /gene_synonym="Adig; Ctrp7"
                     /coded_by="NM_001107221.1:70..939"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:305423"
                     /db_xref="RGD:1306978"
ORIGIN      
        1 mivllyvtsl aicasgqprg nqakgesysp ryicsipglp gppgppgang spgphgrigl
       61 pgrdgrdgrk gekgekgtag lkgktgplgl agekgdqget gkkgpigpeg ekgevgpagp
      121 pgpkgdrgdq gdpglpgvcr cgsivlksaf svgittsype erlpiifnkv lfnegehynp
      181 atgkficafp giyyfsydit lankhlaigl vhngqyrirt fdantgnhdv asgstviylq
      241 pedevwleif fndqnglfsd pgwadslfsg fllyvdtdyl dsiseddel
//
LOCUS       NP_001423617             310 aa            linear   ROD 21-MAR-2025
DEFINITION  oxidoreductase NAD-binding domain-containing protein 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423617 XP_006252685
VERSION     NP_001423617.1
DBSOURCE    REFSEQ: accession NM_001436688.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 19, 2025 this sequence version replaced XP_006252685.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.47352.1,
                                           SRR26643291.37712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..310
                     /product="oxidoreductase NAD-binding domain-containing
                     protein 1 isoform 1"
                     /note="oxidoreductase NAD-binding domain-containing
                     protein 1"
                     /calculated_mol_wt=34716
     Region          68..307
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cd00322"
                     /db_xref="CDD:99778"
     Site            order(95,107..110,127..129,133..136,177)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(107,109..110)
                     /site_type="other"
                     /note="conserved FAD binding motif [chemical binding]"
                     /db_xref="CDD:99778"
     Site            order(133,136,139,146)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99778"
     Site            order(172,176..179,181)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99778"
     Site            order(177..178,213..215,282..283)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99778"
     CDS             1..310
                     /gene="Oxnad1"
                     /gene_synonym="RGD1311534"
                     /coded_by="NM_001436688.1:267..1199"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:306270"
                     /db_xref="RGD:1311534"
ORIGIN      
        1 mahvlipgls rgsvgaictq aaswalptst lrsltlasvm rsrrktdhle rtatvlrrev
       61 maaakvceit hespsvkslr llvadkdfsf kagqwvdffi pgvsvvggfs icsspqqler
      121 eriielavky tnhppavwvh nkctldseva lrvggefffd pqptdaprnl vliaggvgin
      181 pllsilrhsa dlhrdhkekr rgydigtikl fysakntsel lfkknildlv hefpekiacs
      241 fhvtkqttqi sselkpyvtd gritekeire hisaetlfyv cgpppmtdff skhlesshvp
      301 kehicfekww
//
LOCUS       NP_001423651             706 aa            linear   ROD 23-MAR-2025
DEFINITION  rho GTPase-activating protein 22 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423651 XP_063131428
VERSION     NP_001423651.1
DBSOURCE    REFSEQ: accession NM_001436722.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Valnegri,P., Montrasio,C., Brambilla,D., Ko,J., Passafaro,M. and
            Sala,C.
  TITLE     The X-linked intellectual disability protein IL1RAPL1 regulates
            excitatory synapse formation by binding PTPdelta and RhoGAP2
  JOURNAL   Hum Mol Genet 20 (24), 4797-4809 (2011)
   PUBMED   21926414
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_063131428.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1619976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663602, SAMN14984024
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..706
                     /product="rho GTPase-activating protein 22 isoform 1"
                     /note="rho GTPase-activating protein 22"
                     /calculated_mol_wt=77643
     Region          42..157
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          157..355
                     /region_name="RhoGAP_ARHGAP22_24_25"
                     /note="GTPase-activator protein (GAP) domain for Rho-like
                     GTPases found in ARHGAP22, 24 and 25-like proteins; longer
                     isoforms of these proteins contain an additional
                     N-terminal pleckstrin homology (PH) domain. ARHGAP25
                     (KIA0053) has been identified as a GAP for...; cd04390"
                     /db_xref="CDD:239855"
     Site            order(201,238,242,313,316..317,341)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239855"
     Site            201
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239855"
     Region          <372..>687
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          <598..>688
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..706
                     /gene="Arhgap22"
                     /coded_by="NM_001436722.1:374..2494"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306279"
                     /db_xref="RGD:1307237"
ORIGIN      
        1 mlpaasskrr tfasryftrs kslvmgeqsr spgrplaphk lgpvlkagwl rkqksimknw
       61 qqrwfvlrgd qlfyykdkde gkpqgfislq gtqvtellpd pddpgkhlfe itpggaaere
      121 kvpanpeall lmassqrdme dwvqairrvi waplgggifg qrledtvhhe rkfgprlapl
      181 lveqcvdfir erglseeglf rmpgqanlvr dlqdsfdcge kplfdsttdv htvasllkly
      241 lrelpepvip faryedflsc aqlltkdege gtvelakqvs nlpqanynll ryicrfldev
      301 qahsdvnkms vqnlatvfgp nilrpqvedp vtimegtslv qhlmtvlirk hgqlfatpsf
      361 eepasprgtv qgtvewgsee vtrdhqgepg ssglpthrts sldgpaaavl srtspprlgs
      421 qagpaatspg krmhtlpgwk ssfrqqgsrs espkgvsssl evpiissggn wlinglsslr
      481 shrrassgdr lkdtgsaqrl stydnvppss hlsstasvas tawsvasssr easigsctac
      541 rasnssacss lhtewaleps plpssseghp spdlghslde acvgsgssep ndpgspsqah
      601 vrrcralqgq vaelraelch qrieyqrslk sieegnsdlr kqmcrleeel dqekkkyaml
      661 eiklrnsera redaerrnql lqremeeffa tlgsltagtk garape
//
LOCUS       NP_001423670             623 aa            linear   ROD 23-MAR-2025
DEFINITION  transketolase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423670 XP_006252723
VERSION     NP_001423670.1
DBSOURCE    REFSEQ: accession NM_001436741.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Zhao,Y., Wu,Y., Hu,H., Cai,J., Ning,M., Ni,X. and Zhong,C.
  TITLE     Downregulation of transketolase activity is related to inhibition
            of hippocampal progenitor cell proliferation induced by thiamine
            deficiency
  JOURNAL   Biomed Res Int 2014, 572915 (2014)
   PUBMED   25028661
  REMARK    GeneRIF: results suggest that modulation of transketolase activity
            might be one of the mechanisms by which thiamine regulates the
            proliferation of hippocampal progenitor cells.
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Mitschke,L., Parthier,C., Schroder-Tittmann,K., Coy,J., Ludtke,S.
            and Tittmann,K.
  TITLE     The crystal structure of human transketolase and new insights into
            its mode of action
  JOURNAL   J Biol Chem 285 (41), 31559-31570 (2010)
   PUBMED   20667822
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Wang,J.J., Martin,P.R. and Singleton,C.K.
  TITLE     Aspartate 155 of human transketolase is essential for thiamine
            diphosphate-magnesium binding, and cofactor binding is required for
            dimer formation
  JOURNAL   Biochim Biophys Acta 1341 (2), 165-172 (1997)
   PUBMED   9357955
REFERENCE   7  (residues 1 to 623)
  AUTHORS   McCool,B.A., Plonk,S.G., Martin,P.R. and Singleton,C.K.
  TITLE     Cloning of human transketolase cDNAs and comparison of the
            nucleotide sequence of the coding region in Wernicke-Korsakoff and
            non-Wernicke-Korsakoff individuals
  JOURNAL   J Biol Chem 268 (2), 1397-1404 (1993)
   PUBMED   8419340
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Bublitz,C. and Steavenson,S.
  TITLE     The pentose phosphate pathway in the endoplasmic reticulum
  JOURNAL   J Biol Chem 263 (26), 12849-12853 (1988)
   PUBMED   2843500
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Casazza,J.P. and Veech,R.L.
  TITLE     The interdependence of glycolytic and pentose cycle intermediates
            in ad libitum fed rats
  JOURNAL   J Biol Chem 261 (2), 690-698 (1986)
   PUBMED   3079759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006252723.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55230.1,
                                           SRR22399484.1527130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..623
                     /product="transketolase isoform 1"
                     /EC_number="2.2.1.1"
                     /note="TK"
                     /calculated_mol_wt=67485
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Region          8..620
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            37
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P40142; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            258
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            538
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P40142; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     Site            603
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29401; propagated from
                     UniProtKB/Swiss-Prot (P50137.1)"
     CDS             1..623
                     /gene="Tkt"
                     /coded_by="NM_001436741.1:84..1955"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64524"
                     /db_xref="RGD:621036"
ORIGIN      
        1 megyhkpdqq klqalkdtan rlrissiqat taagsghpts ccsaaeimav lffhtmryka
       61 ldprnphndr fvlskghaap ilyavwaeag flpeaellnl rkissdldgh pvpkqaftdv
      121 atgslgqglg aacgmaytgk yfdkasyrvy cmlgdgevse gsvweamafa giykldnlva
      181 ifdinrlgqs dpaplqhqvd vyqkrceafg whaiivdghs veelckafgq akhqptaiia
      241 ktfkgrgitg iedkeawhgk plpknmaeqi iqeiysqvqs kkkilatppq edapsvdian
      301 irmptppnyk vgdkiatrka yglalaklgh asdriialdg dtknstfsel fkkehpdrfi
      361 ecyiaeqnmv siavgcatrd rtvpfcstfa afftrafdqi rmaaisesni nlcgshcgvs
      421 igedgpsqma ledlamfrsv pmstvfypsd gvatekavel aantkgicfi rtsrpenaii
      481 ysnnedfqvg qakvvlkskd dqvtvigagv tlhealaaae mlkkekigvr vldpftikpl
      541 dkklildcar atkgriltve dhyyeggige avsaavvgep gvtvtrlavs qvprsgkpae
      601 llkmfgidkd aivqavkglv tkg
//
LOCUS       NP_001423692            1962 aa            linear   ROD 23-MAR-2025
DEFINITION  CASP8-associated protein 2 [Rattus norvegicus].
ACCESSION   NP_001423692 XP_006238036
VERSION     NP_001423692.1
DBSOURCE    REFSEQ: accession NM_001436763.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1962)
  AUTHORS   Wu,T.Y., Leng,Q. and Tian,L.Q.
  TITLE     The microRNA-210/Casp8ap2 Axis Alleviates Hypoxia-Induced
            Myocardial Injury by Regulating Apoptosis and Autophagy
  JOURNAL   Cytogenet Genome Res 161 (3-4), 132-142 (2021)
   PUBMED   33882492
  REMARK    GeneRIF: The microRNA-210/Casp8ap2 Axis Alleviates Hypoxia-Induced
            Myocardial Injury by Regulating Apoptosis and Autophagy.
REFERENCE   2  (residues 1 to 1962)
  AUTHORS   Li,K., Pan,J., Li,Q., Li,S., Li,K., Cheng,Y., Chai,L., Li,C.,
            Li,J., Fu,Z., Wang,D. and Bai,Y.
  TITLE     The MicroRNA-210/Casp8ap2 Pathway Alleviates Hypoxia-Induced Injury
            in Myocardial Cells by Regulating Apoptosis and Autophagy
  JOURNAL   Heart Surg Forum 23 (6), E797-E802 (2020)
   PUBMED   33234216
  REMARK    GeneRIF: The MicroRNA-210/Casp8ap2 Pathway Alleviates
            Hypoxia-Induced Injury in Myocardial Cells by Regulating Apoptosis
            and Autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1962)
  AUTHORS   Li,T., Song,X., Zhang,J., Zhao,L., Shi,Y., Li,Z., Liu,J., Liu,N.,
            Yan,Y., Xiao,Y., Tian,X., Sun,W., Guan,Y. and Liu,B.
  TITLE     Protection of Human Umbilical Vein Endothelial Cells against
            Oxidative Stress by MicroRNA-210
  JOURNAL   Oxid Med Cell Longev 2017, 3565613 (2017)
   PUBMED   28367268
REFERENCE   4  (residues 1 to 1962)
  AUTHORS   Sun,H. and Hunter,T.
  TITLE     Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins
            identified through a string search
  JOURNAL   J Biol Chem 287 (50), 42071-42083 (2012)
   PUBMED   23086935
REFERENCE   5  (residues 1 to 1962)
  AUTHORS   Kim,H.W., Mallick,F., Durrani,S., Ashraf,M., Jiang,S. and
            Haider,K.H.
  TITLE     Concomitant activation of miR-107/PDCD10 and hypoxamir-210/Casp8ap2
            and their role in cytoprotection during ischemic preconditioning of
            stem cells
  JOURNAL   Antioxid Redox Signal 17 (8), 1053-1065 (2012)
   PUBMED   22482882
  REMARK    GeneRIF: The ischemic preconditioning (IPC) enhances stem cell
            survival via the combined participation of hypoxia responsive miRs
            miR-107 and miR-210 via their respective putative target genes
            Pdcd10 and Casp8ap2.
REFERENCE   6  (residues 1 to 1962)
  AUTHORS   Kim,H.W., Haider,H.K., Jiang,S. and Ashraf,M.
  TITLE     Ischemic preconditioning augments survival of stem cells via
            miR-210 expression by targeting caspase-8-associated protein 2
  JOURNAL   J Biol Chem 284 (48), 33161-33168 (2009)
   PUBMED   19721136
  REMARK    GeneRIF: Data identified FLICE-associated huge protein
            (FLASH)/caspase-8-associated protein-2 (Casp8ap2) in (PC)MSCs as
            the target gene of miR-210.
REFERENCE   7  (residues 1 to 1962)
  AUTHORS   Smith,A.J., Karpova,Y., D'Agostino,R. Jr., Willingham,M. and
            Kulik,G.
  TITLE     Expression of the Bcl-2 protein BAD promotes prostate cancer growth
  JOURNAL   PLoS One 4 (7), e6224 (2009)
   PUBMED   19593445
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1962)
  AUTHORS   Milovic-Holm,K., Krieghoff,E., Jensen,K., Will,H. and Hofmann,T.G.
  TITLE     FLASH links the CD95 signaling pathway to the cell nucleus and
            nuclear bodies
  JOURNAL   EMBO J 26 (2), 391-401 (2007)
   PUBMED   17245429
REFERENCE   9  (residues 1 to 1962)
  AUTHORS   Kino,T. and Chrousos,G.P.
  TITLE     Tumor necrosis factor alpha receptor- and Fas-associated FLASH
            inhibit transcriptional activity of the glucocorticoid receptor by
            binding to and interfering with its interaction with p160 type
            nuclear receptor coactivators
  JOURNAL   J Biol Chem 278 (5), 3023-3029 (2003)
   PUBMED   12477726
REFERENCE   10 (residues 1 to 1962)
  AUTHORS   Imai,Y., Kimura,T., Murakami,A., Yajima,N., Sakamaki,K. and
            Yonehara,S.
  TITLE     The CED-4-homologous protein FLASH is involved in Fas-mediated
            activation of caspase-8 during apoptosis
  JOURNAL   Nature 398 (6730), 777-785 (1999)
   PUBMED   10235259
  REMARK    Erratum:[Nature 1999 Jul 1;400(6739):89]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006238036.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1962
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..1962
                     /product="CASP8-associated protein 2"
                     /calculated_mol_wt=219560
     Region          <70..142
                     /region_name="ADIP"
                     /note="Afadin- and alpha -actinin-Binding; pfam11559"
                     /db_xref="CDD:463295"
     Region          1896..1960
                     /region_name="CASP8AP2"
                     /note="Caspase 8-associated protein 2 myb-like domain;
                     cd12202"
                     /db_xref="CDD:213401"
     CDS             1..1962
                     /gene="Casp8ap2"
                     /coded_by="NM_001436763.1:372..6260"
                     /db_xref="GeneID:313128"
                     /db_xref="RGD:1305771"
ORIGIN      
        1 maadddngdg tglfdvcpas plknndegsl diyagldstv sdstarscvs frncldlyee
       61 ilteegtake atysdlqiey gkcqqqmkdl mkrfkeiqtq nlnlknenqs lkknisalik
      121 tarveinrkd eeinhlhqrl sefphfrnnh ktartkdsrs ksphldncsk tdhgvksdvq
      181 kdihpntsqp nlekegkshs eaqnslhlst giekhctnnv wsrspyqvse gnsnednrrg
      241 rngvrhsqgs rgtdrtqkdl nsscndgepr dkeaasrlhg npekhgssea raenkiseik
      301 sstglgnkse rsassweket srerphtrve pqndknlerq nerlqnthrk elqsqdkaer
      361 kgdvkfkpag eeqghrgrvd ralpphsknd mkyygfnkyh peerrgredg krdrgmsshg
      421 fqdrrcsssl ssnrnskyph skevsvahqw entpfkaerh rtedrrkrer enkeesrhvk
      481 sdkksppehl qrthkdtkks tangkrqteq khgkgpvsts elskgtdnre ctmkvengpn
      541 eakgkdlkls fmeklnltls pakkqpvcqd nehqiigvpk psgvcdsqsl ektetvaclp
      601 svseqdreep kselpepkea lsatsqprts ipenkvkeen rllfksvent vpcellacgt
      661 eisfpapvei eqarclvqsm eveetcagar aaasvvmrvl pehasedfsq elgtkrhddi
      721 nscdiseggk kkvvlspkaa aaseshlepv veepsispvn csgdnnpkle psleerpkve
      781 nkssplepcl pkemfvpspq ktelidhkid tgesnsvyqd ddnsvlsidf nnlrpipepi
      841 splnspvrpv skvlsmessc tiplydsshk defpsnstls tfksqsdlnk enekpvpkld
      901 kcseaesckn lsvdeleege irsddeesva qkrleksarp rtstevppgk ispgsrrstv
      961 hvhkdngrtv vklprdritw sqrsnesrps nterksktms isslekilpl ilapssvwev
     1021 mhmlrllgkh vrknymkfki kfsltqfhri iesailsfts liryldlski cksvstlqks
     1081 lcdviesnlk qvkkngivdr lfeqqqtdmk kklwkfvdeq ldylfeklkk illkfcdsvk
     1141 hendssegkl gkkykeraqh sncqkkkmdn keirrekvlk sentvnfkss lgcekfeekh
     1201 qdqnktnttt vkhdvkrtfs tctdnntkns eckeqflgmn cpstprpget egnveegtpa
     1261 aqhacvkser gfeilteqqa ssltfnlvsd aqmgeifksl lqgsdlldtg gtekaewelk
     1321 tpekqllesl kcesapactt eelvseaasl cpkvisddnw sllssekgps lssglslpvh
     1381 pdvldencmf evssnlalsk dnvysseksk pcissilled lavsltvpsp lksdghlsfl
     1441 kpevlststp eevisahfse dalleeedas eqdihlales dnsssksscs swtsrsvasg
     1501 fqyhpnlpmh avimeksndh fivkirratp stspglkhgm vaeesltplp rtgkeadgaa
     1561 ekeptlfqst vlnpvqdlen sdksidkskp thedqnsivq tqvpdiyefl kdasnkvvhc
     1621 dqvvddcfkl hqvwepkvse slqelpsmek nahsvddhlp nthidltkdp atetkslelm
     1681 dvtvldidhl ehskpnldqd aqitctslqh davdafidlt hdvsneskne snepvltveg
     1741 vgcqvicidd dnhkegkvgk vnsslectve etcidltses agsfevkrht lkseppsksd
     1801 clelpetlgn ghkkrknspa vshssqkkqr kdmdlssekt krlspnsdrt gdahrkhgsk
     1861 krepavsdts lssevnpevk gstaplatfp gslsaknvik kkgeiivswt rnddreille
     1921 cqkrmpslkt fthlavklnk npnqvserfq qlkklfeksk cr
//
LOCUS       NP_001423691            1811 aa            linear   ROD 23-MAR-2025
DEFINITION  protein virilizer homolog isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423691 XP_063143645
VERSION     NP_001423691.1
DBSOURCE    REFSEQ: accession NM_001436762.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1811)
  AUTHORS   Hong,H., Xu,G., Bao,G., Zhang,J., Chen,C., Chen,J., Wu,C.,
            Jiang,J., Huang,J., Huang,H. and Cui,Z.
  TITLE     VIRMA promotes neuron apoptosis via inducing m6A methylation of
            STK10 in spinal cord injury animal models
  JOURNAL   CNS Neurosci Ther 30 (3), e14453 (2024)
   PUBMED   37721438
  REMARK    GeneRIF: VIRMA promotes neuron apoptosis via inducing m6A
            methylation of STK10 in spinal cord injury animal models.
REFERENCE   2  (residues 1 to 1811)
  AUTHORS   Wen,J., Lv,R., Ma,H., Shen,H., He,C., Wang,J., Jiao,F., Liu,H.,
            Yang,P., Tan,L., Lan,F., Shi,Y.G., He,C., Shi,Y. and Diao,J.
  TITLE     Zc3h13 Regulates Nuclear RNA m6A Methylation and Mouse Embryonic
            Stem Cell Self-Renewal
  JOURNAL   Mol Cell 69 (6), 1028-1038 (2018)
   PUBMED   29547716
REFERENCE   3  (residues 1 to 1811)
  AUTHORS   Yue,Y., Liu,J., Cui,X., Cao,J., Luo,G., Zhang,Z., Cheng,T., Gao,M.,
            Shu,X., Ma,H., Wang,F., Wang,X., Shen,B., Wang,Y., Feng,X., He,C.
            and Liu,J.
  TITLE     VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near
            stop codon and associates with alternative polyadenylation
  JOURNAL   Cell Discov 4, 10 (2018)
   PUBMED   29507755
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1811)
  AUTHORS   Schwartz,S., Mumbach,M.R., Jovanovic,M., Wang,T., Maciag,K.,
            Bushkin,G.G., Mertins,P., Ter-Ovanesyan,D., Habib,N.,
            Cacchiarelli,D., Sanjana,N.E., Freinkman,E., Pacold,M.E.,
            Satija,R., Mikkelsen,T.S., Hacohen,N., Zhang,F., Carr,S.A.,
            Lander,E.S. and Regev,A.
  TITLE     Perturbation of m6A writers reveals two distinct classes of mRNA
            methylation at internal and 5' sites
  JOURNAL   Cell Rep 8 (1), 284-296 (2014)
   PUBMED   24981863
REFERENCE   5  (residues 1 to 1811)
  AUTHORS   Horiuchi,K., Kawamura,T., Iwanari,H., Ohashi,R., Naito,M.,
            Kodama,T. and Hamakubo,T.
  TITLE     Identification of Wilms' tumor 1-associating protein complex and
            its role in alternative splicing and the cell cycle
  JOURNAL   J Biol Chem 288 (46), 33292-33302 (2013)
   PUBMED   24100041
REFERENCE   6  (residues 1 to 1811)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_063143645.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.14777.1,
                                           SRR26643295.20652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1811
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..1811
                     /product="protein virilizer homolog isoform 1"
                     /calculated_mol_wt=201399
     Region          5..235
                     /region_name="VIR_N"
                     /note="Virilizer, N-terminal; pfam15912"
                     /db_xref="CDD:464938"
     CDS             1..1811
                     /gene="Virma"
                     /gene_synonym="RGD1559904"
                     /coded_by="NM_001436762.1:25..5460"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:313061"
                     /db_xref="RGD:1559904"
ORIGIN      
        1 mavdssmell fldtfkhpsa eqsshidvvr fpcvvyinev rvippgvrah sglpdnrayg
       61 etsphtfqld lffnnvskps apvfdrlgsl eydentsiif rpnskvntdg lvlrgwyncl
      121 tlaiygsvdr vlshdrdspp pppppppppq pqptlkrslk hadgekedqf ngspprpqpr
      181 gprtppgppp pdddeddpms lpvsgdkeed vphredyfep ispdrnsvpq egqysdegev
      241 eeeqqeeged deddvdvdee edededdcht vdsipdddee deeeegeede egegddgyeq
      301 issdedgiad leretfkypn fdveytpedl asvppmtydp ydrelvplly fscpykttfe
      361 ieinrmkdqg pdkensgaie aslkltelld lyhedrgakw vtaleevpsl iikglsylql
      421 kntkqdslgq lvdwtmqaln lqvafrqpia lnvrqlkagt klvtslaecg apgvtellqa
      481 gvisvlfdll fadhvssslk lnafkaldsv ismtegmeaf lrstqseksg yqkllelill
      541 dqtvrvvtag sailqkchfy evlseikrlg dhiaektssv pnpsepdhdt davleranpd
      601 yeneveasmd mdllessnis egeieklinl leevfhlmet aphtmiqppv ksfptiarit
      661 gpperddpyp vlfrylhshh flelvtllls ipitsahpgv lqatkdvlkf laqsqkgllf
      721 fmseyeatnl liralchlyd qdeeeglqsd gvddafalwl qdstqtlqcv telfshfqrc
      781 taseetdhsd llgtlhnlyl itfnpvgrsa vghvfsldkn lqslitlmey yskealgdsk
      841 skksvaynya cililvvvqs ssdvqmleqh aasllklcka dennaklqel gkwleplknl
      901 rfeincipnl ieyvkqnidn lmtaegvglt talrvlcnva cppppvegqq kdlkwnlavi
      961 qlfsaegmdt firvlqklns iltqpwrlhv nmgttlhrvt tismarctlt llktmltell
     1021 rggsfefkdm rvpsalvtlh mllcsiplsg rldsdeqkiq ndiidilltf tqgvneklti
     1081 seetlanntw slmlkevlss ilkvpegffs glillsellp lplpmqttqv iephdisval
     1141 ntrklwsmhl hvqakllqei vrsfsgttcq piqhmlrric vqlcdlaspt allimrtvld
     1201 livedlqsts edkekqytsq ttrllallda lashkackla ilhlingtik gdekyaeifq
     1261 dllalvrspg dsvirqqcve yvtsilqslc dqdialilps psegpgsele qlsnslpske
     1321 lmaaicdcll atlansesty nclltcvrtm mflaehdygl fhlksslrkn ssalhsllkr
     1381 vvstfskdtg eltsasldfm rqilnsdamg ccgddsglme vesahpprtm sinaaelkql
     1441 lqskeespes lfleleklvl ehskeddsle slldnviglk qmlessgdpl plsdqdvepv
     1501 lsapeslqnl fnnrtayvla dvmddqlksm wftpfqaeei dtdldlvkvd lielsekccs
     1561 dfdlhseler sflsepsspg rakttkgfkl gkhkhetfit ssgkseyiep akrahvvppp
     1621 rgrgrggfgq girphdifrq rkqntsrpps mhvddfvaae skevvpqdgi pppkrplkvs
     1681 qkissrggfs gnrggrgafh sqnrfftppa skgnysrreg trgsswsaqn tprgnynesr
     1741 ggqsnfnrgp lpplrplsst gyrpsprdra srgrgglgps wastnsgsgg srgkfvsggs
     1801 grgrhvrsft r
//
LOCUS       NP_001423686             329 aa            linear   ROD 23-MAR-2025
DEFINITION  DGAT1/2-independent enzyme synthesizing storage lipids isoform a
            [Rattus norvegicus].
ACCESSION   NP_001423686 XP_006237889
VERSION     NP_001423686.1
DBSOURCE    REFSEQ: accession NM_001436757.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006237889.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.443737.1,
                                           SRR26643286.15762.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..329
                     /product="DGAT1/2-independent enzyme synthesizing storage
                     lipids isoform a"
                     /note="DGAT1/2-independent enzyme synthesizing storage
                     lipids"
                     /calculated_mol_wt=37665
     Region          103..309
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(129,132,135,150..153,198..200)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..329
                     /gene="Tmem68"
                     /gene_synonym="RGD1309006"
                     /coded_by="NM_001436757.1:269..1258"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:312946"
                     /db_xref="RGD:1309006"
ORIGIN      
        1 minnnqtcaa gqdsvpyvtc mlhvleewlg veqledylnf anhllwvftp lillilpyft
       61 ifllyltiif lhiykrknvl keayshnlwd garktvatlw dghaavwhgy evhgmekipe
      121 gpaliifyhg aipidfyyfm akifihkgrt crvvadhfvf kipgfsllld vfcalhgpre
      181 kcveilrsgh llaispggvr eallsdetyn iiwgnrkgfa qvaidakvpi ipmftqnire
      241 gfrslggtrl fkwlyekfry pfapmyggfp vklrtflgdp ipydpevtae elaektknav
      301 qalidkhqri pgnirsalld rfhkeqkan
//
LOCUS       NP_001423665             612 aa            linear   ROD 23-MAR-2025
DEFINITION  pleckstrin homology domain-containing family N member 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423665 XP_006239627
VERSION     NP_001423665.1
DBSOURCE    REFSEQ: accession NM_001436736.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Kuriyama,S., Tsuji,T., Sakuma,T., Yamamoto,T. and Tanaka,M.
  TITLE     PLEKHN1 promotes apoptosis by enhancing Bax-Bak
            hetro-oligomerization through interaction with Bid in human colon
            cancer
  JOURNAL   Cell Death Discov 4, 11 (2018)
   PUBMED   29531808
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Maeda,A., Uchida,M., Nishikawa,S., Nishino,T. and Konishi,H.
  TITLE     Role of N-myristoylation in stability and subcellular localization
            of the CLPABP protein
  JOURNAL   Biochem Biophys Res Commun 495 (1), 1249-1256 (2018)
   PUBMED   29180010
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Nishino,T., Matsunaga,R., Jikihara,H., Uchida,M., Maeda,A., Qi,G.,
            Abe,T., Kiyonari,H., Tashiro,S., Inagaki-Ohara,K., Shimamoto,F. and
            Konishi,H.
  TITLE     Antagonizing effect of CLPABP on the function of HuR as a regulator
            of ARE-containing leptin mRNA stability and the effect of its
            depletion on obesity in old male mouse
  JOURNAL   Biochim Biophys Acta 1861 (11), 1816-1827 (2016)
   PUBMED   27616329
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Sano,E., Shono,S., Tashiro,K., Konishi,H., Yamauchi,E. and
            Taniguchi,H.
  TITLE     Novel tyrosine phosphorylated and cardiolipin-binding protein
            CLPABP functions as mitochondrial RNA granule
  JOURNAL   Biochim Biophys Acta 1783 (6), 1036-1047 (2008)
   PUBMED   18191643
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006239627.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.25210.1,
                                           SRR26643294.24142.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..612
                     /product="pleckstrin homology domain-containing family N
                     member 1 isoform 1"
                     /note="pleckstrin homology domain containing, family N
                     member 1"
                     /calculated_mol_wt=67146
     Region          96..188
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          222..341
                     /region_name="PH_PLEKHN1"
                     /note="Pleckstrin homology domain containing family N
                     member 1Pleckstrin homology-like domain; cd13323"
                     /db_xref="CDD:270132"
     CDS             1..612
                     /gene="Plekhn1"
                     /gene_synonym="RGD1311019"
                     /coded_by="NM_001436736.1:43..1881"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298694"
                     /db_xref="RGD:1311019"
ORIGIN      
        1 mgnshcvpqt prrlrasfsr kpslkgnred sarklaglfg tearpdgdta ankifhyipg
       61 tdilgpenhp enleqpflsv fkkgwrrtpv rnlgkvvhys kvqlrfqhsq disdcylelf
      121 pshlyfqahg segltfqgll pltelsicpi dgsrehafqi tgplpapllv lchseaelsh
      181 wlyhlekqma llglrqchsa ppqgslgdkl pwtqlwrahg cepmnsaica srvklqhlps
      241 qeqwdrllvl ypaslaifse epeglnfkge lplsaihinl eekekeirsf liegrlinti
      301 rvvcasyedy sqwllclrtv shrdgahllp gpesfpglqr ptqvlgrgrg slssngrtsr
      361 klecpvfpts qslpepsvpt tigvpahpvp nqtnsncvst gqtkvelrhs gssqfprgka
      421 qrevsgstap lplhldltkm svlnldsgpe aqdcspdiph splyadpytp paiahhkitd
      481 iqgldeflca vqtspgpels spfpsvsvsv pvsdsnsgis ssprplgshl lskkgalqsr
      541 asqrhrgsik srapqpsdfp qlvtparegt psslppppde eapiwnktss pshqkwshpr
      601 kpaveggfiq wi
//
LOCUS       NP_001423667             850 aa            linear   ROD 23-MAR-2025
DEFINITION  solute carrier organic anion transporter family member 5A1 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001423667 XP_008761717
VERSION     NP_001423667.1
DBSOURCE    REFSEQ: accession NM_001436738.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Kindla,J., Rau,T.T., Jung,R., Fasching,P.A., Strick,R., Stoehr,R.,
            Hartmann,A., Fromm,M.F. and Konig,J.
  TITLE     Expression and localization of the uptake transporters OATP2B1,
            OATP3A1 and OATP5A1 in non-malignant and malignant breast tissue
  JOURNAL   Cancer Biol Ther 11 (6), 584-591 (2011)
   PUBMED   21278488
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_008761717.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.14590.1,
                                           SRR26643289.14626.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q11"
     Protein         1..850
                     /product="solute carrier organic anion transporter family
                     member 5A1 isoform 1"
                     /calculated_mol_wt=92296
     Region          131..676
                     /region_name="MFS_SLCO5_OATP5"
                     /note="Solute carrier organic anion transporter 5 family
                     of the Major Facilitator Superfamily of transporters;
                     cd17404"
                     /db_xref="CDD:340962"
     Site            order(145..146,149..150,153,185,281..282,284..286,289,309,
                     312..313,316,442,445..446,449..451,454,483,487,528..529,
                     533,537,599,602..603,606..607,610)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340962"
     CDS             1..850
                     /gene="Slco5a1"
                     /coded_by="NM_001436738.1:690..3242"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:312907"
                     /db_xref="RGD:1307132"
ORIGIN      
        1 mdegaaqsra qeqleapslv gavqenfese sfrskslpvl hsascrqnls agnadgklal
       61 gsieasghqe thpgrnlivp spsapstsag tttelmdcnh rrdpsktvsv sstlatlqer
      121 rclyvvltds rcflvcmcfl tfiqalmvsg ylssvittie rryslksses gllvscfdig
      181 nlvvvvfvsy fggrgrrplw lavgglliai gaalfalphf isppyqiqel nasasndglc
      241 qngnstaile pppcpkdsgg nshwiyvalf vcaqvligmg stpiytlgpt ylddnvkkdn
      301 aslylaimyv mgalgpavgy llgglligfy vdprnpvlld qndprfignw wsgfllcaia
      361 mflvifpmft fpkklpprhk kkkkfsadvv sdddiikeks ntseqvnkkv ssmgfgknvr
      421 dlpraavril snmtflfvsl sytaesaivt afitfipkfi esqfgipasn asiytgviiv
      481 psagvgivlg gyiikklklg aresaklami csgvsllcfs tlfivgcesi nlgginipyt
      541 tgpsltmphr nltgscnvnc gckiheyepv cgsdgityfn pclagcinsg nlttgvrnyt
      601 ectcvqsrqv itpptvgqrs qlrvvivkty lnengyavsg kckracntli pflvflfivt
      661 fitacaqpsa iivtlrsved eerpfalgmq fvllrtlayi ptpiyfgavi dttcmlwqqe
      721 cgvqgscwey nvtsfrfvyf glaaglkfvg fififlawys ikykedelqr rrcrdfplst
      781 vsehvgrpsk aekysrttsc pafstqgesh eetalqkgfp gttltypgpf seaesssadr
      841 gldesldaal
//
LOCUS       NP_001423660             277 aa            linear   ROD 23-MAR-2025
DEFINITION  F-actin-capping protein subunit beta isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423660 XP_006239239
VERSION     NP_001423660.1
DBSOURCE    REFSEQ: accession NM_001436731.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Kim,J., Kwon,J.T., Jeong,J., Kim,J., Hong,S.H., Kim,J., Park,Z.Y.,
            Chung,K.H., Eddy,E.M. and Cho,C.
  TITLE     SPATC1L maintains the integrity of the sperm head-tail junction
  JOURNAL   EMBO Rep 19 (9) (2018)
   PUBMED   30026308
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Lin,Y.H., Warren,C.M., Li,J., McKinsey,T.A. and Russell,B.
  TITLE     Myofibril growth during cardiac hypertrophy is regulated through
            dual phosphorylation and acetylation of the actin capping protein
            CapZ
  JOURNAL   Cell Signal 28 (8), 1015-1024 (2016)
   PUBMED   27185186
  REMARK    GeneRIF: The goal of this study was to test the hypothesis that
            actin filament assembly during cardiomyocyte growth is regulated by
            post-translational modifications (PTMs) of CapZbeta1.
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Lin,Y.H., Swanson,E.R., Li,J., Mkrtschjan,M.A. and Russell,B.
  TITLE     Cyclic mechanical strain of myocytes modifies CapZbeta1 post
            translationally via PKCepsilon
  JOURNAL   J Muscle Res Cell Motil 36 (4-5), 329-337 (2015)
   PUBMED   26429793
  REMARK    GeneRIF: with strain there was significant PKCepsilon translocation
            to the Z-disc and co-localization with CapZbeta1 or alpha-actinin,
            which was quantified on confocal images.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Mi,N., Chen,Y., Wang,S., Chen,M., Zhao,M., Yang,G., Ma,M., Su,Q.,
            Luo,S., Shi,J., Xu,J., Guo,Q., Gao,N., Sun,Y., Chen,Z. and Yu,L.
  TITLE     CapZ regulates autophagosomal membrane shaping by promoting actin
            assembly inside the isolation membrane
  JOURNAL   Nat Cell Biol 17 (9), 1112-1123 (2015)
   PUBMED   26237647
  REMARK    GeneRIF: Binding of CapZ to PtdIns(3)P, which is enriched in
            omegasomes, stimulates actin polymerization.
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Kitazawa,M., Yamakuni,T., Song,S.Y., Kato,C., Tsuchiya,R.,
            Ishida,M., Suzuki,N., Adachi,E., Iwashita,S., Ueno,S.,
            Yanagihara,N., Taoka,M., Isobe,T. and Ohizumi,Y.
  TITLE     Intracellular cAMP controls a physical association of V-1 with CapZ
            in cultured mammalian endocrine cells
  JOURNAL   Biochem Biophys Res Commun 331 (1), 181-186 (2005)
   PUBMED   15845376
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Pyle,W.G., Hart,M.C., Cooper,J.A., Sumandea,M.P., de Tombe,P.P. and
            Solaro,R.J.
  TITLE     Actin capping protein: an essential element in protein kinase
            signaling to the myofilaments
  JOURNAL   Circ Res 90 (12), 1299-1306 (2002)
   PUBMED   12089068
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Palmgren,S., Ojala,P.J., Wear,M.A., Cooper,J.A. and Lappalainen,P.
  TITLE     Interactions with PIP2, ADP-actin monomers, and capping protein
            regulate the activity and localization of yeast twinfilin
  JOURNAL   J Cell Biol 155 (2), 251-260 (2001)
   PUBMED   11604420
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Hart,M.C. and Cooper,J.A.
  TITLE     Vertebrate isoforms of actin capping protein beta have distinct
            functions In vivo
  JOURNAL   J Cell Biol 147 (6), 1287-1298 (1999)
   PUBMED   10601341
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006239239.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2784071.1,
                                           SRR22399481.1200869.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..277
                     /product="F-actin-capping protein subunit beta isoform 1"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     F-actin capping protein beta subunit; capping protein
                     (actin filament) muscle Z-line, beta; capping actin
                     protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=31214
     Region          11..239
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..277
                     /gene="Capzb"
                     /coded_by="NM_001436731.1:100..933"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298584"
                     /db_xref="RGD:1359099"
ORIGIN      
        1 msdqqldcal dlmrrlppqq ieknlsdlid lvpslcedll ssvdqplkia rdkvvgkdyl
       61 lcdynrdgds yrspwsnkyd ppledgamps arlrklevea nnafdqyrdl yfeggvssvy
      121 lwdldhgfag vilikkagdg skkikgcwds ihvvevqeks sgrtahyklt stvmlwlqtn
      181 ksgsgtmnlg gsltrqmekd etvsdcsphi anigrlvedm enkirstlne iyfgktkdiv
      241 nglrsldaip dnhkfkqlqr elsqvltqrq vyiqpdn
//
LOCUS       NP_665710                263 aa            linear   ROD 23-MAR-2025
DEFINITION  dorsal root ganglia homeobox protein [Rattus norvegicus].
ACCESSION   NP_665710
VERSION     NP_665710.2
DBSOURCE    REFSEQ: accession NM_145767.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Ito,T., Sakai,A., Maruyama,M., Miyagawa,Y., Okada,T., Fukayama,H.
            and Suzuki,H.
  TITLE     Dorsal Root Ganglia Homeobox downregulation in primary sensory
            neurons contributes to neuropathic pain in rats
  JOURNAL   Mol Pain 16, 1744806920904462 (2020)
   PUBMED   32000573
  REMARK    GeneRIF: Dorsal Root Ganglia Homeobox downregulation in primary
            sensory neurons contributes to neuropathic pain in rats.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Rebelo,S., Chen,Z.F., Anderson,D.J. and Lima,D.
  TITLE     Involvement of DRG11 in the development of the primary afferent
            nociceptive system
  JOURNAL   Mol Cell Neurosci 33 (3), 236-246 (2006)
   PUBMED   16978876
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Ding,Y.Q., Yin,J., Kania,A., Zhao,Z.Q., Johnson,R.L. and Chen,Z.F.
  TITLE     Lmx1b controls the differentiation and migration of the superficial
            dorsal horn neurons of the spinal cord
  JOURNAL   Development 131 (15), 3693-3703 (2004)
   PUBMED   15229182
  REMARK    Erratum:[Development. 2009 Jun;136(11):1961]
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Samad,T.A., Srinivasan,A., Karchewski,L.A., Jeong,S.J.,
            Campagna,J.A., Ji,R.R., Fabrizio,D.A., Zhang,Y., Lin,H.Y., Bell,E.
            and Woolf,C.J.
  TITLE     DRAGON: a member of the repulsive guidance molecule-related family
            of neuronal- and muscle-expressed membrane proteins is regulated by
            DRG11 and has neuronal adhesive properties
  JOURNAL   J Neurosci 24 (8), 2027-2036 (2004)
   PUBMED   14985445
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Ding,Y.Q., Yin,J., Xu,H.M., Jacquin,M.F. and Chen,Z.F.
  TITLE     Formation of whisker-related principal sensory nucleus-based
            lemniscal pathway requires a paired homeodomain transcription
            factor, Drg11
  JOURNAL   J Neurosci 23 (19), 7246-7254 (2003)
   PUBMED   12917357
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Chen,Z.F., Rebelo,S., White,F., Malmberg,A.B., Baba,H., Lima,D.,
            Woolf,C.J., Basbaum,A.I. and Anderson,D.J.
  TITLE     The paired homeodomain protein DRG11 is required for the projection
            of cutaneous sensory afferent fibers to the dorsal spinal cord
  JOURNAL   Neuron 31 (1), 59-73 (2001)
   PUBMED   11498051
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Saito,T., Greenwood,A., Sun,Q. and Anderson,D.J.
  TITLE     Identification by differential RT-PCR of a novel paired homeodomain
            protein specifically expressed in sensory neurons and a subset of
            their CNS targets
  JOURNAL   Mol Cell Neurosci 6 (3), 280-292 (1995)
   PUBMED   7496632
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Nov 27, 2020 this sequence version replaced NP_665710.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U29174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN17050747, SAMN17050756
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..263
                     /product="dorsal root ganglia homeobox protein"
                     /note="homeobox protein DRG11; dorsal root ganglion 11;
                     paired-related homeobox protein-like 1; paired-like
                     homeodomain trancription factor Drg11"
                     /calculated_mol_wt=28520
     Region          34..90
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          88..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     Region          201..218
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          204..217
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     Region          219..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     CDS             1..263
                     /gene="Drgx"
                     /gene_synonym="Drg11; Prrxl1"
                     /coded_by="NM_145767.2:279..1070"
                     /db_xref="GeneID:252880"
                     /db_xref="RGD:628616"
ORIGIN      
        1 mfyfhcppql egtapfgnhs tgdfddgflr rkqrrnrttf tlqqlealea vfaqthypdv
       61 ftreelamki nltearvqvw fqnrrakwrk tergasdqep gakepmaevt pppvrninsp
      121 ppgdqargkk ealeaqqslg rtvgpagpff psclpgtlln tatyaqalsh vaslkggplc
      181 sccvpdpmgl sflptygcqs nrtasvaalr mkarehseav lqsanllpst ssspgpaskq
      241 vppegsqdkp sptkeqsege ksv
//
LOCUS       NP_001423673             263 aa            linear   ROD 23-MAR-2025
DEFINITION  dorsal root ganglia homeobox protein [Rattus norvegicus].
ACCESSION   NP_001423673 XP_063131133
VERSION     NP_001423673.1
DBSOURCE    REFSEQ: accession NM_001436744.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Ito,T., Sakai,A., Maruyama,M., Miyagawa,Y., Okada,T., Fukayama,H.
            and Suzuki,H.
  TITLE     Dorsal Root Ganglia Homeobox downregulation in primary sensory
            neurons contributes to neuropathic pain in rats
  JOURNAL   Mol Pain 16, 1744806920904462 (2020)
   PUBMED   32000573
  REMARK    GeneRIF: Dorsal Root Ganglia Homeobox downregulation in primary
            sensory neurons contributes to neuropathic pain in rats.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Rebelo,S., Chen,Z.F., Anderson,D.J. and Lima,D.
  TITLE     Involvement of DRG11 in the development of the primary afferent
            nociceptive system
  JOURNAL   Mol Cell Neurosci 33 (3), 236-246 (2006)
   PUBMED   16978876
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Ding,Y.Q., Yin,J., Kania,A., Zhao,Z.Q., Johnson,R.L. and Chen,Z.F.
  TITLE     Lmx1b controls the differentiation and migration of the superficial
            dorsal horn neurons of the spinal cord
  JOURNAL   Development 131 (15), 3693-3703 (2004)
   PUBMED   15229182
  REMARK    Erratum:[Development. 2009 Jun;136(11):1961]
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Samad,T.A., Srinivasan,A., Karchewski,L.A., Jeong,S.J.,
            Campagna,J.A., Ji,R.R., Fabrizio,D.A., Zhang,Y., Lin,H.Y., Bell,E.
            and Woolf,C.J.
  TITLE     DRAGON: a member of the repulsive guidance molecule-related family
            of neuronal- and muscle-expressed membrane proteins is regulated by
            DRG11 and has neuronal adhesive properties
  JOURNAL   J Neurosci 24 (8), 2027-2036 (2004)
   PUBMED   14985445
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Ding,Y.Q., Yin,J., Xu,H.M., Jacquin,M.F. and Chen,Z.F.
  TITLE     Formation of whisker-related principal sensory nucleus-based
            lemniscal pathway requires a paired homeodomain transcription
            factor, Drg11
  JOURNAL   J Neurosci 23 (19), 7246-7254 (2003)
   PUBMED   12917357
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Chen,Z.F., Rebelo,S., White,F., Malmberg,A.B., Baba,H., Lima,D.,
            Woolf,C.J., Basbaum,A.I. and Anderson,D.J.
  TITLE     The paired homeodomain protein DRG11 is required for the projection
            of cutaneous sensory afferent fibers to the dorsal spinal cord
  JOURNAL   Neuron 31 (1), 59-73 (2001)
   PUBMED   11498051
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Saito,T., Greenwood,A., Sun,Q. and Anderson,D.J.
  TITLE     Identification by differential RT-PCR of a novel paired homeodomain
            protein specifically expressed in sensory neurons and a subset of
            their CNS targets
  JOURNAL   Mol Cell Neurosci 6 (3), 280-292 (1995)
   PUBMED   7496632
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_063131133.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN17050747,
                              SAMN17050755 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression, longest
                                         protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..263
                     /product="dorsal root ganglia homeobox protein"
                     /note="homeobox protein DRG11; dorsal root ganglion 11;
                     paired-related homeobox protein-like 1; paired-like
                     homeodomain trancription factor Drg11"
                     /calculated_mol_wt=28520
     Region          34..90
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          88..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     Region          201..218
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          204..217
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     Region          219..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62798.1)"
     CDS             1..263
                     /gene="Drgx"
                     /gene_synonym="Drg11; Prrxl1"
                     /coded_by="NM_001436744.1:241..1032"
                     /db_xref="GeneID:252880"
                     /db_xref="RGD:628616"
ORIGIN      
        1 mfyfhcppql egtapfgnhs tgdfddgflr rkqrrnrttf tlqqlealea vfaqthypdv
       61 ftreelamki nltearvqvw fqnrrakwrk tergasdqep gakepmaevt pppvrninsp
      121 ppgdqargkk ealeaqqslg rtvgpagpff psclpgtlln tatyaqalsh vaslkggplc
      181 sccvpdpmgl sflptygcqs nrtasvaalr mkarehseav lqsanllpst ssspgpaskq
      241 vppegsqdkp sptkeqsege ksv
//
LOCUS       NP_001423606             342 aa            linear   ROD 23-MAR-2025
DEFINITION  transmembrane protein 268 [Rattus norvegicus].
ACCESSION   NP_001423606 XP_063143423
VERSION     NP_001423606.1
DBSOURCE    REFSEQ: accession NM_001436677.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 19, 2025 this sequence version replaced XP_063143423.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.21924.1,
                                           SRR26360190.76421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..342
                     /product="transmembrane protein 268"
                     /note="transmembrane protein C9orf91 homolog"
                     /calculated_mol_wt=37799
     Region          39..328
                     /region_name="DUF4481"
                     /note="Domain of unknown function (DUF4481); pfam14800"
                     /db_xref="CDD:464322"
     CDS             1..342
                     /gene="Tmem268"
                     /gene_synonym="RGD1304595"
                     /coded_by="NM_001436677.1:2317..3345"
                     /db_xref="GeneID:298104"
                     /db_xref="RGD:1304595"
ORIGIN      
        1 maceppsdpg gaagplptst lgcstlpqgn ppgwgeelhn gqvlsvlrid ntcapisfdl
       61 rvaeeqlqaw giqvpaeqyr slaesallep qvrryiiyns rpmrlafavv fyvlvwaniy
      121 stsqmfalgn qwagvllatl aavsltltlv lvferqqrka ntntdlrlva angallrhrv
      181 llgvtdtveg cqsviqlwfv yfdlencvqf lsdhvqemkr sqesllrsrl sqlcvvmetg
      241 vspvverped ledspllprt pgpqerpltq telyqlvpea epeemarqll avfggyytrl
      301 lvtsqlpqpm gtrhmdsari pcpcqlievh ilgtgccpfl ar
//
LOCUS       NP_001423693             606 aa            linear   ROD 24-MAR-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423693 XP_063143661
VERSION     NP_001423693.1
DBSOURCE    REFSEQ: accession NM_001436764.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Loh,K.H., Stawski,P.S., Draycott,A.S., Udeshi,N.D., Lehrman,E.K.,
            Wilton,D.K., Svinkina,T., Deerinck,T.J., Ellisman,M.H., Stevens,B.,
            Carr,S.A. and Ting,A.Y.
  TITLE     Proteomic Analysis of Unbounded Cellular Compartments: Synaptic
            Clefts
  JOURNAL   Cell 166 (5), 1295-1307 (2016)
   PUBMED   27565350
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063143661.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840105
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21-q22"
     Protein         1..606
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2
                     precursor"
                     /note="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2"
                     /calculated_mol_wt=65220
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2949
     Region          27..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          39..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          48..>340
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          59..82
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          131..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          155..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          203..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          251..274
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          275..298
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          299..322
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          323..343
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          327..>391
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          411..500
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          428..432
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          441..445
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..485
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          493..496
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..606
                     /gene="Lingo2"
                     /gene_synonym="RGD1310773"
                     /coded_by="NM_001436764.1:1187..3007"
                     /db_xref="GeneID:313156"
                     /db_xref="RGD:1310773"
ORIGIN      
        1 mlhtaipcwq pflglamvll fmgstigcpa rcecsaqnks vschrrrlia ipegipietk
       61 ildlsknrlk sinpeefisy plleeidlsd niianvepga fnnlfnlrsl rlkgnrlklv
      121 plgvftglsn ltkldisenk ivilldymfq dlhnlkslev gdndlvyish rafsglfsle
      181 qltlekcnlt avptealshl rslitlhlkh lninnmpvya fkrlfhlkql eidywplldm
      241 mpanslygln ltslsitntn lstvpflafk hlvylthlnl synpistiea gmfsdlirlq
      301 elhvvgaqlr tiephsfqgl rflrvlnvsq nlletleenv fsspralevl sinnnplacd
      361 crllwllqrq atlqfggqqp mcagpdtire rsfkdfhsta lsfyftckkp kirekklqhl
      421 lvdegqtvql ecnadgdpqp viswvtprrr fittksngra tvlgdgtlei rfaqdqdsgm
      481 yvciasnaag ndtftasltv kgftsdrfly anrtpmymtd sndtvsngtn antfsldlkt
      541 ilvstamgcf tflgvvlfcf lllfvwsrgk gkhknsidle yvprknngav aegevagprr
      601 fnmkmi
//
LOCUS       NP_001423755             262 aa            linear   ROD 24-MAR-2025
DEFINITION  R-spondin-1 precursor [Rattus norvegicus].
ACCESSION   NP_001423755 XP_008762241
VERSION     NP_001423755.1
DBSOURCE    REFSEQ: accession NM_001436826.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Li,J.Y., Wu,X., Lee,A., Zhou,S.Y. and Owyang,C.
  TITLE     Altered R-spondin 1/CART neurocircuit in the hypothalamus
            contributes to hyperphagia in diabetes
  JOURNAL   J Neurophysiol 121 (3), 928-939 (2019)
   PUBMED   30649980
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Szenker-Ravi,E., Altunoglu,U., Leushacke,M., Bosso-Lefevre,C.,
            Khatoo,M., Thi Tran,H., Naert,T., Noelanders,R., Hajamohideen,A.,
            Beneteau,C., de Sousa,S.B., Karaman,B., Latypova,X., Basaran,S.,
            Yucel,E.B., Tan,T.T., Vlaminck,L., Nayak,S.S., Shukla,A.,
            Girisha,K.M., Le Caignec,C., Soshnikova,N., Uyguner,Z.O.,
            Vleminckx,K., Barker,N., Kayserili,H. and Reversade,B.
  TITLE     RSPO2 inhibition of RNF43 and ZNRF3 governs limb development
            independently of LGR4/5/6
  JOURNAL   Nature 557 (7706), 564-569 (2018)
   PUBMED   29769720
  REMARK    Erratum:[Nature. 2018 Sep;561(7722):E7. doi:
            10.1038/s41586-018-0296-7. PMID: 29977062]
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Li,J.Y., Chai,B., Zhang,W., Fritze,D.M., Zhang,C. and
            Mulholland,M.W.
  TITLE     LGR4 and its ligands, R-spondin 1 and R-spondin 3, regulate food
            intake in the hypothalamus of male rats
  JOURNAL   Endocrinology 155 (2), 429-440 (2014)
   PUBMED   24280058
  REMARK    GeneRIF: These data indicate that Rspo1 and Rspo3 and their
            receptor LGR4 form novel circuits in the brain to regulate energy
            homeostasis.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Niehrs,C.
  TITLE     The complex world of WNT receptor signalling
  JOURNAL   Nat Rev Mol Cell Biol 13 (12), 767-779 (2012)
   PUBMED   23151663
  REMARK    Review article
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Ruffner,H., Sprunger,J., Charlat,O., Leighton-Davies,J.,
            Grosshans,B., Salathe,A., Zietzling,S., Beck,V., Therier,M.,
            Isken,A., Xie,Y., Zhang,Y., Hao,H., Shi,X., Liu,D., Song,Q.,
            Clay,I., Hintzen,G., Tchorz,J., Bouchez,L.C., Michaud,G., Finan,P.,
            Myer,V.E., Bouwmeester,T., Porter,J., Hild,M., Bassilana,F.,
            Parker,C.N. and Cong,F.
  TITLE     R-Spondin potentiates Wnt/beta-catenin signaling through orphan
            receptors LGR4 and LGR5
  JOURNAL   PLoS One 7 (7), e40976 (2012)
   PUBMED   22815884
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Carmon,K.S., Gong,X., Lin,Q., Thomas,A. and Liu,Q.
  TITLE     R-spondins function as ligands of the orphan receptors LGR4 and
            LGR5 to regulate Wnt/beta-catenin signaling
  JOURNAL   Proc Natl Acad Sci U S A 108 (28), 11452-11457 (2011)
   PUBMED   21693646
REFERENCE   7  (residues 1 to 262)
  AUTHORS   de Lau,W., Barker,N., Low,T.Y., Koo,B.K., Li,V.S., Teunissen,H.,
            Kujala,P., Haegebarth,A., Peters,P.J., van de Wetering,M.,
            Stange,D.E., van Es,J.E., Guardavaccaro,D., Schasfoort,R.B.,
            Mohri,Y., Nishimori,K., Mohammed,S., Heck,A.J. and Clevers,H.
  TITLE     Lgr5 homologues associate with Wnt receptors and mediate R-spondin
            signalling
  JOURNAL   Nature 476 (7360), 293-297 (2011)
   PUBMED   21727895
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Binnerts,M.E., Kim,K.A., Bright,J.M., Patel,S.M., Tran,K., Zhou,M.,
            Leung,J.M., Liu,Y., Lomas,W.E. 3rd, Dixon,M., Hazell,S.A.,
            Wagle,M., Nie,W.S., Tomasevic,N., Williams,J., Zhan,X., Levy,M.D.,
            Funk,W.D. and Abo,A.
  TITLE     R-Spondin1 regulates Wnt signaling by inhibiting internalization of
            LRP6
  JOURNAL   Proc Natl Acad Sci U S A 104 (37), 14700-14705 (2007)
   PUBMED   17804805
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Nam,J.S., Turcotte,T.J., Smith,P.F., Choi,S. and Yoon,J.K.
  TITLE     Mouse cristin/R-spondin family proteins are novel ligands for the
            Frizzled 8 and LRP6 receptors and activate beta-catenin-dependent
            gene expression
  JOURNAL   J Biol Chem 281 (19), 13247-13257 (2006)
   PUBMED   16543246
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Kamata,T., Katsube,K., Michikawa,M., Yamada,M., Takada,S. and
            Mizusawa,H.
  TITLE     R-spondin, a novel gene with thrombospondin type 1 domain, was
            expressed in the dorsal neural tube and affected in Wnts mutants
  JOURNAL   Biochim Biophys Acta 1676 (1), 51-62 (2004)
   PUBMED   14732490
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_008762241.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168963.1, SRR26643290.20365.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..262
                     /product="R-spondin-1 precursor"
                     /calculated_mol_wt=26749
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2139
     Region          42..142
                     /region_name="Furin-like_2"
                     /note="Furin-like repeat, cysteine-rich; pfam15913"
                     /db_xref="CDD:464939"
     Region          148..203
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     CDS             1..262
                     /gene="Rspo1"
                     /gene_synonym="RGD1565558"
                     /coded_by="NM_001436826.1:440..1228"
                     /db_xref="GeneID:313589"
                     /db_xref="RGD:1565558"
ORIGIN      
        1 mrlglcvval vlswthlavg srgikgkrqr risaegsqsc akgcelcsev ngclkcspkl
       61 fillerndir qvgvclpscp pgyfdarnpd mnkcikckie hceacfshnf ctkcqeglyl
      121 hkgrcypacp egstaanstm ecgspaqcem sewspwgpcs kkrklcgfrk gseertrrvl
      181 hapggdqtnc sdtketrkct vrrtpcpegq krkkasqgrr enanrhptrk nskepgsnsr
      241 rhkgqqqpqp gtagpltsvg pt
//
LOCUS       NP_001423737            1062 aa            linear   ROD 24-MAR-2025
DEFINITION  lysine-specific demethylase 4A isoform a [Rattus norvegicus].
ACCESSION   NP_001423737 XP_017448880
VERSION     NP_001423737.1
DBSOURCE    REFSEQ: accession NM_001436808.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Li,L., Ding,Z., Ma,F., Zhang,K., Lu,D., Wang,H. and Yang,K.
  TITLE     Spinal nerve transection-induced upregulation of KDM4A in the
            dorsal root ganglia contributes to the development and maintenance
            of neuropathic pain via promoting CCL2 expression in rats
  JOURNAL   Eur J Neurosci 60 (6), 5169-5188 (2024)
   PUBMED   39136140
  REMARK    GeneRIF: Spinal nerve transection-induced upregulation of KDM4A in
            the dorsal root ganglia contributes to the development and
            maintenance of neuropathic pain via promoting CCL2 expression in
            rats.
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Li,W., Zhang,Y., Lv,J., Zhang,Y., Bai,J., Zhen,L. and He,X.
  TITLE     MicroRNA-137-mediated lysine demethylase 4A regulates the recovery
            of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis
  JOURNAL   Int J Neurosci 133 (1), 37-50 (2023)
   PUBMED   33499717
  REMARK    GeneRIF: MicroRNA-137-mediated lysine demethylase 4A regulates the
            recovery of spinal cord injury via the SFRP4-Wnt/beta-Catenin axis.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Liu,Y., Zhao,L., Zhang,J., Lv,L., Han,K., Huang,C. and Xu,Z.
  TITLE     Histone Demethylase KDM4A Inhibition Represses Neuroinflammation
            and Improves Functional Recovery in Ischemic Stroke
  JOURNAL   Curr Pharm Des 27 (21), 2528-2536 (2021)
   PUBMED   33402077
  REMARK    GeneRIF: Histone Demethylase KDM4A Inhibition Represses
            Neuroinflammation and Improves Functional Recovery in Ischemic
            Stroke.
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Qin,G., Li,Y., Wang,H., Yang,J., Chen,Q., Tang,H., Wang,Y.,
            Zhang,M., Jiang,T., Lin,S. and Huo,S.
  TITLE     Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation
            via Regulating the Binding Ability of H3K9me3 with the Promoters of
            Runx2, Osterix and Osteocalcin
  JOURNAL   J Biomed Nanotechnol 16 (6), 899-909 (2020)
   PUBMED   33187585
  REMARK    GeneRIF: Lysine-Specific Demethylase 4A Regulates Osteogenic
            Differentiation via Regulating the Binding Ability of H3K9me3 with
            the Promoters of Runx2, Osterix and Osteocalcin.
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Johansson,C., Velupillai,S., Tumber,A., Szykowska,A., Hookway,E.S.,
            Nowak,R.P., Strain-Damerell,C., Gileadi,C., Philpott,M.,
            Burgess-Brown,N., Wu,N., Kopec,J., Nuzzi,A., Steuber,H., Egner,U.,
            Badock,V., Munro,S., LaThangue,N.B., Westaway,S., Brown,J.,
            Athanasou,N., Prinjha,R., Brennan,P.E. and Oppermann,U.
  TITLE     Structural analysis of human KDM5B guides histone demethylase
            inhibitor development
  JOURNAL   Nat Chem Biol 12 (7), 539-545 (2016)
   PUBMED   27214403
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Sohi,G., Marchand,K., Revesz,A., Arany,E. and Hardy,D.B.
  TITLE     Maternal protein restriction elevates cholesterol in adult rat
            offspring due to repressive changes in histone modifications at the
            cholesterol 7alpha-hydroxylase promoter
  JOURNAL   Mol Endocrinol 25 (5), 785-798 (2011)
   PUBMED   21372147
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Trojer,P., Zhang,J., Yonezawa,M., Schmidt,A., Zheng,H., Jenuwein,T.
            and Reinberg,D.
  TITLE     Dynamic Histone H1 Isotype 4 Methylation and Demethylation by
            Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji
            Domain-containing JMJD2/KDM4 Proteins
  JOURNAL   J Biol Chem 284 (13), 8395-8405 (2009)
   PUBMED   19144645
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Fodor,B.D., Kubicek,S., Yonezawa,M., O'Sullivan,R.J., Sengupta,R.,
            Perez-Burgos,L., Opravil,S., Mechtler,K., Schotta,G. and
            Jenuwein,T.
  TITLE     Jmjd2b antagonizes H3K9 trimethylation at pericentric
            heterochromatin in mammalian cells
  JOURNAL   Genes Dev 20 (12), 1557-1562 (2006)
   PUBMED   16738407
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Gray,S.G., Iglesias,A.H., Lizcano,F., Villanueva,R., Camelo,S.,
            Jingu,H., Teh,B.T., Koibuchi,N., Chin,W.W., Kokkotou,E. and
            Dangond,F.
  TITLE     Functional characterization of JMJD2A, a histone deacetylase- and
            retinoblastoma-binding protein
  JOURNAL   J Biol Chem 280 (31), 28507-28518 (2005)
   PUBMED   15927959
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Zhang,D., Yoon,H.G. and Wong,J.
  TITLE     JMJD2A is a novel N-CoR-interacting protein and is involved in
            repression of the human transcription factor achaete scute-like
            homologue 2 (ASCL2/Hash2)
  JOURNAL   Mol Cell Biol 25 (15), 6404-6414 (2005)
   PUBMED   16024779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017448880.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20536.1,
                                           SRR26643298.28609.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1062
                     /product="lysine-specific demethylase 4A isoform a"
                     /EC_number="1.14.11.-"
                     /note="lysine-specific demethylase 4A; jumonji domain
                     containing 2A; lysine (K)-specific demethylase 4A"
                     /calculated_mol_wt=120270
     Region          13..55
                     /region_name="JmjN"
                     /note="Small domain found in the jumonji family of
                     transcription factors; smart00545"
                     /db_xref="CDD:128818"
     Region          175..291
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          665..764
                     /region_name="PHD_JMJD2A"
                     /note="PHD finger found in Jumonji domain-containing
                     protein 2A (JMJD2A); cd15575"
                     /db_xref="CDD:277050"
     Site            order(665,732..736,740,759)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277050"
     Region          773..882
                     /region_name="ePHD_JMJD2A"
                     /note="Extended PHD finger (ePHD) found in Jumonji
                     domain-containing protein 2A (JMJD2A); cd15713"
                     /db_xref="CDD:277183"
     Site            order(827,841..845,851,877)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277183"
     Region          897..951
                     /region_name="Tudor_JMJD2A_rpt1"
                     /note="first Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20463"
                     /db_xref="CDD:410534"
     Site            order(929..930,932..935,937)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410534"
     Region          954..1009
                     /region_name="Tudor_JMJD2A_rpt2"
                     /note="second Tudor domain found in Jumonji
                     domain-containing protein 2A (JMJD2A) and similar
                     proteins; cd20466"
                     /db_xref="CDD:410537"
     Site            order(965..967,971)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410537"
     CDS             1..1062
                     /gene="Kdm4a"
                     /gene_synonym="Jmjd2a"
                     /coded_by="NM_001436808.1:137..3325"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313539"
                     /db_xref="RGD:1306378"
ORIGIN      
        1 masesetlnp sarimtfypt meefrnfsry iayiesqgah raglakvvpp kewkprtsyd
       61 diddlvipap iqqlvtgqsg lftqyniqkk amtvrefrki ansdkyctpr ysefeelerk
      121 ywknltfnpp iygadvngtl yeqhvdewni grlktildlv ekesgitieg vntpylyfgm
      181 wktsfawhte dmdlysinyl hfgepkswys vppehgkrle rlakgffpgs aqsceaflrh
      241 kmtlisplml kkygipfdkv tqeagefmit fpygyhagfn hgfncaestn fatrrwieyg
      301 kqavlcscrk dmvkismdvf vrrfqperyk lwkagkdstv idhtlptpea aeflkdsglt
      361 pragneecpe edseaaeqge egdvkrslak hrigtkrhrv cleipqevsq selfpkeels
      421 sgqyemtecq atlapvrpth ssvrqvedsl pfpdysdpte vkfeelknvk leeededeep
      481 eaaaldlsvn pesvegrlvf sgskkkasss lgssssqdsv ssdsettesv scqgqektvl
      541 tvhsysrgdg kaapgepsvk rqrsaprsis eqelaevade ymlsleenkk tkgrrqplsk
      601 lprhhplvlq ecgsddetse qltpeeeaee teawakplsq lwqnrppnfe aekefnelma
      661 qqaphcavcm ifqtyhqvef ggfsqscgna sepaaqpqrt kplipemcft ttgcstdinl
      721 stpyleedgt smlvsckkcs vrvhascygv ppakaseewm csrcsanale edcclcslrg
      781 galqranddr wvhvscavai learfvniae rspvdvskip lprfklkcvf ckkrrkrnag
      841 ccvqcshgrc ptafhvscaq aagvmmqpdd wpfvvfitcf rhkipnlera kgallsitag
      901 qkviskhkng rfyqcevvrl ttetfyevnf ddgsfsdnly pedivsqdcl qlgppaegev
      961 vqvrwtdgqv ygakfvashp iqmyqvefed gsqlvvkrdd vytldeelpk rvksrlsvas
     1021 dmrfneifte kevkqekkrq rvinsryred yiepalyrai me
//
LOCUS       NP_001108495             480 aa            linear   ROD 24-MAR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX49 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001108495
VERSION     NP_001108495.2
DBSOURCE    REFSEQ: accession NM_001115023.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Awasthi,S., Verma,M., Mahesh,A., K Khan,M.I., Govindaraju,G.,
            Rajavelu,A., Chavali,P.L., Chavali,S. and Dhayalan,A.
  TITLE     DDX49 is an RNA helicase that affects translation by regulating
            mRNA export and the levels of pre-ribosomal RNA
  JOURNAL   Nucleic Acids Res 46 (12), 6304-6317 (2018)
   PUBMED   29618122
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced NP_001108495.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158855.1, SRR26643298.71041.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..480
                     /product="probable ATP-dependent RNA helicase DDX49
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase DDX49; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 49"
                     /calculated_mol_wt=54114
     Region          1..380
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          <359..>460
                     /region_name="Spc7"
                     /note="Spc7 kinetochore protein; smart00787"
                     /db_xref="CDD:197874"
     CDS             1..480
                     /gene="Ddx49"
                     /coded_by="NM_001115023.2:31..1473"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290660"
                     /db_xref="RGD:1311124"
ORIGIN      
        1 magfaelrls swlveqcrql glkqptpvql gcipailegr dclgcaktgs gktaafvlpi
       61 lqklsedpyg ifclvltptr elayqiaeqf rvlgkplglk dciivggmdm vtqalelsrk
      121 phvviatpgr ladhlrssnt fnmkkirflv ldeadrlleq gctdftadle tilsavparr
      181 qtllfsatlt dtlkelqgla tnqpffweaq atvrtveqld qryllvpekv kdaylvhlvq
      241 tfqdqledcs iiiftntckt cqilcmmlrk fnfptvalhs mmkqkerfaa larfksstyr
      301 iliatdvasr gldiptvqvv inhntpglpk iyihrvgrta ragrqgqait lvtqydihll
      361 haieeeikqq laelaveeaq vlqiltqvnv vrreceikle ashfdekkei nkrkqmileg
      421 kdpdleakrk aelakikqqn rrfkekveqt lrqqkagstg rrsrpprprp qeparaeaqn
//
LOCUS       NP_001178541             418 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger protein 362 isoform a [Rattus norvegicus].
ACCESSION   NP_001178541 XP_006238984 XP_216345
VERSION     NP_001178541.1
DBSOURCE    REFSEQ: accession NM_001191612.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 18, 2025 this sequence version replaced
            XP_006238984.1, XP_216345.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.20499.1,
                                           SRR26643429.20918.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..418
                     /product="zinc finger protein 362 isoform a"
                     /calculated_mol_wt=45541
     Region          <27..>131
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          227..247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          239..264
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          253..275
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(260,262,264,266..267,270..271,274,288,290,294..295,
                     298..299,302,318,320,322,324..325,328..329,332)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          267..292
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <305..357
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          311..333
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..418
                     /gene="Zfp362"
                     /gene_synonym="RGD1306498"
                     /coded_by="NM_001191612.2:403..1659"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:297879"
                     /db_xref="RGD:1306498"
ORIGIN      
        1 msrsspsgkg psrmaeprfn npyfwppppt mpsqldnlvl inkikeqlma ekirpphlpp
       61 tsassqqpll vppapaessq avmslpklqq vpglhpqsvp qpdvalharp atstvtglgl
      121 ssrtpavsts estpgtgtgt stpstpttts qsrliasspt lisgitsppl ldsiktiqgh
      181 gllgppkser grkkikaenp ggppvlvvpy pilasgetak egktyrckvc pltfftksem
      241 qihskshtea kphkcphcsk sfanasylaq hlrihlgvkp yhcsycdksf rqlshlqqht
      301 rihtgdrpyk cphpgcekaf tqlsnlqshq rqhnkdkpyk cpncyraysd saslqihlsa
      361 haikhakayc csmcgrayts etylmkhmsk htvvehlvsh hspqrtespg ipvrisli
//
LOCUS       NP_001423723             259 aa            linear   ROD 24-MAR-2025
DEFINITION  DNA-binding protein RFXANK isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423723 XP_006252962
VERSION     NP_001423723.1
DBSOURCE    REFSEQ: accession NM_001436794.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   McKinsey,T.A., Kuwahara,K., Bezprozvannaya,S. and Olson,E.N.
  TITLE     Class II histone deacetylases confer signal responsiveness to the
            ankyrin-repeat proteins ANKRA2 and RFXANK
  JOURNAL   Mol Biol Cell 17 (1), 438-447 (2006)
   PUBMED   16236793
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Louise-Plence,P.,
            Prochnicka-Chalufour,A., Selz,F., Picard,C., Le Deist,F.,
            Eliaou,J.F., Fischer,A. and Lisowska-Grospierre,B.
  TITLE     Novel mutations in the RFXANK gene: RFX complex containing
            in-vitro-generated RFXANK mutant binds the promoter without
            transactivating MHC II
  JOURNAL   Immunogenetics 54 (11), 747-755 (2003)
   PUBMED   12618906
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006252962.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ231410.1, SRR26643296.35371.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..259
                     /product="DNA-binding protein RFXANK isoform 1"
                     /note="DNA-binding protein RFXANK"
                     /calculated_mol_wt=28101
     Region          <93..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          93..120
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(122,124,128..129,132..134,136..137,141,144,153,155,
                     157,161..162,165..167,169..170,174,177,186,188,190,
                     194..195,198..200,202..203,207,210)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          122..153
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          155..186
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          188..216
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..259
                     /gene="Rfxank"
                     /coded_by="NM_001436794.1:214..993"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306353"
                     /db_xref="RGD:1311390"
ORIGIN      
        1 meptqvaenl ipnqqslapd ledpedrrde spdssdtvvl slfpctpdav npeadasass
       61 lqgsflkhst tltnrqrgne vsalpatlds lsihqlaaqg elsqlkdhlr kgdnlvnkpd
      121 ergftpliwa safgeietvr flldwgadph ilakeresal slasmggytd ivrllldrdv
      181 diniydwngg tpllyavrgn hvkcvealla rgadlttead sgytpmdlav algyrkvqqv
      241 meshilklfq gtlgpadpe
//
LOCUS       NP_001101384            1560 aa            linear   ROD 24-MAR-2025
DEFINITION  adhesion G protein-coupled receptor B2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001101384 XP_001062170 XP_001062231 XP_001062290 XP_006238996
            XP_232778
VERSION     NP_001101384.1
DBSOURCE    REFSEQ: accession NM_001107914.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1560)
  AUTHORS   Purcell,R.H., Toro,C., Gahl,W.A. and Hall,R.A.
  TITLE     A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2)
            increases receptor signaling activity
  JOURNAL   Hum Mutat 38 (12), 1751-1760 (2017)
   PUBMED   28891236
REFERENCE   2  (residues 1 to 1560)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   3  (residues 1 to 1560)
  AUTHORS   Kee,H.J., Koh,J.T., Kim,M.Y., Ahn,K.Y., Kim,J.K., Bae,C.S.,
            Park,S.S. and Kim,K.K.
  TITLE     Expression of brain-specific angiogenesis inhibitor 2 (BAI2) in
            normal and ischemic brain: involvement of BAI2 in the
            ischemia-induced brain angiogenesis
  JOURNAL   J Cereb Blood Flow Metab 22 (9), 1054-1067 (2002)
   PUBMED   12218411
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 20, 2025 this sequence version replaced
            XP_006238996.1, XP_001062290.1, XP_001062231.1, XP_232778.4,
            XP_001062170.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1560
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1560
                     /product="adhesion G protein-coupled receptor B2
                     precursor"
                     /note="brain-specific angiogenesis inhibitor 2"
                     /calculated_mol_wt=167586
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2084
     Region          26..220
                     /region_name="AGRB_N"
                     /note="Adhesion GPCR B N-terminal region; pfam19188"
                     /db_xref="CDD:465991"
     Region          304..352
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          357..407
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          412..462
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          468..518
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          521..585
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Region          604..>759
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Region          863..916
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          922..1212
                     /region_name="7tmB2_BAI2"
                     /note="brain-specific angiogenesis inhibitor 2, a group
                     VII adhesion GPCR, member of the class B2 family of
                     seven-transmembrane G protein-coupled receptors; cd15988"
                     /db_xref="CDD:320654"
     Region          924..949
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320654"
     Site            order(929,933,976,979..980,983,990,997,1069..1070,1072,
                     1074,1161,1164,1177,1181)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320654"
     Region          959..981
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320654"
     Region          990..1018
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320654"
     Region          1028..1048
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320654"
     Region          1066..1095
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320654"
     Region          1142..1169
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320654"
     Region          1174..1199
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320654"
     CDS             1..1560
                     /gene="Adgrb2"
                     /gene_synonym="Bai2"
                     /coded_by="NM_001107914.2:454..5136"
                     /db_xref="GeneID:313058"
                     /db_xref="RGD:1309431"
ORIGIN      
        1 mtpacpllls vilslrlata fdpapsacsa lasgvlygaf slqdlfptia sgcswtlenp
       61 dptkyslylr fnrqeqvcth faprllpldh ylvnftclrp gpeeatarae sevgrpeeea
      121 eaeaaatgle lcggsgpftf lhfdknfvql clsaepseap rllapaalaf rfvevllinn
      181 nnssqftcgv lcrwseecgr aagracgfaq pgcscpgeag aspatttppg ppaahtlsna
      241 lvpggpappa eadlhsgssn dlfttemryg eepeeepkvk tqwprsadep glymaqtgdp
      301 aaeewspwsv csltcgqglq vrtrscvssp ygtlcsgplr etrpcnnsat cpvhgvweew
      361 gswslcsrsc grgsrsrmrt cvppqhggka cegpelqtkl csmaacpveg qwlewgpwgp
      421 cssscangtq qrsrkcsvag pawatcagal tdtrecsnfd cpatdgkwgp wnawslcskt
      481 cdtgwqrrfr mcqasgtqgy pcegtgeevk pcsekrcpaf hemcrdeyvm lmtwkraaag
      541 eiiynkcppn asgsasrrcl lsaqgvaywg lpsfarcish eyrylylslr ehlakgqrml
      601 agegmsqvvr slqellarrt yysgdllfsv dilrnvtdtf kratyvpsad dvqrffqvvs
      661 fmvdsenkdk wddaqqvspg svhllrvved fihlvgdalk afqsslivtd nlvisiqrep
      721 isavssditf pmrgrrgmkd wvrhsedrlf lpkevlslss pgkpatpgaa tagspgrgrg
      781 pgtvppgpgp ahqrllpadp eesssyfvig avlyrtlgli lppprpplav tsrvmtvtvr
      841 pptqppaepl itvelsyiin gttdphcasw dysradaslg dwntescqtl etqaahtrcq
      901 cqhlstfavl aqppkdltle lagapsvplv igcavscmal ltllaiyaaf wrfiksersi
      961 illnfclsil asnililvgq srvlskgvct mtaaflhfff lssfcwvlte awqsylavig
     1021 rmrtrlvrkr flclgwglpa lvvavsvgft rtkgygtssy cwlsleggll yafvgpaavi
     1081 vlvnmligii vfnklmardg vsdkskkqra gsercpwasl llpcsacgav pspllssasa
     1141 rnamaslwss cvvlpllalt wmsavlamtd rrsvlfqalf avfnsaqgfv itavhcflrr
     1201 evqdvvkcqm gvcrtdesed spdsckngql qilsdfekdv dlacqtvlfk evntcnpsti
     1261 tgtlsrlsld edeepksclv gpegglsfsp lpgnilvpma aspglgeppp pqetnpvymc
     1321 gegglrqldl twlrpsepgs egdymvlprr tlslqpgggg tggeeaprar pegtprraak
     1381 tvahtegyps flsvehsglg lgpaygslqn pygmtfqppp ptpsarqvpe pgersrtmpr
     1441 tvpgstmklg slerkklrys dldfekvmht rkrhselyhe lnqkfhtfdr yrsqssakek
     1501 psppggrpgl sqhrrhqsws tfksmtlgsl ppkprerlal hrtaawepte ppdgdfqtev
//
LOCUS       NP_001423748             365 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger MYND domain-containing protein 12 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423748 XP_006238822
VERSION     NP_001423748.1
DBSOURCE    REFSEQ: accession NM_001436819.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238822.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.485705.1,
                                           SRR26360181.3349888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..365
                     /product="zinc finger MYND domain-containing protein 12
                     isoform a"
                     /note="zinc finger MYND domain-containing protein 12; zinc
                     finger, MYND domain containing 12"
                     /calculated_mol_wt=41233
     Region          17..54
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          77..>264
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          132..162
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(134..135,138..139,141,173,176..177,180..181,
                     183..184,215,218..219,222..223,226)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          171..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          214..242
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..365
                     /gene="Zmynd12"
                     /coded_by="NM_001436819.1:26..1123"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313552"
                     /db_xref="RGD:1307175"
ORIGIN      
        1 mnviyplavp kgrrlccevc eapaermcta ctvtyycgpv hqkadwgsih akicqllipl
       61 rtsmpffnse eerqhglqql qrrqehlief cytvaqkylf egrhedavpa alhslrfrmn
      121 vhglssvelv paylllaeas lglgrivqae eylsqaqwtv lkstdcsnat hsllhrnlgl
      181 lyiakknlee aryhlandiy fascafgted vrtsggyfhl anifyslkkm eladtlytkv
      241 seiwytylss hyqallhart qqtdllgkqf mndtgldeaq eaeairilts iliiqestst
      301 qapqkgilil ktlgilyylm lefskakeya tkalslaevy lseeeqgviq ellsailaee
      361 kqltt
//
LOCUS       NP_001423712             629 aa            linear   ROD 24-MAR-2025
DEFINITION  transcriptional repressor p66-alpha isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423712 XP_038950270
VERSION     NP_001423712.1
DBSOURCE    REFSEQ: accession NM_001436783.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Basta,J. and Rauchman,M.
  TITLE     The nucleosome remodeling and deacetylase complex in development
            and disease
  JOURNAL   Transl Res 165 (1), 36-47 (2015)
   PUBMED   24880148
  REMARK    Review article
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Marino,S. and Nusse,R.
  TITLE     Mutants in the mouse NuRD/Mi2 component P66alpha are embryonic
            lethal
  JOURNAL   PLoS One 2 (6), e519 (2007)
   PUBMED   17565372
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Brackertz,M., Boeke,J., Zhang,R. and Renkawitz,R.
  TITLE     Two highly related p66 proteins comprise a new family of potent
            transcriptional repressors interacting with MBD2 and MBD3
  JOURNAL   J Biol Chem 277 (43), 40958-40966 (2002)
   PUBMED   12183469
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_038950270.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.864705.1,
                                           SRR21887622.3468384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..629
                     /product="transcriptional repressor p66-alpha isoform 4"
                     /note="p66 alpha; transcriptional repressor p66-alpha"
                     /calculated_mol_wt=67310
     Region          133..172
                     /region_name="P66_CC"
                     /note="Coiled-coil and interaction region of P66A and P66B
                     with MBD2; pfam16563"
                     /db_xref="CDD:465178"
     Region          416..449
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cl29608"
                     /db_xref="CDD:453031"
     CDS             1..629
                     /gene="Gatad2a"
                     /gene_synonym="RGD1310596"
                     /coded_by="NM_001436783.1:300..2189"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="GeneID:290669"
                     /db_xref="RGD:1310596"
ORIGIN      
        1 mseeacrtrs qkrafepdlt eddveskkmk mergpselpv dgdsrvmpep sagpaqgllr
       61 tteamgtgsg egllgdgpvd mrtshsdmks ekrppspdvi vlsdseqpss prvnglttva
      121 lkdtsteall ksspeererm ikqlkeelrl eeaklvllkk lrqsqiqkea taqkptassg
      181 stvttppplv rgpqnipagk pslqtsstri pgsiippplv rggqqvsakl gpqassqvvm
      241 pplvrgaqih nirqhsstgp pplllapras vpsmqiqgqr iiqqglirva nvpntsllvn
      301 ipqptaaslk gttvgsaqan stpssvasvv asaespasrq aaaklalrkq lektlleipp
      361 pkppapemnf lpsaannefi ylvgleevvq nlletqagri satsaaavls repymcvqck
      421 tdftcrwrek ggavmcencm tsnqkkalkv ehtsrlkaaf vkalqqeqem eqrllqqgvg
      481 tasikaetaa phpslkqvik prrklafrsg eardwnngsv lqtssqlsrg sattprgvlh
      541 tfsqspklqn aasatalvsr tgrhservvg tskgtasnwk ktplstggtl afvspslavh
      601 ksssavdrqr eylldmippr sipqsatwk
//
LOCUS       NP_001423720            1443 aa            linear   ROD 24-MAR-2025
DEFINITION  histone-lysine N-methyltransferase NSD3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423720 XP_006253369
VERSION     NP_001423720.1
DBSOURCE    REFSEQ: accession NM_001436791.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1443)
  AUTHORS   Black,J.C., Van Rechem,C. and Whetstine,J.R.
  TITLE     Histone lysine methylation dynamics: establishment, regulation, and
            biological impact
  JOURNAL   Mol Cell 48 (4), 491-507 (2012)
   PUBMED   23200123
  REMARK    Review article
REFERENCE   2  (residues 1 to 1443)
  AUTHORS   Rahman,S., Sowa,M.E., Ottinger,M., Smith,J.A., Shi,Y., Harper,J.W.
            and Howley,P.M.
  TITLE     The Brd4 extraterminal domain confers transcription activation
            independent of pTEFb by recruiting multiple proteins, including
            NSD3
  JOURNAL   Mol Cell Biol 31 (13), 2641-2652 (2011)
   PUBMED   21555454
REFERENCE   3  (residues 1 to 1443)
  AUTHORS   Kim,S.M., Kee,H.J., Eom,G.H., Choe,N.W., Kim,J.Y., Kim,Y.S.,
            Kim,S.K., Kook,H., Kook,H. and Seo,S.B.
  TITLE     Characterization of a novel WHSC1-associated SET domain protein
            with H3K4 and H3K27 methyltransferase activity
  JOURNAL   Biochem Biophys Res Commun 345 (1), 318-323 (2006)
   PUBMED   16682010
REFERENCE   4  (residues 1 to 1443)
  AUTHORS   Rosati,R., La Starza,R., Veronese,A., Aventin,A., Schwienbacher,C.,
            Vallespi,T., Negrini,M., Martelli,M.F. and Mecucci,C.
  TITLE     NUP98 is fused to the NSD3 gene in acute myeloid leukemia
            associated with t(8;11)(p11.2;p15)
  JOURNAL   Blood 99 (10), 3857-3860 (2002)
   PUBMED   11986249
  REMARK    Erratum:[Blood 2002 Aug 15;100(4):1132]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006253369.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1443
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..1443
                     /product="histone-lysine N-methyltransferase NSD3 isoform
                     1"
                     /EC_number="2.1.1.354"
                     /note="histone-lysine N-methyltransferase NSD3;
                     Wolf-Hirschhorn syndrome candidate 1-like 1"
                     /calculated_mol_wt=160802
     Region          275..404
                     /region_name="PWWP_NSD3_rpt1"
                     /note="first PWWP domain found in nuclear SET
                     domain-containing protein 3 (NSD3) and similar proteins;
                     cd20163"
                     /db_xref="CDD:438991"
     Site            order(288,291,319)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438991"
     Site            289..292
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438991"
     Site            order(356..358,361..362)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438991"
     Region          710..752
                     /region_name="PHD1_NSD3"
                     /note="PHD finger 1 found in nuclear SET domain-containing
                     protein 3 (NSD3); cd15649"
                     /db_xref="CDD:277119"
     Site            order(710,720..724,729,747)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277119"
     Region          758..804
                     /region_name="PHD2_NSD3"
                     /note="PHD finger 2 found in nuclear SET domain-containing
                     protein 3 (NSD3); cd15652"
                     /db_xref="CDD:277122"
     Site            order(758,768..772,778,799)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277122"
     Region          805..857
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Site            order(805,823..826,830,852)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276966"
     Region          924..959
                     /region_name="PHD4_NSD3"
                     /note="PHD finger 4 found in nuclear SET domain-containing
                     protein 3 (NSD3); cd15658"
                     /db_xref="CDD:277128"
     Site            order(929..933,937,954)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277128"
     Region          966..1060
                     /region_name="PWWP_NSD3_rpt2"
                     /note="second PWWP domain found in nuclear SET
                     domain-containing protein 3 (NSD3) and similar proteins;
                     cd20166"
                     /db_xref="CDD:438994"
     Site            order(978,981,1009)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438994"
     Site            979..982
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438994"
     Region          1111..1149
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1151..1292
                     /region_name="SET_NSD3"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 3
                     (NSD3) and similar proteins; cd19212"
                     /db_xref="CDD:380989"
     Site            order(1162..1164,1181,1191,1195,1204..1210,1227..1231,
                     1238..1240,1255,1266..1276,1278..1282,1291)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380989"
     Site            order(1162..1164,1204..1207,1227..1231,1268,1275,
                     1279..1282,1291)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380989"
     Site            order(1181,1191,1195,1206..1210,1238..1240,1255,
                     1266..1270)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380989"
     Site            order(1233,1280,1282,1287)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380989"
     Region          1329..1371
                     /region_name="PHD5_NSD3"
                     /note="PHD finger 5 found in nuclear SET domain-containing
                     protein 3 (NSD3); cd15661"
                     /db_xref="CDD:277131"
     Site            order(1329,1338..1342,1348,1366)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277131"
     Region          1370..1419
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     CDS             1..1443
                     /gene="Nsd3"
                     /gene_synonym="Whsc1l1"
                     /coded_by="NM_001436791.1:525..4856"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290831"
                     /db_xref="RGD:1308980"
ORIGIN      
        1 mdfsfsfmqg imgntiqqpp qlidsanirq edafdnnsdi vedggptpfe atlqqgfqcp
       61 patedlpplt ngyppsisly etqtkyppys qypngsangf gavrnfsptd yyhseipntr
      121 pheilekpsp pqpppppllp pppppvpqtv ipkktgspei klkitktiqn grelfesslc
      181 gdllnevqas ehlkskhesr kekrkkssrh essrseerks hkvpklepeg qnrpnervdp
      241 apekpreepv lkeavpvqpi lssvpttets tgvkfqvgdl vwskvgtypw wpcmvssdpq
      301 levhtkintr gareyhvqff snqperawvh ekrvreykgh eqyeellaea akqasnhsek
      361 qkirkprpqr eraqwdigia haekalqmtr eerveqytfi yidkqpeesp sqakksvtsk
      421 aevkkprrpr svgnsqpeqt sagevaspqs stdprrqsqr rhtsveedgp ppvkiawrta
      481 aarkslpasi tmhkgsldlh kcnmspvvki eqvfalqnat gdgkfidqfv ystkgignkt
      541 eisvrgqdrl iisspsqrne kstpsasppe atsgsagpve kkqqrrsirt rsesekstev
      601 vskkkikkeq vetspqaslk tglqkgasei sdsckplkkr srastdveta sctyrdtsds
      661 dsrgpsdgqv gfgkqvdsps aaadadasda qsvdsslsrr gvglskkdtv cqvcentgds
      721 lvacegeccr hfhpeclgla avpegrftce ecetgqhpcf sckvsgkdvk rcsvsvcgkf
      781 yheacvrkfp taifeskgfr cpqhccsscs mekdihkask grmmkclrcp iayhfgdacv
      841 aagsvsvssh ilicsnhskr sshsaainvg fcfvcargli vqdhsdpmfs syaykshyll
      901 sesnraelmk lpmipsssas kkrcekggrl lccescpasf hpeclsidmp egcwncndck
      961 agkklhykqi vwvklgnyrw wpaetcsprs vplniqglkh gvgdfpvlff gshdyywvhq
     1021 grvfpyvegd tnfaegqtsi nktfkkalee aakrfqelka qreskealei ektsrkpppy
     1081 khikankvig kvqiqvadls eiprcnckpg denpcglese clnrmsqyec hpqvcpagdr
     1141 cqnqcftkrl ypdaeiikte rrgwglrtkr sikkgefvne yvgelideee crlrikrahe
     1201 nsvtnfymlt vtkdriidag pkgnysrfmn hscnpncetq kwtvngdvrv glfalcdipa
     1261 gmeltfnynl dclgngrtvc hcgadncsgf lgvrpksact saadektkna klkkrrrgka
     1321 eakqihedyc fqcgdggelv mcdkkdcpka yhllclnltq ppygkwecpw hqcdecgsaa
     1381 isfcefcphs fckahekgal vpsalegrlc csnhdpaspv speywskmrc kwesqdggee
     1441 vke
//
LOCUS       NP_001423761             922 aa            linear   ROD 24-MAR-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423761 XP_006239244
VERSION     NP_001423761.1
DBSOURCE    REFSEQ: accession NM_001436832.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Lapolla,A., Porcu,S., Roverso,M., Desoye,G., Cosma,C.,
            Nardelli,G.B., Bogana,G., Carrozzini,M. and Traldi,P.
  TITLE     A preliminary investigation on placenta protein profile reveals
            only modest changes in well controlled gestational diabetes
            mellitus
  JOURNAL   Eur J Mass Spectrom (Chichester) 19 (3), 211-223 (2013)
   PUBMED   24308201
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   5  (residues 1 to 922)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 922)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006239244.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1866106.1,
                                           SRR26643284.8149.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..922
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 1"
                     /note="serine/arginine repetitive matrix protein 1;
                     serine/arginine repetitive matrix 1"
                     /calculated_mol_wt=103948
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <389..817
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..922
                     /gene="Srrm1"
                     /coded_by="NM_001436832.1:26..2794"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:313620"
                     /db_xref="RGD:1311258"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek laslkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkeks pelpepsvrm kdssvqeats
      241 tsdilkapkp epvpepkeps peknskkeke ktrprsrsrs ksrsrtrsrs pshtrprrrh
      301 rsrsrsyspr rrpsprrrps prrrtpprrm pppprhrrsr spgrrrrrss aslsgsssss
      361 sssrsrsppk kppkrtsspp rktrrlspsa spprrrhrps spatpppktr hsptpqqsnr
      421 arksrvsvsp grtsgkvtkh kgtekresps papkprkvel seseedkgsk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssts ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rmqmgkrwqs pvtkssrrrr spsppparrr rspspapppp ppppprrrrs ptppprrrtp
      601 sppprrrsps prrysppiqr ryspspppkr rtaspppppk rraspspppk rrvshspppk
      661 qrsppvtkrr spslsskhrk gsspgrstre arspqpnkrh spsprprapq tsspppvrrg
      721 asaspqgrqs pspstrpirr vsrtpepkki kkaaspspqs vrrvsssrsv sgspeptakk
      781 ppappspvqs qspstnwspa apakkakspt pspsparnsd qegggkkkkk kkdkkhkkdk
      841 khkkhkkhkk ekavavatpa paapaavsaa atpsaqeepa aapeprkete seaeddnldd
      901 lerhlrekal rsmrkaqvsp qs
//
LOCUS       NP_001423759             296 aa            linear   ROD 24-MAR-2025
DEFINITION  complement C1q tumor necrosis factor-related protein 7 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001423759 XP_006251135
VERSION     NP_001423759.1
DBSOURCE    REFSEQ: accession NM_001436830.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Bi,J., Duan,Y., Wang,M., He,C., Li,X., Zhang,X., Tao,Y., Du,Y. and
            Liu,H.
  TITLE     Deletion of large-conductance calcium-activated potassium channels
            promotes vascular remodelling through the CTRP7-mediated PI3K/Akt
            signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (12), 1-11 (2022)
   PUBMED   36514218
  REMARK    GeneRIF: Deletion of large-conductance calcium-activated potassium
            channels promotes vascular remodelling through the CTRP7-mediated
            PI3K/Akt signaling pathway.
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Rohrbach,S., Aurich,A.C., Li,L. and Niemann,B.
  TITLE     Age-associated loss in adiponectin-activation by caloric
            restriction: lack of compensation by enhanced inducibility of
            adiponectin paralogs CTRP2 and CTRP7
  JOURNAL   Mol Cell Endocrinol 277 (1-2), 26-34 (2007)
   PUBMED   17716811
  REMARK    GeneRIF: The purpose of the current study was to investigate
            age-dependent effects of caloric restriction on the release of
            adiponectin, expression and activation of adiponectin-related
            signaling and on parameters of altered insulin sensitivity.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Wong,G.W., Wang,J., Hug,C., Tsao,T.S. and Lodish,H.F.
  TITLE     A family of Acrp30/adiponectin structural and functional paralogs
  JOURNAL   Proc Natl Acad Sci U S A 101 (28), 10302-10307 (2004)
   PUBMED   15231994
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006251135.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166720.1, FQ220553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786, SAMN16676806
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..296
                     /product="complement C1q tumor necrosis factor-related
                     protein 7 isoform 2 precursor"
                     /note="complement C1q tumor necrosis factor-related
                     protein 7; C1q and tumor necrosis factor related protein
                     7; adiponectin g"
                     /calculated_mol_wt=28867
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2521
     Region          <63..>144
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          156..280
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..296
                     /gene="C1qtnf7"
                     /gene_synonym="Adig; Ctrp7"
                     /coded_by="NM_001436830.1:189..1079"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:305423"
                     /db_xref="RGD:1306978"
ORIGIN      
        1 mprkepkmiv llyvtslaic asgqprgnqa kgesyspryi csipglpgpp gppgangspg
       61 phgriglpgr dgrdgrkgek gekgtaglkg ktgplglage kgdqgetgkk gpigpegekg
      121 evgpagppgp kgdrgdqgdp glpgvcrcgs ivlksafsvg ittsypeerl piifnkvlfn
      181 egehynpatg kficafpgiy yfsyditlan khlaiglvhn gqyrirtfda ntgnhdvasg
      241 stviylqped evwleiffnd qnglfsdpgw adslfsgfll yvdtdyldsi seddel
//
LOCUS       NP_001423733             369 aa            linear   ROD 24-MAR-2025
DEFINITION  beta-1,4-galactosyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_001423733 XP_006238729
VERSION     NP_001423733.1
DBSOURCE    REFSEQ: accession NM_001436804.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Yoshihara,T., Sugihara,K., Kizuka,Y., Oka,S. and Asano,M.
  TITLE     Learning/memory impairment and reduced expression of the HNK-1
            carbohydrate in beta4-galactosyltransferase-II-deficient mice
  JOURNAL   J Biol Chem 284 (18), 12550-12561 (2009)
   PUBMED   19265195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238729.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20525.1,
                                           SRR21887621.63796.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..369
                     /product="beta-1,4-galactosyltransferase 2"
                     /EC_number="2.4.1.38"
                     /note="UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,
                     polypeptide 2"
                     /calculated_mol_wt=41838
     Region          142..358
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(147,149,151,186,213..215)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(213,215,308)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..369
                     /gene="B4galt2"
                     /coded_by="NM_001436804.1:420..1529"
                     /db_xref="GeneID:313536"
                     /db_xref="RGD:1305358"
ORIGIN      
        1 msrllggtle rvckavlllc llhflvavil yfdvyaqhla ffsrfstrsp ahalypaass
       61 stncsrpntt aassglpevp sarpgptapv ippcpdvppg lvgrvvieft spmplervqr
      121 enpgvllggr ysppdctpaq tvaviipfrh rehhlrywlh ylhpmlrrqr lrygvyvinq
      181 hgeetfnrak llnvgfleal kedatydcfi fsdvdlvpmd drnlyrcgdq prhfaiamdk
      241 fgfrlpyasy fggvsglska qflringfpn eywgwggedd difnrisltg mkisrpdvri
      301 gryrmikhdr dkhnepnpqr fnkiqntkms mkwdgigsvr yrvlevsrqp lftnitvdig
      361 qpmswltqg
//
LOCUS       NP_001423745             994 aa            linear   ROD 24-MAR-2025
DEFINITION  storkhead-box protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423745 XP_017455603
VERSION     NP_001423745.1
DBSOURCE    REFSEQ: accession NM_001436816.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Fenstad,M.H., Johnson,M.P., Loset,M., Mundal,S.B., Roten,L.T.,
            Eide,I.P., Bjorge,L., Sande,R.K., Johansson,A.K., Dyer,T.D.,
            Forsmo,S., Blangero,J., Moses,E.K. and Austgulen,R.
  TITLE     STOX2 but not STOX1 is differentially expressed in decidua from
            pre-eclamptic women: data from the Second Nord-Trondelag Health
            Study
  JOURNAL   Mol Hum Reprod 16 (12), 960-968 (2010)
   PUBMED   20643876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_017455603.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..994
                     /product="storkhead-box protein 2 isoform 1"
                     /note="knockout CG10573-PA related; storkhead-box protein
                     2; spinelinin"
                     /calculated_mol_wt=110116
     Region          131..209
                     /region_name="Stork_head"
                     /note="Winged helix Storkhead-box1 domain; pfam10264"
                     /db_xref="CDD:431182"
     CDS             1..994
                     /gene="Stox2"
                     /coded_by="NM_001436816.1:340..3324"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306459"
                     /db_xref="RGD:708477"
ORIGIN      
        1 mpgkmekflq iaphslaivl gpadcpaeek pgtiqpspqv ptqprqlarh higyeifadf
       61 kaenmqhfwn kkvtaavaet fflgwideqv lliqgkeehl ealregwtrr alrppsgfqi
      121 rclgdvspis mspisqsqfi plgeilclai samnsarkpv tqealmehlt tcfpgvptps
      181 qeilrhtlnt lvrerkiypt pdgyfivtpq tyfitpslir tnskwyhlde rvpdrsqcts
      241 pqpgtitpsa sgcvrertlp rkhcdschcc redmhsmhas tlqrkpakdc kdpycppplc
      301 qvpptdksks tinfsyktet lskpkdgekq skkfglklfr lsfkkdktkq lanfsaqfpp
      361 eewplrdedt pttiprevem eiirrinpdl tvenvmrhta lmkkleeeka hrskagssah
      421 hsgrskksrt hrkshgksrs hsktrvskgd psdgshldip gereyefcdp ltrapregcf
      481 iiehkgdnfi mhsntnvies hfpmtpewdv sgelakrrte mpfpepsrgs shskvhrshs
      541 htqdrrsrne rsnkakersr smdnskgplg asslgtpedl aegcsqddqt asqsyiddst
      601 lrpaqtighq rahipsasyk evcipeivgg skepssacsl lepgkspesm psygelspcp
      661 aktavddyfq cntssetvlt apsplgknke dhdtltlveg vkklspserq tphssrdpvg
      721 hkeespkgpg ggpaasggva eglangrlvq hhsaepsnld krkeifskdt lfkplhstls
      781 vnsyhkssls llkshpkspa dtlpgrcekm epslgtsaaq amppsqrqqe pggnqeasfd
      841 yynvsdddds eegankntee eknrddvgtm qwllereker dlqrkfeknl tllapketds
      901 ssnqrathsa rldsmdsssi tvdsgfnspr treslasnts sivesnrrqn palspahgga
      961 gptfnfrast dpptseaekl qkpsnclqas vtsv
//
LOCUS       NP_001423725             563 aa            linear   ROD 24-MAR-2025
DEFINITION  mesoderm induction early response protein 1 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423725 XP_006238541
VERSION     NP_001423725.1
DBSOURCE    REFSEQ: accession NM_001436796.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238541.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.15368.1,
                                           SRR26643429.20124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..563
                     /product="mesoderm induction early response protein 1
                     isoform a"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=63020
     Region          233..282
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          339..383
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(339,369..370,372..373,375..377,379..381)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          393..>539
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..563
                     /gene="Mier1"
                     /gene_synonym="RGD1562337"
                     /coded_by="NM_001436796.1:29..1720"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313418"
                     /db_xref="RGD:1562337"
ORIGIN      
        1 mdgaspgggg ssggggsggg ygvvarfsqc laefrtwlrt nwlrfnadkt dvmlpsvess
       61 spggsaased hefdpsadml vhdfddertl eeeemmeget nfsseiedla regdmpidel
      121 lslygygstv qlpeeeeeee eeeeegedde dadnddnsgc sgenkeenik dssgqedetq
      181 ssnddpsqsv tsqdaqeiir prrckyfdtn seieeeseed edyipsedwk keimvgsmfq
      241 aeipvgvcry kenekvyend dqllwdpeyl pedkvivflk dasrrtgdek gveaipegsh
      301 ikdneqalye lvkcsfdtee alrrlrfnvk aareelsvwt eeecrnfeqg lkaygkdfhl
      361 iqankvrtrs vgecvafyym wkkserydff aqqtrfgkkk ynlhpgvtdy mdrlldeses
      421 aassrapspp ptasnsstsq sekedgtlsn snqngvssng pgeilnkeev kveglhvngp
      481 tggnkkpllt dvdtngyeen nlatdpklah mtarnendfd eknerpakrr rinssgkesp
      541 gsseffqeav shgkfeehen tnd
//
LOCUS       NP_001423697             973 aa            linear   ROD 24-MAR-2025
DEFINITION  E3 ubiquitin-protein ligase BRE1A [Rattus norvegicus].
ACCESSION   NP_001423697 XP_006238216
VERSION     NP_001423697.1
DBSOURCE    REFSEQ: accession NM_001436768.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Lai,C.Y., Hsieh,M.C., Ho,Y.C., Wang,H.H., Chou,D., Wen,Y.C.,
            Yang,P.S., Cheng,J.K. and Peng,H.Y.
  TITLE     Spinal RNF20-Mediated Histone H2B Monoubiquitylation Regulates
            mGluR5 Transcription for Neuropathic Allodynia
  JOURNAL   J Neurosci 38 (43), 9160-9174 (2018)
   PUBMED   30201771
  REMARK    GeneRIF: RNF20-drive H2B monoubiquitination, which facilitates
            phosphorylated mGluR5 transcription in the dorsal horn in the
            development of neuropathic allodynia.
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Stracker,T.H., Roig,I., Knobel,P.A. and Marjanovic,M.
  TITLE     The ATM signaling network in development and disease
  JOURNAL   Front Genet 4, 37 (2013)
   PUBMED   23532176
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Wang,E., Kawaoka,S., Yu,M., Shi,J., Ni,T., Yang,W., Zhu,J.,
            Roeder,R.G. and Vakoc,C.R.
  TITLE     Histone H2B ubiquitin ligase RNF20 is required for MLL-rearranged
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 110 (10), 3901-3906 (2013)
   PUBMED   23412334
REFERENCE   4  (residues 1 to 973)
  AUTHORS   Vethantham,V., Yang,Y., Bowman,C., Asp,P., Lee,J.H., Skalnik,D.G.
            and Dynlacht,B.D.
  TITLE     Dynamic loss of H2B ubiquitylation without corresponding changes in
            H3K4 trimethylation during myogenic differentiation
  JOURNAL   Mol Cell Biol 32 (6), 1044-1055 (2012)
   PUBMED   22252316
REFERENCE   5  (residues 1 to 973)
  AUTHORS   Liu,Z., Oh,S.M., Okada,M., Liu,X., Cheng,D., Peng,J., Brat,D.J.,
            Sun,S.Y., Zhou,W., Gu,W. and Ye,K.
  TITLE     Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor
  JOURNAL   Mol Biol Cell 20 (3), 757-768 (2009)
   PUBMED   19037095
REFERENCE   6  (residues 1 to 973)
  AUTHORS   Shema,E., Tirosh,I., Aylon,Y., Huang,J., Ye,C., Moskovits,N.,
            Raver-Shapira,N., Minsky,N., Pirngruber,J., Tarcic,G.,
            Hublarova,P., Moyal,L., Gana-Weisz,M., Shiloh,Y., Yarden,Y.,
            Johnsen,S.A., Vojtesek,B., Berger,S.L. and Oren,M.
  TITLE     The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a
            putative tumor suppressor through selective regulation of gene
            expression
  JOURNAL   Genes Dev 22 (19), 2664-2676 (2008)
   PUBMED   18832071
  REMARK    Erratum:[Genes Dev. 2017 Sep 15;31(18):1926. doi:
            10.1101/gad.307207.117. PMID: 29051390]
REFERENCE   7  (residues 1 to 973)
  AUTHORS   Tan,L.B., Chen,K.T., Tyan,Y.C., Liao,P.C. and Guo,H.R.
  TITLE     Proteomic analysis for human urinary proteins associated with
            arsenic intoxication
  JOURNAL   Proteomics Clin Appl 2 (7-8), 1087-1098 (2008)
   PUBMED   21136906
REFERENCE   8  (residues 1 to 973)
  AUTHORS   Pavri,R., Zhu,B., Li,G., Trojer,P., Mandal,S., Shilatifard,A. and
            Reinberg,D.
  TITLE     Histone H2B monoubiquitination functions cooperatively with FACT to
            regulate elongation by RNA polymerase II
  JOURNAL   Cell 125 (4), 703-717 (2006)
   PUBMED   16713563
REFERENCE   9  (residues 1 to 973)
  AUTHORS   Kim,J., Hake,S.B. and Roeder,R.G.
  TITLE     The human homolog of yeast BRE1 functions as a transcriptional
            coactivator through direct activator interactions
  JOURNAL   Mol Cell 20 (5), 759-770 (2005)
   PUBMED   16337599
REFERENCE   10 (residues 1 to 973)
  AUTHORS   Zhu,B., Zheng,Y., Pham,A.D., Mandal,S.S., Erdjument-Bromage,H.,
            Tempst,P. and Reinberg,D.
  TITLE     Monoubiquitination of human histone H2B: the factors involved and
            their roles in HOX gene regulation
  JOURNAL   Mol Cell 20 (4), 601-611 (2005)
   PUBMED   16307923
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 21, 2025 this sequence version replaced XP_006238216.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.14878.1,
                                           SRR26643298.27323.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..973
                     /product="E3 ubiquitin-protein ligase BRE1A"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 20, E3 ubiquitin protein
                     ligase"
                     /calculated_mol_wt=113329
     Region          <320..934
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          900..973
                     /region_name="RING-HC_RNF20"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 20 (RNF20); cd16814"
                     /db_xref="CDD:438463"
     CDS             1..973
                     /gene="Rnf20"
                     /coded_by="NM_001436768.1:307..3228"
                     /db_xref="GeneID:313216"
                     /db_xref="RGD:1311936"
ORIGIN      
        1 msgignkraa gepgtsvppe kktavedsgt tvetiklggv ssteeldirt lqsknrklae
       61 mldqrqaied elrehiekle rrqatddasl livnrywsqf deniriilkr ydldqglgdl
      121 lterkalvvp epepdsdsnq erkddrerge gqepafsfla tlasssseem esqlqerves
      181 srravsqivt vydklqekvd llsrklnsgd nlimeeavqe lnsflaqenv rlqeltdllq
      241 ekhhtmsqef cklqgkveta esrvsvlesm iddlqwdidk irkreqrlnr hlaevlervn
      301 skgykvygag sslyggtiti narkfeemna eleenkelaq nrhceleklr qdfeevttqn
      361 eklkvelrsa veevvketpe yrcmqsqfsv lyneslqlka hldeartllh gtrgthqrqv
      421 elierdevsl hkklrteviq ledtlaqvrk eyemlriefe qtlaaneqag pinremrhli
      481 sslqnhnhql kgevlrykrk lreaqsdlnk trlrsgsall qsqsstedak deptelkqds
      541 edlathssal kasqedevks krdeeerere rrekererer erekekerer ekqklkesek
      601 erdpvkdkdk gkhddgrkke aeiikqlkte lkkaqesqke mkllldmyrs apkeqrdkvq
      661 lmaaekkska eledlrqrlk dledkekken kkmadedalr kiraveeqie ylqkklavak
      721 qeeeallsem dvtgqafedm qeqnirlmqq lrekddanfk lmseriksnq ihkllkeeke
      781 eladqvltlk tqvdaqlqvv rkleekehll qsnigtgeke lglrtqalem nkrkameaaq
      841 laddlkaqle laqkklhdfq deivensvtk ekdlfnfkra qedisrlrrk lettkkpdnv
      901 pkcdeilmee ikdykarltc pccnmrkkda vltkcfhvfc fecvktrydt rqrkcpkcna
      961 afgandfhri yig
//
LOCUS       NP_001015008             348 aa            linear   ROD 24-MAR-2025
DEFINITION  transcription elongation factor A protein 3 [Rattus norvegicus].
ACCESSION   NP_001015008 XP_216552
VERSION     NP_001015008.1
DBSOURCE    REFSEQ: accession NM_001015008.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Kwak,H. and Lis,J.T.
  TITLE     Control of transcriptional elongation
  JOURNAL   Annu Rev Genet 47, 483-508 (2013)
   PUBMED   24050178
  REMARK    Review article
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Nishiyama,A., Xin,L., Sharov,A.A., Thomas,M., Mowrer,G., Meyers,E.,
            Piao,Y., Mehta,S., Yee,S., Nakatake,Y., Stagg,C., Sharova,L.,
            Correa-Cerro,L.S., Bassey,U., Hoang,H., Kim,E., Tapnio,R., Qian,Y.,
            Dudekula,D., Zalzman,M., Li,M., Falco,G., Yang,H.T., Lee,S.L.,
            Monti,M., Stanghellini,I., Islam,M.N., Nagaraja,R., Goldberg,I.,
            Wang,W., Longo,D.L., Schlessinger,D. and Ko,M.S.
  TITLE     Uncovering early response of gene regulatory networks in ESCs by
            systematic induction of transcription factors
  JOURNAL   Cell Stem Cell 5 (4), 420-433 (2009)
   PUBMED   19796622
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216552.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091180.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..348
                     /product="transcription elongation factor A protein 3"
                     /note="transcription elongation factor A (SII), 3"
                     /calculated_mol_wt=38847
     Region          5..348
                     /region_name="TFSII"
                     /note="transcription elongation factor S-II; TIGR01385"
                     /db_xref="CDD:273592"
     CDS             1..348
                     /gene="Tcea3"
                     /coded_by="NM_001015008.2:104..1150"
                     /db_xref="GeneID:298559"
                     /db_xref="RGD:1311369"
ORIGIN      
        1 mgleeellri akklekmvar kktegaldll kklnscqmsi qllqttrigv avngvrkhcs
       61 dkevvslakv liknwkrlld sprttkgere arekakkkek glgssgwkpe aglspprkke
      121 ggepktrrds vdsrssttss pkrpslersn ssrskvetpk tpsspstptf apavcllasc
      181 yltgdsvrdk cvemlsaalk aeddfkdygv ncdklaseie dhiyqelkst dmkyrnrvrs
      241 risnlkdprn pglrrnvlsg tispeliakm taeemasdel relrnamtqe airehqmakt
      301 ggtttdllrc skckkkncty nqvqtrsade pmttfvlcne cgnrwkfc
//
LOCUS       NP_445810                361 aa            linear   ROD 24-MAR-2025
DEFINITION  single-stranded DNA-binding protein 3 isoform a [Rattus
            norvegicus].
ACCESSION   NP_445810
VERSION     NP_445810.2
DBSOURCE    REFSEQ: accession NM_053358.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Joshi,K., Lee,S., Lee,B., Lee,J.W. and Lee,S.K.
  TITLE     LMO4 controls the balance between excitatory and inhibitory spinal
            V2 interneurons
  JOURNAL   Neuron 61 (6), 839-851 (2009)
   PUBMED   19323994
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Nishioka,N., Nagano,S., Nakayama,R., Kiyonari,H., Ijiri,T.,
            Taniguchi,K., Shawlot,W., Hayashizaki,Y., Westphal,H.,
            Behringer,R.R., Matsuda,Y., Sakoda,S., Kondoh,H. and Sasaki,H.
  TITLE     Ssdp1 regulates head morphogenesis of mouse embryos by activating
            the Lim1-Ldb1 complex
  JOURNAL   Development 132 (11), 2535-2546 (2005)
   PUBMED   15857913
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 26, 2020 this sequence version replaced NP_445810.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107666.1, AF121893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..361
                     /product="single-stranded DNA-binding protein 3 isoform a"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=37566
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Region          17..43
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          81..338
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     Site            128
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            134
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            138
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Region          140..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R050.1)"
     Region          184..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D032; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWW4; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R050.1)"
     CDS             1..361
                     /gene="Ssbp3"
                     /gene_synonym="Ssdp; Ssdp3"
                     /coded_by="NM_053358.3:360..1445"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:84354"
                     /db_xref="RGD:621502"
ORIGIN      
        1 mfakgkgsav psdgqarekl alyvyeyllh vgaqksaqtf lseirwekni tlgeppgflh
       61 swwcvfwdly caaperrdtc ehsseakafh dysaaaapsp vlgnippndg mpggpippgf
      121 fqpfmsprya ggprppirmg nqppggvpgt qpllpnsmdp trqqghpnmg gsmqrmnppr
      181 gmgpmgpgpq nygsgmrppp nslgpampgi nmgpgagrpw pnpnsansip ysssspgtyv
      241 gppggggppg tpimpspads tnssdniytm inpvppggsr snfpmgpgsd gpmggmggme
      301 phhmngslgs gdidglpkns pnnisgisnp pgtprddgel ggnflhsfqn dnyspsmtms
      361 v
//
LOCUS       NP_001099531             524 aa            linear   ROD 24-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001099531 XP_001055379 XP_224588
VERSION     NP_001099531.1
DBSOURCE    REFSEQ: accession NM_001106061.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_224588.4, XP_001055379.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.49700.1,
                                           SRR26360186.1447654.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..524
                     /product="rho guanine nucleotide exchange factor 3 isoform
                     3"
                     /note="Rho guanine nucleotide exchange factor (GEF) 3"
                     /calculated_mol_wt=59514
     Region          125..301
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          315..447
                     /region_name="PH_RhoGEF3_XPLN"
                     /note="Rho guanine nucleotide exchange factor 3 Pleckstrin
                     homology (PH) domain; cd10572"
                     /db_xref="CDD:269976"
     CDS             1..524
                     /gene="Arhgef3"
                     /coded_by="NM_001106061.2:136..1710"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:290541"
                     /db_xref="RGD:1310672"
ORIGIN      
        1 mvakdypfyl tvkrancsle aplgsgvakd eepsnkrvkp lsrvtslanl ippvkttplk
       61 rfsqtlqrsi sfrnesrpdi laprawsrna tssstkrrds klwsetfdvc vsqvltakei
      121 krqeaifels qgeedliedl klakkayhdp mlklsimteq elnqifgtld sliplhedll
      181 sqlrdvrkpd gstehvgpil vgwlpclssy dsycsnqvaa kalldhkkqd hrvqdflqrc
      241 lespfsrkld lwnfldiprs rlvkyplllr eilrhtpndn pdqqhleeai niiqgivaei
      301 ntktgesecr yykerllyle egqkdslids srvlcchgel knnrgvklhv flfqevlvit
      361 ravthneqlc yqlyrqpipv kdltledlqd gevrlggslr gafsnnerik nffrvsfkng
      421 sqsqthslqa ndtfnkqqwl ncirqaketv lsaagqagll dseslsqspg tenrelrget
      481 kleqmdqsds esdcsmdtse vslecermeq tdascansrp eenv
//
LOCUS       NP_001423734             542 aa            linear   ROD 24-MAR-2025
DEFINITION  cilia- and flagella-associated protein 97 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423734 XP_063131497
VERSION     NP_001423734.1
DBSOURCE    REFSEQ: accession NM_001436805.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 21, 2025 this sequence version replaced XP_063131497.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50596.1,
                                           SRR26643293.74849.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..542
                     /product="cilia- and flagella-associated protein 97
                     isoform 1"
                     /calculated_mol_wt=60985
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          85..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2B7; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H34.1)"
     Region          355..457
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H34.1)"
     CDS             1..542
                     /gene="Cfap97"
                     /gene_synonym="RGD1307325"
                     /coded_by="NM_001436805.1:184..1812"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306469"
                     /db_xref="RGD:1307325"
ORIGIN      
        1 mdrfgdiseg evdhsffdsd fedtkkcesn sifdkqnddd fkeginkdik nlnlkfgvqn
       61 dnlkekidnd tenvnvklgi qtkenyltqk gnerkpkfps keqhvendpi qtrspsllts
      121 srskklcdtt kgnklhlpvp nripkivkge ddyytdgees sddgkkyhvr sksakpssnl
      181 kknntskkys kasssslsss ssrsssdcsd igsdmqnkpd sgssgkrvss vtpsspkqkc
      241 ksgrkssakq kagdynaese dnvtdvtpas tpdsspaqpf elsqsqnqkv kvkrqenvsr
      301 dvyedvealk ndsrclksak rkekhgqnfa pkssvldanl drrskqkvlh dtmdlnhllk
      361 aflqldkkgp qkhhfeqpsi iprknysftr eevrqidren qrllkelsrq aekpgnksti
      421 pgrslghppk lyhsalnrqr eqqrierenm allkrleavk ptvgmkrseq lmdyhrnisy
      481 lnpspsvrrv rstlghyspl rgasrtssat sglscktdrs vldtssgfll rpkppnvrta
      541 wl
//
LOCUS       NP_001423825             448 aa            linear   ROD 24-MAR-2025
DEFINITION  nephrocystin-4 isoform b [Rattus norvegicus].
ACCESSION   NP_001423825
VERSION     NP_001423825.1
DBSOURCE    REFSEQ: accession NM_001436896.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Dharmat,R., Eblimit,A., Robichaux,M.A., Zhang,Z., Nguyen,T.T.,
            Jung,S.Y., He,F., Jain,A., Li,Y., Qin,J., Overbeek,P., Roepman,R.,
            Mardon,G., Wensel,T.G. and Chen,R.
  TITLE     SPATA7 maintains a novel photoreceptor-specific zone in the distal
            connecting cilium
  JOURNAL   J Cell Biol 217 (8), 2851-2865 (2018)
   PUBMED   29899041
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Borgal,L., Habbig,S., Hatzold,J., Liebau,M.C., Dafinger,C.,
            Sacarea,I., Hammerschmidt,M., Benzing,T. and Schermer,B.
  TITLE     The ciliary protein nephrocystin-4 translocates the canonical Wnt
            regulator Jade-1 to the nucleus to negatively regulate beta-catenin
            signaling
  JOURNAL   J Biol Chem 287 (30), 25370-25380 (2012)
   PUBMED   22654112
REFERENCE   3  (residues 1 to 448)
  AUTHORS   French,V.M., van de Laar,I.M., Wessels,M.W., Rohe,C.,
            Roos-Hesselink,J.W., Wang,G., Frohn-Mulder,I.M., Severijnen,L.A.,
            de Graaf,B.M., Schot,R., Breedveld,G., Mientjes,E., van
            Tienhoven,M., Jadot,E., Jiang,Z., Verkerk,A., Swagemakers,S.,
            Venselaar,H., Rahimi,Z., Najmabadi,H., Meijers-Heijboer,H., de
            Graaff,E., Helbing,W.A., Willemsen,R., Devriendt,K., Belmont,J.W.,
            Oostra,B.A., Amack,J.D. and Bertoli-Avella,A.M.
  TITLE     NPHP4 variants are associated with pleiotropic heart malformations
  JOURNAL   Circ Res 110 (12), 1564-1574 (2012)
   PUBMED   22550138
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Hoefele,J., Wolf,M.T., O'Toole,J.F., Otto,E.A., Schultheiss,U.,
            Deschenes,G., Attanasio,M., Utsch,B., Antignac,C. and
            Hildebrandt,F.
  TITLE     Evidence of oligogenic inheritance in nephronophthisis
  JOURNAL   J Am Soc Nephrol 18 (10), 2789-2795 (2007)
   PUBMED   17855640
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Arts,H.H., Doherty,D., van Beersum,S.E., Parisi,M.A.,
            Letteboer,S.J., Gorden,N.T., Peters,T.A., Marker,T., Voesenek,K.,
            Kartono,A., Ozyurek,H., Farin,F.M., Kroes,H.Y., Wolfrum,U.,
            Brunner,H.G., Cremers,F.P., Glass,I.A., Knoers,N.V. and Roepman,R.
  TITLE     Mutations in the gene encoding the basal body protein RPGRIP1L, a
            nephrocystin-4 interactor, cause Joubert syndrome
  JOURNAL   Nat Genet 39 (7), 882-888 (2007)
   PUBMED   17558407
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Hoefele,J., Sudbrak,R., Reinhardt,R., Lehrack,S., Hennig,S.,
            Imm,A., Muerb,U., Utsch,B., Attanasio,M., O'Toole,J.F., Otto,E. and
            Hildebrandt,F.
  TITLE     Mutational analysis of the NPHP4 gene in 250 patients with
            nephronophthisis
  JOURNAL   Hum Mutat 25 (4), 411 (2005)
   PUBMED   15776426
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Hoefele,J., Otto,E., Felten,H., Kuhn,K., Bley,T.A., Zauner,I.,
            Hildebrandt,F. and Neumann,H.P.
  TITLE     Clinical and histological presentation of 3 siblings with mutations
            in the NPHP4 gene
  JOURNAL   Am J Kidney Dis 43 (2), 358-364 (2004)
   PUBMED   14750102
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Otto,E., Hoefele,J., Ruf,R., Mueller,A.M., Hiller,K.S., Wolf,M.T.,
            Schuermann,M.J., Becker,A., Birkenhager,R., Sudbrak,R.,
            Hennies,H.C., Nurnberg,P. and Hildebrandt,F.
  TITLE     A gene mutated in nephronophthisis and retinitis pigmentosa encodes
            a novel protein, nephroretinin, conserved in evolution
  JOURNAL   Am J Hum Genet 71 (5), 1161-1167 (2002)
   PUBMED   12205563
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1094807.1,
                                           SRR26643299.25723.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..448
                     /product="nephrocystin-4 isoform b"
                     /note="nephronophthisis 4 (juvenile) homolog"
                     /calculated_mol_wt=50194
     Region          55..>434
                     /region_name="NPHP4"
                     /note="Nephrocystin-4; cd22239"
                     /db_xref="CDD:412072"
     CDS             1..448
                     /gene="Nphp4"
                     /coded_by="NM_001436896.1:227..1573"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313749"
                     /db_xref="RGD:1560172"
ORIGIN      
        1 mddwhraftq ntlvpphpqr arqfgkesta fqcilkwldg plikqgildm lselechlrv
       61 slfdvtykhf fgrtwkttvk ptnqlskqpp rilfneplyf httlshpsiv avievvaegr
      121 krdgalqvls cgfgilrifg nkpesptsag qdkrlrlyhg tprallhpll qdpieqnrym
      181 tmmencslqy tlkphpplep afhllpenfl isglqqipgl lpphgdtgda lrkprfqkpt
      241 tlhlddlfft lypslekfee elvqllisdh fregvgllds gtlevlerrl hvcvhnglgf
      301 vhrpqvvvlv pemdmtltrs asfsrritas sksssgnqal vlrshlrlpe mvnhpsfaiv
      361 fqleyvfnsp sgadgsasss tslsslacmh mvrwavwnpd leagpgkvtl plqggvqhnp
      421 srclvykvps asmsseesvf gcipiirh
//
LOCUS       NP_001423874              58 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform g [Rattus norvegicus].
ACCESSION   NP_001423874
VERSION     NP_001423874.1
DBSOURCE    REFSEQ: accession NM_001436945.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 58)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 58)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 58)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 58)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 58)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 58)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 58)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2002041.1,
                                           SRR26360190.74433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..58
                     /product="C-C motif chemokine 27 isoform g"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=6225
     CDS             1..58
                     /gene="Ccl27"
                     /coded_by="NM_001436945.1:51..227"
                     /note="isoform g is encoded by transcript variant 13"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 mwrrerssah preqkleplr glmsclssgl rpapqrsgrg llcrtptaaa qtagalki
//
LOCUS       NP_001423785             515 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423785 XP_063143859
VERSION     NP_001423785.1
DBSOURCE    REFSEQ: accession NM_001436856.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143859.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.704735.1,
                                           SRR26360186.1852656.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..515
                     /product="heterochromatin protein 1-binding protein 3
                     isoform b"
                     /calculated_mol_wt=56678
     Region          117..201
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(124,136,168,182)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            163..174
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          226..286
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          302..369
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <431..>505
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..515
                     /gene="Hp1bp3"
                     /coded_by="NM_001436856.1:241..1788"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mpirravnst retppkskla egeeekpepd gsseesistv eepenetppa psreaeqpkg
       61 epesgekees ksaeetkkee kdqskekekk vkktipawat lsasqlaraq kqtpmasspr
      121 pkmdailtea ikacfqksga svvairkyii hkypsldler rgyllkqalk relnrgvikq
      181 vkgkgasgsf vvvqksktpq ksknrkkgsa vdpepqvkle dvlplaftrl cepkeasysl
      241 irkyvsqyyp klrvdirpql lknalqrave rgqleqitgk gasgtfqlkk sgekpllggs
      301 lmeyailsai aamnepktcs ttalkkyvle nhpgtnsnyq mhllkktlqk cekngwleqi
      361 sgkgfsgtfq lcfpyypspg vlfpkkvsdg sededeeede eessedsede epppkrslqk
      421 ktpakpqgkt asmkqrgakp arkvpaaqrg kvrplpkkap pkaktparkg rpapsavkkp
      481 sgstskkpva narkeaklpg kgksamkkks fktkk
//
LOCUS       NP_001102130             164 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform a [Rattus norvegicus].
ACCESSION   NP_001102130 XP_001061271 XP_342824
VERSION     NP_001102130.1
DBSOURCE    REFSEQ: accession NM_001108660.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342824.2, XP_001061271.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2337140.1,
                                           SRR26360181.3322328.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..164
                     /product="C-C motif chemokine 27 isoform a"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=19360
     Region          76..136
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..164
                     /gene="Ccl27"
                     /coded_by="NM_001108660.2:299..793"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerspmpp tsqrlslepp rlpltgwhpw
       61 nktkekqeal plpsstscct qlyrqplptr llrrivrvel qeadgdchlq avvlhltrrs
      121 vcvhpqnrsl arwlerhgkr lqgtlpslnp vlqkkmcpsp qkqk
//
LOCUS       NP_001423786             514 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423786
VERSION     NP_001423786.1
DBSOURCE    REFSEQ: accession NM_001436857.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2180327.1,
                                           SRR26360176.1831048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..514
                     /product="heterochromatin protein 1-binding protein 3
                     isoform c"
                     /calculated_mol_wt=56550
     Region          117..201
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(124,136,168,182)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            163..174
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          225..285
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          301..368
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <430..>504
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..514
                     /gene="Hp1bp3"
                     /coded_by="NM_001436857.1:123..1667"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mpirravnst retppkskla egeeekpepd gsseesistv eepenetppa psreaeqpkg
       61 epesgekees ksaeetkkee kdqskekekk vkktipawat lsasqlaraq kqtpmasspr
      121 pkmdailtea ikacfqksga svvairkyii hkypsldler rgyllkqalk relnrgvikq
      181 vkgkgasgsf vvvqksktpq ksknrkgsav dpepqvkled vlplaftrlc epkeasysli
      241 rkyvsqyypk lrvdirpqll knalqraver gqleqitgkg asgtfqlkks gekpllggsl
      301 meyailsaia amnepktcst talkkyvlen hpgtnsnyqm hllkktlqkc ekngwleqis
      361 gkgfsgtfql cfpyypspgv lfpkkvsdgs ededeeedee essedsedee pppkrslqkk
      421 tpakpqgkta smkqrgakpa rkvpaaqrgk vrplpkkapp kaktparkgr papsavkkps
      481 gstskkpvan arkeaklpgk gksamkkksf ktkk
//
LOCUS       NP_001423780             446 aa            linear   ROD 24-MAR-2025
DEFINITION  probable tRNA methyltransferase 9B [Rattus norvegicus].
ACCESSION   NP_001423780 XP_006253285
VERSION     NP_001423780.1
DBSOURCE    REFSEQ: accession NM_001436851.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Begley,U., Sosa,M.S., Avivar-Valderas,A., Patil,A., Endres,L.,
            Estrada,Y., Chan,C.T., Su,D., Dedon,P.C., Aguirre-Ghiso,J.A. and
            Begley,T.
  TITLE     A human tRNA methyltransferase 9-like protein prevents tumour
            growth by regulating LIN9 and HIF1-alpha
  JOURNAL   EMBO Mol Med 5 (3), 366-383 (2013)
   PUBMED   23381944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006253285.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3021924.1,
                                           SRR26360172.2759995.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840122 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..446
                     /product="probable tRNA methyltransferase 9B"
                     /calculated_mol_wt=49925
     Region          30..143
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     CDS             1..446
                     /gene="Trmt9b"
                     /gene_synonym="RGD1304810"
                     /coded_by="NM_001436851.1:568..1908"
                     /db_xref="GeneID:306504"
                     /db_xref="RGD:1304810"
ORIGIN      
        1 mdpeavqlek qhvhkvyest apyfsdlqnk awprvrqflq dqkpgsliad igcgtgkylk
       61 vnsqvhtlgc dycgplveia rnrgcevmvc dnlnlpfrdq gfdaiisigv ihhfstkqrr
      121 iraikemarv lapggqlmiy vwameqknrh fekqdvlvpw nralcsrlls eshqswghsc
      181 ehptsqgyqg pgsacscavc fkgrcdskrs hsmdygpava rtcceaiske gqqenglysn
      241 fgksfrswff srsldestlr kqiervrpmk iegwanstvs hqpsrypsvd lhaqepfstk
      301 rpnldevfvd assqrhvgcl gvpstsdnfi ghkggesrrk eggnfldttd tgnsvaarng
      361 gdrsarkilr rvsafdstds tsedpsfveg qqdgpdskaf mryyhvfreg elssllqecv
      421 selqvlssgn dhgnwciiae kkrswd
//
LOCUS       NP_001423794            1345 aa            linear   ROD 24-MAR-2025
DEFINITION  SH3 domain and tetratricopeptide repeat-containing protein 1
            [Rattus norvegicus].
ACCESSION   NP_001423794 XP_006251189
VERSION     NP_001423794.1
DBSOURCE    REFSEQ: accession NM_001436865.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1345)
  AUTHORS   Senderek,J., Bergmann,C., Stendel,C., Kirfel,J., Verpoorten,N., De
            Jonghe,P., Timmerman,V., Chrast,R., Verheijen,M.H., Lemke,G.,
            Battaloglu,E., Parman,Y., Erdem,S., Tan,E., Topaloglu,H., Hahn,A.,
            Muller-Felber,W., Rizzuto,N., Fabrizi,G.M., Stuhrmann,M.,
            Rudnik-Schoneborn,S., Zuchner,S., Michael Schroder,J., Buchheim,E.,
            Straub,V., Klepper,J., Huehne,K., Rautenstrauss,B., Buttner,R.,
            Nelis,E. and Zerres,K.
  TITLE     Mutations in a gene encoding a novel SH3/TPR domain protein cause
            autosomal recessive Charcot-Marie-Tooth type 4C neuropathy
  JOURNAL   Am J Hum Genet 73 (5), 1106-1119 (2003)
   PUBMED   14574644
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006251189.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.54899.1,
                                           SRR26643297.43714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1345
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1345
                     /product="SH3 domain and tetratricopeptide
                     repeat-containing protein 1"
                     /note="SH3 domain and tetratricopeptide repeats-containing
                     protein 1"
                     /calculated_mol_wt=149038
     Region          312..366
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(317,319,322,326,346..347,362,364..365)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212818"
     Region          605..655
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(606,609..610,613..614,616,668,671..672,675..676,
                     678..679,710,713..714,717..718,721)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <666..900
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          666..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          701..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <775..1230
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            order(1162,1165..1166,1169..1170,1172,1196,1205..1206,
                     1209..1210,1212..1213,1246,1249..1250,1254..1255,1258)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1162..1189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1165..1233
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          1194..1230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1203..1276
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          1245..1274
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1345
                     /gene="Sh3tc1"
                     /coded_by="NM_001436865.1:127..4164"
                     /db_xref="GeneID:305441"
                     /db_xref="RGD:1305610"
ORIGIN      
        1 mrsfreeeat sedlstmgqg peeppggcsl edkiqsismg lptsqertgp eeaeattvrg
       61 dvappcgmvg qaaeppsnqm avyptdltlq llavrrksgl rspslqqtlr srlrllends
      121 revarvlgel sarllsihsd qdrivvtfkt feeiwkfsty halgfthhcl enllvdqtfw
      181 llspseeeet ailiyvnkda lkqthkslla qegsffvlcp dhcvrrtkep qgagkgpqtl
      241 rrasgvtlgv pvvetvsssp tpsmsskaea veaepepltp fhqwtlrvpw dpidesmsgp
      301 gtpdaqfmrf glasaiadfq gsgpeemsfs vgdvieivga qvpglpwclg qhmasgqvgf
      361 vrtglvrmqg pasdlessif lseeersffr seahfsdeda rrllcrtsgt dvcttcsldw
      421 leeaegeqle qqemslphln pepheslhmv knvlekckac pdhpedpvsw slgavssrvs
      481 spdleeppfc ldpdddwtdp eppdsllqvl sapgyraqfr slydislpcl stalysfdde
      541 eelaerlaqa rgvakkvdlg malarlclll grlcarklkl sqarvyfeea lgalegsfgd
      601 lslvaavyss latvylkqkn gekcvqlapk aaalllgtpg hscstdaell kyalrrvvcg
      661 lspqaearac fllarhythl kqpeealpyl erllrlnrdv gtpqaswped cyllladiyg
      721 rkclphlals clkvsslwtr cslagslrsv dlvlqnapgp nsqrstghsl psqiahylrq
      781 alaslppgtg qtlrgplyas laqlysyhqq ygqaiafmsq aaeadtaagv hpvvdrlval
      841 awlhllcgks lvamdilkcv sdaavankdq ecvmmnmvam alkrmgrtrq aaegyfralh
      901 maysqghlqs qavvlanfga lclqagarsl aqhylreavg lfsqlpsgvc grdftqvllw
      961 lgqlctrrtl pqqakcyyew aflvavetdh lesqlqavqk lchfyskvmp nevrcviyhe
     1021 fqlalarkta dkvlegqlle aisqlylslg terayksald ytkrslgifi dlqqkekear
     1081 awlqagkiyy ilrqnelvdl yiqvaqnaal ytgdpklgle lfeaagdiff ngtwerekav
     1141 sfyrdralpl avtvgdqeve lrlcnklval lsaleapqeg lefahealal sitlgdrlne
     1201 rvayhrlatl hhrlghgela ehfflkalsl ctsplefdee tlyyvkvylv lgdiifyelk
     1261 dpfdaagyyq lalaaavdlg hkkaqlkiyt rlatiyhnfl mdremslffy qkartfasel
     1321 nlrrtnlvpq hfcsrapwla pgyps
//
LOCUS       NP_001007093             952 aa            linear   ROD 24-MAR-2025
DEFINITION  calsyntenin-1 isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001007093 XP_001075647 XP_243040
VERSION     NP_001007093.1
DBSOURCE    REFSEQ: accession NM_001007092.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Zhou,F., Hu,R., Wang,Y., Wu,X., Chen,X., Xi,Z. and Zeng,K.
  TITLE     Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models
  JOURNAL   Synapse 78 (5), e22307 (2024)
   PUBMED   39171546
  REMARK    GeneRIF: Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models.
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Ster,J., Steuble,M., Orlando,C., Diep,T.M., Akhmedov,A.,
            Raineteau,O., Pernet,V., Sonderegger,P. and Gerber,U.
  TITLE     Calsyntenin-1 regulates targeting of dendritic NMDA receptors and
            dendritic spine maturation in CA1 hippocampal pyramidal cells
            during postnatal development
  JOURNAL   J Neurosci 34 (26), 8716-8727 (2014)
   PUBMED   24966372
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Vagnoni,A., Perkinton,M.S., Gray,E.H., Francis,P.T., Noble,W. and
            Miller,C.C.
  TITLE     Calsyntenin-1 mediates axonal transport of the amyloid precursor
            protein and regulates Abeta production
  JOURNAL   Hum Mol Genet 21 (13), 2845-2854 (2012)
   PUBMED   22434822
  REMARK    GeneRIF: findings show that amyloid precursor protein (APP) and
            calsyntenin-1 are co-transported through axons, that loss of
            calsyntenin-1 disrupts axonal transport of APP and that
            calsyntenin-1 loss also leads to altered APP processing and
            increased production of Abeta
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Araki,Y., Kawano,T., Taru,H., Saito,Y., Wada,S., Miyamoto,K.,
            Kobayashi,H., Ishikawa,H.O., Ohsugi,Y., Yamamoto,T., Matsuno,K.,
            Kinjo,M. and Suzuki,T.
  TITLE     The novel cargo Alcadein induces vesicle association of kinesin-1
            motor components and activates axonal transport
  JOURNAL   EMBO J 26 (6), 1475-1486 (2007)
   PUBMED   17332754
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Konecna,A., Frischknecht,R., Kinter,J., Ludwig,A., Steuble,M.,
            Meskenaite,V., Indermuhle,M., Engel,M., Cen,C., Mateos,J.M.,
            Streit,P. and Sonderegger,P.
  TITLE     Calsyntenin-1 docks vesicular cargo to kinesin-1
  JOURNAL   Mol Biol Cell 17 (8), 3651-3663 (2006)
   PUBMED   16760430
  REMARK    GeneRIF: Calsyntenin-1 links a certain type of vesicular and
            tubulovesicular organelles to the Kinesin-1 motor.
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Araki,Y., Tomita,S., Yamaguchi,H., Miyagi,N., Sumioka,A., Kirino,Y.
            and Suzuki,T.
  TITLE     Novel cadherin-related membrane proteins, Alcadeins, enhance the
            X11-like protein-mediated stabilization of amyloid beta-protein
            precursor metabolism
  JOURNAL   J Biol Chem 278 (49), 49448-49458 (2003)
   PUBMED   12972431
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Vogt,L., Schrimpf,S.P., Meskenaite,V., Frischknecht,R., Kinter,J.,
            Leone,D.P., Ziegler,U. and Sonderegger,P.
  TITLE     Calsyntenin-1, a proteolytically processed postsynaptic membrane
            protein with a cytoplasmic calcium-binding domain
  JOURNAL   Mol Cell Neurosci 17 (1), 151-166 (2001)
   PUBMED   11161476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 18, 2011 this sequence version replaced
            XP_243040.5, XP_001075647.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY569014.1, SRR26643429.21974.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..952
                     /product="calsyntenin-1 isoform 4 precursor"
                     /note="alc-alpha; alcadein-alpha"
                     /calculated_mol_wt=103317
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2963
     mat_peptide     29..952
                     /product="Calsyntenin-1. /id=PRO_0000323601"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
                     /calculated_mol_wt=103317
     mat_peptide     29..796
                     /product="Soluble Alc-alpha. /evidence=ECO:0000250.
                     /id=PRO_0000323602"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
                     /calculated_mol_wt=85710
     Region          41..149
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(48..49,107,109,146,148..149)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          158..248
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          355..515
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          537..889
                     /region_name="CLSTN_C"
                     /note="Calsyntenin C-terminal; pfam19699"
                     /db_xref="CDD:466150"
     Site            795..796
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     mat_peptide     797..952
                     /product="CTF1-alpha. /evidence=ECO:0000250.
                     /id=PRO_0000323603"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
                     /calculated_mol_wt=17625
     Site            824..825
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Site            831..851
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          886..952
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     CDS             1..952
                     /gene="Clstn1"
                     /coded_by="NM_001007092.2:207..3065"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:313717"
                     /db_xref="RGD:1306458"
ORIGIN      
        1 mlrrpapala ravrlllagl lygggvwaar vnkhkpwlep tyhgivtend ntvlldppli
       61 aldkdsplrf ageicgfkih gqnvpfdavv vdkstgegii rskekldcel qkdytftiqa
      121 ydcgkgpdgt gvkkshkatv hiqvndvney apvfkeksyk aavvegkqhg silrveavda
      181 dcspqfsqic syeiltpdvp ftvdkdgyik nteklnygke hqykltvtay dcgkkrated
      241 vlvkisvkpt cspgwqgwss rieyepgtga lavfpsihle tcdepvasvq atveletshi
      301 gkgcdrdtys ekslhrlcga aagtsellps psssfnwtvg lptdnghdsd qvfefngtqa
      361 vripdgvvtl dpkepftisv wmrhgpfgrk ketilcssdk tdmnrhhysl yvhgcrlifl
      421 lrqdpseekk yrpaefhwkl nqvcdedwhh fvlnvevpsv tlyvdgvshe pfsvtedypl
      481 hptkietqlv vgacwqggdl hmtqffrgnl agltvrsgkl adkkvidcly tckegldlqv
      541 pedgnrgvqi qtsssqavlt legenvgeld kamqhisyln srqfptpgir rlkitstvkc
      601 fneaacievp pvegyvmvlq peepkislsg vhhfaraase fespegvslf pelkiistit
      661 revepeadga edptvqeslv seeivhdldt cevtvegeel naeqeslevd varlqqkgie
      721 vnhsdlgvvf tgvetmasye evlhllryrn whtrslldrk fklicselng rylsnefkve
      781 vnvihtanpv ehanhmaaqp qfvhpehrsf vdlsghnlas phpfavvpst atvvivvcvs
      841 flvfmiilgv friraahqrt mrdqdtgken emdwddsalt itvnpmetye dqhsseeeee
      901 eeeeeesedg eeeeditsae sesseeeegg pgdgqnttrq qqlewdystl sy
//
LOCUS       NP_001423836             339 aa            linear   ROD 24-MAR-2025
DEFINITION  RING finger protein 215 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423836 XP_063129276
VERSION     NP_001423836.1
DBSOURCE    REFSEQ: accession NM_001436907.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063129276.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.1602318.1,
                                           SRR26360194.598409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..339
                     /product="RING finger protein 215 isoform 2 precursor"
                     /calculated_mol_wt=32668
     sig_peptide     1..45
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4517
     Region          285..334
                     /region_name="RING-H2_RNF215"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 215 (RNF215) and similar proteins; cd16670"
                     /db_xref="CDD:438332"
     CDS             1..339
                     /gene="Rnf215"
                     /gene_synonym="RGD1310738"
                     /coded_by="NM_001436907.1:65..1084"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:305478"
                     /db_xref="RGD:1310738"
ORIGIN      
        1 mgpadrpalr spssppppps ppsplllllp llplwlglmg pgaaadgsep earagrggar
       61 avrvdvklpr qdalvlegvr igseaspepl lggrlllmdv vdaeqeipad gwiavayvgk
      121 eqvaqfhqen qgssqkaypk alvqqmrral flgasallll ilnhsvvrel disqlllrpv
      181 ivlhyssnvt klleallqrt qataeissge slsaniewkl tlwttcglsk dgyggwqdlv
      241 clggaqaqeq edlfkrrvvr rlaslktrrc rlsraahslp epgaetcavc ldyfcnkqwl
      301 rvlpckhefh rdcvdpwlml qqtcplckfn vlgnhysdd
//
LOCUS       NP_001423813             768 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 10
            [Rattus norvegicus].
ACCESSION   NP_001423813 XP_038950548
VERSION     NP_001423813.1
DBSOURCE    REFSEQ: accession NM_001436884.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 768)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038950548.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2681282.1,
                                           SRR26360176.1269646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..768
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 10"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=84295
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..768
                     /gene="Eps15l1"
                     /coded_by="NM_001436884.1:35..2341"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskl pgpvgrllkt aalhpape
//
LOCUS       NP_001423845             686 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform b [Rattus norvegicus].
ACCESSION   NP_001423845 XP_008761770
VERSION     NP_001423845.1
DBSOURCE    REFSEQ: accession NM_001436916.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_008761770.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.334257.1,
                                           SRR26360176.363230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..686
                     /product="protein CBFA2T1 isoform b"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=75343
     Region          204..293
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          419..485
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          525..>579
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          597..633
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..686
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436916.1:64..2124"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 mntkrrcggr aagrlarspp egnlrgragg ggagrgvgaa pqrsradksq gsedvtcyre
       61 lllaargnlh lkitegeged lpfvvlgeee aaalasllsp ntsaiqtgtr gdrtekhstm
      121 pdspvdvktq srltppampp ppttqgaprt ssftpttltn gtshsptaln gapsppngfs
      181 ngpsssssss lanqqlppac garqlsklkr flttlqqfgn dispeigerv rtlvlglvns
      241 tltieefhsk lqeatnfplr pfvipflkan lpllqrellh carlakqnpa qylaqheqll
      301 ldasttspvd ssellldvne ngkrrtpdrt kengfdrepl hsehpskrpc tispgqrysp
      361 nnglsyqpng lphptppppq hyrlddmaia hhyrdsyrhp shrdlrdrnr pmglhgtrqe
      421 emidhrltdr ewaeewkhld hllncimdmv ektrrsltvl rrcqeadree lnywirrysd
      481 aedlkkggsg ssshsrqqsp vnpdpvalda hreflhrpas gyvpeeiwkk aeeavnevkr
      541 qamtelqkav seaerkahdm itterakmer tvaeakrqaa edalavinqq edssescwnc
      601 grkasetcsg cntarycgsf cqhkdwekhh hicgqtlqap qqgetpavss svtpssgags
      661 pmdtppaatp rsttpgtpst iettpr
//
LOCUS       NP_001423838             525 aa            linear   ROD 24-MAR-2025
DEFINITION  thymocyte selection-associated high mobility group box protein TOX
            [Rattus norvegicus].
ACCESSION   NP_001423838 XP_006237906
VERSION     NP_001423838.1
DBSOURCE    REFSEQ: accession NM_001436909.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Artegiani,B., de Jesus Domingues,A.M., Bragado Alonso,S.,
            Brandl,E., Massalini,S., Dahl,A. and Calegari,F.
  TITLE     Tox: a multifunctional transcription factor and novel regulator of
            mammalian corticogenesis
  JOURNAL   EMBO J 34 (7), 896-910 (2015)
   PUBMED   25527292
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Yun,S., Lee,S.H., Yoon,S.R., Kim,M.S., Piao,Z.H., Myung,P.K.,
            Kim,T.D., Jung,H. and Choi,I.
  TITLE     TOX regulates the differentiation of human natural killer cells
            from hematopoietic stem cells in vitro
  JOURNAL   Immunol Lett 136 (1), 29-36 (2011)
   PUBMED   21126536
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Aliahmad,P., de la Torre,B. and Kaye,J.
  TITLE     Shared dependence on the DNA-binding factor TOX for the development
            of lymphoid tissue-inducer cell and NK cell lineages
  JOURNAL   Nat Immunol 11 (10), 945-952 (2010)
   PUBMED   20818394
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Aliahmad,P. and Kaye,J.
  TITLE     Development of all CD4 T lineages requires nuclear factor TOX
  JOURNAL   J Exp Med 205 (1), 245-256 (2008)
   PUBMED   18195075
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Aliahmad,P., O'Flaherty,E., Han,P., Goularte,O.D., Wilkinson,B.,
            Satake,M., Molkentin,J.D. and Kaye,J.
  TITLE     TOX provides a link between calcineurin activation and CD8 lineage
            commitment
  JOURNAL   J Exp Med 199 (8), 1089-1099 (2004)
   PUBMED   15078895
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Wilkinson,B., Chen,J.Y., Han,P., Rufner,K.M., Goularte,O.D. and
            Kaye,J.
  TITLE     TOX: an HMG box protein implicated in the regulation of thymocyte
            selection
  JOURNAL   Nat Immunol 3 (3), 272-280 (2002)
   PUBMED   11850626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006237906.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.26530.1,
                                           SRR26643429.18799.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..525
                     /product="thymocyte selection-associated high mobility
                     group box protein TOX"
                     /note="thymocyte selection-associated HMG box"
                     /calculated_mol_wt=57155
     Region          262..331
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(262..263,265..269,272..273,280,292..293,296,
                     299..300,307,311,314,318,321)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..525
                     /gene="Tox"
                     /coded_by="NM_001436909.1:112..1689"
                     /db_xref="GeneID:362481"
                     /db_xref="RGD:1310455"
ORIGIN      
        1 mdvrfypppa qpaaapaapc lgpspcldpy ycnkfdgenm ymsmtepsqd yvpvsqsypg
       61 pslesedfni ppitppslpd hslvhlneve sgyhslchpm nhngllpfhp qnmdlpeitv
      121 snmlgqdgtl lsnsisvmqe ignaegaqys shpqlaamrp rgqptdlrqq asmmqhgqlt
      181 tinqsqlsaq lglnmggtnv phnspsppgs ksatpspsss vhedecedts kinggekrpa
      241 sdmgkkpktp kkkkkkdpne pqkpvsayal ffrdtqaaik gqnpnatfge vskivasmwd
      301 glgeeqkqvy kkkteaakke ylkqlaayra slvsksyndp vdvktsqppq lvnskpsvfh
      361 gpsqahsaly lsshyhqqpg mtpqltamhp slprniapkp nnqmpvtvsi anmavspppp
      421 lqispplhqh lsmqqhqplv qqplasqlpm qvqtalhspt mqqgftlqpd yqtiinptst
      481 aaqvvtqame yvrsgcrnpp pqpvdwstdy cssggmqrdk alylt
//
LOCUS       NP_001423868             119 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform d precursor [Rattus norvegicus].
ACCESSION   NP_001423868 XP_006238143
VERSION     NP_001423868.1
DBSOURCE    REFSEQ: accession NM_001436939.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 119)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006238143.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228666.1, AW530079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..119
                     /product="C-C motif chemokine 27 isoform d precursor"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=10983
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2364
     Region          31..91
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..119
                     /gene="Ccl27"
                     /coded_by="NM_001436939.1:706..1065"
                     /note="isoform d precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 meglsltgsl plillllspv peaalplpss tscctqlyrq plptrllrri vrvelqeadg
       61 dchlqavvlh ltrrsvcvhp qnrslarwle rhgkrlqgtl pslnpvlqkk mcpspqkqk
//
LOCUS       NP_001423872              87 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform f [Rattus norvegicus].
ACCESSION   NP_001423872
VERSION     NP_001423872.1
DBSOURCE    REFSEQ: accession NM_001436943.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW528290.1, CR464309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..87
                     /product="C-C motif chemokine 27 isoform f"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=9969
     CDS             1..87
                     /gene="Ccl27"
                     /coded_by="NM_001436943.1:93..356"
                     /note="isoform f is encoded by transcript variant 11"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerssahp reqkleplrg lmsclssglr
       61 papqrsgrgl lcrtptaaaq tagalki
//
LOCUS       NP_001423803             911 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001423803 XP_017455655
VERSION     NP_001423803.1
DBSOURCE    REFSEQ: accession NM_001436874.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017455655.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1703719.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..911
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 2"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=99583
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>598
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..911
                     /gene="Eps15l1"
                     /coded_by="NM_001436874.1:35..2770"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamvkd
      601 dpfknkallf snnsqelhpd pfqaedpfks dpfkgadpfk gdpfqsdpfs eqqtavtdpf
      661 ggdpfkesdp fhsstsddff kkqtkndpft sdpftknpsl pskldpfess dpfssssiss
      721 kgsdpfgtld pfgsssfssa egfadfsqms kpppsgpfss slggtgfsdd pfkskqdtpa
      781 lppkkpappr pkppsgqstp vsqlgssafp espdpfqple adsgdpfqnk kgfgdpfsgk
      841 dpfapsssak ppkasssgfa dftsfgneeq qlawakrese kaeqerlarl rrqeqedlel
      901 aialskadmp a
//
LOCUS       NP_001423865             149 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform b [Rattus norvegicus].
ACCESSION   NP_001423865
VERSION     NP_001423865.1
DBSOURCE    REFSEQ: accession NM_001436936.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 149)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 149)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 149)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1614177.1,
                                           SRR26360194.522045.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..149
                     /product="C-C motif chemokine 27 isoform b"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=17741
     Region          61..121
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..149
                     /gene="Ccl27"
                     /coded_by="NM_001436936.1:299..748"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerrlplt gwhpwnktke kqealplpss
       61 tscctqlyrq plptrllrri vrvelqeadg dchlqavvlh ltrrsvcvhp qnrslarwle
      121 rhgkrlqgtl pslnpvlqkk mcpspqkqk
//
LOCUS       NP_001423808             796 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 6
            [Rattus norvegicus].
ACCESSION   NP_001423808 XP_063131565
VERSION     NP_001423808.1
DBSOURCE    REFSEQ: accession NM_001436879.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131565.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.305029.1,
                                           SRR26360186.2885249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..796
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 6"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=87842
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <385..>566
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..796
                     /gene="Eps15l1"
                     /coded_by="NM_001436879.1:35..2425"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskf gneeqqlawa kresekaeqe rlarlrrqeq
      781 edlelaials kadmpa
//
LOCUS       NP_001423871              87 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform f [Rattus norvegicus].
ACCESSION   NP_001423871 XP_038966153
VERSION     NP_001423871.1
DBSOURCE    REFSEQ: accession NM_001436942.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966153.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1454908.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..87
                     /product="C-C motif chemokine 27 isoform f"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=9969
     CDS             1..87
                     /gene="Ccl27"
                     /coded_by="NM_001436942.1:85..348"
                     /note="isoform f is encoded by transcript variant 10"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerssahp reqkleplrg lmsclssglr
       61 papqrsgrgl lcrtptaaaq tagalki
//
LOCUS       NP_001423809             796 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 7
            [Rattus norvegicus].
ACCESSION   NP_001423809 XP_063131564
VERSION     NP_001423809.1
DBSOURCE    REFSEQ: accession NM_001436880.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131564.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.652970.1,
                                           SRR26643297.46656.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..796
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 7"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=87269
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..796
                     /gene="Eps15l1"
                     /coded_by="NM_001436880.1:35..2425"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskp ppsgpfsssl ggtgfsddpf kskqdtpalp
      781 pkkpapprpk ppsvwq
//
LOCUS       NP_001012038            1194 aa            linear   ROD 24-MAR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001012038 XP_223569
VERSION     NP_001012038.1
DBSOURCE    REFSEQ: accession NM_001012038.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Walker,D.M., Urbe,S., Dove,S.K., Tenza,D., Raposo,G. and
            Clague,M.J.
  TITLE     Characterization of MTMR3. an inositol lipid 3-phosphatase with
            novel substrate specificity
  JOURNAL   Curr Biol 11 (20), 1600-1605 (2001)
   PUBMED   11676921
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Taylor,G.S., Maehama,T. and Dixon,J.E.
  TITLE     Myotubularin, a protein tyrosine phosphatase mutated in myotubular
            myopathy, dephosphorylates the lipid second messenger,
            phosphatidylinositol 3-phosphate
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8910-8915 (2000)
   PUBMED   10900271
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Zhao,R., Qi,Y. and Zhao,Z.J.
  TITLE     FYVE-DSP1, a dual-specificity protein phosphatase containing an
            FYVE domain
  JOURNAL   Biochem Biophys Res Commun 270 (1), 222-229 (2000)
   PUBMED   10733931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 11, 2005 this sequence version replaced XP_223569.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087045.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1194
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR3 isoform 1"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3"
                     /calculated_mol_wt=133369
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          19..112
                     /region_name="PH-GRAM_MTMR3"
                     /note="Myotubularian (MTM) related 3 protein (MTMR3)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13341"
                     /db_xref="CDD:270149"
     Region          165..481
                     /region_name="PTP-MTMR3"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 3;
                     cd14586"
                     /db_xref="CDD:350434"
     Region          583..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          693..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          852..871
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          876..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13615; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          932..971
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          988..1017
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K296; propagated from
                     UniProtKB/Swiss-Prot (Q5PQT2.1)"
     Region          1111..1171
                     /region_name="FYVE_MTMR3"
                     /note="FYVE domain found in myotubularin-related protein 3
                     (MTMR3) and similar proteins; cd15732"
                     /db_xref="CDD:277271"
     Site            order(1112,1115,1133..1138,1140..1141,1165..1167)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277271"
     CDS             1..1194
                     /gene="Mtmr3"
                     /coded_by="NM_001012038.2:243..3827"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305482"
                     /db_xref="RGD:1310972"
ORIGIN      
        1 mrhsleciqa nqifprkqli redenlqvpf lelhgestey vgraedaiia lsnyrlhikf
       61 keslvnvplq liesvecrdi fqlhltckdc kvircqfptf eqcqdwlkrl nnairppgki
      121 edlfsfayha wcmevyasek eqhgdlcrpg ehvtsrfkne vermgfdmnn awrisninek
      181 yklcgsypqe livpawitdk elesvagfrs wkripaviyr hqsngaviar cgqpevswwg
      241 wrnaddehlv qsvakacasd sqssvgkvst rnscrgfpna gdlsdvefda slsnasgtes
      301 lalqpqklli ldarsyaaav anrakgggce cpeyypncev vfmgmanihs irrsfqslrl
      361 lctqmpdpgn wlsalestkw lhhlsvllks allvvhavdr dqrpvlvhcs dgwdrtpqiv
      421 alakllldpy yrtvegfqvl vemewldfgh kfadrcghge nsddlnercp vflqwldcvh
      481 qlqrqfpcsf efneaflvkl vqhtysclfg tflcnnaker gekqtqertc svwsllragn
      541 kafknllyss qseavlypvc hvrnlmlwsa vylpcpspst ptddscapyp apgtspdepp
      601 lsrlpktrsf dnltttcdnm vplasrrssd pslnekwqeh grslelssfa gsgeevpaid
      661 slrrpsrllg gaelsvaagv aegqmenilq eatkeesgve epthrehtev pevkeeapla
      721 kesrtaaqgs gvlyqepqld datlrshlgp slssfsqgip ehrevghsvl ssslpaslrg
      781 edsqevpveq pqveniaedr envvpavpvd vkiglgtses spllpsqvpf etrgphmnns
      841 vhmlledkvk sesgpqlhhr pclassgrfs gkdmlpiape prsaerpqwd svlhrtsspg
      901 ntlslmmqap calpldkcrq rivcngalet enkaseqpag fdtlqkyptp nghcangetg
      961 rskdslshql satsyssahs csrnlhhkwl nshsgrpstt nspeqpsrsh ldddgmpvyt
     1021 dtiqqrlrqi esghqqevet lkkqvqelks rlesqyltss lrfngdfgde vtsipdsesn
     1081 ldqnclsrcs teifseaswe qvdkqdtemt rwlpdhlaah cyacdsafwl asrkhhcrnc
     1141 gnvfcssccn qkvpvpsqql fepsrvcksc ysslhptsss idleldkpia atsn
//
LOCUS       NP_001423806             273 aa            linear   ROD 24-MAR-2025
DEFINITION  SPRY domain-containing SOCS box protein 1 [Rattus norvegicus].
ACCESSION   NP_001423806
VERSION     NP_001423806.1
DBSOURCE    REFSEQ: accession NM_001436877.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Nishiya,T., Matsumoto,K., Maekawa,S., Kajita,E., Horinouchi,T.,
            Fujimuro,M., Ogasawara,K., Uehara,T. and Miwa,S.
  TITLE     Regulation of inducible nitric-oxide synthase by the SPRY domain-
            and SOCS box-containing proteins
  JOURNAL   J Biol Chem 286 (11), 9009-9019 (2011)
   PUBMED   21199876
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.21509.1,
                                           SRR26360176.2055833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..273
                     /product="SPRY domain-containing SOCS box protein 1"
                     /calculated_mol_wt=30640
     Region          54..227
                     /region_name="SPRY_SOCS1-2-4"
                     /note="SPRY domain in the suppressor of cytokine signaling
                     1, 2, 4 families (SOCS1, SOCS2, SOCS4); cd12906"
                     /db_xref="CDD:293963"
     Site            order(77,79,111,129,216..218)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:293963"
     Region          232..273
                     /region_name="SOCS"
                     /note="SOCS (suppressors of cytokine signaling) box. The
                     SOCS box is found in the C-terminal region of CIS/SOCS
                     family proteins (in combination with a SH2 domain), ASBs
                     (ankyrin repeat-containing proteins with a SOCS box), SSBs
                     (SPRY domain-containing proteins...; cl02533"
                     /db_xref="CDD:470605"
     Site            order(233..238,244,254,260)
                     /site_type="active"
                     /note="elongin B/C interaction [active]"
                     /db_xref="CDD:239641"
     CDS             1..273
                     /gene="Spsb1"
                     /gene_synonym="RGD1309319"
                     /coded_by="NM_001436877.1:360..1181"
                     /db_xref="GeneID:313722"
                     /db_xref="RGD:1309319"
ORIGIN      
        1 mgqkvtggik tvdmrdptyr plkqelqgld yckptrldll ldmppvsydv qllhswnnnd
       61 rslnvfvked dklifhrhpv aqstdairgk vgytrglhvw qitwamrqrg thavvgvata
      121 daplhsvgyt tlvgnnhesw gwdlgrnrly hdgknqpskt ypaflepdet fivpdsflva
      181 ldmddgtlsf ivdgqymgva frglkgkkly pvvsavwghc eirmryvngl dpeplplmdl
      241 crrsvrlalg kerlgaipal plpaslkayl lyq
//
LOCUS       NP_001100784             446 aa            linear   ROD 24-MAR-2025
DEFINITION  probable tRNA methyltransferase 9B [Rattus norvegicus].
ACCESSION   NP_001100784 XP_001066385 XP_224905
VERSION     NP_001100784.1
DBSOURCE    REFSEQ: accession NM_001107314.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Begley,U., Sosa,M.S., Avivar-Valderas,A., Patil,A., Endres,L.,
            Estrada,Y., Chan,C.T., Su,D., Dedon,P.C., Aguirre-Ghiso,J.A. and
            Begley,T.
  TITLE     A human tRNA methyltransferase 9-like protein prevents tumour
            growth by regulating LIN9 and HIF1-alpha
  JOURNAL   EMBO Mol Med 5 (3), 366-383 (2013)
   PUBMED   23381944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001066385.1, XP_224905.4.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26643429.50752.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..446
                     /product="probable tRNA methyltransferase 9B"
                     /calculated_mol_wt=49925
     Region          30..143
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     CDS             1..446
                     /gene="Trmt9b"
                     /gene_synonym="RGD1304810"
                     /coded_by="NM_001107314.2:715..2055"
                     /db_xref="GeneID:306504"
                     /db_xref="RGD:1304810"
ORIGIN      
        1 mdpeavqlek qhvhkvyest apyfsdlqnk awprvrqflq dqkpgsliad igcgtgkylk
       61 vnsqvhtlgc dycgplveia rnrgcevmvc dnlnlpfrdq gfdaiisigv ihhfstkqrr
      121 iraikemarv lapggqlmiy vwameqknrh fekqdvlvpw nralcsrlls eshqswghsc
      181 ehptsqgyqg pgsacscavc fkgrcdskrs hsmdygpava rtcceaiske gqqenglysn
      241 fgksfrswff srsldestlr kqiervrpmk iegwanstvs hqpsrypsvd lhaqepfstk
      301 rpnldevfvd assqrhvgcl gvpstsdnfi ghkggesrrk eggnfldttd tgnsvaarng
      361 gdrsarkilr rvsafdstds tsedpsfveg qqdgpdskaf mryyhvfreg elssllqecv
      421 selqvlssgn dhgnwciiae kkrswd
//
LOCUS       NP_062122               1898 aa            linear   ROD 24-MAR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase F isoform 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_062122 XP_038966091 XP_346988
VERSION     NP_062122.2
DBSOURCE    REFSEQ: accession NM_019249.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1898)
  AUTHORS   Dyck,S., Kataria,H., Akbari-Kelachayeh,K., Silver,J. and
            Karimi-Abdolrezaee,S.
  TITLE     LAR and PTPsigma receptors are negative regulators of
            oligodendrogenesis and oligodendrocyte integrity in spinal cord
            injury
  JOURNAL   Glia 67 (1), 125-145 (2019)
   PUBMED   30394599
  REMARK    GeneRIF: In a spinal cord injury model, blocking LAR and PTPalpha
            receptors promotes oligodendrogenesis.
REFERENCE   2  (residues 1 to 1898)
  AUTHORS   Shijo,T., Warita,H., Suzuki,N., Kitajima,Y., Ikeda,K., Akiyama,T.,
            Ono,H., Mitsuzawa,S., Nishiyama,A., Izumi,R. and Aoki,M.
  TITLE     Aberrant astrocytic expression of chondroitin sulfate proteoglycan
            receptors in a rat model of amyotrophic lateral sclerosis
  JOURNAL   J Neurosci Res 96 (2), 222-233 (2018)
   PUBMED   28752900
  REMARK    GeneRIF: This study showed that astrocytes aberrantly and
            progressively expressed PTPsigma and LAR at the site of motor
            neuron degeneration in Tg ALS model rats with mutant SOD1.
REFERENCE   3  (residues 1 to 1898)
  AUTHORS   Choi,Y., Nam,J., Whitcomb,D.J., Song,Y.S., Kim,D., Jeon,S.,
            Um,J.W., Lee,S.G., Woo,J., Kwon,S.K., Li,Y., Mah,W., Kim,H.M.,
            Ko,J., Cho,K. and Kim,E.
  TITLE     SALM5 trans-synaptically interacts with LAR-RPTPs in a
            splicing-dependent manner to regulate synapse development
  JOURNAL   Sci Rep 6, 26676 (2016)
   PUBMED   27225731
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1898)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
REFERENCE   5  (residues 1 to 1898)
  AUTHORS   Song,Y.S., Lee,H.J., Prosselkov,P., Itohara,S. and Kim,E.
  TITLE     Trans-induced cis interaction in the tripartite NGL-1, netrin-G1
            and LAR adhesion complex promotes development of excitatory
            synapses
  JOURNAL   J Cell Sci 126 (Pt 21), 4926-4938 (2013)
   PUBMED   23986473
REFERENCE   6  (residues 1 to 1898)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Increased abundance of specific skeletal muscle protein-tyrosine
            phosphatases in a genetic model of insulin-resistant obesity and
            diabetes mellitus
  JOURNAL   Metabolism 44 (9), 1175-1184 (1995)
   PUBMED   7666792
REFERENCE   7  (residues 1 to 1898)
  AUTHORS   Ahmad,F., Considine,R.V. and Goldstein,B.J.
  TITLE     Increased abundance of the receptor-type protein-tyrosine
            phosphatase LAR accounts for the elevated insulin receptor
            dephosphorylating activity in adipose tissue of obese human
            subjects
  JOURNAL   J Clin Invest 95 (6), 2806-2812 (1995)
   PUBMED   7769120
REFERENCE   8  (residues 1 to 1898)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Purification, identification and subcellular distribution of three
            predominant protein-tyrosine phosphatase enzymes in skeletal muscle
            tissue
  JOURNAL   Biochim Biophys Acta 1248 (1), 57-69 (1995)
   PUBMED   7711057
REFERENCE   9  (residues 1 to 1898)
  AUTHORS   Pot,D.A., Woodford,T.A., Remboutsika,E., Haun,R.S. and Dixon,J.E.
  TITLE     Cloning, bacterial expression, purification, and characterization
            of the cytoplasmic domain of rat LAR, a receptor-like protein
            tyrosine phosphatase
  JOURNAL   J Biol Chem 266 (29), 19688-19696 (1991)
   PUBMED   1918076
REFERENCE   10 (residues 1 to 1898)
  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.
  TITLE     A new member of the immunoglobulin superfamily that has a
            cytoplasmic region homologous to the leukocyte common antigen
  JOURNAL   J Exp Med 168 (5), 1523-1530 (1988)
   PUBMED   2972792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 24, 2025 this sequence version replaced
            XP_038966091.1, NP_062122.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19839.1,
                                           SRR26643295.22390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1898
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1898
                     /product="receptor-type tyrosine-protein phosphatase F
                     isoform 3 precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase F;
                     leukocyte antigen-related (LAR) PTP receptor; leukocyte
                     common antigen related"
                     /calculated_mol_wt=208639
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2941
     mat_peptide     30..1898
                     /product="Receptor-type tyrosine-protein phosphatase F.
                     /id=PRO_5000142152"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
                     /calculated_mol_wt=208639
     Region          33..124
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          136..226
                     /region_name="IgI_2_RPTP_IIa_LAR_like"
                     /note="Second immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F; member of
                     the I-set of IgSF domains; cd05738"
                     /db_xref="CDD:409400"
     Region          136..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409400"
     Region          143..147
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409400"
     Region          150..159
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409400"
     Region          164..170
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409400"
     Region          172..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409400"
     Region          183..187
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409400"
     Region          190..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409400"
     Region          204..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409400"
     Region          214..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409400"
     Region          235..316
                     /region_name="IgI_3_RPTP_IIa_LAR_like"
                     /note="Third immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F (also known
                     as LAR), type IIa; member of the I-set of IgSF domains;
                     cd05739"
                     /db_xref="CDD:409401"
     Region          235..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409401"
     Region          241..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409401"
     Region          248..256
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409401"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          261..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409401"
     Region          269..271
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409401"
     Region          274..278
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409401"
     Region          283..288
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409401"
     Region          288..712
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          295..302
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409401"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          306..315
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409401"
     Region          592..1050
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          693..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            941
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            957
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1255..1275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10586; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          1326..1601
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1603..1893
                     /region_name="R-PTP-F-2"
                     /note="PTP-like domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 2; cd14629"
                     /db_xref="CDD:350477"
     CDS             1..1898
                     /gene="Ptprf"
                     /gene_synonym="LARFN5C"
                     /coded_by="NM_019249.3:313..6009"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:360406"
                     /db_xref="RGD:3453"
ORIGIN      
        1 mapepapgrr mvplvpalvm lglmagahgd skpvfvkvpe dqiglsggva sfvcqatgep
       61 kpritwmkkg kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa
      121 klsvleedql psgfptidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpass
      181 ngrikqlrsg alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss
      241 qevmpggnvn ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv mrsanytcva
      301 isslgmieat aqvtvkalpk ppidlvvtet tatsvtltwd sgntepvsfy giqyraagtd
      361 gpfqevdgva strysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv
      421 qarmlsastm lvqweppeep nglvrgyrvy ytpdsrrpls awhkhntdag llttvgsllp
      481 gityslrvla ftavgdgpps ptiqvktqqg vpaqpadfqa kaesdtriql swllppqeri
      541 ikyelvywaa edegqqhkvt fdptssytle dlkpdtlyhf qlaarsdlgv gvftptvear
      601 taqstpsapp qkvtcvstgs ttvrvswvpp padsrngiit qysvayeavd gedrkrhvvd
      661 gisrehsswd llglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl
      721 nstavhvswk lpvpnkqhgq irgyqvtyvr lengeprgqp iiqdvmlaea qettisgltp
      781 ettysitvaa yttkgdgars kpkvvtttga vpgrptmmvs ttamhtallq whppkelpge
      841 llgyrlqyrr adearpntid fgkddqhftv tglhkgatyi frlaaknrag pgeefekeit
      901 tpedapsgfp qnlrvtgltt sttelawdpp vlaerngrit nytvvyrdin sqhelqnvtg
      961 dvhltllglk pdttydikvr ahtskgagpl spsiqsqtmp meqvfaknfr vaaamktsvl
     1021 lswevpdsyk savpfkilyn gqsvevdghs mrkliadlqp nteysfvlmn rgssagglqh
     1081 lvsirtapdl lpqkplpasa fiedgrfsls mpqvqdpslv rwfyivvvpi drvggnllap
     1141 rwstpeelel delleaieqg eekqrrrrrq aerlkpyvaa qvdelpetft lgdkknyrgf
     1201 ynrplspdls yqcfvlaslk epmdqkryas spysdeivvq vtpaqqqeep emlwvtgpvl
     1261 aviliilivi aillfkrkrt hspsskdeqs iglkdsllah ssdpvemrrl nyqtpgmrdh
     1321 ppipitdlad nierlkandg lkfsqeyesi dpgqqftwen snsevnkpkn ryanviaydh
     1381 srvlltsidg vpgsdyinan yidgyrkqna yiatqgplpe tmgdfwrmvw eqrtatvvmm
     1441 trleeksrvk cdqywpargt etygliqvtl vdtvelatyt mrtfalhksg ssekrelrqf
     1501 qfmawpdhgv peyptpilaf lrrvkacnpl dagpmvvhcs agvgrtgcfi vidamlermk
     1561 hektvdiygh vtcmrsqrny mvqtedqyvf ihealleaam cghtevlarn lyahiqklgq
     1621 vppgesvtam elefkllans kahtsrfisa nlpcnkfknr lvnimpyelt rvclqpirgv
     1681 egsdyinasf ldgyrqqkay iatqgplaes tedfwrmlwe hnstiivmlt klremgrekc
     1741 hqywpaersa ryqyfvvdpm aeynmpqyil refkvtdard gqsrtirqfq ftdwpeqgvp
     1801 ktgegfidfi gqvhktkeqf gqdgpitvhc sagvgrtgvf itlsivlerm ryegvvdmfq
     1861 tvktlrtqrp amvqtedqyq lcyraaleyl gsfdhyat
//
LOCUS       NP_001007704             216 aa            linear   ROD 24-MAR-2025
DEFINITION  ceramide-1-phosphate transfer protein isoform a [Rattus
            norvegicus].
ACCESSION   NP_001007704 XP_233718
VERSION     NP_001007704.1
DBSOURCE    REFSEQ: accession NM_001007703.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Mishra,S.K., Gao,Y.G., Deng,Y., Chalfant,C.E., Hinchcliffe,E.H. and
            Brown,R.E.
  TITLE     CPTP: A sphingolipid transfer protein that regulates autophagy and
            inflammasome activation
  JOURNAL   Autophagy 14 (5), 862-879 (2018)
   PUBMED   29164996
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Simanshu,D.K., Kamlekar,R.K., Wijesinghe,D.S., Zou,X., Zhai,X.,
            Mishra,S.K., Molotkovsky,J.G., Malinina,L., Hinchcliffe,E.H.,
            Chalfant,C.E., Brown,R.E. and Patel,D.J.
  TITLE     Non-vesicular trafficking by a ceramide-1-phosphate transfer
            protein regulates eicosanoids
  JOURNAL   Nature 500 (7463), 463-467 (2013)
   PUBMED   23863933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 29, 2004 this sequence version replaced XP_233718.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083599.1, SRR26643295.24081.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..216
                     /product="ceramide-1-phosphate transfer protein isoform a"
                     /note="glycolipid transfer protein domain-containing
                     protein 1; glycolipid transfer protein domain containing
                     1"
                     /calculated_mol_wt=24391
     Region          27..175
                     /region_name="GLTP"
                     /note="Glycolipid transfer protein (GLTP); pfam08718"
                     /db_xref="CDD:462575"
     CDS             1..216
                     /gene="Cptp"
                     /gene_synonym="Gltpd1"
                     /coded_by="NM_001007703.2:249..899"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:313771"
                     /db_xref="RGD:1359656"
ORIGIN      
        1 mdgperdfnl kvvlisfkkc ltdkgevlld hytaswkglv rflnslgavf sfiskdvvsk
       61 lqimehlrsg pqsehyislq smvayevsnk lvdrdsrsrp rhpnsgcrtv lrlhralhwl
      121 qlfleglrts sedartstlc seaynatlaa yhswivrqav nvafhalppr kvfleamnmg
      181 sseqavemlg ealpfieqvy disqklyaeh slldlp
//
LOCUS       NP_001423801             962 aa            linear   ROD 24-MAR-2025
DEFINITION  calsyntenin-1 isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001423801 XP_038966030
VERSION     NP_001423801.1
DBSOURCE    REFSEQ: accession NM_001436872.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Zhou,F., Hu,R., Wang,Y., Wu,X., Chen,X., Xi,Z. and Zeng,K.
  TITLE     Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models
  JOURNAL   Synapse 78 (5), e22307 (2024)
   PUBMED   39171546
  REMARK    GeneRIF: Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models.
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Ster,J., Steuble,M., Orlando,C., Diep,T.M., Akhmedov,A.,
            Raineteau,O., Pernet,V., Sonderegger,P. and Gerber,U.
  TITLE     Calsyntenin-1 regulates targeting of dendritic NMDA receptors and
            dendritic spine maturation in CA1 hippocampal pyramidal cells
            during postnatal development
  JOURNAL   J Neurosci 34 (26), 8716-8727 (2014)
   PUBMED   24966372
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 962)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 962)
  AUTHORS   Vagnoni,A., Perkinton,M.S., Gray,E.H., Francis,P.T., Noble,W. and
            Miller,C.C.
  TITLE     Calsyntenin-1 mediates axonal transport of the amyloid precursor
            protein and regulates Abeta production
  JOURNAL   Hum Mol Genet 21 (13), 2845-2854 (2012)
   PUBMED   22434822
  REMARK    GeneRIF: findings show that amyloid precursor protein (APP) and
            calsyntenin-1 are co-transported through axons, that loss of
            calsyntenin-1 disrupts axonal transport of APP and that
            calsyntenin-1 loss also leads to altered APP processing and
            increased production of Abeta
REFERENCE   6  (residues 1 to 962)
  AUTHORS   Araki,Y., Kawano,T., Taru,H., Saito,Y., Wada,S., Miyamoto,K.,
            Kobayashi,H., Ishikawa,H.O., Ohsugi,Y., Yamamoto,T., Matsuno,K.,
            Kinjo,M. and Suzuki,T.
  TITLE     The novel cargo Alcadein induces vesicle association of kinesin-1
            motor components and activates axonal transport
  JOURNAL   EMBO J 26 (6), 1475-1486 (2007)
   PUBMED   17332754
REFERENCE   7  (residues 1 to 962)
  AUTHORS   Konecna,A., Frischknecht,R., Kinter,J., Ludwig,A., Steuble,M.,
            Meskenaite,V., Indermuhle,M., Engel,M., Cen,C., Mateos,J.M.,
            Streit,P. and Sonderegger,P.
  TITLE     Calsyntenin-1 docks vesicular cargo to kinesin-1
  JOURNAL   Mol Biol Cell 17 (8), 3651-3663 (2006)
   PUBMED   16760430
  REMARK    GeneRIF: Calsyntenin-1 links a certain type of vesicular and
            tubulovesicular organelles to the Kinesin-1 motor.
REFERENCE   8  (residues 1 to 962)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
REFERENCE   9  (residues 1 to 962)
  AUTHORS   Araki,Y., Tomita,S., Yamaguchi,H., Miyagi,N., Sumioka,A., Kirino,Y.
            and Suzuki,T.
  TITLE     Novel cadherin-related membrane proteins, Alcadeins, enhance the
            X11-like protein-mediated stabilization of amyloid beta-protein
            precursor metabolism
  JOURNAL   J Biol Chem 278 (49), 49448-49458 (2003)
   PUBMED   12972431
REFERENCE   10 (residues 1 to 962)
  AUTHORS   Vogt,L., Schrimpf,S.P., Meskenaite,V., Frischknecht,R., Kinter,J.,
            Leone,D.P., Ziegler,U. and Sonderegger,P.
  TITLE     Calsyntenin-1, a proteolytically processed postsynaptic membrane
            protein with a cytoplasmic calcium-binding domain
  JOURNAL   Mol Cell Neurosci 17 (1), 151-166 (2001)
   PUBMED   11161476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966030.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.15012.1,
                                           SRR26643295.23837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..962
                     /product="calsyntenin-1 isoform 3 precursor"
                     /note="alc-alpha; alcadein-alpha"
                     /calculated_mol_wt=104467
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2963
     Region          41..159
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(48..49,117,119,156,158..159)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          168..258
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          365..525
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Site            366
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          547..899
                     /region_name="CLSTN_C"
                     /note="Calsyntenin C-terminal; pfam19699"
                     /db_xref="CDD:466150"
     Site            805..806
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     mat_peptide     807..962
                     /product="CTF1-alpha. /evidence=ECO:0000250.
                     /id=PRO_0000323603"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
                     /calculated_mol_wt=17625
     Site            834..835
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Site            841..861
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          896..962
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     CDS             1..962
                     /gene="Clstn1"
                     /coded_by="NM_001436872.1:207..3095"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:313717"
                     /db_xref="RGD:1306458"
ORIGIN      
        1 mlrrpapala ravrlllagl lygggvwaar vnkhkpwlep tyhgivtend ntvlldppli
       61 aldkdsplrf aesfevtvtk egeicgfkih gqnvpfdavv vdkstgegii rskekldcel
      121 qkdytftiqa ydcgkgpdgt gvkkshkatv hiqvndvney apvfkeksyk aavvegkqhg
      181 silrveavda dcspqfsqic syeiltpdvp ftvdkdgyik nteklnygke hqykltvtay
      241 dcgkkrated vlvkisvkpt cspgwqgwss rieyepgtga lavfpsihle tcdepvasvq
      301 atveletshi gkgcdrdtys ekslhrlcga aagtsellps psssfnwtvg lptdnghdsd
      361 qvfefngtqa vripdgvvtl dpkepftisv wmrhgpfgrk ketilcssdk tdmnrhhysl
      421 yvhgcrlifl lrqdpseekk yrpaefhwkl nqvcdedwhh fvlnvevpsv tlyvdgvshe
      481 pfsvtedypl hptkietqlv vgacwqggdl hmtqffrgnl agltvrsgkl adkkvidcly
      541 tckegldlqv pedgnrgvqi qtsssqavlt legenvgeld kamqhisyln srqfptpgir
      601 rlkitstvkc fneaacievp pvegyvmvlq peepkislsg vhhfaraase fespegvslf
      661 pelkiistit revepeadga edptvqeslv seeivhdldt cevtvegeel naeqeslevd
      721 varlqqkgie vnhsdlgvvf tgvetmasye evlhllryrn whtrslldrk fklicselng
      781 rylsnefkve vnvihtanpv ehanhmaaqp qfvhpehrsf vdlsghnlas phpfavvpst
      841 atvvivvcvs flvfmiilgv friraahqrt mrdqdtgken emdwddsalt itvnpmetye
      901 dqhsseeeee eeeeeesedg eeeeditsae sesseeeegg pgdgqnttrq qqlewdystl
      961 sy
//
LOCUS       NP_113835                863 aa            linear   ROD 24-MAR-2025
DEFINITION  scm-like with four MBT domains protein 1 [Rattus norvegicus].
ACCESSION   NP_113835
VERSION     NP_113835.2
DBSOURCE    REFSEQ: accession NM_031647.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Zhang,J., Bonasio,R., Strino,F., Kluger,Y., Holloway,J.K.,
            Modzelewski,A.J., Cohen,P.E. and Reinberg,D.
  TITLE     SFMBT1 functions with LSD1 to regulate expression of canonical
            histone genes and chromatin-related factors
  JOURNAL   Genes Dev 27 (7), 749-766 (2013)
   PUBMED   23592795
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Lin,S., Shen,H., Li,J.L., Tang,S., Gu,Y., Chen,Z., Hu,C.,
            Rice,J.C., Lu,J. and Wu,L.
  TITLE     Proteomic and functional analyses reveal the role of chromatin
            reader SFMBT1 in regulating epigenetic silencing and the myogenic
            gene program
  JOURNAL   J Biol Chem 288 (9), 6238-6247 (2013)
   PUBMED   23349461
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Wu,S., Trievel,R.C. and Rice,J.C.
  TITLE     Human SFMBT is a transcriptional repressor protein that selectively
            binds the N-terminal tail of histone H3
  JOURNAL   FEBS Lett 581 (17), 3289-3296 (2007)
   PUBMED   17599839
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   5  (residues 1 to 863)
  AUTHORS   Usui,H., Ichikawa,T., Kobayashi,K. and Kumanishi,T.
  TITLE     Cloning of a novel murine gene Sfmbt, Scm-related gene containing
            four mbt domains, structurally belonging to the Polycomb group of
            genes
  JOURNAL   Gene 248 (1-2), 127-135 (2000)
   PUBMED   10806358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 20, 2007 this sequence version replaced NP_113835.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081770.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..863
                     /product="scm-like with four MBT domains protein 1"
                     /note="Scm-related gene containing four mbt domains"
                     /calculated_mol_wt=97375
     Region          20..120
                     /region_name="MBT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          47..140
                     /region_name="MBT"
                     /note="malignant brain tumor (MBT) repeat; cl45897"
                     /db_xref="CDD:459242"
     Site            order(60,63,66,68,84,87,93)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439080"
     Region          128..232
                     /region_name="MBT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          159..255
                     /region_name="MBT_SFMBT1_rpt2"
                     /note="second malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20113"
                     /db_xref="CDD:439103"
     Site            order(172,175,178,180,196,199,205)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439103"
     Region          242..346
                     /region_name="MBT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          271..364
                     /region_name="MBT_SFMBT1_rpt3"
                     /note="third malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20115"
                     /db_xref="CDD:439105"
     Region          354..451
                     /region_name="MBT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          380..469
                     /region_name="MBT"
                     /note="malignant brain tumor (MBT) repeat; cl45897"
                     /db_xref="CDD:459242"
     Site            order(392,395,398,400,416,419,424)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439080"
     Region          499..614
                     /region_name="SLED"
                     /note="SLED domain; pfam12140"
                     /db_xref="CDD:463469"
     Region          638..773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          779..863
                     /region_name="SAM_Scm-like-4MBT1,2"
                     /note="SAM domain of Scm-like-4MBT1,2 proteins of Polycomb
                     group; cd09581"
                     /db_xref="CDD:188980"
     Site            order(818..820,822..823,826..827,830..831,836)
                     /site_type="other"
                     /note="putative oligomer interface ML [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     Site            order(839..842,844..845,848,851)
                     /site_type="other"
                     /note="putative oligomer interface EH [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     CDS             1..863
                     /gene="Sfmbt1"
                     /gene_synonym="Sfmbt"
                     /coded_by="NM_031647.3:513..3104"
                     /db_xref="GeneID:58967"
                     /db_xref="RGD:61999"
ORIGIN      
        1 mngeqqldad lgsgveveef swedyleetg attapyasfk hvdiclqsgf apgmkleval
       61 rkdpetywva tvitaceqll llryegyged rkadfwcdir raglypigwc qqnkktleap
      121 egirdkvsdw saflqrtltg acgppvalle glrngrnpld liapgsrlec qdfrdsvstw
      181 ivtvvenigg rlklqyegle rhdgfehwly yldpflhhig waaqqgyelq pplairhlkn
      241 eadwqeilar vkeeeplpsy lfkdkqvirt hefsinmkle avdpwspfgi spatiakvfd
      301 dkyflveidd lrpedharrs fvchanspgi fpvqwslkng lhinpppgfr sqdfdwadyl
      361 kqcgaeaapq kcfpqsvseh qfkenmklea vnplfpeevs iatvtavrgs ylwlqlegsk
      421 kpvpefivsv esmnifplgw cetnghplst prrarghklr kiavvqpekq ilssrtvheg
      481 lknqlnsphs vmingkyccp kiyfnhrcfs gpylnkgria elpqcvgpgn cvlvlrevlt
      541 llinaaykps rvlrelqldk dsvwhgcgev lkakykgksy ratveivrta drvtefcrqt
      601 cikleccpnl fgprmvldtc sencsvltkt kythyygkkk nkrigrppgg hsnlscalkk
      661 tskrrkrrkn ifvhkkkrss asvdntpvgs pqgsggeded daddgdddsl tegstseqqd
      721 elheesevse kkscspsptq semstplppd tqtdkreaqt sslsdgenkp pspkeiriev
      781 derlhldsnp lkwsvadvvr firstdcapl arifldqeid gqalllltlp tvqecmdlkl
      841 gpaiklchhi erikfafyeq fan
//
LOCUS       NP_001423812             782 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 9
            [Rattus norvegicus].
ACCESSION   NP_001423812 XP_063131566
VERSION     NP_001423812.1
DBSOURCE    REFSEQ: accession NM_001436883.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131566.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2299230.1,
                                           SRR21887623.1466001.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..782
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 9"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=86136
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..782
                     /gene="Eps15l1"
                     /coded_by="NM_001436883.1:35..2383"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmsks prqeelrvcr hklqkevgsp tcltiqkcpl
      781 sl
//
LOCUS       NP_001102127             577 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform e [Rattus norvegicus].
ACCESSION   NP_001102127 XP_001053893 XP_342809
VERSION     NP_001102127.1
DBSOURCE    REFSEQ: accession NM_001108657.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001053893.1, XP_342809.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.26545.1,
                                           SRR26360172.1727209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..577
                     /product="protein CBFA2T1 isoform e"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=64191
     Region          95..184
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          310..376
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          416..>470
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          488..524
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..577
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001108657.2:381..2114"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 mpdrtekhst mpdspvdvkt qsrltppamp pppttqgapr tssftpttlt ngtshsptal
       61 ngapsppngf sngpssssss slanqqlppa cgarqlsklk rflttlqqfg ndispeiger
      121 vrtlvlglvn stltieefhs klqeatnfpl rpfvipflka nlpllqrell hcarlakqnp
      181 aqylaqheql lldasttspv dssellldvn engkrrtpdr tkengfdrep lhsehpskrp
      241 ctispgqrys pnnglsyqpn glphptpppp qhyrlddmai ahhyrdsyrh pshrdlrdrn
      301 rpmglhgtrq eemidhrltd rewaeewkhl dhllncimdm vektrrsltv lrrcqeadre
      361 elnywirrys daedlkkggs gssshsrqqs pvnpdpvald ahreflhrpa sgyvpeeiwk
      421 kaeeavnevk rqamtelqka vseaerkahd mitterakme rtvaeakrqa aedalavinq
      481 qedssescwn cgrkasetcs gcntarycgs fcqhkdwekh hhicgqtlqa pqqgetpavs
      541 ssvtpssgag spmdtppaat prsttpgtps tiettpr
//
LOCUS       NP_001423832            1907 aa            linear   ROD 24-MAR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase F isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001423832 XP_038966089
VERSION     NP_001423832.1
DBSOURCE    REFSEQ: accession NM_001436903.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1907)
  AUTHORS   Dyck,S., Kataria,H., Akbari-Kelachayeh,K., Silver,J. and
            Karimi-Abdolrezaee,S.
  TITLE     LAR and PTPsigma receptors are negative regulators of
            oligodendrogenesis and oligodendrocyte integrity in spinal cord
            injury
  JOURNAL   Glia 67 (1), 125-145 (2019)
   PUBMED   30394599
  REMARK    GeneRIF: In a spinal cord injury model, blocking LAR and PTPalpha
            receptors promotes oligodendrogenesis.
REFERENCE   2  (residues 1 to 1907)
  AUTHORS   Shijo,T., Warita,H., Suzuki,N., Kitajima,Y., Ikeda,K., Akiyama,T.,
            Ono,H., Mitsuzawa,S., Nishiyama,A., Izumi,R. and Aoki,M.
  TITLE     Aberrant astrocytic expression of chondroitin sulfate proteoglycan
            receptors in a rat model of amyotrophic lateral sclerosis
  JOURNAL   J Neurosci Res 96 (2), 222-233 (2018)
   PUBMED   28752900
  REMARK    GeneRIF: This study showed that astrocytes aberrantly and
            progressively expressed PTPsigma and LAR at the site of motor
            neuron degeneration in Tg ALS model rats with mutant SOD1.
REFERENCE   3  (residues 1 to 1907)
  AUTHORS   Choi,Y., Nam,J., Whitcomb,D.J., Song,Y.S., Kim,D., Jeon,S.,
            Um,J.W., Lee,S.G., Woo,J., Kwon,S.K., Li,Y., Mah,W., Kim,H.M.,
            Ko,J., Cho,K. and Kim,E.
  TITLE     SALM5 trans-synaptically interacts with LAR-RPTPs in a
            splicing-dependent manner to regulate synapse development
  JOURNAL   Sci Rep 6, 26676 (2016)
   PUBMED   27225731
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1907)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
REFERENCE   5  (residues 1 to 1907)
  AUTHORS   Song,Y.S., Lee,H.J., Prosselkov,P., Itohara,S. and Kim,E.
  TITLE     Trans-induced cis interaction in the tripartite NGL-1, netrin-G1
            and LAR adhesion complex promotes development of excitatory
            synapses
  JOURNAL   J Cell Sci 126 (Pt 21), 4926-4938 (2013)
   PUBMED   23986473
REFERENCE   6  (residues 1 to 1907)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Increased abundance of specific skeletal muscle protein-tyrosine
            phosphatases in a genetic model of insulin-resistant obesity and
            diabetes mellitus
  JOURNAL   Metabolism 44 (9), 1175-1184 (1995)
   PUBMED   7666792
REFERENCE   7  (residues 1 to 1907)
  AUTHORS   Ahmad,F., Considine,R.V. and Goldstein,B.J.
  TITLE     Increased abundance of the receptor-type protein-tyrosine
            phosphatase LAR accounts for the elevated insulin receptor
            dephosphorylating activity in adipose tissue of obese human
            subjects
  JOURNAL   J Clin Invest 95 (6), 2806-2812 (1995)
   PUBMED   7769120
REFERENCE   8  (residues 1 to 1907)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Purification, identification and subcellular distribution of three
            predominant protein-tyrosine phosphatase enzymes in skeletal muscle
            tissue
  JOURNAL   Biochim Biophys Acta 1248 (1), 57-69 (1995)
   PUBMED   7711057
REFERENCE   9  (residues 1 to 1907)
  AUTHORS   Pot,D.A., Woodford,T.A., Remboutsika,E., Haun,R.S. and Dixon,J.E.
  TITLE     Cloning, bacterial expression, purification, and characterization
            of the cytoplasmic domain of rat LAR, a receptor-like protein
            tyrosine phosphatase
  JOURNAL   J Biol Chem 266 (29), 19688-19696 (1991)
   PUBMED   1918076
REFERENCE   10 (residues 1 to 1907)
  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.
  TITLE     A new member of the immunoglobulin superfamily that has a
            cytoplasmic region homologous to the leukocyte common antigen
  JOURNAL   J Exp Med 168 (5), 1523-1530 (1988)
   PUBMED   2972792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966089.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19842.1,
                                           SRR26643299.23919.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1907
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1907
                     /product="receptor-type tyrosine-protein phosphatase F
                     isoform 2 precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase F;
                     leukocyte antigen-related (LAR) PTP receptor; leukocyte
                     common antigen related"
                     /calculated_mol_wt=209831
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2941
     Region          33..124
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          136..226
                     /region_name="IgI_2_RPTP_IIa_LAR_like"
                     /note="Second immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F; member of
                     the I-set of IgSF domains; cd05738"
                     /db_xref="CDD:409400"
     Region          136..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409400"
     Region          143..147
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409400"
     Region          150..159
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409400"
     Region          164..170
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409400"
     Region          172..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409400"
     Region          183..187
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409400"
     Region          190..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409400"
     Region          204..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409400"
     Region          214..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409400"
     Region          235..316
                     /region_name="IgI_3_RPTP_IIa_LAR_like"
                     /note="Third immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F (also known
                     as LAR), type IIa; member of the I-set of IgSF domains;
                     cd05739"
                     /db_xref="CDD:409401"
     Region          235..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409401"
     Region          241..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409401"
     Region          248..256
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409401"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          261..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409401"
     Region          269..271
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409401"
     Region          274..278
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409401"
     Region          283..288
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409401"
     Region          288..712
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          295..302
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409401"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          306..315
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409401"
     Region          592..1059
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          693..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            950
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            966
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1264..1284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10586; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          1335..1610
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1612..1902
                     /region_name="R-PTP-F-2"
                     /note="PTP-like domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 2; cd14629"
                     /db_xref="CDD:350477"
     CDS             1..1907
                     /gene="Ptprf"
                     /gene_synonym="LARFN5C"
                     /coded_by="NM_001436903.1:313..6036"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:360406"
                     /db_xref="RGD:3453"
ORIGIN      
        1 mapepapgrr mvplvpalvm lglmagahgd skpvfvkvpe dqiglsggva sfvcqatgep
       61 kpritwmkkg kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa
      121 klsvleedql psgfptidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpass
      181 ngrikqlrsg alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss
      241 qevmpggnvn ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv mrsanytcva
      301 isslgmieat aqvtvkalpk ppidlvvtet tatsvtltwd sgntepvsfy giqyraagtd
      361 gpfqevdgva strysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv
      421 qarmlsastm lvqweppeep nglvrgyrvy ytpdsrrpls awhkhntdag llttvgsllp
      481 gityslrvla ftavgdgpps ptiqvktqqg vpaqpadfqa kaesdtriql swllppqeri
      541 ikyelvywaa edegqqhkvt fdptssytle dlkpdtlyhf qlaarsdlgv gvftptvear
      601 taqstpsapp qkvtcvstgs ttvrvswvpp padsrngiit qysvayeavd gedrkrhvvd
      661 gisrehsswd llglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl
      721 nstavhvswk lpvpnkqhgq irgyqvtyvr lengeprgqp iiqdvmlaea qwrpeesedy
      781 ettisgltpe ttysitvaay ttkgdgarsk pkvvtttgav pgrptmmvst tamhtallqw
      841 hppkelpgel lgyrlqyrra dearpntidf gkddqhftvt glhkgatyif rlaaknragp
      901 geefekeitt pedapsgfpq nlrvtgltts ttelawdppv laerngritn ytvvyrdins
      961 qhelqnvtgd vhltllglkp dttydikvra htskgagpls psiqsqtmpm eqvfaknfrv
     1021 aaamktsvll swevpdsyks avpfkilyng qsvevdghsm rkliadlqpn teysfvlmnr
     1081 gssagglqhl vsirtapdll pqkplpasaf iedgrfslsm pqvqdpslvr wfyivvvpid
     1141 rvggnllapr wstpeeleld elleaieqge ekqrrrrrqa erlkpyvaaq vdelpetftl
     1201 gdkknyrgfy nrplspdlsy qcfvlaslke pmdqkryass pysdeivvqv tpaqqqeepe
     1261 mlwvtgpvla viliilivia illfkrkrth spsskdeqsi glkdsllahs sdpvemrrln
     1321 yqtpgmrdhp pipitdladn ierlkandgl kfsqeyesid pgqqftwens nsevnkpknr
     1381 yanviaydhs rvlltsidgv pgsdyinany idgyrkqnay iatqgplpet mgdfwrmvwe
     1441 qrtatvvmmt rleeksrvkc dqywpargte tygliqvtlv dtvelatytm rtfalhksgs
     1501 sekrelrqfq fmawpdhgvp eyptpilafl rrvkacnpld agpmvvhcsa gvgrtgcfiv
     1561 idamlermkh ektvdiyghv tcmrsqrnym vqtedqyvfi healleaamc ghtevlarnl
     1621 yahiqklgqv ppgesvtame lefkllansk ahtsrfisan lpcnkfknrl vnimpyeltr
     1681 vclqpirgve gsdyinasfl dgyrqqkayi atqgplaest edfwrmlweh nstiivmltk
     1741 lremgrekch qywpaersar yqyfvvdpma eynmpqyilr efkvtdardg qsrtirqfqf
     1801 tdwpeqgvpk tgegfidfig qvhktkeqfg qdgpitvhcs agvgrtgvfi tlsivlermr
     1861 yegvvdmfqt vktlrtqrpa mvqtedqyql cyraaleylg sfdhyat
//
LOCUS       NP_001423843             604 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform a [Rattus norvegicus].
ACCESSION   NP_001423843 XP_008761772
VERSION     NP_001423843.1
DBSOURCE    REFSEQ: accession NM_001436914.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_008761772.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2692079.1,
                                           SRR26360172.2446015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..604
                     /product="protein CBFA2T1 isoform a"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=67376
     Region          122..211
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          337..403
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          443..>497
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          515..551
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..604
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436914.1:210..2024"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 misikrntwr alsvvigdcr kkanfeycqd rtekhstmpd spvdvktqsr ltppampppp
       61 ttqgaprtss ftpttltngt shsptalnga psppngfsng psssssssla nqqlppacga
      121 rqlsklkrfl ttlqqfgndi speigervrt lvlglvnstl tieefhsklq eatnfplrpf
      181 vipflkanlp llqrellhca rlakqnpaqy laqheqllld asttspvdss ellldvneng
      241 krrtpdrtke ngfdreplhs ehpskrpcti spgqryspnn glsyqpnglp hptppppqhy
      301 rlddmaiahh yrdsyrhpsh rdlrdrnrpm glhgtrqeem idhrltdrew aeewkhldhl
      361 lncimdmvek trrsltvlrr cqeadreeln ywirrysdae dlkkggsgss shsrqqspvn
      421 pdpvaldahr eflhrpasgy vpeeiwkkae eavnevkrqa mtelqkavse aerkahdmit
      481 terakmertv aeakrqaaed alavinqqed ssescwncgr kasetcsgcn tarycgsfcq
      541 hkdwekhhhi cgqtlqapqq getpavsssv tpssgagspm dtppaatprs ttpgtpstie
      601 ttpr
//
LOCUS       NP_001423807             798 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 5
            [Rattus norvegicus].
ACCESSION   NP_001423807 XP_017455658
VERSION     NP_001423807.1
DBSOURCE    REFSEQ: accession NM_001436878.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017455658.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.162120.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..798
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 5"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=88069
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <385..>566
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..798
                     /gene="Eps15l1"
                     /coded_by="NM_001436878.1:35..2431"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamvkd
      601 dpfknkallf snnsqelhpd pfqaedpfks dpfkgadpfk gdpfqsdpfs eqqtavtdpf
      661 ggdpfkesdp fhsstsddff kkqtkndpft sdpftknpsl pskldpfess dpfssssiss
      721 kgsdpfgtld pfgsssfssa egfadfsqms kfgneeqqla wakresekae qerlarlrrq
      781 eqedlelaia lskadmpa
//
LOCUS       NP_001423864             164 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform a [Rattus norvegicus].
ACCESSION   NP_001423864 XP_063143974
VERSION     NP_001423864.1
DBSOURCE    REFSEQ: accession NM_001436935.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143974.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.1724433.1,
                                           SRR26360172.1265873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..164
                     /product="C-C motif chemokine 27 isoform a"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=19360
     Region          76..136
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..164
                     /gene="Ccl27"
                     /coded_by="NM_001436935.1:85..579"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerspmpp tsqrlslepp rlpltgwhpw
       61 nktkekqeal plpsstscct qlyrqplptr llrrivrvel qeadgdchlq avvlhltrrs
      121 vcvhpqnrsl arwlerhgkr lqgtlpslnp vlqkkmcpsp qkqk
//
LOCUS       NP_001423834            1600 aa            linear   ROD 24-MAR-2025
DEFINITION  GATOR1 complex protein DEPDC5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423834 XP_063129235
VERSION     NP_001423834.1
DBSOURCE    REFSEQ: accession NM_001436905.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1600)
  AUTHORS   Chen,J., Ou,Y., Yang,Y., Li,W., Xu,Y., Xie,Y. and Liu,Y.
  TITLE     KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
            tumorigenesis and ageing
  JOURNAL   Nature 557 (7706), 585-589 (2018)
   PUBMED   29769719
REFERENCE   2  (residues 1 to 1600)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   3  (residues 1 to 1600)
  AUTHORS   Marsan,E., Ishida,S., Schramm,A., Weckhuysen,S., Muraca,G.,
            Lecas,S., Liang,N., Treins,C., Pende,M., Roussel,D., Le Van
            Quyen,M., Mashimo,T., Kaneko,T., Yamamoto,T., Sakuma,T., Mahon,S.,
            Miles,R., Leguern,E., Charpier,S. and Baulac,S.
  TITLE     Depdc5 knockout rat: A novel model of mTORopathy
  JOURNAL   Neurobiol Dis 89, 180-189 (2016)
   PUBMED   26873552
  REMARK    GeneRIF: DEP-domain containing 5 knockout rats exhibit multiple
            features of rodent models of mechanistic target of rapamycin
            complex 1 (mTOR) mTORopathies, and thus, stand as a relevant model
            to study their underlying pathogenic mechanisms.
REFERENCE   4  (residues 1 to 1600)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   5  (residues 1 to 1600)
  AUTHORS   Bar-Peled,L. and Sabatini,D.M.
  TITLE     Regulation of mTORC1 by amino acids
  JOURNAL   Trends Cell Biol 24 (7), 400-406 (2014)
   PUBMED   24698685
  REMARK    Review article
REFERENCE   6  (residues 1 to 1600)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   7  (residues 1 to 1600)
  AUTHORS   Dibbens,L.M., de Vries,B., Donatello,S., Heron,S.E., Hodgson,B.L.,
            Chintawar,S., Crompton,D.E., Hughes,J.N., Bellows,S.T., Klein,K.M.,
            Callenbach,P.M., Corbett,M.A., Gardner,A.E., Kivity,S., Iona,X.,
            Regan,B.M., Weller,C.M., Crimmins,D., O'Brien,T.J.,
            Guerrero-Lopez,R., Mulley,J.C., Dubeau,F., Licchetta,L.,
            Bisulli,F., Cossette,P., Thomas,P.Q., Gecz,J., Serratosa,J.,
            Brouwer,O.F., Andermann,F., Andermann,E., van den Maagdenberg,A.M.,
            Pandolfo,M., Berkovic,S.F. and Scheffer,I.E.
  TITLE     Mutations in DEPDC5 cause familial focal epilepsy with variable
            foci
  JOURNAL   Nat Genet 45 (5), 546-551 (2013)
   PUBMED   23542697
REFERENCE   8  (residues 1 to 1600)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063129235.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.55086.1,
                                           SRR26360181.2667518.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1600
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1600
                     /product="GATOR1 complex protein DEPDC5 isoform 2"
                     /note="DEP domain-containing protein 5; GATOR complex
                     protein DEPDC5; GATOR1 complex protein DEPDC5"
                     /calculated_mol_wt=180891
     Region          101..381
                     /region_name="IML1"
                     /note="Vacuolar membrane-associated protein Iml1;
                     pfam12257"
                     /db_xref="CDD:463510"
     Region          1176..1257
                     /region_name="DEP_DEPDC5-like"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in DEPDC5-like proteins. DEPDC5, in human also known
                     as KIAA0645, is a DEP domain containing protein of unknown
                     function; cd04449"
                     /db_xref="CDD:239896"
     Region          1275..1582
                     /region_name="DEPDC5_CTD"
                     /note="DEPDC5 protein C-terminal region; pfam19418"
                     /db_xref="CDD:466071"
     CDS             1..1600
                     /gene="Depdc5"
                     /coded_by="NM_001436905.1:103..4905"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305464"
                     /db_xref="RGD:1311535"
ORIGIN      
        1 mrttkvyklv ihkkgfggsd delvvnpkvf phiklgdive iahpndeysp lllqvkslke
       61 dlqketisvd qtvtqvfrlr pyqdvyvnvv dpkdvtldlv eltfkdqyig rgdmwrlkks
      121 lvstcayitq kvefagiraq agelwvknek vmcgyiseet rvvfrstsam vyifiqmsce
      181 mwdfdiygdl yfekavngfl adlftkwkek ncshevtvvl fsrtfydaks idefpevnra
      241 siqqdhkgrf yedfykvvvq nerreewtsl lvtikklfiq ypvlvrleqa ggfpqgdnst
      301 saqgnyleai nlsfnvfdkh yinrnfdrtg qmsvvitpgv gvfevdrllm iltkqrmidn
      361 gigvdlvcmg eqplhavplf klhnrsvprd srlgddynip hwinhsfyts ksqlfcnsft
      421 priklagkks atektkngrd tslgapkese ntlpiqvdyd aydaqvfrlp gpsraqrlat
      481 crsvreqenh nrksasscdv ssspslpsra lpteevrsqa sddsslgkst nilmipnphl
      541 hqyevssslg ytstrdvlen mieppqrdss apgrfhvgsa esmlhvrpgg ytpqralinp
      601 fapsrmpmkl tsnrrrwmht fpvgpsgeai qihhqtrqnm aelqgsrqrd pthssaelle
      661 layheaagrh stsrqpgdsm slnfsgteel svsllsnsgt gmnprnqnkd sledgvstsp
      721 dpiltlsapp vvpgfcctvg vdwkslttpa clplttdyfp drqglqndyt egcydllpea
      781 dmdrrdeegv qmtaqqvfee ficqrlmqgy qiivqpktqk psttvpppls ssplysrglv
      841 srnrpeeegq ywlsmgrtfh kvtlkdkmit vtrylpkypy esaqihytys lcpshsdsef
      901 vscwvefche rleeykwnyl dqyicsagse dfslieslkf wrtrflllpa cvtatkrite
      961 gevhcdiygd kpradedewq lldgfirfve glnrirrrhr sdrmirkgta mkglqmtgpi
     1021 sahslestgp pvgkkgtsal sallemeasq kslgeqqtsv hgksstqpae nssvamtpty
     1081 vdsprkdgaf fmefvrsprt assafypqas vdqtaplvld stslgvstcq svdrgnnqtf
     1141 gnsqnieqaf pstgsgdgss qqhiasslts sstlveilea mkhpstgvql lseqkglspc
     1201 cfisaevvhw lmnnvegvqt qamgidimqk mleeqliaha sgeawrtfvy gfyfykivtd
     1261 repervamqq psapwhtagv ddfasfqrkw fevafvaeel vhseipafll pwlpsrpasy
     1321 asrhssfsrs fggrsqaaal laatvpeqrt vtldvdvnnr tdrlewcscy yhgnfslnaa
     1381 feiklhwmav tatvlfemvq gwhrkatscg fllvpvlegp falpsylygd plraqlfipl
     1441 nlgcllkegs ehlfdsfepe tywdrmhlfq eaiahrfgfv qdkysasafn fpaenkpqyi
     1501 hvtgtvflql pyskrkfsgq qrrrrnstss tnqnmfceer vgynwayntm ltktwrssat
     1561 gdekfadrll kdftdfcinr dnrlvtfwtn clekmhasap
//
LOCUS       NP_001423820             601 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 17
            [Rattus norvegicus].
ACCESSION   NP_001423820
VERSION     NP_001423820.1
DBSOURCE    REFSEQ: accession NM_001436891.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50080.1,
                                           SRR26643298.70772.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..601
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 17"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=66212
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <385..>566
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..601
                     /gene="Eps15l1"
                     /coded_by="NM_001436891.1:35..1840"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamvkv
      601 e
//
LOCUS       NP_001423844             604 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform a [Rattus norvegicus].
ACCESSION   NP_001423844
VERSION     NP_001423844.1
DBSOURCE    REFSEQ: accession NM_001436915.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2232071.1,
                                           SRR26360176.736893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..604
                     /product="protein CBFA2T1 isoform a"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=67376
     Region          122..211
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          337..403
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          443..>497
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          515..551
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..604
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436915.1:480..2294"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 misikrntwr alsvvigdcr kkanfeycqd rtekhstmpd spvdvktqsr ltppampppp
       61 ttqgaprtss ftpttltngt shsptalnga psppngfsng psssssssla nqqlppacga
      121 rqlsklkrfl ttlqqfgndi speigervrt lvlglvnstl tieefhsklq eatnfplrpf
      181 vipflkanlp llqrellhca rlakqnpaqy laqheqllld asttspvdss ellldvneng
      241 krrtpdrtke ngfdreplhs ehpskrpcti spgqryspnn glsyqpnglp hptppppqhy
      301 rlddmaiahh yrdsyrhpsh rdlrdrnrpm glhgtrqeem idhrltdrew aeewkhldhl
      361 lncimdmvek trrsltvlrr cqeadreeln ywirrysdae dlkkggsgss shsrqqspvn
      421 pdpvaldahr eflhrpasgy vpeeiwkkae eavnevkrqa mtelqkavse aerkahdmit
      481 terakmertv aeakrqaaed alavinqqed ssescwncgr kasetcsgcn tarycgsfcq
      541 hkdwekhhhi cgqtlqapqq getpavsssv tpssgagspm dtppaatprs ttpgtpstie
      601 ttpr
//
LOCUS       NP_001423867             120 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform c [Rattus norvegicus].
ACCESSION   NP_001423867
VERSION     NP_001423867.1
DBSOURCE    REFSEQ: accession NM_001436938.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 120)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 120)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 120)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.190457.1,
                                           SRR26360194.1854877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN12840124
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..120
                     /product="C-C motif chemokine 27 isoform c"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=13997
     Region          32..92
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..120
                     /gene="Ccl27"
                     /coded_by="NM_001436938.1:51..413"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 mwrrerrlpl tgwhpwnktk ekqealplps stscctqlyr qplptrllrr ivrvelqead
       61 gdchlqavvl hltrrsvcvh pqnrslarwl erhgkrlqgt lpslnpvlqk kmcpspqkqk
//
LOCUS       NP_001423866             149 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform b [Rattus norvegicus].
ACCESSION   NP_001423866
VERSION     NP_001423866.1
DBSOURCE    REFSEQ: accession NM_001436937.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 149)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 149)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 149)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB715300.1, SRR26360186.437627.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..149
                     /product="C-C motif chemokine 27 isoform b"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=17741
     Region          61..121
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..149
                     /gene="Ccl27"
                     /coded_by="NM_001436937.1:93..542"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerrlplt gwhpwnktke kqealplpss
       61 tscctqlyrq plptrllrri vrvelqeadg dchlqavvlh ltrrsvcvhp qnrslarwle
      121 rhgkrlqgtl pslnpvlqkk mcpspqkqk
//
LOCUS       NP_001423833            1705 aa            linear   ROD 24-MAR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase F isoform 4 precursor
            [Rattus norvegicus].
ACCESSION   NP_001423833 XP_063143947
VERSION     NP_001423833.1
DBSOURCE    REFSEQ: accession NM_001436904.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1705)
  AUTHORS   Dyck,S., Kataria,H., Akbari-Kelachayeh,K., Silver,J. and
            Karimi-Abdolrezaee,S.
  TITLE     LAR and PTPsigma receptors are negative regulators of
            oligodendrogenesis and oligodendrocyte integrity in spinal cord
            injury
  JOURNAL   Glia 67 (1), 125-145 (2019)
   PUBMED   30394599
  REMARK    GeneRIF: In a spinal cord injury model, blocking LAR and PTPalpha
            receptors promotes oligodendrogenesis.
REFERENCE   2  (residues 1 to 1705)
  AUTHORS   Shijo,T., Warita,H., Suzuki,N., Kitajima,Y., Ikeda,K., Akiyama,T.,
            Ono,H., Mitsuzawa,S., Nishiyama,A., Izumi,R. and Aoki,M.
  TITLE     Aberrant astrocytic expression of chondroitin sulfate proteoglycan
            receptors in a rat model of amyotrophic lateral sclerosis
  JOURNAL   J Neurosci Res 96 (2), 222-233 (2018)
   PUBMED   28752900
  REMARK    GeneRIF: This study showed that astrocytes aberrantly and
            progressively expressed PTPsigma and LAR at the site of motor
            neuron degeneration in Tg ALS model rats with mutant SOD1.
REFERENCE   3  (residues 1 to 1705)
  AUTHORS   Choi,Y., Nam,J., Whitcomb,D.J., Song,Y.S., Kim,D., Jeon,S.,
            Um,J.W., Lee,S.G., Woo,J., Kwon,S.K., Li,Y., Mah,W., Kim,H.M.,
            Ko,J., Cho,K. and Kim,E.
  TITLE     SALM5 trans-synaptically interacts with LAR-RPTPs in a
            splicing-dependent manner to regulate synapse development
  JOURNAL   Sci Rep 6, 26676 (2016)
   PUBMED   27225731
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1705)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
REFERENCE   5  (residues 1 to 1705)
  AUTHORS   Song,Y.S., Lee,H.J., Prosselkov,P., Itohara,S. and Kim,E.
  TITLE     Trans-induced cis interaction in the tripartite NGL-1, netrin-G1
            and LAR adhesion complex promotes development of excitatory
            synapses
  JOURNAL   J Cell Sci 126 (Pt 21), 4926-4938 (2013)
   PUBMED   23986473
REFERENCE   6  (residues 1 to 1705)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Increased abundance of specific skeletal muscle protein-tyrosine
            phosphatases in a genetic model of insulin-resistant obesity and
            diabetes mellitus
  JOURNAL   Metabolism 44 (9), 1175-1184 (1995)
   PUBMED   7666792
REFERENCE   7  (residues 1 to 1705)
  AUTHORS   Ahmad,F., Considine,R.V. and Goldstein,B.J.
  TITLE     Increased abundance of the receptor-type protein-tyrosine
            phosphatase LAR accounts for the elevated insulin receptor
            dephosphorylating activity in adipose tissue of obese human
            subjects
  JOURNAL   J Clin Invest 95 (6), 2806-2812 (1995)
   PUBMED   7769120
REFERENCE   8  (residues 1 to 1705)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Purification, identification and subcellular distribution of three
            predominant protein-tyrosine phosphatase enzymes in skeletal muscle
            tissue
  JOURNAL   Biochim Biophys Acta 1248 (1), 57-69 (1995)
   PUBMED   7711057
REFERENCE   9  (residues 1 to 1705)
  AUTHORS   Pot,D.A., Woodford,T.A., Remboutsika,E., Haun,R.S. and Dixon,J.E.
  TITLE     Cloning, bacterial expression, purification, and characterization
            of the cytoplasmic domain of rat LAR, a receptor-like protein
            tyrosine phosphatase
  JOURNAL   J Biol Chem 266 (29), 19688-19696 (1991)
   PUBMED   1918076
REFERENCE   10 (residues 1 to 1705)
  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.
  TITLE     A new member of the immunoglobulin superfamily that has a
            cytoplasmic region homologous to the leukocyte common antigen
  JOURNAL   J Exp Med 168 (5), 1523-1530 (1988)
   PUBMED   2972792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143947.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19845.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1705
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1705
                     /product="receptor-type tyrosine-protein phosphatase F
                     isoform 4 precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase F;
                     leukocyte antigen-related (LAR) PTP receptor; leukocyte
                     common antigen related"
                     /calculated_mol_wt=187208
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2941
     Region          33..124
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          136..226
                     /region_name="IgI_2_RPTP_IIa_LAR_like"
                     /note="Second immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F; member of
                     the I-set of IgSF domains; cd05738"
                     /db_xref="CDD:409400"
     Region          136..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409400"
     Region          143..147
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409400"
     Region          150..159
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409400"
     Region          164..170
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409400"
     Region          172..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409400"
     Region          183..187
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409400"
     Region          190..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409400"
     Region          204..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409400"
     Region          214..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409400"
     Region          235..316
                     /region_name="IgI_3_RPTP_IIa_LAR_like"
                     /note="Third immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F (also known
                     as LAR), type IIa; member of the I-set of IgSF domains;
                     cd05739"
                     /db_xref="CDD:409401"
     Region          235..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409401"
     Region          241..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409401"
     Region          248..256
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409401"
     Region          261..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409401"
     Region          269..271
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409401"
     Region          274..278
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409401"
     Region          283..288
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409401"
     Region          288..712
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          295..302
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409401"
     Region          306..315
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409401"
     Region          710..807
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(796..797,799..800)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          814..>873
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          1133..1408
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1410..1700
                     /region_name="R-PTP-F-2"
                     /note="PTP-like domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 2; cd14629"
                     /db_xref="CDD:350477"
     CDS             1..1705
                     /gene="Ptprf"
                     /gene_synonym="LARFN5C"
                     /coded_by="NM_001436904.1:313..5430"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:360406"
                     /db_xref="RGD:3453"
ORIGIN      
        1 mapepapgrr mvplvpalvm lglmagahgd skpvfvkvpe dqiglsggva sfvcqatgep
       61 kpritwmkkg kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa
      121 klsvleedql psgfptidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpass
      181 ngrikqlrsg alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss
      241 qevmpggnvn ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv mrsanytcva
      301 isslgmieat aqvtvkalpk ppidlvvtet tatsvtltwd sgntepvsfy giqyraagtd
      361 gpfqevdgva strysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv
      421 qarmlsastm lvqweppeep nglvrgyrvy ytpdsrrpls awhkhntdag llttvgsllp
      481 gityslrvla ftavgdgpps ptiqvktqqg vpaqpadfqa kaesdtriql swllppqeri
      541 ikyelvywaa edegqqhkvt fdptssytle dlkpdtlyhf qlaarsdlgv gvftptvear
      601 taqstpsapp qkvtcvstgs ttvrvswvpp padsrngiit qysvayeavd gedrkrhvvd
      661 gisrehsswd llglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl
      721 nstavhvswk lpvpnkqhgq irgyqvtyvr lengeprgqp iiqdvmlaea qettisgltp
      781 ettysitvaa yttkgdgars kpkvvtttga vfaknfrvaa amktsvllsw evpdsyksav
      841 pfkilyngqs vevdghsmrk liadlqpnte ysfvlmnrgs sagglqhlvs irtapdllpq
      901 kplpasafie dgrfslsmpq vqdpslvrwf yivvvpidrv ggnllaprws tpeeleldel
      961 leaieqgeek qrrrrrqaer lkpyvaaqvd elpetftlgd kknyrgfynr plspdlsyqc
     1021 fvlaslkepm dqkryasspy sdeivvqvtp aqqqeepeml wvtgpvlavi liiliviail
     1081 lfkrkrthsp sskdeqsigl kdsllahssd pvemrrlnyq tpgmrdhppi pitdladnie
     1141 rlkandglkf sqeyesidpg qqftwensns evnkpknrya nviaydhsrv lltsidgvpg
     1201 sdyinanyid gyrkqnayia tqgplpetmg dfwrmvweqr tatvvmmtrl eeksrvkcdq
     1261 ywpargtety gliqvtlvdt velatytmrt falhksgsse krelrqfqfm awpdhgvpey
     1321 ptpilaflrr vkacnpldag pmvvhcsagv grtgcfivid amlermkhek tvdiyghvtc
     1381 mrsqrnymvq tedqyvfihe alleaamcgh tevlarnlya hiqklgqvpp gesvtamele
     1441 fkllanskah tsrfisanlp cnkfknrlvn impyeltrvc lqpirgvegs dyinasfldg
     1501 yrqqkayiat qgplaested fwrmlwehns tiivmltklr emgrekchqy wpaersaryq
     1561 yfvvdpmaey nmpqyilref kvtdardgqs rtirqfqftd wpeqgvpktg egfidfigqv
     1621 hktkeqfgqd gpitvhcsag vgrtgvfitl sivlermrye gvvdmfqtvk tlrtqrpamv
     1681 qtedqyqlcy raaleylgsf dhyat
//
LOCUS       NP_001423847             584 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform d [Rattus norvegicus].
ACCESSION   NP_001423847 XP_006237966
VERSION     NP_001423847.1
DBSOURCE    REFSEQ: accession NM_001436918.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006237966.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.14727.1,
                                           SRR26643299.22048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..584
                     /product="protein CBFA2T1 isoform d"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=64986
     Region          102..191
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          317..383
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          423..>477
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          495..531
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..584
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436918.1:343..2097"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 mvglfslvqy rtekhstmpd spvdvktqsr ltppampppp ttqgaprtss ftpttltngt
       61 shsptalnga psppngfsng psssssssla nqqlppacga rqlsklkrfl ttlqqfgndi
      121 speigervrt lvlglvnstl tieefhsklq eatnfplrpf vipflkanlp llqrellhca
      181 rlakqnpaqy laqheqllld asttspvdss ellldvneng krrtpdrtke ngfdreplhs
      241 ehpskrpcti spgqryspnn glsyqpnglp hptppppqhy rlddmaiahh yrdsyrhpsh
      301 rdlrdrnrpm glhgtrqeem idhrltdrew aeewkhldhl lncimdmvek trrsltvlrr
      361 cqeadreeln ywirrysdae dlkkggsgss shsrqqspvn pdpvaldahr eflhrpasgy
      421 vpeeiwkkae eavnevkrqa mtelqkavse aerkahdmit terakmertv aeakrqaaed
      481 alavinqqed ssescwncgr kasetcsgcn tarycgsfcq hkdwekhhhi cgqtlqapqq
      541 getpavsssv tpssgagspm dtppaatprs ttpgtpstie ttpr
//
LOCUS       NP_001423781             553 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423781 XP_038965990
VERSION     NP_001423781.1
DBSOURCE    REFSEQ: accession NM_001436852.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038965990.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16713.1,
                                           SRR26643429.21496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..553
                     /product="heterochromatin protein 1-binding protein 3
                     isoform a"
                     /calculated_mol_wt=60676
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          30..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          155..239
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            order(162,174,206,220)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3TEA8; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            201..212
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          231..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          253..257
                     /region_name="PxVxL motif.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          264..324
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          340..407
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          422..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          <469..>543
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..553
                     /gene="Hp1bp3"
                     /coded_by="NM_001436852.1:132..1793"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 matdmsqgel ihpkalpliv gaqlihadkl gekaddstmp irravnstre tppksklaeg
       61 eeekpepdgs seesistvee penetppaps reaeqpkgep esgekeesks aeetkkeekd
      121 qskekekkvk ktipawatls asqlaraqkq tpmassprpk mdailteaik acfqksgasv
      181 vairkyiihk ypsldlerrg yllkqalkre lnrgvikqvk gkgasgsfvv vqksktpqks
      241 knrkkgsavd pepqvkledv lplaftrlce pkeasyslir kyvsqyypkl rvdirpqllk
      301 nalqraverg qleqitgkga sgtfqlkksg ekpllggslm eyailsaiaa mnepktcstt
      361 alkkyvlenh pgtnsnyqmh llkktlqkce kngwleqisg kgfsgtfqlc fpyypspgvl
      421 fpkkvsdgse dedeeedeee ssedsedeep ppkrslqkkt pakpqgktas mkqrgakpar
      481 kvpaaqrgkv rplpkkappk aktparkgrp apsavkkpsg stskkpvana rkeaklpgkg
      541 ksamkkksfk tkk
//
LOCUS       NP_001423800             971 aa            linear   ROD 24-MAR-2025
DEFINITION  calsyntenin-1 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423800 XP_038966029
VERSION     NP_001423800.1
DBSOURCE    REFSEQ: accession NM_001436871.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Zhou,F., Hu,R., Wang,Y., Wu,X., Chen,X., Xi,Z. and Zeng,K.
  TITLE     Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models
  JOURNAL   Synapse 78 (5), e22307 (2024)
   PUBMED   39171546
  REMARK    GeneRIF: Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models.
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Ster,J., Steuble,M., Orlando,C., Diep,T.M., Akhmedov,A.,
            Raineteau,O., Pernet,V., Sonderegger,P. and Gerber,U.
  TITLE     Calsyntenin-1 regulates targeting of dendritic NMDA receptors and
            dendritic spine maturation in CA1 hippocampal pyramidal cells
            during postnatal development
  JOURNAL   J Neurosci 34 (26), 8716-8727 (2014)
   PUBMED   24966372
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 971)
  AUTHORS   Vagnoni,A., Perkinton,M.S., Gray,E.H., Francis,P.T., Noble,W. and
            Miller,C.C.
  TITLE     Calsyntenin-1 mediates axonal transport of the amyloid precursor
            protein and regulates Abeta production
  JOURNAL   Hum Mol Genet 21 (13), 2845-2854 (2012)
   PUBMED   22434822
  REMARK    GeneRIF: findings show that amyloid precursor protein (APP) and
            calsyntenin-1 are co-transported through axons, that loss of
            calsyntenin-1 disrupts axonal transport of APP and that
            calsyntenin-1 loss also leads to altered APP processing and
            increased production of Abeta
REFERENCE   6  (residues 1 to 971)
  AUTHORS   Araki,Y., Kawano,T., Taru,H., Saito,Y., Wada,S., Miyamoto,K.,
            Kobayashi,H., Ishikawa,H.O., Ohsugi,Y., Yamamoto,T., Matsuno,K.,
            Kinjo,M. and Suzuki,T.
  TITLE     The novel cargo Alcadein induces vesicle association of kinesin-1
            motor components and activates axonal transport
  JOURNAL   EMBO J 26 (6), 1475-1486 (2007)
   PUBMED   17332754
REFERENCE   7  (residues 1 to 971)
  AUTHORS   Konecna,A., Frischknecht,R., Kinter,J., Ludwig,A., Steuble,M.,
            Meskenaite,V., Indermuhle,M., Engel,M., Cen,C., Mateos,J.M.,
            Streit,P. and Sonderegger,P.
  TITLE     Calsyntenin-1 docks vesicular cargo to kinesin-1
  JOURNAL   Mol Biol Cell 17 (8), 3651-3663 (2006)
   PUBMED   16760430
  REMARK    GeneRIF: Calsyntenin-1 links a certain type of vesicular and
            tubulovesicular organelles to the Kinesin-1 motor.
REFERENCE   8  (residues 1 to 971)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
REFERENCE   9  (residues 1 to 971)
  AUTHORS   Araki,Y., Tomita,S., Yamaguchi,H., Miyagi,N., Sumioka,A., Kirino,Y.
            and Suzuki,T.
  TITLE     Novel cadherin-related membrane proteins, Alcadeins, enhance the
            X11-like protein-mediated stabilization of amyloid beta-protein
            precursor metabolism
  JOURNAL   J Biol Chem 278 (49), 49448-49458 (2003)
   PUBMED   12972431
REFERENCE   10 (residues 1 to 971)
  AUTHORS   Vogt,L., Schrimpf,S.P., Meskenaite,V., Frischknecht,R., Kinter,J.,
            Leone,D.P., Ziegler,U. and Sonderegger,P.
  TITLE     Calsyntenin-1, a proteolytically processed postsynaptic membrane
            protein with a cytoplasmic calcium-binding domain
  JOURNAL   Mol Cell Neurosci 17 (1), 151-166 (2001)
   PUBMED   11161476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966029.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21973.1,
                                           SRR26643297.21146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..971
                     /product="calsyntenin-1 isoform 2 precursor"
                     /note="alc-alpha; alcadein-alpha"
                     /calculated_mol_wt=105257
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2963
     Region          41..149
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(48..49,107,109,146,148..149)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          158..248
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          355..>467
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          556..908
                     /region_name="CLSTN_C"
                     /note="Calsyntenin C-terminal; pfam19699"
                     /db_xref="CDD:466150"
     Site            814..815
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     mat_peptide     816..971
                     /product="CTF1-alpha. /evidence=ECO:0000250.
                     /id=PRO_0000323603"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
                     /calculated_mol_wt=17625
     Site            843..844
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Site            850..870
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     Region          905..971
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q0N0.1)"
     CDS             1..971
                     /gene="Clstn1"
                     /coded_by="NM_001436871.1:207..3122"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:313717"
                     /db_xref="RGD:1306458"
ORIGIN      
        1 mlrrpapala ravrlllagl lygggvwaar vnkhkpwlep tyhgivtend ntvlldppli
       61 aldkdsplrf ageicgfkih gqnvpfdavv vdkstgegii rskekldcel qkdytftiqa
      121 ydcgkgpdgt gvkkshkatv hiqvndvney apvfkeksyk aavvegkqhg silrveavda
      181 dcspqfsqic syeiltpdvp ftvdkdgyik nteklnygke hqykltvtay dcgkkrated
      241 vlvkisvkpt cspgwqgwss rieyepgtga lavfpsihle tcdepvasvq atveletshi
      301 gkgcdrdtys ekslhrlcga aagtsellps psssfnwtvg lptdnghdsd qvfefngtqa
      361 vripdgvvtl dpkepftisv wmrhgpfgrk ketilcssdk tdmnrhhysl yvhgcrlifl
      421 lrqdpseekk yrpaefhwkl nqvcdedwhh fvlnvevpsv tlyvdgvshe pfsvtedypl
      481 hptkietqlv vgacwqeysg vesgnetepv tmasaggdlh mtqffrgnla gltvrsgkla
      541 dkkvidclyt ckegldlqvp edgnrgvqiq tsssqavltl egenvgeldk amqhisylns
      601 rqfptpgirr lkitstvkcf neaacievpp vegyvmvlqp eepkislsgv hhfaraasef
      661 espegvslfp elkiistitr evepeadgae dptvqeslvs eeivhdldtc evtvegeeln
      721 aeqeslevdv arlqqkgiev nhsdlgvvft gvetmasyee vlhllryrnw htrslldrkf
      781 klicselngr ylsnefkvev nvihtanpve hanhmaaqpq fvhpehrsfv dlsghnlasp
      841 hpfavvpsta tvvivvcvsf lvfmiilgvf riraahqrtm rdqdtgkene mdwddsalti
      901 tvnpmetyed qhsseeeeee eeeeesedge eeeditsaes esseeeeggp gdgqnttrqq
      961 qlewdystls y
//
LOCUS       NP_001423839             525 aa            linear   ROD 24-MAR-2025
DEFINITION  thymocyte selection-associated high mobility group box protein TOX
            [Rattus norvegicus].
ACCESSION   NP_001423839 XP_017448956
VERSION     NP_001423839.1
DBSOURCE    REFSEQ: accession NM_001436910.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Artegiani,B., de Jesus Domingues,A.M., Bragado Alonso,S.,
            Brandl,E., Massalini,S., Dahl,A. and Calegari,F.
  TITLE     Tox: a multifunctional transcription factor and novel regulator of
            mammalian corticogenesis
  JOURNAL   EMBO J 34 (7), 896-910 (2015)
   PUBMED   25527292
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Yun,S., Lee,S.H., Yoon,S.R., Kim,M.S., Piao,Z.H., Myung,P.K.,
            Kim,T.D., Jung,H. and Choi,I.
  TITLE     TOX regulates the differentiation of human natural killer cells
            from hematopoietic stem cells in vitro
  JOURNAL   Immunol Lett 136 (1), 29-36 (2011)
   PUBMED   21126536
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Aliahmad,P., de la Torre,B. and Kaye,J.
  TITLE     Shared dependence on the DNA-binding factor TOX for the development
            of lymphoid tissue-inducer cell and NK cell lineages
  JOURNAL   Nat Immunol 11 (10), 945-952 (2010)
   PUBMED   20818394
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Aliahmad,P. and Kaye,J.
  TITLE     Development of all CD4 T lineages requires nuclear factor TOX
  JOURNAL   J Exp Med 205 (1), 245-256 (2008)
   PUBMED   18195075
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Aliahmad,P., O'Flaherty,E., Han,P., Goularte,O.D., Wilkinson,B.,
            Satake,M., Molkentin,J.D. and Kaye,J.
  TITLE     TOX provides a link between calcineurin activation and CD8 lineage
            commitment
  JOURNAL   J Exp Med 199 (8), 1089-1099 (2004)
   PUBMED   15078895
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Wilkinson,B., Chen,J.Y., Han,P., Rufner,K.M., Goularte,O.D. and
            Kaye,J.
  TITLE     TOX: an HMG box protein implicated in the regulation of thymocyte
            selection
  JOURNAL   Nat Immunol 3 (3), 272-280 (2002)
   PUBMED   11850626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017448956.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1602773.1,
                                           SRR26360190.1790262.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..525
                     /product="thymocyte selection-associated high mobility
                     group box protein TOX"
                     /note="thymocyte selection-associated HMG box"
                     /calculated_mol_wt=57155
     Region          262..331
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(262..263,265..269,272..273,280,292..293,296,
                     299..300,307,311,314,318,321)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..525
                     /gene="Tox"
                     /coded_by="NM_001436910.1:161..1738"
                     /db_xref="GeneID:362481"
                     /db_xref="RGD:1310455"
ORIGIN      
        1 mdvrfypppa qpaaapaapc lgpspcldpy ycnkfdgenm ymsmtepsqd yvpvsqsypg
       61 pslesedfni ppitppslpd hslvhlneve sgyhslchpm nhngllpfhp qnmdlpeitv
      121 snmlgqdgtl lsnsisvmqe ignaegaqys shpqlaamrp rgqptdlrqq asmmqhgqlt
      181 tinqsqlsaq lglnmggtnv phnspsppgs ksatpspsss vhedecedts kinggekrpa
      241 sdmgkkpktp kkkkkkdpne pqkpvsayal ffrdtqaaik gqnpnatfge vskivasmwd
      301 glgeeqkqvy kkkteaakke ylkqlaayra slvsksyndp vdvktsqppq lvnskpsvfh
      361 gpsqahsaly lsshyhqqpg mtpqltamhp slprniapkp nnqmpvtvsi anmavspppp
      421 lqispplhqh lsmqqhqplv qqplasqlpm qvqtalhspt mqqgftlqpd yqtiinptst
      481 aaqvvtqame yvrsgcrnpp pqpvdwstdy cssggmqrdk alylt
//
LOCUS       NP_001423829             277 aa            linear   ROD 24-MAR-2025
DEFINITION  caspase-3 [Rattus norvegicus].
ACCESSION   NP_001423829
VERSION     NP_001423829.1
DBSOURCE    REFSEQ: accession NM_001436900.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Niedermeyer,S., Yun,X., Trujillo,M., Jiang,H., Andrade,M.R.,
            Kolb,T.M., Suresh,K., Damarla,M. and Shimoda,L.A.
  TITLE     A novel interaction between aquaporin 1 and caspase-3 in pulmonary
            arterial smooth muscle cells
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 326 (5), L638-L645 (2024)
   PUBMED   38375595
  REMARK    GeneRIF: A novel interaction between aquaporin 1 and caspase-3 in
            pulmonary arterial smooth muscle cells.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Holota,R., Decmanova,V., Alexovic Matiasova,A., Kosuth,J.,
            Slovinska,L., Pacut,L., Tomori,Z., Daxnerova,Z. and Sevc,J.
  TITLE     Cleaved caspase-3 is present in the majority of glial cells in the
            intact rat spinal cord during postnatal life
  JOURNAL   Histochem Cell Biol 161 (3), 269-286 (2024)
   PUBMED   37938347
  REMARK    GeneRIF: Cleaved caspase-3 is present in the majority of glial
            cells in the intact rat spinal cord during postnatal life.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Tan,W., Li,Y., Ma,L., Fu,X., Long,Q., Yan,F., Li,W., Liu,X.,
            Ding,H., Wang,Y. and Zhang,W.
  TITLE     Exosomes of endothelial progenitor cells repair injured vascular
            endothelial cells through the Bcl2/Bax/Caspase-3 pathway
  JOURNAL   Sci Rep 14 (1), 4465 (2024)
   PUBMED   38396011
  REMARK    GeneRIF: Exosomes of endothelial progenitor cells repair injured
            vascular endothelial cells through the Bcl2/Bax/Caspase-3 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Galichanin,K. and Yu,Z.
  TITLE     Expression of active caspase 3 in the rat lens after in vivo
            exposure to subthreshold dose of UVR-B
  JOURNAL   BMC Ophthalmol 24 (1), 29 (2024)
   PUBMED   38254051
  REMARK    GeneRIF: Expression of active caspase 3 in the rat lens after in
            vivo exposure to subthreshold dose of UVR-B.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Li,C., Zhang,H., Mo,J., Zuo,J. and Ye,L.
  TITLE     Caspase-3/GSDME dependent pyroptosis contributes to offspring lung
            injury induced by gestational PFOS exposure via PERK/ATF4 signaling
  JOURNAL   Arch Toxicol 98 (1), 207-221 (2024)
   PUBMED   37955688
  REMARK    GeneRIF: Caspase-3/GSDME dependent pyroptosis contributes to
            offspring lung injury induced by gestational PFOS exposure via
            PERK/ATF4 signaling.
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Vito,P., Ghayur,T. and D'Adamio,L.
  TITLE     Generation of anti-apoptotic presenilin-2 polypeptides by
            alternative transcription, proteolysis, and caspase-3 cleavage
  JOURNAL   J Biol Chem 272 (45), 28315-28320 (1997)
   PUBMED   9353287
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Ni,B., Wu,X., Du,Y., Su,Y., Hamilton-Byrd,E., Rockey,P.K.,
            Rosteck,P. Jr., Poirier,G.G. and Paul,S.M.
  TITLE     Cloning and expression of a rat brain interleukin-1beta-converting
            enzyme (ICE)-related protease (IRP) and its possible role in
            apoptosis of cultured cerebellar granule neurons
  JOURNAL   J Neurosci 17 (5), 1561-1569 (1997)
   PUBMED   9030616
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Juan,T.S., McNiece,I.K., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.
            and Fletcher,F.A.
  TITLE     Molecular characterization of mouse and rat CPP32 beta gene
            encoding a cysteine protease resembling interleukin-1 beta
            converting enzyme and CED-3
  JOURNAL   Oncogene 13 (4), 749-755 (1996)
   PUBMED   8761296
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Liu,X., Kim,C.N., Yang,J., Jemmerson,R. and Wang,X.
  TITLE     Induction of apoptotic program in cell-free extracts: requirement
            for dATP and cytochrome c
  JOURNAL   Cell 86 (1), 147-157 (1996)
   PUBMED   8689682
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Flaws,J.A., Kugu,K., Trbovich,A.M., DeSanti,A., Tilly,K.I.,
            Hirshfield,A.N. and Tilly,J.L.
  TITLE     Interleukin-1 beta-converting enzyme-related proteases (IRPs) and
            mammalian cell death: dissociation of IRP-induced oligonucleosomal
            endonuclease activity from morphological apoptosis in granulosa
            cells of the ovarian follicle
  JOURNAL   Endocrinology 136 (11), 5042-5053 (1995)
   PUBMED   7588240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.532354.1,
                                           SRR26643299.58847.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..277
                     /product="caspase-3"
                     /EC_number="3.4.22.56"
                     /note="IRP; SCA-1; CASP-3; CPP-32; apopain; cysteine
                     protease CPP32; SREBP cleavage activity 1; protein Yama;
                     Caspase 3, apoptosis related cysteine protease (ICE-like
                     cysteine protease); CPP32beta; cysteine protease p32-beta"
                     /calculated_mol_wt=31361
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P70677; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     mat_peptide     29..175
                     /product="Caspase-3 subunit p17.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004591"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=16508
     Region          37..277
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; smart00115"
                     /db_xref="CDD:214521"
     Site            order(64,122,161,168,204..209,213..214)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(121,163)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(169,189..190,197,200,203,226,234,240,260,265..266,
                     268,271..272)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(170,188)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     mat_peptide     176..277
                     /product="Caspase-3 subunit p12.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004592"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=11890
     CDS             1..277
                     /gene="Casp3"
                     /gene_synonym="CPP32-beta; Lice; Yama"
                     /coded_by="NM_001436900.1:246..1079"
                     /db_xref="GeneID:25402"
                     /db_xref="RGD:2275"
ORIGIN      
        1 mdnnetsvds ksinnfetkt ihgsksmdsg iyldssykmd ypemglciii nnknfhkstg
       61 msarngtdvd aanlretfma lkyevrnknd ltreeimelm dsvskedhsk rssfvcvils
      121 hgdegvifgt ngpvdlkklt sffrgdycrs ltgkpklfii qacrgteldc gietdsgtdd
      181 dmacqkipve adflyaysta pgyyswrnsr dgswfiqslc amlklyahkl efmhiltrvn
      241 rkvatefesf sldatfhakk qipcivsmlt kelyfyh
//
LOCUS       NP_001423814             765 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 11
            [Rattus norvegicus].
ACCESSION   NP_001423814 XP_063131567
VERSION     NP_001423814.1
DBSOURCE    REFSEQ: accession NM_001436885.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131567.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.274648.1,
                                           SRR26360172.1021774.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..765
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 11"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=84229
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..765
                     /gene="Eps15l1"
                     /coded_by="NM_001436885.1:35..2332"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqddpf knkallfsnn sqelhpdpfq aedpfksdpf
      601 kgadpfkgdp fqsdpfseqq tavtdpfggd pfkesdpfhs stsddffkkq tkndpftsdp
      661 ftknpslpsk ldpfessdpf ssssisskgs dpfgtldpfg sssfssaegf adfsqmskpp
      721 psgpfssslg gtgfsddpfk skqdtpalpp kkpapprpkp psvwq
//
LOCUS       NP_001025092             878 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 4
            [Rattus norvegicus].
ACCESSION   NP_001025092 XP_341408
VERSION     NP_001025092.1
DBSOURCE    REFSEQ: accession NM_001029921.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Jul 29, 2005 this sequence version replaced XP_341408.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098004.1, SRR26360194.1809503.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..878
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 4"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=96316
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..878
                     /gene="Eps15l1"
                     /coded_by="NM_001029921.2:35..2671"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqddpf knkallfsnn sqelhpdpfq aedpfksdpf
      601 kgadpfkgdp fqsdpfseqq tavtdpfggd pfkesdpfhs stsddffkkq tkndpftsdp
      661 ftknpslpsk ldpfessdpf ssssisskgs dpfgtldpfg sssfssaegf adfsqmskpp
      721 psgpfssslg gtgfsddpfk skqdtpalpp kkpapprpkp psgqstpvsq lgssafpesp
      781 dpfqpleads gdpfqnkkgf gdpfsgkdpf apsssakppk asssgfadft sfgneeqqla
      841 wakresekae qerlarlrrq eqedlelaia lskadmpa
//
LOCUS       NP_001423817             751 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 14
            [Rattus norvegicus].
ACCESSION   NP_001423817 XP_063131571
VERSION     NP_001423817.1
DBSOURCE    REFSEQ: accession NM_001436888.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131571.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3177135.1,
                                           SRR26360181.737804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..751
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 14"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=83095
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..751
                     /gene="Eps15l1"
                     /coded_by="NM_001436888.1:35..2290"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqddpf knkallfsnn sqelhpdpfq aedpfksdpf
      601 kgadpfkgdp fqsdpfseqq tavtdpfggd pfkesdpfhs stsddffkkq tkndpftsdp
      661 ftknpslpsk ldpfessdpf ssssisskgs dpfgtldpfg sssfssaegf adfsqmsksp
      721 rqeelrvcrh klqkevgspt cltiqkcpls l
//
LOCUS       NP_001423859            1170 aa            linear   ROD 24-MAR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 isoform 4
            [Rattus norvegicus].
ACCESSION   NP_001423859 XP_038947975
VERSION     NP_001423859.1
DBSOURCE    REFSEQ: accession NM_001436930.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   4  (residues 1 to 1170)
  AUTHORS   Walker,D.M., Urbe,S., Dove,S.K., Tenza,D., Raposo,G. and
            Clague,M.J.
  TITLE     Characterization of MTMR3. an inositol lipid 3-phosphatase with
            novel substrate specificity
  JOURNAL   Curr Biol 11 (20), 1600-1605 (2001)
   PUBMED   11676921
REFERENCE   5  (residues 1 to 1170)
  AUTHORS   Taylor,G.S., Maehama,T. and Dixon,J.E.
  TITLE     Myotubularin, a protein tyrosine phosphatase mutated in myotubular
            myopathy, dephosphorylates the lipid second messenger,
            phosphatidylinositol 3-phosphate
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8910-8915 (2000)
   PUBMED   10900271
REFERENCE   6  (residues 1 to 1170)
  AUTHORS   Zhao,R., Qi,Y. and Zhao,Z.J.
  TITLE     FYVE-DSP1, a dual-specificity protein phosphatase containing an
            FYVE domain
  JOURNAL   Biochem Biophys Res Commun 270 (1), 222-229 (2000)
   PUBMED   10733931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038947975.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.49476.1,
                                           SRR26643296.33374.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1170
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR3 isoform 4"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3"
                     /calculated_mol_wt=130816
     Region          23..116
                     /region_name="PH-GRAM_MTMR3"
                     /note="Myotubularian (MTM) related 3 protein (MTMR3)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13341"
                     /db_xref="CDD:270149"
     Region          169..485
                     /region_name="PTP-MTMR3"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 3;
                     cd14586"
                     /db_xref="CDD:350434"
     Region          1078..1147
                     /region_name="FYVE_MTMR3"
                     /note="FYVE domain found in myotubularin-related protein 3
                     (MTMR3) and similar proteins; cd15732"
                     /db_xref="CDD:277271"
     Site            order(1079,1082,1100..1105,1116..1117,1141..1143)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277271"
     CDS             1..1170
                     /gene="Mtmr3"
                     /coded_by="NM_001436930.1:530..4042"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:305482"
                     /db_xref="RGD:1310972"
ORIGIN      
        1 mdeemrhsle ciqanqifpr kqliredenl qvpflelhge steyvgraed aiialsnyrl
       61 hikfkeslvn vplqliesve crdifqlhlt ckdckvircq fptfeqcqdw lkrlnnairp
      121 pgkiedlfsf ayhawcmevy asekeqhgdl crpgehvtsr fknevermgf dmnnawrisn
      181 inekyklcgs ypqelivpaw itdkelesva gfrswkripa viyrhqsnga viarcgqpev
      241 swwgwrnadd ehlvqsvaka casdsqssvg kvstrnscrg fpnagdlsdv efdaslsnas
      301 gteslalqpq kllildarsy aaavanrakg ggcecpeyyp ncevvfmgma nihsirrsfq
      361 slrllctqmp dpgnwlsale stkwlhhlsv llksallvvh avdrdqrpvl vhcsdgwdrt
      421 pqivalakll ldpyyrtveg fqvlvemewl dfghkfadrc ghgensddln ercpvflqwl
      481 dcvhqlqrqf pcsfefneaf lvklvqhtys clfgtflcnn akergekqtq ertcsvwsll
      541 ragnkafknl lyssqseavl ypvchvrnlm lwsavylpcp spstptddsc apypapgtsp
      601 depplsrlpk trsfdnlttt cdnmvplasr rssdpslnek wqehgrslel ssfagsgeev
      661 paidslrrps rllggaelsv aagvaegqme nilqeatkee sgveepthre htevpevkee
      721 aplakesrta aqgsgvlyqe pqlddatlrs hlgpslssfs qgipehrevg hsvlssslpa
      781 slrgedsqev pveqpqveni aedrenvvpa vpvdvkiglg tsesspllps qvpfetrgph
      841 mnnsvhmlle dkvksesgpq lhhrpclass grfsgkdmlp iapeprsaer pqwdsvlhrt
      901 sspgntlslm mqapcalpld kcrqrivcng aletenkase qpagfdtlqk yptpnghcan
      961 getgrskdsl shqlsatsys sahscsrnlh hkwlnshsgr psttnspeqp srshldddgm
     1021 pvytdtiqqr lrqiesghqq evetlkkqvq elksrlesqy ltsslrfngd fgdevmtrwl
     1081 pdhlaahcya cdsafwlasr khhcrdtdrv dqtwncgnvf cssccnqkvp vpsqqlfeps
     1141 rvckscyssl hptsssidle ldkpiaatsn
//
LOCUS       NP_001423818             750 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 16
            [Rattus norvegicus].
ACCESSION   NP_001423818 XP_063131572
VERSION     NP_001423818.1
DBSOURCE    REFSEQ: accession NM_001436889.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131572.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55533.1,
                                           SRR26360194.1360841.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..750
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 16"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=82490
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..750
                     /gene="Eps15l1"
                     /coded_by="NM_001436889.1:35..2287"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskd
//
LOCUS       NP_001012105             801 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001012105 XP_233676
VERSION     NP_001012105.1
DBSOURCE    REFSEQ: accession NM_001012105.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Feb 11, 2005 this sequence version replaced XP_233676.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..801
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform b"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=87522
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          304..635
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(367,369,371,373..374,377..378,381,395,397,401..402,
                     405..406,409,423,425,427,429..430,433..434,437)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          390..410
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          418..438
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          446..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          474..494
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(479,481,483,485..486,489..490,493,507,509,513..514,
                     517..518,521,535,537,539,541..542,545..546,549)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          502..522
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          530..550
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          558..578
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          586..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          614..633
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..801
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001012105.2:208..2613"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae evccvlspgg dkrakeekaa atvlsrldqa rssssagpgr elkeewggqa
      181 esasrgaeqt ekadaprepp pvelkpdpts smaaaeaeal sesseqemev epaskgeegq
      241 eeegpgpatv keegvhleng eppeeneesa gtdsghelgm egqnlrsgty gdrteskayg
      301 siihkcedcg kefthtgnfk rhirihtgek pfscrecska fsdpaackah ekthsplkpy
      361 gceecgksyr lisllnlhkk rhsgearyrc gdcgklftts gnlkrhqlvh sgqkpyqcdy
      421 cgrsfsdpts kmrhlethdt dkehkcphcd kkfnqvgnlk ahlkihiadg plkcrecgkq
      481 fttsgnlkrh lrihsgekpy vcthcqrqfa dpgalqrhvr ihtgekpcqc vicgkaftqa
      541 ssliahvrqh tgekpyvcer cgkrfvqssq lanhirhhdn irphkcsvcs kafvnvgdls
      601 khiiihtgek pylcdkcgrg fnrvdnlrsh vktvhqgkag ikilepeegg evsvvtvddm
      661 vtlatealaa tavtqltvvp vgaavtadet evlkaeiska vkqvqeedpn thilyacdsc
      721 gdkfldansl aqhvrihtaq alvmfqtdad fyqqygpgga wpagqmlqag elvfrprdgt
      781 egqptlaetp ptapdclppa e
//
LOCUS       NP_001423815             765 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 12
            [Rattus norvegicus].
ACCESSION   NP_001423815 XP_008769344
VERSION     NP_001423815.1
DBSOURCE    REFSEQ: accession NM_001436886.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_008769344.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.55529.1,
                                           SRR26643298.70777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..765
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 12"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=84801
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <385..>566
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..765
                     /gene="Eps15l1"
                     /coded_by="NM_001436886.1:35..2332"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqddpf knkallfsnn sqelhpdpfq aedpfksdpf
      601 kgadpfkgdp fqsdpfseqq tavtdpfggd pfkesdpfhs stsddffkkq tkndpftsdp
      661 ftknpslpsk ldpfessdpf ssssisskgs dpfgtldpfg sssfssaegf adfsqmskfg
      721 neeqqlawak resekaeqer larlrrqeqe dlelaialsk admpa
//
LOCUS       NP_001423860            1161 aa            linear   ROD 24-MAR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 isoform 5
            [Rattus norvegicus].
ACCESSION   NP_001423860 XP_038947976
VERSION     NP_001423860.1
DBSOURCE    REFSEQ: accession NM_001436931.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   4  (residues 1 to 1161)
  AUTHORS   Walker,D.M., Urbe,S., Dove,S.K., Tenza,D., Raposo,G. and
            Clague,M.J.
  TITLE     Characterization of MTMR3. an inositol lipid 3-phosphatase with
            novel substrate specificity
  JOURNAL   Curr Biol 11 (20), 1600-1605 (2001)
   PUBMED   11676921
REFERENCE   5  (residues 1 to 1161)
  AUTHORS   Taylor,G.S., Maehama,T. and Dixon,J.E.
  TITLE     Myotubularin, a protein tyrosine phosphatase mutated in myotubular
            myopathy, dephosphorylates the lipid second messenger,
            phosphatidylinositol 3-phosphate
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8910-8915 (2000)
   PUBMED   10900271
REFERENCE   6  (residues 1 to 1161)
  AUTHORS   Zhao,R., Qi,Y. and Zhao,Z.J.
  TITLE     FYVE-DSP1, a dual-specificity protein phosphatase containing an
            FYVE domain
  JOURNAL   Biochem Biophys Res Commun 270 (1), 222-229 (2000)
   PUBMED   10733931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038947976.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.47256.1,
                                           SRR26643287.30689.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1161
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR3 isoform 5"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3"
                     /calculated_mol_wt=129699
     Region          23..116
                     /region_name="PH-GRAM_MTMR3"
                     /note="Myotubularian (MTM) related 3 protein (MTMR3)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13341"
                     /db_xref="CDD:270149"
     Region          169..485
                     /region_name="PTP-MTMR3"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 3;
                     cd14586"
                     /db_xref="CDD:350434"
     Region          1078..1138
                     /region_name="FYVE_MTMR3"
                     /note="FYVE domain found in myotubularin-related protein 3
                     (MTMR3) and similar proteins; cd15732"
                     /db_xref="CDD:277271"
     Site            order(1079,1082,1100..1105,1107..1108,1132..1134)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277271"
     CDS             1..1161
                     /gene="Mtmr3"
                     /coded_by="NM_001436931.1:530..4015"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:305482"
                     /db_xref="RGD:1310972"
ORIGIN      
        1 mdeemrhsle ciqanqifpr kqliredenl qvpflelhge steyvgraed aiialsnyrl
       61 hikfkeslvn vplqliesve crdifqlhlt ckdckvircq fptfeqcqdw lkrlnnairp
      121 pgkiedlfsf ayhawcmevy asekeqhgdl crpgehvtsr fknevermgf dmnnawrisn
      181 inekyklcgs ypqelivpaw itdkelesva gfrswkripa viyrhqsnga viarcgqpev
      241 swwgwrnadd ehlvqsvaka casdsqssvg kvstrnscrg fpnagdlsdv efdaslsnas
      301 gteslalqpq kllildarsy aaavanrakg ggcecpeyyp ncevvfmgma nihsirrsfq
      361 slrllctqmp dpgnwlsale stkwlhhlsv llksallvvh avdrdqrpvl vhcsdgwdrt
      421 pqivalakll ldpyyrtveg fqvlvemewl dfghkfadrc ghgensddln ercpvflqwl
      481 dcvhqlqrqf pcsfefneaf lvklvqhtys clfgtflcnn akergekqtq ertcsvwsll
      541 ragnkafknl lyssqseavl ypvchvrnlm lwsavylpcp spstptddsc apypapgtsp
      601 depplsrlpk trsfdnlttt cdnmvplasr rssdpslnek wqehgrslel ssfagsgeev
      661 paidslrrps rllggaelsv aagvaegqme nilqeatkee sgveepthre htevpevkee
      721 aplakesrta aqgsgvlyqe pqlddatlrs hlgpslssfs qgipehrevg hsvlssslpa
      781 slrgedsqev pveqpqveni aedrenvvpa vpvdvkiglg tsesspllps qvpfetrgph
      841 mnnsvhmlle dkvksesgpq lhhrpclass grfsgkdmlp iapeprsaer pqwdsvlhrt
      901 sspgntlslm mqapcalpld kcrqrivcng aletenkase qpagfdtlqk yptpnghcan
      961 getgrskdsl shqlsatsys sahscsrnlh hkwlnshsgr psttnspeqp srshldddgm
     1021 pvytdtiqqr lrqiesghqq evetlkkqvq elksrlesqy ltsslrfngd fgdevmtrwl
     1081 pdhlaahcya cdsafwlasr khhcrncgnv fcssccnqkv pvpsqqlfep srvckscyss
     1141 lhptsssidl eldkpiaats n
//
LOCUS       NP_001423869             108 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform e [Rattus norvegicus].
ACCESSION   NP_001423869 XP_017448960
VERSION     NP_001423869.1
DBSOURCE    REFSEQ: accession NM_001436940.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017448960.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2349994.1,
                                           SRR26360181.87742.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..108
                     /product="C-C motif chemokine 27 isoform e"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=12192
     CDS             1..108
                     /gene="Ccl27"
                     /coded_by="NM_001436940.1:209..535"
                     /note="isoform e is encoded by transcript variant 8"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 meewssedgc agpaepfgar dmsrlrryev aleaeeeiyw gcfyffpwlr mwrrerssah
       61 preqkleplr glmsclssgl rpapqrsgrg llcrtptaaa qtagalki
//
LOCUS       NP_001423792             819 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423792 XP_063143885
VERSION     NP_001423792.1
DBSOURCE    REFSEQ: accession NM_001436863.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143885.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..819
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform a"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=89382
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          322..653
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          352..372
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(385,387,389,391..392,395..396,399,413,415,419..420,
                     423..424,427,441,443,445,447..448,451..452,455)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          464..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(497,499,501,503..504,507..508,511,525,527,531..532,
                     535..536,539,553,555,557,559..560,563..564,567)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          632..651
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..819
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001436863.1:429..2888"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae eggdkrakee kaaatvlsrl dqarssssag pgrelkeewg gqaesasrgf
      181 vpameethlt saqspnpash pssgaeqtek adaprepppv elkpdptssm aaaeaealse
      241 sseqemevep askgeegqee egpgpatvke egvhlengep peeneesagt dsghelgmeg
      301 qnlrsgtygd rteskaygsi ihkcedcgke fthtgnfkrh irihtgekpf screcskafs
      361 dpaackahek thsplkpygc eecgksyrli sllnlhkkrh sgearyrcgd cgklfttsgn
      421 lkrhqlvhsg qkpyqcdycg rsfsdptskm rhlethdtdk ehkcphcdkk fnqvgnlkah
      481 lkihiadgpl kcrecgkqft tsgnlkrhlr ihsgekpyvc thcqrqfadp galqrhvrih
      541 tgekpcqcvi cgkaftqass liahvrqhtg ekpyvcercg krfvqssqla nhirhhdnir
      601 phkcsvcska fvnvgdlskh iiihtgekpy lcdkcgrgfn rvdnlrshvk tvhqgkagik
      661 ilepeeggev svvtvddmvt latealaata vtqltvvpvg aavtadetev lkaeiskavk
      721 qvqeedpnth ilyacdscgd kfldanslaq hvrihtaqal vmfqtdadfy qqygpggawp
      781 agqmlqagel vfrprdgteg qptlaetppt apdclppae
//
LOCUS       NP_001423878             428 aa            linear   ROD 24-MAR-2025
DEFINITION  DNA-binding protein Ikaros isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423878 XP_008768537
VERSION     NP_001423878.1
DBSOURCE    REFSEQ: accession NM_001436949.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Young,G.P., Symonds,E.L., Nielsen,H.J., Ferm,L., Christensen,I.J.,
            Dekker,E., van der Vlugt,M., Mallant-Hent,R.C., Boulter,N., Yu,B.,
            Chan,M., Tevz,G., LaPointe,L.C. and Pedersen,S.K.
  TITLE     Evaluation of a panel of tumor-specific differentially-methylated
            DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of
            colorectal cancer
  JOURNAL   Clin Epigenetics 13 (1), 14 (2021)
   PUBMED   33478584
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Sharma,B., Shah,R., Jamwal,R.S., Verma,S., Bhat,A., Bhat,G.R.,
            Bakshi,D., Singh,S., Angurana,S., Bhat,A., Vaishnavi,S. and
            Kumar,R.
  TITLE     Evaluation of newly identified Ikaros family zinc finger 1 loci in
            colorectal cancer
  JOURNAL   J Cancer Res Ther 17 (1), 46-50 (2021)
   PUBMED   33723131
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Musher,B.L., Melson,J.E., Amato,G., Chan,D., Hill,M., Khan,I.,
            Kochuparambil,S.T., Lyons,S.E., Orsini,J. Jr., Pedersen,S.K.,
            Robb,B., Saltzman,J., Silinsky,J., Gaur,S., Tuck,M.K.,
            LaPointe,L.C. and Young,G.P.
  TITLE     Evaluation of Circulating Tumor DNA for Methylated BCAT1 and IKZF1
            to Detect Recurrence of Stage II/Stage III Colorectal Cancer (CRC)
  JOURNAL   Cancer Epidemiol Biomarkers Prev 29 (12), 2702-2709 (2020)
   PUBMED   32958500
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Zhao,W., Chen,T.B. and Wang,H.
  TITLE     Ikaros is heterogeneously expressed in lung adenocarcinoma and is
            involved in its progression
  JOURNAL   J Int Med Res 48 (8), 300060520945860 (2020)
   PUBMED   32787735
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Symonds,E.L., Pedersen,S.K., Murray,D., Byrne,S.E., Roy,A.,
            Karapetis,C., Hollington,P., Rabbitt,P., Jones,F.S., LaPointe,L.,
            Segelov,E. and Young,G.P.
  TITLE     Circulating epigenetic biomarkers for detection of recurrent
            colorectal cancer
  JOURNAL   Cancer 126 (7), 1460-1469 (2020)
   PUBMED   31909823
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Honma,Y., Kiyosawa,H., Mori,T., Oguri,A., Nikaido,T., Kanazawa,K.,
            Tojo,M., Takeda,J., Tanno,Y., Yokoya,S., Kawabata,I., Ikeda,H. and
            Wanaka,A.
  TITLE     Eos: a novel member of the Ikaros gene family expressed
            predominantly in the developing nervous system
  JOURNAL   FEBS Lett 447 (1), 76-80 (1999)
   PUBMED   10218586
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Kelley,C.M., Ikeda,T., Koipally,J., Avitahl,N., Wu,L.,
            Georgopoulos,K. and Morgan,B.A.
  TITLE     Helios, a novel dimerization partner of Ikaros expressed in the
            earliest hematopoietic progenitors
  JOURNAL   Curr Biol 8 (9), 508-515 (1998)
   PUBMED   9560339
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Boggs,S.S., Trevisan,M., Patrene,K. and Geogopoulos,K.
  TITLE     Lack of natural killer cell precursors in fetal liver of Ikaros
            knockout mutant mice
  JOURNAL   Nat Immun 16 (4), 137-145 (1998)
   PUBMED   10366784
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Molnar,A. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of functionally diverse zinc
            finger DNA-binding proteins
  JOURNAL   Mol Cell Biol 14 (12), 8292-8303 (1994)
   PUBMED   7969165
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Georgopoulos,K., Bigby,M., Wang,J.H., Molnar,A., Wu,P., Winandy,S.
            and Sharpe,A.
  TITLE     The Ikaros gene is required for the development of all lymphoid
            lineages
  JOURNAL   Cell 79 (1), 143-156 (1994)
   PUBMED   7923373
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_008768537.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.17390.1,
                                           SRR26643292.52730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..428
                     /product="DNA-binding protein Ikaros isoform 1"
                     /note="DNA-binding protein Ikaros"
                     /calculated_mol_wt=47806
     Region          <1..>130
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          57..79
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          59..79
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(64,66,68,70..71,74..75,78,92,94,98..99,102..103,106,
                     120,122,124,126..127,130..131,135)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          71..96
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          87..107
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          115..136
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..428
                     /gene="Ikzf1"
                     /gene_synonym="RGD1562979"
                     /coded_by="NM_001436949.1:66..1352"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:305501"
                     /db_xref="RGD:1562979"
ORIGIN      
        1 mdvdegqdms qvsgkesppv sdtpdegdep mpvpedlsts gaqqnsksdr gmgerpfqcn
       61 qcgasftqkg nllrhiklhs gekpfkchlc nyacrrrdal tghlrthsvg kphkcgycgr
      121 sykqrsslee hkerchnyle smglpgmypv ikeetnhsem aedlckigae rslvldrlas
      181 nvakrkssmp qkflgdkcls dmpydsanye kdemmtshvm dqainnainy lgaeslrplv
      241 qtppgssevv pvissmyqlh kppsdgpprs nhsaqdsave nllllskaks vssereasps
      301 nscqdstdte snaeeqrsgl iyltnhitph arnglalkee qrayevlraa sensqdafrv
      361 vstsgeqlkv ykcehcrvlf ldhvmytihm gchgfrdpfe cnmcgyhsqd ryefsshitr
      421 gehryhls
//
LOCUS       NP_001423783             515 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423783 XP_038965991
VERSION     NP_001423783.1
DBSOURCE    REFSEQ: accession NM_001436854.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038965991.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217687.1, SRR26643288.24451.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..515
                     /product="heterochromatin protein 1-binding protein 3
                     isoform b"
                     /calculated_mol_wt=56678
     Region          117..201
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(124,136,168,182)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            163..174
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          226..286
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          302..369
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <431..>505
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..515
                     /gene="Hp1bp3"
                     /coded_by="NM_001436854.1:123..1670"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mpirravnst retppkskla egeeekpepd gsseesistv eepenetppa psreaeqpkg
       61 epesgekees ksaeetkkee kdqskekekk vkktipawat lsasqlaraq kqtpmasspr
      121 pkmdailtea ikacfqksga svvairkyii hkypsldler rgyllkqalk relnrgvikq
      181 vkgkgasgsf vvvqksktpq ksknrkkgsa vdpepqvkle dvlplaftrl cepkeasysl
      241 irkyvsqyyp klrvdirpql lknalqrave rgqleqitgk gasgtfqlkk sgekpllggs
      301 lmeyailsai aamnepktcs ttalkkyvle nhpgtnsnyq mhllkktlqk cekngwleqi
      361 sgkgfsgtfq lcfpyypspg vlfpkkvsdg sededeeede eessedsede epppkrslqk
      421 ktpakpqgkt asmkqrgakp arkvpaaqrg kvrplpkkap pkaktparkg rpapsavkkp
      481 sgstskkpva narkeaklpg kgksamkkks fktkk
//
LOCUS       NP_001423827             153 aa            linear   ROD 24-MAR-2025
DEFINITION  ceramide-1-phosphate transfer protein isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423827 XP_038966049
VERSION     NP_001423827.1
DBSOURCE    REFSEQ: accession NM_001436898.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Mishra,S.K., Gao,Y.G., Deng,Y., Chalfant,C.E., Hinchcliffe,E.H. and
            Brown,R.E.
  TITLE     CPTP: A sphingolipid transfer protein that regulates autophagy and
            inflammasome activation
  JOURNAL   Autophagy 14 (5), 862-879 (2018)
   PUBMED   29164996
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Simanshu,D.K., Kamlekar,R.K., Wijesinghe,D.S., Zou,X., Zhai,X.,
            Mishra,S.K., Molotkovsky,J.G., Malinina,L., Hinchcliffe,E.H.,
            Chalfant,C.E., Brown,R.E. and Patel,D.J.
  TITLE     Non-vesicular trafficking by a ceramide-1-phosphate transfer
            protein regulates eicosanoids
  JOURNAL   Nature 500 (7463), 463-467 (2013)
   PUBMED   23863933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966049.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.25887.1,
                                           SRR26643285.21769.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..153
                     /product="ceramide-1-phosphate transfer protein isoform b"
                     /note="glycolipid transfer protein domain-containing
                     protein 1; glycolipid transfer protein domain containing
                     1"
                     /calculated_mol_wt=17291
     Region          <2..112
                     /region_name="GLTP"
                     /note="Glycolipid transfer protein (GLTP); pfam08718"
                     /db_xref="CDD:462575"
     CDS             1..153
                     /gene="Cptp"
                     /gene_synonym="Gltpd1"
                     /coded_by="NM_001436898.1:303..764"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313771"
                     /db_xref="RGD:1359656"
ORIGIN      
        1 mehlrsgpqs ehyislqsmv ayevsnklvd rdsrsrprhp nsgcrtvlrl hralhwlqlf
       61 leglrtssed artstlcsea ynatlaayhs wivrqavnva fhalpprkvf leamnmgsse
      121 qavemlgeal pfieqvydis qklyaehsll dlp
//
LOCUS       NP_001423857            1207 aa            linear   ROD 24-MAR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001423857 XP_006251364
VERSION     NP_001423857.1
DBSOURCE    REFSEQ: accession NM_001436928.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Walker,D.M., Urbe,S., Dove,S.K., Tenza,D., Raposo,G. and
            Clague,M.J.
  TITLE     Characterization of MTMR3. an inositol lipid 3-phosphatase with
            novel substrate specificity
  JOURNAL   Curr Biol 11 (20), 1600-1605 (2001)
   PUBMED   11676921
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Taylor,G.S., Maehama,T. and Dixon,J.E.
  TITLE     Myotubularin, a protein tyrosine phosphatase mutated in myotubular
            myopathy, dephosphorylates the lipid second messenger,
            phosphatidylinositol 3-phosphate
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8910-8915 (2000)
   PUBMED   10900271
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Zhao,R., Qi,Y. and Zhao,Z.J.
  TITLE     FYVE-DSP1, a dual-specificity protein phosphatase containing an
            FYVE domain
  JOURNAL   Biochem Biophys Res Commun 270 (1), 222-229 (2000)
   PUBMED   10733931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006251364.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.17304.1,
                                           SRR26643429.47255.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1207
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR3 isoform 2"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3"
                     /calculated_mol_wt=134991
     Region          23..116
                     /region_name="PH-GRAM_MTMR3"
                     /note="Myotubularian (MTM) related 3 protein (MTMR3)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13341"
                     /db_xref="CDD:270149"
     Region          169..485
                     /region_name="PTP-MTMR3"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 3;
                     cd14586"
                     /db_xref="CDD:350434"
     Region          1115..1184
                     /region_name="FYVE_MTMR3"
                     /note="FYVE domain found in myotubularin-related protein 3
                     (MTMR3) and similar proteins; cd15732"
                     /db_xref="CDD:277271"
     Site            order(1116,1119,1137..1142,1153..1154,1178..1180)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277271"
     CDS             1..1207
                     /gene="Mtmr3"
                     /coded_by="NM_001436928.1:530..4153"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305482"
                     /db_xref="RGD:1310972"
ORIGIN      
        1 mdeemrhsle ciqanqifpr kqliredenl qvpflelhge steyvgraed aiialsnyrl
       61 hikfkeslvn vplqliesve crdifqlhlt ckdckvircq fptfeqcqdw lkrlnnairp
      121 pgkiedlfsf ayhawcmevy asekeqhgdl crpgehvtsr fknevermgf dmnnawrisn
      181 inekyklcgs ypqelivpaw itdkelesva gfrswkripa viyrhqsnga viarcgqpev
      241 swwgwrnadd ehlvqsvaka casdsqssvg kvstrnscrg fpnagdlsdv efdaslsnas
      301 gteslalqpq kllildarsy aaavanrakg ggcecpeyyp ncevvfmgma nihsirrsfq
      361 slrllctqmp dpgnwlsale stkwlhhlsv llksallvvh avdrdqrpvl vhcsdgwdrt
      421 pqivalakll ldpyyrtveg fqvlvemewl dfghkfadrc ghgensddln ercpvflqwl
      481 dcvhqlqrqf pcsfefneaf lvklvqhtys clfgtflcnn akergekqtq ertcsvwsll
      541 ragnkafknl lyssqseavl ypvchvrnlm lwsavylpcp spstptddsc apypapgtsp
      601 depplsrlpk trsfdnlttt cdnmvplasr rssdpslnek wqehgrslel ssfagsgeev
      661 paidslrrps rllggaelsv aagvaegqme nilqeatkee sgveepthre htevpevkee
      721 aplakesrta aqgsgvlyqe pqlddatlrs hlgpslssfs qgipehrevg hsvlssslpa
      781 slrgedsqev pveqpqveni aedrenvvpa vpvdvkiglg tsesspllps qvpfetrgph
      841 mnnsvhmlle dkvksesgpq lhhrpclass grfsgkdmlp iapeprsaer pqwdsvlhrt
      901 sspgntlslm mqapcalpld kcrqrivcng aletenkase qpagfdtlqk yptpnghcan
      961 getgrskdsl shqlsatsys sahscsrnlh hkwlnshsgr psttnspeqp srshldddgm
     1021 pvytdtiqqr lrqiesghqq evetlkkqvq elksrlesqy ltsslrfngd fgdevtsipd
     1081 sesnldqncl srcsteifse asweqvdkqd temtrwlpdh laahcyacds afwlasrkhh
     1141 crdtdrvdqt wncgnvfcss ccnqkvpvps qqlfepsrvc kscysslhpt sssidleldk
     1201 piaatsn
//
LOCUS       NP_954539                553 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform a [Rattus
            norvegicus].
ACCESSION   NP_954539 XP_233579
VERSION     NP_954539.1
DBSOURCE    REFSEQ: accession NM_199108.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 1, 2004 this sequence version replaced XP_233579.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061837.1, SRR26360194.2463005.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..553
                     /product="heterochromatin protein 1-binding protein 3
                     isoform a"
                     /calculated_mol_wt=60676
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          30..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          155..239
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            order(162,174,206,220)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3TEA8; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            201..212
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          231..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          253..257
                     /region_name="PxVxL motif.
                     /evidence=ECO:0000250|UniProtKB:Q5SSJ5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          264..324
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          340..407
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          422..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P747.1)"
     Region          <469..>543
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..553
                     /gene="Hp1bp3"
                     /coded_by="NM_199108.2:203..1864"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 matdmsqgel ihpkalpliv gaqlihadkl gekaddstmp irravnstre tppksklaeg
       61 eeekpepdgs seesistvee penetppaps reaeqpkgep esgekeesks aeetkkeekd
      121 qskekekkvk ktipawatls asqlaraqkq tpmassprpk mdailteaik acfqksgasv
      181 vairkyiihk ypsldlerrg yllkqalkre lnrgvikqvk gkgasgsfvv vqksktpqks
      241 knrkkgsavd pepqvkledv lplaftrlce pkeasyslir kyvsqyypkl rvdirpqllk
      301 nalqraverg qleqitgkga sgtfqlkksg ekpllggslm eyailsaiaa mnepktcstt
      361 alkkyvlenh pgtnsnyqmh llkktlqkce kngwleqisg kgfsgtfqlc fpyypspgvl
      421 fpkkvsdgse dedeeedeee ssedsedeep ppkrslqkkt pakpqgktas mkqrgakpar
      481 kvpaaqrgkv rplpkkappk aktparkgrp apsavkkpsg stskkpvana rkeaklpgkg
      541 ksamkkksfk tkk
//
LOCUS       NP_001100698             402 aa            linear   ROD 24-MAR-2025
DEFINITION  protein FAM53A [Rattus norvegicus].
ACCESSION   NP_001100698 XP_001062281 XP_223544
VERSION     NP_001100698.1
DBSOURCE    REFSEQ: accession NM_001107228.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001062281.1, XP_223544.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168895.1, SRR26643286.39035.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..402
                     /product="protein FAM53A"
                     /calculated_mol_wt=42925
     Region          1..299
                     /region_name="FAM53"
                     /note="Family of FAM53; pfam15242"
                     /db_xref="CDD:464582"
     CDS             1..402
                     /gene="Fam53a"
                     /gene_synonym="RGD1563315"
                     /coded_by="NM_001107228.3:545..1753"
                     /db_xref="GeneID:305461"
                     /db_xref="RGD:1563315"
ORIGIN      
        1 mvtliteklq nqslddltrr aceavpysae kldksghlfp leigvdkspw kashggwpfr
       61 sraasgpfsv gphgvshteg lkwqlespgp mavgrfldlr estgppaapp tkrhcrslse
      121 peelarcrsp wrpgsskvwt piskrrcnsg gsatlqccsg lgnpalqgsl apglprkpvs
      181 ptgptspmtp rpasassgfv dgsegstssg ppwlstgpcp fssrrrlsls qehlvdagac
      241 lpsasstpts tpelgrhhgl lrcrsqpcvl dgrrvrrkrr reedarwtrp sldflkmtrt
      301 lknskslcsl dyeddeddtq aktvvsspcn sqglvgiitp ssspriprpg paspsvwasg
      361 epetstgegg ssgepsdwds ageegifpld hgdldleqie nn
//
LOCUS       NP_001102124             525 aa            linear   ROD 24-MAR-2025
DEFINITION  thymocyte selection-associated high mobility group box protein TOX
            [Rattus norvegicus].
ACCESSION   NP_001102124 XP_001063218 XP_342801
VERSION     NP_001102124.1
DBSOURCE    REFSEQ: accession NM_001108654.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Artegiani,B., de Jesus Domingues,A.M., Bragado Alonso,S.,
            Brandl,E., Massalini,S., Dahl,A. and Calegari,F.
  TITLE     Tox: a multifunctional transcription factor and novel regulator of
            mammalian corticogenesis
  JOURNAL   EMBO J 34 (7), 896-910 (2015)
   PUBMED   25527292
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Yun,S., Lee,S.H., Yoon,S.R., Kim,M.S., Piao,Z.H., Myung,P.K.,
            Kim,T.D., Jung,H. and Choi,I.
  TITLE     TOX regulates the differentiation of human natural killer cells
            from hematopoietic stem cells in vitro
  JOURNAL   Immunol Lett 136 (1), 29-36 (2011)
   PUBMED   21126536
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Aliahmad,P., de la Torre,B. and Kaye,J.
  TITLE     Shared dependence on the DNA-binding factor TOX for the development
            of lymphoid tissue-inducer cell and NK cell lineages
  JOURNAL   Nat Immunol 11 (10), 945-952 (2010)
   PUBMED   20818394
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Aliahmad,P. and Kaye,J.
  TITLE     Development of all CD4 T lineages requires nuclear factor TOX
  JOURNAL   J Exp Med 205 (1), 245-256 (2008)
   PUBMED   18195075
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Aliahmad,P., O'Flaherty,E., Han,P., Goularte,O.D., Wilkinson,B.,
            Satake,M., Molkentin,J.D. and Kaye,J.
  TITLE     TOX provides a link between calcineurin activation and CD8 lineage
            commitment
  JOURNAL   J Exp Med 199 (8), 1089-1099 (2004)
   PUBMED   15078895
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Wilkinson,B., Chen,J.Y., Han,P., Rufner,K.M., Goularte,O.D. and
            Kaye,J.
  TITLE     TOX: an HMG box protein implicated in the regulation of thymocyte
            selection
  JOURNAL   Nat Immunol 3 (3), 272-280 (2002)
   PUBMED   11850626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342801.3, XP_001063218.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.248158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..525
                     /product="thymocyte selection-associated high mobility
                     group box protein TOX"
                     /note="thymocyte selection-associated HMG box"
                     /calculated_mol_wt=57155
     Region          262..331
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(262..263,265..269,272..273,280,292..293,296,
                     299..300,307,311,314,318,321)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..525
                     /gene="Tox"
                     /coded_by="NM_001108654.2:211..1788"
                     /db_xref="GeneID:362481"
                     /db_xref="RGD:1310455"
ORIGIN      
        1 mdvrfypppa qpaaapaapc lgpspcldpy ycnkfdgenm ymsmtepsqd yvpvsqsypg
       61 pslesedfni ppitppslpd hslvhlneve sgyhslchpm nhngllpfhp qnmdlpeitv
      121 snmlgqdgtl lsnsisvmqe ignaegaqys shpqlaamrp rgqptdlrqq asmmqhgqlt
      181 tinqsqlsaq lglnmggtnv phnspsppgs ksatpspsss vhedecedts kinggekrpa
      241 sdmgkkpktp kkkkkkdpne pqkpvsayal ffrdtqaaik gqnpnatfge vskivasmwd
      301 glgeeqkqvy kkkteaakke ylkqlaayra slvsksyndp vdvktsqppq lvnskpsvfh
      361 gpsqahsaly lsshyhqqpg mtpqltamhp slprniapkp nnqmpvtvsi anmavspppp
      421 lqispplhqh lsmqqhqplv qqplasqlpm qvqtalhspt mqqgftlqpd yqtiinptst
      481 aaqvvtqame yvrsgcrnpp pqpvdwstdy cssggmqrdk alylt
//
LOCUS       NP_001423787             470 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423787
VERSION     NP_001423787.1
DBSOURCE    REFSEQ: accession NM_001436858.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.132270.1,
                                           SRR26360194.2137449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN17050754, SAMN17050766
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..470
                     /product="heterochromatin protein 1-binding protein 3
                     isoform d"
                     /calculated_mol_wt=52074
     Region          72..156
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(79,91,123,137)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            118..129
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          181..241
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          257..324
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <371..447
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     CDS             1..470
                     /gene="Hp1bp3"
                     /coded_by="NM_001436858.1:256..1668"
                     /note="isoform d is encoded by transcript variant 8"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mrlhllhpgr qssprgslrv errkrasllr kprkkkdqsk ekekkvkkti pawatlsasq
       61 laraqkqtpm assprpkmda ilteaikacf qksgasvvai rkyiihkyps ldlerrgyll
      121 kqalkrelnr gvikqvkgkg asgsfvvvqk sktpqksknr kkgsavdpep qvkledvlpl
      181 aftrlcepke asyslirkyv sqyypklrvd irpqllknal qravergqle qitgkgasgt
      241 fqlkksgekp llggslmeya ilsaiaamne pktcsttalk kyvlenhpgt nsnyqmhllk
      301 ktlqkcekng wleqisgkgf sgtfqlcfpy ypspgvlfpk kvsdgseded eeedeeesse
      361 dsedeepppk rslqkktpak pqgktasmkq rgakparkvp aaqrgkvrpl pkkappkakt
      421 parkgrpaps avkkpsgsts kkpvanarke aklpgkgksa mkkksfktkk
//
LOCUS       NP_001423796             794 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423796 XP_063143887
VERSION     NP_001423796.1
DBSOURCE    REFSEQ: accession NM_001436867.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143887.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.23594.1,
                                           SRR26643296.16622.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..794
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform c"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=86820
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          297..628
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(360,362,364,366..367,370..371,374,388,390,394..395,
                     398..399,402,416,418,420,422..423,426..427,430)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(472,474,476,478..479,482..483,486,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..599
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          607..626
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..794
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001436867.1:305..2689"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae eggdkrakee kaaatvlsrl dqarssssag pgrelkeewg gqaesasrga
      181 eqtekadapr epppvelkpd ptssmaaaea ealsesseqe mevepaskge egqeeegpgp
      241 atvkeegvhl engeppeene esagtdsghe lgmegqnlrs gtygdrtesk aygsiihkce
      301 dcgkefthtg nfkrhiriht gekpfscrec skafsdpaac kahekthspl kpygceecgk
      361 syrlisllnl hkkrhsgear yrcgdcgklf ttsgnlkrhq lvhsgqkpyq cdycgrsfsd
      421 ptskmrhlet hdtdkehkcp hcdkkfnqvg nlkahlkihi adgplkcrec gkqfttsgnl
      481 krhlrihsge kpyvcthcqr qfadpgalqr hvrihtgekp cqcvicgkaf tqassliahv
      541 rqhtgekpyv cercgkrfvq ssqlanhirh hdnirphkcs vcskafvnvg dlskhiiiht
      601 gekpylcdkc grgfnrvdnl rshvktvhqg kagikilepe eggevsvvtv ddmvtlatea
      661 laatavtqlt vvpvgaavta detevlkaei skavkqvqee dpnthilyac dscgdkflda
      721 nslaqhvrih taqalvmfqt dadfyqqygp ggawpagqml qagelvfrpr dgtegqptla
      781 etpptapdcl ppae
//
LOCUS       NP_001423846             596 aa            linear   ROD 24-MAR-2025
DEFINITION  protein CBFA2T1 isoform c [Rattus norvegicus].
ACCESSION   NP_001423846 XP_006237965
VERSION     NP_001423846.1
DBSOURCE    REFSEQ: accession NM_001436917.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006237965.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1254603.1,
                                           SRR26360172.1554205.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840109, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..596
                     /product="protein CBFA2T1 isoform c"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=66229
     Region          114..203
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          329..395
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          435..>489
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          507..543
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..596
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436917.1:64..1854"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 mntkrrcggr aagrlarspp edrtekhstm pdspvdvktq srltppampp ppttqgaprt
       61 ssftpttltn gtshsptaln gapsppngfs ngpsssssss lanqqlppac garqlsklkr
      121 flttlqqfgn dispeigerv rtlvlglvns tltieefhsk lqeatnfplr pfvipflkan
      181 lpllqrellh carlakqnpa qylaqheqll ldasttspvd ssellldvne ngkrrtpdrt
      241 kengfdrepl hsehpskrpc tispgqrysp nnglsyqpng lphptppppq hyrlddmaia
      301 hhyrdsyrhp shrdlrdrnr pmglhgtrqe emidhrltdr ewaeewkhld hllncimdmv
      361 ektrrsltvl rrcqeadree lnywirrysd aedlkkggsg ssshsrqqsp vnpdpvalda
      421 hreflhrpas gyvpeeiwkk aeeavnevkr qamtelqkav seaerkahdm itterakmer
      481 tvaeakrqaa edalavinqq edssescwnc grkasetcsg cntarycgsf cqhkdwekhh
      541 hicgqtlqap qqgetpavss svtpssgags pmdtppaatp rsttpgtpst iettpr
//
LOCUS       NP_001423791             819 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423791 XP_038966007
VERSION     NP_001423791.1
DBSOURCE    REFSEQ: accession NM_001436862.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21641.1,
                                           SRR26643293.31324.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..819
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform a"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=89382
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          322..653
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          352..372
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(385,387,389,391..392,395..396,399,413,415,419..420,
                     423..424,427,441,443,445,447..448,451..452,455)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          464..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(497,499,501,503..504,507..508,511,525,527,531..532,
                     535..536,539,553,555,557,559..560,563..564,567)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          632..651
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..819
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001436862.1:208..2667"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae eggdkrakee kaaatvlsrl dqarssssag pgrelkeewg gqaesasrgf
      181 vpameethlt saqspnpash pssgaeqtek adaprepppv elkpdptssm aaaeaealse
      241 sseqemevep askgeegqee egpgpatvke egvhlengep peeneesagt dsghelgmeg
      301 qnlrsgtygd rteskaygsi ihkcedcgke fthtgnfkrh irihtgekpf screcskafs
      361 dpaackahek thsplkpygc eecgksyrli sllnlhkkrh sgearyrcgd cgklfttsgn
      421 lkrhqlvhsg qkpyqcdycg rsfsdptskm rhlethdtdk ehkcphcdkk fnqvgnlkah
      481 lkihiadgpl kcrecgkqft tsgnlkrhlr ihsgekpyvc thcqrqfadp galqrhvrih
      541 tgekpcqcvi cgkaftqass liahvrqhtg ekpyvcercg krfvqssqla nhirhhdnir
      601 phkcsvcska fvnvgdlskh iiihtgekpy lcdkcgrgfn rvdnlrshvk tvhqgkagik
      661 ilepeeggev svvtvddmvt latealaata vtqltvvpvg aavtadetev lkaeiskavk
      721 qvqeedpnth ilyacdscgd kfldanslaq hvrihtaqal vmfqtdadfy qqygpggawp
      781 agqmlqagel vfrprdgteg qptlaetppt apdclppae
//
LOCUS       NP_001423816             753 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 13
            [Rattus norvegicus].
ACCESSION   NP_001423816 XP_063131569
VERSION     NP_001423816.1
DBSOURCE    REFSEQ: accession NM_001436887.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131569.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50078.1,
                                           SRR26643287.32330.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..753
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 13"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=82672
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>596
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..753
                     /gene="Eps15l1"
                     /coded_by="NM_001436887.1:35..2296"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskg paa
//
LOCUS       NP_001423788             470 aa            linear   ROD 24-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001423788
VERSION     NP_001423788.1
DBSOURCE    REFSEQ: accession NM_001436859.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1139717.1,
                                           SRR26360194.2033830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN17050754, SAMN17050766
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..470
                     /product="heterochromatin protein 1-binding protein 3
                     isoform d"
                     /calculated_mol_wt=52074
     Region          72..156
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(79,91,123,137)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            118..129
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          181..241
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          257..324
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <371..447
                     /region_name="valS"
                     /note="valyl-tRNA synthetase; Provisional; PRK14900"
                     /db_xref="CDD:237855"
     CDS             1..470
                     /gene="Hp1bp3"
                     /coded_by="NM_001436859.1:450..1862"
                     /note="isoform d is encoded by transcript variant 9"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mrlhllhpgr qssprgslrv errkrasllr kprkkkdqsk ekekkvkkti pawatlsasq
       61 laraqkqtpm assprpkmda ilteaikacf qksgasvvai rkyiihkyps ldlerrgyll
      121 kqalkrelnr gvikqvkgkg asgsfvvvqk sktpqksknr kkgsavdpep qvkledvlpl
      181 aftrlcepke asyslirkyv sqyypklrvd irpqllknal qravergqle qitgkgasgt
      241 fqlkksgekp llggslmeya ilsaiaamne pktcsttalk kyvlenhpgt nsnyqmhllk
      301 ktlqkcekng wleqisgkgf sgtfqlcfpy ypspgvlfpk kvsdgseded eeedeeesse
      361 dsedeepppk rslqkktpak pqgktasmkq rgakparkvp aaqrgkvrpl pkkappkakt
      421 parkgrpaps avkkpsgsts kkpvanarke aklpgkgksa mkkksfktkk
//
LOCUS       NP_001423795             794 aa            linear   ROD 24-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423795 XP_063143886
VERSION     NP_001423795.1
DBSOURCE    REFSEQ: accession NM_001436866.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143886.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.29983.1,
                                           SRR26360181.1164224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..794
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform c"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=86820
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          297..628
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(360,362,364,366..367,370..371,374,388,390,394..395,
                     398..399,402,416,418,420,422..423,426..427,430)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(472,474,476,478..479,482..483,486,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..599
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          607..626
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..794
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001436866.1:332..2716"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae eggdkrakee kaaatvlsrl dqarssssag pgrelkeewg gqaesasrga
      181 eqtekadapr epppvelkpd ptssmaaaea ealsesseqe mevepaskge egqeeegpgp
      241 atvkeegvhl engeppeene esagtdsghe lgmegqnlrs gtygdrtesk aygsiihkce
      301 dcgkefthtg nfkrhiriht gekpfscrec skafsdpaac kahekthspl kpygceecgk
      361 syrlisllnl hkkrhsgear yrcgdcgklf ttsgnlkrhq lvhsgqkpyq cdycgrsfsd
      421 ptskmrhlet hdtdkehkcp hcdkkfnqvg nlkahlkihi adgplkcrec gkqfttsgnl
      481 krhlrihsge kpyvcthcqr qfadpgalqr hvrihtgekp cqcvicgkaf tqassliahv
      541 rqhtgekpyv cercgkrfvq ssqlanhirh hdnirphkcs vcskafvnvg dlskhiiiht
      601 gekpylcdkc grgfnrvdnl rshvktvhqg kagikilepe eggevsvvtv ddmvtlatea
      661 laatavtqlt vvpvgaavta detevlkaei skavkqvqee dpnthilyac dscgdkflda
      721 nslaqhvrih taqalvmfqt dadfyqqygp ggawpagqml qagelvfrpr dgtegqptla
      781 etpptapdcl ppae
//
LOCUS       NP_001423811             784 aa            linear   ROD 24-MAR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 8
            [Rattus norvegicus].
ACCESSION   NP_001423811 XP_017455659
VERSION     NP_001423811.1
DBSOURCE    REFSEQ: accession NM_001436882.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017455659.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1029982.1,
                                           SRR26360190.2964261.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..784
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 8"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=86363
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>598
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..784
                     /gene="Eps15l1"
                     /coded_by="NM_001436882.1:35..2389"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamvkd
      601 dpfknkallf snnsqelhpd pfqaedpfks dpfkgadpfk gdpfqsdpfs eqqtavtdpf
      661 ggdpfkesdp fhsstsddff kkqtkndpft sdpftknpsl pskldpfess dpfssssiss
      721 kgsdpfgtld pfgsssfssa egfadfsqms ksprqeelrv crhklqkevg sptcltiqkc
      781 plsl
//
LOCUS       NP_058880                187 aa            linear   ROD 24-MAR-2025
DEFINITION  troponin I, slow skeletal muscle [Rattus norvegicus].
ACCESSION   NP_058880
VERSION     NP_058880.2
DBSOURCE    REFSEQ: accession NM_017184.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Lin,Y.H., Schmidt,W., Fritz,K.S., Jeong,M.Y., Cammarato,A.,
            Foster,D.B., Biesiadecki,B.J., McKinsey,T.A. and Woulfe,K.C.
  TITLE     Site-specific acetyl-mimetic modification of cardiac troponin I
            modulates myofilament relaxation and calcium sensitivity
  JOURNAL   J Mol Cell Cardiol 139, 135-147 (2020)
   PUBMED   31981571
  REMARK    GeneRIF: Site-specific acetyl-mimetic modification of cardiac
            troponin I modulates myofilament relaxation and calcium
            sensitivity.
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Liu,W., Kuang,H., Xia,Y., Pope,Z.C., Wang,Z., Tang,C. and Yin,D.
  TITLE     Regular aerobic exercise-ameliorated troponin I carbonylation to
            mitigate aged rat soleus muscle functional recession
  JOURNAL   Exp Physiol 104 (5), 715-728 (2019)
   PUBMED   30820991
  REMARK    GeneRIF: regular aerobic exercise appeared to have antioxidant
            effects in the muscle that reduced TNNI1 slow carbonylation and
            promoted Ca(2+) /calmodulin-dependent protein kinase IIalpha and
            TNNI1 expression for skeletal muscle contraction regulation
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Potluri,P.R., Chamoun,J., Cooke,J.A., Badr,M., Guse,J.A., Rayes,R.,
            Cordina,N.M., McCamey,D., Fajer,P.G. and Brown,L.J.
  TITLE     The concerted movement of the switch region of Troponin I in
            cardiac muscle thin filaments as tracked by conventional and pulsed
            (DEER) EPR
  JOURNAL   J Struct Biol 200 (3), 376-387 (2017)
   PUBMED   28864299
  REMARK    GeneRIF: Troponin I interaction with calcium and Troponin C in
            cardiac muscle
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Cheng,Y., Rao,V., Tu,A.Y., Lindert,S., Wang,D., Oxenford,L.,
            McCulloch,A.D., McCammon,J.A. and Regnier,M.
  TITLE     Troponin I Mutations R146G and R21C Alter Cardiac Troponin
            Function, Contractile Properties, and Modulation by Protein Kinase
            A (PKA)-mediated Phosphorylation
  JOURNAL   J Biol Chem 290 (46), 27749-27766 (2015)
   PUBMED   26391394
  REMARK    GeneRIF: these results suggest that cTnI(R146G) and cTnI(R21C)
            blunt PKA modulation of activation and relaxation kinetics by
            prohibiting cardiac-specific N-terminal interaction with the cTnI
            inhibitory peptide.
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Christopher,B., Pizarro,G.O., Nicholson,B., Yuen,S., Hoit,B.D. and
            Ogut,O.
  TITLE     Reduced force production during low blood flow to the heart
            correlates with altered troponin I phosphorylation
  JOURNAL   J Muscle Res Cell Motil 30 (3-4), 111-123 (2009)
   PUBMED   19507043
  REMARK    GeneRIF: These findings suggest that altered TnI function, due to
            changes in the distribution of phosphorylated sites, is an early
            contributor to reduced contractility of the heart.
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Takimoto,E., Soergel,D.G., Janssen,P.M., Stull,L.B., Kass,D.A. and
            Murphy,A.M.
  TITLE     Frequency- and afterload-dependent cardiac modulation in vivo by
            troponin I with constitutively active protein kinase A
            phosphorylation sites
  JOURNAL   Circ Res 94 (4), 496-504 (2004)
   PUBMED   14726477
  REMARK    GeneRIF: A novel role is described for cardiac TnI PKA
            phosphorylation in the rate-dependent enhancement of systolic &
            diastolic function in vivo & afterload sensitivity of relaxation.
            This has implications for cardiac failure.
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Westfall,M.V. and Borton,A.R.
  TITLE     Role of troponin I phosphorylation in protein kinase C-mediated
            enhanced contractile performance of rat myocytes
  JOURNAL   J Biol Chem 278 (36), 33694-33700 (2003)
   PUBMED   12815045
  REMARK    GeneRIF: troponin I phosphorylation has a role in protein kinase
            C-mediated enhanced contractile performance of myocytes
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Metzger,J.M., Michele,D.E., Rust,E.M., Borton,A.R. and
            Westfall,M.V.
  TITLE     Sarcomere thin filament regulatory isoforms. Evidence of a dominant
            effect of slow skeletal troponin I on cardiac contraction
  JOURNAL   J Biol Chem 278 (15), 13118-13123 (2003)
   PUBMED   12551900
REFERENCE   9  (residues 1 to 187)
  AUTHORS   Huang,X., Pi,Y., Lee,K.J., Henkel,A.S., Gregg,R.G., Powers,P.A. and
            Walker,J.W.
  TITLE     Cardiac troponin I gene knockout: a mouse model of myocardial
            troponin I deficiency
  JOURNAL   Circ Res 84 (1), 1-8 (1999)
   PUBMED   9915769
REFERENCE   10 (residues 1 to 187)
  AUTHORS   Koppe,R.I., Hallauer,P.L., Karpati,G. and Hastings,K.E.
  TITLE     cDNA clone and expression analysis of rodent fast and slow skeletal
            muscle troponin I mRNAs
  JOURNAL   J Biol Chem 264 (24), 14327-14333 (1989)
   PUBMED   2760067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Nov 26, 2020 this sequence version replaced NP_058880.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217411.1, CR756258.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..187
                     /product="troponin I, slow skeletal muscle"
                     /note="troponin I, skeletal, slow 1; troponin I type 1
                     (skeletal, slow)"
                     /calculated_mol_wt=21567
     Region          2..48
                     /region_name="Involved in binding TNC"
                     /note="propagated from UniProtKB/Swiss-Prot (P13413.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylproline.
                     /evidence=ECO:0000250|UniProtKB:P02645; propagated from
                     UniProtKB/Swiss-Prot (P13413.2)"
     Region          15..146
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P13413.2)"
     Region          97..118
                     /region_name="Involved in binding TNC and actin"
                     /note="propagated from UniProtKB/Swiss-Prot (P13413.2)"
     CDS             1..187
                     /gene="Tnni1"
                     /coded_by="NM_017184.3:124..687"
                     /db_xref="GeneID:29388"
                     /db_xref="RGD:621765"
ORIGIN      
        1 mpeverkski tasrklmlks lmlakakecw eqeheereae kvrylserip tlqtrglsls
       61 alqdlcrelh akvevvdeer ydieakclhn treikdlklk vldlrgkfkr pplrrvrvsa
      121 damlrallgs khkvsmdlra nlksvkkedt ekerpvevgd wrknveamsg megrkkmfda
      181 aksptsq
//
LOCUS       NP_001101464             273 aa            linear   ROD 24-MAR-2025
DEFINITION  SPRY domain-containing SOCS box protein 1 [Rattus norvegicus].
ACCESSION   NP_001101464 XP_001075317 XP_233686
VERSION     NP_001101464.1
DBSOURCE    REFSEQ: accession NM_001107994.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Nishiya,T., Matsumoto,K., Maekawa,S., Kajita,E., Horinouchi,T.,
            Fujimuro,M., Ogasawara,K., Uehara,T. and Miwa,S.
  TITLE     Regulation of inducible nitric-oxide synthase by the SPRY domain-
            and SOCS box-containing proteins
  JOURNAL   J Biol Chem 286 (11), 9009-9019 (2011)
   PUBMED   21199876
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001075317.1, XP_233686.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158603.1, SRR26643293.31629.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..273
                     /product="SPRY domain-containing SOCS box protein 1"
                     /calculated_mol_wt=30640
     Region          54..227
                     /region_name="SPRY_SOCS1-2-4"
                     /note="SPRY domain in the suppressor of cytokine signaling
                     1, 2, 4 families (SOCS1, SOCS2, SOCS4); cd12906"
                     /db_xref="CDD:293963"
     Site            order(77,79,111,129,216..218)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:293963"
     Region          232..273
                     /region_name="SOCS"
                     /note="SOCS (suppressors of cytokine signaling) box. The
                     SOCS box is found in the C-terminal region of CIS/SOCS
                     family proteins (in combination with a SH2 domain), ASBs
                     (ankyrin repeat-containing proteins with a SOCS box), SSBs
                     (SPRY domain-containing proteins...; cl02533"
                     /db_xref="CDD:470605"
     Site            order(233..238,244,254,260)
                     /site_type="active"
                     /note="elongin B/C interaction [active]"
                     /db_xref="CDD:239641"
     CDS             1..273
                     /gene="Spsb1"
                     /gene_synonym="RGD1309319"
                     /coded_by="NM_001107994.3:325..1146"
                     /db_xref="GeneID:313722"
                     /db_xref="RGD:1309319"
ORIGIN      
        1 mgqkvtggik tvdmrdptyr plkqelqgld yckptrldll ldmppvsydv qllhswnnnd
       61 rslnvfvked dklifhrhpv aqstdairgk vgytrglhvw qitwamrqrg thavvgvata
      121 daplhsvgyt tlvgnnhesw gwdlgrnrly hdgknqpskt ypaflepdet fivpdsflva
      181 ldmddgtlsf ivdgqymgva frglkgkkly pvvsavwghc eirmryvngl dpeplplmdl
      241 crrsvrlalg kerlgaipal plpaslkayl lyq
//
LOCUS       NP_037054                277 aa            linear   ROD 24-MAR-2025
DEFINITION  caspase-3 [Rattus norvegicus].
ACCESSION   NP_037054
VERSION     NP_037054.1
DBSOURCE    REFSEQ: accession NM_012922.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Niedermeyer,S., Yun,X., Trujillo,M., Jiang,H., Andrade,M.R.,
            Kolb,T.M., Suresh,K., Damarla,M. and Shimoda,L.A.
  TITLE     A novel interaction between aquaporin 1 and caspase-3 in pulmonary
            arterial smooth muscle cells
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 326 (5), L638-L645 (2024)
   PUBMED   38375595
  REMARK    GeneRIF: A novel interaction between aquaporin 1 and caspase-3 in
            pulmonary arterial smooth muscle cells.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Holota,R., Decmanova,V., Alexovic Matiasova,A., Kosuth,J.,
            Slovinska,L., Pacut,L., Tomori,Z., Daxnerova,Z. and Sevc,J.
  TITLE     Cleaved caspase-3 is present in the majority of glial cells in the
            intact rat spinal cord during postnatal life
  JOURNAL   Histochem Cell Biol 161 (3), 269-286 (2024)
   PUBMED   37938347
  REMARK    GeneRIF: Cleaved caspase-3 is present in the majority of glial
            cells in the intact rat spinal cord during postnatal life.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Tan,W., Li,Y., Ma,L., Fu,X., Long,Q., Yan,F., Li,W., Liu,X.,
            Ding,H., Wang,Y. and Zhang,W.
  TITLE     Exosomes of endothelial progenitor cells repair injured vascular
            endothelial cells through the Bcl2/Bax/Caspase-3 pathway
  JOURNAL   Sci Rep 14 (1), 4465 (2024)
   PUBMED   38396011
  REMARK    GeneRIF: Exosomes of endothelial progenitor cells repair injured
            vascular endothelial cells through the Bcl2/Bax/Caspase-3 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Galichanin,K. and Yu,Z.
  TITLE     Expression of active caspase 3 in the rat lens after in vivo
            exposure to subthreshold dose of UVR-B
  JOURNAL   BMC Ophthalmol 24 (1), 29 (2024)
   PUBMED   38254051
  REMARK    GeneRIF: Expression of active caspase 3 in the rat lens after in
            vivo exposure to subthreshold dose of UVR-B.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Li,C., Zhang,H., Mo,J., Zuo,J. and Ye,L.
  TITLE     Caspase-3/GSDME dependent pyroptosis contributes to offspring lung
            injury induced by gestational PFOS exposure via PERK/ATF4 signaling
  JOURNAL   Arch Toxicol 98 (1), 207-221 (2024)
   PUBMED   37955688
  REMARK    GeneRIF: Caspase-3/GSDME dependent pyroptosis contributes to
            offspring lung injury induced by gestational PFOS exposure via
            PERK/ATF4 signaling.
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Vito,P., Ghayur,T. and D'Adamio,L.
  TITLE     Generation of anti-apoptotic presenilin-2 polypeptides by
            alternative transcription, proteolysis, and caspase-3 cleavage
  JOURNAL   J Biol Chem 272 (45), 28315-28320 (1997)
   PUBMED   9353287
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Ni,B., Wu,X., Du,Y., Su,Y., Hamilton-Byrd,E., Rockey,P.K.,
            Rosteck,P. Jr., Poirier,G.G. and Paul,S.M.
  TITLE     Cloning and expression of a rat brain interleukin-1beta-converting
            enzyme (ICE)-related protease (IRP) and its possible role in
            apoptosis of cultured cerebellar granule neurons
  JOURNAL   J Neurosci 17 (5), 1561-1569 (1997)
   PUBMED   9030616
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Juan,T.S., McNiece,I.K., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.
            and Fletcher,F.A.
  TITLE     Molecular characterization of mouse and rat CPP32 beta gene
            encoding a cysteine protease resembling interleukin-1 beta
            converting enzyme and CED-3
  JOURNAL   Oncogene 13 (4), 749-755 (1996)
   PUBMED   8761296
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Liu,X., Kim,C.N., Yang,J., Jemmerson,R. and Wang,X.
  TITLE     Induction of apoptotic program in cell-free extracts: requirement
            for dATP and cytochrome c
  JOURNAL   Cell 86 (1), 147-157 (1996)
   PUBMED   8689682
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Flaws,J.A., Kugu,K., Trbovich,A.M., DeSanti,A., Tilly,K.I.,
            Hirshfield,A.N. and Tilly,J.L.
  TITLE     Interleukin-1 beta-converting enzyme-related proteases (IRPs) and
            mammalian cell death: dissociation of IRP-induced oligonucleosomal
            endonuclease activity from morphological apoptosis in granulosa
            cells of the ovarian follicle
  JOURNAL   Endocrinology 136 (11), 5042-5053 (1995)
   PUBMED   7588240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081854.1, SRR26360172.2159321.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..277
                     /product="caspase-3"
                     /EC_number="3.4.22.56"
                     /note="IRP; SCA-1; CASP-3; CPP-32; apopain; cysteine
                     protease CPP32; SREBP cleavage activity 1; protein Yama;
                     Caspase 3, apoptosis related cysteine protease (ICE-like
                     cysteine protease); CPP32beta; cysteine protease p32-beta"
                     /calculated_mol_wt=31361
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P70677; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     mat_peptide     29..175
                     /product="Caspase-3 subunit p17.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004591"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=16508
     Region          37..277
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; smart00115"
                     /db_xref="CDD:214521"
     Site            order(64,122,161,168,204..209,213..214)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(121,163)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(169,189..190,197,200,203,226,234,240,260,265..266,
                     268,271..272)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(170,188)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     mat_peptide     176..277
                     /product="Caspase-3 subunit p12.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004592"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=11890
     CDS             1..277
                     /gene="Casp3"
                     /gene_synonym="CPP32-beta; Lice; Yama"
                     /coded_by="NM_012922.3:77..910"
                     /db_xref="GeneID:25402"
                     /db_xref="RGD:2275"
ORIGIN      
        1 mdnnetsvds ksinnfetkt ihgsksmdsg iyldssykmd ypemglciii nnknfhkstg
       61 msarngtdvd aanlretfma lkyevrnknd ltreeimelm dsvskedhsk rssfvcvils
      121 hgdegvifgt ngpvdlkklt sffrgdycrs ltgkpklfii qacrgteldc gietdsgtdd
      181 dmacqkipve adflyaysta pgyyswrnsr dgswfiqslc amlklyahkl efmhiltrvn
      241 rkvatefesf sldatfhakk qipcivsmlt kelyfyh
//
LOCUS       NP_001423870             108 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform e [Rattus norvegicus].
ACCESSION   NP_001423870 XP_063143977
VERSION     NP_001423870.1
DBSOURCE    REFSEQ: accession NM_001436941.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063143977.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.991906.1,
                                           SRR26360181.1773401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..108
                     /product="C-C motif chemokine 27 isoform e"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=12192
     CDS             1..108
                     /gene="Ccl27"
                     /coded_by="NM_001436941.1:206..532"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 meewssedgc agpaepfgar dmsrlrryev aleaeeeiyw gcfyffpwlr mwrrerssah
       61 preqkleplr glmsclssgl rpapqrsgrg llcrtptaaa qtagalki
//
LOCUS       NP_001423873              87 aa            linear   ROD 24-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform f [Rattus norvegicus].
ACCESSION   NP_001423873
VERSION     NP_001423873.1
DBSOURCE    REFSEQ: accession NM_001436944.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1920693.1,
                                           SRR26360181.2473773.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..87
                     /product="C-C motif chemokine 27 isoform f"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=9969
     CDS             1..87
                     /gene="Ccl27"
                     /coded_by="NM_001436944.1:299..562"
                     /note="isoform f is encoded by transcript variant 12"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerssahp reqkleplrg lmsclssglr
       61 papqrsgrgl lcrtptaaaq tagalki
//
LOCUS       NP_001100699            1456 aa            linear   ROD 24-MAR-2025
DEFINITION  GATOR1 complex protein DEPDC5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100699 XP_001065993 XP_223584
VERSION     NP_001100699.1
DBSOURCE    REFSEQ: accession NM_001107229.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1456)
  AUTHORS   Chen,J., Ou,Y., Yang,Y., Li,W., Xu,Y., Xie,Y. and Liu,Y.
  TITLE     KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
            tumorigenesis and ageing
  JOURNAL   Nature 557 (7706), 585-589 (2018)
   PUBMED   29769719
REFERENCE   2  (residues 1 to 1456)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   3  (residues 1 to 1456)
  AUTHORS   Marsan,E., Ishida,S., Schramm,A., Weckhuysen,S., Muraca,G.,
            Lecas,S., Liang,N., Treins,C., Pende,M., Roussel,D., Le Van
            Quyen,M., Mashimo,T., Kaneko,T., Yamamoto,T., Sakuma,T., Mahon,S.,
            Miles,R., Leguern,E., Charpier,S. and Baulac,S.
  TITLE     Depdc5 knockout rat: A novel model of mTORopathy
  JOURNAL   Neurobiol Dis 89, 180-189 (2016)
   PUBMED   26873552
  REMARK    GeneRIF: DEP-domain containing 5 knockout rats exhibit multiple
            features of rodent models of mechanistic target of rapamycin
            complex 1 (mTOR) mTORopathies, and thus, stand as a relevant model
            to study their underlying pathogenic mechanisms.
REFERENCE   4  (residues 1 to 1456)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   5  (residues 1 to 1456)
  AUTHORS   Bar-Peled,L. and Sabatini,D.M.
  TITLE     Regulation of mTORC1 by amino acids
  JOURNAL   Trends Cell Biol 24 (7), 400-406 (2014)
   PUBMED   24698685
  REMARK    Review article
REFERENCE   6  (residues 1 to 1456)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   7  (residues 1 to 1456)
  AUTHORS   Dibbens,L.M., de Vries,B., Donatello,S., Heron,S.E., Hodgson,B.L.,
            Chintawar,S., Crompton,D.E., Hughes,J.N., Bellows,S.T., Klein,K.M.,
            Callenbach,P.M., Corbett,M.A., Gardner,A.E., Kivity,S., Iona,X.,
            Regan,B.M., Weller,C.M., Crimmins,D., O'Brien,T.J.,
            Guerrero-Lopez,R., Mulley,J.C., Dubeau,F., Licchetta,L.,
            Bisulli,F., Cossette,P., Thomas,P.Q., Gecz,J., Serratosa,J.,
            Brouwer,O.F., Andermann,F., Andermann,E., van den Maagdenberg,A.M.,
            Pandolfo,M., Berkovic,S.F. and Scheffer,I.E.
  TITLE     Mutations in DEPDC5 cause familial focal epilepsy with variable
            foci
  JOURNAL   Nat Genet 45 (5), 546-551 (2013)
   PUBMED   23542697
REFERENCE   8  (residues 1 to 1456)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473963.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223584.4, XP_001065993.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132261, SAMD00132262
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1456
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1456
                     /product="GATOR1 complex protein DEPDC5 isoform 1"
                     /note="DEP domain-containing protein 5; GATOR complex
                     protein DEPDC5; GATOR1 complex protein DEPDC5"
                     /calculated_mol_wt=164614
     Region          1..268
                     /region_name="IML1"
                     /note="Vacuolar membrane-associated protein Iml1;
                     pfam12257"
                     /db_xref="CDD:463510"
     Region          1032..1113
                     /region_name="DEP_DEPDC5-like"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in DEPDC5-like proteins. DEPDC5, in human also known
                     as KIAA0645, is a DEP domain containing protein of unknown
                     function; cd04449"
                     /db_xref="CDD:239896"
     Region          1131..1438
                     /region_name="DEPDC5_CTD"
                     /note="DEPDC5 protein C-terminal region; pfam19418"
                     /db_xref="CDD:466071"
     CDS             1..1456
                     /gene="Depdc5"
                     /coded_by="NM_001107229.1:478..4848"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305464"
                     /db_xref="RGD:1311535"
ORIGIN      
        1 mwrlkkslvs tcayitqkve fagiraqage lwvknekvmc gyiseetrvv frstsamvyi
       61 fiqmscemwd fdiygdlyfe kavngfladl ftkwkekncs hevtvvlfsr tfydakside
      121 fpevnrasiq qdhkgrfyed fykvvvqner reewtsllvt ikklfiqypv lvrleqaggf
      181 pqgdnstsaq gnyleainls fnvfdkhyin rnfdrtgqms vvitpgvgvf evdrllmilt
      241 kqrmidngig vdlvcmgeqp lhavplfklh nrsvprdsrl gddyniphwi nhsfytsksq
      301 lfcnsftpri klagkksate ktkngrdtsl gapkesentl piqvdydayd aqvfrlpgps
      361 raqrlatcrs vreqenhnrk sasscdvsss pslpsralpt eevrsqasdd sslgkstnil
      421 mipnphlhqy evssslgyts trdvlenmie ppqrdssapg rfhvgsaesm lhvrpggytp
      481 qralinpfap srmpmkltsn rrrwmhtfpv gpsgeaiqih hqtrqnmael qgsrqrdpth
      541 ssaellelay heaagrhsts rqpgdsmsln fsgteelsvs llsnsgtgmn prnqnkdsle
      601 dgvstspdpm pgfcctvgvd wkslttpacl plttdyfpdr qglqndyteg cydllpeadm
      661 drrdeegvqm taqqvfeefi cqrlmqgyqi ivqpktqkps ttvppplsss plysrglvsr
      721 nrpeeegqyw lsmgrtfhkv tlkdkmitvt rylpkypyes aqihytyslc pshsdsefvs
      781 cwvefcherl eeykwnyldq yicsagsedf slieslkfwr trflllpacv tatkritege
      841 vhcdiygdkp radedewqll dgfirfvegl nrirrrhrsd rmirkgtamk glqmtgpisa
      901 hslestgppv gkkgtsalsa llemeasqks lgeqqtsvhg ksstqpaens svamtptyvd
      961 sprkasvdqt aplvldstsl gvstcqsvdr gnnqtfgnsq nieqafpstg sgdgssqqhi
     1021 assltssstl veileamkhp stgvqllseq kglspccfis aevvhwlmnn vegvqtqamg
     1081 idimqkmlee qliahasgea wrtfvygfyf ykivtdrepe rvamqqpsap whtagvddfa
     1141 sfqrkwfeva fvaeelvhse ipafllpwlp srpasyasrh ssfsrsfggr sqaaallaat
     1201 vpeqrtvtld vdvnnrtdrl ewcscyyhgn fslnaafeik lhwmavtatv lfemvqgwhr
     1261 katscgfllv pvlegpfalp sylygdplra qlfiplnlgc llkegsehlf dsfepetywd
     1321 rmhlfqeaia hrfgfvqdky sasafnfpae nkpqyihvtg tvflqlpysk rkfsgqqrrr
     1381 rnstsstnqn mfceervgyn wayntmltkt wrssatgdek fadrllkdft dfcinrdnrl
     1441 vtfwtnclek mhasap
//
LOCUS       NP_001101821             366 aa            linear   ROD 24-MAR-2025
DEFINITION  SERTA domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_001101821 XP_001069683 XP_341175
VERSION     NP_001101821.1
DBSOURCE    REFSEQ: accession NM_001108351.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473985.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_341175.3, XP_001069683.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00155308, SAMD00155321
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..366
                     /product="SERTA domain-containing protein 4"
                     /calculated_mol_wt=40030
     Region          108..142
                     /region_name="SERTA"
                     /note="SERTA motif; pfam06031"
                     /db_xref="CDD:461806"
     CDS             1..366
                     /gene="Sertad4"
                     /gene_synonym="RGD1565408"
                     /coded_by="NM_001108351.1:193..1293"
                     /db_xref="GeneID:360899"
                     /db_xref="RGD:1565408"
ORIGIN      
        1 mtlvlsmnrf cepivsegaa eiagyhtlwe adsyggaspp gpahvpsqgd rgagpqlags
       61 hyrgisnpvs tpkvtyfkrk yaeeeelptp lsscshktis ifeerahily msleklrfid
      121 dpevylrrsv linnlmkrih geivmqnswy lpacslsgts aqewflaqdc pyrkrprvak
      181 qewekfhtcc fyqecgghcl nlplsvsdgv gsasaaavas passssspst sspsspssss
      241 sslssplplp scshhvdfdv gsapiyksqv paseifvtnv rslgvqekik fnsdgkvshe
      301 tsrdgnalgq epvgndldfe ckgqfydyfe tgyternrms eswkkslrkk elspsnklcc
      361 srggkm
//
LOCUS       NP_001099538             378 aa            linear   ROD 24-MAR-2025
DEFINITION  N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
            precursor [Rattus norvegicus].
ACCESSION   NP_001099538 XP_001069599 XP_224719
VERSION     NP_001099538.1
DBSOURCE    REFSEQ: accession NM_001106068.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Shiraishi,N., Natsume,A., Togayachi,A., Endo,T., Akashima,T.,
            Yamada,Y., Imai,N., Nakagawa,S., Koizumi,S., Sekine,S.,
            Narimatsu,H. and Sasaki,K.
  TITLE     Identification and characterization of three novel beta
            1,3-N-acetylglucosaminyltransferases structurally related to the
            beta 1,3-galactosyltransferase family
  JOURNAL   J Biol Chem 276 (5), 3498-3507 (2001)
   PUBMED   11042166
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474031.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_224719.2, XP_001069599.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132295
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..378
                     /product="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 3 precursor"
                     /EC_number="2.4.1.146"
                     /note="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 3"
                     /calculated_mol_wt=39817
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     Region          119..308
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..378
                     /gene="B3gnt3"
                     /coded_by="NM_001106068.1:93..1229"
                     /db_xref="GeneID:290638"
                     /db_xref="RGD:1305151"
ORIGIN      
        1 mrlprlrpvv slllalaall llltcqspps cpapesptep kddpawapdl srahaapcra
       61 nlsvsahpaf arlpshvrdf llyrhcrdfa vlrepkatkc aqpaflllai ksspanygrr
      121 qvlrttware rrvrgaslrr lflvgsdrdp qqarkfnrll eleakaygdi lqwdfhdsff
      181 nltlkqvlfl ewqrthctna sfvlngdddv fahtdnmvty lqgrdpdqhl fvghliqnvg
      241 pirvpwskyf iptlvtaedk yppycggggf llsrftmaal hraarvlpif piddvflgmc
      301 lqqqglapga hsgvrtagvl ppsprvssfd pcfyrdlllv hrflpfemll mwdalsrpql
      361 acgrqsppll tglggrhp
//
LOCUS       NP_001100707             428 aa            linear   ROD 24-MAR-2025
DEFINITION  DNA-binding protein Ikaros isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100707 XP_001056046 XP_223600
VERSION     NP_001100707.1
DBSOURCE    REFSEQ: accession NM_001107237.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Young,G.P., Symonds,E.L., Nielsen,H.J., Ferm,L., Christensen,I.J.,
            Dekker,E., van der Vlugt,M., Mallant-Hent,R.C., Boulter,N., Yu,B.,
            Chan,M., Tevz,G., LaPointe,L.C. and Pedersen,S.K.
  TITLE     Evaluation of a panel of tumor-specific differentially-methylated
            DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of
            colorectal cancer
  JOURNAL   Clin Epigenetics 13 (1), 14 (2021)
   PUBMED   33478584
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Sharma,B., Shah,R., Jamwal,R.S., Verma,S., Bhat,A., Bhat,G.R.,
            Bakshi,D., Singh,S., Angurana,S., Bhat,A., Vaishnavi,S. and
            Kumar,R.
  TITLE     Evaluation of newly identified Ikaros family zinc finger 1 loci in
            colorectal cancer
  JOURNAL   J Cancer Res Ther 17 (1), 46-50 (2021)
   PUBMED   33723131
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Musher,B.L., Melson,J.E., Amato,G., Chan,D., Hill,M., Khan,I.,
            Kochuparambil,S.T., Lyons,S.E., Orsini,J. Jr., Pedersen,S.K.,
            Robb,B., Saltzman,J., Silinsky,J., Gaur,S., Tuck,M.K.,
            LaPointe,L.C. and Young,G.P.
  TITLE     Evaluation of Circulating Tumor DNA for Methylated BCAT1 and IKZF1
            to Detect Recurrence of Stage II/Stage III Colorectal Cancer (CRC)
  JOURNAL   Cancer Epidemiol Biomarkers Prev 29 (12), 2702-2709 (2020)
   PUBMED   32958500
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Zhao,W., Chen,T.B. and Wang,H.
  TITLE     Ikaros is heterogeneously expressed in lung adenocarcinoma and is
            involved in its progression
  JOURNAL   J Int Med Res 48 (8), 300060520945860 (2020)
   PUBMED   32787735
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Symonds,E.L., Pedersen,S.K., Murray,D., Byrne,S.E., Roy,A.,
            Karapetis,C., Hollington,P., Rabbitt,P., Jones,F.S., LaPointe,L.,
            Segelov,E. and Young,G.P.
  TITLE     Circulating epigenetic biomarkers for detection of recurrent
            colorectal cancer
  JOURNAL   Cancer 126 (7), 1460-1469 (2020)
   PUBMED   31909823
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Honma,Y., Kiyosawa,H., Mori,T., Oguri,A., Nikaido,T., Kanazawa,K.,
            Tojo,M., Takeda,J., Tanno,Y., Yokoya,S., Kawabata,I., Ikeda,H. and
            Wanaka,A.
  TITLE     Eos: a novel member of the Ikaros gene family expressed
            predominantly in the developing nervous system
  JOURNAL   FEBS Lett 447 (1), 76-80 (1999)
   PUBMED   10218586
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Kelley,C.M., Ikeda,T., Koipally,J., Avitahl,N., Wu,L.,
            Georgopoulos,K. and Morgan,B.A.
  TITLE     Helios, a novel dimerization partner of Ikaros expressed in the
            earliest hematopoietic progenitors
  JOURNAL   Curr Biol 8 (9), 508-515 (1998)
   PUBMED   9560339
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Boggs,S.S., Trevisan,M., Patrene,K. and Geogopoulos,K.
  TITLE     Lack of natural killer cell precursors in fetal liver of Ikaros
            knockout mutant mice
  JOURNAL   Nat Immun 16 (4), 137-145 (1998)
   PUBMED   10366784
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Molnar,A. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of functionally diverse zinc
            finger DNA-binding proteins
  JOURNAL   Mol Cell Biol 14 (12), 8292-8303 (1994)
   PUBMED   7969165
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Georgopoulos,K., Bigby,M., Wang,J.H., Molnar,A., Wu,P., Winandy,S.
            and Sharpe,A.
  TITLE     The Ikaros gene is required for the development of all lymphoid
            lineages
  JOURNAL   Cell 79 (1), 143-156 (1994)
   PUBMED   7923373
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474055.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001056046.1, XP_223600.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680412,
                              SAMN06680417 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..428
                     /product="DNA-binding protein Ikaros isoform 1"
                     /note="DNA-binding protein Ikaros"
                     /calculated_mol_wt=47806
     Region          <1..>130
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          57..79
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          59..79
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(64,66,68,70..71,74..75,78,92,94,98..99,102..103,106,
                     120,122,124,126..127,130..131,135)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          71..96
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          87..107
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          115..136
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..428
                     /gene="Ikzf1"
                     /gene_synonym="RGD1562979"
                     /coded_by="NM_001107237.1:213..1499"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305501"
                     /db_xref="RGD:1562979"
ORIGIN      
        1 mdvdegqdms qvsgkesppv sdtpdegdep mpvpedlsts gaqqnsksdr gmgerpfqcn
       61 qcgasftqkg nllrhiklhs gekpfkchlc nyacrrrdal tghlrthsvg kphkcgycgr
      121 sykqrsslee hkerchnyle smglpgmypv ikeetnhsem aedlckigae rslvldrlas
      181 nvakrkssmp qkflgdkcls dmpydsanye kdemmtshvm dqainnainy lgaeslrplv
      241 qtppgssevv pvissmyqlh kppsdgpprs nhsaqdsave nllllskaks vssereasps
      301 nscqdstdte snaeeqrsgl iyltnhitph arnglalkee qrayevlraa sensqdafrv
      361 vstsgeqlkv ykcehcrvlf ldhvmytihm gchgfrdpfe cnmcgyhsqd ryefsshitr
      421 gehryhls
//
LOCUS       NP_001423895             475 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001423895 XP_063143981
VERSION     NP_001423895.1
DBSOURCE    REFSEQ: accession NM_001436966.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143981.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1520231.1,
                                           SRR26360194.149824.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..475
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform b"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=53325
     Region          169..>405
                     /region_name="TrhO"
                     /note="tRNA U34 5'-hydroxylase TrhO, rhodanese family
                     [Translation, ribosomal structure and biogenesis];
                     COG1054"
                     /db_xref="CDD:440674"
     CDS             1..475
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436966.1:275..1702"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsgsgk
      421 sglwreqwtk sssgydksrs lcpqhpqhil klknlpgsvy lsdplpsfht mscsp
//
LOCUS       NP_001101829             292 aa            linear   ROD 25-MAR-2025
DEFINITION  DCN1-like protein 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001101829 XP_001068939 XP_341207
VERSION     NP_001101829.1
DBSOURCE    REFSEQ: accession NM_001108359.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001068939.1, XP_341207.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2194291.1,
                                           SRR26360190.3167530.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..292
                     /product="DCN1-like protein 4 isoform 1"
                     /note="DCN1-like protein 4; DCN1, defective in cullin
                     neddylation 1, domain containing 4"
                     /calculated_mol_wt=33835
     Region          175..285
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..292
                     /gene="Dcun1d4"
                     /gene_synonym="RGD1310422"
                     /coded_by="NM_001108359.2:109..987"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360928"
                     /db_xref="RGD:1310422"
ORIGIN      
        1 mhsdaaavnf qlnshlstla nihkiyhtln klnltedvgq ddhqtgslrs csssdcfskv
       61 mpprkkrrpa sgddlsakks rhdsmyrkye strikteeea fsskrclewf yeyagtedav
      121 gpegmekfce digvepenvv mlvlawklda qnmgyftlqe wlkgmtslqc dtteklrttl
      181 dylrsllndt tnfkliyrya fdfarekdqr sldintakcm lglllgkiwp lfpvfhqfle
      241 qskykvinkd qwcnvlefsr tisldlsnyd edgawpvlld efvewykdkq ms
//
LOCUS       NP_001423896             475 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001423896 XP_063143980
VERSION     NP_001423896.1
DBSOURCE    REFSEQ: accession NM_001436967.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143980.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2251424.1,
                                           SRR26360190.72806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..475
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform b"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=53325
     Region          169..>405
                     /region_name="TrhO"
                     /note="tRNA U34 5'-hydroxylase TrhO, rhodanese family
                     [Translation, ribosomal structure and biogenesis];
                     COG1054"
                     /db_xref="CDD:440674"
     CDS             1..475
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436967.1:275..1702"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsgsgk
      421 sglwreqwtk sssgydksrs lcpqhpqhil klknlpgsvy lsdplpsfht mscsp
//
LOCUS       NP_001423897             475 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001423897 XP_006238152
VERSION     NP_001423897.1
DBSOURCE    REFSEQ: accession NM_001436968.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006238152.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1176755.1,
                                           SRR26360176.1415762.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..475
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform b"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=53325
     Region          169..>405
                     /region_name="TrhO"
                     /note="tRNA U34 5'-hydroxylase TrhO, rhodanese family
                     [Translation, ribosomal structure and biogenesis];
                     COG1054"
                     /db_xref="CDD:440674"
     CDS             1..475
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436968.1:110..1537"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsgsgk
      421 sglwreqwtk sssgydksrs lcpqhpqhil klknlpgsvy lsdplpsfht mscsp
//
LOCUS       NP_001423934             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423934 XP_063143991
VERSION     NP_001423934.1
DBSOURCE    REFSEQ: accession NM_001437005.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143991.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18996.1,
                                           SRR26643287.13259.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437005.1:317..1702"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423914             255 aa            linear   ROD 25-MAR-2025
DEFINITION  DCN1-like protein 4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423914 XP_006250969
VERSION     NP_001423914.1
DBSOURCE    REFSEQ: accession NM_001436985.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006250969.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.43230.1,
                                           SRR26643290.44242.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..255
                     /product="DCN1-like protein 4 isoform 4"
                     /note="DCN1-like protein 4; DCN1, defective in cullin
                     neddylation 1, domain containing 4"
                     /calculated_mol_wt=29679
     Region          138..248
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..255
                     /gene="Dcun1d4"
                     /gene_synonym="RGD1310422"
                     /coded_by="NM_001436985.1:109..876"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:360928"
                     /db_xref="RGD:1310422"
ORIGIN      
        1 mhsdaaavrs lrscsssdcf skvmpprkkr rpasgddlsa kksrhdsmyr kyestrikte
       61 eeafsskrcl ewfyeyagte davgpegmek fcedigvepe nvvmlvlawk ldaqnmgyft
      121 lqewlkgmts lqcdtteklr ttldylrsll ndttnfkliy ryafdfarek dqrsldinta
      181 kcmlglllgk iwplfpvfhq fleqskykvi nkdqwcnvle fsrtisldls nydedgawpv
      241 lldefvewyk dkqms
//
LOCUS       NP_001423917             465 aa            linear   ROD 25-MAR-2025
DEFINITION  homeobox protein Meis1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423917 XP_063129698
VERSION     NP_001423917.1
DBSOURCE    REFSEQ: accession NM_001436988.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Yao,M.Z., Ge,X.Y., Liu,T., Huang,N., Liu,H., Chen,Y., Zhang,Z. and
            Hu,C.P.
  TITLE     MEIS1 regulated proliferation and migration of pulmonary artery
            smooth muscle cells in hypoxia-induced pulmonary hypertension
  JOURNAL   Life Sci 255, 117822 (2020)
   PUBMED   32450174
  REMARK    GeneRIF: MEIS1 regulated the proliferation and migration of
            pulmonary artery smooth muscle cells during hypoxia-induced
            pulmonary hypertension
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,Y., Si,Y. and Ma,N.
  TITLE     Meis1 promotes poly (rC)-binding protein 2 expression and inhibits
            angiotensin II-induced cardiomyocyte hypertrophy
  JOURNAL   IUBMB Life 68 (1), 13-22 (2016)
   PUBMED   26597775
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Pandey,R., Yang,Y., Jackson,L. and Ahmed,R.P.
  TITLE     MicroRNAs regulating meis1 expression and inducing cardiomyocyte
            proliferation
  JOURNAL   Cardiovasc Regen Med 3 (2016)
   PUBMED   28111633
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Jolma,A., Yin,Y., Nitta,K.R., Dave,K., Popov,A., Taipale,M.,
            Enge,M., Kivioja,T., Morgunova,E. and Taipale,J.
  TITLE     DNA-dependent formation of transcription factor pairs alters their
            binding specificity
  JOURNAL   Nature 527 (7578), 384-388 (2015)
   PUBMED   26550823
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Spieler,D., Kaffe,M., Knauf,F., Bessa,J., Tena,J.J., Giesert,F.,
            Schormair,B., Tilch,E., Lee,H., Horsch,M., Czamara,D., Karbalai,N.,
            von Toerne,C., Waldenberger,M., Gieger,C., Lichtner,P.,
            Claussnitzer,M., Naumann,R., Muller-Myhsok,B., Torres,M.,
            Garrett,L., Rozman,J., Klingenspor,M., Gailus-Durner,V., Fuchs,H.,
            Hrabe de Angelis,M., Beckers,J., Holter,S.M., Meitinger,T.,
            Hauck,S.M., Laumen,H., Wurst,W., Casares,F., Gomez-Skarmeta,J.L.
            and Winkelmann,J.
  TITLE     Restless legs syndrome-associated intronic common variant in Meis1
            alters enhancer function in the developing telencephalon
  JOURNAL   Genome Res 24 (4), 592-603 (2014)
   PUBMED   24642863
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Toresson,H., Parmar,M. and Campbell,K.
  TITLE     Expression of Meis and Pbx genes and their protein products in the
            developing telencephalon: implications for regional differentiation
  JOURNAL   Mech Dev 94 (1-2), 183-187 (2000)
   PUBMED   10842069
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Jacobs,Y., Schnabel,C.A. and Cleary,M.L.
  TITLE     Trimeric association of Hox and TALE homeodomain proteins mediates
            Hoxb2 hindbrain enhancer activity
  JOURNAL   Mol Cell Biol 19 (7), 5134-5142 (1999)
   PUBMED   10373562
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Knoepfler,P.S., Calvo,K.R., Chen,H., Antonarakis,S.E. and
            Kamps,M.P.
  TITLE     Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an
            interaction surface disrupted in oncoprotein E2a-Pbx1
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14553-14558 (1997)
   PUBMED   9405651
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Shen,W.F., Montgomery,J.C., Rozenfeld,S., Moskow,J.J.,
            Lawrence,H.J., Buchberg,A.M. and Largman,C.
  TITLE     AbdB-like Hox proteins stabilize DNA binding by the Meis1
            homeodomain proteins
  JOURNAL   Mol Cell Biol 17 (11), 6448-6458 (1997)
   PUBMED   9343407
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Chang,C.P., Jacobs,Y., Nakamura,T., Jenkins,N.A., Copeland,N.G. and
            Cleary,M.L.
  TITLE     Meis proteins are major in vivo DNA binding partners for wild-type
            but not chimeric Pbx proteins
  JOURNAL   Mol Cell Biol 17 (10), 5679-5687 (1997)
   PUBMED   9315626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063129698.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.62063.1,
                                           SRR21887623.80887.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..465
                     /product="homeobox protein Meis1 isoform 2"
                     /note="homeobox protein Meis1; Meis1, myeloid ecotropic
                     viral integration site 1 homolog"
                     /calculated_mol_wt=50587
     Region          108..192
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Site            order(278,321,324..325,328)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          291..329
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          <326..449
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     CDS             1..465
                     /gene="Meis1"
                     /coded_by="NM_001436988.1:727..2124"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:686117"
                     /db_xref="RGD:1585482"
ORIGIN      
        1 maqryddlph yggmdgvgip stmygdphaa rsmqpvhhln hgpplhshqy phtahtnama
       61 psmgssvnda lkrdkdaiyg hplfpllali fekcelatct prepgvaggd vcssesfned
      121 iavfakqira ekplfssnpe ldnlmiqaiq vlrfhllele kvhelcdnfc hryisclkgk
      181 mpidlviddr eggsksdsed vtraanltdq pswnrdhddt astrsggtpg pssgghtshs
      241 gdnsseqgdg ldnsvaspst gddddpdkdk krhkkrgifp kvatnimraw lfqhlthpyp
      301 seeqkkqlaq dtgltilqvn nwfinarrri vqpmidqsnr agnqgtpynp dgqpmggfvm
      361 dgqqhmgira pglqsmpgey varggpmgvs mgqpsytqaq mpphpaqlrh gppmhtyipg
      421 hphhpavmmh ggqphpgmpm sasspsvlnt gdptmsgqvm nihaq
//
LOCUS       NP_001423913             257 aa            linear   ROD 25-MAR-2025
DEFINITION  DCN1-like protein 4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423913 XP_063129407
VERSION     NP_001423913.1
DBSOURCE    REFSEQ: accession NM_001436984.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063129407.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.54138.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..257
                     /product="DCN1-like protein 4 isoform 3"
                     /note="DCN1-like protein 4; DCN1, defective in cullin
                     neddylation 1, domain containing 4"
                     /calculated_mol_wt=29752
     Region          175..250
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..257
                     /gene="Dcun1d4"
                     /gene_synonym="RGD1310422"
                     /coded_by="NM_001436984.1:109..882"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:360928"
                     /db_xref="RGD:1310422"
ORIGIN      
        1 mhsdaaavnf qlnshlstla nihkiyhtln klnltedvgq ddhqtgslrs csssdcfskv
       61 mpprkkrrpa sgddlsakks rhdsmyrkye strikteeea fsskrclewf yeyagtedav
      121 gpegmekfce digvepenvv mlvlawklda qnmgyftlqe wlkgmtslqc dtteklrttl
      181 dylrsllndt tnfkliyrya fdfarqskyk vinkdqwcnv lefsrtisld lsnydedgaw
      241 pvlldefvew ykdkqms
//
LOCUS       NP_001423940             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423940
VERSION     NP_001423940.1
DBSOURCE    REFSEQ: accession NM_001437011.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2410013.1,
                                           SRR22582419.714723.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN17050752
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437011.1:868..2253"
                     /note="isoform a is encoded by transcript variant 8"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423894             475 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001423894 XP_063143982
VERSION     NP_001423894.1
DBSOURCE    REFSEQ: accession NM_001436965.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143982.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.19197.1,
                                           SRR26643429.19404.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..475
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform b"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=53325
     Region          169..>405
                     /region_name="TrhO"
                     /note="tRNA U34 5'-hydroxylase TrhO, rhodanese family
                     [Translation, ribosomal structure and biogenesis];
                     COG1054"
                     /db_xref="CDD:440674"
     CDS             1..475
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436965.1:275..1702"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsgsgk
      421 sglwreqwtk sssgydksrs lcpqhpqhil klknlpgsvy lsdplpsfht mscsp
//
LOCUS       NP_001423893             493 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform a [Rattus norvegicus].
ACCESSION   NP_001423893 XP_063143979
VERSION     NP_001423893.1
DBSOURCE    REFSEQ: accession NM_001436964.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143979.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18847.1,
                                           SRR26643296.15133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840111 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..493
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform a"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=55342
     Region          169..459
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            354
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238776"
     CDS             1..493
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436964.1:281..1762"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsecsy
      421 cgapwdqykl cstpqcrqlv ltcsacqgqg ftaccvmcqd kggkqasdpt qdsfkeecec
      481 tarrpripqe qra
//
LOCUS       NP_001423902             275 aa            linear   ROD 25-MAR-2025
DEFINITION  myb/SANT-like DNA-binding domain-containing protein 3 [Rattus
            norvegicus].
ACCESSION   NP_001423902 XP_038966170
VERSION     NP_001423902.1
DBSOURCE    REFSEQ: accession NM_001436973.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Oleskevich,S., Leck,K.J., Matthaei,K. and Hendry,I.A.
  TITLE     Enhanced serotonin response in the hippocampus of Galphaz protein
            knock-out mice
  JOURNAL   Neuroreport 16 (9), 921-925 (2005)
   PUBMED   15931062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_038966170.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.21273.1,
                                           SRR26360186.1742771.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..275
                     /product="myb/SANT-like DNA-binding domain-containing
                     protein 3"
                     /note="Myb/SANT-like DNA-binding domain containing 3"
                     /calculated_mol_wt=32245
     Region          10..87
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     CDS             1..275
                     /gene="Msantd3"
                     /gene_synonym="RGD1308165"
                     /coded_by="NM_001436973.1:147..974"
                     /db_xref="GeneID:362516"
                     /db_xref="RGD:1308165"
ORIGIN      
        1 mqnneiikpa kyfseleksi llalvekyky vleckksdar tialkqrtwq alaheynsqp
       61 svslrdfkql kkcwenikar tkkimaherr ekvkrsgspl lsthvldkek igsmlpeqly
      121 flqsppeeep eyhqdaaaqe sfavsnrelc ddekefvhfp vcegtsqpep scsavritan
      181 knyrsktpqe galkkmheee hhqqmsilql qliqmnevhv akiqqierec emaeeehrik
      241 mevlnkkkmy werklqtftk ewpvssfnrp fpnsp
//
LOCUS       NP_001423899             300 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform c [Rattus norvegicus].
ACCESSION   NP_001423899
VERSION     NP_001423899.1
DBSOURCE    REFSEQ: accession NM_001436970.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO768849.1, SRR26360176.573906.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840132,
                                           SAMN16676784 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..300
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform c"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=33773
     Region          169..>267
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     CDS             1..300
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436970.1:110..1012"
                     /note="isoform c is encoded by transcript variant 9"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgml mfyrsvtlrh rykvykkvky
//
LOCUS       NP_001423939             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423939
VERSION     NP_001423939.1
DBSOURCE    REFSEQ: accession NM_001437010.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.21333.1,
                                           SRR26643297.18991.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437010.1:180..1565"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423936             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423936 XP_008761934
VERSION     NP_001423936.1
DBSOURCE    REFSEQ: accession NM_001437007.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_008761934.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18992.1,
                                           SRR26360176.1245506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437007.1:472..1857"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001102133             493 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform a [Rattus norvegicus].
ACCESSION   NP_001102133 XP_001071828 XP_342833
VERSION     NP_001102133.1
DBSOURCE    REFSEQ: accession NM_001108663.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342833.2, XP_001071828.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.21183.1,
                                           SRR26643287.13162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..493
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform a"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=55342
     Region          169..459
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            354
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238776"
     CDS             1..493
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001108663.2:275..1756"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsecsy
      421 cgapwdqykl cstpqcrqlv ltcsacqgqg ftaccvmcqd kggkqasdpt qdsfkeecec
      481 tarrpripqe qra
//
LOCUS       NP_001102134             275 aa            linear   ROD 25-MAR-2025
DEFINITION  myb/SANT-like DNA-binding domain-containing protein 3 [Rattus
            norvegicus].
ACCESSION   NP_001102134 XP_001055826 XP_342835
VERSION     NP_001102134.1
DBSOURCE    REFSEQ: accession NM_001108664.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Oleskevich,S., Leck,K.J., Matthaei,K. and Hendry,I.A.
  TITLE     Enhanced serotonin response in the hippocampus of Galphaz protein
            knock-out mice
  JOURNAL   Neuroreport 16 (9), 921-925 (2005)
   PUBMED   15931062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342835.1, XP_001055826.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26643285.19280.1, CB585133.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN12840111, SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..275
                     /product="myb/SANT-like DNA-binding domain-containing
                     protein 3"
                     /note="Myb/SANT-like DNA-binding domain containing 3"
                     /calculated_mol_wt=32245
     Region          10..87
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     CDS             1..275
                     /gene="Msantd3"
                     /gene_synonym="RGD1308165"
                     /coded_by="NM_001108664.2:63..890"
                     /db_xref="GeneID:362516"
                     /db_xref="RGD:1308165"
ORIGIN      
        1 mqnneiikpa kyfseleksi llalvekyky vleckksdar tialkqrtwq alaheynsqp
       61 svslrdfkql kkcwenikar tkkimaherr ekvkrsgspl lsthvldkek igsmlpeqly
      121 flqsppeeep eyhqdaaaqe sfavsnrelc ddekefvhfp vcegtsqpep scsavritan
      181 knyrsktpqe galkkmheee hhqqmsilql qliqmnevhv akiqqierec emaeeehrik
      241 mevlnkkkmy werklqtftk ewpvssfnrp fpnsp
//
LOCUS       NP_001128174             390 aa            linear   ROD 25-MAR-2025
DEFINITION  homeobox protein Meis1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001128174 XP_001054791 XP_001054850 XP_001054906 XP_001054960
            XP_001055028 XP_001070142 XP_001070196 XP_001070244 XP_001070286
            XP_001070326
VERSION     NP_001128174.1
DBSOURCE    REFSEQ: accession NM_001134702.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Yao,M.Z., Ge,X.Y., Liu,T., Huang,N., Liu,H., Chen,Y., Zhang,Z. and
            Hu,C.P.
  TITLE     MEIS1 regulated proliferation and migration of pulmonary artery
            smooth muscle cells in hypoxia-induced pulmonary hypertension
  JOURNAL   Life Sci 255, 117822 (2020)
   PUBMED   32450174
  REMARK    GeneRIF: MEIS1 regulated the proliferation and migration of
            pulmonary artery smooth muscle cells during hypoxia-induced
            pulmonary hypertension
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Zhang,Y., Si,Y. and Ma,N.
  TITLE     Meis1 promotes poly (rC)-binding protein 2 expression and inhibits
            angiotensin II-induced cardiomyocyte hypertrophy
  JOURNAL   IUBMB Life 68 (1), 13-22 (2016)
   PUBMED   26597775
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pandey,R., Yang,Y., Jackson,L. and Ahmed,R.P.
  TITLE     MicroRNAs regulating meis1 expression and inducing cardiomyocyte
            proliferation
  JOURNAL   Cardiovasc Regen Med 3 (2016)
   PUBMED   28111633
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Jolma,A., Yin,Y., Nitta,K.R., Dave,K., Popov,A., Taipale,M.,
            Enge,M., Kivioja,T., Morgunova,E. and Taipale,J.
  TITLE     DNA-dependent formation of transcription factor pairs alters their
            binding specificity
  JOURNAL   Nature 527 (7578), 384-388 (2015)
   PUBMED   26550823
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Spieler,D., Kaffe,M., Knauf,F., Bessa,J., Tena,J.J., Giesert,F.,
            Schormair,B., Tilch,E., Lee,H., Horsch,M., Czamara,D., Karbalai,N.,
            von Toerne,C., Waldenberger,M., Gieger,C., Lichtner,P.,
            Claussnitzer,M., Naumann,R., Muller-Myhsok,B., Torres,M.,
            Garrett,L., Rozman,J., Klingenspor,M., Gailus-Durner,V., Fuchs,H.,
            Hrabe de Angelis,M., Beckers,J., Holter,S.M., Meitinger,T.,
            Hauck,S.M., Laumen,H., Wurst,W., Casares,F., Gomez-Skarmeta,J.L.
            and Winkelmann,J.
  TITLE     Restless legs syndrome-associated intronic common variant in Meis1
            alters enhancer function in the developing telencephalon
  JOURNAL   Genome Res 24 (4), 592-603 (2014)
   PUBMED   24642863
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Toresson,H., Parmar,M. and Campbell,K.
  TITLE     Expression of Meis and Pbx genes and their protein products in the
            developing telencephalon: implications for regional differentiation
  JOURNAL   Mech Dev 94 (1-2), 183-187 (2000)
   PUBMED   10842069
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Jacobs,Y., Schnabel,C.A. and Cleary,M.L.
  TITLE     Trimeric association of Hox and TALE homeodomain proteins mediates
            Hoxb2 hindbrain enhancer activity
  JOURNAL   Mol Cell Biol 19 (7), 5134-5142 (1999)
   PUBMED   10373562
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Knoepfler,P.S., Calvo,K.R., Chen,H., Antonarakis,S.E. and
            Kamps,M.P.
  TITLE     Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an
            interaction surface disrupted in oncoprotein E2a-Pbx1
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14553-14558 (1997)
   PUBMED   9405651
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Shen,W.F., Montgomery,J.C., Rozenfeld,S., Moskow,J.J.,
            Lawrence,H.J., Buchberg,A.M. and Largman,C.
  TITLE     AbdB-like Hox proteins stabilize DNA binding by the Meis1
            homeodomain proteins
  JOURNAL   Mol Cell Biol 17 (11), 6448-6458 (1997)
   PUBMED   9343407
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Chang,C.P., Jacobs,Y., Nakamura,T., Jenkins,N.A., Copeland,N.G. and
            Cleary,M.L.
  TITLE     Meis proteins are major in vivo DNA binding partners for wild-type
            but not chimeric Pbx proteins
  JOURNAL   Mol Cell Biol 17 (10), 5679-5687 (1997)
   PUBMED   9315626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Sep 5, 2008 this sequence version replaced
            XP_001054960.1, XP_001055028.1, XP_001054850.1, XP_001054791.1,
            XP_001054906.1, XP_001070286.1, XP_001070326.1, XP_001070196.1,
            XP_001070244.1, XP_001070142.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161984.1, SRR26643291.36107.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..390
                     /product="homeobox protein Meis1 isoform 1"
                     /note="homeobox protein Meis1; Meis1, myeloid ecotropic
                     viral integration site 1 homolog"
                     /calculated_mol_wt=42855
     Region          108..192
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Site            order(278,321,324..325,328)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          291..329
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     CDS             1..390
                     /gene="Meis1"
                     /coded_by="NM_001134702.2:727..1899"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:686117"
                     /db_xref="RGD:1585482"
ORIGIN      
        1 maqryddlph yggmdgvgip stmygdphaa rsmqpvhhln hgpplhshqy phtahtnama
       61 psmgssvnda lkrdkdaiyg hplfpllali fekcelatct prepgvaggd vcssesfned
      121 iavfakqira ekplfssnpe ldnlmiqaiq vlrfhllele kvhelcdnfc hryisclkgk
      181 mpidlviddr eggsksdsed vtraanltdq pswnrdhddt astrsggtpg pssgghtshs
      241 gdnsseqgdg ldnsvaspst gddddpdkdk krhkkrgifp kvatnimraw lfqhlthpyp
      301 seeqkkqlaq dtgltilqvn nwfinarrri vqpmidqsnr avsqgtpynp dgqpmggfvm
      361 dgqqhmgira pgpmsgmgmn mgmegqwhym
//
LOCUS       NP_001102137             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001102137 XP_001057514 XP_342839
VERSION     NP_001102137.1
DBSOURCE    REFSEQ: accession NM_001108667.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342839.1, XP_001057514.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2284575.1,
                                           SRR26360172.159457.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001108667.2:107..1492"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423943             317 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform c [Rattus norvegicus].
ACCESSION   NP_001423943 XP_038966176
VERSION     NP_001423943.1
DBSOURCE    REFSEQ: accession NM_001437014.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_038966176.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2233762.1,
                                           SRR26643297.18997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..317
                     /product="ribitol-5-phosphate transferase FKTN isoform c"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=36227
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     CDS             1..317
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437014.1:262..1215"
                     /note="isoform c is encoded by transcript variant 11"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgicspsl hcagrsl
//
LOCUS       NP_001423942             317 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform c [Rattus norvegicus].
ACCESSION   NP_001423942 XP_063143997
VERSION     NP_001423942.1
DBSOURCE    REFSEQ: accession NM_001437013.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143997.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.948531.1,
                                           SRR26643299.22863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..317
                     /product="ribitol-5-phosphate transferase FKTN isoform c"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=36227
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     CDS             1..317
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437013.1:107..1060"
                     /note="isoform c is encoded by transcript variant 10"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgicspsl hcagrsl
//
LOCUS       NP_001423937             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423937 XP_063143993
VERSION     NP_001423937.1
DBSOURCE    REFSEQ: accession NM_001437008.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_063143993.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.27356.1,
                                           SRR26360194.384153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437008.1:658..2043"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423898             300 aa            linear   ROD 25-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform c [Rattus norvegicus].
ACCESSION   NP_001423898
VERSION     NP_001423898.1
DBSOURCE    REFSEQ: accession NM_001436969.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.770443.1,
                                           SRR26360194.841120.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840117,
                                           SAMN12840132 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..300
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform c"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=33773
     Region          169..>267
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     CDS             1..300
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436969.1:281..1183"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgml mfyrsvtlrh rykvykkvky
//
LOCUS       NP_001423935             461 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423935 XP_006238228
VERSION     NP_001423935.1
DBSOURCE    REFSEQ: accession NM_001437006.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006238228.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18993.1,
                                           SRR26643293.27878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437006.1:390..1775"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423941             370 aa            linear   ROD 25-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform b [Rattus norvegicus].
ACCESSION   NP_001423941 XP_038966175
VERSION     NP_001423941.1
DBSOURCE    REFSEQ: accession NM_001437012.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_038966175.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.13262.1,
                                           SRR26643297.19000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..370
                     /product="ribitol-5-phosphate transferase FKTN isoform b"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=42381
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..370
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437012.1:262..1374"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkvs vpqvytvldg
      361 vcrhkspcsl
//
LOCUS       NP_001011973             440 aa            linear   ROD 25-MAR-2025
DEFINITION  actin-like protein 7A [Rattus norvegicus].
ACCESSION   NP_001011973 XP_232920
VERSION     NP_001011973.1
DBSOURCE    REFSEQ: accession NM_001011973.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Afsharpad,M., Nowroozi,M.R., Mobasheri,M.B., Ayati,M.,
            Nekoohesh,L., Saffari,M., Zendehdel,K. and Modarressi,M.H.
  TITLE     Cancer-Testis Antigens as New Candidate Diagnostic Biomarkers for
            Transitional Cell Carcinoma of Bladder
  JOURNAL   Pathol Oncol Res 25 (1), 191-199 (2019)
   PUBMED   29058301
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Fu,J., Yao,R., Luo,Y., Yang,D., Cao,Y., Qiu,Y., Song,W., Miao,S.,
            Gu,Y. and Wang,L.
  TITLE     Immune Infertility Should Be Positively Diagnosed Using an Accurate
            Method by Monitoring the Level of Anti-ACTL7a Antibody
  JOURNAL   Sci Rep 6, 22844 (2016)
   PUBMED   26957350
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Boeda,B., Knowles,P.P., Briggs,D.C., Murray-Rust,J., Soriano,E.,
            Garvalov,B.K., McDonald,N.Q. and Way,M.
  TITLE     Molecular recognition of the Tes LIM2-3 domains by the
            actin-related protein Arp7A
  JOURNAL   J Biol Chem 286 (13), 11543-11554 (2011)
   PUBMED   21278383
  REMARK    GeneRIF: Molecular recognition of the Tes LIM2-3 domains by the
            actin-related protein Arp7A.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Tanaka,H., Iguchi,N., Egydio de Carvalho,C., Tadokoro,Y.,
            Yomogida,K. and Nishimune,Y.
  TITLE     Novel actin-like proteins T-ACTIN 1 and T-ACTIN 2 are
            differentially expressed in the cytoplasm and nucleus of mouse
            haploid germ cells
  JOURNAL   Biol Reprod 69 (2), 475-482 (2003)
   PUBMED   12672658
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Feb 11, 2005 this sequence version replaced XP_232920.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26360186.1932091.1, BC082101.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..440
                     /product="actin-like protein 7A"
                     /calculated_mol_wt=49437
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W9.1)"
     Region          6..70
                     /region_name="ACTL7A_N"
                     /note="Actin-like protein 7A N-terminus; pfam16840"
                     /db_xref="CDD:465280"
     Region          36..56
                     /region_name="Required for interaction with TES.
                     /evidence=ECO:0000250|UniProtKB:Q9Y615"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W9.1)"
     Region          72..439
                     /region_name="ASKHA_NBD_ACTL7"
                     /note="nucleotide-binding domain (NBD) of the actin-like
                     protein 7 (ACTL7)-like family; cd10214"
                     /db_xref="CDD:466819"
     CDS             1..440
                     /gene="Actl7a"
                     /gene_synonym="Arp7a; T-actin 2; Tact2"
                     /coded_by="NM_001011973.2:48..1370"
                     /db_xref="GeneID:298017"
                     /db_xref="RGD:1304697"
ORIGIN      
        1 msldavwapq tanigdgpak kasdqtsmqt qvlqtaslrd gpakravwvr rdnaekeepv
       61 ksavskdrpr levtkavvvd lgtgfckcgf aglpkpthki sttvgkpyme taktgdnrke
      121 tfvgrelfnp dihlklvnpl rhgiivdwdt vqdiweylfr qemkiapeeh avlvsdppls
      181 phtnrekyae mlfetfntpa mhiayqsrls mysygrtsgl vvevghgvsy vvpiyegypl
      241 psitgrldya gsdltnylmn lmnncgkhfs edhlsivedi ktkccfvald pieekkipps
      301 eheihytlpd gkeirlgqer flcsemffkp sliksmqlgl htqtvsclnk cdialkrdlm
      361 gnillcggst mlrgfpnrlq kelssmcpnd tpqvnvlper dtavwtggsi laslqgfqpl
      421 wvhrleyeeh gpfflyrrcf
//
LOCUS       NP_001013053             299 aa            linear   ROD 25-MAR-2025
DEFINITION  prohibitin-2 [Rattus norvegicus].
ACCESSION   NP_001013053 XP_342756
VERSION     NP_001013053.1
DBSOURCE    REFSEQ: accession NM_001013035.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,S., Zhang,R., Zhang,L., Yang,A., Guo,Y., Jiang,L., Wang,H.,
            Xu,S. and Zhou,H.
  TITLE     Oxidative stress suppresses PHB2-mediated mitophagy in beta-cells
            via the Nrf2/PHB2 pathway
  JOURNAL   J Diabetes Investig 15 (5), 559-571 (2024)
   PUBMED   38260951
  REMARK    GeneRIF: Oxidative stress suppresses PHB2-mediated mitophagy in
            beta-cells via the Nrf2/PHB2 pathway.
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Zheng,X., Liu,K., Xie,Q., Xin,H., Chen,W., Lin,S., Feng,D. and
            Zhu,T.
  TITLE     PHB2 Alleviates Neurotoxicity of Prion Peptide PrP106-126 via
            PINK1/Parkin-Dependent Mitophagy
  JOURNAL   Int J Mol Sci 24 (21), 15919 (2023)
   PUBMED   37958902
  REMARK    GeneRIF: PHB2 Alleviates Neurotoxicity of Prion Peptide
            PrP[106-126] via PINK1/Parkin-Dependent Mitophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Vila,E., Pinacho,R., Prades,R., Tarrago,T., Castro,E.,
            Munarriz-Cuezva,E., Meana,J.J., Eugui-Anta,A., Roldan,M.,
            Vera-Montecinos,A. and Ramos,B.
  TITLE     Inhibition of Prolyl Oligopeptidase Restores Prohibitin 2 Levels in
            Psychosis Models: Relationship to Cognitive Deficits in
            Schizophrenia
  JOURNAL   Int J Mol Sci 24 (7), 6016 (2023)
   PUBMED   37046989
  REMARK    GeneRIF: Inhibition of Prolyl Oligopeptidase Restores Prohibitin 2
            Levels in Psychosis Models: Relationship to Cognitive Deficits in
            Schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Jia,Y., Wang,M., Mao,C., Yu,F., Wang,Y., Xiao,R., Jiang,C.,
            Zheng,L., Xu,Q., Zheng,M., Fu,Y., Hu,Q. and Kong,W.
  TITLE     COMP-prohibitin 2 interaction maintains mitochondrial homeostasis
            and controls smooth muscle cell identity
  JOURNAL   Cell Death Dis 9 (6), 676 (2018)
   PUBMED   29867124
  REMARK    GeneRIF: COMP-prohibitin 2 interaction in mitochondria plays an
            important role in maintaining the contractile phenotype of Vascular
            smooth muscle cells by regulating mitochondrial oxidative
            phosphorylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Zhou,T.B., Ou,C., Rong,L. and Drummen,G.P.
  TITLE     Effect of all-trans retinoic acid treatment on prohibitin and
            renin-angiotensin-aldosterone system expression in hypoxia-induced
            renal tubular epithelial cell injury
  JOURNAL   J Renin Angiotensin Aldosterone Syst 15 (3), 243-249 (2014)
   PUBMED   25031298
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Kurtev,V., Margueron,R., Kroboth,K., Ogris,E., Cavailles,V. and
            Seiser,C.
  TITLE     Transcriptional regulation by the repressor of estrogen receptor
            activity via recruitment of histone deacetylases
  JOURNAL   J Biol Chem 279 (23), 24834-24843 (2004)
   PUBMED   15140878
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Coates,P.J., Nenutil,R., McGregor,A., Picksley,S.M., Crouch,D.H.,
            Hall,P.A. and Wright,E.G.
  TITLE     Mammalian prohibitin proteins respond to mitochondrial stress and
            decrease during cellular senescence
  JOURNAL   Exp Cell Res 265 (2), 262-273 (2001)
   PUBMED   11302691
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Adams,L.D., Lemire,J.M. and Schwartz,S.M.
  TITLE     A systematic analysis of 40 random genes in cultured vascular
            smooth muscle subtypes reveals a heterogeneity of gene expression
            and identifies the tight junction gene zonula occludens 2 as a
            marker of epithelioid 'pup' smooth muscle cells and a participant
            in carotid neointimal formation
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (11), 2600-2608 (1999)
   PUBMED   10559001
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Montano,M.M., Ekena,K., Delage-Mourroux,R., Chang,W., Martini,P.
            and Katzenellenbogen,B.S.
  TITLE     An estrogen receptor-selective coregulator that potentiates the
            effectiveness of antiestrogens and represses the activity of
            estrogens
  JOURNAL   Proc Natl Acad Sci U S A 96 (12), 6947-6952 (1999)
   PUBMED   10359819
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083705.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342756.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083705.1, CF110063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..299
                     /product="prohibitin-2"
                     /note="B-cell receptor associated protein 37; B-cell
                     receptor-associated protein BAP37"
                     /calculated_mol_wt=33181
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q99623; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Region          19..49
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250|UniProtKB:Q99623"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Region          40..235
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99623; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            147
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35129; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Region          150..174
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250|UniProtKB:Q99623"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35129; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            236
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35129; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            250
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99623; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     Site            262
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35129; propagated from
                     UniProtKB/Swiss-Prot (Q5XIH7.1)"
     CDS             1..299
                     /gene="Phb2"
                     /gene_synonym="Bap; Bap-37; Bap37; Bcap27; Bcap37"
                     /coded_by="NM_001013035.1:127..1026"
                     /db_xref="GeneID:114766"
                     /db_xref="RGD:620203"
ORIGIN      
        1 maqnlkdlag rlpsgprgmg talklllgag avaygvresv ftvegghrai ffnriggvqq
       61 dtilaeglhf ripwfqypii ydirarprki ssptgskdlq mvnislrvls rpnaqelpsm
      121 yqrlgldyee rvlpsivnev lksvvakfna sqlitqraqv sllirrelte rakdfslild
      181 dvaitelsfs reytaaveak qvaqqeaqra qflvekakqe qrqkivqaeg eaeaakmlge
      241 alsknpgyik lrkiraaqni sktiatsqnr iyltadnlvl nlqdesftrg sdslikgkk
//
LOCUS       NP_062191                369 aa            linear   ROD 25-MAR-2025
DEFINITION  transcription factor Maf isoform 2 [Rattus norvegicus].
ACCESSION   NP_062191 XP_001078144
VERSION     NP_062191.2
DBSOURCE    REFSEQ: accession NM_019318.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kim,M., Wende,H., Walcher,J., Kuhnemund,J., Cheret,C., Kempa,S.,
            McShane,E., Selbach,M., Lewin,G.R. and Birchmeier,C.
  TITLE     Maf links Neuregulin1 signaling to cholesterol synthesis in
            myelinating Schwann cells
  JOURNAL   Genes Dev 32 (9-10), 645-657 (2018)
   PUBMED   29748249
  REMARK    GeneRIF: a crucial role of the transcription factor Maf in
            myelination and cholesterol biosynthesis and show that Maf acts
            downstream from Neuregulin1
            Erratum:[Genes Dev. 2018 Aug 1;32(15-16):1101. doi:
            10.1101/gad.318477.118. PMID: 30068704]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Narumi,Y., Nishina,S., Tokimitsu,M., Aoki,Y., Kosaki,R., Wakui,K.,
            Azuma,N., Murata,T., Takada,F., Fukushima,Y. and Kosho,T.
  TITLE     Identification of a novel missense mutation of MAF in a Japanese
            family with congenital cataract by whole exome sequencing: a
            clinical report and review of literature
  JOURNAL   Am J Med Genet A 164A (5), 1272-1276 (2014)
   PUBMED   24664492
  REMARK    Review article
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Aguayo-Mazzucato,C., Zavacki,A.M., Marinelarena,A.,
            Hollister-Lock,J., El Khattabi,I., Marsili,A., Weir,G.C.,
            Sharma,A., Larsen,P.R. and Bonner-Weir,S.
  TITLE     Thyroid hormone promotes postnatal rat pancreatic beta-cell
            development and glucose-responsive insulin secretion through MAFA
  JOURNAL   Diabetes 62 (5), 1569-1580 (2013)
   PUBMED   23305647
  REMARK    GeneRIF: Data suggest that triiodothyronine (T3) acts as
            physiological regulator of functional maturation of islet
            beta-cells via induction of MAFA/c-Maf; T3 has a direct
            receptor-ligand interaction with MAFA/c-Maf promoter.
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Lu,C.C., Appler,J.M., Houseman,E.A. and Goodrich,L.V.
  TITLE     Developmental profiling of spiral ganglion neurons reveals insights
            into auditory circuit assembly
  JOURNAL   J Neurosci 31 (30), 10903-10918 (2011)
   PUBMED   21795542
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Motomura,Y., Kitamura,H., Hijikata,A., Matsunaga,Y., Matsumoto,K.,
            Inoue,H., Atarashi,K., Hori,S., Watarai,H., Zhu,J., Taniguchi,M.
            and Kubo,M.
  TITLE     The transcription factor E4BP4 regulates the production of IL-10
            and IL-13 in CD4+ T cells
  JOURNAL   Nat Immunol 12 (5), 450-459 (2011)
   PUBMED   21460847
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Ring,B.Z., Cordes,S.P., Overbeek,P.A. and Barsh,G.S.
  TITLE     Regulation of mouse lens fiber cell development and differentiation
            by the Maf gene
  JOURNAL   Development 127 (2), 307-317 (2000)
   PUBMED   10603348
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Kawauchi,S., Takahashi,S., Nakajima,O., Ogino,H., Morita,M.,
            Nishizawa,M., Yasuda,K. and Yamamoto,M.
  TITLE     Regulation of lens fiber cell differentiation by transcription
            factor c-Maf
  JOURNAL   J Biol Chem 274 (27), 19254-19260 (1999)
   PUBMED   10383433
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Kim,J.I., Ho,I.C., Grusby,M.J. and Glimcher,L.H.
  TITLE     The transcription factor c-Maf controls the production of
            interleukin-4 but not other Th2 cytokines
  JOURNAL   Immunity 10 (6), 745-751 (1999)
   PUBMED   10403649
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Matsushima-Hibiya,Y., Nishi,S. and Sakai,M.
  TITLE     Rat maf-related factors: the specificities of DNA binding and
            heterodimer formation
  JOURNAL   Biochem Biophys Res Commun 245 (2), 412-418 (1998)
   PUBMED   9571165
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Sakai,M., Imaki,J., Yoshida,K., Ogata,A., Matsushima-Hibaya,Y.,
            Kuboki,Y., Nishizawa,M. and Nishi,S.
  TITLE     Rat maf related genes: specific expression in chondrocytes, lens
            and spinal cord
  JOURNAL   Oncogene 14 (6), 745-750 (1997)
   PUBMED   9038383
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Nov 26, 2020 this sequence version replaced NP_062191.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: U56242.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..369
                     /product="transcription factor Maf isoform 2"
                     /note="transcription factor Maf; C-Maf; proto-oncogene
                     c-maf; transcription factor Maf-2; v-maf avian
                     musculoaponeurotic fibrosarcoma oncogene homolog; bZip
                     transcription factor c-maf"
                     /calculated_mol_wt=38266
     Region          57..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          86..119
                     /region_name="Maf_N"
                     /note="Maf N-terminal region; pfam08383"
                     /db_xref="CDD:462456"
     Region          126..369
                     /region_name="Represses ARE-mediated transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          175..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          279..347
                     /region_name="bZIP_Maf_large"
                     /note="Basic leucine zipper (bZIP) domain of large
                     musculoaponeurotic fibrosarcoma (Maf) proteins: a
                     DNA-binding and dimerization domain; cd14718"
                     /db_xref="CDD:269866"
     Region          279..347
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269866"
     Region          284..309
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Site            order(286,289..291,293..295,297..299,301..302,304..305)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269866"
     Site            order(305,312,315..316,319..320,322..323,326..327,
                     329..330,333,336..337,340..341,343..344)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269866"
     Region          312..333
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     CDS             1..369
                     /gene="Maf"
                     /gene_synonym="cMaf; Maf2"
                     /coded_by="NM_019318.2:178..1287"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:54267"
                     /db_xref="RGD:3034"
ORIGIN      
        1 maselamnns dlptsplame yvndfdlmkf evkkepvetd riisqcgrli aggslsstpm
       61 stpcssvpps psfsapspgs gseqkahled yywmtgypqq lnpealgfsp edavealisn
      121 shqlqggfdg yargaqqlaa aagagagasl ggsgeemgpa aavvsaviaa aaaqsggaph
      181 yhhhhhhatg hhhhptagap gaagsasasa sgaggagggg pasagggggg ggggtagagg
      241 alhphhaagg lhfddrfsde qlvtmsvrel nrqlrgvske evirlkqkrr tlknrgyaqs
      301 crfkrvqqrh vleseknqll qqvdhlkqei srlvrerday kekyeklvss gfrengsssd
      361 npsspeffm
//
LOCUS       NP_872611                193 aa            linear   ROD 25-MAR-2025
DEFINITION  ras homolog gene family, member A [Rattus norvegicus].
ACCESSION   NP_872611
VERSION     NP_872611.2
DBSOURCE    REFSEQ: accession NM_182670.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Zhang,N., Liang,J., Tian,Y., Yuan,L., Wu,L., Miao,S., Zong,S. and
            Wang,L.
  TITLE     A novel testis-specific GTPase serves as a link to proteasome
            biogenesis: functional characterization of RhoS/RSA-14-44 in
            spermatogenesis
  JOURNAL   Mol Biol Cell 21 (24), 4312-4324 (2010)
   PUBMED   20980621
  REMARK    GeneRIF: RSA-14-44 associates with PSMB5, a catalytic subunit of
            the proteasome, in a series of stage-specific spermatogenic cells.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK603687.1 and BC083656.1.
            
            On Nov 23, 2005 this sequence version replaced NP_872611.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC083656.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q31"
     Protein         1..193
                     /product="ras homolog gene family, member A"
                     /calculated_mol_wt=21504
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     CDS             1..193
                     /gene="Rhoal1"
                     /gene_synonym="RSA-14-44"
                     /coded_by="NM_182670.2:146..727"
                     /db_xref="GeneID:297173"
                     /db_xref="RGD:735071"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pdvyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvl licfsignpd sfgniphkwi pevkhfcpnv piilvgskkd
      121 lrndlntiqe lakrkqepvk peqgrdlans igafeyvecs aktkdgvrkv fekatraalq
      181 tnrvkkktgc fvf
//
LOCUS       NP_058705                430 aa            linear   ROD 25-MAR-2025
DEFINITION  glial fibrillary acidic protein [Rattus norvegicus].
ACCESSION   NP_058705 XP_346411
VERSION     NP_058705.2
DBSOURCE    REFSEQ: accession NM_017009.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Dandi,Epsilon., Theotokis,P., Petri,M.C., Sideropoulou,V.,
            Spandou,E. and Tata,D.A.
  TITLE     Environmental enrichment initiated in adolescence restores the
            reduced expression of synaptophysin and GFAP in the hippocampus of
            chronically stressed rats in a sex-specific manner
  JOURNAL   Dev Psychobiol 65 (7), e22422 (2023)
   PUBMED   37796476
  REMARK    GeneRIF: Environmental enrichment initiated in adolescence restores
            the reduced expression of synaptophysin and GFAP in the hippocampus
            of chronically stressed rats in a sex-specific manner.
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Gok,E. and Deveci,E.
  TITLE     Histopathological evaluation of IBA-1, GFAP activity in the brain
            cortex of rats administered cadmium chloride
  JOURNAL   Arch Ital Biol 160 (1-2), 20-27 (2022)
   PUBMED   35913387
  REMARK    GeneRIF: Histopathological evaluation of IBA-1, GFAP activity in
            the brain cortex of rats administered cadmium chloride.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Aamodt,A.H., Hogestol,E.A., Popperud,T.H., Holter,J.C.,
            Dyrhol-Riise,A.M., Tonby,K., Stiksrud,B., Quist-Paulsen,E.,
            Berge,T., Barratt-Due,A., Aukrust,P., Heggelund,L., Blennow,K.,
            Zetterberg,H. and Harbo,H.F.
  TITLE     Blood neurofilament light concentration at admittance: a potential
            prognostic marker in COVID-19
  JOURNAL   J Neurol 268 (10), 3574-3583 (2021)
   PUBMED   33743046
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Othman,H., Lopez-Furelos,A., Leiro-Vidal,J.M., Ammari,M., Sakly,M.,
            Abdelmelek,H., Salas-Sanchez,A.A., Ares-Pena,F. and Lopez-Martin,E.
  TITLE     Exposure to 2.45 GHz Radiation Triggers Changes in HSP-70,
            Glucocorticoid Receptors and GFAP Biomarkers in Rat Brain
  JOURNAL   Int J Mol Sci 22 (10), 5103 (2021)
   PUBMED   34065959
  REMARK    GeneRIF: Exposure to 2.45 GHz Radiation Triggers Changes in HSP-70,
            Glucocorticoid Receptors and GFAP Biomarkers in Rat Brain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Tsyba,D.L., Kirik,O.V., Kolpakova,M.E., Yakovleva,A.A. and
            Korzhevskii,D.E.
  TITLE     Expression of Nestin and Glial Fibrillary Acidic Protein in the
            Marginal Ischemic Zone of the Brain in SHR Rats
  JOURNAL   Bull Exp Biol Med 169 (4), 576-581 (2020)
   PUBMED   32910393
  REMARK    GeneRIF: Expression of Nestin and Glial Fibrillary Acidic Protein
            in the Marginal Ischemic Zone of the Brain in SHR Rats.
REFERENCE   6  (residues 1 to 430)
  AUTHORS   McCall,M.A., Gregg,R.G., Behringer,R.R., Brenner,M., Delaney,C.L.,
            Galbreath,E.J., Zhang,C.L., Pearce,R.A., Chiu,S.Y. and Messing,A.
  TITLE     Targeted deletion in astrocyte intermediate filament (Gfap) alters
            neuronal physiology
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6361-6366 (1996)
   PUBMED   8692820
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Molthagen,M., Schachner,M. and Bartsch,U.
  TITLE     Apoptotic cell death of photoreceptor cells in mice deficient for
            the adhesion molecule on glia (AMOG, the beta 2- subunit of the Na,
            K-ATPase)
  JOURNAL   J Neurocytol 25 (4), 243-255 (1996)
   PUBMED   8793730
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Condorelli,D.F., Nicoletti,V.G., Barresi,V., Caruso,A.,
            Conticello,S., de Vellis,J. and Giuffrida Stella,A.M.
  TITLE     Tissue-specific DNA methylation patterns of the rat glial
            fibrillary acidic protein gene
  JOURNAL   J Neurosci Res 39 (6), 694-707 (1994)
   PUBMED   7897704
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Feinstein,D.L., Weinmaster,G.A. and Milner,R.J.
  TITLE     Isolation of cDNA clones encoding rat glial fibrillary acidic
            protein: expression in astrocytes and in Schwann cells
  JOURNAL   J Neurosci Res 32 (1), 1-14 (1992)
   PUBMED   1629938
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Nichols,N.R., Osterburg,H.H., Masters,J.N., Millar,S.L. and
            Finch,C.E.
  TITLE     Messenger RNA for glial fibrillary acidic protein is decreased in
            rat brain following acute and chronic corticosterone treatment
  JOURNAL   Brain Res Mol Brain Res 7 (1), 1-7 (1990)
   PUBMED   2153890
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088851.1.
            
            On Oct 12, 2007 this sequence version replaced NP_058705.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088851.1, U03700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..430
                     /product="glial fibrillary acidic protein"
                     /note="intermediate filament; glial fibrillary acidic
                     protein alpha; glial fibrillary acidic protein delta"
                     /calculated_mol_wt=49826
     Region          1..70
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          4..64
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB and ROCK1.
                     /evidence=ECO:0000250|UniProtKB:P14136; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            11
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P03995; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            21
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P03995; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK1.
                     /evidence=ECO:0000250|UniProtKB:P14136; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P03995; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Region          66..374
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          71..102
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Region          103..113
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          114..212
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Region          213..228
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          229..250
                     /region_name="Coil 2A"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          251..254
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Region          255..375
                     /region_name="Coil 2B"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     Region          376..430
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (P47819.2)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47819.2)"
     CDS             1..430
                     /gene="Gfap"
                     /coded_by="NM_017009.2:2..1294"
                     /db_xref="GeneID:24387"
                     /db_xref="RGD:2679"
ORIGIN      
        1 merrritsar rsyassetmv rghgptrhlg tiprlslsrm tpplparvdf slagalnagf
       61 ketraserae mmelndrfas yiekvrfleq qnkalaaeln qlrakeptkl advyqaelre
      121 lrlrldqltt nsarleverd nltqdlgtlr qklqdetnlr leaennlavy rqeadeatla
      181 rvdlerkves leeeiqflrk iheeevrelq eqlaqqqvhv emdvakpdlt aalreirtqy
      241 eavatsnmqe teewyrskfa dltdvasrna ellrqakhea ndyrrqlqal tcdleslrgt
      301 neslerqmre qeerharesa syqealarle eegqslkeem arhlqeyqdl lnvklaldie
      361 iatyrklleg eenritipvq tfsnlqiret sldtksvseg hlkrnivvkt vemrdgevik
      421 eskqehkdvm
//
LOCUS       NP_001257725             752 aa            linear   ROD 25-MAR-2025
DEFINITION  85/88 kDa calcium-independent phospholipase A2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257725
VERSION     NP_001257725.1
DBSOURCE    REFSEQ: accession NM_001270796.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Kuwata,H., Yuzurihara,C., Kinoshita,N., Taki,Y., Ikegami,Y.,
            Washio,S., Hirakawa,Y., Yoda,E., Aiuchi,T., Itabe,H., Nakatani,Y.
            and Hara,S.
  TITLE     The group VIA calcium-independent phospholipase A2 and NFATc4
            pathway mediates IL-1beta-induced expression of chemokines CCL2 and
            CXCL10 in rat fibroblasts
  JOURNAL   FEBS J 285 (11), 2056-2070 (2018)
   PUBMED   29637744
  REMARK    GeneRIF: the transcriptional activation of nuclear factor of
            activated T-cell proteins (NFATs), but not nuclear factor-kappaB,
            by IL-1beta stimulation was markedly attenuated by the iPLA2
            inhibitor bromoenol lactone, and NFATc4 knockdown markedly
            attenuated the IL-1beta-induced expression of both CCL2 and CXCL10.
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Zhou,Z., Wang,Z., Guan,Q., Qiu,F., Li,Y., Liu,Z., Zhang,H., Dong,H.
            and Zhang,Z.
  TITLE     PEDF Inhibits the Activation of NLRP3 Inflammasome in Hypoxia
            Cardiomyocytes through PEDF Receptor/Phospholipase A2
  JOURNAL   Int J Mol Sci 17 (12), 2064 (2016)
   PUBMED   27973457
  REMARK    GeneRIF: PEDF can protect against hypoxia-induced activation of the
            NLRP3 inflammasome by inhibiting mitochondrial fission though
            PEDFR/iPLA2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Caporarello,N., Salmeri,M., Scalia,M., Motta,C., Parrino,C.,
            Frittitta,L., Olivieri,M., Toscano,M.A., Anfuso,C.D. and Lupo,G.
  TITLE     Role of cytosolic and calcium independent phospholipases A(2) in
            insulin secretion impairment of INS-1E cells infected by S. aureus
  JOURNAL   FEBS Lett 589 (24 Pt B), 3969-3976 (2015)
   PUBMED   26632509
  REMARK    GeneRIF: Data suggest glucose-induced insulin secretion is first
            up-regulated (acute infection), then down-regulated (chronic
            infection) in beta cells infected with S. aureus; Pla2g4a is
            up-regulated in acute infection; Pla2g6 is up-regulated in chronic
            infection.
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Rauckhorst,A.J., Pfeiffer,D.R. and Broekemeier,K.M.
  TITLE     The iPLA(2)gamma is identified as the membrane potential sensitive
            phospholipase in liver mitochondria
  JOURNAL   FEBS Lett 589 (18), 2367-2371 (2015)
   PUBMED   26206229
  REMARK    GeneRIF: membrane potential sensitive activity is the iPLA2gamma
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Takatani-Nakase,T. and Takahashi,K.
  TITLE     Leptin suppresses non-apoptotic cell death in ischemic rat
            cardiomyocytes by reduction of iPLA(2) activity
  JOURNAL   Biochem Biophys Res Commun 463 (1-2), 13-17 (2015)
   PUBMED   25979360
  REMARK    GeneRIF: Leptin was shown to significantly inhibit the activity of
            iPLA2, which is considered to play crucial roles in non-apoptotic
            cell death, resulting in effective prevention of ischemia-induced
            myocyte death.
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Jenkins,C.M., Han,X., Mancuso,D.J. and Gross,R.W.
  TITLE     Identification of calcium-independent phospholipase A2 (iPLA2)
            beta, and not iPLA2gamma, as the mediator of arginine
            vasopressin-induced arachidonic acid release in A-10 smooth muscle
            cells. Enantioselective mechanism-based discrimination of mammalian
            iPLA2s
  JOURNAL   J Biol Chem 277 (36), 32807-32814 (2002)
   PUBMED   12089145
  REMARK    GeneRIF: The agonist-stimulated release of arachidonic acid (AA)
            from cellular phospholipids in many cell types (e.g. myocytes,
            beta-cells, and neurons) has been demonstrated to be primarily
            mediated by calcium-independent phospholipases A(2) (iPLA(2)s).
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Seegers,H.C., Gross,R.W. and Boyle,W.A.
  TITLE     Calcium-independent phospholipase A(2)-derived arachidonic acid is
            essential for endothelium-dependent relaxation by acetylcholine
  JOURNAL   J Pharmacol Exp Ther 302 (3), 918-923 (2002)
   PUBMED   12183647
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Bloch-Shilderman,E., Abu-Raya,S., Trembovler,V., Boschwitz,H.,
            Gruzman,A., Linial,M. and Lazarovici,P.
  TITLE     Pardaxin stimulation of phospholipases A2 and their involvement in
            exocytosis in PC-12 cells
  JOURNAL   J Pharmacol Exp Ther 301 (3), 953-962 (2002)
   PUBMED   12023524
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Ma,Z., Ramanadham,S., Wohltmann,M., Bohrer,A., Hsu,F.F. and Turk,J.
  TITLE     Studies of insulin secretory responses and of arachidonic acid
            incorporation into phospholipids of stably transfected insulinoma
            cells that overexpress group VIA phospholipase A2 (iPLA2beta)
            indicate a signaling rather than a housekeeping role for iPLA2beta
  JOURNAL   J Biol Chem 276 (16), 13198-13208 (2001)
   PUBMED   11278673
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Ma,Z., Ramanadham,S., Kempe,K., Chi,X.S., Ladenson,J. and Turk,J.
  TITLE     Pancreatic islets express a Ca2+-independent phospholipase A2
            enzyme that contains a repeated structural motif homologous to the
            integral membrane protein binding domain of ankyrin
  JOURNAL   J Biol Chem 272 (17), 11118-11127 (1997)
   PUBMED   9111008
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC081916.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate in-frame exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061866.1, SRR26643429.28019.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..752
                     /product="85/88 kDa calcium-independent phospholipase A2
                     isoform 2"
                     /EC_number="3.1.1.5"
                     /EC_number="3.1.1.4"
                     /EC_number="3.1.2.2"
                     /note="85 kDa calcium-independent phospholipase A2;
                     patatin-like phospholipase domain-containing protein 9;
                     intracellular membrane-associated calcium-independent
                     phospholipase A2 beta; 85/88 kDa calcium-independent
                     phospholipase A2; phospholipase A2, group VI (cytosolic,
                     calcium-independent); palmitoyl-CoA hydrolase;
                     2-lysophosphatidylcholine acylhydrolase"
                     /calculated_mol_wt=83431
     Region          102..392
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          119..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(151,153,157..158,161..163,165..166,170,173,183,185,
                     187,191..192,195..197,199..200,204,207,217,219,221,
                     225..226,229..231,233..234,238,241)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          151..183
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          185..217
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          219..248
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(286,288,292..293,295,297..298,302,305,314,316,318,
                     322..323,326..328,330..331,335,338,347,349,351,355..356,
                     359..361,363..364,368,371,380)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          286..314
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          316..347
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          349..380
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          426..739
                     /region_name="Pat_PNPLA9"
                     /note="Patatin-like phospholipase domain containing
                     protein 9; cd07212"
                     /db_xref="CDD:132851"
     Site            order(432..433,435,465,598)
                     /site_type="active"
                     /db_xref="CDD:132851"
     Site            463..467
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132851"
     CDS             1..752
                     /gene="Pla2g6"
                     /gene_synonym="caI-PLA2; GVI PLA2; iPla2; iPLA2-beta;
                     PNPLA9"
                     /coded_by="NM_001270796.1:173..2431"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360426"
                     /db_xref="RGD:628867"
ORIGIN      
        1 mqffgrlvnt lssvtnlfsn pfrvkevsla dyasservre egqlillqna snrtwdcvlv
       61 sprnpqsgfr lfqleseada lvnfqqyssq lppfyessvq vlhvevlqhl tdlirnhpsw
      121 tvthlavelg irecfhhsri iscanstene egctplhlac rkgdseilve lvqychaqmd
      181 vtdnkgetaf hyavqgdnpq vlqllgknas aglnqvnnqg ltplhlacqm gkqemvrvll
      241 lcnarcnimg pggfpihtam kfsqkgcaem iismdsnqih skdprygasp lhwaknaema
      301 rmllkrgcdv dstsasgnta lhvavtrnrf dcvmvlltyg anagargehg ntplhlamsk
      361 dnmemvkali vfgaevdtpn dfgetpafia skiskqlqdl mpvsrarkpa filssmrdek
      421 rshdhllcld gggvkglvii qlliaiekas gvatkdlfdw vagtstggil alailhsksm
      481 aymrgvyfrm kdevfrgsrp yesgpleefl krefgehtkm tdvkkpkvml tgtlsdrqpa
      541 elhlfrnyda peavreprct pninlkpptq padqlvwraa rssgaaptyf rpngrfldgg
      601 llannptlda mteiheynqd mirkgqgnkv kklsivvslg tgkspqvpvt cvdvfrpsnp
      661 welaktvfga kelgkmvvdc ctdpdgravd rarawcemvg iqyfrlnpql gsdimldevs
      721 davlvnalwe tevyiyehre efqklvqlll sp
//
LOCUS       NP_058874                394 aa            linear   ROD 25-MAR-2025
DEFINITION  bone morphogenetic protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_058874
VERSION     NP_058874.2
DBSOURCE    REFSEQ: accession NM_017178.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Zheng,Z., Wang,D., Zhang,W., Yu,H., Zhang,Y., Feng,T. and Zhong,X.
  TITLE     MiR-20 promotes cartilage repair in knee osteoarthritis rats via
            BMP2/Smad1 signaling pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 256-261 (2023)
   PUBMED   38063098
  REMARK    GeneRIF: MiR-20 promotes cartilage repair in knee osteoarthritis
            rats via BMP2/Smad1 signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Deng,J., Zhao,H.J., Zhong,Y., Hu,C., Meng,J., Wang,C., Lan,X.,
            Wang,X., Chen,Z.J., Yan,J., Wang,W. and Li,Y.
  TITLE     H3K27me3-modulated Hofbauer cell BMP2 signalling enhancement
            compensates for shallow trophoblast invasion in preeclampsia
  JOURNAL   EBioMedicine 93, 104664 (2023)
   PUBMED   37331163
  REMARK    GeneRIF: H3K27me3-modulated Hofbauer cell BMP2 signalling
            enhancement compensates for shallow trophoblast invasion in
            preeclampsia.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Wang,M., Qiu,Y., Gao,L., Qi,F. and Bi,L.
  TITLE     The impact of IGF-1 on alveolar bone remodeling and BMP-2
            expression in orthodontic tooth movement in diabetic rats
  JOURNAL   Adv Clin Exp Med 32 (3), 349-356 (2023)
   PUBMED   36421043
  REMARK    GeneRIF: The impact of IGF-1 on alveolar bone remodeling and BMP-2
            expression in orthodontic tooth movement in diabetic rats.
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Manzano-Lista,F.J., Sanz-Gomez,M., Gonzalez-Moreno,D.,
            Vega-Martin,E., Gil-Ortega,M., Schulz,A., Rubio,M.A.,
            Ruiz-Hurtado,G., Ruilope,L.M., Aranguez,I., Kreutz,R. and
            Fernandez-Alfonso,M.S.
  TITLE     Imbalance in Bone Morphogenic Proteins 2 and 7 Is Associated with
            Renal and Cardiovascular Damage in Chronic Kidney Disease
  JOURNAL   Int J Mol Sci 24 (1), 40 (2022)
   PUBMED   36613483
  REMARK    GeneRIF: Imbalance in Bone Morphogenic Proteins 2 and 7 Is
            Associated with Renal and Cardiovascular Damage in Chronic Kidney
            Disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Howard,M.T., Wang,S., Berger,A.G., Martin,J.R.,
            Jalili-Firoozinezhad,S., Padera,R.F. and Hammond,P.T.
  TITLE     Sustained release of BMP-2 using self-assembled layer-by-layer
            film-coated implants enhances bone regeneration over burst release
  JOURNAL   Biomaterials 288, 121721 (2022)
   PUBMED   35981926
  REMARK    GeneRIF: Sustained release of BMP-2 using self-assembled
            layer-by-layer film-coated implants enhances bone regeneration over
            burst release.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Yamaji,N., Celeste,A.J., Thies,R.S., Song,J.J., Bernier,S.M.,
            Goltzman,D., Lyons,K.M., Nove,J., Rosen,V. and Wozney,J.M.
  TITLE     A mammalian serine/threonine kinase receptor specifically binds
            BMP-2 and BMP-4
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1944-1951 (1994)
   PUBMED   7811286
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Begue-Kirn,C., Smith,A.J., Loriot,M., Kupferle,C., Ruch,J.V. and
            Lesot,H.
  TITLE     Comparative analysis of TGF beta s, BMPs, IGF1, msxs, fibronectin,
            osteonectin and bone sialoprotein gene expression during normal and
            in vitro-induced odontoblast differentiation
  JOURNAL   Int J Dev Biol 38 (3), 405-420 (1994)
   PUBMED   7848824
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Ohta,S., Hiraki,Y., Shigeno,C., Suzuki,F., Kasai,R., Ikeda,T.,
            Kohno,H., Lee,K., Kikuchi,H., Konishi,J. et al.
  TITLE     Bone morphogenetic proteins (BMP-2 and BMP-3) induce the late phase
            expression of the proto-oncogene c-fos in murine osteoblastic
            MC3T3-E1 cells
  JOURNAL   FEBS Lett 314 (3), 356-360 (1992)
   PUBMED   1468569
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Kaplan,F.S., Tabas,J.A. and Zasloff,M.A.
  TITLE     Fibrodysplasia ossificans progressiva: a clue from the fly?
  JOURNAL   Calcif Tissue Int 47 (2), 117-125 (1990)
   PUBMED   2117991
  REMARK    Review article
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Wozney,J.M., Rosen,V., Celeste,A.J., Mitsock,L.M., Whitters,M.J.,
            Kriz,R.W., Hewick,R.M. and Wang,E.A.
  TITLE     Novel regulators of bone formation: molecular clones and activities
  JOURNAL   Science 242 (4885), 1528-1534 (1988)
   PUBMED   3201241
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Dec 5, 2020 this sequence version replaced NP_058874.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z25868.1, L20678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..394
                     /product="bone morphogenetic protein 2 precursor"
                     /note="BMP-2; BMP-2A; bone morphogenetic protein 2A"
                     /calculated_mol_wt=42472
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
                     /calculated_mol_wt=2010
     Region          51..265
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; pfam00688"
                     /db_xref="CDD:459906"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12644; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
     Region          269..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49001.1)"
     mat_peptide     281..394
                     /product="Bone morphogenetic protein 2.
                     /id=PRO_0000033831"
                     /note="propagated from UniProtKB/Swiss-Prot (P49001.1)"
                     /calculated_mol_wt=12905
     Region          292..394
                     /region_name="TGF_beta_BMP2"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in bone morphogenetic protein 2 (BMP-2) and
                     similar proteins; cd19390"
                     /db_xref="CDD:381660"
     Site            order(294..331,333..351,353..374,376..394)
                     /site_type="other"
                     /note="polypeptide substrate binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:381660"
     Site            order(299,301,305..306,308,318,320..322,339..340,343..344,
                     346..347,350,353..355,358,360..361,364,384..386,388,394)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381660"
     Site            order(305..306,308,311,313..316,365,368..370,376..378,380,
                     382..383,385..386,389)
                     /site_type="other"
                     /note="polypeptide substrate binding site 3 [polypeptide
                     binding]"
                     /db_xref="CDD:381660"
     Site            order(308,311,314..315,320..322,338..340,342..344,346,
                     354..355,358,360..361,368,370,378..386,388,394)
                     /site_type="other"
                     /note="polypeptide substrate binding site 1 [polypeptide
                     binding]"
                     /db_xref="CDD:381660"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49001.1)"
     CDS             1..394
                     /gene="Bmp2"
                     /coded_by="NM_017178.2:252..1436"
                     /db_xref="GeneID:29373"
                     /db_xref="RGD:2211"
ORIGIN      
        1 mvagtrcllv lllpqvllgg aaglipelgr kkfagasgrp lsrpsddvls efelrllsmf
       61 glkqrptpsk dvvvppymld lyrrhsgqpg apapdhrler aasrantvrs fhheeaieel
      121 pemsgktsrr fffnlssvpt defltsaelq ifreqmqeal gnssfqhrin iyeiikpata
      181 sskfpvtrll dtrlvtqnts qwesfdvtpa vmrwtaqght nhgfvvevah leekpgvskr
      241 hvrisrslhq dehswsqvrp llvtfghdgk ghplhkrekr qakhkqrkrl kssckrhply
      301 vdfsdvgwnd wivappgyha fychgecpfp ladhlnstnh aivqtlvnsv nskipkaccv
      361 ptelsaisml yldenekvvl knyqdmvveg cgcr
//
LOCUS       NP_062051                835 aa            linear   ROD 25-MAR-2025
DEFINITION  toll-like receptor 4 precursor [Rattus norvegicus].
ACCESSION   NP_062051
VERSION     NP_062051.2
DBSOURCE    REFSEQ: accession NM_019178.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Tao,X., Hu,Y., Mao,N., Shen,M., Fang,M., Zhang,M., Lou,J., Fang,Y.,
            Guo,X. and Lin,Z.
  TITLE     Echinatin alleviates inflammation and pyroptosis in
            hypoxic-ischemic brain damage by inhibiting TLR4/ NF-kappaB pathway
  JOURNAL   Int Immunopharmacol 136, 112372 (2024)
   PUBMED   38850784
  REMARK    GeneRIF: Echinatin alleviates inflammation and pyroptosis in
            hypoxic-ischemic brain damage by inhibiting TLR4/ NF-kappaB
            pathway.
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Xu,L., Zhang,Y., Yu,J., Huo,W., Xu,J., Yang,H., Zhang,M., Yu,S.,
            Wu,Y. and Wang,M.
  TITLE     miR-708-5p deficiency involves the degeneration of mandibular
            condylar chondrocytes via the TLR4/NF-kappaB pathway
  JOURNAL   Osteoarthritis Cartilage 32 (6), 666-679 (2024)
   PUBMED   38403153
  REMARK    GeneRIF: miR-708-5p deficiency involves the degeneration of
            mandibular condylar chondrocytes via the TLR4/NF-kappaB pathway.
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Cao,W., Zeng,Y., Su,Y., Gong,H., He,J., Liu,Y. and Li,C.
  TITLE     The involvement of oxidative stress and the TLR4/NF-kappaB/NLRP3
            pathway in acute lung injury induced by high-altitude hypoxia
  JOURNAL   Immunobiology 229 (3), 152809 (2024)
   PUBMED   38788361
  REMARK    GeneRIF: The involvement of oxidative stress and the
            TLR4/NF-kappaB/NLRP3 pathway in acute lung injury induced by
            high-altitude hypoxia.
REFERENCE   4  (residues 1 to 835)
  AUTHORS   de Oliveira,A.A., Elder,E., Spaans,F., Graton,M.E., Quon,A.,
            Kirschenman,R., Wooldridge,A.L., Cooke,C.M. and Davidge,S.T.
  TITLE     Excessive hypercholesterolemia in pregnancy impairs rat uterine
            artery function via activation of Toll-like receptor 4
  JOURNAL   Clin Sci (Lond) 138 (4), 137-151 (2024)
   PUBMED   38299431
  REMARK    GeneRIF: Excessive hypercholesterolemia in pregnancy impairs rat
            uterine artery function via activation of Toll-like receptor 4.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Khomula,E.V., Araldi,D., Green,P.G. and Levine,J.D.
  TITLE     Sensitization of human and rat nociceptors by low dose morphine is
            toll-like receptor 4-dependent
  JOURNAL   Mol Pain 20, 17448069241227922 (2024)
   PUBMED   38195088
  REMARK    GeneRIF: Sensitization of human and rat nociceptors by low dose
            morphine is toll-like receptor 4-dependent.
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Ohashi,K., Burkart,V., Flohe,S. and Kolb,H.
  TITLE     Cutting edge: heat shock protein 60 is a putative endogenous ligand
            of the toll-like receptor-4 complex
  JOURNAL   J Immunol 164 (2), 558-561 (2000)
   PUBMED   10623794
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Takeuchi,O., Takeda,K., Hoshino,K., Adachi,O., Ogawa,T. and
            Akira,S.
  TITLE     Cellular responses to bacterial cell wall components are mediated
            through MyD88-dependent signaling cascades
  JOURNAL   Int Immunol 12 (1), 113-117 (2000)
   PUBMED   10607756
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Takeuchi,O., Hoshino,K., Kawai,T., Sanjo,H., Takada,H., Ogawa,T.,
            Takeda,K. and Akira,S.
  TITLE     Differential roles of TLR2 and TLR4 in recognition of gram-negative
            and gram-positive bacterial cell wall components
  JOURNAL   Immunity 11 (4), 443-451 (1999)
   PUBMED   10549626
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Frantz,S., Kobzik,L., Kim,Y.D., Fukazawa,R., Medzhitov,R., Lee,R.T.
            and Kelly,R.A.
  TITLE     Toll4 (TLR4) expression in cardiac myocytes in normal and failing
            myocardium
  JOURNAL   J Clin Invest 104 (3), 271-280 (1999)
   PUBMED   10430608
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Vogel,S.N., Johnson,D., Perera,P.Y., Medvedev,A., Lariviere,L.,
            Qureshi,S.T. and Malo,D.
  TITLE     Cutting edge: functional characterization of the effect of the
            C3H/HeJ defect in mice that lack an Lpsn gene: in vivo evidence for
            a dominant negative mutation
  JOURNAL   J Immunol 162 (10), 5666-5670 (1999)
   PUBMED   10229796
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 27, 2020 this sequence version replaced NP_062051.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            22 bp suspected to be vector contamination from the 5' end.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ175880.1, AF057025.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..835
                     /product="toll-like receptor 4 precursor"
                     /EC_number="3.2.2.6"
                     /note="toll4"
                     /calculated_mol_wt=93377
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
                     /calculated_mol_wt=2699
     Region          23..>456
                     /region_name="PLN00113"
                     /note="leucine-rich repeat receptor-like protein kinase;
                     Provisional"
                     /db_xref="CDD:215061"
     mat_peptide     26..835
                     /product="Toll-like receptor 4. /id=PRO_0000034728"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
                     /calculated_mol_wt=93377
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          54..75
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          58..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          78..99
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          79..102
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          102..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          103..126
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          126..147
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          127..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          151..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          175..198
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          176..204
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          204..224
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          205..226
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          226..247
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          256..310
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          <370..>578
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          372..381
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          373..398
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          398..420
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          399..421
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          421..442
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          422..446
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          446..467
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          447..470
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          470..491
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          471..495
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            492
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          495..516
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          496..519
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          519..540
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          520..543
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          543..564
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          544..567
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            572
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            575
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            622
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX05.1)"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX05.1)"
     Region          672..813
                     /region_name="TIR"
                     /note="Toll - interleukin 1 - resistance; smart00255"
                     /db_xref="CDD:214587"
     CDS             1..835
                     /gene="Tlr4"
                     /coded_by="NM_019178.2:238..2745"
                     /db_xref="GeneID:29260"
                     /db_xref="RGD:3870"
ORIGIN      
        1 mmpllhlagt limalflscl rpgslnpcie vlpnityqcm dqnlskiphd ipystknldl
       61 sfnplkilrs ysfsnfsqlq wldlsrceie tiedkawhgl nqlstlvltg npiksfspgs
      121 fsgltnlenl vavetkmtsl egfhigqlis lkklnvahnl ihsfklpeyf snltnlehvd
      181 lsynyiqtis vkdlqflren pqvnlsldls lnpidsiqaq afqgirlhel tlrsnfnssn
      241 vlkmclqnmt glhvhrlilg efknernles fdrsvmeglc nvsidefrlt yinhfsddiy
      301 nlnclanisa msftgvhikh iadvprhfkw qslsiirchl kpfpklslpf lkswtlttnr
      361 edisfgqlal pslryldlsr namsfrgccs ysdfgtnnlk yldlsfngvi lmsanfmgle
      421 eleyldfqhs tlkkvtefsv flslekllyl disytntkid fdgiflglis lntlkmagns
      481 fkdntlsnvf tnttnltfld lskcqleqis rgvfdtlyrl qllnmshnnl lfldpshykq
      541 lyslrtldcs fnrietskgi lqhfpkslav fnltnnsvac iceyqnflqw vkdqkmflvn
      601 veqmkcaspi dmkaslvldf tnstcyiykt iisvsvvsvl vvatvafliy hfyfhlilia
      661 gckkysrges iydafviyss qnedwvrnel vknleegvpr fqlclhyrdf ipgvaiaani
      721 iqegfhksrk vivvvsrhfi qsrwcifeye iaqtwqflss rsgiifivle kveksllrqq
      781 velyrllsrn tylewednal grhifwrrlk kalldgkaln pdetseeeqe attlt
//
LOCUS       NP_001265412             529 aa            linear   ROD 25-MAR-2025
DEFINITION  runt-related transcription factor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001265412
VERSION     NP_001265412.1
DBSOURCE    REFSEQ: accession NM_001278483.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Gopinathan,G., Luan,X. and Diekwisch,T.G.H.
  TITLE     Epigenetic Repression of RUNX2 and OSX Promoters Controls the
            Nonmineralized State of the Periodontal Ligament
  JOURNAL   Genes (Basel) 14 (1), 201 (2023)
   PUBMED   36672941
  REMARK    GeneRIF: Epigenetic Repression of RUNX2 and OSX Promoters Controls
            the Nonmineralized State of the Periodontal Ligament.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Ma,Z., Wang,Y., Xue,Y., Zhang,W., Li,D., Li,Y., Li,G., Zhou,H.,
            Hu,X., Deng,T. and Hu,K.
  TITLE     Traumatic temporomandibular joint bony ankylosis in growing rats
  JOURNAL   BMC Oral Health 22 (1), 585 (2022)
   PUBMED   36494653
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Xie,S., Chen,M., Fang,W., Liu,S., Wu,Q., Liu,C., Xing,Y., Shi,W.,
            Xu,M., Zhang,M., Chen,S., Zeng,X., Wang,S., Deng,W. and Tang,Q.
  TITLE     Diminished arachidonate 5-lipoxygenase perturbs phase separation
            and transcriptional response of Runx2 to reverse pathological
            ventricular remodeling
  JOURNAL   EBioMedicine 86, 104359 (2022)
   PUBMED   36395739
  REMARK    GeneRIF: Diminished arachidonate 5-lipoxygenase perturbs phase
            separation and transcriptional response of Runx2 to reverse
            pathological ventricular remodeling.
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Zhou,W., Feng,Q., Cheng,M., Zhang,D., Jin,J., Zhang,S., Bai,Y. and
            Xu,J.
  TITLE     LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2
  JOURNAL   Cell Signal 91, 110220 (2022)
   PUBMED   34923106
  REMARK    GeneRIF: LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2.
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Wang,G., Wang,Z., Gao,S., Wang,Y. and Li,Q.
  TITLE     Curcumin enhances the proliferation and myelinization of Schwann
            cells through Runx2 to repair sciatic nerve injury
  JOURNAL   Neurosci Lett 770, 136391 (2022)
   PUBMED   34902518
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Xiao,Z.S., Thomas,R., Hinson,T.K. and Quarles,L.D.
  TITLE     Genomic structure and isoform expression of the mouse, rat and
            human Cbfa1/Osf2 transcription factor
  JOURNAL   Gene 214 (1-2), 187-197 (1998)
   PUBMED   9651525
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Thirunavukkarasu,K., Mahajan,M., McLarren,K.W., Stifani,S. and
            Karsenty,G.
  TITLE     Two domains unique to osteoblast-specific transcription factor
            Osf2/Cbfa1 contribute to its transactivation function and its
            inability to heterodimerize with Cbfbeta
  JOURNAL   Mol Cell Biol 18 (7), 4197-4208 (1998)
   PUBMED   9632804
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Ducy,P., Zhang,R., Geoffroy,V., Ridall,A.L. and Karsenty,G.
  TITLE     Osf2/Cbfa1: a transcriptional activator of osteoblast
            differentiation
  JOURNAL   Cell 89 (5), 747-754 (1997)
   PUBMED   9182762
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Satake,M., Nomura,S., Yamaguchi-Iwai,Y., Takahama,Y., Hashimoto,Y.,
            Niki,M., Kitamura,Y. and Ito,Y.
  TITLE     Expression of the Runt domain-encoding PEBP2 alpha genes in T cells
            during thymic development
  JOURNAL   Mol Cell Biol 15 (3), 1662-1670 (1995)
   PUBMED   7862157
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.49330.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:9632804)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..529
                     /product="runt-related transcription factor 2 isoform 1"
                     /note="core-binding factor subunit alpha-1;
                     osteoblast-specific transcription factor 2; runt-related
                     transcription factor 2"
                     /calculated_mol_wt=57498
     Region          110..238
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <274..489
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          438..529
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..529
                     /gene="Runx2"
                     /gene_synonym="CBF-alpha-1; Cbfa1; OSF-2"
                     /coded_by="NM_001278483.2:209..1798"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:367218"
                     /db_xref="RGD:2282"
ORIGIN      
        1 masnslfsav tpcqqnffwd pstsrrfspp ssslqpgkms dvspvvaaqq qqqqqqqqqq
       61 qqqqqqqqqq qqqqqqqqqe aaaaaaaaaa aaaaaaavpr lrpphdnrtm veiiadhpae
      121 lvrtdspnfl csvlpshwrc nktlpvafkv valgevpdgt vvtvmagnde nysaelrnas
      181 avmknqvarf ndlrfvgrsg rgksftltit vftnppqvat yhraikvtvd gpreprrhrq
      241 klddskpslf sdrlsdlgri phpsmrvgvp pqnprpslns apspfnpqgq sqitdprqtq
      301 ssppwsydqs ypsylsqmts psihsttpls strgtglpai tdvprrisdd dtatsdfclw
      361 psslskksqa gaselgpfsd prqfpgissl tesrfsnprm hypatftytp pvtsgmslgm
      421 satthyhtyl pppypgssqs qsgpfqtsst pylyygtssa syqfpmvpgg drspsrmvpp
      481 ctttsngstl lnpnlpnqnd gvdadgshss sptvlnssgr mdesvwrpy
//
LOCUS       NP_476490                318 aa            linear   ROD 25-MAR-2025
DEFINITION  tumor necrosis factor ligand superfamily member 11 [Rattus
            norvegicus].
ACCESSION   NP_476490 XP_003751569 XP_006252436
VERSION     NP_476490.2
DBSOURCE    REFSEQ: accession NM_057149.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Wu,Z., Duan,S., Li,M., Zhang,A., Yang,H., Luo,J., Cheng,R. and
            Hu,T.
  TITLE     Autophagy regulates bone loss via the RANKL/RANK/OPG axis in an
            experimental rat apical periodontitis model
  JOURNAL   Int Endod J 57 (9), 1315-1325 (2024)
   PUBMED   38923421
  REMARK    GeneRIF: Autophagy regulates bone loss via the RANKL/RANK/OPG axis
            in an experimental rat apical periodontitis model.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Lim,J.H., Kim,H.Y., Kang,H.G., Jeong,H.J. and Kim,H.M.
  TITLE     RANKL down-regulates the mast cell proliferation through inducing
            senescence
  JOURNAL   Cytokine 159, 156018 (2022)
   PUBMED   36054965
  REMARK    GeneRIF: RANKL down-regulates the mast cell proliferation through
            inducing senescence.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Zhou,J., Guo,L., Yang,Y., Liu,Y. and Zhang,C.
  TITLE     Mechanical force regulates root resorption in rats through RANKL
            and OPG
  JOURNAL   BMC Oral Health 22 (1), 290 (2022)
   PUBMED   35842599
  REMARK    GeneRIF: Mechanical force regulates root resorption in rats through
            RANKL and OPG.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Han,S.Y. and Kim,Y.K.
  TITLE     Yukmijihwang-Tang Suppresses Receptor Activator of Nuclear Factor
            Kappa-B Ligand (RANKL)-Induced Osteoclast Differentiation and
            Prevents Ovariectomy (OVX)-Mediated Bone Loss
  JOURNAL   Molecules 26 (24), 7579 (2021)
   PUBMED   34946658
  REMARK    GeneRIF: Yukmijihwang-Tang Suppresses Receptor Activator of Nuclear
            Factor Kappa-B Ligand (RANKL)-Induced Osteoclast Differentiation
            and Prevents Ovariectomy (OVX)-Mediated Bone Loss.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Tomaszewska,E., Rudyk,H., Swietlicka,I., Hulas-Stasiak,M.,
            Donaldson,J., Arczewska,M., Muszynski,S., Dobrowolski,P., Puzio,I.,
            Kushnir,V., Brezvyn,O., Muzyka,V. and Kotsyumbas,I.
  TITLE     The Influence of Prenatal Fumonisin Exposure on Bone Properties, as
            well as OPG and RANKL Expression and Immunolocalization, in Newborn
            Offspring Is Sex and Dose Dependent
  JOURNAL   Int J Mol Sci 22 (24), 13234 (2021)
   PUBMED   34948030
  REMARK    GeneRIF: The Influence of Prenatal Fumonisin Exposure on Bone
            Properties, as well as OPG and RANKL Expression and
            Immunolocalization, in Newborn Offspring Is Sex and Dose Dependent.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Odgren,P.R., Kim,N., van Wesenbeeck,L., MacKay,C., Mason-Savas,A.,
            Safadi,F.F., Popoff,S.N., Lengner,C., van-Hul,W., Choi,Y. and
            Marks,S.C. Jr.
  TITLE     Evidence that the rat osteopetrotic mutation toothless (tl) is not
            in the TNFSF11 (TRANCE, RANKL, ODF, OPGL) gene
  JOURNAL   Int J Dev Biol 45 (8), 853-859 (2001)
   PUBMED   11804028
  REMARK    GeneRIF: the toothless (tl) osteopetrotic rat mutation is not in
            the TNFSF11 locus
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Xu,J., Tan,J.W., Huang,L., Gao,X.H., Laird,R., Liu,D., Wysocki,S.
            and Zheng,M.H.
  TITLE     Cloning, sequencing, and functional characterization of the rat
            homologue of receptor activator of NF-kappaB ligand
  JOURNAL   J Bone Miner Res 15 (11), 2178-2186 (2000)
   PUBMED   11092398
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Fata,J.E., Kong,Y.Y., Li,J., Sasaki,T., Irie-Sasaki,J.,
            Moorehead,R.A., Elliott,R., Scully,S., Voura,E.B., Lacey,D.L.,
            Boyle,W.J., Khokha,R. and Penninger,J.M.
  TITLE     The osteoclast differentiation factor osteoprotegerin-ligand is
            essential for mammary gland development
  JOURNAL   Cell 103 (1), 41-50 (2000)
   PUBMED   11051546
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Kong,Y.Y., Yoshida,H., Sarosi,I., Tan,H.L., Timms,E.,
            Capparelli,C., Morony,S., Oliveira-dos-Santos,A.J., Van,G.,
            Itie,A., Khoo,W., Wakeham,A., Dunstan,C.R., Lacey,D.L., Mak,T.W.,
            Boyle,W.J. and Penninger,J.M.
  TITLE     OPGL is a key regulator of osteoclastogenesis, lymphocyte
            development and lymph-node organogenesis
  JOURNAL   Nature 397 (6717), 315-323 (1999)
   PUBMED   9950424
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Anderson,D.M., Maraskovsky,E., Billingsley,W.L., Dougall,W.C.,
            Tometsko,M.E., Roux,E.R., Teepe,M.C., DuBose,R.F., Cosman,D. and
            Galibert,L.
  TITLE     A homologue of the TNF receptor and its ligand enhance T-cell
            growth and dendritic-cell function
  JOURNAL   Nature 390 (6656), 175-179 (1997)
   PUBMED   9367155
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Sep 13, 2022 this sequence version replaced NP_476490.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.54384.1,
                                           SRR26643292.54782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680414, SAMN06680432
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..318
                     /product="tumor necrosis factor ligand superfamily member
                     11"
                     /note="osteoprotegerin ligand; osteoclast differentiation
                     factor; TNF-related activation-induced cytokine; receptor
                     activator of nuclear factor kappa-B ligand; tumor necrosis
                     factor (ligand) superfamily, member 11; tumor necrosis
                     factor superfamily member 11"
                     /calculated_mol_wt=35211
     Region          13..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESE2.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESE2.1)"
     Site            140..141
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9ESE2.1)"
     Site            order(168,216,218,277,282,308,312)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Region          186..314
                     /region_name="TNF"
                     /note="TNF(Tumour Necrosis Factor) family; pfam00229"
                     /db_xref="CDD:425540"
     Site            order(189..190,195,240,247,252)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESE2.1)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESE2.1)"
     CDS             1..318
                     /gene="Tnfsf11"
                     /gene_synonym="ODF; OPGL; RANKL; TRANCE"
                     /coded_by="NM_057149.2:155..1111"
                     /db_xref="GeneID:117516"
                     /db_xref="RGD:620784"
ORIGIN      
        1 mrrasrdygk ylrgseemgs cpgvphegpl hpapsapapa pppaasrfmf lallglglgq
       61 vvcsialfly fraqmdpnri sedstrcfyr ilrlrentgl qdstlesedt ealpdscrrm
      121 kqafqgavqr elqhivgpqr fsgvpammeg swldvarrgk peaqpfahlt inaanipsgs
      181 hkvslsswyh drgwakisnm tlsngklrvn qdgfyylyan icfrhhetsg svpadylqlm
      241 vyvvktsiki psshnlmkgg stknwsgnse fhfysinvgg ffklrageei svqvsnpsll
      301 dpdqdatyfg afkvqdid
//
LOCUS       NP_037195               1014 aa            linear   ROD 25-MAR-2025
DEFINITION  poly [ADP-ribose] polymerase 1 [Rattus norvegicus].
ACCESSION   NP_037195
VERSION     NP_037195.1
DBSOURCE    REFSEQ: accession NM_013063.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1014)
  AUTHORS   Wen,J.J., Dejesus,J.E., Radhakrishnan,G.L. and Radhakrishnan,R.S.
  TITLE     PARP1 Inhibition and Effect on Burn Injury-Induced Inflammatory
            Response and Cardiac Function
  JOURNAL   J Am Coll Surg 236 (4), 783-802 (2023)
   PUBMED   36728307
  REMARK    GeneRIF: PARP1 Inhibition and Effect on Burn Injury-Induced
            Inflammatory Response and Cardiac Function.
REFERENCE   2  (residues 1 to 1014)
  AUTHORS   Chen,Q., Zhang,E., Wang,C., Zhang,P. and Huang,L.
  TITLE     PARP-1 Inhibition Repressed Imbalance of Th17 and Treg Cells in
            Preterm Rats with Intrauterine Infection-Induced Acute Respiratory
            Distress Syndrome by Reducing the Expression Level of IL-6
  JOURNAL   J Healthc Eng 2022, 1255674 (2022)
   PUBMED   35190759
  REMARK    GeneRIF: PARP-1 Inhibition Repressed Imbalance of Th17 and Treg
            Cells in Preterm Rats with Intrauterine Infection-Induced Acute
            Respiratory Distress Syndrome by Reducing the Expression Level of
            IL-6.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1014)
  AUTHORS   Wang,L., Wang,P., Xu,S., Li,Z., Duan,D.D., Ye,J., Li,J., Ding,Y.,
            Zhang,W., Lu,J. and Liu,P.
  TITLE     The cross-talk between PARylation and SUMOylation in C/EBPbeta at
            K134 site participates in pathological cardiac hypertrophy
  JOURNAL   Int J Biol Sci 18 (2), 783-799 (2022)
   PUBMED   35002525
  REMARK    GeneRIF: The cross-talk between PARylation and SUMOylation in
            C/EBPbeta at K134 site participates in pathological cardiac
            hypertrophy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1014)
  AUTHORS   Zhao,R., Jin,X., Li,A., Xu,B., Shen,Y., Wang,W., Huang,J., Zhang,Y.
            and Li,X.
  TITLE     Precise Diabetic Wound Therapy: PLS Nanospheres Eliminate Senescent
            Cells via DPP4 Targeting and PARP1 Activation
  JOURNAL   Adv Sci (Weinh) 9 (1), e2104128 (2022)
   PUBMED   34738744
  REMARK    GeneRIF: Precise Diabetic Wound Therapy: PLS Nanospheres Eliminate
            Senescent Cells via DPP4 Targeting and PARP1 Activation.
REFERENCE   5  (residues 1 to 1014)
  AUTHORS   Kuchmerovska,T., Guzyk,M., Tykhonenko,T., Yanitska,L.,
            Pryvrotska,I. and Diakun,K.
  TITLE     The parp-1 and bax genes as potential targets for treatment of the
            heart functioning impairments induced by type 1 diabetes mellitus
  JOURNAL   Endocr Regul 55 (2), 61-71 (2021)
   PUBMED   34020532
  REMARK    GeneRIF: The parp-1 and bax genes as potential targets for
            treatment of the heart functioning impairments induced by type 1
            diabetes mellitus.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1014)
  AUTHORS   Endres,M., Wang,Z.Q., Namura,S., Waeber,C. and Moskowitz,M.A.
  TITLE     Ischemic brain injury is mediated by the activation of
            poly(ADP-ribose)polymerase
  JOURNAL   J Cereb Blood Flow Metab 17 (11), 1143-1151 (1997)
   PUBMED   9390645
REFERENCE   7  (residues 1 to 1014)
  AUTHORS   Beneke,S., Meyer,R. and Burkle,A.
  TITLE     Isolation of cDNA encoding full-length rat (Rattus norvegicus) poly
            (ADP-ribose) polymerase
  JOURNAL   Biochem Mol Biol Int 43 (4), 755-761 (1997)
   PUBMED   9385436
  REMARK    Erratum:[Biochem Mol Biol Int 1998 May;44(6):1273]
REFERENCE   8  (residues 1 to 1014)
  AUTHORS   Marsischky,G.T., Wilson,B.A. and Collier,R.J.
  TITLE     Role of glutamic acid 988 of human poly-ADP-ribose polymerase in
            polymer formation. Evidence for active site similarities to the
            ADP-ribosylating toxins
  JOURNAL   J Biol Chem 270 (7), 3247-3254 (1995)
   PUBMED   7852410
REFERENCE   9  (residues 1 to 1014)
  AUTHORS   Potvin,F., Thibodeau,J., Kirkland,J.B., Dandenault,B., Duchaine,C.
            and Poirier,G.G.
  TITLE     Structural analysis of the putative regulatory region of the rat
            gene encoding poly(ADP-ribose) polymerase
  JOURNAL   FEBS Lett 302 (3), 269-273 (1992)
   PUBMED   1601134
REFERENCE   10 (residues 1 to 1014)
  AUTHORS   Thibodeau,J., Gradwohl,G., Dumas,C., Clairoux-Moreau,S., Brunet,G.,
            Penning,C., Poirier,G.G. and Moreau,P.
  TITLE     Cloning of rodent cDNA coding the poly(ADP-ribose) polymerase
            catalytic domain and analysis of mRNA levels during the cell cycle
  JOURNAL   Biochem Cell Biol 67 (9), 653-660 (1989)
   PUBMED   2508731
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085765.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085765.1, U94340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..1014
                     /product="poly [ADP-ribose] polymerase 1"
                     /EC_number="2.4.2.30"
                     /note="poly[ADP-ribose] synthetase 1; NAD(+)
                     ADP-ribosyltransferase 1; ADPRT 1; DNA
                     ADP-ribosyltransferase PARP1; protein
                     poly-ADP-ribosyltransferase PARP1; poly[ADP-ribose]
                     synthase 1; ADP-ribosyltransferase (NAD+; poly
                     (ADP-ribose) polymerase); poly(ADP-ribose) polymerase
                     PARP-1; poly (ADP-ribose) polymerase family, member 1;
                     ADP-ribosyltransferase diphtheria toxin-like 1"
                     /calculated_mol_wt=112530
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Region          9..1010
                     /region_name="PLN03123"
                     /note="poly [ADP-ribose] polymerase; Provisional"
                     /db_xref="CDD:215590"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Region          207..209
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P09874"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Site            214..215
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and caspase-7.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Region          221..226
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P09874"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Region          291..333
                     /region_name="Zinc ribbon.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01351"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Region          357..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Region          374..524
                     /region_name="Automodification domain.
                     /evidence=ECO:0000250|UniProtKB:P09874"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Region          496..519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27008.4)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            600
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            621
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09874; propagated from
                     UniProtKB/Swiss-Prot (P27008.4)"
     CDS             1..1014
                     /gene="Parp1"
                     /gene_synonym="Adprt; ARTD1; Parp-1"
                     /coded_by="NM_013063.2:63..3107"
                     /db_xref="GeneID:25591"
                     /db_xref="RGD:2053"
ORIGIN      
        1 maeaterlyr veyaksgras ckkcsesipk dslrmaimvq spmfdgkvph wyhfscfwkv
       61 ghsirqpdte vdgfselrwd dqqkvkktae aggvagkgqh ggggkaektl gdfaaeyaks
      121 nrstckgcme kiekgqmrls kkmldpekpq lgmidrwyhp tcfvknrdel gfrpeysasq
      181 lkgfsllsae dkealkkqlp avksegkrkc devdgideva kkkskkgkdk essklekalk
      241 aqnelvwnik delkkacstn dlkellifnq qqvpsgesai ldrvadgmaf gallpckecs
      301 gqlvfksday yctgdvtawt kcmvktqnps rkewvtpkef reisylkklk ikkqdrlfpp
      361 essapappap pvsitsapta vnssapadkp lsnmkiltlg klsqnkdeak amieklggkl
      421 tgsankaslc istkkevekm skkmeevkaa nvrvvcedfl qdvsasaksl qellsahsls
      481 swgaevkvep gevvvpkgks aapskkskga vkeegvnkse krmkltlkgg aavdpdsgle
      541 hsahvlekgg kvfsatlglv divkgtnsyy klqllesdke srywifrswg rvgtvigsnk
      601 leqmpskeda vehfmklyee ktgnawhskn ftkypkkfyp leidygqdee avkklavkpg
      661 tksklpkpvq elvgmifdve smkkalveye idlqkmplgk lsrrqiqaay silsevqqav
      721 sqgssesqil dlsnrfytli phdfgmkkpp llnntdsvqa kvemldnlld ievaysllrg
      781 gsddsskdpi dvnyeklktd ikvvdrdsee aevirkyvkn thatthnayd levidifkie
      841 regesqrykp frqlhnrrll whgsrttnfa gilsqglria ppeapvtgym fgkgiyfadm
      901 vsksanycht sqgdpiglil lgevalgnmy elkhashisk lpkgkhsvkg lgktapdpsa
      961 sitldgvevp lgtgipsgvn dtcllyneyi vydiaqvnlk yllklkfnfk tslw
//
LOCUS       NP_653345                244 aa            linear   ROD 25-MAR-2025
DEFINITION  adiponectin precursor [Rattus norvegicus].
ACCESSION   NP_653345
VERSION     NP_653345.1
DBSOURCE    REFSEQ: accession NM_144744.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Zhou,Y., Zhang,S., Jia,Y., Wang,X., Liu,Y., Zhang,H., Yuan,Z.,
            Han,Y. and Weng,Q.
  TITLE     Regulation and Role of Adiponectin Secretion in Rat Ovarian
            Granulosa Cells
  JOURNAL   Int J Mol Sci 25 (10), 5155 (2024)
   PUBMED   38791193
  REMARK    GeneRIF: Regulation and Role of Adiponectin Secretion in Rat
            Ovarian Granulosa Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Khoramipour,K., Bejeshk,M.A., Rajizadeh,M.A., Najafipour,H.,
            Dehghan,P. and Farahmand,F.
  TITLE     High-Intensity Interval Training Ameliorates Molecular Changes in
            the Hippocampus of Male Rats with the Diabetic Brain: the Role of
            Adiponectin
  JOURNAL   Mol Neurobiol 60 (6), 3486-3495 (2023)
   PUBMED   36877358
  REMARK    GeneRIF: High-Intensity Interval Training Ameliorates Molecular
            Changes in the Hippocampus of Male Rats with the Diabetic Brain:
            the Role of Adiponectin.
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Cheng,R., Xu,X., Yang,S., Mi,Z., Zhao,Y., Wang,C., Shi,X., Gao,J.,
            Yu,F. and Ren,X.
  TITLE     The effect of APN, hs-CRP and APN/hs-CRP in periodontitis with DAA
  JOURNAL   BMC Oral Health 23 (1), 85 (2023)
   PUBMED   36765308
  REMARK    GeneRIF: The effect of APN, hs-CRP and APN/hs-CRP in periodontitis
            with DAA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Marine-Casado,R., Domenech-Coca,C., Crescenti,A., Rodriguez
            Gomez,M.A., Del Bas,J.M., Arola,L., Boque,N. and Caimari,A.
  TITLE     Maternal Supplementation with a Cocoa Extract during Lactation
            Deeply Modulates Dams' Metabolism, Increases Adiponectin
            Circulating Levels and Improves the Inflammatory Profile in Obese
            Rat Offspring
  JOURNAL   Nutrients 14 (23), 5134 (2022)
   PUBMED   36501173
  REMARK    GeneRIF: Maternal Supplementation with a Cocoa Extract during
            Lactation Deeply Modulates Dams' Metabolism, Increases Adiponectin
            Circulating Levels and Improves the Inflammatory Profile in Obese
            Rat Offspring.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Qiao,N., Zhang,J., Zhang,Y. and Liu,X.
  TITLE     Crosstalk between CD93, C1q and GIPC in the Regulation of
            Pneumococcal Meningitis Inflammation
  JOURNAL   Ann Clin Lab Sci 52 (4), 634-641 (2022)
   PUBMED   36197773
  REMARK    GeneRIF: Crosstalk between CD93, C1q and GIPC in the Regulation of
            Pneumococcal Meningitis Inflammation.
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Yokota,T., Oritani,K., Takahashi,I., Ishikawa,J., Matsuyama,A.,
            Ouchi,N., Kihara,S., Funahashi,T., Tenner,A.J., Tomiyama,Y. and
            Matsuzawa,Y.
  TITLE     Adiponectin, a new member of the family of soluble defense
            collagens, negatively regulates the growth of myelomonocytic
            progenitors and the functions of macrophages
  JOURNAL   Blood 96 (5), 1723-1732 (2000)
   PUBMED   10961870
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Ouchi,N., Kihara,S., Arita,Y., Maeda,K., Kuriyama,H., Okamoto,Y.,
            Hotta,K., Nishida,M., Takahashi,M., Nakamura,T., Yamashita,S.,
            Funahashi,T. and Matsuzawa,Y.
  TITLE     Novel modulator for endothelial adhesion molecules:
            adipocyte-derived plasma protein adiponectin
  JOURNAL   Circulation 100 (25), 2473-2476 (1999)
   PUBMED   10604883
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Bogan,J.S. and Lodish,H.F.
  TITLE     Two compartments for insulin-stimulated exocytosis in 3T3-L1
            adipocytes defined by endogenous ACRP30 and GLUT4
  JOURNAL   J Cell Biol 146 (3), 609-620 (1999)
   PUBMED   10444069
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Schaffler,A., Orso,E., Palitzsch,K.D., Buchler,C., Drobnik,W.,
            Furst,A., Scholmerich,J. and Schmitz,G.
  TITLE     The human apM-1, an adipocyte-specific gene linked to the family of
            TNF's and to genes expressed in activated T cells, is mapped to
            chromosome 1q21.3-q23, a susceptibility locus identified for
            familial combined hyperlipidaemia (FCH)
  JOURNAL   Biochem Biophys Res Commun 260 (2), 416-425 (1999)
   PUBMED   10403784
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Scherer,P.E., Williams,S., Fogliano,M., Baldini,G. and Lodish,H.F.
  TITLE     A novel serum protein similar to C1q, produced exclusively in
            adipocytes
  JOURNAL   J Biol Chem 270 (45), 26746-26749 (1995)
   PUBMED   7592907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM047633.1 and JAXUCZ010000011.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078720.1, FM047633.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..244
                     /product="adiponectin precursor"
                     /note="adipocyte complement related protein of 30 kDa;
                     adiponectin d"
                     /calculated_mol_wt=24406
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2022
     Region          51..107
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          109..242
                     /region_name="C1Q"
                     /note="Complement component C1q domain; smart00110"
                     /db_xref="CDD:128420"
     CDS             1..244
                     /gene="Adipoq"
                     /gene_synonym="Acdc; Acrp30; Adid"
                     /coded_by="NM_144744.3:86..820"
                     /db_xref="GeneID:246253"
                     /db_xref="RGD:628748"
ORIGIN      
        1 mlllqallfl lilpshegit ategpgalvp ppketcagwm agipgypghn gipgrdgrdg
       61 tpgekgekgd agvlgpkgdp gdagmtgaeg prgfpgtpgr kgepgeaaym yhsafsvgle
      121 trvtvpnvpi rftkifynqq nhydgstgkf hcnipglyyf syhitvymkd vkvslfkkdk
      181 avlftydqyq eknvdqasgs mllhlevgdq vwlqvygegd nnglyadnvn dstftgflly
      241 hdtn
//
LOCUS       NP_001402684             529 aa            linear   ROD 25-MAR-2025
DEFINITION  runt-related transcription factor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001402684
VERSION     NP_001402684.1
DBSOURCE    REFSEQ: accession NM_001415755.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Gopinathan,G., Luan,X. and Diekwisch,T.G.H.
  TITLE     Epigenetic Repression of RUNX2 and OSX Promoters Controls the
            Nonmineralized State of the Periodontal Ligament
  JOURNAL   Genes (Basel) 14 (1), 201 (2023)
   PUBMED   36672941
  REMARK    GeneRIF: Epigenetic Repression of RUNX2 and OSX Promoters Controls
            the Nonmineralized State of the Periodontal Ligament.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Ma,Z., Wang,Y., Xue,Y., Zhang,W., Li,D., Li,Y., Li,G., Zhou,H.,
            Hu,X., Deng,T. and Hu,K.
  TITLE     Traumatic temporomandibular joint bony ankylosis in growing rats
  JOURNAL   BMC Oral Health 22 (1), 585 (2022)
   PUBMED   36494653
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Xie,S., Chen,M., Fang,W., Liu,S., Wu,Q., Liu,C., Xing,Y., Shi,W.,
            Xu,M., Zhang,M., Chen,S., Zeng,X., Wang,S., Deng,W. and Tang,Q.
  TITLE     Diminished arachidonate 5-lipoxygenase perturbs phase separation
            and transcriptional response of Runx2 to reverse pathological
            ventricular remodeling
  JOURNAL   EBioMedicine 86, 104359 (2022)
   PUBMED   36395739
  REMARK    GeneRIF: Diminished arachidonate 5-lipoxygenase perturbs phase
            separation and transcriptional response of Runx2 to reverse
            pathological ventricular remodeling.
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Zhou,W., Feng,Q., Cheng,M., Zhang,D., Jin,J., Zhang,S., Bai,Y. and
            Xu,J.
  TITLE     LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2
  JOURNAL   Cell Signal 91, 110220 (2022)
   PUBMED   34923106
  REMARK    GeneRIF: LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2.
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Wang,G., Wang,Z., Gao,S., Wang,Y. and Li,Q.
  TITLE     Curcumin enhances the proliferation and myelinization of Schwann
            cells through Runx2 to repair sciatic nerve injury
  JOURNAL   Neurosci Lett 770, 136391 (2022)
   PUBMED   34902518
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Xiao,Z.S., Thomas,R., Hinson,T.K. and Quarles,L.D.
  TITLE     Genomic structure and isoform expression of the mouse, rat and
            human Cbfa1/Osf2 transcription factor
  JOURNAL   Gene 214 (1-2), 187-197 (1998)
   PUBMED   9651525
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Thirunavukkarasu,K., Mahajan,M., McLarren,K.W., Stifani,S. and
            Karsenty,G.
  TITLE     Two domains unique to osteoblast-specific transcription factor
            Osf2/Cbfa1 contribute to its transactivation function and its
            inability to heterodimerize with Cbfbeta
  JOURNAL   Mol Cell Biol 18 (7), 4197-4208 (1998)
   PUBMED   9632804
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Ducy,P., Zhang,R., Geoffroy,V., Ridall,A.L. and Karsenty,G.
  TITLE     Osf2/Cbfa1: a transcriptional activator of osteoblast
            differentiation
  JOURNAL   Cell 89 (5), 747-754 (1997)
   PUBMED   9182762
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Satake,M., Nomura,S., Yamaguchi-Iwai,Y., Takahama,Y., Hashimoto,Y.,
            Niki,M., Kitamura,Y. and Ito,Y.
  TITLE     Expression of the Runt domain-encoding PEBP2 alpha genes in T cells
            during thymic development
  JOURNAL   Mol Cell Biol 15 (3), 1662-1670 (1995)
   PUBMED   7862157
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.49329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..529
                     /product="runt-related transcription factor 2 isoform 1"
                     /note="core-binding factor subunit alpha-1;
                     osteoblast-specific transcription factor 2; runt-related
                     transcription factor 2"
                     /calculated_mol_wt=57498
     Region          110..238
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <274..489
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          438..529
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..529
                     /gene="Runx2"
                     /gene_synonym="CBF-alpha-1; Cbfa1; OSF-2"
                     /coded_by="NM_001415755.1:242..1831"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:367218"
                     /db_xref="RGD:2282"
ORIGIN      
        1 masnslfsav tpcqqnffwd pstsrrfspp ssslqpgkms dvspvvaaqq qqqqqqqqqq
       61 qqqqqqqqqq qqqqqqqqqe aaaaaaaaaa aaaaaaavpr lrpphdnrtm veiiadhpae
      121 lvrtdspnfl csvlpshwrc nktlpvafkv valgevpdgt vvtvmagnde nysaelrnas
      181 avmknqvarf ndlrfvgrsg rgksftltit vftnppqvat yhraikvtvd gpreprrhrq
      241 klddskpslf sdrlsdlgri phpsmrvgvp pqnprpslns apspfnpqgq sqitdprqtq
      301 ssppwsydqs ypsylsqmts psihsttpls strgtglpai tdvprrisdd dtatsdfclw
      361 psslskksqa gaselgpfsd prqfpgissl tesrfsnprm hypatftytp pvtsgmslgm
      421 satthyhtyl pppypgssqs qsgpfqtsst pylyygtssa syqfpmvpgg drspsrmvpp
      481 ctttsngstl lnpnlpnqnd gvdadgshss sptvlnssgr mdesvwrpy
//
LOCUS       NP_001034124             238 aa            linear   ROD 25-MAR-2025
DEFINITION  serine/arginine-rich splicing factor 7 [Rattus norvegicus].
ACCESSION   NP_001034124 XP_343004
VERSION     NP_001034124.2
DBSOURCE    REFSEQ: accession NM_001039035.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Ding,S., Shi,J., Qian,W., Iqbal,K., Grundke-Iqbal,I., Gong,C.X. and
            Liu,F.
  TITLE     Regulation of alternative splicing of tau exon 10 by 9G8 and Dyrk1A
  JOURNAL   Neurobiol Aging 33 (7), 1389-1399 (2012)
   PUBMED   21215488
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Piekielko-Witkowska,A., Wiszomirska,H., Wojcicka,A., Poplawski,P.,
            Boguslawska,J., Tanski,Z. and Nauman,A.
  TITLE     Disturbed expression of splicing factors in renal cancer affects
            alternative splicing of apoptosis regulators, oncogenes, and tumor
            suppressors
  JOURNAL   PLoS One 5 (10), e13690 (2010)
   PUBMED   21082031
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Wang,J., Gao,Q.S., Wang,Y., Lafyatis,R., Stamm,S. and Andreadis,A.
  TITLE     Tau exon 10, whose missplicing causes frontotemporal dementia, is
            regulated by an intricate interplay of cis elements and trans
            factors
  JOURNAL   J Neurochem 88 (5), 1078-1090 (2004)
   PUBMED   15009664
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Venables,J.P., Elliott,D.J., Makarova,O.V., Makarov,E.M.,
            Cooke,H.J. and Eperon,I.C.
  TITLE     RBMY, a probable human spermatogenesis factor, and other hnRNP G
            proteins interact with Tra2beta and affect splicing
  JOURNAL   Hum Mol Genet 9 (5), 685-694 (2000)
   PUBMED   10749975
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Zhang,H., Wada,J., Kanwar,Y.S., Tsuchiyama,Y., Hiragushi,K.,
            Hida,K., Shikata,K. and Makino,H.
  TITLE     Screening for genes up-regulated in 5/6 nephrectomized mouse kidney
  JOURNAL   Kidney Int 56 (2), 549-558 (1999)
   PUBMED   10432394
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Cavaloc,Y., Popielarz,M., Fuchs,J.P., Gattoni,R. and Stevenin,J.
  TITLE     Characterization and cloning of the human splicing factor 9G8: a
            novel 35 kDa factor of the serine/arginine protein family
  JOURNAL   EMBO J 13 (11), 2639-2649 (1994)
   PUBMED   8013463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM084661.1, FM085512.1, JAXUCZ010000006.1, FM092264.1 and
            FM079490.1.
            
            On Sep 14, 2010 this sequence version replaced NP_001034124.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.1186195.1,
                                           SRR22399492.812506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..238
                     /product="serine/arginine-rich splicing factor 7"
                     /note="splicing factor, arginine/serine-rich 7, 35kDa"
                     /calculated_mol_wt=27246
     Region          12..88
                     /region_name="RRM_SRSF7"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     serine/arginine-rich splicing factor 7 (SRSF7); cd12646"
                     /db_xref="CDD:410050"
     Site            order(41,43..45,49,51,82,84)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410050"
     CDS             1..238
                     /gene="Srsf7"
                     /gene_synonym="Sfrs7"
                     /coded_by="NM_001039035.2:96..812"
                     /db_xref="GeneID:362687"
                     /db_xref="RGD:1307425"
ORIGIN      
        1 msrygrygge tkvyvgnlgt gagkgelera fsyygplrtv wiarnppgfa fvefedprda
       61 edavrgldgk vicgsrvrve lstgmprrsr fdrpparrpf dpndrcyecg ekghyaydch
      121 rysrrrrsrs rsrshsrsrg rrysrsrsrs rgrrsrsasp rrsrsvslrr srsaslrrsr
      181 sgsiigsryf qsrsrsrsrs rsisrprssr sksrspspkr srspsgsphr saspermd
//
LOCUS       NP_037002                401 aa            linear   ROD 25-MAR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 11B precursor
            [Rattus norvegicus].
ACCESSION   NP_037002
VERSION     NP_037002.1
DBSOURCE    REFSEQ: accession NM_012870.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Wu,Z., Duan,S., Li,M., Zhang,A., Yang,H., Luo,J., Cheng,R. and
            Hu,T.
  TITLE     Autophagy regulates bone loss via the RANKL/RANK/OPG axis in an
            experimental rat apical periodontitis model
  JOURNAL   Int Endod J 57 (9), 1315-1325 (2024)
   PUBMED   38923421
  REMARK    GeneRIF: Autophagy regulates bone loss via the RANKL/RANK/OPG axis
            in an experimental rat apical periodontitis model.
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhou,J., Guo,L., Yang,Y., Liu,Y. and Zhang,C.
  TITLE     Mechanical force regulates root resorption in rats through RANKL
            and OPG
  JOURNAL   BMC Oral Health 22 (1), 290 (2022)
   PUBMED   35842599
  REMARK    GeneRIF: Mechanical force regulates root resorption in rats through
            RANKL and OPG.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Tomaszewska,E., Rudyk,H., Swietlicka,I., Hulas-Stasiak,M.,
            Donaldson,J., Arczewska,M., Muszynski,S., Dobrowolski,P., Puzio,I.,
            Kushnir,V., Brezvyn,O., Muzyka,V. and Kotsyumbas,I.
  TITLE     The Influence of Prenatal Fumonisin Exposure on Bone Properties, as
            well as OPG and RANKL Expression and Immunolocalization, in Newborn
            Offspring Is Sex and Dose Dependent
  JOURNAL   Int J Mol Sci 22 (24), 13234 (2021)
   PUBMED   34948030
  REMARK    GeneRIF: The Influence of Prenatal Fumonisin Exposure on Bone
            Properties, as well as OPG and RANKL Expression and
            Immunolocalization, in Newborn Offspring Is Sex and Dose Dependent.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Sabry,M., Mostafa,S., Kamar,S., Rashed,L. and Estaphan,S.
  TITLE     The cross-talk between matrix metalloproteinase-9, RANKL/OPG system
            and cardiovascular risk factors in ovariectomized rat model of
            postmenopausal osteoporosis
  JOURNAL   PLoS One 16 (10), e0258254 (2021)
   PUBMED   34610044
  REMARK    GeneRIF: The cross-talk between matrix metalloproteinase-9,
            RANKL/OPG system and cardiovascular risk factors in ovariectomized
            rat model of postmenopausal osteoporosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Wang,L.Y., Wang,B., Cong,B.B., Cui,T., Du,Y.Q. and Song,Y.
  TITLE     [Effect of different orthodontic forces on the expression of T
            helper cell 17 cell-related cytokines in the pressure side of
            periodontal tissue in rats]
  JOURNAL   Hua Xi Kou Qiang Yi Xue Za Zhi 39 (2), 143-152 (2021)
   PUBMED   33834668
  REMARK    GeneRIF: [Effect of different orthodontic forces on the expression
            of T helper cell 17 cell-related cytokines in the pressure side of
            periodontal tissue in rats].
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Cundy,T., Hegde,M., Naot,D., Chong,B., King,A., Wallace,R.,
            Mulley,J., Love,D.R., Seidel,J., Fawkner,M., Banovic,T.,
            Callon,K.E., Grey,A.B., Reid,I.R., Middleton-Hardie,C.A. and
            Cornish,J.
  TITLE     A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an
            idiopathic hyperphosphatasia phenotype
  JOURNAL   Hum Mol Genet 11 (18), 2119-2127 (2002)
   PUBMED   12189164
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Wise,G.E., Yao,S., Zhang,Q. and Ren,Y.
  TITLE     Inhibition of osteoclastogenesis by the secretion of
            osteoprotegerin in vitro by rat dental follicle cells and its
            implications for tooth eruption
  JOURNAL   Arch Oral Biol 47 (3), 247-254 (2002)
   PUBMED   11839361
  REMARK    GeneRIF: except for the period of time in tooth eruption, where
            osteoclast formation is needed to form an eruption pathway,
            secretion of OPG (osteoprotegerin) prevents resorption of alveolar
            bone and subsequent disruption of the periodontal ligament
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Yang,X., Halladay,D., Onyia,J.E., Martin,T.J. and Chandrasekhar,S.
  TITLE     Protein Kinase C is a mediator of the synthesis and secretion of
            osteoprotegerin in osteoblast-like cells
  JOURNAL   Biochem Biophys Res Commun 290 (1), 42-46 (2002)
   PUBMED   11779130
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Gold,B.G., Zeleny-Pooley,M., Chaturvedi,P. and Wang,M.S.
  TITLE     Oral administration of a nonimmunosuppressant FKBP-12 ligand speeds
            nerve regeneration
  JOURNAL   Neuroreport 9 (3), 553-558 (1998)
   PUBMED   9512405
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Simonet,W.S., Lacey,D.L., Dunstan,C.R., Kelley,M., Chang,M.S.,
            Luthy,R., Nguyen,H.Q., Wooden,S., Bennett,L., Boone,T.,
            Shimamoto,G., DeRose,M., Elliott,R., Colombero,A., Tan,H.L.,
            Trail,G., Sullivan,J., Davy,E., Bucay,N., Renshaw-Gegg,L.,
            Hughes,T.M., Hill,D., Pattison,W., Campbell,P., Sander,S., Van,G.,
            Tarpley,J., Derby,P., Lee,R. and Boyle,W.J.
  TITLE     Osteoprotegerin: a novel secreted protein involved in the
            regulation of bone density
  JOURNAL   Cell 89 (2), 309-319 (1997)
   PUBMED   9108485
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081830.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081830.1, U94330.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q32"
     Protein         1..401
                     /product="tumor necrosis factor receptor superfamily
                     member 11B precursor"
                     /note="Osteoprotegerin"
                     /calculated_mol_wt=43670
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2541
     Region          7..151
                     /region_name="TNFRSF11B"
                     /note="Tumor necrosis factor receptor superfamily member
                     11B (TNFRSF11B), also known as Osteoprotegerin (OPG);
                     cd10581"
                     /db_xref="CDD:276907"
     Region          7..62
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276907"
     mat_peptide     22..401
                     /product="Tumor necrosis factor receptor superfamily
                     member 11B. /id=PRO_0000034589"
                     /note="propagated from UniProtKB/Swiss-Prot (O08727.1)"
                     /calculated_mol_wt=43670
     Region          24..62
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O08727.1)"
     Region          65..105
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276907"
     Region          65..105
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O08727.1)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08727.1)"
     Region          107..145
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276907"
     Region          107..142
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O08727.1)"
     Region          124..>187
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          145..186
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276924"
     Region          145..185
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O08727.1)"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08727.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08727.1)"
     Region          278..365
                     /region_name="Death"
                     /note="Death domain; pfam00531"
                     /db_xref="CDD:459845"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08727.1)"
     Site            400
                     /site_type="other"
                     /note="Involved in dimerization. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O08727.1)"
     CDS             1..401
                     /gene="Tnfrsf11b"
                     /gene_synonym="Opg"
                     /coded_by="NM_012870.2:105..1310"
                     /db_xref="GeneID:25341"
                     /db_xref="RGD:619802"
ORIGIN      
        1 mnkwlccall vfldiiewtt qetfppkylh ydpetgrqll cdkcapgtyl kqhctvrrkt
       61 lcvpcpdysy tdswhtsdec vycspvckel qtvkqecnrt hnrvceceeg rylelefclk
      121 hrscppglgv lqagtpernt vckrcpdgff sgetsskapc rkhtncsslg llliqkgnat
      181 hdnvcsgnre atqncgidvt lceeaffrfa vptkiipnwl svlvdslpgt kvnaesveri
      241 krrhssqeqt fqllklwkhq nrdqemvkki iqdidlcess vqrhighanl tteqlrilme
      301 slpgkkispd eiertrktck pseqllklls lwrikngdqd tlkglmyalk hlkayhfpkt
      361 vthslrktir flhsftmyrl yqklflemig nqvqsvkisc l
//
LOCUS       NP_001265413             515 aa            linear   ROD 25-MAR-2025
DEFINITION  runt-related transcription factor 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001265413
VERSION     NP_001265413.1
DBSOURCE    REFSEQ: accession NM_001278484.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Gopinathan,G., Luan,X. and Diekwisch,T.G.H.
  TITLE     Epigenetic Repression of RUNX2 and OSX Promoters Controls the
            Nonmineralized State of the Periodontal Ligament
  JOURNAL   Genes (Basel) 14 (1), 201 (2023)
   PUBMED   36672941
  REMARK    GeneRIF: Epigenetic Repression of RUNX2 and OSX Promoters Controls
            the Nonmineralized State of the Periodontal Ligament.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Ma,Z., Wang,Y., Xue,Y., Zhang,W., Li,D., Li,Y., Li,G., Zhou,H.,
            Hu,X., Deng,T. and Hu,K.
  TITLE     Traumatic temporomandibular joint bony ankylosis in growing rats
  JOURNAL   BMC Oral Health 22 (1), 585 (2022)
   PUBMED   36494653
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Xie,S., Chen,M., Fang,W., Liu,S., Wu,Q., Liu,C., Xing,Y., Shi,W.,
            Xu,M., Zhang,M., Chen,S., Zeng,X., Wang,S., Deng,W. and Tang,Q.
  TITLE     Diminished arachidonate 5-lipoxygenase perturbs phase separation
            and transcriptional response of Runx2 to reverse pathological
            ventricular remodeling
  JOURNAL   EBioMedicine 86, 104359 (2022)
   PUBMED   36395739
  REMARK    GeneRIF: Diminished arachidonate 5-lipoxygenase perturbs phase
            separation and transcriptional response of Runx2 to reverse
            pathological ventricular remodeling.
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Zhou,W., Feng,Q., Cheng,M., Zhang,D., Jin,J., Zhang,S., Bai,Y. and
            Xu,J.
  TITLE     LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2
  JOURNAL   Cell Signal 91, 110220 (2022)
   PUBMED   34923106
  REMARK    GeneRIF: LncRNA H19 sponges miR-103-3p to promote the high
            phosphorus-induced osteoblast phenotypic transition of vascular
            smooth muscle cells by upregulating Runx2.
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Wang,G., Wang,Z., Gao,S., Wang,Y. and Li,Q.
  TITLE     Curcumin enhances the proliferation and myelinization of Schwann
            cells through Runx2 to repair sciatic nerve injury
  JOURNAL   Neurosci Lett 770, 136391 (2022)
   PUBMED   34902518
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Xiao,Z.S., Thomas,R., Hinson,T.K. and Quarles,L.D.
  TITLE     Genomic structure and isoform expression of the mouse, rat and
            human Cbfa1/Osf2 transcription factor
  JOURNAL   Gene 214 (1-2), 187-197 (1998)
   PUBMED   9651525
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Thirunavukkarasu,K., Mahajan,M., McLarren,K.W., Stifani,S. and
            Karsenty,G.
  TITLE     Two domains unique to osteoblast-specific transcription factor
            Osf2/Cbfa1 contribute to its transactivation function and its
            inability to heterodimerize with Cbfbeta
  JOURNAL   Mol Cell Biol 18 (7), 4197-4208 (1998)
   PUBMED   9632804
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Ducy,P., Zhang,R., Geoffroy,V., Ridall,A.L. and Karsenty,G.
  TITLE     Osf2/Cbfa1: a transcriptional activator of osteoblast
            differentiation
  JOURNAL   Cell 89 (5), 747-754 (1997)
   PUBMED   9182762
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Satake,M., Nomura,S., Yamaguchi-Iwai,Y., Takahama,Y., Hashimoto,Y.,
            Niki,M., Kitamura,Y. and Ito,Y.
  TITLE     Expression of the Runt domain-encoding PEBP2 alpha genes in T cells
            during thymic development
  JOURNAL   Mol Cell Biol 15 (3), 1662-1670 (1995)
   PUBMED   7862157
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1250638.1,
                                           SRR26360181.250837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..515
                     /product="runt-related transcription factor 2 isoform 2"
                     /note="core-binding factor subunit alpha-1;
                     osteoblast-specific transcription factor 2; runt-related
                     transcription factor 2"
                     /calculated_mol_wt=55934
     Region          96..224
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <260..475
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          424..515
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..515
                     /gene="Runx2"
                     /gene_synonym="CBF-alpha-1; Cbfa1; OSF-2"
                     /coded_by="NM_001278484.3:26..1573"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:367218"
                     /db_xref="RGD:2282"
ORIGIN      
        1 mripvdpsts rrfsppsssl qpgkmsdvsp vvaaqqqqqq qqqqqqqqqq qqqqqqqqqq
       61 qqqqqeaaaa aaaaaaaaaa aaavprlrpp hdnrtmveii adhpaelvrt dspnflcsvl
      121 pshwrcnktl pvafkvvalg evpdgtvvtv magndenysa elrnasavmk nqvarfndlr
      181 fvgrsgrgks ftltitvftn ppqvatyhra ikvtvdgpre prrhrqkldd skpslfsdrl
      241 sdlgriphps mrvgvppqnp rpslnsapsp fnpqgqsqit dprqtqsspp wsydqsypsy
      301 lsqmtspsih sttplsstrg tglpaitdvp rrisdddtat sdfclwpssl skksqagase
      361 lgpfsdprqf pgissltesr fsnprmhypa tftytppvts gmslgmsatt hyhtylpppy
      421 pgssqsqsgp fqtsstpyly ygtssasyqf pmvpggdrsp srmvppcttt sngstllnpn
      481 lpnqndgvda dgshsssptv lnssgrmdes vwrpy
//
LOCUS       NP_058892                147 aa            linear   ROD 25-MAR-2025
DEFINITION  allograft inflammatory factor 1 [Rattus norvegicus].
ACCESSION   NP_058892 NP_071619 XP_346598
VERSION     NP_058892.1
DBSOURCE    REFSEQ: accession NM_017196.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Wu,Q., Qin,B., Wu,X., Zhang,M., Gan,Z., Lan,Y., Ma,C. and Fu,W.
  TITLE     Allograft inflammatory factor-1 enhances inflammation and oxidative
            stress via the NF-kappaB pathway of bladder urothelium in diabetic
            rat model
  JOURNAL   Cytokine 173, 156438 (2024)
   PUBMED   37976702
  REMARK    GeneRIF: Allograft inflammatory factor-1 enhances inflammation and
            oxidative stress via the NF-kappaB pathway of bladder urothelium in
            diabetic rat model.
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Gheorghe,R.O., Grosu,A.V., Magercu,M., Ghenghea,M.S., Zbarcea,C.E.,
            Tanase,A., Negres,S., Filippi,A., Chiritoiu,G., Gherghiceanu,M.,
            Dinescu,S., Gaina,G., Sapunar,D. and Ristoiu,V.
  TITLE     Switching Rat Resident Macrophages from M1 to M2 Phenotype by Iba1
            Silencing Has Analgesic Effects in SNL-Induced Neuropathic Pain
  JOURNAL   Int J Mol Sci 24 (21), 15831 (2023)
   PUBMED   37958812
  REMARK    GeneRIF: Switching Rat Resident Macrophages from M1 to M2 Phenotype
            by Iba1 Silencing Has Analgesic Effects in SNL-Induced Neuropathic
            Pain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jeong,S., Yoon,K.S., Lee,J.M., Jo,E.S., Kim,D. and Choi,S.O.
  TITLE     Neurotoxic and cardiotoxic effects of
            N-methyl-1-(naphthalen-2-yl)propan-2-amine (methamnetamine) and
            1-phenyl-2-pyrrolidinylpentane (prolintane)
  JOURNAL   Drug Chem Toxicol 46 (3), 430-440 (2023)
   PUBMED   35296205
  REMARK    GeneRIF: Neurotoxic and cardiotoxic effects of
            N-methyl-1-(naphthalen-2-yl)propan-2-amine (methamnetamine) and
            1-phenyl-2-pyrrolidinylpentane (prolintane).
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Gok,E. and Deveci,E.
  TITLE     Histopathological evaluation of IBA-1, GFAP activity in the brain
            cortex of rats administered cadmium chloride
  JOURNAL   Arch Ital Biol 160 (1-2), 20-27 (2022)
   PUBMED   35913387
  REMARK    GeneRIF: Histopathological evaluation of IBA-1, GFAP activity in
            the brain cortex of rats administered cadmium chloride.
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Hung,T.W., Wu,K.J., Wang,Y.S., Bae,E.K., Song,Y., Yoon,J. and
            Yu,S.J.
  TITLE     Human Milk Oligosaccharide 2'-Fucosyllactose Induces
            Neuroprotection from Intracerebral Hemorrhage Stroke
  JOURNAL   Int J Mol Sci 22 (18), 9881 (2021)
   PUBMED   34576050
  REMARK    GeneRIF: Human Milk Oligosaccharide 2'-Fucosyllactose Induces
            Neuroprotection from Intracerebral Hemorrhage Stroke.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Chen,Z.W., Ahren,B., Ostenson,C.G., Cintra,A., Bergman,T.,
            Moller,C., Fuxe,K., Mutt,V., Jornvall,H. and Efendic,S.
  TITLE     Identification, isolation, and characterization of daintain
            (allograft inflammatory factor 1), a macrophage polypeptide with
            effects on insulin secretion and abundantly present in the pancreas
            of prediabetic BB rats
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13879-13884 (1997)
   PUBMED   9391121
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Imai,Y., Ibata,I., Ito,D., Ohsawa,K. and Kohsaka,S.
  TITLE     A novel gene iba1 in the major histocompatibility complex class III
            region encoding an EF hand protein expressed in a monocytic lineage
  JOURNAL   Biochem Biophys Res Commun 224 (3), 855-862 (1996)
   PUBMED   8713135
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Autieri,M.V., Prystowsky,M.B. and Ohlstein,E.H.
  TITLE     Isolation and characterization of BART-1: A novel balloon
            angioplasty responsive transcript in rat carotid arteries
  JOURNAL   DNA Cell Biol 15 (4), 297-304 (1996)
   PUBMED   8639266
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Autieri,M.V., Feuerstein,G.Z., Yue,T.L., Ohlstein,E.H. and
            Douglas,S.A.
  TITLE     Use of differential display to identify differentially expressed
            mRNAs induced by rat carotid artery balloon angioplasty
  JOURNAL   Lab Invest 72 (6), 656-661 (1995)
   PUBMED   7783423
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Utans,U., Arceci,R.J., Yamashita,Y. and Russell,M.E.
  TITLE     Cloning and characterization of allograft inflammatory factor-1: a
            novel macrophage factor identified in rat cardiac allografts with
            chronic rejection
  JOURNAL   J Clin Invest 95 (6), 2954-2962 (1995)
   PUBMED   7769138
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883046.1, FM053942.1 and BC081822.1.
            
            On or before Jan 12, 2005 this sequence version replaced
            XP_346598.1, NP_071619.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000818.1, FQ231499.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..147
                     /product="allograft inflammatory factor 1"
                     /note="protein BART-1; balloon angioplasty responsive
                     transcript; ionized calcium binding adapter molecule 1;
                     AIF-1; microglia response factor; balloon
                     angioplasty-responsive transcript 1"
                     /calculated_mol_wt=16696
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P81076; propagated from
                     UniProtKB/Swiss-Prot (P55009.1)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55008; propagated from
                     UniProtKB/Swiss-Prot (P55009.1)"
     Region          38..>113
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55008; propagated from
                     UniProtKB/Swiss-Prot (P55009.1)"
     Region          127..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55009.1)"
     CDS             1..147
                     /gene="Aif1"
                     /gene_synonym="BART-1; Bart1; iba1; mrf-1"
                     /coded_by="NM_017196.3:99..542"
                     /db_xref="GeneID:29427"
                     /db_xref="RGD:61924"
ORIGIN      
        1 msqskdlqgg kafgllkaqq eerldginkh flddpkyssd edlqskleaf ktkymefdln
       61 gngdidimsl krmleklgvp kthlelkkli revssgseet fsysdflrmm lgkrsailrm
      121 ilmyeeknke hqkptgppak kaiselp
//
LOCUS       NP_001020580             482 aa            linear   ROD 25-MAR-2025
DEFINITION  histone deacetylase 1 [Rattus norvegicus].
ACCESSION   NP_001020580 XP_216349
VERSION     NP_001020580.1
DBSOURCE    REFSEQ: accession NM_001025409.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Dunaway,L.S., Cook,A.K., Kellum,C.E., Edell,C., Botta,D.,
            Molina,P.A., Sedaka,R.S., d'Uscio,L.V., Katusic,Z.S., Pollock,D.M.,
            Inscho,E.W. and Pollock,J.S.
  TITLE     Endothelial histone deacetylase 1 activity impairs kidney
            microvascular NO signaling in rats fed a high-salt diet
  JOURNAL   Acta Physiol (Oxf) 240 (9), e14201 (2024)
   PUBMED   39007513
  REMARK    GeneRIF: Endothelial histone deacetylase 1 activity impairs kidney
            microvascular NO signaling in rats fed a high-salt diet.
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Yang,H.T., Wang,G., Zhu,P.C. and Xiao,Z.Y.
  TITLE     Silencing EIF3A ameliorates pulmonary arterial hypertension through
            HDAC1 and PTEN/PI3K/AKT pathway in vitro and in vivo
  JOURNAL   Exp Cell Res 426 (1), 113555 (2023)
   PUBMED   36921705
  REMARK    GeneRIF: Silencing EIF3A ameliorates pulmonary arterial
            hypertension through HDAC1 and PTEN/PI3K/AKT pathway in vitro and
            in vivo.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Chen,Y., Cai,K., Du,Y., Liu,Z. and Gong,Y.
  TITLE     HDAC1 overexpression promoted by METTL3-IGF2BP2 inhibits FGF21
            expression in metabolic syndrome-related liver injury
  JOURNAL   Biochem Cell Biol 101 (1), 52-63 (2023)
   PUBMED   36542845
  REMARK    GeneRIF: HDAC1 overexpression promoted by METTL3-IGF2BP2 inhibits
            FGF21 expression in metabolic syndrome-related liver injury.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Pascoal,T.A., Chamoun,M., Lax,E., Wey,H.Y., Shin,M., Ng,K.P.,
            Kang,M.S., Mathotaarachchi,S., Benedet,A.L., Therriault,J.,
            Lussier,F.Z., Schroeder,F.A., DuBois,J.M., Hightower,B.G.,
            Gilbert,T.M., Zurcher,N.R., Wang,C., Hopewell,R., Chakravarty,M.,
            Savard,M., Thomas,E., Mohaddes,S., Farzin,S., Salaciak,A.,
            Tullo,S., Cuello,A.C., Soucy,J.P., Massarweh,G., Hwang,H.,
            Kobayashi,E., Hyman,B.T., Dickerson,B.C., Guiot,M.C., Szyf,M.,
            Gauthier,S., Hooker,J.M. and Rosa-Neto,P.
  TITLE     [11C]Martinostat PET analysis reveals reduced HDAC I availability
            in Alzheimer's disease
  JOURNAL   Nat Commun 13 (1), 4171 (2022)
   PUBMED   35853847
  REMARK    GeneRIF: [(11)C]Martinostat PET analysis reveals reduced HDAC I
            availability in Alzheimer's disease.
            Erratum:[Nat Commun. 2022 Oct 3;13(1):5833. doi:
            10.1038/s41467-022-33668-0. PMID: 36192402]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Grabowska,A., Sas-Nowosielska,H., Wojtas,B., Holm-Kaczmarek,D.,
            Januszewicz,E., Yushkevich,Y., Czaban,I., Trzaskoma,P.,
            Krawczyk,K., Gielniewski,B., Martin-Gonzalez,A., Filipkowski,R.K.,
            Olszynski,K.H., Bernas,T., Szczepankiewicz,A.A., Sliwinska,M.A.,
            Kanhema,T., Bramham,C.R., Bokota,G., Plewczynski,D.,
            Wilczynski,G.M. and Magalska,A.
  TITLE     Activation-induced chromatin reorganization in neurons depends on
            HDAC1 activity
  JOURNAL   Cell Rep 38 (7), 110352 (2022)
   PUBMED   35172152
  REMARK    GeneRIF: Activation-induced chromatin reorganization in neurons
            depends on HDAC1 activity.
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Cai,R.L., Yan-Neale,Y., Cueto,M.A., Xu,H. and Cohen,D.
  TITLE     HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9,
            two G2/M checkpoint Rad proteins
  JOURNAL   J Biol Chem 275 (36), 27909-27916 (2000)
   PUBMED   10846170
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Fuks,F., Burgers,W.A., Brehm,A., Hughes-Davies,L. and Kouzarides,T.
  TITLE     DNA methyltransferase Dnmt1 associates with histone deacetylase
            activity
  JOURNAL   Nat Genet 24 (1), 88-91 (2000)
   PUBMED   10615135
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Huang,Y., Myers,S.J. and Dingledine,R.
  TITLE     Transcriptional repression by REST: recruitment of Sin3A and
            histone deacetylase to neuronal genes
  JOURNAL   Nat Neurosci 2 (10), 867-872 (1999)
   PUBMED   10491605
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Bartl,S., Taplick,J., Lagger,G., Khier,H., Kuchler,K. and Seiser,C.
  TITLE     Identification of mouse histone deacetylase 1 as a growth
            factor-inducible gene
  JOURNAL   Mol Cell Biol 17 (9), 5033-5043 (1997)
   PUBMED   9271381
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Yang,W.M., Inouye,C., Zeng,Y., Bearss,D. and Seto,E.
  TITLE     Transcriptional repression by YY1 is mediated by interaction with a
            mammalian homolog of the yeast global regulator RPD3
  JOURNAL   Proc Natl Acad Sci U S A 93 (23), 12845-12850 (1996)
   PUBMED   8917507
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097943.1.
            
            On Jul 15, 2005 this sequence version replaced XP_216349.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097943.1, BC107476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..482
                     /product="histone deacetylase 1"
                     /EC_number="3.5.1.98"
                     /note="HD1; protein deacetylase HDAC1; protein
                     decrotonylase HDAC1; protein deacylase HDAC1"
                     /calculated_mol_wt=54962
     Region          4..374
                     /region_name="HDAC1"
                     /note="Histone deacetylase 1 (HDAC1); cd10010"
                     /db_xref="CDD:212534"
     Region          9..321
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            order(140..141,149..150,176,178,264,271,301,303)
                     /site_type="active"
                     /db_xref="CDD:212534"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Region          390..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92769; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     Site            432
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q4QQW4.1)"
     CDS             1..482
                     /gene="Hdac1"
                     /coded_by="NM_001025409.1:19..1467"
                     /db_xref="GeneID:297893"
                     /db_xref="RGD:1309799"
ORIGIN      
        1 maqtqgtkrk vcyyydgdvg nyyygqghpm kphrirmthn lllnyglyrk meiyrphkan
       61 aeemtkyhsd dyikflrsir pdnmseyskq mqrfnvgedc pvfdglfefc qlstggsvas
      121 avklnkqqtd iavnwagglh hakkseasgf cyvndivlai lellkyhqrv lyididihhg
      181 dgveeafytt drvmtvsfhk ygeyfpgtgd lrdigagkgk yyavnyplrd giddesyeai
      241 fkpvmskvme mfqpsavvlq cgsdslsgdr lgcfnltikg hakcvefvks fnlpmlmlgg
      301 ggytirnvar cwtyetaval dteipnelpy ndyfeyfgpd fklhispsnm tnqntneyle
      361 kikqrlfenl rmlphapgvq mqaipedaip eesgdedeed pdkrisicss dkriaceeef
      421 sdsdeegegg rknssnfkka krvktedeke kdpeekkevt eeektkeekp eakgvkeevk
      481 ma
//
LOCUS       NP_038200                 99 aa            linear   ROD 25-MAR-2025
DEFINITION  osteocalcin preproprotein [Rattus norvegicus].
ACCESSION   NP_038200
VERSION     NP_038200.1
DBSOURCE    REFSEQ: accession NM_013414.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Pinheiro,G.V.V.D.S., Sabino-Silva,R., Araujo,M.R., Gomes,S.P.,
            Oliveira,S.W., Aguiar,E.M.G., Cardoso-Sousa,L., Gonzaga,C.C. and
            Claudino,M.
  TITLE     Experimental Acute Sepsis Reduced Number of Osteocalcin
            Immunolabeled Cells in Periodontal Ligament
  JOURNAL   Braz Dent J 31 (2), 143-151 (2020)
   PUBMED   32556013
  REMARK    GeneRIF: acute sepsis induction resulted in reduced number of
            osteocalcin labelled cells in periodontal ligament region.
            Moreover, no significant histological differences were observed in
            the periodontium of rats under acute sepsis
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Sadek,N.B., Gamal,S.M., Aboulhoda,B.E., Rashed,L.A., Shawky,H.M.
            and Gamal El-Din,M.M.
  TITLE     The Potential Role of Undercarboxylated Osteocalcin Upregulation in
            Microvascular Insufficiency in a Rat Model of Diabetic
            Cardiomyopathy
  JOURNAL   J Cardiovasc Pharmacol Ther 25 (1), 86-97 (2020)
   PUBMED   31533469
  REMARK    GeneRIF: The Potential Role of Undercarboxylated Osteocalcin
            Upregulation in Microvascular Insufficiency in a Rat Model of
            Diabetic Cardiomyopathy.
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Qi,S., He,J., Zheng,H., Chen,C. and Lan,S.
  TITLE     Icariin Prevents Diabetes-Induced Bone Loss in Rats by Reducing
            Blood Glucose and Suppressing Bone Turnover
  JOURNAL   Molecules 24 (10), 1871 (2019)
   PUBMED   31096652
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Wu,J.Z., Liu,P.C., Liu,R. and Cai,M.
  TITLE     Icariin Restores Bone Structure and Strength in a Rat Model of
            Chronic High-Dose Alcohol-Induced Osteopenia
  JOURNAL   Cell Physiol Biochem 46 (4), 1727-1736 (2018)
   PUBMED   29698972
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Gao,J., Bai,T., Ren,L., Ding,Y., Zhong,X., Wang,H., Guo,Y., Li,J.,
            Liu,Y. and Zhang,Y.
  TITLE     The PLC/PKC/Ras/MEK/Kv channel pathway is involved in
            uncarboxylated osteocalcin-regulated insulin secretion in rats
  JOURNAL   Peptides 86, 72-79 (2016)
   PUBMED   27746193
  REMARK    GeneRIF: Uncarboxylated osteocalcin potentiates insulin secretion,
            inhibits Kv channels and increases [Ca(2+)]i.
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Thomas,S., Movsowitz,C., Epstein,S., Jowell,P. and Ismail,F.
  TITLE     The response of circulating parameters of bone mineral metabolism
            to ethanol- and EDTA-induced hypocalcemia in the rat
  JOURNAL   Bone Miner 8 (1), 1-6 (1990)
   PUBMED   2106357
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Theofan,G., Haberstroh,L.M. and Price,P.A.
  TITLE     Molecular structure of the rat bone Gla protein gene and
            identification of putative regulatory elements
  JOURNAL   DNA 8 (3), 213-221 (1989)
   PUBMED   2785907
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Lian,J., Stewart,C., Puchacz,E., Mackowiak,S., Shalhoub,V.,
            Collart,D., Zambetti,G. and Stein,G.
  TITLE     Structure of the rat osteocalcin gene and regulation of vitamin
            D-dependent expression
  JOURNAL   Proc Natl Acad Sci U S A 86 (4), 1143-1147 (1989)
   PUBMED   2784002
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Wientroub,S., Price,P.A. and Reddi,A.H.
  TITLE     The dichotomy in the effects of 1,25 dihydroxyvitamin D3 and
            24,25-dihydroxyvitamin D3 on bone gamma-carboxyglutamic
            acid-containing protein in serum and bone in vitamin D-deficient
            rats
  JOURNAL   Calcif Tissue Int 40 (3), 166-172 (1987)
   PUBMED   3105848
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Celeste,A.J., Rosen,V., Buecker,J.L., Kriz,R., Wang,E.A. and
            Wozney,J.M.
  TITLE     Isolation of the human gene for bone gla protein utilizing mouse
            and rat cDNA clones
  JOURNAL   EMBO J 5 (8), 1885-1890 (1986)
   PUBMED   3019668
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M25490.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M11777.1, X04141.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680429, SAMN06680433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..99
                     /product="osteocalcin preproprotein"
                     /note="gamma-carboxyglutamic acid-containing protein; bone
                     Gla-protein; osteocalcin; bone gamma-carboxyglutamate
                     protein 2; bone gamma-carboxyglutamate (gla) protein
                     (osteocalcin); bone gamma-carboxyglutamic acid (Gla)
                     protein (osteocalcin)"
                     /calculated_mol_wt=8551
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2395
     Region          31..95
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     mat_peptide     50..99
                     /product="osteocalcin"
                     /calculated_mol_wt=5588
     Site            58
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:3875856; propagated from
                     UniProtKB/Swiss-Prot (P04640.1)"
     Site            66
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P02818,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P04640.1)"
     Site            70
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P83489,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P04640.1)"
     Site            73
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P83489,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P04640.1)"
     CDS             1..99
                     /gene="Bglap"
                     /gene_synonym="Bglap2; Bgp; Bgpr; Bgpra"
                     /coded_by="NM_013414.1:50..349"
                     /db_xref="GeneID:25295"
                     /db_xref="RGD:2206"
ORIGIN      
        1 mrtlslltll altafclsdl agakpsdses dkafmskqeg skvvnrlrry lnnglgapap
       61 ypdplephre vcelnpncde ladhigfqda ykriygttv
//
LOCUS       NP_075249                295 aa            linear   ROD 25-MAR-2025
DEFINITION  aquaporin-9 [Rattus norvegicus].
ACCESSION   NP_075249
VERSION     NP_075249.1
DBSOURCE    REFSEQ: accession NM_022960.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wu,J., Wang,C. and Ding,H.
  TITLE     LncRNA MALAT1 promotes neuropathic pain progression through the
            miR-154-5p/AQP9 axis in CCI rat models
  JOURNAL   Mol Med Rep 21 (1), 291-303 (2020)
   PUBMED   31746418
  REMARK    GeneRIF: LncRNA MALAT1 promotes neuropathic pain progression
            through the miR1545p/AQP9 axis in CCI rat models.
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Huang,X., Yu,X., Li,H., Han,L. and Yang,X.
  TITLE     Regulation mechanism of aquaporin 9 gene on inflammatory response
            and cardiac function in rats with myocardial infarction through
            extracellular signal-regulated kinase1/2 pathway
  JOURNAL   Heart Vessels 34 (12), 2041-2051 (2019)
   PUBMED   31218464
  REMARK    GeneRIF: the combination of AQP9 gene knock-down and U0126 showed
            no further effect. Silencing AQP9 gene can inhibit the activation
            of ERK1/2 signaling pathway, attenuate the inflammatory response in
            rats with MI, inhibit apoptosis of myocardial cells, and improve
            cardiac function
REFERENCE   3  (residues 1 to 295)
  AUTHORS   de Mello Santos,T., Cavariani,M.M., Pereira,D.N., Schimming,B.C.,
            Chuffa,L.G.A. and Domeniconi,R.F.
  TITLE     Maternal Protein Restriction Modulates Angiogenesis and AQP9
            Expression Leading to a Delay in Postnatal Epididymal Development
            in Rat
  JOURNAL   Cells 8 (9), 1094 (2019)
   PUBMED   31533210
  REMARK    GeneRIF: The maternal low-protein diet decreased AQP9 and VEGFr-2
            expression, decreased epididymal microvascularity and altered the
            morphometric features of the epididymal epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Liu,J.Y., Chen,X.X., Chen,H.Y., Shi,J., Leung,G.P., Tang,S.C.,
            Lao,L.X., Yip,H.K., Lee,K.F., Sze,S.C., Zhang,Z.J. and Zhang,K.Y.
  TITLE     Downregulation of Aquaporin 9 Exacerbates Beta-amyloid-induced
            Neurotoxicity in Alzheimer's Disease Models In vitro and In vivo
  JOURNAL   Neuroscience 394, 72-82 (2018)
   PUBMED   30266683
  REMARK    GeneRIF: Downregulation of aquaporin 9 exacerbates
            beta-amyloid-induced neurotoxicity in Alzheimer's disease models in
            vitro and in vivo.
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Gotfryd,K., Mosca,A.F., Missel,J.W., Truelsen,S.F., Wang,K.,
            Spulber,M., Krabbe,S., Helix-Nielsen,C., Laforenza,U., Soveral,G.,
            Pedersen,P.A. and Gourdon,P.
  TITLE     Human adipose glycerol flux is regulated by a pH gate in AQP10
  JOURNAL   Nat Commun 9 (1), 4749 (2018)
   PUBMED   30420639
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Kuriyama,H., Kawamoto,S., Ishida,N., Ohno,I., Mita,S.,
            Matsuzawa,Y., Matsubara,K. and Okubo,K.
  TITLE     Molecular cloning and expression of a novel human aquaporin from
            adipose tissue with glycerol permeability
  JOURNAL   Biochem Biophys Res Commun 241 (1), 53-58 (1997)
   PUBMED   9405233
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Kuwahara,M., Gu,Y., Ishibashi,K., Marumo,F. and Sasaki,S.
  TITLE     Mercury-sensitive residues and pore site in AQP3 water channel
  JOURNAL   Biochemistry 36 (46), 13973-13978 (1997)
   PUBMED   9369468
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085731.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085731.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..295
                     /product="aquaporin-9"
                     /note="AQP-9; aquaglyceroporin-9; neutral solute channel
                     aquaporin 9"
                     /calculated_mol_wt=31740
     Region          4..266
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            25..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            58..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            order(64,82..84,212..213,216,219)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(84..86,216..218)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     Region          84..86
                     /region_name="NPA 1.
                     /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            99..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            161..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            191..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Region          216..218
                     /region_name="NPA 2.
                     /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56627.1)"
     CDS             1..295
                     /gene="Aqp9"
                     /coded_by="NM_022960.2:464..1351"
                     /db_xref="GeneID:65054"
                     /db_xref="RGD:68433"
ORIGIN      
        1 mpsekdgakk slmqrlalks riaketlsef lgtfimivlg cssiaqavls rerfggiiti
       61 nigfasavvm alyvtfgisg ghinpavsfa mcafgrmewf kfpfyvgaqf lgafvgaatv
      121 fgiyydglma faggkllvvg enatafifat ypapfistpg afvdqvvstm flllivfamf
      181 dsrnlgvprg lepvviglli ivlscslgln sgcamnpard lsprlftala gwgfevftvg
      241 nnfwwipvvg pmigaflggl iyilfiqmhh skldpdmkae psennlekhe lsvim
//
LOCUS       NP_073159                245 aa            linear   ROD 25-MAR-2025
DEFINITION  myelin-oligodendrocyte glycoprotein precursor [Rattus norvegicus].
ACCESSION   NP_073159
VERSION     NP_073159.2
DBSOURCE    REFSEQ: accession NM_022668.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zhang,Z., Wang,J., Song,Z., Wang,Y., Cheng,Z., Guo,Q., Wang,E.,
            Jian,Y. and Wu,L.
  TITLE     Downregulation of microRNA-199a-5p alleviated lidocaine-induced
            sensory dysfunction and spinal cord myelin lesions in a rat model
  JOURNAL   Toxicol Lett 336, 1-10 (2021)
   PUBMED   33166664
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ntountaniotis,D., Vanioti,Mu., Kordopati,G.G., Kellici,T.F.,
            Marousis,K.D., Mavromoustakos,T., Spyroulias,G.A., Golic
            Grdadolnik,S. and Tselios,T.V.
  TITLE     A combined NMR and molecular dynamics simulation study to determine
            the conformational properties of rat/mouse 35-55 myelin
            oligodendrocyte glycoprotein epitope implicated in the induction of
            experimental autoimmune encephalomyelitis
  JOURNAL   J Biomol Struct Dyn 35 (7), 1559-1567 (2017)
   PUBMED   27483998
  REMARK    GeneRIF: The aim of this work was to explore the conformational
            characteristics of rat/mouse MOG35-55 immunodominant epitope. The
            results are discussed in terms of rational design of altered
            peptide ligands or non-peptide mimetics based on rat MOG35-55 that
            could be served as potential inhibitors of experimental autoimmune
            encephalomyelitis.
REFERENCE   3  (residues 1 to 245)
  AUTHORS   von Budingen,H.C., Mei,F., Greenfield,A., Jahn,S., Shen,Y.A.,
            Reid,H.H., McKemy,D.D. and Chan,J.R.
  TITLE     The myelin oligodendrocyte glycoprotein directly binds nerve growth
            factor to modulate central axon circuitry
  JOURNAL   J Cell Biol 210 (6), 891-898 (2015)
   PUBMED   26347141
  REMARK    GeneRIF: Identify nerve growth factor as a binding partner for MOG
            and demonstrate that this interaction is capable of sequestering
            NGF from TrkA-expressing neurons to modulate axon growth and
            survival.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Mony,J.T., Khorooshi,R. and Owens,T.
  TITLE     MOG extracellular domain (p1-125) triggers elevated frequency of
            CXCR3+ CD4+ Th1 cells in the CNS of mice and induces greater
            incidence of severe EAE
  JOURNAL   Mult Scler 20 (10), 1312-1321 (2014)
   PUBMED   24552747
  REMARK    GeneRIF: MOG(1-125) immunization resulted in an increased incidence
            of severe experimental autoimmune encephalomyelitis and was
            accompanied by an increased percentage of CXCR3-expressing CD4+ T
            cells producing IFNgamma in the CNS.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Kitley,J., Waters,P., Woodhall,M., Leite,M.I., Murchison,A.,
            George,J., Kuker,W., Chandratre,S., Vincent,A. and Palace,J.
  TITLE     Neuromyelitis optica spectrum disorders with aquaporin-4 and
            myelin-oligodendrocyte glycoprotein antibodies: a comparative study
  JOURNAL   JAMA Neurol 71 (3), 276-283 (2014)
   PUBMED   24425068
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Salvati,S., Sanchez,M., Campeggi,L.M., Suchanek,G., Breitschop,H.
            and Lassmann,H.
  TITLE     Accelerated myelinogenesis by dietary lipids in rat brain
  JOURNAL   J Neurochem 67 (4), 1744-1750 (1996)
   PUBMED   8858961
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Birling,M.C. and Nussbaum,J.L.
  TITLE     Comparative immunohistochemical study of C1G5F2 antigen and
            myelin/oligodendrocyte glycoprotein (MOG) expression in brain of
            several animal species
  JOURNAL   Neurosci Lett 185 (1), 9-12 (1995)
   PUBMED   7731558
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Pham-Dinh,D., Mattei,M.G., Nussbaum,J.L., Roussel,G.,
            Pontarotti,P., Roeckel,N., Mather,I.H., Artzt,K., Lindahl,K.F. and
            Dautigny,A.
  TITLE     Myelin/oligodendrocyte glycoprotein is a member of a subset of the
            immunoglobulin superfamily encoded within the major
            histocompatibility complex
  JOURNAL   Proc Natl Acad Sci U S A 90 (17), 7990-7994 (1993)
   PUBMED   8367453
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Gardinier,M.V., Amiguet,P., Linington,C. and Matthieu,J.M.
  TITLE     Myelin/oligodendrocyte glycoprotein is a unique member of the
            immunoglobulin superfamily
  JOURNAL   J Neurosci Res 33 (1), 177-187 (1992)
   PUBMED   1453482
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Amiguet,P., Gardinier,M.V., Zanetta,J.P. and Matthieu,J.M.
  TITLE     Purification and partial structural and functional characterization
            of mouse myelin/oligodendrocyte glycoprotein
  JOURNAL   J Neurochem 58 (5), 1676-1682 (1992)
   PUBMED   1373175
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087717.1.
            
            On Oct 13, 2007 this sequence version replaced NP_073159.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087717.1, FQ214199.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..245
                     /product="myelin-oligodendrocyte glycoprotein precursor"
                     /note="dystonia 2, torsion (autosomal recessive)"
                     /calculated_mol_wt=24964
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2883
     mat_peptide     28..245
                     /product="Myelin-oligodendrocyte glycoprotein.
                     /id=PRO_0000014890"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63345.1)"
                     /calculated_mol_wt=24964
     Region          30..142
                     /region_name="IgV_MOG_like"
                     /note="Immunoglobulin (Ig)-like domain of myelin
                     oligodendrocyte glycoprotein (MOG); cd05713"
                     /db_xref="CDD:409378"
     Region          30..53
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409378"
     Region          31..35
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409378"
     Region          38..42
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409378"
     Region          45..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409378"
     Region          54..62
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409378"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63345.1)"
     Site            order(60..61,80,91,128..129,131..132,134..135)
                     /site_type="other"
                     /note="Fab binding site [polypeptide binding]"
                     /db_xref="CDD:409378"
     Region          62..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409378"
     Region          63..67
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          68..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          72..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          81..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          88..128
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          95..100
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409378"
     Region          106..114
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Region          121..129
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409378"
     Region          129..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          131..142
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409378"
     Region          132..142
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409378"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63345.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63345.1)"
     CDS             1..245
                     /gene="Mog"
                     /coded_by="NM_022668.2:89..826"
                     /db_xref="GeneID:24558"
                     /db_xref="RGD:3102"
ORIGIN      
        1 magvwslslp scllslllll qlscsyagqf rvigpghpir alvgdeaelp crispgknat
       61 gmevgwyrsp fsrvvhlyrn gkdqdaeqap eyrgrtellk esigegkval riqnvrfsde
      121 ggytcffrdh syqeeaavel kvedpfywin pgvlalialv pmlllqvsvg lvflflqhrl
      181 rgklraeven lhrtfdphfl rvpcwkitlf vivpvlgplv aliicynwlh rrlagqflee
      241 lrnpf
//
LOCUS       NP_001005560             807 aa            linear   ROD 25-MAR-2025
DEFINITION  85/88 kDa calcium-independent phospholipase A2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001005560 NP_446344 XP_346804
VERSION     NP_001005560.1
DBSOURCE    REFSEQ: accession NM_001005560.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Kuwata,H., Yuzurihara,C., Kinoshita,N., Taki,Y., Ikegami,Y.,
            Washio,S., Hirakawa,Y., Yoda,E., Aiuchi,T., Itabe,H., Nakatani,Y.
            and Hara,S.
  TITLE     The group VIA calcium-independent phospholipase A2 and NFATc4
            pathway mediates IL-1beta-induced expression of chemokines CCL2 and
            CXCL10 in rat fibroblasts
  JOURNAL   FEBS J 285 (11), 2056-2070 (2018)
   PUBMED   29637744
  REMARK    GeneRIF: the transcriptional activation of nuclear factor of
            activated T-cell proteins (NFATs), but not nuclear factor-kappaB,
            by IL-1beta stimulation was markedly attenuated by the iPLA2
            inhibitor bromoenol lactone, and NFATc4 knockdown markedly
            attenuated the IL-1beta-induced expression of both CCL2 and CXCL10.
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Zhou,Z., Wang,Z., Guan,Q., Qiu,F., Li,Y., Liu,Z., Zhang,H., Dong,H.
            and Zhang,Z.
  TITLE     PEDF Inhibits the Activation of NLRP3 Inflammasome in Hypoxia
            Cardiomyocytes through PEDF Receptor/Phospholipase A2
  JOURNAL   Int J Mol Sci 17 (12), 2064 (2016)
   PUBMED   27973457
  REMARK    GeneRIF: PEDF can protect against hypoxia-induced activation of the
            NLRP3 inflammasome by inhibiting mitochondrial fission though
            PEDFR/iPLA2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Caporarello,N., Salmeri,M., Scalia,M., Motta,C., Parrino,C.,
            Frittitta,L., Olivieri,M., Toscano,M.A., Anfuso,C.D. and Lupo,G.
  TITLE     Role of cytosolic and calcium independent phospholipases A(2) in
            insulin secretion impairment of INS-1E cells infected by S. aureus
  JOURNAL   FEBS Lett 589 (24 Pt B), 3969-3976 (2015)
   PUBMED   26632509
  REMARK    GeneRIF: Data suggest glucose-induced insulin secretion is first
            up-regulated (acute infection), then down-regulated (chronic
            infection) in beta cells infected with S. aureus; Pla2g4a is
            up-regulated in acute infection; Pla2g6 is up-regulated in chronic
            infection.
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Rauckhorst,A.J., Pfeiffer,D.R. and Broekemeier,K.M.
  TITLE     The iPLA(2)gamma is identified as the membrane potential sensitive
            phospholipase in liver mitochondria
  JOURNAL   FEBS Lett 589 (18), 2367-2371 (2015)
   PUBMED   26206229
  REMARK    GeneRIF: membrane potential sensitive activity is the iPLA2gamma
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Takatani-Nakase,T. and Takahashi,K.
  TITLE     Leptin suppresses non-apoptotic cell death in ischemic rat
            cardiomyocytes by reduction of iPLA(2) activity
  JOURNAL   Biochem Biophys Res Commun 463 (1-2), 13-17 (2015)
   PUBMED   25979360
  REMARK    GeneRIF: Leptin was shown to significantly inhibit the activity of
            iPLA2, which is considered to play crucial roles in non-apoptotic
            cell death, resulting in effective prevention of ischemia-induced
            myocyte death.
REFERENCE   6  (residues 1 to 807)
  AUTHORS   Jenkins,C.M., Han,X., Mancuso,D.J. and Gross,R.W.
  TITLE     Identification of calcium-independent phospholipase A2 (iPLA2)
            beta, and not iPLA2gamma, as the mediator of arginine
            vasopressin-induced arachidonic acid release in A-10 smooth muscle
            cells. Enantioselective mechanism-based discrimination of mammalian
            iPLA2s
  JOURNAL   J Biol Chem 277 (36), 32807-32814 (2002)
   PUBMED   12089145
  REMARK    GeneRIF: The agonist-stimulated release of arachidonic acid (AA)
            from cellular phospholipids in many cell types (e.g. myocytes,
            beta-cells, and neurons) has been demonstrated to be primarily
            mediated by calcium-independent phospholipases A(2) (iPLA(2)s).
REFERENCE   7  (residues 1 to 807)
  AUTHORS   Seegers,H.C., Gross,R.W. and Boyle,W.A.
  TITLE     Calcium-independent phospholipase A(2)-derived arachidonic acid is
            essential for endothelium-dependent relaxation by acetylcholine
  JOURNAL   J Pharmacol Exp Ther 302 (3), 918-923 (2002)
   PUBMED   12183647
REFERENCE   8  (residues 1 to 807)
  AUTHORS   Bloch-Shilderman,E., Abu-Raya,S., Trembovler,V., Boschwitz,H.,
            Gruzman,A., Linial,M. and Lazarovici,P.
  TITLE     Pardaxin stimulation of phospholipases A2 and their involvement in
            exocytosis in PC-12 cells
  JOURNAL   J Pharmacol Exp Ther 301 (3), 953-962 (2002)
   PUBMED   12023524
REFERENCE   9  (residues 1 to 807)
  AUTHORS   Ma,Z., Ramanadham,S., Wohltmann,M., Bohrer,A., Hsu,F.F. and Turk,J.
  TITLE     Studies of insulin secretory responses and of arachidonic acid
            incorporation into phospholipids of stably transfected insulinoma
            cells that overexpress group VIA phospholipase A2 (iPLA2beta)
            indicate a signaling rather than a housekeeping role for iPLA2beta
  JOURNAL   J Biol Chem 276 (16), 13198-13208 (2001)
   PUBMED   11278673
REFERENCE   10 (residues 1 to 807)
  AUTHORS   Ma,Z., Ramanadham,S., Kempe,K., Chi,X.S., Ladenson,J. and Turk,J.
  TITLE     Pancreatic islets express a Ca2+-independent phospholipase A2
            enzyme that contains a repeated structural motif homologous to the
            integral membrane protein binding domain of ankyrin
  JOURNAL   J Biol Chem 272 (17), 11118-11127 (1997)
   PUBMED   9111008
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC081916.1.
            
            On or before Oct 14, 2004 this sequence version replaced
            NP_446344.1, XP_346804.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081916.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..807
                     /product="85/88 kDa calcium-independent phospholipase A2
                     isoform 1"
                     /EC_number="3.1.1.5"
                     /EC_number="3.1.1.4"
                     /EC_number="3.1.2.2"
                     /note="85 kDa calcium-independent phospholipase A2;
                     patatin-like phospholipase domain-containing protein 9;
                     intracellular membrane-associated calcium-independent
                     phospholipase A2 beta; 85/88 kDa calcium-independent
                     phospholipase A2; phospholipase A2, group VI (cytosolic,
                     calcium-independent); palmitoyl-CoA hydrolase;
                     2-lysophosphatidylcholine acylhydrolase"
                     /calculated_mol_wt=89425
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97570.2)"
     Region          102..407
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          119..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          120..147
                     /region_name="ANK 1.
                     /evidence=ECO:0000250|UniProtKB:A0A3L7I2I8"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Site            order(151,153,157..158,161..163,165..166,170,173,183,185,
                     187,191..192,195..197,199..200,204,207,217,219,221,
                     225..226,229..231,233..234,238,241)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          151..183
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..181
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          185..217
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          185..215
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          219..248
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          219..248
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          251..281
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Site            order(286,288,292..293,295,297..298,302,305,314,316,318,
                     322..323,326..328,330..331,335,338,347,349,351,355..356,
                     359..361,363..364,368,371,380)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          286..314
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          286..312
                     /region_name="ANK 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          316..347
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          316..345
                     /region_name="ANK 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          349..380
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          349..378
                     /region_name="ANK 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          382..403
                     /region_name="ANK 9.
                     /evidence=ECO:0000250|UniProtKB:A0A3L7I2I8"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          481..794
                     /region_name="Pat_PNPLA9"
                     /note="Patatin-like phospholipase domain containing
                     protein 9; cd07212"
                     /db_xref="CDD:132851"
     Site            481..501
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          486..491
                     /region_name="GXGXXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Site            order(487..488,490,520,653)
                     /site_type="active"
                     /db_xref="CDD:132851"
     Site            512..532
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          518..522
                     /region_name="GXSXG.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Site            518..522
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132851"
     Region          653..655
                     /region_name="DGA/G.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01161"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          678..687
                     /region_name="Calmodulin-binding (1-9-14 motif).
                     /evidence=ECO:0000269|PubMed:11118454"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     Region          749..760
                     /region_name="Calmodulin-binding (IQ motif).
                     /evidence=ECO:0000269|PubMed:11118454"
                     /note="propagated from UniProtKB/Swiss-Prot (P97570.2)"
     CDS             1..807
                     /gene="Pla2g6"
                     /gene_synonym="caI-PLA2; GVI PLA2; iPla2; iPLA2-beta;
                     PNPLA9"
                     /coded_by="NM_001005560.1:94..2517"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360426"
                     /db_xref="RGD:628867"
ORIGIN      
        1 mqffgrlvnt lssvtnlfsn pfrvkevsla dyasservre egqlillqna snrtwdcvlv
       61 sprnpqsgfr lfqleseada lvnfqqyssq lppfyessvq vlhvevlqhl tdlirnhpsw
      121 tvthlavelg irecfhhsri iscanstene egctplhlac rkgdseilve lvqychaqmd
      181 vtdnkgetaf hyavqgdnpq vlqllgknas aglnqvnnqg ltplhlacqm gkqemvrvll
      241 lcnarcnimg pggfpihtam kfsqkgcaem iismdsnqih skdprygasp lhwaknaema
      301 rmllkrgcdv dstsasgnta lhvavtrnrf dcvmvlltyg anagargehg ntplhlamsk
      361 dnmemvkali vfgaevdtpn dfgetpafia skisklitrk alltllktvg adyhfpfiqg
      421 vsteqssaag phpffsldrt qpptislnnl elqdlmpvsr arkpafilss mrdekrshdh
      481 llcldgggvk glviiqllia iekasgvatk dlfdwvagts tggilalail hsksmaymrg
      541 vyfrmkdevf rgsrpyesgp leeflkrefg ehtkmtdvkk pkvmltgtls drqpaelhlf
      601 rnydapeavr eprctpninl kpptqpadql vwraarssga aptyfrpngr fldggllann
      661 ptldamteih eynqdmirkg qgnkvkklsi vvslgtgksp qvpvtcvdvf rpsnpwelak
      721 tvfgakelgk mvvdcctdpd gravdraraw cemvgiqyfr lnpqlgsdim ldevsdavlv
      781 nalwetevyi yehreefqkl vqlllsp
//
LOCUS       NP_598235                752 aa            linear   ROD 25-MAR-2025
DEFINITION  cytosolic phospholipase A2 [Rattus norvegicus].
ACCESSION   NP_598235
VERSION     NP_598235.2
DBSOURCE    REFSEQ: accession NM_133551.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Yao,H.H., Min,Y.J., Hong,D.Y., Wang,L., Lu,X.Y. and Yang,Y.H.
  TITLE     [Electroacupuncture improves limb motor function by down-regulating
            cytosolic phospholi-pase A2 and reducing apoptosis of nerve cells
            in rats with spinal cord injury]
  JOURNAL   Zhen Ci Yan Jiu 48 (8), 782-790 (2023)
   PUBMED   37614136
  REMARK    GeneRIF: [Electroacupuncture improves limb motor function by
            down-regulating cytosolic phospholi-pase A2 and reducing apoptosis
            of nerve cells in rats with spinal cord injury].
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Bera,A., Srivastava,A., Dubey,V., Dixit,A.B., Tripathi,M.,
            Sharma,M.C., Lalwani,S., Chandra,P.S. and Banerjee,J.
  TITLE     Altered hippocampal expression and function of cytosolic
            phospholipase A2 (cPLA2) in temporal lobe epilepsy (TLE)
  JOURNAL   Neurol Res 44 (8), 748-753 (2022)
   PUBMED   35285418
  REMARK    GeneRIF: Altered hippocampal expression and function of cytosolic
            phospholipase A2 (cPLA2) in temporal lobe epilepsy (TLE).
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Santerre-Anderson,J.L. and Werner,D.F.
  TITLE     Ethanol Stimulation of Microglia Release Increases ERK1/2-Dependent
            Neuronal cPLA2 Activity in Immature Cultured Cortical Preparations
  JOURNAL   Neurochem Res 45 (7), 1592-1601 (2020)
   PUBMED   32274627
  REMARK    GeneRIF: Ethanol Stimulation of Microglia Release Increases
            ERK1/2-Dependent Neuronal cPLA2 Activity in Immature Cultured
            Cortical Preparations.
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Rajagopal,S., Fitzgerald,A.A., Deep,S.N., Paul,S. and Poddar,R.
  TITLE     Role of GluN2A NMDA receptor in homocysteine-induced prostaglandin
            E2 release from neurons
  JOURNAL   J Neurochem 150 (1), 44-55 (2019)
   PUBMED   31125437
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Villamil-Ortiz,J.G. and Cardona-Gomez,G.P.
  TITLE     cPLA2 and desaturases underlie the tau hyperphosphorylation offset
            induced by BACE knock-down in neuronal primary cultures
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1864 (11), 3696-3707 (2018)
   PUBMED   30251689
  REMARK    GeneRIF: Study utilizing glutamate excitotoxicity model in rat
            cortical primary cell cultures suggests for the first time a more
            direct action of BACE1 on the hyperphosphorylation state of tau
            (implemented in Alzheimer's disease pathogenesis) that is mediated
            through cPLA2 and desaturases SCD1 and FADS6 modulation during
            glutamate excitotoxicity.
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Xia,P., Kramer,R.M. and King,G.L.
  TITLE     Identification of the mechanism for the inhibition of
            Na+,K(+)-adenosine triphosphatase by hyperglycemia involving
            activation of protein kinase C and cytosolic phospholipase A2
  JOURNAL   J Clin Invest 96 (2), 733-740 (1995)
   PUBMED   7635966
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Hanel,A.M. and Gelb,M.H.
  TITLE     Multiple enzymatic activities of the human cytosolic 85-kDa
            phospholipase A2: hydrolytic reactions and acyl transfer to
            glycerol
  JOURNAL   Biochemistry 34 (24), 7807-7818 (1995)
   PUBMED   7794891
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Owada,Y., Tominaga,T., Yoshimoto,T. and Kondo,H.
  TITLE     Molecular cloning of rat cDNA for cytosolic phospholipase A2 and
            the increased gene expression in the dentate gyrus following
            transient forebrain ischemia
  JOURNAL   Brain Res Mol Brain Res 25 (3-4), 364-368 (1994)
   PUBMED   7808237
  REMARK    Erratum:[Brain Res Mol Brain Res. 1994 Dec;27(2):355. doi:
            10.1016/0169-328x(94)90023-x. PMID: 7898324]
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Kitayama,S., Shimada,S. and Uhl,G.R.
  TITLE     Parkinsonism-inducing neurotoxin MPP+: uptake and toxicity in
            nonneuronal COS cells expressing dopamine transporter cDNA
  JOURNAL   Ann Neurol 32 (1), 109-111 (1992)
   PUBMED   1642464
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Tovey,J.A., Sundar,A.S., Ikram,S., Smith,S. and Penny,W.J.
  TITLE     Human cardiac muscle magnesium and potassium concentrations: can
            skeletal muscle, mononuclear blood cells, erythrocyte and plasma
            concentrations provide a surrogate measure?
  JOURNAL   Ann Clin Biochem 29 (Pt 4), 461-462 (1992)
   PUBMED   1642455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070940.1.
            
            On Mar 8, 2007 this sequence version replaced NP_598235.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070940.1, U38376.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..752
                     /product="cytosolic phospholipase A2"
                     /EC_number="3.1.1.5"
                     /EC_number="3.1.1.4"
                     /note="phospholipase A2 cytosolic; phospholipase A2, group
                     IVA (cytosolic, calcium-dependent); cytosolic
                     phospholipase A2-like; phospholipase A2 group IVA"
                     /calculated_mol_wt=85518
     Region          1..178
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P50393.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47712; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Region          20..138
                     /region_name="C2_cPLA2"
                     /note="C2 domain present in cytosolic PhosphoLipase A2
                     (cPLA2); cd04036"
                     /db_xref="CDD:176001"
     Site            order(40,43,65,93,95)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176001"
     Region          144..730
                     /region_name="cPLA2_Grp-IVA"
                     /note="Group IVA cytosolic phospholipase A2; catalytic
                     domain; Ca-dependent; cd07200"
                     /db_xref="CDD:132839"
     Site            order(197..198,200,228,549)
                     /site_type="active"
                     /db_xref="CDD:132839"
     Site            226..230
                     /site_type="other"
                     /note="nucleophile elbow"
                     /db_xref="CDD:132839"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47712; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            order(403,486)
                     /site_type="other"
                     /note="flexible lid region"
                     /db_xref="CDD:132839"
     Region          427..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50393.1)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47712; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:P47712; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47712; propagated from
                     UniProtKB/Swiss-Prot (P50393.1)"
     CDS             1..752
                     /gene="Pla2g4a"
                     /gene_synonym="cPLA2; Pla2c; Pla2g4"
                     /coded_by="NM_133551.2:172..2430"
                     /db_xref="GeneID:24653"
                     /db_xref="RGD:67366"
ORIGIN      
        1 msfidpyqhi ivehqyshkf tvvvlratkv tkgtfgdmld tpdpyvelfi sttpdsrkrt
       61 rhfnndinpv wnetfefild pnqenvleit lmdanyvmde tlgtatfpvs smkvgekkev
      121 pfifnqvtem ilemslevcs cpdlrfsmal cdqektfrqq rkenikenmk kllgpkkseg
      181 lystrdvpvv ailgsgggfr amvgfsgvmk alyesgildc atyvaglsgs twymstlysh
      241 pdfpekgpee ineelmknvs hnplllltpq kvkryveslw kkkssgqpvt ftdifgmlig
      301 etliqnrmst tlsslkekvs aarcplplft clhvkpdvse lmfadwvefs pyeigmakyg
      361 tfmtpdlfgs kffmgtvvkk yeenplhflm gvwgsafsil fnrvlgvsgs qnkgstmeee
      421 lenitakhiv sndssdsdde aqgpkgtene daereyqndn qaswvhrmlm alvsdsalfn
      481 tregragkvh nfmlglnlnt syplsplrdf spqdsfddde ldaavadpde feriyepldv
      541 kskkihvvds gltfnlpypl ilrpqrgvdl iisfdfsarp sdtsppfkel llaekwakmn
      601 klpfpkidpy vfdreglkec yvfkpknpdv ekdcptiihf vlaninfrky kapgvlretk
      661 eekeiadfdi fddpespfst fnfqypnqaf krlhdlmyfn tlnnidvikd aivesieyrr
      721 qnpsrcsvsl snvearkffn keflskptae si
//
LOCUS       NP_001423995             664 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001423995 XP_063133691
VERSION     NP_001423995.1
DBSOURCE    REFSEQ: accession NM_001437066.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133691.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.526075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..664
                     /product="transcription factor 4 isoform 4"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=70793
     Region          81..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          555..639
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(563,567,569..571,573,578,599..600)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(576..577,580..581,583..584,587,591,601,604,608,611,
                     614..619)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..664
                     /gene="Tcf4"
                     /coded_by="NM_001437066.1:184..2178"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsgtavws
      361 rnggqasssp nyegplhslq sriedrlerl ddaihvlrnh avgpstavpg ghgdmhgiig
      421 pshngamgsl gsgygtglls anrhslmvga hredgvalrg shsllpnqvp vpqlpvqsat
      481 spdlnppqdp yrgmppglqg qsvssgssei ksddegdenl qdtkssedkk ldddkkdiks
      541 itsnnddedl tpeqkaerek errmannare rlrvrdinea fkelgrmvql hlksdkpqtk
      601 llilhqavav ilsleqqvre rnlnpkaacl krreeekvss eppplslagp hpgmgdaanh
      661 mgqm
//
LOCUS       NP_001424013            1107 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 10 [Rattus norvegicus].
ACCESSION   NP_001424013 XP_063144121
VERSION     NP_001424013.1
DBSOURCE    REFSEQ: accession NM_001437084.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1107)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1107)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1107)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1107)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1107)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1107)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1107)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1107)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1107)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1107)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144121.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16354.1,
                                           SRR26643292.23340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1107
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1107
                     /product="pumilio homolog 1 isoform 10"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=118216
     Region          764..1085
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(820..821,824,856..857,860,893,896,928..929,932,
                     961..962,964..965,968,997..998,1000..1001,1004,1040..1041,
                     1043..1044,1047,1077,1080)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1107
                     /gene="Pum1"
                     /coded_by="NM_001437084.1:114..3437"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigla
      421 paafvpnpyi isaappgtdp ytaglaaaat lgpavvphqy ygvtpwgvyp aslfqqqaaa
      481 aaaatnsatq qsapqaqqgq qqvlrggasq rpltpnqnqq gqqtdplvaa aavnsalafg
      541 qglaagmpgy pvlapaayyd qtgalvvnag arnglgapvr lvapapviis ssaaqaavaa
      601 aaasangaag glagttngpf rplgtqqpqp qpqqqpsnnl asssfygnns lssnsqsssl
      661 fsqgsaqpan tslgfgssss lgatlgsalg gfgtaggltn gsgryisaap gaeakyrsas
      721 sasslfspss tlfsssrlry gmsdvmpsgr srlledfrnn rypnlqlrei aghimefsqd
      781 qhgsrfiqlk lerataaerq lvfneilqaa yqlmvdvfgn yviqkffefg sheqklalae
      841 rirghvlsla lqmygcrviq kalefipsdq qnemvreldg hvlkcvkdqn gnhvvqkcie
      901 cvqpqslqfi idafkgqvfa lsthpygcrv iqrilehclp dqtlpileel hqhteqlvqd
      961 qygnyviqhv lehgrpedks kivaeirgnv lvlsqhkfas nvvekcvtha srteravlid
     1021 evctmndgph salytmmkdq yanyvvqkmi dvaepgqrki vmhkirphia tlrkytygkh
     1081 ilaklekyym kngvdlgpic gppngii
//
LOCUS       NP_001424028             669 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 21 [Rattus norvegicus].
ACCESSION   NP_001424028 XP_038953085
VERSION     NP_001424028.1
DBSOURCE    REFSEQ: accession NM_001437099.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953085.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.63244.1,
                                           SRR26643298.74595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..669
                     /product="transcription factor 4 isoform 21"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=71350
     Region          135..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          560..644
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(568,572,574..576,578,583,604..605)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(581..582,585..586,588..589,592,596,606,609,613,616,
                     619..624)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..669
                     /gene="Tcf4"
                     /coded_by="NM_001437099.1:299..2308"
                     /note="isoform 21 is encoded by transcript variant 23"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw
      361 srnggqasss pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii
      421 gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa
      481 tspdlnppqd pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik
      541 sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr dineafkelg rmvqlhlksd
      601 kpqtkllilh qavavilsle qqvrernlnp kaaclkrree ekvssepppl slagphpgmg
      661 daanhmgqm
//
LOCUS       NP_001424029             645 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 22 [Rattus norvegicus].
ACCESSION   NP_001424029 XP_038953097
VERSION     NP_001424029.1
DBSOURCE    REFSEQ: accession NM_001437100.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 645)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 645)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 645)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 645)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953097.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74593.1,
                                           SRR26643299.63243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..645
                     /product="transcription factor 4 isoform 22"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68653
     Region          111..>272
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          536..620
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(544,548,550..552,554,559,580..581)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(557..558,561..562,564..565,568,572,582,585,589,592,
                     595..600)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..645
                     /gene="Tcf4"
                     /coded_by="NM_001437100.1:560..2497"
                     /note="isoform 22 is encoded by transcript variant 24"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqqs llggdmdmgn pgtlsptkpg
      121 sqyypyssnn arrrplhsst mevqtkkvrk vppglpssvy apsastadyn rdspgysssk
      181 paastfsssf fmqdghhssd pwssssgmnq pgyggmlgns hipqsssycs lhpherlsyp
      241 shssadinss lppmstfhrs gtnhystssc tppangtdsi manrgtgaag ssqtgdalgk
      301 alasiyspdh tnnsfssnps tpvgsppsls agtavwsrng gqassspnye gplhslqsri
      361 edrlerldda ihvlrnhavg pstavpgghg dmhgiigpsh ngamgslgsg ygtgllsanr
      421 hslmvgahre dgvalrgshs llpnqvpvpq lpvqsatspd lnppqdpyrg mppglqgqsv
      481 ssgsseiksd degdenlqdt kssedkkldd dkkdiksitr srssnndded ltpeqkaere
      541 kerrmannar erlrvrdine afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr
      601 ernlnpkaac lkrreeekvs seppplslag phpgmgdaan hmgqm
//
LOCUS       NP_001423957             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423957
VERSION     NP_001423957.1
DBSOURCE    REFSEQ: accession NM_001437028.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1661953.1,
                                           SRR26360176.2016860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437028.1:364..1929"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424030             645 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 22 [Rattus norvegicus].
ACCESSION   NP_001424030 XP_063133692
VERSION     NP_001424030.1
DBSOURCE    REFSEQ: accession NM_001437101.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 645)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 645)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 645)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 645)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133692.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.60182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..645
                     /product="transcription factor 4 isoform 22"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68653
     Region          111..>272
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          536..620
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(544,548,550..552,554,559,580..581)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(557..558,561..562,564..565,568,572,582,585,589,592,
                     595..600)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..645
                     /gene="Tcf4"
                     /coded_by="NM_001437101.1:279..2216"
                     /note="isoform 22 is encoded by transcript variant 25"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqqs llggdmdmgn pgtlsptkpg
      121 sqyypyssnn arrrplhsst mevqtkkvrk vppglpssvy apsastadyn rdspgysssk
      181 paastfsssf fmqdghhssd pwssssgmnq pgyggmlgns hipqsssycs lhpherlsyp
      241 shssadinss lppmstfhrs gtnhystssc tppangtdsi manrgtgaag ssqtgdalgk
      301 alasiyspdh tnnsfssnps tpvgsppsls agtavwsrng gqassspnye gplhslqsri
      361 edrlerldda ihvlrnhavg pstavpgghg dmhgiigpsh ngamgslgsg ygtgllsanr
      421 hslmvgahre dgvalrgshs llpnqvpvpq lpvqsatspd lnppqdpyrg mppglqgqsv
      481 ssgsseiksd degdenlqdt kssedkkldd dkkdiksitr srssnndded ltpeqkaere
      541 kerrmannar erlrvrdine afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr
      601 ernlnpkaac lkrreeekvs seppplslag phpgmgdaan hmgqm
//
LOCUS       NP_001423950             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423950 XP_006252680
VERSION     NP_001423950.1
DBSOURCE    REFSEQ: accession NM_001437021.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252680.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.70558.1,
                                           SRR26643290.47341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437021.1:85..1650"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424023            1090 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 15 [Rattus norvegicus].
ACCESSION   NP_001424023 XP_038966296
VERSION     NP_001424023.1
DBSOURCE    REFSEQ: accession NM_001437094.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1090)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1090)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1090)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1090)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1090)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1090)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1090)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1090)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1090)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1090)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038966296.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2371232.1,
                                           SRR26360172.2209461.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1090
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1090
                     /product="pumilio homolog 1 isoform 15"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=115750
     Region          747..1068
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(803..804,807,839..840,843,876,879,911..912,915,
                     944..945,947..948,951,980..981,983..984,987,1023..1024,
                     1026..1027,1030,1060,1063)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1090
                     /gene="Pum1"
                     /coded_by="NM_001437094.1:114..3386"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgegprdad sdendkgekk nkgafdgdkl gdlkeegdvm
      181 dktnglpvqn gidadvkdfs rtpgncqssa nevdllgpnq ngseglaqlt stngakpved
      241 fsnmesqsvp ldpmehvgme plqfdysgtq vpvdsaaatv glfdynsqqq lfqrpnalav
      301 qqltaaqqqq yalaaahqph iglapaafvp npyiisaapp gtdpytagla aaatlgpavv
      361 phqyygvtpw gvypaslfqq qaaaaaaatn satqqsapqa qqgqqqvlrg gasqrpltpn
      421 qnqqgqqtdp lvaaaavnsa lafgqglaag mpgypvlapa ayydqtgalv vnagarnglg
      481 apvrlvapap viisssaaqa avaaaaasan gaagglagtt ngpfrplgtq qpqpqpqqqp
      541 snnlasssfy gnnslssnsq ssslfsqgsa qpantslgfg sssslgatlg salggfgtav
      601 ansntgsgsr rdsltgssdl ykrtssslap ighsfynsls fssspgpvgm plpsqgpghs
      661 qtpppslssh gsssslnlgg ltngsgryis aapgaeakyr sassasslfs psstlfsssr
      721 lrygmsdvmp sgrsrlledf rnnrypnlql reiaghimef sqdqhgsrfi qlklerataa
      781 erqlvfneil qaayqlmvdv fgnyviqkff efgsheqkla laerirghvl slalqmygcr
      841 viqkalefip sdqqnemvre ldghvlkcvk dqngnhvvqk ciecvqpqsl qfiidafkgq
      901 vfalsthpyg crviqrileh clpdqtlpil eelhqhteql vqdqygnyvi qhvlehgrpe
      961 dkskivaeir gnvlvlsqhk fasnvvekcv thasrterav lidevctmnd gphsalytmm
     1021 kdqyanyvvq kmidvaepgq rkivmhkirp hiatlrkyty gkhilaklek yymkngvdlg
     1081 picgppngii
//
LOCUS       NP_001424005            1187 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424005 XP_063144100
VERSION     NP_001424005.1
DBSOURCE    REFSEQ: accession NM_001437076.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1187)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1187)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1187)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1187)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1187)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1187)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1187)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1187)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1187)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1187)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144100.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.14440.1,
                                           SRR26643285.20653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1187
                     /product="pumilio homolog 1 isoform 5"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126230
     Region          844..1165
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(900..901,904,936..937,940,973,976,1008..1009,1012,
                     1041..1042,1044..1045,1048,1077..1078,1080..1081,1084,
                     1120..1121,1123..1124,1127,1157,1160)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1187
                     /gene="Pum1"
                     /coded_by="NM_001437076.1:114..3677"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphiagl
      421 apaafvpnpy iisaappgtd pytaglaaaa tlgpavvphq yygvtpwgvy paslfqqqaa
      481 aaaaatnsat qqsapqaqqg qqqvlrggas qrpltpnqnq qgqqtdplva aaavnsalaf
      541 gqglaagmpg ypvlapaayy dqtgalvvna garnglgapv rlvapapvii sssaaqaava
      601 aaaasangaa gglagttngp frplgtqqpq pqpqqqpsnn lasssfygnn slssnsqsss
      661 lfsqgsaqpa ntslgfgsss slgatlgsal ggfgtavans ntgsgsrrds ltgssdlykr
      721 tssslapigh sfynslsfss spgpvgmplp sqgpghsqtp ppslsshgss sslnlggltn
      781 gsgryisaap gaeakyrsas sasslfspss tlfsssrlry gmsdvmpsgr srlledfrnn
      841 rypnlqlrei aghimefsqd qhgsrfiqlk lerataaerq lvfneilqaa yqlmvdvfgn
      901 yviqkffefg sheqklalae rirghvlsla lqmygcrviq kalefipsdq qnemvreldg
      961 hvlkcvkdqn gnhvvqkcie cvqpqslqfi idafkgqvfa lsthpygcrv iqrilehclp
     1021 dqtlpileel hqhteqlvqd qygnyviqhv lehgrpedks kivaeirgnv lvlsqhkfas
     1081 nvvekcvtha srteravlid evctmndgph salytmmkdq yanyvvqkmi dvaepgqrki
     1141 vmhkirphia tlrkytygkh ilaklekyym kngvdlgpic gppngii
//
LOCUS       NP_075579                989 aa            linear   ROD 26-MAR-2025
DEFINITION  gamma-aminobutyric acid receptor subunit epsilon precursor [Rattus
            norvegicus].
ACCESSION   NP_075579
VERSION     NP_075579.1
DBSOURCE    REFSEQ: accession NM_023091.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Hengen,K.B., Nelson,N.R., Stang,K.M., Johnson,S.M., Smith,S.M.,
            Watters,J.J., Mitchell,G.S. and Behan,M.
  TITLE     Daily isoflurane exposure increases barbiturate insensitivity in
            medullary respiratory and cortical neurons via expression of
            epsilon-subunit containing GABA ARs
  JOURNAL   PLoS One 10 (3), e0119351 (2015)
   PUBMED   25748028
  REMARK    GeneRIF: Daily isoflurane exposure increases barbiturate
            insensitivity in medullary respiratory and cortical neurons via
            expression of epsilon-subunit containing GABA ARs.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Hengen,K.B., Nelson,N.R., Stang,K.M., Johnson,S.M., Crader,S.M.,
            Watters,J.J., Mitchell,G.S. and Behan,M.
  TITLE     Increased GABA(A) receptor epsilon-subunit expression on ventral
            respiratory column neurons protects breathing during pregnancy
  JOURNAL   PLoS One 7 (1), e30608 (2012)
   PUBMED   22303446
  REMARK    GeneRIF: Increased epsilon subunit expression may be critical to
            preserve respiratory function (and life) despite increased
            neurosteroid levels during pregnancy.
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Belujon,P., Baufreton,J., Grandoso,L., Boue-Grabot,E., Batten,T.F.,
            Ugedo,L., Garret,M. and Taupignon,A.I.
  TITLE     Inhibitory transmission in locus coeruleus neurons expressing GABAA
            receptor epsilon subunit has a number of unique properties
  JOURNAL   J Neurophysiol 102 (4), 2312-2325 (2009)
   PUBMED   19625540
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Pape,J.R., Bertrand,S.S., Lafon,P., Odessa,M.F., Chaigniau,M.,
            Stiles,J.K. and Garret,M.
  TITLE     Expression of GABA(A) receptor alpha3-, theta-, and epsilon-subunit
            mRNAs during rat CNS development and immunolocalization of the
            epsilon subunit in developing postnatal spinal cord
  JOURNAL   Neuroscience 160 (1), 85-96 (2009)
   PUBMED   19249336
  REMARK    GeneRIF: Our findings suggest that various combinations of GABA(A)
            alpha3-, theta- and epsilon-subunits may be assembled at a regional
            and developmental level in the brain.
REFERENCE   5  (residues 1 to 989)
  AUTHORS   Sergeeva,O.A., Andreeva,N., Garret,M., Scherer,A. and Haas,H.L.
  TITLE     Pharmacological properties of GABAA receptors in rat hypothalamic
            neurons expressing the epsilon-subunit
  JOURNAL   J Neurosci 25 (1), 88-95 (2005)
   PUBMED   15634770
  REMARK    GeneRIF: We addressed the localization of the GABAA receptor
            epsilon subunit protein in two identified hypothalamic neuron
            groups, tuberomamillary and orexinergic, and the related functional
            properties.
REFERENCE   6  (residues 1 to 989)
  AUTHORS   Moragues,N., Ciofi,P., Lafon,P., Tramu,G. and Garret,M.
  TITLE     GABAA receptor epsilon subunit expression in identified peptidergic
            neurons of the rat hypothalamus
  JOURNAL   Brain Res 967 (1-2), 285-289 (2003)
   PUBMED   12650990
  REMARK    GeneRIF: Expression of GABA-A receptors containing the epsilon
            subunit in neurons of the rat hypothalamus suggests that these
            receptors are likely to be involved in the GABAergic control of
            these neurons.
REFERENCE   7  (residues 1 to 989)
  AUTHORS   Kasparov,S., Davies,K.A., Patel,U.A., Boscan,P., Garret,M. and
            Paton,J.F.
  TITLE     GABA(A) receptor epsilon-subunit may confer benzodiazepine
            insensitivity to the caudal aspect of the nucleus tractus solitarii
            of the rat
  JOURNAL   J Physiol 536 (Pt 3), 785-796 (2001)
   PUBMED   11691872
REFERENCE   8  (residues 1 to 989)
  AUTHORS   Moragues,N., Ciofi,P., Lafon,P., Odessa,M.F., Tramu,G. and
            Garret,M.
  TITLE     cDNA cloning and expression of a gamma-aminobutyric acid A receptor
            epsilon-subunit in rat brain
  JOURNAL   Eur J Neurosci 12 (12), 4318-4330 (2000)
   PUBMED   11122342
REFERENCE   9  (residues 1 to 989)
  AUTHORS   Sinkkonen,S.T., Hanna,M.C., Kirkness,E.F. and Korpi,E.R.
  TITLE     GABA(A) receptor epsilon and theta subunits display unusual
            structural variation between species and are enriched in the rat
            locus ceruleus
  JOURNAL   J Neurosci 20 (10), 3588-3595 (2000)
   PUBMED   10804200
REFERENCE   10 (residues 1 to 989)
  AUTHORS   Davies,P.A., Hanna,M.C., Hales,T.G. and Kirkness,E.F.
  TITLE     Insensitivity to anaesthetic agents conferred by a class of GABA(A)
            receptor subunit
  JOURNAL   Nature 385 (6619), 820-823 (1997)
   PUBMED   9039914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF189262.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..989
                     /product="gamma-aminobutyric acid receptor subunit epsilon
                     precursor"
                     /note="gamma-aminobutyric acid receptor subunit epsilon;
                     GABA(A) receptor subunit epsilon; gamma-aminobutyric acid
                     (GABA-A) receptor, subunit epsilon; gamma-aminobutyric
                     acid A receptor, epsilon; gamma-aminobutyric acid type A
                     receptor epsilon subunit; gamma-aminobutyric acid (GABA) A
                     receptor, epsilon; GABAAR subunit epsilon"
                     /calculated_mol_wt=111321
     sig_peptide     1..17
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ES14.1)"
                     /calculated_mol_wt=1989
     Region          <54..124
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <120..177
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <196..249
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <263..315
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <290..357
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <338..405
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <376..443
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          <466..519
                     /region_name="Trypan_PARP"
                     /note="Procyclic acidic repetitive protein (PARP);
                     pfam05887"
                     /db_xref="CDD:368653"
     Region          557..983
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          579..760
                     /region_name="LGIC_ECD_GABAAR_E"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit epsilon (GABRE); cd19002"
                     /db_xref="CDD:349803"
     Site            order(586,605)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349803"
     Site            order(589,591..592,597..598,605,607..608,625,627..628,
                     637..642,645,647,649..650,656..658,660,670..672,700,760)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349803"
     Region          679..693
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349803"
     CDS             1..989
                     /gene="Gabre"
                     /coded_by="NM_023091.2:51..3020"
                     /db_xref="GeneID:65191"
                     /db_xref="RGD:68320"
ORIGIN      
        1 mlpkvllmll nmflalqwrv gphiklenkp paqdkvvfgp qpqpvpqpli ppespagddv
       61 vfdsqpqpqs espghddvfs sqpqplpqpq plpepqplpe pepqpqpqpq pqpqpqplag
      121 rqplpqplpw plpqpqpepe pqpepqpepq pepqpepqpe pqpepqpepq pqpqplagrq
      181 plpwplplpl pepqpdpqpd pqpepqpepq pepqpqpqtp gqvqagrqpr pkpqpdphph
      241 pqpepqpepr lhpfhrlrlr phpypephpg pqpepepepe pepqpepqpe pqpepqpepe
      301 pqpepepepe pepepepepe pepepepepe pepepepepe pepqpepepe pepepepepe
      361 pepepepqpe pqpepepepe pqpepqpepe pepepepepe pepepepqpe pqpepepqpe
      421 pqpdpepqpe pgpepgpepe pepqlepqpe pepepqpepe seldlepepe pqplpepqpe
      481 pepepepepe pepepepepe pepepepepe pepelelepq sqlepqpsgk klparetelt
      541 adhtterprg kltrasqiln tilsnydhkl rpsigekptv vtvkvfvnsl gpisildmey
      601 sidiifyqtw yderlryndt fetlilhgnv vsqlwipdtf frnskrtqey ditipnqmal
      661 ihkdgkvlyt vrmtidarcs lhmlnfpmds hscplsfssf sydehemiyk wenfklkida
      721 kntwkllefd ftgvnnktei istpvgdfmv mtfffnvsrr fgfivfqnyi pssvttmlsw
      781 vsfwikieaa aarasvgvss vltmatlgtf srknfprvsy ltaldfyiai cfvlcfctll
      841 eftvlnflty nnierqaspk fyqfptnsra nartrarart rararararq qqevfvceiv
      901 tyeenaeegy qwsprsrrpq cpwrrcgrsy vcfrvlrkyf cmvpgcegns wqrgricihv
      961 yrldnysrvl fpitffffnv vywviclnl
//
LOCUS       NP_001424019            1092 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 13 [Rattus norvegicus].
ACCESSION   NP_001424019 XP_006239100
VERSION     NP_001424019.1
DBSOURCE    REFSEQ: accession NM_001437090.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1092)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1092)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1092)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1092)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1092)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1092)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1092)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006239100.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2044449.1,
                                           SRR26360176.787075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1092
                     /product="pumilio homolog 1 isoform 13"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=115962
     Region          747..1070
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(803..804,807,839..840,843,878,881,913..914,917,
                     946..947,949..950,953,982..983,985..986,989,1025..1026,
                     1028..1029,1032,1062,1065)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1092
                     /gene="Pum1"
                     /coded_by="NM_001437090.1:114..3392"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgegprdad sdendkgekk nkgafdgdkl gdlkeegdvm
      181 dktnglpvqn gidadvkdfs rtpgncqssa nevdllgpnq ngseglaqlt stngakpved
      241 fsnmesqsvp ldpmehvgme plqfdysgtq vpvdsaaatv glfdynsqqq lfqrpnalav
      301 qqltaaqqqq yalaaahqph iglapaafvp npyiisaapp gtdpytagla aaatlgpavv
      361 phqyygvtpw gvypaslfqq qaaaaaaatn satqqsapqa qqgqqqvlrg gasqrpltpn
      421 qnqqgqqtdp lvaaaavnsa lafgqglaag mpgypvlapa ayydqtgalv vnagarnglg
      481 apvrlvapap viisssaaqa avaaaaasan gaagglagtt ngpfrplgtq qpqpqpqqqp
      541 snnlasssfy gnnslssnsq ssslfsqgsa qpantslgfg sssslgatlg salggfgtav
      601 ansntgsgsr rdsltgssdl ykrtssslap ighsfynsls fssspgpvgm plpsqgpghs
      661 qtpppslssh gsssslnlgg ltngsgryis aapgaeakyr sassasslfs psstlfsssr
      721 lrygmsdvmp sgrsrlledf rnnrypnlql reiaghimef sqdqhgsrfi qlklerataa
      781 erqlvfneil qaayqlmvdv fgnyviqkff efgsheqkla laerirghvl slalqmygcr
      841 viqkalefip sdqqvinemv reldghvlkc vkdqngnhvv qkciecvqpq slqfiidafk
      901 gqvfalsthp ygcrviqril ehclpdqtlp ileelhqhte qlvqdqygny viqhvlehgr
      961 pedkskivae irgnvlvlsq hkfasnvvek cvthasrter avlidevctm ndgphsalyt
     1021 mmkdqyanyv vqkmidvaep gqrkivmhki rphiatlrky tygkhilakl ekyymkngvd
     1081 lgpicgppng ii
//
LOCUS       NP_001424020             505 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 17 [Rattus norvegicus].
ACCESSION   NP_001424020 XP_038953118
VERSION     NP_001424020.1
DBSOURCE    REFSEQ: accession NM_001437091.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953118.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2007875.1,
                                           SRR26643285.52655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..505
                     /product="transcription factor 4 isoform 17"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=53747
     Region          396..480
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(404,408,410..412,414,419,440..441)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(417..418,421..422,424..425,428,432,442,445,449,452,
                     455..460)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..505
                     /gene="Tcf4"
                     /coded_by="NM_001437091.1:104..1621"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsgtavw srnggqasss pnyegplhsl qsriedrler lddaihvlrn
      241 havgpstavp gghgdmhgii gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr
      301 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      361 lqdtkssedk kldddkkdik sitsnndded ltpeqkaere kerrmannar erlrvrdine
      421 afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr ernlnpkaac lkrreeekvs
      481 seppplslag phpgmgdaan hmgqm
//
LOCUS       NP_001424007            1186 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424007 XP_006239095
VERSION     NP_001424007.1
DBSOURCE    REFSEQ: accession NM_001437078.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1186)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1186)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1186)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1186)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1186)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1186)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1186)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006239095.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21068.1,
                                           SRR26643295.22933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1186
                     /product="pumilio homolog 1 isoform 6"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126159
     Region          843..1164
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(899..900,903,935..936,939,972,975,1007..1008,1011,
                     1040..1041,1043..1044,1047,1076..1077,1079..1080,1083,
                     1119..1120,1122..1123,1126,1156,1159)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1186
                     /gene="Pum1"
                     /coded_by="NM_001437078.1:114..3674"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigla
      421 paafvpnpyi isaappgtdp ytaglaaaat lgpavvphqy ygvtpwgvyp aslfqqqaaa
      481 aaaatnsatq qsapqaqqgq qqvlrggasq rpltpnqnqq gqqtdplvaa aavnsalafg
      541 qglaagmpgy pvlapaayyd qtgalvvnag arnglgapvr lvapapviis ssaaqaavaa
      601 aaasangaag glagttngpf rplgtqqpqp qpqqqpsnnl asssfygnns lssnsqsssl
      661 fsqgsaqpan tslgfgssss lgatlgsalg gfgtavansn tgsgsrrdsl tgssdlykrt
      721 ssslapighs fynslsfsss pgpvgmplps qgpghsqtpp pslsshgsss slnlggltng
      781 sgryisaapg aeakyrsass asslfspsst lfsssrlryg msdvmpsgrs rlledfrnnr
      841 ypnlqlreia ghimefsqdq hgsrfiqlkl erataaerql vfneilqaay qlmvdvfgny
      901 viqkffefgs heqklalaer irghvlslal qmygcrviqk alefipsdqq nemvreldgh
      961 vlkcvkdqng nhvvqkciec vqpqslqfii dafkgqvfal sthpygcrvi qrilehclpd
     1021 qtlpileelh qhteqlvqdq ygnyviqhvl ehgrpedksk ivaeirgnvl vlsqhkfasn
     1081 vvekcvthas rteravlide vctmndgphs alytmmkdqy anyvvqkmid vaepgqrkiv
     1141 mhkirphiat lrkytygkhi laklekyymk ngvdlgpicg ppngii
//
LOCUS       NP_001424006             536 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424006 XP_063133698
VERSION     NP_001424006.1
DBSOURCE    REFSEQ: accession NM_001437077.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133698.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.358023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..536
                     /product="transcription factor 4 isoform 11"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=57082
     Region          6..>167
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          427..511
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(435,439,441..443,445,450,471..472)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(448..449,452..453,455..456,459,463,473,476,480,483,
                     486..491)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..536
                     /gene="Tcf4"
                     /coded_by="NM_001437077.1:219..1829"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyp yssnnarrrp lhsstmevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg yssskpaast fsssffmqdg hhssdpwsss sgmnqpgygg mlgnshipqs
      121 ssycslhphe rlsypshssa dinsslppms tfhrsgtnhy stssctppan gtdsimanrg
      181 tgaagssqtg dalgkalasi yspdhtnnsf ssnpstpvgs ppslsagtav wsrnggqass
      241 spnyegplhs lqsriedrle rlddaihvlr nhavgpstav pgghgdmhgi igpshngamg
      301 slgsgygtgl lsanrhslmv gahredgval rgshsllpnq vpvpqlpvqs atspdlnppq
      361 dpyrgmppgl qgqsvssgss eiksddegde nlqdtkssed kkldddkkdi ksitsnndde
      421 dltpeqkaer ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav
      481 avilsleqqv rernlnpkaa clkrreeekv sseppplsla gphpgmgdaa nhmgqm
//
LOCUS       NP_001424004            1191 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424004 XP_006239093
VERSION     NP_001424004.1
DBSOURCE    REFSEQ: accession NM_001437075.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1191)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006239093.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.30487.1,
                                           SRR26360176.502459.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1191
                     /product="pumilio homolog 1 isoform 3"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126663
     Region          848..1169
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(904..905,908,940..941,944,977,980,1012..1013,1016,
                     1045..1046,1048..1049,1052,1081..1082,1084..1085,1088,
                     1124..1125,1127..1128,1131,1161,1164)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1191
                     /gene="Pum1"
                     /coded_by="NM_001437075.1:114..3689"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigmf
      421 paglapaafv pnpyiisaap pgtdpytagl aaaatlgpav vphqyygvtp wgvypaslfq
      481 qqaaaaaaat nsatqqsapq aqqgqqqvlr ggasqrpltp nqnqqgqqtd plvaaaavns
      541 alafgqglaa gmpgypvlap aayydqtgal vvnagarngl gapvrlvapa pviisssaaq
      601 aavaaaaasa ngaagglagt tngpfrplgt qqpqpqpqqq psnnlasssf ygnnslssns
      661 qssslfsqgs aqpantslgf gsssslgatl gsalggfgta vansntgsgs rrdsltgssd
      721 lykrtsssla pighsfynsl sfssspgpvg mplpsqgpgh sqtpppslss hgsssslnlg
      781 gltngsgryi saapgaeaky rsassasslf spsstlfsss rlrygmsdvm psgrsrlled
      841 frnnrypnlq lreiaghime fsqdqhgsrf iqlklerata aerqlvfnei lqaayqlmvd
      901 vfgnyviqkf fefgsheqkl alaerirghv lslalqmygc rviqkalefi psdqqnemvr
      961 eldghvlkcv kdqngnhvvq kciecvqpqs lqfiidafkg qvfalsthpy gcrviqrile
     1021 hclpdqtlpi leelhqhteq lvqdqygnyv iqhvlehgrp edkskivaei rgnvlvlsqh
     1081 kfasnvvekc vthasrtera vlidevctmn dgphsalytm mkdqyanyvv qkmidvaepg
     1141 qrkivmhkir phiatlrkyt ygkhilakle kyymkngvdl gpicgppngi i
//
LOCUS       NP_001423955             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423955 XP_038950384
VERSION     NP_001423955.1
DBSOURCE    REFSEQ: accession NM_001437026.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038950384.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2454217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437026.1:544..2109"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424003             595 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 10 [Rattus norvegicus].
ACCESSION   NP_001424003 XP_063133697
VERSION     NP_001424003.1
DBSOURCE    REFSEQ: accession NM_001437074.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 595)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 595)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 595)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 595)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 595)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133697.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..595
                     /product="transcription factor 4 isoform 10"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=63799
     Region          65..>226
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          486..570
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(494,498,500..502,504,509,530..531)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(507..508,511..512,514..515,518,522,532,535,539,542,
                     545..550)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..595
                     /gene="Tcf4"
                     /coded_by="NM_001437074.1:132..1919"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mkdiffqflv arvrkrhsls clhtlpvvsp lrktergsys sygrenvqgc hqqsllggdm
       61 dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp ssvyapsast
      121 adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm lgnshipqss
      181 sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang tdsimanrgt
      241 gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw srnggqasss
      301 pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii gpshngamgs
      361 lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa tspdlnppqd
      421 pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik sitsnndded
      481 ltpeqkaere kerrmannar erlrvrdine afkelgrmvq lhlksdkpqt kllilhqava
      541 vilsleqqvr ernlnpkaac lkrreeekvs seppplslag phpgmgdaan hmgqm
//
LOCUS       NP_001099470             331 aa            linear   ROD 26-MAR-2025
DEFINITION  mitochondrial inner membrane protein COX18 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001099470 XP_001072704 XP_214011
VERSION     NP_001099470.1
DBSOURCE    REFSEQ: accession NM_001106000.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Bourens,M. and Barrientos,A.
  TITLE     Human mitochondrial cytochrome c oxidase assembly factor COX18 acts
            transiently as a membrane insertase within the subunit 2 maturation
            module
  JOURNAL   J Biol Chem 292 (19), 7774-7783 (2017)
   PUBMED   28330871
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Gaisne,M. and Bonnefoy,N.
  TITLE     The COX18 gene, involved in mitochondrial biogenesis, is
            functionally conserved and tightly regulated in humans and fission
            yeast
  JOURNAL   FEMS Yeast Res 6 (6), 869-882 (2006)
   PUBMED   16911509
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Sacconi,S., Trevisson,E., Pistollato,F., Baldoin,M.C.,
            Rezzonico,R., Bourget,I., Desnuelle,C., Tenconi,R., Basso,G.,
            DiMauro,S. and Salviati,L.
  TITLE     hCOX18 and hCOX19: two human genes involved in cytochrome c oxidase
            assembly
  JOURNAL   Biochem Biophys Res Commun 337 (3), 832-839 (2005)
   PUBMED   16212937
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_214011.4, XP_001072704.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.364187.1,
                                           SRR26360186.2585082.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..331
                     /product="mitochondrial inner membrane protein COX18
                     isoform 1"
                     /note="mitochondrial inner membrane protein COX18; COX18
                     cytochrome c oxidase assembly homolog; cytochrome c
                     oxidase assembly homolog 18; cytochrome c oxidase assembly
                     protein 18; COX18, cytochrome c oxidase assembly factor"
                     /calculated_mol_wt=36188
     Region          76..296
                     /region_name="5TM_Oxa1-like"
                     /note="Five transmembrane core domain of mitochondrial
                     inner membrane protein Oxa1 and similar proteins; cd20069"
                     /db_xref="CDD:410993"
     CDS             1..331
                     /gene="Cox18"
                     /gene_synonym="RGD1559547"
                     /coded_by="NM_001106000.2:68..1063"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289522"
                     /db_xref="RGD:1559547"
ORIGIN      
        1 mlcgscagll rslrtlqlra pgslpawssa rlptlpvwaa asvsaaspgg wyealaasap
       61 vhaaeemlls aqettglpww gnillstvvl rgavtlplaa yqhyilakve nlqpeikdia
      121 krlnqevavc arqfgwskrv arltylknir rlvselyvrd nchpfkatvl vwvqlpmwvf
      181 isvalrnlst gathsdgisv qdqlaaggtl wfpdltavds twilpvsvgv vnlliveifa
      241 lqkigksrfq myvtnfvrav svlmvpvaat vpsalvlywl csslmglsqn lllrspgfrq
      301 lcrippsrsd setpyrdlsa afcakflsrk r
//
LOCUS       NP_001423956             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423956 XP_006252676
VERSION     NP_001423956.1
DBSOURCE    REFSEQ: accession NM_001437027.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252676.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2071364.1,
                                           SRR26643297.46336.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437027.1:525..2090"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 13"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424008             536 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 12 [Rattus norvegicus].
ACCESSION   NP_001424008 XP_063133699
VERSION     NP_001424008.1
DBSOURCE    REFSEQ: accession NM_001437079.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133699.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1917391.1,
                                           SRR26360194.1990626.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..536
                     /product="transcription factor 4 isoform 12"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=57082
     Region          6..>167
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          427..511
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(435,439,441..443,445,450,471..472)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(448..449,452..453,455..456,459,463,473,476,480,483,
                     486..491)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..536
                     /gene="Tcf4"
                     /coded_by="NM_001437079.1:401..2011"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyp yssnnarrrp lhsstmevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg yssskpaast fsssffmqdg hhssdpwsss sgmnqpgygg mlgnshipqs
      121 ssycslhphe rlsypshssa dinsslppms tfhrsgtnhy stssctppan gtdsimanrg
      181 tgaagssqtg dalgkalasi yspdhtnnsf ssnpstpvgs ppslsagtav wsrnggqass
      241 spnyegplhs lqsriedrle rlddaihvlr nhavgpstav pgghgdmhgi igpshngamg
      301 slgsgygtgl lsanrhslmv gahredgval rgshsllpnq vpvpqlpvqs atspdlnppq
      361 dpyrgmppgl qgqsvssgss eiksddegde nlqdtkssed kkldddkkdi ksitsnndde
      421 dltpeqkaer ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav
      481 avilsleqqv rernlnpkaa clkrreeekv sseppplsla gphpgmgdaa nhmgqm
//
LOCUS       NP_001424002            1193 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424002 XP_006239091
VERSION     NP_001424002.1
DBSOURCE    REFSEQ: accession NM_001437073.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1193)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1193)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1193)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1193)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1193)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1193)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1193)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1193)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1193)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1193)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006239091.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.493683.1,
                                           SRR26360186.2800755.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1193
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1193
                     /product="pumilio homolog 1 isoform 2"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126875
     Region          848..1171
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(904..905,908,940..941,944,979,982,1014..1015,1018,
                     1047..1048,1050..1051,1054,1083..1084,1086..1087,1090,
                     1126..1127,1129..1130,1133,1163,1166)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1193
                     /gene="Pum1"
                     /coded_by="NM_001437073.1:114..3695"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigmf
      421 paglapaafv pnpyiisaap pgtdpytagl aaaatlgpav vphqyygvtp wgvypaslfq
      481 qqaaaaaaat nsatqqsapq aqqgqqqvlr ggasqrpltp nqnqqgqqtd plvaaaavns
      541 alafgqglaa gmpgypvlap aayydqtgal vvnagarngl gapvrlvapa pviisssaaq
      601 aavaaaaasa ngaagglagt tngpfrplgt qqpqpqpqqq psnnlasssf ygnnslssns
      661 qssslfsqgs aqpantslgf gsssslgatl gsalggfgta vansntgsgs rrdsltgssd
      721 lykrtsssla pighsfynsl sfssspgpvg mplpsqgpgh sqtpppslss hgsssslnlg
      781 gltngsgryi saapgaeaky rsassasslf spsstlfsss rlrygmsdvm psgrsrlled
      841 frnnrypnlq lreiaghime fsqdqhgsrf iqlklerata aerqlvfnei lqaayqlmvd
      901 vfgnyviqkf fefgsheqkl alaerirghv lslalqmygc rviqkalefi psdqqvinem
      961 vreldghvlk cvkdqngnhv vqkciecvqp qslqfiidaf kgqvfalsth pygcrviqri
     1021 lehclpdqtl pileelhqht eqlvqdqygn yviqhvlehg rpedkskiva eirgnvlvls
     1081 qhkfasnvve kcvthasrte ravlidevct mndgphsaly tmmkdqyany vvqkmidvae
     1141 pgqrkivmhk irphiatlrk ytygkhilak lekyymkngv dlgpicgppn gii
//
LOCUS       NP_001423951             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423951 XP_006252684
VERSION     NP_001423951.1
DBSOURCE    REFSEQ: accession NM_001437022.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252684.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.51999.1,
                                           SRR26643285.49875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437022.1:163..1728"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424011            1108 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424011 XP_017449005
VERSION     NP_001424011.1
DBSOURCE    REFSEQ: accession NM_001437082.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1108)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1108)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1108)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1108)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1108)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1108)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1108)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_017449005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.24530.1,
                                           SRR26360194.185885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1108
                     /product="pumilio homolog 1 isoform 9"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=118287
     Region          765..1086
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(821..822,825,857..858,861,894,897,929..930,933,
                     962..963,965..966,969,998..999,1001..1002,1005,1041..1042,
                     1044..1045,1048,1078,1081)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1108
                     /gene="Pum1"
                     /coded_by="NM_001437082.1:114..3440"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphiagl
      421 apaafvpnpy iisaappgtd pytaglaaaa tlgpavvphq yygvtpwgvy paslfqqqaa
      481 aaaaatnsat qqsapqaqqg qqqvlrggas qrpltpnqnq qgqqtdplva aaavnsalaf
      541 gqglaagmpg ypvlapaayy dqtgalvvna garnglgapv rlvapapvii sssaaqaava
      601 aaaasangaa gglagttngp frplgtqqpq pqpqqqpsnn lasssfygnn slssnsqsss
      661 lfsqgsaqpa ntslgfgsss slgatlgsal ggfgtagglt ngsgryisaa pgaeakyrsa
      721 ssasslfsps stlfsssrlr ygmsdvmpsg rsrlledfrn nrypnlqlre iaghimefsq
      781 dqhgsrfiql klerataaer qlvfneilqa ayqlmvdvfg nyviqkffef gsheqklala
      841 erirghvlsl alqmygcrvi qkalefipsd qqnemvreld ghvlkcvkdq ngnhvvqkci
      901 ecvqpqslqf iidafkgqvf alsthpygcr viqrilehcl pdqtlpilee lhqhteqlvq
      961 dqygnyviqh vlehgrpedk skivaeirgn vlvlsqhkfa snvvekcvth asrteravli
     1021 devctmndgp hsalytmmkd qyanyvvqkm idvaepgqrk ivmhkirphi atlrkytygk
     1081 hilaklekyy mkngvdlgpi cgppngii
//
LOCUS       NP_001423971             527 aa            linear   ROD 26-MAR-2025
DEFINITION  F-box-like/WD repeat-containing protein TBL1X [Rattus norvegicus].
ACCESSION   NP_001423971 XP_038955594
VERSION     NP_001423971.1
DBSOURCE    REFSEQ: accession NM_001437042.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Huang,J., Cardamone,M.D., Johnson,H.E., Neault,M., Chan,M.,
            Floyd,Z.E., Mallette,F.A. and Perissi,V.
  TITLE     Exchange Factor TBL1 and Arginine Methyltransferase PRMT6 Cooperate
            in Protecting G Protein Pathway Suppressor 2 (GPS2) from
            Proteasomal Degradation
  JOURNAL   J Biol Chem 290 (31), 19044-19054 (2015)
   PUBMED   26070566
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Oberoi,J., Fairall,L., Watson,P.J., Yang,J.C., Czimmerer,Z.,
            Kampmann,T., Goult,B.T., Greenwood,J.A., Gooch,J.T.,
            Kallenberger,B.C., Nagy,L., Neuhaus,D. and Schwabe,J.W.
  TITLE     Structural basis for the assembly of the SMRT/NCoR core
            transcriptional repression machinery
  JOURNAL   Nat Struct Mol Biol 18 (2), 177-184 (2011)
   PUBMED   21240272
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Perissi,V., Scafoglio,C., Zhang,J., Ohgi,K.A., Rose,D.W.,
            Glass,C.K. and Rosenfeld,M.G.
  TITLE     TBL1 and TBLR1 phosphorylation on regulated gene promoters
            overcomes dual CtBP and NCoR/SMRT transcriptional repression
            checkpoints
  JOURNAL   Mol Cell 29 (6), 755-766 (2008)
   PUBMED   18374649
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Ishii,S., Kurasawa,Y., Wong,J. and Yu-Lee,L.Y.
  TITLE     Histone deacetylase 3 localizes to the mitotic spindle and is
            required for kinetochore-microtubule attachment
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4179-4184 (2008)
   PUBMED   18326024
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Li,J. and Wang,C.Y.
  TITLE     TBL1-TBLR1 and beta-catenin recruit each other to Wnt target-gene
            promoter for transcription activation and oncogenesis
  JOURNAL   Nat Cell Biol 10 (2), 160-169 (2008)
   PUBMED   18193033
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Yoon,H.G., Choi,Y., Cole,P.A. and Wong,J.
  TITLE     Reading and function of a histone code involved in targeting
            corepressor complexes for repression
  JOURNAL   Mol Cell Biol 25 (1), 324-335 (2005)
   PUBMED   15601853
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Perissi,V., Aggarwal,A., Glass,C.K., Rose,D.W. and Rosenfeld,M.G.
  TITLE     A corepressor/coactivator exchange complex required for
            transcriptional activation by nuclear receptors and other regulated
            transcription factors
  JOURNAL   Cell 116 (4), 511-526 (2004)
   PUBMED   14980219
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Yoon,H.G., Chan,D.W., Huang,Z.Q., Li,J., Fondell,J.D., Qin,J. and
            Wong,J.
  TITLE     Purification and functional characterization of the human N-CoR
            complex: the roles of HDAC3, TBL1 and TBLR1
  JOURNAL   EMBO J 22 (6), 1336-1346 (2003)
   PUBMED   12628926
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Guenther,M.G., Lane,W.S., Fischle,W., Verdin,E., Lazar,M.A. and
            Shiekhattar,R.
  TITLE     A core SMRT corepressor complex containing HDAC3 and TBL1, a
            WD40-repeat protein linked to deafness
  JOURNAL   Genes Dev 14 (9), 1048-1057 (2000)
   PUBMED   10809664
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Bassi,M.T., Ramesar,R.S., Caciotti,B., Winship,I.M., De Grandi,A.,
            Riboni,M., Townes,P.L., Beighton,P., Ballabio,A. and Borsani,G.
  TITLE     X-linked late-onset sensorineural deafness caused by a deletion
            involving OA1 and a novel gene containing WD-40 repeats
  JOURNAL   Am J Hum Genet 64 (6), 1604-1616 (1999)
   PUBMED   10330347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038955594.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.31949.1,
                                           SRR26643285.22342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..527
                     /product="F-box-like/WD repeat-containing protein TBL1X"
                     /calculated_mol_wt=56671
     Region          7..31
                     /region_name="LisH"
                     /note="pfam08513"
                     /db_xref="CDD:462501"
     Region          177..483
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(181,199,203,209..210,232..233,255,259,265,277..278,
                     295,300,306..307,320,336,341,347..348,360..361,379,383,
                     389..390,402..403,429,434,440..441,453..454,472,476,
                     482..483)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          185..232
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          242..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          282..318
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          325..359
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          365..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          407..452
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <457..527
                     /region_name="8prop_heme_binding_protein"
                     /note="eight-bladed beta-propeller heme-binding domain in
                     cytochrome cd1 and similar proteins; cl49617"
                     /db_xref="CDD:483957"
     Region          458..482
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          460..494
                     /region_name="propeller blade"
                     /note="propeller blade [structural motif]"
                     /db_xref="CDD:467722"
     Region          499..525
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..527
                     /gene="Tbl1x"
                     /gene_synonym="RGD1563868"
                     /coded_by="NM_001437042.1:358..1941"
                     /db_xref="GeneID:302711"
                     /db_xref="RGD:1563868"
ORIGIN      
        1 msitsdevnf lvyrylqesg fshsaftfgi eshisqsnin gtlvppaali silqkglqyv
       61 eaeisinedg tvfdgrpies lslidavmpd vvqtrqqafr eklaqqqana aaaaaaaaat
      121 atstaattpa aaaqqnppkn geatvngeen gahainnhsk pmeidgdvei ppskatvlrg
      181 hesevficaw npvsdllasg sgdstariwn lnensnggst qlvlrhcire gghdvpsnkd
      241 vtsldwnsdg tllatgsydg fariwtedgn lastlgqhkg pifalkwnkk gnyilsagvd
      301 kttiiwdaht geakqqfpfh sapaldvdwq nnttfascst dmcihvcrlg cdrpvktfqg
      361 htnevnaikw dpsgmllasc sddmtlkiws mkqdacvhdl qahskeiyti kwsptgpats
      421 npnsnimlas asfdstvrlw dvergvciht ltkhqepvys vafspdgkyl asgsfdkcvh
      481 iwntqsgslv hsyrgtggif evcwnargdk vgasasdgsv cvldlrk
//
LOCUS       NP_001025223             106 aa            linear   ROD 26-MAR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 [Rattus
            norvegicus].
ACCESSION   NP_001025223 XP_342908
VERSION     NP_001025223.1
DBSOURCE    REFSEQ: accession NM_001030052.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Huang,G., Chen,Y., Lu,H. and Cao,X.
  TITLE     Coupling mitochondrial respiratory chain to cell death: an
            essential role of mitochondrial complex I in the interferon-beta
            and retinoic acid-induced cancer cell death
  JOURNAL   Cell Death Differ 14 (2), 327-337 (2007)
   PUBMED   16826196
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Aug 11, 2005 this sequence version replaced XP_342908.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB716681.1, BC168721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN12840122
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..106
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 5"
                     /EC_number="7.1.1.2"
                     /note="NADH dehydrogenase (ubiquinone) Fe-S protein 5b,
                     15kDa (NADH-coenzyme Q reductase)"
                     /calculated_mol_wt=12569
     Region          1..96
                     /region_name="NDUFS5-like"
                     /note="mitochondrial complex I subunit NDUFS5 and similar
                     proteins; cl10892"
                     /db_xref="CDD:472051"
     CDS             1..106
                     /gene="Ndufs5"
                     /gene_synonym="Ndufs5b"
                     /coded_by="NM_001030052.2:111..431"
                     /db_xref="GeneID:362588"
                     /db_xref="RGD:1311081"
ORIGIN      
        1 mpfldvqkrl gisldrhfif lsaeqpykna archafekew iecahgigat rakkeckiey
       61 edfeecflrf ktirrmheik kqreklmkeg kytppphhlg keeprp
//
LOCUS       NP_001423945             535 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423945 XP_006252672
VERSION     NP_001423945.1
DBSOURCE    REFSEQ: accession NM_001437016.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252672.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.431981.1,
                                           SRR26643295.51997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437016.1:88..1695"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001424017            1093 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 12 [Rattus norvegicus].
ACCESSION   NP_001424017 XP_063144111
VERSION     NP_001424017.1
DBSOURCE    REFSEQ: accession NM_001437088.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1093)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1093)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1093)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1093)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1093)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1093)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1093)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144111.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.23334.1,
                                           SRR26643287.14444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1093
                     /product="pumilio homolog 1 isoform 12"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=116033
     Region          748..1071
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(804..805,808,840..841,844,879,882,914..915,918,
                     947..948,950..951,954,983..984,986..987,990,1026..1027,
                     1029..1030,1033,1063,1066)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1093
                     /gene="Pum1"
                     /coded_by="NM_001437088.1:114..3395"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgegprdad sdendkgekk nkgafdgdkl gdlkeegdvm
      181 dktnglpvqn gidadvkdfs rtpgncqssa nevdllgpnq ngseglaqlt stngakpved
      241 fsnmesqsvp ldpmehvgme plqfdysgtq vpvdsaaatv glfdynsqqq lfqrpnalav
      301 qqltaaqqqq yalaaahqph iaglapaafv pnpyiisaap pgtdpytagl aaaatlgpav
      361 vphqyygvtp wgvypaslfq qqaaaaaaat nsatqqsapq aqqgqqqvlr ggasqrpltp
      421 nqnqqgqqtd plvaaaavns alafgqglaa gmpgypvlap aayydqtgal vvnagarngl
      481 gapvrlvapa pviisssaaq aavaaaaasa ngaagglagt tngpfrplgt qqpqpqpqqq
      541 psnnlasssf ygnnslssns qssslfsqgs aqpantslgf gsssslgatl gsalggfgta
      601 vansntgsgs rrdsltgssd lykrtsssla pighsfynsl sfssspgpvg mplpsqgpgh
      661 sqtpppslss hgsssslnlg gltngsgryi saapgaeaky rsassasslf spsstlfsss
      721 rlrygmsdvm psgrsrlled frnnrypnlq lreiaghime fsqdqhgsrf iqlklerata
      781 aerqlvfnei lqaayqlmvd vfgnyviqkf fefgsheqkl alaerirghv lslalqmygc
      841 rviqkalefi psdqqvinem vreldghvlk cvkdqngnhv vqkciecvqp qslqfiidaf
      901 kgqvfalsth pygcrviqri lehclpdqtl pileelhqht eqlvqdqygn yviqhvlehg
      961 rpedkskiva eirgnvlvls qhkfasnvve kcvthasrte ravlidevct mndgphsaly
     1021 tmmkdqyany vvqkmidvae pgqrkivmhk irphiatlrk ytygkhilak lekyymkngv
     1081 dlgpicgppn gii
//
LOCUS       NP_001423953             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423953 XP_038950382
VERSION     NP_001423953.1
DBSOURCE    REFSEQ: accession NM_001437024.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038950382.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.561000.1,
                                           SRR26360186.2718100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437024.1:598..2163"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424027             669 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 21 [Rattus norvegicus].
ACCESSION   NP_001424027 XP_038953087
VERSION     NP_001424027.1
DBSOURCE    REFSEQ: accession NM_001437098.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953087.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.60178.1,
                                           SRR26643299.63242.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..669
                     /product="transcription factor 4 isoform 21"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=71350
     Region          135..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          560..644
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(568,572,574..576,578,583,604..605)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(581..582,585..586,588..589,592,596,606,609,613,616,
                     619..624)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..669
                     /gene="Tcf4"
                     /coded_by="NM_001437098.1:580..2589"
                     /note="isoform 21 is encoded by transcript variant 22"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw
      361 srnggqasss pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii
      421 gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa
      481 tspdlnppqd pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik
      541 sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr dineafkelg rmvqlhlksd
      601 kpqtkllilh qavavilsle qqvrernlnp kaaclkrree ekvssepppl slagphpgmg
      661 daanhmgqm
//
LOCUS       NP_001012047             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001012047 XP_038950385 XP_224619
VERSION     NP_001012047.1
DBSOURCE    REFSEQ: accession NM_001012047.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Mar 26, 2025 this sequence version replaced
            XP_038950385.1, XP_224619.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1506989.1,
                                           SRR26360190.3006068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001012047.3:265..1830"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 14"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001423944             535 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423944 XP_006252681
VERSION     NP_001423944.1
DBSOURCE    REFSEQ: accession NM_001437015.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252681.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.163488.1,
                                           SRR26643287.32219.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437015.1:239..1846"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001423952             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423952 XP_006252677
VERSION     NP_001423952.1
DBSOURCE    REFSEQ: accession NM_001437023.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252677.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.51995.1,
                                           SRR26643290.47338.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437023.1:447..2012"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001424012             510 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 13 [Rattus norvegicus].
ACCESSION   NP_001424012 XP_038953114
VERSION     NP_001424012.1
DBSOURCE    REFSEQ: accession NM_001437083.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953114.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54618.1,
                                           SRR26643298.74603.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..510
                     /product="transcription factor 4 isoform 13"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=54305
     Region          401..485
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(409,413,415..417,419,424,445..446)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(422..423,426..427,429..430,433,437,447,450,454,457,
                     460..465)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..510
                     /gene="Tcf4"
                     /coded_by="NM_001437083.1:104..1636"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsagtav wsrnggqass spnyegplhs lqsriedrle rlddaihvlr
      241 nhavgpstav pgghgdmhgi igpshngamg slgsgygtgl lsanrhslmv gahredgval
      301 rgshsllpnq vpvpqlpvqs atspdlnppq dpyrgmppgl qgqsvssgss eiksddegde
      361 nlqdtkssed kkldddkkdi ksitrsrssn nddedltpeq kaerekerrm annarerlrv
      421 rdineafkel grmvqlhlks dkpqtkllil hqavavilsl eqqvrernln pkaaclkrre
      481 eekvsseppp lslagphpgm gdaanhmgqm
//
LOCUS       NP_001423949             535 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423949 XP_063131420
VERSION     NP_001423949.1
DBSOURCE    REFSEQ: accession NM_001437020.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063131420.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.49873.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437020.1:281..1888"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001424016             509 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 15 [Rattus norvegicus].
ACCESSION   NP_001424016 XP_038953116
VERSION     NP_001424016.1
DBSOURCE    REFSEQ: accession NM_001437087.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953116.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1736198.1,
                                           SRR26360176.1170088.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..509
                     /product="transcription factor 4 isoform 15"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=54234
     Region          400..484
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(408,412,414..416,418,423,444..445)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(421..422,425..426,428..429,432,436,446,449,453,456,
                     459..464)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..509
                     /gene="Tcf4"
                     /coded_by="NM_001437087.1:104..1633"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsgtavw srnggqasss pnyegplhsl qsriedrler lddaihvlrn
      241 havgpstavp gghgdmhgii gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr
      301 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      361 lqdtkssedk kldddkkdik sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr
      421 dineafkelg rmvqlhlksd kpqtkllilh qavavilsle qqvrernlnp kaaclkrree
      481 ekvssepppl slagphpgmg daanhmgqm
//
LOCUS       NP_001424009            1185 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424009 XP_063144104
VERSION     NP_001424009.1
DBSOURCE    REFSEQ: accession NM_001437080.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1185)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1185)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1185)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1185)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1185)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1185)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1185)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1185)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1185)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1185)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144104.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1642106.1,
                                           SRR26360176.1182857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1185
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1185
                     /product="pumilio homolog 1 isoform 7"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126031
     Region          842..1163
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(898..899,902,934..935,938,971,974,1006..1007,1010,
                     1039..1040,1042..1043,1046,1075..1076,1078..1079,1082,
                     1118..1119,1121..1122,1125,1155,1158)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1185
                     /gene="Pum1"
                     /coded_by="NM_001437080.1:114..3671"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgellpgkk fwetdesskd gpkgiflgdq wrdsawgtsd
      181 hsvsqpimvq rrpgqsfhvn sevnsvlspr sesgglgvsm veyvlssspg dsclrkggfg
      241 prdadsdend kgekknkgaf dgdklgdlke egdvmdktng lpvqngidad vkdfsrtpgn
      301 cqssanevdl lgpnqngseg laqltstnga kpvedfsnme sqsvpldpme hvgmeplqfd
      361 ysgtqvpvds aaatvglfdy nsqqqlfqrp nalavqqlta aqqqqyalaa ahqphiglap
      421 aafvpnpyii saappgtdpy taglaaaatl gpavvphqyy gvtpwgvypa slfqqqaaaa
      481 aaatnsatqq sapqaqqgqq qvlrggasqr pltpnqnqqg qqtdplvaaa avnsalafgq
      541 glaagmpgyp vlapaayydq tgalvvnaga rnglgapvrl vapapviiss saaqaavaaa
      601 aasangaagg lagttngpfr plgtqqpqpq pqqqpsnnla sssfygnnsl ssnsqssslf
      661 sqgsaqpant slgfgssssl gatlgsalgg fgtavansnt gsgsrrdslt gssdlykrts
      721 sslapighsf ynslsfsssp gpvgmplpsq gpghsqtppp slsshgssss lnlggltngs
      781 gryisaapga eakyrsassa sslfspsstl fsssrlrygm sdvmpsgrsr lledfrnnry
      841 pnlqlreiag himefsqdqh gsrfiqlkle rataaerqlv fneilqaayq lmvdvfgnyv
      901 iqkffefgsh eqklalaeri rghvlslalq mygcrviqka lefipsdqqn emvreldghv
      961 lkcvkdqngn hvvqkciecv qpqslqfiid afkgqvfals thpygcrviq rilehclpdq
     1021 tlpileelhq hteqlvqdqy gnyviqhvle hgrpedkski vaeirgnvlv lsqhkfasnv
     1081 vekcvthasr teravlidev ctmndgphsa lytmmkdqya nyvvqkmidv aepgqrkivm
     1141 hkirphiatl rkytygkhil aklekyymkn gvdlgpicgp pngii
//
LOCUS       NP_001424014             509 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 14 [Rattus norvegicus].
ACCESSION   NP_001424014 XP_038953115
VERSION     NP_001424014.1
DBSOURCE    REFSEQ: accession NM_001437085.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953115.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ221525.1, SRR26643292.60189.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..509
                     /product="transcription factor 4 isoform 14"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=54177
     Region          400..484
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(408,412,414..416,418,423,444..445)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(421..422,425..426,428..429,432,436,446,449,453,456,
                     459..464)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..509
                     /gene="Tcf4"
                     /coded_by="NM_001437085.1:104..1633"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsagtav wsrnggqass spnyegplhs lsriedrler lddaihvlrn
      241 havgpstavp gghgdmhgii gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr
      301 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      361 lqdtkssedk kldddkkdik sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr
      421 dineafkelg rmvqlhlksd kpqtkllilh qavavilsle qqvrernlnp kaaclkrree
      481 ekvssepppl slagphpgmg daanhmgqm
//
LOCUS       NP_001423996             644 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001423996 XP_063133694
VERSION     NP_001423996.1
DBSOURCE    REFSEQ: accession NM_001437067.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133694.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1776742.1,
                                           SRR26360186.1645629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..644
                     /product="transcription factor 4 isoform 5"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68582
     Region          111..>272
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          535..619
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(543,547,549..551,553,558,579..580)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(556..557,560..561,563..564,567,571,581,584,588,591,
                     594..599)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..644
                     /gene="Tcf4"
                     /coded_by="NM_001437067.1:560..2494"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqqs llggdmdmgn pgtlsptkpg
      121 sqyypyssnn arrrplhsst mevqtkkvrk vppglpssvy apsastadyn rdspgysssk
      181 paastfsssf fmqdghhssd pwssssgmnq pgyggmlgns hipqsssycs lhpherlsyp
      241 shssadinss lppmstfhrs gtnhystssc tppangtdsi manrgtgaag ssqtgdalgk
      301 alasiyspdh tnnsfssnps tpvgsppsls gtavwsrngg qassspnyeg plhslqsrie
      361 drlerlddai hvlrnhavgp stavpgghgd mhgiigpshn gamgslgsgy gtgllsanrh
      421 slmvgahred gvalrgshsl lpnqvpvpql pvqsatspdl nppqdpyrgm ppglqgqsvs
      481 sgsseiksdd egdenlqdtk ssedkklddd kkdiksitrs rssnnddedl tpeqkaerek
      541 errmannare rlrvrdinea fkelgrmvql hlksdkpqtk llilhqavav ilsleqqvre
      601 rnlnpkaacl krreeekvss eppplslagp hpgmgdaanh mgqm
//
LOCUS       NP_001423959             412 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423959
VERSION     NP_001423959.1
DBSOURCE    REFSEQ: accession NM_001437030.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.53239.1,
                                           SRR26360194.1264410.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..412
                     /product="biotinidase isoform 3"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=45983
     Region          <7..230
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cl11424"
                     /db_xref="CDD:448250"
     Site            order(81,85,87,114..115,117..118,140)
                     /site_type="active"
                     /db_xref="CDD:143591"
     Site            order(82..86,93..95,115,117..121,124..125,146..147,
                     149..151,153..154,178..179,226..229)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          262..411
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..412
                     /gene="Btd"
                     /coded_by="NM_001437030.1:153..1391"
                     /note="isoform 3 is encoded by transcript variant 17"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mpsprlvswn pclepfrfnd tevlqrlscm aikgkmflva nlgtkqpclg sdpgcpqdgr
       61 yqfntnvafs dngtlvgryr khnlyfeeaf dspadvdltt fdtpfagkfg mftcfdilff
      121 dpavrllrdf evkhiaypta wmnqlpllaa ieiqkafata fgvtvlaani hhptlgmtgs
      181 gihtplksfw yhnmddpegh liiarvatnp qglvgtentt semdpshrkf lkvlsgdpyc
      241 ekdaqevrcd eaakwnlnap ptfhsemmyd nftlvpvwgk eghlqvcsns lcchllferp
      301 alskelyalg vfdglhtvhg tyyvqacalv kcggagfetc gqeiseaegl fdfhlwgnfs
      361 tlyvfplflt sgmtldtpdq lgwesdhyfl rkrglssglv taalygrlye rn
//
LOCUS       NP_001423994             665 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423994 XP_063133689
VERSION     NP_001423994.1
DBSOURCE    REFSEQ: accession NM_001437065.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133689.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74598.1,
                                           SRR21887620.904550.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..665
                     /product="transcription factor 4 isoform 3"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=70864
     Region          81..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          556..640
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(564,568,570..572,574,579,600..601)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(577..578,581..582,584..585,588,592,602,605,609,612,
                     615..620)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..665
                     /gene="Tcf4"
                     /coded_by="NM_001437065.1:184..2181"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw
      361 srnggqasss pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii
      421 gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa
      481 tspdlnppqd pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik
      541 sitsnndded ltpeqkaere kerrmannar erlrvrdine afkelgrmvq lhlksdkpqt
      601 kllilhqava vilsleqqvr ernlnpkaac lkrreeekvs seppplslag phpgmgdaan
      661 hmgqm
//
LOCUS       NP_001423999             640 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001423999 XP_063133696
VERSION     NP_001423999.1
DBSOURCE    REFSEQ: accession NM_001437070.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 640)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 640)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133696.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1040193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..640
                     /product="transcription factor 4 isoform 8"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68039
     Region          57..>271
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          531..615
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(539,543,545..547,549,554,575..576)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(552..553,556..557,559..560,563,567,577,580,584,587,
                     590..595)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..640
                     /gene="Tcf4"
                     /coded_by="NM_001437070.1:560..2482"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqsl lggdmdmgnp gtlsptkpgs
      121 qyypyssnna rrrplhsstm evqtkkvrkv ppglpssvya psastadynr dspgyssskp
      181 aastfsssff mqdghhssdp wssssgmnqp gyggmlgnsh ipqsssycsl hpherlsyps
      241 hssadinssl ppmstfhrsg tnhystssct ppangtdsim anrgtgaags sqtgdalgka
      301 lasiyspdht nnsfssnpst pvgsppslsa gtavwsrngg qassspnyeg plhslqsrie
      361 drlerlddai hvlrnhavgp stavpgghgd mhgiigpshn gamgslgsgy gtgllsanrh
      421 slmvgahred gvalrgshsl lpnqvpvpql pvqsatspdl nppqdpyrgm ppglqgqsvs
      481 sgsseiksdd egdenlqdtk ssedkklddd kkdiksitsn nddedltpeq kaerekerrm
      541 annarerlrv rdineafkel grmvqlhlks dkpqtkllil hqavavilsl eqqvrernln
      601 pkaaclkrre eekvsseppp lslagphpgm gdaanhmgqm
//
LOCUS       NP_001423981             590 aa            linear   ROD 26-MAR-2025
DEFINITION  RNA-binding protein 47 [Rattus norvegicus].
ACCESSION   NP_001423981 XP_063129196
VERSION     NP_001423981.1
DBSOURCE    REFSEQ: accession NM_001437052.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Fossat,N., Tourle,K., Radziewic,T., Barratt,K., Liebhold,D.,
            Studdert,J.B., Power,M., Jones,V., Loebel,D.A. and Tam,P.P.
  TITLE     C to U RNA editing mediated by APOBEC1 requires RNA-binding protein
            RBM47
  JOURNAL   EMBO Rep 15 (8), 903-910 (2014)
   PUBMED   24916387
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063129196.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2641049.1,
                                           SRR26643294.49972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..590
                     /product="RNA-binding protein 47"
                     /note="hypothetical RNA binding protein RGD1359713"
                     /calculated_mol_wt=63963
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H68.1)"
     Region          11..590
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            396
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96; propagated from
                     UniProtKB/Swiss-Prot (Q66H68.1)"
     Site            407
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96; propagated from
                     UniProtKB/Swiss-Prot (Q66H68.1)"
     CDS             1..590
                     /gene="Rbm47"
                     /gene_synonym="RGD1359713"
                     /coded_by="NM_001437052.1:639..2411"
                     /db_xref="GeneID:305340"
                     /db_xref="RGD:1359713"
ORIGIN      
        1 mtaedsttam nsdptvgsst kvpegvagap neaallalme rtgynmvqen gqrkyggppp
       61 gwegphpqrg cevfvgkipr dvyedelvpv fetvgriyel rlmmdfdgkn rgyafvmych
      121 kheakravre lnnyeirpgr llgvccsvdn crlfiggipk mkkrgeilee iakvtegvln
      181 vivyasaadk mknrgfafve yeshraaama rrklmpgriq lwghqiavdw aepeidvded
      241 vmqtvkilyv rnlmiettee tikrsfgqfn pgcvervkki rdyafvhfts redavhamnn
      301 lngtelegsc levtlakpvd keqysryqka akggggsaea vaqqpsyvys cdpytlayyg
      361 ypynaligpn rdyfvktgsi rgrgrgaagn rtpgprgsyl ggysagrgiy sryhegkgkq
      421 qekgyelvpn leisavnpva ikpgtvaipa igaqysmfqa apapkiiedg kihtmehmis
      481 piavqpdpat aaaaaaaaaa aavipavstp ppfqgrpitp vytvapnvpr iptagiygas
      541 yvpfaapata tiatlqknaa aavyggyagy ipqafpaalq vpihdvyqty
//
LOCUS       NP_445821                664 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_445821 XP_063133690
VERSION     NP_445821.2
DBSOURCE    REFSEQ: accession NM_053369.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Mar 26, 2025 this sequence version replaced
            XP_063133690.1, NP_445821.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..664
                     /product="transcription factor 4 isoform 1"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=70736
     Region          81..>295
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          555..639
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(563,567,569..571,573,578,599..600)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(576..577,580..581,583..584,587,591,601,604,608,611,
                     614..619)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..664
                     /gene="Tcf4"
                     /coded_by="NM_053369.3:184..2178"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqsllggdmd mgnpgtlspt kpgsqyypys snnarrrplh sstmevqtkk vrkvppglps
      181 svyapsasta dynrdspgys sskpaastfs ssffmqdghh ssdpwssssg mnqpgyggml
      241 gnshipqsss ycslhpherl sypshssadi nsslppmstf hrsgtnhyst ssctppangt
      301 dsimanrgtg aagssqtgda lgkalasiys pdhtnnsfss npstpvgspp slsagtavws
      361 rnggqasssp nyegplhslq sriedrlerl ddaihvlrnh avgpstavpg ghgdmhgiig
      421 pshngamgsl gsgygtglls anrhslmvga hredgvalrg shsllpnqvp vpqlpvqsat
      481 spdlnppqdp yrgmppglqg qsvssgssei ksddegdenl qdtkssedkk ldddkkdiks
      541 itsnnddedl tpeqkaerek errmannare rlrvrdinea fkelgrmvql hlksdkpqtk
      601 llilhqavav ilsleqqvre rnlnpkaacl krreeekvss eppplslagp hpgmgdaanh
      661 mgqm
//
LOCUS       NP_001424022             505 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 18 [Rattus norvegicus].
ACCESSION   NP_001424022 XP_063133700
VERSION     NP_001424022.1
DBSOURCE    REFSEQ: accession NM_001437093.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133700.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.177477.1,
                                           SRR26360172.1400247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..505
                     /product="transcription factor 4 isoform 18"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=53690
     Region          396..480
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(404,408,410..412,414,419,440..441)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(417..418,421..422,424..425,428,432,442,445,449,452,
                     455..460)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..505
                     /gene="Tcf4"
                     /coded_by="NM_001437093.1:104..1621"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsagtav wsrnggqass spnyegplhs lsriedrler lddaihvlrn
      241 havgpstavp gghgdmhgii gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr
      301 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      361 lqdtkssedk kldddkkdik sitsnndded ltpeqkaere kerrmannar erlrvrdine
      421 afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr ernlnpkaac lkrreeekvs
      481 seppplslag phpgmgdaan hmgqm
//
LOCUS       NP_001424010            1109 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424010 XP_063144107
VERSION     NP_001424010.1
DBSOURCE    REFSEQ: accession NM_001437081.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1109)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1109)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1109)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1109)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1109)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1109)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1109)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144107.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.789757.1,
                                           SRR26643290.20647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1109
                     /product="pumilio homolog 1 isoform 8"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=118428
     Region          764..1087
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(820..821,824,856..857,860,895,898,930..931,934,
                     963..964,966..967,970,999..1000,1002..1003,1006,
                     1042..1043,1045..1046,1049,1079,1082)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1109
                     /gene="Pum1"
                     /coded_by="NM_001437081.1:114..3443"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigla
      421 paafvpnpyi isaappgtdp ytaglaaaat lgpavvphqy ygvtpwgvyp aslfqqqaaa
      481 aaaatnsatq qsapqaqqgq qqvlrggasq rpltpnqnqq gqqtdplvaa aavnsalafg
      541 qglaagmpgy pvlapaayyd qtgalvvnag arnglgapvr lvapapviis ssaaqaavaa
      601 aaasangaag glagttngpf rplgtqqpqp qpqqqpsnnl asssfygnns lssnsqsssl
      661 fsqgsaqpan tslgfgssss lgatlgsalg gfgtaggltn gsgryisaap gaeakyrsas
      721 sasslfspss tlfsssrlry gmsdvmpsgr srlledfrnn rypnlqlrei aghimefsqd
      781 qhgsrfiqlk lerataaerq lvfneilqaa yqlmvdvfgn yviqkffefg sheqklalae
      841 rirghvlsla lqmygcrviq kalefipsdq qvinemvrel dghvlkcvkd qngnhvvqkc
      901 iecvqpqslq fiidafkgqv falsthpygc rviqrilehc lpdqtlpile elhqhteqlv
      961 qdqygnyviq hvlehgrped kskivaeirg nvlvlsqhkf asnvvekcvt hasrteravl
     1021 idevctmndg phsalytmmk dqyanyvvqk midvaepgqr kivmhkirph iatlrkytyg
     1081 khilakleky ymkngvdlgp icgppngii
//
LOCUS       NP_001424021            1091 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 14 [Rattus norvegicus].
ACCESSION   NP_001424021 XP_063144122
VERSION     NP_001424021.1
DBSOURCE    REFSEQ: accession NM_001437092.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144122.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.16250.1,
                                           SRR26643297.20302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1091
                     /product="pumilio homolog 1 isoform 14"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=115821
     Region          748..1069
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(804..805,808,840..841,844,877,880,912..913,916,
                     945..946,948..949,952,981..982,984..985,988,1024..1025,
                     1027..1028,1031,1061,1064)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1091
                     /gene="Pum1"
                     /coded_by="NM_001437092.1:114..3389"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgegprdad sdendkgekk nkgafdgdkl gdlkeegdvm
      181 dktnglpvqn gidadvkdfs rtpgncqssa nevdllgpnq ngseglaqlt stngakpved
      241 fsnmesqsvp ldpmehvgme plqfdysgtq vpvdsaaatv glfdynsqqq lfqrpnalav
      301 qqltaaqqqq yalaaahqph iaglapaafv pnpyiisaap pgtdpytagl aaaatlgpav
      361 vphqyygvtp wgvypaslfq qqaaaaaaat nsatqqsapq aqqgqqqvlr ggasqrpltp
      421 nqnqqgqqtd plvaaaavns alafgqglaa gmpgypvlap aayydqtgal vvnagarngl
      481 gapvrlvapa pviisssaaq aavaaaaasa ngaagglagt tngpfrplgt qqpqpqpqqq
      541 psnnlasssf ygnnslssns qssslfsqgs aqpantslgf gsssslgatl gsalggfgta
      601 vansntgsgs rrdsltgssd lykrtsssla pighsfynsl sfssspgpvg mplpsqgpgh
      661 sqtpppslss hgsssslnlg gltngsgryi saapgaeaky rsassasslf spsstlfsss
      721 rlrygmsdvm psgrsrlled frnnrypnlq lreiaghime fsqdqhgsrf iqlklerata
      781 aerqlvfnei lqaayqlmvd vfgnyviqkf fefgsheqkl alaerirghv lslalqmygc
      841 rviqkalefi psdqqnemvr eldghvlkcv kdqngnhvvq kciecvqpqs lqfiidafkg
      901 qvfalsthpy gcrviqrile hclpdqtlpi leelhqhteq lvqdqygnyv iqhvlehgrp
      961 edkskivaei rgnvlvlsqh kfasnvvekc vthasrtera vlidevctmn dgphsalytm
     1021 mkdqyanyvv qkmidvaepg qrkivmhkir phiatlrkyt ygkhilakle kyymkngvdl
     1081 gpicgppngi i
//
LOCUS       NP_001423997             644 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001423997 XP_063133693
VERSION     NP_001423997.1
DBSOURCE    REFSEQ: accession NM_001437068.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133693.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1463682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..644
                     /product="transcription factor 4 isoform 6"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68525
     Region          57..>271
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          535..619
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(543,547,549..551,553,558,579..580)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(556..557,560..561,563..564,567,571,581,584,588,591,
                     594..599)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..644
                     /gene="Tcf4"
                     /coded_by="NM_001437068.1:560..2494"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqsl lggdmdmgnp gtlsptkpgs
      121 qyypyssnna rrrplhsstm evqtkkvrkv ppglpssvya psastadynr dspgyssskp
      181 aastfsssff mqdghhssdp wssssgmnqp gyggmlgnsh ipqsssycsl hpherlsyps
      241 hssadinssl ppmstfhrsg tnhystssct ppangtdsim anrgtgaags sqtgdalgka
      301 lasiyspdht nnsfssnpst pvgsppslsa gtavwsrngg qassspnyeg plhslqsrie
      361 drlerlddai hvlrnhavgp stavpgghgd mhgiigpshn gamgslgsgy gtgllsanrh
      421 slmvgahred gvalrgshsl lpnqvpvpql pvqsatspdl nppqdpyrgm ppglqgqsvs
      481 sgsseiksdd egdenlqdtk ssedkklddd kkdiksitrs rssnnddedl tpeqkaerek
      541 errmannare rlrvrdinea fkelgrmvql hlksdkpqtk llilhqavav ilsleqqvre
      601 rnlnpkaacl krreeekvss eppplslagp hpgmgdaanh mgqm
//
LOCUS       NP_001424018             506 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 16 [Rattus norvegicus].
ACCESSION   NP_001424018 XP_038953117
VERSION     NP_001424018.1
DBSOURCE    REFSEQ: accession NM_001437089.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953117.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54619.1,
                                           SRR26643299.63249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..506
                     /product="transcription factor 4 isoform 16"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=53818
     Region          397..481
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(405,409,411..413,415,420,441..442)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(418..419,422..423,425..426,429,433,443,446,450,453,
                     456..461)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..506
                     /gene="Tcf4"
                     /coded_by="NM_001437089.1:104..1624"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsagtav wsrnggqass spnyegplhs lqsriedrle rlddaihvlr
      241 nhavgpstav pgghgdmhgi igpshngamg slgsgygtgl lsanrhslmv gahredgval
      301 rgshsllpnq vpvpqlpvqs atspdlnppq dpyrgmppgl qgqsvssgss eiksddegde
      361 nlqdtkssed kkldddkkdi ksitsnndde dltpeqkaer ekerrmanna rerlrvrdin
      421 eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv rernlnpkaa clkrreeekv
      481 sseppplsla gphpgmgdaa nhmgqm
//
LOCUS       NP_001424024             504 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 19 [Rattus norvegicus].
ACCESSION   NP_001424024 XP_063133701
VERSION     NP_001424024.1
DBSOURCE    REFSEQ: accession NM_001437095.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133701.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2240825.1,
                                           SRR26360176.2350447.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..504
                     /product="transcription factor 4 isoform 19"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=53619
     Region          395..479
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(403,407,409..411,413,418,439..440)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(416..417,420..421,423..424,427,431,441,444,448,451,
                     454..459)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..504
                     /gene="Tcf4"
                     /coded_by="NM_001437095.1:104..1618"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mycaytipgm ggnslmyyyn gkavyapsas tadynrdspg yssskpaast fsssffmqdg
       61 hhssdpwsss sgmnqpgygg mlgnshipqs ssycslhphe rlsypshssa dinsslppms
      121 tfhrsgtnhy stssctppan gtdsimanrg tgaagssqtg dalgkalasi yspdhtnnsf
      181 ssnpstpvgs ppslsgtavw srnggqasss pnyegplhsl sriedrlerl ddaihvlrnh
      241 avgpstavpg ghgdmhgiig pshngamgsl gsgygtglls anrhslmvga hredgvalrg
      301 shsllpnqvp vpqlpvqsat spdlnppqdp yrgmppglqg qsvssgssei ksddegdenl
      361 qdtkssedkk ldddkkdiks itsnnddedl tpeqkaerek errmannare rlrvrdinea
      421 fkelgrmvql hlksdkpqtk llilhqavav ilsleqqvre rnlnpkaacl krreeekvss
      481 eppplslagp hpgmgdaanh mgqm
//
LOCUS       NP_001423958             521 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423958
VERSION     NP_001423958.1
DBSOURCE    REFSEQ: accession NM_001437029.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1649567.1,
                                           SRR21887622.2182944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437029.1:442..2007"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 16"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001423946             535 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423946 XP_038950381
VERSION     NP_001423946.1
DBSOURCE    REFSEQ: accession NM_001437017.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038950381.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32220.1,
                                           SRR26643295.51996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437017.1:166..1773"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001423980             106 aa            linear   ROD 26-MAR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 [Rattus
            norvegicus].
ACCESSION   NP_001423980 XP_006238890
VERSION     NP_001423980.1
DBSOURCE    REFSEQ: accession NM_001437051.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Huang,G., Chen,Y., Lu,H. and Cao,X.
  TITLE     Coupling mitochondrial respiratory chain to cell death: an
            essential role of mitochondrial complex I in the interferon-beta
            and retinoic acid-induced cancer cell death
  JOURNAL   Cell Death Differ 14 (2), 327-337 (2007)
   PUBMED   16826196
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006238890.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.2028829.1,
                                           SRR22399484.995025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..106
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 5"
                     /EC_number="7.1.1.2"
                     /note="NADH dehydrogenase (ubiquinone) Fe-S protein 5b,
                     15kDa (NADH-coenzyme Q reductase)"
                     /calculated_mol_wt=12569
     Region          1..96
                     /region_name="NDUFS5-like"
                     /note="mitochondrial complex I subunit NDUFS5 and similar
                     proteins; cl10892"
                     /db_xref="CDD:472051"
     CDS             1..106
                     /gene="Ndufs5"
                     /gene_synonym="Ndufs5b"
                     /coded_by="NM_001437051.1:160..480"
                     /db_xref="GeneID:362588"
                     /db_xref="RGD:1311081"
ORIGIN      
        1 mpfldvqkrl gisldrhfif lsaeqpykna archafekew iecahgigat rakkeckiey
       61 edfeecflrf ktirrmheik kqreklmkeg kytppphhlg keeprp
//
LOCUS       NP_001423993             668 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423993 XP_063133686
VERSION     NP_001423993.1
DBSOURCE    REFSEQ: accession NM_001437064.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133686.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360176.2345999.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..668
                     /product="transcription factor 4 isoform 2"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=71279
     Region          135..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          559..643
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(567,571,573..575,577,582,603..604)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(580..581,584..585,587..588,591,595,605,608,612,615,
                     618..623)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..668
                     /gene="Tcf4"
                     /coded_by="NM_001437064.1:184..2190"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsgtavws
      361 rnggqasssp nyegplhslq sriedrlerl ddaihvlrnh avgpstavpg ghgdmhgiig
      421 pshngamgsl gsgygtglls anrhslmvga hredgvalrg shsllpnqvp vpqlpvqsat
      481 spdlnppqdp yrgmppglqg qsvssgssei ksddegdenl qdtkssedkk ldddkkdiks
      541 itrsrssnnd dedltpeqka erekerrman narerlrvrd ineafkelgr mvqlhlksdk
      601 pqtkllilhq avavilsleq qvrernlnpk aaclkrreee kvssepppls lagphpgmgd
      661 aanhmgqm
//
LOCUS       NP_001423998             641 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001423998 XP_063133695
VERSION     NP_001423998.1
DBSOURCE    REFSEQ: accession NM_001437069.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 641)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 641)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 641)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 641)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063133695.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.63240.1,
                                           SRR26360186.1499892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..641
                     /product="transcription factor 4 isoform 7"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=68167
     Region          111..>272
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          532..616
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(540,544,546..548,550,555,576..577)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(553..554,557..558,560..561,564,568,578,581,585,588,
                     591..596)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..641
                     /gene="Tcf4"
                     /coded_by="NM_001437069.1:560..2485"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr envqgchqqs llggdmdmgn pgtlsptkpg
      121 sqyypyssnn arrrplhsst mevqtkkvrk vppglpssvy apsastadyn rdspgysssk
      181 paastfsssf fmqdghhssd pwssssgmnq pgyggmlgns hipqsssycs lhpherlsyp
      241 shssadinss lppmstfhrs gtnhystssc tppangtdsi manrgtgaag ssqtgdalgk
      301 alasiyspdh tnnsfssnps tpvgsppsls agtavwsrng gqassspnye gplhslqsri
      361 edrlerldda ihvlrnhavg pstavpgghg dmhgiigpsh ngamgslgsg ygtgllsanr
      421 hslmvgahre dgvalrgshs llpnqvpvpq lpvqsatspd lnppqdpyrg mppglqgqsv
      481 ssgsseiksd degdenlqdt kssedkkldd dkkdiksits nnddedltpe qkaerekerr
      541 mannarerlr vrdineafke lgrmvqlhlk sdkpqtklli lhqavavils leqqvrernl
      601 npkaaclkrr eeekvssepp plslagphpg mgdaanhmgq m
//
LOCUS       NP_001423947             535 aa            linear   ROD 26-MAR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423947 XP_063131419
VERSION     NP_001423947.1
DBSOURCE    REFSEQ: accession NM_001437018.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063131419.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1850297.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680435
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437018.1:208..1815"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001414112             652 aa            linear   ROD 26-MAR-2025
DEFINITION  cylicin-2 [Rattus norvegicus].
ACCESSION   NP_001414112 XP_008761941
VERSION     NP_001414112.1
DBSOURCE    REFSEQ: accession NM_001427183.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 11, 2024 this sequence version replaced XP_008761941.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1454343.1,
                                           SRR26643293.27809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q23"
     Protein         1..652
                     /product="cylicin-2"
                     /note="cylicin, basic protein of sperm head cytoskeleton
                     2"
                     /calculated_mol_wt=68652
     Region          8..113
                     /region_name="Cylicin_N"
                     /note="Cylicin N-terminus; pfam15241"
                     /db_xref="CDD:464581"
     Region          <108..572
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     CDS             1..652
                     /gene="Cylc2"
                     /gene_synonym="RGD1562799"
                     /coded_by="NM_001427183.2:41..1999"
                     /db_xref="GeneID:500458"
                     /db_xref="RGD:1562799"
ORIGIN      
        1 msiprflkvt ygaydnyipv selskkswnq qyfslafpkp prpgkkrrsl psqlqnnpap
       61 videqklgih kpplwmhrsl mriserpsvy laarkslppk pprfgkgefk ragttktlas
      121 ekskkevklk kdeceakekk alktekeenl kpvdtkiskd sqkdkgkiss gsegekagvk
      181 kdvttskkgt kgtdsasetg sdkpgvkkdi ktskkgtkgt dsasesgnek asgkkeakts
      241 kkgpkakdsa setgsekagg kkeaksskkg lkakesasds gsekaggkke aksskkglka
      301 kesasdsgse kaggkkgvkg skkglkakes asdsgsekag gkkgvkgskk gskakdsase
      361 tgsekaggkk dakaskkvsk dkssasesgg ekaggkkeak askkvskdks sasesggeka
      421 ggkkeakask kvskdkasps esevakaggk keakaskkvs kdkvsasesg gekaggkkea
      481 kaskkvskdk vsasesdgek sggkkearas kkgskdkasa sesggekagg kkeakadkks
      541 pkqsketlvs kavdkdvgkk eeksvkqgsk gkdvvadsas ekgdagkeak kkeekekkkk
      601 gegdakegsk kekkdkkdkk dkkdkkdkkd kkdkkdkkek kdkkekkekk ak
//
LOCUS       NP_001424025             454 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 20 [Rattus norvegicus].
ACCESSION   NP_001424025 XP_038953119
VERSION     NP_001424025.1
DBSOURCE    REFSEQ: accession NM_001437096.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953119.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.419797.1,
                                           SRR26643429.54622.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..454
                     /product="transcription factor 4 isoform 20"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=48318
     Region          345..429
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(353,357,359..361,363,368,389..390)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(366..367,370..371,373..374,377,381,391,394,398,401,
                     404..409)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..454
                     /gene="Tcf4"
                     /coded_by="NM_001437096.1:678..2042"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mqdghhssdp wssssgmnqp gyggmlgnsh ipqsssycsl hpherlsyps hssadinssl
       61 ppmstfhrsg tnhystssct ppangtdsim anrgtgaags sqtgdalgka lasiyspdht
      121 nnsfssnpst pvgsppslsa gtavwsrngg qassspnyeg plhslqsrie drlerlddai
      181 hvlrnhavgp stavpgghgd mhgiigpshn gamgslgsgy gtgllsanrh slmvgahred
      241 gvalrgshsl lpnqvpvpql pvqsatspdl nppqdpyrgm ppglqgqsvs sgsseiksdd
      301 egdenlqdtk ssedkklddd kkdiksitrs rssnnddedl tpeqkaerek errmannare
      361 rlrvrdinea fkelgrmvql hlksdkpqtk llilhqavav ilsleqqvre rnlnpkaacl
      421 krreeekvss eppplslagp hpgmgdaanh mgqm
//
LOCUS       NP_001102154            1189 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001102154 XP_001063603 XP_342929
VERSION     NP_001102154.1
DBSOURCE    REFSEQ: accession NM_001108684.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1189)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1189)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1189)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1189)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1189)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1189)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1189)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001063603.1, XP_342929.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.22932.1,
                                           SRR26643299.24531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1189
                     /product="pumilio homolog 1 isoform 4"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126443
     Region          844..1167
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(900..901,904,936..937,940,975,978,1010..1011,1014,
                     1043..1044,1046..1047,1050,1079..1080,1082..1083,1086,
                     1122..1123,1125..1126,1129,1159,1162)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1189
                     /gene="Pum1"
                     /coded_by="NM_001108684.2:114..3683"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphiagl
      421 apaafvpnpy iisaappgtd pytaglaaaa tlgpavvphq yygvtpwgvy paslfqqqaa
      481 aaaaatnsat qqsapqaqqg qqqvlrggas qrpltpnqnq qgqqtdplva aaavnsalaf
      541 gqglaagmpg ypvlapaayy dqtgalvvna garnglgapv rlvapapvii sssaaqaava
      601 aaaasangaa gglagttngp frplgtqqpq pqpqqqpsnn lasssfygnn slssnsqsss
      661 lfsqgsaqpa ntslgfgsss slgatlgsal ggfgtavans ntgsgsrrds ltgssdlykr
      721 tssslapigh sfynslsfss spgpvgmplp sqgpghsqtp ppslsshgss sslnlggltn
      781 gsgryisaap gaeakyrsas sasslfspss tlfsssrlry gmsdvmpsgr srlledfrnn
      841 rypnlqlrei aghimefsqd qhgsrfiqlk lerataaerq lvfneilqaa yqlmvdvfgn
      901 yviqkffefg sheqklalae rirghvlsla lqmygcrviq kalefipsdq qvinemvrel
      961 dghvlkcvkd qngnhvvqkc iecvqpqslq fiidafkgqv falsthpygc rviqrilehc
     1021 lpdqtlpile elhqhteqlv qdqygnyviq hvlehgrped kskivaeirg nvlvlsqhkf
     1081 asnvvekcvt hasrteravl idevctmndg phsalytmmk dqyanyvvqk midvaepgqr
     1141 kivmhkirph iatlrkytyg khilakleky ymkngvdlgp icgppngii
//
LOCUS       NP_001099421            1621 aa            linear   ROD 26-MAR-2025
DEFINITION  phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing
            subunit beta isoform 2 [Rattus norvegicus].
ACCESSION   NP_001099421 XP_001060466 XP_213879
VERSION     NP_001099421.1
DBSOURCE    REFSEQ: accession NM_001105951.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1621)
  AUTHORS   Kozhevnikova,O.S., Telegina,D.V., Devyatkin,V.A. and Kolosova,N.G.
  TITLE     Involvement of the autophagic pathway in the progression of
            AMD-like retinopathy in senescence-accelerated OXYS rats
  JOURNAL   Biogerontology 19 (3-4), 223-235 (2018)
   PUBMED   29492791
  REMARK    GeneRIF: Missense single-nucleotide polymorphism in the Pik3c2b
            gene associated with autophagy regulation in in the progression of
            Age-related macular degeneration was found.
REFERENCE   2  (residues 1 to 1621)
  AUTHORS   Devereaux,K., Dall'Armi,C., Alcazar-Roman,A., Ogasawara,Y.,
            Zhou,X., Wang,F., Yamamoto,A., De Camilli,P. and Di Paolo,G.
  TITLE     Regulation of mammalian autophagy by class II and III PI 3-kinases
            through PI3P synthesis
  JOURNAL   PLoS One 8 (10), e76405 (2013)
   PUBMED   24098492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1621)
  AUTHORS   Das,M., Scappini,E., Martin,N.P., Wong,K.A., Dunn,S., Chen,Y.J.,
            Miller,S.L., Domin,J. and O'Bryan,J.P.
  TITLE     Regulation of neuron survival through an
            intersectin-phosphoinositide 3'-kinase C2beta-AKT pathway
  JOURNAL   Mol Cell Biol 27 (22), 7906-7917 (2007)
   PUBMED   17875942
REFERENCE   4  (residues 1 to 1621)
  AUTHORS   Sindic,A., Crljen,V., Matkovic,K., Lukinovic-Skudar,V., Visnjic,D.
            and Banfic,H.
  TITLE     Activation of phosphoinositide 3-kinase C2 beta in the nuclear
            matrix during compensatory liver growth
  JOURNAL   Adv Enzyme Regul 46, 280-287 (2006)
   PUBMED   16857245
  REMARK    GeneRIF: Activated during compensatory liver growth, which clearly
            demonstrates that different class II PI3K enzymes have different
            subnuclear localization.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_213879.3, XP_001060466.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..1621
                     /product="phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta isoform 2"
                     /EC_number="2.7.1.154"
                     /note="phosphoinositide-3-kinase, class 2, beta
                     polypeptide; nuclear cap binding protein subunit 2;
                     phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta"
                     /calculated_mol_wt=183007
     Region          363..465
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          609..781
                     /region_name="C2A_PI3K_class_II"
                     /note="C2 domain first repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd04012"
                     /db_xref="CDD:175979"
     Region          800..968
                     /region_name="PI3Ka_II"
                     /note="Phosphoinositide 3-kinase (PI3K) class II,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, class II PI3-kinases...; cd00869"
                     /db_xref="CDD:238441"
     Region          974..1327
                     /region_name="PI3Kc_C2_beta"
                     /note="Catalytic domain of Class II Phosphoinositide
                     3-kinase beta; cd00895"
                     /db_xref="CDD:119421"
     Site            order(1044,1046..1048,1050,1068,1070,1073,1104,1116..1119,
                     1124,1127,1187,1189,1199..1200)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:119421"
     Site            1179..1187
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:119421"
     Site            1200..1224
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:119421"
     Region          1356..1464
                     /region_name="PX_PI3K_C2_beta"
                     /note="The phosphoinositide binding Phox Homology Domain
                     of the Beta Isoform of Class II Phosphoinositide
                     3-Kinases; cd07290"
                     /db_xref="CDD:132823"
     Site            order(1392..1394,1418..1419,1433)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132823"
     Region          1492..1614
                     /region_name="C2B_PI3K_class_II"
                     /note="C2 domain second repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd08381"
                     /db_xref="CDD:176027"
     Site            1542..1552
                     /site_type="active"
                     /note="nuclear localization signal [active]"
                     /db_xref="CDD:176027"
     CDS             1..1621
                     /gene="Pik3c2b"
                     /coded_by="NM_001105951.2:528..5393"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289021"
                     /db_xref="RGD:1306541"
ORIGIN      
        1 msstqgngeh wkslesvgis rkelamaeal qmeydalsrl rhhkeesrak qntepslisw
       61 depaldfysk pagrrtelkl lrglsgsdpt lnynsisppe elpnstsqdp qpgtdpwpkg
      121 sqsgdylyif dgsdgrcsls pvsgdtdgsc kklsppplpp rvsiwdappl pprkgspsps
      181 kisqpddins fslveqpsdk llgaqdpgeg elpngggqrh vlgsvdydgi ndaitrlnlk
      241 stydseilsd atrgwkegrg pldfskdtsg kpvarsktmp pqvpprtytp ryanrknatp
      301 gknrrisaap vssrthtvtn ghelfevsee rdeevaafch mldilrtgsd tqdysltgcv
      361 wstvtpspeh lgdevnlkvt vlcdslrepl tftcncsstv dlliyqtlcy thdelrevdv
      421 gdfvlkpcgl eeflqnkhal gsheyiqhcr kfdinirlql meqkairsdl artvnddqsp
      481 stlnylihlq erpvkqtisr qalsllfdty hnevdaflla egdfplkadr vvqsvkaicn
      541 alaavetpei tsalnqlppc psrmqpkiqk kvvealtaai ldlvelycst fnadfqtavp
      601 gsrkhdlvqe achfsgalaf tvygthripi iwatsyeefy lscslshggk elcsplqtrr
      661 ahfskylfhl iiwdqqicfp vqvnrlpret llcatlyalp ipppgsssea nkqkrvpeal
      721 gwvttplfnf rqvltcgrkl lglwpatqen ssarwsapnf hqpdsvilqi dfptsafdik
      781 ftsppgdkfs pryefgslre edqrklkdit qkeslywlsd adkkqlwekr yychtevssl
      841 plvlasapsw ewaclpdiya llqqwthmnh qdalgllhat fpdqevrrma vqwigslsda
      901 elldylpqlv qalkyecyld splvrfllkr aisdlrvthy ffwllkdslk dsqfsiryqy
      961 llaallcccg kglreefnrq cwlvntlakl aqqvreatps arqgilragl eevrqffaln
     1021 gscrlplsps llvkgivprd csyfnsnavp lklafqnvdp lgenirvifk cgddlrqdml
     1081 tlqmirimsk iwvqegldmr mvifrcfstg rgkgmvemip naetlrkiqv ehgvtgsfkd
     1141 rpladwlqkh npgedeyeka venfiyscag ccvatyilgi cdrhndniml kttghmfhid
     1201 fgrflghaqm fgnikrdrap fvftsdmayv inggdkpssr fhdfvdlccq aynlirkhth
     1261 lflnllglml scgipelsdl edlkyvydal rpqdteanat tyftrliess lgsvatklnf
     1321 fihnlaqmkf tgsddrltls faprthtlks sgrirdvflc rhekvfhpsk gyiyvvkvmr
     1381 enaheatyiq rtfeefqelh nklrllfpss flpsfpsrfv igrsrgeava errkeelngy
     1441 iwhlihaape vaecdlvytf fhplprdekt sgpspapkss dgtwarpvgk vggevklsis
     1501 yknnklfimv mhirglqplq dgsdpdpyvk iyllpdpqka tkrktkvark tcnptyneml
     1561 vydgipkgdl qqrelqlsvl seqgfwenvl lgevhirlre ldlaqektgw falgsrghgt
     1621 l
//
LOCUS       NP_001424000             599 aa            linear   ROD 26-MAR-2025
DEFINITION  transcription factor 4 isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424000 XP_038953101
VERSION     NP_001424000.1
DBSOURCE    REFSEQ: accession NM_001437071.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953101.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2160421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..599
                     /product="transcription factor 4 isoform 9"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=64285
     Region          65..>226
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          490..574
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(498,502,504..506,508,513,534..535)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(511..512,515..516,518..519,522,526,536,539,543,546,
                     549..554)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..599
                     /gene="Tcf4"
                     /coded_by="NM_001437071.1:132..1931"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mkdiffqflv arvrkrhsls clhtlpvvsp lrktergsys sygrenvqgc hqqsllggdm
       61 dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp ssvyapsast
      121 adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm lgnshipqss
      181 sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang tdsimanrgt
      241 gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw srnggqasss
      301 pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii gpshngamgs
      361 lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa tspdlnppqd
      421 pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik sitrsrssnn
      481 ddedltpeqk aerekerrma nnarerlrvr dineafkelg rmvqlhlksd kpqtkllilh
      541 qavavilsle qqvrernlnp kaaclkrree ekvssepppl slagphpgmg daanhmgqm
//
LOCUS       NP_001424015            1095 aa            linear   ROD 26-MAR-2025
DEFINITION  pumilio homolog 1 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424015 XP_063144110
VERSION     NP_001424015.1
DBSOURCE    REFSEQ: accession NM_001437086.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1095)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1095)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1095)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1095)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1095)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1095)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1095)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_063144110.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3025406.1,
                                           SRR26360194.1825152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1095
                     /product="pumilio homolog 1 isoform 11"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=116253
     Region          752..1073
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(808..809,812,844..845,848,881,884,916..917,920,
                     949..950,952..953,956,985..986,988..989,992,1028..1029,
                     1031..1032,1035,1065,1068)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1095
                     /gene="Pum1"
                     /coded_by="NM_001437086.1:114..3401"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgegprdad sdendkgekk nkgafdgdkl gdlkeegdvm
      181 dktnglpvqn gidadvkdfs rtpgncqssa nevdllgpnq ngseglaqlt stngakpved
      241 fsnmesqsvp ldpmehvgme plqfdysgtq vpvdsaaatv glfdynsqqq lfqrpnalav
      301 qqltaaqqqq yalaaahqph igmfpaglap aafvpnpyii saappgtdpy taglaaaatl
      361 gpavvphqyy gvtpwgvypa slfqqqaaaa aaatnsatqq sapqaqqgqq qvlrggasqr
      421 pltpnqnqqg qqtdplvaaa avnsalafgq glaagmpgyp vlapaayydq tgalvvnaga
      481 rnglgapvrl vapapviiss saaqaavaaa aasangaagg lagttngpfr plgtqqpqpq
      541 pqqqpsnnla sssfygnnsl ssnsqssslf sqgsaqpant slgfgssssl gatlgsalgg
      601 fgtavansnt gsgsrrdslt gssdlykrts sslapighsf ynslsfsssp gpvgmplpsq
      661 gpghsqtppp slsshgssss lnlggltngs gryisaapga eakyrsassa sslfspsstl
      721 fsssrlrygm sdvmpsgrsr lledfrnnry pnlqlreiag himefsqdqh gsrfiqlkle
      781 rataaerqlv fneilqaayq lmvdvfgnyv iqkffefgsh eqklalaeri rghvlslalq
      841 mygcrviqka lefipsdqqn emvreldghv lkcvkdqngn hvvqkciecv qpqslqfiid
      901 afkgqvfals thpygcrviq rilehclpdq tlpileelhq hteqlvqdqy gnyviqhvle
      961 hgrpedkski vaeirgnvlv lsqhkfasnv vekcvthasr teravlidev ctmndgphsa
     1021 lytmmkdqya nyvvqkmidv aepgqrkivm hkirphiatl rkytygkhil aklekyymkn
     1081 gvdlgpicgp pngii
//
LOCUS       NP_001017495             117 aa            linear   ROD 26-MAR-2025
DEFINITION  uncharacterized protein C4orf36 homolog [Rattus norvegicus].
ACCESSION   NP_001017495 XP_573553
VERSION     NP_001017495.1
DBSOURCE    REFSEQ: accession NM_001017495.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079214.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573553.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079214.1, CK598909.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..117
                     /product="uncharacterized protein C4orf36 homolog"
                     /note="AFF1 antisense RNA 1"
                     /calculated_mol_wt=13199
     Region          1..117
                     /region_name="DUF4522"
                     /note="Protein of unknown function (DUF4522); pfam15022"
                     /db_xref="CDD:434399"
     CDS             1..117
                     /gene="C14h4orf36"
                     /gene_synonym="Aff1-as1"
                     /coded_by="NM_001017495.1:325..678"
                     /db_xref="GeneID:498330"
                     /db_xref="RGD:1564576"
ORIGIN      
        1 mayglprrnt vqnilkgscy kiqepwdlae ltktwysnlt ninlpflgei afgspmnlla
       61 gqtkqdcplp smqtmaleke yeakrlaklk skenackemq vslreksvgl rrplqpk
//
LOCUS       NP_001423823             863 aa            linear   ROD 26-MAR-2025
DEFINITION  scm-like with four MBT domains protein 1 [Rattus norvegicus].
ACCESSION   NP_001423823 XP_063131750
VERSION     NP_001423823.1
DBSOURCE    REFSEQ: accession NM_001436894.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Zhang,J., Bonasio,R., Strino,F., Kluger,Y., Holloway,J.K.,
            Modzelewski,A.J., Cohen,P.E. and Reinberg,D.
  TITLE     SFMBT1 functions with LSD1 to regulate expression of canonical
            histone genes and chromatin-related factors
  JOURNAL   Genes Dev 27 (7), 749-766 (2013)
   PUBMED   23592795
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Lin,S., Shen,H., Li,J.L., Tang,S., Gu,Y., Chen,Z., Hu,C.,
            Rice,J.C., Lu,J. and Wu,L.
  TITLE     Proteomic and functional analyses reveal the role of chromatin
            reader SFMBT1 in regulating epigenetic silencing and the myogenic
            gene program
  JOURNAL   J Biol Chem 288 (9), 6238-6247 (2013)
   PUBMED   23349461
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Wu,S., Trievel,R.C. and Rice,J.C.
  TITLE     Human SFMBT is a transcriptional repressor protein that selectively
            binds the N-terminal tail of histone H3
  JOURNAL   FEBS Lett 581 (17), 3289-3296 (2007)
   PUBMED   17599839
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   5  (residues 1 to 863)
  AUTHORS   Usui,H., Ichikawa,T., Kobayashi,K. and Kumanishi,T.
  TITLE     Cloning of a novel murine gene Sfmbt, Scm-related gene containing
            four mbt domains, structurally belonging to the Polycomb group of
            genes
  JOURNAL   Gene 248 (1-2), 127-135 (2000)
   PUBMED   10806358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063131750.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.51910.1,
                                           SRR26643288.54981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..863
                     /product="scm-like with four MBT domains protein 1"
                     /note="Scm-related gene containing four mbt domains"
                     /calculated_mol_wt=97375
     Region          20..120
                     /region_name="MBT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          47..140
                     /region_name="MBT"
                     /note="malignant brain tumor (MBT) repeat; cl45897"
                     /db_xref="CDD:459242"
     Site            order(60,63,66,68,84,87,93)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439080"
     Region          128..232
                     /region_name="MBT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          159..255
                     /region_name="MBT_SFMBT1_rpt2"
                     /note="second malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20113"
                     /db_xref="CDD:439103"
     Site            order(172,175,178,180,196,199,205)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439103"
     Region          242..346
                     /region_name="MBT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          271..364
                     /region_name="MBT_SFMBT1_rpt3"
                     /note="third malignant brain tumor (MBT) repeat found in
                     Scm-like with four MBT domains protein 1 (SFMBT1);
                     cd20115"
                     /db_xref="CDD:439105"
     Region          354..451
                     /region_name="MBT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          380..469
                     /region_name="MBT"
                     /note="malignant brain tumor (MBT) repeat; cl45897"
                     /db_xref="CDD:459242"
     Site            order(392,395,398,400,416,419,424)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439080"
     Region          499..614
                     /region_name="SLED"
                     /note="SLED domain; pfam12140"
                     /db_xref="CDD:463469"
     Region          638..773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JMD2.2)"
     Region          779..863
                     /region_name="SAM_Scm-like-4MBT1,2"
                     /note="SAM domain of Scm-like-4MBT1,2 proteins of Polycomb
                     group; cd09581"
                     /db_xref="CDD:188980"
     Site            order(818..820,822..823,826..827,830..831,836)
                     /site_type="other"
                     /note="putative oligomer interface ML [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     Site            order(839..842,844..845,848,851)
                     /site_type="other"
                     /note="putative oligomer interface EH [polypeptide
                     binding]"
                     /db_xref="CDD:188980"
     CDS             1..863
                     /gene="Sfmbt1"
                     /gene_synonym="Sfmbt"
                     /coded_by="NM_001436894.1:360..2951"
                     /db_xref="GeneID:58967"
                     /db_xref="RGD:61999"
ORIGIN      
        1 mngeqqldad lgsgveveef swedyleetg attapyasfk hvdiclqsgf apgmkleval
       61 rkdpetywva tvitaceqll llryegyged rkadfwcdir raglypigwc qqnkktleap
      121 egirdkvsdw saflqrtltg acgppvalle glrngrnpld liapgsrlec qdfrdsvstw
      181 ivtvvenigg rlklqyegle rhdgfehwly yldpflhhig waaqqgyelq pplairhlkn
      241 eadwqeilar vkeeeplpsy lfkdkqvirt hefsinmkle avdpwspfgi spatiakvfd
      301 dkyflveidd lrpedharrs fvchanspgi fpvqwslkng lhinpppgfr sqdfdwadyl
      361 kqcgaeaapq kcfpqsvseh qfkenmklea vnplfpeevs iatvtavrgs ylwlqlegsk
      421 kpvpefivsv esmnifplgw cetnghplst prrarghklr kiavvqpekq ilssrtvheg
      481 lknqlnsphs vmingkyccp kiyfnhrcfs gpylnkgria elpqcvgpgn cvlvlrevlt
      541 llinaaykps rvlrelqldk dsvwhgcgev lkakykgksy ratveivrta drvtefcrqt
      601 cikleccpnl fgprmvldtc sencsvltkt kythyygkkk nkrigrppgg hsnlscalkk
      661 tskrrkrrkn ifvhkkkrss asvdntpvgs pqgsggeded daddgdddsl tegstseqqd
      721 elheesevse kkscspsptq semstplppd tqtdkreaqt sslsdgenkp pspkeiriev
      781 derlhldsnp lkwsvadvvr firstdcapl arifldqeid gqalllltlp tvqecmdlkl
      841 gpaiklchhi erikfafyeq fan
//
LOCUS       NP_001099463             596 aa            linear   ROD 26-MAR-2025
DEFINITION  glomulin [Rattus norvegicus].
ACCESSION   NP_001099463 XP_001057583 XP_213992
VERSION     NP_001099463.1
DBSOURCE    REFSEQ: accession NM_001105993.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Tron,A.E., Arai,T., Duda,D.M., Kuwabara,H., Olszewski,J.L.,
            Fujiwara,Y., Bahamon,B.N., Signoretti,S., Schulman,B.A. and
            DeCaprio,J.A.
  TITLE     The glomuvenous malformation protein Glomulin binds Rbx1 and
            regulates cullin RING ligase-mediated turnover of Fbw7
  JOURNAL   Mol Cell 46 (1), 67-78 (2012)
   PUBMED   22405651
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Krummrei,U., Baulieu,E.E. and Chambraud,B.
  TITLE     The FKBP-associated protein FAP48 is an antiproliferative molecule
            and a player in T cell activation that increases IL2 synthesis
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2444-2449 (2003)
   PUBMED   12604780
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Brouillard,P., Boon,L.M., Mulliken,J.B., Enjolras,O., Ghassibe,M.,
            Warman,M.L., Tan,O.T., Olsen,B.R. and Vikkula,M.
  TITLE     Mutations in a novel factor, glomulin, are responsible for
            glomuvenous malformations ('glomangiomas')
  JOURNAL   Am J Hum Genet 70 (4), 866-874 (2002)
   PUBMED   11845407
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Grisendi,S., Chambraud,B., Gout,I., Comoglio,P.M. and Crepaldi,T.
  TITLE     Ligand-regulated binding of FAP68 to the hepatocyte growth factor
            receptor
  JOURNAL   J Biol Chem 276 (49), 46632-46638 (2001)
   PUBMED   11571281
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Chambraud,B., Radanyi,C., Camonis,J.H., Shazand,K., Rajkowski,K.
            and Baulieu,E.E.
  TITLE     FAP48, a new protein that forms specific complexes with both
            immunophilins FKBP59 and FKBP12. Prevention by the
            immunosuppressant drugs FK506 and rapamycin
  JOURNAL   J Biol Chem 271 (51), 32923-32929 (1996)
   PUBMED   8955134
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474079.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057583.1, XP_213992.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389,
                              SAMN12840122 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..596
                     /product="glomulin"
                     /note="FKBP associated protein"
                     /calculated_mol_wt=67448
     Region          1..524
                     /region_name="Kinetochor_Ybp2"
                     /note="Uncharacterized protein family, YAP/Alf4/glomulin;
                     pfam08568"
                     /db_xref="CDD:400745"
     CDS             1..596
                     /gene="Glmn"
                     /coded_by="NM_001105993.1:115..1905"
                     /db_xref="GeneID:289437"
                     /db_xref="RGD:1588600"
ORIGIN      
        1 maveelqcii krcqileehd fkeedfglfq lagqrciedg yinqlleiiq deknktiikt
       61 mgwnlvgpvv rcllrgreed kreecflifd llvklcnpke lllgllelie epsgkqisqi
      121 illllqplqt viqklpnnka ysaglalstl wsqlsllpvp hseeqiqadd yglcqccral
      181 ieftkpfvae vasdkedpan tklkdellkf cfkslkcpll taqfleqsee vgndpfrcfa
      241 seiigflsqi gypvpqiiln hgrkkrtwdy lefeeeedrq ladsvaalty lvfvqgigtd
      301 qlpmvlspsy llqlnmehie vllqrteqsv yskglellet sllrlednsl cyqyleiksf
      361 lavpqglvkv mtlcpietlr ktglamlqly idkldsqgky tlfrcllnts nhsgveafvi
      421 qniknqidls ykkthnrwfa gaqltslldl vlslpegaet dllqnsdrim aslnllrylv
      481 ikdneddnqt glwtelgkie nnflqplhvg lnmskahyea eiknsqqnsq aasmcksvcs
      541 vtvggeeipt mppemqlkvl hsalftfdli esvlarveel ieikskstse enagmk
//
LOCUS       NP_001423863             164 aa            linear   ROD 26-MAR-2025
DEFINITION  C-C motif chemokine 27 isoform a [Rattus norvegicus].
ACCESSION   NP_001423863 XP_006238139
VERSION     NP_001423863.1
DBSOURCE    REFSEQ: accession NM_001436934.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Maerki,C., Meuter,S., Liebi,M., Muhlemann,K., Frederick,M.J.,
            Yawalkar,N., Moser,B. and Wolf,M.
  TITLE     Potent and broad-spectrum antimicrobial activity of CXCL14 suggests
            an immediate role in skin infections
  JOURNAL   J Immunol 182 (1), 507-514 (2009)
   PUBMED   19109182
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Baumer,W., Seegers,U., Braun,M., Tschernig,T. and Kietzmann,M.
  TITLE     TARC and RANTES, but not CTACK, are induced in two models of
            allergic contact dermatitis. Effects of cilomilast and diflorasone
            diacetate on T-cell-attracting chemokines
  JOURNAL   Br J Dermatol 151 (4), 823-830 (2004)
   PUBMED   15491423
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Kakinuma,T., Saeki,H., Tsunemi,Y., Fujita,H., Asano,N., Mitsui,H.,
            Tada,Y., Wakugawa,M., Watanabe,T., Torii,H., Komine,M., Asahina,A.,
            Nakamura,K. and Tamaki,K.
  TITLE     Increased serum cutaneous T cell-attracting chemokine (CCL27)
            levels in patients with atopic dermatitis and psoriasis vulgaris
  JOURNAL   J Allergy Clin Immunol 111 (3), 592-597 (2003)
   PUBMED   12642842
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Hieshima,K., Ohtani,H., Shibano,M., Izawa,D., Nakayama,T.,
            Kawasaki,Y., Shiba,F., Shiota,M., Katou,F., Saito,T. and Yoshie,O.
  TITLE     CCL28 has dual roles in mucosal immunity as a chemokine with
            broad-spectrum antimicrobial activity
  JOURNAL   J Immunol 170 (3), 1452-1461 (2003)
   PUBMED   12538707
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Gortz,A., Nibbs,R.J., McLean,P., Jarmin,D., Lambie,W., Baird,J.W.
            and Graham,G.J.
  TITLE     The chemokine ESkine/CCL27 displays novel modes of intracrine and
            paracrine function
  JOURNAL   J Immunol 169 (3), 1387-1394 (2002)
   PUBMED   12133963
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Jarmin,D.I., Rits,M., Bota,D., Gerard,N.P., Graham,G.J.,
            Clark-Lewis,I. and Gerard,C.
  TITLE     Cutting edge: identification of the orphan receptor
            G-protein-coupled receptor 2 as CCR10, a specific receptor for the
            chemokine ESkine
  JOURNAL   J Immunol 164 (7), 3460-3464 (2000)
   PUBMED   10725696
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Morales,J., Homey,B., Vicari,A.P., Hudak,S., Oldham,E., Hedrick,J.,
            Orozco,R., Copeland,N.G., Jenkins,N.A., McEvoy,L.M. and Zlotnik,A.
  TITLE     CTACK, a skin-associated chemokine that preferentially attracts
            skin-homing memory T cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (25), 14470-14475 (1999)
   PUBMED   10588729
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Baird,J.W., Nibbs,R.J., Komai-Koma,M., Connolly,J.A.,
            Ottersbach,K., Clark-Lewis,I., Liew,F.Y. and Graham,G.J.
  TITLE     ESkine, a novel beta-chemokine, is differentially spliced to
            produce secretable and nuclear targeted isoforms
  JOURNAL   J Biol Chem 274 (47), 33496-33503 (1999)
   PUBMED   10559234
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006238139.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF978637.1, SRR26360181.2112375.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..164
                     /product="C-C motif chemokine 27 isoform a"
                     /note="C-C motif chemokine 27; chemokine (C-C motif)
                     ligand 27"
                     /calculated_mol_wt=19360
     Region          76..136
                     /region_name="IL8"
                     /note="Small cytokines (intecrine/chemokine),
                     interleukin-8 like; pfam00048"
                     /db_xref="CDD:459650"
     CDS             1..164
                     /gene="Ccl27"
                     /coded_by="NM_001436934.1:93..587"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:362505"
                     /db_xref="RGD:1304660"
ORIGIN      
        1 msrlrryeva leaeeeiywg cfyffpwlrm wrrerspmpp tsqrlslepp rlpltgwhpw
       61 nktkekqeal plpsstscct qlyrqplptr llrrivrvel qeadgdchlq avvlhltrrs
      121 vcvhpqnrsl arwlerhgkr lqgtlpslnp vlqkkmcpsp qkqk
//
LOCUS       NP_001423831            1909 aa            linear   ROD 26-MAR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase F isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001423831 XP_038966087
VERSION     NP_001423831.1
DBSOURCE    REFSEQ: accession NM_001436902.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1909)
  AUTHORS   Dyck,S., Kataria,H., Akbari-Kelachayeh,K., Silver,J. and
            Karimi-Abdolrezaee,S.
  TITLE     LAR and PTPsigma receptors are negative regulators of
            oligodendrogenesis and oligodendrocyte integrity in spinal cord
            injury
  JOURNAL   Glia 67 (1), 125-145 (2019)
   PUBMED   30394599
  REMARK    GeneRIF: In a spinal cord injury model, blocking LAR and PTPalpha
            receptors promotes oligodendrogenesis.
REFERENCE   2  (residues 1 to 1909)
  AUTHORS   Shijo,T., Warita,H., Suzuki,N., Kitajima,Y., Ikeda,K., Akiyama,T.,
            Ono,H., Mitsuzawa,S., Nishiyama,A., Izumi,R. and Aoki,M.
  TITLE     Aberrant astrocytic expression of chondroitin sulfate proteoglycan
            receptors in a rat model of amyotrophic lateral sclerosis
  JOURNAL   J Neurosci Res 96 (2), 222-233 (2018)
   PUBMED   28752900
  REMARK    GeneRIF: This study showed that astrocytes aberrantly and
            progressively expressed PTPsigma and LAR at the site of motor
            neuron degeneration in Tg ALS model rats with mutant SOD1.
REFERENCE   3  (residues 1 to 1909)
  AUTHORS   Choi,Y., Nam,J., Whitcomb,D.J., Song,Y.S., Kim,D., Jeon,S.,
            Um,J.W., Lee,S.G., Woo,J., Kwon,S.K., Li,Y., Mah,W., Kim,H.M.,
            Ko,J., Cho,K. and Kim,E.
  TITLE     SALM5 trans-synaptically interacts with LAR-RPTPs in a
            splicing-dependent manner to regulate synapse development
  JOURNAL   Sci Rep 6, 26676 (2016)
   PUBMED   27225731
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1909)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
REFERENCE   5  (residues 1 to 1909)
  AUTHORS   Song,Y.S., Lee,H.J., Prosselkov,P., Itohara,S. and Kim,E.
  TITLE     Trans-induced cis interaction in the tripartite NGL-1, netrin-G1
            and LAR adhesion complex promotes development of excitatory
            synapses
  JOURNAL   J Cell Sci 126 (Pt 21), 4926-4938 (2013)
   PUBMED   23986473
REFERENCE   6  (residues 1 to 1909)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Increased abundance of specific skeletal muscle protein-tyrosine
            phosphatases in a genetic model of insulin-resistant obesity and
            diabetes mellitus
  JOURNAL   Metabolism 44 (9), 1175-1184 (1995)
   PUBMED   7666792
REFERENCE   7  (residues 1 to 1909)
  AUTHORS   Ahmad,F., Considine,R.V. and Goldstein,B.J.
  TITLE     Increased abundance of the receptor-type protein-tyrosine
            phosphatase LAR accounts for the elevated insulin receptor
            dephosphorylating activity in adipose tissue of obese human
            subjects
  JOURNAL   J Clin Invest 95 (6), 2806-2812 (1995)
   PUBMED   7769120
REFERENCE   8  (residues 1 to 1909)
  AUTHORS   Ahmad,F. and Goldstein,B.J.
  TITLE     Purification, identification and subcellular distribution of three
            predominant protein-tyrosine phosphatase enzymes in skeletal muscle
            tissue
  JOURNAL   Biochim Biophys Acta 1248 (1), 57-69 (1995)
   PUBMED   7711057
REFERENCE   9  (residues 1 to 1909)
  AUTHORS   Pot,D.A., Woodford,T.A., Remboutsika,E., Haun,R.S. and Dixon,J.E.
  TITLE     Cloning, bacterial expression, purification, and characterization
            of the cytoplasmic domain of rat LAR, a receptor-like protein
            tyrosine phosphatase
  JOURNAL   J Biol Chem 266 (29), 19688-19696 (1991)
   PUBMED   1918076
REFERENCE   10 (residues 1 to 1909)
  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.
  TITLE     A new member of the immunoglobulin superfamily that has a
            cytoplasmic region homologous to the leukocyte common antigen
  JOURNAL   J Exp Med 168 (5), 1523-1530 (1988)
   PUBMED   2972792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966087.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.14188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1909
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1909
                     /product="receptor-type tyrosine-protein phosphatase F
                     isoform 1 precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase F;
                     leukocyte antigen-related (LAR) PTP receptor; leukocyte
                     common antigen related"
                     /calculated_mol_wt=209670
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2941
     Region          33..124
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          136..226
                     /region_name="IgI_2_RPTP_IIa_LAR_like"
                     /note="Second immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F; member of
                     the I-set of IgSF domains; cd05738"
                     /db_xref="CDD:409400"
     Region          136..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409400"
     Region          143..147
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409400"
     Region          150..159
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409400"
     Region          164..170
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409400"
     Region          172..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409400"
     Region          183..187
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409400"
     Region          190..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409400"
     Region          204..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409400"
     Region          214..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409400"
     Region          235..316
                     /region_name="IgI_3_RPTP_IIa_LAR_like"
                     /note="Third immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F (also known
                     as LAR), type IIa; member of the I-set of IgSF domains;
                     cd05739"
                     /db_xref="CDD:409401"
     Region          235..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409401"
     Region          241..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409401"
     Region          248..256
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409401"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          261..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409401"
     Region          269..271
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409401"
     Region          274..278
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409401"
     Region          283..288
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409401"
     Region          288..712
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          295..302
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409401"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          306..315
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409401"
     Region          592..1050
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          693..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            941
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            957
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1255..1275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64604.1)"
     Site            1296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10586; propagated from
                     UniProtKB/Swiss-Prot (Q64604.1)"
     Region          1337..1612
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1614..1904
                     /region_name="R-PTP-F-2"
                     /note="PTP-like domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 2; cd14629"
                     /db_xref="CDD:350477"
     CDS             1..1909
                     /gene="Ptprf"
                     /gene_synonym="LARFN5C"
                     /coded_by="NM_001436902.1:313..6042"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:360406"
                     /db_xref="RGD:3453"
ORIGIN      
        1 mapepapgrr mvplvpalvm lglmagahgd skpvfvkvpe dqiglsggva sfvcqatgep
       61 kpritwmkkg kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa
      121 klsvleedql psgfptidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpass
      181 ngrikqlrsg alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss
      241 qevmpggnvn ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv mrsanytcva
      301 isslgmieat aqvtvkalpk ppidlvvtet tatsvtltwd sgntepvsfy giqyraagtd
      361 gpfqevdgva strysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv
      421 qarmlsastm lvqweppeep nglvrgyrvy ytpdsrrpls awhkhntdag llttvgsllp
      481 gityslrvla ftavgdgpps ptiqvktqqg vpaqpadfqa kaesdtriql swllppqeri
      541 ikyelvywaa edegqqhkvt fdptssytle dlkpdtlyhf qlaarsdlgv gvftptvear
      601 taqstpsapp qkvtcvstgs ttvrvswvpp padsrngiit qysvayeavd gedrkrhvvd
      661 gisrehsswd llglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl
      721 nstavhvswk lpvpnkqhgq irgyqvtyvr lengeprgqp iiqdvmlaea qettisgltp
      781 ettysitvaa yttkgdgars kpkvvtttga vpgrptmmvs ttamhtallq whppkelpge
      841 llgyrlqyrr adearpntid fgkddqhftv tglhkgatyi frlaaknrag pgeefekeit
      901 tpedapsgfp qnlrvtgltt sttelawdpp vlaerngrit nytvvyrdin sqhelqnvtg
      961 dvhltllglk pdttydikvr ahtskgagpl spsiqsqtmp meqvfaknfr vaaamktsvl
     1021 lswevpdsyk savpfkilyn gqsvevdghs mrkliadlqp nteysfvlmn rgssagglqh
     1081 lvsirtapdl lpqkplpasa fiedgrfsls mpqvqdpslv rwfyivvvpi drvggnllap
     1141 rwstpeelel delleaieqg eekqrrrrrq aerlkpyvaa qvdelpetft lgdkknyrgf
     1201 ynrplspdls yqcfvlaslk epmdqkryas spysdeivvq vtpaqqqeep emlwvtgpvl
     1261 aviliilivi aillfkrkrt hspsskdeqs iglkdsllah ssdpvemrrl nyqtpgssap
     1321 scpnissmrd hppipitdla dnierlkand glkfsqeyes idpgqqftwe nsnsevnkpk
     1381 nryanviayd hsrvlltsid gvpgsdyina nyidgyrkqn ayiatqgplp etmgdfwrmv
     1441 weqrtatvvm mtrleeksrv kcdqywparg tetygliqvt lvdtvelaty tmrtfalhks
     1501 gssekrelrq fqfmawpdhg vpeyptpila flrrvkacnp ldagpmvvhc sagvgrtgcf
     1561 ividamlerm khektvdiyg hvtcmrsqrn ymvqtedqyv fihealleaa mcghtevlar
     1621 nlyahiqklg qvppgesvta melefkllan skahtsrfis anlpcnkfkn rlvnimpyel
     1681 trvclqpirg vegsdyinas fldgyrqqka yiatqgplae stedfwrmlw ehnstiivml
     1741 tklremgrek chqywpaers aryqyfvvdp maeynmpqyi lrefkvtdar dgqsrtirqf
     1801 qftdwpeqgv pktgegfidf igqvhktkeq fgqdgpitvh csagvgrtgv fitlsivler
     1861 mryegvvdmf qtvktlrtqr pamvqtedqy qlcyraaley lgsfdhyat
//
LOCUS       NP_001423837             525 aa            linear   ROD 26-MAR-2025
DEFINITION  thymocyte selection-associated high mobility group box protein TOX
            [Rattus norvegicus].
ACCESSION   NP_001423837 XP_038966143
VERSION     NP_001423837.1
DBSOURCE    REFSEQ: accession NM_001436908.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Artegiani,B., de Jesus Domingues,A.M., Bragado Alonso,S.,
            Brandl,E., Massalini,S., Dahl,A. and Calegari,F.
  TITLE     Tox: a multifunctional transcription factor and novel regulator of
            mammalian corticogenesis
  JOURNAL   EMBO J 34 (7), 896-910 (2015)
   PUBMED   25527292
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Yun,S., Lee,S.H., Yoon,S.R., Kim,M.S., Piao,Z.H., Myung,P.K.,
            Kim,T.D., Jung,H. and Choi,I.
  TITLE     TOX regulates the differentiation of human natural killer cells
            from hematopoietic stem cells in vitro
  JOURNAL   Immunol Lett 136 (1), 29-36 (2011)
   PUBMED   21126536
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Aliahmad,P., de la Torre,B. and Kaye,J.
  TITLE     Shared dependence on the DNA-binding factor TOX for the development
            of lymphoid tissue-inducer cell and NK cell lineages
  JOURNAL   Nat Immunol 11 (10), 945-952 (2010)
   PUBMED   20818394
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Aliahmad,P. and Kaye,J.
  TITLE     Development of all CD4 T lineages requires nuclear factor TOX
  JOURNAL   J Exp Med 205 (1), 245-256 (2008)
   PUBMED   18195075
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Aliahmad,P., O'Flaherty,E., Han,P., Goularte,O.D., Wilkinson,B.,
            Satake,M., Molkentin,J.D. and Kaye,J.
  TITLE     TOX provides a link between calcineurin activation and CD8 lineage
            commitment
  JOURNAL   J Exp Med 199 (8), 1089-1099 (2004)
   PUBMED   15078895
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Wilkinson,B., Chen,J.Y., Han,P., Rufner,K.M., Goularte,O.D. and
            Kaye,J.
  TITLE     TOX: an HMG box protein implicated in the regulation of thymocyte
            selection
  JOURNAL   Nat Immunol 3 (3), 272-280 (2002)
   PUBMED   11850626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966143.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.20913.1,
                                           SRR26643288.21413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..525
                     /product="thymocyte selection-associated high mobility
                     group box protein TOX"
                     /note="thymocyte selection-associated HMG box"
                     /calculated_mol_wt=57155
     Region          262..331
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(262..263,265..269,272..273,280,292..293,296,
                     299..300,307,311,314,318,321)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..525
                     /gene="Tox"
                     /coded_by="NM_001436908.1:343..1920"
                     /db_xref="GeneID:362481"
                     /db_xref="RGD:1310455"
ORIGIN      
        1 mdvrfypppa qpaaapaapc lgpspcldpy ycnkfdgenm ymsmtepsqd yvpvsqsypg
       61 pslesedfni ppitppslpd hslvhlneve sgyhslchpm nhngllpfhp qnmdlpeitv
      121 snmlgqdgtl lsnsisvmqe ignaegaqys shpqlaamrp rgqptdlrqq asmmqhgqlt
      181 tinqsqlsaq lglnmggtnv phnspsppgs ksatpspsss vhedecedts kinggekrpa
      241 sdmgkkpktp kkkkkkdpne pqkpvsayal ffrdtqaaik gqnpnatfge vskivasmwd
      301 glgeeqkqvy kkkteaakke ylkqlaayra slvsksyndp vdvktsqppq lvnskpsvfh
      361 gpsqahsaly lsshyhqqpg mtpqltamhp slprniapkp nnqmpvtvsi anmavspppp
      421 lqispplhqh lsmqqhqplv qqplasqlpm qvqtalhspt mqqgftlqpd yqtiinptst
      481 aaqvvtqame yvrsgcrnpp pqpvdwstdy cssggmqrdk alylt
//
LOCUS       NP_001423779             446 aa            linear   ROD 26-MAR-2025
DEFINITION  probable tRNA methyltransferase 9B [Rattus norvegicus].
ACCESSION   NP_001423779 XP_006253284
VERSION     NP_001423779.1
DBSOURCE    REFSEQ: accession NM_001436850.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Begley,U., Sosa,M.S., Avivar-Valderas,A., Patil,A., Endres,L.,
            Estrada,Y., Chan,C.T., Su,D., Dedon,P.C., Aguirre-Ghiso,J.A. and
            Begley,T.
  TITLE     A human tRNA methyltransferase 9-like protein prevents tumour
            growth by regulating LIN9 and HIF1-alpha
  JOURNAL   EMBO Mol Med 5 (3), 366-383 (2013)
   PUBMED   23381944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006253284.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.71730.1,
                                           SRR26360186.2699504.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..446
                     /product="probable tRNA methyltransferase 9B"
                     /calculated_mol_wt=49925
     Region          30..143
                     /region_name="UbiE"
                     /note="Ubiquinone/menaquinone biosynthesis C-methylase
                     UbiE/MenG [Coenzyme transport and metabolism]; COG2226"
                     /db_xref="CDD:441828"
     CDS             1..446
                     /gene="Trmt9b"
                     /gene_synonym="RGD1304810"
                     /coded_by="NM_001436850.1:733..2073"
                     /db_xref="GeneID:306504"
                     /db_xref="RGD:1304810"
ORIGIN      
        1 mdpeavqlek qhvhkvyest apyfsdlqnk awprvrqflq dqkpgsliad igcgtgkylk
       61 vnsqvhtlgc dycgplveia rnrgcevmvc dnlnlpfrdq gfdaiisigv ihhfstkqrr
      121 iraikemarv lapggqlmiy vwameqknrh fekqdvlvpw nralcsrlls eshqswghsc
      181 ehptsqgyqg pgsacscavc fkgrcdskrs hsmdygpava rtcceaiske gqqenglysn
      241 fgksfrswff srsldestlr kqiervrpmk iegwanstvs hqpsrypsvd lhaqepfstk
      301 rpnldevfvd assqrhvgcl gvpstsdnfi ghkggesrrk eggnfldttd tgnsvaarng
      361 gdrsarkilr rvsafdstds tsedpsfveg qqdgpdskaf mryyhvfreg elssllqecv
      421 selqvlssgn dhgnwciiae kkrswd
//
LOCUS       NP_001423842             604 aa            linear   ROD 26-MAR-2025
DEFINITION  protein CBFA2T1 isoform a [Rattus norvegicus].
ACCESSION   NP_001423842 XP_006237963
VERSION     NP_001423842.1
DBSOURCE    REFSEQ: accession NM_001436913.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Indjeian,V.B., Kingman,G.A., Jones,F.C., Guenther,C.A.,
            Grimwood,J., Schmutz,J., Myers,R.M. and Kingsley,D.M.
  TITLE     Evolving New Skeletal Traits by cis-Regulatory Changes in Bone
            Morphogenetic Proteins
  JOURNAL   Cell 164 (1-2), 45-56 (2016)
   PUBMED   26774823
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Linqing,Z., Guohua,J., Haoming,L., Xuelei,T., Jianbing,Q. and
            Meiling,T.
  TITLE     Runx1t1 regulates the neuronal differentiation of radial glial
            cells from the rat hippocampus
  JOURNAL   Stem Cells Transl Med 4 (1), 110-116 (2015)
   PUBMED   25473084
  REMARK    GeneRIF: We have concluded that Runx1t1 could be involved in the
            process through which radial glial cells differentiate into neurons
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Barrett,C.W., Smith,J.J., Lu,L.C., Markham,N., Stengel,K.R.,
            Short,S.P., Zhang,B., Hunt,A.A., Fingleton,B.M., Carnahan,R.H.,
            Engel,M.E., Chen,X., Beauchamp,R.D., Wilson,K.T., Hiebert,S.W.,
            Reynolds,A.B. and Williams,C.S.
  TITLE     Kaiso directs the transcriptional corepressor MTG16 to the Kaiso
            binding site in target promoters
  JOURNAL   PLoS One 7 (12), e51205 (2012)
   PUBMED   23251453
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Kim,Y.R., Kim,M.S., Lee,S.H. and Yoo,N.J.
  TITLE     Mutational analysis of RUNX1T1 gene in acute leukemias, breast and
            lung carcinomas
  JOURNAL   Leuk Res 35 (9), e157-e158 (2011)
   PUBMED   21571369
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Rochford,J.J., Semple,R.K., Laudes,M., Boyle,K.B.,
            Christodoulides,C., Mulligan,C., Lelliott,C.J., Schinner,S.,
            Hadaschik,D., Mahadevan,M., Sethi,J.K., Vidal-Puig,A. and
            O'Rahilly,S.
  TITLE     ETO/MTG8 is an inhibitor of C/EBPbeta activity and a regulator of
            early adipogenesis
  JOURNAL   Mol Cell Biol 24 (22), 9863-9872 (2004)
   PUBMED   15509789
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Wood,J.D., Nucifora,F.C. Jr., Duan,K., Zhang,C., Wang,J., Kim,Y.,
            Schilling,G., Sacchi,N., Liu,J.M. and Ross,C.A.
  TITLE     Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene
            product, interacts with ETO/MTG8 in the nuclear matrix and
            represses transcription
  JOURNAL   J Cell Biol 150 (5), 939-948 (2000)
   PUBMED   10973986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006237963.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2210231.1,
                                           SRR26360194.2413634.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..604
                     /product="protein CBFA2T1 isoform a"
                     /note="CBFA2T1 identified gene homolog; core-binding
                     factor, runt domain, alpha subunit 2; translocated to, 1;
                     cyclin D-related; RUNX1 translocation partner 1; acute
                     myelogenous leukemia 1 translocation 1 protein; protein
                     CBFA2T1; core-binding factor, runt domain, alpha subunit
                     2, translocated to, 1; runt-related transcription factor
                     1; translocated to, 1 (cyclin D-related)"
                     /calculated_mol_wt=67376
     Region          122..211
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Region          337..403
                     /region_name="NHR2"
                     /note="NHR2 domain like; pfam08788"
                     /db_xref="CDD:430219"
     Region          443..>497
                     /region_name="NtpE"
                     /note="Archaeal/vacuolar-type H+-ATPase subunit E/Vma4
                     [Energy production and conversion]; COG1390"
                     /db_xref="CDD:441000"
     Region          515..551
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..604
                     /gene="Runx1t1"
                     /gene_synonym="Cbfa2t1"
                     /coded_by="NM_001436913.1:453..2267"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:362489"
                     /db_xref="RGD:1305490"
ORIGIN      
        1 misikrntwr alsvvigdcr kkanfeycqd rtekhstmpd spvdvktqsr ltppampppp
       61 ttqgaprtss ftpttltngt shsptalnga psppngfsng psssssssla nqqlppacga
      121 rqlsklkrfl ttlqqfgndi speigervrt lvlglvnstl tieefhsklq eatnfplrpf
      181 vipflkanlp llqrellhca rlakqnpaqy laqheqllld asttspvdss ellldvneng
      241 krrtpdrtke ngfdreplhs ehpskrpcti spgqryspnn glsyqpnglp hptppppqhy
      301 rlddmaiahh yrdsyrhpsh rdlrdrnrpm glhgtrqeem idhrltdrew aeewkhldhl
      361 lncimdmvek trrsltvlrr cqeadreeln ywirrysdae dlkkggsgss shsrqqspvn
      421 pdpvaldahr eflhrpasgy vpeeiwkkae eavnevkrqa mtelqkavse aerkahdmit
      481 terakmertv aeakrqaaed alavinqqed ssescwncgr kasetcsgcn tarycgsfcq
      541 hkdwekhhhi cgqtlqapqq getpavsssv tpssgagspm dtppaatprs ttpgtpstie
      601 ttpr
//
LOCUS       NP_001100704             379 aa            linear   ROD 26-MAR-2025
DEFINITION  RING finger protein 215 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001100704 XP_001065855 XP_223565
VERSION     NP_001100704.1
DBSOURCE    REFSEQ: accession NM_001107234.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223565.2, XP_001065855.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.564712.1,
                                           SRR22582424.110341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..379
                     /product="RING finger protein 215 isoform 1 precursor"
                     /calculated_mol_wt=37081
     sig_peptide     1..45
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4517
     Region          325..374
                     /region_name="RING-H2_RNF215"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 215 (RNF215) and similar proteins; cd16670"
                     /db_xref="CDD:438332"
     CDS             1..379
                     /gene="Rnf215"
                     /gene_synonym="RGD1310738"
                     /coded_by="NM_001107234.2:65..1204"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:305478"
                     /db_xref="RGD:1310738"
ORIGIN      
        1 mgpadrpalr spssppppps ppsplllllp llplwlglmg pgaaadgsep earagrggar
       61 avrvdvklpr qdalvlegvr igseaspepl lggrlllmdv vdaeqeipad gwiavayvgk
      121 eqvaqfhqen qgssqkaypk alvqqmrral flgasallll ilnhsvvrel disqlllrpv
      181 ivlhyssnvt klleallqrt qataeissge slsaniewkl tlwttcglsk dgyggwqdlv
      241 clggaqaqeq kplqqlwnai llvvmllctg lvvqaqrqas rqsqqepggq edlfkrrvvr
      301 rlaslktrrc rlsraahslp epgaetcavc ldyfcnkqwl rvlpckhefh rdcvdpwlml
      361 qqtcplckfn vlgnhysdd
//
LOCUS       NP_001423877             514 aa            linear   ROD 26-MAR-2025
DEFINITION  DNA-binding protein Ikaros isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423877
VERSION     NP_001423877.1
DBSOURCE    REFSEQ: accession NM_001436948.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Young,G.P., Symonds,E.L., Nielsen,H.J., Ferm,L., Christensen,I.J.,
            Dekker,E., van der Vlugt,M., Mallant-Hent,R.C., Boulter,N., Yu,B.,
            Chan,M., Tevz,G., LaPointe,L.C. and Pedersen,S.K.
  TITLE     Evaluation of a panel of tumor-specific differentially-methylated
            DNA regions in IRF4, IKZF1 and BCAT1 for blood-based detection of
            colorectal cancer
  JOURNAL   Clin Epigenetics 13 (1), 14 (2021)
   PUBMED   33478584
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Sharma,B., Shah,R., Jamwal,R.S., Verma,S., Bhat,A., Bhat,G.R.,
            Bakshi,D., Singh,S., Angurana,S., Bhat,A., Vaishnavi,S. and
            Kumar,R.
  TITLE     Evaluation of newly identified Ikaros family zinc finger 1 loci in
            colorectal cancer
  JOURNAL   J Cancer Res Ther 17 (1), 46-50 (2021)
   PUBMED   33723131
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Musher,B.L., Melson,J.E., Amato,G., Chan,D., Hill,M., Khan,I.,
            Kochuparambil,S.T., Lyons,S.E., Orsini,J. Jr., Pedersen,S.K.,
            Robb,B., Saltzman,J., Silinsky,J., Gaur,S., Tuck,M.K.,
            LaPointe,L.C. and Young,G.P.
  TITLE     Evaluation of Circulating Tumor DNA for Methylated BCAT1 and IKZF1
            to Detect Recurrence of Stage II/Stage III Colorectal Cancer (CRC)
  JOURNAL   Cancer Epidemiol Biomarkers Prev 29 (12), 2702-2709 (2020)
   PUBMED   32958500
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Zhao,W., Chen,T.B. and Wang,H.
  TITLE     Ikaros is heterogeneously expressed in lung adenocarcinoma and is
            involved in its progression
  JOURNAL   J Int Med Res 48 (8), 300060520945860 (2020)
   PUBMED   32787735
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Symonds,E.L., Pedersen,S.K., Murray,D., Byrne,S.E., Roy,A.,
            Karapetis,C., Hollington,P., Rabbitt,P., Jones,F.S., LaPointe,L.,
            Segelov,E. and Young,G.P.
  TITLE     Circulating epigenetic biomarkers for detection of recurrent
            colorectal cancer
  JOURNAL   Cancer 126 (7), 1460-1469 (2020)
   PUBMED   31909823
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Honma,Y., Kiyosawa,H., Mori,T., Oguri,A., Nikaido,T., Kanazawa,K.,
            Tojo,M., Takeda,J., Tanno,Y., Yokoya,S., Kawabata,I., Ikeda,H. and
            Wanaka,A.
  TITLE     Eos: a novel member of the Ikaros gene family expressed
            predominantly in the developing nervous system
  JOURNAL   FEBS Lett 447 (1), 76-80 (1999)
   PUBMED   10218586
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Kelley,C.M., Ikeda,T., Koipally,J., Avitahl,N., Wu,L.,
            Georgopoulos,K. and Morgan,B.A.
  TITLE     Helios, a novel dimerization partner of Ikaros expressed in the
            earliest hematopoietic progenitors
  JOURNAL   Curr Biol 8 (9), 508-515 (1998)
   PUBMED   9560339
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Boggs,S.S., Trevisan,M., Patrene,K. and Geogopoulos,K.
  TITLE     Lack of natural killer cell precursors in fetal liver of Ikaros
            knockout mutant mice
  JOURNAL   Nat Immun 16 (4), 137-145 (1998)
   PUBMED   10366784
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Molnar,A. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of functionally diverse zinc
            finger DNA-binding proteins
  JOURNAL   Mol Cell Biol 14 (12), 8292-8303 (1994)
   PUBMED   7969165
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Georgopoulos,K., Bigby,M., Wang,J.H., Molnar,A., Wu,P., Winandy,S.
            and Sharpe,A.
  TITLE     The Ikaros gene is required for the development of all lymphoid
            lineages
  JOURNAL   Cell 79 (1), 143-156 (1994)
   PUBMED   7923373
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.44182.1,
                                           SRR26643292.52728.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..514
                     /product="DNA-binding protein Ikaros isoform 2"
                     /note="DNA-binding protein Ikaros"
                     /calculated_mol_wt=56916
     Region          117..137
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(122,124,126,128..129,132..133,136,150,152,156..157,
                     160..161,164,178,180,182,184..185,188..189,192)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          130..154
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          141..>420
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          145..165
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          157..182
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          173..193
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          201..222
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..514
                     /gene="Ikzf1"
                     /gene_synonym="RGD1562979"
                     /coded_by="NM_001436948.1:66..1610"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305501"
                     /db_xref="RGD:1562979"
ORIGIN      
        1 mdvdegqdms qvsgkesppv sdtpdegdep mpvpedlsts gaqqnsksdr gmasnvkvet
       61 qsdeengrac emngecaedl rmldasgekm ngshrdqgst alsgvggirl pngklkcdic
      121 givcigpnvl mvhkrshtge rpfqcnqcga sftqkgnllr hiklhsgekp fkchlcnyac
      181 rrrdaltghl rthsvgkphk cgycgrsykq rssleehker chnylesmgl pgmypvikee
      241 tnhsemaedl ckigaerslv ldrlasnvak rkssmpqkfl gdkclsdmpy dsanyekdem
      301 mtshvmdqai nnainylgae slrplvqtpp gssevvpvis smyqlhkpps dgpprsnhsa
      361 qdsavenlll lskaksvsse reaspsnscq dstdtesnae eqrsgliylt nhitpharng
      421 lalkeeqray evlraasens qdafrvvsts geqlkvykce hcrvlfldhv mytihmgchg
      481 frdpfecnmc gyhsqdryef sshitrgehr yhls
//
LOCUS       NP_001423828             277 aa            linear   ROD 26-MAR-2025
DEFINITION  caspase-3 [Rattus norvegicus].
ACCESSION   NP_001423828 XP_006253192
VERSION     NP_001423828.1
DBSOURCE    REFSEQ: accession NM_001436899.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Niedermeyer,S., Yun,X., Trujillo,M., Jiang,H., Andrade,M.R.,
            Kolb,T.M., Suresh,K., Damarla,M. and Shimoda,L.A.
  TITLE     A novel interaction between aquaporin 1 and caspase-3 in pulmonary
            arterial smooth muscle cells
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 326 (5), L638-L645 (2024)
   PUBMED   38375595
  REMARK    GeneRIF: A novel interaction between aquaporin 1 and caspase-3 in
            pulmonary arterial smooth muscle cells.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Holota,R., Decmanova,V., Alexovic Matiasova,A., Kosuth,J.,
            Slovinska,L., Pacut,L., Tomori,Z., Daxnerova,Z. and Sevc,J.
  TITLE     Cleaved caspase-3 is present in the majority of glial cells in the
            intact rat spinal cord during postnatal life
  JOURNAL   Histochem Cell Biol 161 (3), 269-286 (2024)
   PUBMED   37938347
  REMARK    GeneRIF: Cleaved caspase-3 is present in the majority of glial
            cells in the intact rat spinal cord during postnatal life.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Tan,W., Li,Y., Ma,L., Fu,X., Long,Q., Yan,F., Li,W., Liu,X.,
            Ding,H., Wang,Y. and Zhang,W.
  TITLE     Exosomes of endothelial progenitor cells repair injured vascular
            endothelial cells through the Bcl2/Bax/Caspase-3 pathway
  JOURNAL   Sci Rep 14 (1), 4465 (2024)
   PUBMED   38396011
  REMARK    GeneRIF: Exosomes of endothelial progenitor cells repair injured
            vascular endothelial cells through the Bcl2/Bax/Caspase-3 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Galichanin,K. and Yu,Z.
  TITLE     Expression of active caspase 3 in the rat lens after in vivo
            exposure to subthreshold dose of UVR-B
  JOURNAL   BMC Ophthalmol 24 (1), 29 (2024)
   PUBMED   38254051
  REMARK    GeneRIF: Expression of active caspase 3 in the rat lens after in
            vivo exposure to subthreshold dose of UVR-B.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Li,C., Zhang,H., Mo,J., Zuo,J. and Ye,L.
  TITLE     Caspase-3/GSDME dependent pyroptosis contributes to offspring lung
            injury induced by gestational PFOS exposure via PERK/ATF4 signaling
  JOURNAL   Arch Toxicol 98 (1), 207-221 (2024)
   PUBMED   37955688
  REMARK    GeneRIF: Caspase-3/GSDME dependent pyroptosis contributes to
            offspring lung injury induced by gestational PFOS exposure via
            PERK/ATF4 signaling.
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Vito,P., Ghayur,T. and D'Adamio,L.
  TITLE     Generation of anti-apoptotic presenilin-2 polypeptides by
            alternative transcription, proteolysis, and caspase-3 cleavage
  JOURNAL   J Biol Chem 272 (45), 28315-28320 (1997)
   PUBMED   9353287
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Ni,B., Wu,X., Du,Y., Su,Y., Hamilton-Byrd,E., Rockey,P.K.,
            Rosteck,P. Jr., Poirier,G.G. and Paul,S.M.
  TITLE     Cloning and expression of a rat brain interleukin-1beta-converting
            enzyme (ICE)-related protease (IRP) and its possible role in
            apoptosis of cultured cerebellar granule neurons
  JOURNAL   J Neurosci 17 (5), 1561-1569 (1997)
   PUBMED   9030616
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Juan,T.S., McNiece,I.K., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.
            and Fletcher,F.A.
  TITLE     Molecular characterization of mouse and rat CPP32 beta gene
            encoding a cysteine protease resembling interleukin-1 beta
            converting enzyme and CED-3
  JOURNAL   Oncogene 13 (4), 749-755 (1996)
   PUBMED   8761296
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Liu,X., Kim,C.N., Yang,J., Jemmerson,R. and Wang,X.
  TITLE     Induction of apoptotic program in cell-free extracts: requirement
            for dATP and cytochrome c
  JOURNAL   Cell 86 (1), 147-157 (1996)
   PUBMED   8689682
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Flaws,J.A., Kugu,K., Trbovich,A.M., DeSanti,A., Tilly,K.I.,
            Hirshfield,A.N. and Tilly,J.L.
  TITLE     Interleukin-1 beta-converting enzyme-related proteases (IRPs) and
            mammalian cell death: dissociation of IRP-induced oligonucleosomal
            endonuclease activity from morphological apoptosis in granulosa
            cells of the ovarian follicle
  JOURNAL   Endocrinology 136 (11), 5042-5053 (1995)
   PUBMED   7588240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006253192.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.50606.1,
                                           SRR26643291.38239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..277
                     /product="caspase-3"
                     /EC_number="3.4.22.56"
                     /note="IRP; SCA-1; CASP-3; CPP-32; apopain; cysteine
                     protease CPP32; SREBP cleavage activity 1; protein Yama;
                     Caspase 3, apoptosis related cysteine protease (ICE-like
                     cysteine protease); CPP32beta; cysteine protease p32-beta"
                     /calculated_mol_wt=31361
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P70677; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42574; propagated from
                     UniProtKB/Swiss-Prot (P55213.2)"
     mat_peptide     29..175
                     /product="Caspase-3 subunit p17.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004591"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=16508
     Region          37..277
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; smart00115"
                     /db_xref="CDD:214521"
     Site            order(64,122,161,168,204..209,213..214)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(121,163)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(169,189..190,197,200,203,226,234,240,260,265..266,
                     268,271..272)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(170,188)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     mat_peptide     176..277
                     /product="Caspase-3 subunit p12.
                     /evidence=ECO:0000250|UniProtKB:P42574.
                     /id=PRO_0000004592"
                     /note="propagated from UniProtKB/Swiss-Prot (P55213.2)"
                     /calculated_mol_wt=11890
     CDS             1..277
                     /gene="Casp3"
                     /gene_synonym="CPP32-beta; Lice; Yama"
                     /coded_by="NM_001436899.1:82..915"
                     /db_xref="GeneID:25402"
                     /db_xref="RGD:2275"
ORIGIN      
        1 mdnnetsvds ksinnfetkt ihgsksmdsg iyldssykmd ypemglciii nnknfhkstg
       61 msarngtdvd aanlretfma lkyevrnknd ltreeimelm dsvskedhsk rssfvcvils
      121 hgdegvifgt ngpvdlkklt sffrgdycrs ltgkpklfii qacrgteldc gietdsgtdd
      181 dmacqkipve adflyaysta pgyyswrnsr dgswfiqslc amlklyahkl efmhiltrvn
      241 rkvatefesf sldatfhakk qipcivsmlt kelyfyh
//
LOCUS       NP_001423830             378 aa            linear   ROD 26-MAR-2025
DEFINITION  N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
            precursor [Rattus norvegicus].
ACCESSION   NP_001423830 XP_017455515
VERSION     NP_001423830.1
DBSOURCE    REFSEQ: accession NM_001436901.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Shiraishi,N., Natsume,A., Togayachi,A., Endo,T., Akashima,T.,
            Yamada,Y., Imai,N., Nakagawa,S., Koizumi,S., Sekine,S.,
            Narimatsu,H. and Sasaki,K.
  TITLE     Identification and characterization of three novel beta
            1,3-N-acetylglucosaminyltransferases structurally related to the
            beta 1,3-galactosyltransferase family
  JOURNAL   J Biol Chem 276 (5), 3498-3507 (2001)
   PUBMED   11042166
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017455515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.37947.1,
                                           SRR22582416.110235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680446, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..378
                     /product="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 3 precursor"
                     /EC_number="2.4.1.146"
                     /note="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 3"
                     /calculated_mol_wt=39817
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     Region          119..308
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..378
                     /gene="B3gnt3"
                     /coded_by="NM_001436901.1:300..1436"
                     /db_xref="GeneID:290638"
                     /db_xref="RGD:1305151"
ORIGIN      
        1 mrlprlrpvv slllalaall llltcqspps cpapesptep kddpawapdl srahaapcra
       61 nlsvsahpaf arlpshvrdf llyrhcrdfa vlrepkatkc aqpaflllai ksspanygrr
      121 qvlrttware rrvrgaslrr lflvgsdrdp qqarkfnrll eleakaygdi lqwdfhdsff
      181 nltlkqvlfl ewqrthctna sfvlngdddv fahtdnmvty lqgrdpdqhl fvghliqnvg
      241 pirvpwskyf iptlvtaedk yppycggggf llsrftmaal hraarvlpif piddvflgmc
      301 lqqqglapga hsgvrtagvl ppsprvssfd pcfyrdlllv hrflpfemll mwdalsrpql
      361 acgrqsppll tglggrhp
//
LOCUS       NP_001092947             843 aa            linear   ROD 26-MAR-2025
DEFINITION  vomeronasal 2 receptor 70 [Rattus norvegicus].
ACCESSION   NP_001092947 XP_344198
VERSION     NP_001092947.1
DBSOURCE    REFSEQ: accession NM_001099477.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000014.1.
            
            On Jul 26, 2007 this sequence version replaced XP_344198.3.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..843
                     /product="vomeronasal 2 receptor 70"
                     /calculated_mol_wt=96262
     Region          45..501
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,167..168,392)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          510..563
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          584..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          584..608
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(586,589..590,593..594,596..597,631,635,638..639,647,
                     651)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          620..641
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(640,652..653,656..657,660,740,745,748..749,752,786,
                     789..790,793,797,805..806,809,812,816)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          650..674
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          698..714
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          741..767
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          775..798
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          803..828
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..843
                     /gene="Vom2r70"
                     /gene_synonym="RGD1562647"
                     /coded_by="NM_001099477.1:1..2532"
                     /db_xref="GeneID:364086"
                     /db_xref="RGD:1562647"
ORIGIN      
        1 mkklcaftia flilkfslil fhltepscfw riknseetdg dlrsdcgfvl ftfeepieen
       61 fynqlinfri sarkyefflv mffatdeink npyllpnmsl ifslgdrmck dtlgvldqiy
      121 sqknhswhfi nyvcglerrc digltgpswt tslklamdsr tpkvffgpln snlrdheqfp
      181 yvhqiaikdt rlphgmvslm lqfgwtwvgl iisdndqgiq flsdlreemq rhgiclafvn
      241 mipetmqiym tkakiydqql itssakvvii ygemnstlev sfrrwaylge qriwvtnsqw
      301 dviinktdfs ldffhgtvtf ahhhsgmtif rnvmqtists kypvdisqsm lgwnhfncsi
      361 sdnrhskmdh ftfnntlewl alhkfdmvls eegynlynav yavahtyhel ilqqvesqkv
      421 skhkglftdc qqvasllktr vftnpvgelv nmnhrenqca eydifiiwnf pqglglkvki
      481 asyfpcfphd qqlrisedle wategtlvss smcsvtciag frkihqkqta dccfdcvqcp
      541 enevsnetad meqcarcpdd kyanseqtyc lqravtylay edslgmalgc malffsvtti
      601 lvlvtfvkyk dtpivkannr ilsyillisl ifcflcsllf ighpnkatci lqqitfgvff
      661 svavsavlak tvtvvmafkl ttpgrrmrgm lalgapnlvi pictliqlvl cgiwlvispp
      721 fidrdiqseh gktiiicnkg sviafhftlg ylgtlalmsf avaflarklp drfneakflt
      781 fsmlvfysvw itflpvyhst rgkvmvvvev fsilassagl lgcifvpkcy vilvrpdlnf
      841 lqk
//
LOCUS       NP_071579                335 aa            linear   ROD 26-MAR-2025
DEFINITION  3-hydroxyisobutyrate dehydrogenase, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_071579 XP_342687
VERSION     NP_071579.1
DBSOURCE    REFSEQ: accession NM_022243.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Murin,R., Schaer,A., Kowtharapu,B.S., Verleysdonk,S. and
            Hamprecht,B.
  TITLE     Expression of 3-hydroxyisobutyrate dehydrogenase in cultured neural
            cells
  JOURNAL   J Neurochem 105 (4), 1176-1186 (2008)
   PUBMED   18284611
  REMARK    GeneRIF: The expression of 3-hydroxyisobutyrate dehydrogenase in
            neural cells demonstrates their potential to utilize valine
            imported into the brain for the generation of energy.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Loupatty,F.J., van der Steen,A., Ijlst,L., Ruiter,J.P., Ofman,R.,
            Baumgartner,M.R., Ballhausen,D., Yamaguchi,S., Duran,M. and
            Wanders,R.J.
  TITLE     Clinical, biochemical, and molecular findings in three patients
            with 3-hydroxyisobutyric aciduria
  JOURNAL   Mol Genet Metab 87 (3), 243-248 (2006)
   PUBMED   16466957
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Hawes,J.W., Harper,E.T., Crabb,D.W. and Harris,R.A.
  TITLE     Structural and mechanistic similarities of 6-phosphogluconate and
            3-hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the
            3-hydroxyacid dehydrogenases
  JOURNAL   FEBS Lett 389 (3), 263-267 (1996)
   PUBMED   8766712
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Rougraff,P.M., Zhang,B., Kuntz,M.J., Harris,R.A. and Crabb,D.W.
  TITLE     Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate
            dehydrogenase. Evidence for its evolutionary relationship to other
            pyridine nucleotide-dependent dehydrogenases
  JOURNAL   J Biol Chem 264 (10), 5899-5903 (1989)
   PUBMED   2647728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            J04628.1 and AA859729.1.
            
            On Dec 24, 2005 this sequence version replaced XP_342687.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127442.1, J04628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..335
                     /product="3-hydroxyisobutyrate dehydrogenase,
                     mitochondrial precursor"
                     /EC_number="1.1.1.31"
                     /note="3-hydroxyisobutyrate dehydrogenase, mitochondrial"
                     /calculated_mol_wt=31635
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P29266.3)"
                     /calculated_mol_wt=3686
     mat_peptide     36..335
                     /product="3-hydroxyisobutyrate dehydrogenase,
                     mitochondrial. /id=PRO_0000007160"
                     /note="propagated from UniProtKB/Swiss-Prot (P29266.3)"
                     /calculated_mol_wt=31635
     Region          43..330
                     /region_name="HIBADH"
                     /note="3-hydroxyisobutyrate dehydrogenase; TIGR01692"
                     /db_xref="CDD:130753"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            148
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            237
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     Site            320
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99L13; propagated from
                     UniProtKB/Swiss-Prot (P29266.3)"
     CDS             1..335
                     /gene="Hibadh"
                     /coded_by="NM_022243.1:33..1040"
                     /db_xref="GeneID:63938"
                     /db_xref="RGD:708399"
ORIGIN      
        1 maaslgfrga asglrywsgr rrpvgslaav csrsmasktp vgfiglgnmg npmaknlikh
       61 gyplilydvf pdvckefkea geqvasspad vaekadriit mlpssmnsie vysgangilk
      121 kvkkgsllid sstidpsvsk elakevekmg avfmdapvsg gvgaarsgnl tfmvggvene
      181 faaaqellgc mgsnvlycga vgsgqsakic nnmllaismi gtaeamnlgi rsgldpklla
      241 kilnmssgrc wssdtynpvp gvmdgvpssn nyqggfgttl makdlglaqd satstktpil
      301 lgsvahqiyr mmcskgyskk dfssvfqylr eeetf
//
LOCUS       NP_001423856             366 aa            linear   ROD 26-MAR-2025
DEFINITION  SERTA domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_001423856 XP_038946871
VERSION     NP_001423856.1
DBSOURCE    REFSEQ: accession NM_001436927.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038946871.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.3386871.1,
                                           SRR26643291.34720.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840117 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..366
                     /product="SERTA domain-containing protein 4"
                     /calculated_mol_wt=40030
     Region          108..142
                     /region_name="SERTA"
                     /note="SERTA motif; pfam06031"
                     /db_xref="CDD:461806"
     CDS             1..366
                     /gene="Sertad4"
                     /gene_synonym="RGD1565408"
                     /coded_by="NM_001436927.1:280..1380"
                     /db_xref="GeneID:360899"
                     /db_xref="RGD:1565408"
ORIGIN      
        1 mtlvlsmnrf cepivsegaa eiagyhtlwe adsyggaspp gpahvpsqgd rgagpqlags
       61 hyrgisnpvs tpkvtyfkrk yaeeeelptp lsscshktis ifeerahily msleklrfid
      121 dpevylrrsv linnlmkrih geivmqnswy lpacslsgts aqewflaqdc pyrkrprvak
      181 qewekfhtcc fyqecgghcl nlplsvsdgv gsasaaavas passssspst sspsspssss
      241 sslssplplp scshhvdfdv gsapiyksqv paseifvtnv rslgvqekik fnsdgkvshe
      301 tsrdgnalgq epvgndldfe ckgqfydyfe tgyternrms eswkkslrkk elspsnklcc
      361 srggkm
//
LOCUS       NP_001014157             606 aa            linear   ROD 26-MAR-2025
DEFINITION  WD repeat-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001014157 XP_341229
VERSION     NP_001014157.1
DBSOURCE    REFSEQ: accession NM_001014135.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Lechuga,S., Baranwal,S. and Ivanov,A.I.
  TITLE     Actin-interacting protein 1 controls assembly and permeability of
            intestinal epithelial apical junctions
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 308 (9), G745-G756 (2015)
   PUBMED   25792565
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Luxenburg,C., Heller,E., Pasolli,H.A., Chai,S., Nikolova,M.,
            Stokes,N. and Fuchs,E.
  TITLE     Wdr1-mediated cell shape dynamics and cortical tension are
            essential for epidermal planar cell polarity
  JOURNAL   Nat Cell Biol 17 (5), 592-604 (2015)
   PUBMED   25915128
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Yuan,B., Wan,P., Chu,D., Nie,J., Cao,Y., Luo,W., Lu,S., Chen,J. and
            Yang,Z.
  TITLE     A cardiomyocyte-specific Wdr1 knockout demonstrates essential
            functional roles for actin disassembly during myocardial growth and
            maintenance in mice
  JOURNAL   Am J Pathol 184 (7), 1967-1980 (2014)
   PUBMED   24840128
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Song,J.J., Adler,H.J., Lee,H.S., Jang,J.H., Park,M.H., Lee,J.H.,
            Chang,S.O. and Oh,S.H.
  TITLE     WDR1 expression in normal and noise-damaged Sprague-Dawley rat
            cochleae
  JOURNAL   J Comp Neurol 521 (7), 1470-1481 (2013)
   PUBMED   22821633
  REMARK    GeneRIF: elevated WDR1 expression after acoustic overstimulation in
            the current experiments may provide a mechanism for protection
            against noise exposure.
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Doukhanine,E., Gavino,C., Haines,J.D., Almazan,G. and Richard,S.
  TITLE     The QKI-6 RNA binding protein regulates actin-interacting protein-1
            mRNA stability during oligodendrocyte differentiation
  JOURNAL   Mol Biol Cell 21 (17), 3029-3040 (2010)
   PUBMED   20631256
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Kile,B.T., Panopoulos,A.D., Stirzaker,R.A., Hacking,D.F.,
            Tahtamouni,L.H., Willson,T.A., Mielke,L.A., Henley,K.J.,
            Zhang,J.G., Wicks,I.P., Stevenson,W.S., Nurden,P., Watowich,S.S.
            and Justice,M.J.
  TITLE     Mutations in the cofilin partner Aip1/Wdr1 cause autoinflammatory
            disease and macrothrombocytopenia
  JOURNAL   Blood 110 (7), 2371-2380 (2007)
   PUBMED   17515402
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Fujibuchi,T., Abe,Y., Takeuchi,T., Imai,Y., Kamei,Y., Murase,R.,
            Ueda,N., Shigemoto,K., Yamamoto,H. and Kito,K.
  TITLE     AIP1/WDR1 supports mitotic cell rounding
  JOURNAL   Biochem Biophys Res Commun 327 (1), 268-275 (2005)
   PUBMED   15629458
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085864.1.
            
            On Apr 20, 2005 this sequence version replaced XP_341229.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085864.1, AY986483.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..606
                     /product="WD repeat-containing protein 1"
                     /note="WD repeat protein 1"
                     /calculated_mol_wt=66051
     Region          4..45
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          48..87
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          54..389
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(57,75,79,85..86,100..101,119,127,133..134,144..145,
                     163,168,174..175,188,205,210,216..217,229,233,251,255,
                     261..262,318..319,338,343,349..350,363..364,381,385)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          62..100
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          93..135
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Site            95
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          105..143
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          129..605
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          138..176
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          150..186
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          180..218
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          192..228
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          224..263
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          237..273
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          270..306
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          311..351
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          325..361
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          358..408
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          432..474
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          445..487
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          480..518
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Site            480
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75083; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          492..516
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          523..561
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          535..572
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          566..604
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI0.3)"
     Region          579..604
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..606
                     /gene="Wdr1"
                     /coded_by="NM_001014135.1:14..1834"
                     /db_xref="GeneID:360950"
                     /db_xref="RGD:1305789"
ORIGIN      
        1 mpyeikkvfa slpqvergvs kilggdpkgd nflytngkcv ilrnidnpav adiytehahq
       61 vvvakyapsg fyiasgdisg klriwdttqk ehilkyeyqp fagkikdiaw tedskriavv
      121 gegrekfgav flwdtgssvg eitghnkvin svdikqnrpy rlatgsddnc aaffegppfk
      181 fkftigdhsr fvncvrfspd gnrfatasad gqifiydgkt gekvcalggs kahdggiyai
      241 swspdsthll sasgdktski wdvnvnsvvs tfpmgsnvld qqlgclwqkd hllsislsgy
      301 inyldknnps kplrvikghs ksiqcltvhk nggksyiysg shdghinywd setgendsfs
      361 gkghtnqvsr mtvdesgqlv scsmddtvry tnltlrdysg qgvvkldvqp kcvavgpggy
      421 tvvvcigqiv llkdqkkcfs idnpgyepev vavhpggdtv avggsdgnvr vysilgatlk
      481 degklleakg pvtdlayshd gaflavcdas kvvtvfsvad gysennvfyg hhakivclaw
      541 spdnehfasg gmdmmvyvwt lsdpetkvki qdahrlhhvs slawldehtl vttshdasvk
      601 ewtity
//
LOCUS       NP_001423858            1198 aa            linear   ROD 26-MAR-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001423858 XP_038947974
VERSION     NP_001423858.1
DBSOURCE    REFSEQ: accession NM_001436929.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   4  (residues 1 to 1198)
  AUTHORS   Walker,D.M., Urbe,S., Dove,S.K., Tenza,D., Raposo,G. and
            Clague,M.J.
  TITLE     Characterization of MTMR3. an inositol lipid 3-phosphatase with
            novel substrate specificity
  JOURNAL   Curr Biol 11 (20), 1600-1605 (2001)
   PUBMED   11676921
REFERENCE   5  (residues 1 to 1198)
  AUTHORS   Taylor,G.S., Maehama,T. and Dixon,J.E.
  TITLE     Myotubularin, a protein tyrosine phosphatase mutated in myotubular
            myopathy, dephosphorylates the lipid second messenger,
            phosphatidylinositol 3-phosphate
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8910-8915 (2000)
   PUBMED   10900271
REFERENCE   6  (residues 1 to 1198)
  AUTHORS   Zhao,R., Qi,Y. and Zhao,Z.J.
  TITLE     FYVE-DSP1, a dual-specificity protein phosphatase containing an
            FYVE domain
  JOURNAL   Biochem Biophys Res Commun 270 (1), 222-229 (2000)
   PUBMED   10733931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038947974.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.35306.1,
                                           SRR26643295.49483.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1198
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR3 isoform 3"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3"
                     /calculated_mol_wt=133874
     Region          23..116
                     /region_name="PH-GRAM_MTMR3"
                     /note="Myotubularian (MTM) related 3 protein (MTMR3)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13341"
                     /db_xref="CDD:270149"
     Region          169..485
                     /region_name="PTP-MTMR3"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 3;
                     cd14586"
                     /db_xref="CDD:350434"
     Region          1115..1175
                     /region_name="FYVE_MTMR3"
                     /note="FYVE domain found in myotubularin-related protein 3
                     (MTMR3) and similar proteins; cd15732"
                     /db_xref="CDD:277271"
     Site            order(1116,1119,1137..1142,1144..1145,1169..1171)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277271"
     CDS             1..1198
                     /gene="Mtmr3"
                     /coded_by="NM_001436929.1:530..4126"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:305482"
                     /db_xref="RGD:1310972"
ORIGIN      
        1 mdeemrhsle ciqanqifpr kqliredenl qvpflelhge steyvgraed aiialsnyrl
       61 hikfkeslvn vplqliesve crdifqlhlt ckdckvircq fptfeqcqdw lkrlnnairp
      121 pgkiedlfsf ayhawcmevy asekeqhgdl crpgehvtsr fknevermgf dmnnawrisn
      181 inekyklcgs ypqelivpaw itdkelesva gfrswkripa viyrhqsnga viarcgqpev
      241 swwgwrnadd ehlvqsvaka casdsqssvg kvstrnscrg fpnagdlsdv efdaslsnas
      301 gteslalqpq kllildarsy aaavanrakg ggcecpeyyp ncevvfmgma nihsirrsfq
      361 slrllctqmp dpgnwlsale stkwlhhlsv llksallvvh avdrdqrpvl vhcsdgwdrt
      421 pqivalakll ldpyyrtveg fqvlvemewl dfghkfadrc ghgensddln ercpvflqwl
      481 dcvhqlqrqf pcsfefneaf lvklvqhtys clfgtflcnn akergekqtq ertcsvwsll
      541 ragnkafknl lyssqseavl ypvchvrnlm lwsavylpcp spstptddsc apypapgtsp
      601 depplsrlpk trsfdnlttt cdnmvplasr rssdpslnek wqehgrslel ssfagsgeev
      661 paidslrrps rllggaelsv aagvaegqme nilqeatkee sgveepthre htevpevkee
      721 aplakesrta aqgsgvlyqe pqlddatlrs hlgpslssfs qgipehrevg hsvlssslpa
      781 slrgedsqev pveqpqveni aedrenvvpa vpvdvkiglg tsesspllps qvpfetrgph
      841 mnnsvhmlle dkvksesgpq lhhrpclass grfsgkdmlp iapeprsaer pqwdsvlhrt
      901 sspgntlslm mqapcalpld kcrqrivcng aletenkase qpagfdtlqk yptpnghcan
      961 getgrskdsl shqlsatsys sahscsrnlh hkwlnshsgr psttnspeqp srshldddgm
     1021 pvytdtiqqr lrqiesghqq evetlkkqvq elksrlesqy ltsslrfngd fgdevtsipd
     1081 sesnldqncl srcsteifse asweqvdkqd temtrwlpdh laahcyacds afwlasrkhh
     1141 crncgnvfcs sccnqkvpvp sqqlfepsrv ckscysslhp tsssidleld kpiaatsn
//
LOCUS       NP_001423782             515 aa            linear   ROD 26-MAR-2025
DEFINITION  heterochromatin protein 1-binding protein 3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001423782
VERSION     NP_001423782.1
DBSOURCE    REFSEQ: accession NM_001436853.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Dutta,B., Yan,R., Lim,S.K., Tam,J.P. and Sze,S.K.
  TITLE     Quantitative profiling of chromatome dynamics reveals a novel role
            for HP1BP3 in hypoxia-induced oncogenesis
  JOURNAL   Mol Cell Proteomics 13 (12), 3236-3249 (2014)
   PUBMED   25100860
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Dutta,B., Ren,Y., Hao,P., Sim,K.H., Cheow,E., Adav,S., Tam,J.P. and
            Sze,S.K.
  TITLE     Profiling of the Chromatin-associated Proteome Identifies HP1BP3 as
            a Novel Regulator of Cell Cycle Progression
  JOURNAL   Mol Cell Proteomics 13 (9), 2183-2197 (2014)
   PUBMED   24830416
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Hayashihara,K., Uchiyama,S., Shimamoto,S., Kobayashi,S.,
            Tomschik,M., Wakamatsu,H., No,D., Sugahara,H., Hori,N., Noda,M.,
            Ohkubo,T., Zlatanova,J., Matsunaga,S. and Fukui,K.
  TITLE     The middle region of an HP1-binding protein, HP1-BP74, associates
            with linker DNA at the entry/exit site of nucleosomal DNA
  JOURNAL   J Biol Chem 285 (9), 6498-6507 (2010)
   PUBMED   20042602
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16714.1,
                                           SRR26643284.8234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..515
                     /product="heterochromatin protein 1-binding protein 3
                     isoform b"
                     /calculated_mol_wt=56678
     Region          117..201
                     /region_name="H15"
                     /note="linker histone 1 and histone 5 domains; the basic
                     subunit of chromatin is the nucleosome, consisting of an
                     octamer of core histones, two full turns of DNA, a linker
                     histone (H1 or H5) and a variable length of linker DNA;
                     H1/H5 are chromatin-associated...; cd00073"
                     /db_xref="CDD:238028"
     Site            order(124,136,168,182)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Site            163..174
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:238028"
     Region          226..286
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          302..369
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          <431..>505
                     /region_name="PRK13808"
                     /note="adenylate kinase; Provisional"
                     /db_xref="CDD:172341"
     CDS             1..515
                     /gene="Hp1bp3"
                     /coded_by="NM_001436853.1:52..1599"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:313647"
                     /db_xref="RGD:735099"
ORIGIN      
        1 mpirravnst retppkskla egeeekpepd gsseesistv eepenetppa psreaeqpkg
       61 epesgekees ksaeetkkee kdqskekekk vkktipawat lsasqlaraq kqtpmasspr
      121 pkmdailtea ikacfqksga svvairkyii hkypsldler rgyllkqalk relnrgvikq
      181 vkgkgasgsf vvvqksktpq ksknrkkgsa vdpepqvkle dvlplaftrl cepkeasysl
      241 irkyvsqyyp klrvdirpql lknalqrave rgqleqitgk gasgtfqlkk sgekpllggs
      301 lmeyailsai aamnepktcs ttalkkyvle nhpgtnsnyq mhllkktlqk cekngwleqi
      361 sgkgfsgtfq lcfpyypspg vlfpkkvsdg sededeeede eessedsede epppkrslqk
      421 ktpakpqgkt asmkqrgakp arkvpaaqrg kvrplpkkap pkaktparkg rpapsavkkp
      481 sgstskkpva narkeaklpg kgksamkkks fktkk
//
LOCUS       NP_001423835            1578 aa            linear   ROD 26-MAR-2025
DEFINITION  GATOR1 complex protein DEPDC5 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423835 XP_017454701
VERSION     NP_001423835.1
DBSOURCE    REFSEQ: accession NM_001436906.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1578)
  AUTHORS   Chen,J., Ou,Y., Yang,Y., Li,W., Xu,Y., Xie,Y. and Liu,Y.
  TITLE     KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
            tumorigenesis and ageing
  JOURNAL   Nature 557 (7706), 585-589 (2018)
   PUBMED   29769719
REFERENCE   2  (residues 1 to 1578)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   3  (residues 1 to 1578)
  AUTHORS   Marsan,E., Ishida,S., Schramm,A., Weckhuysen,S., Muraca,G.,
            Lecas,S., Liang,N., Treins,C., Pende,M., Roussel,D., Le Van
            Quyen,M., Mashimo,T., Kaneko,T., Yamamoto,T., Sakuma,T., Mahon,S.,
            Miles,R., Leguern,E., Charpier,S. and Baulac,S.
  TITLE     Depdc5 knockout rat: A novel model of mTORopathy
  JOURNAL   Neurobiol Dis 89, 180-189 (2016)
   PUBMED   26873552
  REMARK    GeneRIF: DEP-domain containing 5 knockout rats exhibit multiple
            features of rodent models of mechanistic target of rapamycin
            complex 1 (mTOR) mTORopathies, and thus, stand as a relevant model
            to study their underlying pathogenic mechanisms.
REFERENCE   4  (residues 1 to 1578)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   5  (residues 1 to 1578)
  AUTHORS   Bar-Peled,L. and Sabatini,D.M.
  TITLE     Regulation of mTORC1 by amino acids
  JOURNAL   Trends Cell Biol 24 (7), 400-406 (2014)
   PUBMED   24698685
  REMARK    Review article
REFERENCE   6  (residues 1 to 1578)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   7  (residues 1 to 1578)
  AUTHORS   Dibbens,L.M., de Vries,B., Donatello,S., Heron,S.E., Hodgson,B.L.,
            Chintawar,S., Crompton,D.E., Hughes,J.N., Bellows,S.T., Klein,K.M.,
            Callenbach,P.M., Corbett,M.A., Gardner,A.E., Kivity,S., Iona,X.,
            Regan,B.M., Weller,C.M., Crimmins,D., O'Brien,T.J.,
            Guerrero-Lopez,R., Mulley,J.C., Dubeau,F., Licchetta,L.,
            Bisulli,F., Cossette,P., Thomas,P.Q., Gecz,J., Serratosa,J.,
            Brouwer,O.F., Andermann,F., Andermann,E., van den Maagdenberg,A.M.,
            Pandolfo,M., Berkovic,S.F. and Scheffer,I.E.
  TITLE     Mutations in DEPDC5 cause familial focal epilepsy with variable
            foci
  JOURNAL   Nat Genet 45 (5), 546-551 (2013)
   PUBMED   23542697
REFERENCE   8  (residues 1 to 1578)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_017454701.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.43835.1,
                                           SRR26643298.55084.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1578
                     /product="GATOR1 complex protein DEPDC5 isoform 3"
                     /note="DEP domain-containing protein 5; GATOR complex
                     protein DEPDC5; GATOR1 complex protein DEPDC5"
                     /calculated_mol_wt=178398
     Region          101..381
                     /region_name="IML1"
                     /note="Vacuolar membrane-associated protein Iml1;
                     pfam12257"
                     /db_xref="CDD:463510"
     Region          1154..1235
                     /region_name="DEP_DEPDC5-like"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in DEPDC5-like proteins. DEPDC5, in human also known
                     as KIAA0645, is a DEP domain containing protein of unknown
                     function; cd04449"
                     /db_xref="CDD:239896"
     Region          1253..1560
                     /region_name="DEPDC5_CTD"
                     /note="DEPDC5 protein C-terminal region; pfam19418"
                     /db_xref="CDD:466071"
     CDS             1..1578
                     /gene="Depdc5"
                     /coded_by="NM_001436906.1:146..4882"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:305464"
                     /db_xref="RGD:1311535"
ORIGIN      
        1 mrttkvyklv ihkkgfggsd delvvnpkvf phiklgdive iahpndeysp lllqvkslke
       61 dlqketisvd qtvtqvfrlr pyqdvyvnvv dpkdvtldlv eltfkdqyig rgdmwrlkks
      121 lvstcayitq kvefagiraq agelwvknek vmcgyiseet rvvfrstsam vyifiqmsce
      181 mwdfdiygdl yfekavngfl adlftkwkek ncshevtvvl fsrtfydaks idefpevnra
      241 siqqdhkgrf yedfykvvvq nerreewtsl lvtikklfiq ypvlvrleqa ggfpqgdnst
      301 saqgnyleai nlsfnvfdkh yinrnfdrtg qmsvvitpgv gvfevdrllm iltkqrmidn
      361 gigvdlvcmg eqplhavplf klhnrsvprd srlgddynip hwinhsfyts ksqlfcnsft
      421 priklagkks atektkngrd tslgapkese ntlpiqvdyd aydaqvfrlp gpsraqrlat
      481 crsvreqenh nrksasscdv ssspslpsra lpteevrsqa sddsslgkst nilmipnphl
      541 hqyevssslg ytstrdvlen mieppqrdss apgrfhvgsa esmlhvrpgg ytpqralinp
      601 fapsrmpmkl tsnrrrwmht fpvgpsgeai qihhqtrqnm aelqgsrqrd pthssaelle
      661 layheaagrh stsrqpgdsm slnfsgteel svsllsnsgt gmnprnqnkd sledgvstsp
      721 dpiltlsapp vvpgfcctvg vdwkslttpa clplttdyfp drqglqndyt egcydllpea
      781 dmdrrdeegv qmtaqqvfee ficqrlmqgy qiivqpktqk psttvpppls ssplysrglv
      841 srnrpeeegq ywlsmgrtfh kvtlkdkmit vtrylpkypy esaqihytys lcpshsdsef
      901 vscwvefche rleeykwnyl dqyicsagse dfslieslkf wrtrflllpa cvtatkrite
      961 gevhcdiygd kpradedewq lldgfirfve glnrirrrhr sdrmirkgta mkglqmtgpi
     1021 sahslestgp pvgkkgtsal sallemeasq kslgeqqtsv hgksstqpae nssvamtpty
     1081 vdsprkasvd qtaplvldst slgvstcqsv drgnnqtfgn sqnieqafps tgsgdgssqq
     1141 hiassltsss tlveileamk hpstgvqlls eqkglspccf isaevvhwlm nnvegvqtqa
     1201 mgidimqkml eeqliahasg eawrtfvygf yfykivtdre pervamqqps apwhtagvdd
     1261 fasfqrkwfe vafvaeelvh seipafllpw lpsrpasyas rhssfsrsfg grsqaaalla
     1321 atvpeqrtvt ldvdvnnrtd rlewcscyyh gnfslnaafe iklhwmavta tvlfemvqgw
     1381 hrkatscgfl lvpvlegpfa lpsylygdpl raqlfiplnl gcllkegseh lfdsfepety
     1441 wdrmhlfqea iahrfgfvqd kysasafnfp aenkpqyihv tgtvflqlpy skrkfsgqqr
     1501 rrrnstsstn qnmfceervg ynwayntmlt ktwrssatgd ekfadrllkd ftdfcinrdn
     1561 rlvtfwtncl ekmhasap
//
LOCUS       NP_001032739            1428 aa            linear   ROD 26-MAR-2025
DEFINITION  nephrocystin-4 isoform a [Rattus norvegicus].
ACCESSION   NP_001032739 XP_233698
VERSION     NP_001032739.2
DBSOURCE    REFSEQ: accession NM_001037650.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1428)
  AUTHORS   Dharmat,R., Eblimit,A., Robichaux,M.A., Zhang,Z., Nguyen,T.T.,
            Jung,S.Y., He,F., Jain,A., Li,Y., Qin,J., Overbeek,P., Roepman,R.,
            Mardon,G., Wensel,T.G. and Chen,R.
  TITLE     SPATA7 maintains a novel photoreceptor-specific zone in the distal
            connecting cilium
  JOURNAL   J Cell Biol 217 (8), 2851-2865 (2018)
   PUBMED   29899041
REFERENCE   2  (residues 1 to 1428)
  AUTHORS   Borgal,L., Habbig,S., Hatzold,J., Liebau,M.C., Dafinger,C.,
            Sacarea,I., Hammerschmidt,M., Benzing,T. and Schermer,B.
  TITLE     The ciliary protein nephrocystin-4 translocates the canonical Wnt
            regulator Jade-1 to the nucleus to negatively regulate beta-catenin
            signaling
  JOURNAL   J Biol Chem 287 (30), 25370-25380 (2012)
   PUBMED   22654112
REFERENCE   3  (residues 1 to 1428)
  AUTHORS   French,V.M., van de Laar,I.M., Wessels,M.W., Rohe,C.,
            Roos-Hesselink,J.W., Wang,G., Frohn-Mulder,I.M., Severijnen,L.A.,
            de Graaf,B.M., Schot,R., Breedveld,G., Mientjes,E., van
            Tienhoven,M., Jadot,E., Jiang,Z., Verkerk,A., Swagemakers,S.,
            Venselaar,H., Rahimi,Z., Najmabadi,H., Meijers-Heijboer,H., de
            Graaff,E., Helbing,W.A., Willemsen,R., Devriendt,K., Belmont,J.W.,
            Oostra,B.A., Amack,J.D. and Bertoli-Avella,A.M.
  TITLE     NPHP4 variants are associated with pleiotropic heart malformations
  JOURNAL   Circ Res 110 (12), 1564-1574 (2012)
   PUBMED   22550138
REFERENCE   4  (residues 1 to 1428)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 1428)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Wolf,M.T., O'Toole,J.F., Otto,E.A., Schultheiss,U.,
            Deschenes,G., Attanasio,M., Utsch,B., Antignac,C. and
            Hildebrandt,F.
  TITLE     Evidence of oligogenic inheritance in nephronophthisis
  JOURNAL   J Am Soc Nephrol 18 (10), 2789-2795 (2007)
   PUBMED   17855640
REFERENCE   7  (residues 1 to 1428)
  AUTHORS   Arts,H.H., Doherty,D., van Beersum,S.E., Parisi,M.A.,
            Letteboer,S.J., Gorden,N.T., Peters,T.A., Marker,T., Voesenek,K.,
            Kartono,A., Ozyurek,H., Farin,F.M., Kroes,H.Y., Wolfrum,U.,
            Brunner,H.G., Cremers,F.P., Glass,I.A., Knoers,N.V. and Roepman,R.
  TITLE     Mutations in the gene encoding the basal body protein RPGRIP1L, a
            nephrocystin-4 interactor, cause Joubert syndrome
  JOURNAL   Nat Genet 39 (7), 882-888 (2007)
   PUBMED   17558407
REFERENCE   8  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Sudbrak,R., Reinhardt,R., Lehrack,S., Hennig,S.,
            Imm,A., Muerb,U., Utsch,B., Attanasio,M., O'Toole,J.F., Otto,E. and
            Hildebrandt,F.
  TITLE     Mutational analysis of the NPHP4 gene in 250 patients with
            nephronophthisis
  JOURNAL   Hum Mutat 25 (4), 411 (2005)
   PUBMED   15776426
REFERENCE   9  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Otto,E., Felten,H., Kuhn,K., Bley,T.A., Zauner,I.,
            Hildebrandt,F. and Neumann,H.P.
  TITLE     Clinical and histological presentation of 3 siblings with mutations
            in the NPHP4 gene
  JOURNAL   Am J Kidney Dis 43 (2), 358-364 (2004)
   PUBMED   14750102
REFERENCE   10 (residues 1 to 1428)
  AUTHORS   Otto,E., Hoefele,J., Ruf,R., Mueller,A.M., Hiller,K.S., Wolf,M.T.,
            Schuermann,M.J., Becker,A., Birkenhager,R., Sudbrak,R.,
            Hennies,H.C., Nurnberg,P. and Hildebrandt,F.
  TITLE     A gene mutated in nephronophthisis and retinitis pigmentosa encodes
            a novel protein, nephroretinin, conserved in evolution
  JOURNAL   Am J Hum Genet 71 (5), 1161-1167 (2002)
   PUBMED   12205563
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473968.1.
            
            On May 30, 2008 this sequence version replaced NP_001032739.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1428
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1428
                     /product="nephrocystin-4 isoform a"
                     /note="nephronophthisis 4 (juvenile) homolog"
                     /calculated_mol_wt=158087
     Region          55..1420
                     /region_name="NPHP4"
                     /note="Nephrocystin-4; cd22239"
                     /db_xref="CDD:412072"
     CDS             1..1428
                     /gene="Nphp4"
                     /coded_by="NM_001037650.2:341..4627"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:313749"
                     /db_xref="RGD:1560172"
ORIGIN      
        1 mddwhraftq ntlvpphpqr arqfgkesta fqcilkwldg plikqgildm lselechlrv
       61 slfdvtykhf fgrtwkttvk ptnqlskqpp rilfneplyf httlshpsiv avievvaegr
      121 krdgalqvls cgfgilrifg nkpesptsag qdkrlrlyhg tprallhpll qdpieqnrym
      181 tmmencslqy tlkphpplep afhllpenfl isglqqipgl lpphgdtgda lrkprfqkpt
      241 tlhlddlfft lypslekfee elvqllisdh fregvgllds gtlevlerrl hvcvhnglgf
      301 vhrpqvvvlv pemdmtltrs asfsrritas sksssgnqal vlrshlrlpe mvnhpsfaiv
      361 fqleyvfnsp sgadgsasss tslsslacmh mvrwavwnpd leagpgkvtl plqggvqhnp
      421 srclvykvps asmsseevkq vesgtiqfhf slssdalteh angpragrrs trkaltspsg
      481 tpalaardla aiqdspvgpg lslsqlaasp qslasqrsfk pppqpldgsq spegpqlqag
      541 svlesrishl eadlsqppfs vqgtptvehl qelpftplha pivvgaqtrs srsqlsraam
      601 vllqssgfpe ildarqqpve avnpmdpvrf npqkeesdcl lgneivlqfl afsraaqdcp
      661 gapwpqtvyf tfqfyrfppe ttprlqlvkl drtgkngsas lshilvhink dgsfdagspg
      721 fqlrymvdpg flkpgeqrwf aqylaaqtlq vdvwdgdsll ligsagiqmk hllrqgrpav
      781 qvshelevva teyeqemmvv sgdvagfgsv kpigvhtvvk grlhltlanv gheceprarg
      841 snalppsrsr visnngasff sggsllipgg pkrkrvvqaq kladvdsela amllthtrag
      901 qgpqavgqea davhrrkler mrlvrlqeag gdsdsrrisv larhsvraqh srdlqviday
      961 rertkaenia svlsqaitth htlyatlgta effefalknp hntqhtvaie idspelsiil
     1021 dsqewryfke atglltplee dmfhlrgsla pqlylrpret ahipfkfqnf svgppaptqa
     1081 paevisekda esgphwkcsa mptkhakvlf rvetgqliav lcltvepqph vvdqvfrfyh
     1141 peltflkkai rlppwhtlpg apvgmpgedp pvhvrcsdpn viceaqnvgl geprdvflkv
     1201 asgpspeikd ffvviyadrw lavpvqtwqv clhslqrvdv scvagqmtrl slvlrgtqtv
     1261 rkvraftshp qelktdpagv fvlpphgvqd lhvgvrprra gsrfihlnlv dvdyhqlvas
     1321 wlvclscrqp liskafeitm aagegkgank ritytnpyps rrtyrlhsdr pdllhfkeds
     1381 fqvaggetyt iglrflpsgs agqeeiliyi ndqddkneet fcvkvlyq
//
LOCUS       NP_001423805             273 aa            linear   ROD 26-MAR-2025
DEFINITION  SPRY domain-containing SOCS box protein 1 [Rattus norvegicus].
ACCESSION   NP_001423805 XP_006239524
VERSION     NP_001423805.1
DBSOURCE    REFSEQ: accession NM_001436876.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Nishiya,T., Matsumoto,K., Maekawa,S., Kajita,E., Horinouchi,T.,
            Fujimuro,M., Ogasawara,K., Uehara,T. and Miwa,S.
  TITLE     Regulation of inducible nitric-oxide synthase by the SPRY domain-
            and SOCS box-containing proteins
  JOURNAL   J Biol Chem 286 (11), 9009-9019 (2011)
   PUBMED   21199876
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006239524.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.23870.1,
                                           SRR26643288.24897.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840113 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..273
                     /product="SPRY domain-containing SOCS box protein 1"
                     /calculated_mol_wt=30640
     Region          54..227
                     /region_name="SPRY_SOCS1-2-4"
                     /note="SPRY domain in the suppressor of cytokine signaling
                     1, 2, 4 families (SOCS1, SOCS2, SOCS4); cd12906"
                     /db_xref="CDD:293963"
     Site            order(77,79,111,129,216..218)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:293963"
     Region          232..273
                     /region_name="SOCS"
                     /note="SOCS (suppressors of cytokine signaling) box. The
                     SOCS box is found in the C-terminal region of CIS/SOCS
                     family proteins (in combination with a SH2 domain), ASBs
                     (ankyrin repeat-containing proteins with a SOCS box), SSBs
                     (SPRY domain-containing proteins...; cl02533"
                     /db_xref="CDD:470605"
     Site            order(233..238,244,254,260)
                     /site_type="active"
                     /note="elongin B/C interaction [active]"
                     /db_xref="CDD:239641"
     CDS             1..273
                     /gene="Spsb1"
                     /gene_synonym="RGD1309319"
                     /coded_by="NM_001436876.1:314..1135"
                     /db_xref="GeneID:313722"
                     /db_xref="RGD:1309319"
ORIGIN      
        1 mgqkvtggik tvdmrdptyr plkqelqgld yckptrldll ldmppvsydv qllhswnnnd
       61 rslnvfvked dklifhrhpv aqstdairgk vgytrglhvw qitwamrqrg thavvgvata
      121 daplhsvgyt tlvgnnhesw gwdlgrnrly hdgknqpskt ypaflepdet fivpdsflva
      181 ldmddgtlsf ivdgqymgva frglkgkkly pvvsavwghc eirmryvngl dpeplplmdl
      241 crrsvrlalg kerlgaipal plpaslkayl lyq
//
LOCUS       NP_001423822             402 aa            linear   ROD 26-MAR-2025
DEFINITION  protein FAM53A [Rattus norvegicus].
ACCESSION   NP_001423822 XP_006251324
VERSION     NP_001423822.1
DBSOURCE    REFSEQ: accession NM_001436893.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006251324.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.35209.1,
                                           SRR26643288.52204.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..402
                     /product="protein FAM53A"
                     /calculated_mol_wt=42925
     Region          1..299
                     /region_name="FAM53"
                     /note="Family of FAM53; pfam15242"
                     /db_xref="CDD:464582"
     CDS             1..402
                     /gene="Fam53a"
                     /gene_synonym="RGD1563315"
                     /coded_by="NM_001436893.1:518..1726"
                     /db_xref="GeneID:305461"
                     /db_xref="RGD:1563315"
ORIGIN      
        1 mvtliteklq nqslddltrr aceavpysae kldksghlfp leigvdkspw kashggwpfr
       61 sraasgpfsv gphgvshteg lkwqlespgp mavgrfldlr estgppaapp tkrhcrslse
      121 peelarcrsp wrpgsskvwt piskrrcnsg gsatlqccsg lgnpalqgsl apglprkpvs
      181 ptgptspmtp rpasassgfv dgsegstssg ppwlstgpcp fssrrrlsls qehlvdagac
      241 lpsasstpts tpelgrhhgl lrcrsqpcvl dgrrvrrkrr reedarwtrp sldflkmtrt
      301 lknskslcsl dyeddeddtq aktvvsspcn sqglvgiitp ssspriprpg paspsvwasg
      361 epetstgegg ssgepsdwds ageegifpld hgdldleqie nn
//
LOCUS       NP_001423793             794 aa            linear   ROD 26-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 17 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001423793 XP_006239365
VERSION     NP_001423793.1
DBSOURCE    REFSEQ: accession NM_001436864.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Wanzel,M., Russ,A.C., Kleine-Kohlbrecher,D., Colombo,E.,
            Pelicci,P.G. and Eilers,M.
  TITLE     A ribosomal protein L23-nucleophosmin circuit coordinates Mizl
            function with cell growth
  JOURNAL   Nat Cell Biol 10 (9), 1051-1061 (2008)
   PUBMED   19160485
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Alter-Koltunoff,M., Goren,S., Nousbeck,J., Feng,C.G., Sher,A.,
            Ozato,K., Azriel,A. and Levi,B.Z.
  TITLE     Innate immunity to intraphagosomal pathogens is mediated by
            interferon regulatory factor 8 (IRF-8) that stimulates the
            expression of macrophage-specific Nramp1 through antagonizing
            repression by c-Myc
  JOURNAL   J Biol Chem 283 (5), 2724-2733 (2008)
   PUBMED   18045875
  REMARK    Erratum:[J Biol Chem. 2008 Aug 8;283(32):22336]
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Adhikary,S., Peukert,K., Karsunky,H., Beuger,V., Lutz,W.,
            Elsasser,H.P., Moroy,T. and Eilers,M.
  TITLE     Miz1 is required for early embryonic development during
            gastrulation
  JOURNAL   Mol Cell Biol 23 (21), 7648-7657 (2003)
   PUBMED   14560010
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Piluso,D., Bilan,P. and Capone,J.P.
  TITLE     Host cell factor-1 interacts with and antagonizes transactivation
            by the cell cycle regulatory factor Miz-1
  JOURNAL   J Biol Chem 277 (48), 46799-46808 (2002)
   PUBMED   12244100
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Peukert,K., Staller,P., Schneider,A., Carmichael,G., Hanel,F. and
            Eilers,M.
  TITLE     An alternative pathway for gene regulation by Myc
  JOURNAL   EMBO J 16 (18), 5672-5686 (1997)
   PUBMED   9312026
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006239365.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20947.1,
                                           SRR26643295.23596.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..794
                     /product="zinc finger and BTB domain-containing protein 17
                     isoform c"
                     /note="zinc finger protein 100; zinc finger and BTB
                     domain-containing protein 17"
                     /calculated_mol_wt=86820
     Region          2..113
                     /region_name="BTB_POZ_ZBTB17_MIZ1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 17 (ZBTB17); cd18206"
                     /db_xref="CDD:349515"
     Site            order(3..4,6..11,13..14,17,22..23,38,40,43..45,50,76..77,
                     80..83,103)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349515"
     Site            order(21,24..32,34,36,39,59..60,62..63,65)
                     /site_type="other"
                     /note="putative tetramer (dimer of dimer) interface
                     [polypeptide binding]"
                     /db_xref="CDD:349515"
     Region          297..628
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(360,362,364,366..367,370..371,374,388,390,394..395,
                     398..399,402,416,418,420,422..423,426..427,430)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(472,474,476,478..479,482..483,486,500,502,506..507,
                     510..511,514,528,530,532,534..535,538..539,542)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..599
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          607..626
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..794
                     /gene="Zbtb17"
                     /gene_synonym="Zfp100"
                     /coded_by="NM_001436864.1:208..2592"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:313666"
                     /db_xref="RGD:1307143"
ORIGIN      
        1 mdfpqhsqrv leqlnqqrqm gllcdctfvv dgvdfkahka vlaacseyfk mlfvdqkdvv
       61 hldisnaagl gqvlefmyta klhlspenvd dvlavasflq mqdiitacht lkslaeptst
      121 tgesadasae eggdkrakee kaaatvlsrl dqarssssag pgrelkeewg gqaesasrga
      181 eqtekadapr epppvelkpd ptssmaaaea ealsesseqe mevepaskge egqeeegpgp
      241 atvkeegvhl engeppeene esagtdsghe lgmegqnlrs gtygdrtesk aygsiihkce
      301 dcgkefthtg nfkrhiriht gekpfscrec skafsdpaac kahekthspl kpygceecgk
      361 syrlisllnl hkkrhsgear yrcgdcgklf ttsgnlkrhq lvhsgqkpyq cdycgrsfsd
      421 ptskmrhlet hdtdkehkcp hcdkkfnqvg nlkahlkihi adgplkcrec gkqfttsgnl
      481 krhlrihsge kpyvcthcqr qfadpgalqr hvrihtgekp cqcvicgkaf tqassliahv
      541 rqhtgekpyv cercgkrfvq ssqlanhirh hdnirphkcs vcskafvnvg dlskhiiiht
      601 gekpylcdkc grgfnrvdnl rshvktvhqg kagikilepe eggevsvvtv ddmvtlatea
      661 laatavtqlt vvpvgaavta detevlkaei skavkqvqee dpnthilyac dscgdkflda
      721 nslaqhvrih taqalvmfqt dadfyqqygp ggawpagqml qagelvfrpr dgtegqptla
      781 etpptapdcl ppae
//
LOCUS       NP_001423824            1428 aa            linear   ROD 26-MAR-2025
DEFINITION  nephrocystin-4 isoform a [Rattus norvegicus].
ACCESSION   NP_001423824 XP_038966033
VERSION     NP_001423824.1
DBSOURCE    REFSEQ: accession NM_001436895.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1428)
  AUTHORS   Dharmat,R., Eblimit,A., Robichaux,M.A., Zhang,Z., Nguyen,T.T.,
            Jung,S.Y., He,F., Jain,A., Li,Y., Qin,J., Overbeek,P., Roepman,R.,
            Mardon,G., Wensel,T.G. and Chen,R.
  TITLE     SPATA7 maintains a novel photoreceptor-specific zone in the distal
            connecting cilium
  JOURNAL   J Cell Biol 217 (8), 2851-2865 (2018)
   PUBMED   29899041
REFERENCE   2  (residues 1 to 1428)
  AUTHORS   Borgal,L., Habbig,S., Hatzold,J., Liebau,M.C., Dafinger,C.,
            Sacarea,I., Hammerschmidt,M., Benzing,T. and Schermer,B.
  TITLE     The ciliary protein nephrocystin-4 translocates the canonical Wnt
            regulator Jade-1 to the nucleus to negatively regulate beta-catenin
            signaling
  JOURNAL   J Biol Chem 287 (30), 25370-25380 (2012)
   PUBMED   22654112
REFERENCE   3  (residues 1 to 1428)
  AUTHORS   French,V.M., van de Laar,I.M., Wessels,M.W., Rohe,C.,
            Roos-Hesselink,J.W., Wang,G., Frohn-Mulder,I.M., Severijnen,L.A.,
            de Graaf,B.M., Schot,R., Breedveld,G., Mientjes,E., van
            Tienhoven,M., Jadot,E., Jiang,Z., Verkerk,A., Swagemakers,S.,
            Venselaar,H., Rahimi,Z., Najmabadi,H., Meijers-Heijboer,H., de
            Graaff,E., Helbing,W.A., Willemsen,R., Devriendt,K., Belmont,J.W.,
            Oostra,B.A., Amack,J.D. and Bertoli-Avella,A.M.
  TITLE     NPHP4 variants are associated with pleiotropic heart malformations
  JOURNAL   Circ Res 110 (12), 1564-1574 (2012)
   PUBMED   22550138
REFERENCE   4  (residues 1 to 1428)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 1428)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Wolf,M.T., O'Toole,J.F., Otto,E.A., Schultheiss,U.,
            Deschenes,G., Attanasio,M., Utsch,B., Antignac,C. and
            Hildebrandt,F.
  TITLE     Evidence of oligogenic inheritance in nephronophthisis
  JOURNAL   J Am Soc Nephrol 18 (10), 2789-2795 (2007)
   PUBMED   17855640
REFERENCE   7  (residues 1 to 1428)
  AUTHORS   Arts,H.H., Doherty,D., van Beersum,S.E., Parisi,M.A.,
            Letteboer,S.J., Gorden,N.T., Peters,T.A., Marker,T., Voesenek,K.,
            Kartono,A., Ozyurek,H., Farin,F.M., Kroes,H.Y., Wolfrum,U.,
            Brunner,H.G., Cremers,F.P., Glass,I.A., Knoers,N.V. and Roepman,R.
  TITLE     Mutations in the gene encoding the basal body protein RPGRIP1L, a
            nephrocystin-4 interactor, cause Joubert syndrome
  JOURNAL   Nat Genet 39 (7), 882-888 (2007)
   PUBMED   17558407
REFERENCE   8  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Sudbrak,R., Reinhardt,R., Lehrack,S., Hennig,S.,
            Imm,A., Muerb,U., Utsch,B., Attanasio,M., O'Toole,J.F., Otto,E. and
            Hildebrandt,F.
  TITLE     Mutational analysis of the NPHP4 gene in 250 patients with
            nephronophthisis
  JOURNAL   Hum Mutat 25 (4), 411 (2005)
   PUBMED   15776426
REFERENCE   9  (residues 1 to 1428)
  AUTHORS   Hoefele,J., Otto,E., Felten,H., Kuhn,K., Bley,T.A., Zauner,I.,
            Hildebrandt,F. and Neumann,H.P.
  TITLE     Clinical and histological presentation of 3 siblings with mutations
            in the NPHP4 gene
  JOURNAL   Am J Kidney Dis 43 (2), 358-364 (2004)
   PUBMED   14750102
REFERENCE   10 (residues 1 to 1428)
  AUTHORS   Otto,E., Hoefele,J., Ruf,R., Mueller,A.M., Hiller,K.S., Wolf,M.T.,
            Schuermann,M.J., Becker,A., Birkenhager,R., Sudbrak,R.,
            Hennies,H.C., Nurnberg,P. and Hildebrandt,F.
  TITLE     A gene mutated in nephronophthisis and retinitis pigmentosa encodes
            a novel protein, nephroretinin, conserved in evolution
  JOURNAL   Am J Hum Genet 71 (5), 1161-1167 (2002)
   PUBMED   12205563
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966033.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.22107.1,
                                           SRR26643298.30540.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1428
                     /product="nephrocystin-4 isoform a"
                     /note="nephronophthisis 4 (juvenile) homolog"
                     /calculated_mol_wt=158087
     Region          55..1420
                     /region_name="NPHP4"
                     /note="Nephrocystin-4; cd22239"
                     /db_xref="CDD:412072"
     CDS             1..1428
                     /gene="Nphp4"
                     /coded_by="NM_001436895.1:227..4513"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313749"
                     /db_xref="RGD:1560172"
ORIGIN      
        1 mddwhraftq ntlvpphpqr arqfgkesta fqcilkwldg plikqgildm lselechlrv
       61 slfdvtykhf fgrtwkttvk ptnqlskqpp rilfneplyf httlshpsiv avievvaegr
      121 krdgalqvls cgfgilrifg nkpesptsag qdkrlrlyhg tprallhpll qdpieqnrym
      181 tmmencslqy tlkphpplep afhllpenfl isglqqipgl lpphgdtgda lrkprfqkpt
      241 tlhlddlfft lypslekfee elvqllisdh fregvgllds gtlevlerrl hvcvhnglgf
      301 vhrpqvvvlv pemdmtltrs asfsrritas sksssgnqal vlrshlrlpe mvnhpsfaiv
      361 fqleyvfnsp sgadgsasss tslsslacmh mvrwavwnpd leagpgkvtl plqggvqhnp
      421 srclvykvps asmsseevkq vesgtiqfhf slssdalteh angpragrrs trkaltspsg
      481 tpalaardla aiqdspvgpg lslsqlaasp qslasqrsfk pppqpldgsq spegpqlqag
      541 svlesrishl eadlsqppfs vqgtptvehl qelpftplha pivvgaqtrs srsqlsraam
      601 vllqssgfpe ildarqqpve avnpmdpvrf npqkeesdcl lgneivlqfl afsraaqdcp
      661 gapwpqtvyf tfqfyrfppe ttprlqlvkl drtgkngsas lshilvhink dgsfdagspg
      721 fqlrymvdpg flkpgeqrwf aqylaaqtlq vdvwdgdsll ligsagiqmk hllrqgrpav
      781 qvshelevva teyeqemmvv sgdvagfgsv kpigvhtvvk grlhltlanv gheceprarg
      841 snalppsrsr visnngasff sggsllipgg pkrkrvvqaq kladvdsela amllthtrag
      901 qgpqavgqea davhrrkler mrlvrlqeag gdsdsrrisv larhsvraqh srdlqviday
      961 rertkaenia svlsqaitth htlyatlgta effefalknp hntqhtvaie idspelsiil
     1021 dsqewryfke atglltplee dmfhlrgsla pqlylrpret ahipfkfqnf svgppaptqa
     1081 paevisekda esgphwkcsa mptkhakvlf rvetgqliav lcltvepqph vvdqvfrfyh
     1141 peltflkkai rlppwhtlpg apvgmpgedp pvhvrcsdpn viceaqnvgl geprdvflkv
     1201 asgpspeikd ffvviyadrw lavpvqtwqv clhslqrvdv scvagqmtrl slvlrgtqtv
     1261 rkvraftshp qelktdpagv fvlpphgvqd lhvgvrprra gsrfihlnlv dvdyhqlvas
     1321 wlvclscrqp liskafeitm aagegkgank ritytnpyps rrtyrlhsdr pdllhfkeds
     1381 fqvaggetyt iglrflpsgs agqeeiliyi ndqddkneet fcvkvlyq
//
LOCUS       NP_001424078              59 aa            linear   ROD 27-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424078
VERSION     NP_001424078.1
DBSOURCE    REFSEQ: accession NM_001437149.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.549361.1,
                                           SRR26360190.411716.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437149.1:326..505"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001424076              59 aa            linear   ROD 27-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424076
VERSION     NP_001424076.1
DBSOURCE    REFSEQ: accession NM_001437147.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2159867.1,
                                           SRR22582419.1897513.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437147.1:209..388"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001424068             144 aa            linear   ROD 27-MAR-2025
DEFINITION  putative uncharacterized protein CIMIP3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424068 XP_038940424
VERSION     NP_001424068.1
DBSOURCE    REFSEQ: accession NM_001437139.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038940424.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3179837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..144
                     /product="putative uncharacterized protein CIMIP3 isoform
                     2"
                     /note="Guca1a neighbor"
                     /calculated_mol_wt=16556
     CDS             1..144
                     /gene="Cimip3"
                     /gene_synonym="Guca1anb"
                     /coded_by="NM_001437139.1:112..546"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100912849"
                     /db_xref="RGD:6485345"
ORIGIN      
        1 mdhavvttks glwserkrre legrvtpkes qkslipghrq kttsgrkgkk vppptptpls
       61 qkwkrdrkqs lesayvpvvv dprgqepdss frfnfynsqy snslnpfytl qkptcgylyq
      121 retdhtrkcf gippanlvlw rsty
//
LOCUS       NP_001424079              59 aa            linear   ROD 27-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424079
VERSION     NP_001424079.1
DBSOURCE    REFSEQ: accession NM_001437150.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.1636669.1,
                                           SRR22582419.609025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437150.1:521..700"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001424041            1592 aa            linear   ROD 27-MAR-2025
DEFINITION  transcription factor Gibbin [Rattus norvegicus].
ACCESSION   NP_001424041 XP_008762373
VERSION     NP_001424041.1
DBSOURCE    REFSEQ: accession NM_001437112.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1592)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_008762373.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.23034.1,
                                           SRR21887622.460945.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1592
                     /product="transcription factor Gibbin"
                     /note="A.T hook DNA-binding motif-containing protein 1;
                     AT-hook DNA-binding motif-containing protein 1"
                     /calculated_mol_wt=168046
     Region          <590..638
                     /region_name="DUF4683"
                     /note="Domain of unknown function (DUF4683); pfam15735"
                     /db_xref="CDD:464832"
     Region          <856..1047
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1592
                     /gene="Ahdc1"
                     /gene_synonym="RGD1310031"
                     /coded_by="NM_001437112.1:774..5552"
                     /db_xref="GeneID:362617"
                     /db_xref="RGD:1310031"
ORIGIN      
        1 mrvkpqglvv tssavcsspd ylrepkyypg gpptprpllp trppasppdk afsthtfsen
       61 prppprrdps srrppvlakg ddllppraar pvsqahcptp apdnnslrhw dngrvnlhpv
      121 vqlidimkdl trlsqdlqhs gvhldcgglr lsrppapppg dlqysffssp slansirspe
      181 eratphakpe rpnhplyepe peprdspqpg qghgpgatat atglppepep dgpdypelad
      241 adilselasl tcpeaqllea qaleppspqp epqlldpqpr fldpqalepl geglelpplq
      301 pladplglps ltlqaldtlp dslesqlldp qaldplpkll dvpgrrlepq qslghcqlae
      361 plrldlcsph gppgpeghpk yalrrtdrpk ilcrrrkagr grkvdsgpeg rllplpmptg
      421 laaalaeppp lpppppppal sgpvpelepe ssqtpmvptr kgkcrgvrrm vvkmakipvs
      481 lgrrnkttyk vsslssslsv egkelglrvs septpllkmk nngrnvvvvf ppgempiilk
      541 rkrgrppknl llgpgkpkep tvvaaeaaav taatmampev kkrrrrkqkl aspqpsyaad
      601 andskaeysd vlaklaflnr qsqcagrcsp prcwtpsepe svhqapdtqs isqflhrvqg
      661 frrrggktgg fggrggghaa kaarcsfsdf fegigkkkkv vavaatgvvg pgltelghpr
      721 krgrgevdav tgkpkrkrrs rkngtlfpeq vpsgpgfgea gaewagdkgg gwaphhghpg
      781 gqagrncgfq gtearafast glesgasgrg syyagapsgq telsqerqnl ftgyfrslld
      841 sddssdlldf alsasrpesr kasgnyagpp ssalpaqrgl atfpsrgakg spvavgnsga
      901 gtdpsfqpvl psrqtfppgr atsygitpat sdcraaetfp klapppsava rsptthppan
      961 typpqyggyg agqsvfapak pfsgqdcans kdcsfaygsg nslpaspssa hsagyapppt
     1021 ggpclppska sffnsseggp fsgsaptplr cdsrastvsp ggymvpkgtt asaasaasss
     1081 sssfqpspen crqfvgasqw pfrqgyggld waseafsqly npnfdchvse pnvildisny
     1141 tpqkvkqqta vsetfsesss dstqfnqpvg ggfrransea sssegqssls sleklmmdwn
     1201 eassapgynw nqsvlfqsss kpgrgrrkkv dlfeashlgf ststsatasg ypskrstgpr
     1261 qprggrgsga csakkerggt aakakfipkp qpvnplfqds pdlgldyysg dssmsplpsq
     1321 srafgvgerd pcdfmgpysm npstpsdgtf gqgfhcdsps lgapdldskh fpplahpptv
     1381 fdaglqkays ptcsptlgfk eelrpppskl taceplkhgl qgaslshaaq ahlscrdlpl
     1441 gqphyespsc kgtaywyppg saarsppyeg kvgsglladf lgrteavcls aphlasppat
     1501 pkadkeplem trppgpprgp aaatagygcp llsdltlspv prdsllplqd tayrypgfmp
     1561 qthpglgggp ksgflgpmae phpedtftvt sl
//
LOCUS       NP_001424085            1169 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424085 XP_063144147
VERSION     NP_001424085.1
DBSOURCE    REFSEQ: accession NM_001437156.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1169)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1169)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1169)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1169)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1169)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1169)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1169)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1169)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1169)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1169)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_063144147.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.29950.1,
                                           SRR26643299.25298.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1169
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1169
                     /product="polyamine-transporting ATPase 13A2 isoform 2"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=127032
     Region          39..1112
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1169
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437156.1:168..3677"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkt gtltedgldi mgvvplkgqm llplvpepch
      541 lppgpllral vtchalsqlh dtlvgdpmdl kmvestgwvl eegsaagsap etqvlvvmrp
      601 pprgpqqqee spepvsvlrr fpfssalqrm dvvvtwpgat qpeayvkgsp elvaslcspe
      661 tvprdfpqvl qsytaagyrv valagkplpt apsleaaqql trdtveqels llgllvmrnl
      721 lkpqttpviq tlrktgirtv mvtgdnlqta vtvakacgmv gtqehlaiih athpeqgqpa
      781 aleflpteps aamngakdpv qatdypvepe sqsrhlalsg stfavlqkhf pkllpkatvf
      841 armapeqktq lvcelqrlqy cvgmcgdgan dcgalkaadv gislsqaeas vvspftssma
      901 siecvptvir egrcsldtsf svfkymalys ltqfisvlil ytintnlgdl qflaidlfit
      961 ttvavlmsrt gpaltlvrar ppgallsvpv lgslllqval vagiqlggyf lviaqpwfvp
     1021 lnrtvpapdn lpnyentvif slsgfqylil aaavskgapf rqplytnvpf lvalallgsv
     1081 lvglilvpgl lqgplglrni adssfkllll glvafnfvga fmlesvldqc lpaclqwlrp
     1141 kraskkqfkq lqrelaerpw ptlpvgsvr
//
LOCUS       NP_001424088            1115 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424088 XP_063144148
VERSION     NP_001424088.1
DBSOURCE    REFSEQ: accession NM_001437159.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1115)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1115)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1115)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1115)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1115)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1115)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1115)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_063144148.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.21176.1,
                                           SRR26643298.29954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1115
                     /product="polyamine-transporting ATPase 13A2 isoform 6"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=120640
     Region          39..1067
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1115
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437159.1:168..3515"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkt gtltedgldi mgvvplkgqm llplvpepch
      541 lppgpllral vtchalsqlh dtlvgdpmdl kmvestgwvl eegsaagsap etqvlvvmrp
      601 pprgpqqqee spepvsvlrr fpfssalqrm dvvvtwpgat qpeayvkgsp elvaslcspe
      661 tvprdfpqvl qsytaagyrv valagkplpt apsleaaqql trdtveqels llgllvmrnl
      721 lkpqttpviq tlrktgirtv mvtgdnlqta vtvakacgmv gtqehlaiih athpeqgqpa
      781 aleflpteps aamngakdpv qatdypvepe sqsrhlalsg stfavlqkhf pkllpkatvf
      841 armapeqktq lvcelqrlqy cvgmcgdgan dcgalkaadv gislsqaeas vvspftssma
      901 siecvptvir egrcsldtsf svfkymalys ltqfisvlil ytintnlgdl qflaidlfit
      961 ttvavlmsrt gpaltlvrar ppgallsvpv lgslllqval vagiqlggyf lviaqpwfvp
     1021 lnrtvpapdn lpnyentvif slsgfqylil aaavskgapf rqplytngat rteehcgqlf
     1081 qvaaagsgrl qlcgrlhage ragpvspslp avaaa
//
LOCUS       NP_663707                371 aa            linear   ROD 27-MAR-2025
DEFINITION  N-acetyllactosaminide alpha-1,3-galactosyltransferase isoform 1
            [Rattus norvegicus].
ACCESSION   NP_663707
VERSION     NP_663707.1
DBSOURCE    REFSEQ: accession NM_145674.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Fullmer,J.M., Riedl,M., Williams,F.G., Sandrin,M. and Elde,R.
  TITLE     Enzymes that synthesize the IB4 epitope are not sufficient to
            impart IB4 binding in dorsal root ganglia of rat
  JOURNAL   J Comp Neurol 501 (1), 70-82 (2007)
   PUBMED   17206613
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Taylor,S.G., McKenzie,I.F. and Sandrin,M.S.
  TITLE     Characterization of the rat alpha(1,3)galactosyltransferase:
            evidence for two independent genes encoding glycosyltransferases
            that synthesize Galalpha(1,3)Gal by two separate glycosylation
            pathways
  JOURNAL   Glycobiology 13 (5), 327-337 (2003)
   PUBMED   12626403
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ222249.1, SRR26643297.11073.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786, SAMN16676788
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..371
                     /product="N-acetyllactosaminide
                     alpha-1,3-galactosyltransferase isoform 1"
                     /EC_number="2.4.1.87"
                     /note="glycoprotein galactosyltransferase alpha 1, 3;
                     N-acetyllactosaminide alpha-1,3-galactosyltransferase;
                     glycoprotein, alpha-galactosyltransferase 1,3;
                     UDP-galactose:beta-D-galactosyl-1,
                     4-N-acetyl-D-glucosaminide
                     alpha-1,3-galactosyltransferase"
                     /calculated_mol_wt=43411
     Site            41..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3L7M0.2)"
     Region          86..369
                     /region_name="Glyco_transf_6"
                     /note="Glycosyltransferase family 6; pfam03414"
                     /db_xref="CDD:427285"
     Site            order(137..139,142,201,205,228..230,362,364,368)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133008"
     Site            order(137..139,142,228..230,250..253,262,281,317,320)
                     /site_type="active"
                     /db_xref="CDD:133008"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3L7M0.2)"
     CDS             1..371
                     /gene="Ggta1"
                     /gene_synonym="Ggta1p"
                     /coded_by="NM_145674.2:378..1493"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:246766"
                     /db_xref="RGD:629476"
ORIGIN      
        1 mvtmpqdlhv kvsmsrskse tsllssrsgs qekimnvkgk iilsvlmvst vlvvfweyvn
       61 rthsyqeedi erarekgrng dsivepqlwd wfnpknrpev ltvtpwkapi vwegtydtal
      121 lekyyarqki tvgltvfavg kyiehyledf lesankyfmv ghrvifyvmm ddtsrmpavh
      181 lsplhslqvf eirsekrwqd ismmrmktig ehildhiqhe vdflfcmdvd qvfqdnfgve
      241 tlgqlvaqlq awwykaspde ftyerrelsa ayipfgegdf yyhaavfggt pvhilnltre
      301 cfkgilqdkk hdieaqwhde shlnkyflfn kptkilspey cwdyhiglps diknvkiawq
      361 tkeynlvrsn v
//
LOCUS       NP_001424034             364 aa            linear   ROD 27-MAR-2025
DEFINITION  ecto-ADP-ribosyltransferase 3 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424034 XP_006250790
VERSION     NP_001424034.1
DBSOURCE    REFSEQ: accession NM_001437105.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Shi,W., Gong,P., Fan,J., Yan,Y.H., Ni,L., Wu,X., Cui,G., Wu,X.,
            Gu,X. and Chen,J.
  TITLE     The expression pattern of ADP-ribosyltransferase 3 in rat traumatic
            brain injury
  JOURNAL   J Mol Histol 43 (1), 37-47 (2012)
   PUBMED   22037978
  REMARK    GeneRIF: ART3 may play important roles in CNS pathophysiology after
            traumatic brain injury (TBI).
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Wang,B., Golemis,E.A. and Kruh,G.D.
  TITLE     ArgBP2, a multiple Src homology 3 domain-containing,
            Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed
            cells and localized in stress fibers and cardiocyte Z-disks
  JOURNAL   J Biol Chem 272 (28), 17542-17550 (1997)
   PUBMED   9211900
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Koch-Nolte,F., Haag,F., Braren,R., Kuhl,M., Hoovers,J.,
            Balasubramanian,S., Bazan,F. and Thiele,H.G.
  TITLE     Two novel human members of an emerging mammalian gene family
            related to mono-ADP-ribosylating bacterial toxins
  JOURNAL   Genomics 39 (3), 370-376 (1997)
   PUBMED   9119374
  REMARK    Erratum:[Genomics 1999 Jan 1;55(1):130]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006250790.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.49565.1,
                                           SRR26643288.51094.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..364
                     /product="ecto-ADP-ribosyltransferase 3 isoform 2
                     precursor"
                     /EC_number="2.4.2.31"
                     /note="ecto-ADP-ribosyltransferase 3"
                     /calculated_mol_wt=37675
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2925
     Region          29..251
                     /region_name="VIP2"
                     /note="A family of actin-ADP-ribosylating toxin. A member
                     of the Bacillus-prodiced vegetative insecticidal proteins
                     (VIPs) possesses high specificity against the major insect
                     pest, corn rootworms, and belongs to a classs of binary
                     toxins and regulators of...; cl00173"
                     /db_xref="CDD:469640"
     CDS             1..364
                     /gene="Art3"
                     /coded_by="NM_001437105.1:123..1217"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:305235"
                     /db_xref="RGD:628833"
ORIGIN      
        1 mkmghfelvt tllaamvlmd vfqvqaevld maenvfddey lkcnsrmemk yiprmhgeel
       61 andellqsvw dkagiqweaq kaqlslpknf kdaygialta yvteaqdqsp fyhtfnravk
      121 iaglsrrryi ynfpfkafhf ylvralqllr rpceesyknv vystspnisf afgeqnqarl
      181 gnftlaysak pqtaneqrll tiqtcfgvav gkllnkeseg ivliplsevf qvsrkgtddd
      241 lilhsinstc syyecsflgg lkagscttnp enpdpgylnn pgrksldsvk mpeikvlqge
      301 enpllpdekp edrnrgkanv ptpglvpvpg pkshpssssg hrllpsdtas tilliaaavd
      361 fial
//
LOCUS       NP_001424063             328 aa            linear   ROD 27-MAR-2025
DEFINITION  putative P2Y purinoceptor 10 [Rattus norvegicus].
ACCESSION   NP_001424063
VERSION     NP_001424063.1
DBSOURCE    REFSEQ: accession NM_001437134.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.65743.1,
                                           SRR26360186.1830181.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..328
                     /product="putative P2Y purinoceptor 10"
                     /note="purinergic receptor P2Y, G-protein coupled, 10;
                     purinergic receptor P2Y10"
                     /calculated_mol_wt=37149
     Region          23..305
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          25..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          58..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          95..117
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          139..155
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          185..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          231..253
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          273..298
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..328
                     /gene="P2ry10"
                     /gene_synonym="RGD1561912"
                     /coded_by="NM_001437134.1:394..1380"
                     /db_xref="GeneID:317219"
                     /db_xref="RGD:1561912"
ORIGIN      
        1 mgsnststve sncnainvtf qnslyattyi fifipgllan saalwvlfrf iskknkaiif
       61 minlsvadla hilslplriy yyinrhwpfq ralcllcfyl kylnmyasif fltcislqrc
      121 lfllkpfrar nwkrrydvgi saavwiivgt aclpfpimrs aglanntdsc fadlgykqmd
      181 plvlvtmiti aelagfvipv ltiacctwkt tvslkhppia fqgiserkka lrmvfmcaav
      241 fvicftpyhi nfifytmvke niitscpivk samyfhpfsl claslcclld pilyyfmase
      301 frdqlsrhgs svtrsrlmsr esgssmvs
//
LOCUS       NP_001424061             371 aa            linear   ROD 27-MAR-2025
DEFINITION  N-acetyllactosaminide alpha-1,3-galactosyltransferase isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001424061 XP_006234095
VERSION     NP_001424061.1
DBSOURCE    REFSEQ: accession NM_001437132.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Fullmer,J.M., Riedl,M., Williams,F.G., Sandrin,M. and Elde,R.
  TITLE     Enzymes that synthesize the IB4 epitope are not sufficient to
            impart IB4 binding in dorsal root ganglia of rat
  JOURNAL   J Comp Neurol 501 (1), 70-82 (2007)
   PUBMED   17206613
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Taylor,S.G., McKenzie,I.F. and Sandrin,M.S.
  TITLE     Characterization of the rat alpha(1,3)galactosyltransferase:
            evidence for two independent genes encoding glycosyltransferases
            that synthesize Galalpha(1,3)Gal by two separate glycosylation
            pathways
  JOURNAL   Glycobiology 13 (5), 327-337 (2003)
   PUBMED   12626403
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006234095.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166599.1, SRR26643429.11435.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840111 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..371
                     /product="N-acetyllactosaminide
                     alpha-1,3-galactosyltransferase isoform 1"
                     /EC_number="2.4.1.87"
                     /note="glycoprotein galactosyltransferase alpha 1, 3;
                     N-acetyllactosaminide alpha-1,3-galactosyltransferase;
                     glycoprotein, alpha-galactosyltransferase 1,3;
                     UDP-galactose:beta-D-galactosyl-1,
                     4-N-acetyl-D-glucosaminide
                     alpha-1,3-galactosyltransferase"
                     /calculated_mol_wt=43411
     Site            41..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3L7M0.2)"
     Region          86..369
                     /region_name="Glyco_transf_6"
                     /note="Glycosyltransferase family 6; pfam03414"
                     /db_xref="CDD:427285"
     Site            order(137..139,142,201,205,228..230,362,364,368)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133008"
     Site            order(137..139,142,228..230,250..253,262,281,317,320)
                     /site_type="active"
                     /db_xref="CDD:133008"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3L7M0.2)"
     CDS             1..371
                     /gene="Ggta1"
                     /gene_synonym="Ggta1p"
                     /coded_by="NM_001437132.1:392..1507"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:246766"
                     /db_xref="RGD:629476"
ORIGIN      
        1 mvtmpqdlhv kvsmsrskse tsllssrsgs qekimnvkgk iilsvlmvst vlvvfweyvn
       61 rthsyqeedi erarekgrng dsivepqlwd wfnpknrpev ltvtpwkapi vwegtydtal
      121 lekyyarqki tvgltvfavg kyiehyledf lesankyfmv ghrvifyvmm ddtsrmpavh
      181 lsplhslqvf eirsekrwqd ismmrmktig ehildhiqhe vdflfcmdvd qvfqdnfgve
      241 tlgqlvaqlq awwykaspde ftyerrelsa ayipfgegdf yyhaavfggt pvhilnltre
      301 cfkgilqdkk hdieaqwhde shlnkyflfn kptkilspey cwdyhiglps diknvkiawq
      361 tkeynlvrsn v
//
LOCUS       NP_001128428            1592 aa            linear   ROD 27-MAR-2025
DEFINITION  transcription factor Gibbin [Rattus norvegicus].
ACCESSION   NP_001128428 XP_017449006 XP_342937
VERSION     NP_001128428.1
DBSOURCE    REFSEQ: accession NM_001134956.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1592)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 27, 2025 this sequence version replaced
            XP_017449006.1, XP_342937.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR21887621.101430.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760386, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1592
                     /product="transcription factor Gibbin"
                     /note="A.T hook DNA-binding motif-containing protein 1;
                     AT-hook DNA-binding motif-containing protein 1"
                     /calculated_mol_wt=168046
     Region          <590..638
                     /region_name="DUF4683"
                     /note="Domain of unknown function (DUF4683); pfam15735"
                     /db_xref="CDD:464832"
     Region          <856..1047
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1592
                     /gene="Ahdc1"
                     /gene_synonym="RGD1310031"
                     /coded_by="NM_001134956.2:788..5566"
                     /db_xref="GeneID:362617"
                     /db_xref="RGD:1310031"
ORIGIN      
        1 mrvkpqglvv tssavcsspd ylrepkyypg gpptprpllp trppasppdk afsthtfsen
       61 prppprrdps srrppvlakg ddllppraar pvsqahcptp apdnnslrhw dngrvnlhpv
      121 vqlidimkdl trlsqdlqhs gvhldcgglr lsrppapppg dlqysffssp slansirspe
      181 eratphakpe rpnhplyepe peprdspqpg qghgpgatat atglppepep dgpdypelad
      241 adilselasl tcpeaqllea qaleppspqp epqlldpqpr fldpqalepl geglelpplq
      301 pladplglps ltlqaldtlp dslesqlldp qaldplpkll dvpgrrlepq qslghcqlae
      361 plrldlcsph gppgpeghpk yalrrtdrpk ilcrrrkagr grkvdsgpeg rllplpmptg
      421 laaalaeppp lpppppppal sgpvpelepe ssqtpmvptr kgkcrgvrrm vvkmakipvs
      481 lgrrnkttyk vsslssslsv egkelglrvs septpllkmk nngrnvvvvf ppgempiilk
      541 rkrgrppknl llgpgkpkep tvvaaeaaav taatmampev kkrrrrkqkl aspqpsyaad
      601 andskaeysd vlaklaflnr qsqcagrcsp prcwtpsepe svhqapdtqs isqflhrvqg
      661 frrrggktgg fggrggghaa kaarcsfsdf fegigkkkkv vavaatgvvg pgltelghpr
      721 krgrgevdav tgkpkrkrrs rkngtlfpeq vpsgpgfgea gaewagdkgg gwaphhghpg
      781 gqagrncgfq gtearafast glesgasgrg syyagapsgq telsqerqnl ftgyfrslld
      841 sddssdlldf alsasrpesr kasgnyagpp ssalpaqrgl atfpsrgakg spvavgnsga
      901 gtdpsfqpvl psrqtfppgr atsygitpat sdcraaetfp klapppsava rsptthppan
      961 typpqyggyg agqsvfapak pfsgqdcans kdcsfaygsg nslpaspssa hsagyapppt
     1021 ggpclppska sffnsseggp fsgsaptplr cdsrastvsp ggymvpkgtt asaasaasss
     1081 sssfqpspen crqfvgasqw pfrqgyggld waseafsqly npnfdchvse pnvildisny
     1141 tpqkvkqqta vsetfsesss dstqfnqpvg ggfrransea sssegqssls sleklmmdwn
     1201 eassapgynw nqsvlfqsss kpgrgrrkkv dlfeashlgf ststsatasg ypskrstgpr
     1261 qprggrgsga csakkerggt aakakfipkp qpvnplfqds pdlgldyysg dssmsplpsq
     1321 srafgvgerd pcdfmgpysm npstpsdgtf gqgfhcdsps lgapdldskh fpplahpptv
     1381 fdaglqkays ptcsptlgfk eelrpppskl taceplkhgl qgaslshaaq ahlscrdlpl
     1441 gqphyespsc kgtaywyppg saarsppyeg kvgsglladf lgrteavcls aphlasppat
     1501 pkadkeplem trppgpprgp aaatagygcp llsdltlspv prdsllplqd tayrypgfmp
     1561 qthpglgggp ksgflgpmae phpedtftvt sl
//
LOCUS       NP_001424062             337 aa            linear   ROD 27-MAR-2025
DEFINITION  N-acetyllactosaminide alpha-1,3-galactosyltransferase isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001424062 XP_008759924
VERSION     NP_001424062.1
DBSOURCE    REFSEQ: accession NM_001437133.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Fullmer,J.M., Riedl,M., Williams,F.G., Sandrin,M. and Elde,R.
  TITLE     Enzymes that synthesize the IB4 epitope are not sufficient to
            impart IB4 binding in dorsal root ganglia of rat
  JOURNAL   J Comp Neurol 501 (1), 70-82 (2007)
   PUBMED   17206613
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Taylor,S.G., McKenzie,I.F. and Sandrin,M.S.
  TITLE     Characterization of the rat alpha(1,3)galactosyltransferase:
            evidence for two independent genes encoding glycosyltransferases
            that synthesize Galalpha(1,3)Gal by two separate glycosylation
            pathways
  JOURNAL   Glycobiology 13 (5), 327-337 (2003)
   PUBMED   12626403
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Mar 27, 2025 this sequence version replaced XP_008759924.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.7719.1,
                                           SRR26643299.13694.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840111 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..337
                     /product="N-acetyllactosaminide
                     alpha-1,3-galactosyltransferase isoform 2"
                     /EC_number="2.4.1.87"
                     /note="glycoprotein galactosyltransferase alpha 1, 3;
                     N-acetyllactosaminide alpha-1,3-galactosyltransferase;
                     glycoprotein, alpha-galactosyltransferase 1,3;
                     UDP-galactose:beta-D-galactosyl-1,
                     4-N-acetyl-D-glucosaminide
                     alpha-1,3-galactosyltransferase"
                     /calculated_mol_wt=39664
     Region          52..335
                     /region_name="Glyco_transf_6"
                     /note="Glycosyltransferase family 6; pfam03414"
                     /db_xref="CDD:427285"
     Site            order(103..105,108,167,171,194..196,328,330,334)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133008"
     Site            order(103..105,108,194..196,216..219,228,247,283,286)
                     /site_type="active"
                     /db_xref="CDD:133008"
     CDS             1..337
                     /gene="Ggta1"
                     /gene_synonym="Ggta1p"
                     /coded_by="NM_001437133.1:317..1330"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:246766"
                     /db_xref="RGD:629476"
ORIGIN      
        1 mnvkgkiils vlmvstvlvv fweyvnrths yqeedierar ekgrngdsiv epqlwdwfnp
       61 knrpevltvt pwkapivweg tydtalleky yarqkitvgl tvfavgkyie hyledflesa
      121 nkyfmvghrv ifyvmmddts rmpavhlspl hslqvfeirs ekrwqdismm rmktigehil
      181 dhiqhevdfl fcmdvdqvfq dnfgvetlgq lvaqlqawwy kaspdeftye rrelsaayip
      241 fgegdfyyha avfggtpvhi lnltrecfkg ilqdkkhdie aqwhdeshln kyflfnkptk
      301 ilspeycwdy higlpsdikn vkiawqtkey nlvrsnv
//
LOCUS       NP_001424086            1119 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424086 XP_006239312
VERSION     NP_001424086.1
DBSOURCE    REFSEQ: accession NM_001437157.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006239312.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.29949.1,
                                           SRR26643284.8281.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1119
                     /product="polyamine-transporting ATPase 13A2 isoform 4"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=121079
     Region          39..1071
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1119
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437157.1:168..3527"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkt gtltedgldi mgvvplkgqm llplvpepch
      541 lppgpllral vtchalsqlh dtlvgdpmdl kmvestgwvl eegsaagsap etqvlvvmrp
      601 pprgpqqqee spepvsvlrr fpfssalqrm dvvvtwpgat qpeayvkgsp elvaslcspe
      661 tvprdfpqvl qsytaagyrv valagkplpt apsleaaqql trdtveqels llgllvmrnl
      721 lkpqttpviq tlrktgirtv mvtgdnlqta vtvakacgmv gtqehlaiih athpeqgqpa
      781 aleflpteps aamngakdpv qatdypvepe sqsrhlalsg stfavlqkhf pkllpkvlvq
      841 atvfarmape qktqlvcelq rlqycvgmcg dgandcgalk aadvgislsq aeasvvspft
      901 ssmasiecvp tviregrcsl dtsfsvfkym alysltqfis vlilytintn lgdlqflaid
      961 lfitttvavl msrtgpaltl vrarppgall svpvlgslll qvalvagiql ggyflviaqp
     1021 wfvplnrtvp apdnlpnyen tvifslsgfq ylilaaavsk gapfrqplyt ngatrteehc
     1081 gqlfqvaaag sgrlqlcgrl hageragpvs pslpavaaa
//
LOCUS       NP_001424075              59 aa            linear   ROD 27-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424075
VERSION     NP_001424075.1
DBSOURCE    REFSEQ: accession NM_001437146.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR23984936.251610.1,
                                           SRR26360190.1447954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093046, SAMN17050749
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437146.1:216..395"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001102917             423 aa            linear   ROD 27-MAR-2025
DEFINITION  galactosylceramide sulfotransferase [Rattus norvegicus].
ACCESSION   NP_001102917 XP_001067165
VERSION     NP_001102917.2
DBSOURCE    REFSEQ: accession NM_001109447.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Honke,K., Hirahara,Y., Dupree,J., Suzuki,K., Popko,B.,
            Fukushima,K., Fukushima,J., Nagasawa,T., Yoshida,N., Wada,Y. and
            Taniguchi,N.
  TITLE     Paranodal junction formation and spermatogenesis require
            sulfoglycolipids
  JOURNAL   Proc Natl Acad Sci U S A 99 (7), 4227-4232 (2002)
   PUBMED   11917099
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Hirahara,Y., Tsuda,M., Wada,Y. and Honke,K.
  TITLE     cDNA cloning, genomic cloning, and tissue-specific regulation of
            mouse cerebroside sulfotransferase
  JOURNAL   Eur J Biochem 267 (7), 1909-1917 (2000)
   PUBMED   10727929
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced NP_001102917.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360194.1412120.1, SRR26360190.409382.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            inferred exon combination        :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..423
                     /product="galactosylceramide sulfotransferase"
                     /EC_number="2.8.2.11"
                     /calculated_mol_wt=48787
     Region          4..408
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; cl22970"
                     /db_xref="CDD:451469"
     CDS             1..423
                     /gene="Gal3st1"
                     /coded_by="NM_001109447.2:423..1694"
                     /db_xref="GeneID:683713"
                     /db_xref="RGD:1583379"
ORIGIN      
        1 mtllpkkpck skakglvlga lltsflllly syvvpplypn lafttseaaa pcspvpnepv
       61 aatpangsag gcqprrdivf mkthktasst llnilfrfgq khelkfafpn grndfhypsy
      121 farslvqdyr pgacfniicn hmrfhyeevr glvrpgatfi tvirdparlf essfhyfgsv
      181 vpltwklssr dklaeflqdp dryydpssyn ahylrnllff dlgydssldp gsprvqehil
      241 everrfhlvl lqeyfdeslv llrellcwdl edvlyfklna rrdspeprls gelyrrataw
      301 nlldvrlyrh fnasfwrkve afgrermase vaklrraneh mrsicidggq avdaeaiqds
      361 amqpwqplgi ksilgynlkk sigpqheqlc rrmltpeiqy lsdlganlwi tklwkffrdf
      421 lrw
//
LOCUS       NP_001424080              59 aa            linear   ROD 27-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424080 XP_038937633
VERSION     NP_001424080.1
DBSOURCE    REFSEQ: accession NM_001437151.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038937633.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.467054.1,
                                           SRR22582416.1266474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437151.1:478..657"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001424042            1592 aa            linear   ROD 27-MAR-2025
DEFINITION  transcription factor Gibbin [Rattus norvegicus].
ACCESSION   NP_001424042 XP_038966325
VERSION     NP_001424042.1
DBSOURCE    REFSEQ: accession NM_001437113.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1592)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038966325.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.24680.1,
                                           SRR26643289.16421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1592
                     /product="transcription factor Gibbin"
                     /note="A.T hook DNA-binding motif-containing protein 1;
                     AT-hook DNA-binding motif-containing protein 1"
                     /calculated_mol_wt=168046
     Region          <590..638
                     /region_name="DUF4683"
                     /note="Domain of unknown function (DUF4683); pfam15735"
                     /db_xref="CDD:464832"
     Region          <856..1047
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1592
                     /gene="Ahdc1"
                     /gene_synonym="RGD1310031"
                     /coded_by="NM_001437113.1:672..5450"
                     /db_xref="GeneID:362617"
                     /db_xref="RGD:1310031"
ORIGIN      
        1 mrvkpqglvv tssavcsspd ylrepkyypg gpptprpllp trppasppdk afsthtfsen
       61 prppprrdps srrppvlakg ddllppraar pvsqahcptp apdnnslrhw dngrvnlhpv
      121 vqlidimkdl trlsqdlqhs gvhldcgglr lsrppapppg dlqysffssp slansirspe
      181 eratphakpe rpnhplyepe peprdspqpg qghgpgatat atglppepep dgpdypelad
      241 adilselasl tcpeaqllea qaleppspqp epqlldpqpr fldpqalepl geglelpplq
      301 pladplglps ltlqaldtlp dslesqlldp qaldplpkll dvpgrrlepq qslghcqlae
      361 plrldlcsph gppgpeghpk yalrrtdrpk ilcrrrkagr grkvdsgpeg rllplpmptg
      421 laaalaeppp lpppppppal sgpvpelepe ssqtpmvptr kgkcrgvrrm vvkmakipvs
      481 lgrrnkttyk vsslssslsv egkelglrvs septpllkmk nngrnvvvvf ppgempiilk
      541 rkrgrppknl llgpgkpkep tvvaaeaaav taatmampev kkrrrrkqkl aspqpsyaad
      601 andskaeysd vlaklaflnr qsqcagrcsp prcwtpsepe svhqapdtqs isqflhrvqg
      661 frrrggktgg fggrggghaa kaarcsfsdf fegigkkkkv vavaatgvvg pgltelghpr
      721 krgrgevdav tgkpkrkrrs rkngtlfpeq vpsgpgfgea gaewagdkgg gwaphhghpg
      781 gqagrncgfq gtearafast glesgasgrg syyagapsgq telsqerqnl ftgyfrslld
      841 sddssdlldf alsasrpesr kasgnyagpp ssalpaqrgl atfpsrgakg spvavgnsga
      901 gtdpsfqpvl psrqtfppgr atsygitpat sdcraaetfp klapppsava rsptthppan
      961 typpqyggyg agqsvfapak pfsgqdcans kdcsfaygsg nslpaspssa hsagyapppt
     1021 ggpclppska sffnsseggp fsgsaptplr cdsrastvsp ggymvpkgtt asaasaasss
     1081 sssfqpspen crqfvgasqw pfrqgyggld waseafsqly npnfdchvse pnvildisny
     1141 tpqkvkqqta vsetfsesss dstqfnqpvg ggfrransea sssegqssls sleklmmdwn
     1201 eassapgynw nqsvlfqsss kpgrgrrkkv dlfeashlgf ststsatasg ypskrstgpr
     1261 qprggrgsga csakkerggt aakakfipkp qpvnplfqds pdlgldyysg dssmsplpsq
     1321 srafgvgerd pcdfmgpysm npstpsdgtf gqgfhcdsps lgapdldskh fpplahpptv
     1381 fdaglqkays ptcsptlgfk eelrpppskl taceplkhgl qgaslshaaq ahlscrdlpl
     1441 gqphyespsc kgtaywyppg saarsppyeg kvgsglladf lgrteavcls aphlasppat
     1501 pkadkeplem trppgpprgp aaatagygcp llsdltlspv prdsllplqd tayrypgfmp
     1561 qthpglgggp ksgflgpmae phpedtftvt sl
//
LOCUS       NP_001424067             119 aa            linear   ROD 27-MAR-2025
DEFINITION  putative uncharacterized protein CIMIP3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424067 XP_038940429
VERSION     NP_001424067.1
DBSOURCE    REFSEQ: accession NM_001437138.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038940429.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2483652.1,
                                           SRR26643293.49057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..119
                     /product="putative uncharacterized protein CIMIP3 isoform
                     1"
                     /note="Guca1a neighbor"
                     /calculated_mol_wt=13679
     CDS             1..119
                     /gene="Cimip3"
                     /gene_synonym="Guca1anb"
                     /coded_by="NM_001437138.1:87..446"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100912849"
                     /db_xref="RGD:6485345"
ORIGIN      
        1 mlkesqksli pghrqkttsg rkgkkvpppt ptplsqkwkr drkqslesay vpvvvdprgq
       61 epdssfrfnf ynsqysnsln pfytlqkptc gylyqretdh trkcfgippa nlvlwrsty
//
LOCUS       NP_001424047             239 aa            linear   ROD 27-MAR-2025
DEFINITION  calcipressin-3 [Rattus norvegicus].
ACCESSION   NP_001424047 XP_038966333
VERSION     NP_001424047.1
DBSOURCE    REFSEQ: accession NM_001437118.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Guasch,A., Aranguren-Ibanez,A., Perez-Luque,R., Aparicio,D.,
            Martinez-Hoyer,S., Mulero,M.C., Serrano-Candelas,E., Perez-Riba,M.
            and Fita,I.
  TITLE     Calcineurin Undergoes a Conformational Switch Evoked via
            Peptidyl-Prolyl Isomerization
  JOURNAL   PLoS One 10 (8), e0134569 (2015)
   PUBMED   26248042
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Canaider,S., Facchin,F., Griffoni,C., Casadei,R., Vitale,L.,
            Lenzi,L., Frabetti,F., D'Addabbo,P., Carinci,P., Zannotti,M. and
            Strippoli,P.
  TITLE     Proteins encoded by human Down syndrome critical region gene 1-like
            2 (DSCR1L2) mRNA and by a novel DSCR1L2 mRNA isoform interact with
            cardiac troponin I (TNNI3)
  JOURNAL   Gene 372, 128-136 (2006)
   PUBMED   16516408
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038966333.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.16610.1,
                                           SRR26643296.16395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..239
                     /product="calcipressin-3"
                     /note="regulator of calcineurin 3; Down syndrome critical
                     region gene 1-like 2"
                     /calculated_mol_wt=27050
     Region          58..225
                     /region_name="Calcipressin"
                     /note="pfam04847"
                     /db_xref="CDD:282674"
     CDS             1..239
                     /gene="Rcan3"
                     /gene_synonym="Dscr1l2"
                     /coded_by="NM_001437118.1:412..1131"
                     /db_xref="GeneID:362627"
                     /db_xref="RGD:1311826"
ORIGIN      
        1 mlrdslkswn dsqsdlcssd qeeeeemvfg eneddleemm dlsdlptslf acsvheavfe
       61 vqeqkerfea lftlyddqvt fqlfksfrrv rinfskpeaa ararielhes efhgrklkly
      121 faqvqvsgea rdksyllppq ptkqflispp asppvgwkqs edatpvinyd llcavsklgp
      181 gekyelhagt estpsvvvhv ceseteeeed tknpkqkitq trrpeaptaa lserldcal
//
LOCUS       NP_001424087            1118 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424087 XP_006239313
VERSION     NP_001424087.1
DBSOURCE    REFSEQ: accession NM_001437158.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1118)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1118)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1118)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1118)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1118)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1118)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1118)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1118)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1118)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1118)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006239313.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212004.1, SRR22582424.1103289.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1118
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1118
                     /product="polyamine-transporting ATPase 13A2 isoform 5"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=120951
     Region          39..1070
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1118
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437158.1:168..3524"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeaqvlryy ilqgqryvwm etqqafcqvs
      181 lldhgracdd ihcsssglsl qdqavrktiy gpnvigipvk sylqllvdea lnpyygfqaf
      241 sialwladhy ywyavcifli saisiclsly ktrkqsmtlr dmvklsvrvq vcrpggeeew
      301 vdsselvpgd clvlpqeggm mpcdaalvag ecvvnesslt gesipvlkta lpegpqpycp
      361 ethrrhtlfc gtlvlqaray lgprvlavvt rtgfctakgg lvssilhprp isfkfyrhsm
      421 kfvaalsvla llgtiysiii lyrnrvpvke iviraldlvt vvvppalpaa mtvctlyaqs
      481 rlrtqgifci hplrinlggk lrlvcfdktg tltedgldim gvvplkgqml lplvpepchl
      541 ppgpllralv tchalsqlhd tlvgdpmdlk mvestgwvle egsaagsape tqvlvvmrpp
      601 prgpqqqees pepvsvlrrf pfssalqrmd vvvtwpgatq peayvkgspe lvaslcspet
      661 vprdfpqvlq sytaagyrvv alagkplpta psleaaqqlt rdtveqelsl lgllvmrnll
      721 kpqttpviqt lrktgirtvm vtgdnlqtav tvakacgmvg tqehlaiiha thpeqgqpaa
      781 leflptepsa amngakdpvq atdypvepes qsrhlalsgs tfavlqkhfp kllpkvlvqa
      841 tvfarmapeq ktqlvcelqr lqycvgmcgd gandcgalka advgislsqa easvvspfts
      901 smasiecvpt viregrcsld tsfsvfkyma lysltqfisv lilytintnl gdlqflaidl
      961 fitttvavlm srtgpaltlv rarppgalls vpvlgslllq valvagiqlg gyflviaqpw
     1021 fvplnrtvpa pdnlpnyent vifslsgfqy lilaaavskg apfrqplytn gatrteehcg
     1081 qlfqvaaags grlqlcgrlh ageragpvsp slpavaaa
//
LOCUS       NP_001424089            1104 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424089 XP_063144149
VERSION     NP_001424089.1
DBSOURCE    REFSEQ: accession NM_001437160.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1104)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1104)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1104)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1104)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_063144149.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21615.1,
                                           SRR26643297.20924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1104
                     /product="polyamine-transporting ATPase 13A2 isoform 7"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=120120
     Region          39..1047
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1104
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437160.1:168..3482"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkv leegsaagsa petqvlvvmr ppprgpqqqe
      541 espepvsvlr rfpfssalqr mdvvvtwpga tqpeayvkgs pelvaslcsp etvprdfpqv
      601 lqsytaagyr vvalagkplp tapsleaaqq ltrdtveqel sllgllvmrn llkpqttpvi
      661 qtlrktgirt vmvtgdnlqt avtvakacgm vgtqehlaii hathpeqgqp aaleflptep
      721 saamngakdp vqatdypvep esqsrhlals gstfavlqkh fpkllpkvlv qatvfarmap
      781 eqktqlvcel qrlqycvgmc gdgandcgal kaadvgisls qaeasvvspf tssmasiecv
      841 ptviregrcs ldtsfsvfky malysltqfi svlilytint nlgdlqflai dlfitttvav
      901 lmsrtgpalt lvrarppgal lsvpvlgsll lqvalvagiq lggyflviaq pwfvplnrtv
      961 papdnlpnye ntvifslsgf qylilaaavs kgapfrqply tnvpflvala llgsvlvgli
     1021 lvpgllqgpl glrniadssf kllllglvaf nfvgafmles vldqclpacl qwlrpkrask
     1081 kqfkqlqrel aerpwptlpv gsvr
//
LOCUS       NP_001424069             144 aa            linear   ROD 27-MAR-2025
DEFINITION  putative uncharacterized protein CIMIP3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424069 XP_038940423
VERSION     NP_001424069.1
DBSOURCE    REFSEQ: accession NM_001437140.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038940423.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2683837.1,
                                           SRR26360181.3292085.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..144
                     /product="putative uncharacterized protein CIMIP3 isoform
                     2"
                     /note="Guca1a neighbor"
                     /calculated_mol_wt=16556
     CDS             1..144
                     /gene="Cimip3"
                     /gene_synonym="Guca1anb"
                     /coded_by="NM_001437140.1:252..686"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:100912849"
                     /db_xref="RGD:6485345"
ORIGIN      
        1 mdhavvttks glwserkrre legrvtpkes qkslipghrq kttsgrkgkk vppptptpls
       61 qkwkrdrkqs lesayvpvvv dprgqepdss frfnfynsqy snslnpfytl qkptcgylyq
      121 retdhtrkcf gippanlvlw rsty
//
LOCUS       NP_067735                502 aa            linear   ROD 27-MAR-2025
DEFINITION  A-kinase anchor protein 14 [Rattus norvegicus].
ACCESSION   NP_067735
VERSION     NP_067735.1
DBSOURCE    REFSEQ: accession NM_021703.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Carnegie,G.K., Means,C.K. and Scott,J.D.
  TITLE     A-kinase anchoring proteins: from protein complexes to physiology
            and disease
  JOURNAL   IUBMB Life 61 (4), 394-406 (2009)
   PUBMED   19319965
  REMARK    Review article
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Tasken,K. and Aandahl,E.M.
  TITLE     Localized effects of cAMP mediated by distinct routes of protein
            kinase A
  JOURNAL   Physiol Rev 84 (1), 137-167 (2004)
   PUBMED   14715913
  REMARK    Review article
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Kultgen,P.L., Byrd,S.K., Ostrowski,L.E. and Milgram,S.L.
  TITLE     Characterization of an A-kinase anchoring protein in human ciliary
            axonemes
  JOURNAL   Mol Biol Cell 13 (12), 4156-4166 (2002)
   PUBMED   12475942
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Mei,X., Singh,I.S., Erlichman,J. and Orr,G.A.
  TITLE     Cloning and characterization of a testis-specific, developmentally
            regulated A-kinase-anchoring protein (TAKAP-80) present on the
            fibrous sheath of rat sperm
  JOURNAL   Eur J Biochem 246 (2), 425-432 (1997)
   PUBMED   9208934
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ002474.1, SRR26360181.2918524.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq35"
     Protein         1..502
                     /product="A-kinase anchor protein 14"
                     /note="TAKAP-1.2; testis-specific A-kinase-anchoring
                     protein TAKAP-80; AKAP-14; Testis-specific
                     A-kinase-anchoring-protein; A kinase (PRKA) anchor protein
                     14"
                     /calculated_mol_wt=55625
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35817.1)"
     Region          199..265
                     /region_name="8 X 4 AA repeat of P-X-X-P"
                     /note="propagated from UniProtKB/Swiss-Prot (O35817.1)"
     Region          258..378
                     /region_name="RII-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O35817.1)"
     Region          374..493
                     /region_name="AKAP28"
                     /note="28 kDa A-kinase anchor; pfam14469"
                     /db_xref="CDD:464180"
     CDS             1..502
                     /gene="Akap14"
                     /coded_by="NM_021703.2:87..1595"
                     /db_xref="GeneID:60332"
                     /db_xref="RGD:708510"
ORIGIN      
        1 mnnkkkppnq kaktventst akakkpeape pknvtepkds kavedpkksv tnqkekktvt
       61 iiadpkdkks vtepkekktv tisdpkdkkp viekdkrtvt fvtdvkdkri vtdtkenria
      121 sidtkekgpv vpevkekkvq lidpkekvva pvapvapvah aaqvphaaqv phavqvphav
      181 pvahaapvah taqvshaapv apslpvvppa pvvplapvvp papvahtepv ahavpfappa
      241 pvappasvap pvpdapvalv apvapqvkqk irvsevkrkk evpprvpqlk emkvvlftpe
      301 ikekkvvsei kektqvidgk eklivpdvke kkpavvekkd ermneiartv vegvlaasvq
      361 fveearnpik nikwlthgef taekgrkqie kfvstwefqn rwvyyadfie kkdlihsfhy
      421 iyrvrwsapt avrpmarvsa nayftikfnk skpadmpvdv syifensell qrpgkirfre
      481 qwlrditetk hillesipfk vv
//
LOCUS       NP_001166903            1145 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001166903 XP_001072145 XP_342963
VERSION     NP_001166903.2
DBSOURCE    REFSEQ: accession NM_001173432.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1145)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1145)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1145)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced NP_001166903.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168672.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1145
                     /product="polyamine-transporting ATPase 13A2 isoform 3"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=124707
     Region          39..1071
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1145
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001173432.2:168..3605"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkt gtltedgldi mgvvplkgqm llplvpepch
      541 lppgpllral vtchalsqlh dtlvgdpmdl kmvestgwvl eegsaagsap etqvlvvmrp
      601 pprgpqqqee spepvsvlrr fpfssalqrm dvvvtwpgat qpeayvkgsp elvaslcspe
      661 tvprdfpqvl qsytaagyrv valagkplpt apsleaaqql trdtveqels llgllvmrnl
      721 lkpqttpviq tlrktgirtv mvtgdnlqta vtvakacgmv gtqehlaiih athpeqgqpa
      781 aleflpteps aamngakdpv qatdypvepe sqsrhlalsg stfavlqkhf pkllpkvlvq
      841 atvfarmape qktqlvcelq rlqycvgmcg dgandcgalk aadvgislsq aeasvvspft
      901 ssmasiecvp tviregrcsl dtsfsvfkym alysltqfis vlilytintn lgdlqflaid
      961 lfitttvavl msrtgpaltl vrarppgall svpvlgslll qvalvagiql ggyflviaqp
     1021 wfvplnrtvp apdnlpnyen tvifslsgfq ylilaaavsk gapfrqplyt nglrniadss
     1081 fkllllglva fnfvgafmle svldqclpac lqwlrpkras kkqfkqlqre laerpwptlp
     1141 vgsvr
//
LOCUS       NP_001424071             168 aa            linear   ROD 27-MAR-2025
DEFINITION  putative uncharacterized protein CIMIP3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424071 XP_038940421
VERSION     NP_001424071.1
DBSOURCE    REFSEQ: accession NM_001437142.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038940421.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2070147.1,
                                           SRR26360181.2815694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..168
                     /product="putative uncharacterized protein CIMIP3 isoform
                     4"
                     /note="Guca1a neighbor"
                     /calculated_mol_wt=19268
     CDS             1..168
                     /gene="Cimip3"
                     /gene_synonym="Guca1anb"
                     /coded_by="NM_001437142.1:112..618"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:100912849"
                     /db_xref="RGD:6485345"
ORIGIN      
        1 msrvrglprd gkqgsrfcpa ligflndlki idtkdgsrgc hyqkwtlert ekesqkslip
       61 ghrqkttsgr kgkkvppptp tplsqkwkrd rkqslesayv pvvvdprgqe pdssfrfnfy
      121 nsqysnslnp fytlqkptcg ylyqretdht rkcfgippan lvlwrsty
//
LOCUS       NP_001424090            1050 aa            linear   ROD 27-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424090 XP_063144151
VERSION     NP_001424090.1
DBSOURCE    REFSEQ: accession NM_001437161.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1050)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1050)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1050)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1050)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1050)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_063144151.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20922.1,
                                           SRR26643296.16593.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1050
                     /product="polyamine-transporting ATPase 13A2 isoform 8"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=113728
     Region          39..1002
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1050
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437161.1:168..3320"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkv leegsaagsa petqvlvvmr ppprgpqqqe
      541 espepvsvlr rfpfssalqr mdvvvtwpga tqpeayvkgs pelvaslcsp etvprdfpqv
      601 lqsytaagyr vvalagkplp tapsleaaqq ltrdtveqel sllgllvmrn llkpqttpvi
      661 qtlrktgirt vmvtgdnlqt avtvakacgm vgtqehlaii hathpeqgqp aaleflptep
      721 saamngakdp vqatdypvep esqsrhlals gstfavlqkh fpkllpkvlv qatvfarmap
      781 eqktqlvcel qrlqycvgmc gdgandcgal kaadvgisls qaeasvvspf tssmasiecv
      841 ptviregrcs ldtsfsvfky malysltqfi svlilytint nlgdlqflai dlfitttvav
      901 lmsrtgpalt lvrarppgal lsvpvlgsll lqvalvagiq lggyflviaq pwfvplnrtv
      961 papdnlpnye ntvifslsgf qylilaaavs kgapfrqply tngatrteeh cgqlfqvaaa
     1021 gsgrlqlcgr lhageragpv spslpavaaa
//
LOCUS       NP_001100684             607 aa            linear   ROD 27-MAR-2025
DEFINITION  SLAIN motif-containing protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100684 XP_001076917 XP_223362
VERSION     NP_001100684.1
DBSOURCE    REFSEQ: accession NM_001107214.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   van der Vaart,B., Manatschal,C., Grigoriev,I., Olieric,V.,
            Gouveia,S.M., Bjelic,S., Demmers,J., Vorobjev,I., Hoogenraad,C.C.,
            Steinmetz,M.O. and Akhmanova,A.
  TITLE     SLAIN2 links microtubule plus end-tracking proteins and controls
            microtubule growth in interphase
  JOURNAL   J Cell Biol 193 (6), 1083-1099 (2011)
   PUBMED   21646404
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223362.3, XP_001076917.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.54472.1,
                                           SRR26643289.34850.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..607
                     /product="SLAIN motif-containing protein 2 isoform 1"
                     /note="SLAIN motif-containing protein 2"
                     /calculated_mol_wt=65229
     Region          130..607
                     /region_name="SLAIN"
                     /note="SLAIN motif-containing family; pfam15301"
                     /db_xref="CDD:464627"
     CDS             1..607
                     /gene="Slain2"
                     /gene_synonym="RGD1311593"
                     /coded_by="NM_001107214.2:197..2020"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305310"
                     /db_xref="RGD:1311593"
ORIGIN      
        1 medvnsnvna dqevrklqel vkklekqneq lrsrsgavqs agllgpgspa ragvstpssg
       61 aasprgfplg lgakasggag sgprrtssed lrdatsllaa gegglldeve plrpdelerl
      121 sgweeeeesw lysspkkklt pmqksvsplv wcrqvldyps pdvecakksl ihkldqtmsa
      181 lkrqnlynnp fnsmsysspy spnasspyss gfnspsstpv rppivkqlil pgnsgnfkss
      241 sdrnpplspq ssidselsas eldedsigsn yklndvtdvq ilarmqeesl rqeyaattsr
      301 rssgsscnst rrgtfsdqel daqslddedd smhhavypav nrfspsprns prpspkqspr
      361 nsprsrspar gieysraspq pmisrlqqpr lslqghptdl qtsnvkneek lrrslpnlsr
      421 tsntqvdsvk ssrsdsnfqv pnggiprmqp qasatsqrlk slprtplkak qvlptpstnr
      481 vpspgkfrsp aapsplalrq pvkafsnhgs gsgsqettqf tqttsspgpp vvqntapanp
      541 ssninsatlt rpagtaamrs glprpsapsa ggipvprskl vqpvrrslpa pktygsmkdd
      601 swkdgcy
//
LOCUS       NP_001178800            1255 aa            linear   ROD 27-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 40 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001178800 XP_342954
VERSION     NP_001178800.1
DBSOURCE    REFSEQ: accession NM_001191871.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1255)
  AUTHORS   Matsuoka,S., Ballif,B.A., Smogorzewska,A., McDonald,E.R. 3rd,
            Hurov,K.E., Luo,J., Bakalarski,C.E., Zhao,Z., Solimini,N.,
            Lerenthal,Y., Shiloh,Y., Gygi,S.P. and Elledge,S.J.
  TITLE     ATM and ATR substrate analysis reveals extensive protein networks
            responsive to DNA damage
  JOURNAL   Science 316 (5828), 1160-1166 (2007)
   PUBMED   17525332
REFERENCE   2  (residues 1 to 1255)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   3  (residues 1 to 1255)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 17, 2010 this sequence version replaced XP_342954.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1255
                     /product="zinc finger and BTB domain-containing protein 40
                     isoform 2"
                     /note="zinc finger and BTB domain-containing protein 40"
                     /calculated_mol_wt=138115
     Region          1..116
                     /region_name="BTB_POZ_ZBTB40"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 40 (ZBTB40); cd18225"
                     /db_xref="CDD:349534"
     Region          824..845
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          853..873
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(858,860,862,864..865,868..869,872,886,888,892,922,
                     925..926,929,943,945,947,949..950,953..954,957)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <869..1122
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          881..930
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          938..957
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          968..986
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          1024..1044
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1064..1083
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1093..1114
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1122..1141
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1153..1170
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1255
                     /gene="Zbtb40"
                     /gene_synonym="RGD1309866"
                     /coded_by="NM_001191871.2:316..4083"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362635"
                     /db_xref="RGD:1309866"
ORIGIN      
        1 melpnysqql llqlyalcke qrfcdctisi gniyfrahkp vlaaasllfk tlldstdais
       61 idasvvspee falllemtyt gklpvgkhnf skiisladsl qmfdvavcck nlltnlvncs
      121 vqgqvvrdis vlsseaggke sekpqvevls segagepsss levsampagt ekaktqevih
      181 mvtqeisadp piaqevqvaa eitgatphtt evcsplpagq ipseakaast eagcerkqdq
      241 ltllleyesv fssaalltpd mlrrlegcse iegpqketvm ecleaegggs afqrildkvh
      301 dgsldvqval slmrlcqest paekvsqieg sagegktlsv lllehkedli qcvtqlrpiv
      361 efletakeef lpdsekrviq iccegrtpke tvenllhrvt eektlpaksl vkllqavrta
      421 fpnlglllen lqkvaespgt tgltratret awteepkrlc ipadrvdgss pnpdaygael
      481 lrkyhenlse ilidsqvllk visrlkslap gdrevmqtlv kqdsgsggvs slmsaalerq
      541 tvsaaaiwql llaaqetetc plnllleeve repgagaffr avtapestvl etilrhsklv
      601 reaiqqtvgr ehlsseeehl aetvkemlsi ssetvspeas lrvvlsrame ksvsasvvch
      661 llcsvhrsfp glqplmqela hvgfltkena eerwkvtdgl hpgakdktee aaeaaredgr
      721 ameqkeqgpe pvperqekdt saspdaakks fvckacdksf hfycrlkvhm krcrvakskq
      781 aqgkgdsdtr dsekelgrqq pearsagaep dapkkkkkrl pvtcdlcgre fahasgmqyh
      841 kltehfdekp fsceecgakf aanstlknhl rlhtgdrpfm ckhclmtftq asalayhtkk
      901 khsegkmyac qycdavfaqs ielsrhvrth tgdkpyvcrd cgkgfrqang lsihlhtfht
      961 diedpydckk crmsfstlqd hrkhihdvhs keyhpcptcg kifsapsmle rhmvthvggk
     1021 pfscgicnka yqqlsglwyh nrthhpdvfa aqnhrspkfs slqcsscdkt fsntiehkkh
     1081 iktehadlkf hecgqckelf ptpallqvhv kcqhsgsqpf rclycaatfr fpgalqhhvt
     1141 tehfkqsest fpcelcgelf tsqaqldghl esehpkvtgt etqaaasrmv qviqapepaa
     1201 paeqvitlee tqlagsqvfv tlpdpqtsqn sselvavtve dlldgtvtli cgeak
//
LOCUS       NP_001099415             178 aa            linear   ROD 27-MAR-2025
DEFINITION  nanos homolog 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001099415 XP_001072052 XP_222459
VERSION     NP_001099415.1
DBSOURCE    REFSEQ: accession NM_001105945.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Bhandari,D., Raisch,T., Weichenrieder,O., Jonas,S. and
            Izaurralde,E.
  TITLE     Structural basis for the Nanos-mediated recruitment of the CCR4-NOT
            complex and translational repression
  JOURNAL   Genes Dev 28 (8), 888-901 (2014)
   PUBMED   24736845
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Jorgensen,A., Nielsen,J.E., Blomberg Jensen,M., Graem,N. and
            Rajpert-De Meyts,E.
  TITLE     Analysis of meiosis regulators in human gonads: a sexually
            dimorphic spatio-temporal expression pattern suggests involvement
            of DMRT1 in meiotic entry
  JOURNAL   Mol Hum Reprod 18 (11), 523-534 (2012)
   PUBMED   22899867
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Julaton,V.T. and Reijo Pera,R.A.
  TITLE     NANOS3 function in human germ cell development
  JOURNAL   Hum Mol Genet 20 (11), 2238-2250 (2011)
   PUBMED   21421998
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Suzuki,H., Tsuda,M., Kiso,M. and Saga,Y.
  TITLE     Nanos3 maintains the germ cell lineage in the mouse by suppressing
            both Bax-dependent and -independent apoptotic pathways
  JOURNAL   Dev Biol 318 (1), 133-142 (2008)
   PUBMED   18436203
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Lolicato,F., Marino,R., Paronetto,M.P., Pellegrini,M., Dolci,S.,
            Geremia,R. and Grimaldi,P.
  TITLE     Potential role of Nanos3 in maintaining the undifferentiated
            spermatogonia population
  JOURNAL   Dev Biol 313 (2), 725-738 (2008)
   PUBMED   18089289
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Tsuda,M., Sasaoka,Y., Kiso,M., Abe,K., Haraguchi,S., Kobayashi,S.
            and Saga,Y.
  TITLE     Conserved role of nanos proteins in germ cell development
  JOURNAL   Science 301 (5637), 1239-1241 (2003)
   PUBMED   12947200
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001072052.1, XP_222459.2.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..178
                     /product="nanos homolog 3 isoform 2"
                     /note="nanos homolog 3"
                     /calculated_mol_wt=19005
     Region          57..110
                     /region_name="zf-nanos"
                     /note="Nanos RNA binding domain; pfam05741"
                     /db_xref="CDD:461728"
     CDS             1..178
                     /gene="Nanos3"
                     /coded_by="NM_001105945.1:25..561"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:288909"
                     /db_xref="RGD:1306672"
ORIGIN      
        1 mgtfnlwtdy lglarlvgal heeeepdvrl dpkpepkpss asqqaskess aaperlcsfc
       61 khngesraiy qshvlkdeag rvlcpilrdy vcpqcgatqe hahtrrfcpl tgqgytsvyc
      121 yttrnsagkk ltrpdkaktq naghrlggea aagvyagsks grkppgpsps accpstta
//
LOCUS       NP_001100686            1672 aa            linear   ROD 27-MAR-2025
DEFINITION  arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing
            protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100686 XP_001053361 XP_223437
VERSION     NP_001100686.1
DBSOURCE    REFSEQ: accession NM_001107216.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1672)
  AUTHORS   Krugmann,S., Anderson,K.E., Ridley,S.H., Risso,N., McGregor,A.,
            Coadwell,J., Davidson,K., Eguinoa,A., Ellson,C.D., Lipp,P.,
            Manifava,M., Ktistakis,N., Painter,G., Thuring,J.W., Cooper,M.A.,
            Lim,Z.Y., Holmes,A.B., Dove,S.K., Michell,R.H., Grewal,A.,
            Nazarian,A., Erdjument-Bromage,H., Tempst,P., Stephens,L.R. and
            Hawkins,P.T.
  TITLE     Identification of ARAP3, a novel PI3K effector regulating both Arf
            and Rho GTPases, by selective capture on phosphoinositide affinity
            matrices
  JOURNAL   Mol Cell 9 (1), 95-108 (2002)
   PUBMED   11804589
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473963.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223437.4, XP_001053361.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1672
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..1672
                     /product="arf-GAP with Rho-GAP domain, ANK repeat and PH
                     domain-containing protein 2 isoform 1"
                     /note="arf-GAP with Rho-GAP domain, ANK repeat and PH
                     domain-containing protein 2; centaurin, delta 1"
                     /calculated_mol_wt=189689
     Region          6..68
                     /region_name="SAM_Arap1,2,3"
                     /note="SAM domain of Arap1,2,3 (angiotensin
                     receptor-associated protein); cd09490"
                     /db_xref="CDD:188889"
     Site            order(19,43,58..59,62)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188889"
     Region          480..571
                     /region_name="PH1_ARAP"
                     /note="ArfGAP with RhoGAP domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain, repeat 1; cd13253"
                     /db_xref="CDD:270073"
     Region          581..671
                     /region_name="PH2_ARAP"
                     /note="ArfGAP with RhoGAP domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain, repeat 2; cd13254"
                     /db_xref="CDD:270074"
     Region          676..796
                     /region_name="ArfGap_ARAP2"
                     /note="ArfGap with Rho-Gap domain, ANK repeat and PH
                     domain-containing protein 2; cd08856"
                     /db_xref="CDD:350081"
     Site            order(696,699,716,719,724)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350081"
     Site            order(696,699,716,719)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350081"
     Region          888..998
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          1011..1106
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          1110..1289
                     /region_name="RhoGAP_ARAP"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in ARAPs. ARAPs (also known
                     as centaurin deltas) contain, besides the RhoGAP domain,
                     an Arf GAP, ankyrin repeat ras-associating, and PH
                     domains. Since their ArfGAP activity...; cd04385"
                     /db_xref="CDD:239850"
     Site            order(1147,1186,1190,1259,1262..1263,1279)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239850"
     Site            1147
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239850"
     Region          1298..1395
                     /region_name="RA_ARAP2"
                     /note="Ras-associating (RA) domain found in Arf-GAP with
                     Rho-GAP domain, ANK repeat and PH domain-containing
                     protein 2 (ARAP2); cd17227"
                     /db_xref="CDD:340747"
     Region          1401..1512
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..1672
                     /gene="Arap2"
                     /gene_synonym="Centd1"
                     /coded_by="NM_001107216.1:209..5227"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305367"
                     /db_xref="RGD:1306452"
ORIGIN      
        1 msavsevnvd iqdflmsinl eqyllhfqef gfytvkdcts indnvlhqig isptghrrri
       61 lkqlqmifsk mqdfpiyanv yktkngstpk eqhsapssss ntciefsdsv tvhrpgpaps
      121 emvttnvlse gnchsstshd klslsssdlp cpeeeicqnv dssqdylfgr vnvkidslit
      181 qqavehtage eqtekvnlvs edsskalntn teclpsvdhp asethcgngt ngvlesfpps
      241 pffqfqgemv vnelyvpssp ihspmrsrsk lvsrpsrsfl lrhrpvpeip gstksisgsy
      301 frdrksitts agksltlkda nednstsifp ygetflfqrl esskkrsikn efwahedtvk
      361 eeaatsrnsi ltkssiydsr kekvsedkve diwipredkn nlpqdsases eystveecfq
      421 slrrknskas ksrtqkafyl dpfnrhsypl sstsentdps tianaispya cfygssaakv
      481 ksgwldklsp qgkrmfqkrw vkfdglsisy ynndremysk giipltaist vraqgdnkfe
      541 ivttqrtfvf rvekeeernd wisvllsalk spsltsqlqa avapekcgyl elrgykakif
      601 tvlrgnsvwl ckteqdfksg lgitiipmnv anvkqidrav kqsfeiitpy rsfsftadse
      661 kekqewieav qqsiaetlsd yevaekiwfn esnrscadck apdpdwasin lcvvickkca
      721 gqhrslgpkd skvrslkmda siwsneliel fivignkran dfwagnlkkd eeiqmdspvd
      781 krkifitqky kegkfrktfl asltkeelnk alcaavvkpd vletmallfs gadvmcatgd
      841 pvhctpylla kkagqslqme flyhnkfsdf pqydahsegg ssqeatqstf lcdflyqata
      901 sasrvstekk lleetnkkwc vleggflsyy endrcttpng tinisevicl tvhkedfyln
      961 tgpififeiy lpservflfg aktsqiqrkw tetiakrfvp fvaenltead ydligqlfyk
     1021 dchaldqwrk gwfamdkssl cfclqtqeaq eermhlrrlq eltistvvqn gekvdvlllv
     1081 ekgrtlyihg ytkldftvwr naiekaagtd gntlqdqqlc kndvpiivns ciafvtqygl
     1141 gckyiyqkdg dplsiselle sfkkdarsvk lrvgkhqled vtgvlksfls diddalltke
     1201 lypywvsald aqdekqrtdk yraficslpg vnratlaali ehlyrvqkcs einhmnahnl
     1261 alvfssclfq tkgqtseevn viedlinnyv eifevsqagd llievfaerk epdcsiiirv
     1321 spvmeaeelt ndilaiknil ptkgdiwatf evieneeler plhytenvle qvlqwsslae
     1381 pgsaylvvkr fltidtikqc reksikegil klkeepskil sgnkfqdrcv vlrdghlfiy
     1441 kdpkstkhek mfplrlmkfy lgvkkkmkpp tswgltacse khhwhlccds lqaqmewmas
     1501 ifiaqhendi wppagkerkr sitknpkigg lplipiqhek natqarknie maraelerlr
     1561 lserhdgdft dsslkdrasi igyclehkde klrnrarkhr sfncledtea evppglpkgy
     1621 kglktvkkte drnskatlep nnklpskvie elsvvlqrsr shpkelpdeq tl
//
LOCUS       NP_001012034             374 aa            linear   ROD 27-MAR-2025
DEFINITION  ecto-ADP-ribosyltransferase 3 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001012034 XP_223235
VERSION     NP_001012034.1
DBSOURCE    REFSEQ: accession NM_001012034.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Shi,W., Gong,P., Fan,J., Yan,Y.H., Ni,L., Wu,X., Cui,G., Wu,X.,
            Gu,X. and Chen,J.
  TITLE     The expression pattern of ADP-ribosyltransferase 3 in rat traumatic
            brain injury
  JOURNAL   J Mol Histol 43 (1), 37-47 (2012)
   PUBMED   22037978
  REMARK    GeneRIF: ART3 may play important roles in CNS pathophysiology after
            traumatic brain injury (TBI).
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Wang,B., Golemis,E.A. and Kruh,G.D.
  TITLE     ArgBP2, a multiple Src homology 3 domain-containing,
            Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed
            cells and localized in stress fibers and cardiocyte Z-disks
  JOURNAL   J Biol Chem 272 (28), 17542-17550 (1997)
   PUBMED   9211900
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Koch-Nolte,F., Haag,F., Braren,R., Kuhl,M., Hoovers,J.,
            Balasubramanian,S., Bazan,F. and Thiele,H.G.
  TITLE     Two novel human members of an emerging mammalian gene family
            related to mono-ADP-ribosylating bacterial toxins
  JOURNAL   Genomics 39 (3), 370-376 (1997)
   PUBMED   9119374
  REMARK    Erratum:[Genomics 1999 Jan 1;55(1):130]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079018.1.
            
            On Feb 11, 2005 this sequence version replaced XP_223235.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..374
                     /product="ecto-ADP-ribosyltransferase 3 isoform 1
                     precursor"
                     /EC_number="2.4.2.31"
                     /note="ecto-ADP-ribosyltransferase 3"
                     /calculated_mol_wt=38806
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2925
     Region          29..251
                     /region_name="VIP2"
                     /note="A family of actin-ADP-ribosylating toxin. A member
                     of the Bacillus-prodiced vegetative insecticidal proteins
                     (VIPs) possesses high specificity against the major insect
                     pest, corn rootworms, and belongs to a classs of binary
                     toxins and regulators of...; cl00173"
                     /db_xref="CDD:469640"
     CDS             1..374
                     /gene="Art3"
                     /coded_by="NM_001012034.1:99..1223"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:305235"
                     /db_xref="RGD:628833"
ORIGIN      
        1 mkmghfelvt tllaamvlmd vfqvqaevld maenvfddey lkcnsrmemk yiprmhgeel
       61 andellqsvw dkagiqweaq kaqlslpknf kdaygialta yvteaqdqsp fyhtfnravk
      121 iaglsrrryi ynfpfkafhf ylvralqllr rpceesyknv vystspnisf afgeqnqarl
      181 gnftlaysak pqtaneqrll tiqtcfgvav gkllnkeseg ivliplsevf qvsrkgtddd
      241 lilhsinstc syyecsflgg lkagscttnp enpdpgylnn pdldsqkled sgrksldsvk
      301 mpeikvlqge enpllpdekp edrnrgkanv ptpglvpvpg pkshpssssg hrllpsdtas
      361 tilliaaavd fial
//
LOCUS       NP_001171153             328 aa            linear   ROD 27-MAR-2025
DEFINITION  putative P2Y purinoceptor 10 [Rattus norvegicus].
ACCESSION   NP_001171153 XP_001059224 XP_228500
VERSION     NP_001171153.1
DBSOURCE    REFSEQ: accession NM_001177682.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168967.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_228500.4, XP_001059224.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168967.1, CO559392.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345330, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..328
                     /product="putative P2Y purinoceptor 10"
                     /note="purinergic receptor P2Y, G-protein coupled, 10;
                     purinergic receptor P2Y10"
                     /calculated_mol_wt=37149
     Region          23..305
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          25..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          58..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          95..117
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          139..155
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          185..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          231..253
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          273..298
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..328
                     /gene="P2ry10"
                     /gene_synonym="RGD1561912"
                     /coded_by="NM_001177682.1:280..1266"
                     /db_xref="GeneID:317219"
                     /db_xref="RGD:1561912"
ORIGIN      
        1 mgsnststve sncnainvtf qnslyattyi fifipgllan saalwvlfrf iskknkaiif
       61 minlsvadla hilslplriy yyinrhwpfq ralcllcfyl kylnmyasif fltcislqrc
      121 lfllkpfrar nwkrrydvgi saavwiivgt aclpfpimrs aglanntdsc fadlgykqmd
      181 plvlvtmiti aelagfvipv ltiacctwkt tvslkhppia fqgiserkka lrmvfmcaav
      241 fvicftpyhi nfifytmvke niitscpivk samyfhpfsl claslcclld pilyyfmase
      301 frdqlsrhgs svtrsrlmsr esgssmvs
//
LOCUS       NP_001424101             247 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424101
VERSION     NP_001424101.1
DBSOURCE    REFSEQ: accession NM_001437172.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77783.1,
                                           SRR26360181.1304922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..247
                     /product="maestro isoform 5"
                     /note="protein maestro"
                     /calculated_mol_wt=28474
     Region          52..199
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..247
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437172.1:220..963"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kvrkykkvml dllvhglydp vssevihesv ktltimlgki
      121 qgqrlgsffi ditlqtrtll ddeddsvrys afvlfgqlaa fagrkwkkff thqvnqtqds
      181 llshlqdesp qvakactmav qacvpylkpr keqsfqseed qknrrlsqql shyhpeillf
      241 fyankil
//
LOCUS       NP_001424115             750 aa            linear   ROD 28-MAR-2025
DEFINITION  alpha-adducin isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424115 XP_063128911
VERSION     NP_001424115.1
DBSOURCE    REFSEQ: accession NM_001437186.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_063128911.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.57435.1,
                                           SRR26643289.35161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..750
                     /product="alpha-adducin isoform 5"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=81764
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Region          572..>721
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     CDS             1..750
                     /gene="Add1"
                     /coded_by="NM_001437186.1:181..2433"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kppnayascp
      481 phgllhwtke dghrtstsav pnlfvplntn pkevqemrnk ireqnlqdik tagpqsqvlc
      541 gvmmdrslvq gelvtaskai iekeyqphvi vsttgpnpfn tltdreleey rreverkqkg
      601 seenldetre qkeksppdqs avpntppstp vklegglpqe ptsrdgsdat tskptppdls
      661 pdepsealaf ptvaeeahas pdttqplaea dpepasasap gaeevaspat eegspmdpgs
      721 dgspgkspsk kkkkfrtpsf lkkskkksds
//
LOCUS       NP_001424099             248 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424099
VERSION     NP_001424099.1
DBSOURCE    REFSEQ: accession NM_001437170.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.607854.1,
                                           SRR26360194.372641.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..248
                     /product="maestro isoform 4"
                     /note="protein maestro"
                     /calculated_mol_wt=28602
     Region          52..200
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..248
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437170.1:251..997"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kqvrkykkvm ldllvhglyd pvssevihes vktltimlgk
      121 iqgqrlgsff iditlqtrtl lddeddsvry safvlfgqla afagrkwkkf fthqvnqtqd
      181 sllshlqdes pqvakactma vqacvpylkp rkeqsfqsee dqknrrlsqq lshyhpeill
      241 ffyankil
//
LOCUS       NP_001424098             248 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424098
VERSION     NP_001424098.1
DBSOURCE    REFSEQ: accession NM_001437169.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2734115.1,
                                           SRR26643429.54677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..248
                     /product="maestro isoform 4"
                     /note="protein maestro"
                     /calculated_mol_wt=28602
     Region          52..200
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..248
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437169.1:220..966"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kqvrkykkvm ldllvhglyd pvssevihes vktltimlgk
      121 iqgqrlgsff iditlqtrtl lddeddsvry safvlfgqla afagrkwkkf fthqvnqtqd
      181 sllshlqdes pqvakactma vqacvpylkp rkeqsfqsee dqknrrlsqq lshyhpeill
      241 ffyankil
//
LOCUS       NP_001424131             750 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424131 XP_006250867
VERSION     NP_001424131.1
DBSOURCE    REFSEQ: accession NM_001437202.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250867.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.56327.1,
                                           SRR26643290.44123.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..750
                     /product="YTH domain-containing protein 1 isoform 2"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=87172
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          371..507
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          524..578
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          630..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          692..750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     CDS             1..750
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437202.1:288..2540"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreeke dcqdcsswlf sdgelnvldd iltevpeqdd elynpeseqd knekkgskrk
       61 sermesidtk rqkpsihsrq liskplsssv snnkrivstk gksvteykne eyqrsernkr
      121 ldadrkirls ssssrepyks qpekpclrkr dserrakspt pdgserigle vdrrasrssq
      181 sskeegnsee ygsdhetgss asseqgnnte neeeggeedv eedeevdedg dddeevdeda
      241 eeeedeeede eeedeeeeee eeeeyeqder dqkeegndyd trseasdsgs esvsftdgsv
      301 rsgsgtdgsd ekkkerkrar gispivfdrs gssasesyag sekkheklss svravrkdqt
      361 sklkyvlqda rffliksnnh envslakakg vwstlpvnek klnlafrsar svilifsvre
      421 sgkfqgfarl sseshhggsp ihwvlpagms akmlggvfki dwicrrelpf tksahltnpw
      481 nehkpvkigr dgqeielecg tqlcllfppd esidlyqlih kmrhkrrmhs qprsrgrpsr
      541 repvrdvgrr rpedydihns rkkpridypp efhqrpgylk dpryqevdsf tnlipnrrfs
      601 gvrrdvflng syndyvrefh nmgppppwqg mppypgieqp phhpyyqhha pppqahppys
      661 ghhpvphear yrdkrvhdyd mrvddflrrt qavvsgrrsr prerdrerer drprdnrrdr
      721 erdrgrdrer erericdrdr drgergryrr
//
LOCUS       NP_001424140             604 aa            linear   ROD 28-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424140 XP_006250944
VERSION     NP_001424140.1
DBSOURCE    REFSEQ: accession NM_001437211.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250944.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.465503.1,
                                           SRR26643290.44223.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..604
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     2"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=67382
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..604
                     /gene="Fip1l1"
                     /coded_by="NM_001437211.1:203..2017"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki taedctmevt pgaeiqdgrf nlfkvqqgrt
      241 gnsekeaalp stkaeftspp slfktglpps rnstssqsqt stasrkasss vgkwqdrygr
      301 aespdlrrlp gaidvigqti tisrvegrrr anensniqvl sdrsatevdn nfskpppffp
      361 pgappthlpp ppflpppptv stapplippp gipitvpppg fppppgappp sliptiesgh
      421 ssgydsrsar afpygnvafp hltssapswp slvdttkqwd yyarrekdrd rdrerdrdre
      481 rerdrdrere rtrerererd hsptpsvfns deeryryrey aergyerhra srekeerhre
      541 rrhrekeetr hkssrsnsrr rheseegdsh rrhkhkkskr skegkeagse pvpeqestea
      601 apae
//
LOCUS       NP_001424103             247 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424103
VERSION     NP_001424103.1
DBSOURCE    REFSEQ: accession NM_001437174.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35236.1,
                                           SRR26643293.77786.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..247
                     /product="maestro isoform 5"
                     /note="protein maestro"
                     /calculated_mol_wt=28474
     Region          52..199
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..247
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437174.1:392..1135"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kvrkykkvml dllvhglydp vssevihesv ktltimlgki
      121 qgqrlgsffi ditlqtrtll ddeddsvrys afvlfgqlaa fagrkwkkff thqvnqtqds
      181 llshlqdesp qvakactmav qacvpylkpr keqsfqseed qknrrlsqql shyhpeillf
      241 fyankil
//
LOCUS       NP_001424111              55 aa            linear   ROD 28-MAR-2025
DEFINITION  transmembrane protein 240 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424111
VERSION     NP_001424111.1
DBSOURCE    REFSEQ: accession NM_001437182.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 55)
  AUTHORS   Trinidad,J.C., Barkan,D.T., Gulledge,B.F., Thalhammer,A., Sali,A.,
            Schoepfer,R. and Burlingame,A.L.
  TITLE     Global identification and characterization of both O-GlcNAcylation
            and phosphorylation at the murine synapse
  JOURNAL   Mol Cell Proteomics 11 (8), 215-229 (2012)
   PUBMED   22645316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.615456.1,
                                           SRR22582416.200667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..55
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..55
                     /product="transmembrane protein 240 isoform 2"
                     /calculated_mol_wt=6071
     Region          1..>55
                     /region_name="TMEM240"
                     /note="TMEM240 family; pfam15207"
                     /db_xref="CDD:405814"
     CDS             1..55
                     /gene="Tmem240"
                     /coded_by="NM_001437182.1:287..454"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100362471"
                     /db_xref="RGD:2318117"
ORIGIN      
        1 msmsantmif milgasivma iaclmdmnal ldrfhnyilp hlrgedrvch cncgr
//
LOCUS       NP_001424141             581 aa            linear   ROD 28-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424141 XP_006250946
VERSION     NP_001424141.1
DBSOURCE    REFSEQ: accession NM_001437212.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250946.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.46587.1,
                                           SRR26643298.54094.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..581
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     3"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=64828
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..581
                     /gene="Fip1l1"
                     /coded_by="NM_001437212.1:203..1948"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki tvqqgrtgns ekeaalpstk aeftsppslf
      241 ktglppsrns tssqsqtsta srkasssvgk wqdrygraes pdlrrlpgai dvigqtitis
      301 rvegrrrane nsniqvlsdr satevdnnfs kpppffppga ppthlppppf lpppptvsta
      361 pplipppgip itvpppgfpp ppgapppsli ptiesghssg ydsrsarafp ygnvafphlt
      421 ssapswpslv dttkqwdyya rrekdrdrdr erdrdrerer drdrerertr erererdhsp
      481 tpsvfnsdee ryryreyaer gyerhrasre keerhrerrh rekeetrhks srsnsrrrhe
      541 seegdshrrh khkkskrske gkeagsepvp eqesteaapa e
//
LOCUS       NP_001424095             286 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424095
VERSION     NP_001424095.1
DBSOURCE    REFSEQ: accession NM_001437166.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77785.1,
                                           SRR26643286.44721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..286
                     /product="maestro isoform 1"
                     /note="protein maestro"
                     /calculated_mol_wt=32790
     Region          90..238
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          128..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          171..200
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..286
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437166.1:406..1266"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mcsktkmtek tnphpplrpt esaalmrgcl rglesvsfme qmqripnqpl ptpasqskkr
       61 rtplssffsk vswklrlqkr eplknlffvl aerargpnpr krhlamrglg ilaheapdkq
      121 vrkykkvmld llvhglydpv ssevihesvk tltimlgkiq gqrlgsffid itlqtrtlld
      181 deddsvrysa fvlfgqlaaf agrkwkkfft hqvnqtqdsl lshlqdespq vakactmavq
      241 acvpylkprk eqsfqseedq knrrlsqqls hyhpeillff yankil
//
LOCUS       NP_001424102             247 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424102
VERSION     NP_001424102.1
DBSOURCE    REFSEQ: accession NM_001437173.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35233.1,
                                           SRR26643429.54679.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..247
                     /product="maestro isoform 5"
                     /note="protein maestro"
                     /calculated_mol_wt=28474
     Region          52..199
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..247
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437173.1:251..994"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kvrkykkvml dllvhglydp vssevihesv ktltimlgki
      121 qgqrlgsffi ditlqtrtll ddeddsvrys afvlfgqlaa fagrkwkkff thqvnqtqds
      181 llshlqdesp qvakactmav qacvpylkpr keqsfqseed qknrrlsqql shyhpeillf
      241 fyankil
//
LOCUS       NP_001424116             694 aa            linear   ROD 28-MAR-2025
DEFINITION  alpha-adducin isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424116 XP_017454554
VERSION     NP_001424116.1
DBSOURCE    REFSEQ: accession NM_001437187.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_017454554.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.54878.1,
                                           SRR26360194.2431842.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..694
                     /product="alpha-adducin isoform 6"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=76447
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..694
                     /gene="Add1"
                     /coded_by="NM_001437187.1:181..2265"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kvwtnithdh
      481 vkpllqslss gvcvpscitn clwtkedghr tstsavpnlf vplntnpkev qemrnkireq
      541 nlqdiktagp qsqvlcgvmm drslvqdapl sdctetiegl erteqtfspa ksvsfrkgel
      601 vtaskaiiek eyqphvivst tgpnpfntlt dreleeyrre verkqkgsee nldetreqke
      661 ksppdqsavp ntppstpvkl egagdgcake yllp
//
LOCUS       NP_058686                735 aa            linear   ROD 28-MAR-2025
DEFINITION  alpha-adducin isoform 1 [Rattus norvegicus].
ACCESSION   NP_058686
VERSION     NP_058686.3
DBSOURCE    REFSEQ: accession NM_016990.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced NP_058686.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107657.1, SRR21887623.2491154.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..735
                     /product="alpha-adducin isoform 1"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=80208
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63028.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Region          418..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63028.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Region          557..>706
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          576..735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63028.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYC0; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     Region          715..732
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63028.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKC.
                     /evidence=ECO:0000250|UniProtKB:P35611; propagated from
                     UniProtKB/Swiss-Prot (Q63028.2)"
     CDS             1..735
                     /gene="Add1"
                     /coded_by="NM_016990.3:181..2388"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kwtkedghrt
      481 stsavpnlfv plntnpkevq emrnkireqn lqdiktagpq sqvlcgvmmd rslvqgelvt
      541 askaiiekey qphvivsttg pnpfntltdr eleeyrreve rkqkgseenl detreqkeks
      601 ppdqsavpnt ppstpvkleg glpqeptsrd gsdattskpt ppdlspdeps ealafptvae
      661 eahaspdttq plaeadpepa sasapgaeev aspateegsp mdpgsdgspg kspskkkkkf
      721 rtpsflkksk kksds
//
LOCUS       NP_001424106             232 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424106
VERSION     NP_001424106.1
DBSOURCE    REFSEQ: accession NM_001437177.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1765616.1,
                                           SRR26360186.1376871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..232
                     /product="maestro isoform 7"
                     /note="protein maestro"
                     /calculated_mol_wt=26759
     CDS             1..232
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437177.1:392..1090"
                     /note="isoform 7 is encoded by transcript variant 14"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kvrkykkvml dllvhglydp vssevihesv ktltimlgki
      121 qgqrlgsffi ditlqtrtll ddlaafagrk wkkffthqvn qtqdsllshl qdespqvaka
      181 ctmavqacvp ylkprkeqsf qseedqknrr lsqqlshyhp eillffyank il
//
LOCUS       NP_001424113             781 aa            linear   ROD 28-MAR-2025
DEFINITION  alpha-adducin isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424113 XP_006251221
VERSION     NP_001424113.1
DBSOURCE    REFSEQ: accession NM_001437184.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 781)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 781)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 781)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 781)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 781)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 781)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006251221.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.35166.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..781
                     /product="alpha-adducin isoform 3"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=85190
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Region          603..>752
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     CDS             1..781
                     /gene="Add1"
                     /coded_by="NM_001437184.1:181..2526"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kppnayascp
      481 phgllhwtke dghrtstsav pnlfvplntn pkevqemrnk ireqnlqdik tagpqsqvlc
      541 gvmmdrslvq daplsdctet ieglerteqt fspaksvsfr kgelvtaska iiekeyqphv
      601 ivsttgpnpf ntltdrelee yrreverkqk gseenldetr eqkeksppdq savpntppst
      661 pvklegglpq eptsrdgsda ttskptppdl spdepseala fptvaeeaha spdttqplae
      721 adpepasasa pgaeevaspa teegspmdpg sdgspgksps kkkkkfrtps flkkskkksd
      781 s
//
LOCUS       NP_001424132             742 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424132 XP_038947518
VERSION     NP_001424132.1
DBSOURCE    REFSEQ: accession NM_001437203.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 742)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 742)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 742)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 742)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 742)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_038947518.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.53941.1,
                                           SRR26643293.56320.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..742
                     /product="YTH domain-containing protein 1 isoform 3"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=86285
     Region          371..507
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     CDS             1..742
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437203.1:288..2516"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreeke dcqdcsswlf sdgelnvldd iltevpeqdd elynpeseqd knekkgskrk
       61 sermesidtk rqkpsihsrq liskplsssv snnkrivstk gksvteykne eyqrsernkr
      121 ldadrkirls ssssrepyks qpekpclrkr dserrakspt pdgserigle vdrrasrssq
      181 sskeegnsee ygsdhetgss asseqgnnte neeeggeedv eedeevdedg dddeevdeda
      241 eeeedeeede eeedeeeeee eeeeyeqder dqkeegndyd trseasdsgs esvsftdgsv
      301 rsgsgtdgsd ekkkerkrar gispivfdrs gssasesyag sekkheklss svravrkdqt
      361 sklkyvlqda rffliksnnh envslakakg vwstlpvnek klnlafrsar svilifsvre
      421 sgkfqgfarl sseshhggsp ihwvlpagms akmlggvfki dwicrrelpf tksahltnpw
      481 nehkpvkigr dgqeielecg tqlcllfppd esidlyqlih kmrhkrrmhs qprsrgrpsr
      541 repvrdvgrr rpedydihns rkkpridypp efhqrpgylk dpryqevdrr fsgvrrdvfl
      601 ngsyndyvre fhnmgppppw qgmppypgie qpphhpyyqh happpqahpp ysghhpvphe
      661 aryrdkrvhd ydmrvddflr rtqavvsgrr srprerdrer erdrprdnrr drerdrgrdr
      721 ererericdr drdrgergry rr
//
LOCUS       NP_001424135             720 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424135 XP_063128907
VERSION     NP_001424135.1
DBSOURCE    REFSEQ: accession NM_001437206.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 720)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 720)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 720)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 720)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 720)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 720)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_063128907.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.53944.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..720
                     /product="YTH domain-containing protein 1 isoform 6"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=83762
     Region          341..477
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     CDS             1..720
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437206.1:288..2450"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreekd gelnvlddil tevpeqddel ynpeseqdkn ekkgskrkse rmesidtkrq
       61 kpsihsrqli skplsssvsn nkrivstkgk svteykneey qrsernkrld adrkirlsss
      121 ssrepyksqp ekpclrkrds erraksptpd gseriglevd rrasrssqss keegnseeyg
      181 sdhetgssas seqgnntene eeggeedvee deevdedgdd deevdedaee eedeeedeee
      241 edeeeeeeee eeyeqderdq keegndydtr seasdsgses vsftdgsvrs gsgtdgsdek
      301 kkerkrargi spivfdrsgs sasesyadqt sklkyvlqda rffliksnnh envslakakg
      361 vwstlpvnek klnlafrsar svilifsvre sgkfqgfarl sseshhggsp ihwvlpagms
      421 akmlggvfki dwicrrelpf tksahltnpw nehkpvkigr dgqeielecg tqlcllfppd
      481 esidlyqlih kmrhkrrmhs qprsrgrpsr repvrdvgrr rpedydihns rkkpridypp
      541 efhqrpgylk dpryqevdsf tnlipnrrfs gvrrdvflng syndyvrefh nmgppppwqg
      601 mppypgieqp phhpyyqhha pppqahppys ghhpvphear yrdkrvhdyd mrvddflrrt
      661 qavvsgrrsr prerdrerer drprdnrrdr erdrgrdrer erericdrdr drgergryrr
//
LOCUS       NP_001424105             232 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424105
VERSION     NP_001424105.1
DBSOURCE    REFSEQ: accession NM_001437176.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54676.1,
                                           SRR26360186.844327.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..232
                     /product="maestro isoform 7"
                     /note="protein maestro"
                     /calculated_mol_wt=26759
     CDS             1..232
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437176.1:220..918"
                     /note="isoform 7 is encoded by transcript variant 13"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kvrkykkvml dllvhglydp vssevihesv ktltimlgki
      121 qgqrlgsffi ditlqtrtll ddlaafagrk wkkffthqvn qtqdsllshl qdespqvaka
      181 ctmavqacvp ylkprkeqsf qseedqknrr lsqqlshyhp eillffyank il
//
LOCUS       NP_001008296             536 aa            linear   ROD 28-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001008296 XP_214044
VERSION     NP_001008296.1
DBSOURCE    REFSEQ: accession NM_001008295.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Dec 16, 2004 this sequence version replaced XP_214044.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.46591.1, BC085767.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..536
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     1"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=60057
     Region          1..296
                     /region_name="Necessary for stimulating PAPOLA activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          1..110
                     /region_name="Sufficient for interaction with PAPOLA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          136..219
                     /region_name="Sufficient for interaction with CPSF4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     Region          212..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          300..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          383..536
                     /region_name="Sufficient for interaction with CPSF1 and
                     CSTF3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          397..432
                     /region_name="Arg/Asp/Glu-rich domain.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     CDS             1..536
                     /gene="Fip1l1"
                     /coded_by="NM_001008295.2:203..1813"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki tvqqgrtgns ekeaalpstk aeftsppslf
      241 ktglppsrrl pgaidvigqt itisrvegrr ranensniqv lsdrsatevd nnfskpppff
      301 ppgappthlp pppflppppt vstapplipp pgfppppgap ppslipties ghssgydsrs
      361 arafpygnva fphltssaps wpslvdttkq wdyyarrekd rdrdrerdrd rererdrdre
      421 rertrerere rdhsptpsvf nsdeeryryr eyaergyerh rasrekeerh rerrhrekee
      481 trhkssrsns rrrheseegd shrrhkhkks krskegkeag sepvpeqest eaapae
//
LOCUS       NP_001424136             712 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424136 XP_006250870
VERSION     NP_001424136.1
DBSOURCE    REFSEQ: accession NM_001437207.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250870.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D78303.1, SRR26643298.53947.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..712
                     /product="YTH domain-containing protein 1 isoform 7"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=82875
     Region          341..477
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     CDS             1..712
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437207.1:288..2426"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreekd gelnvlddil tevpeqddel ynpeseqdkn ekkgskrkse rmesidtkrq
       61 kpsihsrqli skplsssvsn nkrivstkgk svteykneey qrsernkrld adrkirlsss
      121 ssrepyksqp ekpclrkrds erraksptpd gseriglevd rrasrssqss keegnseeyg
      181 sdhetgssas seqgnntene eeggeedvee deevdedgdd deevdedaee eedeeedeee
      241 edeeeeeeee eeyeqderdq keegndydtr seasdsgses vsftdgsvrs gsgtdgsdek
      301 kkerkrargi spivfdrsgs sasesyadqt sklkyvlqda rffliksnnh envslakakg
      361 vwstlpvnek klnlafrsar svilifsvre sgkfqgfarl sseshhggsp ihwvlpagms
      421 akmlggvfki dwicrrelpf tksahltnpw nehkpvkigr dgqeielecg tqlcllfppd
      481 esidlyqlih kmrhkrrmhs qprsrgrpsr repvrdvgrr rpedydihns rkkpridypp
      541 efhqrpgylk dpryqevdrr fsgvrrdvfl ngsyndyvre fhnmgppppw qgmppypgie
      601 qpphhpyyqh happpqahpp ysghhpvphe aryrdkrvhd ydmrvddflr rtqavvsgrr
      661 srprerdrer erdrprdnrr drerdrgrdr ererericdr drdrgergry rr
//
LOCUS       NP_001424109             159 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424109
VERSION     NP_001424109.1
DBSOURCE    REFSEQ: accession NM_001437180.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54678.1,
                                           SRR26360186.1889133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..159
                     /product="maestro isoform 9"
                     /note="protein maestro"
                     /calculated_mol_wt=18175
     CDS             1..159
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437180.1:237..716"
                     /note="isoform 9 is encoded by transcript variant 17"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mldllvhgly dpvssevihe svktltimlg kiqgqrlgsf fiditlqtrt llddeddsvr
       61 ysafvlfgql aafagrkwkk ffthqvnqtq dsllshlqde spqvakactm avqacvpylk
      121 prkeqsfqse edqknrrlsq qlshyhpeil lffyankil
//
LOCUS       NP_001424142             568 aa            linear   ROD 28-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424142 XP_006250947
VERSION     NP_001424142.1
DBSOURCE    REFSEQ: accession NM_001437213.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250947.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.48778.1,
                                           SRR26360194.2246078.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..568
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     4"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=63483
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..568
                     /gene="Fip1l1"
                     /coded_by="NM_001437213.1:203..1909"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki taedctmevt pgaeiqdgrf nlfkvqqgrt
      241 gnsekeaalp stkaeftspp slfktglpps rrlpgaidvi gqtitisrve grrranensn
      301 iqvlsdrsat evdnnfskpp pffppgappt hlppppflpp pptvstappl ipppgipitv
      361 pppgfppppg apppslipti esghssgyds rsarafpygn vafphltssa pswpslvdtt
      421 kqwdyyarre kdrdrdrerd rdrererdrd rerertrere rerdhsptps vfnsdeeryr
      481 yreyaergye rhrasrekee rhrerrhrek eetrhkssrs nsrrrhesee gdshrrhkhk
      541 kskrskegke agsepvpeqe steaapae
//
LOCUS       NP_001424139             621 aa            linear   ROD 28-MAR-2025
DEFINITION  kelch-like protein 8 [Rattus norvegicus].
ACCESSION   NP_001424139 XP_008768228
VERSION     NP_001424139.1
DBSOURCE    REFSEQ: accession NM_001437210.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_008768228.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.43804.1,
                                           SRR26360172.1194614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..621
                     /product="kelch-like protein 8"
                     /note="kelch-like 8"
                     /calculated_mol_wt=68437
     Region          53..172
                     /region_name="BTB_POZ_KLHL8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 8 (KLHL8); cd18238"
                     /db_xref="CDD:349547"
     Region          61..536
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          357..400
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          404..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          451..496
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          498..543
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..587
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          556..601
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..621
                     /gene="Klhl8"
                     /coded_by="NM_001437210.1:448..2313"
                     /db_xref="GeneID:289457"
                     /db_xref="RGD:1304685"
ORIGIN      
        1 masestngkl arshvtkgrr qqqqqqqvrs rssvsecdgd dsfifeanea wkdfhgsllg
       61 fyengelcdv tlkvgsklis chklalacvi pyframflse mseakqalie irdfdgdave
      121 dlvkfvyssr ltltvdnvqp llyaacilqv elvaraccey mklhfhpsnc lavrafaesh
      181 nrtdlmdmad qyacehftev vecedfvsvs pqhlhkllss sdlnidsekq vysaaikwll
      241 anpqhhpkwl detlaqvrlp llpvdflmgv vakeqivkqn lkcrdlldea rnyhlhlssk
      301 pvpdfeysvr ttprkhtagv lfcvggrggs gdpfrsiecy sintnswffg pemnsrrrhv
      361 gvisvegkvy avgghdgneh lgsmemfdpl tnkwmvkasm ntkrrgiala slggpiyaig
      421 glddntcfsd verydiesdq wstvapmntp rggvgsvali nhvyavggnd gvaslssver
      481 yhphldkwve vkemgqrrag ngvselhgcl yvvggfddns plssverydp rsnkwdyvaa
      541 lttprggvgi atvmgkifav gghngnayln tveafdpvln kwelvgpvsh cragagvavc
      601 dcltsqirdv ghgstnvvdc m
//
LOCUS       NP_001424108             198 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424108
VERSION     NP_001424108.1
DBSOURCE    REFSEQ: accession NM_001437179.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74654.1,
                                           SRR26360176.2433630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..198
                     /product="maestro isoform 8"
                     /note="protein maestro"
                     /calculated_mol_wt=22776
     Region          40..73
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          83..112
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..198
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437179.1:392..988"
                     /note="isoform 8 is encoded by transcript variant 16"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvrkykkvm ldllvhglyd pvssevihes
       61 vktltimlgk iqgqrlgsff iditlqtrtl lddeddsvry safvlfgqla afagrkwkkf
      121 fthqvnqtqd sllshlqdes pqvakactma vqacvpylkp rkeqsfqsee dqknrrlsqq
      181 lshyhpeill ffyankil
//
LOCUS       NP_001424143             559 aa            linear   ROD 28-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001424143 XP_038947615
VERSION     NP_001424143.1
DBSOURCE    REFSEQ: accession NM_001437214.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_038947615.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.51564.1,
                                           SRR26643284.17027.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..559
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     5"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=62610
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..559
                     /gene="Fip1l1"
                     /coded_by="NM_001437214.1:203..1882"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki taedctmevt pgaeiqdgrf nlfkvqqgrt
      241 gnsekeaalp stkaeftspp slfktglpps rrlpgaidvi gqtitisrve grrranensn
      301 iqvlsdrsat evdnnfskpp pffppgappt hlppppflpp pptvstappl ipppgfpppp
      361 gapppslipt iesghssgyd srsarafpyg nvafphltss apswpslvdt tkqwdyyarr
      421 ekdrdrdrer drdrererdr drerertrer ererdhsptp svfnsdeery ryreyaergy
      481 erhrasreke erhrerrhre keetrhkssr snsrrrhese egdshrrhkh kkskrskegk
      541 eagsepvpeq esteaapae
//
LOCUS       NP_001424117             647 aa            linear   ROD 28-MAR-2025
DEFINITION  alpha-adducin isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424117 XP_063128917
VERSION     NP_001424117.1
DBSOURCE    REFSEQ: accession NM_001437188.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_063128917.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1303223.1,
                                           SRR26360176.1479920.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..647
                     /product="alpha-adducin isoform 7"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=71229
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..647
                     /gene="Add1"
                     /coded_by="NM_001437188.1:181..2124"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kppnayascp
      481 phgllhwtke dghrtstsav pnlfvplntn pkevqemrnk ireqnlqdik tagpqsqvlc
      541 gvmmdrslvq gelvtaskai iekeyqphvi vsttgpnpfn tltdreleey rreverkqkg
      601 seenldetre qkeksppdqs avpntppstp vklegagdgc akeyllp
//
LOCUS       NP_001424134             724 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424134 XP_038947520
VERSION     NP_001424134.1
DBSOURCE    REFSEQ: accession NM_001437205.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_038947520.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.56333.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..724
                     /product="YTH domain-containing protein 1 isoform 5"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=84277
     Region          353..489
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     CDS             1..724
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437205.1:288..2462"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreeke dcqdcsswlf sdgelnvldd iltevpeqdd elynpeseqd knekkgskrk
       61 sermesidtk rqkpsihsrq liskplsssv snnkrivstk gksvteykne eyqrsernkr
      121 ldadrkirls ssssrepyks qpekpclrkr dserrakspt pdgserigle vdrrasrssq
      181 sskeegnsee ygsdhetgss asseqgnnte neeeggeedv eedeevdedg dddeevdeda
      241 eeeedeeede eeedeeeeee eeeeyeqder dqkeegndyd trseasdsgs esvsftdgsv
      301 rsgsgtdgsd ekkkerkrar gispivfdrs gssasesyad qtsklkyvlq darffliksn
      361 nhenvslaka kgvwstlpvn ekklnlafrs arsvilifsv resgkfqgfa rlsseshhgg
      421 spihwvlpag msakmlggvf kidwicrrel pftksahltn pwnehkpvki grdgqeiele
      481 cgtqlcllfp pdesidlyql ihkmrhkrrm hsqprsrgrp srrepvrdvg rrrpedydih
      541 nsrkkpridy ppefhqrpgy lkdpryqevd rrfsgvrrdv flngsyndyv refhnmgppp
      601 pwqgmppypg ieqpphhpyy qhhapppqah ppysghhpvp hearyrdkrv hdydmrvddf
      661 lrrtqavvsg rrsrprerdr ererdrprdn rrdrerdrgr drerereric drdrdrgerg
      721 ryrr
//
LOCUS       NP_001424107             198 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424107
VERSION     NP_001424107.1
DBSOURCE    REFSEQ: accession NM_001437178.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35237.1,
                                           SRR26643298.74648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..198
                     /product="maestro isoform 8"
                     /note="protein maestro"
                     /calculated_mol_wt=22776
     Region          40..73
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          83..112
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..198
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437178.1:251..847"
                     /note="isoform 8 is encoded by transcript variant 15"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvrkykkvm ldllvhglyd pvssevihes
       61 vktltimlgk iqgqrlgsff iditlqtrtl lddeddsvry safvlfgqla afagrkwkkf
      121 fthqvnqtqd sllshlqdes pqvakactma vqacvpylkp rkeqsfqsee dqknrrlsqq
      181 lshyhpeill ffyankil
//
LOCUS       NP_001424100             248 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424100
VERSION     NP_001424100.1
DBSOURCE    REFSEQ: accession NM_001437171.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.139832.1,
                                           SRR26643298.74655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..248
                     /product="maestro isoform 4"
                     /note="protein maestro"
                     /calculated_mol_wt=28602
     Region          52..200
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     CDS             1..248
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437171.1:392..1138"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kqvrkykkvm ldllvhglyd pvssevihes vktltimlgk
      121 iqgqrlgsff iditlqtrtl lddeddsvry safvlfgqla afagrkwkkf fthqvnqtqd
      181 sllshlqdes pqvakactma vqacvpylkp rkeqsfqsee dqknrrlsqq lshyhpeill
      241 ffyankil
//
LOCUS       NP_001424138             621 aa            linear   ROD 28-MAR-2025
DEFINITION  kelch-like protein 8 [Rattus norvegicus].
ACCESSION   NP_001424138 XP_008768226
VERSION     NP_001424138.1
DBSOURCE    REFSEQ: accession NM_001437209.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_008768226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1331123.1,
                                           SRR26643297.42726.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..621
                     /product="kelch-like protein 8"
                     /note="kelch-like 8"
                     /calculated_mol_wt=68437
     Region          53..172
                     /region_name="BTB_POZ_KLHL8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 8 (KLHL8); cd18238"
                     /db_xref="CDD:349547"
     Region          61..536
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          357..400
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          404..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          451..496
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          498..543
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..587
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          556..601
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..621
                     /gene="Klhl8"
                     /coded_by="NM_001437209.1:606..2471"
                     /db_xref="GeneID:289457"
                     /db_xref="RGD:1304685"
ORIGIN      
        1 masestngkl arshvtkgrr qqqqqqqvrs rssvsecdgd dsfifeanea wkdfhgsllg
       61 fyengelcdv tlkvgsklis chklalacvi pyframflse mseakqalie irdfdgdave
      121 dlvkfvyssr ltltvdnvqp llyaacilqv elvaraccey mklhfhpsnc lavrafaesh
      181 nrtdlmdmad qyacehftev vecedfvsvs pqhlhkllss sdlnidsekq vysaaikwll
      241 anpqhhpkwl detlaqvrlp llpvdflmgv vakeqivkqn lkcrdlldea rnyhlhlssk
      301 pvpdfeysvr ttprkhtagv lfcvggrggs gdpfrsiecy sintnswffg pemnsrrrhv
      361 gvisvegkvy avgghdgneh lgsmemfdpl tnkwmvkasm ntkrrgiala slggpiyaig
      421 glddntcfsd verydiesdq wstvapmntp rggvgsvali nhvyavggnd gvaslssver
      481 yhphldkwve vkemgqrrag ngvselhgcl yvvggfddns plssverydp rsnkwdyvaa
      541 lttprggvgi atvmgkifav gghngnayln tveafdpvln kwelvgpvsh cragagvavc
      601 dcltsqirdv ghgstnvvdc m
//
LOCUS       NP_001424094             286 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424094
VERSION     NP_001424094.1
DBSOURCE    REFSEQ: accession NM_001437165.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54680.1,
                                           SRR26643287.35239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..286
                     /product="maestro isoform 1"
                     /note="protein maestro"
                     /calculated_mol_wt=32790
     Region          90..238
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          128..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          171..200
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..286
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437165.1:265..1125"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mcsktkmtek tnphpplrpt esaalmrgcl rglesvsfme qmqripnqpl ptpasqskkr
       61 rtplssffsk vswklrlqkr eplknlffvl aerargpnpr krhlamrglg ilaheapdkq
      121 vrkykkvmld llvhglydpv ssevihesvk tltimlgkiq gqrlgsffid itlqtrtlld
      181 deddsvrysa fvlfgqlaaf agrkwkkfft hqvnqtqdsl lshlqdespq vakactmavq
      241 acvpylkprk eqsfqseedq knrrlsqqls hyhpeillff yankil
//
LOCUS       NP_001424104             233 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424104
VERSION     NP_001424104.1
DBSOURCE    REFSEQ: accession NM_001437175.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77780.1,
                                           SRR26360186.1703029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..233
                     /product="maestro isoform 6"
                     /note="protein maestro"
                     /calculated_mol_wt=26887
     CDS             1..233
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437175.1:220..921"
                     /note="isoform 6 is encoded by transcript variant 12"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 meqmqripnq plptpasqsk krrtplssff skvswklrlq kreplknlff vlaerargpn
       61 prkrhlamrg lgilaheapd kqvrkykkvm ldllvhglyd pvssevihes vktltimlgk
      121 iqgqrlgsff iditlqtrtl lddlaafagr kwkkffthqv nqtqdsllsh lqdespqvak
      181 actmavqacv pylkprkeqs fqseedqknr rlsqqlshyh peillffyan kil
//
LOCUS       NP_001424097             266 aa            linear   ROD 28-MAR-2025
DEFINITION  maestro isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424097
VERSION     NP_001424097.1
DBSOURCE    REFSEQ: accession NM_001437168.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.686711.1,
                                           SRR26360176.1907309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..266
                     /product="maestro isoform 3"
                     /note="protein maestro"
                     /calculated_mol_wt=30633
     Region          67..95
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          71..218
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          107..142
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          151..176
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..266
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437168.1:183..983"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mlcwlqiprg psgfsfcsfm eqmqripnqp lptpasqskk rrtplssffs kvswklrlqk
       61 replknlffv laerargpnp rkrhlamrgl gilaheapdk vrkykkvmld llvhglydpv
      121 ssevihesvk tltimlgkiq gqrlgsffid itlqtrtlld deddsvrysa fvlfgqlaaf
      181 agrkwkkfft hqvnqtqdsl lshlqdespq vakactmavq acvpylkprk eqsfqseedq
      241 knrrlsqqls hyhpeillff yankil
//
LOCUS       NP_596914                738 aa            linear   ROD 28-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_596914
VERSION     NP_596914.2
DBSOURCE    REFSEQ: accession NM_133423.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced NP_596914.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF144731.1, SRR26360190.1179073.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..738
                     /product="YTH domain-containing protein 1 isoform 1"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=85771
     Region          1..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          359..495
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          512..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          618..654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          680..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     CDS             1..738
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_133423.2:288..2504"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreekd gelnvlddil tevpeqddel ynpeseqdkn ekkgskrkse rmesidtkrq
       61 kpsihsrqli skplsssvsn nkrivstkgk svteykneey qrsernkrld adrkirlsss
      121 ssrepyksqp ekpclrkrds erraksptpd gseriglevd rrasrssqss keegnseeyg
      181 sdhetgssas seqgnntene eeggeedvee deevdedgdd deevdedaee eedeeedeee
      241 edeeeeeeee eeyeqderdq keegndydtr seasdsgses vsftdgsvrs gsgtdgsdek
      301 kkerkrargi spivfdrsgs sasesyagse kkheklsssv ravrkdqtsk lkyvlqdarf
      361 fliksnnhen vslakakgvw stlpvnekkl nlafrsarsv ilifsvresg kfqgfarlss
      421 eshhggspih wvlpagmsak mlggvfkidw icrrelpftk sahltnpwne hkpvkigrdg
      481 qeielecgtq lcllfppdes idlyqlihkm rhkrrmhsqp rsrgrpsrre pvrdvgrrrp
      541 edydihnsrk kpridyppef hqrpgylkdp ryqevdsftn lipnrrfsgv rrdvflngsy
      601 ndyvrefhnm gppppwqgmp pypgieqpph hpyyqhhapp pqahppysgh hpvphearyr
      661 dkrvhdydmr vddflrrtqa vvsgrrsrpr erdrererdr prdnrrdrer drgrdrerer
      721 ericdrdrdr gergryrr
//
LOCUS       NP_001423985             554 aa            linear   ROD 28-MAR-2025
DEFINITION  hyaluronan synthase 3 [Rattus norvegicus].
ACCESSION   NP_001423985 XP_006255623
VERSION     NP_001423985.1
DBSOURCE    REFSEQ: accession NM_001437056.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Bart,G., Vico,N.O., Hassinen,A., Pujol,F.M., Deen,A.J., Ruusala,A.,
            Tammi,R.H., Squire,A., Heldin,P., Kellokumpu,S. and Tammi,M.I.
  TITLE     Fluorescence resonance energy transfer (FRET) and proximity
            ligation assays reveal functionally relevant homo- and heteromeric
            complexes among hyaluronan synthases HAS1, HAS2, and HAS3
  JOURNAL   J Biol Chem 290 (18), 11479-11490 (2015)
   PUBMED   25795779
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Torronen,K., Nikunen,K., Karna,R., Tammi,M., Tammi,R. and Rilla,K.
  TITLE     Tissue distribution and subcellular localization of hyaluronan
            synthase isoenzymes
  JOURNAL   Histochem Cell Biol 141 (1), 17-31 (2014)
   PUBMED   24057227
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Rauhala,L., Hamalainen,L., Salonen,P., Bart,G., Tammi,M.,
            Pasonen-Seppanen,S. and Tammi,R.
  TITLE     Low dose ultraviolet B irradiation increases hyaluronan synthesis
            in epidermal keratinocytes via sequential induction of hyaluronan
            synthases Has1-3 mediated by p38 and Ca2+/calmodulin-dependent
            protein kinase II (CaMKII) signaling
  JOURNAL   J Biol Chem 288 (25), 17999-18012 (2013)
   PUBMED   23645665
  REMARK    GeneRIF: Data indicate that p38 and Ca(2+)/calmodulin-dependent
            protein kinase II pathways were found to be involved in the
            UVB-induced up-regulation of Has2 and Has3 expression.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Ormiston,M.L., Slaughter,G.R., Deng,Y., Stewart,D.J. and
            Courtman,D.W.
  TITLE     The enzymatic degradation of hyaluronan is associated with disease
            progression in experimental pulmonary hypertension
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 298 (2), L148-L157 (2010)
   PUBMED   19915162
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Mrabat,H., Beagle,J., Hang,Z., Garg,H.G., Hales,C.A. and Quinn,D.A.
  TITLE     Inhibition of HA synthase 3 mRNA expression, with a
            phosphodiesterase 3 inhibitor, blocks lung injury in a septic
            ventilated rat model
  JOURNAL   Lung 187 (4), 233-239 (2009)
   PUBMED   19572173
  REMARK    GeneRIF: Inhibition of HA synthase 3 mRNA expression, with a
            phosphodiesterase 3 inhibitor, blocks lung injury in a septic
            ventilated rat model.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Karvinen,S., Pasonen-Seppanen,S., Hyttinen,J.M., Pienimaki,J.P.,
            Torronen,K., Jokela,T.A., Tammi,M.I. and Tammi,R.
  TITLE     Keratinocyte growth factor stimulates migration and hyaluronan
            synthesis in the epidermis by activation of keratinocyte hyaluronan
            synthases 2 and 3
  JOURNAL   J Biol Chem 278 (49), 49495-49504 (2003)
   PUBMED   14506240
  REMARK    GeneRIF: belongs to the targets of keratinocyte growth factor in
            keratinocytes, and support the idea that enhanced hyaluronan
            synthesis acts an effector for the migratory response of
            keratinocytes in wound healing
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Pasonen-Seppanen,S., Karvinen,S., Torronen,K., Hyttinen,J.M.,
            Jokela,T., Lammi,M.J., Tammi,M.I. and Tammi,R.
  TITLE     EGF upregulates, whereas TGF-beta downregulates, the hyaluronan
            synthases Has2 and Has3 in organotypic keratinocyte cultures:
            correlations with epidermal proliferation and differentiation
  JOURNAL   J Invest Dermatol 120 (6), 1038-1044 (2003)
   PUBMED   12787132
  REMARK    GeneRIF: Epidermal hyaluronan synthesis, controlled by epidermal
            growth factor and transforming growth factor beta through changes
            in expression of Has2 and Has3, correlates with epidermal
            proliferation, thickness, and differentiation.
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Oishi,Y., Kato,H. and Noguchi,T.
  TITLE     Dietary protein as a potent regulator of the hyaluronan synthase
            gene in rat skin
  JOURNAL   Biosci Biotechnol Biochem 67 (4), 736-742 (2003)
   PUBMED   12784612
  REMARK    GeneRIF: protein malnutrition has a primary impact on the gene
            expression of Has2 and Has3, which leads to the reduction of
            hyaluronan content and to disfunction of the skin
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Itano,N., Sawai,T., Yoshida,M., Lenas,P., Yamada,Y., Imagawa,M.,
            Shinomura,T., Hamaguchi,M., Yoshida,Y., Ohnuki,Y., Miyauchi,S.,
            Spicer,A.P., McDonald,J.A. and Kimata,K.
  TITLE     Three isoforms of mammalian hyaluronan synthases have distinct
            enzymatic properties
  JOURNAL   J Biol Chem 274 (35), 25085-25092 (1999)
   PUBMED   10455188
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Hoock,T.C., Peters,L.L. and Lux,S.E.
  TITLE     Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate
            with mouse macrophage lysosomes
  JOURNAL   J Cell Biol 136 (5), 1059-1070 (1997)
   PUBMED   9060470
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006255623.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.52876.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN12840106
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..554
                     /product="hyaluronan synthase 3"
                     /EC_number="2.4.1.212"
                     /calculated_mol_wt=63219
     Region          87..365
                     /region_name="GT2_HAS"
                     /note="Hyaluronan synthases catalyze polymerization of
                     hyaluronan; cd06434"
                     /db_xref="CDD:133056"
     Site            216..218
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133056"
     CDS             1..554
                     /gene="Has3"
                     /coded_by="NM_001437056.1:117..1781"
                     /db_xref="GeneID:266805"
                     /db_xref="RGD:628656"
ORIGIN      
        1 mpvqlttalr vvgtslfalv vlggilaayv tgyqfihtek hylsfglyga ilglhlliqs
       61 lfaflehrrm rragrplklh csqrrrsval ciaayqedpe ylrkclrsaq riafpnlkvv
      121 mvvdgnrqed aymldifhev lggteqagff vwrsnfheag egeteaslqe gmervravvw
      181 astfscimqk wggkrevmyt afkalgnsvd yiqvcdsdtv ldpactieml rvleedpqvg
      241 gvggdvqiln kydswisfls svrywmafnv eracqsyfgc vqcisgplgm yrnsllqqfl
      301 edwyhqkflg skcsfgddrh ltnrvlslgy rtkytarskc ltetptkylr wlnqqtrwsk
      361 syfrewlyns lwfhkhhlwm tyesvvtgff pffliatviq lfyrgriwni llflltvqlv
      421 giikatyacf lrgnaemifm slysllymss llpakifaia tinksgwgts grktivvnfi
      481 glipvsiwva vllgglayta ycqdlfsete laflvsgail ygcywvallm lylaiiarrc
      541 gkkpeqysla faev
//
LOCUS       NP_001424001            1188 aa            linear   ROD 28-MAR-2025
DEFINITION  pumilio homolog 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424001 XP_006239094
VERSION     NP_001424001.1
DBSOURCE    REFSEQ: accession NM_001437072.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Lee,S., Kopp,F., Chang,T.C., Sataluri,A., Chen,B., Sivakumar,S.,
            Yu,H., Xie,Y. and Mendell,J.T.
  TITLE     Noncoding RNA NORAD Regulates Genomic Stability by Sequestering
            PUMILIO Proteins
  JOURNAL   Cell 164 (1-2), 69-80 (2016)
   PUBMED   26724866
REFERENCE   4  (residues 1 to 1188)
  AUTHORS   Gennarino,V.A., Singh,R.K., White,J.J., De Maio,A., Han,K.,
            Kim,J.Y., Jafar-Nejad,P., di Ronza,A., Kang,H., Sayegh,L.S.,
            Cooper,T.A., Orr,H.T., Sillitoe,R.V. and Zoghbi,H.Y.
  TITLE     Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
            increasing wild-type Ataxin1 levels
  JOURNAL   Cell 160 (6), 1087-1098 (2015)
   PUBMED   25768905
REFERENCE   5  (residues 1 to 1188)
  AUTHORS   Narita,R., Takahasi,K., Murakami,E., Hirano,E., Yamamoto,S.P.,
            Yoneyama,M., Kato,H. and Fujita,T.
  TITLE     A novel function of human Pumilio proteins in cytoplasmic sensing
            of viral infection
  JOURNAL   PLoS Pathog 10 (10), e1004417 (2014)
   PUBMED   25340845
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1188)
  AUTHORS   Chen,D., Zheng,W., Lin,A., Uyhazi,K., Zhao,H. and Lin,H.
  TITLE     Pumilio 1 suppresses multiple activators of p53 to safeguard
            spermatogenesis
  JOURNAL   Curr Biol 22 (5), 420-425 (2012)
   PUBMED   22342750
REFERENCE   7  (residues 1 to 1188)
  AUTHORS   Miles,W.O., Tschop,K., Herr,A., Ji,J.Y. and Dyson,N.J.
  TITLE     Pumilio facilitates miRNA regulation of the E2F3 oncogene
  JOURNAL   Genes Dev 26 (4), 356-368 (2012)
   PUBMED   22345517
REFERENCE   8  (residues 1 to 1188)
  AUTHORS   Filipovska,A., Razif,M.F., Nygard,K.K. and Rackham,O.
  TITLE     A universal code for RNA recognition by PUF proteins
  JOURNAL   Nat Chem Biol 7 (7), 425-427 (2011)
   PUBMED   21572425
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1188)
  AUTHORS   Kedde,M., van Kouwenhove,M., Zwart,W., Oude Vrielink,J.A., Elkon,R.
            and Agami,R.
  TITLE     A Pumilio-induced RNA structure switch in p27-3' UTR controls
            miR-221 and miR-222 accessibility
  JOURNAL   Nat Cell Biol 12 (10), 1014-1020 (2010)
   PUBMED   20818387
REFERENCE   10 (residues 1 to 1188)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006239094.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.16251.1,
                                           SRR26643297.20301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1188
                     /product="pumilio homolog 1 isoform 1"
                     /note="pumilio 1; pumilio homolog 1"
                     /calculated_mol_wt=126372
     Region          843..1166
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(899..900,903,935..936,939,974,977,1009..1010,1013,
                     1042..1043,1045..1046,1049,1078..1079,1081..1082,1085,
                     1121..1122,1124..1125,1128,1158,1161)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1188
                     /gene="Pum1"
                     /coded_by="NM_001437072.1:114..3680"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362609"
                     /db_xref="RGD:1307190"
ORIGIN      
        1 msvacvlkrk avlwqdsfsp hlkhhpqepa npnmpvvlts gtgsqaqpqp aanqalaagt
       61 hsspvpgsig vagrsqddam vdyffqrqhg eqlggggsgg ggyntskhrw ptgdnihaeh
      121 qvrsmdelnh dfqalalegr amgeqllpgk kfwetdessk dgpkgiflgd qwrdsawgts
      181 dhsvsqpimv qrrpgqsfhv nsevnsvlsp rsesgglgvs mveyvlsssp gdsclrkggf
      241 gprdadsden dkgekknkga fdgdklgdlk eegdvmdktn glpvqngida dvkdfsrtpg
      301 ncqssanevd llgpnqngse glaqltstng akpvedfsnm esqsvpldpm ehvgmeplqf
      361 dysgtqvpvd saaatvglfd ynsqqqlfqr pnalavqqlt aaqqqqyala aahqphigla
      421 paafvpnpyi isaappgtdp ytaglaaaat lgpavvphqy ygvtpwgvyp aslfqqqaaa
      481 aaaatnsatq qsapqaqqgq qqvlrggasq rpltpnqnqq gqqtdplvaa aavnsalafg
      541 qglaagmpgy pvlapaayyd qtgalvvnag arnglgapvr lvapapviis ssaaqaavaa
      601 aaasangaag glagttngpf rplgtqqpqp qpqqqpsnnl asssfygnns lssnsqsssl
      661 fsqgsaqpan tslgfgssss lgatlgsalg gfgtavansn tgsgsrrdsl tgssdlykrt
      721 ssslapighs fynslsfsss pgpvgmplps qgpghsqtpp pslsshgsss slnlggltng
      781 sgryisaapg aeakyrsass asslfspsst lfsssrlryg msdvmpsgrs rlledfrnnr
      841 ypnlqlreia ghimefsqdq hgsrfiqlkl erataaerql vfneilqaay qlmvdvfgny
      901 viqkffefgs heqklalaer irghvlslal qmygcrviqk alefipsdqq vinemvreld
      961 ghvlkcvkdq ngnhvvqkci ecvqpqslqf iidafkgqvf alsthpygcr viqrilehcl
     1021 pdqtlpilee lhqhteqlvq dqygnyviqh vlehgrpedk skivaeirgn vlvlsqhkfa
     1081 snvvekcvth asrteravli devctmndgp hsalytmmkd qyanyvvqkm idvaepgqrk
     1141 ivmhkirphi atlrkytygk hilaklekyy mkngvdlgpi cgppngii
//
LOCUS       NP_001423521             218 aa            linear   ROD 28-MAR-2025
DEFINITION  clathrin light chain A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423521 XP_006238168
VERSION     NP_001423521.1
DBSOURCE    REFSEQ: accession NM_001436592.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Li,H., Alavian,K.N., Lazrove,E., Mehta,N., Jones,A., Zhang,P.,
            Licznerski,P., Graham,M., Uo,T., Guo,J., Rahner,C., Duman,R.S.,
            Morrison,R.S. and Jonas,E.A.
  TITLE     A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
            during endocytosis
  JOURNAL   Nat Cell Biol 15 (7), 773-785 (2013)
   PUBMED   23792689
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Bu,W., Lim,K.B., Yu,Y.H., Chou,A.M., Sudhaharan,T. and Ahmed,S.
  TITLE     Cdc42 interaction with N-WASP and Toca-1 regulates membrane
            tubulation, vesicle formation and vesicle motility: implications
            for endocytosis
  JOURNAL   PLoS One 5 (8), e12153 (2010)
   PUBMED   20730103
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Mettlen,M., Loerke,D., Yarar,D., Danuser,G. and Schmid,S.L.
  TITLE     Cargo- and adaptor-specific mechanisms regulate clathrin-mediated
            endocytosis
  JOURNAL   J Cell Biol 188 (6), 919-933 (2010)
   PUBMED   20231386
  REMARK    GeneRIF: The results underscore the highly dynamic and
            cargo-responsive nature of CCP assembly and suggest that the
            observed heterogeneity is, in part, related to compositional
            differences (e.g., cargo and adaptors) between CCPs.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Drake,M.T., Downs,M.A. and Traub,L.M.
  TITLE     Epsin binds to clathrin by associating directly with the
            clathrin-terminal domain. Evidence for cooperative binding through
            two discrete sites
  JOURNAL   J Biol Chem 275 (9), 6479-6489 (2000)
   PUBMED   10692452
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Saito,Y., Tsubuki,S., Ito,H., Ohmi-Imajo,S. and Kawashima,S.
  TITLE     Possible involvement of clathrin in neuritogenesis induced by a
            protease inhibitor (benzyloxycarbonyl-Leu-Leu-Leu-aldehyde) in PC12
            cells
  JOURNAL   J Biochem 112 (4), 448-455 (1992)
   PUBMED   1490999
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Maycox,P.R., Link,E., Reetz,A., Morris,S.A. and Jahn,R.
  TITLE     Clathrin-coated vesicles in nervous tissue are involved primarily
            in synaptic vesicle recycling
  JOURNAL   J Cell Biol 118 (6), 1379-1388 (1992)
   PUBMED   1325974
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Kirchhausen,T., Scarmato,P., Harrison,S.C., Monroe,J.J., Chow,E.P.,
            Mattaliano,R.J., Ramachandran,K.L., Smart,J.E., Ahn,A.H. and
            Brosius,J.
  TITLE     Clathrin light chains LCA and LCB are similar, polymorphic, and
            share repeated heptad motifs
  JOURNAL   Science 236 (4799), 320-324 (1987)
   PUBMED   3563513
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Brodsky,F.M.
  TITLE     Clathrin structure characterized with monoclonal antibodies. II.
            Identification of in vivo forms of clathrin
  JOURNAL   J Cell Biol 101 (6), 2055-2062 (1985)
   PUBMED   4066749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238168.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220908.1, BC087577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..218
                     /product="clathrin light chain A isoform 1"
                     /note="clathrin, light polypeptide (Lca); clathrin, light
                     chain (Lca); lca"
                     /calculated_mol_wt=23435
     Region          22..218
                     /region_name="Clathrin_lg_ch"
                     /note="Clathrin light chain; pfam01086"
                     /db_xref="CDD:460056"
     CDS             1..218
                     /gene="Clta"
                     /gene_synonym="LCA1; LCA2; LCA3"
                     /coded_by="NM_001436592.1:124..780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:83800"
                     /db_xref="RGD:70919"
ORIGIN      
        1 maeldpfgap agapggpalg ngvagageed paaaflaqqe seiagiende afaildggap
       61 gpqahgeppg gpdavdgvmn geyyqesngp tdsyaaisev drlqsepesi rkwreeqter
      121 lealdansrk qeaewkekav keleewyarq deqlqktkas nraaeeafvn didesspgte
      181 wervarlcdf npksskqakd vsrmrsvlis lkqaplvh
//
LOCUS       NP_001423918             465 aa            linear   ROD 28-MAR-2025
DEFINITION  homeobox protein Meis1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001423918 XP_006251591
VERSION     NP_001423918.1
DBSOURCE    REFSEQ: accession NM_001436989.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Yao,M.Z., Ge,X.Y., Liu,T., Huang,N., Liu,H., Chen,Y., Zhang,Z. and
            Hu,C.P.
  TITLE     MEIS1 regulated proliferation and migration of pulmonary artery
            smooth muscle cells in hypoxia-induced pulmonary hypertension
  JOURNAL   Life Sci 255, 117822 (2020)
   PUBMED   32450174
  REMARK    GeneRIF: MEIS1 regulated the proliferation and migration of
            pulmonary artery smooth muscle cells during hypoxia-induced
            pulmonary hypertension
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,Y., Si,Y. and Ma,N.
  TITLE     Meis1 promotes poly (rC)-binding protein 2 expression and inhibits
            angiotensin II-induced cardiomyocyte hypertrophy
  JOURNAL   IUBMB Life 68 (1), 13-22 (2016)
   PUBMED   26597775
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Pandey,R., Yang,Y., Jackson,L. and Ahmed,R.P.
  TITLE     MicroRNAs regulating meis1 expression and inducing cardiomyocyte
            proliferation
  JOURNAL   Cardiovasc Regen Med 3 (2016)
   PUBMED   28111633
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Jolma,A., Yin,Y., Nitta,K.R., Dave,K., Popov,A., Taipale,M.,
            Enge,M., Kivioja,T., Morgunova,E. and Taipale,J.
  TITLE     DNA-dependent formation of transcription factor pairs alters their
            binding specificity
  JOURNAL   Nature 527 (7578), 384-388 (2015)
   PUBMED   26550823
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Spieler,D., Kaffe,M., Knauf,F., Bessa,J., Tena,J.J., Giesert,F.,
            Schormair,B., Tilch,E., Lee,H., Horsch,M., Czamara,D., Karbalai,N.,
            von Toerne,C., Waldenberger,M., Gieger,C., Lichtner,P.,
            Claussnitzer,M., Naumann,R., Muller-Myhsok,B., Torres,M.,
            Garrett,L., Rozman,J., Klingenspor,M., Gailus-Durner,V., Fuchs,H.,
            Hrabe de Angelis,M., Beckers,J., Holter,S.M., Meitinger,T.,
            Hauck,S.M., Laumen,H., Wurst,W., Casares,F., Gomez-Skarmeta,J.L.
            and Winkelmann,J.
  TITLE     Restless legs syndrome-associated intronic common variant in Meis1
            alters enhancer function in the developing telencephalon
  JOURNAL   Genome Res 24 (4), 592-603 (2014)
   PUBMED   24642863
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Toresson,H., Parmar,M. and Campbell,K.
  TITLE     Expression of Meis and Pbx genes and their protein products in the
            developing telencephalon: implications for regional differentiation
  JOURNAL   Mech Dev 94 (1-2), 183-187 (2000)
   PUBMED   10842069
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Jacobs,Y., Schnabel,C.A. and Cleary,M.L.
  TITLE     Trimeric association of Hox and TALE homeodomain proteins mediates
            Hoxb2 hindbrain enhancer activity
  JOURNAL   Mol Cell Biol 19 (7), 5134-5142 (1999)
   PUBMED   10373562
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Knoepfler,P.S., Calvo,K.R., Chen,H., Antonarakis,S.E. and
            Kamps,M.P.
  TITLE     Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an
            interaction surface disrupted in oncoprotein E2a-Pbx1
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14553-14558 (1997)
   PUBMED   9405651
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Shen,W.F., Montgomery,J.C., Rozenfeld,S., Moskow,J.J.,
            Lawrence,H.J., Buchberg,A.M. and Largman,C.
  TITLE     AbdB-like Hox proteins stabilize DNA binding by the Meis1
            homeodomain proteins
  JOURNAL   Mol Cell Biol 17 (11), 6448-6458 (1997)
   PUBMED   9343407
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Chang,C.P., Jacobs,Y., Nakamura,T., Jenkins,N.A., Copeland,N.G. and
            Cleary,M.L.
  TITLE     Meis proteins are major in vivo DNA binding partners for wild-type
            but not chimeric Pbx proteins
  JOURNAL   Mol Cell Biol 17 (10), 5679-5687 (1997)
   PUBMED   9315626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006251591.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.47505.1,
                                           SRR26643299.55625.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..465
                     /product="homeobox protein Meis1 isoform 3"
                     /note="homeobox protein Meis1; Meis1, myeloid ecotropic
                     viral integration site 1 homolog"
                     /calculated_mol_wt=50602
     Region          108..192
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Site            order(278,321,324..325,328)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          291..329
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          <301..445
                     /region_name="Cytadhesin_P30"
                     /note="Cytadhesin P30/P32; pfam07271"
                     /db_xref="CDD:429374"
     CDS             1..465
                     /gene="Meis1"
                     /coded_by="NM_001436989.1:727..2124"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:686117"
                     /db_xref="RGD:1585482"
ORIGIN      
        1 maqryddlph yggmdgvgip stmygdphaa rsmqpvhhln hgpplhshqy phtahtnama
       61 psmgssvnda lkrdkdaiyg hplfpllali fekcelatct prepgvaggd vcssesfned
      121 iavfakqira ekplfssnpe ldnlmiqaiq vlrfhllele kvhelcdnfc hryisclkgk
      181 mpidlviddr eggsksdsed vtraanltdq pswnrdhddt astrsggtpg pssgghtshs
      241 gdnsseqgdg ldnsvaspst gddddpdkdk krhkkrgifp kvatnimraw lfqhlthpyp
      301 seeqkkqlaq dtgltilqvn nwfinarrri vqpmidqsnr avsqgtpynp dgqpmggfvm
      361 dgqqhmgira pglqsmpgey varggpmgvs mgqpsytqaq mpphpaqlrh gppmhtyipg
      421 hphhpavmmh ggqphpgmpm sasspsvlnt gdptmsgqvm nihaq
//
LOCUS       NP_001423586             425 aa            linear   ROD 28-MAR-2025
DEFINITION  probable G-protein coupled receptor 63 [Rattus norvegicus].
ACCESSION   NP_001423586 XP_006238011
VERSION     NP_001423586.1
DBSOURCE    REFSEQ: accession NM_001436657.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006238011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.12882.1,
                                           SRR26360190.2754819.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..425
                     /product="probable G-protein coupled receptor 63"
                     /calculated_mol_wt=47887
     Region          88..388
                     /region_name="7tmA_GPR63"
                     /note="G protein-coupled receptor 63, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15404"
                     /db_xref="CDD:320526"
     Region          89..115
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320526"
     Region          122..147
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320526"
     Site            order(144,147..148,160..165,167..168,171,213,215..219,245,
                     248..250,252..254,256..257,333,336..337,339..340,343,
                     355..356,358..360,363,366..367)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320526"
     Region          160..190
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320526"
     Region          199..221
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320526"
     Region          245..274
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320526"
     Region          313..343
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320526"
     Region          356..381
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320526"
     CDS             1..425
                     /gene="Gpr63"
                     /coded_by="NM_001436657.1:337..1614"
                     /db_xref="GeneID:297952"
                     /db_xref="RGD:1306460"
ORIGIN      
        1 mvvsgvltap avlttphtgt snmtfvvyen spmnitaplp fqhpspgpll rysletmtst
       61 gfsslavnst vvtpapavfk slnlalqiil saimifilfv sflgnlvvcl mvyqkaamrs
      121 ainillasma fadmllavln mpfalvtilt trwifgkffc rlsamffwlf viegvailli
      181 isidrfliiv qrqdklnpyr akvliavswa tafsvafpla vgnpdlqips rapqcvfgyt
      241 tnsgyqayvi lislisffip flvilysfmg ilntlrhnal rihsypegic lsqvsklglm
      301 slqrpfqmsi dmsfktraft tililfavfi vcwapfttys lvatfskhfy yqhnffeist
      361 wllwlcylks alnpliyywr ikkfhdacld mmpksfkflp rlpghtrrri rpsavyvcge
      421 hrtvl
//
LOCUS       NP_001423921             379 aa            linear   ROD 28-MAR-2025
DEFINITION  transcription factor Maf isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423921 XP_038953885
VERSION     NP_001423921.1
DBSOURCE    REFSEQ: accession NM_001436992.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Kim,M., Wende,H., Walcher,J., Kuhnemund,J., Cheret,C., Kempa,S.,
            McShane,E., Selbach,M., Lewin,G.R. and Birchmeier,C.
  TITLE     Maf links Neuregulin1 signaling to cholesterol synthesis in
            myelinating Schwann cells
  JOURNAL   Genes Dev 32 (9-10), 645-657 (2018)
   PUBMED   29748249
  REMARK    GeneRIF: a crucial role of the transcription factor Maf in
            myelination and cholesterol biosynthesis and show that Maf acts
            downstream from Neuregulin1
            Erratum:[Genes Dev. 2018 Aug 1;32(15-16):1101. doi:
            10.1101/gad.318477.118. PMID: 30068704]
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Narumi,Y., Nishina,S., Tokimitsu,M., Aoki,Y., Kosaki,R., Wakui,K.,
            Azuma,N., Murata,T., Takada,F., Fukushima,Y. and Kosho,T.
  TITLE     Identification of a novel missense mutation of MAF in a Japanese
            family with congenital cataract by whole exome sequencing: a
            clinical report and review of literature
  JOURNAL   Am J Med Genet A 164A (5), 1272-1276 (2014)
   PUBMED   24664492
  REMARK    Review article
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Aguayo-Mazzucato,C., Zavacki,A.M., Marinelarena,A.,
            Hollister-Lock,J., El Khattabi,I., Marsili,A., Weir,G.C.,
            Sharma,A., Larsen,P.R. and Bonner-Weir,S.
  TITLE     Thyroid hormone promotes postnatal rat pancreatic beta-cell
            development and glucose-responsive insulin secretion through MAFA
  JOURNAL   Diabetes 62 (5), 1569-1580 (2013)
   PUBMED   23305647
  REMARK    GeneRIF: Data suggest that triiodothyronine (T3) acts as
            physiological regulator of functional maturation of islet
            beta-cells via induction of MAFA/c-Maf; T3 has a direct
            receptor-ligand interaction with MAFA/c-Maf promoter.
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Lu,C.C., Appler,J.M., Houseman,E.A. and Goodrich,L.V.
  TITLE     Developmental profiling of spiral ganglion neurons reveals insights
            into auditory circuit assembly
  JOURNAL   J Neurosci 31 (30), 10903-10918 (2011)
   PUBMED   21795542
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Motomura,Y., Kitamura,H., Hijikata,A., Matsunaga,Y., Matsumoto,K.,
            Inoue,H., Atarashi,K., Hori,S., Watarai,H., Zhu,J., Taniguchi,M.
            and Kubo,M.
  TITLE     The transcription factor E4BP4 regulates the production of IL-10
            and IL-13 in CD4+ T cells
  JOURNAL   Nat Immunol 12 (5), 450-459 (2011)
   PUBMED   21460847
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Ring,B.Z., Cordes,S.P., Overbeek,P.A. and Barsh,G.S.
  TITLE     Regulation of mouse lens fiber cell development and differentiation
            by the Maf gene
  JOURNAL   Development 127 (2), 307-317 (2000)
   PUBMED   10603348
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Kawauchi,S., Takahashi,S., Nakajima,O., Ogino,H., Morita,M.,
            Nishizawa,M., Yasuda,K. and Yamamoto,M.
  TITLE     Regulation of lens fiber cell differentiation by transcription
            factor c-Maf
  JOURNAL   J Biol Chem 274 (27), 19254-19260 (1999)
   PUBMED   10383433
REFERENCE   8  (residues 1 to 379)
  AUTHORS   Kim,J.I., Ho,I.C., Grusby,M.J. and Glimcher,L.H.
  TITLE     The transcription factor c-Maf controls the production of
            interleukin-4 but not other Th2 cytokines
  JOURNAL   Immunity 10 (6), 745-751 (1999)
   PUBMED   10403649
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Matsushima-Hibiya,Y., Nishi,S. and Sakai,M.
  TITLE     Rat maf-related factors: the specificities of DNA binding and
            heterodimer formation
  JOURNAL   Biochem Biophys Res Commun 245 (2), 412-418 (1998)
   PUBMED   9571165
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Sakai,M., Imaki,J., Yoshida,K., Ogata,A., Matsushima-Hibaya,Y.,
            Kuboki,Y., Nishizawa,M. and Nishi,S.
  TITLE     Rat maf related genes: specific expression in chondrocytes, lens
            and spinal cord
  JOURNAL   Oncogene 14 (6), 745-750 (1997)
   PUBMED   9038383
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Mar 25, 2025 this sequence version replaced XP_038953885.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.53119.1,
                                           SRR26643298.76609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..379
                     /product="transcription factor Maf isoform 1"
                     /note="transcription factor Maf; C-Maf; proto-oncogene
                     c-maf; transcription factor Maf-2; v-maf avian
                     musculoaponeurotic fibrosarcoma oncogene homolog; bZip
                     transcription factor c-maf"
                     /calculated_mol_wt=39391
     mat_peptide     1..369
                     /product="Transcription factor Maf. /id=PRO_0000076493"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
                     /calculated_mol_wt=38398
     Region          57..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          86..119
                     /region_name="Maf_N"
                     /note="Maf N-terminal region; pfam08383"
                     /db_xref="CDD:462456"
     Region          126..369
                     /region_name="Represses ARE-mediated transcription.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          175..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Region          279..347
                     /region_name="bZIP_Maf_large"
                     /note="Basic leucine zipper (bZIP) domain of large
                     musculoaponeurotic fibrosarcoma (Maf) proteins: a
                     DNA-binding and dimerization domain; cd14718"
                     /db_xref="CDD:269866"
     Region          279..347
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269866"
     Region          284..309
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     Site            order(286,289..291,293..295,297..299,301..302,304..305)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269866"
     Site            order(305,312,315..316,319..320,322..323,326..327,
                     329..330,333,336..337,340..341,343..344)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269866"
     Region          312..333
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P54844.1)"
     CDS             1..379
                     /gene="Maf"
                     /gene_synonym="cMaf; Maf2"
                     /coded_by="NM_001436992.1:957..2096"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:54267"
                     /db_xref="RGD:3034"
ORIGIN      
        1 maselamnns dlptsplame yvndfdlmkf evkkepvetd riisqcgrli aggslsstpm
       61 stpcssvpps psfsapspgs gseqkahled yywmtgypqq lnpealgfsp edavealisn
      121 shqlqggfdg yargaqqlaa aagagagasl ggsgeemgpa aavvsaviaa aaaqsggaph
      181 yhhhhhhatg hhhhptagap gaagsasasa sgaggagggg pasagggggg ggggtagagg
      241 alhphhaagg lhfddrfsde qlvtmsvrel nrqlrgvske evirlkqkrr tlknrgyaqs
      301 crfkrvqqrh vleseknqll qqvdhlkqei srlvrerday kekyeklvss gfrengsssd
      361 npsspeffmy prdsstsvm
//
LOCUS       NP_001020136             140 aa            linear   ROD 28-MAR-2025
DEFINITION  trafficking protein particle complex subunit 2 [Rattus norvegicus].
ACCESSION   NP_001020136 XP_576952
VERSION     NP_001020136.1
DBSOURCE    REFSEQ: accession NM_001024965.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Milev,M.P., Hasaj,B., Saint-Dic,D., Snounou,S., Zhao,Q. and
            Sacher,M.
  TITLE     TRAMM/TrappC12 plays a role in chromosome congression, kinetochore
            stability, and CENP-E recruitment
  JOURNAL   J Cell Biol 209 (2), 221-234 (2015)
   PUBMED   25918224
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Menon,S., Cai,H., Lu,H., Dong,G., Cai,Y., Reinisch,K. and
            Ferro-Novick,S.
  TITLE     mBET3 is required for the organization of the TRAPP complexes
  JOURNAL   Biochem Biophys Res Commun 350 (3), 669-677 (2006)
   PUBMED   17027922
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Fan,L., Yu,W. and Zhu,X.
  TITLE     Interaction of Sedlin with chloride intracellular channel proteins
  JOURNAL   FEBS Lett 540 (1-3), 77-80 (2003)
   PUBMED   12681486
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Ghosh,A.K., Majumder,M., Steele,R., White,R.A. and Ray,R.B.
  TITLE     A novel 16-kilodalton cellular protein physically interacts with
            and antagonizes the functional activity of c-myc promoter-binding
            protein 1
  JOURNAL   Mol Cell Biol 21 (2), 655-662 (2001)
   PUBMED   11134351
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Gedeon,A.K., Colley,A., Jamieson,R., Thompson,E.M., Rogers,J.,
            Sillence,D., Tiller,G.E., Mulley,J.C. and Gecz,J.
  TITLE     Identification of the gene (SEDL) causing X-linked
            spondyloepiphyseal dysplasia tarda
  JOURNAL   Nat Genet 22 (4), 400-404 (1999)
   PUBMED   10431248
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091429.1.
            
            On or before Apr 26, 2006 this sequence version replaced
            XP_576952.1, XP_213295.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FN802820.1, CV110307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..140
                     /product="trafficking protein particle complex subunit 2"
                     /note="sedlin; trafficking protein particle complex
                     protein 2"
                     /calculated_mol_wt=16310
     Region          4..138
                     /region_name="TRAPPC2_sedlin"
                     /note="Trafficking protein particle complex subunit 2;
                     cd14825"
                     /db_xref="CDD:341429"
     Site            order(53..54,76..78,80,103,107,111)
                     /site_type="other"
                     /note="TRAPPC5 interface [polypeptide binding]"
                     /db_xref="CDD:341429"
     Site            order(108,111..114)
                     /site_type="other"
                     /note="TRAPPC3 interface [polypeptide binding]"
                     /db_xref="CDD:341429"
     CDS             1..140
                     /gene="Trappc2"
                     /coded_by="NM_001024965.1:105..527"
                     /db_xref="GeneID:501550"
                     /db_xref="RGD:1306925"
ORIGIN      
        1 msgsfyfviv ghhdnpvfem eflppgkaes kddhrhlnqf iahaaldlvd enmwlsnnmy
       61 lktvdkfnew fvsafvtagh mrfimlhdvr qedgiknfft dvydlyikfa mnpfyepnsp
      121 irssafdrkv qflgkkhlls
//
LOCUS       NP_001164022            3507 aa            linear   ROD 28-MAR-2025
DEFINITION  WD repeat and FYVE domain-containing protein 3 [Rattus norvegicus].
ACCESSION   NP_001164022 XP_001060345 XP_001060403 XP_223196
VERSION     NP_001164022.3
DBSOURCE    REFSEQ: accession NM_001170551.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3507)
  AUTHORS   Filimonenko,M., Isakson,P., Finley,K.D., Anderson,M., Jeong,H.,
            Melia,T.J., Bartlett,B.J., Myers,K.M., Birkeland,H.C., Lamark,T.,
            Krainc,D., Brech,A., Stenmark,H., Simonsen,A. and Yamamoto,A.
  TITLE     The selective macroautophagic degradation of aggregated proteins
            requires the PI3P-binding protein Alfy
  JOURNAL   Mol Cell 38 (2), 265-279 (2010)
   PUBMED   20417604
REFERENCE   2  (residues 1 to 3507)
  AUTHORS   Clausen,T.H., Lamark,T., Isakson,P., Finley,K., Larsen,K.B.,
            Brech,A., Overvatn,A., Stenmark,H., Bjorkoy,G., Simonsen,A. and
            Johansen,T.
  TITLE     p62/SQSTM1 and ALFY interact to facilitate the formation of p62
            bodies/ALIS and their degradation by autophagy
  JOURNAL   Autophagy 6 (3), 330-344 (2010)
   PUBMED   20168092
REFERENCE   3  (residues 1 to 3507)
  AUTHORS   Simonsen,A., Birkeland,H.C., Gillooly,D.J., Mizushima,N., Kuma,A.,
            Yoshimori,T., Slagsvold,T., Brech,A. and Stenmark,H.
  TITLE     Alfy, a novel FYVE-domain-containing protein associated with
            protein granules and autophagic membranes
  JOURNAL   J Cell Sci 117 (Pt 18), 4239-4251 (2004)
   PUBMED   15292400
REFERENCE   4  (residues 1 to 3507)
  AUTHORS   Chen,G.Y., Muramatsu,H., Ichihara-Tanaka,K. and Muramatsu,T.
  TITLE     Expression profile of mouse BWF1, a protein with a BEACH domain,
            WD40 domain and FYVE domain
  JOURNAL   Cell Struct Funct 29 (2), 35-42 (2004)
   PUBMED   15342963
REFERENCE   5  (residues 1 to 3507)
  AUTHORS   Uehara,K. and Muramatsu,T.
  TITLE     Molecular cloning and characterization of
            beta-1,4-galactosyltransferase expressed in mouse testis
  JOURNAL   Eur J Biochem 244 (3), 706-712 (1997)
   PUBMED   9108238
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Nov 27, 2020 this sequence version replaced NP_001164022.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3507
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..3507
                     /product="WD repeat and FYVE domain-containing protein 3"
                     /calculated_mol_wt=391690
     Region          2517..2640
                     /region_name="PH_BEACH"
                     /note="Pleckstrin homology domain in BEACH domain
                     containing proteins; cd01201"
                     /db_xref="CDD:275391"
     Region          2679..2959
                     /region_name="Beach"
                     /note="Beige/BEACH domain; pfam02138"
                     /db_xref="CDD:460459"
     Region          <3028..3230
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          3028..3055
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3067..3108
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3114..3150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3155..3192
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3199..3234
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3430..3494
                     /region_name="FYVE_WDFY3"
                     /note="FYVE domain found in WD40 repeat and FYVE
                     domain-containing protein 3 (WDFY3) and similar proteins;
                     cd15719"
                     /db_xref="CDD:277259"
     Site            order(3432,3435,3453..3458,3460..3461,3485..3487)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277259"
     CDS             1..3507
                     /gene="Wdfy3"
                     /coded_by="NM_001170551.4:220..10743"
                     /db_xref="GeneID:305164"
                     /db_xref="RGD:1307097"
ORIGIN      
        1 mnmvkrimgr prqeecspqd nalglmhlrr lftelchppr hmtqkeqeek lymmlpvfnr
       61 vfgnappstm tekfsdllqf ttqvsrlmvt eirrrasnks teaasraivq fleinqseea
      121 srgwmlltti nllassgqka vdcmttmsvp stlvkclylf fdlphvpeag ggaqselpla
      181 errgllqkaf vqilvklcsf vspaeelaqk ddlqllfsai tswcppynlp wrksagevlm
      241 tisrhglsvn vvkyihekec lstcvqnmqq sddlspleiv emfaglscfl kdssdvsqtl
      301 lddfriwqgy nflcdlllrl eqakeaecrd alkdlvslvt slttygvsel kpagvttgap
      361 fllpgfsvpq pagkghsvrn iqafavlqna flkaktnfla qiildaitdi ymadsanyfi
      421 lesqhtlsqf aekisklpev qskyfemlef vvfslnyipc kelisvsill ksssshhcsi
      481 vamktllkft rhdyifkdvf revgllevmv nllhkyaall kdpaqalgeq gdsrnnssve
      541 dqkhlallvm ealtvllqgs ntnagifref ggarcahniv kypqcrqhal mtiqqlvlsp
      601 ngeddmgtll glmhsappte lqlktdilra llsvlreshr srtvfrkvgg fvyitsllva
      661 merslssppk ngwekvnqnq vfellhtvfc tltaalryep anshffktei qyekladavr
      721 flgcfsdlrk isavnvfpsn tspfqrllee gavpmdsvsp tlrhcsklfi ylykvatdsf
      781 dsrteqippc ltsesslpsp wgtpalsrkr hafhcvstpp vypaksvtdl klqvtssplp
      841 sseaviihpg amlamldlla svgsvtqpeh aldlqlavan ilqslvhter nqqvmceagl
      901 harllqrcga aladedhslh pplqrmferl asqalepmvl reflrlaspl ncgawdkkll
      961 kqyrvhkpss lsfepdmrss vvtsleglgs dsvfsshedn hyriskslvk saegstvplt
     1021 rvkclvsmtt phdirlhgss vtpafvefdt slegfgclfl pslaphnapt nnavttgltd
     1081 gavvsgigsg erffpppsgl syscwfcieh fssppnnhpv rlltvvrran sseqhyvcla
     1141 ivlsakdrsl ivstkeellq nyvddfsees sfyeilpcca rfrcgelvve gqwhhlallm
     1201 srgmlknsta alyidgqlvs tvklhyvhst pggsgsanpp vlstvyayig tppaqrqmas
     1261 lvwrlgpthf leevlppssv taiyelgpdy vgsfqavlvp ckdsksegii pspvslvaee
     1321 kvsfglyals vssltvarir kvynkldska iakqlgissh enatpvklvh naaghlngpa
     1381 rtigaaligy lgvrtfvpkp vattlqyigg aaailglvam asdveglyaa vkalvcvvks
     1441 nplaskemer ikgyqllaml lkkrrsllns hilhltfslv gtvdsghets iipnstafqd
     1501 llcdfevwlh apyelhlslf ehfielltes seasknaklm refqlipkll ltlrdmslsq
     1561 ptiaamsnvl shllqgfpns ndllrfgqfi sstlptfavc ekfvvmeiin egkpdsgaee
     1621 efgglvsanl illrnrlldi llklvytske ktninlqace elvrtlgfdw immfmeehlh
     1681 pttvtaamri lvvllsnqsi likfkeglsg ggwleqtdsv ltnkigtvlg fnvgrsaggr
     1741 stvreinrda chfpgflvlq sflpkhtnvp alyfllmalf lqqpvselpe nlqvsvpvtn
     1801 srckqgcqfd ldsiwtfifg vpassgtvvs sihnvctesa flllgmlrsm lnspwqseee
     1861 gswlreypvt lmqffrylyh nvpdlasmwl spdflcalaa tvfpfnirpy semvtdldde
     1921 vgspaeefka faadtgmnrs qseycnvgtk tyltnhpakk fvfdfmrvli idnlcltpas
     1981 kqtplidlll easperstrt qqkefqthil dsvmdhllaa dvllgedasl pitsggsyqv
     2041 lvnnvfyftq rvvdklwqgm fnkeskllid fiiqliaqsk rrsqglslda vyhclnrtil
     2101 yqfsrahktv pqqvalldsl rvltvnrnli lgpgnhdqef isclahclin lhagssvegf
     2161 gleaearmtt whimipsdie pdggysqdis egrqllikav nrvwtelihs kkqvleevfk
     2221 vslpvndrgh vdiavarpli eeaglkgwqn hlahekkcis rgealvpttq sklsrvssgf
     2281 glskltgsrr nrkesglhkh spspqeisqw mfthiavvrd lvdtqykeyq erqqnalkyv
     2341 teewcqiece llrerglwgp pigshldkwm lemtegpcrm rkkmvrndmf ynhypyvpet
     2401 eqeasvgkpa ryrraisyds keyylrlasg nptivqdaiv essegeatqq epehgedtia
     2461 kvkglvkppl krsrsapdgg deetqeqlqd qiaesgsiee eektdnatll rlleegekiq
     2521 hmyrcarvqg ldtseglllf gkehfyvidg ftmtatreir dietlppnmh epiiprgarq
     2581 gpsqlkrtcs ifayedikev hkrryllqpi avevfsgdgr nyllafqkgi rnkvyqrfla
     2641 vvpsltdsse svsgqrpnts veqgsgllst lvgeksvtqr wergeisnfq ylmhlntlag
     2701 rsyndlmqyp vfpwiladyd seevdltnpk tfrnlakpmg aqtderlaqy kkrykdwedp
     2761 ngetpayhyg thyssamiva sylvrmepft qiflrlqggh fdladrmfhs vreawysask
     2821 hnmadvkeli peffylpefl fnsnnfdlgc kqngtklgdv ilppwakgdp refirvhrea
     2881 lecdyvsahl hewidlifgy kqqgpaavea vnvfhhlfye gqvdiynind plketatigf
     2941 innfgqipkq lfkkphppkr vrsrlngena glsvppgats dkiffhhldn lrpsltpvke
     3001 lkepvgqivc tdkgilaveq nkvlippawn ktfawgyadl scrlgtyesd kavavyecls
     3061 ewgqilcavc pspklvitgg tstvvcvwem gtskekakpl tlkqallght dtvtcatasi
     3121 ayhiivsgsr drtciiwdln klsfltqlrg hrapvsalci neltgdivsc agtyvhvwsi
     3181 ngnpivsvnt ftgrsqqivc ccmsemnewd tqnvivtghs dgvvrfwrme flqvpetpap
     3241 epvedlemqe gcpeaqigqq aqdedssdse aeepsvsqdp kdtpsqpsst shrpraascr
     3301 atatwctdsg sddsrrwsdq lsldekdgfi fvnysegqar ahpqgshshp nptearsysr
     3361 lkpgyrwerq lvfrskltmh tafdrkdnth paevtalgvs kdhsrilvgd srgrvfswsv
     3421 sdqpgrsaad hwvkdeggds csgcsvrfsl terrhhcrnc gqlfcqkcsr fqseikrlki
     3481 sspvrvcqnc yyslqherga ddgprnc
//
LOCUS       NP_001423979             106 aa            linear   ROD 28-MAR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 [Rattus
            norvegicus].
ACCESSION   NP_001423979 XP_006238889
VERSION     NP_001423979.1
DBSOURCE    REFSEQ: accession NM_001437050.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Huang,G., Chen,Y., Lu,H. and Cao,X.
  TITLE     Coupling mitochondrial respiratory chain to cell death: an
            essential role of mitochondrial complex I in the interferon-beta
            and retinoic acid-induced cancer cell death
  JOURNAL   Cell Death Differ 14 (2), 327-337 (2007)
   PUBMED   16826196
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006238889.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM090517.1, BP489095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN16676784
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..106
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 5"
                     /EC_number="7.1.1.2"
                     /note="NADH dehydrogenase (ubiquinone) Fe-S protein 5b,
                     15kDa (NADH-coenzyme Q reductase)"
                     /calculated_mol_wt=12569
     Region          1..96
                     /region_name="NDUFS5-like"
                     /note="mitochondrial complex I subunit NDUFS5 and similar
                     proteins; cl10892"
                     /db_xref="CDD:472051"
     CDS             1..106
                     /gene="Ndufs5"
                     /gene_synonym="Ndufs5b"
                     /coded_by="NM_001437050.1:73..393"
                     /db_xref="GeneID:362588"
                     /db_xref="RGD:1311081"
ORIGIN      
        1 mpfldvqkrl gisldrhfif lsaeqpykna archafekew iecahgigat rakkeckiey
       61 edfeecflrf ktirrmheik kqreklmkeg kytppphhlg keeprp
//
LOCUS       NP_001102566             540 aa            linear   ROD 28-MAR-2025
DEFINITION  probable G-protein coupled receptor 75 [Rattus norvegicus].
ACCESSION   NP_001102566 XP_001066164 XP_006251678 XP_573685
VERSION     NP_001102566.1
DBSOURCE    REFSEQ: accession NM_001109096.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Liu,B., Hassan,Z., Amisten,S., King,A.J., Bowe,J.E., Huang,G.C.,
            Jones,P.M. and Persaud,S.J.
  TITLE     The novel chemokine receptor, G-protein-coupled receptor 75, is
            expressed by islets and is coupled to stimulation of insulin
            secretion and improved glucose homeostasis
  JOURNAL   Diabetologia 56 (11), 2467-2476 (2013)
   PUBMED   23979485
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Ignatov,A., Robert,J., Gregory-Evans,C. and Schaller,H.C.
  TITLE     RANTES stimulates Ca2+ mobilization and inositol trisphosphate
            (IP3) formation in cells transfected with G protein-coupled
            receptor 75
  JOURNAL   Br J Pharmacol 149 (5), 490-497 (2006)
   PUBMED   17001303
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Mar 25, 2025 this sequence version replaced
            XP_006251678.1, XP_001066164.1, XP_573685.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.56130.1,
                                           SRR26360172.136069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..540
                     /product="probable G-protein coupled receptor 75"
                     /note="G protein-coupled receptor GPR75"
                     /calculated_mol_wt=59367
     Region          44..387
                     /region_name="7tmA_GPR75"
                     /note="G protein-coupled receptor 75, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15007"
                     /db_xref="CDD:320136"
     Region          44..70
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320136"
     Region          79..104
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320136"
     Site            order(101,104..105,118..123,125..126,129,173,175..179,199,
                     202..204,206..208,210..211,334,337..338,340..341,344,
                     354..355,357..359,362,365..366)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320136"
     Region          118..148
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320136"
     Region          159..181
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320136"
     Region          199..228
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320136"
     Region          314..344
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320136"
     Region          355..380
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320136"
     CDS             1..540
                     /gene="Gpr75"
                     /coded_by="NM_001109096.2:270..1892"
                     /db_xref="GeneID:498434"
                     /db_xref="RGD:1566385"
ORIGIN      
        1 mnssaplqnv pnatllytpp lqggnntslq eglrdfihta tlvtctvlla iifclgsygn
       61 fivflsffdp afrkfrtnfd fmilnlsfcd lficgatapm ftfvlffssa rsipdsfcft
      121 fhltssgfii mslkmvavia lhrlrmvmgk qpnctasfsc illltlllwa tsftlatlat
      181 lrtskshlcl pmsslmdgeg kailslyvvd ftfcvavvsv syimiaqtlr knaqvkkcpp
      241 vitvdasrpq pfmgasvkgn gdpiqctmpa lyrnqnynkl qhnqthgytk nanqmpipsa
      301 srlqlvsavn lstakdskav vtcmvivlsv lvcclplgis llqvvlsdsg sfilyqfelf
      361 gftliffksg lnpfiysrns aglrrkvlwc lrytglgflc ckqktrlram gkgnleinrn
      421 ksshhetnsa ymlspkpqkk fvdqacgpsh skesvaspkv saghhpcgqs sstpintrie
      481 pyysiynssp sqqesspanl qpvnsfgfas syiamhyytt ndlmqdydst sakqipipsv
//
LOCUS       NP_001424026             669 aa            linear   ROD 28-MAR-2025
DEFINITION  transcription factor 4 isoform 21 [Rattus norvegicus].
ACCESSION   NP_001424026 XP_038953086
VERSION     NP_001424026.1
DBSOURCE    REFSEQ: accession NM_001437097.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Sirp,A., Roots,K., Nurm,K., Tuvikene,J., Sepp,M. and Timmusk,T.
  TITLE     Functional consequences of TCF4 missense substitutions associated
            with Pitt-Hopkins syndrome, mild intellectual disability, and
            schizophrenia
  JOURNAL   J Biol Chem 297 (6), 101381 (2021)
   PUBMED   34748727
  REMARK    GeneRIF: Functional consequences of TCF4 missense substitutions
            associated with Pitt-Hopkins syndrome, mild intellectual
            disability, and schizophrenia.
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Li,N., Liu,B., Wu,W., Hong,Y., Zhang,J., Liu,Y., Zhang,M., Zhang,X.
            and Duan,G.
  TITLE     Upregulation of transcription factor 4 downregulates NaV1.8
            expression in DRG neurons and prevents the development of rat
            inflammatory and neuropathic hypersensitivity
  JOURNAL   Exp Neurol 327, 113240 (2020)
   PUBMED   32045596
  REMARK    GeneRIF: Upregulation of transcription factor 4 downregulates
            NaV1.8 expression in DRG neurons and prevents the development of
            rat inflammatory and neuropathic hypersensitivity.
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Han,F., Liu,W.B., Shi,X.Y., Yang,J.T., Zhang,X., Li,Z.M., Jiang,X.,
            Yin,L., Li,J.J., Huang,C.S., Cao,J. and Liu,J.Y.
  TITLE     SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling
            via Transcriptional and Posttranslational Regulation of
            beta-Catenin in Lung Cancer
  JOURNAL   EBioMedicine 31, 253-266 (2018)
   PUBMED   29739711
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Sepp,M., Vihma,H., Nurm,K., Urb,M., Page,S.C., Roots,K., Hark,A.,
            Maher,B.J., Pruunsild,P. and Timmusk,T.
  TITLE     The Intellectual Disability and Schizophrenia Associated
            Transcription Factor TCF4 Is Regulated by Neuronal Activity and
            Protein Kinase A
  JOURNAL   J Neurosci 37 (43), 10516-10527 (2017)
   PUBMED   28951451
  REMARK    GeneRIF: TCF4-controlled transcription in primary cortical neurons
            is induced by neuronal activity and protein kinase A.
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Chen,B. and Lim,R.W.
  TITLE     Physical and functional interactions between the transcriptional
            inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism
            regulating muscle-specific gene expression
  JOURNAL   J Biol Chem 272 (4), 2459-2463 (1997)
   PUBMED   8999959
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Pscherer,A., Dorflinger,U., Kirfel,J., Gawlas,K., Ruschoff,J.,
            Buettner,R. and Schule,R.
  TITLE     The helix-loop-helix transcription factor SEF-2 regulates the
            activity of a novel initiator element in the promoter of the human
            somatostatin receptor II gene
  JOURNAL   EMBO J 15 (23), 6680-6690 (1996)
   PUBMED   8978694
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Yoon,S.O. and Chikaraishi,D.M.
  TITLE     Isolation of two E-box binding factors that interact with the rat
            tyrosine hydroxylase enhancer
  JOURNAL   J Biol Chem 269 (28), 18453-18462 (1994)
   PUBMED   7913462
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038953086.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35215.1,
                                           SRR26643290.51896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..669
                     /product="transcription factor 4 isoform 21"
                     /note="ITF-2; SEF-2; RITF-2; SL3-3 enhancer factor 2;
                     immunoglobulin transcription factor 2; TCF-4; R8f
                     DNA-binding protein"
                     /calculated_mol_wt=71350
     Region          135..>296
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          560..644
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(568,572,574..576,578,583,604..605)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(581..582,585..586,588..589,592,596,606,609,613,616,
                     619..624)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..669
                     /gene="Tcf4"
                     /coded_by="NM_001437097.1:184..2193"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="GeneID:84382"
                     /db_xref="RGD:69271"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygrenvqgc
      121 hqqsllggdm dmgnpgtlsp tkpgsqyypy ssnnarrrpl hsstmevqtk kvrkvppglp
      181 ssvyapsast adynrdspgy ssskpaastf sssffmqdgh hssdpwssss gmnqpgyggm
      241 lgnshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgt gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsagtavw
      361 srnggqasss pnyegplhsl qsriedrler lddaihvlrn havgpstavp gghgdmhgii
      421 gpshngamgs lgsgygtgll sanrhslmvg ahredgvalr gshsllpnqv pvpqlpvqsa
      481 tspdlnppqd pyrgmppglq gqsvssgsse iksddegden lqdtkssedk kldddkkdik
      541 sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr dineafkelg rmvqlhlksd
      601 kpqtkllilh qavavilsle qqvrernlnp kaaclkrree ekvssepppl slagphpgmg
      661 daanhmgqm
//
LOCUS       NP_001423932             461 aa            linear   ROD 28-MAR-2025
DEFINITION  ribitol-5-phosphate transferase FKTN isoform a [Rattus norvegicus].
ACCESSION   NP_001423932 XP_006238231
VERSION     NP_001423932.1
DBSOURCE    REFSEQ: accession NM_001437003.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Willer,T., Inamori,K., Venzke,D., Harvey,C., Morgensen,G., Hara,Y.,
            Beltran Valero de Bernabe,D., Yu,L., Wright,K.M. and Campbell,K.P.
  TITLE     The glucuronyltransferase B4GAT1 is required for initiation of
            LARGE-mediated alpha-dystroglycan functional glycosylation
  JOURNAL   Elife 3, e03941 (2014)
   PUBMED   25279699
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fortunato,M.J., Ball,C.E., Hollinger,K., Patel,N.B., Modi,J.N.,
            Rajasekaran,V., Nonneman,D.J., Ross,J.W., Kennedy,E.J., Selsby,J.T.
            and Beedle,A.M.
  TITLE     Development of rabbit monoclonal antibodies for detection of
            alpha-dystroglycan in normal and dystrophic tissue
  JOURNAL   PLoS One 9 (5), e97567 (2014)
   PUBMED   24824861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yis,U., Uyanik,G., Heck,P.B., Smitka,M., Nobel,H., Ebinger,F.,
            Dirik,E., Feng,L., Kurul,S.H., Brocke,K., Unalp,A., Ozer,E.,
            Cakmakci,H., Sewry,C., Cirak,S., Muntoni,F., Hehr,U. and
            Morris-Rosendahl,D.J.
  TITLE     Fukutin mutations in non-Japanese patients with congenital muscular
            dystrophy: less severe mutations predominate in patients with a
            non-Walker-Warburg phenotype
  JOURNAL   Neuromuscul Disord 21 (1), 20-30 (2011)
   PUBMED   20961758
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chang,W., Winder,T.L., LeDuc,C.A., Simpson,L.L., Millar,W.S.,
            Dungan,J., Ginsberg,N., Plaga,S., Moore,S.A. and Chung,W.K.
  TITLE     Founder Fukutin mutation causes Walker-Warburg syndrome in four
            Ashkenazi Jewish families
  JOURNAL   Prenat Diagn 29 (6), 560-569 (2009)
   PUBMED   19266496
  REMARK    Erratum:[Prenat Diagn. 2012 Oct;32(10):1019]
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Puckett,R.L., Moore,S.A., Winder,T.L., Willer,T., Romansky,S.G.,
            Covault,K.K., Campbell,K.P. and Abdenur,J.E.
  TITLE     Further evidence of Fukutin mutations as a cause of childhood onset
            limb-girdle muscular dystrophy without mental retardation
  JOURNAL   Neuromuscul Disord 19 (5), 352-356 (2009)
   PUBMED   19342235
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Esapa,C.T., Benson,M.A., Schroder,J.E., Martin-Rendon,E.,
            Brockington,M., Brown,S.C., Muntoni,F., Kroger,S. and Blake,D.J.
  TITLE     Functional requirements for fukutin-related protein in the Golgi
            apparatus
  JOURNAL   Hum Mol Genet 11 (26), 3319-3331 (2002)
   PUBMED   12471058
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Hayashi,Y.K., Ogawa,M., Tagawa,K., Noguchi,S., Ishihara,T.,
            Nonaka,I. and Arahata,K.
  TITLE     Selective deficiency of alpha-dystroglycan in Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Neurology 57 (1), 115-121 (2001)
   PUBMED   11445638
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Saito,Y., Mizuguchi,M., Oka,A. and Takashima,S.
  TITLE     Fukutin protein is expressed in neurons of the normal developing
            human brain but is reduced in Fukuyama-type congenital muscular
            dystrophy brain
  JOURNAL   Ann Neurol 47 (6), 756-764 (2000)
   PUBMED   10852541
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kondo-Iida,E., Kobayashi,K., Watanabe,M., Sasaki,J., Kumagai,T.,
            Koide,H., Saito,K., Osawa,M., Nakamura,Y. and Toda,T.
  TITLE     Novel mutations and genotype-phenotype relationships in 107
            families with Fukuyama-type congenital muscular dystrophy (FCMD)
  JOURNAL   Hum Mol Genet 8 (12), 2303-2309 (1999)
   PUBMED   10545611
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kobayashi,K., Nakahori,Y., Miyake,M., Matsumura,K., Kondo-Iida,E.,
            Nomura,Y., Segawa,M., Yoshioka,M., Saito,K., Osawa,M., Hamano,K.,
            Sakakihara,Y., Nonaka,I., Nakagome,Y., Kanazawa,I., Nakamura,Y.,
            Tokunaga,K. and Toda,T.
  TITLE     An ancient retrotransposal insertion causes Fukuyama-type
            congenital muscular dystrophy
  JOURNAL   Nature 394 (6691), 388-392 (1998)
   PUBMED   9690476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006238231.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2476814.1,
                                           SRR26643295.21337.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..461
                     /product="ribitol-5-phosphate transferase FKTN isoform a"
                     /note="Fukuyama type congenital muscular dystrophy
                     homolog; Fukuyama type congenital muscular dystrophy
                     (fukutin); ribitol-5-phosphate transferase FKTN"
                     /calculated_mol_wt=53337
     Region          1..278
                     /region_name="FKTN_N"
                     /note="Fukutin N-terminal; pfam19737"
                     /db_xref="CDD:466166"
     Region          289..>327
                     /region_name="LicD"
                     /note="LicD family; cl01378"
                     /db_xref="CDD:470175"
     CDS             1..461
                     /gene="Fktn"
                     /gene_synonym="Fcmd"
                     /coded_by="NM_001437003.1:262..1647"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:362520"
                     /db_xref="RGD:1310087"
ORIGIN      
        1 msrvnknvvl alltlmscaf llfqlyyykh ylsarngtgs skskgnrvgf dstqwravkk
       61 fimltssqnv pvflidpwil esinknfeqv knasqgsase crffcvprdf tafalqyhlw
      121 knedgwfqma enmgfqclki eskdprldgi dslsgteipl hyvcklatha ihlvvfhers
      181 gnylwhghlr lkghmdrkfv pfrrlqfgry pgafdrpelq qvtvdgldml ipkdpgrfle
      241 evphsrfiec rykearaflq qyvddntvda mafrkrakel lqlaaktlka lgvpfwlssg
      301 tclgwyrqcs iipyskdvdl gifiqdykpd ivlafqdagl plkhkfgkve dslelsfqgq
      361 advkldifff yeetdhmwng gtqartgkkf kylfpkftlc wtefvdikvh vpcetvdyie
      421 anygkawkip vktwdwkssp pnvqpngvwp isewdeviql y
//
LOCUS       NP_001423992            1633 aa            linear   ROD 28-MAR-2025
DEFINITION  phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing
            subunit beta isoform 1 [Rattus norvegicus].
ACCESSION   NP_001423992 XP_006249816
VERSION     NP_001423992.1
DBSOURCE    REFSEQ: accession NM_001437063.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1633)
  AUTHORS   Kozhevnikova,O.S., Telegina,D.V., Devyatkin,V.A. and Kolosova,N.G.
  TITLE     Involvement of the autophagic pathway in the progression of
            AMD-like retinopathy in senescence-accelerated OXYS rats
  JOURNAL   Biogerontology 19 (3-4), 223-235 (2018)
   PUBMED   29492791
  REMARK    GeneRIF: Missense single-nucleotide polymorphism in the Pik3c2b
            gene associated with autophagy regulation in in the progression of
            Age-related macular degeneration was found.
REFERENCE   2  (residues 1 to 1633)
  AUTHORS   Devereaux,K., Dall'Armi,C., Alcazar-Roman,A., Ogasawara,Y.,
            Zhou,X., Wang,F., Yamamoto,A., De Camilli,P. and Di Paolo,G.
  TITLE     Regulation of mammalian autophagy by class II and III PI 3-kinases
            through PI3P synthesis
  JOURNAL   PLoS One 8 (10), e76405 (2013)
   PUBMED   24098492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1633)
  AUTHORS   Das,M., Scappini,E., Martin,N.P., Wong,K.A., Dunn,S., Chen,Y.J.,
            Miller,S.L., Domin,J. and O'Bryan,J.P.
  TITLE     Regulation of neuron survival through an
            intersectin-phosphoinositide 3'-kinase C2beta-AKT pathway
  JOURNAL   Mol Cell Biol 27 (22), 7906-7917 (2007)
   PUBMED   17875942
REFERENCE   4  (residues 1 to 1633)
  AUTHORS   Sindic,A., Crljen,V., Matkovic,K., Lukinovic-Skudar,V., Visnjic,D.
            and Banfic,H.
  TITLE     Activation of phosphoinositide 3-kinase C2 beta in the nuclear
            matrix during compensatory liver growth
  JOURNAL   Adv Enzyme Regul 46, 280-287 (2006)
   PUBMED   16857245
  REMARK    GeneRIF: Activated during compensatory liver growth, which clearly
            demonstrates that different class II PI3K enzymes have different
            subnuclear localization.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006249816.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..1633
                     /product="phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta isoform 1"
                     /EC_number="2.7.1.154"
                     /note="phosphoinositide-3-kinase, class 2, beta
                     polypeptide; nuclear cap binding protein subunit 2;
                     phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta"
                     /calculated_mol_wt=184403
     Region          363..465
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          621..793
                     /region_name="C2A_PI3K_class_II"
                     /note="C2 domain first repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd04012"
                     /db_xref="CDD:175979"
     Region          812..980
                     /region_name="PI3Ka_II"
                     /note="Phosphoinositide 3-kinase (PI3K) class II,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, class II PI3-kinases...; cd00869"
                     /db_xref="CDD:238441"
     Region          986..1339
                     /region_name="PI3Kc_C2_beta"
                     /note="Catalytic domain of Class II Phosphoinositide
                     3-kinase beta; cd00895"
                     /db_xref="CDD:119421"
     Site            order(1056,1058..1060,1062,1080,1082,1085,1116,1128..1131,
                     1136,1139,1199,1201,1211..1212)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:119421"
     Site            1191..1199
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:119421"
     Site            1212..1236
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:119421"
     Region          1368..1476
                     /region_name="PX_PI3K_C2_beta"
                     /note="The phosphoinositide binding Phox Homology Domain
                     of the Beta Isoform of Class II Phosphoinositide
                     3-Kinases; cd07290"
                     /db_xref="CDD:132823"
     Site            order(1404..1406,1430..1431,1445)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132823"
     Region          1504..1626
                     /region_name="C2B_PI3K_class_II"
                     /note="C2 domain second repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd08381"
                     /db_xref="CDD:176027"
     Site            1554..1564
                     /site_type="active"
                     /note="nuclear localization signal [active]"
                     /db_xref="CDD:176027"
     CDS             1..1633
                     /gene="Pik3c2b"
                     /coded_by="NM_001437063.1:528..5429"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289021"
                     /db_xref="RGD:1306541"
ORIGIN      
        1 msstqgngeh wkslesvgis rkelamaeal qmeydalsrl rhhkeesrak qntepslisw
       61 depaldfysk pagrrtelkl lrglsgsdpt lnynsisppe elpnstsqdp qpgtdpwpkg
      121 sqsgdylyif dgsdgrcsls pvsgdtdgsc kklsppplpp rvsiwdappl pprkgspsps
      181 kisqpddins fslveqpsdk llgaqdpgeg elpngggqrh vlgsvdydgi ndaitrlnlk
      241 stydseilsd atrgwkegrg pldfskdtsg kpvarsktmp pqvpprtytp ryanrknatp
      301 gknrrisaap vssrthtvtn ghelfevsee rdeevaafch mldilrtgsd tqdysltgcv
      361 wstvtpspeh lgdevnlkvt vlcdslrepl tftcncsstv dlliyqtlcy thdelrevdv
      421 gdfvlkpcgl eeflqnkhal gsheyiqhcr kfdinirlql meqkairsdl artvnddqsp
      481 stlnylihlq erpvkqtisr qalsllfdty hnevdaflla egdfplkadr vvqsvkaicn
      541 alaavetpei tsalnqlppc psrmqpkiqk dpsvltvren rekvvealta aildlvelyc
      601 stfnadfqta vpgsrkhdlv qeachfsgal aftvygthri piiwatsyee fylscslshg
      661 gkelcsplqt rrahfskylf hliiwdqqic fpvqvnrlpr etllcatlya lpipppgsss
      721 eankqkrvpe algwvttplf nfrqvltcgr kllglwpatq enssarwsap nfhqpdsvil
      781 qidfptsafd ikftsppgdk fspryefgsl reedqrklkd itqkeslywl sdadkkqlwe
      841 kryychtevs slplvlasap swewaclpdi yallqqwthm nhqdalgllh atfpdqevrr
      901 mavqwigsls daelldylpq lvqalkyecy ldsplvrfll kraisdlrvt hyffwllkds
      961 lkdsqfsiry qyllaallcc cgkglreefn rqcwlvntla klaqqvreat psarqgilra
     1021 gleevrqffa lngscrlpls psllvkgivp rdcsyfnsna vplklafqnv dplgenirvi
     1081 fkcgddlrqd mltlqmirim skiwvqegld mrmvifrcfs tgrgkgmvem ipnaetlrki
     1141 qvehgvtgsf kdrpladwlq khnpgedeye kavenfiysc agccvatyil gicdrhndni
     1201 mlkttghmfh idfgrflgha qmfgnikrdr apfvftsdma yvinggdkps srfhdfvdlc
     1261 cqaynlirkh thlflnllgl mlscgipels dledlkyvyd alrpqdtean attyftrlie
     1321 sslgsvatkl nffihnlaqm kftgsddrlt lsfaprthtl kssgrirdvf lcrhekvfhp
     1381 skgyiyvvkv mrenaheaty iqrtfeefqe lhnklrllfp ssflpsfpsr fvigrsrgea
     1441 vaerrkeeln gyiwhlihaa pevaecdlvy tffhplprde ktsgpspapk ssdgtwarpv
     1501 gkvggevkls isyknnklfi mvmhirglqp lqdgsdpdpy vkiyllpdpq katkrktkva
     1561 rktcnptyne mlvydgipkg dlqqrelqls vlseqgfwen vllgevhirl reldlaqekt
     1621 gwfalgsrgh gtl
//
LOCUS       NP_001423975             332 aa            linear   ROD 28-MAR-2025
DEFINITION  mitochondrial inner membrane protein COX18 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423975 XP_006250833
VERSION     NP_001423975.1
DBSOURCE    REFSEQ: accession NM_001437046.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Bourens,M. and Barrientos,A.
  TITLE     Human mitochondrial cytochrome c oxidase assembly factor COX18 acts
            transiently as a membrane insertase within the subunit 2 maturation
            module
  JOURNAL   J Biol Chem 292 (19), 7774-7783 (2017)
   PUBMED   28330871
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Gaisne,M. and Bonnefoy,N.
  TITLE     The COX18 gene, involved in mitochondrial biogenesis, is
            functionally conserved and tightly regulated in humans and fission
            yeast
  JOURNAL   FEMS Yeast Res 6 (6), 869-882 (2006)
   PUBMED   16911509
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Sacconi,S., Trevisson,E., Pistollato,F., Baldoin,M.C.,
            Rezzonico,R., Bourget,I., Desnuelle,C., Tenconi,R., Basso,G.,
            DiMauro,S. and Salviati,L.
  TITLE     hCOX18 and hCOX19: two human genes involved in cytochrome c oxidase
            assembly
  JOURNAL   Biochem Biophys Res Commun 337 (3), 832-839 (2005)
   PUBMED   16212937
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006250833.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.83180.1,
                                           SRR26643297.43059.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..332
                     /product="mitochondrial inner membrane protein COX18
                     isoform 2"
                     /note="mitochondrial inner membrane protein COX18; COX18
                     cytochrome c oxidase assembly homolog; cytochrome c
                     oxidase assembly homolog 18; cytochrome c oxidase assembly
                     protein 18; COX18, cytochrome c oxidase assembly factor"
                     /calculated_mol_wt=36259
     Region          76..297
                     /region_name="5TM_Oxa1-like"
                     /note="Five transmembrane core domain of mitochondrial
                     inner membrane protein Oxa1 and similar proteins; cd20069"
                     /db_xref="CDD:410993"
     CDS             1..332
                     /gene="Cox18"
                     /gene_synonym="RGD1559547"
                     /coded_by="NM_001437046.1:68..1066"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289522"
                     /db_xref="RGD:1559547"
ORIGIN      
        1 mlcgscagll rslrtlqlra pgslpawssa rlptlpvwaa asvsaaspgg wyealaasap
       61 vhaaeemlls aqettglpww gnillstvvl rgavtlplaa yqhyilakve nlqpeikdia
      121 krlnqevavc arqfgwskrv arltylknir rlvselyvrd nchpfkatvl vwvqlpmwvf
      181 isvalrnlst gathsdagis vqdqlaaggt lwfpdltavd stwilpvsvg vvnlliveif
      241 alqkigksrf qmyvtnfvra vsvlmvpvaa tvpsalvlyw lcsslmglsq nlllrspgfr
      301 qlcrippsrs dsetpyrdls aafcakflsr kr
//
LOCUS       NP_001423912             306 aa            linear   ROD 28-MAR-2025
DEFINITION  DCN1-like protein 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001423912 XP_017454777
VERSION     NP_001423912.1
DBSOURCE    REFSEQ: accession NM_001436983.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_017454777.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1990344.1,
                                           SRR26360181.458866.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..306
                     /product="DCN1-like protein 4 isoform 2"
                     /note="DCN1-like protein 4; DCN1, defective in cullin
                     neddylation 1, domain containing 4"
                     /calculated_mol_wt=35735
     Region          189..299
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     CDS             1..306
                     /gene="Dcun1d4"
                     /gene_synonym="RGD1310422"
                     /coded_by="NM_001436983.1:64..984"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360928"
                     /db_xref="RGD:1310422"
ORIGIN      
        1 meftqehqac hpqgseemkh wkdfqlnshl stlanihkiy htlnklnlte dvgqddhqtg
       61 slrscsssdc fskvmpprkk rrpasgddls akksrhdsmy rkyestrikt eeeafsskrc
      121 lewfyeyagt edavgpegme kfcedigvep envvmlvlaw kldaqnmgyf tlqewlkgmt
      181 slqcdttekl rttldylrsl lndttnfkli yryafdfare kdqrsldint akcmlglllg
      241 kiwplfpvfh qfleqskykv inkdqwcnvl efsrtisldl snydedgawp vlldefvewy
      301 kdkqms
//
LOCUS       NP_064699                709 aa            linear   ROD 28-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_064699 XP_344539
VERSION     NP_064699.1
DBSOURCE    REFSEQ: accession NM_020303.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2005 this sequence version replaced XP_344539.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091169.1, SRR26643293.75524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..709
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 3"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=79777
     Region          <20..98
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     mat_peptide     99..709
                     /product="Disintegrin and metalloproteinase
                     domain-containing protein 5. /id=PRO_0000349303"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK84.1)"
                     /calculated_mol_wt=69071
     Region          141..334
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          355..429
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          433..576
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            650..670
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK84.1)"
     Region          690..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK84.1)"
     CDS             1..709
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_020303.2:223..2352"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 mktpissilk snglgiflyr sfitstavsy tydrqdvrhs qslsslkncn yngyvagfpn
       61 sivsltvcsg lrgmiqfenv sygiepvetl sgfihviyen tnqqakipdl genqtyswsd
      121 eldyqfrsnm kksgfavlrp ryiktdivvd kklfdymgsd trvvlqkviq iigfintmfs
      181 klkltvlins veiwskenri dfpeapenll vqflhwkhky rpqhisylla fvehpastga
      241 lypgnlckpi ygaaialypk glslesysvi vlqllsigig ltydnadsch ctgdvclmtp
      301 kaiysggvkd fstcslddfk ylstqdlecl qdlpmerqkk kpsrprricg ngilemneqc
      361 dcgtlkncth kkccdpmscr lkskavcgsg eccgqdckvk pvnvlcrksk necdfeeycn
      421 gndaycvpdt farngqycds gqafcysglc mtsnnqcmnl lgkyvrgasf acyeefnsrn
      481 drfgncirkf csfenslcgk lvctwpfkrl lmkdnmsaay gqirddlcis lykggrplkt
      541 tlstysdmse rdetfvkdgt icgpdmfcle tqcketrflv dfqqcntsrd cndhgvcnnf
      601 nhchcdkgyn ppycesvkgq fgsiddghky yidegksakq qnrgihpkqq lqlilyitlp
      661 limiisavfi kqsklsrlcg rersegtsci tedsvsntkm ttnegstlh
//
LOCUS       NP_001423969            1018 aa            linear   ROD 28-MAR-2025
DEFINITION  unconventional myosin-Ig [Rattus norvegicus].
ACCESSION   NP_001423969 XP_006251280
VERSION     NP_001423969.1
DBSOURCE    REFSEQ: accession NM_001437040.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Gerard,A., Patino-Lopez,G., Beemiller,P., Nambiar,R., Ben-Aissa,K.,
            Liu,Y., Totah,F.J., Tyska,M.J., Shaw,S. and Krummel,M.F.
  TITLE     Detection of rare antigen-presenting cells through T cell-intrinsic
            meandering motility, mediated by Myo1g
  JOURNAL   Cell 158 (3), 492-505 (2014)
   PUBMED   25083865
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Maravillas-Montero,J.L., Lopez-Ortega,O., Patino-Lopez,G. and
            Santos-Argumedo,L.
  TITLE     Myosin 1g regulates cytoskeleton plasticity, cell migration,
            exocytosis, and endocytosis in B lymphocytes
  JOURNAL   Eur J Immunol 44 (3), 877-886 (2014)
   PUBMED   24310084
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Dart,A.E., Tollis,S., Bright,M.D., Frankel,G. and Endres,R.G.
  TITLE     The motor protein myosin 1G functions in FcgammaR-mediated
            phagocytosis
  JOURNAL   J Cell Sci 125 (Pt 24), 6020-6029 (2012)
   PUBMED   23038771
REFERENCE   4  (residues 1 to 1018)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 1018)
  AUTHORS   Olety,B., Walte,M., Honnert,U., Schillers,H. and Bahler,M.
  TITLE     Myosin 1G (Myo1G) is a haematopoietic specific myosin that
            localises to the plasma membrane and regulates cell elasticity
  JOURNAL   FEBS Lett 584 (3), 493-499 (2010)
   PUBMED   19968988
REFERENCE   6  (residues 1 to 1018)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006251280.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.52685.1,
                                           SRR26643290.45097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1018
                     /product="unconventional myosin-Ig"
                     /note="myosin-Ig"
                     /calculated_mol_wt=116568
     Region          23..694
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(50..53,58,102..109,151..161,395..400)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(50..53,58)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            102..109
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            151..161
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            395..400
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(424..435,438..445,447)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Site            626..636
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(638..664,681..694)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          815..986
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1018
                     /gene="Myo1g"
                     /coded_by="NM_001437040.1:108..3164"
                     /db_xref="GeneID:289785"
                     /db_xref="RGD:1306016"
ORIGIN      
        1 medeegpeyg kpdfvlldql tmeefmknlq lrfekgriyt yigevlvsvn pyqelplygp
       61 eaiakyqgre lyerpphlya vanaaykamk rrsrdtcivi sgesgagkte askhimqyia
      121 avtnpsqrae vervkdvllk stcvleafgn artnrnhnss rfgkymdinf dfkgdpvggh
      181 ihsylleksr vlkqhvgern fhafyqllrg sedqelqelh lernpavynf trqgaglnmg
      241 vhnalgsdek shqgvmeamk iigfspeeve sihrilaail hlgniefvet eengpqkggl
      301 evadealvgy vakltatpsd lvlrtllart vasggrevie kshtvaeasy ardacakamy
      361 qrlfewvvnk insimeprdr dprrdgkdtv igvldiygfe vfpvnsfeqf cinycneklq
      421 qlfiqlilkq eqeeyeregi twqsieyfnn ativelveqp rrgilavlde acstagpitd
      481 riflqtldth hrhhphyssr qlcptdktme fgrdfqikhy agdvtysveg fidknrdslf
      541 qdfkrllyns mdptlramwp dgqqditevt krpltagtlf knsmialven laskepfyvr
      601 cikpnedkvp grldeahcrh qveylgllen vrvrragfas rqpyprfllr ykmtceytwp
      661 nhllgsdrea vsalleqhgl qgdvafghsk lfirsprtlv tleqsrahli piivlllqka
      721 wrgtlarwrc rrlraiytim gwfrrhkvra hlielqrrfq aarqpplygr dlvwptppav
      781 lqpfqdtchi lfsrwrarql vknippsdmt qikakvaamg alqglrqdwg cqrawardyl
      841 ssdtdnptas hlfaeqlkal rekdgfgtvl fsshvrkvnr frkrrdrall ltdrhlykle
      901 pgrqyrvmra vpldavtgls vtsgrdqlvv lhaqghddlv vclhrsqppl dnrigelvgm
      961 lvshcqgegr tleirvsdci plsqrgarrl isveprpeqt epdfqcsrst ftllwpsh
//
LOCUS       NP_001423970             527 aa            linear   ROD 28-MAR-2025
DEFINITION  F-box-like/WD repeat-containing protein TBL1X [Rattus norvegicus].
ACCESSION   NP_001423970 XP_038955593
VERSION     NP_001423970.1
DBSOURCE    REFSEQ: accession NM_001437041.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Huang,J., Cardamone,M.D., Johnson,H.E., Neault,M., Chan,M.,
            Floyd,Z.E., Mallette,F.A. and Perissi,V.
  TITLE     Exchange Factor TBL1 and Arginine Methyltransferase PRMT6 Cooperate
            in Protecting G Protein Pathway Suppressor 2 (GPS2) from
            Proteasomal Degradation
  JOURNAL   J Biol Chem 290 (31), 19044-19054 (2015)
   PUBMED   26070566
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Oberoi,J., Fairall,L., Watson,P.J., Yang,J.C., Czimmerer,Z.,
            Kampmann,T., Goult,B.T., Greenwood,J.A., Gooch,J.T.,
            Kallenberger,B.C., Nagy,L., Neuhaus,D. and Schwabe,J.W.
  TITLE     Structural basis for the assembly of the SMRT/NCoR core
            transcriptional repression machinery
  JOURNAL   Nat Struct Mol Biol 18 (2), 177-184 (2011)
   PUBMED   21240272
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Perissi,V., Scafoglio,C., Zhang,J., Ohgi,K.A., Rose,D.W.,
            Glass,C.K. and Rosenfeld,M.G.
  TITLE     TBL1 and TBLR1 phosphorylation on regulated gene promoters
            overcomes dual CtBP and NCoR/SMRT transcriptional repression
            checkpoints
  JOURNAL   Mol Cell 29 (6), 755-766 (2008)
   PUBMED   18374649
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Ishii,S., Kurasawa,Y., Wong,J. and Yu-Lee,L.Y.
  TITLE     Histone deacetylase 3 localizes to the mitotic spindle and is
            required for kinetochore-microtubule attachment
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4179-4184 (2008)
   PUBMED   18326024
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Li,J. and Wang,C.Y.
  TITLE     TBL1-TBLR1 and beta-catenin recruit each other to Wnt target-gene
            promoter for transcription activation and oncogenesis
  JOURNAL   Nat Cell Biol 10 (2), 160-169 (2008)
   PUBMED   18193033
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Yoon,H.G., Choi,Y., Cole,P.A. and Wong,J.
  TITLE     Reading and function of a histone code involved in targeting
            corepressor complexes for repression
  JOURNAL   Mol Cell Biol 25 (1), 324-335 (2005)
   PUBMED   15601853
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Perissi,V., Aggarwal,A., Glass,C.K., Rose,D.W. and Rosenfeld,M.G.
  TITLE     A corepressor/coactivator exchange complex required for
            transcriptional activation by nuclear receptors and other regulated
            transcription factors
  JOURNAL   Cell 116 (4), 511-526 (2004)
   PUBMED   14980219
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Yoon,H.G., Chan,D.W., Huang,Z.Q., Li,J., Fondell,J.D., Qin,J. and
            Wong,J.
  TITLE     Purification and functional characterization of the human N-CoR
            complex: the roles of HDAC3, TBL1 and TBLR1
  JOURNAL   EMBO J 22 (6), 1336-1346 (2003)
   PUBMED   12628926
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Guenther,M.G., Lane,W.S., Fischle,W., Verdin,E., Lazar,M.A. and
            Shiekhattar,R.
  TITLE     A core SMRT corepressor complex containing HDAC3 and TBL1, a
            WD40-repeat protein linked to deafness
  JOURNAL   Genes Dev 14 (9), 1048-1057 (2000)
   PUBMED   10809664
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Bassi,M.T., Ramesar,R.S., Caciotti,B., Winship,I.M., De Grandi,A.,
            Riboni,M., Townes,P.L., Beighton,P., Ballabio,A. and Borsani,G.
  TITLE     X-linked late-onset sensorineural deafness caused by a deletion
            involving OA1 and a novel gene containing WD-40 repeats
  JOURNAL   Am J Hum Genet 64 (6), 1604-1616 (1999)
   PUBMED   10330347
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Mar 26, 2025 this sequence version replaced XP_038955593.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.44825.1,
                                           SRR26360186.282753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..527
                     /product="F-box-like/WD repeat-containing protein TBL1X"
                     /calculated_mol_wt=56671
     Region          7..31
                     /region_name="LisH"
                     /note="pfam08513"
                     /db_xref="CDD:462501"
     Region          177..483
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(181,199,203,209..210,232..233,255,259,265,277..278,
                     295,300,306..307,320,336,341,347..348,360..361,379,383,
                     389..390,402..403,429,434,440..441,453..454,472,476,
                     482..483)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          185..232
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          242..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          282..318
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          325..359
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          365..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          407..452
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <457..527
                     /region_name="8prop_heme_binding_protein"
                     /note="eight-bladed beta-propeller heme-binding domain in
                     cytochrome cd1 and similar proteins; cl49617"
                     /db_xref="CDD:483957"
     Region          458..482
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          460..494
                     /region_name="propeller blade"
                     /note="propeller blade [structural motif]"
                     /db_xref="CDD:467722"
     Region          499..525
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..527
                     /gene="Tbl1x"
                     /gene_synonym="RGD1563868"
                     /coded_by="NM_001437041.1:417..2000"
                     /db_xref="GeneID:302711"
                     /db_xref="RGD:1563868"
ORIGIN      
        1 msitsdevnf lvyrylqesg fshsaftfgi eshisqsnin gtlvppaali silqkglqyv
       61 eaeisinedg tvfdgrpies lslidavmpd vvqtrqqafr eklaqqqana aaaaaaaaat
      121 atstaattpa aaaqqnppkn geatvngeen gahainnhsk pmeidgdvei ppskatvlrg
      181 hesevficaw npvsdllasg sgdstariwn lnensnggst qlvlrhcire gghdvpsnkd
      241 vtsldwnsdg tllatgsydg fariwtedgn lastlgqhkg pifalkwnkk gnyilsagvd
      301 kttiiwdaht geakqqfpfh sapaldvdwq nnttfascst dmcihvcrlg cdrpvktfqg
      361 htnevnaikw dpsgmllasc sddmtlkiws mkqdacvhdl qahskeiyti kwsptgpats
      421 npnsnimlas asfdstvrlw dvergvciht ltkhqepvys vafspdgkyl asgsfdkcvh
      481 iwntqsgslv hsyrgtggif evcwnargdk vgasasdgsv cvldlrk
//
LOCUS       NP_001094359            1986 aa            linear   ROD 28-MAR-2025
DEFINITION  protein Shroom3 [Rattus norvegicus].
ACCESSION   NP_001094359 XP_001070669 XP_223229
VERSION     NP_001094359.1
DBSOURCE    REFSEQ: accession NM_001100889.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1986)
  AUTHORS   Yeo,N.C., O'Meara,C.C., Bonomo,J.A., Veth,K.N., Tomar,R.,
            Flister,M.J., Drummond,I.A., Bowden,D.W., Freedman,B.I., Lazar,J.,
            Link,B.A. and Jacob,H.J.
  TITLE     Shroom3 contributes to the maintenance of the glomerular filtration
            barrier integrity
  JOURNAL   Genome Res 25 (1), 57-65 (2015)
   PUBMED   25273069
  REMARK    GeneRIF: variants disrupting the actin-binding domain of SHROOM3
            may cause podocyte effacement and impairment of the glomerular
            filtration barrier
REFERENCE   2  (residues 1 to 1986)
  AUTHORS   Hildebrand,J.D.
  TITLE     Shroom regulates epithelial cell shape via the apical positioning
            of an actomyosin network
  JOURNAL   J Cell Sci 118 (Pt 22), 5191-5203 (2005)
   PUBMED   16249236
REFERENCE   3  (residues 1 to 1986)
  AUTHORS   Klezovitch,O., Fernandez,T.E., Tapscott,S.J. and Vasioukhin,V.
  TITLE     Loss of cell polarity causes severe brain dysplasia in Lgl1
            knockout mice
  JOURNAL   Genes Dev 18 (5), 559-571 (2004)
   PUBMED   15037549
REFERENCE   4  (residues 1 to 1986)
  AUTHORS   Hildebrand,J.D. and Soriano,P.
  TITLE     Shroom, a PDZ domain-containing actin-binding protein, is required
            for neural tube morphogenesis in mice
  JOURNAL   Cell 99 (5), 485-497 (1999)
   PUBMED   10589677
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Dec 20, 2009 this sequence version replaced
            XP_223229.4, XP_001070669.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. The extent of this transcript is supported
            by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760400
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1986
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..1986
                     /product="protein Shroom3"
                     /calculated_mol_wt=215955
     Region          26..107
                     /region_name="PDZ_shroom2_3_4-like"
                     /note="PDZ domain of shroom2, shroom3, shroom4, and
                     related domains; cd06750"
                     /db_xref="CDD:467232"
     Site            order(36..42,54,57,87,91,94..95)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467232"
     Region          <746..1005
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          891..1074
                     /region_name="ASD1"
                     /note="Apx/Shroom domain ASD1; pfam08688"
                     /db_xref="CDD:462562"
     Region          1661..1946
                     /region_name="ASD2"
                     /note="Apx/Shroom domain ASD2; pfam08687"
                     /db_xref="CDD:462561"
     CDS             1..1986
                     /gene="Shroom3"
                     /gene_synonym="RGD1310470; Shrm"
                     /coded_by="NM_001100889.1:1..5961"
                     /db_xref="GeneID:305230"
                     /db_xref="RGD:1310470"
ORIGIN      
        1 mrtpenleep satpnssrtp keryvyleal leggapwgft lkgglehgep liiskieegg
       61 kadsvssglq tgdevihine vvlsssrrea vslvkgsykt lrlvvrrdvc aapghadpgt
      121 snsissellt cspqhrkatw sggvklrlkq rcsepaarph swhttkfget qadvsmmris
      181 qgtvgppwhq schsssstsd lsnydhaylr rspdrcssqg smeslgprgg sppchllspa
      241 kstssidqlg hlhnkrdsay ssfstsssif eypppggsar ersgsldmip arggllegmr
      301 qadiryvktv ydtrrgvsse yevnpsalll qgrdahtsad sqgcakwhsi prgkgtpplp
      361 wsqqcsgspe tadnpphkag apmpptrsds yvalrhrerp sswssldqkr fcrpqtnslg
      421 sqktpfveeq lhtvperspe nsppvkpkhn ytqktqpgqp llptgiypvp spephfaqvp
      481 qpsvsgngtv ypalvkesgy taaqgtcskm aaldengnqk evsrpgfafc qppehdsmtp
      541 vekkpeprak yipykvhfss vpenedsslk rhvtpphgns lypserknvh gggsrpcsnh
      601 hslpsaqaqa phagdddrrp srlfqpwegd fqedhnanlr qkveregqgq glpgnsggtk
      661 stfsplqnip enlrrqssvd lgeglevypg grstcatttt kvedpgrkag pdnrgyldrs
      721 vsyprpegkm naaesfhsad sryeeplaap pqqtsgmsqr rlsasstpal qykkphcsvl
      781 ekvskieere qgrhrptsvg ssayalsyrp grtgptpsts ssdlddpkas sshfsesaae
      841 hlrngeqnpp ngepkleeas rqqcnqllrr ttadgrgppa rgsepsrpea rllrsqstfq
      901 lfseaereas wsedrpstpe splldapfsr ayrnsikdaq srvlgatsfr rrdlepgtpa
      961 tsrpwrprpa sahvgmrspe asaplsspht prerhsvtpa tgtppapqaa rrgarrrlta
     1021 eqkkrsysep ekmnevgvse eaesvhcvpq rpaqlrfses tvadrrrlfe rdgkacstls
     1081 lsgpelkqfq qsaladyiqr ktgkrptgaa ctpepglrer aqsvyfqavp aapegpglas
     1141 acslsslrep evlpckehph qsaadgpqtp rdrsssfasg rlvgerrrwd pqaprqllsg
     1201 ancgprgvqr mdrtsrgpps wdmvvgksgk sksaedller sdtltvpvhv rsrssptsdk
     1261 kgqdvllred sgfgfvkdpy lagpgsrpls ysdrgqkeqa lplhhpatcw ngsgykatvv
     1321 sstessgapd hlkqlrapcp rplsagmhgh fpdarassva plssplpspv psgyrsqldm
     1381 dqqmghqplp spasavtqpp sprsheleeg mwkraslpqr pprpwkwaha vredglaeda
     1441 ssapefatlk hyknqlslps scstsdpdtp grislrises alqasppprg dyddevfvkd
     1501 lhpkvpsspt fealpppppp psplsqeplt cgsddfpspp pqamceapld gevseepgsg
     1561 scglprvtat regqvpgagh aegsqimvai ppqtsaegsa aesstaarvs aqpplhsfpg
     1621 kqpcpsqarn ltyepadrtq dlgkkihaep qktsedirte alakeivhqd ksladildpd
     1681 srmkttmdlm eglfprdagv lkenaerrav dsttrragwe vetsdhkeaa gvlvncpayy
     1741 svsaakaell nkikdmpeel reeeeqedvn ekkaeligsl thkletlqea kgslltdirl
     1801 nnalgeevea liselckpne fdkykmfigd ldkvvnllls lsgrlarven vlsglgedas
     1861 keersslnek rkvlagqhed arelkenldr rervvldila nylsaeqlqd yqhfvkmkst
     1921 llieqrkldd kiklgqeqvr clleslpsdf rpkagaislp palashvtpg ggpafggvfp
     1981 tltspl
//
LOCUS       NP_001423964             117 aa            linear   ROD 28-MAR-2025
DEFINITION  uncharacterized protein C4orf36 homolog [Rattus norvegicus].
ACCESSION   NP_001423964 XP_017454816
VERSION     NP_001423964.1
DBSOURCE    REFSEQ: accession NM_001437035.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 26, 2025 this sequence version replaced XP_017454816.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3348945.1,
                                           SRR26360181.1086271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..117
                     /product="uncharacterized protein C4orf36 homolog"
                     /note="AFF1 antisense RNA 1"
                     /calculated_mol_wt=13199
     Region          1..117
                     /region_name="DUF4522"
                     /note="Protein of unknown function (DUF4522); pfam15022"
                     /db_xref="CDD:434399"
     CDS             1..117
                     /gene="C14h4orf36"
                     /gene_synonym="Aff1-as1"
                     /coded_by="NM_001437035.1:204..557"
                     /db_xref="GeneID:498330"
                     /db_xref="RGD:1564576"
ORIGIN      
        1 mayglprrnt vqnilkgscy kiqepwdlae ltktwysnlt ninlpflgei afgspmnlla
       61 gqtkqdcplp smqtmaleke yeakrlaklk skenackemq vslreksvgl rrplqpk
//
LOCUS       NP_001423892             493 aa            linear   ROD 28-MAR-2025
DEFINITION  thiosulfate sulfurtransferase/rhodanese-like domain-containing
            protein 2 isoform a [Rattus norvegicus].
ACCESSION   NP_001423892 XP_006238150
VERSION     NP_001423892.1
DBSOURCE    REFSEQ: accession NM_001436963.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006238150.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.22689.1,
                                           SRR26643294.21079.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840111 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..493
                     /product="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2 isoform a"
                     /note="thiosulfate sulfurtransferase/rhodanese-like
                     domain-containing protein 2; thiosulfate sulfurtransferase
                     (rhodanese)-like domain containing 2"
                     /calculated_mol_wt=55342
     Region          169..459
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            354
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238776"
     CDS             1..493
                     /gene="Tstd2"
                     /gene_synonym="RGD1310893"
                     /coded_by="NM_001436963.1:110..1591"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:362514"
                     /db_xref="RGD:1310893"
ORIGIN      
        1 mpsptsadee dgletcvlkt fdldlkesni vtpsnslkae ldgstkkkys fakkkafalf
       61 vktkqvpvps yevkerrwrc cqqlfaeqts ihrhvatqha edvyqqtasi lkqltaalrt
      121 pqsltptdrr sspkdclpps qdvsawlpdv shvspqelrs gqgneegevl lyycycdled
      181 pdwvcawqaa lcrhlhltgk iriateging tvggskvatr lymevmlscp lfkdylsedd
      241 fksskggshc fpelrvgvfe eivpmgisps evsyknpgih lspgefhkei ekllsqanqe
      301 qgdtllldcr nfyeskigrf qgclapdirk fsyfpsyvdk nldifrqkrv lmyctggirc
      361 ergsaylrak gvckevfqlk ggihkyleef pdgffkgklf vfderfalay nsavvsecsy
      421 cgapwdqykl cstpqcrqlv ltcsacqgqg ftaccvmcqd kggkqasdpt qdsfkeecec
      481 tarrpripqe qra
//
LOCUS       NP_001099550             627 aa            linear   ROD 28-MAR-2025
DEFINITION  transketolase-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001099550 XP_001073142 XP_224769
VERSION     NP_001099550.1
DBSOURCE    REFSEQ: accession NM_001106080.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_224769.1, XP_001073142.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26360181.146874.1,
                                        SRR26360181.2908926.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..627
                     /product="transketolase-like protein 2"
                     /EC_number="2.2.1.1"
                     /calculated_mol_wt=68233
     Region          17..623
                     /region_name="PRK05899"
                     /note="transketolase; Reviewed"
                     /db_xref="CDD:235639"
     CDS             1..627
                     /gene="Tktl2"
                     /gene_synonym="RGD1304767"
                     /coded_by="NM_001106080.2:30..1913"
                     /db_xref="GeneID:290685"
                     /db_xref="RGD:1304767"
ORIGIN      
        1 malardakle sdifqalqdv anrlrihsir atcasssghp tsccsaaeim avlffhtmry
       61 kqadpehpdn drfvlskgha apilyavwve vgricesdll nlrkihcdle ghptprlsfv
      121 dvatgslgqg lgaacgmayt gkyfdkasyr vfclmgdges segsvweala fashykldnl
      181 laifdvnrlg qsgtaplehc tdiyetrcqa fgwntyvvdg hdvealcqaf wkaaqvknkp
      241 taliaktfkg rgipnvedae nwhgkpmpkd rvdgivklie sqiqtnrnlt pkppvedspr
      301 isisntkmts lpayklgdmi atreaygval aklghsnqrv ivldgdtkns tfsevfkkeh
      361 perfiecfia eqnmvsvalg catrgrtiaf vstfaafltr afdqirmgai sqtnvnfvgs
      421 hcgvsigedg psqmaledla mfrsipncti fypsdavste haiylaantk gmcfirttrp
      481 klaviytsee nfvigqakvi rhsaddkvtv vgagvtlhea leaadelsqq gisirvidpf
      541 tikpldasti iqsakatggq iitvedhyre ggigeavcaa isrepdivvh qlavtevprs
      601 gkpselldmf gisarhiiaa vkdtvmk
//
LOCUS       NP_001423668             423 aa            linear   ROD 28-MAR-2025
DEFINITION  transcription factor SOX-17 [Rattus norvegicus].
ACCESSION   NP_001423668 XP_038965679
VERSION     NP_001423668.1
DBSOURCE    REFSEQ: accession NM_001436739.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Walters,R., Vasilaki,E., Aman,J., Chen,C.N., Wu,Y., Liang,O.D.,
            Ashek,A., Dubois,O., Zhao,L., Sabrin,F., Cebola,I., Ferrer,J.,
            Morrell,N.W., Klinger,J.R., Wilkins,M.R., Zhao,L. and Rhodes,C.J.
  TITLE     SOX17 Enhancer Variants Disrupt Transcription Factor Binding And
            Enhancer Inactivity Drives Pulmonary Hypertension
  JOURNAL   Circulation 147 (21), 1606-1621 (2023)
   PUBMED   37066790
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zou,X., Liu,T., Huang,Z., Zhou,W., Yuan,M., Zhao,H., Pan,Z.,
            Chen,P., Shao,Y., Hu,X., Zhang,S., Zheng,S., Zhang,Y. and Huang,P.
  TITLE     SOX17 is a Critical Factor in Maintaining Endothelial Function in
            Pulmonary Hypertension by an Exosome-Mediated Autocrine Manner
  JOURNAL   Adv Sci (Weinh) 10 (14), e2206139 (2023)
   PUBMED   36919784
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Sangam,S., Sun,X., Schwantes-An,T.H., Yegambaram,M., Lu,Q., Shi,Y.,
            Cook,T., Fisher,A., Frump,A.L., Coleman,A., Sun,Y., Liang,S.,
            Crawford,H., Lutz,K.A., Maun,A.D., Pauciulo,M.W., Karnes,J.H.,
            Chaudhary,K.R., Stewart,D.J., Langlais,P.R., Jain,M., Alotaibi,M.,
            Lahm,T., Jin,Y., Gu,H., Tang,H., Nichols,W.C., Black,S.M. and
            Desai,A.A.
  TITLE     SOX17 Deficiency Mediates Pulmonary Hypertension: At the Crossroads
            of Sex, Metabolism, and Genetics
  JOURNAL   Am J Respir Crit Care Med 207 (8), 1055-1069 (2023)
   PUBMED   36913491
  REMARK    GeneRIF: SOX17 Deficiency Mediates Pulmonary Hypertension: At the
            Crossroads of Sex, Metabolism, and Genetics.
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Wan,Q., Liu,H., Xu,Y., Zhang,Q. and Tao,L.
  TITLE     Upregulated miR-194-5p suppresses retinal microvascular endothelial
            cell dysfunction and mitigates the symptoms of hypertensive
            retinopathy in mice by targeting SOX17 and VEGF signaling
  JOURNAL   Cell Cycle 22 (3), 331-346 (2023)
   PUBMED   36200131
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Park,C.S., Kim,S.H., Yang,H.Y., Kim,J.H., Schermuly,R.T., Cho,Y.S.,
            Kang,H., Park,J.H., Lee,E., Park,H., Yang,J.M., Noh,T.W., Lee,S.P.,
            Bae,S.S., Han,J., Ju,Y.S., Park,J.B. and Kim,I.
  TITLE     Sox17 Deficiency Promotes Pulmonary Arterial Hypertension via
            HGF/c-Met Signaling
  JOURNAL   Circ Res 131 (10), 792-806 (2022)
   PUBMED   36205124
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Park,K.S., Wells,J.M., Zorn,A.M., Wert,S.E. and Whitsett,J.A.
  TITLE     Sox17 influences the differentiation of respiratory epithelial
            cells
  JOURNAL   Dev Biol 294 (1), 192-202 (2006)
   PUBMED   16574095
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Niimi,T., Hayashi,Y., Futaki,S. and Sekiguchi,K.
  TITLE     SOX7 and SOX17 regulate the parietal endoderm-specific enhancer
            activity of mouse laminin alpha1 gene
  JOURNAL   J Biol Chem 279 (36), 38055-38061 (2004)
   PUBMED   15220343
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Murakami,A., Shen,H., Ishida,S. and Dickson,C.
  TITLE     SOX7 and GATA-4 are competitive activators of Fgf-3 transcription
  JOURNAL   J Biol Chem 279 (27), 28564-28573 (2004)
   PUBMED   15082719
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Kanai-Azuma,M., Kanai,Y., Gad,J.M., Tajima,Y., Taya,C.,
            Kurohmaru,M., Sanai,Y., Yonekawa,H., Yazaki,K., Tam,P.P. and
            Hayashi,Y.
  TITLE     Depletion of definitive gut endoderm in Sox17-null mutant mice
  JOURNAL   Development 129 (10), 2367-2379 (2002)
   PUBMED   11973269
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Kanai,Y., Kanai-Azuma,M., Noce,T., Saido,T.C., Shiroishi,T.,
            Hayashi,Y. and Yazaki,K.
  TITLE     Identification of two Sox17 messenger RNA isoforms, with and
            without the high mobility group box region, and their differential
            expression in mouse spermatogenesis
  JOURNAL   J Cell Biol 133 (3), 667-681 (1996)
   PUBMED   8636240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 20, 2025 this sequence version replaced XP_038965679.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.18615.1,
                                           SRR26643299.21868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..423
                     /product="transcription factor SOX-17"
                     /note="SRY-box containing gene 17; SRY (sex determining
                     region Y)-box 17; SRY box 17"
                     /calculated_mol_wt=44908
     Region          62..142
                     /region_name="HMG-box_SoxF_SOX17"
                     /note="high mobility group (HMG)-box found in sex
                     determining region Y (SRY)-box 17 (SOX17) and similar
                     proteins; cd22047"
                     /db_xref="CDD:438850"
     Site            order(69..70,72..73,75..76,80,83,94..96,99..100,103,106,
                     136..137,139..141)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438850"
     Region          203..253
                     /region_name="Sox17_18_mid"
                     /note="Sox 17/18 central domain; pfam12067"
                     /db_xref="CDD:463454"
     CDS             1..423
                     /gene="Sox17"
                     /coded_by="NM_001436739.1:719..1990"
                     /db_xref="GeneID:312936"
                     /db_xref="RGD:1305371"
ORIGIN      
        1 msspdagyas ddqsqprsaq pavmaglgpc pwaeslsslg dvkvkgevva ssgapagtss
       61 rakaesrirr pmnafmvwak derkrlaqqn pdlhnaelsk mlgkswkalt laekrpfvee
      121 aerlrvqhmq dhpnykyrpr rrkqvkrmkr veggflhala epqagalgpe ggrvamdglg
      181 lpfpepgypa gpplmsphmg ahyrdcqglg apaldgyplp tpdtspldgv eqdpaffaap
      241 lpgdcpaaga ytyaqvsdya vpaepsagpm rvgpdpsgsa mpgilappsa lhlyygamgs
      301 paasagrgfh aqpqqplqpq pppppppppp pqqhpthgpg qpspppealp crdgtepnqp
      361 tellgevdrt efeqylhfvy kpemglpyqg hdcgvnlsds hgaissvvsd assavyycny
      421 pdi
//
LOCUS       NP_001099465             621 aa            linear   ROD 28-MAR-2025
DEFINITION  kelch-like protein 8 [Rattus norvegicus].
ACCESSION   NP_001099465 XP_001065538 XP_213995
VERSION     NP_001099465.1
DBSOURCE    REFSEQ: accession NM_001105995.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474022.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_213995.4, XP_001065538.1.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..621
                     /product="kelch-like protein 8"
                     /note="kelch-like 8"
                     /calculated_mol_wt=68437
     Region          53..172
                     /region_name="BTB_POZ_KLHL8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 8 (KLHL8); cd18238"
                     /db_xref="CDD:349547"
     Region          61..536
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          357..400
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          404..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          451..496
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          498..543
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..587
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          556..601
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..621
                     /gene="Klhl8"
                     /coded_by="NM_001105995.1:283..2148"
                     /db_xref="GeneID:289457"
                     /db_xref="RGD:1304685"
ORIGIN      
        1 masestngkl arshvtkgrr qqqqqqqvrs rssvsecdgd dsfifeanea wkdfhgsllg
       61 fyengelcdv tlkvgsklis chklalacvi pyframflse mseakqalie irdfdgdave
      121 dlvkfvyssr ltltvdnvqp llyaacilqv elvaraccey mklhfhpsnc lavrafaesh
      181 nrtdlmdmad qyacehftev vecedfvsvs pqhlhkllss sdlnidsekq vysaaikwll
      241 anpqhhpkwl detlaqvrlp llpvdflmgv vakeqivkqn lkcrdlldea rnyhlhlssk
      301 pvpdfeysvr ttprkhtagv lfcvggrggs gdpfrsiecy sintnswffg pemnsrrrhv
      361 gvisvegkvy avgghdgneh lgsmemfdpl tnkwmvkasm ntkrrgiala slggpiyaig
      421 glddntcfsd verydiesdq wstvapmntp rggvgsvali nhvyavggnd gvaslssver
      481 yhphldkwve vkemgqrrag ngvselhgcl yvvggfddns plssverydp rsnkwdyvaa
      541 lttprggvgi atvmgkifav gghngnayln tveafdpvln kwelvgpvsh cragagvavc
      601 dcltsqirdv ghgstnvvdc m
//
LOCUS       NP_001129228             601 aa            linear   ROD 28-MAR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase-like 6 [Rattus
            norvegicus].
ACCESSION   NP_001129228 XP_017455671 XP_341430
VERSION     NP_001129228.1
DBSOURCE    REFSEQ: accession NM_001135756.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Zhang,S., Wang,X., Chen,G., Tong,L., Dai,T., Wang,L., Zhu,L.,
            Zhang,H. and Du,D.
  TITLE     CircRNA Galntl6 sponges miR-335 to ameliorate stress-induced
            hypertension through upregulating Lig3 in rostral ventrolateral
            medulla
  JOURNAL   Redox Biol 64, 102782 (2023)
   PUBMED   37315345
  REMARK    GeneRIF: CircRNA Galntl6 sponges miR-335 to ameliorate
            stress-induced hypertension through upregulating Lig3 in rostral
            ventrolateral medulla.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Raman,J., Guan,Y., Perrine,C.L., Gerken,T.A. and Tabak,L.A.
  TITLE     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferases: completion of the family tree
  JOURNAL   Glycobiology 22 (6), 768-777 (2012)
   PUBMED   22186971
  REMARK    Erratum:[Glycobiology. 2015 Apr;25(4):465. doi:
            10.1093/glycob/cwv003. PMID: 25715345]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Mar 17, 2025 this sequence version replaced
            XP_017455671.1, XP_341430.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2139697.1,
                                           SRR26643298.71383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840106
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p12-p11"
     Protein         1..601
                     /product="polypeptide
                     N-acetylgalactosaminyltransferase-like 6"
                     /EC_number="2.4.1.41"
                     /note="polypeptide N-acetylgalactosaminyltransferase 17;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase-like 6"
                     /calculated_mol_wt=69640
     Region          143..438
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(147..149,151,180,209,212,216,232..234,314..315,
                     337..338,340,365,368,373)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(232,234,365)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          449..594
                     /region_name="beta-trefoil_Ricin_GALNTL6"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide
                     N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and
                     similar proteins; cd23477"
                     /db_xref="CDD:467355"
     Site            order(520,531,534,538..539)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467355"
     CDS             1..601
                     /gene="Galntl6"
                     /gene_synonym="Galnt17; RGD1564773"
                     /coded_by="NM_001135756.2:1398..3203"
                     /db_xref="GeneID:361142"
                     /db_xref="RGD:1564773"
ORIGIN      
        1 mkrkqkrflq mtllftvali flpniglwsl ykdkhlmksa epaehqtfpl glgdgqfysw
       61 tdglrrkdwh dyvsiqkdal rsgkgehgkp yplteedhdd sayrengfni fvsnnialer
      121 slpdirhanc khkmylerlp ntsiiipfhn egwtsllrti hsiinrtpes liaeiilvdd
      181 fsdrehlkdk ledymarfpi vrivrtkkre glirtrllga svargevltf ldshcevnvn
      241 wlppllnqia lnhktivcpm idvidhshfg yeaqagdamr gafdwemyyk ripippelqr
      301 adpsepfesp vmagglfavd rkwfwelggy dpgleiwgge qyeisfkvwm cggemfdvpc
      361 srvghiyrky vpykvpsgts larnlkrvae twmdefaeyi yqrrpeyrhl stgdisaqke
      421 lrkrlkckdf kwfmaavawd vpkyyppvep lpaawgeirn vaanlcvdsk hgamgtelrl
      481 dicvkdgser twsheqlftf gwredirpge plhtrkfcld aishsspvtl ydchgmkgnq
      541 lwgyredrtl fhpvsnscmd cnpaekkvfm arcdplsetq qwmfehinmt vlekishyai
      601 s
//
LOCUS       NP_001100796             633 aa            linear   ROD 28-MAR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 11 [Rattus
            norvegicus].
ACCESSION   NP_001100796 XP_001074785 XP_006253454 XP_240482
VERSION     NP_001100796.1
DBSOURCE    REFSEQ: accession NM_001107326.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Mar 17, 2025 this sequence version replaced
            XP_006253454.1, XP_240482.2, XP_001074785.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.72145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN12840113
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..633
                     /product="kelch repeat and BTB domain-containing protein
                     11"
                     /note="kelch repeat and BTB (POZ) domain containing 11"
                     /calculated_mol_wt=67718
     Region          144..246
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          237..313
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     Region          341..574
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          356..404
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          496..546
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..633
                     /gene="Kbtbd11"
                     /gene_synonym="RGD1563576"
                     /coded_by="NM_001107326.2:976..2877"
                     /db_xref="GeneID:306617"
                     /db_xref="RGD:1563576"
ORIGIN      
        1 mensvapfvl ypgteprtpg edslplpaee egaaspaqtp cslsaslcfs sgddsppqsr
       61 asaaegseas ppslrsdlrv vetqwdvssa aspespqeca rpeepaspee ppsrreharp
      121 velesldelg epvpvppgvg sehgepdlvi evagrrlrah kavlaarsdy frarasrdvl
      181 rvqgvsftal rllladaysg cmagvrpdnv aevvagarrl qlpgaaqrat eamapqlsld
      241 ncyevlsagk rqrlselrda ayrfmcdhyl evlrepavfg rlsgaerdll lrrrlgtgra
      301 cllaaalgtt gersgsrpqs psgdaesrgd aavycyqaea gewreltrlp egapargcgl
      361 cvlfnylfva ggvapagpdg rarpsdqvfc ynpvtdcwst vrplrqarsq vqllaldghl
      421 yalggeclls verydpradr wtavaplprg afavaheaat cngeiyvsgg slfyrllkyd
      481 prrdewqecp csssrersad mvaldgflyr fdlcgsrgda qaatgsgggv svfryhclak
      541 qwsqcaahlr ppgapaglqp frcvaldgti ycvsragtwr fvpsqdteag sdmgpggsfe
      601 peplgspldv rgvlfpfvln lpekpdrgeq gaa
//
LOCUS       NP_001099548             273 aa            linear   ROD 28-MAR-2025
DEFINITION  testis-specific serine/threonine-protein kinase 6 [Rattus
            norvegicus].
ACCESSION   NP_001099548 XP_001071471 XP_224740
VERSION     NP_001099548.1
DBSOURCE    REFSEQ: accession NM_001106078.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Jha,K.N., Coleman,A.R., Wong,L., Salicioni,A.M., Howcroft,E. and
            Johnson,G.R.
  TITLE     Heat shock protein 90 functions to stabilize and activate the
            testis-specific serine/threonine kinases, a family of kinases
            essential for male fertility
  JOURNAL   J Biol Chem 288 (23), 16308-16320 (2013)
   PUBMED   23599433
REFERENCE   2  (residues 1 to 273)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Spiridonov,N.A., Wong,L., Zerfas,P.M., Starost,M.F., Pack,S.D.,
            Paweletz,C.P. and Johnson,G.R.
  TITLE     Identification and characterization of SSTK, a serine/threonine
            protein kinase essential for male fertility
  JOURNAL   Mol Cell Biol 25 (10), 4250-4261 (2005)
   PUBMED   15870294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474031.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001071471.1, XP_224740.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..273
                     /product="testis-specific serine/threonine-protein kinase
                     6"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=30156
     Region          11..267
                     /region_name="STKc_TSSK6-like"
                     /note="Catalytic domain of testis-specific
                     serine/threonine kinase 6 and similar proteins; cd14164"
                     /db_xref="CDD:271066"
     Site            order(18..22,26,39,41,73,90..93,96,98..99,101,134..135,
                     137,139..140,142,153..154,157,172..176,178,208..211)
                     /site_type="active"
                     /db_xref="CDD:271066"
     Site            order(18..21,26,39,41,73,90..93,96,139..140,142,153..154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271066"
     Site            order(96,98..99,101,135,137,139,157,172..176,178,208..211)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271066"
     Site            153..176
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271066"
     CDS             1..273
                     /gene="Tssk6"
                     /gene_synonym="RGD1559764"
                     /coded_by="NM_001106078.1:94..915"
                     /db_xref="GeneID:290670"
                     /db_xref="RGD:1559764"
ORIGIN      
        1 msgdkllsel gyklgrtige gsyskvkvat skkykgtvai kvvdrrrapp dfvnkflpre
       61 lsilrgvrhp hivhvfefie vcngklyivm eaaatdllqa vqrngripgs qarelfsqia
      121 gavrylhdhh lvhrdlkcen vllspderrv kltdfgfgrq ahgypdlstt ycgsaayasp
      181 evllgipydp kkydvwslgv vlyvmvtgcm pfddsdiagl prrqkrgvly pdglelserc
      241 ksliaellqf spsarpsagq varngwlrag dsg
//
LOCUS       NP_001101442            2350 aa            linear   ROD 28-MAR-2025
DEFINITION  transcription factor HIVEP3 [Rattus norvegicus].
ACCESSION   NP_001101442 XP_001053243 XP_017448885 XP_233464
VERSION     NP_001101442.1
DBSOURCE    REFSEQ: accession NM_001107972.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2350)
  AUTHORS   Rajan,S., Chu Pham Dang,H., Djambazian,H., Zuzan,H., Fedyshyn,Y.,
            Ketela,T., Moffat,J., Hudson,T.J. and Sladek,R.
  TITLE     Analysis of early C2C12 myogenesis identifies stably and
            differentially expressed transcriptional regulators whose
            knock-down inhibits myoblast differentiation
  JOURNAL   Physiol Genomics 44 (2), 183-197 (2012)
   PUBMED   22147266
REFERENCE   2  (residues 1 to 2350)
  AUTHORS   Wu,L.C., Goettl,V.M., Madiai,F., Hackshaw,K.V. and Hussain,S.R.
  TITLE     Reciprocal regulation of nuclear factor kappa B and its inhibitor
            ZAS3 after peripheral nerve injury
  JOURNAL   BMC Neurosci 7, 4 (2006)
   PUBMED   16409637
  REMARK    GeneRIF: ZAS3 is expressed in nervous tissues involved in cognitive
            function and pain modulation; reciprocal changes in the expression
            of ZAS3 and NF-kappaB might generate neuropathic pain after
            peripheral nerve injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2350)
  AUTHORS   Bettelli,E., Dastrange,M. and Oukka,M.
  TITLE     Foxp3 interacts with nuclear factor of activated T cells and
            NF-kappa B to repress cytokine gene expression and effector
            functions of T helper cells
  JOURNAL   Proc Natl Acad Sci U S A 102 (14), 5138-5143 (2005)
   PUBMED   15790681
REFERENCE   4  (residues 1 to 2350)
  AUTHORS   Hicar,M.D., Robinson,M.L. and Wu,L.C.
  TITLE     Embryonic expression and regulation of the large zinc finger
            protein KRC
  JOURNAL   Genesis 33 (1), 8-20 (2002)
   PUBMED   12001065
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 21, 2025 this sequence version replaced
            XP_017448885.1, XP_001053243.1, XP_233464.4.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360194.96769.1, SRR21887620.956298.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression, longest
                                         protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2350
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..2350
                     /product="transcription factor HIVEP3"
                     /note="human immunodeficiency virus type I enhancer
                     binding protein 3"
                     /calculated_mol_wt=253691
     Region          194..214
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          207..231
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          222..242
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <1035..1274
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1722..1744
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1724..1744
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1736..1761
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1752..1774
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1943..>2320
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..2350
                     /gene="Hivep3"
                     /gene_synonym="Zas3"
                     /coded_by="NM_001107972.2:973..8025"
                     /db_xref="GeneID:313557"
                     /db_xref="RGD:1311252"
ORIGIN      
        1 mdpdqsikgt kkadgsprkr ltkgeaiqts vssstpypgs sttassegas qellapqpfs
       61 gpsvalrega qektgqqqkp prrpsieasa hipklpqhpl tpafmspskp ehllegstwq
      121 lvdptrpgps gsfvapglhp qsqllpshas ilppedlpgi pkvfvprpsq vslkpteeah
      181 kkerkpqkpg kyicqycsrp cakpsvlqkh irshtgerpy pcgpcgfsfk tksnlykhrk
      241 shahrikagl asgsssemyp pglemeripg eefeeptege stdseeetga tsgpstdvlp
      301 kskhpllsss lyssgshgss qercsqssta psledptpfa eassehplsh kledthtikq
      361 klalrlserk klieeqtfls pgskgstesg yfsrsesaeq qvsppntnak syaeiifgkc
      421 grigqrtsml aststqpllp lsaedkpslv plsvprtqvi ehitklitin eavvdtseid
      481 svkprrsslt rrssvespks slyreslssh gektkqeqsl lslqhppsst hpvpllrshs
      541 mpsaactist hhhtfrgsys fddhiadpev psrstpvfts hprmlkrqpa ielplgaeys
      601 seepgpsskd pitkpsdepe pkesdltkkt kkglktkgvn yecticgary kkrdnyeahk
      661 kyycselqit kahpagahev ektqaepepw sqmmhyklga tleltplrkr rkekslgdee
      721 eppgfsspgp sdaahnlple stkspaeask svptlegpts fqprtpkpgs gsepgkerrt
      781 mskeisviqh tssfeksdpp eqpgsleedk plapfssppp aphgrsahsl qprlvrqpni
      841 qvpeilvtee pdrpdtepep ppkepektee fqwpqrsqtl aqlpaeklpp kkkrlrlaem
      901 aqssgessfe ssvplsrsps qessislsgs srsasfdred hgkaetpgpl sdtrsktlgt
      961 hmltvpshhp haremrrsas eqspnvphss hmtetrsksf dygslsptgp svavpaappp
     1021 paapperrkc flvrqaslsr ppeaeleatp kgkqesseep saskpstkss maqisvatiq
     1081 gglsgsksqm qdrpplgssp pytealqvfq plgtqlpppv slfslqqllp qeqeqsseff
     1141 ptqamaglls spysvpplpp slfqapplpl qptvlhpsql hlpqllphaa dipfqqppsf
     1201 lpmpcpapst lsgyflplqs qfalqlpgei eshlpsikts lpplatgppg psssteyssd
     1261 iqlppvtpqa tspaptsasp lalpacpdam vslvvpvriq thmpsygsam yttlsqilvt
     1321 qspgsstsma ltkyeepssk smtvcgadvy eaepgpssis keqsrgfqtp ylrvperkgt
     1381 alssegilsl egcsstasgs krvlspagsl eltmetqqqk rvkeeeaska deklelvstc
     1441 nvvltstedr kktekphvgs qgrsrretet lsclssdvsd pkelsplsqs tlshgtapgs
     1501 ealkeyaqps skahrrclpp lsvkkedpke qtdlpplapp sslplsdtsp rpaklqegtd
     1561 skkvlqfpsl htttnvswcy lnyikpnhiq hadrrssvya gwcislynpn lpgvstkaal
     1621 sllrskqkvs ketytmatap hpeagrlvps nsrkprmtev hlpsmvsles qkdparveke
     1681 ekaeegtpts krgeptrvki feggyksnee yiyvrgrgrg kyvceecgir ckkpsmlkkh
     1741 irthtdvrpy vcrhchfafk tkgnltkhmk skahskkcqe tgvleeleae egtsddllqd
     1801 segregseav eehqfsdled sdsdsdlded eeeeeeeeee sqdelsrpss eaaplclpat
     1861 lqedsslirg pqppdatsda aprgssisea trltasscst psqgtqglpr lglaplekgt
     1921 ssalspkats prrpwspske agsrpsltrk hsltktdssp qrcsparaqa svastpgpqt
     1981 gpgrdlsphl cgsprpelsc ltpypigrev paglesatvt gtprcsptrr rslgraessp
     2041 phtvlpgtwa lggpcspsvd kyglglgpvp rallqpvplp htllsrspet casawktesr
     2101 spsagpapls srpssaphdf hghlpsrsee nlfshlplhs qhlnrtpcpl ipiggiqmvq
     2161 arpgahptll sgpcaawvsg fsgggsdltg areaqersrw sptespsasv spvakvskft
     2221 lsseleeert srgpgrppaw ephraeapae tmgthspcpp qlpqghplap swrgllesph
     2281 alanlkassf ppldrsssmd claetstcfp prsrnlsgep rtrpdspell gsgelrtplf
     2341 lskdsgppsi
//
LOCUS       NP_001423493            1048 aa            linear   ROD 28-MAR-2025
DEFINITION  malignant fibrous histiocytoma-amplified sequence 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423493 XP_006253286
VERSION     NP_001423493.1
DBSOURCE    REFSEQ: accession NM_001436564.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Wang,H.H., Sun,P.F., Chen,W.K., Zhong,J., Shi,Q.Q., Weng,M.L.,
            Ma,D. and Miao,C.H.
  TITLE     High Glucose Stimulates Expression of MFHAS1 to Mitigate
            Inflammation via Akt/HO-1 Pathway in Human Umbilical Vein
            Endothelial Cells
  JOURNAL   Inflammation 41 (2), 400-408 (2018)
   PUBMED   29168081
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Shi,Q., Xiong,B., Zhong,J., Wang,H., Ma,D. and Miao,C.
  TITLE     MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C
            subunit cytoplasm translocation and inhibition of c-Jun
            dephosphorylation at Thr239
  JOURNAL   Mol Immunol 88, 79-88 (2017)
   PUBMED   28609714
REFERENCE   3  (residues 1 to 1048)
  AUTHORS   Zhong,J., Wang,H., Chen,W., Sun,Z., Chen,J., Xu,Y., Weng,M.,
            Shi,Q., Ma,D. and Miao,C.
  TITLE     Ubiquitylation of MFHAS1 by the ubiquitin ligase praja2 promotes M1
            macrophage polarization by activating JNK and p38 pathways
  JOURNAL   Cell Death Dis 8 (5), e2763 (2017)
   PUBMED   28471450
  REMARK    Erratum:[Cell Death Dis. 2018 Jul 16;9(8):782. doi:
            10.1038/s41419-018-0828-y. PMID: 30013073]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1048)
  AUTHORS   Zhong,J., Shi,Q.Q., Zhu,M.M., Shen,J., Wang,H.H., Ma,D. and
            Miao,C.H.
  TITLE     MFHAS1 Is Associated with Sepsis and Stimulates TLR2/NF-kappaB
            Signaling Pathway Following Negative Regulation
  JOURNAL   PLoS One 10 (11), e0143662 (2015)
   PUBMED   26599367
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1048)
  AUTHORS   Dihanich,S., Civiero,L., Manzoni,C., Mamais,A., Bandopadhyay,R.,
            Greggio,E. and Lewis,P.A.
  TITLE     GTP binding controls complex formation by the human ROCO protein
            MASL1
  JOURNAL   FEBS J 281 (1), 261-274 (2014)
   PUBMED   24286120
REFERENCE   6  (residues 1 to 1048)
  AUTHORS   Kumkhaek,C., Aerbajinai,W., Liu,W., Zhu,J., Uchida,N.,
            Kurlander,R., Hsieh,M.M., Tisdale,J.F. and Rodgers,G.P.
  TITLE     MASL1 induces erythroid differentiation in human
            erythropoietin-dependent CD34+ cells through the Raf/MEK/ERK
            pathway
  JOURNAL   Blood 121 (16), 3216-3227 (2013)
   PUBMED   23327923
REFERENCE   7  (residues 1 to 1048)
  AUTHORS   Ng,A.C., Eisenberg,J.M., Heath,R.J., Huett,A., Robinson,C.M.,
            Nau,G.J. and Xavier,R.J.
  TITLE     Human leucine-rich repeat proteins: a genome-wide bioinformatic
            categorization and functional analysis in innate immunity
  JOURNAL   Proc Natl Acad Sci U S A 108 Suppl 1 (Suppl 1), 4631-4638 (2011)
   PUBMED   20616063
REFERENCE   8  (residues 1 to 1048)
  AUTHORS   Sakabe,T., Shinomiya,T., Mori,T., Ariyama,Y., Fukuda,Y.,
            Fujiwara,T., Nakamura,Y. and Inazawa,J.
  TITLE     Identification of a novel gene, MASL1, within an amplicon at 8p23.1
            detected in malignant fibrous histiocytomas by comparative genomic
            hybridization
  JOURNAL   Cancer Res 59 (3), 511-515 (1999)
   PUBMED   9973190
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 17, 2025 this sequence version replaced XP_006253286.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32846.1,
                                           SRR26643288.55887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN16676806
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..1048
                     /product="malignant fibrous histiocytoma-amplified
                     sequence 1 isoform 1"
                     /note="malignant fibrous histiocytoma amplified sequence
                     1"
                     /calculated_mol_wt=116427
     Region          61..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <109..>371
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          109..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..155
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          156..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          225..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          248..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          294..316
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          317..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          340..360
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          405..>548
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            412..419
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206741"
     Site            451
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206741"
     Site            455..457
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206741"
     Site            473..476
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206741"
     Site            order(475..476,492..493)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206741"
     Site            533..536
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206741"
     Region          656..902
                     /region_name="COR"
                     /note="C-terminal of Roc, COR, domain; pfam16095"
                     /db_xref="CDD:406489"
     CDS             1..1048
                     /gene="Mfhas1"
                     /coded_by="NM_001436564.1:603..3749"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:306508"
                     /db_xref="RGD:1308812"
ORIGIN      
        1 magkdsgnlk tvrlwrdaal rarklrsnlr qltlscpgag gdslespdap qlvlpanigd
       61 ievlnlgnng ledvpeglgs algslrvlvl rrnrfarlpp avaelghhlt eldvshnrlt
      121 ilgaevvsal relrklnlsh nqlpalpaql galahleeld vsfnrlahlp dsfsclnhlr
      181 tldvdhnqlt afpqqllqla aleeldvssn rlrglpedis alralkilwl sgaelgtlps
      241 gfcelasles lmldnnglqa lpdefsrlqr lkmlnlssnl feefpaallp lagleelyls
      301 rnqltsvpsl iaglgrlltl wldnnriryl pdsiveltgl eelvlqgnqi avlpdnfgql
      361 srvglwkikd npliqppyev cmkgipyiaa yqkelahsqp avqprlklll mghkaagktl
      421 lrhcltedkv eggqgggdke ksylpfpplg skgievtswt adasrglrfi vydlagdesy
      481 eviqpfflsp galyvlvvnl atyeprcfpt tvgsflhrvg arvphavvci vgthadlcge
      541 releekcldi hrqialqekh daeglshlak vvdealardf elrsasphaa yygvsdknlr
      601 rrkahfqyll nhrlqilspv lpvscrdplq lqrlrdklls vaehreifpn lhrvlprswq
      661 vleelhfqpp qaqrlwlsww dsarlglqag ltedrlqsal sylhesgkll yfedspalke
      721 hvfhnltrli dilnvffqrd aslllhklll gtngegegeg esfptiavpt pgqdplratq
      781 lhhyvegfll hgllpahiir lllkphvqaq qdlqlllell ekmglcycln kpkgkplngs
      841 aawykfpcyv qnevphaeaw ingtnlagqs fvaeqlqiey sfpftfppgl farysvqins
      901 hvvhrsdgkf qifayrgkvp vvvsyrpakg vlqpdtlsia shaslpniwt awqaitplve
      961 elnvllqewp glhytvhilc skclkrgspn phafpgells qprpegvaei icpkngserv
     1021 nvalvypptp tvispcskkn vgekhrnq
//
LOCUS       NP_001423541             753 aa            linear   ROD 28-MAR-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 5
            isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423541 XP_006253384
VERSION     NP_001423541.1
DBSOURCE    REFSEQ: accession NM_001436612.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Rosselot,C., Kierszenbaum,A.L., Rivkin,E. and Tres,L.L.
  TITLE     Chronological gene expression of ADAMs during testicular
            development: prespermatogonia (gonocytes) express fertilin beta
            (ADAM2)
  JOURNAL   Dev Dyn 227 (3), 458-467 (2003)
   PUBMED   12815633
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Frayne,J., Jury,J.A., Barker,H.L. and Hall,L.
  TITLE     Rat MDC family of proteins: sequence analysis, tissue distribution,
            and expression in prepubertal and adult rat testis
  JOURNAL   Mol Reprod Dev 48 (2), 159-167 (1997)
   PUBMED   9291465
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Cho,C., Primakoff,P., White,J.M. and Myles,D.G.
  TITLE     Chromosomal assignment of four testis-expressed mouse genes from a
            new family of transmembrane proteins (ADAMs) involved in cell-cell
            adhesion and fusion
  JOURNAL   Genomics 34 (3), 413-417 (1996)
   PUBMED   8786143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 18, 2025 this sequence version replaced XP_006253384.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079016.1, SRR26360186.1697656.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..753
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 5 isoform 1 precursor"
                     /note="a disintegrin and metalloprotease domain (ADAM) 5;
                     tMDC II; a disintegrin and metalloprotease domain 5;
                     disintegrin and metalloproteinase domain-containing
                     protein 5; transmembrane metalloproteinase-like,
                     disintegrin-like, and cysteine-rich protein II; a
                     disintegrin and metallopeptidase domain 5"
                     /calculated_mol_wt=83188
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     Region          26..142
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          185..378
                     /region_name="Reprolysin"
                     /note="Reprolysin (M12B) family zinc metalloprotease;
                     pfam01421"
                     /db_xref="CDD:426256"
     Region          399..473
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Region          477..620
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     CDS             1..753
                     /gene="Adam5"
                     /gene_synonym="tMDCII"
                     /coded_by="NM_001436612.1:66..2327"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:498654"
                     /db_xref="RGD:621471"
ORIGIN      
        1 mflllllvvh lnglqagqhp qktilqttvp ekisspdvet dpenhmayli tinenphfih
       61 lkkqsfitst avsytydrqd vrhsqslssl kncnyngyva gfpnsivslt vcsglrgmiq
      121 fenvsygiep vetlsgfihv iyentnqqak ipdlgenqty swsdeldyqf rsnmkksgfa
      181 vlrpryiktd ivvdkklfdy mgsdtrvvlq kviqiigfin tmfsklkltv linsveiwsk
      241 enridfpeap enllvqflhw khkyrpqhis yllafvehpa stgalypgnl ckpiygaaia
      301 lypkglsles ysvivlqlls igigltydna dschctgdvc lmtpkaiysg gvkdfstcsl
      361 ddfkylstqd leclqdlpme rqkkkpsrpr ricgngilem neqcdcgtlk ncthkkccdp
      421 mscrlkskav cgsgeccgqd ckvkpvnvlc rksknecdfe eycngndayc vpdtfarngq
      481 ycdsgqafcy sglcmtsnnq cmnllgkyvr gasfacyeef nsrndrfgnc irkfcsfens
      541 lcgklvctwp fkrllmkdnm saaygqirdd lcislykggr plkttlstys dmserdetfv
      601 kdgticgpdm fcletqcket rflvdfqqcn tsrdcndhgv cnnfnhchcd kgynppyces
      661 vkgqfgsidd ghkyyidegk sakqqnrgih pkqqlqlily itlplimiis avfikqskls
      721 rlcgrerseg tscitedsvs ntkmttnegs tlh
//
LOCUS       NP_786941                528 aa            linear   ROD 28-MAR-2025
DEFINITION  PC4 and SFRS1-interacting protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_786941 XP_063143704
VERSION     NP_786941.2
DBSOURCE    REFSEQ: accession NM_175765.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Baude,A., Aaes,T.L., Zhai,B., Al-Nakouzi,N., Oo,H.Z., Daugaard,M.,
            Rohde,M. and Jaattela,M.
  TITLE     Hepatoma-derived growth factor-related protein 2 promotes DNA
            repair by homologous recombination
  JOURNAL   Nucleic Acids Res 44 (5), 2214-2226 (2016)
   PUBMED   26721387
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Tsutsui,K.M., Sano,K., Hosoya,O., Miyamoto,T. and Tsutsui,K.
  TITLE     Nuclear protein LEDGF/p75 recognizes supercoiled DNA by a novel
            DNA-binding domain
  JOURNAL   Nucleic Acids Res 39 (12), 5067-5081 (2011)
   PUBMED   21345933
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Hendrix,J., Gijsbers,R., De Rijck,J., Voet,A., Hotta,J.,
            McNeely,M., Hofkens,J., Debyser,Z. and Engelborghs,Y.
  TITLE     The transcriptional co-activator LEDGF/p75 displays a dynamic
            scan-and-lock mechanism for chromatin tethering
  JOURNAL   Nucleic Acids Res 39 (4), 1310-1325 (2011)
   PUBMED   20974633
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Nishizawa,Y., Usukura,J., Singh,D.P., Chylack,L.T. Jr. and
            Shinohara,T.
  TITLE     Spatial and temporal dynamics of two alternatively spliced
            regulatory factors, lens epithelium-derived growth factor
            (ledgf/p75) and p52, in the nucleus
  JOURNAL   Cell Tissue Res 305 (1), 107-114 (2001)
   PUBMED   11512661
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Sharma,P., Singh,D.P., Fatma,N., Chylack,L.T. Jr. and Shinohara,T.
  TITLE     Activation of LEDGF gene by thermal-and oxidative-stresses
  JOURNAL   Biochem Biophys Res Commun 276 (3), 1320-1324 (2000)
   PUBMED   11027629
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Ge,H., Si,Y. and Wolffe,A.P.
  TITLE     A novel transcriptional coactivator, p52, functionally interacts
            with the essential splicing factor ASF/SF2
  JOURNAL   Mol Cell 2 (6), 751-759 (1998)
   PUBMED   9885563
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Ge,H., Si,Y. and Roeder,R.G.
  TITLE     Isolation of cDNAs encoding novel transcription coactivators p52
            and p75 reveals an alternate regulatory mechanism of
            transcriptional activation
  JOURNAL   EMBO J 17 (22), 6723-6729 (1998)
   PUBMED   9822615
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Tsutsui,K., Tsutsui,K. and Muller,M.T.
  TITLE     The nuclear scaffold exhibits DNA-binding sites selective for
            supercoiled DNA
  JOURNAL   J Biol Chem 263 (15), 7235-7241 (1988)
   PUBMED   3366776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Mar 21, 2025 this sequence version replaced
            XP_063143704.1, NP_786941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.28334.1,
                                           SRR26643287.13454.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..528
                     /product="PC4 and SFRS1-interacting protein isoform 1"
                     /note="PC4 and SFRS1-interacting protein; supercoiled DNA
                     binding protein 75; PC4 and SFRS1 interacting protein 2;
                     lens epithelium-derived growth factor; PC4 and SFRS1
                     interacting protein 1"
                     /calculated_mol_wt=59485
     Region          5..92
                     /region_name="PWWP_PSIP"
                     /note="PWWP domain found in PC4 and SFRS1-interacting
                     protein (PSIP); cd20151"
                     /db_xref="CDD:438979"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438979"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438979"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438979"
     Region          86..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          <90..523
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JF8; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          146..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          338..415
                     /region_name="Integrase-binding domain (IBD).
                     /evidence=ECO:0000250|UniProtKB:O75475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          347..448
                     /region_name="LEDGF"
                     /note="Lens epithelium-derived growth factor (LEDGF);
                     pfam11467"
                     /db_xref="CDD:463284"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Region          444..528
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75475; propagated from
                     UniProtKB/Swiss-Prot (Q812D1.1)"
     CDS             1..528
                     /gene="Psip1"
                     /gene_synonym="Ledgf; Psip2; SBP75"
                     /coded_by="NM_175765.3:283..1869"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:313323"
                     /db_xref="RGD:631439"
ORIGIN      
        1 mtrdfkpgdl ifakmkgyph wparvdevpd gavkpptnkl pifffgthet aflgpkdifp
       61 ysenkekygk pnkrkgfneg lweidnnpkv kfssqqvstk qsnassdvea eeketsvske
      121 dtdqeekasn edvtkaadit tpkaarrgrk rkaekqvdte eagvvtaata snvkaspkrg
      181 rpaatevkip kprgrpkvvk qpcpsesdmv idedkskkkg peekppkkql kkeeegqkee
      241 ekprkepdkk egkkeveskr knlakpgvts tsdseedddq egekkrkggr nfqaahrrnm
      301 lkgqhekeaa drkrkqeeqm eteqqtkdeg kkpevkkvek kretsmdsrl qrihaeikns
      361 lkidnldvnr ciealdelas lqvtmqqaqk htemittlkk irrfkvsqvi mekstmlynk
      421 fknmflvgeg dsvitqvlnk slaeqrqhee anktkdqgkk gpnkklekeq tgtkslnggs
      481 daqesnhpqh ngdsaeeskd sreagsktkt pgeereaevs lkestldn
//
LOCUS       NP_001423982             596 aa            linear   ROD 28-MAR-2025
DEFINITION  glomulin [Rattus norvegicus].
ACCESSION   NP_001423982 XP_008768144
VERSION     NP_001423982.1
DBSOURCE    REFSEQ: accession NM_001437053.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Tron,A.E., Arai,T., Duda,D.M., Kuwabara,H., Olszewski,J.L.,
            Fujiwara,Y., Bahamon,B.N., Signoretti,S., Schulman,B.A. and
            DeCaprio,J.A.
  TITLE     The glomuvenous malformation protein Glomulin binds Rbx1 and
            regulates cullin RING ligase-mediated turnover of Fbw7
  JOURNAL   Mol Cell 46 (1), 67-78 (2012)
   PUBMED   22405651
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Krummrei,U., Baulieu,E.E. and Chambraud,B.
  TITLE     The FKBP-associated protein FAP48 is an antiproliferative molecule
            and a player in T cell activation that increases IL2 synthesis
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2444-2449 (2003)
   PUBMED   12604780
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Brouillard,P., Boon,L.M., Mulliken,J.B., Enjolras,O., Ghassibe,M.,
            Warman,M.L., Tan,O.T., Olsen,B.R. and Vikkula,M.
  TITLE     Mutations in a novel factor, glomulin, are responsible for
            glomuvenous malformations ('glomangiomas')
  JOURNAL   Am J Hum Genet 70 (4), 866-874 (2002)
   PUBMED   11845407
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Grisendi,S., Chambraud,B., Gout,I., Comoglio,P.M. and Crepaldi,T.
  TITLE     Ligand-regulated binding of FAP68 to the hepatocyte growth factor
            receptor
  JOURNAL   J Biol Chem 276 (49), 46632-46638 (2001)
   PUBMED   11571281
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Chambraud,B., Radanyi,C., Camonis,J.H., Shazand,K., Rajkowski,K.
            and Baulieu,E.E.
  TITLE     FAP48, a new protein that forms specific complexes with both
            immunophilins FKBP59 and FKBP12. Prevention by the
            immunosuppressant drugs FK506 and rapamycin
  JOURNAL   J Biol Chem 271 (51), 32923-32929 (1996)
   PUBMED   8955134
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 26, 2025 this sequence version replaced XP_008768144.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.45951.1,
                                           SRR26643294.49292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..596
                     /product="glomulin"
                     /note="FKBP associated protein"
                     /calculated_mol_wt=67448
     Region          1..524
                     /region_name="Kinetochor_Ybp2"
                     /note="Uncharacterized protein family, YAP/Alf4/glomulin;
                     pfam08568"
                     /db_xref="CDD:400745"
     CDS             1..596
                     /gene="Glmn"
                     /coded_by="NM_001437053.1:81..1871"
                     /db_xref="GeneID:289437"
                     /db_xref="RGD:1588600"
ORIGIN      
        1 maveelqcii krcqileehd fkeedfglfq lagqrciedg yinqlleiiq deknktiikt
       61 mgwnlvgpvv rcllrgreed kreecflifd llvklcnpke lllgllelie epsgkqisqi
      121 illllqplqt viqklpnnka ysaglalstl wsqlsllpvp hseeqiqadd yglcqccral
      181 ieftkpfvae vasdkedpan tklkdellkf cfkslkcpll taqfleqsee vgndpfrcfa
      241 seiigflsqi gypvpqiiln hgrkkrtwdy lefeeeedrq ladsvaalty lvfvqgigtd
      301 qlpmvlspsy llqlnmehie vllqrteqsv yskglellet sllrlednsl cyqyleiksf
      361 lavpqglvkv mtlcpietlr ktglamlqly idkldsqgky tlfrcllnts nhsgveafvi
      421 qniknqidls ykkthnrwfa gaqltslldl vlslpegaet dllqnsdrim aslnllrylv
      481 ikdneddnqt glwtelgkie nnflqplhvg lnmskahyea eiknsqqnsq aasmcksvcs
      541 vtvggeeipt mppemqlkvl hsalftfdli esvlarveel ieikskstse enagmk
//
LOCUS       NP_001424083             423 aa            linear   ROD 30-MAR-2025
DEFINITION  galactosylceramide sulfotransferase [Rattus norvegicus].
ACCESSION   NP_001424083 XP_006251444
VERSION     NP_001424083.1
DBSOURCE    REFSEQ: accession NM_001437154.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Honke,K., Hirahara,Y., Dupree,J., Suzuki,K., Popko,B.,
            Fukushima,K., Fukushima,J., Nagasawa,T., Yoshida,N., Wada,Y. and
            Taniguchi,N.
  TITLE     Paranodal junction formation and spermatogenesis require
            sulfoglycolipids
  JOURNAL   Proc Natl Acad Sci U S A 99 (7), 4227-4232 (2002)
   PUBMED   11917099
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Hirahara,Y., Tsuda,M., Wada,Y. and Honke,K.
  TITLE     cDNA cloning, genomic cloning, and tissue-specific regulation of
            mouse cerebroside sulfotransferase
  JOURNAL   Eur J Biochem 267 (7), 1909-1917 (2000)
   PUBMED   10727929
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006251444.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.2939026.1,
                                           SRR22399484.1421061.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..423
                     /product="galactosylceramide sulfotransferase"
                     /EC_number="2.8.2.11"
                     /calculated_mol_wt=48787
     Region          4..408
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; cl22970"
                     /db_xref="CDD:451469"
     CDS             1..423
                     /gene="Gal3st1"
                     /coded_by="NM_001437154.1:202..1473"
                     /db_xref="GeneID:683713"
                     /db_xref="RGD:1583379"
ORIGIN      
        1 mtllpkkpck skakglvlga lltsflllly syvvpplypn lafttseaaa pcspvpnepv
       61 aatpangsag gcqprrdivf mkthktasst llnilfrfgq khelkfafpn grndfhypsy
      121 farslvqdyr pgacfniicn hmrfhyeevr glvrpgatfi tvirdparlf essfhyfgsv
      181 vpltwklssr dklaeflqdp dryydpssyn ahylrnllff dlgydssldp gsprvqehil
      241 everrfhlvl lqeyfdeslv llrellcwdl edvlyfklna rrdspeprls gelyrrataw
      301 nlldvrlyrh fnasfwrkve afgrermase vaklrraneh mrsicidggq avdaeaiqds
      361 amqpwqplgi ksilgynlkk sigpqheqlc rrmltpeiqy lsdlganlwi tklwkffrdf
      421 lrw
//
LOCUS       NP_001424091            1695 aa            linear   ROD 30-MAR-2025
DEFINITION  arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing
            protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424091 XP_038947858
VERSION     NP_001424091.1
DBSOURCE    REFSEQ: accession NM_001437162.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1695)
  AUTHORS   Krugmann,S., Anderson,K.E., Ridley,S.H., Risso,N., McGregor,A.,
            Coadwell,J., Davidson,K., Eguinoa,A., Ellson,C.D., Lipp,P.,
            Manifava,M., Ktistakis,N., Painter,G., Thuring,J.W., Cooper,M.A.,
            Lim,Z.Y., Holmes,A.B., Dove,S.K., Michell,R.H., Grewal,A.,
            Nazarian,A., Erdjument-Bromage,H., Tempst,P., Stephens,L.R. and
            Hawkins,P.T.
  TITLE     Identification of ARAP3, a novel PI3K effector regulating both Arf
            and Rho GTPases, by selective capture on phosphoinositide affinity
            matrices
  JOURNAL   Mol Cell 9 (1), 95-108 (2002)
   PUBMED   11804589
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038947858.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.54667.1,
                                           SRR26360176.2079258.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1695
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..1695
                     /product="arf-GAP with Rho-GAP domain, ANK repeat and PH
                     domain-containing protein 2 isoform 2"
                     /note="arf-GAP with Rho-GAP domain, ANK repeat and PH
                     domain-containing protein 2; centaurin, delta 1"
                     /calculated_mol_wt=192482
     Region          6..68
                     /region_name="SAM_Arap1,2,3"
                     /note="SAM domain of Arap1,2,3 (angiotensin
                     receptor-associated protein); cd09490"
                     /db_xref="CDD:188889"
     Site            order(19,43,58..59,62)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188889"
     Region          480..571
                     /region_name="PH1_ARAP"
                     /note="ArfGAP with RhoGAP domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain, repeat 1; cd13253"
                     /db_xref="CDD:270073"
     Region          581..671
                     /region_name="PH2_ARAP"
                     /note="ArfGAP with RhoGAP domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain, repeat 2; cd13254"
                     /db_xref="CDD:270074"
     Region          676..796
                     /region_name="ArfGap_ARAP2"
                     /note="ArfGap with Rho-Gap domain, ANK repeat and PH
                     domain-containing protein 2; cd08856"
                     /db_xref="CDD:350081"
     Site            order(696,699,716,719,724)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350081"
     Site            order(696,699,716,719)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350081"
     Region          888..998
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          1011..1106
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          1110..1289
                     /region_name="RhoGAP_ARAP"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain present in ARAPs. ARAPs (also known
                     as centaurin deltas) contain, besides the RhoGAP domain,
                     an Arf GAP, ankyrin repeat ras-associating, and PH
                     domains. Since their ArfGAP activity...; cd04385"
                     /db_xref="CDD:239850"
     Site            order(1147,1186,1190,1259,1262..1263,1279)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239850"
     Site            1147
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239850"
     Region          1321..1418
                     /region_name="RA_ARAP2"
                     /note="Ras-associating (RA) domain found in Arf-GAP with
                     Rho-GAP domain, ANK repeat and PH domain-containing
                     protein 2 (ARAP2); cd17227"
                     /db_xref="CDD:340747"
     Region          1424..1535
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..1695
                     /gene="Arap2"
                     /gene_synonym="Centd1"
                     /coded_by="NM_001437162.1:582..5669"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305367"
                     /db_xref="RGD:1306452"
ORIGIN      
        1 msavsevnvd iqdflmsinl eqyllhfqef gfytvkdcts indnvlhqig isptghrrri
       61 lkqlqmifsk mqdfpiyanv yktkngstpk eqhsapssss ntciefsdsv tvhrpgpaps
      121 emvttnvlse gnchsstshd klslsssdlp cpeeeicqnv dssqdylfgr vnvkidslit
      181 qqavehtage eqtekvnlvs edsskalntn teclpsvdhp asethcgngt ngvlesfpps
      241 pffqfqgemv vnelyvpssp ihspmrsrsk lvsrpsrsfl lrhrpvpeip gstksisgsy
      301 frdrksitts agksltlkda nednstsifp ygetflfqrl esskkrsikn efwahedtvk
      361 eeaatsrnsi ltkssiydsr kekvsedkve diwipredkn nlpqdsases eystveecfq
      421 slrrknskas ksrtqkafyl dpfnrhsypl sstsentdps tianaispya cfygssaakv
      481 ksgwldklsp qgkrmfqkrw vkfdglsisy ynndremysk giipltaist vraqgdnkfe
      541 ivttqrtfvf rvekeeernd wisvllsalk spsltsqlqa avapekcgyl elrgykakif
      601 tvlrgnsvwl ckteqdfksg lgitiipmnv anvkqidrav kqsfeiitpy rsfsftadse
      661 kekqewieav qqsiaetlsd yevaekiwfn esnrscadck apdpdwasin lcvvickkca
      721 gqhrslgpkd skvrslkmda siwsneliel fivignkran dfwagnlkkd eeiqmdspvd
      781 krkifitqky kegkfrktfl asltkeelnk alcaavvkpd vletmallfs gadvmcatgd
      841 pvhctpylla kkagqslqme flyhnkfsdf pqydahsegg ssqeatqstf lcdflyqata
      901 sasrvstekk lleetnkkwc vleggflsyy endrcttpng tinisevicl tvhkedfyln
      961 tgpififeiy lpservflfg aktsqiqrkw tetiakrfvp fvaenltead ydligqlfyk
     1021 dchaldqwrk gwfamdkssl cfclqtqeaq eermhlrrlq eltistvvqn gekvdvlllv
     1081 ekgrtlyihg ytkldftvwr naiekaagtd gntlqdqqlc kndvpiivns ciafvtqygl
     1141 gckyiyqkdg dplsiselle sfkkdarsvk lrvgkhqled vtgvlksfls diddalltke
     1201 lypywvsald aqdekqrtdk yraficslpg vnratlaali ehlyrvqkcs einhmnahnl
     1261 alvfssclfq tkgqtseevn viedlinnyv eifevkedqv kqmdiensfi tkwkntqvsq
     1321 agdllievfa erkepdcsii irvspvmeae eltndilaik nilptkgdiw atfevienee
     1381 lerplhyten vleqvlqwss laepgsaylv vkrfltidti kqcreksike gilklkeeps
     1441 kilsgnkfqd rcvvlrdghl fiykdpkstk hekmfplrlm kfylgvkkkm kpptswglta
     1501 csekhhwhlc cdslqaqmew masifiaqhe ndiwppagke rkrsitknpk igglplipiq
     1561 heknatqark niemaraele rlrlserhdg dftdsslkdr asiigycleh kdeklrnrar
     1621 khrsfncled teaevppglp kgykglktvk ktedrnskat lepnnklpsk vieelsvvlq
     1681 rsrshpkelp deqtl
//
LOCUS       NP_001424073            1254 aa            linear   ROD 30-MAR-2025
DEFINITION  zinc finger and BTB domain-containing protein 40 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424073 XP_006239294
VERSION     NP_001424073.1
DBSOURCE    REFSEQ: accession NM_001437144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1254)
  AUTHORS   Matsuoka,S., Ballif,B.A., Smogorzewska,A., McDonald,E.R. 3rd,
            Hurov,K.E., Luo,J., Bakalarski,C.E., Zhao,Z., Solimini,N.,
            Lerenthal,Y., Shiloh,Y., Gygi,S.P. and Elledge,S.J.
  TITLE     ATM and ATR substrate analysis reveals extensive protein networks
            responsive to DNA damage
  JOURNAL   Science 316 (5828), 1160-1166 (2007)
   PUBMED   17525332
REFERENCE   2  (residues 1 to 1254)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   3  (residues 1 to 1254)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006239294.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.23932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1254
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1254
                     /product="zinc finger and BTB domain-containing protein 40
                     isoform 1"
                     /note="zinc finger and BTB domain-containing protein 40"
                     /calculated_mol_wt=138013
     Region          1..116
                     /region_name="BTB_POZ_ZBTB40"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 40 (ZBTB40); cd18225"
                     /db_xref="CDD:349534"
     Region          824..845
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(824,827,840,845)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          853..873
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(853,856,869,873)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(858,860,862,864..865,868..869,872,886,888,892,922,
                     925..926,929,943,945,947,949..950,953..954,957)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <869..1121
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          881..930
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          938..957
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          967..985
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          1023..1043
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1063..1082
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1092..1113
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1121..1140
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1152..1169
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1254
                     /gene="Zbtb40"
                     /gene_synonym="RGD1309866"
                     /coded_by="NM_001437144.1:316..4080"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362635"
                     /db_xref="RGD:1309866"
ORIGIN      
        1 melpnysqql llqlyalcke qrfcdctisi gniyfrahkp vlaaasllfk tlldstdais
       61 idasvvspee falllemtyt gklpvgkhnf skiisladsl qmfdvavcck nlltnlvncs
      121 vqgqvvrdis vlsseaggke sekpqvevls segagepsss levsampagt ekaktqevih
      181 mvtqeisadp piaqevqvaa eitgatphtt evcsplpagq ipseakaast eagcerkqdq
      241 ltllleyesv fssaalltpd mlrrlegcse iegpqketvm ecleaegggs afqrildkvh
      301 dgsldvqval slmrlcqest paekvsqieg sagegktlsv lllehkedli qcvtqlrpiv
      361 efletakeef lpdsekrviq iccegrtpke tvenllhrvt eektlpaksl vkllqavrta
      421 fpnlglllen lqkvaespgt tgltratret awteepkrlc ipadrvdgss pnpdaygael
      481 lrkyhenlse ilidsqvllk visrlkslap gdrevmqtlv kqdsgsggvs slmsaalerq
      541 tvsaaaiwql llaaqetetc plnllleeve repgagaffr avtapestvl etilrhsklv
      601 reaiqqtvgr ehlsseeehl aetvkemlsi ssetvspeas lrvvlsrame ksvsasvvch
      661 llcsvhrsfp glqplmqela hvgfltkena eerwkvtdgl hpgakdktee aaeaaredgr
      721 ameqkeqgpe pvperqekdt saspdaakks fvckacdksf hfycrlkvhm krcrvakskq
      781 aqgkgdsdtr dsekelgrqq pearsagaep dapkkkkkrl pvtcdlcgre fahasgmqyh
      841 kltehfdekp fsceecgakf aanstlknhl rlhtgdrpfm ckhclmtftq asalayhtkk
      901 khsegkmyac qycdavfaqs ielsrhvrth tgdkpyvcrd cgkgfrqang lsihlhtfhn
      961 iedpydckkc rmsfstlqdh rkhihdvhsk eyhpcptcgk ifsapsmler hmvthvggkp
     1021 fscgicnkay qqlsglwyhn rthhpdvfaa qnhrspkfss lqcsscdktf sntiehkkhi
     1081 ktehadlkfh ecgqckelfp tpallqvhvk cqhsgsqpfr clycaatfrf pgalqhhvtt
     1141 ehfkqsestf pcelcgelft sqaqldghle sehpkvtgte tqaaasrmvq viqapepaap
     1201 aeqvitleet qlagsqvfvt lpdpqtsqns selvavtved lldgtvtlic geak
//
LOCUS       NP_001424046             239 aa            linear   ROD 30-MAR-2025
DEFINITION  calcipressin-3 [Rattus norvegicus].
ACCESSION   NP_001424046 XP_006239280
VERSION     NP_001424046.1
DBSOURCE    REFSEQ: accession NM_001437117.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Guasch,A., Aranguren-Ibanez,A., Perez-Luque,R., Aparicio,D.,
            Martinez-Hoyer,S., Mulero,M.C., Serrano-Candelas,E., Perez-Riba,M.
            and Fita,I.
  TITLE     Calcineurin Undergoes a Conformational Switch Evoked via
            Peptidyl-Prolyl Isomerization
  JOURNAL   PLoS One 10 (8), e0134569 (2015)
   PUBMED   26248042
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Canaider,S., Facchin,F., Griffoni,C., Casadei,R., Vitale,L.,
            Lenzi,L., Frabetti,F., D'Addabbo,P., Carinci,P., Zannotti,M. and
            Strippoli,P.
  TITLE     Proteins encoded by human Down syndrome critical region gene 1-like
            2 (DSCR1L2) mRNA and by a novel DSCR1L2 mRNA isoform interact with
            cardiac troponin I (TNNI3)
  JOURNAL   Gene 372, 128-136 (2006)
   PUBMED   16516408
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006239280.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR23984936.226081.1,
                                           SRR26360172.1428134.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..239
                     /product="calcipressin-3"
                     /note="regulator of calcineurin 3; Down syndrome critical
                     region gene 1-like 2"
                     /calculated_mol_wt=27050
     Region          58..225
                     /region_name="Calcipressin"
                     /note="pfam04847"
                     /db_xref="CDD:282674"
     CDS             1..239
                     /gene="Rcan3"
                     /gene_synonym="Dscr1l2"
                     /coded_by="NM_001437117.1:270..989"
                     /db_xref="GeneID:362627"
                     /db_xref="RGD:1311826"
ORIGIN      
        1 mlrdslkswn dsqsdlcssd qeeeeemvfg eneddleemm dlsdlptslf acsvheavfe
       61 vqeqkerfea lftlyddqvt fqlfksfrrv rinfskpeaa ararielhes efhgrklkly
      121 faqvqvsgea rdksyllppq ptkqflispp asppvgwkqs edatpvinyd llcavsklgp
      181 gekyelhagt estpsvvvhv ceseteeeed tknpkqkitq trrpeaptaa lserldcal
//
LOCUS       NP_001100676            1170 aa            linear   ROD 30-MAR-2025
DEFINITION  AF4/FMR2 family member 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001100676 XP_001065599 XP_223161
VERSION     NP_001100676.1
DBSOURCE    REFSEQ: accession NM_001107206.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   Luo,Z., Lin,C. and Shilatifard,A.
  TITLE     The super elongation complex (SEC) family in transcriptional
            control
  JOURNAL   Nat Rev Mol Cell Biol 13 (9), 543-547 (2012)
   PUBMED   22895430
  REMARK    Review article
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Baskaran,K., Erfurth,F., Taborn,G., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A., Iannaccone,P.M. and Domer,P.H.
  TITLE     Cloning and developmental expression of the murine homolog of the
            acute leukemia proto-oncogene AF4
  JOURNAL   Oncogene 15 (16), 1967-1978 (1997)
   PUBMED   9365243
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474022.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223161.4, XP_001065599.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760389, SAMEA5760494
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..1170
                     /product="AF4/FMR2 family member 1 isoform 3"
                     /note="myeloid/lymphoid or mixed-lineage leukemia
                     (trithorax homolog, Drosophila); translocated to, 2;
                     AF4/FMR2 family, member 1"
                     /calculated_mol_wt=127121
     Region          17..515
                     /region_name="AF-4"
                     /note="AF-4 proto-oncoprotein N-terminal region;
                     pfam05110"
                     /db_xref="CDD:461550"
     Region          491..>626
                     /region_name="PHA03418"
                     /note="hypothetical E4 protein; Provisional"
                     /db_xref="CDD:177646"
     Region          <588..720
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          776..790
                     /region_name="AF4_int"
                     /note="AF4 interaction motif; pfam18875"
                     /db_xref="CDD:436798"
     Region          965..>1111
                     /region_name="AF-4_C"
                     /note="AF-4 proto-oncoprotein C-terminal region;
                     pfam18876"
                     /db_xref="CDD:465894"
     CDS             1..1170
                     /gene="Aff1"
                     /gene_synonym="Mllt2"
                     /coded_by="NM_001107206.1:133..3645"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:305152"
                     /db_xref="RGD:1307940"
ORIGIN      
        1 metkirpger gkfaclyned rnllrireke rrnqeahqek eafpekaplf aepyktakgd
       61 elssriqtml gdyeemkefl sskshphrld gsedrpgkpr ypschdrgsg asgsfrthvy
      121 hqpthtsapg slsvsnvsqs pkmaqprmep vpslhakiyg apdgprpaqd rlsqghcsrk
      181 cdrraegdse rklspfissl pspvpplspa hsrpqatska hgsgtgtqsc yaskpskdpv
      241 vtaqeketpl dslvavtslg aappqppcqt fpppplpsks iamqqkptay vrpmdgqdqa
      301 psespelkpp ledfgqqsfe kpdlkvpaka kltrlrmpsq tveqpysnev hcveeilkem
      361 thswpsplta ihtpstaeps rfpfptkdpl hissatqsqk qydapskthp npqqgtsmle
      421 ddlqlsdsee sdveqavekp psppappsap qtipepvasa hsssaesess esdsssdses
      481 essssdseen epletqapep eppttnkwql dnwltkvnqp svplesrgst esprcrqesk
      541 gggegssdqq hpdskdpplk ssskalrgps egpqpgkrnc pkspaqqetp pprqtvgskq
      601 prkptkgstq aeqpqassrv egeagpvayg skeqtskdkp kvktkgrpra vgsrepksev
      661 pvpvpqaavp kpqppaptpi ekrkhkssta pskalsgpqp tkdsagdrnq ehpalvsltq
      721 sqgqpnsgrg sgggrtsgcr qavitqedsc rdklllplrd tkllsplrds ppptslvvki
      781 tldlltrvpq ppgkggrprk sehkqlpagk kqdleargcd sssrvtkkrk aepekehshk
      841 rlrldksqts ssssshaess ksktprpsse csrkemlppp pvvpssssss sssqkpskpa
      901 hkrprpdadi gsqdpprssg stkssctdss vpkhrkvqar dsehkgssgd aanpfpvpsl
      961 pngnskpgkp qvksdrqqad fhmkeakklk ckaeamvdka gkafkyleav lsfiecgmat
     1021 esessaksay tvysetvdli kfvmslksfs dntvpaqeki favlclrcqs llnmamfrck
     1081 kdtvmkysrt lsehfrstsk vaqapspcva rqvhrrsvpr lpnafscqlc wipdecwqqy
     1141 gghggdghrq hpghhpehdl llchhhipcp
//
LOCUS       NP_001178516            1788 aa            linear   ROD 30-MAR-2025
DEFINITION  BCL-6 corepressor-like protein 1 [Rattus norvegicus].
ACCESSION   NP_001178516 XP_002730337 XP_038955598
VERSION     NP_001178516.1
DBSOURCE    REFSEQ: accession NM_001191587.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1788)
  AUTHORS   Xu,Q., Zhu,Q., Zhou,Z., Wang,Y., Liu,X., Yin,G., Tong,X. and Tu,K.
  TITLE     MicroRNA-876-5p inhibits epithelial-mesenchymal transition and
            metastasis of hepatocellular carcinoma by targeting BCL6
            corepressor like 1
  JOURNAL   Biomed Pharmacother 103, 645-652 (2018)
   PUBMED   29679906
  REMARK    Erratum:[Biomed Pharmacother. 2023 Jul;163:114804. doi:
            10.1016/j.biopha.2023.114804. PMID: 37121830]
REFERENCE   2  (residues 1 to 1788)
  AUTHORS   Zhao,X., Tuo,H., Si,M., Wang,L. and Liang,P.
  TITLE     [Expression and clinical significance of BCL6 corepressor-like 1 in
            non-small cell lung cancer]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 31 (12), 1677-1681 (2015)
   PUBMED   26648304
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Mar 27, 2025 this sequence version replaced
            XP_038955598.1, XP_002730337.1.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1788
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..1788
                     /product="BCL-6 corepressor-like protein 1"
                     /calculated_mol_wt=191049
     Region          <201..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1499..1615
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1501..1532
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1502,1506..1507,1510..1512,1514..1515,1519,1523,
                     1532,1534,1536,1540..1541,1544..1546,1548..1549,1553,1556,
                     1565,1567,1569,1573..1574,1577..1579,1581..1582,1586,1589)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1534..1565
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1567..1596
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1669..1782
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Site            order(1671,1673..1683,1685,1687,1696..1698,1700,
                     1741..1742,1744,1747,1769,1780,1782)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1788
                     /gene="Bcorl1"
                     /gene_synonym="RGD1566108"
                     /coded_by="NM_001191587.2:251..5617"
                     /db_xref="GeneID:302810"
                     /db_xref="RGD:1566108"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argtnpdgst teklghrsed qpddpqakmd yvgntaeaeg llvplsspgd
      121 slklptpdgt eashsrancs wtplstqmsk qvdcspagvk aldsrhsvge kntfilatlg
      181 tgvpvegtlp lvttnfsqlp apicppapgs asgtpsvpdp fqvplsvpap vphsglvpvq
      241 vatsasapsp plapvpalap aapsvptlis dsnplsvsas vlvpvpvsap hsvpvplsap
      301 aptpltvsvs applaliqap vppsaptlvl asvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpnqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar plasdsklvs levnrlscts pssstnsqpa
      541 pegvpgplad tslttasakv lptsqpllpa psgssvplhp skmpggtdqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aagsnvtscl gstsspfvif pemvrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk stgvtcgkkg sqvaaegqps
      781 tvksrytpar iapglpgcqt kelslwkptg ltnmyprcsi ngkptstqqv lpvgwspyhq
      841 asllsigiss agqltpsqgv plrptsivse fsgvsslgss eavhglpegq prpggpfape
      901 qdavtknktc riaakpyeeq vnpvlltlsp qtgtlalsvq pnsgdigvnq gseeseshlc
      961 sdstpkvegp qaacglklag dtkpksqvla tymshelvla npqnlckmpe lpllphdshs
     1021 kelildvvps sergpstdls qlgsqvdlgr vkmekadgdv vfnlancfra dglpavpqrg
     1081 qaearakagq arvkregvgv ftcknswqpd eeteslppkk vkcnkekeie eepqqqlppq
     1141 phdkpmvrss vgskcrklpg dpqeptkksp rgaldsgkeh ngvrgkhkhr kptkpeslpa
     1201 gkradgheeg slekkakssf rdfipvvlst rtrsqsgsic ssftgladsd mgsqevfpte
     1261 eeeevaptpa krrkvrktqr dtqyrshhaq dktllsqgrr hlwrarempw rteaarqmwd
     1321 tneeeedeee eglvkrkkrr rqksrkyqtg eylteqeeqr rkgradskar kqktssqsse
     1381 hclrnrdlll sskaqgisds pngflpnnle epaclensek psgkrkcktk hmanvseear
     1441 skgrwsqqkt rssksptpvk ptepctpsky rsagseetse sptarqippe arrlivnkna
     1501 getllqraar lgykdvvlyc lqkhsedvnh rdnagytalh eacsrgwtdi lnillqhgan
     1561 vncssqdgtr pvhdavvndn letiwlllsy gadptlatys gqtamklass dnmkrflsdh
     1621 lsdlqgraeg dpraswdfys ssvlekkdgf acdllhnppg saeqgddseq ddfmfelsdk
     1681 pllpcynlqv svsrgpcnwf lfsdvlkrlk lssrifqarf phleittlpk aefyrqvass
     1741 qlltpaerpg sledrsppgs setvelvqye pellrllgse veyqswss
//
LOCUS       NP_001424064             328 aa            linear   ROD 30-MAR-2025
DEFINITION  putative P2Y purinoceptor 10 [Rattus norvegicus].
ACCESSION   NP_001424064 XP_063136091
VERSION     NP_001424064.1
DBSOURCE    REFSEQ: accession NM_001437135.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Mar 27, 2025 this sequence version replaced XP_063136091.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.21504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663597, SAMN13663609
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..328
                     /product="putative P2Y purinoceptor 10"
                     /note="purinergic receptor P2Y, G-protein coupled, 10;
                     purinergic receptor P2Y10"
                     /calculated_mol_wt=37149
     Region          23..305
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          25..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          58..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          95..117
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          139..155
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          185..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          231..253
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          273..298
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..328
                     /gene="P2ry10"
                     /gene_synonym="RGD1561912"
                     /coded_by="NM_001437135.1:374..1360"
                     /db_xref="GeneID:317219"
                     /db_xref="RGD:1561912"
ORIGIN      
        1 mgsnststve sncnainvtf qnslyattyi fifipgllan saalwvlfrf iskknkaiif
       61 minlsvadla hilslplriy yyinrhwpfq ralcllcfyl kylnmyasif fltcislqrc
      121 lfllkpfrar nwkrrydvgi saavwiivgt aclpfpimrs aglanntdsc fadlgykqmd
      181 plvlvtmiti aelagfvipv ltiacctwkt tvslkhppia fqgiserkka lrmvfmcaav
      241 fvicftpyhi nfifytmvke niitscpivk samyfhpfsl claslcclld pilyyfmase
      301 frdqlsrhgs svtrsrlmsr esgssmvs
//
LOCUS       NP_001424077             174 aa            linear   ROD 30-MAR-2025
DEFINITION  nanos homolog 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424077 XP_006255297
VERSION     NP_001424077.1
DBSOURCE    REFSEQ: accession NM_001437148.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Bhandari,D., Raisch,T., Weichenrieder,O., Jonas,S. and
            Izaurralde,E.
  TITLE     Structural basis for the Nanos-mediated recruitment of the CCR4-NOT
            complex and translational repression
  JOURNAL   Genes Dev 28 (8), 888-901 (2014)
   PUBMED   24736845
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Jorgensen,A., Nielsen,J.E., Blomberg Jensen,M., Graem,N. and
            Rajpert-De Meyts,E.
  TITLE     Analysis of meiosis regulators in human gonads: a sexually
            dimorphic spatio-temporal expression pattern suggests involvement
            of DMRT1 in meiotic entry
  JOURNAL   Mol Hum Reprod 18 (11), 523-534 (2012)
   PUBMED   22899867
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Julaton,V.T. and Reijo Pera,R.A.
  TITLE     NANOS3 function in human germ cell development
  JOURNAL   Hum Mol Genet 20 (11), 2238-2250 (2011)
   PUBMED   21421998
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Suzuki,H., Tsuda,M., Kiso,M. and Saga,Y.
  TITLE     Nanos3 maintains the germ cell lineage in the mouse by suppressing
            both Bax-dependent and -independent apoptotic pathways
  JOURNAL   Dev Biol 318 (1), 133-142 (2008)
   PUBMED   18436203
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Lolicato,F., Marino,R., Paronetto,M.P., Pellegrini,M., Dolci,S.,
            Geremia,R. and Grimaldi,P.
  TITLE     Potential role of Nanos3 in maintaining the undifferentiated
            spermatogonia population
  JOURNAL   Dev Biol 313 (2), 725-738 (2008)
   PUBMED   18089289
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Tsuda,M., Sasaoka,Y., Kiso,M., Abe,K., Haraguchi,S., Kobayashi,S.
            and Saga,Y.
  TITLE     Conserved role of nanos proteins in germ cell development
  JOURNAL   Science 301 (5637), 1239-1241 (2003)
   PUBMED   12947200
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006255297.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2399938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..174
                     /product="nanos homolog 3 isoform 1"
                     /note="nanos homolog 3"
                     /calculated_mol_wt=18615
     Region          57..110
                     /region_name="zf-nanos"
                     /note="Nanos RNA binding domain; pfam05741"
                     /db_xref="CDD:461728"
     CDS             1..174
                     /gene="Nanos3"
                     /coded_by="NM_001437148.1:766..1290"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288909"
                     /db_xref="RGD:1306672"
ORIGIN      
        1 mgtfnlwtdy lglarlvgal heeeepdvrl dpkpepkpss asqqaskess aaperlcsfc
       61 khngesraiy qshvlkdeag rvlcpilrdy vcpqcgatqe hahtrrfcpl tgqgytsvyc
      121 yttrnsagkk ltrpdkaktq naghrlggea aagsksgrkp pgpspsaccp stta
//
LOCUS       NP_001424084            1173 aa            linear   ROD 30-MAR-2025
DEFINITION  polyamine-transporting ATPase 13A2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424084 XP_006239308
VERSION     NP_001424084.1
DBSOURCE    REFSEQ: accession NM_001437155.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   van Veen,S., Martin,S., Van den Haute,C., Benoy,V., Lyons,J.,
            Vanhoutte,R., Kahler,J.P., Decuypere,J.P., Gelders,G., Lambie,E.,
            Zielich,J., Swinnen,J.V., Annaert,W., Agostinis,P., Ghesquiere,B.,
            Verhelst,S., Baekelandt,V., Eggermont,J. and Vangheluwe,P.
  TITLE     ATP13A2 deficiency disrupts lysosomal polyamine export
  JOURNAL   Nature 578 (7795), 419-424 (2020)
   PUBMED   31996848
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Marcos,A.L., Corradi,G.R., Mazzitelli,L.R., Casali,C.I., Fernandez
            Tome,M.D.C., Adamo,H.P. and de Tezanos Pinto,F.
  TITLE     The Parkinson-associated human P5B-ATPase ATP13A2 modifies lipid
            homeostasis
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182993 (2019)
   PUBMED   31132336
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wang,R., Tan,J., Chen,T., Han,H., Tian,R., Tan,Y., Wu,Y., Cui,J.,
            Chen,F., Li,J., Lv,L., Guan,X., Shang,S., Lu,J. and Zhang,Z.
  TITLE     ATP13A2 facilitates HDAC6 recruitment to lysosome to promote
            autophagosome-lysosome fusion
  JOURNAL   J Cell Biol 218 (1), 267-284 (2019)
   PUBMED   30538141
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Bento,C.F., Ashkenazi,A., Jimenez-Sanchez,M. and Rubinsztein,D.C.
  TITLE     The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
            autophagy via a common pathway
  JOURNAL   Nat Commun 7, 11803 (2016)
   PUBMED   27278822
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Kelm-Nelson,C.A., Stevenson,S.A. and Ciucci,M.R.
  TITLE     Atp13a2 expression in the periaqueductal gray is decreased in the
            Pink1 -/- rat model of Parkinson disease
  JOURNAL   Neurosci Lett 621, 75-82 (2016)
   PUBMED   27057733
  REMARK    GeneRIF: Pink1 -/- rats show significantly decreased levels of
            Atp13a2, a transmembrane lysosomal P5-type ATPase suggesting a
            potential mechanism for the observed abnormal aggregation.
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Ramonet,D., Podhajska,A., Stafa,K., Sonnay,S., Trancikova,A.,
            Tsika,E., Pletnikova,O., Troncoso,J.C., Glauser,L. and Moore,D.J.
  TITLE     PARK9-associated ATP13A2 localizes to intracellular acidic vesicles
            and regulates cation homeostasis and neuronal integrity
  JOURNAL   Hum Mol Genet 21 (8), 1725-1743 (2012)
   PUBMED   22186024
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Tan,J., Zhang,T., Jiang,L., Chi,J., Hu,D., Pan,Q., Wang,D. and
            Zhang,Z.
  TITLE     Regulation of intracellular manganese homeostasis by Kufor-Rakeb
            syndrome-associated ATP13A2 protein
  JOURNAL   J Biol Chem 286 (34), 29654-29662 (2011)
   PUBMED   21724849
  REMARK    GeneRIF: Regulation of intracellular manganese homeostasis by
            Kufor-Rakeb syndrome-associated ATP13A2 protein.
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Park,J.S., Mehta,P., Cooper,A.A., Veivers,D., Heimbach,A.,
            Stiller,B., Kubisch,C., Fung,V.S., Krainc,D., Mackay-Sim,A. and
            Sue,C.M.
  TITLE     Pathogenic effects of novel mutations in the P-type ATPase ATP13A2
            (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset
            parkinsonism
  JOURNAL   Hum Mutat 32 (8), 956-964 (2011)
   PUBMED   21542062
REFERENCE   9  (residues 1 to 1173)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   10 (residues 1 to 1173)
  AUTHORS   Ramirez,A., Heimbach,A., Grundemann,J., Stiller,B., Hampshire,D.,
            Cid,L.P., Goebel,I., Mubaidin,A.F., Wriekat,A.L., Roeper,J.,
            Al-Din,A., Hillmer,A.M., Karsak,M., Liss,B., Woods,C.G.,
            Behrens,M.I. and Kubisch,C.
  TITLE     Hereditary parkinsonism with dementia is caused by mutations in
            ATP13A2, encoding a lysosomal type 5 P-type ATPase
  JOURNAL   Nat Genet 38 (10), 1184-1191 (2006)
   PUBMED   16964263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006239308.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20921.1,
                                           SRR26643290.21177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1173
                     /product="polyamine-transporting ATPase 13A2 isoform 1"
                     /EC_number="7.2.2.10"
                     /note="probable cation-transporting ATPase 13A2; ATPase
                     type 13A2; polyamine-transporting ATPase 13A2"
                     /calculated_mol_wt=127472
     Region          39..1116
                     /region_name="P-ATPase-V"
                     /note="P-type ATPase of unknown pump specificity (type V);
                     TIGR01657"
                     /db_xref="CDD:273738"
     CDS             1..1173
                     /gene="Atp13a2"
                     /gene_synonym="RGD1307977"
                     /coded_by="NM_001437155.1:168..3689"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362645"
                     /db_xref="RGD:1307977"
ORIGIN      
        1 msadsspllg stppsygtlm tgtsidplss svssvrlsgy cgspwraigy haavwmlagi
       61 pwllfrwkpl wgvrlrlrpc slaraetlvi eirdkegssr qlftvqvqte avvdgslelp
      121 sqakaedgrs laavgvapes mwqdttqlhr qkeakqvlry yilqgqryvw metqqafcqv
      181 slldhgracd dihcsssgls lqdqavrkti ygpnvigipv ksylqllvde alnpyygfqa
      241 fsialwladh yywyavcifl isaisiclsl yktrkqsmtl rdmvklsvrv qvcrpggeee
      301 wvdsselvpg dclvlpqegg mmpcdaalva gecvvnessl tgesipvlkt alpegpqpyc
      361 pethrrhtlf cgtlvlqara ylgprvlavv trtgfctakg glvssilhpr pisfkfyrhs
      421 mkfvaalsvl allgtiysii ilyrnrvpvk eiviraldlv tvvvppalpa amtvctlyaq
      481 srlrtqgifc ihplrinlgg klrlvcfdkt gtltedgldi mgvvplkgqm llplvpepch
      541 lppgpllral vtchalsqlh dtlvgdpmdl kmvestgwvl eegsaagsap etqvlvvmrp
      601 pprgpqqqee spepvsvlrr fpfssalqrm dvvvtwpgat qpeayvkgsp elvaslcspe
      661 tvprdfpqvl qsytaagyrv valagkplpt apsleaaqql trdtveqels llgllvmrnl
      721 lkpqttpviq tlrktgirtv mvtgdnlqta vtvakacgmv gtqehlaiih athpeqgqpa
      781 aleflpteps aamngakdpv qatdypvepe sqsrhlalsg stfavlqkhf pkllpkvlvq
      841 atvfarmape qktqlvcelq rlqycvgmcg dgandcgalk aadvgislsq aeasvvspft
      901 ssmasiecvp tviregrcsl dtsfsvfkym alysltqfis vlilytintn lgdlqflaid
      961 lfitttvavl msrtgpaltl vrarppgall svpvlgslll qvalvagiql ggyflviaqp
     1021 wfvplnrtvp apdnlpnyen tvifslsgfq ylilaaavsk gapfrqplyt nvpflvalal
     1081 lgsvlvglil vpgllqgplg lrniadssfk llllglvafn fvgafmlesv ldqclpaclq
     1141 wlrpkraskk qfkqlqrela erpwptlpvg svr
//
LOCUS       NP_001424070             142 aa            linear   ROD 30-MAR-2025
DEFINITION  putative uncharacterized protein CIMIP3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424070 XP_038940428
VERSION     NP_001424070.1
DBSOURCE    REFSEQ: accession NM_001437141.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038940428.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.413344.1,
                                           SRR26360190.782975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..142
                     /product="putative uncharacterized protein CIMIP3 isoform
                     3"
                     /note="Guca1a neighbor"
                     /calculated_mol_wt=16426
     CDS             1..142
                     /gene="Cimip3"
                     /gene_synonym="Guca1anb"
                     /coded_by="NM_001437141.1:87..515"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:100912849"
                     /db_xref="RGD:6485345"
ORIGIN      
        1 mlkiidtkdg srgchyqkwt lertekesqk slipghrqkt tsgrkgkkvp pptptplsqk
       61 wkrdrkqsle sayvpvvvdp rgqepdssfr fnfynsqysn slnpfytlqk ptcgylyqre
      121 tdhtrkcfgi ppanlvlwrs ty
//
LOCUS       NP_001424074              59 aa            linear   ROD 30-MAR-2025
DEFINITION  single-pass membrane and coiled-coil domain-containing protein 4
            [Rattus norvegicus].
ACCESSION   NP_001424074 XP_017451213
VERSION     NP_001424074.1
DBSOURCE    REFSEQ: accession NM_001437145.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 27, 2025 this sequence version replaced XP_017451213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.575308.1,
                                           SRR26360186.736926.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..59
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..59
                     /product="single-pass membrane and coiled-coil
                     domain-containing protein 4"
                     /calculated_mol_wt=6605
     Region          1..55
                     /region_name="DUF4519"
                     /note="Domain of unknown function (DUF4519); pfam15012"
                     /db_xref="CDD:464444"
     CDS             1..59
                     /gene="Smco4"
                     /gene_synonym="RGD1309410"
                     /coded_by="NM_001437145.1:220..399"
                     /db_xref="GeneID:363020"
                     /db_xref="RGD:1309410"
ORIGIN      
        1 mrqlkgkpkk etskdkkerk qamqearqqi ttvvlptlav vvllivvfvy vatrpivte
//
LOCUS       NP_001424092             806 aa            linear   ROD 30-MAR-2025
DEFINITION  rho guanine nucleotide exchange factor 19 [Rattus norvegicus].
ACCESSION   NP_001424092 XP_038966353
VERSION     NP_001424092.1
DBSOURCE    REFSEQ: accession NM_001437163.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Caddy,J., Wilanowski,T., Darido,C., Dworkin,S., Ting,S.B., Zhao,Q.,
            Rank,G., Auden,A., Srivastava,S., Papenfuss,T.A., Murdoch,J.N.,
            Humbert,P.O., Parekh,V., Boulos,N., Weber,T., Zuo,J.,
            Cunningham,J.M. and Jane,S.M.
  TITLE     Epidermal wound repair is regulated by the planar cell polarity
            signaling pathway
  JOURNAL   Dev Cell 19 (1), 138-147 (2010)
   PUBMED   20643356
  REMARK    Erratum:[Dev Cell. 2010 Aug 17;19(2):353. Parekh, Vishwas [added]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_038966353.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.2158715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..806
                     /product="rho guanine nucleotide exchange factor 19"
                     /note="Rho guanine nucleotide exchange factor (GEF) 19"
                     /calculated_mol_wt=89335
     Region          386..562
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          584..710
                     /region_name="PH_ephexin"
                     /note="Ephexin Pleckstrin homology (PH) domain; cd01221"
                     /db_xref="CDD:269929"
     Region          723..777
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(728,730,733,737,755..756,771,773..774)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     CDS             1..806
                     /gene="Arhgef19"
                     /coded_by="NM_001437163.1:92..2512"
                     /db_xref="GeneID:362648"
                     /db_xref="RGD:1304766"
ORIGIN      
        1 mdcgppatlq phlagppgta rrpvavcqqe slsfvelptl hppspvcvdl fpitpeelqa
       61 pgsrwslatp aplqgllwpt ssggpdthis ttggmrpsra gswphcpgaq pptlvgpwss
      121 qhmqpqrras hggseksawr kmqvyhneea tggteppmgl letgqavqgq alcaqeprpq
      181 elsgntrggl eaqerrrfsa selmtrlhss lrlgrstapr altsgsgagv iregklpgre
      241 prraetrmds vslpapvdln evqgglvepr ldtndkptqd tnsaterrqs rfllnsvlyq
      301 eysdvasare lrrqqreeeg pgdgaegaee gpgppranls psssfraqrs trgstfslwq
      361 dipdvrgsgv latlslrdck lqeakfelit seasyihsls vavghflgsv elseclgtqd
      421 kqwlfsklpe vkstserflh dleqrleadv lrfsvcdvvl hhcpafrrvy lpyvtnqayq
      481 ertyqrllle npkfpgilar leespvcqrl pltsflilpf qrvtrlkmlv enilkrttpg
      541 sqdedmatka fsalkelvqe cnasvqsmkr teelihlskk ihfegkifpl isqarwlvrh
      601 gelvelaplp aappaklkls skavylhlfn dclllsrrke lgkfavfvha nmaelqvrdl
      661 slklqgipgh vfllrllhgq rarhqlllra rtesekqrwi salrpsspqe dkeitcdged
      721 rpqvqcvrty kalqpdeltl ektdilavkt rtsdgwlegv rladgekgwv pqahveeiss
      781 lsarlrnlre ykrvsnvssk lgdppa
//
LOCUS       NP_001012230             448 aa            linear   ROD 31-MAR-2025
DEFINITION  XK-related protein 2 [Rattus norvegicus].
ACCESSION   NP_001012230 XP_577015
VERSION     NP_001012230.1
DBSOURCE    REFSEQ: accession NM_001012230.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Apr 20, 2005 this sequence version replaced XP_577015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.68360.1, AY534257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680416, SAMN06680419
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..448
                     /product="XK-related protein 2"
                     /note="X Kell blood group precursor related X linked; XK,
                     Kell blood group complex subunit-related, X-linked"
                     /calculated_mol_wt=51917
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Region          35..406
                     /region_name="XK-related"
                     /note="XK-related protein; pfam09815"
                     /db_xref="CDD:462912"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH60.1)"
     CDS             1..448
                     /gene="Xkrx"
                     /gene_synonym="XRG2"
                     /coded_by="NM_001012230.2:1146..2492"
                     /db_xref="GeneID:497101"
                     /db_xref="RGD:1359223"
ORIGIN      
        1 mdrvyeipee pnvvpiasle dvirgpnprf tfpfsilfst flycgeaasa lymvriyrkn
       61 netfwmtytf sffmfssimv qltlifvhrd lakdrplslf mhlillgpvi rcleamikyl
      121 tlwkkegqee pyvsltrkkm lidgqevlie wevghsirtl amhrnaykrm sqiqaflgsv
      181 pqltyqlyvt lisaevplgr avlmffslis vtygatlcnm laiqikyddy kirlgpvevl
      241 citiwrtlei tsrlmilvlf satlklkavp flvlnfliil fepwvkfwrs gaqmpnniek
      301 nfsrvgtlvv lisvtilyag infscwsamq lkladrdlvd kgqnwghmgl hysvrlvenv
      361 imvlvfkyfg vkvllnyshs lmaiqliiay lisigfmllf fqylhplrsl fthnvvdylh
      421 ciccrrhhre rvensetsce pdtrqsiv
//
LOCUS       NP_001424133             730 aa            linear   ROD 31-MAR-2025
DEFINITION  YTH domain-containing protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424133 XP_006250868
VERSION     NP_001424133.1
DBSOURCE    REFSEQ: accession NM_001437204.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Yu,Z., Xia,Y., Li,J., Jiang,J., Li,Y., Li,Y. and Wang,L.
  TITLE     METTL3 mediates m6A modification of lncRNA CRNDE to promote ATG10
            expression and improve brain ischemia/reperfusion injury through
            YTHDC1
  JOURNAL   Biol Direct 19 (1), 92 (2024)
   PUBMED   39407279
  REMARK    GeneRIF: METTL3 mediates m6A modification of lncRNA CRNDE to
            promote ATG10 expression and improve brain ischemia/reperfusion
            injury through YTHDC1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Lin,W., Liu,Y., Zhou,Y., Lin,M., Liu,C., Tang,Y., Wu,B. and Lin,C.
  TITLE     Methyltransferase-like 3 modulates visceral hypersensitivity
            through regulating the nuclear export of circKcnk9 in
            YTHDC1-dependent manner
  JOURNAL   Mol Pain 18, 17448069221144540 (2022)
   PUBMED   36443649
  REMARK    GeneRIF: Methyltransferase-like 3 modulates visceral
            hypersensitivity through regulating the nuclear export of circKcnk9
            in YTHDC1-dependent manner.
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Zhang,Z., Wang,Q., Zhao,X., Shao,L., Liu,G., Zheng,X., Xie,L.,
            Zhang,Y., Sun,C. and Xu,R.
  TITLE     YTHDC1 mitigates ischemic stroke by promoting Akt phosphorylation
            through destabilizing PTEN mRNA
  JOURNAL   Cell Death Dis 11 (11), 977 (2020)
   PUBMED   33188203
  REMARK    GeneRIF: YTHDC1 mitigates ischemic stroke by promoting Akt
            phosphorylation through destabilizing PTEN mRNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Kasowitz,S.D., Ma,J., Anderson,S.J., Leu,N.A., Xu,Y., Gregory,B.D.,
            Schultz,R.M. and Wang,P.J.
  TITLE     Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
            splicing during mouse oocyte development
  JOURNAL   PLoS Genet 14 (5), e1007412 (2018)
   PUBMED   29799838
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Shima,H., Matsumoto,M., Ishigami,Y., Ebina,M., Muto,A., Sato,Y.,
            Kumagai,S., Ochiai,K., Suzuki,T. and Igarashi,K.
  TITLE     S-Adenosylmethionine Synthesis Is Regulated by Selective
            N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and
            YTHDC1
  JOURNAL   Cell Rep 21 (12), 3354-3363 (2017)
   PUBMED   29262316
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Heinrich,B., Zhang,Z., Raitskin,O., Hiller,M., Benderska,N.,
            Hartmann,A.M., Bracco,L., Elliott,D., Ben-Ari,S., Soreq,H.,
            Sperling,J., Sperling,R. and Stamm,S.
  TITLE     Heterogeneous nuclear ribonucleoprotein G regulates splice site
            selection by binding to CC(A/C)-rich regions in pre-mRNA
  JOURNAL   J Biol Chem 284 (21), 14303-14315 (2009)
   PUBMED   19282290
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   8  (residues 1 to 730)
  AUTHORS   Nayler,O., Hartmann,A.M. and Stamm,S.
  TITLE     The ER repeat protein YT521-B localizes to a novel subnuclear
            compartment
  JOURNAL   J Cell Biol 150 (5), 949-962 (2000)
   PUBMED   10973987
REFERENCE   9  (residues 1 to 730)
  AUTHORS   Hartmann,A.M., Nayler,O., Schwaiger,F.W., Obermeier,A. and Stamm,S.
  TITLE     The interaction and colocalization of Sam68 with the
            splicing-associated factor YT521-B in nuclear dots is regulated by
            the Src family kinase p59(fyn)
  JOURNAL   Mol Biol Cell 10 (11), 3909-3926 (1999)
   PUBMED   10564280
REFERENCE   10 (residues 1 to 730)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250868.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.559084.1,
                                           SRR26643289.34675.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..730
                     /product="YTH domain-containing protein 1 isoform 4"
                     /note="YTH domain-containing protein 1; RA301-binding
                     protein; putative splicing factor YT521; splicing factor
                     YT521-B; YTH domain containing 1"
                     /calculated_mol_wt=84884
     Region          1..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          359..495
                     /region_name="YTH"
                     /note="YTH (YT521-B homology) domains are RNA-binding
                     domains that belong to the PUA superfamily; cd21134"
                     /db_xref="CDD:410979"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          512..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96MU7; propagated from
                     UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          610..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     Region          672..730
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY02.2)"
     CDS             1..730
                     /gene="Ythdc1"
                     /gene_synonym="Yt521"
                     /coded_by="NM_001437204.1:288..2480"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:170956"
                     /db_xref="RGD:621706"
ORIGIN      
        1 maadsreekd gelnvlddil tevpeqddel ynpeseqdkn ekkgskrkse rmesidtkrq
       61 kpsihsrqli skplsssvsn nkrivstkgk svteykneey qrsernkrld adrkirlsss
      121 ssrepyksqp ekpclrkrds erraksptpd gseriglevd rrasrssqss keegnseeyg
      181 sdhetgssas seqgnntene eeggeedvee deevdedgdd deevdedaee eedeeedeee
      241 edeeeeeeee eeyeqderdq keegndydtr seasdsgses vsftdgsvrs gsgtdgsdek
      301 kkerkrargi spivfdrsgs sasesyagse kkheklsssv ravrkdqtsk lkyvlqdarf
      361 fliksnnhen vslakakgvw stlpvnekkl nlafrsarsv ilifsvresg kfqgfarlss
      421 eshhggspih wvlpagmsak mlggvfkidw icrrelpftk sahltnpwne hkpvkigrdg
      481 qeielecgtq lcllfppdes idlyqlihkm rhkrrmhsqp rsrgrpsrre pvrdvgrrrp
      541 edydihnsrk kpridyppef hqrpgylkdp ryqevdrrfs gvrrdvflng syndyvrefh
      601 nmgppppwqg mppypgieqp phhpyyqhha pppqahppys ghhpvphear yrdkrvhdyd
      661 mrvddflrrt qavvsgrrsr prerdrerer drprdnrrdr erdrgrdrer erericdrdr
      721 drgergryrr
//
LOCUS       NP_001424110             173 aa            linear   ROD 31-MAR-2025
DEFINITION  transmembrane protein 240 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424110
VERSION     NP_001424110.1
DBSOURCE    REFSEQ: accession NM_001437181.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Trinidad,J.C., Barkan,D.T., Gulledge,B.F., Thalhammer,A., Sali,A.,
            Schoepfer,R. and Burlingame,A.L.
  TITLE     Global identification and characterization of both O-GlcNAcylation
            and phosphorylation at the murine synapse
  JOURNAL   Mol Cell Proteomics 11 (8), 215-229 (2012)
   PUBMED   22645316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2131922.1,
                                           SRR26360194.1357990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..173
                     /product="transmembrane protein 240 isoform 1"
                     /calculated_mol_wt=19874
     Region          1..173
                     /region_name="TMEM240"
                     /note="TMEM240 family; pfam15207"
                     /db_xref="CDD:405814"
     CDS             1..173
                     /gene="Tmem240"
                     /coded_by="NM_001437181.1:287..808"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100362471"
                     /db_xref="RGD:2318117"
ORIGIN      
        1 msmsantmif milgasivma iaclmdmnal ldrfhnyilp hlrgedrvch cncgrhhihy
       61 vipydgdqsv vdasenyfvt dnvtkqeidl mlglllgfci swflvwmdgv lhcavrawra
      121 grrydgswtw lpklcslrel grrphrpfee ptgnmvhvkq klyhnghpsp rhl
//
LOCUS       NP_001424144             545 aa            linear   ROD 31-MAR-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001424144 XP_006250949
VERSION     NP_001424144.1
DBSOURCE    REFSEQ: accession NM_001437215.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Qu,S.Q., Ai,X.F., Li,C.W., Li,Q.H., Xu,Z.F., Qin,T.J., Zhang,Y. and
            Xiao,Z.J.
  TITLE     [Characteristics of cytogenetics and molecular biology in patients
            with eosinophilia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 20 (5), 1216-1220 (2012)
   PUBMED   23114151
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Arefi,M., Garcia,J.L., Briz,M.M., de Arriba,F., Rodriguez,J.N.,
            Martin-Nunez,G., Martinez,J., Lopez,J., Suarez,J.G., Moreno,M.J.,
            Merino,M.A., Gutierrez,N.C. and Hernandez-Rivas,J.M.
  TITLE     Response to imatinib mesylate in patients with hypereosinophilic
            syndrome
  JOURNAL   Int J Hematol 96 (3), 320-326 (2012)
   PUBMED   22806436
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Chan,S., Choi,E.A. and Shi,Y.
  TITLE     Pre-mRNA 3'-end processing complex assembly and function
  JOURNAL   Wiley Interdiscip Rev RNA 2 (3), 321-335 (2011)
   PUBMED   21957020
  REMARK    Review article
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Kiefer,H., Mizutani,A., Iemura,S., Natsume,T., Ando,H., Kuroda,Y.
            and Mikoshiba,K.
  TITLE     Inositol 1,4,5-triphosphate receptor-binding protein released with
            inositol 1,4,5-triphosphate (IRBIT) associates with components of
            the mRNA 3' processing machinery in a phosphorylation-dependent
            manner and inhibits polyadenylation
  JOURNAL   J Biol Chem 284 (16), 10694-10705 (2009)
   PUBMED   19224921
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250949.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2333461.1,
                                           SRR26360190.1818591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..545
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     6"
                     /note="pre-mRNA 3'-end-processing factor FIP1; FIP1-like 1
                     protein"
                     /calculated_mol_wt=60929
     Region          1..296
                     /region_name="Necessary for stimulating PAPOLA activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          1..110
                     /region_name="Sufficient for interaction with PAPOLA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          136..219
                     /region_name="Sufficient for interaction with CPSF4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          153..195
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     Region          212..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          392..545
                     /region_name="Sufficient for interaction with CPSF1 and
                     CSTF3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Region          406..441
                     /region_name="Arg/Asp/Glu-rich domain.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6UN15; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U317.1)"
     CDS             1..545
                     /gene="Fip1l1"
                     /coded_by="NM_001437215.1:203..1840"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:289582"
                     /db_xref="RGD:1309336"
ORIGIN      
        1 msageverlv elsggtggde eeewlyggpw dvhvhsdlak dldeneverp eeenasanpp
       61 sgieeeaaen gvakpkvtet eddsdsdsdd deddvhvtig diktgapqyg sygtapvnln
      121 ikaggrvygn tgtkvkgvdl dapgsingvp llevdldsfe dkpwrkpgad lsdyfnygfn
      181 edtwkaycek qkrirmglev ipvtsttnki tvqqgrtgns ekeaalpstk aeftsppslf
      241 ktglppsrrl pgaidvigqt itisrvegrr ranensniqv lsdrsatevd nnfskpppff
      301 ppgappthlp pppflppppt vstapplipp pgipitvppp gfppppgapp psliptiesg
      361 hssgydsrsa rafpygnvaf phltssapsw pslvdttkqw dyyarrekdr drdrerdrdr
      421 ererdrdrer ertrererer dhsptpsvfn sdeeryryre yaergyerhr asrekeerhr
      481 errhrekeet rhkssrsnsr rrheseegds hrrhkhkksk rskegkeags epvpeqeste
      541 aapae
//
LOCUS       NP_001424033             374 aa            linear   ROD 31-MAR-2025
DEFINITION  ecto-ADP-ribosyltransferase 3 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424033 XP_006250789
VERSION     NP_001424033.1
DBSOURCE    REFSEQ: accession NM_001437104.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Shi,W., Gong,P., Fan,J., Yan,Y.H., Ni,L., Wu,X., Cui,G., Wu,X.,
            Gu,X. and Chen,J.
  TITLE     The expression pattern of ADP-ribosyltransferase 3 in rat traumatic
            brain injury
  JOURNAL   J Mol Histol 43 (1), 37-47 (2012)
   PUBMED   22037978
  REMARK    GeneRIF: ART3 may play important roles in CNS pathophysiology after
            traumatic brain injury (TBI).
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Wang,B., Golemis,E.A. and Kruh,G.D.
  TITLE     ArgBP2, a multiple Src homology 3 domain-containing,
            Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed
            cells and localized in stress fibers and cardiocyte Z-disks
  JOURNAL   J Biol Chem 272 (28), 17542-17550 (1997)
   PUBMED   9211900
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Koch-Nolte,F., Haag,F., Braren,R., Kuhl,M., Hoovers,J.,
            Balasubramanian,S., Bazan,F. and Thiele,H.G.
  TITLE     Two novel human members of an emerging mammalian gene family
            related to mono-ADP-ribosylating bacterial toxins
  JOURNAL   Genomics 39 (3), 370-376 (1997)
   PUBMED   9119374
  REMARK    Erratum:[Genomics 1999 Jan 1;55(1):130]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006250789.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223913.1, FQ224878.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..374
                     /product="ecto-ADP-ribosyltransferase 3 isoform 1
                     precursor"
                     /EC_number="2.4.2.31"
                     /note="ecto-ADP-ribosyltransferase 3"
                     /calculated_mol_wt=38806
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2925
     Region          29..251
                     /region_name="VIP2"
                     /note="A family of actin-ADP-ribosylating toxin. A member
                     of the Bacillus-prodiced vegetative insecticidal proteins
                     (VIPs) possesses high specificity against the major insect
                     pest, corn rootworms, and belongs to a classs of binary
                     toxins and regulators of...; cl00173"
                     /db_xref="CDD:469640"
     CDS             1..374
                     /gene="Art3"
                     /coded_by="NM_001437104.1:123..1247"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:305235"
                     /db_xref="RGD:628833"
ORIGIN      
        1 mkmghfelvt tllaamvlmd vfqvqaevld maenvfddey lkcnsrmemk yiprmhgeel
       61 andellqsvw dkagiqweaq kaqlslpknf kdaygialta yvteaqdqsp fyhtfnravk
      121 iaglsrrryi ynfpfkafhf ylvralqllr rpceesyknv vystspnisf afgeqnqarl
      181 gnftlaysak pqtaneqrll tiqtcfgvav gkllnkeseg ivliplsevf qvsrkgtddd
      241 lilhsinstc syyecsflgg lkagscttnp enpdpgylnn pdldsqkled sgrksldsvk
      301 mpeikvlqge enpllpdekp edrnrgkanv ptpglvpvpg pkshpssssg hrllpsdtas
      361 tilliaaavd fial
//
LOCUS       NP_001424137             621 aa            linear   ROD 31-MAR-2025
DEFINITION  kelch-like protein 8 [Rattus norvegicus].
ACCESSION   NP_001424137 XP_008768227
VERSION     NP_001424137.1
DBSOURCE    REFSEQ: accession NM_001437208.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_008768227.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.53831.1,
                                           SRR26360190.2770607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..621
                     /product="kelch-like protein 8"
                     /note="kelch-like 8"
                     /calculated_mol_wt=68437
     Region          53..172
                     /region_name="BTB_POZ_KLHL8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 8 (KLHL8); cd18238"
                     /db_xref="CDD:349547"
     Region          61..536
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          357..400
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          404..448
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          451..496
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          498..543
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..587
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          556..601
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..621
                     /gene="Klhl8"
                     /coded_by="NM_001437208.1:510..2375"
                     /db_xref="GeneID:289457"
                     /db_xref="RGD:1304685"
ORIGIN      
        1 masestngkl arshvtkgrr qqqqqqqvrs rssvsecdgd dsfifeanea wkdfhgsllg
       61 fyengelcdv tlkvgsklis chklalacvi pyframflse mseakqalie irdfdgdave
      121 dlvkfvyssr ltltvdnvqp llyaacilqv elvaraccey mklhfhpsnc lavrafaesh
      181 nrtdlmdmad qyacehftev vecedfvsvs pqhlhkllss sdlnidsekq vysaaikwll
      241 anpqhhpkwl detlaqvrlp llpvdflmgv vakeqivkqn lkcrdlldea rnyhlhlssk
      301 pvpdfeysvr ttprkhtagv lfcvggrggs gdpfrsiecy sintnswffg pemnsrrrhv
      361 gvisvegkvy avgghdgneh lgsmemfdpl tnkwmvkasm ntkrrgiala slggpiyaig
      421 glddntcfsd verydiesdq wstvapmntp rggvgsvali nhvyavggnd gvaslssver
      481 yhphldkwve vkemgqrrag ngvselhgcl yvvggfddns plssverydp rsnkwdyvaa
      541 lttprggvgi atvmgkifav gghngnayln tveafdpvln kwelvgpvsh cragagvavc
      601 dcltsqirdv ghgstnvvdc m
//
LOCUS       NP_113868                361 aa            linear   ROD 31-MAR-2025
DEFINITION  P2Y purinoceptor 4 [Rattus norvegicus].
ACCESSION   NP_113868
VERSION     NP_113868.1
DBSOURCE    REFSEQ: accession NM_031680.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Dosh,R.H., Khalfa,H.M., Al-Rehemi,S.M., Almsaid,H.L. and Hadi,N.
  TITLE     IN VIVO ACTIVATION OF P2Y4 PURINERGIC RECEPTORS USING ATP IN RAT
            EPIDERMAL TISSUE
  JOURNAL   Wiad Lek 75 (11 pt 2), 2729-2733 (2022)
   PUBMED   36591760
  REMARK    GeneRIF: IN VIVO ACTIVATION OF P2Y4 PURINERGIC RECEPTORS USING ATP
            IN RAT EPIDERMAL TISSUE.
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Szrejder,M., Rachubik,P., Rogacka,D., Audzeyenka,I., Rychlowski,M.,
            Angielski,S. and Piwkowska,A.
  TITLE     Extracellular ATP modulates podocyte function through P2Y
            purinergic receptors and pleiotropic effects on AMPK and cAMP/PKA
            signaling pathways
  JOURNAL   Arch Biochem Biophys 695, 108649 (2020)
   PUBMED   33122160
  REMARK    GeneRIF: Extracellular ATP modulates podocyte function through P2Y
            purinergic receptors and pleiotropic effects on AMPK and cAMP/PKA
            signaling pathways.
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Gohar,E.Y., Kasztan,M., Becker,B.K., Speed,J.S. and Pollock,D.M.
  TITLE     Ovariectomy uncovers purinergic receptor activation of
            endothelin-dependent natriuresis
  JOURNAL   Am J Physiol Renal Physiol 313 (2), F361-F369 (2017)
   PUBMED   28468962
  REMARK    GeneRIF: Activation of renal medullary P2Y2/P2Y4 receptors promotes
            ET-1-dependent natriuresis in ovariectomized rats.
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Anikina,T.A., Anisimova,I.N., Zverev,A.A., Sitdikov,F.G. and
            Zefirov,T.L.
  TITLE     Involvement of P2Y(2,4) receptors in the regulation of myocardial
            contractility in growing rats
  JOURNAL   Bull Exp Biol Med 156 (3), 299-302 (2014)
   PUBMED   24771361
  REMARK    GeneRIF: in 100-day-old animals, the myocardial inotropic response
            to the administration of uridine triphosphate was mediated by R2Y2
            receptors. R2Y4 receptors took part in the realization of negative
            inotropic response to uridine triphosphate in all age groups
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Traves,P.G., Pimentel-Santillana,M., Carrasquero,L.M.,
            Perez-Sen,R., Delicado,E.G., Luque,A., Izquierdo,M.,
            Martin-Sanz,P., Miras-Portugal,M.T. and Bosca,L.
  TITLE     Selective impairment of P2Y signaling by prostaglandin E2 in
            macrophages: implications for Ca2+-dependent responses
  JOURNAL   J Immunol 190 (8), 4226-4235 (2013)
   PUBMED   23479225
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Dranoff,J.A., Masyuk,A.I., Kruglov,E.A., LaRusso,N.F. and
            Nathanson,M.H.
  TITLE     Polarized expression and function of P2Y ATP receptors in rat bile
            duct epithelia
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 281 (4), G1059-G1067 (2001)
   PUBMED   11557527
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Lazarowski,E.R., Rochelle,L.G., O'Neal,W.K., Ribeiro,C.M.,
            Grubb,B.R., Zhang,V., Harden,T.K. and Boucher,R.C.
  TITLE     Cloning and functional characterization of two murine uridine
            nucleotide receptors reveal a potential target for correcting ion
            transport deficiency in cystic fibrosis gallbladder
  JOURNAL   J Pharmacol Exp Ther 297 (1), 43-49 (2001)
   PUBMED   11259526
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Suarez-Huerta,N., Pouillon,V., Boeynaems,J. and Robaye,B.
  TITLE     Molecular cloning and characterization of the mouse P2Y4 nucleotide
            receptor
  JOURNAL   Eur J Pharmacol 416 (3), 197-202 (2001)
   PUBMED   11290369
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Webb,T.E., Henderson,D.J., Roberts,J.A. and Barnard,E.A.
  TITLE     Molecular cloning and characterization of the rat P2Y4 receptor
  JOURNAL   J Neurochem 71 (4), 1348-1357 (1998)
   PUBMED   9751165
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Bogdanov,Y.D., Wildman,S.S., Clements,M.P., King,B.F. and
            Burnstock,G.
  TITLE     Molecular cloning and characterization of rat P2Y4 nucleotide
            receptor
  JOURNAL   Br J Pharmacol 124 (3), 428-430 (1998)
   PUBMED   9647463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y11433.1, SRR26643295.61063.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..361
                     /product="P2Y purinoceptor 4"
                     /note="pyrimidinergic receptor P2Y, G-protein coupled, 4;
                     purinergic receptor P2Y, G-protein coupled 4; P2Y ATP
                     receptor 4"
                     /calculated_mol_wt=40763
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Site            31..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Region          32..313
                     /region_name="7tmA_P2Y4"
                     /note="P2Y purinoceptor 4, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15374"
                     /db_xref="CDD:320496"
     Region          32..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320496"
     Region          66..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320496"
     Site            69..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Site            order(87,90..91,104..109,111..112,115,160,162..166,180,
                     182..184,193,196..198,200..202,204..205,254,257..258,
                     260..261,264,280..281,283..285,288,291..292)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320496"
     Region          104..134
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320496"
     Site            109..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Region          146..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320496"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35811.1)"
     Region          193..222
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320496"
     Site            193..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Region          234..264
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320496"
     Site            243..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     Region          281..306
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320496"
     Site            284..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35811.1)"
     CDS             1..361
                     /gene="P2ry4"
                     /gene_synonym="P2Y4"
                     /coded_by="NM_031680.2:84..1169"
                     /db_xref="GeneID:63843"
                     /db_xref="RGD:61798"
ORIGIN      
        1 mtsaesllft slgpspssgd gdcrfneefk fillpmsyav vfvlglalna ptlwlflfrl
       61 rpwdatatym fhlalsdtly vlslptlvyy yaarnhwpfg tglckfvrfl fywnlycsvl
      121 fltcisvhry lgichplrai rwgrprfasl lclgvwlvva gclvpnlffv ttnangttil
      181 chdttlpeef dhyvyfssav mvllfglpfl itlvcyglma rrlyrplpga gqsssrlrsl
      241 rtiavvltvf avcfvpfhit rtiyyqarll qadchvlniv nvvykvtrpl asanscldpv
      301 lylftgdkyr nqlqqlcrgs kpkprtaass lalvtlhees isrwadthqd stfsayegdr
      361 l
//
LOCUS       NP_001156991             194 aa            linear   ROD 11-SEP-2014
DEFINITION  coiled-coil domain-containing protein 166 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001156991 XP_001074627
VERSION     NP_001156991.1
DBSOURCE    REFSEQ: accession NM_001163519.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD,
            Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg
            B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T,
            Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin
            GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL,
            Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P,
            Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy
            SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH,
            Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW,
            Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J,
            Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M,
            Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW,
            Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J,
            Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U,
            Smailus DE, Schnerch A, Schein JE, Jones SJ and Marra MA.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC160829.1.
            
            On Jul 24, 2009 this sequence version replaced XP_001074627.1.
            
            Transcript Variant: This variant (2) retains an intron resulting in
            a frameshift, compared to variant 1. The resulting isoform (2) has
            a shorter and distinct C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC160829.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..194
                     /product="coiled-coil domain-containing protein 166
                     isoform 2"
                     /note="coiled-coil domain-containing protein 166"
                     /calculated_mol_wt=21133
     Region          69..>145
                     /region_name="DUF4515"
                     /note="Domain of unknown function (DUF4515); pfam14988"
                     /db_xref="CDD:405647"
     CDS             1..194
                     /gene="Ccdc166"
                     /coded_by="NM_001163519.1:227..811"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:680799"
                     /db_xref="RGD:1588167"
ORIGIN      
        1 mapkkkrgqn agrkqagqsg epqlsergqy lqreyamlse slavceqrid evlqsnafln
       61 seaqrlkeen rlfvgyvsah alrcanaivr ledqnrtdla qirwqraela sfyhgredgv
      121 raqlqemkkr aenmtqqvqe lqpykasara padragsrgv gtlptgalig thrptsphvg
      181 vaagaagtnp dpga
//
LOCUS       NP_001009650             337 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 5 [Rattus norvegicus].
ACCESSION   NP_001009650 XP_220099
VERSION     NP_001009650.1
DBSOURCE    REFSEQ: accession NM_001009650.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Li,Q., Korzan,W.J., Ferrero,D.M., Chang,R.B., Roy,D.S., Buchi,M.,
            Lemon,J.K., Kaur,A.W., Stowers,L., Fendt,M. and Liberles,S.D.
  TITLE     Synchronous evolution of an odor biosynthesis pathway and
            behavioral response
  JOURNAL   Curr Biol 23 (1), 11-20 (2013)
   PUBMED   23177478
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Wallrabenstein,I., Kuklan,J., Weber,L., Zborala,S., Werner,M.,
            Altmuller,J., Becker,C., Schmidt,A., Hatt,H., Hummel,T. and
            Gisselmann,G.
  TITLE     Human trace amine-associated receptor TAAR5 can be activated by
            trimethylamine
  JOURNAL   PLoS One 8 (2), e54950 (2013)
   PUBMED   23393561
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Ferrero,D.M., Wacker,D., Roque,M.A., Baldwin,M.W., Stevens,R.C. and
            Liberles,S.D.
  TITLE     Agonists for 13 trace amine-associated receptors provide insight
            into the molecular basis of odor selectivity
  JOURNAL   ACS Chem Biol 7 (7), 1184-1189 (2012)
   PUBMED   22545963
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Staubert,C., Boselt,I., Bohnekamp,J., Rompler,H., Enard,W. and
            Schoneberg,T.
  TITLE     Structural and functional evolution of the trace amine-associated
            receptors TAAR3, TAAR4 and TAAR5 in primates
  JOURNAL   PLoS One 5 (6), e11133 (2010)
   PUBMED   20559446
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Liberles,S.D. and Buck,L.B.
  TITLE     A second class of chemosensory receptors in the olfactory
            epithelium
  JOURNAL   Nature 442 (7103), 645-650 (2006)
   PUBMED   16878137
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702318.1.
            
            On Jan 13, 2005 this sequence version replaced XP_220099.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..337
                     /product="trace amine-associated receptor 5"
                     /calculated_mol_wt=38087
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          35..316
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          37..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320441"
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          70..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320441"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320441"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          153..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320441"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          176..189
                     /region_name="Extracellular Loop 2 (ECL2).
                     /evidence=ECO:0000250|UniProtKB:Q5QD04"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          197..220
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320441"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          251..273
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320441"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     Region          284..309
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320441"
     Site            285..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD23.1)"
     CDS             1..337
                     /gene="Taar5"
                     /gene_synonym="taR-5"
                     /coded_by="NM_001009650.1:1..1014"
                     /db_xref="GeneID:294123"
                     /db_xref="RGD:1359185"
ORIGIN      
        1 mravllpgsg eqpaafcyqv ngscprtvhp lairvliyla cavgmlitvl gnlfvvfavs
       61 yfkvlhtptn flllslalad mllgllvlpl stvrsvescw ffgdflcrlh tyldtlfclt
      121 sifhlcfisi drhcaicdpl lypskftvri alryiaagwg ipaaytaffl ytdvverals
      181 qwleempcvg scqllfnkfw gwlnfpaffi pclimislyl kifvvatrqa qqirtlsqsl
      241 sgavkrerka aktlgiavgi ylvcwlpftv dtlvdsllnf vtpplvfdif iwfayfnsac
      301 npiiyvfsyr wfrkalklll sreilsprtq tadlfhd
//
LOCUS       NP_110467                744 aa            linear   ROD 02-APR-2025
DEFINITION  prestin [Rattus norvegicus].
ACCESSION   NP_110467
VERSION     NP_110467.1
DBSOURCE    REFSEQ: accession NM_030840.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Costanzi,E., Coletti,A., Zambelli,B., Macchiarulo,A., Bellanda,M.
            and Battistutta,R.
  TITLE     Calmodulin binds to the STAS domain of SLC26A5 prestin with a
            calcium-dependent, one-lobe, binding mode
  JOURNAL   J Struct Biol 213 (2), 107714 (2021)
   PUBMED   33667636
  REMARK    GeneRIF: Calmodulin binds to the STAS domain of SLC26A5 prestin
            with a calcium-dependent, one-lobe, binding mode.
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Parham,K., Sohal,M., Petremann,M., Romanet,C., Broussy,A., Tran Van
            Ba,C. and Dyhrfjeld-Johnsen,J.
  TITLE     Noise-induced trauma produces a temporal pattern of change in blood
            levels of the outer hair cell biomarker prestin
  JOURNAL   Hear Res 371, 98-104 (2019)
   PUBMED   30529910
  REMARK    GeneRIF: These results suggest that there is a temporal pattern of
            change in serum prestin level after noise-induced hearing loss that
            is related to severity of hearing loss. Circulatory levels of
            prestin may be able to act as surrogate biomarker for hearing loss
            involving outer hair cell loss.
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Parham,K. and Dyhrfjeld-Johnsen,J.
  TITLE     Outer Hair Cell Molecular Protein, Prestin, as a Serum Biomarker
            for Hearing Loss: Proof of Concept
  JOURNAL   Otol Neurotol 37 (9), 1217-1222 (2016)
   PUBMED   27636386
  REMARK    GeneRIF: work, for the first time, provides proof of concept that
            the levels of prestin, an otologic serum biomarker, can change
            after acoustic trauma and hearing loss
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Lolli,G., Pasqualetto,E., Costanzi,E., Bonetto,G. and
            Battistutta,R.
  TITLE     The STAS domain of mammalian SLC26A5 prestin harbours an
            anion-binding site
  JOURNAL   Biochem J 473 (4), 365-370 (2016)
   PUBMED   26635354
  REMARK    GeneRIF: in chicken STAS, the anion-binding site is lacking because
            of a local structural rearrangement, indicating that the presence
            of the STAS anion-binding site is exclusive to mammalian prestin
REFERENCE   5  (residues 1 to 744)
  AUTHORS   Hang,J., Pan,W., Chang,A., Li,S., Li,C., Fu,M. and Tang,J.
  TITLE     Synchronized Progression of Prestin Expression and Auditory
            Brainstem Response during Postnatal Development in Rats
  JOURNAL   Neural Plast 2016, 4545826 (2016)
   PUBMED   28097024
  REMARK    GeneRIF: Prestin expression first appeared at postnatal day 6 (P6)
            in the auditory brainstem and reached mature level by P14.
REFERENCE   6  (residues 1 to 744)
  AUTHORS   Weber,T., Zimmermann,U., Winter,H., Mack,A., Kopschall,I.,
            Rohbock,K., Zenner,H.P. and Knipper,M.
  TITLE     Thyroid hormone is a critical determinant for the regulation of the
            cochlear motor protein prestin
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2901-2906 (2002)
   PUBMED   11867734
  REMARK    Erratum:[Proc Natl Acad Sci U S A 2002 May 28;99(11):7809]
REFERENCE   7  (residues 1 to 744)
  AUTHORS   Oliver,D., He,D.Z., Klocker,N., Ludwig,J., Schulte,U.,
            Waldegger,S., Ruppersberg,J.P., Dallos,P. and Fakler,B.
  TITLE     Intracellular anions as the voltage sensor of prestin, the outer
            hair cell motor protein
  JOURNAL   Science 292 (5525), 2340-2343 (2001)
   PUBMED   11423665
REFERENCE   8  (residues 1 to 744)
  AUTHORS   Ludwig,J., Oliver,D., Frank,G., Klocker,N., Gummer,A.W. and
            Fakler,B.
  TITLE     Reciprocal electromechanical properties of rat prestin: the motor
            molecule from rat outer hair cells
  JOURNAL   Proc Natl Acad Sci U S A 98 (7), 4178-4183 (2001)
   PUBMED   11274441
REFERENCE   9  (residues 1 to 744)
  AUTHORS   Belyantseva,I.A., Adler,H.J., Curi,R., Frolenkov,G.I. and Kachar,B.
  TITLE     Expression and localization of prestin and the sugar transporter
            GLUT-5 during development of electromotility in cochlear outer hair
            cells
  JOURNAL   J Neurosci 20 (24), RC116 (2000)
   PUBMED   11125015
REFERENCE   10 (residues 1 to 744)
  AUTHORS   Bostjancic,W., Braun,J.S., Reheis,G., Weisshaar,D., Akkerman,J.W.,
            Banauch,D. and Koller,P.U.
  TITLE     [Pre-stained slides for differential blood counts (author's
            transl)]
  JOURNAL   Dtsch Med Wochenschr 102 (33), 1175-1177 (1977)
   PUBMED   70328
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ303372.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ303372.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..744
                     /product="prestin"
                     /note="prestin (motor protein); solute carrier family 26
                     (anion exchanger), member 5"
                     /calculated_mol_wt=81148
     Region          66..709
                     /region_name="PRK11660"
                     /note="putative transporter; Provisional; cl46980"
                     /db_xref="CDD:481320"
     Site            76..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            109..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            138..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Region          158..168
                     /region_name="Involved in motor function.
                     /evidence=ECO:0000250|UniProtKB:Q9JKQ2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            169..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            207..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            259..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            292..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            333..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            371..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            397..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            398
                     /site_type="other"
                     /note="Controls the electromotile activity.
                     /evidence=ECO:0000269|PubMed:24710176; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            399
                     /site_type="other"
                     /note="Contributes to anion binding.
                     /evidence=ECO:0000269|PubMed:24710176; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            437..464
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            466..481
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Site            485..504
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Region          505..718
                     /region_name="Extended region for STAS domain.
                     /evidence=ECO:0000269|PubMed:20471983,
                     ECO:0007744|PDB:3LLO"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     Region          720..744
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH0.1)"
     CDS             1..744
                     /gene="Slc26a5"
                     /gene_synonym="Pres; prestin"
                     /coded_by="NM_030840.1:1..2235"
                     /db_xref="GeneID:83819"
                     /db_xref="RGD:69334"
ORIGIN      
        1 mdhaeeneip aetqkylver pifshpvlqe rlhvkdkvtd sigdklkqaf tctpkkvrni
       61 iymflpitkw lpaykfkeyv lgdlvsgist gvlqlpqgla famlaavppv fglyssfypv
      121 imycffgtsr hisigpfavi slmiggvavr lvpddivipg gvnatngtea rdalrvkvam
      181 svtllsgiiq fclgvcrfgf vaiylteplv rgfttaaavh vftsmlkylf gvktkrysgi
      241 fsvvystvav lqnvknlnvc slgvglmvfg lllggkefne rfkeklpapi pleffavvmg
      301 tgisagfnlh esysvdvvgt lplgllppan pdtslfhlvy vdaiaiaivg fsvtismakt
      361 lankhgyqvd gnqelialgi cnsigslfqt fsiscslsrs lvqegtggkt qlagclaslm
      421 illvilatgf lfeslpqavl saivivnlkg mfmqfsdlpf fwrtskielt iwlttfvssl
      481 flgldyglit aviialltvi yrtqspsytv lgqlpdtdvy ididayeevk eipgikifqi
      541 napiyyansd lyssalkrkt gvnpaiimga rrkamrkyak evgnaniana tvvkvdaevd
      601 genatkpeee ddevkfppiv ikttfpeelq rflpqgenih tvildftqvn fmdsvgvktl
      661 agivkeygdv giyvylagcs aqvvndltsn rffenpalke llfhsihdav lgsqvreama
      721 eqettvlppq edmepnatpt tpea
//
LOCUS       NP_001014779             779 aa            linear   ROD 02-APR-2025
DEFINITION  protocadherin beta 8 [Rattus norvegicus].
ACCESSION   NP_001014779 XP_226000
VERSION     NP_001014779.1
DBSOURCE    REFSEQ: accession NM_001014779.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Wu,Q.
  TITLE     Comparative genomics and diversifying selection of the clustered
            vertebrate protocadherin genes
  JOURNAL   Genetics 169 (4), 2179-2188 (2005)
   PUBMED   15744052
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Zhang,T., Haws,P. and Wu,Q.
  TITLE     Multiple variable first exons: a mechanism for cell- and
            tissue-specific gene regulation
  JOURNAL   Genome Res 14 (1), 79-89 (2004)
   PUBMED   14672974
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473974.1.
            
            On Apr 8, 2005 this sequence version replaced XP_226000.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..779
                     /product="protocadherin beta 8"
                     /calculated_mol_wt=84613
     Region          30..112
                     /region_name="Cadherin_2"
                     /note="Cadherin-like; pfam08266"
                     /db_xref="CDD:462413"
     Region          140..238
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(144..145,201,203,234,236..237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          247..342
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(253..254,307,309,338,340..341)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          354..446
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(357..358,409,411,442,444..445)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          454..556
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(461..462,519,521,552,554..555)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          575..663
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          685..766
                     /region_name="Cadherin_C_2"
                     /note="Cadherin cytoplasmic C-terminal; pfam16492"
                     /db_xref="CDD:465139"
     CDS             1..779
                     /gene="Pcdhb8"
                     /coded_by="NM_001014779.1:1..2340"
                     /db_xref="GeneID:680020"
                     /db_xref="RGD:1309895"
ORIGIN      
        1 metalaktpe krqviflail lllwesgsea irysmpeete sgylianlak dlglqigels
       61 trgarihhng nkellqldak rgnlllkekp drealcgate pcvlhfqiil enpvqffqtd
      121 lqltdindhs pefpdtemll kiqesvqpgt vfplkaaqds digsnavqny tvnpnlhfhv
      181 lthshtdgrk ypelvldral dreeqpeltl iltaldggap pksgtttvri evvdindnap
      241 qfvqslyave vpedsplnal vvtvsardld tgihgnvays lfqgsgglqp fvideisgei
      301 rlkgaldfea tpyynmeiva tdsgglsgkc tvsiqvvdvn dnapkltiss ltrsipenap
      361 eavvavfsvs dpdsgdngrv lcsiqnelpf llkptfknfy tlvtespldr esraeyniti
      421 svsdlgtprl ttqhtitvqv sdindnaptf tqtsytlfvh ennspalhig tisatdadsg
      481 sngfinysll pphdqqlalv slisinsdng qlfalraldy eavqafefhv gatdggspal
      541 ssqalvrvvv lddndnapfv lyplqnasap ctellpraae pgylvtkvva vdadsgqnaw
      601 lsfqllkate pglfnvwahn gevrtarlls erdvpkhrll lvvkdngepp rsasimlqvl
      661 vvdgfsqpyl plpevalnpt keedmltlyl vialasvssl fllsvllfvg vrlcrkaraa
      721 slgdcsipeg hfpghlvdvs sagtlsqnyh yevcltedsg tsdfkfmnpi iptsllqds
//
LOCUS       NP_001009968             194 aa            linear   ROD 02-APR-2025
DEFINITION  Spetex-2F protein [Rattus norvegicus].
ACCESSION   NP_001009968 XP_006251742 XP_008768763 XP_229523
VERSION     NP_001009968.1
DBSOURCE    REFSEQ: accession NM_001009968.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Iwamoto,Y., Kaneko,T., Ichinose,J., Mori,T., Shibata,Y.,
            Toshimori,K. and Iida,H.
  TITLE     Molecular cloning of rat Spetex2 family genes mapped on chromosome
            15p16, encoding a 23-kilodalton protein associated with the plasma
            membranes of haploid spermatids
  JOURNAL   Biol Reprod 72 (2), 284-292 (2005)
   PUBMED   15371276
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB180081.1.
            
            On or before Aug 24, 2014 this sequence version replaced
            XP_008768763.1, XP_006251742.1, XP_229523.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB180081.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..194
                     /product="Spetex-2F protein"
                     /calculated_mol_wt=23134
     Region          34..114
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..194
                     /gene="Spetex2f"
                     /gene_synonym="Spetex-2F"
                     /coded_by="NM_001009968.1:1..585"
                     /db_xref="GeneID:316940"
                     /db_xref="RGD:1359579"
ORIGIN      
        1 mfhqllklvq kergdqgetr lrqkktglls wfirkassen fisnhekhik kleelkleiq
       61 kckierdels rildlyvndg lnyrlsvelp mlksqhemrm mdmhkmtnwi sdamekykel
      121 tqennsyrir nfqllnecne lkknvrilmn enrkllveqt elqasfeegk rfceeaskti
      181 ytadieslcp vtfe
//
LOCUS       NP_001009177             112 aa            linear   ROD 02-APR-2025
DEFINITION  stefin A3-like 1 precursor [Rattus norvegicus].
ACCESSION   NP_001009177 XP_579281
VERSION     NP_001009177.1
DBSOURCE    REFSEQ: accession NM_001009177.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000375.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579281.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000375.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..112
                     /product="stefin A3-like 1 precursor"
                     /function="cysteine protease inhibitor"
                     /calculated_mol_wt=10386
     sig_peptide     1..22
                     /calculated_mol_wt=2336
     mat_peptide     23..112
                     /product="stefin A3-like 1"
                     /calculated_mol_wt=10386
     Region          <43..106
                     /region_name="Cystatin"
                     /note="Cystatin domain; pfam00031"
                     /db_xref="CDD:425431"
     Site            order(66..68,70)
                     /site_type="active"
                     /note="putative proteinase inhibition site [active]"
                     /db_xref="CDD:238002"
     CDS             1..112
                     /gene="Stfa3l1"
                     /coded_by="NM_001009177.1:1..339"
                     /db_xref="GeneID:408215"
                     /db_xref="RGD:1302997"
ORIGIN      
        1 mgeqqasvsl lcqfpvtssi pllttvillr vvlpfkwlgc ylvkplleek tnekyekfqa
       61 vdykvqvvag knyfikmdvg hikvfqglsg eddlelsgyh tnktkndelt sf
//
LOCUS       NP_001257315             114 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC688925 [Rattus norvegicus].
ACCESSION   NP_001257315 XP_003750920 XP_003752398
VERSION     NP_001257315.1
DBSOURCE    REFSEQ: accession NM_001270386.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            AY387069.1.
            
            On or before Jul 3, 2012 this sequence version replaced
            XP_003752398.1, XP_003750920.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY387069.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..114
                     /product="uncharacterized protein LOC688925"
                     /calculated_mol_wt=13141
     Region          1..67
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Region          <74..112
                     /region_name="GST_C_family"
                     /note="C-terminal, alpha helical domain of the Glutathione
                     S-transferase family; cl02776"
                     /db_xref="CDD:470672"
     CDS             1..114
                     /gene="Gsta4l1"
                     /gene_synonym="LRRGT00083"
                     /coded_by="NM_001270386.1:1..345"
                     /db_xref="GeneID:688925"
                     /db_xref="RGD:1582982"
ORIGIN      
        1 mesicwllvt tgvefeeefl etreqyeklq kdgcllfgrv plveidgmll tqtrailrfl
       61 aakhnlygkn lkdrafktri sniptikkfl qpgsqrkppp dghyddmvrt vlkf
//
LOCUS       NP_001102699             619 aa            linear   ROD 02-APR-2025
DEFINITION  monooxygenase, DBH-like 2 precursor [Rattus norvegicus].
ACCESSION   NP_001102699 XP_001070939 XP_575443
VERSION     NP_001102699.1
DBSOURCE    REFSEQ: accession NM_001109229.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473959.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_575443.1, XP_001070939.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN16676807, SAMN16676808
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..619
                     /product="monooxygenase, DBH-like 2 precursor"
                     /calculated_mol_wt=67292
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2527
     Region          36..159
                     /region_name="DOMON_DOH"
                     /note="DOMON-like domain of copper-dependent
                     monooxygenases and related proteins; cd09631"
                     /db_xref="CDD:187689"
     Site            order(66,68..69,81..83,143,145,152)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:187689"
     Region          193..317
                     /region_name="Cu2_monooxygen"
                     /note="Copper type II ascorbate-dependent monooxygenase,
                     N-terminal domain; pfam01082"
                     /db_xref="CDD:460053"
     Region          336..482
                     /region_name="Cu2_monoox_C"
                     /note="Copper type II ascorbate-dependent monooxygenase,
                     C-terminal domain; pfam03712"
                     /db_xref="CDD:461021"
     CDS             1..619
                     /gene="Moxd2"
                     /gene_synonym="RGD1564286"
                     /coded_by="NM_001109229.1:1..1860"
                     /db_xref="GeneID:500092"
                     /db_xref="RGD:1564286"
ORIGIN      
        1 mgyflffrlf llwvlaafsq gkrlsptspl rysrfldpsh avflrwdfdy eteiitfelq
       61 vqttgwvglg itdrytfvgs dlvvggvlpn gnvyfsdqhl ldedtleqdg sqdaellklt
      121 edsvsttmrf srpfrscdph dhditsdtmr vlaayglddi pkmnrertfv ksifllqilq
      181 yddedapedt viydlkisnf lipeedttya ctflplpivs kkhhiykfep ilvernetmv
      241 hhvlvyacgn ssvlptgige cygadpafsl cshviagwav gglsyqfpdd vgisigtpfd
      301 pqwirleihy snfqnlpgir dtsgmrlyyt shlrkydmgv lqlgisvfpi hfippgaeaf
      361 lsyglcktdk feemngapva diyvsacllh thlagrslqa lqyrngtqlq ivckdfsydf
      421 nlqesrdlph pvvikpgdel liechyqtld rdfmtfggas tinemcliff fyypriniss
      481 cmgypdiiyv tnelgeease npmenlmvln nvewtpenik taekackesq qtvliktide
      541 eventtgwip diiptprgac lessggkvep qdktpagfra vpmalsgsnt atlrhlpmit
      601 vlflqgclsw llamlqtgv
//
LOCUS       NP_001008824             449 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type I cytoskeletal 27 [Rattus norvegicus].
ACCESSION   NP_001008824 XP_579221
VERSION     NP_001008824.1
DBSOURCE    REFSEQ: accession NM_001008824.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Tanaka,S., Miura,I., Yoshiki,A., Kato,Y., Yokoyama,H., Shinogi,A.,
            Masuya,H., Wakana,S., Tamura,M. and Shiroishi,T.
  TITLE     Mutations in the helix termination motif of mouse type I IRS
            keratin genes impair the assembly of keratin intermediate filament
  JOURNAL   Genomics 90 (6), 703-711 (2007)
   PUBMED   17920809
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004030.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579221.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004030.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..449
                     /product="keratin, type I cytoskeletal 27"
                     /note="K27; CK-27; cytokeratin-27; type I inner root
                     sheath-specific keratin-K25irs3; type I keratin KA40;
                     keratin 27, type I"
                     /calculated_mol_wt=48978
     Region          1..73
                     /region_name="Head. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          73..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          74..109
                     /region_name="Coil 1A. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          110..131
                     /region_name="Linker 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          132..223
                     /region_name="Coil 1B. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          224..246
                     /region_name="Linker 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          247..385
                     /region_name="Coil 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          386..449
                     /region_name="Tail. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     Region          425..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW8.1)"
     CDS             1..449
                     /gene="Krt27"
                     /gene_synonym="Ka40"
                     /coded_by="NM_001008824.1:1..1350"
                     /db_xref="GeneID:450229"
                     /db_xref="RGD:1359115"
ORIGIN      
        1 msvrfssasr rlgsvrlssp gaalgagntc gvpgigsgfs cafggsslag glgmggascg
       61 aftvnehgll sgnekvtmqn lndrlasyle nvqaleeana dleqkikdwy ekfgpgscrg
      121 ldhdysryfp iiddlrtqii sataqnaniv lqndnarlta ddfrmkyene lalhqsvdad
      181 inglrrvlde ltlcrtdlev qletlseela ylkknheeem qalqcaaggn vnvemnaapg
      241 vdltvllnnm raeyealaeq nrrdaeawfq eksaslqqqi sddagattsa rneltemkrt
      301 lqtleielqs llamkhslec sltetegnyc tqlaqiqaqi saleeqlhqv rtetegqkle
      361 yeqllnvkah lekeietycl liggdegscv kskgqggpgn qtkdspktai vktvveeldp
      421 rgkvlssrvh tleekstkvn nkneqrips
//
LOCUS       NP_001019857             304 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 4 [Rattus norvegicus].
ACCESSION   NP_001019857
VERSION     NP_001019857.1
DBSOURCE    REFSEQ: accession NM_001024686.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Krasteva,G., Canning,B.J., Hartmann,P., Veres,T.Z., Papadakis,T.,
            Muhlfeld,C., Schliecker,K., Tallini,Y.N., Braun,A., Hackstein,H.,
            Baal,N., Weihe,E., Schutz,B., Kotlikoff,M., Ibanez-Tallon,I. and
            Kummer,W.
  TITLE     Cholinergic chemosensory cells in the trachea regulate breathing
  JOURNAL   Proc Natl Acad Sci U S A 108 (23), 9478-9483 (2011)
   PUBMED   21606356
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Wu,S.V., Chen,M.C. and Rozengurt,E.
  TITLE     Genomic organization, expression, and function of bitter taste
            receptors (T2R) in mouse and rat
  JOURNAL   Physiol Genomics 22 (2), 139-149 (2005)
   PUBMED   15886333
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY916510.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY916510.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..304
                     /product="taste receptor type 2 member 4"
                     /note="T2R4; T2R20; taste receptor type 2 member 20;
                     bitter taste receptor T2R16"
                     /calculated_mol_wt=34680
     Region          7..281
                     /region_name="7tm_TAS2R4"
                     /note="mammalian taste receptor 2, subtype 4, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15013"
                     /db_xref="CDD:320141"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320141"
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320141"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Region          81..103
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320141"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Region          130..146
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320141"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET0.1)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Region          173..196
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320141"
     Region          221..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320141"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     Region          257..281
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320141"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET0.1)"
     CDS             1..304
                     /gene="Tas2r108"
                     /gene_synonym="T2R16; Tas2r4"
                     /coded_by="NM_001024686.1:1..915"
                     /db_xref="GeneID:554302"
                     /db_xref="RGD:1561194"
ORIGIN      
        1 mlwelyafvf aasvvfnfvg ivanlfiivi isktwvkshk isssdkilfs laitrfltlg
       61 lfllntvyia tntgrsvyfs tffllcwkfl dsnslwlvtf lnclycvkit hfqhpvflll
      121 krtvsmktts lllacllisa fttllyfvlt qisrfpehii grndtlfdvs dgiltlaasl
      181 ilssllqfll nvtfasllih slrrhvqkmq rnrssfwnpq teahvgamrl micflvlyip
      241 ysiaallyfp symrknlraq aacmiitaay ppghsillii thhklkakak kiccfyklrd
      301 fvsn
//
LOCUS       NP_001099647             399 aa            linear   ROD 02-APR-2025
DEFINITION  heat shock factor protein 4 [Rattus norvegicus].
ACCESSION   NP_001099647 XP_001075468 XP_214668
VERSION     NP_001099647.1
DBSOURCE    REFSEQ: accession NM_001106177.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Fujimoto,M., Oshima,K., Shinkawa,T., Wang,B.B., Inouye,S.,
            Hayashida,N., Takii,R. and Nakai,A.
  TITLE     Analysis of HSF4 binding regions reveals its necessity for gene
            regulation during development and heat shock response in mouse
            lenses
  JOURNAL   J Biol Chem 283 (44), 29961-29970 (2008)
   PUBMED   18755693
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ho,E.A. and Piquette-Miller,M.
  TITLE     KLF6 and HSF4 transcriptionally regulate multidrug resistance
            transporters during inflammation
  JOURNAL   Biochem Biophys Res Commun 353 (3), 679-685 (2007)
   PUBMED   17196161
  REMARK    GeneRIF: KLF6 and HSF4 are stimuli-specific regulatory elements
            which may be important in the control of the rat mdr1b and mrp3
            genes during health and disease.
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Talamas,E., Jackson,L., Koeberl,M., Jackson,T., McElwee,J.L.,
            Hawes,N.L., Chang,B., Jablonski,M.M. and Sidjanin,D.J.
  TITLE     Early transposable element insertion in intron 9 of the Hsf4 gene
            results in autosomal recessive cataracts in lop11 and ldis1 mice
  JOURNAL   Genomics 88 (1), 44-51 (2006)
   PUBMED   16595169
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hu,Y. and Mivechi,N.F.
  TITLE     Association and regulation of heat shock transcription factor 4b
            with both extracellular signal-regulated kinase mitogen-activated
            protein kinase and dual-specificity tyrosine phosphatase DUSP26
  JOURNAL   Mol Cell Biol 26 (8), 3282-3294 (2006)
   PUBMED   16581800
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Min,J.N., Zhang,Y., Moskophidis,D. and Mivechi,N.F.
  TITLE     Unique contribution of heat shock transcription factor 4 in ocular
            lens development and fiber cell differentiation
  JOURNAL   Genesis 40 (4), 205-217 (2004)
   PUBMED   15593327
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Fujimoto,M., Izu,H., Seki,K., Fukuda,K., Nishida,T., Yamada,S.,
            Kato,K., Yonemura,S., Inouye,S. and Nakai,A.
  TITLE     HSF4 is required for normal cell growth and differentiation during
            mouse lens development
  JOURNAL   EMBO J 23 (21), 4297-4306 (2004)
   PUBMED   15483628
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Somasundaram,T. and Bhat,S.P.
  TITLE     Developmentally dictated expression of heat shock factors:
            exclusive expression of HSF4 in the postnatal lens and its specific
            interaction with alphaB-crystallin heat shock promoter
  JOURNAL   J Biol Chem 279 (43), 44497-44503 (2004)
   PUBMED   15308659
  REMARK    GeneRIF: HSF4 binds to alphaB-crystallin, Hsp70, and Hsp82
            promoters and has a role in interacting with the canonical heat
            shock element of the alphaB-crystallin gene [HSF4]
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Jablonski,M.M., Lu,L., Wang,X., Chesler,E.J., Carps,E., Qi,S.,
            Gu,J. and Williams,R.W.
  TITLE     The ldis1 lens mutation in RIIIS/J mice maps to chromosome 8 near
            cadherin 1
  JOURNAL   Mol Vis 10, 577-587 (2004)
   PUBMED   15343150
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Bu,L., Jin,Y., Shi,Y., Chu,R., Ban,A., Eiberg,H., Andres,L.,
            Jiang,H., Zheng,G., Qian,M., Cui,B., Xia,Y., Liu,J., Hu,L.,
            Zhao,G., Hayden,M.R. and Kong,X.
  TITLE     Mutant DNA-binding domain of HSF4 is associated with autosomal
            dominant lamellar and Marner cataract
  JOURNAL   Nat Genet 31 (3), 276-278 (2002)
   PUBMED   12089525
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001075468.1, XP_214668.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760475,
                              SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..399
                     /product="heat shock factor protein 4"
                     /calculated_mol_wt=43089
     Region          <18..60
                     /region_name="HSF_DNA-bind"
                     /note="HSF-type DNA-binding; cl12113"
                     /db_xref="CDD:472277"
     CDS             1..399
                     /gene="Hsf4"
                     /coded_by="NM_001106177.1:139..1338"
                     /db_xref="GeneID:291960"
                     /db_xref="RGD:1310808"
ORIGIN      
        1 mgagrrprhr pphplepdgf rkvvsieqgg llrperdhve fqhpsfvrgc eqllervrrk
       61 vpalrgddtr wrpedlgrll gevqalrgvq estearlqel rqqneilwre vvtlrqshsq
      121 qhrvigkliq clfgplqtgp sstgakrkls lmldegsacs asakfnacpv sgallqdpyf
      181 iqspstcsps qrppwasalt gpeglsslts qktahllkdt gflppvlaga ppplpvavvq
      241 ailegkgsfs pegprsiqqp eprgprevpd rgtlgldrgn rspesllppv llrpppetve
      301 pmdalgpslh grewtlmdld melslmqpla peraeaeltv kdltssgvgk dhtlgtplml
      361 dvqadlegaa lsvpgaltly natesnasyl dpgaspssp
//
LOCUS       NP_001009532             342 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 3 [Rattus norvegicus].
ACCESSION   NP_001009532 XP_579306
VERSION     NP_001009532.1
DBSOURCE    REFSEQ: accession NM_001009532.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Staubert,C., Boselt,I., Bohnekamp,J., Rompler,H., Enard,W. and
            Schoneberg,T.
  TITLE     Structural and functional evolution of the trace amine-associated
            receptors TAAR3, TAAR4 and TAAR5 in primates
  JOURNAL   PLoS One 5 (6), e11133 (2010)
   PUBMED   20559446
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Liberles,S.D. and Buck,L.B.
  TITLE     A second class of chemosensory receptors in the olfactory
            epithelium
  JOURNAL   Nature 442 (7103), 645-650 (2006)
   PUBMED   16878137
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702317.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579306.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..342
                     /product="trace amine-associated receptor 3"
                     /note="taR-3; trace amine receptor 3"
                     /calculated_mol_wt=38527
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD24.1)"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          33..319
                     /region_name="7tmA_TAAR2_3_4"
                     /note="trace amine-associated receptors 2, 3, 4, and
                     similar receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15312"
                     /db_xref="CDD:320437"
     Region          33..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320437"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          66..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320437"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          104..134
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320437"
     Site            order(107,111..112,115..116,191,198,201..202,205,268,
                     271..272,275,290,294,298)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320437"
     Region          146..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320437"
     Site            151..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          173..186
                     /region_name="Extracellular Loop 2 (ECL2).
                     /evidence=ECO:0000250|UniProtKB:Q5QD04"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          194..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320437"
     Site            199..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          248..278
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320437"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     Region          287..312
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320437"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD24.1)"
     CDS             1..342
                     /gene="Taar3"
                     /coded_by="NM_001009532.1:1..1029"
                     /db_xref="GeneID:494319"
                     /db_xref="RGD:1359566"
ORIGIN      
        1 mdliyipedl sscpkfgnks cpptnrsfrv rlimyllmtg amvitifgnl viiisishfk
       61 qlhsptnfli lsmattdfll gfvimpysmv rsvescwyfg dsfckfhasf dmmlsltsif
      121 hlcsiaidrf yavcaplhyt ttmtasmikr llffcwaapa lfsfglvlse anvsgmqsye
      181 iliacfnfca ltfnkfwgti lfttcfftpg simvgiygki fivsrrhara lgnmpentkg
      241 agrnlskkkd rkaaktlgiv mgvflacwlp cflavlidpy ldystpiivl dllvwlgyfn
      301 stcnplihgf fypwfrkale hivsgkifrs nsdtanlfpe ah
//
LOCUS       NP_997471                337 aa            linear   ROD 02-APR-2025
DEFINITION  2-oxoglutarate receptor 1 [Rattus norvegicus].
ACCESSION   NP_997471 XP_224529
VERSION     NP_997471.1
DBSOURCE    REFSEQ: accession NM_207588.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Kerschner,J.E., Hong,W., Taylor,S.R., Kerschner,J.A., Khampang,P.,
            Wrege,K.C. and North,P.E.
  TITLE     A novel model of spontaneous otitis media with effusion (OME) in
            the Oxgr1 knock-out mouse
  JOURNAL   Int J Pediatr Otorhinolaryngol 77 (1), 79-84 (2013)
   PUBMED   23200873
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Inbe,H., Watanabe,S., Miyawaki,M., Tanabe,E. and Encinas,J.A.
  TITLE     Identification and characterization of a cell-surface receptor,
            P2Y15, for AMP and adenosine
  JOURNAL   J Biol Chem 279 (19), 19790-19799 (2004)
   PUBMED   15001573
  REMARK    GeneRIF: P2Y15 is a cell surface receptor for AMP and adenosine
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY191367.1.
            
            On Aug 30, 2004 this sequence version replaced XP_224529.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY191367.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24"
     Protein         1..337
                     /product="2-oxoglutarate receptor 1"
                     /note="P2Y purinoceptor 15; alpha-ketoglutarate receptor
                     1; G protein-coupled receptor 80; oxoglutarate
                     (alpha-ketoglutarate) receptor 1"
                     /calculated_mol_wt=38246
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          35..313
                     /region_name="7tmA_OXGR1"
                     /note="2-oxoglutarate receptor 1, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15375"
                     /db_xref="CDD:320497"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320497"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          68..93
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320497"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Site            order(89,92..93,106..111,113..114,117,162,164..168,182,
                     184..186,195,198..200,202..204,206..207,254,257..258,
                     260..261,264,280..281,283..285,288,291..292)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320497"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320497"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          148..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320497"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          195..224
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320497"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          234..264
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320497"
     Site            243..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     Region          281..306
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320497"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Y1R5.1)"
     CDS             1..337
                     /gene="Oxgr1"
                     /gene_synonym="Gpr80; P2Y15"
                     /coded_by="NM_207588.1:1..1014"
                     /db_xref="GeneID:290493"
                     /db_xref="RGD:1303155"
ORIGIN      
        1 mietldspan dsdfldyita lenctdeqis fkmqylpviy siiflvgfpg ntvaisiyvf
       61 kmrpwkssti imlnlaltdl lyltslpfli hyyasgenwi fgdfmckfir fgfhfnlyss
      121 ilfltcfslf ryiviihpms cfsiqktrwa vvacagvwvi slvavmpmtf litsttrtnr
      181 sacldltssd dlttikwynl iltattfclp llivtlcytt iistlthgpr thscfkqkar
      241 rltillllvf yvcflpfhil rviriesrll siscsieshi heayivsrpl aalntfgnll
      301 lyvvvsnnfq qafcsavrck aigdleqakk dscsnnp
//
LOCUS       NP_062214                181 aa            linear   ROD 02-APR-2025
DEFINITION  regulator of G-protein signaling 5 [Rattus norvegicus].
ACCESSION   NP_062214
VERSION     NP_062214.1
DBSOURCE    REFSEQ: accession NM_019341.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Hong,K., Li,M., Nourian,Z., Meininger,G.A. and Hill,M.A.
  TITLE     Angiotensin II Type 1 Receptor Mechanoactivation Involves RGS5
            (Regulator of G Protein Signaling 5) in Skeletal Muscle Arteries:
            Impaired Trafficking of RGS5 in Hypertension
  JOURNAL   Hypertension 70 (6), 1264-1272 (2017)
   PUBMED   29061726
  REMARK    GeneRIF: AT1R activation results in translocation of RGS5 toward
            the plasma membrane, limiting AT1R-mediated vasoconstriction
            through its role in Gq/11 protein-dependent signaling.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Kang,B.W., Jeon,H.S., Chae,Y.S., Lee,S.J., Park,J.S., Choi,G.S. and
            Kim,J.G.
  TITLE     Impact of Genetic Variation in MicroRNA-binding Site on
            Susceptibility to Colorectal Cancer
  JOURNAL   Anticancer Res 36 (7), 3353-3361 (2016)
   PUBMED   27354594
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Zhao,P. and Chidiac,P.
  TITLE     Regulation of RGS5 GAP activity by GPSM3
  JOURNAL   Mol Cell Biochem 405 (1-2), 33-40 (2015)
   PUBMED   25842189
  REMARK    GeneRIF: The enhancement of RGS5 activity by GPSM3 is maintained
            under these conditions.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Bokenkamp,R., van Brempt,R., van Munsteren,J.C., van den
            Wijngaert,I., de Hoogt,R., Finos,L., Goeman,J., Groot,A.C.,
            Poelmann,R.E., Blom,N.A. and DeRuiter,M.C.
  TITLE     Dlx1 and Rgs5 in the ductus arteriosus: vessel-specific genes
            identified by transcriptional profiling of laser-capture
            microdissected endothelial and smooth muscle cells
  JOURNAL   PLoS One 9 (1), e86892 (2014)
   PUBMED   24489801
  REMARK    GeneRIF: Rgs5 and Dlx1 represent novel molecular targets for the
            regulation of ductus arteriosus maturation and closure.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Zarzuelo,M.J., Jimenez,R., Galindo,P., Sanchez,M., Nieto,A.,
            Romero,M., Quintela,A.M., Lopez-Sepulveda,R., Gomez-Guzman,M.,
            Bailon,E., Rodriguez-Gomez,I., Zarzuelo,A., Galvez,J., Tamargo,J.,
            Perez-Vizcaino,F. and Duarte,J.
  TITLE     Antihypertensive effects of peroxisome proliferator-activated
            receptor-beta activation in spontaneously hypertensive rats
  JOURNAL   Hypertension 58 (4), 733-743 (2011)
   PUBMED   21825230
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Wang,X., Adams,L.D., Pabon,L.M., Mahoney,W.M. Jr., Beaudry,D.,
            Gunaje,J., Geary,R.L., Deblois,D. and Schwartz,S.M.
  TITLE     RGS5, RGS4, and RGS2 expression and aortic contractibility are
            dynamically co-regulated during aortic banding-induced hypertrophy
  JOURNAL   J Mol Cell Cardiol 44 (3), 539-550 (2008)
   PUBMED   18207159
  REMARK    GeneRIF: After 2 days of aortic banding-induced hypertrophy,
            thoracic aorta lost expression of Rgs5, it returned to normal at 1
            week and increased many fold at 28 days, indicating that RGS
            expression and function correlate with vascular remodeling.
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Grayson,T.H., Ohms,S.J., Brackenbury,T.D., Meaney,K.R., Peng,K.,
            Pittelkow,Y.E., Wilson,S.R., Sandow,S.L. and Hill,C.E.
  TITLE     Vascular microarray profiling in two models of hypertension
            identifies caveolin-1, Rgs2 and Rgs5 as antihypertensive targets
  JOURNAL   BMC Genomics 8, 404 (2007)
   PUBMED   17986358
  REMARK    GeneRIF: changes in common to caveolin-1 expression and G protein
            signalling, through attenuation of Rgs2 and Rgs5, may contribute to
            hypertension through augmentation of vasoconstrictor pathways
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Lovschall,H., Mitsiadis,T.A., Poulsen,K., Jensen,K.H. and
            Kjeldsen,A.L.
  TITLE     Coexpression of Notch3 and Rgs5 in the pericyte-vascular smooth
            muscle cell axis in response to pulp injury
  JOURNAL   Int J Dev Biol 51 (8), 715-721 (2007)
   PUBMED   17939118
  REMARK    GeneRIF: Rgs5 and Notch3 are expressed in pericytes of developing
            and injured teeth and have roles along with vascular-derived stem
            cells during pulp healing
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Wang,Q., Liu,M., Mullah,B., Siderovski,D.P. and Neubig,R.R.
  TITLE     Receptor-selective effects of endogenous RGS3 and RGS5 to regulate
            mitogen-activated protein kinase activation in rat vascular smooth
            muscle cells
  JOURNAL   J Biol Chem 277 (28), 24949-24958 (2002)
   PUBMED   12006602
  REMARK    GeneRIF: role in regulating mitogen-activated protein kinase
            activation in rat vascular smooth muscle cells
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Koelle,M.R. and Horvitz,H.R.
  TITLE     EGL-10 regulates G protein signaling in the C. elegans nervous
            system and shares a conserved domain with many mammalian proteins
  JOURNAL   Cell 84 (1), 115-125 (1996)
   PUBMED   8548815
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF241259.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF241259.1, EF568934.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..181
                     /product="regulator of G-protein signaling 5"
                     /calculated_mol_wt=20921
     Region          65..178
                     /region_name="RGS_RGS5"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS5 protein; cd08717"
                     /db_xref="CDD:188672"
     CDS             1..181
                     /gene="Rgs5"
                     /coded_by="NM_019341.1:1..546"
                     /db_xref="GeneID:54294"
                     /db_xref="RGD:3568"
ORIGIN      
        1 mckglaalph sclerakeik iklgillqkp dsavdlvipy nekpekpaka hkpsleevlq
       61 wrqsldkllq snygfasfks flksefseen lefwvaceny kkikspikma ekakqiyeef
      121 iqteapkevn idhftkditm knlvepsphs fdlaqkriya lmekdslprf vrsefykeli
      181 n
//
LOCUS       NP_001100435             331 aa            linear   ROD 02-APR-2025
DEFINITION  melanoma-associated antigen B3 [Rattus norvegicus].
ACCESSION   NP_001100435 XP_001061758 XP_229038
VERSION     NP_001100435.1
DBSOURCE    REFSEQ: accession NM_001106965.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473966.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001061758.1, XP_229038.3.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..331
                     /product="melanoma-associated antigen B3"
                     /note="melanoma antigen family B, 3"
                     /calculated_mol_wt=36978
     Region          5..87
                     /region_name="MAGE_N"
                     /note="Melanoma associated antigen family N terminal;
                     pfam12440"
                     /db_xref="CDD:463582"
     Region          <199..285
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     CDS             1..331
                     /gene="Mageb3"
                     /gene_synonym="RGD1562343"
                     /coded_by="NM_001106965.1:1..996"
                     /db_xref="GeneID:302746"
                     /db_xref="RGD:1562343"
ORIGIN      
        1 mprgqkrklh agkkcyqagg etqdlqgaqa laevekscpp pssphvgvta htksasklqt
       61 tskvpqrals tteskglsht rpckvakyki krkqqssqts pstekcprss ltstvrlvvn
      121 ymmnmckmkr pilkadvmkm vtnthkvhia eilrrasfnl evllgvdlke adsmdsytla
      181 skmnlpnngv lttgrgfpkt gllmnllgvi flkgncatee siweflnkmk iydgkkhfif
      241 geprklitqd lvklkyleyr qvpnrsptsy eflwgprsha etskmkilkf lakinhivps
      301 afqsrydeal kdeeersqaa atfgdttint k
//
LOCUS       NP_001101043             470 aa            linear   ROD 02-APR-2025
DEFINITION  tigger transposable element-derived protein 3 [Rattus norvegicus].
ACCESSION   NP_001101043 XP_001071012 XP_219522
VERSION     NP_001101043.1
DBSOURCE    REFSEQ: accession NM_001107573.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473953.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_219522.1, XP_001071012.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132263 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..470
                     /product="tigger transposable element-derived protein 3"
                     /note="tigger transposable element derived 3 homolog"
                     /calculated_mol_wt=52284
     Region          6..57
                     /region_name="CENP-B_N"
                     /note="CENP-B N-terminal DNA-binding domain; pfam04218"
                     /db_xref="CDD:461229"
     Region          76..133
                     /region_name="HTH_Tnp_Tc5"
                     /note="Tc5 transposase DNA-binding domain; pfam03221"
                     /db_xref="CDD:460850"
     Region          193..360
                     /region_name="DDE_3"
                     /note="DDE superfamily endonuclease; cl46863"
                     /db_xref="CDD:481203"
     CDS             1..470
                     /gene="Tigd3"
                     /coded_by="NM_001107573.1:174..1586"
                     /db_xref="GeneID:309174"
                     /db_xref="RGD:1305393"
ORIGIN      
        1 melntkkklh alslaekiqv lelldeskms qsevarrfqv sqpqisrick nkeklladwc
       61 sgtanherkr kreskysgid eallcwyhia rakawdvtgp mllhkakela dimgqdfvps
      121 igwlvrwkrr nnvgfgtrqv lvpllppepp pavspsqaqp plslkdfspe dvfgcaevpl
      181 lyravpgrvf ecdrlqvllc ansrgtekrr vfvgglqpap rcffgvnsea lpasyhpdla
      241 ipwsewlaqf dqdmgqqgrq valllasgvv eewasppglh hvrllplsts sttpslpgsv
      301 vlafkahyrh rllsklaamq sgkegtsrae aranitvlda lhmvaaawak vprqliltsf
      361 iqeglapgkt plsldkdtem spvpsglsqe efshfvdled edpgprvcke etstedngre
      421 edgfeslptk adalralctl rrwlecnsts pelfekfydc eveveqlccl
//
LOCUS       NP_579825                144 aa            linear   ROD 02-APR-2025
DEFINITION  seminal vesicle antigen-like 2 precursor [Rattus norvegicus].
ACCESSION   NP_579825
VERSION     NP_579825.1
DBSOURCE    REFSEQ: accession NM_133291.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Yoshida,M., Kaneko,M., Kurachi,H. and Osawa,M.
  TITLE     Identification of two rodent genes encoding homologues to seminal
            vesicle autoantigen: a gene family including the gene for
            prolactin-inducible protein
  JOURNAL   Biochem Biophys Res Commun 281 (1), 94-100 (2001)
   PUBMED   11178965
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB051831.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB051831.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..144
                     /product="seminal vesicle antigen-like 2 precursor"
                     /calculated_mol_wt=12840
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3233
     Region          3..124
                     /region_name="SVA"
                     /note="Seminal vesicle autoantigen (SVA); pfam05326"
                     /db_xref="CDD:398804"
     CDS             1..144
                     /gene="Sval2"
                     /gene_synonym="SLP-M"
                     /coded_by="NM_133291.1:1..435"
                     /db_xref="GeneID:84605"
                     /db_xref="RGD:620869"
ORIGIN      
        1 maslqmfyqp raamhllilc lfletaygqd iwsnplslel ivsplkkane ftvtlqvknn
       61 vdqcmavkvs tvsnpnikyi sshaiytscl cdvnnyfwdi qviantalqg kaevvpakdi
      121 cpndenifpv tsyigtatqk ifvs
//
LOCUS       NP_001002283             328 aa            linear   ROD 02-APR-2025
DEFINITION  mas-related G-protein coupled receptor member B8 [Rattus
            norvegicus].
ACCESSION   NP_001002283 XP_218594
VERSION     NP_001002283.1
DBSOURCE    REFSEQ: accession NM_001002283.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Zylka,M.J., Dong,X., Southwell,A.L. and Anderson,D.J.
  TITLE     Atypical expansion in mice of the sensory neuron-specific Mrg G
            protein-coupled receptor family
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 10043-10048 (2003)
   PUBMED   12909716
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY266420.1.
            
            On Apr 19, 2005 this sequence version replaced XP_218594.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..328
                     /product="mas-related G-protein coupled receptor member
                     B8"
                     /note="MAS-related G protein-coupled receptor, member B8;
                     MAS-related gene B8"
                     /calculated_mol_wt=36910
     Site            16
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TN50.1)"
     Region          31..308
                     /region_name="7tmA_MrgprB"
                     /note="mas-related G protein-coupled receptor subtype B,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15107"
                     /db_xref="CDD:320235"
     Region          32..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320235"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Region          64..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320235"
     Site            order(85,88,90,104..109,111..112,115,158,160..164,187,
                     190..192,194..196,198..199,236,239..240,242..243,246,
                     258..259,261..263,266,269..270)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320235"
     Region          104..132
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320235"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Region          144..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320235"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Region          187..212
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320235"
     Region          216..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320235"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     Region          259..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320235"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN50.1)"
     CDS             1..328
                     /gene="Mrgprb13"
                     /gene_synonym="MrgB8; Mrgprb8"
                     /coded_by="NM_001002283.1:1..987"
                     /db_xref="GeneID:404643"
                     /db_xref="RGD:738051"
ORIGIN      
        1 mdssipdpea dliqlngsyh tetspcvies rvmillsiii affglagnam vlwllafrmr
       61 rnvfsvyiln laganflflc thtafsleki ivlfhsvhih ipllfytlst laylagvsmv
      121 taisaeywls giwpywyqgq rlkhtttvic tglwglalll sllegkscgf lgstynqdvc
      181 wkldfiivaw llvlfavlsr siqvllvrif cgsqrtpvtk lhvtivltal vlvicgfpfg
      241 iifyllywtt evyyimpcns fhetilllsy inscanpiic llvgsirhcr fqcgtlrlll
      301 hramqdipee egeeleevvg ervqnsip
//
LOCUS       NP_076485                308 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 107 [Rattus norvegicus].
ACCESSION   NP_076485
VERSION     NP_076485.1
DBSOURCE    REFSEQ: accession NM_023995.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sekine,H., Takao,K., Yoshinaga,K., Kokubun,S. and Ikeda,M.
  TITLE     Effects of zinc deficiency and supplementation on gene expression
            of bitter taste receptors (TAS2Rs) on the tongue in rats
  JOURNAL   Laryngoscope 122 (11), 2411-2417 (2012)
   PUBMED   23070743
  REMARK    GeneRIF: Gene expression frequency of TAS2R40 and TAS2R107 on the
            tongue significantly decreased in rats fed a zinc-deficient diet,
            and frequency of TAS2R107 significantly increased following zinc
            administration.
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Singh,N., Vrontakis,M., Parkinson,F. and Chelikani,P.
  TITLE     Functional bitter taste receptors are expressed in brain cells
  JOURNAL   Biochem Biophys Res Commun 406 (1), 146-151 (2011)
   PUBMED   21303656
  REMARK    GeneRIF: T2R4 is localized in the neuronal cells of the rat brain
            stem.
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227142.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227142.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..308
                     /product="taste receptor type 2 member 107"
                     /note="T2R107; taste receptor type 2 member 4; taste
                     receptor T2R4; taste receptor, type 2, member 10"
                     /calculated_mol_wt=34921
     Region          7..290
                     /region_name="7tm_TAS2R10"
                     /note="mammalian taste receptor 2, subtype 10, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15021"
                     /db_xref="CDD:320149"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320149"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320149"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320149"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          131..147
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320149"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          172..195
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320149"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          220..245
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320149"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     Region          257..282
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320149"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT9.1)"
     CDS             1..308
                     /gene="Tas2r107"
                     /gene_synonym="T2R4; Tas2r10"
                     /coded_by="NM_023995.1:1..927"
                     /db_xref="GeneID:78981"
                     /db_xref="RGD:620736"
ORIGIN      
        1 mlsaaegill cvvtseavlg vlgdtfiala ncmeyaknkk lskigfilig laisrigvvw
       61 iiilqgymqv ffphiltfgn iteyityiwv flnhlsvwfa tnlnilyflk ianfsnsvfl
      121 wlksrvrvvf iflsgcllts wllcfpqfsk mlnnskmywg ntswlqqqkn vflinqsltn
      181 lgifffiivs litcfllivf lwrhirqmhs dgsglrdlnt eahvkamrvl isfavlfilh
      241 fvglsiqvlc fflpqnnllf itgliatcly pcghsiilil gnkqlkqasl kalqhltcce
      301 tkrnlsvt
//
LOCUS       NP_996764                493 aa            linear   ROD 02-APR-2025
DEFINITION  amphoterin-induced protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_996764 XP_227582
VERSION     NP_996764.1
DBSOURCE    REFSEQ: accession NM_206881.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Peltola,M.A., Kuja-Panula,J., Liuhanen,J., Voikar,V., Piepponen,P.,
            Hiekkalinna,T., Taira,T., Lauri,S.E., Suvisaari,J., Kulesskaya,N.,
            Paunio,T. and Rauvala,H.
  TITLE     AMIGO-Kv2.1 Potassium Channel Complex Is Associated With
            Schizophrenia-Related Phenotypes
  JOURNAL   Schizophr Bull 42 (1), 191-201 (2016)
   PUBMED   26240432
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Chen,Y., Hor,H.H. and Tang,B.L.
  TITLE     AMIGO is expressed in multiple brain cell types and may regulate
            dendritic growth and neuronal survival
  JOURNAL   J Cell Physiol 227 (5), 2217-2229 (2012)
   PUBMED   21938721
  REMARK    GeneRIF: Data show that AMIGO is a glycosylated protein widely
            expressed in the central nervous system (CNS), and can be found in
            neurons, astrocytes as well as oligodendrocytes.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Peltola,M.A., Kuja-Panula,J., Lauri,S.E., Taira,T. and Rauvala,H.
  TITLE     AMIGO is an auxiliary subunit of the Kv2.1 potassium channel
  JOURNAL   EMBO Rep 12 (12), 1293-1299 (2011)
   PUBMED   22056818
  REMARK    GeneRIF: AMIGO is a function-modulating auxiliary subunit for
            Kv2.1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY237729.1.
            
            On Apr 5, 2004 this sequence version replaced XP_227582.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY237729.1, BC167749.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..493
                     /product="amphoterin-induced protein 1 precursor"
                     /note="amphoterin-induced protein 1; AMIGO-1; alivin-2;
                     amphoretin-induced gene and ORF; transmembrane protein
                     AMIGO"
                     /calculated_mol_wt=52089
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3213
     mat_peptide     28..493
                     /product="Amphoterin-induced protein 1.
                     /evidence=ECO:0000255. /id=PRO_0000014508"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
                     /calculated_mol_wt=52089
     Region          44..64
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..83
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          65..87
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <66..>224
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          87..108
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          88..111
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          111..132
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          112..135
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          135..156
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          136..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          159..179
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..206
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          187..210
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          279..358
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          286..290
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          298..302
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          324..328
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          338..343
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          351..354
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Site            373..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Region          405..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80ZD8; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD7.1)"
     CDS             1..493
                     /gene="Amigo1"
                     /gene_synonym="Amigo"
                     /coded_by="NM_206881.1:1..1482"
                     /db_xref="GeneID:295365"
                     /db_xref="RGD:1303079"
ORIGIN      
        1 mqpqrdlrgl wllllslfll lfevaragrp vvscpanclc asnilscskq qlpnvpqslp
       61 gytalldlsh nnlsrlkaew tptrltnlhs lllshnhlnf isseafvpvp nlryldlssn
      121 hlhtldeflf sglqalevll lynnhivvvd rnafedmaql qklylsqnmi srfplelikd
      181 anrlpkltll dlssnklkkl pltdlqklpa wvknglylhn nplecdckly qlfshwqyrq
      241 lssvmdfqed lycvhskklh nvfsldffnc seykesawea hlgdtltitc dtkqqgmtkv
      301 wvtpsneqvl nqgangtvtv sedgnlhfke vqvedggvyt cyamgetfne tlsvelkvyn
      361 ftlhghhdtl ntayttlvgc ilsvvlvliy lyltpcrcwc rgvekpsshq gdslsssmls
      421 ttpnhdpmag gdkddgfdrr vaflepagpg qgqngklkpg ntlpvpeatg kgqrrmsdpe
      481 svssvfsdtp ivv
//
LOCUS       NP_001020321             319 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 40 [Rattus norvegicus].
ACCESSION   NP_001020321 XP_575452
VERSION     NP_001020321.1
DBSOURCE    REFSEQ: accession NM_001025150.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Tomas,J., Santos,C.R.A., Duarte,A.C., Maltez,M., Quintela,T.,
            Lemos,M.C. and Goncalves,I.
  TITLE     Bitter taste signaling mediated by Tas2r144 is down-regulated by
            17beta-estradiol and progesterone in the rat choroid plexus
  JOURNAL   Mol Cell Endocrinol 495, 110521 (2019)
   PUBMED   31352039
  REMARK    GeneRIF: the bitter receptors Tas2r109, Tas2r144, and the
            taste-related genes Plcb2 and Trpm5 were down-regulated by ovarian
            hormones
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362738.1.
            
            On Jul 1, 2005 this sequence version replaced XP_575452.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..319
                     /product="taste receptor type 2 member 40"
                     /note="T2R18; T2R40; taste receptor type 2 member 18;
                     taste receptor, type 2, member 40"
                     /calculated_mol_wt=36826
     Region          18..307
                     /region_name="7tm_TAS2R40"
                     /note="mammalian taste receptor 2, subtype 40, member of
                     the seven-transmembrane G-protein coupled receptor
                     superfamily; cd15014"
                     /db_xref="CDD:320142"
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          19..44
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320142"
     Region          56..80
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320142"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          94..116
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320142"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          143..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320142"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET2.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          190..213
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320142"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          238..263
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320142"
     Site            252..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     Region          274..299
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320142"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET2.1)"
     CDS             1..319
                     /gene="Tas2r144"
                     /gene_synonym="RGD1562314; Tas2r40"
                     /coded_by="NM_001025150.1:1..960"
                     /db_xref="GeneID:500101"
                     /db_xref="RGD:1562314"
ORIGIN      
        1 maiittdsdy ythryeviip fvvstidciv giigngfitv iygtelvrsk rlptgehlml
       61 mlsfsrlllq iwimveityq lffpmiynhn amyklfktis vflnycnlwf aawlnvfycl
      121 kivnfahplf lmmkqkivvl mprlmslsvl vsislssffs kdifnvymnt svpipfsnst
      181 kmkyffktnv lnlaflyymg ifiplfmfim aaillitslk rhtlnmesst tgsrdssmea
      241 hlgaikstsy slilyiinal alfismsnif gaystwnsvc sfiltaypag qsvhlilrnp
      301 glrrawrrfq hhvrlylkr
//
LOCUS       NP_001002285             314 aa            linear   ROD 02-APR-2025
DEFINITION  MAS-related G protein-coupled receptor, member X2-like [Rattus
            norvegicus].
ACCESSION   NP_001002285 XP_218595
VERSION     NP_001002285.1
DBSOURCE    REFSEQ: accession NM_001002285.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Zylka,M.J., Dong,X., Southwell,A.L. and Anderson,D.J.
  TITLE     Atypical expansion in mice of the sensory neuron-specific Mrg G
            protein-coupled receptor family
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 10043-10048 (2003)
   PUBMED   12909716
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF518240.1.
            
            On Apr 19, 2005 this sequence version replaced XP_218595.3.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..314
                     /product="MAS-related G protein-coupled receptor, member
                     X2-like"
                     /note="MAS-related G protein-coupled receptor, member B2;
                     MAS-related gene B2"
                     /calculated_mol_wt=35575
     Region          9..284
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          11..35
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          43..65
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          82..102
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          125..141
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          162..185
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          199..221
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          235..260
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..314
                     /gene="Mrgprx2l"
                     /gene_synonym="MrgB2; Mrgprb2"
                     /coded_by="NM_001002285.1:1..945"
                     /db_xref="GeneID:404645"
                     /db_xref="RGD:738053"
ORIGIN      
        1 msscgimsct miflsliiai vvlvgnaivi wllgfqmcrn afsiyilnla gadflfigfq
       61 igycfyiifd iytipiklpl ffivmlnfay lcglsilsav sierclcvmr pfwyrcqlpr
      121 htsavictml wvlslvlsls egkecgflpg tnisdwckti dliitswliv lfvvllvssl
      181 alvitifcgl yripvtrlyv vivftvlffl lfglpygiyl fllvwaetfy yvfpcgflpv
      241 tiflscintc anpiiyflvg svrhhrfqrk slklllqqar qdtpeteeyv emgslgrsre
      301 vnslqgtesc fdqa
//
LOCUS       NP_001002287             323 aa            linear   ROD 02-APR-2025
DEFINITION  mas-related G-protein coupled receptor member B4 [Rattus
            norvegicus].
ACCESSION   NP_001002287 XP_579075
VERSION     NP_001002287.1
DBSOURCE    REFSEQ: accession NM_001002287.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Zylka,M.J., Dong,X., Southwell,A.L. and Anderson,D.J.
  TITLE     Atypical expansion in mice of the sensory neuron-specific Mrg G
            protein-coupled receptor family
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 10043-10048 (2003)
   PUBMED   12909716
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF518242.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579075.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..323
                     /product="mas-related G-protein coupled receptor member
                     B4"
                     /note="MAS-related G protein-coupled receptor, member B4;
                     MAS-related gene B4"
                     /calculated_mol_wt=36657
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          31..300
                     /region_name="7tmA_MrgprB"
                     /note="mas-related G protein-coupled receptor subtype B,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15107"
                     /db_xref="CDD:320235"
     Region          32..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320235"
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          64..90
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320235"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Site            order(85,88..89,100..105,107..108,111,154,156..160,183,
                     186..188,190..192,194..195,232,235..236,238..239,242,
                     250..251,253..255,258,261..262)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320235"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          100..128
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320235"
     Region          140..160
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320235"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          183..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320235"
     Region          212..242
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320235"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          251..276
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320235"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     Region          298..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN45.1)"
     CDS             1..323
                     /gene="Mrgprb4"
                     /gene_synonym="MrgB4"
                     /coded_by="NM_001002287.1:1..972"
                     /db_xref="GeneID:404658"
                     /db_xref="RGD:738043"
ORIGIN      
        1 mspttqawsi nntvvkenyy teilscittf ntlnflivii svvgmagnat vlwllgfhmh
       61 rnafsvyvln lagadflylc aqtvyslecv lqfdnsyfyf lltilmfnyl agfcmiaais
      121 terclsvtwp iwyhcqrprh tsatvcalfw afslllslll gqgcgflfsk fdysfcrycn
      181 fiataflivi fmvlfvssla llakiicgsh ripvtrfyvt ialtvlvfif fglpigicvf
      241 llpwihmmls sffyemvtll scvnscanpi iyffvgsirh hrlqrqtlkl llqramqdtp
      301 eeeggergps qksedlevvr css
//
LOCUS       NP_001032823            1628 aa            linear   ROD 02-APR-2025
DEFINITION  transient receptor potential cation channel subfamily M member 1
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001032823
VERSION     NP_001032823.1
DBSOURCE    REFSEQ: accession NM_001037734.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1628)
  AUTHORS   Jirku,M., Lansky,Z., Bednarova,L., Sulc,M., Monincova,L., Majer,P.,
            Vyklicky,L., Vondrasek,J., Teisinger,J. and Bousova,K.
  TITLE     The characterization of a novel S100A1 binding site in the
            N-terminus of TRPM1
  JOURNAL   Int J Biochem Cell Biol 78, 186-193 (2016)
   PUBMED   27435061
  REMARK    GeneRIF: a molecular mechanism for the potential regulation of
            TRPM1 by S100A1
REFERENCE   2  (residues 1 to 1628)
  AUTHORS   Devi,S., Markandeya,Y., Maddodi,N., Dhingra,A., Vardi,N.,
            Balijepalli,R.C. and Setaluri,V.
  TITLE     Metabotropic glutamate receptor 6 signaling enhances TRPM1 calcium
            channel function and increases melanin content in human melanocytes
  JOURNAL   Pigment Cell Melanoma Res 26 (3), 348-356 (2013)
   PUBMED   23452348
REFERENCE   3  (residues 1 to 1628)
  AUTHORS   Thameem,F., Puppala,S., Arar,N.H., Blangero,J., Duggirala,R. and
            Abboud,H.E.
  TITLE     Genetic variants in transient receptor potential cation channel,
            subfamily M 1 (TRPM1) and their risk of albuminuria-related traits
            in Mexican Americans
  JOURNAL   Clin Chim Acta 412 (23-24), 2058-2062 (2011)
   PUBMED   21439949
REFERENCE   4  (residues 1 to 1628)
  AUTHORS   Won,J., Shi,L.Y., Hicks,W., Wang,J., Hurd,R., Naggert,J.K.,
            Chang,B. and Nishina,P.M.
  TITLE     Mouse model resources for vision research
  JOURNAL   J Ophthalmol 2011, 391384 (2011)
   PUBMED   21052544
REFERENCE   5  (residues 1 to 1628)
  AUTHORS   Koike,C., Obara,T., Uriu,Y., Numata,T., Sanuki,R., Miyata,K.,
            Koyasu,T., Ueno,S., Funabiki,K., Tani,A., Ueda,H., Kondo,M.,
            Mori,Y., Tachibana,M. and Furukawa,T.
  TITLE     TRPM1 is a component of the retinal ON bipolar cell transduction
            channel in the mGluR6 cascade
  JOURNAL   Proc Natl Acad Sci U S A 107 (1), 332-337 (2010)
   PUBMED   19966281
REFERENCE   6  (residues 1 to 1628)
  AUTHORS   Morgans,C.W., Zhang,J., Jeffrey,B.G., Nelson,S.M., Burke,N.S.,
            Duvoisin,R.M. and Brown,R.L.
  TITLE     TRPM1 is required for the depolarizing light response in retinal
            ON-bipolar cells
  JOURNAL   Proc Natl Acad Sci U S A 106 (45), 19174-19178 (2009)
   PUBMED   19861548
REFERENCE   7  (residues 1 to 1628)
  AUTHORS   Audo,I., Kohl,S., Leroy,B.P., Munier,F.L., Guillonneau,X.,
            Mohand-Said,S., Bujakowska,K., Nandrot,E.F., Lorenz,B.,
            Preising,M., Kellner,U., Renner,A.B., Bernd,A., Antonio,A.,
            Moskova-Doumanova,V., Lancelot,M.E., Poloschek,C.M., Drumare,I.,
            Defoort-Dhellemmes,S., Wissinger,B., Leveillard,T., Hamel,C.P.,
            Schorderet,D.F., De Baere,E., Berger,W., Jacobson,S.G., Zrenner,E.,
            Sahel,J.A., Bhattacharya,S.S. and Zeitz,C.
  TITLE     TRPM1 is mutated in patients with autosomal-recessive complete
            congenital stationary night blindness
  JOURNAL   Am J Hum Genet 85 (5), 720-729 (2009)
   PUBMED   19896113
REFERENCE   8  (residues 1 to 1628)
  AUTHORS   van Genderen,M.M., Bijveld,M.M., Claassen,Y.B., Florijn,R.J.,
            Pearring,J.N., Meire,F.M., McCall,M.A., Riemslag,F.C., Gregg,R.G.,
            Bergen,A.A. and Kamermans,M.
  TITLE     Mutations in TRPM1 are a common cause of complete congenital
            stationary night blindness
  JOURNAL   Am J Hum Genet 85 (5), 730-736 (2009)
   PUBMED   19896109
REFERENCE   9  (residues 1 to 1628)
  AUTHORS   Li,Z., Sergouniotis,P.I., Michaelides,M., Mackay,D.S., Wright,G.A.,
            Devery,S., Moore,A.T., Holder,G.E., Robson,A.G. and Webster,A.R.
  TITLE     Recessive mutations of the gene TRPM1 abrogate ON bipolar cell
            function and cause complete congenital stationary night blindness
            in humans
  JOURNAL   Am J Hum Genet 85 (5), 711-719 (2009)
   PUBMED   19878917
REFERENCE   10 (residues 1 to 1628)
  AUTHORS   Wang,H.P., Pu,X.Y. and Wang,X.H.
  TITLE     Distribution profiles of transient receptor potential
            melastatin-related and vanilloid-related channels in prostatic
            tissue in rat
  JOURNAL   Asian J Androl 9 (5), 634-640 (2007)
   PUBMED   17712480
  REMARK    GeneRIF: Polymerase chain reaction used to check the expression of
            all TRPM and TRPV channel members with specific primers.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ867482.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ867482.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1628
                     /organism="Rattus norvegicus"
                     /strain="DA"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1628
                     /product="transient receptor potential cation channel
                     subfamily M member 1 isoform 1"
                     /function="putative ion channel protein"
                     /note="melastatin; melastatin-1"
                     /calculated_mol_wt=184188
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          65..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          116..381
                     /region_name="LSDAT_euk"
                     /note="SLOG in TRPM; pfam18139"
                     /db_xref="CDD:465665"
     Region          451..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          618..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          <757..1161
                     /region_name="TRPV"
                     /note="Transient Receptor Potential channel, Vanilloid
                     subfamily (TRPV); cl40437"
                     /db_xref="CDD:454755"
     Region          822..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            876..896
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            943..963
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            974..994
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1007..1027
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1106..1126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1157..1177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          1230..1285
                     /region_name="TRPM_tetra"
                     /note="tetramerization domain of TRPM; pfam16519"
                     /db_xref="CDD:465156"
     Region          1360..1412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          1573..1628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     CDS             1..1628
                     /gene="Trpm1"
                     /coded_by="NM_001037734.1:144..5030"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361586"
                     /db_xref="RGD:1597140"
ORIGIN      
        1 mgsmrkmsss fkrgsiksst sgsqkgqkaw iektfckrec ifvipstkdp nrcccgqltn
       61 qhipplpsvt psstaedtkq gdaqsgkwsv skhtqsyptd sygilefqgg gysnkamyir
      121 vsydtkpdsl lhlmvkdwql elpkllisvh gglqsfemqp klkqvfgkgl ikaamttgaw
      181 iftggvstgv vshvgdalkd hssksrgrlc aigiapwgmv enkedlvgkd vtrvyqtmsn
      241 plsklsvlnn shthfiladn gtlgkygaev klrrqlekhi slqkintrlg qgvpvvglvv
      301 eggpnvvsiv leylredppv pvvvcdgsgr asdilsfahk ycdeggvine slrdqllvti
      361 qktfnysksq shqlfaiime cmkkkelvtv frmgsegqqd vemailtall kgtnvsapdq
      421 lslalawnrv diarsqifvf gphwpplgsl appvdtkvae kekkpptatt kgrgkgkgkk
      481 kgkvkeevee etdprkiell nwvnaleqam ldalvldrvd fvklliengv nmqhfltipr
      541 leelyntrlg ppntlhllvr dvkksnlppd yhislidigl vleylmggay rcnytrksfr
      601 tlynnlfgpk rpkalkllgm eddeppakgk kkkkkkkeee ididvddpav srfqypfhel
      661 mvwavlmkrq kmavflwqrg eecmakalva cklykamahe sseselvddi sqdldnnskd
      721 fgqlavelld qsykhdeqva mklltyelkn wsnstclkla vaakhrdfia htcsqmlltd
      781 mwmgrlrmrk npglkvimgi lipptilfle frsyddfsyq tskenedgke keeenvdana
      841 dagsrkgdee nehkkqrsip igtkicefyn apivkfwfyt isylgylllf nyvilvrmdg
      901 wpspqewivi syivslalek ireilmsepg klsqkikvwl qeywnitdlv aismfmvgai
      961 lrlqnqpymg ygrviycvdi ilwyirvldi fgvnkylgpy vmmigkmmid mlyfvvimlv
     1021 vlmsfgvarq ailhpeekps wklarnifym pywmiygevf adqidrktri hiyameinpp
     1081 cgenlydeeg krlppcipga wltpalmacy llvanillvn lliavfnntf fevksisnqv
     1141 wkfqryqlim tfhdrpvlpp pmiilshiyi ivmrlsgrcr kkregdqeer drglklflsd
     1201 eelkklhefe eqcvqehfre kedeqqsssd erirvtserv enmsmrleei nerenfmkas
     1261 lqtvdlrlsq leelsgrmvg alenlagidr sdliqarsra sseceatyll rqssinsadg
     1321 ysmyryhfng eellfeepal stspgtvfrk ktcsfrvkee dvkphldqps slhhtpgpsp
     1381 patpgrsrla ldgplstelr pgldpgisag eldpradfks aevapslnta nvastqltve
     1441 stvshplres klaryypgdl ntyktmksrs fvysegrklv rglsnwgaey ssimdqtwns
     1501 aewrcqvqri trsrstdipy ivseaasqde fedehresll apqisrsalt vsdrpekenl
     1561 lsvkphqtlg fpclrsrslh ghprsakpsp skldraghas stsnlavmsd apegqntqqe
     1621 kgnpetec
//
LOCUS       NP_001002833             475 aa            linear   ROD 02-APR-2025
DEFINITION  Sumo1/sentrin/SMT3 specific peptidase 17 [Rattus norvegicus].
ACCESSION   NP_001002833 XP_579093
VERSION     NP_001002833.1
DBSOURCE    REFSEQ: accession NM_001002833.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Kamitani,T., Kito,K., Nguyen,H.P., Wada,H., Fukuda-Kamitani,T. and
            Yeh,E.T.
  TITLE     Identification of three major sentrinization sites in PML
  JOURNAL   J Biol Chem 273 (41), 26675-26682 (1998)
   PUBMED   9756909
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000370.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579093.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BN000370.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..475
                     /product="Sumo1/sentrin/SMT3 specific peptidase 17"
                     /function="SUMO cysteine protease"
                     /note="Sumo1/sentrin/Smt3 specific protease 17; sentrin
                     17"
                     /calculated_mol_wt=54094
     Region          <244..470
                     /region_name="Peptidase_C48"
                     /note="Ulp1 protease family, C-terminal catalytic domain;
                     cl23802"
                     /db_xref="CDD:420019"
     CDS             1..475
                     /gene="Senp17"
                     /coded_by="NM_001002833.1:1..1428"
                     /db_xref="GeneID:408216"
                     /db_xref="RGD:1303080"
ORIGIN      
        1 mwqpkqpgvg mkpeaseqrr krkhldqsgt etesealgqg pswncqggtq mvfqkpgkar
       61 kktrqehqdq klkkeqpgkg qgqktqeegs gnikplecqp dqtvveklae ggkcrkrqys
      121 vlqekpqspq nekharsleh lqgghpvrsd phrphptfsd tsnnkggmpg hphgretahg
      181 drqpstevls tkrekrcaee kcvrgnsleh glrgtenani ldsgggrllp dkvavvagek
      241 nalpeqennq ekeftkemek evekalgpga qeeilstgfk lkitrgdmqt lkngqwpnde
      301 iinfymnllv qrnenqgypa lhafstffya klkhggynsv krwtrginlf ekelilvpih
      361 qrvhwslvvi dlrkrsivyl dsmgqtgkni cetifhylqn esktrrnmel dpvewkqysl
      421 tsqeipqqln gsdcgmftck yadyisrdqp vtfsqqhmpl frrrmvweil hshll
//
LOCUS       NP_001074406             295 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 120 [Rattus norvegicus].
ACCESSION   NP_001074406 XP_001074477
VERSION     NP_001074406.1
DBSOURCE    REFSEQ: accession NM_001080937.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362737.1.
            
            On Jan 31, 2007 this sequence version replaced XP_001074477.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..295
                     /product="taste receptor type 2 member 120"
                     /note="putative taste receptor T2R17; T2R120; taste
                     receptor type 2 member 17"
                     /calculated_mol_wt=33447
     Region          3..279
                     /region_name="7tm_TAS2R43-like"
                     /note="mammalian taste receptor 2, subtype 43, and related
                     proteins, member of the seven-transmembrane G
                     protein-coupled receptor superfamily; cd15027"
                     /db_xref="CDD:320155"
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          7..32
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320155"
     Region          44..68
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320155"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          81..103
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320155"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          130..146
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320155"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          172..195
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320155"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          220..245
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320155"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     Region          254..279
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320155"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET3.1)"
     CDS             1..295
                     /gene="Tas2r120"
                     /coded_by="NM_001080937.1:1..888"
                     /db_xref="GeneID:690448"
                     /db_xref="RGD:1596060"
ORIGIN      
        1 mdltewivti immiefllgn canffimvvn aidcmkrrki ssadriital aisrigllwa
       61 mlmnwhsrvy ttdtysfqvt afsgiiwait nhfttwlgti lsmfylfkia nfsnclflhl
      121 krkldsvllv iflvssllvf aylgvvnikk iawlsvhegn vtvksklmni asirdtllfs
      181 liniapfgis ltcvllliys lgkhlknmkf ygkgcqdqst mvhiralqtv vsflllyaty
      241 sscviisgws iqnvpiflfc vtigafypag hsciliwgnq klkqflllfl rqmkc
//
LOCUS       NP_783175                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7a [Rattus norvegicus].
ACCESSION   NP_783175
VERSION     NP_783175.1
DBSOURCE    REFSEQ: accession NM_175585.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Shows that expression of Taar family members is limited to
            specific tissue subpopulations and developmental stages in mouse.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380196.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7a"
                     /note="taR-8; taR-7a; trace amine receptor 7a; trace amine
                     receptor 8"
                     /calculated_mol_wt=40016
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y2.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320439"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320439"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320439"
     Site            122..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320439"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320439"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y2.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320439"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320439"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y2.1)"
     CDS             1..358
                     /gene="Taar7a"
                     /gene_synonym="Ta8"
                     /coded_by="NM_175585.1:1..1077"
                     /db_xref="GeneID:294125"
                     /db_xref="RGD:631387"
ORIGIN      
        1 mdklvdnfls gqsrtmsedl lsasspqlcy enlngscirs pyspgprlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadflvgltv mpfstvrsve gcwyfgdtyc
      121 kfhscfegsf cyssifhlcf isvdryiavs dpliyptrft asvsgkcitf swllsiiysf
      181 sllytganea gledlvsalt cvggcqiavn qswvfinfll flvptlvmmt vyskifliak
      241 qqaqniekms kqttrasesy kdrvakrerk aaktlgiava afllswlpyf idsiidaflg
      301 fitptyvyei lvwiayynsa mnpliyaffy pwfrkaikli vtgkilrqns svtnlfpe
//
LOCUS       NP_076489                309 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 105 [Rattus norvegicus].
ACCESSION   NP_076489
VERSION     NP_076489.1
DBSOURCE    REFSEQ: accession NM_023999.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bufe,B., Hofmann,T., Krautwurst,D., Raguse,J.D. and Meyerhof,W.
  TITLE     The human TAS2R16 receptor mediates bitter taste in response to
            beta-glucopyranosides
  JOURNAL   Nat Genet 32 (3), 397-401 (2002)
   PUBMED   12379855
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227146.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227146.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..309
                     /product="taste receptor type 2 member 105"
                     /note="T2R105; taste receptor type 2 member 9; taste
                     receptor T2R9"
                     /calculated_mol_wt=35018
     Region          7..291
                     /region_name="7tm_TAS2R10"
                     /note="mammalian taste receptor 2, subtype 10, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15021"
                     /db_xref="CDD:320149"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320149"
     Site            10..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320149"
     Site            45..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320149"
     Site            87..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Site            130..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          131..147
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320149"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          173..196
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320149"
     Site            178..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          221..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320149"
     Site            227..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320149"
     Site            259..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT5.1)"
     CDS             1..309
                     /gene="Tas2r105"
                     /gene_synonym="T2R9"
                     /coded_by="NM_023999.1:1..930"
                     /db_xref="GeneID:78985"
                     /db_xref="RGD:620741"
ORIGIN      
        1 mlsaaegill siatveaglg vlgntfialv ncmdwaknkk lskigfllfg latsrifivw
       61 ilildayakl ffpgkylsks lteiisciwm tvnhmtvwfa tslsifyflk ianfshyifl
      121 wlkrrtdkvf afllwcllis waisfsftvk vmksnpknhg nrtsgthwek reftsnyvli
      181 nigvisllim tltacfllii slwkhsrqmq snvsgfrdln teahvkaikf lisfiilfil
      241 yfigvaveii cmfipenkll fifglttasv ypcchsvili ltnsqlkqaf vkvleglkfs
      301 engkdlrat
//
LOCUS       NP_001102944             230 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC685544 [Rattus norvegicus].
ACCESSION   NP_001102944 XP_001064244
VERSION     NP_001102944.1
DBSOURCE    REFSEQ: accession NM_001109474.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473953.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001064244.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..230
                     /product="uncharacterized protein LOC685544"
                     /calculated_mol_wt=20440
     CDS             1..230
                     /gene="Krtap5-8"
                     /coded_by="NM_001109474.1:1..693"
                     /db_xref="GeneID:685544"
                     /db_xref="RGD:1592604"
ORIGIN      
        1 mtccgcsggc gsscggcgss cggcgsscgg cgsccggcgs ccckpvcccv pvcscsscgg
       61 ckggcgscgg csscggckgg cgscggckgg cgscggckgg cgscggckgg cgscggcssc
      121 ggckggcgsc ggckggcgsc ggckggcgsc ggckggccqs scckpcccqs scckpccssg
      181 cgssccqssc ckpcccqssc ckpcccqssc ckpcccqssc capvccqcki
//
LOCUS       NP_001019409            1486 aa            linear   ROD 02-APR-2025
DEFINITION  bifunctional glutamate/proline--tRNA ligase isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001019409 XP_213969
VERSION     NP_001019409.1
DBSOURCE    REFSEQ: accession NM_001024238.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1486)
  AUTHORS   Arif,A., Terenzi,F., Potdar,A.A., Jia,J., Sacks,J., China,A.,
            Halawani,D., Vasu,K., Li,X., Brown,J.M., Chen,J., Kozma,S.C.,
            Thomas,G. and Fox,P.L.
  TITLE     EPRS is a critical mTORC1-S6K1 effector that influences adiposity
            in mice
  JOURNAL   Nature 542 (7641), 357-361 (2017)
   PUBMED   28178239
REFERENCE   2  (residues 1 to 1486)
  AUTHORS   Forster,F., Paster,W., Supper,V., Schatzlmaier,P., Sunzenauer,S.,
            Ostler,N., Saliba,A., Eckerstorfer,P., Britzen-Laurent,N.,
            Schutz,G., Schmid,J.A., Zlabinger,G.J., Naschberger,E., Sturzl,M.
            and Stockinger,H.
  TITLE     Guanylate binding protein 1-mediated interaction of T cell antigen
            receptor signaling with the cytoskeleton
  JOURNAL   J Immunol 192 (2), 771-781 (2014)
   PUBMED   24337748
REFERENCE   3  (residues 1 to 1486)
  AUTHORS   Son,J., Lee,E.H., Park,M., Kim,J.H., Kim,J., Kim,S., Jeon,Y.H. and
            Hwang,K.Y.
  TITLE     Conformational changes in human prolyl-tRNA synthetase upon binding
            of the substrates proline and ATP and the inhibitor halofuginone
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 10), 2136-2145 (2013)
   PUBMED   24100331
REFERENCE   4  (residues 1 to 1486)
  AUTHORS   Zhou,H., Sun,L., Yang,X.L. and Schimmel,P.
  TITLE     ATP-directed capture of bioactive herbal-based medicine on human
            tRNA synthetase
  JOURNAL   Nature 494 (7435), 121-124 (2013)
   PUBMED   23263184
REFERENCE   5  (residues 1 to 1486)
  AUTHORS   Arif,A., Chatterjee,P., Moodt,R.A. and Fox,P.L.
  TITLE     Heterotrimeric GAIT complex drives transcript-selective translation
            inhibition in murine macrophages
  JOURNAL   Mol Cell Biol 32 (24), 5046-5055 (2012)
   PUBMED   23071094
REFERENCE   6  (residues 1 to 1486)
  AUTHORS   Kaminska,M., Havrylenko,S., Decottignies,P., Le Marechal,P.,
            Negrutskii,B. and Mirande,M.
  TITLE     Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the
            Cytoplasm of Human Cells
  JOURNAL   J Biol Chem 284 (20), 13746-13754 (2009)
   PUBMED   19289464
REFERENCE   7  (residues 1 to 1486)
  AUTHORS   Kaminska,M., Havrylenko,S., Decottignies,P., Gillet,S., Le
            Marechal,P., Negrutskii,B. and Mirande,M.
  TITLE     Dissection of the structural organization of the aminoacyl-tRNA
            synthetase complex
  JOURNAL   J Biol Chem 284 (10), 6053-6060 (2009)
   PUBMED   19131329
REFERENCE   8  (residues 1 to 1486)
  AUTHORS   Sampath,P., Mazumder,B., Seshadri,V., Gerber,C.A., Chavatte,L.,
            Kinter,M., Ting,S.M., Dignam,J.D., Kim,S., Driscoll,D.M. and
            Fox,P.L.
  TITLE     Noncanonical function of glutamyl-prolyl-tRNA synthetase:
            gene-specific silencing of translation
  JOURNAL   Cell 119 (2), 195-208 (2004)
   PUBMED   15479637
REFERENCE   9  (residues 1 to 1486)
  AUTHORS   Kim,J.Y., Kang,Y.S., Lee,J.W., Kim,H.J., Ahn,Y.H., Park,H., Ko,Y.G.
            and Kim,S.
  TITLE     p38 is essential for the assembly and stability of macromolecular
            tRNA synthetase complex: implications for its physiological
            significance
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7912-7916 (2002)
   PUBMED   12060739
REFERENCE   10 (residues 1 to 1486)
  AUTHORS   Ko,Y.G., Kang,Y.S., Kim,E.K., Park,S.G. and Kim,S.
  TITLE     Nucleolar localization of human methionyl-tRNA synthetase and its
            role in ribosomal RNA synthesis
  JOURNAL   J Cell Biol 149 (3), 567-574 (2000)
   PUBMED   10791971
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY383705.1.
            
            On May 30, 2005 this sequence version replaced XP_213969.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY383705.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN13663622,
                                           SAMN13663629 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1486
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..1486
                     /product="bifunctional glutamate/proline--tRNA ligase
                     isoform 1"
                     /note="bifunctional aminoacyl-tRNA synthetase;
                     bifunctional glutamate/proline--tRNA ligase; proline--tRNA
                     ligase-like"
                     /calculated_mol_wt=166651
     Region          30..685
                     /region_name="PLN02907"
                     /note="glutamate-tRNA ligase"
                     /db_xref="CDD:215492"
     Region          727..776
                     /region_name="WEPRS_RNA"
                     /note="WEPRS_RNA binding domain. This short RNA-binding
                     domain is found in several higher eukaryote aminoacyl-tRNA
                     synthetases (aaRSs). It is found in multiple copies in
                     eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases
                     (EPRS) in a region that separates...; cd00936"
                     /db_xref="CDD:238473"
     Site            order(734,736,739,744,749,753,761,769)
                     /site_type="other"
                     /note="tRNA binding site [nucleotide binding]"
                     /db_xref="CDD:238473"
     Region          800..849
                     /region_name="WEPRS_RNA"
                     /note="WEPRS_RNA binding domain. This short RNA-binding
                     domain is found in several higher eukaryote aminoacyl-tRNA
                     synthetases (aaRSs). It is found in multiple copies in
                     eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases
                     (EPRS) in a region that separates...; cd00936"
                     /db_xref="CDD:238473"
     Site            order(807,809,812,817,822,826,834,842)
                     /site_type="other"
                     /note="tRNA binding site [nucleotide binding]"
                     /db_xref="CDD:238473"
     Region          878..930
                     /region_name="WHEP-TRS"
                     /note="WHEP-TRS domain; pfam00458"
                     /db_xref="CDD:459819"
     Region          992..1486
                     /region_name="proS_fam_I"
                     /note="prolyl-tRNA synthetase, family I; TIGR00408"
                     /db_xref="CDD:273062"
     CDS             1..1486
                     /gene="Eprs1"
                     /gene_synonym="Eprs"
                     /coded_by="NM_001024238.1:1..4461"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289352"
                     /db_xref="RGD:1310952"
ORIGIN      
        1 maalcltvna gnpplgcrvk vnkrnksfml sfleallave hvkgdvsisv eegkenllrv
       61 sesvvftdtn silrylarva atsglygsnl mehteidhwl efsatklssc dvltsaikel
      121 nhclslrtyl vgnsltladl cvwatlkgna acqehlrqsk tlvhvnrwyg fleaqqafrs
      181 vgtkwdasan katgapdrkq digkfvelpg aemgkvtvrf ppeasgylhi ghakaallnq
      241 hyqvnfkgkl imrfddtnpe kekedfekvi ledvamlhik pdqftytsdh fetimkyaek
      301 lieegkayvd dtpademkae pveknlqmwe emkrgsqfgq scclrakidm ssnngcmrdp
      361 tlyrckiqph prtgnkynvy ptydfacpiv dsiegvthal rtteyhdrde qfywiiealg
      421 irkpyiweys rlnlnntvls krkltwfvne glgssrsvvn mewdkiwafn kkvidpvapr
      481 yvallkkevi pvnildaqee mkevarhpkn pdvglkpvwy spkvfiegad aetfsegemv
      541 tfinwgnini tkihknpdgk itsldaklnl enkdykkttk itwlaettqa lpvpavcvty
      601 ehlitkpvlg kdedfkqyvn kdskheelml gdpclkdlkk gdiiqlqrrg fficdqpyep
      661 vspysckeap ciliyipdgh tkemptsgsk ektkveiskk etgsapkerp aaavsapcaa
      721 aedaailysr vavqgdavrd lkakkapked idaavkqllt lkaeykektg qeyrpgnppt
      781 aavqtvstks psntgeytsl ynkvaaqgel vrklkaekap kakindavec llslkaeyke
      841 ktgkeyvpgq lpasqnshss pvsnakpvgs etpeakllfd rvacqgevvr klkaekaskd
      901 qvdsavqell qlkaqykslt gieykpvsat gaedkdkkkk ekenksekqn kpqkqndgqg
      961 kdssksqgsg lssggagegq gpkkqtrlgl eakkeenlae wysqvitkse mieyydvsgc
     1021 yilrpwsysi wesikdffda eikklgvenc yfpifvsqga lekeknhiad fapevawvtr
     1081 sgktelaepi airptsetvm ypayakwvqs hrdlpirlnq wcnvvrwefk hpqpflrtre
     1141 flwqeghsaf atfeeaadev lqilelyarv yeellaipvv rgrktekekf aggdytttle
     1201 afisasgrai qgatshhlgq nfskmceivf edpktpgekq fayqcswglt trtigvmimv
     1261 hgdnmglvlp prvasvqvvv ipcgitntls eedrealmak cneyrrrllg adirarvdlr
     1321 dnyspgwkfn hwelkgvpvr levgprdmks cqfvavrrdt gekltiaeke aesklkgvle
     1381 diqlnlftra sedlkshmvv sdtledfqkv ldsgkvaqip fcgeidcedw ikkttardqd
     1441 vepgapsmga kslcipfnpl celqpgamcv cgknpakfyt lfgrsy
//
LOCUS       NP_001008853             332 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class I, locus M6, gene 2 precursor [Rattus norvegicus].
ACCESSION   NP_001008853 XP_345077
VERSION     NP_001008853.1
DBSOURCE    REFSEQ: accession NM_001008853.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Lambracht-Washington,D., Moore,Y.F., Wonigeit,K. and Lindahl,K.F.
  TITLE     Structure and expression of MHC class Ib genes of the central M
            region in rat and mouse: M4, M5, and M6
  JOURNAL   Immunogenetics 60 (3-4), 131-145 (2008)
   PUBMED   18324395
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BX883052.1.
            
            On Jan 5, 2005 this sequence version replaced XP_345077.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN09345238, SAMN09345329
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..332
                     /product="RT1 class I, locus M6, gene 2 precursor"
                     /note="MHC class Ib antigen"
                     /calculated_mol_wt=35428
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2282
     Region          29..187
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          191..284
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          192..199
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          207..216
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(210,212,241..242,244..246,252,254)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(217..219,249,274)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          221..226
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          229..234
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          238..246
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          249..259
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          266..273
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          280..283
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     Region          288..319
                     /region_name="TM_EGFR-like"
                     /note="Transmembrane domain of the Epidermal Growth Factor
                     Receptor family of Protein Tyrosine Kinases; cd12087"
                     /db_xref="CDD:213052"
     Site            order(289,292..293,296..297,299..300,302..303,306)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:213052"
     CDS             1..332
                     /gene="RT1-M6-2"
                     /coded_by="NM_001008853.1:1..999"
                     /db_xref="GeneID:365527"
                     /db_xref="RGD:1595815"
ORIGIN      
        1 mgapvlhatl lllsaflalt qtknqsfags hsrqylvtat tsrpglrdph vfivgyvdhm
       61 pfmrfdsdgv aqriqargpw vkqmgpeyle merknaerys hrarenlrfa iqvynqsdkg
      121 hhrhafdgqh yislnsdltt wsvadstaqi tkrrweadgv aeafshflkv scvewlqkhl
      181 etgketlqrs dppkthvthh prpegdatlr cwaldfypad itltwqeeee eeeltqdmel
      241 vetrpagdgt fqkwasvvvp sgeeqkytch vyheglpepl tlrwkpatwp vvgitvgvvl
      301 lgfvtigali aivtmrkkra dpvdpvdlmd pv
//
LOCUS       NP_075232                994 aa            linear   ROD 02-APR-2025
DEFINITION  tyrosine-protein kinase Mer precursor [Rattus norvegicus].
ACCESSION   NP_075232
VERSION     NP_075232.1
DBSOURCE    REFSEQ: accession NM_022943.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Su,X., Chen,W., Fu,Y., Wu,B., Mao,F., Zhao,Y., Yang,Q. and Lan,D.
  TITLE     Protective Role of MerTK in Diabetic Peripheral Neuropathy via
            Inhibition of the NF-kappaB Signaling Pathway
  JOURNAL   Exp Clin Endocrinol Diabetes 132 (7), 396-406 (2024)
   PUBMED   38588709
  REMARK    GeneRIF: Protective Role of MerTK in Diabetic Peripheral Neuropathy
            via Inhibition of the NF-kappaB Signaling Pathway.
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Edvinsson,J.C.A., Ran,C., Olofsgard,F.J., Steinberg,A.,
            Edvinsson,L. and Belin,A.C.
  TITLE     MERTK in the rat trigeminal system: a potential novel target for
            cluster headache?
  JOURNAL   J Headache Pain 25 (1), 85 (2024)
   PUBMED   38783191
  REMARK    GeneRIF: MERTK in the rat trigeminal system: a potential novel
            target for cluster headache?
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Pele,T., Giraud,S., Joffrion,S., Ameteau,V., Delwail,A.,
            Goujon,J.M., Macchi,L., Hauet,T., Dkhissi,F. and Benzakour,O.
  TITLE     Study of the Role of the Tyrosine Kinase Receptor MerTK in the
            Development of Kidney Ischemia-Reperfusion Injury in RCS Rats
  JOURNAL   Int J Mol Sci 22 (22), 12103 (2021)
   PUBMED   34829984
  REMARK    GeneRIF: Study of the Role of the Tyrosine Kinase Receptor MerTK in
            the Development of Kidney Ischemia-Reperfusion Injury in RCS Rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 994)
  AUTHORS   Mao,Y. and Finnemann,S.C.
  TITLE     Acute RhoA/Rho Kinase Inhibition Is Sufficient to Restore
            Phagocytic Capacity to Retinal Pigment Epithelium Lacking the
            Engulfment Receptor MerTK
  JOURNAL   Cells 10 (8), 1927 (2021)
   PUBMED   34440696
  REMARK    GeneRIF: Acute RhoA/Rho Kinase Inhibition Is Sufficient to Restore
            Phagocytic Capacity to Retinal Pigment Epithelium Lacking the
            Engulfment Receptor MerTK.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 994)
  AUTHORS   Lorach,H., Kang,S., Dalal,R., Bhuckory,M.B., Quan,Y. and
            Palanker,D.
  TITLE     Long-term Rescue of Photoreceptors in a Rodent Model of Retinitis
            Pigmentosa Associated with MERTK Mutation
  JOURNAL   Sci Rep 8 (1), 11312 (2018)
   PUBMED   30054542
  REMARK    GeneRIF: The long-term preservation of photoreceptors we observed
            indicates that MERTK-related form of inherited retinal
            degeneration, which has currently no cure, could be amenable to
            laser therapy or subretinal surgery, to extend the visual function,
            potentially for life.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 994)
  AUTHORS   Vollrath,D., Feng,W., Duncan,J.L., Yasumura,D., D'Cruz,P.M.,
            Chappelow,A., Matthes,M.T., Kay,M.A. and LaVail,M.M.
  TITLE     Correction of the retinal dystrophy phenotype of the RCS rat by
            viral gene transfer of Mertk
  JOURNAL   Proc Natl Acad Sci U S A 98 (22), 12584-12589 (2001)
   PUBMED   11592982
REFERENCE   7  (residues 1 to 994)
  AUTHORS   Lu,Q. and Lemke,G.
  TITLE     Homeostatic regulation of the immune system by receptor tyrosine
            kinases of the Tyro 3 family
  JOURNAL   Science 293 (5528), 306-311 (2001)
   PUBMED   11452127
REFERENCE   8  (residues 1 to 994)
  AUTHORS   D'Cruz,P.M., Yasumura,D., Weir,J., Matthes,M.T., Abderrahim,H.,
            LaVail,M.M. and Vollrath,D.
  TITLE     Mutation of the receptor tyrosine kinase gene Mertk in the retinal
            dystrophic RCS rat
  JOURNAL   Hum Mol Genet 9 (4), 645-651 (2000)
   PUBMED   10699188
REFERENCE   9  (residues 1 to 994)
  AUTHORS   Lu,Q., Gore,M., Zhang,Q., Camenisch,T., Boast,S., Casagranda,F.,
            Lai,C., Skinner,M.K., Klein,R., Matsushima,G.K., Earp,H.S.,
            Goff,S.P. and Lemke,G.
  TITLE     Tyro-3 family receptors are essential regulators of mammalian
            spermatogenesis
  JOURNAL   Nature 398 (6729), 723-728 (1999)
   PUBMED   10227296
REFERENCE   10 (residues 1 to 994)
  AUTHORS   Fernando,C.C. and Fraser,H.H.
  TITLE     Technical report: fallopian tube recanalization facilitated by a
            hydrophillic glide wire
  JOURNAL   Australas Radiol 36 (4), 323 (1992)
   PUBMED   1299193
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF208235.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF208235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Rattus norvegicus"
                     /strain="RCS-rdy+"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..994
                     /product="tyrosine-protein kinase Mer precursor"
                     /EC_number="2.7.10.1"
                     /note="proto-oncogene tyrosine-protein kinase MER;
                     tyrosine-protein kinase Mer; retinal dystrophy; receptor
                     tyrosine kinase MerTK; proto-oncogene c-Mer; Receptor
                     tyrosine tinase gene probably the gene for Rdy; c-mer
                     proto-oncogene tyrosine kinase"
                     /calculated_mol_wt=107491
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
                     /calculated_mol_wt=1951
     mat_peptide     19..994
                     /product="Tyrosine-protein kinase Mer. /id=PRO_0000024445"
                     /note="propagated from UniProtKB/Swiss-Prot (P57097.1)"
                     /calculated_mol_wt=107491
     Region          24..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57097.1)"
     Region          96..189
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          105..109
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          122..126
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          153..157
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          167..172
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          181..184
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..274
                     /region_name="IgI_2_Axl_Tyro3_like"
                     /note="Second immunoglobulin (Ig)-like domain of Axl/Tyro3
                     family receptor tyrosine kinases (RTKs); member of the
                     I-set of Ig superfamily (IgSF) domains; cd05749"
                     /db_xref="CDD:409407"
     Region          193..196
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409407"
     Region          199..203
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409407"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          207..216
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409407"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          221..228
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409407"
     Site            229
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          230..233
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409407"
     Region          238..249
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409407"
     Region          252..261
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409407"
     Site            260..265
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409407"
     Site            order(263..265,267)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409407"
     Region          265..274
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409407"
     Region          279..373
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(279,346,361)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            order(362..363,365..366)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          381..473
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            384
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            order(464..465,467..468)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            498..518
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57097.1)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12866; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Region          574..857
                     /region_name="PTKc_Mer"
                     /note="Catalytic Domain of the Protein Tyrosine Kinase,
                     Mer; cd14204"
                     /db_xref="CDD:271106"
     Site            order(588..592,596,612,614,645,667..669,673,718,722..723,
                     725,736,754..758,767,801)
                     /site_type="active"
                     /db_xref="CDD:271106"
     Site            order(588..589,596,612,645,667..669,673,718,722..723,725,
                     736)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271106"
     Site            order(718,722,754..758,767,801)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271106"
     Site            735..760
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271106"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q12866; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q12866; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q12866; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     Site            867
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q60805; propagated from
                     UniProtKB/Swiss-Prot (P57097.1)"
     CDS             1..994
                     /gene="Mertk"
                     /gene_synonym="rdy"
                     /coded_by="NM_022943.1:40..3024"
                     /db_xref="GeneID:65037"
                     /db_xref="RGD:69283"
ORIGIN      
        1 mvlaplllgl lllsalwngg taekeeeikp dqpfsgplpg slpadhrpff aphssgdqls
       61 psqtgrshpa htatpqmtsa asnllppvaf kntigrivls ehksvkfncs inipnvyqet
      121 agiswwkdgk ellgahhsit qfypdeegvs iialfsitsv qrsdngsyic kmkvndrevv
      181 sdpiyvevqg lpyftkqpes vnvtrntafn ltcqavgppe pvnifwvqns srvnenpers
      241 psvltvaglt etavfsceah ndkgltvskg vqinikvips pptevhilns tahsilvswv
      301 pgfdgysplq ncsiqvkead qlsngsvmvf ntsasphlye vqqlqalany svtvscrnei
      361 gwsavspwil asttegapav aplnitvfln essnnleirw tkppikrqdg elvgyrishv
      421 wesagtskel seevsqngsw aqvpvqmhna tctvriavit kggigpfsep vdvaipehsr
      481 vdyapsstpa pgntesmlii lgcfcgfvlm glilylslai krrvqetkfg gafseedsql
      541 vvnyrakksf crraieltlq slgvseelqn kledvvvdrn llilgkvlge gefgsvmegn
      601 lkqedgtsqk vavktmkldn fslreieefl seaacmkdfn hpnvirllgv cielssqgip
      661 kpmvilpfmk ygdlhtflly sriesvpksi plqtllkfmv diaqgmeyls srnflhrdla
      721 arncmlrddm tvcvadfgls kkiysgdyyr qgriakmpvk wiaiesladr vytsksdvwa
      781 fgvtmweiat rgmtpypgvq nhemydyllh ghrlkqpedc lddlyeimys cwsadpldrp
      841 tfsvlrlqle klseslpdaq dkesiiyint qllescegla nrsslagldm nidpdsiias
      901 ctagaavsvv maevhennlh eeryilnggn eewedvastp fatvtagkdg vlpedrltkn
      961 giswshhstl plgspspdel lfaddssgds evlm
//
LOCUS       NP_076483                335 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 119 [Rattus norvegicus].
ACCESSION   NP_076483
VERSION     NP_076483.1
DBSOURCE    REFSEQ: accession NM_023993.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Dehkordi,O., Rose,J.E., Fatemi,M., Allard,J.S., Balan,K.V.,
            Young,J.K., Fatima,S., Millis,R.M. and Jayam-Trouth,A.
  TITLE     Neuronal expression of bitter taste receptors and downstream
            signaling molecules in the rat brainstem
  JOURNAL   Brain Res 1475, 1-10 (2012)
   PUBMED   22836012
  REMARK    GeneRIF: T2R1, a receptor for bitter taste, is expressed in
            brainstem.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227140.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227140.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..335
                     /product="taste receptor type 2 member 119"
                     /note="T2R19; T2R119; taste receptor type 2 member 1;
                     taste receptor type 2 member 19"
                     /calculated_mol_wt=37721
     Region          7..287
                     /region_name="7tm_TAS2R1"
                     /note="mammalian taste receptor 2, subtype 1, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15016"
                     /db_xref="CDD:320144"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320144"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320144"
     Region          79..101
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320144"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          128..144
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320144"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          171..194
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320144"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          218..243
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320144"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          254..279
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320144"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     Region          308..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU1.1)"
     CDS             1..335
                     /gene="Tas2r119"
                     /gene_synonym="T2R1; Tas2r1"
                     /coded_by="NM_023993.1:1..1008"
                     /db_xref="GeneID:78979"
                     /db_xref="RGD:620733"
ORIGIN      
        1 mmeghilfff lvvmvqfvtg vlanglivvv haidlimwkk mapldlllfc latsriilql
       61 cilfaqlclf slvrhtlfed nitfvfiine lslwfatwlg vfycakiati phplflwlkm
      121 risrlvpwli lgsvlyviit tfihsretsa ilkpifislf pknatqvgtg hatllsvlvl
      181 gltlplfift vavllliysl wnysrqmrtm vgtreysgha hisamlsils flilylshym
      241 vavlistqvl ylgsrtfvfc llvigmypsi hsivlilgnp klkrnakmfi vhckcchctr
      301 awvtsrsprl sdlpvppthp sanktscsea cimps
//
LOCUS       NP_001008852             330 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class I, locus M6, gene 1 precursor [Rattus norvegicus].
ACCESSION   NP_001008852 XP_579246
VERSION     NP_001008852.1
DBSOURCE    REFSEQ: accession NM_001008852.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Lambracht-Washington,D., Moore,Y.F., Wonigeit,K. and Lindahl,K.F.
  TITLE     Structure and expression of MHC class Ib genes of the central M
            region in rat and mouse: M4, M5, and M6
  JOURNAL   Immunogenetics 60 (3-4), 131-145 (2008)
   PUBMED   18324395
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Lambracht-Washington,D. and Fischer Lindahl,K.
  TITLE     Active MHC class Ib genes in rat are pseudogenes in the mouse
  JOURNAL   Immunogenetics 56 (2), 118-121 (2004)
   PUBMED   15069589
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BX883052.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579246.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..330
                     /product="RT1 class I, locus M6, gene 1 precursor"
                     /note="MHC class Ib antigen"
                     /calculated_mol_wt=34700
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2282
     Region          29..187
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          189..283
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          207..211
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409606"
     Region          222..226
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409606"
     Region          253..257
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409606"
     Region          264..269
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409606"
     Region          279..282
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409606"
     Region          286..317
                     /region_name="TM_EGFR-like"
                     /note="Transmembrane domain of the Epidermal Growth Factor
                     Receptor family of Protein Tyrosine Kinases; cd12087"
                     /db_xref="CDD:213052"
     Site            order(287,290..291,294..295,297..298,300..301,304)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:213052"
     CDS             1..330
                     /gene="RT1-M6-1"
                     /gene_synonym="RT1-M6"
                     /coded_by="NM_001008852.1:1..993"
                     /db_xref="GeneID:414785"
                     /db_xref="RGD:1598232"
ORIGIN      
        1 mgapvlhatl lllsaflalt qtknqsfags hfmqylvttt ssqpglqdsh vcivghvdym
       61 pfmrfdsdga aqriqtrgpw mkqmgpeyle merknaegys hrarenlrfa iqvynqsdka
      121 hyshafdgqh yislnsdltt wsvgdstaqi tkrrweadgv aealshflkv scvehlqkhl
      181 etgketlqrs dppkahvtlh prpegdvtlr cwalgfypad itltwqlnge dltqdmelve
      241 trpagdgtfq kwasvvvpng eeqkytclve heglpepltl rwkpatwpvv gitvgvvllg
      301 fviigaliai vtmrkkradp vdpvdlmdpv
//
LOCUS       NP_001099419             287 aa            linear   ROD 02-APR-2025
DEFINITION  complement C1q-like protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001099419 XP_001054566 XP_222564
VERSION     NP_001099419.1
DBSOURCE    REFSEQ: accession NM_001105949.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474028.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001054566.1, XP_222564.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q11"
     Protein         1..287
                     /product="complement C1q-like protein 2 precursor"
                     /note="complement C1q-like protein 2; complement component
                     1, q subcomponent-like 2; adiponectin i"
                     /calculated_mol_wt=27310
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2001
     Region          160..284
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..287
                     /gene="C1ql2"
                     /gene_synonym="Adii"
                     /coded_by="NM_001105949.1:90..953"
                     /db_xref="GeneID:288979"
                     /db_xref="RGD:1594583"
ORIGIN      
        1 malglliavp lllqaappga ahyemlgtcr micdpytvsp aggpagakap ppgpstaale
       61 vmqdlsanpp ppfiqgpkgd pgrpgkpgpr gppgepgppg prgppgekgd sgrpglpglq
      121 lttsaaggvg vvgggtgggg dtegevtsal saafsgpkia fyvglksphe gyevlkfddv
      181 vtnlgnhydp ttgkfscqvr giyfftyhil mrggdgtsmw adlckngqvr asaiaqdadq
      241 nydyasnsvv lhldsgdevy vkldggkahg gnnnkystfs gfllypd
//
LOCUS       NP_001013431            1651 aa            linear   ROD 02-APR-2025
DEFINITION  alsin [Rattus norvegicus].
ACCESSION   NP_001013431 XP_001061827 XP_001064519 XP_001064573 XP_343575
VERSION     NP_001013431.1
DBSOURCE    REFSEQ: accession NM_001013413.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1651)
  AUTHORS   Masutani,T., Taguchi,K., Kumanogoh,H., Nakamura,S. and Maekawa,S.
  TITLE     Molecular interaction of neurocalcin alpha with alsin (ALS2)
  JOURNAL   Neurosci Lett 438 (1), 26-28 (2008)
   PUBMED   18482800
  REMARK    GeneRIF: These results suggest that alsin binds cell membrane in a
            Ca(2+)-dependent manner through NCalpha and regulates membrane
            dynamics.
REFERENCE   2  (residues 1 to 1651)
  AUTHORS   Suzuki-Utsunomiya,K., Hadano,S., Otomo,A., Kunita,R., Mizumura,H.,
            Osuga,H. and Ikeda,J.E.
  TITLE     ALS2CL, a novel ALS2-interactor, modulates ALS2-mediated endosome
            dynamics
  JOURNAL   Biochem Biophys Res Commun 354 (2), 491-497 (2007)
   PUBMED   17239822
REFERENCE   3  (residues 1 to 1651)
  AUTHORS   Lai,C., Xie,C., McCormack,S.G., Chiang,H.C., Michalak,M.K., Lin,X.,
            Chandran,J., Shim,H., Shimoji,M., Cookson,M.R., Huganir,R.L.,
            Rothstein,J.D., Price,D.L., Wong,P.C., Martin,L.J., Zhu,J.J. and
            Cai,H.
  TITLE     Amyotrophic lateral sclerosis 2-deficiency leads to neuronal
            degeneration in amyotrophic lateral sclerosis through altered AMPA
            receptor trafficking
  JOURNAL   J Neurosci 26 (45), 11798-11806 (2006)
   PUBMED   17093100
REFERENCE   4  (residues 1 to 1651)
  AUTHORS   Jacquier,A., Buhler,E., Schafer,M.K., Bohl,D., Blanchard,S.,
            Beclin,C. and Haase,G.
  TITLE     Alsin/Rac1 signaling controls survival and growth of spinal
            motoneurons
  JOURNAL   Ann Neurol 60 (1), 105-117 (2006)
   PUBMED   16802292
REFERENCE   5  (residues 1 to 1651)
  AUTHORS   Devon,R.S., Orban,P.C., Gerrow,K., Barbieri,M.A., Schwab,C.,
            Cao,L.P., Helm,J.R., Bissada,N., Cruz-Aguado,R., Davidson,T.L.,
            Witmer,J., Metzler,M., Lam,C.K., Tetzlaff,W., Simpson,E.M.,
            McCaffery,J.M., El-Husseini,A.E., Leavitt,B.R. and Hayden,M.R.
  TITLE     Als2-deficient mice exhibit disturbances in endosome trafficking
            associated with motor behavioral abnormalities
  JOURNAL   Proc Natl Acad Sci U S A 103 (25), 9595-9600 (2006)
   PUBMED   16769894
REFERENCE   6  (residues 1 to 1651)
  AUTHORS   Bros,V., Shemilt,S.J., Cooper,J.D., Skaper,S.D., Leigh,P.N. and
            Gallo,J.M.
  TITLE     A novel somatodendritic marker defined by a peptide derived from
            the ALS2 protein
  JOURNAL   Neuroreport 15 (14), 2155-2159 (2004)
   PUBMED   15371724
REFERENCE   7  (residues 1 to 1651)
  AUTHORS   Kunita,R., Otomo,A., Mizumura,H., Suzuki,K., Showguchi-Miyata,J.,
            Yanagisawa,Y., Hadano,S. and Ikeda,J.E.
  TITLE     Homo-oligomerization of ALS2 through its unique carboxyl-terminal
            regions is essential for the ALS2-associated Rab5 guanine
            nucleotide exchange activity and its regulatory function on
            endosome trafficking
  JOURNAL   J Biol Chem 279 (37), 38626-38635 (2004)
   PUBMED   15247254
REFERENCE   8  (residues 1 to 1651)
  AUTHORS   Topp,J.D., Gray,N.W., Gerard,R.D. and Horazdovsky,B.F.
  TITLE     Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor
  JOURNAL   J Biol Chem 279 (23), 24612-24623 (2004)
   PUBMED   15033976
  REMARK    GeneRIF: Als2 gene encodes a large protein termed alsin, which
            contains a number of predicted cell signaling and protein
            trafficking sequence motifs.
REFERENCE   9  (residues 1 to 1651)
  AUTHORS   Otomo,A., Hadano,S., Okada,T., Mizumura,H., Kunita,R.,
            Nishijima,H., Showguchi-Miyata,J., Yanagisawa,Y., Kohiki,E.,
            Suga,E., Yasuda,M., Osuga,H., Nishimoto,T., Narumiya,S. and
            Ikeda,J.E.
  TITLE     ALS2, a novel guanine nucleotide exchange factor for the small
            GTPase Rab5, is implicated in endosomal dynamics
  JOURNAL   Hum Mol Genet 12 (14), 1671-1687 (2003)
   PUBMED   12837691
REFERENCE   10 (residues 1 to 1651)
  AUTHORS   Yang,Y., Hentati,A., Deng,H.X., Dabbagh,O., Sasaki,T., Hirano,M.,
            Hung,W.Y., Ouahchi,K., Yan,J., Azim,A.C., Cole,N., Gascon,G.,
            Yagmour,A., Ben-Hamida,M., Pericak-Vance,M., Hentati,F. and
            Siddique,T.
  TITLE     The gene encoding alsin, a protein with three guanine-nucleotide
            exchange factor domains, is mutated in a form of recessive
            amyotrophic lateral sclerosis
  JOURNAL   Nat Genet 29 (2), 160-165 (2001)
   PUBMED   11586297
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK005190.1.
            
            On or before Feb 3, 2007 this sequence version replaced
            XP_343575.2, XP_001061827.1, XP_001064519.1, XP_001064573.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK005190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1651
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..1651
                     /product="alsin"
                     /note="amyotrophic lateral sclerosis protein 2 homolog;
                     ALS2, alsin Rho guanine nucleotide exchange factor;
                     amyotrophic lateral sclerosis 2 protein homolog;
                     amyotrophic lateral sclerosis 2 (juvenile)"
                     /calculated_mol_wt=182318
     Region          <18..219
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          59..108
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          109..167
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          169..218
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          444..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96Q42; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96Q42; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          519..570
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          522..>622
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Site            527
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96Q42; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          572..621
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          689..873
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cl02571"
                     /db_xref="CDD:470622"
     Site            order(691,695,796,828..829,832..833,835..836,839..840,
                     844..845,873)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          899..1004
                     /region_name="PH_alsin"
                     /note="Alsin Pleckstrin homology (PH) domain; cd13269"
                     /db_xref="CDD:241423"
     Region          <1012..1243
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          1043..1065
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1066..1088
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1094..1116
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1117..1139
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1145..1167
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1169..1191
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1192..1214
                     /region_name="MORN 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1215..1238
                     /region_name="MORN 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C5Y8.1)"
     Region          1546..1650
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1651
                     /gene="Als2"
                     /coded_by="NM_001013413.1:113..5068"
                     /db_xref="GeneID:363235"
                     /db_xref="RGD:1310372"
ORIGIN      
        1 mdskkkssae aegskerglv hvwqagsfsl tperlpgwgg ktvlqaalgv khgvlltedg
       61 evysfgtlpw kseaaeicps spllesalvg hhvvtvatgs fhsgavtesg vvymwgenaa
      121 gqcavanqqy vsepspvsis dsetspllav rilqlacgee htlalsisre iwawgtgcql
      181 glitttfpvt kpqkvehlag rvvlqvacga fhslalvqcl ppqdlkpvpe rcnqcsqlli
      241 tmtdkedhvi isdshccplg vtlsesqaek hastvtsphp etldgqgevf entvaeaeln
      301 mgsdqttsgs aisaqqnivg maevssarta psypdtqtvt aylqklsehs vkenhereek
      361 lpqvqplvee avpdlhsppt tstsalnslv vscasavgvr vaatyeagal slkkvmnfys
      421 tapcepgaps gtastgpesl kdlreeqvkq eslqgkksss lmdireeese ggsrrlslpg
      481 llsqvsprll rkaarvktrt vvltptysge adallpslrt evwtwgkgke gqlghgdvlp
      541 rlqplcvkcl dgkevihlea ggshslalta ksqvyswgsn tfgqlghsef pttvprlskv
      601 ssesgvwsva aghgyslflv dtedfqpgly ysgrqdraeg dtlpenpsgt ttpvllscsk
      661 lgyisrvtag kdsylalvdk nimgyiaslh elatterrfy sklseiksqi lrpllslehl
      721 gtvttvqllq evasrfsklc yligqhgasl ssylqgmkea rnlvimkhss lfldsyteyc
      781 tsvsnflvmg gsqllakpai dflnknqell qdlsevnden tqlmeilnal fflpirrlhn
      841 yakvllklat cfevtspeyq klqdssscye slalhlgkkr keaeytlsfw ktfpgkmtds
      901 lrkperrllc essnralslq hagrfsvnwf ilfndalvha qfsthhvfpl atlwaeplse
      961 etggvnglki ttpeeqftli sstpqektkw lraisqavdq alrgtsdfpl yggsstvqrq
     1021 eppisrsaky tfykdtrlkd atydgrwlsg kphgrgvlkw pdgkvysgtf rngledgyge
     1081 yripnkalnk edhyvghwke gkmcgqgvys yasgevfegc fqdnmrhghg llrsgkltss
     1141 spsmfigqwv mdkkagygvf dditrgekym gmwqddacqg ngvvvtqfgl yyegnfhlnk
     1201 mmgngvllse ddtiyegefs ddwtlcgkgt ltmpngdyie gyfsgewgsg ikitgtyfkp
     1261 slyesdkdrp kafrklgnla vaadekwrav fdecwrqlgc espgqgevwk awdniavalt
     1321 tnrrqhkdsp eilsrsqtqt lesleyipqh vgafsvekyd dikkylikac dtplhplgrl
     1381 vetlvavyrm tyvgvganrr llqeavkeik sylkrifqlv rflfpelpee gstvplsapl
     1441 ptgrrsfctg ksdsrsespe pgyvvtssgl llpvllprly pplfmlyald ndreediywe
     1501 cvlrlnkqpd iallgflgvq rkfwpatlsi lgeskkvlps tkdacfasav eclqqisttf
     1561 tpsdklkviq qtfeeisqsv laslqedflw smddlfpvfl yvvlrarirn lgsevhlied
     1621 lmdpylqhge qgimfttlka cyyqiqrekl n
//
LOCUS       NP_001100411             523 aa            linear   ROD 02-APR-2025
DEFINITION  melanoma-associated antigen E2 [Rattus norvegicus].
ACCESSION   NP_001100411 XP_001056951 XP_228532
VERSION     NP_001100411.1
DBSOURCE    REFSEQ: accession NM_001106941.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473969.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_228532.1, XP_001056951.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..523
                     /product="melanoma-associated antigen E2"
                     /note="melanoma antigen, family E, 2"
                     /calculated_mol_wt=59874
     Region          95..264
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     Region          349..478
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     CDS             1..523
                     /gene="Magee2"
                     /gene_synonym="RGD1564872"
                     /coded_by="NM_001106941.1:216..1787"
                     /db_xref="GeneID:302392"
                     /db_xref="RGD:1564872"
ORIGIN      
        1 msvvsqnarq graettadys dsqgemqatn asgppnsmlv peaaqgleip ddpqgasapq
       61 aaqdprdiev lideqsrrlg alrvhdplee rsvalvnflr mksqsegsir qsemleflne
      121 ysdqfpeilr rasayldrvf glnlrvldpq tdtynliskp gpqtterlae tldmpkagll
      181 alvlghilln gnrareasiw dlllkvevid etqrinnlfg ntrnllttdf vqmrfleywp
      241 vygtnplefe flwgsrahre itkmealkfi aeahdeepws wpeeynkale sdkakersqa
      301 aglefwsedt mndkandvvq laingteell pihqdellah tgkefedvfp nilsratlil
      361 dlfygfslie vdasdhiyll vpqpeseeeq vmleslgrpt heymmpilgl iflmgnrvke
      421 akiwnllrrf nvdvgrkhai tcklmrqryl ecrplsysnp veyellwgpr ahleitkmka
      481 leymarlyrk qpqdwpeqyr eavedeeara rseatamfff gsm
//
LOCUS       NP_001019856             331 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 38 [Rattus norvegicus].
ACCESSION   NP_001019856 XP_575442
VERSION     NP_001019856.1
DBSOURCE    REFSEQ: accession NM_001024685.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Wu,S.V., Chen,M.C. and Rozengurt,E.
  TITLE     Genomic organization, expression, and function of bitter taste
            receptors (T2R) in mouse and rat
  JOURNAL   Physiol Genomics 22 (2), 139-149 (2005)
   PUBMED   15886333
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bufe,B., Hofmann,T., Krautwurst,D., Raguse,J.D. and Meyerhof,W.
  TITLE     The human TAS2R16 receptor mediates bitter taste in response to
            beta-glucopyranosides
  JOURNAL   Nat Genet 32 (3), 397-401 (2002)
   PUBMED   12379855
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362746.1.
            
            On Jun 9, 2005 this sequence version replaced XP_575442.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY916512.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..331
                     /product="taste receptor type 2 member 38"
                     /note="T2R26; taste receptor type 2 member 26; taste
                     receptor, type 2, member 38"
                     /calculated_mol_wt=37128
     Region          16..308
                     /region_name="7tm_TAS2R38"
                     /note="mammalian taste receptor 2, subtype 38, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15025"
                     /db_xref="CDD:320153"
     Region          17..42
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320153"
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          54..78
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320153"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          93..115
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320153"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          142..158
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320153"
     Site            143..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          190..213
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320153"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          238..263
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320153"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     Region          275..300
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320153"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VHE7.1)"
     CDS             1..331
                     /gene="Tas2r138"
                     /gene_synonym="T2R38; Tas2r38"
                     /coded_by="NM_001024685.1:1..996"
                     /db_xref="GeneID:500091"
                     /db_xref="RGD:1560649"
ORIGIN      
        1 mltltpvltv syeakisflf lsvvefavgi manafivlvn fwdmvkkqpl nncdiallcl
       61 sitrlflqgl llldaiqlac fqqmkdplsh nyqailtlwm ianqvslwla aclsllycak
      121 ivrfshtfpl hlaswvsrrf lqmllvallf sgvctalclw dffsrshtvv tsmlhmnnte
      181 fnlqieklnf fysfvfcnvg svppslvfli ssgvlvislg nhmrtmksqt rgsrdpslea
      241 hvraiiflvs flcfyvvsfc aalisipllv lwhnkggvmv cigmmaacps ghaailisgn
      301 aklkkvivti lfwfqsrqkv rrvhkvlpri l
//
LOCUS       NP_036748                163 aa            linear   ROD 02-APR-2025
DEFINITION  olfactory marker protein [Rattus norvegicus].
ACCESSION   NP_036748
VERSION     NP_036748.1
DBSOURCE    REFSEQ: accession NM_012616.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Makeyeva,Y., Nicol,C., Ledger,W.L. and Ryugo,D.K.
  TITLE     Immunocytochemical Localization of Olfactory-signaling Molecules in
            Human and Rat Spermatozoa
  JOURNAL   J Histochem Cytochem 68 (7), 491-513 (2020)
   PUBMED   32603211
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Sadrian,B., Cheng,T.W., Shull,O. and Gong,Q.
  TITLE     Rap1gap2 regulates axon outgrowth in olfactory sensory neurons
  JOURNAL   Mol Cell Neurosci 50 (3-4), 272-282 (2012)
   PUBMED   22732430
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Choi,P.S., Zakhary,L., Choi,W.Y., Caron,S., Alvarez-Saavedra,E.,
            Miska,E.A., McManus,M., Harfe,B., Giraldez,A.J., Horvitz,H.R.,
            Schier,A.F. and Dulac,C.
  TITLE     Members of the miRNA-200 family regulate olfactory neurogenesis
  JOURNAL   Neuron 57 (1), 41-55 (2008)
   PUBMED   18184563
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Fleischer,J., Schwarzenbacher,K., Besser,S., Hass,N. and Breer,H.
  TITLE     Olfactory receptors and signalling elements in the Grueneberg
            ganglion
  JOURNAL   J Neurochem 98 (2), 543-554 (2006)
   PUBMED   16805845
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Yang,P., Baker,K.A. and Hagg,T.
  TITLE     A disintegrin and metalloprotease 21 (ADAM21) is associated with
            neurogenesis and axonal growth in developing and adult rodent CNS
  JOURNAL   J Comp Neurol 490 (2), 163-179 (2005)
   PUBMED   16052496
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Buiakova,O.I., Baker,H., Scott,J.W., Farbman,A., Kream,R.,
            Grillo,M., Franzen,L., Richman,M., Davis,L.M., Abbondanzo,S.,
            Stewart,C.L. and Margolis,F.L.
  TITLE     Olfactory marker protein (OMP) gene deletion causes altered
            physiological activity of olfactory sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 93 (18), 9858-9863 (1996)
   PUBMED   8790421
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Kudrycki,K., Stein-Izsak,C., Behn,C., Grillo,M., Akeson,R. and
            Margolis,F.L.
  TITLE     Olf-1-binding site: characterization of an olfactory
            neuron-specific promoter motif
  JOURNAL   Mol Cell Biol 13 (5), 3002-3014 (1993)
   PUBMED   8474458
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Danciger,E., Mettling,C., Vidal,M., Morris,R. and Margolis,F.
  TITLE     Olfactory marker protein gene: its structure and olfactory
            neuron-specific expression in transgenic mice
  JOURNAL   Proc Natl Acad Sci U S A 86 (21), 8565-8569 (1989)
   PUBMED   2701951
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Rogers,K.E., Dasgupta,P., Gubler,U., Grillo,M., Khew-Goodall,Y.S.
            and Margolis,F.L.
  TITLE     Molecular cloning and sequencing of a cDNA for olfactory marker
            protein
  JOURNAL   Proc Natl Acad Sci U S A 84 (6), 1704-1708 (1987)
   PUBMED   3470751
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Sydor,W., Teitelbaum,Z., Blacher,R., Sun,S., Benz,W. and
            Margolis,F.L.
  TITLE     Amino acid sequence of a unique neuronal protein: rat olfactory
            marker protein
  JOURNAL   Arch Biochem Biophys 249 (2), 351-362 (1986)
   PUBMED   3753006
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M26926.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..163
                     /product="olfactory marker protein"
                     /note="olfactory neuronal-specific protein"
                     /calculated_mol_wt=18721
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:3753006; propagated from
                     UniProtKB/Swiss-Prot (P08523.2)"
     Region          12..161
                     /region_name="Olfactory_mark"
                     /note="Olfactory marker protein; pfam06554"
                     /db_xref="CDD:399511"
     CDS             1..163
                     /gene="Omp"
                     /coded_by="NM_012616.1:60..551"
                     /db_xref="GeneID:24612"
                     /db_xref="RGD:3231"
ORIGIN      
        1 maedgpqkqq ldmplvldqd ltkqmrlrve slkqrgekkq dgekllrpae svyrldfiqq
       61 qklqfdhwnv vldkpgkvti tgtsqnwtpd ltnlmtrqll dpaaifwrke dsdamdwnea
      121 dalefgerls dlakirkvmy flitfgegve panlkasvvf nql
//
LOCUS       NP_001014786             192 aa            linear   ROD 02-APR-2025
DEFINITION  interferon alpha-1 precursor [Rattus norvegicus].
ACCESSION   NP_001014786 XP_216443
VERSION     NP_001014786.1
DBSOURCE    REFSEQ: accession NM_001014786.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Hu,G., Xue,J., Duan,H., Yang,Z., Gao,L., Luo,H., Mu,X. and Cui,S.
  TITLE     IFN-gamma induces IFN-alpha and IFN-beta expressions in cultured
            rat intestinal mucosa microvascular endothelial cells
  JOURNAL   Immunopharmacol Immunotoxicol 32 (4), 656-662 (2010)
   PUBMED   20214528
  REMARK    GeneRIF: IFN-gamma is able to activate rat intestinal mucous
            microvascular endothelial cells, thereby leading to upregulated
            expressions of IFN-alpha/beta.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   van der Meide,P.H., Dijkema,R., Caspers,M., Vijverberg,K. and
            Schellekens,H.
  TITLE     Cloning, expression, and purification of rat IFN-alpha 1
  JOURNAL   Methods Enzymol 119, 441-453 (1986)
   PUBMED   3020354
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Dijkema,R., Pouwels,P., de Reus,A. and Schellekens,H.
  TITLE     Structure and expression in Escherichia coli of a cloned rat
            interferon-alpha gene
  JOURNAL   Nucleic Acids Res 12 (2), 1227-1242 (1984)
   PUBMED   6320120
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X00336.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216443.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..192
                     /product="interferon alpha-1 precursor"
                     /note="interferon-alpha 1; interferon-alpha 1-like 1"
                     /calculated_mol_wt=19429
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2524
     mat_peptide     24..192
                     /product="interferon alpha-1"
                     /note="mature rat IFN"
                     /calculated_mol_wt=19429
     Region          26..185
                     /region_name="Interferon"
                     /note="Interferon alpha/beta domain; pfam00143"
                     /db_xref="CDD:459689"
     Site            order(28..29,32,35..36,39,42..43,100..101,103..104,
                     106..107,110,113..114,117..118,121)
                     /site_type="active"
                     /note="putative IFNAR-1 binding site [active]"
                     /db_xref="CDD:238047"
     Site            order(53..60,62..64,70..71,141..142,144..145,148..149,
                     151..152,155..160)
                     /site_type="active"
                     /note="putative IFNAR-2 binding site [active]"
                     /db_xref="CDD:238047"
     Site            101
                     /site_type="other"
                     /note="N-glycosylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238047"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:6320120; propagated from
                     UniProtKB/Swiss-Prot (P05011.1)"
     CDS             1..192
                     /gene="Ifna5"
                     /gene_synonym="IFN-alpha1; Ifna1; Ifna1l1"
                     /coded_by="NM_001014786.1:1..579"
                     /db_xref="GeneID:298210"
                     /db_xref="RGD:1359312"
ORIGIN      
        1 marlcaflms lvvvsywsac clgcdlphth nlrnkrvftl laqmrrlspv sclkdrkyfg
       61 fplekvdgqq iqkaqaipvl heltqqilsl ftskesstaw datlldsfcn dlqqqlsglq
      121 aclmqqvgvq espltqedsl lavreyfhri tvylrenkhs pcawevvkae vwralsssan
      181 lmgrlreern es
//
LOCUS       NP_596901                183 aa            linear   ROD 02-APR-2025
DEFINITION  ras-related protein Rap-2b [Rattus norvegicus].
ACCESSION   NP_596901
VERSION     NP_596901.1
DBSOURCE    REFSEQ: accession NM_133410.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Monteiro,A.C., Sumagin,R., Rankin,C.R., Leoni,G., Mina,M.J.,
            Reiter,D.M., Stehle,T., Dermody,T.S., Schaefer,S.A., Hall,R.A.,
            Nusrat,A. and Parkos,C.A.
  TITLE     JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c
            and regulate epithelial barrier function
  JOURNAL   Mol Biol Cell 24 (18), 2849-2860 (2013)
   PUBMED   23885123
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Hussain,N.K., Hsin,H., Huganir,R.L. and Sheng,M.
  TITLE     MINK and TNIK differentially act on Rap2-mediated signal
            transduction to regulate neuronal structure and AMPA receptor
            function
  JOURNAL   J Neurosci 30 (44), 14786-14794 (2010)
   PUBMED   21048137
  REMARK    GeneRIF: MINK interaction with Rap2 plays a critical role in
            maintaining the morphological integrity of dendrites and synaptic
            transmission.
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Uechi,Y., Bayarjargal,M., Umikawa,M., Oshiro,M., Takei,K.,
            Yamashiro,Y., Asato,T., Endo,S., Misaki,R., Taguchi,T. and
            Kariya,K.
  TITLE     Rap2 function requires palmitoylation and recycling endosome
            localization
  JOURNAL   Biochem Biophys Res Commun 378 (4), 732-737 (2009)
   PUBMED   19061864
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Canobbio,I., Trionfini,P., Guidetti,G.F., Balduini,C. and Torti,M.
  TITLE     Targeting of the small GTPase Rap2b, but not Rap1b, to lipid rafts
            is promoted by palmitoylation at Cys176 and Cys177 and is required
            for efficient protein activation in human platelets
  JOURNAL   Cell Signal 20 (9), 1662-1670 (2008)
   PUBMED   18582561
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Kukimoto-Niino,M., Takagi,T., Akasaka,R., Murayama,K.,
            Uchikubo-Kamo,T., Terada,T., Inoue,M., Watanabe,S., Tanaka,A.,
            Hayashizaki,Y., Kigawa,T., Shirouzu,M. and Yokoyama,S.
  TITLE     Crystal structure of the RUN domain of the RAP2-interacting protein
            x
  JOURNAL   J Biol Chem 281 (42), 31843-31853 (2006)
   PUBMED   16928684
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Greco,F., Ciana,A., Pietra,D., Balduini,C., Minetti,G. and Torti,M.
  TITLE     Rap2, but not Rap1 GTPase is expressed in human red blood cells and
            is involved in vesiculation
  JOURNAL   Biochim Biophys Acta 1763 (3), 330-335 (2006)
   PUBMED   16540189
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Paganini,S., Guidetti,G.F., Catricala,S., Trionfini,P., Panelli,S.,
            Balduini,C. and Torti,M.
  TITLE     Identification and biochemical characterization of Rap2C, a new
            member of the Rap family of small GTP-binding proteins
  JOURNAL   Biochimie 88 (3-4), 285-295 (2006)
   PUBMED   16213650
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF386786.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF386786.1, DV216028.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..183
                     /product="ras-related protein Rap-2b"
                     /EC_number="3.6.5.2"
                     /calculated_mol_wt=20373
     mat_peptide     1..180
                     /product="Ras-related protein Rap-2b. /id=PRO_0000030219"
                     /note="propagated from UniProtKB/Swiss-Prot (P61227.1)"
                     /calculated_mol_wt=20179
     Region          3..165
                     /region_name="Rap2"
                     /note="Rap2 family GTPase consists of Rap2a, Rap2b, and
                     Rap2c; cd04176"
                     /db_xref="CDD:133376"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133376"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133376"
     Site            order(13..18,28..31,116..117,119,146..147)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133376"
     Site            order(17..18,32,34,40..41,54..55,57,59..60,148)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133376"
     Site            order(25,31,33,36..41)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133376"
     Region          32..40
                     /region_name="Effector region. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P61227.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133376"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133376"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133376"
     Site            order(59..65,68..73,76..77)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133376"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133376"
     Site            146..148
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133376"
     Site            180
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61226; propagated from
                     UniProtKB/Swiss-Prot (P61227.1)"
     CDS             1..183
                     /gene="Rap2b"
                     /coded_by="NM_133410.1:1..552"
                     /db_xref="GeneID:170923"
                     /db_xref="RGD:620591"
ORIGIN      
        1 mreykvvvlg sggvgksalt vqfvtgsfie kydptiedfy rkeievdssp svleildtag
       61 teqfasmrdl yikngqgfil vyslvnqqsf qdikpmrdqi irvkryervp milvgnkvdl
      121 egerevsyge gkalaeewsc pfmetsaknk asvdelfaei vrqmnyaaqp ngdegccsac
      181 vil
//
LOCUS       NP_783176                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7b [Rattus norvegicus].
ACCESSION   NP_783176
VERSION     NP_783176.2
DBSOURCE    REFSEQ: accession NM_175586.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ferrero,D.M., Wacker,D., Roque,M.A., Baldwin,M.W., Stevens,R.C. and
            Liberles,S.D.
  TITLE     Agonists for 13 trace amine-associated receptors provide insight
            into the molecular basis of odor selectivity
  JOURNAL   ACS Chem Biol 7 (7), 1184-1189 (2012)
   PUBMED   22545963
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702319.1.
            
            On Nov 18, 2005 this sequence version replaced NP_783176.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7b"
                     /note="taR-12; taR-7b; trace amine receptor 7b; trace
                     amine receptor 12"
                     /calculated_mol_wt=40160
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923X8.2)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320439"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320439"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320439"
     Site            126..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320439"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320439"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923X8.2)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320439"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320439"
     Site            310..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X8.2)"
     CDS             1..358
                     /gene="Taar7b"
                     /gene_synonym="TA12"
                     /coded_by="NM_175586.2:1..1077"
                     /db_xref="GeneID:294126"
                     /db_xref="RGD:631392"
ORIGIN      
        1 matdddrfpw dqdsilsrdl lsassmqlcy eklnrscvrs pyspgprlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadflvgltv mpfsmvrsve gcwyfgdiyc
      121 kfhssfdgsf cyssifhlcf isadryiavs dpliyptrft asvsgkcitf swllsiiysf
      181 slfytgvnea gledlvsalt cvggcqiavn qswvfinfll flvpalvmmt vyskifliak
      241 qqaqniekmg kqtarasesy kdrvakrerk aaktlgiava afllswlpyf idsiidaflg
      301 fvtptyvyei lvwigyynsa mnpliyaffy pwfrkaikli vtgkilrens satnlfpe
//
LOCUS       NP_001074408             320 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 109 [Rattus norvegicus].
ACCESSION   NP_001074408 XP_001074843
VERSION     NP_001074408.1
DBSOURCE    REFSEQ: accession NM_001080939.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY486338.1.
            
            On Jan 31, 2007 this sequence version replaced XP_001074843.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..320
                     /product="taste receptor type 2 member 109"
                     /note="putative taste receptor T2R38; T2R109; taste
                     receptor type 2 member 38"
                     /calculated_mol_wt=37351
     Region          15..305
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          15..40
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          52..76
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          90..112
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          139..155
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          184..207
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          232..257
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B9.1)"
     CDS             1..320
                     /gene="Tas2r109"
                     /coded_by="NM_001080939.1:1..963"
                     /db_xref="GeneID:690572"
                     /db_xref="RGD:1594689"
ORIGIN      
        1 mehflksifd isknvlpiil fieliigiig ngfmalvhcm dwvkrkkmsl vnqilttlat
       61 sricllwfml lgllitlldp dlasarmmiq vasnlwiian hmsiwlatcl tvfyflkian
      121 fssslflylk wrvekvisvi flvslvllfl nmllmnlend mciaeyhqin isysfiyhyr
      181 adcerrvlrl hiiilsvpfv lslptfllli fslwthhkkm qqhvqgrrda sttahfkalq
      241 tviaflllyc ifilsmllqf wkyelmkkpl filfchivyg afpsfhsyvl ilgdmklrqa
      301 slsvllwlkc rpnyietldl
//
LOCUS       NP_001032941             133 aa            linear   ROD 02-APR-2025
DEFINITION  sperm-associated antigen 11B isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001032941
VERSION     NP_001032941.1
DBSOURCE    REFSEQ: accession NM_001037852.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Ribeiro,C.M., Queiroz,D.B., Patrao,M.T., Denadai-Souza,A.,
            Romano,R.M., Silva,E.J. and Avellar,M.C.
  TITLE     Dynamic changes in the spatio-temporal expression of the
            beta-defensin SPAG11C in the developing rat epididymis and its
            regulation by androgens
  JOURNAL   Mol Cell Endocrinol 404, 141-150 (2015)
   PUBMED   25657045
  REMARK    GeneRIF: Results from the spatio-temporal expression, cellular
            distribution showed that SPAG11C may play a role in epididymal
            development and/or sperm function.
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Yenugu,S., Hamil,K.G., French,F.S. and Hall,S.H.
  TITLE     Antimicrobial actions of human and macaque sperm associated antigen
            (SPAG) 11 isoforms: influence of the N-terminal peptide
  JOURNAL   Mol Cell Biochem 284 (1-2), 25-37 (2006)
   PUBMED   16411022
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Patil,A.A., Cai,Y., Sang,Y., Blecha,F. and Zhang,G.
  TITLE     Cross-species analysis of the mammalian beta-defensin gene family:
            presence of syntenic gene clusters and preferential expression in
            the male reproductive tract
  JOURNAL   Physiol Genomics 23 (1), 5-17 (2005)
   PUBMED   16033865
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ012093.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ012093.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..133
                     /product="sperm-associated antigen 11B isoform 1
                     precursor"
                     /note="sperm associated antigen 11C-like; sperm associated
                     antigen 11b-like"
                     /calculated_mol_wt=12225
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2508
     Region          <41..92
                     /region_name="Sperm_Ag_HE2"
                     /note="Sperm antigen HE2; pfam05324"
                     /db_xref="CDD:461622"
     CDS             1..133
                     /gene="Spag11b"
                     /gene_synonym="Spag11; Spag11bl; Spag11c"
                     /coded_by="NM_001037852.1:1..402"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:100362580"
                     /db_xref="RGD:1562239"
ORIGIN      
        1 mkrrllpsfv slllaalllp gkaetwlrsw tqalsagvtl gsssassinh lvteppsspq
       61 defpaqggng sgllhhrvkr fpprtppyhe pgpnyqivnc kknegfcqky cnfmetqvgy
      121 cskkkeaccl hpf
//
LOCUS       NP_001247413             101 aa            linear   ROD 02-APR-2025
DEFINITION  prostate and testis expressed 14 like 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001247413 XP_002727063 XP_002729934
VERSION     NP_001247413.1
DBSOURCE    REFSEQ: accession NM_001260484.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Rajesh,A. and Yenugu,S.
  TITLE     Genomic organization, tissue distribution and functional
            characterization of the rat Pate gene cluster
  JOURNAL   PLoS One 7 (3), e32633 (2012)
   PUBMED   22479333
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from JQ031758.1.
            
            On or before May 7, 2012 this sequence version replaced
            XP_002727063.1, XP_002729934.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ031758.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..101
                     /product="prostate and testis expressed 14 like 2
                     precursor"
                     /note="prostate and testis expressed protein P; Secreted
                     seminal-vesicle Ly-6 protein 1-like; rCG64165-like"
                     /calculated_mol_wt=8851
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2216
     Region          20..98
                     /region_name="TFP_LU_ECD_SP10_like"
                     /note="extracellular domain (ECD) found in acrosomal
                     protein SP-10, prostate and testis expressed protein 14
                     (Pate14) and similar proteins; cd23628"
                     /db_xref="CDD:467148"
     CDS             1..101
                     /gene="Pate14l2"
                     /coded_by="NM_001260484.1:1..306"
                     /db_xref="GeneID:100360049"
                     /db_xref="RGD:2322896"
ORIGIN      
        1 mgkdilllll glsllvssmq altcikcerf nsqgicerge gcceaqpgek caslitykdg
       61 kiqfgsqrca dlcyrgtven ggltikmncc shrsfcnkpy p
//
LOCUS       NP_001102817             309 aa            linear   ROD 02-APR-2025
DEFINITION  olfactory receptor family 2 subfamily A member 52 [Rattus
            norvegicus].
ACCESSION   NP_001102817 XP_001072921 XP_578256
VERSION     NP_001102817.1
DBSOURCE    REFSEQ: accession NM_001109347.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473959.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001072921.1, XP_578256.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..309
                     /product="olfactory receptor family 2 subfamily A member
                     52"
                     /note="olfactory receptor 437"
                     /calculated_mol_wt=34587
     Region          24..300
                     /region_name="7tmA_OR2A-like"
                     /note="olfactory receptor subfamily 2A and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15420"
                     /db_xref="CDD:320542"
     Region          25..51
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320542"
     Region          58..84
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320542"
     Site            order(80,83..84,96..101,103..104,107,152,154..158,194,
                     197..199,201..203,205..206,251,254..255,257..258,261,
                     267..268,270..272,275,278..279)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320542"
     Region          96..126
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320542"
     Region          139..160
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320542"
     Region          194..224
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320542"
     Region          231..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320542"
     Region          268..293
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320542"
     CDS             1..309
                     /gene="Or2a52"
                     /gene_synonym="Olr437"
                     /coded_by="NM_001109347.1:1..930"
                     /db_xref="GeneID:502758"
                     /db_xref="RGD:1587195"
ORIGIN      
        1 mganqtwvte filvglqlsa gmemflfwif sllyilslla ngiilalicl dprlhtpmyf
       61 flshlaildm syasnnvpkm lsnlvnqkkt isfvpcvtqt flylafaase clilaamsyd
      121 rfvaichplh ytvimswkvc valavtswsc gfilsvahti lllklpfcgp qevnhlfcei
      181 lavlklacad tlinqivila acvfvlvgpl csmlvsythi lwtilkmqsk egrkkafstc
      241 sshlcvvglf fgiamlvymv pdsdqreeqe kilslfhslf npmlnpliys lrnaqvkeaf
      301 hralqkrsv
//
LOCUS       NP_001026994             421 aa            linear   ROD 02-APR-2025
DEFINITION  bone morphogenetic protein 10 precursor [Rattus norvegicus].
ACCESSION   NP_001026994 XP_575595
VERSION     NP_001026994.1
DBSOURCE    REFSEQ: accession NM_001031824.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Hirono,K., Saito,K., Munkhsaikhan,U., Xu,F., Wang,C., Lu,L.,
            Ichida,F., Towbin,J.A. and Purevjav,E.
  TITLE     Familial Left Ventricular Non-Compaction Is Associated With a Rare
            p.V407I Variant in Bone Morphogenetic Protein 10
  JOURNAL   Circ J 83 (8), 1737-1746 (2019)
   PUBMED   31243186
  REMARK    GeneRIF: W143*-NRG1and V470I-BMP10 variants are associated with
            left ventricular non-compaction.
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Sun,L., Yu,J., Qi,S., Hao,Y., Liu,Y. and Li,Z.
  TITLE     Bone morphogenetic protein-10 induces cardiomyocyte proliferation
            and improves cardiac function after myocardial infarction
  JOURNAL   J Cell Biochem 115 (11), 1868-1876 (2014)
   PUBMED   24906204
  REMARK    GeneRIF: These data indicated that BMP10 stimulated cardiomyocyte
            proliferation and repaired cardiac function after heart injury.
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Yan,Y., Gong,P., Jin,W., Xu,J., Wu,X., Xu,T., Hang,Q., Fu,H.,
            Kei,K. and Gao,Y.
  TITLE     The cell-specific upregulation of bone morphogenetic protein-10
            (BMP-10) in a model of rat cortical brain injury
  JOURNAL   J Mol Histol 43 (5), 543-552 (2012)
   PUBMED   22797972
  REMARK    GeneRIF: the present data suggested that BMP-10 may be implicated
            in CNS pathophysiology after traumatic brain injury
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Somekawa,S., Imagawa,K., Hayashi,H., Sakabe,M., Ioka,T., Sato,G.E.,
            Inada,K., Iwamoto,T., Mori,T., Uemura,S., Nakagawa,O. and Saito,Y.
  TITLE     Tmem100, an ALK1 receptor signaling-dependent gene essential for
            arterial endothelium differentiation and vascular morphogenesis
  JOURNAL   Proc Natl Acad Sci U S A 109 (30), 12064-12069 (2012)
   PUBMED   22783020
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Seemann,P., Brehm,A., Konig,J., Reissner,C., Stricker,S., Kuss,P.,
            Haupt,J., Renninger,S., Nickel,J., Sebald,W., Groppe,J.C.,
            Ploger,F., Pohl,J., Schmidt-von Kegler,M., Walther,M., Gassner,I.,
            Rusu,C., Janecke,A.R., Dathe,K. and Mundlos,S.
  TITLE     Mutations in GDF5 reveal a key residue mediating BMP inhibition by
            NOGGIN
  JOURNAL   PLoS Genet 5 (11), e1000747 (2009)
   PUBMED   19956691
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Chen,H., Yong,W., Ren,S., Shen,W., He,Y., Cox,K.A., Zhu,W., Li,W.,
            Soonpaa,M., Payne,R.M., Franco,D., Field,L.J., Rosen,V., Wang,Y.
            and Shou,W.
  TITLE     Overexpression of bone morphogenetic protein 10 in myocardium
            disrupts cardiac postnatal hypertrophic growth
  JOURNAL   J Biol Chem 281 (37), 27481-27491 (2006)
   PUBMED   16798733
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Mazerbourg,S., Sangkuhl,K., Luo,C.W., Sudo,S., Klein,C. and
            Hsueh,A.J.
  TITLE     Identification of receptors and signaling pathways for orphan bone
            morphogenetic protein/growth differentiation factor ligands based
            on genomic analyses
  JOURNAL   J Biol Chem 280 (37), 32122-32132 (2005)
   PUBMED   16049014
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Tsuji,A.B., Sugyo,A., Ogiu,T., Sagara,M., Kimura,T., Ishikawa,A.,
            Sudo,H., Ohtsuki,M., Aburatani,H., Imai,T. and Harada,Y.N.
  TITLE     Fine mapping of radiation susceptibility and gene expression
            analysis of LEC congenic rat lines
  JOURNAL   Genomics 86 (3), 271-279 (2005)
   PUBMED   15978772
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Chen,H., Shi,S., Acosta,L., Li,W., Lu,J., Bao,S., Chen,Z., Yang,Z.,
            Schneider,M.D., Chien,K.R., Conway,S.J., Yoder,M.C., Haneline,L.S.,
            Franco,D. and Shou,W.
  TITLE     BMP10 is essential for maintaining cardiac growth during murine
            cardiogenesis
  JOURNAL   Development 131 (9), 2219-2231 (2004)
   PUBMED   15073151
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Neuhaus,H., Rosen,V. and Thies,R.S.
  TITLE     Heart specific expression of mouse BMP-10 a novel member of the
            TGF-beta superfamily
  JOURNAL   Mech Dev 80 (2), 181-184 (1999)
   PUBMED   10072785
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB158417.1.
            
            On Aug 19, 2005 this sequence version replaced XP_575595.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB158417.1, AB158418.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Rattus norvegicus"
                     /strain="F344/DuCrj"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..421
                     /product="bone morphogenetic protein 10 precursor"
                     /note="BMP-10"
                     /calculated_mol_wt=45681
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2105
     Region          55..256
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4AEG6.1)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4AEG6.1)"
     mat_peptide     314..421
                     /product="Bone morphogenetic protein 10.
                     /evidence=ECO:0000255. /id=PRO_0000310576"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4AEG6.1)"
                     /calculated_mol_wt=12118
     Region          318..421
                     /region_name="TGF_beta_BMP10"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in bone morphogenetic protein 10 (BMP-10) and
                     similar proteins; cd19401"
                     /db_xref="CDD:381671"
     Site            order(325,327,331..332,334,344,346..348,365..366,369..370,
                     372..373,376,380..382,385,387..388,391,411..413,415,421)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381671"
     CDS             1..421
                     /gene="Bmp10"
                     /coded_by="NM_001031824.1:1..1266"
                     /db_xref="GeneID:500245"
                     /db_xref="RGD:1562986"
ORIGIN      
        1 mgslvlplsa vfclvarlas gspimgleqs pleedmpffd difteqdgid fntllqsmkd
       61 eflktlnlsd ippqdtgrvd ppeymlelyn kfatdrtsmp saniirsfkn edlfsqpvsf
      121 ngirkypllf nvsiphheev vmaelrlytl vqrdrlmydg vdrkiiifev lesadgsede
      181 rsmlvlvste iygtnsewet fditdatrrw qksgpsthql eihiesrqnq aedtgrgqle
      241 idmsaqnkhd pllvvfsddq sgdkeqkeel nelisheqdl dlgtdgffgg pdeeallqmr
      301 snmiddstar irrnakgnyc kktplyidfk eigwdswiia ppgyeayecr gvcnyplaeh
      361 ltptkhaiiq alvhlknsqk askaccvptk ldpisilyld kgvvtykfky egmavsecgc
      421 r
//
LOCUS       NP_001102897             365 aa            linear   ROD 02-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 65 [Rattus norvegicus].
ACCESSION   NP_001102897 XP_001058618
VERSION     NP_001102897.1
DBSOURCE    REFSEQ: accession NM_001109427.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Boiko,T., Vakulenko,M., Ewers,H., Yap,C.C., Norden,C. and
            Winckler,B.
  TITLE     Ankyrin-dependent and -independent mechanisms orchestrate axonal
            compartmentalization of L1 family members neurofascin and
            L1/neuron-glia cell adhesion molecule
  JOURNAL   J Neurosci 27 (3), 590-603 (2007)
   PUBMED   17234591
  REMARK    GeneRIF: Ankyrin B is expressed along the entire lengths of axons.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001058618.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132292, SAMD00132297
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..365
                     /product="ankyrin repeat domain-containing protein 65"
                     /calculated_mol_wt=38484
     Region          33..63
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(34,38..39,42..44,46..47,51,54,63,65,67,71..72,
                     75..77,79..80,84,87,96,98,100,104..105,108..110,112..113,
                     117,120)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          37..124
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          65..96
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          98..123
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          114..364
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          197..224
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          227..257
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(259,261,265..266,269..271,273..274,278,281,290,292,
                     294,298..299,302..304,306..307,311,314,323,325,327,
                     331..332,335..337,339..340,344,347)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          259..290
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          292..323
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          325..355
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..365
                     /gene="Ankrd65"
                     /gene_synonym="RGD1562345"
                     /coded_by="NM_001109427.1:172..1269"
                     /db_xref="GeneID:680734"
                     /db_xref="RGD:1588232"
ORIGIN      
        1 mdssrlkqel qwmklvweet padktdrplt pqgwstlfqa vwwgapslvm qllrqgasve
       61 erdhtgrtpl hlavmrghap lvrlllqrga lagavdhtgr tplheaawhg hsnvaelllr
      121 rgasaaapcs qtgltplhga aalgrtllvt cftaapdsvp dvkdirgwta thwaaacgql
      181 pvlelltagg svdldgallv savagsasal rllltlgakv daldstgata lglaaglghh
      241 qeievllghg adpnirdrnn rsalhraasg gclraiqllv akgtdvdard slgltplhya
      301 argghrevvs hlldrgahvd aagwlhktpl hlavecghtt ilelllsrga npslrtqwge
      361 vaqip
//
LOCUS       NP_783189                374 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 8a [Rattus norvegicus].
ACCESSION   NP_783189
VERSION     NP_783189.1
DBSOURCE    REFSEQ: accession NM_175599.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Chiellini,G., Erba,P., Carnicelli,V., Manfredi,C., Frascarelli,S.,
            Ghelardoni,S., Mariani,G. and Zucchi,R.
  TITLE     Distribution of exogenous [125I]-3-iodothyronamine in mouse in
            vivo: relationship with trace amine-associated receptors
  JOURNAL   J Endocrinol 213 (3), 223-230 (2012)
   PUBMED   22442117
  REMARK    GeneRIF: Data show that TAARs were expressed only at trace amounts
            in most of the tissues, the exceptions being TAAR1 in stomach and
            testis and TAAR8a in intestine, spleen, and testis.
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380199.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..374
                     /product="trace amine-associated receptor 8a"
                     /note="taR-11; taR-8a; trace amine receptor 8a; trace
                     amine receptor 11; trace amine receptor 5"
                     /calculated_mol_wt=41364
     Region          62..353
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          64..88
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          97..119
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          135..157
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          180..196
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          224..247
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          288..310
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          321..346
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..374
                     /gene="Taar8a"
                     /gene_synonym="Ta11; Trar5"
                     /coded_by="NM_175599.1:1..1125"
                     /db_xref="GeneID:319104"
                     /db_xref="RGD:631391"
ORIGIN      
        1 mecisfifvs hncrcllagq kslkhqkgri mtsnfsqapl qlcyenvnas ciktpyspgl
       61 rvllymvfgf gavlavcgnl lvvisvlhfk qlhspanfli aslasadflv gisvmpfsmv
      121 rsiescwyfg dtfcslhscc daafcysslf hlcfisvdry iavtdplvyp tkftvsvsgi
      181 cisiswilpl vyssavfytg isatgienlv salncvggcq ivvnqdwvli dfllfliptl
      241 vmiilyskif lvakqqavki etsisgskge ssleshkarv akrerkaakt lgvtvvafmv
      301 swlpytidtl idafmgfitp ayvyeiccws ayynsamnpl iyaffypwfr kaiklilsge
      361 ilkshsstms lfse
//
LOCUS       NP_001011701             194 aa            linear   ROD 02-APR-2025
DEFINITION  Spetex-2D protein [Rattus norvegicus].
ACCESSION   NP_001011701 XP_344304
VERSION     NP_001011701.1
DBSOURCE    REFSEQ: accession NM_001011701.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Iwamoto,Y., Kaneko,T., Ichinose,J., Mori,T., Shibata,Y.,
            Toshimori,K. and Iida,H.
  TITLE     Molecular cloning of rat Spetex2 family genes mapped on chromosome
            15p16, encoding a 23-kilodalton protein associated with the plasma
            membranes of haploid spermatids
  JOURNAL   Biol Reprod 72 (2), 284-292 (2005)
   PUBMED   15371276
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB180079.1.
            
            On Feb 9, 2005 this sequence version replaced XP_344304.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB180079.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..194
                     /product="Spetex-2D protein"
                     /calculated_mol_wt=23087
     Region          34..114
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..194
                     /gene="Spetex2d"
                     /gene_synonym="Spetex-2D"
                     /coded_by="NM_001011701.1:1..585"
                     /db_xref="GeneID:364260"
                     /db_xref="RGD:1359263"
ORIGIN      
        1 mfhqllklvq kergdqgetr prqkkaglls wfirkassen fisnhekrik kleevkseiq
       61 kckierdels qildlyvndg lnyrlsvelp mlksqhemrm mdmhkmtnwi sdamekykel
      121 mqennsyrir nfhllnerne lkknvrilmn enrkllveqt elqasceegk rfceeaskti
      181 ytadieslcp vtfe
//
LOCUS       NP_695216                300 aa            linear   ROD 02-APR-2025
DEFINITION  free fatty acid receptor 1 [Rattus norvegicus].
ACCESSION   NP_695216
VERSION     NP_695216.1
DBSOURCE    REFSEQ: accession NM_153304.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Li,S.N., Yu,Y.L., Wang,B.Y., Qiao,S.Y., Hu,M.M., Wang,H., Fu,C.N.
            and Dong,B.
  TITLE     Overexpression of G Protein-Coupled Receptor 40 Protects
            Obesity-Induced Cardiomyopathy Through the SIRT1/LKB1/AMPK Pathway
  JOURNAL   Hum Gene Ther 33 (11-12), 598-613 (2022)
   PUBMED   35018806
  REMARK    GeneRIF: Overexpression of G Protein-Coupled Receptor 40 Protects
            Obesity-Induced Cardiomyopathy Through the SIRT1/LKB1/AMPK Pathway.
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Xiao,J., Cai,T., Fang,Y., Liu,R., Flores,J.J., Wang,W., Gao,L.,
            Liu,Y., Lu,Q., Tang,L., Zhang,J.H., Lu,H. and Tang,J.
  TITLE     Activation of GPR40 attenuates neuroinflammation and improves
            neurological function via PAK4/CREB/KDM6B pathway in an
            experimental GMH rat model
  JOURNAL   J Neuroinflammation 18 (1), 160 (2021)
   PUBMED   34275493
  REMARK    GeneRIF: Activation of GPR40 attenuates neuroinflammation and
            improves neurological function via PAK4/CREB/KDM6B pathway in an
            experimental GMH rat model.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Cho,Y.J., Choi,S.H., Lee,R., Hwang,H., Rhim,H., Cho,I.H., Kim,H.C.,
            Lee,J.I., Hwang,S.H. and Nah,S.Y.
  TITLE     Ginseng Gintonin Contains Ligands for GPR40 and GPR55
  JOURNAL   Molecules 25 (5), 1102 (2020)
   PUBMED   32121640
  REMARK    GeneRIF: Ginseng Gintonin Contains Ligands for GPR40 and GPR55.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Kim,C.S., Joo,S.Y., Kim,I.J., Choi,H.I., Bae,E.H., Kim,S.W. and
            Ma,S.K.
  TITLE     Anti-Apoptotic Effect of G-Protein-Coupled Receptor 40 Activation
            on Tumor Necrosis Factor-alpha-Induced Injury of Rat Proximal
            Tubular Cells
  JOURNAL   Int J Mol Sci 20 (14), 3386 (2019)
   PUBMED   31295865
  REMARK    GeneRIF: our results demonstrate that GPR40 activation rescued cell
            death and activated the pro-apoptotic signaling pathway in
            TNF-alpha-induced injury of NRK52E cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Feng,X.T., Duan,H.M. and Li,S.L.
  TITLE     Protective role of Pollen Typhae total flavone against the palmitic
            acid-induced impairment of glucose-stimulated insulin secretion
            involving GPR40 signaling in INS-1 cells
  JOURNAL   Int J Mol Med 40 (3), 922-930 (2017)
   PUBMED   28731171
  REMARK    GeneRIF: The results indicate that Pollen Typhae total flavone
            exerts a protective role against PA-induced impairment of GSIS
            involving GPR40 signaling in INS-1 cells.
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Stoddart,L.A., Brown,A.J. and Milligan,G.
  TITLE     Uncovering the pharmacology of the G protein-coupled receptor
            GPR40: high apparent constitutive activity in guanosine
            5'-O-(3-[35S]thio)triphosphate binding studies reflects binding of
            an endogenous agonist
  JOURNAL   Mol Pharmacol 71 (4), 994-1005 (2007)
   PUBMED   17200419
  REMARK    GeneRIF: GPR40 responded to fatty acids with different on-rates,
            and could be occupied by endogenous agonists before assay, masking
            the pharmacology of the receptor
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Fujiwara,K., Maekawa,F. and Yada,T.
  TITLE     Oleic acid interacts with GPR40 to induce Ca2+ signaling in rat
            islet beta-cells: mediation by PLC and L-type Ca2+ channel and link
            to insulin release
  JOURNAL   Am J Physiol Endocrinol Metab 289 (4), E670-E677 (2005)
   PUBMED   15914509
  REMARK    GeneRIF: These results demonstrate that OA interacts with GPR40 to
            increase [Ca(2+)](i) via PLC- and L-type Ca(2+) channel-mediated
            pathway in rat islet beta-cells, which may be link to insulin
            release.
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Shapiro,H., Shachar,S., Sekler,I., Hershfinkel,M. and Walker,M.D.
  TITLE     Role of GPR40 in fatty acid action on the beta cell line INS-1E
  JOURNAL   Biochem Biophys Res Commun 335 (1), 97-104 (2005)
   PUBMED   16081037
  REMARK    GeneRIF: GPR40 promotes Ca2+ influx through up-regulation of L-type
            calcium channels pre-activated by glucose and membrane
            depolarization
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Briscoe,C.P., Tadayyon,M., Andrews,J.L., Benson,W.G.,
            Chambers,J.K., Eilert,M.M., Ellis,C., Elshourbagy,N.A., Goetz,A.S.,
            Minnick,D.T., Murdock,P.R., Sauls,H.R. Jr., Shabon,U.,
            Spinage,L.D., Strum,J.C., Szekeres,P.G., Tan,K.B., Way,J.M.,
            Ignar,D.M., Wilson,S. and Muir,A.I.
  TITLE     The orphan G protein-coupled receptor GPR40 is activated by medium
            and long chain fatty acids
  JOURNAL   J Biol Chem 278 (13), 11303-11311 (2003)
   PUBMED   12496284
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Itoh,Y., Kawamata,Y., Harada,M., Kobayashi,M., Fujii,R.,
            Fukusumi,S., Ogi,K., Hosoya,M., Tanaka,Y., Uejima,H., Tanaka,H.,
            Maruyama,M., Satoh,R., Okubo,S., Kizawa,H., Komatsu,H.,
            Matsumura,F., Noguchi,Y., Shinohara,T., Hinuma,S., Fujisawa,Y. and
            Fujino,M.
  TITLE     Free fatty acids regulate insulin secretion from pancreatic beta
            cells through GPR40
  JOURNAL   Nature 422 (6928), 173-176 (2003)
   PUBMED   12629551
  REMARK    GeneRIF: Free fatty acids regulate insulin secretion from
            pancreatic beta cells through GPR40
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF539810.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF539810.1, AB095744.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..300
                     /product="free fatty acid receptor 1"
                     /note="G-protein coupled receptor 40"
                     /calculated_mol_wt=31705
     Region          6..289
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          8..32
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            9..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Site            42..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Region          42..63
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          80..102
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            80..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Region          125..141
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            145
                     /site_type="other"
                     /note="Important for receptor activation.
                     /evidence=ECO:0000250|UniProtKB:O14842; propagated from
                     UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Site            172
                     /site_type="other"
                     /note="Important for receptor activation.
                     /evidence=ECO:0000250|UniProtKB:O14842; propagated from
                     UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Site            179..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Region          180..203
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          223..245
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            224..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     Region          255..280
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            257..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3T4.1)"
     CDS             1..300
                     /gene="Ffar1"
                     /gene_synonym="Gpr40"
                     /coded_by="NM_153304.2:3..905"
                     /db_xref="GeneID:266607"
                     /db_xref="RGD:628613"
ORIGIN      
        1 mdlppqlsfa lyvsafalgf plnllairga vshaklrltp slvytlhlac sdlllaitlp
       61 lkavealasg vwplplpfcp vfalahfapl yagggflaal sagrylgaaf pfgyqairrp
      121 cyswgvcvai walvlchlgl algleaprgw vdnttsslgi nipvngspvc leawdpdsar
      181 parlsfsill fflplvitaf cyvgclralv hsglshkrkl raawvaggal ltlllclgpy
      241 nasnvasfin pdlegswrkl glitgawsvv lnplvtgylg tgpgqgticv trtprgtiqk
//
LOCUS       NP_783181                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7d [Rattus norvegicus].
ACCESSION   NP_783181
VERSION     NP_783181.2
DBSOURCE    REFSEQ: accession NM_175591.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Guo,L., Cheng,J., Lian,S., Liu,Q., Lu,Y., Zheng,Y., Zhu,K.,
            Zhang,M., Kong,Y., Zhang,C., Rong,N., Zhuang,Y., Fang,G., Jiang,J.,
            Zhang,T., Han,X., Liu,Z., Xia,M., Liu,S., Zhang,L., Liberles,S.D.,
            Yu,X., Xu,Y., Yang,F., Li,Q. and Sun,J.P.
  TITLE     Structural basis of amine odorant perception by a mammal olfactory
            receptor
  JOURNAL   Nature 618 (7963), 193-200 (2023)
   PUBMED   37225986
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Ferrero,D.M., Wacker,D., Roque,M.A., Baldwin,M.W., Stevens,R.C. and
            Liberles,S.D.
  TITLE     Agonists for 13 trace amine-associated receptors provide insight
            into the molecular basis of odor selectivity
  JOURNAL   ACS Chem Biol 7 (7), 1184-1189 (2012)
   PUBMED   22545963
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Lewin,A.H.
  TITLE     Receptors of mammalian trace amines
  JOURNAL   AAPS J 8 (1), E138-E145 (2006)
   PUBMED   16584120
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702321.1.
            
            On Nov 18, 2005 this sequence version replaced NP_783181.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7d"
                     /note="taR-15; taR-7d; trace amine receptor 7d;
                     trace-amine-associated receptor 7c; trace amine receptor
                     15"
                     /calculated_mol_wt=40454
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923X5.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          49..336
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X5.1)"
     CDS             1..358
                     /gene="Taar7d"
                     /gene_synonym="TA15; Taar7c"
                     /coded_by="NM_175591.2:1..1077"
                     /db_xref="GeneID:294134"
                     /db_xref="RGD:631395"
ORIGIN      
        1 mrvdddrfpw dqdsilsrdl lsasslqlcy enlnrscvrs pyspgprlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadllvgltv mpfsmvrsve gcwyfgdtyc
      121 klhtsfdvsf cycslfhlcf isvdryiavs dpliyptrft asvsgkcitf swllsiiygf
      181 pliytgasea gledlvsalt cvggcqipmn qkfvlinfll flvptlvmmt vyskifliar
      241 qqaqniekmr kqtarasesy kdrvckrerk aaktlgiava afllswlpyf idsiidaflg
      301 fitptyvyei liwivyynss mnpliyaffy pwfrkatkli vtgkilrens stinlfpe
//
LOCUS       NP_075587                377 aa            linear   ROD 02-APR-2025
DEFINITION  probable G-protein coupled receptor 27 [Rattus norvegicus].
ACCESSION   NP_075587
VERSION     NP_075587.1
DBSOURCE    REFSEQ: accession NM_023099.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Dolanc,D., Zorec,T.M., Smole,Z., Maver,A., Horvat,A., Pillaiyar,T.,
            Trkov Bobnar,S., Vardjan,N., Kreft,M., Chowdhury,H.H. and Zorec,R.
  TITLE     The Activation of GPR27 Increases Cytosolic L-Lactate in 3T3
            Embryonic Cells and Astrocytes
  JOURNAL   Cells 11 (6), 1009 (2022)
   PUBMED   35326460
  REMARK    GeneRIF: The Activation of GPR27 Increases Cytosolic L-Lactate in
            3T3 Embryonic Cells and Astrocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Ku,G.M., Pappalardo,Z., Luo,C.C., German,M.S. and McManus,M.T.
  TITLE     An siRNA screen in pancreatic beta cells reveals a role for Gpr27
            in insulin production
  JOURNAL   PLoS Genet 8 (1), e1002449 (2012)
   PUBMED   22253604
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Matsumoto,M., Saito,T., Takasaki,J., Kamohara,M., Sugimoto,T.,
            Kobayashi,M., Tadokoro,M., Matsumoto,S., Ohishi,T. and Furuichi,K.
  TITLE     An evolutionarily conserved G-protein coupled receptor family,
            SREB, expressed in the central nervous system
  JOURNAL   Biochem Biophys Res Commun 272 (2), 576-582 (2000)
   PUBMED   10833454
REFERENCE   4  (residues 1 to 377)
  AUTHORS   O'Dowd,B.F., Nguyen,T., Marchese,A., Cheng,R., Lynch,K.R.,
            Heng,H.H., Kolakowski,L.F. Jr. and George,S.R.
  TITLE     Discovery of three novel G-protein-coupled receptor genes
  JOURNAL   Genomics 47 (2), 310-313 (1998)
   PUBMED   9479505
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Shen,P. and Howlett,G.J.
  TITLE     Two coding regions closely linked to the rat apolipoprotein E gene:
            nucleotide sequences of rat apolipoprotein C-I and ECL cDNA
  JOURNAL   Arch Biochem Biophys 297 (2), 345-353 (1992)
   PUBMED   1379790
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB040802.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AB040802.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..377
                     /product="probable G-protein coupled receptor 27"
                     /note="super conserved receptor expressed in brain 1"
                     /calculated_mol_wt=39761
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          20..351
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          22..46
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            25..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          55..77
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          97..119
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          143..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          183..206
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          285..307
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     Region          319..344
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJH3.1)"
     CDS             1..377
                     /gene="Gpr27"
                     /gene_synonym="Sreb1"
                     /coded_by="NM_023099.1:1..1134"
                     /db_xref="GeneID:65275"
                     /db_xref="RGD:71067"
ORIGIN      
        1 manasepggg gggaeaaalg lrlatlslll cvslagnvlf allivrersl hrapyyllld
       61 lcladglral aclpavmlaa rraaaaagtp pgalgcklla flaalfcfha aflllgvgvt
      121 rylaiahhrf yaerlagwpc aamlvcaawa lalaaafppv ldgggadded apcaleqrpd
      181 gapgalgfll llaavvgath lvylrllffi hdrrkmrpar lvpavshdwt fhgpgatgqa
      241 aanwtagfgr gptppalvgi rpagpgrgar rllvleefkt ekrlckmfya itllflllwg
      301 pyvvasylrv lvrpgavpqa yltasvwltf aqaginpvvc flfnrelrdc fraqfpccqs
      361 pqatqatlpc dlkgigl
//
LOCUS       NP_620272                284 aa            linear   ROD 02-APR-2025
DEFINITION  F-box only protein 6 [Rattus norvegicus].
ACCESSION   NP_620272
VERSION     NP_620272.3
DBSOURCE    REFSEQ: accession NM_138917.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Groisman,B., Shenkman,M., Ron,E. and Lederkremer,G.Z.
  TITLE     Mannose trimming is required for delivery of a glycoprotein from
            EDEM1 to XTP3-B and to late endoplasmic reticulum-associated
            degradation steps
  JOURNAL   J Biol Chem 286 (2), 1292-1300 (2011)
   PUBMED   21062743
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Zhang,Y.W., Brognard,J., Coughlin,C., You,Z., Dolled-Filhart,M.,
            Aslanian,A., Manning,G., Abraham,R.T. and Hunter,T.
  TITLE     The F box protein Fbx6 regulates Chk1 stability and cellular
            sensitivity to replication stress
  JOURNAL   Mol Cell 35 (4), 442-453 (2009)
   PUBMED   19716789
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Yoshida,Y., Adachi,E., Fukiya,K., Iwai,K. and Tanaka,K.
  TITLE     Glycoprotein-specific ubiquitin ligases recognize N-glycans in
            unfolded substrates
  JOURNAL   EMBO Rep 6 (3), 239-244 (2005)
   PUBMED   15723043
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Yoshida,Y., Tokunaga,F., Chiba,T., Iwai,K., Tanaka,K. and Tai,T.
  TITLE     Fbs2 is a new member of the E3 ubiquitin ligase family that
            recognizes sugar chains
  JOURNAL   J Biol Chem 278 (44), 43877-43884 (2003)
   PUBMED   12939278
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Ilyin,G.P., Serandour,A.L., Pigeon,C., Rialland,M., Glaise,D. and
            Guguen-Guillouzo,C.
  TITLE     A new subfamily of structurally related human F-box proteins
  JOURNAL   Gene 296 (1-2), 11-20 (2002)
   PUBMED   12383498
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF393484.1.
            
            On Jun 10, 2007 this sequence version replaced NP_620272.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF393484.1, BC063148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..284
                     /product="F-box only protein 6"
                     /note="F-box/G-domain protein 2; F-box protein that
                     recognizes sugar chains 2; F-box only protein 6b; F-box
                     only protein 6 b"
                     /calculated_mol_wt=32655
     Region          1..83
                     /region_name="F-box_FBXO6-like"
                     /note="F-box domain found in F-box only proteins FBXO6,
                     FBXO44 and similar proteins; cd22168"
                     /db_xref="CDD:438939"
     Site            order(1,3..5,7..8,11,15,18,20,22..23,25,28..33,35..36,68)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438939"
     Region          70..248
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRD1; propagated from
                     UniProtKB/Swiss-Prot (Q923V4.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZN4; propagated from
                     UniProtKB/Swiss-Prot (Q923V4.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q923V4.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q923V4.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q923V4.1)"
     CDS             1..284
                     /gene="Fbxo6"
                     /gene_synonym="Fbg2; Fbxo6b"
                     /coded_by="NM_138917.3:22..876"
                     /db_xref="GeneID:192351"
                     /db_xref="RGD:620418"
ORIGIN      
        1 mvninelpen illelfthvp apqllrncrl vcslwrdlid vmtlwkrksl regfvtkdrd
       61 epvddwkify ilcslqrnll rnpcaeenlr swridsnggd ewkveslpgd hgtsfpdtkv
      121 kkyfvtsygm clksqmvdlk aegyseklld tvrpdivvkd wfapradcgc tyhlrvqlas
      181 adyivlasfe pppvtieqwn daswqeisht fsnyppgvrh ilfqhggkdt qfwkgwygpr
      241 vtnssiivsh rtaknpapar tlpeedtsnr rkilsfgswe dlsp
//
LOCUS       NP_570829                225 aa            linear   ROD 02-APR-2025
DEFINITION  fibroblast growth factor 11 [Rattus norvegicus].
ACCESSION   NP_570829
VERSION     NP_570829.1
DBSOURCE    REFSEQ: accession NM_130816.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Olsen,S.K., Garbi,M., Zampieri,N., Eliseenkova,A.V., Ornitz,D.M.,
            Goldfarb,M. and Mohammadi,M.
  TITLE     Fibroblast growth factor (FGF) homologous factors share structural
            but not functional homology with FGFs
  JOURNAL   J Biol Chem 278 (36), 34226-34236 (2003)
   PUBMED   12815063
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB079263.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB079263.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..225
                     /product="fibroblast growth factor 11"
                     /note="fibroblast growth factor 1d"
                     /calculated_mol_wt=25015
     Region          70..199
                     /region_name="beta-trefoil_FGF11-like"
                     /note="FGF domain, beta-trefoil fold, found in the
                     fibroblast growth factor 11 (FGF11)-like family; cd23309"
                     /db_xref="CDD:466995"
     CDS             1..225
                     /gene="Fgf11"
                     /gene_synonym="Fgf1d"
                     /coded_by="NM_130816.1:1..678"
                     /db_xref="GeneID:170632"
                     /db_xref="RGD:620162"
ORIGIN      
        1 maalasslir qkrevrepgg srpvsaqrrv cprgtkslcq kqllillskv rlcggrptrq
       61 drgpepqlkg ivtklfcrqg fylqanpdgs iqgtpedtss fthfnlipvg lrvvtiqsak
      121 lghymamnae gllyssphft aecrfkecvf enyyvlyasa lyrqrrsgra wylgldkegr
      181 vmkgnrvkkt kaaahfvpkl levavyreps lhsvpetsps sppah
//
LOCUS       NP_783173                347 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 4 [Rattus norvegicus].
ACCESSION   NP_783173
VERSION     NP_783173.1
DBSOURCE    REFSEQ: accession NM_175583.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Staubert,C., Bohnekamp,J. and Schoneberg,T.
  TITLE     Determinants involved in subtype-specific functions of rat trace
            amine-associated receptors 1 and 4
  JOURNAL   Br J Pharmacol 168 (5), 1266-1278 (2013)
   PUBMED   23072560
  REMARK    GeneRIF: The different functionality of rat Taar subtypes 1 and 4
            mainly correlates with receptor's cell surface expression rather
            than with specific amino acid residues involved in ligand binding
            specificity.
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Staubert,C., Boselt,I., Bohnekamp,J., Rompler,H., Enard,W. and
            Schoneberg,T.
  TITLE     Structural and functional evolution of the trace amine-associated
            receptors TAAR3, TAAR4 and TAAR5 in primates
  JOURNAL   PLoS One 5 (6), e11133 (2010)
   PUBMED   20559446
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380188.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..347
                     /product="trace amine-associated receptor 4"
                     /note="trace amine receptor 4; trace amine receptor 2;
                     2-phenylethylamine receptor"
                     /calculated_mol_wt=38652
     Site            20
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          34..324
                     /region_name="7tmA_TAAR2_3_4"
                     /note="trace amine-associated receptors 2, 3, 4, and
                     similar receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15312"
                     /db_xref="CDD:320437"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320437"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          68..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320437"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320437"
     Site            order(109,113..114,117..118,193,200,203..204,207,273,
                     276..277,280,295,299,303)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320437"
     Site            111..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          148..171
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320437"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          175..188
                     /region_name="Extracellular Loop 2 (ECL2).
                     /evidence=ECO:0000250|UniProtKB:Q5QD04"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          196..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320437"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          253..283
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320437"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     Region          292..317
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320437"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y7.1)"
     CDS             1..347
                     /gene="Taar4"
                     /gene_synonym="Ta2; taR-2; taR-4"
                     /coded_by="NM_175583.1:1..1044"
                     /db_xref="GeneID:294122"
                     /db_xref="RGD:631382"
ORIGIN      
        1 mnspdlwysp etqfcfaaan nscprkarpa lvvcamylvm igaivmtmlg nmvviisiah
       61 fkqlhsptnf lilsmattdf llscvvmpfs mvrsiescwy fgdlfckvhs ccdimlctts
      121 ifhlcfisvd rhyavcdplh yvtqitvgvv gvflliswsv pilfafglvf selnligaed
      181 fvaaidctgl cvlifnklwg vlasfiaffl pgaimvgiyi hiftvarkha rkigpgprtk
      241 ralseskmka tsgkeskatk tlsivmgvfv lcwlpffvlt itdpfigftt pedlynvflw
      301 lgyfnstfnp iiygmfypwf rkalrmivtg tifrsdssts slhpahp
//
LOCUS       NP_001020320             316 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 3 [Rattus norvegicus].
ACCESSION   NP_001020320 XP_575440
VERSION     NP_001020320.1
DBSOURCE    REFSEQ: accession NM_001025149.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362733.1.
            
            On Jul 1, 2005 this sequence version replaced XP_575440.1.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..316
                     /product="taste receptor type 2 member 3"
                     /note="T2R3; T2R11"
                     /calculated_mol_wt=36134
     Region          7..296
                     /region_name="7tm_TAS2R3"
                     /note="mammalian taste receptor 2, subtype 3, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15020"
                     /db_xref="CDD:320148"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320148"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320148"
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320148"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320148"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          178..201
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320148"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          226..251
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320148"
     Site            235..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     Region          263..288
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320148"
     Site            267..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET7.1)"
     CDS             1..316
                     /gene="Tas2r137"
                     /gene_synonym="RGD1560602; Tas2r3"
                     /coded_by="NM_001025149.1:1..951"
                     /db_xref="GeneID:500089"
                     /db_xref="RGD:1560602"
ORIGIN      
        1 mlgftegifl vltvtefilg nlvngfivsv ngshwfkskk islsdfiits lalfrifllw
       61 iiftdsliiv fsyhthdsgi rmqlidvfwt ftnhfsiwli sclsvfyclk iatfshpsfl
      121 wlkwrasrvv vgmlwgalvl scvctmslmn efkiysaltg srdtqnmtey irlkrheynl
      181 mhvlgnlwki pslivsliay fllllslgkh tqqmqkysvg srdqsaeahr ramriilsfl
      241 lfflfyflsf vilsssrflp etkiariigv vitmsylvgd slililgnnk lkqtfvailp
      301 cecghpkpgs krffas
//
LOCUS       NP_001102799             482 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC501899 [Rattus norvegicus].
ACCESSION   NP_001102799 XP_001069875 XP_577323
VERSION     NP_001102799.1
DBSOURCE    REFSEQ: accession NM_001109329.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH474196.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_577323.2, XP_001069875.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..482
                     /product="uncharacterized protein LOC501899"
                     /calculated_mol_wt=55936
     Region          <199..>403
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     CDS             1..482
                     /gene="Pramef8l1"
                     /gene_synonym="RGD1561226"
                     /coded_by="NM_001109329.1:1..1449"
                     /db_xref="GeneID:501899"
                     /db_xref="RGD:1561226"
ORIGIN      
        1 msfqtpptlq klarqtllrn eavamscvge lpivlfpalf keafegrhin lvkemvaawp
       61 fpclpvgalm ktpnaetlqa vldgvdmrlt rkfhprrikl qvldlrnvkh afwntwtgae
      121 dcscsaenle ekqvvkvfpr yalrrqrvkv itelsifscl eeqqacflkw aqermgslyf
      181 cctkmkiwdl pvcvireiln vfdpqhitel elhtewtlle lehfapyfgq mrnlrkvfle
      241 pfhkvtlsnr netrdreakc ikkfisqfsk fnclqhlcmf cthflrdhmn qvlgclmtpl
      301 etlsvtccvi sqndldsfsc clslfhlkhl dlrgvvlhdl dvmplrvlle kvadtletld
      361 lqwcrmknsq lyallpalrh csqlttvkfy snkfsmpilk dllqhtanws kvnveqypap
      421 qecyddssqv sverfsqlch elmdthrair qpknisfate icytcgercv yhngprlccc
      481 lq
//
LOCUS       NP_001008311             476 aa            linear   ROD 02-APR-2025
DEFINITION  relaxin-3 receptor 1 [Rattus norvegicus].
ACCESSION   NP_001008311 XP_226835
VERSION     NP_001008311.1
DBSOURCE    REFSEQ: accession NM_001008310.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Golyszny,M., Zielinski,M. and Obuchowicz,E.
  TITLE     Acute Stress Affects the Relaxin/Insulin-Like Family Peptide
            Receptor 3 mRNA Expression in Brain of Pubertal Male Wistar Rats
  JOURNAL   Dev Psychobiol 66 (6), e22523 (2024)
   PUBMED   38970242
  REMARK    GeneRIF: Acute Stress Affects the Relaxin/Insulin-Like Family
            Peptide Receptor 3 mRNA Expression in Brain of Pubertal Male Wistar
            Rats.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Vafaei,Z., Khodagholi,F., Nategh,M., Nikseresht,S.,
            Hashemirad,S.R., Raise-Abdullahi,P., Vafaei,A.A. and Motamedi,F.
  TITLE     Involvement of relaxin-family peptide-3 receptor (RXFP3) in the
            ventral dentate gyrus of the hippocampus in spatial and fear memory
            in rats
  JOURNAL   Peptides 178, 171244 (2024)
   PUBMED   38788901
  REMARK    GeneRIF: Involvement of relaxin-family peptide-3 receptor (RXFP3)
            in the ventral dentate gyrus of the hippocampus in spatial and fear
            memory in rats.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Kania,A., Szlaga,A., Sambak,P., Gugula,A., Blasiak,E., Micioni Di
            Bonaventura,M.V., Hossain,M.A., Cifani,C., Hess,G., Gundlach,A.L.
            and Blasiak,A.
  TITLE     RLN3/RXFP3 Signaling in the PVN Inhibits Magnocellular Neurons via
            M-like Current Activation and Contributes to Binge Eating Behavior
  JOURNAL   J Neurosci 40 (28), 5362-5375 (2020)
   PUBMED   32532885
  REMARK    GeneRIF: RLN3/RXFP3 Signaling in the PVN Inhibits Magnocellular
            Neurons via M-like Current Activation and Contributes to Binge
            Eating Behavior.
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Furuya,W.I., Dhingra,R.R., Gundlach,A.L., Hossain,M.A. and
            Dutschmann,M.
  TITLE     Relaxin-3 receptor (RXFP3) activation in the nucleus of the
            solitary tract modulates respiratory rate and the arterial
            chemoreceptor reflex in rat
  JOURNAL   Respir Physiol Neurobiol 271, 103310 (2020)
   PUBMED   31568840
  REMARK    GeneRIF: Activation of RXFP3 in the nucleus of the solitary tract
            selectively modulates respiration.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Zhang,X., Pan,L., Yang,K., Fu,Y., Liu,Y., Chen,W., Ma,X. and Yin,X.
  TITLE     Alterations of relaxin and its receptor system components in
            experimental diabetic cardiomyopathy rats
  JOURNAL   Cell Tissue Res 370 (2), 297-304 (2017)
   PUBMED   28776188
  REMARK    GeneRIF: Relaxin-1 mRNA in the hearts of diabetic rats was
            significantly increased and that relaxin-3 mRNA expression at
            different time points was decreased. In addition, significant
            down-regulation of the mRNA expression of RXFP1 and RXFP3 was
            observed at 4 weeks after Streptozocin.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Ma,S., Bonaventure,P., Ferraro,T., Shen,P.J., Burazin,T.C.,
            Bathgate,R.A., Liu,C., Tregear,G.W., Sutton,S.W. and Gundlach,A.L.
  TITLE     Relaxin-3 in GABA projection neurons of nucleus incertus suggests
            widespread influence on forebrain circuits via G-protein-coupled
            receptor-135 in the rat
  JOURNAL   Neuroscience 144 (1), 165-190 (2007)
   PUBMED   17071007
  REMARK    GeneRIF: RLX3 is the endogenous ligand for GPCR135 in rat brain
REFERENCE   7  (residues 1 to 476)
  AUTHORS   McGowan,B.M., Stanley,S.A., Smith,K.L., Minnion,J.S., Donovan,J.,
            Thompson,E.L., Patterson,M., Connolly,M.M., Abbott,C.R.,
            Small,C.J., Gardiner,J.V., Ghatei,M.A. and Bloom,S.R.
  TITLE     Effects of acute and chronic relaxin-3 on food intake and energy
            expenditure in rats
  JOURNAL   Regul Pept 136 (1-3), 72-77 (2006)
   PUBMED   16764952
  REMARK    GeneRIF: relaxin-3 and GPCR153 have roles in food intake and energy
            expenditure in rats
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Susens,U., Hermans-Borgmeyer,I., Urny,J. and Schaller,H.C.
  TITLE     Characterisation and differential expression of two very closely
            related G-protein-coupled receptors, GPR139 and GPR142, in mouse
            tissue and during mouse development
  JOURNAL   Neuropharmacology 50 (4), 512-520 (2006)
   PUBMED   16378626
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Tanaka,M., Iijima,N., Miyamoto,Y., Fukusumi,S., Itoh,Y., Ozawa,H.
            and Ibata,Y.
  TITLE     Neurons expressing relaxin 3/INSL 7 in the nucleus incertus respond
            to stress
  JOURNAL   Eur J Neurosci 21 (6), 1659-1670 (2005)
   PUBMED   15845093
  REMARK    GeneRIF: We then confirmed that c-Fos was induced in 60% of relaxin
            3 neurons in the nucleus incertus (NI) and the expression of
            relaxin 3 mRNA increased significantly in the NI after
            water-restraint stress.
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Chen,J., Kuei,C., Sutton,S.W., Bonaventure,P., Nepomuceno,D.,
            Eriste,E., Sillard,R., Lovenberg,T.W. and Liu,C.
  TITLE     Pharmacological characterization of relaxin-3/INSL7 receptors
            GPCR135 and GPCR142 from different mammalian species
  JOURNAL   J Pharmacol Exp Ther 312 (1), 83-95 (2005)
   PUBMED   15367576
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY633764.1.
            
            On Dec 16, 2004 this sequence version replaced XP_226835.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY633764.1, AY633763.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..476
                     /product="relaxin-3 receptor 1"
                     /note="relaxin-3/INSL7 receptor 1; G-protein coupled
                     receptor SALPR; relaxin/insulin-like family peptide
                     receptor 3"
                     /calculated_mol_wt=51899
     Region          89..407
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          91..115
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          125..146
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          163..185
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          223..239
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          272..295
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          332..354
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          375..400
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..476
                     /gene="Rxfp3"
                     /gene_synonym="GPCR135; RGD1311550; Rln3r1; Salpr"
                     /coded_by="NM_001008310.1:1..1431"
                     /db_xref="GeneID:294807"
                     /db_xref="RGD:1311550"
ORIGIN      
        1 mpkahlsmqv asattaapms kaaagdelsg ffglipdlle vanrssnasl qlqdlwwelg
       61 lelpdgaapg hppgsggaes adtearvril isavywvvca lglagnllvl ylmkskqgwr
      121 kssinlfvtn laltdfqfvl tlpfwavena ldfkwpfgka mckivsmvts mnmyasvffl
      181 tamsvaryhs vasalkshrt rghgrgdccg qslgesccfs akvlcgliwa saaiaslpnv
      241 ifsttinvlg eelclmhfpd kllgwdrqfw lglyhlqkvl lgfllplsii slcylllvrf
      301 isdrrvvgtt dgatapggsl stagarrrsk vtksvtivvl sfflcwlpnq alttwsilik
      361 fnvvpfsqey fqcqvyafpv svclahsnsc lnpilyclvr refrkalknl lwriaspslt
      421 smrpftattk pepedhglqa laplnataep dliyyppgvv vysggrydll psssay
//
LOCUS       NP_001102864             219 aa            linear   ROD 02-APR-2025
DEFINITION  claudin-20 [Rattus norvegicus].
ACCESSION   NP_001102864 XP_001054648
VERSION     NP_001102864.1
DBSOURCE    REFSEQ: accession NM_001109394.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Berndt,P., Winkler,L., Cording,J., Breitkreuz-Korff,O., Rex,A.,
            Dithmer,S., Rausch,V., Blasig,R., Richter,M., Sporbert,A.,
            Wolburg,H., Blasig,I.E. and Haseloff,R.F.
  TITLE     Tight junction proteins at the blood-brain barrier: far more than
            claudin-5
  JOURNAL   Cell Mol Life Sci 76 (10), 1987-2002 (2019)
   PUBMED   30734065
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Krause,G., Winkler,L., Mueller,S.L., Haseloff,R.F., Piontek,J. and
            Blasig,I.E.
  TITLE     Structure and function of claudins
  JOURNAL   Biochim Biophys Acta 1778 (3), 631-645 (2008)
   PUBMED   18036336
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474052.2.
            
            On Oct 4, 2007 this sequence version replaced XP_001054648.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..219
                     /product="claudin-20"
                     /calculated_mol_wt=23540
     Region          5..181
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     CDS             1..219
                     /gene="Cldn20"
                     /coded_by="NM_001109394.1:1..660"
                     /db_xref="GeneID:680178"
                     /db_xref="RGD:1595446"
ORIGIN      
        1 masaglqlla filavsgvsg vlaatllpnw kvnadagsti vtaivqvhgl wmdctwystg
       61 mfsctlkysi lslpvyvqaa ratmvlacil salgictaiv gmkcthlggd ahtkshisfa
      121 ggvcfitagi saliptvwyt keiisnfldl tvpeshkyep ggavyigfis amllliagii
      181 fcisyikknq epwiyppkqr ltstwqpknr laynlkdyv
//
LOCUS       NP_001019490             303 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 7-like [Rattus norvegicus].
ACCESSION   NP_001019490 XP_575388
VERSION     NP_001019490.1
DBSOURCE    REFSEQ: accession NM_001024319.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362742.1.
            
            On May 27, 2005 this sequence version replaced XP_575388.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q21"
     Protein         1..303
                     /product="taste receptor type 2 member 7-like"
                     /note="putative taste receptor T2R22"
                     /calculated_mol_wt=35061
     Region          8..290
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          10..34
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          46..67
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          84..106
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          133..149
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          177..200
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          228..250
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          261..286
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..303
                     /gene="Tas2r7l"
                     /gene_synonym="RGD1564521"
                     /coded_by="NM_001024319.1:1..912"
                     /db_xref="GeneID:500033"
                     /db_xref="RGD:1564521"
ORIGIN      
        1 mtfffpaiyh mvimtaefli gttvngflii vncydlfksr afpilptllm ctglsrlglq
       61 imlmtqsffs vffpysyeen iysskimfvw mffssiglwf atclsvfycl kisgftqpwf
      121 lwlkfriskl ifwlllgsll aslgtatvci evgfpliedg yilrntrlnn snvklmrnnn
      181 lllinltlll pltvfvmcts mlfislykhm yrmrsesqrm snarteahin alktvtsffc
      241 ffvsyfaafm anmtfripyr shqffvvkei maaypaghsv iiilsnskfk dlftrmiclq
      301 keg
//
LOCUS       NP_001101458            1216 aa            linear   ROD 02-APR-2025
DEFINITION  von Willebrand factor A domain-containing protein 5B1 [Rattus
            norvegicus].
ACCESSION   NP_001101458 XP_001070856 XP_233587
VERSION     NP_001101458.1
DBSOURCE    REFSEQ: accession NM_001107988.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_233587.4, XP_001070856.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132299, SAMD00155312
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1216
                     /product="von Willebrand factor A domain-containing
                     protein 5B1"
                     /calculated_mol_wt=134608
     Region          2..79
                     /region_name="VIT_2"
                     /note="Vault protein inter-alpha-trypsin domain;
                     pfam13757"
                     /db_xref="CDD:404621"
     Region          350..519
                     /region_name="vWA_interalpha_trypsin_inhibitor"
                     /note="vWA_interalpha trypsin inhibitor (ITI): ITI is a
                     glycoprotein composed of three polypeptides- two heavy
                     chains and one light chain (bikunin). Bikunin confers the
                     protease-inhibitor function while the heavy chains are
                     involved in rendering stability to...; cd01461"
                     /db_xref="CDD:238738"
     Site            order(359,361,363,430,457)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238738"
     CDS             1..1216
                     /gene="Vwa5b1"
                     /gene_synonym="RGD1308559"
                     /coded_by="NM_001107988.1:133..3783"
                     /db_xref="GeneID:313653"
                     /db_xref="RGD:1308559"
ORIGIN      
        1 mpgllncftg aalpltasdv tsyvsgyalg ltasltygnl eaqpfqglfv yptdecttvv
       61 gfeaviadrv vtiqlrdkak ldrsyldvqs atvtgnlpee eipitpgkvt ldedlerilf
      121 vvnlgtiapm envtifists selptlpsga vrvllpaica ptvhpfcahr fgssrqqprg
      181 kdphcfgtqs kdsykrlcla tlldtkvtnp meyefkfqle irgpcllagv esptheirad
      241 aapsahsaks iiitlakkht fdrpveillh psephmphvl vekgdmtlge fyqhlkrkad
      301 fvrgtkkdni aerktevirk rlhkdiphhs vimlnfcpdl esvqpnprrt hgefiflidr
      361 sssmsktniq cikeamlval kslmpaclfn vigfgstfkt vfassqiyne enlalaceci
      421 qrmradmggt nifsplkwvl rqplrqghpr llflitdgsv nntgkvlelv rnhassircy
      481 sfgigptvcy rlvkglasvs kgsaeflmeg erlqpkmvks lkkamapvls dvtvewvfpe
      541 ttealispvs tsslfpgerl vgygivcdas lyisnsrsdk rrkygmlhaq essssvfyhs
      601 qdeglrpgsg ncaknfnqgq tkdahpcngd slshhgldgs rrrraystnq isshkacsra
      661 ttasdptgtt rryplrkakv qdlahqssse sqqwqidlqp lltrghdpsq gprlhgpgar
      721 rpsllpqgcq pmrfsgpepq awspvrelgl gsgrksvlns rssedlatep ppfpstlepe
      781 tssdleptae leeqapyrta tpspvlgkvl vkgvcdnqhm qwevsfelep palrredtqn
      841 ddmwgetfhh laaraiiref ehlaqredei elgsnrryqv navhtskacn viskytafvp
      901 vdinkrqylp tvvkyhnsga llsfrnltrq wkgfstglrr sqsmlrehss aagdskfqtl
      961 alhesltstf nktpspghek yataegppqn lstsslsstk aseaifgsrl ilnksrlltr
     1021 atknflsksl pkapevnpgs qssdyvplvs lqlasgafll nevfcrtiqi pmeklkwtsp
     1081 fnclrmslvt rrhdlktqsp gdctslsspp ppsddislks gakdssdqes sellehtgkl
     1141 watvvalawl ehssasyiie welvaakass wvelqevpeg rtlstikata rqlfvllrhw
     1201 denlefnmlc ynpnym
//
LOCUS       NP_001004130             481 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type I cytoskeletal 39 [Rattus norvegicus].
ACCESSION   NP_001004130 XP_220946
VERSION     NP_001004130.1
DBSOURCE    REFSEQ: accession NM_001004130.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004035.1.
            
            On Sep 5, 2004 this sequence version replaced XP_220946.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004035.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN09345329,
                                           SAMN16093044 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..481
                     /product="keratin, type I cytoskeletal 39"
                     /note="K39; CK-39; cytokeratin-39; type I hair keratin
                     KA35; keratin 39, type I"
                     /calculated_mol_wt=54207
     Region          1..90
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          90..400
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          91..125
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          126..136
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          137..237
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          238..253
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Region          254..397
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     Site            339
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q6IFW3.1)"
     Region          398..481
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW3.1)"
     CDS             1..481
                     /gene="Krt39"
                     /gene_synonym="Ka35"
                     /coded_by="NM_001004130.1:1..1446"
                     /db_xref="GeneID:303523"
                     /db_xref="RGD:1303032"
ORIGIN      
        1 mdtkgstvti ssstppqncs gntnvrtnss nkscyhdvqs tghalqtpqg qgcrpspcly
       61 rcpnylirty sfhpcpddcs rcsdginshe ketmqilner lasylekvrm legenadled
      121 kiqeecsktl pilcpdylsy yttieqlqqk ilctkaensr lvsqidntkl aaddlrakye
      181 aelslrqlve adanglkqil daltlskadl earvqsltee llclktnhee einslqcqlg
      241 drinievtaa psvdlnqilq kmrcqyesiv etnrkdveew fntqmeelnq qvvsssqqqq
      301 ccqkdiielr rtisalevel qaqhrmrdsq ecilaetear ytallaqiqs lihnleaqva
      361 eirsalqrqn qeyevlldik srleceiaty rsllesldgr lpcnpctttw epscqarame
      421 cltpvytsis lpgihkpcra sgppsrilvk ictitkeikd gkvisshehv qpcyitrpak
      481 v
//
LOCUS       NP_001008820             455 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type I cuticular Ha5 [Rattus norvegicus].
ACCESSION   NP_001008820 XP_220970
VERSION     NP_001008820.1
DBSOURCE    REFSEQ: accession NM_001008820.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004042.1.
            
            On Jan 5, 2005 this sequence version replaced XP_220970.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004042.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN12840107,
                                           SAMN12840108 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..455
                     /product="keratin, type I cuticular Ha5"
                     /note="keratin complex 1, acidic, gene 2; type I hair
                     keratin KA30; keratin 35, type I"
                     /calculated_mol_wt=50544
     Region          96..407
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     CDS             1..455
                     /gene="Krt35"
                     /gene_synonym="Ka30; Krt1-2"
                     /coded_by="NM_001008820.1:1..1368"
                     /db_xref="GeneID:287697"
                     /db_xref="RGD:1305300"
ORIGIN      
        1 maskcfkasf ssgslkspgk agggstrmsr mysssscklp spsrgarsfs vcsaglgrgn
       61 yrlssclpal clptggfatg ysmgggwfge giltgneket mqslndrlas ylekvrqleq
      121 enaslesrir ewceqqvpym cpdyqsyfrt meelqkktlc skaenarlvv qidnaklaad
      181 dfrtkyetev slrqlveadi nglrrilddl tlckadleaq veslkeellc lkknheeevn
      241 slrcqlgdrl nvevdaappv dlnrvldemr cqyetlvenn rrdaedwydt qteelnqqvv
      301 tsseqlqscq sdiielrrtv nsleielqaq qsmrdaldst laetearyss qlaqmqclig
      361 svesqlgeir adlerqnqey qvlldvrarl eceintyrgl lesedsklpc npcapdysps
      421 ksclpclpav scstgaartt csprpvcvpc pggrf
//
LOCUS       NP_783178                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7g [Rattus norvegicus].
ACCESSION   NP_783178
VERSION     NP_783178.1
DBSOURCE    REFSEQ: accession NM_175588.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380197.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7g"
                     /note="taR-9; taR-7g; trace amine receptor 7g; trace amine
                     receptor 9"
                     /calculated_mol_wt=39832
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y1.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            124..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y1.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y1.1)"
     CDS             1..358
                     /gene="Taar7g"
                     /gene_synonym="Ta9"
                     /coded_by="NM_175588.1:1..1077"
                     /db_xref="GeneID:294131"
                     /db_xref="RGD:631388"
ORIGIN      
        1 matddgsfpw tqesilsrdl lsalspqlcy enlnrscvrs pyspgsrlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadllvgltv mpfsmvrsve gcwyfgdsyc
      121 klhscfdisf csssllhlcf isvdrhiavs dpliyptrft asvsgkyitf swllsiiygf
      181 sliytgasea gledlvsalt cvggcqvavn qswvfinfll flvpalvmmt vyskifliak
      241 qqaqnmekms kqtarasdsy kdrvakrerk aaktlgiava afllswlpyf vdsiidaflg
      301 fitptyvyei lawiayynsa mnpliyaffy pwfrkaikli vtgkilkens stinlfpe
//
LOCUS       NP_001160152             307 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 106 [Rattus norvegicus].
ACCESSION   NP_001160152
VERSION     NP_001160152.1
DBSOURCE    REFSEQ: accession NM_001166680.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362739.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..307
                     /product="taste receptor type 2 member 106"
                     /note="T2R19; T2R106; taste receptor type 2 member 19"
                     /calculated_mol_wt=35195
     Region          7..289
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          9..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          44..65
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          82..104
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            82..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          131..147
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          171..194
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          222..244
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     Region          256..281
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET1.1)"
     CDS             1..307
                     /gene="Tas2r106"
                     /coded_by="NM_001166680.1:1..924"
                     /db_xref="GeneID:100310878"
                     /db_xref="RGD:2314260"
ORIGIN      
        1 mltipegill cfitsgsvlg vlgngfilhv nctdcvrqkf sttgfiftgl aisricvici
       61 iisdgylklf sphmvasdah iigisylwii tnhtstcfat ilnlfyflki anfshyiffc
      121 lkrklntifi fllgclfisw svafpqtvki fndkmkhrnt swkfhlhksk fiinhillnl
      181 gviffcmvai itsflliisl wkhnrkmqly vsrfkslnte vhlkvmkvli sfiillilhv
      241 igilietlsf lryenkllli lglnfssmyp cchsfilila nnqlkqaslk alkqfkchkk
      301 dkdvret
//
LOCUS       NP_001020232             294 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 143 [Rattus norvegicus].
ACCESSION   NP_001020232 XP_578254
VERSION     NP_001020232.1
DBSOURCE    REFSEQ: accession NM_001025061.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362747.1.
            
            On Jun 25, 2005 this sequence version replaced XP_578254.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..294
                     /product="taste receptor type 2 member 143"
                     /note="T2R27; T2R143; taste receptor type 2 member 27"
                     /calculated_mol_wt=33980
     Region          7..291
                     /region_name="7tm_TAS2R16"
                     /note="mammalian taste receptor 2, subtype 16, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15017"
                     /db_xref="CDD:320145"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320145"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320145"
     Region          78..100
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320145"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Region          127..143
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320145"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES3.1)"
     Region          174..197
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320145"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Region          222..247
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320145"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320145"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES3.1)"
     CDS             1..294
                     /gene="Tas2r143"
                     /gene_synonym="RGD1566290"
                     /coded_by="NM_001025061.1:1..885"
                     /db_xref="GeneID:502756"
                     /db_xref="RGD:1566290"
ORIGIN      
        1 mpstptlifi vifflvsvas mlqngfmiiv lgrewmrnra lpavdmivas lassrfclhg
       61 iailnnflas fdfcyqanfv gilwdfintl ilwltawlai fycvkissfs hpvlfwlkwr
      121 isqlvprlll vslimgglsa iisatgniia nqmiisqgfh gnctfghmsl dfyryyylsh
      181 avlmwftpff lflvsiiflm fslyrhvekm rghrpgpwdp rtqahtmalk sltvfitfyi
      241 lfflaliiss tksktmhsyw ywvreiiiyt giflnsiilv lsnpklrkal kmrf
//
LOCUS       NP_064475               1181 aa            linear   ROD 02-APR-2025
DEFINITION  sodium/potassium/calcium exchanger 1 [Rattus norvegicus].
ACCESSION   NP_064475 XP_346826
VERSION     NP_064475.1
DBSOURCE    REFSEQ: accession NM_020090.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Jalloul,A.H., Szerencsei,R.T. and Schnetkamp,P.P.
  TITLE     Cation dependencies and turnover rates of the human K-dependent
            Na-Ca(2) exchangers NCKX1, NCKX2, NCKX3 and NCKX4
  JOURNAL   Cell Calcium 59 (1), 1-11 (2016)
   PUBMED   26631410
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Zheng,M., Gong,Y., Wang,X., Xie,Q., Tang,H., Wang,D. and Chen,X.
  TITLE     Alteration of intracellular calcium and its modulator SLC24A6 after
            experimental intracerebral hemorrhage
  JOURNAL   Acta Neurochir Suppl 118, 169-173 (2013)
   PUBMED   23564126
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Lytton,J.
  TITLE     Na+/Ca2+ exchangers: three mammalian gene families control Ca2+
            transport
  JOURNAL   Biochem J 406 (3), 365-382 (2007)
   PUBMED   17716241
  REMARK    Review article
REFERENCE   4  (residues 1 to 1181)
  AUTHORS   Altimimi,H.F. and Schnetkamp,P.P.
  TITLE     Na+/Ca2+-K+ exchangers (NCKX): functional properties and
            physiological roles
  JOURNAL   Channels (Austin) 1 (2), 62-69 (2007)
   PUBMED   18690016
  REMARK    Review article
REFERENCE   5  (residues 1 to 1181)
  AUTHORS   Li,X.F. and Lytton,J.
  TITLE     Differential expression of Na/Ca exchanger and Na/Ca + K exchanger
            transcripts in rat brain
  JOURNAL   Ann N Y Acad Sci 976, 64-66 (2002)
   PUBMED   12502535
  REMARK    GeneRIF: Differential expression in the rat brain
REFERENCE   6  (residues 1 to 1181)
  AUTHORS   Poon,S., Leach,S., Li,X.F., Tucker,J.E., Schnetkamp,P.P. and
            Lytton,J.
  TITLE     Alternatively spliced isoforms of the rat eye
            sodium/calcium+potassium exchanger NCKX1
  JOURNAL   Am J Physiol Cell Physiol 278 (4), C651-C660 (2000)
   PUBMED   10751314
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF176688.1.
            
            On May 4, 2006 this sequence version replaced XP_346826.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF176688.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1181
                     /product="sodium/potassium/calcium exchanger 1"
                     /note="retinal rod Na-Ca+K exchanger;
                     Na(+)/K(+)/Ca(2+)-exchange protein 1;
                     sodium/calcium/potassium exchanger; solute carrier family
                     24 (sodium/potassium/calcium exchanger), member 1; retinal
                     Na/Ca,K exchanger"
                     /calculated_mol_wt=129851
     Region          1..1181
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          107..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          255..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          300..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            420..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          461..501
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            465..485
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            492..512
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            520..544
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            553..569
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          598..617
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          650..983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60721; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          730..905
                     /region_name="14 X approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            990..1010
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            1018..1038
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            1054..1074
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Region          1061..1092
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            1093..1113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            1122..1142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     Site            1151..1171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM6.1)"
     CDS             1..1181
                     /gene="Slc24a1"
                     /gene_synonym="Nckx1"
                     /coded_by="NM_020090.1:5..3550"
                     /db_xref="GeneID:56814"
                     /db_xref="RGD:620080"
ORIGIN      
        1 mgklirmgtq errllrpkrl hwsrllfflg mliigstyqh lrrpqnppsm wtkvssqqpi
       61 klairdlpnd eitvtdkdpp eassevegem lapqdtviig eaapsiamed tpnppittki
      121 tptslknnys pttagtrrqk enipptpsra pshfistsgr qrvksytpkp rggrkssspt
      181 htreegrmht pspagaprti sptstekdse ttatyrmlep rsertagkts lkrmvpntrt
      241 fltrevetdl vtspslvgkn tlgsprrger nssttplrav lqptpatsee qvtasirmgs
      301 tpattegsta aqrignplsg tstpavrias vtdrekrpst ahgtlvtpqv kavlttqvhr
      361 cvvvkpapav pmtpspsmta ilfpeaptsg psalppgwpn lhpkaeyppd lfsvedrrqg
      421 wvvlhifgmt yvfvalaivc deyfvpalgv itdklqised vagatfmaag gsapelftsl
      481 igvfishsnv gigtivgsav fnilfvigtc alfsreilnl twwplfrdvs fyildlsmli
      541 vffldsliaw weslllllay alyvftmkwn kqierwvkeq lsrrpvakvm algdlskpsd
      601 gaieeneqqd nkklklpsvl trgsssaslh nsiirstiyh lmlhsldplg earpskdkqe
      661 slnqearvlp qtkaesssde eepaelpavt vtpapapedk gdqeedpgcq edvdeaehrg
      721 dmtgeegere teaegkkdee geteaerked gqeeetetkg kekqegetes egkdeqeget
      781 eaegkeadhe geteaegkev ehegeteaeg tedeqegete aegkeveqeg eteaegkeve
      841 heveteaerk etnhegetea egkeadhege teaegnvehq geteaegkve hegeteagek
      901 dehegqsetq addtevkdge geaeanaedq cetaqgekga dggggsdggd seeeedeede
      961 eeeeeeeeee eeeeseepls lewpesrqkq aiylfllpiv fplwltipdv rrqearkffv
     1021 itflgsiiwi amfsylmvww ahqvgetigi seeimgltil aagtsipdli tsvivarkgl
     1081 gdmavsssvg snifditvgl pvpwllfsli nalqpipvss nglfcaivll flmllfvifs
     1141 iasckwrmnk ilgftmflly fvflvisvml edriiscpvs v
//
LOCUS       NP_001103614             220 aa            linear   ROD 02-APR-2025
DEFINITION  putative claudin-24 [Rattus norvegicus].
ACCESSION   NP_001103614 XP_001059310 XP_577519
VERSION     NP_001103614.1
DBSOURCE    REFSEQ: accession NM_001110144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Mineta,K., Yamamoto,Y., Yamazaki,Y., Tanaka,H., Tada,Y., Saito,K.,
            Tamura,A., Igarashi,M., Endo,T., Takeuchi,K. and Tsukita,S.
  TITLE     Predicted expansion of the claudin multigene family
  JOURNAL   FEBS Lett 585 (4), 606-612 (2011)
   PUBMED   21276448
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473995.2.
            
            On or before Oct 26, 2007 this sequence version replaced
            XP_577519.1, XP_001059310.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..220
                     /product="putative claudin-24"
                     /note="claudin 22 like"
                     /calculated_mol_wt=24046
     Region          7..180
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     CDS             1..220
                     /gene="Cldn24"
                     /gene_synonym="RGD1562043"
                     /coded_by="NM_001110144.1:1..663"
                     /db_xref="GeneID:502083"
                     /db_xref="RGD:1562043"
ORIGIN      
        1 mafifktamq svalslsllg wvlaitttyl phwknlnlel nemenwtmgl wkscviqeev
       61 grqckdfdsf lalpaelqis rilmslsngl gllgllasgc gldclrlget rkglkrrlli
      121 lggtllwtsg vmvlvpvswv ahmtvqefwd etvpeivprw efgealflgw faglclvlgg
      181 cvlhcaacwr pappasghya vaglgdhssy lengtaqpkv
//
LOCUS       NP_001013937             329 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 134 [Rattus norvegicus].
ACCESSION   NP_001013937 XP_003753770 XP_008773599 XP_229912
VERSION     NP_001013937.1
DBSOURCE    REFSEQ: accession NM_001013915.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wu,S.V., Chen,M.C. and Rozengurt,E.
  TITLE     Genomic organization, expression, and function of bitter taste
            receptors (T2R) in mouse and rat
  JOURNAL   Physiol Genomics 22 (2), 139-149 (2005)
   PUBMED   15886333
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362743.1.
            
            On or before Aug 24, 2014 this sequence version replaced
            XP_008773599.1, XP_003753770.1, XP_229912.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..329
                     /product="taste receptor type 2 member 134"
                     /note="taste receptor type 2 member 23"
                     /calculated_mol_wt=37931
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          32..312
                     /region_name="7tm_TAS2R16"
                     /note="mammalian taste receptor 2, subtype 16, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15017"
                     /db_xref="CDD:320145"
     Region          33..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320145"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          70..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320145"
     Region          103..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320145"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          152..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320145"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          195..218
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320145"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          243..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320145"
     Site            252..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     Region          279..304
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320145"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES7.1)"
     CDS             1..329
                     /gene="Tas2r134"
                     /gene_synonym="GPCR; T2R134; T2R23; T2R34"
                     /coded_by="NM_001013915.1:1..990"
                     /db_xref="GeneID:295589"
                     /db_xref="RGD:1359393"
ORIGIN      
        1 mrcslrgcvq grggksgvsl skfspkkmsf ffifmvifci qslvallqng flatvlgrew
       61 vrsqglpagd mivaclaasr fclhgvaivn nfltfvklws qkiyfsvlwd fvntvnfwct
      121 twlaifycvk issfshpiff wikwrisrsv prlllgslvi gglsavssat gntiafqmta
      181 cenytlayrt rafyayyfrc hamlmwiipf flfllsvill mfslyrhleh mryrrpwshd
      241 ystqahtmal kslafflvfy tsyvlflvis vtrvvnvhss whwawevity mgillhstil
      301 tlsnpkmrka lkikfpdlcv arsqdkrrg
//
LOCUS       NP_001102432             253 aa            linear   ROD 02-APR-2025
DEFINITION  peptidase inhibitor R3HDML precursor [Rattus norvegicus].
ACCESSION   NP_001102432 XP_001070429
VERSION     NP_001102432.1
DBSOURCE    REFSEQ: accession NM_001108962.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474005.2.
            
            On Oct 4, 2007 this sequence version replaced XP_001070429.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16418971
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..253
                     /product="peptidase inhibitor R3HDML precursor"
                     /note="peptidase inhibitor R3HDML; R3H domain (binds
                     single-stranded nucleic acids) containing-like"
                     /calculated_mol_wt=25899
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2413
     Region          63..208
                     /region_name="CAP_R3HDML"
                     /note="CAP (cysteine-rich secretory proteins, antigen 5,
                     and pathogenesis-related 1 proteins) domain of peptidase
                     inhibitor R3HDML; cd18815"
                     /db_xref="CDD:349409"
     CDS             1..253
                     /gene="R3hdml"
                     /coded_by="NM_001108962.1:171..932"
                     /db_xref="GeneID:366245"
                     /db_xref="RGD:1305296"
ORIGIN      
        1 mpllysivgl aglllwmght vgalrmpntt lvqgrpknia vwplsglgvp rhrrkrhisa
       61 rdmnalldyh nhirasvhpp asnmeymvwd eqlaraaeaw atqciwahgp sqltkyvgqn
      121 lsvhsgryrs vvdlvkswse ekrhysfpap kdctphcpwl csgpvcshyt qmvwasssrl
      181 gcaihtcssi nvwgstwqqa vylvcnyaik gnwigeapyk tgkpcsacpp syqgncnsnm
      241 cfsglksnrl pwv
//
LOCUS       NP_001160150             330 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 136 [Rattus norvegicus].
ACCESSION   NP_001160150
VERSION     NP_001160150.1
DBSOURCE    REFSEQ: accession NM_001166678.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473964.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..330
                     /product="taste receptor type 2 member 136"
                     /note="T2R40; T2R136; taste receptor type 2 member 40"
                     /calculated_mol_wt=37227
     Region          26..316
                     /region_name="7tm_TAS2R43-like"
                     /note="mammalian taste receptor 2, subtype 43, and related
                     proteins, member of the seven-transmembrane G
                     protein-coupled receptor superfamily; cd15027"
                     /db_xref="CDD:320155"
     Region          31..56
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320155"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          68..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320155"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          104..126
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320155"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          153..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320155"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          195..218
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320155"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675B7.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          243..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320155"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     Region          280..305
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320155"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B7.1)"
     CDS             1..330
                     /gene="Tas2r136"
                     /coded_by="NM_001166678.1:1..993"
                     /db_xref="GeneID:100310876"
                     /db_xref="RGD:2314262"
ORIGIN      
        1 mksqpvtqel hfifplfkti ssdimsflvs iagiamlaqi vlgtfanvfi vlvtctdcir
       61 rrklfladgi ltslafcrig mlwviliswc sivfhqalsl qvrfsicvgw avtnhfnmwl
      121 atilsilyll kignfsnlif lglkrkiksv fivvllaslv llfpnlitvt vcetvqangy
      181 rgnltgktkr tyfmnltami sftldniisf tismvcflll iyslckhlrt mrlygkgphn
      241 psasahikal qavisflllf smfilsliis gynymkplne pvhlicqlig tlypsshsyv
      301 llwgnrrikl afvlamvqvr arlwlkeekp
//
LOCUS       NP_001011702             194 aa            linear   ROD 02-APR-2025
DEFINITION  Spetex-2E protein [Rattus norvegicus].
ACCESSION   NP_001011702 XP_008768812 XP_341288
VERSION     NP_001011702.1
DBSOURCE    REFSEQ: accession NM_001011702.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Iwamoto,Y., Kaneko,T., Ichinose,J., Mori,T., Shibata,Y.,
            Toshimori,K. and Iida,H.
  TITLE     Molecular cloning of rat Spetex2 family genes mapped on chromosome
            15p16, encoding a 23-kilodalton protein associated with the plasma
            membranes of haploid spermatids
  JOURNAL   Biol Reprod 72 (2), 284-292 (2005)
   PUBMED   15371276
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB180080.1.
            
            On or before Aug 24, 2014 this sequence version replaced
            XP_008768812.1, XP_341288.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB180080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..194
                     /product="Spetex-2E protein"
                     /note="Spetex-2G protein-like"
                     /calculated_mol_wt=23065
     Region          34..114
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..194
                     /gene="Spetex2e"
                     /gene_synonym="Spetex-2E"
                     /coded_by="NM_001011702.1:1..585"
                     /db_xref="GeneID:361012"
                     /db_xref="RGD:1359714"
ORIGIN      
        1 mfhqllkliq kergdqgetr prqkkaglls wfirkassen fisnhekrik kleelkseiq
       61 kckierdels qildlyvndg lnyrlsvelp mlksqhemrm mdmhkmtnwi sdamekykel
      121 tqennsyrir nfhllnerne lkknirilmn enrkllveqt elqasceegk rlceeaskti
      181 ytadieslcp vtfe
//
LOCUS       NP_001102383             116 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC365238 [Rattus norvegicus].
ACCESSION   NP_001102383 XP_001073383 XP_001080052
VERSION     NP_001102383.1
DBSOURCE    REFSEQ: accession NM_001108913.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001080052.1, XP_001073383.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..116
                     /product="uncharacterized protein LOC365238"
                     /calculated_mol_wt=13498
     CDS             1..116
                     /gene="Fam32al1"
                     /coded_by="NM_001108913.1:2112..2462"
                     /db_xref="GeneID:365238"
                     /db_xref="RGD:1583796"
ORIGIN      
        1 maastmeaye qvqkgplklk gvaelgvtkr rkkkdkdkak mletmgmrkk seeekqhcld
       61 krtpaqaafe kmqekrqter ilkkaskthk qrvedfnrhl dtltehydip kvswtk
//
LOCUS       NP_001020233             321 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 135 [Rattus norvegicus].
ACCESSION   NP_001020233 XP_578255
VERSION     NP_001020233.1
DBSOURCE    REFSEQ: accession NM_001025062.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362748.1.
            
            On Jun 25, 2005 this sequence version replaced XP_578255.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..321
                     /product="taste receptor type 2 member 135"
                     /note="T2R28; T2R35; T2R135; taste receptor type 2 member
                     28"
                     /calculated_mol_wt=36360
     Region          27..317
                     /region_name="7tm_TAS2R41-like"
                     /note="mammalian taste receptor 2, subtype 41, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15018"
                     /db_xref="CDD:320146"
     Region          28..53
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320146"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          65..89
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320146"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          103..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320146"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          152..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320146"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          200..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320146"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          248..273
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320146"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     Region          284..309
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320146"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES2.1)"
     CDS             1..321
                     /gene="Tas2r135"
                     /gene_synonym="RGD1561078"
                     /coded_by="NM_001025062.1:1..966"
                     /db_xref="GeneID:502757"
                     /db_xref="RGD:1561078"
ORIGIN      
        1 mgpimstget stahtvlgcq itdktvitlf vilvfsclva vvgngfiiia lgmkwllrrt
       61 lsahnkllis laasrfclqc vvigkniyvf lnpssfpynp viqllnlmwd fltaatiwfc
      121 sllgffycvk iatlthpvfv wlkyrlpgwv pwmllsavgm ssltsilcfi gnhmiyqnya
      181 rrghqpwnat gnslrhslek fyfisikiim wtvptvifsi fmslllvslv rhmkktllal
      241 selrdvwaqa hfkallplls fiilfiscfl tlvlssasst pyqefrywmw qvvihlctvi
      301 hpivillsnp vlrvvmkrgc c
//
LOCUS       NP_001032721             410 aa            linear   ROD 02-APR-2025
DEFINITION  transcription factor Sp7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001032721
VERSION     NP_001032721.1
DBSOURCE    REFSEQ: accession NM_001037632.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   da Silva Sasso,G.R., Florencio-Silva,R., Sasso-Cerri,E., Gil,C.D.,
            de Jesus Simoes,M. and Cerri,P.S.
  TITLE     Spatio-temporal immunolocalization of VEGF-A, Runx2, and osterix
            during the early steps of intramembranous ossification of the
            alveolar process in rat embryos
  JOURNAL   Dev Biol 478, 133-143 (2021)
   PUBMED   34245724
  REMARK    GeneRIF: Spatio-temporal immunolocalization of VEGF-A, Runx2, and
            osterix during the early steps of intramembranous ossification of
            the alveolar process in rat embryos.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Pokrovskaya,L.A., Nadezhdin,S.V., Zubareva,E.V., Burda,Y.E. and
            Gnezdyukova,E.S.
  TITLE     Expression of RUNX2 and Osterix in Rat Mesenchymal Stem Cells
            during Culturing in Osteogenic-Conditioned Medium
  JOURNAL   Bull Exp Biol Med 169 (4), 571-575 (2020)
   PUBMED   32910396
  REMARK    GeneRIF: Expression of RUNX2 and Osterix in Rat Mesenchymal Stem
            Cells during Culturing in Osteogenic-Conditioned Medium.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Qin,G., Li,Y., Wang,H., Yang,J., Chen,Q., Tang,H., Wang,Y.,
            Zhang,M., Jiang,T., Lin,S. and Huo,S.
  TITLE     Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation
            via Regulating the Binding Ability of H3K9me3 with the Promoters of
            Runx2, Osterix and Osteocalcin
  JOURNAL   J Biomed Nanotechnol 16 (6), 899-909 (2020)
   PUBMED   33187585
  REMARK    GeneRIF: Lysine-Specific Demethylase 4A Regulates Osteogenic
            Differentiation via Regulating the Binding Ability of H3K9me3 with
            the Promoters of Runx2, Osterix and Osteocalcin.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Xi,Y., Miao,X., Li,Y., Lai,K., Du,X., Jiang,Z., Wang,Y. and Yang,G.
  TITLE     BMP2-mimicking peptide modified with E7 coupling to calcined bovine
            bone enhanced bone regeneration associating with activation of the
            Runx2/SP7 signaling axis
  JOURNAL   J Biomed Mater Res B Appl Biomater 108 (1), 80-93 (2020)
   PUBMED   30912295
  REMARK    GeneRIF: BMP2-mimicking peptide modified with E7 coupling to
            calcined bovine bone enhanced bone regeneration associating with
            activation of the Runx2/SP7 signaling axis.
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Fukuda,M., Yoshizawa,T., Karim,M.F., Sobuz,S.U., Korogi,W.,
            Kobayasi,D., Okanishi,H., Tasaki,M., Ono,K., Sawa,T., Sato,Y.,
            Chirifu,M., Masuda,T., Nakamura,T., Tanoue,H., Nakashima,K.,
            Kobashigawa,Y., Morioka,H., Bober,E., Ohtsuki,S., Yamagata,Y.,
            Ando,Y., Oike,Y., Araki,N., Takeda,S., Mizuta,H. and Yamagata,K.
  TITLE     SIRT7 has a critical role in bone formation by regulating lysine
            acylation of SP7/Osterix
  JOURNAL   Nat Commun 9 (1), 2833 (2018)
   PUBMED   30026585
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Amorim,B.R., Okamura,H., Yoshida,K., Qiu,L., Morimoto,H. and
            Haneji,T.
  TITLE     The transcriptional factor Osterix directly interacts with RNA
            helicase A
  JOURNAL   Biochem Biophys Res Commun 355 (2), 347-351 (2007)
   PUBMED   17303075
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Wang,B.L., Dai,C.L., Quan,J.X., Zhu,Z.F., Zheng,F., Zhang,H.X.,
            Guo,S.Y., Guo,G., Zhang,J.Y. and Qiu,M.C.
  TITLE     Parathyroid hormone regulates osterix and Runx2 mRNA expression
            predominantly through protein kinase A signaling in osteoblast-like
            cells
  JOURNAL   J Endocrinol Invest 29 (2), 101-108 (2006)
   PUBMED   16610234
  REMARK    GeneRIF: Parathyroid hormone (1-34) regulates osterix mRNA
            expression, in rat osteoblast-like cell line UMR 106, in a dose-
            and time-dependent manner.
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Koga,T., Matsui,Y., Asagiri,M., Kodama,T., de Crombrugghe,B.,
            Nakashima,K. and Takayanagi,H.
  TITLE     NFAT and Osterix cooperatively regulate bone formation
  JOURNAL   Nat Med 11 (8), 880-885 (2005)
   PUBMED   16041384
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Milona,M.A., Gough,J.E. and Edgar,A.J.
  TITLE     Expression of alternatively spliced isoforms of human Sp7 in
            osteoblast-like cells
  JOURNAL   BMC Genomics 4, 43 (2003)
   PUBMED   14604442
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Nakashima,K., Zhou,X., Kunkel,G., Zhang,Z., Deng,J.M.,
            Behringer,R.R. and de Crombrugghe,B.
  TITLE     The novel zinc finger-containing transcription factor osterix is
            required for osteoblast differentiation and bone formation
  JOURNAL   Cell 108 (1), 17-29 (2002)
   PUBMED   11792318
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK001413.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..410
                     /product="transcription factor Sp7 isoform 1"
                     /note="osterix; Transcription factor Sp7"
                     /calculated_mol_wt=42645
     Region          1..274
                     /region_name="SP6-9_N"
                     /note="N-terminal domains of transcription factor
                     Specificity Proteins (SP) 6-9, and similar proteins;
                     cl41771"
                     /db_xref="CDD:425402"
     Region          278..297
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(282,284,286,288..289,292..293,296,312,314,318..319,
                     322..323,326,340,342,344,346..347,350..351,354)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          289..316
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          305..327
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..344
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          335..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..410
                     /gene="Sp7"
                     /gene_synonym="Osx"
                     /coded_by="NM_001037632.1:273..1505"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300260"
                     /db_xref="RGD:631377"
ORIGIN      
        1 mltaacskfg gssplrdsta lgkggtkkpy tdlsapktmg daypapfsst ngllspagsp
       61 papasgyand yppfphsfpg ptgaqdpgll vpkghsssdc lpsvytsldm shpygswyka
      121 gihagispgp gntptpwwdm hpggnwlggg qgqgdglqgt lstgpaqppl npqlptypsd
      181 faplnpapyp aphllqpgpq hvlpqdvykp kavgnsgqle gsgagkpprg agtggsggya
      241 gsgagrstcd cpncqelerl gaaaaglrkk pihschipgc gkvygkashl kahlrwhtge
      301 rpfvcnwlfc gkrftrsdel erhvrthtre kkftcllcsk rftrsdhlsk hqrthgepgp
      361 gpppsgpkel gegrsvgeee anqpprssts pappekapgg speqsnllei
//
LOCUS       NP_001020451             434 aa            linear   ROD 02-APR-2025
DEFINITION  sodium/bile acid cotransporter 5 precursor [Rattus norvegicus].
ACCESSION   NP_001020451 XP_226952
VERSION     NP_001020451.1
DBSOURCE    REFSEQ: accession NM_001025280.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Fernandes,C.F., Godoy,J.R., Doring,B., Cavalcanti,M.C.,
            Bergmann,M., Petzinger,E. and Geyer,J.
  TITLE     The novel putative bile acid transporter SLC10A5 is highly
            expressed in liver and kidney
  JOURNAL   Biochem Biophys Res Commun 361 (1), 26-32 (2007)
   PUBMED   17632081
  REMARK    GeneRIF: Molecular cloning and characterization of SLC10A5 as an
            orphan carrier with yet non-identified substrates.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ074435.1.
            
            On Jul 13, 2005 this sequence version replaced XP_226952.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: DQ074435.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..434
                     /product="sodium/bile acid cotransporter 5 precursor"
                     /note="sodium/bile acid cotransporter 5; Na(+)/bile acid
                     cotransporter 5; solute carrier family 10 (sodium/bile
                     acid cotransporter family), member 5"
                     /calculated_mol_wt=46179
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1915
     mat_peptide     19..434
                     /product="Sodium/bile acid cotransporter 5.
                     /id=PRO_0000263747"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
                     /calculated_mol_wt=46179
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            96
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            130..150
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Region          152..421
                     /region_name="SBF"
                     /note="Sodium Bile acid symporter family; cl19217"
                     /db_xref="CDD:450274"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            233..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            332..352
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4JLT5.1)"
     CDS             1..434
                     /gene="Slc10a5"
                     /coded_by="NM_001025280.1:1..1305"
                     /db_xref="GeneID:310230"
                     /db_xref="RGD:1306036"
ORIGIN      
        1 msgklfiill llvtpgeark sflrflniqn pemlsftkpe etvivrssye gkrphssyll
       61 vkledptvlq vvnvtktsld ftdftinlkt fpgetnltmq lwesegrqtr lieeitnirv
      121 svfrqtedsl fqepihvnss vfllvllmil lnkcafgcki elqvlqtvwk rplpillgav
      181 tqfflmpfcg fllsqilgls kaqafgfvmt ctcpgggggy lfalllegdv tlailmacts
      241 tslalimmpv nsylyscllg lagvfhvpvl kivstllfil tpvsigivik hrmpkkavcl
      301 ervvqplslt lmlvgvylaf rmglvflrma nlevfllgll vpvlgfsfgy sfakvyllpl
      361 pvcktvaies gmlnsflala iiqlsfpqsk ayeasvapft vamcssceml llllvykakk
      421 rpllstenek aplv
//
LOCUS       NP_783177                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7h [Rattus norvegicus].
ACCESSION   NP_783177
VERSION     NP_783177.1
DBSOURCE    REFSEQ: accession NM_175587.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Ferrero,D.M., Wacker,D., Roque,M.A., Baldwin,M.W., Stevens,R.C. and
            Liberles,S.D.
  TITLE     Agonists for 13 trace amine-associated receptors provide insight
            into the molecular basis of odor selectivity
  JOURNAL   ACS Chem Biol 7 (7), 1184-1189 (2012)
   PUBMED   22545963
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380194.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7h"
                     /note="taR-6; taR-7h; trace amine receptor 7h; trace amine
                     receptor 6"
                     /calculated_mol_wt=39943
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y4.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            126..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y4.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y4.1)"
     CDS             1..358
                     /gene="Taar7h"
                     /gene_synonym="Ta6"
                     /coded_by="NM_175587.1:1..1077"
                     /db_xref="GeneID:294130"
                     /db_xref="RGD:631385"
ORIGIN      
        1 matddesfpw dqdsilsrdl lsalspqlcy enlnrscvrs pyspgprlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadllvgltv mpfsmvrsve gcwyfgdsyc
      121 klhtsfdmsf ccssllhlcf isvdryiavs dpliypirft asvsgkcitf swflsiiygf
      181 sliytgasea glkdlvsals cvggcqipmn qscvlinfll flvptlvmmt vyskifliak
      241 qqaqnmekms kqttrasdsy kdrvakrerk aaktlgiava afllswlpyl idsiidaflg
      301 fitpsyvyei lvwivyynsa mnpliyaffy pwfrnaikli vtgkilkqns sttnlfse
//
LOCUS       NP_001032611              73 aa            linear   ROD 02-APR-2025
DEFINITION  beta-defensin 39 precursor [Rattus norvegicus].
ACCESSION   NP_001032611
VERSION     NP_001032611.1
DBSOURCE    REFSEQ: accession NM_001037522.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Patil,A.A., Cai,Y., Sang,Y., Blecha,F. and Zhang,G.
  TITLE     Cross-species analysis of the mammalian beta-defensin gene family:
            presence of syntenic gene clusters and preferential expression in
            the male reproductive tract
  JOURNAL   Physiol Genomics 23 (1), 5-17 (2005)
   PUBMED   16033865
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY621366.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY621366.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..73
                     /product="beta-defensin 39 precursor"
                     /note="BD-39; beta-defensin 39"
                     /calculated_mol_wt=5823
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2503
     mat_peptide     24..73
                     /product="Beta-defensin 39. /id=PRO_0000352715"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32ZF7.1)"
                     /calculated_mol_wt=5823
     Region          25..60
                     /region_name="Defensin_beta"
                     /note="Beta defensin; pfam00711"
                     /db_xref="CDD:459914"
     CDS             1..73
                     /gene="Defb39"
                     /coded_by="NM_001037522.1:70..291"
                     /db_xref="GeneID:641646"
                     /db_xref="RGD:1563816"
ORIGIN      
        1 mkiscflllv lslscfqins vsgidsvkcf qknntchtir cpyfqdevgt cyegrgkccq
       61 krllsirvpk kkv
//
LOCUS       NP_076441                188 aa            linear   ROD 02-APR-2025
DEFINITION  homeobox protein SEBOX [Rattus norvegicus].
ACCESSION   NP_076441
VERSION     NP_076441.1
DBSOURCE    REFSEQ: accession NM_023951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Moreno,D.L., Salazar,Z., Betancourt,M., Casas,E., Ducolomb,Y.,
            Gonzalez,C. and Bonilla,E.
  TITLE     Sebox plays an important role during the early mouse oogenesis in
            vitro
  JOURNAL   Zygote 22 (1), 64-68 (2014)
   PUBMED   22805237
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Kim,K.H., Kim,E.Y. and Lee,K.A.
  TITLE     SEBOX is essential for early embryogenesis at the two-cell stage in
            the mouse
  JOURNAL   Biol Reprod 79 (6), 1192-1201 (2008)
   PUBMED   18753614
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Cinquanta,M., Rovescalli,A.C., Kozak,C.A. and Nirenberg,M.
  TITLE     Mouse Sebox homeobox gene expression in skin, brain, oocytes, and
            two-cell embryos
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8904-8909 (2000)
   PUBMED   10922053
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF284338.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5756307,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q25"
     Protein         1..188
                     /product="homeobox protein SEBOX"
                     /note="homeobox OG-9; skin-, embryo-, brain- and
                     oocyte-specific homeobox; OG9 homeobox"
                     /calculated_mol_wt=20065
     Region          <13..121
                     /region_name="COG5576"
                     /note="Homeodomain-containing transcription factor
                     [Transcription]"
                     /db_xref="CDD:227863"
     Region          19..72
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          80..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERS8.1)"
     CDS             1..188
                     /gene="Sebox"
                     /gene_synonym="Og9x"
                     /coded_by="NM_023951.1:1..567"
                     /db_xref="GeneID:58922"
                     /db_xref="RGD:62077"
ORIGIN      
        1 maspveaspg casglgphrr krttfsvgql lelervfaar pypdistreh laqithlpea
       61 kiqvwfqnrr akrikdrkpg alnarlelpp ncslpdtpql swdpgtpshp lhstssaqqt
      121 sacppqtscl apilgpgqsw sgakaaapwg tsevsgvhsl eqivpqtslg nlsdliytsa
      181 ivtnvdhs
//
LOCUS       NP_001008821             431 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type I cytoskeletal 40 [Rattus norvegicus].
ACCESSION   NP_001008821 XP_220947
VERSION     NP_001008821.1
DBSOURCE    REFSEQ: accession NM_001008821.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004036.1.
            
            On Jan 5, 2005 this sequence version replaced XP_220947.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004036.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..431
                     /product="keratin, type I cytoskeletal 40"
                     /note="K40; CK-40; cytokeratin-40; type I hair keratin
                     KA36; keratin 40, type I"
                     /calculated_mol_wt=48165
     Region          1..89
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Region          88..399
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          90..124
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Region          125..135
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Region          136..236
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Region          237..252
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Region          253..396
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     Site            338
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q6IFW2.1)"
     Region          397..431
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFW2.1)"
     CDS             1..431
                     /gene="Krt40"
                     /gene_synonym="Ka36"
                     /coded_by="NM_001008821.1:1..1296"
                     /db_xref="GeneID:287679"
                     /db_xref="RGD:1359145"
ORIGIN      
        1 masegspdcc ssepyagass cttasfcpts ttylpstcat srcqtpsflc rahlpagcls
       61 pcyltggcns pclvgncawc eegtfnsnek etmqflndrl asylervrsl eennaelecr
      121 ireqcepdat pvcpdyqryf dtieelqqki lctkaensrl avqvdnckla addfrskyes
      181 elslrqlven disglrgilg eltlcksdle ahveslkddl lclkkdheee vnllreqlgd
      241 rlnveldtap tvdlnkvlde mrcqyervla nnrrdaeewf aaqteelnqq qmssaeqlqg
      301 cqtemlelkr tantleielq aqqtltesle ctvaeteaqy stqlaqmqcl idsvehqlae
      361 ircdlerqnq eykvlldtka rleceintyr gllekedsrl pcnpgstasi snsacepcsa
      421 yvictvencc a
//
LOCUS       NP_001100872             900 aa            linear   ROD 02-APR-2025
DEFINITION  desmocollin-3 [Rattus norvegicus].
ACCESSION   NP_001100872 XP_001053804 XP_226122
VERSION     NP_001100872.1
DBSOURCE    REFSEQ: accession NM_001107402.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Xu,X., Dong,C. and Vogel,B.E.
  TITLE     Hemicentins assemble on diverse epithelia in the mouse
  JOURNAL   J Histochem Cytochem 55 (2), 119-126 (2007)
   PUBMED   17015624
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Den,Z., Cheng,X., Merched-Sauvage,M. and Koch,P.J.
  TITLE     Desmocollin 3 is required for pre-implantation development of the
            mouse embryo
  JOURNAL   J Cell Sci 119 (Pt 3), 482-489 (2006)
   PUBMED   16418220
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Cheng,X., Mihindukulasuriya,K., Den,Z., Kowalczyk,A.P.,
            Calkins,C.C., Ishiko,A., Shimizu,A. and Koch,P.J.
  TITLE     Assessment of splice variant-specific functions of desmocollin 1 in
            the skin
  JOURNAL   Mol Cell Biol 24 (1), 154-163 (2004)
   PUBMED   14673151
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Kowalczyk,A.P., Palka,H.L., Luu,H.H., Nilles,L.A., Anderson,J.E.,
            Wheelock,M.J. and Green,K.J.
  TITLE     Posttranslational regulation of plakoglobin expression. Influence
            of the desmosomal cadherins on plakoglobin metabolic stability
  JOURNAL   J Biol Chem 269 (49), 31214-31223 (1994)
   PUBMED   7983064
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473974.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_226122.4, XP_001053804.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760400, SAMEA5760434
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..900
                     /product="desmocollin-3"
                     /calculated_mol_wt=100590
     Region          33..115
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; smart01055"
                     /db_xref="CDD:214999"
     Region          144..238
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          251..355
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(258..259,316,318,351,353..354)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          364..472
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(370..371,428,430,469,471..472)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          480..578
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(487..488,539,541,574,576..577)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          599..674
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Region          851..895
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..900
                     /gene="Dsc3"
                     /coded_by="NM_001107402.1:176..2878"
                     /db_xref="GeneID:307563"
                     /db_xref="RGD:1311782"
ORIGIN      
        1 mamamavpel rslpyrapft kflltlwvfs fvgeackdvt fyvpstlead kiigrvslke
       61 clssadgimp sdpdfrvldd gsvyptravv lsdekrsfti qlsdskmrkq keitvilerq
      121 kevmmkrhtn etvlrrakrr wapipcsmqe nslgpfplfl qqvqsdsaqn ynifysisgr
      181 gvdqeplnlf fierdtgnly ctrpvdreey dvfdliayas tadgysadlp lplpikvede
      241 ndnyplftea iynfevpess rlgtvvgtvc atdkdepdtm htrlkysile qsppspglfs
      301 vhpdtgvitt vshymdrevv dkyklilkvq dmngqffgli ststciitvq dsndnaptfr
      361 qnayetsvee ntynveilri pvddkdmvns anwkanftil kgnengwfki ttdpatnegv
      421 lcvvkpldye enrqvtleig vnneapfird vasriptmnr amvtvqvrdq negpeckpre
      481 qivrikensa igskingyka ydpetknsng lrykklqdpk dwvsieevsg sltiskildr
      541 eimaprndly nitvmaidqe grsctgtlav niedmndnap eiiqddivic kprmgytdis
      601 avdpdepihg ppfqfalass spevnriwtl nqvndtaarl syqktadvqi ysvpvtvtdr
      661 agqsatkilr vnlcdcthps qcllrsrrag itlgkwaila illgiallfs vlltlvcgvv
      721 taqkgkhfpe dlaqqnliis nteapgddrv csangfttht annssqgfcg tmgsgmrngg
      781 qetiemmkgh qtldscrvag hhhtldscrg ghmetdncry tysewhsftq prlgeklhvc
      841 nqnedhipsq dyvltynyeg rgspagsvgc csekqeeegl dflnnlepkf ltlaetctkr
//
LOCUS       NP_001252515             119 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC100359924 precursor [Rattus norvegicus].
ACCESSION   NP_001252515 XP_002727061 XP_002729932
VERSION     NP_001252515.1
DBSOURCE    REFSEQ: accession NM_001265586.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Rajesh,A. and Yenugu,S.
  TITLE     Genomic organization, tissue distribution and functional
            characterization of the rat Pate gene cluster
  JOURNAL   PLoS One 7 (3), e32633 (2012)
   PUBMED   22479333
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            HQ687477.1.
            
            On or before May 21, 2012 this sequence version replaced
            XP_002727061.1, XP_002729932.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ687477.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN09345329 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..119
                     /product="uncharacterized protein LOC100359924 precursor"
                     /note="prostate and testis expressed N; prostate and
                     testis expressed N-like"
                     /calculated_mol_wt=11556
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2609
     Region          23..104
                     /region_name="TFP"
                     /note="three-fingered protein (TFP) fold found in Ly6/uPAR
                     (LU) and snake toxin superfamily; cl45932"
                     /db_xref="CDD:480272"
     CDS             1..119
                     /gene="Pate10"
                     /coded_by="NM_001265586.1:1..360"
                     /db_xref="GeneID:100359924"
                     /db_xref="RGD:2323120"
ORIGIN      
        1 mdwllfllfp gllilyksht mgepsfctsc deyvddtcrr nlgvchpryp dfacqtkevy
       61 iqlntgeyly kysilgcprr cveyvrfikf eknifsccne sycnsfqakh thfkennfv
//
LOCUS       NP_001101616             884 aa            linear   ROD 02-APR-2025
DEFINITION  probable ribonuclease ZC3H12C [Rattus norvegicus].
ACCESSION   NP_001101616 XP_001071727 XP_236237
VERSION     NP_001101616.1
DBSOURCE    REFSEQ: accession NM_001108146.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473975.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001071727.1, XP_236237.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840131
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..884
                     /product="probable ribonuclease ZC3H12C"
                     /calculated_mol_wt=99269
     Region          163..204
                     /region_name="UBA_6"
                     /note="UBA-like domain; pfam18039"
                     /db_xref="CDD:407876"
     Region          249..379
                     /region_name="PIN_Zc3h12-like"
                     /note="PRORP-like PIN domain of ribonuclease Zc3h12a and
                     related proteins; cd18729"
                     /db_xref="CDD:350296"
     Region          416..434
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          836..879
                     /region_name="Regnase_1_C"
                     /note="Endoribonuclease Regnase 1/ ZC3H12 C-terminal
                     domain; pfam18561"
                     /db_xref="CDD:465803"
     CDS             1..884
                     /gene="Zc3h12c"
                     /gene_synonym="RGD1565078"
                     /coded_by="NM_001108146.1:55..2709"
                     /db_xref="GeneID:315658"
                     /db_xref="RGD:1565078"
ORIGIN      
        1 maaektlqey gvlciqeyrk sskvessarn sfmglkdhlg hdlghlymes adpqisaavp
       61 wpmaekptmd tvsagkeekg vseenvssgd seestnsdhe seqlsslsve pclltkthrq
      121 lcrspcleph llkhsdvlqd fkpeesqtps kevkkppdvv reyqtklefa lklgyseeqv
      181 qlvlnklgtd alindilgel vklgnksead qtvstvnsam retsslesqr sespmpeivt
      241 ddgenlrpvv idgsnvamsh gnkevfscrg iklavdwfle rghkditvfv pawrkeqsrp
      301 dalitdqeil rklekekilv ftpsrrvqgr rvvcyddrfi vklafesdgi ivsndnyrdl
      361 anekpewkkf iderllmysf vndkfmppdd plgrhgpsld nflrkkpivp ehkkqpcpyg
      421 kkctyghkck yyhpergsqp qrsvadelra msrntaaktt negglvksns vpcstkadst
      481 sdvkrgapkr qsdpsirthv yqdieeklpt knkletrsvp slvsipatst akpqsttsls
      541 nglpsgvhfp pqdqrpqgqy ppmmmatknh gapmpyeqyp kcespvdvgy ysmlnaysnl
      601 sisgprsper rfsldtdyrv nsvasdcsse gsmscgssds yvgysdrsyv sspdpqleen
      661 lkgqhmhphs rlnsqpflqs fhdpltrvqs ysheepkfhh krplphlamh lqhpavgars
      721 scpgdypspp ssahskashl grslvatrid sisdsrlyds spsrqrkpys rqeglgswdr
      781 psygmdaygy rqtyslpdns tppcyesitf qslpeqqept wripycgmph dppryqdsre
      841 kiyinlcnif ppdlvrlvmk rnphmtdaqq laaailveks qlgy
//
LOCUS       NP_001103097             371 aa            linear   ROD 02-APR-2025
DEFINITION  elongin BC and Polycomb repressive complex 2-associated protein
            [Rattus norvegicus].
ACCESSION   NP_001103097 XP_001077023
VERSION     NP_001103097.1
DBSOURCE    REFSEQ: accession NM_001109627.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Liefke,R., Karwacki-Neisius,V. and Shi,Y.
  TITLE     EPOP Interacts with Elongin BC and USP7 to Modulate the Chromatin
            Landscape
  JOURNAL   Mol Cell 64 (4), 659-672 (2016)
   PUBMED   27863226
  REMARK    Erratum:[Mol Cell. 2017 Jan 5;65(1):202. doi:
            10.1016/j.molcel.2016.12.006. PMID: 28061330]
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Beringer,M., Pisano,P., Di Carlo,V., Blanco,E., Chammas,P.,
            Vizan,P., Gutierrez,A., Aranda,S., Payer,B., Wierer,M. and Di
            Croce,L.
  TITLE     EPOP Functionally Links Elongin and Polycomb in Pluripotent Stem
            Cells
  JOURNAL   Mol Cell 64 (4), 645-658 (2016)
   PUBMED   27863225
REFERENCE   3  (residues 1 to 371)
  AUTHORS   De Cegli,R., Iacobacci,S., Flore,G., Gambardella,G., Mao,L.,
            Cutillo,L., Lauria,M., Klose,J., Illingworth,E., Banfi,S. and di
            Bernardo,D.
  TITLE     Reverse engineering a mouse embryonic stem cell-specific
            transcriptional network reveals a new modulator of neuronal
            differentiation
  JOURNAL   Nucleic Acids Res 41 (2), 711-726 (2013)
   PUBMED   23180766
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001077023.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..371
                     /product="elongin BC and Polycomb repressive complex
                     2-associated protein"
                     /note="uncharacterized protein C17orf96 homolog"
                     /calculated_mol_wt=38682
     Region          <46..237
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <297..362
                     /region_name="EPOP"
                     /note="Elongin BC and Polycomb repressive complex
                     2-associated protein; pfam15223"
                     /db_xref="CDD:434546"
     CDS             1..371
                     /gene="Epop"
                     /coded_by="NM_001109627.1:406..1521"
                     /db_xref="GeneID:691153"
                     /db_xref="RGD:1587434"
ORIGIN      
        1 metlcppprl avpasprgsp csptprkprr gtpefsplcl ralafcalak prpsslglgp
       61 gelaprtpvl lgsraspctg gwaadglkhl gaqagrpsdv ssatredadv avcpdrgeee
      121 eggggfphfg sgsctppgrc pagprespts parspprpar glesqldaas spplgsssrp
      181 psppaglspe papteqpmrd seapeggdpa rvapeapals pstadatpda pgdlrqehfn
      241 rlirrsklwc yakgfaldtp slrrgperpa akargaakkr rrpappprsv qprrpaptlp
      301 tsstfhlldc fpcppalvve engdlgpass lrlqgdakpp pahplwkwqm ggpavpeppg
      361 lkswwvnlee l
//
LOCUS       NP_001157079            1691 aa            linear   ROD 02-APR-2025
DEFINITION  serine/threonine-protein kinase WNK3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001157079
VERSION     NP_001157079.1
DBSOURCE    REFSEQ: accession NM_001163607.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1691)
  AUTHORS   Zhu,J., Lin,X., Chen,C., Tan,H., Gao,Y., Li,D. and Chen,G.
  TITLE     WNK3 Promotes Neuronal Survival after Traumatic Brain Injury in
            Rats
  JOURNAL   Neuroscience 477, 76-88 (2021)
   PUBMED   34626749
  REMARK    GeneRIF: WNK3 Promotes Neuronal Survival after Traumatic Brain
            Injury in Rats.
REFERENCE   2  (residues 1 to 1691)
  AUTHORS   Wu,D., Lai,N., Deng,R., Liang,T., Pan,P., Yuan,G., Li,X., Li,H.,
            Shen,H., Wang,Z. and Chen,G.
  TITLE     Activated WNK3 induced by intracerebral hemorrhage deteriorates
            brain injury maybe via WNK3/SPAK/NKCC1 pathway
  JOURNAL   Exp Neurol 332, 113386 (2020)
   PUBMED   32589890
  REMARK    GeneRIF: Activated WNK3 induced by intracerebral hemorrhage
            deteriorates brain injury maybe via WNK3/SPAK/NKCC1 pathway.
REFERENCE   3  (residues 1 to 1691)
  AUTHORS   Zhang,J., Gao,G., Begum,G., Wang,J., Khanna,A.R., Shmukler,B.E.,
            Daubner,G.M., de Los Heros,P., Davies,P., Varghese,J.,
            Bhuiyan,M.I., Duan,J., Zhang,J., Duran,D., Alper,S.L., Sun,D.,
            Elledge,S.J., Alessi,D.R. and Kahle,K.T.
  TITLE     Functional kinomics establishes a critical node of volume-sensitive
            cation-Cl- cotransporter regulation in the mammalian brain
  JOURNAL   Sci Rep 6, 35986 (2016)
   PUBMED   27782176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1691)
  AUTHORS   Zhang,Z., Xu,X., Xiang,Z., Yu,Z., Feng,J. and He,C.
  TITLE     LINGO-1 receptor promotes neuronal apoptosis by inhibiting WNK3
            kinase activity
  JOURNAL   J Biol Chem 288 (17), 12152-12160 (2013)
   PUBMED   23482566
  REMARK    GeneRIF: LINGO-1 potentiates neuronal apoptosis, likely by
            inhibiting WNK3 kinase activity.
REFERENCE   5  (residues 1 to 1691)
  AUTHORS   Cruz-Rangel,S., Melo,Z., Vazquez,N., Meade,P., Bobadilla,N.A.,
            Pasantes-Morales,H., Gamba,G. and Mercado,A.
  TITLE     Similar effects of all WNK3 variants on SLC12 cotransporters
  JOURNAL   Am J Physiol Cell Physiol 301 (3), C601-C608 (2011)
   PUBMED   21613606
REFERENCE   6  (residues 1 to 1691)
  AUTHORS   Yang,C.L., Zhu,X. and Ellison,D.H.
  TITLE     The thiazide-sensitive Na-Cl cotransporter is regulated by a WNK
            kinase signaling complex
  JOURNAL   J Clin Invest 117 (11), 3403-3411 (2007)
   PUBMED   17975670
REFERENCE   7  (residues 1 to 1691)
  AUTHORS   Dorwart,M.R., Shcheynikov,N., Wang,Y., Stippec,S. and Muallem,S.
  TITLE     SLC26A9 is a Cl(-) channel regulated by the WNK kinases
  JOURNAL   J Physiol 584 (Pt 1), 333-345 (2007)
   PUBMED   17673510
REFERENCE   8  (residues 1 to 1691)
  AUTHORS   Verissimo,F., Silva,E., Morris,J.D., Pepperkok,R. and Jordan,P.
  TITLE     Protein kinase WNK3 increases cell survival in a
            caspase-3-dependent pathway
  JOURNAL   Oncogene 25 (30), 4172-4182 (2006)
   PUBMED   16501604
REFERENCE   9  (residues 1 to 1691)
  AUTHORS   Rinehart,J., Kahle,K.T., de Los Heros,P., Vazquez,N., Meade,P.,
            Wilson,F.H., Hebert,S.C., Gimenez,I., Gamba,G. and Lifton,R.P.
  TITLE     WNK3 kinase is a positive regulator of NKCC2 and NCC, renal
            cation-Cl- cotransporters required for normal blood pressure
            homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 102 (46), 16777-16782 (2005)
   PUBMED   16275913
REFERENCE   10 (residues 1 to 1691)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474063.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1691
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..1691
                     /product="serine/threonine-protein kinase WNK3 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase WNK3"
                     /calculated_mol_wt=185653
     Region          135..409
                     /region_name="STKc_WNK3"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 3; cd14031"
                     /db_xref="CDD:270933"
     Site            order(152..156,158,160,173,175,206,226..229,233,235,274,
                     276,278..279,281,293,296,310..313)
                     /site_type="active"
                     /db_xref="CDD:270933"
     Site            order(152..156,160,173,175,206,226..229,233,274,276,
                     278..279,281,293)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270933"
     Site            order(156,233,235,274,276,278,296,310..313)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270933"
     Site            292..313
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270933"
     Region          425..488
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     CDS             1..1691
                     /gene="Wnk3"
                     /gene_synonym="RGD1563131"
                     /coded_by="NM_001163607.1:1..5076"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:317420"
                     /db_xref="RGD:1563131"
ORIGIN      
        1 matdsgepas tedsekpdgv sfqsrvarav apltvearik ekystfsasg etierkrffr
       61 ksvemteddk vaqssrrder kvatnisrve kvptnvlrgg qevkyeqcsk atsesskdcf
      121 kektekemee eaemkavats psgrflkfdi elgrgafktv ykgldtetwv evawcelqdr
      181 kltkaeqqrf keeaemlkgl qhpnivrfyd swesilkgkk civlvtelmt sgtlktylkr
      241 fkvmkpkvlr swcrqilkgl qflhtrtppi ihrdlkcdni fitgptgsvk igdlglatlm
      301 rtsfaksvig tpefmapemy eehydesvdv yafgmcmlem atseypysec qnaaqiyrkv
      361 tsgikpasfn kvtdpevkei iegcirqnks erlsikdlln haffaedtgl rvelaeeddc
      421 snsslalrlw vedpkklkgk hkdneaiefs fnleadtpee vayemvksgf fhesdskava
      481 ksirdrvtli kkirekkpag cleerrdsqc kharnvnpqq qtatlrpapg phnaaeceet
      541 evdqhvrqql vqgkaqqqps svrgdtssep aagpvlhsdt sshptvayss nqatssqeqp
      601 kltrspvlpv vqgqssvmpi yaagpavasq sqispltiqk vsqikpvsqp igaeqqatpp
      661 npdfvrslnq dvtsvkentn spdtpsgngk qdrikqrras cprpekgtkf qltvlqvsvs
      721 gdnmvecqle thnnkmvtfk fdvdgdaped iadymtgsse qvlinsastq tsnesapqss
      781 pvgrwrfcin qtiknreaqs ppslqpsvam vpglhpfpnn tsnqeisqdt lftvpghhvv
      841 ftskldgkig erasveteqt svpyqaeddk lkapatdtsn ysatlvcpdp agcealtsqa
      901 gmfiptypcq qaavpadvlm shpgesvqig snavvtsvlv ssdqkpqsls vqqptidaef
      961 isqegettvn setsspkavg atqtpgfept vllpatiles dgerppkmef tdnriktlde
     1021 klrnllyqeh sisticpesq kdtqsidspf sssaedilss pmpeviaish cgiqdsqaqs
     1081 pnfqptgski lsnvaasqpa hipvlkrdln vitsvpselc lhemspdasl pgdpeaypaa
     1141 vssdgtihlq tgggyfglsf tcpslknpis rkswtrklks wayrlrqsts ffkrskvrqv
     1201 etedkrsaia sdpipltref sadtralsrc kamsgsfqrg rfqvitvpqq qpvkmmsfgk
     1261 ehrppskktt aqsneqaltf teaavtqlie vepaipthka svssqklrtl yetfkedkgd
     1321 peqgdilsls taretsvssv tteknveets ttgisvqsgs emldkekdes tpgkqtctne
     1381 fsatpagsgk svakaapksg qhlparaqtq sslfyspssp mssdneseie dedlkaelqr
     1441 lrekhiqevv slqtqqnkel qelyerlrat kdskaqssev pmppasprrp rsfksklrsr
     1501 pqslthsdnl vvvkdvqrae sntaprqqsp askkgmftdd lhklvddwtr etvgnfpskp
     1561 slnqlkqsqq kseaenwnkl hestpstvgy tstwisslsq irgaapsslp hglplpsfpg
     1621 plasygmpha cqynpvgaas ypvqwvgisg aaqqsvvlpt qsgglfqpgm nlqsfpappv
     1681 qnppsippgp k
//
LOCUS       NP_001100821             337 aa            linear   ROD 02-APR-2025
DEFINITION  serine (or cysteine) peptidase inhibitor, clade B, member 9d
            [Rattus norvegicus].
ACCESSION   NP_001100821 XP_001066335 XP_225267
VERSION     NP_001100821.1
DBSOURCE    REFSEQ: accession NM_001107351.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473977.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225267.4, XP_001066335.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..337
                     /product="serine (or cysteine) peptidase inhibitor, clade
                     B, member 9d"
                     /note="serine (or cysteine) proteinase inhibitor, clade B,
                     member 9e"
                     /calculated_mol_wt=38627
     Region          1..334
                     /region_name="serpin"
                     /note="SERine Proteinase INhibitors (serpin) family;
                     cl38926"
                     /db_xref="CDD:476815"
     Site            order(288..298,315)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381000"
     CDS             1..337
                     /gene="Serpinb9d"
                     /gene_synonym="Serpinb9e"
                     /coded_by="NM_001107351.1:70..1083"
                     /db_xref="GeneID:306890"
                     /db_xref="RGD:1308725"
ORIGIN      
        1 mvllgakgdt avqisqalnl nkhpdedihk dfqlllhnln kpkshyclri anrlfaentc
       61 klvptykesc lrfynseieq lsfakaaees rkhintwvsk qtegkipell ssdsvgsetk
      121 limvnalyfq gswlhcfdke ftmempfkin kketkpvqmm wqeetfdvay vkeiqaqilv
      181 mpyrgmemsf mvllpdegvd irkvessltf ekltawtkpe fiystevyvy lpkfqlqeqy
      241 dmtalfqhlg midvfseika dlsgmcpekd lcvskfvhec vvevneegte aaaasaadcc
      301 yscseytptf cadrpflffi rhnqtnsilf cgrfssp
//
LOCUS       NP_001041320             321 aa            linear   ROD 02-APR-2025
DEFINITION  E3 ubiquitin-protein ligase DTX4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001041320 XP_001076321 XP_238163
VERSION     NP_001041320.1
DBSOURCE    REFSEQ: accession NM_001047855.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY383692.1.
            
            On or before Sep 8, 2006 this sequence version replaced
            XP_238163.4, XP_001076321.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY383692.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..321
                     /product="E3 ubiquitin-protein ligase DTX4 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="deltex 4 homolog; protein deltex-4; deltex homolog
                     4; E3 ubiquitin-protein ligase DTX4; deltex 4, E3
                     ubiquitin ligase"
                     /calculated_mol_wt=34954
     Region          108..174
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(111,114,142,144,147,150,166,169)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          177..311
                     /region_name="DTC"
                     /note="Deltex C-terminal domain; pfam18102"
                     /db_xref="CDD:465650"
     Site            order(186..190,192,204,206,208..210,231..233,235,269,
                     282..283,291)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:193607"
     CDS             1..321
                     /gene="Dtx4"
                     /gene_synonym="LRRGT00037"
                     /coded_by="NM_001047855.1:1..966"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:293774"
                     /db_xref="RGD:1311767"
ORIGIN      
        1 mmmmvmmmmv vvvwvptvpv knlngsspvn palagitgil msaaglpvcl trppklvlhp
       61 ppvskseiks ipgvsntsrk ttkkqakkgk tpeevlkkyl qkvrhppeed cticmerlta
      121 psgykgpqpt vkpdlvgkls kcghiyhiyc lvamynngnk dgslqcptck tiygvktgtq
      181 ppgkmeyhli phslpghpdc ktiriiysip pgiqgpehpn pgksfsargf prhcylpdse
      241 kgrkvlklll vawdrrlifa igtssttges dtviwnevhh ktefgsnltg hgypdanyld
      301 nvlaelaaqg isedstsqek d
//
LOCUS       NP_001103079             589 aa            linear   ROD 02-APR-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 3 precursor [Rattus norvegicus].
ACCESSION   NP_001103079 XP_001075512
VERSION     NP_001103079.1
DBSOURCE    REFSEQ: accession NM_001109609.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474029.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001075512.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB577790.1, FQ087862.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..589
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 3
                     precursor"
                     /note="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 3"
                     /calculated_mol_wt=62293
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2503
     Region          23..55
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          34..53
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          55..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <56..>349
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          79..102
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          103..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          199..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          223..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          247..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..292
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          295..316
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          319..342
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          331..>405
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          407..489
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          424..428
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          437..441
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          462..466
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          476..481
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..589
                     /gene="Lingo3"
                     /coded_by="NM_001109609.1:144..1913"
                     /db_xref="GeneID:690755"
                     /db_xref="RGD:1592209"
ORIGIN      
        1 mtcwlhmlgl hllllptapl atgcparcec sastrtvacg rrrltavpeg ipaetrmlel
       61 srnrirclnp gdlaslptle eldlnhnvia hvepgafanl prlrvlrlrg nqlklippgv
      121 fthldsltll dlsenklvil ldfsfqdlrs lqrlevgdnd lvfisrrafa gllglaeltl
      181 ercnltslsp eslghlrglg alrlrhlaia aledqnfqkl pgllhleidn wplleevapg
      241 slrglnltsl sithtnitav paaalrqqah ltclnlshnp ismvprgsfr dlvrlrelhl
      301 agallaviep qafvglrqir llnlsdnlls tleentfhsv ntletlrvdg nplacdcrll
      361 wivqrrktln fdgrlpacat paevrgdalh nlpdsvlfey fvcrkpkire rrlqhvtate
      421 gddvrflcra egepaptvaw vtpqhhsvta asrgrarvlp ggtlaitdtr pqdsgtytcv
      481 asnaggndty fatltihpaa nrtqsdghne tqvgvrfpld lttilvstam gcitflgvvl
      541 fcflllfvws rgrgqhknnf sveysfrkvd gpaaaagqgg arkfnmkmi
//
LOCUS       NP_001012231             153 aa            linear   ROD 02-APR-2025
DEFINITION  probable inactive ribonuclease-like protein 13 precursor [Rattus
            norvegicus].
ACCESSION   NP_001012231 XP_573761
VERSION     NP_001012231.1
DBSOURCE    REFSEQ: accession NM_001012231.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Cho,S., Beintema,J.J. and Zhang,J.
  TITLE     The ribonuclease A superfamily of mammals and birds: identifying
            new members and tracing evolutionary histories
  JOURNAL   Genomics 85 (2), 208-220 (2005)
   PUBMED   15676279
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY665836.1.
            
            On Apr 20, 2005 this sequence version replaced XP_573761.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..153
                     /product="probable inactive ribonuclease-like protein 13
                     precursor"
                     /note="ribonuclease-like protein 13; ribonuclease 13;
                     probable inactive ribonuclease-like protein 13;
                     ribonuclease, RNase A family, 13 (non-active)"
                     /calculated_mol_wt=15223
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5GAL7.1)"
                     /calculated_mol_wt=2241
     mat_peptide     23..153
                     /product="Probable inactive ribonuclease-like protein 13.
                     /id=PRO_0000308707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GAL7.1)"
                     /calculated_mol_wt=15223
     Region          27..145
                     /region_name="RnaseA"
                     /note="Pancreatic ribonuclease; pfam00074"
                     /db_xref="CDD:459661"
     Site            order(70,102,113,128,130,132..133,135)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119386"
     CDS             1..153
                     /gene="Rnase13"
                     /coded_by="NM_001012231.1:1..462"
                     /db_xref="GeneID:497194"
                     /db_xref="RGD:1359386"
ORIGIN      
        1 masdaasllv lqlvlqptlv tgitiqtaik nfrilhvdyp mvnypkgfhg ycnglmayvr
       61 gklqdwycpk ihyvvhapfe siqkfckyse sfcedyneyc tltqnsfpit vctldhkqap
      121 tscsynstlt nqrlyllcsr khdaepigvi gly
//
LOCUS       NP_001160153             302 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 104 [Rattus norvegicus].
ACCESSION   NP_001160153
VERSION     NP_001160153.1
DBSOURCE    REFSEQ: accession NM_001166681.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362741.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..302
                     /product="taste receptor type 2 member 104"
                     /note="T2R21; T2R104; taste receptor type 2 member 21"
                     /calculated_mol_wt=34972
     Region          7..291
                     /region_name="7tm_TAS2R10"
                     /note="mammalian taste receptor 2, subtype 10, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15021"
                     /db_xref="CDD:320149"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320149"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320149"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320149"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Region          131..147
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320149"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES9.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES9.1)"
     Region          173..196
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320149"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Region          221..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320149"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320149"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES9.1)"
     CDS             1..302
                     /gene="Tas2r104"
                     /coded_by="NM_001166681.1:1..909"
                     /db_xref="GeneID:100310879"
                     /db_xref="RGD:2314259"
ORIGIN      
        1 mlsmlesill svatseamlg ilgnifivlv nctnwvrnkk lskinfiltg laisrvftiw
       61 iitldaytkv fflttlmpsn lhecisyiwv iinhlsvwfa tslsifyflk ianfshyifl
      121 wlkrradkvf vfligyliit wlasfplavt viknikvhhn ntswliqlek rellinyvfa
      181 nmgpislfmv avftcfllti slwrhrrrmq stgskfrdln tevhvkamkv lisfiilfil
      241 yfmgvlietl clfltenill fifgftlsst ypcchsfili ltsrelkqas mralqrlkcc
      301 et
//
LOCUS       NP_001102960             180 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC686031 [Rattus norvegicus].
ACCESSION   NP_001102960 XP_001066250
VERSION     NP_001102960.1
DBSOURCE    REFSEQ: accession NM_001109490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH474014.2.
            
            On Oct 4, 2007 this sequence version replaced XP_001066250.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..180
                     /product="uncharacterized protein LOC686031"
                     /calculated_mol_wt=20338
     Region          3..180
                     /region_name="FANCD2OS"
                     /note="FANCD2 opposite strand protein; pfam15124"
                     /db_xref="CDD:434479"
     CDS             1..180
                     /gene="Fancd2osl1"
                     /coded_by="NM_001109490.1:1..543"
                     /db_xref="GeneID:686031"
                     /db_xref="RGD:1586665"
ORIGIN      
        1 magyqlwspw spldeslqwl rhttptfask hpfrfspffp qspcdvevqq cfhevavvsv
       61 mprmiaarss elpghplepq kgtaakktpt irkpqpirll gvdsvfgrvi tvqppkwtgt
      121 fkisktsafs kiiskeqqwp tglkepqiem tlamckqmlr silllyaiyk kctfalqhsq
//
LOCUS       NP_001020096             373 aa            linear   ROD 02-APR-2025
DEFINITION  probable G-protein coupled receptor 34 [Rattus norvegicus].
ACCESSION   NP_001020096
VERSION     NP_001020096.1
DBSOURCE    REFSEQ: accession NM_001024925.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Kitamura,H., Makide,K., Shuto,A., Ikubo,M., Inoue,A., Suzuki,K.,
            Sato,Y., Nakamura,S., Otani,Y., Ohwada,T. and Aoki,J.
  TITLE     GPR34 is a receptor for lysophosphatidylserine with a fatty acid at
            the sn-2 position
  JOURNAL   J Biochem 151 (5), 511-518 (2012)
   PUBMED   22343749
  REMARK    GeneRIF: The present studies confirm that GPR34 is a cellular
            receptor for LysoPS, especially with a fatty acid at the sn-2
            position.
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Sugo,T., Tachimoto,H., Chikatsu,T., Murakami,Y., Kikukawa,Y.,
            Sato,S., Kikuchi,K., Nagi,T., Harada,M., Ogi,K., Ebisawa,M. and
            Mori,M.
  TITLE     Identification of a lysophosphatidylserine receptor on mast cells
  JOURNAL   Biochem Biophys Res Commun 341 (4), 1078-1087 (2006)
   PUBMED   16460680
  REMARK    GeneRIF: results suggest that GPR34 is the functional mast cell
            lysophosphatidylserine receptor
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Leonoudakis,D., Conti,L.R., Radeke,C.M., McGuire,L.M. and
            Vandenberg,C.A.
  TITLE     A multiprotein trafficking complex composed of SAP97, CASK, Veli,
            and Mint1 is associated with inward rectifier Kir2 potassium
            channels
  JOURNAL   J Biol Chem 279 (18), 19051-19063 (2004)
   PUBMED   14960569
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Schulz,A. and Schoneberg,T.
  TITLE     The structural evolution of a P2Y-like G-protein-coupled receptor
  JOURNAL   J Biol Chem 278 (37), 35531-35541 (2003)
   PUBMED   12835326
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Schuh,K., Uldrijan,S., Gambaryan,S., Roethlein,N. and Neyses,L.
  TITLE     Interaction of the plasma membrane Ca2+ pump 4b/CI with the
            Ca2+/calmodulin-dependent membrane-associated kinase CASK
  JOURNAL   J Biol Chem 278 (11), 9778-9783 (2003)
   PUBMED   12511555
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB159443.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB159443.1, FM092260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663598, SAMN13663601
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..373
                     /product="probable G-protein coupled receptor 34"
                     /calculated_mol_wt=42712
     Region          47..330
                     /region_name="7tmA_GPR34-like"
                     /note="putative G protein-coupled receptor 34, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15148"
                     /db_xref="CDD:320276"
     Region          47..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320276"
     Region          81..106
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320276"
     Site            order(102,105..106,119..124,126..127,130,175,177..181,207,
                     210..212,214..216,218..219,271,274..275,277..278,281,
                     297..298,300..302,305,308..309)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320276"
     Region          119..149
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320276"
     Region          161..183
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320276"
     Region          207..236
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320276"
     Region          251..281
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320276"
     Region          298..323
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320276"
     CDS             1..373
                     /gene="Gpr34"
                     /coded_by="NM_001024925.2:178..1299"
                     /db_xref="GeneID:554353"
                     /db_xref="RGD:1563681"
ORIGIN      
        1 mtttvdswlc sspgmhfitn dsdqvsqnfs gvsnvtscpm dekllstvlt tfysvifivg
       61 lvgniialyv flgihrkrns iqiyllnvav adlllifclp frimyhinqn rwtlgvilck
      121 vvgtlfymnm yisiillgfi sldryikinr siqqrraitt kqsvyvccvv wtvalagflt
      181 miiltlkkgg hnstmcfhyr dkhnakgeai fnfalvvmfw liflliilsy ikigknllri
      241 skrrskfpns gkyattarns fivliiftic fvpyhafrfi yissqlnass cywkeiihkt
      301 neimlvlssf nscldpvmyf lmssnirkim cqllfrrfqs dtsrsestse fkpgyslhdl
      361 svtvkmqyst kgn
//
LOCUS       NP_071518                194 aa            linear   ROD 02-APR-2025
DEFINITION  fibroblast growth factor 7 precursor [Rattus norvegicus].
ACCESSION   NP_071518 XP_346673
VERSION     NP_071518.1
DBSOURCE    REFSEQ: accession NM_022182.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Wang,X., Gao,Y. and Sun,X.
  TITLE     Effect of Taspine hydrochloride on the repair of rat skin wounds by
            regulating keratinocyte growth factor signal
  JOURNAL   Bioengineered 13 (1), 789-799 (2022)
   PUBMED   34898359
  REMARK    GeneRIF: Effect of Taspine hydrochloride on the repair of rat skin
            wounds by regulating keratinocyte growth factor signal.
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Zhou,L., Zhang,S., Zhang,L., Li,F., Sun,H. and Feng,J.
  TITLE     MiR-199a-3p inhibits the proliferation, migration, and invasion of
            endothelial cells and retinal pericytes of diabetic retinopathy
            rats through regulating FGF7 via EGFR/PI3K/AKT pathway
  JOURNAL   J Recept Signal Transduct Res 41 (1), 19-31 (2021)
   PUBMED   32586178
  REMARK    GeneRIF: MiR-199a-3p inhibits the proliferation, migration, and
            invasion of endothelial cells and retinal pericytes of diabetic
            retinopathy rats through regulating FGF7 via EGFR/PI3K/AKT pathway.
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Zhang,C., Han,M. and Wu,S.
  TITLE     Silencing fibroblast growth factor 7 inhibits krypton laser-induced
            choroidal neovascularization in a rat model
  JOURNAL   J Cell Biochem 120 (8), 13792-13801 (2019)
   PUBMED   31017714
  REMARK    GeneRIF: Silencing fibroblast growth factor 7 inhibits krypton
            laser-induced choroidal neovascularization in a rat model.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Peng,Y., Wu,S., Tang,Q., Li,S. and Peng,C.
  TITLE     KGF-1 accelerates wound contraction through the TGF-beta1/Smad
            signaling pathway in a double-paracrine manner
  JOURNAL   J Biol Chem 294 (21), 8361-8370 (2019)
   PUBMED   30894415
  REMARK    GeneRIF: findings demonstrate that KGF-1 promotes fibroblast
            contraction and accelerates wound contraction via the
            TGF-beta1/Smad signaling pathway in a double-paracrine manner.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Zhou,C., Chen,Y., Kang,W., Lv,H., Fang,Z., Yan,F., Li,L., Zhang,W.
            and Shi,J.
  TITLE     Mir-455-3p-1 represses FGF7 expression to inhibit pulmonary
            arterial hypertension through inhibiting the RAS/ERK signaling
            pathway
  JOURNAL   J Mol Cell Cardiol 130, 23-35 (2019)
   PUBMED   30858037
  REMARK    GeneRIF: findings illustrate a role for miR-455-3p-1 in modulating
            FGF7-RAS/ERK signaling and suggest that an agomir of miR-455-3p-1
            could inhibit the proliferation of PASMCs and mitigate PAH in vivo.
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Siegfried,S., Pekonen,F., Nyman,T., Ammala,M. and Rutanen,E.M.
  TITLE     Distinct patterns of expression of keratinocyte growth factor and
            its receptor in endometrial carcinoma
  JOURNAL   Cancer 79 (6), 1166-1171 (1997)
   PUBMED   9070494
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Kitsberg,D.I. and Leder,P.
  TITLE     Keratinocyte growth factor induces mammary and prostatic
            hyperplasia and mammary adenocarcinoma in transgenic mice
  JOURNAL   Oncogene 13 (12), 2507-2515 (1996)
   PUBMED   9000125
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Ornitz,D.M., Xu,J., Colvin,J.S., McEwen,D.G., MacArthur,C.A.,
            Coulier,F., Gao,G. and Goldfarb,M.
  TITLE     Receptor specificity of the fibroblast growth factor family
  JOURNAL   J Biol Chem 271 (25), 15292-15297 (1996)
   PUBMED   8663044
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Yan,G., Fukabori,Y., Nikolaropoulos,S., Wang,F. and McKeehan,W.L.
  TITLE     Heparin-binding keratinocyte growth factor is a candidate
            stromal-to-epithelial-cell andromedin
  JOURNAL   Mol Endocrinol 6 (12), 2123-2128 (1992)
   PUBMED   1491693
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Yan,G.C., Nikolaropoulos,S., Wang,F. and McKeehan,W.L.
  TITLE     Sequence of rat keratinocyte growth factor (heparin-binding growth
            factor type 7)
  JOURNAL   In Vitro Cell Dev Biol 27A (6), 437-438 (1991)
   PUBMED   1869483
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X56551.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346673.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X56551.1, AF295300.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..194
                     /product="fibroblast growth factor 7 precursor"
                     /note="FGF-7; HBGF-7; heparin-binding growth factor 7;
                     Keratinocyte Growth Factor Fgf-7; fibroblast growth factor
                     5b"
                     /calculated_mol_wt=18673
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3613
     mat_peptide     32..194
                     /product="Fibroblast growth factor 7. /id=PRO_0000008968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02195.1)"
                     /calculated_mol_wt=18673
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02195.1)"
     Region          57..192
                     /region_name="beta-trefoil_FGF7"
                     /note="FGF domain, beta-trefoil fold, found in fibroblast
                     growth factor 7 (FGF7) and similar proteins; cd23319"
                     /db_xref="CDD:467005"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02195.1)"
     CDS             1..194
                     /gene="Fgf7"
                     /gene_synonym="Fgf5b; Kgf; KGF/FGF7"
                     /coded_by="NM_022182.1:109..693"
                     /db_xref="GeneID:29348"
                     /db_xref="RGD:61805"
ORIGIN      
        1 mrkwiltril ptplyrpcfh lvclvgtisl acndmspeqt atsvncsspe rhtrsydyme
       61 ggdirvrrlf crtqwylrid krgkvkgtqe mrnsynimei mtvavgivai kgveseyyla
      121 mnkqgelyak kecnedcnfk elilenhynt sasakwthsg gemfvalnqk glpvkgkktk
      181 keqktahflp mait
//
LOCUS       NP_001160161             309 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 113 [Rattus norvegicus].
ACCESSION   NP_001160161
VERSION     NP_001160161.1
DBSOURCE    REFSEQ: accession NM_001166689.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362749.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..309
                     /product="taste receptor type 2 member 113"
                     /note="taste receptor type 2 member 30; T2R113"
                     /calculated_mol_wt=35890
     Region          8..297
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          176..199
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          224..249
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     Region          261..286
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES1.1)"
     CDS             1..309
                     /gene="Tas2r113"
                     /gene_synonym="T2R30"
                     /coded_by="NM_001166689.1:1..930"
                     /db_xref="GeneID:100310885"
                     /db_xref="RGD:2314255"
ORIGIN      
        1 mvavlqstfa iifsmefivg tlgngfiilm tcidwvrrrk islvdqilta laitritlil
       61 lvfidwwvsv lfpalhetgk ilrmyfiswt vinhcnlwlt aslsiiyflk iasfssiifl
      121 ylkfrvknvv fvtllvslff lfintaivnv yfdvcfdgvq rnvsqvsrly nheqickfls
      181 ftnpmfafip fvtsmatffl lifslwrhlk nmkhnaegcr dvstivhira lqtiivsvvl
      241 ystfflsffv kvwssgsper yliflfvwal gnavlpahtf vliwgncrlr waslslmlwl
      301 ryrfknidv
//
LOCUS       NP_001102612             237 aa            linear   ROD 02-APR-2025
DEFINITION  regulator of G-protein signaling 9-binding protein [Rattus
            norvegicus].
ACCESSION   NP_001102612 XP_001079782 XP_574424
VERSION     NP_001102612.1
DBSOURCE    REFSEQ: accession NM_001109142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Tian,M., Zallocchi,M., Wang,W., Chen,C.K., Palczewski,K.,
            Delimont,D., Cosgrove,D. and Peng,Y.W.
  TITLE     Light-induced translocation of RGS9-1 and Gbeta5L in mouse rod
            photoreceptors
  JOURNAL   PLoS One 8 (3), e58832 (2013)
   PUBMED   23555598
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Arshavsky,V.Y. and Burns,M.E.
  TITLE     Photoreceptor signaling: supporting vision across a wide range of
            light intensities
  JOURNAL   J Biol Chem 287 (3), 1620-1626 (2012)
   PUBMED   22074925
  REMARK    Review article
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Keresztes,G., Martemyanov,K.A., Krispel,C.M., Mutai,H., Yoo,P.J.,
            Maison,S.F., Burns,M.E., Arshavsky,V.Y. and Heller,S.
  TITLE     Absence of the RGS9.Gbeta5 GTPase-activating complex in
            photoreceptors of the R9AP knockout mouse
  JOURNAL   J Biol Chem 279 (3), 1581-1584 (2004)
   PUBMED   14625292
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_574424.1, XP_001079782.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..237
                     /product="regulator of G-protein signaling 9-binding
                     protein"
                     /note="regulator of G-protein signalling 9 binding
                     protein"
                     /calculated_mol_wt=25077
     Region          22..>78
                     /region_name="Syntaxin_2"
                     /note="Syntaxin-like protein; pfam14523"
                     /db_xref="CDD:464199"
     CDS             1..237
                     /gene="Rgs9bp"
                     /gene_synonym="RGD1561747"
                     /coded_by="NM_001109142.1:1..714"
                     /db_xref="GeneID:499132"
                     /db_xref="RGD:1561747"
ORIGIN      
        1 mareeckall dalnkttacy hhlvltvggs adtqdlreel qktrqkarel amatgsrltv
       61 alrdrslate eraeferlwv afsgcldlle admqralalg aafplhaprr plvrtgvagg
      121 ssavaarals arslrheaes dfdvadlpql erevlqvgem idnmemkvnv prwtvqarqs
      181 agaellsgas agassaggis veeragpcdp sralaatvfs avllvavala lcvakls
//
LOCUS       NP_001161804             354 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class I, M1, gene 5 precursor [Rattus norvegicus].
ACCESSION   NP_001161804 XP_001059138 XP_001075866
VERSION     NP_001161804.1
DBSOURCE    REFSEQ: accession NM_001168332.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from BX883051.1.
            
            On or before Dec 3, 2009 this sequence version replaced
            XP_001075866.1, XP_001059138.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760434, SAMN14984027
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..354
                     /product="RT1 class I, M1, gene 5 precursor"
                     /note="histocompatibility 2, M region locus 9"
                     /calculated_mol_wt=37908
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2530
     Region          25..203
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          209..298
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          209..215
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          223..232
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(226,228,255..256,258..260,266,268)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(233..235,263,288)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          237..242
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          245..248
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          252..260
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          263..273
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          280..287
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..354
                     /gene="RT1-M1-5"
                     /gene_synonym="H2-M9"
                     /coded_by="NM_001168332.1:1..1065"
                     /db_xref="GeneID:680842"
                     /db_xref="RGD:1587041"
ORIGIN      
        1 mktfvhqall lllivtlait ghpkglhsln ykqtllewpg flelqfiavi yaddiqflgl
       61 nsiwgssrae nkvpwmdede petsekvtqs mldekdlltk imkkvlhiyn ysmtgyhtiq
      121 rrrgcyvvpg ghfshgfvel tfnnhdyiml nedletwsvv gkaaemirqd feeenfakym
      181 reylrgpcve gilgllqyge kallragtpk thvthkvtad gkitlrcwal nfypaeitli
      241 wqkdgsnktq dvevietrps gdgnfqkwaa vvvpsgeeqr ftchveherl pkpitlrwes
      301 pqsinstmai aiavvlgall mgavltffiw krrtkgkekq slsswlhgni kpnl
//
LOCUS       NP_001009919             267 aa            linear   ROD 02-APR-2025
DEFINITION  immunoreceptor Ly49si3 [Rattus norvegicus].
ACCESSION   NP_001009919
VERSION     NP_001009919.1
DBSOURCE    REFSEQ: accession NM_001009919.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Nylenna,O., Naper,C., Vaage,J.T., Woon,P.Y., Gauguier,D.,
            Dissen,E., Ryan,J.C. and Fossum,S.
  TITLE     The genes and gene organization of the Ly49 region of the rat
            natural killer cell gene complex
  JOURNAL   Eur J Immunol 35 (1), 261-272 (2005)
   PUBMED   15593300
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY653730.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY653730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rattus norvegicus"
                     /strain="PVG"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..267
                     /product="immunoreceptor Ly49si3"
                     /note="T-cell surface glycoprotein YE1/48-like; killer
                     cell lectin-like receptor 7"
                     /calculated_mol_wt=31607
     Region          40..158
                     /region_name="Ly49"
                     /note="Ly49-like protein, N-terminal region; pfam08391"
                     /db_xref="CDD:462461"
     Region          145..260
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            order(199,226,244,246..247)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     CDS             1..267
                     /gene="Ly49si3"
                     /coded_by="NM_001009919.1:1..804"
                     /db_xref="GeneID:494209"
                     /db_xref="RGD:1359669"
ORIGIN      
        1 mseqevsysn vrfqkcsdlq nqvrpeetqr araaghrers vpwqlivval vilcslrlva
       61 vamfvtnifq ythekhelhe tlshkyncts mpndidlkee mlrnmsincs rgndlllslk
      121 reqtrwyres ktvipssqht gknveiywfc ygikcyyfil dkktwircqq acqksrlsll
      181 kiddedelkf lqlqvlsdqy wiglsynkak eewswidngq sefslnlkky nekyggcmfl
      241 sqtrlenamc mnrypcicqk rlekfpd
//
LOCUS       NP_001032822            1622 aa            linear   ROD 02-APR-2025
DEFINITION  transient receptor potential cation channel subfamily M member 1
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001032822 XP_341869
VERSION     NP_001032822.1
DBSOURCE    REFSEQ: accession NM_001037733.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1622)
  AUTHORS   Jirku,M., Lansky,Z., Bednarova,L., Sulc,M., Monincova,L., Majer,P.,
            Vyklicky,L., Vondrasek,J., Teisinger,J. and Bousova,K.
  TITLE     The characterization of a novel S100A1 binding site in the
            N-terminus of TRPM1
  JOURNAL   Int J Biochem Cell Biol 78, 186-193 (2016)
   PUBMED   27435061
  REMARK    GeneRIF: a molecular mechanism for the potential regulation of
            TRPM1 by S100A1
REFERENCE   2  (residues 1 to 1622)
  AUTHORS   Devi,S., Markandeya,Y., Maddodi,N., Dhingra,A., Vardi,N.,
            Balijepalli,R.C. and Setaluri,V.
  TITLE     Metabotropic glutamate receptor 6 signaling enhances TRPM1 calcium
            channel function and increases melanin content in human melanocytes
  JOURNAL   Pigment Cell Melanoma Res 26 (3), 348-356 (2013)
   PUBMED   23452348
REFERENCE   3  (residues 1 to 1622)
  AUTHORS   Thameem,F., Puppala,S., Arar,N.H., Blangero,J., Duggirala,R. and
            Abboud,H.E.
  TITLE     Genetic variants in transient receptor potential cation channel,
            subfamily M 1 (TRPM1) and their risk of albuminuria-related traits
            in Mexican Americans
  JOURNAL   Clin Chim Acta 412 (23-24), 2058-2062 (2011)
   PUBMED   21439949
REFERENCE   4  (residues 1 to 1622)
  AUTHORS   Won,J., Shi,L.Y., Hicks,W., Wang,J., Hurd,R., Naggert,J.K.,
            Chang,B. and Nishina,P.M.
  TITLE     Mouse model resources for vision research
  JOURNAL   J Ophthalmol 2011, 391384 (2011)
   PUBMED   21052544
REFERENCE   5  (residues 1 to 1622)
  AUTHORS   Koike,C., Obara,T., Uriu,Y., Numata,T., Sanuki,R., Miyata,K.,
            Koyasu,T., Ueno,S., Funabiki,K., Tani,A., Ueda,H., Kondo,M.,
            Mori,Y., Tachibana,M. and Furukawa,T.
  TITLE     TRPM1 is a component of the retinal ON bipolar cell transduction
            channel in the mGluR6 cascade
  JOURNAL   Proc Natl Acad Sci U S A 107 (1), 332-337 (2010)
   PUBMED   19966281
REFERENCE   6  (residues 1 to 1622)
  AUTHORS   Morgans,C.W., Zhang,J., Jeffrey,B.G., Nelson,S.M., Burke,N.S.,
            Duvoisin,R.M. and Brown,R.L.
  TITLE     TRPM1 is required for the depolarizing light response in retinal
            ON-bipolar cells
  JOURNAL   Proc Natl Acad Sci U S A 106 (45), 19174-19178 (2009)
   PUBMED   19861548
REFERENCE   7  (residues 1 to 1622)
  AUTHORS   Audo,I., Kohl,S., Leroy,B.P., Munier,F.L., Guillonneau,X.,
            Mohand-Said,S., Bujakowska,K., Nandrot,E.F., Lorenz,B.,
            Preising,M., Kellner,U., Renner,A.B., Bernd,A., Antonio,A.,
            Moskova-Doumanova,V., Lancelot,M.E., Poloschek,C.M., Drumare,I.,
            Defoort-Dhellemmes,S., Wissinger,B., Leveillard,T., Hamel,C.P.,
            Schorderet,D.F., De Baere,E., Berger,W., Jacobson,S.G., Zrenner,E.,
            Sahel,J.A., Bhattacharya,S.S. and Zeitz,C.
  TITLE     TRPM1 is mutated in patients with autosomal-recessive complete
            congenital stationary night blindness
  JOURNAL   Am J Hum Genet 85 (5), 720-729 (2009)
   PUBMED   19896113
REFERENCE   8  (residues 1 to 1622)
  AUTHORS   van Genderen,M.M., Bijveld,M.M., Claassen,Y.B., Florijn,R.J.,
            Pearring,J.N., Meire,F.M., McCall,M.A., Riemslag,F.C., Gregg,R.G.,
            Bergen,A.A. and Kamermans,M.
  TITLE     Mutations in TRPM1 are a common cause of complete congenital
            stationary night blindness
  JOURNAL   Am J Hum Genet 85 (5), 730-736 (2009)
   PUBMED   19896109
REFERENCE   9  (residues 1 to 1622)
  AUTHORS   Li,Z., Sergouniotis,P.I., Michaelides,M., Mackay,D.S., Wright,G.A.,
            Devery,S., Moore,A.T., Holder,G.E., Robson,A.G. and Webster,A.R.
  TITLE     Recessive mutations of the gene TRPM1 abrogate ON bipolar cell
            function and cause complete congenital stationary night blindness
            in humans
  JOURNAL   Am J Hum Genet 85 (5), 711-719 (2009)
   PUBMED   19878917
REFERENCE   10 (residues 1 to 1622)
  AUTHORS   Wang,H.P., Pu,X.Y. and Wang,X.H.
  TITLE     Distribution profiles of transient receptor potential
            melastatin-related and vanilloid-related channels in prostatic
            tissue in rat
  JOURNAL   Asian J Androl 9 (5), 634-640 (2007)
   PUBMED   17712480
  REMARK    GeneRIF: Polymerase chain reaction used to check the expression of
            all TRPM and TRPV channel members with specific primers.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ867483.1.
            
            On Dec 15, 2005 this sequence version replaced XP_341869.2.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region compared to variant 1. The resulting protein
            (isoform 2) is shorter but has the same N- and C-termini compared
            to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ867483.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1622
                     /organism="Rattus norvegicus"
                     /strain="DA"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1622
                     /product="transient receptor potential cation channel
                     subfamily M member 1 isoform 2"
                     /function="putative ion channel protein"
                     /note="melastatin; melastatin-1"
                     /calculated_mol_wt=183396
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          65..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          116..381
                     /region_name="LSDAT_euk"
                     /note="SLOG in TRPM; pfam18139"
                     /db_xref="CDD:465665"
     Region          451..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          618..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          <757..1155
                     /region_name="TRPV"
                     /note="Transient Receptor Potential channel, Vanilloid
                     subfamily (TRPV); cl40437"
                     /db_xref="CDD:454755"
     Region          822..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            876..896
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            943..963
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            974..994
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1007..1027
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1100..1120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Site            1151..1171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          1224..1279
                     /region_name="TRPM_tetra"
                     /note="tetramerization domain of TRPM; pfam16519"
                     /db_xref="CDD:465156"
     Region          1354..1406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     Region          1567..1622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WEA5.2)"
     CDS             1..1622
                     /gene="Trpm1"
                     /coded_by="NM_001037733.1:144..5012"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361586"
                     /db_xref="RGD:1597140"
ORIGIN      
        1 mgsmrkmsss fkrgsiksst sgsqkgqkaw iektfckrec ifvipstkdp nrcccgqltn
       61 qhipplpsvt psstaedtkq gdaqsgkwsv skhtqsyptd sygilefqgg gysnkamyir
      121 vsydtkpdsl lhlmvkdwql elpkllisvh gglqsfemqp klkqvfgkgl ikaamttgaw
      181 iftggvstgv vshvgdalkd hssksrgrlc aigiapwgmv enkedlvgkd vtrvyqtmsn
      241 plsklsvlnn shthfiladn gtlgkygaev klrrqlekhi slqkintrlg qgvpvvglvv
      301 eggpnvvsiv leylredppv pvvvcdgsgr asdilsfahk ycdeggvine slrdqllvti
      361 qktfnysksq shqlfaiime cmkkkelvtv frmgsegqqd vemailtall kgtnvsapdq
      421 lslalawnrv diarsqifvf gphwpplgsl appvdtkvae kekkpptatt kgrgkgkgkk
      481 kgkvkeevee etdprkiell nwvnaleqam ldalvldrvd fvklliengv nmqhfltipr
      541 leelyntrlg ppntlhllvr dvkksnlppd yhislidigl vleylmggay rcnytrksfr
      601 tlynnlfgpk rpkalkllgm eddeppakgk kkkkkkkeee ididvddpav srfqypfhel
      661 mvwavlmkrq kmavflwqrg eecmakalva cklykamahe sseselvddi sqdldnnskd
      721 fgqlavelld qsykhdeqva mklltyelkn wsnstclkla vaakhrdfia htcsqmlltd
      781 mwmgrlrmrk npglkvimgi lipptilfle frsyddfsyq tskenedgke keeenvdana
      841 dagsrkgdee nehkkqrsip igtkicefyn apivkfwfyt isylgylllf nyvilvrmdg
      901 wpspqewivi syivslalek ireilmsepg klsqkikvwl qeywnitdlv aismfmvgai
      961 lrlqnqpymg ygrviycvdi ilwyirvldi fgvnkylgpy vmmigkmmid mlyfvvimlv
     1021 vlmsfgvarq ailhpeekps wklarnifym pywmiygevf adqidlyame inppcgenly
     1081 deegkrlppc ipgawltpal macyllvani llvnlliavf nntffevksi snqvwkfqry
     1141 qlimtfhdrp vlpppmiils hiyiivmrls grcrkkregd qeerdrglkl flsdeelkkl
     1201 hefeeqcvqe hfrekedeqq sssderirvt servenmsmr leeinerenf mkaslqtvdl
     1261 rlsqleelsg rmvgalenla gidrsdliqa rsrassecea tyllrqssin sadgysmyry
     1321 hfngeellfe epalstspgt vfrkktcsfr vkeedvkphl dqpsslhhtp gpsppatpgr
     1381 srlaldgpls telrpgldpg isageldpra dfksaevaps lntanvastq ltvestvshp
     1441 lresklaryy pgdlntyktm ksrsfvyseg rklvrglsnw gaeyssimdq twnsaewrcq
     1501 vqritrsrst dipyivseaa sqdefedehr esllapqisr saltvsdrpe kenllsvkph
     1561 qtlgfpclrs rslhghprsa kpspskldra ghasstsnla vmsdapegqn tqqekgnpet
     1621 ec
//
LOCUS       NP_001100247             132 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC299713 [Rattus norvegicus].
ACCESSION   NP_001100247 XP_001080032 XP_235021
VERSION     NP_001100247.1
DBSOURCE    REFSEQ: accession NM_001106777.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473960.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_235021.1, XP_001080032.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..132
                     /product="uncharacterized protein LOC299713"
                     /calculated_mol_wt=14434
     Region          16..111
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..132
                     /gene="Rps12l4"
                     /gene_synonym="RGD1561102"
                     /coded_by="NM_001106777.1:390..788"
                     /db_xref="GeneID:299713"
                     /db_xref="RGD:1561102"
ORIGIN      
        1 makedtaagv imdvntalqe vlktalvhdg largiheaak algkrqahlc vlaancdkpm
       61 yiklvetlca ehqinlikvd dnkklgewvg lckidrkgkp rkvigcscvv vkdygqesqa
      121 kdvieeyfkc kk
//
LOCUS       NP_001011928             481 aa            linear   ROD 02-APR-2025
DEFINITION  dipeptidase 2 precursor [Rattus norvegicus].
ACCESSION   NP_001011928 XP_214684
VERSION     NP_001011928.1
DBSOURCE    REFSEQ: accession NM_001011928.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Habib,G.M., Shi,Z.Z., Cuevas,A.A. and Lieberman,M.W.
  TITLE     Identification of two additional members of the membrane-bound
            dipeptidase family
  JOURNAL   FASEB J 17 (10), 1313-1315 (2003)
   PUBMED   12738806
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088195.1.
            
            On Feb 11, 2005 this sequence version replaced XP_214684.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088195.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..481
                     /product="dipeptidase 2 precursor"
                     /EC_number="3.4.13.19"
                     /calculated_mol_wt=50028
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M872.1)"
                     /calculated_mol_wt=3275
     mat_peptide     31..462
                     /product="Dipeptidase 2. /id=PRO_0000231607"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M872.1)"
                     /calculated_mol_wt=48042
     Region          80..400
                     /region_name="Peptidase_M19"
                     /note="Membrane dipeptidase (Peptidase family M19);
                     pfam01244"
                     /db_xref="CDD:395996"
     Site            order(90,92,136,189,262,283,294,352,355)
                     /site_type="active"
                     /db_xref="CDD:238626"
     Site            112
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M872.1)"
     Site            order(138,147..149,151..152,155,159,199..200,202..203,
                     206..207)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238626"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M872.1)"
     Region          434..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M872.1)"
     CDS             1..481
                     /gene="Dpep2"
                     /coded_by="NM_001011928.1:95..1540"
                     /db_xref="GeneID:291984"
                     /db_xref="RGD:1305746"
ORIGIN      
        1 mslkgleghw vlsqvfllvv vllllgpsep liraqtkpgi adastapspl rtltkpaifs
       61 ipttpgnpnf pdlrdrtral mqdfplidgh ndlplvlrqf yqnglqdtnl rnfthgqtsl
      121 nrlkdgfvga qfwsayvpcq tqdrdalrlt leqidlirrm casyselelv tsvqalnstq
      181 klacligveg ghsldnslav lrsfyllgvr yltlthtcnt pwaessskdv hsfyssvkgl
      241 tsfgekvvae mnrlgmmidl shvsdatarq alevsqapvi fshsaaravc pnarnlpddi
      301 lqllkknggi vmvtfavgvl pcnplanvst vadhfdhirt vigsefigvg gdydgtkqfp
      361 qgledvstyp vlieellrrg wgeqelqgvl rgnllrvfrq veqvreknkw qspledmipe
      421 eqldsachsv lphrrqypek dppetpdsht hklspkmpys kssplrassl timatflgll
      481 i
//
LOCUS       NP_955783                378 aa            linear   ROD 02-APR-2025
DEFINITION  C-C chemokine receptor type 7 precursor [Rattus norvegicus].
ACCESSION   NP_955783 XP_213486
VERSION     NP_955783.1
DBSOURCE    REFSEQ: accession NM_199489.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wurm,S., Steege,A., Rom-Jurek,E.M., van Roeyen,C.R., Kurtz,A.,
            Banas,B. and Banas,M.C.
  TITLE     CCR7 Is Important for Mesangial Cell Physiology and Repair
  JOURNAL   J Histochem Cytochem 66 (1), 7-22 (2018)
   PUBMED   29077526
  REMARK    GeneRIF: This study shows induction of renal CCR7 expression in the
            Model of Anti-Thy1.1 Mesangioproliferative Glomerulonephritis in
            rat.
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Ma,T., Luan,S.L., Huang,H., Sun,X.K., Yang,Y.M., Zhang,H.,
            Han,W.D., Li,H. and Han,Y.
  TITLE     Upregulation of CC Chemokine Receptor 7 (CCR7) Enables Migration of
            Xenogeneic Human Adipose-Derived Mesenchymal Stem Cells to Rat
            Secondary Lymphoid Organs
  JOURNAL   Med Sci Monit 22, 5206-5217 (2016)
   PUBMED   28035134
  REMARK    GeneRIF: These results suggest that upregulation of rat CCR7
            expression does not change the phenotype, differentiation, or
            proliferation capacity of human adipose-derived stem cells (hASCs),
            but does enable efficient migration of hASCs to rat secondary
            lymphoid organs.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Zhang,W., Tu,G., Lv,C., Long,J., Cong,L. and Han,Y.
  TITLE     Matrix metalloproteinase-9 is up-regulated by CCL19/CCR7
            interaction via PI3K/Akt pathway and is involved in CCL19-driven
            BMSCs migration
  JOURNAL   Biochem Biophys Res Commun 451 (2), 222-228 (2014)
   PUBMED   25086360
  REMARK    GeneRIF: CCL19/CCR7 contributes to the migration of bone marrow
            mesenchymal stem cells by upregulating MMP9 potentially via the
            PI3K/Akt pathway.
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Nakamura,K., White,A.J., Parnell,S.M., Lane,P.J., Jenkinson,E.J.,
            Jenkinson,W.E. and Anderson,G.
  TITLE     Differential requirement for CCR4 in the maintenance but not
            establishment of the invariant Vgamma5(+) dendritic epidermal
            T-cell pool
  JOURNAL   PLoS One 8 (9), e74019 (2013)
   PUBMED   24069263
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Chiang,Y.J., Ho,K.C., Sun,C.T., Chiu,J.J., Lee,F.J., Liao,F.,
            Yang-Yen,H.F. and Yen,J.J.
  TITLE     CBAP functions as a novel component in chemokine-induced
            ZAP70-mediated T-cell adhesion and migration
  JOURNAL   PLoS One 8 (4), e61761 (2013)
   PUBMED   23620790
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Debes,G.F., Bonhagen,K., Wolff,T., Kretschmer,U., Krautwald,S.,
            Kamradt,T. and Hamann,A.
  TITLE     CC chemokine receptor 7 expression by effector/memory CD4+ T cells
            depends on antigen specificity and tissue localization during
            influenza A virus infection
  JOURNAL   J Virol 78 (14), 7528-7535 (2004)
   PUBMED   15220427
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Gibejova,A., Mrazek,F., Subrtova,D., Sekerova,V., Szotkowska,J.,
            Kolek,V., du Bois,R.M. and Petrek,M.
  TITLE     Expression of macrophage inflammatory protein-3 beta/CCL19 in
            pulmonary sarcoidosis
  JOURNAL   Am J Respir Crit Care Med 167 (12), 1695-1703 (2003)
   PUBMED   12626344
REFERENCE   8  (residues 1 to 378)
  AUTHORS   Bouchon,A., Hernandez-Munain,C., Cella,M. and Colonna,M.
  TITLE     A DAP12-mediated pathway regulates expression of CC chemokine
            receptor 7 and maturation of human dendritic cells
  JOURNAL   J Exp Med 194 (8), 1111-1122 (2001)
   PUBMED   11602640
REFERENCE   9  (residues 1 to 378)
  AUTHORS   Forster,R., Schubel,A., Breitfeld,D., Kremmer,E., Renner-Muller,I.,
            Wolf,E. and Lipp,M.
  TITLE     CCR7 coordinates the primary immune response by establishing
            functional microenvironments in secondary lymphoid organs
  JOURNAL   Cell 99 (1), 23-33 (1999)
   PUBMED   10520991
REFERENCE   10 (residues 1 to 378)
  AUTHORS   Yoshida,R., Nagira,M., Kitaura,M., Imagawa,N., Imai,T. and
            Yoshie,O.
  TITLE     Secondary lymphoid-tissue chemokine is a functional ligand for the
            CC chemokine receptor CCR7
  JOURNAL   J Biol Chem 273 (12), 7118-7122 (1998)
   PUBMED   9507024
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY379972.1.
            
            On Jan 23, 2004 this sequence version replaced XP_213486.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY379972.1, BC089762.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..378
                     /product="C-C chemokine receptor type 7 precursor"
                     /note="C-C chemokine receptor type 7; chemokine (C-C
                     motif) receptor 7"
                     /calculated_mol_wt=40189
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2651
     Region          59..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          61..85
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          94..115
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          130..152
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          177..193
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          221..244
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          262..284
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..378
                     /gene="Ccr7"
                     /coded_by="NM_199489.4:79..1215"
                     /db_xref="GeneID:287673"
                     /db_xref="RGD:735151"
ORIGIN      
        1 mdlgkptknv lvvallvifq vcfcqdevtd dyigenttvd ytlyesvcfk kdvrnfkawf
       61 lplmysvicf vgllgnglvv ltyiyfkrlk tmtdtyllnl avadilflmi lpfwayseak
      121 swifgaylck sifgiyklsf fsgmllllci sidryvaivq avsahrhrar vllisklsci
      181 giwtlaffls ipellysglq knsgedtwrc slvsaqveal iaiqvaqmvv gfvlpmlams
      241 fcylviirtl lqarnfernk aikviiavvv vfvvfqlpyn gvvlaqtvan fnitnsscea
      301 skqlniaydv tyslasvrcc vnpflyafig vkfrsdlfkl fkdlgclsqe rlrqwsscrh
      361 vrhtsvsmea ettttfsp
//
LOCUS       NP_001160154             318 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 117 [Rattus norvegicus].
ACCESSION   NP_001160154
VERSION     NP_001160154.1
DBSOURCE    REFSEQ: accession NM_001166682.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY486339.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..318
                     /product="taste receptor type 2 member 117"
                     /note="T2R39; T2R117; taste receptor type 2 member 39"
                     /calculated_mol_wt=36959
     Region          15..303
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          15..40
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          52..76
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          89..111
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          138..154
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          182..205
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          230..255
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     Region          267..292
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675B8.1)"
     CDS             1..318
                     /gene="Tas2r117"
                     /coded_by="NM_001166682.1:1..957"
                     /db_xref="GeneID:100310880"
                     /db_xref="RGD:2314258"
ORIGIN      
        1 mqhnlktifv ishstltiil ftelvtgiig ngfmalvhcm dwlrrkkisl vnqiltalai
       61 srifqlcllf islvisfsyp dltttslikv tcnlwiivnh fniwlatclg ifyflkisnf
      121 snslflylkw rvekvvlvtl lvslvlltln sllinleini cineyqrnit ysfnsyyhan
      181 chrqmlslhi iflsvpfvls lstflllifs lgthhkkmqq hvqgrrdast mahfkalqtv
      241 iaflllysif ilsvlvqiwk yellkknlfi lfcqvayvaf psfhsyilil gdmkmrqacl
      301 svlwwqkfrk nyvepldl
//
LOCUS       NP_058970                828 aa            linear   ROD 02-APR-2025
DEFINITION  glycerol-3-phosphate acyltransferase 1, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_058970
VERSION     NP_058970.1
DBSOURCE    REFSEQ: accession NM_017274.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Zhang,H., Li,Y., Hu,J., Shen,W.J., Singh,M., Hou,X., Bittner,A.,
            Bittner,S., Cortez,Y., Tabassum,J., Kraemer,F.B. and Azhar,S.
  TITLE     Effect of Creosote Bush-Derived NDGA on Expression of Genes
            Involved in Lipid Metabolism in Liver of High-Fructose Fed Rats:
            Relevance to NDGA Amelioration of Hypertriglyceridemia and Hepatic
            Steatosis
  JOURNAL   PLoS One 10 (9), e0138203 (2015)
   PUBMED   26394137
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Cattaneo,E.R., Pellon-Maison,M., Rabassa,M.E., Lacunza,E.,
            Coleman,R.A. and Gonzalez-Baro,M.R.
  TITLE     Glycerol-3-phosphate acyltransferase-2 is expressed in spermatic
            germ cells and incorporates arachidonic acid into triacylglycerols
  JOURNAL   PLoS One 7 (8), e42986 (2012)
   PUBMED   22905194
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Guha,P., Aneja,K.K., Shilpi,R.Y. and Haldar,D.
  TITLE     Transcriptional regulation of mitochondrial glycerophosphate
            acyltransferase is mediated by distal promoter via ChREBP and
            SREBP-1
  JOURNAL   Arch Biochem Biophys 490 (2), 85-95 (2009)
   PUBMED   19682972
  REMARK    GeneRIF: ChREBP and SREBP-1 bind to the mtGPAT distal promoter.
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Karlsson,E.A., Wang,S., Shi,Q., Coleman,R.A. and Beck,M.A.
  TITLE     Glycerol-3-phosphate acyltransferase 1 is essential for the immune
            response to infection with coxsackievirus B3 in mice
  JOURNAL   J Nutr 139 (4), 779-783 (2009)
   PUBMED   19193813
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Rodriguez-Calvo,R., Barroso,E., Serrano,L., Coll,T., Sanchez,R.M.,
            Merlos,M., Palomer,X., Laguna,J.C. and Vazquez-Carrera,M.
  TITLE     Atorvastatin prevents carbohydrate response element binding protein
            activation in the fructose-fed rat by activating protein kinase A
  JOURNAL   Hepatology 49 (1), 106-115 (2009)
   PUBMED   19053045
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Onorato,T.M. and Haldar,D.
  TITLE     Casein kinase II stimulates rat liver mitochondrial
            glycerophosphate acyltransferase activity
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1091-1096 (2002)
   PUBMED   12207885
  REMARK    GeneRIF: Casein kinase II stimulates rat liver mitochondrial
            glycerophosphate acyltransferase activity
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Park,H., Kaushik,V.K., Constant,S., Prentki,M., Przybytkowski,E.,
            Ruderman,N.B. and Saha,A.K.
  TITLE     Coordinate regulation of malonyl-CoA decarboxylase,
            sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase
            by AMP-activated protein kinase in rat tissues in response to
            exercise
  JOURNAL   J Biol Chem 277 (36), 32571-32577 (2002)
   PUBMED   12065578
  REMARK    GeneRIF: Gpam regulation in rats in response to exercise
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Balija,V.S., Chakraborty,T.R., Nikonov,A.V., Morimoto,T. and
            Haldar,D.
  TITLE     Identification of two transmembrane regions and a cytosolic domain
            of rat mitochondrial glycerophosphate acyltransferase
  JOURNAL   J Biol Chem 275 (41), 31668-31673 (2000)
   PUBMED   10924502
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Ganesh Bhat,B., Wang,P., Kim,J.H., Black,T.M., Lewin,T.M.,
            Fiedorek,F.T. Jr. and Coleman,R.A.
  TITLE     Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and
            characterization of the cDNA and expressed protein
  JOURNAL   Biochim Biophys Acta 1439 (3), 415-423 (1999)
   PUBMED   10446428
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Lee,Y., Hirose,H., Zhou,Y.T., Esser,V., McGarry,J.D. and Unger,R.H.
  TITLE     Increased lipogenic capacity of the islets of obese rats: a role in
            the pathogenesis of NIDDM
  JOURNAL   Diabetes 46 (3), 408-413 (1997)
   PUBMED   9032096
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF021348.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF021348.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..828
                     /product="glycerol-3-phosphate acyltransferase 1,
                     mitochondrial"
                     /EC_number="2.3.1.15"
                     /note="GPAT; GPAT-1"
                     /calculated_mol_wt=93584
     Region          80..120
                     /region_name="Important for mitochondrial localization.
                     /evidence=ECO:0000250|UniProtKB:Q9HCL2"
                     /note="propagated from UniProtKB/Swiss-Prot (P97564.3)"
     Region          131..656
                     /region_name="PlsB"
                     /note="Glycerol-3-phosphate O-acyltransferase [Lipid
                     transport and metabolism]; COG2937"
                     /db_xref="CDD:442180"
     Region          201..411
                     /region_name="LPLAT_DHAPAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: GPAT-like; cd07993"
                     /db_xref="CDD:153255"
     Site            order(230,233,235,256..259,316..318)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153255"
     Region          230..235
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q9HCL2"
                     /note="propagated from UniProtKB/Swiss-Prot (P97564.3)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P97564.3)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97564.3)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97564.3)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61586; propagated from
                     UniProtKB/Swiss-Prot (P97564.3)"
     Site            784
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61586; propagated from
                     UniProtKB/Swiss-Prot (P97564.3)"
     CDS             1..828
                     /gene="Gpam"
                     /coded_by="NM_017274.1:160..2646"
                     /db_xref="GeneID:29653"
                     /db_xref="RGD:61847"
ORIGIN      
        1 meessvtigt idvsylpnss eyslgrckht nedwvdcgfk ptffrsatlk wkeslmsrkr
       61 pfvgrccysc tpqswerffn psipslglrn viyinethtr hrgwlarrls yilfvqerdv
      121 hkgmfatsit dnvlnssrvq eaiaevaael npdgsaqqqs kaiqkvkrka rkilqemvat
      181 vspgmirltg wvllklfnsf fwniqihkgq lemvkaatet nlpllflpvh rshidylllt
      241 filfchnika pyiasgnnln ipifstlihk lggffirrrl detpdgrkdi lyrallhghi
      301 vellrqqqfl eiflegtrsr sgktscarag llsvvvdtls sntipdilvi pvgisydrii
      361 eghyngeqlg kpkkneslws vargvirmlr knygyvrvdf aqpfslkeyl egqsqkpvsa
      421 plsleqallp ailpsrpdaa aaehedmssn esrnaadeaf rrrlianlae hilftasksc
      481 aimsthivac lllyrhrqgi hlstlvedff vmkeevlard fdlgfsgnse dvvmhaiqll
      541 gncvtithts rkdeffitps ttvpsvfeln fysngvlhvf imeaiiacsi yavqnkrgsg
      601 gsagglgnli sqeqlvrkaa slcyllsneg tislpcqtfy qvcqetvgkf iqygiltvae
      661 qddqedvspg laeqqwnkkl peplnwrsde ededsdfgee qrdcylkvsq akehqqfitf
      721 lqrllgplle ayssaaifvh tfrgpvpese ylqklhryll trternvavy aesatyclvk
      781 navkmfkdig vfketkqkra svlelsttfl pqgsrqklle yilsfvvl
//
LOCUS       NP_075231                597 aa            linear   ROD 02-APR-2025
DEFINITION  cholinesterase precursor [Rattus norvegicus].
ACCESSION   NP_075231
VERSION     NP_075231.1
DBSOURCE    REFSEQ: accession NM_022942.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Szmicsekova,K., Bies Pivackova,L., Kilianova,Z., Slobodova,L.,
            Krenek,P. and Hrabovska,A.
  TITLE     Aortic butyrylcholinesterase is reduced in spontaneously
            hypertensive rats
  JOURNAL   Physiol Res 70 (5), 809-813 (2021)
   PUBMED   34505519
  REMARK    GeneRIF: Aortic butyrylcholinesterase is reduced in spontaneously
            hypertensive rats.
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Munir,S., Habib,R., Awan,S., Bibi,N., Tanveer,A., Batool,S. and
            Nurulain,S.M.
  TITLE     Biochemical Analysis and Association of Butyrylcholinesterase SNPs
            rs3495 and rs1803274 with Substance Abuse Disorder
  JOURNAL   J Mol Neurosci 67 (3), 445-455 (2019)
   PUBMED   30707402
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Tonin,A.A., da Silva,A.S., Thorstenberg,M.L., Castilhos,L.G.,
            Franca,R.T., Leal,D.B., Duarte,M.M., Vogel,F.S., de La Rue,M.L. and
            dos Anjos Lopes,S.T.
  TITLE     Influence of Toxoplasma gondii acute infection on cholinesterase
            activities of Wistar rats
  JOURNAL   Korean J Parasitol 51 (4), 421-426 (2013)
   PUBMED   24039284
  REMARK    GeneRIF: No significant difference was observed in the activity of
            BChE in serum after Toxoplasma gondii infection.
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Koohestani,F., Brown,C.M. and Meisami,E.
  TITLE     Differential effects of developmental hypo- and hyperthyroidism on
            acetylcholinesterase and butyrylcholinesterase activity in the
            spinal cord of developing postnatal rat pups
  JOURNAL   Int J Dev Neurosci 30 (7), 570-577 (2012)
   PUBMED   22982053
  REMARK    GeneRIF: the neurochemical development of glia and other
            non-neuronal cells, where BuChE is mainly localized, is
            comparatively unaffected cy hypo- and hyperthyroidism
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Koohestani,F., Brown,C.M. and Meisami,E.
  TITLE     Postnatal growth hormone deficiency in growing rats causes marked
            decline in the activity of spinal cord acetylcholinesterase but not
            butyrylcholinesterase
  JOURNAL   Int J Dev Neurosci 30 (7), 578-583 (2012)
   PUBMED   22922167
  REMARK    GeneRIF: the absence of any effects on BuChE activity implies that
            growth hormone does not affect the development of non-neuronal
            elements
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Basu,P.S., Batabyal,S.K., Bhattacharya,A. and Datta,T.K.
  TITLE     Cholinesterase activities in cerebrospinal fluid of patients with
            idiopathic convulsive disorders
  JOURNAL   Clin Chim Acta 235 (1), 107-112 (1995)
   PUBMED   7634486
REFERENCE   7  (residues 1 to 597)
  AUTHORS   McGuire,M.C., Nogueira,C.P., Bartels,C.F., Lightstone,H., Hajra,A.,
            Van der Spek,A.F., Lockridge,O. and La Du,B.N.
  TITLE     Identification of the structural mutation responsible for the
            dibucaine-resistant (atypical) variant form of human serum
            cholinesterase
  JOURNAL   Proc Natl Acad Sci U S A 86 (3), 953-957 (1989)
   PUBMED   2915989
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Ruberg,M., Villageois,A., Bonnet,A.M., Pillon,B., Rieger,F. and
            Agid,Y.
  TITLE     Acetylcholinesterase and butyrylcholinesterase activity in the
            cerebrospinal fluid of patients with neurodegenerative diseases
            involving cholinergic systems
  JOURNAL   J Neurol Neurosurg Psychiatry 50 (5), 538-543 (1987)
   PUBMED   2953866
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Godfrey,D.A. and Matschinsky,F.M.
  TITLE     Enzymes of the cholinergic system in islets of Langerhans
  JOURNAL   J Histochem Cytochem 23 (9), 645-651 (1975)
   PUBMED   126256
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Flumerfelt,B.A. and Lewis,P.R.
  TITLE     Cholinesterase activity in the hypoglossal nucleus of the rat and
            the changes produced by axotomy: a light and electron microscopic
            study
  JOURNAL   J Anat 119 (Pt 2), 309-331 (1975)
   PUBMED   1133098
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF244349.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF244349.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676787 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q32"
     Protein         1..597
                     /product="cholinesterase precursor"
                     /EC_number="3.1.1.8"
                     /note="cholinesterase"
                     /calculated_mol_wt=65048
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2746
     Region          25..545
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(138..140,220..222,225,376,380..381,416,462,465)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(221,348,461)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Region          560..594
                     /region_name="AChE_tetra"
                     /note="Acetylcholinesterase tetramerization domain;
                     pfam08674"
                     /db_xref="CDD:430146"
     CDS             1..597
                     /gene="Bche"
                     /coded_by="NM_022942.1:85..1878"
                     /db_xref="GeneID:65036"
                     /db_xref="RGD:619996"
ORIGIN      
        1 mvteihfllw illlcmlfgk shteedviit tktgrvrgls mpilggtvta flgipyaqpp
       61 lgslrfkkpq plnkwpdvyn atkyanscyq nidqafpgfq gsemwnpntn lsedclylnv
      121 wipvpkpkna tvmvwvyggg fqtgtsslpv ydgkfltrve rvivvsmnyr vgalgflafp
      181 gnseapgnmg lfdqqlalqw iqrniaafgg npksvtlfge sagaasvslh llcpqsyplf
      241 trailesgss napwavkhpe earnrtltla kfigcskene keiitclrsk dpqeillnek
      301 lvlpsdsirs infgptvdgd fltdmphtll qlgkvktaqi lvgvnkdegt aflvygapgf
      361 skdndslitr refqeglnmy fpgvsslgke ailfyyvdwl gdqtpevyre afddiigdyn
      421 iicpaleftk kfaeleinaf fyyfehrssk lpwpewmgvm hgyeiefvfg lplerrvnyt
      481 raeeifsrsi mktwanfaky ghpngtqgns tvwpvftste qkyltlntek skinsklrap
      541 qcqfwrlffp kvleitgdid ereqewkagf hrwsnymmdw knqfndytsk ketctdl
//
LOCUS       NP_001100675             647 aa            linear   ROD 02-APR-2025
DEFINITION  ATP-binding cassette, sub-family G (WHITE), member 3 family member
            [Rattus norvegicus].
ACCESSION   NP_001100675 XP_001064705 XP_223174
VERSION     NP_001100675.1
DBSOURCE    REFSEQ: accession NM_001107205.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474022.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223174.4, XP_001064705.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..647
                     /product="ATP-binding cassette, sub-family G (WHITE),
                     member 3 family member"
                     /calculated_mol_wt=73299
     Region          64..644
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     CDS             1..647
                     /gene="Abcg3l3"
                     /gene_synonym="RGD1564709"
                     /coded_by="NM_001107205.1:59..2002"
                     /db_xref="GeneID:305142"
                     /db_xref="RGD:1564709"
ORIGIN      
        1 msssndptvi pmaerrygdl petntsdpet lteeavlsfh nisyretvqs gfplrqqthv
       61 merlssisgi mgpglnaimg pqdgsrslll dvlaarrdpc glsgdilvng kpqpanfkct
      121 sgyvpqndvi mhtvtvrdnl efsaalrlpm titrnekrrr inevlellhl ekeqntkprs
      181 kelrkrtsia velvtehpil flddpttgld lrtttdiiav lrrmskkgrt vifsinqpqy
      241 sifrffdslt lvasgklmfh gpaqdaleyf tsagyqyesh nnpadffldv ingglcdtee
      301 dgheadehed lyerlhqvte klanmyaqsp lhsdtrakld qllgeqkqdr rsamettfvt
      361 pfwhqfgwit lrsfknfkgf pwvtviqaii avilavfvgt ifrllqnvct evkaragllf
      421 fltgfecils vsagelflld rnhflhehts gyyrvssyff gkllaelipr rllpsmiftl
      481 ityfiagmkt gvkgffvtif tvmmlassas slslslgage ntaalpttli tiyfmfmlff
      541 sglslfsinf lpqlswiqyl siphygfral lhneflgqnf cpehnteevs rcqnyvictg
      601 eeflqnldid ssswgfwenh laltcimiil lmisyvrllr lkkrihc
//
LOCUS       NP_001008803             493 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type II cuticular Hb2 [Rattus norvegicus].
ACCESSION   NP_001008803 XP_345877
VERSION     NP_001008803.1
DBSOURCE    REFSEQ: accession NM_001008803.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Rogers,M.A., Winter,H., Langbein,L., Wolf,C. and Schweizer,J.
  TITLE     Characterization of a 300 kbp region of human DNA containing the
            type II hair keratin gene domain
  JOURNAL   J Invest Dermatol 114 (3), 464-472 (2000)
   PUBMED   10692104
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK003979.1.
            
            On Jan 5, 2005 this sequence version replaced XP_345877.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK003979.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMD00132285,
                                           SAMD00132286 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..493
                     /product="keratin, type II cuticular Hb2"
                     /note="type II keratin Kb22; keratin 82, type II"
                     /calculated_mol_wt=54352
     Region          <18..91
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          95..405
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     CDS             1..493
                     /gene="Krt82"
                     /gene_synonym="Kb22"
                     /coded_by="NM_001008803.1:1..1482"
                     /db_xref="GeneID:366991"
                     /db_xref="RGD:1359276"
ORIGIN      
        1 mprmvthyev skvpsrpgvg gglralgclg srslcnvgfg rprvasrcgm pgfgyragaa
       61 cgspacitpv tinesllvpl eleidptvqs vkrdekeqik clnnrfasfi nkvrfleqkn
      121 klletkwnfm qqqrscqsnm eplfegyica lrrqldcvsg dhgrleaelc slqealegyk
      181 kkyeeelslr pcaenefvtl kkdvdtaflv kadletnlea leheieflka lfeeeisllq
      241 sqisetsviv kmdnsrdldv dgivaeikaq yddiasrska eaeawyqcry eelrmtagnh
      301 sdnlrnrkne ilemnkliqr lqqdietvka qrcklegaia qaeqqgeaal sdakcklagl
      361 eealqkakqd macllkeyqe vmnsklgldi eiatyrrlle geehrlcegi gpvnisvsss
      421 kgavlyepcv vgtpmlrtey ctgatgvlrn sggcsvvgtg elyipcepqg llgcgsgrss
      481 smkmgagsns csh
//
LOCUS       NP_620205                761 aa            linear   ROD 02-APR-2025
DEFINITION  prolyl endopeptidase FAP [Rattus norvegicus].
ACCESSION   NP_620205
VERSION     NP_620205.1
DBSOURCE    REFSEQ: accession NM_138850.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Kilvaer,T.K., Rakaee,M., Hellevik,T., Ostman,A., Strell,C.,
            Bremnes,R.M., Busund,L.T., Donnem,T. and Martinez-Zubiaurre,I.
  TITLE     Tissue analyses reveal a potential immune-adjuvant function of
            FAP-1 positive fibroblasts in non-small cell lung cancer
  JOURNAL   PLoS One 13 (2), e0192157 (2018)
   PUBMED   29415055
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Tillmanns,J., Hoffmann,D., Habbaba,Y., Schmitto,J.D., Sedding,D.,
            Fraccarollo,D., Galuppo,P. and Bauersachs,J.
  TITLE     Fibroblast activation protein alpha expression identifies activated
            fibroblasts after myocardial infarction
  JOURNAL   J Mol Cell Cardiol 87, 194-203 (2015)
   PUBMED   26319660
  REMARK    GeneRIF: In this study, we show for the first time the expression
            of FAP in activated fibroblasts after MI and its activation by
            TGFbeta1. Effects of FAP on fibroblast migration and gelatinolytic
            activity indicate a potential role in cardiac wound healing
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Kilvaer,T.K., Khanehkenari,M.R., Hellevik,T., Al-Saad,S.,
            Paulsen,E.E., Bremnes,R.M., Busund,L.T., Donnem,T. and
            Martinez,I.Z.
  TITLE     Cancer Associated Fibroblasts in Stage I-IIIA NSCLC: Prognostic
            Impact and Their Correlations with Tumor Molecular Markers
  JOURNAL   PLoS One 10 (8), e0134965 (2015)
   PUBMED   26252379
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Augoff,K., Hryniewicz-Jankowska,A., Tabola,R., Czapla,L.,
            Szelachowski,P., Wierzbicki,J., Grabowski,K. and Sikorski,A.F.
  TITLE     Upregulated expression and activation of membrane-associated
            proteases in esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 31 (6), 2820-2826 (2014)
   PUBMED   24789592
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Rowton,M., Ramos,P., Anderson,D.M., Rhee,J.M., Cunliffe,H.E. and
            Rawls,A.
  TITLE     Regulation of mesenchymal-to-epithelial transition by PARAXIS
            during somitogenesis
  JOURNAL   Dev Dyn 242 (11), 1332-1344 (2013)
   PUBMED   24038871
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Park,J.E., Lenter,M.C., Zimmermann,R.N., Garin-Chesa,P., Old,L.J.
            and Rettig,W.J.
  TITLE     Fibroblast activation protein, a dual specificity serine protease
            expressed in reactive human tumor stromal fibroblasts
  JOURNAL   J Biol Chem 274 (51), 36505-36512 (1999)
   PUBMED   10593948
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Mueller,S.C., Ghersi,G., Akiyama,S.K., Sang,Q.X., Howard,L.,
            Pineiro-Sanchez,M., Nakahara,H., Yeh,Y. and Chen,W.T.
  TITLE     A novel protease-docking function of integrin at invadopodia
  JOURNAL   J Biol Chem 274 (35), 24947-24952 (1999)
   PUBMED   10455171
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Niedermeyer,J., Enenkel,B., Park,J.E., Lenter,M., Rettig,W.J.,
            Damm,K. and Schnapp,A.
  TITLE     Mouse fibroblast-activation protein--conserved Fap gene
            organization and biochemical function as a serine protease
  JOURNAL   Eur J Biochem 254 (3), 650-654 (1998)
   PUBMED   9688278
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Pineiro-Sanchez,M.L., Goldstein,L.A., Dodt,J., Howard,L., Yeh,Y.,
            Tran,H., Argraves,W.S. and Chen,W.T.
  TITLE     Identification of the 170-kDa melanoma membrane-bound gelatinase
            (seprase) as a serine integral membrane protease
  JOURNAL   J Biol Chem 272 (12), 7595-7601 (1997)
   PUBMED   9065413
  REMARK    Erratum:[J Biol Chem. 1998 May 22:273(21):13366]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF493782.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF493782.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..761
                     /product="prolyl endopeptidase FAP"
                     /note="seprase"
                     /calculated_mol_wt=87713
     Region          106..473
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          553..757
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..761
                     /gene="Fap"
                     /coded_by="NM_138850.1:8..2293"
                     /db_xref="GeneID:192203"
                     /db_xref="RGD:621253"
ORIGIN      
        1 mktwlktvfg vttlvalalv vicivlrpsr vyspegntgr sltlkdilng tfsyktyfpn
       61 wiseqeylhq seddnivfyn ietresyiil snstmksvna tdyglspdrq fiylesdysk
      121 lwrysytaty yiydlqngef vrgyelprpi qylcwspvgs klayvyqnni ylkqrpgdpp
      181 fqitytgren rifngipdwv yeeemlatky alwwspdgky layvefndsd ipiiaysyyg
      241 dgqyprtini pypkagaknp ivrvfivdti yphhvgpiev pvpemiassd yyftwltwvt
      301 nervclqwlk rvqnvsvlsi cdfredwhaw dcpknqehie esrtgwaggf fvstpafsqd
      361 aasyykifsd kdgykhihyi kdtvenaiqi tsgkweaiyi frvtqdslfy ssnefegypg
      421 rrniyrisig nsppskkcvt chlrkercqy ytasfsykak yyalicygpg lpistlhdgr
      481 tdqeiqvlee nkelenalrn iqlpaveikk ledggmtfwy kmilppqfdr skkyplliqv
      541 yggpcsqsvk svfsvnwity laskegivva lvdgrgtafq gdkflhavyr klgvyevedq
      601 ltavrkfiem gfidegriai wgwsyggyvs slalasgtgl fkcgiavapv ssweyyasiy
      661 terfmglptk ddnlehykns tvmaraeyfr nvdyllihgt addnvhfqns aqiakalvna
      721 qvdfqamwys dqnhgissgr sqnhlythmt hflkqcfsls d
//
LOCUS       NP_783180                358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7e [Rattus norvegicus].
ACCESSION   NP_783180
VERSION     NP_783180.2
DBSOURCE    REFSEQ: accession NM_175590.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702322.1.
            
            On Jan 21, 2005 this sequence version replaced NP_783180.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7e"
                     /note="taR-14; taR-7e; trace amine receptor 7e; trace
                     amine receptor 14"
                     /calculated_mol_wt=40060
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923X6.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            122..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923X6.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            310..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923X6.1)"
     CDS             1..358
                     /gene="Taar7e"
                     /gene_synonym="TA14"
                     /coded_by="NM_175590.2:1..1077"
                     /db_xref="GeneID:294133"
                     /db_xref="RGD:631394"
ORIGIN      
        1 matddasfpw dqdsilsrdl lsasssqlcy enlnrscirs pyspgprlil havfgfsavl
       61 avcgnllvmt silhfrqlhs panflvasla cadllvgltv mpfsmvrsve gcwyfgdiyc
      121 kfhssfdvsf cycslfhlcf isvdryiavs dpliyptrft asvsgkcitf swflsiiysf
      181 sllytgasea gledlvsalt cvggcqlavn qswvfinfll flvptlvmmt vyskvfliak
      241 qqaqniekig kqtarasesy kdrvakrerk aaktlgitva afllswlpyf idsiidaflg
      301 fitptyvyei lvwiayynsa mnpliyaffy pwfrkaikli vtgkilrens satnlfpe
//
LOCUS       NP_571983                208 aa            linear   ROD 02-APR-2025
DEFINITION  fibroblast growth factor 6 precursor [Rattus norvegicus].
ACCESSION   NP_571983
VERSION     NP_571983.1
DBSOURCE    REFSEQ: accession NM_131908.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Cai,Q., Wu,G., Zhu,M., Ge,H., Xue,C., Zhang,Q., Cheng,B., Xu,S. and
            Wu,P.
  TITLE     FGF6 enhances muscle regeneration after nerve injury by relying on
            ERK1/2 mechanism
  JOURNAL   Life Sci 248, 117465 (2020)
   PUBMED   32105707
  REMARK    GeneRIF: FGF6 enhances muscle regeneration after nerve injury via
            ERK1/ERK2 activation.
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Sautter,N.B., Delaney,K.L., Hausman,F.A. and Trune,D.R.
  TITLE     Tissue remodeling in the acute otitis media mouse model
  JOURNAL   Int J Pediatr Otorhinolaryngol 75 (11), 1368-1371 (2011)
   PUBMED   21889218
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Ropiquet,F., Giri,D., Kwabi-Addo,B., Mansukhani,A. and Ittmann,M.
  TITLE     Increased expression of fibroblast growth factor 6 in human
            prostatic intraepithelial neoplasia and prostate cancer
  JOURNAL   Cancer Res 60 (15), 4245-4250 (2000)
   PUBMED   10945637
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Kastner,S., Elias,M.C., Rivera,A.J. and Yablonka-Reuveni,Z.
  TITLE     Gene expression patterns of the fibroblast growth factors and their
            receptors during myogenesis of rat satellite cells
  JOURNAL   J Histochem Cytochem 48 (8), 1079-1096 (2000)
   PUBMED   10898801
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Sakuma,K., Watanabe,K., Sano,M., Uramoto,I. and Totsuka,T.
  TITLE     Differential adaptation of growth and differentiation factor
            8/myostatin, fibroblast growth factor 6 and leukemia inhibitory
            factor in overloaded, regenerating and denervated rat muscles
  JOURNAL   Biochim Biophys Acta 1497 (1), 77-88 (2000)
   PUBMED   10838161
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Ornitz,D.M., Xu,J., Colvin,J.S., McEwen,D.G., MacArthur,C.A.,
            Coulier,F., Gao,G. and Goldfarb,M.
  TITLE     Receptor specificity of the fibroblast growth factor family
  JOURNAL   J Biol Chem 271 (25), 15292-15297 (1996)
   PUBMED   8663044
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Grass,S., Arnold,H.H. and Braun,T.
  TITLE     Alterations in somite patterning of Myf-5-deficient mice: a
            possible role for FGF-4 and FGF-6
  JOURNAL   Development 122 (1), 141-150 (1996)
   PUBMED   8565825
REFERENCE   8  (residues 1 to 208)
  AUTHORS   deLapeyriere,O., Ollendorff,V., Planche,J., Ott,M.O., Pizette,S.,
            Coulier,F. and Birnbaum,D.
  TITLE     Expression of the Fgf6 gene is restricted to developing skeletal
            muscle in the mouse embryo
  JOURNAL   Development 118 (2), 601-611 (1993)
   PUBMED   8223280
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Dinwiddie,S.H., Reich,T. and Cloninger,C.R.
  TITLE     Solvent use and psychiatric comorbidity
  JOURNAL   Br J Addict 85 (12), 1647-1656 (1990)
   PUBMED   2289066
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB079674.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB079674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..208
                     /product="fibroblast growth factor 6 precursor"
                     /note="fibroblast growth factor 7b"
                     /calculated_mol_wt=18536
     sig_peptide     1..42
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4271
     Region          84..208
                     /region_name="beta-trefoil_FGF6"
                     /note="FGF domain, beta-trefoil fold, found in fibroblast
                     growth factor 6 (FGF6) and similar proteins; cd23318"
                     /db_xref="CDD:467004"
     CDS             1..208
                     /gene="Fgf6"
                     /gene_synonym="Fgf7b"
                     /coded_by="NM_131908.1:1..627"
                     /db_xref="GeneID:170700"
                     /db_xref="RGD:620130"
ORIGIN      
        1 malgqrlfit msrgagrvqg tlqalvflgv lvgmvvpspa garangtlld srgwgtllsr
       61 sraglageis gvnwesgylv gikrqrrlyc nvgigfhlqv ppdgrisgth eenpysllei
      121 stvergvvsl fgvksalfia mnskgrlytt psfqdeckfr etllpnnyna yesdlyrgty
      181 ialskygrvk rgskvspimt vthflpri
//
LOCUS       NP_596891                586 aa            linear   ROD 02-APR-2025
DEFINITION  APOBEC1 complementation factor [Rattus norvegicus].
ACCESSION   NP_596891 XP_346580
VERSION     NP_596891.1
DBSOURCE    REFSEQ: accession NM_133400.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Rasheed,H., Stamp,L.K., Dalbeth,N. and Merriman,T.R.
  TITLE     Interaction of the GCKR and A1CF loci with alcohol consumption to
            influence the risk of gout
  JOURNAL   Arthritis Res Ther 19 (1), 161 (2017)
   PUBMED   28679452
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Dong,Z., Zhou,J., Jiang,S., Li,Y., Zhao,D., Yang,C., Ma,Y.,
            Wang,Y., He,H., Ji,H., Yang,Y., Wang,X., Xu,X., Pang,Y., Zou,H.,
            Jin,L. and Wang,J.
  TITLE     Effects of multiple genetic loci on the pathogenesis from serum
            urate to gout
  JOURNAL   Sci Rep 7, 43614 (2017)
   PUBMED   28252667
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Fossat,N., Tourle,K., Radziewic,T., Barratt,K., Liebhold,D.,
            Studdert,J.B., Power,M., Jones,V., Loebel,D.A. and Tam,P.P.
  TITLE     C to U RNA editing mediated by APOBEC1 requires RNA-binding protein
            RBM47
  JOURNAL   EMBO Rep 15 (8), 903-910 (2014)
   PUBMED   24916387
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Galloway,C.A., Ashton,J., Sparks,J.D., Mooney,R.A. and Smith,H.C.
  TITLE     Metabolic regulation of APOBEC-1 complementation factor trafficking
            in mouse models of obesity and its positive correlation with the
            expression of ApoB protein in hepatocytes
  JOURNAL   Biochim Biophys Acta 1802 (11), 976-985 (2010)
   PUBMED   20541607
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Galloway,C.A., Kumar,A., Krucinska,J. and Smith,H.C.
  TITLE     APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers
  JOURNAL   Biochem Biophys Res Commun 398 (1), 38-43 (2010)
   PUBMED   20541536
  REMARK    GeneRIF: N-terminal 320 amino acids of ACF retained RNA-binding
            selectivity and supported complementation of editing activity and
            in addition demonstrate a novel RNA-bridged multimerization of ACF.
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Sowden,M.P., Ballatori,N., Jensen,K.L., Reed,L.H. and Smith,H.C.
  TITLE     The editosome for cytidine to uridine mRNA editing has a native
            complexity of 27S: identification of intracellular domains
            containing active and inactive editing factors
  JOURNAL   J Cell Sci 115 (Pt 5), 1027-1039 (2002)
   PUBMED   11870221
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Lellek,H., Kirsten,R., Diehl,I., Apostel,F., Buck,F. and Greeve,J.
  TITLE     Purification and molecular cloning of a novel essential component
            of the apolipoprotein B mRNA editing enzyme-complex
  JOURNAL   J Biol Chem 275 (26), 19848-19856 (2000)
   PUBMED   10781591
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Mehta,A., Kinter,M.T., Sherman,N.E. and Driscoll,D.M.
  TITLE     Molecular cloning of apobec-1 complementation factor, a novel
            RNA-binding protein involved in the editing of apolipoprotein B
            mRNA
  JOURNAL   Mol Cell Biol 20 (5), 1846-1854 (2000)
   PUBMED   10669759
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Romanenko,A.V.
  TITLE     [Experience in the certification of veterinary specialists]
  JOURNAL   Veterinariia (12), 47-48 (1978)
   PUBMED   734901
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Dabrowski,Z., Gregorczyk,J., Samochowiec,L., Wojcicki,J.,
            Lawczynski,L., Antoszczyk,M., Chrzanowska-Ansilewska,K., Jurek,D.
            and Sych,Z.
  TITLE     [Effect of truncal vagotomy on the exocrine function of the
            pancreas in the dog]
  JOURNAL   Pol Tyg Lek 33 (28), 1093-1095 (1978)
   PUBMED   704405
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF290984.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346580.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF290984.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..586
                     /product="APOBEC1 complementation factor"
                     /note="APOBEC1-stimulating protein; APOBEC1
                     complementation factort; Apobec-1 complementation factor,
                     APOBEC-1 stimulating protein"
                     /calculated_mol_wt=64543
     Region          2..586
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQ94; propagated from
                     UniProtKB/Swiss-Prot (Q923K9.1)"
     CDS             1..586
                     /gene="A1cf"
                     /gene_synonym="A1cft; Acf; Apobec-1"
                     /coded_by="NM_133400.1:103..1863"
                     /db_xref="GeneID:170912"
                     /db_xref="RGD:619834"
ORIGIN      
        1 mesnhksgdg lsgtqkeaal ralvqrtgys lvqengqrky ggpppgwdtt ppergceifi
       61 gklprdlfed eliplcekig kiyemrmmmd fngnnrgyaf vtfsnkqeak naikqlnnye
      121 irngrllgvc asvdncrlfv ggipktkkre eilsemkkvt egvvdvivyp saadktknrg
      181 fafveyeshr aaamarrrll pgriqlwghp iavdwaepev evdedtmssv kilyvrnlml
      241 stseemieke fnsikpgave rvkkirdyaf vhfsnredav eamkalngkv ldgspievtl
      301 akpvdkdsyv rytrgtggrn tmlqeytypl shvydpttty lgapvfytpq ayaaipslhf
      361 patkghlsnr alirtpsvrg aagvrglggr gylaytglgr gyqvkgdkrq dklydllpgm
      421 eltpmntisl kpqgvklapq ileeicqknn wgqpvyqlhs aigqdqrqlf lykvtipala
      481 sqnpaihpft ppklsayvde akryaaehtl qtlgiptegg dagttaptat satvfpgyav
      541 psatapvsta qlkqavtlgq dlaayttyev yptfavttrg dgygtf
//
LOCUS       NP_071538                908 aa            linear   ROD 02-APR-2025
DEFINITION  metabotropic glutamate receptor 8 precursor [Rattus norvegicus].
ACCESSION   NP_071538 XP_347219
VERSION     NP_071538.1
DBSOURCE    REFSEQ: accession NM_022202.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Xie,Y., Chen,L., Chen,J., Luo,Y., Peng,Z., Zhang,H., Pan,Z. and
            Chen,Y.
  TITLE     Metabotropic Glutamate Receptor 8 Suppresses M1 Polarization in
            Microglia by Alleviating Endoplasmic Reticulum Stress and
            Mitochondrial Dysfunction
  JOURNAL   J Integr Neurosci 23 (2), 26 (2024)
   PUBMED   38419440
  REMARK    GeneRIF: Metabotropic Glutamate Receptor 8 Suppresses M1
            Polarization in Microglia by Alleviating Endoplasmic Reticulum
            Stress and Mitochondrial Dysfunction.
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Katona,L., Hartwich,K., Tomioka,R., Somogyi,J., Roberts,J.D.B.,
            Wagner,K., Joshi,A., Klausberger,T., Rockland,K.S. and Somogyi,P.
  TITLE     Synaptic organisation and behaviour-dependent activity of
            mGluR8a-innervated GABAergic trilaminar cells projecting from the
            hippocampus to the subiculum
  JOURNAL   Brain Struct Funct 225 (2), 705-734 (2020)
   PUBMED   32016558
  REMARK    GeneRIF: Synaptic organisation and behaviour-dependent activity of
            mGluR8a-innervated GABAergic trilaminar cells projecting from the
            hippocampus to the subiculum.
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Carmichael,R.E., Wilkinson,K.A., Craig,T.J., Ashby,M.C. and
            Henley,J.M.
  TITLE     MEF2A regulates mGluR-dependent AMPA receptor trafficking
            independently of Arc/Arg3.1
  JOURNAL   Sci Rep 8 (1), 5263 (2018)
   PUBMED   29588465
  REMARK    GeneRIF: This study shows via knockdown of endogenous MEF2A in
            primary neuronal culture, that MEF2A is specifically required for
            Group I metabotropic glutamate receptor (mGluR)-mediated GluA2
            internalisation, but does not regulate AMPAR expression or
            trafficking under basal conditions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Govea,R.M., Zhou,S. and Carlton,S.M.
  TITLE     Group III mGluR8 negatively modulates TRPA1
  JOURNAL   Neuroscience 334, 134-147 (2016)
   PUBMED   27497709
  REMARK    GeneRIF: Results show that group III mGluRs negatively modulate
            TRPA1 activity on cutaneous nociceptors. Furthermore, it is likely
            that this modulation occurs intracellularly at the level of the
            cAMP/PKA pathway. This study demonstrates that group III agonists
            may be effective in the treatment of mechanical hypersensitivity
            which can develop as a result of inflammation, nerve injury,
            chemotherapy and other disease states.
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Long,E.C., Aliev,F., Wang,J.C., Edenberg,H.J., Nurnberger,J. Jr.,
            Hesselbrock,V., Porjesz,B. and Dick,D.M.
  TITLE     Further Analyses of Genetic Association Between GRM8 and Alcohol
            Dependence Symptoms Among Young Adults
  JOURNAL   J Stud Alcohol Drugs 76 (3), 414-418 (2015)
   PUBMED   25978827
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Corti,C., Restituito,S., Rimland,J.M., Brabet,I., Corsi,M.,
            Pin,J.P. and Ferraguti,F.
  TITLE     Cloning and characterization of alternative mRNA forms for the rat
            metabotropic glutamate receptors mGluR7 and mGluR8
  JOURNAL   Eur J Neurosci 10 (12), 3629-3641 (1998)
   PUBMED   9875342
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Wu,S., Wright,R.A., Rockey,P.K., Burgett,S.G., Arnold,J.S.,
            Rosteck,P.R. Jr., Johnson,B.G., Schoepp,D.D. and Belagaje,R.M.
  TITLE     Group III human metabotropic glutamate receptors 4, 7 and 8:
            molecular cloning, functional expression, and comparison of
            pharmacological properties in RGT cells
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 88-97 (1998)
   PUBMED   9473604
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Shigemoto,R., Kinoshita,A., Wada,E., Nomura,S., Ohishi,H.,
            Takada,M., Flor,P.J., Neki,A., Abe,T., Nakanishi,S. and Mizuno,N.
  TITLE     Differential presynaptic localization of metabotropic glutamate
            receptor subtypes in the rat hippocampus
  JOURNAL   J Neurosci 17 (19), 7503-7522 (1997)
   PUBMED   9295396
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Saugstad,J.A., Kinzie,J.M., Shinohara,M.M., Segerson,T.P. and
            Westbrook,G.L.
  TITLE     Cloning and expression of rat metabotropic glutamate receptor 8
            reveals a distinct pharmacological profile
  JOURNAL   Mol Pharmacol 51 (1), 119-125 (1997)
   PUBMED   9016353
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Duvoisin,R.M., Zhang,C. and Ramonell,K.
  TITLE     A novel metabotropic glutamate receptor expressed in the retina and
            olfactory bulb
  JOURNAL   J Neurosci 15 (4), 3075-3083 (1995)
   PUBMED   7722646
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U63288.1.
            
            On Dec 17, 2003 this sequence version replaced XP_347219.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U63288.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..908
                     /product="metabotropic glutamate receptor 8 precursor"
                     /note="G protein-coupled receptor, family C, group 1,
                     member H; metabotropic glutamate receptor subtype 8b;
                     metabotropic glutamate receptor 8; glutamate receptor,
                     metabotropic 8"
                     /calculated_mol_wt=97971
     sig_peptide     1..33
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
                     /calculated_mol_wt=3914
     mat_peptide     34..908
                     /product="Metabotropic glutamate receptor 8.
                     /id=PRO_0000012943"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
                     /calculated_mol_wt=97971
     Region          40..504
                     /region_name="PBP1_mGluR_groupIII"
                     /note="ligand-binding domain of the group III metabotropic
                     glutamate receptor; cd06376"
                     /db_xref="CDD:380599"
     Site            order(53,68,71,154,156,226..227)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380599"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
     Site            order(110,113,161,164,187,252)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380599"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
     Site            452
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
     Region          512..562
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Site            565
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70579.1)"
     Region          582..892
                     /region_name="7tmC_mGluR8"
                     /note="metabotropic glutamate receptor 8 in group 3,
                     member of the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15454"
                     /db_xref="CDD:320570"
     Region          582..607
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320570"
     Site            584..608
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Site            order(585,588..589,592..593,595..596,630,634,637..638,646,
                     650)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320570"
     Region          619..640
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320570"
     Site            621..641
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Site            order(639,651..652,655..656,659,744,749,752..753,756,790,
                     793..794,797,801,814..815,818,821,825)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320570"
     Site            648..668
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Region          649..673
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320570"
     Region          695..715
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320570"
     Site            696..716
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Region          745..771
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320570"
     Site            747..768
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Region          779..802
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320570"
     Site            782..803
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     Region          812..837
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320570"
     Site            819..843
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70579.1)"
     CDS             1..908
                     /gene="Grm8"
                     /gene_synonym="Glur8; Gprc1h; mGlur; Mglur8; mGluR8b"
                     /coded_by="NM_022202.1:67..2793"
                     /db_xref="GeneID:60590"
                     /db_xref="RGD:619858"
ORIGIN      
        1 mvcegkrlas cpcfflltak fywiltmmqr thsqeyahsi rvdgdiilgg lfpvhakger
       61 gvpcgelkke kgihrleaml yaidqinkdp dllsnitlgv rildtcsrdt yaleqsltfv
      121 qaliekdasd vkcangdppi ftkpdkisgv igaaassvsi mvanilrlfk ipqisyasta
      181 pelsdntryd ffsrvvppds yqaqamvdiv talgwnyvst lasegnyges gveaftqisr
      241 eiggvciaqs qkipreprpg efekiikrll etpnaravim faneddirri leaakklnqs
      301 ghflwigsds wgskiapvyq qeeiaegavt ilpkrasidg fdryfrsrtl annrrnvwfa
      361 efweenfgck lgshgkrnsh ikkctgleri ardssyeqeg kvqfvidavy smayalhnmh
      421 kercpgyigl cprmvtidgk ellgyiravn fngsagtpvt fnengdapgr ydifqyqinn
      481 ksteykiigh wtnqlhlkve dmqwanreht hpasvcslpc kpgerkktvk gvpccwhcer
      541 cegynyqvde lscelcpldq rpninrtgcq ripiiklewh spwavvpvfi ailgiiattf
      601 vivtfvrynd tpivrasgre lsyvlltgif lcysitflmi aapdtiicsf rriflglgmc
      661 fsyaalltkt nrihrifeqg kksvtapkfi spasqlvitf slisvqllgv fvwfvvdpph
      721 tiidygeqrt ldpenargvl kcdisdlsli cslgysillm vtctvyaikt rgvpetfnea
      781 kpigftmytt ciiwlafipi ffgtaqsaek myiqtttltv smslsasvsl gmlympkvyi
      841 iifhpeqnvq krkrsfkavv taatmqskli qkgndrpnge vkselcesle tntsstktty
      901 isysnhsi
//
LOCUS       NP_783191                344 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 8b [Rattus norvegicus].
ACCESSION   NP_783191
VERSION     NP_783191.1
DBSOURCE    REFSEQ: accession NM_175601.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380195.1.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..344
                     /product="trace amine-associated receptor 8b"
                     /note="taR-7; taR-8b; trace amine receptor 8b; trace amine
                     receptor 7"
                     /calculated_mol_wt=37913
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y3.1)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y3.1)"
     Region          32..323
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          34..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320439"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Region          67..89
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320439"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Site            103..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Region          105..127
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320439"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Region          150..166
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320439"
     Region          194..217
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320439"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     Region          258..280
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320439"
     Region          291..316
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320439"
     Site            296..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y3.1)"
     CDS             1..344
                     /gene="Taar8b"
                     /gene_synonym="Ta7"
                     /coded_by="NM_175601.1:1..1035"
                     /db_xref="GeneID:319106"
                     /db_xref="RGD:631386"
ORIGIN      
        1 mtsnfsqatl qlcyenvnas ciktpyspgl rvllymvfgf gavlavcgnl lvvisvlhfk
       61 qlhspanfli aslasadflv gisvmpfsmv rsiescwyfg dtfcslhscc daafcysslf
      121 hlcfisvdry iavteplvyp tkftmsvsgi cisiswilpl vyssavfytg isatgienlv
      181 salncvggcq vainqdwvli sfllffiptl vmiilyskif lvakqqavki etsisgskge
      241 ssleshkarv akrerkaakt lgvtvmafmv swlpytidtl idafmgfitp ayvyeicgwi
      301 ayynsamnpl iyaffypwfr kaiklilsgk ilkghsstts lfse
//
LOCUS       NP_001254710             108 aa            linear   ROD 02-APR-2025
DEFINITION  prostate and testis expressed protein 2 [Rattus norvegicus].
ACCESSION   NP_001254710 XP_002729973 XP_003754447
VERSION     NP_001254710.1
DBSOURCE    REFSEQ: accession NM_001267781.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Rajesh,A. and Yenugu,S.
  TITLE     Genomic organization, tissue distribution and functional
            characterization of the rat Pate gene cluster
  JOURNAL   PLoS One 7 (3), e32633 (2012)
   PUBMED   22479333
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Levitin,F., Weiss,M., Hahn,Y., Stern,O., Papke,R.L., Matusik,R.,
            Nandana,S.R., Ziv,R., Pichinuk,E., Salame,S., Bera,T., Vincent,J.,
            Lee,B., Pastan,I. and Wreschner,D.H.
  TITLE     PATE gene clusters code for multiple, secreted TFP/Ly-6/uPAR
            proteins that are expressed in reproductive and neuron-rich tissues
            and possess neuromodulatory activity
  JOURNAL   J Biol Chem 283 (24), 16928-16939 (2008)
   PUBMED   18387948
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from HQ687476.1.
            
            On or before Jun 26, 2012 this sequence version replaced
            XP_003754447.1, XP_002729973.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ687476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840127 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..108
                     /product="prostate and testis expressed protein 2"
                     /calculated_mol_wt=12536
     Region          23..103
                     /region_name="TFP_LU_ECD_PATE2"
                     /note="extracellular domain (ECD) found in prostate and
                     testis expressed protein 2 (PATE2) and similar proteins;
                     cd23578"
                     /db_xref="CDD:467108"
     CDS             1..108
                     /gene="Pate2"
                     /coded_by="NM_001267781.1:1..327"
                     /db_xref="GeneID:100361465"
                     /db_xref="RGD:2320100"
ORIGIN      
        1 mlvivclfcq ywgvlnepek dlgtmcykck kyhlglcygl mrsctlkhrq scaaenfyil
       61 tnrgqsmyhy srlscmtnce dinflsferr telicckhss ycnlpmgl
//
LOCUS       NP_001160149             333 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 110 [Rattus norvegicus].
ACCESSION   NP_001160149
VERSION     NP_001160149.1
DBSOURCE    REFSEQ: accession NM_001166677.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362732.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..333
                     /product="taste receptor type 2 member 110"
                     /note="T2R10; T2R110; taste receptor type 2 member 10"
                     /calculated_mol_wt=38275
     Region          13..318
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          13..38
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          50..74
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          88..110
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          137..153
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          179..220
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          245..270
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     Region          282..307
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE8.2)"
     CDS             1..333
                     /gene="Tas2r110"
                     /coded_by="NM_001166677.1:1..1002"
                     /db_xref="GeneID:100310875"
                     /db_xref="RGD:2314263"
ORIGIN      
        1 mflhtikqrd iftliiiffv eitmgilgng fialvnivdw ikrrrissvd kilttlaltr
       61 liyawsmlif illfilgphl imrseiltsm gviwvvnnhf siwlatclgv fyflkianfs
      121 nslflylkwr vkkvvlmiiv vsliflilni fsleiydhfs idvyegnmsy slgdsthfpr
      181 iflfansskv flitnssqvf lpinslfmli pftvslvaff mlifslwkhh kkmevnakgp
      241 rdasttahik alqtglsfll lyaiyllfiv igilshkfmg gklilifdhi caivfpishs
      301 fvlilgnskl rrstlsvlrf lrcrskhihi mdp
//
LOCUS       NP_001100482             667 aa            linear   ROD 02-APR-2025
DEFINITION  non-receptor tyrosine-protein kinase TNK1 [Rattus norvegicus].
ACCESSION   NP_001100482 XP_001079627 XP_220614
VERSION     NP_001100482.1
DBSOURCE    REFSEQ: accession NM_001107012.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Hoare,K., Hoare,S., Smith,O.M., Kalmaz,G., Small,D. and Stratford
            May,W.
  TITLE     Kos1, a nonreceptor tyrosine kinase that suppresses Ras signaling
  JOURNAL   Oncogene 22 (23), 3562-3577 (2003)
   PUBMED   12789265
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Felschow,D.M., Civin,C.I. and Hoehn,G.T.
  TITLE     Characterization of the tyrosine kinase Tnk1 and its binding with
            phospholipase C-gamma1
  JOURNAL   Biochem Biophys Res Commun 273 (1), 294-301 (2000)
   PUBMED   10873601
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_220614.4, XP_001079627.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..667
                     /product="non-receptor tyrosine-protein kinase TNK1"
                     /EC_number="2.7.10.2"
                     /calculated_mol_wt=73139
     Region          16..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          120..380
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(122..125,128,130,146,148,181,196..199,245,249..250,
                     252,262..263)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <395..436
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Region          595..638
                     /region_name="UBA_like_SF"
                     /note="UBA domain-like superfamily; cl21463"
                     /db_xref="CDD:473871"
     Region          625..664
                     /region_name="UBA_like_SF"
                     /note="UBA domain-like superfamily; cl21463"
                     /db_xref="CDD:473871"
     CDS             1..667
                     /gene="Tnk1"
                     /coded_by="NM_001107012.1:52..2055"
                     /db_xref="GeneID:303247"
                     /db_xref="RGD:1310113"
ORIGIN      
        1 mlpeasslwl lrllrdvqla qfyrpileel nvtrpehfdf vrpedldnlg mgrpaqrrlt
       61 ealkryrsgv ksknwvykil ggfapeqkei ppysdslphl hepegglkcl ipegavcrge
      121 llgsgcfgvv hqglwtlpgg qsipvavksl rvgpegpmgt elgdflrevs vmmklehphv
      181 lrlhglvlgq plqmvmelap lgslharlta papmpplpvt llclflrqla gamaylgscg
      241 lvhrdlatrn lllasprkik vadfglvrpl ggargryvmg gprpipyawc apeslrqgaf
      301 saasdvwmfg vtlwemfsgg eepwagvppy lilqrlekdr arlpkpalcs ralyslalrc
      361 waphpadrpt fsnlegllqe awlsegrcvr evtepgalrm epgdpitiie gspdtttwkg
      421 qngrtlkvgn fpasavtlad lggspvthpv hrgspargek yrggtdgdre kavlqdlppa
      481 rnqrrkvplq rmkgisksle svlslgprpa gggssppelr rgctrawpqg ladlpprppd
      541 lpprppiics sqpiqphrvr pkreplhnhc tgapgsskvt ippggplsds ewqrkiveve
      601 lsvhgvtyqe cqmalrtmgg dvasairnlk vdqlfhlsnr sradcrrile hhhwdlsaas
      661 ryvlars
//
LOCUS       NP_647551                308 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 41 [Rattus norvegicus].
ACCESSION   NP_647551
VERSION     NP_647551.1
DBSOURCE    REFSEQ: accession NM_139335.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF240768.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF240768.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..308
                     /product="taste receptor type 2 member 41"
                     /note="T2R12; T2R41; taste receptor rT2R12"
                     /calculated_mol_wt=35879
     Region          7..296
                     /region_name="7tm_TAS2R41-like"
                     /note="mammalian taste receptor 2, subtype 41, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15018"
                     /db_xref="CDD:320146"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320146"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320146"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320146"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320146"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          179..202
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320146"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          227..252
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320146"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     Region          263..288
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320146"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKE7.1)"
     CDS             1..308
                     /gene="Tas2r126"
                     /gene_synonym="Tas2r41"
                     /coded_by="NM_139335.1:1..927"
                     /db_xref="GeneID:246219"
                     /db_xref="RGD:727853"
ORIGIN      
        1 mlstvsvffm sifvllcflg ilangfivlm lsrewlwrgr llpsdmills lgtsrfcqqc
       61 vglvnsfyys lhlveysrsl arqlislhmd flnsatfwfg twlsvlfcik ianfshpafl
      121 wlkwrfpalv pwlllgsilv sfivtlmffw gnhtvyqafl rrkfsgnttf kewnrrleid
      181 yfmplklvtt sipcslflvs illlinslrr hsqrmqhnah slqdpntqah sralkslisf
      241 lvlyalsyvs mvidatvvis sdnvwywpwq iilylcmsvh pfilitnnlk frgtfrqlll
      301 largfwvt
//
LOCUS       NP_001103066             310 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 125 [Rattus norvegicus].
ACCESSION   NP_001103066 NP_001078818 XP_001074563
VERSION     NP_001103066.1
DBSOURCE    REFSEQ: accession NM_001109596.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473964.2.
            
            On or before May 24, 2008 this sequence version replaced
            NP_001078818.1, XP_001074563.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..310
                     /product="taste receptor type 2 member 125"
                     /note="putative taste receptor T2R16; T2r125; taste
                     receptor type 2 member 16"
                     /calculated_mol_wt=35495
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          15..295
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET4.1)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          176..199
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ET4.1)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          224..249
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     Region          261..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ET4.1)"
     CDS             1..310
                     /gene="Tas2r125"
                     /coded_by="NM_001109596.1:4..936"
                     /db_xref="GeneID:690481"
                     /db_xref="RGD:1596030"
ORIGIN      
        1 mgivigiica fiiivqfiig nvangfialv niidwvkrrk islvdqiita laisridmlc
       61 stfliilits lypdlntavn mvkisnniwi vanhfsiwla tslsifyflk ianfsnyvfl
      121 clrwrlskvv svtlllslvl llmnilimnm hidtwsdgfk rnvsfgfrsk nctlffklal
      181 linttftcdp ftvsmvafll lifslwrhlk nmqyhakgsr dpstavhika lqmvvvfvlf
      241 ytffflslai qlwtseslek nnlfyvtlii tfpsvhscml ilrnsklrqa sllvlwwllc
      301 rskdiqtlvp
//
LOCUS       NP_695213                677 aa            linear   ROD 02-APR-2025
DEFINITION  polyunsaturated fatty acid lipoxygenase ALOX15B [Rattus
            norvegicus].
ACCESSION   NP_695213
VERSION     NP_695213.1
DBSOURCE    REFSEQ: accession NM_153301.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Wakabayashi,M., Yoshioka,T., Higashino,K., Numata,Y., Igarashi,Y.
            and Kihara,A.
  TITLE     Decreases in 15-lipoxygenase metabolites in Olmsted syndrome model
            rats
  JOURNAL   J Dermatol Sci 85 (3), 186-196 (2017)
   PUBMED   28024685
  REMARK    GeneRIF: Consistent with the decreases in the 15-LOX metabolites,
            expression levels of the genes that encode the 15-LOXs, Alox15 and
            Alox15b, were largely reduced in Olmsted syndrome model rats.
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Bender,G., Schexnaydre,E.E., Murphy,R.C., Uhlson,C. and
            Newcomer,M.E.
  TITLE     Membrane-dependent Activities of Human 15-LOX-2 and Its Murine
            Counterpart: IMPLICATIONS FOR MURINE MODELS OF ATHEROSCLEROSIS
  JOURNAL   J Biol Chem 291 (37), 19413-19424 (2016)
   PUBMED   27435673
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Green,A.R., Barbour,S., Horn,T., Carlos,J., Raskatov,J.A. and
            Holman,T.R.
  TITLE     Strict Regiospecificity of Human Epithelial 15-Lipoxygenase-2
            Delineates Its Transcellular Synthesis Potential
  JOURNAL   Biochemistry 55 (20), 2832-2840 (2016)
   PUBMED   27145229
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Kobe,M.J., Neau,D.B., Mitchell,C.E., Bartlett,S.G. and
            Newcomer,M.E.
  TITLE     The structure of human 15-lipoxygenase-2 with a substrate mimic
  JOURNAL   J Biol Chem 289 (12), 8562-8569 (2014)
   PUBMED   24497644
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Shen,T., Ma,J., Zhang,L., Yu,X., Liu,M., Hou,Y., Wang,Y., Ma,C.,
            Li,S. and Zhu,D.
  TITLE     Positive feedback-loop of telomerase reverse transcriptase and
            15-lipoxygenase-2 promotes pulmonary hypertension
  JOURNAL   PLoS One 8 (12), e83132 (2013)
   PUBMED   24376652
  REMARK    GeneRIF: Positive feedback-loop of TERT and 15-lipoxygenase-2
            promotes pulmonary hypertension.
            Erratum:[PLoS One. 2024 Aug 8;19(8):e0308871. doi:
            10.1371/journal.pone.0308871. PMID: 39116122]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Muga,S.J., Thuillier,P., Pavone,A., Rundhaug,J.E., Boeglin,W.E.,
            Jisaka,M., Brash,A.R. and Fischer,S.M.
  TITLE     8S-lipoxygenase products activate peroxisome proliferator-activated
            receptor alpha and induce differentiation in murine keratinocytes
  JOURNAL   Cell Growth Differ 11 (8), 447-454 (2000)
   PUBMED   10965849
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Jisaka,M., Kim,R.B., Boeglin,W.E. and Brash,A.R.
  TITLE     Identification of amino acid determinants of the positional
            specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2
  JOURNAL   J Biol Chem 275 (2), 1287-1293 (2000)
   PUBMED   10625675
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Kilty,I., Logan,A. and Vickers,P.J.
  TITLE     Differential characteristics of human 15-lipoxygenase isozymes and
            a novel splice variant of 15S-lipoxygenase
  JOURNAL   Eur J Biochem 266 (1), 83-93 (1999)
   PUBMED   10542053
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Jisaka,M., Kim,R.B., Boeglin,W.E., Nanney,L.B. and Brash,A.R.
  TITLE     Molecular cloning and functional expression of a phorbol
            ester-inducible 8S-lipoxygenase from mouse skin
  JOURNAL   J Biol Chem 272 (39), 24410-24416 (1997)
   PUBMED   9305900
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Brash,A.R., Boeglin,W.E. and Chang,M.S.
  TITLE     Discovery of a second 15S-lipoxygenase in humans
  JOURNAL   Proc Natl Acad Sci U S A 94 (12), 6148-6152 (1997)
   PUBMED   9177185
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF415240.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF415240.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMD00132270,
                                           SAMD00132302 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..677
                     /product="polyunsaturated fatty acid lipoxygenase ALOX15B"
                     /EC_number="1.13.11.33"
                     /note="arachidonate 15-lipoxygenase type II; arachidonate
                     15-lipoxygenase B; 15-LOX-2; 15-LOX-B; 15-lipoxygenase 2;
                     arachidonate 15-lipoxygenase, second type; linoleate
                     13-lipoxygenase 15-LOb"
                     /calculated_mol_wt=76015
     Region          2..122
                     /region_name="PLAT_LOX"
                     /note="PLAT domain of 12/15-lipoxygenase. As a unique
                     subfamily of the mammalian lipoxygenases, they catalyze
                     enzymatic lipid peroxidation in complex biological
                     structures via direct dioxygenation of phospholipids and
                     cholesterol esters of biomembranes and...; cd01753"
                     /db_xref="CDD:238851"
     Region          <233..668
                     /region_name="Lipoxygenase"
                     /note="pfam00305"
                     /db_xref="CDD:459754"
     CDS             1..677
                     /gene="Alox15b"
                     /coded_by="NM_153301.2:29..2062"
                     /db_xref="GeneID:266604"
                     /db_xref="RGD:628809"
ORIGIN      
        1 makfrvrvst geacgagtwd kvsvsivgth gesplvpldh lgkefsagae edfevtlpqd
       61 vgtvlmlrih kappeaplpl lsfppdawyc rwfelewlpg aalrfpcyqw legagelvlr
      121 egaakvswqd hhrtlqdqrq kelesrkdmy swktyiegwp hcldhetvkd ldlnikysam
      181 knakfffkaq saftelkfkg lldrtglwrs lremkrmfnf hntpaaeyvf ahwqedaffa
      241 sqflnglnpv lirrcrrlpe nfpvtdemva pvlgpgtslq aelekgslfl vdhgilsgvq
      301 tnvingkpqf saapmtllyq spgsgpllpi aiqlkqtpgp dnpiflpsdd kwdwllaktw
      361 vrnaefsihe althllhahl ipevfalatl rqlphchplf klliphtryt lhintlarel
      421 liapgkvvdk stglgiggfs dlikrnmeql sysvlclped irardvgdlp gyyyrddgmq
      481 iwsairsfvs eivdiyypsd asvrddqelq awvgeifseg flsqessgmp slldtqealv
      541 qyvtmviftc sakhaavsas qfdscvwmpn lppsmqlppp tskgqaspeg fiatlpavna
      601 tcdviialwl lskepgdrrp lghypdehft eevprrsiaa fqrkliqiss girkrnqsla
      661 lpytyldppl iensvsi
//
LOCUS       NP_059033               1141 aa            linear   ROD 02-APR-2025
DEFINITION  cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A [Rattus
            norvegicus].
ACCESSION   NP_059033 XP_001073892
VERSION     NP_059033.1
DBSOURCE    REFSEQ: accession NM_017337.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Skryabin,E.B., De Jong,K.A., Subramanian,H., Bork,N.I., Froese,A.,
            Skryabin,B.V. and Nikolaev,V.O.
  TITLE     CRISPR/Cas9 Knock-Out in Primary Neonatal and Adult Cardiomyocytes
            Reveals Distinct cAMP Dynamics Regulation by Various PDE2A and
            PDE3A Isoforms
  JOURNAL   Cells 12 (11), 1543 (2023)
   PUBMED   37296663
  REMARK    GeneRIF: CRISPR/Cas9 Knock-Out in Primary Neonatal and Adult
            Cardiomyocytes Reveals Distinct cAMP Dynamics Regulation by Various
            PDE2A and PDE3A Isoforms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Ercu,M., Mucke,M.B., Pallien,T., Marko,L., Sholokh,A.,
            Schachterle,C., Aydin,A., Kidd,A., Walter,S., Esmati,Y.,
            McMurray,B.J., Lato,D.F., Yumi Sunaga-Franze,D., Dierks,P.H.,
            Flores,B.I.M., Walker-Gray,R., Gong,M., Merticariu,C., Zuhlke,K.,
            Russwurm,M., Liu,T., Batolomaeus,T.U.P., Pautz,S., Schelenz,S.,
            Taube,M., Napieczynska,H., Heuser,A., Eichhorst,J., Lehmann,M.,
            Miller,D.C., Diecke,S., Qadri,F., Popova,E., Langanki,R.,
            Movsesian,M.A., Herberg,F.W., Forslund,S.K., Muller,D.N.,
            Borodina,T., Maass,P.G., Bahring,S., Hubner,N., Bader,M. and
            Klussmann,E.
  TITLE     Mutant Phosphodiesterase 3A Protects From Hypertension-Induced
            Cardiac Damage
  JOURNAL   Circulation 146 (23), 1758-1778 (2022)
   PUBMED   36259389
  REMARK    GeneRIF: Mutant Phosphodiesterase 3A Protects From
            Hypertension-Induced Cardiac Damage.
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Ercu,M., Marko,L., Schachterle,C., Tsvetkov,D., Cui,Y.,
            Maghsodi,S., Bartolomaeus,T.U.P., Maass,P.G., Zuhlke,K.,
            Gregersen,N., Hubner,N., Hodge,R., Muhl,A., Pohl,B., Illas,R.M.,
            Geelhaar,A., Walter,S., Napieczynska,H., Schelenz,S., Taube,M.,
            Heuser,A., Anistan,Y.M., Qadri,F., Todiras,M., Plehm,R., Popova,E.,
            Langanki,R., Eichhorst,J., Lehmann,M., Wiesner,B., Russwurm,M.,
            Forslund,S.K., Kamer,I., Muller,D.N., Gollasch,M., Aydin,A.,
            Bahring,S., Bader,M., Luft,F.C. and Klussmann,E.
  TITLE     Phosphodiesterase 3A and Arterial Hypertension
  JOURNAL   Circulation 142 (2), 133-149 (2020)
   PUBMED   32524868
  REMARK    GeneRIF: Phosphodiesterase 3A and Arterial Hypertension.
REFERENCE   4  (residues 1 to 1141)
  AUTHORS   Gershon,E., Maimon,I., Galiani,D., Elbaz,M., Karasenti,S. and
            Dekel,N.
  TITLE     High cGMP and low PDE3A activity are associated with oocyte meiotic
            incompetence
  JOURNAL   Cell Cycle 18 (20), 2629-2640 (2019)
   PUBMED   31401933
  REMARK    GeneRIF: High cGMP and low PDE3A activity are associated with
            oocyte meiotic incompetence.
REFERENCE   5  (residues 1 to 1141)
  AUTHORS   Berrisch,S., Ostermeyer,J., Kaever,V., Kalble,S.,
            Hilfiker-Kleiner,D., Seifert,R. and Schneider,E.H.
  TITLE     cUMP hydrolysis by PDE3A
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 390 (3), 269-280 (2017)
   PUBMED   27975297
  REMARK    GeneRIF: PDE3A is a low-affinity and high-velocity enzyme for
            hydrolysis of cUMP in cardiac myocytes.
REFERENCE   6  (residues 1 to 1141)
  AUTHORS   Richard,F.J., Tsafriri,A. and Conti,M.
  TITLE     Role of phosphodiesterase type 3A in rat oocyte maturation
  JOURNAL   Biol Reprod 65 (5), 1444-1451 (2001)
   PUBMED   11673261
REFERENCE   7  (residues 1 to 1141)
  AUTHORS   Shitsukawa,K., Andersen,C.B., Richard,F.J., Horner,A.K.,
            Wiersma,A., van Duin,M. and Conti,M.
  TITLE     Cloning and characterization of the cyclic guanosine
            monophosphate-inhibited phosphodiesterase PDE3A expressed in mouse
            oocyte
  JOURNAL   Biol Reprod 65 (1), 188-196 (2001)
   PUBMED   11420239
REFERENCE   8  (residues 1 to 1141)
  AUTHORS   Liu,H. and Maurice,D.H.
  TITLE     Expression of cyclic GMP-inhibited phosphodiesterases 3A and 3B
            (PDE3A and PDE3B) in rat tissues: differential subcellular
            localization and regulated expression by cyclic AMP
  JOURNAL   Br J Pharmacol 125 (7), 1501-1510 (1998)
   PUBMED   9884079
REFERENCE   9  (residues 1 to 1141)
  AUTHORS   Nagaoka,T., Shirakawa,T., Balon,T.W., Russell,J.C. and
            Fujita-Yamaguchi,Y.
  TITLE     Cyclic nucleotide phosphodiesterase 3 expression in vivo: evidence
            for tissue-specific expression of phosphodiesterase 3A or 3B mRNA
            and activity in the aorta and adipose tissue of
            atherosclerosis-prone insulin-resistant rats
  JOURNAL   Diabetes 47 (7), 1135-1144 (1998)
   PUBMED   9648839
REFERENCE   10 (residues 1 to 1141)
  AUTHORS   He,R., Komas,N., Ekholm,D., Murata,T., Taira,M., Hockman,S.,
            Degerman,E. and Manganiello,V.C.
  TITLE     Expression and characterization of deletion recombinants of two
            cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE-3)
  JOURNAL   Cell Biochem Biophys 29 (1-2), 89-111 (1998)
   PUBMED   9631240
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U38179.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001073892.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U38179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..1141
                     /product="cGMP-inhibited 3',5'-cyclic phosphodiesterase
                     3A"
                     /EC_number="3.1.4.17"
                     /note="cGMP-inhibited 3',5'-cyclic phosphodiesterase A;
                     CGI-PDE A; cyclic GMP-inhibited phosphodiesterase A;
                     cyclic nucleotide phosphodiesterase; phosphodiesterase 3A,
                     cGMP inhibited"
                     /calculated_mol_wt=124170
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Region          89..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            182..202
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Region          262..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14432; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Region          433..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14432; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Region          504..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14432; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0X4; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0X4; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Region          669..1141
                     /region_name="Interaction with SLFN12.
                     /evidence=ECO:0000250|UniProtKB:Q14432"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Region          751..1012
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     Region          1024..1062
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0X4; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Site            1036
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0X4; propagated from
                     UniProtKB/Swiss-Prot (Q62865.1)"
     Region          1098..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62865.1)"
     CDS             1..1141
                     /gene="Pde3a"
                     /gene_synonym="RNPDE3A"
                     /coded_by="NM_017337.1:1..3426"
                     /db_xref="GeneID:50678"
                     /db_xref="RGD:61942"
ORIGIN      
        1 mavrgeaaqd wakpglrgps papvargdhr crggspsspr gsgccwrala lqplrrspql
       61 ssalcagsls vllallvrlv ggevggeles sqeaaaeeee eegarggvfp gprggapggg
      121 aqlspwlqpa allfsllcaf fwmglcllra gvrlplaval laaccageal vqlslgvgdg
      181 rllslpaagv llsclggatw lvlrlrlgvl mvaltsalrt valvslerfk vawrpylayl
      241 aavlglllar yaeqllpqcs gpapprerfg sqssartkee ipgwkrrrrs ssvvagemsg
      301 cggkshrrts lpcipreqlm ghsewdhkrg srgsqsgtsv tvdiavmgea hglitdllad
      361 pslppnvcts lravsnllst qltfqaihkp rvnptvtfse nytcsdseeg lekdklaipk
      421 rlrrslppgl lrrvsstwtt ttsatglptl epapvrrdrs asikpheaps psavnpdswn
      481 apvlmtltks rsftssyavs aanhvkakkq nrpggldkis pvpspssspp qgsptsspvs
      541 giasvqfpes pevttkrgpg shraltytqs apdlspqipp spvicsscgr pysqgnpadg
      601 psersgpamq kpnrtddtsq vtsdyetnnn sdssdilqnd eeaecqrepl rkasacgtyt
      661 pqtmifldkp ilapeplvmd nldsimdqln twnfpifdlv enigrkcgri lsqvsyrlfe
      721 dmglfeafki pvrefmnyfh aleigyrdip yhnrihatdv lhavwylttq pipglpsvig
      781 dhgsasdsds dsgfthghmg yvfskayhvp ddkygclsgn ipalelmaly vaaamhdydh
      841 pgrtnaflva tsapqavlyn drsvlenhha aaawnlfmsr peynflvnld hvefkhfrfl
      901 vieailatdl kkhfdfvakf nakvnddvgi dwtnendrll vcqmciklad ingpakckdl
      961 hlrwtegias efyeqgdeea slglpispfm drsapqlanl qesfishivg plchsydsag
     1021 lmpgkwvdds ddsgdtddpe eeeeeaetph eeetcensea prkksfkrrr iycqitqhll
     1081 qnhmmwkkvi eeeqclsgte nqapdqaplq hsseqiqaik eeeeekgkpr aeetlapqpd
     1141 l
//
LOCUS       NP_001004129             103 aa            linear   ROD 02-APR-2025
DEFINITION  stefin-3 [Rattus norvegicus].
ACCESSION   NP_001004129 XP_579128
VERSION     NP_001004129.1
DBSOURCE    REFSEQ: accession NM_001004129.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000376.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579128.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..103
                     /product="stefin-3"
                     /function="cysteine protease inhibitor"
                     /note="stefin A2"
                     /calculated_mol_wt=11479
     Region          10..97
                     /region_name="Cystatin"
                     /note="Cystatin domain; pfam00031"
                     /db_xref="CDD:425431"
     Site            order(10,52..54,56)
                     /site_type="active"
                     /note="putative proteinase inhibition site [active]"
                     /db_xref="CDD:238002"
     CDS             1..103
                     /gene="Stfa2l1"
                     /gene_synonym="Stfa2"
                     /coded_by="NM_001004129.1:1..312"
                     /db_xref="GeneID:408214"
                     /db_xref="RGD:1303106"
ORIGIN      
        1 mnqdtivitg glsearpatp eiqeiadkvk tlleektngk yekfeaiqyk vqvvagrnyf
       61 ikmdvghgcf thikvfqgls gkddlelsgy qtnktkndel thf
//
LOCUS       NP_001074407             309 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 124 [Rattus norvegicus].
ACCESSION   NP_001074407 XP_001074538
VERSION     NP_001074407.1
DBSOURCE    REFSEQ: accession NM_001080938.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362745.1.
            
            On Jan 31, 2007 this sequence version replaced XP_001074538.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..309
                     /product="taste receptor type 2 member 124"
                     /note="putative taste receptor T2R25; T2R124; taste
                     receptor type 2 member 25"
                     /calculated_mol_wt=35655
     Region          7..291
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          9..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          45..66
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          81..103
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          130..146
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          174..197
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES5.1)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          225..247
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     Site            255
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ES5.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ES5.1)"
     CDS             1..309
                     /gene="Tas2r124"
                     /coded_by="NM_001080938.1:1..930"
                     /db_xref="GeneID:690472"
                     /db_xref="RGD:1596038"
ORIGIN      
        1 mvsvlhsist iiiiaefvwg nlsnglivlk ncldwinike lstldqilil laisrisliw
       61 etllmwvkdk lissitieel kmimfsfmls shfslwlata lstfylfria ncswqiflyl
      121 kwrlkhlivq mllgsvmfli aniiqititl ekrfyqykgn tsvnsiqnef alliemmlfn
      181 mtifsvipfl lalisfflli fslwkhlqrm qlnsredrdp stkahrnalg imvsflllyt
      241 myvlsllisw iaqknqselv hiicmitsll npsvhssili lgnfklkqss lcilrhlgcr
      301 lksqntptt
//
LOCUS       NP_001040578             461 aa            linear   ROD 02-APR-2025
DEFINITION  ribonuclease/angiogenin inhibitor [Rattus norvegicus].
ACCESSION   NP_001040578
VERSION     NP_001040578.1
DBSOURCE    REFSEQ: accession NM_001047113.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Zhao,C.F., Liu,Y., Que,H.P., Yang,S.G., Liu,Z.Q., Weng,X.C.,
            Hui,H.D. and Liu,S.J.
  TITLE     SCIRR39 promotes differentiation of oligodendrocyte precursor cells
            and regulates expression of myelin-associated inhibitory factors
  JOURNAL   J Mol Neurosci 50 (3), 533-541 (2013)
   PUBMED   23440710
  REMARK    GeneRIF: The results indicate the important role of SCIRR39 either
            in oligodendrocyte precursor cell differentiation or in axon
            myelination.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhao,C.F., Liu,Y., Ni,Y.L., Yang,J.W., Hui,H.D., Sun,Z.B. and
            Liu,S.J.
  TITLE     SCIRR39 promotes neurite extension via RhoA in NGF-induced PC12
            cells
  JOURNAL   Dev Neurosci 35 (5), 373-383 (2013)
   PUBMED   24021527
  REMARK    GeneRIF: Our results indicated that SCIRR39 increased the neurite
            extension in NGF-treated PC12 cells via RhoA, suggesting that
            SCIRR39 contributes to the regeneration of neuron injury by
            specifically altering the differentiation program.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY240937.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY240937.2 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
     Protein         1..461
                     /product="ribonuclease/angiogenin inhibitor"
                     /note="ribonuclease inhibitor"
                     /calculated_mol_wt=49741
     Region          6..325
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     Region          6..29
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(8,10,13,15,30,33,35,38,40,58,61,63,66,68,87,90,92,
                     95,97,115,118,120,123,125,144,147,149,152,154,172,175,177,
                     180,182,201,204,206,209,211,229,232,234,237,239,258,261,
                     263,266,268,286,289,291,294,296,315,318,320,323,325)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          30..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(36..37,94,151,179,236,262,264,290,319)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          58..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          87..114
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          115..143
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          144..171
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          201..228
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <228..430
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          229..257
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          258..278
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          286..314
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          315..338
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          343..367
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          372..399
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..461
                     /gene="LOC641544"
                     /coded_by="NM_001047113.1:1..1386"
                     /db_xref="GeneID:641544"
                     /db_xref="RGD:1590758"
ORIGIN      
        1 msldiqsldi qceelsdarw aellpllqqc qvvrlddcgl tearckdiss alrvnpalae
       61 lnlrsnelgd vgvhcvlqgl qtpsckiqkl slqnccltga gcgvlsstlr tlptlqelhl
      121 sdnllgdagl qllceglldp qcrleklqle ycslsaasce plasvlrakp dfkeltvsnn
      181 dineagvrvl cqglkdspcq lealklescg vtsdncrdlc givaskaslr elalgsnklg
      241 dvgmaelcpg llhpssrlrt lwiwecgita kgcgdlcrvl rakeslkels lagnelgdeg
      301 arllcetlle pgcqleslwv kscsftaacc shfssvlaqn rfllelqisn nrledagvae
      361 lcqgpgqpgs vlrvlwladc dvsdsscssl aatllanhsl reldlsnncl gdagilqlve
      421 svrqpgclle qlvlydiyws eemedrlqal ekdkpslrvi s
//
LOCUS       NP_001002284             353 aa            linear   ROD 02-APR-2025
DEFINITION  mas-related G-protein coupled receptor member B5 [Rattus
            norvegicus].
ACCESSION   NP_001002284 XP_579074
VERSION     NP_001002284.1
DBSOURCE    REFSEQ: accession NM_001002284.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zylka,M.J., Dong,X., Southwell,A.L. and Anderson,D.J.
  TITLE     Atypical expansion in mice of the sensory neuron-specific Mrg G
            protein-coupled receptor family
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 10043-10048 (2003)
   PUBMED   12909716
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF518243.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579074.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..353
                     /product="mas-related G-protein coupled receptor member
                     B5"
                     /note="MAS-related gene B5"
                     /calculated_mol_wt=39994
     Site            26
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TN44.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          64..334
                     /region_name="7tmA_MrgprB"
                     /note="mas-related G protein-coupled receptor subtype B,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15107"
                     /db_xref="CDD:320235"
     Region          65..91
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320235"
     Site            68..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          97..123
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320235"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Site            order(118,121..122,133..138,140..141,144,187,189..193,216,
                     219..221,223..225,227..228,265,268..269,271..272,275,
                     287..289,292,295..296)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320235"
     Site            132..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          133..161
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320235"
     Region          173..193
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320235"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          216..241
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320235"
     Region          245..275
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320235"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          286..310
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320235"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     Region          333..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TN44.1)"
     CDS             1..353
                     /gene="Mrgprb5"
                     /gene_synonym="MrgB5"
                     /coded_by="NM_001002284.1:1..1062"
                     /db_xref="GeneID:404644"
                     /db_xref="RGD:738052"
ORIGIN      
        1 mpdsptesyg pdreyhvfis lflcrntsgk flsvgpatpg wsinntvvke nyyteklsci
       61 itfntlnflt atisvvgtag natvlrllgf hmhryafsvy vfnlagadfl ylctqtvysl
      121 ecvlqfdnsy fyflltilmf aylaalcmip aisterclsv twpiwyhcqr prhtsatvca
      181 lfwafslllr lllgqgcgfl fgkydyyfcr ycsfittafl ivlfvvpfvs slamltkiic
      241 gshripvtrf yvtiavtvlv ftffglpvgi islllprivv frgvfyiyki vtflysvncc
      301 anpiiyflig sirhhrlqrq slklllqram qdtpeeeggv kgpsqksnel eiv
//
LOCUS       NP_001008816             452 aa            linear   ROD 02-APR-2025
DEFINITION  keratin, type I cytoskeletal 42 [Rattus norvegicus].
ACCESSION   NP_001008816 XP_579213
VERSION     NP_001008816.1
DBSOURCE    REFSEQ: accession NM_001008816.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004051.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004051.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN12840122,
                                           SAMN16418971 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..452
                     /product="keratin, type I cytoskeletal 42"
                     /note="K42; CK-42; cytokeratin-42; type I keratin KA22"
                     /calculated_mol_wt=50082
     Region          4..93
                     /region_name="Head. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          93..404
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          94..129
                     /region_name="Coil 1A. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          130..147
                     /region_name="Linker 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          148..239
                     /region_name="Coil 1B. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          240..262
                     /region_name="Linker 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          263..401
                     /region_name="Coil 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     Region          402..452
                     /region_name="Tail. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU7.1)"
     CDS             1..452
                     /gene="Krt42"
                     /gene_synonym="Ka22"
                     /coded_by="NM_001008816.1:1..1359"
                     /db_xref="GeneID:450231"
                     /db_xref="RGD:1359182"
ORIGIN      
        1 masttsirqf stsgsvkglc apgmgfsrms svriggacra psllgggscs nmsvtssrfs
       61 aglggsyggg ytcslgggfg ssfgvsdall ggseketmqn lndrlatyld rvraleeant
      121 dlevkirewy kkqgpgpard yspyfktied lrnkilaati dnasivlqid narlaaddfr
      181 tkyetelnlr msveadingl rrvldeltla radlemqiet lkeelaylkk nheeemnalr
      241 gqvggdvnve mdaapgvdls rilnemrdqy ekmaeknrkd aeewfftkte elnrevatnt
      301 ealqssrtei telrrsvqnl eielqsqlsm kaslenslae tearygaqla qlqglissme
      361 qqlcelrcdm erqnheyqvl ldvktrleqe iatyrrlleg edahlatqys sslasqasre
      421 gtvtsrqvrt iveevqdgkv vssreqvhrs th
//
LOCUS       NP_001129159             223 aa            linear   ROD 02-APR-2025
DEFINITION  killer cell lectin-like receptor subfamily B member 1A [Rattus
            norvegicus].
ACCESSION   NP_001129159
VERSION     NP_001129159.1
DBSOURCE    REFSEQ: accession NM_001135687.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Kveberg,L., Dai,K.Z., Westgaard,I.H., Daws,M.R., Fossum,S.,
            Naper,C. and Vaage,J.T.
  TITLE     Two major groups of rat NKR-P1 receptors can be distinguished based
            on chromosomal localization, phylogenetic analysis and Clr ligand
            binding
  JOURNAL   Eur J Immunol 39 (2), 541-551 (2009)
   PUBMED   19130483
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from FJ158033.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ158033.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Rattus norvegicus"
                     /strain="AUG"
                     /db_xref="taxon:10116"
                     /chromosome="4"
     Protein         1..223
                     /product="killer cell lectin-like receptor subfamily B
                     member 1A"
                     /note="killer cell lectin-like receptor subfamily B member
                     1A-like"
                     /calculated_mol_wt=24460
     Region          94..212
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            order(151,178,196,198..199)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     CDS             1..223
                     /gene="RGD2301395"
                     /gene_synonym="Kl4b1a; Klrb1al"
                     /coded_by="NM_001135687.1:1..672"
                     /db_xref="GeneID:100190921"
                     /db_xref="RGD:2301395"
ORIGIN      
        1 mdtarvylsl kpsktaagaq cvsppslppd acrcprshrl alklscagli llvlalvgms
       61 ilvrvlvqkp svepcrvliq enlsktdspa klkcpkdwls hrdkcfhvsq asntwkesla
      121 dcdgkgatll liqsqeelrf lrylikgkgs sfwiglsytl pdrnwkwing stlnpdvlsi
      181 fgdtkqnsca svsqdkvlse scssdnlwic qkelkcecmc ngs
//
LOCUS       NP_001008750             491 aa            linear   ROD 02-APR-2025
DEFINITION  type I keratin KA11 [Rattus norvegicus].
ACCESSION   NP_001008750 XP_579201
VERSION     NP_001008750.1
DBSOURCE    REFSEQ: accession NM_001008750.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK004048.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579201.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK004048.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, longest
                                      protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..491
                     /product="type I keratin KA11"
                     /calculated_mol_wt=52465
     Region          133..441
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     CDS             1..491
                     /gene="Ka11"
                     /coded_by="NM_001008750.1:1..1476"
                     /db_xref="GeneID:450226"
                     /db_xref="RGD:1359526"
ORIGIN      
        1 matcnrqfts sscwkgscgi gggfsrmssv laggscraps tyggmsvtss rfssrgacgi
       61 gggyggrfss ssfgggiggg lgggiggglg ggiggglggg iggglggglg ggiggglggg
      121 igdglgngll vgsekvtmqn lndrlsnymd qvralekans dlevkirdwy qrqrptelkd
      181 yrshfrtied lksqimtatq enaqtnlqid narlaandfr tkyeselfls qsveidvqni
      241 tkvlddlgsi gadlemqiqs lteelaalnr nhqeemlalr gqtggdvnve mdaapgvdls
      301 rilnemrdqy eqmaeknrrd veawfqskte elnqevasnh eliqsgrsev selrrvfqgl
      361 eielqsqlsv kaslenslee tkgrycvqls qiqgligsle eqlaqlrcem eqqsqeynil
      421 ldvktrleqe iatyrrllds envhssssqh ssgqsyssge vfssssrqpr silkdqgsts
      481 fsqsqsqssg n
//
LOCUS       NP_783192                338 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 9 [Rattus norvegicus].
ACCESSION   NP_783192
VERSION     NP_783192.1
DBSOURCE    REFSEQ: accession NM_175602.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Murtazina,R.Z., Zhukov,I.S., Korenkova,O.M., Popova,E.A.,
            Kuvarzin,S.R., Efimova,E.V., Kubarskaya,L.G., Batotsyrenova,E.G.,
            Zolotoverkhaya,E.A., Vaganova,A.N., Apryatin,S.A., Alenina,N.V. and
            Gainetdinov,R.R.
  TITLE     Genetic Deletion of Trace-Amine Associated Receptor 9 (TAAR9) in
            Rats Leads to Decreased Blood Cholesterol Levels
  JOURNAL   Int J Mol Sci 22 (6), 2942 (2021)
   PUBMED   33799339
  REMARK    GeneRIF: Genetic Deletion of Trace-Amine Associated Receptor 9
            (TAAR9) in Rats Leads to Decreased Blood Cholesterol Levels.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Ferrero,D.M., Wacker,D., Roque,M.A., Baldwin,M.W., Stevens,R.C. and
            Liberles,S.D.
  TITLE     Agonists for 13 trace amine-associated receptors provide insight
            into the molecular basis of odor selectivity
  JOURNAL   ACS Chem Biol 7 (7), 1184-1189 (2012)
   PUBMED   22545963
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380190.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..338
                     /product="trace amine-associated receptor 9"
                     /note="taR-3; taR-9; trace amine receptor 9; trace amine
                     receptor 3"
                     /calculated_mol_wt=37715
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          24..312
                     /region_name="7tmA_TAAR6_8_9"
                     /note="trace amine-associated receptors 6, 8, and 9,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15316"
                     /db_xref="CDD:320439"
     Region          24..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320439"
     Site            24..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          57..83
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320439"
     Site            59..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          95..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320439"
     Site            96..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Site            order(98,102..103,106..107,182,188,191..192,195,261,
                     264..265,268,283,287,291)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320439"
     Region          137..160
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320439"
     Site            139..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          164..177
                     /region_name="Extracellular Loop 2 (ECL2).
                     /evidence=ECO:0000250|UniProtKB:Q5QD04"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          184..213
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320439"
     Site            187..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          241..271
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320439"
     Site            247..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     Region          280..305
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320439"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y6.1)"
     CDS             1..338
                     /gene="Taar9"
                     /gene_synonym="Ta3"
                     /coded_by="NM_175602.1:1..1017"
                     /db_xref="GeneID:319107"
                     /db_xref="RGD:631383"
ORIGIN      
        1 melcyenvng scikssyspw prailyavlg lgallavfgn llvitailhf kqlhtptnfl
       61 vaslacadfl vgvtvmpfst vrsvegcwyf gdtyckfhtc fdtsfcfasl fhlccisidr
      121 yvavtdplty ptkftisvsg vcialswffs vtysfsifyt ganeegieel vvaltcvggc
      181 qaplnqnwvl lcfllfflpt vvmvflygri flvakqqark iegsanqpqa ssesykerva
      241 rrerkaaktl giamaaflvs wlpyiidavi daymnfitpa yvyeilvwcv yynsamnpli
      301 yaffypwfrk aiklivsgkv fradssrtnl fseeagag
//
LOCUS       NP_001019976             147 aa            linear   ROD 02-APR-2025
DEFINITION  hemoglobin subunit epsilon [Rattus norvegicus].
ACCESSION   NP_001019976 XP_577830
VERSION     NP_001019976.1
DBSOURCE    REFSEQ: accession NM_001024805.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Satoh,H., Inokuchi,N., Nagae,Y. and Okazaki,T.
  TITLE     Molecular cloning and characterization of two sets of alpha-theta
            genes in the rat alpha-like globin gene cluster
  JOURNAL   Gene 230 (1), 91-99 (1999)
   PUBMED   10196478
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Iwahara,S.I., Abe,Y. and Okazaki,T.
  TITLE     Identification of five embryonic hemoglobins of rat and ontogeny of
            their constituent globins during fetal development
  JOURNAL   J Biochem 119 (2), 360-366 (1996)
   PUBMED   8882731
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Kohli-Kumar,M., Zwerdling,T. and Rucknagel,D.L.
  TITLE     Hemoglobin F-Cincinnati, alpha 2G gamma 2 41(C7) Phe-->Ser in a
            newborn with cyanosis
  JOURNAL   Am J Hematol 49 (1), 43-47 (1995)
   PUBMED   7741137
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Miller,B.A., Olivieri,N., Salameh,M., Ahmed,M., Antognetti,G.,
            Huisman,T.H., Nathan,D.G. and Orkin,S.H.
  TITLE     Molecular analysis of the high-hemoglobin-F phenotype in Saudi
            Arabian sickle cell anemia
  JOURNAL   N Engl J Med 316 (5), 244-250 (1987)
   PUBMED   2432426
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X56327.1.
            
            On Jun 10, 2005 this sequence version replaced XP_577830.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680427,
                              SAMN06680431 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..147
                     /product="hemoglobin subunit epsilon"
                     /note="epsilon 2 globin; globin b3"
                     /calculated_mol_wt=16257
     Region          8..146
                     /region_name="Hb-beta-like"
                     /note="Hemoglobin beta, gamma, delta, epsilon, and related
                     Hb subunits; cd08925"
                     /db_xref="CDD:381262"
     Site            order(31,34..35,38,41,98,100,103,109,112..113,116..117,
                     120,123..125,128..129,132)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381262"
     Site            order(32,42..43,64,67..68,71,89,93,97,99,103..104,107,142)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381262"
     CDS             1..147
                     /gene="Hbe2"
                     /gene_synonym="Glnb3"
                     /coded_by="NM_001024805.1:1..444"
                     /db_xref="GeneID:502359"
                     /db_xref="RGD:1564524"
ORIGIN      
        1 mvhftaeeka aiisiwekvd leklggetlg rllivypwtq rffdkfgnls sapaimgnpq
       61 irahgkkvlv slglavenmd nlketfahls elhcdklhvd penfkllgnv lvivlssyfg
      121 keftaevqaa wqklvagvat alshkyh
//
LOCUS       NP_001101446             362 aa            linear   ROD 02-APR-2025
DEFINITION  cytosolic 5'-nucleotidase 1A [Rattus norvegicus].
ACCESSION   NP_001101446 XP_001055008 XP_233494
VERSION     NP_001101446.1
DBSOURCE    REFSEQ: accession NM_001107976.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Kulkarni,S.S., Karlsson,H.K., Szekeres,F., Chibalin,A.V., Krook,A.
            and Zierath,J.R.
  TITLE     Suppression of 5'-nucleotidase enzymes promotes AMP-activated
            protein kinase (AMPK) phosphorylation and metabolism in human and
            mouse skeletal muscle
  JOURNAL   J Biol Chem 286 (40), 34567-34574 (2011)
   PUBMED   21873433
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Kaizer,R.R., Maldonado,P.A., Spanevello,R.M., Correa,M.C.,
            Goncalves,J.F., Becker,L.V., Morsch,V.M. and Schetinger,M.R.
  TITLE     The effect of aluminium on NTPDase and 5'-nucleotidase activities
            from rat synaptosomes and platelets
  JOURNAL   Int J Dev Neurosci 25 (6), 381-386 (2007)
   PUBMED   17686601
  REMARK    GeneRIF: Al increases NTPDase and 5'-nucleotidase activities, in
            synaptosomal fractions and platelets. Thus, we suggest that
            platelets could be sensitive peripheral markers of Al toxicity of
            the central nervous system.
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Mackiewicz,M., Nikonova,E.V., Zimmerman,J.E., Galante,R.J.,
            Zhang,L., Cater,J.R., Geiger,J.D. and Pack,A.I.
  TITLE     Enzymes of adenosine metabolism in the brain: diurnal rhythm and
            the effect of sleep deprivation
  JOURNAL   J Neurochem 85 (2), 348-357 (2003)
   PUBMED   12675911
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Hunsucker,S.A., Spychala,J. and Mitchell,B.S.
  TITLE     Human cytosolic 5'-nucleotidase I: characterization and role in
            nucleoside analog resistance
  JOURNAL   J Biol Chem 276 (13), 10498-10504 (2001)
   PUBMED   11133996
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_233494.2, XP_001055008.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760384 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..362
                     /product="cytosolic 5'-nucleotidase 1A"
                     /EC_number="3.1.3.5"
                     /calculated_mol_wt=40400
     Region          78..350
                     /region_name="5-nucleotidase"
                     /note="5'-nucleotidase; pfam06189"
                     /db_xref="CDD:461846"
     CDS             1..362
                     /gene="Nt5c1a"
                     /coded_by="NM_001107976.1:68..1156"
                     /db_xref="GeneID:313574"
                     /db_xref="RGD:1310908"
ORIGIN      
        1 meprqppear epgpgaetaa vprweeaktf ydnlspkkkp kspkpqnavt iavssralfr
       61 mdeeqriyte qgveeyvryq lehenepfsp gpafpfvkal eavnkqlrel ypdsedifdi
      121 vlmtnnhaqv gvrlinsinh ydlfierfcm tggnspicyl kayhtnlyls adaekvreai
      181 degiaaatif spskdvvvsq sqlrvafdgd avlfsdeser ivkahgldrf fehekahenk
      241 plaqgplkgf lealgrlqkk fyskglrlec pirtylvtar saassgaral ktlrswglet
      301 dealflagap kgpllekirp hiffddqmfh vagaqemgtv aahvpygvaq nprrekqslg
      361 aq
//
LOCUS       NP_996730                368 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class Ib, locus Cl precursor [Rattus norvegicus].
ACCESSION   NP_996730 XP_003754722
VERSION     NP_996730.1
DBSOURCE    REFSEQ: accession NM_206848.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Lambracht,D. and Wonigeit,K.
  TITLE     Sequence analysis of the promoter regions of the classical class I
            gene RT1.Al and two other class I genes of the rat MHC
  JOURNAL   Immunogenetics 41 (6), 375-379 (1995)
   PUBMED   7759134
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tiedke,J., Bielski,C., Kinas,J. and Marquardt,B.
  TITLE     Dialysis treatment: are patients aware of their options?
  JOURNAL   Nephrol News Issues 6 (11), 52-53 (1992)
   PUBMED   1300430
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF025308.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003754722.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20"
     Protein         1..368
                     /product="RT1 class Ib, locus Cl precursor"
                     /note="MHC class I antigen; RT1 class Ib gene,
                     RT1-C-region (CI)"
                     /calculated_mol_wt=39037
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     Region          22..200
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Region          202..296
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          220..224
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          235..239
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          266..270
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          277..282
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          292..295
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          340..367
                     /region_name="MHC_I_C"
                     /note="MHC_I C-terminus; pfam06623"
                     /db_xref="CDD:461964"
     CDS             1..368
                     /gene="RT1-Cl"
                     /gene_synonym="RT1.A"
                     /coded_by="NM_206848.1:1..1107"
                     /db_xref="GeneID:24977"
                     /db_xref="RGD:3472"
ORIGIN      
        1 maprtlllll aaalaptqvr agshslryfh tavsrpglge prfiivgyvd dtefvrydsd
       61 aenpryeprv gwmeregpey weretlmvke neqvyrvslr tllryynqse ggshtiqwms
      121 gcdvgsdgsl lrgydqfayd grdylalned lktwmaadta aqmtrnkwdq ageaerhkay
      181 lqgtcvewlr rylelgketl lrsdppkahv tlhprpegdv tlrcwalgfy pagifltwll
      241 ngedltqdme lvetrpagdg tfqkwasvvv plgkeqnytc lveheglpdp ltlrweapps
      301 tdpnmettvi yvvvgavvit gavtmigall tvvrgrkrnt ggkvgvytpa pgkdssessd
      361 vslpdcka
//
LOCUS       NP_445857                396 aa            linear   ROD 02-APR-2025
DEFINITION  potassium channel subfamily K member 9 precursor [Rattus
            norvegicus].
ACCESSION   NP_445857
VERSION     NP_445857.2
DBSOURCE    REFSEQ: accession NM_053405.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Garcia,G., Noriega-Navarro,R., Martinez-Rojas,V.A.,
            Gutierrez-Lara,E.J., Oviedo,N. and Murbartian,J.
  TITLE     Spinal TASK-1 and TASK-3 modulate inflammatory and neuropathic pain
  JOURNAL   Eur J Pharmacol 862, 172631 (2019)
   PUBMED   31472119
  REMARK    GeneRIF: Study analyzed TASK-1 and TASK-3 expression in ipsilateral
            and contralateral dorsal root ganglia and dorsal and ventral spinal
            cord of naive and formalin-treated or nerve injured rats.
            Pharmacological and molecular data suggest that TASK-1 and TASK-3
            reduce the nociceptive transmission in acute/chronic inflammatory
            and neuropathic pain suggesting antinociceptive role of these
            channels in inflammatory and neuropathic pain.
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Zhang,H., Dong,H., Cilz,N.I., Kurada,L., Hu,B., Wada,E.,
            Bayliss,D.A., Porter,J.E. and Lei,S.
  TITLE     Neurotensinergic Excitation of Dentate Gyrus Granule Cells via
            Galphaq-Coupled Inhibition of TASK-3 Channels
  JOURNAL   Cereb Cortex 26 (3), 977-990 (2016)
   PUBMED   25405940
  REMARK    GeneRIF: results demonstrate that neurotensin (NT) transiently
            increased the neuronal excitability of dentate gyrus granule cells
            (GCs) by inhibiting TASK-3 channels; NT-mediated increases in
            neuronal excitability facilitate long-term potentiation at the
            perforant path-GC synapses
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Kubota,K., Ohtake,N., Ohbuchi,K., Mase,A., Imamura,S., Sudo,Y.,
            Miyano,K., Yamamoto,M., Kono,T. and Uezono,Y.
  TITLE     Hydroxy-alpha sanshool induces colonic motor activity in rat
            proximal colon: a possible involvement of KCNK9
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 308 (7), G579-G590 (2015)
   PUBMED   25634809
  REMARK    GeneRIF: Hydroxy-alpha sanshool evokes colonic motility via
            blockage of the neural KCNK9 channel in the colonic myenteric
            plexus.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Marinc,C., Derst,C., Pruss,H. and Veh,R.W.
  TITLE     Immunocytochemical localization of TASK-3 protein (K2P9.1) in the
            rat brain
  JOURNAL   Cell Mol Neurobiol 34 (1), 61-70 (2014)
   PUBMED   24077856
  REMARK    GeneRIF: the entire rat brain was immunocytochemically analyzed for
            expression of TASK-3 protein.
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Blankenship,M.L., Coyle,D.E. and Baccei,M.L.
  TITLE     Transcriptional expression of voltage-gated Na and
            voltage-independent K channels in the developing rat superficial
            dorsal horn
  JOURNAL   Neuroscience 231, 305-314 (2013)
   PUBMED   23219908
  REMARK    GeneRIF: In the dorsal horn of the developing rat, TWIK-related
            acid-sensitive K(+) channels TASK-1 (KCNK3) and TASK-3 (KCNK9) were
            down-regulated during postnatal development
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Czirjak,G. and Enyedi,P.
  TITLE     TASK-3 dominates the background potassium conductance in rat
            adrenal glomerulosa cells
  JOURNAL   Mol Endocrinol 16 (3), 621-629 (2002)
   PUBMED   11875121
  REMARK    GeneRIF: TASK-3 dominates the resting potassium conductance of zona
            glomerulosa cells
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Karschin,C., Wischmeyer,E., Preisig-Muller,R., Rajan,S., Derst,C.,
            Grzeschik,K.H., Daut,J. and Karschin,A.
  TITLE     Expression pattern in brain of TASK-1, TASK-3, and a tandem pore
            domain K(+) channel subunit, TASK-5, associated with the central
            auditory nervous system
  JOURNAL   Mol Cell Neurosci 18 (6), 632-648 (2001)
   PUBMED   11749039
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Vega-Saenz de Miera,E., Lau,D.H., Zhadina,M., Pountney,D.,
            Coetzee,W.A. and Rudy,B.
  TITLE     KT3.2 and KT3.3, two novel human two-pore K(+) channels closely
            related to TASK-1
  JOURNAL   J Neurophysiol 86 (1), 130-142 (2001)
   PUBMED   11431495
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Chapman,C.G., Meadows,H.J., Godden,R.J., Campbell,D.A.,
            Duckworth,M., Kelsell,R.E., Murdock,P.R., Randall,A.D., Rennie,G.I.
            and Gloger,I.S.
  TITLE     Cloning, localisation and functional expression of a novel human,
            cerebellum specific, two pore domain potassium channel
  JOURNAL   Brain Res Mol Brain Res 82 (1-2), 74-83 (2000)
   PUBMED   11042359
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Kim,Y., Bang,H. and Kim,D.
  TITLE     TASK-3, a new member of the tandem pore K(+) channel family
  JOURNAL   J Biol Chem 275 (13), 9340-9347 (2000)
   PUBMED   10734076
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF391084.1.
            
            On Dec 5, 2007 this sequence version replaced NP_445857.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF391084.1, AF192366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..396
                     /product="potassium channel subfamily K member 9
                     precursor"
                     /note="two pore potassium channel KT3.2; TWIK-related
                     acid-sensitive K(+) channel 3; acid-sensitive potassium
                     channel protein TASK-3; two pore K(+) channel KT3.2;
                     potassium channel, subfamily K, member 9 (Task-3);
                     potassium channel, two pore domain subfamily K, member 9;
                     potassium channel subfamily K member 9"
                     /calculated_mol_wt=41344
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3032
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ES08.2)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            78
                     /site_type="other"
                     /note="Forms a cation-pi interaction with protonated H-98,
                     stabilizing the C-type inactivated state.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2; propagated from
                     UniProtKB/Swiss-Prot (Q9ES08.2)"
     Region          93..98
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Site            98
                     /site_type="other"
                     /note="pH sensor. /evidence=ECO:0000250|UniProtKB:Q9NPC2;
                     propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Region          <184..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          199..204
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     Region          243..248
                     /region_name="X-gate.
                     /evidence=ECO:0000250|UniProtKB:Q9NPC2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES08.2)"
     CDS             1..396
                     /gene="Kcnk9"
                     /gene_synonym="Task-3; Task3"
                     /coded_by="NM_053405.2:1..1191"
                     /db_xref="GeneID:84429"
                     /db_xref="RGD:621451"
ORIGIN      
        1 mkrqnvrtls liactftyll vgaavfdale sdhemreeek lkaeevrlrg kynissddyq
       61 qlelvilqse phragvqwkf agsfyfaitv ittigyghaa pgtdagkafc mfyavlgipl
      121 tlvmfqslge rmntfvryll krikkccgmr ntevsmenmv tvgffscmgt lclgaaafsq
      181 cedwsffhay yycfitltti gfgdfvalqs kgalqrkpfy vafsfmyilv gltvigafln
      241 lvvlrfltmn tdedllegev aqilagnprr vvvrvpqsrk rhhpmyflrk ygrtlcylcf
      301 pganwgdddd ddddavenvv vttpvppava aaaaaatpgp strnvratvh svscrveeip
      361 pdvlrntyfr spfgaippgm htcgenhrlh irrksi
//
LOCUS       NP_775458                333 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 123 [Rattus norvegicus].
ACCESSION   NP_775458
VERSION     NP_775458.1
DBSOURCE    REFSEQ: accession NM_173336.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF240765.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF240765.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..333
                     /product="taste receptor type 2 member 123"
                     /note="T2R2; T2R23; T2R123; taste receptor type 2 member
                     2; taste receptor type 2 member 23; taste receptor, type
                     2, member 14; taste receptor rT2R2"
                     /calculated_mol_wt=38033
     Region          13..318
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          13..38
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Site            15..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          50..74
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            58..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          88..110
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            92..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Site            134..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          137..153
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          179..220
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Site            205..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          245..270
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            251..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     Region          282..307
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            283..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF0.1)"
     CDS             1..333
                     /gene="Tas2r123"
                     /gene_synonym="Tas2r14"
                     /coded_by="NM_173336.1:1..1002"
                     /db_xref="GeneID:287003"
                     /db_xref="RGD:727880"
ORIGIN      
        1 mfsqktnysh lftfsiifyv eivtgilgng fialvnimdw lkrrristad qiltalaltr
       61 liyvwsvlic illlflcphl smrpemftai gviwvvdnhf siwlatclgv fyflkiasfs
      121 nslflylkwr vkkvvlmiil isliflmlni sslgmydhfs idvyegnmsy nlvdsthfpr
      181 iflftnsskv fliansshvf lpinslfmli pftvslvaff vlflslwkhh kkmqvnakgp
      241 rdastmahtk alqigfsfll lyaiyllfii tgilnldlmr civillfdhi sgavfsishs
      301 fvlilgnskl rqatlsvlpc lrcrskdmdt vvf
//
LOCUS       NP_076487                305 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 13 [Rattus norvegicus].
ACCESSION   NP_076487
VERSION     NP_076487.1
DBSOURCE    REFSEQ: accession NM_023997.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Zhang,X., Bedigian,A.V., Wang,W. and Eggert,U.S.
  TITLE     G protein-coupled receptors participate in cytokinesis
  JOURNAL   Cytoskeleton (Hoboken) 69 (10), 810-818 (2012)
   PUBMED   22888021
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227144.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227144.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..305
                     /product="taste receptor type 2 member 13"
                     /note="T2R13; taste receptor type 2 member 7; taste
                     receptor T2R7"
                     /calculated_mol_wt=35464
     Region          8..292
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          9..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          45..66
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          176..199
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          227..249
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     Region          260..285
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT7.1)"
     CDS             1..305
                     /gene="Tas2r121"
                     /gene_synonym="T2R7; Tas2r13; Tas2r7"
                     /coded_by="NM_023997.1:1..918"
                     /db_xref="GeneID:78983"
                     /db_xref="RGD:620738"
ORIGIN      
        1 mgsslydilt ivmiaefifg nvtngfivlt nciawlskrt lsfigwiqlf laisrvvliw
       61 emllawlkym kysfsylagt elrvmmltwv vsnhfslwla tilsifyllk iasfsrpvfl
      121 ylkwrvkkvl llillgnlif lmfnilqint hiedwmdqyk rnitwdsrvn efvgfsnlvl
      181 lemimfsvtp ftvalvsfil lifslwkhlq kmhlssrger dpstkahvna lrimvsflll
      241 yatyfisffi slipmahkkg ldlmfsltvg lfypsshsfi lilghsnlrh ssclvitylr
      301 ckekd
//
LOCUS       NP_001074374             319 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 39 [Rattus norvegicus].
ACCESSION   NP_001074374 XP_001056060
VERSION     NP_001074374.1
DBSOURCE    REFSEQ: accession NM_001080905.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362751.1.
            
            On Jan 30, 2007 this sequence version replaced XP_001056060.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..319
                     /product="taste receptor type 2 member 39"
                     /note="putative taste receptor T2R32; T2R39; taste
                     receptor type 2 member 32; taste receptor, type 2, member
                     39"
                     /calculated_mol_wt=36289
     Region          17..305
                     /region_name="7tm_TAS2R39"
                     /note="mammalian taste receptor 2, subtype 39, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15015"
                     /db_xref="CDD:320143"
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          18..43
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320143"
     Region          55..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320143"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          92..114
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320143"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          141..157
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320143"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ER9.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          188..211
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320143"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          236..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320143"
     Site            248..268
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     Region          272..297
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320143"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER9.1)"
     CDS             1..319
                     /gene="Tas2r139"
                     /gene_synonym="Tas2r39"
                     /coded_by="NM_001080905.1:1..960"
                     /db_xref="GeneID:680188"
                     /db_xref="RGD:1595436"
ORIGIN      
        1 maqpsnywkq dllplsilil tlvatectig iiasgiitvv navswvqkra vsittrilll
       61 lsvsriglqs iiliemtssi fnfssynsvl yrvsrvsfvf lnycslwfaa llsffhfvki
      121 anfsyplffk lkwriselmp wllwlsvfis fsssmffcnh kytvynnisl ssnicnftme
      181 lyvaeanvvn vaflfsfgil ppltmfiata tllifslrrh tlhmrngdad srnprveahk
      241 qaiketscfl flyilyaavl flstsniada slfwssvlri slpvypaghs vlliqsnpgl
      301 krtwkqllsq ihlhlqsry
//
LOCUS       NP_835280                508 aa            linear   ROD 02-APR-2025
DEFINITION  amphoterin-induced protein 3 precursor [Rattus norvegicus].
ACCESSION   NP_835280
VERSION     NP_835280.1
DBSOURCE    REFSEQ: accession NM_178144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Ahmed,Z., Douglas,M.R., John,G., Berry,M. and Logan,A.
  TITLE     AMIGO3 is an NgR1/p75 co-receptor signalling axon growth inhibition
            in the acute phase of adult central nervous system injury
  JOURNAL   PLoS One 8 (4), e61878 (2013)
   PUBMED   23613963
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY237731.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY237731.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..508
                     /product="amphoterin-induced protein 3 precursor"
                     /EC_number="2.7.7.13"
                     /note="amphoterin-induced protein 3; AMIGO-3; alivin-3;
                     amphoterin induced gene and ORF 3; transmembrane protein
                     AMIGO3"
                     /calculated_mol_wt=53665
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1918
     mat_peptide     20..508
                     /product="Amphoterin-induced protein 3.
                     /evidence=ECO:0000255. /id=PRO_0000014515"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
                     /calculated_mol_wt=53665
     Region          62..83
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          <65..>221
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          65..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          87..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          111..134
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          134..155
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          135..158
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..178
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          159..184
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          184..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          185..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Region          279..355
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80ZD5.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZD5.1)"
     CDS             1..508
                     /gene="Amigo3"
                     /coded_by="NM_178144.1:1..1527"
                     /db_xref="GeneID:316003"
                     /db_xref="RGD:631413"
ORIGIN      
        1 mawlvllgll lcmlgagsgt sdlegvlppd phncpnkcvc aadvlscagr glqdlpaalp
       61 ataaeldlsh nalkrlhpgw laplsrlral ylgynkldvl grgvftnasg lrildlssnl
      121 lrrlrtydld gleeleklll fnnrlmhldl dafqglsmls hlylscnels sfsfnhlhgl
      181 gltrlrtldl ssnwlghvsv pelaalptfl knrlylhnnp lpcdcslyhl lrrwhqrgls
      241 alhdfereyt clafkvaesr vrffehsrvf kncsvaaapg lelpeeelht hvgqslrlfc
      301 nttvpaarva wvspknellv apgsqdgsia vladgslaig rvqeqhaglf vclasgprlh
      361 hnqtleynvs vhkprpepea fntgfttllg civglvlvll ylfappcrgc crccrracrn
      421 rcwprasspl qelsaqssvl sttppdapsr kasvhkhvaf lepgkkglng rvqlavaedf
      481 dlcnpmglql kagsesasst gseglmms
//
LOCUS       NP_942070                544 aa            linear   ROD 02-APR-2025
DEFINITION  prolyl 4-hydroxylase subunit alpha-3 precursor [Rattus norvegicus].
ACCESSION   NP_942070 XP_341891
VERSION     NP_942070.1
DBSOURCE    REFSEQ: accession NM_198775.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Kukkola,L., Hieta,R., Kivirikko,K.I. and Myllyharju,J.
  TITLE     Identification and characterization of a third human, rat, and
            mouse collagen prolyl 4-hydroxylase isoenzyme
  JOURNAL   J Biol Chem 278 (48), 47685-47693 (2003)
   PUBMED   14500733
  REMARK    GeneRIF: analysis of collagen prolyl 4-hydroxylase isoenzyme 3, its
            expression and catalytic properties
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY313450.1.
            
            On Dec 17, 2003 this sequence version replaced XP_341891.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY313450.1, SRR8487227.71417.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..544
                     /product="prolyl 4-hydroxylase subunit alpha-3 precursor"
                     /EC_number="1.14.11.2"
                     /note="4-PH alpha-3;
                     procollagen-proline,2-oxoglutarate-4-dioxygenase subunit
                     alpha-3; procollagen-proline, 2-oxoglutarate 4-dioxygenase
                     (proline 4-hydroxylase), alpha polypeptide III; collagen
                     prolyl 4-hydroxylase alpha III subunit; prolyl
                     4-hydroxylase, alpha polypeptide III"
                     /calculated_mol_wt=58909
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2275
     mat_peptide     25..544
                     /product="Prolyl 4-hydroxylase subunit alpha-3.
                     /id=PRO_0000317768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W3E9.1)"
                     /calculated_mol_wt=58909
     Region          33..160
                     /region_name="P4Ha_N"
                     /note="Prolyl 4-Hydroxylase alpha-subunit, N-terminal
                     region; pfam08336"
                     /db_xref="CDD:462433"
     Region          227..260
                     /region_name="TPR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W3E9.1)"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6W3E9.1)"
     Region          356..528
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6W3E9.1)"
     CDS             1..544
                     /gene="P4ha3"
                     /coded_by="NM_198775.1:26..1660"
                     /db_xref="GeneID:361612"
                     /db_xref="RGD:735150"
ORIGIN      
        1 mgpgarlaal lvllklgvgd paaaagredt fsaltsvara laperrllgt lrrylrgeea
       61 rlrdltrfyd kvlslhedlk ipvvnpllvf tlikrlpsdw rnvvhsleat enirapkdgy
      121 ekveqdlpaf edlegaaral mrlqdaymln vkglaqgvfq rvtgssitdl ysprqlfslt
      181 addcfqvgkv aydtgdyyha ipwleeavsl frrsygewkt edeasledal dylafacyqv
      241 gnvscalsls reflvyspdn krmarnvlky erllaenghl maaetaiqrp nvphlqtrdt
      301 yeglcqtlgs qpthyqipsl ycsyetnssp ylllqparke vihlrplval yhdfvsdeea
      361 qkirelaepw lqrsvvasge kqlqveyris ksawlkdtvd pvlvtldrri aaltgldiqp
      421 pyaeylqvvn ygigghyeph fdhatspssp lykmksgnra atlmiylssv eaggatafiy
      481 gnfsvpvvkn aalfwwnlhr sgegdddtlh agcpvlvgdk wvankwihey gqefrrpcdt
      541 nped
//
LOCUS       NP_861435                468 aa            linear   ROD 02-APR-2025
DEFINITION  glucose-dependent insulinotropic receptor [Rattus norvegicus].
ACCESSION   NP_861435
VERSION     NP_861435.1
DBSOURCE    REFSEQ: accession NM_181770.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Kang,Y., Sato,H., Saito,M., Yin,D.X., Park,S.K., Oh,S.B., Bae,Y.C.
            and Toyoda,H.
  TITLE     A role of CB1R in inducing theta;-rhythm coordination between the
            gustatory and gastrointestinal insula
  JOURNAL   Sci Rep 6, 32529 (2016)
   PUBMED   27581068
  REMARK    GeneRIF: The results demonstrate that the neural coordination
            between the the gustatory and gastrointestinal insula is generated
            or suppressed by the opposing activities between CB1R and GPR119.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Park,E.Y., Kim,E.H., Kim,C.Y., Kim,M.H., Choung,J.S., Oh,Y.S.,
            Moon,H.S. and Jun,H.S.
  TITLE     Angelica dahurica Extracts Improve Glucose Tolerance through the
            Activation of GPR119
  JOURNAL   PLoS One 11 (7), e0158796 (2016)
   PUBMED   27391814
  REMARK    GeneRIF: Angelica dahurica extract-treated cells showed significant
            increases in GPR119 activation, intracellular cAMP levels, GLP-1
            levels and glucose-stimulated insulin secretion as compared with
            controls
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Cornall,L.M., Hryciw,D.H., Mathai,M.L. and McAinch,A.J.
  TITLE     Direct activation of the proposed anti-diabetic receptor, GPR119 in
            cardiomyoblasts decreases markers of muscle metabolic activity
  JOURNAL   Mol Cell Endocrinol 402, 72-85 (2015)
   PUBMED   25578601
  REMARK    GeneRIF: Pathways activated in response to GPR119 modulation in
            cardiac muscle cells differ between healthy and metabolically
            dysregulated states.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Patel,S., Mace,O.J., Tough,I.R., White,J., Cock,T.A., Warpman
            Berglund,U., Schindler,M. and Cox,H.M.
  TITLE     Gastrointestinal hormonal responses on GPR119 activation in lean
            and diseased rodent models of type 2 diabetes
  JOURNAL   Int J Obes (Lond) 38 (10), 1365-1373 (2014)
   PUBMED   24451185
  REMARK    GeneRIF: Results show that functional GPR119 responses are similar
            in lean and diabetic rodent, and human colon; that GPR119
            stimulation can result in glucose lowering through release of
            intestinal peptide hormones.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Cornall,L.M., Mathai,M.L., Hryciw,D.H., Simcocks,A.C.,
            O'Brien,P.E., Wentworth,J.M. and McAinch,A.J.
  TITLE     GPR119 regulates genetic markers of fatty acid oxidation in
            cultured skeletal muscle myotubes
  JOURNAL   Mol Cell Endocrinol 365 (1), 108-118 (2013)
   PUBMED   23069642
  REMARK    GeneRIF: Data suggest that GPR119 activation/up-regulation in
            skeletal muscle impairs fatty acid and glucose oxidation;
            diet-induced obesity appears to up-regulate skeletal muscle GPR119.
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Soga,T., Ohishi,T., Matsui,T., Saito,T., Matsumoto,M., Takasaki,J.,
            Matsumoto,S., Kamohara,M., Hiyama,H., Yoshida,S., Momose,K.,
            Ueda,Y., Matsushime,H., Kobori,M. and Furuichi,K.
  TITLE     Lysophosphatidylcholine enhances glucose-dependent insulin
            secretion via an orphan G-protein-coupled receptor
  JOURNAL   Biochem Biophys Res Commun 326 (4), 744-751 (2005)
   PUBMED   15607732
  REMARK    Erratum:[Biochem Biophys Res Commun. 2005 Apr 1;329(1):417]
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Fredriksson,R., Hoglund,P.J., Gloriam,D.E., Lagerstrom,M.C. and
            Schioth,H.B.
  TITLE     Seven evolutionarily conserved human rhodopsin G protein-coupled
            receptors lacking close relatives
  JOURNAL   FEBS Lett 554 (3), 381-388 (2003)
   PUBMED   14623098
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY288429.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY288429.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..468
                     /product="glucose-dependent insulinotropic receptor"
                     /calculated_mol_wt=51555
     Region          6..290
                     /region_name="7tmA_GPR119_R_insulinotropic_receptor"
                     /note="G protein-coupled receptor 119, also called
                     glucose-dependent insulinotropic receptor, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15104"
                     /db_xref="CDD:320232"
     Region          7..32
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320232"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          40..66
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320232"
     Region          78..108
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320232"
     Site            order(81,85..86,89..90,166,169..170,173,238,241..242,245,
                     261,265,269)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320232"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          120..140
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320232"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          162..191
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320232"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          218..248
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320232"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320232"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TQN8.1)"
     Region          346..>453
                     /region_name="KLF18_N"
                     /note="N-terminal domain of Kruppel-like factor 18;
                     cd21575"
                     /db_xref="CDD:410566"
     CDS             1..468
                     /gene="Gpr119"
                     /coded_by="NM_181770.1:1..1407"
                     /db_xref="GeneID:302813"
                     /db_xref="RGD:727808"
ORIGIN      
        1 messfsfgvi lavltiliia vnalvvvaml lsiykndgvg lcftlnlava dtligvaisg
       61 lvtdqlsssa qhtqktlcsl rmafvtssaa asvltvmlia fdrylaikqp lryfqimngl
      121 vaggciaglw lisyligflp lgvsifqqtt yhgpctffav fhprfvltls cagffpavll
      181 fvffycdmlk iasvhsqhir kmehagamvg acrpprpvnd fkavrtvsvl igsftlswsp
      241 flitsivqva chkcclyqvl ekylwllgvg nsllnpliya ywqrevrqql chmalgllad
      301 gstqpqietl kgkeerkkvg rktlytcdaq tlytcdaqtl ytcdaqtlyt cdacdtqtly
      361 tcdaqtlytc daqtlytcda qtlytcdaqt lytcdaqtly tcdtqtlytc daqtlytcda
      421 qtlytcdaqt lytcdaqtly tsslvtgqte qtplkranms dplrtcrg
//
LOCUS       NP_852098                600 aa            linear   ROD 02-APR-2025
DEFINITION  proton channel OTOP1 [Rattus norvegicus].
ACCESSION   NP_852098
VERSION     NP_852098.1
DBSOURCE    REFSEQ: accession NM_181433.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Tu,Y.H., Cooper,A.J., Teng,B., Chang,R.B., Artiga,D.J.,
            Turner,H.N., Mulhall,E.M., Ye,W., Smith,A.D. and Liman,E.R.
  TITLE     An evolutionarily conserved gene family encodes proton-selective
            ion channels
  JOURNAL   Science 359 (6379), 1047-1050 (2018)
   PUBMED   29371428
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Wang,G.X., Cho,K.W., Uhm,M., Hu,C.R., Li,S., Cozacov,Z., Xu,A.E.,
            Cheng,J.X., Saltiel,A.R., Lumeng,C.N. and Lin,J.D.
  TITLE     Otopetrin 1 protects mice from obesity-associated metabolic
            dysfunction through attenuating adipose tissue inflammation
  JOURNAL   Diabetes 63 (4), 1340-1352 (2014)
   PUBMED   24379350
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Hurle,B., Ignatova,E., Massironi,S.M., Mashimo,T., Rios,X.,
            Thalmann,I., Thalmann,R. and Ornitz,D.M.
  TITLE     Non-syndromic vestibular disorder with otoconial agenesis in
            tilted/mergulhador mice caused by mutations in otopetrin 1
  JOURNAL   Hum Mol Genet 12 (7), 777-789 (2003)
   PUBMED   12651873
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK000651.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK000651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..600
                     /product="proton channel OTOP1"
                     /calculated_mol_wt=65798
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            57..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            87..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            129..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Region          131..586
                     /region_name="Otopetrin"
                     /note="pfam03189"
                     /db_xref="CDD:460840"
     Site            162..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            195..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            263..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            310..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            343..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            387..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            422..442
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            533..551
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Site            570..593
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M734.1)"
     Region          584..596
                     /region_name="putative FYR-box"
                     /note="consensus F-Y-R-[FM]-H-[SA]-X3[LF]-X-E-[VI]"
     CDS             1..600
                     /gene="Otop1"
                     /coded_by="NM_181433.1:25..1827"
                     /db_xref="GeneID:305427"
                     /db_xref="RGD:631389"
ORIGIN      
        1 mpgdrgalss paassgspsa apsgiaacpp ppsplarasp qasgprrgas vpqklaetls
       61 sqyglnvfva gllfllawav hatgvgksdl lcvltalmll qllwmlwyvg rsymqrrlir
      121 pkdthagarw lrgsitlfaf itivlgclkv ayfigfsecl sategvfpvt havhtllqvy
      181 flwghakdii msfktlerfg vihsvftnll lwansvlnes khqlnehker litlgfgnit
      241 ivlddhtpqc nctppalcsa lshgiyylyp fnieyqilas tmlyvlwkni grrvdssrhq
      301 kmqcrfdgvl vgsvlgltvl aatiavvvvy mihigrsksk sesalimfyl yaitvlllmg
      361 aaglvgswiy rvdeksldes knparkldad llvatasgsw llswgsilai acaetrppyt
      421 wynlpysvlv ivekyvqnif iiesvhlepe gvpedvrtlr vvtvcsgeaa alaasslgsq
      481 gtaqdgspav ngnlhlqqrc ekedqeadwe gatgttrcld flqggmkrrl lrnitaflfl
      541 cnislwippa fgcrpeydng leeivfgfep wiivvnlamp fsifyrmhaa aalfevycki
//
LOCUS       NP_076484                299 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 16 [Rattus norvegicus].
ACCESSION   NP_076484
VERSION     NP_076484.1
DBSOURCE    REFSEQ: accession NM_023994.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Meyerhof,W., Batram,C., Kuhn,C., Brockhoff,A., Chudoba,E., Bufe,B.,
            Appendino,G. and Behrens,M.
  TITLE     The molecular receptive ranges of human TAS2R bitter taste
            receptors
  JOURNAL   Chem Senses 35 (2), 157-170 (2010)
   PUBMED   20022913
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Behrens,M., Bartelt,J., Reichling,C., Winnig,M., Kuhn,C. and
            Meyerhof,W.
  TITLE     Members of RTP and REEP gene families influence functional bitter
            taste receptor expression
  JOURNAL   J Biol Chem 281 (29), 20650-20659 (2006)
   PUBMED   16720576
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Zhang,Y., Hoon,M.A., Chandrashekar,J., Mueller,K.L., Cook,B.,
            Wu,D., Zuker,C.S. and Ryba,N.J.
  TITLE     Coding of sweet, bitter, and umami tastes: different receptor cells
            sharing similar signaling pathways
  JOURNAL   Cell 112 (3), 293-301 (2003)
   PUBMED   12581520
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Montmayeur,J.P. and Matsunami,H.
  TITLE     Receptors for bitter and sweet taste
  JOURNAL   Curr Opin Neurobiol 12 (4), 366-371 (2002)
   PUBMED   12139982
  REMARK    Review article
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Wu,S.V., Rozengurt,N., Yang,M., Young,S.H., Sinnett-Smith,J. and
            Rozengurt,E.
  TITLE     Expression of bitter taste receptors of the T2R family in the
            gastrointestinal tract and enteroendocrine STC-1 cells
  JOURNAL   Proc Natl Acad Sci U S A 99 (4), 2392-2397 (2002)
   PUBMED   11854532
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Margolskee,R.F.
  TITLE     Molecular mechanisms of bitter and sweet taste transduction
  JOURNAL   J Biol Chem 277 (1), 1-4 (2002)
   PUBMED   11696554
  REMARK    Review article
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Chandrashekar,J., Mueller,K.L., Hoon,M.A., Adler,E., Feng,L.,
            Guo,W., Zuker,C.S. and Ryba,N.J.
  TITLE     T2Rs function as bitter taste receptors
  JOURNAL   Cell 100 (6), 703-711 (2000)
   PUBMED   10761935
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227141.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227141.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..299
                     /product="taste receptor type 2 member 16"
                     /note="T2R16; T2R18"
                     /calculated_mol_wt=34511
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          8..290
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          10..34
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          46..67
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          79..101
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          128..144
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          175..198
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          224..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     Region          257..282
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKU0.1)"
     CDS             1..299
                     /gene="Tas2r118"
                     /gene_synonym="T2R3; Tas2r16"
                     /coded_by="NM_023994.1:1..900"
                     /db_xref="GeneID:78980"
                     /db_xref="RGD:620735"
ORIGIN      
        1 mvptqvtifs iimyvleslv iivqscttva vlfrewmhfq rlspveiili slgishfclq
       61 wtsmlynfgt ysrpvllfwk vsvvwefmnv ltfwltslla vlycvkvssf shpvflwlrl
      121 kilklvlwll lgaliascls iipsvvkyhi qmelltldhl pknsslilrl qmfewyfsnp
      181 fkmigfgvpf lvflisiill tvslvqhwgq mkhyssssss lraqctvlks latffiffts
      241 yfltivvsfi gtvfdkkswf wvceaviygl vcihftslmm snptlkkalr lqfwspess
//
LOCUS       NP_001160151             324 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 116 [Rattus norvegicus].
ACCESSION   NP_001160151
VERSION     NP_001160151.1
DBSOURCE    REFSEQ: accession NM_001166679.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY362752.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..324
                     /product="taste receptor type 2 member 116"
                     /note="T2R33; T2R116; taste receptor type 2 member 33"
                     /calculated_mol_wt=36889
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          8..296
                     /region_name="7tm_TAS2R14-like"
                     /note="mammalian taste receptor 2, subtype 14, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15019"
                     /db_xref="CDD:320147"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320147"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320147"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320147"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          132..148
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320147"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          175..198
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320147"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          223..248
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320147"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     Region          260..285
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320147"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67ER8.1)"
     CDS             1..324
                     /gene="Tas2r116"
                     /coded_by="NM_001166679.1:1..975"
                     /db_xref="GeneID:100310877"
                     /db_xref="RGD:2314261"
ORIGIN      
        1 mngvlyitft vilsveviig nfgngiialv nimdlakrrk issvdqilta laisrivllw
       61 lvlvswwlsm fypgqwmteg idvivhnvwt tlnqislwla tsfsvfcflk vanfsntiff
      121 ylkirvkkvm tgtlimflll lglniivina sktilipeyk vnmsnslnlk ntqismlfpf
      181 antlfgfipf avslvtflll ffslwkhqrk mhhgaqgcrd sstkahirvl qtliasilly
      241 fvfflslvvk vwislflerm llllitqaak iafpslhpwv lilgnaklrk aslsalqwlr
      301 crhkdehrrv qrpevhscgs scmp
//
LOCUS       NP_072158                336 aa            linear   ROD 02-APR-2025
DEFINITION  ventral anterior homeobox 1 [Rattus norvegicus].
ACCESSION   NP_072158
VERSION     NP_072158.1
DBSOURCE    REFSEQ: accession NM_022636.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Rajan,S., Chu Pham Dang,H., Djambazian,H., Zuzan,H., Fedyshyn,Y.,
            Ketela,T., Moffat,J., Hudson,T.J. and Sladek,R.
  TITLE     Analysis of early C2C12 myogenesis identifies stably and
            differentially expressed transcriptional regulators whose
            knock-down inhibits myoblast differentiation
  JOURNAL   Physiol Genomics 44 (2), 183-197 (2012)
   PUBMED   22147266
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Kim,J.W. and Lemke,G.
  TITLE     Hedgehog-regulated localization of Vax2 controls eye development
  JOURNAL   Genes Dev 20 (20), 2833-2847 (2006)
   PUBMED   17043310
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Mui,S.H., Kim,J.W., Lemke,G. and Bertuzzi,S.
  TITLE     Vax genes ventralize the embryonic eye
  JOURNAL   Genes Dev 19 (10), 1249-1259 (2005)
   PUBMED   15905411
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Soria,J.M., Taglialatela,P., Gil-Perotin,S., Galli,R., Gritti,A.,
            Verdugo,J.M. and Bertuzzi,S.
  TITLE     Defective postnatal neurogenesis and disorganization of the rostral
            migratory stream in absence of the Vax1 homeobox gene
  JOURNAL   J Neurosci 24 (49), 11171-11181 (2004)
   PUBMED   15590934
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Taglialatela,P., Soria,J.M., Caironi,V., Moiana,A. and Bertuzzi,S.
  TITLE     Compromised generation of GABAergic interneurons in the brains of
            Vax1-/- mice
  JOURNAL   Development 131 (17), 4239-4249 (2004)
   PUBMED   15280216
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Hallonet,M., Hollemann,T., Pieler,T. and Gruss,P.
  TITLE     Vax1, a novel homeobox-containing gene, directs development of the
            basal forebrain and visual system
  JOURNAL   Genes Dev 13 (23), 3106-3114 (1999)
   PUBMED   10601036
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Bertuzzi,S., Hindges,R., Mui,S.H., O'Leary,D.D. and Lemke,G.
  TITLE     The homeodomain protein vax1 is required for axon guidance and
            major tract formation in the developing forebrain
  JOURNAL   Genes Dev 13 (23), 3092-3105 (1999)
   PUBMED   10601035
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF113515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF113515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..336
                     /product="ventral anterior homeobox 1"
                     /note="ventral anterior homeobox containing gene 1"
                     /calculated_mol_wt=34881
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM00.1)"
     Region          50..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM00.1)"
     Region          72..99
                     /region_name="vax upstream domain"
     Region          100..159
                     /region_name="homeobox"
     Region          101..157
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          178..189
                     /region_name="vax downstream domain"
     Region          236..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM00.1)"
     Region          315..323
                     /region_name="vax terminal domain"
     CDS             1..336
                     /gene="Vax1"
                     /coded_by="NM_022636.1:1..1011"
                     /db_xref="GeneID:64571"
                     /db_xref="RGD:621132"
ORIGIN      
        1 mfgktdkmdv rchsdteaar vsknahkesr eikgaegslp aaflkepqga fsasgasedc
       61 nksksnssad pdycrrilvr dakgsireii lpkgldldrp krtrtsftae qlyrlemefq
      121 rcqyvvgrer telarqlnls etqvkvwfqn rrtkqkkdqg kdselrsvvs etaatcsvlr
      181 lleqgrllsp pglpallppc atgalgsalr gpslpalgag aaagsaaaaa aaatapgpag
      241 aasqhppavg gapgpgpagp gglhagapta shglfslpvp sllgsvasrl ssapltmags
      301 lagnlqelsa rylsssafep ysrtnnkega ekkald
//
LOCUS       NP_001102638             348 aa            linear   ROD 02-APR-2025
DEFINITION  calcium homeostasis modulator protein 1 [Rattus norvegicus].
ACCESSION   NP_001102638 XP_001059715 XP_574681
VERSION     NP_001102638.1
DBSOURCE    REFSEQ: accession NM_001109168.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Puebla,M., Munoz,M.F., Lillo,M.A., Contreras,J.E. and Figueroa,X.F.
  TITLE     Control of astrocytic Ca2+ signaling by nitric oxide-dependent
            S-nitrosylation of Ca2+ homeostasis modulator 1 channels
  JOURNAL   Biol Res 57 (1), 19 (2024)
   PUBMED   38689353
  REMARK    GeneRIF: Control of astrocytic Ca[2+] signaling by nitric
            oxide-dependent S-nitrosylation of Ca[2+] homeostasis modulator 1
            channels.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Bigiani,A.
  TITLE     Calcium Homeostasis Modulator 1-Like Currents in Rat Fungiform
            Taste Cells Expressing Amiloride-Sensitive Sodium Currents
  JOURNAL   Chem Senses 42 (4), 343-359 (2017)
   PUBMED   28334404
  REMARK    GeneRIF: findings indicate that communication between
            salt-detecting cells and nerve endings might involve ATP release by
            CALMH1 channels.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Liu,W., Ao,Q., Guo,Q., He,W., Peng,L., Jiang,J. and Hu,X.
  TITLE     miR-9 Mediates CALHM1-Activated ATP-P2X7R Signal in Painful
            Diabetic Neuropathy Rats
  JOURNAL   Mol Neurobiol 54 (2), 922-929 (2017)
   PUBMED   26781424
  REMARK    GeneRIF: CALHM1 was increased in painful diabetic neuropathy
            compared with controls.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Taruno,A., Vingtdeux,V., Ohmoto,M., Ma,Z., Dvoryanchikov,G., Li,A.,
            Adrien,L., Zhao,H., Leung,S., Abernethy,M., Koppel,J., Davies,P.,
            Civan,M.M., Chaudhari,N., Matsumoto,I., Hellekant,G., Tordoff,M.G.,
            Marambaud,P. and Foskett,J.K.
  TITLE     CALHM1 ion channel mediates purinergic neurotransmission of sweet,
            bitter and umami tastes
  JOURNAL   Nature 495 (7440), 223-226 (2013)
   PUBMED   23467090
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Siebert,A.P., Ma,Z., Grevet,J.D., Demuro,A., Parker,I. and
            Foskett,J.K.
  TITLE     Structural and functional similarities of calcium homeostasis
            modulator 1 (CALHM1) ion channel with connexins, pannexins, and
            innexins
  JOURNAL   J Biol Chem 288 (9), 6140-6153 (2013)
   PUBMED   23300080
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Ma,Z., Siebert,A.P., Cheung,K.H., Lee,R.J., Johnson,B., Cohen,A.S.,
            Vingtdeux,V., Marambaud,P. and Foskett,J.K.
  TITLE     Calcium homeostasis modulator 1 (CALHM1) is the pore-forming
            subunit of an ion channel that mediates extracellular Ca2+
            regulation of neuronal excitability
  JOURNAL   Proc Natl Acad Sci U S A 109 (28), E1963-E1971 (2012)
   PUBMED   22711817
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Dreses-Werringloer,U., Lambert,J.C., Vingtdeux,V., Zhao,H.,
            Vais,H., Siebert,A., Jain,A., Koppel,J., Rovelet-Lecrux,A.,
            Hannequin,D., Pasquier,F., Galimberti,D., Scarpini,E., Mann,D.,
            Lendon,C., Campion,D., Amouyel,P., Davies,P., Foskett,J.K.,
            Campagne,F. and Marambaud,P.
  TITLE     A polymorphism in CALHM1 influences Ca2+ homeostasis, Abeta levels,
            and Alzheimer's disease risk
  JOURNAL   Cell 133 (7), 1149-1161 (2008)
   PUBMED   18585350
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_574681.1, XP_001059715.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..348
                     /product="calcium homeostasis modulator protein 1"
                     /note="family with sequence similarity 26, member C"
                     /calculated_mol_wt=38858
     Region          2..254
                     /region_name="Ca_hom_mod"
                     /note="Calcium homeostasis modulator; pfam14798"
                     /db_xref="CDD:464320"
     CDS             1..348
                     /gene="Calhm1"
                     /gene_synonym="Fam26c; RGD1564891"
                     /coded_by="NM_001109168.1:1..1047"
                     /db_xref="GeneID:499367"
                     /db_xref="RGD:1564891"
ORIGIN      
        1 mdkfrmifqf lqsnqesfmn gicgimalas aqmysafdfn cpclpgynvv ysmgilltpp
       61 lvlfllglvm nnnismlaee wkrplgrrak dpavlrymfc smaqraliap vvwvavtlld
      121 gkcflcafct avpvatlgng slvpglpape larllarvpc peiydgnwll arevavrylr
      181 cisqalgwsf vllttllafv vrsvrpcftq vaflkskyws hyidierklf detctehaka
      241 fakvciqqff eamnhdlelg hthgvlatas arttateaiq spsdrteeer eklrgitdqg
      301 smnrlltswh kckpplrlgq eaplmsngwa gseprpprke vatyfskv
//
LOCUS       NP_001009969             196 aa            linear   ROD 02-APR-2025
DEFINITION  Spetex-2H protein [Rattus norvegicus].
ACCESSION   NP_001009969 XP_341284
VERSION     NP_001009969.1
DBSOURCE    REFSEQ: accession NM_001009969.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Iwamoto,Y., Kaneko,T., Ichinose,J., Mori,T., Shibata,Y.,
            Toshimori,K. and Iida,H.
  TITLE     Molecular cloning of rat Spetex2 family genes mapped on chromosome
            15p16, encoding a 23-kilodalton protein associated with the plasma
            membranes of haploid spermatids
  JOURNAL   Biol Reprod 72 (2), 284-292 (2005)
   PUBMED   15371276
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB180083.1.
            
            On Jan 22, 2005 this sequence version replaced XP_341284.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB180083.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15"
     Protein         1..196
                     /product="Spetex-2H protein"
                     /calculated_mol_wt=23310
     Region          34..114
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..196
                     /gene="Spetex2h"
                     /gene_synonym="Spergen-2H; Spetex-2H"
                     /coded_by="NM_001009969.1:1..591"
                     /db_xref="GeneID:361008"
                     /db_xref="RGD:1359560"
ORIGIN      
        1 mfhqllklvq kergdqgetr lrqkkaglls wfirkassen fisnhekrik kleelkleiq
       61 kckierdels rildlyvndg lnyrlsvelp mlksqhemrt mdmhkmtnwi sdamekykel
      121 tqennsyhir nfhllnecne lkknvrilmn enrkllveqt elqasceirm gkrfceeask
      181 tiytadiesl cpvtfe
//
LOCUS       NP_001008850             341 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class I, locus M1, gene 4 precursor [Rattus norvegicus].
ACCESSION   NP_001008850 XP_227951
VERSION     NP_001008850.1
DBSOURCE    REFSEQ: accession NM_001008850.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BX883051.1.
            
            On Jan 5, 2005 this sequence version replaced XP_227951.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16418971
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..341
                     /product="RT1 class I, locus M1, gene 4 precursor"
                     /note="histocompatibility 2, M region locus 11"
                     /calculated_mol_wt=37289
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2144
     Region          25..203
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          207..298
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          208..215
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          223..232
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(226,228,255..256,258..260,266,268)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(233..235,263,288)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          237..242
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          245..248
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          252..260
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          263..273
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          280..287
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..341
                     /gene="RT1-M1-4"
                     /gene_synonym="H2-M11"
                     /coded_by="NM_001008850.1:1..1026"
                     /db_xref="GeneID:294213"
                     /db_xref="RGD:1359375"
ORIGIN      
        1 mktfvteall llllavlala shpegshlfg lfqtlltrpg hseplfisag fmdniqferf
       61 nnrsdfpgme hcapwidhrs peywkehtqr alkdirfmrq alklmihtyn ysatgyhtiq
      121 rrigchvlpr gyfshgflel afngqdyiml nedlrtwttv gkaaeilrke wekhsfaqam
      181 kiylevscvd sfltelaygk eillridppk vqvirkvrln rkitlmcwal sfyppeitlt
      241 wqrdgcnqmq dmevvetrpa gdgtfqkwaa vvvssgeeqr ytchvnhkgl pevitmrwep
      301 pepiipitti viavvlgalv vgavmtfliw kmtrgkeraw f
//
LOCUS       NP_001123248             552 aa            linear   ROD 02-APR-2025
DEFINITION  WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing
            protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001123248 XP_001060771 XP_343871
VERSION     NP_001123248.1
DBSOURCE    REFSEQ: accession NM_001129776.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Lee,Y.S. and Lee,S.J.
  TITLE     Regulation of GDF-11 and myostatin activity by GASP-1 and GASP-2
  JOURNAL   Proc Natl Acad Sci U S A 110 (39), E3713-E3722 (2013)
   PUBMED   24019467
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Szlama,G., Kondas,K., Trexler,M. and Patthy,L.
  TITLE     WFIKKN1 and WFIKKN2 bind growth factors TGFbeta1, BMP2 and BMP4 but
            do not inhibit their signalling activity
  JOURNAL   FEBS J 277 (24), 5040-5050 (2010)
   PUBMED   21054789
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Nishida,A.T., Kobuke,K., Kojima,K., Ito,J., Honjo,T. and Tashiro,K.
  TITLE     OC29 is preferentially expressed in the presumptive sensory organ
            region of the otocyst
  JOURNAL   Dev Dyn 231 (4), 766-774 (2004)
   PUBMED   15497143
  REMARK    GeneRIF: OC29 may have a role in the early development of the inner
            ear sensory organ, particularly in the formation of the cristae of
            the semicircular canals [OC29]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 22, 2008 this sequence version replaced
            XP_343871.2, XP_001060771.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132266 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..552
                     /product="WAP, Kazal, immunoglobulin, Kunitz and NTR
                     domain-containing protein 1 precursor"
                     /note="WAP, kazal, immunoglobulin, kunitz and NTR
                     domain-containing protein 1; WAP, FS, Ig, KU, and
                     NTR-containing protein 1"
                     /calculated_mol_wt=57157
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5J5.1)"
                     /calculated_mol_wt=2776
     mat_peptide     26..552
                     /product="WAP, Kazal, immunoglobulin, Kunitz and NTR
                     domain-containing protein 1. /id=PRO_0000307818"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J5.1)"
                     /calculated_mol_wt=57157
     Region          32..81
                     /region_name="WAP"
                     /note="WAP-type (Whey Acidic Protein) 'four-disulfide
                     core'; pfam00095"
                     /db_xref="CDD:459672"
     Region          124..159
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cd00104"
                     /db_xref="CDD:238052"
     Site            126..127
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (P0C5J5.1)"
     Region          190..284
                     /region_name="IgI_3_WFIKKN-like"
                     /note="Third immunoglobulin-like domain of the human
                     WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR
                     domain-containing protein), and similar domains; member of
                     the I-set of Ig superfamily (IgSF) domains; cd05765"
                     /db_xref="CDD:409422"
     Region          190..193
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409422"
     Region          198..201
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409422"
     Region          206..213
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409422"
     Region          220..225
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409422"
     Region          226..228
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409422"
     Region          230..235
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409422"
     Region          243..249
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409422"
     Region          263..271
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409422"
     Region          274..284
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409422"
     Region          302..355
                     /region_name="Kunitz-type"
                     /note="Kunitz/Bovine pancreatic trypsin inhibitor (BPTI)
                     domain; cl00101"
                     /db_xref="CDD:444694"
     Site            order(309..313,317..319,334,338)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438633"
     Region          362..414
                     /region_name="Kunitz_WFIKKN_2-like"
                     /note="second Kunitz domain of WAP, Kazal, immunoglobulin,
                     Kunitz and NTR domain-containing proteins; cd22606"
                     /db_xref="CDD:438649"
     Site            order(369..373,375..377,392,396)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438649"
     Region          431..541
                     /region_name="NTR_like"
                     /note="NTR_like domain; a beta barrel with an
                     oligosaccharide/oligonucleotide-binding fold found in
                     netrins, complement proteins, tissue inhibitors of
                     metalloproteases (TIMP), and procollagen C-proteinase
                     enhancers (PCOLCE), amongst others. In netrins, the...;
                     cl02512"
                     /db_xref="CDD:470599"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5J5.1)"
     CDS             1..552
                     /gene="Wfikkn1"
                     /gene_synonym="Oc29; RGD1565835"
                     /coded_by="NM_001129776.1:1..1659"
                     /db_xref="GeneID:363555"
                     /db_xref="RGD:1565835"
ORIGIN      
        1 mpapqpllpl lfafvlihlt setnllpepg shpgmcpnql sphlwvdaqs tcerectrdq
       61 dcaasekcct nvcglqscva arfpsggpat petaascedf qcpqqgsncd iwdgqpvcrc
      121 rdrcekepsf tcasdgltyy nrcymdaeac lrglhlhvvp ckhilswpps spgppettar
      181 ptpgaapmpp alynspspqa vhvggtaslh cdvsgrpppa vtwekqshqr enlimrpdqm
      241 ygnvvvtsig qlvlynaqle daglytctar naagllradf plsvlqratt qdrdpgvlal
      301 aecqpdtqac vgpptphhvl wrfdpqrgsc mtfpalkcdg aargfetyea cqqacvrgpg
      361 dvcalppvqg pcqgweprwa yspllqqchp fiysgcegns nnfesresce dacpvprtpp
      421 cracrlkskl alslcrsdfa ivgrltevle epeaaggiar valddvlkdd kmglkflgtk
      481 ylevtlsgmd wacpcpnvtv gdgplvimge vregvavlda nsyvraasek rvkkivelle
      541 kkacellnrf qd
//
LOCUS       NP_073163                151 aa            linear   ROD 02-APR-2025
DEFINITION  small ribosomal subunit protein uS11 [Rattus norvegicus].
ACCESSION   NP_073163
VERSION     NP_073163.1
DBSOURCE    REFSEQ: accession NM_022672.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Bayes,A., van de Lagemaat,L.N., Collins,M.O., Croning,M.D.,
            Whittle,I.R., Choudhary,J.S. and Grant,S.G.
  TITLE     Characterization of the proteome, diseases and evolution of the
            human postsynaptic density
  JOURNAL   Nat Neurosci 14 (1), 19-21 (2011)
   PUBMED   21170055
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Tasheva,E.S. and Roufa,D.J.
  TITLE     Regulation of human RPS14 transcription by intronic antisense RNAs
            and ribosomal protein S14
  JOURNAL   Genes Dev 9 (3), 304-316 (1995)
   PUBMED   7867928
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Paz,V., Chan,Y.L., Gluck,A. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein S14
  JOURNAL   Nucleic Acids Res 17 (22), 9484 (1989)
   PUBMED   2587275
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Marion,M.J. and Marion,C.
  TITLE     Ribosomal proteins S2, S6, S10, S14, S15 and S25 are localized on
            the surface of mammalian 40 S subunits and stabilize their
            conformation. A study with immobilized trypsin
  JOURNAL   FEBS Lett 232 (2), 281-285 (1988)
   PUBMED   3378620
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Rhoads,D.D. and Roufa,D.J.
  TITLE     A cloned human ribosomal protein gene functions in rodent cells
  JOURNAL   Mol Cell Biol 7 (10), 3767-3774 (1987)
   PUBMED   3683397
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Collatz,E., Ulbrich,N., Tsurugi,K., Lightfoot,H.N., MacKinlay,W.,
            Lin,A. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 40 S ribosomal subunit proteins Sa, Sc,
            S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18,
            S19, S20, S21, S26, S27', and S29
  JOURNAL   J Biol Chem 252 (24), 9071-9080 (1977)
   PUBMED   925037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X15040.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X15040.1, FQ211449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..151
                     /product="small ribosomal subunit protein uS11"
                     /note="40S ribosomal protein S14"
                     /calculated_mol_wt=16128
     Region          1..140
                     /region_name="PTZ00129"
                     /note="40S ribosomal protein S14; Provisional"
                     /db_xref="CDD:185465"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62263; propagated from
                     UniProtKB/Swiss-Prot (P13471.3)"
     Region          131..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13471.3)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62263; propagated from
                     UniProtKB/Swiss-Prot (P13471.3)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62263; propagated from
                     UniProtKB/Swiss-Prot (P13471.3)"
     CDS             1..151
                     /gene="Rps14"
                     /coded_by="NM_022672.1:37..492"
                     /db_xref="GeneID:29284"
                     /db_xref="RGD:62025"
ORIGIN      
        1 maprkgkdkk eeqvislgpq vaegenvfgv chifasfndt fvhvtdlsgk eticrvtggm
       61 kvkadrdess pyaamlaaqd vaqrckelgi talhiklrat ggnrtktpgp gaqsalrala
      121 rsgmkigrie dvtpipsdst rrkggrrgrr l
//
LOCUS       NP_001100053             456 aa            linear   ROD 02-APR-2025
DEFINITION  G protein-coupled receptor 15-like [Rattus norvegicus].
ACCESSION   NP_001100053 XP_001067990 XP_231463
VERSION     NP_001100053.1
DBSOURCE    REFSEQ: accession NM_001106583.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473966.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_231463.4, XP_001067990.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN14984021,
                              SAMN14984024 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..456
                     /product="G protein-coupled receptor 15-like"
                     /calculated_mol_wt=51238
     Region          73..357
                     /region_name="7tmA_GPR83"
                     /note="G protein-coupled receptor 83, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15389"
                     /db_xref="CDD:320511"
     Region          74..100
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320511"
     Region          107..132
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320511"
     Site            order(129,132..133,145..150,152..153,156,199,201..205,237,
                     240..242,244..246,248..249,306,309..310,312..313,316,
                     324..325,327..329,332,335..336)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320511"
     Region          145..175
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320511"
     Region          186..207
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320511"
     Region          237..266
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320511"
     Region          286..316
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320511"
     Region          325..350
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320511"
     CDS             1..456
                     /gene="Pgr15l"
                     /gene_synonym="RGD1562685"
                     /coded_by="NM_001106583.1:278..1648"
                     /db_xref="GeneID:296867"
                     /db_xref="RGD:1562685"
ORIGIN      
        1 mnasfkeasp fllqmesaid wlgenvswvp siedqscnht tqngtnissa ewggprgtvt
       61 kwlggnphim akivltfaya viivislfgn slvcqvfvkh ketkkstgll ifnlaisdil
      121 iillnspfal arflsgqwvf grimchvsrf aqycslhvst ltlmavamdr hrvilhpmkp
      181 rlthsqslfv vgviwsiavf lalphaiyqn lftlvnmdgd vrsyclpsfp gpstlvskyv
      241 dlgtfillyi lpllvivgty shlgkrlwiq naigdasarq lmahyqkrkk sirmlilivl
      301 vfavcwfpln fyvvlissag vendsvifya fhwfamsstc ynpfiycwln rsfraklrsi
      361 ssfrmqslfv csssqvqqiq preshelrel rtssllrvpl avpepqvfed pslatgdnsq
      421 vsvqgewedp dpsldeepgp strdsyfcih mqtsth
//
LOCUS       NP_001025215             484 aa            linear   ROD 02-APR-2025
DEFINITION  iroquois-class homeodomain protein IRX-5 [Rattus norvegicus].
ACCESSION   NP_001025215 XP_574208
VERSION     NP_001025215.1
DBSOURCE    REFSEQ: accession NM_001030044.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Liu,D., Pattabiraman,V., Bacanamwo,M. and Anderson,L.M.
  TITLE     Iroquois homeobox transcription factor (Irx5) promotes G1/S-phase
            transition in vascular smooth muscle cells by CDK2-dependent
            activation
  JOURNAL   Am J Physiol Cell Physiol 311 (2), C179-C189 (2016)
   PUBMED   27170637
  REMARK    GeneRIF: Irx5 plays an important role in VSMC G1/S-phase cell cycle
            checkpoint control.
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Bonnard,C., Strobl,A.C., Shboul,M., Lee,H., Merriman,B.,
            Nelson,S.F., Ababneh,O.H., Uz,E., Guran,T., Kayserili,H., Hamamy,H.
            and Reversade,B.
  TITLE     Mutations in IRX5 impair craniofacial development and germ cell
            migration via SDF1
  JOURNAL   Nat Genet 44 (6), 709-713 (2012)
   PUBMED   22581230
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 484)
  AUTHORS   He,W., Jia,Y. and Takimoto,K.
  TITLE     Interaction between transcription factors Iroquois proteins 4 and 5
            controls cardiac potassium channel Kv4.2 gene transcription
  JOURNAL   Cardiovasc Res 81 (1), 64-71 (2009)
   PUBMED   18815185
  REMARK    GeneRIF: Interaction between transcription factors Iroquois
            proteins 4 and 5 controls cardiac potassium channel Kv4.2 gene
            transcription across the left ventricular wall of rodent hearts.
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Kerschensteiner,D., Liu,H., Cheng,C.W., Demas,J., Cheng,S.H.,
            Hui,C.C., Chow,R.L. and Wong,R.O.
  TITLE     Genetic control of circuit function: Vsx1 and Irx5 transcription
            factors regulate contrast adaptation in the mouse retina
  JOURNAL   J Neurosci 28 (10), 2342-2352 (2008)
   PUBMED   18322081
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Beisvag,V., Lehre,P.K., Midelfart,H., Aass,H., Geiran,O.,
            Sandvik,A.K., Laegreid,A., Komorowski,J. and Ellingsen,O.
  TITLE     Aetiology-specific patterns in end-stage heart failure patients
            identified by functional annotation and classification of
            microarray data
  JOURNAL   Eur J Heart Fail 8 (4), 381-389 (2006)
   PUBMED   16753336
REFERENCE   6  (residues 1 to 484)
  AUTHORS   Rosati,B., Grau,F. and McKinnon,D.
  TITLE     Regional variation in mRNA transcript abundance within the
            ventricular wall
  JOURNAL   J Mol Cell Cardiol 40 (2), 295-302 (2006)
   PUBMED   16412459
REFERENCE   7  (residues 1 to 484)
  AUTHORS   Cheng,C.W., Chow,R.L., Lebel,M., Sakuma,R., Cheung,H.O.,
            Thanabalasingham,V., Zhang,X., Bruneau,B.G., Birch,D.G., Hui,C.C.,
            McInnes,R.R. and Cheng,S.H.
  TITLE     The Iroquois homeobox gene, Irx5, is required for retinal cone
            bipolar cell development
  JOURNAL   Dev Biol 287 (1), 48-60 (2005)
   PUBMED   16182275
REFERENCE   8  (residues 1 to 484)
  AUTHORS   Costantini,D.L., Arruda,E.P., Agarwal,P., Kim,K.H., Zhu,Y., Zhu,W.,
            Lebel,M., Cheng,C.W., Park,C.Y., Pierce,S.A., Guerchicoff,A.,
            Pollevick,G.D., Chan,T.Y., Kabir,M.G., Cheng,S.H., Husain,M.,
            Antzelevitch,C., Srivastava,D., Gross,G.J., Hui,C.C., Backx,P.H.
            and Bruneau,B.G.
  TITLE     The homeodomain transcription factor Irx5 establishes the mouse
            cardiac ventricular repolarization gradient
  JOURNAL   Cell 123 (2), 347-358 (2005)
   PUBMED   16239150
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ109812.1.
            
            On Aug 5, 2005 this sequence version replaced XP_574208.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ109812.1, AW252100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..484
                     /product="iroquois-class homeodomain protein IRX-5"
                     /note="iroquois homeobox protein 5"
                     /calculated_mol_wt=50536
     Site            order(116..117,119,139,145,158,160..161,164..165,167..169,
                     171..172)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(118,161,164..165,168)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          131..169
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          <223..411
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..484
                     /gene="Irx5"
                     /coded_by="NM_001030044.1:1..1455"
                     /db_xref="GeneID:498918"
                     /db_xref="RGD:1565518"
ORIGIN      
        1 msypqgylyq psaslalysc paystsvisg prtdelgrss sgsafspyag staftapspg
       61 ynshlqygad paaaaaaafs yvgspydhtp gmagslgyhp yaaplgsypy gdpayrknat
      121 rdatatlkaw lnehrknpyp tkgekimlai itkmtltqvs twfvnarrrl kkenkmtwtp
      181 rnrsedeeee enidleknde depqkpedkg dlegpeaggt eqkaaagcer lqgplspagk
      241 etegslsdsd fkespsegrh ddlprpprag epspagpata rlaedagphy pagapapgph
      301 psagelppgs ggssvihspp pppppppavl akpklwslae iatssdkvkd ggggsegspc
      361 ppcpgpiggq tlggsraspa paparspsaq cpfpggtvls rplyytapfy pgytnygsfg
      421 hlhghpgpgp gptagpgshf nglnqtvlnr advlakdpkm lrsqsqldlc kdspyelkkg
      481 msdi
//
LOCUS       NP_001100709             967 aa            linear   ROD 02-APR-2025
DEFINITION  adenylate cyclase type 1 [Rattus norvegicus].
ACCESSION   NP_001100709 XP_001053224 XP_223616
VERSION     NP_001100709.1
DBSOURCE    REFSEQ: accession NM_001107239.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Zhang,X., Pizzoni,A., Hong,K., Naim,N., Qi,C., Korkhov,V. and
            Altschuler,D.L.
  TITLE     CAP1 binds and activates adenylyl cyclase in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 118 (24) (2021)
   PUBMED   34099549
  REMARK    GeneRIF: CAP1 binds and activates adenylyl cyclase in mammalian
            cells.
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Santos-Cortez,R.L., Lee,K., Giese,A.P., Ansar,M., Amin-Ud-Din,M.,
            Rehn,K., Wang,X., Aziz,A., Chiu,I., Hussain Ali,R., Smith,J.D.,
            Shendure,J., Bamshad,M., Nickerson,D.A., Ahmed,Z.M., Ahmad,W.,
            Riazuddin,S. and Leal,S.M.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Adenylate cyclase 1 (ADCY1) mutations cause recessive hearing
            impairment in humans and defects in hair cell function and hearing
            in zebrafish
  JOURNAL   Hum Mol Genet 23 (12), 3289-3298 (2014)
   PUBMED   24482543
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Hwang,C.K., Chaurasia,S.S., Jackson,C.R., Chan,G.C., Storm,D.R. and
            Iuvone,P.M.
  TITLE     Circadian rhythm of contrast sensitivity is regulated by a
            dopamine-neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling
            pathway in retinal ganglion cells
  JOURNAL   J Neurosci 33 (38), 14989-14997 (2013)
   PUBMED   24048828
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Ehling,P., Kanyshkova,T., Baumann,A., Landgraf,P., Meuth,S.G.,
            Pape,H.C. and Budde,T.
  TITLE     Adenylyl cyclases: expression in the developing rat thalamus and
            their role in absence epilepsy
  JOURNAL   J Mol Neurosci 48 (1), 45-52 (2012)
   PUBMED   22531884
  REMARK    GeneRIF: Despite previous hints pointing to a major contribution of
            ACs, the presented data show that there is no apparent causality
            between AC activity and the occurrence of the epileptic phenotype.
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Jensen,J.B., Mikkelsen,J.D. and Mork,A.
  TITLE     Increased adenylyl cyclase type 1 mRNA, but not adenylyl cyclase
            type 2 in the rat hippocampus following antidepressant treatment
  JOURNAL   Eur Neuropsychopharmacol 10 (2), 105-111 (2000)
   PUBMED   10706991
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Wong,S.T., Athos,J., Figueroa,X.A., Pineda,V.V., Schaefer,M.L.,
            Chavkin,C.C., Muglia,L.J. and Storm,D.R.
  TITLE     Calcium-stimulated adenylyl cyclase activity is critical for
            hippocampus-dependent long-term memory and late phase LTP
  JOURNAL   Neuron 23 (4), 787-798 (1999)
   PUBMED   10482244
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Villacres,E.C., Wong,S.T., Chavkin,C. and Storm,D.R.
  TITLE     Type I adenylyl cyclase mutant mice have impaired mossy fiber
            long-term potentiation
  JOURNAL   J Neurosci 18 (9), 3186-3194 (1998)
   PUBMED   9547227
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Matsuoka,I., Suzuki,Y., Defer,N., Nakanishi,H. and Hanoune,J.
  TITLE     Differential expression of type I, II, and V adenylyl cyclase gene
            in the postnatal developing rat brain
  JOURNAL   J Neurochem 68 (2), 498-506 (1997)
   PUBMED   9003034
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Tzavara,E.T., Pouille,Y., Defer,N. and Hanoune,J.
  TITLE     Diurnal variation of the adenylyl cyclase type 1 in the rat pineal
            gland
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 11208-11212 (1996)
   PUBMED   8855334
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474055.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_223616.4, XP_001053224.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..967
                     /product="adenylate cyclase type 1"
                     /EC_number="4.6.1.1"
                     /note="adenylate cyclase 1 (brain)"
                     /calculated_mol_wt=108131
     Region          <6..139
                     /region_name="AC_N"
                     /note="Adenylyl cyclase N-terminal extracellular and
                     transmembrane region; pfam16214"
                     /db_xref="CDD:318454"
     Region          141..323
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(153,155..160,195,197..199,202,264..266,270..271,
                     274..275,309)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(155,199)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(160,172,175..176,179,183,195..196,252,255,265..268,
                     271,309)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          706..903
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(718,720..725,767,769..771,774,844..846,850..851,
                     854..855,891)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(720,771)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(725,741,744..745,748,752,767..768,832,835,845..848,
                     851,891)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..967
                     /gene="Adcy1"
                     /gene_synonym="Ac1"
                     /coded_by="NM_001107239.1:316..3219"
                     /db_xref="GeneID:305509"
                     /db_xref="RGD:1309318"
ORIGIN      
        1 mgsavaeqgv wqlllvtfvs yallpvrsll aigfglvvaa shllvtaalv pakrprlwrt
       61 lganallffg vnmygvfvri ltersqrkaf lqarnciedr lrledenekq erllmsllpr
      121 nvamemkedf lkpperifhk iyiqrhdnvs ilfadivgft glasqctaqe lvkllnelfg
      181 kfdelatenh crrikilgdc yycvsgltqp ktdhahccve mgldmidtit svaeatevdl
      241 nmrvglhtgr vlcgvlglrk wqydvwsndv tlanvmeaag lpgkvhitkt tlaclngdye
      301 vepghghern tflrthniet ffivpshrrk ifpglilsdi kpakrmkfkt vcyllvqlmh
      361 crkmfkaeip fsnvmtcedd dkrralrtas eklrnrssfs tnvvyttpgt rvnryisrll
      421 earqtelema dlnfftlkyk hvereqkyhq lqdeyftsav vlalilatlf gliyllvipq
      481 svavllllvf sicflvactl ylhitrvqcf pgcltiqirt alcvfivvli ysvaqgcvvs
      541 clpwawsshs nsslvvlaag grrtvlpalp cesahhgllc clvgtlplai flrvsslpkm
      601 illsglttsy ilvlelsgyt kvgggalsgr syepimaill fsctlalhar qvdvrlrldy
      661 lwaaqaeeer ddmervkldn krilfnllpa hvaqhflmsn prnmdlyyqs ysqvgvmfas
      721 ipnfndfyie ldgnnmgvec lrllneiiad fdelmdkdfy kdlekiktig stymaavgla
      781 ptagtrakks isshlstlad faidmfdvld einyqsyndf vlrvginvgp vvagvigarr
      841 pqydiwgntv nvasrmdstg vqgriqvtee vhrllnrcsy qfvcrgkvsv kgkgemltyf
      901 legrtdgsss hsrslrlerr mfpygrgggg qarrpplcpa agppikpgls paptsqylss
      961 taagkea
//
LOCUS       NP_001094489             262 aa            linear   ROD 02-APR-2025
DEFINITION  C-type lectin domain family 2 member D3 [Rattus norvegicus].
ACCESSION   NP_001094489 XP_001071896
VERSION     NP_001094489.2
DBSOURCE    REFSEQ: accession NM_001101019.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kveberg,L., Dai,K.Z., Westgaard,I.H., Daws,M.R., Fossum,S.,
            Naper,C. and Vaage,J.T.
  TITLE     Two major groups of rat NKR-P1 receptors can be distinguished based
            on chromosomal localization, phylogenetic analysis and Clr ligand
            binding
  JOURNAL   Eur J Immunol 39 (2), 541-551 (2009)
   PUBMED   19130483
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Voigt,S., Mesci,A., Ettinger,J., Fine,J.H., Chen,P., Chou,W. and
            Carlyle,J.R.
  TITLE     Cytomegalovirus evasion of innate immunity by subversion of the
            NKR-P1B:Clr-b missing-self axis
  JOURNAL   Immunity 26 (5), 617-627 (2007)
   PUBMED   17462921
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from FJ404472.1.
            
            On Jul 20, 2012 this sequence version replaced NP_001094489.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ404472.1, EF100687.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345330, SAMN09345331
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="DA"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..262
                     /product="C-type lectin domain family 2 member D3"
                     /calculated_mol_wt=28865
     Region          <83..253
                     /region_name="PHA02642"
                     /note="C-type lectin-like protein; Provisional"
                     /db_xref="CDD:165024"
     CDS             1..262
                     /gene="Clec2d2l1"
                     /gene_synonym="Clec2d3; RGD1563033"
                     /coded_by="NM_001101019.2:1..789"
                     /db_xref="GeneID:689757"
                     /db_xref="RGD:1588731"
ORIGIN      
        1 msplnprpys msssahlqda ppllsgtltq negqtslrqs sscgpsaasa seslsgytes
       61 riphskvrqg kglrsifpes rvkryccygg vitvvaiaiv vplsvtlsvk qmeqtsinnt
      121 faasinntsa asinntsaac psnwteygnk cfyfseytsn wtfskdfcaa qgaelarfdt
      181 eeelnflkry kgssgywigl hressehpwk wtdntqynnl vpirgdgqcg flsdqlniss
      241 srvyverpwi cskpkkyisq sq
//
LOCUS       NP_001243458              98 aa            linear   ROD 02-APR-2025
DEFINITION  prostate and testis expressed protein 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_001243458 XP_002727071 XP_002729972
VERSION     NP_001243458.1
DBSOURCE    REFSEQ: accession NM_001256529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Rajesh,A. and Yenugu,S.
  TITLE     Genomic organization, tissue distribution and functional
            characterization of the rat Pate gene cluster
  JOURNAL   PLoS One 7 (3), e32633 (2012)
   PUBMED   22479333
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from HQ916281.1.
            
            On or before Feb 6, 2012 this sequence version replaced
            XP_002729972.1, XP_002727071.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ916281.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..98
                     /product="prostate and testis expressed protein 3
                     precursor"
                     /note="prostate and testis expressed DJ; prostate and
                     testis expressed protein 3; prostate and testis expressed
                     DJ-like"
                     /calculated_mol_wt=9463
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2119
     Region          17..96
                     /region_name="TFP_LU_ECD_PATE3"
                     /note="extracellular domain (ECD) found in prostate and
                     testis expressed protein 3 (PATE3) and similar proteins;
                     cd23579"
                     /db_xref="CDD:467109"
     CDS             1..98
                     /gene="Pate3"
                     /coded_by="NM_001256529.1:1..297"
                     /db_xref="GeneID:100361414"
                     /db_xref="RGD:2320151"
ORIGIN      
        1 mnrhflllvs lfcliveatt lkcttchlrt qsdhcrrgfg vclaqkhetc mslriysngs
       61 lqtsymvcqr fcknlaynfn nrtyihkccn ydfcnfrl
//
LOCUS       NP_001254709             108 aa            linear   ROD 02-APR-2025
DEFINITION  prostate and testis expressed protein F precursor [Rattus
            norvegicus].
ACCESSION   NP_001254709
VERSION     NP_001254709.1
DBSOURCE    REFSEQ: accession NM_001267780.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Rajesh,A. and Yenugu,S.
  TITLE     Genomic organization, tissue distribution and functional
            characterization of the rat Pate gene cluster
  JOURNAL   PLoS One 7 (3), e32633 (2012)
   PUBMED   22479333
  REMARK    GeneRIF: Data show that PATE and PATE-F proteins were found to be
            expressed abundantly in the male reproductive tract and on the
            sperm.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from JF412806.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JF412806.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..108
                     /product="prostate and testis expressed protein F
                     precursor"
                     /note="prostate and testis expressed protein 2-like"
                     /calculated_mol_wt=9966
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2266
     Region          22..103
                     /region_name="TFP_LU_ECD_PATE2"
                     /note="extracellular domain (ECD) found in prostate and
                     testis expressed protein 2 (PATE2) and similar proteins;
                     cd23578"
                     /db_xref="CDD:467108"
     CDS             1..108
                     /gene="Pate-f"
                     /coded_by="NM_001267780.1:1..327"
                     /db_xref="GeneID:100913081"
                     /db_xref="RGD:6484596"
ORIGIN      
        1 mgklllllll lgafvllliq aqericmsch mfvngkcves egkctmedgg acrtrdiylf
       61 narggflynh tmlecsksck aseesyfhlk istfccksqd fcnkykgk
//
LOCUS       NP_001004216             568 aa            linear   ROD 02-APR-2025
DEFINITION  NADPH oxidase 3 [Rattus norvegicus].
ACCESSION   NP_001004216 XP_217848
VERSION     NP_001004216.1
DBSOURCE    REFSEQ: accession NM_001004216.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Michihara,A., Oda,A. and Mido,M.
  TITLE     High Expression Levels of NADPH Oxidase 3 in the Cerebrum of
            Ten-Week-Old Stroke-Prone Spontaneously Hypertensive Rats
  JOURNAL   Biol Pharm Bull 39 (2), 252-258 (2016)
   PUBMED   26830484
  REMARK    GeneRIF: These results suggested that the high expression levels of
            NOX3 increased oxidative stress in stroke-prone hypertensive rat
            cerebrum.
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Mukherjea,D., Jajoo,S., Kaur,T., Sheehan,K.E., Ramkumar,V. and
            Rybak,L.P.
  TITLE     Transtympanic administration of short interfering (si)RNA for the
            NOX3 isoform of NADPH oxidase protects against cisplatin-induced
            hearing loss in the rat
  JOURNAL   Antioxid Redox Signal 13 (5), 589-598 (2010)
   PUBMED   20214492
  REMARK    GeneRIF: NOX3 regulates stress-related genes in the cochlea, such
            as TRPV1 and KIM-1, and initiates apoptosis in the cochlea.
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Mukherjea,D., Jajoo,S., Whitworth,C., Bunch,J.R., Turner,J.G.,
            Rybak,L.P. and Ramkumar,V.
  TITLE     Short interfering RNA against transient receptor potential
            vanilloid 1 attenuates cisplatin-induced hearing loss in the rat
  JOURNAL   J Neurosci 28 (49), 13056-13065 (2008)
   PUBMED   19052196
  REMARK    GeneRIF: These data provide a link between NOX3 and TRPV1 in
            cisplatin-induced hearing loss and suggest that targeting these
            proteins for knockdown by siRNA could serve as a novel approach in
            treating cisplatin ototoxicity.
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Nakano,Y., Banfi,B., Jesaitis,A.J., Dinauer,M.C., Allen,L.A. and
            Nauseef,W.M.
  TITLE     Critical roles for p22phox in the structural maturation and
            subcellular targeting of Nox3
  JOURNAL   Biochem J 403 (1), 97-108 (2007)
   PUBMED   17140397
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Banfi,B., Malgrange,B., Knisz,J., Steger,K., Dubois-Dauphin,M. and
            Krause,K.H.
  TITLE     NOX3, a superoxide-generating NADPH oxidase of the inner ear
  JOURNAL   J Biol Chem 279 (44), 46065-46072 (2004)
   PUBMED   15326186
  REMARK    GeneRIF: NOX3 is a relevant source of ROS generation in the
            cochlear and vestibular systems and that NOX3-dependent ROS
            generation might contribute to hearing loss and balance problems in
            response to ototoxic drugs.
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Fuller,P.M., Jones,T.A., Jones,S.M. and Fuller,C.A.
  TITLE     Evidence for macular gravity receptor modulation of hypothalamic,
            limbic and autonomic nuclei
  JOURNAL   Neuroscience 129 (2), 461-471 (2004)
   PUBMED   15501603
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Fuller,P.M., Jones,T.A., Jones,S.M. and Fuller,C.A.
  TITLE     Neurovestibular modulation of circadian and homeostatic regulation:
            vestibulohypothalamic connection?
  JOURNAL   Proc Natl Acad Sci U S A 99 (24), 15723-15728 (2002)
   PUBMED   12434016
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Jones,S.M., Erway,L.C., Bergstrom,R.A., Schimenti,J.C. and
            Jones,T.A.
  TITLE     Vestibular responses to linear acceleration are absent in
            otoconia-deficient C57BL/6JEi-het mice
  JOURNAL   Hear Res 135 (1-2), 56-60 (1999)
   PUBMED   10491954
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY573239.1.
            
            On Sep 10, 2004 this sequence version replaced XP_217848.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY573239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132265,
                                           SAMD00132268 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..568
                     /product="NADPH oxidase 3"
                     /note="superoxide producing enzyme"
                     /calculated_mol_wt=64286
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Region          95..547
                     /region_name="COG4097"
                     /note="Predicted ferric reductase [Inorganic ion transport
                     and metabolism]"
                     /db_xref="CDD:443273"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Site            238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q672K1.1)"
     Region          295..568
                     /region_name="NOX_Duox_like_FAD_NADP"
                     /note="NADPH oxidase (NOX) catalyzes the generation of
                     reactive oxygen species (ROS) such as superoxide and
                     hydrogen peroxide. ROS were originally identified as
                     bactericidal agents in phagocytes, but are now also
                     implicated in cell signaling and metabolism. NOX...;
                     cd06186"
                     /db_xref="CDD:99783"
     Site            order(322,336..339,352..354,357..360,409)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99783"
     Site            order(336,338..339)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99783"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q672K1.1)"
     Site            404..414
                     /site_type="other"
                     /note="NAD pyrophosphate binding region [chemical
                     binding]"
                     /db_xref="CDD:99783"
     Site            order(404,408..411,413)
                     /site_type="other"
                     /note="beta-alpha-beta stucture motif"
                     /db_xref="CDD:99783"
     Site            order(409..410,442..444,536..537)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99783"
     Site            order(440..441,444)
                     /site_type="other"
                     /note="NADP ribose binding motif [chemical binding]"
                     /db_xref="CDD:99783"
     CDS             1..568
                     /gene="Nox3"
                     /coded_by="NM_001004216.1:1..1707"
                     /db_xref="GeneID:292279"
                     /db_xref="RGD:1303190"
ORIGIN      
        1 mptcwilnes vsfvvallwl ainiylfidt fcwyaeeesf fytrvilgsa lawarasavc
       61 lnfncmlill pvsrnfvslv rgtsvccrgp wrrqldknlk fhklvaygia vnsvihivah
      121 lfnleryhlg qakdaeglla alsklgnapn esylnpvrtl ytgtttqllm tvsgitglvi
      181 slalilimts stefirqssy elfwythhif iflfislaih gggriirgqt peslrlhnvt
      241 fcrdhfdewq eaascpvpqf sgkepsawkw tlgpvvlyac eiiirfwrsh qevvitkvvs
      301 hpsavlelhm kkrdfkmapg qyifiqcpsi splewhpftl tsapqedffs vhirasgdwt
      361 eallkafgae gqapselcsm prlavdgpfg gsladvfhyp vsvciatgig vtpfasllks
      421 vwykccesqs lpglskvyfy wicrdaaafe wfadlllsle tqmseqgkah llsyhiyltg
      481 wdeyqaihia lhwdesldvi tglkqktfyg rpnwneefkq iaynhpsssi gvffcgpkam
      541 sktlqkmcrl ysssdprgvh fyynkenf
//
LOCUS       NP_001001397             308 aa            linear   ROD 02-APR-2025
DEFINITION  olfactory receptor family 12 subfamily D member 2 [Rattus
            norvegicus].
ACCESSION   NP_001001397 XP_227937
VERSION     NP_001001397.1
DBSOURCE    REFSEQ: accession NM_001001397.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BX883052.1.
            
            On Aug 30, 2004 this sequence version replaced XP_227937.2.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This record was generated from the set of rat
            olfactory receptors mined from Rnor3.1 assembly (NCBI Build 2.1).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..308
                     /product="olfactory receptor family 12 subfamily D member
                     2"
                     /note="olfactory receptor 15; olfactory receptor Olr1735;
                     olfactory receptor gene Olr1735; olfactory receptor 1735"
                     /calculated_mol_wt=34932
     Region          23..293
                     /region_name="7tmA_OR12D-like"
                     /note="olfactory receptor subfamily 12D and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15915"
                     /db_xref="CDD:320581"
     Region          24..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320581"
     Region          57..83
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320581"
     Site            order(79,82..83,95..100,102..103,106,151,153..157,193,
                     196..198,200..202,204..205,251,254..255,257..258,261,
                     267..268,270..272,275,278..279)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320581"
     Region          95..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320581"
     Region          138..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320581"
     Region          193..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320581"
     Region          231..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320581"
     Region          268..293
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320581"
     CDS             1..308
                     /gene="Or12d2"
                     /gene_synonym="Olr1735; Or15;
                     ratchr20-1349773-1350699_ORF"
                     /coded_by="NM_001001397.1:1..927"
                     /db_xref="GeneID:294190"
                     /db_xref="RGD:1334001"
ORIGIN      
        1 msnqtsvtef lllgvtdiqe lnpilfviff tiyfvnitgn gailmivild prlhspmyff
       61 lgnlacldic fstvtvpkml enllstskai sflgcitqlh ffhflgstea lllpvmafdr
      121 fvaicrplhy svimnrqlcs hmtvtiwimg flhallhsvm tsrlsfcgpn hvhhffcdik
      181 plldlacgnt elnlwllntv tgtialtpff ltflsyfyii tylflkthsc smlhkalstc
      241 ashfmvvill yvpvlfnyir passsaldqe riiaimysvv tpalnpliyt lrnkevrnal
      301 nkkvrrwl
//
LOCUS       NP_001100661             504 aa            linear   ROD 02-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 37 [Rattus
            norvegicus].
ACCESSION   NP_001100661 XP_001073910 XP_222803
VERSION     NP_001100661.1
DBSOURCE    REFSEQ: accession NM_001107191.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473958.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001073910.1, XP_222803.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..504
                     /product="zinc finger and BTB domain-containing protein
                     37"
                     /calculated_mol_wt=55922
     Region          9..131
                     /region_name="BTB_POZ_ZBTB37"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 37 (ZBTB37); cd18222"
                     /db_xref="CDD:349531"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(382,384,386,388..389,392..393,396,410,412,416..417,
                     420..421,424,438,440,442,444..445,448..449)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          389..414
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          403..425
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          418..440
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          433..451
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..504
                     /gene="Zbtb37"
                     /gene_synonym="RGD1308731"
                     /coded_by="NM_001107191.1:261..1775"
                     /db_xref="GeneID:304918"
                     /db_xref="RGD:1308731"
ORIGIN      
        1 mtmeksgniq leipdfsnsv lshlnqlrmq grlcdivvnv qgqafrahkv vlaasspyfr
       61 dhmslnemst vsisviknpt vfeqllsfcy tgriclqlad iisyltaasf lqmqhiidkc
      121 tqilegihfk invaeveael sqtrtkhper ppeshrvtpn ltrslsprhn askgnwrgqv
      181 savldirels ppeestspqi ieqssdvegr epilrinrag qwyvetgiad qgpqsgdevr
      241 vlgavhikte nleewlgpen qpsgedgssa eevaamvidt tghgsvgqes ytlgssgakv
      301 arptssevdr fspsgsvvsm terhrarses pgrmdepkql ssqveesamm gvsayveylr
      361 eqevserwfr ynprltciyc aksfnqkgsl drhmrlhmgi tpfvcrmcgk kytrkdqley
      421 hirkhtgnkp fhchvcgksf pfqailnqhf rknhpgcipl egphsispet tvtsrqaeeg
      481 spsheetvap gesaqgsvst tgpd
//
LOCUS       NP_001129272             204 aa            linear   ROD 02-APR-2025
DEFINITION  cardiotrophin-2 precursor [Rattus norvegicus].
ACCESSION   NP_001129272 XP_001080300 XP_219355
VERSION     NP_001129272.1
DBSOURCE    REFSEQ: accession NM_001135800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Derouet,D., Rousseau,F., Alfonsi,F., Froger,J., Hermann,J.,
            Barbier,F., Perret,D., Diveu,C., Guillet,C., Preisser,L.,
            Dumont,A., Barbado,M., Morel,A., deLapeyriere,O., Gascan,H. and
            Chevalier,S.
  TITLE     Neuropoietin, a new IL-6-related cytokine signaling through the
            ciliary neurotrophic factor receptor
  JOURNAL   Proc Natl Acad Sci U S A 101 (14), 4827-4832 (2004)
   PUBMED   15051883
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from AY518205.1.
            
            On or before Oct 16, 2008 this sequence version replaced
            XP_219355.2, XP_001080300.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..204
                     /product="cardiotrophin-2 precursor"
                     /note="neuropoietin; cardiotrophin 2, pseudogene"
                     /calculated_mol_wt=19643
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2303
     Region          <41..202
                     /region_name="LIF_OSM"
                     /note="LIF / OSM family; cl21565"
                     /db_xref="CDD:419736"
     CDS             1..204
                     /gene="Ctf2"
                     /gene_synonym="Ctf2p"
                     /coded_by="NM_001135800.1:1..615"
                     /db_xref="GeneID:293515"
                     /db_xref="RGD:1308254"
ORIGIN      
        1 mycllaaplc llslllspls paapispsep igqayslaly mqkntsallq tylqyqgspf
       61 sdpgfsapel qlstlpsaav sfktwhamgd aerlrqaqga flaltqhlql vgddqsdlnp
      121 gspillaqlg aarlraqgll gnmvtimtal glpvppeedt lgivpfgasa ferkcrgyiv
      181 treyghwtdr avrdlallka kypa
//
LOCUS       NP_775432                561 aa            linear   ROD 02-APR-2025
DEFINITION  carbohydrate sulfotransferase 15 [Rattus norvegicus].
ACCESSION   NP_775432
VERSION     NP_775432.3
DBSOURCE    REFSEQ: accession NM_173310.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Karumbaiah,L., Anand,S., Thazhath,R., Zhong,Y., McKeon,R.J. and
            Bellamkonda,R.V.
  TITLE     Targeted downregulation of N-acetylgalactosamine 4-sulfate
            6-O-sulfotransferase significantly mitigates chondroitin sulfate
            proteoglycan-mediated inhibition
  JOURNAL   Glia 59 (6), 981-996 (2011)
   PUBMED   21456043
  REMARK    GeneRIF: Downregulation of N-acetylgalactosamine 4-sulfate
            6-O-sulfotransferase (CS-E) via siRNA targeting of GalNAc4S6ST
            mitigates chondroitin sulfate proteoglycan-mediated inhibition of
            neurons, potentially offering an intervention strategy for brain
            injury.
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Ohtake,S., Ito,Y., Fukuta,M. and Habuchi,O.
  TITLE     Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is
            related to human B cell recombination activating gene-associated
            gene
  JOURNAL   J Biol Chem 276 (47), 43894-43900 (2001)
   PUBMED   11572857
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB086953.1.
            
            On Aug 12, 2007 this sequence version replaced NP_775432.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB086953.1, SRR8487230.151441.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMN14984024
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..561
                     /product="carbohydrate sulfotransferase 15"
                     /EC_number="2.8.2.33"
                     /note="B cell RAG associated protein;
                     N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase;
                     carbohydrate (N-acetylgalactosamine 4-sulfate 6-O)
                     sulfotransferase 15"
                     /calculated_mol_wt=64913
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI9.1)"
     Region          253..>505
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; cl21551"
                     /db_xref="CDD:473908"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI9.1)"
     CDS             1..561
                     /gene="Chst15"
                     /gene_synonym="Galnac4s-6st; GalNAc4S6ST"
                     /coded_by="NM_173310.3:16..1701"
                     /db_xref="GeneID:286974"
                     /db_xref="RGD:628881"
ORIGIN      
        1 mrhcincciq lfpedahkqq vacqggphhs hqacpsckge dkilfrvdsk qmnllavlev
       61 rtegnenwgg flrfrkgkrc slvfgliimt lvmasyilsg ahqellissp fhyggfpsnp
      121 svmdsespsd vkehhyqpsv nnisyvkdyp nikliidsia arnefttrql pdlqdlkrqe
      181 lhmfsvipnk flptskspcw yeefsgrntt dpyltnsyvl yskrfrstfd tlrkafwghl
      241 shvhgkhfrl rclphfyiig qpkcgttdly drlrlhpevk fsaikephww trkrfgivrl
      301 rdglrdrypv edyldlfdla ahqihqglqa asaeqtskmn riiigeasas tmwdnnawtf
      361 fydnstdgep pfltqdfiha fqpeakllvm lrdpverlys dylyfassnk saddfhekvt
      421 ealqlfencm ldyslracvy nntlnnampv rlqvglyavy lldwltvfsk eqflilrled
      481 hasnvkytmh kvfqflnlgp lsekqealmt kspasntrrp edrslgpmwp itqkilrdfy
      541 gpfntrlaqv lddeafawkt t
//
LOCUS       NP_076486                309 aa            linear   ROD 02-APR-2025
DEFINITION  taste receptor type 2 member 114 [Rattus norvegicus].
ACCESSION   NP_076486
VERSION     NP_076486.1
DBSOURCE    REFSEQ: accession NM_023996.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Adler,E., Hoon,M.A., Mueller,K.L., Chandrashekar,J., Ryba,N.J. and
            Zuker,C.S.
  TITLE     A novel family of mammalian taste receptors
  JOURNAL   Cell 100 (6), 693-702 (2000)
   PUBMED   10761934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF227143.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF227143.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..309
                     /product="taste receptor type 2 member 114"
                     /note="T2R114; taste receptor type 2 member 5; taste
                     receptor T2R5"
                     /calculated_mol_wt=35473
     Region          7..291
                     /region_name="7tm_TAS2R10"
                     /note="mammalian taste receptor 2, subtype 10, member of
                     the seven-transmembrane G protein-coupled receptor
                     superfamily; cd15021"
                     /db_xref="CDD:320149"
     Region          8..33
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320149"
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Region          45..69
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320149"
     Region          83..105
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320149"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Site            128..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Region          131..147
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320149"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Region          173..196
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320149"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Region          221..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320149"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     Region          258..283
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320149"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKT8.1)"
     CDS             1..309
                     /gene="Tas2r114"
                     /gene_synonym="T2R5; Tas2r5"
                     /coded_by="NM_023996.1:1..930"
                     /db_xref="GeneID:78982"
                     /db_xref="RGD:620737"
ORIGIN      
        1 mlgamegvll svatseallg ivgntfialv ncmdctrnkn lynigfiltg laisriclvw
       61 iliteayiki fspqllspin iielisylwi itsqlnvwfa tslsifyflk ianfshhifl
      121 wlkrrinivf afligcllms wlfsfpvvvk mvkdkkmlyi nsswqihmkk seliinyvft
      181 nggvfllfii mlivcfllii slwrhskwmq snesgfrdln tevhvktikv llsfiilfil
      241 hligitinvi cllvpennll fvfgltiafl ypcchslili lansrlkrcf vrilqqlmcs
      301 eegkefrnt
//
LOCUS       NP_001004097             246 aa            linear   ROD 02-APR-2025
DEFINITION  trypsin 10 precursor [Rattus norvegicus].
ACCESSION   NP_001004097 XP_579123
VERSION     NP_001004097.1
DBSOURCE    REFSEQ: accession NM_001004097.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000327.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579123.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000327.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760434,
                                           SAMN06621351 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..246
                     /product="trypsin 10 precursor"
                     /function="serine protease"
                     /calculated_mol_wt=24217
     sig_peptide     1..20
                     /calculated_mol_wt=1927
     mat_peptide     21..246
                     /product="trypsin 10"
                     /calculated_mol_wt=24217
     Region          24..242
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            24
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(63,107,200)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(194,215,217)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..246
                     /gene="Try10"
                     /coded_by="NM_001004097.1:1..741"
                     /db_xref="GeneID:408247"
                     /db_xref="RGD:1359400"
ORIGIN      
        1 mnavlilalv gaavafpaad ddkivggytc qensvpyqvs lnsgyhfcgg slineqwvvs
       61 aahcyksriq vrlgehninv legneqfvna akiikhpnfi rktlnndiml iklsspvkln
      121 srvatvalps scapagtqcl isgwgntlsf gvnepdllqc ldapllpqad ceasypgkit
      181 dnmvcagfle ggkdscqgds ggpvvcngel qgivswgygc alpdnpgvyt kvcnyvdwiq
      241 dtiaan
//
LOCUS       NP_036631               2842 aa            linear   ROD 02-APR-2025
DEFINITION  adenomatous polyposis coli protein [Rattus norvegicus].
ACCESSION   NP_036631
VERSION     NP_036631.1
DBSOURCE    REFSEQ: accession NM_012499.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2842)
  AUTHORS   Shirakami,Y., Nakanishi,T., Ozawa,N., Ideta,T., Kochi,T.,
            Kubota,M., Sakai,H., Ibuka,T., Tanaka,T. and Shimizu,M.
  TITLE     Inhibitory effects of a selective prostaglandin E2 receptor
            antagonist RQ-15986 on inflammation-related colon tumorigenesis in
            APC-mutant rats
  JOURNAL   PLoS One 16 (5), e0251942 (2021)
   PUBMED   34003864
  REMARK    GeneRIF: Inhibitory effects of a selective prostaglandin E2
            receptor antagonist RQ-15986 on inflammation-related colon
            tumorigenesis in APC-mutant rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2842)
  AUTHORS   Yuan,B., Wu,W., Zhang,H., Gu,H., Guo,D., Jiang,J. and Wang,X.
  TITLE     Adenomatous polyposis coli as a predictor of environmental
            chemical-induced transgenerational effects related to male
            infertility
  JOURNAL   J Biochem Mol Toxicol 33 (7), e22331 (2019)
   PUBMED   30934153
  REMARK    GeneRIF: the miR-30 family/APC interaction is a potential mechanism
            for the transgenerational effects induced by the environmental
            chemical.
REFERENCE   3  (residues 1 to 2842)
  AUTHORS   Torricelli,F., Nicoli,D., Bellazzi,R., Ciarrocchi,A., Farnetti,E.,
            Mastrofilippo,V., Zamponi,R., La Sala,G.B., Casali,B. and
            Mandato,V.D.
  TITLE     Computational development of a molecular-based approach to improve
            risk stratification of endometrial cancer patients
  JOURNAL   Oncotarget 9 (39), 25517-25528 (2018)
   PUBMED   29876005
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2842)
  AUTHORS   Arif,M., Pandey,R., Alam,P., Jiang,S., Sadayappan,S., Paul,A. and
            Ahmed,R.P.H.
  TITLE     MicroRNA-210-mediated proliferation, survival, and angiogenesis
            promote cardiac repair post myocardial infarction in rodents
  JOURNAL   J Mol Med (Berl) 95 (12), 1369-1385 (2017)
   PUBMED   28948298
REFERENCE   5  (residues 1 to 2842)
  AUTHORS   Council,L.N., Shanmugam,C., Suswam,E.A., Katkoori,V.R.,
            Heslin,M.J., Hanna,A., Jhala,N.C., Varambally,S. and Manne,U.
  TITLE     Association between Hepatitis C Virus Infection, p53 Phenotypes,
            and Gene Variants of Adenomatous Polyposis Coli in Hepatocellular
            Carcinomas
  JOURNAL   J Dig Dis Hepatol 2016 (5) (2016)
   PUBMED   28203651
REFERENCE   6  (residues 1 to 2842)
  AUTHORS   Clarke,A.R., Cummings,M.C. and Harrison,D.J.
  TITLE     Interaction between murine germline mutations in p53 and APC
            predisposes to pancreatic neoplasia but not to increased intestinal
            malignancy
  JOURNAL   Oncogene 11 (9), 1913-1920 (1995)
   PUBMED   7478622
REFERENCE   7  (residues 1 to 2842)
  AUTHORS   Kakiuchi,H., Watanabe,M., Ushijima,T., Toyota,M., Imai,K.,
            Weisburger,J.H., Sugimura,T. and Nagao,M.
  TITLE     Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat
            colon tumors induced by
            2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
  JOURNAL   Proc Natl Acad Sci U S A 92 (3), 910-914 (1995)
   PUBMED   7846077
REFERENCE   8  (residues 1 to 2842)
  AUTHORS   Hulsken,J., Birchmeier,W. and Behrens,J.
  TITLE     E-cadherin and APC compete for the interaction with beta-catenin
            and the cytoskeleton
  JOURNAL   J Cell Biol 127 (6 Pt 2), 2061-2069 (1994)
   PUBMED   7806582
REFERENCE   9  (residues 1 to 2842)
  AUTHORS   Horii,A., Nakatsuru,S., Miyoshi,Y., Ichii,S., Nagase,H., Ando,H.,
            Yanagisawa,A., Tsuchiya,E., Kato,Y. and Nakamura,Y.
  TITLE     Frequent somatic mutations of the APC gene in human pancreatic
            cancer
  JOURNAL   Cancer Res 52 (23), 6696-6698 (1992)
   PUBMED   1423316
REFERENCE   10 (residues 1 to 2842)
  AUTHORS   Moser,A.R., Dove,W.F., Roth,K.A. and Gordon,J.I.
  TITLE     The Min (multiple intestinal neoplasia) mutation: its effect on gut
            epithelial cell differentiation and interaction with a modifier
            system
  JOURNAL   J Cell Biol 116 (6), 1517-1526 (1992)
   PUBMED   1541640
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D38629.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D38629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2842
                     /organism="Rattus norvegicus"
                     /strain="F344/N"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..2842
                     /product="adenomatous polyposis coli protein"
                     /note="adenomatosis polyposis coli; WNT signaling pathway
                     regulator; APC, WNT signaling pathway regulator"
                     /calculated_mol_wt=310403
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <22..>311
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          125..205
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          238..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          338..390
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          391..464
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          451..493
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          457..508
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          463..506
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(497,501,505,540,544,548,584,588,592)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          503..545
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          510..551
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          514..551
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          546..589
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          558..593
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..636
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          601..642
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          637..681
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          647..687
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          651..685
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          682..723
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          689..729
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          693..729
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          724..765
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          730..1017
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          828..877
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          921..942
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          956..988
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1018..1167
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000250|UniProtKB:P25054"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1034..1133
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1040
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1058..1078
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1092..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1188..1249
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1254..>1271
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1280..1365
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          1306..1373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            1357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1398..1474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            1435
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1525..1568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            1565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1584..1609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1635..1658
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1660..1712
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1661..1711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1714..1735
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Site            1714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1744..1837
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1748..1950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            1772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          1864..1891
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          1871..1945
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1963..2010
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            1969
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            1971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2032..2051
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2034..2058
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250|UniProtKB:P25054"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          2043..2067
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            2087
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2148..2173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            2151
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2167..2674
                     /region_name="Basic region.
                     /evidence=ECO:0000250|UniProtKB:P25054"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          2223..2568
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2234..2641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            2260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2475..2842
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000250|UniProtKB:P25054"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2664..2842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          2670..2842
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2674..2842
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000250|UniProtKB:P25054"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Site            2674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2679
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Site            2788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25054; propagated from
                     UniProtKB/Swiss-Prot (P70478.1)"
     Region          2802..2805
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     Region          2840..2842
                     /region_name="PDZ-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P70478.1)"
     CDS             1..2842
                     /gene="Apc"
                     /gene_synonym="RATAPC"
                     /coded_by="NM_012499.1:54..8582"
                     /db_xref="GeneID:24205"
                     /db_xref="RGD:2123"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltelete asnmkevlkq lqgsiedetm
       61 tsgqidller lkefnldsnf pgvklrskms lrsygsregs vssrsgecsp vpmgsfprra
      121 fvngsrestg yleelekers llladldkee kekdwyyaql qnltkridsl pltenfslqt
      181 dmtrrqleye arqiraamee qlgtcqdmek raqrriariq qiekdilrvr qllqsqaaea
      241 erssqskhet asheaerqle gqgvaesnla tsgsgqssaa rvdhetagvl sssgthsapr
      301 rltshlgtkv emvysllsml gthdkddmsr tllamsssqd scismrqsgc lplliqllhg
      361 ndkdsvllgn srgskearar asaalhniih sqpddkrgrr eirvlhlleq iraycetcwe
      421 wqeaheqgmd qdknpmpapv ehqicpavcv lmklsfdeeh rhamnelggl qaiaellqvd
      481 cemhgltddh ysvtlrryag maltnltfgd vankatlcsm kgcmralvaq lksesedlqq
      541 viasvlrnls wradvnskkt lrevgsvkal mecalevkke stlksvlsal wnlsahcten
      601 kadicavdga laflvgtlty rsqtntlaii esgggilrnv ssliatnedh rqilrenncl
      661 qtllqhlksh sltivsnacg tlwnlsarnp kdqealwdmg avsmlknlih skhkmiamgs
      721 aaalrnlman rpakykdani mspgsslpsl hvrkqkalea eldaqhlset fdnidnlspk
      781 ashrskqrhk qnlygdyvfd asrhddnrsd nfntgnmtvl spylnttvlp sssssrgsld
      841 ssrsekdrsl erergiglst yhsatenpgt sskrglqlsa taaqiakvme evsalhtsqd
      901 drspasaael hcvaeertaa rrssashthp nthnfakses snrtcsmpya kveykrssnd
      961 slnsvtssdg ygkrgqmkps vesyseddeg kfcsygqypa dlahkihsan hmddnggeld
     1021 tpinyslkys deqlnsgrqs psqnerwarp khviedeikq neqrqsrsqn tnfpvysent
     1081 ddkhlkfqqh fgqqecvspy rsrgtngset nrmgsshavn qnvnqslcqe ddyeddkptn
     1141 yseryseeeq heeeerptny sikyneekhh vdqpidyslk yatdisssqk psfsfsktps
     1201 vqgtktehns psseaasaps snakrqsqlh pssaqrngqt pkgtackvps inqetmqtyc
     1261 vedtpicfsr csslsslssa edeigcdqtt qeadsantlq iaeikendvt rsaqdpasdv
     1321 pavsqstrtk psrlqasgla sesarhkave fssgakspsk sgaqtpkspp ehyvqetplv
     1381 fsrctsvssl dsfesrsias svqsepcsgm vsgivspsdl pdspgqtmpp srsktppppp
     1441 ppqpvqtkre vpktkvpaae qreggpkqta vsaavqrvqv lpdadtllhf atestpdgfs
     1501 cssslsalsl depfiqkdve lrimppvqen dngnetepeq peesnenqdk evekpdsekd
     1561 llddsddddi eileeciisa mptkssrkak klaqtasklp ppvarkpsql pvykllpsqs
     1621 rlqaqkhvsf tpgddvprvy cvegtpinfs tatslsdlti esppnelaag dgvrasvqsg
     1681 efekrdtipt egrstdeaqr gkvssiaipd ldgskaeegd ilaecinsal pkgrshkpfr
     1741 vkkimdqvqq asmtssgtnk nqidtkkkkp tspvkpmpqn teyrtrvrkn tdskvnvnte
     1801 etfsdnkdsk kqslknnpkd lndklpdned rvrggftfds phhyapiegt pycfsrndsl
     1861 ssldfddddv dlsrekaelr kgkeskdsea kvtchtepss sqqsarkaqa stkhpvnrgp
     1921 skpllqeqpt fpqsskdvpd rgaatdeklq nfaientpvc fsrnsslssl sdvdqennnn
     1981 eetgpvrdae panaqgqpgk pqasgyapks fhvedtpvcf srnsslssls idseddllre
     2041 cissampkkr rpsrlkgege wqsprkvgsv laedltldlk diqrpesehg lspdsenfdw
     2101 kaiqegansi vsslhqaaaa aaclsrqass dsdsilslks gvslgspfhl tpdqeekpft
     2161 shkgprilkp gekstleakk iesenkgikg gkkvykslit gkirsnseis sqmkqplqtn
     2221 mpsisrgrtm ihipgvrnss sstspvskkg pplktpasks psegpvatts prgtkpavks
     2281 elspitrqts hisgsnkgps rsgsrdstps rptqqplsrp mqspgrnsis pgrngistpn
     2341 klsqlprtss pstastkssg sgkmsytspg rqlsqqnlsk qtglsknass iprsesaskg
     2401 lnqmnnsngs nkkvelsrms stkssgsesd rserpalvrq stfikeapsp tlrrkleesa
     2461 sfeslspssr pdsptrsqaq tpvlspslpd mslsthpsvq aggwrklppn lsptieysdg
     2521 rpskrhdiar shsespsrlp vnragtwkre hskhssslpr vstwrrtgss ssilsasses
     2581 sekaksedek hvnsvpgprq mkenqvptkg twrkikesei sptntvsqtt ssgaasgaes
     2641 ktliyqmapa vsrtedvwvr iedcpinnpr sgrsptgntp pvidsisekg npsikdskdt
     2701 qgkqsvgsgs pvqtvglenr lnsfiqveap eqkgtetkag qgspapvaet getcmaertp
     2761 fsssssskhs spsgtvaarv tpfnynpspr kssadstsar psqiptpvgs stkkrdsktd
     2821 stessgaqsp krhsgsylvt sv
//
LOCUS       NP_001041419             224 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC500028 [Rattus norvegicus].
ACCESSION   NP_001041419 XP_001056185 XP_575383
VERSION     NP_001041419.1
DBSOURCE    REFSEQ: accession NM_001047954.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            AY383683.1.
            
            On or before Sep 8, 2006 this sequence version replaced
            XP_575383.1, XP_001056185.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AY383683.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q21"
     Protein         1..224
                     /product="uncharacterized protein LOC500028"
                     /calculated_mol_wt=24805
     Region          9..>72
                     /region_name="fliH"
                     /note="flagellar assembly protein FliH; PRK05687"
                     /db_xref="CDD:235562"
     Region          48..86
                     /region_name="Yae1_N"
                     /note="Essential protein Yae1, N terminal; pfam09811"
                     /db_xref="CDD:430844"
     CDS             1..224
                     /gene="Yae1l1"
                     /coded_by="NM_001047954.1:1..675"
                     /db_xref="GeneID:500028"
                     /db_xref="RGD:1560448"
ORIGIN      
        1 maramswfra tpeipspgeq dvfdeeades llvqrewqdh mrkrvqegyr dgidagkavt
       61 lqqgfnqgyk egadvilnyg llrgtlsall swchlhgnss tligkinnll navgqceecv
      121 ikhlksvtsp pritdlldsi edldlchvvp pekaveargd tsadistdad rspngmdcsh
      181 peccrtqeha hlekpsltwi leqtsnlvkq lgisvdilqh lrql
//
LOCUS       NP_852039                428 aa            linear   ROD 02-APR-2025
DEFINITION  transcription factor Sp7 isoform 2 [Rattus norvegicus].
ACCESSION   NP_852039
VERSION     NP_852039.2
DBSOURCE    REFSEQ: accession NM_181374.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   da Silva Sasso,G.R., Florencio-Silva,R., Sasso-Cerri,E., Gil,C.D.,
            de Jesus Simoes,M. and Cerri,P.S.
  TITLE     Spatio-temporal immunolocalization of VEGF-A, Runx2, and osterix
            during the early steps of intramembranous ossification of the
            alveolar process in rat embryos
  JOURNAL   Dev Biol 478, 133-143 (2021)
   PUBMED   34245724
  REMARK    GeneRIF: Spatio-temporal immunolocalization of VEGF-A, Runx2, and
            osterix during the early steps of intramembranous ossification of
            the alveolar process in rat embryos.
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Pokrovskaya,L.A., Nadezhdin,S.V., Zubareva,E.V., Burda,Y.E. and
            Gnezdyukova,E.S.
  TITLE     Expression of RUNX2 and Osterix in Rat Mesenchymal Stem Cells
            during Culturing in Osteogenic-Conditioned Medium
  JOURNAL   Bull Exp Biol Med 169 (4), 571-575 (2020)
   PUBMED   32910396
  REMARK    GeneRIF: Expression of RUNX2 and Osterix in Rat Mesenchymal Stem
            Cells during Culturing in Osteogenic-Conditioned Medium.
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Qin,G., Li,Y., Wang,H., Yang,J., Chen,Q., Tang,H., Wang,Y.,
            Zhang,M., Jiang,T., Lin,S. and Huo,S.
  TITLE     Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation
            via Regulating the Binding Ability of H3K9me3 with the Promoters of
            Runx2, Osterix and Osteocalcin
  JOURNAL   J Biomed Nanotechnol 16 (6), 899-909 (2020)
   PUBMED   33187585
  REMARK    GeneRIF: Lysine-Specific Demethylase 4A Regulates Osteogenic
            Differentiation via Regulating the Binding Ability of H3K9me3 with
            the Promoters of Runx2, Osterix and Osteocalcin.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Xi,Y., Miao,X., Li,Y., Lai,K., Du,X., Jiang,Z., Wang,Y. and Yang,G.
  TITLE     BMP2-mimicking peptide modified with E7 coupling to calcined bovine
            bone enhanced bone regeneration associating with activation of the
            Runx2/SP7 signaling axis
  JOURNAL   J Biomed Mater Res B Appl Biomater 108 (1), 80-93 (2020)
   PUBMED   30912295
  REMARK    GeneRIF: BMP2-mimicking peptide modified with E7 coupling to
            calcined bovine bone enhanced bone regeneration associating with
            activation of the Runx2/SP7 signaling axis.
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Fukuda,M., Yoshizawa,T., Karim,M.F., Sobuz,S.U., Korogi,W.,
            Kobayasi,D., Okanishi,H., Tasaki,M., Ono,K., Sawa,T., Sato,Y.,
            Chirifu,M., Masuda,T., Nakamura,T., Tanoue,H., Nakashima,K.,
            Kobashigawa,Y., Morioka,H., Bober,E., Ohtsuki,S., Yamagata,Y.,
            Ando,Y., Oike,Y., Araki,N., Takeda,S., Mizuta,H. and Yamagata,K.
  TITLE     SIRT7 has a critical role in bone formation by regulating lysine
            acylation of SP7/Osterix
  JOURNAL   Nat Commun 9 (1), 2833 (2018)
   PUBMED   30026585
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Amorim,B.R., Okamura,H., Yoshida,K., Qiu,L., Morimoto,H. and
            Haneji,T.
  TITLE     The transcriptional factor Osterix directly interacts with RNA
            helicase A
  JOURNAL   Biochem Biophys Res Commun 355 (2), 347-351 (2007)
   PUBMED   17303075
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Wang,B.L., Dai,C.L., Quan,J.X., Zhu,Z.F., Zheng,F., Zhang,H.X.,
            Guo,S.Y., Guo,G., Zhang,J.Y. and Qiu,M.C.
  TITLE     Parathyroid hormone regulates osterix and Runx2 mRNA expression
            predominantly through protein kinase A signaling in osteoblast-like
            cells
  JOURNAL   J Endocrinol Invest 29 (2), 101-108 (2006)
   PUBMED   16610234
  REMARK    GeneRIF: Parathyroid hormone (1-34) regulates osterix mRNA
            expression, in rat osteoblast-like cell line UMR 106, in a dose-
            and time-dependent manner.
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Koga,T., Matsui,Y., Asagiri,M., Kodama,T., de Crombrugghe,B.,
            Nakashima,K. and Takayanagi,H.
  TITLE     NFAT and Osterix cooperatively regulate bone formation
  JOURNAL   Nat Med 11 (8), 880-885 (2005)
   PUBMED   16041384
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Milona,M.A., Gough,J.E. and Edgar,A.J.
  TITLE     Expression of alternatively spliced isoforms of human Sp7 in
            osteoblast-like cells
  JOURNAL   BMC Genomics 4, 43 (2003)
   PUBMED   14604442
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Nakashima,K., Zhou,X., Kunkel,G., Zhang,Z., Deng,J.M.,
            Behringer,R.R. and de Crombrugghe,B.
  TITLE     The novel zinc finger-containing transcription factor osterix is
            required for osteoblast differentiation and bone formation
  JOURNAL   Cell 108 (1), 17-29 (2002)
   PUBMED   11792318
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK001412.1.
            
            On Dec 23, 2004 this sequence version replaced NP_852039.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..428
                     /product="transcription factor Sp7 isoform 2"
                     /note="osterix; Transcription factor Sp7"
                     /calculated_mol_wt=44519
     Region          2..292
                     /region_name="SP6-9_N"
                     /note="N-terminal domains of transcription factor
                     Specificity Proteins (SP) 6-9, and similar proteins;
                     cl41771"
                     /db_xref="CDD:425402"
     Region          296..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(300,302,304,306..307,310..311,314,330,332,336..337,
                     340..341,344,358,360,362,364..365,368..369,372)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          307..334
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          323..345
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          337..362
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..428
                     /gene="Sp7"
                     /gene_synonym="Osx"
                     /coded_by="NM_181374.2:99..1385"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300260"
                     /db_xref="RGD:631377"
ORIGIN      
        1 masslleeea hygssplaml taacskfggs splrdstalg kggtkkpytd lsapktmgda
       61 ypapfsstng llspagsppa pasgyandyp pfphsfpgpt gaqdpgllvp kghsssdclp
      121 svytsldmsh pygswykagi hagispgpgn tptpwwdmhp ggnwlgggqg qgdglqgtls
      181 tgpaqpplnp qlptypsdfa plnpapypap hllqpgpqhv lpqdvykpka vgnsgqlegs
      241 gagkpprgag tggsggyags gagrstcdcp ncqelerlga aaaglrkkpi hschipgcgk
      301 vygkashlka hlrwhtgerp fvcnwlfcgk rftrsdeler hvrthtrekk ftcllcskrf
      361 trsdhlskhq rthgepgpgp ppsgpkelge grsvgeeean qpprsstspa ppekapggsp
      421 eqsnllei
//
LOCUS       NP_001155163             400 aa            linear   ROD 02-APR-2025
DEFINITION  retinoic acid early transcript 1L like 1 [Rattus norvegicus].
ACCESSION   NP_001155163 XP_001054610
VERSION     NP_001155163.1
DBSOURCE    REFSEQ: accession NM_001161691.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Zhuo,M., Fujiki,M., Wang,M., Piard-Ruster,K., Wai,L.E., Wei,L.,
            Martinez,O.M. and Krams,S.M.
  TITLE     Identification of the rat NKG2D ligands, RAE1L and RRLT, and their
            role in allograft rejection
  JOURNAL   Eur J Immunol 40 (6), 1748-1757 (2010)
   PUBMED   20306467
  REMARK    GeneRIF: We cloned and expressed two rat NKG2D ligands RAE1L and
            RRLT, and demonstrate that these ligands can induce IFN-gamma
            secretion and cytotoxicity by rat NK cells
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Savithri,B. and Khar,A.
  TITLE     A transmembrane-anchored rat RAE-1-like transcript as a ligand for
            NKR-P2, the rat ortholog of human and mouse NKG2D
  JOURNAL   Eur J Immunol 36 (1), 107-117 (2006)
   PUBMED   16323246
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from FJ971664.1.
            
            On Jun 12, 2009 this sequence version replaced XP_001054610.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ971664.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..400
                     /product="retinoic acid early transcript 1L like 1"
                     /note="Rae-1-like protein"
                     /calculated_mol_wt=44654
     Region          106..279
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     CDS             1..400
                     /gene="Raet1ll1"
                     /gene_synonym="Rrlt"
                     /coded_by="NM_001161691.1:1..1203"
                     /db_xref="GeneID:679825"
                     /db_xref="RGD:1583663"
ORIGIN      
        1 meggvqapsl tgrpsrvavi ltegqasykv pdncwsysvg drhfreslsg ilcgaaqnph
       61 gfsqlrshll lragmaenta aehplftgas cvlvflsclg stlcadvhsl scnliirspt
      121 kaeplwyegq csmdgnvfls snnvnktmpl gnqekmanat evwtcltqwi drckqdlrdk
      181 vseikgdttk tsghptlrvt mlsnhsheqi igascvfnis enysfildlk tmkwklinpv
      241 pedimkewkd dktlmkhlnl fivecspkfn eflnqheert rsttrapdit qppptsqvpy
      301 kevlipvgli isiifiiflc icvkrmccph ggrelqllkd ycinwhkpqr negleetkge
      361 vpnqrtkmls qeedpktlgg prrasesvel elqmfsstgs
//
LOCUS       NP_001009975             358 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 7c [Rattus norvegicus].
ACCESSION   NP_001009975 XP_579328
VERSION     NP_001009975.1
DBSOURCE    REFSEQ: accession NM_001009975.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Fleischer,J., Schwarzenbacher,K. and Breer,H.
  TITLE     Expression of trace amine-associated receptors in the Grueneberg
            ganglion
  JOURNAL   Chem Senses 32 (6), 623-631 (2007)
   PUBMED   17556730
  REMARK    GeneRIF: Expression of Taar family members is limited to specific
            tissue subpopulations and developmental stages in mouse.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702320.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579328.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..358
                     /product="trace amine-associated receptor 7c"
                     /note="taR-7c; trace amine receptor 7c; trace amine
                     associated receptor 7c"
                     /calculated_mol_wt=40172
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD21.1)"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          49..337
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          50..74
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          83..105
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          121..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            126..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          166..182
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          210..233
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          272..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     Region          305..330
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            310..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD21.1)"
     CDS             1..358
                     /gene="Taar7c"
                     /coded_by="NM_001009975.1:1..1077"
                     /db_xref="GeneID:494535"
                     /db_xref="RGD:1359258"
ORIGIN      
        1 matdddsfpw dqdsilsrdl lsasslqlcy enlnrscvrs pyspgsrlil yavfgfgavl
       61 avcgnllvmt silhfrqlhs panflvasla cadllvgltv mpfsmvrsve gcwyfgntyc
      121 kfhscfegsf cysslfhlcf isldryiavs dpliyptrft asisgkcitf swllsiiysf
      181 sllytganea gledlvsalt cvggcqvavn qswvfinfll flvpalvmmt vyskifliak
      241 qqaqniekms kqtarasesy kdrvakrerk aaktlgiava afllswlpyf idsiidaflg
      301 fitptymyei lvwivyynsa mnpliyaffy pwfrkaikli vtgkilrens stinlfpe
//
LOCUS       NP_071525                437 aa            linear   ROD 02-APR-2025
DEFINITION  5-hydroxytryptamine receptor 3B precursor [Rattus norvegicus].
ACCESSION   NP_071525
VERSION     NP_071525.1
DBSOURCE    REFSEQ: accession NM_022189.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Enoch,M.A., Gorodetsky,E., Hodgkinson,C., Roy,A. and Goldman,D.
  TITLE     Functional genetic variants that increase synaptic serotonin and
            5-HT3 receptor sensitivity predict alcohol and drug dependence
  JOURNAL   Mol Psychiatry 16 (11), 1139-1146 (2011)
   PUBMED   20838391
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Ge,Q.F. and Zhang,H.Y.
  TITLE     [Effects of Chinese herbal medicines for regulating liver qi on
            expression of 5-hydroxytryptamine 3B receptor in hypothalamic
            tissues of rats with anger emotion]
  JOURNAL   Zhong Xi Yi Jie He Xue Bao 9 (8), 871-877 (2011)
   PUBMED   21849148
  REMARK    GeneRIF: Chinese herbal medicines for regulating liver qi may treat
            anger emotion in rats by improving the hypothalamic 5-HT3BR protein
            and gene expression levels.
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Doucet,E., Latremoliere,A., Darmon,M., Hamon,M. and Emerit,M.B.
  TITLE     Immunolabelling of the 5-HT 3B receptor subunit in the central and
            peripheral nervous systems in rodents
  JOURNAL   Eur J Neurosci 26 (2), 355-366 (2007)
   PUBMED   17650111
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Yamada,K., Hattori,E., Iwayama,Y., Ohnishi,T., Ohba,H., Toyota,T.,
            Takao,H., Minabe,Y., Nakatani,N., Higuchi,T., Detera-Wadleigh,S.D.
            and Yoshikawa,T.
  TITLE     Distinguishable haplotype blocks in the HTR3A and HTR3B region in
            the Japanese reveal evidence of association of HTR3B with female
            major depression
  JOURNAL   Biol Psychiatry 60 (2), 192-201 (2006)
   PUBMED   16487942
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Reeves,D.C. and Lummis,S.C.
  TITLE     Detection of human and rodent 5-HT3B receptor subunits by
            anti-peptide polyclonal antibodies
  JOURNAL   BMC Neurosci 7, 27 (2006)
   PUBMED   16571125
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Morales,M. and Wang,S.D.
  TITLE     Differential composition of 5-hydroxytryptamine3 receptors
            synthesized in the rat CNS and peripheral nervous system
  JOURNAL   J Neurosci 22 (15), 6732-6741 (2002)
   PUBMED   12151552
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hanna,M.C., Davies,P.A., Hales,T.G. and Kirkness,E.F.
  TITLE     Evidence for expression of heteromeric serotonin 5-HT(3) receptors
            in rodents
  JOURNAL   J Neurochem 75 (1), 240-247 (2000)
   PUBMED   10854267
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Davies,P.A., Pistis,M., Hanna,M.C., Peters,J.A., Lambert,J.J.,
            Hales,T.G. and Kirkness,E.F.
  TITLE     The 5-HT3B subunit is a major determinant of serotonin-receptor
            function
  JOURNAL   Nature 397 (6717), 359-363 (1999)
   PUBMED   9950429
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF155044.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF155044.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132271 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..437
                     /product="5-hydroxytryptamine receptor 3B precursor"
                     /note="serotonin-gated ion channel subunit; 5-HT3B;
                     5-HT-3B; serotonin receptor 3B; 5-HT3-B;
                     5-hydroxytryptamine (serotonin) receptor 3B, ionotropic"
                     /calculated_mol_wt=48183
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ16.1)"
                     /calculated_mol_wt=2171
     mat_peptide     22..437
                     /product="5-hydroxytryptamine receptor 3B.
                     /id=PRO_0000312291"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
                     /calculated_mol_wt=48183
     Region          25..233
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Site            order(63,65,71..72,79,101,103,112..113,115,117..118,
                     128..130,132,142,144,146,150,172)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Region          236..432
                     /region_name="LGIC_TM_5-HT3"
                     /note="transmembrane domain of 5-hydroxytryptamine 3
                     (5-HT3) receptor; cd19063"
                     /db_xref="CDD:349865"
     Region          236..260
                     /region_name="TM1 helix"
                     /note="TM1 helix [structural motif]"
                     /db_xref="CDD:349865"
     Site            236..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Site            order(248,252,255,258..260,264..265,267..269,271..272,
                     274..276,278,282..283,289..290,306,310,313..314,317,
                     320..321,324,402,406)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349865"
     Site            267..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Region          268..289
                     /region_name="TM2 helix"
                     /note="TM2 helix [structural motif]"
                     /db_xref="CDD:349865"
     Site            296..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Region          300..322
                     /region_name="TM3 helix"
                     /note="TM3 helix [structural motif]"
                     /db_xref="CDD:349865"
     Region          377..409
                     /region_name="HA-stretch, determines single-channel
                     conductance in 5-HT3 receptors.
                     /evidence=ECO:0000250|UniProtKB:O95264"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
     Region          407..429
                     /region_name="TM4 helix"
                     /note="TM4 helix [structural motif]"
                     /db_xref="CDD:349865"
     Site            411..434
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ16.1)"
     CDS             1..437
                     /gene="Htr3b"
                     /coded_by="NM_022189.1:33..1346"
                     /db_xref="GeneID:58963"
                     /db_xref="RGD:61820"
ORIGIN      
        1 millwscllv avvgilgtat pqpgnsslhr ltrqllqqyh kevrpvynwa eattvyldlc
       61 vhavldvdvq nqklktsmwy revwndefls wnsslfddiq eislplsaiw apdiiinefv
      121 dverspdlpy vyvnssgtir nhkpiqvvsa cslqtyafpf diqncsltfn silhtvedid
      181 lgflrnqedi endkrsflnd sewqllsvts tyhirqssag dfaqirfnvv irrcplayvv
      241 sllipsiflm lvdlgsfylp pncrarivfk tnvlvgytvf rvnmsdevpr sagctsligv
      301 fftvcmallv lslsksilli kflyeerhse qerplmclrg dsdanesrly lrapcaedte
      361 spvrqehqvp sdtlkdfwfq lqsinnslrt rdqvyqkeve wlailchfdq llfriylavl
      421 glytvtlcsl walwsrm
//
LOCUS       NP_001094487             263 aa            linear   ROD 02-APR-2025
DEFINITION  uncharacterized protein LOC688090 precursor [Rattus norvegicus].
ACCESSION   NP_001094487 XP_001081089
VERSION     NP_001094487.1
DBSOURCE    REFSEQ: accession NM_001101017.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Tuncel,J., Haag,S., Yau,A.C., Norin,U., Baud,A., Lonnblom,E.,
            Maratou,K., Ytterberg,A.J., Ekman,D., Thordardottir,S.,
            Johannesson,M., Gillett,A., Stridh,P., Jagodic,M., Olsson,T.,
            Fernandez-Teruel,A., Zubarev,R.A., Mott,R., Aitman,T.J., Flint,J.
            and Holmdahl,R.
  CONSRTM   EURATRANS Consortium
  TITLE     Natural polymorphisms in Tap2 influence negative selection and
            CD4ratioCD8 lineage commitment in the rat
  JOURNAL   PLoS Genet 10 (2), e1004151 (2014)
   PUBMED   24586191
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Ettinger,R.A., Moustakas,A.K. and Lobaton,S.D.
  TITLE     Open reading frame sequencing and structure-based alignment of
            polypeptides encoded by RT1-Bb, RT1-Ba, RT1-Db, and RT1-Da alleles
  JOURNAL   Immunogenetics 56 (8), 585-596 (2004)
   PUBMED   15517241
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Fujii,H., Kakinuma,M., Yoshiki,T. and Natori,T.
  TITLE     Polymorphism of the class II gene of rat major histocompatibility
            complex, RT1: partial sequence comparison of the first domain of
            the RT1.B beta 1 alleles
  JOURNAL   Immunogenetics 33 (5-6), 399-403 (1991)
   PUBMED   1904838
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            AY626184.1.
            
            On Aug 13, 2007 this sequence version replaced XP_001081089.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY626181.1, AY626184.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rattus norvegicus"
                     /strain="SHR/NCrlBR"
                     /db_xref="taxon:10116"
                     /chromosome="20"
     Protein         1..263
                     /product="uncharacterized protein LOC688090 precursor"
                     /note="MHC class II antigen RT1.B beta chain"
                     /calculated_mol_wt=27147
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2729
     Region          40..109
                     /region_name="MHC_II_beta"
                     /note="Class II histocompatibility antigen, beta domain;
                     smart00921"
                     /db_xref="CDD:197989"
     Region          121..216
                     /region_name="IgC1_MHC_II_beta_HLA-DQ_I-A"
                     /note="Class II major histocompatibility complex (MHC)
                     beta chain immunoglobulin domain of histocompatibility
                     antigen (HLA) DQ and I-A; member of the C1-set of Ig
                     superfamily (IgSF) domains; cd21001"
                     /db_xref="CDD:409592"
     Region          122..130
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409592"
     Site            order(128,146..147,149,175..182)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409592"
     Region          140..149
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409592"
     Site            order(149,177..179,181)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409592"
     Region          153..159
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409592"
     Region          161..164
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409592"
     Region          168..176
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409592"
     Region          179..189
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409592"
     Region          196..203
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409592"
     Region          210..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409592"
     CDS             1..263
                     /gene="LOC688090"
                     /gene_synonym="Bb; RT1-Bb"
                     /coded_by="NM_001101017.1:1..792"
                     /db_xref="GeneID:688090"
                     /db_xref="RGD:1593573"
ORIGIN      
        1 malqtpsfll paavvvlmvl sspgtegrds prdfvyqfeg qcyytngtqr mrlvtrhiyn
       61 reeyvrfdsd lgeyraltel grpsaeywnk qyleqtrael drvcrynyeg paaltslrrl
      121 eqpnvaisls rtealnhhnl lvcsvtdfyp aqikvrwfrn gqeettgvvs tqlirngdwt
      181 fqilvmlemt pqrgdvytch vdhpslespv tvewraqses aqskmlsgig gfvlgviflg
      241 lglfihhksq kgprgpppag llq
//
LOCUS       NP_599155                332 aa            linear   ROD 02-APR-2025
DEFINITION  trace amine-associated receptor 1 [Rattus norvegicus].
ACCESSION   NP_599155
VERSION     NP_599155.1
DBSOURCE    REFSEQ: accession NM_134328.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Raony,I., Domith,I., Lourenco,M.V., Paes-de-Carvalho,R. and
            Pandolfo,P.
  TITLE     Trace amine-associated receptor 1 modulates motor hyperactivity,
            cognition, and anxiety-like behavior in an animal model of ADHD
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 117, 110555 (2022)
   PUBMED   35346791
  REMARK    GeneRIF: Trace amine-associated receptor 1 modulates motor
            hyperactivity, cognition, and anxiety-like behavior in an animal
            model of ADHD.
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Liu,J.F., Siemian,J.N., Seaman,R. Jr., Zhang,Y. and Li,J.X.
  TITLE     Role of TAAR1 within the Subregions of the Mesocorticolimbic
            Dopaminergic System in Cocaine-Seeking Behavior
  JOURNAL   J Neurosci 37 (4), 882-892 (2017)
   PUBMED   28123023
  REMARK    GeneRIF: TAAR1 in different subregions of the mesocorticolimbic
            system contributes to reinstatement of cocaine-seeking behavior.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   De Gregorio,D., Posa,L., Ochoa-Sanchez,R., McLaughlin,R.,
            Maione,S., Comai,S. and Gobbi,G.
  TITLE     The hallucinogen d-lysergic diethylamide (LSD) decreases dopamine
            firing activity through 5-HT1A, D2 and TAAR1 receptors
  JOURNAL   Pharmacol Res 113 (Pt A), 81-91 (2016)
   PUBMED   27544651
  REMARK    GeneRIF: Pretreatment with the trace amine-associate receptor 1
            (TAAR1) antagonist EPPTB (5mg/kg, i.v.) blocked the inhibitory
            effect of LSD on VTA DA neurons.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Harmeier,A., Obermueller,S., Meyer,C.A., Revel,F.G., Buchy,D.,
            Chaboz,S., Dernick,G., Wettstein,J.G., Iglesias,A., Rolink,A.,
            Bettler,B. and Hoener,M.C.
  TITLE     Trace amine-associated receptor 1 activation silences GSK3beta
            signaling of TAAR1 and D2R heteromers
  JOURNAL   Eur Neuropsychopharmacol 25 (11), 2049-2061 (2015)
   PUBMED   26372541
  REMARK    GeneRIF: Results demonstrate that betaArr2 signaling may be an
            important pathway for TAAR1 function and that the activation of the
            TAAR1-D2R complex negatively modulates GSK3b signaling
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Staubert,C., Bohnekamp,J. and Schoneberg,T.
  TITLE     Determinants involved in subtype-specific functions of rat trace
            amine-associated receptors 1 and 4
  JOURNAL   Br J Pharmacol 168 (5), 1266-1278 (2013)
   PUBMED   23072560
  REMARK    GeneRIF: The different functionality of rat Taar subtypes 1 and 4
            mainly correlates with receptor's cell surface expression rather
            than with specific amino acid residues involved in ligand binding
            specificity.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Miller,G.M.
  TITLE     The emerging role of trace amine-associated receptor 1 in the
            functional regulation of monoamine transporters and dopaminergic
            activity
  JOURNAL   J Neurochem 116 (2), 164-176 (2011)
   PUBMED   21073468
  REMARK    GeneRIF: Overview focuses on recent studies which reveal a role for
            TAAR1 in the functional regulation of monoamine transporters and
            the neuronal regulatory mechanisms that modulate dopaminergic
            activity. [review]
            Review article
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Kitahama,K., Araneda,S., Geffard,M., Sei,H. and Okamura,H.
  TITLE     Tyramine-immunoreactive neuronal structures in the rat brain:
            abundance in the median eminence of the mediobasal hypothalamus
  JOURNAL   Neurosci Lett 383 (3), 215-219 (2005)
   PUBMED   15955414
  REMARK    GeneRIF: The Tyramine highly concentrated in the median eminence of
            the mediobasal hypothalamus, in which its physiological function on
            prolactin release has been demonstrated.
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Bunzow,J.R., Sonders,M.S., Arttamangkul,S., Harrison,L.M.,
            Zhang,G., Quigley,D.I., Darland,T., Suchland,K.L., Pasumamula,S.,
            Kennedy,J.L., Olson,S.B., Magenis,R.E., Amara,S.G. and Grandy,D.K.
  TITLE     Amphetamine, 3,4-methylenedioxymethamphetamine, lysergic acid
            diethylamide, and metabolites of the catecholamine
            neurotransmitters are agonists of a rat trace amine receptor
  JOURNAL   Mol Pharmacol 60 (6), 1181-1188 (2001)
   PUBMED   11723224
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF421352.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF421352.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..332
                     /product="trace amine-associated receptor 1"
                     /calculated_mol_wt=37905
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y9.1)"
     Site            16
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          25..312
                     /region_name="7tmA_TAAR1"
                     /note="trace amine-associated receptor 1 and similar
                     receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15314"
                     /db_xref="CDD:320438"
     Region          25..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320438"
     Site            25..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          57..83
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320438"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          95..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320438"
     Site            order(98,102..103,106..107,183,190,193..194,197,261,
                     264..265,268,283,287,291)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320438"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          137..160
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320438"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          186..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320438"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          241..271
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320438"
     Site            250..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     Region          280..305
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320438"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y9.1)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y9.1)"
     CDS             1..332
                     /gene="Taar1"
                     /gene_synonym="taR-1; Tar1; Trar1"
                     /coded_by="NM_134328.1:1..999"
                     /db_xref="GeneID:113914"
                     /db_xref="RGD:621621"
ORIGIN      
        1 mhlchnsani shtnsnwsrd vraslyslis liilttlvgn liviisishf kqlhtptnwl
       61 lhsmavvdfl lgclvmpysm vrtvehcwyf gelfcklhts tdimlssasi lhlafisidr
      121 yyavcdplry kakinlaaif vmiliswslp avfafgmifl elnlegveeq yhnqvfclrg
      181 cfpffskvsg vlafmtsfyi pgsvmlfvyy riyfiakgqa rsinranlqv glegesrapq
      241 sketkaaktl gimvgvfllc wcpfffcmvl dpflgyvipp tlndtlnwfg ylnsafnpmv
      301 yaffypwfrr alkmvlfgki fqkdssrskl fl
//
LOCUS       NP_001102731             391 aa            linear   ROD 02-APR-2025
DEFINITION  paired box protein Pax-5 [Rattus norvegicus].
ACCESSION   NP_001102731 XP_001070941 XP_575815
VERSION     NP_001102731.1
DBSOURCE    REFSEQ: accession NM_001109261.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ohtsuka,N., Badurek,S., Busslinger,M., Benes,F.M., Minichiello,L.
            and Rudolph,U.
  TITLE     GABAergic neurons regulate lateral ventricular development via
            transcription factor Pax5
  JOURNAL   Genesis 51 (4), 234-245 (2013)
   PUBMED   23349049
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Rajan,S., Chu Pham Dang,H., Djambazian,H., Zuzan,H., Fedyshyn,Y.,
            Ketela,T., Moffat,J., Hudson,T.J. and Sladek,R.
  TITLE     Analysis of early C2C12 myogenesis identifies stably and
            differentially expressed transcriptional regulators whose
            knock-down inhibits myoblast differentiation
  JOURNAL   Physiol Genomics 44 (2), 183-197 (2012)
   PUBMED   22147266
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Holmes,M.L., Carotta,S., Corcoran,L.M. and Nutt,S.L.
  TITLE     Repression of Flt3 by Pax5 is crucial for B-cell lineage commitment
  JOURNAL   Genes Dev 20 (8), 933-938 (2006)
   PUBMED   16618805
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Johnson,K., Pflugh,D.L., Yu,D., Hesslein,D.G., Lin,K.I.,
            Bothwell,A.L., Thomas-Tikhonenko,A., Schatz,D.G. and Calame,K.
  TITLE     B cell-specific loss of histone 3 lysine 9 methylation in the V(H)
            locus depends on Pax5
  JOURNAL   Nat Immunol 5 (8), 853-861 (2004)
   PUBMED   15258579
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Wu,C.X., Zhao,W.P., Kishi,H., Dokan,J., Jin,Z.X., Wei,X.C.,
            Yokoyama,K.K. and Muraguchi,A.
  TITLE     Activation of mouse RAG-2 promoter by Myc-associated zinc finger
            protein
  JOURNAL   Biochem Biophys Res Commun 317 (4), 1096-1102 (2004)
   PUBMED   15094381
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Merluzzi,S., Moretti,M., Altamura,S., Zwollo,P., Sigvardsson,M.,
            Vitale,G. and Pucillo,C.
  TITLE     CD40 stimulation induces Pax5/BSAP and EBF activation through a
            APE/Ref-1-dependent redox mechanism
  JOURNAL   J Biol Chem 279 (3), 1777-1786 (2004)
   PUBMED   14594818
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Jin,Z.X., Kishi,H., Wei,X.C., Matsuda,T., Saito,S. and Muraguchi,A.
  TITLE     Lymphoid enhancer-binding factor-1 binds and activates the
            recombination-activating gene-2 promoter together with c-Myb and
            Pax-5 in immature B cells
  JOURNAL   J Immunol 169 (7), 3783-3792 (2002)
   PUBMED   12244173
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473962.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_575815.2, XP_001070941.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680425
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..391
                     /product="paired box protein Pax-5"
                     /calculated_mol_wt=42104
     Region          16..140
                     /region_name="PAX"
                     /note="Paired Box domain; smart00351"
                     /db_xref="CDD:128645"
     Site            order(21..22,27,29..31,33,38,50,52,61,64,66..67,71,80..86,
                     88..91,110..112,131,133..134,137,140)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238076"
     Region          279..390
                     /region_name="Pax2_C"
                     /note="Paired-box protein 2 C terminal; pfam12403"
                     /db_xref="CDD:463563"
     CDS             1..391
                     /gene="Pax5"
                     /gene_synonym="RGD1565236"
                     /coded_by="NM_001109261.1:33..1208"
                     /db_xref="GeneID:500453"
                     /db_xref="RGD:1565236"
ORIGIN      
        1 mdleknyptp rtirtghggv nqlggvfvng rplpdvvrqr ivelahqgvr pcdisrqlrv
       61 shgcvskilg ryyetgsikp gviggskpkv atpkvvekia eykrqnptmf aweirdrlla
      121 ervcdndtvp svssinriir tkvqqppnqp vpasshsivs tgsvtqvssv stdsagssys
      181 isgilgitsp sadtnkrkrd egiqespvpn ghslpgrdfl rkqmrgdlft qqqlevldrv
      241 ferqhysdif tttepikpeq tteysamasl agslddmkan ltsptpadig ssvpgpqsyp
      301 ivtgrdlast tlpgypphvp pagqgsysap tltgmvpgse fsgspyshpq yssyndswrf
      361 pnpgllgspy yysaaargaa ppaaataydr h
//
LOCUS       NP_065412                386 aa            linear   ROD 02-APR-2025
DEFINITION  urotensin-2 receptor [Rattus norvegicus].
ACCESSION   NP_065412
VERSION     NP_065412.1
DBSOURCE    REFSEQ: accession NM_020537.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ajiboye,B.O., Oyinloye,B.E., Onikanni,S.A., Osukoya,O.A.,
            Lawal,O.E. and Bamisaye,F.A.
  TITLE     Sterculia tragacantha Lindl Aqueous Leaf Extract Ameliorate
            Cardiomyopathy in Streptozotocin-induced Diabetic Rats via
            Urotensin II and FABP3 Expressions
  JOURNAL   J Oleo Sci 70 (12), 1805-1814 (2021)
   PUBMED   34866110
  REMARK    GeneRIF: Sterculia tragacantha Lindl Aqueous Leaf Extract
            Ameliorate Cardiomyopathy in Streptozotocin-induced Diabetic Rats
            via Urotensin II and FABP3 Expressions.
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Cadirci,E., Halici,Z., Yayla,M., Toktay,E., Bayir,Y., Karakus,E.,
            Topcu,A., Buyuk,B. and Albayrak,A.
  TITLE     Blocking of urotensin receptors as new target for treatment of
            carrageenan induced inflammation in rats
  JOURNAL   Peptides 82, 35-43 (2016)
   PUBMED   27208703
  REMARK    GeneRIF: This study investigated possible role of U-II and its
            receptor expression in inflammation by using UTR agonist and
            antagonist in carrageenan induced acute inflammation
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Liu,L.M., Liang,D.Y., Ye,C.G., Tu,W.J. and Zhu,T.
  TITLE     The UII/UT system mediates upregulation of proinflammatory
            cytokines through p38 MAPK and NF-kappaB pathways in LPS-stimulated
            Kupffer cells
  JOURNAL   PLoS One 10 (3), e0121383 (2015)
   PUBMED   25803040
  REMARK    GeneRIF: The UII/UT system mediates upregulation of proinflammatory
            cytokines through p38 MAPK and NF-kappaB pathways in LPS-stimulated
            Kupffer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Sainsily,X., Cabana,J., Holleran,B.J., Escher,E., Lavigne,P. and
            Leduc,R.
  TITLE     Identification of transmembrane domain 1 & 2 residues that
            contribute to the formation of the ligand-binding pocket of the
            urotensin-II receptor
  JOURNAL   Biochem Pharmacol 92 (2), 280-288 (2014)
   PUBMED   25175740
  REMARK    GeneRIF: Key transmembrane domain 1 and 2 residues were identified
            in urotensin-II receptor (UT) that participate in the formation of
            the UT receptor binding pocket.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Tian,L., Li,Y., Hua,W., Jia,Y., Zhou,M., Gu,Y. and Qi,J.
  TITLE     Expression of Urotensin II During Focal Cerebral Ischemic in
            Diabetic Rats
  JOURNAL   Can J Neurol Sci 41 (4), 498-503 (2014)
   PUBMED   24878476
  REMARK    GeneRIF: Expression of GPR14 was increased at mRNA and protein
            levels in brain from cerebral ischemia rats.
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Sugo,T., Murakami,Y., Shimomura,Y., Harada,M., Abe,M.,
            Ishibashi,Y., Kitada,C., Miyajima,N., Suzuki,N., Mori,M. and
            Fujino,M.
  TITLE     Identification of urotensin II-related peptide as the urotensin
            II-immunoreactive molecule in the rat brain
  JOURNAL   Biochem Biophys Res Commun 310 (3), 860-868 (2003)
   PUBMED   14550283
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Boucard,A.A., Sauve,S.S., Guillemette,G., Escher,E. and Leduc,R.
  TITLE     Photolabelling the rat urotensin II/GPR14 receptor identifies a
            ligand-binding site in the fourth transmembrane domain
  JOURNAL   Biochem J 370 (Pt 3), 829-838 (2003)
   PUBMED   12495432
  REMARK    GeneRIF: Results indicate that position 6 of urotensin-II normally
            occupied by phenylalanine would interact with Met(184) and/or
            Met(185) of the fourth transmembrane domain of the urotensin-II
            receptor (GPR14).
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Liu,Q., Pong,S.S., Zeng,Z., Zhang,Q., Howard,A.D., Williams,D.L.
            Jr., Davidoff,M., Wang,R., Austin,C.P., McDonald,T.P., Bai,C.,
            George,S.R., Evans,J.F. and Caskey,C.T.
  TITLE     Identification of urotensin II as the endogenous ligand for the
            orphan G-protein-coupled receptor GPR14
  JOURNAL   Biochem Biophys Res Commun 266 (1), 174-178 (1999)
   PUBMED   10581185
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Marchese,A., Heiber,M., Nguyen,T., Heng,H.H., Saldivia,V.R.,
            Cheng,R., Murphy,P.M., Tsui,L.C., Shi,X., Gregor,P. et al.
  TITLE     Cloning and chromosomal mapping of three novel genes, GPR9, GPR10,
            and GPR14, encoding receptors related to interleukin 8,
            neuropeptide Y, and somatostatin receptors
  JOURNAL   Genomics 29 (2), 335-344 (1995)
   PUBMED   8666380
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Tal,M., Ammar,D.A., Karpuj,M., Krizhanovsky,V., Naim,M. and
            Thompson,D.A.
  TITLE     A novel putative neuropeptide receptor expressed in neural tissue,
            including sensory epithelia
  JOURNAL   Biochem Biophys Res Commun 209 (2), 752-759 (1995)
   PUBMED   7733947
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB012210.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AB029611.1, AB012210.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..386
                     /product="urotensin-2 receptor"
                     /note="urotensin II receptor; UR-II-R; G-protein coupled
                     receptor 14; G-protein coupled sensory epithelial
                     neuropeptide-like receptor; putative G protein-coupled
                     receptor (SENR)"
                     /calculated_mol_wt=42576
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49684.2)"
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49684.2)"
     Region          54..328
                     /region_name="7tmA_UII-R"
                     /note="urotensin-II receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd14999"
                     /db_xref="CDD:320130"
     Region          54..79
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320130"
     Site            55..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Region          86..110
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320130"
     Site            88..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Site            order(107,110..111,123..128,130..131,134,178,180..184,208,
                     211..213,215..217,219..220,272,275..276,278..279,282,
                     295..296,298..300,303,306..307)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320130"
     Region          123..153
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320130"
     Site            125..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Region          165..186
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320130"
     Site            168..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Region          208..237
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320130"
     Site            210..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Region          252..282
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320130"
     Site            259..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     Region          296..321
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320130"
     Site            300..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49684.2)"
     CDS             1..386
                     /gene="Uts2r"
                     /gene_synonym="Gpr14; Senr; UR-2-R"
                     /coded_by="NM_020537.1:1..1161"
                     /db_xref="GeneID:57305"
                     /db_xref="RGD:621884"
ORIGIN      
        1 malslestts fhmltvsgst vtelpgdsnv slnsswsgpt dpsslkdlva tgvigavlsa
       61 mgvvgmvgnv ytlvvmcrfl rasasmyvyv vnlaladlly llsipfiiat yvtkdwhfgd
      121 vgcrvlfsld fltmhasift ltimsserya avlrpldtvq rskgyrkllv lgtwllalll
      181 tlpmmlaiql vrrgskslcl pawgprahrt yltllfgtsi vgpglvigll yvrlaraywl
      241 sqqasfkqtr rlpnprvlyl ilgivllfwa cflpfwlwql laqyheampl tpetarivny
      301 lttcltygns cinpflytll tknyreylrg rqrslgssch spgspgsflp srvhlqqdsg
      361 rslssssqqa tetlmlspvp rngall
//
LOCUS       NP_446097                414 aa            linear   ROD 02-APR-2025
DEFINITION  interleukin-5 receptor subunit alpha precursor [Rattus norvegicus].
ACCESSION   NP_446097
VERSION     NP_446097.1
DBSOURCE    REFSEQ: accession NM_053645.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Zhou,Y., Li,C., Li,D., Zheng,Y. and Wang,J.
  TITLE     IL-5 blocks apoptosis and tau hyperphosphorylation induced by
            Abeta25-35 peptide in PC12 cells
  JOURNAL   J Physiol Biochem 73 (2), 259-266 (2017)
   PUBMED   28132394
  REMARK    GeneRIF: Data suggest that IL5/IL5Ra signaling activates JAK2 in
            neurons down-regulating cell apoptosis and down-regulating
            hyperphosphorylation of Tau [up-regulated in Alzheimer disease via
            amyloid-beta(25-35) peptide]. [IL5 = interleukin-5 ; IL5Ra =
            interleukin-5 receptor, alpha subunit; JAK2 = Janus kinase 2]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Wilson,T.M., Maric,I., Shukla,J., Brown,M., Santos,C., Simakova,O.,
            Khoury,P., Fay,M.P., Kozhich,A., Kolbeck,R., Metcalfe,D.D. and
            Klion,A.D.
  TITLE     IL-5 receptor alpha levels in patients with marked eosinophilia or
            mastocytosis
  JOURNAL   J Allergy Clin Immunol 128 (5), 1086-92 (2011)
   PUBMED   21762978
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Park,C.S.
  TITLE     Eosinophilic bronchitis, eosinophilia associated genetic variants,
            and notch signaling in asthma
  JOURNAL   Allergy Asthma Immunol Res 2 (3), 188-194 (2010)
   PUBMED   20592918
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Busse,W.W., Katial,R., Gossage,D., Sari,S., Wang,B., Kolbeck,R.,
            Coyle,A.J., Koike,M., Spitalny,G.L., Kiener,P.A., Geba,G.P. and
            Molfino,N.A.
  TITLE     Safety profile, pharmacokinetics, and biologic activity of
            MEDI-563, an anti-IL-5 receptor alpha antibody, in a phase I study
            of subjects with mild asthma
  JOURNAL   J Allergy Clin Immunol 125 (6), 1237-1244 (2010)
   PUBMED   20513521
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Mao,H., Wen,F.Q., Liu,C.T., Liang,Z.A., Wang,Z.L. and Yin,K.S.
  TITLE     Effect of interleukin-5 receptor-alpha short hairpin RNA-expressing
            vector on bone marrow eosinophilopoiesis in asthmatic mice
  JOURNAL   Adv Ther 23 (6), 938-956 (2006)
   PUBMED   17276963
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Gevaert,P., Bachert,C., Holtappels,G., Novo,C.P., Van der
            Heyden,J., Fransen,L., Depraetere,S., Walter,H., van Cauwenberge,P.
            and Tavernier,J.
  TITLE     Enhanced soluble interleukin-5 receptor alpha expression in nasal
            polyposis
  JOURNAL   Allergy 58 (5), 371-379 (2003)
   PUBMED   12752323
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Saito,H., Matsumoto,K., Denburg,A.E., Crawford,L., Ellis,R.,
            Inman,M.D., Sehmi,R., Takatsu,K., Matthaei,K.I. and Denburg,J.A.
  TITLE     Pathogenesis of murine experimental allergic rhinitis: a study of
            local and systemic consequences of IL-5 deficiency
  JOURNAL   J Immunol 168 (6), 3017-3023 (2002)
   PUBMED   11884474
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Pierrot,C., Begue,A., Szpirer,C., Capron,A., Capron,M. and
            Khalife,J.
  TITLE     Cloning of the rat IL-5Ralpha gene: analysis of 5'-upstream region
            and expression by B cells
  JOURNAL   Biochem Biophys Res Commun 288 (2), 328-339 (2001)
   PUBMED   11606047
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Tanaka,H., Kawada,N., Yamada,T., Kawada,K., Takatsu,K. and Nagai,H.
  TITLE     Allergen-induced airway inflammation and bronchial responsiveness
            in interleukin-5 receptor alpha chain-deficient mice
  JOURNAL   Clin Exp Allergy 30 (6), 874-881 (2000)
   PUBMED   10848907
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Denburg,J.A., Sehmi,R., Upham,J., Wood,L., Gauvreau,G. and
            O'Byrne,P.
  TITLE     Regulation of IL-5 and IL-5 receptor expression in the bone marrow
            of allergic asthmatics
  JOURNAL   Int Arch Allergy Immunol 118 (2-4), 101-103 (1999)
   PUBMED   10224351
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB056101.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB056101.1, AF324153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q41"
     Protein         1..414
                     /product="interleukin-5 receptor subunit alpha precursor"
                     /note="interleukin 5 receptor, alpha"
                     /calculated_mol_wt=45389
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1737
     mat_peptide     18..414
                     /product="interleukin-5 receptor subunit alpha"
                     /calculated_mol_wt=45389
     Region          126..231
                     /region_name="IL6Ra-bind"
                     /note="Interleukin-6 receptor alpha chain, binding;
                     pfam09240"
                     /db_xref="CDD:401252"
     CDS             1..414
                     /gene="Il5ra"
                     /coded_by="NM_053645.1:1..1245"
                     /db_xref="GeneID:114103"
                     /db_xref="RGD:70938"
ORIGIN      
        1 mvpvllilmg asatlhadll spekflllpp vnftikatgl aqvllhwdpn pdqdpvdley
       61 hvkinvpqed eydtkntesk cvtplhecfa asvrtilksi hsplasswvs aelkappgss
      121 gtsvmnltct tntvksshth frpyqvslrc twlvgkdape dtqyflyyrf svwteecqey
      181 srdalnrnia cwfprtfins kgfeqlavhi ngsskhaatk pldqlftlya idqvnppmnv
      241 tveiennsly iqwgkplsaf pvhcfkyklk iyntkngysq menlvtnkfi skiddvstys
      301 iqvraavssp crmsgswgew sqpiyvgkkk kplvewhliv lptaicfill ifslicrvyh
      361 lwtrlfppvp apkssikdlp vvteyekppw netkieivhf veedgfevme nslf
//
LOCUS       NP_001011697             194 aa            linear   ROD 02-APR-2025
DEFINITION  Spetex-2B protein [Rattus norvegicus].
ACCESSION   NP_001011697
VERSION     NP_001011697.1
DBSOURCE    REFSEQ: accession NM_001011697.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Iwamoto,Y., Kaneko,T., Ichinose,J., Mori,T., Shibata,Y.,
            Toshimori,K. and Iida,H.
  TITLE     Molecular cloning of rat Spetex2 family genes mapped on chromosome
            15p16, encoding a 23-kilodalton protein associated with the plasma
            membranes of haploid spermatids
  JOURNAL   Biol Reprod 72 (2), 284-292 (2005)
   PUBMED   15371276
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB180077.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB180077.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15"
     Protein         1..194
                     /product="Spetex-2B protein"
                     /calculated_mol_wt=23000
     Region          34..114
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..194
                     /gene="Spetex2b"
                     /gene_synonym="Spetex-2B"
                     /coded_by="NM_001011697.1:1..585"
                     /db_xref="GeneID:497084"
                     /db_xref="RGD:1359347"
ORIGIN      
        1 mfhqllklvq kergdqgetr trqkkaglls wfirkassen fisnhekrik kleevkseiq
       61 kckiegdels rildlyvndg lnyrlnielp mlksqhemrt mdmhkmtnwi sdamekykel
      121 tqennsyrir nfhllnerne lkknvrilmn enrkllveqt elqasceegk rfceeaskti
      181 ytadieslcp vtfe
//
LOCUS       NP_001102558             567 aa            linear   ROD 02-APR-2025
DEFINITION  proton-coupled zinc antiporter SLC30A9, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001102558 XP_001057251 XP_001070327
VERSION     NP_001102558.1
DBSOURCE    REFSEQ: accession NM_001109088.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Yu,G., Zhu,Y., Song,C., Chen,L., Tang,Z. and Wu,T.
  TITLE     The ZIP9-centered androgen pathway compensates for the 2605 MHz
            radiofrequency electromagnetic radiation-mediated reduction in
            resistance to H2O2 damage in Sertoli cells of adult rats
  JOURNAL   Ecotoxicol Environ Saf 254, 114733 (2023)
   PUBMED   36889209
  REMARK    GeneRIF: The ZIP9-centered androgen pathway compensates for the
            2605 MHz radiofrequency electromagnetic radiation-mediated
            reduction in resistance to H2O2 damage in Sertoli cells of adult
            rats.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Perez,Y., Shorer,Z., Liani-Leibson,K., Chabosseau,P., Kadir,R.,
            Volodarsky,M., Halperin,D., Barber-Zucker,S., Shalev,H.,
            Schreiber,R., Gradstein,L., Gurevich,E., Zarivach,R., Rutter,G.A.,
            Landau,D. and Birk,O.S.
  TITLE     SLC30A9 mutation affecting intracellular zinc homeostasis causes a
            novel cerebro-renal syndrome
  JOURNAL   Brain 140 (4), 928-939 (2017)
   PUBMED   28334855
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Chen,Y.H., Kim,J.H. and Stallcup,M.R.
  TITLE     GAC63, a GRIP1-dependent nuclear receptor coactivator
  JOURNAL   Mol Cell Biol 25 (14), 5965-5972 (2005)
   PUBMED   15988012
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Sim,D.L. and Chow,V.T.
  TITLE     The novel human HUEL (C4orf1) gene maps to chromosome 4p12-p13 and
            encodes a nuclear protein containing the nuclear receptor
            interaction motif
  JOURNAL   Genomics 59 (2), 224-233 (1999)
   PUBMED   10409434
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473981.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001070327.1, XP_001057251.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..567
                     /product="proton-coupled zinc antiporter SLC30A9,
                     mitochondrial"
                     /note="zinc transporter 9; solute carrier family 30 (zinc
                     transporter), member 9"
                     /calculated_mol_wt=62553
     Region          127..214
                     /region_name="NTD_ZNT9"
                     /note="N-terminal domain found in zinc transporter 9
                     (ZNT9) and similar proteins; cd21078"
                     /db_xref="CDD:410964"
     Region          237..562
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
     CDS             1..567
                     /gene="Slc30a9"
                     /coded_by="NM_001109088.1:75..1778"
                     /db_xref="GeneID:498358"
                     /db_xref="RGD:1593180"
ORIGIN      
        1 mfpglaaaaa ahrcswaalc rlgggpavar grsqgwknlm tfesftsmip sihpqisvln
       61 qvklystnvq kggqgsqtpr tdkappltqa aenigaelka plkqdplqvr vkavlkkrey
      121 gskytknnfi tgvrainefc lkssdleqlr kirrrsphdd tesftvflrs dveakalevw
      181 gslealarek klrkeaeiey rerlfrnqri lreygdflgn tkprsraisv flkgpgkvvm
      241 vaicinglnc ffkflawiyt gsasmfseai hslsdtcnqg llalgisksv qtpdpshpyg
      301 fsnmryissl isgvgifmmg aglswyhgim gllhpqpmes llwaycilag slvsegatll
      361 vainelrrsa qangtsfyky vmesrdpstn villedtaav lgvmiaatcm gltsitgnpl
      421 ydslgslgvg tllgvvsafl istnieallg rsiqpeqvqr ltellesdps vraihdvkat
      481 dlglgkvrfk aevdfdgrvv trsylekqdf dqmmqeieev ktpeqleafm lkhgeniidt
      541 lgaevdrlek elkkrnpevr hvdleil
//
LOCUS       NP_036778                392 aa            linear   ROD 02-APR-2025
DEFINITION  RT1 class Ib, locus N1 precursor [Rattus norvegicus].
ACCESSION   NP_036778
VERSION     NP_036778.1
DBSOURCE    REFSEQ: accession NM_012646.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kirisits,M.J., Kunz,H.W., Hassett,A.L. and Gill,T.J. 3rd.
  TITLE     Genomic DNA sequence and organization of a TL-like gene in the
            grc-G/C region of the rat
  JOURNAL   Immunogenetics 35 (6), 365-377 (1992)
   PUBMED   1349585
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M74822.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Rattus norvegicus"
                     /strain="R21"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..392
                     /product="RT1 class Ib, locus N1 precursor"
                     /note="RT1 class Ib gene H2-TL-like grc region; RT1 class
                     Ib gene, H2-TL-like, grc region (N1)"
                     /calculated_mol_wt=41331
     sig_peptide     1..30
                     /note="putative"
                     /calculated_mol_wt=3432
     mat_peptide     31..392
                     /product="RT1 class Ib, locus N1"
                     /calculated_mol_wt=41331
     Region          31..201
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          202..298
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          221..225
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          236..240
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          267..271
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          278..283
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..296
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..392
                     /gene="RT1-N1"
                     /gene_synonym="MHTLL"
                     /coded_by="NM_012646.1:1..1179"
                     /db_xref="GeneID:24748"
                     /db_xref="RGD:3498"
ORIGIN      
        1 mlwvpkagal wlsallllln acfswtwtpe gshslryfsi vmswlglrep riivsgcidd
       61 tefvrldtnk etvslkplvp wqeqegleyw eqqvhkvktq eqqsarnlmm lvrfynksmd
      121 dfhtlqwqqg cdvgsdgrll hwydqlafdg vdhptlnkdl rfwtawtstv aqisqpelea
      181 rlkdncsell qkypekeker llrsdpprah vtrqprpegd vtlrcwalgf ypaditltwq
      241 lngedliqem efvetrpagd gtfqkwasvv vplgkeqkyt clveheglse pltlrwepaq
      301 dstttiilii lptvsaivlc vaaaaaicic lkkkagergr hdtqeadgds pqdscrivvd
      361 dqeiegpswn tenyrthlgf hsgtlgllsl sf
//
LOCUS       NP_998896                321 aa            linear   ROD 02-APR-2025
DEFINITION  olfactory receptor family 12 subfamily D member 17 [Rattus
            norvegicus].
ACCESSION   NP_998896
VERSION     NP_998896.1
DBSOURCE    REFSEQ: accession NM_213731.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AL603724.3.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..321
                     /product="olfactory receptor family 12 subfamily D member
                     17"
                     /note="olfactory receptor 29; olfactory receptor 1868"
                     /calculated_mol_wt=36105
     Region          23..295
                     /region_name="7tmA_OR12D-like"
                     /note="olfactory receptor subfamily 12D and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15915"
                     /db_xref="CDD:320581"
     Region          24..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320581"
     Region          57..83
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320581"
     Site            order(79,82..83,95..100,102..103,106,151,153..157,193,
                     196..198,200..202,204..205,251,254..255,257..258,261,
                     269..270,272..274,277,280..281)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320581"
     Region          95..125
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320581"
     Region          138..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320581"
     Region          193..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320581"
     Region          231..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320581"
     Region          270..295
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320581"
     CDS             1..321
                     /gene="Or12d17"
                     /gene_synonym="MOR250-1; Olr1868; Or29"
                     /coded_by="NM_213731.1:1..966"
                     /db_xref="GeneID:408030"
                     /db_xref="RGD:1303153"
ORIGIN      
        1 menstsvdef lllglttvqk lqpiffvmfl tiyllnlvgn gvilmivtle rrlhspmyff
       61 lgnlscldic yssvtlpkvl inllsrhrti sflgcitqly ffhflgstea illavmafdr
      121 fvaicsplry taimnpqlci llaatawlts ffyallhsvm tahlnfchsh klshffcdvk
      181 pllevacgst vlnqwllsvv tgsismgafl livlsyfyii afllfknrsc rmlrkalstc
      241 tshfmvvclf ygpvgftyir patasassms edrmvaiiys avtpvlnpli ytlrnkevml
      301 alkrnfgkkl fkdnqlhagd q
//
LOCUS       NP_001243078              99 aa            linear   ROD 02-APR-2025
DEFINITION  Secreted seminal-vesicle Ly-6 protein 1-like precursor [Rattus
            norvegicus].
ACCESSION   NP_001243078 XP_002727075 XP_002729980
VERSION     NP_001243078.1
DBSOURCE    REFSEQ: accession NM_001256149.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from HQ840742.1.
            
            On or before Jan 9, 2012 this sequence version replaced
            XP_002727075.1, XP_002729980.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ840742.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..99
                     /product="Secreted seminal-vesicle Ly-6 protein 1-like
                     precursor"
                     /note="spleen protein 3; secreted seminal-vesicle Ly-6
                     protein 1-like; rCG64164-like"
                     /calculated_mol_wt=8875
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2338
     Region          20..98
                     /region_name="TFP"
                     /note="three-fingered protein (TFP) fold found in Ly6/uPAR
                     (LU) and snake toxin superfamily; cl45932"
                     /db_xref="CDD:480272"
     CDS             1..99
                     /gene="Patel14l2"
                     /coded_by="NM_001256149.1:1..300"
                     /db_xref="GeneID:100362690"
                     /db_xref="RGD:2324268"
ORIGIN      
        1 mgkhfllfll glsfvvgflq altcwdcdml nsdgicekgy stckskddqe cgklvvstgd
       61 kilywmqdcs smclnktfth shltlnftcc hdqslcnef
//
LOCUS       NP_001424261             361 aa            linear   ROD 02-APR-2025
DEFINITION  nucleoporin SEH1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424261 XP_056840912
VERSION     NP_001424261.1
DBSOURCE    REFSEQ: accession NM_001437332.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Bonnet,A. and Palancade,B.
  TITLE     Regulation of mRNA trafficking by nuclear pore complexes
  JOURNAL   Genes (Basel) 5 (3), 767-791 (2014)
   PUBMED   25184662
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Ahn,S.H., Deshmukh,H., Johnson,N., Cowell,L.G., Rude,T.H.,
            Scott,W.K., Nelson,C.L., Zaas,A.K., Marchuk,D.A., Keum,S.,
            Lamlertthon,S., Sharma-Kuinkel,B.K., Sempowski,G.D. and Fowler,V.G.
            Jr.
  TITLE     Two genes on A/J chromosome 18 are associated with susceptibility
            to Staphylococcus aureus infection by combined microarray and QTL
            analyses
  JOURNAL   PLoS Pathog 6 (9), e1001088 (2010)
   PUBMED   20824097
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Zuccolo,M., Alves,A., Galy,V., Bolhy,S., Formstecher,E., Racine,V.,
            Sibarita,J.B., Fukagawa,T., Shiekhattar,R., Yen,T. and Doye,V.
  TITLE     The human Nup107-160 nuclear pore subcomplex contributes to proper
            kinetochore functions
  JOURNAL   EMBO J 26 (7), 1853-1864 (2007)
   PUBMED   17363900
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Glavy,J.S., Krutchinsky,A.N., Cristea,I.M., Berke,I.C., Boehmer,T.,
            Blobel,G. and Chait,B.T.
  TITLE     Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
            subcomplex
  JOURNAL   Proc Natl Acad Sci U S A 104 (10), 3811-3816 (2007)
   PUBMED   17360435
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Loiodice,I., Alves,A., Rabut,G., Van Overbeek,M., Ellenberg,J.,
            Sibarita,J.B. and Doye,V.
  TITLE     The entire Nup107-160 complex, including three new members, is
            targeted as one entity to kinetochores in mitosis
  JOURNAL   Mol Biol Cell 15 (7), 3333-3344 (2004)
   PUBMED   15146057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 2, 2025 this sequence version replaced XP_056840912.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2113785.1,
                                           SRR26360190.3024161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..361
                     /product="nucleoporin SEH1 isoform 2"
                     /note="nucleoporin SEH1; nucleoporin SEH1-like"
                     /calculated_mol_wt=39702
     Region          <11..328
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          15..55
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          61..111
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..149
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..267
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          281..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..361
                     /gene="Seh1l"
                     /coded_by="NM_001437332.1:83..1168"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100911798"
                     /db_xref="RGD:6490353"
ORIGIN      
        1 mfvarsiaad hkdlihdvsf dfhgrrmatc ssdqsvkvwd ksesgdwhct aswkthsgsv
       61 wrvtwahpef gqvlascsfd rtaavweeiv gesndklrgq shwvkrttlv dsrtsvtdvk
      121 fapkhmglml atcsadgivr vyeapdvmnl sqwslqheis cklccscisw npsssrahpp
      181 miavgsddss pnsmakvqif eynentrkya kaetlmtvtd pvhdiafapn lgrsfhilai
      241 atkdvriftl kpvrkeltss ggptkfeihi vaqfdnhnsq vwrvswnitg tvlassgddg
      301 cvrlwkanym dnwkctgilk gngspvngss qlgnstpsls snipnlqnsl ngtsagsrkh
      361 s
//
LOCUS       NP_001424146             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424146 XP_006249180
VERSION     NP_001424146.1
DBSOURCE    REFSEQ: accession NM_001437217.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249180.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437217.1:133..2529"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424240             544 aa            linear   ROD 03-APR-2025
DEFINITION  protein hinderin isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424240 XP_038952959
VERSION     NP_001424240.1
DBSOURCE    REFSEQ: accession NM_001437311.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952959.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.76445.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..544
                     /product="protein hinderin isoform 4"
                     /calculated_mol_wt=61966
     Region          28..351
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     CDS             1..544
                     /gene="Kiaa1328"
                     /gene_synonym="RGD1562608; RGD1564140"
                     /coded_by="NM_001437311.1:318..1952"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:498831"
                     /db_xref="RGD:1562608"
ORIGIN      
        1 meslkgagds vaeqsfckrg lksaslkdlc vedkrrianl ikelarvsee kevteerlkt
       61 eqesfekkir qleeqnelii kerealqlqy recqellsly qkylseqqek ltmslselga
      121 araqeqqitk kkithqsslv nldgsylsva kpqtcqtrar pksenqdsas eshtalrnns
      181 lkpvtlhhpk qdlermstet rtctyespgr rlinaapvee alpeelkikd ypnllptpss
      241 qycghkyses eayvhenyhp tnmasqcckt hpescshcrm swaslmhdgv tlqpretdie
      301 kqlsedrrqq lmlqkmelei ekerlqqlla qqetklllkq qqlhqsrldy nwlrtqavfr
      361 srelvadkdf pkpgsdsgps llkpkcdgwl rgtsssfrkc pdspnsaqnq kekktvefqs
      421 hvengiqwtc qqndtcrlqr etatgvrkda stspmstqsp khpltpasss skhktsryet
      481 slldlvqsls pnsapkcqph ssraagtwsa lrptpktstw kkvgthkspe dleenqiled
      541 iffi
//
LOCUS       NP_001424272             780 aa            linear   ROD 03-APR-2025
DEFINITION  centrosomal protein of 120 kDa isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424272
VERSION     NP_001424272.1
DBSOURCE    REFSEQ: accession NM_001437343.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Chang,C.W., Hsu,W.B., Tsai,J.J., Tang,C.J. and Tang,T.K.
  TITLE     CEP295 interacts with microtubules and is required for centriole
            elongation
  JOURNAL   J Cell Sci 129 (13), 2501-2513 (2016)
   PUBMED   27185865
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Wu,C., Yang,M., Li,J., Wang,C., Cao,T., Tao,K. and Wang,B.
  TITLE     Talpid3-binding centrosomal protein Cep120 is required for
            centriole duplication and proliferation of cerebellar granule
            neuron progenitors
  JOURNAL   PLoS One 9 (9), e107943 (2014)
   PUBMED   25251415
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Iwakoshi,N.N., Pypaert,M. and Glimcher,L.H.
  TITLE     The transcription factor XBP-1 is essential for the development and
            survival of dendritic cells
  JOURNAL   J Exp Med 204 (10), 2267-2275 (2007)
   PUBMED   17875675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77400.1,
                                           SRR26360181.96477.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..780
                     /product="centrosomal protein of 120 kDa isoform 2"
                     /note="centrosomal protein 120kDa; coiled-coil domain
                     containing 100; centrosomal protein of 120 kDa"
                     /calculated_mol_wt=89341
     Region          <1..131
                     /region_name="DUF3668"
                     /note="Cep120 protein; pfam12416"
                     /db_xref="CDD:463569"
     Region          <444..>778
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..780
                     /gene="Cep120"
                     /gene_synonym="Ccdc100; RGD1565619"
                     /coded_by="NM_001437343.1:774..3116"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:307302"
                     /db_xref="RGD:1565619"
ORIGIN      
        1 mklperqpef ffyysllgnd vtnepfsdli npnfeperas vrirssvevl rvylalhskl
       61 qihlccgdqs lgsteiplsg llkkgstein qhpvtvegaf tldppnrakq klapvpvela
      121 ptvgvsvalq regigsqsli elktqnghep ehsqkrvltp ikektltgpk sprvspappq
      181 nqtpptkdda teseveslqy dkepkqvvkg tgsipaslaq peatgnpsev vtsgqkiavp
      241 atshhfcfsi dlrsihglei sfpvncilry sypffgsaap imtnppvevr knmevflpqs
      301 ycafdfatmp hqlqdtflri pllvelwhkd kmskdlllgi ariqlsnils sektrflgan
      361 geqcwrqtys ekvpviaaqg snnrivdlsy tmtledyglv kmreifvses sqgmsavgqr
      421 asppppppap cpseiqvepr etleykaale lemwkemqed ifesqlkqke lahmqalaee
      481 wkkrdreres lvkkkvaeys ilegklqqal telesreqql vtaetelqre rkelqlerer
      541 nlqelqdsvr rarddcvhqv elerlklkql eedkhrlqqq lndaenkyki lekdfqqfkd
      601 qqnnkpeirl qseinlltle kvelerkles atksklhykq qwgralkela rlkqreqesq
      661 marlkkqqee leqmrlryla aeekdtvkte qqelldirne lnrlrqqeqk qyqdykeias
      721 gkqgsprgsg leeglddylt rlieerdtlm rtgvynhedr iiseldrqir evltknsasn
//
LOCUS       NP_001009258             663 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CHFR isoform 2 [Rattus norvegicus].
ACCESSION   NP_001009258 XP_213807
VERSION     NP_001009258.1
DBSOURCE    REFSEQ: accession NM_001009258.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Perdereau,D., Cailliau,K., Browaeys-Poly,E., Lescuyer,A., Carre,N.,
            Benhamed,F., Goenaga,D. and Burnol,A.F.
  TITLE     Insulin-induced cell division is controlled by the adaptor Grb14 in
            a Chfr-dependent manner
  JOURNAL   Cell Signal 27 (4), 798-806 (2015)
   PUBMED   25578860
  REMARK    GeneRIF: These results show that Chfr and Grb14 collaborate in a
            negative feedback loop controlling insulin-stimulated cell
            division.
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Jung,I., Sohn,D.H., Choi,J., Kim,J.M., Jeon,S., Seol,J.H. and
            Seong,R.H.
  TITLE     SRG3/mBAF155 stabilizes the SWI/SNF-like BAF complex by blocking
            CHFR mediated ubiquitination and degradation of its major
            components
  JOURNAL   Biochem Biophys Res Commun 418 (3), 512-517 (2012)
   PUBMED   22285184
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Oh,Y.M., Kwon,Y.E., Kim,J.M., Bae,S.J., Lee,B.K., Yoo,S.J.,
            Chung,C.H., Deshaies,R.J. and Seol,J.H.
  TITLE     Chfr is linked to tumour metastasis through the downregulation of
            HDAC1
  JOURNAL   Nat Cell Biol 11 (3), 295-302 (2009)
   PUBMED   19182791
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Ahel,I., Ahel,D., Matsusaka,T., Clark,A.J., Pines,J., Boulton,S.J.
            and West,S.C.
  TITLE     Poly(ADP-ribose)-binding zinc finger motifs in DNA
            repair/checkpoint proteins
  JOURNAL   Nature 451 (7174), 81-85 (2008)
   PUBMED   18172500
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Yu,X., Minter-Dykhouse,K., Malureanu,L., Zhao,W.M., Zhang,D.,
            Merkle,C.J., Ward,I.M., Saya,H., Fang,G., van Deursen,J. and
            Chen,J.
  TITLE     Chfr is required for tumor suppression and Aurora A regulation
  JOURNAL   Nat Genet 37 (4), 401-406 (2005)
   PUBMED   15793587
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Daniels,M.J., Marson,A. and Venkitaraman,A.R.
  TITLE     PML bodies control the nuclear dynamics and function of the CHFR
            mitotic checkpoint protein
  JOURNAL   Nat Struct Mol Biol 11 (11), 1114-1121 (2004)
   PUBMED   15467728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jan 7, 2005 this sequence version replaced XP_213807.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087162.1, SRR26643299.51242.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..663
                     /product="E3 ubiquitin-protein ligase CHFR isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CHFR; checkpoint with
                     forkhead and ring finger domains, E3 ubiquitin protein
                     ligase"
                     /calculated_mol_wt=73822
     Region          15..124
                     /region_name="FHA_CHFR"
                     /note="forkhead associated (FHA) domain found in
                     checkpoint with forkhead and RING finger domains protein
                     (CHFR); cd22672"
                     /db_xref="CDD:438724"
     Site            order(15..22,40,48,50,53,55..56,60..61,72..78,80..92,
                     95..98,101..108,116..124)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438724"
     Region          39..>252
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Site            order(41..43,57..58,60,78..81)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438724"
     Region          299..352
                     /region_name="RING-HC_CHFR"
                     /note="RING finger, HC subclass, found in checkpoint with
                     forkhead and RING finger domains protein (CHFR); cd16503"
                     /db_xref="CDD:438166"
     Region          468..619
                     /region_name="zf-CRD"
                     /note="Cysteine rich domain with multizinc binding
                     regions; pfam17979"
                     /db_xref="CDD:465602"
     Region          631..654
                     /region_name="zf-CCHH"
                     /note="PBZ domain; pfam10283"
                     /db_xref="CDD:463043"
     CDS             1..663
                     /gene="Chfr"
                     /coded_by="NM_001009258.2:86..2077"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:288734"
                     /db_xref="RGD:1306360"
ORIGIN      
        1 mephgedeqp pprepwgrll rlgaeedepq illwkrewti grrrgcdlsf psnklvsgdh
       61 cklrvdeksg evtledtstn gtvinklrvv kkqtyplqsg diiylvyrkn epehnvayly
      121 eslngkqslt qesleanken mfhvtkessg pgqgddpqvp llspmaqtcl eepqpststs
      181 dllptastss tepeltsagq khssssgpgt isispkecss lvangelssl ssvfqdneas
      241 fsllktedte elepakkkmk gdgeldlnlq lsvadqrgia qtssedvkda svkpdkmeet
      301 ltciicqdll hdcvslqpcm htfcaacysg wmersslcpt crcpverick nhilnnlvea
      361 yllqhpdksr seedvrsmda rnkitqdmlq pkvrrsfsde egssedllel sdvdsessdi
      421 sqpyivcrqc peyrrqavqs lpcpvpesel gatqalggea pstsasltta pgytcplqgs
      481 haictccfqp mpdrraeheq dsriapqqca vclqpfchly wgctrtgcfg clapfcelnl
      541 gdkcldgvln nnnyesdilk nylttrgltw knmlteslla lqrgvfilsd yritgntvlc
      601 yccglrsfre ltyqyrqnip aselpvtvts rpdcywgrnc rtqvkahham kfnhiceqtr
      661 fkn
//
LOCUS       NP_001424331             445 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424331 XP_038952630
VERSION     NP_001424331.1
DBSOURCE    REFSEQ: accession NM_001437402.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952630.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77199.1,
                                           SRR26360181.1741339.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..445
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 5"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=50615
     Region          <2..96
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          75..123
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          147..210
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          232..435
                     /region_name="SPRY_PRY_TRIM36"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 36 (TRIM36); cd12894"
                     /db_xref="CDD:293951"
     CDS             1..445
                     /gene="Trim36"
                     /coded_by="NM_001437402.1:283..1620"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 mketecnger akeealahfe klfeiledrk ssvlkaidas kklrldkfht qmeeyqglle
       61 nnglvgyaqe vlketdqscf vqtakqlhlr iqkateslks frpaaqasfe dyvvniskqt
      121 evlgelsffs sgidipeine eqskvynnal idwhhpekdk adsyvleyrk inrdeemisw
      181 neievhgtsk vvsnlesnsp yafrvrayrg sicspcsrel vlhtppapvf sflfdekcgy
      241 ntehlllnlk rdrvesragf nvllaaeriq vghytsldyi igdvgitkgk hfwacrvepy
      301 sylvkvgvas sdklqewlrs prdaasprye qdsghdsgse dayfdssqpf tlvtigmkkf
      361 fipksptssn epenrvlpmp tsigifldcd kgkvsfydmd hmkclyerqv dcshtmypaf
      421 almgsggiql eetitakyle yeedv
//
LOCUS       NP_001424292             526 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424292 XP_063127393
VERSION     NP_001424292.1
DBSOURCE    REFSEQ: accession NM_001437363.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127393.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2363587.1,
                                           SRR26360181.2363588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..526
                     /product="coiled-coil domain-containing protein 63 isoform
                     3"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=61429
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..526
                     /gene="Ccdc63"
                     /coded_by="NM_001437363.1:139..1719"
                     /note="isoform 3 is encoded by transcript variant 12"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeelcpgcsg ipsgpq
//
LOCUS       NP_001424306             565 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424306 XP_006254976
VERSION     NP_001424306.1
DBSOURCE    REFSEQ: accession NM_001437377.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254976.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.467802.1,
                                           SRR26360194.1407939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..565
                     /product="methyl-CpG-binding domain protein 1 isoform 7"
                     /calculated_mol_wt=61735
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          <291..549
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..565
                     /gene="Mbd1"
                     /coded_by="NM_001437377.1:162..1859"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elkrllpsig pgseeearll
      361 phhthqkrsa strqlqlssp lkaplavvtt ppgpvqdsgk rqagsgfvlp qpdtdlvylq
      421 egtsslmqvp gpaaastenp aqetqgsapg wvvalpqvkq ekadapeewt avttfltsst
      481 vqpgflskas gldpppvkre ppgpeedgee nkeddvsesa paeeiggigt pviteifslg
      541 gtrlrdaeaw lprskdlkkp gakmq
//
LOCUS       NP_001424303             620 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424303 XP_017456372
VERSION     NP_001424303.1
DBSOURCE    REFSEQ: accession NM_001437374.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017456372.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.505374.1,
                                           SRR26360176.2435227.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..620
                     /product="methyl-CpG-binding domain protein 1 isoform 4"
                     /calculated_mol_wt=68165
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          346..392
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..620
                     /gene="Mbd1"
                     /coded_by="NM_001437374.1:162..2024"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elpytnqrqn rkcgacaacl
      361 rrmdcghcdf ccdkpkfggs nqkrqkcrwr qclqfamkrl lpsigpgsee earllphhth
      421 qkrsastrql qlssplkapl avvttppgpv qdsgkrqags gfvlpqpdtd lvylqegtss
      481 lmqvpgpaaa stenpaqetq gsapgwvval pqvkqekada peewtavttf ltsstvqpgf
      541 lskasgldpp pvkreppgpe edgeenkedd vsesapaeei ggigtpvite ifslggtrlr
      601 daeawlprsk dlkkpgakmq
//
LOCUS       NP_001004204             314 aa            linear   ROD 03-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001004204 XP_213763
VERSION     NP_001004204.1
DBSOURCE    REFSEQ: accession NM_001004204.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Sep 10, 2004 this sequence version replaced XP_213763.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001004204.3:557..1501"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001424343             338 aa            linear   ROD 03-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424343 XP_063141750
VERSION     NP_001424343.1
DBSOURCE    REFSEQ: accession NM_001437414.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063141750.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.2896.1,
                                           SRR26360172.409910.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..338
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 3"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=36577
     Region          <3..81
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..338
                     /gene="Xndc1"
                     /coded_by="NM_001437414.1:747..1763"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 msidvgrssw pldrpfvtll patmlmsltd skegknrsgv rmfkdddfli pasgeswdrl
       61 rltcsqpftr hqsfglaflr vrssldslsd pvkdpsspgs sglnqnssdk lesdpspwlt
      121 npsirrtffp dpqtstkeis alkgmlkqlq pgplgraarm vlsaahkapp asvvspnnsh
      181 gepdsshper aepraeepnr knnasrgkrr kvqeqrrpls ssssqpnrra tgrtkqrqqr
      241 pqaksdgsgv qatgqcpict gsfsiealpr haatcgessp pqpasptsls ssesvlwvss
      301 pesspppssw vqcpicelqf sareieehas vcgevfpa
//
LOCUS       NP_001020836             559 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001020836 XP_222186
VERSION     NP_001020836.1
DBSOURCE    REFSEQ: accession NM_001025665.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jul 22, 2005 this sequence version replaced XP_222186.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..559
                     /product="coiled-coil domain-containing protein 63 isoform
                     1"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65977
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..559
                     /gene="Ccdc63"
                     /coded_by="NM_001025665.2:340..2019"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eevphralsw vqwntlwttv asgswswrtt
      541 frrneeknhr rhcwrrgtr
//
LOCUS       NP_001424307             172 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424307 XP_038950768
VERSION     NP_001424307.1
DBSOURCE    REFSEQ: accession NM_001437378.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038950768.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.104598.1,
                                           SRR26360181.2560874.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680446,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..172
                     /product="uncharacterized protein CFAP97D2 isoform 2"
                     /calculated_mol_wt=20600
     Region          28..119
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..172
                     /gene="Cfap97d2"
                     /coded_by="NM_001437378.1:78..596"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkmee
       61 erlsiidrnn ylllqrvasa mktgrridgq nnftwrrksr eqalmkvqkq nqavperlrs
      121 sepwygaqrw redwtamatr pctcrhtwrk gadreaqqgh sliwmrslkr kg
//
LOCUS       NP_001424301             631 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424301 XP_006254972
VERSION     NP_001424301.1
DBSOURCE    REFSEQ: accession NM_001437372.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254972.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1893458.1,
                                           SRR26360172.788548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..631
                     /product="methyl-CpG-binding domain protein 1 isoform 2"
                     /calculated_mol_wt=69622
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          346..392
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..631
                     /gene="Mbd1"
                     /coded_by="NM_001437372.1:162..2057"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elpytnqrqn rkcgacaacl
      361 rrmdcghcdf ccdkpkfggs nqkrqkcrwr qclqfamkrl lpsigpgsee earllphhth
      421 qkrsastrql qlssplkapl avvttppgpv qdsgkrqags gfvlpqpdtd lvylqegtss
      481 lmqvpgpaaa stenpaqetq gsapgwvval pqvkqekada peewtavttf ltsstvqpgf
      541 lskasgldpp pvkreppgpe edgeenkedd vsesapaeei ggigtpvite ifslggtrlr
      601 daeawlprlh kllavneney ftelqlkeei l
//
LOCUS       NP_001424151             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424151
VERSION     NP_001424151.1
DBSOURCE    REFSEQ: accession NM_001437222.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.34966.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437222.1:35..2431"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424235             104 aa            linear   ROD 03-APR-2025
DEFINITION  family with sequence similarity 186 member A isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424235
VERSION     NP_001424235.1
DBSOURCE    REFSEQ: accession NM_001437306.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2108385.1,
                                           SRR26360181.63576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..104
                     /product="family with sequence similarity 186 member A
                     isoform 2"
                     /note="Protein FAM186A-like"
                     /calculated_mol_wt=11665
     CDS             1..104
                     /gene="Fam186a"
                     /coded_by="NM_001437306.1:305..619"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100362820"
                     /db_xref="RGD:2323958"
ORIGIN      
        1 mpsissfkki pkftklqrpv ldlliddskr sdvfkrrgqa pveavwnadl stssypvvek
       61 tpmnllwaql ggypdipkll qldiqstlrk slasicprsk kirk
//
LOCUS       NP_001424148             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424148
VERSION     NP_001424148.1
DBSOURCE    REFSEQ: accession NM_001437219.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.34954.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437219.1:105..2501"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424329             584 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424329 XP_038952628
VERSION     NP_001424329.1
DBSOURCE    REFSEQ: accession NM_001437400.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952628.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77206.1,
                                           SRR26360181.2995621.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..584
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 4"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=66271
     Region          16..113
                     /region_name="RING-HC_TRIM36_C-I"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd16756"
                     /db_xref="CDD:438414"
     Region          139..193
                     /region_name="Bbox1_TRIM36_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19848"
                     /db_xref="CDD:380906"
     Region          198..242
                     /region_name="Bbox2_TRIM36_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19778"
                     /db_xref="CDD:380836"
     Region          244..368
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          347..395
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          419..482
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          504..>560
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..584
                     /gene="Trim36"
                     /coded_by="NM_001437400.1:278..2032"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 megdasdsqv tikniekeli cpackelfth plilpcqhsv chkcvkelll slddsfndva
       61 sdssnqsspr lrltspsmdk idkinrpgwk rnsltprptm fpcpgcehdv dlgergvsgl
      121 frnftletiv eryrqaaraa taimcdlckp ppqestkscm dcsasycnec fkiyhpwgtv
      181 kaqheyvgpt tnfrpkilmc peheterinm ycelcrrpvc hlcklggnhs nhrvttmssa
      241 yktlkeklsk didfligkes qvksqiseln llmketecng erakeealah feklfeiled
      301 rkssvlkaid askklrldkf htqmeeyqgl lennglvgya qevlketdqs cfvqtakqlh
      361 lriqkatesl ksfrpaaqas fedyvvnisk qtevlgelsf fssgidipei neeqskvynn
      421 alidwhhpek dkadsyvley rkinrdeemi swneievhgt skvvsnlesn spyafrvray
      481 rgsicspcsr elvlhtppap vfsflfdekc gyntehllln lkrdrvesra gfnvllaaer
      541 iqvghytsld yiigdvgitk dmsktvgmta evrtpililh nrlh
//
LOCUS       NP_001424341             355 aa            linear   ROD 03-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424341 XP_006229968
VERSION     NP_001424341.1
DBSOURCE    REFSEQ: accession NM_001437412.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229968.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.785394.1,
                                           SRR26360194.334944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..355
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 2"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=38498
     Region          1..98
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..355
                     /gene="Xndc1"
                     /coded_by="NM_001437412.1:566..1633"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 mapvkishvv sfssqdpkyp venllnpdsh kgpwlscprd ktgqlkvefq leravpisyi
       61 dvddflipas geswdrlrlt csqpftrhqs fglaflrvrs sldslsdpvk dpsspgssgl
      121 nqnssdkles dpspwltnps irrtffpdpq tstkeisalk gmlkqlqpgp lgraarmvls
      181 aahkappasv vspnnshgep dsshperaep raeepnrknn asrgkrrkvq eqrrplssss
      241 sqpnrratgr tkqrqqrpqa ksdgsgvqat gqcpictgsf siealprhaa tcgessppqp
      301 asptslssse svlwvsspes spppsswvqc picelqfsar eieehasvcg evfpa
//
LOCUS       NP_001424203            1044 aa            linear   ROD 03-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform a [Rattus norvegicus].
ACCESSION   NP_001424203 XP_063144208
VERSION     NP_001424203.1
DBSOURCE    REFSEQ: accession NM_001437274.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1044)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1044)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1044)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1044)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1044)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1044)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1044)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063144208.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.24359.1,
                                           SRR26643284.8347.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1044
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform a"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=119762
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..281
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          314..481
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          504..684
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          676..1042
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(752,754..756,758,760,777,779,782,813,825..828,833,
                     836,898,900,910..911)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(820..821,922..923,925,927,993,996)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            867
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            890..898
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            911..935
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1044
                     /gene="Pik3cd"
                     /coded_by="NM_001437274.1:329..3463"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse esftfqvstk dmplalmaca lrkkatvfrq plverpeeya
      241 lqvngrheyl ygsyplchfq yicsclhsgl tphltmvhss silamrdeqs npapqvqkpr
      301 vkpppipakk pssvslwsle qpfcielieg rkvnadermk lvvqaglfhg nemlcktvss
      361 sevnvcsepv wkqrlefdis icdlprmarl cfalyavvek akkarstkkk skkadcpiaw
      421 anlmlfdykd qlktgercly mwpsvpdekg elmnpagtvr gnpntesaaa lviylpevap
      481 hpvyfpalek ilelgrhger griteeeqlq lreilerrgs gelyehekdl vwkmrhevqe
      541 hfpealarll lvtkwnkhed vaqmlyllcs wpelpvlsal elldfsfpdc yvgsfaiksl
      601 rkltddelfq yllqlvqvlk yesyldcelt kfllgralan rkighflfwh lrsemhvpsv
      661 alrfglimea ycrgsthhmk vlmkqgeals klkalndfvk assqkttkpq tkemmhmcmr
      721 qetymealsh lqspldpstl leevcveqct fmdskmkplw imyssekagg agsvgiifkn
      781 gddlrqdmlt lqmiqlmdfl wkqegldlrm tpygclptgd rtglievvlh sdtianiqln
      841 ksnmaataaf nkdallnwlk sknpgealdr aieeftlsca gycvatyvlg igdrhsdnim
      901 iresgqlfhi dfghflgnfk tkfginrerv pfiltydfvh viqqgktnns ekferfrgyc
      961 eraytilrrh gllflhlfal mraaglpels cskdiqylkd slalgkteee alkhfrvkfn
     1021 ealreswktk vnwlahnvsk dnrq
//
LOCUS       NP_001424302             621 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424302 XP_006254973
VERSION     NP_001424302.1
DBSOURCE    REFSEQ: accession NM_001437373.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254973.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54695.1,
                                           SRR26643298.74677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..621
                     /product="methyl-CpG-binding domain protein 1 isoform 3"
                     /calculated_mol_wt=68294
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          347..393
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..621
                     /gene="Mbd1"
                     /coded_by="NM_001437373.1:162..2027"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elqpytnqrq nrkcgacaac
      361 lrrmdcghcd fccdkpkfgg snqkrqkcrw rqclqfamkr llpsigpgse eearllphht
      421 hqkrsastrq lqlssplkap lavvttppgp vqdsgkrqag sgfvlpqpdt dlvylqegts
      481 slmqvpgpaa astenpaqet qgsapgwvva lpqvkqekad apeewtavtt fltsstvqpg
      541 flskasgldp ppvkreppgp eedgeenked dvsesapaee iggigtpvit eifslggtrl
      601 rdaeawlprs kdlkkpgakm q
//
LOCUS       NP_001100610            2050 aa            linear   ROD 03-APR-2025
DEFINITION  kinetochore-associated protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100610 XP_001074897 XP_222157
VERSION     NP_001100610.1
DBSOURCE    REFSEQ: accession NM_001107140.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2050)
  AUTHORS   Civril,F., Wehenkel,A., Giorgi,F.M., Santaguida,S., Di Fonzo,A.,
            Grigorean,G., Ciccarelli,F.D. and Musacchio,A.
  TITLE     Structural analysis of the RZZ complex reveals common ancestry with
            multisubunit vesicle tethering machinery
  JOURNAL   Structure 18 (5), 616-626 (2010)
   PUBMED   20462495
REFERENCE   2  (residues 1 to 2050)
  AUTHORS   Chan,G.K., Jablonski,S.A., Starr,D.A., Goldberg,M.L. and Yen,T.J.
  TITLE     Human Zw10 and ROD are mitotic checkpoint proteins that bind to
            kinetochores
  JOURNAL   Nat Cell Biol 2 (12), 944-947 (2000)
   PUBMED   11146660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_222157.4, XP_001074897.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2050
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15-q16"
     Protein         1..2050
                     /product="kinetochore-associated protein 1 isoform 2"
                     /note="kinetochore-associated protein 1;
                     kinetochore-associated protein 1-like"
                     /calculated_mol_wt=233116
     Region          380..>619
                     /region_name="Rod_C"
                     /note="Rough deal protein C-terminal region; pfam10493"
                     /db_xref="CDD:463114"
     Region          1425..1972
                     /region_name="Rod_C"
                     /note="Rough deal protein C-terminal region; pfam10493"
                     /db_xref="CDD:463114"
     CDS             1..2050
                     /gene="Kntc1"
                     /coded_by="NM_001107140.2:141..6293"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304477"
                     /db_xref="RGD:1307905"
ORIGIN      
        1 mwnniellts ddtgsgflnv gsrkesvtal yqvdllgkis sektslspki qacslsdgfi
       61 ivadqsvill dstcrslqlf lifdtdvdvv glcpegkflf vgersgnfhl iyvtskrtlf
      121 tkafvekaed ertyrslvie kdgsnegtyy mllltnngff yitnlqlsqi eqaientdld
      181 sakkgtgsca fskwepdstk kdmslknfvd tdiirgaksf qlidnllfvl dtdnvlslwd
      241 aytltpvwnw pslpieqfll tteadspssv tclcedsvsn lelryltevl penrlsrllh
      301 khrfadaesf aiqfgldvel vykvksndil eklalisdks eqsewqqlvd eakenlckiq
      361 dddfvvnfcl kaqwvtyett qemlsyaktr vlkahakltt fygafgpekf sgsawvefln
      421 neddlkdifv qlsegnfdca qylwlrhrad feskfdvkml enllnsistq ipveklcswf
      481 kndvipfvrr ivpegqnila kwleqasrnl eltdkanwpe nglqlaevff taektdkfgf
      541 ssswhwisld yqnteevqql rtlvsklqel iilhrkyncr lalsefeken attvvfrmfd
      601 rvsapelips vlekfvrvyi reqnlqeeel lllyiedllk rcssksmtlf dtaweakama
      661 virclsdtdl ifdavlkimy kavvpwsaav eqlvrqhlem dhpkvkllqe syrlmemkkl
      721 lrgygirevn llnkeimrvv ryilkqdips sledalkvaq gyrlsddeiy slrvidlidr
      781 dqgedcllll rslppseaek taerviiwar lalqeepdgs eedkawrisv aktsmdilki
      841 lcdiqkdnlq kkddaeeflk rfkmvaslqe nfevflpfed ysdtglvagl reqyikaqen
      901 aqaehkfrgp pgptpamgtn asvksklhrq alvlqvstqe leaemalral kdgkvavals
      961 kcrdllkhyc nadtgrllfv vcqklchmla ddvpmvapvg lnlpseihdl tchavticsp
     1021 dflldvlels kytltavelc rqcqmddcgi lmkaavgthk dpyeewsysd ffsedgivle
     1081 sqvvlpviye lissvvplae gkrrpldsis lpycstsege nlilplvssi sallrnlqes
     1141 sqwelalrfv vasfgtclqh svsnvmsmsl sekllgkstl assrqiimel keksiafirg
     1201 sattllhkvf ncrlvdldla layctllpqk dvfenlwkfi dkawqnydki lalslvgsrl
     1261 anlyqdvetg lrfhelsida kwgirlgklg isfqpafrqn flskkdlika lvnnidmdts
     1321 lileycstfq ldsdaalrlf ietllrntts qsqggdapep tqhqhskllq katemvpllk
     1381 stkdlvislt eilykalnll rhlksyrrms ppvdleyqym lehlitlppa aqtrlpfhli
     1441 lfgtaqnfwk ilsselsees lptllliskl mkfsldtlyv stakhvfekn lkpkllksaq
     1501 arssvmskev dklvqtlesy llsivnpewa vaiaisltqe ipegpfkmts lkfclylaer
     1561 wlqnippqde tcekvkalqk klylqfrlsg teavliahkl ndqeylrvvg kpahlivsly
     1621 ehpsiserlc ttsgkdypdi haaakeiaev neinlekiwd mllekwlcps tapgekasef
     1681 feleedevlh rvvyllqarp idyssrmlfv fatsatstlg irqltfahra ralqcllyla
     1741 dketieslfk kpteemksyl kcitflasfe tlnipityel fcnspkegmi kglwknhshe
     1801 pmavrlvael cleykiydlq lwngllqkll gfnmipylrk vlscissvhs lwqvpyfska
     1861 wqrviqipll sascplrpsq ladcceslva ilecpvsddl dmmgvakqyv qlelpafalt
     1921 cltlmphsek rhqqiknfln scdaqiilqq leehmnagql aglsqqirsl vlnhvvnkke
     1981 fgilaktkyf qllkrhvint dnvtelvnyl andlsldeas sliteyskhc gkpvpadtap
     2041 seilktflgs
//
LOCUS       NP_001424269             492 aa            linear   ROD 03-APR-2025
DEFINITION  beta-Ala-His dipeptidase [Rattus norvegicus].
ACCESSION   NP_001424269
VERSION     NP_001424269.1
DBSOURCE    REFSEQ: accession NM_001437340.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Veiga-da-Cunha,M., Chevalier,N., Stroobant,V., Vertommen,D. and Van
            Schaftingen,E.
  TITLE     Metabolite proofreading in carnosine and homocarnosine synthesis:
            molecular identification of PM20D2 as beta-alanyl-lysine
            dipeptidase
  JOURNAL   J Biol Chem 289 (28), 19726-19736 (2014)
   PUBMED   24891507
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Chakkera,H.A., Hanson,R.L., Kobes,S., Millis,M.P., Nelson,R.G.,
            Knowler,W.C. and Distefano,J.K.
  TITLE     Association of variants in the carnosine peptidase 1 gene (CNDP1)
            with diabetic nephropathy in American Indians
  JOURNAL   Mol Genet Metab 103 (2), 185-190 (2011)
   PUBMED   21393041
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Kilis-Pstrusinska,K., Zwolinska,D. and Grzeszczak,W.
  CONSRTM   Study Group
  TITLE     Is carnosinase 1 gene (CNDP1) polymorphism associated with chronic
            kidney disease progression in children and young adults? results of
            a family-based study
  JOURNAL   Arch Med Res 41 (5), 356-362 (2010)
   PUBMED   20851293
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Teufel,M., Saudek,V., Ledig,J.P., Bernhardt,A., Boularand,S.,
            Carreau,A., Cairns,N.J., Carter,C., Cowley,D.J., Duverger,D.,
            Ganzhorn,A.J., Guenet,C., Heintzelmann,B., Laucher,V., Sauvage,C.
            and Smirnova,T.
  TITLE     Sequence identification and characterization of human carnosinase
            and a closely related non-specific dipeptidase
  JOURNAL   J Biol Chem 278 (8), 6521-6531 (2003)
   PUBMED   12473676
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35360.1,
                                           SRR22582416.268304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..492
                     /product="beta-Ala-His dipeptidase"
                     /EC_number="3.4.13.20"
                     /note="CNDP dipeptidase 1; carnosine dipeptidase 1
                     (metallopeptidase M20 family)"
                     /calculated_mol_wt=54797
     Region          13..481
                     /region_name="M20_dipept_like_CNDP"
                     /note="M20 cytosolic nonspecific dipeptidases including
                     anserinase and serum carnosinase; cd05676"
                     /db_xref="CDD:349925"
     Site            order(107,140,174..175,203,205,218,351,388,422,424..426,
                     453)
                     /site_type="active"
                     /db_xref="CDD:349925"
     Site            order(111,117,219,221,223,225,231..234,236..246,248,252,
                     255..256,259..261,295,298..300,303..304,312,315..316,
                     321..328,332..339,341..342,347,351,376..377,379,388,
                     423..424,452..455)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349925"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q66HG3.1)"
     CDS             1..492
                     /gene="Cndp1"
                     /coded_by="NM_001437340.1:336..1814"
                     /db_xref="GeneID:307212"
                     /db_xref="RGD:1359493"
ORIGIN      
        1 mlspphsgtl eklfqyidlh qdefvqtlke wvaiesdsvq pmprlrqelf rmmalaadkl
       61 rnlgarvdsv dlgsqqmpdg qslptppiil aelgndpkkp svcfyghldv qpaqkedgwl
      121 tdpytltevd gklygrgatd nkgpvlawin avstfralqq dlpvnvkfil egmeeagsva
      181 leelvkrekd nffsgvdyiv isdnlwlsqk kpaltcgtrg ncyftvevkc rdqdfhsgtf
      241 ggilnepmad lvallgslvd ssghilvpgi ydqmapitee ektmyenidl dleeyqkssr
      301 verflfdtke ellthlwryp slsihgiega fdepgtktvi pgrvlgkfsi rlvphmtpsv
      361 vetqvtqhle avfskrnsfn kmavsmvlgl qpwtaningt qylaarraiq tvfgvdpdmi
      421 qdgstipiak ifqditqksv mmlplgavdd gehsqnekin rwnyiqgskl faafflelsk
      481 lhsgqqvpsg af
//
LOCUS       NP_001424186             127 aa            linear   ROD 03-APR-2025
DEFINITION  small ribosomal subunit protein uS17m [Rattus norvegicus].
ACCESSION   NP_001424186
VERSION     NP_001424186.1
DBSOURCE    REFSEQ: accession NM_001437257.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399492.2036807.1,
                                           SRR26360194.921237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..127
                     /product="small ribosomal subunit protein uS17m"
                     /note="28S ribosomal protein S17, mitochondrial"
                     /calculated_mol_wt=13868
     Region          11..84
                     /region_name="Ribosomal_uS17"
                     /note="Ribosomal protein uS17; cd00364"
                     /db_xref="CDD:466775"
     CDS             1..127
                     /gene="Mrps17"
                     /coded_by="NM_001437257.1:257..640"
                     /db_xref="GeneID:288621"
                     /db_xref="RGD:1307650"
ORIGIN      
        1 msivrsavha kwvvgkvigt amvktakvra trlvldpyll kyfnkrktyf ahdalqqcsv
       61 gdivllralp vprakhvkhe laeiifkvgr vidpvtgkpc agtaylespl sseatppces
      121 reelkss
//
LOCUS       NP_001424309             154 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424309 XP_063131808
VERSION     NP_001424309.1
DBSOURCE    REFSEQ: accession NM_001437380.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063131808.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1196189.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680446,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..154
                     /product="uncharacterized protein CFAP97D2 isoform 4"
                     /calculated_mol_wt=18368
     CDS             1..154
                     /gene="Cfap97d2"
                     /coded_by="NM_001437380.1:78..542"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkrva
       61 samktgrrid gqnnftwrrk sreqalmkvq kqnqavperl rssepwygaq rwredwtama
      121 trpctcrhtw rkgadreaqq ghsliwmrsl krkg
//
LOCUS       NP_001020443             288 aa            linear   ROD 03-APR-2025
DEFINITION  serine/threonine-protein phosphatase PGAM5, mitochondrial isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001020443 XP_222256
VERSION     NP_001020443.2
DBSOURCE    REFSEQ: accession NM_001025272.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chen,Y., Huang,J., Zhou,H., Lin,J. and Tao,J.
  TITLE     Pgam5 aggravates hyperglycemia-induced myocardial dysfunction
            through disrupting Phb2-dependent mitochondrial dynamics
  JOURNAL   Int J Med Sci 21 (7), 1194-1203 (2024)
   PUBMED   38818468
  REMARK    GeneRIF: Pgam5 aggravates hyperglycemia-induced myocardial
            dysfunction through disrupting Phb2-dependent mitochondrial
            dynamics.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Fu,G., Wang,B., He,B., Feng,M. and Yu,Y.
  TITLE     LPS induces cardiomyocyte necroptosis through the Ripk3/Pgam5
            signaling pathway
  JOURNAL   J Recept Signal Transduct Res 41 (1), 32-37 (2021)
   PUBMED   32580628
  REMARK    GeneRIF: LPS induces cardiomyocyte necroptosis through the
            Ripk3/Pgam5 signaling pathway.
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Liu,G., Qian,M., Chen,M., Chen,T. and Qin,S.
  TITLE     miR-21-5p Suppresses Mitophagy to Alleviate Hyperoxia-Induced Acute
            Lung Injury by Directly Targeting PGAM5
  JOURNAL   Biomed Res Int 2020, 4807254 (2020)
   PUBMED   33681349
  REMARK    GeneRIF: miR-21-5p Suppresses Mitophagy to Alleviate
            Hyperoxia-Induced Acute Lung Injury by Directly Targeting PGAM5.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Yang,C., Liu,X., Yang,F., Zhang,W., Chen,Z., Yan,D., You,Q. and
            Wu,X.
  TITLE     Mitochondrial phosphatase PGAM5 regulates Keap1-mediated Bcl-xL
            degradation and controls cardiomyocyte apoptosis driven by
            myocardial ischemia/reperfusion injury
  JOURNAL   In Vitro Cell Dev Biol Anim 53 (3), 248-257 (2017)
   PUBMED   27815660
  REMARK    GeneRIF: PGAM5 controls cardiomyocyte apoptosis induced by MIRI
            through regulating Keap1-mediated Bcl-xL degradation, which may
            supply a novel molecular target for acute myocardial infarction
            (AMI) therapy.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Sekine,S., Yao,A., Hattori,K., Sugawara,S., Naguro,I., Koike,M.,
            Uchiyama,Y., Takeda,K. and Ichijo,H.
  TITLE     The Ablation of Mitochondrial Protein Phosphatase Pgam5 Confers
            Resistance Against Metabolic Stress
  JOURNAL   EBioMedicine 5, 82-92 (2016)
   PUBMED   27077115
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Wei,H., Liu,L. and Chen,Q.
  TITLE     Selective removal of mitochondria via mitophagy: distinct pathways
            for different mitochondrial stresses
  JOURNAL   Biochim Biophys Acta 1853 (10 Pt B), 2784-2790 (2015)
   PUBMED   25840011
  REMARK    Review article
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Hayes,J.D. and Dinkova-Kostova,A.T.
  TITLE     The Nrf2 regulatory network provides an interface between redox and
            intermediary metabolism
  JOURNAL   Trends Biochem Sci 39 (4), 199-218 (2014)
   PUBMED   24647116
  REMARK    Review article
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Wang,Z., Jiang,H., Chen,S., Du,F. and Wang,X.
  TITLE     The mitochondrial phosphatase PGAM5 functions at the convergence
            point of multiple necrotic death pathways
  JOURNAL   Cell 148 (1-2), 228-243 (2012)
   PUBMED   22265414
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Takeda,K., Komuro,Y., Hayakawa,T., Oguchi,H., Ishida,Y.,
            Murakami,S., Noguchi,T., Kinoshita,H., Sekine,Y., Iemura,S.,
            Natsume,T. and Ichijo,H.
  TITLE     Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic
            activity as a protein serine/threonine phosphatase to activate ASK1
  JOURNAL   Proc Natl Acad Sci U S A 106 (30), 12301-12305 (2009)
   PUBMED   19590015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced NP_001020443.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092607.1, SRR26643288.48362.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..288
                     /product="serine/threonine-protein phosphatase PGAM5,
                     mitochondrial isoform 1"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase PGAM5,
                     mitochondrial; phosphoglycerate mutase family member 5"
                     /calculated_mol_wt=31869
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q562B5.1)"
     Region          13..286
                     /region_name="HP"
                     /note="Histidine phosphatase domain found in a
                     functionally diverse set of proteins, mostly phosphatases;
                     contains a His residue which is phosphorylated during the
                     reaction; cl11399"
                     /db_xref="CDD:472174"
     Site            24..25
                     /site_type="cleavage"
                     /note="Cleavage, by PARL.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            order(103..104,151,229..230)
                     /site_type="active"
                     /note="catalytic core [active]"
                     /db_xref="CDD:132718"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     CDS             1..288
                     /gene="Pgam5"
                     /gene_synonym="RGD1312028"
                     /coded_by="NM_001025272.2:31..897"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288731"
                     /db_xref="RGD:1312028"
ORIGIN      
        1 mafrqalqla acglaggsaa vlfsavavgk praggdadtr tteplawtga rpghgvwdsn
       61 wdrreplsli nlkkrnvesg edelasrldh ykakatrhif lirhsqynvd gsmekdrtlt
      121 plgreqaelt girlaslglk fnkivhssmt ravettdiis khlpgvcrvs tdllregapi
      181 epdppvshwk peavqyyedg arieaafrny ihradakqee dsyeificha nviryivcra
      241 lqfppegwlr lslnngsith lvirpngrva lrtlgdtgfm ppdkitrs
//
LOCUS       NP_001424356             556 aa            linear   ROD 03-APR-2025
DEFINITION  inactive serine/threonine-protein kinase PLK5 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424356 XP_063119488
VERSION     NP_001424356.1
DBSOURCE    REFSEQ: accession NM_001437427.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   de Carcer,G., Escobar,B., Higuero,A.M., Garcia,L., Anson,A.,
            Perez,G., Mollejo,M., Manning,G., Melendez,B., Abad-Rodriguez,J.
            and Malumbres,M.
  TITLE     Plk5, a polo box domain-only protein with specific roles in neuron
            differentiation and glioblastoma suppression
  JOURNAL   Mol Cell Biol 31 (6), 1225-1239 (2011)
   PUBMED   21245385
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Andrysik,Z., Bernstein,W.Z., Deng,L., Myer,D.L., Li,Y.Q.,
            Tischfield,J.A., Stambrook,P.J. and Bahassi el,M.
  TITLE     The novel mouse Polo-like kinase 5 responds to DNA damage and
            localizes in the nucleolus
  JOURNAL   Nucleic Acids Res 38 (9), 2931-2943 (2010)
   PUBMED   20100802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063119488.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38029.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..556
                     /product="inactive serine/threonine-protein kinase PLK5
                     isoform 4"
                     /EC_number="2.7.11.21"
                     /note="polo-like kinase 5 pseudogene;
                     serine/threonine-protein kinase PLK5; inactive
                     serine/threonine-protein kinase PLK5"
                     /calculated_mol_wt=60964
     Region          25..240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          371..458
                     /region_name="POLO_box_1"
                     /note="First polo-box domain (PBD) of polo-like kinases
                     Plk1, Plk2, Plk3, and Plk5; cd13118"
                     /db_xref="CDD:240561"
     Site            order(377..380,449,451..455)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:240561"
     CDS             1..556
                     /gene="Plk5"
                     /gene_synonym="Plk5p"
                     /coded_by="NM_001437427.1:79..1749"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:314627"
                     /db_xref="RGD:1305038"
ORIGIN      
        1 meprlrrrrs rqlvatflrd pgsgrvyrrg kligkgafsr cykltdmsts avfalkvvpr
       61 ggagrlrlrg kslahvlkvr rtltepevry yfrglvsglr ylhqqrivhr dlkpsnffln
      121 knmevkigdl glaarvgpag rchrvlcgtp nfqapevvsr nghsaksdiw algcimytvl
      181 tgtppfaaap lsemyqnird ghyleptqls psarsliarl lapdpderps ldhllqddff
      241 sqgftperlp phschsppvf afppplgrlf rkvgqllltq crppcpftsk easgpgeest
      301 epdhmeasne egaplctesr ihlltlgtpr tdpadakgtl alqlevatrk lclcldagpv
      361 agqdppgeqr svlwapkwvd yslkygfgyq lsdggsgvlf rdgshmalrp pgghvsyqpd
      421 qgtlwifalr dvpgplrakl avlrlfacym qrrlreegta pmtatpaspd fcllsftada
      481 qalamlfsng tvqvssktsp vqlvlsgege dflltiqepg gpsmgtsytl dvlrshgisl
      541 avrhhlrlgl hllqsv
//
LOCUS       NP_001011924             533 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001011924 XP_214530
VERSION     NP_001011924.1
DBSOURCE    REFSEQ: accession NM_001011924.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Feb 11, 2005 this sequence version replaced XP_214530.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081932.1, SRR26643293.77805.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..533
                     /product="methyl-CpG-binding domain protein 1 isoform 8"
                     /calculated_mol_wt=58025
     Region          3..72
                     /region_name="MBD"
                     /note="Methyl-CpG binding domain; smart00391"
                     /db_xref="CDD:128673"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..533
                     /gene="Mbd1"
                     /coded_by="NM_001011924.2:162..1763"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekg
      241 kydhskrgpr vasrrhsrap plpphaasqh peptelhisd qtptapaefv ydcveedelk
      301 rllpsigpgs eeearllphh thqkrsastr qlqlssplka plavvttppg pvqdsgkrqa
      361 gsgfvlpqpd tdlvylqegt sslmqvpgpa aastenpaqe tqgsapgwvv alpqvkqeka
      421 dapeewtavt tfltsstvqp gflskasgld pppvkreppg peedgeenke ddvsesapae
      481 eiggigtpvi teifslggtr lrdaeawlpr lhkllavnen eyftelqlke eil
//
LOCUS       NP_001424322             293 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 68 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424322 XP_063133259
VERSION     NP_001424322.1
DBSOURCE    REFSEQ: accession NM_001437393.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133259.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1000149.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..293
                     /product="coiled-coil domain-containing protein 68 isoform
                     2"
                     /note="CTCL tumor antigen se57-1; coiled-coil
                     domain-containing protein 68"
                     /calculated_mol_wt=33579
     Region          <85..271
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..293
                     /gene="Ccdc68"
                     /gene_synonym="RGD1561424"
                     /coded_by="NM_001437393.1:148..1029"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:291530"
                     /db_xref="RGD:1561424"
ORIGIN      
        1 mttvtvtmev psggktedrs ifsgpssaqi ieeteyvrki rttlekirnr mfkeedgrgn
       61 arhkvdaeqs gnvqngldst tdptrldlll esmrrkdqql lemnkenevl qikleasrea
      121 gaaalrnaaq rlfdnyqtqs edlekkhkds khvlqvnkle keqtlkqrak nlsqlseklg
      181 ekheqivgle nrvqrmeneq ichlqfvihs qhqnlrniiq emeglkntlk eqdkkienlk
      241 ekvtvleaqn eelktkvahw tesprtsvsk avstselkte gaspylmlir lrk
//
LOCUS       NP_001424283             559 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424283
VERSION     NP_001424283.1
DBSOURCE    REFSEQ: accession NM_001437354.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85237.1,
                                           SRR26360181.3026278.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..559
                     /product="coiled-coil domain-containing protein 63 isoform
                     1"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65977
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..559
                     /gene="Ccdc63"
                     /coded_by="NM_001437354.1:172..1851"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eevphralsw vqwntlwttv asgswswrtt
      541 frrneeknhr rhcwrrgtr
//
LOCUS       NP_001102446             122 aa            linear   ROD 03-APR-2025
DEFINITION  U7 snRNA-associated Sm-like protein LSm10 [Rattus norvegicus].
ACCESSION   NP_001102446 XP_001056695 XP_345582
VERSION     NP_001102446.1
DBSOURCE    REFSEQ: accession NM_001108976.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Yang,X.C., Torres,M.P., Marzluff,W.F. and Dominski,Z.
  TITLE     Three proteins of the U7-specific Sm ring function as the molecular
            ruler to determine the site of 3'-end processing in mammalian
            histone pre-mRNA
  JOURNAL   Mol Cell Biol 29 (15), 4045-4056 (2009)
   PUBMED   19470752
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Wagner,E.J. and Marzluff,W.F.
  TITLE     ZFP100, a component of the active U7 snRNP limiting for histone
            pre-mRNA processing, is required for entry into S phase
  JOURNAL   Mol Cell Biol 26 (17), 6702-6712 (2006)
   PUBMED   16914750
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Pillai,R.S., Will,C.L., Luhrmann,R., Schumperli,D. and Muller,B.
  TITLE     Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain
            Lsm10, a new 14 kDa Sm D1-like protein
  JOURNAL   EMBO J 20 (19), 5470-5479 (2001)
   PUBMED   11574479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_345582.1, XP_001056695.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20782.1,
                                           SRR26360176.858815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..122
                     /product="U7 snRNA-associated Sm-like protein LSm10"
                     /note="U7 snRNP-specific Sm-like protein LSM10"
                     /calculated_mol_wt=13749
     Region          8..85
                     /region_name="LSm10"
                     /note="Like-Sm protein 10; cd01733"
                     /db_xref="CDD:212480"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212480"
     Site            order(47,49,75)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212480"
     Site            71..82
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212480"
     CDS             1..122
                     /gene="Lsm10"
                     /coded_by="NM_001108976.2:79..447"
                     /db_xref="GeneID:366468"
                     /db_xref="RGD:1584914"
ORIGIN      
        1 malshsvker tisensliil lqglqgqitt vdlrdesvar gridnvdafm nirlanvtyt
       61 drwghqveld dlfvtgrnvr yvhipdgvni tatieqqlqi ihrvrnfggk gqgrrefpsk
      121 rp
//
LOCUS       NP_001424291             526 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424291
VERSION     NP_001424291.1
DBSOURCE    REFSEQ: accession NM_001437362.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1526770.1,
                                           SRR26360181.226334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..526
                     /product="coiled-coil domain-containing protein 63 isoform
                     3"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=61429
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..526
                     /gene="Ccdc63"
                     /coded_by="NM_001437362.1:172..1752"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeelcpgcsg ipsgpq
//
LOCUS       NP_001424207            1038 aa            linear   ROD 03-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform c [Rattus norvegicus].
ACCESSION   NP_001424207 XP_063144212
VERSION     NP_001424207.1
DBSOURCE    REFSEQ: accession NM_001437278.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1038)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1038)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1038)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1038)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1038)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1038)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1038)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063144212.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21986.1,
                                           SRR26360181.2275346.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1038
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform c"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=119022
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..275
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          308..475
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          498..678
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          670..1036
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(746,748..750,752,754,771,773,776,807,819..822,827,
                     830,892,894,904..905)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(814..815,916..917,919,921,987,990)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            861
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            884..892
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            905..929
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1038
                     /gene="Pik3cd"
                     /coded_by="NM_001437278.1:317..3433"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse vstkdmplal macalrkkat vfrqplverp eeyalqvngr
      241 heylygsypl chfqyicscl hsgltphltm vhsssilamr deqsnpapqv qkprvkpppi
      301 pakkpssvsl wsleqpfcie liegrkvnad ermklvvqag lfhgnemlck tvsssevnvc
      361 sepvwkqrle fdisicdlpr marlcfalya vvekakkars tkkkskkadc piawanlmlf
      421 dykdqlktge rclymwpsvp dekgelmnpa gtvrgnpnte saaalviylp evaphpvyfp
      481 alekilelgr hgergritee eqlqlreile rrgsgelyeh ekdlvwkmrh evqehfpeal
      541 arlllvtkwn khedvaqmly llcswpelpv lsalelldfs fpdcyvgsfa ikslrkltdd
      601 elfqyllqlv qvlkyesyld celtkfllgr alanrkighf lfwhlrsemh vpsvalrfgl
      661 imeaycrgst hhmkvlmkqg ealsklkaln dfvkassqkt tkpqtkemmh mcmrqetyme
      721 alshlqspld pstlleevcv eqctfmdskm kplwimysse kaggagsvgi ifkngddlrq
      781 dmltlqmiql mdflwkqegl dlrmtpygcl ptgdrtglie vvlhsdtian iqlnksnmaa
      841 taafnkdall nwlksknpge aldraieeft lscagycvat yvlgigdrhs dnimiresgq
      901 lfhidfghfl gnfktkfgin rervpfilty dfvhviqqgk tnnsekferf rgycerayti
      961 lrrhgllflh lfalmraagl pelscskdiq ylkdslalgk teeealkhfr vkfnealres
     1021 wktkvnwlah nvskdnrq
//
LOCUS       NP_001102441             716 aa            linear   ROD 03-APR-2025
DEFINITION  myogenesis-regulating glycosidase [Rattus norvegicus].
ACCESSION   NP_001102441 XP_001068567 XP_345525
VERSION     NP_001102441.1
DBSOURCE    REFSEQ: accession NM_001108971.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Datta,K., Guan,T. and Gerace,L.
  TITLE     NET37, a nuclear envelope transmembrane protein with glycosidase
            homology, is involved in myoblast differentiation
  JOURNAL   J Biol Chem 284 (43), 29666-29676 (2009)
   PUBMED   19706595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_345525.1, XP_001068567.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.19021.1,
                                           SRR26643296.14972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..716
                     /product="myogenesis-regulating glycosidase"
                     /calculated_mol_wt=81212
     Region          313..684
                     /region_name="GH31_NET37"
                     /note="glucosidase NET37; cd06592"
                     /db_xref="CDD:269878"
     Site            order(352..353,460,462..463,501,519,603,605)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269878"
     CDS             1..716
                     /gene="Myorg"
                     /gene_synonym="RGD1309821"
                     /coded_by="NM_001108971.2:185..2335"
                     /db_xref="GeneID:366360"
                     /db_xref="RGD:1309821"
ORIGIN      
        1 mpqnlqeksq vyprhrlgsh agpkslevip gatmytflpd nfspakpkpt kelrpllcsv
       61 vlglllvlaa vvawcyysas lrkaerlrae lldlnrggfs irnqkgeqvf rlafrsgald
      121 ldscsrdgal lgcsrtadgr plhffiqtvr pkdtvmcyrv rweeaapgra vehamflgda
      181 aahwyggaem rtqhwpirld gqqepqpfvt sdvyssdaaf ggilerywls sraaaikvnd
      241 svpfhlgwns tersmrlqar yhhtsykppa grtaapelsy rvcvgsdvts ihkymvrryf
      301 nkpsrvpase afrdpiwstw alygrsvdqn kvlqfaqqir qhrfnsshle iddmytpayg
      361 dfdfdeskfp natdlfhrlr dagfrvtlwv hpfvnynssr fgegverelf vreptgrlpa
      421 lvrwwngiga vldftrpear ewfqghlrrl rsrynvasfk fdagevsylp pdfstykpls
      481 dpsvwsrryt emalpffsla evrvgyqsqn iscffrlvdr dsvwgydlgl rslipavltv
      541 smlgypfilp dmiggnavpe rtagrpdgpg perelyvrwl evaafmpamq fsippwqyda
      601 evvaiahkfa alraslvapl llelagevtd tgdpivrplw wiapgdetah ridsqfligd
      661 tllvapvlep gkqerdvylp agkwrsykge lfdktpvllt dypvdldeva yftwas
//
LOCUS       NP_001424205            1047 aa            linear   ROD 03-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform b [Rattus norvegicus].
ACCESSION   NP_001424205 XP_038966427
VERSION     NP_001424205.1
DBSOURCE    REFSEQ: accession NM_001437276.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038966427.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1213213.1,
                                           SRR26643298.30339.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1047
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform b"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=120091
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..281
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          314..481
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          504..687
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          679..1045
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(755,757..759,761,763,780,782,785,816,828..831,836,
                     839,901,903,913..914)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(823..824,925..926,928,930,996,999)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            870
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            893..901
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            914..938
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1047
                     /gene="Pik3cd"
                     /coded_by="NM_001437276.1:204..3347"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse esftfqvstk dmplalmaca lrkkatvfrq plverpeeya
      241 lqvngrheyl ygsyplchfq yicsclhsgl tphltmvhss silamrdeqs npapqvqkpr
      301 vkpppipakk pssvslwsle qpfcielieg rkvnadermk lvvqaglfhg nemlcktvss
      361 sevnvcsepv wkqrlefdis icdlprmarl cfalyavvek akkarstkkk skkadcpiaw
      421 anlmlfdykd qlktgercly mwpsvpdekg elmnpagtvr gnpntesaaa lviylpevap
      481 hpvyfpalek ilelgrhger griteeeqlq lreilerrgs gelyehekdl vwkmrhevqe
      541 hfpealarll lvtkwnkhed vaqlsqmlyl lcswpelpvl salelldfsf pdcyvgsfai
      601 kslrkltdde lfqyllqlvq vlkyesyldc eltkfllgra lanrkighfl fwhlrsemhv
      661 psvalrfgli meaycrgsth hmkvlmkqge alsklkalnd fvkassqktt kpqtkemmhm
      721 cmrqetymea lshlqspldp stlleevcve qctfmdskmk plwimyssek aggagsvgii
      781 fkngddlrqd mltlqmiqlm dflwkqegld lrmtpygclp tgdrtgliev vlhsdtiani
      841 qlnksnmaat aafnkdalln wlksknpgea ldraieeftl scagycvaty vlgigdrhsd
      901 nimiresgql fhidfghflg nfktkfginr ervpfiltyd fvhviqqgkt nnsekferfr
      961 gyceraytil rrhgllflhl falmraaglp elscskdiqy lkdslalgkt eeealkhfrv
     1021 kfnealresw ktkvnwlahn vskdnrq
//
LOCUS       NP_001424147             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424147
VERSION     NP_001424147.1
DBSOURCE    REFSEQ: accession NM_001437218.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.34968.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437218.1:86..2482"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424305             576 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424305 XP_006254975
VERSION     NP_001424305.1
DBSOURCE    REFSEQ: accession NM_001437376.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254975.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77807.1,
                                           SRR26643287.35257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..576
                     /product="methyl-CpG-binding domain protein 1 isoform 6"
                     /calculated_mol_wt=63192
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          <291..549
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..576
                     /gene="Mbd1"
                     /coded_by="NM_001437376.1:162..1892"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elkrllpsig pgseeearll
      361 phhthqkrsa strqlqlssp lkaplavvtt ppgpvqdsgk rqagsgfvlp qpdtdlvylq
      421 egtsslmqvp gpaaastenp aqetqgsapg wvvalpqvkq ekadapeewt avttfltsst
      481 vqpgflskas gldpppvkre ppgpeedgee nkeddvsesa paeeiggigt pviteifslg
      541 gtrlrdaeaw lprlhkllav neneyftelq lkeeil
//
LOCUS       NP_001424175             122 aa            linear   ROD 03-APR-2025
DEFINITION  U7 snRNA-associated Sm-like protein LSm10 [Rattus norvegicus].
ACCESSION   NP_001424175
VERSION     NP_001424175.1
DBSOURCE    REFSEQ: accession NM_001437246.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Yang,X.C., Torres,M.P., Marzluff,W.F. and Dominski,Z.
  TITLE     Three proteins of the U7-specific Sm ring function as the molecular
            ruler to determine the site of 3'-end processing in mammalian
            histone pre-mRNA
  JOURNAL   Mol Cell Biol 29 (15), 4045-4056 (2009)
   PUBMED   19470752
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Wagner,E.J. and Marzluff,W.F.
  TITLE     ZFP100, a component of the active U7 snRNP limiting for histone
            pre-mRNA processing, is required for entry into S phase
  JOURNAL   Mol Cell Biol 26 (17), 6702-6712 (2006)
   PUBMED   16914750
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Pillai,R.S., Will,C.L., Luhrmann,R., Schumperli,D. and Muller,B.
  TITLE     Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain
            Lsm10, a new 14 kDa Sm D1-like protein
  JOURNAL   EMBO J 20 (19), 5470-5479 (2001)
   PUBMED   11574479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.999440.1,
                                           SRR26360172.868169.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..122
                     /product="U7 snRNA-associated Sm-like protein LSm10"
                     /note="U7 snRNP-specific Sm-like protein LSM10"
                     /calculated_mol_wt=13749
     Region          8..85
                     /region_name="LSm10"
                     /note="Like-Sm protein 10; cd01733"
                     /db_xref="CDD:212480"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212480"
     Site            order(47,49,75)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212480"
     Site            71..82
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212480"
     CDS             1..122
                     /gene="Lsm10"
                     /coded_by="NM_001437246.1:906..1274"
                     /db_xref="GeneID:366468"
                     /db_xref="RGD:1584914"
ORIGIN      
        1 malshsvker tisensliil lqglqgqitt vdlrdesvar gridnvdafm nirlanvtyt
       61 drwghqveld dlfvtgrnvr yvhipdgvni tatieqqlqi ihrvrnfggk gqgrrefpsk
      121 rp
//
LOCUS       NP_001424244             910 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF216 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424244 XP_038945291
VERSION     NP_001424244.1
DBSOURCE    REFSEQ: accession NM_001437315.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Chen,T., Zhu,J. and Wang,Y.H.
  TITLE     RNF216 mediates neuronal injury following experimental subarachnoid
            hemorrhage through the Arc/Arg3.1-AMPAR pathway
  JOURNAL   FASEB J 34 (11), 15080-15092 (2020)
   PUBMED   32918771
  REMARK    GeneRIF: RNF216 mediates neuronal injury following experimental
            subarachnoid hemorrhage through the Arc/Arg3.1-AMPAR pathway.
            Erratum:[FASEB J. 2024 May 15;38(9):e23652. doi:
            10.1096/fj.202400924. PMID: 38708783]
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Mabb,A.M., Je,H.S., Wall,M.J., Robinson,C.G., Larsen,R.S.,
            Qiang,Y., Correa,S.A. and Ehlers,M.D.
  TITLE     Triad3A regulates synaptic strength by ubiquitination of Arc
  JOURNAL   Neuron 82 (6), 1299-1316 (2014)
   PUBMED   24945773
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Nakhaei,P., Mesplede,T., Solis,M., Sun,Q., Zhao,T., Yang,L.,
            Chuang,T.H., Ware,C.F., Lin,R. and Hiscott,J.
  TITLE     The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
            signaling pathway by targeting TRAF3 for degradation
  JOURNAL   PLoS Pathog 5 (11), e1000650 (2009)
   PUBMED   19893624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038945291.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.30440.1,
                                           SRR26643284.15416.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..910
                     /product="E3 ubiquitin-protein ligase RNF216 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF216"
                     /calculated_mol_wt=104014
     Region          558..614
                     /region_name="RING-HC_RBR_RNF216"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 216 (RNF216) and similar proteins; cd16630"
                     /db_xref="CDD:438292"
     Region          647..698
                     /region_name="BRcat_RBR_RNF216"
                     /note="BRcat domain found in RING finger protein 216
                     (RNF216); cd20339"
                     /db_xref="CDD:439000"
     Region          709..765
                     /region_name="Rcat_RBR_RNF216"
                     /note="Rcat domain found in RING finger protein 216
                     (RNF216); cd20353"
                     /db_xref="CDD:439014"
     CDS             1..910
                     /gene="Rnf216"
                     /gene_synonym="RGD1565135"
                     /coded_by="NM_001437315.1:226..2958"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:304294"
                     /db_xref="RGD:1565135"
ORIGIN      
        1 maegnnqeev ihlnnfhchr gkewmavreg pitisdssde egipmlvtpa teqqeddldd
       61 dviltethkp qtsrpnlikp aaewqdlnrl geerprksra dfeadthsyf sfcnnslfds
      121 gaqddsedec ggfldlktek kggeakpgps nkqtadntvs prleqkviil gengllfses
      181 eplevqnqls edsetdllsn pgepaasvde qlieeeywld hpyfqalnpq pqertnqlvp
      241 qerhsesemg pmffrhdfpe pafprpepqq egipgpaspq pahplgeled qqlaidedpg
      301 payplpgpqe anlanvwgqe aaegdqelip llvketearf pdvangyvee iihlknyydl
      361 nvlcnfllen pdypkredri lihpssslla sqddvklpki dffdyskltp ldqrcfiqaa
      421 dllmadfkml ssqdikwalh elkghyaitr kafsdaikkw qelspetsgk rkkrkemnqy
      481 sfidfkfeqg nikiekrmff lenkrrhcrs ydqqallpav qqeqefyeqk ikemaehedf
      541 llalqmneeq yqkdgqliec rccygefpfe eltqcadahl fckeclirya qeavfgsgks
      601 elscmegsct csfptselek vlpqtilyky yerkaeeeva aayadelvrc pscsfpalld
      661 sdvkrfscpn prcrketcrk cqglwkehng ltceelaekd dikyrtsiee kmtaarirkc
      721 hkcgtgliks egcnrmscrc gaqmcylcrv singydhfcq hprspgapcq ecsrcslwtd
      781 pteddeklie eiqkeaeeeq krkngentfk rigpplekpa ekvqrvealp rpvpqnlhpq
      841 mppyafvhpp fplppvrpvf nnfpinmgpv papyvpplpn vrvnfdfghv hvplehnlpm
      901 hfgpqprhrf
//
LOCUS       NP_001100592             910 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF216 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100592 XP_001064065 XP_038945292 XP_221922
VERSION     NP_001100592.1
DBSOURCE    REFSEQ: accession NM_001107122.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Chen,T., Zhu,J. and Wang,Y.H.
  TITLE     RNF216 mediates neuronal injury following experimental subarachnoid
            hemorrhage through the Arc/Arg3.1-AMPAR pathway
  JOURNAL   FASEB J 34 (11), 15080-15092 (2020)
   PUBMED   32918771
  REMARK    GeneRIF: RNF216 mediates neuronal injury following experimental
            subarachnoid hemorrhage through the Arc/Arg3.1-AMPAR pathway.
            Erratum:[FASEB J. 2024 May 15;38(9):e23652. doi:
            10.1096/fj.202400924. PMID: 38708783]
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Mabb,A.M., Je,H.S., Wall,M.J., Robinson,C.G., Larsen,R.S.,
            Qiang,Y., Correa,S.A. and Ehlers,M.D.
  TITLE     Triad3A regulates synaptic strength by ubiquitination of Arc
  JOURNAL   Neuron 82 (6), 1299-1316 (2014)
   PUBMED   24945773
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Nakhaei,P., Mesplede,T., Solis,M., Sun,Q., Zhao,T., Yang,L.,
            Chuang,T.H., Ware,C.F., Lin,R. and Hiscott,J.
  TITLE     The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
            signaling pathway by targeting TRAF3 for degradation
  JOURNAL   PLoS Pathog 5 (11), e1000650 (2009)
   PUBMED   19893624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_038945292.1, XP_221922.4, XP_001064065.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.40498.1,
                                           SRR26360190.2659199.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..910
                     /product="E3 ubiquitin-protein ligase RNF216 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF216"
                     /calculated_mol_wt=104014
     Region          558..614
                     /region_name="RING-HC_RBR_RNF216"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 216 (RNF216) and similar proteins; cd16630"
                     /db_xref="CDD:438292"
     Region          647..698
                     /region_name="BRcat_RBR_RNF216"
                     /note="BRcat domain found in RING finger protein 216
                     (RNF216); cd20339"
                     /db_xref="CDD:439000"
     Region          709..765
                     /region_name="Rcat_RBR_RNF216"
                     /note="Rcat domain found in RING finger protein 216
                     (RNF216); cd20353"
                     /db_xref="CDD:439014"
     CDS             1..910
                     /gene="Rnf216"
                     /gene_synonym="RGD1565135"
                     /coded_by="NM_001107122.2:161..2893"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304294"
                     /db_xref="RGD:1565135"
ORIGIN      
        1 maegnnqeev ihlnnfhchr gkewmavreg pitisdssde egipmlvtpa teqqeddldd
       61 dviltethkp qtsrpnlikp aaewqdlnrl geerprksra dfeadthsyf sfcnnslfds
      121 gaqddsedec ggfldlktek kggeakpgps nkqtadntvs prleqkviil gengllfses
      181 eplevqnqls edsetdllsn pgepaasvde qlieeeywld hpyfqalnpq pqertnqlvp
      241 qerhsesemg pmffrhdfpe pafprpepqq egipgpaspq pahplgeled qqlaidedpg
      301 payplpgpqe anlanvwgqe aaegdqelip llvketearf pdvangyvee iihlknyydl
      361 nvlcnfllen pdypkredri lihpssslla sqddvklpki dffdyskltp ldqrcfiqaa
      421 dllmadfkml ssqdikwalh elkghyaitr kafsdaikkw qelspetsgk rkkrkemnqy
      481 sfidfkfeqg nikiekrmff lenkrrhcrs ydqqallpav qqeqefyeqk ikemaehedf
      541 llalqmneeq yqkdgqliec rccygefpfe eltqcadahl fckeclirya qeavfgsgks
      601 elscmegsct csfptselek vlpqtilyky yerkaeeeva aayadelvrc pscsfpalld
      661 sdvkrfscpn prcrketcrk cqglwkehng ltceelaekd dikyrtsiee kmtaarirkc
      721 hkcgtgliks egcnrmscrc gaqmcylcrv singydhfcq hprspgapcq ecsrcslwtd
      781 pteddeklie eiqkeaeeeq krkngentfk rigpplekpa ekvqrvealp rpvpqnlhpq
      841 mppyafvhpp fplppvrpvf nnfpinmgpv papyvpplpn vrvnfdfghv hvplehnlpm
      901 hfgpqprhrf
//
LOCUS       NP_001424204            1044 aa            linear   ROD 03-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform a [Rattus norvegicus].
ACCESSION   NP_001424204 XP_063144209
VERSION     NP_001424204.1
DBSOURCE    REFSEQ: accession NM_001437275.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1044)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1044)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1044)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1044)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1044)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1044)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1044)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063144209.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.25629.1,
                                           SRR26643429.21985.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1044
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform a"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=119762
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..281
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          314..481
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          504..684
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          676..1042
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(752,754..756,758,760,777,779,782,813,825..828,833,
                     836,898,900,910..911)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(820..821,922..923,925,927,993,996)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            867
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            890..898
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            911..935
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1044
                     /gene="Pik3cd"
                     /coded_by="NM_001437275.1:317..3451"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse esftfqvstk dmplalmaca lrkkatvfrq plverpeeya
      241 lqvngrheyl ygsyplchfq yicsclhsgl tphltmvhss silamrdeqs npapqvqkpr
      301 vkpppipakk pssvslwsle qpfcielieg rkvnadermk lvvqaglfhg nemlcktvss
      361 sevnvcsepv wkqrlefdis icdlprmarl cfalyavvek akkarstkkk skkadcpiaw
      421 anlmlfdykd qlktgercly mwpsvpdekg elmnpagtvr gnpntesaaa lviylpevap
      481 hpvyfpalek ilelgrhger griteeeqlq lreilerrgs gelyehekdl vwkmrhevqe
      541 hfpealarll lvtkwnkhed vaqmlyllcs wpelpvlsal elldfsfpdc yvgsfaiksl
      601 rkltddelfq yllqlvqvlk yesyldcelt kfllgralan rkighflfwh lrsemhvpsv
      661 alrfglimea ycrgsthhmk vlmkqgeals klkalndfvk assqkttkpq tkemmhmcmr
      721 qetymealsh lqspldpstl leevcveqct fmdskmkplw imyssekagg agsvgiifkn
      781 gddlrqdmlt lqmiqlmdfl wkqegldlrm tpygclptgd rtglievvlh sdtianiqln
      841 ksnmaataaf nkdallnwlk sknpgealdr aieeftlsca gycvatyvlg igdrhsdnim
      901 iresgqlfhi dfghflgnfk tkfginrerv pfiltydfvh viqqgktnns ekferfrgyc
      961 eraytilrrh gllflhlfal mraaglpels cskdiqylkd slalgkteee alkhfrvkfn
     1021 ealreswktk vnwlahnvsk dnrq
//
LOCUS       NP_001424165             314 aa            linear   ROD 03-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001424165 XP_063127232
VERSION     NP_001424165.1
DBSOURCE    REFSEQ: accession NM_001437236.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127232.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.84522.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001437236.1:243..1187"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001424160             268 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein C9orf153 homolog isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424160 XP_063132079
VERSION     NP_001424160.1
DBSOURCE    REFSEQ: accession NM_001437231.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063132079.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.819143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..268
                     /product="uncharacterized protein C9orf153 homolog isoform
                     1"
                     /note="uncharacterized protein C9orf153 homolog"
                     /calculated_mol_wt=30879
     Region          1..92
                     /region_name="DUF5532"
                     /note="Family of unknown function (DUF5532); pfam17673"
                     /db_xref="CDD:465450"
     CDS             1..268
                     /gene="C17h9orf153"
                     /coded_by="NM_001437231.1:298..1104"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:100912252"
                     /db_xref="RGD:6488044"
ORIGIN      
        1 msstrhhtwt rgsigslylh rcslpelyas leifnkeskk snlqkicgms fkeaqevlwk
       61 ilgglisdsy dtvkgderhp sipvnkeerk tpsmsdllhq sllkgynvpl eqvhssqqrl
      121 aqvgippppl sfphglsnel pvilpaqhfr kriqsvtfrk lllssvapgr lfyeekptsq
      181 qvsfdpgkqf ldladlqwry fkglakwgkm prrfsllnie ynsekryven qrmsglifpp
      241 lvrktlmvyp qaeydkegql yltwkivy
//
LOCUS       NP_001424162             209 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein C9orf153 homolog isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424162 XP_063132081
VERSION     NP_001424162.1
DBSOURCE    REFSEQ: accession NM_001437233.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063132081.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1239906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..209
                     /product="uncharacterized protein C9orf153 homolog isoform
                     2"
                     /note="uncharacterized protein C9orf153 homolog"
                     /calculated_mol_wt=23405
     Region          1..92
                     /region_name="DUF5532"
                     /note="Family of unknown function (DUF5532); pfam17673"
                     /db_xref="CDD:465450"
     CDS             1..209
                     /gene="C17h9orf153"
                     /coded_by="NM_001437233.1:233..862"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:100912252"
                     /db_xref="RGD:6488044"
ORIGIN      
        1 msstrhhtwt rgsigslylh rcslpelyas leifnkeskk snlqkicgms fkeaqevlwk
       61 ilgglisdsy dtvkgderhp sipvnkeerk tpsmsdllhq sllkgynvpl eqvhssqqrl
      121 aqvgippppl sfphglsnel pvilpaqhfr kriqsvtfrk lllssvapgr lfyeekptsq
      181 qvsfdpgkqf ldladlqwss qdsdglpss
//
LOCUS       NP_001424311              74 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424311 XP_038950770
VERSION     NP_001424311.1
DBSOURCE    REFSEQ: accession NM_001437382.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038950770.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2469682.1,
                                           SRR26360194.1476070.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..74
                     /product="uncharacterized protein CFAP97D2 isoform 6"
                     /calculated_mol_wt=8444
     CDS             1..74
                     /gene="Cfap97d2"
                     /coded_by="NM_001437382.1:85..309"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkeli
       61 vkpnkatass gcaa
//
LOCUS       NP_001424290             558 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424290 XP_063127392
VERSION     NP_001424290.1
DBSOURCE    REFSEQ: accession NM_001437361.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127392.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..558
                     /product="coiled-coil domain-containing protein 63 isoform
                     2"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65522
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..558
                     /gene="Ccdc63"
                     /coded_by="NM_001437361.1:705..2381"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeveypldhs slrqlvleny lqkergkepq
      541 etllekgdei rvkkkvis
//
LOCUS       NP_001424334             497 aa            linear   ROD 03-APR-2025
DEFINITION  myotilin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424334 XP_006254729
VERSION     NP_001424334.1
DBSOURCE    REFSEQ: accession NM_001437405.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   von Nandelstadh,P., Ismail,M., Gardin,C., Suila,H., Zara,I.,
            Belgrano,A., Valle,G., Carpen,O. and Faulkner,G.
  TITLE     A class III PDZ binding motif in the myotilin and FATZ families
            binds enigma family proteins: a common link for Z-disc myopathies
  JOURNAL   Mol Cell Biol 29 (3), 822-834 (2009)
   PUBMED   19047374
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Hauser,M.A., Horrigan,S.K., Salmikangas,P., Torian,U.M.,
            Viles,K.D., Dancel,R., Tim,R.W., Taivainen,A., Bartoloni,L.,
            Gilchrist,J.M., Stajich,J.M., Gaskell,P.C., Gilbert,J.R.,
            Vance,J.M., Pericak-Vance,M.A., Carpen,O., Westbrook,C.A. and
            Speer,M.C.
  TITLE     Myotilin is mutated in limb girdle muscular dystrophy 1A
  JOURNAL   Hum Mol Genet 9 (14), 2141-2147 (2000)
   PUBMED   10958653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254729.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.56275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..497
                     /product="myotilin isoform 2"
                     /note="titin immunoglobulin domain protein (myotilin)"
                     /calculated_mol_wt=55120
     Region          249..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409405"
     Region          279..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409405"
     Region          305..309
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409405"
     Region          319..324
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409405"
     Region          332..335
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409405"
     Region          348..439
                     /region_name="IgI_Myotilin_C"
                     /note="C-terminal immunoglobulin (Ig)-like domain of
                     myotilin; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05892"
                     /db_xref="CDD:409473"
     Region          348..351
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409473"
     Region          354..359
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409473"
     Region          364..371
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409473"
     Region          378..384
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409473"
     Region          385..388
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409473"
     Region          395..401
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409473"
     Region          404..414
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409473"
     Region          418..426
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409473"
     Region          428..439
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409473"
     CDS             1..497
                     /gene="Myot"
                     /gene_synonym="Ttid"
                     /coded_by="NM_001437405.1:271..1764"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:291605"
                     /db_xref="RGD:1310569"
ORIGIN      
        1 mfnyerpkhf iqsqnpcgsg lqppgpevss fpnqtkqssi viqprqcteq rfsasstvss
       61 hitvsssayp asqqlagpnp gqkvtatynq spasflssil psqpdysnsk ipstvdsnyq
      121 qssvhqpvna vssqaagakp tprtpdheiq gskealiqdl erklkckdtl lhngnqrlty
      181 eekmarrllg pqnaaavfqa qnsdvqdssq qhnpeharlq vptsqvrsrs ssradandqd
      241 aiqekfyppr fiqvpenmsi eegrfcrmdf kvsglpapdv swylngrlvq sdelhkmivs
      301 ekgfhslife vvrasdagpy acvarnrage atftvqldvl akehkrapmf iykpqskkvf
      361 egesvklecq isaipppklf wkrnnemvqf ntdrislyhd nagrvtllik dvnkkdagwy
      421 tvsavneagv ttcntrldvt arpnqtppap kqlrvrptfs kylalngkgl dvkqafnpeg
      481 efqrlaaqsg lyeseel
//
LOCUS       NP_001071135             270 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 68 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001071135 XP_001068607 XP_225849
VERSION     NP_001071135.1
DBSOURCE    REFSEQ: accession NM_001077667.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_225849.4, XP_001068607.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..270
                     /product="coiled-coil domain-containing protein 68 isoform
                     1"
                     /note="CTCL tumor antigen se57-1; coiled-coil
                     domain-containing protein 68"
                     /calculated_mol_wt=30769
     Region          85..>235
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..270
                     /gene="Ccdc68"
                     /gene_synonym="RGD1561424"
                     /coded_by="NM_001077667.2:152..964"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:291530"
                     /db_xref="RGD:1561424"
ORIGIN      
        1 mttvtvtmev psggktedrs ifsgpssaqi ieeteyvrki rttlekirnr mfkeedgrgn
       61 arhkvdaeqs gnvqngldst tdptrldlll esmrrkdqql lemnkenevl qikleasrea
      121 gaaalrnaaq rlfdnyqtqs edlekkhkds khvlqvnkle keqtlkqrak nlsqlseklg
      181 ekheqivgle nrvqrmenme glkntlkeqd kkienlkekv tvleaqneel ktkvahwtes
      241 prtsvskavs tselktegas pylmlirlrk
//
LOCUS       NP_001424330             445 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424330 XP_038952631
VERSION     NP_001424330.1
DBSOURCE    REFSEQ: accession NM_001437401.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952631.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77201.1,
                                           SRR26360181.297594.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..445
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 5"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=50615
     Region          <2..96
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          75..123
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          147..210
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          232..435
                     /region_name="SPRY_PRY_TRIM36"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 36 (TRIM36); cd12894"
                     /db_xref="CDD:293951"
     CDS             1..445
                     /gene="Trim36"
                     /coded_by="NM_001437401.1:141..1478"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 mketecnger akeealahfe klfeiledrk ssvlkaidas kklrldkfht qmeeyqglle
       61 nnglvgyaqe vlketdqscf vqtakqlhlr iqkateslks frpaaqasfe dyvvniskqt
      121 evlgelsffs sgidipeine eqskvynnal idwhhpekdk adsyvleyrk inrdeemisw
      181 neievhgtsk vvsnlesnsp yafrvrayrg sicspcsrel vlhtppapvf sflfdekcgy
      241 ntehlllnlk rdrvesragf nvllaaeriq vghytsldyi igdvgitkgk hfwacrvepy
      301 sylvkvgvas sdklqewlrs prdaasprye qdsghdsgse dayfdssqpf tlvtigmkkf
      361 fipksptssn epenrvlpmp tsigifldcd kgkvsfydmd hmkclyerqv dcshtmypaf
      421 almgsggiql eetitakyle yeedv
//
LOCUS       NP_001424232              74 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424232
VERSION     NP_001424232.1
DBSOURCE    REFSEQ: accession NM_001437303.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1175280.1,
                                           SRR26360176.372334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..74
                     /product="mitochondrial ribosomal protein S6 isoform 5"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=7698
     Region          <1..>32
                     /region_name="bS6"
                     /note="Bacterial ribosomal protein S6; cl00414"
                     /db_xref="CDD:469763"
     CDS             1..74
                     /gene="Mrps6"
                     /coded_by="NM_001437303.1:189..413"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggdsartsl fvgeglmesh iaegatgggv
       61 lstlskkgeh lpea
//
LOCUS       NP_001424245             910 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF216 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424245 XP_038945294
VERSION     NP_001424245.1
DBSOURCE    REFSEQ: accession NM_001437316.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Chen,T., Zhu,J. and Wang,Y.H.
  TITLE     RNF216 mediates neuronal injury following experimental subarachnoid
            hemorrhage through the Arc/Arg3.1-AMPAR pathway
  JOURNAL   FASEB J 34 (11), 15080-15092 (2020)
   PUBMED   32918771
  REMARK    GeneRIF: RNF216 mediates neuronal injury following experimental
            subarachnoid hemorrhage through the Arc/Arg3.1-AMPAR pathway.
            Erratum:[FASEB J. 2024 May 15;38(9):e23652. doi:
            10.1096/fj.202400924. PMID: 38708783]
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Mabb,A.M., Je,H.S., Wall,M.J., Robinson,C.G., Larsen,R.S.,
            Qiang,Y., Correa,S.A. and Ehlers,M.D.
  TITLE     Triad3A regulates synaptic strength by ubiquitination of Arc
  JOURNAL   Neuron 82 (6), 1299-1316 (2014)
   PUBMED   24945773
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Nakhaei,P., Mesplede,T., Solis,M., Sun,Q., Zhao,T., Yang,L.,
            Chuang,T.H., Ware,C.F., Lin,R. and Hiscott,J.
  TITLE     The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
            signaling pathway by targeting TRAF3 for degradation
  JOURNAL   PLoS Pathog 5 (11), e1000650 (2009)
   PUBMED   19893624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038945294.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2021162.1,
                                           SRR26643293.83815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..910
                     /product="E3 ubiquitin-protein ligase RNF216 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF216"
                     /calculated_mol_wt=104014
     Region          558..614
                     /region_name="RING-HC_RBR_RNF216"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 216 (RNF216) and similar proteins; cd16630"
                     /db_xref="CDD:438292"
     Region          647..698
                     /region_name="BRcat_RBR_RNF216"
                     /note="BRcat domain found in RING finger protein 216
                     (RNF216); cd20339"
                     /db_xref="CDD:439000"
     Region          709..765
                     /region_name="Rcat_RBR_RNF216"
                     /note="Rcat domain found in RING finger protein 216
                     (RNF216); cd20353"
                     /db_xref="CDD:439014"
     CDS             1..910
                     /gene="Rnf216"
                     /gene_synonym="RGD1565135"
                     /coded_by="NM_001437316.1:210..2942"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:304294"
                     /db_xref="RGD:1565135"
ORIGIN      
        1 maegnnqeev ihlnnfhchr gkewmavreg pitisdssde egipmlvtpa teqqeddldd
       61 dviltethkp qtsrpnlikp aaewqdlnrl geerprksra dfeadthsyf sfcnnslfds
      121 gaqddsedec ggfldlktek kggeakpgps nkqtadntvs prleqkviil gengllfses
      181 eplevqnqls edsetdllsn pgepaasvde qlieeeywld hpyfqalnpq pqertnqlvp
      241 qerhsesemg pmffrhdfpe pafprpepqq egipgpaspq pahplgeled qqlaidedpg
      301 payplpgpqe anlanvwgqe aaegdqelip llvketearf pdvangyvee iihlknyydl
      361 nvlcnfllen pdypkredri lihpssslla sqddvklpki dffdyskltp ldqrcfiqaa
      421 dllmadfkml ssqdikwalh elkghyaitr kafsdaikkw qelspetsgk rkkrkemnqy
      481 sfidfkfeqg nikiekrmff lenkrrhcrs ydqqallpav qqeqefyeqk ikemaehedf
      541 llalqmneeq yqkdgqliec rccygefpfe eltqcadahl fckeclirya qeavfgsgks
      601 elscmegsct csfptselek vlpqtilyky yerkaeeeva aayadelvrc pscsfpalld
      661 sdvkrfscpn prcrketcrk cqglwkehng ltceelaekd dikyrtsiee kmtaarirkc
      721 hkcgtgliks egcnrmscrc gaqmcylcrv singydhfcq hprspgapcq ecsrcslwtd
      781 pteddeklie eiqkeaeeeq krkngentfk rigpplekpa ekvqrvealp rpvpqnlhpq
      841 mppyafvhpp fplppvrpvf nnfpinmgpv papyvpplpn vrvnfdfghv hvplehnlpm
      901 hfgpqprhrf
//
LOCUS       NP_001424159             268 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein C9orf153 homolog isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424159 XP_063132078
VERSION     NP_001424159.1
DBSOURCE    REFSEQ: accession NM_001437230.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063132078.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.70561.1,
                                           SRR26360181.1898673.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..268
                     /product="uncharacterized protein C9orf153 homolog isoform
                     1"
                     /note="uncharacterized protein C9orf153 homolog"
                     /calculated_mol_wt=30879
     Region          1..92
                     /region_name="DUF5532"
                     /note="Family of unknown function (DUF5532); pfam17673"
                     /db_xref="CDD:465450"
     CDS             1..268
                     /gene="C17h9orf153"
                     /coded_by="NM_001437230.1:233..1039"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100912252"
                     /db_xref="RGD:6488044"
ORIGIN      
        1 msstrhhtwt rgsigslylh rcslpelyas leifnkeskk snlqkicgms fkeaqevlwk
       61 ilgglisdsy dtvkgderhp sipvnkeerk tpsmsdllhq sllkgynvpl eqvhssqqrl
      121 aqvgippppl sfphglsnel pvilpaqhfr kriqsvtfrk lllssvapgr lfyeekptsq
      181 qvsfdpgkqf ldladlqwry fkglakwgkm prrfsllnie ynsekryven qrmsglifpp
      241 lvrktlmvyp qaeydkegql yltwkivy
//
LOCUS       NP_001424353             614 aa            linear   ROD 03-APR-2025
DEFINITION  inactive serine/threonine-protein kinase PLK5 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424353 XP_006240983
VERSION     NP_001424353.1
DBSOURCE    REFSEQ: accession NM_001437424.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   de Carcer,G., Escobar,B., Higuero,A.M., Garcia,L., Anson,A.,
            Perez,G., Mollejo,M., Manning,G., Melendez,B., Abad-Rodriguez,J.
            and Malumbres,M.
  TITLE     Plk5, a polo box domain-only protein with specific roles in neuron
            differentiation and glioblastoma suppression
  JOURNAL   Mol Cell Biol 31 (6), 1225-1239 (2011)
   PUBMED   21245385
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Andrysik,Z., Bernstein,W.Z., Deng,L., Myer,D.L., Li,Y.Q.,
            Tischfield,J.A., Stambrook,P.J. and Bahassi el,M.
  TITLE     The novel mouse Polo-like kinase 5 responds to DNA damage and
            localizes in the nucleolus
  JOURNAL   Nucleic Acids Res 38 (9), 2931-2943 (2010)
   PUBMED   20100802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006240983.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38032.1,
                                           SRR26643292.28401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..614
                     /product="inactive serine/threonine-protein kinase PLK5
                     isoform 1"
                     /EC_number="2.7.11.21"
                     /note="polo-like kinase 5 pseudogene;
                     serine/threonine-protein kinase PLK5; inactive
                     serine/threonine-protein kinase PLK5"
                     /calculated_mol_wt=67769
     Region          25..279
                     /region_name="STKc_PLK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Polo-like kinases; cd14099"
                     /db_xref="CDD:271001"
     Site            order(33..37,41,54,56,88,104..107,111,113,150,152,
                     154..155,157,168,171,187..190)
                     /site_type="active"
                     /db_xref="CDD:271001"
     Site            order(33..37,41,54,56,88,105..107,157,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271001"
     Site            order(37,111,113,150,152,154,171,187..190)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271001"
     Site            order(167..175,180..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271001"
     Region          429..516
                     /region_name="POLO_box_1"
                     /note="First polo-box domain (PBD) of polo-like kinases
                     Plk1, Plk2, Plk3, and Plk5; cd13118"
                     /db_xref="CDD:240561"
     Site            order(435..438,507,509..513)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:240561"
     CDS             1..614
                     /gene="Plk5"
                     /gene_synonym="Plk5p"
                     /coded_by="NM_001437424.1:79..1923"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314627"
                     /db_xref="RGD:1305038"
ORIGIN      
        1 meprlrrrrs rqlvatflrd pgsgrvyrrg kligkgafsr cykltdmsts avfalkvvpr
       61 ggagrlrlrg kvereialhs rlhhrnivaf hahfadrdhv ymvleycsrq slahvlkvrr
      121 tltepevryy frglvsglry lhqqrivhrd lkpsnfflnk nmevkigdlg laarvgpagr
      181 chrvlcgtpn fqapevvsrn ghsaksdiwa lgcimytvlt gtppfaaapl semyqnirdg
      241 hyleptqlsp sarsliarll apdpderpsl dhllqddffs qgftperlpp hschsppvfa
      301 fppplgrlfr kvgqllltqc rppcpftske asgpgeeste pdhmeasnee gaplctesri
      361 hlltlgtprt dpadakgtla lqlevatrkl clcldagpvg rtatpkcrte aawrgpkpag
      421 qdppgeqrsv lwapkwvdys lkygfgyqls dggsgvlfrd gshmalrppg ghvsyqpdqg
      481 tlwifalrdv pgplraklav lrlfacymqr rlreegtapm tatpaspdfc llsftadaqa
      541 lamlfsngtv qvssktspvq lvlsgegedf lltiqepggp smgtsytldv lrshgislav
      601 rhhlrlglhl lqsv
//
LOCUS       NP_001424263            1335 aa            linear   ROD 03-APR-2025
DEFINITION  membrane-associated phosphatidylinositol transfer protein 2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001424263 XP_063127373
VERSION     NP_001424263.1
DBSOURCE    REFSEQ: accession NM_001437334.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1335)
  AUTHORS   Lu,C., Vihtelic,T.S., Hyde,D.R. and Li,T.
  TITLE     A neuronal-specific mammalian homolog of the Drosophila retinal
            degeneration B gene with expression restricted to the retina and
            dentate gyrus
  JOURNAL   J Neurosci 19 (17), 7317-7325 (1999)
   PUBMED   10460238
REFERENCE   2  (residues 1 to 1335)
  AUTHORS   Lev,S., Hernandez,J., Martinez,R., Chen,A., Plowman,G. and
            Schlessinger,J.
  TITLE     Identification of a novel family of targets of PYK2 related to
            Drosophila retinal degeneration B (rdgB) protein
  JOURNAL   Mol Cell Biol 19 (3), 2278-2288 (1999)
   PUBMED   10022914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127373.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1335
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..1335
                     /product="membrane-associated phosphatidylinositol
                     transfer protein 2 isoform 1"
                     /note="membrane-associated phosphatidylinositol transfer
                     protein 2"
                     /calculated_mol_wt=148181
     Region          1..258
                     /region_name="SRPBCC_PITPNM1-2_like"
                     /note="Lipid-binding SRPBCC domain of mammalian PITPNM1-2
                     and related proteins (Class IIA PITPs); cd08889"
                     /db_xref="CDD:176898"
     Site            order(21..22,25,29,32,40,59,61,63,65,68,70,73,77,81..82,
                     84,86,88,90,95,97,99,102..103,109,111,192,198,200,210,
                     218..220,223)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176898"
     Site            65..83
                     /site_type="active"
                     /note="putative lipid exchange loop [active]"
                     /db_xref="CDD:176898"
     Site            order(118..147,153..177,186..187)
                     /site_type="active"
                     /note="putatative regulatory loop [active]"
                     /db_xref="CDD:176898"
     Site            164
                     /site_type="other"
                     /note="putative PKC phosphorylation site
                     [posttranslational modification]"
                     /db_xref="CDD:176898"
     Region          701..948
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     Region          1094..1225
                     /region_name="LNS2"
                     /note="This domain is found in Saccharomyces cerevisiae
                     protein SMP2, proteins with an N-terminal lipin domain and
                     phosphatidylinositol transfer proteins; smart00775"
                     /db_xref="CDD:197870"
     CDS             1..1335
                     /gene="Pitpnm2"
                     /coded_by="NM_001437334.1:341..4348"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304474"
                     /db_xref="RGD:1310867"
ORIGIN      
        1 miikeyripl pmtveeyria qlymiqkksr netygqgsgv eilenrpytd gpggsgqyth
       61 kvyhvgmhip gwfrsilpka alrvveeswn aypytrtrft cpfvekfsid ietfyktdtg
      121 ennnvfnlsp veknqlitdi idivkdpvtp seykteedpk lfqsiktrrg plsenwiqey
      181 kkrllpimca yklckvefry wgmqskierf ihdtglrrvm vrahrqawcw qdewygltme
      241 kirelekevq lmlsrkmaqf seegpselsk estikdqatg atpepsssng eslgrglkkq
      301 wstsskssrs skrgaspsrh sisewrmqsi ardsdessee effdaqenlq hkeemytkdi
      361 tkwssndlmd kmenpepees qdslyhqsgs efrvassveq lntiedevsq platppskih
      421 vlllvlhggt ildtgagdps skqgdtntit nvfdtvmrvh ypsalghlai rlvpcppica
      481 dafalvsnls pyghdegcls ssqdhiplaa lpllatsspq yqeavatviq ranlaygdfi
      541 ksqegvtfng qvcligdcvg gilafdalcy sgqpvsesqs ssrrgsvvsm qdadllspgi
      601 lvnaahcsgg sgggsgggss lessrhlsrs nidiprsngt edsrkqmprk rsdsstyeld
      661 tiqqhqafls slhasvlrne pssrrsssst mldgagalgk fdfeiadlfl fgcplglvla
      721 lrktvipsld vfqlrpacqq vynlfhpadp sasrleplle rrfhtlppfn ipryqryplg
      781 dgcstllada lqthntvfqe haapsspgta pasrgfrras eisiasqvsg maesytasgi
      841 aqkgpsslnh tpsirrlsll alpppspttq gprararqvs pnlergpclp dldigevaak
      901 wwgqkridya lycpdalmaf ptvalphlfh asywestdvv sfllrqvmrh dsasileldg
      961 kevsvftpsq prekwqrkrt hvklrnvaan hrindavane dgpqvvtgrf mygpldmvtl
     1021 tgekvdvhim tqppsgewly ldtlvtnssg rvsytipeth rlgvgvypik mvvrgdhtfa
     1081 dsyitvlpkg tefvvfsidg sfaasvsimg sdpkvragav dvvrhwqdlg yliiyvtgrp
     1141 dmqkqrvvaw laqhnfphgv vsfcdglvhd plrhkanflk lliselhlra haaygstkdv
     1201 avynsislsp mhiyivgrpt kklqqqcqfi tdgyaahlaq lkynhrarpa rntatrmalr
     1261 kgsfglpgqg dflrsrnhll rtisaqpsgp shrhdrtqtq mdleqrgqrs msmaascwgr
     1321 amagrlepga atgpk
//
LOCUS       NP_001424254             768 aa            linear   ROD 03-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 2 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001424254 XP_063133437
VERSION     NP_001424254.1
DBSOURCE    REFSEQ: accession NM_001437325.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Cruz-Garcia,D., Vazquez-Martinez,R., Peinado,J.R., Anouar,Y.,
            Tonon,M.C., Vaudry,H., Castano,J.P. and Malagon,M.M.
  TITLE     Identification and characterization of two novel (neuro)endocrine
            long coiled-coil proteins
  JOURNAL   FEBS Lett 581 (17), 3149-3156 (2007)
   PUBMED   17572408
  REMARK    GeneRIF: NECC 1 & 2 proteins primarily expressed in
            (neuro)endocrine tissues in vertebrates thus supporting a role for
            these proteins in the regulated secretory pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133437.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2139602.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..768
                     /product="janus kinase and microtubule-interacting protein
                     2 isoform 2"
                     /calculated_mol_wt=89885
     Region          <2..746
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          367..539
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     CDS             1..768
                     /gene="Jakmip2"
                     /gene_synonym="RGD1559742"
                     /coded_by="NM_001437325.1:343..2649"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307479"
                     /db_xref="RGD:1559742"
ORIGIN      
        1 mvsklerekt qeakrirele qrkhtvlvte lkaklheekm kelqavrenl ikqheqemsr
       61 tvkvrdgeiq rlksalcalr dgssdkvrta ltieareear kqfdaerlkl lqeitdlkta
      121 kkqvdealsn miqadkikag dlrsehqshq eaiskikwes erdirrlmde ikakdriifs
      181 lekeletqtg yvqklqlqke aldeqlflvk eaecnmsspk reipgragdg sehcsspdlr
      241 rnqkriaeln atirkledrn tllgdernel lkrvretekq ckpllernkc lakrndelmv
      301 slqrmeeklk aitkensemr ekitshpplk klkslndldq aneeqetefl klqvieqqni
      361 ideltrdrek lirrrkhrrs skpikrpvld pfigydedsm dsetssmtsf rtdrtpatpd
      421 ddldeslaae eselrfrqlt keyqalqray allqeqtggi idaereakaq eqlqaevlry
      481 rakiedleat laqkgqiekq eaenhrlqqe lqdardqnel lefrnlelee rerrsppfnl
      541 qihpfsdgvs alqiycmkeg vkdvnipdli kqldilgdng nlrneeqvai iqastvlsla
      601 ekwiqqiega eaalhqkmme lesdmeqfck ikgyleeeld yrkqaldqay mriqeleatl
      661 ynalqqetvi kfgellsdkq qeelrtavek lrrqmlrksr eydcqilqer mellqqahqr
      721 irdledktdi qkrqikdlee kknqelgsyp kkanafkpsk maklftpm
//
LOCUS       NP_001424150             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424150 XP_006249179
VERSION     NP_001424150.1
DBSOURCE    REFSEQ: accession NM_001437221.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249179.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.34967.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437221.1:152..2548"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424340             407 aa            linear   ROD 03-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424340 XP_063141632
VERSION     NP_001424340.1
DBSOURCE    REFSEQ: accession NM_001437411.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063141632.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.78666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..407
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 1"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=44228
     Region          1..150
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..407
                     /gene="Xndc1"
                     /coded_by="NM_001437411.1:393..1616"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 mapvkishvv sfssqdpkyp venllnpdsh kgpwlscprd ktgqlkvefq leravpisyi
       61 dvgncgcafl qidvgrsswp ldrpfvtllp atmlmsltds kegknrsgvr mfkdddflip
      121 asgeswdrlr ltcsqpftrh qsfglaflrv rssldslsdp vkdpsspgss glnqnssdkl
      181 esdpspwltn psirrtffpd pqtstkeisa lkgmlkqlqp gplgraarmv lsaahkappa
      241 svvspnnshg epdsshpera epraeepnrk nnasrgkrrk vqeqrrplss sssqpnrrat
      301 grtkqrqqrp qaksdgsgvq atgqcpictg sfsiealprh aatcgesspp qpasptslss
      361 sesvlwvssp esspppsswv qcpicelqfs areieehasv cgevfpa
//
LOCUS       NP_001424230              96 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424230
VERSION     NP_001424230.1
DBSOURCE    REFSEQ: accession NM_001437301.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.68572.1,
                                           SRR26360181.695046.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..96
                     /product="mitochondrial ribosomal protein S6 isoform 4"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=10885
     Region          <1..67
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(16,18..20,34,36,61,65)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     Site            order(20,24,43,46..47,54,61,64..66)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     CDS             1..96
                     /gene="Mrps6"
                     /coded_by="NM_001437301.1:406..696"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggyflvdfy aptnavesml ehlardtdvv
       61 rpnivkhplt qevkecdgiv pvpleeklys tkrrkk
//
LOCUS       NP_001424200             624 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CHFR isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424200 XP_006249598
VERSION     NP_001424200.1
DBSOURCE    REFSEQ: accession NM_001437271.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Perdereau,D., Cailliau,K., Browaeys-Poly,E., Lescuyer,A., Carre,N.,
            Benhamed,F., Goenaga,D. and Burnol,A.F.
  TITLE     Insulin-induced cell division is controlled by the adaptor Grb14 in
            a Chfr-dependent manner
  JOURNAL   Cell Signal 27 (4), 798-806 (2015)
   PUBMED   25578860
  REMARK    GeneRIF: These results show that Chfr and Grb14 collaborate in a
            negative feedback loop controlling insulin-stimulated cell
            division.
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Jung,I., Sohn,D.H., Choi,J., Kim,J.M., Jeon,S., Seol,J.H. and
            Seong,R.H.
  TITLE     SRG3/mBAF155 stabilizes the SWI/SNF-like BAF complex by blocking
            CHFR mediated ubiquitination and degradation of its major
            components
  JOURNAL   Biochem Biophys Res Commun 418 (3), 512-517 (2012)
   PUBMED   22285184
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Oh,Y.M., Kwon,Y.E., Kim,J.M., Bae,S.J., Lee,B.K., Yoo,S.J.,
            Chung,C.H., Deshaies,R.J. and Seol,J.H.
  TITLE     Chfr is linked to tumour metastasis through the downregulation of
            HDAC1
  JOURNAL   Nat Cell Biol 11 (3), 295-302 (2009)
   PUBMED   19182791
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Ahel,I., Ahel,D., Matsusaka,T., Clark,A.J., Pines,J., Boulton,S.J.
            and West,S.C.
  TITLE     Poly(ADP-ribose)-binding zinc finger motifs in DNA
            repair/checkpoint proteins
  JOURNAL   Nature 451 (7174), 81-85 (2008)
   PUBMED   18172500
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Yu,X., Minter-Dykhouse,K., Malureanu,L., Zhao,W.M., Zhang,D.,
            Merkle,C.J., Ward,I.M., Saya,H., Fang,G., van Deursen,J. and
            Chen,J.
  TITLE     Chfr is required for tumor suppression and Aurora A regulation
  JOURNAL   Nat Genet 37 (4), 401-406 (2005)
   PUBMED   15793587
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Daniels,M.J., Marson,A. and Venkitaraman,A.R.
  TITLE     PML bodies control the nuclear dynamics and function of the CHFR
            mitotic checkpoint protein
  JOURNAL   Nat Struct Mol Biol 11 (11), 1114-1121 (2004)
   PUBMED   15467728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249598.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85960.1,
                                           SRR26643296.31404.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..624
                     /product="E3 ubiquitin-protein ligase CHFR isoform 3"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CHFR; checkpoint with
                     forkhead and ring finger domains, E3 ubiquitin protein
                     ligase"
                     /calculated_mol_wt=69450
     Region          15..124
                     /region_name="FHA_CHFR"
                     /note="forkhead associated (FHA) domain found in
                     checkpoint with forkhead and RING finger domains protein
                     (CHFR); cd22672"
                     /db_xref="CDD:438724"
     Site            order(15..22,40,48,50,53,55..56,60..61,72..78,80..92,
                     95..98,101..108,116..124)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438724"
     Region          39..>252
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Site            order(41..43,57..58,60,78..81)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438724"
     Region          299..352
                     /region_name="RING-HC_CHFR"
                     /note="RING finger, HC subclass, found in checkpoint with
                     forkhead and RING finger domains protein (CHFR); cd16503"
                     /db_xref="CDD:438166"
     Region          <471..580
                     /region_name="zf-CRD"
                     /note="Cysteine rich domain with multizinc binding
                     regions; pfam17979"
                     /db_xref="CDD:465602"
     Region          592..615
                     /region_name="zf-CCHH"
                     /note="PBZ domain; pfam10283"
                     /db_xref="CDD:463043"
     CDS             1..624
                     /gene="Chfr"
                     /coded_by="NM_001437271.1:86..1960"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:288734"
                     /db_xref="RGD:1306360"
ORIGIN      
        1 mephgedeqp pprepwgrll rlgaeedepq illwkrewti grrrgcdlsf psnklvsgdh
       61 cklrvdeksg evtledtstn gtvinklrvv kkqtyplqsg diiylvyrkn epehnvayly
      121 eslngkqslt qesleanken mfhvtkessg pgqgddpqvp llspmaqtcl eepqpststs
      181 dllptastss tepeltsagq khssssgpgt isispkecss lvangelssl ssvfqdneas
      241 fsllktedte elepakkkmk gdgeldlnlq lsvadqrgia qtssedvkda svkpdkmeet
      301 ltciicqdll hdcvslqpcm htfcaacysg wmersslcpt crcpverick nhilnnlvea
      361 yllqhpdksr seedvrsmda rnkitqdmlq pkvrrsfsde egssedllel sdvdsessdi
      421 sqpyivcrqc peyrrqavqs lpcpvpesel gatqalggea pstsaslttg avclqpfchl
      481 ywgctrtgcf gclapfceln lgdkcldgvl nnnnyesdil knylttrglt wknmltesll
      541 alqrgvfils dyritgntvl cyccglrsfr eltyqyrqni paselpvtvt srpdcywgrn
      601 crtqvkahha mkfnhiceqt rfkn
//
LOCUS       NP_001358562             904 aa            linear   ROD 03-APR-2025
DEFINITION  sarcalumenin isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001358562 XP_003750819
VERSION     NP_001358562.1
DBSOURCE    REFSEQ: accession NM_001371633.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Zhao,X., Yoshida,M., Brotto,L., Takeshima,H., Weisleder,N.,
            Hirata,Y., Nosek,T.M., Ma,J. and Brotto,M.
  TITLE     Enhanced resistance to fatigue and altered calcium handling
            properties of sarcalumenin knockout mice
  JOURNAL   Physiol Genomics 23 (1), 72-78 (2005)
   PUBMED   15998745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jul 19, 2019 this sequence version replaced XP_003750819.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.25364.1,
                                           SRR26643295.37071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..904
                     /product="sarcalumenin isoform 1 precursor"
                     /calculated_mol_wt=96274
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2109
     Region          <76..309
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <271..>483
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          490..522
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          526..767
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Site            531..538
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(536..539,621,687,689,723..725)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Site            562
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            566..568
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Site            621..624
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(623..624,650..651)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Site            686..689
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Site            723..725
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     CDS             1..904
                     /gene="Srl"
                     /coded_by="NM_001371633.2:11..2725"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:302948"
                     /db_xref="RGD:1306564"
ORIGIN      
        1 mkallllccf laslllsgqa elqvsasggt edvgnllenh fsagdaslee keralyadaa
       61 pgdknlllhy pdgreaesfe qppagapsta ngqgseseas lsnssaaesa ppgdvegpge
      121 eeegphaagt lppggaegpe erpefssgee agqeeagvgl ptegaanmea eaqeelqgrl
      181 gdgpmeeaaa gaaepvapqs tegeeaegeg sigsdhqste ldgaqdaipa gedsdadvaa
      241 eareeaedqp edhslpseda appgpdhqpt dphavsdmas sevgaeedae dskaevdaet
      301 geeaedqgep rpsleagsar easeksedtq ssevretegq asgmseedla easseeegge
      361 edgrengglp skeesgedsg dgasseeegs tsgeaaepqk tpratgheee gaqldvedln
      421 tgsegvktqd teaeaseerq qgrgnpviah qeeaedvsee apmrdrshie ktlmlnedkp
      481 addysavlqr lrkiyhtsik pleqsykyne lrqheitdge itskpmvlfl gpwsvgkstm
      541 inyllgledt ryqlytgaep ttseftvlmh gpklktiegi vmaadsarsf splekfgqnf
      601 lekligievp hkllervtfv dtpgiienrk qqergypfnd vcqwfidrad lifvvfdptk
      661 ldvgleleml frqlkgresq iriilnkadn latqmlmrvy galfwslapl invtepprvy
      721 vssfwpqdyk pdthrdlflk eeislledln qvienrlenk iafirqhair vrihallvdr
      781 ylqtykdkmt ffsdgelvfk divedpdkfy ifktilaktn vskfdlpnre aykdffginp
      841 isnfkllsqq csymggcfle kieraitqel psllgsiglg knpgapncdk tgcgetpknr
      901 ykkh
//
LOCUS       NP_001424251             485 aa            linear   ROD 03-APR-2025
DEFINITION  sarcalumenin isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001424251 XP_063124971
VERSION     NP_001424251.1
DBSOURCE    REFSEQ: accession NM_001437322.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Zhao,X., Yoshida,M., Brotto,L., Takeshima,H., Weisleder,N.,
            Hirata,Y., Nosek,T.M., Ma,J. and Brotto,M.
  TITLE     Enhanced resistance to fatigue and altered calcium handling
            properties of sarcalumenin knockout mice
  JOURNAL   Physiol Genomics 23 (1), 72-78 (2005)
   PUBMED   15998745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063124971.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.25368.1,
                                           SRR26643295.37073.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..485
                     /product="sarcalumenin isoform 3 precursor"
                     /calculated_mol_wt=53566
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2109
     Region          59..86
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          107..348
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Site            112..119
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(117..120,202,268,270,304..306)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Site            143
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            147..149
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Site            202..205
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(204..205,231..232)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Site            267..270
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Site            304..306
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     CDS             1..485
                     /gene="Srl"
                     /coded_by="NM_001437322.1:11..1468"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:302948"
                     /db_xref="RGD:1306564"
ORIGIN      
        1 mkallllccf laslllsgqa eeaedvseea pmrdrshiek tlmlnedkpa ddysavlqrl
       61 rkiyhtsikp leqsykynel rqheitvlgm apralsildg eitskpmvlf lgpwsvgkst
      121 minyllgled tryqlytgae pttseftvlm hgpklktieg ivmaadsars fsplekfgqn
      181 flekligiev phkllervtf vdtpgiienr kqqergypfn dvcqwfidra dlifvvfdpt
      241 kldvglelem lfrqlkgres qiriilnkad nlatqmlmrv ygalfwslap linvtepprv
      301 yvssfwpqdy kpdthrdlfl keeislledl nqvienrlen kiafirqhai rvrihallvd
      361 rylqtykdkm tffsdgelvf kdivedpdkf yifktilakt nvskfdlpnr eaykdffgin
      421 pisnfkllsq qcsymggcfl ekieraitqe lpsllgsigl gknpgapncd ktgcgetpkn
      481 rykkh
//
LOCUS       NP_001424161             209 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein C9orf153 homolog isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424161 XP_063132080
VERSION     NP_001424161.1
DBSOURCE    REFSEQ: accession NM_001437232.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063132080.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2238807.1,
                                           SRR26360181.350186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..209
                     /product="uncharacterized protein C9orf153 homolog isoform
                     2"
                     /note="uncharacterized protein C9orf153 homolog"
                     /calculated_mol_wt=23405
     Region          1..92
                     /region_name="DUF5532"
                     /note="Family of unknown function (DUF5532); pfam17673"
                     /db_xref="CDD:465450"
     CDS             1..209
                     /gene="C17h9orf153"
                     /coded_by="NM_001437232.1:276..905"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:100912252"
                     /db_xref="RGD:6488044"
ORIGIN      
        1 msstrhhtwt rgsigslylh rcslpelyas leifnkeskk snlqkicgms fkeaqevlwk
       61 ilgglisdsy dtvkgderhp sipvnkeerk tpsmsdllhq sllkgynvpl eqvhssqqrl
      121 aqvgippppl sfphglsnel pvilpaqhfr kriqsvtfrk lllssvapgr lfyeekptsq
      181 qvsfdpgkqf ldladlqwss qdsdglpss
//
LOCUS       NP_001099617             729 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099617 XP_001053970 XP_225947
VERSION     NP_001099617.1
DBSOURCE    REFSEQ: accession NM_001106147.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225947.4, XP_001053970.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1395623.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..729
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=82741
     Region          28..125
                     /region_name="RING-HC_TRIM36_C-I"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd16756"
                     /db_xref="CDD:438414"
     Region          151..205
                     /region_name="Bbox1_TRIM36_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19848"
                     /db_xref="CDD:380906"
     Region          210..254
                     /region_name="Bbox2_TRIM36_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19778"
                     /db_xref="CDD:380836"
     Region          256..380
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          359..407
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          431..494
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          516..719
                     /region_name="SPRY_PRY_TRIM36"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 36 (TRIM36); cd12894"
                     /db_xref="CDD:293951"
     CDS             1..729
                     /gene="Trim36"
                     /coded_by="NM_001106147.2:243..2432"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 msesgemsef gyimellakg kvtiknieke licpackelf thplilpcqh svchkcvkel
       61 llslddsfnd vasdssnqss prlrltspsm dkidkinrpg wkrnsltprp tmfpcpgceh
      121 dvdlgergvs glfrnftlet iveryrqaar aataimcdlc kpppqestks cmdcsasycn
      181 ecfkiyhpwg tvkaqheyvg pttnfrpkil mcpeheteri nmycelcrrp vchlcklggn
      241 hsnhrvttms sayktlkekl skdidfligk esqvksqise lnllmketec ngerakeeal
      301 ahfeklfeil edrkssvlka idaskklrld kfhtqmeeyq gllennglvg yaqevlketd
      361 qscfvqtakq lhlriqkate slksfrpaaq asfedyvvni skqtevlgel sffssgidip
      421 eineeqskvy nnalidwhhp ekdkadsyvl eyrkinrdee miswneievh gtskvvsnle
      481 snspyafrvr ayrgsicspc srelvlhtpp apvfsflfde kcgyntehll lnlkrdrves
      541 ragfnvllaa eriqvghyts ldyiigdvgi tkgkhfwacr vepysylvkv gvassdklqe
      601 wlrsprdaas pryeqdsghd sgsedayfds sqpftlvtig mkkffipksp tssnepenrv
      661 lpmptsigif ldcdkgkvsf ydmdhmkcly erqvdcshtm ypafalmgsg giqleetita
      721 kyleyeedv
//
LOCUS       NP_001424285             559 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424285 XP_063127387
VERSION     NP_001424285.1
DBSOURCE    REFSEQ: accession NM_001437356.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127387.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.262635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..559
                     /product="coiled-coil domain-containing protein 63 isoform
                     1"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65977
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..559
                     /gene="Ccdc63"
                     /coded_by="NM_001437356.1:251..1930"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eevphralsw vqwntlwttv asgswswrtt
      541 frrneeknhr rhcwrrgtr
//
LOCUS       NP_001424258             419 aa            linear   ROD 03-APR-2025
DEFINITION  carbohydrate sulfotransferase 12 [Rattus norvegicus].
ACCESSION   NP_001424258 XP_038945315
VERSION     NP_001424258.1
DBSOURCE    REFSEQ: accession NM_001437329.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Prisco,S.Z., Prokop,J.W., Sarkis,A.B., Yeo,N.C., Hoffman,M.J.,
            Hansen,C.C., Jacob,H.J., Flister,M.J. and Lazar,J.
  TITLE     Refined mapping of a hypertension susceptibility locus on rat
            chromosome 12
  JOURNAL   Hypertension 64 (4), 883-890 (2014)
   PUBMED   25001272
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Hiraoka,N., Nakagawa,H., Ong,E., Akama,T.O., Fukuda,M.N. and
            Fukuda,M.
  TITLE     Molecular cloning and expression of two distinct human chondroitin
            4-O-sulfotransferases that belong to the HNK-1 sulfotransferase
            gene family
  JOURNAL   J Biol Chem 275 (26), 20188-20196 (2000)
   PUBMED   10781601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038945315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.1001473.1,
                                           SRR21887622.1001468.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..419
                     /product="carbohydrate sulfotransferase 12"
                     /EC_number="2.8.2.5"
                     /note="carbohydrate (chondroitin 4) sulfotransferase 12"
                     /calculated_mol_wt=49124
     Region          165..411
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     CDS             1..419
                     /gene="Chst12"
                     /coded_by="NM_001437329.1:172..1431"
                     /db_xref="GeneID:304322"
                     /db_xref="RGD:1308214"
ORIGIN      
        1 mtkprlfrlw lalgsalmil liivywdnvg tahfylhtsl srphileplp tqglaeenvl
       61 asdvdefldt llssdakhnd lsrrkteqpp vltpskpvls hmeenvrgyd wsthdaqqnp
      121 drdrqqaerr sllrdfcana slafptkdrs fddipnyeln hlivddrhgv iycyvpkvac
      181 tnwkrvmivl seslldrgsp yrdpldipre hvhntsthlt fnkfwrrygk fsrhlmkvkl
      241 kkytkflfvr dpfvrlisaf rskfelenee fyrkfavpml rlyanhtslp asvseafsag
      301 lkvsfanfiq ylldphtekl apfnehwrqv yrlchpcqid ydfvgkletl dedaaqllrs
      361 lkvdsqlhfp psyrnrtass weedwfanip lawrqqlykl yeadfvlfgy pkpenllrd
//
LOCUS       NP_001424274             111 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein LOC100363294 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424274 XP_063133118
VERSION     NP_001424274.1
DBSOURCE    REFSEQ: accession NM_001437345.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Thelie,A., Pascal,G., Angulo,L., Perreau,C., Papillier,P. and
            Dalbies-Tran,R.
  TITLE     An oocyte-preferential histone mRNA stem-loop-binding protein like
            is expressed in several mammalian species
  JOURNAL   Mol Reprod Dev 79 (6), 380-391 (2012)
   PUBMED   22467188
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133118.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2185532.1,
                                           SRR26360181.1792987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..111
                     /product="uncharacterized protein LOC100363294 isoform 2"
                     /note="stem loop binding protein 2"
                     /calculated_mol_wt=13063
     Region          27..96
                     /region_name="SLBP_RNA_bind"
                     /note="Histone RNA hairpin-binding protein RNA-binding
                     domain; pfam15247"
                     /db_xref="CDD:464587"
     CDS             1..111
                     /gene="Slbpl"
                     /gene_synonym="SLBP2"
                     /coded_by="NM_001437345.1:343..678"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100363294"
                     /db_xref="RGD:2323347"
ORIGIN      
        1 mslssrmemv svgvttepch arwevetdev vlrrrqkqid ygkctpgyqs flqqvpraqr
       61 qpgfhpqtpn knrrysrrsw daqirqwrra lhtwdppsqp lhdrqaeglh t
//
LOCUS       NP_001424178             122 aa            linear   ROD 03-APR-2025
DEFINITION  U7 snRNA-associated Sm-like protein LSm10 [Rattus norvegicus].
ACCESSION   NP_001424178 XP_017449030
VERSION     NP_001424178.1
DBSOURCE    REFSEQ: accession NM_001437249.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Yang,X.C., Torres,M.P., Marzluff,W.F. and Dominski,Z.
  TITLE     Three proteins of the U7-specific Sm ring function as the molecular
            ruler to determine the site of 3'-end processing in mammalian
            histone pre-mRNA
  JOURNAL   Mol Cell Biol 29 (15), 4045-4056 (2009)
   PUBMED   19470752
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Wagner,E.J. and Marzluff,W.F.
  TITLE     ZFP100, a component of the active U7 snRNP limiting for histone
            pre-mRNA processing, is required for entry into S phase
  JOURNAL   Mol Cell Biol 26 (17), 6702-6712 (2006)
   PUBMED   16914750
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Pillai,R.S., Will,C.L., Luhrmann,R., Schumperli,D. and Muller,B.
  TITLE     Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain
            Lsm10, a new 14 kDa Sm D1-like protein
  JOURNAL   EMBO J 20 (19), 5470-5479 (2001)
   PUBMED   11574479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017449030.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.60054.1,
                                           SRR26360176.2439179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..122
                     /product="U7 snRNA-associated Sm-like protein LSm10"
                     /note="U7 snRNP-specific Sm-like protein LSM10"
                     /calculated_mol_wt=13749
     Region          8..85
                     /region_name="LSm10"
                     /note="Like-Sm protein 10; cd01733"
                     /db_xref="CDD:212480"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212480"
     Site            order(47,49,75)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212480"
     Site            71..82
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212480"
     CDS             1..122
                     /gene="Lsm10"
                     /coded_by="NM_001437249.1:379..747"
                     /db_xref="GeneID:366468"
                     /db_xref="RGD:1584914"
ORIGIN      
        1 malshsvker tisensliil lqglqgqitt vdlrdesvar gridnvdafm nirlanvtyt
       61 drwghqveld dlfvtgrnvr yvhipdgvni tatieqqlqi ihrvrnfggk gqgrrefpsk
      121 rp
//
LOCUS       NP_001424287             558 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424287
VERSION     NP_001424287.1
DBSOURCE    REFSEQ: accession NM_001437358.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85238.1,
                                           SRR26360181.1826346.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..558
                     /product="coiled-coil domain-containing protein 63 isoform
                     2"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65522
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..558
                     /gene="Ccdc63"
                     /coded_by="NM_001437358.1:172..1848"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeveypldhs slrqlvleny lqkergkepq
      541 etllekgdei rvkkkvis
//
LOCUS       NP_001424237             581 aa            linear   ROD 03-APR-2025
DEFINITION  protein hinderin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424237 XP_017456501
VERSION     NP_001424237.1
DBSOURCE    REFSEQ: accession NM_001437308.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017456501.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.76441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..581
                     /product="protein hinderin isoform 2"
                     /calculated_mol_wt=66012
     Region          65..388
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     CDS             1..581
                     /gene="Kiaa1328"
                     /gene_synonym="RGD1562608; RGD1564140"
                     /coded_by="NM_001437308.1:39..1784"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:498831"
                     /db_xref="RGD:1562608"
ORIGIN      
        1 mvtgistern trsrlklinp kvdakvkvpk vtdipasmes lkgagdsvae qsfckrglks
       61 aslkdlcved krrianlike larvseekev teerlkteqe sfekkirqle eqneliiker
      121 ealqlqyrec qellslyqky lseqqekltm slselgaara qeqqitkkki thqsslvnld
      181 gsylsvakpq tcqtrarpks enqdsasesh talrnnslkp vtlhhpkqdl ermstetrtc
      241 tyespgrrli naapveealp eelkikdypn llptpssqyc ghkyseseay vhenyhptnm
      301 asqcckthpe scshcrmswa slmhdgvtlq pretdiekql sedrrqqlml qkmeleieke
      361 rlqqllaqqe tklllkqqql hqsrldynwl rtqavfrsre lvadkdfpkp gsdsgpsllk
      421 pkcdgwlrgt sssfrkcpds pnsaqnqkek ktvefqshve ngiqwtcqqn dtcrlqreta
      481 tgvrkdasts pmstqspkhp ltpasssskh ktsryetsll dlvqslspns apkcqphssr
      541 aagtwsalrp tpktstwkkv gthkspedle enqilediff i
//
LOCUS       NP_001424206            1047 aa            linear   ROD 03-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform b [Rattus norvegicus].
ACCESSION   NP_001424206 XP_063144204
VERSION     NP_001424206.1
DBSOURCE    REFSEQ: accession NM_001437277.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063144204.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.30338.1,
                                           SRR21887620.876226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1047
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform b"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=120091
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..281
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          314..481
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          504..687
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          679..1045
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(755,757..759,761,763,780,782,785,816,828..831,836,
                     839,901,903,913..914)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(823..824,925..926,928,930,996,999)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            870
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            893..901
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            914..938
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1047
                     /gene="Pik3cd"
                     /coded_by="NM_001437277.1:317..3460"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse esftfqvstk dmplalmaca lrkkatvfrq plverpeeya
      241 lqvngrheyl ygsyplchfq yicsclhsgl tphltmvhss silamrdeqs npapqvqkpr
      301 vkpppipakk pssvslwsle qpfcielieg rkvnadermk lvvqaglfhg nemlcktvss
      361 sevnvcsepv wkqrlefdis icdlprmarl cfalyavvek akkarstkkk skkadcpiaw
      421 anlmlfdykd qlktgercly mwpsvpdekg elmnpagtvr gnpntesaaa lviylpevap
      481 hpvyfpalek ilelgrhger griteeeqlq lreilerrgs gelyehekdl vwkmrhevqe
      541 hfpealarll lvtkwnkhed vaqlsqmlyl lcswpelpvl salelldfsf pdcyvgsfai
      601 kslrkltdde lfqyllqlvq vlkyesyldc eltkfllgra lanrkighfl fwhlrsemhv
      661 psvalrfgli meaycrgsth hmkvlmkqge alsklkalnd fvkassqktt kpqtkemmhm
      721 cmrqetymea lshlqspldp stlleevcve qctfmdskmk plwimyssek aggagsvgii
      781 fkngddlrqd mltlqmiqlm dflwkqegld lrmtpygclp tgdrtgliev vlhsdtiani
      841 qlnksnmaat aafnkdalln wlksknpgea ldraieeftl scagycvaty vlgigdrhsd
      901 nimiresgql fhidfghflg nfktkfginr ervpfiltyd fvhviqqgkt nnsekferfr
      961 gyceraytil rrhgllflhl falmraaglp elscskdiqy lkdslalgkt eeealkhfrv
     1021 kfnealresw ktkvnwlahn vskdnrq
//
LOCUS       NP_001424271             780 aa            linear   ROD 03-APR-2025
DEFINITION  centrosomal protein of 120 kDa isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424271
VERSION     NP_001424271.1
DBSOURCE    REFSEQ: accession NM_001437342.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Chang,C.W., Hsu,W.B., Tsai,J.J., Tang,C.J. and Tang,T.K.
  TITLE     CEP295 interacts with microtubules and is required for centriole
            elongation
  JOURNAL   J Cell Sci 129 (13), 2501-2513 (2016)
   PUBMED   27185865
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Wu,C., Yang,M., Li,J., Wang,C., Cao,T., Tao,K. and Wang,B.
  TITLE     Talpid3-binding centrosomal protein Cep120 is required for
            centriole duplication and proliferation of cerebellar granule
            neuron progenitors
  JOURNAL   PLoS One 9 (9), e107943 (2014)
   PUBMED   25251415
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Iwakoshi,N.N., Pypaert,M. and Glimcher,L.H.
  TITLE     The transcription factor XBP-1 is essential for the development and
            survival of dendritic cells
  JOURNAL   J Exp Med 204 (10), 2267-2275 (2007)
   PUBMED   17875675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77385.1,
                                           SRR26360181.2462081.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..780
                     /product="centrosomal protein of 120 kDa isoform 2"
                     /note="centrosomal protein 120kDa; coiled-coil domain
                     containing 100; centrosomal protein of 120 kDa"
                     /calculated_mol_wt=89341
     Region          <1..131
                     /region_name="DUF3668"
                     /note="Cep120 protein; pfam12416"
                     /db_xref="CDD:463569"
     Region          <444..>778
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..780
                     /gene="Cep120"
                     /gene_synonym="Ccdc100; RGD1565619"
                     /coded_by="NM_001437342.1:662..3004"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:307302"
                     /db_xref="RGD:1565619"
ORIGIN      
        1 mklperqpef ffyysllgnd vtnepfsdli npnfeperas vrirssvevl rvylalhskl
       61 qihlccgdqs lgsteiplsg llkkgstein qhpvtvegaf tldppnrakq klapvpvela
      121 ptvgvsvalq regigsqsli elktqnghep ehsqkrvltp ikektltgpk sprvspappq
      181 nqtpptkdda teseveslqy dkepkqvvkg tgsipaslaq peatgnpsev vtsgqkiavp
      241 atshhfcfsi dlrsihglei sfpvncilry sypffgsaap imtnppvevr knmevflpqs
      301 ycafdfatmp hqlqdtflri pllvelwhkd kmskdlllgi ariqlsnils sektrflgan
      361 geqcwrqtys ekvpviaaqg snnrivdlsy tmtledyglv kmreifvses sqgmsavgqr
      421 asppppppap cpseiqvepr etleykaale lemwkemqed ifesqlkqke lahmqalaee
      481 wkkrdreres lvkkkvaeys ilegklqqal telesreqql vtaetelqre rkelqlerer
      541 nlqelqdsvr rarddcvhqv elerlklkql eedkhrlqqq lndaenkyki lekdfqqfkd
      601 qqnnkpeirl qseinlltle kvelerkles atksklhykq qwgralkela rlkqreqesq
      661 marlkkqqee leqmrlryla aeekdtvkte qqelldirne lnrlrqqeqk qyqdykeias
      721 gkqgsprgsg leeglddylt rlieerdtlm rtgvynhedr iiseldrqir evltknsasn
//
LOCUS       NP_001424170            1181 aa            linear   ROD 03-APR-2025
DEFINITION  lysine-specific demethylase hairless [Rattus norvegicus].
ACCESSION   NP_001424170
VERSION     NP_001424170.1
DBSOURCE    REFSEQ: accession NM_001437241.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Kuramoto,T., Kuwamura,M., Tagami,F., Mashimo,T., Nose,M. and
            Serikawa,T.
  TITLE     Kyoto rhino rats derived by ENU mutagenesis undergo congenital hair
            loss and exhibit focal glomerulosclerosis
  JOURNAL   Exp Anim 60 (1), 57-63 (2011)
   PUBMED   21325752
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Hsieh,J.C., Slater,S.A., Whitfield,G.K., Dawson,J.L., Hsieh,G.,
            Sheedy,C., Haussler,C.A. and Haussler,M.R.
  TITLE     Analysis of hairless corepressor mutants to characterize molecular
            cooperation with the vitamin D receptor in promoting the mammalian
            hair cycle
  JOURNAL   J Cell Biochem 110 (3), 671-686 (2010)
   PUBMED   20512927
  REMARK    GeneRIF: Hr and VDR interact via multiple protein-protein
            interfaces, catalyzing histone demethylation to effect chromatin
            remodeling and repress the transcription of VDR target genes that
            control the hair cycle.
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Wen,Y., Liu,Y., Xu,Y., Zhao,Y., Hua,R., Wang,K., Sun,M., Li,Y.,
            Yang,S., Zhang,X.J., Kruse,R., Cichon,S., Betz,R.C., Nothen,M.M.,
            van Steensel,M.A., van Geel,M., Steijlen,P.M., Hohl,D., Huber,M.,
            Dunnill,G.S., Kennedy,C., Messenger,A., Munro,C.S., Terrinoni,A.,
            Hovnanian,A., Bodemer,C., de Prost,Y., Paller,A.S., Irvine,A.D.,
            Sinclair,R., Green,J., Shang,D., Liu,Q., Luo,Y., Jiang,L.,
            Chen,H.D., Lo,W.H., McLean,W.H., He,C.D. and Zhang,X.
  TITLE     Loss-of-function mutations of an inhibitory upstream ORF in the
            human hairless transcript cause Marie Unna hereditary hypotrichosis
  JOURNAL   Nat Genet 41 (2), 228-233 (2009)
   PUBMED   19122663
  REMARK    Erratum:[Nat Genet. 2009 Jun;41(6):762]
REFERENCE   4  (residues 1 to 1181)
  AUTHORS   Hsieh,J.C., Sisk,J.M., Jurutka,P.W., Haussler,C.A., Slater,S.A.,
            Haussler,M.R. and Thompson,C.C.
  TITLE     Physical and functional interaction between the vitamin D receptor
            and hairless corepressor, two proteins required for hair cycling
  JOURNAL   J Biol Chem 278 (40), 38665-38674 (2003)
   PUBMED   12847098
REFERENCE   5  (residues 1 to 1181)
  AUTHORS   Fernandez,A., Silio,L., Noguera,J.L., Sanchez,A. and Ovilo,C.
  TITLE     Linkage mapping of the porcine hairless gene (HR) to chromosome 14
  JOURNAL   Anim Genet 34 (4), 317-318 (2003)
   PUBMED   12873232
REFERENCE   6  (residues 1 to 1181)
  AUTHORS   Potter,G.B., Zarach,J.M., Sisk,J.M. and Thompson,C.C.
  TITLE     The thyroid hormone-regulated corepressor hairless associates with
            histone deacetylases in neonatal rat brain
  JOURNAL   Mol Endocrinol 16 (11), 2547-2560 (2002)
   PUBMED   12403844
REFERENCE   7  (residues 1 to 1181)
  AUTHORS   Zlotogorski,A., Ahmad,W. and Christiano,A.M.
  TITLE     Congenital atrichia in five Arab Palestinian families resulting
            from a deletion mutation in the human hairless gene
  JOURNAL   Hum Genet 103 (4), 400-404 (1998)
   PUBMED   9856480
REFERENCE   8  (residues 1 to 1181)
  AUTHORS   Cichon,S., Anker,M., Vogt,I.R., Rohleder,H., Putzstuck,M.,
            Hillmer,A., Farooq,S.A., Al-Dhafri,K.S., Ahmad,M., Haque,S.,
            Rietschel,M., Propping,P., Kruse,R. and Nothen,M.M.
  TITLE     Cloning, genomic organization, alternative transcripts and
            mutational analysis of the gene responsible for autosomal recessive
            universal congenital alopecia
  JOURNAL   Hum Mol Genet 7 (11), 1671-1679 (1998)
   PUBMED   9736769
  REMARK    Erratum:[Hum Mol Genet 1998 Nov;7(12):1987-8]
REFERENCE   9  (residues 1 to 1181)
  AUTHORS   Thompson,C.C. and Bottcher,M.C.
  TITLE     The product of a thyroid hormone-responsive gene interacts with
            thyroid hormone receptors
  JOURNAL   Proc Natl Acad Sci U S A 94 (16), 8527-8532 (1997)
   PUBMED   9238010
REFERENCE   10 (residues 1 to 1181)
  AUTHORS   Thompson,C.C.
  TITLE     Thyroid hormone-responsive genes in developing cerebellum include a
            novel synaptotagmin and a hairless homolog
  JOURNAL   J Neurosci 16 (24), 7832-7840 (1996)
   PUBMED   8987811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            Summary: This gene encodes a protein that is involved in hair
            growth. This protein functions as a transcriptional corepressor of
            multiple nuclear receptors, including thyroid hormone receptor, the
            retinoic acid receptor-related orphan receptors and the vitamin D
            receptors, and it interacts with histone deacetylases. The
            translation of this protein is modulated by a regulatory open
            reading frame (ORF) that exists upstream of the primary ORF.
            Mutations in this upstream ORF cause Marie Unna hereditary
            hypotrichosis (MUHH), an autosomal dominant form of genetic hair
            loss in human. [provided by RefSeq, Oct 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.57889.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p11"
     Protein         1..1181
                     /product="lysine-specific demethylase hairless"
                     /EC_number="1.14.11.65"
                     /note="protein hairless; hairless homolog; hairless
                     protein; hair growth associated; [histone
                     H3]-dimethyl-L-lysine(9) demethylase hairless"
                     /calculated_mol_wt=127233
     Region          311..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          413..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          509..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          560..564
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          696..745
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          752..756
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          <1081..1132
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..1181
                     /gene="Hr"
                     /coded_by="NM_001437241.1:757..4302"
                     /db_xref="GeneID:60563"
                     /db_xref="RGD:620634"
ORIGIN      
        1 mesmpsflkd tpawektapv ngivgqepgt spqdglhhga lclgepvpfw rgvlsapdsw
       61 lppgflqgpk dtlsvvegeg srngerkanw lgskeglrwk eamlahplaf cgpacppryg
      121 plipehssgh pksdpvafrp lhcpflletk ilerapfwvp tclppylmss lppersydwp
      181 lapspwvysg sqpkvpsafs lgskgfyhkd pnilrpakep laasesgmlg lapgghlqqa
      241 cdaegpslhq rdgetgagrq qnlcpvflgy pdtvprtpwp scppglvhtl gnvwagpgsn
      301 sfgyqlgppv tprcpspgpp tppggccssh lparegdpgp crkcqdspeg sssgpgesse
      361 ernkagsras ppshhtklkk twltrhseqf ecpggcpgkg espatglral kragspevqg
      421 argpapkrps htfpgtgrqg arawqetpet stgskaeaqq qeeqrgprdg rirlresrle
      481 dtscqhhlag vtqcpscvqa ageveiltsh sqkshrlple ekpleedsca tseegggssp
      541 easinkglak hllsglgdrl crllrkerea lawaqregqg pamtedspgi phccsrchhg
      601 lfnthwrcsh cshrlcvacg riagagknre ktgsreqrtd dcaqeaghaa csliltqfvs
      661 sqalaelstv mhqvwakfdi rghcfcqvda rvwapgdggq qkeptektpp apqlscngds
      721 nrtkdikeet pdstespaed ragrsplpcp slcellasta vklclgheri hmafapvtpa
      781 lpsddritni ldsiiaqvve rkiqekalgp glragsglrk glslplspvr trlsppgall
      841 wlqeprpkhg frlfqehwrq gqpvlvsgiq ktlrlslwgm ealgtlggqv qtltalgppq
      901 ptsldstafw kgfshpearp kldegsvlll hrplgdkdes rvenlasslp lpeycahqgk
      961 lnlasylplg ltlhplepql waaygvnshr ghlgtknlcv evsdlisilv haeaqlppwy
     1021 raqkdflsgl dgeglwspgs qtstvwhvfr aqdaqrirrf lqmvcpagag tlepgapgsc
     1081 yldsglrrrl reewgvscwt llqapgeavl vpagaphqvq glvstisvtq hflspetsal
     1141 saqlchqgas lppdhrmlya qmdravfqav kvavgtlqea k
//
LOCUS       NP_001424228              96 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424228
VERSION     NP_001424228.1
DBSOURCE    REFSEQ: accession NM_001437299.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.3010172.1,
                                           SRR26360172.2825189.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..96
                     /product="mitochondrial ribosomal protein S6 isoform 4"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=10885
     Region          <1..67
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(16,18..20,34,36,61,65)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     Site            order(20,24,43,46..47,54,61,64..66)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     CDS             1..96
                     /gene="Mrps6"
                     /coded_by="NM_001437299.1:189..479"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggyflvdfy aptnavesml ehlardtdvv
       61 rpnivkhplt qevkecdgiv pvpleeklys tkrrkk
//
LOCUS       NP_001424247             853 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF216 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424247 XP_063127331
VERSION     NP_001424247.1
DBSOURCE    REFSEQ: accession NM_001437318.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Chen,T., Zhu,J. and Wang,Y.H.
  TITLE     RNF216 mediates neuronal injury following experimental subarachnoid
            hemorrhage through the Arc/Arg3.1-AMPAR pathway
  JOURNAL   FASEB J 34 (11), 15080-15092 (2020)
   PUBMED   32918771
  REMARK    GeneRIF: RNF216 mediates neuronal injury following experimental
            subarachnoid hemorrhage through the Arc/Arg3.1-AMPAR pathway.
            Erratum:[FASEB J. 2024 May 15;38(9):e23652. doi:
            10.1096/fj.202400924. PMID: 38708783]
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Mabb,A.M., Je,H.S., Wall,M.J., Robinson,C.G., Larsen,R.S.,
            Qiang,Y., Correa,S.A. and Ehlers,M.D.
  TITLE     Triad3A regulates synaptic strength by ubiquitination of Arc
  JOURNAL   Neuron 82 (6), 1299-1316 (2014)
   PUBMED   24945773
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Nakhaei,P., Mesplede,T., Solis,M., Sun,Q., Zhao,T., Yang,L.,
            Chuang,T.H., Ware,C.F., Lin,R. and Hiscott,J.
  TITLE     The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
            signaling pathway by targeting TRAF3 for degradation
  JOURNAL   PLoS Pathog 5 (11), e1000650 (2009)
   PUBMED   19893624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127331.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.47099.1,
                                           SRR26643291.32028.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..853
                     /product="E3 ubiquitin-protein ligase RNF216 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF216"
                     /calculated_mol_wt=97465
     Region          501..557
                     /region_name="RING-HC_RBR_RNF216"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 216 (RNF216) and similar proteins; cd16630"
                     /db_xref="CDD:438292"
     Region          590..641
                     /region_name="BRcat_RBR_RNF216"
                     /note="BRcat domain found in RING finger protein 216
                     (RNF216); cd20339"
                     /db_xref="CDD:439000"
     Region          652..708
                     /region_name="Rcat_RBR_RNF216"
                     /note="Rcat domain found in RING finger protein 216
                     (RNF216); cd20353"
                     /db_xref="CDD:439014"
     CDS             1..853
                     /gene="Rnf216"
                     /gene_synonym="RGD1565135"
                     /coded_by="NM_001437318.1:161..2722"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:304294"
                     /db_xref="RGD:1565135"
ORIGIN      
        1 maegnnqeev ihlnnfhchr gkewmavreg pitisdssde egipmlvtpa teqqeddldd
       61 dvilteddse decggfldlk tekkggeakp gpsnkqtadn tvsprleqkv iilgengllf
      121 seseplevqn qlsedsetdl lsnpgepaas vdeqlieeey wldhpyfqal npqpqertnq
      181 lvpqerhses emgpmffrhd fpepafprpe pqqegipgpa spqpahplge ledqqlaide
      241 dpgpayplpg pqeanlanvw gqeaaegdqe lipllvkete arfpdvangy veeiihlkny
      301 ydlnvlcnfl lenpdypkre drilihpsss llasqddvkl pkidffdysk ltpldqrcfi
      361 qaadllmadf kmlssqdikw alhelkghya itrkafsdai kkwqelspet sgkrkkrkem
      421 nqysfidfkf eqgnikiekr mfflenkrrh crsydqqall pavqqeqefy eqkikemaeh
      481 edfllalqmn eeqyqkdgql iecrccygef pfeeltqcad ahlfckecli ryaqeavfgs
      541 gkselscmeg sctcsfptse lekvlpqtil ykyyerkaee evaaayadel vrcpscsfpa
      601 lldsdvkrfs cpnprcrket crkcqglwke hngltceela ekddikyrts ieekmtaari
      661 rkchkcgtgl iksegcnrms crcgaqmcyl crvsingydh fcqhprspga pcqecsrcsl
      721 wtdpteddek lieeiqkeae eeqkrkngen tfkrigpple kpaekvqrve alprpvpqnl
      781 hpqmppyafv hppfplppvr pvfnnfpinm gpvpapyvpp lpnvrvnfdf ghvhvplehn
      841 lpmhfgpqpr hrf
//
LOCUS       NP_001424324             333 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 68 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424324 XP_038952586
VERSION     NP_001424324.1
DBSOURCE    REFSEQ: accession NM_001437395.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952586.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.56810.1,
                                           SRR26360190.3140741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..333
                     /product="coiled-coil domain-containing protein 68 isoform
                     3"
                     /note="CTCL tumor antigen se57-1; coiled-coil
                     domain-containing protein 68"
                     /calculated_mol_wt=38099
     Region          <85..>297
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..333
                     /gene="Ccdc68"
                     /gene_synonym="RGD1561424"
                     /coded_by="NM_001437395.1:152..1153"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:291530"
                     /db_xref="RGD:1561424"
ORIGIN      
        1 mttvtvtmev psggktedrs ifsgpssaqi ieeteyvrki rttlekirnr mfkeedgrgn
       61 arhkvdaeqs gnvqngldst tdptrldlll esmrrkdqql lemnkenevl qikleasrea
      121 gaaalrnaaq rlfdnyqtqs edlekkhkds khvlqvnkle keqtlkqrak nlsqlseklg
      181 ekheqivgle nrvqrmenek kallerklcl eskllqlksn aanskscqhl qteisilqeq
      241 ichlqfvihs qhqnlrniiq emeglkntlk eqdkkienlk ekvtvleaqn eelktkvahw
      301 tesprtsvsk avstselkte gaspylmlir lrk
//
LOCUS       NP_001424229              96 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424229
VERSION     NP_001424229.1
DBSOURCE    REFSEQ: accession NM_001437300.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.612492.1,
                                           SRR26643293.68573.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..96
                     /product="mitochondrial ribosomal protein S6 isoform 4"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=10885
     Region          <1..67
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(16,18..20,34,36,61,65)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     Site            order(20,24,43,46..47,54,61,64..66)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     CDS             1..96
                     /gene="Mrps6"
                     /coded_by="NM_001437300.1:571..861"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggyflvdfy aptnavesml ehlardtdvv
       61 rpnivkhplt qevkecdgiv pvpleeklys tkrrkk
//
LOCUS       NP_001424253             820 aa            linear   ROD 03-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 2 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001424253
VERSION     NP_001424253.1
DBSOURCE    REFSEQ: accession NM_001437324.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Cruz-Garcia,D., Vazquez-Martinez,R., Peinado,J.R., Anouar,Y.,
            Tonon,M.C., Vaudry,H., Castano,J.P. and Malagon,M.M.
  TITLE     Identification and characterization of two novel (neuro)endocrine
            long coiled-coil proteins
  JOURNAL   FEBS Lett 581 (17), 3149-3156 (2007)
   PUBMED   17572408
  REMARK    GeneRIF: NECC 1 & 2 proteins primarily expressed in
            (neuro)endocrine tissues in vertebrates thus supporting a role for
            these proteins in the regulated secretory pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1350845.1,
                                           SRR26643298.73922.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..820
                     /product="janus kinase and microtubule-interacting protein
                     2 isoform 1"
                     /calculated_mol_wt=96200
     Region          19..>600
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          409..602
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          478..>804
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..820
                     /gene="Jakmip2"
                     /gene_synonym="RGD1559742"
                     /coded_by="NM_001437324.1:494..2956"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307479"
                     /db_xref="RGD:1559742"
ORIGIN      
        1 mskkgrnkge kpealivalq aanedlrtkl tdiqielhqe kskvsklere ktqeakrire
       61 leqrkhtvlv telkaklhee kmkelqavre nlikqheqem srtvkvrdge iqrlksalca
      121 lrdgssdkvr taltiearee arkqfdaerl kllqeitdlk takkqvdeal snmiqadkik
      181 agdlrsehqs hqeaiskikw eserdirrlm deikakdrii fslekeletq tgyvqklqlq
      241 kealdeqlfl vkeaecnmss pkreipgrag dgsehcsspd lrrnqkriae lnatirkled
      301 rntllgdern ellkrvrete kqckpllern kclakrndel mvslqrmeek lkaitkense
      361 mrekitshpp lkklkslndl dqaneeqete flklqvieqq niideltrdr eklirrrkhr
      421 rsskpikrpv ldpfigyded smdsetssmt sfrtdrtpat pdddldesla aeeselrfrq
      481 ltkeyqalqr ayallqeqtg giidaereak aqeqlqaevl ryrakiedle atlaqkgqds
      541 hwvedkqlfi krnqelleki ekqeaenhrl qqelqdardq nellefrnle leererrspp
      601 fnlqihpfsd gvsalqiycm kegvkdvnip dlikqldilg dngnlrneeq vaiiqastvl
      661 slaekwiqqi egaeaalhqk mmelesdmeq fckikgylee eldyrkqald qaymriqele
      721 atlynalqqe tvikfgells dkqqeelrta veklrrqmlr ksreydcqil qermellqqa
      781 hqrirdledk tdiqkrqikd leekflflfl ffslafilwp
//
LOCUS       NP_001424167             314 aa            linear   ROD 03-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001424167 XP_063127230
VERSION     NP_001424167.1
DBSOURCE    REFSEQ: accession NM_001437238.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127230.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.84525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001437238.1:413..1357"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001424227              96 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424227
VERSION     NP_001424227.1
DBSOURCE    REFSEQ: accession NM_001437298.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.947200.1,
                                           SRR26360190.1534691.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..96
                     /product="mitochondrial ribosomal protein S6 isoform 4"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=10885
     Region          <1..67
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(16,18..20,34,36,61,65)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     Site            order(20,24,43,46..47,54,61,64..66)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     CDS             1..96
                     /gene="Mrps6"
                     /coded_by="NM_001437298.1:123..413"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggyflvdfy aptnavesml ehlardtdvv
       61 rpnivkhplt qevkecdgiv pvpleeklys tkrrkk
//
LOCUS       NP_001389383             268 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein C9orf153 homolog isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001389383 XP_017456171
VERSION     NP_001389383.1
DBSOURCE    REFSEQ: accession NM_001402454.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Mar 14, 2022 this sequence version replaced XP_017456171.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.204017.1,
                                           SRR26360181.2702757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..268
                     /product="uncharacterized protein C9orf153 homolog isoform
                     1"
                     /note="uncharacterized protein C9orf153 homolog"
                     /calculated_mol_wt=30879
     Region          1..92
                     /region_name="DUF5532"
                     /note="Family of unknown function (DUF5532); pfam17673"
                     /db_xref="CDD:465450"
     CDS             1..268
                     /gene="C17h9orf153"
                     /coded_by="NM_001402454.2:276..1082"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:100912252"
                     /db_xref="RGD:6488044"
ORIGIN      
        1 msstrhhtwt rgsigslylh rcslpelyas leifnkeskk snlqkicgms fkeaqevlwk
       61 ilgglisdsy dtvkgderhp sipvnkeerk tpsmsdllhq sllkgynvpl eqvhssqqrl
      121 aqvgippppl sfphglsnel pvilpaqhfr kriqsvtfrk lllssvapgr lfyeekptsq
      181 qvsfdpgkqf ldladlqwry fkglakwgkm prrfsllnie ynsekryven qrmsglifpp
      241 lvrktlmvyp qaeydkegql yltwkivy
//
LOCUS       NP_001424164             314 aa            linear   ROD 03-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001424164 XP_063127233
VERSION     NP_001424164.1
DBSOURCE    REFSEQ: accession NM_001437235.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127233.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.2536092.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001437235.1:408..1352"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001424308             157 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424308 XP_038950769
VERSION     NP_001424308.1
DBSOURCE    REFSEQ: accession NM_001437379.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038950769.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.2154549.1,
                                           SRR26360172.2439696.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..157
                     /product="uncharacterized protein CFAP97D2 isoform 3"
                     /calculated_mol_wt=18682
     Region          28..104
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..157
                     /gene="Cfap97d2"
                     /coded_by="NM_001437379.1:78..551"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkrva
       61 samktgrrid gqnnftwrsl nrksreqalm kvqkqnqavp erlrssepwy gaqrwredwt
      121 amatrpctcr htwrkgadre aqqghsliwm rslkrkg
//
LOCUS       NP_001099393             127 aa            linear   ROD 03-APR-2025
DEFINITION  small ribosomal subunit protein uS17m [Rattus norvegicus].
ACCESSION   NP_001099393 XP_001078418 XP_213762
VERSION     NP_001099393.1
DBSOURCE    REFSEQ: accession NM_001105923.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_213762.4, XP_001078418.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.4039202.1,
                                           SRR26360176.1497545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..127
                     /product="small ribosomal subunit protein uS17m"
                     /note="28S ribosomal protein S17, mitochondrial"
                     /calculated_mol_wt=13868
     Region          11..84
                     /region_name="Ribosomal_uS17"
                     /note="Ribosomal protein uS17; cd00364"
                     /db_xref="CDD:466775"
     CDS             1..127
                     /gene="Mrps17"
                     /coded_by="NM_001105923.2:438..821"
                     /db_xref="GeneID:288621"
                     /db_xref="RGD:1307650"
ORIGIN      
        1 msivrsavha kwvvgkvigt amvktakvra trlvldpyll kyfnkrktyf ahdalqqcsv
       61 gdivllralp vprakhvkhe laeiifkvgr vidpvtgkpc agtaylespl sseatppces
      121 reelkss
//
LOCUS       NP_001424273             687 aa            linear   ROD 03-APR-2025
DEFINITION  centrosomal protein of 120 kDa isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424273 XP_063133374
VERSION     NP_001424273.1
DBSOURCE    REFSEQ: accession NM_001437344.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Chang,C.W., Hsu,W.B., Tsai,J.J., Tang,C.J. and Tang,T.K.
  TITLE     CEP295 interacts with microtubules and is required for centriole
            elongation
  JOURNAL   J Cell Sci 129 (13), 2501-2513 (2016)
   PUBMED   27185865
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Wu,C., Yang,M., Li,J., Wang,C., Cao,T., Tao,K. and Wang,B.
  TITLE     Talpid3-binding centrosomal protein Cep120 is required for
            centriole duplication and proliferation of cerebellar granule
            neuron progenitors
  JOURNAL   PLoS One 9 (9), e107943 (2014)
   PUBMED   25251415
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Iwakoshi,N.N., Pypaert,M. and Glimcher,L.H.
  TITLE     The transcription factor XBP-1 is essential for the development and
            survival of dendritic cells
  JOURNAL   J Exp Med 204 (10), 2267-2275 (2007)
   PUBMED   17875675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133374.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.352627.1,
                                           SRR26643293.77410.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..687
                     /product="centrosomal protein of 120 kDa isoform 3"
                     /note="centrosomal protein 120kDa; coiled-coil domain
                     containing 100; centrosomal protein of 120 kDa"
                     /calculated_mol_wt=76474
     Region          9..114
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          118..340
                     /region_name="DUF3668"
                     /note="Cep120 protein; pfam12416"
                     /db_xref="CDD:463569"
     CDS             1..687
                     /gene="Cep120"
                     /gene_synonym="Ccdc100; RGD1565619"
                     /coded_by="NM_001437344.1:150..2213"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:307302"
                     /db_xref="RGD:1565619"
ORIGIN      
        1 mvpksdqlli vvsilegrhf pkrpkhmlvv eakfdgeqla tdpvdhtdqp efatelawei
       61 drkvlhqhrl qrtpiklqcf aldpqtsake tvgyivldlr taqetkqapk wyqllsnkyt
      121 kfksevqisi tletdtkaqv dsfkakgapp rdgkvpasll gvdpkdivav lneeggyhqi
      181 gpaecctdsf tlsvtiafat qleqlipctm klperqpeff fyysllgndv tnepfsdlin
      241 pnfeperasv rirssvevlr vylalhsklq ihlccgdqsl gsteiplsgl lkkgsteinq
      301 hpvtvegaft ldppnrakqk lapvpvelap tvgvsvalqr egigsqslie lktqnghepe
      361 hsqkrvltpi kektltgpks prvspappqn qtpptkddat eseveslqyd kepkqvvkgt
      421 gsipaslaqp eatgnpsevv tsgqkiavpa tshhfcfsid lrsihgleis fpvncilrys
      481 ypffgsaapi mtnppvevrk nmevflpqsy cafdfatmph qlqdtflrip llvelwhkdk
      541 mskdlllgia riqlsnilss ektrflgang eqcwrqtyse kvpviaaqgs nnrivdlsyt
      601 mtledyglvk mreifvsess qgmsavgqra sppppppapc pseiqvepre tleykaalel
      661 emwkemqedi fesqflrlst mflrfiv
//
LOCUS       NP_001178626             989 aa            linear   ROD 03-APR-2025
DEFINITION  centrosomal protein of 120 kDa isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178626 XP_225760
VERSION     NP_001178626.1
DBSOURCE    REFSEQ: accession NM_001191697.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Chang,C.W., Hsu,W.B., Tsai,J.J., Tang,C.J. and Tang,T.K.
  TITLE     CEP295 interacts with microtubules and is required for centriole
            elongation
  JOURNAL   J Cell Sci 129 (13), 2501-2513 (2016)
   PUBMED   27185865
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Wu,C., Yang,M., Li,J., Wang,C., Cao,T., Tao,K. and Wang,B.
  TITLE     Talpid3-binding centrosomal protein Cep120 is required for
            centriole duplication and proliferation of cerebellar granule
            neuron progenitors
  JOURNAL   PLoS One 9 (9), e107943 (2014)
   PUBMED   25251415
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   5  (residues 1 to 989)
  AUTHORS   Iwakoshi,N.N., Pypaert,M. and Glimcher,L.H.
  TITLE     The transcription factor XBP-1 is essential for the development and
            survival of dendritic cells
  JOURNAL   J Exp Med 204 (10), 2267-2275 (2007)
   PUBMED   17875675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Jul 17, 2010 this sequence version replaced XP_225760.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1949000.1,
                                           SRR26360181.1904640.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..989
                     /product="centrosomal protein of 120 kDa isoform 1"
                     /note="centrosomal protein 120kDa; coiled-coil domain
                     containing 100; centrosomal protein of 120 kDa"
                     /calculated_mol_wt=112690
     Region          9..114
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          118..340
                     /region_name="DUF3668"
                     /note="Cep120 protein; pfam12416"
                     /db_xref="CDD:463569"
     Region          <653..>987
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..989
                     /gene="Cep120"
                     /gene_synonym="Ccdc100; RGD1565619"
                     /coded_by="NM_001191697.2:150..3119"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307302"
                     /db_xref="RGD:1565619"
ORIGIN      
        1 mvpksdqlli vvsilegrhf pkrpkhmlvv eakfdgeqla tdpvdhtdqp efatelawei
       61 drkvlhqhrl qrtpiklqcf aldpqtsake tvgyivldlr taqetkqapk wyqllsnkyt
      121 kfksevqisi tletdtkaqv dsfkakgapp rdgkvpasll gvdpkdivav lneeggyhqi
      181 gpaecctdsf tlsvtiafat qleqlipctm klperqpeff fyysllgndv tnepfsdlin
      241 pnfeperasv rirssvevlr vylalhsklq ihlccgdqsl gsteiplsgl lkkgsteinq
      301 hpvtvegaft ldppnrakqk lapvpvelap tvgvsvalqr egigsqslie lktqnghepe
      361 hsqkrvltpi kektltgpks prvspappqn qtpptkddat eseveslqyd kepkqvvkgt
      421 gsipaslaqp eatgnpsevv tsgqkiavpa tshhfcfsid lrsihgleis fpvncilrys
      481 ypffgsaapi mtnppvevrk nmevflpqsy cafdfatmph qlqdtflrip llvelwhkdk
      541 mskdlllgia riqlsnilss ektrflgang eqcwrqtyse kvpviaaqgs nnrivdlsyt
      601 mtledyglvk mreifvsess qgmsavgqra sppppppapc pseiqvepre tleykaalel
      661 emwkemqedi fesqlkqkel ahmqalaeew kkrdreresl vkkkvaeysi legklqqalt
      721 elesreqqlv taetelqrer kelqlerern lqelqdsvrr arddcvhqve lerlklkqle
      781 edkhrlqqql ndaenkykil ekdfqqfkdq qnnkpeirlq seinlltlek velerklesa
      841 tksklhykqq wgralkelar lkqreqesqm arlkkqqeel eqmrlrylaa eekdtvkteq
      901 qelldirnel nrlrqqeqkq yqdykeiasg kqgsprgsgl eeglddyltr lieerdtlmr
      961 tgvynhedri iseldrqire vltknsasn
//
LOCUS       NP_001424328             618 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424328 XP_063133283
VERSION     NP_001424328.1
DBSOURCE    REFSEQ: accession NM_001437399.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133283.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77209.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..618
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=70282
     Region          <1..14
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          40..94
                     /region_name="Bbox1_TRIM36_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19848"
                     /db_xref="CDD:380906"
     Region          99..143
                     /region_name="Bbox2_TRIM36_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19778"
                     /db_xref="CDD:380836"
     Region          145..269
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          248..296
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          320..383
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          405..608
                     /region_name="SPRY_PRY_TRIM36"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 36 (TRIM36); cd12894"
                     /db_xref="CDD:293951"
     CDS             1..618
                     /gene="Trim36"
                     /coded_by="NM_001437399.1:673..2529"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 mfpcpgcehd vdlgergvsg lfrnftleti veryrqaara ataimcdlck pppqestksc
       61 mdcsasycne cfkiyhpwgt vkaqheyvgp ttnfrpkilm cpeheterin mycelcrrpv
      121 chlcklggnh snhrvttmss ayktlkekls kdidfligke sqvksqisel nllmketecn
      181 gerakeeala hfeklfeile drkssvlkai daskklrldk fhtqmeeyqg llennglvgy
      241 aqevlketdq scfvqtakql hlriqkates lksfrpaaqa sfedyvvnis kqtevlgels
      301 ffssgidipe ineeqskvyn nalidwhhpe kdkadsyvle yrkinrdeem iswneievhg
      361 tskvvsnles nspyafrvra yrgsicspcs relvlhtppa pvfsflfdek cgyntehlll
      421 nlkrdrvesr agfnvllaae riqvghytsl dyiigdvgit kgkhfwacrv epysylvkvg
      481 vassdklqew lrsprdaasp ryeqdsghds gsedayfdss qpftlvtigm kkffipkspt
      541 ssnepenrvl pmptsigifl dcdkgkvsfy dmdhmkclye rqvdcshtmy pafalmgsgg
      601 iqleetitak yleyeedv
//
LOCUS       NP_001424288             558 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424288 XP_063127390
VERSION     NP_001424288.1
DBSOURCE    REFSEQ: accession NM_001437359.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127390.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..558
                     /product="coiled-coil domain-containing protein 63 isoform
                     2"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65522
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..558
                     /gene="Ccdc63"
                     /coded_by="NM_001437359.1:251..1927"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeveypldhs slrqlvleny lqkergkepq
      541 etllekgdei rvkkkvis
//
LOCUS       NP_001424226             103 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424226
VERSION     NP_001424226.1
DBSOURCE    REFSEQ: accession NM_001437297.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2458210.1,
                                           SRR26360172.988737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..103
                     /product="mitochondrial ribosomal protein S6 isoform 3"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=11023
     Region          3..>61
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     CDS             1..103
                     /gene="Mrps6"
                     /coded_by="NM_001437297.1:106..417"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mpryelalil kamrrpetaa alkrtieslm drgaivrnle nlgeralpyr isshsqqhsr
       61 ggdsartslf vgeglmeshi aegatgggvl stlskkgehl pea
//
LOCUS       NP_001424184             127 aa            linear   ROD 03-APR-2025
DEFINITION  small ribosomal subunit protein uS17m [Rattus norvegicus].
ACCESSION   NP_001424184 XP_038945151
VERSION     NP_001424184.1
DBSOURCE    REFSEQ: accession NM_001437255.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038945151.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1139249.1,
                                           SRR26360194.2275248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..127
                     /product="small ribosomal subunit protein uS17m"
                     /note="28S ribosomal protein S17, mitochondrial"
                     /calculated_mol_wt=13868
     Region          11..84
                     /region_name="Ribosomal_uS17"
                     /note="Ribosomal protein uS17; cd00364"
                     /db_xref="CDD:466775"
     CDS             1..127
                     /gene="Mrps17"
                     /coded_by="NM_001437255.1:218..601"
                     /db_xref="GeneID:288621"
                     /db_xref="RGD:1307650"
ORIGIN      
        1 msivrsavha kwvvgkvigt amvktakvra trlvldpyll kyfnkrktyf ahdalqqcsv
       61 gdivllralp vprakhvkhe laeiifkvgr vidpvtgkpc agtaylespl sseatppces
      121 reelkss
//
LOCUS       NP_001424289             558 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424289 XP_063127391
VERSION     NP_001424289.1
DBSOURCE    REFSEQ: accession NM_001437360.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127391.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.595138.1,
                                           SRR26360181.1357217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..558
                     /product="coiled-coil domain-containing protein 63 isoform
                     2"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65522
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..558
                     /gene="Ccdc63"
                     /coded_by="NM_001437360.1:38..1714"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeveypldhs slrqlvleny lqkergkepq
      541 etllekgdei rvkkkvis
//
LOCUS       NP_001424304             589 aa            linear   ROD 03-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424304 XP_017456371
VERSION     NP_001424304.1
DBSOURCE    REFSEQ: accession NM_001437375.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017456371.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1401258.1,
                                           SRR26360181.1631580.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..589
                     /product="methyl-CpG-binding domain protein 1 isoform 5"
                     /calculated_mol_wt=64584
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          304..350
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..589
                     /gene="Mbd1"
                     /coded_by="NM_001437375.1:162..1931"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekg
      241 kydhskrgpr vasrrhsrap plpphaasqh peptelhisd qtptapaefv ydcveedelq
      301 pytnqrqnrk cgacaaclrr mdcghcdfcc dkpkfggsnq krqkcrwrqc lqfamkrllp
      361 sigpgseeea rllphhthqk rsastrqlql ssplkaplav vttppgpvqd sgkrqagsgf
      421 vlpqpdtdlv ylqegtsslm qvpgpaaast enpaqetqgs apgwvvalpq vkqekadape
      481 ewtavttflt sstvqpgfls kasgldpppv kreppgpeed geenkeddvs esapaeeigg
      541 igtpviteif slggtrlrda eawlprlhkl lavneneyft elqlkeeil
//
LOCUS       NP_001424239             544 aa            linear   ROD 03-APR-2025
DEFINITION  protein hinderin isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424239 XP_038952960
VERSION     NP_001424239.1
DBSOURCE    REFSEQ: accession NM_001437310.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952960.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.76444.1,
                                           SRR26360181.2656524.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..544
                     /product="protein hinderin isoform 4"
                     /calculated_mol_wt=61966
     Region          28..351
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     CDS             1..544
                     /gene="Kiaa1328"
                     /gene_synonym="RGD1562608; RGD1564140"
                     /coded_by="NM_001437310.1:247..1881"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:498831"
                     /db_xref="RGD:1562608"
ORIGIN      
        1 meslkgagds vaeqsfckrg lksaslkdlc vedkrrianl ikelarvsee kevteerlkt
       61 eqesfekkir qleeqnelii kerealqlqy recqellsly qkylseqqek ltmslselga
      121 araqeqqitk kkithqsslv nldgsylsva kpqtcqtrar pksenqdsas eshtalrnns
      181 lkpvtlhhpk qdlermstet rtctyespgr rlinaapvee alpeelkikd ypnllptpss
      241 qycghkyses eayvhenyhp tnmasqcckt hpescshcrm swaslmhdgv tlqpretdie
      301 kqlsedrrqq lmlqkmelei ekerlqqlla qqetklllkq qqlhqsrldy nwlrtqavfr
      361 srelvadkdf pkpgsdsgps llkpkcdgwl rgtsssfrkc pdspnsaqnq kekktvefqs
      421 hvengiqwtc qqndtcrlqr etatgvrkda stspmstqsp khpltpasss skhktsryet
      481 slldlvqsls pnsapkcqph ssraagtwsa lrptpktstw kkvgthkspe dleenqiled
      541 iffi
//
LOCUS       NP_001424255             799 aa            linear   ROD 03-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 2 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001424255
VERSION     NP_001424255.1
DBSOURCE    REFSEQ: accession NM_001437326.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Cruz-Garcia,D., Vazquez-Martinez,R., Peinado,J.R., Anouar,Y.,
            Tonon,M.C., Vaudry,H., Castano,J.P. and Malagon,M.M.
  TITLE     Identification and characterization of two novel (neuro)endocrine
            long coiled-coil proteins
  JOURNAL   FEBS Lett 581 (17), 3149-3156 (2007)
   PUBMED   17572408
  REMARK    GeneRIF: NECC 1 & 2 proteins primarily expressed in
            (neuro)endocrine tissues in vertebrates thus supporting a role for
            these proteins in the regulated secretory pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.73921.1,
                                           SRR26360194.391520.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..799
                     /product="janus kinase and microtubule-interacting protein
                     2 isoform 3"
                     /calculated_mol_wt=93562
     Region          19..>576
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          409..581
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          <476..>782
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..799
                     /gene="Jakmip2"
                     /gene_synonym="RGD1559742"
                     /coded_by="NM_001437326.1:494..2893"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:307479"
                     /db_xref="RGD:1559742"
ORIGIN      
        1 mskkgrnkge kpealivalq aanedlrtkl tdiqielhqe kskvsklere ktqeakrire
       61 leqrkhtvlv telkaklhee kmkelqavre nlikqheqem srtvkvrdge iqrlksalca
      121 lrdgssdkvr taltiearee arkqfdaerl kllqeitdlk takkqvdeal snmiqadkik
      181 agdlrsehqs hqeaiskikw eserdirrlm deikakdrii fslekeletq tgyvqklqlq
      241 kealdeqlfl vkeaecnmss pkreipgrag dgsehcsspd lrrnqkriae lnatirkled
      301 rntllgdern ellkrvrete kqckpllern kclakrndel mvslqrmeek lkaitkense
      361 mrekitshpp lkklkslndl dqaneeqete flklqvieqq niideltrdr eklirrrkhr
      421 rsskpikrpv ldpfigyded smdsetssmt sfrtdrtpat pdddldesla aeeselrfrq
      481 ltkeyqalqr ayallqeqtg giidaereak aqeqlqaevl ryrakiedle atlaqkgqie
      541 kqeaenhrlq qelqdardqn ellefrnlel eererrsppf nlqihpfsdg vsalqiycmk
      601 egvkdvnipd likqldilgd ngnlrneeqv aiiqastvls laekwiqqie gaeaalhqkm
      661 melesdmeqf ckikgyleee ldyrkqaldq aymriqelea tlynalqqet vikfgellsd
      721 kqqeelrtav eklrrqmlrk sreydcqilq ermellqqah qrirdledkt diqkrqikdl
      781 eekflflflf fslafilwp
//
LOCUS       NP_001424252             916 aa            linear   ROD 03-APR-2025
DEFINITION  sarcalumenin isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001424252 XP_063124970
VERSION     NP_001424252.1
DBSOURCE    REFSEQ: accession NM_001437323.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Zhao,X., Yoshida,M., Brotto,L., Takeshima,H., Weisleder,N.,
            Hirata,Y., Nosek,T.M., Ma,J. and Brotto,M.
  TITLE     Enhanced resistance to fatigue and altered calcium handling
            properties of sarcalumenin knockout mice
  JOURNAL   Physiol Genomics 23 (1), 72-78 (2005)
   PUBMED   15998745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063124970.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.25363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..916
                     /product="sarcalumenin isoform 4 precursor"
                     /calculated_mol_wt=97496
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2109
     Region          <76..309
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <271..>483
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          490..517
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          538..779
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Site            543..550
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(548..551,633,699,701,735..737)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Site            574
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            578..580
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Site            633..636
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(635..636,662..663)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Site            698..701
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Site            735..737
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     CDS             1..916
                     /gene="Srl"
                     /coded_by="NM_001437323.1:11..2761"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:302948"
                     /db_xref="RGD:1306564"
ORIGIN      
        1 mkallllccf laslllsgqa elqvsasggt edvgnllenh fsagdaslee keralyadaa
       61 pgdknlllhy pdgreaesfe qppagapsta ngqgseseas lsnssaaesa ppgdvegpge
      121 eeegphaagt lppggaegpe erpefssgee agqeeagvgl ptegaanmea eaqeelqgrl
      181 gdgpmeeaaa gaaepvapqs tegeeaegeg sigsdhqste ldgaqdaipa gedsdadvaa
      241 eareeaedqp edhslpseda appgpdhqpt dphavsdmas sevgaeedae dskaevdaet
      301 geeaedqgep rpsleagsar easeksedtq ssevretegq asgmseedla easseeegge
      361 edgrengglp skeesgedsg dgasseeegs tsgeaaepqk tpratgheee gaqldvedln
      421 tgsegvktqd teaeaseerq qgrgnpviah qeeaedvsee apmrdrshie ktlmlnedkp
      481 addysavlqr lrkiyhtsik pleqsykyne lrqheitvlg mapralsild geitskpmvl
      541 flgpwsvgks tminyllgle dtryqlytga epttseftvl mhgpklktie givmaadsar
      601 sfsplekfgq nflekligie vphkllervt fvdtpgiien rkqqergypf ndvcqwfidr
      661 adlifvvfdp tkldvglele mlfrqlkgre sqiriilnka dnlatqmlmr vygalfwsla
      721 plinvteppr vyvssfwpqd ykpdthrdlf lkeeislled lnqvienrle nkiafirqha
      781 irvrihallv drylqtykdk mtffsdgelv fkdivedpdk fyifktilak tnvskfdlpn
      841 reaykdffgi npisnfklls qqcsymggcf lekieraitq elpsllgsig lgknpgapnc
      901 dktgcgetpk nrykkh
//
LOCUS       NP_001424185             127 aa            linear   ROD 03-APR-2025
DEFINITION  small ribosomal subunit protein uS17m [Rattus norvegicus].
ACCESSION   NP_001424185 XP_063127235
VERSION     NP_001424185.1
DBSOURCE    REFSEQ: accession NM_001437256.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127235.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.848498.1,
                                           SRR26643429.43019.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..127
                     /product="small ribosomal subunit protein uS17m"
                     /note="28S ribosomal protein S17, mitochondrial"
                     /calculated_mol_wt=13868
     Region          11..84
                     /region_name="Ribosomal_uS17"
                     /note="Ribosomal protein uS17; cd00364"
                     /db_xref="CDD:466775"
     CDS             1..127
                     /gene="Mrps17"
                     /coded_by="NM_001437256.1:891..1274"
                     /db_xref="GeneID:288621"
                     /db_xref="RGD:1307650"
ORIGIN      
        1 msivrsavha kwvvgkvigt amvktakvra trlvldpyll kyfnkrktyf ahdalqqcsv
       61 gdivllralp vprakhvkhe laeiifkvgr vidpvtgkpc agtaylespl sseatppces
      121 reelkss
//
LOCUS       NP_001099386             798 aa            linear   ROD 03-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001099386 XP_001068938 XP_222022
VERSION     NP_001099386.1
DBSOURCE    REFSEQ: accession NM_001105916.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_222022.4, XP_001068938.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.34953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001105916.2:187..2583"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001424342             355 aa            linear   ROD 03-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424342 XP_063141722
VERSION     NP_001424342.1
DBSOURCE    REFSEQ: accession NM_001437413.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063141722.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2969352.1,
                                           SRR26643429.2897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..355
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 2"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=38498
     Region          1..98
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..355
                     /gene="Xndc1"
                     /coded_by="NM_001437413.1:425..1492"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 mapvkishvv sfssqdpkyp venllnpdsh kgpwlscprd ktgqlkvefq leravpisyi
       61 dvddflipas geswdrlrlt csqpftrhqs fglaflrvrs sldslsdpvk dpsspgssgl
      121 nqnssdkles dpspwltnps irrtffpdpq tstkeisalk gmlkqlqpgp lgraarmvls
      181 aahkappasv vspnnshgep dsshperaep raeepnrknn asrgkrrkvq eqrrplssss
      241 sqpnrratgr tkqrqqrpqa ksdgsgvqat gqcpictgsf siealprhaa tcgessppqp
      301 asptslssse svlwvsspes spppsswvqc picelqfsar eieehasvcg evfpa
//
LOCUS       NP_001424166             314 aa            linear   ROD 03-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001424166 XP_063127231
VERSION     NP_001424166.1
DBSOURCE    REFSEQ: accession NM_001437237.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127231.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.84528.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001437237.1:387..1331"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001358710             473 aa            linear   ROD 03-APR-2025
DEFINITION  sarcalumenin isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001358710 XP_008765732
VERSION     NP_001358710.1
DBSOURCE    REFSEQ: accession NM_001371781.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Zhao,X., Yoshida,M., Brotto,L., Takeshima,H., Weisleder,N.,
            Hirata,Y., Nosek,T.M., Ma,J. and Brotto,M.
  TITLE     Enhanced resistance to fatigue and altered calcium handling
            properties of sarcalumenin knockout mice
  JOURNAL   Physiol Genomics 23 (1), 72-78 (2005)
   PUBMED   15998745
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jul 25, 2019 this sequence version replaced XP_008765732.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.41574.1,
                                           SRR26643295.37072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..473
                     /product="sarcalumenin isoform 2 precursor"
                     /calculated_mol_wt=52343
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2109
     Region          59..91
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          95..336
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Site            100..107
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(105..108,190,256,258,292..294)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Site            131
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            135..137
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Site            190..193
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(192..193,219..220)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Site            255..258
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Site            292..294
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     CDS             1..473
                     /gene="Srl"
                     /coded_by="NM_001371781.2:11..1432"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:302948"
                     /db_xref="RGD:1306564"
ORIGIN      
        1 mkallllccf laslllsgqa eeaedvseea pmrdrshiek tlmlnedkpa ddysavlqrl
       61 rkiyhtsikp leqsykynel rqheitdgei tskpmvlflg pwsvgkstmi nyllgledtr
      121 yqlytgaept tseftvlmhg pklktiegiv maadsarsfs plekfgqnfl ekligievph
      181 kllervtfvd tpgiienrkq qergypfndv cqwfidradl ifvvfdptkl dvglelemlf
      241 rqlkgresqi riilnkadnl atqmlmrvyg alfwslapli nvtepprvyv ssfwpqdykp
      301 dthrdlflke eislledlnq vienrlenki afirqhairv rihallvdry lqtykdkmtf
      361 fsdgelvfkd ivedpdkfyi fktilaktnv skfdlpnrea ykdffginpi snfkllsqqc
      421 symggcflek ieraitqelp sllgsiglgk npgapncdkt gcgetpknry kkh
//
LOCUS       NP_001424286             559 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424286 XP_063127388
VERSION     NP_001424286.1
DBSOURCE    REFSEQ: accession NM_001437357.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127388.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3322296.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..559
                     /product="coiled-coil domain-containing protein 63 isoform
                     1"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65977
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..559
                     /gene="Ccdc63"
                     /coded_by="NM_001437357.1:38..1717"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eevphralsw vqwntlwttv asgswswrtt
      541 frrneeknhr rhcwrrgtr
//
LOCUS       NP_001424284             559 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424284 XP_063127386
VERSION     NP_001424284.1
DBSOURCE    REFSEQ: accession NM_001437355.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127386.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.85247.1,
                                           SRR26360181.634133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..559
                     /product="coiled-coil domain-containing protein 63 isoform
                     1"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65977
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..559
                     /gene="Ccdc63"
                     /coded_by="NM_001437355.1:139..1818"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eevphralsw vqwntlwttv asgswswrtt
      541 frrneeknhr rhcwrrgtr
//
LOCUS       NP_001424293             526 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424293 XP_063127394
VERSION     NP_001424293.1
DBSOURCE    REFSEQ: accession NM_001437364.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127394.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2324488.1,
                                           SRR26360181.1377122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..526
                     /product="coiled-coil domain-containing protein 63 isoform
                     3"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=61429
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..526
                     /gene="Ccdc63"
                     /coded_by="NM_001437364.1:38..1618"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeelcpgcsg ipsgpq
//
LOCUS       NP_001424169             716 aa            linear   ROD 03-APR-2025
DEFINITION  myogenesis-regulating glycosidase [Rattus norvegicus].
ACCESSION   NP_001424169 XP_006238156
VERSION     NP_001424169.1
DBSOURCE    REFSEQ: accession NM_001437240.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Datta,K., Guan,T. and Gerace,L.
  TITLE     NET37, a nuclear envelope transmembrane protein with glycosidase
            homology, is involved in myoblast differentiation
  JOURNAL   J Biol Chem 284 (43), 29666-29676 (2009)
   PUBMED   19706595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006238156.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228576.1, SRR26643296.14973.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..716
                     /product="myogenesis-regulating glycosidase"
                     /calculated_mol_wt=81212
     Region          313..684
                     /region_name="GH31_NET37"
                     /note="glucosidase NET37; cd06592"
                     /db_xref="CDD:269878"
     Site            order(352..353,460,462..463,501,519,603,605)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269878"
     CDS             1..716
                     /gene="Myorg"
                     /gene_synonym="RGD1309821"
                     /coded_by="NM_001437240.1:140..2290"
                     /db_xref="GeneID:366360"
                     /db_xref="RGD:1309821"
ORIGIN      
        1 mpqnlqeksq vyprhrlgsh agpkslevip gatmytflpd nfspakpkpt kelrpllcsv
       61 vlglllvlaa vvawcyysas lrkaerlrae lldlnrggfs irnqkgeqvf rlafrsgald
      121 ldscsrdgal lgcsrtadgr plhffiqtvr pkdtvmcyrv rweeaapgra vehamflgda
      181 aahwyggaem rtqhwpirld gqqepqpfvt sdvyssdaaf ggilerywls sraaaikvnd
      241 svpfhlgwns tersmrlqar yhhtsykppa grtaapelsy rvcvgsdvts ihkymvrryf
      301 nkpsrvpase afrdpiwstw alygrsvdqn kvlqfaqqir qhrfnsshle iddmytpayg
      361 dfdfdeskfp natdlfhrlr dagfrvtlwv hpfvnynssr fgegverelf vreptgrlpa
      421 lvrwwngiga vldftrpear ewfqghlrrl rsrynvasfk fdagevsylp pdfstykpls
      481 dpsvwsrryt emalpffsla evrvgyqsqn iscffrlvdr dsvwgydlgl rslipavltv
      541 smlgypfilp dmiggnavpe rtagrpdgpg perelyvrwl evaafmpamq fsippwqyda
      601 evvaiahkfa alraslvapl llelagevtd tgdpivrplw wiapgdetah ridsqfligd
      661 tllvapvlep gkqerdvylp agkwrsykge lfdktpvllt dypvdldeva yftwas
//
LOCUS       NP_001424231              74 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424231
VERSION     NP_001424231.1
DBSOURCE    REFSEQ: accession NM_001437302.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3266738.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..74
                     /product="mitochondrial ribosomal protein S6 isoform 5"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=7698
     Region          <1..>32
                     /region_name="bS6"
                     /note="Bacterial ribosomal protein S6; cl00414"
                     /db_xref="CDD:469763"
     CDS             1..74
                     /gene="Mrps6"
                     /coded_by="NM_001437302.1:571..795"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mdrgaivrnl enlgeralpy risshsqqhs rggdsartsl fvgeglmesh iaegatgggv
       61 lstlskkgeh lpea
//
LOCUS       NP_001424355             575 aa            linear   ROD 03-APR-2025
DEFINITION  inactive serine/threonine-protein kinase PLK5 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424355 XP_006240985
VERSION     NP_001424355.1
DBSOURCE    REFSEQ: accession NM_001437426.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   de Carcer,G., Escobar,B., Higuero,A.M., Garcia,L., Anson,A.,
            Perez,G., Mollejo,M., Manning,G., Melendez,B., Abad-Rodriguez,J.
            and Malumbres,M.
  TITLE     Plk5, a polo box domain-only protein with specific roles in neuron
            differentiation and glioblastoma suppression
  JOURNAL   Mol Cell Biol 31 (6), 1225-1239 (2011)
   PUBMED   21245385
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Andrysik,Z., Bernstein,W.Z., Deng,L., Myer,D.L., Li,Y.Q.,
            Tischfield,J.A., Stambrook,P.J. and Bahassi el,M.
  TITLE     The novel mouse Polo-like kinase 5 responds to DNA damage and
            localizes in the nucleolus
  JOURNAL   Nucleic Acids Res 38 (9), 2931-2943 (2010)
   PUBMED   20100802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006240985.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38028.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..575
                     /product="inactive serine/threonine-protein kinase PLK5
                     isoform 3"
                     /EC_number="2.7.11.21"
                     /note="polo-like kinase 5 pseudogene;
                     serine/threonine-protein kinase PLK5; inactive
                     serine/threonine-protein kinase PLK5"
                     /calculated_mol_wt=63030
     Region          25..240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          27..457
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     CDS             1..575
                     /gene="Plk5"
                     /gene_synonym="Plk5p"
                     /coded_by="NM_001437426.1:79..1806"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:314627"
                     /db_xref="RGD:1305038"
ORIGIN      
        1 meprlrrrrs rqlvatflrd pgsgrvyrrg kligkgafsr cykltdmsts avfalkvvpr
       61 ggagrlrlrg kslahvlkvr rtltepevry yfrglvsglr ylhqqrivhr dlkpsnffln
      121 knmevkigdl glaarvgpag rchrvlcgtp nfqapevvsr nghsaksdiw algcimytvl
      181 tgtppfaaap lsemyqnird ghyleptqls psarsliarl lapdpderps ldhllqddff
      241 sqgftperlp phschsppvf afppplgrlf rkvgqllltq crppcpftsk easgpgeest
      301 epdhmeasne egaplctesr ihlltlgtpr tdpadakgtl alqlevatrk lclcldagpv
      361 grtatpkcrt eaawrgpkpa gqdppgeqrs vlwapkwvdy slkygfgyql sdggsgvlfr
      421 dgshmalrpp gghvsyqpdq gtlwifalrd vpgplrakla vlrlfacymq rrlreegtap
      481 mtatpaspdf cllsftadaq alamlfsngt vqvssktspv qlvlsgeged flltiqepgg
      541 psmgtsytld vlrshgisla vrhhlrlglh llqsv
//
LOCUS       NP_001424310             115 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424310 XP_063131809
VERSION     NP_001424310.1
DBSOURCE    REFSEQ: accession NM_001437381.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063131809.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1595485.1,
                                           SRR26360176.1858894.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..115
                     /product="uncharacterized protein CFAP97D2 isoform 5"
                     /calculated_mol_wt=13319
     CDS             1..115
                     /gene="Cfap97d2"
                     /coded_by="NM_001437381.1:85..432"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkskq
       61 eiertgides aetkssrsrk tqklralvws temaggldch ghaslhmqth lekrs
//
LOCUS       NP_001424398             392 aa            linear   ROD 03-APR-2025
DEFINITION  GRAM domain-containing protein 2B isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424398 XP_063133369
VERSION     NP_001424398.1
DBSOURCE    REFSEQ: accession NM_001437469.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133369.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.41451.1,
                                           SRR22399492.515284.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11-q12.1"
     Protein         1..392
                     /product="GRAM domain-containing protein 2B isoform 3"
                     /note="GRAM domain-containing protein 3; GRAM
                     domain-containing protein 2B; GRAM domain containing 3"
                     /calculated_mol_wt=43531
     Region          82..174
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     CDS             1..392
                     /gene="Gramd2b"
                     /gene_synonym="Gramd3; RGD1311016"
                     /coded_by="NM_001437469.1:129..1307"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:307288"
                     /db_xref="RGD:1311016"
ORIGIN      
        1 mtelqqeved akpakvltkr egkvgpaqsk ssfdgsnlls dkndcktesk adskterkks
       61 ssssqykanm hfhklfldvp teeplrqsft calqkeilyq gklfvsenwi cfhskvfgkd
      121 tkisipafsv tlikktktal lvpnaliiat vtdryifvsl lsrdstykll ksicghlent
      181 svgnspnpss aensfradrp sslrldfnde fsdldgvvqq rrqdlegyss sgsqtpesen
      241 srdfhvtesq tvlnvtkget kpprtdahgs rapdgkakil pahgqsetig ilhkmesrkc
      301 ptlrhilify aiivcaliis tfymryrint leerlgslts imdphsteqt apsslgsqvq
      361 lnvevlcqel tanivtleki qnnlqkllen gd
//
LOCUS       NP_001424382             546 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 11 [Rattus
            norvegicus].
ACCESSION   NP_001424382 XP_063140209
VERSION     NP_001424382.1
DBSOURCE    REFSEQ: accession NM_001437453.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140209.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2424813.1,
                                           SRR26360181.934275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..546
                     /product="testis-specific serine kinase substrate isoform
                     11"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=59658
     Region          26..546
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>219
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..546
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437453.1:60..1700"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kencrkvtrs vedaeiktnv
      181 lkqnsallee klrylqqqlq detprrqeae lqeleqklea glsrhglgpt tpiqgcsgpp
      241 gspeepprpr glpsngwgma iragegpsls eqelqkvssg leelrrevss laarwhqeeg
      301 avqealrllg glggrldgfl gqweraqreq aqsarglqel rgradelctm versavsvas
      361 lrselealgp vkpileelgr qlqnsrrgpd hvlnldrpaq gpcprcasqg qqlsteslqq
      421 lleraltplv devkqkglap acpscqrlhk kilelerqal akhvraeals stlrlaqdea
      481 vraknllltd kmkpeekvat ldymhlkmcs lhdqlshlpl egstgamggg stggappkrg
      541 gpgseq
//
LOCUS       NP_001424399             323 aa            linear   ROD 03-APR-2025
DEFINITION  GRAM domain-containing protein 2B isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424399
VERSION     NP_001424399.1
DBSOURCE    REFSEQ: accession NM_001437470.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77421.1,
                                           SRR26360181.651196.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11-q12.1"
     Protein         1..323
                     /product="GRAM domain-containing protein 2B isoform 4"
                     /note="GRAM domain-containing protein 3; GRAM
                     domain-containing protein 2B; GRAM domain containing 3"
                     /calculated_mol_wt=36011
     Region          13..105
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     CDS             1..323
                     /gene="Gramd2b"
                     /gene_synonym="Gramd3; RGD1311016"
                     /coded_by="NM_001437470.1:364..1335"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:307288"
                     /db_xref="RGD:1311016"
ORIGIN      
        1 mhfhklfldv pteeplrqsf tcalqkeily qgklfvsenw icfhskvfgk dtkisipafs
       61 vtlikktkta llvpnaliia tvtdryifvs llsrdstykl lksicghlen tsvgnspnps
      121 saensfradr psslrldfnd efsdldgvvq qrrqdlegys ssgsqtpese nsrdfhvtes
      181 qtvlnvtkge tkpprtdahg srapdgkaki lpahgqseti gilhkmesrk cptlrhilif
      241 yaiivcalii stfymryrin tleerlgslt simdphsteq tapsslgsqv qlnvevlcqe
      301 ltanivtlek iqnnlqklle ngd
//
LOCUS       NP_001424387             495 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 15 [Rattus
            norvegicus].
ACCESSION   NP_001424387
VERSION     NP_001424387.1
DBSOURCE    REFSEQ: accession NM_001437458.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2067184.1,
                                           SRR26643293.2974.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..495
                     /product="testis-specific serine kinase substrate isoform
                     15"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=54483
     Region          26..495
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>219
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..495
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437458.1:60..1547"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kencrkvtrs vedaeiktnv
      181 lkqnsallee klrylqqqlq detprrqeae lqeleqklea glsrhglgpt tpiqgcsgpp
      241 gspeepprpr glpsngwgma iragegpsls eqelqkvssg leelrrevss laarwhqeeg
      301 avqealrllg glggrldgfl gqweraqreq aqsarglqel rgradelctm versavsvas
      361 lrselealgp vkpileelgr qlqnsrrgpd hvlnldrpaq gpcprcasqg qqlsteslqq
      421 lleraltplv devkqkglap acpscqrlhk kilelerqal akhvraeals stlrlaqdea
      481 vraknllltd kmkpe
//
LOCUS       NP_001424407             913 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424407 XP_063133376
VERSION     NP_001424407.1
DBSOURCE    REFSEQ: accession NM_001437478.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133376.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1909050.1,
                                           SRR26643289.41435.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..913
                     /product="synphilin-1 isoform 2"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=99755
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..913
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437478.1:91..2832"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaa
//
LOCUS       NP_001424364             524 aa            linear   ROD 03-APR-2025
DEFINITION  ras and Rab interactor-like protein isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424364 XP_063139469
VERSION     NP_001424364.1
DBSOURCE    REFSEQ: accession NM_001437435.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Woller,B., Luiskandl,S., Popovic,M., Prieler,B.E., Ikonge,G.,
            Mutzl,M., Rehmann,H. and Herbst,R.
  TITLE     Rin-like, a novel regulator of endocytosis, acts as guanine
            nucleotide exchange factor for Rab5a and Rab22
  JOURNAL   Biochim Biophys Acta 1813 (6), 1198-1210 (2011)
   PUBMED   21419809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063139469.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2099835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..524
                     /product="ras and Rab interactor-like protein isoform 3"
                     /note="ras and Rab interactor-like protein"
                     /calculated_mol_wt=58221
     Region          43..136
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(58,76,97,99)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198256"
     Site            order(98,125)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198256"
     CDS             1..524
                     /gene="Rinl"
                     /gene_synonym="RGD1310133"
                     /coded_by="NM_001437435.1:103..1677"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:292760"
                     /db_xref="RGD:1310133"
ORIGIN      
        1 mrlaqpdmvs aatteearls wplaegadks plrvlsttes llrlqrtqrv wqvpeldaeh
       61 akaflkpwpl gsflvigqdp dqvlmlktgp ssgdintyqi qkfpggvsle ssnlcmpdfp
      121 hllaflsasr dvlprtlllp tptvgpgdkh sdprrlgciq vdtsgrvlsv vnqlylethg
      181 gwetetpqqt kpetgqkrsl aprmptphrv swveeslkpe ahhtgqevhh perqvhypgp
      241 eahslgpevh fpspvleeee evnndsykde eegcedmlta hiralasars syvarqyqcl
      301 rarlisdsgn pyspgdpate llqdvrqllt dlqdylakdp dvravfgnrg psipreedlg
      361 pavevalcra vleplkpalw tklrtlraqe lrrlrrrqia lrvgagpegq spalrnriha
      421 rlahlhaaca prrkvallla vcsdvyagla ggenkagyyl ttwfgalyhi ahyqpdagra
      481 pqelsseara slrqwhrrrt lhqqaqptap enqpfeepwa igdp
//
LOCUS       NP_001101317            1447 aa            linear   ROD 03-APR-2025
DEFINITION  golgin subfamily A member 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001101317 XP_001078840 XP_231418
VERSION     NP_001101317.1
DBSOURCE    REFSEQ: accession NM_001107847.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1447)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1447)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 1447)
  AUTHORS   Ohta,E., Misumi,Y., Sohda,M., Fujiwara,T., Yano,A. and Ikehara,Y.
  TITLE     Identification and characterization of GCP16, a novel acylated
            Golgi protein that interacts with GCP170
  JOURNAL   J Biol Chem 278 (51), 51957-51967 (2003)
   PUBMED   14522980
REFERENCE   4  (residues 1 to 1447)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
REFERENCE   5  (residues 1 to 1447)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
REFERENCE   6  (residues 1 to 1447)
  AUTHORS   Fritzler,M.J., Hamel,J.C., Ochs,R.L. and Chan,E.K.
  TITLE     Molecular characterization of two human autoantigens: unique cDNAs
            encoding 95- and 160-kD proteins of a putative family in the Golgi
            complex
  JOURNAL   J Exp Med 178 (1), 49-62 (1993)
   PUBMED   8315394
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_231418.3, XP_001078840.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.41750.1,
                                           SRR26643294.47062.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1447
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..1447
                     /product="golgin subfamily A member 3 isoform 2"
                     /note="Golgin subfamily A member 3; golgi autoantigen,
                     golgin subfamily a, 3"
                     /calculated_mol_wt=162414
     Region          <298..946
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          623..1311
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1447
                     /gene="Golga3"
                     /coded_by="NM_001107847.2:231..4574"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:312077"
                     /db_xref="RGD:1305262"
ORIGIN      
        1 mdgasakqdg lwenksssdi sscpeaslet vgslaqlpdq qdtaqdgsve vnrvfkeegs
       61 pdrssqvpic qngqipdlql sldpttspvg pdastgstas slplekeeqv rlqarkrlee
      121 qlmqyrvkrh rerssqpatk mklfstldpe lmlnpenlpr asavavtkey sflrtsvprg
      181 pkvgslglla hskekknsks skirsladyr tedpsdsggl gstadavgss lkqsrsstsv
      241 vsevspscet dnraesasla gdsvseadgn esdssshssf sargacavlg nvgtpgaayv
      301 vdgqeisaea lgqfpsikdv lqaaaaqhqd qnqeangevq srrdsicssv smessfaepq
      361 eellqilkdk rrlegqveal sleasqalqe kaelqaqlaa lstrlqaqve hshssqqkqd
      421 slssevdtlk qscwdleram tdlqnmleak naslassnnd lqvaeeqyqr lmakveamqr
      481 nilskdntvh dlrqqmtalq sqlqqvqler ttltsklqas qaeitslqqa rqwyqqqlal
      541 aqearvrlqg emahiqvgqm tqagllehlk lenvslshql tetqhrsike keriavqlqs
      601 ieadmldqea afvqireakt mveedlqrkl eefegereql qkvadaaasl eqqleqvklt
      661 lfqrdqqlaa lqqehldvik qltstqealq akgqslddlq trydelqarl eelqreadsr
      721 edaihflqne kivlevalhs arsdkeeldr garrleedte etsglleqlr qdvavksnqv
      781 ehlqqetatl rkqmqkvkeq flqqkvmvea yrrdaaskdq linelkatkk rldsemkelr
      841 qeliklhgek ktvevehsrl qkdmslvhqq maeleghlqs vqkerdemei hlqslkfdke
      901 qmialteane tlkkqieelq qeakkaiteq kqkmkrlgsd ltsaqkemkt khkayenavs
      961 ilsrrlqeal ankeatdael nqlraqstgg ssdpalheki halevelqnv gqskilleke
     1021 lqevitmtsq eleesrekvl eledelqesr gfrrkikrle esnkklalel ehergkltgl
     1081 gqsnaalreh nsiletalak readlvqlnl qvqavlqrke eedrqmkqlv qalqisleke
     1141 ktevsslkeq maaarveagh nrrhfkaatl elsevkkelq akehlvqtlq aevdelqiqe
     1201 gkhsqeiaqf qtelaeartq lqllqkklee qrsqqptgsq emedlkweld qkereiqslk
     1261 qqldltehqg kkelegtqqt lqtikselet vqedlsetqk dkfmlqakvs elknnmktll
     1321 qqnqqlkldl rrgaakkkep kgessssspa tpikipdcpv paslleellr pppavskepl
     1381 knlnsclqql kqemdslqrq meehtitvhe slsswaqvea apaehaharg dtkvhnqnsv
     1441 pgeglgq
//
LOCUS       NP_001424390             301 aa            linear   ROD 03-APR-2025
DEFINITION  nitric oxide synthase-interacting protein [Rattus norvegicus].
ACCESSION   NP_001424390 XP_063140243
VERSION     NP_001424390.1
DBSOURCE    REFSEQ: accession NM_001437461.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Yu,X., Zhong,Y., Zhu,Z., Wu,T., Shen,A. and Huang,Y.
  TITLE     Increased expression of nitric oxide synthase interacting protein
            (NOSIP) following traumatic spinal cord injury in rats
  JOURNAL   J Mol Histol 43 (6), 661-668 (2012)
   PUBMED   23135205
  REMARK    GeneRIF: Data suggested that NOSIP may play an important roles in
            astrogliogenesis after a spinal cord injury.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dreyer,J., Schleicher,M., Tappe,A., Schilling,K., Kuner,T.,
            Kusumawidijaja,G., Muller-Esterl,W., Oess,S. and Kuner,R.
  TITLE     Nitric oxide synthase (NOS)-interacting protein interacts with
            neuronal NOS and regulates its distribution and activity
  JOURNAL   J Neurosci 24 (46), 10454-10465 (2004)
   PUBMED   15548660
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Dedio,J., Konig,P., Wohlfart,P., Schroeder,C., Kummer,W. and
            Muller-Esterl,W.
  TITLE     NOSIP, a novel modulator of endothelial nitric oxide synthase
            activity
  JOURNAL   FASEB J 15 (1), 79-89 (2001)
   PUBMED   11149895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140243.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.2331.1,
                                           SRR26360181.2907997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..301
                     /product="nitric oxide synthase-interacting protein"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=33126
     Region          4..78
                     /region_name="zf-NOSIP"
                     /note="Zinc-finger of nitric oxide synthase-interacting
                     protein; pfam15906"
                     /db_xref="CDD:318178"
     Region          220..287
                     /region_name="RING-Ubox2_NOSIP"
                     /note="U-box domain 2, a modified RING finger, found in
                     nitric oxide synthase-interacting protein (NOSIP) and
                     similar proteins; cd16662"
                     /db_xref="CDD:438324"
     CDS             1..301
                     /gene="Nosip"
                     /coded_by="NM_001437461.1:297..1202"
                     /db_xref="GeneID:292894"
                     /db_xref="RGD:1309992"
ORIGIN      
        1 mtrhgkncta gavytyhekk kdtaasgygt qnirlsrdav kdfdccclsl qpchdpvvtp
       61 dgylyereai leyilhqkre iarqmkayek qrgarreeqk elqraaaqdq vrgflekesa
      121 ivsrplnpfm pkaatlpntd geqpgpsvgp lgkdkdkalp sfwipsltpe akatklekps
      181 rtvtcpmsgk plrmsdltsv rftqlddsvd rvglitrser yvcavtrdsl snatpcavlr
      241 psgavvtlec veklirkdmv dpvngdtlte rdiivlqrgg tgfagsgvkl qaemsrpvmq
      301 a
//
LOCUS       NP_001424424            1685 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424424 XP_063140434
VERSION     NP_001424424.1
DBSOURCE    REFSEQ: accession NM_001437495.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1685)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1685)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1685)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1685)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1685)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1685)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1685)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1685)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1685)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1685)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140434.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.2129.1,
                                           SRR26643298.3339.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1685
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1685
                     /product="tight junction protein ZO-1 isoform 4"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=188789
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <1092..1501
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1553..1651
                     /region_name="ZU5"
                     /note="ZU5 domain; pfam00791"
                     /db_xref="CDD:459941"
     CDS             1..1685
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437495.1:434..5491"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qvyrkepype emmrqnhilk qpalghpgqr ldkepnpayd
      961 pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf edrvptyedq wsyyddkqpy
     1021 ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd srpryeqlpr tstlrheeqp
     1081 tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq vpppgftskt ghyeplhgaa
     1141 vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp qsvltrvkmf enkrsaslen
     1201 kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk tlyrlpepqk pqakppediv
     1261 rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs epakpvhsqs qpnfssyssk
     1321 gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl snsslhihsk aaqsegnsvs
     1381 ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks fpdkasvnga eqtqktitpa
     1441 ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel sskpppspkt lmkahsstqp
     1501 pefdsgvetf svhtdkpkyq innistmpka vpvspsavee dededghtvv atargifnsn
     1561 ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp pldkekgetl lsplvmcgph
     1621 glkflkpvel rlphcasmtp dgwsfalkss dsssgdpktw qnkclpgdpn ylvgancvsv
     1681 lidhf
//
LOCUS       NP_001424384             543 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 13 [Rattus
            norvegicus].
ACCESSION   NP_001424384 XP_063140218
VERSION     NP_001424384.1
DBSOURCE    REFSEQ: accession NM_001437455.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140218.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2980.1,
                                           SRR26360181.140237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..543
                     /product="testis-specific serine kinase substrate isoform
                     13"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=58855
     Region          26..>462
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>228
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..543
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437455.1:60..1691"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kgprpdvltq encrkvtrsv
      181 edaeiktnvl kqnsalleek lrylqqqlqd etprrqeael qeleqkleag lsrhglgptt
      241 piqgcsgppg speepprprg lpsngwgmai ragegpslse qelqkvssgl eelrrevssl
      301 aarwhqeega vqealrllgg lggrldgflg qweraqreqa qsarglqelr gradelctmv
      361 ersavsvasl rselealgpv kpileelgrq lqnsrrgpdh vlnldrpaqg pcprcasqgq
      421 qlsteslqql leraltplvd evkqkglapa cpscqrlhkk ilpspvspaa ptllspgaga
      481 pglgqtrqgr gpelhpsagp rrsrsgqept adgqdeagge gghfglyafe dvfpprptqp
      541 pat
//
LOCUS       NP_001014033             445 aa            linear   ROD 03-APR-2025
DEFINITION  GRAM domain-containing protein 2B isoform 1 [Rattus norvegicus].
ACCESSION   NP_001014033 XP_225748
VERSION     NP_001014033.1
DBSOURCE    REFSEQ: accession NM_001014011.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 20, 2005 this sequence version replaced XP_225748.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090001.1, SRR26643287.35034.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11-q12.1"
     Protein         1..445
                     /product="GRAM domain-containing protein 2B isoform 1"
                     /note="GRAM domain-containing protein 3; GRAM
                     domain-containing protein 2B; GRAM domain containing 3"
                     /calculated_mol_wt=49098
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96HH9; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG8.1)"
     Region          135..227
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PEM6; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG8.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PEM6; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG8.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG8.1)"
     Region          277..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG8.1)"
     CDS             1..445
                     /gene="Gramd2b"
                     /gene_synonym="Gramd3; RGD1311016"
                     /coded_by="NM_001014011.2:132..1469"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307288"
                     /db_xref="RGD:1311016"
ORIGIN      
        1 mvkkpisssd evfkfeipss pkssagashs stdspssvfl sseaengved rkrfskspta
       61 qsptssveae spdqkrslgl wskssfdgsn llsdkndckt eskadskter kksssssqyk
      121 anmhfhklfl dvpteeplrq sftcalqkei lyqgklfvse nwicfhskvf gkdtkisipa
      181 fsvtlikktk tallvpnali iatvtdryif vsllsrdsty kllksicghl entsvgnspn
      241 pssaensfra drpsslrldf ndefsdldgv vqqrrqdleg ysssgsqtpe sensrdfhvt
      301 esqtvlnvtk getkpprtda hgsrapdgka kilpahgqse tigilhkmes rkcptlrhil
      361 ifyaiivcal iistfymryr intleerlgs ltsimdphst eqtapsslgs qvqlnvevlc
      421 qeltanivtl ekiqnnlqkl lengd
//
LOCUS       NP_001424460             353 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424460 XP_063133612
VERSION     NP_001424460.1
DBSOURCE    REFSEQ: accession NM_001437531.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133612.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1310525.1,
                                           SRR26643295.56154.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..353
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=39762
     Region          92..150
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          179..235
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          268..335
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..353
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437531.1:512..1573"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 mqflkeetlt ylnivspfel kmgsqkkvqr rttaqassnt elalggaaaa aaasdvdqed
       61 svderavqdv eslssliqei ldfnqdrqmk cfnsklflcs icfceklgsd cmyflecrhv
      121 yckaclkdyf eiqikdgqvk clncpepqcs svatpgqvke lveadlfary drlllqstld
      181 lmadvvycpr pccqlpvmqe pggtmaicss cnfafctlcr ltyhgvspck vtaeklidlr
      241 neylqadeat krfleqrygk rviqkaleem eskdwlekns kscpccgtpi qkldgcnkmt
      301 ctgcmqyfcw vcmgslsran pykhftdpds pcfnrlfhav dvngdiwede ied
//
LOCUS       NP_001424366            1415 aa            linear   ROD 03-APR-2025
DEFINITION  trafficking protein particle complex subunit 8 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424366 XP_006254523
VERSION     NP_001424366.1
DBSOURCE    REFSEQ: accession NM_001437437.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1415)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254523.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.49478.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1415
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..1415
                     /product="trafficking protein particle complex subunit 8
                     isoform 2"
                     /note="trafficking protein particle complex subunit
                     8-like; trafficking protein particle complex 8"
                     /calculated_mol_wt=158303
     Region          160..586
                     /region_name="TRAPPC-Trs85"
                     /note="ER-Golgi trafficking TRAPP I complex 85 kDa
                     subunit; pfam12739"
                     /db_xref="CDD:463688"
     CDS             1..1415
                     /gene="Trappc8"
                     /gene_synonym="RGD1309102"
                     /coded_by="NM_001437437.1:344..4591"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:291750"
                     /db_xref="RGD:1309102"
ORIGIN      
        1 maqcvqsvqe lipdsfvpcv aalcsdeaer ltrlnhlsfa ellkpfsrlt sevhmrdpnn
       61 qlhiiknlki avsnivtqpp qpgaigklln dvvsgsqpae glvanvitag dydlnisatt
      121 pwfesyretf lqsmpasdhe flnhylacml vassaeaepm eqfsklsqeq hriqhnsdys
      181 ypkwfipntl kyyvllhdvt sgdeqraesi yeemkqkygt qgcyllkins rapnrasdeq
      241 ipdpwsqylq knsiqnqesy edgpctmtsi dglpdncrvh plqidqcgdt phntdgsdha
      301 ksassvhetk kastglirga cltltdhdri rqfiqeftfr gllphvekti rqlndqlisr
      361 kglsrslfsa tkkwfsgskv peksiselks tsgllyppea pelqirkmad lcflvqhydl
      421 ayscyhtakk dflndqamly aagalemaav saflqpgapr pypahymdta iqtyrdickn
      481 mvlaercvll saeilksqsk yaeaaallir ltsedsdlrs allleqaahc finmknpmvr
      541 kyafhmilag hrfskagqkk halrcycqam qvykgkgwsl aedhinftig rqsytlrqld
      601 navsafrhil ineskqsaaq qgaflreyly vyknvnqlsp dgplpqlplp yinssatrvf
      661 fghdrrpadg ekqaathvsl dqeydaessq qwreleehvv avankgvips sfyptqycln
      721 sysdnsrfpl avveepitve vafrnplkvp lllsdlsllw kfqpkdtsgk dtekervtge
      781 pemigtevis eflinseesk varlklfphh igelhilgvv ynlgtiqgsv tvdgigalpg
      841 chtgkhslgm svrgrqdlei qgprlnntke ektsvkygpd rrldpivtee mpllevffih
      901 fptgllcgei rkayvefvnv sqcpltalkv vskrpefftf ggntaaltpl spstsencsa
      961 yktvvtasps lgtafvstas svdfgtgtgq qleaipvplp dsvllpgasv qlpmwlrgpd
     1021 eegvheinfl fyyesvkkqp kkrhrilrht avictsrsln vratvcrsns ledeegrggn
     1081 mlvfvdvent ntseagvkef hmvqvssssk hwqlhrsvni senrdaklas rekgkfcfka
     1141 vrckqkegdk qssekytfad iifgneqiis saspcadffy rslsselrrt qdqlpaypek
     1201 nasegavrli ekcsevdlsi vvlwkayvve dnkqlilegq hhvvvrtvgk eacshsqkqe
     1261 ppemellkff rpenttvsar psveqlsnli ktslhypesf hhpfhqkslc lvpvtlllsn
     1321 cskaevdviv dlrhkttspe alethgsftw lgqtqyklql ksqethslql kacfvhtgvy
     1381 nlgtprvfak lsdqvtvfet sqqnsmpali iinna
//
LOCUS       NP_001424379             525 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 8 [Rattus
            norvegicus].
ACCESSION   NP_001424379 XP_006229082
VERSION     NP_001424379.1
DBSOURCE    REFSEQ: accession NM_001437450.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229082.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.195893.1,
                                           SRR26643293.2997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..525
                     /product="testis-specific serine kinase substrate isoform
                     8"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=57262
     Region          48..525
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>249
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          253..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..525
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437450.1:46..1623"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kencrkvtrs vedaeiktnv lkqnsallee klrylqqqlq detprrqeae
      241 lqeleqklea glsrhglgpt tpiqgcsgpp gspeepprpr glpsngwgma iragegpsls
      301 eqelqkvssg leelrrevss laarwhqeeg avqealrllg glggrldgfl gqweraqreq
      361 aqsarglqel rgradelctm versavsvas lrselealgp vkpileelgr qlqnsrrgpd
      421 hvlnldrpaq gpcprcasqg qqlsteslqq lleraltplv devkqkglap acpscqrlhk
      481 kilelerqal akhvraeals stlrlaqdea vraknllltd kmkpe
//
LOCUS       NP_001424449             858 aa            linear   ROD 03-APR-2025
DEFINITION  dynamin-3 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424449 XP_063128083
VERSION     NP_001424449.1
DBSOURCE    REFSEQ: accession NM_001437520.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Reubold,T.F., Faelber,K., Plattner,N., Posor,Y., Ketel,K.,
            Curth,U., Schlegel,J., Anand,R., Manstein,D.J., Noe,F., Haucke,V.,
            Daumke,O. and Eschenburg,S.
  TITLE     Crystal structure of the dynamin tetramer
  JOURNAL   Nature 525 (7569), 404-408 (2015)
   PUBMED   26302298
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Li,J., Zhang,D.S., Ye,J.C., Li,C.M., Qi,M., Liang,D.D., Xu,X.R.,
            Xu,L., Liu,Y., Zhang,H., Zhang,Y.Y., Deng,F.F., Feng,J., Shi,D.,
            Chen,J.J., Li,L., Chen,G., Sun,Y.F., Peng,L.Y. and Chen,Y.H.
  TITLE     Dynamin-2 mediates heart failure by modulating Ca2+ -dependent
            cardiomyocyte apoptosis
  JOURNAL   Int J Cardiol 168 (3), 2109-2119 (2013)
   PUBMED   23410488
  REMARK    GeneRIF: DNM2 mediates HF by modulating Ca(2+)-dependent apoptotic
            death of cardiomyocyte.
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Ikeuchi,Y., de la Torre-Ubieta,L., Matsuda,T., Steen,H., Okazawa,H.
            and Bonni,A.
  TITLE     The XLID protein PQBP1 and the GTPase Dynamin 2 define a signaling
            link that orchestrates ciliary morphogenesis in postmitotic neurons
  JOURNAL   Cell Rep 4 (5), 879-889 (2013)
   PUBMED   23994472
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Grossman,G.H., Ebke,L.A., Beight,C.D., Jang,G.F., Crabb,J.W. and
            Hagstrom,S.A.
  TITLE     Protein partners of dynamin-1 in the retina
  JOURNAL   Vis Neurosci 30 (4), 129-139 (2013)
   PUBMED   23746204
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Tanifuji,S., Funakoshi-Tago,M., Ueda,F., Kasahara,T. and Mochida,S.
  TITLE     Dynamin isoforms decode action potential firing for synaptic
            vesicle recycling
  JOURNAL   J Biol Chem 288 (26), 19050-19059 (2013)
   PUBMED   23687302
  REMARK    GeneRIF: dynamin isoforms select appropriate vesicle reuse pathways
            associated with specific neuronal firing patterns
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Gray,N.W., Fourgeaud,L., Huang,B., Chen,J., Cao,H., Oswald,B.J.,
            Hemar,A. and McNiven,M.A.
  TITLE     Dynamin 3 is a component of the postsynapse, where it interacts
            with mGluR5 and Homer
  JOURNAL   Curr Biol 13 (6), 510-515 (2003)
   PUBMED   12646135
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Zhang,Y., Moheban,D.B., Conway,B.R., Bhattacharyya,A. and
            Segal,R.A.
  TITLE     Cell surface Trk receptors mediate NGF-induced survival while
            internalized receptors regulate NGF-induced differentiation
  JOURNAL   J Neurosci 20 (15), 5671-5678 (2000)
   PUBMED   10908605
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Cao,H., Garcia,F. and McNiven,M.A.
  TITLE     Differential distribution of dynamin isoforms in mammalian cells
  JOURNAL   Mol Biol Cell 9 (9), 2595-2609 (1998)
   PUBMED   9725914
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Cook,T., Mesa,K. and Urrutia,R.
  TITLE     Three dynamin-encoding genes are differentially expressed in
            developing rat brain
  JOURNAL   J Neurochem 67 (3), 927-931 (1996)
   PUBMED   8752097
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Nakata,T., Takemura,R. and Hirokawa,N.
  TITLE     A novel member of the dynamin family of GTP-binding proteins is
            expressed specifically in the testis
  JOURNAL   J Cell Sci 105 (Pt 1), 1-5 (1993)
   PUBMED   8360266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063128083.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.33659.1,
                                           SRR26360194.497191.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..858
                     /product="dynamin-3 isoform 3"
                     /EC_number="3.6.5.5"
                     /note="T-dynamin; dynamin, testicular; testicular dynamin"
                     /calculated_mol_wt=96529
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          526..635
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(526,528..529,531,548,617..618,621,624..625,628)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          655..745
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          <753..843
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     CDS             1..858
                     /gene="Dnm3"
                     /gene_synonym="dynamin-2"
                     /coded_by="NM_001437520.1:172..2748"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:171574"
                     /db_xref="RGD:727949"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqgtnlp psrqivirkg wltvsnigim
      541 kggskgywfv ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr
      601 nvykdyrsle lacdsqedvd swkasllrag vypdksften dengqaenfs mdpqlerqve
      661 tirnlvdsym siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesve
      721 qaqrrdemlr myqalkeala iigdintvtv stpapppvdd swlqhsrrsp ppspttqrrl
      781 tlsaplprpa ssrgpapaip spgphsgapp vpfrpgplpp fpnssdsyga ppqvpsrptr
      841 appsvprfga vkeeavep
//
LOCUS       NP_001424403             963 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424403 XP_006254782
VERSION     NP_001424403.1
DBSOURCE    REFSEQ: accession NM_001437474.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254782.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.177602.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..963
                     /product="synphilin-1 isoform 1"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=105664
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..963
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437474.1:91..2982"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaamysscih lpsnalveeh lrdyarlndi krntkktynv khiaepepke
      961 lfl
//
LOCUS       NP_001424362             568 aa            linear   ROD 03-APR-2025
DEFINITION  ras and Rab interactor-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424362
VERSION     NP_001424362.1
DBSOURCE    REFSEQ: accession NM_001437433.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Woller,B., Luiskandl,S., Popovic,M., Prieler,B.E., Ikonge,G.,
            Mutzl,M., Rehmann,H. and Herbst,R.
  TITLE     Rin-like, a novel regulator of endocytosis, acts as guanine
            nucleotide exchange factor for Rab5a and Rab22
  JOURNAL   Biochim Biophys Acta 1813 (6), 1198-1210 (2011)
   PUBMED   21419809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.1494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..568
                     /product="ras and Rab interactor-like protein isoform 1"
                     /note="ras and Rab interactor-like protein"
                     /calculated_mol_wt=63096
     Region          43..136
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(58,76,97,99)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(98,125)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Region          417..519
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..568
                     /gene="Rinl"
                     /gene_synonym="RGD1310133"
                     /coded_by="NM_001437433.1:115..1821"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:292760"
                     /db_xref="RGD:1310133"
ORIGIN      
        1 mrlaqpdmvs aatteearls wplaegadks plrvlsttes llrlqrtqrv wqvpeldaeh
       61 akaflkpwpl gsflvigqdp dqvlmlktgp ssgdintyqi qkfpggvsle ssnlcmpdfp
      121 hllaflsasr dvlprtlllp tptvgpgdkh sdprrlgciq vdtsgrvlsv vnqlylethg
      181 gwetetpqqt kpetgqkrsl aprmptphrv swveeslkpe ahhtgqevhh perqvhypgp
      241 eahslgpevh fpspvleeee evnndsykde eegcedmlta hiralasars syvarqyqcl
      301 rarlisdsgn pyspgdpate llqdvrqllt dlqdylakdp dvravfgnrg psipreedlg
      361 pavevalcra vleplkpalw tklrtlraqe lrrlrrrqia lrvgagpegq spalrnriha
      421 rlahlhaaca prrkvallla vcsdvyagla ggenkeplga daflpaltee liwsphiget
      481 qldveflmel ldpgelrgea gyylttwfga lyhiahyqpd agrapqelss earaslrqwh
      541 rrrtlhqqaq ptapenqpfe epwaigdp
//
LOCUS       NP_001424469             209 aa            linear   ROD 03-APR-2025
DEFINITION  melanoma antigen recognized by T-cells 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424469
VERSION     NP_001424469.1
DBSOURCE    REFSEQ: accession NM_001437540.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Hoashi,T., Watabe,H., Muller,J., Yamaguchi,Y., Vieira,W.D. and
            Hearing,V.J.
  TITLE     MART-1 is required for the function of the melanosomal matrix
            protein PMEL17/GP100 and the maturation of melanosomes
  JOURNAL   J Biol Chem 280 (14), 14006-14016 (2005)
   PUBMED   15695812
REFERENCE   2  (residues 1 to 209)
  AUTHORS   De Maziere,A.M., Muehlethaler,K., van Donselaar,E., Salvi,S.,
            Davoust,J., Cerottini,J.C., Levy,F., Slot,J.W. and Rimoldi,D.
  TITLE     The melanocytic protein Melan-A/MART-1 has a subcellular
            localization distinct from typical melanosomal proteins
  JOURNAL   Traffic 3 (9), 678-693 (2002)
   PUBMED   12191019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO793296.1, FO793504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..209
                     /product="melanoma antigen recognized by T-cells 1 isoform
                     2"
                     /note="melanoma antigen recognized by T-cells 1"
                     /calculated_mol_wt=23556
     Region          2..84
                     /region_name="MLANA"
                     /note="Protein melan-A; pfam14991"
                     /db_xref="CDD:464426"
     CDS             1..209
                     /gene="Mlana"
                     /coded_by="NM_001437540.1:56..685"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293890"
                     /db_xref="RGD:1306525"
ORIGIN      
        1 mpreevhfgy prkghshsyi taeeaagigi lvvalgiall igcwycrrrs gyraltdpgs
       61 vpsnhtvahs ppklqsqric qpllvsrvtr naqwtkgvml vlkippgkda yvrvlitkta
      121 dcllkkkttn lwfptlhlpm rsslqttrhh hihpesreaa knsesflhaf alrlsrcpcf
      181 alecyrmysy tnrpglnswq gkqkggeew
//
LOCUS       NP_001424457             479 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424457 XP_017456519
VERSION     NP_001424457.1
DBSOURCE    REFSEQ: accession NM_001437528.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017456519.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.37634.1,
                                           SRR26643290.51322.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..479
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53976
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          218..276
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          305..361
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          394..461
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..479
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437528.1:688..2127"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 msaedleaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrtta qassntelal ggaaaaaaas
      181 dvdqedsvde ravqdvesls sliqeildfn qdrqmkcfns klflcsicfc eklgsdcmyf
      241 lecrhvycka clkdyfeiqi kdgqvkclnc pepqcssvat pgqvkelvea dlfarydrll
      301 lqstldlmad vvycprpccq lpvmqepggt maicsscnfa fctlcrltyh gvspckvtae
      361 klidlrneyl qadeatkrfl eqrygkrviq kaleemeskd wleknskscp ccgtpiqkld
      421 gcnkmtctgc mqyfcwvcmg slsranpykh ftdpdspcfn rlfhavdvng diwedeied
//
LOCUS       NP_892000                368 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 24 [Rattus norvegicus].
ACCESSION   NP_892000 XP_214606
VERSION     NP_892000.1
DBSOURCE    REFSEQ: accession NM_182955.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Howng,S.Y., Avila,R.L., Emery,B., Traka,M., Lin,W., Watkins,T.,
            Cook,S., Bronson,R., Davisson,M., Barres,B.A. and Popko,B.
  TITLE     ZFP191 is required by oligodendrocytes for CNS myelination
  JOURNAL   Genes Dev 24 (3), 301-311 (2010)
   PUBMED   20080941
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Wang,H., Sun,R., Liu,G., Yao,M., Fei,J. and Shen,H.
  TITLE     Characterization of the target DNA sequence for the DNA-binding
            domain of zinc finger protein 191
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 40 (8), 704-710 (2008)
   PUBMED   18685786
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Dec 17, 2003 this sequence version replaced XP_214606.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.49530.1,
                                           SRR26643285.51629.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..368
                     /product="zinc finger protein 24"
                     /note="zfp-191; zinc finger protein 191"
                     /calculated_mol_wt=41779
     Region          48..159
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          <249..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          251..301
                     /region_name="Necessary and sufficient for nuclear
                     localization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          305..>358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..368
                     /gene="Zfp24"
                     /gene_synonym="Zfp191; Znf24"
                     /coded_by="NM_182955.2:198..1304"
                     /db_xref="GeneID:360204"
                     /db_xref="RGD:727963"
ORIGIN      
        1 msaqsveeds iliipnpdee ekilrvklee dpdgeegssi swnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailprelqt lvrehhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lveeiasqed aqglpsseld avenqlkwas
      181 welhslrhcd ddataengal apkqeiasag eshevpgtln igvpqifkyg etcfpkgrfe
      241 rkrnpsrkkq hicdecgkhf sqgsalilhq rihsgekpyg cvecgkafsr ssilvqhqrv
      301 htgekpykcl ecgkafsqns glinhqriht gekpyecvqc gksysqssnl frhqrrhnae
      361 kllnvvkv
//
LOCUS       NP_001424378             534 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001424378 XP_006229081
VERSION     NP_001424378.1
DBSOURCE    REFSEQ: accession NM_001437449.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229081.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..534
                     /product="testis-specific serine kinase substrate isoform
                     7"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=58226
     Region          48..534
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>258
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          262..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..534
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437449.1:46..1650"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kgprpdvltq encrkvtrsv edaeiktnvl kqnsalleek lrylqqqlqd
      241 etprrqeael qeleqkleag lsrhglgptt piqgcsgppg speepprprg lpsngwgmai
      301 ragegpslse qelqkvssgl eelrrevssl aarwhqeega vqealrllgg lggrldgflg
      361 qweraqreqa qsarglqelr gradelctmv ersavsvasl rselealgpv kpileelgrq
      421 lqnsrrgpdh vlnldrpaqg pcprcasqgq qlsteslqql leraltplvd evkqkglapa
      481 cpscqrlhkk ilelerqala khvraealss tlrlaqdeav raknllltdk mkpe
//
LOCUS       NP_001424426            1672 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424426
VERSION     NP_001424426.1
DBSOURCE    REFSEQ: accession NM_001437497.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1672)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1672)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1672)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1672)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1672)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1672)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1672)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1672)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1672)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1672)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.2149575.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1672
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1672
                     /product="tight junction protein ZO-1 isoform 6"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=187448
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <1092..1501
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1549..1662
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     CDS             1..1672
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437497.1:434..5452"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qvyrkepype emmrqnhilk qpalghpgqr ldkepnpayd
      961 pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf edrvptyedq wsyyddkqpy
     1021 ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd srpryeqlpr tstlrheeqp
     1081 tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq vpppgftskt ghyeplhgaa
     1141 vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp qsvltrvkmf enkrsaslen
     1201 kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk tlyrlpepqk pqakppediv
     1261 rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs epakpvhsqs qpnfssyssk
     1321 gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl snsslhihsk aaqsegnsvs
     1381 ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks fpdkasvnga eqtqktitpa
     1441 ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel sskpppspkt lmkahsstqp
     1501 pefdsgvetf svhtdkpkyq innistmpka vpvspsavee dededghtvv atargifnsn
     1561 ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp pldkekgetl lsplvmcgph
     1621 glkflkpvel rlphcasmtp dgdpktwqnk clpgdpnylv gancvsvlid hf
//
LOCUS       NP_001123485            1551 aa            linear   ROD 03-APR-2025
DEFINITION  serine/threonine-protein kinase MRCK gamma isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001123485 XP_001071634 XP_219530
VERSION     NP_001123485.1
DBSOURCE    REFSEQ: accession NM_001130013.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1551)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   2  (residues 1 to 1551)
  AUTHORS   Ng,Y., Tan,I., Lim,L. and Leung,T.
  TITLE     Expression of the human myotonic dystrophy kinase-related
            Cdc42-binding kinase gamma is regulated by promoter DNA methylation
            and Sp1 binding
  JOURNAL   J Biol Chem 279 (33), 34156-34164 (2004)
   PUBMED   15194684
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Jul 12, 2008 this sequence version replaced
            XP_219530.4, XP_001071634.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.5793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1551
                     /product="serine/threonine-protein kinase MRCK gamma
                     isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase MRCK gamma; CDC42
                     binding protein kinase gamma (DMPK-like)"
                     /calculated_mol_wt=172197
     Region          69..399
                     /region_name="STKc_DMPK_like"
                     /note="Catalytic domain of Myotonic Dystrophy protein
                     kinase (DMPK)-like Serine/Threonine Kinases; cd05597"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,148..149,151,155,157,195,197,
                     199..200,202,212..213,216,231..236,268,274,277)
                     /site_type="active"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,149..151,155,195,197,199..200,
                     202,212..213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270748"
     Site            order(81,155,157,195,197,199,216,231..236,268,274,277)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270748"
     Site            order(212..222,225..236)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270748"
     Site            393..398
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270748"
     Region          <446..>801
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          879..930
                     /region_name="C1_MRCKgamma"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in myotonic dystrophy kinase-related Cdc42-binding
                     kinase gamma (MRCK gamma) and similar proteins; cd20866"
                     /db_xref="CDD:410416"
     Site            order(884..890,898..902,905)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410416"
     Region          938..1070
                     /region_name="PH_MRCK"
                     /note="MRCK (myotonic dystrophy-related Cdc42-binding
                     kinase) pleckstrin homology (PH) domain; cd01243"
                     /db_xref="CDD:269949"
     Region          1102..1360
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     CDS             1..1551
                     /gene="Cdc42bpg"
                     /gene_synonym="RGD1307260"
                     /coded_by="NM_001130013.2:179..4834"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293693"
                     /db_xref="RGD:1307260"
ORIGIN      
        1 meqrlraleq lvrgeaggsp gldglldlll gvhqelssap lrrernvaqf lswagpfvtk
       61 vkelrlqrdd feilkvigrg afgevavvrq rdsgqifamk mlhkwemlkr aetacfreer
      121 dvlvkgdsrw vtalhyafqd eeylylvmdy yaggdlltll srfedrlppe laqfylaemv
      181 laihslhqlg yvhrdvkpdn illdmnghir ladfgsclrl nnngmvdssv avgtpdyisp
      241 eilqameegk ghygpqcdww slgvcayell fgetpfyaes lvetygkimn hedhlqfpsd
      301 vddvpasaqa lirqllcrqe erlgrggldd frshpffegv dwerlatsta pyipelrgpv
      361 dtsnfdvddd tlnrpetlpp sshgafsghh lpfvgftyts gsltddksse lmatpewkph
      421 gveqmkvels qkcqealhss lqpqelvrlq kevqvlqekl tetlrdskas lsqadglhvr
      481 spapdiqlqq ekdrlqqela eaqaalqvrd aelcqaqnrq eeflqrlwea qereaaaasq
      541 iqalnsqlee awvvrreleg qvntlsqevt qlqgqckqds ssqaktvhaa petngigspe
      601 gqsqeaqlrk evaalreqle cacsqgvnvg keevlcrlqe enqrlsreqe rlaeeldlel
      661 qsrqrleger resesnweaq iadilswvnd ekvsrgylqa latkmaeele slrnvgtqtl
      721 ptrpldhqwk arrlqkmeas arlelqsale aeirakqglq eqltqvqeaq rqaerrlqea
      781 ekqnqalqqe vaelreelqa rgpgdakpct slipllsfwn tekdsakdpg nsgesprsga
      841 eaelrpegrr slrmgsvfpr vpaanptpae gppakpgsht lrprsfpspt kclhctslml
      901 glgrqglgcd tcgyfchsac atqappcpvp pellrtalgv hpetgtgtay egflsvprps
      961 gvrrgwqrvy aalsdsrlll fdapdprgsm asgvllqald lrdpqfsatp vlapdvihaq
     1021 skdlprifrv tasqltvpps tctvlllaen egererwlqv lselqrllld arprprpvyt
     1081 lkeaydnglp llphtlcaai idrerlalgt eeglfvihlh sndifqvgdc rrvqrltvss
     1141 aagllvvlcg rgpsvrlftl selenaevag akipesrgcq alvagsilqa rtpvlcvavk
     1201 rqvlcyqlgp gpgpwqrrir elqapapvqs lgllgdrlcv gaagtfalyp llneaaplal
     1261 gtglvaeelp asrgglgeal gavelslsel lllfatagvy vdgagrksrs hellwpvapt
     1321 gwgytapylt vfsensidvf dvrraewvqt vplkkvrpln pegslllygt ekvrltylrn
     1381 plaekdefdi pdltdnsrrq lfrtkskrrf ffrvsdelrq qqrremlkdp fvrskfispp
     1441 tnfnhlvhvg ptegrpgprd gtraqeqksr gtrssgpqrp hsfsealrrp vsmgndglpg
     1501 etdplkrkvw tslssesvsc pqgslspaas liqvserprs lppdpesegs p
//
LOCUS       NP_001424363             562 aa            linear   ROD 03-APR-2025
DEFINITION  ras and Rab interactor-like protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424363 XP_006228719
VERSION     NP_001424363.1
DBSOURCE    REFSEQ: accession NM_001437434.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Woller,B., Luiskandl,S., Popovic,M., Prieler,B.E., Ikonge,G.,
            Mutzl,M., Rehmann,H. and Herbst,R.
  TITLE     Rin-like, a novel regulator of endocytosis, acts as guanine
            nucleotide exchange factor for Rab5a and Rab22
  JOURNAL   Biochim Biophys Acta 1813 (6), 1198-1210 (2011)
   PUBMED   21419809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006228719.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.1638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..562
                     /product="ras and Rab interactor-like protein isoform 2"
                     /note="ras and Rab interactor-like protein"
                     /calculated_mol_wt=62471
     Region          37..130
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(52,70,91,93)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(92,119)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Region          411..513
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..562
                     /gene="Rinl"
                     /gene_synonym="RGD1310133"
                     /coded_by="NM_001437434.1:104..1792"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:292760"
                     /db_xref="RGD:1310133"
ORIGIN      
        1 mtlgllepvh srlswplaeg adksplrvls ttesllrlqr tqrvwqvpel daehakaflk
       61 pwplgsflvi gqdpdqvlml ktgpssgdin tyqiqkfpgg vslessnlcm pdfphllafl
      121 sasrdvlprt lllptptvgp gdkhsdprrl gciqvdtsgr vlsvvnqlyl ethggwetet
      181 pqqtkpetgq krslaprmpt phrvswvees lkpeahhtgq evhhperqvh ypgpeahslg
      241 pevhfpspvl eeeeevnnds ykdeeegced mltahirala sarssyvarq yqclrarlis
      301 dsgnpyspgd patellqdvr qlltdlqdyl akdpdvravf gnrgpsipre edlgpaveva
      361 lcravleplk palwtklrtl raqelrrlrr rqialrvgag pegqspalrn riharlahlh
      421 aacaprrkva lllavcsdvy aglaggenke plgadaflpa lteeliwsph igetqldvef
      481 lmelldpgel rgeagyyltt wfgalyhiah yqpdagrapq elssearasl rqwhrrrtlh
      541 qqaqptapen qpfeepwaig dp
//
LOCUS       NP_001424445             648 aa            linear   ROD 03-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424445 XP_063133446
VERSION     NP_001424445.1
DBSOURCE    REFSEQ: accession NM_001437516.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133446.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.424848.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..648
                     /product="band 4.1-like protein 4A isoform 2"
                     /note="erythrocyte protein band 4.1-like 4a; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=73781
     Region          13..211
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          207..296
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(215,232,234,240)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(244,249..252,285,289,292..293)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            285..296
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Region          311..355
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     CDS             1..648
                     /gene="Epb41l4a"
                     /gene_synonym="Epb4.1l4a"
                     /coded_by="NM_001437516.1:723..2669"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:307514"
                     /db_xref="RGD:1306034"
ORIGIN      
        1 mgcfcavpee fycevlllde skltlttqhq gikkstkgsv vldhvfrhvn lveidyfglr
       61 ycdrshqtyw ldpaktlaeh kelintgppy tlyfgikfya edpcklkeei tryqfflqvk
      121 qdalqgrlpc pvniaaqlga yaiqaelgdh dpckhtagyv seyrfvpdqk eeleesieri
      181 hktlmgqaps eaelnylrta kslemygvdl hpvygenkse yflgltpvgv vvyknkkqvg
      241 kyfwpritkv hfketqfelr vlgkdcnets fffearskta ckhlwkcsve hhtffrmpet
      301 esnslsrkls kfgsisykhr ysgrtalqms rdlsiqlprp nqnvvrsrsk typkrvaqtq
      361 pagsnsinrm tanlengene gttkiiapsp vksfkkakne nspdpqrsks hapweengpq
      421 sglynspsdr tkspkfpctr qrnlscgsdn dssqpmrrrk ahhsgedsdl kqrrrsrsrc
      481 ntssgsesen snrehrkkrn rrspdiqake elwkhiqkel vdpsglseeq lkeipytkve
      541 tqgdpvrirh shsprsyrqy rrsqcsdger svlsevnskt dlvpplpvtr ssdaqgsggs
      601 tvhqrrngsk dslieeksql sttnlagkht aktiktiqaa rlktdvtg
//
LOCUS       NP_001424385             534 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 14 [Rattus
            norvegicus].
ACCESSION   NP_001424385 XP_063140220
VERSION     NP_001424385.1
DBSOURCE    REFSEQ: accession NM_001437456.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140220.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3012374.1,
                                           SRR26360181.377395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..534
                     /product="testis-specific serine kinase substrate isoform
                     14"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=57891
     Region          26..>453
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>219
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..534
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437456.1:60..1664"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kencrkvtrs vedaeiktnv
      181 lkqnsallee klrylqqqlq detprrqeae lqeleqklea glsrhglgpt tpiqgcsgpp
      241 gspeepprpr glpsngwgma iragegpsls eqelqkvssg leelrrevss laarwhqeeg
      301 avqealrllg glggrldgfl gqweraqreq aqsarglqel rgradelctm versavsvas
      361 lrselealgp vkpileelgr qlqnsrrgpd hvlnldrpaq gpcprcasqg qqlsteslqq
      421 lleraltplv devkqkglap acpscqrlhk kilpspvspa aptllspgag apglgqtrqg
      481 rgpelhpsag prrsrsgqep tadgqdeagg egghfglyaf edvfpprptq ppat
//
LOCUS       NP_001120845            1136 aa            linear   ROD 03-APR-2025
DEFINITION  activity-dependent neuroprotector homeobox protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001120845 XP_001057780 XP_225732
VERSION     NP_001120845.1
DBSOURCE    REFSEQ: accession NM_001127373.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Kushnir,M., Dresner,E., Mandel,S. and Gozes,I.
  TITLE     Silencing of the ADNP-family member, ADNP2, results in changes in
            cellular viability under oxidative stress
  JOURNAL   J Neurochem 105 (2), 537-545 (2008)
   PUBMED   18179478
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before May 17, 2008 this sequence version replaced
            XP_225732.4, XP_001057780.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166606.1, SRR26643429.54820.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..1136
                     /product="activity-dependent neuroprotector homeobox
                     protein 2"
                     /note="ADNP homeobox protein 2"
                     /calculated_mol_wt=123046
     Region          1..998
                     /region_name="ADNP_N"
                     /note="Activity-dependent neuroprotector homeobox protein
                     N-terminal; pfam19627"
                     /db_xref="CDD:466132"
     Region          1045..1098
                     /region_name="HOX"
                     /note="Homeodomain; smart00389"
                     /db_xref="CDD:197696"
     Site            order(1047..1050,1052,1069,1075,1088,1090..1091,
                     1094..1095,1097..1099,1101..1102)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(1048,1051,1091,1094..1095,1098)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     CDS             1..1136
                     /gene="Adnp2"
                     /gene_synonym="RGD1308279"
                     /coded_by="NM_001127373.2:144..3554"
                     /db_xref="GeneID:307236"
                     /db_xref="RGD:1308279"
ORIGIN      
        1 mfqipvqnld nirkvrkrvk gilvdiglds ckellkdlkg fdpgekyfcn tswgdvslwe
       61 psgkrakyrt kpyccslcry stkvltslkn hlhryheeea dqelmipcpn cpfasqpkvv
      121 gkhfrmfhap arkvqsytvn ilgeaktsrs dvisftclkc nfsntlyysm kkhvlvahfn
      181 ylinsyfglr teetgeqpka sdpvsvdkal pfdkyyckkc saiassqdal myhiltsdah
      241 rdlenklrsv isehikrtgf lkqmhiapkp vthialppns sapsiaappp cfqlalpqns
      301 qspgtvqsvt vapgtsgslt hsppttaqsh valvssslpv cqssltlqqs apppvflshs
      361 vplsqpvsts vlpltqplgp vnksvgtsll pvnqamcsvn qavrpgvlpl pkpmgpinrp
      421 vgpgvlpvgp svnsgvlqat spgvisvgra vpsgvlpagq vtpagvipgq tatsgvlptg
      481 qvvqssvlpv gqtapsrvlp pgqtvplrvl pagqvvppgl lspnqtvpsg vvpvnqgvns
      541 gvlqlsqpvt pgvlpvgppv rpgvlqlsps vstsilpvsq pvragtsqnt tfltsgsilr
      601 qliptgkqvn giptytlapv svtlpvpsag glaavgpppq vpvqflpsss gtqmgsslps
      661 lpspqvlvsp apsvfvqatp pvadanqalr qakqwktcpv cnelfpanvy qvhmevahtq
      721 seakssekpe perlaacapf lkwmrektvr clsckclvsq eelmhhllmh glgclfcpct
      781 fhdvrglveh srtkhlgkkr lsmdysnrgf qldldangnl lfphldfiti lpreklgere
      841 vylailagih skslvpvyvk vrpqpevapk ipnrqkltcp fcfgtfmaad ayelhlkerh
      901 hvmptvhtml rspafkcihc cgvytgnmtl gaiavhllrc rsapkdsssd lqaqpdfies
      961 sellmvngev ipestfplkr klpeghlgpe eqgdgdepql tvdtdaspgs ekglsavplk
     1021 rqknesrteg sgasddslqv laldpskygs rsyeekkqfl rdyfhkrpyp srkevellss
     1081 llwvwkidva sffgkrryic mkaikshkps vllgfdmsel knvkhrlnfe cesenl
//
LOCUS       NP_001099719             568 aa            linear   ROD 03-APR-2025
DEFINITION  sialic acid-binding Ig-like lectin 5 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001099719 XP_001080306 XP_218613
VERSION     NP_001099719.2
DBSOURCE    REFSEQ: accession NM_001106249.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Tateno,H., Li,H., Schur,M.J., Bovin,N., Crocker,P.R.,
            Wakarchuk,W.W. and Paulson,J.C.
  TITLE     Distinct endocytic mechanisms of CD22 (Siglec-2) and Siglec-F
            reflect roles in cell signaling and innate immunity
  JOURNAL   Mol Cell Biol 27 (16), 5699-5710 (2007)
   PUBMED   17562860
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Zhang,J.Q., Biedermann,B., Nitschke,L. and Crocker,P.R.
  TITLE     The murine inhibitory receptor mSiglec-E is expressed broadly on
            cells of the innate immune system whereas mSiglec-F is restricted
            to eosinophils
  JOURNAL   Eur J Immunol 34 (4), 1175-1184 (2004)
   PUBMED   15048729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 12, 2008 this sequence version replaced NP_001099719.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.2153.1,
                                           SRR26643284.632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..568
                     /product="sialic acid-binding Ig-like lectin 5 isoform 1
                     precursor"
                     /calculated_mol_wt=60274
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1783
     Region          20..133
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          122..128
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          139..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          153..157
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          170..174
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          189..193
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          203..208
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..221
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          252..325
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          261..265
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          274..281
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          305..310
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..323
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          <347..419
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          356..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:319310"
     Region          388..392
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:319310"
     Region          401..406
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:319310"
     Region          414..417
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:319310"
     CDS             1..568
                     /gene="Siglec5"
                     /coded_by="NM_001106249.3:292..1998"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:292843"
                     /db_xref="RGD:1305432"
ORIGIN      
        1 mlwaqllpll wagslaveny elsltesvtv qeglcvfvpc qvkypasggs vfgywfqdga
       61 ntnlnspvat ndphrpvqqe tqgrfylvgg idtkncsldi rdarksdtgk yffrldgsvk
      121 ysfrnrmlsv hvtaltktpn lqvtstlvsg tstrvicsvl waceqgtppi fswmssalts
      181 lgrrtilsse lnltprpqdn gtnlicqvtf pgagvtvert qqlsvtyapq kltirvswgd
      241 gtetkvlqsg aslqiqeges lrlvcvadsn psamlswkrq tqknfrlskg delqlprvel
      301 edqgkyicqa knslgtqtas vslsirsllq llapscswds eglhcscssr awpapslgwr
      361 lgegllegns snasftvmss sagpwvnssl slsvefstdh rlsceawndy gvqrativlv
      421 pgqgvsqdks etsggavqga iwgaglmall avsfcliffi vkflrkksal evaamegnhl
      481 aknlvstins asmissnipl rypiqdhlne sesqtqkeep platapdipk depelhyasl
      541 sfqgprpqqp kntetiksvy teikihkr
//
LOCUS       NP_001424377             564 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001424377 XP_063140200
VERSION     NP_001424377.1
DBSOURCE    REFSEQ: accession NM_001437448.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140200.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2996.1,
                                           SRR26360181.2953937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..564
                     /product="testis-specific serine kinase substrate isoform
                     6"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=60670
     Region          48..>483
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>249
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          253..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..564
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437448.1:46..1740"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kencrkvtrs vedaeiktnv lkqnsallee klrylqqqlq detprrqeae
      241 lqeleqklea glsrhglgpt tpiqgcsgpp gspeepprpr glpsngwgma iragegpsls
      301 eqelqkvssg leelrrevss laarwhqeeg avqealrllg glggrldgfl gqweraqreq
      361 aqsarglqel rgradelctm versavsvas lrselealgp vkpileelgr qlqnsrrgpd
      421 hvlnldrpaq gpcprcasqg qqlsteslqq lleraltplv devkqkglap acpscqrlhk
      481 kilpspvspa aptllspgag apglgqtrqg rgpelhpsag prrsrsgqep tadgqdeagg
      541 egghfglyaf edvfpprptq ppat
//
LOCUS       NP_001424412             664 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424412 XP_063133379
VERSION     NP_001424412.1
DBSOURCE    REFSEQ: accession NM_001437483.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133379.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77364.1,
                                           SRR26360181.1691712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..664
                     /product="synphilin-1 isoform 3"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=73234
     Region          <36..209
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(49,51,55..56,59..61,63..64,68,73,82,84,86,125..126,
                     129..131,133..134,138,145,154,156,158,162..163,166..168,
                     170..171,175,178,187)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          49..82
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          84..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          212..255
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     Region          <461..>617
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..664
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437483.1:285..2279"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 mkstlvmtfl iqshlsrpsq hcaedvthrt ktdqphlaad nldkihdeng nnllhvaask
       61 ghaeclqhlt slmgedclne rnaeqltpag laikngqlec vrwmvsetea iaelscskdf
      121 pslihyagcy gqekillwll qfmqeqgisl devdqegnsa vhvasqhgyl gciqtlveyg
      181 anvtmqnhag ekpsqsaerh ghtlcsrylv vvetcmslas qvvkltkqlk eqtvervtlq
      241 sqlqqlleaq ksegkslpss psspsspasr ksqwkildad destgksklg tqegiqvlgn
      301 lssrartkgk dedsdkilrq llgkeisenv ctqeklslef qdaqvssrns kkiplekrel
      361 klarlrqlmq rslsesdtds nnsedpkntp vkrvdrprpq pivesvenmd saeslhlmik
      421 khsvasgrrf pfgmkasksl dghspsptse ssepdldshc pslgmtpptq psteatqcsp
      481 dsataqkvat spksalksps skrrtsqnsk lrvtfeepvv qmeqtsleln gekdkergra
      541 pqrtsesgeq mkrpfgtfrs imeslsgnqn nnnnyqpasq lktctlplts lgrktadakg
      601 npvspaskgk nkaamyssci hlpsnalvee hlrdyarlnd ikrntkktyn vkhiaepepk
      661 elfl
//
LOCUS       NP_001424442             883 aa            linear   ROD 03-APR-2025
DEFINITION  macrophage colony-stimulating factor 1 receptor isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001424442 XP_038952764
VERSION     NP_001424442.1
DBSOURCE    REFSEQ: accession NM_001437513.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Hume,D.A., Teakle,N., Keshvari,S. and Irvine,K.M.
  TITLE     Macrophage deficiency in CSF1R-knockout rat embryos does not
            compromise placental or embryo development
  JOURNAL   J Leukoc Biol 114 (5), 421-433 (2023)
   PUBMED   37167456
  REMARK    GeneRIF: Macrophage deficiency in CSF1R-knockout rat embryos does
            not compromise placental or embryo development.
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Sehgal,A., Carter-Cusack,D., Keshvari,S., Patkar,O., Huang,S.,
            Summers,K.M., Hume,D.A. and Irvine,K.M.
  TITLE     Intraperitoneal transfer of wild-type bone marrow repopulates
            tissue macrophages in the Csf1r knockout rat without contributing
            to monocytopoiesis
  JOURNAL   Eur J Immunol 53 (8), e2250312 (2023)
   PUBMED   37059596
  REMARK    GeneRIF: Intraperitoneal transfer of wild-type bone marrow
            repopulates tissue macrophages in the Csf1r knockout rat without
            contributing to monocytopoiesis.
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Keshvari,S., Caruso,M., Teakle,N., Batoon,L., Sehgal,A.,
            Patkar,O.L., Ferrari-Cestari,M., Snell,C.E., Chen,C., Stevenson,A.,
            Davis,F.M., Bush,S.J., Pridans,C., Summers,K.M., Pettit,A.R.,
            Irvine,K.M. and Hume,D.A.
  TITLE     CSF1R-dependent macrophages control postnatal somatic growth and
            organ maturation
  JOURNAL   PLoS Genet 17 (6), e1009605 (2021)
   PUBMED   34081701
  REMARK    GeneRIF: CSF1R-dependent macrophages control postnatal somatic
            growth and organ maturation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Patkar,O.L., Caruso,M., Teakle,N., Keshvari,S., Bush,S.J.,
            Pridans,C., Belmer,A., Summers,K.M., Irvine,K.M. and Hume,D.A.
  TITLE     Analysis of homozygous and heterozygous Csf1r knockout in the rat
            as a model for understanding microglial function in brain
            development and the impacts of human CSF1R mutations
  JOURNAL   Neurobiol Dis 151, 105268 (2021)
   PUBMED   33450391
  REMARK    GeneRIF: Analysis of homozygous and heterozygous Csf1r knockout in
            the rat as a model for understanding microglial function in brain
            development and the impacts of human CSF1R mutations.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Sharon,A., Jankowski,M.M., Shmoel,N., Erez,H. and Spira,M.E.
  TITLE     Inflammatory Foreign Body Response Induced by Neuro-Implants in Rat
            Cortices Depleted of Resident Microglia by a CSF1R Inhibitor and
            Its Implications
  JOURNAL   Front Neurosci 15, 646914 (2021)
   PUBMED   33841088
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 883)
  AUTHORS   Storga,D., Pecina-Slaus,N., Pavelic,J., Pavelic,Z.P. and Pavelic,K.
  TITLE     c-fms is present in primary tumours as well as in their metastases
            in bone marrow
  JOURNAL   Int J Exp Pathol 73 (4), 527-533 (1992)
   PUBMED   1390197
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Borycki,A.G., Guillier,M., Leibovitch,M.P. and Leibovitch,S.A.
  TITLE     Molecular cloning of CSF-1 receptor from rat myoblasts. Sequence
            analysis and regulation during myogenesis
  JOURNAL   Growth Factors 6 (3), 209-218 (1992)
   PUBMED   1389227
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Claycomb,W.C. and Lanson,N.A. Jr.
  TITLE     Proto-oncogene expression in proliferating and differentiating
            cardiac and skeletal muscle
  JOURNAL   Biochem J 247 (3), 701-706 (1987)
   PUBMED   2447874
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Leibovitch,S.A., Leibovitch,M.P., Guillier,M., Hillion,J. and
            Harel,J.
  TITLE     Differential expression of protooncogenes related to transformation
            and cancer progression in rat myoblasts
  JOURNAL   Cancer Res 46 (8), 4097-4103 (1986)
   PUBMED   2425941
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Sherr,C.J., Rettenmier,C.W., Sacca,R., Roussel,M.F., Look,A.T. and
            Stanley,E.R.
  TITLE     The c-fms proto-oncogene product is related to the receptor for the
            mononuclear phagocyte growth factor, CSF-1
  JOURNAL   Cell 41 (3), 665-676 (1985)
   PUBMED   2408759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952764.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74237.1,
                                           SRR26643299.62937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..883
                     /product="macrophage colony-stimulating factor 1 receptor
                     isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="macrophage colony-stimulating factor 1 receptor;
                     fms proto-oncogene; proto-oncogene fms; proto-oncogene
                     c-Fms; CSF-1 receptor"
                     /calculated_mol_wt=96428
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1977
     Region          28..101
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409410"
     Region          55..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409410"
     Region          66..70
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409410"
     Region          88..91
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409410"
     Region          108..200
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          125..129
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409530"
     Region          139..143
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409530"
     Region          164..168
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409530"
     Region          180..185
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409530"
     Region          193..196
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409530"
     Region          204..303
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          224..228
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409364"
     Region          238..242
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409364"
     Region          267..271
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409364"
     Region          281..286
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409364"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409364"
     Region          304..392
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          446..818
                     /region_name="PTKc_CSF-1R"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Colony-Stimulating Factor-1 Receptor; cd05106"
                     /db_xref="CDD:133237"
     Site            order(491..492,494..497,499,517,519,567,569,573,681,
                     685..686,688,699,717..721,730,765)
                     /site_type="active"
                     /db_xref="CDD:133237"
     Site            order(491..492,494..497,499,517,519,567,569,573,685..686,
                     688,699)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133237"
     Site            order(681,685,717..721,730,765)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133237"
     Site            698..723
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133237"
     CDS             1..883
                     /gene="Csf1r"
                     /gene_synonym="c-fms; CSF-1-R; CSF-1R; M-CSF-R; mrfms"
                     /coded_by="NM_001437513.1:109..2760"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:307403"
                     /db_xref="RGD:2425"
ORIGIN      
        1 melgaplvll latawhgqga pviepsgpel vvepgatvtl rcvsngsvew dgpispywtl
       61 dsespgsili tknatfkntg tyrcteledp mrgstaihly vkahpgpphi ileptklvri
      121 rgeaaqivcs athsevefnv ilkrgdtkle ipinsdfqdn aykkvltlnl navdfqdagi
      181 yscvannaag sntatmnfqv vesaylnlts eqsllqevsv genldltvia daypglqryn
      241 wtylgpffed phnlefrtqw ttysysfklh lnrvkpleag ryslmaqnka gwnnltfelt
      301 lryppevsvt wipvngsdvl lcdvsgypqp nvtwmecrgh tdrcdeaqas qvwddtqpev
      361 lsqkpfhrvi lqsqlpigtl khnmtyvcra hnnvgnssqf fraislgqsk qlpdeylftp
      421 vvvacisvms llvlllllll ykykqkpkyq vrwkiiesye gnnytfidpt qlpynekwef
      481 prnnlqfgkt lgagafgkvv eatafglgke davlkvavkm lkstahadek ealmselkim
      541 shlgqheniv nllgacthgg pvlviteycc ygdllnflrr kaeamlgpsl spgqdpegds
      601 syknihlekk yvrrdsgfss qgvdtyvemr pvstssndsf fkqdldkeas rplelwdllh
      661 fssqvaqgma flaskncihr dvaarnvllt sghvakigdf glardimnds nyvvkgnarl
      721 pvkwmapesi fdcvytvqsd vwsygillwe ifslglnpyp gilvnnkfyk lvkdgyqmaq
      781 pvfapeniys imqscwdlep tkrptfqqic fllqeqarle rreqdyanlp ssssssssss
      841 dsgggsggss sepeeessse hlaccepgdi aqpllqpnny qfc
//
LOCUS       NP_001424404             913 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424404 XP_038952718
VERSION     NP_001424404.1
DBSOURCE    REFSEQ: accession NM_001437475.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952718.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54181.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..913
                     /product="synphilin-1 isoform 2"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=99755
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..913
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437475.1:257..2998"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaa
//
LOCUS       NP_001424422            1752 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424422 XP_063140428
VERSION     NP_001424422.1
DBSOURCE    REFSEQ: accession NM_001437493.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1752)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1752)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1752)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1752)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1752)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1752)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1752)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1752)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1752)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1752)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140428.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.2200.1,
                                           SRR26643287.1278.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1752
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1752
                     /product="tight junction protein ZO-1 isoform 2"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=195677
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          825..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <959..1566
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1023..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1092..1585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1150..1370
                     /region_name="Actin-binding region (ABR).
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1629..1742
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     CDS             1..1752
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437493.1:434..5692"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qkaeasspvp ylspetnpas sasavkhnvn ltnvnleept
      961 papptshvsq adclgapspe aphtmlrdeg vslpshvdpa kvyrkepype emmrqnhilk
     1021 qpalghpgqr ldkepnpayd pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf
     1081 edrvptyedq wsyyddkqpy ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd
     1141 srpryeqlpr tstlrheeqp tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq
     1201 vpppgftskt ghyeplhgaa vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp
     1261 qsvltrvkmf enkrsaslen kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk
     1321 tlyrlpepqk pqakppediv rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs
     1381 epakpvhsqs qpnfssyssk gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl
     1441 snsslhihsk aaqsegnsvs ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks
     1501 fpdkasvnga eqtqktitpa ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel
     1561 sskpppspkt lmkahsstqp pefdsgvetf svhtdkpkyq innistmpka vpvspsavee
     1621 dededghtvv atargifnsn ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp
     1681 pldkekgetl lsplvmcgph glkflkpvel rlphcasmtp dgdpktwqnk clpgdpnylv
     1741 gancvsvlid hf
//
LOCUS       NP_001424456             479 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424456 XP_063133610
VERSION     NP_001424456.1
DBSOURCE    REFSEQ: accession NM_001437527.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133610.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77026.1,
                                           SRR26360181.2458730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..479
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53976
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          218..276
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          305..361
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          394..461
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..479
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437527.1:300..1739"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 msaedleaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrtta qassntelal ggaaaaaaas
      181 dvdqedsvde ravqdvesls sliqeildfn qdrqmkcfns klflcsicfc eklgsdcmyf
      241 lecrhvycka clkdyfeiqi kdgqvkclnc pepqcssvat pgqvkelvea dlfarydrll
      301 lqstldlmad vvycprpccq lpvmqepggt maicsscnfa fctlcrltyh gvspckvtae
      361 klidlrneyl qadeatkrfl eqrygkrviq kaleemeskd wleknskscp ccgtpiqkld
      421 gcnkmtctgc mqyfcwvcmg slsranpykh ftdpdspcfn rlfhavdvng diwedeied
//
LOCUS       NP_001424446             504 aa            linear   ROD 03-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424446 XP_038952803
VERSION     NP_001424446.1
DBSOURCE    REFSEQ: accession NM_001437517.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952803.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.49651.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..504
                     /product="band 4.1-like protein 4A isoform 3"
                     /note="erythrocyte protein band 4.1-like 4a; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=57433
     Region          <2..27
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          23..112
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(31,48,50,56)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(60,65..68,101,105,108..109)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            101..112
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Region          127..171
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     CDS             1..504
                     /gene="Epb41l4a"
                     /gene_synonym="Epb4.1l4a"
                     /coded_by="NM_001437517.1:1610..3124"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:307514"
                     /db_xref="RGD:1306034"
ORIGIN      
        1 mgqapseael nylrtaksle mygvdlhpvy genkseyflg ltpvgvvvyk nkkqvgkyfw
       61 pritkvhfke tqfelrvlgk dcnetsfffe arsktackhl wkcsvehhtf frmpetesns
      121 lsrklskfgs isykhrysgr talqmsrdls iqlprpnqnv vrsrsktypk rvaqtqpags
      181 nsinrmtanl engenegttk iiapspvksf kkaknenspd pqrskshapw eengpqsgly
      241 nspsdrtksp kfpctrqrnl scgsdndssq pmrrrkahhs gedsdlkqrr rsrsrcntss
      301 gsesensnre hrkkrnrirq endmvdsapq weavlrrqke knqvdpnnrr srhrsrsrsp
      361 diqakeelwk hiqkelvdps glseeqlkei pytkvetqgd pvrirhshsp rsyrqyrrsq
      421 csdgersvls evnsktdlvp plpvtrssda qgsggstvhq rrngskdsli eeksqlsttn
      481 lagkhtakti ktiqaarlkt dvtg
//
LOCUS       NP_001424380             571 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 9 [Rattus
            norvegicus].
ACCESSION   NP_001424380 XP_063140191
VERSION     NP_001424380.1
DBSOURCE    REFSEQ: accession NM_001437451.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140191.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2984.1,
                                           SRR26360181.1869169.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..571
                     /product="testis-specific serine kinase substrate isoform
                     9"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=61441
     Region          26..571
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>219
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..571
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437451.1:60..1775"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kencrkvtrs vedaeiktnv
      181 lkqnsallee klrylqqqlq detprrqeae lqeleqklea glsrhglgpt tpiqgcsgpp
      241 gspeepprpr glpsngwgma iragegpsls eqelqkvssg leelrrevss laarwhqeeg
      301 avqealrllg glggrldgfl gqweraqreq aqsarglqel rgradelctm versavsvas
      361 lrselealgp vkpileelgr qlqnsrrgpd hvlnldrpaq gpcprcasqg qqlsteslqq
      421 lleraltplv devkqkglap acpscqrlhk kilpspvspa aptllspgag apglgqtrqg
      481 rgpelhpsag prrsrsgqep tadgqdeagv rteaegmggg ekvatldymh lkmcslhdql
      541 shlplegstg amgggstgga ppkrggpgse q
//
LOCUS       NP_001030167             479 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001030167 XP_001066493
VERSION     NP_001030167.1
DBSOURCE    REFSEQ: accession NM_001034995.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Sep 5, 2008 this sequence version replaced XP_001066493.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103648.1, SRR26360176.116176.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..479
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53976
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          218..276
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          305..361
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          394..461
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..479
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001034995.2:240..1679"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 msaedleaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrtta qassntelal ggaaaaaaas
      181 dvdqedsvde ravqdvesls sliqeildfn qdrqmkcfns klflcsicfc eklgsdcmyf
      241 lecrhvycka clkdyfeiqi kdgqvkclnc pepqcssvat pgqvkelvea dlfarydrll
      301 lqstldlmad vvycprpccq lpvmqepggt maicsscnfa fctlcrltyh gvspckvtae
      361 klidlrneyl qadeatkrfl eqrygkrviq kaleemeskd wleknskscp ccgtpiqkld
      421 gcnkmtctgc mqyfcwvcmg slsranpykh ftdpdspcfn rlfhavdvng diwedeied
//
LOCUS       NP_001424428            1665 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424428 XP_063140440
VERSION     NP_001424428.1
DBSOURCE    REFSEQ: accession NM_001437499.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1665)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1665)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1665)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1665)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1665)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1665)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1665)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1665)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1665)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1665)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140440.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.3340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1665
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1665
                     /product="tight junction protein ZO-1 isoform 7"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=186789
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <1092..1501
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1549..1655
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     CDS             1..1665
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437499.1:434..5431"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qvyrkepype emmrqnhilk qpalghpgqr ldkepnpayd
      961 pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf edrvptyedq wsyyddkqpy
     1021 ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd srpryeqlpr tstlrheeqp
     1081 tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq vpppgftskt ghyeplhgaa
     1141 vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp qsvltrvkmf enkrsaslen
     1201 kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk tlyrlpepqk pqakppediv
     1261 rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs epakpvhsqs qpnfssyssk
     1321 gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl snsslhihsk aaqsegnsvs
     1381 ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks fpdkasvnga eqtqktitpa
     1441 ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel sskpppspkt lmkahsstqp
     1501 pefdsgvetf svhtdkpkyq innistmpka vpvspsavee dededghtvv atargifnsn
     1561 ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp pldkekgetl lsplvmcgph
     1621 glkflkpvel rlphcdpktw qnkclpgdpn ylvgancvsv lidhf
//
LOCUS       NP_001424421            1765 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424421 XP_063140420
VERSION     NP_001424421.1
DBSOURCE    REFSEQ: accession NM_001437492.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1765)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1765)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1765)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1765)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1765)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1765)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1765)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1765)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1765)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1765)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140420.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2304236.1,
                                           SRR26643290.2199.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1765
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1765
                     /product="tight junction protein ZO-1 isoform 1"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=197018
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          825..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <959..1566
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1023..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1092..1585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1150..1370
                     /region_name="Actin-binding region (ABR).
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1633..1731
                     /region_name="ZU5"
                     /note="ZU5 domain; pfam00791"
                     /db_xref="CDD:459941"
     CDS             1..1765
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437492.1:434..5731"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qkaeasspvp ylspetnpas sasavkhnvn ltnvnleept
      961 papptshvsq adclgapspe aphtmlrdeg vslpshvdpa kvyrkepype emmrqnhilk
     1021 qpalghpgqr ldkepnpayd pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf
     1081 edrvptyedq wsyyddkqpy ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd
     1141 srpryeqlpr tstlrheeqp tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq
     1201 vpppgftskt ghyeplhgaa vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp
     1261 qsvltrvkmf enkrsaslen kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk
     1321 tlyrlpepqk pqakppediv rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs
     1381 epakpvhsqs qpnfssyssk gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl
     1441 snsslhihsk aaqsegnsvs ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks
     1501 fpdkasvnga eqtqktitpa ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel
     1561 sskpppspkt lmkahsstqp pefdsgvetf svhtdkpkyq innistmpka vpvspsavee
     1621 dededghtvv atargifnsn ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp
     1681 pldkekgetl lsplvmcgph glkflkpvel rlphcasmtp dgwsfalkss dsssgdpktw
     1741 qnkclpgdpn ylvgancvsv lidhf
//
LOCUS       NP_001424423            1745 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424423 XP_063140430
VERSION     NP_001424423.1
DBSOURCE    REFSEQ: accession NM_001437494.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1745)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1745)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1745)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1745)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1745)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1745)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1745)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1745)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1745)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1745)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140430.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.1918.1,
                                           SRR26643288.2692.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1745
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1745
                     /product="tight junction protein ZO-1 isoform 3"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=195018
     Region          22..108
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(33..39,57,60,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          102..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          186..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(186..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          296..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          422..501
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(432..438,448,451,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          517..581
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(517..519,547..549,554,557,576)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(519..525,538..539,542,557,565..566,574..576,
                     580..581)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(525,527,530,534,555..556,575,577..578)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          615..794
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          633..876
                     /region_name="Occludin (OCLN)-binding region.
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          825..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          <959..1566
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1023..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1092..1585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1150..1370
                     /region_name="Actin-binding region (ABR).
                     /evidence=ECO:0000250|UniProtKB:Q07157"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2K2P5.1)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39447; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07157; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2K2P5.1)"
     Region          1629..1735
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     CDS             1..1745
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437494.1:434..5671"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 msaraaaaks tameetaiwe qhtvtlhrap gfgfgiaisg grdnphfqsg etsivisdvl
       61 kggpaegqlq endrvamvng vsmdnvehaf avqqlrksgk nakitirrkk kvqipvshpd
      121 pdpvsdnedd sydedvhdpr sgrgalanrr gekswardrs asrdrslspr sdrrsvassq
      181 pakptkvtlv ksrkneeygl rlashifvke isqdslaard gniqegdvvl kingtvtenm
      241 sltdaktlie rskgklkmvv qrderatlln vpdlsdsihs anaserddis eiqslasdhs
      301 vrshdrpprr sqsrspdqrs epsdhstqsp qqpsngslrs reeermskpg avstpvkhvd
      361 dhtpkaveev tvekhekqtp tlpepkpvya qvgqpdvdlp vspsdgvlpn sthedgilrp
      421 smklvkfrkg dsvglrlagg ndvgifvagv ledspaakeg leegdqilrv nnvdftniir
      481 eeavlflldl pkgeevtila qkkkdvyrri vesdvgdsfy irthfeyeke spyglsfnkg
      541 evfrvvdtly ngklgswlai rigknhkeve rgivpnknra eqlasvqytl pktaggdrad
      601 fwrfrglrss krnlrksred lsaqpvqtkf payervvlre agflrpvtif gpiadvarek
      661 lareepdiyq iakseprdag tdhrssgiir lhtikqiidq dkhalldvtp navdrlnyaq
      721 wypivvflnp dskqgvktmr mrlcpesrks arklyershk lrknnhhlft ttinlnsmnd
      781 gwygalkeai qqqqnqlvwv segkadgats ddldlhddrl sylsapgsey smystdsrht
      841 sdyedtdteg gaytdqelde tlndevgtpp esaitrssep vredssgmhh enqtyppysp
      901 qaqpqaihri dspglktasq qkaeasspvp ylspetnpas sasavkhnvn ltnvnleept
      961 papptshvsq adclgapspe aphtmlrdeg vslpshvdpa kvyrkepype emmrqnhilk
     1021 qpalghpgqr ldkepnpayd pqlpyvekqa srdleqppyr yesssytdqf srnydhrlrf
     1081 edrvptyedq wsyyddkqpy ptrpfdtqhp rdldsrqhpe easergyfqr feepaplpyd
     1141 srpryeqlpr tstlrheeqp tsgyevhnry rpeaqpyapa gpkssepkqy fdqyprsyeq
     1201 vpppgftskt ghyeplhgaa vvpplipssq hkpevlpsat kpqppppalt eeeedpamkp
     1261 qsvltrvkmf enkrsaslen kkdvndtasf kppevaskpp saslvgpkpv sqtqfsehdk
     1321 tlyrlpepqk pqakppediv rsnhydpeed eeyyrkqlsy fdrrsfeskp pahipaghhs
     1381 epakpvhsqs qpnfssyssk gkpetdamdr sfsekrydpt qamppppplp sqysqpvppl
     1441 snsslhihsk aaqsegnsvs ldfqnsyisk pdpppsqskp atfrpptred ppqtfypqks
     1501 fpdkasvnga eqtqktitpa ynrftpkpyt ssarpferkf espkfnhnll psetvhkpel
     1561 sskpppspkt lmkahsstqp pefdsgvetf svhtdkpkyq innistmpka vpvspsavee
     1621 dededghtvv atargifnsn ggvlssietg vsiiipqgai pegieqeiyf kvcrdnsilp
     1681 pldkekgetl lsplvmcgph glkflkpvel rlphcdpktw qnkclpgdpn ylvgancvsv
     1741 lidhf
//
LOCUS       NP_001424373             610 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424373 XP_006229076
VERSION     NP_001424373.1
DBSOURCE    REFSEQ: accession NM_001437444.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229076.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..610
                     /product="testis-specific serine kinase substrate isoform
                     1"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=65185
     Region          48..610
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          142..>258
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..610
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437444.1:46..1878"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kgprpdvltq encrkvtrsv edaeiktnvl kqnsalleek lrylqqqlqd
      241 etprrqeael qeleqkleag lsrhglgptt piqgcsgppg speepprprg lpsngwgmai
      301 ragegpslse qelqkvssgl eelrrevssl aarwhqeega vqealrllgg lggrldgflg
      361 qweraqreqa qsarglqelr gradelctmv ersavsvasl rselealgpv kpileelgrq
      421 lqnsrrgpdh vlnldrpaqg pcprcasqgq qlsteslqql leraltplvd evkqkglapa
      481 cpscqrlhkk ilpspvspaa ptllspgaga pglgqtrqgr gpelhpsagp rrsrsgqept
      541 adgqdeagvr teaegmggge kvatldymhl kmcslhdqls hlplegstga mgggstggap
      601 pkrggpgseq
//
LOCUS       NP_612547                869 aa            linear   ROD 03-APR-2025
DEFINITION  dynamin-3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_612547
VERSION     NP_612547.1
DBSOURCE    REFSEQ: accession NM_138538.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Reubold,T.F., Faelber,K., Plattner,N., Posor,Y., Ketel,K.,
            Curth,U., Schlegel,J., Anand,R., Manstein,D.J., Noe,F., Haucke,V.,
            Daumke,O. and Eschenburg,S.
  TITLE     Crystal structure of the dynamin tetramer
  JOURNAL   Nature 525 (7569), 404-408 (2015)
   PUBMED   26302298
REFERENCE   2  (residues 1 to 869)
  AUTHORS   Li,J., Zhang,D.S., Ye,J.C., Li,C.M., Qi,M., Liang,D.D., Xu,X.R.,
            Xu,L., Liu,Y., Zhang,H., Zhang,Y.Y., Deng,F.F., Feng,J., Shi,D.,
            Chen,J.J., Li,L., Chen,G., Sun,Y.F., Peng,L.Y. and Chen,Y.H.
  TITLE     Dynamin-2 mediates heart failure by modulating Ca2+ -dependent
            cardiomyocyte apoptosis
  JOURNAL   Int J Cardiol 168 (3), 2109-2119 (2013)
   PUBMED   23410488
  REMARK    GeneRIF: DNM2 mediates HF by modulating Ca(2+)-dependent apoptotic
            death of cardiomyocyte.
REFERENCE   3  (residues 1 to 869)
  AUTHORS   Ikeuchi,Y., de la Torre-Ubieta,L., Matsuda,T., Steen,H., Okazawa,H.
            and Bonni,A.
  TITLE     The XLID protein PQBP1 and the GTPase Dynamin 2 define a signaling
            link that orchestrates ciliary morphogenesis in postmitotic neurons
  JOURNAL   Cell Rep 4 (5), 879-889 (2013)
   PUBMED   23994472
REFERENCE   4  (residues 1 to 869)
  AUTHORS   Grossman,G.H., Ebke,L.A., Beight,C.D., Jang,G.F., Crabb,J.W. and
            Hagstrom,S.A.
  TITLE     Protein partners of dynamin-1 in the retina
  JOURNAL   Vis Neurosci 30 (4), 129-139 (2013)
   PUBMED   23746204
REFERENCE   5  (residues 1 to 869)
  AUTHORS   Tanifuji,S., Funakoshi-Tago,M., Ueda,F., Kasahara,T. and Mochida,S.
  TITLE     Dynamin isoforms decode action potential firing for synaptic
            vesicle recycling
  JOURNAL   J Biol Chem 288 (26), 19050-19059 (2013)
   PUBMED   23687302
  REMARK    GeneRIF: dynamin isoforms select appropriate vesicle reuse pathways
            associated with specific neuronal firing patterns
REFERENCE   6  (residues 1 to 869)
  AUTHORS   Gray,N.W., Fourgeaud,L., Huang,B., Chen,J., Cao,H., Oswald,B.J.,
            Hemar,A. and McNiven,M.A.
  TITLE     Dynamin 3 is a component of the postsynapse, where it interacts
            with mGluR5 and Homer
  JOURNAL   Curr Biol 13 (6), 510-515 (2003)
   PUBMED   12646135
REFERENCE   7  (residues 1 to 869)
  AUTHORS   Zhang,Y., Moheban,D.B., Conway,B.R., Bhattacharyya,A. and
            Segal,R.A.
  TITLE     Cell surface Trk receptors mediate NGF-induced survival while
            internalized receptors regulate NGF-induced differentiation
  JOURNAL   J Neurosci 20 (15), 5671-5678 (2000)
   PUBMED   10908605
REFERENCE   8  (residues 1 to 869)
  AUTHORS   Cao,H., Garcia,F. and McNiven,M.A.
  TITLE     Differential distribution of dynamin isoforms in mammalian cells
  JOURNAL   Mol Biol Cell 9 (9), 2595-2609 (1998)
   PUBMED   9725914
REFERENCE   9  (residues 1 to 869)
  AUTHORS   Cook,T., Mesa,K. and Urrutia,R.
  TITLE     Three dynamin-encoding genes are differentially expressed in
            developing rat brain
  JOURNAL   J Neurochem 67 (3), 927-931 (1996)
   PUBMED   8752097
REFERENCE   10 (residues 1 to 869)
  AUTHORS   Nakata,T., Takemura,R. and Hirokawa,N.
  TITLE     A novel member of the dynamin family of GTP-binding proteins is
            expressed specifically in the testis
  JOURNAL   J Cell Sci 105 (Pt 1), 1-5 (1993)
   PUBMED   8360266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF201839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..869
                     /product="dynamin-3 isoform 1"
                     /EC_number="3.6.5.5"
                     /note="T-dynamin; dynamin, testicular; testicular dynamin"
                     /calculated_mol_wt=97784
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          526..635
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(526,528..529,531,548,617..618,621,624..625,628)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          655..745
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          752..869
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Region          <753..841
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     CDS             1..869
                     /gene="Dnm3"
                     /gene_synonym="dynamin-2"
                     /coded_by="NM_138538.3:172..2781"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171574"
                     /db_xref="RGD:727949"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqgtnlp psrqivirkg wltvsnigim
      541 kggskgywfv ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr
      601 nvykdyrsle lacdsqedvd swkasllrag vypdksften dengqaenfs mdpqlerqve
      661 tirnlvdsym siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesve
      721 qaqrrdemlr myqalkeala iigdintvtv stpapppvdd swlqhsrrsp ppspttqrrl
      781 tlsaplprpa ssrgpapaip spgphsgapp vpfrpgplpp fpnssdsyga ppqvpsrptr
      841 appsvpsrrp ppsptrptii rplesslld
//
LOCUS       NP_001424389             301 aa            linear   ROD 03-APR-2025
DEFINITION  nitric oxide synthase-interacting protein [Rattus norvegicus].
ACCESSION   NP_001424389 XP_063140242
VERSION     NP_001424389.1
DBSOURCE    REFSEQ: accession NM_001437460.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Yu,X., Zhong,Y., Zhu,Z., Wu,T., Shen,A. and Huang,Y.
  TITLE     Increased expression of nitric oxide synthase interacting protein
            (NOSIP) following traumatic spinal cord injury in rats
  JOURNAL   J Mol Histol 43 (6), 661-668 (2012)
   PUBMED   23135205
  REMARK    GeneRIF: Data suggested that NOSIP may play an important roles in
            astrogliogenesis after a spinal cord injury.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dreyer,J., Schleicher,M., Tappe,A., Schilling,K., Kuner,T.,
            Kusumawidijaja,G., Muller-Esterl,W., Oess,S. and Kuner,R.
  TITLE     Nitric oxide synthase (NOS)-interacting protein interacts with
            neuronal NOS and regulates its distribution and activity
  JOURNAL   J Neurosci 24 (46), 10454-10465 (2004)
   PUBMED   15548660
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Dedio,J., Konig,P., Wohlfart,P., Schroeder,C., Kummer,W. and
            Muller-Esterl,W.
  TITLE     NOSIP, a novel modulator of endothelial nitric oxide synthase
            activity
  JOURNAL   FASEB J 15 (1), 79-89 (2001)
   PUBMED   11149895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140242.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3041.1,
                                           SRR26643286.1537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..301
                     /product="nitric oxide synthase-interacting protein"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=33126
     Region          4..78
                     /region_name="zf-NOSIP"
                     /note="Zinc-finger of nitric oxide synthase-interacting
                     protein; pfam15906"
                     /db_xref="CDD:318178"
     Region          220..287
                     /region_name="RING-Ubox2_NOSIP"
                     /note="U-box domain 2, a modified RING finger, found in
                     nitric oxide synthase-interacting protein (NOSIP) and
                     similar proteins; cd16662"
                     /db_xref="CDD:438324"
     CDS             1..301
                     /gene="Nosip"
                     /coded_by="NM_001437460.1:223..1128"
                     /db_xref="GeneID:292894"
                     /db_xref="RGD:1309992"
ORIGIN      
        1 mtrhgkncta gavytyhekk kdtaasgygt qnirlsrdav kdfdccclsl qpchdpvvtp
       61 dgylyereai leyilhqkre iarqmkayek qrgarreeqk elqraaaqdq vrgflekesa
      121 ivsrplnpfm pkaatlpntd geqpgpsvgp lgkdkdkalp sfwipsltpe akatklekps
      181 rtvtcpmsgk plrmsdltsv rftqlddsvd rvglitrser yvcavtrdsl snatpcavlr
      241 psgavvtlec veklirkdmv dpvngdtlte rdiivlqrgg tgfagsgvkl qaemsrpvmq
      301 a
//
LOCUS       NP_001424381             555 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 10 [Rattus
            norvegicus].
ACCESSION   NP_001424381 XP_063140205
VERSION     NP_001424381.1
DBSOURCE    REFSEQ: accession NM_001437452.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140205.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1155523.1,
                                           SRR26360181.2546591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..555
                     /product="testis-specific serine kinase substrate isoform
                     10"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=60622
     Region          26..555
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>228
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..555
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437452.1:60..1727"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kgprpdvltq encrkvtrsv
      181 edaeiktnvl kqnsalleek lrylqqqlqd etprrqeael qeleqkleag lsrhglgptt
      241 piqgcsgppg speepprprg lpsngwgmai ragegpslse qelqkvssgl eelrrevssl
      301 aarwhqeega vqealrllgg lggrldgflg qweraqreqa qsarglqelr gradelctmv
      361 ersavsvasl rselealgpv kpileelgrq lqnsrrgpdh vlnldrpaqg pcprcasqgq
      421 qlsteslqql leraltplvd evkqkglapa cpscqrlhkk ilelerqala khvraealss
      481 tlrlaqdeav raknllltdk mkpeekvatl dymhlkmcsl hdqlshlple gstgamgggs
      541 tggappkrgg pgseq
//
LOCUS       NP_001424413             541 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 655 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424413 XP_006248957
VERSION     NP_001424413.1
DBSOURCE    REFSEQ: accession NM_001437484.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Houlard,M., Romero-Portillo,F., Germani,A., Depaux,A.,
            Regnier-Ricard,F., Gisselbrecht,S. and Varin-Blank,N.
  TITLE     Characterization of VIK-1: a new Vav-interacting Kruppel-like
            protein
  JOURNAL   Oncogene 24 (1), 28-38 (2005)
   PUBMED   15558030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006248957.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.42338.1,
                                           SRR26643299.49489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN16676787
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..541
                     /product="zinc finger protein 655 isoform 2"
                     /note="vav-1 interacting Kruppel-like protein; zinc finger
                     protein 205-like"
                     /calculated_mol_wt=63469
     Region          237..>527
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(250,252,254,256..257,260..261,264,313,315,319..320,
                     323..324,327,341,343,345,347..348,351..352,355)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          273..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          363..383
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(368,370,372,374..375,378..379,382,418,420,424..425,
                     428..429,432,446,448,450,452..453,456..457,460)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..541
                     /gene="Zfp655"
                     /gene_synonym="RGD1309158; Znf655"
                     /coded_by="NM_001437484.1:116..1741"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:360764"
                     /db_xref="RGD:1309158"
ORIGIN      
        1 meeitsqeaa esprvqfqsl esqseclspe lrflrdteme qgytdgfpis kpdgisqreq
       61 dlqvfdletq nregvrndcs dgetreenkl lipkrkisee vhsykvrvgk fkqdiaqvpe
      121 treayksedr lerlqeilrk flflerefrq itiskktfsn ekntepeksf sldstldtdq
      181 rvlriqtidd skydmnfnqn pavgeqepin ltenfqntdy keslmdlshl nkwesmpttd
      241 rsykcdtcgk tfhqasaltr hqrihtrekp ykckeceksf sqssslsrhk rihtreksyr
      301 ceasdkscda sdkscsqssd vlqhkkvhak aksykcgtce rvfsrsvhlt qhqrthkdta
      361 ckctvcgsdf chtsylvehq rlhhqeksye ydecglayvk qqgirfrekp yscnecgkdf
      421 rlnshlvqhq rihtgeklhe cnergkafsq tsclsqhhkm hrkeksyeyn nyeesfshns
      481 dltlqqevpi rervfdcdaw eenfsqrahl ipherahtke kpyecnelge tfsqvqasfn
      541 m
//
LOCUS       NP_954519                585 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_954519 XP_214920
VERSION     NP_954519.1
DBSOURCE    REFSEQ: accession NM_199088.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 1, 2004 this sequence version replaced XP_214920.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY346104.1, SRR26360181.1919480.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..585
                     /product="testis-specific serine kinase substrate isoform
                     3"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=63401
     Region          48..585
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>258
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          262..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          559..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..585
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_199088.2:46..1803"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kgprpdvltq encrkvtrsv edaeiktnvl kqnsalleek lrylqqqlqd
      241 etprrqeael qeleqkleag lsrhglgptt piqgcsgppg speepprprg lpsngwgmai
      301 ragegpslse qelqkvssgl eelrrevssl aarwhqeega vqealrllgg lggrldgflg
      361 qweraqreqa qsarglqelr gradelctmv ersavsvasl rselealgpv kpileelgrq
      421 lqnsrrgpdh vlnldrpaqg pcprcasqgq qlsteslqql leraltplvd evkqkglapa
      481 cpscqrlhkk ilelerqala khvraealss tlrlaqdeav raknllltdk mkpeekvatl
      541 dymhlkmcsl hdqlshlple gstgamgggs tggappkrgg pgseq
//
LOCUS       NP_001424461             353 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424461 XP_006254701
VERSION     NP_001424461.1
DBSOURCE    REFSEQ: accession NM_001437532.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254701.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.37625.1,
                                           SRR26643285.52071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..353
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=39762
     Region          92..150
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          179..235
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          268..335
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..353
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437532.1:773..1834"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 mqflkeetlt ylnivspfel kmgsqkkvqr rttaqassnt elalggaaaa aaasdvdqed
       61 svderavqdv eslssliqei ldfnqdrqmk cfnsklflcs icfceklgsd cmyflecrhv
      121 yckaclkdyf eiqikdgqvk clncpepqcs svatpgqvke lveadlfary drlllqstld
      181 lmadvvycpr pccqlpvmqe pggtmaicss cnfafctlcr ltyhgvspck vtaeklidlr
      241 neylqadeat krfleqrygk rviqkaleem eskdwlekns kscpccgtpi qkldgcnkmt
      301 ctgcmqyfcw vcmgslsran pykhftdpds pcfnrlfhav dvngdiwede ied
//
LOCUS       NP_001424455             368 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 24 [Rattus norvegicus].
ACCESSION   NP_001424455 XP_006254527
VERSION     NP_001424455.1
DBSOURCE    REFSEQ: accession NM_001437526.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Howng,S.Y., Avila,R.L., Emery,B., Traka,M., Lin,W., Watkins,T.,
            Cook,S., Bronson,R., Davisson,M., Barres,B.A. and Popko,B.
  TITLE     ZFP191 is required by oligodendrocytes for CNS myelination
  JOURNAL   Genes Dev 24 (3), 301-311 (2010)
   PUBMED   20080941
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Wang,H., Sun,R., Liu,G., Yao,M., Fei,J. and Shen,H.
  TITLE     Characterization of the target DNA sequence for the DNA-binding
            domain of zinc finger protein 191
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 40 (8), 704-710 (2008)
   PUBMED   18685786
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254527.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.76373.1,
                                           SRR26360186.2712890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN12840121
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..368
                     /product="zinc finger protein 24"
                     /note="zfp-191; zinc finger protein 191"
                     /calculated_mol_wt=41779
     Region          48..159
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          <249..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          251..301
                     /region_name="Necessary and sufficient for nuclear
                     localization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          305..>358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..368
                     /gene="Zfp24"
                     /gene_synonym="Zfp191; Znf24"
                     /coded_by="NM_001437526.1:297..1403"
                     /db_xref="GeneID:360204"
                     /db_xref="RGD:727963"
ORIGIN      
        1 msaqsveeds iliipnpdee ekilrvklee dpdgeegssi swnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailprelqt lvrehhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lveeiasqed aqglpsseld avenqlkwas
      181 welhslrhcd ddataengal apkqeiasag eshevpgtln igvpqifkyg etcfpkgrfe
      241 rkrnpsrkkq hicdecgkhf sqgsalilhq rihsgekpyg cvecgkafsr ssilvqhqrv
      301 htgekpykcl ecgkafsqns glinhqriht gekpyecvqc gksysqssnl frhqrrhnae
      361 kllnvvkv
//
LOCUS       NP_001424451             848 aa            linear   ROD 03-APR-2025
DEFINITION  dynamin-3 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424451 XP_063128085
VERSION     NP_001424451.1
DBSOURCE    REFSEQ: accession NM_001437522.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Reubold,T.F., Faelber,K., Plattner,N., Posor,Y., Ketel,K.,
            Curth,U., Schlegel,J., Anand,R., Manstein,D.J., Noe,F., Haucke,V.,
            Daumke,O. and Eschenburg,S.
  TITLE     Crystal structure of the dynamin tetramer
  JOURNAL   Nature 525 (7569), 404-408 (2015)
   PUBMED   26302298
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Li,J., Zhang,D.S., Ye,J.C., Li,C.M., Qi,M., Liang,D.D., Xu,X.R.,
            Xu,L., Liu,Y., Zhang,H., Zhang,Y.Y., Deng,F.F., Feng,J., Shi,D.,
            Chen,J.J., Li,L., Chen,G., Sun,Y.F., Peng,L.Y. and Chen,Y.H.
  TITLE     Dynamin-2 mediates heart failure by modulating Ca2+ -dependent
            cardiomyocyte apoptosis
  JOURNAL   Int J Cardiol 168 (3), 2109-2119 (2013)
   PUBMED   23410488
  REMARK    GeneRIF: DNM2 mediates HF by modulating Ca(2+)-dependent apoptotic
            death of cardiomyocyte.
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Ikeuchi,Y., de la Torre-Ubieta,L., Matsuda,T., Steen,H., Okazawa,H.
            and Bonni,A.
  TITLE     The XLID protein PQBP1 and the GTPase Dynamin 2 define a signaling
            link that orchestrates ciliary morphogenesis in postmitotic neurons
  JOURNAL   Cell Rep 4 (5), 879-889 (2013)
   PUBMED   23994472
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Grossman,G.H., Ebke,L.A., Beight,C.D., Jang,G.F., Crabb,J.W. and
            Hagstrom,S.A.
  TITLE     Protein partners of dynamin-1 in the retina
  JOURNAL   Vis Neurosci 30 (4), 129-139 (2013)
   PUBMED   23746204
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Tanifuji,S., Funakoshi-Tago,M., Ueda,F., Kasahara,T. and Mochida,S.
  TITLE     Dynamin isoforms decode action potential firing for synaptic
            vesicle recycling
  JOURNAL   J Biol Chem 288 (26), 19050-19059 (2013)
   PUBMED   23687302
  REMARK    GeneRIF: dynamin isoforms select appropriate vesicle reuse pathways
            associated with specific neuronal firing patterns
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Gray,N.W., Fourgeaud,L., Huang,B., Chen,J., Cao,H., Oswald,B.J.,
            Hemar,A. and McNiven,M.A.
  TITLE     Dynamin 3 is a component of the postsynapse, where it interacts
            with mGluR5 and Homer
  JOURNAL   Curr Biol 13 (6), 510-515 (2003)
   PUBMED   12646135
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Zhang,Y., Moheban,D.B., Conway,B.R., Bhattacharyya,A. and
            Segal,R.A.
  TITLE     Cell surface Trk receptors mediate NGF-induced survival while
            internalized receptors regulate NGF-induced differentiation
  JOURNAL   J Neurosci 20 (15), 5671-5678 (2000)
   PUBMED   10908605
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Cao,H., Garcia,F. and McNiven,M.A.
  TITLE     Differential distribution of dynamin isoforms in mammalian cells
  JOURNAL   Mol Biol Cell 9 (9), 2595-2609 (1998)
   PUBMED   9725914
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Cook,T., Mesa,K. and Urrutia,R.
  TITLE     Three dynamin-encoding genes are differentially expressed in
            developing rat brain
  JOURNAL   J Neurochem 67 (3), 927-931 (1996)
   PUBMED   8752097
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Nakata,T., Takemura,R. and Hirokawa,N.
  TITLE     A novel member of the dynamin family of GTP-binding proteins is
            expressed specifically in the testis
  JOURNAL   J Cell Sci 105 (Pt 1), 1-5 (1993)
   PUBMED   8360266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063128085.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.42632.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..848
                     /product="dynamin-3 isoform 5"
                     /EC_number="3.6.5.5"
                     /note="T-dynamin; dynamin, testicular; testicular dynamin"
                     /calculated_mol_wt=95420
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          514..625
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(516,518..519,521,538,607..608,611,614..615,618)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          645..735
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          <743..829
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     CDS             1..848
                     /gene="Dnm3"
                     /gene_synonym="dynamin-2"
                     /coded_by="NM_001437522.1:172..2718"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:171574"
                     /db_xref="RGD:727949"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqvirkg wltvsnigim kggskgywfv
      541 ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr nvykdyrsle
      601 lacdsqedvd swkasllrag vypdksften dengqaenfs mdpqlerqve tirnlvdsym
      661 siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesve qaqrrdemlr
      721 myqalkeala iigdintvtv stpapppvdd swlqhsrrsp ppspttqrrl tlsaplprpa
      781 ssrgpapaip spgphsgapp vpfrpgplpp fpnssdsyga ppqvpsrptr appsvprrpp
      841 pavpgrps
//
LOCUS       NP_001424376             573 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001424376 XP_006229080
VERSION     NP_001424376.1
DBSOURCE    REFSEQ: accession NM_001437447.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229080.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2994.1,
                                           SRR26360181.1016221.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..573
                     /product="testis-specific serine kinase substrate isoform
                     5"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=61634
     Region          48..>492
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>258
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          262..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..573
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437447.1:46..1767"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kgprpdvltq encrkvtrsv edaeiktnvl kqnsalleek lrylqqqlqd
      241 etprrqeael qeleqkleag lsrhglgptt piqgcsgppg speepprprg lpsngwgmai
      301 ragegpslse qelqkvssgl eelrrevssl aarwhqeega vqealrllgg lggrldgflg
      361 qweraqreqa qsarglqelr gradelctmv ersavsvasl rselealgpv kpileelgrq
      421 lqnsrrgpdh vlnldrpaqg pcprcasqgq qlsteslqql leraltplvd evkqkglapa
      481 cpscqrlhkk ilpspvspaa ptllspgaga pglgqtrqgr gpelhpsagp rrsrsgqept
      541 adgqdeagge gghfglyafe dvfpprptqp pat
//
LOCUS       NP_001424434            1031 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 532 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424434
VERSION     NP_001424434.1
DBSOURCE    REFSEQ: accession NM_001437505.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.497092.1,
                                           SRR21887622.497091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..1031
                     /product="zinc finger protein 532 isoform 2"
                     /calculated_mol_wt=110457
     Region          753..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(758,760,762,764..765,768..769,791,793,797..798,
                     801..802,805,824,826,828,830..831,834..835)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          786..807
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          816..836
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          906..926
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(911,913,915,917..918,921..922,925,940,942,946..947,
                     950..951,955,1001,1003,1005,1007..1008,1011..1012,1015)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          931..957
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          935..956
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          995..1016
                     /region_name="zf-C2H2_6"
                     /note="C2H2-type zinc finger; pfam13912"
                     /db_xref="CDD:433576"
     Region          996..1016
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1031
                     /gene="Zfp532"
                     /gene_synonym="Znf532"
                     /coded_by="NM_001437505.1:476..3571"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307362"
                     /db_xref="RGD:1311719"
ORIGIN      
        1 mtmgdmktpd fddllaafdi pdmvdpkaai esghddhesh ikqnahvddd shtpsssdvg
       61 vsvivknvrn idssegvekd ghnptgnglh ngfltassld sygkdgaksl kgdtpasevt
      121 lkdpafsqfs pissaeefed dekievddpp dkeetranfr snvltgsapq qdfdklkalg
      181 gentsktgvs asghadknkv kreaesnsit lsvyepfkvr kaedklkens ekmlesrvld
      241 gkpssekndp aiaaatsskt ksssklssci aaiaalsakk aasdsckepv ansreasplp
      301 kevndspkaa dkspesqnli dgtkkaslkp sdsprsvsse nsskgspssp vgstpaipkv
      361 riktiktssg eikrtvtrvl pevdldsgkk pseqaasvma svtsllsssa saavlssppr
      421 aplptamvts avssaeltpk qvtikpvata flpvsavkta gsqvinlkla nnttvkatvi
      481 saasvqsass aiikaanaiq qqtvvvpass lanaklvpkt vhlanlnllp qgaqatselr
      541 qvltkpqqqi kqailnaaaa qppkkvsrvq vvsslqssvv eafnkvlssv npvpvyipnl
      601 sppasagitl pmrgykclec gdsfaleksl sqhydrrsvr ievtcnhctk nlvfynkcsl
      661 lsharghkek gvvmqcshli lkpvpadqmi vspssntaas tlpssvgaat htvakvqpgl
      721 tgavisapps tpispampld edpsklcrhs lkclecnevf qdetslathf qhaadtcgqq
      781 mkkhpcrqcd ksfssshslc rhnrikhkgi rkvyacshcp dsrrtftkrl mlekhiqlmh
      841 gikdpdvkel sdevtneeev eikedakvps pkrkleepvl efrpprgait qplkklkinv
      901 fkvhkcavcg fttenllqfh ehipqhksdg ssyqcrecgl cytshvslsr hlfivhklke
      961 pqpvskqnga gedsqqenkp spedeaaega vsdrkckvca ktfeteaaln thmrthgmaf
     1021 ikskrmssae k
//
LOCUS       NP_001424425            1673 aa            linear   ROD 03-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424425
VERSION     NP_001424425.1
DBSOURCE    REFSEQ: accession NM_001437496.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1673)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1673)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1673)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1673)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1673)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1673)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1673)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1673)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1673)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1673)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.315137.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1673
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1673
                     /product="tight junction protein ZO-1 isoform 5"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=187671
     Region          10..96
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(21..27,45,48,76,80,83..84)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          174..251
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(174..179,184..200,203..205,208,210..211,218,
                     226..227,229..230,242..248)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(185..191,197,200,230,234,237..238)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          410..489
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(420..426,436,439,468,472,475..476)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          505..569
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(505..507,535..537,542,545,564)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(507..513,526..527,530,545,553..554,562..564,
                     568..569)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(513,515,518,522,543..544,563,565..566)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          603..782
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Region          <1080..1489
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1541..1639
                     /region_name="ZU5"
                     /note="ZU5 domain; pfam00791"
                     /db_xref="CDD:459941"
     CDS             1..1673
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437496.1:119..5140"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 meetaiweqh tvtlhrapgf gfgiaisggr dnphfqsget sivisdvlkg gpaegqlqen
       61 drvamvngvs mdnvehafav qqlrksgkna kitirrkkkv qipvshpdpd pvsdneddsy
      121 dedvhdprsg rgalanrrge kswardrsas rdrslsprsd rrsvassqpa kptkvtlvks
      181 rkneeyglrl ashifvkeis qdslaardgn iqegdvvlki ngtvtenmsl tdaktliers
      241 kgklkmvvqr deratllnvp dlsdsihsan aserddisei qslasdhsvr shdrpprrsq
      301 srspdqrsep sdhstqspqq psngslrsre eermskpgav stpvkhvddh tpkaveevtv
      361 ekhekqtptl pepkpvyaqv gqpdvdlpvs psdgvlpnst hedgilrpsm klvkfrkgds
      421 vglrlaggnd vgifvagvle dspaakegle egdqilrvnn vdftniiree avlflldlpk
      481 geevtilaqk kkdvyrrive sdvgdsfyir thfeyekesp yglsfnkgev frvvdtlyng
      541 klgswlairi gknhkeverg ivpnknraeq lasvqytlpk taggdradfw rfrglrsskr
      601 nlrksredls aqpvqtkfpa yervvlreag flrpvtifgp iadvarekla reepdiyqia
      661 kseprdagtd hrssgiirlh tikqiidqdk halldvtpna vdrlnyaqwy pivvflnpds
      721 kqgvktmrmr lcpesrksar klyershklr knnhhlfttt inlnsmndgw ygalkeaiqq
      781 qqnqlvwvse gkadgatsdd ldlhddrlsy lsapgseysm ystdsrhtsd yedtdtegga
      841 ytdqeldetl ndevgtppes aitrssepvr edssgmhhen qtyppyspqa qpqaihrids
      901 pglktasqqv yrkepypeem mrqnhilkqp alghpgqrld kepnpaydpq lpyvekqasr
      961 dleqppyrye sssytdqfsr nydhrlrfed rvptyedqws yyddkqpypt rpfdtqhprd
     1021 ldsrqhpeea sergyfqrfe epaplpydsr pryeqlprts tlrheeqpts gyevhnryrp
     1081 eaqpyapagp kssepkqyfd qyprsyeqvp ppgftsktgh yeplhgaavv pplipssqhk
     1141 pevlpsatkp qppppaltee eedpamkpqs vltrvkmfen krsaslenkk dvndtasfkp
     1201 pevaskppsa slvgpkpvsq tqfsehdktl yrlpepqkpq akppedivrs nhydpeedee
     1261 yyrkqlsyfd rrsfeskppa hipaghhsep akpvhsqsqp nfssysskgk petdamdrsf
     1321 sekrydptqa mppppplpsq ysqpvpplsn sslhihskaa qsegnsvsld fqnsyiskpd
     1381 pppsqskpat frpptredpp qtfypqksfp dkasvngaeq tqktitpayn rftpkpytss
     1441 arpferkfes pkfnhnllps etvhkpelss kpppspktlm kahsstqppe fdsgvetfsv
     1501 htdkpkyqin nistmpkavp vspsaveede dedghtvvat argifnsngg vlssietgvs
     1561 iiipqgaipe gieqeiyfkv crdnsilppl dkekgetlls plvmcgphgl kflkpvelrl
     1621 phcasmtpdg wsfalkssds ssgdpktwqn kclpgdpnyl vgancvsvli dhf
//
LOCUS       NP_001424435            1031 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 532 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424435
VERSION     NP_001424435.1
DBSOURCE    REFSEQ: accession NM_001437506.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.853446.1,
                                           SRR26360194.853551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..1031
                     /product="zinc finger protein 532 isoform 2"
                     /calculated_mol_wt=110457
     Region          753..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(758,760,762,764..765,768..769,791,793,797..798,
                     801..802,805,824,826,828,830..831,834..835)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          786..807
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          816..836
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          906..926
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(911,913,915,917..918,921..922,925,940,942,946..947,
                     950..951,955,1001,1003,1005,1007..1008,1011..1012,1015)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          931..957
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          935..956
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          995..1016
                     /region_name="zf-C2H2_6"
                     /note="C2H2-type zinc finger; pfam13912"
                     /db_xref="CDD:433576"
     Region          996..1016
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1031
                     /gene="Zfp532"
                     /gene_synonym="Znf532"
                     /coded_by="NM_001437506.1:247..3342"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:307362"
                     /db_xref="RGD:1311719"
ORIGIN      
        1 mtmgdmktpd fddllaafdi pdmvdpkaai esghddhesh ikqnahvddd shtpsssdvg
       61 vsvivknvrn idssegvekd ghnptgnglh ngfltassld sygkdgaksl kgdtpasevt
      121 lkdpafsqfs pissaeefed dekievddpp dkeetranfr snvltgsapq qdfdklkalg
      181 gentsktgvs asghadknkv kreaesnsit lsvyepfkvr kaedklkens ekmlesrvld
      241 gkpssekndp aiaaatsskt ksssklssci aaiaalsakk aasdsckepv ansreasplp
      301 kevndspkaa dkspesqnli dgtkkaslkp sdsprsvsse nsskgspssp vgstpaipkv
      361 riktiktssg eikrtvtrvl pevdldsgkk pseqaasvma svtsllsssa saavlssppr
      421 aplptamvts avssaeltpk qvtikpvata flpvsavkta gsqvinlkla nnttvkatvi
      481 saasvqsass aiikaanaiq qqtvvvpass lanaklvpkt vhlanlnllp qgaqatselr
      541 qvltkpqqqi kqailnaaaa qppkkvsrvq vvsslqssvv eafnkvlssv npvpvyipnl
      601 sppasagitl pmrgykclec gdsfaleksl sqhydrrsvr ievtcnhctk nlvfynkcsl
      661 lsharghkek gvvmqcshli lkpvpadqmi vspssntaas tlpssvgaat htvakvqpgl
      721 tgavisapps tpispampld edpsklcrhs lkclecnevf qdetslathf qhaadtcgqq
      781 mkkhpcrqcd ksfssshslc rhnrikhkgi rkvyacshcp dsrrtftkrl mlekhiqlmh
      841 gikdpdvkel sdevtneeev eikedakvps pkrkleepvl efrpprgait qplkklkinv
      901 fkvhkcavcg fttenllqfh ehipqhksdg ssyqcrecgl cytshvslsr hlfivhklke
      961 pqpvskqnga gedsqqenkp spedeaaega vsdrkckvca ktfeteaaln thmrthgmaf
     1021 ikskrmssae k
//
LOCUS       NP_001009682             511 aa            linear   ROD 03-APR-2025
DEFINITION  2'-5'-oligoadenylate synthase-like protein 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001009682 XP_222236
VERSION     NP_001009682.1
DBSOURCE    REFSEQ: accession NM_001009682.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Perelygin,A.A., Zharkikh,A.A., Scherbik,S.V. and Brinton,M.A.
  TITLE     The mammalian 2'-5' oligoadenylate synthetase gene family: evidence
            for concerted evolution of paralogous Oas1 genes in Rodentia and
            Artiodactyla
  JOURNAL   J Mol Evol 63 (4), 562-576 (2006)
   PUBMED   17024523
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jan 13, 2005 this sequence version replaced XP_222236.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY237116.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..511
                     /product="2'-5'-oligoadenylate synthase-like protein 2
                     isoform 1"
                     /EC_number="2.7.7.84"
                     /note="54 kDa 2'-5'-oligoadenylate synthase-like protein
                     2"
                     /calculated_mol_wt=59275
     Region          29..214
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(67..69,72,74..76,81,83,126..127,137,154,200,204,207)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(68..69,81,83,127,200,204,207)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(81,83,154)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          170..347
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     Region          359..432
                     /region_name="Ubl1_OASL"
                     /note="ubiquitin-like (Ubl) domain 1 found in
                     2'-5'-oligoadenylate synthase-like protein (OASL) and
                     similar proteins; cd01811"
                     /db_xref="CDD:340509"
     Region          438..509
                     /region_name="Ubl2_OASL"
                     /note="ubiquitin-like (Ubl) domain 2 found in
                     2'-5'-oligoadenylate synthase-like protein (OASL) and
                     similar proteins; cd16103"
                     /db_xref="CDD:340520"
     CDS             1..511
                     /gene="Oasl2"
                     /coded_by="NM_001009682.2:101..1636"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304549"
                     /db_xref="RGD:1307351"
ORIGIN      
        1 mdtlpdlygt vgdsldyfle hslqpqrdwk eegkdaweri erffrekcfc dellldqevr
       61 vlkvvkggss gkgtalnhrs dqdmilflsc fssfkqqard rkavidfiks klihcrksla
      121 ynitvrqhke gkrtprsltl eiqsrksndi icmdilpayn algsfsrdck pepeiyenli
      181 rckgypgdfs psfaelqrhf vksrpvklkn llrlvkfwhl kylrhkyrra vlpskyalel
      241 ltiyawemgt dssdnfnlde gfvavmellr dyqdiciywt kyydfqnevv rnflkeqlkg
      301 drpiildpad ptnnlgrrgk welvakeaty cllqlccvta drwnvqvsia hylrgardvq
      361 vtvkqtgree willtnphsp irklkakikk rmnlcgelri sfqepggerq plsgrktlsd
      421 ygifskvnir vmetfppeiq vfvrypggqn kpfaidpdat ilslwekiee dggpctedwv
      481 llfegeeldd ddnlaelqik dcdtiqlsrv s
//
LOCUS       NP_001424409             913 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424409 XP_063133377
VERSION     NP_001424409.1
DBSOURCE    REFSEQ: accession NM_001437480.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133377.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1223926.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..913
                     /product="synphilin-1 isoform 2"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=99755
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..913
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437480.1:368..3109"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaa
//
LOCUS       NP_001008363             541 aa            linear   ROD 03-APR-2025
DEFINITION  zinc finger protein 655 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001008363 XP_341035
VERSION     NP_001008363.1
DBSOURCE    REFSEQ: accession NM_001008362.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Houlard,M., Romero-Portillo,F., Germani,A., Depaux,A.,
            Regnier-Ricard,F., Gisselbrecht,S. and Varin-Blank,N.
  TITLE     Characterization of VIK-1: a new Vav-interacting Kruppel-like
            protein
  JOURNAL   Oncogene 24 (1), 28-38 (2005)
   PUBMED   15558030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Dec 16, 2004 this sequence version replaced XP_341035.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085937.1, SRR26643297.39250.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..541
                     /product="zinc finger protein 655 isoform 2"
                     /note="vav-1 interacting Kruppel-like protein; zinc finger
                     protein 205-like"
                     /calculated_mol_wt=63469
     Region          237..>527
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(250,252,254,256..257,260..261,264,313,315,319..320,
                     323..324,327,341,343,345,347..348,351..352,355)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          273..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          363..383
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(368,370,372,374..375,378..379,382,418,420,424..425,
                     428..429,432,446,448,450,452..453,456..457,460)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..541
                     /gene="Zfp655"
                     /gene_synonym="RGD1309158; Znf655"
                     /coded_by="NM_001008362.2:91..1716"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360764"
                     /db_xref="RGD:1309158"
ORIGIN      
        1 meeitsqeaa esprvqfqsl esqseclspe lrflrdteme qgytdgfpis kpdgisqreq
       61 dlqvfdletq nregvrndcs dgetreenkl lipkrkisee vhsykvrvgk fkqdiaqvpe
      121 treayksedr lerlqeilrk flflerefrq itiskktfsn ekntepeksf sldstldtdq
      181 rvlriqtidd skydmnfnqn pavgeqepin ltenfqntdy keslmdlshl nkwesmpttd
      241 rsykcdtcgk tfhqasaltr hqrihtrekp ykckeceksf sqssslsrhk rihtreksyr
      301 ceasdkscda sdkscsqssd vlqhkkvhak aksykcgtce rvfsrsvhlt qhqrthkdta
      361 ckctvcgsdf chtsylvehq rlhhqeksye ydecglayvk qqgirfrekp yscnecgkdf
      421 rlnshlvqhq rihtgeklhe cnergkafsq tsclsqhhkm hrkeksyeyn nyeesfshns
      481 dltlqqevpi rervfdcdaw eenfsqrahl ipherahtke kpyecnelge tfsqvqasfn
      541 m
//
LOCUS       NP_001424374             601 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424374 XP_006229077
VERSION     NP_001424374.1
DBSOURCE    REFSEQ: accession NM_001437445.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229077.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2871944.1,
                                           SRR26643293.2999.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..601
                     /product="testis-specific serine kinase substrate isoform
                     2"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=64220
     Region          48..601
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          142..>249
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..601
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437445.1:46..1851"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kencrkvtrs vedaeiktnv lkqnsallee klrylqqqlq detprrqeae
      241 lqeleqklea glsrhglgpt tpiqgcsgpp gspeepprpr glpsngwgma iragegpsls
      301 eqelqkvssg leelrrevss laarwhqeeg avqealrllg glggrldgfl gqweraqreq
      361 aqsarglqel rgradelctm versavsvas lrselealgp vkpileelgr qlqnsrrgpd
      421 hvlnldrpaq gpcprcasqg qqlsteslqq lleraltplv devkqkglap acpscqrlhk
      481 kilpspvspa aptllspgag apglgqtrqg rgpelhpsag prrsrsgqep tadgqdeagv
      541 rteaegmggg ekvatldymh lkmcslhdql shlplegstg amgggstgga ppkrggpgse
      601 q
//
LOCUS       NP_001100867             688 aa            linear   ROD 03-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100867 XP_001060647 XP_006254645 XP_226060
VERSION     NP_001100867.2
DBSOURCE    REFSEQ: accession NM_001107397.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006254645.1, NP_001100867.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.62223.1,
                                           SRR26643294.56980.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..688
                     /product="band 4.1-like protein 4A isoform 1"
                     /note="erythrocyte protein band 4.1-like 4a; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=78652
     Region          13..211
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          207..296
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(215,232,234,240)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(244,249..252,285,289,292..293)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            285..296
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Region          311..355
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     CDS             1..688
                     /gene="Epb41l4a"
                     /gene_synonym="Epb4.1l4a"
                     /coded_by="NM_001107397.3:1077..3143"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307514"
                     /db_xref="RGD:1306034"
ORIGIN      
        1 mgcfcavpee fycevlllde skltlttqhq gikkstkgsv vldhvfrhvn lveidyfglr
       61 ycdrshqtyw ldpaktlaeh kelintgppy tlyfgikfya edpcklkeei tryqfflqvk
      121 qdalqgrlpc pvniaaqlga yaiqaelgdh dpckhtagyv seyrfvpdqk eeleesieri
      181 hktlmgqaps eaelnylrta kslemygvdl hpvygenkse yflgltpvgv vvyknkkqvg
      241 kyfwpritkv hfketqfelr vlgkdcnets fffearskta ckhlwkcsve hhtffrmpet
      301 esnslsrkls kfgsisykhr ysgrtalqms rdlsiqlprp nqnvvrsrsk typkrvaqtq
      361 pagsnsinrm tanlengene gttkiiapsp vksfkkakne nspdpqrsks hapweengpq
      421 sglynspsdr tkspkfpctr qrnlscgsdn dssqpmrrrk ahhsgedsdl kqrrrsrsrc
      481 ntssgsesen snrehrkkrn rirqendmvd sapqweavlr rqkeknqvdp nnrrsrhrsr
      541 srspdiqake elwkhiqkel vdpsglseeq lkeipytkve tqgdpvrirh shsprsyrqy
      601 rrsqcsdger svlsevnskt dlvpplpvtr ssdaqgsggs tvhqrrngsk dslieeksql
      661 sttnlagkht aktiktiqaa rlktdvtg
//
LOCUS       NP_001424405             913 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424405 XP_063133378
VERSION     NP_001424405.1
DBSOURCE    REFSEQ: accession NM_001437476.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133378.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2455797.1,
                                           SRR26360172.2669888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..913
                     /product="synphilin-1 isoform 2"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=99755
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..913
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437476.1:179..2920"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaa
//
LOCUS       NP_001424383             545 aa            linear   ROD 03-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 12 [Rattus
            norvegicus].
ACCESSION   NP_001424383 XP_063140213
VERSION     NP_001424383.1
DBSOURCE    REFSEQ: accession NM_001437454.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063140213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3073929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..545
                     /product="testis-specific serine kinase substrate isoform
                     12"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=59528
     Region          26..545
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          112..>218
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..545
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437454.1:60..1697"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 mdhqlrarre gckslteael qekktngvep rmshepmhwc lnlkrssact nvsllnlaam
       61 epdssgtdst tedsgplalp gppaspttpw apedpditel lsgvnsglvr akdsitslke
      121 kttrvnqhvq tlqsecsvls enlerrrqea eelegycsql kncrkvtrsv edaeiktnvl
      181 kqnsalleek lrylqqqlqd etprrqeael qeleqkleag lsrhglgptt piqgcsgppg
      241 speepprprg lpsngwgmai ragegpslse qelqkvssgl eelrrevssl aarwhqeega
      301 vqealrllgg lggrldgflg qweraqreqa qsarglqelr gradelctmv ersavsvasl
      361 rselealgpv kpileelgrq lqnsrrgpdh vlnldrpaqg pcprcasqgq qlsteslqql
      421 leraltplvd evkqkglapa cpscqrlhkk ilelerqala khvraealss tlrlaqdeav
      481 raknllltdk mkpeekvatl dymhlkmcsl hdqlshlple gstgamgggs tggappkrgg
      541 pgseq
//
LOCUS       NP_001424459             479 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424459 XP_063133609
VERSION     NP_001424459.1
DBSOURCE    REFSEQ: accession NM_001437530.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133609.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.56164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663595, SAMN13663597
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..479
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53976
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          218..276
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          305..361
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          394..461
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..479
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437530.1:525..1964"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 msaedleaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrtta qassntelal ggaaaaaaas
      181 dvdqedsvde ravqdvesls sliqeildfn qdrqmkcfns klflcsicfc eklgsdcmyf
      241 lecrhvycka clkdyfeiqi kdgqvkclnc pepqcssvat pgqvkelvea dlfarydrll
      301 lqstldlmad vvycprpccq lpvmqepggt maicsscnfa fctlcrltyh gvspckvtae
      361 klidlrneyl qadeatkrfl eqrygkrviq kaleemeskd wleknskscp ccgtpiqkld
      421 gcnkmtctgc mqyfcwvcmg slsranpykh ftdpdspcfn rlfhavdvng diwedeied
//
LOCUS       NP_001424447             504 aa            linear   ROD 03-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424447 XP_063133447
VERSION     NP_001424447.1
DBSOURCE    REFSEQ: accession NM_001437518.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133447.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.73201.1,
                                           SRR26360176.1479250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..504
                     /product="band 4.1-like protein 4A isoform 3"
                     /note="erythrocyte protein band 4.1-like 4a; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=57433
     Region          <2..27
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          23..112
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(31,48,50,56)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(60,65..68,101,105,108..109)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            101..112
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Region          127..171
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     CDS             1..504
                     /gene="Epb41l4a"
                     /gene_synonym="Epb4.1l4a"
                     /coded_by="NM_001437518.1:620..2134"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:307514"
                     /db_xref="RGD:1306034"
ORIGIN      
        1 mgqapseael nylrtaksle mygvdlhpvy genkseyflg ltpvgvvvyk nkkqvgkyfw
       61 pritkvhfke tqfelrvlgk dcnetsfffe arsktackhl wkcsvehhtf frmpetesns
      121 lsrklskfgs isykhrysgr talqmsrdls iqlprpnqnv vrsrsktypk rvaqtqpags
      181 nsinrmtanl engenegttk iiapspvksf kkaknenspd pqrskshapw eengpqsgly
      241 nspsdrtksp kfpctrqrnl scgsdndssq pmrrrkahhs gedsdlkqrr rsrsrcntss
      301 gsesensnre hrkkrnrirq endmvdsapq weavlrrqke knqvdpnnrr srhrsrsrsp
      361 diqakeelwk hiqkelvdps glseeqlkei pytkvetqgd pvrirhshsp rsyrqyrrsq
      421 csdgersvls evnsktdlvp plpvtrssda qgsggstvhq rrngskdsli eeksqlsttn
      481 lagkhtakti ktiqaarlkt dvtg
//
LOCUS       NP_001100849             963 aa            linear   ROD 03-APR-2025
DEFINITION  synphilin-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100849 XP_001055030 XP_225768
VERSION     NP_001100849.1
DBSOURCE    REFSEQ: accession NM_001107379.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225768.4, XP_001055030.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..963
                     /product="synphilin-1 isoform 1"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=105664
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..963
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001107379.2:368..3259"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaamysscih lpsnalveeh lrdyarlndi krntkktynv khiaepepke
      961 lfl
//
LOCUS       NP_001108074             797 aa            linear   ROD 03-APR-2025
DEFINITION  protocadherin beta-4 [Rattus norvegicus].
ACCESSION   NP_001108074 NP_001014781 XP_001064542 XP_226003
VERSION     NP_001108074.2
DBSOURCE    REFSEQ: accession NM_001114602.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Wu,Q.
  TITLE     Comparative genomics and diversifying selection of the clustered
            vertebrate protocadherin genes
  JOURNAL   Genetics 169 (4), 2179-2188 (2005)
   PUBMED   15744052
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Zhang,T., Haws,P. and Wu,Q.
  TITLE     Multiple variable first exons: a mechanism for cell- and
            tissue-specific gene regulation
  JOURNAL   Genome Res 14 (1), 79-89 (2004)
   PUBMED   14672974
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Jun 28, 2018 this sequence version replaced NP_001108074.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26643298.73641.1,
                                        SRR26643294.57249.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..797
                     /product="protocadherin beta-4"
                     /calculated_mol_wt=87563
     Region          29..111
                     /region_name="Cadherin_2"
                     /note="Cadherin-like; pfam08266"
                     /db_xref="CDD:462413"
     Region          139..237
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(143..144,200,202,233,235..236)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          245..342
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(252..253,307,309,338,340..341)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          354..446
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(357..358,409,411,442,444..445)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          454..556
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(461..462,519,521,552,554..555)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          570..663
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          687..769
                     /region_name="Cadherin_C_2"
                     /note="Cadherin cytoplasmic C-terminal; pfam16492"
                     /db_xref="CDD:465139"
     CDS             1..797
                     /gene="Pcdhb5"
                     /coded_by="NM_001114602.2:190..2583"
                     /db_xref="GeneID:291654"
                     /db_xref="RGD:1304665"
ORIGIN      
        1 meklernhan rqvipflfml lwgqvlmvpt rysvleeaer gsfvahlakd lglgagelaa
       61 rsarvvsdfd nqqfmvdpdt gdlllrekld reelcgsvdp cvmhfqvfle kpvqffqgel
      121 liqdindnsp efpdkelllk ipensqpgtr fplnlaqdld vgsnglqeyr vstnphfhvl
      181 trnnsegkky pelvqdrald reeqaelslt lmaldgrspp rsgtalvril imdindnape
      241 fvnspyevqv pescppdspi ltvlapdada gnfgsvsygl fqasdeiqkt fsinevtgei
      301 rlkkeldfek tesyrveiea tdggglsgkg svvievldvn dnapeltiss ltssvpenap
      361 etvvaiirir drdsgdngkm icsisdhvpf tlkpsyknfy tlvteraldr esraeyniti
      421 svsdqgtprl ttqhtitvqv sdindnapaf tqtsytmfvh ennspalhig tisatdsdsg
      481 snahitysll ppydpqlald slisinpdng qlfalraldy ealqafefrv aatdggspal
      541 ssqalvrvmv lddndnapfv lyplqnasap ytellpraae pgylitkvva vdrdsgqnsw
      601 lsfqllkste pglfsvwahn gevrttrlls erdvpkhrll lvvkdngepp rsasitlqvv
      661 lvdgfsqpyl plpevardsa kdgadlltly lvialasvss lfllsvllfv gvrlcrrara
      721 aslgdctvpe ghfpghlvdv sragtlsqsy qyevcltgds gagefkflks mvpnlmvqdp
      781 greiaenlhc rdsfvfs
//
LOCUS       NP_001129182             696 aa            linear   ROD 03-APR-2025
DEFINITION  SEC14-like protein 5 [Rattus norvegicus].
ACCESSION   NP_001129182 XP_001079060
VERSION     NP_001129182.2
DBSOURCE    REFSEQ: accession NM_001135710.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jun 28, 2018 this sequence version replaced NP_001129182.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.25308.1,
                                           SRR26643284.12795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..696
                     /product="SEC14-like protein 5"
                     /note="SEC14-like 5 protein"
                     /calculated_mol_wt=78593
     Region          17..173
                     /region_name="PRELI"
                     /note="PRELI-like family; pfam04707"
                     /db_xref="CDD:398400"
     Region          243..288
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          314..476
                     /region_name="CRAL_TRIO"
                     /note="CRAL/TRIO domain; pfam00650"
                     /db_xref="CDD:459890"
     CDS             1..696
                     /gene="Sec14l5"
                     /gene_synonym="RGD1564638"
                     /coded_by="NM_001135710.2:143..2233"
                     /db_xref="GeneID:287060"
                     /db_xref="RGD:1564638"
ORIGIN      
        1 mvqkyqspvr vykypfelvm aayekrfptc plipvflgse vlsecrsadg avhtverscr
       61 lrvdaprllr kiagvehvvf iqrnvlnwre rtllidahne tfasrvtvke hcrytvhpen
      121 edwtcfeqsa sldvrsffgf estlekiamk qytanvkrgk eviehylsel isqgashipr
      181 wtpapvread vrsqlvcpcp ssletdgpsd apapasemat adgdkldady ierclghlsp
      241 mqesclvqlr rwlqethkgk ipkdehilrf lrardfhldk ardmlcqsls wrkqhqvdll
      301 lqtwrppapl qefyaggwhy qdidgrplyi lrlgqmdtkg lmkavgeeal lqhvlsvnee
      361 gqkrcegntr qfgrpisswt clldleglnm rhlwrpgvka llrmievved nypetlgrll
      421 ivraprvfpv lwtlvspfin entrrkfliy sgsnyqgpgg lvdyldkdvi pdflggesvc
      481 nvpeggmvpk slylteeeqe qadqlrqwse tyhsasvlrg sphevameip egesvitwdf
      541 dilrgdvvfs lyhakqapkl spqepgvras gqlidknwil gvdysrveap licregqsiq
      601 gshvtqwpgv yllqwqihsp pesvacslpg vddvltalhs pgpkckllyy cevlasedfr
      661 gsmsslesca srfsqlsatt tssssgqshs gsmvsr
//
LOCUS       NP_001160232             274 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 99 [Rattus norvegicus].
ACCESSION   NP_001160232 XP_002726458 XP_002729445
VERSION     NP_001160232.1
DBSOURCE    REFSEQ: accession NM_001166760.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_002726458.1, XP_002729445.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..274
                     /product="vomeronasal 1 receptor 99"
                     /note="vomeronasal 1 receptor Vom1r99; vomeronasal 1
                     receptor pseudogene 113"
                     /calculated_mol_wt=31142
     Region          27..>257
                     /region_name="7tm_V1R_pheromone"
                     /note="vomeronasal organ pheromone receptor type-1 family,
                     member of the seven-transmembrane G protein-coupled
                     receptor superfamily; cd13949"
                     /db_xref="CDD:320087"
     Region          28..53
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320087"
     Region          65..86
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320087"
     Region          101..123
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320087"
     Region          149..165
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320087"
     Region          200..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320087"
     CDS             1..274
                     /gene="Vom1r99"
                     /gene_synonym="Vom1r-ps113"
                     /coded_by="NM_001166760.1:1..825"
                     /db_xref="GeneID:685880"
                     /db_xref="RGD:1589006"
ORIGIN      
        1 mseilfvfpq plfsyvmstn srlhtdshir dtffteigig isvnnlpllf hiftlirgqr
       61 srltdlpidl lsllnllmll mwllatdifi swrgwddiic kflvylyrsf rglslcttcl
      121 lsvlqaiils prssclakfk hmpthqvsna mlflsvlymf isshlllsit atpslttndf
      181 ihvtqscsil plsylmpsmf sillairvvf lislmvlstw ymlallfrhr kqsrhlqgts
      241 lspkaspgqr vthsilmhkr gtqikssgyl qlsi
//
LOCUS       NP_001178726            1454 aa            linear   ROD 03-APR-2025
DEFINITION  nik-related protein kinase isoform 2 [Rattus norvegicus].
ACCESSION   NP_001178726 XP_236524
VERSION     NP_001178726.1
DBSOURCE    REFSEQ: accession NM_001191797.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1454)
  AUTHORS   Denda,K., Nakao-Wakabayashi,K., Okamoto,N., Kitamura,N., Ryu,J.Y.,
            Tagawa,Y.I., Ichisaka,T., Yamanaka,S. and Komada,M.
  TITLE     Nrk, an X-linked protein kinase in the germinal center kinase
            family, is required for placental development and fetoplacental
            induction of labor
  JOURNAL   J Biol Chem 286 (33), 28802-28810 (2011)
   PUBMED   21715335
REFERENCE   2  (residues 1 to 1454)
  AUTHORS   Nakano,K., Yamauchi,J., Nakagawa,K., Itoh,H. and Kitamura,N.
  TITLE     NESK, a member of the germinal center kinase family that activates
            the c-Jun N-terminal kinase pathway and is expressed during the
            late stages of embryogenesis
  JOURNAL   J Biol Chem 275 (27), 20533-20539 (2000)
   PUBMED   10801798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 17, 2010 this sequence version replaced XP_236524.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760389, SAMN09345238
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1454
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..1454
                     /product="nik-related protein kinase isoform 2"
                     /EC_number="2.7.11.1"
                     /note="nik-related protein kinase"
                     /calculated_mol_wt=164827
     Region          14..296
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(31..34,37,39,52,54,107,129..132,177,181..182,184,
                     194..195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <458..638
                     /region_name="PRK10927"
                     /note="cell division protein FtsN"
                     /db_xref="CDD:236797"
     Region          1146..1420
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     CDS             1..1454
                     /gene="Nrk"
                     /gene_synonym="RGD1566163"
                     /coded_by="NM_001191797.1:1..4365"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315907"
                     /db_xref="RGD:1566163"
ORIGIN      
        1 magpgswrdk evtdlghlpd ptgifslekt iglgtygriy lglhektgsf vaikvmnark
       61 tplpeigkrv rvnkyrksvg wrysdeeedl rtelnllrky sfhknivtfy gaffklnppg
      121 hqhqlwmvme lcaagsvtdv vrmtrnqslk edwiayicre ilqglahlha hqvihrdikg
      181 qnvlltqdae vkivdfgvsa qvsrtngrrn sfigtpywma pevihcdedp rrsydyrvtl
      241 cnlqplealf vilreaaptv kssgwsrkfq nfmencmikn flfrptsgnm lhhpfvhdik
      301 nerrvveslt khltgiiqkr erkgiplafe geeavneqyi trrfrgpsct pellrvptss
      361 rcrplrvlhg eppqprwlpd eeqpedqelq qlqeaarmfm plhsqdktlk plqkqaqlpq
      421 hlhvapqvlm pvqveatvat plakkirapp qlskaawglt sppsqdnkas spevqapipr
      481 eqqaqndale teqpedldqv peefqgqdra aeeqrqgqaa eqeqrqngvp eqhpeenrep
      541 eqaevqeeav eppqaeveek dpeviqvhar vflplqsqnh hvflplhldt qllipvgeqn
      601 eeapraqawd leasraagav qalveglsrd llrapnafts kplgplqill eslctngfyt
      661 epeavqkkks rvsslkkaiv krltpkrfra kalwrrqdfe csdvessrrr rqrrweeifn
      721 qheeqlreve ndrddddssd ndevfhsiqa evqiepyapn rtgnevqers apmpcnrnrt
      781 hrvkfspsvc eqalleeaqq pmdirprnsl nprnfqaese ssseedspvt rrksqssppy
      841 stidqrllid ihvpdgfkvg kisppvyltn ewvgcnplse vfwddwvnpt patrrheedg
      901 dyvelydada ngdgrasnya yeenyasghd dmnhqangyr ghgnrhysdg sfrnrgdsrg
      961 aafngprasy crggilknag ndgrdlrrga fraygdneas nyhgaasgas aafgsqeghe
     1021 ghmggrrgnr yrevngssge ngacgfhrdg agldqqhvfp dfeneqeqsd agtetsdsia
     1081 leitsfsldg eqnndraept lgfplrrsss rgsasdtdim sdsynkpiih ayerefshei
     1141 fcgslwgvnl llgtkshlyl mdrsgkaeii klvkrrpfrq iqvveqlnll itisgrknrl
     1201 rvyhltwlrn kilnndpesk krqkamlkre kacksldkli gcehfsilhh eettyiaial
     1261 kssihlyawa pksfnestai kvfpthdlkp vtvdlavgse ktlkiffssa ngyhiidaes
     1321 evmsdvtlps nnvillpdsl gvgvmlsfnd etapeeaneq llkkildvwk dipssaafec
     1381 tqritgwdqk avevrslqat ilenelkrrs ikklrflcsr gdklffasll nnehslvyyv
     1441 siaklealqr ryav
//
LOCUS       NP_001008512             339 aa            linear   ROD 03-APR-2025
DEFINITION  trace amine-associated receptor 2 [Rattus norvegicus].
ACCESSION   NP_001008512 XP_220097
VERSION     NP_001008512.1
DBSOURCE    REFSEQ: accession NM_001008512.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Lindemann,L., Ebeling,M., Kratochwil,N.A., Bunzow,J.R., Grandy,D.K.
            and Hoener,M.C.
  TITLE     Trace amine-associated receptors form structurally and functionally
            distinct subfamilies of novel G protein-coupled receptors
  JOURNAL   Genomics 85 (3), 372-385 (2005)
   PUBMED   15718104
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY702316.1.
            
            On Dec 16, 2004 this sequence version replaced XP_220097.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY702316.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /strain="WIST/Crl"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..339
                     /product="trace amine-associated receptor 2"
                     /note="G-protein coupled receptor 58; taR-2; trace amine
                     receptor 2"
                     /calculated_mol_wt=38426
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          33..314
                     /region_name="7tmA_TAAR2_3_4"
                     /note="trace amine-associated receptors 2, 3, 4, and
                     similar receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15312"
                     /db_xref="CDD:320437"
     Region          33..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320437"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          66..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320437"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          104..134
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320437"
     Site            order(107,111..112,115..116,191,198,201..202,205,263,
                     266..267,270,285,289,293)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320437"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          146..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320437"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          194..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320437"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          244..273
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320437"
     Site            252..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5QD25.1)"
     Region          282..307
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320437"
     Site            288..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD25.1)"
     CDS             1..339
                     /gene="Taar2"
                     /gene_synonym="Gpr58"
                     /coded_by="NM_001008512.1:1..1020"
                     /db_xref="GeneID:294121"
                     /db_xref="RGD:1311240"
ORIGIN      
        1 mtsfeaqqet fdcseygngs cpenerslgv raamyslmag aifitifgnl vmiisisyfk
       61 qlhtptnlli lsmavtdfll gftimpysmv rsvencwyfg ltfckihysf dlmlsitsif
      121 hlcsvaidrf yaichplhyc tkmtipvvkr lllvcwsvpg afafgvvfse ayadgiegyd
      181 ilvacssscp vmfnklwgtt lfvagfftps smmvgiygki favskkharv idnlpenqnn
      241 qmrkdkkaak tlgivmgvfl lcwfpcffti lldpflnfst pailfdaltw fgyfnstcnp
      301 liygffypwf rralryillg kifsshfhnt nlftqkete
//
LOCUS       NP_001092952             860 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 25 precursor [Rattus norvegicus].
ACCESSION   NP_001092952 XP_577748
VERSION     NP_001092952.3
DBSOURCE    REFSEQ: accession NM_001099482.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 3, 2021 this sequence version replaced NP_001092952.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..860
                     /product="vomeronasal 2 receptor 25 precursor"
                     /calculated_mol_wt=95436
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2349
     Region          41..507
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(74,173..174,398)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(114,117,160,247)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          515..567
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          588..839
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          588..613
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(591,594..595,598..599,601..602,636,640,643..644,652,
                     656)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          625..646
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(645,657..658,661..662,665,745,750,753..754,757,791,
                     794..795,798,802,810..811,814,817,821)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          655..679
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          703..719
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          746..772
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          780..803
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          808..833
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..860
                     /gene="Vom2r25"
                     /gene_synonym="RGD1564853"
                     /coded_by="NM_001099482.3:1..2583"
                     /db_xref="GeneID:502286"
                     /db_xref="RGD:1564853"
ORIGIN      
        1 mlfswtfisc flqipilvcs ytsseclvrm nyrihgegnv viigyfpaya iyplnkttdw
       61 rmlkfnrdfm veiklknyqc ilammfaiee innnpyllpn tslgfevnni sqgqrytlan
      121 vfrslstsac vdlnyrnahe snfaavltgp swaiseyigt lldlykfpql tfgpfdslqs
      181 eqrrfsslyq vapkdtfltl givslmlhfh wiwvglfiid ddkgaqtlsd lrsemdkngv
      241 ctafvemivv trgsfftksw knqvqiless snviiihgds dsllslivni kqklltwkvw
      301 vlisqwdvsk fddyfmvdsl hgalifshhr edipnftdfm qksnpskype dtylhvlwhi
      361 ffncsfvntd ckivhnclpn aslgflpgni fdmamseesy nvynavyava hslhemilnq
      421 vqfqthekgk kmvffpwqlh pylrktlfnq devnevldwk rkshveydil nfwnfpkglg
      481 lnvkvgtfsp sapknqklsi ssnmiqwatg paeipqsvcs eschpgfrkm hkegivaccf
      541 dctpcpenei snetdmdqcv kcpeshygdt dkihclqktv tflaygdpwg ktlcflslgf
      601 ssltaavlgv flknrdtpiv kannlplsyt llitlmlcfl cpllfighps tascilqqni
      661 fgllftmals tvlaksitvv lafkitaagr irrwllisra pnfiiplctl lqvflsaiwl
      721 ttsppfvdkd ahsehghiii icnkgsaiaf hctlgylgal alasyfmafl srnlpdtfne
      781 akflafsmlv fcsvwvtflp vyhstkgkvt vamevfsila sstsllgiif vpkcylillr
      841 pernslnyir eksyarrkkp
//
LOCUS       NP_001161024             315 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 60 [Rattus norvegicus].
ACCESSION   NP_001161024
VERSION     NP_001161024.1
DBSOURCE    REFSEQ: accession NM_001167552.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..315
                     /product="vomeronasal 1 receptor 60"
                     /note="vomeronasal 1 receptor Vom1r60; vomeronasal 1
                     receptor, J4-like"
                     /calculated_mol_wt=35892
     Region          6..300
                     /region_name="V1R"
                     /note="Vomeronasal organ pheromone receptor family, V1R;
                     pfam03402"
                     /db_xref="CDD:460912"
     CDS             1..315
                     /gene="Vom1r60"
                     /coded_by="NM_001167552.1:1..948"
                     /db_xref="GeneID:100312671"
                     /db_xref="RGD:2316470"
ORIGIN      
        1 mlpsdtivqi flilqfclgv mgnsalllly iytfvfrpqy kklidsvfih ltivnilliv
       61 flltkhimlp fgvpnflddi gcktvlfsfr vsrglsicst cvistfqvit itpstskwaw
      121 lkprlstwif ssllcswlin lliygymldm viaktnntlv ghgytdgycv nkqvgnhnsg
      181 sflsiviihd lffvtimmca slymvlflyr yrkgaqhlrs pnlsfqpspe rkathsilsl
      241 vscfvliywl nncvtlysfy sseriprves inailttcyp ticpflfmkn nkvilqfiss
      301 fsiqrmtcfq ssihg
//
LOCUS       NP_001178001             568 aa            linear   ROD 03-APR-2025
DEFINITION  protein phosphatase 1 regulatory inhibitor subunit 16B [Rattus
            norvegicus].
ACCESSION   NP_001178001 XP_001058014
VERSION     NP_001178001.1
DBSOURCE    REFSEQ: accession NM_001191072.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Boratko,A., Peter,M., Thalwieser,Z., Kovacs,E. and Csortos,C.
  TITLE     Elongation factor-1A1 is a novel substrate of the protein
            phosphatase 1-TIMAP complex
  JOURNAL   Int J Biochem Cell Biol 69, 105-113 (2015)
   PUBMED   26497934
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Obeidat,M., Li,L. and Ballermann,B.J.
  TITLE     TIMAP promotes angiogenesis by suppressing PTEN-mediated Akt
            inhibition in human glomerular endothelial cells
  JOURNAL   Am J Physiol Renal Physiol 307 (5), F623-F633 (2014)
   PUBMED   25007873
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Poirier,C., Gorshkov,B.A., Zemskova,M.A., Bogatcheva,N.V. and
            Verin,A.D.
  TITLE     TIMAP protects endothelial barrier from LPS-induced vascular
            leakage and is down-regulated by LPS
  JOURNAL   Respir Physiol Neurobiol 179 (2-3), 334-337 (2011)
   PUBMED   21907835
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Czikora,I., Kim,K.M., Kasa,A., Becsi,B., Verin,A.D., Gergely,P.,
            Erdodi,F. and Csortos,C.
  TITLE     Characterization of the effect of TIMAP phosphorylation on its
            interaction with protein phosphatase 1
  JOURNAL   Biochimie 93 (7), 1139-1145 (2011)
   PUBMED   21466834
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Csortos,C., Czikora,I., Bogatcheva,N.V., Adyshev,D.M., Poirier,C.,
            Olah,G. and Verin,A.D.
  TITLE     TIMAP is a positive regulator of pulmonary endothelial barrier
            function
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 295 (3), L440-L450 (2008)
   PUBMED   18586956
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Kim,K., Li,L., Kozlowski,K., Suh,H.S., Cao,W. and Ballermann,B.J.
  TITLE     The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1
            phosphorylation
  JOURNAL   Biochem Biophys Res Commun 338 (3), 1327-1334 (2005)
   PUBMED   16263087
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Cao,W., Mattagajasingh,S.N., Xu,H., Kim,K., Fierlbeck,W., Deng,J.,
            Lowenstein,C.J. and Ballermann,B.J.
  TITLE     TIMAP, a novel CAAX box protein regulated by TGF-beta1 and
            expressed in endothelial cells
  JOURNAL   Am J Physiol Cell Physiol 283 (1), C327-C337 (2002)
   PUBMED   12055102
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jul 17, 2010 this sequence version replaced XP_001058014.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.15404.1,
                                           SRR26643284.5111.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..568
                     /product="protein phosphatase 1 regulatory inhibitor
                     subunit 16B"
                     /note="protein phosphatase 1, regulatory (inhibitor)
                     subunit 16B"
                     /calculated_mol_wt=63438
     Region          71..321
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          71..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(73..74,77..79,81..82,86,89,98,100,102,106..107,
                     110..112,114..115,119,122,131,133,135,139..140,143..145,
                     147..148,152,155,164)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          100..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          133..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          166..259
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          261..292
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          294..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..568
                     /gene="Ppp1r16b"
                     /coded_by="NM_001191072.1:180..1886"
                     /db_xref="GeneID:680616"
                     /db_xref="RGD:1589460"
ORIGIN      
        1 mashvdllte lqllekvptl erlraaqkrr aqqlkkwaqy eqdllhrkrk herkrstggr
       61 rkkvsfeasv alleaslrnd aeevryflkn kvspdlcned gltalhqcci dnfeeivkll
      121 lshganvnak dnelwtplha aatcghinlv kilvqygadl lavnsdgnmp ydlcedeptl
      181 dvietcmayq gitqekinem raapeqkmis dihcmiaagq dldwidgqga tllhiagang
      241 ylraaellld hgvrvdvkdw dgweplhaaa fwgqmpmael lvshgaslsa rtsmdempid
      301 lceeeefkvl llelkhkhdv imksqlrhks slsrrtssag srgkvvrras lsdrtnlyrk
      361 eyegeailwq qrsaaeeqrt styngdiret rtdqenkdpn prlekpvlls efstkisrge
      421 ldgpvenglr apvstyqyal angdiwkmhe ipdysmaygn pgmadvpppw sgfkeqspqt
      481 llelkrqraa akllshpfls thlgssvars gegssegkap liggrtspys sngtsvyytv
      541 tsgdppllkf kapmeemeek vhgccris
//
LOCUS       NP_001178758             319 aa            linear   ROD 03-APR-2025
DEFINITION  cell surface A33 antigen precursor [Rattus norvegicus].
ACCESSION   NP_001178758 XP_341150
VERSION     NP_001178758.1
DBSOURCE    REFSEQ: accession NM_001191829.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   van Niel,G., Raposo,G., Candalh,C., Boussac,M., Hershberg,R.,
            Cerf-Bensussan,N. and Heyman,M.
  TITLE     Intestinal epithelial cells secrete exosome-like vesicles
  JOURNAL   Gastroenterology 121 (2), 337-349 (2001)
   PUBMED   11487543
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Abud,H.E., Johnstone,C.N., Tebbutt,N.C. and Heath,J.K.
  TITLE     The murine A33 antigen is expressed at two distinct sites during
            development, the ICM of the blastocyst and the intestinal
            epithelium
  JOURNAL   Mech Dev 98 (1-2), 111-114 (2000)
   PUBMED   11044613
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341150.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.34164.1,
                                           SRR26643288.49767.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..319
                     /product="cell surface A33 antigen precursor"
                     /note="cell surface A33 antigen; glycoprotein A33
                     (transmembrane)"
                     /calculated_mol_wt=33270
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2252
     Region          26..138
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Region          139..220
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          153..162
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          172..176
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          208..213
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..319
                     /gene="Gpa33"
                     /coded_by="NM_001191829.1:118..1077"
                     /db_xref="GeneID:360873"
                     /db_xref="RGD:1306711"
ORIGIN      
        1 mlgtvgpvlw mfcaiwvaad aitvettqdv lraargksvt lpciystpvs drqgfiqwdk
       61 llrsqtekva twtfetkkyt ygsryenrvr isndaelsna sitidqltmd dngtyecsvs
      121 lmsdqdvtsr srvrllvlvp pskpdcgieg etvignniql tchsaegsps pqyswksyna
      181 qnqqrplaqp vsgeplllkn isadtagyyi ctssndvgte fcnitvaprp psmnialyag
      241 iaggvfvali iigvivyccc crekddkaqe metvrpdraa yqepknqrte isrewededd
      301 rrhedqrssg rgspdqpfq
//
LOCUS       NP_001396077             310 aa            linear   ROD 03-APR-2025
DEFINITION  olfactory receptor family 5 subfamily P member 80 [Rattus
            norvegicus].
ACCESSION   NP_001396077 XP_038952369
VERSION     NP_001396077.1
DBSOURCE    REFSEQ: accession NM_001409148.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Jul 12, 2022 this sequence version replaced XP_038952369.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..310
                     /product="olfactory receptor family 5 subfamily P member
                     80"
                     /note="olfactory receptor 508"
                     /calculated_mol_wt=34273
     Region          25..303
                     /region_name="7tmA_OR5P-like"
                     /note="olfactory receptor subfamily 5P and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15416"
                     /db_xref="CDD:320538"
     Region          26..52
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320538"
     Region          59..85
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320538"
     Site            order(81,84..85,97..102,104..105,108,153,155..159,195,
                     198..200,202..204,206..207,252,255..256,258..259,262,
                     268..269,271..273,276,279..280)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320538"
     Region          97..127
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320538"
     Region          140..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320538"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320538"
     Region          232..262
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320538"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320538"
     CDS             1..310
                     /gene="Or5p80"
                     /coded_by="NM_001409148.1:1..933"
                     /db_xref="GeneID:687082"
                     /db_xref="RGD:1590087"
ORIGIN      
        1 mesgnytvvt elillgfaed atvrailfvv fliiysvtli gnmsiimlir rssqlhtpmy
       61 lflshlafvd igysssvtpi mlkgflrkei silvagcvtq lyfavtfgsv ecfllaamay
      121 dryvaicspl lyatqmsstv cillvgasyl ggcvnawtft gcllnlsfcr pnkvnhffcd
      181 yspllkiscs hgfssevipa issgsiivvt vfiialsyvy ilvsilkmrs pegrqkafst
      241 ctshltavtl fygtitfiyv mpkssystdq nkvvsvfytv vipmlnpiiy slrnkdvkea
      301 mkklmadthw
//
LOCUS       NP_001178764             160 aa            linear   ROD 03-APR-2025
DEFINITION  complexin-4 [Rattus norvegicus].
ACCESSION   NP_001178764 XP_341626
VERSION     NP_001178764.1
DBSOURCE    REFSEQ: accession NM_001191835.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Reim,K., Wegmeyer,H., Brandstatter,J.H., Xue,M., Rosenmund,C.,
            Dresbach,T., Hofmann,K. and Brose,N.
  TITLE     Structurally and functionally unique complexins at retinal ribbon
            synapses
  JOURNAL   J Cell Biol 169 (4), 669-680 (2005)
   PUBMED   15911881
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341626.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB748805.1, CB801796.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..160
                     /product="complexin-4"
                     /calculated_mol_wt=18219
     Region          1..140
                     /region_name="Synaphin"
                     /note="Synaphin protein; pfam05835"
                     /db_xref="CDD:461755"
     CDS             1..160
                     /gene="Cplx4"
                     /coded_by="NM_001191835.1:131..613"
                     /db_xref="GeneID:361342"
                     /db_xref="RGD:1307643"
ORIGIN      
        1 maffvknmis nqvknlgfgg gseekkeegg tsdpaaakgm treeyeeyqk qmieekmerd
       61 aaftqkkaer aclrvhlrdk yrlpksemde tqiqlagddv dlpedlrkmv dedqdeeeek
      121 dsilgqlqnl qnmdldtike kaqatfteik qsaeqkcsvm
//
LOCUS       NP_001092927             646 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 2 [Rattus norvegicus].
ACCESSION   NP_001092927 XP_218099
VERSION     NP_001092927.3
DBSOURCE    REFSEQ: accession NM_001099457.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Mar 31, 2024 this sequence version replaced NP_001092927.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..646
                     /product="vomeronasal 2 receptor 2"
                     /calculated_mol_wt=73654
     Region          <1..305
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          313..366
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          386..637
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          386..411
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(389,392..393,396..397,399..400,434,438,441..442,450,
                     454)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          423..444
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(443,455..456,459..460,463,543,548,551..552,555,589,
                     592..593,596,600,608..609,612,615,619)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          453..477
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          501..517
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          544..570
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          578..601
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          606..631
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..646
                     /gene="Vom2r2"
                     /gene_synonym="RGD1561757"
                     /coded_by="NM_001099457.3:97..2037"
                     /db_xref="GeneID:292438"
                     /db_xref="RGD:1561757"
ORIGIN      
        1 mvslmfhfew twigliitdd dqgiqfhsdl reemqrhaic lafvimipes iklyntkfki
       61 ydqqlmtssa kvtiiygkmi stlelnfarw tylvarriwi ttskldvity dkdfsldffh
      121 gtvifahhhn diatfrnfmq iintskypvd isqsmgqwnh fncsisknkk kmdffmlknp
      181 mewltqhtfd mvlseegynl ynavyavaht yhelifqqve sqemakpkgl ftdcqqvasl
      241 lktrvftnpv gelvnmnhke nqcakydifi iwnfpnglgl kvkigsyfpc lqqsqhlhis
      301 edwewvtget lvpssvcset ctagfrkshq kqtanccfdc vqcqeneian dtdmeqcvrc
      361 pddsyanleq tqclqravtf layedplgma lgcmalsfsa itvlvlvtfv kyrdtpivka
      421 nnrilsyill islvfcflcs llfighpnqa tcilqqatfa ifftvaistv laktitvvta
      481 fklttpgrri rkmmikgath llipictliq lvlcaiwlvt sppfidrdiq sehgkviiic
      541 nkgsviafhf vlgylgslal gsftvaflar nlpdrfneak fltfsmlvfy svwitflpvy
      601 hstrgkvmvi vevfsilass agllgcifvq kcyvllvrpd lnvlqk
//
LOCUS       NP_001178944             571 aa            linear   ROD 03-APR-2025
DEFINITION  solute carrier family 15 member 5 [Rattus norvegicus].
ACCESSION   NP_001178944 XP_578419
VERSION     NP_001178944.1
DBSOURCE    REFSEQ: accession NM_001192015.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_578419.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2485107.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..571
                     /product="solute carrier family 15 member 5"
                     /calculated_mol_wt=62752
     Region          33..523
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(46..47,50..51,54,87,159..160,162..164,167,190,
                     193..194,197,310,313..314,317..319,322,353,357,435..436,
                     440,444,460,463..464,467..468,471)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340907"
     CDS             1..571
                     /gene="Slc15a5"
                     /gene_synonym="RGD1564925"
                     /coded_by="NM_001192015.1:1..1716"
                     /db_xref="GeneID:502918"
                     /db_xref="RGD:1564925"
ORIGIN      
        1 mfvtgfiind ekaplplhgg perqktvghl gcfrvgicsl lvelcerftf fevvcnmipf
       61 ctrrlgcynh qaailnlcfi gasvltpvfm gwlsdskylg rnklvyiavf lhflgtalls
      121 vlafpsedfy ggtspasnmp mkkraglfhv alltlclgtg giravvclpd acghweqesk
      181 kpmsfcnwas wsmnlntavv flgvssiqll gsgavmillp slsvftasvt lymtycdliy
      241 epenhcslpt vsrafarvlk trcllychlg ragsswlara makqgvchce lqeeetenvf
      301 sallslfsfq liyrmcltqi psgyylqtmh snrtlggvpl pialmnaisl lplltlgpfm
      361 dffsncllps krdgpflsvc iiagnicaaf svavagflei hrklaqeqsp sgklssvssm
      421 acvylvpqyv llgvsevlvn pavstvtrrv vpstfrrasm tcltlfhgsa yfagalliel
      481 vylisegnwf pntlnkgnle sfffvlaslt llnilglwrv lprccnlnhf naqrihgnnc
      541 eetlllseks lkfygstqet sssidlreta f
//
LOCUS       NP_001092980             854 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 51 [Rattus norvegicus].
ACCESSION   NP_001092980 XP_578392
VERSION     NP_001092980.1
DBSOURCE    REFSEQ: accession NM_001099510.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On Aug 17, 2007 this sequence version replaced XP_578392.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..854
                     /product="vomeronasal 2 receptor 51"
                     /calculated_mol_wt=96029
     Region          40..510
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(76,175..176,401)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(114,117,162,249)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          518..571
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          591..842
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          591..616
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(594,597..598,601..602,604..605,639,643,646..647,655,
                     659)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          628..649
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(648,660..661,664..665,668,748,753,756..757,760,794,
                     797..798,801,805,813..814,817,820,824)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          658..682
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          706..722
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          749..775
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          783..806
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          811..836
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..854
                     /gene="Vom2r51"
                     /gene_synonym="RGD1561712"
                     /coded_by="NM_001099510.1:1..2565"
                     /db_xref="GeneID:502891"
                     /db_xref="RGD:1561712"
ORIGIN      
        1 mklliafsll ivlivfqeqi swfslsipas pgyyqdgdfv igglfslrvt agdtkskfgf
       61 kdtismpdiv yadftkhyqh mlamvfaien inkdpnilfn mslgfylfnv dfiemkaves
      121 smallsgetp pvpnyscrpe ktdklvavig gistgistqi srvlslynvp qisyapfdqs
      181 lgtevqlqsp yqfpvhttal yqgiiqllly ftwiwvglvv pddvrgelfl rditeemnnh
      241 glcvafaekv pefpardtin rklfmerfil trvivafgdt ysllrfvyni ycntpfgniw
      301 ittsdwditt lpfqqnlgyt yfggglsfsv htdeilefkd flrsvqprky pqdifiqdvw
      361 snlfecpyld kdwirelsqc eqngnlstrp lylwdmntsp ssykvhfavy aiaealheel
      421 sltvegdslr kggprallpw klhpflqkcq lgrssneqnv mnnevsatkl difnyqslqs
      481 gtkaqvkvgk fvyeshsvqh fslndkiimw gehhnhtpfs vcsqscplgf rkspiegkpf
      541 ccfdclpcpd geianetdmd qcikcpedqy pnkqrnwchp kitaflshed tlgavlvsva
      601 islsvfsami lglficyrdt pivrannrnl sylllvslml cffcslifig qprtvtcvlr
      661 qtifgvvfsi aisailaktf ivvvafkaik pgstlqtwmv trvsnaivcc gsiiqvcica
      721 vwlgtyppfp dvdmhsefgq iilwcnegst lafycvlgyl gflaslslli aflarrlpdt
      781 fneaktitfs mlvfcsvwis fvpaylsskg ktmvaveilt ilassagllg ciflpkcfvi
      841 llksgglprk kfsi
//
LOCUS       NP_001178885             344 aa            linear   ROD 03-APR-2025
DEFINITION  calcium homeostasis modulator protein 3 [Rattus norvegicus].
ACCESSION   NP_001178885 XP_574682
VERSION     NP_001178885.1
DBSOURCE    REFSEQ: accession NM_001191956.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Ma,Z., Taruno,A., Ohmoto,M., Jyotaki,M., Lim,J.C., Miyazaki,H.,
            Niisato,N., Marunaka,Y., Lee,R.J., Hoff,H., Payne,R., Demuro,A.,
            Parker,I., Mitchell,C.H., Henao-Mejia,J., Tanis,J.E., Matsumoto,I.,
            Tordoff,M.G. and Foskett,J.K.
  TITLE     CALHM3 Is Essential for Rapid Ion Channel-Mediated Purinergic
            Neurotransmission of GPCR-Mediated Tastes
  JOURNAL   Neuron 98 (3), 547-561 (2018)
   PUBMED   29681531
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_574682.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1811448.1,
                                           SRR26360181.1839856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..344
                     /product="calcium homeostasis modulator protein 3"
                     /note="family with sequence similarity 26, member A"
                     /calculated_mol_wt=38657
     Region          2..252
                     /region_name="Ca_hom_mod"
                     /note="Calcium homeostasis modulator; pfam14798"
                     /db_xref="CDD:464320"
     CDS             1..344
                     /gene="Calhm3"
                     /gene_synonym="Fam26a; RGD1560215"
                     /coded_by="NM_001191956.1:1..1035"
                     /db_xref="GeneID:499368"
                     /db_xref="RGD:1560215"
ORIGIN      
        1 mdrfrmlfqn fqsssesvtn giclllaavt vkmyssldfn cpclehynal yglgllltpp
       61 lalflcgllv nrqsvlmvee wrrpaghrrk dlgiirymcs svlqralaap lvwillalld
      121 gkclvcafsn svdpekfldf anmtpsqvql flakvpcked elvktspark avsrylrcls
      181 qaigwsitll vivvaflarc lrpcfnqtvf lqrrywsnym dleqklfdet ccehardfah
      241 rcvlhffasm qselralglh rdpageiles qeppeppeep gsesgkahlr aissreqvnh
      301 llstwysskp pldlaasprl wepglnhrap iaapgtklgh qldv
//
LOCUS       NP_001093125             849 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 16 [Rattus norvegicus].
ACCESSION   NP_001093125
VERSION     NP_001093125.1
DBSOURCE    REFSEQ: accession NM_001099655.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..849
                     /product="vomeronasal 2 receptor, 16"
                     /calculated_mol_wt=97344
     Region          41..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,170..171,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          512..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..836
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..849
                     /gene="Vom2r16"
                     /coded_by="NM_001099655.1:1..2550"
                     /db_xref="GeneID:690691"
                     /db_xref="RGD:1593384"
ORIGIN      
        1 mhtlilffll lnipllvvsl ihprcfwrmk qneekngnlk tgcifafgvv kwpvekeyyy
       61 nilstqtnte nhqfslalaf smdeinknpd llpnksllfd fpfysckshs elttlihgsv
      121 qqydifpnyv cnnetmctll ltgpnwkisv ilrtyldlyk sqqflqltyg pfhpvlsdne
      181 qfpylyqmap ketslalalv sflihfswnw iglaisdndq gnqflsylrt emgkytvcfa
      241 fvnmipvnmq lfmtrtdvyy nqiitsstnv vivygdtdst lalgfkmwks lgvqriwvtt
      301 sewdvitskr dftfdtfhsi iafqhhhgei sgfknfvqtl npfkysdkyl vklewmyfnc
      361 eisasncktl knclynesfe wlseqtfdma fsdgthdiyn aayavahalh efflqqgdnq
      421 qkyrgkwpns vclklhsllk kthftnpvgd rvimnqrekm qeeydifyiw nfpqglglkv
      481 kigefspyys sgkqlwlfed miewttgnrq mpssvcnsdc gpgfrkiwke gmstccfdci
      541 hcqeneisne tnvdqcvkcp edqyanpeqn hcihkalifl tyqetlgmtl slvalclstl
      601 taailgvfvk yhttpivkan ncrltyilli tlifcflcpl lyighpnsvt cvlqqvtfgi
      661 vftvaistvl aktitvilaf kvtapqrmik yflisgvfny iipictliqv fvctlwlgts
      721 ppsvdfdpqs ehghiiivcn kgsvtafycm lgylsclalg sftlaflsrn lpgtfneakf
      781 ltfsmlvfcs vwitflpvyh stkgkvmvav eifstlassa gmlgcifipk cyiillrper
      841 nslqrirek
//
LOCUS       NP_001381923             360 aa            linear   ROD 03-APR-2025
DEFINITION  nucleoporin SEH1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001381923
VERSION     NP_001381923.1
DBSOURCE    REFSEQ: accession NM_001394994.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Bonnet,A. and Palancade,B.
  TITLE     Regulation of mRNA trafficking by nuclear pore complexes
  JOURNAL   Genes (Basel) 5 (3), 767-791 (2014)
   PUBMED   25184662
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Ahn,S.H., Deshmukh,H., Johnson,N., Cowell,L.G., Rude,T.H.,
            Scott,W.K., Nelson,C.L., Zaas,A.K., Marchuk,D.A., Keum,S.,
            Lamlertthon,S., Sharma-Kuinkel,B.K., Sempowski,G.D. and Fowler,V.G.
            Jr.
  TITLE     Two genes on A/J chromosome 18 are associated with susceptibility
            to Staphylococcus aureus infection by combined microarray and QTL
            analyses
  JOURNAL   PLoS Pathog 6 (9), e1001088 (2010)
   PUBMED   20824097
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Zuccolo,M., Alves,A., Galy,V., Bolhy,S., Formstecher,E., Racine,V.,
            Sibarita,J.B., Fukagawa,T., Shiekhattar,R., Yen,T. and Doye,V.
  TITLE     The human Nup107-160 nuclear pore subcomplex contributes to proper
            kinetochore functions
  JOURNAL   EMBO J 26 (7), 1853-1864 (2007)
   PUBMED   17363900
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Glavy,J.S., Krutchinsky,A.N., Cristea,I.M., Berke,I.C., Boehmer,T.,
            Blobel,G. and Chait,B.T.
  TITLE     Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
            subcomplex
  JOURNAL   Proc Natl Acad Sci U S A 104 (10), 3811-3816 (2007)
   PUBMED   17360435
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Loiodice,I., Alves,A., Rabut,G., Van Overbeek,M., Ellenberg,J.,
            Sibarita,J.B. and Doye,V.
  TITLE     The entire Nup107-160 complex, including three new members, is
            targeted as one entity to kinetochores in mitosis
  JOURNAL   Mol Biol Cell 15 (7), 3333-3344 (2004)
   PUBMED   15146057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR23984936.252759.1,
                                           SRR26360190.1746549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..360
                     /product="nucleoporin SEH1 isoform 1"
                     /note="nucleoporin SEH1; nucleoporin SEH1-like"
                     /calculated_mol_wt=39615
     Region          <11..328
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          15..55
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          61..111
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..149
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..267
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          281..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..360
                     /gene="Seh1l"
                     /coded_by="NM_001394994.1:131..1213"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100911798"
                     /db_xref="RGD:6490353"
ORIGIN      
        1 mfvarsiaad hkdlihdvsf dfhgrrmatc ssdqsvkvwd ksesgdwhct aswkthsgsv
       61 wrvtwahpef gqvlascsfd rtaavweeiv gesndklrgq shwvkrttlv dsrtsvtdvk
      121 fapkhmglml atcsadgivr vyeapdvmnl sqwslqheis cklccscisw npsssrahpp
      181 miavgsddss pnsmakvqif eynentrkya kaetlmtvtd pvhdiafapn lgrsfhilai
      241 atkdvriftl kpvrkeltss ggptkfeihi vaqfdnhnsq vwrvswnitg tvlassgddg
      301 cvrlwkanym dnwkctgilk gngspvngss qlgnstpsls snipnlqnsl ngtsagrkhs
//
LOCUS       NP_001128079             516 aa            linear   ROD 03-APR-2025
DEFINITION  protein hinderin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001128079 XP_574112
VERSION     NP_001128079.1
DBSOURCE    REFSEQ: accession NM_001134607.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473974.1.
            
            On Sep 4, 2008 this sequence version replaced XP_574112.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132262, SAMD00132264
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..516
                     /product="protein hinderin isoform 1"
                     /calculated_mol_wt=58869
     Region          28..351
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     CDS             1..516
                     /gene="Kiaa1328"
                     /gene_synonym="RGD1562608; RGD1564140"
                     /coded_by="NM_001134607.1:136..1686"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:498831"
                     /db_xref="RGD:1562608"
ORIGIN      
        1 meslkgagds vaeqsfckrg lksaslkdlc vedkrrianl ikelarvsee kevteerlkt
       61 eqesfekkir qleeqnelii keredillky recqellsly qkylseqqek ltmslselga
      121 araqeqqitk kkithqsslv nldgsylsva kpqtcqtrar pksenqdsas eshtalrnns
      181 lkpvtlhhpk qdlermstet rtctyespgr rlinaapvee alpeelkikd ypnllptpss
      241 qycghkyses eayvhenyhp tnmasqcckt hpescshcrm swaslmhdgv tlqpretdie
      301 kqlsedrrqq lmlqkmelei ekerlqqlla qqetklllkq qqlhqsrldy ncllkpkcdg
      361 wlrgtsssfr kcpdspnsaq nqkekktvef qshvengiqw tcqqndtcrl qretatgvrk
      421 dastspmstq spkhpltpas ssskhktsry etslldlvqs lspnsapkcq phssraagtw
      481 salrptpkts twkkvgthks pedleenqil ediffi
//
LOCUS       NP_036887                537 aa            linear   ROD 03-APR-2025
DEFINITION  tyrosine-protein kinase Fyn [Rattus norvegicus].
ACCESSION   NP_036887 XP_001062721
VERSION     NP_036887.1
DBSOURCE    REFSEQ: accession NM_012755.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Li,H., Zhou,X., Chen,R., Xiao,Y. and Zhou,T.
  TITLE     The Src-Kinase Fyn is Required for Cocaine-Associated Memory
            Through Regulation of Tau
  JOURNAL   Front Pharmacol 13, 769827 (2022)
   PUBMED   35185557
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,L., Wang,L., Xiao,H., Gan,H., Chen,H., Zheng,S., Jian,D.,
            Zhai,X., Jiang,N., Jing,Z. and Liang,P.
  TITLE     Tyrosine kinase Fyn promotes apoptosis after intracerebral
            hemorrhage in rats by activating Drp1 signaling
  JOURNAL   J Mol Med (Berl) 99 (3), 359-371 (2021)
   PUBMED   33409551
  REMARK    GeneRIF: Tyrosine kinase Fyn promotes apoptosis after intracerebral
            hemorrhage in rats by activating Drp1 signaling.
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Luo,X., Li,Z., Zhao,J., Deng,Y., Zhong,Y. and Zhang,M.
  TITLE     Fyn gene silencing reduces oligodendrocytes apoptosis through
            inhibiting ERK1/2 phosphorylation in epilepsy
  JOURNAL   Artif Cells Nanomed Biotechnol 48 (1), 298-304 (2020)
   PUBMED   31852295
  REMARK    GeneRIF: Fyn gene silencing reduced the apoptosis of OLs through
            inhibiting the phosphorylation of ERK1/2 in epileptic model
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Egervari,G., Akpoyibo,D., Rahman,T., Fullard,J.F., Callens,J.E.,
            Landry,J.A., Ly,A., Zhou,X., Warren,N., Hauberg,M.E., Hoffman,G.,
            Ellis,R., Ferland,J.N., Miller,M.L., Keller,E., Zhang,B.,
            Roussos,P. and Hurd,Y.L.
  TITLE     Chromatin accessibility mapping of the striatum identifies tyrosine
            kinase FYN as a therapeutic target for heroin use disorder
  JOURNAL   Nat Commun 11 (1), 4634 (2020)
   PUBMED   32929078
  REMARK    GeneRIF: Chromatin accessibility mapping of the striatum identifies
            tyrosine kinase FYN as a therapeutic target for heroin use
            disorder.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Mao,L.M. and Wang,J.Q.
  TITLE     Linkage of Non-receptor Tyrosine Kinase Fyn to mGlu5 Receptors in
            Striatal Neurons in a Depression Model
  JOURNAL   Neuroscience 433, 11-20 (2020)
   PUBMED   32145272
  REMARK    GeneRIF: Linkage of Non-receptor Tyrosine Kinase Fyn to mGlu5
            Receptors in Striatal Neurons in a Depression Model.
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Grant,S.G., O'Dell,T.J., Karl,K.A., Stein,P.L., Soriano,P. and
            Kandel,E.R.
  TITLE     Impaired long-term potentiation, spatial learning, and hippocampal
            development in fyn mutant mice
  JOURNAL   Science 258 (5090), 1903-1910 (1992)
   PUBMED   1361685
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Bell,G.M., Bolen,J.B. and Imboden,J.B.
  TITLE     Association of Src-like protein tyrosine kinases with the CD2 cell
            surface molecule in rat T lymphocytes and natural killer cells
  JOURNAL   Mol Cell Biol 12 (12), 5548-5554 (1992)
   PUBMED   1280324
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Alai,M., Mui,A.L., Cutler,R.L., Bustelo,X.R., Barbacid,M. and
            Krystal,G.
  TITLE     Steel factor stimulates the tyrosine phosphorylation of the
            proto-oncogene product, p95vav, in human hemopoietic cells
  JOURNAL   J Biol Chem 267 (25), 18021-18025 (1992)
   PUBMED   1381360
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Appleby,M.W., Gross,J.A., Cooke,M.P., Levin,S.D., Qian,X. and
            Perlmutter,R.M.
  TITLE     Defective T cell receptor signaling in mice lacking the thymic
            isoform of p59fyn
  JOURNAL   Cell 70 (5), 751-763 (1992)
   PUBMED   1516132
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Beyers,A.D., Spruyt,L.L. and Williams,A.F.
  TITLE     Molecular associations between the T-lymphocyte antigen receptor
            complex and the surface antigens CD2, CD4, or CD8 and CD5
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2945-2949 (1992)
   PUBMED   1372996
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001062721.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U35365.1, SRR26643295.60207.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..537
                     /product="tyrosine-protein kinase Fyn"
                     /EC_number="2.7.10.2"
                     /note="proto-oncogene tyrosine-protein kinase Fyn; FYN
                     oncogene related to SRC, FGR, YES; p59-Fyn; proto-oncogene
                     c-Fyn"
                     /calculated_mol_wt=60571
     Region          14..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62844.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06241; propagated from
                     UniProtKB/Swiss-Prot (Q62844.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06241; propagated from
                     UniProtKB/Swiss-Prot (Q62844.1)"
     Region          85..140
                     /region_name="SH3_Fyn_Yrk"
                     /note="Src homology 3 domain of Fyn and Yrk Protein
                     Tyrosine Kinases; cd12006"
                     /db_xref="CDD:212939"
     Site            order(91,93,96..97,100,116..119,132,134,136..137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Site            order(93,96..100,116,119,132)
                     /site_type="other"
                     /note="SAP interaction site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Region          145..245
                     /region_name="SH2_Src_Fyn_isoform_a_like"
                     /note="Src homology 2 (SH2) domain found in Fyn isoform a
                     like proteins; cd10418"
                     /db_xref="CDD:198281"
     Site            order(156,176,178..181,186,202,204,237)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198281"
     Site            order(156,176,202,204)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198281"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39688; propagated from
                     UniProtKB/Swiss-Prot (Q62844.1)"
     Site            order(203,231)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198281"
     Region          261..534
                     /region_name="PTKc_Fyn"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fyn; cd05070"
                     /db_xref="CDD:270655"
     Site            order(277,279..281,285,297,299,342..345,349,390,394..395,
                     397,408,425..429,438,472)
                     /site_type="active"
                     /db_xref="CDD:270655"
     Site            order(277,280,285,297,299,342..345,349,390,392,395,397,
                     408)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270655"
     Site            order(291,293,325,328,330,343,369,373,401,521)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(379,382..383,446,508..510,512,514..515,518,522,
                     525..526,530)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(390,394,425..429,438,472)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270655"
     Site            407..431
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270655"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P39688; propagated from
                     UniProtKB/Swiss-Prot (Q62844.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62844.1)"
     CDS             1..537
                     /gene="Fyn"
                     /coded_by="NM_012755.2:232..1845"
                     /db_xref="GeneID:25150"
                     /db_xref="RGD:2641"
ORIGIN      
        1 mgcvqckdke aaklteerdg slnqssgyry gtdptpqhyp sfgvtsipny nnfhaaggqg
       61 ltvfggvnss shtgtlrtrg gtgvtlfval ydyeartedd lsfhkgekfq ilnssegdww
      121 earslttget gyipsnyvap vdsiqaeewy fgklgrkdae rqllsfgnpr gtflireset
      181 tkgayslsir dwddmkgdhv khykirkldn ggyyittraq fetlqqlvqh yseraaglcc
      241 rlvvpchkgm prltdlsvkt kdvweipres lqlikrlgng qfgevwmgtw ngntkvaikt
      301 lkpgtmspes fleeaqimkk lkhdklvqly avvseepiyi vteymnkgsl ldflkdgegr
      361 alklpnlvdm aaqvaagmay iermnyihrd lrsanilvgn glickiadfg larliedney
      421 tarqgakfpi kwtapeaaly grftiksdvw sfgilltelv tkgrvpypgm nnrevleqve
      481 rgyrmpcpqd cpislhelmi hcwkkdpeer ptfeylqgfl edyftatepq yqpgenl
//
LOCUS       NP_001092987             843 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 72 [Rattus norvegicus].
ACCESSION   NP_001092987 XP_001068097 XP_001068149 XP_001068193
VERSION     NP_001092987.2
DBSOURCE    REFSEQ: accession NM_001099517.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 3, 2021 this sequence version replaced NP_001092987.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..843
                     /product="vomeronasal 2 receptor, 72"
                     /calculated_mol_wt=95769
     Region          45..501
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,167..168,392)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(111,114,157,241)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          509..563
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          583..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          583..608
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(586,589..590,593..594,596..597,631,635,638..639,647,
                     651)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          620..641
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(640,652..653,656..657,660,740,745,748..749,752,786,
                     789..790,793,797,805..806,809,812,816)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          650..674
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          698..714
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          741..767
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          775..798
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          803..828
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..843
                     /gene="Vom2r72"
                     /coded_by="NM_001099517.2:1..2532"
                     /db_xref="GeneID:689072"
                     /db_xref="RGD:1597414"
ORIGIN      
        1 mkklcafpit flilkfsliy fhltepscfw riknseetdg dlrsdcgfvl lafeepieen
       61 yynelinfri patkyefflv mffatdeink npdllpnmsl ifnlvgrmce dtlglldeiy
      121 sqenktsyii nyvcgielsc didligpsrt tslklaihsm mpkvffgpfn snlidhdqfp
      181 yiyqiaikdt clphgmvslm lqfgwtwvgl iisdndqgiq ffsdlreemq rhgiclafvn
      241 vipetmqrys trakiydkql mtssakvvii ygemnstlev sfrrwaylgv qriwvtnsqw
      301 dviinkrdfs ldffhgtvtf ahhhsgmtif rnvmqtmnts kypidlsqsm lgwnyfncsi
      361 senrhsktdh ftfnntlewl alhkfdmvls eegynlynav yavahtyhel isqnvesqkv
      421 aepkglftdc qqvasllkat vftnpvgelv nmnhrenqca eydifiiwnf peglglkvki
      481 asyfpcfphn qqlhtsedle wategtlvps smcsatctag frkihqkqta dccfdcvqcp
      541 enevsnetad meqcarcpdd kyanseqtyc lqrtvsflay edplgmalgc malffsaiti
      601 lvlvtfvkyk dtpivkannc ilsyillisl ifcflcsllf ighpnkatci lqqttfgvff
      661 tvavsavlak tvtvvmafkl ttpgrrmrgm lasgatnlvi pictliqlvl ygiwlaispp
      721 fidrdiqseh gktiiicnkg sviafhfvlg ylgslalgsi tvaflarnlp drfneakflt
      781 fsmlvfysvw itflpvyhst rgkvmvvvev fsilassagl lgcifvpkcy vilvrpdlnf
      841 lqk
//
LOCUS       NP_001092932             842 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 5 precursor [Rattus norvegicus].
ACCESSION   NP_001092932 XP_001053048 XP_001053116
VERSION     NP_001092932.1
DBSOURCE    REFSEQ: accession NM_001099462.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_001053116.1, XP_001053048.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..842
                     /product="vomeronasal 2 receptor, 5 precursor"
                     /calculated_mol_wt=93428
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2935
     Region          45..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,167..168,391)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          508..562
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          582..833
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          582..607
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(585,588..589,592..593,595..596,630,634,637..638,646,
                     650)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          619..640
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(639,651..652,655..656,659,739,744,747..748,751,785,
                     788..789,792,796,804..805,808,811,815)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          649..673
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          697..713
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          740..766
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          774..797
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          802..827
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..842
                     /gene="Vom2r5"
                     /coded_by="NM_001099462.1:1..2529"
                     /db_xref="GeneID:679691"
                     /db_xref="RGD:1585898"
ORIGIN      
        1 mkklcaftia ifslkfclil csltepncfw rikssedndg dlrsdcgfvl fthegpiped
       61 fyndiinfri parkyefflv llfatdeink npyllpnmsl ifniifglce dtlgvldkay
      121 lhqnsnself nyycginqlc dvdltgpswt tslklsiysr tpkiffgsfn pnlsdhdqfp
      181 yiyqiaakdt ylfhgmvslm fhfgwtwigl visdddqgiq flsdlreemq rhaiclafvn
      241 mipetmqiyk trvkiydqql mtssakvvii ygevnstlel sfrrwaylga qriwittsqw
      301 dvithkkdfs ldfshgtvtf ahhhndiavf rnfmqtints mypvdisqsm lqwnhfncsi
      361 sknkkkmdcf tfknplewli qhtfdmvlse egynlynavy avahtyhkli fqqvesqkme
      421 epkglftdcq qvtsllktie ftnpvgelvd tkhkenqcat ydifitwnfp qglglkvkig
      481 syfpclpqsq qlhisedwew vtgetlipps vcsmtctagf rkihqketad ccfdcvqcqe
      541 neiandtadm eqcvkcpdds yanleqsqcl qrvvtflaye dplgmalgcm alsfsaitil
      601 vlvtfvkykd tpivkannri lsyillislv fcflcsllyi ghpnqatcil qqttfaifft
      661 vaistvlakt itvvtafklt tperrikkim ikgainllip ictliqlvlc avwlvisppf
      721 idrdiqsehg kviiicnkgs viafhfvlgy lgslalgsft vaflarnlpd rfneakfltf
      781 smlvfysvwi tflpvyhstr gkdmvivevf silassagll gciffqkcyv llvrpdlnvl
      841 rk
//
LOCUS       NP_085073                213 aa            linear   ROD 03-APR-2025
DEFINITION  sclerostin precursor [Rattus norvegicus].
ACCESSION   NP_085073
VERSION     NP_085073.1
DBSOURCE    REFSEQ: accession NM_030584.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Osumi,R., Wang,Z., Ishihara,Y., Odagaki,N., Iimura,T. and
            Kamioka,H.
  TITLE     Changes in the intra- and peri-cellular sclerostin distribution in
            lacuno-canalicular system induced by mechanical unloading
  JOURNAL   J Bone Miner Metab 39 (2), 148-159 (2021)
   PUBMED   32844318
  REMARK    GeneRIF: Changes in the intra- and peri-cellular sclerostin
            distribution in lacuno-canalicular system induced by mechanical
            unloading.
            Erratum:[J Bone Miner Metab. 2021 Mar;39(2):160-162. doi:
            10.1007/s00774-020-01155-5. PMID: 33025107]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Huang,Y., Wang,X., Wu,F., Lu,Y., Liang,G. and Liu,A.
  TITLE     The Possible Role of Sclerostin in the Pathogenesis of
            Tympanosclerosis
  JOURNAL   Audiol Neurootol 26 (2), 102-110 (2021)
   PUBMED   33508832
  REMARK    GeneRIF: The Possible Role of Sclerostin in the Pathogenesis of
            Tympanosclerosis.
REFERENCE   3  (residues 1 to 213)
  AUTHORS   De Mare,A., Maudsley,S., Azmi,A., Hendrickx,J.O., Opdebeeck,B.,
            Neven,E., D'Haese,P.C. and Verhulst,A.
  TITLE     Sclerostin as Regulatory Molecule in Vascular Media Calcification
            and the Bone-Vascular Axis
  JOURNAL   Toxins (Basel) 11 (7), 428 (2019)
   PUBMED   31330917
  REMARK    GeneRIF: Sclerostin as Regulatory Molecule in Vascular Media
            Calcification and the Bone-Vascular Axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Korn,P., Kramer,I., Schlottig,F., Todtman,N., Eckelt,U., Burki,A.,
            Ferguson,S.J., Kautz,A., Schnabelrauch,M., Range,U., Kneissel,M.
            and Stadlinger,B.
  TITLE     Systemic sclerostin antibody treatment increases osseointegration
            and biomechanical competence of zoledronic-acid-coated dental
            implants in a rat osteoporosis model
  JOURNAL   Eur Cell Mater 37, 333-346 (2019)
   PUBMED   31112281
  REMARK    GeneRIF: The combination of ZOL and the osteoanabolic sclerostin
            antibody was more effective than either agent alone.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Wang,J., Qiu,X., Xu,T., Sheng,Z. and Yao,L.
  TITLE     Sclerostin/Receptor Related Protein 4 and Ginkgo Biloba Extract
            Alleviates beta-Glycerophosphate-Induced Vascular Smooth Muscle
            Cell Calcification By Inhibiting Wnt/beta-Catenin Pathway
  JOURNAL   Blood Purif 47 Suppl 1 (Suppl 1), 17-23 (2019)
   PUBMED   30699436
  REMARK    GeneRIF: beta-GP induced VSMC calcification by activating the
            Wnt/beta-catenin signaling pathway. Sclerostin and Lrp4 were
            involved in beta-GP-induced VSMC calcification and play an
            important role. GBE could alleviate VSMC calcification induced by
            beta-GP through inhibiting the Wnt/beta-catenin signaling pathway.
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Keller,H. and Kneissel,M.
  TITLE     SOST is a target gene for PTH in bone
  JOURNAL   Bone 37 (2), 148-158 (2005)
   PUBMED   15946907
  REMARK    GeneRIF: SOST regulation may play a role in mediating PTH action in
            bone
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Semenov,M., Tamai,K. and He,X.
  TITLE     SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor
  JOURNAL   J Biol Chem 280 (29), 26770-26775 (2005)
   PUBMED   15908424
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Winkler,D.G., Yu,C., Geoghegan,J.C., Ojala,E.W., Skonier,J.E.,
            Shpektor,D., Sutherland,M.K. and Latham,J.A.
  TITLE     Noggin and sclerostin bone morphogenetic protein antagonists form a
            mutually inhibitory complex
  JOURNAL   J Biol Chem 279 (35), 36293-36298 (2004)
   PUBMED   15199066
  REMARK    GeneRIF: noggin and sclerostin form a mutually inhibitory complex
            that fine-tunes of BMP activity in bone homeostasis
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Winkler,D.G., Sutherland,M.K., Geoghegan,J.C., Yu,C., Hayes,T.,
            Skonier,J.E., Shpektor,D., Jonas,M., Kovacevich,B.R.,
            Staehling-Hampton,K., Appleby,M., Brunkow,M.E. and Latham,J.A.
  TITLE     Osteocyte control of bone formation via sclerostin, a novel BMP
            antagonist
  JOURNAL   EMBO J 22 (23), 6267-6276 (2003)
   PUBMED   14633986
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Brunkow,M.E., Gardner,J.C., Van Ness,J., Paeper,B.W.,
            Kovacevich,B.R., Proll,S., Skonier,J.E., Zhao,L., Sabo,P.J., Fu,Y.,
            Alisch,R.S., Gillett,L., Colbert,T., Tacconi,P., Galas,D.,
            Hamersma,H., Beighton,P. and Mulligan,J.
  TITLE     Bone dysplasia sclerosteosis results from loss of the SOST gene
            product, a novel cystine knot-containing protein
  JOURNAL   Am J Hum Genet 68 (3), 577-589 (2001)
   PUBMED   11179006
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF326741.1, BE101082.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..213
                     /product="sclerostin precursor"
                     /note="sclerosteosis"
                     /calculated_mol_wt=21035
     Region          1..210
                     /region_name="GHB_like"
                     /note="Glycoprotein hormone beta chain homologues;
                     cl21545"
                     /db_xref="CDD:473907"
     sig_peptide     1..28
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99P67.1)"
                     /calculated_mol_wt=2958
     mat_peptide     29..213
                     /product="Sclerostin. /id=PRO_0000033179"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P67.1)"
                     /calculated_mol_wt=21035
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99P67.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99P67.1)"
     Region          178..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P67.1)"
     CDS             1..213
                     /gene="Sost"
                     /coded_by="NM_030584.2:28..669"
                     /db_xref="GeneID:80722"
                     /db_xref="RGD:69358"
ORIGIN      
        1 mqlslapcla cllvhaafva vesqgwqafk ndateiipgl reypeppqel ennqtmnrae
       61 nggrpphhpy dtkdvseysc relhytrfvt dgpcrsakpv telvcsgqcg parllpnaig
      121 rvkwwrpngp dfrcipdryr aqrvqllcpg gaaprsrkvr lvasckckrl trfhnqselk
      181 dfgpetarpq kgrkprprar gakanqaele nay
//
LOCUS       NP_001178710             425 aa            linear   ROD 03-APR-2025
DEFINITION  probable imidazolonepropionase [Rattus norvegicus].
ACCESSION   NP_001178710 XP_235065
VERSION     NP_001178710.1
DBSOURCE    REFSEQ: accession NM_001191781.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Jul 17, 2010 this sequence version replaced XP_235065.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.22356.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..425
                     /product="probable imidazolonepropionase"
                     /EC_number="3.5.2.7"
                     /calculated_mol_wt=46440
     Region          42..419
                     /region_name="Imidazolone-5PH"
                     /note="Imidazolonepropionase/imidazolone-5-propionate
                     hydrolase (Imidazolone-5PH) catalyzes the third step in
                     the histidine degradation pathway, the hydrolysis of
                     (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to
                     N-formimidoyl-L-glutamate. In bacteria; cd01296"
                     /db_xref="CDD:238621"
     Site            order(86,88,259,262,282,333)
                     /site_type="active"
                     /db_xref="CDD:238621"
     CDS             1..425
                     /gene="Amdhd1"
                     /gene_synonym="RGD1308879"
                     /coded_by="NM_001191781.1:13..1290"
                     /db_xref="GeneID:299735"
                     /db_xref="RGD:1308879"
ORIGIN      
        1 mnghrlllen aqqvvlvcar gelyltgsel rslavlegas lvvgtdglik avgpadiirr
       61 qfsgetfeer idcsgkcilp glvdahthpv wagervhefa mklagatymd ihqaggginf
      121 tvehtrqase eelfrsfqqr lqcmmragtt lvecksgygl nletelkmlr vierarrelh
      181 lslsatycga hsvpkgktav eaaddiishh lprlkelsek gelhvdnidv fcekgvfdld
      241 ttrrileggk kvglqinfhg delhpmkaae lgaelgarai shleevsdeg iaamaaaqcs
      301 avllpttaym lrlkqprark mldegvival gsdfnpnayc fsmpmvmhla cvnmrmsmpe
      361 alaaatinaa yalgkshthg slevgkqgda iiinasrweh liyqfgghqe lidyvitkgk
      421 viykk
//
LOCUS       NP_001092939             858 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 10 [Rattus norvegicus].
ACCESSION   NP_001092939 XP_001058365 XP_218017
VERSION     NP_001092939.1
DBSOURCE    REFSEQ: accession NM_001099469.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On or before Aug 19, 2007 this sequence version replaced
            XP_218017.4, XP_001058365.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..858
                     /product="vomeronasal 2 receptor 10"
                     /calculated_mol_wt=98433
     Region          43..502
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(78,176..177,396)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(116,119,163,250)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          510..563
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          583..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          583..608
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(586,589..590,593..594,596..597,631,635,638..639,647,
                     651)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          620..641
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(640,652..653,656..657,660,740,745,748..749,752,786,
                     789..790,793,797,805..806,809,812,816)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          650..674
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          698..714
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          741..767
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          775..798
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          803..828
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..858
                     /gene="Vom2r10"
                     /gene_synonym="RGD1565464"
                     /coded_by="NM_001099469.1:1..2577"
                     /db_xref="GeneID:292414"
                     /db_xref="RGD:1565464"
ORIGIN      
        1 mmfswififw llqilkfvsa ivfnisrcyy iiteefhheg divigaffpl htfytgkkmp
       61 dptlpyqyld nyiqynfrny qyilallfai eeingnpnll pnislgfdfy nvrfteketl
      121 mnaviwltah vqrkvlpnyn ckkkkfsaal tgtswttsaq igtllqlfkf pqitfgpydp
      181 llsdhgqyss lyqmapkdts lslaivslmv yfrwswvgli lpddhkgnki lsdyreemer
      241 qrvciafvkm ipatwtsyfp rfwenmnetn viiihgdids lesllrnigq rlltrnvwvm
      301 nierhvtefs dyfmldsfhg slifkhnyre kfeftkfiqt vnpnrypedi ylpklwnllf
      361 kcsfsdrncq vldncqtnas ldilpshifd vamseesisi yngvyavahs lhdmrlhqvq
      421 mrpyengegm ifipwqlntf lkdlevrdnr slnwiqtida eydilnlwnl pkglglkvki
      481 gsfsanapkg qqlslseqii qwpeifskvp qsvcsescgp gfrkvtlegk piccykctpc
      541 aeneisnetd sdqcvrcpes hypnteksnc yqktssflaf eeplgmalas ialclsalta
      601 fvigifvkyr dtpivkannq alsyillitl kfcflcslnf igqpntaaci lqqttfgvaf
      661 tvalatvlak aitvvlafkv sfpgrmvrwl misrgpyyiv pictliqlll cgiwmtmspp
      721 fidqdphteh ghiiilcnkg sslafhavlg ylcllalgsy tmaflsrnlp dtfneskfls
      781 lsmlvffcvw vtflpvyyst kgkvmvamev fsilasstal lafifgpkcy iillrpdkns
      841 fnhvrkkahf rrknspki
//
LOCUS       NP_001178899            1645 aa            linear   ROD 03-APR-2025
DEFINITION  thrombospondin type-1 domain-containing protein 7A precursor
            [Rattus norvegicus].
ACCESSION   NP_001178899 XP_575387
VERSION     NP_001178899.2
DBSOURCE    REFSEQ: accession NM_001191970.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1645)
  AUTHORS   Aktepe,O.H., Sahin,T.K., Guner,G., Guven,D.C., Yeter,H.H.,
            Kurtulan,O., Ozercan,I.H., Dizdar,O. and Yalcin,S.
  TITLE     Correlation Between THSD7A Expression and Tumor Characteristics of
            Azoxymethane-Induced Colon Cancer Model in Rats
  JOURNAL   Turk J Gastroenterol 32 (12), 1049-1056 (2021)
   PUBMED   34876395
  REMARK    GeneRIF: Correlation Between THSD7A Expression and Tumor
            Characteristics of Azoxymethane-Induced Colon Cancer Model in Rats.
REFERENCE   2  (residues 1 to 1645)
  AUTHORS   Tomas,N.M., Hoxha,E., Reinicke,A.T., Fester,L., Helmchen,U.,
            Gerth,J., Bachmann,F., Budde,K., Koch-Nolte,F., Zahner,G., Rune,G.,
            Lambeau,G., Meyer-Schwesinger,C. and Stahl,R.A.
  TITLE     Autoantibodies against thrombospondin type 1 domain-containing 7A
            induce membranous nephropathy
  JOURNAL   J Clin Invest 126 (7), 2519-2532 (2016)
   PUBMED   27214550
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On Feb 3, 2021 this sequence version replaced NP_001178899.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1645
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q21"
     Protein         1..1645
                     /product="thrombospondin type-1 domain-containing protein
                     7A precursor"
                     /note="thrombospondin type-1 domain-containing protein 7A;
                     thrombospondin, type I, domain containing 7A"
                     /calculated_mol_wt=180094
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3704
     Region          184..235
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          350..401
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          502..562
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Region          624..683
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          688..756
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1025..>1065
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          1088..1150
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1155..1206
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          1276..1329
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Region          1404..1463
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     CDS             1..1645
                     /gene="Thsd7a"
                     /gene_synonym="RGD1566201"
                     /coded_by="NM_001191970.2:1..4938"
                     /db_xref="GeneID:500032"
                     /db_xref="RGD:1566201"
ORIGIN      
        1 mglragrlas lsrgvlqlmr lpllllllls sgargaaaqg dtevptlylw ktgpwgrcmg
       61 ddcgpggiqt ravwcahseg wttlhtnckq avrpsnqqnc fkvcdwhkel ydwrlgpwnq
      121 cqpvisksle karecvkgee giqvreitci qkdkdipaed iiceyfepkp lleqaclipc
      181 qqdcivsefs swsecsrtcg sglqhrtrhv vappqfggsg cpnltefqvc qsnpceaees
      241 myslqvgpws acsvphsrqa rqarrrgknk erekergkav kdpearelik kkrnrnrqnr
      301 qenrywdiqi gyqtrdvmcl nrtgksadls fcqqerlpmt fqscvitkec qvsewsewsp
      361 csktchdvts ptgtrvrtrt irqfpigsek ecpeleekep clsqgdgavl catygwrtte
      421 wtechvdpll sqqdkrranq talcgggvqt reiyciqtnd illshintqk dkeaskpvds
      481 klctgpvpnt tqlchvpcpi ecevspwsaw gpctyencnd qqgkkgfklr krritneptg
      541 gsgatgncph lleaipceep scydwksvrl gdcepdngka cgpgtqvqev vcinsdgeev
      601 drqlcrdaif pipvacdapc pkdcvlsaws twsscshtcs gkttegkqir arsilayage
      661 eggircpnss alqevrscne hpctvyhwqt gpwgqciedt svssfntttt wtgetscsvg
      721 mqtrkvicvr vnvgqvgpkk cpeslrpetv rpcllpcrkd cimtpysdwt pcpsscregd
      781 sgarkqsrqr viiqlpaygg recsdplyee kaceapptch syrwkthkwr rcqlvpwsiq
      841 qdvpgaqegc gpgrqarait crkqdggqas iqeclqyagp vpaltqacqi pcqddcqfts
      901 wskfsscngd cgavrtrkra ivgkskkkek cknshlypli etqycpcdky naqpvgnwsd
      961 cilpegkaev llgvkvqgdn kecgqgyryq amacydqngr lvetsrcnsh gyieeaciip
     1021 cpsdcklsew snwsrcsksc gsgvkvrskw lrekpynggr pcpkldhvnq aqvyevvpch
     1081 sdcnqyiwvt epwsvckvtf vdmrdncgeg vqtrkvrcmq ntadgpsehv edylcdpedm
     1141 plgsrecklp cpedcvisew gpwtqcslpc npsgsrqrsa dpirqpadeg racpdaveke
     1201 pcnlnkncyr ydynvtdwst cqlsekavcg ngiktrmldc vrsdgksvdl kyceelglek
     1261 nwqmnssctv ecplncqlsd wspwsecsqt cgltgkmirr rtvtqpfqgd grpcpslmeq
     1321 skpcpvkpcy rwqygqwspc qvqeaqcgeg trtrniscvv sdgsaddfsk avdeefcani
     1381 eliidgnkqi vleetctqpc pgdcylndws swslcqltcv ngedlgfggi qvrsraviiq
     1441 elenqhlcpe qiletkscdd gqcyeykwma sawkgssrtv wcqrsdgvnv tggclvvsqp
     1501 dadrscnppc sqphsycsem kacrceegyt evmssnstle qctlipvvvi ptvedkrdvk
     1561 tsravhptqp ssnpagrgrt wflqpfgpdg rlktwvygva agafvllvfi vsmiylackk
     1621 pkkpqrrqnn rlkpltlayd gdadm
//
LOCUS       NP_001100266             280 aa            linear   ROD 03-APR-2025
DEFINITION  homeobox protein Hox-C12 [Rattus norvegicus].
ACCESSION   NP_001100266 XP_001068476 XP_235696
VERSION     NP_001100266.1
DBSOURCE    REFSEQ: accession NM_001106796.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474035.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001068476.1, XP_235696.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..280
                     /product="homeobox protein Hox-C12"
                     /calculated_mol_wt=30177
     Region          213..269
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..280
                     /gene="Hoxc12"
                     /coded_by="NM_001106796.1:1..843"
                     /db_xref="GeneID:300262"
                     /db_xref="RGD:1310539"
ORIGIN      
        1 mgehnllnpg fvgplvniht gdtfyfpnfr asgaqlpglp slsyprrdnv cslpwpsaep
       61 cngypqpylg spvslnppfg rtcelarved skgyyrepca eggggglkre ergrepgagp
      121 gaallqleps gppalgfkyd ypagggggdg ntgpphdpps cqslesdsss sllnegnkga
      181 sagdpgslvs plnpggglsa sgapwypihs rsrkkrkpys klqlaelege flvnefitrq
      241 rrrelsdrln lsdqqvkiwf qnrrmkkkrl llreqalsff
//
LOCUS       NP_001396169             328 aa            linear   ROD 03-APR-2025
DEFINITION  mas-related G-protein coupled receptor member B8-like [Rattus
            norvegicus].
ACCESSION   NP_001396169 XP_038952139
VERSION     NP_001396169.1
DBSOURCE    REFSEQ: accession NM_001409240.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Jul 12, 2022 this sequence version replaced XP_038952139.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..328
                     /product="mas-related G-protein coupled receptor member
                     B8-like"
                     /calculated_mol_wt=36883
     Region          31..308
                     /region_name="7tmA_MrgprB"
                     /note="mas-related G protein-coupled receptor subtype B,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15107"
                     /db_xref="CDD:320235"
     Region          32..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320235"
     Region          64..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320235"
     Site            order(85,88,90,104..109,111..112,115,158,160..164,187,
                     190..192,194..196,198..199,236,239..240,242..243,246,
                     258..259,261..263,266,269..270)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320235"
     Region          104..132
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320235"
     Region          144..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320235"
     Region          187..212
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320235"
     Region          216..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320235"
     Region          259..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320235"
     CDS             1..328
                     /gene="LOC120093062"
                     /coded_by="NM_001409240.1:1..987"
                     /db_xref="GeneID:120093062"
                     /db_xref="RGD:41298225"
ORIGIN      
        1 mdssipdpea dliqlngsyh tetspcvies rvmillsiii affglagnam vlwllafrmr
       61 rnvfsvyiln laganflflc thtafsleki ivlfhsvhih ipllfytlst laylagvsmv
      121 taisaeywls giwpywyqgq rlkhtttvic tglwglalll sllegkscgf lgstynqdvc
      181 wkldfiivaw llvlfavlsr siqvllvrif cgsqrtpvtk lhvtivltal vlvicgfpfg
      241 iifyllywtt evyyimpcns fhetilllsy inscanpiic llvgsirhcr fqcgtlrlll
      301 hramqdipee egeeleevvg ervqssip
//
LOCUS       NP_001092933             858 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 7 [Rattus norvegicus].
ACCESSION   NP_001092933 XP_001064298
VERSION     NP_001092933.1
DBSOURCE    REFSEQ: accession NM_001099463.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 18, 2007 this sequence version replaced XP_001064298.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..858
                     /product="vomeronasal 2 receptor, 7"
                     /calculated_mol_wt=98048
     Region          43..502
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          510..563
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          583..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          583..608
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(586,589..590,593..594,596..597,631,635,638..639,647,
                     651)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          620..641
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(640,652..653,656..657,660,740,745,748..749,752,786,
                     789..790,793,797,805..806,809,812,816)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          650..674
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          698..714
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          741..767
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          775..798
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          803..828
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..858
                     /gene="Vom2r7"
                     /coded_by="NM_001099463.1:1..2577"
                     /db_xref="GeneID:685557"
                     /db_xref="RGD:1592591"
ORIGIN      
        1 mfywifiswf lqipkfvssf mtvnislcfy ktpedfhyeg dvvigaffpi htyyspnkvp
       61 hktvpyqymd nylqynfkny qyilalvlai eeingnpnll pnislgfdfy nirfteketl
      121 mnaciwitgq gqkkilpnyn cnkrvftaal tgtswtasaq igtllqlfkf pqlsfgpydp
      181 ilsdrgqyss lyqmtpkyts lsqgivslmv hfrwswvgii lpddhkgnki lsefrenmek
      241 kgvciafvki ipftwtkyfn kfwenmdetn viiiysdids itgimrnigq rlltwkvwvm
      301 niephitdya dyfmldsfhg slifthhfke sfeltkfiqt vnpykypedi ylpklwhlff
      361 kcsfsdidcq llancqsnas ldvlpshild maiseesnti ynavyavahs lhqmtlqqve
      421 iqpqengevm tffpwqlnif lkdidkrdnm slggrkklna eydifnlwnl pkglgrkvki
      481 gsfsgnapeg qqlslsepmi qwaerfseip qsvcskscmp gfrkvtlegk aiccynctpc
      541 adneisnetd vdqcmkcpes hyanpeknhc fqktvsflay edplgmilas islclsalta
      601 fvigvfvkyr etpivkannr glsytlliti tfcllcslnf igqpnaatci fqqtifgiaf
      661 tvalatvlak aitvviafka tipgrmvrwl misrapnyii pictliqlll caiwmatspp
      721 fidqdfhaeh ghilllcnkg sslafhcvlg ylcslaiggy tmaflsrnlp dtfneskfls
      781 fsmlvffcvw vtflpvyhst kgkvmvamev fsilassaal lgfifapkcy iillrpekns
      841 fhhmrdkths rknksiki
//
LOCUS       NP_001078850             396 aa            linear   ROD 03-APR-2025
DEFINITION  gap junction gamma-1 protein [Rattus norvegicus].
ACCESSION   NP_001078850 XP_001081521
VERSION     NP_001078850.1
DBSOURCE    REFSEQ: accession NM_001085381.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Luetic,M., Kretzschmar,G., Grobe,M., Jercic,L., Bota,I., Ivic,V.,
            Balog,M., Zjalic,M., Vitlov Uljevic,M., Heffer,M., Gaspar,R.,
            Tabi,T., Vukojevic,K., Vari,S.G. and Filipovic,N.
  TITLE     Sex-specific effects of metformin and liraglutide on renal
            pathology and expression of connexin 45 and pannexin 1 following
            long-term high-fat high-sugar diet
  JOURNAL   Acta Histochem 123 (8), 151817 (2021)
   PUBMED   34808525
  REMARK    GeneRIF: Sex-specific effects of metformin and liraglutide on renal
            pathology and expression of connexin 45 and pannexin 1 following
            long-term high-fat high-sugar diet.
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Nagy,J.I. and Rash,J.E.
  TITLE     Cx36, Cx43 and Cx45 in mouse and rat cerebellar cortex:
            species-specific expression, compensation in Cx36 null mice and
            co-localization in neurons vs. glia
  JOURNAL   Eur J Neurosci 46 (2), 1790-1804 (2017)
   PUBMED   28561933
  REMARK    GeneRIF: Cx45-puncta in the cerebellar molecular layer were
            co-localized with Cx36-puncta and additionally occurred along
            Bergmann glial processes adjacent to Cx43-puncta. Expression of
            both Cx43 and Cx45 in Bergmann glia of rat may contribute to the
            complex properties of junctional coupling between these cells and
            perhaps to their reported coupling with Purkinje cells.
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Beheshti,S., Zeinali,R. and Esmaeili,A.
  TITLE     Rapid upregulation of the hippocampal connexins 36 and 45 mRNA
            levels during memory consolidation
  JOURNAL   Behav Brain Res 320, 85-90 (2017)
   PUBMED   27913256
  REMARK    GeneRIF: The results of the present study revealed that during
            memory consolidation in a passive avoidance paradigm, a rapid
            upregulation of Cx45 mRNAs level occurs in the hippocampus, which
            declines to the control level by 24 h after training.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Guo,C.X., Tran,H., Green,C.R., Danesh-Meyer,H.V. and Acosta,M.L.
  TITLE     Gap junction proteins in the light-damaged albino rat
  JOURNAL   Mol Vis 20, 670-682 (2014)
   PUBMED   24883012
  REMARK    GeneRIF: Changes in connexins, including Cx36, Cx43, and Cx45, may
            contribute to the damage process.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Cea,L.A., Cisterna,B.A., Puebla,C., Frank,M., Figueroa,X.F.,
            Cardozo,C., Willecke,K., Latorre,R. and Saez,J.C.
  TITLE     De novo expression of connexin hemichannels in denervated fast
            skeletal muscles leads to atrophy
  JOURNAL   Proc Natl Acad Sci U S A 110 (40), 16229-16234 (2013)
   PUBMED   24043768
  REMARK    GeneRIF: The absence of Cx43/Cx45 hemichannels in skeltal muscles
            cells greatly attenuates the inflammasome activation and muscle
            atrophy.
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Johnson,C.M., Kanter,E.M., Green,K.G., Laing,J.G., Betsuyaku,T.,
            Beyer,E.C., Steinberg,T.H., Saffitz,J.E. and Yamada,K.A.
  TITLE     Redistribution of connexin45 in gap junctions of
            connexin43-deficient hearts
  JOURNAL   Cardiovasc Res 53 (4), 921-935 (2002)
   PUBMED   11922902
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Li,X. and Simard,J.M.
  TITLE     Connexin45 gap junction channels in rat cerebral vascular smooth
            muscle cells
  JOURNAL   Am J Physiol Heart Circ Physiol 281 (5), H1890-H1898 (2001)
   PUBMED   11668048
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Laing,J.G., Manley-Markowski,R.N., Koval,M., Civitelli,R. and
            Steinberg,T.H.
  TITLE     Connexin45 interacts with zonula occludens-1 in osteoblastic cells
  JOURNAL   Cell Commun Adhes 8 (4-6), 209-212 (2001)
   PUBMED   12064590
  REMARK    GeneRIF: data suggests that connexin 45 and ZO-1 directly interact
            in osteoblastic cells (ROS/Cx45) [ZO-1]
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Kruger,O., Plum,A., Kim,J.S., Winterhager,E., Maxeiner,S.,
            Hallas,G., Kirchhoff,S., Traub,O., Lamers,W.H. and Willecke,K.
  TITLE     Defective vascular development in connexin 45-deficient mice
  JOURNAL   Development 127 (19), 4179-4193 (2000)
   PUBMED   10976050
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Davis,L.M., Kanter,H.L., Beyer,E.C. and Saffitz,J.E.
  TITLE     Distinct gap junction protein phenotypes in cardiac tissues with
            disparate conduction properties
  JOURNAL   J Am Coll Cardiol 24 (4), 1124-1132 (1994)
   PUBMED   7930207
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 27, 2007 this sequence version replaced XP_001081521.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.41211.1,
                                           SRR26643299.45972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..396
                     /product="gap junction gamma-1 protein"
                     /note="gap junction channel protein connexin 45;
                     connexin-45; gap junction alpha-7 protein; gap junction
                     membrane channel protein alpha 7; connexin q"
                     /calculated_mol_wt=45535
     Region          2..255
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     Region          145..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     Site            176..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     Region          357..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GG66.1)"
     CDS             1..396
                     /gene="Gjc1"
                     /gene_synonym="Cx45; Cxnq; Gja7"
                     /coded_by="NM_001085381.2:404..1594"
                     /db_xref="GeneID:266706"
                     /db_xref="RGD:628889"
ORIGIN      
        1 mswsfltrll eeihnhstfv gkiwltvliv frivltavgg esiyydeqsk fvcnteqpgc
       61 envcydafap lshvrfwvfq iilvatpsvm ylgyaihkia kmehgeadkk aarskpyamr
      121 wkqhraleet eedheedpmm ypemelesek enkeqsqpkp khdgrrrire dglmkiyvlq
      181 llartvfevg fligqyflyg fqvhpfyvcs rlpcphkidc fisrptekti fllimygvtg
      241 lclllniwem lhlgfgtird slnskrreld dpgaynypft wntpsappgy niavkpdqiq
      301 ytelsnakia ykqnkaniaq eqqygsheeh lpadletlqr eirmaqerld laiqayhhqn
      361 nphgprekka kvgsksgsnk ssissksgdg ktsvwi
//
LOCUS       NP_001178570             485 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM58 [Rattus norvegicus].
ACCESSION   NP_001178570 XP_220473
VERSION     NP_001178570.1
DBSOURCE    REFSEQ: accession NM_001191641.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Thom,C.S., Traxler,E.A., Khandros,E., Nickas,J.M., Zhou,O.Y.,
            Lazarus,J.E., Silva,A.P., Prabhu,D., Yao,Y., Aribeana,C.,
            Fuchs,S.Y., Mackay,J.P., Holzbaur,E.L. and Weiss,M.J.
  TITLE     Trim58 degrades Dynein and regulates terminal erythropoiesis
  JOURNAL   Dev Cell 30 (6), 688-700 (2014)
   PUBMED   25241935
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jul 17, 2010 this sequence version replaced XP_220473.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.13265.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..485
                     /product="E3 ubiquitin-protein ligase TRIM58"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 58"
                     /calculated_mol_wt=55180
     Region          11..62
                     /region_name="RING-HC_TRIM58_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein TRIM58 and similar proteins;
                     cd16606"
                     /db_xref="CDD:438268"
     Region          91..134
                     /region_name="Bbox2_TRIM39-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM39, TRIM58 and similar
                     proteins; cd19780"
                     /db_xref="CDD:380838"
     Region          <132..>224
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          291..458
                     /region_name="SPRY_PRY_TRIM58"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     58 (TRIM58), also known as BIA2; cd15816"
                     /db_xref="CDD:293988"
     CDS             1..485
                     /gene="Trim58"
                     /gene_synonym="RGD1566174"
                     /coded_by="NM_001191641.1:1..1458"
                     /db_xref="GeneID:303167"
                     /db_xref="RGD:1566174"
ORIGIN      
        1 matapgerlq eearcsvcld flqepisvdc ghsfclrcis elceksdsaq gvyacpqcrg
       61 pfrpssfrpn rqlaslvdtv rqlglgtgha gsrqcsrhge dlshfceedq amvcwvcdts
      121 pehrshrtep lqeaasryqr mlqvalelvk kemeealtqe anvgkktiiw kekvemqrqr
      181 frlefekhrg flaqeeqlql rrleeeerat lqrlrdsrnr laqqnkalke laeeleemsq
      241 rpavallega rgvltrseam trlepeavpm elktvcripg mremlrkfqv dvkldpatah
      301 pslllttdlr svqdaevwrd vpsnperfdt wpcilglqgf ssgrhywevi vgeraewglg
      361 vcqdsvlrkg ettpspengv wamwllrgse ymvlsspsvp vfqderprri gifldyeagq
      421 isfynvtngs yiytfnhlfs gvlrpyffvc dttplilppm teagpgnwts rglldfavaa
      481 rseey
//
LOCUS       NP_001092931             838 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 1 precursor isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001092931 XP_001053213
VERSION     NP_001092931.2
DBSOURCE    REFSEQ: accession NM_001099461.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Mar 15, 2021 this sequence version replaced NP_001092931.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..838
                     /product="vomeronasal 2 receptor 1 precursor isoform 2
                     precursor"
                     /note="vomeronasal type-2 receptor 26-like"
                     /calculated_mol_wt=93381
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2979
     Region          45..496
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          504..558
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          578..829
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          578..603
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(581,584..585,588..589,591..592,626,630,633..634,642,
                     646)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          615..636
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(635,647..648,651..652,655,735,740,743..744,747,781,
                     784..785,788,792,800..801,804,807,811)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          645..669
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          693..709
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          736..762
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          770..793
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          798..823
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..838
                     /gene="Vom2r1"
                     /coded_by="NM_001099461.2:1..2517"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:678740"
                     /db_xref="RGD:1596944"
ORIGIN      
        1 mkklcaftia ffplkfclil csltepncfw rikkievydg dlqndcgfvl ftlespieen
       61 fynhiinfrk yefflvmffa tdeinknpyl lsnmslifsf ifgmcedtmg vldkaylhqn
      121 nyfdllnync grkkrcdvkl tgpswktslk lsvnsrapki ffgpfnpnls dhdqfpyiyq
      181 iatkdtyllh gmvslmfhfe wtwigliitd ddqgiqfhsd lreemqrhai clafvimipe
      241 siklyntkfk iydqqlmtss akvtiiygkm istlelnfar wtylvarriw ittskldvit
      301 ydkdfsldff hgtvifahhh ndiatfrnfm qiintskypv disqsmgqwn hfncsisknk
      361 kkmdffmlkn pmewltqhtf dmvlseegyn lynavyavah tyhelifqqv esqemakpkg
      421 lftdcqqvas llktrvftnp vgelvnmnhk enqcakydif iiwnfpnglg lkvkigsyfp
      481 clqqsqhlhi sedwewvtge tlvpssvcse tctagfrksh qkqtanccfd cvqcqeneia
      541 ndtadmeqcv rcpddsyanl eqtqclqrav tflayedplg malgcmalsf saitvlvlvt
      601 fvkyrdtpiv kannrilsyi llislvfcfl csllfighpn qatcilqqat faifftvais
      661 tvlaktitvv tafklttpgr rirkmmikva thllipictl iqlvlcaiwl vtsppfidrd
      721 iqsehgkvii icnkgsviaf hfvlgylgsl algsftvafl arnlpdrfne akfltfsmlv
      781 fysvwitflp vyhstrgkvm vivevfsila ssagllgcif vqkcyvllvr pdlnvlqk
//
LOCUS       NP_001385510             222 aa            linear   ROD 03-APR-2025
DEFINITION  mitochondrial cardiolipin hydrolase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001385510 XP_220517
VERSION     NP_001385510.1
DBSOURCE    REFSEQ: accession NM_001398581.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Nishimasu,H., Ishizu,H., Saito,K., Fukuhara,S., Kamatani,M.K.,
            Bonnefond,L., Matsumoto,N., Nishizawa,T., Nakanaga,K., Aoki,J.,
            Ishitani,R., Siomi,H., Siomi,M.C. and Nureki,O.
  TITLE     Structure and function of Zucchini endoribonuclease in piRNA
            biogenesis
  JOURNAL   Nature 491 (7423), 284-287 (2012)
   PUBMED   23064230
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Ipsaro,J.J., Haase,A.D., Knott,S.R., Joshua-Tor,L. and Hannon,G.J.
  TITLE     The structural biochemistry of Zucchini implicates it as a nuclease
            in piRNA biogenesis
  JOURNAL   Nature 491 (7423), 279-283 (2012)
   PUBMED   23064227
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Palmer,C.S., Osellame,L.D., Stojanovski,D. and Ryan,M.T.
  TITLE     The regulation of mitochondrial morphology: intricate mechanisms
            and dynamic machinery
  JOURNAL   Cell Signal 23 (10), 1534-1545 (2011)
   PUBMED   21683788
  REMARK    Review article
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Huang,H., Gao,Q., Peng,X., Choi,S.Y., Sarma,K., Ren,H., Morris,A.J.
            and Frohman,M.A.
  TITLE     piRNA-associated germline nuage formation and spermatogenesis
            require MitoPLD profusogenic mitochondrial-surface lipid signaling
  JOURNAL   Dev Cell 20 (3), 376-387 (2011)
   PUBMED   21397848
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Watanabe,T., Chuma,S., Yamamoto,Y., Kuramochi-Miyagawa,S.,
            Totoki,Y., Toyoda,A., Hoki,Y., Fujiyama,A., Shibata,T., Sado,T.,
            Noce,T., Nakano,T., Nakatsuji,N., Lin,H. and Sasaki,H.
  TITLE     MITOPLD is a mitochondrial protein essential for nuage formation
            and piRNA biogenesis in the mouse germline
  JOURNAL   Dev Cell 20 (3), 364-375 (2011)
   PUBMED   21397847
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Choi,S.Y., Huang,P., Jenkins,G.M., Chan,D.C., Schiller,J. and
            Frohman,M.A.
  TITLE     A common lipid links Mfn-mediated mitochondrial fusion and
            SNARE-regulated exocytosis
  JOURNAL   Nat Cell Biol 8 (11), 1255-1262 (2006)
   PUBMED   17028579
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000010.1.
            
            On Dec 20, 2021 this sequence version replaced XP_220517.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.36849.1,
                                           SRR26643293.63057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..222
                     /product="mitochondrial cardiolipin hydrolase isoform 1"
                     /EC_number="3.1.4.4"
                     /note="mitochondrial cardiolipin hydrolase"
                     /calculated_mol_wt=24997
     Region          93..204
                     /region_name="PLDc_vPLD6_like"
                     /note="Catalytic domain of vertebrate phospholipase D6 and
                     similar proteins; cd09171"
                     /db_xref="CDD:197268"
     Site            order(154,156,169,171,182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197268"
     Site            154
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:197268"
     CDS             1..222
                     /gene="Pld6"
                     /gene_synonym="RGD1311987"
                     /coded_by="NM_001398581.1:111..779"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:287366"
                     /db_xref="RGD:1311987"
ORIGIN      
        1 mgrsswrlvf aagaglalal ealpwlmrwl lagrrprrev lffpsqvtct eallqapglp
       61 pgpssgcpcs lphsesslsr llrallaars slelclfafs spqlgravql lhqrgvrvrv
      121 itdcdymaln gsqigllrka giqvrhdqdl gymhhkfaiv dkkvlitgsl nwttqaiqnn
      181 renvlimedt eyvrlfleef eriweefdpt kysffpqkhr gh
//
LOCUS       NP_001108501             691 aa            linear   ROD 03-APR-2025
DEFINITION  protein LEKR1 [Rattus norvegicus].
ACCESSION   NP_001108501 XP_001064656 XP_342256
VERSION     NP_001108501.2
DBSOURCE    REFSEQ: accession NM_001115029.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158627.1,
            CA339992.1 and JAXUCZ010000002.1.
            
            On Oct 31, 2009 this sequence version replaced NP_001108501.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.12403.1,
                                           SRR26360181.2640322.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..691
                     /product="protein LEKR1"
                     /note="leucine-, glutamate- and lysine-rich protein 1"
                     /calculated_mol_wt=80737
     Region          42..>601
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..691
                     /gene="Lekr1"
                     /gene_synonym="RGD1562738; RGD1565425"
                     /coded_by="NM_001115029.2:467..2542"
                     /db_xref="GeneID:361953"
                     /db_xref="RGD:1565425"
ORIGIN      
        1 mdrhipmhal pkeiqqmspe etvckycgvs ylilhefkam eeklkavqee lkfyqgsier
       61 ekrlqeklqs lsqefekykt dseskkervq hasmqlkkqq nefqrvqkel shlqlelkik
      121 qkqsqvfsqr lseykyfwnk tlllltftkr eltsikyein dnfqnwtslk gevflqiksi
      181 sdtalaeidm lnksltvsqr nkvsleeemk clkvlsdaai lrsqqmeask qhevnlqarc
      241 yelqkealdl qcqvealglr lqktvkeldn ckemlmkksn danncerelr klkfesiise
      301 srhkrllkek edslitcqql yktvqeeltt kgrqeedikr rinlaenele mtktlllqtq
      361 eeiltlkner elmlvshqks ieqlqetlrq kllsddswre kieaelsker arhriefqdq
      421 allfkeeakl eldiekekhq eiirkyqkeq eglqskiadl iadatkdlrl evaslqeklh
      481 esharytees eskkkeiedl knlvaelecr lkeetghdds vskelkkemk qksdelervr
      541 laqtqllqqf sqsqeentfl qetvrrecee rfeltealsq akeqllelkr sggslrcsln
      601 kgalthpvsa vsnhrelsnv rhncgrgtss aslrglpkpt atptpdklkk vdssglpals
      661 qaypprgrai svtearqrlt aiirrrlsqq r
//
LOCUS       NP_001092959             853 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 13 [Rattus norvegicus].
ACCESSION   NP_001092959 XP_001074899
VERSION     NP_001092959.3
DBSOURCE    REFSEQ: accession NM_001099489.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 1, 2024 this sequence version replaced NP_001092959.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..853
                     /product="vomeronasal 2 receptor, 13"
                     /calculated_mol_wt=96476
     Region          41..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,170..171,390)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(111,114,154,244)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          508..561
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          582..832
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          582..606
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(584,587..588,591..592,594..595,629,633,636..637,645,
                     649)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          618..639
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(638,650..651,654..655,658,738,743,746..747,750,784,
                     787..788,791,795,803..804,807,810,814)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          648..672
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          696..712
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          739..765
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          773..796
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          801..826
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..853
                     /gene="Vom2r13"
                     /coded_by="NM_001099489.3:1..2562"
                     /db_xref="GeneID:690593"
                     /db_xref="RGD:1594671"
ORIGIN      
        1 mftlilsflf lnipfqvtgf iyptcswrik enkdksgner igcffliqav qkpvekeyfs
       61 hffntqkhte ihkyslvlaf smievnrnpd llpnmslvfs freiicgwqp elsifievnl
      121 ddygvlpnyt ckdeslcgva ltgvnwaptl llytilnnfk sqqfphltyg hfhpvlsdhe
      181 nfpylyqmas ddtslalalv sfiihfrwnw iglaisdndq gtqflsylkr gmeknaicla
      241 fvsmipvnmh lymsraevyy sqimtssanv viiygdtgst lavsfrmwes lglqrlwitt
      301 tqldvtpsmk dnvyglfafg hhhgvisgfk nfvqtlnpvt ysnenlakle wmhfncevsa
      361 skwktlknfs snhslewlme htfemtfseg syniynavyt vahvlhemtf qkfhnlpnak
      421 gkvenyvcnk lgaplrkihf tnpvgdrvsm nqedklqeey difyiwnfpq glefkvkigl
      481 fspyfingqq lhlsgdmkew argstqmpts vcsadcgpgf rkfrkkemsa ccfdcspcpe
      541 neisnetnle mcvlcpedky antgqndcip kaliflsyed hlgmalslma lgfsaftavi
      601 lgifvkhhst pivkannstl tyilllslif cflcpllfig hpdsvtcilq qitfgvlftm
      661 aistvlakti tvilafkvta pqrmmkyfll sgvstyiipi ctliqvivca vclgvsppsv
      721 eidaqsehgh iiivcnkgsv tcfysilgyl acltfvsftl aflsrnlpgv fneaklitfs
      781 mlvvcsvwvt flpvyhstkg kimvageiis ilasssgmlv cifipkcyii lfrpeknslk
      841 mirekspsht his
//
LOCUS       NP_001160235             298 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 55 [Rattus norvegicus].
ACCESSION   NP_001160235
VERSION     NP_001160235.1
DBSOURCE    REFSEQ: accession NM_001166763.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..298
                     /product="vomeronasal 1 receptor 55"
                     /note="vomeronasal 1 receptor Vom1r55; vomeronasal 1
                     receptor 1-like"
                     /calculated_mol_wt=33281
     Region          12..298
                     /region_name="V1R"
                     /note="Vomeronasal organ pheromone receptor family, V1R;
                     pfam03402"
                     /db_xref="CDD:460912"
     CDS             1..298
                     /gene="Vom1r55"
                     /coded_by="NM_001166763.1:1..897"
                     /db_xref="GeneID:691791"
                     /db_xref="RGD:1595934"
ORIGIN      
        1 mvqitvddmv lkvvillqmg tgllantyll fmhsfvlltg hrpkptelil snlalanslv
       61 llskgaqqvm edlglvhvle gfgcqvffyf hrvsrelllc stsllscfqa vtvsprhgvw
      121 tglrrwvyrh vgcscffcws fnlvistisp ieikvfgdii snssmgdgia cqyvvavsgl
      181 caiplailga llmtlmvaas thmvcllhrh hqrvqhvrsc nltyrtspem rathsilllv
      241 agfilfyfln siyifysiks fssylwlqhs lkffatcfps lsplvlifqn srtpspcf
//
LOCUS       NP_001396328             320 aa            linear   ROD 03-APR-2025
DEFINITION  olfactory receptor family 13 subfamily C member 3B [Rattus
            norvegicus].
ACCESSION   NP_001396328 XP_006238235
VERSION     NP_001396328.1
DBSOURCE    REFSEQ: accession NM_001409399.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000005.1.
            
            On Jul 15, 2022 this sequence version replaced XP_006238235.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q23"
     Protein         1..320
                     /product="olfactory receptor family 13 subfamily C member
                     3B"
                     /note="olfactory receptor 13C3; olfactory receptor
                     13C3-like"
                     /calculated_mol_wt=35579
     Region          28..303
                     /region_name="7tmA_OR13-like"
                     /note="olfactory receptor family 13 and related proteins,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15430"
                     /db_xref="CDD:320547"
     Region          29..55
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320547"
     Region          62..88
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320547"
     Site            order(84,87..88,100..105,107..108,111,156,158..162,198,
                     201..203,205..207,209..210,255,258..259,261..262,265,
                     277..278,280..282,285,288..289)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320547"
     Region          100..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320547"
     Region          143..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320547"
     Region          198..228
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320547"
     Region          235..265
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320547"
     Region          278..303
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320547"
     CDS             1..320
                     /gene="Or13c3b"
                     /coded_by="NM_001409399.1:16..978"
                     /db_xref="GeneID:100912327"
                     /db_xref="RGD:6487777"
ORIGIN      
        1 mddmdknnqt fvseflllgl sgypkteily fvivlvmylv iltgngvlii asifdshlht
       61 pmyfflgnls fldicyttss vpstlvslis kkrnisfsgc tvqmfvgfam gsteclllgm
      121 mafdryvaic nplrysvims kevyvsmasa swfsgginsv vqtslamrlp fcgnnvinhf
      181 tcevlavlkl acadislniv tmvisnmafl vlpllliffs yvfilytilr mnsasgrrka
      241 fstcsahltv vvifygtifs myakpksqdl tgkdkfqtsd kiislfygvv tpmlnpiiys
      301 lrnkdvkaav kyilkqkyip
//
LOCUS       NP_001161021             315 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 16 [Rattus norvegicus].
ACCESSION   NP_001161021
VERSION     NP_001161021.1
DBSOURCE    REFSEQ: accession NM_001167549.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..315
                     /product="vomeronasal 1 receptor 16"
                     /note="vomeronasal 1 receptor Vom1r16"
                     /calculated_mol_wt=35635
     Region          8..290
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          8..32
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          44..65
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          82..104
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          130..146
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          181..204
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          233..255
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          265..290
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..315
                     /gene="Vom1r16"
                     /coded_by="NM_001167549.1:1..948"
                     /db_xref="GeneID:100312668"
                     /db_xref="RGD:2316472"
ORIGIN      
        1 mdaselsigv iilsqtvigv lanffllyhc milyltryrl rsidcvlmql svaniltils
       61 kgitqtiaaf glkdflndig ckltffvhkv gksvcigsts flsvfqaiii sprdsrcskl
      121 kvkvhkyicy svylnwviff iisiinllhl rakynnesti tlksyvycys vrhdptsdil
      181 havlvsgpdi iflglmmysn gfmvltlyrh kqkmqqmprm nvssisspas ratktilllv
      241 stfvsfytis slchllvvil ynpswilvnv aamsasffpt vypfllmshd swalsfclll
      301 krnryfpkds sqeln
//
LOCUS       NP_001092985             854 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 49 precursor [Rattus norvegicus].
ACCESSION   NP_001092985 XP_001066737
VERSION     NP_001092985.1
DBSOURCE    REFSEQ: accession NM_001099515.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 26, 2007 this sequence version replaced XP_001066737.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN09345330 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..854
                     /product="vomeronasal 2 receptor, 49 precursor"
                     /calculated_mol_wt=93779
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2496
     Region          40..509
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          518..571
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          591..842
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          591..616
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(594,597..598,601..602,604..605,639,643,646..647,655,
                     659)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          628..649
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(648,660..661,664..665,668,748,753,756..757,760,794,
                     797..798,801,805,813..814,817,820,824)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          658..682
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          706..722
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          749..775
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          783..806
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          811..836
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..854
                     /gene="Vom2r49"
                     /coded_by="NM_001099515.1:1..2565"
                     /db_xref="GeneID:688392"
                     /db_xref="RGD:1589986"
ORIGIN      
        1 mklliafsll illtafqeqi scfslskpas pgyyqdgdfv igglfslrvt agdtrskfgf
       61 tdtthipehv yvdftkhyqh mlamvfaien inkdpnilfn mslgfylfnv dfiemkaves
      121 smallsgesp avpnyscrpe ktdklvavig gistgistqi sqllslynvp qisyapfdqs
      181 fetkvqlqsp yqfpvhttal yqgiiqllly fswvwvglvv pddvrgelfl rditeemnnh
      241 glcvafaekf pefpakdtgn rehfmerftl trvivafgdt ysllrfvyii fcntpfgnvw
      301 vttsdwditt lpfqqnlgyt yfggglsfsv hmdeilgfkn flrsvqprky pqdifiqdvw
      361 silfecpyfd qhwirelsqc eqngnlstrp lhfwdmntsp ssykvheavy aiaqalheel
      421 lltlegdslh kdlpqaplpw klhpflqkgq lrrssneenv vnkevsatkl difnyqslqn
      481 gskaqvkvge fvfeshsvqh fslneelitf gehhsqtpfs vcspscplgf rkspvegkpf
      541 ccfdclpcpd geianetdmd qcikcpedqy pnrqrnqclp kiteflshed tlgavfvsia
      601 islsalsami lglficyrdt sivrannrnl sylllvslml cffcslifig qprtvtcvlr
      661 qmifgivfsv avstilaktf ivvvafkaik pgsalkmsmv irlsntivfc gsiiqvcica
      721 vwlgtyppfp dvdmhsefgq iilwcnegst lafycvlgyl gflaslslli aflarrlpds
      781 fnetktitfs mlvfcsvwis fvptylsskg ktmvaveils ilassagllg ciflpkcymi
      841 lmssgghsri kffk
//
LOCUS       NP_001397192             395 aa            linear   ROD 03-APR-2025
DEFINITION  RT1 class I, locus T24, gene 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001397192
VERSION     NP_001397192.1
DBSOURCE    REFSEQ: accession NM_001410263.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Brorson,K.A., Hunt,S.W. 3rd, Hunkapiller,T., Sun,Y.H.,
            Cheroutre,H., Nickerson,D.A. and Hood,L.
  TITLE     Comparison of exon 5 sequences from 35 class I genes of the BALB/c
            mouse
  JOURNAL   J Exp Med 170 (6), 1837-1858 (1989)
   PUBMED   2584927
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CM038666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR8487231.76902.1,
                                           SRR8487230.143865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /strain="SHRSP/BbbUtx"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..395
                     /product="RT1 class I, locus T24, gene 1 isoform 1"
                     /note="histocompatibility 2, T region locus 24"
                     /calculated_mol_wt=45193
     Region          19..203
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          208..299
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          209..216
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          224..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(227,229,256..257,259..261,267,269)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(234..236,264,289)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          238..243
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          246..249
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          253..261
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          264..274
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          281..288
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          295..298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..395
                     /gene="RT1-T24-1"
                     /gene_synonym="H2-T24"
                     /coded_by="NM_001410263.1:47..1234"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361787"
                     /db_xref="RGD:1359499"
ORIGIN      
        1 mwslifcfls hpqdtgarsh slhysysavt epgpgvpaff asgfvdnqpf ihydsrkmea
       61 epcadwlren pyyfdeetqv ftnrmkifql slrniqqyyn ssgdrsqrad gfhqqagpht
      121 lqftygcemq gnrttghwqy gydgrdyltl dldsmeytaa tfiagytkhk wqnneywler
      181 ektylekecv lwlkryltmg genftrtdpp qttvthhprp egdvtlrcwa lgfypaditl
      241 twqlngedlt qdmelvetrp tgdgtfqkwa avvvplgkeq kytchveheg lpepltqrwe
      301 appgtdsnmg inviavvlqa vaiiaavaii ivtvvrrrrr rrrntggegd ytpaprslsi
      361 fiqpapqarr swltqqawla wkshastpii tplpa
//
LOCUS       NP_001093119             862 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 23 [Rattus norvegicus].
ACCESSION   NP_001093119
VERSION     NP_001093119.1
DBSOURCE    REFSEQ: accession NM_001099649.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..862
                     /product="vomeronasal 2 receptor 23"
                     /calculated_mol_wt=97583
     Region          41..508
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(76,173..174,398)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(114,117,160,247)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          516..569
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          589..840
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          589..614
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(592,595..596,599..600,602..603,637,641,644..645,653,
                     657)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          626..647
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(646,658..659,662..663,666,746,751,754..755,758,792,
                     795..796,799,803,811..812,815,818,822)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          656..680
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          704..720
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          747..773
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          781..804
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          809..834
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..862
                     /gene="Vom2r23"
                     /gene_synonym="RGD1560836"
                     /coded_by="NM_001099649.1:1..2589"
                     /db_xref="GeneID:308303"
                     /db_xref="RGD:1560836"
ORIGIN      
        1 mllfwifisc flqtpillcs yrsseclvki nyrlkgkgnm viigffpafa vypinkttdw
       61 rmmrfnrdfm vefklrnyqc ilammfaiee innnpfllpn tslgfevnnv phgqrntlat
      121 lfgslsgsdn aipncgsare snptavltgp swaiseyigt lldlykfpql tfgpfdsqlg
      181 eqrrfsslyq vapkdtsltv givslmlhfh wiwvglfiid ddkgaqtlsd lrsemdknrv
      241 ctafvemivv skgsyftksw knqvqiless anviiiygds dsllslivni kqklltwkvw
      301 vlisqwdvsk fddyfmvdsl hgalifshhr edipnftdfm qksnpskfpe dtylhvlwhi
      361 ffncsfvntd ckivhnclpn aslgllpgni fdmvmseesy nvynavyava hslhemilnq
      421 vqfqphekgk ktiffpwllh pflrktqfis hdganmvldf krkshidydi vnfwnfpkgl
      481 glnvkvgtfs snapnnhkls issymiqwat gsteipqsvc seschpgfrk thkegsvvcc
      541 fdciscpene isnetdmdqc vkcpethyan tnkiyclpkt vtflayddpl gktlcfmslg
      601 fssltaavlw vflknrdtpi vkannlalsy tllitlmlcl lcpllfighp stascilqqn
      661 ifgllftvsl stvlaktitv viafkitspg rirrwllisr apnfiiplct llqvflsaiw
      721 lttsppfidk daqsehghii iicnkgsava fhcnlgylga lalvsyfmaf lsrnlpdtfn
      781 eakflafsml vfcsvwitfl piyhstkgkt tvamevfsil asgtsllgii fapkcyiill
      841 rpernslhyi rdkkyakrrk ps
//
LOCUS       NP_001092969             852 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 63 [Rattus norvegicus].
ACCESSION   NP_001092969 XP_001075977 XP_221987
VERSION     NP_001092969.1
DBSOURCE    REFSEQ: accession NM_001099499.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000012.1.
            
            On or before Aug 17, 2007 this sequence version replaced
            XP_221987.4, XP_001075977.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..852
                     /product="vomeronasal 2 receptor 63"
                     /calculated_mol_wt=95662
     Region          40..503
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(71,168..169,393)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(109,112,155,242)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..564
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          584..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          584..609
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(587,590..591,594..595,597..598,632,636,639..640,648,
                     652)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          621..642
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(641,653..654,657..658,661,741,746,749..750,753,787,
                     790..791,794,798,806..807,810,813,817)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          651..675
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          699..715
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          742..768
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          776..799
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          804..829
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..852
                     /gene="Vom2r63"
                     /gene_synonym="RGD1564022"
                     /coded_by="NM_001099499.1:1..2559"
                     /db_xref="GeneID:288541"
                     /db_xref="RGD:1564022"
ORIGIN      
        1 mptwifffft lklpmflckl lthecfvsst dniyqdgdlv isaflplyty qtsqhtegae
       61 sidvsprits qnyqfvmali faideinrnp illpnmtlgy nihsagsies etvvsflkwl
      121 tgqdrlipny tcktkeksva aitgttweis sligiflgly kypqlsigpf epsmnnsekf
      181 pflyqmaake sslalgmvsm fvhfkwnwvg lvisedengv nfvtdlipqm ernticvafm
      241 efitvthmmd lenayeypir imrnpakvvi iyantdtslg vlfrrweyil pwriwvttsq
      301 wevvtsmrhl ildsfhgtli fsqrqgdist fkefvktvrp skypddifla rlweiyfdca
      361 isnatcksle ncssrgnlgl lpwyhfdiav stgsyhvyna vyavahtmhk mliqeidiqg
      421 vknggsmdfp plklnsllkn ikfmnpggdp islnpseklh idydilnfwd fpqgltykvk
      481 vgtfspyfpp gqqlsisedr iewsigveqq ipasvcsesc gpgfrkslqe ekaaccfdcv
      541 pcpeneisng tgkccvkcte dqyantdrtv ciqkavtfla fenplgmtla smalcfsilt
      601 sfvlgifvkh qstlvvkann stlsyillis ltfcflcsfl figqpnavtc ilqqttfgvv
      661 ftvavstvla ktttvilafk stapgrrlrg llisgaskfi ipictliqiv lcgiwlgisp
      721 pfvdtdahse hghiiimcnk gsvtafycvl gylgalslvs ftvafmarnl pdifneakfl
      781 tfsmlvflsv witffpvyhs tkgkimvave vfsilasstg llgcifipkc yiilarpdmn
      841 slkcrrnrvq wk
//
LOCUS       NP_001178814             351 aa            linear   ROD 03-APR-2025
DEFINITION  glycerol-3-phosphate dehydrogenase 1-like protein [Rattus
            norvegicus].
ACCESSION   NP_001178814 XP_343499
VERSION     NP_001178814.1
DBSOURCE    REFSEQ: accession NM_001191885.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Liu,M., Sanyal,S., Gao,G., Gurung,I.S., Zhu,X., Gaconnet,G.,
            Kerchner,L.J., Shang,L.L., Huang,C.L., Grace,A., London,B. and
            Dudley,S.C. Jr.
  TITLE     Cardiac Na+ current regulation by pyridine nucleotides
  JOURNAL   Circ Res 105 (8), 737-745 (2009)
   PUBMED   19745168
  REMARK    GeneRIF: Mutations of GPD1-L may downregulate Na(v)1.5 by altering
            the oxidized to reduced NAD(H) balance.
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Valdivia,C.R., Ueda,K., Ackerman,M.J. and Makielski,J.C.
  TITLE     GPD1L links redox state to cardiac excitability by PKC-dependent
            phosphorylation of the sodium channel SCN5A
  JOURNAL   Am J Physiol Heart Circ Physiol 297 (4), H1446-H1452 (2009)
   PUBMED   19666841
REFERENCE   3  (residues 1 to 351)
  AUTHORS   London,B., Michalec,M., Mehdi,H., Zhu,X., Kerchner,L., Sanyal,S.,
            Viswanathan,P.C., Pfahnl,A.E., Shang,L.L., Madhusudanan,M.,
            Baty,C.J., Lagana,S., Aleong,R., Gutmann,R., Ackerman,M.J.,
            McNamara,D.M., Weiss,R. and Dudley,S.C. Jr.
  TITLE     Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L)
            decreases cardiac Na+ current and causes inherited arrhythmias
  JOURNAL   Circulation 116 (20), 2260-2268 (2007)
   PUBMED   17967977
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_343499.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211779.1, FQ217318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..351
                     /product="glycerol-3-phosphate dehydrogenase 1-like
                     protein"
                     /EC_number="1.1.1.8"
                     /note="glycerol-3-phosphate dehydrogenase 1 like 1"
                     /calculated_mol_wt=37935
     Region          7..344
                     /region_name="glycerol3P_DH"
                     /note="glycerol-3-phosphate dehydrogenase (NAD(+));
                     TIGR03376"
                     /db_xref="CDD:274551"
     CDS             1..351
                     /gene="Gpd1l"
                     /gene_synonym="Gpd1l1; RGD1560123"
                     /coded_by="NM_001191885.1:206..1261"
                     /db_xref="GeneID:363159"
                     /db_xref="RGD:1560123"
ORIGIN      
        1 maaaplkvci vgsgnwgsav akiigsnvkn lqkfsstvkm wvfeetvngr kltdiinndh
       61 envkylpghk lpenvvavpn lgeavqdadl lvfviphqfi hkicdeitgr vpkkavgitl
      121 ikgidegpdg lklisdiire kmgidisvlm ganiasevaa ekfcettigs kvlqngllfk
      181 ellqtpnfri tvvddadtve lcgalkniva vgagfcdglc cgdntkaavi rlglmemiaf
      241 akifckgqvs tatflescgv adlittcygg rnrkvaeafa rtgktieele kellngqklq
      301 gpqtsaevyr ilkqkglldk fplftavyqi cyegrpvtqm lsclqshpeh i
//
LOCUS       NP_001129187             770 aa            linear   ROD 03-APR-2025
DEFINITION  tripartite motif-containing protein 67 [Rattus norvegicus].
ACCESSION   NP_001129187 XP_226563
VERSION     NP_001129187.1
DBSOURCE    REFSEQ: accession NM_001135715.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Yaguchi,H., Okumura,F., Takahashi,H., Kano,T., Kameda,H.,
            Uchigashima,M., Tanaka,S., Watanabe,M., Sasaki,H. and Hatakeyama,S.
  TITLE     TRIM67 protein negatively regulates Ras activity through
            degradation of 80K-H and induces neuritogenesis
  JOURNAL   J Biol Chem 287 (15), 12050-12059 (2012)
   PUBMED   22337885
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Oct 8, 2008 this sequence version replaced XP_226563.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..770
                     /product="tripartite motif-containing protein 67"
                     /calculated_mol_wt=82563
     Region          2..>47
                     /region_name="RING-HC_TRIM67"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 67 (TRIM67) and similar proteins;
                     cd16758"
                     /db_xref="CDD:438416"
     Region          204..249
                     /region_name="Bbox1_TRIM67_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 67 (TRIM67) and similar proteins;
                     cd19844"
                     /db_xref="CDD:380902"
     Region          290..334
                     /region_name="Bbox2_TRIM67_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 67 (TRIM67) and similar proteins;
                     cd19827"
                     /db_xref="CDD:380885"
     Region          336..462
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          515..591
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(580..581,583..584)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          588..759
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..770
                     /gene="Trim67"
                     /gene_synonym="RGD1560667"
                     /coded_by="NM_001135715.1:452..2764"
                     /db_xref="GeneID:307938"
                     /db_xref="RGD:1560667"
ORIGIN      
        1 meeelkcpvc gslfrepiil pcshnvclpc artiavqtpd geqhlpppll lsrgaaaaaa
       61 apppdqdaaa gatcggagas tagglgggaa gggdhadkls lysetdsgyg sytpslkspn
      121 gvrvlpmvpa ppgssaaaar gaacsslcss sssitcpqch rsasldhrgl rgfqrnrlle
      181 givqryqqgr gvaagasaap avaicqlcdr tppepaatlc eqcdvlycat cqlkchpsrg
      241 pfakhrlvqp ppppappeat sasvgtstas saggcrspgg agapvprkfp tcpehemeny
      301 smycvscrsp vcymcleegr hgkhevkplg atwkqhkaql sqalngvsdk akeakeflvq
      361 lknilqqiqe ngldyeaclv aqcdalvdal trqkaklltk vtkereqklk mvwdqinhct
      421 lklrqstglm eycleviked dpsgflqisd alikrvqtsq eqwvkgalep kvsaefdltl
      481 dsepllqaih qldfvqmklp pvpllqlekc ctrnnsatla wrtppfthsp adgyileldd
      541 gdggqfrevy vgketlctid glhfnstyna rvkafnssgv gpysktvvlq tsdvawftfd
      601 pnsghrdiil sndnqtatcs syddrvvlgt aafskgahyw elhvdrydnh pdpafgvara
      661 svvkdmmlgk ddkawamyvd nnrswfmhcn shtnrteggv ckgatvgvll dlnkhtltff
      721 ingqqqgpta fshvdgvfmp alslnrnvqv tlhtglevpt nlgrpklsgn
//
LOCUS       NP_001121688             333 aa            linear   ROD 03-APR-2025
DEFINITION  cathepsin 8 precursor [Rattus norvegicus].
ACCESSION   NP_001121688 XP_001058557
VERSION     NP_001121688.1
DBSOURCE    REFSEQ: accession NM_001128216.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Jun 10, 2008 this sequence version replaced XP_001058557.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..333
                     /product="cathepsin 8 precursor"
                     /calculated_mol_wt=36316
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1726
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Region          115..331
                     /region_name="Peptidase_C1A"
                     /note="Peptidase C1A subfamily (MEROPS database
                     nomenclature); composed of cysteine peptidases (CPs)
                     similar to papain, including the mammalian CPs (cathepsins
                     B, C, F, H, L, K, O, S, V, X and W). Papain is an
                     endopeptidase with specific substrate preferences;
                     cd02248"
                     /db_xref="CDD:239068"
     Site            order(132,138,276,300)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            order(182..183,248,274,277,327)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     CDS             1..333
                     /gene="Cts8"
                     /coded_by="NM_001128216.1:1..1002"
                     /db_xref="GeneID:680718"
                     /db_xref="RGD:1588248"
ORIGIN      
        1 mspvvllail clgvaratqp sdpsldsewq ewktkyekny sleeegqkra vweenmkvvk
       61 qhnieydqek knftmelnaf admtgeefrk mmtnipvqnl rkkksihqpi frylpkfvdw
      121 rrrgyvtsvk nqgtcnscwa fsvagaiegq mfrktgrlvs lspqnlvdcs rpegnhgchm
      181 gstlyalkyv wsnggleaes typyegkegp crylprrsaa rvtgfstvar seealmhava
      241 tigpisvgid ashvsfrfyr rgiyyeprcs snrinhsvlv vgygyegres dgrkywlikn
      301 shgvgwgmng ymklargwnn hcgiatygfy prv
//
LOCUS       NP_001092928             841 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 4 precursor [Rattus norvegicus].
ACCESSION   NP_001092928 XP_001067385 XP_218106
VERSION     NP_001092928.1
DBSOURCE    REFSEQ: accession NM_001099458.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_218106.4, XP_001067385.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..841
                     /product="vomeronasal 2 receptor 4 precursor"
                     /note="vomeronasal type-2 receptor 116-like"
                     /calculated_mol_wt=93531
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3070
     Region          45..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,167..168,391)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          508..561
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          581..832
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          581..606
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(584,587..588,591..592,594..595,629,633,636..637,645,
                     649)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          618..639
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(638,650..651,654..655,658,738,743,746..747,750,784,
                     787..788,791,795,803..804,807,810,814)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          648..672
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          696..712
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          739..765
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          773..796
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          801..826
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..841
                     /gene="Vom2r4"
                     /gene_synonym="RGD1564110"
                     /coded_by="NM_001099458.1:1..2526"
                     /db_xref="GeneID:308248"
                     /db_xref="RGD:1564110"
ORIGIN      
        1 mkkmwaftia ffslkfclil csltepscfw rikrsedndg dlrsdcgfvl ftlespieen
       61 fytriinfri parkyefflv lffaideink npyllsnmsl ifsiivglce dtmgvldkay
      121 shqskifkri nyfcgikqrc dinltgpswt tslklsiysr tpkiffgsfn pnlsdhdqfp
      181 yiyqrankdt ylfcgmvslm fhfgwtwigl visnddqgiq flsdlreemq rhaiclafvi
      241 mipetmqiyk trvkiydqql mtssakvvvi ygemnstlel sfrrwaylga qriwittsqw
      301 dvitnqkdfs ldfshgtvtf ahhhnditif rnfmqtints kypidisqsm lqwnhfncsi
      361 sknkkkmdcf tfnnplewlv qhtfdmvlse egynlynavy avahtyheli fqqaesqkma
      421 dpkgvftdcq qvasllktrv finpvgelvn mnhkenycak ydifiiwyfp qglglkvkig
      481 syfpclpqsq qlhisedwew vteetlvpss vcsvtctagf rkihqkqtad ccfdcvqcqe
      541 neiandtdme hcvrcpedsy anleqteclq rvvtflayed plgmalgcma lsfsaitilv
      601 lvtfvkyrdt pivkannril syillislaf cflcsllfig hpnqatcilq qttfaifftv
      661 aistvlakti tvvtafkltt pgrrirkmmi kgainllipi ctliqlvlca iwlvtsppfi
      721 drdiqsehgk iiiicnkgsv iafhivlgyl gslalgsftv aflarnlpdr fneakfltfs
      781 mlvfysvwit flpvyhstrg kvmvvvevfs ilassagllg cifvqkcyvl lvqpdlnvlq
      841 k
//
LOCUS       NP_001161020             316 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 13 [Rattus norvegicus].
ACCESSION   NP_001161020
VERSION     NP_001161020.1
DBSOURCE    REFSEQ: accession NM_001167548.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 19952141
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..316
                     /product="vomeronasal 1 receptor 13"
                     /note="vomeronasal 1 receptor Vom1r13"
                     /calculated_mol_wt=36127
     Region          26..316
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          26..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          61..82
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          99..121
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          147..163
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          198..221
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          250..272
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          282..307
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..316
                     /gene="Vom1r13"
                     /coded_by="NM_001167548.1:1..951"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:100312667"
                     /db_xref="RGD:2316473"
ORIGIN      
        1 mrnvwqhilk svflsntmda rnlgvgitfl lqsvvgllgn islifyylii yykkhkikpm
       61 dlilmhliiv niliilskgl attmatfglk lffndwsyqf fmyvlrvfrs msivticlls
      121 vfqaitimpr nsclknlrvk ttmdisfcis lcwvlyiiin vifplymsit lsrknitkdt
      181 nfklytivgy dkitgslytt ffvfpeilfs glitwssssm ivllyrhkrr vqylqsthas
      241 hssspesrat qnilvlvsif lafytisais haysalfhss dgwlmifsni ltlclptssl
      301 fvlmshsssl sklcfl
//
LOCUS       NP_001333363             175 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein CFAP97D2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001333363
VERSION     NP_001333363.1
DBSOURCE    REFSEQ: accession NM_001346434.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.1209443.1,
                                           SRR22582416.337887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..175
                     /product="uncharacterized protein CFAP97D2 isoform 1"
                     /calculated_mol_wt=20914
     Region          28..122
                     /region_name="Hmw_CFAP97"
                     /note="Hemingway/CFA97; pfam13879"
                     /db_xref="CDD:464014"
     CDS             1..175
                     /gene="Cfap97d2"
                     /coded_by="NM_001346434.1:77..604"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:688801"
                     /db_xref="RGD:1584165"
ORIGIN      
        1 mhrvpqlttp wasrdlqraw ektyqnhrkk vqnaqplvdt rppqtyshlh lkfkklkmee
       61 erlsiidrnn ylllqrvasa mktgrridgq nnftwrslnr ksreqalmkv qkqnqavper
      121 lrssepwyga qrwredwtam atrpctcrht wrkgadreaq qghsliwmrs lkrkg
//
LOCUS       NP_001104791             851 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 80 precursor [Rattus norvegicus].
ACCESSION   NP_001104791 XP_001061151 XP_577747
VERSION     NP_001104791.1
DBSOURCE    REFSEQ: accession NM_001111321.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On or before Dec 14, 2007 this sequence version replaced
            XP_577747.2, XP_001061151.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..851
                     /product="vomeronasal 2 receptor 80 precursor"
                     /calculated_mol_wt=94392
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2160
     Region          40..498
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,168..169,388)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(107,110,152,242)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          506..559
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          579..830
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          579..604
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(582,585..586,589..590,592..593,627,631,634..635,643,
                     647)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          616..637
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(636,648..649,652..653,656,736,741,744..745,748,782,
                     785..786,789,793,801..802,805,808,812)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          646..670
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          694..710
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          737..763
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          771..794
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          799..824
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..851
                     /gene="Vom2r80"
                     /gene_synonym="RGD1559687"
                     /coded_by="NM_001111321.1:1..2556"
                     /db_xref="GeneID:502285"
                     /db_xref="RGD:1559687"
ORIGIN      
        1 mftlilffll lnnpvhvagf nyptcswrik qnrgkggnse tdciflilpv kgpvekddfk
       61 pllntqtlte nhkhalvlaf svneinrnpd llpnmsltmd ipscnwtskf rntiydslhn
      121 ykilpnyscq dnllcvvalt ggnwattlll ytvlsyfiyq qfflltyrpf hpalhdhenf
      181 pylyqmssdd tslalalvsf iihfswnwig laisdneqst hflsylkrgm erntvcfafv
      241 smipvdmdly msraevyynq ivtsstnvvi iygdtggtla vsfrmweslg lqklwitttr
      301 wdvtpskkdn lyglfafghh hgeipgfknf vqtlnpvtss denlaklewm yfncevsask
      361 ckalkncssn hslewlmaht femtftegsy diynavyaaa hvfheinlqi fhnppiakgk
      421 vqnyvcnklg sslrkihftn pvgdrinmnq rdkqqeiydi fyiwnfpqgl efkvkiglfs
      481 pyfingqqlh lsgdmiewar gstqmptsvc ssdcgpgfrk frkkemsacc fdcnpcpene
      541 isnetnvemc ilcpedqyan tgqnhciqka lifltyedpl grvlslmalg fsaftalvlg
      601 iflkhhhtpi vkannstlty illislifcf lcpllfiglp dlatcilqqi tfgvvftvai
      661 stvlaktitv ilafkvtapq rmmkyflvsr vpnyiipict llellvcavw lgafppsvdi
      721 ddqsehghii iicnkgsvta fycvlgylac lafvsftlaf lsrnlpstfn esksitfsml
      781 vvcsvwvtfl pvyhstkgkv mvaveifsil asssgmllci fvpkcyiilf rpdrnsfqmi
      841 rekssshthi s
//
LOCUS       NP_001161023             305 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 39 [Rattus norvegicus].
ACCESSION   NP_001161023
VERSION     NP_001161023.1
DBSOURCE    REFSEQ: accession NM_001167551.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..305
                     /product="vomeronasal 1 receptor 39"
                     /note="vomeronasal 1 receptor Vom1r39"
                     /calculated_mol_wt=34435
     Region          14..292
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          16..40
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320087"
     Region          52..73
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320087"
     Region          90..112
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320087"
     Region          138..154
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320087"
     Region          188..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320087"
     Region          237..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320087"
     Region          268..292
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320087"
     CDS             1..305
                     /gene="Vom1r39"
                     /coded_by="NM_001167551.1:1..918"
                     /db_xref="GeneID:100312670"
                     /db_xref="RGD:2316471"
ORIGIN      
        1 mpapdkslkt teevalqill lcqfgvgtva niflfihnfs piltgsqqra thmiltniav
       61 antlilfvtv fpinmmtfaq rspltdlkck fefftrlvar stnlcstcvl siqqfltlvp
      121 vhrskvllra nvpnfatysc cscwvfsvln niyipvmvtg pqitdnktds krklfcstsg
      181 ftvgivflrf ihdvtfisim vwtsvsmvll lhrhlqrmqh iltpnqntrg qaetrathti
      241 lmlvvtfvsf yilnficiif hnffmdsrlf vrhvsealvl gfptisplll ifrdpknpcs
      301 vlfss
//
LOCUS       NP_001092984             856 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 48 [Rattus norvegicus].
ACCESSION   NP_001092984 XP_001066682
VERSION     NP_001092984.1
DBSOURCE    REFSEQ: accession NM_001099514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 26, 2007 this sequence version replaced XP_001066682.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.908748.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN09345330,
                                           SAMN09345331 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..856
                     /product="vomeronasal 2 receptor, 48"
                     /calculated_mol_wt=96833
     Region          40..512
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(77,176..177,403)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(115,118,163,250)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          520..573
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          593..844
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          593..618
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(596,599..600,603..604,606..607,641,645,648..649,657,
                     661)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          630..651
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(650,662..663,666..667,670,750,755,758..759,762,796,
                     799..800,803,807,815..816,819,822,826)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          660..684
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          708..724
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          751..777
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          785..808
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          813..838
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..856
                     /gene="Vom2r48"
                     /coded_by="NM_001099514.1:1..2571"
                     /db_xref="GeneID:686145"
                     /db_xref="RGD:1585454"
ORIGIN      
        1 mkllivfsll ivlivfqvqi syvslnnpas pgyyqdgdfv igglfslrmt tgdtrsklfd
       61 fkdaiylpey vygyltkhyq hmlamifaie kinkdpnilf nmslgfylfn vdfiekkaie
      121 ssmallsges ppvpnyscrp ektdklvavi ggistgistq isrvlslyni pqisyapfdh
      181 slgtrvqlqs pyqfpmhtta lyhgiiqlll yftwvwvgmv vtddmrgelf lrditeemnn
      241 hglcvafvek ipefsaqdrv tkkafmeryt strvivgfgd tysllrfvss iifhtnfgnv
      301 wittsywdft ilpfyqfisr alfsvgrlsf svrmdqilgf kdflrsvqpr kyphdiflqd
      361 vwsilfkcpy syqhgvrilt qceqngtlst rplhvwdmnt lppsykvhaa vyaiaqalhe
      421 elslgmegds ftkcvpqthl pwklhpflqk gklwrrtnqe niinkevlat vfdifnsqsl
      481 qkgnevqvqv gefvfeshsv qhfslnekli twprnqkeip lslcsqscpl gfrktpvegk
      541 psccfdclpc pdgeianetd mdqcikcped qypnkqrnqc lpkitaflsc edplgavlvs
      601 vaislsafsa milglfihyr dtpivrannr nlsylllvsl mlcffcslif icqpttvtci
      661 lrqmifgvvf sitisailak tfivvvafkv ikpgstlqtw mvtrvsnaiv ccgssiqvci
      721 cavwlgtypp fpdvdmqsef gqiilwcneg stlafycvlg ylgflaslsl liaflarrlp
      781 dtfneaktit fsmlvfcsvw isfvptylss kgktmvavei lsilassstl lgciflpkcy
      841 vilmrsgghs rkkifk
//
LOCUS       NP_001092949             857 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 58 precursor [Rattus norvegicus].
ACCESSION   NP_001092949 XP_001067069
VERSION     NP_001092949.1
DBSOURCE    REFSEQ: accession NM_001099479.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Aug 15, 2007 this sequence version replaced XP_001067069.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..857
                     /product="vomeronasal 2 receptor, 58 precursor"
                     /calculated_mol_wt=95627
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2428
     Region          41..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(72,169..170,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(110,113,156,243)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..836
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..857
                     /gene="Vom2r58"
                     /coded_by="NM_001099479.1:1..2574"
                     /db_xref="GeneID:501793"
                     /db_xref="RGD:1583708"
ORIGIN      
        1 mmlllifmfl llqyssdvys fdrsycastt ktsvykdgdm vvaaflplft itvdsasdnp
       61 snnnfyiqfn lknyqivlam vyateeinrn philpnvslg ydiynvlfne wftldrcitw
      121 lsgpkkyvpn ytcrremksi aaltgiswii stgirtllel yrypqltigs fdpnlnnheq
      181 fhdiyqiayk dmslthgivs llnyfhwnwv glivsegqng fqiisevrae mdrnkicvef
      241 velirvsevs ylpsyllnpt hlvksttnvi itygdsdflr gfmlysrqif vtrkvwimns
      301 dwdiitqsqh filnslhgsl ifahhhkets gyrnfiqtvh pskypedfyl trfwfflfnc
      361 sfadddcntl enclpnaslh ettgnhfdmv mtefaynmyn avyavaqslh kmllhevevr
      421 qvrkaedltf svwqlhpflk nihftnpvge qvsldetmkl naeydilnyw nfpeglhlkv
      481 kvgqfspygp vgqqlslsed iiewpteite tprsvcsesc gpgfrkslie gkriccfdci
      541 pcpeneisne tdvdqcmqcl dnqyantaqn hclqksitfl dyedpmgigl scialcfsal
      601 tslvlgiflk qkntpivkan nrtltyvlli alnfcflcsf lfighpntat cilqqttfav
      661 lftvavstvl aktitvvlaf kvtapgrrir wllvtrapnf tvpictliqi vlcgvwlgns
      721 ppfidtdtrs ehehiiimcn kgsvtafycv lgylgalalg sftlaflarn lpdtfneakf
      781 ltfsmlvfcs vwvtflpvyh stkgkhmvvv evfsilvssa gllgcifapk cyiillrpqr
      841 kslqghrdki hynykty
//
LOCUS       NP_783174                345 aa            linear   ROD 03-APR-2025
DEFINITION  trace amine-associated receptor 6 [Rattus norvegicus].
ACCESSION   NP_783174
VERSION     NP_783174.1
DBSOURCE    REFSEQ: accession NM_175584.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Borowsky,B., Adham,N., Jones,K.A., Raddatz,R., Artymyshyn,R.,
            Ogozalek,K.L., Durkin,M.M., Lakhlani,P.P., Bonini,J.A.,
            Pathirana,S., Boyle,N., Pu,X., Kouranova,E., Lichtblau,H.,
            Ochoa,F.Y., Branchek,T.A. and Gerald,C.
  TITLE     Trace amines: identification of a family of mammalian G
            protein-coupled receptors
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 8966-8971 (2001)
   PUBMED   11459929
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF380191.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..345
                     /product="trace amine-associated receptor 6"
                     /note="trace amine receptor 6; taR-4; taR-6; trace amine
                     receptor 4"
                     /calculated_mol_wt=38180
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          33..322
                     /region_name="7tmA_TAAR6_8_9"
                     /note="trace amine-associated receptors 6, 8, and 9,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15316"
                     /db_xref="CDD:320439"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          34..60
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320439"
     Region          67..93
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320439"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          105..135
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320439"
     Site            order(108,112..113,116..117,192,198,201..202,205,271,
                     274..275,278,293,297,301)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320439"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          147..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320439"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          194..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320439"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          251..281
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320439"
     Site            260..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Site            283..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923Y5.1)"
     Region          290..315
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320439"
     CDS             1..345
                     /gene="Taar6"
                     /gene_synonym="Ta4; TRAR4"
                     /coded_by="NM_175584.1:1..1038"
                     /db_xref="GeneID:294124"
                     /db_xref="RGD:631384"
ORIGIN      
        1 mgsnssppav lqlcyenvng scvktpyspg prvllyavfg fgavlavfgn llvmisilhf
       61 kqlhsptnfl iaslacadfw vgvsvmpfsm vrsiescwyf grsfctfhtc cdvafcyssl
      121 fhlsfisidr yiavtdplvy ptkftvsvsg icisiswilp laysgavfyt gvyadgleev
      181 sdavncvggc qvvvnqnwvl idflsflipt lvmiilygni flvarqqakk ietvgnkaes
      241 ssesykarva rrerkaaktl gitvvafmis wlpysidslv dafmgfitpa yiyeicvwca
      301 yynsamnpli yalfypwfkk aikvimsgqv fknssatmnl fseqi
//
LOCUS       NP_001178006             343 aa            linear   ROD 03-APR-2025
DEFINITION  membrane progestin receptor delta [Rattus norvegicus].
ACCESSION   NP_001178006 XP_001059976
VERSION     NP_001178006.1
DBSOURCE    REFSEQ: accession NM_001191077.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Tang,Y.T., Hu,T., Arterburn,M., Boyle,B., Bright,J.M., Emtage,P.C.
            and Funk,W.D.
  TITLE     PAQR proteins: a novel membrane receptor family defined by an
            ancient 7-transmembrane pass motif
  JOURNAL   J Mol Evol 61 (3), 372-380 (2005)
   PUBMED   16044242
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_001059976.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.34527.1,
                                           SRR26643284.3074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..343
                     /product="membrane progestin receptor delta"
                     /note="progestin and adipoQ receptor family member VI"
                     /calculated_mol_wt=38140
     Region          43..271
                     /region_name="HlyIII"
                     /note="Haemolysin-III related; pfam03006"
                     /db_xref="CDD:427098"
     CDS             1..343
                     /gene="Paqr6"
                     /coded_by="NM_001191077.1:64..1095"
                     /db_xref="GeneID:681021"
                     /db_xref="RGD:1584722"
ORIGIN      
        1 mlslklpqll rvhqvprvfw eegimsgyrc ptssaldcvl ssfqmtnetv niwthflptw
       61 yflwrllalg spgfhaepyh lpllvfllpt clypfascca htfssmspra rhicyfldyg
      121 alslyslgca fpyaaysmpa swlhsrlhql fvpaaalnsf lctglscysr fpelenpgls
      181 kvlrtaafay pflfdnlplf yrlrlcwgra hscgrdalsc shgyhllcal ltgflfaarl
      241 perlapgrfd yighshqlfh icavlgthfq leavladmgs rrgwlamqep ilgleatvat
      301 lslavignll iiaaftasll rspgacpllq ggpleeelea kqq
//
LOCUS       NP_001182487             366 aa            linear   ROD 03-APR-2025
DEFINITION  leucine-rich repeat-containing protein 58 [Rattus norvegicus].
ACCESSION   NP_001182487 XP_001069929 XP_221433
VERSION     NP_001182487.1
DBSOURCE    REFSEQ: accession NM_001195558.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On or before Nov 24, 2010 this sequence version replaced
            XP_221433.4, XP_001069929.1.
            
            Sequence Note: This RefSeq record was created from Celera genomic
            sequence data as a full-length  transcript is not represented in
            the current reference genome assembly. The genomic coordinates used
            for the transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.39357.1,
                                           SRR26643299.48131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..366
                     /product="leucine-rich repeat-containing protein 58"
                     /calculated_mol_wt=39996
     Region          4..>242
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          41..64
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          65..87
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          88..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          140..162
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          163..185
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          209..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..366
                     /gene="Lrrc58"
                     /gene_synonym="RGD1307440"
                     /coded_by="NM_001195558.1:55..1155"
                     /db_xref="GeneID:303919"
                     /db_xref="RGD:1307440"
ORIGIN      
        1 meeaalgeae lnwsrlsvsa ealeselear aeerrgsrea llrlllpynr ltslpralgs
       61 gfphlqlldv sgnaltalgp elltlsglrt llarnnrlgg pgslpkglgq splcrslqvl
      121 nlsgncfqel pasllelral qtlslggnql qsipaeienl qsleclylgg nfikeippel
      181 anlpslnylv lcdnkiqsvp pqlsqlhslr slslhnnllt ylpreilnli hleelslrgn
      241 plvvrfvrdl tydpptllel aartikirsi sytpydlpgn llrylgsasn cpnpkcggvy
      301 fdccvrqikf vdfcgkyrlp lmhylcspec sspcssashs stsqsesdse deasvaahrm
      361 qkvllg
//
LOCUS       NP_001092960             857 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 15 [Rattus norvegicus].
ACCESSION   NP_001092960 XP_001075192
VERSION     NP_001092960.1
DBSOURCE    REFSEQ: accession NM_001099490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 26, 2007 this sequence version replaced XP_001075192.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..857
                     /product="vomeronasal 2 receptor, 15"
                     /calculated_mol_wt=98005
     Region          42..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,170..171,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(109,111,154,244)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          513..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..836
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..857
                     /gene="Vom2r15"
                     /coded_by="NM_001099490.1:1..2574"
                     /db_xref="GeneID:690680"
                     /db_xref="RGD:1593392"
ORIGIN      
        1 mftlslffll lnipllmtcl iyprcfwsmr qdeyenrsle rgcaffirav kwpvekeyfs
       61 nalniqthte nqkyalalaf smneinlnpn llpnmslvft ystdacdwea ifksvihldl
      121 qehkilpnyi ctedikcgva ltgfnwattv tihillnnfi fqkfihltyg sfypvlsdhe
      181 kfpylyqmas edtslalalv sfiihfswnw vglaisdndk gtqflsylrr emekntvcfa
      241 fvnmipvnmr lfmsraevyy nqimtsstnv vimygdkdst lavsfrmwvs lgiqriwitt
      301 aqwdvtprmk dltfdnlcgt fafgqhhgei yglknyaqtl npfiysdeyl lklewmyfnc
      361 nvtaskwkpf kncssnhsle wlmthtfdma fiegsydiyn avyafahalh qvtfqkgdnl
      421 ptdnrkeqdy dckklcsflr kthftnpagd rvnmnqiekl qeeydifyiw nfpqgiglkl
      481 kigifspyfq tgqhlhlsed iiewakegsq mltsvcsadc gpgfrkfrkn gmpaccfdcs
      541 pcpenkisne tnvemcilcp edqyanteqn hciqkplifl tyeeplgiti slmalcfsal
      601 tavilgvfvk hhstpivkas nhiltyilli slifcflcpl lfighpnsat cilqqitfgv
      661 vftvaistvl aktitvilaf kvtapqrmmk yflvqrasny iipmctliqv ivcavwlgas
      721 ppfvdidtqs ehghiiivcn kgsvtafycv lgylaclsfa sfflaffsrn lpgnfneaks
      781 mtfsmllfcs vwitflpvyh gtkgkvmvav eifstlassa gmlgcifipk cytilfrpdk
      841 nslqmirekl sshthis
//
LOCUS       NP_001092936             856 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 59 precursor [Rattus norvegicus].
ACCESSION   NP_001092936 XP_221799
VERSION     NP_001092936.1
DBSOURCE    REFSEQ: accession NM_001099466.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Aug 19, 2007 this sequence version replaced XP_221799.4.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..856
                     /product="vomeronasal 2 receptor, 59 precursor"
                     /calculated_mol_wt=95897
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2455
     Region          41..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(72,169..170,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(110,113,156,243)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..836
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..856
                     /gene="Vom2r59"
                     /gene_synonym="RGD1566381"
                     /coded_by="NM_001099466.1:1..2571"
                     /db_xref="GeneID:288396"
                     /db_xref="RGD:1566381"
ORIGIN      
        1 mmlllifmfl llqysndvys fdrsycasrt ktsvykdgdm vvaaflplft itvdsasdnq
       61 snnnfhiqfn lknyqivlam vyaieeinrn philpnvslg ydiynvlfne wftlhrcisw
      121 lsgpkkyvpn ytcrremksi aaltgiswii stdirtllel yrypqltigs fdpnlnnheq
      181 fhdiyqiayk dmslthgivs llnyfhwnwv glivsegqng fqiisevrae mdrnkicldf
      241 velirvsevs ylpsyllnpt hlakltanvi itygdsdflr gfmfysrqif vtrkvwimns
      301 dwdiitqsqh filhslhgsl ifahhhkets gyrnfiqtvh pskypedfyl trfwfyffnc
      361 sfadddcstl enclpnaslh etpgnrfdmv mtefaynmyn avyavahslh kmllhevevr
      421 evrkaedlif sawqlhpflk nmqftnpage qvtldekmkl naeydilnyw nfpeglhlkv
      481 kvgqfspygp ldqqlslsed iiewpteite tprsvcsesc gpgfrkslpe gkriccfdci
      541 pcpeneisne tdvdqcmqcl dhqyantaqn hclqksmtfl hyedpmgisl scialcfsal
      601 tslvlgiflk qkntpivkan nrtltyilli alnfcflcsf lfighpntvt cilqqttfav
      661 vftvavstvl aktitvvlaf kvtapgrrir wllvtrapnf ivpictliqi ilcgvwlgns
      721 ppfidtdths enehiiimcn kgsvtafycv lgylgalalg sftlaflarn lpdtfneakf
      781 ltfsmlvfcs vwvtflpvyh stkgkhmvvv evfsilvssa gllgcifapk cyiillrpqr
      841 nslqshrhki hykymt
//
LOCUS       NP_001178706             277 aa            linear   ROD 03-APR-2025
DEFINITION  protein CIMAP1D [Rattus norvegicus].
ACCESSION   NP_001178706 XP_234905
VERSION     NP_001178706.1
DBSOURCE    REFSEQ: accession NM_001191777.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Jul 17, 2010 this sequence version replaced XP_234905.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760475,
                              SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..277
                     /product="protein CIMAP1D"
                     /note="outer dense fiber protein 3-like protein 2; outer
                     dense fiber of sperm tails 3-like 2"
                     /calculated_mol_wt=29524
     Region          <52..262
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..277
                     /gene="Cimap1d"
                     /gene_synonym="Odf3l2; RGD1310260"
                     /coded_by="NM_001191777.1:1..834"
                     /db_xref="GeneID:299600"
                     /db_xref="RGD:1310260"
ORIGIN      
        1 mgtlscdpva rpatvplarr vadghipetg lrkscgvatl engsgpglyv lpstvgyvnh
       61 dctkaaspay slarrpseap lqdsspgpvy fldpkvtrfg rscppaysmq grgkirglev
      121 tpgpgayspe ktppirqrna paftlgsrlr qkppdtsapa pnaytmpplw gsqifikpss
      181 psytvvgrtp parppqdpse tpgpgqyesp dpntyrqrrp afsilgrprt prppedtpgp
      241 gthnpeqvtv nrarapaytm girhskrast mvgdtkc
//
LOCUS       NP_001092958             853 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 12 precursor [Rattus norvegicus].
ACCESSION   NP_001092958 XP_001074831
VERSION     NP_001092958.3
DBSOURCE    REFSEQ: accession NM_001099488.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 3, 2021 this sequence version replaced NP_001092958.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..853
                     /product="vomeronasal 2 receptor, 12 precursor"
                     /calculated_mol_wt=94382
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2134
     Region          41..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,170..171,390)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(111,114,154,244)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          508..561
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          582..832
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          582..606
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(584,587..588,591..592,594..595,629,633,636..637,645,
                     649)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          618..639
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(638,650..651,654..655,658,738,743,746..747,750,784,
                     787..788,791,795,803..804,807,810,814)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          648..672
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          696..712
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          739..765
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          773..796
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          801..826
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..853
                     /gene="Vom2r12"
                     /coded_by="NM_001099488.3:1..2562"
                     /db_xref="GeneID:690566"
                     /db_xref="RGD:1594694"
ORIGIN      
        1 mftlilsfll lniplqvtgf iyptcswrik enkdksgner igcffliqav qkpvekeyfs
       61 hffntqkhte ihkyslvlaf smievnrnpd llpnmslvfs freiicgwqp elsifievnl
      121 ddygvlpnyt ckddslcgvv ltglnwaptl llytilnnfk sqqfphltyg hyhpvpsdhe
      181 nfpylyqmas ddtslalalv sfiihfswnw iglafsdndq gthflsylkr gmeknavcla
      241 fvsmipvdmh lymsraevyy sqiltssanv viiygdtgst lavsfrmwes lglqrlwitt
      301 tqldvtpsmk eniyglfafg hhhgvisgfk nfvqtlnpvt ysndnlakle wmhfncevsa
      361 skwktlknfs snhslewlme ntfemtfseg syniynavyt vahvlhkmtf qkfhnlpnak
      421 gkvqnyvcnk lgaplrkihf tnpvgdrinm nredklqeey difyiwnfpq glafkvkigl
      481 fspyfingqq lhlsgdmiew argstqmpts vcsadcgpgf rkfrkkemsa ccfdcspcpe
      541 neisnetnme mcvlcpedky antgqndcip kaliflsyed hlgmalslma lgfsaftavv
      601 lgifvkhhst pivkannrtl tyilllslif cflcpllfig hpdsvtcilq qitfgvlftv
      661 aistvlakti tvilafkvta pqrmmkyfll sgvsmyiipi ctliqvivca vclgvsppsv
      721 didaqsehgh iivvcnngsv tcfysvlgyl acltfvsftl aflsrnlpga fneaksitfs
      781 mlvvcsvwvt flpvyhstkg kimvaveiis ilasssgmlv cifipkcyii lfrpeknslk
      841 mirekspsht his
//
LOCUS       NP_001092929             841 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 6 precursor [Rattus norvegicus].
ACCESSION   NP_001092929 XP_001067478 XP_218121
VERSION     NP_001092929.3
DBSOURCE    REFSEQ: accession NM_001099459.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Feb 3, 2021 this sequence version replaced NP_001092929.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMN17050755
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..841
                     /product="vomeronasal 2 receptor 6 precursor"
                     /calculated_mol_wt=93454
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2969
     Region          45..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,167..168,391)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          508..561
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          581..832
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          581..606
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(584,587..588,591..592,594..595,629,633,636..637,645,
                     649)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          618..639
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(638,650..651,654..655,658,738,743,746..747,750,784,
                     787..788,791,795,803..804,807,810,814)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          648..672
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          696..712
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          739..765
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          773..796
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          801..826
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..841
                     /gene="Vom2r6"
                     /gene_synonym="RGD1562697"
                     /coded_by="NM_001099459.3:1..2526"
                     /db_xref="GeneID:308257"
                     /db_xref="RGD:1562697"
ORIGIN      
        1 mkklcaftia ffslkfclil csltepncfw rikksedndg dlrsdcgfvl ftdedpieed
       61 fynriinfri pgrkyefflv lffatdeink npnllsnmsl sfsiivglce dtlgvlekay
      121 shknnnfeli nyycrmkqcc dveltgpswt tslklsiysr kpkiffgsfn pnlsdhdqfp
      181 yiyqiaakdt ylfhgmvslm fhfgwtwigl visdddqgiq flsdlreeiq rheiclafvn
      241 mipetmqifk trlkiydqql mtssakvvvi ygemnstlel sfrrwaylga qriwittsqw
      301 dvtthkkdfs ldffhgtvtf ahhhndiavf rnfmqtints kypidisqsm lhwnhfncsi
      361 sknnnkmdcl tfnnslewla qhtfdmalsd egynlynavy avahtyheli fqqvesqkme
      421 epkgicadcq qvasllktrv ftnpvgelvn mnhkenqcak ydifmiwnfp qglglkvkig
      481 syfpclpqsq qlhisenwew vtgetvvpss vcsvtctagf rkihqkqtad ccfdcvqcqe
      541 neiandtdme qcvrcpddsy anleqtqclq ravtflayed plgmalgcma lsfsaittlv
      601 lvtfvkyrdt pivkannril syillislvf cflcsllfig hpnqatcilq qttfaifftv
      661 aistvlakti tvvtafkltt pgrrirrmmi kgatnllipi ctliqlvlcg iwlvtsppfi
      721 drdtqsehgk iviicnkgsd iafhfvlgyl gslalgsftv aflarnlpdr fneakfltfs
      781 mlvfysvwit flpvyhstrg kvmvvvevfs ilascagllg cifvqkcyil lfrtdlnflq
      841 k
//
LOCUS       NP_001099618             496 aa            linear   ROD 03-APR-2025
DEFINITION  myotilin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099618 XP_001053135 XP_001053210 XP_214563
VERSION     NP_001099618.1
DBSOURCE    REFSEQ: accession NM_001106148.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   von Nandelstadh,P., Ismail,M., Gardin,C., Suila,H., Zara,I.,
            Belgrano,A., Valle,G., Carpen,O. and Faulkner,G.
  TITLE     A class III PDZ binding motif in the myotilin and FATZ families
            binds enigma family proteins: a common link for Z-disc myopathies
  JOURNAL   Mol Cell Biol 29 (3), 822-834 (2009)
   PUBMED   19047374
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hauser,M.A., Horrigan,S.K., Salmikangas,P., Torian,U.M.,
            Viles,K.D., Dancel,R., Tim,R.W., Taivainen,A., Bartoloni,L.,
            Gilchrist,J.M., Stajich,J.M., Gaskell,P.C., Gilbert,J.R.,
            Vance,J.M., Pericak-Vance,M.A., Carpen,O., Westbrook,C.A. and
            Speer,M.C.
  TITLE     Myotilin is mutated in limb girdle muscular dystrophy 1A
  JOURNAL   Hum Mol Genet 9 (14), 2141-2147 (2000)
   PUBMED   10958653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH474178.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001053135.1, XP_001053210.1, XP_214563.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760384,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..496
                     /product="myotilin isoform 1"
                     /note="titin immunoglobulin domain protein (myotilin)"
                     /calculated_mol_wt=54992
     Region          248..338
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          278..282
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          347..438
                     /region_name="IgI_Myotilin_C"
                     /note="C-terminal immunoglobulin (Ig)-like domain of
                     myotilin; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05892"
                     /db_xref="CDD:409473"
     Region          347..350
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409473"
     Region          353..358
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409473"
     Region          363..370
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409473"
     Region          377..383
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409473"
     Region          384..387
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409473"
     Region          394..400
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409473"
     Region          403..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409473"
     Region          417..425
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409473"
     Region          427..438
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409473"
     CDS             1..496
                     /gene="Myot"
                     /gene_synonym="Ttid"
                     /coded_by="NM_001106148.1:271..1761"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:291605"
                     /db_xref="RGD:1310569"
ORIGIN      
        1 mfnyerpkhf iqsqnpcgsg lqppgpevss fpnqtkqssi viqprqcteq rfsasstvss
       61 hitvsssayp asqqlagpnp gqkvtatynq spasflssil psqpdysnsk ipstvdsnyq
      121 qssvhqpvna vssqaagakp tprtpdheiq gskealiqdl erklkckdtl lhngnqrlty
      181 eekmarrllg pqnaaavfqa qnsdvqdssq hnpeharlqv ptsqvrsrss sradandqda
      241 iqekfypprf iqvpenmsie egrfcrmdfk vsglpapdvs wylngrlvqs delhkmivse
      301 kgfhslifev vrasdagpya cvarnragea tftvqldvla kehkrapmfi ykpqskkvfe
      361 gesvklecqi saipppklfw krnnemvqfn tdrislyhdn agrvtllikd vnkkdagwyt
      421 vsavneagvt tcntrldvta rpnqtppapk qlrvrptfsk ylalngkgld vkqafnpege
      481 fqrlaaqsgl yeseel
//
LOCUS       NP_001161044             301 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 17 [Rattus norvegicus].
ACCESSION   NP_001161044
VERSION     NP_001161044.1
DBSOURCE    REFSEQ: accession NM_001167572.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..301
                     /product="vomeronasal 1 receptor 17"
                     /note="vomeronasal 1 receptor Vom1r17; vomeronasal type-1
                     receptor 4-like; vomeronasal V1r-type receptor V1rf4;
                     vomeronasal type-1 receptor 3-like"
                     /calculated_mol_wt=33806
     Region          8..287
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          8..32
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          44..65
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          82..104
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          130..143
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          178..201
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          230..252
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          262..287
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..301
                     /gene="Vom1r17"
                     /coded_by="NM_001167572.1:1..906"
                     /db_xref="GeneID:100312945"
                     /db_xref="RGD:2316476"
ORIGIN      
        1 mnaselsigv iilsqtvigv lanffllyhc milyltryrl rsidcvlmql svaniltils
       61 kgipqtiaaf glkdflndig ckltffvhkv gksvcigsts flsvlqaiii spkdsrcpkl
      121 kvkvrkyicy svwviffiis ilnllhlrap ytnestitlk sfvycycvrh dptsdilhav
      181 lvsgpdiifl glmlytsgft vltlyrhkqk mqqmprmnvs sisspasrat ktilllvstf
      241 vsfytistlc hllvvilynp swilvnvaam sasffptvyp fllmshdswa lsfclllkrn
      301 r
//
LOCUS       NP_001157393             554 aa            linear   ROD 03-APR-2025
DEFINITION  EF-hand and coiled-coil domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001157393 XP_001062782 XP_001062901 XP_001075064 XP_001075115
VERSION     NP_001157393.1
DBSOURCE    REFSEQ: accession NM_001163921.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Aug 8, 2009 this sequence version replaced
            XP_001062782.1, XP_001062901.1, XP_001075064.1, XP_001075115.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..554
                     /product="EF-hand and coiled-coil domain-containing
                     protein 1"
                     /note="coiled-coil domain containing 48 like; coiled-coil
                     domain containing 48-like1; EF-hand domain-containing
                     protein ENSP00000381169 homolog"
                     /calculated_mol_wt=61684
     Region          7..553
                     /region_name="CCD48"
                     /note="Coiled-coil domain-containing protein 48;
                     pfam15799"
                     /db_xref="CDD:464878"
     CDS             1..554
                     /gene="Efcc1"
                     /gene_synonym="Ccdc48; Ccdc48l1"
                     /coded_by="NM_001163921.1:25..1689"
                     /db_xref="GeneID:685202"
                     /db_xref="RGD:1596494"
ORIGIN      
        1 messagdpyr rparraqwll salahhygld rgveneivvl atgldqylqe vfhhldcrga
       61 grlpradfra lcavlglnad geaakedans tevaaknpat gmiaggdadv reeallalra
      121 dppeltfrqf harlcgyfss ragsrlprga lsehietqir lrrprrrrrp gspslhggay
      181 gervahleee nsslrelved lraalqssda rclalqvglw ksqsdipeaa ahelqraqga
      241 laeaeararr lqrgqvevrl rteearqavr rslhrvrele slarrvprlq rqvqrleael
      301 rryrsegpql ltppqtsprp gnkngeptar gtrdsdttse gvlqsdtkee qlfrsvegqa
      361 aseeeeeerw qekpgrpqah sevplmqpsg cvnrcddqta etlkasfghc dgaehvctle
      421 lephvtrlge qlqtlgcnpf yqaelqqmve tehlrlelqm vetervrlsl meeklvdvlq
      481 llqrlrdlni skralgkmll naldqnpsqe gtrgtlaild tlhqalvgce llqrnpsapa
      541 skapahtnpf lvsc
//
LOCUS       NP_001178612             835 aa            linear   ROD 03-APR-2025
DEFINITION  B-cell lymphoma/leukemia 11A [Rattus norvegicus].
ACCESSION   NP_001178612 XP_223693
VERSION     NP_001178612.1
DBSOURCE    REFSEQ: accession NM_001191683.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Zhang,Y., Shen,Y., Zhao,L., Zhao,Q., Zhao,L. and Yi,S.
  TITLE     Transcription Factor BCL11A Regulates Schwann Cell Behavior During
            Peripheral Nerve Regeneration
  JOURNAL   Mol Neurobiol 60 (9), 5352-5365 (2023)
   PUBMED   37316757
  REMARK    GeneRIF: Transcription Factor BCL11A Regulates Schwann Cell
            Behavior During Peripheral Nerve Regeneration.
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Basak,A., Hancarova,M., Ulirsch,J.C., Balci,T.B., Trkova,M.,
            Pelisek,M., Vlckova,M., Muzikova,K., Cermak,J., Trka,J.,
            Dyment,D.A., Orkin,S.H., Daly,M.J., Sedlacek,Z. and Sankaran,V.G.
  TITLE     BCL11A deletions result in fetal hemoglobin persistence and
            neurodevelopmental alterations
  JOURNAL   J Clin Invest 125 (6), 2363-2368 (2015)
   PUBMED   25938782
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Al-Allawi,N.A., Puehringer,H., Raheem,R.A. and Oberkanins,C.
  TITLE     Genetic Modifiers in beta-Thalassemia Intermedia: A Study on 102
            Iraqi Arab Patients
  JOURNAL   Genet Test Mol Biomarkers 19 (5), 242-247 (2015)
   PUBMED   25751242
REFERENCE   4  (residues 1 to 835)
  AUTHORS   De Rubeis,S., He,X., Goldberg,A.P., Poultney,C.S., Samocha,K.,
            Cicek,A.E., Kou,Y., Liu,L., Fromer,M., Walker,S., Singh,T.,
            Klei,L., Kosmicki,J., Shih-Chen,F., Aleksic,B., Biscaldi,M.,
            Bolton,P.F., Brownfeld,J.M., Cai,J., Campbell,N.G., Carracedo,A.,
            Chahrour,M.H., Chiocchetti,A.G., Coon,H., Crawford,E.L.,
            Curran,S.R., Dawson,G., Duketis,E., Fernandez,B.A., Gallagher,L.,
            Geller,E., Guter,S.J., Hill,R.S., Ionita-Laza,J., Jimenz
            Gonzalez,P., Kilpinen,H., Klauck,S.M., Kolevzon,A., Lee,I., Lei,I.,
            Lei,J., Lehtimaki,T., Lin,C.F., Ma'ayan,A., Marshall,C.R.,
            McInnes,A.L., Neale,B., Owen,M.J., Ozaki,N., Parellada,M.,
            Parr,J.R., Purcell,S., Puura,K., Rajagopalan,D., Rehnstrom,K.,
            Reichenberg,A., Sabo,A., Sachse,M., Sanders,S.J., Schafer,C.,
            Schulte-Ruther,M., Skuse,D., Stevens,C., Szatmari,P., Tammimies,K.,
            Valladares,O., Voran,A., Li-San,W., Weiss,L.A., Willsey,A.J.,
            Yu,T.W., Yuen,R.K., Cook,E.H., Freitag,C.M., Gill,M., Hultman,C.M.,
            Lehner,T., Palotie,A., Schellenberg,G.D., Sklar,P., State,M.W.,
            Sutcliffe,J.S., Walsh,C.A., Scherer,S.W., Zwick,M.E., Barett,J.C.,
            Cutler,D.J., Roeder,K., Devlin,B., Daly,M.J. and Buxbaum,J.D.
  CONSRTM   DDD Study; Homozygosity Mapping Collaborative for Autism; UK10K
            Consortium
  TITLE     Synaptic, transcriptional and chromatin genes disrupted in autism
  JOURNAL   Nature 515 (7526), 209-215 (2014)
   PUBMED   25363760
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Chu,N.L., Wu,Z.K., Zhang,X.H., Fang,S.P., Wang,W.J. and Cheng,Y.L.
  TITLE     Molecular mechanism of yisui shengxue granule, a complex chinese
            medicine, on thalassemia patients suffering from hemolysis and
            anemia of erythrocytes
  JOURNAL   Evid Based Complement Alternat Med 2014, 213782 (2014)
   PUBMED   25574177
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Lettre,G., Sankaran,V.G., Bezerra,M.A., Araujo,A.S., Uda,M.,
            Sanna,S., Cao,A., Schlessinger,D., Costa,F.F., Hirschhorn,J.N. and
            Orkin,S.H.
  TITLE     DNA polymorphisms at the BCL11A, HBS1L-MYB, and beta-globin loci
            associate with fetal hemoglobin levels and pain crises in sickle
            cell disease
  JOURNAL   Proc Natl Acad Sci U S A 105 (33), 11869-11874 (2008)
   PUBMED   18667698
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Kuo,T.Y. and Hsueh,Y.P.
  TITLE     Expression of zinc finger transcription factor Bcl11A/Evi9/CTIP1 in
            rat brain
  JOURNAL   J Neurosci Res 85 (8), 1628-1636 (2007)
   PUBMED   17455301
  REMARK    GeneRIF: regional and subcellular distributions of
            Bcl11A/Evi9/CTIP1 in rat brain were investigated by immunostaining
            and biochemical fractionation
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Liu,P., Keller,J.R., Ortiz,M., Tessarollo,L., Rachel,R.A.,
            Nakamura,T., Jenkins,N.A. and Copeland,N.G.
  TITLE     Bcl11a is essential for normal lymphoid development
  JOURNAL   Nat Immunol 4 (6), 525-532 (2003)
   PUBMED   12717432
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Satterwhite,E., Sonoki,T., Willis,T.G., Harder,L., Nowak,R.,
            Arriola,E.L., Liu,H., Price,H.P., Gesk,S., Steinemann,D.,
            Schlegelberger,B., Oscier,D.G., Siebert,R., Tucker,P.W. and
            Dyer,M.J.
  TITLE     The BCL11 gene family: involvement of BCL11A in lymphoid
            malignancies
  JOURNAL   Blood 98 (12), 3413-3420 (2001)
   PUBMED   11719382
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Avram,D., Fields,A., Pretty On Top,K., Nevrivy,D.J., Ishmael,J.E.
            and Leid,M.
  TITLE     Isolation of a novel family of C(2)H(2) zinc finger proteins
            implicated in transcriptional repression mediated by chicken
            ovalbumin upstream promoter transcription factor (COUP-TF) orphan
            nuclear receptors
  JOURNAL   J Biol Chem 275 (14), 10315-10322 (2000)
   PUBMED   10744719
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jul 17, 2010 this sequence version replaced XP_223693.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.47681.1, DY315645.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..835
                     /product="B-cell lymphoma/leukemia 11A"
                     /note="B-cell CLL/lymphoma 11A (zinc finger protein);
                     BCL11A, BAF complex component; BAF chromatin remodeling
                     complex subunit BCL11A"
                     /calculated_mol_wt=91016
     Region          378..399
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          391..416
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          743..764
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          744..764
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(749,751,753,755..756,759..760,763,777,779,783..784,
                     787..788,791,807,809,811,813..814,817..818)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          756..781
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          772..792
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          802..820
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..835
                     /gene="Bcl11a"
                     /coded_by="NM_001191683.1:243..2750"
                     /db_xref="GeneID:305589"
                     /db_xref="RGD:1309923"
ORIGIN      
        1 msrrkqgkpq hlskrefspe pleailtdde pdhgplgape gdhdlltcgq cqmnfplgdi
       61 lifiehkrkq cngslclekg vdkppspspi emkkasnpve vgiqvtpedd dclstssrgi
      121 cpkqehiadk llhwrglssp rsahgalipt pgmsaeyapq gickdepssy tcttckqpft
      181 sawfllqhaq nthglriyle sehgspltpr vgipsglgae cpsqpslhgi piadnnpfnl
      241 lripgsvsre asglaegrfp ptpplfsppp rhhldphrie rlgaeemala thhpsafdrv
      301 lrlnpmamep pamdfsrrlr elagntsspp lspgrpspmq rllqpfqpgs kppflatppl
      361 pplqsappps qppvksksce fcgktfkfqs nlvvhrrsht gekpykcnlc dhactqaskl
      421 krhmkthmhk sspmtvksdd glstasspep gtsdlvgsas salksvvakf ksendpnlip
      481 engdeeeeed deeeeeeeee eeeelteser vdygfglsle aarhhenssr gavvgvgdeg
      541 ralpdvmqgm vlssmqhfse afhqvlgekh krshlaeaeg hrdtcdedsv agesdriddg
      601 tvngrgcspg esasgglskk lllgspssls pfskriklek efdlppaamp ntenvysqwl
      661 agyaasrqlk dpfltfgdsr qspfassseh ssengslrfs tppgeldggi sgrsgtgsgg
      721 stphisgpgp grpsskegrr sdtceycgkv fkncsnltvh rrshtgerpy kcelcnyaca
      781 qsskltrhmk thgqvgkdvy kceickmpfs vystlekhmk kwhsdrvlnn dikte
//
LOCUS       NP_001092976             821 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 47 [Rattus norvegicus].
ACCESSION   NP_001092976 XP_001059944 XP_345219
VERSION     NP_001092976.1
DBSOURCE    REFSEQ: accession NM_001099506.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Martini,S., Silvotti,L., Shirazi,A., Ryba,N.J. and Tirindelli,R.
  TITLE     Co-expression of putative pheromone receptors in the sensory
            neurons of the vomeronasal organ
  JOURNAL   J Neurosci 21 (3), 843-848 (2001)
   PUBMED   11157070
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_345219.2, XP_001059944.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..821
                     /product="vomeronasal 2 receptor 47"
                     /note="vomeronasal receptor V2R2a"
                     /calculated_mol_wt=92599
     Region          1..447
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          455..508
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          528..780
                     /region_name="7tmC_V2R-like"
                     /note="vomeronasal type-2 receptor-like proteins, member
                     of the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15280"
                     /db_xref="CDD:320407"
     Region          528..553
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320407"
     Site            order(531,534..535,538..539,541..542,576,580,583..584,592,
                     596)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320407"
     Region          565..586
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320407"
     Site            order(585,597..598,601..602,605,684,689,692..693,696,730,
                     733..734,737,741,749..750,753,756,760)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320407"
     Region          595..619
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320407"
     Region          642..658
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320407"
     Region          685..711
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320407"
     Region          719..742
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320407"
     Region          747..772
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320407"
     CDS             1..821
                     /gene="Vom2r47"
                     /coded_by="NM_001099506.1:10..2475"
                     /db_xref="GeneID:365807"
                     /db_xref="RGD:1559813"
ORIGIN      
        1 mktmihtike inerkdilpn htlgyqifdt cfsisktves tfvfltgqee ykpnfrnssg
       61 kylagiigsg gsslsvassr ilevyymsqv gytssssils dhfrfptfyr tipsdkiqte
      121 amvnlikhfg wvwvgaiaad ddygkygiks fkeklersnl cvafsetipk vysnekmqka
      181 inavksstak vvvlyatdid lrpfvlevvh hnitdrtwia seawitsali akpeyfpyfg
      241 gtigfaiprs vipglkefly dvhpskdpnd vltiefwqta fnctwpnssv pynvdyrgnm
      301 tgkedrfyam sdrlctgeek ledlkntyld tsqlritnnv kqavyllaha ldrlsrcdvp
      361 qpdvkcsqip nfdpfelmiy imrmeftthd grkieldrsg dvkngyydil nwqmddagei
      421 afvkfgeykf tsskyelvls knstlfwnte sselpdsfct klcppgtrkg irqgkptccf
      481 dcipcadgyv sekpgqrecd pcseddwsna ekskcvpklv eflsyeealg ftlvilsifg
      541 alvvmavtvv yvihrhtplv kandrelsff iqmslvitvl ssmlfigkpc nwscmarqvt
      601 lalgfclcls silgktislf fayriskskt rlismhpifr klivlicvvg eigvctaylv
      661 lepprmfkni epqnvkiife cnegsiefly sifgfnvlla llcflttfva rqlpdnyyeg
      721 kcitfgmlvf fivwisfvpa ylstkgkfkv aveifailas sygllgcvfl pkcfiillrp
      781 krntdetvgg rvptldksiq ltsasvssel nntaesivld e
//
LOCUS       NP_001092979             855 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 62 [Rattus norvegicus].
ACCESSION   NP_001092979 XP_001059771
VERSION     NP_001092979.1
DBSOURCE    REFSEQ: accession NM_001099509.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Aug 15, 2007 this sequence version replaced XP_001059771.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..855
                     /product="vomeronasal 2 receptor, 62"
                     /calculated_mol_wt=96086
     Region          40..503
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(71,168..169,393)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(109,112,155,242)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..567
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          587..837
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          587..612
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(590,593..594,597..598,600..601,635,639,642..643,651,
                     655)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          624..645
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(644,656..657,660..661,664,744,749,752..753,756,790,
                     793..794,797,801,809..810,813,816,820)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          654..678
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          702..718
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          745..771
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          779..802
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          807..832
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..855
                     /gene="Vom2r62"
                     /coded_by="NM_001099509.1:1..2568"
                     /db_xref="GeneID:501816"
                     /db_xref="RGD:1598200"
ORIGIN      
        1 mptwifffft lmlpmllckl lthkcfvsst dsvyqdgdlv isaflplyty qtsqhtegae
       61 sidvssritp ynyqyamali faieeinrnp illpnvtlgy nihnagsies etvlsflkwl
      121 tgqdifipny tcktkeksva aitgktweis slialflgly kypqlsigpf epsmnnsekf
      181 pflyqmaake sslalgmvsl fvhfrwnwvg lvisedengv nfvtdlipqm erntvcvafm
      241 efipvthmmd ldnayeyhir imrypakvvi vyantdsslg vlfrrweyil pwriwvttsq
      301 wevitsmrhl ildsfhgtli fsqrqgdist fkefvktvrp skypddifla rlweiyfdca
      361 isnatckslk ncssrgnlgl lpwyhfdiav stssyhvyna vyavahtmhk mltqkgdlqg
      421 mknggsmdfp plklssllkn ikfmnpggdp islnpseklh idydilnfwd fpqgltykvk
      481 igtfspyfpp gqqlsisedr iewsigleqq spvsvcsesc vpgfrkslqe gkaaccfdcv
      541 pcpeneisng tgkyidqcvk ctedqyantd rtvciqkavt flalesplgm tlasmalcfs
      601 ilssfvlgif vkhqntpvvk annstlsyil lisltfcflc sflfigqpna vtcilqqttf
      661 gvvftvavst vlaktitvil afkstapgrr lrrllisgap kfiipictli qtvlcgiwlg
      721 isppfvdtna hsehghiiim cnkgsviafy cvlgylgvls lvsftvafma rnlpdtfnea
      781 kfltfsmlvf lsvwitflpv yhstkgkimv avevfsilas stgllgcifi pkcyiilarp
      841 dmnsskcqrn rvqwk
//
LOCUS       NP_001108075             793 aa            linear   ROD 03-APR-2025
DEFINITION  protocadherin beta-5 precursor [Rattus norvegicus].
ACCESSION   NP_001108075 NP_001014778 XP_001064875 XP_226045
VERSION     NP_001108075.1
DBSOURCE    REFSEQ: accession NM_001114603.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Wu,Q.
  TITLE     Comparative genomics and diversifying selection of the clustered
            vertebrate protocadherin genes
  JOURNAL   Genetics 169 (4), 2179-2188 (2005)
   PUBMED   15744052
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Zhang,T., Haws,P. and Wu,Q.
  TITLE     Multiple variable first exons: a mechanism for cell- and
            tissue-specific gene regulation
  JOURNAL   Genome Res 14 (1), 79-89 (2004)
   PUBMED   14672974
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Feb 15, 2008 this sequence version replaced
            NP_001014778.1, XP_001064875.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26643289.41242.1,
                                        SRR26643295.56088.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..793
                     /product="protocadherin beta-5 precursor"
                     /note="protocadherin beta-5"
                     /calculated_mol_wt=84362
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2792
     Region          26..108
                     /region_name="Cadherin_2"
                     /note="Cadherin-like; pfam08266"
                     /db_xref="CDD:462413"
     Region          136..234
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(140..141,197,199,230,232..233)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          243..338
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(249..250,303,305,334,336..337)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          350..442
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(353..354,405,407,438,440..441)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          450..552
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(457..458,515,517,548,550..551)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          571..659
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          683..765
                     /region_name="Cadherin_C_2"
                     /note="Cadherin cytoplasmic C-terminal; pfam16492"
                     /db_xref="CDD:465139"
     CDS             1..793
                     /gene="Pcdhb10"
                     /coded_by="NM_001114603.1:167..2548"
                     /db_xref="GeneID:291649"
                     /db_xref="RGD:1308364"
ORIGIN      
        1 metasekrqv vfltillllw ksdaetirys mpeetesgyl vanlakdlgl rvgelatrga
       61 rihhkgnkdl lqldaetgnl ilkekpdrev lcratepcvl hfqiilenpv qffqtelqlt
      121 dindhapefp drkmllkise saqpgtmfpl kaaqdpdigs navqnytvsp nlhfhviths
      181 rtdgrkypel vldraldree qpeltltlia ldggapsrsg tttvhievvd indnppkfdq
      241 slyevqipen splnalvatv sardldagih gtviyslfqg gelsqpfeid evageirlkg
      301 tldfeatpyy nieivatdpg gfsgkcsvai qvvdvndnap kltisslnss ipenapeavv
      361 avfsvsdpds gengrivcsi qnelpfllkp tfenyytlvt erpldresra dynititvsd
      421 lgiprlttqh tiivqvsdin dnapafnqts ytllvrenns palhigtisa tdsdtganah
      481 isylllplyd mqlaltslvs inqengqlfv lraldyetlq tfefsvgatd hgspalssqa
      541 lvrvvvlddn dnapfvlypl qnasvpctel lpraaepgyl vtkvvavdcd sgqnawlsfq
      601 llkatepglf nvwahngevr ttrllserdv pkhklllvvk dngehqrsat vtlhvllvdg
      661 fsqpylplpe vardpvqdde dvltlylvia lasvsslflf svllfigmrl ckrareaslg
      721 vcsvpeghfp ghlvdvsgtg tlsqsyqyev cltgdsgtge fkflkpmisn lmvqdpgrev
      781 kesppcrdsf vfs
//
LOCUS       NP_001178682             419 aa            linear   ROD 03-APR-2025
DEFINITION  ras association domain-containing protein 8 [Rattus norvegicus].
ACCESSION   NP_001178682 XP_232528
VERSION     NP_001178682.1
DBSOURCE    REFSEQ: accession NM_001191753.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Liu,J., Liu,W., Li,H., Deng,Q., Yang,M., Li,X. and Liang,Z.
  TITLE     Identification of key genes and pathways associated with
            cholangiocarcinoma development based on weighted gene correlation
            network analysis
  JOURNAL   PeerJ 7, e7968 (2019)
   PUBMED   31687280
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_232528.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.25854.1,
                                           SRR26643429.18453.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..419
                     /product="ras association domain-containing protein 8"
                     /note="Ras association (RalGDS/AF-6) domain family 8; Ras
                     association (RalGDS/AF-6) domain family (N-terminal)
                     member 8"
                     /calculated_mol_wt=47840
     Region          2..83
                     /region_name="RA_RASSF8"
                     /note="Ras-associating (RA) domain found in N-terminal
                     Ras-association domain family 8 (RASSF8); cd16134"
                     /db_xref="CDD:340551"
     Region          <153..>344
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..419
                     /gene="Rassf8"
                     /gene_synonym="RGD1308820"
                     /coded_by="NM_001191753.1:161..1420"
                     /db_xref="GeneID:312846"
                     /db_xref="RGD:1308820"
ORIGIN      
        1 melkvwvdgv qrivcgvtev ttcqevvial aqaigrtgry tliekwrdte rhlaphenpi
       61 vslnkwgqya sdvqlilrrt gpslserpts dsvaripert lyrqslppla klrpqvdksi
      121 rrrepkrksl tftggakglt difgkgkete frqkvlsncr ataeeltrli rlqtgklqai
      181 ekqlesseae irfweqkysc sleeeivrle qrikrndvei eeeefwenel qieqenekql
      241 qdqleemrqk vadcegrlkd ylaqihtmes glqaeklhre vqeaqvneee vkgkiekvkg
      301 evdlqgqqsl rlengirava rslgqatkrl qdkeqeleql tkelrqvnlq qfiqqtgtkv
      361 tvlpaeptei easqadiete apfpsgslkr pgssrqlpsn lrilqnpvss gfnpegiyv
//
LOCUS       NP_001092977             857 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 50 precursor [Rattus norvegicus].
ACCESSION   NP_001092977 XP_001061646 XP_575663
VERSION     NP_001092977.1
DBSOURCE    REFSEQ: accession NM_001099507.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Ryba,N.J. and Tirindelli,R.
  TITLE     A new multigene family of putative pheromone receptors
  JOURNAL   Neuron 19 (2), 371-379 (1997)
   PUBMED   9292726
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_575663.2, XP_001061646.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..857
                     /product="vomeronasal 2 receptor, 50 precursor"
                     /note="putative pheromone receptor V2R1-1"
                     /calculated_mol_wt=93571
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2848
     Region          43..513
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(79,178..179,404)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(117,120,165,252)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          521..574
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          594..845
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          594..619
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(597,600..601,604..605,607..608,642,646,649..650,658,
                     662)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          631..652
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(651,663..664,667..668,671,751,756,759..760,763,797,
                     800..801,804,808,816..817,820,823,827)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          661..685
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          709..725
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          752..778
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          786..809
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          814..839
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..857
                     /gene="Vom2r50"
                     /coded_by="NM_001099507.1:1..2574"
                     /db_xref="GeneID:500312"
                     /db_xref="RGD:1566165"
ORIGIN      
        1 mkllivliaf sllivlivfq eqiscfsltk paspgyyqdg dfviggifsl rvtagdtrsr
       61 fgfkdtiyip eyvyvdltkh yqhilamvfa iekinkdtni lfnmslgfyl fnvdfidmka
      121 vessmallsg qtppvpnysc rpektdklva viggistgis trisqvlsly nvpqisyapf
      181 dqslgtgvql qspyqfpvyt talyqgiiql llyftwvwvg lvvpddvrge lflrditeem
      241 nnhglcvafa ekvpefpakd tvdrelfmer ftlthvivaf gdtysllrfv ynifcntpfg
      301 nvwittsdwd ittlpfqqnl gytyfgggls fsvhmdeilg fkdflrrvqp rkypqdifiq
      361 dvwsnlfecp yldkdwirel sqceqngnls trplhlwdmn tspssykiha avyaiaqalh
      421 eelslivegd llnkgvprap lpwklhpflq ngqlgrstne etvvnkevsa tkldifnyqs
      481 lqsstkaqvk vgefvfeshs vqhfslndel itwgehhsqt pfavcsqscm lgfrktpveg
      541 kpfccfdclp cpdgeianet dmdqcikcpe dqypnkqrnq clpkitafls hedtlgavfi
      601 slaisfsafs amilglficy rdtpivrann rnlsylllvs lmlcffcsli figqprtvtc
      661 vlrqtifgvv fsiaisaila ktfivvvafk aikpgstlqt wmvtrvsnai vccgssiqvc
      721 icavwlgtyp pfpdvdmqse fgqiilwcne gstlafycvl gylgflasls lliaflarrl
      781 pdtfneakti tfsmlvfcsv wisfvpayls skgknvvave ilailassag llgciflpkc
      841 fvillrsddl prkkffk
//
LOCUS       NP_001178823             397 aa            linear   ROD 03-APR-2025
DEFINITION  serine/threonine-protein kinase 32A [Rattus norvegicus].
ACCESSION   NP_001178823 XP_344678
VERSION     NP_001178823.1
DBSOURCE    REFSEQ: accession NM_001191894.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Jul 17, 2010 this sequence version replaced XP_344678.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1124959.1,
                                           SRR26360172.1588172.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..397
                     /product="serine/threonine-protein kinase 32A"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=46185
     Region          22..281
                     /region_name="STKc_Yank1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Yank1; cd05578"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,100..101,103,107,109,146,148,
                     150..151,153,163..164,167,180..185,215,221,224)
                     /site_type="active"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,101..103,107,146,148,150..151,
                     153,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270730"
     Site            order(33,107,109,146,148,150,167,180..185,215,221,224)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270730"
     Site            order(163..173,177..185)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270730"
     CDS             1..397
                     /gene="Stk32a"
                     /coded_by="NM_001191894.1:244..1437"
                     /db_xref="GeneID:364858"
                     /db_xref="RGD:1308338"
ORIGIN      
        1 mgantsskap vldenedvnf dhfeilraig kgsfgkvciv qkndtkkmya mkymnkqkcv
       61 ernevrnvfk elqimqgleh pflvnlwysf qdeedmfmvv dlllggdlry hlqqnvhfqe
      121 dtvklficel amaldylqsq riihrdmkpd nilldehghv hitdfniaam lpketrittv
      181 agtkpymape mfssrkesgy sfavdwwslg vtayellrgr rpyhirssts skeivnmfet
      241 aivtypsaws aemvsllkkl lepnpdqrfs hltdiqnfpy msdmnwdavl qkrlipgfvp
      301 tkgrlncdpt feleemiles kplhkkkkrl akkekemkkc dspqmcllqe hldavqkefi
      361 ifnrekvkrd fnqrqanial eqtknnteee dgqnnnl
//
LOCUS       NP_001178663             888 aa            linear   ROD 03-APR-2025
DEFINITION  patched domain-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001178663 XP_228985
VERSION     NP_001178663.1
DBSOURCE    REFSEQ: accession NM_001191734.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Tora,D., Gomez,A.M., Michaud,J.F., Yam,P.T., Charron,F. and
            Scheiffele,P.
  TITLE     Cellular Functions of the Autism Risk Factor PTCHD1 in Mice
  JOURNAL   J Neurosci 37 (49), 11993-12005 (2017)
   PUBMED   29118110
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Wells,M.F., Wimmer,R.D., Schmitt,L.I., Feng,G. and Halassa,M.M.
  TITLE     Thalamic reticular impairment underlies attention deficit in
            Ptchd1(Y/-) mice
  JOURNAL   Nature 532 (7597), 58-63 (2016)
   PUBMED   27007844
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Noor,A., Whibley,A., Marshall,C.R., Gianakopoulos,P.J., Piton,A.,
            Carson,A.R., Orlic-Milacic,M., Lionel,A.C., Sato,D., Pinto,D.,
            Drmic,I., Noakes,C., Senman,L., Zhang,X., Mo,R., Gauthier,J.,
            Crosbie,J., Pagnamenta,A.T., Munson,J., Estes,A.M., Fiebig,A.,
            Franke,A., Schreiber,S., Stewart,A.F., Roberts,R., McPherson,R.,
            Guter,S.J., Cook,E.H. Jr., Dawson,G., Schellenberg,G.D.,
            Battaglia,A., Maestrini,E., Jeng,L., Hutchison,T.,
            Rajcan-Separovic,E., Chudley,A.E., Lewis,S.M., Liu,X., Holden,J.J.,
            Fernandez,B., Zwaigenbaum,L., Bryson,S.E., Roberts,W., Szatmari,P.,
            Gallagher,L., Stratton,M.R., Gecz,J., Brady,A.F., Schwartz,C.E.,
            Schachar,R.J., Monaco,A.P., Rouleau,G.A., Hui,C.C., Lucy
            Raymond,F., Scherer,S.W. and Vincent,J.B.
  CONSRTM   Autism Genome Project Consortium
  TITLE     Disruption at the PTCHD1 Locus on Xp22.11 in Autism spectrum
            disorder and intellectual disability
  JOURNAL   Sci Transl Med 2 (49), 49ra68 (2010)
   PUBMED   20844286
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 17, 2010 this sequence version replaced XP_228985.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.31932.1,
                                           SRR26360176.996656.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..888
                     /product="patched domain-containing protein 1"
                     /calculated_mol_wt=101359
     Region          105..851
                     /region_name="Patched"
                     /note="Patched family; pfam02460"
                     /db_xref="CDD:308203"
     CDS             1..888
                     /gene="Ptchd1"
                     /gene_synonym="RGD1564527"
                     /coded_by="NM_001191734.1:10..2676"
                     /db_xref="GeneID:317517"
                     /db_xref="RGD:1564527"
ORIGIN      
        1 mlrqvlhrgl rtcfsrlghf iashpvffas apvlisillg asfsryqvee svehllapqh
       61 slakiernlv nslfpvnrsk hrlysdlqtp grygrvivts yqkanmldqh htdlilklht
      121 avtkiqvprp gfnytfahic vlnndktciv ddivhvleel knaratnrtn faitypithl
      181 kdgravyngh qlggvtvhsk drvksaeaiq ltyylqsins lndmvaerwe ssfcdtvklf
      241 qksnskvkiy pytssslred fqktsrvser ylvtslilvv tmailccsmq dcvrskpwlg
      301 llglvtisla tltaagiinl tggkynstfl gvpfvmlghg lygtfemlss wrktredqhv
      361 kertaevyad smlsfsltta mylvtfgiga spftnieaar ifccnsciai lfnylyvlsf
      421 ygsslvftgy iennyqhsif crkvpkpevl qekpawyrfl ltarfsedta egeeantyes
      481 hllvcflkry ycdwitntyv kpfvvlfyli yisfalmgyl qvsegsdlsn ivatatqtie
      541 yttahqkyfn nyspvigfyi yesieywnss vqedvleytk gfvriswfes ylnylrklnv
      601 stdlpkknft dmlrnsflka pqfshfqedi ifskkyndev dvvasrmflv aktmetnree
      661 lydlletlrr lsvtskvkfi vfnpsfvymd ryasslgapl hnscisalfl lffsaflvad
      721 slinvwitlt vvsvefgvig fmtlwkveld cisvlcliyg inytidncap llstfvlgkd
      781 ftrtkwvkna levhgvailq sylcyivglf plaavpsnlt ctlfrclfli afvtffhcfa
      841 ilpviltflp pskkkrkekk npenreeiec vemldidstr vvdqittv
//
LOCUS       NP_001396168             328 aa            linear   ROD 03-APR-2025
DEFINITION  mas-related G-protein coupled receptor member B8-like [Rattus
            norvegicus].
ACCESSION   NP_001396168 XP_038952137
VERSION     NP_001396168.1
DBSOURCE    REFSEQ: accession NM_001409239.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Jul 12, 2022 this sequence version replaced XP_038952137.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..328
                     /product="mas-related G-protein coupled receptor member
                     B8-like"
                     /note="mas-related G-protein coupled receptor member B8"
                     /calculated_mol_wt=36883
     Region          31..308
                     /region_name="7tmA_MrgprB"
                     /note="mas-related G protein-coupled receptor subtype B,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15107"
                     /db_xref="CDD:320235"
     Region          32..58
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320235"
     Region          64..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320235"
     Site            order(85,88,90,104..109,111..112,115,158,160..164,187,
                     190..192,194..196,198..199,236,239..240,242..243,246,
                     258..259,261..263,266,269..270)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320235"
     Region          104..132
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320235"
     Region          144..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320235"
     Region          187..212
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320235"
     Region          216..246
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320235"
     Region          259..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320235"
     CDS             1..328
                     /gene="LOC100361204"
                     /coded_by="NM_001409239.1:1..987"
                     /db_xref="GeneID:100361204"
                     /db_xref="RGD:2320559"
ORIGIN      
        1 mdssipdpea dliqlngsyh tetspcvies rvmillsiii affglagnam vlwllafrmr
       61 rnvfsvyiln laganflflc thtafsleki ivlfhsvhih ipllfytlst laylagvsmv
      121 taisaeywls giwpywyqgq rlkhtttvic tglwglalll sllegkscgf lgstynqdvc
      181 wkldfiivaw llvlfavlsr siqvllvrif cgsqrtpvtk lhvtivltal vlvicgfpfg
      241 iifyllywtt evyyimpcns fhetilllsy inscanpiic llvgsirhcr fqcgtlrlll
      301 hramqdipee egeeleevvg ervqssip
//
LOCUS       NP_001316812             238 aa            linear   ROD 03-APR-2025
DEFINITION  proteasome 20S subunit beta 6 like 1 [Rattus norvegicus].
ACCESSION   NP_001316812
VERSION     NP_001316812.1
DBSOURCE    REFSEQ: accession NM_001329883.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000325.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BN000325.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..238
                     /product="proteasome 20S subunit beta 6 like 1"
                     /note="proteasome subunit beta type-6; Proteasome subunit
                     beta type-6-like"
                     /calculated_mol_wt=25173
     Region          34..221
                     /region_name="proteasome_beta_type_6"
                     /note="proteasome beta type-6 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03762"
                     /db_xref="CDD:239731"
     Site            order(34,50,52,66,163,200,203..204)
                     /site_type="active"
                     /db_xref="CDD:239731"
     Site            order(52,55,57..62,82,84,99,111,114..115,117..118,121,124,
                     148,150,152..155,158,166..167,169..170,173..175,191,
                     198..201,204..205)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239731"
     CDS             1..238
                     /gene="Psmb6l1"
                     /coded_by="NM_001329883.1:1..717"
                     /db_xref="GeneID:100360846"
                     /db_xref="RGD:2321312"
ORIGIN      
        1 maaalavrga isapafgpea ltpdwenrev stgttimavq fdggvvlgad srtttgsyia
       61 nrvtdkltpi hdhifccrsg saadtqavad avtyqlgfhs ielnepplvh taaslfkemc
      121 yryredlmag iiiagwdpqe ggqvysvpmg gmmvrqsfai ggsgssyiyg yvdatyregm
      181 tkdeclqfta nalalamerd gssggvirla aiqqsgverq vllgdqipkv tistlppp
//
LOCUS       NP_001092975             863 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 76 precursor [Rattus norvegicus].
ACCESSION   NP_001092975 XP_001058271 XP_236825
VERSION     NP_001092975.1
DBSOURCE    REFSEQ: accession NM_001099505.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000009.1.
            
            On or before Aug 17, 2007 this sequence version replaced
            XP_001058271.1, XP_236825.4.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..863
                     /product="vomeronasal 2 receptor, 76 precursor"
                     /calculated_mol_wt=96379
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2368
     Region          42..507
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(75,172..173,397)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(113,116,159,246)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          515..567
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          588..839
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          588..613
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(591,594..595,598..599,601..602,636,640,643..644,652,
                     656)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          625..646
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(645,657..658,661..662,665,745,750,753..754,757,791,
                     794..795,798,802,810..811,814,817,821)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          655..679
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          703..719
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          746..772
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          780..803
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          808..833
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..863
                     /gene="Vom2r76"
                     /coded_by="NM_001099505.1:1..2592"
                     /db_xref="GeneID:301154"
                     /db_xref="RGD:1588569"
ORIGIN      
        1 mqsswlyicc cflqmptlls tieipscipk tktllyhdgs mvisaffpif yfypqsetew
       61 ktsfdtgnmf smdernyqlv lamlfaihei nwnsyilpnt slgleiynll hfernilrnv
      121 fhwltglsms ipnyncrker dsaavltgis rktseliatv ldlykfpqit fgpfdhvltd
      181 rnqfpslyqv apndisvfyg iaslmlhfnw twvglfttdd hggaqflsdl kkeldenric
      241 iafvetvsfv gesvynilnd nqelnlqssa nviiiygeia filtviesrh rkhilkkvwv
      301 mnskwsgqkf evyemldlsh gtltfsphhe eifgftnfiq qatpikyped iclhilwkry
      361 fncsllhsnc kifdnclpna slellpgnif emgmteesyn vynavyavah slhdmilnqv
      421 qfhpqskkdr imllpwqlhp flkniqvkns vddhvvldwk rktdpeydin nlwnfptgls
      481 lfvkvgtfsp rapkrqqlsi sefmiewpia fteipqsvcs esctpgfrkv ileskpaccf
      541 dctpcpenei snetgmdqcf kcpethytsa ekkhclkktv tflayddplg kgltfvslgf
      601 saltifvigt fvnhrdtpiv kannrtlsyi llvtltlcfl cpllfiglpn tatcilqqnv
      661 fgilftvals tvlaktttvv iafkitapgr kerwllisqa pnfiipvctl iqvllsgiwl
      721 gtsppfvdmd ahsehgyiii lcnkgstfaf yctlaylgvm afgsylmafl srnlpdtfne
      781 akflsfsmlv fccvwvtflp vyhsttgkfm vamevfsila ssasilslif apkcyiilfr
      841 perntfhfir dkrqnrcknl ikt
//
LOCUS       NP_001178635             401 aa            linear   ROD 03-APR-2025
DEFINITION  arylacetamide deacetylase-like 2 [Rattus norvegicus].
ACCESSION   NP_001178635 XP_227188
VERSION     NP_001178635.1
DBSOURCE    REFSEQ: accession NM_001191706.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_227188.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.8897.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..401
                     /product="arylacetamide deacetylase-like 2"
                     /calculated_mol_wt=45436
     Region          107..372
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
     CDS             1..401
                     /gene="Aadacl2"
                     /gene_synonym="RGD1563197"
                     /coded_by="NM_001191706.1:1..1206"
                     /db_xref="GeneID:295076"
                     /db_xref="RGD:1563197"
ORIGIN      
        1 mgfkalcvgl lcvsflsyiy tpmpdnieep wklialdava ktfsltalcl enigvmryee
       61 fismiinldy tqphsdehit vtdtafvdip vrlylpksks eaprraviyf hgggfcfgsf
      121 kqrafdflnr wtaskldavv vgvdyrlapq hhfpaqfedg vtavkfflqd kmltkygvdp
      181 triaisgdss ggtlaaavtq qvqidpevkh kfklqallyp glqvidthlp shlenergiv
      241 ltrdiaiklv slfftkdeal qwamrknqhm pleskhlfrf vnwsallpdk frknyvytep
      301 vlgrsafslp almdhralpl landahlqhl pqtyiltcqy dvlrddgimy asrlqsvgve
      361 vyhdhvedgi hgalsymtsp lhlnlglrir dmyvswldkn l
//
LOCUS       NP_001092983             852 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 64 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001092983 XP_001060234
VERSION     NP_001092983.3
DBSOURCE    REFSEQ: accession NM_001099513.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 1, 2024 this sequence version replaced NP_001092983.2.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..852
                     /product="vomeronasal 2 receptor, 64 isoform 2"
                     /calculated_mol_wt=95821
     Region          40..503
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(71,168..169,393)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(109,112,155,242)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..564
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          584..834
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          584..609
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(587,590..591,594..595,597..598,632,636,639..640,648,
                     652)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          621..642
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(641,653..654,657..658,661,741,746,749..750,753,787,
                     790..791,794,798,806..807,810,813,817)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          651..675
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          699..715
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          742..768
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          776..799
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          804..829
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..852
                     /gene="Vom2r64"
                     /coded_by="NM_001099513.3:1..2559"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:681079"
                     /db_xref="RGD:1584665"
ORIGIN      
        1 mptwifffft lklpmllckl fthecfvsfi dnvyqdgdmv isaflplyty qtsqhtegae
       61 nkdvsariap qnyqfvmali faieeinrnp illpnmtlgy nihsagaigs etvvsflkwl
      121 tgqdrlipny tcktkeksva aitgttweis sligiflsly kypqlsigpf eqsmnnseef
      181 pflyqmaake sslalgmvsl fvhfkwnwvg lvisedengv nfvtdlipqm erntvcvafm
      241 efipvthmmd lentyeypir imrnpakvvi iyantdsslg vlfrrweyil lwriwvttsq
      301 wevvtsmrhl ildsfhgtli fskrqgdist fkefvksvrp skypddifla rlweiyfgca
      361 isnatckslk ncssrgnlgl lpwylfdiav stgsyhvyna vyavahtmhk mliqeidieg
      421 mknggsmdfp plklnsllkn ikfmnpggdp islnpseslh idydilnfwd fpqgltykvk
      481 vgtfspyfpp gqqlsisedr iewsigveqq ipvsvcseic gpgfrkslqe gkaaccfdcv
      541 lcseneisng tgkccvkcte dqyantdrtv ciqkavtfla lenplgmtla smalcfsilt
      601 sfvlgifvkh qntpvvkann rtlsyillis ltfcflcsfl figqpnavtc ilqqttfgvv
      661 ftvavstvla ktitvilafk stapgrrlrw llisgapkfi ipictliqtv fcgvwlrisp
      721 pfvdtdaqse hghiiimcnk gsvtafycvl gylgalslvs ftvafmarnl pdafneakfl
      781 tfsmlvflsv wvtflpvyhs tkgkimvave vfsilasstg llgcifipkc yiilarpemn
      841 slkcrrnrvq wk
//
LOCUS       NP_001160233             321 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 1 receptor 104 [Rattus norvegicus].
ACCESSION   NP_001160233 XP_001076115
VERSION     NP_001160233.1
DBSOURCE    REFSEQ: accession NM_001166761.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     PROVISIONAL REFSEQ: This record is based on preliminary annotation
            provided by NCBI staff in collaboration with Janet Young. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On Feb 3, 2010 this sequence version replaced XP_001076115.1.
            
            Sequence Note: A set of diverse V1R queries was aligned via BLAST
            to the RGSCv3.4 assembly to find candidate V1R-containing genomic
            regions. Open reading frames (ORFs) for V1R genes and pseudogenes
            were then identified.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..321
                     /product="vomeronasal 1 receptor 104"
                     /note="vomernasal 1 receptor Vom1r104; vomeronasal 1
                     receptor, A1"
                     /calculated_mol_wt=36792
     Region          27..315
                     /region_name="7tm_V1R_pheromone"
                     /note="vomeronasal organ pheromone receptor type-1 family,
                     member of the seven-transmembrane G protein-coupled
                     receptor superfamily; cd13949"
                     /db_xref="CDD:320087"
     Region          28..53
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320087"
     Region          97..119
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320087"
     Region          145..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320087"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320087"
     Region          245..270
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320087"
     Region          280..305
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320087"
     CDS             1..321
                     /gene="Vom1r104"
                     /gene_synonym="V1ra1"
                     /coded_by="NM_001166761.1:1..966"
                     /db_xref="GeneID:685945"
                     /db_xref="RGD:1587829"
ORIGIN      
        1 mseflffslq plfsymmnkn irlhtnsnir ntffseigig isgnsllllf hiikfihgqr
       61 srltdlpigl llmllmvafi atdifisqre wddiickflv ylyrifrgls lcttcmlsvl
      121 qaiilsprss clakfkhksp yyvscamlfl salymiissh llvsiiatpn lttnelmhvt
      181 qscsilpvsy lmqsmfsilv airdiflisl mvfstwymva llcrhrkqtq hlqgtslspk
      241 gspeqratrs ilmlmsffvl msifdsivsc srtmflndpt syniqifvmh iyatvspfvf
      301 msiekhivnf frsmcvrvmn v
//
LOCUS       NP_001178898             521 aa            linear   ROD 03-APR-2025
DEFINITION  hyccin [Rattus norvegicus].
ACCESSION   NP_001178898 XP_575330
VERSION     NP_001178898.1
DBSOURCE    REFSEQ: accession NM_001191969.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Baskin,J.M., Wu,X., Christiano,R., Oh,M.S., Schauder,C.M.,
            Gazzerro,E., Messa,M., Baldassari,S., Assereto,S., Biancheri,R.,
            Zara,F., Minetti,C., Raimondi,A., Simons,M., Walther,T.C.,
            Reinisch,K.M. and De Camilli,P.
  TITLE     The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P
            synthesis at the plasma membrane
  JOURNAL   Nat Cell Biol 18 (1), 132-138 (2016)
   PUBMED   26571211
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Gazzerro,E., Baldassari,S., Giacomini,C., Musante,V., Fruscione,F.,
            La Padula,V., Biancheri,R., Scarfi,S., Prada,V., Sotgia,F.,
            Duncan,I.D., Zara,F., Werner,H.B., Lisanti,M.P., Nobbio,L.,
            Corradi,A. and Minetti,C.
  TITLE     Hyccin, the molecule mutated in the leukodystrophy hypomyelination
            and congenital cataract (HCC), is a neuronal protein
  JOURNAL   PLoS One 7 (3), e32180 (2012)
   PUBMED   22461884
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_575330.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.17930.1,
                                           SRR26643298.21290.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..521
                     /product="hyccin"
                     /note="down-regulated by Ctnnb1, A; family with sequence
                     similarity 126, member A"
                     /calculated_mol_wt=57024
     Region          22..330
                     /region_name="Hyccin"
                     /note="pfam09790"
                     /db_xref="CDD:462903"
     CDS             1..521
                     /gene="Hycc1"
                     /gene_synonym="Drctnnb1a; Fam126a; RGD1562906"
                     /coded_by="NM_001191969.1:233..1798"
                     /db_xref="GeneID:499975"
                     /db_xref="RGD:1562906"
ORIGIN      
        1 mftseigvve ewlsefktlp etslpnyatn lkdksslvss lykviqepqs ellepvchql
       61 fefyrsgeeq llrftlqflp eliwcylavs asrnvhssgc iealllgvyn leivdkhghs
      121 kvlsftipsl skpsvyheps sigsmaltes alsqhglskv vysgphpqre mltaqnrfev
      181 ltflllcyna altympsvsl qslcqicsri cvcgyprqhv rkyggassri pissgfmvqm
      241 ltgvyfaiyn gewdlaqkal ddiiyraqle lypepllvan aikaslppga mksskegtrc
      301 iqveitptss risrnavtsm sirghrwkrh gdteltgqee lteitevdeg fysraassts
      361 qsglsisshn cshktsvgkn qrrsggskag akeretages crdhfarkqt qraqsenlel
      421 lslkrltlts sqslpkpssh glaqtaatvf sksfeqvsgv pgprspspai gcvagadahr
      481 fsacslqeek liygseridl plkcqagqrg ppsvsitlsa d
//
LOCUS       NP_001178722             315 aa            linear   ROD 03-APR-2025
DEFINITION  PIH1 domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001178722 XP_236221
VERSION     NP_001178722.1
DBSOURCE    REFSEQ: accession NM_001191793.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Simicek,M., Lievens,S., Laga,M., Guzenko,D., Aushev,V.N., Kalev,P.,
            Baietti,M.F., Strelkov,S.V., Gevaert,K., Tavernier,J. and
            Sablina,A.A.
  TITLE     The deubiquitylase USP33 discriminates between RALB functions in
            autophagy and innate immune response
  JOURNAL   Nat Cell Biol 15 (10), 1220-1230 (2013)
   PUBMED   24056301
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_236221.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.45116.1,
                                           SRR26643295.31614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..315
                     /product="PIH1 domain-containing protein 2"
                     /calculated_mol_wt=35705
     Region          25..168
                     /region_name="alpha-crystallin domain (ACD) found in
                     alpha-crystallin-type small heat shock proteins, and a
                     similar domain found in p23 (a cochaperone for Hsp90) and
                     in other p23-like proteins."
                     /note="The alpha-crystallin-Hsps_p23-like superfamily
                     includes the alpha-crystallin domain (ACD) of
                     alpha-crystallin-type small heat shock proteins (sHsps)
                     and a similar domain found in p23-like proteins. sHsps are
                     small stress induced proteins with monomeric...; cl00175"
                     /db_xref="CDD:469641"
     Region          <246..313
                     /region_name="PIH1_CS"
                     /note="PIH1 CS-like domain; pfam18201"
                     /db_xref="CDD:408028"
     CDS             1..315
                     /gene="Pih1d2"
                     /gene_synonym="RGD1310503"
                     /coded_by="NM_001191793.1:357..1304"
                     /db_xref="GeneID:315645"
                     /db_xref="RGD:1310503"
ORIGIN      
        1 mkasskgllt hisqfwsmld dlaendpery rnfiqqelkd gkqlcadpep qlclqtkilk
       61 pkekvlfinl cqweripapq sathpvpisv grpedfpets dactiidvay npgvlqaaek
      121 dqgikdqlir mamrcieerl qltlahsyhv thfrvkgsiq rmkerlmgik thfpnfkemm
      181 rkdntlerir sstvsepshl pevlltkkqv sakgrcliee iassevqvea ktpayelkvv
      241 kdqnekplki elkvelpgik avslcelsvs evdllievse myrlclnlpe sintemttak
      301 fiknksilii tmpla
//
LOCUS       NP_001397193             304 aa            linear   ROD 03-APR-2025
DEFINITION  RT1 class I, locus T24, gene 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001397193
VERSION     NP_001397193.1
DBSOURCE    REFSEQ: accession NM_001410264.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Brorson,K.A., Hunt,S.W. 3rd, Hunkapiller,T., Sun,Y.H.,
            Cheroutre,H., Nickerson,D.A. and Hood,L.
  TITLE     Comparison of exon 5 sequences from 35 class I genes of the BALB/c
            mouse
  JOURNAL   J Exp Med 170 (6), 1837-1858 (1989)
   PUBMED   2584927
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CM038666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR8487230.59626.1,
                                           SRR8487227.221037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="SHRSP/BbbUtx"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..304
                     /product="RT1 class I, locus T24, gene 1 isoform 2"
                     /note="histocompatibility 2, T region locus 24"
                     /calculated_mol_wt=34288
     Region          19..>106
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          117..208
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          118..125
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          133..142
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(136,138,165..166,168..170,176,178)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(143..145,173,198)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          147..152
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          155..158
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          162..170
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          173..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          190..197
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          204..207
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..304
                     /gene="RT1-T24-1"
                     /gene_synonym="H2-T24"
                     /coded_by="NM_001410264.1:47..961"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361787"
                     /db_xref="RGD:1359499"
ORIGIN      
        1 mwslifcfls hpqdtgarsh slhysysavt epgpgvpaff asgfvdnqpf ihydsrkmea
       61 epcadwlren pyyfdeetqv ftnrmkifql slrniqqyyn ssgdrsqrad gfhqqadppq
      121 ttvthhprpe gdvtlrcwal gfypaditlt wqlngedltq dmelvetrpt gdgtfqkwaa
      181 vvvplgkeqk ytchvehegl pepltqrwea ppgtdsnmgi nviavvlqav aiiaavaiii
      241 vtvvrrrrrr rrntggegdy tpaprslsif iqpapqarrs wltqqawlaw kshastpiit
      301 plpa
//
LOCUS       NP_001316819             407 aa            linear   ROD 03-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001316819 XP_006223494 XP_006229965
VERSION     NP_001316819.1
DBSOURCE    REFSEQ: accession NM_001329890.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC169022.1.
            
            On or before Aug 4, 2016 this sequence version replaced
            XP_006229965.1, XP_006223494.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..407
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 1"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=44228
     Region          1..150
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..407
                     /gene="Xndc1"
                     /coded_by="NM_001329890.1:415..1638"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 mapvkishvv sfssqdpkyp venllnpdsh kgpwlscprd ktgqlkvefq leravpisyi
       61 dvgncgcafl qidvgrsswp ldrpfvtllp atmlmsltds kegknrsgvr mfkdddflip
      121 asgeswdrlr ltcsqpftrh qsfglaflrv rssldslsdp vkdpsspgss glnqnssdkl
      181 esdpspwltn psirrtffpd pqtstkeisa lkgmlkqlqp gplgraarmv lsaahkappa
      241 svvspnnshg epdsshpera epraeepnrk nnasrgkrrk vqeqrrplss sssqpnrrat
      301 grtkqrqqrp qaksdgsgvq atgqcpictg sfsiealprh aatcgesspp qpasptslss
      361 sesvlwvssp esspppsswv qcpicelqfs areieehasv cgevfpa
//
LOCUS       NP_001178730             855 aa            linear   ROD 03-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM71 [Rattus norvegicus].
ACCESSION   NP_001178730 XP_236676
VERSION     NP_001178730.1
DBSOURCE    REFSEQ: accession NM_001191801.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Loedige,I., Gaidatzis,D., Sack,R., Meister,G. and Filipowicz,W.
  TITLE     The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
            function
  JOURNAL   Nucleic Acids Res 41 (1), 518-532 (2013)
   PUBMED   23125361
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Chang,H.M., Martinez,N.J., Thornton,J.E., Hagan,J.P., Nguyen,K.D.
            and Gregory,R.I.
  TITLE     Trim71 cooperates with microRNAs to repress Cdkn1a expression and
            promote embryonic stem cell proliferation
  JOURNAL   Nat Commun 3, 923 (2012)
   PUBMED   22735451
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Chen,J., Lai,F. and Niswander,L.
  TITLE     The ubiquitin ligase mLin41 temporally promotes neural progenitor
            cell maintenance through FGF signaling
  JOURNAL   Genes Dev 26 (8), 803-815 (2012)
   PUBMED   22508726
  REMARK    Erratum:[Genes Dev. 2012 Jun 15;26(12):1392]
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Rybak,A., Fuchs,H., Hadian,K., Smirnova,L., Wulczyn,E.A.,
            Michel,G., Nitsch,R., Krappmann,D. and Wulczyn,F.G.
  TITLE     The let-7 target gene mouse lin-41 is a stem cell specific E3
            ubiquitin ligase for the miRNA pathway protein Ago2
  JOURNAL   Nat Cell Biol 11 (12), 1411-1420 (2009)
   PUBMED   19898466
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Maller Schulman,B.R., Liang,X., Stahlhut,C., DelConte,C.,
            Stefani,G. and Slack,F.J.
  TITLE     The let-7 microRNA target gene, Mlin41/Trim71 is required for mouse
            embryonic survival and neural tube closure
  JOURNAL   Cell Cycle 7 (24), 3935-3942 (2008)
   PUBMED   19098426
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Rybak,A., Fuchs,H., Smirnova,L., Brandt,C., Pohl,E.E., Nitsch,R.
            and Wulczyn,F.G.
  TITLE     A feedback loop comprising lin-28 and let-7 controls pre-let-7
            maturation during neural stem-cell commitment
  JOURNAL   Nat Cell Biol 10 (8), 987-993 (2008)
   PUBMED   18604195
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_236676.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..855
                     /product="E3 ubiquitin-protein ligase TRIM71"
                     /EC_number="2.3.2.27"
                     /note="Drosophila dappled/ vertebrate TRipartite Motif
                     protein related; B-box zinc finger, Filamin and NHL repeat
                     containing protein (123.8 kD) (lin-41); tripartite
                     motif-containing protein 71; protein lin-41 homolog;
                     tripartite motif containing 71, E3 ubiquitin protein
                     ligase; RING-type E3 ubiquitin transferase TRIM71"
                     /calculated_mol_wt=91995
     Region          1..101
                     /region_name="RING-HC_TRIM71_C-VII"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 71 (TRIM71) and similar proteins;
                     cd16589"
                     /db_xref="CDD:438251"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q2Q1W2; propagated from
                     UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          26..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          126..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          185..227
                     /region_name="Bbox1_TRIM71_C-VII"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 71 (TRIM71) and similar proteins;
                     cd19812"
                     /db_xref="CDD:380870"
     Region          264..309
                     /region_name="Bbox2_TRIM71_C-VII"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 71 (TRIM71) and similar proteins;
                     cd19796"
                     /db_xref="CDD:380854"
     Region          301..431
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Site            order(315..316,318..320,323,326,340..341,344,347..348,
                     351..352,355,362..363,366,369..370,373..374,377,387..388,
                     391,395,398..399,402..403,405..406,414,417..418,421,
                     424..425)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467844"
     Region          466..567
                     /region_name="Filamin"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          469..564
                     /region_name="Filamin"
                     /note="Filamin/ABP280 repeat; pfam00630"
                     /db_xref="CDD:395505"
     Region          571..855
                     /region_name="NHL_TRIM71_like"
                     /note="NHL repeat domain of the tripartite
                     motif-containing protein 71 (TRIM71) and related proteins;
                     cd14954"
                     /db_xref="CDD:271324"
     Region          580..623
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          596..635
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          627..670
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          643..682
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          674..717
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          690..726
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          691..727
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          721..764
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          734..774
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          768..811
                     /region_name="NHL 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          782..821
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          783..813
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          815..855
                     /region_name="NHL 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVM4.1)"
     Region          829..855
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271324"
     Region          831..855
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..855
                     /gene="Trim71"
                     /gene_synonym="RGD1566388"
                     /coded_by="NM_001191801.1:1..2568"
                     /db_xref="GeneID:301042"
                     /db_xref="RGD:1566388"
ORIGIN      
        1 masfpetdfq icllckemcg spaplsssss asssssqtst ssaggggpga aarrlhvlpc
       61 lhafcrpcle ahrlpapgga gpaealklrc pvcdqkvvla eaagmdalps safllsnlld
      121 avvatadepp pkngragggp ggagghsnhr hhahhpaqra aapapqpppg paaspgslll
      181 rrphgcsscd egnaassrcl dcqehlcdnc vrahqrvrlt kdhyiergpp gpaaasaaqq
      241 lglgppfaga pfsilsvfpe rlgfcqhhdd evlhlycdtc svpicrectl grhgghsfay
      301 lqdalqdsra ltiqlladaq qgrqaiqlsi eqaqtvaeqv emkakvvqse vkavtarhkk
      361 aleerecell wkvekirqvk akslylqvek lrqnlnkles tisavqqvle egraldilla
      421 rdrmlaqvqe lktirgllqp qeddrvmftp pdqalylalk sfgfvssgaf apltkaagdg
      481 ikralqgkva sftvmgydhn geprlsggdl msvvvlgpdg nlfgaevsdq qngtyvvsyr
      541 pqlegehlvs vtlynqhien spfkvvvksg rsyvgiglpv lsfgsegdge gklcrpwgvs
      601 vdkegyiiva drsnnriqvf kpcgsfhhkf gtlgsrpgqf drpagvacda srrivvadkd
      661 nhriqiftfe gqfllkfgek gtkngqfnyp wdvavnsegk ilvsdtrnhr iqlfgpdgvf
      721 lnkygfegsl wkhfdsprgv afnheghlvv tdfnnhrllv ihpdcqsarf lgsegtgngq
      781 flrpqgvavd qegriivads rnhrvqmfea ngsflckfga qgsgfgqmdr psgiavtpeg
      841 livvvdfgnn rilif
//
LOCUS       NP_001178849             572 aa            linear   ROD 03-APR-2025
DEFINITION  multidrug and toxin extrusion protein 2 [Rattus norvegicus].
ACCESSION   NP_001178849 XP_573107
VERSION     NP_001178849.1
DBSOURCE    REFSEQ: accession NM_001191920.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Gong,L., Goswami,S., Giacomini,K.M., Altman,R.B. and Klein,T.E.
  TITLE     Metformin pathways: pharmacokinetics and pharmacodynamics
  JOURNAL   Pharmacogenet Genomics 22 (11), 820-827 (2012)
   PUBMED   22722338
  REMARK    Review article
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000010.1.
            
            On Jul 17, 2010 this sequence version replaced XP_573107.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.37006.1,
                                           SRR26643293.63193.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..572
                     /product="multidrug and toxin extrusion protein 2"
                     /note="solute carrier family 47 (multidrug and toxin
                     extrusion), member 2"
                     /calculated_mol_wt=61406
     Region          51..476
                     /region_name="MATE_eukaryotic"
                     /note="Eukaryotic members of the multidrug and toxic
                     compound extrusion (MATE) family; cd13132"
                     /db_xref="CDD:240537"
     Site            order(281,285,311,314,393,397,424,450,454)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:240537"
     CDS             1..572
                     /gene="Slc47a2"
                     /gene_synonym="RGD1562382"
                     /coded_by="NM_001191920.1:1..1719"
                     /db_xref="GeneID:497921"
                     /db_xref="RGD:1562382"
ORIGIN      
        1 mepaedslga aiqppelapv perslrillg lrealssdvr qeaaalaala gpvflaqlmi
       61 flisivssif cghlgkveld avtlavsvvn vtgisvgtgl asacdtlmsq sfggknlkrv
      121 gvilqrgili lllccfpcwa iflnterlll flrqdpevar laqvyvmici palpaaflfq
      181 lqtrylqsqg iimpqvivgi aanvvnvgmn afllyaldlg vvgsawantt sqfflsallf
      241 lyvwwkgihi htwggwtrec fqewssytrl aipsmfmvci ewwtfeigtf laglvnvtel
      301 gaqaviyela svaymvpfgf gvaasvrvgn algagnadqa rcscttvllc tgvcallvgi
      361 llaalkdvva yvftndkdii slvsqvmpif apfhlfdala gtcggvlrgt gkqkigavln
      421 aigyygfgfp igvslmfaak lgiiglwagl ivcvffqals yliyilrtnw nrvaeqaqvr
      481 aglksnkemi ptpadlpile revidgvilp diirpesqtg qlvveensqc vvptvgevlt
      541 grqlvvyrgt alivsiavli agivvrvind rg
//
LOCUS       NP_001129189             533 aa            linear   ROD 03-APR-2025
DEFINITION  probable RNA-binding protein 46 [Rattus norvegicus].
ACCESSION   NP_001129189 XP_227311
VERSION     NP_001129189.1
DBSOURCE    REFSEQ: accession NM_001135717.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Wang,C., Chen,Y., Deng,H., Gao,S. and Li,L.
  TITLE     Rbm46 regulates trophectoderm differentiation by stabilizing Cdx2
            mRNA in early mouse embryos
  JOURNAL   Stem Cells Dev 24 (7), 904-915 (2015)
   PUBMED   25397698
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Oct 8, 2008 this sequence version replaced XP_227311.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.12641.1,
                                           SRR26360181.1621883.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..533
                     /product="probable RNA-binding protein 46"
                     /calculated_mol_wt=59995
     Region          18..464
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     CDS             1..533
                     /gene="Rbm46"
                     /gene_synonym="RGD1560205"
                     /coded_by="NM_001135717.1:187..1788"
                     /db_xref="GeneID:310548"
                     /db_xref="RGD:1560205"
ORIGIN      
        1 mneentdgtn gcskvrtgtq neaallalme ktgynmvqen gqrkfggppp gwegpppprg
       61 cevfvgkipr dmyedelvpv feragkiyef rlmmefsgen rgyafvmytt keeaqlairi
      121 lnnyeirpgk figvcvsldn crlfigaipk ekkkeeilde mkkvtegvvd vivypsatdk
      181 tknrgfafve yeshraaama rrklipgtfq lwghtiqvdw adpekevdee tmqrvkvlyv
      241 rnlmisttee tikaefnkfk pgavervkkl rdyafvhffn redavaamsv mngkcidgas
      301 ievtlakpvn kentwrqhln gqispnsenl lvyankeesh skslgkpptl ptrlngqhsp
      361 sppeiercty pffpgtkltp ismyslksnh fnsavmhldy ycnknnwapp eyylysttsq
      421 dgkvllvyki vipaiangsq syfmpdklct tledakelaa qftllhldyn frrssinsls
      481 pvsatlstgt psvlpytsrp ysypsyplsp tislangshv gqrlyisnqa sff
//
LOCUS       NP_001092940             864 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 11 [Rattus norvegicus].
ACCESSION   NP_001092940 XP_001058654 XP_218020
VERSION     NP_001092940.1
DBSOURCE    REFSEQ: accession NM_001099470.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On or before Aug 19, 2007 this sequence version replaced
            XP_218020.3, XP_001058654.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..864
                     /product="vomeronasal 2 receptor 11"
                     /calculated_mol_wt=99613
     Region          42..503
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(79,177..178,402)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(117,120,164,251)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          511..564
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          584..835
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          584..609
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(587,590..591,594..595,597..598,632,636,639..640,648,
                     652)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          621..642
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(641,653..654,657..658,661,741,746,749..750,753,787,
                     790..791,794,798,806..807,810,813,817)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          651..675
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          699..715
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          742..768
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          776..799
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          804..829
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..864
                     /gene="Vom2r11"
                     /gene_synonym="RGD1563778"
                     /coded_by="NM_001099470.1:1..2595"
                     /db_xref="GeneID:292417"
                     /db_xref="RGD:1563778"
ORIGIN      
        1 mkmfswifit sflqtpylvf tfnlsicyyl itedfhhegd lmigaffpvh tyytvnkipn
       61 vqfpniyyyq dyylqfnfkn yqyvlalefa ieeinrnpnl lpnltlgfdf ynvkfteket
      121 lmnvcmwlta hkrgkvlpny nceeknftaa ftgtswttsa higtllqlfr fpqlsigpyd
      181 talndhgqys slyqmatkdt slshgivslm lyfrwswvgl llpddhkgnk vlsefrdeme
      241 rervciafvk mipttwtlyf nkqwknmeei eesstnviii ygdvdslqgl mrnigqrllt
      301 gkvwvmnfeq ditdhadyfl ldsfhgsfif tqhygesfef tkfiqtvnpy kypediylpk
      361 mwhyffkcsy sevdcklldn cqanatlnvl prhifdvsms kesyniynav yavahslhei
      421 tlkqvqmqpc kngeellfyp wqinsflrkn mgldwrqkrn eeydilnlwn fpkglglkik
      481 igkysenapd gqqltlsdqm iqwpekfsei pqsvcsescg pgfrkvtleg qavccynctp
      541 caeneisnet dvdhcvkcpe syyanteknh clqkaqsfla yedplgmalt sisllfsalt
      601 vivvgifvrh rhtpmvkann ralsytllis lnfcflcsln figqpntatc ilqqtifgva
      661 ftvalatvla kaitvviafk atfpgriirw lmisrapnyt ipictliqlv lcgiwmatfp
      721 pfvdqddhte hghviifcnk gssvafhcal gylcflalgs yamaffsrnl pdtfneskfl
      781 sfsmlvffcv witflpvyhs tkgkimlame vfcilassaa llgfiftpkc yiillrpekn
      841 sfhrirnkih skgnvsqtiv qkpi
//
LOCUS       NP_001178761            1234 aa            linear   ROD 03-APR-2025
DEFINITION  retinol-binding protein 3 precursor [Rattus norvegicus].
ACCESSION   NP_001178761 XP_341401
VERSION     NP_001178761.1
DBSOURCE    REFSEQ: accession NM_001191832.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1234)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   2  (residues 1 to 1234)
  AUTHORS   Daiger,S.P., Sullivan,L.S. and Bowne,S.J.
  TITLE     Genes and mutations causing retinitis pigmentosa
  JOURNAL   Clin Genet 84 (2), 132-141 (2013)
   PUBMED   23701314
  REMARK    Review article
REFERENCE   3  (residues 1 to 1234)
  AUTHORS   Li,S., Yang,Z., Hu,J., Gordon,W.C., Bazan,N.G., Haas,A.L., Bok,D.
            and Jin,M.
  TITLE     Secretory defect and cytotoxicity: the potential disease mechanisms
            for the retinitis pigmentosa (RP)-associated interphotoreceptor
            retinoid-binding protein (IRBP)
  JOURNAL   J Biol Chem 288 (16), 11395-11406 (2013)
   PUBMED   23486466
REFERENCE   4  (residues 1 to 1234)
  AUTHORS   Garlipp,M.A., Nowak,K.R. and Gonzalez-Fernandez,F.
  TITLE     Cone outer segment extracellular matrix as binding domain for
            interphotoreceptor retinoid-binding protein
  JOURNAL   J Comp Neurol 520 (4), 756-769 (2012)
   PUBMED   21935947
REFERENCE   5  (residues 1 to 1234)
  AUTHORS   Kiser,P.D., Golczak,M., Maeda,A. and Palczewski,K.
  TITLE     Key enzymes of the retinoid (visual) cycle in vertebrate retina
  JOURNAL   Biochim Biophys Acta 1821 (1), 137-151 (2012)
   PUBMED   21447403
  REMARK    Review article
REFERENCE   6  (residues 1 to 1234)
  AUTHORS   Suzuki,H., Tsuchiya,K. and Takezaki,N.
  TITLE     A molecular phylogenetic framework for the Ryukyu endemic rodents
            Tokudaia osimensis and Diplothrix legata
  JOURNAL   Mol Phylogenet Evol 15 (1), 15-24 (2000)
   PUBMED   10764531
REFERENCE   7  (residues 1 to 1234)
  AUTHORS   Serizawa,K., Suzuki,H. and Tsuchiya,K.
  TITLE     A phylogenetic view on species radiation in Apodemus inferred from
            variation of nuclear and mitochondrial genes
  JOURNAL   Biochem Genet 38 (1-2), 27-40 (2000)
   PUBMED   10862357
REFERENCE   8  (residues 1 to 1234)
  AUTHORS   Katz,M.L., Gao,C.L. and Stientjes,H.J.
  TITLE     Regulation of the interphotoreceptor retinoid-binding protein
            content of the retina by vitamin A
  JOURNAL   Exp Eye Res 57 (4), 393-401 (1993)
   PUBMED   8282025
REFERENCE   9  (residues 1 to 1234)
  AUTHORS   Gonzalez-Fernandez,F., Van Niel,E., Edmonds,C., Beaver,H.,
            Nickerson,J.M., Garcia-Fernandez,J.M., Campohiaro,P.A. and
            Foster,R.G.
  TITLE     Differential expression of interphotoreceptor retinoid-binding
            protein, opsin, cellular retinaldehyde-binding protein, and basic
            fibroblastic growth factor
  JOURNAL   Exp Eye Res 56 (4), 411-427 (1993)
   PUBMED   7916695
  REMARK    Erratum:[Exp Eye Res 1993 Jul;57(1):127]
REFERENCE   10 (residues 1 to 1234)
  AUTHORS   Gonzalez-Fernandez,F. and Healy,J.I.
  TITLE     Early expression of the gene for interphotoreceptor retinol-binding
            protein during photoreceptor differentiation suggests a critical
            role for the interphotoreceptor matrix in retinal development
  JOURNAL   J Cell Biol 111 (6 Pt 1), 2775-2784 (1990)
   PUBMED   1703544
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341401.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1203846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1234
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..1234
                     /product="retinol-binding protein 3 precursor"
                     /note="retinol-binding protein 2; interphotoreceptor
                     retinol- binding protein; interphotoreceptor retinoid
                     binding protein; retinol binding protein 3, interstitial"
                     /calculated_mol_wt=132774
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1978
     Region          27..318
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(86,237,297)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
     Region          329..624
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(384,545,605)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
     Region          637..929
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(696,848,906)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
     Region          938..1224
                     /region_name="Peptidase_S41_IRBP"
                     /note="Interphotoreceptor retinoid-binding protein; serine
                     protease family S41; cd07563"
                     /db_xref="CDD:143479"
     Site            order(995,1147,1205)
                     /site_type="active"
                     /note="active site triad [active]"
                     /db_xref="CDD:143479"
     CDS             1..1234
                     /gene="Rbp3"
                     /gene_synonym="Irbp"
                     /coded_by="NM_001191832.1:73..3777"
                     /db_xref="GeneID:24711"
                     /db_xref="RGD:3545"
ORIGIN      
        1 mmrewvlvls tllcvlagpt hlfqpslvld makvlldnyc fpenlmgmqa aieqamkshe
       61 ilgisdpqtl ahvltvgvqs slndprlfis yepstleapq qapaltdltr eellaqiqrn
      121 irhevlednv gylrvddlpg qevlselgef lvshvwkqlt gtsslvldlr hcagghvsgi
      181 pyvisylhpg ntvlhvdtiy drpsntttei wtlpkvlger ysadkdvvvl tsghtggvae
      241 diayilkqmr raivvgerte ggaldlqklr igqsdffltv pvsrslgplg gggqtwegsg
      301 vlpcvgipae qalekalail tlrralpgvv lrlqealqdy ytlvdrvpgl lhhlasmdys
      361 avvseedlvt klnaglqavs edprllvrat gpretpsrpe tgpneppavt pevpkeedar
      421 ralvdsvfqv svlpgnvgyl rfdrfadasv lktlgpyvlr qvweplqdte hlimdlrhnp
      481 ggpssavplv lsyfqgpeag pvrlfttydr rtnitqehfs hkellgqryg nrrgvyllts
      541 hrtataaeef aflmqslswa tlvgeitags llhtctvpll dspeggltlt vpvltfidnh
      601 geawlgggvv pdaivlaeea leraqevldf hrslgalveg tgrlleahya rpeiaeqard
      661 llqsklaqga yrtavdlesl asqltadlqe vsedhrllvf hspgelvaee vplpppaips
      721 peelsyliea lfktdvlpgh lgylrfdama eletvkaigp qlvrlvwqrl vdtaalvvdl
      781 rynpgsyssa vpllcsyffe eeprqhlysv fdratsrvte iwtlplvagq rygshkdlyi
      841 lmshtsgsaa eafahtmqdl qratvigept aggalsvgiy qvdnsplyas mptqmalsat
      901 tgeawdlagv epditvpmse alstaqdiva lrakvptvlq tagklvadny aspelgakma
      961 aklsglqsry arvtsegala emlgadlqml sgdphlktah ipedakdrip givpmqipsp
     1021 evfedlikfs fhtnvfedni gylrfdmfgd celliqvsel lvehiwkkiv htdaliidmr
     1081 fniggptssi salcsyffde appvlldkiy nrpndsisel wthsqltger ygskksvail
     1141 tsgvtagaae eftyimkrlg ralvvgevts ggcqppqtyh vddthlyiti ptarsvgatd
     1201 gsswegvgvt pnvvvssela ltrakeilqr alra
//
LOCUS       NP_640352                228 aa            linear   ROD 03-APR-2025
DEFINITION  death domain-containing membrane protein NRADD [Rattus norvegicus].
ACCESSION   NP_640352
VERSION     NP_640352.1
DBSOURCE    REFSEQ: accession NM_139259.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Gowrishankar,K., Zeidler,M.G. and Vincenz,C.
  TITLE     Release of a membrane-bound death domain by gamma-secretase
            processing of the p75NTR homolog NRADD
  JOURNAL   J Cell Sci 117 (Pt 18), 4099-4111 (2004)
   PUBMED   15280425
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Wang,X., Shao,Z., Zetoune,F.S., Zeidler,M.G., Gowrishankar,K. and
            Vincenz,C.
  TITLE     NRADD, a novel membrane protein with a death domain involved in
            mediating apoptosis in response to ER stress
  JOURNAL   Cell Death Differ 10 (5), 580-591 (2003)
   PUBMED   12728256
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Frankowski,H., Castro-Obregon,S., del Rio,G., Rao,R.V. and
            Bredesen,D.E.
  TITLE     PLAIDD, a type II death domain protein that interacts with p75
            neurotrophin receptor
  JOURNAL   Neuromolecular Med 1 (3), 153-170 (2002)
   PUBMED   12095158
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF497263.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF497263.1, SRR8487230.65671.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..228
                     /product="death domain-containing membrane protein NRADD"
                     /note="p75-like apoptosis-inducing death domain protein
                     PLAIDD; neurotrophin receptor homolog-2; neurotrophin
                     receptor-alike death domain protein"
                     /calculated_mol_wt=24297
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K5A9.2)"
     Site            37
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8K5A9.2)"
     Region          48..85
                     /region_name="TNFR_16_TM"
                     /note="Tumor necrosis factor receptor member 16
                     trans-membrane domain; pfam18422"
                     /db_xref="CDD:436489"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K5A9.2)"
     Region          138..222
                     /region_name="death domain"
     Region          138..219
                     /region_name="Death_p75NR"
                     /note="Death domain of p75 Neurotrophin Receptor; cd08311"
                     /db_xref="CDD:260025"
     CDS             1..228
                     /gene="Nradd"
                     /gene_synonym="NRH2; PLAIDD"
                     /coded_by="NM_139259.2:185..871"
                     /db_xref="GeneID:246143"
                     /db_xref="RGD:708524"
ORIGIN      
        1 mlhnvskgvv ysdtalkgqd gdregmwvga ggalapntss lfppeppgas sniipvycal
       61 latvvlglla yvafkcwrsr kqrqqlakar tvelgdpdrd qrhgdssvfv dsphglepci
      121 psqgphadlg crlylhipqq qqeevqrlli lgepakgwrg lagqlgyqae avetmacdqd
      181 payallrdwa aqegsgatlr vledaltaig redvvqvlss paegcsvv
//
LOCUS       NP_001092961             857 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 17 [Rattus norvegicus].
ACCESSION   NP_001092961 XP_001075348
VERSION     NP_001092961.1
DBSOURCE    REFSEQ: accession NM_001099491.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 18, 2007 this sequence version replaced XP_001075348.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..857
                     /product="vomeronasal 2 receptor, 17"
                     /calculated_mol_wt=97731
     Region          41..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,170..171,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          512..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..835
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..857
                     /gene="Vom2r17"
                     /coded_by="NM_001099491.1:1..2574"
                     /db_xref="GeneID:690716"
                     /db_xref="RGD:1592248"
ORIGIN      
        1 mltfillffl lnipllvasf iyprcfwsmk kneyqdrnlg tgcmffilav qqpvekkyfs
       61 hisniqipte nqkyplalaf smneinnnpd ilpnmslafk csedscyles qynslfslal
      121 qnheilpnfi caedikcgvv lsglkwettv tlhiilnnfm fqqfrqltyg hfhpalcdhe
      181 nfphlyqmas ddtslalalv sfiihfswnw iglaipdndq gthflsylrr emekntvcfa
      241 fvniipvnmn lymsraelyy sqimtssanv viiygdtgst lavsftmwes lgiqrlwvtt
      301 sqwdvtpfkk dftfdngygt fgfghrhsei sgfkyfvqtl npfkysdeyl vklewmyinc
      361 kilenkcktl kncsfnhsle wlmthtfdma viegsyeiyn avyafahalh emtlqnvdnl
      421 lldnykeqny nckkvypfls kiqftnpvgd tvnmnqrnkl keeydifynw nfpqglgfkv
      481 kigifspyfp kgqqlhlren ilewstgsiq mptsvcsadc gpgfrkvwkn gmpaccfdcs
      541 pcpeneisne tnvelcvqcp eeqyanqeqn hcihkarifl sydeplgmvl slmalclaal
      601 tvvvlgvfvk hhrtpivkan nctltyilli alifcflcpl ffighpnsat cilqqitfgv
      661 vftvaistvl aktttvilaf ritaphrmmk yflisratny iipictliqi ivcaiwlgas
      721 ppsvdidaqs ehghiiivcn kgsvtafycv lgylaclafv sftlaflsrn lpvtfneaks
      781 mtfsmlvfcs vwvtflpvyh stkgkvmvvv eifstlassa gmlgcifvpk cytilcrpdr
      841 nslqmikeks sshthil
//
LOCUS       NP_001178942             524 aa            linear   ROD 03-APR-2025
DEFINITION  homeobox protein NOBOX [Rattus norvegicus].
ACCESSION   NP_001178942 XP_578257
VERSION     NP_001178942.1
DBSOURCE    REFSEQ: accession NM_001192013.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ferrari,I., Bouilly,J., Beau,I., Guizzardi,F., Ferlin,A.,
            Pollazzon,M., Salerno,M., Binart,N., Persani,L. and Rossetti,R.
  TITLE     Impaired protein stability and nuclear localization of NOBOX
            variants associated with premature ovarian insufficiency
  JOURNAL   Hum Mol Genet 25 (23), 5223-5233 (2016)
   PUBMED   27798098
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Choi,M., Lee,O.H., Jeon,S., Park,M., Lee,D.R., Ko,J.J., Yoon,T.K.,
            Rajkovic,A. and Choi,Y.
  TITLE     The oocyte-specific transcription factor, Nobox, regulates the
            expression of Pad6, a peptidylarginine deiminase in the oocyte
  JOURNAL   FEBS Lett 584 (16), 3629-3634 (2010)
   PUBMED   20659469
  REMARK    Erratum:[FEBS Lett. 2010 Nov 5;584(21):4490]
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Monti,M. and Redi,C.
  TITLE     Oogenesis specific genes (Nobox, Oct4, Bmp15, Gdf9, Oogenesin1 and
            Oogenesin2) are differentially expressed during natural and
            gonadotropin-induced mouse follicular development
  JOURNAL   Mol Reprod Dev 76 (10), 994-1003 (2009)
   PUBMED   19480014
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Choi,Y., Qin,Y., Berger,M.F., Ballow,D.J., Bulyk,M.L. and
            Rajkovic,A.
  TITLE     Microarray analyses of newborn mouse ovaries lacking Nobox
  JOURNAL   Biol Reprod 77 (2), 312-319 (2007)
   PUBMED   17494914
  REMARK    Erratum:[Biol Reprod. 2008 Feb;78(2):378]
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Gazdag,E., Rajkovic,A., Torres-Padilla,M.E. and Tora,L.
  TITLE     Analysis of TATA-binding protein 2 (TBP2) and TBP expression
            suggests different roles for the two proteins in regulation of gene
            expression during oogenesis and early mouse development
  JOURNAL   Reproduction 134 (1), 51-62 (2007)
   PUBMED   17641088
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Choi,Y. and Rajkovic,A.
  TITLE     Characterization of NOBOX DNA binding specificity and its
            regulation of Gdf9 and Pou5f1 promoters
  JOURNAL   J Biol Chem 281 (47), 35747-35756 (2006)
   PUBMED   16997917
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Rajkovic,A., Pangas,S.A., Ballow,D., Suzumori,N. and Matzuk,M.M.
  TITLE     NOBOX deficiency disrupts early folliculogenesis and
            oocyte-specific gene expression
  JOURNAL   Science 305 (5687), 1157-1159 (2004)
   PUBMED   15326356
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_578257.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..524
                     /product="homeobox protein NOBOX"
                     /calculated_mol_wt=56897
     Region          136..192
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..524
                     /gene="Nobox"
                     /gene_synonym="RGD1563929"
                     /coded_by="NM_001192013.1:1..1575"
                     /db_xref="GeneID:502759"
                     /db_xref="RGD:1563929"
ORIGIN      
        1 meppeklcrk mrgqeagdkp rtaaqdtegp pqdpaplvqg dpdklsslpr aglgkrplsk
       61 tsgdcidadt crvhtapspa vcspkpqkkg sslqekkaet vkpsmsagpg qvpnplnfre
      121 rdlkkeplea tcqfrkktrt lyrsdqleel erifqedhyp dsdkrheiaq mvgvtpqrim
      181 vwfqnrrakw rkveklneke dnngpappra nssqcrsape llgpmptdle pgpvppenil
      241 dgfteppvll tsdqtltssq hnesaervav tppllspppi rrtnlplplg pfqapqvlpp
      301 lrdvpgsdsi ykdkpcgswg tsitsppiys nledmgpqdy qasnqlgsfq ltqapqtplf
      361 pplqsqvpyl ppfplpipsp lpflppedsl fsfpfglngd ssqdyypgpq sgqillqpta
      421 gntgpgpwsg hclpeppfpr phhpqghplg aegyfpdlfp tpcaptlskq pslglsgllg
      481 gtravtgtsi skmpdeqtss sleqpapeev rdknkdsqvg gake
//
LOCUS       NP_001032632             187 aa            linear   ROD 03-APR-2025
DEFINITION  cerebral dopamine neurotrophic factor precursor [Rattus
            norvegicus].
ACCESSION   NP_001032632 XP_341562
VERSION     NP_001032632.1
DBSOURCE    REFSEQ: accession NM_001037543.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Stepanova,P., Srinivasan,V., Lindholm,D. and Voutilainen,M.H.
  TITLE     Cerebral dopamine neurotrophic factor (CDNF) protects against
            quinolinic acid-induced toxicity in in vitro and in vivo models of
            Huntington's disease
  JOURNAL   Sci Rep 10 (1), 19045 (2020)
   PUBMED   33154393
  REMARK    GeneRIF: Cerebral dopamine neurotrophic factor (CDNF) protects
            against quinolinic acid-induced toxicity in in vitro and in vivo
            models of Huntington's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Wang,L., Wang,Z., Xu,X., Zhu,R., Bi,J., Liu,W., Feng,X., Wu,H.,
            Zhang,H., Wu,J., Kong,W., Yu,B. and Yu,X.
  TITLE     Recombinant AAV8-mediated intrastriatal gene delivery of CDNF
            protects rats against methamphetamine neurotoxicity
  JOURNAL   Int J Med Sci 14 (4), 340-347 (2017)
   PUBMED   28553166
  REMARK    GeneRIF: Results demonstrated that CDNF overexpression in the brain
            could attenuate the METH-induced dopamine and tyrosine hydroxylase
            loss in the striatum but could not lower METH-induced hyperthermia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Liu,H., Zhao,C., Zhong,L., Liu,J., Zhang,S., Cheng,B. and Gong,L.
  TITLE     Key subdomains in the C-terminal of cerebral dopamine neurotrophic
            factor regulate the protein secretion
  JOURNAL   Biochem Biophys Res Commun 465 (3), 427-432 (2015)
   PUBMED   26271594
  REMARK    GeneRIF: In all, these findings suggest that helix-7 in the
            C-terminal is important for CDNF secretion, which maybe potential
            affect CDNF function in ER stress.
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Cheng,L., Zhao,H., Zhang,W., Liu,B., Liu,Y., Guo,Y. and Nie,L.
  TITLE     Overexpression of conserved dopamine neurotrophic factor (CDNF) in
            astrocytes alleviates endoplasmic reticulum stress-induced cell
            damage and inflammatory cytokine secretion
  JOURNAL   Biochem Biophys Res Commun 435 (1), 34-39 (2013)
   PUBMED   23624196
  REMARK    GeneRIF: Data show that overexpression of conserved dopamine
            neurotrophic factor (CDNF) in astrocytes alleviated cell damage and
            proinflammatory cytokine secretion, which may represent a promising
            strategy for neuroprotection in the central nervous system (CNS).
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Sun,Z.P., Gong,L., Huang,S.H., Geng,Z., Cheng,L. and Chen,Z.Y.
  TITLE     Intracellular trafficking and secretion of cerebral dopamine
            neurotrophic factor in neurosecretory cells
  JOURNAL   J Neurochem 117 (1), 121-132 (2011)
   PUBMED   21235575
  REMARK    GeneRIF: Disruption of the helix-1 domain of cerebral dopamine
            neurotrophic factor significantly reduces its secretion in
            endoplasmic reticulum.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Dec 1, 2005 this sequence version replaced XP_341562.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ128463.1, FQ121633.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..187
                     /product="cerebral dopamine neurotrophic factor precursor"
                     /note="ARMET-like protein 1; conserved dopamine
                     neurotrophic factor; arginine-rich protein mutated in
                     early stage tumors-like 1; arginine-rich, mutated in early
                     stage tumors-like 1"
                     /calculated_mol_wt=18817
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2562
     mat_peptide     25..187
                     /product="Cerebral dopamine neurotrophic factor.
                     /id=PRO_0000306860"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5I0.1)"
                     /calculated_mol_wt=18817
     Region          36..132
                     /region_name="ARMET_N"
                     /note="ARMET, N-terminal; pfam20145"
                     /db_xref="CDD:466306"
     Region          136..178
                     /region_name="ARMET_C"
                     /note="ARMET, C-terminal; pfam10208"
                     /db_xref="CDD:462997"
     CDS             1..187
                     /gene="Cdnf"
                     /gene_synonym="Armetl1"
                     /coded_by="NM_001037543.1:61..624"
                     /db_xref="GeneID:361276"
                     /db_xref="RGD:1307600"
ORIGIN      
        1 mrctspaalv tfcaglwisn hvlaqgleag vrsradcevc keflnrfyns lltrgidfsv
       61 dtieeelisf cadtkgkenr lcyylgatkd satkilgevt rpmsvhmptv kiceklkkmd
      121 sqicelkyek kldlesvdlw kmrvaelkqi lhswgeecra caekhdyvnl ikelapkyve
      181 trpqtel
//
LOCUS       NP_001178897             924 aa            linear   ROD 03-APR-2025
DEFINITION  autophagy-related protein 9B [Rattus norvegicus].
ACCESSION   NP_001178897 XP_575327
VERSION     NP_001178897.1
DBSOURCE    REFSEQ: accession NM_001191968.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Yang,Z. and Klionsky,D.J.
  TITLE     Mammalian autophagy: core molecular machinery and signaling
            regulation
  JOURNAL   Curr Opin Cell Biol 22 (2), 124-131 (2010)
   PUBMED   20034776
  REMARK    Review article
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Wohlgemuth,S.E., Julian,D., Akin,D.E., Fried,J., Toscano,K.,
            Leeuwenburgh,C. and Dunn,W.A. Jr.
  TITLE     Autophagy in the heart and liver during normal aging and calorie
            restriction
  JOURNAL   Rejuvenation Res 10 (3), 281-292 (2007)
   PUBMED   17665967
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Yamada,T., Carson,A.R., Caniggia,I., Umebayashi,K., Yoshimori,T.,
            Nakabayashi,K. and Scherer,S.W.
  TITLE     Endothelial nitric-oxide synthase antisense (NOS3AS) gene encodes
            an autophagy-related protein (APG9-like2) highly expressed in
            trophoblast
  JOURNAL   J Biol Chem 280 (18), 18283-18290 (2005)
   PUBMED   15755735
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_575327.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..924
                     /product="autophagy-related protein 9B"
                     /note="ATG9 autophagy related 9 homolog B"
                     /calculated_mol_wt=101669
     Region          186..678
                     /region_name="ATG9"
                     /note="Autophagy protein ATG9; pfam04109"
                     /db_xref="CDD:461177"
     CDS             1..924
                     /gene="Atg9b"
                     /gene_synonym="RGD1560887"
                     /coded_by="NM_001191968.1:1..2775"
                     /db_xref="GeneID:499973"
                     /db_xref="RGD:1560887"
ORIGIN      
        1 mvrrmgwggs rrqrgrwgdl gpssvpllpm alplpaspcr glgggrisvf slspaprtrs
       61 cssslfppts gspslviqea gasqppfnal ptpatpptqa lptmthtsas pswgshstpp
      121 lasvtpppsc rcpqdhpglr igplipeqdy erledcdpeg sqdssspvhg edhqpllhvp
      181 eglrgswhhi qnldsfftki ysyhqrngfa cilledvfql gqfifivtft tfllrcvdyn
      241 vlfnnqpknh trpgplhskv tlsdailpsa qcaekihgsp llvfllvlaa gfwlfqllrs
      301 vcnlfsywdi qvfyrealhi ppeelssvpw aevqsrllel qrsgglcvqp rplteldvhh
      361 rilrytnyqv alankgllpa rcplpwggsa aflsrglaln vdlllfrgpf slfrggwelp
      421 eaykrsdlrg vlatrwrrtv lllaavnlal splvlawqvl hafyshvell rrepgafgar
      481 rwsrlarlql rhfnelphel rarlgrayrp ataflraaep paplrallar qlvffsgalf
      541 aallvltiyd edvlavehvl ttmtalgvta tvarsfipee qcqgrssqll lqaalahmhy
      601 lpeepgaaga rtssywqmsq llqyravsll eellsplltp lfllfwfrpr alqiidffhh
      661 ftvdvagvgd icsfalmdvk rhghpqwlse gqteaslsqr aedgktelsl mrfslahpqw
      721 qppghsskfl ghlrgrvqqd aaawgapstr spptpgvlsd ctsplpeafl anllvsprpp
      781 qrdlsptapc paaataslla sisrmaqdps cvspggtggq kltqlpelvs aemslhaiyl
      841 hqlhqqqqqe vwgeasassp srpwsspsqp gspdeekpsw ssdgsspass prqqwgtqra
      901 qnlfpkdfqe ttdaqkeplp gslh
//
LOCUS       NP_001136416             451 aa            linear   ROD 03-APR-2025
DEFINITION  tripartite motif-containing 43-like [Rattus norvegicus].
ACCESSION   NP_001136416 XP_001066018 XP_236463
VERSION     NP_001136416.1
DBSOURCE    REFSEQ: accession NM_001142944.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000008.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.829612.1,
                                           SRR26360181.1583777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..451
                     /product="tripartite motif-containing 43-like"
                     /calculated_mol_wt=52277
     Region          10..58
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(15,18,30,32,35,38,52,55)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438495"
     Region          63..>256
                     /region_name="sbcc"
                     /note="exonuclease SbcC; TIGR00618"
                     /db_xref="CDD:129705"
     Region          86..138
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <335..446
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..451
                     /gene="Trim43a"
                     /gene_synonym="RGD1561074"
                     /coded_by="NM_001142944.1:1..1356"
                     /db_xref="GeneID:300884"
                     /db_xref="RGD:1561074"
ORIGIN      
        1 mesdnlqasq eiltcficlg iftdlvltrc ghpfcracll lfsadtqipi hcplcrhpsk
       61 pnfrtaipgk klisivrker ikkylsseeh kcmthkerkt ifcdenrvll cqlcsksqeh
      121 rghrhchiee avlkqmekll kqmesllkki qelqenleae ktmtdqwmdy vtlreemirt
      181 eyrklypsld eeeaqhiecm knqgntnlee lrkseammvh krsqlmkvyq elmtmsqkpy
      241 evlqqglddl frrcelvqlg mpqvmkpels ahpnagltar fsffkvkiff qnliilnckm
      301 sqffdirrft srpchqntsl dsagsyrasw gamdfttgkh yweldlkdce hwavgvcsnv
      361 wlsrshkkig ssgafllvcv kegnhyslft tcpvshhyie kptgrvgvfl dceggcmsfl
      421 dvaksslihs yhpeafslrv rpffstvytr s
//
LOCUS       NP_001092957             783 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 37 [Rattus norvegicus].
ACCESSION   NP_001092957 XP_001074211
VERSION     NP_001092957.1
DBSOURCE    REFSEQ: accession NM_001099487.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 19, 2007 this sequence version replaced XP_001074211.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..783
                     /product="vomeronasal 2 receptor, 37"
                     /calculated_mol_wt=88375
     Region          1..424
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(30,33,76,163)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          432..485
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          505..756
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          505..530
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(508,511..512,515..516,518..519,553,557,560..561,569,
                     573)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          542..563
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(562,574..575,578..579,582,662,667,670..671,674,708,
                     711..712,715,719,727..728,731,734,738)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          572..596
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          620..636
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          663..689
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          697..720
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          725..750
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..783
                     /gene="Vom2r37"
                     /coded_by="NM_001099487.1:28..2379"
                     /db_xref="GeneID:690356"
                     /db_xref="RGD:1597332"
ORIGIN      
        1 mfaieevnrn phllhnttig ydiynipyte knilysallw htgiinplpn cdcghkrksp
       61 vvltgpswsa sahigtllql ykipqltfgp fdstlndqgt snslyqmapk dtslslaivl
      121 lmlhfswswv glmlpddhrg tqflsdlren mesngiciaf skmipgtwna fsnalwksme
      181 kieessanvi viygdiisve glirhiaqll vtwkvwvlns swdvdnhsdy fmvesfhgsl
      241 vfsyhheemi efmnfiqtvn pykypeddyl pkfwflffkc sfskfdcqll encqlnasle
      301 llprhifdpt mseegyniyn avyavayslh elslqqiqiq pyinekgmvf spwqllpflr
      361 ttinkshvkg htvmdggrnl dtkydilnfw nfpsglglkv kvgtyslssy kdvqfslceg
      421 miqwptrftk ipqsvcsesc rpglrkaaqe gkavccfdct pcaeneisne tdmdqcvkcp
      481 eshyanaekn hclrksvsfl ayeeplgmal titalgfsvl tavvlvvfvk hrdtpivkan
      541 nrslsyilll tlficflssl lfigqprtat cilqqtafgi lftvalstvl akaitvviaf
      601 katvparmvr wlmvsrapnf iipfctliqi iicgiwlvts ppfidqdtha elghiiivcn
      661 mgstvafhtv lgylcslalg sytmaflsrn lpdtfneakf lsfsmqvffc vwitflpvyh
      721 stkgkvmvam evfsilassi allglifapk cyiillrtek nscpgirhkk hsksnihlnl
      781 vkn
//
LOCUS       NP_001092943             605 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor, 35 [Rattus norvegicus].
ACCESSION   NP_001092943 XP_001063172 XP_218287
VERSION     NP_001092943.1
DBSOURCE    REFSEQ: accession NM_001099473.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On or before Aug 19, 2007 this sequence version replaced
            XP_218287.4, XP_001063172.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..605
                     /product="vomeronasal 2 receptor, 35"
                     /note="putative zinc finger protein"
                     /calculated_mol_wt=66811
     Region          <1..232
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          253..306
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          349..577
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          363..384
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          393..415
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          441..457
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          484..507
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          519..541
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          546..571
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..605
                     /gene="Vom2r35"
                     /gene_synonym="RGD1559147"
                     /coded_by="NM_001099473.1:286..2103"
                     /db_xref="GeneID:292615"
                     /db_xref="RGD:1559147"
ORIGIN      
        1 mqkctarvvl vflsnsnfql ilhgllavpv sgqvwvskgt lhmalaltvp gvfqvlqgtf
       61 gllyhssrai gfpeflthls psqtpedmfi kkfweftfdc twpyqnstvt egvqicsgne
      121 slknkphpfp evskidaayt avysiahalh dmvasahqdg kgtnsqdfhh wqllhalrkv
      181 hfktpdrsei mfdangdlvt kfdifqgqkn pngvfhlvhv gmidpqassg nkmmiqlkkd
      241 lqvsslnaei tvppsicses clpgfsqvpr lgaphccfdc spcpegqfad qrdmkrcllc
      301 pkeqyssntr dhclprteif lafeeplgfi lalmaillag lallvlgvfl khrdipvvra
      361 nnrtlsyfll islslcslcs llflgrptvt tcllrqttfa vvftvavssv laktvtvvla
      421 frvtkpgsri qvclspgast sviliasliq tvlcgvwlat sppfperdmi seprhiviqc
      481 qegsgatffc vlgflgflav gtfsvaflar dlpdvfnetk fltfsmllfc svwtaflply
      541 hsargkstva veifsilast dgllcgifip kcyiillkpe kntpawlrqg rcahqdrqfs
      601 mlhrr
//
LOCUS       NP_001178600             932 aa            linear   ROD 03-APR-2025
DEFINITION  ER degradation-enhancing alpha-mannosidase-like protein 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_001178600 XP_222721
VERSION     NP_001178600.1
DBSOURCE    REFSEQ: accession NM_001191671.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Ninagawa,S., Okada,T., Sumitomo,Y., Kamiya,Y., Kato,K.,
            Horimoto,S., Ishikawa,T., Takeda,S., Sakuma,T., Yamamoto,T. and
            Mori,K.
  TITLE     EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first
            mannose trimming step
  JOURNAL   J Cell Biol 206 (3), 347-356 (2014)
   PUBMED   25092655
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Hirao,K., Natsuka,Y., Tamura,T., Wada,I., Morito,D., Natsuka,S.,
            Romero,P., Sleno,B., Tremblay,L.O., Herscovics,A., Nagata,K. and
            Hosokawa,N.
  TITLE     EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic
            reticulum-associated degradation and mannose trimming
  JOURNAL   J Biol Chem 281 (14), 9650-9658 (2006)
   PUBMED   16431915
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Jul 17, 2010 this sequence version replaced XP_222721.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.44613.1,
                                           SRR26643298.51537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..932
                     /product="ER degradation-enhancing alpha-mannosidase-like
                     protein 3 precursor"
                     /EC_number="3.2.1.113"
                     /note="ER degradation-enhancing alpha-mannosidase-like 3;
                     ER degradation enhancer, mannosidase alpha-like 3"
                     /calculated_mol_wt=100089
     sig_peptide     1..42
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4160
     Region          60..499
                     /region_name="Glyco_hydro_47"
                     /note="Glycosyl hydrolase family 47; pfam01532"
                     /db_xref="CDD:460241"
     Region          665..790
                     /region_name="PA_EDEM3_like"
                     /note="protease associated domain (PA) domain-containing
                     EDEM3-like proteins. This group contains various PA
                     domain-containing proteins similar to mouse EDEM3
                     (ER-degradation-enhancing mannosidase-like 3 protein).
                     EDEM3 contains a region, similar to Class I...; cd02126"
                     /db_xref="CDD:239041"
     Site            749..751
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239041"
     CDS             1..932
                     /gene="Edem3"
                     /gene_synonym="RGD1561496"
                     /coded_by="NM_001191671.1:119..2917"
                     /db_xref="GeneID:289085"
                     /db_xref="RGD:1561496"
ORIGIN      
        1 mseagggrgc gcrvpqrasw slvaataaly lmlattvcta gaapmsreek qklgnqvlem
       61 fdhaygnyme haypadelmp ltcrgrvrgq epsrgdvdda lgkfsltlid sldtlvvlnk
      121 tkefedavrk vlrdvnldnd vvvsvfetni rvlggllggh slaimlkekg eymqwyndel
      181 lqmakqlgyk llpafnttsg lpyprinlkf girkpeartg tetdtctaca gtlilefaal
      241 srftgatvfe eyarkaldfl wekrqrssnl vgvtinihtg dwvrkdsgvg agidsyyeyl
      301 lkayvllgdd sflerfnthy daimryisqp pllldvhihk pmlnartwmd allaffpglq
      361 vlkgdirpai ethemlyqvi kkhnflpeaf ttdfrvhwaq hplrpefaes tyflykatgd
      421 pyylevgktl ienlnkyarv pcgfaamkdv rtgshedrmd sfflaemfky lyllfadked
      481 iifdiedyif tteahllplw lsttnrnisk knttseytel ddsnfdwtcp ntqilfpndp
      541 lyaqsirepl knvvdkscpr giirveesfr sgakpplrar dfmatnpehl eilkkmgvsl
      601 ihlkdgrvql vqhaiqaass vdaedglrfm qemielssqq qkeqqlppra vqiishpffg
      661 rvvltagpaq fgldlskhke trgfvasskp yngcseltnp eavmgkiali qrgqcmfaek
      721 arniqnagai ggividdneg sssdtaplfq magdgkdtdd ikipmlflfs kegsiildai
      781 reheqvevll sdkardrdpe venedqpsse ndsqnqsaeq mlplpqtvgl adqespgnpl
      841 espseppspa dseeaagfap seqissptet qetagldgec tdldnqlqdq peteedpspn
      901 vswgtkaqpm dsiladwned ieafemmekd el
//
LOCUS       NP_001424118              83 aa            linear   ROD 03-APR-2025
DEFINITION  similar to human chromosome 14 open reading frame 132 [Rattus
            norvegicus].
ACCESSION   NP_001424118
VERSION     NP_001424118.1
DBSOURCE    REFSEQ: accession NM_001437189.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2432225.1,
                                           SRR26360194.2042210.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..83
                     /product="similar to human chromosome 14 open reading
                     frame 132"
                     /note="uncharacterized protein C14orf132 homolog"
                     /calculated_mol_wt=8786
     CDS             1..83
                     /gene="C6h14orf132"
                     /coded_by="NM_001437189.1:245..496"
                     /db_xref="GeneID:100909954"
                     /db_xref="RGD:6501064"
ORIGIN      
        1 mdlsfmaaql pmmggafmds pnedfsteys lfnspanvhs tsnghgqlee sprssndavl
       61 lwiaiiatvg nivvvgvvya ftf
//
LOCUS       NP_001092946             865 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 38 precursor [Rattus norvegicus].
ACCESSION   NP_001092946 XP_001080246 XP_218549
VERSION     NP_001092946.1
DBSOURCE    REFSEQ: accession NM_001099476.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On or before Aug 19, 2007 this sequence version replaced
            XP_218549.4, XP_001080246.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..865
                     /product="vomeronasal 2 receptor 38 precursor"
                     /calculated_mol_wt=96480
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2197
     Region          40..506
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(74,171..172,396)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(112,115,158,245)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          514..567
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          587..838
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          587..612
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(590,593..594,597..598,600..601,635,639,642..643,651,
                     655)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          624..645
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(644,656..657,660..661,664,744,749,752..753,756,790,
                     793..794,797,801,809..810,813,816,820)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          654..678
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          702..718
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          745..771
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          779..802
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          807..832
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..865
                     /gene="Vom2r38"
                     /gene_synonym="RGD1565669"
                     /coded_by="NM_001099476.1:1..2598"
                     /db_xref="GeneID:308551"
                     /db_xref="RGD:1565669"
ORIGIN      
        1 mlwiftfgfl yipnflcalt dnecyvtskd yfyhegdvti gaffplhily tgnkvshkye
       61 pynlqdlhiq ykfknyqfvl almfaieein rnphllpntt lgydiynipy teknilysaf
      121 lwhtgiinpl pncdcghkrk spavltgpsw sasahigtll qlykipqltf gpfdsilndq
      181 gqfnslyqma pkdtslslai vllmlhfsws wvglmlpddh rgtqflsdlr enmesngici
      241 aflkmipgtw nafsnalwkn mekieessan viviygdiis iqglmrhvaq llvtwkvwvl
      301 nsswdidshs dyfmlesfhg slifshhhee miefmnfiqt vnpykypedn ylpkfwflff
      361 kcpfskfdch llencqpnas lellprhifd ptmseegyni ynavyavays lheinlqqtq
      421 tqpytnekgm vfspwqllpf lkttikkshv rghtvmvggr nlntkydiln fwnfpsglgl
      481 kvkvgtysls ahqgvhfslc eemiqwptkf tkipqsvcse scrpgfrkaa qegkavccfn
      541 ctpcaeneis netdmdqclk cpeshyanse knhclrksvs flayeeplgm altitalgfs
      601 vltavvlvvf vkhrdtpivk annrslsyil lltlficfls sllfigqpst atcilqqtaf
      661 gilftvalst vlakaitvvi afkatvparm vrwlmvsrap nfiipfctli qiiicgiwlv
      721 tsppfidqdt haerghiiiv cnmgsivafh tvlgylcsla lgsyamafls rnlpdtfnea
      781 kflsfsmqvf fcvwitflpv yhstkgkvmv smeifstlas siallglifa pkcyiillrp
      841 eknscidirh krhsrrnihl hlvkn
//
LOCUS       NP_001102345             311 aa            linear   ROD 03-APR-2025
DEFINITION  zeta-sarcoglycan [Rattus norvegicus].
ACCESSION   NP_001102345 XP_001066057 XP_344527
VERSION     NP_001102345.2
DBSOURCE    REFSEQ: accession NM_001108875.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wheeler,M.T., Zarnegar,S. and McNally,E.M.
  TITLE     Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is
            reduced in muscular dystrophy
  JOURNAL   Hum Mol Genet 11 (18), 2147-2154 (2002)
   PUBMED   12189167
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 1, 2008 this sequence version replaced NP_001102345.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1268443.1,
                                           SRR26360190.2243250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..311
                     /product="zeta-sarcoglycan"
                     /calculated_mol_wt=34328
     Region          38..296
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     CDS             1..311
                     /gene="Sgcz"
                     /coded_by="NM_001108875.2:220..1155"
                     /db_xref="GeneID:364605"
                     /db_xref="RGD:1307788"
ORIGIN      
        1 mdrstdldiq elkmtreqyi latqqnnlpr penaqlypvg iygwrkrcly ffvllllvtm
       61 ivnlamtiwi lkvmnftvdg mgnlrvtkkg irlegisefl lplyvkeihs rkdsplvlqs
      121 drnvtvnarn hmgqltgqlt vgaeaveaqc krfevrased grvlfsaded eitigaeklk
      181 vtgtegavfg hsvetphvra epsqdlrles ptrslimeap rgvqvsaaag dfkatcrkel
      241 hlqstegeif lnadsirlgn lpigsfsssp sssnsrqtvy elcvcpngkl ylspagvdst
      301 cqssssiclw s
//
LOCUS       NP_001178658             658 aa            linear   ROD 03-APR-2025
DEFINITION  coiled-coil domain-containing protein 120 [Rattus norvegicus].
ACCESSION   NP_001178658 XP_228761
VERSION     NP_001178658.1
DBSOURCE    REFSEQ: accession NM_001191729.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 17, 2010 this sequence version replaced XP_228761.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211363.1, SRR26643298.31208.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..658
                     /product="coiled-coil domain-containing protein 120"
                     /calculated_mol_wt=70712
     Region          2..125
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     CDS             1..658
                     /gene="Ccdc120"
                     /gene_synonym="RGD1561596"
                     /coded_by="NM_001191729.1:42..2018"
                     /db_xref="GeneID:317377"
                     /db_xref="RGD:1561596"
ORIGIN      
        1 mevkgqlins ptfnapaalf geaapqvksd rlrglldrqq alqetlrlkl qelrkvclqe
       61 aeltgqlppe cplepgerpq lvrrrppaar ayppphsnpa hhslcpaeel alealerevs
      121 vqqqiaaaar rlalapdlng eqrrrrrqvq vdalrrlhel eeqlrdfrar lglpvlqplp
      181 lssgapvnaq gvclgtrlaq lsqedvvlhs essslsesga shdneephsc fplterpspp
      241 kawdqfravs ggsperrapw kpppsdiygd lksrrnsvas ptsptrslpr sassfegrsv
      301 patpvltrgs gprlckpegl hprqwsgsqd sqmgfprpdp asdraslfaa rtrrsnssea
      361 llvdraaagg agsppaplap paagppvcks sevlyerpqp vpsfssrttg ppdppraarp
      421 ssaapasrgp prlppvcgdf lldysldrgl prgsggagwg dllpapevpg plsrrdglla
      481 mlpgpppiya adgsspllrs kdpnsrairs kpcglppeav eglevhpnpl lwmppptrip
      541 pagergghkn laleglrdwy irnsglavgp qrrpmlphvg pthtpflhar cyevgqslyg
      601 ppsqaplphs rsftappvsg ryytdflypp elsarlsdlt legeqssssd tqtpgtlv
//
LOCUS       NP_001162620            1003 aa            linear   ROD 03-APR-2025
DEFINITION  NACHT, LRR and PYD domains-containing protein 9 [Rattus
            norvegicus].
ACCESSION   NP_001162620 XP_001072936 XP_218248
VERSION     NP_001162620.1
DBSOURCE    REFSEQ: accession NM_001169149.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Zhu,S., Ding,S., Wang,P., Wei,Z., Pan,W., Palm,N.W., Yang,Y.,
            Yu,H., Li,H.B., Wang,G., Lei,X., de Zoete,M.R., Zhao,J., Zheng,Y.,
            Chen,H., Zhao,Y., Jurado,K.A., Feng,N., Shan,L., Kluger,Y., Lu,J.,
            Abraham,C., Fikrig,E., Greenberg,H.B. and Flavell,R.A.
  TITLE     Nlrp9b inflammasome restricts rotavirus infection in intestinal
            epithelial cells
  JOURNAL   Nature 546 (7660), 667-670 (2017)
   PUBMED   28636595
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Dec 19, 2009 this sequence version replaced
            XP_218248.3, XP_001072936.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.848.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..1003
                     /product="NACHT, LRR and PYD domains-containing protein 9"
                     /note="NACHT, LRR and PYD containing protein 9b; NLR
                     family, pyrin domain containing 9B; NACHT, LRR and PYD
                     containing protein 9a"
                     /calculated_mol_wt=115627
     Region          9..90
                     /region_name="Pyrin_NALPs"
                     /note="Pyrin death domain found in NALP proteins; cd08320"
                     /db_xref="CDD:260032"
     Region          144..308
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          385..>430
                     /region_name="NOD2_WH"
                     /note="NOD2 winged helix domain; pfam17779"
                     /db_xref="CDD:465501"
     Region          440..555
                     /region_name="NLRC4_HD2"
                     /note="NLRC4 helical domain HD2; pfam17776"
                     /db_xref="CDD:465499"
     Region          633..667
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          668..687
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          691..956
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Site            order(694,697,699,702,704,723,726,728,731,733,750,753,755,
                     758,760,779,782,784,787,789,807,810,812,815,817,836,839,
                     841,844,846,864,867,869,872,874,893,896,898,901,903,921,
                     924,926,929,931,950,953,955)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          694..722
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(700..701,730,786,814,871,897,899,925,954)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          723..749
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          750..778
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          779..806
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          807..834
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          836..863
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          893..920
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          921..949
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..1003
                     /gene="Nlrp9"
                     /gene_synonym="Nalp9a; Nalp9b; Nlrp9b"
                     /coded_by="NM_001169149.1:1..3012"
                     /db_xref="GeneID:292577"
                     /db_xref="RGD:1308981"
ORIGIN      
        1 mvdtsgygll khlrklsdge fwsfkellrk epekfklkpi swmkienask eelvmllnth
       61 ypkqawdmal slflqvnred lsimaqkkrr ykqtkykkfm kttfqsiwtl esnicipdrs
      121 yhlivehqyr klqnifdses epvtavvtgp tgegktvflr kamldwasgi lwqnrfqyvf
      181 ffsvlslnnt telslaelis sklpessetl ndilsdpkki lfildgfdyl kfdlelrtnl
      241 cndwrkilpt qiilssllqk imlpesslll elghislpki fpllqyprdi tiqgfsercl
      301 ktyfisffnt ekgievfenl ksnqmlklcs npylcwmfcs clkwqfdree eayfqaktds
      361 vfftsfmvsa fksayasnpp kqnraqlksl ctlavegmwk qlfvfdsedl rrngisesdk
      421 avwlrmkflq nhdnhivfyh ptlqlyfasm fyflkqdkdt hvpvigsipq llrkiyardh
      481 tqwlqigifl fglateqvas llkpyfgfiq hrdvrqevmr ylkslsqrec ceklerpqnl
      541 faclrdnkee kfvrevvdlf eeitvditns hvlsiianhl qkssklkklh lhiqkrvfle
      601 ihdpeysdse tftqdkknaa eywkklchif vnlhvldlds cnfnkqviee lcnvlspspk
      661 iplmafkles llcsfmtnfg dgslfhtllq lphlkylnly gtnlsnsrie nlcsalrrst
      721 ckveelllgk cdisseacgi iatslmnskv khlslvenpl knkgvmslce mlkdpscvle
      781 tlmlsycclt fiacghlyea lvsnkhlsll dlgsnfledt gvnllcealk dpncilkelw
      841 lsgcfltsec ceeisavltc nnnlktlklg nndiedtgvk hlcealshpn ckleclgldl
      901 ckftsdcced lasalttckt lnslnldwkt lehsgvvalc ealnhkkcnl kmlgldksaf
      961 svesqtllqa vekknnnlsi lhypwveeer kkrgvrlvwn skn
//
LOCUS       NP_001178679             869 aa            linear   ROD 03-APR-2025
DEFINITION  interleukin-12 receptor subunit beta-2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001178679 XP_231873
VERSION     NP_001178679.1
DBSOURCE    REFSEQ: accession NM_001191750.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Watanabe,T., Kitani,A., Murray,P.J. and Strober,W.
  TITLE     NOD2 is a negative regulator of Toll-like receptor 2-mediated T
            helper type 1 responses
  JOURNAL   Nat Immunol 5 (8), 800-808 (2004)
   PUBMED   15220916
REFERENCE   2  (residues 1 to 869)
  AUTHORS   Poltorak,A., Merlin,T., Nielsen,P.J., Sandra,O., Smirnova,I.,
            Schupp,I., Boehm,T., Galanos,C. and Freudenberg,M.A.
  TITLE     A point mutation in the IL-12R beta 2 gene underlies the IL-12
            unresponsiveness of Lps-defective C57BL/10ScCr mice
  JOURNAL   J Immunol 167 (4), 2106-2111 (2001)
   PUBMED   11489994
REFERENCE   3  (residues 1 to 869)
  AUTHORS   Oppmann,B., Lesley,R., Blom,B., Timans,J.C., Xu,Y., Hunte,B.,
            Vega,F., Yu,N., Wang,J., Singh,K., Zonin,F., Vaisberg,E.,
            Churakova,T., Liu,M., Gorman,D., Wagner,J., Zurawski,S., Liu,Y.,
            Abrams,J.S., Moore,K.W., Rennick,D., de Waal-Malefyt,R., Hannum,C.,
            Bazan,J.F. and Kastelein,R.A.
  TITLE     Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with
            biological activities similar as well as distinct from IL-12
  JOURNAL   Immunity 13 (5), 715-725 (2000)
   PUBMED   11114383
REFERENCE   4  (residues 1 to 869)
  AUTHORS   Gillespie,K.M., Szeto,C.C., Betin,V.M. and Mathieson,P.W.
  TITLE     Role of beta1 and beta2 subunits of the interleukin-12 receptor in
            determining T helper 1/T helper 2 responses in vivo in the rat
  JOURNAL   Immunology 99 (1), 109-112 (2000)
   PUBMED   10651948
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_231873.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.19587.1,
                                           SRR26643299.19580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q31"
     Protein         1..869
                     /product="interleukin-12 receptor subunit beta-2
                     precursor"
                     /note="interleukin 12 receptor, beta 2"
                     /calculated_mol_wt=95123
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2635
     Region          28..120
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Region          240..332
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(240,302,320)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(321..322,324..325)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          438..526
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(522..523,525..526)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          536..630
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(621..622,624..625)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..869
                     /gene="Il12rb2"
                     /coded_by="NM_001191750.1:1..2610"
                     /db_xref="GeneID:171334"
                     /db_xref="RGD:620026"
ORIGIN      
        1 mahtvrgcsl aliflfmwll ikanidvckl gtvtvqpapv iplgstanis cslnpkqgcs
       61 hypsynelil lkfvndvlve klhgkkvhgh pshssifqvt nlslgmtlfv cklncsnsqk
      121 tqpvpvcgve isvgvapesp qsiscvqkge hgtvacswns gkvtylktyy tlqltgpnnv
      181 tyqnqcysdn rqncsrldlg inltpdlaes rfivhvtatn dlgnsssllh tftfldivrp
      241 lppwdirinf lnasgsrctl qwedegqvvl nrlryqplns tswnmvnatn akgrydlqdl
      301 rpfteyefqi ssklhlsqgs wsnwseslrt rtpeeepvgt ldiwymkqdi dcdrqqislf
      361 wkslnpsear gkilhyqvtl qevtkkttlq nttrhtfwtg viprtgawta svsaanskgt
      421 sapthinivd lcgtgflaph qvsaksgnmd nimvtwqppg kadsvireyi vewralqqgs
      481 vmnltphwlr ippynmsali sekikpyicy eirvhalsed qggcssirgd sshkvplsgp
      541 hitaitekke slfiswthip fleqrgcilh yriywkerhs taqpelceiq yrhsqnshpi
      601 sslqpkvtyv lwmtavtaag espqgneref cpqgkanwkt fvissiciai ivvgtfsiry
      661 frqkaftlls tlkpqwycrt ipdpanstwv kkypimeeki qppmdnllma wsapeepepl
      721 iinevlyqmi pvgrqpycfk rgqgfqgyst skedtiylat npqttgtlta esrqlvnlyk
      781 vlgsrdpdsk lgnltspltv tpvnylpthe gylpsniedl sshevdpsds ldldhqhisl
      841 sifassslrp ltfcgerltl drlkmgyek
//
LOCUS       NP_001092950             864 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 60 precursor [Rattus norvegicus].
ACCESSION   NP_001092950 XP_001065827 XP_577202
VERSION     NP_001092950.1
DBSOURCE    REFSEQ: accession NM_001099480.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000012.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_577202.1, XP_001065827.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..864
                     /product="vomeronasal 2 receptor 60 precursor"
                     /calculated_mol_wt=96325
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2428
     Region          41..511
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(81,176..177,401)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(117,120,163,250)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          519..572
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          592..843
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          592..617
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(595,598..599,602..603,605..606,640,644,647..648,656,
                     660)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          629..650
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(649,661..662,665..666,669,749,754,757..758,761,795,
                     798..799,802,806,814..815,818,821,825)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          659..683
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          707..723
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          750..776
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          784..807
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          812..837
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..864
                     /gene="Vom2r60"
                     /gene_synonym="RGD1560561"
                     /coded_by="NM_001099480.1:1..2595"
                     /db_xref="GeneID:501794"
                     /db_xref="RGD:1560561"
ORIGIN      
        1 mmlllifmfl llqyssdvys fdrsscaakt ktsvykdgdm vlaaflplft itidsasdnq
       61 snnnfyihqh vkeckfihsf hfivlamvya ieeinrnphi lpnvslgydi ynvlfnewwi
      121 lnrcitwlsg pkkyvpnytc rremksiaal tgiswiistn igtllelyky pqltigsfdp
      181 nlnnheqfhd iyqiaykdms lthgivslln yfhwnwvgli vsegqngfqi iselraemdr
      241 nkicvdfvem irvsevsylp syllspthla kstanviity gdsdfmrgfl fylrqilvtr
      301 kvwimnsdwd viiqskhfil qsfhgslifa hhhketsgyr nfiqtvhpsk ypedfyltrf
      361 wfyffncsfa dddcntlenc lpnaslhetp gshfdmvmte fayniynavy avahslhkml
      421 lqqvevtpvk eaedlifsaw qlhpflknmq ftnpageqvn lnekmklnad ydilnywnfp
      481 eglqlkvkvg qfspygplgq qlslsedtie wpteitetpr sicsescgpg frkslpegkv
      541 sccfdcvpcp eneisnetdv dqcmqcldhq yantaqnhcl qksmtfldye dpmgislsci
      601 alcfsaltsl vlsiflkqkn tpivkannrt ltyillialn fcflcsflfi ghpntatcil
      661 qqttfavvft vavstvlakt itvvlafkvt apgrrirwll vtrapnfivp ictliqiilc
      721 gvwlgnsppf idtdtrsehe hiiimcnkgs vtafycvqgy lgalalgsft laflarnlpd
      781 tfneakfltf smlvfcsvwv tflpvyhstk gkhmvvvevf silvssagll gcifapkcyi
      841 illrpqrnsi qghrdkihyn ykts
//
LOCUS       NP_001092982             847 aa            linear   ROD 03-APR-2025
DEFINITION  vomeronasal 2 receptor 43 precursor [Rattus norvegicus].
ACCESSION   NP_001092982 XP_001053623
VERSION     NP_001092982.1
DBSOURCE    REFSEQ: accession NM_001099512.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Aug 15, 2007 this sequence version replaced XP_001053623.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..847
                     /product="vomeronasal 2 receptor 43 precursor"
                     /calculated_mol_wt=94321
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2431
     Region          43..501
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,166..167,391)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Region          511..562
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          582..833
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          582..607
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(585,588..589,592..593,595..596,630,634,637..638,646,
                     650)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          619..640
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(639,651..652,655..656,659,739,744,747..748,751,785,
                     788..789,792,796,804..805,808,811,815)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          649..673
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          697..713
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          740..766
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          774..797
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          802..827
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..847
                     /gene="Vom2r43"
                     /coded_by="NM_001099512.1:1..2544"
                     /db_xref="GeneID:679593"
                     /db_xref="RGD:1587090"
ORIGIN      
        1 midmfslilv llflkasllf ctlndpkcfl rikdkknvdg dkevdcffsi yakhghvknd
       61 ffsgnldkql ttknihlils lyfsieeins tpqvlpnisl lvkiecnlla drskislssr
      121 kgdyfpnfdc rnqrrylivf tgpmwfptam lgpllyisrt pelyygpfhp llntyeqfpy
      181 lyqmaikdts iaigmvtlvi yfswnwvglm isdddlglqf aselreemqr ydiclafvtv
      241 itynsklflt magmyynqii mslakvviiy gdidsflqvi frlwqfvdir riwiatsqwd
      301 iitsngeflf nsfhgtlsfs hhyseisgfk efiqtvypln ysntispakl wwvnfncfwp
      361 ssnckklkkc srkmllkwls nnqfemamse tnynlynavy avahslheli lqqantlsnn
      421 vekelefdsl qvlsslkkiq fvnpagdlvn lnqkenlnvd ydifytgdfl qsygikvkig
      481 nffkyltqpq kllmfdemvd watdirqtlp sicstpcnpg frkspqegka vccfdcnpcp
      541 eneisnmtdm dycykcldnq yansegthcl sktviflsye dpigvtlacl alcfsaltav
      601 vfgiflrnqd tlivkannra lsycllisli ycflcsllfi gkphmvtcim qqtifavaft
      661 vavstvlskt itvvlafkft lpskkmrwlm tsgtsvliip ictmiqliic giwlgtyppy
      721 vdsdghiehg hilivcnkgs vtafycvlgy lgsialasft vaflarnlpd tfneakfltf
      781 smlvfcsvwl tflpvyhsts gkalvivevf ciltstagll icifapkcyi illtpknnsf
      841 htfrhkc
//
LOCUS       NP_001178943             245 aa            linear   ROD 03-APR-2025
DEFINITION  homeobox protein notochord [Rattus norvegicus].
ACCESSION   NP_001178943 XP_578357
VERSION     NP_001178943.1
DBSOURCE    REFSEQ: accession NM_001192014.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Alten,L., Schuster-Gossler,K., Beckers,A., Groos,S., Ulmer,B.,
            Hegermann,J., Ochs,M. and Gossler,A.
  TITLE     Differential regulation of node formation, nodal ciliogenesis and
            cilia positioning by Noto and Foxj1
  JOURNAL   Development 139 (7), 1276-1284 (2012)
   PUBMED   22357932
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Vidigal,J.A., Morkel,M., Wittler,L., Brouwer-Lehmitz,A., Grote,P.,
            Macura,K. and Herrmann,B.G.
  TITLE     An inducible RNA interference system for the functional dissection
            of mouse embryogenesis
  JOURNAL   Nucleic Acids Res 38 (11), e122 (2010)
   PUBMED   20350929
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Zizic Mitrecic,M., Mitrecic,D., Pochet,R., Kostovic-Knezevic,L. and
            Gajovic,S.
  TITLE     The mouse gene Noto is expressed in the tail bud and essential for
            its morphogenesis
  JOURNAL   Cells Tissues Organs 192 (2), 85-92 (2010)
   PUBMED   20197654
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Beckers,A., Alten,L., Viebahn,C., Andre,P. and Gossler,A.
  TITLE     The mouse homeobox gene Noto regulates node morphogenesis,
            notochordal ciliogenesis, and left right patterning
  JOURNAL   Proc Natl Acad Sci U S A 104 (40), 15765-15770 (2007)
   PUBMED   17884984
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2007 Oct 30;104(44):17554]
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Abdelkhalek,H.B., Beckers,A., Schuster-Gossler,K., Pavlova,M.N.,
            Burkhardt,H., Lickert,H., Rossant,J., Reinhardt,R., Schalkwyk,L.C.,
            Muller,I., Herrmann,B.G., Ceolin,M., Rivera-Pomar,R. and Gossler,A.
  TITLE     The mouse homeobox gene Not is required for caudal notochord
            development and affected by the truncate mutation
  JOURNAL   Genes Dev 18 (14), 1725-1736 (2004)
   PUBMED   15231714
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Mitrecic,D., Kostovic-Knezevic,L. and Gajovic,S.
  TITLE     Morphological features of tail bud development in truncate mouse
            mutants
  JOURNAL   Cells Tissues Organs 178 (1), 23-32 (2004)
   PUBMED   15550757
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Dietrich,S., Schubert,F.R. and Gruss,P.
  TITLE     Altered Pax gene expression in murine notochord mutants: the
            notochord is required to initiate and maintain ventral identity in
            the somite
  JOURNAL   Mech Dev 44 (2-3), 189-207 (1993)
   PUBMED   8155581
REFERENCE   8  (residues 1 to 245)
  AUTHORS   THEILER,K.
  TITLE     Anatomy and development of the 'truncate' (boneless) mutation in
            the mouse
  JOURNAL   Am J Anat 104, 319-343 (1959)
   PUBMED   13837681
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_578357.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389,
                              SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..245
                     /product="homeobox protein notochord"
                     /note="notochord homolog"
                     /calculated_mol_wt=26813
     Region          155..211
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..245
                     /gene="Noto"
                     /gene_synonym="RGD1562910"
                     /coded_by="NM_001192014.1:1..738"
                     /db_xref="GeneID:502857"
                     /db_xref="RGD:1562910"
ORIGIN      
        1 msspvpqpas sgtqvqpgdl gpcpvavspv vpnhlargrl essfsveail arpetrehsa
       61 tslplstcts lnfgsvsqyq vlpwvcstgt wlptylsvgi ypmcsmscmp glnvthlfcq
      121 qglrltgsel psclgplkra ptvnlqdhnt erhqkrvrtm fseqqlgele kvfakqhnlv
      181 gkeraqlaar lhltenqvri wfqnrrvkyq kqqklksppp dameepsnss egnvrnedae
      241 agvgs
//
LOCUS       NP_001099806             232 aa            linear   ROD 03-APR-2025
DEFINITION  membrane-spanning 4-domains subfamily A member 10 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001099806 XP_001074991 XP_215198
VERSION     NP_001099806.1
DBSOURCE    REFSEQ: accession NM_001106336.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473953.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001074991.1, XP_215198.1.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..232
                     /product="membrane-spanning 4-domains subfamily A member
                     10 isoform 2"
                     /note="membrane-spanning 4-domains, subfamily A, member
                     10"
                     /calculated_mol_wt=25357
     Region          57..190
                     /region_name="CD20"
                     /note="CD20-like family; pfam04103"
                     /db_xref="CDD:461174"
     CDS             1..232
                     /gene="Ms4a10"
                     /coded_by="NM_001106336.1:81..779"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293739"
                     /db_xref="RGD:1307478"
ORIGIN      
        1 msrqvptvta ssaigqasqw qspgpsqpaq kvaqpqhlvp dgylekpmeg sgllqklggf
       61 hiaiafahlt fggylistvk nlhlvvlkcw yplwgavsfl isgilatttv tfpktslkil
      121 cvvanvislf calagffvia kdlflenpfp wpiwrpypnp tsyiqrlelt llcftfleif
      181 lsastaitac rmkrphaedk ddtplipdtp melkglslgp ppsykdvtqd kd
//
LOCUS       NP_001100631             210 aa            linear   ROD 03-APR-2025
DEFINITION  uncharacterized protein MISP3 [Rattus norvegicus].
ACCESSION   NP_001100631 XP_001072269 XP_222453
VERSION     NP_001100631.1
DBSOURCE    REFSEQ: accession NM_001107161.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001072269.1, XP_222453.4.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..210
                     /product="uncharacterized protein MISP3"
                     /calculated_mol_wt=23359
     Region          37..200
                     /region_name="AKAP2_C"
                     /note="A-kinase anchor protein 2 C-terminus; pfam15304"
                     /db_xref="CDD:464630"
     CDS             1..210
                     /gene="Misp3"
                     /gene_synonym="RGD1310262"
                     /coded_by="NM_001107161.1:145..777"
                     /db_xref="GeneID:304650"
                     /db_xref="RGD:1310262"
ORIGIN      
        1 metpiqreir rscereeslr rsrglspgra geelielrvr pvlsrpgsgi plpralerar
       61 agakmqrdie reahrqaala spavpepsar prpqpldelk rffeaaaedg aslqrqpeag
      121 grlhpalqdg cpvlgqlppl vapslleqev lrvrererel qlqrrsiyga aedrepapsl
      181 tqsrgdgkla vtwpprrqas englekerrp
//
LOCUS       NP_001099819             231 aa            linear   ROD 03-APR-2025
DEFINITION  tumor protein D55 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099819 XP_001079669 XP_219798
VERSION     NP_001099819.1
DBSOURCE    REFSEQ: accession NM_001106349.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473953.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_219798.4, XP_001079669.1.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..231
                     /product="tumor protein D55 isoform 1"
                     /note="tumor protein D55; tumor protein D55-like; tumor
                     protein D52-like 3"
                     /calculated_mol_wt=24680
     Region          78..176
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..231
                     /gene="Tpd52l3"
                     /gene_synonym="RGD1309391; Trpd52l3"
                     /coded_by="NM_001106349.1:79..774"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293894"
                     /db_xref="RGD:1309391"
ORIGIN      
        1 mdpshleshp sgqksepagl dvsstspncf ssnqgldsvy qeldldslne dlslsvsdam
       61 tetsastnef hlasepdlte aeqmelrsel tkleeeilsl rdllaakekr cgelkrklgc
      121 valvglrqnl skswhdvqas ntymkqktst alasmgsaic rklgdmkkss tfksleelvg
      181 tvksrvaggr elgsgllpsp asgsdphsvl gsgyetvsgl ddqlfsllkp e
//
LOCUS       NP_001100842             480 aa            linear   ROD 03-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNG2 [Rattus
            norvegicus].
ACCESSION   NP_001100842 XP_001058122 XP_225718
VERSION     NP_001100842.1
DBSOURCE    REFSEQ: accession NM_001107372.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhu,X.R., Netzer,R., Bohlke,K., Liu,Q. and Pongs,O.
  TITLE     Structural and functional characterization of Kv6.2 a new
            gamma-subunit of voltage-gated potassium channel
  JOURNAL   Recept Channels 6 (5), 337-350 (1999)
   PUBMED   10551266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH474021.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001058122.1, XP_225718.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132296,
                              SAMD00132297 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..480
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNG2"
                     /note="cardiac potassium channel subunit (Kv6.2);
                     voltage-gated potassium channel subunit Kv6.2; potassium
                     voltage-gated channel, subfamily G, member 2; potassium
                     channel, voltage gated modifier subfamily G, member 2"
                     /calculated_mol_wt=52405
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          33..127
                     /region_name="BTB_POZ_Kv6_KCNG"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in KCNG/Kv6
                     subfamily of potassium voltage-gated channels; cd18382"
                     /db_xref="CDD:349691"
     Site            order(36,38..45,48,84,86..87,90,93,97,100,103,105,
                     113..114,117)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349691"
     Region          144..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            188..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          190..429
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            231..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            333..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          382..387
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            397..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          429..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     CDS             1..480
                     /gene="Kcng2"
                     /gene_synonym="Kv6.2"
                     /coded_by="NM_001107372.1:160..1602"
                     /db_xref="GeneID:307234"
                     /db_xref="RGD:1309521"
ORIGIN      
        1 marlpghpev pgaepgsavr ggrggrgara rhviinvggc rvrlawaala rcplarlerl
       61 racrghdell rvcddydvsr defffdrspc afraivallr agklrllrgp calafrdela
      121 ywgidearle rcclrrlrrr eeeaaearat ppargpqtsp gralgsgrle rgrrrlrdvv
      181 enphsglagk lfayvsvafv avtavglcls tmpdvraeee rgecstkcrn lfvletvcva
      241 wfsfefllrs lqaeskcafl rtplaiidil ailpfyvsll aglaagptgs kmleraglvl
      301 rllralrvly vmrlarhslg lrslgltvrr carefgllll flcvamalfa plvhlaerel
      361 gahrdfssvp asywwavism ttvgygdmvp rslpgqvval ssilsgillm afpvtsifht
      421 fsrsyselke qqqraaspep vlredstrdd strsasated ssqdpetaga agslpgpvgp
//
LOCUS       NP_001099833            1638 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001099833 XP_001065637 XP_215259
VERSION     NP_001099833.1
DBSOURCE    REFSEQ: accession NM_001106363.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1638)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215259.4, XP_001065637.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.6317.1,
                                           SRR26643296.4637.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1638
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1638
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 2"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174872
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <977..1361
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1515..1605
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1638
                     /gene="Pprc1"
                     /coded_by="NM_001106363.2:30..4946"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgsidtpqek kpldrlhape
     1201 lanvagltpp atpphqlwkp laavsllaka kspkstaqeg tlkpegitea kppaaaclqe
     1261 gvrgpspvhv gsgdhdycvr srtppkkmpa lvisemgsrw nvkrhqditi kpvlslgsaa
     1321 pplpctttsq epldhrtsse qadpsapcfa pstllspeas pcrnemntrt pseppdkqrs
     1381 mrcyrkacrs asppsrgwqg rrgrssrsvs sgssrtseas ssssvssssr srsrslsppn
     1441 krwrrsscss sgrsrrcsss ssssssssss sssrsrspsv spcrrsdrrr ryssyrsndh
     1501 yqrqrvlqke raieerrvvf igkipgrmtr selkqrfsvf geieectihf rvqgdnygfv
     1561 tyryaeeafa aiesghklrq adeqpfdlcf ggrrqfckrs ysdldsnred fdpapvkskf
     1621 dsldfdtllk qaqknlrr
//
LOCUS       NP_001424483            1634 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424483 XP_063143273
VERSION     NP_001424483.1
DBSOURCE    REFSEQ: accession NM_001437554.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1634)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143273.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.192428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1634
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1634
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 6"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174541
     Region          <375..840
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <627..1112
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <974..1357
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1511..1601
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1634
                     /gene="Pprc1"
                     /coded_by="NM_001437554.1:30..4934"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv emsladspwd fspppflets spklpswrss rprprwsqsp ppqqrsdgee
      241 eeevagfsgq mldgeldnsv ntldfpmhla cpeeedksga anvavsapgd esisslselv
      301 ramhpyclpn ltqlasldae lqeqaddltl pegcvvleiv gqaatagddl eipvvvrqip
      361 sgsqsvlldg svgtdpalql lmpamepgte dgvpkvapcp dqelplssac lleprdimes
      421 lapkeprnlp anasegsqrv prkgrkkkkk eqptaclegc trrlrsssrg qstvatevns
      481 qagnlqkqpq eelqretaap qsrgkprawa rawaaalekt gsedpedqna gqdspaeedv
      541 lelrpklvet sqadptlsln dsaradsipv nsvegdstav dtavpvdqas sctelvgsls
      601 ggpilsspvl ddrtgvepav aiptsnhlsp adailanpgt adpapnglap gdpvlvkcrp
      661 tdprraaaaa taaqgprpsl epsdhpkvit pevkdaggpl kvegstsatt qearprplsl
      721 seyrqrrrqr qieaedrnsq ppagkwpslp etpkgladip clvpsaptkk tapqrspiav
      781 petcsvsvgs npvsptpeps asklmvsths eqvsshempl pvrlppptlq smapagptps
      841 tvptplpfpp slppllplpa sgpgvpslpp pplqppglpv smrqmppdpy tqyapvppwp
      901 cypsvspsgy sclppppamp ivsgtpgtya vpptcnvpwv pppapvspys sssaygslgw
      961 gpglqqppfw stvsppplss astgravppp svepsnssag ppedtlpvpv tpslssrpas
     1021 piappaeptk leaqpvpvsp qpkhkvspvv qspqikvlpt lsaegvaige seserlkpet
     1081 qenrprekpi statkavllp kqstvaklpa vhparlrrls flptpraqgs edvvqafise
     1141 igieasdlss lleqfeksea kkecplpapa dsvavgnsgi dtpqekkpld rlhapelanv
     1201 agltppatpp hqlwkplaav sllakakspk staqegtlkp egiteakppa aaclqegvrg
     1261 pspvhvgsgd hdycvrsrtp pkkmpalvis emgsrwnvkr hqditikpvl slgsaapplp
     1321 ctttsqepld hrtsseqadp sapcfapstl lspeaspcrn emntrtpsep pdkqrsmrcy
     1381 rkacrsaspp srgwqgrrgr ssrsvssgss rtseasssss vssssrsrsr slsppnkrwr
     1441 rsscsssgrs rrcsssssss sssssssssr srspsvspcr rsdrrrryss yrsndhyqrq
     1501 rvlqkeraie errvvfigki pgrmtrselk qrfsvfgeie ectihfrvqg dnygfvtyry
     1561 aeeafaaies ghklrqadeq pfdlcfggrr qfckrsysdl dsnredfdpa pvkskfdsld
     1621 fdtllkqaqk nlrr
//
LOCUS       NP_001424498             376 aa            linear   ROD 04-APR-2025
DEFINITION  CST complex subunit STN1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424498 XP_006231536
VERSION     NP_001424498.1
DBSOURCE    REFSEQ: accession NM_001437569.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Iles,M.M., Bishop,D.T., Taylor,J.C., Hayward,N.K., Brossard,M.,
            Cust,A.E., Dunning,A.M., Lee,J.E., Moses,E.K., Akslen,L.A.,
            Andresen,P.A., Avril,M.F., Azizi,E., Scarra,G.B., Brown,K.M.,
            Debniak,T., Elder,D.E., Friedman,E., Ghiorzo,P., Gillanders,E.M.,
            Goldstein,A.M., Gruis,N.A., Hansson,J., Harland,M., Helsing,P.,
            Hocevar,M., Hoiom,V., Ingvar,C., Kanetsky,P.A., Landi,M.T.,
            Lang,J., Lathrop,G.M., Lubinski,J., Mackie,R.M., Martin,N.G.,
            Molven,A., Montgomery,G.W., Novakovic,S., Olsson,H., Puig,S.,
            Puig-Butille,J.A., Radford-Smith,G.L., Randerson-Moor,J., van der
            Stoep,N., van Doorn,R., Whiteman,D.C., MacGregor,S., Pooley,K.A.,
            Ward,S.V., Mann,G.J., Amos,C.I., Pharoah,P.D., Demenais,F.,
            Law,M.H., Newton Bishop,J.A. and Barrett,J.H.
  CONSRTM   AMFS Investigators; IBD investigators; QMEGA and QTWIN
            Investigators; SDH Study Group; GenoMEL Consortium
  TITLE     The effect on melanoma risk of genes previously associated with
            telomere length
  JOURNAL   J Natl Cancer Inst 106 (10) (2014)
   PUBMED   25231748
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006231536.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399492.762836.1,
                                           SRR26360190.690026.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..376
                     /product="CST complex subunit STN1 isoform 2"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; CST complex subunit STN1;
                     suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1;
                     STN1, CST complex subunit"
                     /calculated_mol_wt=43194
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          211..376
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     CDS             1..376
                     /gene="Stn1"
                     /gene_synonym="Obfc1"
                     /coded_by="NM_001437569.1:238..1368"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:294025"
                     /db_xref="RGD:1305637"
ORIGIN      
        1 mpepcllmqc esspkeeeip slfwgldpvf lafaklyikd ilemkesqqv pgmyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkrps naesssdpai lstsrelsmt
      121 sqlkklqeti eqktkigigd iirvrgyvrm freereicat iyykvddpvw nmqiarmlel
      181 pelykkvydq pfrnpalkee ealnkdtldl agltallsek vkeflqekkv qsfyqkelem
      241 veplqslasq pvthstcsdq velkndaasd ihsvfknalh llqekgfvfq rdggsdklyy
      301 vtskdkdlhq kiyqiikedc qkpnhvekgc hlmhvlncvl lnlrwdlnka vlqqvlelle
      361 dqsdivstgd hyytaf
//
LOCUS       NP_001424485            1373 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424485 XP_063143287
VERSION     NP_001424485.1
DBSOURCE    REFSEQ: accession NM_001437556.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1373)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143287.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.4653.1,
                                           SRR26360172.1522454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1373
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1373
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 8"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=146363
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1250..1340
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1373
                     /gene="Pprc1"
                     /coded_by="NM_001437556.1:30..4151"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgsscsssgr srrcssssss
     1201 ssssssssss rsrspsvspc rrsdrrrrsy rsndhyqrqr vlqkeraiee rrvvfigkip
     1261 grmtrselkq rfsvfgeiee ctihfrvqgd nygfvtyrya eeafaaiesg hklrqadeqp
     1321 fdlcfggrrq fckrsysdld snredfdpap vkskfdsldf dtllkqaqkn lrr
//
LOCUS       NP_001101804            2472 aa            linear   ROD 04-APR-2025
DEFINITION  nuclear receptor corepressor 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001101804 XP_001074041 XP_341073
VERSION     NP_001101804.1
DBSOURCE    REFSEQ: accession NM_001108334.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2472)
  AUTHORS   Barbieri,C.E., Bangma,C.H., Bjartell,A., Catto,J.W., Culig,Z.,
            Gronberg,H., Luo,J., Visakorpi,T. and Rubin,M.A.
  TITLE     The mutational landscape of prostate cancer
  JOURNAL   Eur Urol 64 (4), 567-576 (2013)
   PUBMED   23759327
  REMARK    Review article
REFERENCE   2  (residues 1 to 2472)
  AUTHORS   Yang,J. and Fuller,P.J.
  TITLE     Interactions of the mineralocorticoid receptor--within and without
  JOURNAL   Mol Cell Endocrinol 350 (2), 196-205 (2012)
   PUBMED   21784126
  REMARK    Review article
REFERENCE   3  (residues 1 to 2472)
  AUTHORS   Pei,L., Leblanc,M., Barish,G., Atkins,A., Nofsinger,R., Whyte,J.,
            Gold,D., He,M., Kawamura,K., Li,H.R., Downes,M., Yu,R.T.,
            Powell,H.C., Lingrel,J.B. and Evans,R.M.
  TITLE     Thyroid hormone receptor repression is linked to type I
            pneumocyte-associated respiratory distress syndrome
  JOURNAL   Nat Med 17 (11), 1466-1472 (2011)
   PUBMED   22001906
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2472)
  AUTHORS   Sircoulomb,F., Nicolas,N., Ferrari,A., Finetti,P., Bekhouche,I.,
            Rousselet,E., Lonigro,A., Adelaide,J., Baudelet,E., Esteyries,S.,
            Wicinski,J., Audebert,S., Charafe-Jauffret,E., Jacquemier,J.,
            Lopez,M., Borg,J.P., Sotiriou,C., Popovici,C., Bertucci,F.,
            Birnbaum,D., Chaffanet,M. and Ginestier,C.
  TITLE     ZNF703 gene amplification at 8p12 specifies luminal B breast cancer
  JOURNAL   EMBO Mol Med 3 (3), 153-166 (2011)
   PUBMED   21328542
  REMARK    Erratum:[EMBO Mol Med. 2011 Mar;3(3). doi:10.1002/emmm.201000121]
REFERENCE   5  (residues 1 to 2472)
  AUTHORS   Cui,J., Yang,Y., Zhang,C., Hu,P., Kan,W., Bai,X., Liu,X. and
            Song,H.
  TITLE     FBI-1 functions as a novel AR co-repressor in prostate cancer cells
  JOURNAL   Cell Mol Life Sci 68 (6), 1091-1103 (2011)
   PUBMED   20812024
REFERENCE   6  (residues 1 to 2472)
  AUTHORS   Martinez de Arrieta,C., Koibuchi,N. and Chin,W.W.
  TITLE     Coactivator and corepressor gene expression in rat cerebellum
            during postnatal development and the effect of altered thyroid
            status
  JOURNAL   Endocrinology 141 (5), 1693-1698 (2000)
   PUBMED   10803578
REFERENCE   7  (residues 1 to 2472)
  AUTHORS   Zhou,S., Fujimuro,M., Hsieh,J.J., Chen,L., Miyamoto,A.,
            Weinmaster,G. and Hayward,S.D.
  TITLE     SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
            domain of NotchIC To facilitate NotchIC function
  JOURNAL   Mol Cell Biol 20 (7), 2400-2410 (2000)
   PUBMED   10713164
REFERENCE   8  (residues 1 to 2472)
  AUTHORS   Park,E.J., Schroen,D.J., Yang,M., Li,H., Li,L. and Chen,J.D.
  TITLE     SMRTe, a silencing mediator for retinoid and thyroid hormone
            receptors-extended isoform that is more related to the nuclear
            receptor corepressor
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3519-3524 (1999)
   PUBMED   10097068
REFERENCE   9  (residues 1 to 2472)
  AUTHORS   Ordentlich,P., Downes,M., Xie,W., Genin,A., Spinner,N.B. and
            Evans,R.M.
  TITLE     Unique forms of human and mouse nuclear receptor corepressor SMRT
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2639-2644 (1999)
   PUBMED   10077563
REFERENCE   10 (residues 1 to 2472)
  AUTHORS   Misiti,S., Schomburg,L., Yen,P.M. and Chin,W.W.
  TITLE     Expression and hormonal regulation of coactivator and corepressor
            genes
  JOURNAL   Endocrinology 139 (5), 2493-2500 (1998)
   PUBMED   9564863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_341073.2, XP_001074041.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2472
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..2472
                     /product="nuclear receptor corepressor 2 isoform 2"
                     /note="nuclear receptor corepressor 2"
                     /calculated_mol_wt=269866
     Region          143..229
                     /region_name="GPS2_interact"
                     /note="G-protein pathway suppressor 2-interacting domain;
                     pfam15784"
                     /db_xref="CDD:464868"
     Region          <169..627
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          432..475
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(432,461..462,464..465,467..469,471..473)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          610..653
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Region          <1720..2224
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2472
                     /gene="Ncor2"
                     /coded_by="NM_001108334.2:330..7748"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360801"
                     /db_xref="RGD:1310293"
ORIGIN      
        1 msgstqpvaq twraaepryp phgisypvqi arphtdvgll eyqhhprdyt shlspgsiiq
       61 pqrrrpslls efqpgsersq elhlrpesrt flpelgkpdi efteskrprl ellpdtllrp
      121 apllatgqps gsedltkdrs lagklepvsp pspphadpel eltpsrlske eliqnmdrvd
      181 reitmveqqi sklkkkqqql eeeaakppep ekpvspppie skhrslvqii ydenrkkaea
      241 ahrileglgp qvelplynqp sdtrqyheni kinqamrkkl ilyfkrrnha rkqweqrfcq
      301 rydqlmeawe kkveriennp rrrakeskvr eyyekqfpei rkqrelqerm qsrvgqrgsg
      361 lsmsaarseh evseiidgls eqenlekqmr qlavippmly dadqqrikfi nmnglmddpm
      421 kvykdrqvtn mwseqerdtf rekfmqhpkn fgliasfler ktvaecvlyy yltkknenyk
      481 slvrrsyrrr gksqqqqqqq qqqqqqqmar ssqeekeeke kekeadkeee kqdaenekee
      541 lskektddts gedndekeav askgrktans qgrrkgritr smaneanhee tatpqqssel
      601 asmemnessr wteeemetak kgllehgrnw saiarmvgsk tvsqcknfyf nykkrqnlde
      661 ilqqhklkme kernarrkkk ktpaaaseet afppaaedee measgasane eelaeeaeas
      721 qasgnevprv gecsgpaavn nssdtesvps prteatkdag pkpastealp aatqppvppp
      781 eepatvpdep cpapdasgpp spvaspppaa ppaavdkdeq dqaatvpqte dakeqkseae
      841 elvidvgkte epeapeeppe svksdhkeet eeepedkakg peaietvsea plkveeagsk
      901 aavtkgsssg atqdsdssat csadevdepe ggdkgrllsp rpslltpagd prastspqkp
      961 ldlkqlkqra aaippivtkv heppredtvp pkpappvppp tqhlqpegdv sqqsggsprg
     1021 kcrspvppae keaekasffp afpaegpklp tepprwtsgl pfpipprevi ktsphaadps
     1081 afsytppghp lplglhdsar pvlprppisn ppplissakh pgvlerqlgt isqqgmsvql
     1141 rvphsehaka pmgpltmglp lavdpkklgt algstasgsi tkglpstrta dgpsyrgsit
     1201 hgtpadvlyk gtisrivged spsrldrare dtlpkghviy egkkghvlsy eggmsvsqcs
     1261 kedgrsssgp phetaapkrt ydmmegrvgr titsasiegl mgraipeqhs phlkeqhhir
     1321 gsitqgiprs yveaqedylr reakllkreg tppppppprd ltetyktrpl dplgplklkp
     1381 thegvvatvk eagrsiheip reelrrtpel plaprplkeg sitqgtplky dsgvpssgsk
     1441 khdvrsiigs pgrpfpalhp ldimadaral eracyeeslk srsgtssgag gsitrgapvv
     1501 vpelgkprqs playedhgap ftshlprgsp vttreptprl qegsllsska sqdrkltstp
     1561 reiaksphst vpehhphpis pyehllrgvt gvdlyrghip lafdptsipr gipleaaaaa
     1621 yylprhlaps ptyphlyppy lirgypdtaa lenrqtiind yitsqqmhhn aasamaqrad
     1681 mlrglspres slalnyaagp rgiidlsqvp hlpvlvpptp gtpataidrl aylptapppf
     1741 ssrhssspls pggpthlakp tatssserer erererdksi ltstttveha piwrpgteqs
     1801 sgaggssrpa shthqhspis prtqdalqqr psvlhntsmk gvvtsvepgt ptvlrwarst
     1861 stsspvrpaa tfppathcpl ggtlegvypt lmepvllpke tsrvtrperp rvdaghaflt
     1921 kpparepass psksseprsl appssshtai artpakslap hhaspdlpap tsasdlhrek
     1981 tqskpfsiqe lelrslgyhs gagyspdgve pispvsspsl thdkglskpl eelekshleg
     2041 elrhkqpgpm klsgeaahlp hlrplpesqp ssspllqtap gikghqrvvt laqhisevit
     2101 qdytrhhpqq lsgplpaply sfpgascpvl dlrrppsdly lpppdhgtpa rgsphseggk
     2161 rspepsktvl sssedaiepv sppegmtepg harstaypll yrdgeqgepr mgskspgnts
     2221 qppaffsklt esnsamvksk kqeinkklnt hnrnepeyni gqpgteifnm paitgaglmt
     2281 crsqavqeha stnmgleaii rkalmgkydq weeppplgan afnplnasas lpaaampitt
     2341 adgrsdhplt spggggkakv sgrpssrkak spapglapgd rppsvssvhs egdcnrrtpl
     2401 tnrvwedrps sagstpfpyn plimrlqagv masppppgla agsgplagph hawdeepkpl
     2461 lcsqyetlsd se
//
LOCUS       NP_001014057             495 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001014057 XP_226648
VERSION     NP_001014057.1
DBSOURCE    REFSEQ: accession NM_001014035.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 1, 2005 this sequence version replaced XP_226648.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.1300.1,
                                           SRR21887620.520416.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345329,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..495
                     /product="myocyte-specific enhancer factor 2A isoform 3"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=53138
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          97..154
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          <129..>372
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          175..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            213..214
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          242..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          266..283
                     /region_name="Required for interaction with MAPKs.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          382..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            395
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60929; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     CDS             1..495
                     /gene="Mef2a"
                     /coded_by="NM_001014035.3:311..1798"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivealnk kehrgcdspd pdtsyvltph teekykkine
      121 efdnmmrnhk iapglppqnf smsvtvpvts pnalsytnpg sslvspslaa sstlaessml
      181 spppatlhrn vspgapqrpp stgsaggmls ttdltvpnga gnspvgngfv nsraspnlig
      241 ntgansvgkv mptksppppg ggsvgmnsrk pdlrvvipps skgmmpplna qrisssqatq
      301 platpvvsvt tpslppqglv ysamptaynt dysltsadls alqgftspgm lslgqasawq
      361 qhhlgqaals slvaggqlsq gsnlsintnq niniksepis pprdrmtpsg fqqqqqqqpq
      421 qqpppqppqp qpqprqemgr spvdslssss ssydgsdred prgdfhspiv lgrppnaedr
      481 espsvkrmrm dtwvt
//
LOCUS       NP_001424487            1341 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 10 [Rattus norvegicus].
ACCESSION   NP_001424487 XP_063143291
VERSION     NP_001424487.1
DBSOURCE    REFSEQ: accession NM_001437558.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1341)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143291.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1356056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1341
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1341
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 10"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=143005
     Region          <344..809
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <596..1081
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1218..1308
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1341
                     /gene="Pprc1"
                     /coded_by="NM_001437558.1:30..4055"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspresssve msladspwdf spppfletss
      181 pklpswrssr prprwsqspp pqqrsdgeee eevagfsgqm ldgeldnsvn tldfpmhlac
      241 peeedksgaa nvavsapgde sisslselvr amhpyclpnl tqlasldael qeqaddltlp
      301 egcvvleivg qaatagddle ipvvvrqips gsqsvlldgs vgtdpalqll mpamepgted
      361 gvpkvapcpd qelplssacl leprdimesl apkeprnlpa nasegsqrvp rkgrkkkkke
      421 qptaclegct rrlrsssrgq stvatevnsq agnlqkqpqe elqretaapq srgkprawar
      481 awaaalektg sedpedqnag qdspaeedvl elrpklvets qadptlslnd saradsipvn
      541 svegdstavd tavpvdqass ctelvgslsg gpilsspvld drtgvepava iptsnhlspa
      601 dailanpgta dpapnglapg dpvlvkcrpt dprraaaaat aaqgprpsle psdhpkvitp
      661 evkdaggplk vegstsattq earprplsls eyrqrrrqrq ieaedrnsqp pagkwpslpe
      721 tpkgladipc lvpsaptkkt apqrspiavp etcsvsvgsn pvsptpepsa sklmvsthse
      781 qvsshemplp vrlppptlqs mapagptpst vptplpfpps lppllplpas gpgvpslppp
      841 plqppglpvs mrqmppdpyt qyapvppwpc ypsvspsgys clppppampi vsgtpgtyav
      901 pptcnvpwvp ppapvspyss ssaygslgwg pglqqppfws tvsppplssa stgravppps
      961 vepsnssagp pedtlpvpvt pslssrpasp iappaeptkl eaqpvpvspq pkhkvspvvq
     1021 spqikvlptl saegvaiges eserlkpetq enrprekpis tatkavllpk qstvaklpav
     1081 hparlrrlsf lptpraqgse dvvqafisei gieasdlssl leqfekseak kecplpapad
     1141 svavgnsgss csssgrsrrc ssssssssss ssssssrsrs psvspcrrsd rrrryssyrs
     1201 ndhyqrqrvl qkeraieerr vvfigkipgr mtrselkqrf svfgeieect ihfrvqgdny
     1261 gfvtyryaee afaaiesghk lrqadeqpfd lcfggrrqfc krsysdldsn redfdpapvk
     1321 skfdsldfdt llkqaqknlr r
//
LOCUS       NP_001424490            1364 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 13 [Rattus norvegicus].
ACCESSION   NP_001424490
VERSION     NP_001424490.1
DBSOURCE    REFSEQ: accession NM_001437561.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1364)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2351875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1364
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1364
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 13"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=145797
     Region          <367..832
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <619..1104
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1241..1331
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1364
                     /gene="Pprc1"
                     /coded_by="NM_001437561.1:10..4104"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 mstwllsqav ghlvsaleph crelgvsqpl ppslacagts glevheegdd ssfvslsrlg
       61 pslrekdlem eelilqdetl letmqnymda slisliedfg esrlsledqn emslltalte
      121 ildnadsenl spfdtipdse llvspresss lhkllnlsrt pperdripam dplgpsagss
      181 rvemsladsp wdfspppfle tsspklpswr ssrprprwsq spppqqrsdg eeeeevagfs
      241 gqmldgeldn svntldfpmh lacpeeedks gaanvavsap gdesisslse lvramhpycl
      301 pnltqlasld aelqeqaddl tlpegcvvle ivgqaatagd dleipvvvrq ipsgsqsvll
      361 dgsvgtdpal qllmpamepg tedgvpkvap cpdqelplss aclleprdim eslapkeprn
      421 lpanasegsq rvprkgrkkk kkeqptacle gctrrlrsss rgqstvatev nsqagnlqkq
      481 pqeelqreta apqsrgkpra warawaaale ktgsedpedq nagqdspaee dvlelrpklv
      541 etsqadptls lndsaradsi pvnsvegdst avdtavpvdq assctelvgs lsggpilssp
      601 vlddrtgvep avaiptsnhl spadailanp gtadpapngl apgdpvlvkc rptdprraaa
      661 aataaqgprp slepsdhpkv itpevkdagg plkvegstsa ttqearprpl slseyrqrrr
      721 qrqieaedrn sqppagkwps lpetpkglad ipclvpsapt kktapqrspi avpetcsvsv
      781 gsnpvsptpe psasklmvst hseqvsshem plpvrlpppt lqsmapagpt pstvptplpf
      841 ppslppllpl pasgpgvpsl pppplqppgl pvsmrqmppd pytqyapvpp wpcypsvsps
      901 gysclppppa mpivsgtpgt yavpptcnvp wvpppapvsp yssssaygsl gwgpglqqpp
      961 fwstvspppl ssastgravp ppsvepsnss agppedtlpv pvtpslssrp aspiappaep
     1021 tkleaqpvpv spqpkhkvsp vvqspqikvl ptlsaegvai geseserlkp etqenrprek
     1081 pistatkavl lpkqstvakl pavhparlrr lsflptpraq gsedvvqafi seigieasdl
     1141 sslleqfeks eakkecplpa padsvavgns gsscsssgrs rrcsssssss sssssssssr
     1201 srspsvspcr rsdrrrryss yrsndhyqrq rvlqkeraie errvvfigki pgrmtrselk
     1261 qrfsvfgeie ectihfrvqg dnygfvtyry aeeafaaies ghklrqadeq pfdlcfggrr
     1321 qfckrsysdl dsnredfdpa pvkskfdsld fdtllkqaqk nlrr
//
LOCUS       NP_001424481            1636 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424481 XP_063143262
VERSION     NP_001424481.1
DBSOURCE    REFSEQ: accession NM_001437552.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1636)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143262.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2257340.1,
                                           SRR26643296.4636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1636
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1636
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 4"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174622
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <977..1361
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1513..1603
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1636
                     /gene="Pprc1"
                     /coded_by="NM_001437552.1:30..4940"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgsidtpqek kpldrlhape
     1201 lanvagltpp atpphqlwkp laavsllaka kspkstaqeg tlkpegitea kppaaaclqe
     1261 gvrgpspvhv gsgdhdycvr srtppkkmpa lvisemgsrw nvkrhqditi kpvlslgsaa
     1321 pplpctttsq epldhrtsse qadpsapcfa pstllspeas pcrnemntrt pseppdkqrs
     1381 mrcyrkacrs asppsrgwqg rrgrssrsvs sgssrtseas ssssvssssr srsrslsppn
     1441 krwrrsscss sgrsrrcsss ssssssssss sssrsrspsv spcrrsdrrr rsyrsndhyq
     1501 rqrvlqkera ieerrvvfig kipgrmtrse lkqrfsvfge ieectihfrv qgdnygfvty
     1561 ryaeeafaai esghklrqad eqpfdlcfgg rrqfckrsys dldsnredfd papvkskfds
     1621 ldfdtllkqa qknlrr
//
LOCUS       NP_001424523             717 aa            linear   ROD 04-APR-2025
DEFINITION  epidermal growth factor receptor kinase substrate 8-like protein 1
            [Rattus norvegicus].
ACCESSION   NP_001424523 XP_038937422
VERSION     NP_001424523.1
DBSOURCE    REFSEQ: accession NM_001437594.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Kesti,T., Ruppelt,A., Wang,J.H., Liss,M., Wagner,R., Tasken,K. and
            Saksela,K.
  TITLE     Reciprocal regulation of SH3 and SH2 domain binding via tyrosine
            phosphorylation of a common site in CD3epsilon
  JOURNAL   J Immunol 179 (2), 878-885 (2007)
   PUBMED   17617578
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Offenhauser,N., Borgonovo,A., Disanza,A., Romano,P., Ponzanelli,I.,
            Iannolo,G., Di Fiore,P.P. and Scita,G.
  TITLE     The eps8 family of proteins links growth factor stimulation to
            actin reorganization generating functional redundancy in the
            Ras/Rac pathway
  JOURNAL   Mol Biol Cell 15 (1), 91-98 (2004)
   PUBMED   14565974
  REMARK    Erratum:[Mol Biol Cell. 2019 Sep 1;30(19):2535. doi:
            10.1091/mbc.E03-06-0427-corr. PMID: 31465253]
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Hori,K., Konno,D., Maruoka,H. and Sobue,K.
  TITLE     MALS is a binding partner of IRSp53 at cell-cell contacts
  JOURNAL   FEBS Lett 554 (1-2), 30-34 (2003)
   PUBMED   14596909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_038937422.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.811.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16093045,
                                           SAMN16093046 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..717
                     /product="epidermal growth factor receptor kinase
                     substrate 8-like protein 1"
                     /note="EPS8-like 1"
                     /calculated_mol_wt=79955
     Region          32..162
                     /region_name="PTB_EPS8"
                     /note="Epidermal growth factor receptor kinase substrate
                     (EPS8)-like Phosphotyrosine-binding (PTB) domain; cd01210"
                     /db_xref="CDD:269921"
     Site            order(39,118,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269921"
     Site            order(104..109,125,148,152)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269921"
     Region          482..534
                     /region_name="SH3_Eps8"
                     /note="Src Homology 3 domain of Epidermal growth factor
                     receptor kinase substrate 8 and similar proteins; cd11764"
                     /db_xref="CDD:212698"
     Site            order(482..487,489,492,495..497,504..509,511..519,
                     524..527,531..534)
                     /site_type="other"
                     /note="swapped dimer interface [polypeptide binding]"
                     /db_xref="CDD:212698"
     Site            order(489,493..495,512..514,516,525..526,528..531)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212698"
     Region          623..688
                     /region_name="SAM_EPS8-like"
                     /note="SAM domain of EPS8-like subfamily; cd09540"
                     /db_xref="CDD:188939"
     CDS             1..717
                     /gene="Eps8l1"
                     /coded_by="NM_001437594.1:777..2930"
                     /db_xref="GeneID:361503"
                     /db_xref="RGD:1311146"
ORIGIN      
        1 mstttgpeaa pkpsaksiye qrkrystvvm advsqyhvnh lvtfclgeed gvhtvedasr
       61 klavmdsqgr vwaqemllrv spghvtlldp vskeelesyp ldaivrcdav mprgrsrsll
      121 llvcqepera qpdvhffqgl llgaelired iqgalqnyrs grgerraaal ratqeelrrg
      181 aspaaetppl qrrpsvravi ntvepsavrg rpqvepipet eearkpdpar tttrssdpts
      241 pdlgprgpel aglqaerdvd ilnhvfddve sfvsrlqksa eatrvlehre rgrrtrrraa
      301 geglltlrak ppteaeytdv lqkikyafsl larlrgnian psspellhfl fgplqmivnt
      361 sggpefprsv rrphltleav allrdnvtpr enelwtslgd swtrpgvelp peegspyspe
      421 fysgweppat dpqgrpwedp vekqlqhekr rrqqsapqva vnghqdpele tesqleekar
      481 kwvlcnydfq arngselsvk hrdvlevldd rrkwwkvrdh qgqegyvpyn iltphpgpqv
      541 hcsqssainl etsppppppa aapaptqvrp qwdscdslns ldpsdkekfs qmlcvneelq
      601 arlaqgrsgp srvtpglrap epqlsprsea svvrawlqtk gfssgtvdal gvltgaqlfs
      661 lqkeelrsvc peegarvysq vtvqralled rekvseleav mekqkkkveg etktevi
//
LOCUS       NP_001424510             493 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424510 XP_063121687
VERSION     NP_001424510.1
DBSOURCE    REFSEQ: accession NM_001437581.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063121687.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.1519516.1,
                                           SRR26643429.2185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..493
                     /product="myocyte-specific enhancer factor 2A isoform 4"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=52768
     Region          1..>235
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          <125..>370
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..493
                     /gene="Mef2a"
                     /coded_by="NM_001437581.1:258..1739"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivetlrk kglngcespd addyfehspl sedrfsklne
      121 dsdfifkrgp pglppqnfsm svtvpvtspn alsytnpgss lvspslaass tlaessmlsp
      181 ppatlhrnvs pgapqrppst gsaggmlstt dltvpngagn spvgngfvns raspnlignt
      241 gansvgkvmp tksppppggg svgmnsrkpd lrvvippssk gmmpplnaqr isssqatqpl
      301 atpvvsvttp slppqglvys amptayntdy sltsadlsal qgftspgmls lgqasawqqh
      361 hlgqaalssl vaggqlsqgs nlsintnqni niksepispp rdrmtpsgfq qqqqqqpqqq
      421 pppqppqpqp qprqemgrsp vdslssssss ydgsdredpr gdfhspivlg rppnaedres
      481 psvkrmrmdt wvt
//
LOCUS       NP_001424486            1372 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424486 XP_063143289
VERSION     NP_001424486.1
DBSOURCE    REFSEQ: accession NM_001437557.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1372)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143289.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1038786.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1372
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1372
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 9"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=146370
     Region          <375..840
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <627..1112
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1249..1339
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1372
                     /gene="Pprc1"
                     /coded_by="NM_001437557.1:30..4148"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv emsladspwd fspppflets spklpswrss rprprwsqsp ppqqrsdgee
      241 eeevagfsgq mldgeldnsv ntldfpmhla cpeeedksga anvavsapgd esisslselv
      301 ramhpyclpn ltqlasldae lqeqaddltl pegcvvleiv gqaatagddl eipvvvrqip
      361 sgsqsvlldg svgtdpalql lmpamepgte dgvpkvapcp dqelplssac lleprdimes
      421 lapkeprnlp anasegsqrv prkgrkkkkk eqptaclegc trrlrsssrg qstvatevns
      481 qagnlqkqpq eelqretaap qsrgkprawa rawaaalekt gsedpedqna gqdspaeedv
      541 lelrpklvet sqadptlsln dsaradsipv nsvegdstav dtavpvdqas sctelvgsls
      601 ggpilsspvl ddrtgvepav aiptsnhlsp adailanpgt adpapnglap gdpvlvkcrp
      661 tdprraaaaa taaqgprpsl epsdhpkvit pevkdaggpl kvegstsatt qearprplsl
      721 seyrqrrrqr qieaedrnsq ppagkwpslp etpkgladip clvpsaptkk tapqrspiav
      781 petcsvsvgs npvsptpeps asklmvsths eqvsshempl pvrlppptlq smapagptps
      841 tvptplpfpp slppllplpa sgpgvpslpp pplqppglpv smrqmppdpy tqyapvppwp
      901 cypsvspsgy sclppppamp ivsgtpgtya vpptcnvpwv pppapvspys sssaygslgw
      961 gpglqqppfw stvsppplss astgravppp svepsnssag ppedtlpvpv tpslssrpas
     1021 piappaeptk leaqpvpvsp qpkhkvspvv qspqikvlpt lsaegvaige seserlkpet
     1081 qenrprekpi statkavllp kqstvaklpa vhparlrrls flptpraqgs edvvqafise
     1141 igieasdlss lleqfeksea kkecplpapa dsvavgnsgs scsssgrsrr csssssssss
     1201 sssssssrsr spsvspcrrs drrrryssyr sndhyqrqrv lqkeraieer rvvfigkipg
     1261 rmtrselkqr fsvfgeieec tihfrvqgdn ygfvtyryae eafaaiesgh klrqadeqpf
     1321 dlcfggrrqf ckrsysdlds nredfdpapv kskfdsldfd tllkqaqknl rr
//
LOCUS       NP_001424508             495 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424508 XP_063121676
VERSION     NP_001424508.1
DBSOURCE    REFSEQ: accession NM_001437579.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063121676.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.2697796.1,
                                           SRR26360190.448937.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..495
                     /product="myocyte-specific enhancer factor 2A isoform 3"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=53138
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          97..154
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          <129..>372
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          175..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            213..214
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          242..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          266..283
                     /region_name="Required for interaction with MAPKs.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          382..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            395
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60929; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     CDS             1..495
                     /gene="Mef2a"
                     /coded_by="NM_001437579.1:463..1950"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivealnk kehrgcdspd pdtsyvltph teekykkine
      121 efdnmmrnhk iapglppqnf smsvtvpvts pnalsytnpg sslvspslaa sstlaessml
      181 spppatlhrn vspgapqrpp stgsaggmls ttdltvpnga gnspvgngfv nsraspnlig
      241 ntgansvgkv mptksppppg ggsvgmnsrk pdlrvvipps skgmmpplna qrisssqatq
      301 platpvvsvt tpslppqglv ysamptaynt dysltsadls alqgftspgm lslgqasawq
      361 qhhlgqaals slvaggqlsq gsnlsintnq niniksepis pprdrmtpsg fqqqqqqqpq
      421 qqpppqppqp qpqprqemgr spvdslssss ssydgsdred prgdfhspiv lgrppnaedr
      481 espsvkrmrm dtwvt
//
LOCUS       NP_001424520             717 aa            linear   ROD 04-APR-2025
DEFINITION  epidermal growth factor receptor kinase substrate 8-like protein 1
            [Rattus norvegicus].
ACCESSION   NP_001424520 XP_006228342
VERSION     NP_001424520.1
DBSOURCE    REFSEQ: accession NM_001437591.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Kesti,T., Ruppelt,A., Wang,J.H., Liss,M., Wagner,R., Tasken,K. and
            Saksela,K.
  TITLE     Reciprocal regulation of SH3 and SH2 domain binding via tyrosine
            phosphorylation of a common site in CD3epsilon
  JOURNAL   J Immunol 179 (2), 878-885 (2007)
   PUBMED   17617578
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Offenhauser,N., Borgonovo,A., Disanza,A., Romano,P., Ponzanelli,I.,
            Iannolo,G., Di Fiore,P.P. and Scita,G.
  TITLE     The eps8 family of proteins links growth factor stimulation to
            actin reorganization generating functional redundancy in the
            Ras/Rac pathway
  JOURNAL   Mol Biol Cell 15 (1), 91-98 (2004)
   PUBMED   14565974
  REMARK    Erratum:[Mol Biol Cell. 2019 Sep 1;30(19):2535. doi:
            10.1091/mbc.E03-06-0427-corr. PMID: 31465253]
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Hori,K., Konno,D., Maruoka,H. and Sobue,K.
  TITLE     MALS is a binding partner of IRSp53 at cell-cell contacts
  JOURNAL   FEBS Lett 554 (1-2), 30-34 (2003)
   PUBMED   14596909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006228342.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.800.1,
                                           SRR26643299.1163.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..717
                     /product="epidermal growth factor receptor kinase
                     substrate 8-like protein 1"
                     /note="EPS8-like 1"
                     /calculated_mol_wt=79955
     Region          32..162
                     /region_name="PTB_EPS8"
                     /note="Epidermal growth factor receptor kinase substrate
                     (EPS8)-like Phosphotyrosine-binding (PTB) domain; cd01210"
                     /db_xref="CDD:269921"
     Site            order(39,118,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269921"
     Site            order(104..109,125,148,152)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269921"
     Region          482..534
                     /region_name="SH3_Eps8"
                     /note="Src Homology 3 domain of Epidermal growth factor
                     receptor kinase substrate 8 and similar proteins; cd11764"
                     /db_xref="CDD:212698"
     Site            order(482..487,489,492,495..497,504..509,511..519,
                     524..527,531..534)
                     /site_type="other"
                     /note="swapped dimer interface [polypeptide binding]"
                     /db_xref="CDD:212698"
     Site            order(489,493..495,512..514,516,525..526,528..531)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212698"
     Region          623..688
                     /region_name="SAM_EPS8-like"
                     /note="SAM domain of EPS8-like subfamily; cd09540"
                     /db_xref="CDD:188939"
     CDS             1..717
                     /gene="Eps8l1"
                     /coded_by="NM_001437591.1:161..2314"
                     /db_xref="GeneID:361503"
                     /db_xref="RGD:1311146"
ORIGIN      
        1 mstttgpeaa pkpsaksiye qrkrystvvm advsqyhvnh lvtfclgeed gvhtvedasr
       61 klavmdsqgr vwaqemllrv spghvtlldp vskeelesyp ldaivrcdav mprgrsrsll
      121 llvcqepera qpdvhffqgl llgaelired iqgalqnyrs grgerraaal ratqeelrrg
      181 aspaaetppl qrrpsvravi ntvepsavrg rpqvepipet eearkpdpar tttrssdpts
      241 pdlgprgpel aglqaerdvd ilnhvfddve sfvsrlqksa eatrvlehre rgrrtrrraa
      301 geglltlrak ppteaeytdv lqkikyafsl larlrgnian psspellhfl fgplqmivnt
      361 sggpefprsv rrphltleav allrdnvtpr enelwtslgd swtrpgvelp peegspyspe
      421 fysgweppat dpqgrpwedp vekqlqhekr rrqqsapqva vnghqdpele tesqleekar
      481 kwvlcnydfq arngselsvk hrdvlevldd rrkwwkvrdh qgqegyvpyn iltphpgpqv
      541 hcsqssainl etsppppppa aapaptqvrp qwdscdslns ldpsdkekfs qmlcvneelq
      601 arlaqgrsgp srvtpglrap epqlsprsea svvrawlqtk gfssgtvdal gvltgaqlfs
      661 lqkeelrsvc peegarvysq vtvqralled rekvseleav mekqkkkveg etktevi
//
LOCUS       NP_001424527             588 aa            linear   ROD 04-APR-2025
DEFINITION  myeloid zinc finger 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424527
VERSION     NP_001424527.1
DBSOURCE    REFSEQ: accession NM_001437598.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Xing,F., Gu,H., Niu,Q., Fan,X., Wang,Z., Yuan,J., Li,Z., Xu,J.T.
            and Zhang,W.
  TITLE     MZF1 in the Dorsal Root Ganglia Contributes to the Development and
            Maintenance of Neuropathic Pain via Regulation of TRPV1
  JOURNAL   Neural Plast 2019, 2782417 (2019)
   PUBMED   31582966
  REMARK    GeneRIF: that MZF1 may contribute to neuropathic pain via
            regulation of TRPV1 expression in dorsal root ganglions
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Li,Z., Gu,X., Sun,L., Wu,S., Liang,L., Cao,J., Lutz,B.M.,
            Bekker,A., Zhang,W. and Tao,Y.X.
  TITLE     Dorsal root ganglion myeloid zinc finger protein 1 contributes to
            neuropathic pain after peripheral nerve trauma
  JOURNAL   Pain 156 (4), 711-721 (2015)
   PUBMED   25630025
  REMARK    GeneRIF: This study demonstrated that MZF1 participated in
            CCI-induced reductions in Kv1.2 mRNA and protein and total Kv
            current and the CCI-induced increase in neuronal excitability
            through MZF1-triggered Kv1.2
            Erratum:[Pain. 2022 Feb 1;163(2):e384. doi:
            10.1097/j.pain.0000000000002563. PMID: 35029603]
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Peterson,F.C., Hayes,P.L., Waltner,J.K., Heisner,A.K., Jensen,D.R.,
            Sander,T.L. and Volkman,B.F.
  TITLE     Structure of the SCAN domain from the tumor suppressor protein MZF1
  JOURNAL   J Mol Biol 363 (1), 137-147 (2006)
   PUBMED   16950398
  REMARK    Erratum:[J Mol Biol. 2007 Feb 9;366(1):346]
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Le Mee,S., Fromigue,O. and Marie,P.J.
  TITLE     Sp1/Sp3 and the myeloid zinc finger gene MZF1 regulate the human
            N-cadherin promoter in osteoblasts
  JOURNAL   Exp Cell Res 302 (1), 129-142 (2005)
   PUBMED   15541732
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Morris,J.F., Rauscher,F.J. 3rd, Davis,B., Klemsz,M., Xu,D.,
            Tenen,D. and Hromas,R.
  TITLE     The myeloid zinc finger gene, MZF-1, regulates the CD34 promoter in
            vitro
  JOURNAL   Blood 86 (10), 3640-3647 (1995)
   PUBMED   7579328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.2568867.1,
                                           SRR26360176.1307292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676810 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..588
                     /product="myeloid zinc finger 1 isoform 2"
                     /note="zinc finger protein 98"
                     /calculated_mol_wt=65960
     Region          211..570
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          212..232
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(217,219,221,223..224,227..228,231,245,247,251..252,
                     255..256,259,273,275,277,279..280,283..284,287)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          240..260
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          369..389
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          397..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(402,404,406,408..409,412..413,416,430,432,436..437,
                     440..441,444,458,460,462,464..465,468..469,472)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          425..445
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..473
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..501
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(486,488,490,492..493,496..497,500,514,516,520..521,
                     524..525,528,542,544,546,548..549,552..553,556)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          509..529
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          537..557
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          565..585
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..588
                     /gene="Mzf1"
                     /gene_synonym="Zfp98"
                     /coded_by="NM_001437598.1:1027..2793"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361508"
                     /db_xref="RGD:1308391"
ORIGIN      
        1 mepssfqprp qvklqtpeag settpgatqe lpldlqmkee telmenpell eseplsaaqe
       61 aaatllpkva qghgialdqt sphsdtepdv ppwsedpmpl wheevegils pgftlqmdsi
      121 taepdtvsph lhvpwdldma slsgqmqspt reggfahalv lpsdpgseqd pacedpcpsv
      181 gpalvatrwh aprdrsqghp stgtgvmrgg rcdvcgkvfs qrsnllrhqk ihtgerpfvc
      241 gecgrsfsrs shllrhqlth teerpfvcrd cgqgfvrsar leehrrvhtg eqpfrcaecg
      301 qsfrqrsnll qhqrihgdpp gpappvrsla gvpeppgpfp cseccesfpr ravllehqav
      361 htgdksfgcv ecgerfgrrs vllqhrrvhs gerpfacaec gqsfrqrsnl tqhrrihtge
      421 rpfactecgk afrqrptltq hlrvhtgekp facpecgqrf sqrlkltrhq rthtgekpyr
      481 csecglgftq vsrltehqri htgerpfacp ecgqsfrqha nliqhrriht gerpyacpec
      541 gkafrqrptl tqhlrthrre kpfacqdcgr rfhqstkliq hqrihste
//
LOCUS       NP_001424482            1635 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424482 XP_063143268
VERSION     NP_001424482.1
DBSOURCE    REFSEQ: accession NM_001437553.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1635)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143268.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.6226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1635
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1635
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 5"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174534
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <977..1360
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1512..1602
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1635
                     /gene="Pprc1"
                     /coded_by="NM_001437553.1:30..4937"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgidtpqekk pldrlhapel
     1201 anvagltppa tpphqlwkpl aavsllakak spkstaqegt lkpegiteak ppaaaclqeg
     1261 vrgpspvhvg sgdhdycvrs rtppkkmpal visemgsrwn vkrhqditik pvlslgsaap
     1321 plpctttsqe pldhrtsseq adpsapcfap stllspeasp crnemntrtp seppdkqrsm
     1381 rcyrkacrsa sppsrgwqgr rgrssrsvss gssrtseass sssvssssrs rsrslsppnk
     1441 rwrrsscsss grsrrcssss ssssssssss ssrsrspsvs pcrrsdrrrr syrsndhyqr
     1501 qrvlqkerai eerrvvfigk ipgrmtrsel kqrfsvfgei eectihfrvq gdnygfvtyr
     1561 yaeeafaaie sghklrqade qpfdlcfggr rqfckrsysd ldsnredfdp apvkskfdsl
     1621 dfdtllkqaq knlrr
//
LOCUS       NP_001424497             377 aa            linear   ROD 04-APR-2025
DEFINITION  CST complex subunit STN1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424497 XP_017444532
VERSION     NP_001424497.1
DBSOURCE    REFSEQ: accession NM_001437568.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Iles,M.M., Bishop,D.T., Taylor,J.C., Hayward,N.K., Brossard,M.,
            Cust,A.E., Dunning,A.M., Lee,J.E., Moses,E.K., Akslen,L.A.,
            Andresen,P.A., Avril,M.F., Azizi,E., Scarra,G.B., Brown,K.M.,
            Debniak,T., Elder,D.E., Friedman,E., Ghiorzo,P., Gillanders,E.M.,
            Goldstein,A.M., Gruis,N.A., Hansson,J., Harland,M., Helsing,P.,
            Hocevar,M., Hoiom,V., Ingvar,C., Kanetsky,P.A., Landi,M.T.,
            Lang,J., Lathrop,G.M., Lubinski,J., Mackie,R.M., Martin,N.G.,
            Molven,A., Montgomery,G.W., Novakovic,S., Olsson,H., Puig,S.,
            Puig-Butille,J.A., Radford-Smith,G.L., Randerson-Moor,J., van der
            Stoep,N., van Doorn,R., Whiteman,D.C., MacGregor,S., Pooley,K.A.,
            Ward,S.V., Mann,G.J., Amos,C.I., Pharoah,P.D., Demenais,F.,
            Law,M.H., Newton Bishop,J.A. and Barrett,J.H.
  CONSRTM   AMFS Investigators; IBD investigators; QMEGA and QTWIN
            Investigators; SDH Study Group; GenoMEL Consortium
  TITLE     The effect on melanoma risk of genes previously associated with
            telomere length
  JOURNAL   J Natl Cancer Inst 106 (10) (2014)
   PUBMED   25231748
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_017444532.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5951.1,
                                           SRR26360186.591628.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..377
                     /product="CST complex subunit STN1 isoform 1"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; CST complex subunit STN1;
                     suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1;
                     STN1, CST complex subunit"
                     /calculated_mol_wt=43281
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          212..377
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     CDS             1..377
                     /gene="Stn1"
                     /gene_synonym="Obfc1"
                     /coded_by="NM_001437568.1:136..1269"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:294025"
                     /db_xref="RGD:1305637"
ORIGIN      
        1 mpepcllmqc esspkeeeip slfwgldpvf lafaklyikd ilemkesqqv pgmyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkrps naesssdpai lstsrelsmt
      121 sqlkklqeti eqktkigigd iirvrgyvrm freereicat iyykvddpvw nmqiarmlel
      181 pelykkvydq pfrnpalkee ealnskdtld lagltallse kvkeflqekk vqsfyqkele
      241 mveplqslas qpvthstcsd qvelkndaas dihsvfknal hllqekgfvf qrdggsdkly
      301 yvtskdkdlh qkiyqiiked cqkpnhvekg chlmhvlncv llnlrwdlnk avlqqvlell
      361 edqsdivstg dhyytaf
//
LOCUS       NP_001424504             503 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424504 XP_038936753
VERSION     NP_001424504.1
DBSOURCE    REFSEQ: accession NM_001437575.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_038936753.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1704.1,
                                           SRR26643295.2508.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345329,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..503
                     /product="myocyte-specific enhancer factor 2A isoform 1"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=54097
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          97..154
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Region          <129..>380
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..503
                     /gene="Mef2a"
                     /coded_by="NM_001437575.1:311..1822"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivealnk kehrgcdspd pdtsyvltph teekykkine
      121 efdnmmrnhk iapglppqnf smsvtvpvts pnalsytnpg sslvspslaa sstlaessml
      181 spppatlhrn vspgapqrpp stgsaggmls ttdltvpnga gnspvgngfv nsraspnlig
      241 ntgansvgkv mptksppppg ggsvgmnsrk pdlrvvipps skgmmpplse eeelelnaqr
      301 isssqatqpl atpvvsvttp slppqglvys amptayntdy sltsadlsal qgftspgmls
      361 lgqasawqqh hlgqaalssl vaggqlsqgs nlsintnqni niksepispp rdrmtpsgfq
      421 qqqqqqpqqq pppqppqpqp qprqemgrsp vdslssssss ydgsdredpr gdfhspivlg
      481 rppnaedres psvkrmrmdt wvt
//
LOCUS       NP_001424522             717 aa            linear   ROD 04-APR-2025
DEFINITION  epidermal growth factor receptor kinase substrate 8-like protein 1
            [Rattus norvegicus].
ACCESSION   NP_001424522 XP_008757163
VERSION     NP_001424522.1
DBSOURCE    REFSEQ: accession NM_001437593.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Kesti,T., Ruppelt,A., Wang,J.H., Liss,M., Wagner,R., Tasken,K. and
            Saksela,K.
  TITLE     Reciprocal regulation of SH3 and SH2 domain binding via tyrosine
            phosphorylation of a common site in CD3epsilon
  JOURNAL   J Immunol 179 (2), 878-885 (2007)
   PUBMED   17617578
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Offenhauser,N., Borgonovo,A., Disanza,A., Romano,P., Ponzanelli,I.,
            Iannolo,G., Di Fiore,P.P. and Scita,G.
  TITLE     The eps8 family of proteins links growth factor stimulation to
            actin reorganization generating functional redundancy in the
            Ras/Rac pathway
  JOURNAL   Mol Biol Cell 15 (1), 91-98 (2004)
   PUBMED   14565974
  REMARK    Erratum:[Mol Biol Cell. 2019 Sep 1;30(19):2535. doi:
            10.1091/mbc.E03-06-0427-corr. PMID: 31465253]
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Hori,K., Konno,D., Maruoka,H. and Sobue,K.
  TITLE     MALS is a binding partner of IRSp53 at cell-cell contacts
  JOURNAL   FEBS Lett 554 (1-2), 30-34 (2003)
   PUBMED   14596909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_008757163.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.806.1, SRR26643295.962.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..717
                     /product="epidermal growth factor receptor kinase
                     substrate 8-like protein 1"
                     /note="EPS8-like 1"
                     /calculated_mol_wt=79955
     Region          32..162
                     /region_name="PTB_EPS8"
                     /note="Epidermal growth factor receptor kinase substrate
                     (EPS8)-like Phosphotyrosine-binding (PTB) domain; cd01210"
                     /db_xref="CDD:269921"
     Site            order(39,118,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269921"
     Site            order(104..109,125,148,152)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269921"
     Region          482..534
                     /region_name="SH3_Eps8"
                     /note="Src Homology 3 domain of Epidermal growth factor
                     receptor kinase substrate 8 and similar proteins; cd11764"
                     /db_xref="CDD:212698"
     Site            order(482..487,489,492,495..497,504..509,511..519,
                     524..527,531..534)
                     /site_type="other"
                     /note="swapped dimer interface [polypeptide binding]"
                     /db_xref="CDD:212698"
     Site            order(489,493..495,512..514,516,525..526,528..531)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212698"
     Region          623..688
                     /region_name="SAM_EPS8-like"
                     /note="SAM domain of EPS8-like subfamily; cd09540"
                     /db_xref="CDD:188939"
     CDS             1..717
                     /gene="Eps8l1"
                     /coded_by="NM_001437593.1:189..2342"
                     /db_xref="GeneID:361503"
                     /db_xref="RGD:1311146"
ORIGIN      
        1 mstttgpeaa pkpsaksiye qrkrystvvm advsqyhvnh lvtfclgeed gvhtvedasr
       61 klavmdsqgr vwaqemllrv spghvtlldp vskeelesyp ldaivrcdav mprgrsrsll
      121 llvcqepera qpdvhffqgl llgaelired iqgalqnyrs grgerraaal ratqeelrrg
      181 aspaaetppl qrrpsvravi ntvepsavrg rpqvepipet eearkpdpar tttrssdpts
      241 pdlgprgpel aglqaerdvd ilnhvfddve sfvsrlqksa eatrvlehre rgrrtrrraa
      301 geglltlrak ppteaeytdv lqkikyafsl larlrgnian psspellhfl fgplqmivnt
      361 sggpefprsv rrphltleav allrdnvtpr enelwtslgd swtrpgvelp peegspyspe
      421 fysgweppat dpqgrpwedp vekqlqhekr rrqqsapqva vnghqdpele tesqleekar
      481 kwvlcnydfq arngselsvk hrdvlevldd rrkwwkvrdh qgqegyvpyn iltphpgpqv
      541 hcsqssainl etsppppppa aapaptqvrp qwdscdslns ldpsdkekfs qmlcvneelq
      601 arlaqgrsgp srvtpglrap epqlsprsea svvrawlqtk gfssgtvdal gvltgaqlfs
      661 lqkeelrsvc peegarvysq vtvqralled rekvseleav mekqkkkveg etktevi
//
LOCUS       NP_001424503             486 aa            linear   ROD 04-APR-2025
DEFINITION  monocarboxylate transporter 12 [Rattus norvegicus].
ACCESSION   NP_001424503 XP_017444789
VERSION     NP_001424503.1
DBSOURCE    REFSEQ: accession NM_001437574.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Jomura,R., Tanno,Y., Akanuma,S.I., Kubo,Y., Tachikawa,M. and
            Hosoya,K.I.
  TITLE     Contribution of monocarboxylate transporter 12 to blood supply of
            creatine on the sinusoidal membrane of the hepatocytes
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 321 (2), G113-G122 (2021)
   PUBMED   34075817
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Verouti,S.N., Lambert,D., Mathis,D., Pathare,G., Escher,G., Vogt,B.
            and Fuster,D.G.
  TITLE     Solute carrier SLC16A12 is critical for creatine and
            guanidinoacetate handling in the kidney
  JOURNAL   Am J Physiol Renal Physiol 320 (3), F351-F358 (2021)
   PUBMED   33459166
  REMARK    GeneRIF: Solute carrier SLC16A12 is critical for creatine and
            guanidinoacetate handling in the kidney.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Jomura,R., Tanno,Y., Akanuma,S.I., Kubo,Y., Tachikawa,M. and
            Hosoya,K.I.
  TITLE     Monocarboxylate transporter 12 as a guanidinoacetate efflux
            transporter in renal proximal tubular epithelial cells
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (11), 183434 (2020)
   PUBMED   32781157
  REMARK    GeneRIF: Monocarboxylate transporter 12 as a guanidinoacetate
            efflux transporter in renal proximal tubular epithelial cells.
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Abplanalp,J., Laczko,E., Philp,N.J., Neidhardt,J., Zuercher,J.,
            Braun,P., Schorderet,D.F., Munier,F.L., Verrey,F., Berger,W.,
            Camargo,S.M. and Kloeckener-Gruissem,B.
  TITLE     The cataract and glucosuria associated monocarboxylate transporter
            MCT12 is a new creatine transporter
  JOURNAL   Hum Mol Genet 22 (16), 3218-3226 (2013)
   PUBMED   23578822
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Castorino,J.J., Gallagher-Colombo,S.M., Levin,A.V.,
            Fitzgerald,P.G., Polishook,J., Kloeckener-Gruissem,B., Ostertag,E.
            and Philp,N.J.
  TITLE     Juvenile cataract-associated mutation of solute carrier SLC16A12
            impairs trafficking of the protein to the plasma membrane
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6774-6784 (2011)
   PUBMED   21778275
  REMARK    GeneRIF: a model whereby the SLC16A12 (c.643C>T) mutation causes
            juvenile cataract by a defect in protein trafficking rather than by
            haploinsufficiency.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_017444789.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.3682.1,
                                           SRR26643286.4705.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..486
                     /product="monocarboxylate transporter 12"
                     /note="solute carrier family 16 (monocarboxylic acid
                     transporters), member 12; solute carrier family 16, member
                     12 (monocarboxylic acid transporter 12)"
                     /calculated_mol_wt=52709
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Region          18..431
                     /region_name="MFS_MCT12"
                     /note="Monocarboxylate transporter 12 of the of the Major
                     Facilitator Superfamily of transporters; cd17424"
                     /db_xref="CDD:340982"
     Site            order(29..30,33..34,37,72,123..124,126..128,131,150,
                     153..154,157,260,263..264,267..269,272,299,303,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340982"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            253..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            353..373
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     CDS             1..486
                     /gene="Slc16a12"
                     /gene_synonym="MCT 12; RGD1311468"
                     /coded_by="NM_001437574.1:553..2013"
                     /db_xref="GeneID:309525"
                     /db_xref="RGD:1311468"
ORIGIN      
        1 mtkitrvgsa sppdggwgwm ivagcflvti ctravtrcis iffvefqtyf aqdysqtawi
       61 hsivdcmtml caplgsvvsn qlscqagiml ggllastgli lgsfatslkh lylslgvltg
      121 lgfalcyspa iamvgkyfsr rkafaygiam sgsgigtfil apvvqllieq fswrgallil
      181 ggfvlnlcvc galmrpitlk edpsgpeksh drdaqredck qaspyspltk ewtetrlccs
      241 lqqgygfllm sdfvvlavsv lfmaygcspl fvylvpyals vgvshhqaaf lmsilgvidi
      301 vgnitfgwlt drrclknyry vcylfavald glcylclpml qsfpllvpfs ctfgyfdgay
      361 vtlipvvtae ivgttslssa lgvvyflhav pylvsppiag wlvdttgsyt aafllcgfam
      421 ifssillgfa kiakrmkrtq vpflvkdsdp klhlwtngsv aysiakeldq kdeeslakar
      481 tgcnlt
//
LOCUS       NP_001424489            1627 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 12 [Rattus norvegicus].
ACCESSION   NP_001424489
VERSION     NP_001424489.1
DBSOURCE    REFSEQ: accession NM_001437560.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1627)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1509878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1627
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1627
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 12"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=173962
     Region          <370..835
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <622..1107
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <969..1352
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1504..1594
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1627
                     /gene="Pprc1"
                     /coded_by="NM_001437560.1:10..4893"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 mstwllsqav ghlvsaleph crelgvsqpl ppslacagts glevheegdd ssfvslsrlg
       61 pslrekdlem eelilqdetl letmqnymda slisliedfg esrlsledqn emslltalte
      121 ildnadsenl spfdtipdse llvspresss lhkllnlsrt pperdripam dplgpsagss
      181 rvsgvemsla dspwdfsppp fletsspklp swrssrprpr wsqspppqqr sdgeeeeeva
      241 gfsgqmldge ldnsvntldf pmhlacpeee dksgaanvav sapgdesiss lselvramhp
      301 yclpnltqla sldaelqeqa ddltlpegcv vleivgqaat agddleipvv vrqipsgsqs
      361 vlldgsvgtd palqllmpam epgtedgvpk vapcpdqelp lssacllepr dimeslapke
      421 prnlpanase gsqrvprkgr kkkkkeqpta clegctrrlr sssrgqstva tevnsqagnl
      481 qkqpqeelqr etaapqsrgk prawarawaa alektgsedp edqnagqdsp aeedvlelrp
      541 klvetsqadp tlslndsara dsipvnsveg dstavdtavp vdqassctel vgslsggpil
      601 sspvlddrtg vepavaipts nhlspadail anpgtadpap nglapgdpvl vkcrptdprr
      661 aaaaataaqg prpslepsdh pkvitpevkd aggplkvegs tsattqearp rplslseyrq
      721 rrrqrqieae drnsqppagk wpslpetpkg ladipclvps aptkktapqr spiavpetcs
      781 vsvgsnpvsp tpepsasklm vsthseqvss hemplpvrlp pptlqsmapa gptpstvptp
      841 lpfppslppl lplpasgpgv pslpppplqp pglpvsmrqm ppdpytqyap vppwpcypsv
      901 spsgysclpp ppampivsgt pgtyavpptc nvpwvpppap vspyssssay gslgwgpglq
      961 qppfwstvsp pplssastgr avpppsveps nssagppedt lpvpvtpsls srpaspiapp
     1021 aeptkleaqp vpvspqpkhk vspvvqspqi kvlptlsaeg vaigeseser lkpetqenrp
     1081 rekpistatk avllpkqstv aklpavhpar lrrlsflptp raqgsedvvq afiseigiea
     1141 sdlsslleqf ekseakkecp lpapadsvav gnsgidtpqe kkpldrlhap elanvagltp
     1201 patpphqlwk plaavsllak akspkstaqe gtlkpegite akppaaaclq egvrgpspvh
     1261 vgsgdhdycv rsrtppkkmp alvisemgsr wnvkrhqdit ikpvlslgsa applpcttts
     1321 qepldhrtss eqadpsapcf apstllspea spcrnemntr tpseppdkqr smrcyrkacr
     1381 sasppsrgwq grrgrssrsv ssgssrtsea sssssvssss rsrsrslspp nkrwrrsscs
     1441 ssgrsrrcss ssssssssss ssssrsrsps vspcrrsdrr rrsyrsndhy qrqrvlqker
     1501 aieerrvvfi gkipgrmtrs elkqrfsvfg eieectihfr vqgdnygfvt yryaeeafaa
     1561 iesghklrqa deqpfdlcfg grrqfckrsy sdldsnredf dpapvkskfd sldfdtllkq
     1621 aqknlrr
//
LOCUS       NP_001424505             501 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424505 XP_038936767
VERSION     NP_001424505.1
DBSOURCE    REFSEQ: accession NM_001437576.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_038936767.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1706.1,
                                           SRR26643298.3378.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345329,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..501
                     /product="myocyte-specific enhancer factor 2A isoform 2"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=53727
     Region          1..>235
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          <125..>378
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..501
                     /gene="Mef2a"
                     /coded_by="NM_001437576.1:311..1816"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivetlrk kglngcespd addyfehspl sedrfsklne
      121 dsdfifkrgp pglppqnfsm svtvpvtspn alsytnpgss lvspslaass tlaessmlsp
      181 ppatlhrnvs pgapqrppst gsaggmlstt dltvpngagn spvgngfvns raspnlignt
      241 gansvgkvmp tksppppggg svgmnsrkpd lrvvippssk gmmpplseee elelnaqris
      301 ssqatqplat pvvsvttpsl ppqglvysam ptayntdysl tsadlsalqg ftspgmlslg
      361 qasawqqhhl gqaalsslva ggqlsqgsnl sintnqnini ksepispprd rmtpsgfqqq
      421 qqqqpqqqpp pqppqpqpqp rqemgrspvd slssssssyd gsdredprgd fhspivlgrp
      481 pnaedresps vkrmrmdtwv t
//
LOCUS       NP_001424521             717 aa            linear   ROD 04-APR-2025
DEFINITION  epidermal growth factor receptor kinase substrate 8-like protein 1
            [Rattus norvegicus].
ACCESSION   NP_001424521 XP_006228341
VERSION     NP_001424521.1
DBSOURCE    REFSEQ: accession NM_001437592.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Kesti,T., Ruppelt,A., Wang,J.H., Liss,M., Wagner,R., Tasken,K. and
            Saksela,K.
  TITLE     Reciprocal regulation of SH3 and SH2 domain binding via tyrosine
            phosphorylation of a common site in CD3epsilon
  JOURNAL   J Immunol 179 (2), 878-885 (2007)
   PUBMED   17617578
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Offenhauser,N., Borgonovo,A., Disanza,A., Romano,P., Ponzanelli,I.,
            Iannolo,G., Di Fiore,P.P. and Scita,G.
  TITLE     The eps8 family of proteins links growth factor stimulation to
            actin reorganization generating functional redundancy in the
            Ras/Rac pathway
  JOURNAL   Mol Biol Cell 15 (1), 91-98 (2004)
   PUBMED   14565974
  REMARK    Erratum:[Mol Biol Cell. 2019 Sep 1;30(19):2535. doi:
            10.1091/mbc.E03-06-0427-corr. PMID: 31465253]
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Hori,K., Konno,D., Maruoka,H. and Sobue,K.
  TITLE     MALS is a binding partner of IRSp53 at cell-cell contacts
  JOURNAL   FEBS Lett 554 (1-2), 30-34 (2003)
   PUBMED   14596909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006228341.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.1169.1,
                                           SRR26643297.808.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..717
                     /product="epidermal growth factor receptor kinase
                     substrate 8-like protein 1"
                     /note="EPS8-like 1"
                     /calculated_mol_wt=79955
     Region          32..162
                     /region_name="PTB_EPS8"
                     /note="Epidermal growth factor receptor kinase substrate
                     (EPS8)-like Phosphotyrosine-binding (PTB) domain; cd01210"
                     /db_xref="CDD:269921"
     Site            order(39,118,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269921"
     Site            order(104..109,125,148,152)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269921"
     Region          482..534
                     /region_name="SH3_Eps8"
                     /note="Src Homology 3 domain of Epidermal growth factor
                     receptor kinase substrate 8 and similar proteins; cd11764"
                     /db_xref="CDD:212698"
     Site            order(482..487,489,492,495..497,504..509,511..519,
                     524..527,531..534)
                     /site_type="other"
                     /note="swapped dimer interface [polypeptide binding]"
                     /db_xref="CDD:212698"
     Site            order(489,493..495,512..514,516,525..526,528..531)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212698"
     Region          623..688
                     /region_name="SAM_EPS8-like"
                     /note="SAM domain of EPS8-like subfamily; cd09540"
                     /db_xref="CDD:188939"
     CDS             1..717
                     /gene="Eps8l1"
                     /coded_by="NM_001437592.1:293..2446"
                     /db_xref="GeneID:361503"
                     /db_xref="RGD:1311146"
ORIGIN      
        1 mstttgpeaa pkpsaksiye qrkrystvvm advsqyhvnh lvtfclgeed gvhtvedasr
       61 klavmdsqgr vwaqemllrv spghvtlldp vskeelesyp ldaivrcdav mprgrsrsll
      121 llvcqepera qpdvhffqgl llgaelired iqgalqnyrs grgerraaal ratqeelrrg
      181 aspaaetppl qrrpsvravi ntvepsavrg rpqvepipet eearkpdpar tttrssdpts
      241 pdlgprgpel aglqaerdvd ilnhvfddve sfvsrlqksa eatrvlehre rgrrtrrraa
      301 geglltlrak ppteaeytdv lqkikyafsl larlrgnian psspellhfl fgplqmivnt
      361 sggpefprsv rrphltleav allrdnvtpr enelwtslgd swtrpgvelp peegspyspe
      421 fysgweppat dpqgrpwedp vekqlqhekr rrqqsapqva vnghqdpele tesqleekar
      481 kwvlcnydfq arngselsvk hrdvlevldd rrkwwkvrdh qgqegyvpyn iltphpgpqv
      541 hcsqssainl etsppppppa aapaptqvrp qwdscdslns ldpsdkekfs qmlcvneelq
      601 arlaqgrsgp srvtpglrap epqlsprsea svvrawlqtk gfssgtvdal gvltgaqlfs
      661 lqkeelrsvc peegarvysq vtvqralled rekvseleav mekqkkkveg etktevi
//
LOCUS       NP_001424507             495 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424507 XP_063121681
VERSION     NP_001424507.1
DBSOURCE    REFSEQ: accession NM_001437578.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063121681.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.2714.1,
                                           SRR26643293.3537.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..495
                     /product="myocyte-specific enhancer factor 2A isoform 3"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=53138
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          97..154
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          <129..>372
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          175..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            213..214
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          242..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          266..283
                     /region_name="Required for interaction with MAPKs.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK7 and MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Region          382..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            395
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000269|PubMed:16484498; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60929; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02078; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q2MJT0.1)"
     CDS             1..495
                     /gene="Mef2a"
                     /coded_by="NM_001437578.1:258..1745"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivealnk kehrgcdspd pdtsyvltph teekykkine
      121 efdnmmrnhk iapglppqnf smsvtvpvts pnalsytnpg sslvspslaa sstlaessml
      181 spppatlhrn vspgapqrpp stgsaggmls ttdltvpnga gnspvgngfv nsraspnlig
      241 ntgansvgkv mptksppppg ggsvgmnsrk pdlrvvipps skgmmpplna qrisssqatq
      301 platpvvsvt tpslppqglv ysamptaynt dysltsadls alqgftspgm lslgqasawq
      361 qhhlgqaals slvaggqlsq gsnlsintnq niniksepis pprdrmtpsg fqqqqqqqpq
      421 qqpppqppqp qpqprqemgr spvdslssss ssydgsdred prgdfhspiv lgrppnaedr
      481 espsvkrmrm dtwvt
//
LOCUS       NP_001424506             501 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424506 XP_063121665
VERSION     NP_001424506.1
DBSOURCE    REFSEQ: accession NM_001437577.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063121665.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.1885.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..501
                     /product="myocyte-specific enhancer factor 2A isoform 2"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=53727
     Region          1..>235
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          <125..>378
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..501
                     /gene="Mef2a"
                     /coded_by="NM_001437577.1:258..1763"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivetlrk kglngcespd addyfehspl sedrfsklne
      121 dsdfifkrgp pglppqnfsm svtvpvtspn alsytnpgss lvspslaass tlaessmlsp
      181 ppatlhrnvs pgapqrppst gsaggmlstt dltvpngagn spvgngfvns raspnlignt
      241 gansvgkvmp tksppppggg svgmnsrkpd lrvvippssk gmmpplseee elelnaqris
      301 ssqatqplat pvvsvttpsl ppqglvysam ptayntdysl tsadlsalqg ftspgmlslg
      361 qasawqqhhl gqaalsslva ggqlsqgsnl sintnqnini ksepispprd rmtpsgfqqq
      421 qqqqpqqqpp pqppqpqpqp rqemgrspvd slssssssyd gsdredprgd fhspivlgrp
      481 pnaedresps vkrmrmdtwv t
//
LOCUS       NP_001424484            1375 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424484 XP_063143281
VERSION     NP_001424484.1
DBSOURCE    REFSEQ: accession NM_001437555.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1375)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143281.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1822835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1375
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 7"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=146613
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1252..1342
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1375
                     /gene="Pprc1"
                     /coded_by="NM_001437555.1:30..4157"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgsscsssgr srrcssssss
     1201 ssssssssss rsrspsvspc rrsdrrrrys syrsndhyqr qrvlqkerai eerrvvfigk
     1261 ipgrmtrsel kqrfsvfgei eectihfrvq gdnygfvtyr yaeeafaaie sghklrqade
     1321 qpfdlcfggr rqfckrsysd ldsnredfdp apvkskfdsl dfdtllkqaq knlrr
//
LOCUS       NP_001424525             162 aa            linear   ROD 04-APR-2025
DEFINITION  cdc42 effector protein 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424525
VERSION     NP_001424525.1
DBSOURCE    REFSEQ: accession NM_001437596.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Joberty,G., Perlungher,R.R. and Macara,I.G.
  TITLE     The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
            proteins
  JOURNAL   Mol Cell Biol 19 (10), 6585-6597 (1999)
   PUBMED   10490598
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW918408.1, CB793038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..162
                     /product="cdc42 effector protein 5 isoform 2"
                     /note="CDC42 effector protein (Rho GTPase binding) 5"
                     /calculated_mol_wt=16702
     Region          32..>59
                     /region_name="CRIB"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cl00113"
                     /db_xref="CDD:412170"
     Region          <79..122
                     /region_name="BORG_CEP"
                     /note="Cdc42 effector; pfam14957"
                     /db_xref="CDD:464403"
     CDS             1..162
                     /gene="Cdc42ep5"
                     /coded_by="NM_001437596.1:37..525"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:361505"
                     /db_xref="RGD:1308382"
ORIGIN      
        1 mprswnpyqm allkqvgpaq pkkrlergal sisaplgdfr htlhvgssgd afgdtsflnr
       61 hgggpppeag appvvaphsv pppavpqasv pglrvpspad pllsfhldlg psmldavlgv
      121 mdaergetta tkpsgdaltg mqhpnahccs nadfqlddvi gl
//
LOCUS       NP_001424478            1639 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424478 XP_006231513
VERSION     NP_001424478.1
DBSOURCE    REFSEQ: accession NM_001437549.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1639)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006231513.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.5498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1639
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1639
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 1"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=175000
     Region          <379..844
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <631..1116
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <978..1362
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1516..1606
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1639
                     /gene="Pprc1"
                     /coded_by="NM_001437549.1:30..4949"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfgeq srlsledqne
      121 mslltaltei ldnadsenls pfdtipdsel lvspresssl hkllnlsrtp perdripamd
      181 plgpsagssr vsgvemslad spwdfspppf letsspklps wrssrprprw sqspppqqrs
      241 dgeeeeevag fsgqmldgel dnsvntldfp mhlacpeeed ksgaanvavs apgdesissl
      301 selvramhpy clpnltqlas ldaelqeqad dltlpegcvv leivgqaata gddleipvvv
      361 rqipsgsqsv lldgsvgtdp alqllmpame pgtedgvpkv apcpdqelpl ssaclleprd
      421 imeslapkep rnlpanaseg sqrvprkgrk kkkkeqptac legctrrlrs ssrgqstvat
      481 evnsqagnlq kqpqeelqre taapqsrgkp rawarawaaa lektgsedpe dqnagqdspa
      541 eedvlelrpk lvetsqadpt lslndsarad sipvnsvegd stavdtavpv dqassctelv
      601 gslsggpils spvlddrtgv epavaiptsn hlspadaila npgtadpapn glapgdpvlv
      661 kcrptdprra aaaataaqgp rpslepsdhp kvitpevkda ggplkvegst sattqearpr
      721 plslseyrqr rrqrqieaed rnsqppagkw pslpetpkgl adipclvpsa ptkktapqrs
      781 piavpetcsv svgsnpvspt pepsasklmv sthseqvssh emplpvrlpp ptlqsmapag
      841 ptpstvptpl pfppslppll plpasgpgvp slpppplqpp glpvsmrqmp pdpytqyapv
      901 ppwpcypsvs psgysclppp pampivsgtp gtyavpptcn vpwvpppapv spyssssayg
      961 slgwgpglqq ppfwstvspp plssastgra vpppsvepsn ssagppedtl pvpvtpslss
     1021 rpaspiappa eptkleaqpv pvspqpkhkv spvvqspqik vlptlsaegv aigeseserl
     1081 kpetqenrpr ekpistatka vllpkqstva klpavhparl rrlsflptpr aqgsedvvqa
     1141 fiseigieas dlsslleqfe kseakkecpl papadsvavg nsgsidtpqe kkpldrlhap
     1201 elanvagltp patpphqlwk plaavsllak akspkstaqe gtlkpegite akppaaaclq
     1261 egvrgpspvh vgsgdhdycv rsrtppkkmp alvisemgsr wnvkrhqdit ikpvlslgsa
     1321 applpcttts qepldhrtss eqadpsapcf apstllspea spcrnemntr tpseppdkqr
     1381 smrcyrkacr sasppsrgwq grrgrssrsv ssgssrtsea sssssvssss rsrsrslspp
     1441 nkrwrrsscs ssgrsrrcss ssssssssss ssssrsrsps vspcrrsdrr rryssyrsnd
     1501 hyqrqrvlqk eraieerrvv figkipgrmt rselkqrfsv fgeieectih frvqgdnygf
     1561 vtyryaeeaf aaiesghklr qadeqpfdlc fggrrqfckr sysdldsnre dfdpapvksk
     1621 fdsldfdtll kqaqknlrr
//
LOCUS       NP_001424512             467 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424512
VERSION     NP_001424512.1
DBSOURCE    REFSEQ: accession NM_001437583.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.1961.1,
                                           SRR26360186.1290007.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..467
                     /product="myocyte-specific enhancer factor 2A isoform 5"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=49704
     Region          <1..50
                     /region_name="MADS"
                     /note="MCM1, Agamous, Deficiens, and SRF (serum response
                     factor) box family of eukaryotic transcriptonal
                     regulators. Binds DNA and exists as hetero and
                     homo-dimers. Composed of 2 main subgroups: SRF-like/Type I
                     and MEF2-like (myocyte enhancer factor 2)/ Type...;
                     cl00109"
                     /db_xref="CDD:469617"
     Site            order(1..2,5,9,25..32)
                     /site_type="other"
                     /note="protein interaction site [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            order(1,4..5,7..11,16,18,20,26,28,30)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            31
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          69..126
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Region          <101..>344
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..467
                     /gene="Mef2a"
                     /coded_by="NM_001437583.1:473..1876"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mkkayelsvl cdceialiif nssnklfqya stdmdkvllk yteynephes rtnsdiveal
       61 nkkehrgcds pdpdtsyvlt phteekykki neefdnmmrn hkiapglppq nfsmsvtvpv
      121 tspnalsytn pgsslvspsl aasstlaess mlspppatlh rnvspgapqr ppstgsaggm
      181 lsttdltvpn gagnspvgng fvnsraspnl igntgansvg kvmptksppp pgggsvgmns
      241 rkpdlrvvip psskgmmppl naqrisssqa tqplatpvvs vttpslppqg lvysamptay
      301 ntdysltsad lsalqgftsp gmlslgqasa wqqhhlgqaa lsslvaggql sqgsnlsint
      361 nqniniksep ispprdrmtp sgfqqqqqqq pqqqpppqpp qpqpqprqem grspvdslss
      421 ssssydgsdr edprgdfhsp ivlgrppnae drespsvkrm rmdtwvt
//
LOCUS       NP_001424511             493 aa            linear   ROD 04-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424511 XP_038936771
VERSION     NP_001424511.1
DBSOURCE    REFSEQ: accession NM_001437582.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_038936771.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.2327466.1,
                                           SRR26360172.393950.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..493
                     /product="myocyte-specific enhancer factor 2A isoform 4"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=52768
     Region          1..>235
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          <125..>370
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..493
                     /gene="Mef2a"
                     /coded_by="NM_001437582.1:463..1944"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivetlrk kglngcespd addyfehspl sedrfsklne
      121 dsdfifkrgp pglppqnfsm svtvpvtspn alsytnpgss lvspslaass tlaessmlsp
      181 ppatlhrnvs pgapqrppst gsaggmlstt dltvpngagn spvgngfvns raspnlignt
      241 gansvgkvmp tksppppggg svgmnsrkpd lrvvippssk gmmpplnaqr isssqatqpl
      301 atpvvsvttp slppqglvys amptayntdy sltsadlsal qgftspgmls lgqasawqqh
      361 hlgqaalssl vaggqlsqgs nlsintnqni niksepispp rdrmtpsgfq qqqqqqpqqq
      421 pppqppqpqp qprqemgrsp vdslssssss ydgsdredpr gdfhspivlg rppnaedres
      481 psvkrmrmdt wvt
//
LOCUS       NP_001424488            1629 aa            linear   ROD 04-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424488
VERSION     NP_001424488.1
DBSOURCE    REFSEQ: accession NM_001437559.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1629)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2047303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1629
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1629
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 11"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174212
     Region          <370..835
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <622..1107
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <969..1352
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1506..1596
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1629
                     /gene="Pprc1"
                     /coded_by="NM_001437559.1:10..4899"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 mstwllsqav ghlvsaleph crelgvsqpl ppslacagts glevheegdd ssfvslsrlg
       61 pslrekdlem eelilqdetl letmqnymda slisliedfg esrlsledqn emslltalte
      121 ildnadsenl spfdtipdse llvspresss lhkllnlsrt pperdripam dplgpsagss
      181 rvsgvemsla dspwdfsppp fletsspklp swrssrprpr wsqspppqqr sdgeeeeeva
      241 gfsgqmldge ldnsvntldf pmhlacpeee dksgaanvav sapgdesiss lselvramhp
      301 yclpnltqla sldaelqeqa ddltlpegcv vleivgqaat agddleipvv vrqipsgsqs
      361 vlldgsvgtd palqllmpam epgtedgvpk vapcpdqelp lssacllepr dimeslapke
      421 prnlpanase gsqrvprkgr kkkkkeqpta clegctrrlr sssrgqstva tevnsqagnl
      481 qkqpqeelqr etaapqsrgk prawarawaa alektgsedp edqnagqdsp aeedvlelrp
      541 klvetsqadp tlslndsara dsipvnsveg dstavdtavp vdqassctel vgslsggpil
      601 sspvlddrtg vepavaipts nhlspadail anpgtadpap nglapgdpvl vkcrptdprr
      661 aaaaataaqg prpslepsdh pkvitpevkd aggplkvegs tsattqearp rplslseyrq
      721 rrrqrqieae drnsqppagk wpslpetpkg ladipclvps aptkktapqr spiavpetcs
      781 vsvgsnpvsp tpepsasklm vsthseqvss hemplpvrlp pptlqsmapa gptpstvptp
      841 lpfppslppl lplpasgpgv pslpppplqp pglpvsmrqm ppdpytqyap vppwpcypsv
      901 spsgysclpp ppampivsgt pgtyavpptc nvpwvpppap vspyssssay gslgwgpglq
      961 qppfwstvsp pplssastgr avpppsveps nssagppedt lpvpvtpsls srpaspiapp
     1021 aeptkleaqp vpvspqpkhk vspvvqspqi kvlptlsaeg vaigeseser lkpetqenrp
     1081 rekpistatk avllpkqstv aklpavhpar lrrlsflptp raqgsedvvq afiseigiea
     1141 sdlsslleqf ekseakkecp lpapadsvav gnsgidtpqe kkpldrlhap elanvagltp
     1201 patpphqlwk plaavsllak akspkstaqe gtlkpegite akppaaaclq egvrgpspvh
     1261 vgsgdhdycv rsrtppkkmp alvisemgsr wnvkrhqdit ikpvlslgsa applpcttts
     1321 qepldhrtss eqadpsapcf apstllspea spcrnemntr tpseppdkqr smrcyrkacr
     1381 sasppsrgwq grrgrssrsv ssgssrtsea sssssvssss rsrsrslspp nkrwrrsscs
     1441 ssgrsrrcss ssssssssss ssssrsrsps vspcrrsdrr rryssyrsnd hyqrqrvlqk
     1501 eraieerrvv figkipgrmt rselkqrfsv fgeieectih frvqgdnygf vtyryaeeaf
     1561 aaiesghklr qadeqpfdlc fggrrqfckr sysdldsnre dfdpapvksk fdsldfdtll
     1621 kqaqknlrr
//
LOCUS       NP_001424496             377 aa            linear   ROD 04-APR-2025
DEFINITION  CST complex subunit STN1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424496 XP_038965016
VERSION     NP_001424496.1
DBSOURCE    REFSEQ: accession NM_001437567.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Iles,M.M., Bishop,D.T., Taylor,J.C., Hayward,N.K., Brossard,M.,
            Cust,A.E., Dunning,A.M., Lee,J.E., Moses,E.K., Akslen,L.A.,
            Andresen,P.A., Avril,M.F., Azizi,E., Scarra,G.B., Brown,K.M.,
            Debniak,T., Elder,D.E., Friedman,E., Ghiorzo,P., Gillanders,E.M.,
            Goldstein,A.M., Gruis,N.A., Hansson,J., Harland,M., Helsing,P.,
            Hocevar,M., Hoiom,V., Ingvar,C., Kanetsky,P.A., Landi,M.T.,
            Lang,J., Lathrop,G.M., Lubinski,J., Mackie,R.M., Martin,N.G.,
            Molven,A., Montgomery,G.W., Novakovic,S., Olsson,H., Puig,S.,
            Puig-Butille,J.A., Radford-Smith,G.L., Randerson-Moor,J., van der
            Stoep,N., van Doorn,R., Whiteman,D.C., MacGregor,S., Pooley,K.A.,
            Ward,S.V., Mann,G.J., Amos,C.I., Pharoah,P.D., Demenais,F.,
            Law,M.H., Newton Bishop,J.A. and Barrett,J.H.
  CONSRTM   AMFS Investigators; IBD investigators; QMEGA and QTWIN
            Investigators; SDH Study Group; GenoMEL Consortium
  TITLE     The effect on melanoma risk of genes previously associated with
            telomere length
  JOURNAL   J Natl Cancer Inst 106 (10) (2014)
   PUBMED   25231748
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_038965016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2516049.1,
                                           SRR26643294.7067.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..377
                     /product="CST complex subunit STN1 isoform 1"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; CST complex subunit STN1;
                     suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1;
                     STN1, CST complex subunit"
                     /calculated_mol_wt=43281
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          212..377
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     CDS             1..377
                     /gene="Stn1"
                     /gene_synonym="Obfc1"
                     /coded_by="NM_001437567.1:274..1407"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:294025"
                     /db_xref="RGD:1305637"
ORIGIN      
        1 mpepcllmqc esspkeeeip slfwgldpvf lafaklyikd ilemkesqqv pgmyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkrps naesssdpai lstsrelsmt
      121 sqlkklqeti eqktkigigd iirvrgyvrm freereicat iyykvddpvw nmqiarmlel
      181 pelykkvydq pfrnpalkee ealnskdtld lagltallse kvkeflqekk vqsfyqkele
      241 mveplqslas qpvthstcsd qvelkndaas dihsvfknal hllqekgfvf qrdggsdkly
      301 yvtskdkdlh qkiyqiiked cqkpnhvekg chlmhvlncv llnlrwdlnk avlqqvlell
      361 edqsdivstg dhyytaf
//
LOCUS       NP_001099844             397 aa            linear   ROD 04-APR-2025
DEFINITION  lipase member K precursor [Rattus norvegicus].
ACCESSION   NP_001099844 XP_001079875 XP_220067
VERSION     NP_001099844.1
DBSOURCE    REFSEQ: accession NM_001106374.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473953.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_220067.3, XP_001079875.1.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..397
                     /product="lipase member K precursor"
                     /note="lipase-like, ab-hydrolase domain containing 2;
                     lipase K; lipase member K"
                     /calculated_mol_wt=43253
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2103
     Region          34..388
                     /region_name="PLN02872"
                     /note="triacylglycerol lipase"
                     /db_xref="CDD:215470"
     CDS             1..397
                     /gene="Lipk"
                     /gene_synonym="Lipl2"
                     /coded_by="NM_001106374.1:107..1300"
                     /db_xref="GeneID:294094"
                     /db_xref="RGD:1309724"
ORIGIN      
        1 mwwllatccm flpgpiyghm qesitnpean mniseiisyw gypyerhdvv tedgyilgty
       61 riphgkgcsr kavpkavvyl qhgliasasn wicnlpnnsl aflladsgyd vwlgnsrgnt
      121 wsrkhlrlsp kspeywafsl demakydlpa tinlileksg qkqlfyvghs qgttiafiaf
      181 stnpelakki rmffalapvv tvkytqspmk klttlsrkav kilfgdkmfs thtwleqfia
      241 tkvcnrklfr qlcsnflfsl sgfdpqnlnm srldvymaqs pagtsvqnml hwaqavnsgq
      301 lqafdwgnpd qnmmhfnqlt ppvyniskmr vptamwsggr dvvadekdtk nllpkvanli
      361 yykeiphynh mdfylgqdap qevyrdlitm meeslqn
//
LOCUS       NP_001011943             408 aa            linear   ROD 04-APR-2025
DEFINITION  CST complex subunit STN1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001011943 XP_215273
VERSION     NP_001011943.1
DBSOURCE    REFSEQ: accession NM_001011943.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Iles,M.M., Bishop,D.T., Taylor,J.C., Hayward,N.K., Brossard,M.,
            Cust,A.E., Dunning,A.M., Lee,J.E., Moses,E.K., Akslen,L.A.,
            Andresen,P.A., Avril,M.F., Azizi,E., Scarra,G.B., Brown,K.M.,
            Debniak,T., Elder,D.E., Friedman,E., Ghiorzo,P., Gillanders,E.M.,
            Goldstein,A.M., Gruis,N.A., Hansson,J., Harland,M., Helsing,P.,
            Hocevar,M., Hoiom,V., Ingvar,C., Kanetsky,P.A., Landi,M.T.,
            Lang,J., Lathrop,G.M., Lubinski,J., Mackie,R.M., Martin,N.G.,
            Molven,A., Montgomery,G.W., Novakovic,S., Olsson,H., Puig,S.,
            Puig-Butille,J.A., Radford-Smith,G.L., Randerson-Moor,J., van der
            Stoep,N., van Doorn,R., Whiteman,D.C., MacGregor,S., Pooley,K.A.,
            Ward,S.V., Mann,G.J., Amos,C.I., Pharoah,P.D., Demenais,F.,
            Law,M.H., Newton Bishop,J.A. and Barrett,J.H.
  CONSRTM   AMFS Investigators; IBD investigators; QMEGA and QTWIN
            Investigators; SDH Study Group; GenoMEL Consortium
  TITLE     The effect on melanoma risk of genes previously associated with
            telomere length
  JOURNAL   J Natl Cancer Inst 106 (10) (2014)
   PUBMED   25231748
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079096.1.
            
            On Feb 11, 2005 this sequence version replaced XP_215273.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079096.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..408
                     /product="CST complex subunit STN1 isoform 3"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; CST complex subunit STN1;
                     suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1;
                     STN1, CST complex subunit"
                     /calculated_mol_wt=46652
     Region          8..195
                     /region_name="Interaction with CTC1.
                     /evidence=ECO:0000250|UniProtKB:Q9H668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD2.1)"
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          201..304
                     /region_name="Winged helix-turn-helix (wHTH) 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD2.1)"
     Region          212..408
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     Region          305..408
                     /region_name="Winged helix-turn-helix (wHTH) 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD2.1)"
     CDS             1..408
                     /gene="Stn1"
                     /gene_synonym="Obfc1"
                     /coded_by="NM_001011943.1:198..1424"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:294025"
                     /db_xref="RGD:1305637"
ORIGIN      
        1 mpepcllmqc esspkeeeip slfwgldpvf lafaklyikd ilemkesqqv pgmyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkrps naesssdpai lstsrelsmt
      121 sqlkklqeti eqktkigigd iirvrgyvrm freereicat iyykvddpvw nmqiarmlel
      181 pelykkvydq pfrnpalkee ealnskdtld lagltallse kvkeflqekk vqsfyqkele
      241 mveplqslas qpvthstcsd qvelkndaas dihsvfknal hllqekgfvf qrdggsdkly
      301 yvtskdkdlh qkiyqiiked cqkpnlwcml pqeawrgtee glavvvtlsv clplpvdvek
      361 gchlmhvlnc vllnlrwdln kavlqqvlel ledqsdivst gdhyytaf
//
LOCUS       NP_001424402             963 aa            linear   ROD 06-APR-2025
DEFINITION  synphilin-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424402 XP_006254783
VERSION     NP_001424402.1
DBSOURCE    REFSEQ: accession NM_001437473.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254783.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2494566.1,
                                           SRR26360194.624517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..963
                     /product="synphilin-1 isoform 1"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=105664
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..963
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437473.1:179..3070"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaamysscih lpsnalveeh lrdyarlndi krntkktynv khiaepepke
      961 lfl
//
LOCUS       NP_001100901             418 aa            linear   ROD 07-APR-2025
DEFINITION  carbohydrate sulfotransferase 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100901 XP_001077726 XP_226482
VERSION     NP_001100901.1
DBSOURCE    REFSEQ: accession NM_001107431.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Akama,T.O., Misra,A.K., Hindsgaul,O. and Fukuda,M.N.
  TITLE     Enzymatic synthesis in vitro of the disulfated disaccharide unit of
            corneal keratan sulfate
  JOURNAL   J Biol Chem 277 (45), 42505-42513 (2002)
   PUBMED   12218059
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Akama,T.O., Nakayama,J., Nishida,K., Hiraoka,N., Suzuki,M.,
            McAuliffe,J., Hindsgaul,O., Fukuda,M. and Fukuda,M.N.
  TITLE     Human corneal GlcNac 6-O-sulfotransferase and mouse intestinal
            GlcNac 6-O-sulfotransferase both produce keratan sulfate
  JOURNAL   J Biol Chem 276 (19), 16271-16278 (2001)
   PUBMED   11278593
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Bartes,A., Bhakta,S. and Hemmerich,S.
  TITLE     Sulfation of endothelial mucin by corneal keratan
            N-acetylglucosamine 6-O-sulfotransferase (GST-4beta)
  JOURNAL   Biochem Biophys Res Commun 282 (4), 928-933 (2001)
   PUBMED   11352640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001077726.1, XP_226482.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213398.1, SRR26643299.64821.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..418
                     /product="carbohydrate sulfotransferase 5 isoform 1"
                     /note="carbohydrate (N-acetylglucosamine 6-O)
                     sulfotransferase 5; carbohydrate sulfotransferase 5"
                     /calculated_mol_wt=46727
     Region          182..380
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; cl21551"
                     /db_xref="CDD:473908"
     CDS             1..418
                     /gene="Chst6"
                     /gene_synonym="Chst5; RGD1561144"
                     /coded_by="NM_001107431.2:129..1385"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307859"
                     /db_xref="RGD:1561144"
ORIGIN      
        1 mrpgraaqss teaqpaaqal argmrlprfs stvvlslliv qtgilvflvs rqmpsspagr
       61 gehvhvlvls swrsgssfvg qlfsqhpdvf ylmepawhvw dalsqasapa lhmavrdlir
      121 svflcdmdvf daylpwrrni sdlfqwavsr alcsppvcda fargnissee vckplcatrp
      181 fglaqeacss yshvvlkevr ffnlqvlypl lsdpalnlri vhlvrdprav lrsreqtaka
      241 lardngivlg tngtwveadp rlrvvsevcr shvriaeval hkpppflqdr yrlvryedla
      301 rdpltvirel yaftglgltp qlqtwiynit hgsgpgarre afkttsrdal svsqawrhtl
      361 pfakirrvqe lcagalqllg yrpvhseleq rdlsldlllp rgmdsfkwas stdkqpes
//
LOCUS       NP_067719               1308 aa            linear   ROD 07-APR-2025
DEFINITION  receptor tyrosine-protein kinase erbB-4 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_067719
VERSION     NP_067719.2
DBSOURCE    REFSEQ: accession NM_021687.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1308)
  AUTHORS   Zhang,S., Hu,S., Dong,W., Huang,S., Jiao,Z., Hu,Z., Dai,S., Yi,Y.,
            Gong,X., Li,K., Wang,H. and Xu,D.
  TITLE     Prenatal dexamethasone exposure induces anxiety- and
            depressive-like behavior of male offspring rats through
            intrauterine programming of the activation of NRG1-ErbB4 signaling
            in hippocampal PV interneurons
  JOURNAL   Cell Biol Toxicol 39 (3), 657-678 (2023)
   PUBMED   34189720
REFERENCE   2  (residues 1 to 1308)
  AUTHORS   Yuan,J., Xu,B., Ma,J., Pang,X., Fu,Y., Liang,M., Wang,M., Pan,Y.,
            Duan,Y., Tang,M., Zhu,B., Laher,I. and Li,S.
  TITLE     MOTS-c and aerobic exercise induce cardiac physiological adaptation
            via NRG1/ErbB4/CEBPbeta modification in rats
  JOURNAL   Life Sci 315, 121330 (2023)
   PUBMED   36584915
  REMARK    GeneRIF: MOTS-c and aerobic exercise induce cardiac physiological
            adaptation via NRG1/ErbB4/CEBPbeta modification in rats.
REFERENCE   3  (residues 1 to 1308)
  AUTHORS   Li,S., Wang,M., Ma,J., Pang,X., Yuan,J., Pan,Y., Fu,Y. and Laher,I.
  TITLE     MOTS-c and Exercise Restore Cardiac Function by Activating of
            NRG1-ErbB Signaling in Diabetic Rats
  JOURNAL   Front Endocrinol (Lausanne) 13, 812032 (2022)
   PUBMED   35370955
  REMARK    GeneRIF: MOTS-c and Exercise Restore Cardiac Function by Activating
            of NRG1-ErbB Signaling in Diabetic Rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1308)
  AUTHORS   Xu,L., Li,Z., Rong,J. and Lang,L.
  TITLE     Effect of regulation of the NRG1/ErbB4 signaling pathway on the
            visual cortex synaptic plasticity of amblyopic adult rats
  JOURNAL   J Biochem Mol Toxicol 35 (9), e22841 (2021)
   PUBMED   34273906
  REMARK    GeneRIF: Effect of regulation of the NRG1/ErbB4 signaling pathway
            on the visual cortex synaptic plasticity of amblyopic adult rats.
REFERENCE   5  (residues 1 to 1308)
  AUTHORS   Chen,J.L., Zhou,X., Ding,H.L., Zhan,H.L., Yang,F., Li,W.B.,
            Xie,J.C., Liu,X.G., Xu,Y.C., Su,M.Z., Liu,B.L. and Zhou,X.F.
  TITLE     Neuregulin-1-ErbB signaling promotes microglia activation
            contributing to mechanical allodynia of cyclophosphamide-induced
            cystitis
  JOURNAL   Neurourol Urodyn 38 (5), 1250-1260 (2019)
   PUBMED   30989724
REFERENCE   6  (residues 1 to 1308)
  AUTHORS   Carroll,S.L., Miller,M.L., Frohnert,P.W., Kim,S.S. and Corbett,J.A.
  TITLE     Expression of neuregulins and their putative receptors, ErbB2 and
            ErbB3, is induced during Wallerian degeneration
  JOURNAL   J Neurosci 17 (5), 1642-1659 (1997)
   PUBMED   9030624
REFERENCE   7  (residues 1 to 1308)
  AUTHORS   Riese,D.J., Kim,E.D., Elenius,K., Buckley,S., Klagsbrun,M.,
            Plowman,G.D. and Stern,D.F.
  TITLE     The epidermal growth factor receptor couples transforming growth
            factor-alpha, heparin-binding epidermal growth factor-like factor,
            and amphiregulin to Neu, ErbB-3, and ErbB-4
  JOURNAL   J Biol Chem 271 (33), 20047-20052 (1996)
   PUBMED   8702723
REFERENCE   8  (residues 1 to 1308)
  AUTHORS   Cohen,B.D., Green,J.M., Foy,L. and Fell,H.P.
  TITLE     HER4-mediated biological and biochemical properties in NIH 3T3
            cells. Evidence for HER1-HER4 heterodimers
  JOURNAL   J Biol Chem 271 (9), 4813-4818 (1996)
   PUBMED   8617750
REFERENCE   9  (residues 1 to 1308)
  AUTHORS   Gassmann,M., Casagranda,F., Orioli,D., Simon,H., Lai,C., Klein,R.
            and Lemke,G.
  TITLE     Aberrant neural and cardiac development in mice lacking the ErbB4
            neuregulin receptor
  JOURNAL   Nature 378 (6555), 390-394 (1995)
   PUBMED   7477376
REFERENCE   10 (residues 1 to 1308)
  AUTHORS   Lai,C. and Lemke,G.
  TITLE     An extended family of protein-tyrosine kinase genes differentially
            expressed in the vertebrate nervous system
  JOURNAL   Neuron 6 (5), 691-704 (1991)
   PUBMED   2025425
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Nov 27, 2020 this sequence version replaced NP_067719.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY375306.1, AF041838.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1308
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32-q33"
     Protein         1..1308
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     2 precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-4; c-erbB-4;
                     proto-oncogene-like protein c-ErbB-4; receptor tyrosine
                     kinase; v-erb-a erythroblastic leukemia viral oncogene
                     homolog 4; v-erb-b2 avian erythroblastic leukemia viral
                     oncogene 4"
                     /calculated_mol_wt=144378
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2643
     mat_peptide     26..1308
                     /product="Receptor tyrosine-protein kinase erbB-4.
                     /id=PRO_0000016675"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
                     /calculated_mol_wt=144378
     Region          55..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          186..332
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          358..478
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          502..634
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          642..685
                     /region_name="TM_ErbB4"
                     /note="Transmembrane domain of ErbB4, a Protein Tyrosine
                     Kinase; cd12092"
                     /db_xref="CDD:213053"
     Site            order(642..643,645..648,651..652,655..656,659..660,
                     663..664,667,671)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213053"
     Site            652..675
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          676..684
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          710..1012
                     /region_name="PTKc_HER4"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     HER4; cd05110"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861,882..886,891,895)
                     /site_type="active"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173655"
     Site            860..885
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173655"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            order(882..886,891,895)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173655"
     Region          1032..1035
                     /region_name="PPxy motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1202
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1284
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          1298..1301
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          1306..1308
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     CDS             1..1308
                     /gene="Erbb4"
                     /coded_by="NM_021687.3:793..4719"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:59323"
                     /db_xref="RGD:620486"
ORIGIN      
        1 mklatglwvw gsllvaartv qpsasqsvca gtenklssls dleqqyralr kyyencevvm
       61 gnleitsieh nrdlsflrsi revtgyvlva lnqfrylple nlriirgtkl yedryalaif
      121 lnyrkdgnfg lqelglknlt eilnggvyvd qnkflcyadt ihwqdivrnp wpsnmtlvst
      181 igssgcgrch ksctgrcwgp tenhcqtltr tvcaeqcdgr cygpyvsdcc hrecaggcsg
      241 pkdtdcfacm nfndsgacvt qcpqtfvynp ttfqlehnfn akytygafcv kkcphnfvvd
      301 ssscvracps skmeveengi kmckpctdic pkacdgigtg slmsaqtvds snidkfinct
      361 kingnliflv tgihgdpyna idaidpekln vfrtvreitg flniqswppn mtdfsvfsnl
      421 vtiggrvlys glsllilkqq gitslqfqsl keisagniyi tdnsnlcyyh tinwttlfst
      481 vnqrivirdn rraenctaeg mvcnhlcsnd gcwgpgpdqc lscrrfsrgk iciescnlyd
      541 gefrefengs icvecdsqce kmedglltch gpgpdnctkc shfkdgpncv ekcpdglqga
      601 nsfifkyadq drechpchpn ctqgcngpts hdciyypwtg hstlpqhart pliaagvigg
      661 lfilvimalt favyvrrksi kkkralrrfl etelvepltp sgtapnqaql rilketelkr
      721 vkvlgsgafg tvykgiwvpe getvkipvai kilnettgpk anvefmdeal imasvdhphl
      781 vrllgvclsp tiqlvtqlmp hgclleyvhe hkdnigsqll lnwcvqiakg mmyleerrlv
      841 hrdlaarnvl vkspnhvkit dfglarlleg dekeynadgg kmpikwmale cihyrkfthq
      901 sdvwsygvti welmtfggkp ydgiptreip dllekgerlp qppictidvy mvmvkcwmid
      961 adsrpkfkel aaefsrmard pqrylviqgd drmklpspnd skffqnllde edledmmdae
     1021 eylvpqafni pppiytsrtr idsnrseigh spppaytpms gnqfvyqdgg fatqqgmpmp
     1081 yrattstipe apvaqgatae mfddsccngt lrkpvvphvq edsstqrysa dptvfapern
     1141 praeldeegy mtpmhdkpkq eylnpveenp fvsrrkngdl qaldnpeyhs assgppkaed
     1201 eyvneplyln tftnalgnae ymknsllsvp ekakkafdnp dywnhslppr stlqhpdylq
     1261 eystkyfykq ngrirpivae npeylsefsl kpgtmlpppp yrhrntvv
//
LOCUS       NP_001099791            1600 aa            linear   ROD 07-APR-2025
DEFINITION  low-density lipoprotein receptor-related protein 5 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001099791 XP_001067386 XP_215187
VERSION     NP_001099791.2
DBSOURCE    REFSEQ: accession NM_001106321.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1600)
  AUTHORS   Ubels,J.L., Lin,C.M., Antonetti,D.A., Diaz-Coranguez,M.,
            Diegel,C.R. and Williams,B.O.
  TITLE     Structure and function of the retina of low-density lipoprotein
            receptor-related protein 5 (Lrp5)-deficient rats
  JOURNAL   Exp Eye Res 217, 108977 (2022)
   PUBMED   35139333
  REMARK    GeneRIF: Structure and function of the retina of low-density
            lipoprotein receptor-related protein 5 (Lrp5)-deficient rats.
REFERENCE   2  (residues 1 to 1600)
  AUTHORS   Ju,S., Lim,L., Wi,K., Park,C., Ki,Y.J., Choi,D.H. and Song,H.
  TITLE     LRP5 Regulates HIF-1alpha Stability via Interaction with PHD2 in
            Ischemic Myocardium
  JOURNAL   Int J Mol Sci 22 (12), 6581 (2021)
   PUBMED   34205318
  REMARK    GeneRIF: LRP5 Regulates HIF-1alpha Stability via Interaction with
            PHD2 in Ischemic Myocardium.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1600)
  AUTHORS   Ubels,J.L., Diegel,C.R., Foxa,G.E., Ethen,N.J., Lensing,J.N.,
            Madaj,Z.B. and Williams,B.O.
  TITLE     Low-Density Lipoprotein Receptor-Related Protein 5-Deficient Rats
            Have Reduced Bone Mass and Abnormal Development of the Retinal
            Vasculature
  JOURNAL   CRISPR J 3 (4), 284-298 (2020)
   PUBMED   32833527
  REMARK    GeneRIF: Low-Density Lipoprotein Receptor-Related Protein
            5-Deficient Rats Have Reduced Bone Mass and Abnormal Development of
            the Retinal Vasculature.
REFERENCE   4  (residues 1 to 1600)
  AUTHORS   Ergun,S.G., Akay,G.G., Ergun,M.A. and Percin,E.F.
  TITLE     LRP5-linked osteoporosis-pseudoglioma syndrome mimicking isolated
            microphthalmia
  JOURNAL   Eur J Med Genet 60 (3), 200-204 (2017)
   PUBMED   28111184
REFERENCE   5  (residues 1 to 1600)
  AUTHORS   Huang,W., Li,Q., Amiry-Moghaddam,M., Hokama,M., Sardi,S.H.,
            Nagao,M., Warman,M.L. and Olsen,B.R.
  TITLE     Critical Endothelial Regulation by LRP5 during Retinal Vascular
            Development
  JOURNAL   PLoS One 11 (3), e0152833 (2016)
   PUBMED   27031698
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1600)
  AUTHORS   Kato,M., Patel,M.S., Levasseur,R., Lobov,I., Chang,B.H., Glass,D.A.
            2nd, Hartmann,C., Li,L., Hwang,T.H., Brayton,C.F., Lang,R.A.,
            Karsenty,G. and Chan,L.
  TITLE     Cbfa1-independent decrease in osteoblast proliferation, osteopenia,
            and persistent embryonic eye vascularization in mice deficient in
            Lrp5, a Wnt coreceptor
  JOURNAL   J Cell Biol 157 (2), 303-314 (2002)
   PUBMED   11956231
REFERENCE   7  (residues 1 to 1600)
  AUTHORS   Gong,Y., Slee,R.B., Fukai,N., Rawadi,G., Roman-Roman,S.,
            Reginato,A.M., Wang,H., Cundy,T., Glorieux,F.H., Lev,D.,
            Zacharin,M., Oexle,K., Marcelino,J., Suwairi,W., Heeger,S.,
            Sabatakos,G., Apte,S., Adkins,W.N., Allgrove,J.,
            Arslan-Kirchner,M., Batch,J.A., Beighton,P., Black,G.C.,
            Boles,R.G., Boon,L.M., Borrone,C., Brunner,H.G., Carle,G.F.,
            Dallapiccola,B., De Paepe,A., Floege,B., Halfhide,M.L., Hall,B.,
            Hennekam,R.C., Hirose,T., Jans,A., Juppner,H., Kim,C.A.,
            Keppler-Noreuil,K., Kohlschuetter,A., LaCombe,D., Lambert,M.,
            Lemyre,E., Letteboer,T., Peltonen,L., Ramesar,R.S., Romanengo,M.,
            Somer,H., Steichen-Gersdorf,E., Steinmann,B., Sullivan,B.,
            Superti-Furga,A., Swoboda,W., van den Boogaard,M.J., Van Hul,W.,
            Vikkula,M., Votruba,M., Zabel,B., Garcia,T., Baron,R., Olsen,B.R.
            and Warman,M.L.
  CONSRTM   Osteoporosis-Pseudoglioma Syndrome Collaborative Group
  TITLE     LDL receptor-related protein 5 (LRP5) affects bone accrual and eye
            development
  JOURNAL   Cell 107 (4), 513-523 (2001)
   PUBMED   11719191
REFERENCE   8  (residues 1 to 1600)
  AUTHORS   Mao,J., Wang,J., Liu,B., Pan,W., Farr,G.H. 3rd, Flynn,C., Yuan,H.,
            Takada,S., Kimelman,D., Li,L. and Wu,D.
  TITLE     Low-density lipoprotein receptor-related protein-5 binds to Axin
            and regulates the canonical Wnt signaling pathway
  JOURNAL   Mol Cell 7 (4), 801-809 (2001)
   PUBMED   11336703
REFERENCE   9  (residues 1 to 1600)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   10 (residues 1 to 1600)
  AUTHORS   Dong,Y., Lathrop,W., Weaver,D., Qiu,Q., Cini,J., Bertolini,D. and
            Chen,D.
  TITLE     Molecular cloning and characterization of LR3, a novel LDL receptor
            family protein with mitogenic activity
  JOURNAL   Biochem Biophys Res Commun 251 (3), 784-790 (1998)
   PUBMED   9790987
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC166786.1.
            
            On May 20, 2008 this sequence version replaced NP_001099791.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1600
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42-q43"
     Protein         1..1600
                     /product="low-density lipoprotein receptor-related protein
                     5 isoform 2 precursor"
                     /note="low-density lipoprotein receptor-related protein 5"
                     /calculated_mol_wt=174296
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3153
     Region          23..214
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          102..142
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          163..203
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          187..229
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          230..271
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          299..336
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          366..406
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          408..450
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          451..494
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          495..537
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          538..571
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          605..640
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <654..782
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          710..752
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          799..838
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          838..879
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          906..941
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          970..1009
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1060..1103
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1104..1146
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1217..1253
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1259..1295
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1264,1274,1285..1286)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1278,1281,1285,1291..1292)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1288..1292
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1321..1355
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1326,1334,1345..1346)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1338,1341,1345,1351..1352)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1348..1352
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1600
                     /gene="Lrp5"
                     /coded_by="NM_001106321.2:81..4883"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:293649"
                     /db_xref="RGD:1309329"
ORIGIN      
        1 metaptrapp pppqplllll alccslvpaa asplllfanr rdvrlvdagg vklestivas
       61 gledaaavdf qfskgavywt dvseeaikqt ylnqtgaaaq nivisglvsp dglacdwvgk
      121 klywtdsetn rievanlngt srkvlfwqdl dqpraialdp ahgymywtdw geaprierag
      181 mdgstrkiiv dsdiywpngl tidleeqkly wadaklsfih ranldgsfrq kvvegslthp
      241 faltlsgdtl ywtdwqtrsi hacnkwtgek rkeilsalys pmdiqvlsqe rqppfhtpce
      301 egnggcshlc llsprepfys cacptgvqlq dngktckaga eevlllarrt dlrrisldtp
      361 dftdivlqvg dirhaiaidy dplegyvywt ddevrairra yldgsgaqtl vnteindpdg
      421 iavdwvarnl ywtdtgtdri evtrlngtsr kilvsedlde praivlhpvm glmywtdwge
      481 npkiecanld grdrhvlvnt slgwpnglal dlqegklywg daktdkievi nidgtkrqtl
      541 ledklphifg ftllgdfiyw tdwqrrsier vhkvkasrdv iidqlpdlmg lkavnvakvv
      601 gtnpcadgng gcshlcfftp hatkcgcpig lellsdmktc iipeaflvft sratihrisl
      661 etnnndvaip ltgvkeasal dfdvsnnhiy wtdvslktis rafmngssve hviefgldyp
      721 egmavdwmgk nlywadtgtn rievarldgq frqvlvwrdl dnprslaldp tkgyiywtew
      781 ggkprivraf mdgtncmtlv dkvgrandlt idyadqrlyw tdldtnmies snmlgqermv
      841 iaddlpypfg ltqysdyiyw tdwnlhsier adktsgrnrt liqghldfvm dilvfhssrq
      901 dglndcvhsn gqcgqlclai pgghrcgcas hytldpssrn csppstfllf sqkfaisrmi
      961 pddqlspdli lplhglrnvk ainydpldkf iywvdgrqni krakddgtqp smltspsqsl
     1021 spdrqphdls idiysrtlfw tceatntinv hrldgdamgv vlrgdrdrpr aiavnaergy
     1081 myftnmqdha akierasldg terevlfttg lirpvalvvd nalgklfwvd adlkriescd
     1141 lsganrltle danivqpvgl tvlgrhlywi drqqqmierv ekttgdkrtr vqgrvthltg
     1201 ihaveevsle efsahpcard nggcshicia kgdgtprcsc pvhlvllqnl ltcgepptcs
     1261 pdqfacatge idcipgawrc dgfpecadqs deegcpvcsa sqfpcargqc vdlrlrcdav
     1321 clpnqfrcas gqcvlikqqc dsfpdcadgs delmceinkp psddvpahss aigpvigiil
     1381 slfvmggvyf vcqrvmcqry tgasgpfphe yvggtphvpl nfiapggsqh gpfpgipcsk
     1441 smmssvslvg grgsvplydr nhvtgassss ssstkatlyp pilnpppspa tdpslynmdm
     1501 fyssnipsta rpyrpyiirg mappttpcst dvcdsdysts rwktskyyld lnsdsdpypp
     1561 pptphsqyls aedscppspv tersychlfp pppspctdss
//
LOCUS       NP_001100358            1078 aa            linear   ROD 07-APR-2025
DEFINITION  BRD4-interacting chromatin-remodeling complex-associated
            protein-like [Rattus norvegicus].
ACCESSION   NP_001100358 XP_001065444 XP_217342
VERSION     NP_001100358.1
DBSOURCE    REFSEQ: accession NM_001106888.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Alpsoy,A. and Dykhuizen,E.C.
  TITLE     Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its
            paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes
  JOURNAL   J Biol Chem 293 (11), 3892-3903 (2018)
   PUBMED   29374058
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473987.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217342.4, XP_001065444.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..1078
                     /product="BRD4-interacting chromatin-remodeling
                     complex-associated protein-like"
                     /note="GLTSCR1-like; BRD4 interacting chromatin remodeling
                     complex associated protein like; BRD4 interacting
                     chromatin remodelling complex associated protein like"
                     /calculated_mol_wt=114332
     Region          498..>670
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          712..812
                     /region_name="GLTSCR1"
                     /note="Conserved region of unknown function on GLTSCR
                     protein; pfam15249"
                     /db_xref="CDD:464589"
     CDS             1..1078
                     /gene="Bicral"
                     /gene_synonym="Gltscr1l; RGD1305680"
                     /coded_by="NM_001106888.1:66..3302"
                     /db_xref="GeneID:301235"
                     /db_xref="RGD:1305680"
ORIGIN      
        1 mdddddscll dligdpqaln yflhgpssks sgddvtnagy saansnsifa nstnadpkss
       61 lkgvsnqlge gpsdglplas slqfledele ssplpdlsed qpfdilqksl qeaniteqtl
      121 aeeayldasi gssqqfaqaq lhpsssasft qasnvsnysg qtlqpigvth vpvgasfasn
      181 tvgvqhgfmq hvgisvpsqh lpnssqisgs gqiqligsfg nqpsmmtinn ldgsqiilkg
      241 sgqqapssvs ggllvhrqtp ngnslfgnpt sspgaqpvtv pfnstnfqas lpvhniiiqr
      301 glapnsnkvp iniqpkpiqm gqqstynvns lglqqhhvqq gisfasassp qgsvvgphms
      361 vnivnqqnar kpvtsqavss aggsivihsp mgqphtpqsq fliptslsvs snsvhhvqti
      421 ngqlvqtqps qlisgqvase hvmlnrnssn mlrtnqpyag qmlnnqsaav qlvsgqtfat
      481 sgspvivnha spqivggqmp lqqasptvlh lspgqssvsq grpgfatmas vssmsgparf
      541 pavssastah ptlgpavqsg asgsnftgdq ltqanrtpvp vsvshrlpvs askspstlss
      601 tpgtqqqffc qapkkclnqt apiptpipts kttdslrqpq ipgllstalp gqdcgskimp
      661 aplgttqpqq ensvgsspsq tavqvdshsg qkrpaakqlt kgafilqqlq rdqahavtpd
      721 ksqfrsltdt vqrllsyhvc qgsmpteedl skvdsefeev atqllkrtha mlnkyrslll
      781 edamrinpsa emvmidrmfn qeeraslsrd krlalvdpeg fqadfccsfk ldeaapetpl
      841 drsdqhrskt sslhqvpraq srdrakpgva eatnhdqfhl vpnhivvsae gniskksegh
      901 srtlkfdkgv lgqyrgpped kggrrdpaka sgcspgpegh rktlprpdhg sesklpgila
      961 sshmempcld sfqdkalrns pknevlhtdi mkgsgepqpd lqltkslekt fknilelkna
     1021 grpqndpaas gavdldfpsf spmasqencl ekfipdhseg vvetdsilea avnsilec
//
LOCUS       NP_001421078             706 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001421078 XP_008762916
VERSION     NP_001421078.1
DBSOURCE    REFSEQ: accession NM_001434149.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_008762916.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.822523.1,
                                           SRR26360190.2871652.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..706
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 7"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=78733
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          449..528
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(517..518,520..521)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          525..696
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..706
                     /gene="Trim9"
                     /coded_by="NM_001434149.1:162..2282"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkvpatp ilqleeccth nnsatlswkq pplstvaadg yilelddgsg
      481 gqfrevyvgk etmctvdglh fnstynarvk afnktgvspy sktlvlqtse vawfafdpgs
      541 ahsdiifsnd nltvtcssyd drvvlgktgf skgvhywelt idrydnhpdp afgvaridvm
      601 kdmmlgkddk awamyvdnnr swfmhnnsht nrteggitkg atigvlldln rktltffvnn
      661 eqqgpiafen veglffpavs lnrnvqvtlh tglpvpdfys srasia
//
LOCUS       NP_001421073             806 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001421073 XP_008762913
VERSION     NP_001421073.1
DBSOURCE    REFSEQ: accession NM_001434144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 806)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 806)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 806)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_008762913.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.35815.1,
                                           SRR26360194.1716999.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..806
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=89709
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          631..796
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..806
                     /gene="Trim9"
                     /coded_by="NM_001434144.1:162..2582"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtseaagahe
      541 tkpmkdtdse eqtlpfpvps erlplrrmsp fsstlnlqps fpgrsyfdfr ssphqlslhs
      601 slqslnapgc nfetqsasys qlvdikklla vawfafdpgs ahsdiifsnd nltvtcssyd
      661 drvvlgktgf skgvhywelt idrydnhpdp afgvaridvm kdmmlgkddk awamyvdnnr
      721 swfmhnnsht nrteggitkg atigvlldln rktltffvnn eqqgpiafen veglffpavs
      781 lnrnvqvtlh tglpvpdfys srasia
//
LOCUS       NP_001421076             788 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001421076 XP_008762914
VERSION     NP_001421076.1
DBSOURCE    REFSEQ: accession NM_001434147.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 788)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 788)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 788)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 788)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_008762914.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.35817.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..788
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 5"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=87417
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          631..778
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..788
                     /gene="Trim9"
                     /coded_by="NM_001434147.1:162..2528"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtseaagahe
      541 tkpmkdtdse eqtlpfpvps erlplrrmsp fsstlnlqps fpgrsyfdfr ssphqlslhs
      601 slqslnapgc nfetqsasys qlvdikklla vawfafdpgs ahsdiifsnd nltvtcssyd
      661 drvvlgktgf skgvhywelt idrydnhpdp afgvaridvm kdmmlgkddk awaiteggit
      721 kgatigvlld lnrktltffv nneqqgpiaf enveglffpa vslnrnvqvt lhtglpvpdf
      781 yssrasia
//
LOCUS       NP_001421077             787 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001421077 XP_008762915
VERSION     NP_001421077.1
DBSOURCE    REFSEQ: accession NM_001434148.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 787)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 787)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 787)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 787)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 787)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_008762915.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.908550.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..787
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 6"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=87346
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          630..777
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..787
                     /gene="Trim9"
                     /coded_by="NM_001434148.1:162..2525"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtseagahet
      541 kpmkdtdsee qtlpfpvpse rlplrrmspf sstlnlqpsf pgrsyfdfrs sphqlslhss
      601 lqslnapgcn fetqsasysq lvdikkllav awfafdpgsa hsdiifsndn ltvtcssydd
      661 rvvlgktgfs kgvhywelti drydnhpdpa fgvaridvmk dmmlgkddka waiteggitk
      721 gatigvlldl nrktltffvn neqqgpiafe nveglffpav slnrnvqvtl htglpvpdfy
      781 ssrasia
//
LOCUS       NP_001421079             692 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001421079 XP_038967634
VERSION     NP_001421079.1
DBSOURCE    REFSEQ: accession NM_001434150.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_038967634.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1223218.1,
                                           SRR26360194.2377084.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..692
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 8"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=76783
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          529..682
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..692
                     /gene="Trim9"
                     /coded_by="NM_001434150.1:162..2240"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtsevawfaf
      541 dpgsahsdii fsndnltvtc ssyddrvvlg ktgfskgvhy weltidrydn hpdpafgvar
      601 idvmkdmmlg kddkawaite ggitkgatig vlldlnrktl tffvnneqqg piafenvegl
      661 ffpavslnrn vqvtlhtglp vpdfyssras ia
//
LOCUS       NP_001421074             805 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001421074 XP_017449485
VERSION     NP_001421074.1
DBSOURCE    REFSEQ: accession NM_001434145.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_017449485.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1064931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..805
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=89638
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          630..795
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..805
                     /gene="Trim9"
                     /coded_by="NM_001434145.1:162..2579"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtseagahet
      541 kpmkdtdsee qtlpfpvpse rlplrrmspf sstlnlqpsf pgrsyfdfrs sphqlslhss
      601 lqslnapgcn fetqsasysq lvdikkllav awfafdpgsa hsdiifsndn ltvtcssydd
      661 rvvlgktgfs kgvhywelti drydnhpdpa fgvaridvmk dmmlgkddka wamyvdnnrs
      721 wfmhnnshtn rteggitkga tigvlldlnr ktltffvnne qqgpiafenv eglffpavsl
      781 nrnvqvtlht glpvpdfyss rasia
//
LOCUS       NP_569104                710 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 1 [Rattus norvegicus].
ACCESSION   NP_569104
VERSION     NP_569104.1
DBSOURCE    REFSEQ: accession NM_130420.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF350422.1, SRR26360190.465027.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..710
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=79075
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          529..700
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..710
                     /gene="Trim9"
                     /coded_by="NM_130420.2:162..2294"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtsevawfaf
      541 dpgsahsdii fsndnltvtc ssyddrvvlg ktgfskgvhy weltidrydn hpdpafgvar
      601 idvmkdmmlg kddkawamyv dnnrswfmhn nshtnrtegg itkgatigvl ldlnrktltf
      661 fvnneqqgpi afenveglff pavslnrnvq vtlhtglpvp dfyssrasia
//
LOCUS       NP_001421075             795 aa            linear   ROD 07-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM9 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001421075 XP_017449488
VERSION     NP_001421075.1
DBSOURCE    REFSEQ: accession NM_001434146.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Li,J. and Zeng,Q.
  TITLE     Trim9 regulates the directional differentiation of retinal Muller
            cells to retinal ganglion cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (10), 1561-1571 (2023)
   PUBMED   38432885
  REMARK    GeneRIF: Trim9 regulates the directional differentiation of retinal
            Muller cells to retinal ganglion cells.
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Zeng,Q., Zhou,J. and Hua,X.
  TITLE     TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7
  JOURNAL   In Vitro Cell Dev Biol Anim 59 (8), 586-595 (2023)
   PUBMED   37792226
  REMARK    GeneRIF: TRIM9 promotes Muller cell-derived retinal stem cells to
            differentiate into retinal ganglion cells by regulating Atoh7.
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Morikawa,R.K., Kanamori,T., Yasunaga,K. and Emoto,K.
  TITLE     Different levels of the Tripartite motif protein, Anomalies in
            sensory axon patterning (Asap), regulate distinct axonal
            projections of Drosophila sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19389-19394 (2011)
   PUBMED   22084112
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Tanji,K., Kamitani,T., Mori,F., Kakita,A., Takahashi,H. and
            Wakabayashi,K.
  TITLE     TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
            the brain of Parkinson's disease and dementia with Lewy bodies
  JOURNAL   Neurobiol Dis 38 (2), 210-218 (2010)
   PUBMED   20085810
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Li,Y., Chin,L.S., Weigel,C. and Li,L.
  TITLE     Spring, a novel RING finger protein that regulates synaptic vesicle
            exocytosis
  JOURNAL   J Biol Chem 276 (44), 40824-40833 (2001)
   PUBMED   11524423
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Koroll,M., Rathjen,F.G. and Volkmer,H.
  TITLE     The neural cell recognition molecule neurofascin interacts with
            syntenin-1 but not with syntenin-2, both of which reveal
            self-associating activity
  JOURNAL   J Biol Chem 276 (14), 10646-10654 (2001)
   PUBMED   11152476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 22, 2024 this sequence version replaced XP_017449488.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1999247.1,
                                           SRR26360194.1756340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..795
                     /product="E3 ubiquitin-protein ligase TRIM9 isoform 4"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 9; E3
                     ubiquitin-protein ligase TRIM9; SNAP-25-interacting RING
                     finger protein; tripartite motif protein 9; Spring;
                     RING-type E3 ubiquitin transferase TRIM9"
                     /calculated_mol_wt=88587
     Region          5..49
                     /region_name="RING-HC_TRIM9"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd16755"
                     /db_xref="CDD:438413"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7M3; propagated from
                     UniProtKB/Swiss-Prot (Q91ZY8.1)"
     Region          166..212
                     /region_name="Bbox1_TRIM9_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19843"
                     /db_xref="CDD:380901"
     Region          223..271
                     /region_name="Bbox2_TRIM9_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 9 (TRIM9) and similar proteins;
                     cd19826"
                     /db_xref="CDD:380884"
     Region          273..399
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Region          453..532
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(521..522,524..525)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          620..785
                     /region_name="SPRY_PRY_TRIM67_9"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     proteins, TRIM9 and TRIM67; cd12889"
                     /db_xref="CDD:293947"
     CDS             1..795
                     /gene="Trim9"
                     /coded_by="NM_001434146.1:162..2549"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:155812"
                     /db_xref="RGD:621540"
ORIGIN      
        1 meemeeelkc pvcgsfyrep iilpcshnlc qacarnilvq tpesespqsr rasgsgvsdy
       61 dyldldkmsl yseadsgygs yggfasaptt pcqkspngvr vfppampppp thlspalapv
      121 prnscitcpq chrslilddr glrgfpknrv legvidryqq skaaalkcql cekapkeatv
      181 mceqcdvfyc dpcrlrchpp rgplakhrlv ppaqgrvsrr lsprkvstct dhelenhsmy
      241 cvqckmpvcy qcleegkhss hevkalgamw klhksqlsqa lnglsdrake akeflvqlrt
      301 mvqqiqensv efeaclvaqc dalidalnrr kaqllarvnk ehehklkvvr dqishctvkl
      361 rqttglmeyc levikendps gflqisdali rrvhltedqw gkgtltprmt tdfdlsldns
      421 pllqsihqld fvqvkasspv patpilqlee ccthnnsatl swkqpplstv aadgyileld
      481 dgsggqfrev yvgketmctv dglhfnstyn arvkafnktg vspysktlvl qtsedtdsee
      541 qtlpfpvpse rlplrrmspf sstlnlqpsf pgrsyfdfrs sphqlslhss lqslnapgcn
      601 fetqsasysq lvdikkllav awfafdpgsa hsdiifsndn ltvtcssydd rvvlgktgfs
      661 kgvhywelti drydnhpdpa fgvaridvmk dmmlgkddka wamyvdnnrs wfmhnnshtn
      721 rteggitkga tigvlldlnr ktltffvnne qqgpiafenv eglffpavsl nrnvqvtlht
      781 glpvpdfyss rasia
//
LOCUS       NP_001424493             765 aa            linear   ROD 08-APR-2025
DEFINITION  rasGAP-activating-like protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424493
VERSION     NP_001424493.2
DBSOURCE    REFSEQ: accession NM_001437564.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Hong,Y., Han,Y.Q., Wang,Y.Z., Gao,J.R., Li,Y.X., Liu,Q. and
            Xia,L.Z.
  TITLE     Paridis Rhizoma Sapoinins attenuates liver fibrosis in rats by
            regulating the expression of RASAL1/ERK1/2 signal pathway
  JOURNAL   J Ethnopharmacol 192, 114-122 (2016)
   PUBMED   27396351
  REMARK    GeneRIF: Paridis rhizoma sapoinins attenuate CCl4-induced liver
            fibrosis through the regulation of RASAL1/ERK1/2 signal pathway.
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Yoo,J.C., Lim,Ty., Park,J.S., Hah,Y.S., Park,N., Hong,S.G.,
            Park,J.Y. and Yoon,T.J.
  TITLE     SYT14L, especially its C2 domain, is involved in regulating
            melanocyte differentiation
  JOURNAL   J Dermatol Sci 72 (3), 246-251 (2013)
   PUBMED   23999003
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Tao,H., Huang,C., Yang,J.J., Ma,T.T., Bian,E.B., Zhang,L., Lv,X.W.,
            Jin,Y. and Li,J.
  TITLE     MeCP2 controls the expression of RASAL1 in the hepatic fibrosis in
            rats
  JOURNAL   Toxicology 290 (2-3), 327-333 (2011)
   PUBMED   22056649
  REMARK    GeneRIF: hypermethylation of RASAL1 is associated with the
            perpetuation of fibroblast activation and fibrogenesis in the liver
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Liu,Q., Walker,S.A., Gao,D., Taylor,J.A., Dai,Y.F., Arkell,R.S.,
            Bootman,M.D., Roderick,H.L., Cullen,P.J. and Lockyer,P.J.
  TITLE     CAPRI and RASAL impose different modes of information processing on
            Ras due to contrasting temporal filtering of Ca2+
  JOURNAL   J Cell Biol 170 (2), 183-190 (2005)
   PUBMED   16009725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 8, 2025 this sequence version replaced NP_001424493.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2410031.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN12840109,
                                           SAMN12840117 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..765
                     /product="rasGAP-activating-like protein 1 isoform 2"
                     /note="rasGAP-activating-like protein 1; RAS protein
                     activator like 1 (GAP1 like)"
                     /calculated_mol_wt=85223
     Region          6..88
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          96..216
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          224..512
                     /region_name="RasGAP"
                     /note="Ras GTPase Activating Domain; cl02569"
                     /db_xref="CDD:470620"
     Site            order(263,299,301,303..304,306,309,313,424,432..433,
                     436..437,440,461,464..465,470,474,476,483..484)
                     /site_type="other"
                     /note="RAS interface [polypeptide binding]"
                     /db_xref="CDD:213337"
     Region          516..653
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          645..673
                     /region_name="BTK"
                     /note="BTK motif; pfam00779"
                     /db_xref="CDD:459937"
     CDS             1..765
                     /gene="Rasal1"
                     /coded_by="NM_001437564.2:250..2547"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360814"
                     /db_xref="RGD:1311820"
ORIGIN      
        1 maksgslsir vvegralpak dvsgssdpyc lvkvddevva rhddiigkis lskeaitadp
       61 rgidswinls rvdpdeevqg evclavklle dargrclrch vrqardlapr disgtsdpfa
      121 rvfwgsrsle tstikktrfp hwdevlelre apgttsplrv elwdwdmvgk ndflgmveft
      181 pqtlqqkppn gwfrllpfpr aedsggslga lrlkvrlted rvlpsqyyqp lmelllesvq
      241 gpaeedttsp lalleelasg dcrqdlatkl vklflgrgla gpfldyltrr evartndpnt
      301 lfrsnslask smeqfmklvg mrylhevlrp visrvfeekk ymeldpskmd lnrsrrisfk
      361 gtpteeqvre tslglltgyl gsvvdaivss agrcplalrl afkqlqqcve krfpgmehqd
      421 vkylatsgfl flrffapail tpklfdlrdh hadpqtsrsl lllakvcavq signlgqqlg
      481 qgkeqwlapl hpfllqsisr vrdfldqlvd vdgdeeaggs tcalvqpsti vregfllkrk
      541 eepaslatrf afkkryfrls grdlsysktp ewqvhssipl sciravervd egafqlphvm
      601 qvvtqdgtga shttylqckn vndlnqwlsa lrkasapnpg klaachpgaf rsgrwtcclq
      661 aersavgcsr thsavtlgdw sdpldpdaea qmvyrqlllg rdqlrlklle dssldtapdv
      721 dpgkdssavd gpcaevlaqq reattrllqv ledleqahee fqkrg
//
LOCUS       NP_001424607             578 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424607 XP_006245054
VERSION     NP_001424607.1
DBSOURCE    REFSEQ: accession NM_001437678.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_006245054.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2291159.1,
                                           SRR26360194.619984.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..578
                     /product="SPATS2-like protein isoform 1"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=63767
     Region          79..388
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..578
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437678.1:173..1909"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgiteg srllqqkmsl
      181 dgnpkaihgp sersdglqws agqpcnpskp kaktspvksn apaahleikp delakkrgpn
      241 ieksvkdlqr ctvsltryrv mikeevdssv kkikaafael hnciidkevs lmaemdkvke
      301 eamdiltarq kkaeelkrlt dlasqmaemq laelraeikh fvserkydee lgkaarfscd
      361 ieqlkaqili cgeithpknn yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg
      421 kaanpkmvsg lpstadacqq tmptnkqqng psnqrrrfnp qyhnrlngpa ksqgsgnead
      481 pmvksnnrhe hrrqphngfr pknkggaknq eaplgtkape apphsekarr rqhaadnlet
      541 rpfrgnvgrv sqcnlcptri evsteatvls vpavtlva
//
LOCUS       NP_001424605             578 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424605 XP_038939556
VERSION     NP_001424605.1
DBSOURCE    REFSEQ: accession NM_001437676.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_038939556.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.91717.1,
                                           SRR26360194.791331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..578
                     /product="SPATS2-like protein isoform 1"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=63767
     Region          79..388
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..578
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437676.1:186..1922"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgiteg srllqqkmsl
      181 dgnpkaihgp sersdglqws agqpcnpskp kaktspvksn apaahleikp delakkrgpn
      241 ieksvkdlqr ctvsltryrv mikeevdssv kkikaafael hnciidkevs lmaemdkvke
      301 eamdiltarq kkaeelkrlt dlasqmaemq laelraeikh fvserkydee lgkaarfscd
      361 ieqlkaqili cgeithpknn yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg
      421 kaanpkmvsg lpstadacqq tmptnkqqng psnqrrrfnp qyhnrlngpa ksqgsgnead
      481 pmvksnnrhe hrrqphngfr pknkggaknq eaplgtkape apphsekarr rqhaadnlet
      541 rpfrgnvgrv sqcnlcptri evsteatvls vpavtlva
//
LOCUS       NP_001424604             509 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424604 XP_038939558
VERSION     NP_001424604.1
DBSOURCE    REFSEQ: accession NM_001437675.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_038939558.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.25664.1,
                                           SRR26643297.31713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..509
                     /product="SPATS2-like protein isoform 3"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=56371
     Region          79..319
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..509
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437675.1:187..1716"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgitgp nieksvkdlq
      181 rctvsltryr vmikeevdss vkkikaafae lhnciidkev slmaemdkvk eeamdiltar
      241 qkkaeelkrl tdlasqmaem qlaelraeik hfvserkyde elgkaarfsc dieqlkaqil
      301 icgeithpkn nyssrtpcss llpllnthav asgkqgnfsr kssghnkpne gkaanpkmvs
      361 glpstadacq qtmptnkqqn gpsnqrrrfn pqyhnrlngp aksqgsgnea dpmvksnnrh
      421 ehrrqphngf rpknkggakn qeaplgtkap eapphsekar rrqhaadnle trpfrgnvgr
      481 vsqcnlcptr ievsteatvl svpavtlva
//
LOCUS       NP_001424589             623 aa            linear   ROD 08-APR-2025
DEFINITION  calcium-responsive transcription factor isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424589
VERSION     NP_001424589.1
DBSOURCE    REFSEQ: accession NM_001437660.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Zheng,F., Zhou,X., Luo,Y., Xiao,H., Wayman,G. and Wang,H.
  TITLE     Regulation of brain-derived neurotrophic factor exon IV
            transcription through calcium responsive elements in cortical
            neurons
  JOURNAL   PLoS One 6 (12), e28441 (2011)
   PUBMED   22174809
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Hasan,M.K., Yaguchi,T., Sugihara,T., Kumar,P.K., Taira,K.,
            Reddel,R.R., Kaul,S.C. and Wadhwa,R.
  TITLE     CARF is a novel protein that cooperates with mouse p19ARF (human
            p14ARF) in activating p53
  JOURNAL   J Biol Chem 277 (40), 37765-37770 (2002)
   PUBMED   12154087
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Tao,X., West,A.E., Chen,W.G., Corfas,G. and Greenberg,M.E.
  TITLE     A calcium-responsive transcription factor, CaRF, that regulates
            neuronal activity-dependent expression of BDNF
  JOURNAL   Neuron 33 (3), 383-395 (2002)
   PUBMED   11832226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.50740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..623
                     /product="calcium-responsive transcription factor isoform
                     2"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 8; calcium-response factor;
                     amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8 protein"
                     /calculated_mol_wt=68835
     Region          201..433
                     /region_name="ALS2CR8"
                     /note="Amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8; pfam15299"
                     /db_xref="CDD:464625"
     CDS             1..623
                     /gene="Carf"
                     /gene_synonym="Als2cr8"
                     /coded_by="NM_001437660.1:172..2043"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:301446"
                     /db_xref="RGD:1306822"
ORIGIN      
        1 mdsgdpslgq ndpptilpnt vpethdplts qnipetltdt qalheeqfhl ldqngqpiqy
       61 dlqslgnsta qmtgmeqvvi pqesfadvcs ppgvseekpi ggslpavstd aledsassys
      121 lhsqaslvgp rksgtrtlee pllaplqpls cntpmwacrl rscekigdsy rgycvsetel
      181 esvltfhkqq tqtvwgtrqs pspakpatrl mwksqyvpyd gipfvnagsr avvmecqygp
      241 rrkgfqlkki seqesrschl ykatcpariy ikkvqkfpdy rvptdpqidr ktirmeqeka
      301 ftmlkknlvd aggvlrwyvq lptqqahqyh epetpgvpls pspfpmsple eeeaiirden
      361 cvlpsrlhpq vahkiqelvs qgvgqvyavr kqlrkfvere lfkpdevper hnlsffptvn
      421 diknhihevq kslqtgdvvy nseiipatlq wttdsgnilr etvtvtfaeg nllkepitsk
      481 mgtsqtqtsl speplpllsp lssfqpkift hlqsqnlgtd tclpenssta spmgslpesv
      541 qnlvavdqlv ggedaedagn legnvkrtll gdahtipihi ldshpalvee dtlsmnqvkq
      601 epneptlste aktlldcknv sat
//
LOCUS       NP_001424603             577 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424603 XP_063123268
VERSION     NP_001424603.1
DBSOURCE    REFSEQ: accession NM_001437674.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_063123268.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.48892.1,
                                           SRR26643299.39360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..577
                     /product="SPATS2-like protein isoform 2"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=63639
     Region          79..388
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..577
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437674.1:187..1920"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgiteg srllqqkmsl
      181 dgnpkaihgp sersdglqws agqpcnpskp kaktspvksn apaahleikp delakkrgpn
      241 ieksvkdlqr ctvsltryrv mikeevdssv kkikaafael hnciidkevs lmaemdkvke
      301 eamdiltarq kkaeelkrlt dlasqmaemq laelraeikh fvserkydee lgkaarfscd
      361 ieqlkaqili cgeithpknn yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg
      421 kaanpkmvsg lpstadacqq tmptnkqngp snqrrrfnpq yhnrlngpak sqgsgneadp
      481 mvksnnrheh rrqphngfrp knkggaknqe aplgtkapea pphsekarrr qhaadnletr
      541 pfrgnvgrvs qcnlcptrie vsteatvlsv pavtlva
//
LOCUS       NP_001424606             578 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424606 XP_017451949
VERSION     NP_001424606.1
DBSOURCE    REFSEQ: accession NM_001437677.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_017451949.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1576754.1,
                                           SRR26643295.35384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..578
                     /product="SPATS2-like protein isoform 1"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=63767
     Region          79..388
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..578
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437677.1:185..1921"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgiteg srllqqkmsl
      181 dgnpkaihgp sersdglqws agqpcnpskp kaktspvksn apaahleikp delakkrgpn
      241 ieksvkdlqr ctvsltryrv mikeevdssv kkikaafael hnciidkevs lmaemdkvke
      301 eamdiltarq kkaeelkrlt dlasqmaemq laelraeikh fvserkydee lgkaarfscd
      361 ieqlkaqili cgeithpknn yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg
      421 kaanpkmvsg lpstadacqq tmptnkqqng psnqrrrfnp qyhnrlngpa ksqgsgnead
      481 pmvksnnrhe hrrqphngfr pknkggaknq eaplgtkape apphsekarr rqhaadnlet
      541 rpfrgnvgrv sqcnlcptri evsteatvls vpavtlva
//
LOCUS       NP_001014124             558 aa            linear   ROD 08-APR-2025
DEFINITION  SPATS2-like protein isoform 4 [Rattus norvegicus].
ACCESSION   NP_001014124 XP_237177
VERSION     NP_001014124.1
DBSOURCE    REFSEQ: accession NM_001014102.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 20, 2005 this sequence version replaced XP_237177.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085874.1, SRR26643291.25585.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16093049
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..558
                     /product="SPATS2-like protein isoform 4"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=61643
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUQ6; propagated from
                     UniProtKB/Swiss-Prot (Q5U2T3.1)"
     Region          59..368
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     Region          63..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T3.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUQ6; propagated from
                     UniProtKB/Swiss-Prot (Q5U2T3.1)"
     Region          161..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T3.1)"
     Region          383..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T3.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUQ6; propagated from
                     UniProtKB/Swiss-Prot (Q5U2T3.1)"
     CDS             1..558
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001014102.2:108..1784"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv dkavqafvdg saiqvlkews
       61 mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa plvqnghmng cekdssspds
      121 areklaltpr ekkisileep praqrgiteg srllqqkmsl dgnpkaihgp sersdglqws
      181 agqpcnpskp kaktspvksn apaahleikp delakkrgpn ieksvkdlqr ctvsltryrv
      241 mikeevdssv kkikaafael hnciidkevs lmaemdkvke eamdiltarq kkaeelkrlt
      301 dlasqmaemq laelraeikh fvserkydee lgkaarfscd ieqlkaqili cgeithpknn
      361 yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg kaanpkmvsg lpstadacqq
      421 tmptnkqqng psnqrrrfnp qyhnrlngpa ksqgsgnead pmvksnnrhe hrrqphngfr
      481 pknkggaknq eaplgtkape apphsekarr rqhaadnlet rpfrgnvgrv sqcnlcptri
      541 evsteatvls vpavtlva
//
LOCUS       NP_001178738            1021 aa            linear   ROD 08-APR-2025
DEFINITION  INO80 complex subunit D [Rattus norvegicus].
ACCESSION   NP_001178738 XP_006245093 XP_237220
VERSION     NP_001178738.1
DBSOURCE    REFSEQ: accession NM_001191809.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Apr 8, 2025 this sequence version replaced
            XP_006245093.1, XP_237220.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.757360.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..1021
                     /product="INO80 complex subunit D"
                     /calculated_mol_wt=112291
     Region          18..79
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     Region          <170..>285
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          442..506
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     CDS             1..1021
                     /gene="Ino80d"
                     /gene_synonym="RGD1304808"
                     /coded_by="NM_001191809.2:283..3348"
                     /db_xref="GeneID:316440"
                     /db_xref="RGD:1304808"
ORIGIN      
        1 myegkhihfs evdnkplcsy spklckqrrl ngyafcirhv ledktapfkq ceyvakynsq
       61 rctnpipkse drrycnshlq vlgfipkker kkkndpvdev kvrhqmdama fsltvptlal
      121 kmpngldsms lsppgarvpl hyleteledp fafneedddl kkgvtvrkkl qsklaqnrqr
      181 qreteilkvr qehfstpptp pqqhahlspl ptslkppapp qgsvckspqp qstslpmqgv
      241 aptthsiaqt rqashkrplp llpssrapvs dtprtdrilm katafsphfs cisrlqrlvk
      301 lctqkhqlda dlfphlgldw seesgeeled sdqaspyqva wsvretlrqe rhtsddddae
      361 srssrvtqlc tyfqqkykhl crleraesrq kkcrhtfrka llqaaskepe ctgqliqelr
      421 raacsrdsls qtklkevepa acsgtvkgeq ctnqalpftr hcfqhillnr sqqlfsscta
      481 kfadgqqcsv pvfdithqtp lceehakkmd nflrgdnsrk vqhqqqrkpr kktkppaltk
      541 khkkkrrrgp rrpqkpippa vpqgnlsmpt svslpvqasq irspstpels adelpddian
      601 eitdiphdle lnqedfadvl prlpddlqdf dffegkngdl lptteeaeel eralqavtsl
      661 eclstigvls qsdgvpvqgl sdrgmgvfst gtdasgiqsl srevntdlge llngrivhds
      721 fssleldenl lhsatlsnpp tplagqiqgq fsapasvglt satllsqsal gerafpgqfh
      781 glhdgshasq rphpaqllsk addlitsrqq yssdhshssp hgshydsehv pspysdhits
      841 phtsysgdnm aatfsaempi maqhllptql evplggvvnp rthwgnlpvn lgdpsafsnl
      901 lgadghllst slstppttsn settqpafat vtpssssvlp glpqtsfsgm gpsaelmast
      961 spkqqlpqfs aafghqlssh sgipkdlqps hssiapptgf tvtgatatst nnasppfptp
     1021 n
//
LOCUS       NP_001100385             587 aa            linear   ROD 08-APR-2025
DEFINITION  calcium-responsive transcription factor isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001100385 XP_001069949 XP_217411
VERSION     NP_001100385.1
DBSOURCE    REFSEQ: accession NM_001106915.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Zheng,F., Zhou,X., Luo,Y., Xiao,H., Wayman,G. and Wang,H.
  TITLE     Regulation of brain-derived neurotrophic factor exon IV
            transcription through calcium responsive elements in cortical
            neurons
  JOURNAL   PLoS One 6 (12), e28441 (2011)
   PUBMED   22174809
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Hasan,M.K., Yaguchi,T., Sugihara,T., Kumar,P.K., Taira,K.,
            Reddel,R.R., Kaul,S.C. and Wadhwa,R.
  TITLE     CARF is a novel protein that cooperates with mouse p19ARF (human
            p14ARF) in activating p53
  JOURNAL   J Biol Chem 277 (40), 37765-37770 (2002)
   PUBMED   12154087
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Tao,X., West,A.E., Chen,W.G., Corfas,G. and Greenberg,M.E.
  TITLE     A calcium-responsive transcription factor, CaRF, that regulates
            neuronal activity-dependent expression of BDNF
  JOURNAL   Neuron 33 (3), 383-395 (2002)
   PUBMED   11832226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217411.4, XP_001069949.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760389, SAMN16676789
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..587
                     /product="calcium-responsive transcription factor isoform
                     3"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 8; calcium-response factor;
                     amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8 protein"
                     /calculated_mol_wt=64536
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7U2.1)"
     Region          117..349
                     /region_name="ALS2CR8"
                     /note="Amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8; pfam15299"
                     /db_xref="CDD:464625"
     Region          437..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7U2.1)"
     Region          479..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7U2.1)"
     CDS             1..587
                     /gene="Carf"
                     /gene_synonym="Als2cr8"
                     /coded_by="NM_001106915.2:660..2423"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:301446"
                     /db_xref="RGD:1306822"
ORIGIN      
        1 mlassqmtsv seekpiggsl pavstdaled sassyslhsq aslvgprksg trtleeplla
       61 plqplscntp mwacrlrsce kigdsyrgyc vsetelesvl tfhkqqtqtv wgtrqspspa
      121 kpatrlmwks qyvpydgipf vnagsravvm ecqygprrkg fqlkkiseqe srschlykat
      181 cpariyikkv qkfpdyrvpt dpqidrktir meqekaftml kknlvdaggv lrwyvqlptq
      241 qahqyhepet pgvplspspf pmspleeeea iirdencvlp srlhpqvahk iqelvsqgvg
      301 qvyavrkqlr kfverelfkp devperhnls ffptvndikn hihevqkslq tgdvvynsei
      361 ipatlqwttd sgnilretvt vtfaegnllk epitskmgts qtqtslspep lpllsplssf
      421 qpkifthlqa lklqprlssp dgsqalvsvn shpsssppgl dtagnaeann hslllgqsqn
      481 lgtdtclpen sstaspmgsl pesvqnlvav dqlvggedae dagnlegnvk rtllgdahti
      541 pihildshpa lveedtlsmn qvkqepnept lsteaktlld cknvsat
//
LOCUS       NP_001424183             127 aa            linear   ROD 08-APR-2025
DEFINITION  small ribosomal subunit protein uS17m [Rattus norvegicus].
ACCESSION   NP_001424183 XP_006249326
VERSION     NP_001424183.1
DBSOURCE    REFSEQ: accession NM_001437254.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249326.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223326.1, FM103434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..127
                     /product="small ribosomal subunit protein uS17m"
                     /note="28S ribosomal protein S17, mitochondrial"
                     /calculated_mol_wt=13868
     Region          11..84
                     /region_name="Ribosomal_uS17"
                     /note="Ribosomal protein uS17; cd00364"
                     /db_xref="CDD:466775"
     CDS             1..127
                     /gene="Mrps17"
                     /coded_by="NM_001437254.1:68..451"
                     /db_xref="GeneID:288621"
                     /db_xref="RGD:1307650"
ORIGIN      
        1 msivrsavha kwvvgkvigt amvktakvra trlvldpyll kyfnkrktyf ahdalqqcsv
       61 gdivllralp vprakhvkhe laeiifkvgr vidpvtgkpc agtaylespl sseatppces
      121 reelkss
//
LOCUS       NP_001423909             335 aa            linear   ROD 08-APR-2025
DEFINITION  probable G-protein coupled receptor 174 [Rattus norvegicus].
ACCESSION   NP_001423909 XP_006257226
VERSION     NP_001423909.1
DBSOURCE    REFSEQ: accession NM_001436980.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Barnes,M.J., Li,C.M., Xu,Y., An,J., Huang,Y. and Cyster,J.G.
  TITLE     The lysophosphatidylserine receptor GPR174 constrains regulatory T
            cell development and function
  JOURNAL   J Exp Med 212 (7), 1011-1020 (2015)
   PUBMED   26077720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006257226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.21517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN06680427
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..335
                     /product="probable G-protein coupled receptor 174"
                     /calculated_mol_wt=38611
     Region          20..303
                     /region_name="7tmA_GPR174-like"
                     /note="putative purinergic receptor GPR174, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15152"
                     /db_xref="CDD:320280"
     Region          20..47
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320280"
     Region          54..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320280"
     Site            order(75,78..79,91..96,98..99,102,146,148..152,182,
                     185..187,189..191,193..194,243,246..247,249..250,253,
                     270..271,273..275,278,281..282)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320280"
     Region          91..121
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320280"
     Region          132..154
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320280"
     Region          182..211
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320280"
     Region          223..253
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320280"
     Region          271..296
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320280"
     CDS             1..335
                     /gene="Gpr174"
                     /gene_synonym="RGD1564689"
                     /coded_by="NM_001436980.1:853..1860"
                     /db_xref="GeneID:302373"
                     /db_xref="RGD:1564689"
ORIGIN      
        1 mtdnftcnkt dgdntdfryf iyavtytvil vpglignila lwvfygymke tkravvfmin
       61 laiadllqil slplrifyyl nhdwpfgpgl cmfcfylkyv nmyasiyflv cisvrrfwfl
      121 mypfrfndck qkydlyisiv gwliiclacl lfpllrtndd tpgnrtkcfv dlpirnvnla
      181 qsvamitige vvgfitplmi vlyctwktal slqnkypisq hlgekkkalr miltcaavfl
      241 icfapyhfsf pldflvksne iksclarrvi lifhsvalcl aslnscldpv iyyfttnefr
      301 rrlsrqelpd siqlqtksyk ivnnhgaspt aaelc
//
LOCUS       NP_001424149             798 aa            linear   ROD 08-APR-2025
DEFINITION  transferrin receptor protein 2 [Rattus norvegicus].
ACCESSION   NP_001424149 XP_008767347
VERSION     NP_001424149.1
DBSOURCE    REFSEQ: accession NM_001437220.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Guo,S., Yang,C., Jiang,S., Ni,Y., Zhao,R. and Ma,W.
  TITLE     Repeated Restraint Stress Enhances Hepatic TFR2 Expression and
            Induces Hepatic Iron Accumulation in Rats
  JOURNAL   Biol Trace Elem Res 196 (2), 590-596 (2020)
   PUBMED   31707638
  REMARK    GeneRIF: Repeated Restraint Stress Enhances Hepatic TFR2 Expression
            and Induces Hepatic Iron Accumulation in Rats.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Chen,J. and Enns,C.A.
  TITLE     CD81 promotes both the degradation of transferrin receptor 2 (TfR2)
            and the Tfr2-mediated maintenance of hepcidin expression
  JOURNAL   J Biol Chem 290 (12), 7841-7850 (2015)
   PUBMED   25635054
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Bartnikas,T.B., Wildt,S.J., Wineinger,A.E., Schmitz-Abe,K.,
            Markianos,K., Cooper,D.M. and Fleming,M.D.
  TITLE     A novel rat model of hereditary hemochromatosis due to a mutation
            in transferrin receptor 2
  JOURNAL   Comp Med 63 (2), 143-155 (2013)
   PUBMED   23582421
  REMARK    GeneRIF: A mutation with the Tfr2 gene causes hemochromatosis in
            the rat.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Vujic Spasic,M., Sparla,R., Mleczko-Sanecka,K., Migas,M.C.,
            Breitkopf-Heinlein,K., Dooley,S., Vaulont,S., Fleming,R.E. and
            Muckenthaler,M.U.
  TITLE     Smad6 and Smad7 are co-regulated with hepcidin in mouse models of
            iron overload
  JOURNAL   Biochim Biophys Acta 1832 (1), 76-84 (2013)
   PUBMED   22960056
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Goswami,T. and Andrews,N.C.
  TITLE     Hereditary hemochromatosis protein, HFE, interaction with
            transferrin receptor 2 suggests a molecular mechanism for mammalian
            iron sensing
  JOURNAL   J Biol Chem 281 (39), 28494-28498 (2006)
   PUBMED   16893896
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Weizer-Stern,O., Adamsky,K., Amariglio,N., Rachmilewitz,E.,
            Breda,L., Rivella,S. and Rechavi,G.
  TITLE     mRNA expression of iron regulatory genes in beta-thalassemia
            intermedia and beta-thalassemia major mouse models
  JOURNAL   Am J Hematol 81 (7), 479-483 (2006)
   PUBMED   16755567
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Nakamaki,T., Kawabata,H., Saito,B., Matsunawa,M., Suzuki,J.,
            Adachi,D., Tomoyasu,S. and Phillip Koeffler,H.
  TITLE     Elevated levels of transferrin receptor 2 mRNA, not transferrin
            receptor 1 mRNA, are associated with increased survival in acute
            myeloid leukaemia
  JOURNAL   Br J Haematol 125 (1), 42-49 (2004)
   PUBMED   15015967
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Griffiths,W.J. and Cox,T.M.
  TITLE     Co-localization of the mammalian hemochromatosis gene product (HFE)
            and a newly identified transferrin receptor (TfR2) in intestinal
            tissue and cells
  JOURNAL   J Histochem Cytochem 51 (5), 613-624 (2003)
   PUBMED   12704209
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Camaschella,C., Roetto,A., Cali,A., De Gobbi,M., Garozzo,G.,
            Carella,M., Majorano,N., Totaro,A. and Gasparini,P.
  TITLE     The gene TFR2 is mutated in a new type of haemochromatosis mapping
            to 7q22
  JOURNAL   Nat Genet 25 (1), 14-15 (2000)
   PUBMED   10802645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_008767347.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166451.1, SRR26643286.34952.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..798
                     /product="transferrin receptor protein 2"
                     /calculated_mol_wt=88197
     Region          23..26
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          25..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          139..>192
                     /region_name="Zinc_peptidase_like"
                     /note="Zinc peptidases M18, M20, M28, and M42; cl14876"
                     /db_xref="CDD:472712"
     Region          206..396
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Site            order(298,312..315,317,321..324,327,329..331)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(322,328)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(327,330)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(331,333,337..338)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          404..637
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(411,413,416,418..419,421,465,467,484,487..495)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Site            535
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B2GUY2.1)"
     Region          664..788
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     CDS             1..798
                     /gene="Tfr2"
                     /gene_synonym="Trfr2"
                     /coded_by="NM_001437220.1:264..2660"
                     /db_xref="GeneID:288562"
                     /db_xref="RGD:1310152"
ORIGIN      
        1 meqrwgllrk vqqwsprpsq tiyrrvegpq lenleeedre egeelpaqfc pmelkgperl
       61 gscpgrsipi pwaaagrkaa pylvlttlli ftgafllgyv afrgscqacg dsvlvvgedv
      121 nsedssrgtl ywsdlqdmfl rflgegrmed tirltslrer vagsarmatl vqdildklsr
      181 qkldhvwtdt hyvglqfpdp ahpntlhwvg adgsvqeqlp ledpevycpy satgnatgkl
      241 vyahygrred lqdlkakdve lagslllvra gitsfaqkva iaqdfgahgv liypdpadfs
      301 qdphkpglss dravyghvhl gtgdpytpgf psfnqtqfpp vessglpnip aqpisadvad
      361 rllrkltgpv apqewkgrls dspyrlgpgp glrlvvnnhr tstpisnifa ciegfaepdh
      421 yvvigaqrda wgpgaaksav gtaillelvr tfssmvssgf rprrsllfis wdggdfgsvg
      481 atewlegyls vlhlkavvyv sldnsvlgdg kfhaktspll vslienilkq vdspnhsgqt
      541 lydqvafthp swdaeviqpl pmdssaysft afagvpavef sfmeddrvyp flhtkedtye
      601 nlhkmlrgrl pavvlavaql agqllirlsh dhllpldfgr ygdvvlrhig nlnefsgdlk
      661 argltlqwvy sargdyiraa eklrkeiyss eqsderlmrm ynvrimrvef yflsqyvspa
      721 dspfrhiflg qgdhtlgalv ehlrmlrsdg sgaassglsp glgfqesrfr rqlalltwtl
      781 qgaanalsgd vwnidnnf
//
LOCUS       NP_001100408             335 aa            linear   ROD 08-APR-2025
DEFINITION  probable G-protein coupled receptor 174 [Rattus norvegicus].
ACCESSION   NP_001100408 XP_001059397 XP_006257225 XP_228495
VERSION     NP_001100408.1
DBSOURCE    REFSEQ: accession NM_001106938.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Barnes,M.J., Li,C.M., Xu,Y., An,J., Huang,Y. and Cyster,J.G.
  TITLE     The lysophosphatidylserine receptor GPR174 constrains regulatory T
            cell development and function
  JOURNAL   J Exp Med 212 (7), 1011-1020 (2015)
   PUBMED   26077720
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Mar 25, 2025 this sequence version replaced
            XP_006257225.1, XP_228495.3, XP_001059397.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.65766.1,
                                           SRR26643284.21515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680445, SAMN06680453
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..335
                     /product="probable G-protein coupled receptor 174"
                     /calculated_mol_wt=38611
     Region          20..303
                     /region_name="7tmA_GPR174-like"
                     /note="putative purinergic receptor GPR174, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15152"
                     /db_xref="CDD:320280"
     Region          20..47
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320280"
     Region          54..79
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320280"
     Site            order(75,78..79,91..96,98..99,102,146,148..152,182,
                     185..187,189..191,193..194,243,246..247,249..250,253,
                     270..271,273..275,278,281..282)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320280"
     Region          91..121
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320280"
     Region          132..154
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320280"
     Region          182..211
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320280"
     Region          223..253
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320280"
     Region          271..296
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320280"
     CDS             1..335
                     /gene="Gpr174"
                     /gene_synonym="RGD1564689"
                     /coded_by="NM_001106938.2:857..1864"
                     /db_xref="GeneID:302373"
                     /db_xref="RGD:1564689"
ORIGIN      
        1 mtdnftcnkt dgdntdfryf iyavtytvil vpglignila lwvfygymke tkravvfmin
       61 laiadllqil slplrifyyl nhdwpfgpgl cmfcfylkyv nmyasiyflv cisvrrfwfl
      121 mypfrfndck qkydlyisiv gwliiclacl lfpllrtndd tpgnrtkcfv dlpirnvnla
      181 qsvamitige vvgfitplmi vlyctwktal slqnkypisq hlgekkkalr miltcaavfl
      241 icfapyhfsf pldflvksne iksclarrvi lifhsvalcl aslnscldpv iyyfttnefr
      301 rrlsrqelpd siqlqtksyk ivnnhgaspt aaelc
//
LOCUS       NP_001424325             333 aa            linear   ROD 08-APR-2025
DEFINITION  coiled-coil domain-containing protein 68 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424325 XP_038952587
VERSION     NP_001424325.1
DBSOURCE    REFSEQ: accession NM_001437396.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952587.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1973836.1,
                                           SRR26643291.40897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..333
                     /product="coiled-coil domain-containing protein 68 isoform
                     3"
                     /note="CTCL tumor antigen se57-1; coiled-coil
                     domain-containing protein 68"
                     /calculated_mol_wt=38099
     Region          <85..>297
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..333
                     /gene="Ccdc68"
                     /gene_synonym="RGD1561424"
                     /coded_by="NM_001437396.1:148..1149"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:291530"
                     /db_xref="RGD:1561424"
ORIGIN      
        1 mttvtvtmev psggktedrs ifsgpssaqi ieeteyvrki rttlekirnr mfkeedgrgn
       61 arhkvdaeqs gnvqngldst tdptrldlll esmrrkdqql lemnkenevl qikleasrea
      121 gaaalrnaaq rlfdnyqtqs edlekkhkds khvlqvnkle keqtlkqrak nlsqlseklg
      181 ekheqivgle nrvqrmenek kallerklcl eskllqlksn aanskscqhl qteisilqeq
      241 ichlqfvihs qhqnlrniiq emeglkntlk eqdkkienlk ekvtvleaqn eelktkvahw
      301 tesprtsvsk avstselkte gaspylmlir lrk
//
LOCUS       NP_001424367             569 aa            linear   ROD 08-APR-2025
DEFINITION  sialic acid-binding Ig-like lectin 5 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424367 XP_006229008
VERSION     NP_001424367.1
DBSOURCE    REFSEQ: accession NM_001437438.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Tateno,H., Li,H., Schur,M.J., Bovin,N., Crocker,P.R.,
            Wakarchuk,W.W. and Paulson,J.C.
  TITLE     Distinct endocytic mechanisms of CD22 (Siglec-2) and Siglec-F
            reflect roles in cell signaling and innate immunity
  JOURNAL   Mol Cell Biol 27 (16), 5699-5710 (2007)
   PUBMED   17562860
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Zhang,J.Q., Biedermann,B., Nitschke,L. and Crocker,P.R.
  TITLE     The murine inhibitory receptor mSiglec-E is expressed broadly on
            cells of the innate immune system whereas mSiglec-F is restricted
            to eosinophils
  JOURNAL   Eur J Immunol 34 (4), 1175-1184 (2004)
   PUBMED   15048729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.2151.1,
                                           SRR26643290.1840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..569
                     /product="sialic acid-binding Ig-like lectin 5 isoform 2
                     precursor"
                     /calculated_mol_wt=60346
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1783
     Region          20..133
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          122..128
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          139..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          153..157
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409579"
     Region          170..174
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409579"
     Region          189..193
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409579"
     Region          203..208
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409579"
     Region          218..221
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409579"
     Region          252..325
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          261..265
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          274..281
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          305..310
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..323
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          <347..419
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          356..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          388..392
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          401..406
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          414..417
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..569
                     /gene="Siglec5"
                     /coded_by="NM_001437438.1:292..2001"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:292843"
                     /db_xref="RGD:1305432"
ORIGIN      
        1 mlwaqllpll wagslaveny elsltesvtv qeglcvfvpc qvkypasggs vfgywfqdga
       61 ntnlnspvat ndphrpvqqe tqgrfylvgg idtkncsldi rdarksdtgk yffrldgsvk
      121 ysfrnrmlsv hvtaltktpn lqvtstlvsg tstrvicsvl waceqgtppi fswmssalts
      181 lgrrtilsse lnltprpqdn gtnlicqvtf pgagvtvert qqlsvtyapq kltirvswgd
      241 gtetkvlqsg aslqiqeges lrlvcvadsn psamlswkrq tqknfrlskg delqlprvel
      301 edqgkyicqa knslgtqtas vslsirsllq llapscswds eglhcscssr awpapslgwr
      361 lgegllegns snasftvmss sagpwvnssl slsvefstdh rlsceawndy gvqrativlv
      421 pgqgvsqadk setsggavqg aiwgaglmal lavsfcliff ivkflrkksa levaamegnh
      481 laknlvstin sasmissnip lrypiqdhln esesqtqkee pplatapdip kdepelhyas
      541 lsfqgprpqq pkntetiksv yteikihkr
//
LOCUS       NP_001424388             301 aa            linear   ROD 08-APR-2025
DEFINITION  nitric oxide synthase-interacting protein [Rattus norvegicus].
ACCESSION   NP_001424388 XP_006229087
VERSION     NP_001424388.1
DBSOURCE    REFSEQ: accession NM_001437459.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Yu,X., Zhong,Y., Zhu,Z., Wu,T., Shen,A. and Huang,Y.
  TITLE     Increased expression of nitric oxide synthase interacting protein
            (NOSIP) following traumatic spinal cord injury in rats
  JOURNAL   J Mol Histol 43 (6), 661-668 (2012)
   PUBMED   23135205
  REMARK    GeneRIF: Data suggested that NOSIP may play an important roles in
            astrogliogenesis after a spinal cord injury.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dreyer,J., Schleicher,M., Tappe,A., Schilling,K., Kuner,T.,
            Kusumawidijaja,G., Muller-Esterl,W., Oess,S. and Kuner,R.
  TITLE     Nitric oxide synthase (NOS)-interacting protein interacts with
            neuronal NOS and regulates its distribution and activity
  JOURNAL   J Neurosci 24 (46), 10454-10465 (2004)
   PUBMED   15548660
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Dedio,J., Konig,P., Wohlfart,P., Schroeder,C., Kummer,W. and
            Muller-Esterl,W.
  TITLE     NOSIP, a novel modulator of endothelial nitric oxide synthase
            activity
  JOURNAL   FASEB J 15 (1), 79-89 (2001)
   PUBMED   11149895
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229087.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216351.1, SRR26643299.2383.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..301
                     /product="nitric oxide synthase-interacting protein"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=33126
     Region          4..78
                     /region_name="zf-NOSIP"
                     /note="Zinc-finger of nitric oxide synthase-interacting
                     protein; pfam15906"
                     /db_xref="CDD:318178"
     Region          220..287
                     /region_name="RING-Ubox2_NOSIP"
                     /note="U-box domain 2, a modified RING finger, found in
                     nitric oxide synthase-interacting protein (NOSIP) and
                     similar proteins; cd16662"
                     /db_xref="CDD:438324"
     CDS             1..301
                     /gene="Nosip"
                     /coded_by="NM_001437459.1:144..1049"
                     /db_xref="GeneID:292894"
                     /db_xref="RGD:1309992"
ORIGIN      
        1 mtrhgkncta gavytyhekk kdtaasgygt qnirlsrdav kdfdccclsl qpchdpvvtp
       61 dgylyereai leyilhqkre iarqmkayek qrgarreeqk elqraaaqdq vrgflekesa
      121 ivsrplnpfm pkaatlpntd geqpgpsvgp lgkdkdkalp sfwipsltpe akatklekps
      181 rtvtcpmsgk plrmsdltsv rftqlddsvd rvglitrser yvcavtrdsl snatpcavlr
      241 psgavvtlec veklirkdmv dpvngdtlte rdiivlqrgg tgfagsgvkl qaemsrpvmq
      301 a
//
LOCUS       NP_001424163             314 aa            linear   ROD 08-APR-2025
DEFINITION  transmembrane protein 248 [Rattus norvegicus].
ACCESSION   NP_001424163 XP_006249292
VERSION     NP_001424163.1
DBSOURCE    REFSEQ: accession NM_001437234.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249292.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2197056.1, BC079161.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..314
                     /product="transmembrane protein 248"
                     /note="UPF0458 protein C7orf42 homolog"
                     /calculated_mol_wt=34982
     Region          10..257
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Region          78..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY76.1)"
     CDS             1..314
                     /gene="Tmem248"
                     /coded_by="NM_001437234.1:251..1195"
                     /db_xref="GeneID:288616"
                     /db_xref="RGD:1303319"
ORIGIN      
        1 mfsinplenl klyissrppl vvfmisvsam aiafltlgyf fkikeikspe maedwntfll
       61 rfndldlcvs enetlkhlsn dtttpestmt igqtrsstqp pqsleesgpi nisvaitltl
      121 dplkpfggys rnvthlysti lghqiglsgr eaheeinitf tlpaawnadd calhghceqv
      181 vftacmtlta apgvfpvtvq pphcvpdtys natlwykift tardantkya qdynpfwcyk
      241 gaigkvyhal npkltvivpd ddrslinlhl mhtsyflfvm vitmfcyavi kgrpsklrqs
      301 npefcpekva lada
//
LOCUS       NP_001424365             503 aa            linear   ROD 08-APR-2025
DEFINITION  2'-5'-oligoadenylate synthase-like protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424365 XP_008767549
VERSION     NP_001424365.1
DBSOURCE    REFSEQ: accession NM_001437436.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Perelygin,A.A., Zharkikh,A.A., Scherbik,S.V. and Brinton,M.A.
  TITLE     The mammalian 2'-5' oligoadenylate synthetase gene family: evidence
            for concerted evolution of paralogous Oas1 genes in Rodentia and
            Artiodactyla
  JOURNAL   J Mol Evol 63 (4), 562-576 (2006)
   PUBMED   17024523
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_008767549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.15980.1,
                                           SRR26643298.81249.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840112 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..503
                     /product="2'-5'-oligoadenylate synthase-like protein 2
                     isoform 2"
                     /EC_number="2.7.7.84"
                     /note="54 kDa 2'-5'-oligoadenylate synthase-like protein
                     2"
                     /calculated_mol_wt=58335
     Region          29..214
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(67..69,72,74..76,81,83,126..127,137,154,200,204,207)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(68..69,81,83,127,200,204,207)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(81,83,154)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          170..348
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     Region          351..424
                     /region_name="Ubl1_OASL"
                     /note="ubiquitin-like (Ubl) domain 1 found in
                     2'-5'-oligoadenylate synthase-like protein (OASL) and
                     similar proteins; cd01811"
                     /db_xref="CDD:340509"
     Region          430..501
                     /region_name="Ubl2_OASL"
                     /note="ubiquitin-like (Ubl) domain 2 found in
                     2'-5'-oligoadenylate synthase-like protein (OASL) and
                     similar proteins; cd16103"
                     /db_xref="CDD:340520"
     CDS             1..503
                     /gene="Oasl2"
                     /coded_by="NM_001437436.1:101..1612"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304549"
                     /db_xref="RGD:1307351"
ORIGIN      
        1 mdtlpdlygt vgdsldyfle hslqpqrdwk eegkdaweri erffrekcfc dellldqevr
       61 vlkvvkggss gkgtalnhrs dqdmilflsc fssfkqqard rkavidfiks klihcrksla
      121 ynitvrqhke gkrtprsltl eiqsrksndi icmdilpayn algsfsrdck pepeiyenli
      181 rckgypgdfs psfaelqrhf vksrpvklkn llrlvkfwhl kylrhkyrra vlpskyalel
      241 ltiyawemgt dssdnfnlde gfvavmellr dyqdiciywt kyydfqnevv rnflkeqlkg
      301 drpiildpad ptnnlgrrgk welvakeaty cllqlccvta drwnvqgard vqvtvkqtgr
      361 eewilltnph spirklkaki kkrmnlcgel risfqepgge rqplsgrktl sdygifskvn
      421 irvmetfppe iqvfvrypgg qnkpfaidpd atilslweki eedggpcted wvllfegeel
      481 ddddnlaelq ikdcdtiqls rvs
//
LOCUS       NP_001005882             590 aa            linear   ROD 08-APR-2025
DEFINITION  RNA-binding protein 47 [Rattus norvegicus].
ACCESSION   NP_001005882 XP_006251013 XP_223403
VERSION     NP_001005882.1
DBSOURCE    REFSEQ: accession NM_001005882.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Fossat,N., Tourle,K., Radziewic,T., Barratt,K., Liebhold,D.,
            Studdert,J.B., Power,M., Jones,V., Loebel,D.A. and Tam,P.P.
  TITLE     C to U RNA editing mediated by APOBEC1 requires RNA-binding protein
            RBM47
  JOURNAL   EMBO Rep 15 (8), 903-910 (2014)
   PUBMED   24916387
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Mar 26, 2025 this sequence version replaced
            XP_006251013.1, XP_223403.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.952959.1,
                                           SRR26360176.619287.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..590
                     /product="RNA-binding protein 47"
                     /note="hypothetical RNA binding protein RGD1359713"
                     /calculated_mol_wt=63963
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H68.1)"
     Region          11..590
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            396
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96; propagated from
                     UniProtKB/Swiss-Prot (Q66H68.1)"
     Site            407
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A0AV96; propagated from
                     UniProtKB/Swiss-Prot (Q66H68.1)"
     CDS             1..590
                     /gene="Rbm47"
                     /gene_synonym="RGD1359713"
                     /coded_by="NM_001005882.2:492..2264"
                     /db_xref="GeneID:305340"
                     /db_xref="RGD:1359713"
ORIGIN      
        1 mtaedsttam nsdptvgsst kvpegvagap neaallalme rtgynmvqen gqrkyggppp
       61 gwegphpqrg cevfvgkipr dvyedelvpv fetvgriyel rlmmdfdgkn rgyafvmych
      121 kheakravre lnnyeirpgr llgvccsvdn crlfiggipk mkkrgeilee iakvtegvln
      181 vivyasaadk mknrgfafve yeshraaama rrklmpgriq lwghqiavdw aepeidvded
      241 vmqtvkilyv rnlmiettee tikrsfgqfn pgcvervkki rdyafvhfts redavhamnn
      301 lngtelegsc levtlakpvd keqysryqka akggggsaea vaqqpsyvys cdpytlayyg
      361 ypynaligpn rdyfvktgsi rgrgrgaagn rtpgprgsyl ggysagrgiy sryhegkgkq
      421 qekgyelvpn leisavnpva ikpgtvaipa igaqysmfqa apapkiiedg kihtmehmis
      481 piavqpdpat aaaaaaaaaa aavipavstp ppfqgrpitp vytvapnvpr iptagiygas
      541 yvpfaapata tiatlqknaa aavyggyagy ipqafpaalq vpihdvyqty
//
LOCUS       NP_001009491             362 aa            linear   ROD 08-APR-2025
DEFINITION  2 ' -5 ' oligoadenylate synthetase 1H [Rattus norvegicus].
ACCESSION   NP_001009491 XP_579292
VERSION     NP_001009491.1
DBSOURCE    REFSEQ: accession NM_001009491.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579292.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY196701.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840112,
                                           SAMN16418971 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..362
                     /product="2 ' -5 ' oligoadenylate synthetase 1H"
                     /note="2'-5' oligoadenylate synthetase 1H"
                     /calculated_mol_wt=42697
     Region          29..>157
                     /region_name="NT_Pol-beta-like"
                     /note="Nucleotidyltransferase (NT) domain of DNA
                     polymerase beta and similar proteins; cl11966"
                     /db_xref="CDD:472251"
     Site            order(76,78,149)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143387"
     Region          173..355
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     CDS             1..362
                     /gene="Oas1h"
                     /coded_by="NM_001009491.2:29..1117"
                     /db_xref="GeneID:494200"
                     /db_xref="RGD:1359732"
ORIGIN      
        1 mekdlkstpa wkldkfiqnh lladttfvte akadieflcd fltercfqda shpvrvsriv
       61 mggcydeysm lkgrseatlv vffnnltrfe dqlkrreeli eeiwkhlcql qhekqfklkf
      121 evqsseqdny sslsiklssp qlqqevefdv qpaydvlyel kekleldcef ynkiyarlir
      181 ecitlrkege fsvcfmelqq kflwnrpedl rnllvlvkhw yqlckeklgd slppqyalel
      241 ltvhawenei pakygaqtar gfqsvlelii kytclrvywt fyydilhqdv ssylhkqlrk
      301 erpvildpad ptrnvaglni dgwcelakea eawlkypcfr hidetfvgsw evppekqggv
      361 fl
//
LOCUS       NP_001424223             125 aa            linear   ROD 08-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424223
VERSION     NP_001424223.1
DBSOURCE    REFSEQ: accession NM_001437294.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.1560042.1,
                                           SRR26360190.1613304.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..125
                     /product="mitochondrial ribosomal protein S6 isoform 1"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=14210
     Region          3..96
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(4,49,53,72,75..76,83,90,93..95)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     Site            order(5,7,45,47..49,63,65,90,94)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     CDS             1..125
                     /gene="Mrps6"
                     /coded_by="NM_001437294.1:172..549"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mpryelalil kamrrpetaa alkrtieslm drgaivrnle nlgeralpyr isshsqqhsr
       61 ggyflvdfya ptnavesmle hlardtdvvr pnivkhpltq evkecdgivp vpleeklyst
      121 krrkk
//
LOCUS       NP_001099654             870 aa            linear   ROD 08-APR-2025
DEFINITION  NEDD4-like E3 ubiquitin-protein ligase WWP2 [Rattus norvegicus].
ACCESSION   NP_001099654 XP_001076615 XP_214669
VERSION     NP_001099654.1
DBSOURCE    REFSEQ: accession NM_001106184.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Yang,C., Pan,J., Luo,X., Li,J. and Jiang,Z.
  TITLE     Hypoxia-induced mesenchymal stem cells inhibit corneal fibroblast
            proliferation by regulating the WWP2/Notch1 axis
  JOURNAL   Regen Med 17 (6), 375-388 (2022)
   PUBMED   35545948
  REMARK    GeneRIF: Hypoxia-induced mesenchymal stem cells inhibit corneal
            fibroblast proliferation by regulating the WWP2/Notch1 axis.
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Yuan,L., Lv,Y., Li,H., Gao,H., Song,S., Zhang,Y., Xing,G., Kong,X.,
            Wang,L., Li,Y., Zhou,T., Gao,D., Xiao,Z.X., Yin,Y., Wei,W., He,F.
            and Zhang,L.
  TITLE     Deubiquitylase OTUD3 regulates PTEN stability and suppresses
            tumorigenesis
  JOURNAL   Nat Cell Biol 17 (9), 1169-1181 (2015)
   PUBMED   26280536
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Lee,Y.I., Giovinazzo,D., Kang,H.C., Lee,Y., Jeong,J.S.,
            Doulias,P.T., Xie,Z., Hu,J., Ghasemi,M., Ischiropoulos,H., Qian,J.,
            Zhu,H., Blackshaw,S., Dawson,V.L. and Dawson,T.M.
  TITLE     Protein microarray characterization of the S-nitrosoproteome
  JOURNAL   Mol Cell Proteomics 13 (1), 63-72 (2014)
   PUBMED   24105792
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Nabhan,J.F., Hu,R., Oh,R.S., Cohen,S.N. and Lu,Q.
  TITLE     Formation and release of arrestin domain-containing protein
            1-mediated microvesicles (ARMMs) at plasma membrane by recruitment
            of TSG101 protein
  JOURNAL   Proc Natl Acad Sci U S A 109 (11), 4146-4151 (2012)
   PUBMED   22315426
REFERENCE   5  (residues 1 to 870)
  AUTHORS   Nakamura,Y., Yamamoto,K., He,X., Otsuki,B., Kim,Y., Murao,H.,
            Soeda,T., Tsumaki,N., Deng,J.M., Zhang,Z., Behringer,R.R.,
            Crombrugghe,Bd., Postlethwait,J.H., Warman,M.L., Nakamura,T. and
            Akiyama,H.
  TITLE     Wwp2 is essential for palatogenesis mediated by the interaction
            between Sox9 and mediator subunit 25
  JOURNAL   Nat Commun 2, 251 (2011)
   PUBMED   21427722
REFERENCE   6  (residues 1 to 870)
  AUTHORS   Chen,A., Gao,B., Zhang,J., McEwen,T., Ye,S.Q., Zhang,D. and Fang,D.
  TITLE     The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced
            T-cell death by catalyzing EGR2 ubiquitination
  JOURNAL   Mol Cell Biol 29 (19), 5348-5356 (2009)
   PUBMED   19651900
REFERENCE   7  (residues 1 to 870)
  AUTHORS   Xu,H., Wang,W., Li,C., Yu,H., Yang,A., Wang,B. and Jin,Y.
  TITLE     WWP2 promotes degradation of transcription factor OCT4 in human
            embryonic stem cells
  JOURNAL   Cell Res 19 (5), 561-573 (2009)
   PUBMED   19274063
  REMARK    Erratum:[Cell Res. 2009 Jun;19(6):796]
REFERENCE   8  (residues 1 to 870)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
REFERENCE   9  (residues 1 to 870)
  AUTHORS   Jespersen,T., Membrez,M., Nicolas,C.S., Pitard,B., Staub,O.,
            Olesen,S.P., Baro,I. and Abriel,H.
  TITLE     The KCNQ1 potassium channel is down-regulated by ubiquitylating
            enzymes of the Nedd4/Nedd4-like family
  JOURNAL   Cardiovasc Res 74 (1), 64-74 (2007)
   PUBMED   17289006
REFERENCE   10 (residues 1 to 870)
  AUTHORS   Xu,H.M., Liao,B., Zhang,Q.J., Wang,B.B., Li,H., Zhong,X.M.,
            Sheng,H.Z., Zhao,Y.X., Zhao,Y.M. and Jin,Y.
  TITLE     Wwp2, an E3 ubiquitin ligase that targets transcription factor
            Oct-4 for ubiquitination
  JOURNAL   J Biol Chem 279 (22), 23495-23503 (2004)
   PUBMED   15047715
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001076615.1, XP_214669.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132264 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..870
                     /product="NEDD4-like E3 ubiquitin-protein ligase WWP2"
                     /EC_number="2.3.2.26"
                     /calculated_mol_wt=98647
     Region          17..142
                     /region_name="C2_E3_ubiquitin_ligase"
                     /note="C2 domain present in E3 ubiquitin ligase; cd04021"
                     /db_xref="CDD:175988"
     Region          <163..312
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          302..331
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          332..361
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          407..435
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          447..477
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(461,472)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          516..868
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(521,551,562,623,797,832..833,836..840,860,867)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(651,654..655,657..658,661,668,670,673..674,676,682,
                     687,704,708)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..870
                     /gene="Wwp2"
                     /coded_by="NM_001106184.1:81..2693"
                     /db_xref="GeneID:291999"
                     /db_xref="RGD:1310091"
ORIGIN      
        1 masasssrag valpfeksql tlrvvsakpk vhnrqprins yvevavdglp setkktgkri
       61 gssellwnev ivlnvtaqsh ldlkvwscht lrnellgtas vnlsnvlknn ggkmentqlt
      121 lnlqtenkgs vvsggeltif ldgptvdlgs vpngsavtdg sqppsressg talapetrhq
      181 ppstncfggr srthrhsggs artatatgeq spgarnrhrq pvknpsssgl angtvseept
      241 tasdpeelsv vgvtsppaaa ssvspnpntt slpapstpae geepstsgtq qlpaaaqapd
      301 alpagweqrq lpngrvyyvd hntktttwer plppgwekrt dprgrfyyvd hntrtttwqr
      361 ptaeyvrnye qwqsqrnqlq gamqhfsqrf lyqsssastd hdplgplppg wekrqdngrv
      421 yyvnhntrtt qwedprtqgm iqepalppgw emkytsegvr yfvdhntrtt tfkdprpgfe
      481 sgtkqgspga yersfrwkyh qfrflchsna lpshvkisvs rqtlfedsfq qimnmkpydl
      541 rrrlyiimrg eegldyggia rewffllshe vlnpmyclfe yagknnyclq inpassinpd
      601 hltyfrfigr fiamalyhgk fidtgftlpf ykrmlnkrpt lrdlesidpe fynsiiwike
      661 nnldecglel ffiqdmeilg kvtthelkeg genirvteen keeyimlltd wrftrgveeq
      721 tkafldgfne vaplewlryf dekelelmlc gmqeidmsdw qknaiyrhyt ksskqiqwfw
      781 qvvkemdnek rirllqfvtg tcrlpvggfa eligsngpqk fcidrvgket wlprshtcfn
      841 rldlppyksy eqlkekllya ieetegfgqe
//
LOCUS       NP_001099626             621 aa            linear   ROD 08-APR-2025
DEFINITION  polycystin-2-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001099626 XP_001061050 XP_226056
VERSION     NP_001099626.1
DBSOURCE    REFSEQ: accession NM_001106156.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473974.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_226056.4, XP_001061050.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..621
                     /product="polycystin-2-like protein 2"
                     /note="polycystic kidney disease 2-like 2 protein"
                     /calculated_mol_wt=73170
     Region          77..272
                     /region_name="Polycystin_dom"
                     /note="Polycystin domain; pfam20519"
                     /db_xref="CDD:466668"
     Region          273..497
                     /region_name="PKD_channel"
                     /note="Polycystin cation channel; pfam08016"
                     /db_xref="CDD:462341"
     CDS             1..621
                     /gene="Pkd2l2"
                     /coded_by="NM_001106156.1:45..1910"
                     /db_xref="GeneID:291683"
                     /db_xref="RGD:1310272"
ORIGIN      
        1 mseatwwhrg gtskhdlhyr reaevnttle elllyfifli nlciltfgtv nphmyylnkv
       61 msslfvdtsl pdderssfrs irsitefwkf megplvegly wdswygntql dsvknssliy
      121 yenillgvpr vrqlrvrnst cqvypafqsl asdcynkyta enedfsdfgl khdpewrhsa
      181 psstapwhwg fvgvyrdggy mvtlskskse tkakladlrq nnwigrgtra vfidfslyna
      241 nvnlfciirl laefpatggi ltswqfysvk liryvsyydh fiasceiifc ifllvfitqe
      301 lrklnefksa yfrsvwnwie llllvlcfla vsfyaycnvq cflllgqllr stesypdfyf
      361 laywhiyynn iiaitiffaw ikifkfisfn etmsqlsstl srcmkdivgf aimffiiffa
      421 yaqlaflvfg sqvddfstfq nsifaqfriv lgdfnfagiq qanwilgpiy fitfiffvff
      481 vllnmflaii ndtysevkad ysigrrpdfe lgsiikkscf nileklrlrk aqnnedkkmk
      541 tsvdlaqark egfdeseiqe arqmkrwker lekkyystei qddyqpvtqq efrelflyav
      601 elekelhyls lklnqvmrkl h
//
LOCUS       NP_001099394             757 aa            linear   ROD 08-APR-2025
DEFINITION  coiled-coil-helix-coiled-coil-helix domain-containing protein 2
            [Rattus norvegicus].
ACCESSION   NP_001099394 XP_001078332 XP_222107
VERSION     NP_001099394.1
DBSOURCE    REFSEQ: accession NM_001105924.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_222107.4, XP_001078332.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.84583.1,
                                           SRR26360172.1181469.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..757
                     /product="coiled-coil-helix-coiled-coil-helix
                     domain-containing protein 2"
                     /EC_number="2.3.1.15"
                     /note="zinc finger BED domain-containing protein 5; SCAN
                     domain containing 3; coiled-coil-helix-coiled-coil-helix
                     domain containing protein 2-like 2"
                     /calculated_mol_wt=83904
     Region          <45..110
                     /region_name="COG3416"
                     /note="Uncharacterized conserved protein, DUF2076 domain
                     [Function unknown]"
                     /db_xref="CDD:442642"
     Region          <303..417
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     Region          673..737
                     /region_name="Dimer_Tnp_hAT"
                     /note="hAT family C-terminal dimerization region;
                     pfam05699"
                     /db_xref="CDD:399013"
     CDS             1..757
                     /gene="Zbed5"
                     /gene_synonym="Chchd2l2; Scand3"
                     /coded_by="NM_001105924.2:42..2315"
                     /db_xref="GeneID:288622"
                     /db_xref="RGD:1559988"
ORIGIN      
        1 mprgsrirts rvtplagrap qmraaprrap aaqppataaa psavgspaaa prqpglmaqm
       61 attaagvavg savghtlgha itggfsggan aeparpdity qepqgaplqn qqsfgpcsle
      121 ikqflecaqn qsdvklcegf nevlrqcria nvdhpptvdh geknvkrrky negflqygft
      181 saitagterp qcvicgvvls aesmkpnklk rhfeskhssf ankdtnyfrs kadglkkarf
      241 dtgsktykqn vaaveasylv alriardmkp htfaehllfp vakdsvrvmi gdefvtklsa
      301 vslsndtvrr rihdmsadil dqviqeiksa qlpafsiqld estdvancsq llvyvryikd
      361 gdfkdeflfc kplertttal dvfeavgsfl rqhkiswesv cgvctdgapa tlgcqsgfqr
      421 lvlnespkai gahcmmhlqt lamktlpqdl qdvmksvlss vsfikassln srlflqlcsd
      481 ldapskalll htegrwlsrg kvlkrifelr delkmffnqk airqfealfs dkselqkiay
      541 lvdiftilne lnlslqgqns scldlsekiq sfqmklqlwq kkldenkiym lptlsaffee
      601 hdvephkrtt vvtsvkehld mlageiswyf pnlpdvpfal arnpftvkae dvpktaqdef
      661 ieltnsdaar anfstmpvtq fwvkclqsyp ilsetvlrll lpfattslce tgfssllvik
      721 skyrsrlvve ddlrcalakt tprisdlvrk kqsqpsh
//
LOCUS       NP_001424199             664 aa            linear   ROD 08-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CHFR isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424199 XP_006249597
VERSION     NP_001424199.1
DBSOURCE    REFSEQ: accession NM_001437270.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Perdereau,D., Cailliau,K., Browaeys-Poly,E., Lescuyer,A., Carre,N.,
            Benhamed,F., Goenaga,D. and Burnol,A.F.
  TITLE     Insulin-induced cell division is controlled by the adaptor Grb14 in
            a Chfr-dependent manner
  JOURNAL   Cell Signal 27 (4), 798-806 (2015)
   PUBMED   25578860
  REMARK    GeneRIF: These results show that Chfr and Grb14 collaborate in a
            negative feedback loop controlling insulin-stimulated cell
            division.
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Jung,I., Sohn,D.H., Choi,J., Kim,J.M., Jeon,S., Seol,J.H. and
            Seong,R.H.
  TITLE     SRG3/mBAF155 stabilizes the SWI/SNF-like BAF complex by blocking
            CHFR mediated ubiquitination and degradation of its major
            components
  JOURNAL   Biochem Biophys Res Commun 418 (3), 512-517 (2012)
   PUBMED   22285184
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Oh,Y.M., Kwon,Y.E., Kim,J.M., Bae,S.J., Lee,B.K., Yoo,S.J.,
            Chung,C.H., Deshaies,R.J. and Seol,J.H.
  TITLE     Chfr is linked to tumour metastasis through the downregulation of
            HDAC1
  JOURNAL   Nat Cell Biol 11 (3), 295-302 (2009)
   PUBMED   19182791
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Ahel,I., Ahel,D., Matsusaka,T., Clark,A.J., Pines,J., Boulton,S.J.
            and West,S.C.
  TITLE     Poly(ADP-ribose)-binding zinc finger motifs in DNA
            repair/checkpoint proteins
  JOURNAL   Nature 451 (7174), 81-85 (2008)
   PUBMED   18172500
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Yu,X., Minter-Dykhouse,K., Malureanu,L., Zhao,W.M., Zhang,D.,
            Merkle,C.J., Ward,I.M., Saya,H., Fang,G., van Deursen,J. and
            Chen,J.
  TITLE     Chfr is required for tumor suppression and Aurora A regulation
  JOURNAL   Nat Genet 37 (4), 401-406 (2005)
   PUBMED   15793587
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Daniels,M.J., Marson,A. and Venkitaraman,A.R.
  TITLE     PML bodies control the nuclear dynamics and function of the CHFR
            mitotic checkpoint protein
  JOURNAL   Nat Struct Mol Biol 11 (11), 1114-1121 (2004)
   PUBMED   15467728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.33002.1,
                                           SRR26643299.51245.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..664
                     /product="E3 ubiquitin-protein ligase CHFR isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CHFR; checkpoint with
                     forkhead and ring finger domains, E3 ubiquitin protein
                     ligase"
                     /calculated_mol_wt=73894
     Region          15..124
                     /region_name="FHA_CHFR"
                     /note="forkhead associated (FHA) domain found in
                     checkpoint with forkhead and RING finger domains protein
                     (CHFR); cd22672"
                     /db_xref="CDD:438724"
     Site            order(15..22,40,48,50,53,55..56,60..61,72..78,80..92,
                     95..98,101..108,116..124)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438724"
     Region          39..>252
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Site            order(41..43,57..58,60,78..81)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438724"
     Region          299..352
                     /region_name="RING-HC_CHFR"
                     /note="RING finger, HC subclass, found in checkpoint with
                     forkhead and RING finger domains protein (CHFR); cd16503"
                     /db_xref="CDD:438166"
     Region          466..620
                     /region_name="zf-CRD"
                     /note="Cysteine rich domain with multizinc binding
                     regions; pfam17979"
                     /db_xref="CDD:465602"
     Region          632..655
                     /region_name="zf-CCHH"
                     /note="PBZ domain; pfam10283"
                     /db_xref="CDD:463043"
     CDS             1..664
                     /gene="Chfr"
                     /coded_by="NM_001437270.1:86..2080"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288734"
                     /db_xref="RGD:1306360"
ORIGIN      
        1 mephgedeqp pprepwgrll rlgaeedepq illwkrewti grrrgcdlsf psnklvsgdh
       61 cklrvdeksg evtledtstn gtvinklrvv kkqtyplqsg diiylvyrkn epehnvayly
      121 eslngkqslt qesleanken mfhvtkessg pgqgddpqvp llspmaqtcl eepqpststs
      181 dllptastss tepeltsagq khssssgpgt isispkecss lvangelssl ssvfqdneas
      241 fsllktedte elepakkkmk gdgeldlnlq lsvadqrgia qtssedvkda svkpdkmeet
      301 ltciicqdll hdcvslqpcm htfcaacysg wmersslcpt crcpverick nhilnnlvea
      361 yllqhpdksr seedvrsmda rnkitqdmlq pkvrrsfsde egssedllel sdvdsessdi
      421 sqpyivcrqc peyrrqavqs lpcpvpesel gatqalggea pstsasltta apgytcplqg
      481 shaictccfq pmpdrraehe qdsriapqqc avclqpfchl ywgctrtgcf gclapfceln
      541 lgdkcldgvl nnnnyesdil knylttrglt wknmltesll alqrgvfils dyritgntvl
      601 cyccglrsfr eltyqyrqni paselpvtvt srpdcywgrn crtqvkahha mkfnhiceqt
      661 rfkn
//
LOCUS       NP_001101937             717 aa            linear   ROD 08-APR-2025
DEFINITION  epidermal growth factor receptor kinase substrate 8-like protein 1
            [Rattus norvegicus].
ACCESSION   NP_001101937 XP_001071045 XP_006228340 XP_341783
VERSION     NP_001101937.1
DBSOURCE    REFSEQ: accession NM_001108467.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Kesti,T., Ruppelt,A., Wang,J.H., Liss,M., Wagner,R., Tasken,K. and
            Saksela,K.
  TITLE     Reciprocal regulation of SH3 and SH2 domain binding via tyrosine
            phosphorylation of a common site in CD3epsilon
  JOURNAL   J Immunol 179 (2), 878-885 (2007)
   PUBMED   17617578
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Offenhauser,N., Borgonovo,A., Disanza,A., Romano,P., Ponzanelli,I.,
            Iannolo,G., Di Fiore,P.P. and Scita,G.
  TITLE     The eps8 family of proteins links growth factor stimulation to
            actin reorganization generating functional redundancy in the
            Ras/Rac pathway
  JOURNAL   Mol Biol Cell 15 (1), 91-98 (2004)
   PUBMED   14565974
  REMARK    Erratum:[Mol Biol Cell. 2019 Sep 1;30(19):2535. doi:
            10.1091/mbc.E03-06-0427-corr. PMID: 31465253]
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Hori,K., Konno,D., Maruoka,H. and Sobue,K.
  TITLE     MALS is a binding partner of IRSp53 at cell-cell contacts
  JOURNAL   FEBS Lett 554 (1-2), 30-34 (2003)
   PUBMED   14596909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006228340.1, XP_001071045.1, XP_341783.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.799.1,
                                           SRR26643299.1162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..717
                     /product="epidermal growth factor receptor kinase
                     substrate 8-like protein 1"
                     /note="EPS8-like 1"
                     /calculated_mol_wt=79955
     Region          32..162
                     /region_name="PTB_EPS8"
                     /note="Epidermal growth factor receptor kinase substrate
                     (EPS8)-like Phosphotyrosine-binding (PTB) domain; cd01210"
                     /db_xref="CDD:269921"
     Site            order(39,118,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269921"
     Site            order(104..109,125,148,152)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269921"
     Region          482..534
                     /region_name="SH3_Eps8"
                     /note="Src Homology 3 domain of Epidermal growth factor
                     receptor kinase substrate 8 and similar proteins; cd11764"
                     /db_xref="CDD:212698"
     Site            order(482..487,489,492,495..497,504..509,511..519,
                     524..527,531..534)
                     /site_type="other"
                     /note="swapped dimer interface [polypeptide binding]"
                     /db_xref="CDD:212698"
     Site            order(489,493..495,512..514,516,525..526,528..531)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212698"
     Region          623..688
                     /region_name="SAM_EPS8-like"
                     /note="SAM domain of EPS8-like subfamily; cd09540"
                     /db_xref="CDD:188939"
     CDS             1..717
                     /gene="Eps8l1"
                     /coded_by="NM_001108467.2:396..2549"
                     /db_xref="GeneID:361503"
                     /db_xref="RGD:1311146"
ORIGIN      
        1 mstttgpeaa pkpsaksiye qrkrystvvm advsqyhvnh lvtfclgeed gvhtvedasr
       61 klavmdsqgr vwaqemllrv spghvtlldp vskeelesyp ldaivrcdav mprgrsrsll
      121 llvcqepera qpdvhffqgl llgaelired iqgalqnyrs grgerraaal ratqeelrrg
      181 aspaaetppl qrrpsvravi ntvepsavrg rpqvepipet eearkpdpar tttrssdpts
      241 pdlgprgpel aglqaerdvd ilnhvfddve sfvsrlqksa eatrvlehre rgrrtrrraa
      301 geglltlrak ppteaeytdv lqkikyafsl larlrgnian psspellhfl fgplqmivnt
      361 sggpefprsv rrphltleav allrdnvtpr enelwtslgd swtrpgvelp peegspyspe
      421 fysgweppat dpqgrpwedp vekqlqhekr rrqqsapqva vnghqdpele tesqleekar
      481 kwvlcnydfq arngselsvk hrdvlevldd rrkwwkvrdh qgqegyvpyn iltphpgpqv
      541 hcsqssainl etsppppppa aapaptqvrp qwdscdslns ldpsdkekfs qmlcvneelq
      601 arlaqgrsgp srvtpglrap epqlsprsea svvrawlqtk gfssgtvdal gvltgaqlfs
      661 lqkeelrsvc peegarvysq vtvqralled rekvseleav mekqkkkveg etktevi
//
LOCUS       NP_001424093             286 aa            linear   ROD 08-APR-2025
DEFINITION  maestro isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424093
VERSION     NP_001424093.1
DBSOURCE    REFSEQ: accession NM_001437164.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.77782.1,
                                           SRR26643429.54674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..286
                     /product="maestro isoform 1"
                     /note="protein maestro"
                     /calculated_mol_wt=32790
     Region          90..238
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          128..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          171..200
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..286
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437164.1:234..1094"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mcsktkmtek tnphpplrpt esaalmrgcl rglesvsfme qmqripnqpl ptpasqskkr
       61 rtplssffsk vswklrlqkr eplknlffvl aerargpnpr krhlamrglg ilaheapdkq
      121 vrkykkvmld llvhglydpv ssevihesvk tltimlgkiq gqrlgsffid itlqtrtlld
      181 deddsvrysa fvlfgqlaaf agrkwkkfft hqvnqtqdsl lshlqdespq vakactmavq
      241 acvpylkprk eqsfqseedq knrrlsqqls hyhpeillff yankil
//
LOCUS       NP_001424282             558 aa            linear   ROD 08-APR-2025
DEFINITION  coiled-coil domain-containing protein 63 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424282 XP_063127389
VERSION     NP_001424282.1
DBSOURCE    REFSEQ: accession NM_001437353.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Kato,H., Nozawa,K., Isotani,A.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-Mediated Rapid Generation of Multiple Mouse Lines
            Identified Ccdc63 as Essential for Spermiogenesis
  JOURNAL   Int J Mol Sci 16 (10), 24732-24750 (2015)
   PUBMED   26501274
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127389.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.696435.1,
                                           SRR26643293.85248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..558
                     /product="coiled-coil domain-containing protein 63 isoform
                     2"
                     /note="coiled-coil domain-containing protein 63"
                     /calculated_mol_wt=65522
     Region          <146..419
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..558
                     /gene="Ccdc63"
                     /coded_by="NM_001437353.1:139..1815"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:304484"
                     /db_xref="RGD:1562334"
ORIGIN      
        1 mkkhrrkvse plpelsekak eqlaeaelrk lrqqfrkmvd srkssnfrnq rmiasqykei
       61 enlkaeqaet tlllslvksp knldlnqknf telrfllqtk gdyealissm kvllgelddk
      121 ivqmerkitn qrqiflktqe annprklqkq ihiletrlnl vtvhfdtmlt snaqlrkdie
      181 dllfekaayd hvyqqlqrrl qtqkktmnva ieqstqayeq rveamarmaa mkdrqqkdis
      241 qynleirele rlydhenklk sfllvklndr tefedqakkq eavkikkhgk krkgesfesy
      301 evahlrllkl aengdlnqlt edflakeekn farftyvtel nndmetmhkr tqriqddiin
      361 lrsqqqsshe gtrnilkqme eklrkttedt diyenryrem sktleylkns veklfkkinc
      421 nateilgklg etgkitdsnl qqyfaiiekk tndllllesf rrlqeaegpd vdvpqpfvnp
      481 fwggsallkp peplrvvppv fgadsfsdkv eeveypldhs slrqlvleny lqkergkepq
      541 etllekgdei rvkkkvis
//
LOCUS       NP_001101690             292 aa            linear   ROD 08-APR-2025
DEFINITION  transmembrane protein 237 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001101690 XP_001064402 XP_237179
VERSION     NP_001101690.1
DBSOURCE    REFSEQ: accession NM_001108220.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Huang,L., Szymanska,K., Jensen,V.L., Janecke,A.R., Innes,A.M.,
            Davis,E.E., Frosk,P., Li,C., Willer,J.R., Chodirker,B.N.,
            Greenberg,C.R., McLeod,D.R., Bernier,F.P., Chudley,A.E., Muller,T.,
            Shboul,M., Logan,C.V., Loucks,C.M., Beaulieu,C.L., Bowie,R.V.,
            Bell,S.M., Adkins,J., Zuniga,F.I., Ross,K.D., Wang,J., Ban,M.R.,
            Becker,C., Nurnberg,P., Douglas,S., Craft,C.M., Akimenko,M.A.,
            Hegele,R.A., Ober,C., Utermann,G., Bolz,H.J., Bulman,D.E.,
            Katsanis,N., Blacque,O.E., Doherty,D., Parboosingh,J.S.,
            Leroux,M.R., Johnson,C.A. and Boycott,K.M.
  TITLE     TMEM237 is mutated in individuals with a Joubert syndrome related
            disorder and expands the role of the TMEM family at the ciliary
            transition zone
  JOURNAL   Am J Hum Genet 89 (6), 713-730 (2011)
   PUBMED   22152675
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Zuniga,F.I. and Craft,C.M.
  TITLE     Deciphering the structure and function of Als2cr4 in the mouse
            retina
  JOURNAL   Invest Ophthalmol Vis Sci 51 (9), 4407-4415 (2010)
   PUBMED   20375344
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473965.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064402.1, XP_237179.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..292
                     /product="transmembrane protein 237 isoform 2"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 4"
                     /calculated_mol_wt=32704
     Region          27..269
                     /region_name="TMEM237"
                     /note="Transmembrane protein 237; pfam15383"
                     /db_xref="CDD:464690"
     CDS             1..292
                     /gene="Tmem237"
                     /gene_synonym="Als2cr4"
                     /coded_by="NM_001108220.1:463..1341"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:316412"
                     /db_xref="RGD:1306705"
ORIGIN      
        1 mdvepreevv ipkprrkakk mqpaepqyas elgvededvi tdeqstlehh srftaptgvs
       61 qpvgkifvek srrfqaadrs elikttenvd vsmdmkpswt trdvalsvhr afrmiglfsh
      121 gflagcavwn ivvicvlagd qfsnvsnllq qykplaypfq sllylllals tvsafdridf
      181 aktsvairnf laleptalas flyftaltls lsqqmtsdri ylyepsvngs lwpaeveepv
      241 lmpwvivnlv vallvglawl flsyrpgmdl seelmffsdv deypergvka sp
//
LOCUS       NP_001423799             981 aa            linear   ROD 08-APR-2025
DEFINITION  calsyntenin-1 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423799 XP_038966028
VERSION     NP_001423799.1
DBSOURCE    REFSEQ: accession NM_001436870.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Zhou,F., Hu,R., Wang,Y., Wu,X., Chen,X., Xi,Z. and Zeng,K.
  TITLE     Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models
  JOURNAL   Synapse 78 (5), e22307 (2024)
   PUBMED   39171546
  REMARK    GeneRIF: Calsyntenin-1 expression and function in brain tissue of
            lithium-pilocarpine rat seizure models.
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Ster,J., Steuble,M., Orlando,C., Diep,T.M., Akhmedov,A.,
            Raineteau,O., Pernet,V., Sonderegger,P. and Gerber,U.
  TITLE     Calsyntenin-1 regulates targeting of dendritic NMDA receptors and
            dendritic spine maturation in CA1 hippocampal pyramidal cells
            during postnatal development
  JOURNAL   J Neurosci 34 (26), 8716-8727 (2014)
   PUBMED   24966372
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 981)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 981)
  AUTHORS   Vagnoni,A., Perkinton,M.S., Gray,E.H., Francis,P.T., Noble,W. and
            Miller,C.C.
  TITLE     Calsyntenin-1 mediates axonal transport of the amyloid precursor
            protein and regulates Abeta production
  JOURNAL   Hum Mol Genet 21 (13), 2845-2854 (2012)
   PUBMED   22434822
  REMARK    GeneRIF: findings show that amyloid precursor protein (APP) and
            calsyntenin-1 are co-transported through axons, that loss of
            calsyntenin-1 disrupts axonal transport of APP and that
            calsyntenin-1 loss also leads to altered APP processing and
            increased production of Abeta
REFERENCE   6  (residues 1 to 981)
  AUTHORS   Araki,Y., Kawano,T., Taru,H., Saito,Y., Wada,S., Miyamoto,K.,
            Kobayashi,H., Ishikawa,H.O., Ohsugi,Y., Yamamoto,T., Matsuno,K.,
            Kinjo,M. and Suzuki,T.
  TITLE     The novel cargo Alcadein induces vesicle association of kinesin-1
            motor components and activates axonal transport
  JOURNAL   EMBO J 26 (6), 1475-1486 (2007)
   PUBMED   17332754
REFERENCE   7  (residues 1 to 981)
  AUTHORS   Konecna,A., Frischknecht,R., Kinter,J., Ludwig,A., Steuble,M.,
            Meskenaite,V., Indermuhle,M., Engel,M., Cen,C., Mateos,J.M.,
            Streit,P. and Sonderegger,P.
  TITLE     Calsyntenin-1 docks vesicular cargo to kinesin-1
  JOURNAL   Mol Biol Cell 17 (8), 3651-3663 (2006)
   PUBMED   16760430
  REMARK    GeneRIF: Calsyntenin-1 links a certain type of vesicular and
            tubulovesicular organelles to the Kinesin-1 motor.
REFERENCE   8  (residues 1 to 981)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
REFERENCE   9  (residues 1 to 981)
  AUTHORS   Araki,Y., Tomita,S., Yamaguchi,H., Miyagi,N., Sumioka,A., Kirino,Y.
            and Suzuki,T.
  TITLE     Novel cadherin-related membrane proteins, Alcadeins, enhance the
            X11-like protein-mediated stabilization of amyloid beta-protein
            precursor metabolism
  JOURNAL   J Biol Chem 278 (49), 49448-49458 (2003)
   PUBMED   12972431
REFERENCE   10 (residues 1 to 981)
  AUTHORS   Vogt,L., Schrimpf,S.P., Meskenaite,V., Frischknecht,R., Kinter,J.,
            Leone,D.P., Ziegler,U. and Sonderegger,P.
  TITLE     Calsyntenin-1, a proteolytically processed postsynaptic membrane
            protein with a cytoplasmic calcium-binding domain
  JOURNAL   Mol Cell Neurosci 17 (1), 151-166 (2001)
   PUBMED   11161476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_038966028.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21972.1,
                                           SRR26643297.21145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..981
                     /product="calsyntenin-1 isoform 1 precursor"
                     /note="alc-alpha; alcadein-alpha"
                     /calculated_mol_wt=106407
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2963
     Region          41..159
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(48..49,117,119,156,158..159)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          168..258
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          365..>477
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          566..918
                     /region_name="CLSTN_C"
                     /note="Calsyntenin C-terminal; pfam19699"
                     /db_xref="CDD:466150"
     CDS             1..981
                     /gene="Clstn1"
                     /coded_by="NM_001436870.1:207..3152"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:313717"
                     /db_xref="RGD:1306458"
ORIGIN      
        1 mlrrpapala ravrlllagl lygggvwaar vnkhkpwlep tyhgivtend ntvlldppli
       61 aldkdsplrf aesfevtvtk egeicgfkih gqnvpfdavv vdkstgegii rskekldcel
      121 qkdytftiqa ydcgkgpdgt gvkkshkatv hiqvndvney apvfkeksyk aavvegkqhg
      181 silrveavda dcspqfsqic syeiltpdvp ftvdkdgyik nteklnygke hqykltvtay
      241 dcgkkrated vlvkisvkpt cspgwqgwss rieyepgtga lavfpsihle tcdepvasvq
      301 atveletshi gkgcdrdtys ekslhrlcga aagtsellps psssfnwtvg lptdnghdsd
      361 qvfefngtqa vripdgvvtl dpkepftisv wmrhgpfgrk ketilcssdk tdmnrhhysl
      421 yvhgcrlifl lrqdpseekk yrpaefhwkl nqvcdedwhh fvlnvevpsv tlyvdgvshe
      481 pfsvtedypl hptkietqlv vgacwqeysg vesgnetepv tmasaggdlh mtqffrgnla
      541 gltvrsgkla dkkvidclyt ckegldlqvp edgnrgvqiq tsssqavltl egenvgeldk
      601 amqhisylns rqfptpgirr lkitstvkcf neaacievpp vegyvmvlqp eepkislsgv
      661 hhfaraasef espegvslfp elkiistitr evepeadgae dptvqeslvs eeivhdldtc
      721 evtvegeeln aeqeslevdv arlqqkgiev nhsdlgvvft gvetmasyee vlhllryrnw
      781 htrslldrkf klicselngr ylsnefkvev nvihtanpve hanhmaaqpq fvhpehrsfv
      841 dlsghnlasp hpfavvpsta tvvivvcvsf lvfmiilgvf riraahqrtm rdqdtgkene
      901 mdwddsalti tvnpmetyed qhsseeeeee eeeeesedge eeeditsaes esseeeeggp
      961 gdgqnttrqq qlewdystls y
//
LOCUS       NP_001094440            1128 aa            linear   ROD 08-APR-2025
DEFINITION  adipocyte enhancer-binding protein 1 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001094440 XP_001069152 XP_223583
VERSION     NP_001094440.1
DBSOURCE    REFSEQ: accession NM_001100970.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Blackburn,P.R., Xu,Z., Tumelty,K.E., Zhao,R.W., Monis,W.J.,
            Harris,K.G., Gass,J.M., Cousin,M.A., Boczek,N.J., Mitkov,M.V.,
            Cappel,M.A., Francomano,C.A., Parisi,J.E., Klee,E.W., Faqeih,E.,
            Alkuraya,F.S., Layne,M.D., McDonnell,N.B. and Atwal,P.S.
  TITLE     Bi-allelic Alterations in AEBP1 Lead to Defective Collagen Assembly
            and Connective Tissue Structure Resulting in a Variant of
            Ehlers-Danlos Syndrome
  JOURNAL   Am J Hum Genet 102 (4), 696-705 (2018)
   PUBMED   29606302
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   4  (residues 1 to 1128)
  AUTHORS   Didangelos,A., Yin,X., Mandal,K., Baumert,M., Jahangiri,M. and
            Mayr,M.
  TITLE     Proteomics characterization of extracellular space components in
            the human aorta
  JOURNAL   Mol Cell Proteomics 9 (9), 2048-2062 (2010)
   PUBMED   20551380
REFERENCE   5  (residues 1 to 1128)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 1128)
  AUTHORS   Lyons,P.J., Muise,A.M. and Ro,H.S.
  TITLE     MAPK modulates the DNA binding of adipocyte enhancer-binding
            protein 1
  JOURNAL   Biochemistry 44 (3), 926-931 (2005)
   PUBMED   15654748
REFERENCE   7  (residues 1 to 1128)
  AUTHORS   He,G.P., Muise,A., Li,A.W. and Ro,H.S.
  TITLE     A eukaryotic transcriptional repressor with carboxypeptidase
            activity
  JOURNAL   Nature 378 (6552), 92-96 (1995)
   PUBMED   7477299
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Aug 12, 2007 this sequence version replaced
            XP_223583.4, XP_001069152.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC133065.1, SRR26643299.55417.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1128
                     /product="adipocyte enhancer-binding protein 1 isoform 1
                     precursor"
                     /note="adipocyte enhancer-binding protein 1; aortic
                     carboxypeptidase-like protein"
                     /calculated_mol_wt=125609
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2471
     mat_peptide     26..1128
                     /product="Adipocyte enhancer-binding protein 1.
                     /id=PRO_0000333191"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
                     /calculated_mol_wt=125609
     Region          40..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          378..531
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          382..547
                     /region_name="Required for DNA-binding and interaction
                     with NFKBIA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          413..616
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Site            order(426,454,461)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            520
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          547..977
                     /region_name="Interaction with PTEN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          556..895
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(617,620,682,691..692,755..756,762,866)
                     /site_type="active"
                     /db_xref="CDD:349427"
     Region          899..974
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     Region          933..1128
                     /region_name="Required for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          998..1128
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          1027..1056
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     CDS             1..1128
                     /gene="Aebp1"
                     /coded_by="NM_001100970.2:197..3583"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:305494"
                     /db_xref="RGD:1306922"
ORIGIN      
        1 maavrtasll cgllallalc pegspqtvlt ddeiqefleg flsefetqsp preddveaqp
       61 lpeptqrark skaggkprad aeappeknkd kekkgkkdkg pkaakhlegs trptkkpkek
      121 ppkatkkpke kppkatkkpk ekppkatkkp kekppkatkr psagkrfstv apletpersl
      181 tspsnpgtre lpeergrtsl ntwqgqgeet qvearqhrpe peeetemptl dyndqiered
      241 yedfeyirrq kqprptpsrk riwpeppeek tqepeerkev dpplkpllpp dygdgylipn
      301 yddldyyfph pppqkpdvgq evdeekeelk kpkkegsspk edtedkwaae knkdhkagpr
      361 kgeeleeewg pvekikcppi gmeshriedn qirassmlrh glgaqrgrln mqaganeddy
      421 ydgawcaede sqtqwievdt rrttrftgvi tqgrdssihd dfvttffvgf sndsqtwvmy
      481 tngyeemtfh gnvdkdtpvl selpepvvar firiypltwn gslcmrlevl gcpvtpvysy
      541 yaqnevvttd sldfrhhsyk dmrqlmkvvn eecptitrty slgkssrglk iyameisdnp
      601 gehelgepef rytagmhgne vlgrelllll mqylcheyrd gnprvrnlvq dtrihlvpsl
      661 npdgyevaaq mgsefgnwal glwteegfdi fedfpdlnsv lwaaeekkwv pyrvpnnnlp
      721 iperylspda tvstevraii swmeknpfvl ganlnggerl vsypydmart psqeqllaaa
      781 laaargeded evseaqetpd haifrwlais fasahltmte pyrggcqaqd ytsgmgivng
      841 akwnprsgtf ndfsylhtnc lelsiylgcd kfpheselpr ewennkeall tfmeqvhrgi
      901 kgvvtdeqgi pianatisvs ginhgvktas ggdywrilnp geyrvtahae gytssakicn
      961 vdydigatqc nfilarsnwk rireilamng nrpilrvdps rpmtpqqrrl qqrrlryrlr
     1021 mreqmrlrrl nsttgpatsp tpaltlppsp tpgstsrlwe ilpttaagwe esetetytev
     1081 vtefeteygp dleveeleee eeeeeemdtg ltfpvttvet ytvnfgdf
//
LOCUS       NP_001424275            2205 aa            linear   ROD 08-APR-2025
DEFINITION  kinetochore-associated protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424275 XP_008767450
VERSION     NP_001424275.1
DBSOURCE    REFSEQ: accession NM_001437346.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2205)
  AUTHORS   Civril,F., Wehenkel,A., Giorgi,F.M., Santaguida,S., Di Fonzo,A.,
            Grigorean,G., Ciccarelli,F.D. and Musacchio,A.
  TITLE     Structural analysis of the RZZ complex reveals common ancestry with
            multisubunit vesicle tethering machinery
  JOURNAL   Structure 18 (5), 616-626 (2010)
   PUBMED   20462495
REFERENCE   2  (residues 1 to 2205)
  AUTHORS   Chan,G.K., Jablonski,S.A., Starr,D.A., Goldberg,M.L. and Yen,T.J.
  TITLE     Human Zw10 and ROD are mitotic checkpoint proteins that bind to
            kinetochores
  JOURNAL   Nat Cell Biol 2 (12), 944-947 (2000)
   PUBMED   11146660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_008767450.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.47971.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2205
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15-q16"
     Protein         1..2205
                     /product="kinetochore-associated protein 1 isoform 1"
                     /note="kinetochore-associated protein 1;
                     kinetochore-associated protein 1-like"
                     /calculated_mol_wt=250440
     Region          486..>744
                     /region_name="Rod_C"
                     /note="Rough deal protein C-terminal region; pfam10493"
                     /db_xref="CDD:463114"
     Region          1580..2127
                     /region_name="Rod_C"
                     /note="Rough deal protein C-terminal region; pfam10493"
                     /db_xref="CDD:463114"
     CDS             1..2205
                     /gene="Kntc1"
                     /coded_by="NM_001437346.1:141..6758"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304477"
                     /db_xref="RGD:1307905"
ORIGIN      
        1 mwnniellts ddtgsgflnv gsrkesvtal yqvdllgkis sektslspki qacslsdgfi
       61 ivadqsvill dstcrslqlf lifdtdvdvv glcpegkflf vgersgnfhl iyvtskrtlf
      121 tkafvekaed ertyrslvie kdgsnegtyy mllltnngff yitnlqlsqi eqaientdld
      181 sakklqgqfk csfistesyh ssgclnllas qsgkfanets viiggtgsca fskwepdstk
      241 kdmslknfvd tdiirgaksf qlidnllfvl dtdnvlslwd aytltpvwnw pslpieqfll
      301 tteadspssv twqgitnlkl vtltattkek mrnliiyslp tmeilyslev ssvsslvqtg
      361 istdtiylle gvhkndpnlc edsvsnlelr yltevlpenr lsrllhkhrf adaesfaiqf
      421 gldvelvykv ksndilekla lisdkseqse wqqlvdeake nlckiqdddf vvnfclkaqw
      481 vtyettqeml syaktrlmkk edrtlpacsd dflevlkaha klttfygafg pekfsgsawv
      541 eflnneddlk difvqlsegn fdcaqylwlr hradfeskfd vkmlenllns istqipvekl
      601 cswfkndvip fvrrivpegq nilakwleqa srnleltdka nwpenglqla evfftaektd
      661 kfgfssswhw islkdyqnte evqqlrtlvs klqeliilhr kyncrlalse fekenattvv
      721 frmfdrvsap elipsvlekf vrvyireqnl qeeellllyi edllkrcssk smtlfdtawe
      781 akamavircl sdtdlifdav lkimykavvp wsaaveqlvr qhlemdhpkv kllqesyrlm
      841 emkkllrgyg irevnllnke imrvvryilk qdipssleda lkvaqgyrls ddeiyslrvi
      901 dlidrdqged cllllrslpp seaektaerv iiwarlalqe epdgseedka wrisvaktsm
      961 dilkilcdiq kdnlqkkdda eeflkrfkmv aslqenfevf lpfedysdtg lvaglreqyi
     1021 kaqenaqaeh kfrgppgptp amgtnasvks klhrqalvlq vstqeleaem alralkdgkv
     1081 avalskcrdl lkhycnadtg rllfvvcqkl chmladdvpm vapvglnlps eihdltchav
     1141 ticspdflld vlelskytlt avelcrqcqm ddcgilmkaa vgthkdpyee wsysdffsed
     1201 givlesqvvl pviyelissv vplaegkrrp ldsislpycs tsegenlilp lvssisallr
     1261 nlqessqwel alrfvvasfg tclqhsvsnv msmslsekll gkstlassrq iimelkeksi
     1321 afirgsattl lhkvfncrlv dldlalayct llpqkdvfen lwkfidkawq nydkilalsl
     1381 vgsrlanlyq dvetglrfhe lsidakwgir lgklgisfqp afrqnflskk dlikalvnni
     1441 dmdtsliley cstfqldsda alrlfietll rnttsqsqgg dapeptqhqh skllqkatem
     1501 vpllkstkdl vislteilyk ldpydyemie vvlkvieqan ekittvninq alnllrhlks
     1561 yrrmsppvdl eyqymlehli tlppaaqtrl pfhlilfgta qnfwkilsse lseeslptll
     1621 lisklmkfsl dtlyvstakh vfeknlkpkl lksaqarssv mskevdklvq tlesyllsiv
     1681 npewavaiai sltqeipegp fkmtslkfcl ylaerwlqni ppqdetcekv kalqkklylq
     1741 frlsgteavl iahklndqey lrvvgkpahl ivslyehpsi serlcttsgk dypdihaaak
     1801 eiaevneinl ekiwdmllek wlcpstapge kaseffelee devlhrvvyl lqarpidyss
     1861 rmlfvfatsa tstlgirqlt fahraralqc llyladketi eslfkkptee mksylkcitf
     1921 lasfetlnip ityelfcnsp kegmikglwk nhshepmavr lvaelcleyk iydlqlwngl
     1981 lqkllgfnmi pylrkvlsci ssvhslwqvp yfskawqrvi qipllsascp lrpsqladcc
     2041 eslvailecp vsddldmmgv akqyvqlelp afaltcltlm phsekrhqqi knflnscdaq
     2101 iilqqleehm nagqlaglsq qirslvlnhv vnkkefgila ktkyfqllkr hvintdnvte
     2161 lvnylandls ldeasslite yskhcgkpvp adtapseilk tflgs
//
LOCUS       NP_001424509             493 aa            linear   ROD 08-APR-2025
DEFINITION  myocyte-specific enhancer factor 2A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424509 XP_008757763
VERSION     NP_001424509.1
DBSOURCE    REFSEQ: accession NM_001437580.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Carrillo,E.D., Hernandez,D.I., Clara,M.V., Lezama,I., Garcia,M.C.
            and Sanchez,J.A.
  TITLE     Exercise increases MEF2A abundance in rat cardiac muscle by
            downregulating microRNA-223-5p
  JOURNAL   Sci Rep 13 (1), 14481 (2023)
   PUBMED   37660209
  REMARK    GeneRIF: Exercise increases MEF2A abundance in rat cardiac muscle
            by downregulating microRNA-223-5p.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   He,T., Huang,J., Chen,L., Han,G., Stanmore,D., Krebs-Haupenthal,J.,
            Avkiran,M., Hagenmuller,M. and Backs,J.
  TITLE     Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5
  JOURNAL   J Mol Cell Cardiol 145, 88-98 (2020)
   PUBMED   32485181
  REMARK    GeneRIF: Cyclic AMP represses pathological MEF2 activation by
            myocyte-specific hypo-phosphorylation of HDAC5.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Meyer,M., Berger,I., Winter,J. and Jurek,B.
  TITLE     Oxytocin alters the morphology of hypothalamic neurons via the
            transcription factor myocyte enhancer factor 2A (MEF-2A)
  JOURNAL   Mol Cell Endocrinol 477, 156-162 (2018)
   PUBMED   29928931
  REMARK    GeneRIF: the present study reveals a previously unknown OTR-coupled
            MAPK-MEF-2A pathway, which is responsible for oxytocin-induced
            neurite retraction of hypothalamic neurons.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Wu,R., Wang,J., Yao,J., Dong,Z., Liu,Y. and Liu,M.
  TITLE     MEF2A regulates Calpain 3 expression in L6 myoblasts
  JOURNAL   Gene 668, 204-210 (2018)
   PUBMED   29783071
  REMARK    GeneRIF: MEF2A is a transcriptional regulator for Capn3 gene
            expression.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Zhu,B., Carmichael,R.E., Solabre Valois,L., Wilkinson,K.A. and
            Henley,J.M.
  TITLE     The transcription factor MEF2A plays a key role in the
            differentiation/maturation of rat neural stem cells into neurons
  JOURNAL   Biochem Biophys Res Commun 500 (3), 645-649 (2018)
   PUBMED   29678571
  REMARK    GeneRIF: MEF2A participates in neuronal differentiation/maturation
            from neural stem cells.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Katoh,Y., Molkentin,J.D., Dave,V., Olson,E.N. and Periasamy,M.
  TITLE     MEF2B is a component of a smooth muscle-specific complex that binds
            an A/T-rich element important for smooth muscle myosin heavy chain
            gene expression
  JOURNAL   J Biol Chem 273 (3), 1511-1518 (1998)
   PUBMED   9430690
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Lin,X., Shah,S. and Bulleit,R.F.
  TITLE     The expression of MEF2 genes is implicated in CNS neuronal
            differentiation
  JOURNAL   Brain Res Mol Brain Res 42 (2), 307-316 (1996)
   PUBMED   9013788
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Komuro,I., Schalling,M., Jahn,L., Bodmer,R., Jenkins,N.A.,
            Copeland,N.G. and Izumo,S.
  TITLE     Gtx: a novel murine homeobox-containing gene, expressed
            specifically in glial cells of the brain and germ cells of testis,
            has a transcriptional repressor activity in vitro for a
            serum-inducible promoter
  JOURNAL   EMBO J 12 (4), 1387-1401 (1993)
   PUBMED   8096811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_008757763.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.1302.1,
                                           SRR26643292.2341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345329,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..493
                     /product="myocyte-specific enhancer factor 2A isoform 4"
                     /note="myocyte-specific enhancer factor 2A"
                     /calculated_mol_wt=52768
     Region          1..>235
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          <125..>370
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..493
                     /gene="Mef2a"
                     /coded_by="NM_001437580.1:311..1792"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:309957"
                     /db_xref="RGD:1359360"
ORIGIN      
        1 mgrkkiqitr imdernrqvt ftkrkfglmk kayelsvlcd ceialiifns snklfqyast
       61 dmdkvllkyt eynephesrt nsdivetlrk kglngcespd addyfehspl sedrfsklne
      121 dsdfifkrgp pglppqnfsm svtvpvtspn alsytnpgss lvspslaass tlaessmlsp
      181 ppatlhrnvs pgapqrppst gsaggmlstt dltvpngagn spvgngfvns raspnlignt
      241 gansvgkvmp tksppppggg svgmnsrkpd lrvvippssk gmmpplnaqr isssqatqpl
      301 atpvvsvttp slppqglvys amptayntdy sltsadlsal qgftspgmls lgqasawqqh
      361 hlgqaalssl vaggqlsqgs nlsintnqni niksepispp rdrmtpsgfq qqqqqqpqqq
      421 pppqppqpqp qprqemgrsp vdslssssss ydgsdredpr gdfhspivlg rppnaedres
      481 psvkrmrmdt wvt
//
LOCUS       NP_001099630            1433 aa            linear   ROD 08-APR-2025
DEFINITION  trafficking protein particle complex subunit 8 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001099630 XP_001053125 XP_214614
VERSION     NP_001099630.1
DBSOURCE    REFSEQ: accession NM_001106160.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1433)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_214614.4, XP_001053125.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.226276.1,
                                           SRR26643287.34499.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1433
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..1433
                     /product="trafficking protein particle complex subunit 8
                     isoform 1"
                     /note="trafficking protein particle complex subunit
                     8-like; trafficking protein particle complex 8"
                     /calculated_mol_wt=160220
     Region          160..604
                     /region_name="TRAPPC-Trs85"
                     /note="ER-Golgi trafficking TRAPP I complex 85 kDa
                     subunit; pfam12739"
                     /db_xref="CDD:463688"
     CDS             1..1433
                     /gene="Trappc8"
                     /gene_synonym="RGD1309102"
                     /coded_by="NM_001106160.2:344..4645"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:291750"
                     /db_xref="RGD:1309102"
ORIGIN      
        1 maqcvqsvqe lipdsfvpcv aalcsdeaer ltrlnhlsfa ellkpfsrlt sevhmrdpnn
       61 qlhiiknlki avsnivtqpp qpgaigklln dvvsgsqpae glvanvitag dydlnisatt
      121 pwfesyretf lqsmpasdhe flnhylacml vassaeaepm eqfsklsqeq hriqhnsdys
      181 ypkwfipntl kyyvllhdvt sgdeqraesi yeemkqkygt qgcyllkins rapnrasdeq
      241 ipdpwsqylq knsiqnqesy edgpctmtss knsdsnllsl dgldnevkdg lpdncrvhpl
      301 qidqcgdtph ntdgsdhaks assvhetkka stglirgacl tltdhdrirq fiqeftfrgl
      361 lphvektirq lndqlisrkg lsrslfsatk kwfsgskvpe ksiselksts gllyppeape
      421 lqirkmadlc flvqhydlay scyhtakkdf lndqamlyaa galemaavsa flqpgaprpy
      481 pahymdtaiq tyrdicknmv laercvllsa eilksqskya eaaallirlt sedsdlrsal
      541 lleqaahcfi nmknpmvrky afhmilaghr fskagqkkha lrcycqamqv ykgkgwslae
      601 dhinftigrq sytlrqldna vsafrhilin eskqsaaqqg aflreylyvy knvnqlspdg
      661 plpqlplpyi nssatrvffg hdrrpadgek qaathvsldq eydaessqqw releehvvav
      721 ankgvipssf yptqyclnsy sdnsrfplav veepitveva frnplkvpll lsdlsllwkf
      781 qpkdtsgkdt ekervtgepe migtevisef linseeskva rlklfphhig elhilgvvyn
      841 lgtiqgsvtv dgigalpgch tgkhslgmsv rgrqdleiqg prlnntkeek tsvkygpdrr
      901 ldpivteemp llevffihfp tgllcgeirk ayvefvnvsq cpltalkvvs krpefftfgg
      961 ntaaltplsp stsencsayk tvvtaspslg tafvstassv dfgtgtgqql eaipvplpds
     1021 vllpgasvql pmwlrgpdee gvheinflfy yesvkkqpkk rhrilrhtav ictsrslnvr
     1081 atvcrsnsle deegrggnml vfvdventnt seagvkefhm vqvsssskhw qlhrsvnise
     1141 nrdaklasre kgkfcfkavr ckqkegdkqs sekytfadii fgneqiissa spcadffyrs
     1201 lsselrrtqd qlpaypekna segavrliek csevdlsivv lwkayvvedn kqlilegqhh
     1261 vvvrtvgkea cshsqkqepp emellkffrp enttvsarps veqlsnlikt slhypesfhh
     1321 pfhqkslclv pvtlllsncs kaevdvivdl rhkttspeal ethgsftwlg qtqyklqlks
     1381 qethslqlka cfvhtgvynl gtprvfakls dqvtvfetsq qnsmpaliii nna
//
LOCUS       NP_001099845             614 aa            linear   ROD 08-APR-2025
DEFINITION  bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
            [Rattus norvegicus].
ACCESSION   NP_001099845 XP_001079800 XP_215288
VERSION     NP_001099845.2
DBSOURCE    REFSEQ: accession NM_001106375.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Kurima,K., Singh,B. and Schwartz,N.B.
  TITLE     Genomic organization of the mouse and human genes encoding the ATP
            sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2
  JOURNAL   J Biol Chem 274 (47), 33306-33312 (1999)
   PUBMED   10559207
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Rusiniak,M.E., O'Brien,E.P., Novak,E.K., Barone,S.M., McGarry,M.P.,
            Reddington,M. and Swank,R.T.
  TITLE     Molecular markers near the mouse brachymorphic (bm) gene, which
            affects connective tissues and bleeding time
  JOURNAL   Mamm Genome 7 (2), 98-102 (1996)
   PUBMED   8835524
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Johnson,D.R.
  TITLE     The growth of femur and tibia in three genetically distinct
            chondrodystrophic mutants of the house mouse
  JOURNAL   J Anat 125 (Pt 2), 267-275 (1978)
   PUBMED   624676
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 14, 2008 this sequence version replaced NP_001099845.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169061.1, SRR26643429.5407.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..614
                     /product="bifunctional 3'-phosphoadenosine
                     5'-phosphosulfate synthase 2"
                     /calculated_mol_wt=69281
     Region          22..216
                     /region_name="CysC"
                     /note="Adenylylsulfate kinase or related kinase [Inorganic
                     ion transport and metabolism]; COG0529"
                     /db_xref="CDD:440295"
     Region          243..606
                     /region_name="ATPS"
                     /note="ATP-sulfurylase; cd00517"
                     /db_xref="CDD:173895"
     Site            order(407..411,417,420,484,509..511,513..514,550..552)
                     /site_type="active"
                     /db_xref="CDD:173895"
     Site            414..417
                     /site_type="other"
                     /note="HXXH motif"
                     /db_xref="CDD:173895"
     Site            445..455
                     /site_type="other"
                     /note="flexible loop"
                     /db_xref="CDD:173895"
     CDS             1..614
                     /gene="Papss2"
                     /coded_by="NM_001106375.3:60..1904"
                     /db_xref="GeneID:294103"
                     /db_xref="RGD:1307012"
ORIGIN      
        1 mseikkqktd qqkstnvvyq ahhvsrnkrg qvvgtrggfr gctvwltgls gagkttisfa
       61 leeylvshai pcysldgdnv rhglnknlgf sagdreenir riaevaklfa daglvcitsf
      121 ispfakdren arkihesagl pffeifvdap lnicesrdvk glykrarage ikgftgidsn
      181 yekpetpecv lktnlssvsd cvqqvvellq eqsivphtti kgihelfvpe nkidqirael
      241 etlpslpitk ldlqwvqils egwatplkgf mrekeylqtl hfdtllddgv inmsipivlp
      301 vsgddkarle gcskfalmye grrvallqdp efyehrkeer csrvwgtasa khphikmvme
      361 ggdwlvggdl qvlerirwnd gldqyrltpl elkqkckdmd adavfafqlr npvhnghall
      421 mqdtrrrlle rgykhpvlll hplggwtkdd dvpldwrmkq haavleegil dpkstivaif
      481 pspmlyagpt evqwhcrcrm iaganfyivg rdpagmphpe tkkdlyepth ggkvlsmapg
      541 ltsveiipfr vaaynkikka mdfydparhd efdfisgtrm rklaregedp pdgfmapkaw
      601 kvltdyyrsl ekin
//
LOCUS       NP_001257345             169 aa            linear   ROD 08-APR-2025
DEFINITION  uncharacterized protein LOC100363294 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001257345 XP_002728579 XP_003753082
VERSION     NP_001257345.2
DBSOURCE    REFSEQ: accession NM_001270416.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Thelie,A., Pascal,G., Angulo,L., Perreau,C., Papillier,P. and
            Dalbies-Tran,R.
  TITLE     An oocyte-preferential histone mRNA stem-loop-binding protein like
            is expressed in several mammalian species
  JOURNAL   Mol Reprod Dev 79 (6), 380-391 (2012)
   PUBMED   22467188
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Nov 27, 2020 this sequence version replaced NP_001257345.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ361072.1, SRR26360181.310743.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..169
                     /product="uncharacterized protein LOC100363294 isoform 1"
                     /note="stem loop binding protein 2"
                     /calculated_mol_wt=19608
     Region          27..96
                     /region_name="SLBP_RNA_bind"
                     /note="Histone RNA hairpin-binding protein RNA-binding
                     domain; pfam15247"
                     /db_xref="CDD:464587"
     CDS             1..169
                     /gene="Slbpl"
                     /gene_synonym="SLBP2"
                     /coded_by="NM_001270416.3:343..852"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100363294"
                     /db_xref="RGD:2323347"
ORIGIN      
        1 mslssrmemv svgvttepch arwevetdev vlrrrqkqid ygkctpgyqs flqqvpraqr
       61 qpgfhpqtpn knrrysrrsw daqirqwrra lhtwdppsqp lhdrqaegka agnflrpvdt
      121 aplddlldnw pqdpessenw drgekeaqfa ylkvpascpp qlkdellhh
//
LOCUS       NP_001424458             479 aa            linear   ROD 08-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424458 XP_006254699
VERSION     NP_001424458.1
DBSOURCE    REFSEQ: accession NM_001437529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Xu,K., Shimelis,H., Linn,D.E., Jiang,R., Yang,X., Sun,F., Guo,Z.,
            Chen,H., Li,W., Chen,H., Kong,X., Melamed,J., Fang,S., Xiao,Z.,
            Veenstra,T.D. and Qiu,Y.
  TITLE     Regulation of androgen receptor transcriptional activity and
            specificity by RNF6-induced ubiquitination
  JOURNAL   Cancer Cell 15 (4), 270-282 (2009)
   PUBMED   19345326
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254699.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.73789.1,
                                           SRR26643299.62597.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..479
                     /product="E3 ubiquitin-protein ligase RNF14 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="androgen receptor associated protein 54; triad2
                     protein; E3 ubiquitin-protein ligase RNF14"
                     /calculated_mol_wt=53976
     Region          9..135
                     /region_name="RWD_RNF14"
                     /note="RWD domain of RING finger protein 14 (RNF14) and
                     related proteins; cd23820"
                     /db_xref="CDD:467656"
     Region          218..276
                     /region_name="RING-HC_RBR_RNF14"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 14 (RNF14) and similar proteins; cd16628"
                     /db_xref="CDD:438290"
     Region          305..361
                     /region_name="BRcat_RBR_RNF14"
                     /note="BRcat domain found in RING finger protein 14
                     (RNF14); cd20341"
                     /db_xref="CDD:439002"
     Region          394..461
                     /region_name="Rcat_RBR_RNF14"
                     /note="Rcat domain found in RING finger protein 14
                     (RNF14); cd20354"
                     /db_xref="CDD:439015"
     CDS             1..479
                     /gene="Rnf14"
                     /gene_synonym="ARA54"
                     /coded_by="NM_001437529.1:761..2200"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:619577"
                     /db_xref="RGD:1589576"
ORIGIN      
        1 msaedleaqe dellalasiy dgdefrkaes vqggetriyl dlpqnfkifv sgnsneclqn
       61 sgfeyticfl pplvlnfelp pdypssspps ftlsgkwlsp tqlsalckhl dnlweehrgr
      121 vvlfawmqfl keetltylni vspfelkmgs qkkvqrrtta qassntelal ggaaaaaaas
      181 dvdqedsvde ravqdvesls sliqeildfn qdrqmkcfns klflcsicfc eklgsdcmyf
      241 lecrhvycka clkdyfeiqi kdgqvkclnc pepqcssvat pgqvkelvea dlfarydrll
      301 lqstldlmad vvycprpccq lpvmqepggt maicsscnfa fctlcrltyh gvspckvtae
      361 klidlrneyl qadeatkrfl eqrygkrviq kaleemeskd wleknskscp ccgtpiqkld
      421 gcnkmtctgc mqyfcwvcmg slsranpykh ftdpdspcfn rlfhavdvng diwedeied
//
LOCUS       NP_001424256             799 aa            linear   ROD 08-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 2 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001424256 XP_063133436
VERSION     NP_001424256.1
DBSOURCE    REFSEQ: accession NM_001437327.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Cruz-Garcia,D., Vazquez-Martinez,R., Peinado,J.R., Anouar,Y.,
            Tonon,M.C., Vaudry,H., Castano,J.P. and Malagon,M.M.
  TITLE     Identification and characterization of two novel (neuro)endocrine
            long coiled-coil proteins
  JOURNAL   FEBS Lett 581 (17), 3149-3156 (2007)
   PUBMED   17572408
  REMARK    GeneRIF: NECC 1 & 2 proteins primarily expressed in
            (neuro)endocrine tissues in vertebrates thus supporting a role for
            these proteins in the regulated secretory pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133436.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.73923.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..799
                     /product="janus kinase and microtubule-interacting protein
                     2 isoform 3"
                     /calculated_mol_wt=93562
     Region          19..>576
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          409..581
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          <476..>782
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..799
                     /gene="Jakmip2"
                     /gene_synonym="RGD1559742"
                     /coded_by="NM_001437327.1:725..3124"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:307479"
                     /db_xref="RGD:1559742"
ORIGIN      
        1 mskkgrnkge kpealivalq aanedlrtkl tdiqielhqe kskvsklere ktqeakrire
       61 leqrkhtvlv telkaklhee kmkelqavre nlikqheqem srtvkvrdge iqrlksalca
      121 lrdgssdkvr taltiearee arkqfdaerl kllqeitdlk takkqvdeal snmiqadkik
      181 agdlrsehqs hqeaiskikw eserdirrlm deikakdrii fslekeletq tgyvqklqlq
      241 kealdeqlfl vkeaecnmss pkreipgrag dgsehcsspd lrrnqkriae lnatirkled
      301 rntllgdern ellkrvrete kqckpllern kclakrndel mvslqrmeek lkaitkense
      361 mrekitshpp lkklkslndl dqaneeqete flklqvieqq niideltrdr eklirrrkhr
      421 rsskpikrpv ldpfigyded smdsetssmt sfrtdrtpat pdddldesla aeeselrfrq
      481 ltkeyqalqr ayallqeqtg giidaereak aqeqlqaevl ryrakiedle atlaqkgqie
      541 kqeaenhrlq qelqdardqn ellefrnlel eererrsppf nlqihpfsdg vsalqiycmk
      601 egvkdvnipd likqldilgd ngnlrneeqv aiiqastvls laekwiqqie gaeaalhqkm
      661 melesdmeqf ckikgyleee ldyrkqaldq aymriqelea tlynalqqet vikfgellsd
      721 kqqeelrtav eklrrqmlrk sreydcqilq ermellqqah qrirdledkt diqkrqikdl
      781 eekflflflf fslafilwp
//
LOCUS       NP_001423927             256 aa            linear   ROD 08-APR-2025
DEFINITION  protein YIPF7 [Rattus norvegicus].
ACCESSION   NP_001423927 XP_006251099
VERSION     NP_001423927.1
DBSOURCE    REFSEQ: accession NM_001436998.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 25, 2025 this sequence version replaced XP_006251099.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.34900.1,
                                           SRR26643295.48860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..256
                     /product="protein YIPF7"
                     /calculated_mol_wt=27760
     Region          <78..256
                     /region_name="YIP1"
                     /note="Rab GTPase interacting factor, Golgi membrane
                     protein [Intracellular trafficking and secretion];
                     cl46908"
                     /db_xref="CDD:481248"
     CDS             1..256
                     /gene="Yipf7"
                     /gene_synonym="RGD1310766"
                     /coded_by="NM_001436998.1:41..811"
                     /db_xref="GeneID:364147"
                     /db_xref="RGD:1310766"
ORIGIN      
        1 msnpeqydmd fyqsnyiidn qeqsyndsna ygnfygsrqp qareqcqpss pvppemflss
       61 dyggqlfqpa snlhyysqss svdsfdeepp lleelginfd hiwqktltvl npmkpadgsi
      121 mnetdltgpi lfcvalgatl lmagkaqfgy iygmsaigcf gihallnlms ssgvsygcva
      181 svlgycllpm vilsscavff slqgtagtms alliitwcsl saskifisal amegqqllva
      241 ypcallyglf alltvf
//
LOCUS       NP_001424194            1251 aa            linear   ROD 08-APR-2025
DEFINITION  phospholipid-transporting ATPase IC [Rattus norvegicus].
ACCESSION   NP_001424194 XP_006254904
VERSION     NP_001424194.1
DBSOURCE    REFSEQ: accession NM_001437265.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1251)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   2  (residues 1 to 1251)
  AUTHORS   Haas,M.J., Shah,G.N., Onstead-Haas,L.M. and Mooradian,A.D.
  TITLE     Identification of ATP8B1 as a blood-brain barrier-enriched protein
  JOURNAL   Cell Mol Neurobiol 34 (4), 473-478 (2014)
   PUBMED   24643366
  REMARK    GeneRIF: ATP8B1, a P-type aminophospholipid translocase, is
            enriched in cerebral microvessels and may have a role in plasma
            membrane lipid transport
REFERENCE   3  (residues 1 to 1251)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   4  (residues 1 to 1251)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   5  (residues 1 to 1251)
  AUTHORS   Ray,N.B., Durairaj,L., Chen,B.B., McVerry,B.J., Ryan,A.J.,
            Donahoe,M., Waltenbaugh,A.K., O'Donnell,C.P., Henderson,F.C.,
            Etscheidt,C.A., McCoy,D.M., Agassandian,M., Hayes-Rowan,E.C.,
            Coon,T.A., Butler,P.L., Gakhar,L., Mathur,S.N., Sieren,J.C.,
            Tyurina,Y.Y., Kagan,V.E., McLennan,G. and Mallampalli,R.K.
  TITLE     Dynamic regulation of cardiolipin by the lipid pump Atp8b1
            determines the severity of lung injury in experimental pneumonia
  JOURNAL   Nat Med 16 (10), 1120-1127 (2010)
   PUBMED   20852622
REFERENCE   6  (residues 1 to 1251)
  AUTHORS   Pawlikowska,L., Groen,A., Eppens,E.F., Kunne,C., Ottenhoff,R.,
            Looije,N., Knisely,A.S., Killeen,N.P., Bull,L.N., Elferink,R.P. and
            Freimer,N.B.
  TITLE     A mouse genetic model for familial cholestasis caused by ATP8B1
            mutations reveals perturbed bile salt homeostasis but no impairment
            in bile secretion
  JOURNAL   Hum Mol Genet 13 (8), 881-892 (2004)
   PUBMED   14976163
REFERENCE   7  (residues 1 to 1251)
  AUTHORS   Eppens,E.F., van Mil,S.W., de Vree,J.M., Mok,K.S., Juijn,J.A., Oude
            Elferink,R.P., Berger,R., Houwen,R.H. and Klomp,L.W.
  TITLE     FIC1, the protein affected in two forms of hereditary cholestasis,
            is localized in the cholangiocyte and the canalicular membrane of
            the hepatocyte
  JOURNAL   J Hepatol 35 (4), 436-443 (2001)
   PUBMED   11682026
REFERENCE   8  (residues 1 to 1251)
  AUTHORS   Ujhazy,P., Ortiz,D., Misra,S., Li,S., Moseley,J., Jones,H. and
            Arias,I.M.
  TITLE     Familial intrahepatic cholestasis 1: studies of localization and
            function
  JOURNAL   Hepatology 34 (4 Pt 1), 768-775 (2001)
   PUBMED   11584374
  REMARK    Erratum:[Hepatology 2002 Jan;35(1):246]
REFERENCE   9  (residues 1 to 1251)
  AUTHORS   Tygstrup,N., Steig,B.A., Juijn,J.A., Bull,L.N. and Houwen,R.H.
  TITLE     Recurrent familial intrahepatic cholestasis in the Faeroe Islands.
            Phenotypic heterogeneity but genetic homogeneity
  JOURNAL   Hepatology 29 (2), 506-508 (1999)
   PUBMED   9918928
REFERENCE   10 (residues 1 to 1251)
  AUTHORS   Bull,L.N., van Eijk,M.J., Pawlikowska,L., DeYoung,J.A., Juijn,J.A.,
            Liao,M., Klomp,L.W., Lomri,N., Berger,R., Scharschmidt,B.F.,
            Knisely,A.S., Houwen,R.H. and Freimer,N.B.
  TITLE     A gene encoding a P-type ATPase mutated in two forms of hereditary
            cholestasis
  JOURNAL   Nat Genet 18 (3), 219-224 (1998)
   PUBMED   9500542
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254904.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.63085.1,
                                           SRR26643297.50479.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1251
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..1251
                     /product="phospholipid-transporting ATPase IC"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IC;
                     ATPase, Class I, type 8B, member 1; ATPase,
                     aminophospholipid transporter, class I, type 8B, member 1;
                     P4-ATPase flippase complex alpha subunit ATP8B1"
                     /calculated_mol_wt=143704
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Region          94..1051
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            378
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            order(454..456,596,619..621,685,732..734,867,870,873,893,
                     896)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            953..973
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            983..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            1033..1053
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            1072..1092
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            1095..1115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     Site            1143..1163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AA47.2)"
     CDS             1..1251
                     /gene="Atp8b1"
                     /coded_by="NM_001437265.1:216..3971"
                     /db_xref="GeneID:291555"
                     /db_xref="RGD:1308488"
ORIGIN      
        1 mnterdsett fdedsqpnde vvpysddete deledqgpav epeqnrvnre vekkketfrk
       61 dctwqvkand rkfheqphfm ntkffcikes kyasnaikty kynaltflpm nlfeqfkraa
      121 nfyflillil qaipqistla wyttlvplll vlgitaikdl vddvarhkmd keinnrtcev
      181 ikdgrfkiik wkdiqvgdvi rlkkndfipa dilllsssep nslcyvetae ldgetnlkfk
      241 maleitdqyl qiednlatfd gfieceepnn rldkftgtlf wrnqsfplda dkillrgcvi
      301 rntdvchglv ifagadtkim knsgktrfkr tkidylmnym vytiiivlil vsaglaigha
      361 yweaqignys wylydgenat psyrgflnfw gyiivlntmv pislyvsvev irlgqshfin
      421 wdlqmyyaek dtpaksrttt lneqlgqihy ifsdktgtlt qnimtfkkcc ingtiygdhr
      481 dasqhshski elvdfswnef adgklafydh ylieqiqsgk epevrqfffl lsichtvmvd
      541 ridgqinyqa aspdegalvn aarnfgfafl artqntitvs elgtertysv laildfnsdr
      601 krmsiivrtp egsirlyckg adtviyerlh rmnpmkqetq daldifaset lrtlclcyke
      661 ieekefaewn kkfmaasvas snrdealdkv yeeierdlil lgataiedkl qdgvpetisk
      721 lakadikiwv ltgdkketae nigfacellt edtticyged insllhtrme nqrnrggvsa
      781 kfappayepf fppgenrali itgswlneil lekktkrski lklkfprtee errmrsqsrr
      841 rleekkeqrq knfvdlacec saviccrvtp kqkamvvdlv krykkaitla igdgandvnm
      901 iktahigvgi sgqegmqavm ssdysfaqfr ylqrlllvhg rwsyirmckf lryffyknfa
      961 ftlvhfwysf fngysaqtay edwfitlynv lysslpvllm glldqdvsdk lslrfpglyv
     1021 vgqrdllfny kkffvsllhg vltsmvlffi pfgaylqtvg qdgeapsdyq sfavtmasal
     1081 vitvnfqigl dtsywtfvna fsifgsialy fgimfdfhsa gihvlfpsaf qftgtasnal
     1141 rqpyiwltii ltvavcllpv vairflsmti wpsesdkiqk hrkrlkaeeq wkrrqsvfrr
     1201 gassrrsaya fshqrgyadl issgrsirkk rspldaiiad gtaeyrrtve s
//
LOCUS       NP_001424473             243 aa            linear   ROD 08-APR-2025
DEFINITION  tumor protein D55 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424473 XP_006231322
VERSION     NP_001424473.1
DBSOURCE    REFSEQ: accession NM_001437544.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006231322.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.860937.1, CR463267.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..243
                     /product="tumor protein D55 isoform 2"
                     /note="tumor protein D55; tumor protein D55-like; tumor
                     protein D52-like 3"
                     /calculated_mol_wt=26240
     Region          78..176
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..243
                     /gene="Tpd52l3"
                     /gene_synonym="RGD1309391; Trpd52l3"
                     /coded_by="NM_001437544.1:91..822"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293894"
                     /db_xref="RGD:1309391"
ORIGIN      
        1 mdpshleshp sgqksepagl dvsstspncf ssnqgldsvy qeldldslne dlslsvsdam
       61 tetsastnef hlasepdlte aeqmelrsel tkleeeilsl rdllaakekr cgelkrklgc
      121 valvglrqnl skswhdvqas ntymkqktst alasmgsaic rklgdmkkss tfksleelvg
      181 tvksrvaggr elgsgllpsp asgsdphsvl gsgyetvsgl ddqlfsllkp detkyccqyr
      241 rsr
//
LOCUS       NP_599198               1104 aa            linear   ROD 08-APR-2025
DEFINITION  transient receptor potential cation channel subfamily M member 8
            [Rattus norvegicus].
ACCESSION   NP_599198
VERSION     NP_599198.2
DBSOURCE    REFSEQ: accession NM_134371.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Kozyreva,T.V., Orlov,I.V., Boyarskaya,A.R. and Voronova,I.P.
  TITLE     Hypothalamic TRPM8 and TRPA1 ion channel genes in the regulation of
            temperature homeostasis at water balance changes
  JOURNAL   Neurosci Lett 828, 137763 (2024)
   PUBMED   38574849
  REMARK    GeneRIF: Hypothalamic TRPM8 and TRPA1 ion channel genes in the
            regulation of temperature homeostasis at water balance changes.
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Skagen,C., Lovsletten,N.G., Asoawe,L., Al-Karbawi,Z., Rustan,A.C.,
            Thoresen,G.H. and Haugen,F.
  TITLE     Functional expression of the thermally activated transient receptor
            potential channels TRPA1 and TRPM8 in human myotubes
  JOURNAL   J Therm Biol 116, 103623 (2023)
   PUBMED   37542841
  REMARK    GeneRIF: Functional expression of the thermally activated transient
            receptor potential channels TRPA1 and TRPM8 in human myotubes.
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Chakraborty,R. and Goswami,C.
  TITLE     Both heat-sensitive TRPV4 and cold-sensitive TRPM8 ion channels
            regulate microglial activity
  JOURNAL   Biochem Biophys Res Commun 611, 132-139 (2022)
   PUBMED   35489198
  REMARK    GeneRIF: Both heat-sensitive TRPV4 and cold-sensitive TRPM8 ion
            channels regulate microglial activity.
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Huang,Y., Li,S., Jia,Z., Li,S., He,W., Zhou,C., Zhang,R., Xu,R.,
            Sun,B., Ali,D.W., Michalak,M., Chen,X.Z. and Tang,J.
  TITLE     TRIM4 interacts with TRPM8 and regulates its channel function
            through K423-mediated ubiquitination
  JOURNAL   J Cell Physiol 236 (4), 2934-2949 (2021)
   PUBMED   33037615
  REMARK    GeneRIF: TRIM4 interacts with TRPM8 and regulates its channel
            function through K423-mediated ubiquitination.
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Lai,H., Liu,C., Hou,L., Lin,W., Chen,T. and Hong,A.
  TITLE     TRPM8-regulated calcium mobilization plays a critical role in
            synergistic chemosensitization of Borneol on Doxorubicin
  JOURNAL   Theranostics 10 (22), 10154-10170 (2020)
   PUBMED   32929340
  REMARK    GeneRIF: TRPM8-regulated calcium mobilization plays a critical role
            in synergistic chemosensitization of Borneol on Doxorubicin.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Hu,H.Z., Gu,Q., Wang,C., Colton,C.K., Tang,J., Kinoshita-Kawada,M.,
            Lee,L.Y., Wood,J.D. and Zhu,M.X.
  TITLE     2-aminoethoxydiphenyl borate is a common activator of TRPV1, TRPV2,
            and TRPV3
  JOURNAL   J Biol Chem 279 (34), 35741-35748 (2004)
   PUBMED   15194687
REFERENCE   7  (residues 1 to 1104)
  AUTHORS   Nealen,M.L., Gold,M.S., Thut,P.D. and Caterina,M.J.
  TITLE     TRPM8 mRNA is expressed in a subset of cold-responsive trigeminal
            neurons from rat
  JOURNAL   J Neurophysiol 90 (1), 515-520 (2003)
   PUBMED   12634279
  REMARK    GeneRIF: TRPM8 is preferentially expressed within a subset of
            rapidly responsive, low-threshold (approximately 30 degrees C),
            cold-sensitive neurons in trigeminal ganglia.
REFERENCE   8  (residues 1 to 1104)
  AUTHORS   Story,G.M., Peier,A.M., Reeve,A.J., Eid,S.R., Mosbacher,J.,
            Hricik,T.R., Earley,T.J., Hergarden,A.C., Andersson,D.A.,
            Hwang,S.W., McIntyre,P., Jegla,T., Bevan,S. and Patapoutian,A.
  TITLE     ANKTM1, a TRP-like channel expressed in nociceptive neurons, is
            activated by cold temperatures
  JOURNAL   Cell 112 (6), 819-829 (2003)
   PUBMED   12654248
REFERENCE   9  (residues 1 to 1104)
  AUTHORS   Peier,A.M., Moqrich,A., Hergarden,A.C., Reeve,A.J., Andersson,D.A.,
            Story,G.M., Earley,T.J., Dragoni,I., McIntyre,P., Bevan,S. and
            Patapoutian,A.
  TITLE     A TRP channel that senses cold stimuli and menthol
  JOURNAL   Cell 108 (5), 705-715 (2002)
   PUBMED   11893340
REFERENCE   10 (residues 1 to 1104)
  AUTHORS   McKemy,D.D., Neuhausser,W.M. and Julius,D.
  TITLE     Identification of a cold receptor reveals a general role for TRP
            channels in thermosensation
  JOURNAL   Nature 416 (6876), 52-58 (2002)
   PUBMED   11882888
  REMARK    GeneRIF: CMR1 is a member of the TRP family of excitatory ion
            channels and is proposed to function as a transducer of cold
            stimuli in the somatosensory system
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Sep 30, 2004 this sequence version replaced NP_599198.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY072788.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..1104
                     /product="transient receptor potential cation channel
                     subfamily M member 8"
                     /note="cold menthol receptor 1"
                     /calculated_mol_wt=127498
     Region          116..359
                     /region_name="LSDAT_euk"
                     /note="SLOG in TRPM; cl39032"
                     /db_xref="CDD:476852"
     Region          <657..1005
                     /region_name="TRPV"
                     /note="Transient Receptor Potential channel, Vanilloid
                     subfamily (TRPV); cl40437"
                     /db_xref="CDD:454755"
     Site            734..758
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     Site            766..789
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     Site            797..817
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     Site            823..848
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     Site            854..890
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     Site            954..984
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R455.4)"
     CDS             1..1104
                     /gene="Trpm8"
                     /gene_synonym="CMR1"
                     /coded_by="NM_134371.3:39..3353"
                     /db_xref="GeneID:171384"
                     /db_xref="RGD:620762"
ORIGIN      
        1 msfegarlsm rsrrngtlgs trtlyssvsr stdvsysesd lvnfiqanfk krecvfftrd
       61 skamesickc gyaqsqhieg tqinqnekwn ykkhtkefpt dafgdiqfet lgkkgkylrl
      121 scdtdsetly elltqhwhlk tpnlvisvtg gaknfalkpr mrkifsrliy iaqskgawil
      181 tggthyglmk yigevvrdnt isrnseeniv aigiaawgmv snrdtlirnc ddeghfsaqy
      241 imddfmrdpl yildnnhthl llvdngchgh ptveaklrnq lekyiserts qdsnyggkip
      301 ivcfaqgggr etlkaintsv kskipcvvve gsgqiadvia slvevedvlt ssmvkeklvr
      361 flprtvsrlp eeeieswikw lkeilesphl ltvikmeeag devvssaisy alykafstne
      421 qdkdnwngql klllewnqld lasdeiftnd rrwesadlqe vmftalikdr pkfvrlflen
      481 glnlqkfltn evltelfsth fstlvyrnlq iaknsyndal ltfvwklvan frrsfwkedr
      541 ssredldvel hdaslttrhp lqalfiwail qnkkelskvi weqtkgctla algaskllkt
      601 lakvkndina ageseelane yetravelft ecyssdedla eqllvyscea wggsnclela
      661 veatdqhfia qpgvqnflsk qwygeisrdt knwkiilclf iiplvgcglv sfrkkpidkh
      721 kkllwyyvaf ftspfvvfsw nvvfyiafll lfayvllmdf hsvphtpeli lyalvfvlfc
      781 devrqwymng vnyftdlwnv mdtlglfyfi agivfrlhss nksslysgrv ifcldyiift
      841 lrlihiftvs rnlgpkiiml qrmlidvfff lflfavwmva fgvarqgilr qneqrwrwif
      901 rsviyepyla mfgqvpsdvd sttydfshct fsgneskplc veldeynlpr fpewitiplv
      961 ciymlstnil lvnllvamfg ytvgivqenn dqvwkfqryf lvqeycnrln ipfpfvvfay
     1021 fymvvkkcfk ccckekntes saccfrnedn etlawegvmk enylvkintk andnaeemrh
     1081 rfrqldtkln dlkgllkeia nkik
//
LOCUS       NP_001424444             688 aa            linear   ROD 08-APR-2025
DEFINITION  band 4.1-like protein 4A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424444 XP_006254646
VERSION     NP_001424444.1
DBSOURCE    REFSEQ: accession NM_001437515.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254646.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.62221.1,
                                           SRR26643297.49650.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..688
                     /product="band 4.1-like protein 4A isoform 1"
                     /note="erythrocyte protein band 4.1-like 4a; band 4.1-like
                     protein 4A"
                     /calculated_mol_wt=78652
     Region          13..211
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          207..296
                     /region_name="FERM_C_NBL4_NBL5"
                     /note="FERM domain C-lobe of Novel band 4.1-like protein 4
                     and 5 (NBL4 and 5); cd13186"
                     /db_xref="CDD:270007"
     Site            order(215,232,234,240)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270007"
     Site            order(244,249..252,285,289,292..293)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Site            285..296
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270007"
     Region          311..355
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     CDS             1..688
                     /gene="Epb41l4a"
                     /gene_synonym="Epb4.1l4a"
                     /coded_by="NM_001437515.1:723..2789"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:307514"
                     /db_xref="RGD:1306034"
ORIGIN      
        1 mgcfcavpee fycevlllde skltlttqhq gikkstkgsv vldhvfrhvn lveidyfglr
       61 ycdrshqtyw ldpaktlaeh kelintgppy tlyfgikfya edpcklkeei tryqfflqvk
      121 qdalqgrlpc pvniaaqlga yaiqaelgdh dpckhtagyv seyrfvpdqk eeleesieri
      181 hktlmgqaps eaelnylrta kslemygvdl hpvygenkse yflgltpvgv vvyknkkqvg
      241 kyfwpritkv hfketqfelr vlgkdcnets fffearskta ckhlwkcsve hhtffrmpet
      301 esnslsrkls kfgsisykhr ysgrtalqms rdlsiqlprp nqnvvrsrsk typkrvaqtq
      361 pagsnsinrm tanlengene gttkiiapsp vksfkkakne nspdpqrsks hapweengpq
      421 sglynspsdr tkspkfpctr qrnlscgsdn dssqpmrrrk ahhsgedsdl kqrrrsrsrc
      481 ntssgsesen snrehrkkrn rirqendmvd sapqweavlr rqkeknqvdp nnrrsrhrsr
      541 srspdiqake elwkhiqkel vdpsglseeq lkeipytkve tqgdpvrirh shsprsyrqy
      601 rrsqcsdger svlsevnskt dlvpplpvtr ssdaqgsggs tvhqrrngsk dslieeksql
      661 sttnlagkht aktiktiqaa rlktdvtg
//
LOCUS       NP_001423965             467 aa            linear   ROD 08-APR-2025
DEFINITION  tRNA dimethylallyltransferase [Rattus norvegicus].
ACCESSION   NP_001423965
VERSION     NP_001423965.1
DBSOURCE    REFSEQ: accession NM_001437036.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Yarham,J.W., Lamichhane,T.N., Pyle,A., Mattijssen,S., Baruffini,E.,
            Bruni,F., Donnini,C., Vassilev,A., He,L., Blakely,E.L., Griffin,H.,
            Santibanez-Koref,M., Bindoff,L.A., Ferrero,I., Chinnery,P.F.,
            McFarland,R., Maraia,R.J. and Taylor,R.W.
  TITLE     Defective i6A37 modification of mitochondrial and cytosolic tRNAs
            results from pathogenic mutations in TRIT1 and its substrate tRNA
  JOURNAL   PLoS Genet 10 (6), e1004424 (2014)
   PUBMED   24901367
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.23578.1,
                                           SRR26643298.28774.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..467
                     /product="tRNA dimethylallyltransferase"
                     /EC_number="2.5.1.75"
                     /note="tRNA dimethylallyltransferase, mitochondrial"
                     /calculated_mol_wt=52175
     Region          24..373
                     /region_name="MiaA"
                     /note="tRNA A37 N6-isopentenylltransferase MiaA
                     [Translation, ribosomal structure and biogenesis];
                     COG0324"
                     /db_xref="CDD:440093"
     Region          395..419
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     CDS             1..467
                     /gene="Trit1"
                     /coded_by="NM_001437036.1:14..1417"
                     /db_xref="GeneID:362586"
                     /db_xref="RGD:1304781"
ORIGIN      
        1 maaaaaarav pvssgfrglp rtlplvvilg atgtgkstla lqlgqrlgge ivsadsmqvy
       61 egldiitnkv saqeqkmcrh hmisfvdplv tsytvvdfrn rataliedif ardkipivvg
      121 gtnyyiesll wkvlvttkpq gmgtgkavdr kvelekedgh elhkrlsqvd pemaaklhph
      181 dkrkvarslq vfeetgvshs eflhrqhaee gggplggplk fpnpcilwlh adqavlderl
      241 dkrvddmlaa glleelrdfh rrynlknvse dsqdyqhgif qsigfkefhe ylttegkctp
      301 etsnqllkkg vealkqvtkr yarkqnrwvr nrflsrpgps vppvyglevs dvskweefvl
      361 epalsivqsf iqgskptatp vkipyseten krsyhmcdlc driiigdrew aahtkskshl
      421 hqlkkrrkld ldavsalgsq snspdseler kegessgqrd qelkasv
//
LOCUS       NP_001102331             256 aa            linear   ROD 08-APR-2025
DEFINITION  protein YIPF7 [Rattus norvegicus].
ACCESSION   NP_001102331 XP_001077453 XP_344237
VERSION     NP_001102331.1
DBSOURCE    REFSEQ: accession NM_001108861.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_344237.1, XP_001077453.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM118826.1, SRR26643296.33034.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..256
                     /product="protein YIPF7"
                     /calculated_mol_wt=27760
     Region          <78..256
                     /region_name="YIP1"
                     /note="Rab GTPase interacting factor, Golgi membrane
                     protein [Intracellular trafficking and secretion];
                     cl46908"
                     /db_xref="CDD:481248"
     CDS             1..256
                     /gene="Yipf7"
                     /gene_synonym="RGD1310766"
                     /coded_by="NM_001108861.2:45..815"
                     /db_xref="GeneID:364147"
                     /db_xref="RGD:1310766"
ORIGIN      
        1 msnpeqydmd fyqsnyiidn qeqsyndsna ygnfygsrqp qareqcqpss pvppemflss
       61 dyggqlfqpa snlhyysqss svdsfdeepp lleelginfd hiwqktltvl npmkpadgsi
      121 mnetdltgpi lfcvalgatl lmagkaqfgy iygmsaigcf gihallnlms ssgvsygcva
      181 svlgycllpm vilsscavff slqgtagtms alliitwcsl saskifisal amegqqllva
      241 ypcallyglf alltvf
//
LOCUS       NP_571982                919 aa            linear   ROD 08-APR-2025
DEFINITION  calcium-transporting ATPase type 2C member 1 [Rattus norvegicus].
ACCESSION   NP_571982
VERSION     NP_571982.2
DBSOURCE    REFSEQ: accession NM_131907.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Tang,J., Wang,R., Fan,Y., Zhang,C. and Kong,Y.
  TITLE     Ultrashort wave alleviates oxygen-glucose deprivation/reoxygenation
            injury via up-regulation of SPCA1 expression in N2a cells
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (5), 641-647 (2023)
   PUBMED   37539566
  REMARK    GeneRIF: Ultrashort wave alleviates oxygen-glucose
            deprivation/reoxygenation injury via up-regulation of SPCA1
            expression in N2a cells.
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Fan,Y., Zhang,C., Li,T., Peng,W., Yin,J., Li,X., Kong,Y., Lan,C.,
            Wang,R. and Hu,Z.
  TITLE     A New Approach of Short Wave Protection against Middle Cerebral
            Artery Occlusion/Reperfusion Injury via Attenuation of Golgi
            Apparatus Stress by Inhibition of Downregulation of Secretory
            Pathway Ca(2+)-ATPase Isoform 1 in Rats
  JOURNAL   J Stroke Cerebrovasc Dis 25 (7), 1813-1822 (2016)
   PUBMED   27133772
  REMARK    GeneRIF: Short wave therapy protected against focal cerebral I/R
            injury by increasing SPCA1 expression to modulate Golgi apparatus
            stress.
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Cross,B.M., Hack,A., Reinhardt,T.A. and Rao,R.
  TITLE     SPCA2 regulates Orai1 trafficking and store independent Ca2+ entry
            in a model of lactation
  JOURNAL   PLoS One 8 (6), e67348 (2013)
   PUBMED   23840669
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Leitch,S., Feng,M., Muend,S., Braiterman,L.T., Hubbard,A.L. and
            Rao,R.
  TITLE     Vesicular distribution of Secretory Pathway Ca(2)+-ATPase isoform 1
            and a role in manganese detoxification in liver-derived polarized
            cells
  JOURNAL   Biometals 24 (1), 159-170 (2011)
   PUBMED   20981470
  REMARK    GeneRIF: The secretory pathway Ca(2+)-ATPase isoform 1 (SPCA1) was
            expressed in liver and WIF-B cells.
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Fairclough,R.J., Dode,L., Vanoevelen,J., Andersen,J.P.,
            Missiaen,L., Raeymaekers,L., Wuytack,F. and Hovnanian,A.
  TITLE     Effect of Hailey-Hailey Disease mutations on the function of a new
            variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1)
  JOURNAL   J Biol Chem 278 (27), 24721-24730 (2003)
   PUBMED   12707275
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Ton,V.K., Mandal,D., Vahadji,C. and Rao,R.
  TITLE     Functional expression in yeast of the human secretory pathway
            Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease
  JOURNAL   J Biol Chem 277 (8), 6422-6427 (2002)
   PUBMED   11741891
REFERENCE   8  (residues 1 to 919)
  AUTHORS   Pruitt,K.D. and Maglott,D.R.
  TITLE     RefSeq and LocusLink: NCBI gene-centered resources
  JOURNAL   Nucleic Acids Res 29 (1), 137-140 (2001)
   PUBMED   11125071
REFERENCE   9  (residues 1 to 919)
  AUTHORS   Hu,Z., Bonifas,J.M., Beech,J., Bench,G., Shigihara,T., Ogawa,H.,
            Ikeda,S., Mauro,T. and Epstein,E.H. Jr.
  TITLE     Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey
            disease
  JOURNAL   Nat Genet 24 (1), 61-65 (2000)
   PUBMED   10615129
REFERENCE   10 (residues 1 to 919)
  AUTHORS   Gunteski-Hamblin,A.M., Clarke,D.M. and Shull,G.E.
  TITLE     Molecular cloning and tissue distribution of alternatively spliced
            mRNAs encoding possible mammalian homologues of the yeast secretory
            pathway calcium pump
  JOURNAL   Biochemistry 31 (33), 7600-7608 (1992)
   PUBMED   1380825
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086994.1.
            
            On Dec 26, 2004 this sequence version replaced NP_571982.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086994.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..919
                     /product="calcium-transporting ATPase type 2C member 1"
                     /EC_number="7.2.2.10"
                     /note="calcium-transporting ATPase 2C1; ATP-dependent
                     Ca(2+) pump PMR1; ATPase, Ca++-sequestering; secretory
                     pathway Ca(2+)-ATPase 1; ATPase, Ca++ transporting, type
                     2C, member 1; Ca(2+)/Mn(2+)-ATPase 2C1; secretory pathway
                     Ca(2+)-transporting ATPase type 1"
                     /calculated_mol_wt=100374
     Region          54..896
                     /region_name="P-type_ATPase_SPCA"
                     /note="golgi-associated secretory pathway Ca(2+) transport
                     ATPases, similar to human ATPase secretory pathway Ca(2+)
                     transporting 1/hSPCA1 and Saccharomyces cerevisiae
                     Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; cd02085"
                     /db_xref="CDD:319779"
     Site            79..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            100..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            264..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            296..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            order(350..352,454,480..482,525,570..572,619,622,625,644,
                     647)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319779"
     Site            701..723
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            order(705,709..710,712..713,738,741..742)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319779"
     Site            729..752
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            777..795
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            803..828
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            844..863
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     Site            877..893
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64566.1)"
     CDS             1..919
                     /gene="Atp2c1"
                     /gene_synonym="Spca1"
                     /coded_by="NM_131907.2:468..3227"
                     /db_xref="GeneID:170699"
                     /db_xref="RGD:621311"
ORIGIN      
        1 mkvarfqkip nvenetmipv ltskrasela vsevagllqa dlqnglnkse vshrrafhgw
       61 nefdisedep lwkkyisqfk nplimlllas avisvlmrqf ddavsitvai livvtvafvq
      121 eyrsekslee lsklvppech cvregkleht lardlvpgdt vclsvgdrvp adlrlfeavd
      181 lsidessltg ettpcskvta pqpaatngdl asrsniafmg tlvrcgkakg ivigtgense
      241 fgevfkmmqa eeapktplqk smdllgkqls fysfgiigii mlvgwllgkd ilemftisvs
      301 lavaaipegl pivvtvtlal gvmrmvkkra ivkklpivet lgccnvicsd ktgtltknem
      361 tvthiltsdg lhaevtgvgy nqfgevivdg dvvhgfynpa vsriveagcv cndavirnnt
      421 lmgkptegal ialamkmgld glqqdyirka eypfsseqkw mavkcvhrtq qdrpeicfmk
      481 gayeqvikyc ttynskgqtl altqqqrdly qqekaqmgsa glrvlalasg pdlgqltflg
      541 lvgiidpprt gvkeavttli asgvsikmit gdsqetaiai asrlglyskt sqsvsgeevd
      601 tmevqhlsqi vpkvavfyra sprhkmkiik slqkngsvva mtgdgvndav alkaadigva
      661 mgqtgtdvck eaadmilvdd dfqtimsaie egkgiynnik nfvrfqlsts iaaltlisla
      721 tlmnfpnpln amqilwinii mdgppaqslg vepvdkdvir kpprnwkdsi ltknlilkil
      781 vssiiivcgt lfvfwrelrd nvitprdttm tftcfvffdm fnalssrsqt ksvfeiglcs
      841 nkmfcyavlg simgqllviy fpplqkvfqt eslsildllf llgltssvci vseiikkver
      901 srektqknat stpssflev
//
LOCUS       NP_072125                238 aa            linear   ROD 08-APR-2025
DEFINITION  fibroblast growth factor-binding protein 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_072125 XP_006251140
VERSION     NP_072125.2
DBSOURCE    REFSEQ: accession NM_022603.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Zhu,H.Y., Bai,W.D., Liu,J.Q., Zheng,Z., Guan,H., Zhou,Q., Su,L.L.,
            Xie,S.T., Wang,Y.C., Li,J., Li,N., Zhang,Y.J., Wang,H.T. and
            Hu,D.H.
  TITLE     Up-regulation of FGFBP1 signaling contributes to miR-146a-induced
            angiogenesis in human umbilical vein endothelial cells
  JOURNAL   Sci Rep 6, 25272 (2016)
   PUBMED   27121396
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Yamanaka,Y., Kitano,A., Takao,K., Prasansuklab,A., Mushiroda,T.,
            Yamazaki,K., Kumada,T., Shibata,M., Takaoka,Y., Awaya,T., Kato,T.,
            Abe,T., Iwata,N., Miyakawa,T., Nakamura,Y., Nakahata,T. and
            Heike,T.
  TITLE     Inactivation of fibroblast growth factor binding protein 3 causes
            anxiety-related behaviors
  JOURNAL   Mol Cell Neurosci 46 (1), 200-212 (2011)
   PUBMED   20851768
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Tassi,E., Walter,S., Aigner,A., Cabal-Manzano,R.H., Ray,R.,
            Reier,P.J. and Wellstein,A.
  TITLE     Effects on neurite outgrowth and cell survival of a secreted
            fibroblast growth factor binding protein upregulated during spinal
            cord injury
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 293 (2), R775-R783 (2007)
   PUBMED   17553847
  REMARK    GeneRIF: FGF-BP is an early response gene after spinal cord injury
            and that its upregulation in regenerating spinal cord tissue may
            provide a molecular mechanism for enhancing the initial
            FGF2-mediated neurotrophic effects occurring after such tissue
            damage
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Beer,H.D., Bittner,M., Niklaus,G., Munding,C., Max,N., Goppelt,A.
            and Werner,S.
  TITLE     The fibroblast growth factor binding protein is a novel interaction
            partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity:
            implications for epithelial repair
  JOURNAL   Oncogene 24 (34), 5269-5277 (2005)
   PUBMED   15806171
REFERENCE   5  (residues 1 to 238)
  AUTHORS   West,D.C., Rees,C.G., Duchesne,L., Patey,S.J., Terry,C.J.,
            Turnbull,J.E., Delehedde,M., Heegaard,C.W., Allain,F.,
            Vanpouille,C., Ron,D. and Fernig,D.G.
  TITLE     Interactions of multiple heparin binding growth factors with
            neuropilin-1 and potentiation of the activity of fibroblast growth
            factor-2
  JOURNAL   J Biol Chem 280 (14), 13457-13464 (2005)
   PUBMED   15695515
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Aigner,A., Malerczyk,C., Houghtling,R. and Wellstein,A.
  TITLE     Tissue distribution and retinoid-mediated downregulation of an
            FGF-binding protein (FGF-BP) in the rat
  JOURNAL   Growth Factors 18 (1), 51-62 (2000)
   PUBMED   10831072
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Mar 26, 2025 this sequence version replaced
            XP_006251140.1, NP_072125.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.30460.1,
                                           SRR26643295.49069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423, SAMN06680439
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..238
                     /product="fibroblast growth factor-binding protein 1
                     precursor"
                     /note="FGF-BP; FGF-BP1; FGFBP-1; FGF-binding protein 1;
                     growth factor-binding protein 1"
                     /calculated_mol_wt=24668
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2239
     Region          15..234
                     /region_name="FGF-BP1"
                     /note="FGF binding protein 1 (FGF-BP1); pfam06473"
                     /db_xref="CDD:461927"
     mat_peptide     21..238
                     /product="Fibroblast growth factor-binding protein 1.
                     /id=PRO_0000245514"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY10.1)"
                     /calculated_mol_wt=24668
     Region          25..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY10.1)"
     Site            164
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9QY10.1)"
     Region          197..238
                     /region_name="Sufficient for interaction with FGF2 and
                     FGF2-induced effects. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY10.1)"
     CDS             1..238
                     /gene="Fgfbp1"
                     /coded_by="NM_022603.3:76..792"
                     /db_xref="GeneID:64535"
                     /db_xref="RGD:621211"
ORIGIN      
        1 mrihslills flllaaqvls ekvrktaknv pdstteedms pslgkarnkq rsrtsksmth
       61 gkfvtkdqat crwavteeel ginlkvqctr adqefscvfa gdptgclkyd kdqtywkqva
      121 rtlrkqknic ensksvlktr vcrkkfpesn lkvvnprkek aevsprehnk vqeavsmepn
      181 kvkvdittsp aatvavkdse cledpdvltq rktalefcge swssfctffl nmlqatsc
//
LOCUS       NP_001424233            2114 aa            linear   ROD 08-APR-2025
DEFINITION  unconventional myosin-VIIb [Rattus norvegicus].
ACCESSION   NP_001424233 XP_006254662
VERSION     NP_001424233.1
DBSOURCE    REFSEQ: accession NM_001437304.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2114)
  AUTHORS   Crawley,S.W., Shifrin,D.A. Jr., Grega-Larson,N.E., McConnell,R.E.,
            Benesh,A.E., Mao,S., Zheng,Y., Zheng,Q.Y., Nam,K.T., Millis,B.A.,
            Kachar,B. and Tyska,M.J.
  TITLE     Intestinal brush border assembly driven by protocadherin-based
            intermicrovillar adhesion
  JOURNAL   Cell 157 (2), 433-446 (2014)
   PUBMED   24725409
REFERENCE   2  (residues 1 to 2114)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254662.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.58999.1,
                                           SRR26643291.40217.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2114
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..2114
                     /product="unconventional myosin-VIIb"
                     /calculated_mol_wt=241170
     Region          79..750
                     /region_name="MYSc_Myo7"
                     /note="class VII myosin, motor domain; cd01381"
                     /db_xref="CDD:276832"
     Site            order(106..114,158..165,202..212,437..442)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276832"
     Site            106..114
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276832"
     Site            158..165
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276832"
     Site            202..212
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276832"
     Site            437..442
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276832"
     Site            466..489
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276832"
     Site            681..690
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276832"
     Site            order(693..718,738..750)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276832"
     Region          787..809
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          857..877
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          991..1194
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1198..1296
                     /region_name="FERM1_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 1, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17092"
                     /db_xref="CDD:340612"
     Region          1201..1414
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            order(1248..1253,1258,1266,1288)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340612"
     Region          1408..1504
                     /region_name="FERM_C1_MyoVII"
                     /note="FERM domain C-lobe, repeat 1, of Myosin VII
                     (MyoVII/Myo7); cd13198"
                     /db_xref="CDD:270019"
     Site            order(1408..1409,1413,1415,1430,1445)
                     /site_type="other"
                     /note="CEN1 peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270019"
     Site            order(1418,1440,1442,1449)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270019"
     Site            1491..1502
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270019"
     Region          1505..1565
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(1512,1516,1522,1544..1545,1560,1562..1563)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1646..1793
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1800..1897
                     /region_name="FERM2_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 2, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17093"
                     /db_xref="CDD:340613"
     Region          1802..2014
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          2010..2105
                     /region_name="FERM_C2_MyoVII"
                     /note="FERM domain C-lobe, repeat 2, of Myosin VII
                     (MyoVII, Myo7); cd13199"
                     /db_xref="CDD:270020"
     Site            order(2018,2039,2041,2047)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270020"
     Site            order(2051,2055..2058,2093,2097,2100..2101)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     Site            2093..2104
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     CDS             1..2114
                     /gene="Myo7b"
                     /gene_synonym="RGD1561153"
                     /coded_by="NM_001437304.1:139..6483"
                     /db_xref="GeneID:498834"
                     /db_xref="RGD:1561153"
ORIGIN      
        1 msvfrlgdhv wldppssnkt gvaiggivke tklgktlied degkehwisa edlstlrpmh
       61 pnsaqgvddm irlgdlneag vvhnlliryq qhkiytytgs ilvavnpfqm lplytleqvq
      121 iyysrhmgel pphvfaians cyfnmkknkr dqcciisges gagktettkl ilqflatvsg
      181 qhswieqqvl eanpileafg naktirndns srfgkyidih fnssgviega siehflleks
      241 rvcrqaaeer nyhifycmlm gmsleeknml glgmpseyhy ltmgnctsye glsdakdyah
      301 vrsamkilqf sdsenwdisk llaailhlgn vgfmaavfen ldssdvmetp afpfamklle
      361 vqhqalrdcl ikhtipilge fvsrplniaq aadrrdafvk giyghlflwi vkkinaaift
      421 pqaqdpqnvr raiglldifg fenfqnnsfe qlcinfaneh lqqffvkhvf tmeqeeylse
      481 nitwnyihyt dnqpildmla lkpmsiisll deesrfpqgt dvtmlqklns ihannksflr
      541 pksihdtrfg iahfagdvyy qaegfleknr dvlstdilil ihssknkflk eifnldlpqt
      601 klghgticqv ktktggqifk psdstkrsvt lssqfkqsle qlmkiltncq pyfvrcikpn
      661 eykkpllfdr elciqqlrys gmmetvhirk sgfpirytfd efsqrfrvll pspervqfqn
      721 khrqmtsria dlclgtdkew kmgktkiflk dhqdtmleiq rsqaldgaai riqrvlrghk
      781 yrkeflrqkr aavtlqavwr ghnqrknfkl ilmgferlqa iarshllmrq fqtmrqkivq
      841 lqarcrgylv rqqvqakrra vviiqaharg mvarksywqq kssgppvila kepkgqgval
      901 drkrksiydt vtdtamvekv fgflpamigg qegpaptrfe dlevktqklh evdldtvpmt
      961 empgedvdgl aeytfpkfav tyfqksasht hiqkplrypl lyhendtdhs aalavwiiil
     1021 rfmgdlpepq aygrssltgs svmrqihdrl dkdsvtqgpq hnrstqvasq qnigeevfkf
     1081 dgpisdrpms nlekvhfivg yaimrpglrd eiycqickql senyktssra rgwillslcl
     1141 gcfppserfm kyllnfisqg pasygpfcae rlqrtfangv raepptwlel qavkskkhip
     1201 iqvilatgrs ltisvdsast sreicqqiaq kqglrdklgf slqvavydkf wslgnscdhv
     1261 mdavaqceql awergesqrq apwriyfrke fftpwhdsre dpvsteliyh qvlrgvwsge
     1321 ynfekeedlv ellarhcyvq lgatvksnav qellpscvps klyrtkspek waslviaaha
     1381 kapytqskat plevkeqtve aarllwpllf srlfevttls gprlpktqli lainwkgmyf
     1441 ldqkertllg lsfaevmgli anrdapggks lllstlheey efaspssvai aemvalflag
     1501 lkersvfama lqdrkatddv tllpfkkgdl liltkkqgll asenwvlgqn drtgktglvp
     1561 taclytipsv tkpsaqllnl lamspekrkl aaqevqasep pleeqltelp ytleefsyqy
     1621 frapeketis raampmarsr ghlwayspep lrqpllksvh dkaklrdsac qiflailkyt
     1681 gdypsrqswh sleltdqmfs lalkepalqd elycqilkql thnsirfsee rawqllwlct
     1741 glfppgkall phaqkfidsr kkkplaldcs rrlhrilrvg prkqpphhve vkaaeqnvsk
     1801 lhhevylpnd tnktlevsss srvrdlcegi atrlqlaswd gcslfikitd kvislkegdf
     1861 ffdslrqvsd wvkknrpqke gasttlpyqv ffmrklwlnv tpgkdvnadt ilhyhqelpk
     1921 ymrgfhkcsr edaiylagli ykiqfgsdrs qmasvskilk elvpqnltrl msseewkksl
     1981 llecdkhknk svaeakvefl kriyrwptfg saffevkqts epsypdilli ainrhgllli
     2041 hpktkelldt fpftkissws sgntyfhmal gslgqgsrll cetslgykmd dlltsyvqqi
     2101 lsavnkhrgf ranp
//
LOCUS       NP_001424197             287 aa            linear   ROD 08-APR-2025
DEFINITION  serine/threonine-protein phosphatase PGAM5, mitochondrial isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001424197 XP_006249596
VERSION     NP_001424197.1
DBSOURCE    REFSEQ: accession NM_001437268.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Chen,Y., Huang,J., Zhou,H., Lin,J. and Tao,J.
  TITLE     Pgam5 aggravates hyperglycemia-induced myocardial dysfunction
            through disrupting Phb2-dependent mitochondrial dynamics
  JOURNAL   Int J Med Sci 21 (7), 1194-1203 (2024)
   PUBMED   38818468
  REMARK    GeneRIF: Pgam5 aggravates hyperglycemia-induced myocardial
            dysfunction through disrupting Phb2-dependent mitochondrial
            dynamics.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Fu,G., Wang,B., He,B., Feng,M. and Yu,Y.
  TITLE     LPS induces cardiomyocyte necroptosis through the Ripk3/Pgam5
            signaling pathway
  JOURNAL   J Recept Signal Transduct Res 41 (1), 32-37 (2021)
   PUBMED   32580628
  REMARK    GeneRIF: LPS induces cardiomyocyte necroptosis through the
            Ripk3/Pgam5 signaling pathway.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Liu,G., Qian,M., Chen,M., Chen,T. and Qin,S.
  TITLE     miR-21-5p Suppresses Mitophagy to Alleviate Hyperoxia-Induced Acute
            Lung Injury by Directly Targeting PGAM5
  JOURNAL   Biomed Res Int 2020, 4807254 (2020)
   PUBMED   33681349
  REMARK    GeneRIF: miR-21-5p Suppresses Mitophagy to Alleviate
            Hyperoxia-Induced Acute Lung Injury by Directly Targeting PGAM5.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Yang,C., Liu,X., Yang,F., Zhang,W., Chen,Z., Yan,D., You,Q. and
            Wu,X.
  TITLE     Mitochondrial phosphatase PGAM5 regulates Keap1-mediated Bcl-xL
            degradation and controls cardiomyocyte apoptosis driven by
            myocardial ischemia/reperfusion injury
  JOURNAL   In Vitro Cell Dev Biol Anim 53 (3), 248-257 (2017)
   PUBMED   27815660
  REMARK    GeneRIF: PGAM5 controls cardiomyocyte apoptosis induced by MIRI
            through regulating Keap1-mediated Bcl-xL degradation, which may
            supply a novel molecular target for acute myocardial infarction
            (AMI) therapy.
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Sekine,S., Yao,A., Hattori,K., Sugawara,S., Naguro,I., Koike,M.,
            Uchiyama,Y., Takeda,K. and Ichijo,H.
  TITLE     The Ablation of Mitochondrial Protein Phosphatase Pgam5 Confers
            Resistance Against Metabolic Stress
  JOURNAL   EBioMedicine 5, 82-92 (2016)
   PUBMED   27077115
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Wei,H., Liu,L. and Chen,Q.
  TITLE     Selective removal of mitochondria via mitophagy: distinct pathways
            for different mitochondrial stresses
  JOURNAL   Biochim Biophys Acta 1853 (10 Pt B), 2784-2790 (2015)
   PUBMED   25840011
  REMARK    Review article
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Hayes,J.D. and Dinkova-Kostova,A.T.
  TITLE     The Nrf2 regulatory network provides an interface between redox and
            intermediary metabolism
  JOURNAL   Trends Biochem Sci 39 (4), 199-218 (2014)
   PUBMED   24647116
  REMARK    Review article
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Wang,Z., Jiang,H., Chen,S., Du,F. and Wang,X.
  TITLE     The mitochondrial phosphatase PGAM5 functions at the convergence
            point of multiple necrotic death pathways
  JOURNAL   Cell 148 (1-2), 228-243 (2012)
   PUBMED   22265414
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Takeda,K., Komuro,Y., Hayakawa,T., Oguchi,H., Ishida,Y.,
            Murakami,S., Noguchi,T., Kinoshita,H., Sekine,Y., Iemura,S.,
            Natsume,T. and Ichijo,H.
  TITLE     Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic
            activity as a protein serine/threonine phosphatase to activate ASK1
  JOURNAL   Proc Natl Acad Sci U S A 106 (30), 12301-12305 (2009)
   PUBMED   19590015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249596.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.16027.1,
                                           SRR26643429.43815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..287
                     /product="serine/threonine-protein phosphatase PGAM5,
                     mitochondrial isoform 2"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase PGAM5,
                     mitochondrial; phosphoglycerate mutase family member 5"
                     /calculated_mol_wt=31741
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q562B5.1)"
     Region          13..285
                     /region_name="HP"
                     /note="Histidine phosphatase domain found in a
                     functionally diverse set of proteins, mostly phosphatases;
                     contains a His residue which is phosphorylated during the
                     reaction; cl11399"
                     /db_xref="CDD:472174"
     Site            24..25
                     /site_type="cleavage"
                     /note="Cleavage, by PARL.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            order(103..104,151,228..229)
                     /site_type="active"
                     /note="catalytic core [active]"
                     /db_xref="CDD:132718"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96HS1; propagated from
                     UniProtKB/Swiss-Prot (Q562B5.1)"
     CDS             1..287
                     /gene="Pgam5"
                     /gene_synonym="RGD1312028"
                     /coded_by="NM_001437268.1:31..894"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:288731"
                     /db_xref="RGD:1312028"
ORIGIN      
        1 mafrqalqla acglaggsaa vlfsavavgk praggdadtr tteplawtga rpghgvwdsn
       61 wdrreplsli nlkkrnvesg edelasrldh ykakatrhif lirhsqynvd gsmekdrtlt
      121 plgreqaelt girlaslglk fnkivhssmt ravettdiis khlpgvcrvs tdllregapi
      181 epdppvshwk peavyyedga rieaafrnyi hradakqeed syeifichan viryivcral
      241 qfppegwlrl slnngsithl virpngrval rtlgdtgfmp pdkitrs
//
LOCUS       NP_001424441             978 aa            linear   ROD 08-APR-2025
DEFINITION  macrophage colony-stimulating factor 1 receptor isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001424441 XP_006254875
VERSION     NP_001424441.1
DBSOURCE    REFSEQ: accession NM_001437512.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 978)
  AUTHORS   Hume,D.A., Teakle,N., Keshvari,S. and Irvine,K.M.
  TITLE     Macrophage deficiency in CSF1R-knockout rat embryos does not
            compromise placental or embryo development
  JOURNAL   J Leukoc Biol 114 (5), 421-433 (2023)
   PUBMED   37167456
  REMARK    GeneRIF: Macrophage deficiency in CSF1R-knockout rat embryos does
            not compromise placental or embryo development.
REFERENCE   2  (residues 1 to 978)
  AUTHORS   Sehgal,A., Carter-Cusack,D., Keshvari,S., Patkar,O., Huang,S.,
            Summers,K.M., Hume,D.A. and Irvine,K.M.
  TITLE     Intraperitoneal transfer of wild-type bone marrow repopulates
            tissue macrophages in the Csf1r knockout rat without contributing
            to monocytopoiesis
  JOURNAL   Eur J Immunol 53 (8), e2250312 (2023)
   PUBMED   37059596
  REMARK    GeneRIF: Intraperitoneal transfer of wild-type bone marrow
            repopulates tissue macrophages in the Csf1r knockout rat without
            contributing to monocytopoiesis.
REFERENCE   3  (residues 1 to 978)
  AUTHORS   Keshvari,S., Caruso,M., Teakle,N., Batoon,L., Sehgal,A.,
            Patkar,O.L., Ferrari-Cestari,M., Snell,C.E., Chen,C., Stevenson,A.,
            Davis,F.M., Bush,S.J., Pridans,C., Summers,K.M., Pettit,A.R.,
            Irvine,K.M. and Hume,D.A.
  TITLE     CSF1R-dependent macrophages control postnatal somatic growth and
            organ maturation
  JOURNAL   PLoS Genet 17 (6), e1009605 (2021)
   PUBMED   34081701
  REMARK    GeneRIF: CSF1R-dependent macrophages control postnatal somatic
            growth and organ maturation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 978)
  AUTHORS   Patkar,O.L., Caruso,M., Teakle,N., Keshvari,S., Bush,S.J.,
            Pridans,C., Belmer,A., Summers,K.M., Irvine,K.M. and Hume,D.A.
  TITLE     Analysis of homozygous and heterozygous Csf1r knockout in the rat
            as a model for understanding microglial function in brain
            development and the impacts of human CSF1R mutations
  JOURNAL   Neurobiol Dis 151, 105268 (2021)
   PUBMED   33450391
  REMARK    GeneRIF: Analysis of homozygous and heterozygous Csf1r knockout in
            the rat as a model for understanding microglial function in brain
            development and the impacts of human CSF1R mutations.
REFERENCE   5  (residues 1 to 978)
  AUTHORS   Sharon,A., Jankowski,M.M., Shmoel,N., Erez,H. and Spira,M.E.
  TITLE     Inflammatory Foreign Body Response Induced by Neuro-Implants in Rat
            Cortices Depleted of Resident Microglia by a CSF1R Inhibitor and
            Its Implications
  JOURNAL   Front Neurosci 15, 646914 (2021)
   PUBMED   33841088
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 978)
  AUTHORS   Storga,D., Pecina-Slaus,N., Pavelic,J., Pavelic,Z.P. and Pavelic,K.
  TITLE     c-fms is present in primary tumours as well as in their metastases
            in bone marrow
  JOURNAL   Int J Exp Pathol 73 (4), 527-533 (1992)
   PUBMED   1390197
REFERENCE   7  (residues 1 to 978)
  AUTHORS   Borycki,A.G., Guillier,M., Leibovitch,M.P. and Leibovitch,S.A.
  TITLE     Molecular cloning of CSF-1 receptor from rat myoblasts. Sequence
            analysis and regulation during myogenesis
  JOURNAL   Growth Factors 6 (3), 209-218 (1992)
   PUBMED   1389227
REFERENCE   8  (residues 1 to 978)
  AUTHORS   Claycomb,W.C. and Lanson,N.A. Jr.
  TITLE     Proto-oncogene expression in proliferating and differentiating
            cardiac and skeletal muscle
  JOURNAL   Biochem J 247 (3), 701-706 (1987)
   PUBMED   2447874
REFERENCE   9  (residues 1 to 978)
  AUTHORS   Leibovitch,S.A., Leibovitch,M.P., Guillier,M., Hillion,J. and
            Harel,J.
  TITLE     Differential expression of protooncogenes related to transformation
            and cancer progression in rat myoblasts
  JOURNAL   Cancer Res 46 (8), 4097-4103 (1986)
   PUBMED   2425941
REFERENCE   10 (residues 1 to 978)
  AUTHORS   Sherr,C.J., Rettenmier,C.W., Sacca,R., Roussel,M.F., Look,A.T. and
            Stanley,E.R.
  TITLE     The c-fms proto-oncogene product is related to the receptor for the
            mononuclear phagocyte growth factor, CSF-1
  JOURNAL   Cell 41 (3), 665-676 (1985)
   PUBMED   2408759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254875.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.495349.1,
                                           SRR26360186.2720224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..978
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..978
                     /product="macrophage colony-stimulating factor 1 receptor
                     isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="macrophage colony-stimulating factor 1 receptor;
                     fms proto-oncogene; proto-oncogene fms; proto-oncogene
                     c-Fms; CSF-1 receptor"
                     /calculated_mol_wt=107293
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1977
     Region          28..101
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          66..70
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          88..91
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          113..195
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          203..295
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          220..224
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          234..238
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          259..263
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          275..280
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          288..291
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          299..398
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          319..323
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          333..337
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..366
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          376..381
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          389..392
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          399..487
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          541..913
                     /region_name="PTKc_CSF-1R"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Colony-Stimulating Factor-1 Receptor; cd05106"
                     /db_xref="CDD:133237"
     Site            order(586..587,589..592,594,612,614,662,664,668,776,
                     780..781,783,794,812..816,825,860)
                     /site_type="active"
                     /db_xref="CDD:133237"
     Site            order(586..587,589..592,594,612,614,662,664,668,780..781,
                     783,794)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133237"
     Site            order(776,780,812..816,825,860)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133237"
     Site            793..818
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133237"
     CDS             1..978
                     /gene="Csf1r"
                     /gene_synonym="c-fms; CSF-1-R; CSF-1R; M-CSF-R; mrfms"
                     /coded_by="NM_001437512.1:109..3045"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:307403"
                     /db_xref="RGD:2425"
ORIGIN      
        1 melgaplvll latawhgqga pviepsgpel vvepgatvtl rcvsngsvew dgpispywtl
       61 dsespgsili tknatfkntg tyrcteledp mrgstaihly vkdpvrpwnl laqevtvfeg
      121 qeavlpclit dptlkdsvsl vrewgrpvsr ktvysflpwr gfiihkakfl dshtymckav
      181 vnarestsig irlkvnrahp gpphiilept klvrirgeaa qivcsathse vefnvilkrg
      241 dtkleipins dfqdnaykkv ltlnlnavdf qdagiyscva nnaagsntat mnfqvvesay
      301 lnltseqsll qevsvgenld ltviadaypg lqrynwtylg pffedphnle frtqwttysy
      361 sfklhlnrvk pleagryslm aqnkagwnnl tfeltlrypp evsvtwipvn gsdvllcdvs
      421 gypqpnvtwm ecrghtdrcd eaqasqvwdd tqpevlsqkp fhrvilqsql pigtlkhnmt
      481 yvcrahnnvg nssqffrais lgqskqlpde ylftpvvvac isvmsllvll lllllykykq
      541 kpkyqvrwki iesyegnnyt fidptqlpyn ekwefprnnl qfgktlgaga fgkvveataf
      601 glgkedavlk vavkmlksta hadekealms elkimshlgq henivnllga cthggpvlvi
      661 teyccygdll nflrrkaeam lgpslspgqd pegdssykni hlekkyvrrd sgfssqgvdt
      721 yvemrpvsts sndsffkqdl dkeasrplel wdllhfssqv aqgmaflask ncihrdvaar
      781 nvlltsghva kigdfglard imndsnyvvk gnarlpvkwm apesifdcvy tvqsdvwsyg
      841 illweifslg lnpypgilvn nkfyklvkdg yqmaqpvfap eniysimqsc wdleptkrpt
      901 fqqicfllqe qarlerreqd yanlpsssss sssssdsggg sggsssepee esssehlacc
      961 epgdiaqpll qpnnyqfc
//
LOCUS       NP_001424262             420 aa            linear   ROD 08-APR-2025
DEFINITION  nucleoporin SEH1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424262 XP_056840911
VERSION     NP_001424262.1
DBSOURCE    REFSEQ: accession NM_001437333.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Parmigiani,A., Nourbakhsh,A., Ding,B., Wang,W., Kim,Y.C.,
            Akopiants,K., Guan,K.L., Karin,M. and Budanov,A.V.
  TITLE     Sestrins inhibit mTORC1 kinase activation through the GATOR complex
  JOURNAL   Cell Rep 9 (4), 1281-1291 (2014)
   PUBMED   25457612
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Bonnet,A. and Palancade,B.
  TITLE     Regulation of mRNA trafficking by nuclear pore complexes
  JOURNAL   Genes (Basel) 5 (3), 767-791 (2014)
   PUBMED   25184662
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Ahn,S.H., Deshmukh,H., Johnson,N., Cowell,L.G., Rude,T.H.,
            Scott,W.K., Nelson,C.L., Zaas,A.K., Marchuk,D.A., Keum,S.,
            Lamlertthon,S., Sharma-Kuinkel,B.K., Sempowski,G.D. and Fowler,V.G.
            Jr.
  TITLE     Two genes on A/J chromosome 18 are associated with susceptibility
            to Staphylococcus aureus infection by combined microarray and QTL
            analyses
  JOURNAL   PLoS Pathog 6 (9), e1001088 (2010)
   PUBMED   20824097
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Zuccolo,M., Alves,A., Galy,V., Bolhy,S., Formstecher,E., Racine,V.,
            Sibarita,J.B., Fukagawa,T., Shiekhattar,R., Yen,T. and Doye,V.
  TITLE     The human Nup107-160 nuclear pore subcomplex contributes to proper
            kinetochore functions
  JOURNAL   EMBO J 26 (7), 1853-1864 (2007)
   PUBMED   17363900
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Glavy,J.S., Krutchinsky,A.N., Cristea,I.M., Berke,I.C., Boehmer,T.,
            Blobel,G. and Chait,B.T.
  TITLE     Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
            subcomplex
  JOURNAL   Proc Natl Acad Sci U S A 104 (10), 3811-3816 (2007)
   PUBMED   17360435
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Loiodice,I., Alves,A., Rabut,G., Van Overbeek,M., Ellenberg,J.,
            Sibarita,J.B. and Doye,V.
  TITLE     The entire Nup107-160 complex, including three new members, is
            targeted as one entity to kinetochores in mitosis
  JOURNAL   Mol Biol Cell 15 (7), 3333-3344 (2004)
   PUBMED   15146057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 2, 2025 this sequence version replaced XP_056840911.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.291576.1,
                                           SRR22399492.2302238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..420
                     /product="nucleoporin SEH1 isoform 3"
                     /note="nucleoporin SEH1; nucleoporin SEH1-like"
                     /calculated_mol_wt=46207
     Region          <11..328
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          15..55
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          61..111
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..149
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..267
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          281..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..420
                     /gene="Seh1l"
                     /coded_by="NM_001437333.1:83..1345"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:100911798"
                     /db_xref="RGD:6490353"
ORIGIN      
        1 mfvarsiaad hkdlihdvsf dfhgrrmatc ssdqsvkvwd ksesgdwhct aswkthsgsv
       61 wrvtwahpef gqvlascsfd rtaavweeiv gesndklrgq shwvkrttlv dsrtsvtdvk
      121 fapkhmglml atcsadgivr vyeapdvmnl sqwslqheis cklccscisw npsssrahpp
      181 miavgsddss pnsmakvqif eynentrkya kaetlmtvtd pvhdiafapn lgrsfhilai
      241 atkdvriftl kpvrkeltss ggptkfeihi vaqfdnhnsq vwrvswnitg tvlassgddg
      301 cvrlwkanym dnwkctgilk gngspvngss qlgnstpsls snipnlqnsl ngtsagryff
      361 ppldsprags rwsscaqllp ppapllehsc dadtanlhyp hprrgclsrp lnplpenegv
//
LOCUS       NP_001423826             216 aa            linear   ROD 08-APR-2025
DEFINITION  ceramide-1-phosphate transfer protein isoform a [Rattus
            norvegicus].
ACCESSION   NP_001423826 XP_006239638
VERSION     NP_001423826.1
DBSOURCE    REFSEQ: accession NM_001436897.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Mishra,S.K., Gao,Y.G., Deng,Y., Chalfant,C.E., Hinchcliffe,E.H. and
            Brown,R.E.
  TITLE     CPTP: A sphingolipid transfer protein that regulates autophagy and
            inflammasome activation
  JOURNAL   Autophagy 14 (5), 862-879 (2018)
   PUBMED   29164996
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Simanshu,D.K., Kamlekar,R.K., Wijesinghe,D.S., Zou,X., Zhai,X.,
            Mishra,S.K., Molotkovsky,J.G., Malinina,L., Hinchcliffe,E.H.,
            Chalfant,C.E., Brown,R.E. and Patel,D.J.
  TITLE     Non-vesicular trafficking by a ceramide-1-phosphate transfer
            protein regulates eicosanoids
  JOURNAL   Nature 500 (7463), 463-467 (2013)
   PUBMED   23863933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006239638.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.25180.1,
                                           SRR26643292.24630.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840110 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..216
                     /product="ceramide-1-phosphate transfer protein isoform a"
                     /note="glycolipid transfer protein domain-containing
                     protein 1; glycolipid transfer protein domain containing
                     1"
                     /calculated_mol_wt=24391
     Region          27..175
                     /region_name="GLTP"
                     /note="Glycolipid transfer protein (GLTP); pfam08718"
                     /db_xref="CDD:462575"
     CDS             1..216
                     /gene="Cptp"
                     /gene_synonym="Gltpd1"
                     /coded_by="NM_001436897.1:339..989"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313771"
                     /db_xref="RGD:1359656"
ORIGIN      
        1 mdgperdfnl kvvlisfkkc ltdkgevlld hytaswkglv rflnslgavf sfiskdvvsk
       61 lqimehlrsg pqsehyislq smvayevsnk lvdrdsrsrp rhpnsgcrtv lrlhralhwl
      121 qlfleglrts sedartstlc seaynatlaa yhswivrqav nvafhalppr kvfleamnmg
      181 sseqavemlg ealpfieqvy disqklyaeh slldlp
//
LOCUS       NP_001424454             368 aa            linear   ROD 08-APR-2025
DEFINITION  zinc finger protein 24 [Rattus norvegicus].
ACCESSION   NP_001424454 XP_006254526
VERSION     NP_001424454.1
DBSOURCE    REFSEQ: accession NM_001437525.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Howng,S.Y., Avila,R.L., Emery,B., Traka,M., Lin,W., Watkins,T.,
            Cook,S., Bronson,R., Davisson,M., Barres,B.A. and Popko,B.
  TITLE     ZFP191 is required by oligodendrocytes for CNS myelination
  JOURNAL   Genes Dev 24 (3), 301-311 (2010)
   PUBMED   20080941
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Wang,H., Sun,R., Liu,G., Yao,M., Fei,J. and Shen,H.
  TITLE     Characterization of the target DNA sequence for the DNA-binding
            domain of zinc finger protein 191
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 40 (8), 704-710 (2008)
   PUBMED   18685786
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254526.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.19498.1,
                                           SRR26643292.59012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..368
                     /product="zinc finger protein 24"
                     /note="zfp-191; zinc finger protein 191"
                     /calculated_mol_wt=41779
     Region          48..159
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          <249..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          251..301
                     /region_name="Necessary and sufficient for nuclear
                     localization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          305..>358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P17028; propagated from
                     UniProtKB/Swiss-Prot (Q7TNK3.1)"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..368
                     /gene="Zfp24"
                     /gene_synonym="Zfp191; Znf24"
                     /coded_by="NM_001437525.1:154..1260"
                     /db_xref="GeneID:360204"
                     /db_xref="RGD:727963"
ORIGIN      
        1 msaqsveeds iliipnpdee ekilrvklee dpdgeegssi swnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailprelqt lvrehhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lveeiasqed aqglpsseld avenqlkwas
      181 welhslrhcd ddataengal apkqeiasag eshevpgtln igvpqifkyg etcfpkgrfe
      241 rkrnpsrkkq hicdecgkhf sqgsalilhq rihsgekpyg cvecgkafsr ssilvqhqrv
      301 htgekpykcl ecgkafsqns glinhqriht gekpyecvqc gksysqssnl frhqrrhnae
      361 kllnvvkv
//
LOCUS       NP_001424171            1181 aa            linear   ROD 08-APR-2025
DEFINITION  lysine-specific demethylase hairless [Rattus norvegicus].
ACCESSION   NP_001424171 XP_063130679
VERSION     NP_001424171.1
DBSOURCE    REFSEQ: accession NM_001437242.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Kuramoto,T., Kuwamura,M., Tagami,F., Mashimo,T., Nose,M. and
            Serikawa,T.
  TITLE     Kyoto rhino rats derived by ENU mutagenesis undergo congenital hair
            loss and exhibit focal glomerulosclerosis
  JOURNAL   Exp Anim 60 (1), 57-63 (2011)
   PUBMED   21325752
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Hsieh,J.C., Slater,S.A., Whitfield,G.K., Dawson,J.L., Hsieh,G.,
            Sheedy,C., Haussler,C.A. and Haussler,M.R.
  TITLE     Analysis of hairless corepressor mutants to characterize molecular
            cooperation with the vitamin D receptor in promoting the mammalian
            hair cycle
  JOURNAL   J Cell Biochem 110 (3), 671-686 (2010)
   PUBMED   20512927
  REMARK    GeneRIF: Hr and VDR interact via multiple protein-protein
            interfaces, catalyzing histone demethylation to effect chromatin
            remodeling and repress the transcription of VDR target genes that
            control the hair cycle.
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Wen,Y., Liu,Y., Xu,Y., Zhao,Y., Hua,R., Wang,K., Sun,M., Li,Y.,
            Yang,S., Zhang,X.J., Kruse,R., Cichon,S., Betz,R.C., Nothen,M.M.,
            van Steensel,M.A., van Geel,M., Steijlen,P.M., Hohl,D., Huber,M.,
            Dunnill,G.S., Kennedy,C., Messenger,A., Munro,C.S., Terrinoni,A.,
            Hovnanian,A., Bodemer,C., de Prost,Y., Paller,A.S., Irvine,A.D.,
            Sinclair,R., Green,J., Shang,D., Liu,Q., Luo,Y., Jiang,L.,
            Chen,H.D., Lo,W.H., McLean,W.H., He,C.D. and Zhang,X.
  TITLE     Loss-of-function mutations of an inhibitory upstream ORF in the
            human hairless transcript cause Marie Unna hereditary hypotrichosis
  JOURNAL   Nat Genet 41 (2), 228-233 (2009)
   PUBMED   19122663
  REMARK    Erratum:[Nat Genet. 2009 Jun;41(6):762]
REFERENCE   4  (residues 1 to 1181)
  AUTHORS   Hsieh,J.C., Sisk,J.M., Jurutka,P.W., Haussler,C.A., Slater,S.A.,
            Haussler,M.R. and Thompson,C.C.
  TITLE     Physical and functional interaction between the vitamin D receptor
            and hairless corepressor, two proteins required for hair cycling
  JOURNAL   J Biol Chem 278 (40), 38665-38674 (2003)
   PUBMED   12847098
REFERENCE   5  (residues 1 to 1181)
  AUTHORS   Fernandez,A., Silio,L., Noguera,J.L., Sanchez,A. and Ovilo,C.
  TITLE     Linkage mapping of the porcine hairless gene (HR) to chromosome 14
  JOURNAL   Anim Genet 34 (4), 317-318 (2003)
   PUBMED   12873232
REFERENCE   6  (residues 1 to 1181)
  AUTHORS   Potter,G.B., Zarach,J.M., Sisk,J.M. and Thompson,C.C.
  TITLE     The thyroid hormone-regulated corepressor hairless associates with
            histone deacetylases in neonatal rat brain
  JOURNAL   Mol Endocrinol 16 (11), 2547-2560 (2002)
   PUBMED   12403844
REFERENCE   7  (residues 1 to 1181)
  AUTHORS   Zlotogorski,A., Ahmad,W. and Christiano,A.M.
  TITLE     Congenital atrichia in five Arab Palestinian families resulting
            from a deletion mutation in the human hairless gene
  JOURNAL   Hum Genet 103 (4), 400-404 (1998)
   PUBMED   9856480
REFERENCE   8  (residues 1 to 1181)
  AUTHORS   Cichon,S., Anker,M., Vogt,I.R., Rohleder,H., Putzstuck,M.,
            Hillmer,A., Farooq,S.A., Al-Dhafri,K.S., Ahmad,M., Haque,S.,
            Rietschel,M., Propping,P., Kruse,R. and Nothen,M.M.
  TITLE     Cloning, genomic organization, alternative transcripts and
            mutational analysis of the gene responsible for autosomal recessive
            universal congenital alopecia
  JOURNAL   Hum Mol Genet 7 (11), 1671-1679 (1998)
   PUBMED   9736769
  REMARK    Erratum:[Hum Mol Genet 1998 Nov;7(12):1987-8]
REFERENCE   9  (residues 1 to 1181)
  AUTHORS   Thompson,C.C. and Bottcher,M.C.
  TITLE     The product of a thyroid hormone-responsive gene interacts with
            thyroid hormone receptors
  JOURNAL   Proc Natl Acad Sci U S A 94 (16), 8527-8532 (1997)
   PUBMED   9238010
REFERENCE   10 (residues 1 to 1181)
  AUTHORS   Thompson,C.C.
  TITLE     Thyroid hormone-responsive genes in developing cerebellum include a
            novel synaptotagmin and a hairless homolog
  JOURNAL   J Neurosci 16 (24), 7832-7840 (1996)
   PUBMED   8987811
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063130679.1.
            
            Summary: This gene encodes a protein that is involved in hair
            growth. This protein functions as a transcriptional corepressor of
            multiple nuclear receptors, including thyroid hormone receptor, the
            retinoic acid receptor-related orphan receptors and the vitamin D
            receptors, and it interacts with histone deacetylases. The
            translation of this protein is modulated by a regulatory open
            reading frame (ORF) that exists upstream of the primary ORF.
            Mutations in this upstream ORF cause Marie Unna hereditary
            hypotrichosis (MUHH), an autosomal dominant form of genetic hair
            loss in human. [provided by RefSeq, Oct 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.57288.1,
                                           SRR26643295.51265.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p11"
     Protein         1..1181
                     /product="lysine-specific demethylase hairless"
                     /EC_number="1.14.11.65"
                     /note="protein hairless; hairless homolog; hairless
                     protein; hair growth associated; [histone
                     H3]-dimethyl-L-lysine(9) demethylase hairless"
                     /calculated_mol_wt=127233
     Region          311..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          413..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          509..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          560..564
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          696..745
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          752..756
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P97609.2)"
     Region          <1081..1132
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..1181
                     /gene="Hr"
                     /coded_by="NM_001437242.1:594..4139"
                     /db_xref="GeneID:60563"
                     /db_xref="RGD:620634"
ORIGIN      
        1 mesmpsflkd tpawektapv ngivgqepgt spqdglhhga lclgepvpfw rgvlsapdsw
       61 lppgflqgpk dtlsvvegeg srngerkanw lgskeglrwk eamlahplaf cgpacppryg
      121 plipehssgh pksdpvafrp lhcpflletk ilerapfwvp tclppylmss lppersydwp
      181 lapspwvysg sqpkvpsafs lgskgfyhkd pnilrpakep laasesgmlg lapgghlqqa
      241 cdaegpslhq rdgetgagrq qnlcpvflgy pdtvprtpwp scppglvhtl gnvwagpgsn
      301 sfgyqlgppv tprcpspgpp tppggccssh lparegdpgp crkcqdspeg sssgpgesse
      361 ernkagsras ppshhtklkk twltrhseqf ecpggcpgkg espatglral kragspevqg
      421 argpapkrps htfpgtgrqg arawqetpet stgskaeaqq qeeqrgprdg rirlresrle
      481 dtscqhhlag vtqcpscvqa ageveiltsh sqkshrlple ekpleedsca tseegggssp
      541 easinkglak hllsglgdrl crllrkerea lawaqregqg pamtedspgi phccsrchhg
      601 lfnthwrcsh cshrlcvacg riagagknre ktgsreqrtd dcaqeaghaa csliltqfvs
      661 sqalaelstv mhqvwakfdi rghcfcqvda rvwapgdggq qkeptektpp apqlscngds
      721 nrtkdikeet pdstespaed ragrsplpcp slcellasta vklclgheri hmafapvtpa
      781 lpsddritni ldsiiaqvve rkiqekalgp glragsglrk glslplspvr trlsppgall
      841 wlqeprpkhg frlfqehwrq gqpvlvsgiq ktlrlslwgm ealgtlggqv qtltalgppq
      901 ptsldstafw kgfshpearp kldegsvlll hrplgdkdes rvenlasslp lpeycahqgk
      961 lnlasylplg ltlhplepql waaygvnshr ghlgtknlcv evsdlisilv haeaqlppwy
     1021 raqkdflsgl dgeglwspgs qtstvwhvfr aqdaqrirrf lqmvcpagag tlepgapgsc
     1081 yldsglrrrl reewgvscwt llqapgeavl vpagaphqvq glvstisvtq hflspetsal
     1141 saqlchqgas lppdhrmlya qmdravfqav kvavgtlqea k
//
LOCUS       NP_001424246             853 aa            linear   ROD 08-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF216 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424246 XP_038945295
VERSION     NP_001424246.1
DBSOURCE    REFSEQ: accession NM_001437317.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Chen,T., Zhu,J. and Wang,Y.H.
  TITLE     RNF216 mediates neuronal injury following experimental subarachnoid
            hemorrhage through the Arc/Arg3.1-AMPAR pathway
  JOURNAL   FASEB J 34 (11), 15080-15092 (2020)
   PUBMED   32918771
  REMARK    GeneRIF: RNF216 mediates neuronal injury following experimental
            subarachnoid hemorrhage through the Arc/Arg3.1-AMPAR pathway.
            Erratum:[FASEB J. 2024 May 15;38(9):e23652. doi:
            10.1096/fj.202400924. PMID: 38708783]
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Mabb,A.M., Je,H.S., Wall,M.J., Robinson,C.G., Larsen,R.S.,
            Qiang,Y., Correa,S.A. and Ehlers,M.D.
  TITLE     Triad3A regulates synaptic strength by ubiquitination of Arc
  JOURNAL   Neuron 82 (6), 1299-1316 (2014)
   PUBMED   24945773
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Nakhaei,P., Mesplede,T., Solis,M., Sun,Q., Zhao,T., Yang,L.,
            Chuang,T.H., Ware,C.F., Lin,R. and Hiscott,J.
  TITLE     The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS
            signaling pathway by targeting TRAF3 for degradation
  JOURNAL   PLoS Pathog 5 (11), e1000650 (2009)
   PUBMED   19893624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038945295.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.47098.1,
                                           SRR26643287.27739.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..853
                     /product="E3 ubiquitin-protein ligase RNF216 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF216"
                     /calculated_mol_wt=97465
     Region          501..557
                     /region_name="RING-HC_RBR_RNF216"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 216 (RNF216) and similar proteins; cd16630"
                     /db_xref="CDD:438292"
     Region          590..641
                     /region_name="BRcat_RBR_RNF216"
                     /note="BRcat domain found in RING finger protein 216
                     (RNF216); cd20339"
                     /db_xref="CDD:439000"
     Region          652..708
                     /region_name="Rcat_RBR_RNF216"
                     /note="Rcat domain found in RING finger protein 216
                     (RNF216); cd20353"
                     /db_xref="CDD:439014"
     CDS             1..853
                     /gene="Rnf216"
                     /gene_synonym="RGD1565135"
                     /coded_by="NM_001437317.1:226..2787"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:304294"
                     /db_xref="RGD:1565135"
ORIGIN      
        1 maegnnqeev ihlnnfhchr gkewmavreg pitisdssde egipmlvtpa teqqeddldd
       61 dvilteddse decggfldlk tekkggeakp gpsnkqtadn tvsprleqkv iilgengllf
      121 seseplevqn qlsedsetdl lsnpgepaas vdeqlieeey wldhpyfqal npqpqertnq
      181 lvpqerhses emgpmffrhd fpepafprpe pqqegipgpa spqpahplge ledqqlaide
      241 dpgpayplpg pqeanlanvw gqeaaegdqe lipllvkete arfpdvangy veeiihlkny
      301 ydlnvlcnfl lenpdypkre drilihpsss llasqddvkl pkidffdysk ltpldqrcfi
      361 qaadllmadf kmlssqdikw alhelkghya itrkafsdai kkwqelspet sgkrkkrkem
      421 nqysfidfkf eqgnikiekr mfflenkrrh crsydqqall pavqqeqefy eqkikemaeh
      481 edfllalqmn eeqyqkdgql iecrccygef pfeeltqcad ahlfckecli ryaqeavfgs
      541 gkselscmeg sctcsfptse lekvlpqtil ykyyerkaee evaaayadel vrcpscsfpa
      601 lldsdvkrfs cpnprcrket crkcqglwke hngltceela ekddikyrts ieekmtaari
      661 rkchkcgtgl iksegcnrms crcgaqmcyl crvsingydh fcqhprspga pcqecsrcsl
      721 wtdpteddek lieeiqkeae eeqkrkngen tfkrigpple kpaekvqrve alprpvpqnl
      781 hpqmppyafv hppfplppvr pvfnnfpinm gpvpapyvpp lpnvrvnfdf ghvhvplehn
      841 lpmhfgpqpr hrf
//
LOCUS       NP_001423875            1127 aa            linear   ROD 08-APR-2025
DEFINITION  adipocyte enhancer-binding protein 1 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001423875 XP_006251378
VERSION     NP_001423875.1
DBSOURCE    REFSEQ: accession NM_001436946.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Blackburn,P.R., Xu,Z., Tumelty,K.E., Zhao,R.W., Monis,W.J.,
            Harris,K.G., Gass,J.M., Cousin,M.A., Boczek,N.J., Mitkov,M.V.,
            Cappel,M.A., Francomano,C.A., Parisi,J.E., Klee,E.W., Faqeih,E.,
            Alkuraya,F.S., Layne,M.D., McDonnell,N.B. and Atwal,P.S.
  TITLE     Bi-allelic Alterations in AEBP1 Lead to Defective Collagen Assembly
            and Connective Tissue Structure Resulting in a Variant of
            Ehlers-Danlos Syndrome
  JOURNAL   Am J Hum Genet 102 (4), 696-705 (2018)
   PUBMED   29606302
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   4  (residues 1 to 1127)
  AUTHORS   Didangelos,A., Yin,X., Mandal,K., Baumert,M., Jahangiri,M. and
            Mayr,M.
  TITLE     Proteomics characterization of extracellular space components in
            the human aorta
  JOURNAL   Mol Cell Proteomics 9 (9), 2048-2062 (2010)
   PUBMED   20551380
REFERENCE   5  (residues 1 to 1127)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 1127)
  AUTHORS   Lyons,P.J., Muise,A.M. and Ro,H.S.
  TITLE     MAPK modulates the DNA binding of adipocyte enhancer-binding
            protein 1
  JOURNAL   Biochemistry 44 (3), 926-931 (2005)
   PUBMED   15654748
REFERENCE   7  (residues 1 to 1127)
  AUTHORS   He,G.P., Muise,A., Li,A.W. and Ro,H.S.
  TITLE     A eukaryotic transcriptional repressor with carboxypeptidase
            activity
  JOURNAL   Nature 378 (6552), 92-96 (1995)
   PUBMED   7477299
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006251378.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1444748.1,
                                           SRR26360186.1986541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1127
                     /product="adipocyte enhancer-binding protein 1 isoform 2
                     precursor"
                     /note="adipocyte enhancer-binding protein 1; aortic
                     carboxypeptidase-like protein"
                     /calculated_mol_wt=125538
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2471
     Region          377..530
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          381..546
                     /region_name="Required for DNA-binding and interaction
                     with NFKBIA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          412..615
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Site            order(425,453,460)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            519
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          546..976
                     /region_name="Interaction with PTEN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          555..894
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(616,619,681,690..691,754..755,761,865)
                     /site_type="active"
                     /db_xref="CDD:349427"
     Region          898..973
                     /region_name="Peptidase_M14NE-CP-C_like"
                     /note="Peptidase associated domain: C-terminal domain of
                     M14 N/E carboxypeptidase; putative folding, regulation, or
                     interaction domain; cd11308"
                     /db_xref="CDD:200604"
     Region          932..1127
                     /region_name="Required for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          997..1127
                     /region_name="Interaction with MAPK1 and MAPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     Region          1026..1055
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RUV9.1)"
     CDS             1..1127
                     /gene="Aebp1"
                     /coded_by="NM_001436946.1:197..3580"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:305494"
                     /db_xref="RGD:1306922"
ORIGIN      
        1 maavrtasll cgllallalc pegspqtvlt ddeiqefleg flsefetqsp preddveaqp
       61 lpeptqrark skaggkprad aeappeknkd kekkgkkdkg pkaakhlegs trptkkpkek
      121 ppkatkkpke kppkatkkpk ekppkatkkp kekppkatkr psagkrfstv apletpersl
      181 tspsnpgtre lpeergrtsl ntwqgqgeet qvearqhrpe peeetemptl dyndqiered
      241 yedfeyirrq kqprptpsrk riwpeppeek tqepeerkev dpplkpllpp dygdgylipn
      301 yddldyyfph pppqkpdvgq evdeekeelk kpkkegsspk edtedkwaae knkdhkgprk
      361 geeleeewgp vekikcppig meshriednq irassmlrhg lgaqrgrlnm qaganeddyy
      421 dgawcaedes qtqwievdtr rttrftgvit qgrdssihdd fvttffvgfs ndsqtwvmyt
      481 ngyeemtfhg nvdkdtpvls elpepvvarf iriypltwng slcmrlevlg cpvtpvysyy
      541 aqnevvttds ldfrhhsykd mrqlmkvvne ecptitrtys lgkssrglki yameisdnpg
      601 ehelgepefr ytagmhgnev lgrelllllm qylcheyrdg nprvrnlvqd trihlvpsln
      661 pdgyevaaqm gsefgnwalg lwteegfdif edfpdlnsvl waaeekkwvp yrvpnnnlpi
      721 perylspdat vstevraiis wmeknpfvlg anlnggerlv sypydmartp sqeqllaaal
      781 aaargedede vseaqetpdh aifrwlaisf asahltmtep yrggcqaqdy tsgmgivnga
      841 kwnprsgtfn dfsylhtncl elsiylgcdk fpheselpre wennkeallt fmeqvhrgik
      901 gvvtdeqgip ianatisvsg inhgvktasg gdywrilnpg eyrvtahaeg ytssakicnv
      961 dydigatqcn filarsnwkr ireilamngn rpilrvdpsr pmtpqqrrlq qrrlryrlrm
     1021 reqmrlrrln sttgpatspt paltlppspt pgstsrlwei lpttaagwee setetytevv
     1081 tefeteygpd leveeleeee eeeeemdtgl tfpvttvety tvnfgdf
//
LOCUS       NP_001424465            1552 aa            linear   ROD 08-APR-2025
DEFINITION  serine/threonine-protein kinase MRCK gamma isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424465 XP_006230813
VERSION     NP_001424465.1
DBSOURCE    REFSEQ: accession NM_001437536.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1552)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   2  (residues 1 to 1552)
  AUTHORS   Ng,Y., Tan,I., Lim,L. and Leung,T.
  TITLE     Expression of the human myotonic dystrophy kinase-related
            Cdc42-binding kinase gamma is regulated by promoter DNA methylation
            and Sp1 binding
  JOURNAL   J Biol Chem 279 (33), 34156-34164 (2004)
   PUBMED   15194684
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006230813.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.5578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1552
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1552
                     /product="serine/threonine-protein kinase MRCK gamma
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase MRCK gamma; CDC42
                     binding protein kinase gamma (DMPK-like)"
                     /calculated_mol_wt=172296
     Region          69..399
                     /region_name="STKc_DMPK_like"
                     /note="Catalytic domain of Myotonic Dystrophy protein
                     kinase (DMPK)-like Serine/Threonine Kinases; cd05597"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,148..149,151,155,157,195,197,
                     199..200,202,212..213,216,231..236,268,274,277)
                     /site_type="active"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,149..151,155,195,197,199..200,
                     202,212..213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270748"
     Site            order(81,155,157,195,197,199,216,231..236,268,274,277)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270748"
     Site            order(212..222,225..236)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270748"
     Site            393..398
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270748"
     Region          <446..>801
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          879..930
                     /region_name="C1_MRCKgamma"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in myotonic dystrophy kinase-related Cdc42-binding
                     kinase gamma (MRCK gamma) and similar proteins; cd20866"
                     /db_xref="CDD:410416"
     Site            order(884..890,898..902,905)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410416"
     Region          938..1070
                     /region_name="PH_MRCK"
                     /note="MRCK (myotonic dystrophy-related Cdc42-binding
                     kinase) pleckstrin homology (PH) domain; cd01243"
                     /db_xref="CDD:269949"
     Region          1102..1360
                     /region_name="CNH"
                     /note="CNH domain; pfam00780"
                     /db_xref="CDD:459938"
     CDS             1..1552
                     /gene="Cdc42bpg"
                     /gene_synonym="RGD1307260"
                     /coded_by="NM_001437536.1:179..4837"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293693"
                     /db_xref="RGD:1307260"
ORIGIN      
        1 meqrlraleq lvrgeaggsp gldglldlll gvhqelssap lrrernvaqf lswagpfvtk
       61 vkelrlqrdd feilkvigrg afgevavvrq rdsgqifamk mlhkwemlkr aetacfreer
      121 dvlvkgdsrw vtalhyafqd eeylylvmdy yaggdlltll srfedrlppe laqfylaemv
      181 laihslhqlg yvhrdvkpdn illdmnghir ladfgsclrl nnngmvdssv avgtpdyisp
      241 eilqameegk ghygpqcdww slgvcayell fgetpfyaes lvetygkimn hedhlqfpsd
      301 vddvpasaqa lirqllcrqe erlgrggldd frshpffegv dwerlatsta pyipelrgpv
      361 dtsnfdvddd tlnrpetlpp sshgafsghh lpfvgftyts gsltddksse lmatpewkph
      421 gveqmkvels qkcqealhss lqpqelvrlq kevqvlqekl tetlrdskas lsqadglhvr
      481 spapdiqlqq ekdrlqqela eaqaalqvrd aelcqaqnrq eeflqrlwea qereaaaasq
      541 iqalnsqlee awvvrreleg qvntlsqevt qlqgqckqds ssqaktvhaa petngigspe
      601 gqsqeaqlrk evaalreqle cacsqgvnvg keevlcrlqe enqrlsreqe rlaeeldlel
      661 qsrqrleger resesnweaq iadilswvnd ekvsrgylqa latkmaeele slrnvgtqtl
      721 ptrpldhqwk arrlqkmeas arlelqsale aeirakqglq eqltqvqeaq rqaerrlqea
      781 ekqnqalqqe vaelreelqa rgpgdakpct slipllsfwn tekdsakdpg nsgesprsga
      841 eaelrpegrr slrmgsvfpr vpaanptpae gppakpgsht lrprsfpspt kclhctslml
      901 glgrqglgcd tcgyfchsac atqappcpvp pellrtalgv hpetgtgtay egflsvprps
      961 gvrrgwqrvy aalsdsrlll fdapdprgsm asgvllqald lrdpqfsatp vlapdvihaq
     1021 skdlprifrv tasqltvpps tctvlllaen egererwlqv lselqrllld arprprpvyt
     1081 lkeaydnglp llphtlcaai idrerlalgt eeglfvihlh sndifqvgdc rrvqrltvss
     1141 aagllvvlcg rgpsvrlftl selenaevag akipesrgcq alvagsilqa rtpvlcvavk
     1201 rqvlcyqlgp gpgpwqrrir elqapapvqs lgllgdrlcv gaagtfalyp llneaaplal
     1261 gtglvaeelp asrgglgeal gavelslsel lllfatagvy vdgagrksrs hellwpvapt
     1321 gwgytapylt vfsensidvf dvrraewvqt vplkkvrpln pegslllygt ekvrltylrn
     1381 plaekdefdi pdltdnsrrq lfrtkskrrf ffrvsdelrq qqrremlkdp fvrskfispp
     1441 tnfnhlvhvg ptegrpgprd gtraqeqksr gtrssgpqrp hsfsealrrp vsmgndglpg
     1501 etdplvkrkv wtslssesvs cpqgslspaa sliqvserpr slppdpeseg sp
//
LOCUS       NP_001424432            1299 aa            linear   ROD 08-APR-2025
DEFINITION  zinc finger protein 532 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424432 XP_006254927
VERSION     NP_001424432.1
DBSOURCE    REFSEQ: accession NM_001437503.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254927.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360172.2764272.1, SRR26360194.224558.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1299
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..1299
                     /product="zinc finger protein 532 isoform 1"
                     /calculated_mol_wt=140869
     Region          753..772
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(758,760,762,764..765,768..769,787,789,793..794,
                     797..798,801,816,818,820..821,824..825)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          781..816
                     /region_name="zf-RING_7"
                     /note="C4-type zinc ribbon domain; pfam02591"
                     /db_xref="CDD:426857"
     Region          782..802
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          810..826
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          841..858
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          869..890
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          904..924
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1024..1044
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1029,1031,1033,1035..1036,1039..1040,1043,1059,1061,
                     1065..1066,1069..1070,1073,1092,1094,1096,1098..1099,
                     1102..1103)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1054..1075
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1084..1104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1174..1194
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1179,1181,1183,1185..1186,1189..1190,1193,1208,1210,
                     1214..1215,1218..1219,1223,1269,1271,1273,1275..1276,
                     1279..1280,1283)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1199..1225
                     /region_name="zf-C2H2_11"
                     /note="zinc-finger C2H2-type; pfam16622"
                     /db_xref="CDD:465205"
     Region          1203..1224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1263..1284
                     /region_name="zf-C2H2_6"
                     /note="C2H2-type zinc finger; pfam13912"
                     /db_xref="CDD:433576"
     Region          1264..1284
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1299
                     /gene="Zfp532"
                     /gene_synonym="Znf532"
                     /coded_by="NM_001437503.1:476..4375"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307362"
                     /db_xref="RGD:1311719"
ORIGIN      
        1 mtmgdmktpd fddllaafdi pdmvdpkaai esghddhesh ikqnahvddd shtpsssdvg
       61 vsvivknvrn idssegvekd ghnptgnglh ngfltassld sygkdgaksl kgdtpasevt
      121 lkdpafsqfs pissaeefed dekievddpp dkeetranfr snvltgsapq qdfdklkalg
      181 gentsktgvs asghadknkv kreaesnsit lsvyepfkvr kaedklkens ekmlesrvld
      241 gkpssekndp aiaaatsskt ksssklssci aaiaalsakk aasdsckepv ansreasplp
      301 kevndspkaa dkspesqnli dgtkkaslkp sdsprsvsse nsskgspssp vgstpaipkv
      361 riktiktssg eikrtvtrvl pevdldsgkk pseqaasvma svtsllsssa saavlssppr
      421 aplptamvts avssaeltpk qvtikpvata flpvsavkta gsqvinlkla nnttvkatvi
      481 saasvqsass aiikaanaiq qqtvvvpass lanaklvpkt vhlanlnllp qgaqatselr
      541 qvltkpqqqi kqailnaaaa qppkkvsrvq vvsslqssvv eafnkvlssv npvpvyipnl
      601 sppasagitl pmrgykclec gdsfaleksl sqhydrrsvr ievtcnhctk nlvfynkcsl
      661 lsharghkek gvvmqcshli lkpvpadqmi vspssntaas tlpssvgaat htvakvqpgl
      721 tgavisapps tpispampld edpsklcrhs lkclecnevf qdetslathf qhaadtcgqk
      781 tctvcqmllp nqcsyashqr ihqhkspytc pecgaicrsv hfqshvtknc lhytrrvgfr
      841 cvhcnvvysd vaalkshiqg shcevfykcp icpmafksap sthshaytqh pgvkigepki
      901 iykcsmcdtv ftlqtllyrh fdqhidnqkv svfkcpdcsl lyaqkqlmmd hiksmhgtlk
      961 siegppnlgi nlplsskpat qnsanhsred aksmngkekl ekkspspakk steskkmasl
     1021 gwtcwecdrl ftqrdvylsh mrkehgkqmk khpcrqcdks fssshslcrh nrikhkgirk
     1081 vyacshcpds rrtftkrlml ekhiqlmhgi kdpdvkelsd evtneeevei kedakvpspk
     1141 rkleepvlef rpprgaitqp lkklkinvfk vhkcavcgft tenllqfheh ipqhksdgss
     1201 yqcrecglcy tshvslsrhl fivhklkepq pvskqngage dsqqenkpsp edeaaegavs
     1261 drkckvcakt feteaalnth mrthgmafik skrmssaek
//
LOCUS       NP_001424173             122 aa            linear   ROD 08-APR-2025
DEFINITION  U7 snRNA-associated Sm-like protein LSm10 [Rattus norvegicus].
ACCESSION   NP_001424173 XP_006238957
VERSION     NP_001424173.1
DBSOURCE    REFSEQ: accession NM_001437244.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Yang,X.C., Torres,M.P., Marzluff,W.F. and Dominski,Z.
  TITLE     Three proteins of the U7-specific Sm ring function as the molecular
            ruler to determine the site of 3'-end processing in mammalian
            histone pre-mRNA
  JOURNAL   Mol Cell Biol 29 (15), 4045-4056 (2009)
   PUBMED   19470752
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Wagner,E.J. and Marzluff,W.F.
  TITLE     ZFP100, a component of the active U7 snRNP limiting for histone
            pre-mRNA processing, is required for entry into S phase
  JOURNAL   Mol Cell Biol 26 (17), 6702-6712 (2006)
   PUBMED   16914750
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Pillai,R.S., Will,C.L., Luhrmann,R., Schumperli,D. and Muller,B.
  TITLE     Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain
            Lsm10, a new 14 kDa Sm D1-like protein
  JOURNAL   EMBO J 20 (19), 5470-5479 (2001)
   PUBMED   11574479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006238957.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166902.1, FM099348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..122
                     /product="U7 snRNA-associated Sm-like protein LSm10"
                     /note="U7 snRNP-specific Sm-like protein LSM10"
                     /calculated_mol_wt=13749
     Region          8..85
                     /region_name="LSm10"
                     /note="Like-Sm protein 10; cd01733"
                     /db_xref="CDD:212480"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212480"
     Site            order(47,49,75)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212480"
     Site            71..82
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212480"
     CDS             1..122
                     /gene="Lsm10"
                     /coded_by="NM_001437244.1:174..542"
                     /db_xref="GeneID:366468"
                     /db_xref="RGD:1584914"
ORIGIN      
        1 malshsvker tisensliil lqglqgqitt vdlrdesvar gridnvdafm nirlanvtyt
       61 drwghqveld dlfvtgrnvr yvhipdgvni tatieqqlqi ihrvrnfggk gqgrrefpsk
      121 rp
//
LOCUS       NP_001424327             717 aa            linear   ROD 08-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM36 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424327 XP_006254748
VERSION     NP_001424327.1
DBSOURCE    REFSEQ: accession NM_001437398.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Singh,N., Kumble Bhat,V., Tiwari,A., Kodaganur,S.G.,
            Tontanahal,S.J., Sarda,A., Malini,K.V. and Kumar,A.
  TITLE     A homozygous mutation in TRIM36 causes autosomal recessive
            anencephaly in an Indian family
  JOURNAL   Hum Mol Genet 26 (6), 1104-1114 (2017)
   PUBMED   28087737
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Miyajima,N., Maruyama,S., Nonomura,K. and Hatakeyama,S.
  TITLE     TRIM36 interacts with the kinetochore protein CENP-H and delays
            cell cycle progression
  JOURNAL   Biochem Biophys Res Commun 381 (3), 383-387 (2009)
   PUBMED   19232519
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Kitamura,K., Tanaka,H. and Nishimune,Y.
  TITLE     Haprin, a novel haploid germ cell-specific RING finger protein
            involved in the acrosome reaction
  JOURNAL   J Biol Chem 278 (45), 44417-44423 (2003)
   PUBMED   12917430
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254748.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.50055.1,
                                           SRR26643288.59442.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..717
                     /product="E3 ubiquitin-protein ligase TRIM36 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 36; E3 ubiquitin-protein
                     ligase TRIM36"
                     /calculated_mol_wt=81342
     Region          16..113
                     /region_name="RING-HC_TRIM36_C-I"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd16756"
                     /db_xref="CDD:438414"
     Region          139..193
                     /region_name="Bbox1_TRIM36_C-I"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19848"
                     /db_xref="CDD:380906"
     Region          198..242
                     /region_name="Bbox2_TRIM36_C-I"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 36 (TRIM36) and similar proteins;
                     cd19778"
                     /db_xref="CDD:380836"
     Region          244..368
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          347..395
                     /region_name="COS"
                     /note="TRIM C-terminal subgroup One Signature domain;
                     pfam18568"
                     /db_xref="CDD:465805"
     Region          419..482
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          504..707
                     /region_name="SPRY_PRY_TRIM36"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 36 (TRIM36); cd12894"
                     /db_xref="CDD:293951"
     CDS             1..717
                     /gene="Trim36"
                     /coded_by="NM_001437398.1:278..2431"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:291597"
                     /db_xref="RGD:1308714"
ORIGIN      
        1 megdasdsqv tikniekeli cpackelfth plilpcqhsv chkcvkelll slddsfndva
       61 sdssnqsspr lrltspsmdk idkinrpgwk rnsltprptm fpcpgcehdv dlgergvsgl
      121 frnftletiv eryrqaaraa taimcdlckp ppqestkscm dcsasycnec fkiyhpwgtv
      181 kaqheyvgpt tnfrpkilmc peheterinm ycelcrrpvc hlcklggnhs nhrvttmssa
      241 yktlkeklsk didfligkes qvksqiseln llmketecng erakeealah feklfeiled
      301 rkssvlkaid askklrldkf htqmeeyqgl lennglvgya qevlketdqs cfvqtakqlh
      361 lriqkatesl ksfrpaaqas fedyvvnisk qtevlgelsf fssgidipei neeqskvynn
      421 alidwhhpek dkadsyvley rkinrdeemi swneievhgt skvvsnlesn spyafrvray
      481 rgsicspcsr elvlhtppap vfsflfdekc gyntehllln lkrdrvesra gfnvllaaer
      541 iqvghytsld yiigdvgitk gkhfwacrve pysylvkvgv assdklqewl rsprdaaspr
      601 yeqdsghdsg sedayfdssq pftlvtigmk kffipkspts snepenrvlp mptsigifld
      661 cdkgkvsfyd mdhmkclyer qvdcshtmyp afalmgsggi qleetitaky leyeedv
//
LOCUS       NP_001424393             210 aa            linear   ROD 08-APR-2025
DEFINITION  uncharacterized protein MISP3 [Rattus norvegicus].
ACCESSION   NP_001424393 XP_006255311
VERSION     NP_001424393.1
DBSOURCE    REFSEQ: accession NM_001437464.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006255311.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.35838.1,
                                           SRR26643288.60977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..210
                     /product="uncharacterized protein MISP3"
                     /calculated_mol_wt=23359
     Region          37..200
                     /region_name="AKAP2_C"
                     /note="A-kinase anchor protein 2 C-terminus; pfam15304"
                     /db_xref="CDD:464630"
     CDS             1..210
                     /gene="Misp3"
                     /gene_synonym="RGD1310262"
                     /coded_by="NM_001437464.1:1879..2511"
                     /db_xref="GeneID:304650"
                     /db_xref="RGD:1310262"
ORIGIN      
        1 metpiqreir rscereeslr rsrglspgra geelielrvr pvlsrpgsgi plpralerar
       61 agakmqrdie reahrqaala spavpepsar prpqpldelk rffeaaaedg aslqrqpeag
      121 grlhpalqdg cpvlgqlppl vapslleqev lrvrererel qlqrrsiyga aedrepapsl
      181 tqsrgdgkla vtwpprrqas englekerrp
//
LOCUS       NP_001424480            1637 aa            linear   ROD 08-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma
            coactivator-related protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424480 XP_006231515
VERSION     NP_001424480.1
DBSOURCE    REFSEQ: accession NM_001437551.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1637)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006231515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.5552.1,
                                           SRR26643429.5846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1637
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1637
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1 isoform 3"
                     /note="peroxisome proliferator-activated receptor gamma
                     coactivator-related protein 1; peroxisome proliferative
                     activated receptor, gamma, coactivator-related 1;
                     peroxisome proliferator-activated receptor gamma,
                     coactivator-related 1"
                     /calculated_mol_wt=174785
     Region          <378..843
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <630..1115
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <977..1360
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1514..1604
                     /region_name="RRM_PRC"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator-related
                     protein 1 (PRC) and similar proteins; cd12624"
                     /db_xref="CDD:410035"
     CDS             1..1637
                     /gene="Pprc1"
                     /coded_by="NM_001437551.1:30..4943"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:294007"
                     /db_xref="RGD:1309688"
ORIGIN      
        1 maarrgrrdr vappptggpg pdpgggvrgg gwasrsqaph gtvgsvspae qvheegddss
       61 fvslsrlgps lrekdlemee lilqdetlle tmqnymdasl isliedfges rlsledqnem
      121 slltalteil dnadsenlsp fdtipdsell vspressslh kllnlsrtpp erdripamdp
      181 lgpsagssrv sgvemslads pwdfspppfl etsspklpsw rssrprprws qspppqqrsd
      241 geeeeevagf sgqmldgeld nsvntldfpm hlacpeeedk sgaanvavsa pgdesissls
      301 elvramhpyc lpnltqlasl daelqeqadd ltlpegcvvl eivgqaatag ddleipvvvr
      361 qipsgsqsvl ldgsvgtdpa lqllmpamep gtedgvpkva pcpdqelpls saclleprdi
      421 meslapkepr nlpanasegs qrvprkgrkk kkkeqptacl egctrrlrss srgqstvate
      481 vnsqagnlqk qpqeelqret aapqsrgkpr awarawaaal ektgsedped qnagqdspae
      541 edvlelrpkl vetsqadptl slndsarads ipvnsvegds tavdtavpvd qassctelvg
      601 slsggpilss pvlddrtgve pavaiptsnh lspadailan pgtadpapng lapgdpvlvk
      661 crptdprraa aaataaqgpr pslepsdhpk vitpevkdag gplkvegsts attqearprp
      721 lslseyrqrr rqrqieaedr nsqppagkwp slpetpkgla dipclvpsap tkktapqrsp
      781 iavpetcsvs vgsnpvsptp epsasklmvs thseqvsshe mplpvrlppp tlqsmapagp
      841 tpstvptplp fppslppllp lpasgpgvps lpppplqppg lpvsmrqmpp dpytqyapvp
      901 pwpcypsvsp sgysclpppp ampivsgtpg tyavpptcnv pwvpppapvs pyssssaygs
      961 lgwgpglqqp pfwstvsppp lssastgrav pppsvepsns sagppedtlp vpvtpslssr
     1021 paspiappae ptkleaqpvp vspqpkhkvs pvvqspqikv lptlsaegva igeseserlk
     1081 petqenrpre kpistatkav llpkqstvak lpavhparlr rlsflptpra qgsedvvqaf
     1141 iseigieasd lsslleqfek seakkecplp apadsvavgn sgidtpqekk pldrlhapel
     1201 anvagltppa tpphqlwkpl aavsllakak spkstaqegt lkpegiteak ppaaaclqeg
     1261 vrgpspvhvg sgdhdycvrs rtppkkmpal visemgsrwn vkrhqditik pvlslgsaap
     1321 plpctttsqe pldhrtsseq adpsapcfap stllspeasp crnemntrtp seppdkqrsm
     1381 rcyrkacrsa sppsrgwqgr rgrssrsvss gssrtseass sssvssssrs rsrslsppnk
     1441 rwrrsscsss grsrrcssss ssssssssss ssrsrspsvs pcrrsdrrrr yssyrsndhy
     1501 qrqrvlqker aieerrvvfi gkipgrmtrs elkqrfsvfg eieectihfr vqgdnygfvt
     1561 yryaeeafaa iesghklrqa deqpfdlcfg grrqfckrsy sdldsnredf dpapvkskfd
     1621 sldfdtllkq aqknlrr
//
LOCUS       NP_001424354             595 aa            linear   ROD 08-APR-2025
DEFINITION  inactive serine/threonine-protein kinase PLK5 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424354 XP_006240984
VERSION     NP_001424354.1
DBSOURCE    REFSEQ: accession NM_001437425.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   de Carcer,G., Escobar,B., Higuero,A.M., Garcia,L., Anson,A.,
            Perez,G., Mollejo,M., Manning,G., Melendez,B., Abad-Rodriguez,J.
            and Malumbres,M.
  TITLE     Plk5, a polo box domain-only protein with specific roles in neuron
            differentiation and glioblastoma suppression
  JOURNAL   Mol Cell Biol 31 (6), 1225-1239 (2011)
   PUBMED   21245385
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Andrysik,Z., Bernstein,W.Z., Deng,L., Myer,D.L., Li,Y.Q.,
            Tischfield,J.A., Stambrook,P.J. and Bahassi el,M.
  TITLE     The novel mouse Polo-like kinase 5 responds to DNA damage and
            localizes in the nucleolus
  JOURNAL   Nucleic Acids Res 38 (9), 2931-2943 (2010)
   PUBMED   20100802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006240984.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38033.1,
                                           SRR26643294.27580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..595
                     /product="inactive serine/threonine-protein kinase PLK5
                     isoform 2"
                     /EC_number="2.7.11.21"
                     /note="polo-like kinase 5 pseudogene;
                     serine/threonine-protein kinase PLK5; inactive
                     serine/threonine-protein kinase PLK5"
                     /calculated_mol_wt=65704
     Region          25..279
                     /region_name="STKc_PLK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Polo-like kinases; cd14099"
                     /db_xref="CDD:271001"
     Site            order(33..37,41,54,56,88,104..107,111,113,150,152,
                     154..155,157,168,171,187..190)
                     /site_type="active"
                     /db_xref="CDD:271001"
     Site            order(33..37,41,54,56,88,105..107,157,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271001"
     Site            order(37,111,113,150,152,154,171,187..190)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271001"
     Site            order(167..175,180..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271001"
     Region          410..497
                     /region_name="POLO_box_1"
                     /note="First polo-box domain (PBD) of polo-like kinases
                     Plk1, Plk2, Plk3, and Plk5; cd13118"
                     /db_xref="CDD:240561"
     Site            order(416..419,488,490..494)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:240561"
     CDS             1..595
                     /gene="Plk5"
                     /gene_synonym="Plk5p"
                     /coded_by="NM_001437425.1:79..1866"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314627"
                     /db_xref="RGD:1305038"
ORIGIN      
        1 meprlrrrrs rqlvatflrd pgsgrvyrrg kligkgafsr cykltdmsts avfalkvvpr
       61 ggagrlrlrg kvereialhs rlhhrnivaf hahfadrdhv ymvleycsrq slahvlkvrr
      121 tltepevryy frglvsglry lhqqrivhrd lkpsnfflnk nmevkigdlg laarvgpagr
      181 chrvlcgtpn fqapevvsrn ghsaksdiwa lgcimytvlt gtppfaaapl semyqnirdg
      241 hyleptqlsp sarsliarll apdpderpsl dhllqddffs qgftperlpp hschsppvfa
      301 fppplgrlfr kvgqllltqc rppcpftske asgpgeeste pdhmeasnee gaplctesri
      361 hlltlgtprt dpadakgtla lqlevatrkl clcldagpva gqdppgeqrs vlwapkwvdy
      421 slkygfgyql sdggsgvlfr dgshmalrpp gghvsyqpdq gtlwifalrd vpgplrakla
      481 vlrlfacymq rrlreegtap mtatpaspdf cllsftadaq alamlfsngt vqvssktspv
      541 qlvlsgeged flltiqepgg psmgtsytld vlrshgisla vrhhlrlglh llqsv
//
LOCUS       NP_001099818             116 aa            linear   ROD 08-APR-2025
DEFINITION  melanoma antigen recognized by T-cells 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001099818 XP_001079637 XP_215234
VERSION     NP_001099818.1
DBSOURCE    REFSEQ: accession NM_001106348.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Hoashi,T., Watabe,H., Muller,J., Yamaguchi,Y., Vieira,W.D. and
            Hearing,V.J.
  TITLE     MART-1 is required for the function of the melanosomal matrix
            protein PMEL17/GP100 and the maturation of melanosomes
  JOURNAL   J Biol Chem 280 (14), 14006-14016 (2005)
   PUBMED   15695812
REFERENCE   2  (residues 1 to 116)
  AUTHORS   De Maziere,A.M., Muehlethaler,K., van Donselaar,E., Salvi,S.,
            Davoust,J., Cerottini,J.C., Levy,F., Slot,J.W. and Rimoldi,D.
  TITLE     The melanocytic protein Melan-A/MART-1 has a subcellular
            localization distinct from typical melanosomal proteins
  JOURNAL   Traffic 3 (9), 678-693 (2002)
   PUBMED   12191019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215234.1, XP_001079637.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO783755.1, BG378791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..116
                     /product="melanoma antigen recognized by T-cells 1 isoform
                     1"
                     /note="melanoma antigen recognized by T-cells 1"
                     /calculated_mol_wt=12878
     Region          2..116
                     /region_name="MLANA"
                     /note="Protein melan-A; pfam14991"
                     /db_xref="CDD:464426"
     CDS             1..116
                     /gene="Mlana"
                     /coded_by="NM_001106348.2:56..406"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293890"
                     /db_xref="RGD:1306525"
ORIGIN      
        1 mpreevhfgy prkghshsyi taeeaagigi lvvalgiall igcwycrrrs gyraltdkrr
       61 hagtqntsre rclcesldhq dsrlssqekn hqpvvpnapp ayeklssdhs pppysp
//
LOCUS       NP_001424339             407 aa            linear   ROD 08-APR-2025
DEFINITION  putative short transient receptor potential channel 2-like protein
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424339 XP_006229966
VERSION     NP_001424339.1
DBSOURCE    REFSEQ: accession NM_001437410.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229966.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.871264.1,
                                           SRR26360194.979097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..407
                     /product="putative short transient receptor potential
                     channel 2-like protein isoform 1"
                     /note="short transient receptor potential channel 2-like"
                     /calculated_mol_wt=44228
     Region          1..150
                     /region_name="XRCC1_N"
                     /note="XRCC1 N terminal domain; pfam01834"
                     /db_xref="CDD:460356"
     CDS             1..407
                     /gene="Xndc1"
                     /coded_by="NM_001437410.1:566..1789"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:102549471"
                     /db_xref="RGD:7692537"
ORIGIN      
        1 mapvkishvv sfssqdpkyp venllnpdsh kgpwlscprd ktgqlkvefq leravpisyi
       61 dvgncgcafl qidvgrsswp ldrpfvtllp atmlmsltds kegknrsgvr mfkdddflip
      121 asgeswdrlr ltcsqpftrh qsfglaflrv rssldslsdp vkdpsspgss glnqnssdkl
      181 esdpspwltn psirrtffpd pqtstkeisa lkgmlkqlqp gplgraarmv lsaahkappa
      241 svvspnnshg epdsshpera epraeepnrk nnasrgkrrk vqeqrrplss sssqpnrrat
      301 grtkqrqqrp qaksdgsgvq atgqcpictg sfsiealprh aatcgesspp qpasptslss
      361 sesvlwvssp esspppsswv qcpicelqfs areieehasv cgevfpa
//
LOCUS       NP_001424096             285 aa            linear   ROD 08-APR-2025
DEFINITION  maestro isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424096
VERSION     NP_001424096.1
DBSOURCE    REFSEQ: accession NM_001437167.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Smith,L., Van Hateren,N., Willan,J., Romero,R., Blanco,G.,
            Siggers,P., Walsh,J., Banerjee,R., Denny,P., Ponting,C. and
            Greenfield,A.
  TITLE     Candidate testis-determining gene, Maestro (Mro), encodes a novel
            HEAT repeat protein
  JOURNAL   Dev Dyn 227 (4), 600-607 (2003)
   PUBMED   12889070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2603675.1,
                                           SRR26643287.35234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..285
                     /product="maestro isoform 2"
                     /note="protein maestro"
                     /calculated_mol_wt=32662
     Region          86..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          90..237
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          126..161
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          170..195
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..285
                     /gene="Mro"
                     /gene_synonym="AABR07032520.1; RGD1559803"
                     /coded_by="NM_001437167.1:406..1263"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:361348"
                     /db_xref="RGD:1559803"
ORIGIN      
        1 mcsktkmtek tnphpplrpt esaalmrgcl rglesvsfme qmqripnqpl ptpasqskkr
       61 rtplssffsk vswklrlqkr eplknlffvl aerargpnpr krhlamrglg ilaheapdkv
      121 rkykkvmldl lvhglydpvs sevihesvkt ltimlgkiqg qrlgsffidi tlqtrtlldd
      181 eddsvrysaf vlfgqlaafa grkwkkffth qvnqtqdsll shlqdespqv akactmavqa
      241 cvpylkprke qsfqseedqk nrrlsqqlsh yhpeillffy ankil
//
LOCUS       NP_001424370             480 aa            linear   ROD 08-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNG2 [Rattus
            norvegicus].
ACCESSION   NP_001424370 XP_006255009
VERSION     NP_001424370.1
DBSOURCE    REFSEQ: accession NM_001437441.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhu,X.R., Netzer,R., Bohlke,K., Liu,Q. and Pongs,O.
  TITLE     Structural and functional characterization of Kv6.2 a new
            gamma-subunit of voltage-gated potassium channel
  JOURNAL   Recept Channels 6 (5), 337-350 (1999)
   PUBMED   10551266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006255009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.54839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN11044071 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..480
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNG2"
                     /note="cardiac potassium channel subunit (Kv6.2);
                     voltage-gated potassium channel subunit Kv6.2; potassium
                     voltage-gated channel, subfamily G, member 2; potassium
                     channel, voltage gated modifier subfamily G, member 2"
                     /calculated_mol_wt=52405
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          33..127
                     /region_name="BTB_POZ_Kv6_KCNG"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in KCNG/Kv6
                     subfamily of potassium voltage-gated channels; cd18382"
                     /db_xref="CDD:349691"
     Site            order(36,38..45,48,84,86..87,90,93,97,100,103,105,
                     113..114,117)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349691"
     Region          144..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            188..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          190..429
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            231..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            333..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          382..387
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Site            397..425
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     Region          429..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU3.1)"
     CDS             1..480
                     /gene="Kcng2"
                     /gene_synonym="Kv6.2"
                     /coded_by="NM_001437441.1:132..1574"
                     /db_xref="GeneID:307234"
                     /db_xref="RGD:1309521"
ORIGIN      
        1 marlpghpev pgaepgsavr ggrggrgara rhviinvggc rvrlawaala rcplarlerl
       61 racrghdell rvcddydvsr defffdrspc afraivallr agklrllrgp calafrdela
      121 ywgidearle rcclrrlrrr eeeaaearat ppargpqtsp gralgsgrle rgrrrlrdvv
      181 enphsglagk lfayvsvafv avtavglcls tmpdvraeee rgecstkcrn lfvletvcva
      241 wfsfefllrs lqaeskcafl rtplaiidil ailpfyvsll aglaagptgs kmleraglvl
      301 rllralrvly vmrlarhslg lrslgltvrr carefgllll flcvamalfa plvhlaerel
      361 gahrdfssvp asywwavism ttvgygdmvp rslpgqvval ssilsgillm afpvtsifht
      421 fsrsyselke qqqraaspep vlredstrdd strsasated ssqdpetaga agslpgpvgp
//
LOCUS       NP_001424300             632 aa            linear   ROD 08-APR-2025
DEFINITION  methyl-CpG-binding domain protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424300 XP_006254971
VERSION     NP_001424300.1
DBSOURCE    REFSEQ: accession NM_001437371.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Dick,A.L.W., Zhao,Q., Crossin,R., Baker-Andresen,D., Li,X.,
            Edson,J., Roeh,S., Marshall,V., Bredy,T.W., Lawrence,A.J. and
            Duncan,J.R.
  TITLE     Adolescent chronic intermittent toluene inhalation dynamically
            regulates the transcriptome and neuronal methylome within the rat
            medial prefrontal cortex
  JOURNAL   Addict Biol 26 (3), e12937 (2021)
   PUBMED   32638524
  REMARK    GeneRIF: Adolescent chronic intermittent toluene inhalation
            dynamically regulates the transcriptome and neuronal methylome
            within the rat medial prefrontal cortex.
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Tang,W.Y., Morey,L.M., Cheung,Y.Y., Birch,L., Prins,G.S. and
            Ho,S.M.
  TITLE     Neonatal exposure to estradiol/bisphenol A alters promoter
            methylation and expression of Nsbp1 and Hpcal1 genes and
            transcriptional programs of Dnmt3a/b and Mbd2/4 in the rat prostate
            gland throughout life
  JOURNAL   Endocrinology 153 (1), 42-55 (2012)
   PUBMED   22109888
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Jung,B.P., Zhang,G., Ho,W., Francis,J. and Eubanks,J.H.
  TITLE     Transient forebrain ischemia alters the mRNA expression of methyl
            DNA-binding factors in the adult rat hippocampus
  JOURNAL   Neuroscience 115 (2), 515-524 (2002)
   PUBMED   12421618
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Francis,J., Jung,B., Zhang,G., Cheng,J., Ho,W., Burnham,W.M. and
            Eubanks,J.H.
  TITLE     Kindling induces the mRNA expression of methyl DNA-binding factors
            in the adult rat hippocampus
  JOURNAL   Neuroscience 113 (1), 79-87 (2002)
   PUBMED   12123686
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Ohki,I., Shimotake,N., Fujita,N., Jee,J., Ikegami,T., Nakao,M. and
            Shirakawa,M.
  TITLE     Solution structure of the methyl-CpG binding domain of human MBD1
            in complex with methylated DNA
  JOURNAL   Cell 105 (4), 487-497 (2001)
   PUBMED   11371345
  REMARK    Erratum:[Cell 2001 Jun 15;105(6):815]
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254971.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.51931.1,
                                           SRR26643285.52684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..632
                     /product="methyl-CpG-binding domain protein 1 isoform 1"
                     /calculated_mol_wt=69750
     Region          5..66
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Region          186..233
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          235..280
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          347..393
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     CDS             1..632
                     /gene="Mbd1"
                     /coded_by="NM_001437371.1:162..2060"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:291439"
                     /db_xref="RGD:1305980"
ORIGIN      
        1 maeawqdcpa lgpgwkrrea frksgascgr sdiyyrsptg ekirskielt rylgpacdlt
       61 lfdfrqgilc hpvpkthpla vpskkkkkts kpakakkqqv gpqrsevrke tpregnkvap
      121 atallpvtas apapvpvpvs apapapaplc cencgihlsw dgikrerrrt lckdcraqri
      181 afnreqrmfk rvgcgectac lvkedcgvcs icclqlpndv asglfckceq rrclrivekn
      241 rgcgvcrgcq tqedcghcri clrfprpglk rqwrclqrrc fwgkydhskr gprvasrrhs
      301 rapplpphaa sqhpeptelh isdqtptapa efvydcveed elqpytnqrq nrkcgacaac
      361 lrrmdcghcd fccdkpkfgg snqkrqkcrw rqclqfamkr llpsigpgse eearllphht
      421 hqkrsastrq lqlssplkap lavvttppgp vqdsgkrqag sgfvlpqpdt dlvylqegts
      481 slmqvpgpaa astenpaqet qgsapgwvva lpqvkqekad apeewtavtt fltsstvqpg
      541 flskasgldp ppvkreppgp eedgeenked dvsesapaee iggigtpvit eifslggtrl
      601 rdaeawlprl hkllavnene yftelqlkee il
//
LOCUS       NP_001424202            1044 aa            linear   ROD 08-APR-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            delta isoform isoform a [Rattus norvegicus].
ACCESSION   NP_001424202 XP_038966431
VERSION     NP_001424202.1
DBSOURCE    REFSEQ: accession NM_001437273.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Chang,R., Su,Y., Kong,H., Wang,F., Xing,Y., Jiang,L. and Xin,H.
  TITLE     Upregulation of SEMP1 Contributes to Improving the Biological
            Functions of Trophoblast via the PI3K/AKT Pathway in Preeclampsia
  JOURNAL   Mol Biotechnol 66 (3), 531-543 (2024)
   PUBMED   37277581
  REMARK    GeneRIF: Upregulation of SEMP1 Contributes to Improving the
            Biological Functions of Trophoblast via the PI3K/AKT Pathway in
            Preeclampsia.
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Wang,F., Fan,X., Kong,J., Wang,C., Ma,B., Sun,W., Ye,Z., Liu,P. and
            Wen,J.
  TITLE     Inhibition of mitochondrial fission alters neo-intimal hyperplasia
            via PI3K/Akt signaling in arteriovenous fistulas
  JOURNAL   Vascular 31 (3), 533-543 (2023)
   PUBMED   35130772
  REMARK    GeneRIF: Inhibition of mitochondrial fission alters neo-intimal
            hyperplasia via PI3K/Akt signaling in arteriovenous fistulas.
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Stark,A.K., Chandra,A., Chakraborty,K., Alam,R., Carbonaro,V.,
            Clark,J., Sriskantharajah,S., Bradley,G., Richter,A.G.,
            Banham-Hall,E., Clatworthy,M.R., Nejentsev,S., Hamblin,J.N.,
            Hessel,E.M., Condliffe,A.M. and Okkenhaug,K.
  TITLE     PI3Kdelta hyper-activation promotes development of B cells that
            exacerbate Streptococcus pneumoniae infection in an
            antibody-independent manner
  JOURNAL   Nat Commun 9 (1), 3174 (2018)
   PUBMED   30093657
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1044)
  AUTHORS   Qiao,S., Zheng,N., Sun,L., Pang,G., Wang,S., Jia,P., Uzonna,J.E.,
            Bai,H. and Yang,X.
  TITLE     The p110delta isoforme of phosphatidylinositol 3-kinase plays an
            important role in host defense against chlamydial lung infection
            through influencing CD4+ T-cell function
  JOURNAL   Pathog Dis 76 (6), 5035814 (2018)
   PUBMED   29893841
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1044)
  AUTHORS   Chen,J., Cui,X., Li,L., Qu,J., Raj,J.U. and Gou,D.
  TITLE     MiR-339 inhibits proliferation of pulmonary artery smooth muscle
            cell by targeting FGF signaling
  JOURNAL   Physiol Rep 5 (18) (2017)
   PUBMED   28947594
REFERENCE   6  (residues 1 to 1044)
  AUTHORS   Luk,S.K., Piekorz,R.P., Nurnberg,B. and Tony To,S.S.
  TITLE     The catalytic phosphoinositol 3-kinase isoform p110delta is
            required for glioma cell migration and invasion
  JOURNAL   Eur J Cancer 48 (1), 149-157 (2012)
   PUBMED   22079609
REFERENCE   7  (residues 1 to 1044)
  AUTHORS   Urick,M.E., Rudd,M.L., Godwin,A.K., Sgroi,D., Merino,M. and
            Bell,D.W.
  TITLE     PIK3R1 (p85alpha) is somatically mutated at high frequency in
            primary endometrial cancer
  JOURNAL   Cancer Res 71 (12), 4061-4067 (2011)
   PUBMED   21478295
REFERENCE   8  (residues 1 to 1044)
  AUTHORS   Randis,T.M., Puri,K.D., Zhou,H. and Diacovo,T.G.
  TITLE     Role of PI3Kdelta and PI3Kgamma in inflammatory arthritis and
            tissue localization of neutrophils
  JOURNAL   Eur J Immunol 38 (5), 1215-1224 (2008)
   PUBMED   18412166
REFERENCE   9  (residues 1 to 1044)
  AUTHORS   Hirsch,E., Costa,C. and Ciraolo,E.
  TITLE     Phosphoinositide 3-kinases as a common platform for multi-hormone
            signaling
  JOURNAL   J Endocrinol 194 (2), 243-256 (2007)
   PUBMED   17641274
  REMARK    Review article
REFERENCE   10 (residues 1 to 1044)
  AUTHORS   Clayton,E., Bardi,G., Bell,S.E., Chantry,D., Downes,C.P., Gray,A.,
            Humphries,L.A., Rawlings,D., Reynolds,H., Vigorito,E. and Turner,M.
  TITLE     A crucial role for the p110delta subunit of phosphatidylinositol
            3-kinase in B cell development and activation
  JOURNAL   J Exp Med 196 (6), 753-763 (2002)
   PUBMED   12235209
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038966431.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.21987.1,
                                           SRR26643284.8348.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1044
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit delta isoform isoform a"
                     /EC_number="2.7.1.153"
                     /note="catalytic phosphatidylinositol 3-kinase delta;
                     phosphatidylinositol 3-kinase catalytic delta polypeptide;
                     phosphoinositide-3-kinase, catalytic, delta polypeptide"
                     /calculated_mol_wt=119762
     Region          34..107
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; pfam02192"
                     /db_xref="CDD:460483"
     Region          182..281
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          314..481
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Region          504..684
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); smart00145"
                     /db_xref="CDD:214537"
     Region          676..1042
                     /region_name="PI3Kc_IA_delta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase delta; cd05174"
                     /db_xref="CDD:270718"
     Site            order(752,754..756,758,760,777,779,782,813,825..828,833,
                     836,898,900,910..911)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270718"
     Site            order(820..821,922..923,925,927,993,996)
                     /site_type="other"
                     /note="putative regulatory subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:270718"
     Site            867
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270718"
     Site            890..898
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270718"
     Site            911..935
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270718"
     CDS             1..1044
                     /gene="Pik3cd"
                     /coded_by="NM_001437273.1:204..3338"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:366508"
                     /db_xref="RGD:1310990"
ORIGIN      
        1 mppgvdcpme fwtkeesqsv avdfllptgv ylnfpvsrna nlstikqvlw hraqyepffh
       61 mlsdpeayvf tcvnqtaeqq eledeqrrlc diqpflpvlr lvaregdrvk klinsqisll
      121 igkglhefds lrdpevndfr tkmrqfceea aahrqqlgwv ewlqysfplq lepsargwra
      181 gllhvsnrpl lvnvkfegse esftfqvstk dmplalmaca lrkkatvfrq plverpeeya
      241 lqvngrheyl ygsyplchfq yicsclhsgl tphltmvhss silamrdeqs npapqvqkpr
      301 vkpppipakk pssvslwsle qpfcielieg rkvnadermk lvvqaglfhg nemlcktvss
      361 sevnvcsepv wkqrlefdis icdlprmarl cfalyavvek akkarstkkk skkadcpiaw
      421 anlmlfdykd qlktgercly mwpsvpdekg elmnpagtvr gnpntesaaa lviylpevap
      481 hpvyfpalek ilelgrhger griteeeqlq lreilerrgs gelyehekdl vwkmrhevqe
      541 hfpealarll lvtkwnkhed vaqmlyllcs wpelpvlsal elldfsfpdc yvgsfaiksl
      601 rkltddelfq yllqlvqvlk yesyldcelt kfllgralan rkighflfwh lrsemhvpsv
      661 alrfglimea ycrgsthhmk vlmkqgeals klkalndfvk assqkttkpq tkemmhmcmr
      721 qetymealsh lqspldpstl leevcveqct fmdskmkplw imyssekagg agsvgiifkn
      781 gddlrqdmlt lqmiqlmdfl wkqegldlrm tpygclptgd rtglievvlh sdtianiqln
      841 ksnmaataaf nkdallnwlk sknpgealdr aieeftlsca gycvatyvlg igdrhsdnim
      901 iresgqlfhi dfghflgnfk tkfginrerv pfiltydfvh viqqgktnns ekferfrgyc
      961 eraytilrrh gllflhlfal mraaglpels cskdiqylkd slalgkteee alkhfrvkfn
     1021 ealreswktk vnwlahnvsk dnrq
//
LOCUS       NP_001424040            1592 aa            linear   ROD 08-APR-2025
DEFINITION  transcription factor Gibbin [Rattus norvegicus].
ACCESSION   NP_001424040 XP_008762374
VERSION     NP_001424040.1
DBSOURCE    REFSEQ: accession NM_001437111.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1592)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 27, 2025 this sequence version replaced XP_008762374.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.20394.1,
                                           SRR26643296.16293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1592
                     /product="transcription factor Gibbin"
                     /note="A.T hook DNA-binding motif-containing protein 1;
                     AT-hook DNA-binding motif-containing protein 1"
                     /calculated_mol_wt=168046
     Region          <590..638
                     /region_name="DUF4683"
                     /note="Domain of unknown function (DUF4683); pfam15735"
                     /db_xref="CDD:464832"
     Region          <856..1047
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1592
                     /gene="Ahdc1"
                     /gene_synonym="RGD1310031"
                     /coded_by="NM_001437111.1:669..5447"
                     /db_xref="GeneID:362617"
                     /db_xref="RGD:1310031"
ORIGIN      
        1 mrvkpqglvv tssavcsspd ylrepkyypg gpptprpllp trppasppdk afsthtfsen
       61 prppprrdps srrppvlakg ddllppraar pvsqahcptp apdnnslrhw dngrvnlhpv
      121 vqlidimkdl trlsqdlqhs gvhldcgglr lsrppapppg dlqysffssp slansirspe
      181 eratphakpe rpnhplyepe peprdspqpg qghgpgatat atglppepep dgpdypelad
      241 adilselasl tcpeaqllea qaleppspqp epqlldpqpr fldpqalepl geglelpplq
      301 pladplglps ltlqaldtlp dslesqlldp qaldplpkll dvpgrrlepq qslghcqlae
      361 plrldlcsph gppgpeghpk yalrrtdrpk ilcrrrkagr grkvdsgpeg rllplpmptg
      421 laaalaeppp lpppppppal sgpvpelepe ssqtpmvptr kgkcrgvrrm vvkmakipvs
      481 lgrrnkttyk vsslssslsv egkelglrvs septpllkmk nngrnvvvvf ppgempiilk
      541 rkrgrppknl llgpgkpkep tvvaaeaaav taatmampev kkrrrrkqkl aspqpsyaad
      601 andskaeysd vlaklaflnr qsqcagrcsp prcwtpsepe svhqapdtqs isqflhrvqg
      661 frrrggktgg fggrggghaa kaarcsfsdf fegigkkkkv vavaatgvvg pgltelghpr
      721 krgrgevdav tgkpkrkrrs rkngtlfpeq vpsgpgfgea gaewagdkgg gwaphhghpg
      781 gqagrncgfq gtearafast glesgasgrg syyagapsgq telsqerqnl ftgyfrslld
      841 sddssdlldf alsasrpesr kasgnyagpp ssalpaqrgl atfpsrgakg spvavgnsga
      901 gtdpsfqpvl psrqtfppgr atsygitpat sdcraaetfp klapppsava rsptthppan
      961 typpqyggyg agqsvfapak pfsgqdcans kdcsfaygsg nslpaspssa hsagyapppt
     1021 ggpclppska sffnsseggp fsgsaptplr cdsrastvsp ggymvpkgtt asaasaasss
     1081 sssfqpspen crqfvgasqw pfrqgyggld waseafsqly npnfdchvse pnvildisny
     1141 tpqkvkqqta vsetfsesss dstqfnqpvg ggfrransea sssegqssls sleklmmdwn
     1201 eassapgynw nqsvlfqsss kpgrgrrkkv dlfeashlgf ststsatasg ypskrstgpr
     1261 qprggrgsga csakkerggt aakakfipkp qpvnplfqds pdlgldyysg dssmsplpsq
     1321 srafgvgerd pcdfmgpysm npstpsdgtf gqgfhcdsps lgapdldskh fpplahpptv
     1381 fdaglqkays ptcsptlgfk eelrpppskl taceplkhgl qgaslshaaq ahlscrdlpl
     1441 gqphyespsc kgtaywyppg saarsppyeg kvgsglladf lgrteavcls aphlasppat
     1501 pkadkeplem trppgpprgp aaatagygcp llsdltlspv prdsllplqd tayrypgfmp
     1561 qthpglgggp ksgflgpmae phpedtftvt sl
//
LOCUS       NP_001424414             612 aa            linear   ROD 08-APR-2025
DEFINITION  zinc finger protein 655 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424414 XP_063127515
VERSION     NP_001424414.1
DBSOURCE    REFSEQ: accession NM_001437485.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Houlard,M., Romero-Portillo,F., Germani,A., Depaux,A.,
            Regnier-Ricard,F., Gisselbrecht,S. and Varin-Blank,N.
  TITLE     Characterization of VIK-1: a new Vav-interacting Kruppel-like
            protein
  JOURNAL   Oncogene 24 (1), 28-38 (2005)
   PUBMED   15558030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063127515.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR23984936.183657.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN12840117 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..612
                     /product="zinc finger protein 655 isoform 1"
                     /note="vav-1 interacting Kruppel-like protein; zinc finger
                     protein 205-like"
                     /calculated_mol_wt=71372
     Region          77..131
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          308..>598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(321,323,325,327..328,331..332,335,384,386,390..391,
                     394..395,398,412,414,416,418..419,422..423,426)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          344..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          348..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(439,441,443,445..446,449..450,453,489,491,495..496,
                     499..500,503,517,519,521,523..524,527..528,531)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          484..504
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          512..532
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          568..588
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..612
                     /gene="Zfp655"
                     /gene_synonym="RGD1309158; Znf655"
                     /coded_by="NM_001437485.1:116..1954"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360764"
                     /db_xref="RGD:1309158"
ORIGIN      
        1 meeitsqeaa esprvqfqsl esqseclspe lrflrdteme qgytdappvp qvpalphegs
       61 pgdqaaallt aryqefvtfe dvavhltree wgcldpvqre lyrevmleny gnvvslgfpi
      121 skpdgisqre qdlqvfdlet qnregvrndc sdgetreenk llipkrkise evhsykvrvg
      181 kfkqdiaqvp etreayksed rlerlqeilr kflflerefr qitiskktfs nekntepeks
      241 fsldstldtd qrvlriqtid dskydmnfnq npavgeqepi nltenfqntd ykeslmdlsh
      301 lnkwesmptt drsykcdtcg ktfhqasalt rhqrihtrek pykckeceks fsqssslsrh
      361 krihtreksy rceasdkscd asdkscsqss dvlqhkkvha kaksykcgtc ervfsrsvhl
      421 tqhqrthkdt ackctvcgsd fchtsylveh qrlhhqeksy eydecglayv kqqgirfrek
      481 pyscnecgkd frlnshlvqh qrihtgeklh ecnergkafs qtsclsqhhk mhrkeksyey
      541 nnyeesfshn sdltlqqevp irervfdcda weenfsqrah lipherahtk ekpyecnelg
      601 etfsqvqasf nm
//
LOCUS       NP_001424501             397 aa            linear   ROD 08-APR-2025
DEFINITION  lipase member K precursor [Rattus norvegicus].
ACCESSION   NP_001424501 XP_063143506
VERSION     NP_001424501.1
DBSOURCE    REFSEQ: accession NM_001437572.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_063143506.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.6420.1,
                                           SRR22582416.161929.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..397
                     /product="lipase member K precursor"
                     /note="lipase-like, ab-hydrolase domain containing 2;
                     lipase K; lipase member K"
                     /calculated_mol_wt=43253
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2103
     Region          34..388
                     /region_name="PLN02872"
                     /note="triacylglycerol lipase"
                     /db_xref="CDD:215470"
     CDS             1..397
                     /gene="Lipk"
                     /gene_synonym="Lipl2"
                     /coded_by="NM_001437572.1:239..1432"
                     /db_xref="GeneID:294094"
                     /db_xref="RGD:1309724"
ORIGIN      
        1 mwwllatccm flpgpiyghm qesitnpean mniseiisyw gypyerhdvv tedgyilgty
       61 riphgkgcsr kavpkavvyl qhgliasasn wicnlpnnsl aflladsgyd vwlgnsrgnt
      121 wsrkhlrlsp kspeywafsl demakydlpa tinlileksg qkqlfyvghs qgttiafiaf
      181 stnpelakki rmffalapvv tvkytqspmk klttlsrkav kilfgdkmfs thtwleqfia
      241 tkvcnrklfr qlcsnflfsl sgfdpqnlnm srldvymaqs pagtsvqnml hwaqavnsgq
      301 lqafdwgnpd qnmmhfnqlt ppvyniskmr vptamwsggr dvvadekdtk nllpkvanli
      361 yykeiphynh mdfylgqdap qevyrdlitm meeslqn
//
LOCUS       NP_001424401             963 aa            linear   ROD 08-APR-2025
DEFINITION  synphilin-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424401 XP_006254781
VERSION     NP_001424401.1
DBSOURCE    REFSEQ: accession NM_001437472.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Xie,Y.Y., Zhou,C.J., Zhou,Z.R., Hong,J., Che,M.X., Fu,Q.S.,
            Song,A.X., Lin,D.H. and Hu,H.Y.
  TITLE     Interaction with synphilin-1 promotes inclusion formation of
            alpha-synuclein: mechanistic insights and pathological implication
  JOURNAL   FASEB J 24 (1), 196-205 (2010)
   PUBMED   19762560
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Szargel,R., Rott,R., Eyal,A., Haskin,J., Shani,V., Balan,L.,
            Wolosker,H. and Engelender,S.
  TITLE     Synphilin-1A inhibits seven in absentia homolog (SIAH) and
            modulates alpha-synuclein monoubiquitylation and inclusion
            formation
  JOURNAL   J Biol Chem 284 (17), 11706-11716 (2009)
   PUBMED   19224863
  REMARK    GeneRIF: synphilin-1A has a novel role as a regulator of SIAH
            activity, modulating alpha-synuclein, and formation of Lewy
            body-like inclusions
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Eyal,A., Szargel,R., Avraham,E., Liani,E., Haskin,J., Rott,R. and
            Engelender,S.
  TITLE     Synphilin-1A: an aggregation-prone isoform of synphilin-1 that
            causes neuronal death and is present in aggregates from
            alpha-synucleinopathy patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (15), 5917-5922 (2006)
   PUBMED   16595633
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Lim,K.L., Chew,K.C., Tan,J.M., Wang,C., Chung,K.K., Zhang,Y.,
            Tanaka,Y., Smith,W., Engelender,S., Ross,C.A., Dawson,V.L. and
            Dawson,T.M.
  TITLE     Parkin mediates nonclassical, proteasomal-independent
            ubiquitination of synphilin-1: implications for Lewy body formation
  JOURNAL   J Neurosci 25 (8), 2002-2009 (2005)
   PUBMED   15728840
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Liani,E., Eyal,A., Avraham,E., Shemer,R., Szargel,R., Berg,D.,
            Bornemann,A., Riess,O., Ross,C.A., Rott,R. and Engelender,S.
  TITLE     Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its
            presence in cellular inclusions and Lewy bodies imply a role in
            Parkinson's disease
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5500-5505 (2004)
   PUBMED   15064394
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Nagano,Y., Yamashita,H., Takahashi,T., Kishida,S., Nakamura,T.,
            Iseki,E., Hattori,N., Mizuno,Y., Kikuchi,A. and Matsumoto,M.
  TITLE     Siah-1 facilitates ubiquitination and degradation of synphilin-1
  JOURNAL   J Biol Chem 278 (51), 51504-51514 (2003)
   PUBMED   14506261
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Ribeiro,C.S., Carneiro,K., Ross,C.A., Menezes,J.R. and
            Engelender,S.
  TITLE     Synphilin-1 is developmentally localized to synaptic terminals, and
            its association with synaptic vesicles is modulated by
            alpha-synuclein
  JOURNAL   J Biol Chem 277 (26), 23927-23933 (2002)
   PUBMED   11956199
  REMARK    GeneRIF: Our data indicated that synphilin-1 is a synaptic partner
            of alpha-synuclein, and it may mediate synaptic roles attributed to
            alpha-synuclein.
            Erratum:[J Biol Chem 2002 Sep 13;277(37):34651-4]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254781.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2904200.1,
                                           SRR26360181.1849224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..963
                     /product="synphilin-1 isoform 1"
                     /note="synphilin-1; synuclein, alpha interacting protein
                     (synphilin)"
                     /calculated_mol_wt=105664
     Region          <321..508
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(348,350,354..355,358..360,362..363,367,372,381,383,
                     385,424..425,428..430,432..433,437,444,453,455,457,
                     461..462,465..467,469..470,474,477,486)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          348..381
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          383..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          455..486
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          511..554
                     /region_name="SNCAIP_SNCA_bd"
                     /note="Synphilin-1 alpha-Synuclein-binding domain;
                     pfam16700"
                     /db_xref="CDD:435527"
     CDS             1..963
                     /gene="Sncaip"
                     /gene_synonym="Syph1"
                     /coded_by="NM_001437472.1:257..3148"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:307309"
                     /db_xref="RGD:1309283"
ORIGIN      
        1 meapeyldld eidfsddisy svtslktipa lcrrcdsqne drpvsssswn cgvstlitnp
       61 qkptgiadvy skfrpvkrvs plkhqpetle snesddqknn tveyqkgget dqgpqpeels
      121 pedgvgglpg kgsepsqalg elehydldmd eildvpyiks sqqlapltkv tsekrilglc
      181 ttvnglsakt cpivsaetst pnmaplcvls pvksphlrkv psvlrdqhkl paeesenspa
      241 pgkcgpafes enhskdflnk vfsdphsrka eksgpdcklr pfrlqtsaag akpeeqvngv
      301 swasaqgaee rteylqkvrs ilnivnegqi sllphlaadn ldkihdengn nllhvaaskg
      361 haeclqhlts lmgedclner naeqltpagl aikngqlecv rwmvseteai aelscskdfp
      421 slihyagcyg qekillwllq fmqeqgisld evdqegnsav hvasqhgylg ciqtlveyga
      481 nvtmqnhage kpsqsaerhg htlcsrylvv vetcmslasq vvkltkqlke qtvervtlqs
      541 qlqqlleaqk segkslpssp sspsspasrk sqwkildadd estgksklgt qegiqvlgnl
      601 ssrartkgkd edsdkilrql lgkeisenvc tqeklslefq daqvssrnsk kiplekrelk
      661 larlrqlmqr slsesdtdsn nsedpkntpv krvdrprpqp ivesvenmds aeslhlmikk
      721 hsvasgrrfp fgmkasksld ghspsptses sepdldshcp slgmtpptqp steatqcspd
      781 sataqkvats pksalkspss krrtsqnskl rvtfeepvvq meqtslelng ekdkergrap
      841 qrtsesgeqm krpfgtfrsi meslsgnqnn nnnyqpasql ktctlpltsl grktadakgn
      901 pvspaskgkn kaamysscih lpsnalveeh lrdyarlndi krntkktynv khiaepepke
      961 lfl
//
LOCUS       NP_001102595             108 aa            linear   ROD 08-APR-2025
DEFINITION  zinc finger protein 475 [Rattus norvegicus].
ACCESSION   NP_001102595 XP_001057605 XP_038952972 XP_574151
VERSION     NP_001102595.1
DBSOURCE    REFSEQ: accession NM_001109125.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Apr 2, 2025 this sequence version replaced
            XP_038952972.1, XP_001057605.1, XP_574151.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR460939.1, SRR26643293.77353.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..108
                     /product="zinc finger protein 475"
                     /note="zinc finger protein 474"
                     /calculated_mol_wt=12283
     Region          6..29
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          79..103
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     CDS             1..108
                     /gene="Zfp475"
                     /gene_synonym="RGD1564428; Znf474"
                     /coded_by="NM_001109125.2:94..420"
                     /db_xref="GeneID:498866"
                     /db_xref="RGD:1564428"
ORIGIN      
        1 mirrpptvvc yicgreygtk sisihepqcl kkwhnennll pkelrrpepr kpeirtiaak
       61 gfydldalnd aawtsaqsql vpcnlcgrtf lpdrlivhqr sckpkask
//
LOCUS       NP_001100609            1281 aa            linear   ROD 08-APR-2025
DEFINITION  membrane-associated phosphatidylinositol transfer protein 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001100609 XP_001079124 XP_063127376 XP_222155
VERSION     NP_001100609.1
DBSOURCE    REFSEQ: accession NM_001107139.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1281)
  AUTHORS   Lu,C., Vihtelic,T.S., Hyde,D.R. and Li,T.
  TITLE     A neuronal-specific mammalian homolog of the Drosophila retinal
            degeneration B gene with expression restricted to the retina and
            dentate gyrus
  JOURNAL   J Neurosci 19 (17), 7317-7325 (1999)
   PUBMED   10460238
REFERENCE   2  (residues 1 to 1281)
  AUTHORS   Lev,S., Hernandez,J., Martinez,R., Chen,A., Plowman,G. and
            Schlessinger,J.
  TITLE     Identification of a novel family of targets of PYK2 related to
            Drosophila retinal degeneration B (rdgB) protein
  JOURNAL   Mol Cell Biol 19 (3), 2278-2288 (1999)
   PUBMED   10022914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_063127376.1, XP_222155.4, XP_001079124.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..1281
                     /product="membrane-associated phosphatidylinositol
                     transfer protein 2 isoform 2"
                     /note="membrane-associated phosphatidylinositol transfer
                     protein 2"
                     /calculated_mol_wt=142448
     Region          1..258
                     /region_name="SRPBCC_PITPNM1-2_like"
                     /note="Lipid-binding SRPBCC domain of mammalian PITPNM1-2
                     and related proteins (Class IIA PITPs); cd08889"
                     /db_xref="CDD:176898"
     Site            order(21..22,25,29,32,40,59,61,63,65,68,70,73,77,81..82,
                     84,86,88,90,95,97,99,102..103,109,111,192,198,200,210,
                     218..220,223)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176898"
     Site            65..83
                     /site_type="active"
                     /note="putative lipid exchange loop [active]"
                     /db_xref="CDD:176898"
     Site            order(118..147,153..177,186..187)
                     /site_type="active"
                     /note="putatative regulatory loop [active]"
                     /db_xref="CDD:176898"
     Site            164
                     /site_type="other"
                     /note="putative PKC phosphorylation site
                     [posttranslational modification]"
                     /db_xref="CDD:176898"
     Region          701..894
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     Region          1040..1171
                     /region_name="LNS2"
                     /note="This domain is found in Saccharomyces cerevisiae
                     protein SMP2, proteins with an N-terminal lipin domain and
                     phosphatidylinositol transfer proteins; smart00775"
                     /db_xref="CDD:197870"
     CDS             1..1281
                     /gene="Pitpnm2"
                     /coded_by="NM_001107139.2:560..4405"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304474"
                     /db_xref="RGD:1310867"
ORIGIN      
        1 miikeyripl pmtveeyria qlymiqkksr netygqgsgv eilenrpytd gpggsgqyth
       61 kvyhvgmhip gwfrsilpka alrvveeswn aypytrtrft cpfvekfsid ietfyktdtg
      121 ennnvfnlsp veknqlitdi idivkdpvtp seykteedpk lfqsiktrrg plsenwiqey
      181 kkrllpimca yklckvefry wgmqskierf ihdtglrrvm vrahrqawcw qdewygltme
      241 kirelekevq lmlsrkmaqf seegpselsk estikdqatg atpepsssng eslgrglkkq
      301 wstsskssrs skrgaspsrh sisewrmqsi ardsdessee effdaqenlq hkeemytkdi
      361 tkwssndlmd kmenpepees qdslyhqsgs efrvassveq lntiedevsq platppskih
      421 vlllvlhggt ildtgagdps skqgdtntit nvfdtvmrvh ypsalghlai rlvpcppica
      481 dafalvsnls pyghdegcls ssqdhiplaa lpllatsspq yqeavatviq ranlaygdfi
      541 ksqegvtfng qvcligdcvg gilafdalcy sgqpvsesqs ssrrgsvvsm qdadllspgi
      601 lvnaahcsgg sgggsgggss lessrhlsrs nidiprsngt edsrkqmprk rsdsstyeld
      661 tiqqhqafls slhasvlrne pssrrsssst mldgagalgk fdfeiadlfl fgcplglvla
      721 lrktvipsld vfqlrpacqq vynlfhpadp sasrleplle rrfhtlppfn ipryqryplg
      781 dgcstllada lqthntvfqe haapsspgta pasrgfrras eisiasqvsg maesytasgi
      841 aqiaakwwgq kridyalycp dalmafptva lphlfhasyw estdvvsfll rqvmrhdsas
      901 ileldgkevs vftpsqprek wqrkrthvkl rnvaanhrin davanedgpq vvtgrfmygp
      961 ldmvtltgek vdvhimtqpp sgewlyldtl vtnssgrvsy tipethrlgv gvypikmvvr
     1021 gdhtfadsyi tvlpkgtefv vfsidgsfaa svsimgsdpk vragavdvvr hwqdlgylii
     1081 yvtgrpdmqk qrvvawlaqh nfphgvvsfc dglvhdplrh kanflkllis elhlrahaay
     1141 gstkdvavyn sislspmhiy ivgrptkklq qqcqfitdgy aahlaqlkyn hrarparnta
     1201 trmalrkgsf glpgqgdflr srnhllrtis aqpsgpshrh drtqtqmdle qrgqrsmsma
     1261 ascwgramag rlepgaatgp k
//
LOCUS       NP_001424443            1615 aa            linear   ROD 08-APR-2025
DEFINITION  low-density lipoprotein receptor-related protein 5 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_001424443 XP_063142794
VERSION     NP_001424443.1
DBSOURCE    REFSEQ: accession NM_001437514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1615)
  AUTHORS   Ubels,J.L., Lin,C.M., Antonetti,D.A., Diaz-Coranguez,M.,
            Diegel,C.R. and Williams,B.O.
  TITLE     Structure and function of the retina of low-density lipoprotein
            receptor-related protein 5 (Lrp5)-deficient rats
  JOURNAL   Exp Eye Res 217, 108977 (2022)
   PUBMED   35139333
  REMARK    GeneRIF: Structure and function of the retina of low-density
            lipoprotein receptor-related protein 5 (Lrp5)-deficient rats.
REFERENCE   2  (residues 1 to 1615)
  AUTHORS   Ju,S., Lim,L., Wi,K., Park,C., Ki,Y.J., Choi,D.H. and Song,H.
  TITLE     LRP5 Regulates HIF-1alpha Stability via Interaction with PHD2 in
            Ischemic Myocardium
  JOURNAL   Int J Mol Sci 22 (12), 6581 (2021)
   PUBMED   34205318
  REMARK    GeneRIF: LRP5 Regulates HIF-1alpha Stability via Interaction with
            PHD2 in Ischemic Myocardium.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1615)
  AUTHORS   Ubels,J.L., Diegel,C.R., Foxa,G.E., Ethen,N.J., Lensing,J.N.,
            Madaj,Z.B. and Williams,B.O.
  TITLE     Low-Density Lipoprotein Receptor-Related Protein 5-Deficient Rats
            Have Reduced Bone Mass and Abnormal Development of the Retinal
            Vasculature
  JOURNAL   CRISPR J 3 (4), 284-298 (2020)
   PUBMED   32833527
  REMARK    GeneRIF: Low-Density Lipoprotein Receptor-Related Protein
            5-Deficient Rats Have Reduced Bone Mass and Abnormal Development of
            the Retinal Vasculature.
REFERENCE   4  (residues 1 to 1615)
  AUTHORS   Ergun,S.G., Akay,G.G., Ergun,M.A. and Percin,E.F.
  TITLE     LRP5-linked osteoporosis-pseudoglioma syndrome mimicking isolated
            microphthalmia
  JOURNAL   Eur J Med Genet 60 (3), 200-204 (2017)
   PUBMED   28111184
REFERENCE   5  (residues 1 to 1615)
  AUTHORS   Huang,W., Li,Q., Amiry-Moghaddam,M., Hokama,M., Sardi,S.H.,
            Nagao,M., Warman,M.L. and Olsen,B.R.
  TITLE     Critical Endothelial Regulation by LRP5 during Retinal Vascular
            Development
  JOURNAL   PLoS One 11 (3), e0152833 (2016)
   PUBMED   27031698
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1615)
  AUTHORS   Kato,M., Patel,M.S., Levasseur,R., Lobov,I., Chang,B.H., Glass,D.A.
            2nd, Hartmann,C., Li,L., Hwang,T.H., Brayton,C.F., Lang,R.A.,
            Karsenty,G. and Chan,L.
  TITLE     Cbfa1-independent decrease in osteoblast proliferation, osteopenia,
            and persistent embryonic eye vascularization in mice deficient in
            Lrp5, a Wnt coreceptor
  JOURNAL   J Cell Biol 157 (2), 303-314 (2002)
   PUBMED   11956231
REFERENCE   7  (residues 1 to 1615)
  AUTHORS   Gong,Y., Slee,R.B., Fukai,N., Rawadi,G., Roman-Roman,S.,
            Reginato,A.M., Wang,H., Cundy,T., Glorieux,F.H., Lev,D.,
            Zacharin,M., Oexle,K., Marcelino,J., Suwairi,W., Heeger,S.,
            Sabatakos,G., Apte,S., Adkins,W.N., Allgrove,J.,
            Arslan-Kirchner,M., Batch,J.A., Beighton,P., Black,G.C.,
            Boles,R.G., Boon,L.M., Borrone,C., Brunner,H.G., Carle,G.F.,
            Dallapiccola,B., De Paepe,A., Floege,B., Halfhide,M.L., Hall,B.,
            Hennekam,R.C., Hirose,T., Jans,A., Juppner,H., Kim,C.A.,
            Keppler-Noreuil,K., Kohlschuetter,A., LaCombe,D., Lambert,M.,
            Lemyre,E., Letteboer,T., Peltonen,L., Ramesar,R.S., Romanengo,M.,
            Somer,H., Steichen-Gersdorf,E., Steinmann,B., Sullivan,B.,
            Superti-Furga,A., Swoboda,W., van den Boogaard,M.J., Van Hul,W.,
            Vikkula,M., Votruba,M., Zabel,B., Garcia,T., Baron,R., Olsen,B.R.
            and Warman,M.L.
  CONSRTM   Osteoporosis-Pseudoglioma Syndrome Collaborative Group
  TITLE     LDL receptor-related protein 5 (LRP5) affects bone accrual and eye
            development
  JOURNAL   Cell 107 (4), 513-523 (2001)
   PUBMED   11719191
REFERENCE   8  (residues 1 to 1615)
  AUTHORS   Mao,J., Wang,J., Liu,B., Pan,W., Farr,G.H. 3rd, Flynn,C., Yuan,H.,
            Takada,S., Kimelman,D., Li,L. and Wu,D.
  TITLE     Low-density lipoprotein receptor-related protein-5 binds to Axin
            and regulates the canonical Wnt signaling pathway
  JOURNAL   Mol Cell 7 (4), 801-809 (2001)
   PUBMED   11336703
REFERENCE   9  (residues 1 to 1615)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   10 (residues 1 to 1615)
  AUTHORS   Dong,Y., Lathrop,W., Weaver,D., Qiu,Q., Cini,J., Bertolini,D. and
            Chen,D.
  TITLE     Molecular cloning and characterization of LR3, a novel LDL receptor
            family protein with mitogenic activity
  JOURNAL   Biochem Biophys Res Commun 251 (3), 784-790 (1998)
   PUBMED   9790987
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063142794.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.4351.1,
                                           SRR26643297.4157.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1615
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42-q43"
     Protein         1..1615
                     /product="low-density lipoprotein receptor-related protein
                     5 isoform 1 precursor"
                     /note="low-density lipoprotein receptor-related protein 5"
                     /calculated_mol_wt=175846
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3153
     Region          23..214
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          102..142
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          163..203
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          187..229
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          230..271
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          299..336
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          366..406
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          408..450
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          451..494
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          495..537
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          538..571
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          605..640
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <654..782
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          710..752
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          799..838
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          838..879
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          906..941
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          970..1009
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1060..1103
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1104..1146
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1217..1253
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1259..1295
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1264,1274,1285..1286)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1278,1281,1285,1291..1292)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1288..1292
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1298..1332
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1303,1311,1322..1323)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1315,1318,1322,1328..1329)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1325..1329
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1336..1370
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1341,1349,1360..1361)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1353,1356,1360,1366..1367)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1363..1367
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1615
                     /gene="Lrp5"
                     /coded_by="NM_001437514.1:120..4967"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:293649"
                     /db_xref="RGD:1309329"
ORIGIN      
        1 metaptrapp pppqplllll alccslvpaa asplllfanr rdvrlvdagg vklestivas
       61 gledaaavdf qfskgavywt dvseeaikqt ylnqtgaaaq nivisglvsp dglacdwvgk
      121 klywtdsetn rievanlngt srkvlfwqdl dqpraialdp ahgymywtdw geaprierag
      181 mdgstrkiiv dsdiywpngl tidleeqkly wadaklsfih ranldgsfrq kvvegslthp
      241 faltlsgdtl ywtdwqtrsi hacnkwtgek rkeilsalys pmdiqvlsqe rqphfhtpce
      301 egnggcshlc llsprepfys cacptgvqlq dngktckaga eevlllarrt dlrrisldtp
      361 dftdivlqvg dirhaiaidy dplegyvywt ddevrairra yldgsgaqtl vnteindpdg
      421 iavdwvarnl ywtdtgtdri evtrlngtsr kilvsedlde praivlhpvm glmywtdwge
      481 npkiecanld grdrhvlvnt slgwpnglal dlqegklywg daktdkievi nidgtkrqtl
      541 ledklphifg ftllgdfiyw tdwqrrsier vhkvkasrdv iidqlpdlmg lkavnvakvv
      601 gtnpcadgng gcshlcfftp hatkcgcpig lellsdmktc iipeaflvft sratihrisl
      661 etnnndvaip ltgvkeasal dfdvsnnhiy wtdvslktis rafmngssve hviefgldyp
      721 egmavdwmgk nlywadtgtn rievarldgq frqvlvwrdl dnprslaldp tkgyiywtew
      781 ggkprivraf mdgtncmtlv dkvgrandlt idyadqrlyw tdldtnmies snmlgqermv
      841 iaddlpypfg ltqysdyiyw tdwnlhsier adktsgrnrt liqghldfvm dilvfhssrq
      901 dglndcvhsn gqcgqlclai pgghrcgcas hytldpssrn csppstfllf sqkfaisrmi
      961 pddqlspdli lplhglrnvk ainydpldkf iywvdgrqni krakddgtqp smltspsqsl
     1021 spdrqphdls idiysrtlfw tceatntinv hrldgdamgv vlrgdrdrpr aiavnaergy
     1081 myftnmqdha akierasldg terevlfttg lirpvalvvd nalgklfwvd adlkriescd
     1141 lsganrltle danivqpvgl tvlgrhlywi drqqqmierv ekttgdkrtr vqgrvthltg
     1201 ihaveevsle efsahpcard nggcshicia kgdgtprcsc pvhlvllqnl ltcgepptcs
     1261 pdqfacatge idcipgawrc dgfpecadqs deegcpvcsa sqfpcargqc vdlrlrcdge
     1321 adcqdgsdea ncdavclpnq frcasgqcvl ikqqcdsfpd cadgsdelmc einkppsddv
     1381 pahssaigpv igiilslfvm ggvyfvcqrv mcqrytgasg pfpheyvggt phvplnfiap
     1441 ggsqhgpfpg ipcsksmmss vslvggrgsv plydrnhvtg assssssstk atlyppilnp
     1501 ppspatdpsl ynmdmfyssn ipstarpyrp yiirgmappt tpcstdvcds dystsrwkts
     1561 kyyldlnsds dpypppptph sqylsaedsc ppspvtersy chlfppppsp ctdss
//
LOCUS       NP_001424375             576 aa            linear   ROD 08-APR-2025
DEFINITION  testis-specific serine kinase substrate isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424375 XP_006229079
VERSION     NP_001424375.1
DBSOURCE    REFSEQ: accession NM_001437446.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     Targeted deletion of Tssk1 and 2 causes male infertility due to
            haploinsufficiency
  JOURNAL   Dev Biol 319 (2), 211-222 (2008)
   PUBMED   18533145
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Xu,B., Hao,Z., Jha,K.N., Zhang,Z., Urekar,C., Digilio,L.,
            Pulido,S., Strauss,J.F. 3rd, Flickinger,C.J. and Herr,J.C.
  TITLE     TSKS concentrates in spermatid centrioles during flagellogenesis
  JOURNAL   Dev Biol 319 (2), 201-210 (2008)
   PUBMED   18495105
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Kueng,P., Nikolova,Z., Djonov,V., Hemphill,A., Rohrbach,V.,
            Boehlen,D., Zuercher,G., Andres,A.C. and Ziemiecki,A.
  TITLE     A novel family of serine/threonine kinases participating in
            spermiogenesis
  JOURNAL   J Cell Biol 139 (7), 1851-1859 (1997)
   PUBMED   9412477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006229079.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1295640.1,
                                           SRR26643293.2993.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..576
                     /product="testis-specific serine kinase substrate isoform
                     4"
                     /note="STK22 substrate 1; testis-specific kinase
                     substrate; serine/threonine kinase 22 substrate 1"
                     /calculated_mol_wt=62437
     Region          48..576
                     /region_name="TSKS"
                     /note="Testis-specific serine kinase substrate; pfam15358"
                     /db_xref="CDD:434661"
     Region          91..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Region          142..>249
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          253..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P60531.1)"
     Region          550..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60531.1)"
     CDS             1..576
                     /gene="Tsks"
                     /gene_synonym="Stk22s1"
                     /coded_by="NM_001437446.1:46..1776"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:292890"
                     /db_xref="RGD:727784"
ORIGIN      
        1 masvvvktiw qskeiheagd ppagvesraq lvpeapggvt spakgitkkk kavsfhgvep
       61 rmshepmhwc lnlkrssact nvsllnlaam epdssgtdst tedsgplalp gppaspttpw
      121 apedpditel lsgvnsglvr akdsitslke kttrvnqhvq tlqsecsvls enlerrrqea
      181 eelegycsql kencrkvtrs vedaeiktnv lkqnsallee klrylqqqlq detprrqeae
      241 lqeleqklea glsrhglgpt tpiqgcsgpp gspeepprpr glpsngwgma iragegpsls
      301 eqelqkvssg leelrrevss laarwhqeeg avqealrllg glggrldgfl gqweraqreq
      361 aqsarglqel rgradelctm versavsvas lrselealgp vkpileelgr qlqnsrrgpd
      421 hvlnldrpaq gpcprcasqg qqlsteslqq lleraltplv devkqkglap acpscqrlhk
      481 kilelerqal akhvraeals stlrlaqdea vraknllltd kmkpeekvat ldymhlkmcs
      541 lhdqlshlpl egstgamggg stggappkrg gpgseq
//
LOCUS       NP_001099711             568 aa            linear   ROD 08-APR-2025
DEFINITION  ras and Rab interactor-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099711 XP_001078499 XP_218477
VERSION     NP_001099711.1
DBSOURCE    REFSEQ: accession NM_001106241.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Woller,B., Luiskandl,S., Popovic,M., Prieler,B.E., Ikonge,G.,
            Mutzl,M., Rehmann,H. and Herbst,R.
  TITLE     Rin-like, a novel regulator of endocytosis, acts as guanine
            nucleotide exchange factor for Rab5a and Rab22
  JOURNAL   Biochim Biophys Acta 1813 (6), 1198-1210 (2011)
   PUBMED   21419809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_218477.2, XP_001078499.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.1641.1,
                                           SRR26643284.532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..568
                     /product="ras and Rab interactor-like protein isoform 1"
                     /note="ras and Rab interactor-like protein"
                     /calculated_mol_wt=63096
     Region          43..136
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(58,76,97,99)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(98,125)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Region          417..519
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..568
                     /gene="Rinl"
                     /gene_synonym="RGD1310133"
                     /coded_by="NM_001106241.3:103..1809"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292760"
                     /db_xref="RGD:1310133"
ORIGIN      
        1 mrlaqpdmvs aatteearls wplaegadks plrvlsttes llrlqrtqrv wqvpeldaeh
       61 akaflkpwpl gsflvigqdp dqvlmlktgp ssgdintyqi qkfpggvsle ssnlcmpdfp
      121 hllaflsasr dvlprtlllp tptvgpgdkh sdprrlgciq vdtsgrvlsv vnqlylethg
      181 gwetetpqqt kpetgqkrsl aprmptphrv swveeslkpe ahhtgqevhh perqvhypgp
      241 eahslgpevh fpspvleeee evnndsykde eegcedmlta hiralasars syvarqyqcl
      301 rarlisdsgn pyspgdpate llqdvrqllt dlqdylakdp dvravfgnrg psipreedlg
      361 pavevalcra vleplkpalw tklrtlraqe lrrlrrrqia lrvgagpegq spalrnriha
      421 rlahlhaaca prrkvallla vcsdvyagla ggenkeplga daflpaltee liwsphiget
      481 qldveflmel ldpgelrgea gyylttwfga lyhiahyqpd agrapqelss earaslrqwh
      541 rrrtlhqqaq ptapenqpfe epwaigdp
//
LOCUS       NP_001423876             133 aa            linear   ROD 08-APR-2025
DEFINITION  helix-loop-helix protein 1 [Rattus norvegicus].
ACCESSION   NP_001423876 XP_063128200
VERSION     NP_001423876.1
DBSOURCE    REFSEQ: accession NM_001436947.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Manetopoulos,C., Hansson,A., Karlsson,J., Jonsson,J.I. and
            Axelson,H.
  TITLE     The LIM-only protein LMO4 modulates the transcriptional activity of
            HEN1
  JOURNAL   Biochem Biophys Res Commun 307 (4), 891-899 (2003)
   PUBMED   12878195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Mar 24, 2025 this sequence version replaced XP_063128200.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1155514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN16418971
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..133
                     /product="helix-loop-helix protein 1"
                     /calculated_mol_wt=14683
     Region          61..132
                     /region_name="bHLH_TS_HEN1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     helix-loop-helix protein 1 (HEN-1) and similar proteins;
                     cd19701"
                     /db_xref="CDD:381544"
     Site            order(77,81,83..85,87,92,110..113)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381544"
     Site            order(90..91,94..95,97..98,114,117,121,123..124,128,
                     130..131)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381544"
     CDS             1..133
                     /gene="Nhlh1"
                     /coded_by="NM_001436947.1:586..987"
                     /db_xref="GeneID:289230"
                     /db_xref="RGD:1310261"
ORIGIN      
        1 mmlnsdtmel dlppthsete sgfsdcgggp gpdgagsgdp gvgqvrslel gesgrkdlqh
       61 lsreerrrrr ratakyrtah atrerirvea fnlafaelrk llptlppdkk lskieilrla
      121 icyisylnhv ldv
//
LOCUS       NP_001100696            1345 aa            linear   ROD 08-APR-2025
DEFINITION  SH3 domain and tetratricopeptide repeat-containing protein 1
            [Rattus norvegicus].
ACCESSION   NP_001100696 XP_001057749 XP_001057812 XP_006251187 XP_223527
VERSION     NP_001100696.1
DBSOURCE    REFSEQ: accession NM_001107226.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1345)
  AUTHORS   Senderek,J., Bergmann,C., Stendel,C., Kirfel,J., Verpoorten,N., De
            Jonghe,P., Timmerman,V., Chrast,R., Verheijen,M.H., Lemke,G.,
            Battaloglu,E., Parman,Y., Erdem,S., Tan,E., Topaloglu,H., Hahn,A.,
            Muller-Felber,W., Rizzuto,N., Fabrizi,G.M., Stuhrmann,M.,
            Rudnik-Schoneborn,S., Zuchner,S., Michael Schroder,J., Buchheim,E.,
            Straub,V., Klepper,J., Huehne,K., Rautenstrauss,B., Buttner,R.,
            Nelis,E. and Zerres,K.
  TITLE     Mutations in a gene encoding a novel SH3/TPR domain protein cause
            autosomal recessive Charcot-Marie-Tooth type 4C neuropathy
  JOURNAL   Am J Hum Genet 73 (5), 1106-1119 (2003)
   PUBMED   14574644
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Mar 24, 2025 this sequence version replaced
            XP_006251187.1, XP_001057812.1, XP_001057749.1, XP_223527.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.17197.1,
                                           SRR26643287.30542.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1345
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1345
                     /product="SH3 domain and tetratricopeptide
                     repeat-containing protein 1"
                     /note="SH3 domain and tetratricopeptide repeats-containing
                     protein 1"
                     /calculated_mol_wt=149038
     Region          312..366
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(317,319,322,326,346..347,362,364..365)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212818"
     Region          605..655
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(606,609..610,613..614,616,668,671..672,675..676,
                     678..679,710,713..714,717..718,721)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <666..900
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          666..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          701..733
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <775..1230
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            order(1162,1165..1166,1169..1170,1172,1196,1205..1206,
                     1209..1210,1212..1213,1246,1249..1250,1254..1255,1258)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1162..1189
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1165..1233
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          1194..1230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1203..1276
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          1245..1274
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1345
                     /gene="Sh3tc1"
                     /coded_by="NM_001107226.2:377..4414"
                     /db_xref="GeneID:305441"
                     /db_xref="RGD:1305610"
ORIGIN      
        1 mrsfreeeat sedlstmgqg peeppggcsl edkiqsismg lptsqertgp eeaeattvrg
       61 dvappcgmvg qaaeppsnqm avyptdltlq llavrrksgl rspslqqtlr srlrllends
      121 revarvlgel sarllsihsd qdrivvtfkt feeiwkfsty halgfthhcl enllvdqtfw
      181 llspseeeet ailiyvnkda lkqthkslla qegsffvlcp dhcvrrtkep qgagkgpqtl
      241 rrasgvtlgv pvvetvsssp tpsmsskaea veaepepltp fhqwtlrvpw dpidesmsgp
      301 gtpdaqfmrf glasaiadfq gsgpeemsfs vgdvieivga qvpglpwclg qhmasgqvgf
      361 vrtglvrmqg pasdlessif lseeersffr seahfsdeda rrllcrtsgt dvcttcsldw
      421 leeaegeqle qqemslphln pepheslhmv knvlekckac pdhpedpvsw slgavssrvs
      481 spdleeppfc ldpdddwtdp eppdsllqvl sapgyraqfr slydislpcl stalysfdde
      541 eelaerlaqa rgvakkvdlg malarlclll grlcarklkl sqarvyfeea lgalegsfgd
      601 lslvaavyss latvylkqkn gekcvqlapk aaalllgtpg hscstdaell kyalrrvvcg
      661 lspqaearac fllarhythl kqpeealpyl erllrlnrdv gtpqaswped cyllladiyg
      721 rkclphlals clkvsslwtr cslagslrsv dlvlqnapgp nsqrstghsl psqiahylrq
      781 alaslppgtg qtlrgplyas laqlysyhqq ygqaiafmsq aaeadtaagv hpvvdrlval
      841 awlhllcgks lvamdilkcv sdaavankdq ecvmmnmvam alkrmgrtrq aaegyfralh
      901 maysqghlqs qavvlanfga lclqagarsl aqhylreavg lfsqlpsgvc grdftqvllw
      961 lgqlctrrtl pqqakcyyew aflvavetdh lesqlqavqk lchfyskvmp nevrcviyhe
     1021 fqlalarkta dkvlegqlle aisqlylslg terayksald ytkrslgifi dlqqkekear
     1081 awlqagkiyy ilrqnelvdl yiqvaqnaal ytgdpklgle lfeaagdiff ngtwerekav
     1141 sfyrdralpl avtvgdqeve lrlcnklval lsaleapqeg lefahealal sitlgdrlne
     1201 rvayhrlatl hhrlghgela ehfflkalsl ctsplefdee tlyyvkvylv lgdiifyelk
     1261 dpfdaagyyq lalaaavdlg hkkaqlkiyt rlatiyhnfl mdremslffy qkartfasel
     1321 nlrrtnlvpq hfcsrapwla pgyps
//
LOCUS       NP_001424168             716 aa            linear   ROD 08-APR-2025
DEFINITION  myogenesis-regulating glycosidase [Rattus norvegicus].
ACCESSION   NP_001424168 XP_063144178
VERSION     NP_001424168.1
DBSOURCE    REFSEQ: accession NM_001437239.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Datta,K., Guan,T. and Gerace,L.
  TITLE     NET37, a nuclear envelope transmembrane protein with glycosidase
            homology, is involved in myoblast differentiation
  JOURNAL   J Biol Chem 284 (43), 29666-29676 (2009)
   PUBMED   19706595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063144178.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.26986.1,
                                           SRR26643289.14997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..716
                     /product="myogenesis-regulating glycosidase"
                     /calculated_mol_wt=81212
     Region          313..684
                     /region_name="GH31_NET37"
                     /note="glucosidase NET37; cd06592"
                     /db_xref="CDD:269878"
     Site            order(352..353,460,462..463,501,519,603,605)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269878"
     CDS             1..716
                     /gene="Myorg"
                     /gene_synonym="RGD1309821"
                     /coded_by="NM_001437239.1:325..2475"
                     /db_xref="GeneID:366360"
                     /db_xref="RGD:1309821"
ORIGIN      
        1 mpqnlqeksq vyprhrlgsh agpkslevip gatmytflpd nfspakpkpt kelrpllcsv
       61 vlglllvlaa vvawcyysas lrkaerlrae lldlnrggfs irnqkgeqvf rlafrsgald
      121 ldscsrdgal lgcsrtadgr plhffiqtvr pkdtvmcyrv rweeaapgra vehamflgda
      181 aahwyggaem rtqhwpirld gqqepqpfvt sdvyssdaaf ggilerywls sraaaikvnd
      241 svpfhlgwns tersmrlqar yhhtsykppa grtaapelsy rvcvgsdvts ihkymvrryf
      301 nkpsrvpase afrdpiwstw alygrsvdqn kvlqfaqqir qhrfnsshle iddmytpayg
      361 dfdfdeskfp natdlfhrlr dagfrvtlwv hpfvnynssr fgegverelf vreptgrlpa
      421 lvrwwngiga vldftrpear ewfqghlrrl rsrynvasfk fdagevsylp pdfstykpls
      481 dpsvwsrryt emalpffsla evrvgyqsqn iscffrlvdr dsvwgydlgl rslipavltv
      541 smlgypfilp dmiggnavpe rtagrpdgpg perelyvrwl evaafmpamq fsippwqyda
      601 evvaiahkfa alraslvapl llelagevtd tgdpivrplw wiapgdetah ridsqfligd
      661 tllvapvlep gkqerdvylp agkwrsykge lfdktpvllt dypvdldeva yftwas
//
LOCUS       NP_001424270             989 aa            linear   ROD 08-APR-2025
DEFINITION  centrosomal protein of 120 kDa isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424270 XP_063133372
VERSION     NP_001424270.1
DBSOURCE    REFSEQ: accession NM_001437341.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 989)
  AUTHORS   Chang,C.W., Hsu,W.B., Tsai,J.J., Tang,C.J. and Tang,T.K.
  TITLE     CEP295 interacts with microtubules and is required for centriole
            elongation
  JOURNAL   J Cell Sci 129 (13), 2501-2513 (2016)
   PUBMED   27185865
REFERENCE   2  (residues 1 to 989)
  AUTHORS   Wu,C., Yang,M., Li,J., Wang,C., Cao,T., Tao,K. and Wang,B.
  TITLE     Talpid3-binding centrosomal protein Cep120 is required for
            centriole duplication and proliferation of cerebellar granule
            neuron progenitors
  JOURNAL   PLoS One 9 (9), e107943 (2014)
   PUBMED   25251415
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 989)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 989)
  AUTHORS   Xie,Z., Moy,L.Y., Sanada,K., Zhou,Y., Buchman,J.J. and Tsai,L.H.
  TITLE     Cep120 and TACCs control interkinetic nuclear migration and the
            neural progenitor pool
  JOURNAL   Neuron 56 (1), 79-93 (2007)
   PUBMED   17920017
REFERENCE   5  (residues 1 to 989)
  AUTHORS   Iwakoshi,N.N., Pypaert,M. and Glimcher,L.H.
  TITLE     The transcription factor XBP-1 is essential for the development and
            survival of dendritic cells
  JOURNAL   J Exp Med 204 (10), 2267-2275 (2007)
   PUBMED   17875675
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063133372.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1763008.1,
                                           SRR26643298.74070.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..989
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..989
                     /product="centrosomal protein of 120 kDa isoform 1"
                     /note="centrosomal protein 120kDa; coiled-coil domain
                     containing 100; centrosomal protein of 120 kDa"
                     /calculated_mol_wt=112690
     Region          9..114
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          118..340
                     /region_name="DUF3668"
                     /note="Cep120 protein; pfam12416"
                     /db_xref="CDD:463569"
     Region          <653..>987
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..989
                     /gene="Cep120"
                     /gene_synonym="Ccdc100; RGD1565619"
                     /coded_by="NM_001437341.1:289..3258"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:307302"
                     /db_xref="RGD:1565619"
ORIGIN      
        1 mvpksdqlli vvsilegrhf pkrpkhmlvv eakfdgeqla tdpvdhtdqp efatelawei
       61 drkvlhqhrl qrtpiklqcf aldpqtsake tvgyivldlr taqetkqapk wyqllsnkyt
      121 kfksevqisi tletdtkaqv dsfkakgapp rdgkvpasll gvdpkdivav lneeggyhqi
      181 gpaecctdsf tlsvtiafat qleqlipctm klperqpeff fyysllgndv tnepfsdlin
      241 pnfeperasv rirssvevlr vylalhsklq ihlccgdqsl gsteiplsgl lkkgsteinq
      301 hpvtvegaft ldppnrakqk lapvpvelap tvgvsvalqr egigsqslie lktqnghepe
      361 hsqkrvltpi kektltgpks prvspappqn qtpptkddat eseveslqyd kepkqvvkgt
      421 gsipaslaqp eatgnpsevv tsgqkiavpa tshhfcfsid lrsihgleis fpvncilrys
      481 ypffgsaapi mtnppvevrk nmevflpqsy cafdfatmph qlqdtflrip llvelwhkdk
      541 mskdlllgia riqlsnilss ektrflgang eqcwrqtyse kvpviaaqgs nnrivdlsyt
      601 mtledyglvk mreifvsess qgmsavgqra sppppppapc pseiqvepre tleykaalel
      661 emwkemqedi fesqlkqkel ahmqalaeew kkrdreresl vkkkvaeysi legklqqalt
      721 elesreqqlv taetelqrer kelqlerern lqelqdsvrr arddcvhqve lerlklkqle
      781 edkhrlqqql ndaenkykil ekdfqqfkdq qnnkpeirlq seinlltlek velerklesa
      841 tksklhykqq wgralkelar lkqreqesqm arlkkqqeel eqmrlrylaa eekdtvkteq
      901 qelldirnel nrlrqqeqkq yqdykeiasg kqgsprgsgl eeglddyltr lieerdtlmr
      961 tgvynhedri iseldrqire vltknsasn
//
LOCUS       NP_001424500            2569 aa            linear   ROD 08-APR-2025
DEFINITION  nuclear receptor corepressor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424500 XP_006249367
VERSION     NP_001424500.1
DBSOURCE    REFSEQ: accession NM_001437571.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2569)
  AUTHORS   Barbieri,C.E., Bangma,C.H., Bjartell,A., Catto,J.W., Culig,Z.,
            Gronberg,H., Luo,J., Visakorpi,T. and Rubin,M.A.
  TITLE     The mutational landscape of prostate cancer
  JOURNAL   Eur Urol 64 (4), 567-576 (2013)
   PUBMED   23759327
  REMARK    Review article
REFERENCE   2  (residues 1 to 2569)
  AUTHORS   Yang,J. and Fuller,P.J.
  TITLE     Interactions of the mineralocorticoid receptor--within and without
  JOURNAL   Mol Cell Endocrinol 350 (2), 196-205 (2012)
   PUBMED   21784126
  REMARK    Review article
REFERENCE   3  (residues 1 to 2569)
  AUTHORS   Pei,L., Leblanc,M., Barish,G., Atkins,A., Nofsinger,R., Whyte,J.,
            Gold,D., He,M., Kawamura,K., Li,H.R., Downes,M., Yu,R.T.,
            Powell,H.C., Lingrel,J.B. and Evans,R.M.
  TITLE     Thyroid hormone receptor repression is linked to type I
            pneumocyte-associated respiratory distress syndrome
  JOURNAL   Nat Med 17 (11), 1466-1472 (2011)
   PUBMED   22001906
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2569)
  AUTHORS   Sircoulomb,F., Nicolas,N., Ferrari,A., Finetti,P., Bekhouche,I.,
            Rousselet,E., Lonigro,A., Adelaide,J., Baudelet,E., Esteyries,S.,
            Wicinski,J., Audebert,S., Charafe-Jauffret,E., Jacquemier,J.,
            Lopez,M., Borg,J.P., Sotiriou,C., Popovici,C., Bertucci,F.,
            Birnbaum,D., Chaffanet,M. and Ginestier,C.
  TITLE     ZNF703 gene amplification at 8p12 specifies luminal B breast cancer
  JOURNAL   EMBO Mol Med 3 (3), 153-166 (2011)
   PUBMED   21328542
  REMARK    Erratum:[EMBO Mol Med. 2011 Mar;3(3). doi:10.1002/emmm.201000121]
REFERENCE   5  (residues 1 to 2569)
  AUTHORS   Cui,J., Yang,Y., Zhang,C., Hu,P., Kan,W., Bai,X., Liu,X. and
            Song,H.
  TITLE     FBI-1 functions as a novel AR co-repressor in prostate cancer cells
  JOURNAL   Cell Mol Life Sci 68 (6), 1091-1103 (2011)
   PUBMED   20812024
REFERENCE   6  (residues 1 to 2569)
  AUTHORS   Martinez de Arrieta,C., Koibuchi,N. and Chin,W.W.
  TITLE     Coactivator and corepressor gene expression in rat cerebellum
            during postnatal development and the effect of altered thyroid
            status
  JOURNAL   Endocrinology 141 (5), 1693-1698 (2000)
   PUBMED   10803578
REFERENCE   7  (residues 1 to 2569)
  AUTHORS   Zhou,S., Fujimuro,M., Hsieh,J.J., Chen,L., Miyamoto,A.,
            Weinmaster,G. and Hayward,S.D.
  TITLE     SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
            domain of NotchIC To facilitate NotchIC function
  JOURNAL   Mol Cell Biol 20 (7), 2400-2410 (2000)
   PUBMED   10713164
REFERENCE   8  (residues 1 to 2569)
  AUTHORS   Park,E.J., Schroen,D.J., Yang,M., Li,H., Li,L. and Chen,J.D.
  TITLE     SMRTe, a silencing mediator for retinoid and thyroid hormone
            receptors-extended isoform that is more related to the nuclear
            receptor corepressor
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3519-3524 (1999)
   PUBMED   10097068
REFERENCE   9  (residues 1 to 2569)
  AUTHORS   Ordentlich,P., Downes,M., Xie,W., Genin,A., Spinner,N.B. and
            Evans,R.M.
  TITLE     Unique forms of human and mouse nuclear receptor corepressor SMRT
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2639-2644 (1999)
   PUBMED   10077563
REFERENCE   10 (residues 1 to 2569)
  AUTHORS   Misiti,S., Schomburg,L., Yen,P.M. and Chin,W.W.
  TITLE     Expression and hormonal regulation of coactivator and corepressor
            genes
  JOURNAL   Endocrinology 139 (5), 2493-2500 (1998)
   PUBMED   9564863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006249367.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..2569
                     /product="nuclear receptor corepressor 2 isoform 1"
                     /note="nuclear receptor corepressor 2"
                     /calculated_mol_wt=280230
     Region          143..229
                     /region_name="GPS2_interact"
                     /note="G-protein pathway suppressor 2-interacting domain;
                     pfam15784"
                     /db_xref="CDD:464868"
     Region          159..>405
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          432..475
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(432,461..462,464..465,467..469,471..473)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          <539..>649
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Region          614..657
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Region          <1775..2032
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1917..2321
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2569
                     /gene="Ncor2"
                     /coded_by="NM_001437571.1:376..8085"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360801"
                     /db_xref="RGD:1310293"
ORIGIN      
        1 msgstqpvaq twraaepryp phgisypvqi arphtdvgll eyqhhprdyt shlspgsiiq
       61 pqrrrpslls efqpgsersq elhlrpesrt flpelgkpdi efteskrprl ellpdtllrp
      121 apllatgqps gsedltkdrs lagklepvsp pspphadpel eltpsrlske eliqnmdrvd
      181 reitmveqqi sklkkkqqql eeeaakppep ekpvspppie skhrslvqii ydenrkkaea
      241 ahrileglgp qvelplynqp sdtrqyheni kinqamrkkl ilyfkrrnha rkqweqrfcq
      301 rydqlmeawe kkveriennp rrrakeskvr eyyekqfpei rkqrelqerm qsrvgqrgsg
      361 lsmsaarseh evseiidgls eqenlekqmr qlavippmly dadqqrikfi nmnglmddpm
      421 kvykdrqvtn mwseqerdtf rekfmqhpkn fgliasfler ktvaecvlyy yltkknenyk
      481 slvrrsyrrr gksqqqqqqq qqqqqqqqqq qmarssqeek eekekekead keeekqdaen
      541 ekeelskekt ddtsgednde keavaskgrk tansqgrrkg ritrsmanea nheetatpqq
      601 sselasmemn essrwteeem etakkglleh grnwsaiarm vgsktvsqck nfyfnykkrq
      661 nldeilqqhk lkmekernar rkkkktpaaa seetafppaa edeemeasga saneeelaee
      721 aeasqasgne vprvgecsgp aavnnssdte svpsprteat kdagpkpast ealpaatqpp
      781 vpppeepatv pdepcpapda sgppspvasp ppaappaavd kdeqdqaatv pqtedakeqk
      841 seaeelvidv gkteepeape eppesvksdh keeteeeped kakgpeaiet vseaplkvee
      901 agskaavtkg sssgatqdsd ssatcsadev depeggdkgr llsprpsllt pagdprasts
      961 pqkpldlkql kqraaaippi qvtkvheppr edtvppkpap pvppptqhlq pegdvsqqsg
     1021 gsprgkcrsp vppaekeaek asffpafpae gpklpteppr wtsglpfpip previktsph
     1081 aadpsafsyt ppghplplgl hdsarpvlpr ppisnpppli ssakhpgvle rqlgtisqqg
     1141 msvqlrvphs ehakapmgpl tmglplavdp kklapfsgvk qeqlsprgqa gppeslgvpt
     1201 aqetsvlrgt algstasgsi tkglpstrta dgpsyrgsit hgtpadvlyk gtisrivged
     1261 spsrldrare dtlpkghviy egkkghvlsy eggmsvsqcs kedgrsssgp phetaapkrt
     1321 ydmmegrvgr titsasiegl mgraipeqhs phlkeqhhir gsitqgiprs yveaqedylr
     1381 reakllkreg tppppppprd ltetyktrpl dplgplklkp thegvvatvk eagrsiheip
     1441 reelrrtpel plaprplkeg sitqtyrens iwpatyrpgp spqgtplkyd sgvpssgskk
     1501 hdvrsiigsp grpfpalhpl dimadarale racyeeslks rsgtssgagg sitrgapvvv
     1561 pelgkprqsp layedhgapf tshlprgspv ttreptprlq egsllsskas qdrkltstpr
     1621 eiaksphstv pehhphpisp yehllrgvtg vdlyrghipl afdptsiprg ipleaaaaay
     1681 ylprhlapsp typhlyppyl irgypdtaal enrqtiindy itsqqmhhna asamaqradm
     1741 lrglspress lalnyaagpr giidlsqvph lpvlvpptpg tpataidrla ylptapppfs
     1801 srhsssplsp ggpthlakpt atssserere rererdksil tstttvehap iwrpgteqss
     1861 gaggssrpas hthqhspisp rtqdalqqrp svlhntsmkg vvtsvepgtp tvlrwarsts
     1921 tsspvrpaat fppathcplg gtlegvyptl mepvllpket srvtrperpr vdaghafltk
     1981 pparepassp sksseprsla ppssshtaia rtpakslaph haspdlpapt sasdlhrekt
     2041 qskpfsiqel elrslgkttl taatfidaii trqiahergp reggslaids pgdgyhsgag
     2101 yspdgvepis pvsspslthd kglskpleel ekshlegelr hkqpgpmkls geaahlphlr
     2161 plpesqpsss pllqtapgik ghqrvvtlaq hisevitqdy trhhpqqlsg plpaplysfp
     2221 gascpvldlr rppsdlylpp pdhgtpargs phseggkrsp epsktvlsss edaiepvspp
     2281 egmtepghar staypllyrd geqgeprmgs kspgntsqpp affskltesn samvkskkqe
     2341 inkklnthnr nepeynigqp gteifnmpai tgaglmtcrs qavqehastn mgleaiirka
     2401 lmgkydqwee ppplganafn plnasaslpa aampittadg rsdhpltspg gggkakvsgr
     2461 pssrkakspa pglapgdrpp svssvhsegd cnrrtpltnr vwedrpssag stpfpynpli
     2521 mrlqagvmas ppppglaags gplagphhaw deepkpllcs qyetlsdse
//
LOCUS       NP_001099440             133 aa            linear   ROD 08-APR-2025
DEFINITION  helix-loop-helix protein 1 [Rattus norvegicus].
ACCESSION   NP_001099440 XP_001055226 XP_222898
VERSION     NP_001099440.1
DBSOURCE    REFSEQ: accession NM_001105970.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Manetopoulos,C., Hansson,A., Karlsson,J., Jonsson,J.I. and
            Axelson,H.
  TITLE     The LIM-only protein LMO4 modulates the transcriptional activity of
            HEN1
  JOURNAL   Biochem Biophys Res Commun 307 (4), 891-899 (2003)
   PUBMED   12878195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_222898.1, XP_001055226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.940433.1,
                                           SRR22582416.719706.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..133
                     /product="helix-loop-helix protein 1"
                     /calculated_mol_wt=14683
     Region          61..132
                     /region_name="bHLH_TS_HEN1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     helix-loop-helix protein 1 (HEN-1) and similar proteins;
                     cd19701"
                     /db_xref="CDD:381544"
     Site            order(77,81,83..85,87,92,110..113)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381544"
     Site            order(90..91,94..95,97..98,114,117,121,123..124,128,
                     130..131)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381544"
     CDS             1..133
                     /gene="Nhlh1"
                     /coded_by="NM_001105970.2:483..884"
                     /db_xref="GeneID:289230"
                     /db_xref="RGD:1310261"
ORIGIN      
        1 mmlnsdtmel dlppthsete sgfsdcgggp gpdgagsgdp gvgqvrslel gesgrkdlqh
       61 lsreerrrrr ratakyrtah atrerirvea fnlafaelrk llptlppdkk lskieilrla
      121 icyisylnhv ldv
//
LOCUS       NP_001424400            1487 aa            linear   ROD 08-APR-2025
DEFINITION  golgin subfamily A member 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424400 XP_006249625
VERSION     NP_001424400.1
DBSOURCE    REFSEQ: accession NM_001437471.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1487)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1487)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 1487)
  AUTHORS   Ohta,E., Misumi,Y., Sohda,M., Fujiwara,T., Yano,A. and Ikehara,Y.
  TITLE     Identification and characterization of GCP16, a novel acylated
            Golgi protein that interacts with GCP170
  JOURNAL   J Biol Chem 278 (51), 51957-51967 (2003)
   PUBMED   14522980
REFERENCE   4  (residues 1 to 1487)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
REFERENCE   5  (residues 1 to 1487)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
REFERENCE   6  (residues 1 to 1487)
  AUTHORS   Fritzler,M.J., Hamel,J.C., Ochs,R.L. and Chan,E.K.
  TITLE     Molecular characterization of two human autoantigens: unique cDNAs
            encoding 95- and 160-kD proteins of a putative family in the Golgi
            complex
  JOURNAL   J Exp Med 178 (1), 49-62 (1993)
   PUBMED   8315394
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006249625.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.345643.1,
                                           SRR26643293.85937.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1487
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..1487
                     /product="golgin subfamily A member 3 isoform 1"
                     /note="Golgin subfamily A member 3; golgi autoantigen,
                     golgin subfamily a, 3"
                     /calculated_mol_wt=166827
     Region          <338..986
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          663..1351
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1487
                     /gene="Golga3"
                     /coded_by="NM_001437471.1:231..4694"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:312077"
                     /db_xref="RGD:1305262"
ORIGIN      
        1 mdgasakqdg lwenksssdi sscpeaslet vgslaqlpdq qdtaqdgsve vnrvfkeegs
       61 pdrssqvpic qngqipdlql sldpttspvg pdastgvdgf hdnlrksqgt saegsvrkea
      121 lqslrlslpm qetqlcstas slplekeeqv rlqarkrlee qlmqyrvkrh rerssqpatk
      181 mklfstldpe lmlnpenlpr asavavtkey sflrtsvprg pkvgslglla hskekknsks
      241 skirsladyr tedpsdsggl gstadavgss lkqsrsstsv vsevspscet dnraesasla
      301 gdsvseadgn esdssshssf sargacavlg nvgtpgaayv vdgqeisaea lgqfpsikdv
      361 lqaaaaqhqd qnqeangevq srrdsicssv smessfaepq eellqilkdk rrlegqveal
      421 sleasqalqe kaelqaqlaa lstrlqaqve hshssqqkqd slssevdtlk qscwdleram
      481 tdlqnmleak naslassnnd lqvaeeqyqr lmakveamqr nilskdntvh dlrqqmtalq
      541 sqlqqvqler ttltsklqas qaeitslqqa rqwyqqqlal aqearvrlqg emahiqvgqm
      601 tqagllehlk lenvslshql tetqhrsike keriavqlqs ieadmldqea afvqireakt
      661 mveedlqrkl eefegereql qkvadaaasl eqqleqvklt lfqrdqqlaa lqqehldvik
      721 qltstqealq akgqslddlq trydelqarl eelqreadsr edaihflqne kivlevalhs
      781 arsdkeeldr garrleedte etsglleqlr qdvavksnqv ehlqqetatl rkqmqkvkeq
      841 flqqkvmvea yrrdaaskdq linelkatkk rldsemkelr qeliklhgek ktvevehsrl
      901 qkdmslvhqq maeleghlqs vqkerdemei hlqslkfdke qmialteane tlkkqieelq
      961 qeakkaiteq kqkmkrlgsd ltsaqkemkt khkayenavs ilsrrlqeal ankeatdael
     1021 nqlraqstgg ssdpalheki halevelqnv gqskilleke lqevitmtsq eleesrekvl
     1081 eledelqesr gfrrkikrle esnkklalel ehergkltgl gqsnaalreh nsiletalak
     1141 readlvqlnl qvqavlqrke eedrqmkqlv qalqisleke ktevsslkeq maaarveagh
     1201 nrrhfkaatl elsevkkelq akehlvqtlq aevdelqiqe gkhsqeiaqf qtelaeartq
     1261 lqllqkklee qrsqqptgsq emedlkweld qkereiqslk qqldltehqg kkelegtqqt
     1321 lqtikselet vqedlsetqk dkfmlqakvs elknnmktll qqnqqlkldl rrgaakkkep
     1381 kgessssspa tpikipdcpv paslleellr pppavskepl knlnsclqql kqemdslqrq
     1441 meehtitvhe slsswaqvea apaehaharg dtkvhnqnsv pgeglgq
//
LOCUS       NP_001424172              34 aa            linear   ROD 08-APR-2025
DEFINITION  HR upstream open reading frame [Rattus norvegicus].
ACCESSION   NP_001424172
VERSION     NP_001424172.1
DBSOURCE    REFSEQ: accession NM_001437243.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..34
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15"
     Protein         1..34
                     /product="HR upstream open reading frame"
                     /note="protein HRURF"
                     /calculated_mol_wt=3626
     CDS             1..34
                     /gene="Hrurf"
                     /coded_by="NM_001437243.1:1..105"
                     /db_xref="GeneID:134482144"
                     /db_xref="RGD:402444115"
ORIGIN      
        1 maqptasaqk lvrpiravcr ilqipesdps nlrp
//
LOCUS       NP_001424429            1838 aa            linear   ROD 08-APR-2025
DEFINITION  tight junction protein ZO-1 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424429 XP_038961224
VERSION     NP_001424429.1
DBSOURCE    REFSEQ: accession NM_001437500.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1838)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1838)
  AUTHORS   Lou,X., Mou,Q., Zhao,B., Huang,J., Yao,K., Luo,Z., Ye,M., Hu,Y.,
            Duan,Q., Li,X., Wen,Z., Chen,Z., Zhang,H. and Zhao,Y.
  TITLE     VIP Stabilizes the Cytoskeleton of Schlemm's Canal Endothelia via
            Reducing Caspase-3 Mediated ZO-1 Endolysosomal Degradation
  JOURNAL   Oxid Med Cell Longev 2021, 9397960 (2021)
   PUBMED   34552687
  REMARK    GeneRIF: VIP Stabilizes the Cytoskeleton of Schlemm's Canal
            Endothelia via Reducing Caspase-3 Mediated ZO-1 Endolysosomal
            Degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1838)
  AUTHORS   Xu,X., Zhang,X., Gao,L., Liu,C. and You,K.
  TITLE     Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and ZO-1
            Expression in Rat Kidney Accompanied by Impaired Proximal Tubular
            Development
  JOURNAL   Oxid Med Cell Longev 2020, 2641461 (2020)
   PUBMED   33343804
  REMARK    GeneRIF: Neonatal Hyperoxia Downregulates Claudin-4, Occludin, and
            ZO-1 Expression in Rat Kidney Accompanied by Impaired Proximal
            Tubular Development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1838)
  AUTHORS   Hou,Q., Huang,Y., Wang,Y., Liao,L., Zhu,Z., Zhang,W., Liu,Y.,
            Li,P., Chen,X. and Liu,F.
  TITLE     Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1
  JOURNAL   J Microbiol Biotechnol 30 (10), 1480-1487 (2020)
   PUBMED   32807750
  REMARK    GeneRIF: Lactobacillus casei LC01 Regulates Intestinal Epithelial
            Permeability through miR-144 Targeting of OCLN and ZO1.
REFERENCE   5  (residues 1 to 1838)
  AUTHORS   Ribeiro Hudson,A.S., Nascimento Soares,A.D., Coelho Horta,N.A.,
            Fuscaldi,L.L., Machado-Moreira,C.A., Soares,D.D., Coimbra,C.C., de
            Oliveira Poletini,M., Cardoso,V.N. and Wanner,S.P.
  TITLE     The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats
  JOURNAL   J Therm Biol 91, 102610 (2020)
   PUBMED   32716860
  REMARK    GeneRIF: The magnitude of physical exercise-induced hyperthermia is
            associated with changes in the intestinal permeability and
            expression of tight junction genes in rats.
REFERENCE   6  (residues 1 to 1838)
  AUTHORS   Kawajiri,A., Itoh,N., Fukata,M., Nakagawa,M., Yamaga,M.,
            Iwamatsu,A. and Kaibuchi,K.
  TITLE     Identification of a novel beta-catenin-interacting protein
  JOURNAL   Biochem Biophys Res Commun 273 (2), 712-717 (2000)
   PUBMED   10873669
REFERENCE   7  (residues 1 to 1838)
  AUTHORS   Kidson,S.H., Kume,T., Deng,K., Winfrey,V. and Hogan,B.L.
  TITLE     The forkhead/winged-helix gene, Mf1, is necessary for the normal
            development of the cornea and formation of the anterior chamber in
            the mouse eye
  JOURNAL   Dev Biol 211 (2), 306-322 (1999)
   PUBMED   10395790
REFERENCE   8  (residues 1 to 1838)
  AUTHORS   Toyofuku,T., Yabuki,M., Otsu,K., Kuzuya,T., Hori,M. and Tada,M.
  TITLE     Direct association of the gap junction protein connexin-43 with
            ZO-1 in cardiac myocytes
  JOURNAL   J Biol Chem 273 (21), 12725-12731 (1998)
   PUBMED   9582296
REFERENCE   9  (residues 1 to 1838)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
REFERENCE   10 (residues 1 to 1838)
  AUTHORS   Rajasekaran,A.K., Hojo,M., Huima,T. and Rodriguez-Boulan,E.
  TITLE     Catenins and zonula occludens-1 form a complex during early stages
            in the assembly of tight junctions
  JOURNAL   J Cell Biol 132 (3), 451-463 (1996)
   PUBMED   8636221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038961224.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1838
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1838
                     /product="tight junction protein ZO-1 isoform 8"
                     /note="zona occludens 1; tight junction protein ZO-1; zona
                     occludens protein 1; zonula occludens protein 1"
                     /calculated_mol_wt=205885
     Region          115..201
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(126..132,150,153,181,185,188..189)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          279..356
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(279..284,289..305,308..310,313,315..316,323,
                     331..332,334..335,347..353)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(290..296,302,305,335,339,342..343)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          515..594
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(525..531,541,544,573,577,580..581)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          610..674
                     /region_name="SH3_ZO-1"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 1; cd12026"
                     /db_xref="CDD:212959"
     Site            order(610..612,640..642,647,650,669)
                     /site_type="other"
                     /note="PDZ interface"
                     /db_xref="CDD:212959"
     Site            order(612..618,631..632,635,650,658..659,667..669,
                     673..674)
                     /site_type="other"
                     /note="GuK interface [polypeptide binding]"
                     /db_xref="CDD:212959"
     Site            order(618,620,623,627,648..649,668,670..671)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212959"
     Region          708..887
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Region          <1052..1659
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1722..1828
                     /region_name="ZU5"
                     /note="Domain present in ZO-1 and Unc5-like netrin
                     receptors; smart00218"
                     /db_xref="CDD:128514"
     CDS             1..1838
                     /gene="Tjp1"
                     /gene_synonym="ZO-1"
                     /coded_by="NM_001437500.1:65..5581"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:292994"
                     /db_xref="RGD:1306305"
ORIGIN      
        1 mrrleglclr rrrrrrgpar ersgdkmkyq kyltvlqmai gvtpsnrgsl lplkrklwvt
       61 pssenphgat snvsqgkpsl rrikgrlhrs ksldsidfce ltstameeta iweqhtvtlh
      121 rapgfgfgia isggrdnphf qsgetsivis dvlkggpaeg qlqendrvam vngvsmdnve
      181 hafavqqlrk sgknakitir rkkkvqipvs hpdpdpvsdn eddsydedvh dprsgrgala
      241 nrrgekswar drsasrdrsl sprsdrrsva ssqpakptkv tlvksrknee yglrlashif
      301 vkeisqdsla ardgniqegd vvlkingtvt enmsltdakt lierskgklk mvvqrderat
      361 llnvpdlsds ihsanaserd diseiqslas dhsvrshdrp prrsqsrspd qrsepsdhst
      421 qspqqpsngs lrsreeerms kpgavstpvk hvddhtpkav eevtvekhek qtptlpepkp
      481 vyaqvgqpdv dlpvspsdgv lpnsthedgi lrpsmklvkf rkgdsvglrl aggndvgifv
      541 agvledspaa kegleegdqi lrvnnvdftn iireeavlfl ldlpkgeevt ilaqkkkdvy
      601 rrivesdvgd sfyirthfey ekespyglsf nkgevfrvvd tlyngklgsw lairigknhk
      661 evergivpnk nraeqlasvq ytlpktaggd radfwrfrgl rsskrnlrks redlsaqpvq
      721 tkfpayervv lreagflrpv tifgpiadva reklareepd iyqiaksepr dagtdhrssg
      781 iirlhtikqi idqdkhalld vtpnavdrln yaqwypivvf lnpdskqgvk tmrmrlcpes
      841 rksarklyer shklrknnhh lftttinlns mndgwygalk eaiqqqqnql vwvsegkadg
      901 atsddldlhd drlsylsapg seysmystds rhtsdyedtd teggaytdqe ldetlndevg
      961 tppesaitrs sepvredssg mhhenqtypp yspqaqpqai hridspglkt asqqkaeass
     1021 pvpylspetn passasavkh nvnltnvnle eptpapptsh vsqadclgap speaphtmlr
     1081 degvslpshv dpakvyrkep ypeemmrqnh ilkqpalghp gqrldkepnp aydpqlpyve
     1141 kqasrdleqp pyryesssyt dqfsrnydhr lrfedrvpty edqwsyyddk qpyptrpfdt
     1201 qhprdldsrq hpeeasergy fqrfeepapl pydsrpryeq lprtstlrhe eqptsgyevh
     1261 nryrpeaqpy apagpkssep kqyfdqyprs yeqvpppgft sktghyeplh gaavvpplip
     1321 ssqhkpevlp satkpqpppp alteeeedpa mkpqsvltrv kmfenkrsas lenkkdvndt
     1381 asfkppevas kppsaslvgp kpvsqtqfse hdktlyrlpe pqkpqakppe divrsnhydp
     1441 eedeeyyrkq lsyfdrrsfe skppahipag hhsepakpvh sqsqpnfssy sskgkpetda
     1501 mdrsfsekry dptqampppp plpsqysqpv pplsnsslhi hskaaqsegn svsldfqnsy
     1561 iskpdpppsq skpatfrppt redppqtfyp qksfpdkasv ngaeqtqkti tpaynrftpk
     1621 pytssarpfe rkfespkfnh nllpsetvhk pelsskppps pktlmkahss tqppefdsgv
     1681 etfsvhtdkp kyqinnistm pkavpvspsa veedededgh tvvatargif nsnggvlssi
     1741 etgvsiiipq gaipegieqe iyfkvcrdns ilppldkekg etllsplvmc gphglkflkp
     1801 velrlphcdp ktwqnkclpg dpnylvganc vsvlidhf
//
LOCUS       NP_001424467             239 aa            linear   ROD 08-APR-2025
DEFINITION  membrane-spanning 4-domains subfamily A member 10 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424467 XP_063143035
VERSION     NP_001424467.1
DBSOURCE    REFSEQ: accession NM_001437538.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 3, 2025 this sequence version replaced XP_063143035.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.6310.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..239
                     /product="membrane-spanning 4-domains subfamily A member
                     10 isoform 1"
                     /note="membrane-spanning 4-domains, subfamily A, member
                     10"
                     /calculated_mol_wt=26192
     Region          57..190
                     /region_name="CD20"
                     /note="CD20-like family; pfam04103"
                     /db_xref="CDD:461174"
     CDS             1..239
                     /gene="Ms4a10"
                     /coded_by="NM_001437538.1:104..823"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293739"
                     /db_xref="RGD:1307478"
ORIGIN      
        1 msrqvptvta ssaigqasqw qspgpsqpaq kvaqpqhlvp dgylekpmeg sgllqklggf
       61 hiaiafahlt fggylistvk nlhlvvlkcw yplwgavsfl isgilatttv tfpktslkil
      121 cvvanvislf calagffvia kdlflenpfp wpiwrpypnp tsyiqrlelt llcftfleif
      181 lsastaitac rmkrphaedk ddtplipdtp melkglslgp ppsykdvtqg ntqheqnkr
//
LOCUS       NP_001424333             496 aa            linear   ROD 08-APR-2025
DEFINITION  myotilin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424333 XP_006254730
VERSION     NP_001424333.1
DBSOURCE    REFSEQ: accession NM_001437404.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   von Nandelstadh,P., Ismail,M., Gardin,C., Suila,H., Zara,I.,
            Belgrano,A., Valle,G., Carpen,O. and Faulkner,G.
  TITLE     A class III PDZ binding motif in the myotilin and FATZ families
            binds enigma family proteins: a common link for Z-disc myopathies
  JOURNAL   Mol Cell Biol 29 (3), 822-834 (2009)
   PUBMED   19047374
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Hauser,M.A., Horrigan,S.K., Salmikangas,P., Torian,U.M.,
            Viles,K.D., Dancel,R., Tim,R.W., Taivainen,A., Bartoloni,L.,
            Gilchrist,J.M., Stajich,J.M., Gaskell,P.C., Gilbert,J.R.,
            Vance,J.M., Pericak-Vance,M.A., Carpen,O., Westbrook,C.A. and
            Speer,M.C.
  TITLE     Myotilin is mutated in limb girdle muscular dystrophy 1A
  JOURNAL   Hum Mol Genet 9 (14), 2141-2147 (2000)
   PUBMED   10958653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254730.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.37680.1,
                                           SRR26360194.1722900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..496
                     /product="myotilin isoform 1"
                     /note="titin immunoglobulin domain protein (myotilin)"
                     /calculated_mol_wt=54992
     Region          248..338
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          278..282
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          347..438
                     /region_name="IgI_Myotilin_C"
                     /note="C-terminal immunoglobulin (Ig)-like domain of
                     myotilin; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05892"
                     /db_xref="CDD:409473"
     Region          347..350
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409473"
     Region          353..358
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409473"
     Region          363..370
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409473"
     Region          377..383
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409473"
     Region          384..387
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409473"
     Region          394..400
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409473"
     Region          403..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409473"
     Region          417..425
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409473"
     Region          427..438
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409473"
     CDS             1..496
                     /gene="Myot"
                     /gene_synonym="Ttid"
                     /coded_by="NM_001437404.1:154..1644"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:291605"
                     /db_xref="RGD:1310569"
ORIGIN      
        1 mfnyerpkhf iqsqnpcgsg lqppgpevss fpnqtkqssi viqprqcteq rfsasstvss
       61 hitvsssayp asqqlagpnp gqkvtatynq spasflssil psqpdysnsk ipstvdsnyq
      121 qssvhqpvna vssqaagakp tprtpdheiq gskealiqdl erklkckdtl lhngnqrlty
      181 eekmarrllg pqnaaavfqa qnsdvqdssq hnpeharlqv ptsqvrsrss sradandqda
      241 iqekfypprf iqvpenmsie egrfcrmdfk vsglpapdvs wylngrlvqs delhkmivse
      301 kgfhslifev vrasdagpya cvarnragea tftvqldvla kehkrapmfi ykpqskkvfe
      361 gesvklecqi saipppklfw krnnemvqfn tdrislyhdn agrvtllikd vnkkdagwyt
      421 vsavneagvt tcntrldvta rpnqtppapk qlrvrptfsk ylalngkgld vkqafnpege
      481 fqrlaaqsgl yeseel
//
LOCUS       NP_001424495             377 aa            linear   ROD 08-APR-2025
DEFINITION  CST complex subunit STN1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424495 XP_006231534
VERSION     NP_001424495.1
DBSOURCE    REFSEQ: accession NM_001437566.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Iles,M.M., Bishop,D.T., Taylor,J.C., Hayward,N.K., Brossard,M.,
            Cust,A.E., Dunning,A.M., Lee,J.E., Moses,E.K., Akslen,L.A.,
            Andresen,P.A., Avril,M.F., Azizi,E., Scarra,G.B., Brown,K.M.,
            Debniak,T., Elder,D.E., Friedman,E., Ghiorzo,P., Gillanders,E.M.,
            Goldstein,A.M., Gruis,N.A., Hansson,J., Harland,M., Helsing,P.,
            Hocevar,M., Hoiom,V., Ingvar,C., Kanetsky,P.A., Landi,M.T.,
            Lang,J., Lathrop,G.M., Lubinski,J., Mackie,R.M., Martin,N.G.,
            Molven,A., Montgomery,G.W., Novakovic,S., Olsson,H., Puig,S.,
            Puig-Butille,J.A., Radford-Smith,G.L., Randerson-Moor,J., van der
            Stoep,N., van Doorn,R., Whiteman,D.C., MacGregor,S., Pooley,K.A.,
            Ward,S.V., Mann,G.J., Amos,C.I., Pharoah,P.D., Demenais,F.,
            Law,M.H., Newton Bishop,J.A. and Barrett,J.H.
  CONSRTM   AMFS Investigators; IBD investigators; QMEGA and QTWIN
            Investigators; SDH Study Group; GenoMEL Consortium
  TITLE     The effect on melanoma risk of genes previously associated with
            telomere length
  JOURNAL   J Natl Cancer Inst 106 (10) (2014)
   PUBMED   25231748
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Wan,M., Qin,J., Songyang,Z. and Liu,D.
  TITLE     OB fold-containing protein 1 (OBFC1), a human homolog of yeast
            Stn1, associates with TPP1 and is implicated in telomere length
            regulation
  JOURNAL   J Biol Chem 284 (39), 26725-26731 (2009)
   PUBMED   19648609
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_006231534.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.6414.1,
                                           SRR26360172.995289.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..377
                     /product="CST complex subunit STN1 isoform 1"
                     /note="oligonucleotide/oligosaccharide-binding
                     fold-containing protein 1; CST complex subunit STN1;
                     suppressor of cdc thirteen homolog;
                     oligonucleotide/oligosaccharide-binding fold containing 1;
                     STN1, CST complex subunit"
                     /calculated_mol_wt=43281
     Region          65..165
                     /region_name="hOBFC1_like"
                     /note="A subfamily of OB folds similar to that found in
                     human OB fold containing protein 1 (hOBFC1). Members of
                     this group belong to the Replication protein A subunit 2
                     (RPA2) family of OB folds. RPA is a nuclear ssDNA binding
                     protein (SSB) which appears to be...; cd04483"
                     /db_xref="CDD:239929"
     Site            order(65,141,143,145,163)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239929"
     Site            order(70..72,81..84,86,92..94,96,140,147..149,156..158)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239929"
     Region          212..377
                     /region_name="STN1_2"
                     /note="CST, complex subunit STN1, C terminal; pfam09170"
                     /db_xref="CDD:462701"
     CDS             1..377
                     /gene="Stn1"
                     /gene_synonym="Obfc1"
                     /coded_by="NM_001437566.1:238..1371"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:294025"
                     /db_xref="RGD:1305637"
ORIGIN      
        1 mpepcllmqc esspkeeeip slfwgldpvf lafaklyikd ilemkesqqv pgmyfynghp
       61 irrvdimgav isvkeretfy sygvddatgv incvcwkrps naesssdpai lstsrelsmt
      121 sqlkklqeti eqktkigigd iirvrgyvrm freereicat iyykvddpvw nmqiarmlel
      181 pelykkvydq pfrnpalkee ealnskdtld lagltallse kvkeflqekk vqsfyqkele
      241 mveplqslas qpvthstcsd qvelkndaas dihsvfknal hllqekgfvf qrdggsdkly
      301 yvtskdkdlh qkiyqiiked cqkpnhvekg chlmhvlncv llnlrwdlnk avlqqvlell
      361 edqsdivstg dhyytaf
//
LOCUS       NP_001423852             187 aa            linear   ROD 08-APR-2025
DEFINITION  troponin I, slow skeletal muscle [Rattus norvegicus].
ACCESSION   NP_001423852
VERSION     NP_001423852.1
DBSOURCE    REFSEQ: accession NM_001436923.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Lin,Y.H., Schmidt,W., Fritz,K.S., Jeong,M.Y., Cammarato,A.,
            Foster,D.B., Biesiadecki,B.J., McKinsey,T.A. and Woulfe,K.C.
  TITLE     Site-specific acetyl-mimetic modification of cardiac troponin I
            modulates myofilament relaxation and calcium sensitivity
  JOURNAL   J Mol Cell Cardiol 139, 135-147 (2020)
   PUBMED   31981571
  REMARK    GeneRIF: Site-specific acetyl-mimetic modification of cardiac
            troponin I modulates myofilament relaxation and calcium
            sensitivity.
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Liu,W., Kuang,H., Xia,Y., Pope,Z.C., Wang,Z., Tang,C. and Yin,D.
  TITLE     Regular aerobic exercise-ameliorated troponin I carbonylation to
            mitigate aged rat soleus muscle functional recession
  JOURNAL   Exp Physiol 104 (5), 715-728 (2019)
   PUBMED   30820991
  REMARK    GeneRIF: regular aerobic exercise appeared to have antioxidant
            effects in the muscle that reduced TNNI1 slow carbonylation and
            promoted Ca(2+) /calmodulin-dependent protein kinase IIalpha and
            TNNI1 expression for skeletal muscle contraction regulation
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Potluri,P.R., Chamoun,J., Cooke,J.A., Badr,M., Guse,J.A., Rayes,R.,
            Cordina,N.M., McCamey,D., Fajer,P.G. and Brown,L.J.
  TITLE     The concerted movement of the switch region of Troponin I in
            cardiac muscle thin filaments as tracked by conventional and pulsed
            (DEER) EPR
  JOURNAL   J Struct Biol 200 (3), 376-387 (2017)
   PUBMED   28864299
  REMARK    GeneRIF: Troponin I interaction with calcium and Troponin C in
            cardiac muscle
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Cheng,Y., Rao,V., Tu,A.Y., Lindert,S., Wang,D., Oxenford,L.,
            McCulloch,A.D., McCammon,J.A. and Regnier,M.
  TITLE     Troponin I Mutations R146G and R21C Alter Cardiac Troponin
            Function, Contractile Properties, and Modulation by Protein Kinase
            A (PKA)-mediated Phosphorylation
  JOURNAL   J Biol Chem 290 (46), 27749-27766 (2015)
   PUBMED   26391394
  REMARK    GeneRIF: these results suggest that cTnI(R146G) and cTnI(R21C)
            blunt PKA modulation of activation and relaxation kinetics by
            prohibiting cardiac-specific N-terminal interaction with the cTnI
            inhibitory peptide.
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Christopher,B., Pizarro,G.O., Nicholson,B., Yuen,S., Hoit,B.D. and
            Ogut,O.
  TITLE     Reduced force production during low blood flow to the heart
            correlates with altered troponin I phosphorylation
  JOURNAL   J Muscle Res Cell Motil 30 (3-4), 111-123 (2009)
   PUBMED   19507043
  REMARK    GeneRIF: These findings suggest that altered TnI function, due to
            changes in the distribution of phosphorylated sites, is an early
            contributor to reduced contractility of the heart.
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Takimoto,E., Soergel,D.G., Janssen,P.M., Stull,L.B., Kass,D.A. and
            Murphy,A.M.
  TITLE     Frequency- and afterload-dependent cardiac modulation in vivo by
            troponin I with constitutively active protein kinase A
            phosphorylation sites
  JOURNAL   Circ Res 94 (4), 496-504 (2004)
   PUBMED   14726477
  REMARK    GeneRIF: A novel role is described for cardiac TnI PKA
            phosphorylation in the rate-dependent enhancement of systolic &
            diastolic function in vivo & afterload sensitivity of relaxation.
            This has implications for cardiac failure.
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Westfall,M.V. and Borton,A.R.
  TITLE     Role of troponin I phosphorylation in protein kinase C-mediated
            enhanced contractile performance of rat myocytes
  JOURNAL   J Biol Chem 278 (36), 33694-33700 (2003)
   PUBMED   12815045
  REMARK    GeneRIF: troponin I phosphorylation has a role in protein kinase
            C-mediated enhanced contractile performance of myocytes
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Metzger,J.M., Michele,D.E., Rust,E.M., Borton,A.R. and
            Westfall,M.V.
  TITLE     Sarcomere thin filament regulatory isoforms. Evidence of a dominant
            effect of slow skeletal troponin I on cardiac contraction
  JOURNAL   J Biol Chem 278 (15), 13118-13123 (2003)
   PUBMED   12551900
REFERENCE   9  (residues 1 to 187)
  AUTHORS   Huang,X., Pi,Y., Lee,K.J., Henkel,A.S., Gregg,R.G., Powers,P.A. and
            Walker,J.W.
  TITLE     Cardiac troponin I gene knockout: a mouse model of myocardial
            troponin I deficiency
  JOURNAL   Circ Res 84 (1), 1-8 (1999)
   PUBMED   9915769
REFERENCE   10 (residues 1 to 187)
  AUTHORS   Koppe,R.I., Hallauer,P.L., Karpati,G. and Hastings,K.E.
  TITLE     cDNA clone and expression analysis of rodent fast and slow skeletal
            muscle troponin I mRNAs
  JOURNAL   J Biol Chem 264 (24), 14327-14333 (1989)
   PUBMED   2760067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215749.1, FQ216094.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..187
                     /product="troponin I, slow skeletal muscle"
                     /note="troponin I, skeletal, slow 1; troponin I type 1
                     (skeletal, slow)"
                     /calculated_mol_wt=21567
     Region          2..48
                     /region_name="Involved in binding TNC"
                     /note="propagated from UniProtKB/Swiss-Prot (P13413.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylproline.
                     /evidence=ECO:0000250|UniProtKB:P02645; propagated from
                     UniProtKB/Swiss-Prot (P13413.2)"
     Region          15..146
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P13413.2)"
     Region          97..118
                     /region_name="Involved in binding TNC and actin"
                     /note="propagated from UniProtKB/Swiss-Prot (P13413.2)"
     CDS             1..187
                     /gene="Tnni1"
                     /coded_by="NM_001436923.1:124..687"
                     /db_xref="GeneID:29388"
                     /db_xref="RGD:621765"
ORIGIN      
        1 mpeverkski tasrklmlks lmlakakecw eqeheereae kvrylserip tlqtrglsls
       61 alqdlcrelh akvevvdeer ydieakclhn treikdlklk vldlrgkfkr pplrrvrvsa
      121 damlrallgs khkvsmdlra nlksvkkedt ekerpvevgd wrknveamsg megrkkmfda
      181 aksptsq
//
LOCUS       NP_001423901             275 aa            linear   ROD 08-APR-2025
DEFINITION  myb/SANT-like DNA-binding domain-containing protein 3 [Rattus
            norvegicus].
ACCESSION   NP_001423901 XP_038966169
VERSION     NP_001423901.1
DBSOURCE    REFSEQ: accession NM_001436972.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Oleskevich,S., Leck,K.J., Matthaei,K. and Hendry,I.A.
  TITLE     Enhanced serotonin response in the hippocampus of Galphaz protein
            knock-out mice
  JOURNAL   Neuroreport 16 (9), 921-925 (2005)
   PUBMED   15931062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Mar 25, 2025 this sequence version replaced XP_038966169.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.19279.1,
                                           SRR26643297.18947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..275
                     /product="myb/SANT-like DNA-binding domain-containing
                     protein 3"
                     /note="Myb/SANT-like DNA-binding domain containing 3"
                     /calculated_mol_wt=32245
     Region          10..87
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     CDS             1..275
                     /gene="Msantd3"
                     /gene_synonym="RGD1308165"
                     /coded_by="NM_001436972.1:203..1030"
                     /db_xref="GeneID:362516"
                     /db_xref="RGD:1308165"
ORIGIN      
        1 mqnneiikpa kyfseleksi llalvekyky vleckksdar tialkqrtwq alaheynsqp
       61 svslrdfkql kkcwenikar tkkimaherr ekvkrsgspl lsthvldkek igsmlpeqly
      121 flqsppeeep eyhqdaaaqe sfavsnrelc ddekefvhfp vcegtsqpep scsavritan
      181 knyrsktpqe galkkmheee hhqqmsilql qliqmnevhv akiqqierec emaeeehrik
      241 mevlnkkkmy werklqtftk ewpvssfnrp fpnsp
//
LOCUS       NP_001099468             377 aa            linear   ROD 08-APR-2025
DEFINITION  cyclin-I [Rattus norvegicus].
ACCESSION   NP_001099468 XP_001070498 XP_006250777 XP_214007
VERSION     NP_001099468.1
DBSOURCE    REFSEQ: accession NM_001105998.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On or before Mar 26, 2025 this sequence version replaced
            XP_006250777.1, XP_214007.2, XP_001070498.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223715.1, SRR26643288.50990.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..377
                     /product="cyclin-I"
                     /calculated_mol_wt=42120
     Region          44..142
                     /region_name="CYCLIN_CCNI-like"
                     /note="cyclin box found in cyclin-I (CCNI) and similar
                     proteins; cd20526"
                     /db_xref="CDD:410230"
     CDS             1..377
                     /gene="Ccni"
                     /coded_by="NM_001105998.2:562..1695"
                     /db_xref="GeneID:289500"
                     /db_xref="RGD:1309209"
ORIGIN      
        1 mkfpgplenq rlssllerai sreaqmwkvn vpkiptnqnv spsqrdeviq wlaklkyqfn
       61 lypetfalas slldrflatv kahpkylnci aiscfflaak tveedekipv lkvlardsfc
      121 gcssseilrm eriildklnw dlhtatpldf lhifhaiavs trpqllfslp rlspsqhlav
      181 ltkqllhcma cnqllqfkgs mlalamvsle meklipdwlp ltiellqkaq mdssqlihcr
      241 elvayhlsal qsslplnsvy vyrplkhtlv tcdkgafklh pssisgpdfs kdnskpevpv
      301 rgpaafhlhl pavsgckhts akrkveemev ddlydgikrl ynedsgsenv gsvcgtdlsr
      361 qeghaspcpp lqpvsvm
//
LOCUS       NP_001424371            1136 aa            linear   ROD 08-APR-2025
DEFINITION  activity-dependent neuroprotector homeobox protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001424371 XP_038952700
VERSION     NP_001424371.1
DBSOURCE    REFSEQ: accession NM_001437442.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Kushnir,M., Dresner,E., Mandel,S. and Gozes,I.
  TITLE     Silencing of the ADNP-family member, ADNP2, results in changes in
            cellular viability under oxidative stress
  JOURNAL   J Neurochem 105 (2), 537-545 (2008)
   PUBMED   18179478
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038952700.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.60330.1,
                                           SRR26643299.63451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..1136
                     /product="activity-dependent neuroprotector homeobox
                     protein 2"
                     /note="ADNP homeobox protein 2"
                     /calculated_mol_wt=123046
     Region          1..998
                     /region_name="ADNP_N"
                     /note="Activity-dependent neuroprotector homeobox protein
                     N-terminal; pfam19627"
                     /db_xref="CDD:466132"
     Region          1045..1098
                     /region_name="HOX"
                     /note="Homeodomain; smart00389"
                     /db_xref="CDD:197696"
     Site            order(1047..1050,1052,1069,1075,1088,1090..1091,
                     1094..1095,1097..1099,1101..1102)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(1048,1051,1091,1094..1095,1098)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     CDS             1..1136
                     /gene="Adnp2"
                     /gene_synonym="RGD1308279"
                     /coded_by="NM_001437442.1:140..3550"
                     /db_xref="GeneID:307236"
                     /db_xref="RGD:1308279"
ORIGIN      
        1 mfqipvqnld nirkvrkrvk gilvdiglds ckellkdlkg fdpgekyfcn tswgdvslwe
       61 psgkrakyrt kpyccslcry stkvltslkn hlhryheeea dqelmipcpn cpfasqpkvv
      121 gkhfrmfhap arkvqsytvn ilgeaktsrs dvisftclkc nfsntlyysm kkhvlvahfn
      181 ylinsyfglr teetgeqpka sdpvsvdkal pfdkyyckkc saiassqdal myhiltsdah
      241 rdlenklrsv isehikrtgf lkqmhiapkp vthialppns sapsiaappp cfqlalpqns
      301 qspgtvqsvt vapgtsgslt hsppttaqsh valvssslpv cqssltlqqs apppvflshs
      361 vplsqpvsts vlpltqplgp vnksvgtsll pvnqamcsvn qavrpgvlpl pkpmgpinrp
      421 vgpgvlpvgp svnsgvlqat spgvisvgra vpsgvlpagq vtpagvipgq tatsgvlptg
      481 qvvqssvlpv gqtapsrvlp pgqtvplrvl pagqvvppgl lspnqtvpsg vvpvnqgvns
      541 gvlqlsqpvt pgvlpvgppv rpgvlqlsps vstsilpvsq pvragtsqnt tfltsgsilr
      601 qliptgkqvn giptytlapv svtlpvpsag glaavgpppq vpvqflpsss gtqmgsslps
      661 lpspqvlvsp apsvfvqatp pvadanqalr qakqwktcpv cnelfpanvy qvhmevahtq
      721 seakssekpe perlaacapf lkwmrektvr clsckclvsq eelmhhllmh glgclfcpct
      781 fhdvrglveh srtkhlgkkr lsmdysnrgf qldldangnl lfphldfiti lpreklgere
      841 vylailagih skslvpvyvk vrpqpevapk ipnrqkltcp fcfgtfmaad ayelhlkerh
      901 hvmptvhtml rspafkcihc cgvytgnmtl gaiavhllrc rsapkdsssd lqaqpdfies
      961 sellmvngev ipestfplkr klpeghlgpe eqgdgdepql tvdtdaspgs ekglsavplk
     1021 rqknesrteg sgasddslqv laldpskygs rsyeekkqfl rdyfhkrpyp srkevellss
     1081 llwvwkidva sffgkrryic mkaikshkps vllgfdmsel knvkhrlnfe cesenl
//
LOCUS       NP_001102355             630 aa            linear   ROD 08-APR-2025
DEFINITION  kelch-like protein 14 [Rattus norvegicus].
ACCESSION   NP_001102355 XP_001054994 XP_038952927 XP_344653
VERSION     NP_001102355.1
DBSOURCE    REFSEQ: accession NM_001108885.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Giles,L.M., Li,L. and Chin,L.S.
  TITLE     Printor, a novel torsinA-interacting protein implicated in dystonia
            pathogenesis
  JOURNAL   J Biol Chem 284 (32), 21765-21775 (2009)
   PUBMED   19535332
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Apr 2, 2025 this sequence version replaced
            XP_038952927.1, XP_344653.3, XP_001054994.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.34523.1,
                                           SRR26360176.1282008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423, SAMN06680432
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..630
                     /product="kelch-like protein 14"
                     /note="kelch-like 14"
                     /calculated_mol_wt=70843
     Region          1..190
                     /region_name="BTB_POZ_KLHL14_printor"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 14 (KLHL14); cd18243"
                     /db_xref="CDD:349552"
     Region          183..284
                     /region_name="BACK_KLHL14"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 14 (KLHL14); cd18453"
                     /db_xref="CDD:350528"
     Region          326..579
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          365..412
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          416..460
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          463..508
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          562..604
                     /region_name="Kelch_1"
                     /note="Kelch motif; pfam01344"
                     /db_xref="CDD:396078"
     Region          562..604
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..630
                     /gene="Klhl14"
                     /gene_synonym="RGD1566178"
                     /coded_by="NM_001108885.2:423..2315"
                     /db_xref="GeneID:364823"
                     /db_xref="RGD:1566178"
ORIGIN      
        1 msrsgdrtst fdpshsdnll hglnllwrkq lfcdvtltaq gqqfhchkav lascsqyfrs
       61 lfsshpplgg gvggqdglga pkdqqqqqqp qqqpsqqqqq ppqeepgtps sspddkllts
      121 prainnlvlq gcssiglrlv leylytanvt lsldtveevl svskilhipq vtklcvqfln
      181 dqisvqnykq vckiaalhgl eetkklanky lvedvlllnf eemralldsl pppveselal
      241 fqmsvlwleh dretrmqyap dlmkrlrfal ipapelverv qsvdfmrtdp vcqkllldam
      301 nyhlmpfrqh crqslasrir snkkmlllvg glppgpdrlp snlvqyydde kktwkiltim
      361 pynsahhcvv evenflfvlg gedqwnpngk hstnfvsryd prfnswiqlp pmqerrasfy
      421 acrldkhlyv iggrnetgyl ssvecynldt newryvsslp qplaahagav hngkiyisgg
      481 vhngeyvpwl ycydpvmdvw arkqdmntkr aihtlavmnd rlyaiggnhl kgfshldvml
      541 vecydpkgdq wnilqtpile grsgpgcavl ddsiylvggy swsmgaykss ticycpekgt
      601 wtelegdvae plagpacatv ilpacvpynk
//
LOCUS       NP_001178596             573 aa            linear   ROD 08-APR-2025
DEFINITION  BICD family-like cargo adapter 1 [Rattus norvegicus].
ACCESSION   NP_001178596 XP_222240
VERSION     NP_001178596.1
DBSOURCE    REFSEQ: accession NM_001191667.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Schlager,M.A., Kapitein,L.C., Grigoriev,I., Burzynski,G.M.,
            Wulf,P.S., Keijzer,N., de Graaff,E., Fukuda,M., Shepherd,I.T.,
            Akhmanova,A. and Hoogenraad,C.C.
  TITLE     Pericentrosomal targeting of Rab6 secretory vesicles by
            Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis
  JOURNAL   EMBO J 29 (10), 1637-1651 (2010)
   PUBMED   20360680
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jul 17, 2010 this sequence version replaced XP_222240.5.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.551204.1,
                                           SRR22582424.85624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..573
                     /product="BICD family-like cargo adapter 1"
                     /note="bicaudal D-related protein 1; coiled-coil domain
                     containing 64"
                     /calculated_mol_wt=64728
     Region          <104..479
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..573
                     /gene="Bicdl1"
                     /gene_synonym="Ccdc64; RGD1310292"
                     /coded_by="NM_001191667.3:693..2414"
                     /db_xref="GeneID:304537"
                     /db_xref="RGD:1310292"
ORIGIN      
        1 msafclglag rasapaepds accmelpaga gdavrspaaa aalvsfpggp gelelaleee
       61 lallaagerp sdlgehpqae pgspaeghgp pppptqdpel lsvirqkekd lvlaarlgka
      121 llernqdmsr qyeqmhkelt dklehleqek helrrrfenr egewegrvse letdvkqlqd
      181 elerqqvhlr eadrektrav qelseqnqrl ldqlsrasev erqlsmqvha lkedfrekns
      241 stnqhiirle slqaeikmls drkrelehrl satleendll qgtveelqdr vlilerqghd
      301 kdlqlhqsql elqevrlsyr qlqvkveelt eerslqssaa tstsllseie qsmeaeeleq
      361 ereqlrlqlw eaycqvrylc shlrgndsad savstdssmd essetssakd vpagslrtal
      421 ndlkrliqsi vdgveptvtl lsvemtalke erdrlrvtse dkepkeqlqk airdrdeaia
      481 kkkavelela kckmdmmsln sqlldaiqqk lnlsqqleaw qddmhrvidr qlmdthlkeq
      541 srpaaafprg hgvgrgqeps tdgkrlfsff rki
//
LOCUS       NP_001009492             361 aa            linear   ROD 08-APR-2025
DEFINITION  2'-5' oligoadenylate synthetase 1E [Rattus norvegicus].
ACCESSION   NP_001009492 XP_579293
VERSION     NP_001009492.1
DBSOURCE    REFSEQ: accession NM_001009492.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579293.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY196698.1, SRR26643429.43391.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..361
                     /product="2'-5' oligoadenylate synthetase 1E"
                     /note="2'-5' oligoadenylate synthetase 1C; 2 ' -5 '
                     oligoadenylate synthetase 1C"
                     /calculated_mol_wt=43027
     Region          27..177
                     /region_name="NT_2-5OAS_ClassI-CCAase"
                     /note="Nucleotidyltransferase (NT) domain of
                     2'5'-oligoadenylate (2-5A)synthetase (2-5OAS) and class I
                     CCA-adding enzyme; cd05400"
                     /db_xref="CDD:143390"
     Site            order(62..64,67,69..71,76,78,128..129,132,149,163,167,170)
                     /site_type="active"
                     /db_xref="CDD:143390"
     Site            order(63..64,76,78,129,163,167,170)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143390"
     Site            order(76,78,149)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143390"
     Region          166..351
                     /region_name="OAS1_C"
                     /note="2'-5'-oligoadenylate synthetase 1, domain 2,
                     C-terminus; pfam10421"
                     /db_xref="CDD:463087"
     CDS             1..361
                     /gene="Oas1e"
                     /gene_synonym="Oas1c"
                     /coded_by="NM_001009492.3:361..1446"
                     /db_xref="GeneID:494201"
                     /db_xref="RGD:1359611"
ORIGIN      
        1 msrrlartpi wrldrfiedh llpdttflte vradidsica fltercfqga thpvrvsriv
       61 kggwfnkytm lkgrseatlv vflnnltcfe dqlkrreeft eeiwkhlcql qqekqfklnf
      121 evqsteqpds rtlsiklssp qlqqevefdv qpaydvlyel rdkddfnpdn yreiyarlir
      181 esttlemege fsvcftdlhq nflkyrapkl wniirlvkhw yqlckkrlky plppqyalel
      241 ltvyawergl edrpalhtgh cfrsvldlit eykklriywt wcyefkketf dylsrqikkd
      301 rpvildpadp trnvagsniq swhvlakeaa vwarssffrn sdmtfvngwk vsaqkqecvy
      361 q
//
LOCUS       NP_001424396             432 aa            linear   ROD 08-APR-2025
DEFINITION  GRAM domain-containing protein 2B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424396 XP_006254810
VERSION     NP_001424396.1
DBSOURCE    REFSEQ: accession NM_001437467.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006254810.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.2838225.1,
                                           SRR26643299.62840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11-q12.1"
     Protein         1..432
                     /product="GRAM domain-containing protein 2B isoform 2"
                     /note="GRAM domain-containing protein 3; GRAM
                     domain-containing protein 2B; GRAM domain containing 3"
                     /calculated_mol_wt=47915
     Region          122..214
                     /region_name="PH-GRAM_GRAMDC"
                     /note="GRAM domain-containing protein (GRAMDC) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13220"
                     /db_xref="CDD:275406"
     CDS             1..432
                     /gene="Gramd2b"
                     /gene_synonym="Gramd3; RGD1311016"
                     /coded_by="NM_001437467.1:129..1427"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307288"
                     /db_xref="RGD:1311016"
ORIGIN      
        1 mtelqqeved akpakvltkr egkvgpahse aengvedrkr fsksptaqsp tssveaespd
       61 qkrslglwsk ssfdgsnlls dkndcktesk adskterkks ssssqykanm hfhklfldvp
      121 teeplrqsft calqkeilyq gklfvsenwi cfhskvfgkd tkisipafsv tlikktktal
      181 lvpnaliiat vtdryifvsl lsrdstykll ksicghlent svgnspnpss aensfradrp
      241 sslrldfnde fsdldgvvqq rrqdlegyss sgsqtpesen srdfhvtesq tvlnvtkget
      301 kpprtdahgs rapdgkakil pahgqsetig ilhkmesrkc ptlrhilify aiivcaliis
      361 tfymryrint leerlgslts imdphsteqt apsslgsqvq lnvevlcqel tanivtleki
      421 qnnlqkllen gd
//
LOCUS       NP_036779               2005 aa            linear   ROD 08-APR-2025
DEFINITION  sodium channel protein type 2 subunit alpha [Rattus norvegicus].
ACCESSION   NP_036779
VERSION     NP_036779.2
DBSOURCE    REFSEQ: accession NM_012647.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2005)
  AUTHORS   van Cann,M., Kuzmenkov,A., Isensee,J., Andreev-Andrievskiy,A.,
            Peigneur,S., Khusainov,G., Berkut,A., Tytgat,J., Vassilevski,A. and
            Hucho,T.
  TITLE     Scorpion toxin MeuNaTxalpha-1 sensitizes primary nociceptors by
            selective modulation of voltage-gated sodium channels
  JOURNAL   FEBS J 288 (7), 2418-2435 (2021)
   PUBMED   33051988
  REMARK    GeneRIF: Scorpion toxin MeuNaTxalpha-1 sensitizes primary
            nociceptors by selective modulation of voltage-gated sodium
            channels.
REFERENCE   2  (residues 1 to 2005)
  AUTHORS   Middleton,S.J., Kneller,E.M., Chen,S., Ogiwara,I., Montal,M.,
            Yamakawa,K. and McHugh,T.J.
  TITLE     Altered hippocampal replay is associated with memory impairment in
            mice heterozygous for the Scn2a gene
  JOURNAL   Nat Neurosci 21 (7), 996-1003 (2018)
   PUBMED   29867081
REFERENCE   3  (residues 1 to 2005)
  AUTHORS   Johnson,K.W., Herold,K.F., Milner,T.A., Hemmings,H.C. Jr. and
            Platholi,J.
  TITLE     Sodium channel subtypes are differentially localized to pre- and
            post-synaptic sites in rat hippocampus
  JOURNAL   J Comp Neurol 525 (16), 3563-3578 (2017)
   PUBMED   28758202
  REMARK    GeneRIF: The Nav1.2 are highly expressed in axon terminals in
            central hilus compared to stratum radiatum and in dendrites and
            spines in stratum radiatum compared to central hilus .
REFERENCE   4  (residues 1 to 2005)
  AUTHORS   Berret,E., Barron,T., Xu,J., Debner,E., Kim,E.J. and Kim,J.H.
  TITLE     Oligodendroglial excitability mediated by glutamatergic inputs and
            Nav1.2 activation
  JOURNAL   Nat Commun 8 (1), 557 (2017)
   PUBMED   28916793
  REMARK    GeneRIF: Knockdown of Nav1.2 channels in pre-oligodendrocyte alters
            their morphology, reduces axon-oligodendrocyte interactions and
            impairs myelination.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2005)
  AUTHORS   Hovey,L., Fowler,C.A., Mahling,R., Lin,Z., Miller,M.S., Marx,D.C.,
            Yoder,J.B., Kim,E.H., Tefft,K.M., Waite,B.C., Feldkamp,M.D., Yu,L.
            and Shea,M.A.
  TITLE     Calcium triggers reversal of calmodulin on nested anti-parallel
            sites in the IQ motif of the neuronal voltage-dependent sodium
            channel NaV1.2
  JOURNAL   Biophys Chem 224, 1-19 (2017)
   PUBMED   28343066
  REMARK    GeneRIF: The polarity of (Ca(2+))2-CaMC relative to the IQ motif of
            NaV1.2 was opposite to that seen in apo CaMC-Nav1.2IQp (2KXW),
            revealing that CaMC recognizes nested, anti-parallel sites in
            Nav1.2IQp. (CaMC is C-domain residues of CaM, calmodulin).
REFERENCE   6  (residues 1 to 2005)
  AUTHORS   Sampo,B., Tricaud,N., Leveque,C., Seagar,M., Couraud,F. and
            Dargent,B.
  TITLE     Direct interaction between synaptotagmin and the intracellular loop
            I-II of neuronal voltage-sensitive sodium channels
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3666-3671 (2000)
   PUBMED   10737807
REFERENCE   7  (residues 1 to 2005)
  AUTHORS   Szpirer,C., Szpirer,J., Van Vooren,P., Tissir,F., Simon,J.S.,
            Koike,G., Jacob,H.J., Lander,E.S., Helou,K., Klinga-Levan,K. and
            Levan,G.
  TITLE     Gene-based anchoring of the rat genetic linkage and cytogenetic
            maps: new regional localizations, orientation of the linkage
            groups, and insights into mammalian chromosome evolution
  JOURNAL   Mamm Genome 9 (9), 721-734 (1998)
   PUBMED   9716657
REFERENCE   8  (residues 1 to 2005)
  AUTHORS   Kjaergaard,J.
  TITLE     [Hospitals--new charge by physicians on equally worthy leadership]
  JOURNAL   Sygeplejersken 92 (48), 38-39 (1992)
   PUBMED   1299025
REFERENCE   9  (residues 1 to 2005)
  AUTHORS   Noda,M. and Numa,S.
  TITLE     Structure and function of sodium channel
  JOURNAL   J Recept Res 7 (1-4), 467-497 (1987)
   PUBMED   2442385
REFERENCE   10 (residues 1 to 2005)
  AUTHORS   Noda,M., Ikeda,T., Kayano,T., Suzuki,H., Takeshima,H., Kurasaki,M.,
            Takahashi,H. and Numa,S.
  TITLE     Existence of distinct sodium channel messenger RNAs in rat brain
  JOURNAL   Nature 320 (6058), 188-192 (1986)
   PUBMED   3754035
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Nov 27, 2020 this sequence version replaced NP_036779.1.
            
            Summary: Voltage-gated sodium channels are transmembrane
            glycoprotein complexes composed of a large alpha subunit with four
            repeat domains, each of which is composed of six membrane-spanning
            segments, and one or more regulatory beta subunits. Voltage-gated
            sodium channels are responsible for the generation and propagation
            of action potentials in neurons and muscle. This gene encodes one
            member of the sodium channel alpha subunit gene family. In humans,
            variants of this gene are associated with seizure disorders and
            autism spectrum disorder. Mice homozygous for a knockout mutation
            die with severe hypoxia and extensive neuronal cell death, while
            gain of function mutations result in progressive seizure disorder.
            [provided by RefSeq, Nov 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X03639.1, M22254.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2005
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..2005
                     /product="sodium channel protein type 2 subunit alpha"
                     /note="sodium channel voltage-gated type II alpha
                     polypeptide; RIIA sodium channel protein; sodium channel
                     protein type II subunit alpha; sodium channel protein,
                     brain II subunit alpha; voltage-gated sodium channel
                     subunit alpha Nav1.2; sodium channel, voltage-gated, type
                     2, alpha 1 polypeptide; sodium channel, voltage-gated,
                     type II, alpha subunit; sodium channel, voltage-gated,
                     type 2, alpha 1 subunit; sodium channel, voltage-gated,
                     type II, alpha 1"
                     /calculated_mol_wt=227724
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          28..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          111..456
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          128..435
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            130..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            191..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            215..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            251..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            330
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            362
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            402..422
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          494..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1322892,
                     ECO:0000269|PubMed:20131913, ECO:0007744|PubMed:22673903;
                     Phosphoserine, by PKC, in vitro.
                     /evidence=ECO:0000269|PubMed:1322892,
                     ECO:0000269|PubMed:20131913, ECO:0007744|PubMed:22673903;
                     propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          558..709
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC, in vitro.
                     /evidence=ECO:0000269|PubMed:1322892; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC, in vitro.
                     /evidence=ECO:0000269|PubMed:1322892; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          591..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          741..1013
                     /region_name="II. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          758..971
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            760..778
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            790..809
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            824..843
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            846..863
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            880..898
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            909
                     /site_type="other"
                     /note="Binds SCN2B, via carbonyl oxygen.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            916
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA, via amide nitrogen.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          917..918
                     /region_name="Binds SCN2B.
                     /evidence=ECO:0000250|UniProtKB:Q99250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            920
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA, via carbonyl oxygen.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            945
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            949
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            962..982
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          997..1203
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          1120..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          1190..1504
                     /region_name="III. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          1207..1482
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1210..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1241..1259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1274..1292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1301..1319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1337..1356
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1374
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA, via amide nitrogen.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1429
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1443
                     /site_type="other"
                     /note="Binds Mu-conotoxin KIIIA.
                     /evidence=ECO:0000250|UniProtKB:Q99250; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1448..1469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          1474..1526
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1488..1491
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Site            1489
                     /site_type="other"
                     /note="Important for channel closure; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1506
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:1322892,
                     ECO:0000269|PubMed:1658937; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          1513..1811
                     /region_name="IV. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Region          1531..1786
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1533..1550
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1562..1580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1593..1610
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1624..1640
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1660..1677
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1753..1775
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Region          1933..2005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04775.1)"
     Site            1943
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1966
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     Site            1971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20131913; propagated from
                     UniProtKB/Swiss-Prot (P04775.1)"
     CDS             1..2005
                     /gene="Scn2a"
                     /gene_synonym="NachII; Nav1.2; RII/RIIA; RNSCPIIR; SCN;
                     Scn2a1; Scn2a2; ScpII"
                     /coded_by="NM_012647.3:208..6225"
                     /db_xref="GeneID:24766"
                     /db_xref="RGD:3632"
ORIGIN      
        1 marsvlvppg pdsfrfftre slaaieqria eekakrpkqe rkdeddengp kpnsdleagk
       61 slpfiygdip pemvsepled ldpyyinkkt fivlnkgkai srfsatsaly iltpfnpirk
      121 laikilvhsl fnvlimctil tncvfmtmsn ppdwtknvey tftgiytfes likilargfc
      181 ledftflrdp wnwldftvit fayvtefvnl gnvsalrtfr vlralktisv ipglktivga
      241 liqsvkklsd vmiltvfcls vfaliglqlf mgnlrnkclq wppdnstfei nitsffnnsl
      301 dwngtafnrt vnmfnwdeyi edkshfyfle gqndallcgn ssdagqcpeg yicvkagrnp
      361 nygytsfdtf swaflslfrl mtqdfwenly qltlraagkt ymiffvlvif lgsfylinli
      421 lavvamayee qnqatleeae qkeaefqqml eqlkkqqeea qaaaaaasae srdfsgaggi
      481 gvfsesssva sklsskseke lknrrkkkkq keqageeeke davrksased sirkkgfrfs
      541 legsrltyek rfssphqsll sirgslfspr rnsraslfsf kgrvkdigse ndfaddehst
      601 fedndsrrds lfvphrhger rpsnvsqasr asrgiptlpm ngkmhsavdc ngvvslvggp
      661 saltspvgql lpegtttete irkrrsssyh vsmdlledps rqramsmasi ltntmeelee
      721 srqkcppcwy kfanmcliwd cckpwlkvkh vvnlvvmdpf vdlaiticiv lntlfmameh
      781 ypmteqfssv lsvgnlvftg iftaemflki iamdpyyyfq egwnifdgfi vslslmelgl
      841 anveglsvlr sfrllrvfkl akswptlnml ikiignsvga lgnltlvlai ivfifavvgm
      901 qlfgksykec vckisndcel prwhmhdffh sflivfrvlc gewietmwdc mevagqtmcl
      961 tvfmmvmvig nlvvlnlfla lllssfssdn laatdddnem nnlqiavgrm qkgidfvkrk
     1021 irefiqkafv rkqkaldeik pledlnnkkd scisnhttie igkdlnylkd gngttsgigs
     1081 svekyvvdes dymsfinnps ltvtvpialg esdfenlnte efssesdmee skeklnatss
     1141 segstvdiga paegeqpeae peeslepeac ftedcvrkfk ccqisieegk gklwwnlrkt
     1201 cykivehnwf etfivfmill ssgalafedi yieqrktikt mleyadkvft yifilemllk
     1261 wvaygfqmyf tnawcwldfl ivdvslvslt analgyselg aikslrtlra lrplralsrf
     1321 egmrvvvnal lgaipsimnv llvclifwli fsimgvnlfa gkfyhcinyt tgemfdvsvv
     1381 nnysecqali esnqtarwkn vkvnfdnvgl gylsllqvat fkgwmdimya avdsrnvelq
     1441 pkyednlymy lyfvifiifg sfftlnlfig viidnfnqqk kkfggqdifm teeqkkyyna
     1501 mkklgskkpq kpiprpankf qgmvfdfvtk qvfdisimil iclnmvtmmv etddqsqemt
     1561 nilywinlvf ivlftgecvl klislrhyyf tigwnifdfv vvilsivgmf laeliekyfv
     1621 sptlfrvirl arigrilrli kgakgirtll falmmslpal fniglllflv mfiyaifgms
     1681 nfayvkrevg iddmfnfetf gnsmiclfqi ttsagwdgll apilnsgppd cdpekdhpgs
     1741 svkgdcgnps vgifffvsyi iisflvvvnm yiavilenfs vateesaepl seddfemfye
     1801 vwekfdpdat qfiefcklsd faaaldppll iakpnkvqli amdlpmvsgd rihcldilfa
     1861 ftkrvlgesg emdalriqme erfmasnpsk vsyepitttl krkqeevsai viqrayrryl
     1921 lkqkvkkvss iykkdkgked egtpikedii tdklnenstp ektdvtpstt sppsydsvtk
     1981 pekekfekdk sekedkgkdi reskk
//
LOCUS       NP_001424639             264 aa            linear   ROD 09-APR-2025
DEFINITION  COP9 signalosome complex subunit 7b [Rattus norvegicus].
ACCESSION   NP_001424639
VERSION     NP_001424639.1
DBSOURCE    REFSEQ: accession NM_001437710.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Sharon,M., Mao,H., Boeri Erba,E., Stephens,E., Zheng,N. and
            Robinson,C.V.
  TITLE     Symmetrical modularity of the COP9 signalosome complex suggests its
            multifunctionality
  JOURNAL   Structure 17 (1), 31-40 (2009)
   PUBMED   19141280
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.36206.1,
                                           SRR26643288.38574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..264
                     /product="COP9 signalosome complex subunit 7b"
                     /note="COP9 (constitutive photomorphogenic) homolog,
                     subunit 7b; COP9 constitutive photomorphogenic homolog
                     subunit 7B"
                     /calculated_mol_wt=29502
     Region          88..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     CDS             1..264
                     /gene="Cops7b"
                     /coded_by="NM_001437710.1:105..899"
                     /db_xref="GeneID:363273"
                     /db_xref="RGD:1306918"
ORIGIN      
        1 mageqkpssn lleqfillak gtsgsalttl isqvleapgv yvfgellela nvqelaegan
       61 aaylqllnlf aygtypdyia nkeslpelsa aqqnklkhlt ivslasrmkc ipysvllkdl
      121 emrnlreled liieavytdi iqgkldqrnq llevdfcigr diqkkdinni vktlhewcdg
      181 ceavllgieq qvlranqyke nhhrtqqqve aevsnikktl katasssaqe meqqlaerec
      241 pphteqrqpt kkmskvkglv ssrh
//
LOCUS       NP_445901               1077 aa            linear   ROD 09-APR-2025
DEFINITION  histone deacetylase 4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_445901 XP_001067733 XP_343630
VERSION     NP_445901.1
DBSOURCE    REFSEQ: accession NM_053449.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Gu,X., Li,F., Che,X., Wei,X. and Li,P.
  TITLE     HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model
  JOURNAL   BMC Musculoskelet Disord 25 (1), 467 (2024)
   PUBMED   38879481
  REMARK    GeneRIF: HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Zhang,D., Du,J., Yu,M. and Suo,L.
  TITLE     Urine-derived stem cells-extracellular vesicles ameliorate diabetic
            osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by delivering
            microRNA-26a-5p
  JOURNAL   Cell Biol Toxicol 39 (5), 2243-2257 (2023)
   PUBMED   35554780
  REMARK    GeneRIF: Urine-derived stem cells-extracellular vesicles ameliorate
            diabetic osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by
            delivering microRNA-26a-5p.
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Yang,Y., Wang,Z., Xu,Y., Liu,X., Sun,Y. and Li,W.
  TITLE     Knockdown of lncRNA H19 alleviates ox-LDL-induced HCAECs
            inflammation and injury by mediating miR-20a-5p/HDAC4 axis
  JOURNAL   Inflamm Res 71 (9), 1109-1121 (2022)
   PUBMED   35854140
  REMARK    Erratum:[Inflamm Res. 2023 Apr;72(4):893. doi:
            10.1007/s00011-023-01701-7. PMID: 36806965]
REFERENCE   4  (residues 1 to 1077)
  AUTHORS   Moreno-Ruperez,A., Priego,T., Gonzalez-Nicolas,M.A.,
            Lopez-Calderon,A., Lazaro,A. and Martin,A.I.
  TITLE     Role of Glucocorticoid Signaling and HDAC4 Activation in Diaphragm
            and Gastrocnemius Proteolytic Activity in Septic Rats
  JOURNAL   Int J Mol Sci 23 (7), 3641 (2022)
   PUBMED   35408999
  REMARK    GeneRIF: Role of Glucocorticoid Signaling and HDAC4 Activation in
            Diaphragm and Gastrocnemius Proteolytic Activity in Septic Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1077)
  AUTHORS   Wei,W., Chen,W. and He,N.
  TITLE     HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation
  JOURNAL   J Transl Med 19 (1), 258 (2021)
   PUBMED   34118928
  REMARK    GeneRIF: HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1077)
  AUTHORS   Fischle,W., Dequiedt,F., Hendzel,M.J., Guenther,M.G., Lazar,M.A.,
            Voelter,W. and Verdin,E.
  TITLE     Enzymatic activity associated with class II HDACs is dependent on a
            multiprotein complex containing HDAC3 and SMRT/N-CoR
  JOURNAL   Mol Cell 9 (1), 45-57 (2002)
   PUBMED   11804585
REFERENCE   7  (residues 1 to 1077)
  AUTHORS   Lu,J., McKinsey,T.A., Zhang,C.L. and Olson,E.N.
  TITLE     Regulation of skeletal myogenesis by association of the MEF2
            transcription factor with class II histone deacetylases
  JOURNAL   Mol Cell 6 (2), 233-244 (2000)
   PUBMED   10983972
REFERENCE   8  (residues 1 to 1077)
  AUTHORS   Grozinger,C.M. and Schreiber,S.L.
  TITLE     Regulation of histone deacetylase 4 and 5 and transcriptional
            activity by 14-3-3-dependent cellular localization
  JOURNAL   Proc Natl Acad Sci U S A 97 (14), 7835-7840 (2000)
   PUBMED   10869435
REFERENCE   9  (residues 1 to 1077)
  AUTHORS   Lemercier,C., Verdel,A., Galloo,B., Curtet,S., Brocard,M.P. and
            Khochbin,S.
  TITLE     mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A
            transcriptional activity
  JOURNAL   J Biol Chem 275 (20), 15594-15599 (2000)
   PUBMED   10748098
REFERENCE   10 (residues 1 to 1077)
  AUTHORS   Grozinger,C.M., Hassig,C.A. and Schreiber,S.L.
  TITLE     Three proteins define a class of human histone deacetylases related
            to yeast Hda1p
  JOURNAL   Proc Natl Acad Sci U S A 96 (9), 4868-4873 (1999)
   PUBMED   10220385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_001067733.2, XP_343630.4.
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.23282.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..1077
                     /product="histone deacetylase 4 isoform 3"
                     /EC_number="3.5.1.98"
                     /note="HD4"
                     /calculated_mol_wt=118522
     Region          <90..151
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(92,96,107..108,111,118,122..123)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          117..312
                     /region_name="Interaction with MEF2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          132..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          204..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZM9; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          239..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          348..353
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and 14-3-3 proteins.
                     /evidence=ECO:0000250|UniProtKB:P56524"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          508..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          542..582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          623..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          647..1050
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Region          653..1077
                     /region_name="Histone deacetylase. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            order(795..796,804..805,833,835,927,967)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Region          1044..1077
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          1052..1077
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     CDS             1..1077
                     /gene="Hdac4"
                     /coded_by="NM_053449.2:260..3493"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:363287"
                     /db_xref="RGD:619979"
ORIGIN      
        1 mssqshpdgl sgrdqpvell nparvnhmps tvdvatalpl qvapaavpmd lrldhqfslp
       61 lepalreqql qqellalkqk qqiqrqilia efqrqheqls rqheaqlheh ikqqqemlam
      121 khqqellehq rklerhrqeq elekqhreqk lqqlknkekg kesavastev kmklqefvln
      181 kkkalahrnl nhcmssdpry wygktqhssl dqssppqsgv sasynhpvlg mydakddfpl
      241 rktasepnlk lrsrlkqkva errsspllrr kdgpvatalk krpldvtdsa cssapgsgps
      301 spnsssgnvs tengiaptvp stpaetslah rlvtregsva plplytspsl pnitlglpat
      361 gpaagaagqq daerlalpal qqrislfpgt hltpylstsp lerdggaahn pllqhmvlle
      421 qpptqtplvt glgalplhtq slvgadrvsp sihklrqhrp lgrtqsaplp qnaqalqhlv
      481 iqqqhqqfle khkqqfqqqq lhlskmiskp sepprqpesh peeteeelre hqalldepyl
      541 drlpgqkeps lagvqvkqep ieseeeevea treaepsqrp ateqellfrq qallleqqri
      601 hqlrnyqasm eaagipvsfg shrplsraqs spasatfpms vqepptkprf ttglvydtlm
      661 lkhqctcgnt nshpehagri qsiwsrlqet glrgkcecir grkatleelq tvhseahtll
      721 ygtnplnrqk ldssltsvfv rlpcggvgvd sdtiwnevhs sgaarlavgc vvelvfkvat
      781 gelkngfavv rppghhaees tpmgfcyfns vaiaakllqq rlnvskiliv dwdvhhgngt
      841 qqafyndpnv lymslhrydd gnffpgsgap devgtgpgvg fnvnmaftgg ldppmgdaey
      901 laafrtvvmp ianefapdvv lvssgfdave ghptplggyn lsakcfgylt kqlmglaggr
      961 ivlalegghd ltaicdasea cvsallgnel eplpekvlhq rpnanavhsm ekvmgihsey
     1021 wrclqrlspt vghslieaqk ceneeaetvt amaslsvgvk paekrseeep meeeppl
//
LOCUS       NP_001424725             217 aa            linear   ROD 09-APR-2025
DEFINITION  BPI fold-containing family A member 3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424725 XP_038961812
VERSION     NP_001424725.1
DBSOURCE    REFSEQ: accession NM_001437796.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038961812.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3161349.1,
                                           SRR26360181.2037812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..217
                     /product="BPI fold-containing family A member 3 isoform 4"
                     /calculated_mol_wt=24037
     Region          1..148
                     /region_name="BPI"
                     /note="BPI/LBP/CETP domain; Bactericidal
                     permeability-increasing protein (BPI) /
                     Lipopolysaccharide-binding protein (LBP) / Cholesteryl
                     ester transfer protein (CETP) domain; binds to and
                     neutralizes lipopolysaccharides from the outer membrane of
                     Gram-negative...; cl00188"
                     /db_xref="CDD:412206"
     CDS             1..217
                     /gene="Bpifa3"
                     /gene_synonym="Splunc3"
                     /coded_by="NM_001437796.1:231..884"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:690402"
                     /db_xref="RGD:1596102"
ORIGIN      
        1 mrlldrlnvs gtvapgmvsw lisgmnfqqq qeisinitnv qldcggiqma fpkewfsani
       61 tlefdiefkl pfnsnilkth aqmglaaesw lekdefgrrk lvtgrcqmep ssdsasmtte
      121 aaspkmknfl hnlreslgkv ipnlvesqnr wllitlvspe svksllsgsr glplpaigqk
      181 evllveilrl sqcvasavpw kndpqvprhp vlsnnkl
//
LOCUS       NP_001178486             177 aa            linear   ROD 09-APR-2025
DEFINITION  synaptonemal complex central element protein 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001178486 XP_002728626
VERSION     NP_001178486.1
DBSOURCE    REFSEQ: accession NM_001191557.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Jordan,P.W., Karppinen,J. and Handel,M.A.
  TITLE     Polo-like kinase is required for synaptonemal complex disassembly
            and phosphorylation in mouse spermatocytes
  JOURNAL   J Cell Sci 125 (Pt 21), 5061-5072 (2012)
   PUBMED   22854038
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Modzelewski,A.J., Holmes,R.J., Hilz,S., Grimson,A. and Cohen,P.E.
  TITLE     AGO4 regulates entry into meiosis and influences silencing of sex
            chromosomes in the male mouse germline
  JOURNAL   Dev Cell 23 (2), 251-264 (2012)
   PUBMED   22863743
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Costa,Y., Speed,R., Ollinger,R., Alsheimer,M., Semple,C.A.,
            Gautier,P., Maratou,K., Novak,I., Hoog,C., Benavente,R. and
            Cooke,H.J.
  TITLE     Two novel proteins recruited by synaptonemal complex protein 1
            (SYCP1) are at the centre of meiosis
  JOURNAL   J Cell Sci 118 (Pt 12), 2755-2762 (2005)
   PUBMED   15944401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 17, 2010 this sequence version replaced XP_002728626.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..177
                     /product="synaptonemal complex central element protein 2
                     isoform 1"
                     /calculated_mol_wt=20169
     CDS             1..177
                     /gene="Syce2"
                     /gene_synonym="RGD1311867"
                     /coded_by="NM_001191557.2:43..576"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:364976"
                     /db_xref="RGD:1311867"
ORIGIN      
        1 merqgswlcs qvavppvelk dqeppaives gehqqnenhe etpssvapsa scqlpgpfss
       61 ldssietlkk kaqelienin esrqkdhalm tnfrdslkmk vsdlteklee rmyqvyshhs
      121 kiiqerlqef tqkmakishl emelkqvcqt vetmykdlcv qsevptseeq nykdgec
//
LOCUS       NP_001424692             598 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424692 XP_006248458
VERSION     NP_001424692.1
DBSOURCE    REFSEQ: accession NM_001437763.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248458.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1099090.1,
                                           SRR26360172.1133587.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..598
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 1"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=68499
     Region          239..>430
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          239..258
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          273..282
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          294..314
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          323..369
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..598
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437763.1:180..1976"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqravlkf lakcrkkkkl faswhglqel tdarrvelkq qvddyvkrhp gsqmsdvasr
      481 elhaqaqerl qhyfmgraie eraqqhreal maqistnieq lmkapslkea egkepeqfls
      541 rsrpvaakak qahlttlkhi qapwwkklge epgdemdvpk delsidlgtl figgtkpp
//
LOCUS       NP_001424619             729 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 10 [Rattus norvegicus].
ACCESSION   NP_001424619 XP_038943824
VERSION     NP_001424619.1
DBSOURCE    REFSEQ: accession NM_001437690.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943824.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.46637.1,
                                           SRR26360176.2234693.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..729
                     /product="dynamin-1-like protein isoform 10"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=81342
     Region          23..315
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,159,229,231..232,258..262,265)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,163,176,201,203,205..208,210..211,232,
                     234..237,261..263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            159..162
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(161..162,192..193)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            228..231
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          238..523
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            258..260
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          633..723
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..729
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437690.1:135..2324"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eendpatwkn srhlskgvea eewgkflhtk nklytdfdei
      121 rqeieneter isgnnkgvsp epihlkvfsp nvvnltlvdl pgmtkvpvgd qpkdielqir
      181 elilrfisnp nsiilavtaa ntdmatseal kisrevdpdg rrtlavitkl dlmdagtdam
      241 dvlmgrvipv klgiigvvnr sqldinnkks vtdsirdeya flqkkypsla nrngtkylar
      301 tlnrllmhhi rdclpelktr invlaaqyqs llnsygepvd dksatllqli tkfateycnt
      361 iegtakyiet selcggaric yifhetfgrt lesvdplggl ntidiltair natgprpalf
      421 vpevsfellv krqikrleep slrcvelvhe emqriiqhcs nystqellrf pklhdaivev
      481 vtcllrkrlp vtnemvhnlv aielayintk hpdfadacgl mnnnieeqrr nrlarelpsa
      541 vsrdkliqdn rretknvasa gggigdggri gdggqepttg nwrgmlktsk aeellaeeks
      601 kpipimpasp qkghavnlld vpvpvarkls areqrdcevi erliksyfli vrkniqdsvp
      661 kavmhflvnh vkdtlqselv gqlyksslld dlltesedma qrrkeaadml kalqgasqii
      721 aeirethlw
//
LOCUS       NP_001424644             817 aa            linear   ROD 09-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424644 XP_063126331
VERSION     NP_001424644.1
DBSOURCE    REFSEQ: accession NM_001437715.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Zhang,Z.Y., Bai,H.H., Guo,Z., Li,H.L., Diao,X.T., Zhang,T.Y.,
            Yao,L., Ma,J.J., Cao,Z., Li,Y.X., Bai,X., Chen,H.K., Suo,Z.W.,
            Yang,X. and Hu,X.D.
  TITLE     Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn
  JOURNAL   Sci Signal 13 (638) (2020)
   PUBMED   32606037
  REMARK    GeneRIF: Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Jeong,J.S., Kim,H.Y., Shin,B.S., Lee,A.R., Yoon,J.H., Hahm,T.S. and
            Lee,J.E.
  TITLE     Increased expression of the Cbl family of E3 ubiquitin ligases
            decreases Interleukin-2 production in a rat model of peripheral
            neuropathy
  JOURNAL   BMC Anesthesiol 18 (1), 87 (2018)
   PUBMED   30021515
  REMARK    GeneRIF: results suggest that ubiquitin and the E3 ubiquitin
            ligases c-Cbl and Cbl-b function as neuroimmune modulators in the
            subacute phase of neuropathic pain after nerve injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Uchida,T., Sakashita,Y., Kitahata,K., Yamashita,Y., Tomida,C.,
            Kimori,Y., Komatsu,A., Hirasaka,K., Ohno,A., Nakao,R.,
            Higashitani,A., Higashibata,A., Ishioka,N., Shimazu,T.,
            Kobayashi,T., Okumura,Y., Choi,I., Oarada,M., Mills,E.M.,
            Teshima-Kondo,S., Takeda,S., Tanaka,E., Tanaka,K., Sokabe,M. and
            Nikawa,T.
  TITLE     Reactive oxygen species upregulate expression of muscle
            atrophy-associated ubiquitin ligase Cbl-b in rat L6 skeletal muscle
            cells
  JOURNAL   Am J Physiol Cell Physiol 314 (6), C721-C731 (2018)
   PUBMED   29513566
  REMARK    GeneRIF: Under microgravity conditions, elevated ROS may be a
            crucial mechanotransducer in skeletal muscle cells, regulating
            muscle mass through Cbl-b expression activated by the ERK-Egr
            signaling pathway.
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Li,P., Liu,H.L., Zhang,Z.Q., Lv,X.D., Chang,Y.X., Wang,H.J., Ma,J.,
            Ma,Z.Y., Qu,X.J. and Teng,Y.E.
  TITLE     Single nucleotide polymorphisms of casitas B-lineage lymphoma
            proto-oncogene-b predict outcomes of patients with advanced
            non-small cell lung cancer after first-line platinum based doublet
            chemotherapy
  JOURNAL   J Thorac Dis 10 (3), 1635-1647 (2018)
   PUBMED   29707316
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Li,P., Liu,H., Zhang,Z., Lv,X., Wang,H., Ma,J., Ma,Z., Qu,X. and
            Teng,Y.E.
  TITLE     Expression and Comparison of Cbl-b in Lung Squamous Cell Carcinoma
            and Adenocarcinoma
  JOURNAL   Med Sci Monit 24, 623-635 (2018)
   PUBMED   29384143
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Thirone,A.C., Carvalheira,J.B., Hirata,A.E., Velloso,L.A. and
            Saad,M.J.
  TITLE     Regulation of Cbl-associated protein/Cbl pathway in muscle and
            adipose tissues of two animal models of insulin resistance
  JOURNAL   Endocrinology 145 (1), 281-293 (2004)
   PUBMED   14525909
  REMARK    GeneRIF: CAP-Cbl pathway may have a role in the modulation of
            adiposity in fasting and in monosodium glutamate treated rats.
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Zhang,W., Shao,Y., Fang,D., Huang,J., Jeon,M.S. and Liu,Y.C.
  TITLE     Negative regulation of T cell antigen receptor-mediated Crk-L-C3G
            signaling and cell adhesion by Cbl-b
  JOURNAL   J Biol Chem 278 (26), 23978-23983 (2003)
   PUBMED   12697763
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Nishio,H., Otsuka,M., Kinoshita,S., Tokuoka,T., Nakajima,M.,
            Noda,Y., Fukuyama,Y. and Suzuki,K.
  TITLE     Phosphorylation of c-Cbl protooncogene product following ethanol
            administration in rat cerebellum: possible involvement of Fyn
            kinase
  JOURNAL   Brain Res 950 (1-2), 203-209 (2002)
   PUBMED   12231245
  REMARK    GeneRIF: c-Cbl protooncogene product is tyrosine- phosphorylated in
            rat cerebellum in response to ethanol administration.
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Yokoi,N., Komeda,K., Wang,H.Y., Yano,H., Kitada,K., Saitoh,Y.,
            Seino,Y., Yasuda,K., Serikawa,T. and Seino,S.
  TITLE     Cblb is a major susceptibility gene for rat type 1 diabetes
            mellitus
  JOURNAL   Nat Genet 31 (4), 391-394 (2002)
   PUBMED   12118252
  REMARK    GeneRIF: we report the positional cloning of Iddm/kdp1 and identify
            a nonsense mutation in Cblb, a member of the Cbl/Sli family of
            ubiquitin-protein ligases.Cblb is a major susceptibility gene for
            rat type 1 diabetes mellitus
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Krawczyk,C., Bachmaier,K., Sasaki,T., Jones,R.G., Snapper,S.B.,
            Bouchard,D., Kozieradzki,I., Ohashi,P.S., Alt,F.W. and
            Penninger,J.M.
  TITLE     Cbl-b is a negative regulator of receptor clustering and raft
            aggregation in T cells
  JOURNAL   Immunity 13 (4), 463-473 (2000)
   PUBMED   11070165
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126331.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.30803.1,
                                           SRR26643292.45567.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..817
                     /product="E3 ubiquitin-protein ligase CBL-B isoform 3"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; SH3-binding
                     protein CBL-B; signal transduction protein CBL-B; casitas
                     B-lineage lymphoma proto-oncogene b; RING-type E3
                     ubiquitin transferase CBL-B; Casitas B-lineage lymphoma b;
                     Cas-Br-M (murine) ecotropic retroviral transforming
                     sequence b; Cbl proto-oncogene B, E3 ubiquitin protein
                     ligase; Cbl proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=91188
     Region          41..167
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          171..254
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          248..344
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(266,286,288..291,296,308,310)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(311..314,327..329)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          351..426
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(362..363,366,390,409..412)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(366..368,374..377,396,399..400,403,409..410,412)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          766..806
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(768..769,771..773,775..776,781,785)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..817
                     /gene="Cblb"
                     /coded_by="NM_001437715.1:163..2616"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:171136"
                     /db_xref="RGD:620535"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr rnltklslif shmlaeikai fpngqfqgdn fritkadaae
      181 fwrkffgdkt ivpwkvfrqc lhevhqissg leamalksti dltcndyisv fefdiftrlf
      241 qpwgsilrnw nflavthpgy mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv
      301 tgdgnilqti phnkplfqal idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy
      361 elycemgstf qlckicaend kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep
      421 iivdpfdprd egsrccsiid pfsipmldld ddddreeslm mnrlasvrkc tdrqnspvts
      481 pgssplaqrr kpqpdplqip hlslppvppr ldliqkgivr spcgsptgsp kvfsnghlap
      541 eeydvpprls ppppvtallp sikctgpian clsektrdtv eedddeykip sshpvslnsq
      601 pshchnvkpp vrscdnghci lngthgtpse mkksnipdlg iylkgedafd alppslpppp
      661 pparhslieh skppgsssrp ssgqdlfllp sdpffdpasg qvplpparra pgdgvksnra
      721 sqdydqlpss sdgsqaparp pkprprrtap eihhrkphgp eaalenvdak iaklmgegya
      781 feevkralei aqnnlevars ilrefafppp vsprlnl
//
LOCUS       NP_001424615             744 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424615 XP_038943820
VERSION     NP_001424615.1
DBSOURCE    REFSEQ: accession NM_001437686.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 744)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 744)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 744)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 744)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 744)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 744)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943820.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.67896.1,
                                           SRR26360176.219734.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..744
                     /product="dynamin-1-like protein isoform 6"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=82409
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          23..315
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,159,229,231..232,258..262,265)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,163,176,201,203,205..208,210..211,232,
                     234..237,261..263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          58..60
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          159..162
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            159..162
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(161..162,192..193)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          228..231
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            228..231
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          238..523
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          258..261
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            258..260
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          357..502
                     /region_name="Middle domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            593
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            594
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            605
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K1M6; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            615
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:17301055,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK1 and PKA.
                     /evidence=ECO:0000269|PubMed:28463107; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          648..738
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          662..676
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     CDS             1..744
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437686.1:135..2369"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eendpatwkn srhlskgvea eewgkflhtk nklytdfdei
      121 rqeieneter isgnnkgvsp epihlkvfsp nvvnltlvdl pgmtkvpvgd qpkdielqir
      181 elilrfisnp nsiilavtaa ntdmatseal kisrevdpdg rrtlavitkl dlmdagtdam
      241 dvlmgrvipv klgiigvvnr sqldinnkks vtdsirdeya flqkkypsla nrngtkylar
      301 tlnrllmhhi rdclpelktr invlaaqyqs llnsygepvd dksatllqli tkfateycnt
      361 iegtakyiet selcggaric yifhetfgrt lesvdplggl ntidiltair natgprpalf
      421 vpevsfellv krqikrleep slrcvelvhe emqriiqhcs nystqellrf pklhdaivev
      481 vtcllrkrlp vtnemvhnlv aielayintk hpdfadacgl mnnnieeqrr nrlarelpsa
      541 vsrdksskvp salapasqep spaasaeadg kvasagggig dggrigdggq epttgnwrgm
      601 lktskaeell aeekskpipi mpaspqkgha vnlldvpvpv arklsareqr dcevierlik
      661 syflivrkni qdsvpkavmh flvnhvkdtl qselvgqlyk ssllddllte sedmaqrrke
      721 aadmlkalqg asqiiaeire thlw
//
LOCUS       NP_001424680            1119 aa            linear   ROD 09-APR-2025
DEFINITION  sodium/hydrogen exchanger 10 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424680 XP_038944110
VERSION     NP_001424680.1
DBSOURCE    REFSEQ: accession NM_001437751.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Wang,D., King,S.M., Quill,T.A., Doolittle,L.K. and Garbers,D.L.
  TITLE     A new sperm-specific Na+/H+ exchanger required for sperm motility
            and fertility
  JOURNAL   Nat Cell Biol 5 (12), 1117-1122 (2003)
   PUBMED   14634667
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038944110.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.69084.1,
                                           SRR26360181.2694227.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1119
                     /product="sodium/hydrogen exchanger 10 isoform 2"
                     /note="sperm-specific sodium proton exchanger;
                     sodium/hydrogen exchanger 10; solute carrier family 9,
                     member 10; solute carrier family 9, subfamily C
                     (Na+-transporting carboxylic acid decarboxylase), member
                     1"
                     /calculated_mol_wt=128858
     Region          37..556
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          831..958
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(912..913,922..924)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(944..946,951..953)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..1119
                     /gene="Slc9c1"
                     /gene_synonym="Gm610; Slc9a10"
                     /coded_by="NM_001437751.1:341..3700"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:288117"
                     /db_xref="RGD:1309075"
ORIGIN      
        1 meevfenltt thnvklsnaw ldllksvfls tpqdlpeiil ilslictiga flnmhlkdfp
       61 iplpvilfli gccfeilsfa stqiqlyada iqwmdpdmff giftpviifn vafdmdiyml
      121 qklfwqilli tipgfminyt lilwylqsvn klslktipwl lfsavlissd pmltsasird
      181 lglsrsltnl ingeslltsv isliiysavv qisfkskhmn htlahkvmst awsylvesfi
      241 tgilitkaiq lwmatifgdd vnhitlifsv lylifyvcel igmsgiftla tiglflnsts
      301 fkpgveafll efwnclsfig flmvftfigl lipahtylyi sfsdvyysln iyftlivlrl
      361 lvfllmspil srlghgfswr wafimvwsem kgtpninmal llaysdvslg serersqilf
      421 hgvsvcvitl ivnrfilpma viklglrdvt stkyksvyyt fqhfqeltks tamalkfdkd
      481 lanadwnmvd kaiilqnpya lnqeettehq kvkcpdcnke idetlnieam elanrrllsa
      541 qiasyqrqyr neilsqsamq vlvgaagsfg ekkgeymspe niknyseskk llsflrklll
      601 nwvyntkkdk gvpsrymflh achsivftne feytgyiavl mntypmiicw isrlkdiyqy
      661 eikcanyyfl tfyileallk litpkllqvi dkrmsqqisf ryailkgyvq gemdvlniid
      721 qiasskqakq illkrvirnm dhamkelgyl eydhpeiavt mktkeevnvm lnmareivka
      781 frskgiihkv egaeinklim akkkqvlelq sviqplnvee apyyipwlse dpeaisfiqe
      841 kakvvtfdcg nnifeegdep egiyviisgm vklkrskphl emdrvssese vaqtrsytlp
      901 hteyllsgei igelncltke rmqysatckt vvetyfipis hlyegfekky pnmkykmwqk
      961 iglaitaqki renlsfedwn ykmqlklcnv fvrdipkttk tdiydetvth vvlihgsaed
     1021 cqlrkiykap flipvtchqi qgleeftkvm iiqtsvavrk frwnvkkynp prrismkpds
     1081 tesletlnes seddedkken eeneeyledi idissvskk
//
LOCUS       NP_001424635             432 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424635 XP_063126326
VERSION     NP_001424635.1
DBSOURCE    REFSEQ: accession NM_001437706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126326.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.42961.1,
                                           SRR26643292.45364.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..432
                     /product="transcriptional regulator ERG isoform 4"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=48596
     Region          115..198
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          263..346
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..432
                     /gene="Erg"
                     /coded_by="NM_001437706.1:155..1453"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 mastikeals vvsedqslfe caygtphlak temtassssd ygqtskmspr vpqqdwlsqp
       61 parvtikmec npsqvngsrn spdecsvtkg gkmvgspdtv gmsygsymee khmpppnmtt
      121 nerrvivpad ptlwstdhvr qwlewavkey glldvdvllf qnidgkelck mtkddfqrlt
      181 psynadills hlhylretpl phltsddvdk alqnsprlmh arntaaqpsp stvpktedqr
      241 pqldpyqilg ptssrlanpg sgqiqlwqfl lellsdssns ncitwegtng efkmtdpdev
      301 arrwgerksk pnmnydklsr alryyydkni mtkvhgkrya ykfdfhgiaq alqphppess
      361 lykypsdlpy mgsyhthpqk mnfvaphppa lpvtsssffa tpnpywnspt ggiypntrlp
      421 ashmpshlgt yy
//
LOCUS       NP_001424722             178 aa            linear   ROD 09-APR-2025
DEFINITION  uncharacterized protein C20orf144 homolog isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424722 XP_006235419
VERSION     NP_001424722.1
DBSOURCE    REFSEQ: accession NM_001437793.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006235419.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2786005.1,
                                           SRR26643293.19794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..178
                     /product="uncharacterized protein C20orf144 homolog
                     isoform 3"
                     /note="uncharacterized protein C20orf144 homolog"
                     /calculated_mol_wt=19848
     Region          1..170
                     /region_name="Bclt"
                     /note="Putative Bcl-2 like protein of testis; pfam15318"
                     /db_xref="CDD:434628"
     CDS             1..178
                     /gene="C3h20orf144"
                     /gene_synonym="RGD1561517"
                     /coded_by="NM_001437793.1:54..590"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:499927"
                     /db_xref="RGD:1561517"
ORIGIN      
        1 mgnsgshkrt kapnqaskdr ppdmdkarhk qffshlkrkk pstkivllfp ldkrqqlaea
       61 aagpfvrpvr paedplgapt cfpatvapml rgagdgvdrr egararemkr ilvlllqlda
      121 rlqeegrrva grpgggakaq qywqplyahl ltqreacgeg dpreeqprkr rrcprprp
//
LOCUS       NP_001424698             442 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424698 XP_063126594
VERSION     NP_001424698.1
DBSOURCE    REFSEQ: accession NM_001437769.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126594.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.66961.1,
                                           SRR26360194.1665223.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..442
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 2"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=50542
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <293..>437
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <385..>425
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..442
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437769.1:123..1451"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqraasik isslglerwl sg
//
LOCUS       NP_001424629             556 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 19 [Rattus norvegicus].
ACCESSION   NP_001424629 XP_063126309
VERSION     NP_001424629.1
DBSOURCE    REFSEQ: accession NM_001437700.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126309.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1889992.1,
                                           SRR26643290.40176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..556
                     /product="dynamin-1-like protein isoform 19"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=62022
     Region          <1..106
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          76..361
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          460..550
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..556
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437700.1:424..2094"
                     /note="isoform 19 is encoded by transcript variant 20"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mtkvpvgdqp kdielqirel ilrfisnpns iilavtaant dmatsealki srevdpdgrr
       61 tlavitkldl mdagtdamdv lmgrvipvkl giigvvnrsq ldinnkksvt dsirdeyafl
      121 qkkypslanr ngtkylartl nrllmhhird clpelktrin vlaaqyqsll nsygepvddk
      181 satllqlitk fateycntie gtakyietse lcggaricyi fhetfgrtle svdplgglnt
      241 idiltairna tgprpalfvp evsfellvkr qikrleepsl rcvelvheem qriiqhcsny
      301 stqellrfpk lhdaivevvt cllrkrlpvt nemvhnlvai elayintkhp dfadacglmn
      361 nnieeqrrnr larelpsavs rdkvasaggg igdggrigdg gqepttgnwr gmlktskaee
      421 llaeekskpi pimpaspqkg havnlldvpv pvarklsare qrdcevierl iksyflivrk
      481 niqdsvpkav mhflvnhvkd tlqselvgql ykssllddll tesedmaqrr keaadmlkal
      541 qgasqiiaei rethlw
//
LOCUS       NP_001424617             737 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424617 XP_063126304
VERSION     NP_001424617.1
DBSOURCE    REFSEQ: accession NM_001437688.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126304.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.816473.1,
                                           SRR26360190.161875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..737
                     /product="dynamin-1-like protein isoform 8"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=81720
     Region          23..308
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,152,222,224..225,251..255,258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,156,169,194,196,198..201,203..204,225,
                     227..230,254..256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            152..155
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(154..155,185..186)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            221..224
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          231..516
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            251..253
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          641..731
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..737
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437688.1:135..2348"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswr veaeewgkfl htknklytdf deirqeiene
      121 terisgnnkg vspepihlkv fspnvvnltl vdlpgmtkvp vgdqpkdiel qirelilrfi
      181 snpnsiilav taantdmats ealkisrevd pdgrrtlavi tkldlmdagt damdvlmgrv
      241 ipvklgiigv vnrsqldinn kksvtdsird eyaflqkkyp slanrngtky lartlnrllm
      301 hhirdclpel ktrinvlaaq yqsllnsyge pvddksatll qlitkfatey cntiegtaky
      361 ietselcgga ricyifhetf grtlesvdpl gglntidilt airnatgprp alfvpevsfe
      421 llvkrqikrl eepslrcvel vheemqriiq hcsnystqel lrfpklhdai vevvtcllrk
      481 rlpvtnemvh nlvaielayi ntkhpdfada cglmnnniee qrrnrlarel psavsrdkss
      541 kvpsalapas qepspaasae adgkvasagg gigdggrigd ggqepttgnw rgmlktskae
      601 ellaeekskp ipimpaspqk ghavnlldvp vpvarklsar eqrdcevier liksyflivr
      661 kniqdsvpka vmhflvnhvk dtlqselvgq lykssllddl ltesedmaqr rkeaadmlka
      721 lqgasqiiae irethlw
//
LOCUS       NP_001424694             598 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424694 XP_008766952
VERSION     NP_001424694.1
DBSOURCE    REFSEQ: accession NM_001437765.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_008766952.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.48203.1,
                                           SRR26360172.999044.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..598
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 1"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=68499
     Region          239..>430
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          239..258
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          273..282
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          294..314
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          323..369
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..598
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437765.1:128..1924"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqravlkf lakcrkkkkl faswhglqel tdarrvelkq qvddyvkrhp gsqmsdvasr
      481 elhaqaqerl qhyfmgraie eraqqhreal maqistnieq lmkapslkea egkepeqfls
      541 rsrpvaakak qahlttlkhi qapwwkklge epgdemdvpk delsidlgtl figgtkpp
//
LOCUS       NP_001424718             408 aa            linear   ROD 09-APR-2025
DEFINITION  paired box protein Pax-2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424718 XP_038964961
VERSION     NP_001424718.1
DBSOURCE    REFSEQ: accession NM_001437789.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Ribeiro,P.C., Lojudice,F.H., Fernandes-Charpiot,I.M.M.,
            Baptista,M.A.S.F., de Almeida Araujo,S., Mendes,G.E.F.,
            Sogayar,M.C., Abbud-Filho,M. and Caldas,H.C.
  TITLE     Therapeutic potential of human induced pluripotent stem cells and
            renal progenitor cells in experimental chronic kidney disease
  JOURNAL   Stem Cell Res Ther 11 (1), 530 (2020)
   PUBMED   33298161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Wang,X.L., Hou,L., Zhao,C.G., Tang,Y., Zhang,B., Zhao,J.Y. and
            Wu,Y.B.
  TITLE     Screening of genes involved in epithelial-mesenchymal transition
            and differential expression of complement-related genes induced by
            PAX2 in renal tubules
  JOURNAL   Nephrology (Carlton) 24 (2), 263-271 (2019)
   PUBMED   29280536
  REMARK    GeneRIF: Pax2 overexpression by kidney tubule cells alters the
            expression of complement system proteins to induce
            epithelial-mesenchymal transition.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Hou,L., Du,Y., Zhao,C. and Wu,Y.
  TITLE     PAX2 may induce ADAM10 expression in renal tubular epithelial cells
            and contribute to epithelial-to-mesenchymal transition
  JOURNAL   Int Urol Nephrol 50 (9), 1729-1741 (2018)
   PUBMED   30117015
  REMARK    GeneRIF: PAX2 directly increased expression of ADAM10, the presence
            of which contributed to EMT in renal tubular epithelia and hence
            plays an important role in renal fibrosis.
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Larsson,M.
  TITLE     Pax2 is persistently expressed by GABAergic neurons throughout the
            adult rat dorsal horn
  JOURNAL   Neurosci Lett 638, 96-101 (2017)
   PUBMED   27939388
  REMARK    GeneRIF: Persistent Pax2 expression may be required to maintain a
            GABAergic phenotype.
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Jiang,Y., Jiang,T., Ouyang,J., Zhou,Q., Liang,Y., Cui,Y., Chen,P.
            and Huang,B.
  TITLE     Cell atavistic transition: Paired box 2 re-expression occurs in
            mature tubular epithelial cells during acute kidney injury and is
            regulated by Angiotensin II
  JOURNAL   PLoS One 9 (4), e93563 (2014)
   PUBMED   24710423
  REMARK    GeneRIF: Those findings suggest that mature TECs can
            trans-differentiate into progenitor-like cells by 'atavistic
            transition', which may participate in the recovery of tissue
            structure and Pax2 may play a pivotal role in this process.
            Erratum:[PLoS One. 2015 May 06;10(5):e0127718. doi:
            10.1371/journal.pone.0127718. PMID: 25945929]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Ryan,G., Steele-Perkins,V., Morris,J.F., Rauscher,F.J. 3rd and
            Dressler,G.R.
  TITLE     Repression of Pax-2 by WT1 during normal kidney development
  JOURNAL   Development 121 (3), 867-875 (1995)
   PUBMED   7720589
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Eccles,M.R., Yun,K., Reeve,A.E. and Fidler,A.E.
  TITLE     Comparative in situ hybridization analysis of PAX2, PAX8, and WT1
            gene transcription in human fetal kidney and Wilms' tumors
  JOURNAL   Am J Pathol 146 (1), 40-45 (1995)
   PUBMED   7856737
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Sharma,P.M., Bowman,M., Yu,B.F. and Sukumar,S.
  TITLE     A rodent model for Wilms tumors: embryonal kidney neoplasms induced
            by N-nitroso-N'-methylurea
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9931-9935 (1994)
   PUBMED   7937920
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Poleev,A., Fickenscher,H., Mundlos,S., Winterpacht,A., Zabel,B.,
            Fidler,A., Gruss,P. and Plachov,D.
  TITLE     PAX8, a human paired box gene: isolation and expression in
            developing thyroid, kidney and Wilms' tumors
  JOURNAL   Development 116 (3), 611-623 (1992)
   PUBMED   1337742
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Plachov,D., Chowdhury,K., Walther,C., Simon,D., Guenet,J.L. and
            Gruss,P.
  TITLE     Pax8, a murine paired box gene expressed in the developing
            excretory system and thyroid gland
  JOURNAL   Development 110 (2), 643-651 (1990)
   PUBMED   1723950
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038964961.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.3976.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..408
                     /product="paired box protein Pax-2 isoform 1"
                     /note="paired box protein Pax-2; paired box gene 2; paired
                     box protein 2; paired box homeotic gene 2"
                     /calculated_mol_wt=43736
     Region          15..139
                     /region_name="PAX"
                     /note="Paired Box domain; smart00351"
                     /db_xref="CDD:128645"
     Site            order(20..21,26,28..30,32,37,49,51,60,63,65..66,70,79..85,
                     87..90,109..111,130,132..133,136,139)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238076"
     Region          281..>366
                     /region_name="Pax2_C"
                     /note="Paired-box protein 2 C terminal; pfam12403"
                     /db_xref="CDD:463563"
     CDS             1..408
                     /gene="Pax2"
                     /gene_synonym="Pax-2"
                     /coded_by="NM_001437789.1:692..1918"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293992"
                     /db_xref="RGD:1305568"
ORIGIN      
        1 mdmhckadpf samhrhggvn qlggvfvngr plpdvvrqri velahqgvrp cdisrqlrvs
       61 hgcvskilgr yyetgsikpg viggskpkva tpkvvdkiae ykrqnptmfa weirdrllae
      121 gicdndtvps vssinriirt kvqqpfhptp dgagtgvtap ghtivpstas ppvssasndp
      181 vgsysingil giprsngekr kreedvsegs vpngdsqsgv dslrkhlrad tftqqqleal
      241 drvferpsyp dvfqasehik seqgneyslp altpgldevk sslsastnpe lgsnvsgtqt
      301 ypvvtgrdma sttlpgypph vpptgqgsyp tstlagmvpg sefsgnpysh pqytayneaw
      361 rfsnpallmp ppgapplpll plpmtatsyr gdhiklqads fglhivpv
//
LOCUS       NP_077043                354 aa            linear   ROD 09-APR-2025
DEFINITION  decorin precursor [Rattus norvegicus].
ACCESSION   NP_077043 XP_343202
VERSION     NP_077043.1
DBSOURCE    REFSEQ: accession NM_024129.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Hassan,G.M. and Ebrahim,R.H.
  TITLE     The myokine decorin improves the cardiac function in a rat model of
            isoprenaline-induced myocardial infarction
  JOURNAL   Can J Physiol Pharmacol 101 (6), 286-293 (2023)
   PUBMED   36917819
  REMARK    GeneRIF: The myokine decorin improves the cardiac function in a rat
            model of isoprenaline-induced myocardial infarction.
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Gaspar,R., Gomori,K., Kiss,B., Szantai,A., Paloczi,J., Varga,Z.V.,
            Pipis,J., Varadi,B., Agg,B., Csont,T., Ferdinandy,P., Bartekova,M.
            and Gorbe,A.
  TITLE     Decorin Protects Cardiac Myocytes against Simulated
            Ischemia/Reperfusion Injury
  JOURNAL   Molecules 25 (15), 3426 (2020)
   PUBMED   32731559
  REMARK    GeneRIF: Decorin Protects Cardiac Myocytes against Simulated
            Ischemia/Reperfusion Injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Lai,J., Chen,F., Chen,J., Ruan,G., He,M., Chen,C., Tang,J. and
            Wang,D.W.
  TITLE     Overexpression of decorin promoted angiogenesis in diabetic
            cardiomyopathy via IGF1R-AKT-VEGF signaling
  JOURNAL   Sci Rep 7, 44473 (2017)
   PUBMED   28290552
  REMARK    GeneRIF: overexpression of decorin ameliorated diabetic
            cardiomyopathy and promoted angiogenesis through the IGF1R-AKT-VEGF
            signaling pathway in vivo and in vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   6  (residues 1 to 354)
  AUTHORS   De Cosmo,S., Tassi,V., Thomas,S., Piras,G.P., Trevisan,R., Cavallo
            Perin,P., Bacci,S., Zucaro,L., Cisternino,C., Trischitta,V. and
            Viberti,G.C.
  TITLE     The Decorin gene 179 allelic variant is associated with a slower
            progression of renal disease in patients with type 1 diabetes
  JOURNAL   Nephron 92 (1), 72-76 (2002)
   PUBMED   12187087
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Schaefer,L., Raslik,I., Grone,H.J., Schonherr,E., Macakova,K.,
            Ugorcakova,J., Budny,S., Schaefer,R.M. and Kresse,H.
  TITLE     Small proteoglycans in human diabetic nephropathy: discrepancy
            between glomerular expression and protein accumulation of decorin,
            biglycan, lumican, and fibromodulin
  JOURNAL   FASEB J 15 (3), 559-561 (2001)
   PUBMED   11259366
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Asundi,V.K. and Dreher,K.L.
  TITLE     Molecular characterization of vascular smooth muscle decorin:
            deduced core protein structure and regulation of gene expression
  JOURNAL   Eur J Cell Biol 59 (2), 314-321 (1992)
   PUBMED   1493796
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Abramson,S.R. and Woessner,J.F. Jr.
  TITLE     cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin)
  JOURNAL   Biochim Biophys Acta 1132 (2), 225-227 (1992)
   PUBMED   1390895
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Kokenyesi,R. and Woessner,J.F. Jr.
  TITLE     Purification and characterization of a small dermatan sulphate
            proteoglycan implicated in the dilatation of the rat uterine cervix
  JOURNAL   Biochem J 260 (2), 413-419 (1989)
   PUBMED   2764879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Oct 11, 2004 this sequence version replaced XP_343202.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083750.1, FQ228702.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..354
                     /product="decorin precursor"
                     /note="dermatan sulfate proteoglycan-II (decorin); DSPG;
                     PG40; PG-S2; bone proteoglycan II"
                     /calculated_mol_wt=38032
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1791
     mat_peptide     31..354
                     /product="Decorin. /id=PRO_0000032720"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
                     /calculated_mol_wt=36364
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000269|PubMed:2764879; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          48..80
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          57..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          68..88
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          78..>302
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          89..112
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          102..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          113..136
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          126..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          137..157
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          147..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..181
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          171..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          197..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          218..241
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          229..252
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          242..265
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          253..276
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          277..299
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          289..308
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          300..329
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          312..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          330..354
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     CDS             1..354
                     /gene="Dcn"
                     /coded_by="NM_024129.2:81..1145"
                     /db_xref="GeneID:29139"
                     /db_xref="RGD:61895"
ORIGIN      
        1 mkatlvlfll aqvswagpfe qrglfdfmle deasgiipyd pdnplismcp yrcqchlrvv
       61 qcsdlgldkv pwefppdttl ldlqnnkite ikegafknlk dlhtlilvnn kiskispeaf
      121 kplvklerly lsknhlkelp eklpktlqel rlhdneitkl kksvfnglnr mivielggnp
      181 lknsgienga lqgmkglgyi risdtnitai pqglptsise lhldgnkiak vdaaslkgms
      241 nlsklglsfn sitvvengsl anvphlrelh ldnnkllrvp aglaqhkyvq vvylhnnnis
      301 evgqhdfclp syqtrktsyt avslysnpvr ywqihphtfr cvfgrstiql gnyk
//
LOCUS       NP_001424653             343 aa            linear   ROD 09-APR-2025
DEFINITION  RNA-binding protein 43 [Rattus norvegicus].
ACCESSION   NP_001424653 XP_063139612
VERSION     NP_001424653.1
DBSOURCE    REFSEQ: accession NM_001437724.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063139612.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360172.1657478.1,
                                    SRR26360194.2284316.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN12840107,
                                    SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..343
                     /product="RNA-binding protein 43"
                     /note="rCG37778-like"
                     /calculated_mol_wt=38745
     Region          15..82
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          170..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7D9.1)"
     CDS             1..343
                     /gene="Rbm43"
                     /gene_synonym="RGD1306676"
                     /coded_by="NM_001437724.1:162..1193"
                     /db_xref="GeneID:311020"
                     /db_xref="RGD:1306676"
ORIGIN      
        1 masaltvkdp tvsertvvvs glpvglskdq lvkryfrdeg ghvekviypp rskgvayiif
       61 kekkvaqtii rqkkhplgse plltvshfse kvfnyvmail dlsvfrpqiv leslvvdlkk
      121 kiptlnfspl grsgkisvqg sflailklkq aliskaisal ennrkyager rnwtgqnprr
      181 vlqknensap tlgtsvpepa gspetlvldt dvflylkhkc qfyeptlsky hvlcqervdg
      241 dittlclqda rdgsypgsvr hvkelieewa qefylelrke llvlegrres ekrnmrqafe
      301 qlccryprvl mnvhrthidl igppsdtslf ktqlmksagq kvt
//
LOCUS       NP_001424614             748 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424614 XP_038943819
VERSION     NP_001424614.1
DBSOURCE    REFSEQ: accession NM_001437685.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 748)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 748)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 748)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 748)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 748)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943819.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.67906.1,
                                           SRR26360176.1828767.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..748
                     /product="dynamin-1-like protein isoform 5"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=83089
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          23..308
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,152,222,224..225,251..255,258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,156,169,194,196,198..201,203..204,225,
                     227..230,254..256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          58..60
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          152..155
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            152..155
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(154..155,185..186)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          221..224
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            221..224
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          231..516
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          251..254
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            251..253
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          350..495
                     /region_name="Middle domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          454..697
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          508..575
                     /region_name="B domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          529..603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            597
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            598
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            609
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K1M6; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:17301055,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK1 and PKA.
                     /evidence=ECO:0000269|PubMed:28463107; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          652..742
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          666..680
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     CDS             1..748
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437685.1:135..2381"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswr veaeewgkfl htknklytdf deirqeiene
      121 terisgnnkg vspepihlkv fspnvvnltl vdlpgmtkvp vgdqpkdiel qirelilrfi
      181 snpnsiilav taantdmats ealkisrevd pdgrrtlavi tkldlmdagt damdvlmgrv
      241 ipvklgiigv vnrsqldinn kksvtdsird eyaflqkkyp slanrngtky lartlnrllm
      301 hhirdclpel ktrinvlaaq yqsllnsyge pvddksatll qlitkfatey cntiegtaky
      361 ietselcgga ricyifhetf grtlesvdpl gglntidilt airnatgprp alfvpevsfe
      421 llvkrqikrl eepslrcvel vheemqriiq hcsnystqel lrfpklhdai vevvtcllrk
      481 rlpvtnemvh nlvaielayi ntkhpdfada cglmnnniee qrrnrlarel psavsrdkss
      541 kvpsalapas qepspaasae adgkliqdnr retknvasag ggigdggrig dggqepttgn
      601 wrgmlktska eellaeeksk pipimpaspq kghavnlldv pvpvarklsa reqrdcevie
      661 rliksyfliv rkniqdsvpk avmhflvnhv kdtlqselvg qlyksslldd lltesedmaq
      721 rrkeaadmlk alqgasqiia eirethlw
//
LOCUS       NP_001424636             486 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424636 XP_038943857
VERSION     NP_001424636.1
DBSOURCE    REFSEQ: accession NM_001437707.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943857.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.46680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..486
                     /product="transcriptional regulator ERG isoform 5"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=54650
     Region          122..205
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          317..400
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..486
                     /gene="Erg"
                     /coded_by="NM_001437707.1:260..1720"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 miqtvpdpea qikealsvvs edqslfecay gtphlaktem tassssdygq tskmsprvpq
       61 qdwlsqppar vtikmecnps qvngsrnspd ecsvtkggkm vgspdtvgms ygsymeekhm
      121 pppnmttner rvivpadptl wstdhvrqwl ewavkeygll dvdvllfqni dgkelckmtk
      181 ddfqrltpsy nadillshlh ylretplphl tsddvdkalq nsprlmharn tggaafifpn
      241 tsvypeatqr ittrpdlpye pprrstwtgh shptpqskaa qpspstvpkt edqrpqldpy
      301 qilgptssrl anpgsgqiql wqfllellsd ssnsncitwe gtngefkmtd pdevarrwge
      361 rkskpnmnyd klsralryyy dknimtkvhg kryaykfdfh giaqalqphp pesslykyps
      421 dlpymgsyht hpqkmnfvap hppalpvtss sffatpnpyw nsptggiypn trlpashmps
      481 hlgtyy
//
LOCUS       NP_001424622             718 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 13 [Rattus norvegicus].
ACCESSION   NP_001424622 XP_038943827
VERSION     NP_001424622.1
DBSOURCE    REFSEQ: accession NM_001437693.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943827.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.30247.1,
                                           SRR26643289.31603.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..718
                     /product="dynamin-1-like protein isoform 13"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=79973
     Region          23..315
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,159,229,231..232,258..262,265)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,163,176,201,203,205..208,210..211,232,
                     234..237,261..263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            159..162
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(161..162,192..193)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            228..231
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          238..523
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            258..260
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          622..712
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..718
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437693.1:135..2291"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eendpatwkn srhlskgvea eewgkflhtk nklytdfdei
      121 rqeieneter isgnnkgvsp epihlkvfsp nvvnltlvdl pgmtkvpvgd qpkdielqir
      181 elilrfisnp nsiilavtaa ntdmatseal kisrevdpdg rrtlavitkl dlmdagtdam
      241 dvlmgrvipv klgiigvvnr sqldinnkks vtdsirdeya flqkkypsla nrngtkylar
      301 tlnrllmhhi rdclpelktr invlaaqyqs llnsygepvd dksatllqli tkfateycnt
      361 iegtakyiet selcggaric yifhetfgrt lesvdplggl ntidiltair natgprpalf
      421 vpevsfellv krqikrleep slrcvelvhe emqriiqhcs nystqellrf pklhdaivev
      481 vtcllrkrlp vtnemvhnlv aielayintk hpdfadacgl mnnnieeqrr nrlarelpsa
      541 vsrdkvasag ggigdggrig dggqepttgn wrgmlktska eellaeeksk pipimpaspq
      601 kghavnlldv pvpvarklsa reqrdcevie rliksyfliv rkniqdsvpk avmhflvnhv
      661 kdtlqselvg qlyksslldd lltesedmaq rrkeaadmlk alqgasqiia eirethlw
//
LOCUS       NP_001424612             755 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424612 XP_038943817
VERSION     NP_001424612.1
DBSOURCE    REFSEQ: accession NM_001437683.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 755)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 755)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 755)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 755)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 755)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 755)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943817.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF019043.2, SRR26643298.67900.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..755
                     /product="dynamin-1-like protein isoform 3"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=83778
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          23..315
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,159,229,231..232,258..262,265)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,163,176,201,203,205..208,210..211,232,
                     234..237,261..263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          58..60
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          159..162
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            159..162
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(161..162,192..193)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          228..231
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            228..231
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          238..523
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          258..261
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            258..260
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          357..502
                     /region_name="Middle domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          461..704
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          515..582
                     /region_name="B domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          536..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            604
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            605
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            616
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K1M6; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:17301055,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK1 and PKA.
                     /evidence=ECO:0000269|PubMed:28463107; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          659..749
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          673..687
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     CDS             1..755
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437683.1:135..2402"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eendpatwkn srhlskgvea eewgkflhtk nklytdfdei
      121 rqeieneter isgnnkgvsp epihlkvfsp nvvnltlvdl pgmtkvpvgd qpkdielqir
      181 elilrfisnp nsiilavtaa ntdmatseal kisrevdpdg rrtlavitkl dlmdagtdam
      241 dvlmgrvipv klgiigvvnr sqldinnkks vtdsirdeya flqkkypsla nrngtkylar
      301 tlnrllmhhi rdclpelktr invlaaqyqs llnsygepvd dksatllqli tkfateycnt
      361 iegtakyiet selcggaric yifhetfgrt lesvdplggl ntidiltair natgprpalf
      421 vpevsfellv krqikrleep slrcvelvhe emqriiqhcs nystqellrf pklhdaivev
      481 vtcllrkrlp vtnemvhnlv aielayintk hpdfadacgl mnnnieeqrr nrlarelpsa
      541 vsrdksskvp salapasqep spaasaeadg kliqdnrret knvasagggi gdggrigdgg
      601 qepttgnwrg mlktskaeel laeekskpip impaspqkgh avnlldvpvp varklsareq
      661 rdcevierli ksyflivrkn iqdsvpkavm hflvnhvkdt lqselvgqly kssllddllt
      721 esedmaqrrk eaadmlkalq gasqiiaeir ethlw
//
LOCUS       NP_001424679            1181 aa            linear   ROD 09-APR-2025
DEFINITION  sodium/hydrogen exchanger 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424679 XP_017453416
VERSION     NP_001424679.1
DBSOURCE    REFSEQ: accession NM_001437750.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Wang,D., King,S.M., Quill,T.A., Doolittle,L.K. and Garbers,D.L.
  TITLE     A new sperm-specific Na+/H+ exchanger required for sperm motility
            and fertility
  JOURNAL   Nat Cell Biol 5 (12), 1117-1122 (2003)
   PUBMED   14634667
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_017453416.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.69078.1,
                                           SRR26360181.1921354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1181
                     /product="sodium/hydrogen exchanger 10 isoform 1"
                     /note="sperm-specific sodium proton exchanger;
                     sodium/hydrogen exchanger 10; solute carrier family 9,
                     member 10; solute carrier family 9, subfamily C
                     (Na+-transporting carboxylic acid decarboxylase), member
                     1"
                     /calculated_mol_wt=136095
     Region          37..556
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          893..1020
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(974..975,984..986)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(1006..1008,1013..1015)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..1181
                     /gene="Slc9c1"
                     /gene_synonym="Gm610; Slc9a10"
                     /coded_by="NM_001437750.1:648..4193"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:288117"
                     /db_xref="RGD:1309075"
ORIGIN      
        1 meevfenltt thnvklsnaw ldllksvfls tpqdlpeiil ilslictiga flnmhlkdfp
       61 iplpvilfli gccfeilsfa stqiqlyada iqwmdpdmff giftpviifn vafdmdiyml
      121 qklfwqilli tipgfminyt lilwylqsvn klslktipwl lfsavlissd pmltsasird
      181 lglsrsltnl ingeslltsv isliiysavv qisfkskhmn htlahkvmst awsylvesfi
      241 tgilitkaiq lwmatifgdd vnhitlifsv lylifyvcel igmsgiftla tiglflnsts
      301 fkpgveafll efwnclsfig flmvftfigl lipahtylyi sfsdvyysln iyftlivlrl
      361 lvfllmspil srlghgfswr wafimvwsem kgtpninmal llaysdvslg serersqilf
      421 hgvsvcvitl ivnrfilpma viklglrdvt stkyksvyyt fqhfqeltks tamalkfdkd
      481 lanadwnmvd kaiilqnpya lnqeettehq kvkcpdcnke idetlnieam elanrrllsa
      541 qiasyqrqyr neilsqsamq vlvgaagsfg ekkgeymspe niknyseskk llsflrklll
      601 nwvyntkkdk gvpsrymflh achsivftne feytgyiavl mntypmiicw isrlkdiyqy
      661 eikcanyyfl tfyileallk vaamrkeffs htwllfelgi tlvgildiil ietdsisykf
      721 dltetvvfmn vvrllrilri lklitpkllq vidkrmsqqi sfryailkgy vqgemdvlni
      781 idqiasskqa kqillkrvir nmdhamkelg yleydhpeia vtmktkeevn vmlnmareiv
      841 kafrskgiih kvegaeinkl imakkkqvle lqsviqplnv eeapyyipwl sedpeaisfi
      901 qekakvvtfd cgnnifeegd epegiyviis gmvklkrskp hlemdrvsse sevaqtrsyt
      961 lphteyllsg eiigelnclt kermqysatc ktvvetyfip ishlyegfek kypnmkykmw
     1021 qkiglaitaq kirenlsfed wnykmqlklc nvfvrdipkt tktdiydetv thvvlihgsa
     1081 edcqlrkiyk apflipvtch qiqgleeftk vmiiqtsvav rkfrwnvkky npprrismkp
     1141 dstesletln esseddedkk eneeneeyle diidissvsk k
//
LOCUS       NP_001424688            1057 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424688 XP_063126572
VERSION     NP_001424688.1
DBSOURCE    REFSEQ: accession NM_001437759.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1057)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1057)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1057)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1057)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1057)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1057)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1057)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126572.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1976929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1057
                     /product="activated CDC42 kinase 1 isoform 6"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=117340
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          162..419
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302,321..325,334,368)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(284,288,321..325,334,368)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(301..311,313..327)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          427..476
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(429,431,436,454,456,471,473..474)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          481..546
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <500..963
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          799..857
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          978..1021
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1008..1047
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1057
                     /gene="Tnk2"
                     /coded_by="NM_001437759.1:325..3498"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk vfsgkrqeae
      121 fpshhsqstf rkpsptpggl agegtlqslt cligekdlrl leklgdgsfg vvrrgewdap
      181 agktvsvavk clkpdvlsqp eamddfirev namhsldhrn lirlygvvlt ppmkmvtela
      241 plgslldrlr khqghfllgt lsryavqvae gmgyleskrf ihrdlaarnl llatrdlvki
      301 gdfglmralp qnddhyvmqe hrkvpfawca peslktrtfs hasdtwmfgv tlwemftygq
      361 epwiglngsq ilhkidkege rlprpedcpq diynvmvqcw ahkpedrptf valrdfllea
      421 qptdmralqd feepdklhiq mndvitvieg raenywwrgq ntrtlcvgpf prnvvtsvag
      481 lsaqdisqpl qnsfihtghg dsdprhcwgf pdridelylg npmdppdlls velstsrptq
      541 hlgrmkrepp prppqpaift hkptydpvse dpdplssdfk rlglrkpalp rglwlakpsa
      601 rvpgtkagrs sggevtlidf geepvaptpr pcapslaqla mdacslldkt ppqsptralp
      661 rplhptpvvd wdarplpppp ayddvaqded dfeaqlppal ednlflppqg ggqppssaqt
      721 aeifqalqqe cmrqlqvptg qltpsptpgg ddkpqvpprv pipprptrpr vglspaplge
      781 eeasrwpgps spprvpprep lspqgsrtps plvppgsspl phrlssspgk tmpttqsfas
      841 dpkyatpqvi qapgpragpc ilpivrdgrk vssthyyllp erppyleryq rflreaqspe
      901 epaalpvppl lpppstpapa aptatvrpmp qaapdpkanf stnnsnpgaq ppslrasarl
      961 pqrgcpgdgq eaarpadkvq mlqamvhgvt teecqaalrs hswsiqraaq ylkveqlfgl
     1021 glrprvechk vlemfdwnle qagchllgsc gpahhkr
//
LOCUS       NP_001008337            1040 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001008337 XP_221379
VERSION     NP_001008337.2
DBSOURCE    REFSEQ: accession NM_001008336.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1040)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1040)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1040)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1040)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1040)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1040)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1040)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced NP_001008337.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085825.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1040
                     /product="activated CDC42 kinase 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=114996
     Region          1..110
                     /region_name="SAM-like domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          86..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O54967; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          505..527
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          <580..946
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          623..652
                     /region_name="Required for interaction with SRC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          632..635
                     /region_name="Required for interaction with NEDD4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          722..824
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          733..876
                     /region_name="EBD domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          782..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            839
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54967; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          881..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07912; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X5.1)"
     Region          961..1004
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          991..1030
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1040
                     /gene="Tnk2"
                     /coded_by="NM_001008336.2:298..3420"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nitrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkamc krkswmskvf sgkrqeaefp shhsqstfrk psptpgglag egtlqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapag ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrptqhl grmkkptydp vsedpdplss dfkrlglrkp
      541 alprglwlak psarvpgtka grssggevtl idfgeepvap tprpcapsla qlamdacsll
      601 dktppqsptr alprplhptp vvdwdarplp pppayddvaq deddfevcsi nstlvsaglp
      661 tgpsqgetny afvpeqaqlp palednlflp pqgggqppss aqtaeifqal qqecmrqlqv
      721 ptgqltpspt pggddkpqvp prvpipprpt rprvglspap lgeeeasrwp gpsspprvpp
      781 replspqgsr tpsplvppgs splphrlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd grkvssthyy llperppyle ryqrflreaq speepaalpv ppllpppstp
      901 apaaptatvr pmpqaapdpk anfstnnsnp gaqppslras arlpqrgcpg dgqeaarpad
      961 kvqmlqamvh gvtteecqaa lrshswsiqr aaqylkveql fglglrprve chkvlemfdw
     1021 nleqagchll gscgpahhkr
//
LOCUS       NP_001424618             731 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424618 XP_038943823
VERSION     NP_001424618.1
DBSOURCE    REFSEQ: accession NM_001437689.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943823.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.30240.1,
                                           SRR26643292.46638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..731
                     /product="dynamin-1-like protein isoform 9"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=80887
     Region          23..302
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,146,216,218..219,245..249,252)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,150,163,188,190,192..195,197..198,219,
                     221..224,248..250)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            146..149
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(148..149,179..180)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            215..218
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          225..510
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            245..247
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          635..725
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..731
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437689.1:135..2330"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengveaeew gkflhtknkl ytdfdeirqe ieneterisg
      121 nnkgvspepi hlkvfspnvv nltlvdlpgm tkvpvgdqpk dielqireli lrfisnpnsi
      181 ilavtaantd matsealkis revdpdgrrt lavitkldlm dagtdamdvl mgrvipvklg
      241 iigvvnrsql dinnkksvtd sirdeyaflq kkypslanrn gtkylartln rllmhhirdc
      301 lpelktrinv laaqyqslln sygepvddks atllqlitkf ateycntieg takyietsel
      361 cggaricyif hetfgrtles vdplgglnti diltairnat gprpalfvpe vsfellvkrq
      421 ikrleepslr cvelvheemq riiqhcsnys tqellrfpkl hdaivevvtc llrkrlpvtn
      481 emvhnlvaie layintkhpd fadacglmnn nieeqrrnrl arelpsavsr dksskvpsal
      541 apasqepspa asaeadgkva sagggigdgg rigdggqept tgnwrgmlkt skaeellaee
      601 kskpipimpa spqkghavnl ldvpvpvark lsareqrdce vierliksyf livrkniqds
      661 vpkavmhflv nhvkdtlqse lvgqlykssl lddlltesed maqrrkeaad mlkalqgasq
      721 iiaeirethl w
//
LOCUS       NP_001103058             232 aa            linear   ROD 09-APR-2025
DEFINITION  BPI fold-containing family A member 3 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001103058 XP_001074347
VERSION     NP_001103058.1
DBSOURCE    REFSEQ: accession NM_001109588.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001074347.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1054069.1,
                                           SRR26360181.2751518.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..232
                     /product="BPI fold-containing family A member 3 isoform 1
                     precursor"
                     /calculated_mol_wt=23485
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2277
     Region          47..219
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     CDS             1..232
                     /gene="Bpifa3"
                     /gene_synonym="Splunc3"
                     /coded_by="NM_001109588.2:202..900"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:690402"
                     /db_xref="RGD:1596102"
ORIGIN      
        1 mhllwrflvl llgllalpsa lpkqpwpglt kahkdgrstl ariiaqgllk hnaegriqsm
       61 rlldrlnvsg tvapgmvswl isgmnfqqqq eisinitnvq ldcggiqmaf pkewfsanit
      121 lefdiefklp fnsnilktha qmglaaeswl ekdefgrrkl vtgrcqmeps sdsasmttea
      181 aspkmknflh nlreslgkvi pnlvesqvcp ligeilrqld vkllkglvgg cs
//
LOCUS       NP_001424632             894 aa            linear   ROD 09-APR-2025
DEFINITION  phosphatidate phosphatase LPIN2 [Rattus norvegicus].
ACCESSION   NP_001424632 XP_038939723
VERSION     NP_001424632.1
DBSOURCE    REFSEQ: accession NM_001437703.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Kok,B.P.C., Dyck,J.R.B., Harris,T.E. and Brindley,D.N.
  TITLE     Differential regulation of the expressions of the PGC-1alpha splice
            variants, lipins, and PPARalpha in heart compared to liver
  JOURNAL   J Lipid Res 54 (6), 1662-1677 (2013)
   PUBMED   23505321
  REMARK    GeneRIF: novel differences in the regulation of lipins 1,2,3,
            PPARalpha, and PGC-1alpha splice variants during fasting in heart
            versus liver, even though the ultimate outcome in both tissues is
            to increase FA turnover and oxidation.
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Donkor,J., Zhang,P., Wong,S., O'Loughlin,L., Dewald,J., Kok,B.P.,
            Brindley,D.N. and Reue,K.
  TITLE     A conserved serine residue is required for the phosphatidate
            phosphatase activity but not the transcriptional coactivator
            functions of lipin-1 and lipin-2
  JOURNAL   J Biol Chem 284 (43), 29968-29978 (2009)
   PUBMED   19717560
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Grimsey,N., Han,G.S., O'Hara,L., Rochford,J.J., Carman,G.M. and
            Siniossoglou,S.
  TITLE     Temporal and spatial regulation of the phosphatidate phosphatases
            lipin 1 and 2
  JOURNAL   J Biol Chem 283 (43), 29166-29174 (2008)
   PUBMED   18694939
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Donkor,J., Sariahmetoglu,M., Dewald,J., Brindley,D.N. and Reue,K.
  TITLE     Three mammalian lipins act as phosphatidate phosphatases with
            distinct tissue expression patterns
  JOURNAL   J Biol Chem 282 (6), 3450-3457 (2007)
   PUBMED   17158099
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038939723.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.12723.1,
                                           SRR26643288.39184.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..894
                     /product="phosphatidate phosphatase LPIN2"
                     /EC_number="3.1.3.4"
                     /calculated_mol_wt=99578
     Region          1..107
                     /region_name="Lipin_N"
                     /note="lipin, N-terminal conserved region; pfam04571"
                     /db_xref="CDD:461356"
     Region          <326..483
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          467..559
                     /region_name="Lipin_mid"
                     /note="Lipin/Ned1/Smp2 multi-domain protein middle domain;
                     pfam16876"
                     /db_xref="CDD:465292"
     Region          635..860
                     /region_name="LNS2"
                     /note="LNS2 (Lipin/Ned1/Smp2); pfam08235"
                     /db_xref="CDD:462403"
     Region          873..>891
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     CDS             1..894
                     /gene="Lpin2"
                     /coded_by="NM_001437703.1:277..2961"
                     /db_xref="GeneID:316737"
                     /db_xref="RGD:1304588"
ORIGIN      
        1 mnyvgqlagq vlvtvkelyk ginqatlsgc idvvvvrqqd gsyqcspfhv rfgklgvlrs
       61 kekvidiein gsavdlhmkl gdngeaffve eteeeyeklp aylatspipt edqffkhidp
      121 plvkssgner ppqssdvsht leseavftps svkkkkrrrk kckqdnrkee qaaspvaedv
      181 gdvavssdde kraqaargss naslkeedyk epppfhsgdn yplsdgdwsp letsypqtvc
      241 pksdselevk psesllrses hmewtwggfp estkvskrer ydyhprtati tpsenthfrv
      301 ipsedslire vekdatvedt tctivkpkpr alckqlsdaa stelpesple apqisstlda
      361 dpvpspsaea psepkpaakv dsptkrkgvh krsqhqgpdd iylddlkale pevaalyfpk
      421 sdtdpgsrqw pesdtfsgsq spqsvgsaaa dsgteclsds amdlpdvtls lcgglsenge
      481 iskekfmehi ityhefaenp glidnpnlvi riynryynwa laapmilslq vfqkslpkat
      541 veswvkdkmp kksgrwwfwr kkesmtkqlp etkegksevp pandlpsgte epvsarpaen
      601 dtssdegsqe leetikvdpi smetlshcgt asykkslrls sdqiaklklh dgpndvvfsi
      661 ttqyqgtcrc agtiylwnwn dkviisdidg titksdalgq ilpqlgkdwt hqgiarlyhs
      721 inengykfly csaraigmad mtrgylhwvn dkgtilprgp lmlspsslfs afhreviekk
      781 pekfkiecln diknlfapsr qpfyaafgnr pndvyaytqv gvpdcriftv npkgeliqer
      841 tkgnkssyhr lselvehvfp llnkeqnsaf pcpefssfcy wrdpipdvdl ddla
//
LOCUS       NP_001424634             456 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424634 XP_063126324
VERSION     NP_001424634.1
DBSOURCE    REFSEQ: accession NM_001437705.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126324.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.66346.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..456
                     /product="transcriptional regulator ERG isoform 3"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=51173
     Region          115..198
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          287..370
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..456
                     /gene="Erg"
                     /coded_by="NM_001437705.1:155..1525"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 mastikeals vvsedqslfe caygtphlak temtassssd ygqtskmspr vpqqdwlsqp
       61 parvtikmec npsqvngsrn spdecsvtkg gkmvgspdtv gmsygsymee khmpppnmtt
      121 nerrvivpad ptlwstdhvr qwlewavkey glldvdvllf qnidgkelck mtkddfqrlt
      181 psynadills hlhylretpl phltsddvdk alqnsprlmh arntggaafi fpntsvypea
      241 tqrittrpaa qpspstvpkt edqrpqldpy qilgptssrl anpgsgqiql wqfllellsd
      301 ssnsncitwe gtngefkmtd pdevarrwge rkskpnmnyd klsralryyy dknimtkvhg
      361 kryaykfdfh giaqalqphp pesslykyps dlpymgsyht hpqkmnfvap hppalpvtss
      421 sffatpnpyw nsptggiypn trlpashmps hlgtyy
//
LOCUS       NP_001424689            1055 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424689 XP_063126573
VERSION     NP_001424689.1
DBSOURCE    REFSEQ: accession NM_001437760.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1055)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1055)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1055)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1055)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1055)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1055)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1055)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126573.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.45968.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1055
                     /product="activated CDC42 kinase 1 isoform 7"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=116714
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          145..402
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285,304..308,317,351)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(267,271,304..308,317,351)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(284..294,296..310)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          410..459
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(412,414,419,437,439,454,456..457)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          464..529
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <595..961
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          797..855
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          976..1019
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1006..1045
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1055
                     /gene="Tnk2"
                     /coded_by="NM_001437760.1:325..3492"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk stfrkpsptp
      121 gglagegtlq sltcligekd lrlleklgdg sfgvvrrgew dapagktvsv avkclkpdvl
      181 sqpeamddfi revnamhsld hrnlirlygv vltppmkmvt elaplgslld rlrkhqghfl
      241 lgtlsryavq vaegmgyles krfihrdlaa rnlllatrdl vkigdfglmr alpqnddhyv
      301 mqehrkvpfa wcapeslktr tfshasdtwm fgvtlwemft ygqepwigln gsqilhkidk
      361 egerlprped cpqdiynvmv qcwahkpedr ptfvalrdfl leaqptdmra lqdfeepdkl
      421 hiqmndvitv iegraenyww rgqntrtlcv gpfprnvvts vaglsaqdis qplqnsfiht
      481 ghgdsdprhc wgfpdridel ylgnpmdppd llsvelstsr ptqhlgrmkk ptydpvsedp
      541 dplssdfkrl glrkpalprg lwlakpsarv pgtkagrssg gevtlidfge epvaptprpc
      601 apslaqlamd acslldktpp qsptralprp lhptpvvdwd arplppppay ddvaqdeddf
      661 evcsinstlv saglptgpsq getnyafvpe qaqlppaled nlflppqggg qppssaqtae
      721 ifqalqqecm rqlqvptgql tpsptpggdd kpqvpprvpi pprptrprvg lspaplgeee
      781 asrwpgpssp prvpprepls pqgsrtpspl vppgssplph rlssspgktm pttqsfasdp
      841 kyatpqviqa pgpragpcil pivrdgrkvs sthyyllper ppyleryqrf lreaqspeep
      901 aalpvppllp ppstpapaap tatvrpmpqa apdpkanfst nnsnpgaqpp slrasarlpq
      961 rgcpgdgqea arpadkvqml qamvhgvtte ecqaalrshs wsiqraaqyl kveqlfglgl
     1021 rprvechkvl emfdwnleqa gchllgscgp ahhkr
//
LOCUS       NP_620240               3187 aa            linear   ROD 09-APR-2025
DEFINITION  golgin subfamily B member 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_620240
VERSION     NP_620240.2
DBSOURCE    REFSEQ: accession NM_138885.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3187)
  AUTHORS   Casey,C.A., Thomes,P., Manca,S. and Petrosyan,A.
  TITLE     Giantin Is Required for Post-Alcohol Recovery of Golgi in Liver
            Cells
  JOURNAL   Biomolecules 8 (4), 150 (2018)
   PUBMED   30453527
  REMARK    GeneRIF: Ethanol-induced Golgi disassembly was associated with
            de-dimerization of the largest Golgi matrix protein giantin, along
            with impaired transport of selected hepatic proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3187)
  AUTHORS   Katayama,K., Kuriki,M., Kamiya,T., Tochigi,Y. and Suzuki,H.
  TITLE     Giantin is required for coordinated production of aggrecan, link
            protein and type XI collagen during chondrogenesis
  JOURNAL   Biochem Biophys Res Commun 499 (3), 459-465 (2018)
   PUBMED   29577904
  REMARK    GeneRIF: giantin plays a pivotal role in coordinated production of
            aggrecan, link protein and type XI collagen in chondrocytes.
REFERENCE   3  (residues 1 to 3187)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   4  (residues 1 to 3187)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 3187)
  AUTHORS   Fusco,C., Micale,L., Egorov,M., Monti,M., D'Addetta,E.V.,
            Augello,B., Cozzolino,F., Calcagni,A., Fontana,A., Polishchuk,R.S.,
            Didelot,G., Reymond,A., Pucci,P. and Merla,G.
  TITLE     The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and
            promotes the sequestration and clearance of ubiquitinated proteins
            into the aggresome
  JOURNAL   PLoS One 7 (7), e40440 (2012)
   PUBMED   22792322
REFERENCE   6  (residues 1 to 3187)
  AUTHORS   Katayama,K., Sasaki,T., Goto,S., Ogasawara,K., Maru,H., Suzuki,K.
            and Suzuki,H.
  TITLE     Insertional mutation in the Golgb1 gene is associated with
            osteochondrodysplasia and systemic edema in the OCD rat
  JOURNAL   Bone 49 (5), 1027-1036 (2011)
   PUBMED   21851869
  REMARK    GeneRIF: concluded that mutation of the Golgb1 gene is responsible
            for the phenotypic characteristics including osteochondrodysplasia
            of ocd/ocd, and that giantin plays a pivotal role in multiple
            aspects of chondrogenesis
REFERENCE   7  (residues 1 to 3187)
  AUTHORS   Zhang,B., Zheng,C., Zhu,M., Tao,J., Vasievich,M.P., Baines,A.,
            Kim,J., Schekman,R., Kaufman,R.J. and Ginsburg,D.
  TITLE     Mice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver
            accumulation of alpha1-antitrypsin
  JOURNAL   Blood 118 (12), 3384-3391 (2011)
   PUBMED   21795745
REFERENCE   8  (residues 1 to 3187)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 3187)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
REFERENCE   10 (residues 1 to 3187)
  AUTHORS   Diella,F., Levi,G. and Callahan,R.
  TITLE     Characterization of the INT6 mammary tumor gene product
  JOURNAL   DNA Cell Biol 16 (7), 839-847 (1997)
   PUBMED   9260927
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Nov 27, 2020 this sequence version replaced NP_620240.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D25543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..3187
                     /product="golgin subfamily B member 1 isoform 1"
                     /note="Golgin subfamily B member 1; golgi autoantigen,
                     golgin subfamily b, macrogolgin 1; golgi-associated
                     protein GCP360; golgin B1, golgi integral membrane
                     protein"
                     /calculated_mol_wt=364123
     Region          63..>181
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          137..>906
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          679..1582
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1520..1992
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1835..2591
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          2278..>3027
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..3187
                     /gene="Golgb1"
                     /coded_by="NM_138885.3:315..9878"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:192243"
                     /db_xref="RGD:708429"
ORIGIN      
        1 mlsrlsglan nvlhelsgdy tgwttmtsse aelpqgsame lnnstqkdvl drladaeklv
       61 lelkdiiskq daqlqqkdea lqeekkgaes kikkiklhak akitslnkqi eelktqggaa
      121 sppevqaeel skhdksstee emevekikhe lqekeklisn lqaqldqaqs eqasqldkss
      181 aemedfvlmr qklqekeeli galqtqlsqt qaeqaaqklr vmqrkleehe eallgraqvv
      241 dllqkeltsa eqrnqdlsqq lqlleaehst lrntmeaerq eskilmekve lemaerkeel
      301 yqlqgqlera gqaqaelemq ygtlqqrhet emeektacis llqkneqelq sacdalkeen
      361 skllqeqqeq aaksaqalqq ledelqqksk eisqfvnkpn lekhetssqt slpdvynegv
      421 qavmeesvas lqkrvlelen ekgalllssl eleelraene klcsritlle aqnrageadg
      481 mvcevstagi allnrsdsst eesgqdvlen tfsqkhkels vllvemkeaq eeiaflksql
      541 qgkrpegdye vldrkevqmm eseglpsvta rdvlcaprdk nsvpavegeq agmrdqhgtl
      601 eagplndtgm elnspqpdgv dkslsaphvc lchqgelerl ktqvlelets lhtakethek
      661 nlsekakeis sltqltkefk esaeearstl tavceerdql lyrvkeldvl gelraqvrel
      721 etslaeaekq rgldyesqra qhnllteqih slsieakskd vkietlqrel dgvqlqfseq
      781 gtqirslqsq lqtkesevle gaermkdisk emeelsqals qkeleiaqmd qlllekkkdv
      841 etlqqtiqek dqqvtelsfs mtekmvqlne ekfslgveik tlkeqlslls raegakkeqv
      901 edsgaesspk hgphessaqe pvckdalqqe lewlrkeseq rkrklqaali srkellqkvs
      961 kleeelakvr eestkdslre sekreleeds knkddpekyg tsewrelevs lrltisekev
     1021 elegirrdlk ekaaaeeelq alvqrmtqdl qnktkqidll qeeitenqat iqkfitgtmd
     1081 agdgdsavke tsvsspprag ggehwkpele gkivdlekek tqlqkklqea lisrkailkk
     1141 aqekekhlke elkeqkdayr hlqeqfdgqs keneniaarl rqlqakestd qqlpgtgqqe
     1201 pthgseglsl egtepasesd lhaaqpshpg etatlqatvs vaqiqdqlke ievekeelel
     1261 kissttselt kkseevlllq eqineqglei qnlkaashea kahteqlkqe lessqlkiad
     1321 lehlktlqpe letlqkhvgq keeevsylvg qlgekeqtlt tvqtemeeqe rlikalhtql
     1381 emqakeheer lkqvqveice lkkqpkelee eskakqqlqr klqaalisrk ealkenkslq
     1441 eqlssardav ehltksladv esqvsvqnqe kdallgklal lqeerdkliv emdksllenq
     1501 slggsceslk lalggltedk eklmkelesv rcskiaeste wqekhkelqk eyevllqsye
     1561 nvsneaeriq hvvesvrqek qevyaklrsa esdkrerekq lqdaeqemee mkekmrkfak
     1621 skqqkilele eendrlraea qpvgganesm eallssnasl keeleritle yktlskefea
     1681 lmaekntlse etrnlklqve aqelkqasle tteksdepkd vieevteavv gksqeqdsls
     1741 enakledaea tllansakpg vsetfsshdd innylqqldq lkgriaelem ekqkdrelsq
     1801 tleneknall tqisakdsel klleeevaki nmlnqqiqee lsrvtklket aeeekddlee
     1861 rlmnqlaeln gsignyyqdv tdaqikneql esemqnlkrc vseleeekqq lvkektkves
     1921 eirkeymeki qgaqkgpgsk ihakelqell kekqqevkql qkdcirylgr isalektvka
     1981 lefvhtesqk dldatkgnla qavehhkkaq aelssfkill ddtqseaarv ladnlklkke
     2041 lqsnkesiks qikqkdedll rrleqaeekh rkekknmqek ldalhrekah vedtlaeiqv
     2101 sltrkdkdmk elqqsldstl aqlaaftksm sslqddrdrv ideakkweqr fgdaiqtkee
     2161 evrlkeenct alkdqlrqmt ihmeelkitv srlehdkeiw eskaqtelqh qqkaydklqe
     2221 enkelmsqle eagqlyhdsk neltklesel kslkdqstdl knslekcreh ennlegiikq
     2281 qeadiqnckf nceqletdlt asrelttrlh deinvkeqki isllsgkeea iqvaiaelhq
     2341 qhskeikele nllsqeeeen ltleeenkra vektnqltea letikkesle qkaqldsfvk
     2401 smsslqddrd rivsdyrqle erhlsvilek deliqdaaae nnklkeeirg lrghmddlns
     2461 enakldaeli qyrrdlnevi tikdsqqrql leaqlqqnke lrnecvkleg rlkgseaekq
     2521 slqmsldalq eenqglskei ksfkeqltal heegalavyh aqlrvreeev qkltaalsss
     2581 qkrtvdlqee lvcvqkeask kvseiedklk relkhlhhna gimrneteta eervaelard
     2641 lvemeqkllt vtkenkdlta qiqafgksms slqdsrdhat eelsdlkkky daslkelaql
     2701 kgrqdlgres dvlsqaafpl ttsenissrl eklnqqltsk deqllhlsse lesshnqvqs
     2761 ftkamtslqn erdhlwnele kfrkseegkq rsaapsaass paevqslkka msslqndrdr
     2821 llkelknlqq qylqmnqeit elrplkaqlq esqdqtkalq mmkeelrqen lswqhelhql
     2881 rveknswelh errmkeqylm aisdkdqqlg hlqnllrelr sssqtqilpt qyqrqassgt
     2941 saaldgsqnl vyetdclrtq lndslkeihq kelriqqlns kfsqlleekn ilstqlrdan
     3001 qslrdsqhhy snlfnhcail erqvqqlqat gplnadvapg apqekdgihi ktetettgee
     3061 qpsfsevqqq lcntkhdlse lkklleeerd qrltaenals lakeqirrle hsewesartp
     3121 iigacgsqeq vllmdlpgss crrtrssagw krvlrslcrs rtrvpllaai yflmihvllv
     3181 lcftghl
//
LOCUS       NP_001424625             593 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 16 [Rattus norvegicus].
ACCESSION   NP_001424625 XP_038943829
VERSION     NP_001424625.1
DBSOURCE    REFSEQ: accession NM_001437696.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943829.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2216632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..593
                     /product="dynamin-1-like protein isoform 16"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=65826
     Region          <1..106
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          76..361
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          497..587
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..593
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437696.1:424..2205"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mtkvpvgdqp kdielqirel ilrfisnpns iilavtaant dmatsealki srevdpdgrr
       61 tlavitkldl mdagtdamdv lmgrvipvkl giigvvnrsq ldinnkksvt dsirdeyafl
      121 qkkypslanr ngtkylartl nrllmhhird clpelktrin vlaaqyqsll nsygepvddk
      181 satllqlitk fateycntie gtakyietse lcggaricyi fhetfgrtle svdplgglnt
      241 idiltairna tgprpalfvp evsfellvkr qikrleepsl rcvelvheem qriiqhcsny
      301 stqellrfpk lhdaivevvt cllrkrlpvt nemvhnlvai elayintkhp dfadacglmn
      361 nnieeqrrnr larelpsavs rdksskvpsa lapasqepsp aasaeadgkl iqdnrretkn
      421 vasagggigd ggrigdggqe pttgnwrgml ktskaeella eekskpipim paspqkghav
      481 nlldvpvpva rklsareqrd cevierliks yflivrkniq dsvpkavmhf lvnhvkdtlq
      541 selvgqlyks sllddlltes edmaqrrkea admlkalqga sqiiaeiret hlw
//
LOCUS       NP_001424621             722 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 12 [Rattus norvegicus].
ACCESSION   NP_001424621 XP_038943826
VERSION     NP_001424621.1
DBSOURCE    REFSEQ: accession NM_001437692.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943826.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.70323.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..722
                     /product="dynamin-1-like protein isoform 12"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=80653
     Region          23..308
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,152,222,224..225,251..255,258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,156,169,194,196,198..201,203..204,225,
                     227..230,254..256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            152..155
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(154..155,185..186)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            221..224
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          231..516
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            251..253
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          626..716
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..722
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437692.1:135..2303"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswr veaeewgkfl htknklytdf deirqeiene
      121 terisgnnkg vspepihlkv fspnvvnltl vdlpgmtkvp vgdqpkdiel qirelilrfi
      181 snpnsiilav taantdmats ealkisrevd pdgrrtlavi tkldlmdagt damdvlmgrv
      241 ipvklgiigv vnrsqldinn kksvtdsird eyaflqkkyp slanrngtky lartlnrllm
      301 hhirdclpel ktrinvlaaq yqsllnsyge pvddksatll qlitkfatey cntiegtaky
      361 ietselcgga ricyifhetf grtlesvdpl gglntidilt airnatgprp alfvpevsfe
      421 llvkrqikrl eepslrcvel vheemqriiq hcsnystqel lrfpklhdai vevvtcllrk
      481 rlpvtnemvh nlvaielayi ntkhpdfada cglmnnniee qrrnrlarel psavsrdkli
      541 qdnrretknv asagggigdg grigdggqep ttgnwrgmlk tskaeellae ekskpipimp
      601 aspqkghavn lldvpvpvar klsareqrdc evierliksy flivrkniqd svpkavmhfl
      661 vnhvkdtlqs elvgqlykss llddlltese dmaqrrkeaa dmlkalqgas qiiaeireth
      721 lw
//
LOCUS       NP_001424628             556 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 19 [Rattus norvegicus].
ACCESSION   NP_001424628 XP_063126310
VERSION     NP_001424628.1
DBSOURCE    REFSEQ: accession NM_001437699.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126310.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.603237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..556
                     /product="dynamin-1-like protein isoform 19"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=62022
     Region          <1..106
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          76..361
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          460..550
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..556
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437699.1:442..2112"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mtkvpvgdqp kdielqirel ilrfisnpns iilavtaant dmatsealki srevdpdgrr
       61 tlavitkldl mdagtdamdv lmgrvipvkl giigvvnrsq ldinnkksvt dsirdeyafl
      121 qkkypslanr ngtkylartl nrllmhhird clpelktrin vlaaqyqsll nsygepvddk
      181 satllqlitk fateycntie gtakyietse lcggaricyi fhetfgrtle svdplgglnt
      241 idiltairna tgprpalfvp evsfellvkr qikrleepsl rcvelvheem qriiqhcsny
      301 stqellrfpk lhdaivevvt cllrkrlpvt nemvhnlvai elayintkhp dfadacglmn
      361 nnieeqrrnr larelpsavs rdkvasaggg igdggrigdg gqepttgnwr gmlktskaee
      421 llaeekskpi pimpaspqkg havnlldvpv pvarklsare qrdcevierl iksyflivrk
      481 niqdsvpkav mhflvnhvkd tlqselvgql ykssllddll tesedmaqrr keaadmlkal
      541 qgasqiiaei rethlw
//
LOCUS       NP_598285                938 aa            linear   ROD 09-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform 1 [Rattus norvegicus].
ACCESSION   NP_598285
VERSION     NP_598285.2
DBSOURCE    REFSEQ: accession NM_133601.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Zhang,Z.Y., Bai,H.H., Guo,Z., Li,H.L., Diao,X.T., Zhang,T.Y.,
            Yao,L., Ma,J.J., Cao,Z., Li,Y.X., Bai,X., Chen,H.K., Suo,Z.W.,
            Yang,X. and Hu,X.D.
  TITLE     Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn
  JOURNAL   Sci Signal 13 (638) (2020)
   PUBMED   32606037
  REMARK    GeneRIF: Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jeong,J.S., Kim,H.Y., Shin,B.S., Lee,A.R., Yoon,J.H., Hahm,T.S. and
            Lee,J.E.
  TITLE     Increased expression of the Cbl family of E3 ubiquitin ligases
            decreases Interleukin-2 production in a rat model of peripheral
            neuropathy
  JOURNAL   BMC Anesthesiol 18 (1), 87 (2018)
   PUBMED   30021515
  REMARK    GeneRIF: results suggest that ubiquitin and the E3 ubiquitin
            ligases c-Cbl and Cbl-b function as neuroimmune modulators in the
            subacute phase of neuropathic pain after nerve injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Uchida,T., Sakashita,Y., Kitahata,K., Yamashita,Y., Tomida,C.,
            Kimori,Y., Komatsu,A., Hirasaka,K., Ohno,A., Nakao,R.,
            Higashitani,A., Higashibata,A., Ishioka,N., Shimazu,T.,
            Kobayashi,T., Okumura,Y., Choi,I., Oarada,M., Mills,E.M.,
            Teshima-Kondo,S., Takeda,S., Tanaka,E., Tanaka,K., Sokabe,M. and
            Nikawa,T.
  TITLE     Reactive oxygen species upregulate expression of muscle
            atrophy-associated ubiquitin ligase Cbl-b in rat L6 skeletal muscle
            cells
  JOURNAL   Am J Physiol Cell Physiol 314 (6), C721-C731 (2018)
   PUBMED   29513566
  REMARK    GeneRIF: Under microgravity conditions, elevated ROS may be a
            crucial mechanotransducer in skeletal muscle cells, regulating
            muscle mass through Cbl-b expression activated by the ERK-Egr
            signaling pathway.
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Li,P., Liu,H.L., Zhang,Z.Q., Lv,X.D., Chang,Y.X., Wang,H.J., Ma,J.,
            Ma,Z.Y., Qu,X.J. and Teng,Y.E.
  TITLE     Single nucleotide polymorphisms of casitas B-lineage lymphoma
            proto-oncogene-b predict outcomes of patients with advanced
            non-small cell lung cancer after first-line platinum based doublet
            chemotherapy
  JOURNAL   J Thorac Dis 10 (3), 1635-1647 (2018)
   PUBMED   29707316
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Li,P., Liu,H., Zhang,Z., Lv,X., Wang,H., Ma,J., Ma,Z., Qu,X. and
            Teng,Y.E.
  TITLE     Expression and Comparison of Cbl-b in Lung Squamous Cell Carcinoma
            and Adenocarcinoma
  JOURNAL   Med Sci Monit 24, 623-635 (2018)
   PUBMED   29384143
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Thirone,A.C., Carvalheira,J.B., Hirata,A.E., Velloso,L.A. and
            Saad,M.J.
  TITLE     Regulation of Cbl-associated protein/Cbl pathway in muscle and
            adipose tissues of two animal models of insulin resistance
  JOURNAL   Endocrinology 145 (1), 281-293 (2004)
   PUBMED   14525909
  REMARK    GeneRIF: CAP-Cbl pathway may have a role in the modulation of
            adiposity in fasting and in monosodium glutamate treated rats.
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Zhang,W., Shao,Y., Fang,D., Huang,J., Jeon,M.S. and Liu,Y.C.
  TITLE     Negative regulation of T cell antigen receptor-mediated Crk-L-C3G
            signaling and cell adhesion by Cbl-b
  JOURNAL   J Biol Chem 278 (26), 23978-23983 (2003)
   PUBMED   12697763
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Nishio,H., Otsuka,M., Kinoshita,S., Tokuoka,T., Nakajima,M.,
            Noda,Y., Fukuyama,Y. and Suzuki,K.
  TITLE     Phosphorylation of c-Cbl protooncogene product following ethanol
            administration in rat cerebellum: possible involvement of Fyn
            kinase
  JOURNAL   Brain Res 950 (1-2), 203-209 (2002)
   PUBMED   12231245
  REMARK    GeneRIF: c-Cbl protooncogene product is tyrosine- phosphorylated in
            rat cerebellum in response to ethanol administration.
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Yokoi,N., Komeda,K., Wang,H.Y., Yano,H., Kitada,K., Saitoh,Y.,
            Seino,Y., Yasuda,K., Serikawa,T. and Seino,S.
  TITLE     Cblb is a major susceptibility gene for rat type 1 diabetes
            mellitus
  JOURNAL   Nat Genet 31 (4), 391-394 (2002)
   PUBMED   12118252
  REMARK    GeneRIF: we report the positional cloning of Iddm/kdp1 and identify
            a nonsense mutation in Cblb, a member of the Cbl/Sli family of
            ubiquitin-protein ligases.Cblb is a major susceptibility gene for
            rat type 1 diabetes mellitus
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Krawczyk,C., Bachmaier,K., Sasaki,T., Jones,R.G., Snapper,S.B.,
            Bouchard,D., Kozieradzki,I., Ohashi,P.S., Alt,F.W. and
            Penninger,J.M.
  TITLE     Cbl-b is a negative regulator of receptor clustering and raft
            aggregation in T cells
  JOURNAL   Immunity 13 (4), 463-473 (2000)
   PUBMED   11070165
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced NP_598285.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB071283.1, SRR26360172.345295.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..938
                     /product="E3 ubiquitin-protein ligase CBL-B isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; SH3-binding
                     protein CBL-B; signal transduction protein CBL-B; casitas
                     B-lineage lymphoma proto-oncogene b; RING-type E3
                     ubiquitin transferase CBL-B; Casitas B-lineage lymphoma b;
                     Cas-Br-M (murine) ecotropic retroviral transforming
                     sequence b; Cbl proto-oncogene B, E3 ubiquitin protein
                     ligase; Cbl proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=104492
     Region          35..167
                     /region_name="4H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          41..167
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          168..240
                     /region_name="EF-hand-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          171..254
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          241..343
                     /region_name="SH2-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          248..344
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(266,286,288..291,296,308,310)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCQ.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            order(311..314,327..329)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          344..372
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          351..426
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(362..363,366,390,409..412)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            order(366..368,374..377,396,399..400,403,409..410,412)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          465..588
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          543..567
                     /region_name="Interaction with VAV1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          702..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13191; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          771..885
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          847..883
                     /region_name="Interaction with SH3KBP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4S7.1)"
     Region          887..927
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(889..890,892..894,896..897,902,906)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..938
                     /gene="Cblb"
                     /coded_by="NM_133601.2:163..2979"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171136"
                     /db_xref="RGD:620535"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr rnltklslif shmlaeikai fpngqfqgdn fritkadaae
      181 fwrkffgdkt ivpwkvfrqc lhevhqissg leamalksti dltcndyisv fefdiftrlf
      241 qpwgsilrnw nflavthpgy mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv
      301 tgdgnilqti phnkplfqal idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy
      361 elycemgstf qlckicaend kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep
      421 iivdpfdprd egsrccsiid pfsipmldld ddddreeslm mnrlasvrkc tdrqnspvts
      481 pgssplaqrr kpqpdplqip hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq
      541 dkplpapppp lrdppppper pppippdsrl srhfhhgegv psrdqpmple awcprdafgt
      601 nqvmgcrilg dgspkpgvta nsnlngrhsr mgsdqvlmrk hrrhdlpseg akvfsnghla
      661 peeydvpprl sppppvtall psikctgpia nclsektrdt veedddeyki psshpvslns
      721 qpshchnvkp pvrscdnghc ilngthgtps emkksnipdl giylkgedaf dalppslppp
      781 ppparhslie hskppgsssr pssgqdlfll psdpffdpas gqvplpparr apgdgvksnr
      841 asqdydqlps ssdgsqapar ppkprprrta peihhrkphg peaalenvda kiaklmgegy
      901 afeevkrale iaqnnlevar silrefafpp pvsprlnl
//
LOCUS       NP_446107                716 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_446107
VERSION     NP_446107.2
DBSOURCE    REFSEQ: accession NM_053655.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Oct 20, 2005 this sequence version replaced NP_446107.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085843.1, SRR26643297.39009.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..716
                     /product="dynamin-1-like protein isoform 1"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=79820
     Region          23..302
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,146,216,218..219,245..249,252)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,150,163,188,190,192..195,197..198,219,
                     221..224,248..250)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            146..149
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(148..149,179..180)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            215..218
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          225..510
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            245..247
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          620..710
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..716
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_053655.4:135..2285"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengveaeew gkflhtknkl ytdfdeirqe ieneterisg
      121 nnkgvspepi hlkvfspnvv nltlvdlpgm tkvpvgdqpk dielqireli lrfisnpnsi
      181 ilavtaantd matsealkis revdpdgrrt lavitkldlm dagtdamdvl mgrvipvklg
      241 iigvvnrsql dinnkksvtd sirdeyaflq kkypslanrn gtkylartln rllmhhirdc
      301 lpelktrinv laaqyqslln sygepvddks atllqlitkf ateycntieg takyietsel
      361 cggaricyif hetfgrtles vdplgglnti diltairnat gprpalfvpe vsfellvkrq
      421 ikrleepslr cvelvheemq riiqhcsnys tqellrfpkl hdaivevvtc llrkrlpvtn
      481 emvhnlvaie layintkhpd fadacglmnn nieeqrrnrl arelpsavsr dkliqdnrre
      541 tknvasaggg igdggrigdg gqepttgnwr gmlktskaee llaeekskpi pimpaspqkg
      601 havnlldvpv pvarklsare qrdcevierl iksyflivrk niqdsvpkav mhflvnhvkd
      661 tlqselvgql ykssllddll tesedmaqrr keaadmlkal qgasqiiaei rethlw
//
LOCUS       NP_001424723             276 aa            linear   ROD 09-APR-2025
DEFINITION  BPI fold-containing family A member 3 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424723 XP_038961811
VERSION     NP_001424723.1
DBSOURCE    REFSEQ: accession NM_001437794.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038961811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.528124.1,
                                           SRR26360181.303831.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..276
                     /product="BPI fold-containing family A member 3 isoform 2
                     precursor"
                     /calculated_mol_wt=28438
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2277
     Region          47..207
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     CDS             1..276
                     /gene="Bpifa3"
                     /gene_synonym="Splunc3"
                     /coded_by="NM_001437794.1:202..1032"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:690402"
                     /db_xref="RGD:1596102"
ORIGIN      
        1 mhllwrflvl llgllalpsa lpkqpwpglt kahkdgrstl ariiaqgllk hnaegriqsm
       61 rlldrlnvsg tvapgmvswl isgmnfqqqq eisinitnvq ldcggiqmaf pkewfsanit
      121 lefdiefklp fnsnilktha qmglaaeswl ekdefgrrkl vtgrcqmeps sdsasmttea
      181 aspkmknflh nlreslgkvi pnlvesqnrw llitlvspes vksllsgsrg lplpaigqke
      241 vllveilrls qcvasavpwk ndpqvprhpv lsnnkl
//
LOCUS       NP_001424640             264 aa            linear   ROD 09-APR-2025
DEFINITION  COP9 signalosome complex subunit 7b [Rattus norvegicus].
ACCESSION   NP_001424640
VERSION     NP_001424640.1
DBSOURCE    REFSEQ: accession NM_001437711.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Sharon,M., Mao,H., Boeri Erba,E., Stephens,E., Zheng,N. and
            Robinson,C.V.
  TITLE     Symmetrical modularity of the COP9 signalosome complex suggests its
            multifunctionality
  JOURNAL   Structure 17 (1), 31-40 (2009)
   PUBMED   19141280
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.118827.1,
                                           SRR26360190.1938088.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..264
                     /product="COP9 signalosome complex subunit 7b"
                     /note="COP9 (constitutive photomorphogenic) homolog,
                     subunit 7b; COP9 constitutive photomorphogenic homolog
                     subunit 7B"
                     /calculated_mol_wt=29502
     Region          88..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     CDS             1..264
                     /gene="Cops7b"
                     /coded_by="NM_001437711.1:164..958"
                     /db_xref="GeneID:363273"
                     /db_xref="RGD:1306918"
ORIGIN      
        1 mageqkpssn lleqfillak gtsgsalttl isqvleapgv yvfgellela nvqelaegan
       61 aaylqllnlf aygtypdyia nkeslpelsa aqqnklkhlt ivslasrmkc ipysvllkdl
      121 emrnlreled liieavytdi iqgkldqrnq llevdfcigr diqkkdinni vktlhewcdg
      181 ceavllgieq qvlranqyke nhhrtqqqve aevsnikktl katasssaqe meqqlaerec
      241 pphteqrqpt kkmskvkglv ssrh
//
LOCUS       NP_001424620             724 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424620 XP_038943825
VERSION     NP_001424620.1
DBSOURCE    REFSEQ: accession NM_001437691.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943825.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF132727.1, SRR26643296.30241.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..724
                     /product="dynamin-1-like protein isoform 11"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=80706
     Region          23..321
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,165,235,237..238,264..268,271)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,169,182,207,209,211..214,216..217,238,
                     240..243,267..269)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            165..168
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(167..168,198..199)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            234..237
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          244..529
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            264..266
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          628..718
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..724
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437691.1:135..2309"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswn patwknsrhl skgveaeewg kflhtknkly
      121 tdfdeirqei eneterisgn nkgvspepih lkvfspnvvn ltlvdlpgmt kvpvgdqpkd
      181 ielqirelil rfisnpnsii lavtaantdm atsealkisr evdpdgrrtl avitkldlmd
      241 agtdamdvlm grvipvklgi igvvnrsqld innkksvtds irdeyaflqk kypslanrng
      301 tkylartlnr llmhhirdcl pelktrinvl aaqyqsllns ygepvddksa tllqlitkfa
      361 teycntiegt akyietselc ggaricyifh etfgrtlesv dplgglntid iltairnatg
      421 prpalfvpev sfellvkrqi krleepslrc velvheemqr iiqhcsnyst qellrfpklh
      481 daivevvtcl lrkrlpvtne mvhnlvaiel ayintkhpdf adacglmnnn ieeqrrnrla
      541 relpsavsrd kvasagggig dggrigdggq epttgnwrgm lktskaeell aeekskpipi
      601 mpaspqkgha vnlldvpvpv arklsareqr dcevierlik syflivrkni qdsvpkavmh
      661 flvnhvkdtl qselvgqlyk ssllddllte sedmaqrrke aadmlkalqg asqiiaeire
      721 thlw
//
LOCUS       NP_001424687            1070 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424687 XP_063126571
VERSION     NP_001424687.1
DBSOURCE    REFSEQ: accession NM_001437758.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126571.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.29828.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1070
                     /product="activated CDC42 kinase 1 isoform 5"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=118436
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          145..402
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285,304..308,317,351)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(267,271,304..308,317,351)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(284..294,296..310)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          410..459
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(412,414,419,437,439,454,456..457)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          464..529
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <610..986
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          812..870
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          991..1034
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1021..1060
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1070
                     /gene="Tnk2"
                     /coded_by="NM_001437758.1:325..3537"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk stfrkpsptp
      121 gglagegtlq sltcligekd lrlleklgdg sfgvvrrgew dapagktvsv avkclkpdvl
      181 sqpeamddfi revnamhsld hrnlirlygv vltppmkmvt elaplgslld rlrkhqghfl
      241 lgtlsryavq vaegmgyles krfihrdlaa rnlllatrdl vkigdfglmr alpqnddhyv
      301 mqehrkvpfa wcapeslktr tfshasdtwm fgvtlwemft ygqepwigln gsqilhkidk
      361 egerlprped cpqdiynvmv qcwahkpedr ptfvalrdfl leaqptdmra lqdfeepdkl
      421 hiqmndvitv iegraenyww rgqntrtlcv gpfprnvvts vaglsaqdis qplqnsfiht
      481 ghgdsdprhc wgfpdridel ylgnpmdppd llsvelstsr ptqhlgrmkr eppprppqpa
      541 ifthkptydp vsedpdplss dfkrlglrkp alprglwlak psarvpgtka grssggevtl
      601 idfgeepvap tprpcapsla qlamdacsll dktppqsptr alprplhptp vvdwdarplp
      661 pppayddvaq deddfevcsi nstlvsaglp tgpsqgetny afvpeqaqlp palednlflp
      721 pqgggqppss aqtaeifqal qqecmrqlqv ptgqltpspt pggddkpqvp prvpipprpt
      781 rprvglspap lgeeeasrwp gpsspprvpp replspqgsr tpsplvppgs splphrlsss
      841 pgktmpttqs fasdpkyatp qviqapgpra gpcilpivrd grkvssthyy llperppyle
      901 ryqrflreaq speepaalpv ppllpppstp apaaptatvr pmpqaapdpk anfstnnsnp
      961 gaqppslras arlpqrgcpg dgqeaarpad kvqmlqamvh gvtteecqaa lrshswsiqr
     1021 aaqylkveql fglglrprve chkvlemfdw nleqagchll gscgpahhkr
//
LOCUS       NP_001424637             463 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424637 XP_063126323
VERSION     NP_001424637.1
DBSOURCE    REFSEQ: accession NM_001437708.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126323.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.46681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..463
                     /product="transcriptional regulator ERG isoform 6"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=51993
     Region          122..205
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          294..377
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..463
                     /gene="Erg"
                     /coded_by="NM_001437708.1:260..1651"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 miqtvpdpea qikealsvvs edqslfecay gtphlaktem tassssdygq tskmsprvpq
       61 qdwlsqppar vtikmecnps qvngsrnspd ecsvtkggkm vgspdtvgms ygsymeekhm
      121 pppnmttner rvivpadptl wstdhvrqwl ewavkeygll dvdvllfqni dgkelckmtk
      181 ddfqrltpsy nadillshlh ylretplphl tsddvdkalq nsprlmharn tggaafifpn
      241 tsvypeatqr ittrpaaqps pstvpktedq rpqldpyqil gptssrlanp gsgqiqlwqf
      301 llellsdssn sncitwegtn gefkmtdpde varrwgerks kpnmnydkls ralryyydkn
      361 imtkvhgkry aykfdfhgia qalqphppes slykypsdlp ymgsyhthpq kmnfvaphpp
      421 alpvtsssff atpnpywnsp tggiypntrl pashmpshlg tyy
//
LOCUS       NP_001424696             442 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424696 XP_063126595
VERSION     NP_001424696.1
DBSOURCE    REFSEQ: accession NM_001437767.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126595.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.41306.1,
                                           SRR26360176.1665178.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..442
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 2"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=50542
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <293..>437
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <385..>425
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..442
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437767.1:180..1508"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqraasik isslglerwl sg
//
LOCUS       NP_001008762            1181 aa            linear   ROD 09-APR-2025
DEFINITION  sodium/hydrogen exchanger 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001008762 XP_221463
VERSION     NP_001008762.2
DBSOURCE    REFSEQ: accession NM_001008762.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Wang,D., King,S.M., Quill,T.A., Doolittle,L.K. and Garbers,D.L.
  TITLE     A new sperm-specific Na+/H+ exchanger required for sperm motility
            and fertility
  JOURNAL   Nat Cell Biol 5 (12), 1117-1122 (2003)
   PUBMED   14634667
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Dec 23, 2009 this sequence version replaced NP_001008762.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1181
                     /product="sodium/hydrogen exchanger 10 isoform 1"
                     /note="sperm-specific sodium proton exchanger;
                     sodium/hydrogen exchanger 10; solute carrier family 9,
                     member 10; solute carrier family 9, subfamily C
                     (Na+-transporting carboxylic acid decarboxylase), member
                     1"
                     /calculated_mol_wt=136095
     Region          37..556
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          893..1020
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(974..975,984..986)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(1006..1008,1013..1015)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..1181
                     /gene="Slc9c1"
                     /gene_synonym="Gm610; Slc9a10"
                     /coded_by="NM_001008762.3:210..3755"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288117"
                     /db_xref="RGD:1309075"
ORIGIN      
        1 meevfenltt thnvklsnaw ldllksvfls tpqdlpeiil ilslictiga flnmhlkdfp
       61 iplpvilfli gccfeilsfa stqiqlyada iqwmdpdmff giftpviifn vafdmdiyml
      121 qklfwqilli tipgfminyt lilwylqsvn klslktipwl lfsavlissd pmltsasird
      181 lglsrsltnl ingeslltsv isliiysavv qisfkskhmn htlahkvmst awsylvesfi
      241 tgilitkaiq lwmatifgdd vnhitlifsv lylifyvcel igmsgiftla tiglflnsts
      301 fkpgveafll efwnclsfig flmvftfigl lipahtylyi sfsdvyysln iyftlivlrl
      361 lvfllmspil srlghgfswr wafimvwsem kgtpninmal llaysdvslg serersqilf
      421 hgvsvcvitl ivnrfilpma viklglrdvt stkyksvyyt fqhfqeltks tamalkfdkd
      481 lanadwnmvd kaiilqnpya lnqeettehq kvkcpdcnke idetlnieam elanrrllsa
      541 qiasyqrqyr neilsqsamq vlvgaagsfg ekkgeymspe niknyseskk llsflrklll
      601 nwvyntkkdk gvpsrymflh achsivftne feytgyiavl mntypmiicw isrlkdiyqy
      661 eikcanyyfl tfyileallk vaamrkeffs htwllfelgi tlvgildiil ietdsisykf
      721 dltetvvfmn vvrllrilri lklitpkllq vidkrmsqqi sfryailkgy vqgemdvlni
      781 idqiasskqa kqillkrvir nmdhamkelg yleydhpeia vtmktkeevn vmlnmareiv
      841 kafrskgiih kvegaeinkl imakkkqvle lqsviqplnv eeapyyipwl sedpeaisfi
      901 qekakvvtfd cgnnifeegd epegiyviis gmvklkrskp hlemdrvsse sevaqtrsyt
      961 lphteyllsg eiigelnclt kermqysatc ktvvetyfip ishlyegfek kypnmkykmw
     1021 qkiglaitaq kirenlsfed wnykmqlklc nvfvrdipkt tktdiydetv thvvlihgsa
     1081 edcqlrkiyk apflipvtch qiqgleeftk vmiiqtsvav rkfrwnvkky npprrismkp
     1141 dstesletln esseddedkk eneeneeyle diidissvsk k
//
LOCUS       NP_596888                455 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 1 [Rattus norvegicus].
ACCESSION   NP_596888
VERSION     NP_596888.2
DBSOURCE    REFSEQ: accession NM_133397.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced NP_596888.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217228.1, BC072519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676784,
                                           SAMN16676785 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..455
                     /product="transcriptional regulator ERG isoform 1"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=51253
     Region          115..198
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          286..369
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..455
                     /gene="Erg"
                     /coded_by="NM_133397.3:155..1522"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 mastikeals vvsedqslfe caygtphlak temtassssd ygqtskmspr vpqqdwlsqp
       61 parvtikmec npsqvngsrn spdecsvtkg gkmvgspdtv gmsygsymee khmpppnmtt
      121 nerrvivpad ptlwstdhvr qwlewavkey glldvdvllf qnidgkelck mtkddfqrlt
      181 psynadills hlhylretpl phltsddvdk alqnsprlmh arntdlpyep prrstwtghs
      241 hptpqskaaq pspstvpkte dqrpqldpyq ilgptssrla npgsgqiqlw qfllellsds
      301 snsncitweg tngefkmtdp devarrwger kskpnmnydk lsralryyyd knimtkvhgk
      361 ryaykfdfhg iaqalqphpp esslykypsd lpymgsyhth pqkmnfvaph ppalpvtsss
      421 ffatpnpywn sptggiypnt rlpashmpsh lgtyy
//
LOCUS       NP_001424719             425 aa            linear   ROD 09-APR-2025
DEFINITION  paired box protein Pax-2 isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001424719 XP_063143204
VERSION     NP_001424719.1
DBSOURCE    REFSEQ: accession NM_001437790.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Ribeiro,P.C., Lojudice,F.H., Fernandes-Charpiot,I.M.M.,
            Baptista,M.A.S.F., de Almeida Araujo,S., Mendes,G.E.F.,
            Sogayar,M.C., Abbud-Filho,M. and Caldas,H.C.
  TITLE     Therapeutic potential of human induced pluripotent stem cells and
            renal progenitor cells in experimental chronic kidney disease
  JOURNAL   Stem Cell Res Ther 11 (1), 530 (2020)
   PUBMED   33298161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Wang,X.L., Hou,L., Zhao,C.G., Tang,Y., Zhang,B., Zhao,J.Y. and
            Wu,Y.B.
  TITLE     Screening of genes involved in epithelial-mesenchymal transition
            and differential expression of complement-related genes induced by
            PAX2 in renal tubules
  JOURNAL   Nephrology (Carlton) 24 (2), 263-271 (2019)
   PUBMED   29280536
  REMARK    GeneRIF: Pax2 overexpression by kidney tubule cells alters the
            expression of complement system proteins to induce
            epithelial-mesenchymal transition.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Hou,L., Du,Y., Zhao,C. and Wu,Y.
  TITLE     PAX2 may induce ADAM10 expression in renal tubular epithelial cells
            and contribute to epithelial-to-mesenchymal transition
  JOURNAL   Int Urol Nephrol 50 (9), 1729-1741 (2018)
   PUBMED   30117015
  REMARK    GeneRIF: PAX2 directly increased expression of ADAM10, the presence
            of which contributed to EMT in renal tubular epithelia and hence
            plays an important role in renal fibrosis.
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Larsson,M.
  TITLE     Pax2 is persistently expressed by GABAergic neurons throughout the
            adult rat dorsal horn
  JOURNAL   Neurosci Lett 638, 96-101 (2017)
   PUBMED   27939388
  REMARK    GeneRIF: Persistent Pax2 expression may be required to maintain a
            GABAergic phenotype.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Jiang,Y., Jiang,T., Ouyang,J., Zhou,Q., Liang,Y., Cui,Y., Chen,P.
            and Huang,B.
  TITLE     Cell atavistic transition: Paired box 2 re-expression occurs in
            mature tubular epithelial cells during acute kidney injury and is
            regulated by Angiotensin II
  JOURNAL   PLoS One 9 (4), e93563 (2014)
   PUBMED   24710423
  REMARK    GeneRIF: Those findings suggest that mature TECs can
            trans-differentiate into progenitor-like cells by 'atavistic
            transition', which may participate in the recovery of tissue
            structure and Pax2 may play a pivotal role in this process.
            Erratum:[PLoS One. 2015 May 06;10(5):e0127718. doi:
            10.1371/journal.pone.0127718. PMID: 25945929]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Ryan,G., Steele-Perkins,V., Morris,J.F., Rauscher,F.J. 3rd and
            Dressler,G.R.
  TITLE     Repression of Pax-2 by WT1 during normal kidney development
  JOURNAL   Development 121 (3), 867-875 (1995)
   PUBMED   7720589
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Eccles,M.R., Yun,K., Reeve,A.E. and Fidler,A.E.
  TITLE     Comparative in situ hybridization analysis of PAX2, PAX8, and WT1
            gene transcription in human fetal kidney and Wilms' tumors
  JOURNAL   Am J Pathol 146 (1), 40-45 (1995)
   PUBMED   7856737
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Sharma,P.M., Bowman,M., Yu,B.F. and Sukumar,S.
  TITLE     A rodent model for Wilms tumors: embryonal kidney neoplasms induced
            by N-nitroso-N'-methylurea
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9931-9935 (1994)
   PUBMED   7937920
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Poleev,A., Fickenscher,H., Mundlos,S., Winterpacht,A., Zabel,B.,
            Fidler,A., Gruss,P. and Plachov,D.
  TITLE     PAX8, a human paired box gene: isolation and expression in
            developing thyroid, kidney and Wilms' tumors
  JOURNAL   Development 116 (3), 611-623 (1992)
   PUBMED   1337742
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Plachov,D., Chowdhury,K., Walther,C., Simon,D., Guenet,J.L. and
            Gruss,P.
  TITLE     Pax8, a murine paired box gene expressed in the developing
            excretory system and thyroid gland
  JOURNAL   Development 110 (2), 643-651 (1990)
   PUBMED   1723950
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063143204.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.3973.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..425
                     /product="paired box protein Pax-2 isoform 3 precursor"
                     /note="paired box protein Pax-2; paired box gene 2; paired
                     box protein 2; paired box homeotic gene 2"
                     /calculated_mol_wt=41374
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3984
     Region          47..171
                     /region_name="PAX"
                     /note="Paired Box domain; smart00351"
                     /db_xref="CDD:128645"
     Site            order(52..53,58,60..62,64,69,81,83,92,95,97..98,102,
                     111..117,119..122,141..143,162,164..165,168,171)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238076"
     Region          313..424
                     /region_name="Pax2_C"
                     /note="Paired-box protein 2 C terminal; pfam12403"
                     /db_xref="CDD:463563"
     CDS             1..425
                     /gene="Pax2"
                     /gene_synonym="Pax-2"
                     /coded_by="NM_001437790.1:333..1610"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:293992"
                     /db_xref="RGD:1305568"
ORIGIN      
        1 meqcagravl klslrgdtaa aaallpllcl pmdmhckadp fsamhpghgg vnqlggvfvn
       61 grplpdvvrq rivelahqgv rpcdisrqlr vshgcvskil gryyetgsik pgviggskpk
      121 vatpkvvdki aeykrqnptm faweirdrll aegicdndtv psvssinrii rtkvqqpfhp
      181 tpdgagtgvt apghtivpst asppvssasn dpvgsysing ilgiprsnge krkreedvse
      241 gsvpngdsqs gvdslrkhlr adtftqqqle aldrvferps ypdvfqaseh ikseqgneys
      301 lpaltpglde vksslsastn pelgsnvsgt qtypvvtgrd masttlpgyp phvpptgqgs
      361 yptstlagmv pgsefsgnpy shpqytayne awrfsnpall sspyyysaap rgsapaaaaa
      421 aydrh
//
LOCUS       NP_001424623             711 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 14 [Rattus norvegicus].
ACCESSION   NP_001424623 XP_063126305
VERSION     NP_001424623.1
DBSOURCE    REFSEQ: accession NM_001437694.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 711)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 711)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 711)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 711)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 711)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126305.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.42047.1,
                                           SRR26643296.30243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..711
                     /product="dynamin-1-like protein isoform 14"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=79285
     Region          23..308
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,152,222,224..225,251..255,258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,156,169,194,196,198..201,203..204,225,
                     227..230,254..256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            152..155
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(154..155,185..186)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            221..224
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          231..516
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            251..253
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          615..705
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..711
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437694.1:135..2270"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswr veaeewgkfl htknklytdf deirqeiene
      121 terisgnnkg vspepihlkv fspnvvnltl vdlpgmtkvp vgdqpkdiel qirelilrfi
      181 snpnsiilav taantdmats ealkisrevd pdgrrtlavi tkldlmdagt damdvlmgrv
      241 ipvklgiigv vnrsqldinn kksvtdsird eyaflqkkyp slanrngtky lartlnrllm
      301 hhirdclpel ktrinvlaaq yqsllnsyge pvddksatll qlitkfatey cntiegtaky
      361 ietselcgga ricyifhetf grtlesvdpl gglntidilt airnatgprp alfvpevsfe
      421 llvkrqikrl eepslrcvel vheemqriiq hcsnystqel lrfpklhdai vevvtcllrk
      481 rlpvtnemvh nlvaielayi ntkhpdfada cglmnnniee qrrnrlarel psavsrdkva
      541 sagggigdgg rigdggqept tgnwrgmlkt skaeellaee kskpipimpa spqkghavnl
      601 ldvpvpvark lsareqrdce vierliksyf livrkniqds vpkavmhflv nhvkdtlqse
      661 lvgqlykssl lddlltesed maqrrkeaad mlkalqgasq iiaeirethl w
//
LOCUS       NP_001424648             697 aa            linear   ROD 09-APR-2025
DEFINITION  coiled-coil domain-containing protein 116 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424648 XP_038943994
VERSION     NP_001424648.1
DBSOURCE    REFSEQ: accession NM_001437719.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Wang,Y., Wu,W., Zhu,M., Wang,C., Shen,W., Cheng,Y., Geng,L., Li,Z.,
            Zhang,J., Dai,J., Ma,H., Chen,L., Hu,Z., Jin,G. and Shen,H.
  TITLE     Integrating expression-related SNPs into genome-wide gene- and
            pathway-based analyses identified novel lung cancer susceptibility
            genes
  JOURNAL   Int J Cancer 142 (8), 1602-1610 (2018)
   PUBMED   29193083
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Firat-Karalar,E.N., Sante,J., Elliott,S. and Stearns,T.
  TITLE     Proteomic analysis of mammalian sperm cells identifies new
            components of the centrosome
  JOURNAL   J Cell Sci 127 (Pt 19), 4128-4133 (2014)
   PUBMED   25074808
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943994.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.70220.1,
                                           SRR26360181.2164307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..697
                     /product="coiled-coil domain-containing protein 116
                     isoform 1"
                     /note="coiled-coil domain-containing protein 116; stromal
                     cell-derived factor 2-like 1"
                     /calculated_mol_wt=78077
     Region          18..409
                     /region_name="DUF4702"
                     /note="Domain of unknown function (DUF4702); pfam15774"
                     /db_xref="CDD:464862"
     Region          347..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B5.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8B5.1)"
     CDS             1..697
                     /gene="Ccdc116"
                     /gene_synonym="Sdf2l1"
                     /coded_by="NM_001437719.1:462..2555"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:287936"
                     /db_xref="RGD:1310080"
ORIGIN      
        1 marcrhhsgy laddeaahgt yvarlpkkhl lpemrptckl grvphlpsmn ryserqghqq
       61 nlrrprafgg fldfltegqv ldslqtvveq atecvatmkt eagvplvdvq drvevpnsrh
      121 rsrgrpsint vhrhrarptl caghpnnyps csssmsdshs svtagwlgsr sqdsdlgarg
      181 vgslppmrdk llleknlkrl lrleskgkvl nqhcsqrdsl lwdslgsqss sqptreqpls
      241 wfsgllasts vtpetselgl geqemiflkq elnkeiksll nqptsfnlpt ycplrephrt
      301 ldflsehhlf palqrvvsqa vdklshacrh ngfplfpvts elspvfpgns dlqpsskasl
      361 ptdrearget cysptsassp ktshrkskdr rgspsnavqm atrfrlkspn kflkkkalps
      421 issvsslsyi snpwfeeltn flveqavsll ickykfeesl nkqlgfisfp itevlmdifl
      481 gfkkvkgthi rlssdinwtc llrkleeaem arqalrhvsr sgtsphstsr ivtshhstgp
      541 ssrqpeltrd tdqdqspesh lslhpalpir qvmgprdsri gqkqtantnq searrsvist
      601 agmgsktkev vnieegkdte eeeeeeeeed eeeedeeeed eeedeeedee eeeeeergse
      661 eeetkdfsec ehapspplhe lensvnetti vspgdsq
//
LOCUS       NP_001424613             750 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424613 XP_038943818
VERSION     NP_001424613.1
DBSOURCE    REFSEQ: accession NM_001437684.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943818.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2283970.1,
                                           SRR26360176.886787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..750
                     /product="dynamin-1-like protein isoform 4"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=83142
     Region          23..321
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,165,235,237..238,264..268,271)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,169,182,207,209,211..214,216..217,238,
                     240..243,267..269)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            165..168
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(167..168,198..199)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            234..237
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          244..529
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            264..266
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          654..744
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..750
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437684.1:135..2387"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswn patwknsrhl skgveaeewg kflhtknkly
      121 tdfdeirqei eneterisgn nkgvspepih lkvfspnvvn ltlvdlpgmt kvpvgdqpkd
      181 ielqirelil rfisnpnsii lavtaantdm atsealkisr evdpdgrrtl avitkldlmd
      241 agtdamdvlm grvipvklgi igvvnrsqld innkksvtds irdeyaflqk kypslanrng
      301 tkylartlnr llmhhirdcl pelktrinvl aaqyqsllns ygepvddksa tllqlitkfa
      361 teycntiegt akyietselc ggaricyifh etfgrtlesv dplgglntid iltairnatg
      421 prpalfvpev sfellvkrqi krleepslrc velvheemqr iiqhcsnyst qellrfpklh
      481 daivevvtcl lrkrlpvtne mvhnlvaiel ayintkhpdf adacglmnnn ieeqrrnrla
      541 relpsavsrd ksskvpsala pasqepspaa saeadgkvas agggigdggr igdggqeptt
      601 gnwrgmlkts kaeellaeek skpipimpas pqkghavnll dvpvpvarkl sareqrdcev
      661 ierliksyfl ivrkniqdsv pkavmhflvn hvkdtlqsel vgqlykssll ddlltesedm
      721 aqrrkeaadm lkalqgasqi iaeirethlw
//
LOCUS       NP_001424611             761 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424611 XP_038943816
VERSION     NP_001424611.1
DBSOURCE    REFSEQ: accession NM_001437682.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943816.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.67895.1,
                                           SRR26360194.2130931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..761
                     /product="dynamin-1-like protein isoform 2"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=84510
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          23..321
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,165,235,237..238,264..268,271)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,169,182,207,209,211..214,216..217,238,
                     240..243,267..269)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          58..60
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          165..168
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            165..168
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(167..168,198..199)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          234..237
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            234..237
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          244..529
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          264..267
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            264..266
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          363..508
                     /region_name="Middle domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          467..710
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          521..588
                     /region_name="B domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          542..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            610
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            611
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            622
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K1M6; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:17301055,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK1 and PKA.
                     /evidence=ECO:0000269|PubMed:28463107; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          665..755
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          679..693
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     CDS             1..761
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437682.1:135..2420"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengkfqswn patwknsrhl skgveaeewg kflhtknkly
      121 tdfdeirqei eneterisgn nkgvspepih lkvfspnvvn ltlvdlpgmt kvpvgdqpkd
      181 ielqirelil rfisnpnsii lavtaantdm atsealkisr evdpdgrrtl avitkldlmd
      241 agtdamdvlm grvipvklgi igvvnrsqld innkksvtds irdeyaflqk kypslanrng
      301 tkylartlnr llmhhirdcl pelktrinvl aaqyqsllns ygepvddksa tllqlitkfa
      361 teycntiegt akyietselc ggaricyifh etfgrtlesv dplgglntid iltairnatg
      421 prpalfvpev sfellvkrqi krleepslrc velvheemqr iiqhcsnyst qellrfpklh
      481 daivevvtcl lrkrlpvtne mvhnlvaiel ayintkhpdf adacglmnnn ieeqrrnrla
      541 relpsavsrd ksskvpsala pasqepspaa saeadgkliq dnrretknva sagggigdgg
      601 rigdggqept tgnwrgmlkt skaeellaee kskpipimpa spqkghavnl ldvpvpvark
      661 lsareqrdce vierliksyf livrkniqds vpkavmhflv nhvkdtlqse lvgqlykssl
      721 lddlltesed maqrrkeaad mlkalqgasq iiaeirethl w
//
LOCUS       NP_001424652            1087 aa            linear   ROD 09-APR-2025
DEFINITION  histone deacetylase 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424652 XP_006245500
VERSION     NP_001424652.1
DBSOURCE    REFSEQ: accession NM_001437723.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Gu,X., Li,F., Che,X., Wei,X. and Li,P.
  TITLE     HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model
  JOURNAL   BMC Musculoskelet Disord 25 (1), 467 (2024)
   PUBMED   38879481
  REMARK    GeneRIF: HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Zhang,D., Du,J., Yu,M. and Suo,L.
  TITLE     Urine-derived stem cells-extracellular vesicles ameliorate diabetic
            osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by delivering
            microRNA-26a-5p
  JOURNAL   Cell Biol Toxicol 39 (5), 2243-2257 (2023)
   PUBMED   35554780
  REMARK    GeneRIF: Urine-derived stem cells-extracellular vesicles ameliorate
            diabetic osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by
            delivering microRNA-26a-5p.
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Yang,Y., Wang,Z., Xu,Y., Liu,X., Sun,Y. and Li,W.
  TITLE     Knockdown of lncRNA H19 alleviates ox-LDL-induced HCAECs
            inflammation and injury by mediating miR-20a-5p/HDAC4 axis
  JOURNAL   Inflamm Res 71 (9), 1109-1121 (2022)
   PUBMED   35854140
  REMARK    Erratum:[Inflamm Res. 2023 Apr;72(4):893. doi:
            10.1007/s00011-023-01701-7. PMID: 36806965]
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Moreno-Ruperez,A., Priego,T., Gonzalez-Nicolas,M.A.,
            Lopez-Calderon,A., Lazaro,A. and Martin,A.I.
  TITLE     Role of Glucocorticoid Signaling and HDAC4 Activation in Diaphragm
            and Gastrocnemius Proteolytic Activity in Septic Rats
  JOURNAL   Int J Mol Sci 23 (7), 3641 (2022)
   PUBMED   35408999
  REMARK    GeneRIF: Role of Glucocorticoid Signaling and HDAC4 Activation in
            Diaphragm and Gastrocnemius Proteolytic Activity in Septic Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Wei,W., Chen,W. and He,N.
  TITLE     HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation
  JOURNAL   J Transl Med 19 (1), 258 (2021)
   PUBMED   34118928
  REMARK    GeneRIF: HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Fischle,W., Dequiedt,F., Hendzel,M.J., Guenther,M.G., Lazar,M.A.,
            Voelter,W. and Verdin,E.
  TITLE     Enzymatic activity associated with class II HDACs is dependent on a
            multiprotein complex containing HDAC3 and SMRT/N-CoR
  JOURNAL   Mol Cell 9 (1), 45-57 (2002)
   PUBMED   11804585
REFERENCE   7  (residues 1 to 1087)
  AUTHORS   Lu,J., McKinsey,T.A., Zhang,C.L. and Olson,E.N.
  TITLE     Regulation of skeletal myogenesis by association of the MEF2
            transcription factor with class II histone deacetylases
  JOURNAL   Mol Cell 6 (2), 233-244 (2000)
   PUBMED   10983972
REFERENCE   8  (residues 1 to 1087)
  AUTHORS   Grozinger,C.M. and Schreiber,S.L.
  TITLE     Regulation of histone deacetylase 4 and 5 and transcriptional
            activity by 14-3-3-dependent cellular localization
  JOURNAL   Proc Natl Acad Sci U S A 97 (14), 7835-7840 (2000)
   PUBMED   10869435
REFERENCE   9  (residues 1 to 1087)
  AUTHORS   Lemercier,C., Verdel,A., Galloo,B., Curtet,S., Brocard,M.P. and
            Khochbin,S.
  TITLE     mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A
            transcriptional activity
  JOURNAL   J Biol Chem 275 (20), 15594-15599 (2000)
   PUBMED   10748098
REFERENCE   10 (residues 1 to 1087)
  AUTHORS   Grozinger,C.M., Hassig,C.A. and Schreiber,S.L.
  TITLE     Three proteins define a class of human histone deacetylases related
            to yeast Hda1p
  JOURNAL   Proc Natl Acad Sci U S A 96 (9), 4868-4873 (1999)
   PUBMED   10220385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006245500.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.34725.1,
                                           SRR26643295.36383.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..1087
                     /product="histone deacetylase 4 isoform 2"
                     /EC_number="3.5.1.98"
                     /note="HD4"
                     /calculated_mol_wt=119726
     Region          <90..151
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(92,96,107..108,111,118,122..123)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          117..312
                     /region_name="Interaction with MEF2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          132..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          204..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZM9; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          239..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          348..353
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and 14-3-3 proteins.
                     /evidence=ECO:0000250|UniProtKB:P56524"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          513..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          547..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          628..651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          652..1060
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Site            order(805..806,814..815,843,845,937,977)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Region          1054..1087
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          1062..1087
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     CDS             1..1087
                     /gene="Hdac4"
                     /coded_by="NM_001437723.1:519..3782"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363287"
                     /db_xref="RGD:619979"
ORIGIN      
        1 mssqshpdgl sgrdqpvell nparvnhmps tvdvatalpl qvapaavpmd lrldhqfslp
       61 lepalreqql qqellalkqk qqiqrqilia efqrqheqls rqheaqlheh ikqqqemlam
      121 khqqellehq rklerhrqeq elekqhreqk lqqlknkekg kesavastev kmklqefvln
      181 kkkalahrnl nhcmssdpry wygktqhssl dqssppqsgv sasynhpvlg mydakddfpl
      241 rktasepnlk lrsrlkqkva errsspllrr kdgpvatalk krpldvtdsa cssapgsgps
      301 spnsssgnvs tengiaptvp stpaetslah rlvtregsva plplytspsl pnitlglpat
      361 gpaagaagqq daerlalpal qqrislfpgt hltpylstsp lerdggaahn pllqhmvlle
      421 qpptqtplvt dwylsglgal plhtqslvga drvspsihkl rqhrplgrtq saplpqnaqa
      481 lqhlviqqqh qqflekhkqq fqqqqlhlsk miskpseppr qpeshpeete eelrehqall
      541 depyldrlpg qkepslagvq vkqepiesee eeveatreae psqrpateqe llfrqqalll
      601 eqqrihqlrn yqasmeaagi pvsfgshrpl sraqsspasa tfpmsvqepp tkprfttglv
      661 ydtlmlkhqc tcgntnshpe hagriqsiws rlqetglrgk cecirgrkat leelqtvhse
      721 ahtllygtnp lnrqkldskk llgsltsvfv rlpcggvgvd sdtiwnevhs sgaarlavgc
      781 vvelvfkvat gelkngfavv rppghhaees tpmgfcyfns vaiaakllqq rlnvskiliv
      841 dwdvhhgngt qqafyndpnv lymslhrydd gnffpgsgap devgtgpgvg fnvnmaftgg
      901 ldppmgdaey laafrtvvmp ianefapdvv lvssgfdave ghptplggyn lsakcfgylt
      961 kqlmglaggr ivlalegghd ltaicdasea cvsallgnel eplpekvlhq rpnanavhsm
     1021 ekvmgihsey wrclqrlspt vghslieaqk ceneeaetvt amaslsvgvk paekrseeep
     1081 meeeppl
//
LOCUS       NP_001424678            1181 aa            linear   ROD 09-APR-2025
DEFINITION  sodium/hydrogen exchanger 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424678 XP_017453415
VERSION     NP_001424678.1
DBSOURCE    REFSEQ: accession NM_001437749.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Wang,D., King,S.M., Quill,T.A., Doolittle,L.K. and Garbers,D.L.
  TITLE     A new sperm-specific Na+/H+ exchanger required for sperm motility
            and fertility
  JOURNAL   Nat Cell Biol 5 (12), 1117-1122 (2003)
   PUBMED   14634667
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_017453415.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.69079.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1181
                     /product="sodium/hydrogen exchanger 10 isoform 1"
                     /note="sperm-specific sodium proton exchanger;
                     sodium/hydrogen exchanger 10; solute carrier family 9,
                     member 10; solute carrier family 9, subfamily C
                     (Na+-transporting carboxylic acid decarboxylase), member
                     1"
                     /calculated_mol_wt=136095
     Region          37..556
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          893..1020
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(974..975,984..986)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(1006..1008,1013..1015)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..1181
                     /gene="Slc9c1"
                     /gene_synonym="Gm610; Slc9a10"
                     /coded_by="NM_001437749.1:491..4036"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:288117"
                     /db_xref="RGD:1309075"
ORIGIN      
        1 meevfenltt thnvklsnaw ldllksvfls tpqdlpeiil ilslictiga flnmhlkdfp
       61 iplpvilfli gccfeilsfa stqiqlyada iqwmdpdmff giftpviifn vafdmdiyml
      121 qklfwqilli tipgfminyt lilwylqsvn klslktipwl lfsavlissd pmltsasird
      181 lglsrsltnl ingeslltsv isliiysavv qisfkskhmn htlahkvmst awsylvesfi
      241 tgilitkaiq lwmatifgdd vnhitlifsv lylifyvcel igmsgiftla tiglflnsts
      301 fkpgveafll efwnclsfig flmvftfigl lipahtylyi sfsdvyysln iyftlivlrl
      361 lvfllmspil srlghgfswr wafimvwsem kgtpninmal llaysdvslg serersqilf
      421 hgvsvcvitl ivnrfilpma viklglrdvt stkyksvyyt fqhfqeltks tamalkfdkd
      481 lanadwnmvd kaiilqnpya lnqeettehq kvkcpdcnke idetlnieam elanrrllsa
      541 qiasyqrqyr neilsqsamq vlvgaagsfg ekkgeymspe niknyseskk llsflrklll
      601 nwvyntkkdk gvpsrymflh achsivftne feytgyiavl mntypmiicw isrlkdiyqy
      661 eikcanyyfl tfyileallk vaamrkeffs htwllfelgi tlvgildiil ietdsisykf
      721 dltetvvfmn vvrllrilri lklitpkllq vidkrmsqqi sfryailkgy vqgemdvlni
      781 idqiasskqa kqillkrvir nmdhamkelg yleydhpeia vtmktkeevn vmlnmareiv
      841 kafrskgiih kvegaeinkl imakkkqvle lqsviqplnv eeapyyipwl sedpeaisfi
      901 qekakvvtfd cgnnifeegd epegiyviis gmvklkrskp hlemdrvsse sevaqtrsyt
      961 lphteyllsg eiigelnclt kermqysatc ktvvetyfip ishlyegfek kypnmkykmw
     1021 qkiglaitaq kirenlsfed wnykmqlklc nvfvrdipkt tktdiydetv thvvlihgsa
     1081 edcqlrkiyk apflipvtch qiqgleeftk vmiiqtsvav rkfrwnvkky npprrismkp
     1141 dstesletln esseddedkk eneeneeyle diidissvsk k
//
LOCUS       NP_001424627             567 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 18 [Rattus norvegicus].
ACCESSION   NP_001424627 XP_063126308
VERSION     NP_001424627.1
DBSOURCE    REFSEQ: accession NM_001437698.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126308.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.612294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..567
                     /product="dynamin-1-like protein isoform 18"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=63390
     Region          <1..106
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          76..361
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          471..561
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..567
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437698.1:424..2127"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mtkvpvgdqp kdielqirel ilrfisnpns iilavtaant dmatsealki srevdpdgrr
       61 tlavitkldl mdagtdamdv lmgrvipvkl giigvvnrsq ldinnkksvt dsirdeyafl
      121 qkkypslanr ngtkylartl nrllmhhird clpelktrin vlaaqyqsll nsygepvddk
      181 satllqlitk fateycntie gtakyietse lcggaricyi fhetfgrtle svdplgglnt
      241 idiltairna tgprpalfvp evsfellvkr qikrleepsl rcvelvheem qriiqhcsny
      301 stqellrfpk lhdaivevvt cllrkrlpvt nemvhnlvai elayintkhp dfadacglmn
      361 nnieeqrrnr larelpsavs rdkliqdnrr etknvasagg gigdggrigd ggqepttgnw
      421 rgmlktskae ellaeekskp ipimpaspqk ghavnlldvp vpvarklsar eqrdcevier
      481 liksyflivr kniqdsvpka vmhflvnhvk dtlqselvgq lykssllddl ltesedmaqr
      541 rkeaadmlka lqgasqiiae irethlw
//
LOCUS       NP_001424695             442 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424695 XP_038944281
VERSION     NP_001424695.1
DBSOURCE    REFSEQ: accession NM_001437766.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038944281.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2856034.1,
                                           SRR26360194.1883352.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..442
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 2"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=50542
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <293..>437
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <385..>425
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..442
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437766.1:175..1503"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqraasik isslglerwl sg
//
LOCUS       NP_001019911             540 aa            linear   ROD 09-APR-2025
DEFINITION  coiled-coil domain-containing protein 116 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001019911 XP_237828
VERSION     NP_001019911.1
DBSOURCE    REFSEQ: accession NM_001024740.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wang,Y., Wu,W., Zhu,M., Wang,C., Shen,W., Cheng,Y., Geng,L., Li,Z.,
            Zhang,J., Dai,J., Ma,H., Chen,L., Hu,Z., Jin,G. and Shen,H.
  TITLE     Integrating expression-related SNPs into genome-wide gene- and
            pathway-based analyses identified novel lung cancer susceptibility
            genes
  JOURNAL   Int J Cancer 142 (8), 1602-1610 (2018)
   PUBMED   29193083
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Firat-Karalar,E.N., Sante,J., Elliott,S. and Stearns,T.
  TITLE     Proteomic analysis of mammalian sperm cells identifies new
            components of the centrosome
  JOURNAL   J Cell Sci 127 (Pt 19), 4128-4133 (2014)
   PUBMED   25074808
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Jun 10, 2005 this sequence version replaced XP_237828.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.70231.1,
                                           SRR26360181.2615745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..540
                     /product="coiled-coil domain-containing protein 116
                     isoform 2"
                     /note="coiled-coil domain-containing protein 116; stromal
                     cell-derived factor 2-like 1"
                     /calculated_mol_wt=59549
     Region          18..410
                     /region_name="DUF4702"
                     /note="Domain of unknown function (DUF4702); pfam15774"
                     /db_xref="CDD:464862"
     Region          347..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B5.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8B5.1)"
     CDS             1..540
                     /gene="Ccdc116"
                     /gene_synonym="Sdf2l1"
                     /coded_by="NM_001024740.2:132..1754"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:287936"
                     /db_xref="RGD:1310080"
ORIGIN      
        1 marcrhhsgy laddeaahgt yvarlpkkhl lpemrptckl grvphlpsmn ryserqghqq
       61 nlrrprafgg fldfltegqv ldslqtvveq atecvatmkt eagvplvdvq drvevpnsrh
      121 rsrgrpsint vhrhrarptl caghpnnyps csssmsdshs svtagwlgsr sqdsdlgarg
      181 vgslppmrdk llleknlkrl lrleskgkvl nqhcsqrdsl lwdslgsqss sqptreqpls
      241 wfsgllasts vtpetselgl geqemiflkq elnkeiksll nqptsfnlpt ycplrephrt
      301 ldflsehhlf palqrvvsqa vdklshacrh ngfplfpvts elspvfpgns dlqpsskasl
      361 ptdrearget cysptsassp ktshrkskdr rgspsnavqm atrfrlkvtp tevsnvpips
      421 sqcmlkspns dlklqkqtta snhnhipqpr hglhltlpap gitvevascq gqlrgqvqhs
      481 latpchlhsh fpfpvfspfl plgksfstsp ptlcpevssr aglevleghl kgrgcfthhf
//
LOCUS       NP_001424697             442 aa            linear   ROD 09-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424697 XP_063126596
VERSION     NP_001424697.1
DBSOURCE    REFSEQ: accession NM_001437768.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126596.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1475429.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..442
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 2"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=50542
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <293..>437
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <385..>425
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..442
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437768.1:128..1456"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqraasik isslglerwl sg
//
LOCUS       NP_001424685            1092 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424685 XP_038944235
VERSION     NP_001424685.1
DBSOURCE    REFSEQ: accession NM_001437756.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1092)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1092)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1092)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1092)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1092)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1092)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1092)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038944235.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.29827.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1092
                     /product="activated CDC42 kinase 1 isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=120717
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          145..402
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285,304..308,317,351)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(147..149,155,171,173,220..223,227,267,271..272,274,
                     285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(267,271,304..308,317,351)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(284..294,296..310)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          410..459
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(412,414,419,437,439,454,456..457)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          464..529
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <632..998
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          834..892
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          1013..1056
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1043..1082
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1092
                     /gene="Tnk2"
                     /coded_by="NM_001437756.1:326..3604"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk stfrkpsptp
      121 gglagegtlq sltcligekd lrlleklgdg sfgvvrrgew dapagktvsv avkclkpdvl
      181 sqpeamddfi revnamhsld hrnlirlygv vltppmkmvt elaplgslld rlrkhqghfl
      241 lgtlsryavq vaegmgyles krfihrdlaa rnlllatrdl vkigdfglmr alpqnddhyv
      301 mqehrkvpfa wcapeslktr tfshasdtwm fgvtlwemft ygqepwigln gsqilhkidk
      361 egerlprped cpqdiynvmv qcwahkpedr ptfvalrdfl leaqptdmra lqdfeepdkl
      421 hiqmndvitv iegraenyww rgqntrtlcv gpfprnvvts vaglsaqdis qplqnsfiht
      481 ghgdsdprhc wgfpdridel ylgnpmdppd llsvelstsr ptqhlgrmkr eppprppqpa
      541 ifthskwgcs gclgprplsp lsplleepty dpvsedpdpl ssdfkrlglr kpalprglwl
      601 akpsarvpgt kagrssggev tlidfgeepv aptprpcaps laqlamdacs lldktppqsp
      661 tralprplhp tpvvdwdarp lppppayddv aqdeddfevc sinstlvsag lptgpsqget
      721 nyafvpeqaq lppalednlf lppqgggqpp ssaqtaeifq alqqecmrql qvptgqltps
      781 ptpggddkpq vpprvpippr ptrprvglsp aplgeeeasr wpgpsspprv ppreplspqg
      841 srtpsplvpp gssplphrls sspgktmptt qsfasdpkya tpqviqapgp ragpcilpiv
      901 rdgrkvssth yyllperppy leryqrflre aqspeepaal pvppllppps tpapaaptat
      961 vrpmpqaapd pkanfstnns npgaqppslr asarlpqrgc pgdgqeaarp adkvqmlqam
     1021 vhgvtteecq aalrshswsi qraaqylkve qlfglglrpr vechkvlemf dwnleqagch
     1081 llgscgpahh kr
//
LOCUS       NP_001424686            1072 aa            linear   ROD 09-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424686 XP_017453473
VERSION     NP_001424686.1
DBSOURCE    REFSEQ: accession NM_001437757.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1072)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1072)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1072)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1072)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1072)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1072)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1072)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_017453473.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.45967.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1072
                     /product="activated CDC42 kinase 1 isoform 4"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=118667
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          162..419
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302,321..325,334,368)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(284,288,321..325,334,368)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(301..311,313..327)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          427..476
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(429,431,436,454,456,471,473..474)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          481..546
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <612..978
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          814..872
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          993..1036
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1023..1062
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1072
                     /gene="Tnk2"
                     /coded_by="NM_001437757.1:325..3543"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk vfsgkrqeae
      121 fpshhsqstf rkpsptpggl agegtlqslt cligekdlrl leklgdgsfg vvrrgewdap
      181 agktvsvavk clkpdvlsqp eamddfirev namhsldhrn lirlygvvlt ppmkmvtela
      241 plgslldrlr khqghfllgt lsryavqvae gmgyleskrf ihrdlaarnl llatrdlvki
      301 gdfglmralp qnddhyvmqe hrkvpfawca peslktrtfs hasdtwmfgv tlwemftygq
      361 epwiglngsq ilhkidkege rlprpedcpq diynvmvqcw ahkpedrptf valrdfllea
      421 qptdmralqd feepdklhiq mndvitvieg raenywwrgq ntrtlcvgpf prnvvtsvag
      481 lsaqdisqpl qnsfihtghg dsdprhcwgf pdridelylg npmdppdlls velstsrptq
      541 hlgrmkkpty dpvsedpdpl ssdfkrlglr kpalprglwl akpsarvpgt kagrssggev
      601 tlidfgeepv aptprpcaps laqlamdacs lldktppqsp tralprplhp tpvvdwdarp
      661 lppppayddv aqdeddfevc sinstlvsag lptgpsqget nyafvpeqaq lppalednlf
      721 lppqgggqpp ssaqtaeifq alqqecmrql qvptgqltps ptpggddkpq vpprvpippr
      781 ptrprvglsp aplgeeeasr wpgpsspprv ppreplspqg srtpsplvpp gssplphrls
      841 sspgktmptt qsfasdpkya tpqviqapgp ragpcilpiv rdgrkvssth yyllperppy
      901 leryqrflre aqspeepaal pvppllppps tpapaaptat vrpmpqaapd pkanfstnns
      961 npgaqppslr asarlpqrgc pgdgqeaarp adkvqmlqam vhgvtteecq aalrshswsi
     1021 qraaqylkve qlfglglrpr vechkvlemf dwnleqagch llgscgpahh kr
//
LOCUS       NP_001424626             582 aa            linear   ROD 09-APR-2025
DEFINITION  dynamin-1-like protein isoform 17 [Rattus norvegicus].
ACCESSION   NP_001424626 XP_063126307
VERSION     NP_001424626.1
DBSOURCE    REFSEQ: accession NM_001437697.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063126307.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.691021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..582
                     /product="dynamin-1-like protein isoform 17"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=64458
     Region          <1..106
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          76..361
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          486..576
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..582
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437697.1:424..2172"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mtkvpvgdqp kdielqirel ilrfisnpns iilavtaant dmatsealki srevdpdgrr
       61 tlavitkldl mdagtdamdv lmgrvipvkl giigvvnrsq ldinnkksvt dsirdeyafl
      121 qkkypslanr ngtkylartl nrllmhhird clpelktrin vlaaqyqsll nsygepvddk
      181 satllqlitk fateycntie gtakyietse lcggaricyi fhetfgrtle svdplgglnt
      241 idiltairna tgprpalfvp evsfellvkr qikrleepsl rcvelvheem qriiqhcsny
      301 stqellrfpk lhdaivevvt cllrkrlpvt nemvhnlvai elayintkhp dfadacglmn
      361 nnieeqrrnr larelpsavs rdksskvpsa lapasqepsp aasaeadgkv asagggigdg
      421 grigdggqep ttgnwrgmlk tskaeellae ekskpipimp aspqkghavn lldvpvpvar
      481 klsareqrdc evierliksy flivrkniqd svpkavmhfl vnhvkdtlqs elvgqlykss
      541 llddlltese dmaqrrkeaa dmlkalqgas qiiaeireth lw
//
LOCUS       NP_001424638             447 aa            linear   ROD 09-APR-2025
DEFINITION  transcriptional regulator ERG isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424638 XP_038943860
VERSION     NP_001424638.1
DBSOURCE    REFSEQ: accession NM_001437709.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943860.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.204224.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..447
                     /product="transcriptional regulator ERG isoform 7"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=50391
     Region          83..166
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          278..361
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..447
                     /gene="Erg"
                     /coded_by="NM_001437709.1:332..1675"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 mtassssdyg qtskmsprvp qqdwlsqppa rvtikmecnp sqvngsrnsp decsvtkggk
       61 mvgspdtvgm sygsymeekh mpppnmttne rrvivpadpt lwstdhvrqw lewavkeygl
      121 ldvdvllfqn idgkelckmt kddfqrltps ynadillshl hylretplph ltsddvdkal
      181 qnsprlmhar ntggaafifp ntsvypeatq rittrpdlpy epprrstwtg hshptpqska
      241 aqpspstvpk tedqrpqldp yqilgptssr lanpgsgqiq lwqfllells dssnsncitw
      301 egtngefkmt dpdevarrwg erkskpnmny dklsralryy ydknimtkvh gkryaykfdf
      361 hgiaqalqph ppesslykyp sdlpymgsyh thpqkmnfva phppalpvts ssffatpnpy
      421 wnsptggiyp ntrlpashmp shlgtyy
//
LOCUS       NP_001012164             825 aa            linear   ROD 09-APR-2025
DEFINITION  adhesion G protein-coupled receptor E5 precursor [Rattus
            norvegicus].
ACCESSION   NP_001012164 XP_341663
VERSION     NP_001012164.1
DBSOURCE    REFSEQ: accession NM_001012164.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Griffiths,M.R., Neal,J.W., Fontaine,M., Das,T. and Gasque,P.
  TITLE     Complement factor H, a marker of self protects against experimental
            autoimmune encephalomyelitis
  JOURNAL   J Immunol 182 (7), 4368-4377 (2009)
   PUBMED   19299737
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Aust,G., Steinert,M., Schutz,A., Boltze,C., Wahlbuhl,M., Hamann,J.
            and Wobus,M.
  TITLE     CD97, but not its closely related EGF-TM7 family member EMR2, is
            expressed on gastric, pancreatic, and esophageal carcinomas
  JOURNAL   Am J Clin Pathol 118 (5), 699-707 (2002)
   PUBMED   12428789
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083857.1.
            
            On Feb 11, 2005 this sequence version replaced XP_341663.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132304, SAMD00132308
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..825
                     /product="adhesion G protein-coupled receptor E5
                     precursor"
                     /note="CD97 antigen; CD97 molecule"
                     /calculated_mol_wt=88995
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2159
     Region          69..>101
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(69,72,88)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          171..202
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(171,174,190)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          220..251
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(220,223,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          488..526
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          534..797
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          537..561
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320554"
     Region          570..591
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320554"
     Region          603..625
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320554"
     Region          644..660
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320554"
     Region          680..703
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320554"
     Region          730..752
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320554"
     Region          756..781
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320554"
     CDS             1..825
                     /gene="Adgre5"
                     /gene_synonym="Cd97"
                     /coded_by="NM_001012164.1:27..2504"
                     /db_xref="GeneID:361383"
                     /db_xref="RGD:1305595"
ORIGIN      
        1 mrgvschlll vlcfvpnlsg vgtqkasgca rwcppnsece snrsckckpg fnssspdgli
       61 tnpaqscedi neciqtdnlc gpyamcmnse gsyycvcnlg ykllsgaesf tnksentcqv
      121 svlfpasvdt gmipvpssih tvptarklpe qpttvhprtq lgdsgertpk dvnectsgqn
      181 qchqsthcin kmggyscicr rgwkpapgsp ngpvntvced vdecssgqhq chssaickni
      241 pgsykcrcpp gwiaiprdkp nntvcqephf ptwtllptah sqallsfsve vqnllrdfnp
      301 atvnytiqkl ieavdkllem pmdigtqtqq vatqllsnle qslrtlaqfl pkgpftyksp
      361 sntelalmvk eqdnkdvttv hhsqawmqld wavtagakss engysvagil sspniqklla
      421 ntslnleqkr dtledlygsp vqsvtltfls ninaifltnt dteklasdvt fkfnltsvks
      481 lkareelmca ywkshdngsg swatdgcsmn dtgfchcnhl tsfavlmaqy hvqdprleli
      541 tkvglllslv clllciltfl lvkpiqssrt mvhlhlcicl flgsviflvg veneggevgl
      601 rcrlvamllh fcflaafcwm alegvelyfl vvrvfqgqgl stwhrclvgy gvpllivais
      661 aaarmdgygh atycwldfrk qgflwsfsgp vafiifcnaa ifvitvwklt kkfseinpnm
      721 kklrkarvlt itaiaqllvl gctwgfglfl fnphstwlsy iftllnclqg lflyvtlcll
      781 nkkvreeywk wacmvtgnky teftssttgt gtsqtrtlrp sesgm
//
LOCUS       NP_001101706             894 aa            linear   ROD 09-APR-2025
DEFINITION  phosphatidate phosphatase LPIN2 [Rattus norvegicus].
ACCESSION   NP_001101706 XP_001055334 XP_237521
VERSION     NP_001101706.1
DBSOURCE    REFSEQ: accession NM_001108236.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Kok,B.P.C., Dyck,J.R.B., Harris,T.E. and Brindley,D.N.
  TITLE     Differential regulation of the expressions of the PGC-1alpha splice
            variants, lipins, and PPARalpha in heart compared to liver
  JOURNAL   J Lipid Res 54 (6), 1662-1677 (2013)
   PUBMED   23505321
  REMARK    GeneRIF: novel differences in the regulation of lipins 1,2,3,
            PPARalpha, and PGC-1alpha splice variants during fasting in heart
            versus liver, even though the ultimate outcome in both tissues is
            to increase FA turnover and oxidation.
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Donkor,J., Zhang,P., Wong,S., O'Loughlin,L., Dewald,J., Kok,B.P.,
            Brindley,D.N. and Reue,K.
  TITLE     A conserved serine residue is required for the phosphatidate
            phosphatase activity but not the transcriptional coactivator
            functions of lipin-1 and lipin-2
  JOURNAL   J Biol Chem 284 (43), 29968-29978 (2009)
   PUBMED   19717560
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Grimsey,N., Han,G.S., O'Hara,L., Rochford,J.J., Carman,G.M. and
            Siniossoglou,S.
  TITLE     Temporal and spatial regulation of the phosphatidate phosphatases
            lipin 1 and 2
  JOURNAL   J Biol Chem 283 (43), 29166-29174 (2008)
   PUBMED   18694939
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Donkor,J., Sariahmetoglu,M., Dewald,J., Brindley,D.N. and Reue,K.
  TITLE     Three mammalian lipins act as phosphatidate phosphatases with
            distinct tissue expression patterns
  JOURNAL   J Biol Chem 282 (6), 3450-3457 (2007)
   PUBMED   17158099
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474043.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001055334.1, XP_237521.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132264,
                              SAMD00132295 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..894
                     /product="phosphatidate phosphatase LPIN2"
                     /EC_number="3.1.3.4"
                     /calculated_mol_wt=99578
     Region          1..107
                     /region_name="Lipin_N"
                     /note="lipin, N-terminal conserved region; pfam04571"
                     /db_xref="CDD:461356"
     Region          <326..483
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          467..559
                     /region_name="Lipin_mid"
                     /note="Lipin/Ned1/Smp2 multi-domain protein middle domain;
                     pfam16876"
                     /db_xref="CDD:465292"
     Region          635..860
                     /region_name="LNS2"
                     /note="LNS2 (Lipin/Ned1/Smp2); pfam08235"
                     /db_xref="CDD:462403"
     Region          873..>891
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     CDS             1..894
                     /gene="Lpin2"
                     /coded_by="NM_001108236.1:95..2779"
                     /db_xref="GeneID:316737"
                     /db_xref="RGD:1304588"
ORIGIN      
        1 mnyvgqlagq vlvtvkelyk ginqatlsgc idvvvvrqqd gsyqcspfhv rfgklgvlrs
       61 kekvidiein gsavdlhmkl gdngeaffve eteeeyeklp aylatspipt edqffkhidp
      121 plvkssgner ppqssdvsht leseavftps svkkkkrrrk kckqdnrkee qaaspvaedv
      181 gdvavssdde kraqaargss naslkeedyk epppfhsgdn yplsdgdwsp letsypqtvc
      241 pksdselevk psesllrses hmewtwggfp estkvskrer ydyhprtati tpsenthfrv
      301 ipsedslire vekdatvedt tctivkpkpr alckqlsdaa stelpesple apqisstlda
      361 dpvpspsaea psepkpaakv dsptkrkgvh krsqhqgpdd iylddlkale pevaalyfpk
      421 sdtdpgsrqw pesdtfsgsq spqsvgsaaa dsgteclsds amdlpdvtls lcgglsenge
      481 iskekfmehi ityhefaenp glidnpnlvi riynryynwa laapmilslq vfqkslpkat
      541 veswvkdkmp kksgrwwfwr kkesmtkqlp etkegksevp pandlpsgte epvsarpaen
      601 dtssdegsqe leetikvdpi smetlshcgt asykkslrls sdqiaklklh dgpndvvfsi
      661 ttqyqgtcrc agtiylwnwn dkviisdidg titksdalgq ilpqlgkdwt hqgiarlyhs
      721 inengykfly csaraigmad mtrgylhwvn dkgtilprgp lmlspsslfs afhreviekk
      781 pekfkiecln diknlfapsr qpfyaafgnr pndvyaytqv gvpdcriftv npkgeliqer
      841 tkgnkssyhr lselvehvfp llnkeqnsaf pcpefssfcy wrdpipdvdl ddla
//
LOCUS       NP_001424563            1292 aa            linear   ROD 09-APR-2025
DEFINITION  receptor tyrosine-protein kinase erbB-4 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424563 XP_038940078
VERSION     NP_001424563.1
DBSOURCE    REFSEQ: accession NM_001437634.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1292)
  AUTHORS   Zhang,S., Hu,S., Dong,W., Huang,S., Jiao,Z., Hu,Z., Dai,S., Yi,Y.,
            Gong,X., Li,K., Wang,H. and Xu,D.
  TITLE     Prenatal dexamethasone exposure induces anxiety- and
            depressive-like behavior of male offspring rats through
            intrauterine programming of the activation of NRG1-ErbB4 signaling
            in hippocampal PV interneurons
  JOURNAL   Cell Biol Toxicol 39 (3), 657-678 (2023)
   PUBMED   34189720
REFERENCE   2  (residues 1 to 1292)
  AUTHORS   Yuan,J., Xu,B., Ma,J., Pang,X., Fu,Y., Liang,M., Wang,M., Pan,Y.,
            Duan,Y., Tang,M., Zhu,B., Laher,I. and Li,S.
  TITLE     MOTS-c and aerobic exercise induce cardiac physiological adaptation
            via NRG1/ErbB4/CEBPbeta modification in rats
  JOURNAL   Life Sci 315, 121330 (2023)
   PUBMED   36584915
  REMARK    GeneRIF: MOTS-c and aerobic exercise induce cardiac physiological
            adaptation via NRG1/ErbB4/CEBPbeta modification in rats.
REFERENCE   3  (residues 1 to 1292)
  AUTHORS   Li,S., Wang,M., Ma,J., Pang,X., Yuan,J., Pan,Y., Fu,Y. and Laher,I.
  TITLE     MOTS-c and Exercise Restore Cardiac Function by Activating of
            NRG1-ErbB Signaling in Diabetic Rats
  JOURNAL   Front Endocrinol (Lausanne) 13, 812032 (2022)
   PUBMED   35370955
  REMARK    GeneRIF: MOTS-c and Exercise Restore Cardiac Function by Activating
            of NRG1-ErbB Signaling in Diabetic Rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1292)
  AUTHORS   Xu,L., Li,Z., Rong,J. and Lang,L.
  TITLE     Effect of regulation of the NRG1/ErbB4 signaling pathway on the
            visual cortex synaptic plasticity of amblyopic adult rats
  JOURNAL   J Biochem Mol Toxicol 35 (9), e22841 (2021)
   PUBMED   34273906
  REMARK    GeneRIF: Effect of regulation of the NRG1/ErbB4 signaling pathway
            on the visual cortex synaptic plasticity of amblyopic adult rats.
REFERENCE   5  (residues 1 to 1292)
  AUTHORS   Chen,J.L., Zhou,X., Ding,H.L., Zhan,H.L., Yang,F., Li,W.B.,
            Xie,J.C., Liu,X.G., Xu,Y.C., Su,M.Z., Liu,B.L. and Zhou,X.F.
  TITLE     Neuregulin-1-ErbB signaling promotes microglia activation
            contributing to mechanical allodynia of cyclophosphamide-induced
            cystitis
  JOURNAL   Neurourol Urodyn 38 (5), 1250-1260 (2019)
   PUBMED   30989724
REFERENCE   6  (residues 1 to 1292)
  AUTHORS   Carroll,S.L., Miller,M.L., Frohnert,P.W., Kim,S.S. and Corbett,J.A.
  TITLE     Expression of neuregulins and their putative receptors, ErbB2 and
            ErbB3, is induced during Wallerian degeneration
  JOURNAL   J Neurosci 17 (5), 1642-1659 (1997)
   PUBMED   9030624
REFERENCE   7  (residues 1 to 1292)
  AUTHORS   Riese,D.J., Kim,E.D., Elenius,K., Buckley,S., Klagsbrun,M.,
            Plowman,G.D. and Stern,D.F.
  TITLE     The epidermal growth factor receptor couples transforming growth
            factor-alpha, heparin-binding epidermal growth factor-like factor,
            and amphiregulin to Neu, ErbB-3, and ErbB-4
  JOURNAL   J Biol Chem 271 (33), 20047-20052 (1996)
   PUBMED   8702723
REFERENCE   8  (residues 1 to 1292)
  AUTHORS   Cohen,B.D., Green,J.M., Foy,L. and Fell,H.P.
  TITLE     HER4-mediated biological and biochemical properties in NIH 3T3
            cells. Evidence for HER1-HER4 heterodimers
  JOURNAL   J Biol Chem 271 (9), 4813-4818 (1996)
   PUBMED   8617750
REFERENCE   9  (residues 1 to 1292)
  AUTHORS   Gassmann,M., Casagranda,F., Orioli,D., Simon,H., Lai,C., Klein,R.
            and Lemke,G.
  TITLE     Aberrant neural and cardiac development in mice lacking the ErbB4
            neuregulin receptor
  JOURNAL   Nature 378 (6555), 390-394 (1995)
   PUBMED   7477376
REFERENCE   10 (residues 1 to 1292)
  AUTHORS   Lai,C. and Lemke,G.
  TITLE     An extended family of protein-tyrosine kinase genes differentially
            expressed in the vertebrate nervous system
  JOURNAL   Neuron 6 (5), 691-704 (1991)
   PUBMED   2025425
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 7, 2025 this sequence version replaced XP_038940078.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY375307.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1292
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32-q33"
     Protein         1..1292
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     1 precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-4; c-erbB-4;
                     proto-oncogene-like protein c-ErbB-4; receptor tyrosine
                     kinase; v-erb-a erythroblastic leukemia viral oncogene
                     homolog 4; v-erb-b2 avian erythroblastic leukemia viral
                     oncogene 4"
                     /calculated_mol_wt=142768
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2643
     Region          55..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          186..332
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          358..478
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          502..634
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          642..685
                     /region_name="TM_ErbB4"
                     /note="Transmembrane domain of ErbB4, a Protein Tyrosine
                     Kinase; cd12092"
                     /db_xref="CDD:213053"
     Site            order(642..643,645..648,651..652,655..656,659..660,
                     663..664,667,671)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213053"
     Site            652..675
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          676..684
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          710..1012
                     /region_name="PTKc_HER4"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     HER4; cd05110"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861,882..886,891,895)
                     /site_type="active"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173655"
     Site            860..885
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173655"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            order(882..886,891,895)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173655"
     Region          1032..1035
                     /region_name="PPxy motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1186
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1226
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Site            1268
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15303; propagated from
                     UniProtKB/Swiss-Prot (Q62956.3)"
     Region          1282..1285
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     Region          1290..1292
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62956.3)"
     CDS             1..1292
                     /gene="Erbb4"
                     /coded_by="NM_001437634.1:793..4671"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:59323"
                     /db_xref="RGD:620486"
ORIGIN      
        1 mklatglwvw gsllvaartv qpsasqsvca gtenklssls dleqqyralr kyyencevvm
       61 gnleitsieh nrdlsflrsi revtgyvlva lnqfrylple nlriirgtkl yedryalaif
      121 lnyrkdgnfg lqelglknlt eilnggvyvd qnkflcyadt ihwqdivrnp wpsnmtlvst
      181 igssgcgrch ksctgrcwgp tenhcqtltr tvcaeqcdgr cygpyvsdcc hrecaggcsg
      241 pkdtdcfacm nfndsgacvt qcpqtfvynp ttfqlehnfn akytygafcv kkcphnfvvd
      301 ssscvracps skmeveengi kmckpctdic pkacdgigtg slmsaqtvds snidkfinct
      361 kingnliflv tgihgdpyna idaidpekln vfrtvreitg flniqswppn mtdfsvfsnl
      421 vtiggrvlys glsllilkqq gitslqfqsl keisagniyi tdnsnlcyyh tinwttlfst
      481 vnqrivirdn rraenctaeg mvcnhlcsnd gcwgpgpdqc lscrrfsrgk iciescnlyd
      541 gefrefengs icvecdsqce kmedglltch gpgpdnctkc shfkdgpncv ekcpdglqga
      601 nsfifkyadq drechpchpn ctqgcngpts hdciyypwtg hstlpqhart pliaagvigg
      661 lfilvimalt favyvrrksi kkkralrrfl etelvepltp sgtapnqaql rilketelkr
      721 vkvlgsgafg tvykgiwvpe getvkipvai kilnettgpk anvefmdeal imasvdhphl
      781 vrllgvclsp tiqlvtqlmp hgclleyvhe hkdnigsqll lnwcvqiakg mmyleerrlv
      841 hrdlaarnvl vkspnhvkit dfglarlleg dekeynadgg kmpikwmale cihyrkfthq
      901 sdvwsygvti welmtfggkp ydgiptreip dllekgerlp qppictidvy mvmvkcwmid
      961 adsrpkfkel aaefsrmard pqrylviqgd drmklpspnd skffqnllde edledmmdae
     1021 eylvpqafni pppiytsrtr idsnrnqfvy qdggfatqqg mpmpyratts tipeapvaqg
     1081 ataemfddsc cngtlrkpvv phvqedsstq rysadptvfa pernpraeld eegymtpmhd
     1141 kpkqeylnpv eenpfvsrrk ngdlqaldnp eyhsassgpp kaedeyvnep lylntftnal
     1201 gnaeymknsl lsvpekakka fdnpdywnhs lpprstlqhp dylqeystky fykqngrirp
     1261 ivaenpeyls efslkpgtml ppppyrhrnt vv
//
LOCUS       NP_001102769             153 aa            linear   ROD 09-APR-2025
DEFINITION  transmembrane inner ear expressed protein [Rattus norvegicus].
ACCESSION   NP_001102769 XP_001076090 XP_576477
VERSION     NP_001102769.1
DBSOURCE    REFSEQ: accession NM_001109299.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Shin,M.J., Lee,J.H., Yu,D.H., Kim,H.J., Bae,K.B., Yuh,H.S.,
            Kim,M.O., Hyun,B.H., Lee,S., Park,R. and Ryoo,Z.Y.
  TITLE     Spatiotemporal expression of tmie in the inner ear of rats during
            postnatal development
  JOURNAL   Comp Med 60 (4), 288-294 (2010)
   PUBMED   20819378
  REMARK    GeneRIF: Tmie exists in the cytoplasm and may have a key role in
            the maturation and structure of stereocilia bundles in developing
            hair cells. After hair cell maturation, Tmie is thought to be
            involved in the maintenance of organ of Corti cells.
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Su,M.C., Yang,J.J., Chou,M.Y., Hsin,C.H., Su,C.C. and Li,S.Y.
  TITLE     Expression and localization of Tmie in adult rat cochlea
  JOURNAL   Histochem Cell Biol 130 (1), 119-126 (2008)
   PUBMED   18327602
  REMARK    GeneRIF: Our results point out the presence and localization of
            Tmie products in the cochlea of rat.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Naz,S., Giguere,C.M., Kohrman,D.C., Mitchem,K.L., Riazuddin,S.,
            Morell,R.J., Ramesh,A., Srisailpathy,S., Deshmukh,D., Riazuddin,S.,
            Griffith,A.J., Friedman,T.B., Smith,R.J. and Wilcox,E.R.
  TITLE     Mutations in a novel gene, TMIE, are associated with hearing loss
            linked to the DFNB6 locus
  JOURNAL   Am J Hum Genet 71 (3), 632-636 (2002)
   PUBMED   12145746
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Mitchem,K.L., Hibbard,E., Beyer,L.A., Bosom,K., Dootz,G.A.,
            Dolan,D.F., Johnson,K.R., Raphael,Y. and Kohrman,D.C.
  TITLE     Mutation of the novel gene Tmie results in sensory cell defects in
            the inner ear of spinner, a mouse model of human hearing loss DFNB6
  JOURNAL   Hum Mol Genet 11 (16), 1887-1898 (2002)
   PUBMED   12140191
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473954.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_576477.1, XP_001076090.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760389, SAMN06680413
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..153
                     /product="transmembrane inner ear expressed protein"
                     /calculated_mol_wt=16901
     Region          47..132
                     /region_name="TMIE"
                     /note="TMIE protein; pfam16038"
                     /db_xref="CDD:464987"
     CDS             1..153
                     /gene="Tmie"
                     /gene_synonym="RGD1562523"
                     /coded_by="NM_001109299.1:1312..1773"
                     /db_xref="GeneID:501061"
                     /db_xref="RGD:1562523"
ORIGIN      
        1 magrqrgsgr lwalggaalg aclagvasql vepstappkp kpppltketv vfwdmrlwhv
       61 vgifslfvls iiitlccvfn crvprtrkei earylqrkaa kmytdkletv pplnelteip
      121 gedkkkkkkd svdtvaikve edekneakkk gek
//
LOCUS       NP_001178873            1219 aa            linear   ROD 09-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 18
            precursor [Rattus norvegicus].
ACCESSION   NP_001178873 XP_574244
VERSION     NP_001178873.1
DBSOURCE    REFSEQ: accession NM_001191944.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1219)
  AUTHORS   Xu,B., Zhang,J.E., Ye,L. and Yuan,C.W.
  TITLE     The progression of obstructive renal fibrosis in rats is regulated
            by ADAMTS18 gene methylation in the embryonic kidney through the
            AKT/Notch pathway
  JOURNAL   J Biochem Mol Toxicol 38 (1), e23628 (2024)
   PUBMED   38229317
  REMARK    GeneRIF: The progression of obstructive renal fibrosis in rats is
            regulated by ADAMTS18 gene methylation in the embryonic kidney
            through the AKT/Notch pathway.
REFERENCE   2  (residues 1 to 1219)
  AUTHORS   Aldahmesh,M.A., Alshammari,M.J., Khan,A.O., Mohamed,J.Y.,
            Alhabib,F.A. and Alkuraya,F.S.
  TITLE     The syndrome of microcornea, myopic chorioretinal atrophy, and
            telecanthus (MMCAT) is caused by mutations in ADAMTS18
  JOURNAL   Hum Mutat 34 (9), 1195-1199 (2013)
   PUBMED   23818446
REFERENCE   3  (residues 1 to 1219)
  AUTHORS   Li,Z., Nardi,M.A., Li,Y.S., Zhang,W., Pan,R., Dang,S., Yee,H.,
            Quartermain,D., Jonas,S. and Karpatkin,S.
  TITLE     C-terminal ADAMTS-18 fragment induces oxidative platelet
            fragmentation, dissolves platelet aggregates, and protects against
            carotid artery occlusion and cerebral stroke
  JOURNAL   Blood 113 (24), 6051-6060 (2009)
   PUBMED   19218546
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 17, 2010 this sequence version replaced XP_574244.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.76587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1219
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..1219
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 18 precursor"
                     /note="a disintegrin-like and metallopeptidase (reprolysin
                     type) with thrombospondin type 1 motif, 18; A disintegrin
                     and metalloproteinase with thrombospondin motifs 18"
                     /calculated_mol_wt=130790
     sig_peptide     1..47
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4686
     Region          65..204
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          294..495
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(437..438,441,447)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          512..579
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Region          593..645
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          649..749
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Region          751..862
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Region          884..932
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          936..992
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          996..1049
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1057..1116
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1125..1171
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          1186..1216
                     /region_name="PLAC"
                     /note="PLAC (protease and lacunin) domain; pfam08686"
                     /db_xref="CDD:462560"
     CDS             1..1219
                     /gene="Adamts18"
                     /gene_synonym="RGD1560118"
                     /coded_by="NM_001191944.1:1..3660"
                     /db_xref="GeneID:361412"
                     /db_xref="RGD:1560118"
ORIGIN      
        1 mecallflca lraagpgppw gpaglarlak alqlcclcca svavalasds gssggsglnd
       61 dyvfvvpvev dsggsyishd ilhnrkrrsa hgasssvhyr fsafgqdlhl elkpsallss
      121 hfivqvlgkd gasetrepav vqqclyqgfi rndslssvav stcaglsgli rtrdneflis
      181 plpqllaqqh nyslpaghhp hvlykrtaek rvrryqdypa sqrtypghsp shtppasqsq
      241 eteyrhrrwq kqhfcgrrkk yapkppaeda ylrfdeygga grprrsarks qkglnvetlv
      301 vadakmvekh gkddvttyil tvmnmvsslf kdgtigsdin ivvvslille depggllinh
      361 hadqslnsfc qwqsalvgkn gkrhdhaill tgfdicswkn epcdtlgfap isgmcskyrs
      421 ctinedtglg laftiahesg hnfgmvhdge gnpcrkaegn imsptltgnn gvfswsscsr
      481 qylkkflstp qagclvdepk qtgqykypdk lpgqiydadt qckwqfgaka klcslgvmkd
      541 ickslwchrv ghrcetkfmp aaegtvcgls mwcrqgqcvr lgdlgprpih gqwsawskws
      601 ecsrtcgggv kyqerhcsnp kpqyggkycp gssriyklcn inpchensld fraqqcaeyn
      661 nkpfrgwlyr wrpytkveee drcklyckae nfefffamsg kvkdgtpcsp hrndvcidgi
      721 cepvgcdhel gskavsdacg vckgdnstck fykglylsqh kaneyypvvt ipagarsiei
      781 qelelsssyl avrslsqkyy ltggwnidwp gdftfagttf eyqrpfnrpe rlyapgptne
      841 tlvfeiltqg knpgitwkya lpkvmnvtqp aakrhhhtwr tvqsdcsvtc gggyisikai
      901 clrdqntqvn ssfcsvrtkp atepklcnaf scpaywlpge wstcskscag gqqsrkircv
      961 qkkpfqkeea vlhslcpvst ptqvqvcnsh acppewspgp wsqcsktcgr gvrrrevlct
     1021 spaaetlpes lcssspkpea qegcvlgrcp knnrlqwias awtecsatcg lgvrkrefkc
     1081 mektlqgklm tfperrcrni kkpnleleet cnrracpvys maagwysspw qqctvtcggg
     1141 vqtrsvhcmq qgrpssscll hqkppvlrac ntnfcpvpek rddpscvdff swcrlvpqhg
     1201 vcnhkfygkq ccrscsrks
//
LOCUS       NP_001424557             395 aa            linear   ROD 09-APR-2025
DEFINITION  carbohydrate sulfotransferase 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424557 XP_006255694
VERSION     NP_001424557.1
DBSOURCE    REFSEQ: accession NM_001437628.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Akama,T.O., Misra,A.K., Hindsgaul,O. and Fukuda,M.N.
  TITLE     Enzymatic synthesis in vitro of the disulfated disaccharide unit of
            corneal keratan sulfate
  JOURNAL   J Biol Chem 277 (45), 42505-42513 (2002)
   PUBMED   12218059
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Akama,T.O., Nakayama,J., Nishida,K., Hiraoka,N., Suzuki,M.,
            McAuliffe,J., Hindsgaul,O., Fukuda,M. and Fukuda,M.N.
  TITLE     Human corneal GlcNac 6-O-sulfotransferase and mouse intestinal
            GlcNac 6-O-sulfotransferase both produce keratan sulfate
  JOURNAL   J Biol Chem 276 (19), 16271-16278 (2001)
   PUBMED   11278593
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Bartes,A., Bhakta,S. and Hemmerich,S.
  TITLE     Sulfation of endothelial mucin by corneal keratan
            N-acetylglucosamine 6-O-sulfotransferase (GST-4beta)
  JOURNAL   Biochem Biophys Res Commun 282 (4), 928-933 (2001)
   PUBMED   11352640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Apr 7, 2025 this sequence version replaced XP_006255694.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212819.1, SRR26643298.76541.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..395
                     /product="carbohydrate sulfotransferase 5 isoform 2"
                     /note="carbohydrate (N-acetylglucosamine 6-O)
                     sulfotransferase 5; carbohydrate sulfotransferase 5"
                     /calculated_mol_wt=44419
     Region          159..357
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; cl21551"
                     /db_xref="CDD:473908"
     CDS             1..395
                     /gene="Chst6"
                     /gene_synonym="Chst5; RGD1561144"
                     /coded_by="NM_001437628.1:431..1618"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307859"
                     /db_xref="RGD:1561144"
ORIGIN      
        1 mrlprfsstv vlsllivqtg ilvflvsrqm psspagrgeh vhvlvlsswr sgssfvgqlf
       61 sqhpdvfylm epawhvwdal sqasapalhm avrdlirsvf lcdmdvfday lpwrrnisdl
      121 fqwavsralc sppvcdafar gnisseevck plcatrpfgl aqeacssysh vvlkevrffn
      181 lqvlypllsd palnlrivhl vrdpravlrs reqtakalar dngivlgtng twveadprlr
      241 vvsevcrshv riaevalhkp ppflqdryrl vryedlardp ltvirelyaf tglgltpqlq
      301 twiynithgs gpgarreafk ttsrdalsvs qawrhtlpfa kirrvqelca galqllgyrp
      361 vhseleqrdl sldlllprgm dsfkwasstd kqpes
//
LOCUS       NP_001424578            1078 aa            linear   ROD 09-APR-2025
DEFINITION  BRD4-interacting chromatin-remodeling complex-associated
            protein-like [Rattus norvegicus].
ACCESSION   NP_001424578 XP_038939105
VERSION     NP_001424578.1
DBSOURCE    REFSEQ: accession NM_001437649.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Alpsoy,A. and Dykhuizen,E.C.
  TITLE     Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its
            paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes
  JOURNAL   J Biol Chem 293 (11), 3892-3903 (2018)
   PUBMED   29374058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 7, 2025 this sequence version replaced XP_038939105.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26643429.33054.1, SRR26643292.36732.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..1078
                     /product="BRD4-interacting chromatin-remodeling
                     complex-associated protein-like"
                     /note="GLTSCR1-like; BRD4 interacting chromatin remodeling
                     complex associated protein like; BRD4 interacting
                     chromatin remodelling complex associated protein like"
                     /calculated_mol_wt=114332
     Region          498..>670
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          712..812
                     /region_name="GLTSCR1"
                     /note="Conserved region of unknown function on GLTSCR
                     protein; pfam15249"
                     /db_xref="CDD:464589"
     CDS             1..1078
                     /gene="Bicral"
                     /gene_synonym="Gltscr1l; RGD1305680"
                     /coded_by="NM_001437649.1:427..3663"
                     /db_xref="GeneID:301235"
                     /db_xref="RGD:1305680"
ORIGIN      
        1 mdddddscll dligdpqaln yflhgpssks sgddvtnagy saansnsifa nstnadpkss
       61 lkgvsnqlge gpsdglplas slqfledele ssplpdlsed qpfdilqksl qeaniteqtl
      121 aeeayldasi gssqqfaqaq lhpsssasft qasnvsnysg qtlqpigvth vpvgasfasn
      181 tvgvqhgfmq hvgisvpsqh lpnssqisgs gqiqligsfg nqpsmmtinn ldgsqiilkg
      241 sgqqapssvs ggllvhrqtp ngnslfgnpt sspgaqpvtv pfnstnfqas lpvhniiiqr
      301 glapnsnkvp iniqpkpiqm gqqstynvns lglqqhhvqq gisfasassp qgsvvgphms
      361 vnivnqqnar kpvtsqavss aggsivihsp mgqphtpqsq fliptslsvs snsvhhvqti
      421 ngqlvqtqps qlisgqvase hvmlnrnssn mlrtnqpyag qmlnnqsaav qlvsgqtfat
      481 sgspvivnha spqivggqmp lqqasptvlh lspgqssvsq grpgfatmas vssmsgparf
      541 pavssastah ptlgpavqsg asgsnftgdq ltqanrtpvp vsvshrlpvs askspstlss
      601 tpgtqqqffc qapkkclnqt apiptpipts kttdslrqpq ipgllstalp gqdcgskimp
      661 aplgttqpqq ensvgsspsq tavqvdshsg qkrpaakqlt kgafilqqlq rdqahavtpd
      721 ksqfrsltdt vqrllsyhvc qgsmpteedl skvdsefeev atqllkrtha mlnkyrslll
      781 edamrinpsa emvmidrmfn qeeraslsrd krlalvdpeg fqadfccsfk ldeaapetpl
      841 drsdqhrskt sslhqvpraq srdrakpgva eatnhdqfhl vpnhivvsae gniskksegh
      901 srtlkfdkgv lgqyrgpped kggrrdpaka sgcspgpegh rktlprpdhg sesklpgila
      961 sshmempcld sfqdkalrns pknevlhtdi mkgsgepqpd lqltkslekt fknilelkna
     1021 grpqndpaas gavdldfpsf spmasqencl ekfipdhseg vvetdsilea avnsilec
//
LOCUS       NP_001100355             226 aa            linear   ROD 09-APR-2025
DEFINITION  triggering receptor expressed on myeloid cells 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001100355 XP_001063859 XP_038939102 XP_217336
VERSION     NP_001100355.2
DBSOURCE    REFSEQ: accession NM_001106885.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Sun,X.G., Zhang,M.M., Liu,S.Y., Chu,X.H., Xue,G.Q., Zhang,B.C.,
            Zhu,J.B., Godje Godje,I.S., Zhu,L.J., Hu,H.Y., Hai-Wang, Shen,Y.J.
            and Wang,G.Q.
  TITLE     Role of TREM-1 in the development of early brain injury after
            subarachnoid hemorrhage
  JOURNAL   Exp Neurol 341, 113692 (2021)
   PUBMED   33727099
  REMARK    GeneRIF: Role of TREM-1 in the development of early brain injury
            after subarachnoid hemorrhage.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Liang,Y.B., Song,P.P., Zhu,Y.H., Xu,J.M., Zhu,P.Z., Liu,R.R. and
            Zhang,Y.S.
  TITLE     TREM-1-targeting LP17 attenuates cerebral ischemia-induced neuronal
            injury by inhibiting oxidative stress and pyroptosis
  JOURNAL   Biochem Biophys Res Commun 529 (3), 554-561 (2020)
   PUBMED   32736673
  REMARK    Erratum:[Biochem Biophys Res Commun. 2023 Oct 1;675:184-186. doi:
            10.1016/j.bbrc.2023.07.016. PMID: 37516577]
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Fang,K., Li,H.R., Chen,X.X., Gao,X.R., Huang,L.L., Du,A.Q.,
            Jiang,C., Li,H. and Ge,J.F.
  TITLE     Quercetin Alleviates LPS-Induced Depression-Like Behavior in Rats
            via Regulating BDNF-Related Imbalance of Copine 6 and TREM1/2 in
            the Hippocampus and PFC
  JOURNAL   Front Pharmacol 10, 1544 (2020)
   PUBMED   32009956
  REMARK    Erratum:[Front Pharmacol. 2020 Apr 15;11:518. doi:
            10.3389/fphar.2020.00518. PMID: 32351394]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Gorlier,C., Sellam,J., Laurans,L., Simon,T., Giurgea,I.,
            Bastard,J.P., Fellahi,S., Deshayes,S., Grateau,G., Ait Oufella,H.
            and Georgin-Lavialle,S.
  TITLE     In familial Mediterranean fever, soluble TREM-1 plasma level is
            higher in case of amyloidosis
  JOURNAL   Innate Immun 25 (8), 487-490 (2019)
   PUBMED   31474164
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Zhu,H., Li,W., Wang,Z., Chen,J., Ding,M. and Han,L.
  TITLE     TREM-1 deficiency attenuates the inflammatory responses in
            LPS-induced murine endometritis
  JOURNAL   Microb Biotechnol 12 (6), 1337-1345 (2019)
   PUBMED   31365951
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Gibot,S., Massin,F., Marcou,M., Taylor,V., Stidwill,R., Wilson,P.,
            Singer,M. and Bellingan,G.
  TITLE     TREM-1 promotes survival during septic shock in mice
  JOURNAL   Eur J Immunol 37 (2), 456-466 (2007)
   PUBMED   17230441
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Gibot,S., Alauzet,C., Massin,F., Sennoune,N., Faure,G.C.,
            Bene,M.C., Lozniewski,A., Bollaert,P.E. and Levy,B.
  TITLE     Modulation of the triggering receptor expressed on myeloid cells-1
            pathway during pneumonia in rats
  JOURNAL   J Infect Dis 194 (7), 975-983 (2006)
   PUBMED   16960786
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Determann,R.M., Weisfelt,M., de Gans,J., van der Ende,A.,
            Schultz,M.J. and van de Beek,D.
  TITLE     Soluble triggering receptor expressed on myeloid cells 1: a
            biomarker for bacterial meningitis
  JOURNAL   Intensive Care Med 32 (8), 1243-1247 (2006)
   PUBMED   16786330
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Knapp,S., Gibot,S., de Vos,A., Versteeg,H.H., Colonna,M. and van
            der Poll,T.
  TITLE     Cutting edge: expression patterns of surface and soluble triggering
            receptor expressed on myeloid cells-1 in human endotoxemia
  JOURNAL   J Immunol 173 (12), 7131-7134 (2004)
   PUBMED   15585833
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Bouchon,A., Hernandez-Munain,C., Cella,M. and Colonna,M.
  TITLE     A DAP12-mediated pathway regulates expression of CC chemokine
            receptor 7 and maturation of human dendritic cells
  JOURNAL   J Exp Med 194 (8), 1111-1122 (2001)
   PUBMED   11602640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_038939102.1, NP_001100355.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.31735.1,
                                           SRR26643284.12054.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676806 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..226
                     /product="triggering receptor expressed on myeloid cells 1
                     precursor"
                     /calculated_mol_wt=22564
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2265
     Region          24..132
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          126..129
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..226
                     /gene="Trem1"
                     /coded_by="NM_001106885.2:30..710"
                     /db_xref="GeneID:301229"
                     /db_xref="RGD:1309467"
ORIGIN      
        1 mrkaglwgll lvffvsevka aivpeeeryd lvegqtltvn cpfnimkyar srkawqrlsa
       61 gkepltlvvt erssttssev rvgkytlkdd pteamlfvqm tdlqvtdsgl yrcviyhppn
      121 dpvllfhpvr lvvtkgssgv svpdiipttk ptevpvlitt khstptrslp kstavvsspd
      181 pgvtinngtd ptsvstynvv vpvvcgllik tliffvlfvv tkrsfg
//
LOCUS       NP_001424729             210 aa            linear   ROD 10-APR-2025
DEFINITION  regulator of G-protein signaling 17 [Rattus norvegicus].
ACCESSION   NP_001424729 XP_006227917
VERSION     NP_001424729.1
DBSOURCE    REFSEQ: accession NM_001437800.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Dhukhwa,A., Al Aameri,R.F.H., Sheth,S., Mukherjea,D., Rybak,L. and
            Ramkumar,V.
  TITLE     Regulator of G protein signaling 17 represents a novel target for
            treating cisplatin induced hearing loss
  JOURNAL   Sci Rep 11 (1), 8116 (2021)
   PUBMED   33854102
  REMARK    GeneRIF: Regulator of G protein signaling 17 represents a novel
            target for treating cisplatin induced hearing loss.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Sun,H., Calipari,E.S., Beveridge,T.J., Jones,S.R. and Chen,R.
  TITLE     The brain gene expression profile of dopamine D2/D3 receptors and
            associated signaling proteins following amphetamine
            self-administration
  JOURNAL   Neuroscience 307, 253-261 (2015)
   PUBMED   26321241
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Sokolov,E., Iannitti,D.A., Schrum,L.W. and McKillop,I.H.
  TITLE     Altered expression and function of regulator of G-protein
            signaling-17 (RGS17) in hepatocellular carcinoma
  JOURNAL   Cell Signal 23 (10), 1603-1610 (2011)
   PUBMED   21620966
  REMARK    GeneRIF: RGS17 is differentially expressed in hepatocellular
            carcinoma cells and plays a central role in regulating transformed
            hepatocyte tumorgenicity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006227917.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.716.1,
                                           SRR26360176.2074377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840109, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..210
                     /product="regulator of G-protein signaling 17"
                     /calculated_mol_wt=24189
     Region          41..197
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     CDS             1..210
                     /gene="Rgs17"
                     /coded_by="NM_001437800.1:275..907"
                     /db_xref="GeneID:308118"
                     /db_xref="RGD:1305515"
ORIGIN      
        1 mrkrqqsqne gtqavsqapg nqrpnntccf cwccccscsc ltvrneergd ssgrpphttk
       61 mesiqvleec qnptadevls wsqnfdkmmk apagrnlfre flrteyseen llfwlacedl
      121 kkeqnkkave ekarmiyedy isilspkevs ldsrvrevin rnllepsphm yedaqlqiyt
      181 lmhrdsfprf lnsqiykafv estasstses
//
LOCUS       NP_001424768             499 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424768 XP_063137352
VERSION     NP_001424768.1
DBSOURCE    REFSEQ: accession NM_001437839.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063137352.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1901771.1,
                                           SRR26360194.2086800.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..499
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 8"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=56316
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..499
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437839.1:417..1916"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkes tessnttied edvkarkqei ikvteqliea
      361 inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe nalpkinkpi htiilnphvh
      421 lvgddaacia yirltqymdg ngmpktmqse etrvwhrrdg kwqnihfhrs gsptvpikpp
      481 cipngkenfs ggtslwqni
//
LOCUS       NP_068631                467 aa            linear   ROD 10-APR-2025
DEFINITION  megakaryocyte-associated tyrosine-protein kinase isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_068631
VERSION     NP_068631.1
DBSOURCE    REFSEQ: accession NM_021859.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gunn,N.J., Gorman,M.A., Dobson,R.C., Parker,M.W. and Mulhern,T.D.
  TITLE     Purification, crystallization, small-angle X-ray scattering and
            preliminary X-ray diffraction analysis of the SH2 domain of the
            Csk-homologous kinase
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 336-339
            (2011)
   PUBMED   21393838
  REMARK    GeneRIF: The CHK SH2 was expressed in Escherichia coli and the
            purified protein was characterized as monomeric by synchrotron
            small-angle X-ray scattering in-line with size-exclusion
            chromatography.
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Kuo,S.S., Moran,P., Gripp,J., Armanini,M., Phillips,H.S.,
            Goddard,A. and Caras,I.W.
  TITLE     Identification and characterization of Batk, a predominantly
            brain-specific non-receptor protein tyrosine kinase related to Csk
  JOURNAL   J Neurosci Res 38 (6), 705-715 (1994)
   PUBMED   7807586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087726.1, SRR26643298.37823.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840109 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..467
                     /product="megakaryocyte-associated tyrosine-protein kinase
                     isoform 1"
                     /EC_number="2.7.10.2"
                     /note="megakaryocyte-associated tyrosine-protein kinase;
                     protein kinase BATK; tyrosine-protein kinase CTK;
                     megakaryocyte-associated tyrosine kinase (non-receptor
                     protein tyrosine kinase); non-receptor protein kinase
                     protein"
                     /calculated_mol_wt=51766
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     Region          9..67
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(16,18,21,25,44..45,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          77..174
                     /region_name="SH2_csk_like"
                     /note="Src homology 2 (SH2) domain found in
                     Carboxyl-Terminal Src Kinase (Csk); cd09937"
                     /db_xref="CDD:198190"
     Site            order(88,106,127,129)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198190"
     Site            order(128,155)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198190"
     Region          187..441
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(200..203,206,208,219,221,248,263..266,311,315..316,
                     318,328..329)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          445..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     CDS             1..467
                     /gene="Matk"
                     /gene_synonym="Batk"
                     /coded_by="NM_021859.3:103..1506"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:60450"
                     /db_xref="RGD:69058"
ORIGIN      
        1 mptqrwapgt qcmtkcensr pkpgelafrk gdmvtileac edkswyrakh hssgqeglla
       61 aaalrqreal stdpklslmp wfhgkisgqe aiqqlqpped glflvresar hpgdyvlcvs
      121 fgrdvihyrv lhrdghltid eavcfcnlmd mvehytrdkg aictklvkpk rkqgaksaee
      181 elakagwlld lqhltlgaqi gegefgavlq geylgqkvav knikcdvtaq afldetavmt
      241 klqhrnlvrl lgvilhhgly ivmehvskgn lvnflrtrgr alvstsqllq falhvaegme
      301 yleskklvhr dlaarnilvs edlvakvsdf glakaelrkg ldssrlpvkw tapealkngr
      361 fssksdvwsf gvllwevfsy grapypkmsl kevseavekg yrmeppdscp gpvhtlmgsc
      421 weaepsrrpp frkiveklgr elrsvgvaap aggqeaegsa ptrsqdp
//
LOCUS       NP_001424775             610 aa            linear   ROD 10-APR-2025
DEFINITION  prolactin receptor isoform a precursor [Rattus norvegicus].
ACCESSION   NP_001424775
VERSION     NP_001424775.1
DBSOURCE    REFSEQ: accession NM_001437846.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Ortiz-Perez,A., Limon-Morales,O., Rojas-Castaneda,J.C., Cerbon,M.
            and Picazo,O.
  TITLE     Prolactin prevents the kainic acid-induced neuronal loss in the rat
            hippocampus by inducing prolactin receptor and putatively
            increasing the VGLUT1 overexpression
  JOURNAL   Neurosci Lett 694, 116-123 (2019)
   PUBMED   30500398
  REMARK    GeneRIF: Study indicates that chronic prolactin administration
            before kainic acid induced damage induces hippocampal
            neuroprotection associated with prolactin receptor and VGLUT1
            overexpression.
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Vergara-Castaneda,E., Grattan,D.R., Pasantes-Morales,H.,
            Perez-Dominguez,M., Cabrera-Reyes,E.A., Morales,T. and Cerbon,M.
  TITLE     Prolactin mediates neuroprotection against excitotoxicity in
            primary cell cultures of hippocampal neurons via its receptor
  JOURNAL   Brain Res 1636, 193-199 (2016)
   PUBMED   26874070
  REMARK    GeneRIF: This study demonstrated that the Cultured neurons
            expressed mRNA for both PRL and its receptor (PRLR), and both PRL
            and PRLR expression levels changed after the excitotoxic insult.
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Rojas-Duran,F., Pascual-Mathey,L.I., Serrano,K., Aranda-Abreu,G.E.,
            Manzo,J., Soto-Cid,A.H. and Hernandez,M.E.
  TITLE     Correlation of prolactin levels and PRL-receptor expression with
            Stat and Mapk cell signaling in the prostate of long-term sexually
            active rats
  JOURNAL   Physiol Behav 138, 188-192 (2015)
   PUBMED   25446202
  REMARK    GeneRIF: Results showed that an active sexual life, with constant
            execution of sexual behavior, produces a sustained increase in
            serum PRL, prostate PRL receptors, and the pStat3 signaling pathway
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Arumugam,R., Fleenor,D. and Freemark,M.
  TITLE     Knockdown of prolactin receptors in a pancreatic beta cell line:
            effects on DNA synthesis, apoptosis, and gene expression
  JOURNAL   Endocrine 46 (3), 568-576 (2014)
   PUBMED   24114406
  REMARK    GeneRIF: PRLR signaling is required for DNA synthesis and survival
            of rat insulinoma cells
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Ali,S., Pellegrini,I. and Kelly,P.A.
  TITLE     A prolactin-dependent immune cell line (Nb2) expresses a mutant
            form of prolactin receptor
  JOURNAL   J Biol Chem 266 (30), 20110-20117 (1991)
   PUBMED   1718958
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Shirota,M., Banville,D., Ali,S., Jolicoeur,C., Boutin,J.M.,
            Edery,M., Djiane,J. and Kelly,P.A.
  TITLE     Expression of two forms of prolactin receptor in rat ovary and
            liver
  JOURNAL   Mol Endocrinol 4 (8), 1136-1143 (1990)
   PUBMED   2293022
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Zhang,R., Buczko,E., Tsai-Morris,C.H., Hu,Z.Z. and Dufau,M.L.
  TITLE     Isolation and characterization of two novel rat ovarian lactogen
            receptor cDNA species
  JOURNAL   Biochem Biophys Res Commun 168 (2), 415-422 (1990)
   PUBMED   2159291
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Boutin,J.M., Jolicoeur,C., Okamura,H., Gagnon,J., Edery,M.,
            Shirota,M., Banville,D., Dusanter-Fourt,I., Djiane,J. and
            Kelly,P.A.
  TITLE     Cloning and expression of the rat prolactin receptor, a member of
            the growth hormone/prolactin receptor gene family
  JOURNAL   Cell 53 (1), 69-77 (1988)
   PUBMED   2832068
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Herington,A.C., Harrison,D. and Graystone,J.
  TITLE     Hepatic binding of human and bovine growth hormones and ovine
            prolactin in the dwarf 'little' mouse
  JOURNAL   Endocrinology 112 (6), 2032-2038 (1983)
   PUBMED   6303755
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.8254.1,
                                           SRR26360172.275651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..610
                     /product="prolactin receptor isoform a precursor"
                     /note="PRL-R; lactogen receptor"
                     /calculated_mol_wt=66618
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2000
     Region          19..115
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     mat_peptide     20..610
                     /product="Prolactin receptor. /id=PRO_0000010981"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
                     /calculated_mol_wt=66618
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          122..219
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(122,193,208)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          210..214
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Site            order(210..211,213..214)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            230..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          262..270
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          317..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          458..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          564..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     CDS             1..610
                     /gene="Prlr"
                     /gene_synonym="RATPRLR"
                     /coded_by="NM_001437846.1:341..2173"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:24684"
                     /db_xref="RGD:3407"
ORIGIN      
        1 mpsalafvll vlnisllkgq sppgkpeihk crspdketft cwwnpgtdgg lptnysltys
       61 kegekttyec pdyktsgpns cffskqytsi wkiyiitvna tnqmgssssd plyvdvtyiv
      121 epepprnltl evkqlkdkkt ylwvkwsppt itdvktgwft meyeirlkpe eaeeweihft
      181 ghqtqfkvfd lypgqkylvq trckpdhgyw srwsqessve mpndftlkdt tvwiivails
      241 aviclimvwa valkgysmmt cifppvpgpk ikgfdthlle kgkseellsa lgcqdfppts
      301 dcedllvefl evddnederl mpshskeypg qgvkpthldp dsdsghgsyd shsllsekce
      361 epqaypptlh ipeitekpen peanipptvd pqstnpnfhv dapksstwpl lpgqhmprsp
      421 yhsvadvckl agspvntlds fldkaeenvl klskaletge eevaeqkgak sfpsdkqntp
      481 wpllqekspt vyvkppdyve ihkvnkdgvl slfpkqrenn qtekpgvpet skeyakvsgi
      541 tdnnilvlvp dsraqntall eesakkapps feadqsekdl asftatssnr rlqlgrldyl
      601 dptcfmhsfh
//
LOCUS       NP_001424761             261 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424761
VERSION     NP_001424761.1
DBSOURCE    REFSEQ: accession NM_001437832.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.733.1,
                                           SRR26360172.1815795.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..261
                     /product="sphingosine kinase 2 isoform 2"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=28380
     Region          <152..>248
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..261
                     /gene="Sphk2"
                     /coded_by="NM_001437832.1:671..1456"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggyvdc c
//
LOCUS       NP_058806                129 aa            linear   ROD 10-APR-2025
DEFINITION  cocaine- and amphetamine-regulated transcript protein isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_058806
VERSION     NP_058806.1
DBSOURCE    REFSEQ: accession NM_017110.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Casini,A., Vivacqua,G., Vaccaro,R., Renzi,A., Leone,S.,
            Pannarale,L., Franchitto,A., Onori,P., Mancinelli,R. and Gaudio,E.
  TITLE     Expression and role of cocaine-amphetamine regulated transcript
            (CART) in the proliferation of biliary epithelium
  JOURNAL   Eur J Histochem 67 (4), 3846 (2023)
   PUBMED   37859350
  REMARK    GeneRIF: Expression and role of cocaine-amphetamine regulated
            transcript (CART) in the proliferation of biliary epithelium.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Schuller,J. and Koch,M.
  TITLE     Blockade of the orexin 1-receptors and 'cocaine- and
            amphetamine-regulated transcript' in the nucleus accumbens shell
            alters impulse control in rats
  JOURNAL   Behav Brain Res 440, 114268 (2023)
   PUBMED   36539163
  REMARK    GeneRIF: Blockade of the orexin 1-receptors and 'cocaine- and
            amphetamine-regulated transcript' in the nucleus accumbens shell
            alters impulse control in rats.
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Samson,W.K., Salvemini,D. and Yosten,G.L.C.
  TITLE     Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise
  JOURNAL   Endocrinology 162 (8) (2021)
   PUBMED   34043767
  REMARK    GeneRIF: Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise.
            Review article
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Drott,C.J., Norman,D. and Espes,D.
  TITLE     CART decreases islet blood flow, but has no effect on total
            pancreatic blood flow and glucose tolerance in anesthetized rats
  JOURNAL   Peptides 135, 170431 (2021)
   PUBMED   33098940
  REMARK    GeneRIF: CART decreases islet blood flow, but has no effect on
            total pancreatic blood flow and glucose tolerance in anesthetized
            rats.
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Walker,L.C., Hand,L.J., Letherby,B., Huckstep,K.L., Campbell,E.J.
            and Lawrence,A.J.
  TITLE     Cocaine and amphetamine regulated transcript (CART) signalling in
            the central nucleus of the amygdala modulates stress-induced
            alcohol seeking
  JOURNAL   Neuropsychopharmacology 46 (2), 325-333 (2021)
   PUBMED   32826981
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Walder,K., Morris,C. and Ravussin,E.
  TITLE     A polymorphism in the gene encoding CART is not associated with
            obesity in Pima Indians
  JOURNAL   Int J Obes Relat Metab Disord 24 (4), 520-521 (2000)
   PUBMED   10805512
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Echwald,S.M., Sorensen,T.I., Andersen,T., Hansen,C., Tommerup,N.
            and Pedersen,O.
  TITLE     Sequence variants in the human cocaine and amphetamine-regulated
            transcript (CART) gene in subjects with early onset obesity
  JOURNAL   Obes Res 7 (6), 532-536 (1999)
   PUBMED   10574510
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Thim,L., Nielsen,P.F., Judge,M.E., Andersen,A.S., Diers,I.,
            Egel-Mitani,M. and Hastrup,S.
  TITLE     Purification and characterisation of a new hypothalamic satiety
            peptide, cocaine and amphetamine regulated transcript (CART),
            produced in yeast
  JOURNAL   FEBS Lett 428 (3), 263-268 (1998)
   PUBMED   9654146
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Kristensen,P., Judge,M.E., Thim,L., Ribel,U., Christjansen,K.N.,
            Wulff,B.S., Clausen,J.T., Jensen,P.B., Madsen,O.D., Vrang,N.,
            Larsen,P.J. and Hastrup,S.
  TITLE     Hypothalamic CART is a new anorectic peptide regulated by leptin
  JOURNAL   Nature 393 (6680), 72-76 (1998)
   PUBMED   9590691
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Douglass,J., McKinzie,A.A. and Couceyro,P.
  TITLE     PCR differential display identifies a rat brain mRNA that is
            transcriptionally regulated by cocaine and amphetamine
  JOURNAL   J Neurosci 15 (3 Pt 2), 2471-2481 (1995)
   PUBMED   7891182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U10071.1, SRR26360172.2203744.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..129
                     /product="cocaine- and amphetamine-regulated transcript
                     protein isoform 1 precursor"
                     /note="cocaine and amphetamine regulated transcript;
                     cocaine- and amphetamine-regulated transcript protein"
                     /calculated_mol_wt=11399
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2758
     mat_peptide     28..129
                     /product="Cocaine-and amphetamine-regulated transcript
                     protein. /id=PRO_0000004442"
                     /note="propagated from UniProtKB/Swiss-Prot (P49192.1)"
                     /calculated_mol_wt=11399
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49192.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49192.1)"
     Region          67..129
                     /region_name="CART"
                     /note="Cocaine and amphetamine regulated transcript
                     protein (CART); pfam06373"
                     /db_xref="CDD:461888"
     CDS             1..129
                     /gene="Cartpt"
                     /gene_synonym="Cart"
                     /coded_by="NM_017110.2:20..409"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29131"
                     /db_xref="RGD:2272"
ORIGIN      
        1 messrlrllp vlgaalllll pllgagaqed aelqpraldi ysavddashe kelprrqlra
       61 pgavlqieal qevlkklksk ripiyekkyg qvpmcdageq cavrkgarig klcdcprgts
      121 cnsfllkcl
//
LOCUS       NP_001424808             456 aa            linear   ROD 10-APR-2025
DEFINITION  megakaryocyte-associated tyrosine-protein kinase isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424808 XP_063120271
VERSION     NP_001424808.1
DBSOURCE    REFSEQ: accession NM_001437879.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Gunn,N.J., Gorman,M.A., Dobson,R.C., Parker,M.W. and Mulhern,T.D.
  TITLE     Purification, crystallization, small-angle X-ray scattering and
            preliminary X-ray diffraction analysis of the SH2 domain of the
            Csk-homologous kinase
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 336-339
            (2011)
   PUBMED   21393838
  REMARK    GeneRIF: The CHK SH2 was expressed in Escherichia coli and the
            purified protein was characterized as monomeric by synchrotron
            small-angle X-ray scattering in-line with size-exclusion
            chromatography.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Kuo,S.S., Moran,P., Gripp,J., Armanini,M., Phillips,H.S.,
            Goddard,A. and Caras,I.W.
  TITLE     Identification and characterization of Batk, a predominantly
            brain-specific non-receptor protein tyrosine kinase related to Csk
  JOURNAL   J Neurosci Res 38 (6), 705-715 (1994)
   PUBMED   7807586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063120271.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2424159.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840109 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..456
                     /product="megakaryocyte-associated tyrosine-protein kinase
                     isoform 2"
                     /EC_number="2.7.10.2"
                     /note="megakaryocyte-associated tyrosine-protein kinase;
                     protein kinase BATK; tyrosine-protein kinase CTK;
                     megakaryocyte-associated tyrosine kinase (non-receptor
                     protein tyrosine kinase); non-receptor protein kinase
                     protein"
                     /calculated_mol_wt=50480
     Region          9..67
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(16,18,21,25,44..45,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212745"
     Region          77..163
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(88,106,127,129)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198190"
     Site            order(128,143)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198190"
     Region          176..430
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(189..192,195,197,208,210,237,252..255,300,304..305,
                     307,317..318)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..456
                     /gene="Matk"
                     /gene_synonym="Batk"
                     /coded_by="NM_001437879.1:191..1561"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:60450"
                     /db_xref="RGD:69058"
ORIGIN      
        1 mptqrwapgt qcmtkcensr pkpgelafrk gdmvtileac edkswyrakh hssgqeglla
       61 aaalrqreal stdpklslmp wfhgkisgqe aiqqlqpped glflvresar hpgdyvlcvs
      121 fgrdvihyrv lhrdghltid eahytrdkga ictklvkpkr kqgaksaeee lakagwlldl
      181 qhltlgaqig egefgavlqg eylgqkvavk nikcdvtaqa fldetavmtk lqhrnlvrll
      241 gvilhhglyi vmehvskgnl vnflrtrgra lvstsqllqf alhvaegmey leskklvhrd
      301 laarnilvse dlvakvsdfg lakaelrkgl dssrlpvkwt apealkngrf ssksdvwsfg
      361 vllwevfsyg rapypkmslk evseavekgy rmeppdscpg pvhtlmgscw eaepsrrppf
      421 rkiveklgre lrsvgvaapa ggqeaegsap trsqdp
//
LOCUS       NP_001424786             539 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424786 XP_008768716
VERSION     NP_001424786.1
DBSOURCE    REFSEQ: accession NM_001437857.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 539)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768716.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.33848.1,
                                           SRR26643298.56235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..539
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 7"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=60071
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          407..534
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..539
                     /gene="Camk2g"
                     /coded_by="NM_001437857.1:70..1689"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kpqsnnknsl
      361 vspaqepapl qtamepqttv vhnatdgikg stescnttte dedlkvrkqe iikiteqlie
      421 ainngdfeay tkicdpglts fepealgnlv egmdfhkfyf enllsknskp ihttilnphv
      481 hvigedaaci ayirltqyid gqgrprtsqs eetrvwhrrd gkwlnvhyhc sgapaaplq
//
LOCUS       NP_001424760             261 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424760
VERSION     NP_001424760.1
DBSOURCE    REFSEQ: accession NM_001437831.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.2476.1,
                                           SRR26643294.2461.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..261
                     /product="sphingosine kinase 2 isoform 2"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=28380
     Region          <152..>248
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..261
                     /gene="Sphk2"
                     /coded_by="NM_001437831.1:973..1758"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggyvdc c
//
LOCUS       NP_001424781             577 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424781 XP_008768710
VERSION     NP_001424781.1
DBSOURCE    REFSEQ: accession NM_001437852.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 577)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768710.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.487419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..577
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=63906
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          445..572
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..577
                     /gene="Camk2g"
                     /coded_by="NM_001437852.1:70..1803"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kpqsnnknsl
      361 vspaqepapl qtamepqttv vhnatdgikg stescnttte dedlkaaplr tgngslvpeg
      421 rsprdrtaps agmqpqpslc ssamrkqeii kiteqlieai nngdfeaytk icdpgltsfe
      481 pealgnlveg mdfhkfyfen llsknskpih ttilnphvhv igedaaciay irltqyidgq
      541 grprtsqsee trvwhrrdgk wlnvhyhcsg apaaplq
//
LOCUS       NP_001424771             478 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424771 XP_038957631
VERSION     NP_001424771.1
DBSOURCE    REFSEQ: accession NM_001437842.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038957631.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.69318.1,
                                           SRR26360186.562340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 11"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=54060
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..478
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437842.1:417..1853"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkes tessnttied edvkarkqei ikvteqliea
      361 inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe nalpkinkpi htiilnphvh
      421 lvgddaacia yirltqymdg ngmpktmqse etrvwhrrdg kwqnihfhrs gsptvpin
//
LOCUS       NP_001424804             279 aa            linear   ROD 10-APR-2025
DEFINITION  growth hormone receptor isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001424804 XP_038957699
VERSION     NP_001424804.1
DBSOURCE    REFSEQ: accession NM_001437875.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Klammt,J., Shen,S., Kiess,W., Kratzsch,J., Stobbe,H., Vogel,M.,
            Luo,F. and Pfaffle,R.
  TITLE     Clinical and biochemical consequences of an intragenic growth
            hormone receptor (GHR) deletion in a large Chinese pedigree
  JOURNAL   Clin Endocrinol (Oxf) 82 (3), 453-461 (2015)
   PUBMED   25196842
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Deng,H.Z., Deng,H., Cen,C.Q., Chen,K.Y. and Du,M.L.
  TITLE     Post-receptor crosstalk between growth hormone and insulin signal
            in rats born small for gestational age with catch-up growth
  JOURNAL   PLoS One 9 (6), e100459 (2014)
   PUBMED   24963636
  REMARK    GeneRIF: receptor crosstalk between growth hormone and insulin
            signal in rats born small for gestational age with catch-up growth
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Claessen,K.M., Kloppenburg,M., Kroon,H.M., Bijsterbosch,J.,
            Pereira,A.M., Romijn,J.A., van der Straaten,T., Nelissen,R.G.,
            Hofman,A., Uitterlinden,A.G., Duijnisveld,B.J., Lakenberg,N.,
            Beekman,M., van Meurs,J.B., Slagboom,P.E., Biermasz,N.R. and
            Meulenbelt,I.
  TITLE     Relationship between the functional exon 3 deleted growth hormone
            receptor polymorphism and symptomatic osteoarthritis in women
  JOURNAL   Ann Rheum Dis 73 (2), 433-436 (2014)
   PUBMED   23740230
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Enhamre,E., Carlsson,A., Gronbladh,A., Watanabe,H., Hallberg,M. and
            Nyberg,F.
  TITLE     The expression of growth hormone receptor gene transcript in the
            prefrontal cortex is affected in male mice with diabetes-induced
            learning impairments
  JOURNAL   Neurosci Lett 523 (1), 82-86 (2012)
   PUBMED   22750159
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Frick,G.P. and Goodman,H.M.
  TITLE     Characterization of the short isoform of the growth hormone
            receptor synthesized by rat adipocytes
  JOURNAL   Endocrinology 131 (6), 3083-3090 (1992)
   PUBMED   1446642
REFERENCE   7  (residues 1 to 279)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Godowski,P.J., Leung,D.W., Meacham,L.R., Galgani,J.P., Hellmiss,R.,
            Keret,R., Rotwein,P.S., Parks,J.S., Laron,Z. and Wood,W.I.
  TITLE     Characterization of the human growth hormone receptor gene and
            demonstration of a partial gene deletion in two patients with
            Laron-type dwarfism
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8083-8087 (1989)
   PUBMED   2813379
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Baumbach,W.R., Horner,D.L. and Logan,J.S.
  TITLE     The growth hormone-binding protein in rat serum is an alternatively
            spliced form of the rat growth hormone receptor
  JOURNAL   Genes Dev 3 (8), 1199-1205 (1989)
   PUBMED   2792761
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Mathews,L.S., Enberg,B. and Norstedt,G.
  TITLE     Regulation of rat growth hormone receptor gene expression
  JOURNAL   J Biol Chem 264 (17), 9905-9910 (1989)
   PUBMED   2722883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038957699.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216498.1, BC127501.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..279
                     /product="growth hormone receptor isoform 2 precursor"
                     /note="growth hormone receptor/binding protein; GH
                     receptor; somatotropin receptor; growth hormone receptor
                     variant d5-6"
                     /calculated_mol_wt=29390
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2585
     Region          49..127
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          149..250
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(149,222,239)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          240..244
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000250|UniProtKB:P10912"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            order(240..241,243..244)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..279
                     /gene="Ghr"
                     /gene_synonym="GHR/BP"
                     /coded_by="NM_001437875.1:241..1080"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:25235"
                     /db_xref="RGD:2687"
ORIGIN      
        1 mdlwrvfltl alavssdmfp gsgatpatlg kaspvlqrin pslresssgk prftkcrspe
       61 letfscywte gddhnlkvpg siqlyyarri ahewtpewke cpdyvsagan scyfnssyts
      121 iwipyciklt tngdlldekc ftvdeivqpd ppiglnwtll nislpgirgd iqvswqppps
      181 advlkgwiil eyeiqykevn etkwktmspi wstsvplysl rldkehevrv rsrqrsfeky
      241 sefsevlrvt fpqmdtlaac eegpkfnsqh phqeidnhl
//
LOCUS       NP_001424753             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424753 XP_008757605
VERSION     NP_001424753.1
DBSOURCE    REFSEQ: accession NM_001437824.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008757605.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.2162.1,
                                           SRR26643295.2316.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437824.1:347..2197"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001102029             637 aa            linear   ROD 10-APR-2025
DEFINITION  U4/U6 small nuclear ribonucleoprotein Prp3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102029 XP_001057756 XP_342296
VERSION     NP_001102029.1
DBSOURCE    REFSEQ: accession NM_001108559.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Agafonov,D.E., Kastner,B., Dybkov,O., Hofele,R.V., Liu,W.T.,
            Urlaub,H., Luhrmann,R. and Stark,H.
  TITLE     Molecular architecture of the human U4/U6.U5 tri-snRNP
  JOURNAL   Science 351 (6280), 1416-1420 (2016)
   PUBMED   26912367
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Long,S.W., Ooi,J.Y., Yau,P.M. and Jones,P.L.
  TITLE     A brain-derived MeCP2 complex supports a role for MeCP2 in RNA
            processing
  JOURNAL   Biosci Rep 31 (5), 333-343 (2011)
   PUBMED   21070191
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Song,E.J., Werner,S.L., Neubauer,J., Stegmeier,F., Aspden,J.,
            Rio,D., Harper,J.W., Elledge,S.J., Kirschner,M.W. and Rape,M.
  TITLE     The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
            reversible ubiquitination at the spliceosome
  JOURNAL   Genes Dev 24 (13), 1434-1447 (2010)
   PUBMED   20595234
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Wahl,M.C., Will,C.L. and Luhrmann,R.
  TITLE     The spliceosome: design principles of a dynamic RNP machine
  JOURNAL   Cell 136 (4), 701-718 (2009)
   PUBMED   19239890
  REMARK    Review article
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Schaffert,N., Hossbach,M., Heintzmann,R., Achsel,T. and Luhrmann,R.
  TITLE     RNAi knockdown of hPrp31 leads to an accumulation of U4/U6
            di-snRNPs in Cajal bodies
  JOURNAL   EMBO J 23 (15), 3000-3009 (2004)
   PUBMED   15257298
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Chakarova,C.F., Hims,M.M., Bolz,H., Abu-Safieh,L., Patel,R.J.,
            Papaioannou,M.G., Inglehearn,C.F., Keen,T.J., Willis,C.,
            Moore,A.T., Rosenberg,T., Webster,A.R., Bird,A.C., Gal,A., Hunt,D.,
            Vithana,E.N. and Bhattacharya,S.S.
  TITLE     Mutations in HPRP3, a third member of pre-mRNA splicing factor
            genes, implicated in autosomal dominant retinitis pigmentosa
  JOURNAL   Hum Mol Genet 11 (1), 87-92 (2002)
   PUBMED   11773002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057756.1, XP_342296.2.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..637
                     /product="U4/U6 small nuclear ribonucleoprotein Prp3
                     isoform 1"
                     /note="U4/U6 small nuclear ribonucleoprotein Prp3; PRP3
                     pre-mRNA processing factor 3 homolog"
                     /calculated_mol_wt=72065
     Region          3..73
                     /region_name="PWI"
                     /note="domain in splicing factors; smart00311"
                     /db_xref="CDD:214609"
     Region          308..521
                     /region_name="PRP3"
                     /note="pre-mRNA processing factor 3 (PRP3); pfam08572"
                     /db_xref="CDD:462524"
     Region          541..>615
                     /region_name="Prp3_C"
                     /note="C-terminal domain of U4/U6 small nuclear
                     ribonucleoprotein Prp3; cd24162"
                     /db_xref="CDD:467813"
     CDS             1..637
                     /gene="Prpf3"
                     /coded_by="NM_001108559.2:87..2000"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361995"
                     /db_xref="RGD:1310555"
ORIGIN      
        1 malskrelde lkpwiektvk rvlgfseptv vtaalncvgk gmdkkkaadh lkpflddstl
       61 rfvdklfeav eegrssrhsk sssdrsrkre lkevfgddse iskessgvkk rriprfeeve
      121 eepevipgpp sespgmltkl qikqmmeaat rqieerkkql sfisppapqp ktpsssqper
      181 lpigntiqps qaatfmndai ekarkaaelq ariqaqlalk pglignanmv glanlhamgi
      241 appkvelkdq tkptplilde qgrtvdatgk evelthrmpt lkaniravkr eqfkqqlkek
      301 psedmesntf fdprvsiaps qrqrrtfkfh dkgkfekiaq rlrtkaqlek lqaeisqaar
      361 ktgihtstrl aliapkkelk egdipeieww dsyiipngfd lteenpkred yfgitnlveh
      421 paqlnppvdn dtpvtlgvyl tkkeqkklrr qtrreaqkel qekvrlgltp ppepkvrisn
      481 lmrvlgteav qdptkveahv raqmakrqka heeanaarkl taeqrkvkkv kklkedisqg
      541 vhisvyrvrn lsnpakkfki eanagqlylt gvvvlhkdvn vvvveggpka qkkfkrlmlh
      601 rikwdeqtsn tkgdghsqrp elwrdevqtv pyrehga
//
LOCUS       NP_001424809             467 aa            linear   ROD 10-APR-2025
DEFINITION  megakaryocyte-associated tyrosine-protein kinase isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424809 XP_063120270
VERSION     NP_001424809.1
DBSOURCE    REFSEQ: accession NM_001437880.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gunn,N.J., Gorman,M.A., Dobson,R.C., Parker,M.W. and Mulhern,T.D.
  TITLE     Purification, crystallization, small-angle X-ray scattering and
            preliminary X-ray diffraction analysis of the SH2 domain of the
            Csk-homologous kinase
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 336-339
            (2011)
   PUBMED   21393838
  REMARK    GeneRIF: The CHK SH2 was expressed in Escherichia coli and the
            purified protein was characterized as monomeric by synchrotron
            small-angle X-ray scattering in-line with size-exclusion
            chromatography.
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Kuo,S.S., Moran,P., Gripp,J., Armanini,M., Phillips,H.S.,
            Goddard,A. and Caras,I.W.
  TITLE     Identification and characterization of Batk, a predominantly
            brain-specific non-receptor protein tyrosine kinase related to Csk
  JOURNAL   J Neurosci Res 38 (6), 705-715 (1994)
   PUBMED   7807586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063120270.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.37820.1,
                                           SRR26360176.2256034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..467
                     /product="megakaryocyte-associated tyrosine-protein kinase
                     isoform 1"
                     /EC_number="2.7.10.2"
                     /note="megakaryocyte-associated tyrosine-protein kinase;
                     protein kinase BATK; tyrosine-protein kinase CTK;
                     megakaryocyte-associated tyrosine kinase (non-receptor
                     protein tyrosine kinase); non-receptor protein kinase
                     protein"
                     /calculated_mol_wt=51766
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     Region          9..67
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(16,18,21,25,44..45,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          77..174
                     /region_name="SH2_csk_like"
                     /note="Src homology 2 (SH2) domain found in
                     Carboxyl-Terminal Src Kinase (Csk); cd09937"
                     /db_xref="CDD:198190"
     Site            order(88,106,127,129)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198190"
     Site            order(128,155)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198190"
     Region          187..441
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(200..203,206,208,219,221,248,263..266,311,315..316,
                     318,328..329)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          445..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     CDS             1..467
                     /gene="Matk"
                     /gene_synonym="Batk"
                     /coded_by="NM_001437880.1:324..1727"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:60450"
                     /db_xref="RGD:69058"
ORIGIN      
        1 mptqrwapgt qcmtkcensr pkpgelafrk gdmvtileac edkswyrakh hssgqeglla
       61 aaalrqreal stdpklslmp wfhgkisgqe aiqqlqpped glflvresar hpgdyvlcvs
      121 fgrdvihyrv lhrdghltid eavcfcnlmd mvehytrdkg aictklvkpk rkqgaksaee
      181 elakagwlld lqhltlgaqi gegefgavlq geylgqkvav knikcdvtaq afldetavmt
      241 klqhrnlvrl lgvilhhgly ivmehvskgn lvnflrtrgr alvstsqllq falhvaegme
      301 yleskklvhr dlaarnilvs edlvakvsdf glakaelrkg ldssrlpvkw tapealkngr
      361 fssksdvwsf gvllwevfsy grapypkmsl kevseavekg yrmeppdscp gpvhtlmgsc
      421 weaepsrrpp frkiveklgr elrsvgvaap aggqeaegsa ptrsqdp
//
LOCUS       NP_001424762             533 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424762 XP_008759674
VERSION     NP_001424762.1
DBSOURCE    REFSEQ: accession NM_001437833.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008759674.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.876913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=59951
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          337..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     CDS             1..533
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437833.1:417..2018"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalpki nkpihtiiln phvhlvgdda aciayirltq ymdgngmpkt
      481 mqseetrvwh rrdgkwqnih fhrsgsptvp ikppcipngk enfsggtslw qni
//
LOCUS       NP_001424787             533 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 8 [Rattus norvegicus].
ACCESSION   NP_001424787 XP_008768717
VERSION     NP_001424787.1
DBSOURCE    REFSEQ: accession NM_001437858.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768717.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.44587.1,
                                           SRR26360176.601146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 8"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=59665
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          401..528
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..533
                     /gene="Camk2g"
                     /coded_by="NM_001437858.1:70..1671"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna tdgikgstes cntttededl
      361 kaaplrtgng slvpegrspr drtapsagmq pqpslcssam rkqeiikite qlieainngd
      421 feaytkicdp gltsfepeal gnlvegmdfh kfyfenllsk nskpihttil nphvhviged
      481 aaciayirlt qyidgqgrpr tsqseetrvw hrrdgkwlnv hyhcsgapaa plq
//
LOCUS       NP_001424802             476 aa            linear   ROD 10-APR-2025
DEFINITION  doublesex and mab-3 related transcription factor 3 [Rattus
            norvegicus].
ACCESSION   NP_001424802 XP_063143177
VERSION     NP_001424802.1
DBSOURCE    REFSEQ: accession NM_001437873.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Andersson,L.S., Larhammar,M., Memic,F., Wootz,H., Schwochow,D.,
            Rubin,C.J., Patra,K., Arnason,T., Wellbring,L., Hjalm,G.,
            Imsland,F., Petersen,J.L., McCue,M.E., Mickelson,J.R., Cothran,G.,
            Ahituv,N., Roepstorff,L., Mikko,S., Vallstedt,A., Lindgren,G.,
            Andersson,L. and Kullander,K.
  TITLE     Mutations in DMRT3 affect locomotion in horses and spinal circuit
            function in mice
  JOURNAL   Nature 488 (7413), 642-646 (2012)
   PUBMED   22932389
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Konno,D., Iwashita,M., Satoh,Y., Momiyama,A., Abe,T., Kiyonari,H.
            and Matsuzaki,F.
  TITLE     The mammalian DM domain transcription factor Dmrta2 is required for
            early embryonic development of the cerebral cortex
  JOURNAL   PLoS One 7 (10), e46577 (2012)
   PUBMED   23056351
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Ahituv,N., Zhu,Y., Visel,A., Holt,A., Afzal,V., Pennacchio,L.A. and
            Rubin,E.M.
  TITLE     Deletion of ultraconserved elements yields viable mice
  JOURNAL   PLoS Biol 5 (9), e234 (2007)
   PUBMED   17803355
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Murphy,M.W., Zarkower,D. and Bardwell,V.J.
  TITLE     Vertebrate DM domain proteins bind similar DNA sequences and can
            heterodimerize on DNA
  JOURNAL   BMC Mol Biol 8, 58 (2007)
   PUBMED   17605809
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063143177.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.944210.1,
                                           SRR22582419.957498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840106, SAMN12840108
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..476
                     /product="doublesex and mab-3 related transcription factor
                     3"
                     /calculated_mol_wt=51313
     Region          25..71
                     /region_name="DM"
                     /note="DM DNA binding domain; pfam00751"
                     /db_xref="CDD:459924"
     Region          89..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     Region          147..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     Region          253..295
                     /region_name="CUE_DMA_DMRTA3"
                     /note="CUE-like DMA domain found in doublesex- and
                     mab-3-related transcription factor 3 (DMRTA3); cd14419"
                     /db_xref="CDD:270602"
     Region          418..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     CDS             1..476
                     /gene="Dmrt3"
                     /coded_by="NM_001437873.1:309..1739"
                     /db_xref="GeneID:293976"
                     /db_xref="RGD:1306043"
ORIGIN      
        1 mngygspyly mggpvsqppr aplqrtpkca rcrnhgvlsw lkghkrycrf kdctcekcil
       61 iierqrvmaa qvalrrqqan esleslipds lralpgpppp gdaaataata sqsspasqas
      121 qppapprpat elaaaaalrw vaepqpgtlp aqiakpdlte drlgdsssad naaesfsdkd
      181 tdqrsspdvv kskncftpes peivsvdegg yavqknggnp escpdspkyh aeqshllieg
      241 psgtvslpfs lkanrpplev lkkifpnqkp tvlelilkgc ggdlvsavev llssrssaag
      301 aertaeeslv lpssghifeh tlgsypisss kwsvgsafrv pdtlrfsads snvvpnplav
      361 plqhpfpqpp ryplmlrntl arnqsspflp ndvtlwntmt lqqqyqlrsq yvspfpsnst
      421 svfrsspvls srttedpris ipddgcpiva kqsiyteddy dersdssdsr ilntss
//
LOCUS       NP_001424799            1992 aa            linear   ROD 10-APR-2025
DEFINITION  myosin-14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424799 XP_063117993
VERSION     NP_001424799.1
DBSOURCE    REFSEQ: accession NM_001437870.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1992)
  AUTHORS   Billington,N., Wang,A., Mao,J., Adelstein,R.S. and Sellers,J.R.
  TITLE     Characterization of three full-length human nonmuscle myosin II
            paralogs
  JOURNAL   J Biol Chem 288 (46), 33398-33410 (2013)
   PUBMED   24072716
REFERENCE   2  (residues 1 to 1992)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   3  (residues 1 to 1992)
  AUTHORS   Choi,B.O., Kang,S.H., Hyun,Y.S., Kanwal,S., Park,S.W., Koo,H.,
            Kim,S.B., Choi,Y.C., Yoo,J.H., Kim,J.W., Park,K.D., Choi,K.G.,
            Kim,S.J., Zuchner,S. and Chung,K.W.
  TITLE     A complex phenotype of peripheral neuropathy, myopathy, hoarseness,
            and hearing loss is linked to an autosomal dominant mutation in
            MYH14
  JOURNAL   Hum Mutat 32 (6), 669-677 (2011)
   PUBMED   21480433
REFERENCE   4  (residues 1 to 1992)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 1992)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 1992)
  AUTHORS   Kim,K.Y., Kovacs,M., Kawamoto,S., Sellers,J.R. and Adelstein,R.S.
  TITLE     Disease-associated mutations and alternative splicing alter the
            enzymatic and motile activity of nonmuscle myosins II-B and II-C
  JOURNAL   J Biol Chem 280 (24), 22769-22775 (2005)
   PUBMED   15845534
REFERENCE   7  (residues 1 to 1992)
  AUTHORS   Turney,S.G. and Bridgman,P.C.
  TITLE     Laminin stimulates and guides axonal outgrowth via growth cone
            myosin II activity
  JOURNAL   Nat Neurosci 8 (6), 717-719 (2005)
   PUBMED   15880105
REFERENCE   8  (residues 1 to 1992)
  AUTHORS   Bao,J., Jana,S.S. and Adelstein,R.S.
  TITLE     Vertebrate nonmuscle myosin II isoforms rescue small interfering
            RNA-induced defects in COS-7 cell cytokinesis
  JOURNAL   J Biol Chem 280 (20), 19594-19599 (2005)
   PUBMED   15774463
  REMARK    Erratum:[J Biol Chem. 2006 Apr 14;281(15):10652]
REFERENCE   9  (residues 1 to 1992)
  AUTHORS   Donaudy,F., Snoeckx,R., Pfister,M., Zenner,H.P., Blin,N., Di
            Stazio,M., Ferrara,A., Lanzara,C., Ficarella,R., Declau,F.,
            Pusch,C.M., Nurnberg,P., Melchionda,S., Zelante,L., Ballana,E.,
            Estivill,X., Van Camp,G., Gasparini,P. and Savoia,A.
  TITLE     Nonmuscle myosin heavy-chain gene MYH14 is expressed in cochlea and
            mutated in patients affected by autosomal dominant hearing
            impairment (DFNA4)
  JOURNAL   Am J Hum Genet 74 (4), 770-776 (2004)
   PUBMED   15015131
REFERENCE   10 (residues 1 to 1992)
  AUTHORS   Golomb,E., Ma,X., Jana,S.S., Preston,Y.A., Kawamoto,S.,
            Shoham,N.G., Goldin,E., Conti,M.A., Sellers,J.R. and Adelstein,R.S.
  TITLE     Identification and characterization of nonmuscle myosin II-C, a new
            member of the myosin II family
  JOURNAL   J Biol Chem 279 (4), 2800-2808 (2004)
   PUBMED   14594953
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063117993.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1373.1,
                                           SRR26643289.1557.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1992
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1992
                     /product="myosin-14 isoform 2"
                     /EC_number="5.6.1.8"
                     /note="myosin, heavy polypeptide 14; myosin-14; myosin,
                     heavy chain 14, non-muscle"
                     /calculated_mol_wt=227957
     Region          115..784
                     /region_name="MYSc_Myh14_mammals"
                     /note="class II myosin heavy chain 14 motor domain;
                     cd14930"
                     /db_xref="CDD:276893"
     Site            order(142..150,194..201,247..257,474..479)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276893"
     Site            142..150
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276893"
     Site            194..201
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276893"
     Site            247..257
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276893"
     Site            474..479
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276893"
     Site            order(503..514,517..526)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276893"
     Site            716..725
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276893"
     Site            order(728..744,769..784)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276893"
     Region          861..1941
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     CDS             1..1992
                     /gene="Myh14"
                     /coded_by="NM_001437870.1:42..6020"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:308572"
                     /db_xref="RGD:1306821"
ORIGIN      
        1 matvtlsvpg rkvasrpgpv peaaqpflfa prtpnvggpg gpqvewtarr mvwvpselhg
       61 feaaalrdeg eeeaevelae sgrrlrlprd qiqrmnppkf skaedmaelt clneasvlhn
      121 lreryysgli ytysglfcvv inpykqlpiy teaivemyrg kkrhevpphi yavtegayrs
      181 mlqdredqsi lctgesgagk tentkkviqy lahvasspkg rkepgvpgel erqllqanpi
      241 leafgnaktv kndnssrfgk firinfdiag yivganiety lleksrairq akdecsfhif
      301 yqllggageq lkadlllepy shyrfltngp ssspgqerel fqetleslrv lgllpeeita
      361 mlrtvsavlq fgnivlkker ntdqatmpdn taaqklcrll glgvtdfsra lltprikvgr
      421 dyvqkaqtke qadfaleala katyerlfrw lvlrlnrald rsprqgasfl gildiagfei
      481 fqlnsfeqlc inytneklqq lfnhtmfvle qeeyqregip wtfldfgldl qpcidlierp
      541 anppgllall deecwfpkat dksfvekvaq eqgshpkfqr prnlrdqadf svlhyagkvd
      601 ykanewlmkn mdplndnvaa llhqstdrlt aeiwkdvegi vgleqvsslg dgppggrprr
      661 gmfrtvgqly keslsrlmat lsntnpsfvr civpnhekra gkleprlvld qlrcngvleg
      721 iricrqgfpn rilfqefrqr yeiltpnaip kgfmdgkqac ekmiqaleld pnlyrvgqsk
      781 iffragvlaq leeerdlkvt diivsfqaaa rgylarrafq rrqqqqsalr vmqrncaayl
      841 klrnwqwwrl fikvkpllqv trqdevlqar aqelqkvqel qqqsarevge lqgrvaqlee
      901 erarlaeqlr aeaelcseae etrarlaark qelelvvtel earvgeeeec srqlqsekkr
      961 lqqhiqelet hleaeegarq klqlekvtte akmkkfeedl llledqnskl skerrlleer
     1021 laefssqaae eeekvkslnk lrvkyeatia dmedrlkkee kgrqeleklk rrldgessel
     1081 qeqmmeqkqr aeelliqlgr keeelqsalv raeeeggara qllkslreaq aglaeaqedl
     1141 eaervaraka ekqrrdlgee lealrgeled tldstnaqqe lrskreqevt elkktleeea
     1201 rthevamqel rqrhsqalve lteqleqarr gksvwektrl sleaevselk telsslqtsr
     1261 qegeqkrrrl esqlqevqgr ssdserarae aaeklqraqv elesvstals eaeskairls
     1321 kelssaesql hdtqellqee traklalgsr vraleaeaag lreqmeeevv areragrelq
     1381 ttqaqlsewr rrqeeeaavl eageearrra areaetlaqr laekteaver lerarrrlqq
     1441 elddatvdlg qqkqllstle kkqrkfdqll aeekaavlra vedrerveae grerearals
     1501 ltraleeeqe areelerqnr alraeleall sskddvgknv helerarrva eqaasdlrtq
     1561 vteledelta aedaklrlev tvqalkaqhe rdlqgrddag eerrrqlakq lrdaeverde
     1621 erkqralama arkklelele elkaqtsaag qgkeeavkql kkmqaqmkel wreveetrss
     1681 reemftlsre sekrlkglea evlrlqeela asdrarrqaq qdrdemaeev asgnlskaat
     1741 leekrqlegr lgqleeelee eqnnsellkd hyrklvlqve tlttelsaer sfsakaesgr
     1801 qqlerqiqel rarlgeedag ararqkmlia alesklaqae eqleqesrer ilsgklvrra
     1861 ekrlkevvlq vdeerrvadq lrdqleksnl rlkqlkrqle eaeeeasraq agrrrlqrel
     1921 edvtesaesm nrevttlrnr lrrgpltftt rtvrqvfrle egvasdeeea egaepgsapt
     1981 qepeapppaa pq
//
LOCUS       NP_001424736             505 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424736 XP_063144731
VERSION     NP_001424736.1
DBSOURCE    REFSEQ: accession NM_001437807.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144731.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1014447.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..505
                     /product="phosphatase and actin regulator 2 isoform 6"
                     /calculated_mol_wt=55293
     Region          62..83
                     /region_name="RPEL"
                     /note="RPEL repeat; pfam02755"
                     /db_xref="CDD:460677"
     Region          348..373
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          387..411
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          424..449
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..505
                     /gene="Phactr2"
                     /coded_by="NM_001437807.1:135..1652"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mdkavdgldk asiansdgpp agsqtppfkr kgklstigki fkpwkwrkkk tsdkfretsa
       61 vlerkistrq sreelirrgl lkelpdqags shpkkttgsk assspsasst sshprgpkes
      121 ltgkagavgt trgkkkiskq paaaasrlsp ntvtsetssl kgelsdtgve slkpeetvag
      181 aeeeatgkpk avvvalppvt vppsspalpl ppedpctial dtpmvlvsdg ptlpisalet
      241 splpgteepa nrttpysstg lggsreqakc fttkdgpgka gpqlltpgqm gdslesfsap
      301 edeapreyqa ndsdsdgpil ytddddeedd dddstgesal askirrrdtl aiklgnrpsk
      361 keledknilq rtseeerqel rqqigtklvr rlsqrpttee leqrnilkqk neeeeqeakm
      421 elkrrlsrkl slrptvaelq arrilrfney vevtdspdyd rradkpwarl tpadkaairk
      481 elnefkstem evheesrqft rfhrp
//
LOCUS       NP_001424732             628 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424732 XP_017444590
VERSION     NP_001424732.1
DBSOURCE    REFSEQ: accession NM_001437803.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017444590.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.121.1,
                                           SRR26360181.3308209.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..628
                     /product="phosphatase and actin regulator 2 isoform 1"
                     /calculated_mol_wt=68287
     Region          132..153
                     /region_name="RPEL"
                     /note="RPEL repeat; pfam02755"
                     /db_xref="CDD:460677"
     Region          471..496
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          510..534
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          547..572
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..628
                     /gene="Phactr2"
                     /coded_by="NM_001437803.1:126..2012"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 maeagrspem spdqpdgqea vaaevpdpep eapgppvpal rwlpgdpspr grsqsdlssa
       61 ssrgrplrvh isgsvdgldk asiansdgpp agsqtppfkr kgklstigki fkpwkwrkkk
      121 tsdkfretsa vlerkistrq sreelirrgl lkelpdqdgd vtvnfensng hmihigeeat
      181 qeenvgkpee gnvsvcekgp preeqaeekt agsshpkktt gskassspsa sstsshprgp
      241 kesltgkaga vgttrgkkki skqpaaaasr lspntvtset sslkgelsdt gveslkpeet
      301 vagaeeeatg kpkavvvalp pvtvppsspa lplppedpct ialdtpmvlv sdgptlpisa
      361 letsplpgte epanrttpys stglggsreq akcfttkdgp gkagpqlltp gqmgdslesf
      421 sapedeapre yqandsdsdg pilytdddde edddddstge salaskirrr dtlaiklgnr
      481 pskkeledkn ilqrtseeer qelrqqigtk lvrrlsqrpt teeleqrnil kqkneeeeqe
      541 akmelkrrls rklslrptva elqarrilrf neyvevtdsp dydrradkpw arltpadkaa
      601 irkelnefks temevheesr qftrfhrp
//
LOCUS       NP_001424801             638 aa            linear   ROD 10-APR-2025
DEFINITION  growth hormone receptor isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001424801 XP_038957698
VERSION     NP_001424801.1
DBSOURCE    REFSEQ: accession NM_001437872.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Klammt,J., Shen,S., Kiess,W., Kratzsch,J., Stobbe,H., Vogel,M.,
            Luo,F. and Pfaffle,R.
  TITLE     Clinical and biochemical consequences of an intragenic growth
            hormone receptor (GHR) deletion in a large Chinese pedigree
  JOURNAL   Clin Endocrinol (Oxf) 82 (3), 453-461 (2015)
   PUBMED   25196842
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Deng,H.Z., Deng,H., Cen,C.Q., Chen,K.Y. and Du,M.L.
  TITLE     Post-receptor crosstalk between growth hormone and insulin signal
            in rats born small for gestational age with catch-up growth
  JOURNAL   PLoS One 9 (6), e100459 (2014)
   PUBMED   24963636
  REMARK    GeneRIF: receptor crosstalk between growth hormone and insulin
            signal in rats born small for gestational age with catch-up growth
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Claessen,K.M., Kloppenburg,M., Kroon,H.M., Bijsterbosch,J.,
            Pereira,A.M., Romijn,J.A., van der Straaten,T., Nelissen,R.G.,
            Hofman,A., Uitterlinden,A.G., Duijnisveld,B.J., Lakenberg,N.,
            Beekman,M., van Meurs,J.B., Slagboom,P.E., Biermasz,N.R. and
            Meulenbelt,I.
  TITLE     Relationship between the functional exon 3 deleted growth hormone
            receptor polymorphism and symptomatic osteoarthritis in women
  JOURNAL   Ann Rheum Dis 73 (2), 433-436 (2014)
   PUBMED   23740230
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Enhamre,E., Carlsson,A., Gronbladh,A., Watanabe,H., Hallberg,M. and
            Nyberg,F.
  TITLE     The expression of growth hormone receptor gene transcript in the
            prefrontal cortex is affected in male mice with diabetes-induced
            learning impairments
  JOURNAL   Neurosci Lett 523 (1), 82-86 (2012)
   PUBMED   22750159
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Frick,G.P. and Goodman,H.M.
  TITLE     Characterization of the short isoform of the growth hormone
            receptor synthesized by rat adipocytes
  JOURNAL   Endocrinology 131 (6), 3083-3090 (1992)
   PUBMED   1446642
REFERENCE   7  (residues 1 to 638)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Godowski,P.J., Leung,D.W., Meacham,L.R., Galgani,J.P., Hellmiss,R.,
            Keret,R., Rotwein,P.S., Parks,J.S., Laron,Z. and Wood,W.I.
  TITLE     Characterization of the human growth hormone receptor gene and
            demonstration of a partial gene deletion in two patients with
            Laron-type dwarfism
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8083-8087 (1989)
   PUBMED   2813379
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Baumbach,W.R., Horner,D.L. and Logan,J.S.
  TITLE     The growth hormone-binding protein in rat serum is an alternatively
            spliced form of the rat growth hormone receptor
  JOURNAL   Genes Dev 3 (8), 1199-1205 (1989)
   PUBMED   2792761
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Mathews,L.S., Enberg,B. and Norstedt,G.
  TITLE     Regulation of rat growth hormone receptor gene expression
  JOURNAL   J Biol Chem 264 (17), 9905-9910 (1989)
   PUBMED   2722883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038957698.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.7375.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..638
                     /product="growth hormone receptor isoform 1 precursor"
                     /note="growth hormone receptor/binding protein; GH
                     receptor; somatotropin receptor; growth hormone receptor
                     variant d5-6"
                     /calculated_mol_wt=69187
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=2068
     mat_peptide     19..638
                     /product="Growth hormone receptor. /id=PRO_0000010969"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=69187
     Region          49..127
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          149..250
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(149,222,239)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          240..244
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000250|UniProtKB:P10912"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            order(240..241,243..244)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            266..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          295..380
                     /region_name="Required for JAK2 binding.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          298..306
                     /region_name="Box 1 motif.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          317..616
                     /region_name="GHBP"
                     /note="Growth hormone receptor binding; pfam12772"
                     /db_xref="CDD:463696"
     Region          341..350
                     /region_name="UbE motif.
                     /evidence=ECO:0000305|PubMed:7615519"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          357..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     CDS             1..638
                     /gene="Ghr"
                     /gene_synonym="GHR/BP"
                     /coded_by="NM_001437872.1:50..1966"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:25235"
                     /db_xref="RGD:2687"
ORIGIN      
        1 mdlwrvfltl alavssdmfp gsgatpatlg kaspvlqrin pslresssgk prftkcrspe
       61 letfscywte gddhnlkvpg siqlyyarri ahewtpewke cpdyvsagan scyfnssyts
      121 iwipyciklt tngdlldekc ftvdeivqpd ppiglnwtll nislpgirgd iqvswqppps
      181 advlkgwiil eyeiqykevn etkwktmspi wstsvplysl rldkehevrv rsrqrsfeky
      241 sefsevlrvt fpqmdtlaac eedfrfpwfl iiifgifgva vmlfvvifsk qqrikmlilp
      301 pvpvpkikgi dpdllkegkl eevntilgih dnykpdfynd dswvefield iddadektee
      361 sdtdrllsdd qeksagilga kdddsgrtsc ydpdildtdf htsdmcdgts efaqpqklka
      421 eadllcldqk nlknspydas lgslhpsitl tmedkpqpll gsetesthql pstpmsspvs
      481 lanidfyaqv sditpaggvv lspgqkikag laqgntqlev aapcqenysm nsayfcesda
      541 kkciaaaphm eattcvkpsf nqediyitte sltttarmse tadtapdaep vpdyttvhtv
      601 ksprglilna talplpdkkk flsscgyvst dqlnkimq
//
LOCUS       NP_001019512             366 aa            linear   ROD 10-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001019512 XP_575762
VERSION     NP_001019512.1
DBSOURCE    REFSEQ: accession NM_001024341.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On May 27, 2005 this sequence version replaced XP_575762.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC091289.1, SRR26360194.1205977.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001024341.2:316..1416"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424774             394 aa            linear   ROD 10-APR-2025
DEFINITION  transcriptional enhancer factor TEF-4 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424774 XP_063118099
VERSION     NP_001424774.1
DBSOURCE    REFSEQ: accession NM_001437845.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Tamm,C., Bower,N. and Anneren,C.
  TITLE     Regulation of mouse embryonic stem cell self-renewal by a
            Yes-YAP-TEAD2 signaling pathway downstream of LIF
  JOURNAL   J Cell Sci 124 (Pt 7), 1136-1144 (2011)
   PUBMED   21385842
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Tian,W., Yu,J., Tomchick,D.R., Pan,D. and Luo,X.
  TITLE     Structural and functional analysis of the YAP-binding domain of
            human TEAD2
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7293-7298 (2010)
   PUBMED   20368466
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Bhattaram,P., Penzo-Mendez,A., Sock,E., Colmenares,C., Kaneko,K.J.,
            Vassilev,A., Depamphilis,M.L., Wegner,M. and Lefebvre,V.
  TITLE     Organogenesis relies on SoxC transcription factors for the survival
            of neural and mesenchymal progenitors
  JOURNAL   Nat Commun 1 (1), 9 (2010)
   PUBMED   20596238
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Zhang,H., Liu,C.Y., Zha,Z.Y., Zhao,B., Yao,J., Zhao,S., Xiong,Y.,
            Lei,Q.Y. and Guan,K.L.
  TITLE     TEAD transcription factors mediate the function of TAZ in cell
            growth and epithelial-mesenchymal transition
  JOURNAL   J Biol Chem 284 (20), 13355-13362 (2009)
   PUBMED   19324877
  REMARK    Erratum:[J Biol Chem. 2019 Apr 12;294(15):5808. doi:
            10.1074/jbc.AAC119.008436. PMID: 30979850]
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Zhao,B., Ye,X., Yu,J., Li,L., Li,W., Li,S., Yu,J., Lin,J.D.,
            Wang,C.Y., Chinnaiyan,A.M., Lai,Z.C. and Guan,K.L.
  TITLE     TEAD mediates YAP-dependent gene induction and growth control
  JOURNAL   Genes Dev 22 (14), 1962-1971 (2008)
   PUBMED   18579750
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Sawada,A., Nishizaki,Y., Sato,H., Yada,Y., Nakayama,R.,
            Yamamoto,S., Nishioka,N., Kondoh,H. and Sasaki,H.
  TITLE     Tead proteins activate the Foxa2 enhancer in the node in
            cooperation with a second factor
  JOURNAL   Development 132 (21), 4719-4729 (2005)
   PUBMED   16207754
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Kaneko,K.J., Rein,T., Guo,Z.S., Latham,K. and DePamphilis,M.L.
  TITLE     DNA methylation may restrict but does not determine differential
            gene expression at the Sgy/Tead2 locus during mouse development
  JOURNAL   Mol Cell Biol 24 (5), 1968-1982 (2004)
   PUBMED   14966277
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Milewski,R.C., Chi,N.C., Li,J., Brown,C., Lu,M.M. and Epstein,J.A.
  TITLE     Identification of minimal enhancer elements sufficient for Pax3
            expression in neural crest and implication of Tead2 as a regulator
            of Pax3
  JOURNAL   Development 131 (4), 829-837 (2004)
   PUBMED   14736747
  REMARK    Erratum:[Development. 2004 Mar;131(5):1195]
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Yockey,C.E. and Shimizu,N.
  TITLE     cDNA cloning and characterization of mouse DTEF-1 and ETF, members
            of the TEA/ATTS family of transcription factors
  JOURNAL   DNA Cell Biol 17 (2), 187-196 (1998)
   PUBMED   9502435
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Yasunami,M., Suzuki,K., Houtani,T., Sugimoto,T. and Ohkubo,H.
  TITLE     Molecular characterization of cDNA encoding a novel protein related
            to transcriptional enhancer factor-1 from neural precursor cells
  JOURNAL   J Biol Chem 270 (31), 18649-18654 (1995)
   PUBMED   7629195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063118099.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.4192302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..394
                     /product="transcriptional enhancer factor TEF-4 isoform 2"
                     /note="Embryonic TEA domain containing factor; TEA domain
                     family member 2; transcriptional enhancer factor TEF-4"
                     /calculated_mol_wt=42051
     Region          40..107
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          227..>357
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..394
                     /gene="Tead2"
                     /coded_by="NM_001437845.1:48..1232"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308582"
                     /db_xref="RGD:1593252"
ORIGIN      
        1 mgdprtgapl ddgggwtgse egseegtggs egvggdgspd aegvwspdie qsfqealaiy
       61 ppcgrrkiil sdegkmygrn eliaryiklr tgktrtrkqv sshiqvlarr ksreiqsklk
      121 dqvskdkafq tmatmssaql isapslqakl gpsgpqatel fqfwsgssgp twnvpdvkpf
      181 sqapfsmslt ppatdlpgye pppalsplpp papsppawqa ralgtarlql vefsafvepp
      241 davdsfqrhl fvhisqqcps pgapplesvd vrqiydkfpe kkgglrelyd rgpphafflv
      301 kfwadlnwgp saeeagnsgg aggfygvssq yesrelmtlt csskvcsfgk qvvekvesgp
      361 swragalcta ccalpcvstw stsctssvsc lsat
//
LOCUS       NP_001424815             366 aa            linear   ROD 10-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001424815 XP_063144257
VERSION     NP_001424815.1
DBSOURCE    REFSEQ: accession NM_001437886.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144257.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.485321.1,
                                           SRR26360186.767589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001437886.1:453..1553"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424764             527 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424764 XP_063137349
VERSION     NP_001424764.1
DBSOURCE    REFSEQ: accession NM_001437835.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063137349.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.471440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..527
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 4"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=59497
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          337..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..527
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437835.1:417..2000"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalpki nkpihtiiln phvhlvgdda aciayirltq ymdgngmpkt
      481 mqseetrvwh rrdgkwqnih fhrsgsptvp inywtdvpck rqlllan
//
LOCUS       NP_001424759             261 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424759
VERSION     NP_001424759.1
DBSOURCE    REFSEQ: accession NM_001437830.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.1742.1,
                                           SRR26643292.2164.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..261
                     /product="sphingosine kinase 2 isoform 2"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=28380
     Region          <152..>248
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..261
                     /gene="Sphk2"
                     /coded_by="NM_001437830.1:276..1061"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggyvdc c
//
LOCUS       NP_058790                638 aa            linear   ROD 10-APR-2025
DEFINITION  growth hormone receptor isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_058790
VERSION     NP_058790.1
DBSOURCE    REFSEQ: accession NM_017094.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Klammt,J., Shen,S., Kiess,W., Kratzsch,J., Stobbe,H., Vogel,M.,
            Luo,F. and Pfaffle,R.
  TITLE     Clinical and biochemical consequences of an intragenic growth
            hormone receptor (GHR) deletion in a large Chinese pedigree
  JOURNAL   Clin Endocrinol (Oxf) 82 (3), 453-461 (2015)
   PUBMED   25196842
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Deng,H.Z., Deng,H., Cen,C.Q., Chen,K.Y. and Du,M.L.
  TITLE     Post-receptor crosstalk between growth hormone and insulin signal
            in rats born small for gestational age with catch-up growth
  JOURNAL   PLoS One 9 (6), e100459 (2014)
   PUBMED   24963636
  REMARK    GeneRIF: receptor crosstalk between growth hormone and insulin
            signal in rats born small for gestational age with catch-up growth
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Claessen,K.M., Kloppenburg,M., Kroon,H.M., Bijsterbosch,J.,
            Pereira,A.M., Romijn,J.A., van der Straaten,T., Nelissen,R.G.,
            Hofman,A., Uitterlinden,A.G., Duijnisveld,B.J., Lakenberg,N.,
            Beekman,M., van Meurs,J.B., Slagboom,P.E., Biermasz,N.R. and
            Meulenbelt,I.
  TITLE     Relationship between the functional exon 3 deleted growth hormone
            receptor polymorphism and symptomatic osteoarthritis in women
  JOURNAL   Ann Rheum Dis 73 (2), 433-436 (2014)
   PUBMED   23740230
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Enhamre,E., Carlsson,A., Gronbladh,A., Watanabe,H., Hallberg,M. and
            Nyberg,F.
  TITLE     The expression of growth hormone receptor gene transcript in the
            prefrontal cortex is affected in male mice with diabetes-induced
            learning impairments
  JOURNAL   Neurosci Lett 523 (1), 82-86 (2012)
   PUBMED   22750159
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Frick,G.P. and Goodman,H.M.
  TITLE     Characterization of the short isoform of the growth hormone
            receptor synthesized by rat adipocytes
  JOURNAL   Endocrinology 131 (6), 3083-3090 (1992)
   PUBMED   1446642
REFERENCE   7  (residues 1 to 638)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Godowski,P.J., Leung,D.W., Meacham,L.R., Galgani,J.P., Hellmiss,R.,
            Keret,R., Rotwein,P.S., Parks,J.S., Laron,Z. and Wood,W.I.
  TITLE     Characterization of the human growth hormone receptor gene and
            demonstration of a partial gene deletion in two patients with
            Laron-type dwarfism
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8083-8087 (1989)
   PUBMED   2813379
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Baumbach,W.R., Horner,D.L. and Logan,J.S.
  TITLE     The growth hormone-binding protein in rat serum is an alternatively
            spliced form of the rat growth hormone receptor
  JOURNAL   Genes Dev 3 (8), 1199-1205 (1989)
   PUBMED   2792761
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Mathews,L.S., Enberg,B. and Norstedt,G.
  TITLE     Regulation of rat growth hormone receptor gene expression
  JOURNAL   J Biol Chem 264 (17), 9905-9910 (1989)
   PUBMED   2722883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J04811.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..638
                     /product="growth hormone receptor isoform 1 precursor"
                     /note="growth hormone receptor/binding protein; GH
                     receptor; somatotropin receptor; growth hormone receptor
                     variant d5-6"
                     /calculated_mol_wt=69187
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=2068
     mat_peptide     19..638
                     /product="Growth hormone receptor. /id=PRO_0000010969"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=69187
     Region          49..127
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          149..250
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(149,222,239)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          240..244
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000250|UniProtKB:P10912"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            order(240..241,243..244)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            266..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          295..380
                     /region_name="Required for JAK2 binding.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          298..306
                     /region_name="Box 1 motif.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          317..616
                     /region_name="GHBP"
                     /note="Growth hormone receptor binding; pfam12772"
                     /db_xref="CDD:463696"
     Region          341..350
                     /region_name="UbE motif.
                     /evidence=ECO:0000305|PubMed:7615519"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          357..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     CDS             1..638
                     /gene="Ghr"
                     /gene_synonym="GHR/BP"
                     /coded_by="NM_017094.3:105..2021"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25235"
                     /db_xref="RGD:2687"
ORIGIN      
        1 mdlwrvfltl alavssdmfp gsgatpatlg kaspvlqrin pslresssgk prftkcrspe
       61 letfscywte gddhnlkvpg siqlyyarri ahewtpewke cpdyvsagan scyfnssyts
      121 iwipyciklt tngdlldekc ftvdeivqpd ppiglnwtll nislpgirgd iqvswqppps
      181 advlkgwiil eyeiqykevn etkwktmspi wstsvplysl rldkehevrv rsrqrsfeky
      241 sefsevlrvt fpqmdtlaac eedfrfpwfl iiifgifgva vmlfvvifsk qqrikmlilp
      301 pvpvpkikgi dpdllkegkl eevntilgih dnykpdfynd dswvefield iddadektee
      361 sdtdrllsdd qeksagilga kdddsgrtsc ydpdildtdf htsdmcdgts efaqpqklka
      421 eadllcldqk nlknspydas lgslhpsitl tmedkpqpll gsetesthql pstpmsspvs
      481 lanidfyaqv sditpaggvv lspgqkikag laqgntqlev aapcqenysm nsayfcesda
      541 kkciaaaphm eattcvkpsf nqediyitte sltttarmse tadtapdaep vpdyttvhtv
      601 ksprglilna talplpdkkk flsscgyvst dqlnkimq
//
LOCUS       NP_001424758             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424758
VERSION     NP_001424758.1
DBSOURCE    REFSEQ: accession NM_001437829.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.1798370.1,
                                           SRR21887623.1798373.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437829.1:318..2168"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001424734             536 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424734 XP_063144728
VERSION     NP_001424734.1
DBSOURCE    REFSEQ: accession NM_001437805.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144728.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..536
                     /product="phosphatase and actin regulator 2 isoform 4"
                     /calculated_mol_wt=57938
     Region          379..404
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          418..442
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          455..480
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..536
                     /gene="Phactr2"
                     /coded_by="NM_001437805.1:569..2179"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mihigeeatq eenvgkpeeg nvsvcekgpp reeqaeekte nseihsetpa alpptvpskp
       61 kpkpkpkkss vppkggttsg ashkgdevpp trknvkapsk qapvpppkpt srntsreaag
      121 sshpkkttgs kassspsass tsshprgpke sltgkagavg ttrgkkkisk qpaaaasrls
      181 pntvtsetss lkgelsdtgv eslkpeetva gaeeeatgkp kavvvalppv tvppsspalp
      241 lppedpctia ldtpmvlvsd gptlpisale tsplpgteep anrttpysst glggsreqak
      301 cfttkdgpgk agpqlltpgq mgdslesfsa pedeapreyq andsdsdgpi lytddddeed
      361 ddddstgesa laskirrrdt laiklgnrps kkeledknil qrtseeerqe lrqqigtklv
      421 rrlsqrptte eleqrnilkq kneeeeqeak melkrrlsrk lslrptvael qarrilrfne
      481 yvevtdspdy drradkpwar ltpadkaair kelnefkste mevheesrqf trfhrp
//
LOCUS       NP_001424735             516 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424735 XP_063144730
VERSION     NP_001424735.1
DBSOURCE    REFSEQ: accession NM_001437806.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144730.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.862588.1,
                                           SRR26360186.2486458.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..516
                     /product="phosphatase and actin regulator 2 isoform 5"
                     /calculated_mol_wt=56276
     Region          73..94
                     /region_name="RPEL"
                     /note="RPEL repeat; pfam02755"
                     /db_xref="CDD:460677"
     Region          359..384
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          398..422
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          435..460
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..516
                     /gene="Phactr2"
                     /coded_by="NM_001437806.1:181..1731"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mgqtsvsals pqpgsvdgld kasiansdgp pagsqtppfk rkgklstigk ifkpwkwrkk
       61 ktsdkfrets avlerkistr qsreelirrg llkelpdqag sshpkkttgs kassspsass
      121 tsshprgpke sltgkagavg ttrgkkkisk qpaaaasrls pntvtsetss lkgelsdtgv
      181 eslkpeetva gaeeeatgkp kavvvalppv tvppsspalp lppedpctia ldtpmvlvsd
      241 gptlpisale tsplpgteep anrttpysst glggsreqak cfttkdgpgk agpqlltpgq
      301 mgdslesfsa pedeapreyq andsdsdgpi lytddddeed ddddstgesa laskirrrdt
      361 laiklgnrps kkeledknil qrtseeerqe lrqqigtklv rrlsqrptte eleqrnilkq
      421 kneeeeqeak melkrrlsrk lslrptvael qarrilrfne yvevtdspdy drradkpwar
      481 ltpadkaair kelnefkste mevheesrqf trfhrp
//
LOCUS       NP_001424769             498 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424769 XP_063137353
VERSION     NP_001424769.1
DBSOURCE    REFSEQ: accession NM_001437840.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063137353.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2312438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..498
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 9"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=56164
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          366..493
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..498
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437840.1:417..1913"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpales tessnttied
      361 edvkarkqei ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe
      421 nalpkinkpi htiilnphvh lvgddaacia yirltqymdg ngmpktmqse etrvwhrrdg
      481 kwqnihfhrs gsptvpin
//
LOCUS       NP_001424737             457 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424737
VERSION     NP_001424737.1
DBSOURCE    REFSEQ: accession NM_001437808.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..457
                     /product="phosphatase and actin regulator 2 isoform 7"
                     /calculated_mol_wt=49722
     Region          300..325
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          339..363
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          376..401
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..457
                     /gene="Phactr2"
                     /coded_by="NM_001437808.1:569..1942"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mihigeeatq eenvgkpeeg nvsvcekgpp reeqaeekta gsshpkkttg skassspsas
       61 stsshprgpk esltgkagav gttrgkkkis kqpaaaasrl spntvtsets slkgelsdtg
      121 veslkpeetv agaeeeatgk pkavvvalpp vtvppsspal plppedpcti aldtpmvlvs
      181 dgptlpisal etsplpgtee panrttpyss tglggsreqa kcfttkdgpg kagpqlltpg
      241 qmgdslesfs apedeaprey qandsdsdgp ilytddddee dddddstges alaskirrrd
      301 tlaiklgnrp skkeledkni lqrtseeerq elrqqigtkl vrrlsqrptt eeleqrnilk
      361 qkneeeeqea kmelkrrlsr klslrptvae lqarrilrfn eyvevtdspd ydrradkpwa
      421 rltpadkaai rkelnefkst emevheesrq ftrfhrp
//
LOCUS       NP_001424791             516 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 13 [Rattus norvegicus].
ACCESSION   NP_001424791 XP_008768720
VERSION     NP_001424791.1
DBSOURCE    REFSEQ: accession NM_001437862.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 516)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768720.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.44590.1,
                                           SRR26643285.39724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..516
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 13"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=57666
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          384..511
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..516
                     /gene="Camk2g"
                     /coded_by="NM_001437862.1:70..1620"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kepqttvvhn
      361 atdgikgste scnttteded lkvrkqeiik iteqlieain ngdfeaytki cdpgltsfep
      421 ealgnlvegm dfhkfyfenl lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg
      481 rprtsqseet rvwhrrdgkw lnvhyhcsga paaplq
//
LOCUS       NP_001424783             556 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424783 XP_008768713
VERSION     NP_001424783.1
DBSOURCE    REFSEQ: accession NM_001437854.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 556)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768713.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2023173.1,
                                           SRR26643298.56237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..556
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 4"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=62070
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          424..551
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..556
                     /gene="Camk2g"
                     /coded_by="NM_001437854.1:70..1740"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknslv spaqepaplq tamepqttvv
      361 hnatdgikgs tescnttted edlkaaplrt gngslvpegr sprdrtapsa gmqpqpslcs
      421 samrkqeiik iteqlieain ngdfeaytki cdpgltsfep ealgnlvegm dfhkfyfenl
      481 lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg rprtsqseet rvwhrrdgkw
      541 lnvhyhcsga paaplq
//
LOCUS       NP_001424766             512 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424766 XP_063137351
VERSION     NP_001424766.1
DBSOURCE    REFSEQ: accession NM_001437837.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063137351.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.992584.1,
                                           SRR26360194.249395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..512
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 6"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=57695
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          337..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..512
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437837.1:417..1955"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalpki nkpihtiiln phvhlvgdda aciayirltq ymdgngmpkt
      481 mqseetrvwh rrdgkwqnih fhrsgsptvp in
//
LOCUS       NP_037247                366 aa            linear   ROD 10-APR-2025
DEFINITION  prostaglandin F2-alpha receptor [Rattus norvegicus].
ACCESSION   NP_037247 XP_579372
VERSION     NP_037247.1
DBSOURCE    REFSEQ: accession NM_013115.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Fukuda,M., Aoki,T., Manabe,T., Maekawa,A., Shirakawa,T.,
            Kataoka,H., Takagi,Y., Miyamoto,S. and Narumiya,S.
  TITLE     Exacerbation of intracranial aneurysm and aortic dissection in
            hypertensive rat treated with the prostaglandin F-receptor
            antagonist AS604872
  JOURNAL   J Pharmacol Sci 126 (3), 230-242 (2014)
   PUBMED   25341845
  REMARK    GeneRIF: Prostaglandin F-receptor antagonist AS604872 exacerbates
            vascular inflammation in hypertensive animals, facilitating
            intracranial aneurysm formation and aortic dissection.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Anadol,E., Kanca,H., Yar,A.S., Helvacioglu,F., Menevse,S.,
            Calguner,E. and Erdogan,D.
  TITLE     Prostaglandin F receptor expression in intrauterine tissues of
            pregnant rats
  JOURNAL   J Vet Sci 15 (1), 125-131 (2014)
   PUBMED   24136214
  REMARK    GeneRIF: There was an increase rat prostaglandin F receptor
            expression in rat uterus with advancing gestation, a marked
            elevation of expression at term, and a concominant decrease during
            the postpartum period.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Ueno,T. and Fujimori,K.
  TITLE     Novel suppression mechanism operating in early phase of
            adipogenesis by positive feedback loop for enhancement of
            cyclooxygenase-2 expression through prostaglandin F2alpha receptor
            mediated activation of MEK/ERK-CREB cascade
  JOURNAL   FEBS J 278 (16), 2901-2912 (2011)
   PUBMED   21668646
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Suzuki-Yamamoto,T., Toida,K., Sugimoto,Y. and Ishimura,K.
  TITLE     Colocalization of prostaglandin F(2alpha) receptor FP and
            prostaglandin F synthase-I in the spinal cord
  JOURNAL   J Lipid Res 50 (10), 1996-2003 (2009)
   PUBMED   19429887
  REMARK    GeneRIF: Data found that FP localizes in neuronal somata and
            dendrites but not in ependymal cells, tanycytes, or endothelial
            cells. Immunohistochemical analysis of serial sections showed the
            colocalization of FP and PGFS I.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Almirza,W.H., Dernison,M.M., Peters,P.H., van Zoelen,E.J. and
            Theuvenet,A.P.
  TITLE     Role of the prostanoid FP receptor in action potential generation
            and phenotypic transformation of NRK fibroblasts
  JOURNAL   Cell Signal 20 (11), 2022-2029 (2008)
   PUBMED   18703136
  REMARK    GeneRIF: Activity of PGF(2alpha) by putative pacemaker cells
            underlies the generation of calcium action potentials in normal rat
            kidney monolayers.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Yonekura,H., Sakurai,S., Liu,X., Migita,H., Wang,H., Yamagishi,S.,
            Nomura,M., Abedin,M.J., Unoki,H., Yamamoto,Y. and Yamamoto,H.
  TITLE     Placenta growth factor and vascular endothelial growth factor B and
            C expression in microvascular endothelial cells and pericytes.
            Implication in autocrine and paracrine regulation of angiogenesis
  JOURNAL   J Biol Chem 274 (49), 35172-35178 (1999)
   PUBMED   10575000
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Olofsson,J.I., Leung,C.H., Bjurulf,E., Ohno,T., Selstam,G., Peng,C.
            and Leung,P.C.
  TITLE     Characterization and regulation of a mRNA encoding the
            prostaglandin F2alpha receptor in the rat ovary
  JOURNAL   Mol Cell Endocrinol 123 (1), 45-52 (1996)
   PUBMED   8912810
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Orlicky,D.J.
  TITLE     Negative regulatory activity of a prostaglandin F2 alpha receptor
            associated protein (FPRP)
  JOURNAL   Prostaglandins Leukot Essent Fatty Acids 54 (4), 247-259 (1996)
   PUBMED   8804121
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Lake,S., Gullberg,H., Wahlqvist,J., Sjogren,A.M., Kinhult,A.,
            Lind,P., Hellstrom-Lindahl,E. and Stjernschantz,J.
  TITLE     Cloning of the rat and human prostaglandin F2 alpha receptors and
            the expression of the rat prostaglandin F2 alpha receptor
  JOURNAL   FEBS Lett 355 (3), 317-325 (1994)
   PUBMED   7988697
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Kitanaka,J., Hasimoto,H., Sugimoto,Y., Negishi,M., Aino,H.,
            Gotoh,M., Ichikawa,A. and Baba,A.
  TITLE     Cloning and expression of a cDNA for rat prostaglandin F2 alpha
            receptor
  JOURNAL   Prostaglandins 48 (1), 31-41 (1994)
   PUBMED   7972878
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579372.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D28581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN16093047
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..366
                     /product="prostaglandin F2-alpha receptor"
                     /note="PGF receptor; prostanoid FP receptor; PGF2-alpha
                     receptor"
                     /calculated_mol_wt=40524
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43118.1)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43118.1)"
     Region          27..316
                     /region_name="7tmA_FP"
                     /note="prostaglandin F2-alpha receptor, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15145"
                     /db_xref="CDD:320273"
     Region          28..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320273"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          66..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320273"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Site            order(88,91..92,108..113,115..116,119,164,166..170,197,
                     200..202,204..206,208..209,262,265..266,268..269,272,
                     282..283,285..287,290,293..294)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320273"
     Region          108..138
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320273"
     Site            110..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          150..172
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320273"
     Site            153..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          197..226
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320273"
     Site            199..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          242..272
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320273"
     Site            251..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          283..308
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320273"
     Site            286..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     CDS             1..366
                     /gene="Ptgfr"
                     /gene_synonym="PF2AR"
                     /coded_by="NM_013115.3:134..1234"
                     /db_xref="GeneID:25652"
                     /db_xref="RGD:3436"
ORIGIN      
        1 msinsskqpa ssaagliant tcqtenrlsv ffsiifmtvg ivsnslaiai lmkayqrfrr
       61 kskasfllla sglvitdffg hlinggiavf vyasdkdwir fdqsnilcsv fgismvfsgl
      121 cplflgstma iercigvtnp lfhstkitsk hvkmilsgvc mfavfvallp ilghrdyqiq
      181 asrtwcfynt ehiedwedrf yllffsslgl lalgisfscn avtgvtllrv kfrsqqhrqg
      241 rshhlemviq llaimcvscv cwspflvtma niaingnnsp vtcettlfal rmatwnqild
      301 pwvyillrka vlrnlyklas rccgvniisl hiwelssikn slkvaaises paaekenqqa
      361 sseagl
//
LOCUS       NP_001424770             498 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 10 [Rattus norvegicus].
ACCESSION   NP_001424770 XP_038957624
VERSION     NP_001424770.1
DBSOURCE    REFSEQ: accession NM_001437841.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038957624.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1010564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..498
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 10"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=56163
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          366..493
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..498
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437841.1:417..1913"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpales tessnttied
      361 edvkarkqei ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe
      421 nalpkinkpi htiilnphvh lvgddaacia yirltqymdg ngmpktmqse etrvwhrrdg
      481 kwqnihfhrs gsptvpin
//
LOCUS       NP_001424776             588 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424776 XP_008768708
VERSION     NP_001424776.1
DBSOURCE    REFSEQ: accession NM_001437847.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 588)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768708.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.56231.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..588
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=65147
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          456..583
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..588
                     /gene="Camk2g"
                     /coded_by="NM_001437847.1:70..1836"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik gstescnttt ededlkaapl
      421 rtgngslvpe grsprdrtap sagmqpqpsl cssamrkqei ikiteqliea inngdfeayt
      481 kicdpgltsf epealgnlve gmdfhkfyfe nllsknskpi httilnphvh vigedaacia
      541 yirltqyidg qgrprtsqse etrvwhrrdg kwlnvhyhcs gapaaplq
//
LOCUS       NP_001012066             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001012066 XP_218558
VERSION     NP_001012066.1
DBSOURCE    REFSEQ: accession NM_001012066.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 11, 2005 this sequence version replaced XP_218558.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079120.1, SRR26643429.1931.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001012066.2:671..2521"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001424765             519 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424765 XP_017446099
VERSION     NP_001424765.1
DBSOURCE    REFSEQ: accession NM_001437836.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017446099.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1535975.1,
                                           SRR21887623.3142198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..519
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 5"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=58418
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          366..493
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..519
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437836.1:417..1976"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpales tessnttied
      361 edvkarkqei ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe
      421 nalpkinkpi htiilnphvh lvgddaacia yirltqymdg ngmpktmqse etrvwhrrdg
      481 kwqnihfhrs gsptvpikpp cipngkenfs ggtslwqni
//
LOCUS       NP_001041378             450 aa            linear   ROD 10-APR-2025
DEFINITION  sulfide:quinone oxidoreductase, mitochondrial isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001041378 XP_001077275 XP_001077299 XP_001077317 XP_001077335
            XP_342607
VERSION     NP_001041378.2
DBSOURCE    REFSEQ: accession NM_001047913.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Augustyn,K.D., Jackson,M.R. and Jorns,M.S.
  TITLE     Use of Tissue Metabolite Analysis and Enzyme Kinetics To
            Discriminate between Alternate Pathways for Hydrogen Sulfide
            Metabolism
  JOURNAL   Biochemistry 56 (7), 986-996 (2017)
   PUBMED   28107627
  REMARK    GeneRIF: The role of Sqor in hydrogen sulfide metabolism in the
            heart and liver
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Ackermann,M., Kubitza,M., Hauska,G. and Pina,A.L.
  TITLE     The vertebrate homologue of sulfide-quinone reductase in mammalian
            mitochondria
  JOURNAL   Cell Tissue Res 358 (3), 779-792 (2014)
   PUBMED   25130143
  REMARK    GeneRIF: The present report demonstrates the presence and specific
            localization of SQRDL in various mammalian tissues.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jackson,M.R., Melideo,S.L. and Jorns,M.S.
  TITLE     Human sulfide:quinone oxidoreductase catalyzes the first step in
            hydrogen sulfide metabolism and produces a sulfane sulfur
            metabolite
  JOURNAL   Biochemistry 51 (34), 6804-6815 (2012)
   PUBMED   22852582
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Ackermann,M., Kubitza,M., Maier,K., Brawanski,A., Hauska,G. and
            Pina,A.L.
  TITLE     The vertebrate homolog of sulfide-quinone reductase is expressed in
            mitochondria of neuronal tissues
  JOURNAL   Neuroscience 199, 1-12 (2011)
   PUBMED   22067608
  REMARK    GeneRIF: we demonstrated that the SQRDL protein is expressed in
            neurons, oligodendrocytes, and endothelial cells
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 21, 2008 this sequence version replaced NP_001041378.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158559.1, SRR26643293.18541.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..450
                     /product="sulfide:quinone oxidoreductase, mitochondrial
                     isoform 1"
                     /EC_number="1.8.5.8"
                     /note="sulfide:quinone oxidoreductase, mitochondrial"
                     /calculated_mol_wt=50071
     Region          71..389
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     CDS             1..450
                     /gene="Sqor"
                     /gene_synonym="Cc2-17; Sqrdl"
                     /coded_by="NM_001047913.3:51..1403"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:691966"
                     /db_xref="RGD:1564504"
ORIGIN      
        1 maplvavvss prarlfacfl rlgtqqagpl qlhtgaccta knhyevlvlg ggsggitmat
       61 rmkrrvgaen vaivepserh fyqpiwtlvg agakelsssd rstlsvipsg vqwiqdrvae
      121 lnpdqncirt dngkeisyry liialgiqld yekikglpeg faypkigsny svktvektwk
      181 alqdfkegna lftfpntpvk cagapqkimy lseayfrktg krskaniifn talgtifgvk
      241 kyadalqeii rernvsvnyk hnlievradk qeavfenldk pgethvihye mlhvtppmss
      301 pdvlkrspva dsagwvdvdk etlqhkkypn vfgigdctnl ptsktaaava aqsgildrti
      361 slimknqtpt kkydgytscp lvtgynrvil aefdytaqpl etfpfdqske rismylmkad
      421 mmpflywnmm lrgywggpaf lrklfhlgls
//
LOCUS       NP_001424790             516 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 12 [Rattus norvegicus].
ACCESSION   NP_001424790 XP_063130007
VERSION     NP_001424790.1
DBSOURCE    REFSEQ: accession NM_001437861.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 516)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063130007.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1944582.1,
                                           SRR26360194.792732.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..516
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 12"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=57616
     Region          3..263
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(57,59,95..96,98,100,120,135..139,141)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(116..126,129..139)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(254,256..263)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          384..511
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..516
                     /gene="Camk2g"
                     /coded_by="NM_001437861.1:185..1735"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mhrklnaegw gpedhqkler earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe
       61 divareyyse adashcihqi lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl
      121 aievqgeqqa wfgfagtpgy lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh
      181 klyqqikaga ydfpspewdt vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas
      241 mmhrqetvec lrkfnarrkl kgailttmlv srnfsaaksl lnkksdggvk pqsnnknslv
      301 spaqepaplq tamepqttvv hnatdgikgs tescnttted edlkaaplrt gngslvpegr
      361 sprdrtapsa gmqpqpslcs samrkqeiik iteqlieain ngdfeaytki cdpgltsfep
      421 ealgnlvegm dfhkfyfenl lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg
      481 rprtsqseet rvwhrrdgkw lnvhyhcsga paaplq
//
LOCUS       NP_001424782             567 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424782 XP_008768711
VERSION     NP_001424782.1
DBSOURCE    REFSEQ: accession NM_001437853.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768711.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.63496.1,
                                           SRR26643298.56233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..567
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 3"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=63311
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          435..562
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..567
                     /gene="Camk2g"
                     /coded_by="NM_001437853.1:70..1773"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mpqsnnknsl vspaqepapl
      361 qtamepqttv vhnatdgikg stescnttte dedlkaaplr tgngslvpeg rsprdrtaps
      421 agmqpqpslc ssamrkqeii kiteqlieai nngdfeaytk icdpgltsfe pealgnlveg
      481 mdfhkfyfen llsknskpih ttilnphvhv igedaaciay irltqyidgq grprtsqsee
      541 trvwhrrdgk wlnvhyhcsg apaaplq
//
LOCUS       NP_277020                332 aa            linear   ROD 10-APR-2025
DEFINITION  PRKC apoptosis WT1 regulator protein [Rattus norvegicus].
ACCESSION   NP_277020 XP_038935785
VERSION     NP_277020.2
DBSOURCE    REFSEQ: accession NM_033485.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Hao,Y., Niu,H., An,S., Wang,M. and Wang,Z.
  TITLE     Downregulation of iNOS, IL-1beta, and P2X7 Expression in Mast Cells
            via Activation of PAR4 Contributes to the Inhibition of Visceral
            Hyperalgesia in Rats
  JOURNAL   J Immunol Res 2018, 3256908 (2018)
   PUBMED   29854833
  REMARK    GeneRIF: this study shows that downregulation of iNOS, IL-1beta,
            and P2X7 expression in mast cells via activation of PAR4
            contributes to the Inhibition of visceral hyperalgesia
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Du,W.W., Li,X., Li,T., Li,H., Khorshidi,A., Liu,F. and Yang,B.B.
  TITLE     The microRNA miR-17-3p inhibits mouse cardiac fibroblast senescence
            by targeting Par4
  JOURNAL   J Cell Sci 128 (2), 293-304 (2015)
   PUBMED   25472717
REFERENCE   3  (residues 1 to 332)
  AUTHORS   de Thonel,A., Hazoume,A., Kochin,V., Isoniemi,K., Jego,G.,
            Fourmaux,E., Hammann,A., Mjahed,H., Filhol,O., Micheau,O.,
            Rocchi,P., Mezger,V., Eriksson,J.E., Rangnekar,V.M. and Garrido,C.
  TITLE     Regulation of the proapoptotic functions of prostate apoptosis
            response-4 (Par-4) by casein kinase 2 in prostate cancer cells
  JOURNAL   Cell Death Dis 5 (1), e1016 (2014)
   PUBMED   24457960
  REMARK    GeneRIF: Phosphorylation by CK2 impairs Par-4 proapoptotic
            functions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Wang,Z., Chen,D., Zhang,R., An,S., Zhang,Z. and Ma,Q.
  TITLE     Interleukin-1beta increased the expression of protease-activated
            receptor 4 mRNA and protein in dorsal root ganglion neurons
  JOURNAL   Neurochem Res 38 (9), 1895-1903 (2013)
   PUBMED   23775412
REFERENCE   5  (residues 1 to 332)
  AUTHORS   MacDonald,J.A., Moffat,L.D., Al-Ghabkari,A., Sutherland,C. and
            Walsh,M.P.
  TITLE     Prostate-apoptosis response-4 phosphorylation in vascular smooth
            muscle
  JOURNAL   Arch Biochem Biophys 535 (1), 84-90 (2013)
   PUBMED   23219599
  REMARK    GeneRIF: Par-4 binding does not block MYPT1 phosphorylation in rat
            caudal arterial smooth muscle.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Duan,W., Rangnekar,V.M. and Mattson,M.P.
  TITLE     Prostate apoptosis response-4 production in synaptic compartments
            following apoptotic and excitotoxic insults: evidence for a pivotal
            role in mitochondrial dysfunction and neuronal degeneration
  JOURNAL   J Neurochem 72 (6), 2312-2322 (1999)
   PUBMED   10349840
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Guo,Q., Fu,W., Xie,J., Luo,H., Sells,S.F., Geddes,J.W., Bondada,V.,
            Rangnekar,V.M. and Mattson,M.P.
  TITLE     Par-4 is a mediator of neuronal degeneration associated with the
            pathogenesis of Alzheimer disease
  JOURNAL   Nat Med 4 (8), 957-962 (1998)
   PUBMED   9701251
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Boghaert,E.R., Sells,S.F., Walid,A.J., Malone,P., Williams,N.M.,
            Weinstein,M.H., Strange,R. and Rangnekar,V.M.
  TITLE     Immunohistochemical analysis of the proapoptotic protein Par-4 in
            normal rat tissues
  JOURNAL   Cell Growth Differ 8 (8), 881-890 (1997)
   PUBMED   9269897
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Johnstone,R.W., See,R.H., Sells,S.F., Wang,J., Muthukkumar,S.,
            Englert,C., Haber,D.A., Licht,J.D., Sugrue,S.P., Roberts,T.,
            Rangnekar,V.M. and Shi,Y.
  TITLE     A novel repressor, par-4, modulates transcription and growth
            suppression functions of the Wilms' tumor suppressor WT1
  JOURNAL   Mol Cell Biol 16 (12), 6945-6956 (1996)
   PUBMED   8943350
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Sells,S.F., Wood,D.P. Jr., Joshi-Barve,S.S., Muthukumar,S.,
            Jacob,R.J., Crist,S.A., Humphreys,S. and Rangnekar,V.M.
  TITLE     Commonality of the gene programs induced by effectors of apoptosis
            in androgen-dependent and -independent prostate cells
  JOURNAL   Cell Growth Differ 5 (4), 457-466 (1994)
   PUBMED   8043520
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 10, 2025 this sequence version replaced
            XP_038935785.1, NP_277020.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.30560.1,
                                           SRR26643291.20200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..332
                     /product="PRKC apoptosis WT1 regulator protein"
                     /note="prostate apoptosis response 4 protein;
                     transcriptional repressor Par-4-like protein PAWR; par-4
                     induced by effectors of apoptosis; Prostate apoptosis
                     response protein 4; PRKC, apoptosis, WT1, regulator"
                     /calculated_mol_wt=35722
     Region          1..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          61..65
                     /region_name="B30.2/SPRY domain-binding motif.
                     /evidence=ECO:0000250|UniProtKB:Q96IZ0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          137..195
                     /region_name="Selective for apoptosis induction in cancer
                     cells (SAC)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          137..153
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:15657440; propagated from
                     UniProtKB/Swiss-Prot (Q62627.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IZ0; propagated from
                     UniProtKB/Swiss-Prot (Q62627.1)"
     Region          258..325
                     /region_name="Atg16_CCD"
                     /note="Coiled-coiled domain of autophagy-related 16
                     (Atg16) family proteins; cl46300"
                     /db_xref="CDD:480640"
     Site            order(260..261,263..264,267,270..271,274..275,277..278,
                     281..282,285,288..289,292,295..296,298..299,302,305..306,
                     309..310,312..313,316..317,319..320,323..324)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:439196"
     Region          292..332
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     CDS             1..332
                     /gene="Pawr"
                     /gene_synonym="Par-4; Par4"
                     /coded_by="NM_033485.4:181..1179"
                     /db_xref="GeneID:64513"
                     /db_xref="RGD:69065"
ORIGIN      
        1 matggyrssg sttdfleewk akrekmrakq npvgpgssgg dpaakspagp laqttaagts
       61 elnhgpagaa apaapgpgal ncahgssalp rgapgsrrpe decpiaagaa gapasrgdee
      121 epdsapekgr ssgpsarkgk gqiekrklre krrstgvvni paaecldeye ddeagqkerk
      181 redaitqqnt iqneaaslpd pgtsylpqdp srtvpgryks ttsapeeeil nryprtdrsg
      241 fsrhnrdtsa panfassstl ekriedleke vlrerqenlr ltrlmqdkee migklkeeid
      301 llnrdlddme deneqlkqen ktllkvvgql tr
//
LOCUS       NP_001424756             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424756 XP_038968225
VERSION     NP_001424756.1
DBSOURCE    REFSEQ: accession NM_001437827.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038968225.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.2168.1,
                                           SRR26643429.1934.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437827.1:201..2051"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001424789             518 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 11 [Rattus norvegicus].
ACCESSION   NP_001424789 XP_008768719
VERSION     NP_001424789.1
DBSOURCE    REFSEQ: accession NM_001437860.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 518)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768719.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.33853.1,
                                           SRR26643299.56076.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..518
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 11"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=58235
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          386..513
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..518
                     /gene="Camk2g"
                     /coded_by="NM_001437860.1:70..1626"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknslv spaqepaplq tamepqttvv
      361 hnatdgikgs tescnttted edlkvrkqei ikiteqliea inngdfeayt kicdpgltsf
      421 epealgnlve gmdfhkfyfe nllsknskpi httilnphvh vigedaacia yirltqyidg
      481 qgrprtsqse etrvwhrrdg kwlnvhyhcs gapaaplq
//
LOCUS       NP_001424785             544 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424785 XP_017455065
VERSION     NP_001424785.1
DBSOURCE    REFSEQ: accession NM_001437856.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 544)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 544)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 544)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 544)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 544)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 544)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017455065.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.957026.1,
                                           SRR26360194.341829.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..544
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 6"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=60907
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          412..539
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..544
                     /gene="Camk2g"
                     /coded_by="NM_001437856.1:70..1704"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mepqttvvhn atdgikgste
      361 scnttteded lkaaplrtgn gslvpegrsp rdrtapsagm qpqpslcssa mrkqeiikit
      421 eqlieainng dfeaytkicd pgltsfepea lgnlvegmdf hkfyfenlls knskpihtti
      481 lnphvhvige daaciayirl tqyidgqgrp rtsqseetrv whrrdgkwln vhyhcsgapa
      541 aplq
//
LOCUS       NP_001424763             532 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424763 XP_017446096
VERSION     NP_001424763.1
DBSOURCE    REFSEQ: accession NM_001437834.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017446096.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1422082.1,
                                           SRR26360176.737065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..532
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 3"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=59879
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            317
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          336..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          379..506
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     CDS             1..532
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437834.1:417..2015"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkinn kanvvtspke niptpalepq ttvihnpdgn
      361 kestessntt iededvkark qeiikvteql ieainngdfe aytkicdpgl tafepealgn
      421 lvegmdfhrf yfenalpkin kpihtiilnp hvhlvgddaa ciayirltqy mdgngmpktm
      481 qseetrvwhr rdgkwqnihf hrsgsptvpi kppcipngke nfsggtslwq ni
//
LOCUS       NP_001424733             558 aa            linear   ROD 10-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424733 XP_063144725
VERSION     NP_001424733.1
DBSOURCE    REFSEQ: accession NM_001437804.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144725.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1250329.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..558
                     /product="phosphatase and actin regulator 2 isoform 3"
                     /calculated_mol_wt=61071
     Region          62..83
                     /region_name="RPEL"
                     /note="RPEL repeat; pfam02755"
                     /db_xref="CDD:460677"
     Region          401..426
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          440..464
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          477..502
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     CDS             1..558
                     /gene="Phactr2"
                     /coded_by="NM_001437804.1:135..1811"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mdkavdgldk asiansdgpp agsqtppfkr kgklstigki fkpwkwrkkk tsdkfretsa
       61 vlerkistrq sreelirrgl lkelpdqdgd vtvnfensng hmihigeeat qeenvgkpee
      121 gnvsvcekgp preeqaeekt agsshpkktt gskassspsa sstsshprgp kesltgkaga
      181 vgttrgkkki skqpaaaasr lspntvtset sslkgelsdt gveslkpeet vagaeeeatg
      241 kpkavvvalp pvtvppsspa lplppedpct ialdtpmvlv sdgptlpisa letsplpgte
      301 epanrttpys stglggsreq akcfttkdgp gkagpqlltp gqmgdslesf sapedeapre
      361 yqandsdsdg pilytdddde edddddstge salaskirrr dtlaiklgnr pskkeledkn
      421 ilqrtseeer qelrqqigtk lvrrlsqrpt teeleqrnil kqkneeeeqe akmelkrrls
      481 rklslrptva elqarrilrf neyvevtdsp dydrradkpw arltpadkaa irkelnefks
      541 temevheesr qftrfhrp
//
LOCUS       NP_036762                310 aa            linear   ROD 10-APR-2025
DEFINITION  prolactin receptor isoform b precursor [Rattus norvegicus].
ACCESSION   NP_036762
VERSION     NP_036762.1
DBSOURCE    REFSEQ: accession NM_012630.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Ortiz-Perez,A., Limon-Morales,O., Rojas-Castaneda,J.C., Cerbon,M.
            and Picazo,O.
  TITLE     Prolactin prevents the kainic acid-induced neuronal loss in the rat
            hippocampus by inducing prolactin receptor and putatively
            increasing the VGLUT1 overexpression
  JOURNAL   Neurosci Lett 694, 116-123 (2019)
   PUBMED   30500398
  REMARK    GeneRIF: Study indicates that chronic prolactin administration
            before kainic acid induced damage induces hippocampal
            neuroprotection associated with prolactin receptor and VGLUT1
            overexpression.
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Vergara-Castaneda,E., Grattan,D.R., Pasantes-Morales,H.,
            Perez-Dominguez,M., Cabrera-Reyes,E.A., Morales,T. and Cerbon,M.
  TITLE     Prolactin mediates neuroprotection against excitotoxicity in
            primary cell cultures of hippocampal neurons via its receptor
  JOURNAL   Brain Res 1636, 193-199 (2016)
   PUBMED   26874070
  REMARK    GeneRIF: This study demonstrated that the Cultured neurons
            expressed mRNA for both PRL and its receptor (PRLR), and both PRL
            and PRLR expression levels changed after the excitotoxic insult.
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Rojas-Duran,F., Pascual-Mathey,L.I., Serrano,K., Aranda-Abreu,G.E.,
            Manzo,J., Soto-Cid,A.H. and Hernandez,M.E.
  TITLE     Correlation of prolactin levels and PRL-receptor expression with
            Stat and Mapk cell signaling in the prostate of long-term sexually
            active rats
  JOURNAL   Physiol Behav 138, 188-192 (2015)
   PUBMED   25446202
  REMARK    GeneRIF: Results showed that an active sexual life, with constant
            execution of sexual behavior, produces a sustained increase in
            serum PRL, prostate PRL receptors, and the pStat3 signaling pathway
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Arumugam,R., Fleenor,D. and Freemark,M.
  TITLE     Knockdown of prolactin receptors in a pancreatic beta cell line:
            effects on DNA synthesis, apoptosis, and gene expression
  JOURNAL   Endocrine 46 (3), 568-576 (2014)
   PUBMED   24114406
  REMARK    GeneRIF: PRLR signaling is required for DNA synthesis and survival
            of rat insulinoma cells
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Ali,S., Pellegrini,I. and Kelly,P.A.
  TITLE     A prolactin-dependent immune cell line (Nb2) expresses a mutant
            form of prolactin receptor
  JOURNAL   J Biol Chem 266 (30), 20110-20117 (1991)
   PUBMED   1718958
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Shirota,M., Banville,D., Ali,S., Jolicoeur,C., Boutin,J.M.,
            Edery,M., Djiane,J. and Kelly,P.A.
  TITLE     Expression of two forms of prolactin receptor in rat ovary and
            liver
  JOURNAL   Mol Endocrinol 4 (8), 1136-1143 (1990)
   PUBMED   2293022
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Zhang,R., Buczko,E., Tsai-Morris,C.H., Hu,Z.Z. and Dufau,M.L.
  TITLE     Isolation and characterization of two novel rat ovarian lactogen
            receptor cDNA species
  JOURNAL   Biochem Biophys Res Commun 168 (2), 415-422 (1990)
   PUBMED   2159291
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Boutin,J.M., Jolicoeur,C., Okamura,H., Gagnon,J., Edery,M.,
            Shirota,M., Banville,D., Dusanter-Fourt,I., Djiane,J. and
            Kelly,P.A.
  TITLE     Cloning and expression of the rat prolactin receptor, a member of
            the growth hormone/prolactin receptor gene family
  JOURNAL   Cell 53 (1), 69-77 (1988)
   PUBMED   2832068
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Herington,A.C., Harrison,D. and Graystone,J.
  TITLE     Hepatic binding of human and bovine growth hormones and ovine
            prolactin in the dwarf 'little' mouse
  JOURNAL   Endocrinology 112 (6), 2032-2038 (1983)
   PUBMED   6303755
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M19304.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..310
                     /product="prolactin receptor isoform b precursor"
                     /note="PRL-R; lactogen receptor"
                     /calculated_mol_wt=33370
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2000
     Region          19..115
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          122..219
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(122,193,208)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          210..214
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Site            order(210..211,213..214)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            230..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          262..270
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     CDS             1..310
                     /gene="Prlr"
                     /gene_synonym="RATPRLR"
                     /coded_by="NM_012630.3:184..1116"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:24684"
                     /db_xref="RGD:3407"
ORIGIN      
        1 mpsalafvll vlnisllkgq sppgkpeihk crspdketft cwwnpgtdgg lptnysltys
       61 kegekttyec pdyktsgpns cffskqytsi wkiyiitvna tnqmgssssd plyvdvtyiv
      121 epepprnltl evkqlkdkkt ylwvkwsppt itdvktgwft meyeirlkpe eaeeweihft
      181 ghqtqfkvfd lypgqkylvq trckpdhgyw srwsqessve mpndftlkdt tvwiivails
      241 aviclimvwa valkgysmmt cifppvpgpk ikgfdthlle tgspskykvd lylalpggfq
      301 kldnageldy
//
LOCUS       NP_001424811             366 aa            linear   ROD 10-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001424811 XP_063144256
VERSION     NP_001424811.1
DBSOURCE    REFSEQ: accession NM_001437882.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063144256.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.317170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001437882.1:635..1735"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424754             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424754 XP_038968232
VERSION     NP_001424754.1
DBSOURCE    REFSEQ: accession NM_001437825.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038968232.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.1936.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN06621351 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437825.1:117..1967"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001424813             366 aa            linear   ROD 10-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001424813 XP_006237901
VERSION     NP_001424813.1
DBSOURCE    REFSEQ: accession NM_001437884.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006237901.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.132988.1,
                                           SRR26360190.36827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001437884.1:456..1556"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424795             478 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 17 [Rattus norvegicus].
ACCESSION   NP_001424795 XP_063130010
VERSION     NP_001424795.1
DBSOURCE    REFSEQ: accession NM_001437866.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 478)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063130010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.610423.1,
                                           SRR26360194.480101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 17"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=53780
     Region          3..263
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(57,59,95..96,98,100,120,135..139,141)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(116..126,129..139)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(254,256..263)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..478
                     /gene="Camk2g"
                     /coded_by="NM_001437866.1:185..1621"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mhrklnaegw gpedhqkler earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe
       61 divareyyse adashcihqi lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl
      121 aievqgeqqa wfgfagtpgy lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh
      181 klyqqikaga ydfpspewdt vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas
      241 mmhrqetvec lrkfnarrkl kgailttmlv srnfsaaksl lnkksdggvk pqsnnknslv
      301 spaqepaplq tamepqttvv hnatdgikgs tescnttted edlkvrkqei ikiteqliea
      361 inngdfeayt kicdpgltsf epealgnlve gmdfhkfyfe nllsknskpi httilnphvh
      421 vigedaacia yirltqyidg qgrprtsqse etrvwhrrdg kwlnvhyhcs gapaaplq
//
LOCUS       NP_598289                527 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 10 [Rattus norvegicus].
ACCESSION   NP_598289
VERSION     NP_598289.1
DBSOURCE    REFSEQ: accession NM_133605.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 527)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J04063.1, SRR26360176.419335.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..527
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 10"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=58907
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:Q13555"
                     /note="propagated from UniProtKB/Swiss-Prot (P11730.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13555; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Region          294..316
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000250|UniProtKB:Q13555"
                     /note="propagated from UniProtKB/Swiss-Prot (P11730.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Region          344..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11730.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     Region          395..522
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11730.1)"
     CDS             1..527
                     /gene="Camk2g"
                     /coded_by="NM_133605.2:70..1653"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkvrkqeii kiteqlieai nngdfeaytk
      421 icdpgltsfe pealgnlveg mdfhkfyfen llsknskpih ttilnphvhv igedaaciay
      481 irltqyidgq grprtsqsee trvwhrrdgk wlnvhyhcsg apaaplq
//
LOCUS       NP_001424793             495 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 15 [Rattus norvegicus].
ACCESSION   NP_001424793 XP_008768721
VERSION     NP_001424793.1
DBSOURCE    REFSEQ: accession NM_001437864.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768721.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.56072.1,
                                           SRR26360194.1394486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..495
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 15"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=55830
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          363..490
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..495
                     /gene="Camk2g"
                     /coded_by="NM_001437864.1:70..1557"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna tdgikgstes cntttededl
      361 kvrkqeiiki teqlieainn gdfeaytkic dpgltsfepe algnlvegmd fhkfyfenll
      421 sknskpihtt ilnphvhvig edaaciayir ltqyidgqgr prtsqseetr vwhrrdgkwl
      481 nvhyhcsgap aaplq
//
LOCUS       NP_001424767             512 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424767 XP_017446102
VERSION     NP_001424767.1
DBSOURCE    REFSEQ: accession NM_001437838.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017446102.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1438710.1,
                                           SRR26360194.1177318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..512
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 7"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=57694
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          337..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..512
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_001437838.1:417..1955"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalpki nkpihtiiln phvhlvgdda aciayirltq ymdgngmpkt
      481 mqseetrvwh rrdgkwqnih fhrsgsptvp in
//
LOCUS       NP_001424755             616 aa            linear   ROD 10-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424755
VERSION     NP_001424755.1
DBSOURCE    REFSEQ: accession NM_001437826.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.1740.1,
                                           SRR26360172.1433322.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437826.1:973..2823"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001424796             455 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 18 [Rattus norvegicus].
ACCESSION   NP_001424796 XP_063130012
VERSION     NP_001424796.1
DBSOURCE    REFSEQ: accession NM_001437867.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063130012.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.91706.1,
                                           SRR26360194.2136284.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..455
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 18"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=51376
     Region          3..263
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(57,59,95..96,98,100,120,135..139,141)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(116..126,129..139)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(254,256..263)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          323..450
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..455
                     /gene="Camk2g"
                     /coded_by="NM_001437867.1:185..1552"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mhrklnaegw gpedhqkler earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe
       61 divareyyse adashcihqi lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl
      121 aievqgeqqa wfgfagtpgy lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh
      181 klyqqikaga ydfpspewdt vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas
      241 mmhrqetvec lrkfnarrkl kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna
      301 tdgikgstes cntttededl kvrkqeiiki teqlieainn gdfeaytkic dpgltsfepe
      361 algnlvegmd fhkfyfenll sknskpihtt ilnphvhvig edaaciayir ltqyidgqgr
      421 prtsqseetr vwhrrdgkwl nvhyhcsgap aaplq
//
LOCUS       NP_067722                884 aa            linear   ROD 10-APR-2025
DEFINITION  rap guanine nucleotide exchange factor 3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_067722
VERSION     NP_067722.2
DBSOURCE    REFSEQ: accession NM_021690.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Boileve,A., Romito,O., Hof,T., Levallois,A., Brard,L., d'Hers,S.,
            Fouchet,A., Simard,C., Guinamard,R., Brette,F. and Salle,L.
  TITLE     EPAC1 and 2 inhibit K+ currents via PLC/PKC and NOS/PKG pathways in
            rat ventricular cardiomyocytes
  JOURNAL   Am J Physiol Cell Physiol 327 (3), C557-C570 (2024)
   PUBMED   38985989
  REMARK    GeneRIF: EPAC1 and 2 inhibit K[+] currents via PLC/PKC and NOS/PKG
            pathways in rat ventricular cardiomyocytes.
REFERENCE   2  (residues 1 to 884)
  AUTHORS   Huang,S., Shi,C., Liu,F., Si,Y., Shen,D., Yang,L., Gao,Y. and
            Liao,Y.
  TITLE     Activation of Epac in the BLA disrupts reconsolidation and
            attenuates heroin-seeking behaviour
  JOURNAL   Addict Biol 28 (10), e13330 (2023)
   PUBMED   37753572
  REMARK    GeneRIF: Activation of Epac in the BLA disrupts reconsolidation and
            attenuates heroin-seeking behaviour.
REFERENCE   3  (residues 1 to 884)
  AUTHORS   Sitzia,C., Vianello,E., Dozio,E., Kalousova,M., Zima,T.,
            Brizzola,S., Roccabianca,P., Tedeschi,G., Lamont,J., Tacchini,L.
            and Corsi-Romanelli,M.M.
  TITLE     Unveiling IL-33/ST2 Pathway Unbalance in Cardiac Remodeling Due to
            Obesity in Zucker Fatty Rats
  JOURNAL   Int J Mol Sci 24 (3), 1991 (2023)
   PUBMED   36768322
  REMARK    GeneRIF: Unveiling IL-33/ST2 Pathway Unbalance in Cardiac
            Remodeling Due to Obesity in Zucker Fatty Rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 884)
  AUTHORS   Huang,S.T., Chen,B.B., Song,Z.J., Tang,H.L., Hua,R. and Zhang,Y.M.
  TITLE     Unraveling the role of Epac1-SOCS3 signaling in the development of
            neonatal-CRD-induced visceral hypersensitivity in rats
  JOURNAL   CNS Neurosci Ther 28 (9), 1393-1408 (2022)
   PUBMED   35702948
  REMARK    GeneRIF: Unraveling the role of Epac1-SOCS3 signaling in the
            development of neonatal-CRD-induced visceral hypersensitivity in
            rats.
REFERENCE   5  (residues 1 to 884)
  AUTHORS   Wang,X., Zhang,Y., Yang,Y., Zhang,W., Luo,L., Han,F., Guan,H.,
            Tao,K. and Hu,D.
  TITLE     Curcumin pretreatment protects against hypoxia/reoxgenation injury
            via improvement of mitochondrial function, destabilization of
            HIF-1alpha and activation of Epac1-Akt pathway in rat bone marrow
            mesenchymal stem cells
  JOURNAL   Biomed Pharmacother 109, 1268-1275 (2019)
   PUBMED   30551377
  REMARK    GeneRIF: Activation of Epac1-Akt signaling pathway.
REFERENCE   6  (residues 1 to 884)
  AUTHORS   Weissman,J.T., Ma,J.N., Essex,A., Gao,Y. and Burstein,E.S.
  TITLE     G-protein-coupled receptor-mediated activation of rap GTPases:
            characterization of a novel Galphai regulated pathway
  JOURNAL   Oncogene 23 (1), 241-249 (2004)
   PUBMED   14712229
REFERENCE   7  (residues 1 to 884)
  AUTHORS   Lin,S.L., Johnson-Farley,N.N., Lubinsky,D.R. and Cowen,D.S.
  TITLE     Coupling of neuronal 5-HT7 receptors to activation of
            extracellular-regulated kinase through a protein kinase
            A-independent pathway that can utilize Epac
  JOURNAL   J Neurochem 87 (5), 1076-1085 (2003)
   PUBMED   14622088
  REMARK    GeneRIF: Over-expression of Epac1 enhanced 5-HT7 nicotinic
            receptor-mediated activation of ERK proceeding through
            cAMP-dependent pathways utilizing cAMP-guanine nucleotide exchange
            factors rather than protein kinase A
REFERENCE   8  (residues 1 to 884)
  AUTHORS   Laroche-Joubert,N., Marsy,S., Michelet,S., Imbert-Teboul,M. and
            Doucet,A.
  TITLE     Protein kinase A-independent activation of ERK and H,K-ATPase by
            cAMP in native kidney cells: role of Epac I
  JOURNAL   J Biol Chem 277 (21), 18598-18604 (2002)
   PUBMED   11897793
REFERENCE   9  (residues 1 to 884)
  AUTHORS   Konu,O., Kane,J.K., Barrett,T., Vawter,M.P., Chang,R., Ma,J.Z.,
            Donovan,D.M., Sharp,B., Becker,K.G. and Li,M.D.
  TITLE     Region-specific transcriptional response to chronic nicotine in rat
            brain
  JOURNAL   Brain Res 909 (1-2), 194-203 (2001)
   PUBMED   11478936
REFERENCE   10 (residues 1 to 884)
  AUTHORS   Kawasaki,H., Springett,G.M., Mochizuki,N., Toki,S., Nakaya,M.,
            Matsuda,M., Housman,D.E. and Graybiel,A.M.
  TITLE     A family of cAMP-binding proteins that directly activate Rap1
  JOURNAL   Science 282 (5397), 2275-2279 (1998)
   PUBMED   9856955
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Nov 26, 2020 this sequence version replaced NP_067722.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107667.1, U78167.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..884
                     /product="rap guanine nucleotide exchange factor 3 isoform
                     2"
                     /note="epac 1; cAMP-GEFI; exchange factor directly
                     activated by cAMP 1; exchange protein directly activated
                     by cAMP 1; cAMP-regulated guanine nucleotide exchange
                     factor I (cAMP-GEFI); Rap guanine nucleotide exchange
                     factor (GEF) 3"
                     /calculated_mol_wt=100121
     Region          58..181
                     /region_name="DEP_Epac"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in Epac-like proteins. Epac (exchange proteins
                     directly activated by cAMP) proteins are GEFs
                     (guanine-nucleotide-exchange factors) for the small
                     GTPases, Rap1 and Rap2. They are directly regulated by...;
                     cd04437"
                     /db_xref="CDD:239884"
     Region          205..314
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(269..270,279..281)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(302..304,308..310)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          345..454
                     /region_name="RasGEF_N"
                     /note="RasGEF N-terminal motif; pfam00618"
                     /db_xref="CDD:459873"
     Site            order(361,420,424..425,428,431..432,467..468,471)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:100121"
     Region          619..884
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(652..654,665..666,668..670,672..673,676..677,680,
                     713,716..717,719..721,723..726,728..729,749,752,757..759,
                     762,775..777,780..782,784..786,788..791,805,809,844,
                     847..848)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     CDS             1..884
                     /gene="Rapgef3"
                     /gene_synonym="Epac"
                     /coded_by="NM_021690.3:209..2863"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:59326"
                     /db_xref="RGD:621869"
ORIGIN      
        1 mvlkrmhrpr ccsyqlvfeh rrpsciqglr wtpltnsegs ldfrvsleqa ttehvhkagk
       61 llyrhllaty ptlirdrkyh lrlhrqccsg relvdgilal glgvhsrsqa vgicqvllde
      121 galchvkhdw tfqdrdaqfy rfpgpepqpa gthdveeelv eamallsqrg pdalltvalr
      181 kspgqrtdee ldlifeellh ikavahlsns vkrelaavll fephskagtv lfsqgdkgts
      241 wyiiwkgsvn vvthgkglvt tlhegddfgq lalvndapra atiilrennc hflrvdkqdf
      301 nriikdveak tmrleehgkv vlvlertsqg agpsrpptpg rnrytvmsgt pekilellle
      361 amrpdssahd ptetflsdfl lthsvfmpct qlfaallhhf hvepsepagg seqerstyic
      421 nkrqqilrlv srwvalyspm lrsdpvatsf lqklsdlvsr dtrlsnllre qyperrrhhr
      481 lengcgnvsp qtkarnapvw fpnheeplps sagairvgdk vpydicrpdh svltlhlpvt
      541 asvrevmaal ahedhwtkgq vlvkvnsagd vvglqpdarg vatslglner ifvvdpqevh
      601 eltphpeqlg ptlgssemld lvsakdlagq ltehdwnlfn rihqvelihy vlgpqhlrdv
      661 ttanlerfmr rfnelqywva telclcpvpg praqllrkfi klaahlkeqk nlnsffavmf
      721 glsnsaisrl ahtwerlphk vrklysaler lldpswnhrv yrlaltklsp pvipfmplll
      781 kdmtfihegn htlvenlinf ekmrmmarav rmlhhcrshs taplsplrsr vshihedsqa
      841 sristcseqs lstrspastw ayvqqlkvid nqrelsrlsr elep
//
LOCUS       NP_001424812             366 aa            linear   ROD 10-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001424812 XP_038966463
VERSION     NP_001424812.1
DBSOURCE    REFSEQ: accession NM_001437883.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038966463.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.425899.1,
                                           SRR21887620.199832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001437883.1:540..1640"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424794             493 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 16 [Rattus norvegicus].
ACCESSION   NP_001424794 XP_063130009
VERSION     NP_001424794.1
DBSOURCE    REFSEQ: accession NM_001437865.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 493)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063130009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.440842.1,
                                           SRR26643298.56253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..493
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 16"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=55211
     Region          3..263
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(57,59,95..96,98,100,120,135..139,141)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(116..126,129..139)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(254,256..263)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          361..488
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..493
                     /gene="Camk2g"
                     /coded_by="NM_001437865.1:185..1666"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mhrklnaegw gpedhqkler earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe
       61 divareyyse adashcihqi lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl
      121 aievqgeqqa wfgfagtpgy lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh
      181 klyqqikaga ydfpspewdt vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas
      241 mmhrqetvec lrkfnarrkl kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna
      301 tdgikgstes cntttededl kaaplrtgng slvpegrspr drtapsagmq pqpslcssam
      361 rkqeiikite qlieainngd feaytkicdp gltsfepeal gnlvegmdfh kfyfenllsk
      421 nskpihttil nphvhviged aaciayirlt qyidgqgrpr tsqseetrvw hrrdgkwlnv
      481 hyhcsgapaa plq
//
LOCUS       NP_001424788             529 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 9 [Rattus norvegicus].
ACCESSION   NP_001424788 XP_008768718
VERSION     NP_001424788.1
DBSOURCE    REFSEQ: accession NM_001437859.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 529)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768718.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.56238.1,
                                           SRR26643296.33849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..529
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 9"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=59476
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          397..524
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..529
                     /gene="Camk2g"
                     /coded_by="NM_001437859.1:70..1659"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mpqsnnknsl vspaqepapl
      361 qtamepqttv vhnatdgikg stescnttte dedlkvrkqe iikiteqlie ainngdfeay
      421 tkicdpglts fepealgnlv egmdfhkfyf enllsknskp ihttilnphv hvigedaaci
      481 ayirltqyid gqgrprtsqs eetrvwhrrd gkwlnvhyhc sgapaaplq
//
LOCUS       NP_001424747             435 aa            linear   ROD 10-APR-2025
DEFINITION  sulfide:quinone oxidoreductase, mitochondrial isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424747 XP_038961820
VERSION     NP_001424747.1
DBSOURCE    REFSEQ: accession NM_001437818.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Augustyn,K.D., Jackson,M.R. and Jorns,M.S.
  TITLE     Use of Tissue Metabolite Analysis and Enzyme Kinetics To
            Discriminate between Alternate Pathways for Hydrogen Sulfide
            Metabolism
  JOURNAL   Biochemistry 56 (7), 986-996 (2017)
   PUBMED   28107627
  REMARK    GeneRIF: The role of Sqor in hydrogen sulfide metabolism in the
            heart and liver
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Ackermann,M., Kubitza,M., Hauska,G. and Pina,A.L.
  TITLE     The vertebrate homologue of sulfide-quinone reductase in mammalian
            mitochondria
  JOURNAL   Cell Tissue Res 358 (3), 779-792 (2014)
   PUBMED   25130143
  REMARK    GeneRIF: The present report demonstrates the presence and specific
            localization of SQRDL in various mammalian tissues.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jackson,M.R., Melideo,S.L. and Jorns,M.S.
  TITLE     Human sulfide:quinone oxidoreductase catalyzes the first step in
            hydrogen sulfide metabolism and produces a sulfane sulfur
            metabolite
  JOURNAL   Biochemistry 51 (34), 6804-6815 (2012)
   PUBMED   22852582
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Ackermann,M., Kubitza,M., Maier,K., Brawanski,A., Hauska,G. and
            Pina,A.L.
  TITLE     The vertebrate homolog of sulfide-quinone reductase is expressed in
            mitochondria of neuronal tissues
  JOURNAL   Neuroscience 199, 1-12 (2011)
   PUBMED   22067608
  REMARK    GeneRIF: we demonstrated that the SQRDL protein is expressed in
            neurons, oligodendrocytes, and endothelial cells
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038961820.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.14919.1,
                                           SRR26643296.11274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..435
                     /product="sulfide:quinone oxidoreductase, mitochondrial
                     isoform 2"
                     /EC_number="1.8.5.8"
                     /note="sulfide:quinone oxidoreductase, mitochondrial"
                     /calculated_mol_wt=48402
     Region          71..389
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     CDS             1..435
                     /gene="Sqor"
                     /gene_synonym="Cc2-17; Sqrdl"
                     /coded_by="NM_001437818.1:69..1376"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:691966"
                     /db_xref="RGD:1564504"
ORIGIN      
        1 maplvavvss prarlfacfl rlgtqqagpl qlhtgaccta knhyevlvlg ggsggitmat
       61 rmkrrvgaen vaivepserh fyqpiwtlvg agakelsssd rstlsvipsg vqwiqdrvae
      121 lnpdqncirt dngkeisyry liialgiqld yekikglpeg faypkigsny svktvektwk
      181 alqdfkegna lftfpntpvk cagapqkimy lseayfrktg krskaniifn talgtifgvk
      241 kyadalqeii rernvsvnyk hnlievradk qeavfenldk pgethvihye mlhvtppmss
      301 pdvlkrspva dsagwvdvdk etlqhkkypn vfgigdctnl ptsktaaava aqsgildrti
      361 slimknqtpt kkydgytscp lvtgynrvil aefdytaqpl etfpfdqske rismylmkad
      421 mmpflywnmm lrfna
//
LOCUS       NP_001424792             506 aa            linear   ROD 10-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 14 [Rattus norvegicus].
ACCESSION   NP_001424792 XP_017455066
VERSION     NP_001424792.1
DBSOURCE    REFSEQ: accession NM_001437863.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 506)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017455066.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1822499.1,
                                           SRR26643298.56240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..506
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 14"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=57071
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          374..501
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..506
                     /gene="Camk2g"
                     /coded_by="NM_001437863.1:70..1590"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mepqttvvhn atdgikgste
      361 scnttteded lkvrkqeiik iteqlieain ngdfeaytki cdpgltsfep ealgnlvegm
      421 dfhkfyfenl lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg rprtsqseet
      481 rvwhrrdgkw lnvhyhcsga paaplq
//
LOCUS       NP_001424777             310 aa            linear   ROD 10-APR-2025
DEFINITION  prolactin receptor isoform b precursor [Rattus norvegicus].
ACCESSION   NP_001424777 XP_038957680
VERSION     NP_001424777.1
DBSOURCE    REFSEQ: accession NM_001437848.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Ortiz-Perez,A., Limon-Morales,O., Rojas-Castaneda,J.C., Cerbon,M.
            and Picazo,O.
  TITLE     Prolactin prevents the kainic acid-induced neuronal loss in the rat
            hippocampus by inducing prolactin receptor and putatively
            increasing the VGLUT1 overexpression
  JOURNAL   Neurosci Lett 694, 116-123 (2019)
   PUBMED   30500398
  REMARK    GeneRIF: Study indicates that chronic prolactin administration
            before kainic acid induced damage induces hippocampal
            neuroprotection associated with prolactin receptor and VGLUT1
            overexpression.
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Vergara-Castaneda,E., Grattan,D.R., Pasantes-Morales,H.,
            Perez-Dominguez,M., Cabrera-Reyes,E.A., Morales,T. and Cerbon,M.
  TITLE     Prolactin mediates neuroprotection against excitotoxicity in
            primary cell cultures of hippocampal neurons via its receptor
  JOURNAL   Brain Res 1636, 193-199 (2016)
   PUBMED   26874070
  REMARK    GeneRIF: This study demonstrated that the Cultured neurons
            expressed mRNA for both PRL and its receptor (PRLR), and both PRL
            and PRLR expression levels changed after the excitotoxic insult.
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Rojas-Duran,F., Pascual-Mathey,L.I., Serrano,K., Aranda-Abreu,G.E.,
            Manzo,J., Soto-Cid,A.H. and Hernandez,M.E.
  TITLE     Correlation of prolactin levels and PRL-receptor expression with
            Stat and Mapk cell signaling in the prostate of long-term sexually
            active rats
  JOURNAL   Physiol Behav 138, 188-192 (2015)
   PUBMED   25446202
  REMARK    GeneRIF: Results showed that an active sexual life, with constant
            execution of sexual behavior, produces a sustained increase in
            serum PRL, prostate PRL receptors, and the pStat3 signaling pathway
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Arumugam,R., Fleenor,D. and Freemark,M.
  TITLE     Knockdown of prolactin receptors in a pancreatic beta cell line:
            effects on DNA synthesis, apoptosis, and gene expression
  JOURNAL   Endocrine 46 (3), 568-576 (2014)
   PUBMED   24114406
  REMARK    GeneRIF: PRLR signaling is required for DNA synthesis and survival
            of rat insulinoma cells
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Ali,S., Pellegrini,I. and Kelly,P.A.
  TITLE     A prolactin-dependent immune cell line (Nb2) expresses a mutant
            form of prolactin receptor
  JOURNAL   J Biol Chem 266 (30), 20110-20117 (1991)
   PUBMED   1718958
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Shirota,M., Banville,D., Ali,S., Jolicoeur,C., Boutin,J.M.,
            Edery,M., Djiane,J. and Kelly,P.A.
  TITLE     Expression of two forms of prolactin receptor in rat ovary and
            liver
  JOURNAL   Mol Endocrinol 4 (8), 1136-1143 (1990)
   PUBMED   2293022
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Zhang,R., Buczko,E., Tsai-Morris,C.H., Hu,Z.Z. and Dufau,M.L.
  TITLE     Isolation and characterization of two novel rat ovarian lactogen
            receptor cDNA species
  JOURNAL   Biochem Biophys Res Commun 168 (2), 415-422 (1990)
   PUBMED   2159291
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Boutin,J.M., Jolicoeur,C., Okamura,H., Gagnon,J., Edery,M.,
            Shirota,M., Banville,D., Dusanter-Fourt,I., Djiane,J. and
            Kelly,P.A.
  TITLE     Cloning and expression of the rat prolactin receptor, a member of
            the growth hormone/prolactin receptor gene family
  JOURNAL   Cell 53 (1), 69-77 (1988)
   PUBMED   2832068
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Herington,A.C., Harrison,D. and Graystone,J.
  TITLE     Hepatic binding of human and bovine growth hormones and ovine
            prolactin in the dwarf 'little' mouse
  JOURNAL   Endocrinology 112 (6), 2032-2038 (1983)
   PUBMED   6303755
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_038957680.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092133.1, SRR26643429.7268.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..310
                     /product="prolactin receptor isoform b precursor"
                     /note="PRL-R; lactogen receptor"
                     /calculated_mol_wt=33370
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2000
     Region          19..115
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          122..219
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(122,193,208)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          210..214
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Site            order(210..211,213..214)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            230..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          262..270
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     CDS             1..310
                     /gene="Prlr"
                     /gene_synonym="RATPRLR"
                     /coded_by="NM_001437848.1:214..1146"
                     /note="isoform b precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:24684"
                     /db_xref="RGD:3407"
ORIGIN      
        1 mpsalafvll vlnisllkgq sppgkpeihk crspdketft cwwnpgtdgg lptnysltys
       61 kegekttyec pdyktsgpns cffskqytsi wkiyiitvna tnqmgssssd plyvdvtyiv
      121 epepprnltl evkqlkdkkt ylwvkwsppt itdvktgwft meyeirlkpe eaeeweihft
      181 ghqtqfkvfd lypgqkylvq trckpdhgyw srwsqessve mpndftlkdt tvwiivails
      241 aviclimvwa valkgysmmt cifppvpgpk ikgfdthlle tgspskykvd lylalpggfq
      301 kldnageldy
//
LOCUS       NP_001178477             874 aa            linear   ROD 10-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX54 [Rattus norvegicus].
ACCESSION   NP_001178477 XP_002728019 XP_006249459
VERSION     NP_001178477.2
DBSOURCE    REFSEQ: accession NM_001191548.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Liu,P., Zhang,Y., Li,X. and Ma,M.
  TITLE     DEAD-box helicase 54 regulates microglial inflammatory response in
            rats with chronic constriction injuries through NF-kappaB/NLRP3
            signaling axis
  JOURNAL   J Neurophysiol 130 (2), 392-400 (2023)
   PUBMED   37377223
  REMARK    GeneRIF: DEAD-box helicase 54 regulates microglial inflammatory
            response in rats with chronic constriction injuries through
            NF-kappaB/NLRP3 signaling axis.
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 874)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 874)
  AUTHORS   Rajendran,R.R., Nye,A.C., Frasor,J., Balsara,R.D., Martini,P.G. and
            Katzenellenbogen,B.S.
  TITLE     Regulation of nuclear receptor transcriptional activity by a novel
            DEAD box RNA helicase (DP97)
  JOURNAL   J Biol Chem 278 (7), 4628-4638 (2003)
   PUBMED   12466272
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006249459.2, NP_001178477.1.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1539782.1,
                                           SRR26360186.1252917.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..874
                     /product="ATP-dependent RNA helicase DDX54"
                     /EC_number="3.6.4.13"
                     /note="DEAD (Asp-Glu-Ala-Asp) box polypeptide 54"
                     /calculated_mol_wt=97656
     Region          95..299
                     /region_name="DEADc_DDX54"
                     /note="DEAD-box helicase domain of DEAD box protein 54;
                     cd17959"
                     /db_xref="CDD:350717"
     Site            order(114..115,117..119,122,140..147)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350717"
     Region          310..441
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(400,402,427,430..431)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     Region          706..766
                     /region_name="DBP10CT"
                     /note="DBP10CT (NUC160) domain; pfam08147"
                     /db_xref="CDD:462373"
     CDS             1..874
                     /gene="Ddx54"
                     /gene_synonym="RGD1562539"
                     /coded_by="NM_001191548.2:29..2653"
                     /db_xref="GeneID:360815"
                     /db_xref="RGD:1562539"
ORIGIN      
        1 maagrrvglg prshpamapw kkkrlrkrrt gasqardsds edgefeiqae ddararklgp
       61 gralpsfpts ecvsdvepdt remvraqnkk kkksggfqsm glsypvfkgi mkkgykvptp
      121 iqrktipvil dgkdvvamar tgsgktacfl lpmferlkar saqtgarali lsptrelalq
      181 tmkftkelgk ftglktalil ggdkmedqfa alhenpdiii atpgrlvhva vemnlklqsv
      241 eyvvfdeadr lfemgfaeql qeiigrlpgg hqtvlfsatl pkllvefara gltepvlirl
      301 dvdsklneql ktsfflvred tktavllyll qnvvrpqdqn vvfvatkhha eyltelltgq
      361 gvscahiysa ldqtarkinl akfthnkcst livtdlaarg ldiplldnvi nysfpakgkl
      421 flhrvgrvar agrsgtaysl vapdevpyll dlhlflgrsv tlarpheeps sagavgrdgv
      481 lgrvpqsvvd dedsslqtal qaslelqglq rvannaqqqy lrsrpapspe sikrakeldl
      541 aelglhplfs scfeegelqr lrlvdsikny rtrttifein asskdpssqm mrakrqrdrk
      601 aitsfhqgrq erqdgpadpv pqrelpqkee edmvetvegv ftevvgqkqp rpgpnqgakr
      661 rrkeasqrdq efyvpyrpkd fdserglsvs gaggafeqqv agavldlmgd eaqnmsrgrq
      721 qlkwdrkkkr fvgqsgqedk kkiktesgrf isssykrdly qkwkqkqkid drdseeegps
      781 nrrgpgphrg gkrgrsqgas qsrassvptg hmrselktke qilkqrrqaq kqrflqrggl
      841 kqlsarnrrr aqelrqsafg rgaptrkgkm rkrm
//
LOCUS       NP_001424234            4833 aa            linear   ROD 10-APR-2025
DEFINITION  family with sequence similarity 186 member A isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424234 XP_038936290
VERSION     NP_001424234.1
DBSOURCE    REFSEQ: accession NM_001437305.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 3, 2025 this sequence version replaced XP_038936290.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            inferred exon combination        :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4833
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..4833
                     /product="family with sequence similarity 186 member A
                     isoform 1"
                     /note="Protein FAM186A-like"
                     /calculated_mol_wt=520034
     Region          <289..328
                     /region_name="GvpT"
                     /note="GvpT/GvpP family gas vesicle accessory protein;
                     NF041669"
                     /db_xref="CDD:469551"
     Region          <362..758
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <1143..1503
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1361..1947
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1722..2247
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <2736..>2956
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          3004..>3598
                     /region_name="sbcc"
                     /note="exonuclease SbcC; TIGR00618"
                     /db_xref="CDD:129705"
     Region          <3556..>3868
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          <4247..4583
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..4833
                     /gene="Fam186a"
                     /coded_by="NM_001437305.1:129..14630"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100362820"
                     /db_xref="RGD:2323958"
ORIGIN      
        1 mpvkkrgdfl idsdsddevm dpitmrnpkg skslslqfei pesvqavink ieqsqmiraq
       61 edvitklsgi mtnvqlimtr ynidslspgr kvsisevqkk trkvflekia tcvknadire
      121 ralsktlswl eewnfvlsev gainmdehyh wiakvelmpe mlksinnnvd smirmilfll
      181 eerkrlkkks vargtlwkvw kdraikrpat aqalrpdqmi sdqiglnakv teiqsmlqel
      241 istsmfskle nnaikymsat llnlskalnt vneelrlvsf rvarpflhed qgtekdtdns
      301 qqviqeliee nemlqeklre seekcdqlir vknylgrpih psaptlrtmv tlplqvpyvs
      361 rdvhreeags eeqtddsqkk gaksttvkwe psggevalaa dmqqaedrav mtqdqkklkg
      421 lpltaetsdi nletaekrtg qlaipkamek kkpskqkaqe vkgtpsvlwe qlgkgkseql
      481 lrsspgspgs restlklpdk daksevelmq tesspevqkp etkwkkvaak tgvlasakqs
      541 gkaktpkgts etpeeseqgs lesfqraila flrekssnig kafdpksirk eelslgrtev
      601 eklniirdqm eeyfqrvaet vtaalrtykd ekraqlkeka kkpskvalgt prmlpkqgag
      661 saksevgrvl lseitdppir klvlmlleei dsestfkrtk eqqgveagag keeprlkpkd
      721 raqlletwgq afkapvasqv qdrlgrdaed aeklrkrers hldilkatrq ssislipksp
      781 mktpksqrsq vqvlpvepga mgaaeeeqpk lspfssrasl lsakpppmhv leqvemaghd
      841 iaklsgaslt peqaqpltgp ltgehtvele tafiagqeqh lgtklmvprt leptqtpkgs
      901 ltaeepqavr isqvtteqip gvtgtqrtvl psqevqvkdr iltskqtleq eitlipeqdk
      961 gpritltpqq tqalgitlts eqtkaqrisl theqaralgi mltpeqyqee rlsltpqqaq
     1021 ilgltldlqq akalgitltp eqtkaqrvsl ipqqsqalea tltaqqaeaq rinltpeqae
     1081 vlglsltpqp iihapeqaev lglsltpqpi ihapeqaevl glsltpqpit lypeqaqalg
     1141 itptpqpitl ypeqtqvpgi tptpqpitra peqaqapgit ptpqpithap eqtqapgitp
     1201 tpqpitrape qtqapgitpt pqpitfnpeq arvlainlid eqvslspqqa kalgitptpq
     1261 mttltpeqtq algitptpql itlypeqaqa pgitptpqpi tlapeqaqap gitptpqpit
     1321 lspeqarvla inlideqvsl spqqakalgi tptpqmttlt peqtqalgit pmpqpitlyp
     1381 eqaqapgitp tpqpitlype qaqapgitpt pqpitrapeq aqapgitptp qpitrapeqa
     1441 qapgitpnsq pitrapeqaq apgitptpqp itrapeqtqa pgitptpqpi tftpeqaqap
     1501 gitptpqpit hapeqtqapg itrtpqpitr apeqtqapgi trtpqritra peqaqapgit
     1561 ptpqritrap eqaqapgitp tpqpitrape qaeapgitrt pqpitrapeq aqapgitrip
     1621 qpitrapeqa qapgitrtpq pitrapeqaq apgitptpqp itrapeqtqa pgitptpqpi
     1681 tfnpeqarvl ainlideqvs lspqqakalg itptpqmttl tpeqtqalgi tptpqpitly
     1741 peqaqapgit ptpqpitlsp eqaqapgitp tpqqitrape qaqapgitpt pqpitlspeq
     1801 arvlainlid eqvglspqqa kalgitptpq mttltpeqtq algitptpqp itlspeqaqa
     1861 pgitptpqpi tlspeqaqap gitptpqptt lypeqtqapg itripqpitr apeqaqapgi
     1921 tptpqpitra peqtqalgit ptpqpitftp eqaqapgitp tpqpithape qtqalgitpt
     1981 pqpitftpeq aqvlsvtptl qpitftpeqa qalgitptpq pvtltpkqnq alaialtaeq
     2041 vktqsvslsp kqtqalgitp tpqpitftpd qtqalgitpt pqpitlspeq arvlainlid
     2101 eqvslspqqa kalgitptpq mttltpeqtq algitptpqp itlypeqvqa lgitptpqpi
     2161 tlspeqaqal aitptpppit lapeqtealg itptpqpitl speqvqalgi tstpepitld
     2221 peqaqalgii ptpqpitlap eqtealgitp tpppitltpe eiqnlgisli pkqqeislsp
     2281 qqaealglti tpqqaqvqki yftplqaqal girlspdqae tlkisltpeq ahslgiiltv
     2341 eqakaqrinl tpqqaedlgl tltpeqaqdl gvylipkrqq islspqqaqa lgltltpqqa
     2401 qvqkiyltap qaqalgiiln peqaktlnis ltpeeahslg ltltldqaka qrvsltpqqa
     2461 edlgitltpe qaqdlgisli pkereisfsp eqaqalgltl tpqqaqveki yltpqhaqal
     2521 girlspeqak tmkislspeq aqslgiiltv eqakaqkinl tlqqaedlgl tltpeqaqdl
     2581 gvslipkeqe isfspeqaqa lgltltpqqa qvekiylnpq qaqalgikls peqaktmkis
     2641 lspeqaqslg iiltveqaka qkinltlqqa edlgltltpe qtqdlgvyli pkeqeislsp
     2701 eqaqalgltl tpqqakaqki yltpqqaqal giklspeqak trgfsltseq aqdlgiiltv
     2761 eqakaqrinl tlrqaedlgl tltseqaeal gitpsprqae algitpspgq aealgitptp
     2821 weaealgitp tpweaealgi aptprqaeal giaptpeqae algiaptpeq aealgiaptp
     2881 rqaealgitp spgqaealgi tptpgqakal gvapskrqak alriaptprq akalgvaptp
     2941 rqaeplgitp ipweaedlgl tltpeqaqdl gvslipkeqe islspeqaqa lgltltpqqa
     3001 kaqkiyltpq qaqalgikls peqaktmkis lspeqaqslg iiltveqaka qkinltlqqa
     3061 edlgltltpe qaqdlgvsli pkeqeisfsp eqaqalgltl tpqqaqveki ylnpqqaqal
     3121 girlspeqak tmkislspeq aqslgiiltv eqakaqkinl tlqqaedlgl tltpeqaqdl
     3181 gvslipkeqe isfspeqaqa lgltltpqqa qvekiylnpq qaqalgirls peqaktmkis
     3241 lspeqaqslg iiltveqaka qkinltlqqa edlgltltpe qaqdlgvsli pkeqeisfsp
     3301 eqaqalgltl tpqqaqveki ylnpqqaqal giklspeqak tmkislspeq aqslgiiltv
     3361 eqakaqkinl tlqqaedlgl tltpeqtqdl gvslipkeqe islspeqaqa lgltltpqqa
     3421 kaqkiyltpq qaqalgikls seqaktmkis lspeqaqslg iiltveqaka qkinltlqqa
     3481 edlgltltpe qaqdlgvyli pkeqeislsp eqaqalgltl tpqqakaqki yltpqqaqal
     3541 giklspeqak tmkislspeq aqslgiiltv eqakaqrinl tlrqaedlgl tltseqaeal
     3601 gitlspgqae algiaptpgq aealgvaptp rqaealritp sprqaealgi tpsprqaegl
     3661 gitpsprqae algiaptpeq aealgiaptp rqakalriap tprrakalgi tpspgqakal
     3721 gitpspgqak algitpspkq aealgitpsp kqaealgitp spgqakalgi tpspgqaktl
     3781 gitpspgqak algitpspgq aaalgitpsp gqakalgitp spkqaealgi tpspkqteal
     3841 gitpspgqak algitpspgq aktlgitpsp gqakalgitp spepgkeslg ltpeqvqals
     3901 tsffpketqs lgiyltpkqa wklgitlttt qakvmkislt peqaqalgit ftpeqakarr
     3961 tsltpeqaqa lgvaltpqqa kaqritltpe qaqglgvalt peqalalgia lipdnaqaqg
     4021 ilslrksqdl dvplthkqae alrsrfsvkq lealgtqrli sesvqmpkpa vaskqtqtig
     4081 iplttqlsqg lgvpltkrqd tavgispllp rqtqafepaq akqpplrprq appwqdqlap
     4141 gltktlvfti slqkawnlgl tftyeqmqaa avtltseqva aledalteam awrwetlvtp
     4201 ervqaasnit akhlqalgat arqsvqafrt pftlerpaal vpstdwpplt qapfplttsl
     4261 gvsilpdsek prmsppyrqt ladrgqgvpa qvqgpeevpp ssrqllapga pptpgpplgp
     4321 khffkpkdtw pplvsepyfp hrtppasrvp ptsgeapglv sgdtaaqkel lvsrtslfqp
     4381 pafreqapsp apewqepswt ipmqglvpis ssfplhpsta ealptpgrsq rippssttqr
     4441 sseakplkpk saralpgval gfeaspapfp iektqvpkvs dtseqtqvlq gsfdmqpfgi
     4501 fqpyvtssri prsqspltge kalsrekpgi plpslttqlp qtqqilpsek sqkpqlppid
     4561 kpwtptpvsg treakmmvpp ftdqhsedry vidveaqrkn lvtlnqaaqt sglpeqyltv
     4621 aknliiellh idtvrlgyls rkyvayrliq larnhlskrv ktiqntgkgy elqnlyimln
     4681 ridqyqkkvm qgwtdkqkhl eqrrrqclwt mtqffsqler vfklnlsqpm psissfkkip
     4741 kftklqrpvl dlliddskrs dvfkrrgqap veavwnadls tssypvvekt pmnllwaqlg
     4801 gypdipkllq ldiqstlrks lasicprskk irk
//
LOCUS       NP_001100612             565 aa            linear   ROD 10-APR-2025
DEFINITION  anaphase-promoting complex subunit 7 [Rattus norvegicus].
ACCESSION   NP_001100612 XP_001079480 XP_006249427 XP_222171
VERSION     NP_001100612.1
DBSOURCE    REFSEQ: accession NM_001107142.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Mansfeld,J., Collin,P., Collins,M.O., Choudhary,J.S. and Pines,J.
  TITLE     APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
            checkpoint responsive to kinetochore attachment
  JOURNAL   Nat Cell Biol 13 (10), 1234-1243 (2011)
   PUBMED   21926987
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Song,M.S., Carracedo,A., Salmena,L., Song,S.J., Egia,A.,
            Malumbres,M. and Pandolfi,P.P.
  TITLE     Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a
            phosphatase-independent manner
  JOURNAL   Cell 144 (2), 187-199 (2011)
   PUBMED   21241890
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Jin,L., Williamson,A., Banerjee,S., Philipp,I. and Rape,M.
  TITLE     Mechanism of ubiquitin-chain formation by the human
            anaphase-promoting complex
  JOURNAL   Cell 133 (4), 653-665 (2008)
   PUBMED   18485873
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Dube,P., Herzog,F., Gieffers,C., Sander,B., Riedel,D., Muller,S.A.,
            Engel,A., Peters,J.M. and Stark,H.
  TITLE     Localization of the coactivator Cdh1 and the cullin subunit Apc2 in
            a cryo-electron microscopy model of vertebrate APC/C
  JOURNAL   Mol Cell 20 (6), 867-879 (2005)
   PUBMED   16364912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006249427.2, XP_001079480.1, XP_222171.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.43281.1,
                                           SRR26643284.15757.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..565
                     /product="anaphase-promoting complex subunit 7"
                     /calculated_mol_wt=62863
     Region          <99..392
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          305..530
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(313..314,316,340,343..344,347..348,350..351,374,
                     377..378,381..382,385)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          442..470
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          475..503
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..565
                     /gene="Anapc7"
                     /coded_by="NM_001107142.2:75..1772"
                     /db_xref="GeneID:304490"
                     /db_xref="RGD:1311927"
ORIGIN      
        1 msvidhvrdm aaaglhsnvr llssllltms nnnpelfsps qkyqllvyha dslfhdkeyr
       61 navskytmal qqkkalskts kvrpstgnsa stpqsqclps eievkykmae cytmlkldkd
      121 aiaildgips rqrtpkinmm lanlykkagq erpsvtsyke vlrqcplald ailgllslsv
      181 kgaevasmtm nviqtvpnld wlsvwikaya fvhtgdnsra inticslekk sllrdnvdll
      241 gsladlyfra gdnknsvlkf eqaqmldpyl ikgmdvygyl laregrledv enlgcrlfni
      301 sdqhaepwvv sgchsfyskr ysralylgak aiqlnsnsvq alllkgaalr nmgrvqeaii
      361 hfreairlap crldcyegli ecylasnsir eamvmannvy ktlganaqtl tllatvcled
      421 pvtqekaktl ldkalaqrpd yvkavvkkae llsreqkyed giallrnala nqsdcvlhri
      481 lgdflvsvne yqeamdqysi alsldpndqk slegmqkmek egsptdatqe ddvddmegsg
      541 eegdlegsds eaaqwadqeq wfgmq
//
LOCUS       NP_037356                115 aa            linear   ROD 10-APR-2025
DEFINITION  small ribosomal subunit protein eS26 [Rattus norvegicus].
ACCESSION   NP_037356
VERSION     NP_037356.1
DBSOURCE    REFSEQ: accession NM_013224.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   2  (residues 1 to 115)
  AUTHORS   O'Donohue,M.F., Choesmel,V., Faubladier,M., Fichant,G. and
            Gleizes,P.E.
  TITLE     Functional dichotomy of ribosomal proteins during the synthesis of
            mammalian 40S ribosomal subunits
  JOURNAL   J Cell Biol 190 (5), 853-866 (2010)
   PUBMED   20819938
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Kuwano,Y., Nakanishi,O., Nabeshima,Y., Tanaka,T. and Ogata,K.
  TITLE     Molecular cloning and nucleotide sequence of DNA complementary to
            rat ribosomal protein S26 messenger RNA
  JOURNAL   J Biochem 97 (4), 983-992 (1985)
   PUBMED   2993263
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Stahl,J. and Kobetz,N.D.
  TITLE     Affinity labelling of rat liver ribosomal protein S26 by
            heptauridylate containing a 5'-terminal alkylating group
  JOURNAL   Mol Biol Rep 9 (4), 219-222 (1984)
   PUBMED   6708946
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Collatz,E., Ulbrich,N., Tsurugi,K., Lightfoot,H.N., MacKinlay,W.,
            Lin,A. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 40 S ribosomal subunit proteins Sa, Sc,
            S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18,
            S19, S20, S21, S26, S27', and S29
  JOURNAL   J Biol Chem 252 (24), 9071-9080 (1977)
   PUBMED   925037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X02414.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210888.1, X02414.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..115
                     /product="small ribosomal subunit protein eS26"
                     /note="40S ribosomal protein S26"
                     /calculated_mol_wt=12884
     Region          1..101
                     /region_name="Ribosomal_S26e"
                     /note="Ribosomal protein S26e; pfam01283"
                     /db_xref="CDD:426179"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62854; propagated from
                     UniProtKB/Swiss-Prot (P62856.3)"
     Region          85..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62856.3)"
     CDS             1..115
                     /gene="Rps26"
                     /coded_by="NM_013224.1:24..371"
                     /db_xref="GeneID:27139"
                     /db_xref="RGD:621044"
ORIGIN      
        1 mtkkrrnngr akkgrghvqp irctncarcv pkdkaikkfv irniveaaav rdiseasvfd
       61 ayvlpklyvk lhycvscaih skvvrnrsre arkdrtpppr frpagaaprp ppkpm
//
LOCUS       NP_001424608            1021 aa            linear   ROD 10-APR-2025
DEFINITION  INO80 complex subunit D [Rattus norvegicus].
ACCESSION   NP_001424608 XP_006245094
VERSION     NP_001424608.1
DBSOURCE    REFSEQ: accession NM_001437679.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1021)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_006245094.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2289702.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1021
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..1021
                     /product="INO80 complex subunit D"
                     /calculated_mol_wt=112291
     Region          18..79
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     Region          <170..>285
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          442..506
                     /region_name="zf-C3Hc3H"
                     /note="Potential DNA-binding domain; pfam13891"
                     /db_xref="CDD:464023"
     CDS             1..1021
                     /gene="Ino80d"
                     /gene_synonym="RGD1304808"
                     /coded_by="NM_001437679.1:262..3327"
                     /db_xref="GeneID:316440"
                     /db_xref="RGD:1304808"
ORIGIN      
        1 myegkhihfs evdnkplcsy spklckqrrl ngyafcirhv ledktapfkq ceyvakynsq
       61 rctnpipkse drrycnshlq vlgfipkker kkkndpvdev kvrhqmdama fsltvptlal
      121 kmpngldsms lsppgarvpl hyleteledp fafneedddl kkgvtvrkkl qsklaqnrqr
      181 qreteilkvr qehfstpptp pqqhahlspl ptslkppapp qgsvckspqp qstslpmqgv
      241 aptthsiaqt rqashkrplp llpssrapvs dtprtdrilm katafsphfs cisrlqrlvk
      301 lctqkhqlda dlfphlgldw seesgeeled sdqaspyqva wsvretlrqe rhtsddddae
      361 srssrvtqlc tyfqqkykhl crleraesrq kkcrhtfrka llqaaskepe ctgqliqelr
      421 raacsrdsls qtklkevepa acsgtvkgeq ctnqalpftr hcfqhillnr sqqlfsscta
      481 kfadgqqcsv pvfdithqtp lceehakkmd nflrgdnsrk vqhqqqrkpr kktkppaltk
      541 khkkkrrrgp rrpqkpippa vpqgnlsmpt svslpvqasq irspstpels adelpddian
      601 eitdiphdle lnqedfadvl prlpddlqdf dffegkngdl lptteeaeel eralqavtsl
      661 eclstigvls qsdgvpvqgl sdrgmgvfst gtdasgiqsl srevntdlge llngrivhds
      721 fssleldenl lhsatlsnpp tplagqiqgq fsapasvglt satllsqsal gerafpgqfh
      781 glhdgshasq rphpaqllsk addlitsrqq yssdhshssp hgshydsehv pspysdhits
      841 phtsysgdnm aatfsaempi maqhllptql evplggvvnp rthwgnlpvn lgdpsafsnl
      901 lgadghllst slstppttsn settqpafat vtpssssvlp glpqtsfsgm gpsaelmast
      961 spkqqlpqfs aafghqlssh sgipkdlqps hssiapptgf tvtgatatst nnasppfptp
     1021 n
//
LOCUS       NP_001103027             174 aa            linear   ROD 10-APR-2025
DEFINITION  gamma-crystallin F [Rattus norvegicus].
ACCESSION   NP_001103027 NP_001078849 XP_001072649
VERSION     NP_001103027.1
DBSOURCE    REFSEQ: accession NM_001109557.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Kim,I., Saito,T., Fujii,N., Kanamoto,T., Chatake,T. and Fujii,N.
  TITLE     Site specific oxidation of amino acid residues in rat lens
            gamma-crystallin induced by low-dose gamma-irradiation
  JOURNAL   Biochem Biophys Res Commun 466 (4), 622-628 (2015)
   PUBMED   26385181
  REMARK    GeneRIF: Specific oxidation sites of methionine, cysteine and
            tryptophan in water-soluble and -insoluble gammaE and
            gammaF-crystallin were determined by one-shot analysis after
            low-dose gamma-irradiation.
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Lengler,J., Krausz,E., Tomarev,S., Prescott,A., Quinlan,R.A. and
            Graw,J.
  TITLE     Antagonistic action of Six3 and Prox1 at the gamma-crystallin
            promoter
  JOURNAL   Nucleic Acids Res 29 (2), 515-526 (2001)
   PUBMED   11139622
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Voorter,C.E., De Haard-Hoekman,W.A., Hermans,M.M., Bloemendal,H.
            and De Jong,W.W.
  TITLE     Differential synthesis of crystallins in the developing rat eye
            lens
  JOURNAL   Exp Eye Res 50 (4), 429-437 (1990)
   PUBMED   2338125
REFERENCE   4  (residues 1 to 174)
  AUTHORS   den Dunnen,J.T., van Neck,J.W., Cremers,F.P., Lubsen,N.H. and
            Schoenmakers,J.G.
  TITLE     Nucleotide sequence of the rat gamma-crystallin gene region and
            comparison with an orthologous human region
  JOURNAL   Gene 78 (2), 201-213 (1989)
   PUBMED   2777080
REFERENCE   5  (residues 1 to 174)
  AUTHORS   den Dunnen,J.T., Moormann,R.J., Lubsen,N.H. and Schoenmakers,J.G.
  TITLE     Concerted and divergent evolution within the rat gamma-crystallin
            gene family
  JOURNAL   J Mol Biol 189 (1), 37-46 (1986)
   PUBMED   3783678
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474044.2.
            
            On or before May 29, 2008 this sequence version replaced
            NP_001078849.1, XP_001072649.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF553419.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..174
                     /product="gamma-crystallin F"
                     /note="crystallin, gamma polypeptide 6;
                     gamma-F-crystallin; gamma-crystallin 4-1"
                     /calculated_mol_wt=21225
     Region          3..82
                     /region_name="XTALbg"
                     /note="Beta/gamma crystallins; smart00247"
                     /db_xref="CDD:214583"
     Region          84..87
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P10068.2)"
     Region          89..170
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     CDS             1..174
                     /gene="Crygf"
                     /gene_synonym="Cryg6; Len"
                     /coded_by="NM_001109557.1:96..620"
                     /db_xref="GeneID:689947"
                     /db_xref="RGD:1586353"
ORIGIN      
        1 mgkitfyedr gfqgrhyecs tdhsnlqpyf srcnsvrvds gcwmlyeqpn ftgcqyflrr
       61 geypdyqqwm gfsdsvrsch liphssshri riyeredyrg qmveitddcp hlqdrfhfsd
      121 fhsfhviegy wvlyempnyr grqyllrpre yrryhdwgam narvgslrri mdyy
//
LOCUS       NP_001101805             801 aa            linear   ROD 10-APR-2025
DEFINITION  rasGAP-activating-like protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001101805 XP_001076575 XP_006249457 XP_341089
VERSION     NP_001101805.1
DBSOURCE    REFSEQ: accession NM_001108335.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Hong,Y., Han,Y.Q., Wang,Y.Z., Gao,J.R., Li,Y.X., Liu,Q. and
            Xia,L.Z.
  TITLE     Paridis Rhizoma Sapoinins attenuates liver fibrosis in rats by
            regulating the expression of RASAL1/ERK1/2 signal pathway
  JOURNAL   J Ethnopharmacol 192, 114-122 (2016)
   PUBMED   27396351
  REMARK    GeneRIF: Paridis rhizoma sapoinins attenuate CCl4-induced liver
            fibrosis through the regulation of RASAL1/ERK1/2 signal pathway.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Yoo,J.C., Lim,Ty., Park,J.S., Hah,Y.S., Park,N., Hong,S.G.,
            Park,J.Y. and Yoon,T.J.
  TITLE     SYT14L, especially its C2 domain, is involved in regulating
            melanocyte differentiation
  JOURNAL   J Dermatol Sci 72 (3), 246-251 (2013)
   PUBMED   23999003
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Tao,H., Huang,C., Yang,J.J., Ma,T.T., Bian,E.B., Zhang,L., Lv,X.W.,
            Jin,Y. and Li,J.
  TITLE     MeCP2 controls the expression of RASAL1 in the hepatic fibrosis in
            rats
  JOURNAL   Toxicology 290 (2-3), 327-333 (2011)
   PUBMED   22056649
  REMARK    GeneRIF: hypermethylation of RASAL1 is associated with the
            perpetuation of fibroblast activation and fibrogenesis in the liver
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Liu,Q., Walker,S.A., Gao,D., Taylor,J.A., Dai,Y.F., Arkell,R.S.,
            Bootman,M.D., Roderick,H.L., Cullen,P.J. and Lockyer,P.J.
  TITLE     CAPRI and RASAL impose different modes of information processing on
            Ras due to contrasting temporal filtering of Ca2+
  JOURNAL   J Cell Biol 170 (2), 183-190 (2005)
   PUBMED   16009725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006249457.1, XP_001076575.1, XP_341089.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.45615.1,
                                           SRR26643292.48181.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..801
                     /product="rasGAP-activating-like protein 1 isoform 1"
                     /note="rasGAP-activating-like protein 1; RAS protein
                     activator like 1 (GAP1 like)"
                     /calculated_mol_wt=89466
     Region          6..126
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          134..254
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          262..548
                     /region_name="RasGAP_RASAL"
                     /note="Ras-GTPase Activating Domain of RASAL1 and similar
                     proteins; cd05135"
                     /db_xref="CDD:213337"
     Site            order(301,337,339,341..342,344,347,351,462,470..471,
                     474..475,478,499,502..503,506,510,512,519..520)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213337"
     Region          552..689
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          681..709
                     /region_name="BTK"
                     /note="BTK motif; pfam00779"
                     /db_xref="CDD:459937"
     CDS             1..801
                     /gene="Rasal1"
                     /coded_by="NM_001108335.2:250..2655"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360814"
                     /db_xref="RGD:1311820"
ORIGIN      
        1 maksgslsir vvegralpak dvsgssdpyc lvkvddevva rtatiwrsls pfwgeeytvh
       61 lpldfhhlaf yvldedtvgh ddiigkisls keaitadprg idswinlsrv dpdeevqgev
      121 clavklleda rgrclrchvr qardlaprdi sgtsdpfarv fwgsrslets tikktrfphw
      181 devlelreap gttsplrvel wdwdmvgknd flgmveftpq tlqqkppngw frllpfprae
      241 dsggslgalr lkvrltedrv lpsqyyqplm elllesvqgp aeedttspla lleelasgdc
      301 rqdlatklvk lflgrglagp fldyltrrev artndpntlf rsnslasksm eqfmklvgmr
      361 ylhevlrpvi srvfeekkym eldpskmdln rsrrisfkgt pteeqvrets lglltgylgs
      421 vvdaivssag rcplalrlaf kqlqqcvekr fpgmehqdvk ylatsgflfl rffapailtp
      481 klfdlrdhha dpqtsrslll lakavqsign lgqqlgqgke qwlaplhpfl lqsisrvrdf
      541 ldqlvdvdgd eeaggstcal vqpstivreg fllkrkeepa slatrfafkk ryfrlsgrdl
      601 sysktpewqv hssiplscir avervdegaf qlphvmqvvt qdgtgashtt ylqcknvndl
      661 nqwlsalrka sapnpgklaa chpgafrsgr wtcclqaers avgcsrthsa vtlgdwsdpl
      721 dpdaeaqmvy rqlllgrdql rlklledssl dtapdvdpgk dssavdgpca evlaqqreat
      781 trllqvledl eqaheefqkr g
//
LOCUS       NP_001032864             419 aa            linear   ROD 10-APR-2025
DEFINITION  carbohydrate sulfotransferase 12 [Rattus norvegicus].
ACCESSION   NP_001032864 XP_006248997 XP_221946
VERSION     NP_001032864.1
DBSOURCE    REFSEQ: accession NM_001037775.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Prisco,S.Z., Prokop,J.W., Sarkis,A.B., Yeo,N.C., Hoffman,M.J.,
            Hansen,C.C., Jacob,H.J., Flister,M.J. and Lazar,J.
  TITLE     Refined mapping of a hypertension susceptibility locus on rat
            chromosome 12
  JOURNAL   Hypertension 64 (4), 883-890 (2014)
   PUBMED   25001272
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Hiraoka,N., Nakagawa,H., Ong,E., Akama,T.O., Fukuda,M.N. and
            Fukuda,M.
  TITLE     Molecular cloning and expression of two distinct human chondroitin
            4-O-sulfotransferases that belong to the HNK-1 sulfotransferase
            gene family
  JOURNAL   J Biol Chem 275 (26), 20188-20196 (2000)
   PUBMED   10781601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006248997.1, XP_221946.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.42557.1,
                                           SRR26643289.31903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..419
                     /product="carbohydrate sulfotransferase 12"
                     /EC_number="2.8.2.5"
                     /note="carbohydrate (chondroitin 4) sulfotransferase 12"
                     /calculated_mol_wt=49124
     Region          165..411
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     CDS             1..419
                     /gene="Chst12"
                     /coded_by="NM_001037775.3:141..1400"
                     /db_xref="GeneID:304322"
                     /db_xref="RGD:1308214"
ORIGIN      
        1 mtkprlfrlw lalgsalmil liivywdnvg tahfylhtsl srphileplp tqglaeenvl
       61 asdvdefldt llssdakhnd lsrrkteqpp vltpskpvls hmeenvrgyd wsthdaqqnp
      121 drdrqqaerr sllrdfcana slafptkdrs fddipnyeln hlivddrhgv iycyvpkvac
      181 tnwkrvmivl seslldrgsp yrdpldipre hvhntsthlt fnkfwrrygk fsrhlmkvkl
      241 kkytkflfvr dpfvrlisaf rskfelenee fyrkfavpml rlyanhtslp asvseafsag
      301 lkvsfanfiq ylldphtekl apfnehwrqv yrlchpcqid ydfvgkletl dedaaqllrs
      361 lkvdsqlhfp psyrnrtass weedwfanip lawrqqlykl yeadfvlfgy pkpenllrd
//
LOCUS       NP_001100929             210 aa            linear   ROD 10-APR-2025
DEFINITION  regulator of G-protein signaling 17 [Rattus norvegicus].
ACCESSION   NP_001100929 XP_001059287 XP_217837
VERSION     NP_001100929.1
DBSOURCE    REFSEQ: accession NM_001107459.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Dhukhwa,A., Al Aameri,R.F.H., Sheth,S., Mukherjea,D., Rybak,L. and
            Ramkumar,V.
  TITLE     Regulator of G protein signaling 17 represents a novel target for
            treating cisplatin induced hearing loss
  JOURNAL   Sci Rep 11 (1), 8116 (2021)
   PUBMED   33854102
  REMARK    GeneRIF: Regulator of G protein signaling 17 represents a novel
            target for treating cisplatin induced hearing loss.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Sun,H., Calipari,E.S., Beveridge,T.J., Jones,S.R. and Chen,R.
  TITLE     The brain gene expression profile of dopamine D2/D3 receptors and
            associated signaling proteins following amphetamine
            self-administration
  JOURNAL   Neuroscience 307, 253-261 (2015)
   PUBMED   26321241
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Sokolov,E., Iannitti,D.A., Schrum,L.W. and McKillop,I.H.
  TITLE     Altered expression and function of regulator of G-protein
            signaling-17 (RGS17) in hepatocellular carcinoma
  JOURNAL   Cell Signal 23 (10), 1603-1610 (2011)
   PUBMED   21620966
  REMARK    GeneRIF: RGS17 is differentially expressed in hepatocellular
            carcinoma cells and plays a central role in regulating transformed
            hepatocyte tumorgenicity.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474052.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217837.4, XP_001059287.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132261, SAMD00132262
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..210
                     /product="regulator of G-protein signaling 17"
                     /calculated_mol_wt=24189
     Region          41..197
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     CDS             1..210
                     /gene="Rgs17"
                     /coded_by="NM_001107459.1:257..889"
                     /db_xref="GeneID:308118"
                     /db_xref="RGD:1305515"
ORIGIN      
        1 mrkrqqsqne gtqavsqapg nqrpnntccf cwccccscsc ltvrneergd ssgrpphttk
       61 mesiqvleec qnptadevls wsqnfdkmmk apagrnlfre flrteyseen llfwlacedl
      121 kkeqnkkave ekarmiyedy isilspkevs ldsrvrevin rnllepsphm yedaqlqiyt
      181 lmhrdsfprf lnsqiykafv estasstses
//
LOCUS       NP_001099831             416 aa            linear   ROD 10-APR-2025
DEFINITION  paired box protein Pax-2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001099831 XP_001062747 XP_239083
VERSION     NP_001099831.1
DBSOURCE    REFSEQ: accession NM_001106361.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Ribeiro,P.C., Lojudice,F.H., Fernandes-Charpiot,I.M.M.,
            Baptista,M.A.S.F., de Almeida Araujo,S., Mendes,G.E.F.,
            Sogayar,M.C., Abbud-Filho,M. and Caldas,H.C.
  TITLE     Therapeutic potential of human induced pluripotent stem cells and
            renal progenitor cells in experimental chronic kidney disease
  JOURNAL   Stem Cell Res Ther 11 (1), 530 (2020)
   PUBMED   33298161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Wang,X.L., Hou,L., Zhao,C.G., Tang,Y., Zhang,B., Zhao,J.Y. and
            Wu,Y.B.
  TITLE     Screening of genes involved in epithelial-mesenchymal transition
            and differential expression of complement-related genes induced by
            PAX2 in renal tubules
  JOURNAL   Nephrology (Carlton) 24 (2), 263-271 (2019)
   PUBMED   29280536
  REMARK    GeneRIF: Pax2 overexpression by kidney tubule cells alters the
            expression of complement system proteins to induce
            epithelial-mesenchymal transition.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hou,L., Du,Y., Zhao,C. and Wu,Y.
  TITLE     PAX2 may induce ADAM10 expression in renal tubular epithelial cells
            and contribute to epithelial-to-mesenchymal transition
  JOURNAL   Int Urol Nephrol 50 (9), 1729-1741 (2018)
   PUBMED   30117015
  REMARK    GeneRIF: PAX2 directly increased expression of ADAM10, the presence
            of which contributed to EMT in renal tubular epithelia and hence
            plays an important role in renal fibrosis.
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Larsson,M.
  TITLE     Pax2 is persistently expressed by GABAergic neurons throughout the
            adult rat dorsal horn
  JOURNAL   Neurosci Lett 638, 96-101 (2017)
   PUBMED   27939388
  REMARK    GeneRIF: Persistent Pax2 expression may be required to maintain a
            GABAergic phenotype.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Jiang,Y., Jiang,T., Ouyang,J., Zhou,Q., Liang,Y., Cui,Y., Chen,P.
            and Huang,B.
  TITLE     Cell atavistic transition: Paired box 2 re-expression occurs in
            mature tubular epithelial cells during acute kidney injury and is
            regulated by Angiotensin II
  JOURNAL   PLoS One 9 (4), e93563 (2014)
   PUBMED   24710423
  REMARK    GeneRIF: Those findings suggest that mature TECs can
            trans-differentiate into progenitor-like cells by 'atavistic
            transition', which may participate in the recovery of tissue
            structure and Pax2 may play a pivotal role in this process.
            Erratum:[PLoS One. 2015 May 06;10(5):e0127718. doi:
            10.1371/journal.pone.0127718. PMID: 25945929]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Ryan,G., Steele-Perkins,V., Morris,J.F., Rauscher,F.J. 3rd and
            Dressler,G.R.
  TITLE     Repression of Pax-2 by WT1 during normal kidney development
  JOURNAL   Development 121 (3), 867-875 (1995)
   PUBMED   7720589
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Eccles,M.R., Yun,K., Reeve,A.E. and Fidler,A.E.
  TITLE     Comparative in situ hybridization analysis of PAX2, PAX8, and WT1
            gene transcription in human fetal kidney and Wilms' tumors
  JOURNAL   Am J Pathol 146 (1), 40-45 (1995)
   PUBMED   7856737
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Sharma,P.M., Bowman,M., Yu,B.F. and Sukumar,S.
  TITLE     A rodent model for Wilms tumors: embryonal kidney neoplasms induced
            by N-nitroso-N'-methylurea
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9931-9935 (1994)
   PUBMED   7937920
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Poleev,A., Fickenscher,H., Mundlos,S., Winterpacht,A., Zabel,B.,
            Fidler,A., Gruss,P. and Plachov,D.
  TITLE     PAX8, a human paired box gene: isolation and expression in
            developing thyroid, kidney and Wilms' tumors
  JOURNAL   Development 116 (3), 611-623 (1992)
   PUBMED   1337742
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Plachov,D., Chowdhury,K., Walther,C., Simon,D., Guenet,J.L. and
            Gruss,P.
  TITLE     Pax8, a murine paired box gene expressed in the developing
            excretory system and thyroid gland
  JOURNAL   Development 110 (2), 643-651 (1990)
   PUBMED   1723950
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_239083.4, XP_001062747.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132274, SAMD00132279
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..416
                     /product="paired box protein Pax-2 isoform 2"
                     /note="paired box protein Pax-2; paired box gene 2; paired
                     box protein 2; paired box homeotic gene 2"
                     /calculated_mol_wt=44591
     Region          15..139
                     /region_name="PAX"
                     /note="Paired Box domain; smart00351"
                     /db_xref="CDD:128645"
     Site            order(20..21,26,28..30,32,37,49,51,60,63,65..66,70,79..85,
                     87..90,109..111,130,132..133,136,139)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238076"
     Region          304..415
                     /region_name="Pax2_C"
                     /note="Paired-box protein 2 C terminal; pfam12403"
                     /db_xref="CDD:463563"
     CDS             1..416
                     /gene="Pax2"
                     /gene_synonym="Pax-2"
                     /coded_by="NM_001106361.1:33..1283"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293992"
                     /db_xref="RGD:1305568"
ORIGIN      
        1 mdmhckadpf samhrhggvn qlggvfvngr plpdvvrqri velahqgvrp cdisrqlrvs
       61 hgcvskilgr yyetgsikpg viggskpkva tpkvvdkiae ykrqnptmfa weirdrllae
      121 gicdndtvps vssinriirt kvqqpfhptp dgagtgvtap ghtivpstas ppvssasndp
      181 vgsysingil giprsngekr kreevevytd pahirggggl hlvwtlrdvs egsvpngdsq
      241 sgvdslrkhl radtftqqql ealdrvferp sypdvfqase hikseqgney slpaltpgld
      301 evksslsast npelgsnvsg tqtypvvtgr dmasttlpgy pphvpptgqg syptstlagm
      361 vpgsefsgnp yshpqytayn eawrfsnpal lsspyyysaa prgsapaaaa aaydrh
//
LOCUS       NP_001007688             492 aa            linear   ROD 10-APR-2025
DEFINITION  beta-Ala-His dipeptidase [Rattus norvegicus].
ACCESSION   NP_001007688 XP_008770357 XP_225678
VERSION     NP_001007688.1
DBSOURCE    REFSEQ: accession NM_001007687.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Veiga-da-Cunha,M., Chevalier,N., Stroobant,V., Vertommen,D. and Van
            Schaftingen,E.
  TITLE     Metabolite proofreading in carnosine and homocarnosine synthesis:
            molecular identification of PM20D2 as beta-alanyl-lysine
            dipeptidase
  JOURNAL   J Biol Chem 289 (28), 19726-19736 (2014)
   PUBMED   24891507
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Chakkera,H.A., Hanson,R.L., Kobes,S., Millis,M.P., Nelson,R.G.,
            Knowler,W.C. and Distefano,J.K.
  TITLE     Association of variants in the carnosine peptidase 1 gene (CNDP1)
            with diabetic nephropathy in American Indians
  JOURNAL   Mol Genet Metab 103 (2), 185-190 (2011)
   PUBMED   21393041
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Kilis-Pstrusinska,K., Zwolinska,D. and Grzeszczak,W.
  CONSRTM   Study Group
  TITLE     Is carnosinase 1 gene (CNDP1) polymorphism associated with chronic
            kidney disease progression in children and young adults? results of
            a family-based study
  JOURNAL   Arch Med Res 41 (5), 356-362 (2010)
   PUBMED   20851293
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Teufel,M., Saudek,V., Ledig,J.P., Bernhardt,A., Boularand,S.,
            Carreau,A., Cairns,N.J., Carter,C., Cowley,D.J., Duverger,D.,
            Ganzhorn,A.J., Guenet,C., Heintzelmann,B., Laucher,V., Sauvage,C.
            and Smirnova,T.
  TITLE     Sequence identification and characterization of human carnosinase
            and a closely related non-specific dipeptidase
  JOURNAL   J Biol Chem 278 (8), 6521-6531 (2003)
   PUBMED   12473676
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_008770357.1, XP_225678.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.52841.1,
                                           SRR26643295.57032.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..492
                     /product="beta-Ala-His dipeptidase"
                     /EC_number="3.4.13.20"
                     /note="CNDP dipeptidase 1; carnosine dipeptidase 1
                     (metallopeptidase M20 family)"
                     /calculated_mol_wt=54797
     Region          13..481
                     /region_name="M20_dipept_like_CNDP"
                     /note="M20 cytosolic nonspecific dipeptidases including
                     anserinase and serum carnosinase; cd05676"
                     /db_xref="CDD:349925"
     Site            order(107,140,174..175,203,205,218,351,388,422,424..426,
                     453)
                     /site_type="active"
                     /db_xref="CDD:349925"
     Site            order(111,117,219,221,223,225,231..234,236..246,248,252,
                     255..256,259..261,295,298..300,303..304,312,315..316,
                     321..328,332..339,341..342,347,351,376..377,379,388,
                     423..424,452..455)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349925"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q66HG3.1)"
     CDS             1..492
                     /gene="Cndp1"
                     /coded_by="NM_001007687.3:258..1736"
                     /db_xref="GeneID:307212"
                     /db_xref="RGD:1359493"
ORIGIN      
        1 mlspphsgtl eklfqyidlh qdefvqtlke wvaiesdsvq pmprlrqelf rmmalaadkl
       61 rnlgarvdsv dlgsqqmpdg qslptppiil aelgndpkkp svcfyghldv qpaqkedgwl
      121 tdpytltevd gklygrgatd nkgpvlawin avstfralqq dlpvnvkfil egmeeagsva
      181 leelvkrekd nffsgvdyiv isdnlwlsqk kpaltcgtrg ncyftvevkc rdqdfhsgtf
      241 ggilnepmad lvallgslvd ssghilvpgi ydqmapitee ektmyenidl dleeyqkssr
      301 verflfdtke ellthlwryp slsihgiega fdepgtktvi pgrvlgkfsi rlvphmtpsv
      361 vetqvtqhle avfskrnsfn kmavsmvlgl qpwtaningt qylaarraiq tvfgvdpdmi
      421 qdgstipiak ifqditqksv mmlplgavdd gehsqnekin rwnyiqgskl faafflelsk
      481 lhsgqqvpsg af
//
LOCUS       NP_001102532             333 aa            linear   ROD 10-APR-2025
DEFINITION  probable G-protein coupled receptor 146 [Rattus norvegicus].
ACCESSION   NP_001102532 XP_001065344 XP_006249019 XP_573364
VERSION     NP_001102532.1
DBSOURCE    REFSEQ: accession NM_001109062.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Jiang,Y., Huang,J., Xia,Y., Sun,Z., Hu,P., Wang,D., Liu,Y., Tao,T.
            and Liu,Y.
  TITLE     Hypoxia activates GPR146 which participates in pulmonary vascular
            remodeling by promoting pyroptosis of pulmonary artery endothelial
            cells
  JOURNAL   Eur J Pharmacol 941, 175502 (2023)
   PUBMED   36638952
  REMARK    GeneRIF: Hypoxia activates GPR146 which participates in pulmonary
            vascular remodeling by promoting pyroptosis of pulmonary artery
            endothelial cells.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Martin,J.H., Aitken,R.J., Bromfield,E.G., Cafe,S.L.,
            Sutherland,J.M., Frost,E.R., Nixon,B. and Lord,T.
  TITLE     Investigation into the presence and functional significance of
            proinsulin C-peptide in the female germlinedagger
  JOURNAL   Biol Reprod 100 (5), 1275-1289 (2019)
   PUBMED   30715203
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Yosten,G.L., Kolar,G.R., Redlinger,L.J. and Samson,W.K.
  TITLE     Evidence for an interaction between proinsulin C-peptide and GPR146
  JOURNAL   J Endocrinol 218 (2), B1-B8 (2013)
   PUBMED   23759446
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006249019.1, XP_573364.1, XP_001065344.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.40634.1,
                                           SRR26643292.47235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN12840127
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..333
                     /product="probable G-protein coupled receptor 146"
                     /calculated_mol_wt=36393
     Region          27..305
                     /region_name="7tmA_GPR146"
                     /note="G protein-coupled receptor 146, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd14990"
                     /db_xref="CDD:320121"
     Region          28..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320121"
     Region          61..85
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320121"
     Site            order(82,85..86,102..107,109..110,113,155,157..161,183,
                     186..188,190..192,194..195,245,248..249,251,254,272..273,
                     275..277,280,283..284)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320121"
     Region          101..131
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320121"
     Region          142..163
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320121"
     Region          183..210
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320121"
     Region          225..254
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320121"
     Region          273..298
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320121"
     CDS             1..333
                     /gene="Gpr146"
                     /gene_synonym="RGD1560731"
                     /coded_by="NM_001109062.2:89..1090"
                     /db_xref="GeneID:498153"
                     /db_xref="RGD:1560731"
ORIGIN      
        1 mwscgplnst awaeeplcrn lrlglwvlsl fylgagvpvg lgynallvla nlasknsmtm
       61 pdvyfvnmav aglvltalap ayllgpahsr walwslssea hvtllilfnv aslvtmysta
      121 llsldyyier alprtymasv yntrhvcgfv wggavltsfs sllfyicshv ssriaecarm
      181 qnteaadail vligyvvpgl avlyalalis rigkedtpld qdtsrldpsv hrllvatvct
      241 qfglwtpyyl slghtvlvsr grtveghylg ilqvakdlak flafssssvt pllyryinka
      301 fpsklrrlvk kihcgrrhcs pdpagiqqvm aqa
//
LOCUS       NP_001099408             349 aa            linear   ROD 10-APR-2025
DEFINITION  N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4
            [Rattus norvegicus].
ACCESSION   NP_001099408 XP_001079276 XP_222292
VERSION     NP_001099408.1
DBSOURCE    REFSEQ: accession NM_001105938.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Shiraishi,N., Natsume,A., Togayachi,A., Endo,T., Akashima,T.,
            Yamada,Y., Imai,N., Nakagawa,S., Koizumi,S., Sekine,S.,
            Narimatsu,H. and Sasaki,K.
  TITLE     Identification and characterization of three novel beta
            1,3-N-acetylglucosaminyltransferases structurally related to the
            beta 1,3-galactosyltransferase family
  JOURNAL   J Biol Chem 276 (5), 3498-3507 (2001)
   PUBMED   11042166
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_222292.1, XP_001079276.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1136026.1,
                                           SRR26360194.2452530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..349
                     /product="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 4"
                     /EC_number="2.4.1.149"
                     /calculated_mol_wt=39647
     Region          106..295
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..349
                     /gene="B3gnt4"
                     /coded_by="NM_001105938.2:43..1092"
                     /db_xref="GeneID:288752"
                     /db_xref="RGD:1309612"
ORIGIN      
        1 mlrrlgcvlf ctlvvlllgc llflkertpa gsseahqhfl apprphhsqc spnltvvnts
       61 lslpsrhrlf ltyrhcrnfs illepsecar diflllviks qpahieqraa irstwgrggs
      121 wargrqlklv fllgvagpvp paqllayesw qfddilqwdf aedffnltlk elhvqrwiaa
      181 actqahfilk gdddvfihvp nvleflegwd paqdllvgdv irlarpnrnt kvkyfipfsm
      241 yrarhyppya ggggyvmsqa tvrhlhtame eaelfpiddv fvgmclrklg vtpihhagfk
      301 tfgiqqplnp rdpclyrgll lvhrlsplem wtmwalvtde rlecaarkp
//
LOCUS       NP_001100982             445 aa            linear   ROD 10-APR-2025
DEFINITION  transcriptional enhancer factor TEF-4 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001100982 XP_001080702 XP_218630
VERSION     NP_001100982.1
DBSOURCE    REFSEQ: accession NM_001107512.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Tamm,C., Bower,N. and Anneren,C.
  TITLE     Regulation of mouse embryonic stem cell self-renewal by a
            Yes-YAP-TEAD2 signaling pathway downstream of LIF
  JOURNAL   J Cell Sci 124 (Pt 7), 1136-1144 (2011)
   PUBMED   21385842
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Tian,W., Yu,J., Tomchick,D.R., Pan,D. and Luo,X.
  TITLE     Structural and functional analysis of the YAP-binding domain of
            human TEAD2
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7293-7298 (2010)
   PUBMED   20368466
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Bhattaram,P., Penzo-Mendez,A., Sock,E., Colmenares,C., Kaneko,K.J.,
            Vassilev,A., Depamphilis,M.L., Wegner,M. and Lefebvre,V.
  TITLE     Organogenesis relies on SoxC transcription factors for the survival
            of neural and mesenchymal progenitors
  JOURNAL   Nat Commun 1 (1), 9 (2010)
   PUBMED   20596238
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Zhang,H., Liu,C.Y., Zha,Z.Y., Zhao,B., Yao,J., Zhao,S., Xiong,Y.,
            Lei,Q.Y. and Guan,K.L.
  TITLE     TEAD transcription factors mediate the function of TAZ in cell
            growth and epithelial-mesenchymal transition
  JOURNAL   J Biol Chem 284 (20), 13355-13362 (2009)
   PUBMED   19324877
  REMARK    Erratum:[J Biol Chem. 2019 Apr 12;294(15):5808. doi:
            10.1074/jbc.AAC119.008436. PMID: 30979850]
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Zhao,B., Ye,X., Yu,J., Li,L., Li,W., Li,S., Yu,J., Lin,J.D.,
            Wang,C.Y., Chinnaiyan,A.M., Lai,Z.C. and Guan,K.L.
  TITLE     TEAD mediates YAP-dependent gene induction and growth control
  JOURNAL   Genes Dev 22 (14), 1962-1971 (2008)
   PUBMED   18579750
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Sawada,A., Nishizaki,Y., Sato,H., Yada,Y., Nakayama,R.,
            Yamamoto,S., Nishioka,N., Kondoh,H. and Sasaki,H.
  TITLE     Tead proteins activate the Foxa2 enhancer in the node in
            cooperation with a second factor
  JOURNAL   Development 132 (21), 4719-4729 (2005)
   PUBMED   16207754
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Kaneko,K.J., Rein,T., Guo,Z.S., Latham,K. and DePamphilis,M.L.
  TITLE     DNA methylation may restrict but does not determine differential
            gene expression at the Sgy/Tead2 locus during mouse development
  JOURNAL   Mol Cell Biol 24 (5), 1968-1982 (2004)
   PUBMED   14966277
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Milewski,R.C., Chi,N.C., Li,J., Brown,C., Lu,M.M. and Epstein,J.A.
  TITLE     Identification of minimal enhancer elements sufficient for Pax3
            expression in neural crest and implication of Tead2 as a regulator
            of Pax3
  JOURNAL   Development 131 (4), 829-837 (2004)
   PUBMED   14736747
  REMARK    Erratum:[Development. 2004 Mar;131(5):1195]
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Yockey,C.E. and Shimizu,N.
  TITLE     cDNA cloning and characterization of mouse DTEF-1 and ETF, members
            of the TEA/ATTS family of transcription factors
  JOURNAL   DNA Cell Biol 17 (2), 187-196 (1998)
   PUBMED   9502435
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Yasunami,M., Suzuki,K., Houtani,T., Sugimoto,T. and Ohkubo,H.
  TITLE     Molecular characterization of cDNA encoding a novel protein related
            to transcriptional enhancer factor-1 from neural precursor cells
  JOURNAL   J Biol Chem 270 (31), 18649-18654 (1995)
   PUBMED   7629195
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_218630.3, XP_001080702.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC168947.1 [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..445
                     /product="transcriptional enhancer factor TEF-4 isoform 1"
                     /note="Embryonic TEA domain containing factor; TEA domain
                     family member 2; transcriptional enhancer factor TEF-4"
                     /calculated_mol_wt=48903
     Region          40..107
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          227..442
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..445
                     /gene="Tead2"
                     /coded_by="NM_001107512.1:117..1454"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:308582"
                     /db_xref="RGD:1593252"
ORIGIN      
        1 mgdprtgapl ddgggwtgse egseegtggs egvggdgspd aegvwspdie qsfqealaiy
       61 ppcgrrkiil sdegkmygrn eliaryiklr tgktrtrkqv sshiqvlarr ksreiqsklk
      121 dqvskdkafq tmatmssaql isapslqakl gpsgpqatel fqfwsgssgp twnvpdvkpf
      181 sqapfsmslt ppatdlpgye pppalsplpp papsppawqa ralgtarlql vefsafvepp
      241 davdsfqrhl fvhisqqcps pgapplesvd vrqiydkfpe kkgglrelyd rgpphafflv
      301 kfwadlnwgp saeeagnsgg aggfygvssq yesrelmtlt csskvcsfgk qvvekveter
      361 aqleggrfvy rllrspmcey lvnflhklrq lperymmnsv lenftilqvv tnrdtqelll
      421 ctayvfevst sergaqhhiy rlvrd
//
LOCUS       NP_001424524             153 aa            linear   ROD 10-APR-2025
DEFINITION  cdc42 effector protein 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424524 XP_008757167
VERSION     NP_001424524.1
DBSOURCE    REFSEQ: accession NM_001437595.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Joberty,G., Perlungher,R.R. and Macara,I.G.
  TITLE     The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
            proteins
  JOURNAL   Mol Cell Biol 19 (10), 6585-6597 (1999)
   PUBMED   10490598
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 4, 2025 this sequence version replaced XP_008757167.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.1452369.1,
                                           SRR26360190.2088372.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..153
                     /product="cdc42 effector protein 5 isoform 1"
                     /note="CDC42 effector protein (Rho GTPase binding) 5"
                     /calculated_mol_wt=15542
     Region          23..>50
                     /region_name="CRIB"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cl00113"
                     /db_xref="CDD:412170"
     Region          <70..113
                     /region_name="BORG_CEP"
                     /note="Cdc42 effector; pfam14957"
                     /db_xref="CDD:464403"
     CDS             1..153
                     /gene="Cdc42ep5"
                     /coded_by="NM_001437595.1:262..723"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:361505"
                     /db_xref="RGD:1308382"
ORIGIN      
        1 mallkqvgpa qpkkrlerga lsisaplgdf rhtlhvgssg dafgdtsfln rhgggpppea
       61 gappvvaphs vpppavpqas vpglrvpspa dpllsfhldl gpsmldavlg vmdaergett
      121 atkpsgdalt gmqhpnahcc snadfqlddv igl
//
LOCUS       NP_001424591             413 aa            linear   ROD 10-APR-2025
DEFINITION  transmembrane protein 237 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424591 XP_006245037
VERSION     NP_001424591.1
DBSOURCE    REFSEQ: accession NM_001437662.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Huang,L., Szymanska,K., Jensen,V.L., Janecke,A.R., Innes,A.M.,
            Davis,E.E., Frosk,P., Li,C., Willer,J.R., Chodirker,B.N.,
            Greenberg,C.R., McLeod,D.R., Bernier,F.P., Chudley,A.E., Muller,T.,
            Shboul,M., Logan,C.V., Loucks,C.M., Beaulieu,C.L., Bowie,R.V.,
            Bell,S.M., Adkins,J., Zuniga,F.I., Ross,K.D., Wang,J., Ban,M.R.,
            Becker,C., Nurnberg,P., Douglas,S., Craft,C.M., Akimenko,M.A.,
            Hegele,R.A., Ober,C., Utermann,G., Bolz,H.J., Bulman,D.E.,
            Katsanis,N., Blacque,O.E., Doherty,D., Parboosingh,J.S.,
            Leroux,M.R., Johnson,C.A. and Boycott,K.M.
  TITLE     TMEM237 is mutated in individuals with a Joubert syndrome related
            disorder and expands the role of the TMEM family at the ciliary
            transition zone
  JOURNAL   Am J Hum Genet 89 (6), 713-730 (2011)
   PUBMED   22152675
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zuniga,F.I. and Craft,C.M.
  TITLE     Deciphering the structure and function of Als2cr4 in the mouse
            retina
  JOURNAL   Invest Ophthalmol Vis Sci 51 (9), 4407-4415 (2010)
   PUBMED   20375344
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_006245037.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..413
                     /product="transmembrane protein 237 isoform 1"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 4"
                     /calculated_mol_wt=45839
     Region          148..390
                     /region_name="TMEM237"
                     /note="Transmembrane protein 237; pfam15383"
                     /db_xref="CDD:464690"
     CDS             1..413
                     /gene="Tmem237"
                     /gene_synonym="Als2cr4"
                     /coded_by="NM_001437662.1:94..1335"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:316412"
                     /db_xref="RGD:1306705"
ORIGIN      
        1 mtsretvgep ppllgtstya erppralppv psaiqdeipl shpkkkksrt kstpapasse
       61 glaepvvnrr aegseppaae lkeypeapvq rkqkkirppp eletsftekp sspsllrnen
      121 gmdvepreev vipkprrkak kmqpaepqya selgvededv itdeqstleh hsrftaptgv
      181 sqpvgkifve ksrrfqaadr selikttenv dvsmdmkpsw ttrdvalsvh rafrmiglfs
      241 hgflagcavw nivvicvlag dqfsnvsnll qqykplaypf qsllylllal stvsafdrid
      301 faktsvairn flaleptala sflyftaltl slsqqmtsdr iylyepsvng slwpaeveep
      361 vlmpwvivnl vvallvglaw lflsyrpgmd lseelmffsd vdeypergvk asp
//
LOCUS       NP_001101940             735 aa            linear   ROD 10-APR-2025
DEFINITION  myeloid zinc finger 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001101940 XP_001062114 XP_006228178 XP_341790
VERSION     NP_001101940.1
DBSOURCE    REFSEQ: accession NM_001108470.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Xing,F., Gu,H., Niu,Q., Fan,X., Wang,Z., Yuan,J., Li,Z., Xu,J.T.
            and Zhang,W.
  TITLE     MZF1 in the Dorsal Root Ganglia Contributes to the Development and
            Maintenance of Neuropathic Pain via Regulation of TRPV1
  JOURNAL   Neural Plast 2019, 2782417 (2019)
   PUBMED   31582966
  REMARK    GeneRIF: that MZF1 may contribute to neuropathic pain via
            regulation of TRPV1 expression in dorsal root ganglions
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Li,Z., Gu,X., Sun,L., Wu,S., Liang,L., Cao,J., Lutz,B.M.,
            Bekker,A., Zhang,W. and Tao,Y.X.
  TITLE     Dorsal root ganglion myeloid zinc finger protein 1 contributes to
            neuropathic pain after peripheral nerve trauma
  JOURNAL   Pain 156 (4), 711-721 (2015)
   PUBMED   25630025
  REMARK    GeneRIF: This study demonstrated that MZF1 participated in
            CCI-induced reductions in Kv1.2 mRNA and protein and total Kv
            current and the CCI-induced increase in neuronal excitability
            through MZF1-triggered Kv1.2
            Erratum:[Pain. 2022 Feb 1;163(2):e384. doi:
            10.1097/j.pain.0000000000002563. PMID: 35029603]
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Peterson,F.C., Hayes,P.L., Waltner,J.K., Heisner,A.K., Jensen,D.R.,
            Sander,T.L. and Volkman,B.F.
  TITLE     Structure of the SCAN domain from the tumor suppressor protein MZF1
  JOURNAL   J Mol Biol 363 (1), 137-147 (2006)
   PUBMED   16950398
  REMARK    Erratum:[J Mol Biol. 2007 Feb 9;366(1):346]
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Le Mee,S., Fromigue,O. and Marie,P.J.
  TITLE     Sp1/Sp3 and the myeloid zinc finger gene MZF1 regulate the human
            N-cadherin promoter in osteoblasts
  JOURNAL   Exp Cell Res 302 (1), 129-142 (2005)
   PUBMED   15541732
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Morris,J.F., Rauscher,F.J. 3rd, Davis,B., Klemsz,M., Xu,D.,
            Tenen,D. and Hromas,R.
  TITLE     The myeloid zinc finger gene, MZF-1, regulates the CD34 promoter in
            vitro
  JOURNAL   Blood 86 (10), 3640-3647 (1995)
   PUBMED   7579328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006228178.1, XP_341790.3, XP_001062114.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1589517.1,
                                           SRR26643298.1501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676810 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..735
                     /product="myeloid zinc finger 1 isoform 1"
                     /note="zinc finger protein 98"
                     /calculated_mol_wt=82849
     Region          41..153
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          358..717
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          359..379
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(364,366,368,370..371,374..375,378,392,394,398..399,
                     402..403,406,420,422,424,426..427,430..431,434)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          387..407
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          415..435
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          488..508
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          516..536
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          544..564
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(549,551,553,555..556,559..560,563,577,579,583..584,
                     587..588,591,605,607,609,611..612,615..616,619)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          572..592
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          600..620
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          628..648
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(633,635,637,639..640,643..644,647,661,663,667..668,
                     671..672,675,689,691,693,695..696,699..700,703)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          656..676
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          684..704
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          712..732
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..735
                     /gene="Mzf1"
                     /gene_synonym="Zfp98"
                     /coded_by="NM_001108470.2:218..2425"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361508"
                     /db_xref="RGD:1308391"
ORIGIN      
        1 mkpivpdssg rappenepav vkledsdnyd kredtlwdpg peaarlrfrc fryeeaigpq
       61 ealaqlrelc hqwlrpevhs keqilellvl eqflgalpse iqarvqeqwp gspeeaaalv
      121 drlrweldgp rkwvtvqvqg kevlsekmep ssfqprpqvk lqtpeagset tpgatqelpl
      181 dlqmkeetel menpellese plsaaqeaaa tllpkvaqgh gialdqtsph sdtepdvppw
      241 sedpmplwhe evegilspgf tlqmdsitae pdtvsphlhv pwdldmasls gqmqsptreg
      301 gfahalvlps dpgseqdpac edpcpsvgpa lvatrwhapr drsqghpstg tgvmrggrcd
      361 vcgkvfsqrs nllrhqkiht gerpfvcgec grsfsrsshl lrhqlthtee rpfvcrdcgq
      421 gfvrsarlee hrrvhtgeqp frcaecgqsf rqrsnllqhq rihgdppgpa ppvrslagvp
      481 eppgpfpcse ccesfprrav llehqavhtg dksfgcvecg erfgrrsvll qhrrvhsger
      541 pfacaecgqs frqrsnltqh rrihtgerpf actecgkafr qrptltqhlr vhtgekpfac
      601 pecgqrfsqr lkltrhqrth tgekpyrcse cglgftqvsr ltehqrihtg erpfacpecg
      661 qsfrqhanli qhrrihtger pyacpecgka frqrptltqh lrthrrekpf acqdcgrrfh
      721 qstkliqhqr ihste
//
LOCUS       NP_001178566             486 aa            linear   ROD 10-APR-2025
DEFINITION  monocarboxylate transporter 12 [Rattus norvegicus].
ACCESSION   NP_001178566 XP_017444790 XP_220057
VERSION     NP_001178566.1
DBSOURCE    REFSEQ: accession NM_001191637.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Jomura,R., Tanno,Y., Akanuma,S.I., Kubo,Y., Tachikawa,M. and
            Hosoya,K.I.
  TITLE     Contribution of monocarboxylate transporter 12 to blood supply of
            creatine on the sinusoidal membrane of the hepatocytes
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 321 (2), G113-G122 (2021)
   PUBMED   34075817
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Verouti,S.N., Lambert,D., Mathis,D., Pathare,G., Escher,G., Vogt,B.
            and Fuster,D.G.
  TITLE     Solute carrier SLC16A12 is critical for creatine and
            guanidinoacetate handling in the kidney
  JOURNAL   Am J Physiol Renal Physiol 320 (3), F351-F358 (2021)
   PUBMED   33459166
  REMARK    GeneRIF: Solute carrier SLC16A12 is critical for creatine and
            guanidinoacetate handling in the kidney.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Jomura,R., Tanno,Y., Akanuma,S.I., Kubo,Y., Tachikawa,M. and
            Hosoya,K.I.
  TITLE     Monocarboxylate transporter 12 as a guanidinoacetate efflux
            transporter in renal proximal tubular epithelial cells
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (11), 183434 (2020)
   PUBMED   32781157
  REMARK    GeneRIF: Monocarboxylate transporter 12 as a guanidinoacetate
            efflux transporter in renal proximal tubular epithelial cells.
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Abplanalp,J., Laczko,E., Philp,N.J., Neidhardt,J., Zuercher,J.,
            Braun,P., Schorderet,D.F., Munier,F.L., Verrey,F., Berger,W.,
            Camargo,S.M. and Kloeckener-Gruissem,B.
  TITLE     The cataract and glucosuria associated monocarboxylate transporter
            MCT12 is a new creatine transporter
  JOURNAL   Hum Mol Genet 22 (16), 3218-3226 (2013)
   PUBMED   23578822
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Castorino,J.J., Gallagher-Colombo,S.M., Levin,A.V.,
            Fitzgerald,P.G., Polishook,J., Kloeckener-Gruissem,B., Ostertag,E.
            and Philp,N.J.
  TITLE     Juvenile cataract-associated mutation of solute carrier SLC16A12
            impairs trafficking of the protein to the plasma membrane
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6774-6784 (2011)
   PUBMED   21778275
  REMARK    GeneRIF: a model whereby the SLC16A12 (c.643C>T) mutation causes
            juvenile cataract by a defect in protein trafficking rather than by
            haploinsufficiency.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_017444790.1, XP_220057.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.4706.1,
                                           SRR26643288.6974.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..486
                     /product="monocarboxylate transporter 12"
                     /note="solute carrier family 16 (monocarboxylic acid
                     transporters), member 12; solute carrier family 16, member
                     12 (monocarboxylic acid transporter 12)"
                     /calculated_mol_wt=52709
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Region          18..431
                     /region_name="MFS_MCT12"
                     /note="Monocarboxylate transporter 12 of the of the Major
                     Facilitator Superfamily of transporters; cd17424"
                     /db_xref="CDD:340982"
     Site            order(29..30,33..34,37,72,123..124,126..128,131,150,
                     153..154,157,260,263..264,267..269,272,299,303,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340982"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            253..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            353..373
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A734.1)"
     CDS             1..486
                     /gene="Slc16a12"
                     /gene_synonym="MCT 12; RGD1311468"
                     /coded_by="NM_001191637.2:380..1840"
                     /db_xref="GeneID:309525"
                     /db_xref="RGD:1311468"
ORIGIN      
        1 mtkitrvgsa sppdggwgwm ivagcflvti ctravtrcis iffvefqtyf aqdysqtawi
       61 hsivdcmtml caplgsvvsn qlscqagiml ggllastgli lgsfatslkh lylslgvltg
      121 lgfalcyspa iamvgkyfsr rkafaygiam sgsgigtfil apvvqllieq fswrgallil
      181 ggfvlnlcvc galmrpitlk edpsgpeksh drdaqredck qaspyspltk ewtetrlccs
      241 lqqgygfllm sdfvvlavsv lfmaygcspl fvylvpyals vgvshhqaaf lmsilgvidi
      301 vgnitfgwlt drrclknyry vcylfavald glcylclpml qsfpllvpfs ctfgyfdgay
      361 vtlipvvtae ivgttslssa lgvvyflhav pylvsppiag wlvdttgsyt aafllcgfam
      421 ifssillgfa kiakrmkrtq vpflvkdsdp klhlwtngsv aysiakeldq kdeeslakar
      481 tgcnlt
//
LOCUS       NP_001101939             153 aa            linear   ROD 10-APR-2025
DEFINITION  cdc42 effector protein 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001101939 XP_001070494 XP_008757166 XP_341785
VERSION     NP_001101939.1
DBSOURCE    REFSEQ: accession NM_001108469.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Joberty,G., Perlungher,R.R. and Macara,I.G.
  TITLE     The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
            proteins
  JOURNAL   Mol Cell Biol 19 (10), 6585-6597 (1999)
   PUBMED   10490598
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_008757166.1, XP_001070494.1, XP_341785.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI295807.1, SRR22582416.796775.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..153
                     /product="cdc42 effector protein 5 isoform 1"
                     /note="CDC42 effector protein (Rho GTPase binding) 5"
                     /calculated_mol_wt=15542
     Region          23..>50
                     /region_name="CRIB"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cl00113"
                     /db_xref="CDD:412170"
     Region          <70..113
                     /region_name="BORG_CEP"
                     /note="Cdc42 effector; pfam14957"
                     /db_xref="CDD:464403"
     CDS             1..153
                     /gene="Cdc42ep5"
                     /coded_by="NM_001108469.2:369..830"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361505"
                     /db_xref="RGD:1308382"
ORIGIN      
        1 mallkqvgpa qpkkrlerga lsisaplgdf rhtlhvgssg dafgdtsfln rhgggpppea
       61 gappvvaphs vpppavpqas vpglrvpspa dpllsfhldl gpsmldavlg vmdaergett
      121 atkpsgdalt gmqhpnahcc snadfqlddv igl
//
LOCUS       NP_001102476             610 aa            linear   ROD 10-APR-2025
DEFINITION  solute carrier family 23 member 3 [Rattus norvegicus].
ACCESSION   NP_001102476 XP_001060290 XP_346062
VERSION     NP_001102476.1
DBSOURCE    REFSEQ: accession NM_001109006.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474004.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_346062.2, XP_001060290.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680413,
                              SAMN06680416 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..610
                     /product="solute carrier family 23 member 3"
                     /note="solute carrier family 23 (nucleobase transporters),
                     member 3"
                     /calculated_mol_wt=64573
     Region          79..476
                     /region_name="Xan_ur_permease"
                     /note="Permease family; pfam00860"
                     /db_xref="CDD:395690"
     CDS             1..610
                     /gene="Slc23a3"
                     /coded_by="NM_001109006.1:36..1868"
                     /db_xref="GeneID:367298"
                     /db_xref="RGD:1307402"
ORIGIN      
        1 msrspphpip llsvgsqdtp aprppllppl qdpssrswas wcgpstwgls cllalqhflv
       61 ltsllwashl lllhslppgg lsyppaqlla ssffscgmst vlqtwmgsrl pliqapslef
      121 lipalvltnq klplmtktpg naslslrlcs ltrschgpel wntslrevsg avvmsgllqg
      181 tmgllgvpgr vfpycgplvl apslvvagls ahkevaqfcs ahwglallli llmvvcsqhl
      241 gscqvplcsw rpastssthi yipifrllsv lapvacvwli saclglsvip lqlsepsdap
      301 wfwlphpgew ewplltpkal aagismalaa stsslgcyal cgqllhlspp pphacsrgls
      361 leglgsvlag llgsplgtas sfpnvgtvsl fqtgsrrvah lvglfcmglg lsprlaqlft
      421 niplpvlggv lgvtqavvls agfssfhlad idsgrnvfiv gfsifmalll prwlreapil
      481 lntgwspmdm flrsllaepi flagllgfll entisgtrie rglgqalpts ftaqetqmlq
      541 ksrkkaaqey glplsiknlc scipqplrcl cpmpedsgde ggssktgeta dllpnsgess
      601 spdgregfrs
//
LOCUS       NP_001094160            2000 aa            linear   ROD 10-APR-2025
DEFINITION  myosin-14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001094160 XP_001080622 XP_218617
VERSION     NP_001094160.1
DBSOURCE    REFSEQ: accession NM_001100690.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2000)
  AUTHORS   Billington,N., Wang,A., Mao,J., Adelstein,R.S. and Sellers,J.R.
  TITLE     Characterization of three full-length human nonmuscle myosin II
            paralogs
  JOURNAL   J Biol Chem 288 (46), 33398-33410 (2013)
   PUBMED   24072716
REFERENCE   2  (residues 1 to 2000)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   3  (residues 1 to 2000)
  AUTHORS   Choi,B.O., Kang,S.H., Hyun,Y.S., Kanwal,S., Park,S.W., Koo,H.,
            Kim,S.B., Choi,Y.C., Yoo,J.H., Kim,J.W., Park,K.D., Choi,K.G.,
            Kim,S.J., Zuchner,S. and Chung,K.W.
  TITLE     A complex phenotype of peripheral neuropathy, myopathy, hoarseness,
            and hearing loss is linked to an autosomal dominant mutation in
            MYH14
  JOURNAL   Hum Mutat 32 (6), 669-677 (2011)
   PUBMED   21480433
REFERENCE   4  (residues 1 to 2000)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 2000)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 2000)
  AUTHORS   Kim,K.Y., Kovacs,M., Kawamoto,S., Sellers,J.R. and Adelstein,R.S.
  TITLE     Disease-associated mutations and alternative splicing alter the
            enzymatic and motile activity of nonmuscle myosins II-B and II-C
  JOURNAL   J Biol Chem 280 (24), 22769-22775 (2005)
   PUBMED   15845534
REFERENCE   7  (residues 1 to 2000)
  AUTHORS   Turney,S.G. and Bridgman,P.C.
  TITLE     Laminin stimulates and guides axonal outgrowth via growth cone
            myosin II activity
  JOURNAL   Nat Neurosci 8 (6), 717-719 (2005)
   PUBMED   15880105
REFERENCE   8  (residues 1 to 2000)
  AUTHORS   Bao,J., Jana,S.S. and Adelstein,R.S.
  TITLE     Vertebrate nonmuscle myosin II isoforms rescue small interfering
            RNA-induced defects in COS-7 cell cytokinesis
  JOURNAL   J Biol Chem 280 (20), 19594-19599 (2005)
   PUBMED   15774463
  REMARK    Erratum:[J Biol Chem. 2006 Apr 14;281(15):10652]
REFERENCE   9  (residues 1 to 2000)
  AUTHORS   Donaudy,F., Snoeckx,R., Pfister,M., Zenner,H.P., Blin,N., Di
            Stazio,M., Ferrara,A., Lanzara,C., Ficarella,R., Declau,F.,
            Pusch,C.M., Nurnberg,P., Melchionda,S., Zelante,L., Ballana,E.,
            Estivill,X., Van Camp,G., Gasparini,P. and Savoia,A.
  TITLE     Nonmuscle myosin heavy-chain gene MYH14 is expressed in cochlea and
            mutated in patients affected by autosomal dominant hearing
            impairment (DFNA4)
  JOURNAL   Am J Hum Genet 74 (4), 770-776 (2004)
   PUBMED   15015131
REFERENCE   10 (residues 1 to 2000)
  AUTHORS   Golomb,E., Ma,X., Jana,S.S., Preston,Y.A., Kawamoto,S.,
            Shoham,N.G., Goldin,E., Conti,M.A., Sellers,J.R. and Adelstein,R.S.
  TITLE     Identification and characterization of nonmuscle myosin II-C, a new
            member of the myosin II family
  JOURNAL   J Biol Chem 279 (4), 2800-2808 (2004)
   PUBMED   14594953
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Dec 12, 2007 this sequence version replaced
            XP_218617.3, XP_001080622.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.2273.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2000
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..2000
                     /product="myosin-14 isoform 1"
                     /EC_number="5.6.1.8"
                     /note="myosin, heavy polypeptide 14; myosin-14; myosin,
                     heavy chain 14, non-muscle"
                     /calculated_mol_wt=228784
     Region          115..792
                     /region_name="MYSc_Myh14_mammals"
                     /note="class II myosin heavy chain 14 motor domain;
                     cd14930"
                     /db_xref="CDD:276893"
     Site            order(142..150,194..201,255..265,482..487)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276893"
     Site            142..150
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276893"
     Site            194..201
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276893"
     Site            255..265
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276893"
     Site            482..487
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276893"
     Site            order(511..522,525..534)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276893"
     Site            724..733
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276893"
     Site            order(736..752,777..792)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276893"
     Region          869..1949
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     CDS             1..2000
                     /gene="Myh14"
                     /coded_by="NM_001100690.1:42..6044"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308572"
                     /db_xref="RGD:1306821"
ORIGIN      
        1 matvtlsvpg rkvasrpgpv peaaqpflfa prtpnvggpg gpqvewtarr mvwvpselhg
       61 feaaalrdeg eeeaevelae sgrrlrlprd qiqrmnppkf skaedmaelt clneasvlhn
      121 lreryysgli ytysglfcvv inpykqlpiy teaivemyrg kkrhevpphi yavtegayrs
      181 mlqdredqsi lctgesgagk tentkkviqy lahvasspkg rkepgvpasv stmsygeler
      241 qllqanpile afgnaktvkn dnssrfgkfi rinfdiagyi vganietyll eksrairqak
      301 decsfhifyq llggageqlk adlllepysh yrfltngpss spgqerelfq etleslrvlg
      361 llpeeitaml rtvsavlqfg nivlkkernt dqatmpdnta aqklcrllgl gvtdfsrall
      421 tprikvgrdy vqkaqtkeqa dfalealaka tyerlfrwlv lrlnraldrs prqgasflgi
      481 ldiagfeifq lnsfeqlcin ytneklqqlf nhtmfvleqe eyqregipwt fldfgldlqp
      541 cidlierpan ppgllallde ecwfpkatdk sfvekvaqeq gshpkfqrpr nlrdqadfsv
      601 lhyagkvdyk anewlmknmd plndnvaall hqstdrltae iwkdvegivg leqvsslgdg
      661 ppggrprrgm frtvgqlyke slsrlmatls ntnpsfvrci vpnhekragk leprlvldql
      721 rcngvlegir icrqgfpnri lfqefrqrye iltpnaipkg fmdgkqacek miqaleldpn
      781 lyrvgqskif fragvlaqle eerdlkvtdi ivsfqaaarg ylarrafqrr qqqqsalrvm
      841 qrncaaylkl rnwqwwrlfi kvkpllqvtr qdevlqaraq elqkvqelqq qsarevgelq
      901 grvaqleeer arlaeqlrae aelcseaeet rarlaarkqe lelvvtelea rvgeeeecsr
      961 qlqsekkrlq qhiqelethl eaeegarqkl qlekvtteak mkkfeedlll ledqnsklsk
     1021 errlleerla efssqaaeee ekvkslnklr vkyeatiadm edrlkkeekg rqeleklkrr
     1081 ldgesselqe qmmeqkqrae elliqlgrke eelqsalvra eeeggaraql lkslreaqag
     1141 laeaqedlea ervarakaek qrrdlgeele alrgeledtl dstnaqqelr skreqevtel
     1201 kktleeeart hevamqelrq rhsqalvelt eqleqarrgk svwektrlsl eaevselkte
     1261 lsslqtsrqe geqkrrrles qlqevqgrss dseraraeaa eklqraqvel esvstalsea
     1321 eskairlske lssaesqlhd tqellqeetr aklalgsrvr aleaeaaglr eqmeeevvar
     1381 eragrelqtt qaqlsewrrr qeeeaavlea geearrraar eaetlaqrla ekteaverle
     1441 rarrrlqqel ddatvdlgqq kqllstlekk qrkfdqllae ekaavlrave drerveaegr
     1501 erearalslt raleeeqear eelerqnral raeleallss kddvgknvhe lerarrvaeq
     1561 aasdlrtqvt eledeltaae daklrlevtv qalkaqherd lqgrddagee rrrqlakqlr
     1621 daeverdeer kqralamaar kkleleleel kaqtsaagqg keeavkqlkk mqaqmkelwr
     1681 eveetrssre emftlsrese krlkgleaev lrlqeelaas drarrqaqqd rdemaeevas
     1741 gnlskaatle ekrqlegrlg qleeeleeeq nnsellkdhy rklvlqvetl ttelsaersf
     1801 sakaesgrqq lerqiqelra rlgeedagar arqkmliaal esklaqaeeq leqesreril
     1861 sgklvrraek rlkevvlqvd eerrvadqlr dqleksnlrl kqlkrqleea eeeasraqag
     1921 rrrlqreled vtesaesmnr evttlrnrlr rgpltfttrt vrqvfrleeg vasdeeeaeg
     1981 aepgsaptqe peapppaapq
//
LOCUS       NP_001424225             169 aa            linear   ROD 10-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424225
VERSION     NP_001424225.1
DBSOURCE    REFSEQ: accession NM_001437296.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399492.423247.1,
                                           SRR26360176.889585.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..169
                     /product="mitochondrial ribosomal protein S6 isoform 2"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=19356
     Region          3..140
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(4,49,53,116,119..120,127,134,137..139)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     Site            order(5,7,45,47..49,107,109,134,138)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     CDS             1..169
                     /gene="Mrps6"
                     /coded_by="NM_001437296.1:106..615"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mpryelalil kamrrpetaa alkrtieslm drgaivrnle nlgeralpyr isshsqqhsr
       61 ggwwpsefhl vvyrciklyt hnghiestfl hwaaeaspqg gdllpryflv dfyaptnave
      121 smlehlardt dvvrpnivkh pltqevkecd givpvpleek lystkrrkk
//
LOCUS       NP_001424236             104 aa            linear   ROD 10-APR-2025
DEFINITION  family with sequence similarity 186 member A isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424236
VERSION     NP_001424236.1
DBSOURCE    REFSEQ: accession NM_001437307.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1790288.1,
                                           SRR26360181.971413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..104
                     /product="family with sequence similarity 186 member A
                     isoform 2"
                     /note="Protein FAM186A-like"
                     /calculated_mol_wt=11665
     CDS             1..104
                     /gene="Fam186a"
                     /coded_by="NM_001437307.1:227..541"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:100362820"
                     /db_xref="RGD:2323958"
ORIGIN      
        1 mpsissfkki pkftklqrpv ldlliddskr sdvfkrrgqa pveavwnadl stssypvvek
       61 tpmnllwaql ggypdipkll qldiqstlrk slasicprsk kirk
//
LOCUS       NP_001178595             497 aa            linear   ROD 10-APR-2025
DEFINITION  trichoplein keratin filament-binding protein [Rattus norvegicus].
ACCESSION   NP_001178595 XP_006249513 XP_222232
VERSION     NP_001178595.1
DBSOURCE    REFSEQ: accession NM_001191666.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Kasahara,K., Kawakami,Y., Kiyono,T., Yonemura,S., Kawamura,Y.,
            Era,S., Matsuzaki,F., Goshima,N. and Inagaki,M.
  TITLE     Ubiquitin-proteasome system controls ciliogenesis at the initial
            step of axoneme extension
  JOURNAL   Nat Commun 5, 5081 (2014)
   PUBMED   25270598
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Veleri,S., Manjunath,S.H., Fariss,R.N., May-Simera,H., Brooks,M.,
            Foskett,T.A., Gao,C., Longo,T.A., Liu,P., Nagashima,K.,
            Rachel,R.A., Li,T., Dong,L. and Swaroop,A.
  TITLE     Ciliopathy-associated gene Cc2d2a promotes assembly of subdistal
            appendages on the mother centriole during cilia biogenesis
  JOURNAL   Nat Commun 5, 4207 (2014)
   PUBMED   24947469
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Ibi,M., Zou,P., Inoko,A., Shiromizu,T., Matsuyama,M., Hayashi,Y.,
            Enomoto,M., Mori,D., Hirotsune,S., Kiyono,T., Tsukita,S., Goto,H.
            and Inagaki,M.
  TITLE     Trichoplein controls microtubule anchoring at the centrosome by
            binding to Odf2 and ninein
  JOURNAL   J Cell Sci 124 (Pt 6), 857-864 (2011)
   PUBMED   21325031
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Vecchione,A., Fassan,M., Anesti,V., Morrione,A., Goldoni,S.,
            Baldassarre,G., Byrne,D., D'Arca,D., Palazzo,J.P., Lloyd,J.,
            Scorrano,L., Gomella,L.G., Iozzo,R.V. and Baffa,R.
  TITLE     MITOSTATIN, a putative tumor suppressor on chromosome 12q24.1, is
            downregulated in human bladder and breast cancer
  JOURNAL   Oncogene 28 (2), 257-269 (2009)
   PUBMED   18931701
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Nishizawa,M., Izawa,I., Inoko,A., Hayashi,Y., Nagata,K.,
            Yokoyama,T., Usukura,J. and Inagaki,M.
  TITLE     Identification of trichoplein, a novel keratin filament-binding
            protein
  JOURNAL   J Cell Sci 118 (Pt 5), 1081-1090 (2005)
   PUBMED   15731013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006249513.1, XP_222232.5.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.207504.1,
                                           SRR26643288.48215.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..497
                     /product="trichoplein keratin filament-binding protein"
                     /calculated_mol_wt=60375
     Region          142..481
                     /region_name="TPH"
                     /note="Trichohyalin-plectin-homology domain; pfam13868"
                     /db_xref="CDD:464007"
     CDS             1..497
                     /gene="Tchp"
                     /gene_synonym="RGD1310813"
                     /coded_by="NM_001191666.2:168..1661"
                     /db_xref="GeneID:304547"
                     /db_xref="RGD:1310813"
ORIGIN      
        1 malptlpsyw snrrpaniry rqqqqedefr qqweqnsryf ktwdlhnskq tewtsktsyq
       61 rsmhalycgk meeerrknle vrrerlrklm leeqdllaee leelrlsmsl rerrlreqhr
      121 dlksareeqr klmaeqllye hwrknnpklr eieldlhkkh vinswatqke ekkqqeatek
      181 qenkqfeney aaarqeaear lkaeeerkql egqlqgealr qqmeelkqke meatklkkeq
      241 enllkqhwel erldderkqm aivrrktelg rilrhqynaq lnrrtqqiqe eleadgrilq
      301 allekdnelq qvelarreqa madaaqmkqv ieeqlqleka reaelqqllr eeakemwekr
      361 eaewareqsa rdklmsevlt grqqqiqeki eqnrraqeet lkyreeliks leegkqlalr
      421 akeeseelks arkqeleaqv aerqfqewea arqeeeeeke akkaeqlsna rlqqeartmv
      481 krgyrpkihg hlriawd
//
LOCUS       NP_001100603            1042 aa            linear   ROD 10-APR-2025
DEFINITION  GRB10-interacting GYF protein 1 [Rattus norvegicus].
ACCESSION   NP_001100603 XP_001069187 XP_017453816 XP_222024
VERSION     NP_001100603.1
DBSOURCE    REFSEQ: accession NM_001107133.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Ajiro,M., Nishidate,T., Katagiri,T. and Nakamura,Y.
  TITLE     Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary
            carcinogenesis
  JOURNAL   Int J Oncol 37 (5), 1085-1093 (2010)
   PUBMED   20878056
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Giovannone,B., Lee,E., Laviola,L., Giorgino,F., Cleveland,K.A. and
            Smith,R.J.
  TITLE     Two novel proteins that are linked to insulin-like growth factor
            (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling
  JOURNAL   J Biol Chem 278 (34), 31564-31573 (2003)
   PUBMED   12771153
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_017453816.1, XP_222024.4, XP_001069187.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.40781.1,
                                           SRR26643298.80020.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..1042
                     /product="GRB10-interacting GYF protein 1"
                     /note="PERQ amino acid rich, with GYF domain 1; PERQ amino
                     acid-rich with GYF domain-containing protein 1"
                     /calculated_mol_wt=115884
     Region          112..>265
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          475..528
                     /region_name="GYF"
                     /note="GYF domain: contains conserved Gly-Tyr-Phe
                     residues; Proline-binding domain in CD2-binding and other
                     proteins. Involved in signaling lymphocyte activity. Also
                     present in other unrelated proteins (mainly unknown)
                     derived from diverse eukaryotic species; cd00072"
                     /db_xref="CDD:238027"
     Site            487..503
                     /site_type="active"
                     /note="proline binding motif [active]"
                     /db_xref="CDD:238027"
     Site            order(497,502..503)
                     /site_type="active"
                     /note="proline interaction residues [active]"
                     /db_xref="CDD:238027"
     CDS             1..1042
                     /gene="Gigyf1"
                     /gene_synonym="Perq1"
                     /coded_by="NM_001107133.2:614..3742"
                     /db_xref="GeneID:304378"
                     /db_xref="RGD:1309933"
ORIGIN      
        1 maaetlnfgp ewlralssgg svaspppspa mpkykladyr ygreemlaly vkenkvpeel
       61 qdkefaavlq eeplqplale pltedeqrnf slsvnsvavl rlmgkgagpp laatsrgrgs
      121 trsrgrgrgd scfyqrsiee gdgafgrnpr eiqrsqswdd rgerrfeksa rrdgvrsgfe
      181 eggagprkeh arsdsenwrs lreeqeddss wrlgagprrd gdrwrstspd ggprsagwre
      241 hgerrrkfdf dlrgerggcg eedgrvgggn shlrrcrgld gfeddkdglp ewclddedee
      301 mgtfdasgaf lplkkgpkep ipeeqeldfq gleeeeeeps dgvdeegpea ggkevtplpp
      361 sekssspssl palgplwtan edgeavekel ppaegdemrg lplsprissp pagppadled
      421 eeglkhlqqe aeklvaslqd ssleeeqfta amqtqglrhs taatalplsh gaarkwfykd
      481 pqgeiqgpft tqemaewfqa gyfsmsllvk rgcdegfqpl gevikmwgrv pfapgpsppp
      541 llgnmdqerl kkqqelaaaa lyqqlqhqhf lqlvgsrqlp qcatlrekaa mgdltppqqq
      601 lttflqqlqa lktprggdqn llptmsrsls vpdsgplwdl htsassqsgg easlwdipin
      661 sstqgpileq lqlqhkfqer revelrvkre eeerkrreek rrqqqqqeeq krrqeeeelf
      721 rrkqvrqqel llkllqqqqa tnvpvppaps sppplwagla kqglsmktll elqmeserql
      781 hkqpaprepl raqapnhrvq lgglgtapln qwvseagplw ggpdksggss sgnlglwedt
      841 lksggslars lglknsrssp slsdsyshls grpvrkktee eekllkllqg iprpqdgftq
      901 wceqmlhtls ttssldvpma vailkevesp ydvhdyirsc lgdtleakef akqflerrak
      961 qkasqqrqqq qqqqqqqqqq qqeawlssss lqtafqanhs tklgpgegsk akrralmlhs
     1021 dpsilgyslh gpsgeiesvd dy
//
LOCUS       NP_001100935            1711 aa            linear   ROD 10-APR-2025
DEFINITION  chromodomain-helicase-DNA-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_001100935 XP_001056703 XP_038966704 XP_238731
VERSION     NP_001100935.1
DBSOURCE    REFSEQ: accession NM_001107465.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1711)
  AUTHORS   Pilarowski,G.O., Vernon,H.J., Applegate,C.D., Boukas,L., Cho,M.T.,
            Gurnett,C.A., Benke,P.J., Beaver,E., Heeley,J.M., Medne,L.,
            Krantz,I.D., Azage,M., Niyazov,D., Henderson,L.B., Wentzensen,I.M.,
            Baskin,B., Sacoto,M.J.G., Bowman,G.D. and Bjornsson,H.T.
  TITLE     Missense variants in the chromatin remodeler CHD1 are associated
            with neurodevelopmental disability
  JOURNAL   J Med Genet 55 (8), 561-566 (2018)
   PUBMED   28866611
REFERENCE   2  (residues 1 to 1711)
  AUTHORS   Rodgers,M.J., Banks,D.J., Bradley,K.A. and Young,J.A.
  TITLE     CHD1 and CHD2 are positive regulators of HIV-1 gene expression
  JOURNAL   Virol J 11, 180 (2014)
   PUBMED   25297984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1711)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   4  (residues 1 to 1711)
  AUTHORS   Huang,S., Gulzar,Z.G., Salari,K., Lapointe,J., Brooks,J.D. and
            Pollack,J.R.
  TITLE     Recurrent deletion of CHD1 in prostate cancer with relevance to
            cell invasiveness
  JOURNAL   Oncogene 31 (37), 4164-4170 (2012)
   PUBMED   22179824
REFERENCE   5  (residues 1 to 1711)
  AUTHORS   Grasso,C.S., Wu,Y.M., Robinson,D.R., Cao,X., Dhanasekaran,S.M.,
            Khan,A.P., Quist,M.J., Jing,X., Lonigro,R.J., Brenner,J.C.,
            Asangani,I.A., Ateeq,B., Chun,S.Y., Siddiqui,J., Sam,L.,
            Anstett,M., Mehra,R., Prensner,J.R., Palanisamy,N., Ryslik,G.A.,
            Vandin,F., Raphael,B.J., Kunju,L.P., Rhodes,D.R., Pienta,K.J.,
            Chinnaiyan,A.M. and Tomlins,S.A.
  TITLE     The mutational landscape of lethal castration-resistant prostate
            cancer
  JOURNAL   Nature 487 (7406), 239-243 (2012)
   PUBMED   22722839
REFERENCE   6  (residues 1 to 1711)
  AUTHORS   Dey,P., Ponnusamy,M.P., Deb,S. and Batra,S.K.
  TITLE     Human RNA polymerase II-association factor 1 (hPaf1/PD2) regulates
            histone methylation and chromatin remodeling in pancreatic cancer
  JOURNAL   PLoS One 6 (10), e26926 (2011)
   PUBMED   22046413
REFERENCE   7  (residues 1 to 1711)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   8  (residues 1 to 1711)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   9  (residues 1 to 1711)
  AUTHORS   Chen,Y.X., Yan,J., Keeshan,K., Tubbs,A.T., Wang,H., Silva,A.,
            Brown,E.J., Hess,J.L., Pear,W.S. and Hua,X.
  TITLE     The tumor suppressor menin regulates hematopoiesis and myeloid
            transformation by influencing Hox gene expression
  JOURNAL   Proc Natl Acad Sci U S A 103 (4), 1018-1023 (2006)
   PUBMED   16415155
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_038966704.1, XP_001056703.1, XP_238731.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.745.1, SRR26643292.789.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1711
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..1711
                     /product="chromodomain-helicase-DNA-binding protein 1"
                     /EC_number="3.6.4.12"
                     /calculated_mol_wt=196342
     Region          268..352
                     /region_name="CD1_tandem_CHD1-2_like"
                     /note="repeat 1 of the paired tandem chromodomains of
                     chromodomain helicase DNA-binding protein 1 and 2, and
                     similar proteins; cd18666"
                     /db_xref="CDD:349313"
     Site            order(270,320,322..323,327)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349313"
     Region          385..441
                     /region_name="CD2_tandem_CHD1-2_like"
                     /note="repeat 2 of the paired tandem chromodomains of
                     chromodomain helicase DNA-binding protein 1 and 2, and
                     similar proteins; cd18661"
                     /db_xref="CDD:349308"
     Site            order(406,423)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349308"
     Region          458..695
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          462..>998
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(506..512,612)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          1122..1208
                     /region_name="CDH1_2_SANT_HL1"
                     /note="CDH1/2 SANT-Helical linker 1; cl39715"
                     /db_xref="CDD:477096"
     Region          <1292..1574
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          1408..1498
                     /region_name="DUF4208"
                     /note="Domain of unknown function (DUF4208); pfam13907"
                     /db_xref="CDD:464035"
     Region          1591..>1691
                     /region_name="PHA03420"
                     /note="E4 protein; Provisional"
                     /db_xref="CDD:177648"
     CDS             1..1711
                     /gene="Chd1"
                     /coded_by="NM_001107465.2:475..5610"
                     /db_xref="GeneID:308215"
                     /db_xref="RGD:1306794"
ORIGIN      
        1 mnghsdeesv rngsgessqs eddsgsasgs gsgsssgsss dgsssqsgss dsdsgsdsgs
       61 qsesesdtsr enkvqakppk vdgaefwksn psilavqrsa mlrkqtqqpq qqrpassnsg
      121 seedssssed sdasssdvkr kkhndedwqm sgsgspsqsg sdsesederd ksscdgtesd
      181 yepknkvksr kpqnrsksks gkkilgqkkr qidssededd edydndkrss rrqatvnvsy
      241 kedeemktds ddllevcged vpqtedeefe tierfmdcrv grkgatgatt tiyaieadgd
      301 pnagfekske pgdvqylikw kgwshihntw eteetlkqqn vrgmkkldny kkkdqetkrw
      361 lknaspedve yyncqqeltd dlhkqyqive riiahsnqks aaglpdyyck wqglpysecs
      421 wedgaliskk fqtcideyfs rnqskttpfk dckvlkqrpr fvalkkqpsy iggheglelr
      481 dyqlnglnwl ahswckgnsc ilademglgk tiqtisflny lfhehqlygp fllvvplstl
      541 tswqreiqtw asqmnavvyl gdinsrnmir thewmhpqtk rlkfnilltt yeillkdkaf
      601 lgglnwafig vdeahrlknd dsllyktlid fksnhrllit gtplqnslke lwsllhfimp
      661 ekfsswedfe eehgkgreyg yaslhkelep fllrrvkkdv ekslpakveq ilrmemsalq
      721 kqyykwiltr nykalskgsk gstsgflnim melkkccnhc ylikppdnne fynkqealqh
      781 lirssgklil ldkllirlre rgnrvlifsq mvrmldilae ylkyrqfpfq rldgsikgel
      841 rrqaldhfna egsedfcfll stragglgin lasadtvvif dsdwnpqndl qaqarahrig
      901 qkkqvniyrl vtkgsveedi lerakkkmvl dhlviqrmdt tgktvlhtgs apssstpfnk
      961 eelsailkfg aeelfkepeg eeqepqemdi deilkraeth enepgpltvg dellsqfkva
     1021 nfsnmdeddi elepernskn wediipeeqr rrleeeerqk eleeiymlpr mrncakqisf
     1081 ngsegrrsrs rrysgsdsds iserkrpkkr grprtipren ikgfsdaeir rfiksykkfg
     1141 gplerldaia rdaelvdkse tdlrrlgelv hngcvkalkd sssgteragg rlgkvkgptf
     1201 risgvqvnak lviahedeli plhksipsdp eerkqytipc htkaahfdid wgkeddsnll
     1261 igiyeygygs wemikmdpdl slthkilpdd pdkkpqakql qtradylikl lsrdlakkea
     1321 qrlsgaggsk rrktrakknk amksikvkee iksdssplps erseeeddnv ndskpeskdr
     1381 skksvvsdap vhitasgepv piaeeseeld qktfsicker mrpvkaalkq ldrpekglse
     1441 reqlehtrqc likigdhite clkeysnpeq ikqwrknlwi fvskftefda rklhklykha
     1501 ikkrqesqqn sdqnsnvptt hvirnpdmer lkentnhdds srdgyssdrh lsqchdhhkd
     1561 rhqgdsykks dsrkrpyssf sngkdhrewd hyrqdsryys drekhrkldd hrsrehrpsv
     1621 egslkdrchs dhrshsdhrm hsdhrssteh thhkssrdyr ylsdwqldhr aassgprspl
     1681 dqrspygsrs pfehsaehrs tpehtwssrk t
//
LOCUS       NP_001424257             419 aa            linear   ROD 10-APR-2025
DEFINITION  carbohydrate sulfotransferase 12 [Rattus norvegicus].
ACCESSION   NP_001424257 XP_017453811
VERSION     NP_001424257.1
DBSOURCE    REFSEQ: accession NM_001437328.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Prisco,S.Z., Prokop,J.W., Sarkis,A.B., Yeo,N.C., Hoffman,M.J.,
            Hansen,C.C., Jacob,H.J., Flister,M.J. and Lazar,J.
  TITLE     Refined mapping of a hypertension susceptibility locus on rat
            chromosome 12
  JOURNAL   Hypertension 64 (4), 883-890 (2014)
   PUBMED   25001272
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Hiraoka,N., Nakagawa,H., Ong,E., Akama,T.O., Fukuda,M.N. and
            Fukuda,M.
  TITLE     Molecular cloning and expression of two distinct human chondroitin
            4-O-sulfotransferases that belong to the HNK-1 sulfotransferase
            gene family
  JOURNAL   J Biol Chem 275 (26), 20188-20196 (2000)
   PUBMED   10781601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Apr 3, 2025 this sequence version replaced XP_017453811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.40596.1,
                                           SRR26643284.15484.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..419
                     /product="carbohydrate sulfotransferase 12"
                     /EC_number="2.8.2.5"
                     /note="carbohydrate (chondroitin 4) sulfotransferase 12"
                     /calculated_mol_wt=49124
     Region          165..411
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     CDS             1..419
                     /gene="Chst12"
                     /coded_by="NM_001437328.1:339..1598"
                     /db_xref="GeneID:304322"
                     /db_xref="RGD:1308214"
ORIGIN      
        1 mtkprlfrlw lalgsalmil liivywdnvg tahfylhtsl srphileplp tqglaeenvl
       61 asdvdefldt llssdakhnd lsrrkteqpp vltpskpvls hmeenvrgyd wsthdaqqnp
      121 drdrqqaerr sllrdfcana slafptkdrs fddipnyeln hlivddrhgv iycyvpkvac
      181 tnwkrvmivl seslldrgsp yrdpldipre hvhntsthlt fnkfwrrygk fsrhlmkvkl
      241 kkytkflfvr dpfvrlisaf rskfelenee fyrkfavpml rlyanhtslp asvseafsag
      301 lkvsfanfiq ylldphtekl apfnehwrqv yrlchpcqid ydfvgkletl dedaaqllrs
      361 lkvdsqlhfp psyrnrtass weedwfanip lawrqqlykl yeadfvlfgy pkpenllrd
//
LOCUS       NP_001424602             578 aa            linear   ROD 10-APR-2025
DEFINITION  SPATS2-like protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424602 XP_038939555
VERSION     NP_001424602.1
DBSOURCE    REFSEQ: accession NM_001437673.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 8, 2025 this sequence version replaced XP_038939555.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.35385.1,
                                           SRR26643294.36368.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..578
                     /product="SPATS2-like protein isoform 1"
                     /note="SPATS2-like protein"
                     /calculated_mol_wt=63767
     Region          79..388
                     /region_name="DUF1387"
                     /note="Protein of unknown function (DUF1387); pfam07139"
                     /db_xref="CDD:462100"
     CDS             1..578
                     /gene="Spats2l"
                     /gene_synonym="RGD1309930"
                     /coded_by="NM_001437673.1:187..1923"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:316426"
                     /db_xref="RGD:1309930"
ORIGIN      
        1 magtqetgas tskaytprrk maelnthvnv kekiyavrsv vpnksnneiv lvlqqfdfnv
       61 dkavqafvdg saiqvlkews mtgkkknnkr krskskqhqg nkdakdkger pevgplqpqa
      121 plvqnghmng cekdssspds areklaltpr ekkisileep praqrgiteg srllqqkmsl
      181 dgnpkaihgp sersdglqws agqpcnpskp kaktspvksn apaahleikp delakkrgpn
      241 ieksvkdlqr ctvsltryrv mikeevdssv kkikaafael hnciidkevs lmaemdkvke
      301 eamdiltarq kkaeelkrlt dlasqmaemq laelraeikh fvserkydee lgkaarfscd
      361 ieqlkaqili cgeithpknn yssrtpcssl lpllnthava sgkqgnfsrk ssghnkpneg
      421 kaanpkmvsg lpstadacqq tmptnkqqng psnqrrrfnp qyhnrlngpa ksqgsgnead
      481 pmvksnnrhe hrrqphngfr pknkggaknq eaplgtkape apphsekarr rqhaadnlet
      541 rpfrgnvgrv sqcnlcptri evsteatvls vpavtlva
//
LOCUS       NP_001424224             125 aa            linear   ROD 10-APR-2025
DEFINITION  mitochondrial ribosomal protein S6 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424224
VERSION     NP_001424224.1
DBSOURCE    REFSEQ: accession NM_001437295.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI282247.1, SRR22582416.1563961.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..125
                     /product="mitochondrial ribosomal protein S6 isoform 1"
                     /note="28S ribosomal protein S6, mitochondrial; small
                     ribosomal subunit protein bS6m"
                     /calculated_mol_wt=14210
     Region          3..96
                     /region_name="bS6_mito"
                     /note="Mitochondrial Ribosomal Protein (MRP) S6; cd15465"
                     /db_xref="CDD:275386"
     Site            order(4,49,53,72,75..76,83,90,93..95)
                     /site_type="other"
                     /note="rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:275386"
     Site            order(5,7,45,47..49,63,65,90,94)
                     /site_type="other"
                     /note="S18 interface [polypeptide binding]"
                     /db_xref="CDD:275386"
     CDS             1..125
                     /gene="Mrps6"
                     /coded_by="NM_001437295.1:106..483"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:100360017"
                     /db_xref="RGD:2322928"
ORIGIN      
        1 mpryelalil kamrrpetaa alkrtieslm drgaivrnle nlgeralpyr isshsqqhsr
       61 ggyflvdfya ptnavesmle hlardtdvvr pnivkhpltq evkecdgivp vpleeklyst
      121 krrkk
//
LOCUS       NP_001424238             608 aa            linear   ROD 10-APR-2025
DEFINITION  protein hinderin isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424238
VERSION     NP_001424238.1
DBSOURCE    REFSEQ: accession NM_001437309.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1322829.1,
                                           SRR26643293.76442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..608
                     /product="protein hinderin isoform 3"
                     /calculated_mol_wt=68821
     Region          92..415
                     /region_name="KIAA1328"
                     /note="Uncharacterized protein KIAA1328; pfam15369"
                     /db_xref="CDD:464679"
     CDS             1..608
                     /gene="Kiaa1328"
                     /gene_synonym="RGD1562608; RGD1564140"
                     /coded_by="NM_001437309.1:25..1851"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:498831"
                     /db_xref="RGD:1562608"
ORIGIN      
        1 magaagpslp gsafwsrdfs deeqsvvyvp gisterntrs rlklinpkvd akvkvpkvtd
       61 ipasmeslkg agdsvaeqsf ckrglksasl kdlcvedkrr ianlikelar vseekevtee
      121 rlkteqesfe kkirqleeqn eliikereal qlqyrecqel lslyqkylse qqekltmsls
      181 elgaaraqeq qitkkkithq sslvnldgsy lsvakpqtcq trarpksenq dsaseshtal
      241 rnnslkpvtl hhpkqdlerm stetrtctye spgrrlinaa pveealpeel kikdypnllp
      301 tpssqycghk yseseayvhe nyhptnmasq cckthpescs hcrmswaslm hdgvtlqpre
      361 tdiekqlsed rrqqlmlqkm eleiekerlq qllaqqetkl llkqqqlhqs rldynwlrtq
      421 avfrsrelva dkdfpkpgsd sgpsllkpkc dgwlrgtsss frkcpdspns aqnqkekktv
      481 efqshvengi qwtcqqndtc rlqretatgv rkdastspms tqspkhpltp asssskhkts
      541 ryetslldlv qslspnsapk cqphssraag twsalrptpk tstwkkvgth kspedleenq
      601 ilediffi
//
LOCUS       NP_001424714             428 aa            linear   ROD 11-APR-2025
DEFINITION  rab-3A-interacting protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424714
VERSION     NP_001424714.2
DBSOURCE    REFSEQ: accession NM_001437785.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Vetter,M., Stehle,R., Basquin,C. and Lorentzen,E.
  TITLE     Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3
            and Rabin8 effectors to Rab11
  JOURNAL   Nat Struct Mol Biol 22 (9), 695-702 (2015)
   PUBMED   26258637
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Klip,A., Sun,Y., Chiu,T.T. and Foley,K.P.
  TITLE     Signal transduction meets vesicle traffic: the software and
            hardware of GLUT4 translocation
  JOURNAL   Am J Physiol Cell Physiol 306 (10), C879-C886 (2014)
   PUBMED   24598362
  REMARK    Review article
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Chiba,S., Amagai,Y., Homma,Y., Fukuda,M. and Mizuno,K.
  TITLE     NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by
            switching binding specificity from phosphatidylserine to Sec15
  JOURNAL   EMBO J 32 (6), 874-885 (2013)
   PUBMED   23435566
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Blumer,J., Rey,J., Dehmelt,L., Mazel,T., Wu,Y.W., Bastiaens,P.,
            Goody,R.S. and Itzen,A.
  TITLE     RabGEFs are a major determinant for specific Rab membrane targeting
  JOURNAL   J Cell Biol 200 (3), 287-300 (2013)
   PUBMED   23382462
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Ultanir,S.K., Hertz,N.T., Li,G., Ge,W.P., Burlingame,A.L.,
            Pleasure,S.J., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Chemical genetic identification of NDR1/2 kinase substrates AAK1
            and Rabin8 Uncovers their roles in dendrite arborization and spine
            development
  JOURNAL   Neuron 73 (6), 1127-1142 (2012)
   PUBMED   22445341
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Hattula,K., Furuhjelm,J., Arffman,A. and Peranen,J.
  TITLE     A Rab8-specific GDP/GTP exchange factor is involved in actin
            remodeling and polarized membrane transport
  JOURNAL   Mol Biol Cell 13 (9), 3268-3280 (2002)
   PUBMED   12221131
REFERENCE   7  (residues 1 to 428)
  AUTHORS   de Bruijn,D.R., dos Santos,N.R., Kater-Baats,E., Thijssen,J., van
            den Berk,L., Stap,J., Balemans,M., Schepens,M., Merkx,G. and van
            Kessel,A.G.
  TITLE     The cancer-related protein SSX2 interacts with the human homologue
            of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear
            protein, SSX2IP
  JOURNAL   Genes Chromosomes Cancer 34 (3), 285-298 (2002)
   PUBMED   12007189
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Page,G., Kogel,D., Rangnekar,V. and Scheidtmann,K.H.
  TITLE     Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP
            kinase and Par-4 results in cytoplasmic retention and apoptosis
  JOURNAL   Oncogene 18 (51), 7265-7273 (1999)
   PUBMED   10602480
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Page,G., Lodige,I., Kogel,D. and Scheidtmann,K.H.
  TITLE     AATF, a novel transcription factor that interacts with Dlk/ZIP
            kinase and interferes with apoptosis
  JOURNAL   FEBS Lett 462 (1-2), 187-191 (1999)
   PUBMED   10580117
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Brondyk,W.H., McKiernan,C.J., Fortner,K.A., Stabila,P., Holz,R.W.
            and Macara,I.G.
  TITLE     Interaction cloning of Rabin3, a novel protein that associates with
            the Ras-like GTPase Rab3A
  JOURNAL   Mol Cell Biol 15 (3), 1137-1143 (1995)
   PUBMED   7532276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced NP_001424714.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.39114.1,
                                           SRR26643287.17902.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..428
                     /product="rab-3A-interacting protein isoform 2"
                     /note="rab-3A-interacting protein; rabin-3;
                     SSX2-interacting protein; rab3A-interacting protein"
                     /calculated_mol_wt=47140
     Region          103..>209
                     /region_name="ATG16"
                     /note="Autophagy protein 16 (ATG16); pfam08614"
                     /db_xref="CDD:462536"
     Region          <158..>208
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          234..426
                     /region_name="Rab11BD_RAB3IP"
                     /note="Rab11 binding domain of Rab-3A-interacting protein
                     (RAB3IP); cd21068"
                     /db_xref="CDD:411032"
     Site            order(319..325,380,383..384,387,391,396..400)
                     /site_type="other"
                     /note="Rab11 binding site [polypeptide binding]"
                     /db_xref="CDD:411032"
     CDS             1..428
                     /gene="Rab3ip"
                     /gene_synonym="RABIN3"
                     /coded_by="NM_001437785.2:194..1480"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29885"
                     /db_xref="RGD:620650"
ORIGIN      
        1 mandplegfh evnlasptsp dllgvcdpgt qeqttspsvi yrphpstlcs atiqanalnl
       61 sdlptqpvys sprhlncaei snisihvpep assvasevaa gltrftsrkd scnaereflq
      121 gatvteasag nddifglstd slsrlrspsv levrekgyer lkeelakaqr eahkmvrean
      181 vkqataekql keaqgkidvl qaevaalktl vlsssptspt qeplaagktp fkrghtrnks
      241 tssamsgshq dfsaiqpivk dcreadlsly nefrswkdep tmdrtcpfld kiyqedifpc
      301 ltfakselas avleavennt lsiepvglqp irfvkasave cggpkkcalt gqskpckhri
      361 klgdsssyyy ispvcryrit svcnfftyir yiqqglvkqq dvdqmfwevm qlrkemslak
      421 lgyfkeel
//
LOCUS       NP_001424881             274 aa            linear   ROD 11-APR-2025
DEFINITION  uncharacterized protein LOC290425 [Rattus norvegicus].
ACCESSION   NP_001424881 XP_063130238
VERSION     NP_001424881.1
DBSOURCE    REFSEQ: accession NM_001437952.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063130238.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.458732.1,
                                           SRR26360181.708876.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..274
                     /product="uncharacterized protein LOC290425"
                     /note="spermatid associated like"
                     /calculated_mol_wt=32094
     Region          <48..>251
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <156..>255
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
     CDS             1..274
                     /gene="Golga6l9"
                     /gene_synonym="RGD1306441; Spertl"
                     /coded_by="NM_001437952.1:196..1020"
                     /db_xref="GeneID:290425"
                     /db_xref="RGD:1306441"
ORIGIN      
        1 mnisgskqih krkilrlfsc fsctqnqkkl khksqdvekk lcrenkvlrd enralrkdnk
       61 flwgenkalg renktfrmdn qfirernhil rqqnqllrkv krlisenpkl sgeecnalnt
      121 egrsfwqqnr ameaqitalr qqekafqnea kalheeiksl ceetkalqhq eralrmeeka
      181 llrdgvaael aealtkegaa lemeeqalwk eeqalreenk alreehgalq deevalqeea
      241 rilqewnnll qgkitnnlpe nmnnqdpekc elrm
//
LOCUS       NP_001101543             907 aa            linear   ROD 11-APR-2025
DEFINITION  tight junction protein ZO-3 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001101543 XP_001069839 XP_234924
VERSION     NP_001101543.1
DBSOURCE    REFSEQ: accession NM_001108073.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Qiao,X., Roth,I., Feraille,E. and Hasler,U.
  TITLE     Different effects of ZO-1, ZO-2 and ZO-3 silencing on kidney
            collecting duct principal cell proliferation and adhesion
  JOURNAL   Cell Cycle 13 (19), 3059-3075 (2014)
   PUBMED   25486565
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Capaldo,C.T., Koch,S., Kwon,M., Laur,O., Parkos,C.A. and Nusrat,A.
  TITLE     Tight function zonula occludens-3 regulates cyclin D1-dependent
            cell proliferation
  JOURNAL   Mol Biol Cell 22 (10), 1677-1685 (2011)
   PUBMED   21411630
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Aho,S., Lupo,J., Coly,P.A., Sabine,A., Castellazzi,M., Morand,P.,
            Sergeant,A., Manet,E., Boyer,V. and Gruffat,H.
  TITLE     Characterization of the ubinuclein protein as a new member of the
            nuclear and adhesion complex components (NACos)
  JOURNAL   Biol Cell 101 (6), 319-334 (2009)
   PUBMED   18823282
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Adachi,M., Inoko,A., Hata,M., Furuse,K., Umeda,K., Itoh,M. and
            Tsukita,S.
  TITLE     Normal establishment of epithelial tight junctions in mice and
            cultured cells lacking expression of ZO-3, a tight-junction MAGUK
            protein
  JOURNAL   Mol Cell Biol 26 (23), 9003-9015 (2006)
   PUBMED   17000770
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Inoko,A., Itoh,M., Tamura,A., Matsuda,M., Furuse,M. and Tsukita,S.
  TITLE     Expression and distribution of ZO-3, a tight junction MAGUK
            protein, in mouse tissues
  JOURNAL   Genes Cells 8 (11), 837-845 (2003)
   PUBMED   14622136
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Unda,F.J., Perez-Nanclares,G., Le Morvan,V., Hernandez,C.,
            Vilaxa,A., De-la-Fuente,M. and Gorry,P.
  TITLE     Dynamic assembly of tight junction-associated proteins ZO-1, ZO-2,
            ZO-3 and occludin during mouse tooth development
  JOURNAL   Histol Histopathol 18 (1), 27-38 (2003)
   PUBMED   12507281
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234924.4, XP_001069839.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.29569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN06680417
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..907
                     /product="tight junction protein ZO-3 isoform 3"
                     /note="tight junction protein ZO-3"
                     /calculated_mol_wt=99557
     Region          15..96
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(26..32,45,48,76,80,83..84)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          190..268
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(190..196,201..217,220..222,225,227..228,235,
                     243..244,246..247,259..265)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(202..208,214,217,247,251,254..255)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          373..454
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(384..390,400,403,432,436,439..440)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          469..542
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(477,479,482,486,507..508,536,538..539)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          585..761
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..907
                     /gene="Tjp3"
                     /coded_by="NM_001108073.2:169..2892"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:314640"
                     /db_xref="RGD:1309247"
ORIGIN      
        1 mavadmeelt iweqhtatly kdprrgfgia vsgghdragg pvvvsdvvpg gpaegrlqtg
       61 dhivmvngvs venvtsafai qilktctkta nitvkrprrv qlpatkaspa sghqlsdqee
      121 adhgrgyegd sssgsgrswg ersrrsragr rvrmgshgrr sscggseang ldlvsgykrl
      181 pkqdvlmrpl ksvlvkrrns eefgvklgsq ifikhitesg laarnrglqe gdlilqingv
      241 ssanlslsdt rrlieksegq ltllvlrdsg qflvnippav sdsdsslmed isdltselsq
      301 appshipppp lksrrspeds qtdspvetpq pqrrersvds raiaepespg esrydiyrvp
      361 srqsledrgy spdtrvvrfp kgvsiglrla ggndvgifvs gvqagspadg qgiqegdeil
      421 qvndmpfrnl treeavqfll glpagedvel viqskqdifr kmvqsrvgds fyirthfele
      481 psppyglgft rgdvfhvvdt lyrgsgsghg hsshgglwla armgrdlreq ergvipnqsr
      541 aeqlasleaa qraaglgpga stgsnpraef wrlrglrrga kktmtqrsre dlsaltrqgh
      601 yppyervvlr easfkrpvvi lgpvadiamk rlttevpeqf eiaesvsrtd spskiikldt
      661 vrviaerdkh alldvtpsai erlnyvqyyp vvifcapesr salkalrewl apasrrssrr
      721 lyaqaqklqk hsghlftati plngtsdswy qevkaviqqq qarpiwtaed qlngssedld
      781 lpghglaass gdlscdsran sdyedtdgeg tytdregepq dfdeeappta larssepvwv
      841 ddhqglmghg riaaaevqad shytpdqrrq dsmrtykhea lrkkftrard iessdeegyd
      901 wgpatdl
//
LOCUS       NP_001424883             594 aa            linear   ROD 11-APR-2025
DEFINITION  AT-rich interactive domain-containing protein 3A [Rattus
            norvegicus].
ACCESSION   NP_001424883
VERSION     NP_001424883.1
DBSOURCE    REFSEQ: accession NM_001437954.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Tidwell,J.A., Schmidt,C., Heaton,P., Wilson,V. and Tucker,P.W.
  TITLE     Characterization of a new ARID family transcription factor
            (Brightlike/ARID3C) that co-activates Bright/ARID3A-mediated
            immunoglobulin gene transcription
  JOURNAL   Mol Immunol 49 (1-2), 260-272 (2011)
   PUBMED   21955986
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Nixon,J.C., Rajaiya,J. and Webb,C.F.
  TITLE     Mutations in the DNA-binding domain of the transcription factor
            Bright act as dominant negative proteins and interfere with
            immunoglobulin transactivation
  JOURNAL   J Biol Chem 279 (50), 52465-52472 (2004)
   PUBMED   15456761
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.29828.1,
                                           SRR26643284.9728.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..594
                     /product="AT-rich interactive domain-containing protein
                     3A"
                     /note="dead ringer homolog 1; AT rich interactive domain
                     3A (Bright like)"
                     /calculated_mol_wt=63464
     Region          217..349
                     /region_name="ARID_ARID3A"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 3A (ARID3A) and
                     similar proteins; cd16878"
                     /db_xref="CDD:350642"
     Site            order(259..265,290,292..293,296,304..307,309..311,313,
                     343..344)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350642"
     CDS             1..594
                     /gene="Arid3a"
                     /coded_by="NM_001437954.1:467..2251"
                     /db_xref="GeneID:314616"
                     /db_xref="RGD:1305299"
ORIGIN      
        1 mklqavmetl iqrqqrarqe learqpplpp ppepagvqar ttmtdedrep enarmhrtqm
       61 aalaamraaa aglrhpsspg gsededtaqg gtlsspalhg sgqegpghte gdghlmdmgs
      121 dddtkpkwee qeleelgeee eeededdfee eeedeeeegl glpesaslgs aglftrkapp
      181 tqtfrgdggp rmlsgperlg pgpahpshva sqmpppdhgd wtfeeqfkql yeldadpkrk
      241 eflddlfsfm qkrgtpvnri pimakqvldl fmlyvlvtek gglvevinkk lwreitkgln
      301 lptsitsaaf tlrtqymkyl ypyecerrgl sspnelqaai dsnrregrrq sfggslfays
      361 psgahsmlss pklpvtslgl aastngssit ptpkikkeed saipitvpgr lpvslaghpv
      421 vaaqaaavqa aaaqaavaaq aaaleqlrek lesteppekk malvadeqqr lmqravqqsf
      481 lamtaqlpmn irinsqases rqdpavnlts angsnsisms vemngivytg vlfaqppppt
      541 pppasskggv ssigtnntmg nrtgasgsag ssgqvglagv saptmsstsn nslp
//
LOCUS       NP_001424831             949 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001424831 XP_038934785
VERSION     NP_001424831.1
DBSOURCE    REFSEQ: accession NM_001437902.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934785.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.26756.1,
                                           SRR26643299.32861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..949
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=103214
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          645..>940
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..949
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437902.1:744..3593"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlvsth
      541 hlhssseded iegtfpnels lqqafseyqi qqmtanfvdq fgfndeefad qddninapfd
      601 riaeinfnie adedspsaal feaccsdriq pfdddeediw edeetrctar vmararfgap
      661 htsenyskka vghggqgrkt gsptarnvpg latpssptqk egprsesdsa gttwtavfde
      721 pvnplsaasg aardvgssaw aagpsvaeek gwakftdfqp fccsetgprc sspvdmdhsn
      781 aeggqspgpe kafgptspca wnvcvtrkap lvasdssssg gsdseddeka agavealcag
      841 htgkaspppr taeaaagrae cpdstvlapa cpapsevtis pavatiapsk agsptativv
      901 sssvatavpp gpimavttta paivatlgtm tkdrktdalp dgaalngpv
//
LOCUS       NP_001424906             472 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424906
VERSION     NP_001424906.1
DBSOURCE    REFSEQ: accession NM_001437977.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3039931.1,
                                           SRR26360181.119266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..472
                     /product="gasdermin D like 1 isoform 1"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=51874
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..428
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..472
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437977.1:255..1673"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelvasi lehncnqtee ttsplptgvl calksedevl ilnlvqgcgl
      421 eleksgcqlp wdptvvpqls alyacltglq lltdpspgls rtvpeeetli cp
//
LOCUS       NP_001424848             483 aa            linear   ROD 11-APR-2025
DEFINITION  S-adenosylhomocysteine hydrolase-like protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001424848 XP_006233228
VERSION     NP_001424848.1
DBSOURCE    REFSEQ: accession NM_001437919.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Harvey,K.E., LaVigne,E.K., Dar,M.S., Salyer,A.E., Pratt,E.P.S.,
            Sample,P.A., Aryal,U.K., Gowher,H. and Hockerman,G.H.
  TITLE     RyR2/IRBIT regulates insulin gene transcript, insulin content, and
            secretion in the insulinoma cell line INS-1
  JOURNAL   Sci Rep 12 (1), 7713 (2022)
   PUBMED   35562179
  REMARK    GeneRIF: RyR2/IRBIT regulates insulin gene transcript, insulin
            content, and secretion in the insulinoma cell line INS-1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Borth,H., Weber,N., Meyer,D., Wartenberg,A., Arlt,E., Zierler,S.,
            Breit,A., Wennemuth,G., Gudermann,T. and Boekhoff,I.
  TITLE     The IP3 R Binding Protein Released With Inositol
            1,4,5-Trisphosphate Is Expressed in Rodent Reproductive Tissue and
            Spermatozoa
  JOURNAL   J Cell Physiol 231 (5), 1114-1129 (2016)
   PUBMED   26439876
  REMARK    GeneRIF: The present study documents that IRBIT is expressed in
            Leydig and Sertoli cells.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Ando,H., Hirose,M., Gainche,L., Kawaai,K., Bonneau,B., Ijuin,T.,
            Itoh,T., Takenawa,T. and Mikoshiba,K.
  TITLE     IRBIT Interacts with the Catalytic Core of Phosphatidylinositol
            Phosphate Kinase Type Ialpha and IIalpha through Conserved
            Catalytic Aspartate Residues
  JOURNAL   PLoS One 10 (10), e0141569 (2015)
   PUBMED   26509711
  REMARK    GeneRIF: IRBIT forms signaling complexes with PIPKIalpha and
            NBCe1-B, whose activity is regulated by PI(4,5)P2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Park,S., Shcheynikov,N., Hong,J.H., Zheng,C., Suh,S.H., Kawaai,K.,
            Ando,H., Mizutani,A., Abe,T., Kiyonari,H., Seki,G., Yule,D.,
            Mikoshiba,K. and Muallem,S.
  TITLE     Irbit mediates synergy between ca(2+) and cAMP signaling pathways
            during epithelial transport in mice
  JOURNAL   Gastroenterology 145 (1), 232-241 (2013)
   PUBMED   23542070
REFERENCE   5  (residues 1 to 483)
  AUTHORS   He,P., Klein,J. and Yun,C.C.
  TITLE     Activation of Na+/H+ exchanger NHE3 by angiotensin II is mediated
            by inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3 (IRBIT) and Ca2+/calmodulin-dependent protein
            kinase II
  JOURNAL   J Biol Chem 285 (36), 27869-27878 (2010)
   PUBMED   20584908
  REMARK    GeneRIF: IRBIT is critically involved in mediating activation of
            NHE3 by ANG II via a Ca(2+)/calmodulin-dependent protein kinases
            II-dependent pathway.
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Ando,H., Mizutani,A. and Mikoshiba,K.
  TITLE     An IRBIT homologue lacks binding activity to inositol
            1,4,5-trisphosphate receptor due to the unique N-terminal appendage
  JOURNAL   J Neurochem 109 (2), 539-550 (2009)
   PUBMED   19220705
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Yang,D., Shcheynikov,N., Zeng,W., Ohana,E., So,I., Ando,H.,
            Mizutani,A., Mikoshiba,K. and Muallem,S.
  TITLE     IRBIT coordinates epithelial fluid and HCO3- secretion by
            stimulating the transporters pNBC1 and CFTR in the murine
            pancreatic duct
  JOURNAL   J Clin Invest 119 (1), 193-202 (2009)
   PUBMED   19033647
REFERENCE   8  (residues 1 to 483)
  AUTHORS   He,P., Zhang,H. and Yun,C.C.
  TITLE     IRBIT, inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3
            activity in response to calcium
  JOURNAL   J Biol Chem 283 (48), 33544-33553 (2008)
   PUBMED   18829453
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Shirakabe,K., Priori,G., Yamada,H., Ando,H., Horita,S., Fujita,T.,
            Fujimoto,I., Mizutani,A., Seki,G. and Mikoshiba,K.
  TITLE     IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
            specifically binds to and activates pancreas-type Na+/HCO3-
            cotransporter 1 (pNBC1)
  JOURNAL   Proc Natl Acad Sci U S A 103 (25), 9542-9547 (2006)
   PUBMED   16769890
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Ando,H., Mizutani,A., Matsu-ura,T. and Mikoshiba,K.
  TITLE     IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
            protein, is released from the IP3 receptor upon IP3 binding to the
            receptor
  JOURNAL   J Biol Chem 278 (12), 10602-10612 (2003)
   PUBMED   12525476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006233228.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2272302.1,
                                           SRR26643298.12967.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..483
                     /product="S-adenosylhomocysteine hydrolase-like protein 1
                     isoform 3"
                     /EC_number="3.13.2.1"
                     /note="S-adenosylhomocysteine hydrolase-like 1; putative
                     adenosylhomocysteinase 2; adoHcyase 2;
                     S-adenosyl-L-homocysteine hydrolase 2;
                     S-adenosylhomocysteine hydrolase-like protein 1;
                     IP3R-binding protein released with inositol
                     1,4,5-trisphosphate"
                     /calculated_mol_wt=53623
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Region          18..45
                     /region_name="PEST.
                     /evidence=ECO:0000250|UniProtKB:O43865,
                     ECO:0000250|UniProtKB:Q80SW1"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKD.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80SW1; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Region          59..482
                     /region_name="AdoHcyase"
                     /note="S-adenosyl-L-homocysteine hydrolase; smart00996"
                     /db_xref="CDD:214963"
     Site            order(68,71,75,78..79,213,216..217,233,235,239..240,244,
                     247..248,252,255..256,259..265,273..274,277,286..287,289,
                     294..302,304..307,309..312,315,328..332,342..344,355,
                     372..373,378,402,404,406..407,410,436,442..443,446..447,
                     450,453..454,456..458,460,463..464,467..468)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:240619"
     Region          91..154
                     /region_name="Interaction with BCL2L10.
                     /evidence=ECO:0000250|UniProtKB:O43865"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            order(106,108,110..111,182,207..208,237,241,398,403,408,
                     412)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240619"
     Site            order(208..210,242,246,271,273..275,293..296,299,326..329,
                     332,350..352,395,397,403)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240619"
     Region          234..401
                     /region_name="NAD binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Region          473..483
                     /region_name="PDZ-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     CDS             1..483
                     /gene="Ahcyl1"
                     /gene_synonym="IRBIT"
                     /coded_by="NM_001437919.1:797..2248"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362013"
                     /db_xref="RGD:1309768"
ORIGIN      
        1 mqeftkfptk tgrrslsrsi sqsstdsyss aasytdssdd evsprekqqt nskgssnfcv
       61 knikqaefgr reieiaeqdm salislrkra qgekplagak ivgcthitaq tavlietlca
      121 lgaqcrwsac niystqneva aalaeagvav fawkgesedd fwwcidrcvn mdgwqanmil
      181 ddggdlthwv ykkypnvfkk irgiveesvt gvhrlyqlsk agklcvpamn vndsvtkqkf
      241 dnlyccresi ldglkrttdv mfggkqvvvc gygevgkgcc aalkalgaiv yiteidpica
      301 lqacmdgfrv vklnevirqv dvvitctgnk nvvtrehldr mknscivcnm ghsnteidvt
      361 slrtpeltwe rvrsqvdhvi wpdgkrvvll aegrllnlsc stvptfvlsi tattqalali
      421 elynapegry kqdvyllpkk mdeyvaslhl psfdahltel tddqakylgl nkngpfkpny
      481 yry
//
LOCUS       NP_001129286             478 aa            linear   ROD 11-APR-2025
DEFINITION  alpha-1,3-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase C isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001129286 XP_001080664 XP_235099
VERSION     NP_001129286.1
DBSOURCE    REFSEQ: accession NM_001135814.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Oct 16, 2008 this sequence version replaced
            XP_235099.4, XP_001080664.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2633840.1,
                                           SRR26360176.1744583.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..478
                     /product="alpha-1,3-mannosyl-glycoprotein
                     4-beta-N-acetylglucosaminyltransferase C isoform 1"
                     /EC_number="2.4.1.145"
                     /note="alpha-1,3-mannosyl-glycoprotein
                     4-beta-N-acetylglucosaminyltransferase C; mannosyl
                     (alpha-1,3-)-glycoprotein
                     beta-1,4-N-acetylglucosaminyltransferase, isozyme C
                     (putative)"
                     /calculated_mol_wt=56084
     Region          64..330
                     /region_name="Glyco_transf_54"
                     /note="N-Acetylglucosaminyltransferase-IV (GnT-IV)
                     conserved region; pfam04666"
                     /db_xref="CDD:461384"
     CDS             1..478
                     /gene="Mgat4c"
                     /gene_synonym="RGD1307871"
                     /coded_by="NM_001135814.2:246..1682"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:299756"
                     /db_xref="RGD:1307871"
ORIGIN      
        1 mfkfyqmkyi fqildkmrcl rkrstvsflg vlvvfllfmn vfiedsyvle gdkqlirets
       61 thqlnseryv htfkdlsnfs gtinvtyryl aatplqrkry ltiglssvkr kkgnylleti
      121 ksifeqssye elkeisvvvh ladfnsswrd amvqditqkf ahhiiagrlm vihapeeyyp
      181 vldglkrnyn dpedrvrfrs kqnvdyafll nfcantsdyy vmleddvrcs rnfltaikkv
      241 iaslegtywv tlefsklgyi gklyhshdlp rlahfllmfy qempcdwllt hfrgllaqkn
      301 virfkpslfq hmgyyssykg tenklkdddf eeesfdipdn ppaslytnmn vfenyeaska
      361 yssvdeyfwg kppstgdtfv ivfenpikik kikvntgted rqndilhhga ldvgeklifs
      421 kqirqcetyl rlgefkngnf emsdvnqkip fdihcmricv tktqkewlii rsisiwts
//
LOCUS       NP_001424902             265 aa            linear   ROD 11-APR-2025
DEFINITION  AP-1 complex-associated regulatory protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424902 XP_038958645
VERSION     NP_001424902.1
DBSOURCE    REFSEQ: accession NM_001437973.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Maritzen,T., Zech,T., Schmidt,M.R., Krause,E., Machesky,L.M. and
            Haucke,V.
  TITLE     Gadkin negatively regulates cell spreading and motility via
            sequestration of the actin-nucleating ARP2/3 complex
  JOURNAL   Proc Natl Acad Sci U S A 109 (26), 10382-10387 (2012)
   PUBMED   22689987
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schmidt,M.R., Maritzen,T., Kukhtina,V., Higman,V.A., Doglio,L.,
            Barak,N.N., Strauss,H., Oschkinat,H., Dotti,C.G. and Haucke,V.
  TITLE     Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin
            KIF5 complex
  JOURNAL   Proc Natl Acad Sci U S A 106 (36), 15344-15349 (2009)
   PUBMED   19706427
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038958645.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2014064.1,
                                           SRR26643289.7684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..265
                     /product="AP-1 complex-associated regulatory protein
                     isoform 2"
                     /note="AP-1 complex-associated regulatory protein"
                     /calculated_mol_wt=29756
     Region          24..265
                     /region_name="AP1AR"
                     /note="AP-1 complex-associated regulatory protein;
                     pfam15745"
                     /db_xref="CDD:464841"
     CDS             1..265
                     /gene="Ap1ar"
                     /gene_synonym="RGD1311435"
                     /coded_by="NM_001437973.1:220..1017"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362037"
                     /db_xref="RGD:1311435"
ORIGIN      
        1 mgnccwtqcf gllrreagrl qragggskyf rtcprgehlt iefenlvesd egespgsshr
       61 plteeeivdl qerhydsiae kqkdvdrkiq reqekqriaq ryhpssgdcq svgpeddfea
      121 slrniksqye vfrssrlssd atvltpntes scdlmtktks tsgnddstsl dlewedeegm
      181 nrmlpmrers kteedilraa lkcsskkgsn ptsasddsng lewendfvsa emddngnsey
      241 agfvnpvlel sesaikqsdt dqqir
//
LOCUS       NP_001019969            1105 aa            linear   ROD 11-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 1 [Rattus norvegicus].
ACCESSION   NP_001019969 XP_342285
VERSION     NP_001019969.2
DBSOURCE    REFSEQ: accession NM_001024798.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1105)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1105)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1105)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1105)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Sep 11, 2008 this sequence version replaced NP_001019969.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1105
                     /product="ubiquitin-associated protein 2-like isoform 1"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=116732
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          516..543
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1105
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001024798.3:124..3441"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgref rgqengldgt ksggpsgrgt drgrrgrgrg
      181 rgssgrrggr fsaqgmgtfn padyaepant ddnygsssgn twnntghfep ddgtrldfig
      241 vegsnyprkf etapgawrta teewgtedwn edlsetkift asnvssvplp aenvtitagq
      301 ridlavllgk tpssmendss nldpsqapsl aqplvfsnsk qnaisqpasg ntfshhsmvs
      361 mlgkgfgdvg eakggsttgs qfleqfktaq alaqlaaqhs qsgstttssw dmgsttqsps
      421 lvqydlksan dstvhspftk rqaftpsstm mevflqekpp avatstaapp ppssplpsks
      481 tsapqmspgs sdnqssspqp aqqklkqqkk ktsltskipa lavempgsad isglnlqfga
      541 lqfgsepvls dyestpttsa sssqapssly tstasessst vssnqsqesg yqsgpiqstt
      601 ytsqnnaqgp lyeqrstqtr rypssisssp qkdltqakng fssvqatqlq ttqsvegatg
      661 savksespst ssipslnetv paasllttas qhssslsgls hseeipnttt tqhssalstq
      721 qntlssstss grtststllh tsveseanlh sssstfstts stvsapppvv svssslnsgs
      781 slglslgsns tvtastrssv attsgkappn lppgvppllp npyimapgll hayppqvygy
      841 ddlqmlqtrf pldyysipfp tpttpltgrd gslasnpysg dltkfgrgda sspapattla
      901 qpqqnqtqth httqqtflnp alppgysyts lpyytgvpgl pstfqygpav fpvaptsskq
      961 hgvnvsvnas atpfqqpsgy gshgyntgvs vtssntgvpd isgsvysktq qsfekqgfhs
     1021 gtpaasfnlp salgsggpin pataaayppa pfmhiltphq qphsqilhhh lqqdgqlpyl
     1081 qmilccqrqq eeqdiltlvd dqlge
//
LOCUS       NP_001424832             922 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001424832 XP_063119408
VERSION     NP_001424832.1
DBSOURCE    REFSEQ: accession NM_001437903.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119408.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.31379.1,
                                           SRR26643295.29803.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..922
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=100195
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          618..>913
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..922
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437903.1:616..3384"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlafse
      541 yqiqqmtanf vdqfgfndee fadqddnina pfdriaeinf nieadedsps aalfeaccsd
      601 riqpfdddee diwedeetrc tarvmararf gaphtsenys kkavghggqg rktgsptarn
      661 vpglatpssp tqkegprses dsagttwtav fdepvnplsa asgaardvgs sawaagpsva
      721 eekgwakftd fqpfccsetg prcsspvdmd hsnaeggqsp gpekafgpts pcawnvcvtr
      781 kaplvasdss ssggsdsedd ekaagaveal caghtgkasp pprtaeaaag raecpdstvl
      841 apacpapsev tispavatia pskagsptat ivvsssvata vppgpimavt ttapaivatl
      901 gtmtkdrktd alpdgaalng pv
//
LOCUS       NP_001099229            2058 aa            linear   ROD 11-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001099229 XP_001078910 XP_224538
VERSION     NP_001099229.2
DBSOURCE    REFSEQ: accession NM_001105759.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2058)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2058)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2058)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2058)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2058)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Jul 9, 2010 this sequence version replaced NP_001099229.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments and orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2058
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2058
                     /product="dedicator of cytokinesis protein 9 isoform 4"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=234675
     Region          45..155
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          169..292
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          636..825
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1600..2014
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1704,1714,1716..1717,1719..1720,1723..1724,
                     1726..1727,1730..1731)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1738..1741,1743,1772..1773,1775..1778,1780..1781,
                     1800..1802,1819,1821,1850,1852,1859..1860,1866,1905..1906,
                     1909,1923,1925,1929,1932..1934,1937..1940,1942..1943,1946,
                     1974,1992..1993,1995..1996,1999)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1937..1942
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2058
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001105759.3:269..6445"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 maqqqlpvst etrkftrals kpgtaaelrq svsevvrgsv llakpkliep ldyenvivqk
       61 ktqilndclr emllfpyddf qtailrrqgr yvrstvpana eeeaqslfvt eciktynsdw
      121 hlvtyhyedy sgefrqlpnk vakldklpvh vyevdeeadk dedaaslgsq kggitkhgwl
      181 ykgnmnsais vtmrsfkrrf fhliqlgdgs ynlnfykdek iskepkgsif ldscmgviqn
      241 nrvrrfafel kmqdkssyll aadseaemee wvtvlnkilq lnfeaamqek rngdphedde
      301 qsklegsgsg ldsylpelak streaeiklk sesrvklfyl dpdtqkldfs saepevkpfe
      361 ekfgkrilvk cndlsfnlqc cvaeneegpt tnvepffvtl slfdikynrk isadfhvdln
      421 hfsvrqmlap aspvlmnggq sppafqdalq aamqypkqgi fsvtcphpdi flvariekvl
      481 qgsithcaep ymkssdsskv aqkvlknakq acqrlgqyrm pfawaartlf kdtsgnldkn
      541 arfsaiyrqd snklsnedml klladfrkpe kmaklpvilg nlditidnvs cdfpnylnss
      601 yipmrqfetc skspitfeve efvpcipkht qpytvysnhl yvypkylryd sqksfakarn
      661 iaiciefkds deedsqplkc iygrpggpvf trsalaavlh hqqspefyde ikielpaqlh
      721 ekhhllftff hvscdnstkg stkkkdavet qvgfswlpll kdgrvltneq hipvsanlps
      781 gylgyqelsm grhygpevkw veggkpllki sthlvstvyt qdqhlhnffq ycqktesgaq
      841 asgselvkyl kslhameghv miaflptiln qlfrvltrat qeevavnvtr viihvvaqch
      901 eegleshlrs yvkfaykaep yiaseyktvh eeltksmtti lkpsadflts nkllkyswff
      961 fdvliksmaq hliennkvkl lrnqrfpasy hhavetvvnm lmphitqkfr dnpeasknan
     1021 hslavfikrc ftfmdrgfvf kqinnyiscf apgdpktlfe ykfeflrvvc nhehyiplnl
     1081 pmpfgkgriq ryqdlqldys ltdefcrnhf lvglllrevg talqefrevr viavsvlknl
     1141 likhsfddry tsrshqaria tlylplfgll ienvqrinvr dvspfpvnpg siskdealav
     1201 ptgnplmtpq kgntldhslh kdllgaisgi aspytastpn insvrnadsr gslistdsgn
     1261 slpdrnpeks nsldkqqsgm lgnsvvrcdk ldqseiksll mcflyvlksm sddalftywn
     1321 kastaelmdf ftisevclhq fqymgkryia svrkissvlg isvdngyghs eadvahqsll
     1381 eaniatevcl taldtlslft lafknqllad hghnplmkkv fdvylcflqk hqsemalknv
     1441 ftalrsliyk fpstfyegra dmcaslcyev lkccnsklss irteasqlly flmrnnfdyt
     1501 gkksfvrthl qviisvsqli advvgiggtr fqqslsiinn cansdrlikh tsfssdvkdl
     1561 tkrirtvlma taqmkehend pemlvdlqys laksyastpe lrktwldsma rihvkngdls
     1621 eaamcyvhvt alvaeyltrk gmfrqgctaf rvitpnidee asmmedvgmq dvhfnedvlm
     1681 elleqcadgl wkaeryelia diykliipiy ekrrdferla hlydtlhray skvtevmhsg
     1741 rrllgtyfrv affgqgffed edgkeyiyke pkltplseis qrllklysdk fgsenvkmiq
     1801 dsgkvnpkdl dskfayiqvt hvtpffdeke lqerktefer chnirrfmfe mpftqtgkrq
     1861 ggveeqckrr tiltaihcfp yvkkripvmy qhhtdlnpie vaidemskkv aelrqlcssa
     1921 evdmiklqlk lqgsvsvqvn agplayaraf lddtntkryp dnkvkllkev frqfveacgq
     1981 alavnerlik edqleyqeem kanyremake lsdimreqic pleektsvlp nslhifnais
     2041 gtptstvvqg ltssssvv
//
LOCUS       NP_001424885             233 aa            linear   ROD 11-APR-2025
DEFINITION  caspase-14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424885
VERSION     NP_001424885.1
DBSOURCE    REFSEQ: accession NM_001437956.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Gkegkes,I.D., Aroni,K., Agrogiannis,G., Patsouris,E.S. and
            Konstantinidou,A.E.
  TITLE     Expression of caspase-14 and keratin-19 in the human epidermis and
            appendages during fetal skin development
  JOURNAL   Arch Dermatol Res 305 (5), 379-387 (2013)
   PUBMED   23377137
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Alibardi,L., Tschachler,E. and Eckhart,L.
  TITLE     Distribution of caspase-14 in epidermis and hair follicles is
            evolutionarily conserved among mammals
  JOURNAL   Anat Rec A Discov Mol Cell Evol Biol 286 (2), 962-973 (2005)
   PUBMED   16142807
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.27729.1,
                                           SRR26643295.27357.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..233
                     /product="caspase-14 isoform 1"
                     /calculated_mol_wt=26710
     Region          10..233
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cl00042"
                     /db_xref="CDD:444667"
     Site            order(33,94,128,167..172,176..177)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(129,152..153,160,163,166,190,198,204,217,222..223,
                     225,228..229)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(130,151)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     CDS             1..233
                     /gene="Casp14"
                     /coded_by="NM_001437956.1:181..882"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:299587"
                     /db_xref="RGD:1311781"
ORIGIN      
        1 mdsetinpqp lqeerydmsg arlaltlcvt karegsevdm dalermfqyl kfestmkrdp
       61 taqqflddmd efqqtienwk epvscafvvl mahgeegflk gedgnmvrle dlfevlnnkn
      121 ckalrehrdp geelpgdela vikkknppti ptytdmihiy stvegflsyr hdqkgsgfiq
      181 tltdvfihkk gsitelleei trlmantevm qegkprkvnp eiqstlrkkl ylq
//
LOCUS       NP_001424864             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424864 XP_006242453
VERSION     NP_001424864.1
DBSOURCE    REFSEQ: accession NM_001437935.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006242453.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2786621.1,
                                           SRR26360172.2730191.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437935.1:195..770"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424841            1088 aa            linear   ROD 11-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424841 XP_063138219
VERSION     NP_001424841.1
DBSOURCE    REFSEQ: accession NM_001437912.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1088)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1088)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1088)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1088)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063138219.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.3161.1,
                                           SRR26643295.9797.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1088
                     /product="ubiquitin-associated protein 2-like isoform 6"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=114626
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          516..543
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1088
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001437912.1:124..3390"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgref rgqengldgt ksggpsgrgt drgrrgrgrg
      181 rgssgrrggr fsaqgmgtfn padyaepant ddnygsssgn twnntghfep ddgtrldfig
      241 vegsnyprkf etapgawrta teewgtedwn edlsetkift asnvssvplp aenvtitagq
      301 ridlavllgk tpssmendss nldpsqapsl aqplvfsnsk qnaisqpasg ntfshhsmvs
      361 mlgkgfgdvg eakggsttgs qfleqfktaq alaqlaaqhs qsgstttssw dmgsttqsps
      421 lvqydlksan dstvhspftk rqaftpsstm mevflqekpp avatstaapp ppssplpsks
      481 tsapqmspgs sdnqssspqp aqqklkqqkk ktsltskipa lavempgsad isglnlqfga
      541 lqfgsepvls dyestpttsa sssqapssly tstasessst vssnqsqesg yqsgpiqstt
      601 ytsqnnaqgp lyeqrstqtr rypssisssp qkdltqakng fssvqatqlq ttqsvegatg
      661 savksespst ssipslnetv paasllttas qhssslsgls hseeipnttt tqhssalstq
      721 qntlssstss grtststllh tsveseanlh sssstfstts stvsapppvv svssslnsgs
      781 slglslgsns tvtastrssv attsgkappn lppgvppllp npyimapgll hayppqvygy
      841 ddlqmlqtrf pldyysipfp tpttpltgrd gslasnpysg dltkfgrgda sspapattla
      901 qpqqnqtqth httqqtflnp alppgysyts lpyytgvpgl pstfqygpav fpvaptsskq
      961 hgvnvsvnas atpfqqpsgy gshgyntgvs vtssntgvpd isgsvysktq qsfekqgfhs
     1021 gtpaasfnlp salgsggpin pataaayppa pfmhiltphq qphsqilhhh lqqdgqdilt
     1081 lvddqlge
//
LOCUS       NP_001424891             461 aa            linear   ROD 11-APR-2025
DEFINITION  midnolin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424891 XP_017450304
VERSION     NP_001424891.1
DBSOURCE    REFSEQ: accession NM_001437962.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Obara,Y. and Ishii,K.
  TITLE     Transcriptome Analysis Reveals That Midnolin Regulates mRNA
            Expression Levels of Multiple Parkinson's Disease Causative Genes
  JOURNAL   Biol Pharm Bull 41 (1), 20-23 (2018)
   PUBMED   29311479
  REMARK    GeneRIF: These findings indicate that MIDN regulates the expression
            of a wide variety of genes, including multiple Parkinson's Disease
            causative genes and is associated with Parkinson's Disease onset.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Obara,Y., Imai,T., Sato,H., Takeda,Y., Kato,T. and Ishii,K.
  TITLE     Midnolin is a novel regulator of parkin expression and is
            associated with Parkinson's Disease
  JOURNAL   Sci Rep 7 (1), 5885 (2017)
   PUBMED   28724963
  REMARK    GeneRIF: MIDN promotes the expression of parkin E3 ubiquitin
            ligase, and that MIDN loss can trigger Parkinson's disease-related
            pathogenic mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Hofmeister-Brix,A., Kollmann,K., Langer,S., Schultz,J., Lenzen,S.
            and Baltrusch,S.
  TITLE     Identification of the ubiquitin-like domain of midnolin as a new
            glucokinase interaction partner
  JOURNAL   J Biol Chem 288 (50), 35824-35839 (2013)
   PUBMED   24187134
  REMARK    GeneRIF: midnolin plays a role in cellular signaling of adult
            tissues and regulates glucokinase enzyme activity in pancreatic
            beta cells
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Tsukahara,M., Suemori,H., Noguchi,S., Ji,Z.S. and Tsunoo,H.
  TITLE     Novel nucleolar protein, midnolin, is expressed in the
            mesencephalon during mouse development
  JOURNAL   Gene 254 (1-2), 45-55 (2000)
   PUBMED   10974535
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_017450304.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38089.1,
                                           SRR26643295.27268.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN09345330 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..461
                     /product="midnolin isoform 2"
                     /note="midbrain nucleolar protein"
                     /calculated_mol_wt=48672
     Region          32..101
                     /region_name="Ubl_midnolin"
                     /note="ubiquitin-like (Ubl) domain found in midnolin and
                     similar proteins; cd01804"
                     /db_xref="CDD:340502"
     CDS             1..461
                     /gene="Midn"
                     /coded_by="NM_001437962.1:475..1860"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314623"
                     /db_xref="RGD:1309629"
ORIGIN      
        1 mepqpggars crrgapggac elsttaesaa pmslaihstt gtrydlsvph detveglrkr
       61 lsqrlkvpke rlallhkdtr lssgklqefg vgdgskltlv ptveaglmsq asrpeqsvmq
      121 alesltetqv sdflsgrspl tlalrvgdhm mfvqlqlaaq haplqhrhvl aaaaaaaaaa
      181 rgdssiatpv sspcrpvssa arvppvsssp sspvspspvt agtfqshaas ttcpetdcsp
      241 passnttstp gssptprsrk pgaviesfvn hapgvfsgtf sgtlhpncqd ssgrprrdig
      301 tilqilndll satrhyqgmp asltqlrcha qcspaspapd ltpkttscek latpsllqgq
      361 sqirmckppg drlrqtenra trckverlql llqqkrlrrk arrdargpyh wtpsrkagrs
      421 dssssggggs pseatglgld fedsvwkpev npdiqsefvv a
//
LOCUS       NP_955795                298 aa            linear   ROD 11-APR-2025
DEFINITION  cyclin-dependent kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_955795 XP_343146
VERSION     NP_955795.1
DBSOURCE    REFSEQ: accession NM_199501.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Matveevsky,S., Chassovnikarova,T., Grishaeva,T., Atsaeva,M.,
            Malygin,V., Bakloushinskaya,I. and Kolomiets,O.
  TITLE     Kinase CDK2 in Mammalian Meiotic Prophase I: Screening for Hetero-
            and Homomorphic Sex Chromosomes
  JOURNAL   Int J Mol Sci 22 (4), 1969 (2021)
   PUBMED   33671248
  REMARK    GeneRIF: Kinase CDK2 in Mammalian Meiotic Prophase I: Screening for
            Hetero- and Homomorphic Sex Chromosomes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Peng,T., Peng,J.J., Miao,G.Y., Tan,Z.Q., Liu,B. and Zhou,E.
  TITLE     miR-125/CDK2 axis in cochlear progenitor cell proliferation
  JOURNAL   Mol Med Rep 23 (2) (2021)
   PUBMED   33300064
  REMARK    GeneRIF: miR125/CDK2 axis in cochlear progenitor cell
            proliferation.
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Ren,S., Xing,Y., Wang,C., Jiang,F., Liu,G., Li,Z., Jiang,T., Zhu,Y.
            and Piao,D.
  TITLE     Fraxetin inhibits the growth of colon adenocarcinoma cells via the
            Janus kinase 2/signal transducer and activator of transcription 3
            signalling pathway
  JOURNAL   Int J Biochem Cell Biol 125, 105777 (2020)
   PUBMED   32504672
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Lin,Z., Liu,Z., Wang,X., Qiu,C. and Zheng,S.
  TITLE     MiR-21-3p Plays a Crucial Role in Metabolism Alteration of Renal
            Tubular Epithelial Cells during Sepsis Associated Acute Kidney
            Injury via AKT/CDK2-FOXO1 Pathway
  JOURNAL   Biomed Res Int 2019, 2821731 (2019)
   PUBMED   31223614
  REMARK    GeneRIF: MiR-21-3p mediates metabolism and cell fate alterations of
            tubular epithelial cells (TECs) via manipulating AKT/CDK2-FOXO1
            pathway, and that is crucial in the regulation of energy metabolism
            of TECs during Sepsis and associated acute kidney injury.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Hirai,H., Roussel,M.F., Kato,J.Y., Ashmun,R.A. and Sherr,C.J.
  TITLE     Novel INK4 proteins, p19 and p18, are specific inhibitors of the
            cyclin D-dependent kinases CDK4 and CDK6
  JOURNAL   Mol Cell Biol 15 (5), 2672-2681 (1995)
   PUBMED   7739547
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Kotani,S., Endo,T., Kitagawa,M., Higashi,H. and Onaya,T.
  TITLE     A variant form of cyclin-dependent kinase 2 (Cdk2) in a malignantly
            transformed rat thyroid (FRTL-Tc) cell line
  JOURNAL   Oncogene 10 (4), 663-669 (1995)
   PUBMED   7862443
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Tsai,L.H., Harlow,E. and Meyerson,M.
  TITLE     Isolation of the human cdk2 gene that encodes the cyclin A- and
            adenovirus E1A-associated p33 kinase
  JOURNAL   Nature 353 (6340), 174-177 (1991)
   PUBMED   1653904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Jan 24, 2004 this sequence version replaced XP_343146.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061832.1, SRR26360176.1411493.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..298
                     /product="cyclin-dependent kinase 2 isoform 1"
                     /EC_number="2.7.11.22"
                     /note="cell division protein kinase 2; cyclin dependent
                     kinase 2-alpha"
                     /calculated_mol_wt=33756
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Region          3..286
                     /region_name="STKc_CDK2_3"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Cyclin-Dependent protein Kinase 2 and 3; cd07860"
                     /db_xref="CDD:270844"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            9
                     /site_type="other"
                     /note="CDK7 binding.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            order(10..13,18,31,33,50,64,80..83,86,88..89,127,129,
                     131..132,134,145,148,160,162..165,167,205..206)
                     /site_type="active"
                     /db_xref="CDD:270844"
     Site            order(10..13,18,31,33,64,80..83,86,89,131..132,134,145)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270844"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by WEE1.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            order(37,41..44,46,49..50,52..53,56..57,71..73,116,
                     119..122,150..152,154..155,157..160,272,276..278)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270844"
     Site            order(50,88,127,129,148,160,162..165,167,205..206)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270844"
     Site            88..89
                     /site_type="other"
                     /note="CDK7 binding.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            144..167
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270844"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CAK and CCRK.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     Site            166
                     /site_type="other"
                     /note="CDK7 binding.
                     /evidence=ECO:0000250|UniProtKB:P24941; propagated from
                     UniProtKB/Swiss-Prot (Q63699.1)"
     CDS             1..298
                     /gene="Cdk2"
                     /coded_by="NM_199501.3:190..1086"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362817"
                     /db_xref="RGD:70486"
ORIGIN      
        1 menfqkveki gegtygvvyk aknkltgevv alkkirldte tegvpstair eisllkelnh
       61 pnivklldvi htenklylvf eflhqdlkkf mdasaltgip lpliksylfq llqglafchs
      121 hrvlhrdlkp qnllinaegs ikladfglar afgvpvrtyt hevvtlwyra peillgckyy
      181 stavdiwslg cifaemvtrr alfpgdseid qlfrifrtlg tpdevvwpgv tsmpdykpsf
      241 pkwarqdfsk vvppldedgr sllsqmlhyd pnkrisakaa lahpffqdvt kpvphlrl
//
LOCUS       NP_001424910             472 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424910 XP_063119593
VERSION     NP_001424910.1
DBSOURCE    REFSEQ: accession NM_001437981.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119593.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.939020.1,
                                           SRR26643293.41276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..472
                     /product="gasdermin D like 1 isoform 1"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=51874
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..428
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..472
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437981.1:334..1752"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelvasi lehncnqtee ttsplptgvl calksedevl ilnlvqgcgl
      421 eleksgcqlp wdptvvpqls alyacltglq lltdpspgls rtvpeeetli cp
//
LOCUS       NP_001424866             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424866 XP_038934871
VERSION     NP_001424866.1
DBSOURCE    REFSEQ: accession NM_001437937.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934871.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.352365.1,
                                           SRR26360190.853824.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437937.1:199..774"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424909             460 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424909 XP_038935092
VERSION     NP_001424909.1
DBSOURCE    REFSEQ: accession NM_001437980.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038935092.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1673690.1,
                                           SRR26360186.948703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..460
                     /product="gasdermin D like 1 isoform 2"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=50819
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..>380
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..460
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437980.1:269..1651"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelaqel cksicdmltr vlllyggkvr pqgevalqgn tgqavlpcvs
      421 cigllrsich mtkqnkllrf qpivpmtiqc qsmgssqlnk
//
LOCUS       NP_001424835             554 aa            linear   ROD 11-APR-2025
DEFINITION  aladin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424835 XP_008763927
VERSION     NP_001424835.1
DBSOURCE    REFSEQ: accession NM_001437906.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Juhlen,R., Landgraf,D., Huebner,A. and Koehler,K.
  TITLE     Identification of a novel putative interaction partner of the
            nucleoporin ALADIN
  JOURNAL   Biol Open 5 (11), 1697-1705 (2016)
   PUBMED   27754849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Carvalhal,S., Ribeiro,S.A., Arocena,M., Kasciukovic,T., Temme,A.,
            Koehler,K., Huebner,A. and Griffis,E.R.
  TITLE     The nucleoporin ALADIN regulates Aurora A localization to ensure
            robust mitotic spindle formation
  JOURNAL   Mol Biol Cell 26 (19), 3424-3438 (2015)
   PUBMED   26246606
REFERENCE   3  (residues 1 to 554)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Huebner,A., Mann,P., Rohde,E., Kaindl,A.M., Witt,M., Verkade,P.,
            Jakubiczka,S., Menschikowski,M., Stoltenburg-Didinger,G. and
            Koehler,K.
  TITLE     Mice lacking the nuclear pore complex protein ALADIN show female
            infertility but fail to develop a phenotype resembling human triple
            A syndrome
  JOURNAL   Mol Cell Biol 26 (5), 1879-1887 (2006)
   PUBMED   16479006
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Brooks,B.P., Kleta,R., Stuart,C., Tuchman,M., Jeong,A.,
            Stergiopoulos,S.G., Bei,T., Bjornson,B., Russell,L., Chanoine,J.P.,
            Tsagarakis,S., Kalsner,L. and Stratakis,C.
  TITLE     Genotypic heterogeneity and clinical phenotype in triple A
            syndrome: a review of the NIH experience 2000-2005
  JOURNAL   Clin Genet 68 (3), 215-221 (2005)
   PUBMED   16098009
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Storr,H.L., Clark,A.J., Priestley,J.V. and Michael,G.J.
  TITLE     Identification of the sites of expression of triple A syndrome mRNA
            in the rat using in situ hybridisation
  JOURNAL   Neuroscience 131 (1), 113-123 (2005)
   PUBMED   15680696
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Cronshaw,J.M. and Matunis,M.J.
  TITLE     The nuclear pore complex protein ALADIN is mislocalized in triple A
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (10), 5823-5827 (2003)
   PUBMED   12730363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_008763927.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.28962.1,
                                           SRR26643293.43512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..554
                     /product="aladin isoform 2"
                     /note="achalasia, adrenocortical insufficiency, alacrimia
                     (Allgrove, triple-A)"
                     /calculated_mol_wt=59899
     Region          165..201
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <166..425
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          205..251
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          255..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          299..336
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..554
                     /gene="Aaas"
                     /coded_by="NM_001437906.1:143..1807"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300259"
                     /db_xref="RGD:1308701"
ORIGIN      
        1 mcslglfppp pprgqvtlye hnnelvtgns yespppdfrg qvvgvgdaaw inlpvlhltk
       61 dplkapgrld hgtraafihh reqvwkrcin vwhdvglfgv lneianseee vfewvktass
      121 walalcgras slhgslfphl slrsedliae faqvtnwssc clrvfawhph tnkfavalld
      181 dsirvynans tivpslkhrl qrnvaalawk plsasvlava cqsciliwtl dptslstrps
      241 sgcaqvlshp ghtpvtslaw apnggwllsa spvdavilvw dvstetcvpl pwfrgggvtn
      301 llwspdgskv lattpsavfr vwearmwtce gwptlsgrcq tgcwspdgkr llftvlgeal
      361 iyslsfpepc gtekghvgga ksativadls ettiqtpdge erlggeaham vwdpsgerla
      421 vlmkgnprvq dgnpvillfr trnspvfell pcgviqgepg aqaqlvsfhp afnkgallsv
      481 cwstgrithi plyfvnaqfp rfspvlgraq eppaggggsv hevplftets ptsapwdplp
      541 glpsaqphsp hshl
//
LOCUS       NP_001424830             922 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001424830 XP_038934795
VERSION     NP_001424830.1
DBSOURCE    REFSEQ: accession NM_001437901.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934795.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ230825.1, SRR26643295.29795.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..922
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=100195
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          618..>913
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..922
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437901.1:512..3280"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlafse
      541 yqiqqmtanf vdqfgfndee fadqddnina pfdriaeinf nieadedsps aalfeaccsd
      601 riqpfdddee diwedeetrc tarvmararf gaphtsenys kkavghggqg rktgsptarn
      661 vpglatpssp tqkegprses dsagttwtav fdepvnplsa asgaardvgs sawaagpsva
      721 eekgwakftd fqpfccsetg prcsspvdmd hsnaeggqsp gpekafgpts pcawnvcvtr
      781 kaplvasdss ssggsdsedd ekaagaveal caghtgkasp pprtaeaaag raecpdstvl
      841 apacpapsev tispavatia pskagsptat ivvsssvata vppgpimavt ttapaivatl
      901 gtmtkdrktd alpdgaalng pv
//
LOCUS       NP_001028874             328 aa            linear   ROD 11-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF126 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001028874
VERSION     NP_001028874.1
DBSOURCE    REFSEQ: accession NM_001033702.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Huang,C.Y., Lee,F.L., Peng,S.F., Lin,K.H., Chen,R.J., Ho,T.J.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     HSF1 phosphorylation by ERK/GSK3 suppresses RNF126 to sustain
            IGF-IIR expression for hypertension-induced cardiomyocyte
            hypertrophy
  JOURNAL   J Cell Physiol 233 (2), 979-989 (2018)
   PUBMED   28383811
  REMARK    GeneRIF: Angiotensin II activates ERK/GSK3 to phosphorylate HSF1,
            resulting in RNF126 degradation, which stabilizes IGF-IIR protein
            expression and eventually results in cardiac hypertrophy.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Rodrigo-Brenni,M.C., Gutierrez,E. and Hegde,R.S.
  TITLE     Cytosolic quality control of mislocalized proteins requires RNF126
            recruitment to Bag6
  JOURNAL   Mol Cell 55 (2), 227-237 (2014)
   PUBMED   24981174
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Smith,C.J. and McGlade,C.J.
  TITLE     The ubiquitin ligase RNF126 regulates the retrograde sorting of the
            cation-independent mannose 6-phosphate receptor
  JOURNAL   Exp Cell Res 320 (2), 219-232 (2014)
   PUBMED   24275455
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Smith,C.J., Berry,D.M. and McGlade,C.J.
  TITLE     The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal
            sorting of the epidermal growth factor receptor
  JOURNAL   J Cell Sci 126 (Pt 6), 1366-1380 (2013)
   PUBMED   23418353
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Delker,R.K., Zhou,Y., Strikoudis,A., Stebbins,C.E. and
            Papavasiliou,F.N.
  TITLE     Solubility-based genetic screen identifies RING finger protein 126
            as an E3 ligase for activation-induced cytidine deaminase
  JOURNAL   Proc Natl Acad Sci U S A 110 (3), 1029-1034 (2013)
   PUBMED   23277564
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Zhi,X., Zhao,D., Wang,Z., Zhou,Z., Wang,C., Chen,W., Liu,R. and
            Chen,C.
  TITLE     E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by
            targeting the tumor suppressor p21 for ubiquitin-mediated
            degradation
  JOURNAL   Cancer Res 73 (1), 385-394 (2013)
   PUBMED   23026136
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099810.1, SRR26643299.29881.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..328
                     /product="E3 ubiquitin-protein ligase RNF126 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF126"
                     /calculated_mol_wt=35644
     Region          10..40
                     /region_name="zinc_ribbon_9"
                     /note="zinc-ribbon; pfam14369"
                     /db_xref="CDD:433910"
     Region          245..288
                     /region_name="RING-H2_RNF126"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 126 (RNF126) and similar proteins; cd16801"
                     /db_xref="CDD:438453"
     CDS             1..328
                     /gene="Rnf126"
                     /coded_by="NM_001033702.2:61..1047"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314613"
                     /db_xref="RGD:1306011"
ORIGIN      
        1 maeaspqpgr yfchccsvei vprlpdyicp rcesgfieel peetrnteng sapstaptdq
       61 nrqpfevrqg pwaqarppvl qnvdqhlftl pqgysqfafg ifddsfeipa fppgaqaddg
      121 rdpesrrere hqsrhrygar qprarltarr atgrhegvpt legiiqqlvn giispaavps
      181 lglgpwgvlh snpmdyawga ngldaiitql lnqfentgpp padkekiqal ptvpvteehv
      241 gsglecpvck edyalgervr qlpcnhlfhd scivpwleqh dscpvcrksl tgqntatnpp
      301 gltgvgfsss ssssssssps nenatsns
//
LOCUS       NP_001424877            2056 aa            linear   ROD 11-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424877 XP_063130098
VERSION     NP_001424877.1
DBSOURCE    REFSEQ: accession NM_001437948.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2056)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2056)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2056)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2056)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2056)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063130098.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.41138.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2056
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2056
                     /product="dedicator of cytokinesis protein 9 isoform 6"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=234576
     Region          43..153
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          167..290
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          634..823
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1598..2012
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1702,1712,1714..1715,1717..1718,1721..1722,
                     1724..1725,1728..1729)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1736..1739,1741,1770..1771,1773..1776,1778..1779,
                     1798..1800,1817,1819,1848,1850,1857..1858,1864,1903..1904,
                     1907,1921,1923,1927,1930..1932,1935..1938,1940..1941,1944,
                     1972,1990..1991,1993..1994,1997)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1935..1940
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2056
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001437948.1:138..6308"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 mqadkyrtsg rndkkelvie splqykdaaq adseaensal akpkliepld yenvivqkkt
       61 qilndclrem llfpyddfqt ailrrqgryv rstvpanaee eaqslfvtec iktynsdwhl
      121 vtyhyedysg efrqlpnkva kldklpvhvy evdeeadkde daaslgsqkg gitkhgwlyk
      181 gnmnsaisvt mrsfkrrffh liqlgdgsyn lnfykdekis kepkgsifld scmgviqnnr
      241 vrrfafelkm qdkssyllaa dseaemeewv tvlnkilqln feaamqekrn gdpheddeqs
      301 klegsgsgld sylpelakst reaeiklkse srvklfyldp dtqkldfssa epevkpfeek
      361 fgkrilvkcn dlsfnlqccv aeneegpttn vepffvtlsl fdikynrkis adfhvdlnhf
      421 svrqmlapas pvlmnggqsp pafqdalqaa mqypkqgifs vtcphpdifl variekvlqg
      481 sithcaepym kssdsskvaq kvlknakqac qrlgqyrmpf awaartlfkd tsgnldknar
      541 fsaiyrqdsn klsnedmlkl ladfrkpekm aklpvilgnl ditidnvscd fpnylnssyi
      601 pmrqfetcsk spitfeveef vpcipkhtqp ytvysnhlyv ypkylrydsq ksfakarnia
      661 iciefkdsde edsqplkciy grpggpvftr salaavlhhq qspefydeik ielpaqlhek
      721 hhllftffhv scdnstkgst kkkdavetqv gfswlpllkd grvltneqhi pvsanlpsgy
      781 lgyqelsmgr hygpevkwve ggkpllkist hlvstvytqd qhlhnffqyc qktesgaqas
      841 gselvkylks lhameghvmi aflptilnql frvltratqe evavnvtrvi ihvvaqchee
      901 gleshlrsyv kfaykaepyi aseyktvhee ltksmttilk psadfltsnk llkyswfffd
      961 vliksmaqhl iennkvkllr nqrfpasyhh avetvvnmlm phitqkfrdn peasknanhs
     1021 lavfikrcft fmdrgfvfkq innyiscfap gdpktlfeyk feflrvvcnh ehyiplnlpm
     1081 pfgkgriqry qdlqldyslt defcrnhflv glllrevgta lqefrevrvi avsvlknlli
     1141 khsfddryts rshqariatl ylplfgllie nvqrinvrdv spfpvnpgsi skdealavpt
     1201 gnplmtpqkg ntldhslhkd llgaisgias pytastpnin svrnadsrgs listdsgnsl
     1261 pdrnpeksns ldkqqsgmlg nsvvrcdkld qseiksllmc flyvlksmsd dalftywnka
     1321 staelmdfft isevclhqfq ymgkryiasv rkissvlgis vdngyghsea dvahqsllea
     1381 niatevclta ldtlslftla fknqlladhg hnplmkkvfd vylcflqkhq semalknvft
     1441 alrsliykfp stfyegradm caslcyevlk ccnsklssir teasqllyfl mrnnfdytgk
     1501 ksfvrthlqv iisvsqliad vvgiggtrfq qslsiinnca nsdrlikhts fssdvkdltk
     1561 rirtvlmata qmkehendpe mlvdlqysla ksyastpelr ktwldsmari hvkngdlsea
     1621 amcyvhvtal vaeyltrkgm frqgctafrv itpnideeas mmedvgmqdv hfnedvlmel
     1681 leqcadglwk aeryeliadi ykliipiyek rrdferlahl ydtlhraysk vtevmhsgrr
     1741 llgtyfrvaf fgqgffeded gkeyiykepk ltplseisqr llklysdkfg senvkmiqds
     1801 gkvnpkdlds kfayiqvthv tpffdekelq erkteferch nirrfmfemp ftqtgkrqgg
     1861 veeqckrrti ltaihcfpyv kkripvmyqh htdlnpieva idemskkvae lrqlcssaev
     1921 dmiklqlklq gsvsvqvnag playarafld dtntkrypdn kvkllkevfr qfveacgqal
     1981 avnerliked qleyqeemka nyremakels dimreqicpl eektsvlpns lhifnaisgt
     2041 ptstvvqglt ssssvv
//
LOCUS       NP_001424884             594 aa            linear   ROD 11-APR-2025
DEFINITION  AT-rich interactive domain-containing protein 3A [Rattus
            norvegicus].
ACCESSION   NP_001424884 XP_006240964
VERSION     NP_001424884.1
DBSOURCE    REFSEQ: accession NM_001437955.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Tidwell,J.A., Schmidt,C., Heaton,P., Wilson,V. and Tucker,P.W.
  TITLE     Characterization of a new ARID family transcription factor
            (Brightlike/ARID3C) that co-activates Bright/ARID3A-mediated
            immunoglobulin gene transcription
  JOURNAL   Mol Immunol 49 (1-2), 260-272 (2011)
   PUBMED   21955986
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Nixon,J.C., Rajaiya,J. and Webb,C.F.
  TITLE     Mutations in the DNA-binding domain of the transcription factor
            Bright act as dominant negative proteins and interfere with
            immunoglobulin transactivation
  JOURNAL   J Biol Chem 279 (50), 52465-52472 (2004)
   PUBMED   15456761
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240964.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2414196.1,
                                           SRR26643293.38640.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..594
                     /product="AT-rich interactive domain-containing protein
                     3A"
                     /note="dead ringer homolog 1; AT rich interactive domain
                     3A (Bright like)"
                     /calculated_mol_wt=63464
     Region          217..349
                     /region_name="ARID_ARID3A"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 3A (ARID3A) and
                     similar proteins; cd16878"
                     /db_xref="CDD:350642"
     Site            order(259..265,290,292..293,296,304..307,309..311,313,
                     343..344)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350642"
     CDS             1..594
                     /gene="Arid3a"
                     /coded_by="NM_001437955.1:408..2192"
                     /db_xref="GeneID:314616"
                     /db_xref="RGD:1305299"
ORIGIN      
        1 mklqavmetl iqrqqrarqe learqpplpp ppepagvqar ttmtdedrep enarmhrtqm
       61 aalaamraaa aglrhpsspg gsededtaqg gtlsspalhg sgqegpghte gdghlmdmgs
      121 dddtkpkwee qeleelgeee eeededdfee eeedeeeegl glpesaslgs aglftrkapp
      181 tqtfrgdggp rmlsgperlg pgpahpshva sqmpppdhgd wtfeeqfkql yeldadpkrk
      241 eflddlfsfm qkrgtpvnri pimakqvldl fmlyvlvtek gglvevinkk lwreitkgln
      301 lptsitsaaf tlrtqymkyl ypyecerrgl sspnelqaai dsnrregrrq sfggslfays
      361 psgahsmlss pklpvtslgl aastngssit ptpkikkeed saipitvpgr lpvslaghpv
      421 vaaqaaavqa aaaqaavaaq aaaleqlrek lesteppekk malvadeqqr lmqravqqsf
      481 lamtaqlpmn irinsqases rqdpavnlts angsnsisms vemngivytg vlfaqppppt
      541 pppasskggv ssigtnntmg nrtgasgsag ssgqvglagv saptmsstsn nslp
//
LOCUS       NP_001424861             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424861 XP_038934872
VERSION     NP_001424861.1
DBSOURCE    REFSEQ: accession NM_001437932.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934872.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.43640.1,
                                           SRR26360181.1424345.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437932.1:400..975"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424865             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424865 XP_006242455
VERSION     NP_001424865.1
DBSOURCE    REFSEQ: accession NM_001437936.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006242455.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.969573.1,
                                           SRR26360176.1738214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840106, SAMN12840108
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437936.1:95..670"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424829             949 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001424829 XP_038934788
VERSION     NP_001424829.1
DBSOURCE    REFSEQ: accession NM_001437900.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934788.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.41662.1,
                                           SRR26643296.20655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..949
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=103214
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          645..>940
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..949
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437900.1:616..3465"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlvsth
      541 hlhssseded iegtfpnels lqqafseyqi qqmtanfvdq fgfndeefad qddninapfd
      601 riaeinfnie adedspsaal feaccsdriq pfdddeediw edeetrctar vmararfgap
      661 htsenyskka vghggqgrkt gsptarnvpg latpssptqk egprsesdsa gttwtavfde
      721 pvnplsaasg aardvgssaw aagpsvaeek gwakftdfqp fccsetgprc sspvdmdhsn
      781 aeggqspgpe kafgptspca wnvcvtrkap lvasdssssg gsdseddeka agavealcag
      841 htgkaspppr taeaaagrae cpdstvlapa cpapsevtis pavatiapsk agsptativv
      901 sssvatavpp gpimavttta paivatlgtm tkdrktdalp dgaalngpv
//
LOCUS       NP_001424834             520 aa            linear   ROD 11-APR-2025
DEFINITION  amphoterin-induced protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001424834 XP_063119440
VERSION     NP_001424834.1
DBSOURCE    REFSEQ: accession NM_001437905.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Li,Z., Khan,M.M., Kuja-Panula,J., Wang,H., Chen,Y., Guo,D.,
            Chen,Z.J., Lahesmaa,R., Rauvala,H. and Tian,L.
  TITLE     AMIGO2 modulates T cell functions and its deficiency in mice
            ameliorates experimental autoimmune encephalomyelitis
  JOURNAL   Brain Behav Immun 62, 110-123 (2017)
   PUBMED   28119027
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Kanda,Y., Osaki,M., Onuma,K., Sonoda,A., Kobayashi,M., Hamada,J.,
            Nicolson,G.L., Ochiya,T. and Okada,F.
  TITLE     Amigo2-upregulation in Tumour Cells Facilitates Their Attachment to
            Liver Endothelial Cells Resulting in Liver Metastases
  JOURNAL   Sci Rep 7, 43567 (2017)
   PUBMED   28272394
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Park,H., Lee,S., Shrestha,P., Kim,J., Park,J.A., Ko,Y., Ban,Y.H.,
            Park,D.Y., Ha,S.J., Koh,G.Y., Hong,V.S., Mochizuki,N., Kim,Y.M.,
            Lee,W. and Kwon,Y.G.
  TITLE     AMIGO2, a novel membrane anchor of PDK1, controls cell survival and
            angiogenesis via Akt activation
  JOURNAL   J Cell Biol 211 (3), 619-637 (2015)
   PUBMED   26553931
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Rabenau,K.E., O'Toole,J.M., Bassi,R., Kotanides,H., Witte,L.,
            Ludwig,D.L. and Pereira,D.S.
  TITLE     DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
            expressed in human gastric adenocarcinoma: effects on ploidy,
            chromosomal stability, cell adhesion/migration and tumorigenicity
  JOURNAL   Oncogene 23 (29), 5056-5067 (2004)
   PUBMED   15107827
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Ono,T., Sekino-Suzuki,N., Kikkawa,Y., Yonekawa,H. and Kawashima,S.
  TITLE     Alivin 1, a novel neuronal activity-dependent gene, inhibits
            apoptosis and promotes survival of cerebellar granule neurons
  JOURNAL   J Neurosci 23 (13), 5887-5896 (2003)
   PUBMED   12843293
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119440.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.32160.1,
                                           SRR26643295.29979.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..520
                     /product="amphoterin-induced protein 2 precursor"
                     /note="amphoterin-induced protein 2; alivin 1; AMIGO-2;
                     amphoterin induced gene 2; transmembrane protein AMIGO2;
                     transmembrane protein AMIGO2-like"
                     /calculated_mol_wt=53754
     sig_peptide     1..37
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=4024
     mat_peptide     38..520
                     /product="Amphoterin-induced protein 2.
                     /evidence=ECO:0000255. /id=PRO_0000014512"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=53754
     Region          50..71
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          68..89
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          <69..>229
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          72..94
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          93..114
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          96..117
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          117..138
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          118..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          141..162
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          142..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          165..186
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          166..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          192..213
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          219..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          297..367
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          305..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          319..323
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..341
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          359..364
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          437..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          498..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     CDS             1..520
                     /gene="Amigo2"
                     /gene_synonym="Ali1"
                     /coded_by="NM_001437905.1:370..1932"
                     /db_xref="GeneID:300186"
                     /db_xref="RGD:727911"
ORIGIN      
        1 mslrfhtlpt lpravkpgcr ellcllviav mvspsssglc ptacicatdi vsctnknlsk
       61 vpgnlfrlik rldlsynrig lldadwipvs fvklstlivr hnnitsistg sfsttpnlkc
      121 ldlssnrlks vksamfqelk vlevlllynn hisyldpaaf gglshlqkly lsgnfltkfp
      181 mdlyvgrfkl adltfldvsy nqiasipmhh inlvpgkqlr giflhgnpfv cdcslysllt
      241 fwyrrhfnsv tdfkhdytcr lwldsrhshq llllqdsfln cshsvingsf halgfiheaq
      301 vgeraivhcd gktgngntdf iwvgpdnrll epdkdtgnfr vfyngslvie npgfedagvy
      361 sciamnrqrl lnetvdimin vsnftinrsh haheafntaf ttlaacvvsi vlvllylylt
      421 pcpckcrdkr qknalnqsna hssilspgpt rdasaedrka gkrvvflepl kdpavgqngk
      481 vklvpsetvi aegilkssra ksdsdsvnsv fsdtpfvast
//
LOCUS       NP_001101536             594 aa            linear   ROD 11-APR-2025
DEFINITION  AT-rich interactive domain-containing protein 3A [Rattus
            norvegicus].
ACCESSION   NP_001101536 XP_001076973 XP_234884
VERSION     NP_001101536.2
DBSOURCE    REFSEQ: accession NM_001108066.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Tidwell,J.A., Schmidt,C., Heaton,P., Wilson,V. and Tucker,P.W.
  TITLE     Characterization of a new ARID family transcription factor
            (Brightlike/ARID3C) that co-activates Bright/ARID3A-mediated
            immunoglobulin gene transcription
  JOURNAL   Mol Immunol 49 (1-2), 260-272 (2011)
   PUBMED   21955986
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Nixon,J.C., Rajaiya,J. and Webb,C.F.
  TITLE     Mutations in the DNA-binding domain of the transcription factor
            Bright act as dominant negative proteins and interfere with
            immunoglobulin transactivation
  JOURNAL   J Biol Chem 279 (50), 52465-52472 (2004)
   PUBMED   15456761
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Mar 6, 2009 this sequence version replaced NP_001101536.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168846.1, SRR26360181.2561555.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..594
                     /product="AT-rich interactive domain-containing protein
                     3A"
                     /note="dead ringer homolog 1; AT rich interactive domain
                     3A (Bright like)"
                     /calculated_mol_wt=63464
     Region          217..349
                     /region_name="ARID_ARID3A"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 3A (ARID3A) and
                     similar proteins; cd16878"
                     /db_xref="CDD:350642"
     Site            order(259..265,290,292..293,296,304..307,309..311,313,
                     343..344)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350642"
     CDS             1..594
                     /gene="Arid3a"
                     /coded_by="NM_001108066.3:390..2174"
                     /db_xref="GeneID:314616"
                     /db_xref="RGD:1305299"
ORIGIN      
        1 mklqavmetl iqrqqrarqe learqpplpp ppepagvqar ttmtdedrep enarmhrtqm
       61 aalaamraaa aglrhpsspg gsededtaqg gtlsspalhg sgqegpghte gdghlmdmgs
      121 dddtkpkwee qeleelgeee eeededdfee eeedeeeegl glpesaslgs aglftrkapp
      181 tqtfrgdggp rmlsgperlg pgpahpshva sqmpppdhgd wtfeeqfkql yeldadpkrk
      241 eflddlfsfm qkrgtpvnri pimakqvldl fmlyvlvtek gglvevinkk lwreitkgln
      301 lptsitsaaf tlrtqymkyl ypyecerrgl sspnelqaai dsnrregrrq sfggslfays
      361 psgahsmlss pklpvtslgl aastngssit ptpkikkeed saipitvpgr lpvslaghpv
      421 vaaqaaavqa aaaqaavaaq aaaleqlrek lesteppekk malvadeqqr lmqravqqsf
      481 lamtaqlpmn irinsqases rqdpavnlts angsnsisms vemngivytg vlfaqppppt
      541 pppasskggv ssigtnntmg nrtgasgsag ssgqvglagv saptmsstsn nslp
//
LOCUS       NP_001424838            1099 aa            linear   ROD 11-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424838 XP_063138212
VERSION     NP_001424838.1
DBSOURCE    REFSEQ: accession NM_001437909.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1099)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1099)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1099)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1099)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063138212.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.9537.1,
                                           SRR26643295.9793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1099
                     /product="ubiquitin-associated protein 2-like isoform 3"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=115674
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          527..554
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1099
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001437909.1:124..3423"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgrec mhgalskpav vrgqengldg tksggpsgrg
      181 tdrgrrgrgr grgssgrrgg rfsaqgmgtf npadyaepan tddnygsssg ntwnntghfe
      241 pddgtrldfi gvegsnyprk fetapgawrt ateewgtedw nedlsetkif tasnvssvpl
      301 paenvtitag qridlavllg ktpssmends snldpsqaps laqplvfsns kqnaisqpas
      361 gntfshhsmv smlgkgfgdv geakggsttg sqfleqfkta qalaqlaaqh sqsgstttss
      421 wdmgsttqsp slvqydlksa ndstvhspft krqaftpsst mmevflqekp pavatstaap
      481 pppssplpsk stsapqmspg ssdnqssspq paqqklkqqk kktsltskip alavempgsa
      541 disglnlqfg alqfgsepvl sdyestptts asssqapssl ytstasesss tvssnqsqes
      601 gyqsgpiqst tytsqnnaqg plyeqrstqt rrypssisss pqkdltqakn gfssvqatql
      661 qttqsvegat gsavksesps tssipslnet vpaaslltta sqhssslsgl shseeipntt
      721 ttqhssalst qqntlsssts sgrtststll htsveseanl hsssstfstt sstvsapppv
      781 vsvssslnsg sslglslgsn stvtastrss vattsgkapp nlppgvppll pnpyimapgl
      841 lhayppqvyg yddlqmlqtr fpldyysipf ptpttpltgr dgslasnpys gdltkfgrgd
      901 asspapattl aqpqqnqtqt hhttqqtfln palppgysyt slpyytgvpg lpstfqygpa
      961 vfpvaptssk qhgvnvsvna satpfqqpsg ygshgyntgv svtssntgvp disgsvyskt
     1021 qqsfekqgfh sgtpaasfnl psalgsggpi npataaaypp apfmhiltph qqphsqilhh
     1081 hlqqdgqdil tlvddqlge
//
LOCUS       NP_001424873            2083 aa            linear   ROD 11-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424873 XP_063130094
VERSION     NP_001424873.1
DBSOURCE    REFSEQ: accession NM_001437944.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2083)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2083)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2083)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2083)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2083)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063130094.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.37513.1,
                                           SRR26643296.34889.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2083
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2083
                     /product="dedicator of cytokinesis protein 9 isoform 2"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=237659
     Region          43..153
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          167..290
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          634..823
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1599..2039
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1729,1739,1741..1742,1744..1745,1748..1749,
                     1751..1752,1755..1756)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1763..1766,1768,1797..1798,1800..1803,1805..1806,
                     1825..1827,1844,1846,1875,1877,1884..1885,1891,1930..1931,
                     1934,1948,1950,1954,1957..1959,1962..1965,1967..1968,1971,
                     1999,2017..2018,2020..2021,2024)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1962..1967
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2083
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001437944.1:138..6389"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 mqadkyrtsg rndkkelvie splqykdaaq adseaensal akpkliepld yenvivqkkt
       61 qilndclrem llfpyddfqt ailrrqgryv rstvpanaee eaqslfvtec iktynsdwhl
      121 vtyhyedysg efrqlpnkva kldklpvhvy evdeeadkde daaslgsqkg gitkhgwlyk
      181 gnmnsaisvt mrsfkrrffh liqlgdgsyn lnfykdekis kepkgsifld scmgviqnnr
      241 vrrfafelkm qdkssyllaa dseaemeewv tvlnkilqln feaamqekrn gdpheddeqs
      301 klegsgsgld sylpelakst reaeiklkse srvklfyldp dtqkldfssa epevkpfeek
      361 fgkrilvkcn dlsfnlqccv aeneegpttn vepffvtlsl fdikynrkis adfhvdlnhf
      421 svrqmlapas pvlmnggqsp pafqdalqaa mqypkqgifs vtcphpdifl variekvlqg
      481 sithcaepym kssdsskvaq kvlknakqac qrlgqyrmpf awaartlfkd tsgnldknar
      541 fsaiyrqdsn klsnedmlkl ladfrkpekm aklpvilgnl ditidnvscd fpnylnssyi
      601 pmrqfetcsk spitfeveef vpcipkhtqp ytvysnhlyv ypkylrydsq ksfakarnia
      661 iciefkdsde edsqplkciy grpggpvftr salaavlhhq qspefydeik ielpaqlhek
      721 hhllftffhv scdnstkgst kkkdavetqv gfswlpllkd grvltneqhi pvsanlpsgy
      781 lgyqelsmgr hygpevkwve ggkpllkist hlvstvytqd qhlhnffqyc qktesgaqas
      841 gselvkylks lhameghvmi aflptilnql frvltratqe evavnvtrvi ihvvaqchee
      901 gleshlrsyv kfaykaepyi aseyktvhee ltksmttilk psadfltsnk llkyswfffd
      961 vliksmaqhl iennkvkllr nqrfpasyhh avetvvnmlm phitqkfrdn peasknanhs
     1021 lavfikrcft fmdrgfvfkq innyiscfap gdpktlfeyk feflrvvcnh ehyiplnlpm
     1081 pfgkgriqry qdlqldyslt defcrnhflv glllrevgta lqefrevrvi avsvlknlli
     1141 khsfddryts rshqariatl ylplfgllie nvqrinvrdv spfpvnpgsi skdealavpt
     1201 gnplmtpqkg ntldhslhkd llgaisgias pytastpnin svrnadsrgs listdsgnsl
     1261 pdrnpeksns ldkqqqsgml gnsvvrcdkl dqseiksllm cflyvlksms ddalftywnk
     1321 astaelmdff tisevclhqf qymgkryias vrkissvlgi svdngyghse advahqslle
     1381 aniatevclt aldtlslftl afknqlladh ghnplmkkvf dvylcflqkh qsemalknvf
     1441 talrsliykf pstfyegrad mcaslcyevl kccnsklssi rteasqllyf lmrnnfdytg
     1501 kksfvrthlq viisvsqlia dvvgiggtrf qqslsiinnc ansdrlikht sfssdvkdlt
     1561 krirtvlmat aqmkehendp emlvdlqysl aksyastpel rktwldsmar ihvkngdlse
     1621 aamcyvhvta lvaeyltrke adlalqrepp vfpyshtscq rksrggmfrq gctafrvitp
     1681 nideeasmme dvgmqdvhfn edvlmelleq cadglwkaer yeliadiykl iipiyekrrd
     1741 ferlahlydt lhrayskvte vmhsgrrllg tyfrvaffgq gffededgke yiykepkltp
     1801 lseisqrllk lysdkfgsen vkmiqdsgkv npkdldskfa yiqvthvtpf fdekelqerk
     1861 teferchnir rfmfempftq tgkrqggvee qckrrtilta ihcfpyvkkr ipvmyqhhtd
     1921 lnpievaide mskkvaelrq lcssaevdmi klqlklqgsv svqvnagpla yaraflddtn
     1981 tkrypdnkvk llkevfrqfv eacgqalavn erlikedqle yqeemkanyr emakelsdim
     2041 reqicpleek tsvlpnslhi fnaisgtpts tvvqgltsss svv
//
LOCUS       NP_001424908             460 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424908 XP_038935095
VERSION     NP_001424908.1
DBSOURCE    REFSEQ: accession NM_001437979.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038935095.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1380905.1,
                                           SRR26360181.2625084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..460
                     /product="gasdermin D like 1 isoform 2"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=50819
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..>380
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..460
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437979.1:225..1607"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelaqel cksicdmltr vlllyggkvr pqgevalqgn tgqavlpcvs
      421 cigllrsich mtkqnkllrf qpivpmtiqc qsmgssqlnk
//
LOCUS       NP_001424839            1092 aa            linear   ROD 11-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424839 XP_063138218
VERSION     NP_001424839.1
DBSOURCE    REFSEQ: accession NM_001437910.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1092)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1092)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1092)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1092)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1092)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1092)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1092)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063138218.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.6740.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1092
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1092
                     /product="ubiquitin-associated protein 2-like isoform 4"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=115034
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          521..548
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1092
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001437910.1:59..3337"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgref rgqengldgt ksggpsgrgt drgrrgrgrg
      181 rgssgrrggr fsaqgmgtfn padyaepant ddnygsssgn twnntghfep ddgtrldfig
      241 vegsnyprkf etapgmihpg awrtateewg tedwnedlse tkiftasnvs svplpaenvt
      301 itagqridla vllgktpssm endssnldps qapslaqplv fsnskqnais qpasgntfsh
      361 hsmvsmlgkg fgdvgeakgg sttgsqfleq fktaqalaql aaqhsqsgst ttsswdmgst
      421 tqspslvqyd lksandstvh spftkrqaft psstmmevfl qekppavats taappppssp
      481 lpskstsapq mspgssdnqs sspqpaqqkl kqqkkktslt skipalavem pgsadisgln
      541 lqfgalqfgs epvlsdyest pttsasssqa psslytstas essstvssnq sqesgyqsgp
      601 iqsttytsqn naqgplyeqr stqtrrypss issspqkdlt qakngfssvq atqlqttqsv
      661 egatgsavks espstssips lnetvpaasl lttasqhsss lsglshseei pnttttqhss
      721 alstqqntls sstssgrtst stllhtsves eanlhsssst fsttsstvsa pppvvsvsss
      781 lnsgsslgls lgsnstvtas trssvattsg kappnlppgv ppllpnpyim apgllhaypp
      841 qvygyddlqm lqtrfpldyy sipfptpttp ltgrdgslas npysgdltkf grgdasspap
      901 attlaqpqqn qtqthhttqq tflnpalppg ysytslpyyt gvpglpstfq ygpavfpvap
      961 tsskqhgvnv svnasatpfq qpsgygshgy ntgvsvtssn tgvpdisgsv ysktqsfekq
     1021 gfhsgtpaas fnlpsalgsg gpinpataaa yppapfmhil tphqqphsqi lhhhlqqdgq
     1081 diltlvddql ge
//
LOCUS       NP_001424827             922 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001424827 XP_063119407
VERSION     NP_001424827.1
DBSOURCE    REFSEQ: accession NM_001437898.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119407.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.26751.1,
                                           SRR26643295.29802.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..922
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=100195
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          618..>913
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..922
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437898.1:744..3512"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlafse
      541 yqiqqmtanf vdqfgfndee fadqddnina pfdriaeinf nieadedsps aalfeaccsd
      601 riqpfdddee diwedeetrc tarvmararf gaphtsenys kkavghggqg rktgsptarn
      661 vpglatpssp tqkegprses dsagttwtav fdepvnplsa asgaardvgs sawaagpsva
      721 eekgwakftd fqpfccsetg prcsspvdmd hsnaeggqsp gpekafgpts pcawnvcvtr
      781 kaplvasdss ssggsdsedd ekaagaveal caghtgkasp pprtaeaaag raecpdstvl
      841 apacpapsev tispavatia pskagsptat ivvsssvata vppgpimavt ttapaivatl
      901 gtmtkdrktd alpdgaalng pv
//
LOCUS       NP_001424905             472 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424905 XP_063119588
VERSION     NP_001424905.1
DBSOURCE    REFSEQ: accession NM_001437976.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119588.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.41286.1,
                                           SRR26360181.2388047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..472
                     /product="gasdermin D like 1 isoform 1"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=51874
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..428
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..472
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437976.1:225..1643"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelvasi lehncnqtee ttsplptgvl calksedevl ilnlvqgcgl
      421 eleksgcqlp wdptvvpqls alyacltglq lltdpspgls rtvpeeetli cp
//
LOCUS       NP_001424907             460 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424907 XP_006241704
VERSION     NP_001424907.1
DBSOURCE    REFSEQ: accession NM_001437978.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006241704.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.127880.1,
                                           SRR26643293.41292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..460
                     /product="gasdermin D like 1 isoform 2"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=50819
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..>380
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..460
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437978.1:299..1681"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelaqel cksicdmltr vlllyggkvr pqgevalqgn tgqavlpcvs
      421 cigllrsich mtkqnkllrf qpivpmtiqc qsmgssqlnk
//
LOCUS       NP_001424898             548 aa            linear   ROD 11-APR-2025
DEFINITION  protein LYRIC isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424898 XP_006241586
VERSION     NP_001424898.1
DBSOURCE    REFSEQ: accession NM_001437969.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Xiang,Y., Duan,Y., Peng,Z., Huang,H., Ding,W., Chen,E., Liu,Z.,
            Dou,C., Li,J., Ou,J., Wan,Q., Yang,B. and He,Z.
  TITLE     Microparticles from Hyperphosphatemia-Stimulated Endothelial Cells
            Promote Vascular Calcification Through Astrocyte-Elevated Gene-1
  JOURNAL   Calcif Tissue Int 111 (1), 73-86 (2022)
   PUBMED   35195734
  REMARK    GeneRIF: Microparticles from Hyperphosphatemia-Stimulated
            Endothelial Cells Promote Vascular Calcification Through
            Astrocyte-Elevated Gene-1.
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Wang,Y., Zhang,W., Zhu,X., Wang,Y., Mao,X., Xu,X. and Wang,Y.
  TITLE     Upregulation of AEG-1 Involves in Schwann Cell Proliferation and
            Migration After Sciatic Nerve Crush
  JOURNAL   J Mol Neurosci 60 (2), 248-257 (2016)
   PUBMED   27351433
  REMARK    GeneRIF: AEG-1 was expressed mainly in Schwann cells of the distal
            sciatic nerve segment from injury.  Interference of AEG-1 inhibited
            both proliferation and migration of Schwann cells.
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Watanabe,A., Tatematsu,M., Saeki,K., Shibata,S., Shime,H.,
            Yoshimura,A., Obuse,C., Seya,T. and Matsumoto,M.
  TITLE     Raftlin is involved in the nucleocapture complex to induce
            poly(I:C)-mediated TLR3 activation
  JOURNAL   J Biol Chem 286 (12), 10702-10711 (2011)
   PUBMED   21266579
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Emdad,L., Sarkar,D., Su,Z.Z., Randolph,A., Boukerche,H., Valerie,K.
            and Fisher,P.B.
  TITLE     Activation of the nuclear factor kappaB pathway by astrocyte
            elevated gene-1: implications for tumor progression and metastasis
  JOURNAL   Cancer Res 66 (3), 1509-1516 (2006)
   PUBMED   16452207
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Kang,D.C., Su,Z.Z., Sarkar,D., Emdad,L., Volsky,D.J. and
            Fisher,P.B.
  TITLE     Cloning and characterization of HIV-1-inducible astrocyte elevated
            gene-1, AEG-1
  JOURNAL   Gene 353 (1), 8-15 (2005)
   PUBMED   15927426
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Britt,D.E., Yang,D.F., Yang,D.Q., Flanagan,D., Callanan,H.,
            Lim,Y.P., Lin,S.H. and Hixson,D.C.
  TITLE     Identification of a novel protein, LYRIC, localized to tight
            junctions of polarized epithelial cells
  JOURNAL   Exp Cell Res 300 (1), 134-148 (2004)
   PUBMED   15383321
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Sutherland,H.G., Lam,Y.W., Briers,S., Lamond,A.I. and Bickmore,W.A.
  TITLE     3D3/lyric: a novel transmembrane protein of the endoplasmic
            reticulum and nuclear envelope, which is also present in the
            nucleolus
  JOURNAL   Exp Cell Res 294 (1), 94-105 (2004)
   PUBMED   14980505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006241586.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.725942.1,
                                           SRR26360186.2502169.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..548
                     /product="protein LYRIC isoform 3"
                     /note="protein LYRIC; lysine-rich CEACAM1 co-isolated
                     protein; metastasis adhesion protein"
                     /calculated_mol_wt=60205
     Region          6..389
                     /region_name="LYRIC"
                     /note="Lysine-rich CEACAM1 co-isolated protein family;
                     pfam15686"
                     /db_xref="CDD:434858"
     CDS             1..548
                     /gene="Mtdh"
                     /gene_synonym="Lyric"
                     /coded_by="NM_001437969.1:320..1966"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:170910"
                     /db_xref="RGD:620992"
ORIGIN      
        1 maarswqdel aqqaeegsar lrellsvglg flrtelgldl glepkrypsw vilvgtgalg
       61 llllfllgyg waaacagark krrspprkre evtpptpape dpaqlknlrs eeqkkknrkk
      121 lpekpkpngr tveipedevv rtprsitakq ppetdkknek skknkkksks dakavqnssr
      181 hdgkevdega wetkishrek rqqrkrdkvl tdsgsldsti pgientitvt teqlttasfp
      241 vgskknkgds hlnvqvsnfk sgkgdstlqv ssglnenitv ngggwseksv klssqlsage
      301 ekwnsvppas agkrkteqsa wtqdpgdtna ngkdwgrnws drsifsgidg lssadpssdw
      361 napaeewgnw vdedrasllk sqepisndqk dsdddkekge galptgkskk kkkkkkkqge
      421 dnsitqdted lekdtreelp vntskarpkq ekacslktms tsdpvevlik nsqpiktlpp
      481 aisaepsvtl skgdsdksss qvppmlqdtd kpksnakqns vppsqtkset nwespkqikk
      541 kkkarret
//
LOCUS       NP_001424874            2082 aa            linear   ROD 11-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424874 XP_063130095
VERSION     NP_001424874.1
DBSOURCE    REFSEQ: accession NM_001437945.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2082)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2082)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2082)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2082)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2082)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063130095.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.37511.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2082
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2082
                     /product="dedicator of cytokinesis protein 9 isoform 3"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=237531
     Region          43..153
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          167..290
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          634..823
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1598..2038
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1728,1738,1740..1741,1743..1744,1747..1748,
                     1750..1751,1754..1755)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1762..1765,1767,1796..1797,1799..1802,1804..1805,
                     1824..1826,1843,1845,1874,1876,1883..1884,1890,1929..1930,
                     1933,1947,1949,1953,1956..1958,1961..1964,1966..1967,1970,
                     1998,2016..2017,2019..2020,2023)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1961..1966
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2082
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001437945.1:138..6386"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 mqadkyrtsg rndkkelvie splqykdaaq adseaensal akpkliepld yenvivqkkt
       61 qilndclrem llfpyddfqt ailrrqgryv rstvpanaee eaqslfvtec iktynsdwhl
      121 vtyhyedysg efrqlpnkva kldklpvhvy evdeeadkde daaslgsqkg gitkhgwlyk
      181 gnmnsaisvt mrsfkrrffh liqlgdgsyn lnfykdekis kepkgsifld scmgviqnnr
      241 vrrfafelkm qdkssyllaa dseaemeewv tvlnkilqln feaamqekrn gdpheddeqs
      301 klegsgsgld sylpelakst reaeiklkse srvklfyldp dtqkldfssa epevkpfeek
      361 fgkrilvkcn dlsfnlqccv aeneegpttn vepffvtlsl fdikynrkis adfhvdlnhf
      421 svrqmlapas pvlmnggqsp pafqdalqaa mqypkqgifs vtcphpdifl variekvlqg
      481 sithcaepym kssdsskvaq kvlknakqac qrlgqyrmpf awaartlfkd tsgnldknar
      541 fsaiyrqdsn klsnedmlkl ladfrkpekm aklpvilgnl ditidnvscd fpnylnssyi
      601 pmrqfetcsk spitfeveef vpcipkhtqp ytvysnhlyv ypkylrydsq ksfakarnia
      661 iciefkdsde edsqplkciy grpggpvftr salaavlhhq qspefydeik ielpaqlhek
      721 hhllftffhv scdnstkgst kkkdavetqv gfswlpllkd grvltneqhi pvsanlpsgy
      781 lgyqelsmgr hygpevkwve ggkpllkist hlvstvytqd qhlhnffqyc qktesgaqas
      841 gselvkylks lhameghvmi aflptilnql frvltratqe evavnvtrvi ihvvaqchee
      901 gleshlrsyv kfaykaepyi aseyktvhee ltksmttilk psadfltsnk llkyswfffd
      961 vliksmaqhl iennkvkllr nqrfpasyhh avetvvnmlm phitqkfrdn peasknanhs
     1021 lavfikrcft fmdrgfvfkq innyiscfap gdpktlfeyk feflrvvcnh ehyiplnlpm
     1081 pfgkgriqry qdlqldyslt defcrnhflv glllrevgta lqefrevrvi avsvlknlli
     1141 khsfddryts rshqariatl ylplfgllie nvqrinvrdv spfpvnpgsi skdealavpt
     1201 gnplmtpqkg ntldhslhkd llgaisgias pytastpnin svrnadsrgs listdsgnsl
     1261 pdrnpeksns ldkqqsgmlg nsvvrcdkld qseiksllmc flyvlksmsd dalftywnka
     1321 staelmdfft isevclhqfq ymgkryiasv rkissvlgis vdngyghsea dvahqsllea
     1381 niatevclta ldtlslftla fknqlladhg hnplmkkvfd vylcflqkhq semalknvft
     1441 alrsliykfp stfyegradm caslcyevlk ccnsklssir teasqllyfl mrnnfdytgk
     1501 ksfvrthlqv iisvsqliad vvgiggtrfq qslsiinnca nsdrlikhts fssdvkdltk
     1561 rirtvlmata qmkehendpe mlvdlqysla ksyastpelr ktwldsmari hvkngdlsea
     1621 amcyvhvtal vaeyltrkea dlalqreppv fpyshtscqr ksrggmfrqg ctafrvitpn
     1681 ideeasmmed vgmqdvhfne dvlmelleqc adglwkaery eliadiykli ipiyekrrdf
     1741 erlahlydtl hrayskvtev mhsgrrllgt yfrvaffgqg ffededgkey iykepkltpl
     1801 seisqrllkl ysdkfgsenv kmiqdsgkvn pkdldskfay iqvthvtpff dekelqerkt
     1861 eferchnirr fmfempftqt gkrqggveeq ckrrtiltai hcfpyvkkri pvmyqhhtdl
     1921 npievaidem skkvaelrql cssaevdmik lqlklqgsvs vqvnagplay araflddtnt
     1981 krypdnkvkl lkevfrqfve acgqalavne rlikedqley qeemkanyre makelsdimr
     2041 eqicpleekt svlpnslhif naisgtptst vvqgltssss vv
//
LOCUS       NP_001424837            1123 aa            linear   ROD 11-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424837 XP_063138200
VERSION     NP_001424837.1
DBSOURCE    REFSEQ: accession NM_001437908.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1123)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1123)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1123)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1123)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1123)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1123)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1123)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063138200.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.9802.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1123
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1123
                     /product="ubiquitin-associated protein 2-like isoform 2"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=118210
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          532..559
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1123
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001437908.1:59..3430"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgrec mhgalskpav vrgqengldg tksggpsgrg
      181 tdrgrrgrgr grgssgrrgg rfsaqgmgtf npadyaepan tddnygsssg ntwnntghfe
      241 pddgtrldfi gvegsnyprk fetapgmihp gawrtateew gtedwnedls etkiftasnv
      301 ssvplpaenv titagqridl avllgktpss mendssnldp sqapslaqpl vfsnskqnai
      361 sqpasgntfs hhsmvsmlgk gfgdvgeakg gsttgsqfle qfktaqalaq laaqhsqsgs
      421 tttsswdmgs ttqspslvqy dlksandstv hspftkrqaf tpsstmmevf lqekppavat
      481 staappppss plpskstsap qmspgssdnq ssspqpaqqk lkqqkkktsl tskipalave
      541 mpgsadisgl nlqfgalqfg sepvlsdyes tpttsasssq apsslytsta sessstvssn
      601 qsqesgyqsg piqsttytsq nnaqgplyeq rstqtrryps sissspqkdl tqakngfssv
      661 qatqlqttqs vegatgsavk sespstssip slnetvpaas llttasqhss slsglshsee
      721 ipnttttqhs salstqqntl ssstssgrts tstllhtsve seanlhssss tfsttsstvs
      781 apppvvsvss slnsgsslgl slgsnstvta strssvatts gkappnlppg vppllpnpyi
      841 mapgllhayp pqvygyddlq mlqtrfpldy ysipfptptt pltgrdgsla snpysgdltk
      901 fgrgdasspa pattlaqpqq nqtqthhttq qtflnpalpp gysytslpyy tgvpglpstf
      961 qygpavfpva ptsskqhgvn vsvnasatpf qqpsgygshg yntgvsvtss ntgvpdisgs
     1021 vysktqqsfe kqgfhsgtpa asfnlpsalg sggpinpata aayppapfmh iltphqqphs
     1081 qilhhhlqqd gqtgsgqrsq tssipqkpqt nksaynsysw gan
//
LOCUS       NP_783188                520 aa            linear   ROD 11-APR-2025
DEFINITION  chaperone Ric-8B isoform 1 [Rattus norvegicus].
ACCESSION   NP_783188
VERSION     NP_783188.1
DBSOURCE    REFSEQ: accession NM_175598.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Lopez-Benito,S., Lillo,C., Hernandez-Hernandez,A., Chao,M.V. and
            Arevalo,J.C.
  TITLE     ARMS/Kidins220 and synembryn-B levels regulate NGF-mediated
            secretion
  JOURNAL   J Cell Sci 129 (9), 1866-1877 (2016)
   PUBMED   26966186
  REMARK    GeneRIF: overexpression of ARMS blocked NGF-mediated secretion,
            without affecting basal secretion, a decrease in ARMS resulted in
            potentiation. Similar effects were observed with synembryn-B, a
            protein that interacts directly with ARMS. Downstream of ARMS and
            synembryn-B are Galphaq and Trio proteins, which modulate the
            activity of Rac1 in response to NGF
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Aguilar,R., Grandy,R., Meza,D., Sepulveda,H., Pihan,P., van
            Wijnen,A.J., Lian,J.B., Stein,G.S., Stein,J.L. and Montecino,M.
  TITLE     A functional N-terminal domain in C/EBPbeta-LAP* is required for
            interacting with SWI/SNF and to repress Ric-8B gene transcription
            in osteoblasts
  JOURNAL   J Cell Physiol 229 (10), 1521-1528 (2014)
   PUBMED   24585571
  REMARK    GeneRIF: Results indicate that a functional N-terminus in
            C/EBPbeta-LAP* is required for interacting with SWI/SNF and for
            Ric-8B gene repression in osteoblasts.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Chan,P., Gabay,M., Wright,F.A. and Tall,G.G.
  TITLE     Ric-8B is a GTP-dependent G protein alphas guanine nucleotide
            exchange factor
  JOURNAL   J Biol Chem 286 (22), 19932-19942 (2011)
   PUBMED   21467038
  REMARK    GeneRIF: Ric-8BFL-catalyzed nucleotide exchange probably proceeds
            in the forward direction to produce Galpha-GTP in cells.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Klattenhoff,C., Montecino,M., Soto,X., Guzman,L., Romo,X.,
            Garcia,M.A., Mellstrom,B., Naranjo,J.R., Hinrichs,M.V. and Olate,J.
  TITLE     Human brain synembryn interacts with Gsalpha and Gqalpha and is
            translocated to the plasma membrane in response to isoproterenol
            and carbachol
  JOURNAL   J Cell Physiol 195 (2), 151-157 (2003)
   PUBMED   12652642
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Tall,G.G., Krumins,A.M. and Gilman,A.G.
  TITLE     Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein
            guanine nucleotide exchange factor
  JOURNAL   J Biol Chem 278 (10), 8356-8362 (2003)
   PUBMED   12509430
  REMARK    GeneRIF: two mammalian homologs of the Caenorhabditis elegans
            protein Ric-8 were identified: Ric-8A (Ric-8/synembryn) and Ric-8B
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY177755.1, SRR26360172.698421.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..520
                     /product="chaperone Ric-8B isoform 1"
                     /note="synembryn-B; resistance to inhibitors of
                     cholinesterase 8 homolog B; resistance to inhibitors of
                     cholinesterase 8B; heterotrimeric G protein guanine
                     nucleotide exchange factor-like protein Ric-8B; chaperone
                     Ric-8B"
                     /calculated_mol_wt=58259
     Region          66..483
                     /region_name="Ric8"
                     /note="Guanine nucleotide exchange factor synembryn;
                     pfam10165"
                     /db_xref="CDD:462973"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG0.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG0.1)"
     CDS             1..520
                     /gene="Ric8b"
                     /coded_by="NM_175598.3:88..1650"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314681"
                     /db_xref="RGD:631419"
ORIGIN      
        1 mdeeralyiv rageagaier vlrdysdkhr atfkfesade dkrkklcegi fkvlvkgvpt
       61 tcqvpclevl rilsrdkkil apvtteenmq illrlaklhe sddslekvse fpviveslkc
      121 lcnivfnsqv aqqlslelnl aaklcnllrk ckdrkfindi kcfdlrllfv lsllhtdirs
      181 qlryelqglp lltqilesaf sikwtdeyes aidhsgppls pqetdcaiea lkalfnvtvd
      241 swkvhkesds hqfrvmaavl rhcllivgpt edkteelhsn avnllsnvpv scldvlicpl
      301 theetaqeaa tldelpgdkt aekdtalkss amvyngmnme aihvllsfme kridkgssyr
      361 egltpvlsll tecsrahrni rkflkdqvlp plrdvtnrpe vgstvrnklv rlmthvdlgv
      421 kqiaaeflfv lckervdsll kytgygnaag llaargllag grgdnwysed edtdteeykn
      481 akpkeellkp mglkpdgtit pleealsqys vieetssdtd
//
LOCUS       NP_001424904             381 aa            linear   ROD 11-APR-2025
DEFINITION  gasdermin D like 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424904 XP_038935096
VERSION     NP_001424904.1
DBSOURCE    REFSEQ: accession NM_001437975.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038935096.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.41290.1,
                                           SRR26360181.1065105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..381
                     /product="gasdermin D like 1 isoform 3"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=42222
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..>380
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..381
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437975.1:299..1444"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seeleleysv p
//
LOCUS       NP_001178506             505 aa            linear   ROD 11-APR-2025
DEFINITION  midnolin isoform 3 [Rattus norvegicus].
ACCESSION   NP_001178506 XP_002729811 XP_006240973
VERSION     NP_001178506.1
DBSOURCE    REFSEQ: accession NM_001191577.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Obara,Y. and Ishii,K.
  TITLE     Transcriptome Analysis Reveals That Midnolin Regulates mRNA
            Expression Levels of Multiple Parkinson's Disease Causative Genes
  JOURNAL   Biol Pharm Bull 41 (1), 20-23 (2018)
   PUBMED   29311479
  REMARK    GeneRIF: These findings indicate that MIDN regulates the expression
            of a wide variety of genes, including multiple Parkinson's Disease
            causative genes and is associated with Parkinson's Disease onset.
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Obara,Y., Imai,T., Sato,H., Takeda,Y., Kato,T. and Ishii,K.
  TITLE     Midnolin is a novel regulator of parkin expression and is
            associated with Parkinson's Disease
  JOURNAL   Sci Rep 7 (1), 5885 (2017)
   PUBMED   28724963
  REMARK    GeneRIF: MIDN promotes the expression of parkin E3 ubiquitin
            ligase, and that MIDN loss can trigger Parkinson's disease-related
            pathogenic mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Hofmeister-Brix,A., Kollmann,K., Langer,S., Schultz,J., Lenzen,S.
            and Baltrusch,S.
  TITLE     Identification of the ubiquitin-like domain of midnolin as a new
            glucokinase interaction partner
  JOURNAL   J Biol Chem 288 (50), 35824-35839 (2013)
   PUBMED   24187134
  REMARK    GeneRIF: midnolin plays a role in cellular signaling of adult
            tissues and regulates glucokinase enzyme activity in pancreatic
            beta cells
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Tsukahara,M., Suemori,H., Noguchi,S., Ji,Z.S. and Tsunoo,H.
  TITLE     Novel nucleolar protein, midnolin, is expressed in the
            mesencephalon during mouse development
  JOURNAL   Gene 254 (1-2), 45-55 (2000)
   PUBMED   10974535
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_006240973.1, XP_002729811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.27605.1,
                                           SRR26643290.24867.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..505
                     /product="midnolin isoform 3"
                     /note="midbrain nucleolar protein"
                     /calculated_mol_wt=53548
     Region          32..101
                     /region_name="Ubl_midnolin"
                     /note="ubiquitin-like (Ubl) domain found in midnolin and
                     similar proteins; cd01804"
                     /db_xref="CDD:340502"
     Region          155..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AE48.1)"
     Region          228..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AE48.1)"
     Region          440..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AE48.1)"
     CDS             1..505
                     /gene="Midn"
                     /coded_by="NM_001191577.2:475..1992"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:314623"
                     /db_xref="RGD:1309629"
ORIGIN      
        1 mepqpggars crrgapggac elsttaesaa pmslaihstt gtrydlsvph detveglrkr
       61 lsqrlkvpke rlallhkdtr lssgklqefg vgdgskltlv ptveaglmsq asrpeqsvmq
      121 alesltetqp patpgpgraa gggfrkyrli lfkrpwhrqg pqspergger pqvsdflsgr
      181 spltlalrvg dhmmfvqlql aaqhaplqhr hvlaaaaaaa aaargdssia tpvsspcrpv
      241 ssaarvppvs sspsspvsps pvtagtfqsh aasttcpeqt dcsppassnt tstpgssptp
      301 rsrkpgavie sfvnhapgvf sgtfsgtlhp ncqdssgrpr rdigtilqil ndllsatrhy
      361 qgmpasltql rchaqcspas papdltpktt sceklatpsl lqgqsqirmc kppgdrlrqt
      421 enratrckve rlqlllqqkr lrrkarrdar gpyhwtpsrk agrsdssssg gggspseatg
      481 lgldfedsvw kpevnpdiqs efvva
//
LOCUS       NP_001424867             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424867 XP_017450282
VERSION     NP_001424867.1
DBSOURCE    REFSEQ: accession NM_001437938.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_017450282.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.814045.1,
                                           SRR26360190.1733068.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437938.1:208..783"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424828             949 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001424828 XP_038934791
VERSION     NP_001424828.1
DBSOURCE    REFSEQ: accession NM_001437899.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934791.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.20662.1,
                                           SRR26643298.41658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..949
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=103214
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          645..>940
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..949
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437899.1:512..3361"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlvsth
      541 hlhssseded iegtfpnels lqqafseyqi qqmtanfvdq fgfndeefad qddninapfd
      601 riaeinfnie adedspsaal feaccsdriq pfdddeediw edeetrctar vmararfgap
      661 htsenyskka vghggqgrkt gsptarnvpg latpssptqk egprsesdsa gttwtavfde
      721 pvnplsaasg aardvgssaw aagpsvaeek gwakftdfqp fccsetgprc sspvdmdhsn
      781 aeggqspgpe kafgptspca wnvcvtrkap lvasdssssg gsdseddeka agavealcag
      841 htgkaspppr taeaaagrae cpdstvlapa cpapsevtis pavatiapsk agsptativv
      901 sssvatavpp gpimavttta paivatlgtm tkdrktdalp dgaalngpv
//
LOCUS       NP_001100267             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001100267 XP_001069676 XP_217062
VERSION     NP_001100267.1
DBSOURCE    REFSEQ: accession NM_001106797.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217062.1, XP_001069676.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168739.1, FM071446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001106797.4:204..779"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001424900             488 aa            linear   ROD 11-APR-2025
DEFINITION  chaperone Ric-8B isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424900 XP_063119506
VERSION     NP_001424900.1
DBSOURCE    REFSEQ: accession NM_001437971.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Lopez-Benito,S., Lillo,C., Hernandez-Hernandez,A., Chao,M.V. and
            Arevalo,J.C.
  TITLE     ARMS/Kidins220 and synembryn-B levels regulate NGF-mediated
            secretion
  JOURNAL   J Cell Sci 129 (9), 1866-1877 (2016)
   PUBMED   26966186
  REMARK    GeneRIF: overexpression of ARMS blocked NGF-mediated secretion,
            without affecting basal secretion, a decrease in ARMS resulted in
            potentiation. Similar effects were observed with synembryn-B, a
            protein that interacts directly with ARMS. Downstream of ARMS and
            synembryn-B are Galphaq and Trio proteins, which modulate the
            activity of Rac1 in response to NGF
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Aguilar,R., Grandy,R., Meza,D., Sepulveda,H., Pihan,P., van
            Wijnen,A.J., Lian,J.B., Stein,G.S., Stein,J.L. and Montecino,M.
  TITLE     A functional N-terminal domain in C/EBPbeta-LAP* is required for
            interacting with SWI/SNF and to repress Ric-8B gene transcription
            in osteoblasts
  JOURNAL   J Cell Physiol 229 (10), 1521-1528 (2014)
   PUBMED   24585571
  REMARK    GeneRIF: Results indicate that a functional N-terminus in
            C/EBPbeta-LAP* is required for interacting with SWI/SNF and for
            Ric-8B gene repression in osteoblasts.
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Chan,P., Gabay,M., Wright,F.A. and Tall,G.G.
  TITLE     Ric-8B is a GTP-dependent G protein alphas guanine nucleotide
            exchange factor
  JOURNAL   J Biol Chem 286 (22), 19932-19942 (2011)
   PUBMED   21467038
  REMARK    GeneRIF: Ric-8BFL-catalyzed nucleotide exchange probably proceeds
            in the forward direction to produce Galpha-GTP in cells.
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Klattenhoff,C., Montecino,M., Soto,X., Guzman,L., Romo,X.,
            Garcia,M.A., Mellstrom,B., Naranjo,J.R., Hinrichs,M.V. and Olate,J.
  TITLE     Human brain synembryn interacts with Gsalpha and Gqalpha and is
            translocated to the plasma membrane in response to isoproterenol
            and carbachol
  JOURNAL   J Cell Physiol 195 (2), 151-157 (2003)
   PUBMED   12652642
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Tall,G.G., Krumins,A.M. and Gilman,A.G.
  TITLE     Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein
            guanine nucleotide exchange factor
  JOURNAL   J Biol Chem 278 (10), 8356-8362 (2003)
   PUBMED   12509430
  REMARK    GeneRIF: two mammalian homologs of the Caenorhabditis elegans
            protein Ric-8 were identified: Ric-8A (Ric-8/synembryn) and Ric-8B
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119506.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.19206.1,
                                           SRR26643295.27520.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..488
                     /product="chaperone Ric-8B isoform 3"
                     /note="synembryn-B; resistance to inhibitors of
                     cholinesterase 8 homolog B; resistance to inhibitors of
                     cholinesterase 8B; heterotrimeric G protein guanine
                     nucleotide exchange factor-like protein Ric-8B; chaperone
                     Ric-8B"
                     /calculated_mol_wt=54601
     Region          66..451
                     /region_name="Ric8"
                     /note="Guanine nucleotide exchange factor synembryn;
                     pfam10165"
                     /db_xref="CDD:462973"
     CDS             1..488
                     /gene="Ric8b"
                     /coded_by="NM_001437971.1:88..1554"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:314681"
                     /db_xref="RGD:631419"
ORIGIN      
        1 mdeeralyiv rageagaier vlrdysdkhr atfkfesade dkrkklcegi fkvlvkgvpt
       61 tcqvpclevl rilsrdkkil apvtteenmq illrlaklhe sddslekvse fpviveslkc
      121 lcnivfnsqv aqqlslelnl aaklcnllrk ckdrkfindi kcfdlrllfv lsllhtdirs
      181 qlryelqglp lltqilesaf sikwtdeyes aidhsgppls pqetdcaiea lkalfnvtvd
      241 swkvhkesds hqfrvmaavl rhcllivgpt edkteelhsn avnllsnvpv scldvlicpl
      301 theetaqeaa tldelpgdkt aekdtalkss amvyngmnme aihvllsfme kridkvlppl
      361 rdvtnrpevg stvrnklvrl mthvdlgvkq iaaeflfvlc kervdsllky tgygnaagll
      421 aargllaggr gdnwyseded tdteeyknak pkeellkpmg lkpdgtitpl eealsqysvi
      481 eetssdtd
//
LOCUS       NP_001424862             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424862 XP_038934870
VERSION     NP_001424862.1
DBSOURCE    REFSEQ: accession NM_001437933.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934870.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1594368.1,
                                           SRR26360190.1392179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437933.1:243..818"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_596889                581 aa            linear   ROD 11-APR-2025
DEFINITION  protein LYRIC isoform 1 [Rattus norvegicus].
ACCESSION   NP_596889 XP_003750382 XP_006241584
VERSION     NP_596889.1
DBSOURCE    REFSEQ: accession NM_133398.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Xiang,Y., Duan,Y., Peng,Z., Huang,H., Ding,W., Chen,E., Liu,Z.,
            Dou,C., Li,J., Ou,J., Wan,Q., Yang,B. and He,Z.
  TITLE     Microparticles from Hyperphosphatemia-Stimulated Endothelial Cells
            Promote Vascular Calcification Through Astrocyte-Elevated Gene-1
  JOURNAL   Calcif Tissue Int 111 (1), 73-86 (2022)
   PUBMED   35195734
  REMARK    GeneRIF: Microparticles from Hyperphosphatemia-Stimulated
            Endothelial Cells Promote Vascular Calcification Through
            Astrocyte-Elevated Gene-1.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Wang,Y., Zhang,W., Zhu,X., Wang,Y., Mao,X., Xu,X. and Wang,Y.
  TITLE     Upregulation of AEG-1 Involves in Schwann Cell Proliferation and
            Migration After Sciatic Nerve Crush
  JOURNAL   J Mol Neurosci 60 (2), 248-257 (2016)
   PUBMED   27351433
  REMARK    GeneRIF: AEG-1 was expressed mainly in Schwann cells of the distal
            sciatic nerve segment from injury.  Interference of AEG-1 inhibited
            both proliferation and migration of Schwann cells.
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Watanabe,A., Tatematsu,M., Saeki,K., Shibata,S., Shime,H.,
            Yoshimura,A., Obuse,C., Seya,T. and Matsumoto,M.
  TITLE     Raftlin is involved in the nucleocapture complex to induce
            poly(I:C)-mediated TLR3 activation
  JOURNAL   J Biol Chem 286 (12), 10702-10711 (2011)
   PUBMED   21266579
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Emdad,L., Sarkar,D., Su,Z.Z., Randolph,A., Boukerche,H., Valerie,K.
            and Fisher,P.B.
  TITLE     Activation of the nuclear factor kappaB pathway by astrocyte
            elevated gene-1: implications for tumor progression and metastasis
  JOURNAL   Cancer Res 66 (3), 1509-1516 (2006)
   PUBMED   16452207
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Kang,D.C., Su,Z.Z., Sarkar,D., Emdad,L., Volsky,D.J. and
            Fisher,P.B.
  TITLE     Cloning and characterization of HIV-1-inducible astrocyte elevated
            gene-1, AEG-1
  JOURNAL   Gene 353 (1), 8-15 (2005)
   PUBMED   15927426
REFERENCE   9  (residues 1 to 581)
  AUTHORS   Britt,D.E., Yang,D.F., Yang,D.Q., Flanagan,D., Callanan,H.,
            Lim,Y.P., Lin,S.H. and Hixson,D.C.
  TITLE     Identification of a novel protein, LYRIC, localized to tight
            junctions of polarized epithelial cells
  JOURNAL   Exp Cell Res 300 (1), 134-148 (2004)
   PUBMED   15383321
REFERENCE   10 (residues 1 to 581)
  AUTHORS   Sutherland,H.G., Lam,Y.W., Briers,S., Lamond,A.I. and Bickmore,W.A.
  TITLE     3D3/lyric: a novel transmembrane protein of the endoplasmic
            reticulum and nuclear envelope, which is also present in the
            nucleolus
  JOURNAL   Exp Cell Res 294 (1), 94-105 (2004)
   PUBMED   14980505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006241584.1, XP_003750382.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.28375.1,
                                           SRR26360194.2156001.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..581
                     /product="protein LYRIC isoform 1"
                     /note="protein LYRIC; lysine-rich CEACAM1 co-isolated
                     protein; metastasis adhesion protein"
                     /calculated_mol_wt=63838
     Region          1..71
                     /region_name="Activation of NF-kappa-B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          6..422
                     /region_name="LYRIC"
                     /note="Lysine-rich CEACAM1 co-isolated protein family;
                     pfam15686"
                     /db_xref="CDD:434858"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          72..168
                     /region_name="Interaction with BCCIP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          77..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          100..204
                     /region_name="Interaction with RELA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            263
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q80WJ7; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          280..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Region          380..442
                     /region_name="Lung-homing for mammary tumors.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE4; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1W6.2)"
     CDS             1..581
                     /gene="Mtdh"
                     /gene_synonym="Lyric"
                     /coded_by="NM_133398.3:320..2065"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:170910"
                     /db_xref="RGD:620992"
ORIGIN      
        1 maarswqdel aqqaeegsar lrellsvglg flrtelgldl glepkrypsw vilvgtgalg
       61 llllfllgyg waaacagark krrspprkre evtpptpape dpaqlknlrs eeqkkknrkk
      121 lpekpkpngr tveipedevv rtprsitakq ppetdkknek skknkkksks dakavqnssr
      181 hdgkevdega wetkishrek rqqrkrdkvl tdsgsldsti pgientitvt teqlttasfp
      241 vgskknkgds hlnvqvsnfk sgkgdstlqv ssglnenitv ngggwseksv klssqlsage
      301 ekwnsvppas agkrkteqsa wtqdpgdtna ngkdwgrnws drsifsgigs taepvsqstt
      361 sdyqwdgsrn qphiddewsg lnglssadps sdwnapaeew gnwvdedras llksqepisn
      421 dqkdsdddke kgegalptgk skkkkkkkkk qgednsitqd tedlekdtre elpvntskar
      481 pkqekacslk tmstsdpvev liknsqpikt lppaisaeps vtlskgdsdk sssqvppmlq
      541 dtdkpksnak qnsvppsqtk setnwespkq ikkkkkarre t
//
LOCUS       NP_877968                520 aa            linear   ROD 11-APR-2025
DEFINITION  amphoterin-induced protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_877968
VERSION     NP_877968.3
DBSOURCE    REFSEQ: accession NM_182816.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Li,Z., Khan,M.M., Kuja-Panula,J., Wang,H., Chen,Y., Guo,D.,
            Chen,Z.J., Lahesmaa,R., Rauvala,H. and Tian,L.
  TITLE     AMIGO2 modulates T cell functions and its deficiency in mice
            ameliorates experimental autoimmune encephalomyelitis
  JOURNAL   Brain Behav Immun 62, 110-123 (2017)
   PUBMED   28119027
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Kanda,Y., Osaki,M., Onuma,K., Sonoda,A., Kobayashi,M., Hamada,J.,
            Nicolson,G.L., Ochiya,T. and Okada,F.
  TITLE     Amigo2-upregulation in Tumour Cells Facilitates Their Attachment to
            Liver Endothelial Cells Resulting in Liver Metastases
  JOURNAL   Sci Rep 7, 43567 (2017)
   PUBMED   28272394
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Park,H., Lee,S., Shrestha,P., Kim,J., Park,J.A., Ko,Y., Ban,Y.H.,
            Park,D.Y., Ha,S.J., Koh,G.Y., Hong,V.S., Mochizuki,N., Kim,Y.M.,
            Lee,W. and Kwon,Y.G.
  TITLE     AMIGO2, a novel membrane anchor of PDK1, controls cell survival and
            angiogenesis via Akt activation
  JOURNAL   J Cell Biol 211 (3), 619-637 (2015)
   PUBMED   26553931
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Rabenau,K.E., O'Toole,J.M., Bassi,R., Kotanides,H., Witte,L.,
            Ludwig,D.L. and Pereira,D.S.
  TITLE     DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
            expressed in human gastric adenocarcinoma: effects on ploidy,
            chromosomal stability, cell adhesion/migration and tumorigenicity
  JOURNAL   Oncogene 23 (29), 5056-5067 (2004)
   PUBMED   15107827
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Ono,T., Sekino-Suzuki,N., Kikkawa,Y., Yonekawa,H. and Kawashima,S.
  TITLE     Alivin 1, a novel neuronal activity-dependent gene, inhibits
            apoptosis and promotes survival of cerebellar granule neurons
  JOURNAL   J Neurosci 23 (13), 5887-5896 (2003)
   PUBMED   12843293
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Nov 27, 2020 this sequence version replaced NP_877968.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AB078879.1, AY237730.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..520
                     /product="amphoterin-induced protein 2 precursor"
                     /note="amphoterin-induced protein 2; alivin 1; AMIGO-2;
                     amphoterin induced gene 2; transmembrane protein AMIGO2;
                     transmembrane protein AMIGO2-like"
                     /calculated_mol_wt=53754
     sig_peptide     1..37
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=4024
     mat_peptide     38..520
                     /product="Amphoterin-induced protein 2.
                     /evidence=ECO:0000255. /id=PRO_0000014512"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=53754
     Region          50..71
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          68..89
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          <69..>229
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          72..94
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          93..114
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          96..117
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          117..138
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          118..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          141..162
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          142..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          165..186
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          166..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          192..213
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          219..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          297..367
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          305..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          319..323
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..341
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          359..364
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          437..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          498..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     CDS             1..520
                     /gene="Amigo2"
                     /gene_synonym="Ali1"
                     /coded_by="NM_182816.4:720..2282"
                     /db_xref="GeneID:300186"
                     /db_xref="RGD:727911"
ORIGIN      
        1 mslrfhtlpt lpravkpgcr ellcllviav mvspsssglc ptacicatdi vsctnknlsk
       61 vpgnlfrlik rldlsynrig lldadwipvs fvklstlivr hnnitsistg sfsttpnlkc
      121 ldlssnrlks vksamfqelk vlevlllynn hisyldpaaf gglshlqkly lsgnfltkfp
      181 mdlyvgrfkl adltfldvsy nqiasipmhh inlvpgkqlr giflhgnpfv cdcslysllt
      241 fwyrrhfnsv tdfkhdytcr lwldsrhshq llllqdsfln cshsvingsf halgfiheaq
      301 vgeraivhcd gktgngntdf iwvgpdnrll epdkdtgnfr vfyngslvie npgfedagvy
      361 sciamnrqrl lnetvdimin vsnftinrsh haheafntaf ttlaacvvsi vlvllylylt
      421 pcpckcrdkr qknalnqsna hssilspgpt rdasaedrka gkrvvflepl kdpavgqngk
      481 vklvpsetvi aegilkssra ksdsdsvnsv fsdtpfvast
//
LOCUS       NP_001424875            2057 aa            linear   ROD 11-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424875 XP_038948967
VERSION     NP_001424875.1
DBSOURCE    REFSEQ: accession NM_001437946.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2057)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2057)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2057)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2057)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2057)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038948967.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.37512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2057
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2057
                     /product="dedicator of cytokinesis protein 9 isoform 5"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=234704
     Region          43..153
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          167..290
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          634..823
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1599..2013
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1703,1713,1715..1716,1718..1719,1722..1723,
                     1725..1726,1729..1730)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1737..1740,1742,1771..1772,1774..1777,1779..1780,
                     1799..1801,1818,1820,1849,1851,1858..1859,1865,1904..1905,
                     1908,1922,1924,1928,1931..1933,1936..1939,1941..1942,1945,
                     1973,1991..1992,1994..1995,1998)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1936..1941
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2057
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001437946.1:138..6311"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 mqadkyrtsg rndkkelvie splqykdaaq adseaensal akpkliepld yenvivqkkt
       61 qilndclrem llfpyddfqt ailrrqgryv rstvpanaee eaqslfvtec iktynsdwhl
      121 vtyhyedysg efrqlpnkva kldklpvhvy evdeeadkde daaslgsqkg gitkhgwlyk
      181 gnmnsaisvt mrsfkrrffh liqlgdgsyn lnfykdekis kepkgsifld scmgviqnnr
      241 vrrfafelkm qdkssyllaa dseaemeewv tvlnkilqln feaamqekrn gdpheddeqs
      301 klegsgsgld sylpelakst reaeiklkse srvklfyldp dtqkldfssa epevkpfeek
      361 fgkrilvkcn dlsfnlqccv aeneegpttn vepffvtlsl fdikynrkis adfhvdlnhf
      421 svrqmlapas pvlmnggqsp pafqdalqaa mqypkqgifs vtcphpdifl variekvlqg
      481 sithcaepym kssdsskvaq kvlknakqac qrlgqyrmpf awaartlfkd tsgnldknar
      541 fsaiyrqdsn klsnedmlkl ladfrkpekm aklpvilgnl ditidnvscd fpnylnssyi
      601 pmrqfetcsk spitfeveef vpcipkhtqp ytvysnhlyv ypkylrydsq ksfakarnia
      661 iciefkdsde edsqplkciy grpggpvftr salaavlhhq qspefydeik ielpaqlhek
      721 hhllftffhv scdnstkgst kkkdavetqv gfswlpllkd grvltneqhi pvsanlpsgy
      781 lgyqelsmgr hygpevkwve ggkpllkist hlvstvytqd qhlhnffqyc qktesgaqas
      841 gselvkylks lhameghvmi aflptilnql frvltratqe evavnvtrvi ihvvaqchee
      901 gleshlrsyv kfaykaepyi aseyktvhee ltksmttilk psadfltsnk llkyswfffd
      961 vliksmaqhl iennkvkllr nqrfpasyhh avetvvnmlm phitqkfrdn peasknanhs
     1021 lavfikrcft fmdrgfvfkq innyiscfap gdpktlfeyk feflrvvcnh ehyiplnlpm
     1081 pfgkgriqry qdlqldyslt defcrnhflv glllrevgta lqefrevrvi avsvlknlli
     1141 khsfddryts rshqariatl ylplfgllie nvqrinvrdv spfpvnpgsi skdealavpt
     1201 gnplmtpqkg ntldhslhkd llgaisgias pytastpnin svrnadsrgs listdsgnsl
     1261 pdrnpeksns ldkqqqsgml gnsvvrcdkl dqseiksllm cflyvlksms ddalftywnk
     1321 astaelmdff tisevclhqf qymgkryias vrkissvlgi svdngyghse advahqslle
     1381 aniatevclt aldtlslftl afknqlladh ghnplmkkvf dvylcflqkh qsemalknvf
     1441 talrsliykf pstfyegrad mcaslcyevl kccnsklssi rteasqllyf lmrnnfdytg
     1501 kksfvrthlq viisvsqlia dvvgiggtrf qqslsiinnc ansdrlikht sfssdvkdlt
     1561 krirtvlmat aqmkehendp emlvdlqysl aksyastpel rktwldsmar ihvkngdlse
     1621 aamcyvhvta lvaeyltrkg mfrqgctafr vitpnideea smmedvgmqd vhfnedvlme
     1681 lleqcadglw kaeryeliad iykliipiye krrdferlah lydtlhrays kvtevmhsgr
     1741 rllgtyfrva ffgqgffede dgkeyiykep kltplseisq rllklysdkf gsenvkmiqd
     1801 sgkvnpkdld skfayiqvth vtpffdekel qerkteferc hnirrfmfem pftqtgkrqg
     1861 gveeqckrrt iltaihcfpy vkkripvmyq hhtdlnpiev aidemskkva elrqlcssae
     1921 vdmiklqlkl qgsvsvqvna gplayarafl ddtntkrypd nkvkllkevf rqfveacgqa
     1981 lavnerlike dqleyqeemk anyremakel sdimreqicp leektsvlpn slhifnaisg
     2041 tptstvvqgl tssssvv
//
LOCUS       NP_001424863             191 aa            linear   ROD 11-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424863 XP_038934874
VERSION     NP_001424863.1
DBSOURCE    REFSEQ: accession NM_001437934.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934874.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2817719.1,
                                           SRR26360181.2600024.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437934.1:319..894"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001100259             922 aa            linear   ROD 11-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001100259 XP_001054912 XP_217014
VERSION     NP_001100259.1
DBSOURCE    REFSEQ: accession NM_001106789.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217014.4, XP_001054912.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.29797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..922
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=100195
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          618..>913
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..922
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001106789.2:595..3363"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlafse
      541 yqiqqmtanf vdqfgfndee fadqddnina pfdriaeinf nieadedsps aalfeaccsd
      601 riqpfdddee diwedeetrc tarvmararf gaphtsenys kkavghggqg rktgsptarn
      661 vpglatpssp tqkegprses dsagttwtav fdepvnplsa asgaardvgs sawaagpsva
      721 eekgwakftd fqpfccsetg prcsspvdmd hsnaeggqsp gpekafgpts pcawnvcvtr
      781 kaplvasdss ssggsdsedd ekaagaveal caghtgkasp pprtaeaaag raecpdstvl
      841 apacpapsev tispavatia pskagsptat ivvsssvata vppgpimavt ttapaivatl
      901 gtmtkdrktd alpdgaalng pv
//
LOCUS       NP_001424724             239 aa            linear   ROD 11-APR-2025
DEFINITION  BPI fold-containing family A member 3 isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424724 XP_006235424
VERSION     NP_001424724.1
DBSOURCE    REFSEQ: accession NM_001437795.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006235424.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1468411.1,
                                           SRR26360181.79486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..239
                     /product="BPI fold-containing family A member 3 isoform 3
                     precursor"
                     /calculated_mol_wt=24326
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2277
     Region          47..219
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     CDS             1..239
                     /gene="Bpifa3"
                     /gene_synonym="Splunc3"
                     /coded_by="NM_001437795.1:202..921"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:690402"
                     /db_xref="RGD:1596102"
ORIGIN      
        1 mhllwrflvl llgllalpsa lpkqpwpglt kahkdgrstl ariiaqgllk hnaegriqsm
       61 rlldrlnvsg tvapgmvswl isgmnfqqqq eisinitnvq ldcggiqmaf pkewfsanit
      121 lefdiefklp fnsnilktha qmglaaeswl ekdefgrrkl vtgrcqmeps sdsasmttea
      181 aspkmknflh nlreslgkvi pnlvesqvcp ligeilrqld vkllkglveq vaahnlgqp
//
LOCUS       NP_001128091            1088 aa            linear   ROD 11-APR-2025
DEFINITION  TELO2-interacting protein 1 homolog [Rattus norvegicus].
ACCESSION   NP_001128091 XP_001068226 XP_006235490 XP_575280
VERSION     NP_001128091.1
DBSOURCE    REFSEQ: accession NM_001134619.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Fernandez-Saiz,V., Targosz,B.S., Lemeer,S., Eichner,R., Langer,C.,
            Bullinger,L., Reiter,C., Slotta-Huspenina,J., Schroeder,S.,
            Knorn,A.M., Kurutz,J., Peschel,C., Pagano,M., Kuster,B. and
            Bassermann,F.
  TITLE     SCFFbxo9 and CK2 direct the cellular response to growth factor
            withdrawal via Tel2/Tti1 degradation and promote survival in
            multiple myeloma
  JOURNAL   Nat Cell Biol 15 (1), 72-81 (2013)
   PUBMED   23263282
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Laplante,M. and Sabatini,D.M.
  TITLE     mTOR signaling in growth control and disease
  JOURNAL   Cell 149 (2), 274-293 (2012)
   PUBMED   22500797
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_006235490.1, XP_575280.2, XP_001068226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.5105.1,
                                           SRR26643286.12046.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..1088
                     /product="TELO2-interacting protein 1 homolog"
                     /note="TEL2-interacting protein 1 homolog; Tel2
                     interacting protein 1 homolog"
                     /calculated_mol_wt=120980
     CDS             1..1088
                     /gene="Tti1"
                     /gene_synonym="RGD1562582"
                     /coded_by="NM_001134619.2:98..3364"
                     /db_xref="GeneID:499935"
                     /db_xref="RGD:1562582"
ORIGIN      
        1 mavfdtpeea fgvlrpvcvq ltktqtvenv ehlqtqlqai sdtalqelqq yilfplrfal
       61 ktpgpkrerl vqsvvecltf vlsstcvreq ellqelfsel saclyspnsq kpaalseelk
      121 laviqglstl mhsayrdiil tfyepsilpr lgfavslllg laeqekskqi kiaalqclqv
      181 lllqcdcqdh prpldeleqq qlgdllasfl pgistaltrv itgdfkqghs ivvsslkvfy
      241 ktvgfimade qltripkvra kpavehkvaa lmihreadwv kstggklail ikkiidcvsv
      301 hphwkvrlel vefvevllfk csqslvestg pllkvlvglv ndessevqaq cntvlrrlad
      361 qkvvvgsral adilseslhs latslprlmn tqddqgkfst lslllgylkl lgpkvhviln
      421 svahvqrlsr aliqvlelev advkmveerr wnsdnlsasa easaarpwsr vqrryfrcft
      481 dervflllrk icqllgyygd lyllvdhfme lyhtsivyrk qaamilnelv vgaagldved
      541 ihyecastsp eelreivksi leeytsqenw ylitcieaee eeevmmkqqg lqavtsgvht
      601 cqvvsfpals kpspticsmn sniwqiciql egigqfayal gkdfrlllms alypvlekag
      661 dqtllisqva astmvdicha cgynsvqhli nqnsdylvng islnlrhlal hphtpkvlev
      721 mlrnsdasll plvadvvqdv latldqfydk raasfvsvlh allaalahwf pdsgstgqlq
      781 qhsleevarq tpaaskaspt aedierfvls ylqekdmaeg nvsdleaeev lseeqsvppr
      841 vdesdalpdv epplpvhiqi akdvmercih llsdknlkvr lkvldvlglc vevlqthknq
      901 llplahrawp slvhrltsdd plavlrafkv lqtlgsrcgd flrsrfckdv lpklasslvt
      961 qapisaragp vyshtlafkl qlavlqglgp lcesldlgeg dlnkvadacl iylstkqpvk
     1021 lqeaarsvfl hlikvdpdst wlllhqlhcp vqqftaphps lhpvqwqgat kpqnpyatnv
     1081 chlllqlq
//
LOCUS       NP_001424721             211 aa            linear   ROD 11-APR-2025
DEFINITION  uncharacterized protein C20orf144 homolog isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424721 XP_006235418
VERSION     NP_001424721.1
DBSOURCE    REFSEQ: accession NM_001437792.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006235418.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.19793.1,
                                           SRR26360181.1434935.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..211
                     /product="uncharacterized protein C20orf144 homolog
                     isoform 2"
                     /note="uncharacterized protein C20orf144 homolog"
                     /calculated_mol_wt=23538
     Region          1..203
                     /region_name="Bclt"
                     /note="Putative Bcl-2 like protein of testis; pfam15318"
                     /db_xref="CDD:434628"
     CDS             1..211
                     /gene="C3h20orf144"
                     /gene_synonym="RGD1561517"
                     /coded_by="NM_001437792.1:54..689"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:499927"
                     /db_xref="RGD:1561517"
ORIGIN      
        1 mgnsgshkrt kapnqaskdr ppdmdkarhk qffshlkrkk psptasqhat fpffqwreap
       61 dparvgenpr ikagktkivl lfpldkrqql aeaaagpfvr pvrpaedplg aptcfpatva
      121 pmlrgagdgv drregarare mkrilvlllq ldarlqeegr rvagrpggga kaqqywqply
      181 ahlltqreac gegdpreeqp rkrrrcprpr p
//
LOCUS       NP_001424651            1082 aa            linear   ROD 11-APR-2025
DEFINITION  histone deacetylase 4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424651 XP_063123536
VERSION     NP_001424651.1
DBSOURCE    REFSEQ: accession NM_001437722.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Gu,X., Li,F., Che,X., Wei,X. and Li,P.
  TITLE     HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model
  JOURNAL   BMC Musculoskelet Disord 25 (1), 467 (2024)
   PUBMED   38879481
  REMARK    GeneRIF: HDAC4 represses ER stress induced chondrocyte apoptosis by
            inhibiting ATF4 and attenuates cartilage degeneration in an
            osteoarthritis rat model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Zhang,D., Du,J., Yu,M. and Suo,L.
  TITLE     Urine-derived stem cells-extracellular vesicles ameliorate diabetic
            osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by delivering
            microRNA-26a-5p
  JOURNAL   Cell Biol Toxicol 39 (5), 2243-2257 (2023)
   PUBMED   35554780
  REMARK    GeneRIF: Urine-derived stem cells-extracellular vesicles ameliorate
            diabetic osteoporosis through HDAC4/HIF-1alpha/VEGFA axis by
            delivering microRNA-26a-5p.
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Yang,Y., Wang,Z., Xu,Y., Liu,X., Sun,Y. and Li,W.
  TITLE     Knockdown of lncRNA H19 alleviates ox-LDL-induced HCAECs
            inflammation and injury by mediating miR-20a-5p/HDAC4 axis
  JOURNAL   Inflamm Res 71 (9), 1109-1121 (2022)
   PUBMED   35854140
  REMARK    Erratum:[Inflamm Res. 2023 Apr;72(4):893. doi:
            10.1007/s00011-023-01701-7. PMID: 36806965]
REFERENCE   4  (residues 1 to 1082)
  AUTHORS   Moreno-Ruperez,A., Priego,T., Gonzalez-Nicolas,M.A.,
            Lopez-Calderon,A., Lazaro,A. and Martin,A.I.
  TITLE     Role of Glucocorticoid Signaling and HDAC4 Activation in Diaphragm
            and Gastrocnemius Proteolytic Activity in Septic Rats
  JOURNAL   Int J Mol Sci 23 (7), 3641 (2022)
   PUBMED   35408999
  REMARK    GeneRIF: Role of Glucocorticoid Signaling and HDAC4 Activation in
            Diaphragm and Gastrocnemius Proteolytic Activity in Septic Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1082)
  AUTHORS   Wei,W., Chen,W. and He,N.
  TITLE     HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation
  JOURNAL   J Transl Med 19 (1), 258 (2021)
   PUBMED   34118928
  REMARK    GeneRIF: HDAC4 induces the development of asthma by increasing
            Slug-upregulated CXCL12 expression through KLF5 deacetylation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1082)
  AUTHORS   Fischle,W., Dequiedt,F., Hendzel,M.J., Guenther,M.G., Lazar,M.A.,
            Voelter,W. and Verdin,E.
  TITLE     Enzymatic activity associated with class II HDACs is dependent on a
            multiprotein complex containing HDAC3 and SMRT/N-CoR
  JOURNAL   Mol Cell 9 (1), 45-57 (2002)
   PUBMED   11804585
REFERENCE   7  (residues 1 to 1082)
  AUTHORS   Lu,J., McKinsey,T.A., Zhang,C.L. and Olson,E.N.
  TITLE     Regulation of skeletal myogenesis by association of the MEF2
            transcription factor with class II histone deacetylases
  JOURNAL   Mol Cell 6 (2), 233-244 (2000)
   PUBMED   10983972
REFERENCE   8  (residues 1 to 1082)
  AUTHORS   Grozinger,C.M. and Schreiber,S.L.
  TITLE     Regulation of histone deacetylase 4 and 5 and transcriptional
            activity by 14-3-3-dependent cellular localization
  JOURNAL   Proc Natl Acad Sci U S A 97 (14), 7835-7840 (2000)
   PUBMED   10869435
REFERENCE   9  (residues 1 to 1082)
  AUTHORS   Lemercier,C., Verdel,A., Galloo,B., Curtet,S., Brocard,M.P. and
            Khochbin,S.
  TITLE     mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A
            transcriptional activity
  JOURNAL   J Biol Chem 275 (20), 15594-15599 (2000)
   PUBMED   10748098
REFERENCE   10 (residues 1 to 1082)
  AUTHORS   Grozinger,C.M., Hassig,C.A. and Schreiber,S.L.
  TITLE     Three proteins define a class of human histone deacetylases related
            to yeast Hda1p
  JOURNAL   Proc Natl Acad Sci U S A 96 (9), 4868-4873 (1999)
   PUBMED   10220385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063123536.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.50117.1,
                                           SRR26643284.12627.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..1082
                     /product="histone deacetylase 4 isoform 1"
                     /EC_number="3.5.1.98"
                     /note="HD4"
                     /calculated_mol_wt=119061
     Region          62..151
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(63..64,66..67,70,74,77..78,81..82,84..85,88..89,
                     91..92,95..97,99..101,103..104,106..108,110..111,114,
                     117..118,121..123)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(63..64,66..67,70,74,77,81,84,88..89,91..92,95..96,
                     99,103,106,110,117,121)
                     /site_type="other"
                     /note="dimer interface A, C [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(74,78,82,85,89,92,96..97,100..101,104,108,111)
                     /site_type="other"
                     /note="dimer interface A, D [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(92,96,107..108,111,118,122..123)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          117..312
                     /region_name="Interaction with MEF2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          132..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          204..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZM9; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          239..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          348..353
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and 14-3-3 proteins.
                     /evidence=ECO:0000250|UniProtKB:P56524"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          508..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          542..582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          623..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          647..1055
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Site            order(800..801,809..810,838,840,932,972)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Region          1049..1082
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     Region          1057..1082
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99P99.2)"
     CDS             1..1082
                     /gene="Hdac4"
                     /coded_by="NM_001437722.1:519..3767"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:363287"
                     /db_xref="RGD:619979"
ORIGIN      
        1 mssqshpdgl sgrdqpvell nparvnhmps tvdvatalpl qvapaavpmd lrldhqfslp
       61 lepalreqql qqellalkqk qqiqrqilia efqrqheqls rqheaqlheh ikqqqemlam
      121 khqqellehq rklerhrqeq elekqhreqk lqqlknkekg kesavastev kmklqefvln
      181 kkkalahrnl nhcmssdpry wygktqhssl dqssppqsgv sasynhpvlg mydakddfpl
      241 rktasepnlk lrsrlkqkva errsspllrr kdgpvatalk krpldvtdsa cssapgsgps
      301 spnsssgnvs tengiaptvp stpaetslah rlvtregsva plplytspsl pnitlglpat
      361 gpaagaagqq daerlalpal qqrislfpgt hltpylstsp lerdggaahn pllqhmvlle
      421 qpptqtplvt glgalplhtq slvgadrvsp sihklrqhrp lgrtqsaplp qnaqalqhlv
      481 iqqqhqqfle khkqqfqqqq lhlskmiskp sepprqpesh peeteeelre hqalldepyl
      541 drlpgqkeps lagvqvkqep ieseeeevea treaepsqrp ateqellfrq qallleqqri
      601 hqlrnyqasm eaagipvsfg shrplsraqs spasatfpms vqepptkprf ttglvydtlm
      661 lkhqctcgnt nshpehagri qsiwsrlqet glrgkcecir grkatleelq tvhseahtll
      721 ygtnplnrqk ldskkllgsl tsvfvrlpcg gvgvdsdtiw nevhssgaar lavgcvvelv
      781 fkvatgelkn gfavvrppgh haeestpmgf cyfnsvaiaa kllqqrlnvs kilivdwdvh
      841 hgngtqqafy ndpnvlymsl hryddgnffp gsgapdevgt gpgvgfnvnm aftggldppm
      901 gdaeylaafr tvvmpianef apdvvlvssg fdaveghptp lggynlsakc fgyltkqlmg
      961 laggrivlal egghdltaic daseacvsal lgneleplpe kvlhqrpnan avhsmekvmg
     1021 ihseywrclq rlsptvghsl ieaqkcenee aetvtamasl svgvkpaekr seeepmeeep
     1081 pl
//
LOCUS       NP_001424654             343 aa            linear   ROD 11-APR-2025
DEFINITION  RNA-binding protein 43 [Rattus norvegicus].
ACCESSION   NP_001424654 XP_063139611
VERSION     NP_001424654.1
DBSOURCE    REFSEQ: accession NM_001437725.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063139611.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.881445.1,
                                           SRR26643292.12418.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..343
                     /product="RNA-binding protein 43"
                     /note="rCG37778-like"
                     /calculated_mol_wt=38745
     Region          15..82
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          170..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7D9.1)"
     CDS             1..343
                     /gene="Rbm43"
                     /gene_synonym="RGD1306676"
                     /coded_by="NM_001437725.1:270..1301"
                     /db_xref="GeneID:311020"
                     /db_xref="RGD:1306676"
ORIGIN      
        1 masaltvkdp tvsertvvvs glpvglskdq lvkryfrdeg ghvekviypp rskgvayiif
       61 kekkvaqtii rqkkhplgse plltvshfse kvfnyvmail dlsvfrpqiv leslvvdlkk
      121 kiptlnfspl grsgkisvqg sflailklkq aliskaisal ennrkyager rnwtgqnprr
      181 vlqknensap tlgtsvpepa gspetlvldt dvflylkhkc qfyeptlsky hvlcqervdg
      241 dittlclqda rdgsypgsvr hvkelieewa qefylelrke llvlegrres ekrnmrqafe
      301 qlccryprvl mnvhrthidl igppsdtslf ktqlmksagq kvt
//
LOCUS       NP_001424720             473 aa            linear   ROD 11-APR-2025
DEFINITION  BPI fold-containing family B member 3 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424720 XP_006235414
VERSION     NP_001424720.1
DBSOURCE    REFSEQ: accession NM_001437791.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Andrault,J.B., Gaillard,I., Giorgi,D. and Rouquier,S.
  TITLE     Expansion of the BPI family by duplication on human chromosome 20:
            characterization of the RY gene cluster in 20q11.21 encoding
            olfactory transporters/antimicrobial-like peptides
  JOURNAL   Genomics 82 (2), 172-184 (2003)
   PUBMED   12837268
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Dear,T.N., Boehm,T., Keverne,E.B. and Rabbitts,T.H.
  TITLE     Novel genes for potential ligand-binding proteins in subregions of
            the olfactory mucosa
  JOURNAL   EMBO J 10 (10), 2813-2819 (1991)
   PUBMED   1915264
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006235414.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1434241.1,
                                           SRR22582424.718915.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..473
                     /product="BPI fold-containing family B member 3 isoform 2
                     precursor"
                     /note="Potential ligand-binding protein RYA3; long palate,
                     lung and nasal epithelium carcinoma-associated protein 3;
                     Long palate, lung and nasal epithelium carcinoma
                     associated protein 3; antimicrobial peptide RYA3"
                     /calculated_mol_wt=47848
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2120
     mat_peptide     21..473
                     /product="BPI fold-containing family B member 3.
                     /id=PRO_0000017172"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05701.1)"
                     /calculated_mol_wt=47848
     Site            26..32
                     /site_type="other"
                     /note="BPI dimerizatation interface [polypeptide binding]"
                     /db_xref="CDD:238164"
     Region          30..272
                     /region_name="BPI"
                     /note="BPI/LBP/CETP domain; Bactericidal
                     permeability-increasing protein (BPI) /
                     Lipopolysaccharide-binding protein (LBP) / Cholesteryl
                     ester transfer protein (CETP) domain; binds to and
                     neutralizes lipopolysaccharides from the outer membrane of
                     Gram-negative...; cl00188"
                     /db_xref="CDD:412206"
     Site            order(31,36,39,43,46,107,144,146,156,199,203,207,240)
                     /site_type="active"
                     /note="apolar binding pocket [active]"
                     /db_xref="CDD:238164"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05701.1)"
     Region          273..471
                     /region_name="BPI2"
                     /note="BPI/LBP/CETP C-terminal domain; smart00329"
                     /db_xref="CDD:128624"
     Site            order(279,284,287,291,294,353,386,388,397,433,437,441,467)
                     /site_type="active"
                     /note="apolar binding pocket [active]"
                     /db_xref="CDD:238164"
     CDS             1..473
                     /gene="Bpifb3"
                     /gene_synonym="Lplunc3; Rya3"
                     /coded_by="NM_001437791.1:64..1485"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:499924"
                     /db_xref="RGD:1565613"
ORIGIN      
        1 mmpgvyalll lwglatpclg lletvgtlar idkdelgkai qnslvggpil qnvlgtvtsv
       61 nqgllgaggl lggggllsyg glfslveels glkieeltlp tvsikllpgv gvqlslhtkv
      121 slhgsgplvg llqlaaevnv sskvalgmsp rgtpililkr cntllghisl tsgllptpif
      181 glveqtlckv lpgllcpvvd svlsvvnell gatlslvplg plgsveftla tlplisnqyi
      241 eldinpivks iagdvidfpk prlpvkmppk edhtsqvtvp lylfntvfgl lqtngaldld
      301 itpemvprni pltttdlaal apealgklpp gqhlllslrv mkspmillqn kkvtvsipvt
      361 ihvlssvpqg tpvalfqmng vmtlnahlvp sttklhisls lerltvqlas sfsqpfdasr
      421 leewlsdvvr aaymqklneh levgiplpki lnvnfansvv dvienavvlt vap
//
LOCUS       NP_001424684            1109 aa            linear   ROD 11-APR-2025
DEFINITION  activated CDC42 kinase 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424684 XP_038944232
VERSION     NP_001424684.1
DBSOURCE    REFSEQ: accession NM_001437755.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Strochlic,T.I., Stavrides,K.P., Thomas,S.V., Nicolas,E.,
            O'Reilly,A.M. and Peterson,J.R.
  TITLE     Ack kinase regulates CTP synthase filaments during Drosophila
            oogenesis
  JOURNAL   EMBO Rep 15 (11), 1184-1191 (2014)
   PUBMED   25223282
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Hitomi,Y., Heinzen,E.L., Donatello,S., Dahl,H.H., Damiano,J.A.,
            McMahon,J.M., Berkovic,S.F., Scheffer,I.E., Legros,B., Rai,M.,
            Weckhuysen,S., Suls,A., De Jonghe,P., Pandolfo,M., Goldstein,D.B.,
            Van Bogaert,P. and Depondt,C.
  TITLE     Mutations in TNK2 in severe autosomal recessive infantile onset
            epilepsy
  JOURNAL   Ann Neurol 74 (3), 496-501 (2013)
   PUBMED   23686771
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Abdallah,A.M., Zhou,X., Kim,C., Shah,K.K., Hogden,C.,
            Schoenherr,J.A., Clemens,J.C. and Chang,H.C.
  TITLE     Activated Cdc42 kinase regulates Dock localization in male germ
            cells during Drosophila spermatogenesis
  JOURNAL   Dev Biol 378 (2), 141-153 (2013)
   PUBMED   23562806
REFERENCE   4  (residues 1 to 1109)
  AUTHORS   Shen,H., Ferguson,S.M., Dephoure,N., Park,R., Yang,Y.,
            Volpicelli-Daley,L., Gygi,S., Schlessinger,J. and De Camilli,P.
  TITLE     Constitutive activated Cdc42-associated kinase (Ack)
            phosphorylation at arrested endocytic clathrin-coated pits of cells
            that lack dynamin
  JOURNAL   Mol Biol Cell 22 (4), 493-502 (2011)
   PUBMED   21169560
REFERENCE   5  (residues 1 to 1109)
  AUTHORS   Prieto-Echague,V., Gucwa,A., Brown,D.A. and Miller,W.T.
  TITLE     Regulation of Ack1 localization and activity by the amino-terminal
            SAM domain
  JOURNAL   BMC Biochem 11, 42 (2010)
   PUBMED   20979614
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1109)
  AUTHORS   Shen,F., Lin,Q., Gu,Y., Childress,C. and Yang,W.
  TITLE     Activated Cdc42-associated kinase 1 is a component of EGF receptor
            signaling complex and regulates EGF receptor degradation
  JOURNAL   Mol Biol Cell 18 (3), 732-742 (2007)
   PUBMED   17182860
REFERENCE   7  (residues 1 to 1109)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Purification and enzyme activity of ACK1
  JOURNAL   Methods Enzymol 406, 250-260 (2006)
   PUBMED   16472662
REFERENCE   8  (residues 1 to 1109)
  AUTHORS   Yokoyama,N., Lougheed,J. and Miller,W.T.
  TITLE     Phosphorylation of WASP by the Cdc42-associated kinase ACK1: dual
            hydroxyamino acid specificity in a tyrosine kinase
  JOURNAL   J Biol Chem 280 (51), 42219-42226 (2005)
   PUBMED   16257963
REFERENCE   9  (residues 1 to 1109)
  AUTHORS   Urena,J.M., La Torre,A., Martinez,A., Lowenstein,E., Franco,N.,
            Winsky-Sommerer,R., Fontana,X., Casaroli-Marano,R.,
            Ibanez-Sabio,M.A., Pascual,M., Del Rio,J.A., de Lecea,L. and
            Soriano,E.
  TITLE     Expression, synaptic localization, and developmental regulation of
            Ack1/Pyk1, a cytoplasmic tyrosine kinase highly expressed in the
            developing and adult brain
  JOURNAL   J Comp Neurol 490 (2), 119-132 (2005)
   PUBMED   16052498
REFERENCE   10 (residues 1 to 1109)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038944232.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.29826.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1109
                     /product="activated CDC42 kinase 1 isoform 2"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated CDC42 kinase 1; ACK-1; tyrosine kinase
                     non-receptor protein 2; activated p21cdc42Hs kinase"
                     /calculated_mol_wt=122670
     Region          38..99
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          162..419
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302,321..325,334,368)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(164..166,172,188,190,237..240,244,284,288..289,291,
                     302)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(284,288,321..325,334,368)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(301..311,313..327)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          427..476
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(429,431,436,454,456,471,473..474)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          481..546
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <649..1015
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          851..909
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          1030..1073
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          1060..1099
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1109
                     /gene="Tnk2"
                     /coded_by="NM_001437755.1:325..3654"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:303882"
                     /db_xref="RGD:1305957"
ORIGIN      
        1 mpaarrfpgl elsfpllarl rrrlytrlgs ssmqpeegtg wllellsevq lqqyflrlrd
       61 dlnitrlshf eyvknedlek igmgrpgqrr lweavkrrka mckrkswmsk vfsgkrqeae
      121 fpshhsqstf rkpsptpggl agegtlqslt cligekdlrl leklgdgsfg vvrrgewdap
      181 agktvsvavk clkpdvlsqp eamddfirev namhsldhrn lirlygvvlt ppmkmvtela
      241 plgslldrlr khqghfllgt lsryavqvae gmgyleskrf ihrdlaarnl llatrdlvki
      301 gdfglmralp qnddhyvmqe hrkvpfawca peslktrtfs hasdtwmfgv tlwemftygq
      361 epwiglngsq ilhkidkege rlprpedcpq diynvmvqcw ahkpedrptf valrdfllea
      421 qptdmralqd feepdklhiq mndvitvieg raenywwrgq ntrtlcvgpf prnvvtsvag
      481 lsaqdisqpl qnsfihtghg dsdprhcwgf pdridelylg npmdppdlls velstsrptq
      541 hlgrmkrepp prppqpaift hskwgcsgcl gprplsplsp lleeptydpv sedpdplssd
      601 fkrlglrkpa lprglwlakp sarvpgtkag rssggevtli dfgeepvapt prpcapslaq
      661 lamdacslld ktppqsptra lprplhptpv vdwdarplpp ppayddvaqd eddfevcsin
      721 stlvsaglpt gpsqgetnya fvpeqaqlpp alednlflpp qgggqppssa qtaeifqalq
      781 qecmrqlqvp tgqltpsptp ggddkpqvpp rvpipprptr prvglspapl geeeasrwpg
      841 psspprvppr eplspqgsrt psplvppgss plphrlsssp gktmpttqsf asdpkyatpq
      901 viqapgprag pcilpivrdg rkvssthyyl lperppyler yqrflreaqs peepaalpvp
      961 pllpppstpa paaptatvrp mpqaapdpka nfstnnsnpg aqppslrasa rlpqrgcpgd
     1021 gqeaarpadk vqmlqamvhg vtteecqaal rshswsiqra aqylkveqlf glglrprvec
     1081 hkvlemfdwn leqagchllg scgpahhkr
//
LOCUS       NP_001424701             354 aa            linear   ROD 11-APR-2025
DEFINITION  decorin precursor [Rattus norvegicus].
ACCESSION   NP_001424701 XP_006241347
VERSION     NP_001424701.1
DBSOURCE    REFSEQ: accession NM_001437772.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Hassan,G.M. and Ebrahim,R.H.
  TITLE     The myokine decorin improves the cardiac function in a rat model of
            isoprenaline-induced myocardial infarction
  JOURNAL   Can J Physiol Pharmacol 101 (6), 286-293 (2023)
   PUBMED   36917819
  REMARK    GeneRIF: The myokine decorin improves the cardiac function in a rat
            model of isoprenaline-induced myocardial infarction.
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Gaspar,R., Gomori,K., Kiss,B., Szantai,A., Paloczi,J., Varga,Z.V.,
            Pipis,J., Varadi,B., Agg,B., Csont,T., Ferdinandy,P., Bartekova,M.
            and Gorbe,A.
  TITLE     Decorin Protects Cardiac Myocytes against Simulated
            Ischemia/Reperfusion Injury
  JOURNAL   Molecules 25 (15), 3426 (2020)
   PUBMED   32731559
  REMARK    GeneRIF: Decorin Protects Cardiac Myocytes against Simulated
            Ischemia/Reperfusion Injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Lai,J., Chen,F., Chen,J., Ruan,G., He,M., Chen,C., Tang,J. and
            Wang,D.W.
  TITLE     Overexpression of decorin promoted angiogenesis in diabetic
            cardiomyopathy via IGF1R-AKT-VEGF signaling
  JOURNAL   Sci Rep 7, 44473 (2017)
   PUBMED   28290552
  REMARK    GeneRIF: overexpression of decorin ameliorated diabetic
            cardiomyopathy and promoted angiogenesis through the IGF1R-AKT-VEGF
            signaling pathway in vivo and in vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   6  (residues 1 to 354)
  AUTHORS   De Cosmo,S., Tassi,V., Thomas,S., Piras,G.P., Trevisan,R., Cavallo
            Perin,P., Bacci,S., Zucaro,L., Cisternino,C., Trischitta,V. and
            Viberti,G.C.
  TITLE     The Decorin gene 179 allelic variant is associated with a slower
            progression of renal disease in patients with type 1 diabetes
  JOURNAL   Nephron 92 (1), 72-76 (2002)
   PUBMED   12187087
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Schaefer,L., Raslik,I., Grone,H.J., Schonherr,E., Macakova,K.,
            Ugorcakova,J., Budny,S., Schaefer,R.M. and Kresse,H.
  TITLE     Small proteoglycans in human diabetic nephropathy: discrepancy
            between glomerular expression and protein accumulation of decorin,
            biglycan, lumican, and fibromodulin
  JOURNAL   FASEB J 15 (3), 559-561 (2001)
   PUBMED   11259366
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Asundi,V.K. and Dreher,K.L.
  TITLE     Molecular characterization of vascular smooth muscle decorin:
            deduced core protein structure and regulation of gene expression
  JOURNAL   Eur J Cell Biol 59 (2), 314-321 (1992)
   PUBMED   1493796
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Abramson,S.R. and Woessner,J.F. Jr.
  TITLE     cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin)
  JOURNAL   Biochim Biophys Acta 1132 (2), 225-227 (1992)
   PUBMED   1390895
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Kokenyesi,R. and Woessner,J.F. Jr.
  TITLE     Purification and characterization of a small dermatan sulphate
            proteoglycan implicated in the dilatation of the rat uterine cervix
  JOURNAL   Biochem J 260 (2), 413-419 (1989)
   PUBMED   2764879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006241347.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF110991.1, FQ223184.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..354
                     /product="decorin precursor"
                     /note="dermatan sulfate proteoglycan-II (decorin); DSPG;
                     PG40; PG-S2; bone proteoglycan II"
                     /calculated_mol_wt=38032
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1791
     mat_peptide     31..354
                     /product="Decorin. /id=PRO_0000032720"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
                     /calculated_mol_wt=36364
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000269|PubMed:2764879; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          48..80
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          57..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          68..88
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          78..>302
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          89..112
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          102..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          113..136
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          126..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          137..157
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          147..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..181
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          171..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          197..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          218..241
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          229..252
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          242..265
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          253..276
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          277..299
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          289..308
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01129.1)"
     Region          300..329
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     Region          312..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          330..354
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01129.1)"
     CDS             1..354
                     /gene="Dcn"
                     /coded_by="NM_001437772.1:183..1247"
                     /db_xref="GeneID:29139"
                     /db_xref="RGD:61895"
ORIGIN      
        1 mkatlvlfll aqvswagpfe qrglfdfmle deasgiipyd pdnplismcp yrcqchlrvv
       61 qcsdlgldkv pwefppdttl ldlqnnkite ikegafknlk dlhtlilvnn kiskispeaf
      121 kplvklerly lsknhlkelp eklpktlqel rlhdneitkl kksvfnglnr mivielggnp
      181 lknsgienga lqgmkglgyi risdtnitai pqglptsise lhldgnkiak vdaaslkgms
      241 nlsklglsfn sitvvengsl anvphlrelh ldnnkllrvp aglaqhkyvq vvylhnnnis
      301 evgqhdfclp syqtrktsyt avslysnpvr ywqihphtfr cvfgrstiql gnyk
//
LOCUS       NP_001424677            1181 aa            linear   ROD 11-APR-2025
DEFINITION  sodium/hydrogen exchanger 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424677 XP_017453414
VERSION     NP_001424677.1
DBSOURCE    REFSEQ: accession NM_001437748.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Wang,D., King,S.M., Quill,T.A., Doolittle,L.K. and Garbers,D.L.
  TITLE     A new sperm-specific Na+/H+ exchanger required for sperm motility
            and fertility
  JOURNAL   Nat Cell Biol 5 (12), 1117-1122 (2003)
   PUBMED   14634667
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_017453414.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.542339.1,
                                           SRR26643293.69081.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1181
                     /product="sodium/hydrogen exchanger 10 isoform 1"
                     /note="sperm-specific sodium proton exchanger;
                     sodium/hydrogen exchanger 10; solute carrier family 9,
                     member 10; solute carrier family 9, subfamily C
                     (Na+-transporting carboxylic acid decarboxylase), member
                     1"
                     /calculated_mol_wt=136095
     Region          37..556
                     /region_name="NhaP"
                     /note="NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion
                     transport and metabolism]; COG0025"
                     /db_xref="CDD:439796"
     Region          893..1020
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(974..975,984..986)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(1006..1008,1013..1015)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..1181
                     /gene="Slc9c1"
                     /gene_synonym="Gm610; Slc9a10"
                     /coded_by="NM_001437748.1:341..3886"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:288117"
                     /db_xref="RGD:1309075"
ORIGIN      
        1 meevfenltt thnvklsnaw ldllksvfls tpqdlpeiil ilslictiga flnmhlkdfp
       61 iplpvilfli gccfeilsfa stqiqlyada iqwmdpdmff giftpviifn vafdmdiyml
      121 qklfwqilli tipgfminyt lilwylqsvn klslktipwl lfsavlissd pmltsasird
      181 lglsrsltnl ingeslltsv isliiysavv qisfkskhmn htlahkvmst awsylvesfi
      241 tgilitkaiq lwmatifgdd vnhitlifsv lylifyvcel igmsgiftla tiglflnsts
      301 fkpgveafll efwnclsfig flmvftfigl lipahtylyi sfsdvyysln iyftlivlrl
      361 lvfllmspil srlghgfswr wafimvwsem kgtpninmal llaysdvslg serersqilf
      421 hgvsvcvitl ivnrfilpma viklglrdvt stkyksvyyt fqhfqeltks tamalkfdkd
      481 lanadwnmvd kaiilqnpya lnqeettehq kvkcpdcnke idetlnieam elanrrllsa
      541 qiasyqrqyr neilsqsamq vlvgaagsfg ekkgeymspe niknyseskk llsflrklll
      601 nwvyntkkdk gvpsrymflh achsivftne feytgyiavl mntypmiicw isrlkdiyqy
      661 eikcanyyfl tfyileallk vaamrkeffs htwllfelgi tlvgildiil ietdsisykf
      721 dltetvvfmn vvrllrilri lklitpkllq vidkrmsqqi sfryailkgy vqgemdvlni
      781 idqiasskqa kqillkrvir nmdhamkelg yleydhpeia vtmktkeevn vmlnmareiv
      841 kafrskgiih kvegaeinkl imakkkqvle lqsviqplnv eeapyyipwl sedpeaisfi
      901 qekakvvtfd cgnnifeegd epegiyviis gmvklkrskp hlemdrvsse sevaqtrsyt
      961 lphteyllsg eiigelnclt kermqysatc ktvvetyfip ishlyegfek kypnmkykmw
     1021 qkiglaitaq kirenlsfed wnykmqlklc nvfvrdipkt tktdiydetv thvvlihgsa
     1081 edcqlrkiyk apflipvtch qiqgleeftk vmiiqtsvav rkfrwnvkky npprrismkp
     1141 dstesletln esseddedkk eneeneeyle diidissvsk k
//
LOCUS       NP_001424633             479 aa            linear   ROD 11-APR-2025
DEFINITION  transcriptional regulator ERG isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424633 XP_006248204
VERSION     NP_001424633.1
DBSOURCE    REFSEQ: accession NM_001437704.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wu,L., Zhao,J.C., Kim,J., Jin,H.J., Wang,C.Y. and Yu,J.
  TITLE     ERG is a critical regulator of Wnt/LEF1 signaling in prostate
            cancer
  JOURNAL   Cancer Res 73 (19), 6068-6079 (2013)
   PUBMED   23913826
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Birger,Y., Goldberg,L., Chlon,T.M., Goldenson,B., Muler,I.,
            Schiby,G., Jacob-Hirsch,J., Rechavi,G., Crispino,J.D. and
            Izraeli,S.
  TITLE     Perturbation of fetal hematopoiesis in a mouse model of Down
            syndrome's transient myeloproliferative disorder
  JOURNAL   Blood 122 (6), 988-998 (2013)
   PUBMED   23719302
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Nhili,R., Peixoto,P., Depauw,S., Flajollet,S., Dezitter,X.,
            Munde,M.M., Ismail,M.A., Kumar,A., Farahat,A.A., Stephens,C.E.,
            Duterque-Coquillaud,M., David Wilson,W., Boykin,D.W. and
            David-Cordonnier,M.H.
  TITLE     Targeting the DNA-binding activity of the human ERG transcription
            factor using new heterocyclic dithiophene diamidines
  JOURNAL   Nucleic Acids Res 41 (1), 125-138 (2013)
   PUBMED   23093599
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Vijayaraj,P., Le Bras,A., Mitchell,N., Kondo,M., Juliao,S.,
            Wasserman,M., Beeler,D., Spokes,K., Aird,W.C., Baldwin,H.S. and
            Oettgen,P.
  TITLE     Erg is a crucial regulator of endocardial-mesenchymal
            transformation during cardiac valve morphogenesis
  JOURNAL   Development 139 (21), 3973-3985 (2012)
   PUBMED   22932696
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Yuan,L., Le Bras,A., Sacharidou,A., Itagaki,K., Zhan,Y., Kondo,M.,
            Carman,C.V., Davis,G.E., Aird,W.C. and Oettgen,P.
  TITLE     ETS-related gene (ERG) controls endothelial cell permeability via
            transcriptional regulation of the claudin 5 (CLDN5) gene
  JOURNAL   J Biol Chem 287 (9), 6582-6591 (2012)
   PUBMED   22235125
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Birdsey,G.M., Dryden,N.H., Amsellem,V., Gebhardt,F., Sahnan,K.,
            Haskard,D.O., Dejana,E., Mason,J.C. and Randi,A.M.
  TITLE     Transcription factor Erg regulates angiogenesis and endothelial
            apoptosis through VE-cadherin
  JOURNAL   Blood 111 (7), 3498-3506 (2008)
   PUBMED   18195090
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Jonson,L., Vikesaa,J., Krogh,A., Nielsen,L.K., Hansen,Tv.,
            Borup,R., Johnsen,A.H., Christiansen,J. and Nielsen,F.C.
  TITLE     Molecular composition of IMP1 ribonucleoprotein granules
  JOURNAL   Mol Cell Proteomics 6 (5), 798-811 (2007)
   PUBMED   17289661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248204.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.45363.1,
                                           SRR26643290.38967.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..479
                     /product="transcriptional regulator ERG isoform 2"
                     /note="v-ets erythroblastosis virus E26 oncogene like;
                     avian erythroblastosis virus E-26 (v-ets) oncogene
                     related; transcriptional regulator ERG; v-ets
                     erythroblastosis virus E26 oncogene homolog; v-ets avian
                     erythroblastosis virus E26 oncogene; ERG, ETS
                     transcription factor"
                     /calculated_mol_wt=53830
     Region          115..198
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          310..393
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..479
                     /gene="Erg"
                     /coded_by="NM_001437704.1:155..1594"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:170909"
                     /db_xref="RGD:621108"
ORIGIN      
        1 mastikeals vvsedqslfe caygtphlak temtassssd ygqtskmspr vpqqdwlsqp
       61 parvtikmec npsqvngsrn spdecsvtkg gkmvgspdtv gmsygsymee khmpppnmtt
      121 nerrvivpad ptlwstdhvr qwlewavkey glldvdvllf qnidgkelck mtkddfqrlt
      181 psynadills hlhylretpl phltsddvdk alqnsprlmh arntggaafi fpntsvypea
      241 tqrittrpdl pyepprrstw tghshptpqs kaaqpspstv pktedqrpql dpyqilgpts
      301 srlanpgsgq iqlwqfllel lsdssnsnci twegtngefk mtdpdevarr wgerkskpnm
      361 nydklsralr yyydknimtk vhgkryaykf dfhgiaqalq phppesslyk ypsdlpymgs
      421 yhthpqkmnf vaphppalpv tsssffatpn pywnsptggi ypntrlpash mpshlgtyy
//
LOCUS       NP_001102678             459 aa            linear   ROD 11-APR-2025
DEFINITION  BPI fold-containing family B member 3 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001102678 XP_001063849 XP_575268
VERSION     NP_001102678.1
DBSOURCE    REFSEQ: accession NM_001109208.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Andrault,J.B., Gaillard,I., Giorgi,D. and Rouquier,S.
  TITLE     Expansion of the BPI family by duplication on human chromosome 20:
            characterization of the RY gene cluster in 20q11.21 encoding
            olfactory transporters/antimicrobial-like peptides
  JOURNAL   Genomics 82 (2), 172-184 (2003)
   PUBMED   12837268
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Dear,T.N., Boehm,T., Keverne,E.B. and Rabbitts,T.H.
  TITLE     Novel genes for potential ligand-binding proteins in subregions of
            the olfactory mucosa
  JOURNAL   EMBO J 10 (10), 2813-2819 (1991)
   PUBMED   1915264
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH474050.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_575268.1, XP_001063849.1.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..459
                     /product="BPI fold-containing family B member 3 isoform 1
                     precursor"
                     /note="Potential ligand-binding protein RYA3; long palate,
                     lung and nasal epithelium carcinoma-associated protein 3;
                     Long palate, lung and nasal epithelium carcinoma
                     associated protein 3; antimicrobial peptide RYA3"
                     /calculated_mol_wt=46489
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2120
     Region          26..235
                     /region_name="BPI"
                     /note="BPI/LBP/CETP domain; Bactericidal
                     permeability-increasing protein (BPI) /
                     Lipopolysaccharide-binding protein (LBP) / Cholesteryl
                     ester transfer protein (CETP) domain; binds to and
                     neutralizes lipopolysaccharides from the outer membrane of
                     Gram-negative...; cl00188"
                     /db_xref="CDD:412206"
     Site            26..32
                     /site_type="other"
                     /note="BPI dimerizatation interface [polypeptide binding]"
                     /db_xref="CDD:238164"
     Site            order(31,36,39,43,46,107,130,132,142,185,189,193,226)
                     /site_type="active"
                     /note="apolar binding pocket [active]"
                     /db_xref="CDD:238164"
     Region          259..457
                     /region_name="BPI2"
                     /note="BPI/LBP/CETP C-terminal domain; smart00329"
                     /db_xref="CDD:128624"
     Site            order(265,270,273,277,280,339,372,374,383,419,423,427,453)
                     /site_type="active"
                     /note="apolar binding pocket [active]"
                     /db_xref="CDD:238164"
     CDS             1..459
                     /gene="Bpifb3"
                     /gene_synonym="Lplunc3; Rya3"
                     /coded_by="NM_001109208.1:141..1520"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:499924"
                     /db_xref="RGD:1565613"
ORIGIN      
        1 mmpgvyalll lwglatpclg lletvgtlar idkdelgkai qnslvggpil qnvlgtvtsv
       61 nqgllgaggl lggggllsyg glfslveels glkieeltlp tvsikllpgv gvqlslhtkl
      121 aaevnvsskv algmsprgtp ililkrcntl lghisltsgl lptpifglve qtlckvlpgl
      181 lcpvvdsvls vvnellgatl slvplgplgs veftlatlpl isnqyieldi npivksiagd
      241 vidfpkprlp vkmppkedht sqvtvplylf ntvfgllqtn galdlditpe mvprnipltt
      301 tdlaalapea lgklppgqhl llslrvmksp millqnkkvt vsipvtihvl ssvpqgtpva
      361 lfqmngvmtl nahlvpsttk lhislslerl tvqlassfsq pfdasrleew lsdvvraaym
      421 qklnehlevg iplpkilnvn fansvvdvie navvltvap
//
LOCUS       NP_001129373             197 aa            linear   ROD 11-APR-2025
DEFINITION  uncharacterized protein C20orf144 homolog isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001129373 XP_001062699 XP_575271
VERSION     NP_001129373.1
DBSOURCE    REFSEQ: accession NM_001135901.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Oct 21, 2008 this sequence version replaced
            XP_575271.2, XP_001062699.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ080432.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..197
                     /product="uncharacterized protein C20orf144 homolog
                     isoform 1"
                     /note="uncharacterized protein C20orf144 homolog"
                     /calculated_mol_wt=21833
     Region          1..189
                     /region_name="Bclt"
                     /note="Putative Bcl-2 like protein of testis; pfam15318"
                     /db_xref="CDD:434628"
     CDS             1..197
                     /gene="C3h20orf144"
                     /gene_synonym="RGD1561517"
                     /coded_by="NM_001135901.2:59..652"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:499927"
                     /db_xref="RGD:1561517"
ORIGIN      
        1 mgnsgshkrt kapnqaskdr ppdmdkarhk qffshlkrkk psvkapdpar vgenprikag
       61 ktkivllfpl dkrqqlaeaa agpfvrpvrp aedplgaptc fpatvapmlr gagdgvdrre
      121 gararemkri lvlllqldar lqeegrrvag rpgggakaqq ywqplyahll tqreacgegd
      181 preeqprkrr rcprprp
//
LOCUS       NP_001424645            3228 aa            linear   ROD 11-APR-2025
DEFINITION  golgin subfamily B member 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424645 XP_006248441
VERSION     NP_001424645.1
DBSOURCE    REFSEQ: accession NM_001437716.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3228)
  AUTHORS   Casey,C.A., Thomes,P., Manca,S. and Petrosyan,A.
  TITLE     Giantin Is Required for Post-Alcohol Recovery of Golgi in Liver
            Cells
  JOURNAL   Biomolecules 8 (4), 150 (2018)
   PUBMED   30453527
  REMARK    GeneRIF: Ethanol-induced Golgi disassembly was associated with
            de-dimerization of the largest Golgi matrix protein giantin, along
            with impaired transport of selected hepatic proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3228)
  AUTHORS   Katayama,K., Kuriki,M., Kamiya,T., Tochigi,Y. and Suzuki,H.
  TITLE     Giantin is required for coordinated production of aggrecan, link
            protein and type XI collagen during chondrogenesis
  JOURNAL   Biochem Biophys Res Commun 499 (3), 459-465 (2018)
   PUBMED   29577904
  REMARK    GeneRIF: giantin plays a pivotal role in coordinated production of
            aggrecan, link protein and type XI collagen in chondrocytes.
REFERENCE   3  (residues 1 to 3228)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   4  (residues 1 to 3228)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 3228)
  AUTHORS   Fusco,C., Micale,L., Egorov,M., Monti,M., D'Addetta,E.V.,
            Augello,B., Cozzolino,F., Calcagni,A., Fontana,A., Polishchuk,R.S.,
            Didelot,G., Reymond,A., Pucci,P. and Merla,G.
  TITLE     The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and
            promotes the sequestration and clearance of ubiquitinated proteins
            into the aggresome
  JOURNAL   PLoS One 7 (7), e40440 (2012)
   PUBMED   22792322
REFERENCE   6  (residues 1 to 3228)
  AUTHORS   Katayama,K., Sasaki,T., Goto,S., Ogasawara,K., Maru,H., Suzuki,K.
            and Suzuki,H.
  TITLE     Insertional mutation in the Golgb1 gene is associated with
            osteochondrodysplasia and systemic edema in the OCD rat
  JOURNAL   Bone 49 (5), 1027-1036 (2011)
   PUBMED   21851869
  REMARK    GeneRIF: concluded that mutation of the Golgb1 gene is responsible
            for the phenotypic characteristics including osteochondrodysplasia
            of ocd/ocd, and that giantin plays a pivotal role in multiple
            aspects of chondrogenesis
REFERENCE   7  (residues 1 to 3228)
  AUTHORS   Zhang,B., Zheng,C., Zhu,M., Tao,J., Vasievich,M.P., Baines,A.,
            Kim,J., Schekman,R., Kaufman,R.J. and Ginsburg,D.
  TITLE     Mice deficient in LMAN1 exhibit FV and FVIII deficiencies and liver
            accumulation of alpha1-antitrypsin
  JOURNAL   Blood 118 (12), 3384-3391 (2011)
   PUBMED   21795745
REFERENCE   8  (residues 1 to 3228)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 3228)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
REFERENCE   10 (residues 1 to 3228)
  AUTHORS   Diella,F., Levi,G. and Callahan,R.
  TITLE     Characterization of the INT6 mammary tumor gene product
  JOURNAL   DNA Cell Biol 16 (7), 839-847 (1997)
   PUBMED   9260927
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248441.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3228
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..3228
                     /product="golgin subfamily B member 1 isoform 2"
                     /note="Golgin subfamily B member 1; golgi autoantigen,
                     golgin subfamily b, macrogolgin 1; golgi-associated
                     protein GCP360; golgin B1, golgi integral membrane
                     protein"
                     /calculated_mol_wt=368948
     Region          63..>181
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          189..>947
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          720..1623
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1561..2033
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          1876..2632
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          2319..>3068
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..3228
                     /gene="Golgb1"
                     /coded_by="NM_001437716.1:275..9961"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:192243"
                     /db_xref="RGD:708429"
ORIGIN      
        1 mlsrlsglan nvlhelsgdy tgwttmtsse aelpqgsame lnnstqkdvl drladaeklv
       61 lelkdiiskq daqlqqkdea lqeekkgaes kikkiklhak akitslnkqi eelktqggaa
      121 sppevqaeel skhdksstee emevekikhe lqekeklisn lqaqldqaqs eqasqldkss
      181 aemedfvlmr qklqekeeli galqtqlsqt qaeqaaqlss mqqvvrekda rfetqvrlhe
      241 dellqlvtqs dvetevqqkl rvmqrkleeh eeallgraqv vdllqkelts aeqrnqdlsq
      301 qlqlleaehs tlrntmeaer qeskilmekv elemaerkee lyqlqgqler agqaqaelem
      361 qygtlqqrhe temeektaci sllqkneqel qsacdalkee nskllqeqqe qaaksaqalq
      421 qledelqqks keisqfvnkp nlekhetssq tslpdvyneg vqavmeesva slqkrvlele
      481 nekgalllss leleelraen eklcsritll eaqnragead gmvcevstag iallnrsdss
      541 teesgqdvle ntfsqkhkel svllvemkea qeeiaflksq lqgkrpegdy evldrkevqm
      601 meseglpsvt ardvlcaprd knsvpavege qagmrdqhgt leagplndtg melnspqpdg
      661 vdkslsaphv clchqgeler lktqvlelet slhtakethe knlsekakei ssltqltkef
      721 kesaeearst ltavceerdq llyrvkeldv lgelraqvre letslaeaek qrgldyesqr
      781 aqhnllteqi hslsieaksk dvkietlqre ldgvqlqfse qgtqirslqs qlqtkesevl
      841 egaermkdis kemeelsqal sqkeleiaqm dqlllekkkd vetlqqtiqe kdqqvtelsf
      901 smtekmvqln eekfslgvei ktlkeqlsll sraegakkeq vedsgaessp khgphessaq
      961 epvckdalqq elewlrkese qrkrklqaal isrkellqkv skleeelakv reestkdslr
     1021 esekreleed sknkddpeky gtsewrelev slrltiseke velegirrdl kekaaaeeel
     1081 qalvqrmtqd lqnktkqidl lqeeitenqa tiqkfitgtm dagdgdsavk etsvssppra
     1141 gggehwkpel egkivdleke ktqlqkklqe alisrkailk kaqekekhlk eelkeqkday
     1201 rhlqeqfdgq skeneniaar lrqlqakest dqqlpgtgqq epthgsegls legtepases
     1261 dlhaaqpshp getatlqatv svaqiqdqlk eievekeele lkissttsel tkkseevlll
     1321 qeqineqgle iqnlkaashe akahteqlkq elessqlkia dlehlktlqp eletlqkhvg
     1381 qkeeevsylv gqlgekeqtl ttvqtemeeq erlikalhtq lemqakehee rlkqvqveic
     1441 elkkqpkele eeskakqqlq rklqaalisr kealkenksl qeqlssarda vehltkslad
     1501 vesqvsvqnq ekdallgkla llqeerdkli vemdksllen qslggscesl klalgglted
     1561 keklmkeles vrcskiaest ewqekhkelq keyevllqsy envsneaeri qhvvesvrqe
     1621 kqevyaklrs aesdkrerek qlqdaeqeme emkekmrkfa kskqqkilel eeendrlrae
     1681 aqpvgganes meallssnas lkeeleritl eyktlskefe almaekntls eetrnlklqv
     1741 eaqelkqasl etteksdepk dvieevteav vgksqeqdsl senakledae atllansakp
     1801 gvsetfsshd dinnylqqld qlkgriaele mekqkdrels qtleneknal ltqisakdse
     1861 lklleeevak inmlnqqiqe elsrvtklke taeeekddle erlmnqlael ngsignyyqd
     1921 vtdaqikneq lesemqnlkr cvseleeekq qlvkektkve seirkeymek iqgaqkgpgs
     1981 kihakelqel lkekqqevkq lqkdcirylg risalektvk alefvhtesq kdldatkgnl
     2041 aqavehhkka qaelssfkil lddtqseaar vladnlklkk elqsnkesik sqikqkdedl
     2101 lrrleqaeek hrkekknmqe kldalhreka hvedtlaeiq vsltrkdkdm kelqqsldst
     2161 laqlaaftks msslqddrdr videakkweq rfgdaiqtke eevrlkeenc talkdqlrqm
     2221 tihmeelkit vsrlehdkei weskaqtelq hqqkaydklq eenkelmsql eeagqlyhds
     2281 kneltklese lkslkdqstd lknslekcre hennlegiik qqeadiqnck fnceqletdl
     2341 tasrelttrl hdeinvkeqk iisllsgkee aiqvaiaelh qqhskeikel enllsqeeee
     2401 nltleeenkr avektnqlte aletikkesl eqkaqldsfv ksmsslqddr drivsdyrql
     2461 eerhlsvile kdeliqdaaa ennklkeeir glrghmddln senakldael iqyrrdlnev
     2521 itikdsqqrq lleaqlqqnk elrnecvkle grlkgseaek qslqmsldal qeenqglske
     2581 iksfkeqlta lheegalavy haqlrvreee vqkltaalss sqkrtvdlqe elvcvqkeas
     2641 kkvseiedkl krelkhlhhn agimrnetet aeervaelar dlvemeqkll tvtkenkdlt
     2701 aqiqafgksm sslqdsrdha teelsdlkkk ydaslkelaq lkgrqdlgre sdvlsqaafp
     2761 lttsenissr leklnqqlts kdeqllhlss elesshnqvq sftkamtslq nerdhlwnel
     2821 ekfrkseegk qrsaapsaas spaevqslkk amsslqndrd rllkelknlq qqylqmnqei
     2881 telrplkaql qesqdqtkal qmmkeelrqe nlswqhelhq lrveknswel herrmkeqyl
     2941 maisdkdqql ghlqnllrel rsssqtqilp tqyqrqassg tsaaldgsqn lvyetdclrt
     3001 qlndslkeih qkelriqqln skfsqlleek nilstqlrda nqslrdsqhh ysnlfnhcai
     3061 lerqvqqlqa tgplnadvap gapqekdgih iktetettge eqpsfsevqq qlcntkhdls
     3121 elkklleeer dqrltaenal slakeqirrl ehsewesart piigacgsqe qvllmdlpgs
     3181 scrrtrssag wkrvlrslcr srtrvpllaa iyflmihvll vlcftghl
//
LOCUS       NP_001424691             598 aa            linear   ROD 11-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424691 XP_006248457
VERSION     NP_001424691.1
DBSOURCE    REFSEQ: accession NM_001437762.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248457.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO810735.1, SRR26360172.2291087.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..598
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 1"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=68499
     Region          239..>430
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          239..258
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          273..282
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          294..314
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          323..369
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..598
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437762.1:175..1971"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqravlkf lakcrkkkkl faswhglqel tdarrvelkq qvddyvkrhp gsqmsdvasr
      481 elhaqaqerl qhyfmgraie eraqqhreal maqistnieq lmkapslkea egkepeqfls
      541 rsrpvaakak qahlttlkhi qapwwkklge epgdemdvpk delsidlgtl figgtkpp
//
LOCUS       NP_001099523             274 aa            linear   ROD 11-APR-2025
DEFINITION  uncharacterized protein LOC290425 [Rattus norvegicus].
ACCESSION   NP_001099523 XP_001075379 XP_224432
VERSION     NP_001099523.1
DBSOURCE    REFSEQ: accession NM_001106053.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473951.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001075379.1, XP_224432.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC079439.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..274
                     /product="uncharacterized protein LOC290425"
                     /note="spermatid associated like"
                     /calculated_mol_wt=32094
     Region          <48..>251
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <156..>255
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
     CDS             1..274
                     /gene="Golga6l9"
                     /gene_synonym="RGD1306441; Spertl"
                     /coded_by="NM_001106053.1:172..996"
                     /db_xref="GeneID:290425"
                     /db_xref="RGD:1306441"
ORIGIN      
        1 mnisgskqih krkilrlfsc fsctqnqkkl khksqdvekk lcrenkvlrd enralrkdnk
       61 flwgenkalg renktfrmdn qfirernhil rqqnqllrkv krlisenpkl sgeecnalnt
      121 egrsfwqqnr ameaqitalr qqekafqnea kalheeiksl ceetkalqhq eralrmeeka
      181 llrdgvaael aealtkegaa lemeeqalwk eeqalreenk alreehgalq deevalqeea
      241 rilqewnnll qgkitnnlpe nmnnqdpekc elrm
//
LOCUS       NP_001424641             264 aa            linear   ROD 11-APR-2025
DEFINITION  COP9 signalosome complex subunit 7b [Rattus norvegicus].
ACCESSION   NP_001424641 XP_038939844
VERSION     NP_001424641.1
DBSOURCE    REFSEQ: accession NM_001437712.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Sharon,M., Mao,H., Boeri Erba,E., Stephens,E., Zheng,N. and
            Robinson,C.V.
  TITLE     Symmetrical modularity of the COP9 signalosome complex suggests its
            multifunctionality
  JOURNAL   Structure 17 (1), 31-40 (2009)
   PUBMED   19141280
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038939844.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.32256.1,
                                           SRR26643295.36203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..264
                     /product="COP9 signalosome complex subunit 7b"
                     /note="COP9 (constitutive photomorphogenic) homolog,
                     subunit 7b; COP9 constitutive photomorphogenic homolog
                     subunit 7B"
                     /calculated_mol_wt=29502
     Region          88..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     CDS             1..264
                     /gene="Cops7b"
                     /coded_by="NM_001437712.1:644..1438"
                     /db_xref="GeneID:363273"
                     /db_xref="RGD:1306918"
ORIGIN      
        1 mageqkpssn lleqfillak gtsgsalttl isqvleapgv yvfgellela nvqelaegan
       61 aaylqllnlf aygtypdyia nkeslpelsa aqqnklkhlt ivslasrmkc ipysvllkdl
      121 emrnlreled liieavytdi iqgkldqrnq llevdfcigr diqkkdinni vktlhewcdg
      181 ceavllgieq qvlranqyke nhhrtqqqve aevsnikktl katasssaqe meqqlaerec
      241 pphteqrqpt kkmskvkglv ssrh
//
LOCUS       NP_937843                124 aa            linear   ROD 11-APR-2025
DEFINITION  orexigenic neuropeptide QRFP precursor [Rattus norvegicus].
ACCESSION   NP_937843 XP_063140368
VERSION     NP_937843.1
DBSOURCE    REFSEQ: accession NM_198200.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Schreiber,A.L., Arceneaux,K.P. 3rd, Malbrue,R.A., Mouton,A.J.,
            Chen,C.S., Bench,E.M., Braymer,H.D. and Primeaux,S.D.
  TITLE     The effects of high fat diet and estradiol on hypothalamic
            prepro-QRFP mRNA expression in female rats
  JOURNAL   Neuropeptides 58, 103-109 (2016)
   PUBMED   26823127
  REMARK    GeneRIF: Studies support a role for estradiol (E2) in the
            regulation of prepro-QRFP mRNA in the ventral medial nucleus of the
            hypothalamus/arcuate nucleus and suggest that E2's effects on food
            intake may be via a direct effect on the orexigenic peptide, QRFP.
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Primeaux,S.D., Barnes,M.J. and Braymer,H.D.
  TITLE     Hypothalamic QRFP: regulation of food intake and fat selection
  JOURNAL   Horm Metab Res 45 (13), 967-974 (2013)
   PUBMED   23979792
  REMARK    GeneRIF: The present review discusses the role of QRFP in the
            regulation of feeding behavior, with emphasis on the intake of
            dietary fat.
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Primeaux,S.D.
  TITLE     QRFP in female rats: effects on high fat food intake and
            hypothalamic gene expression across the estrous cycle
  JOURNAL   Peptides 32 (6), 1270-1275 (2011)
   PUBMED   21473894
  REMARK    GeneRIF: QRFP may play a role in coordinating feeding behaviors
            with reproductive function in rats when energy demand is increased.
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Yamamoto,T., Miyazaki,R. and Yamada,T.
  TITLE     Intracerebroventricular administration of 26RFa produces an
            analgesic effect in the rat formalin test
  JOURNAL   Peptides 30 (9), 1683-1688 (2009)
   PUBMED   19520126
  REMARK    GeneRIF: Data suggest that the GPR103-26RFa system modulates
            nociceptive transmission in both the spinal cord and the
            supraspinal brain in the formalin (paw) test.
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Beck,B. and Richy,S.
  TITLE     Suppression of QRFP 43 in the hypothalamic ventromedial nucleus of
            Long-Evans rats fed a high-fat diet
  JOURNAL   Biochem Biophys Res Commun 383 (1), 78-82 (2009)
   PUBMED   19341706
  REMARK    GeneRIF: QRFP 43 might play a role downstream of leptin in the
            regulation of feeding behavior.
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Navarro,V.M., Fernandez-Fernandez,R., Nogueiras,R., Vigo,E.,
            Tovar,S., Chartrel,N., Le Marec,O., Leprince,J., Aguilar,E.,
            Pinilla,L., Dieguez,C., Vaudry,H. and Tena-Sempere,M.
  TITLE     Novel role of 26RFa, a hypothalamic RFamide orexigenic peptide, as
            putative regulator of the gonadotropic axis
  JOURNAL   J Physiol 573 (Pt 1), 237-249 (2006)
   PUBMED   16543265
  REMARK    GeneRIF: potential role of the orexigenic peptide 26RFa in the
            control of the gonadotropic axis, thus suggesting its potential
            involvement in the joint control of energy balance and
            reproduction, especially in the female
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Takayasu,S., Sakurai,T., Iwasaki,S., Teranishi,H., Yamanaka,A.,
            Williams,S.C., Iguchi,H., Kawasawa,Y.I., Ikeda,Y., Sakakibara,I.,
            Ohno,K., Ioka,R.X., Murakami,S., Dohmae,N., Xie,J., Suda,T.,
            Motoike,T., Ohuchi,T., Yanagisawa,M. and Sakai,J.
  TITLE     A neuropeptide ligand of the G protein-coupled receptor GPR103
            regulates feeding, behavioral arousal, and blood pressure in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (19), 7438-7443 (2006)
   PUBMED   16648250
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Chartrel,N., Bruzzone,F., Dujardin,C., Leprince,J., Tollemer,H.,
            Anouar,Y., Vallarino,M., Costentin,J. and Vaudry,H.
  TITLE     Identification of 26RFa from frog brain: a novel hypothalamic
            neuropeptide with orexigenic activity in mammals
  JOURNAL   Ann N Y Acad Sci 1040, 80-83 (2005)
   PUBMED   15891009
  REMARK    GeneRIF: Prepro-26RFa mRNA is expressed exclusively in two
            hypothalamic nuclei involved in the control of feeding behavior.
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Chartrel,N., Dujardin,C., Anouar,Y., Leprince,J., Decker,A.,
            Clerens,S., Do-Rego,J.C., Vandesande,F., Llorens-Cortes,C.,
            Costentin,J., Beauvillain,J.C. and Vaudry,H.
  TITLE     Identification of 26RFa, a hypothalamic neuropeptide of the RFamide
            peptide family with orexigenic activity
  JOURNAL   Proc Natl Acad Sci U S A 100 (25), 15247-15252 (2003)
   PUBMED   14657341
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Fukusumi,S., Yoshida,H., Fujii,R., Maruyama,M., Komatsu,H.,
            Habata,Y., Shintani,Y., Hinuma,S. and Fujino,M.
  TITLE     A new peptidic ligand and its receptor regulating adrenal function
            in rats
  JOURNAL   J Biol Chem 278 (47), 46387-46395 (2003)
   PUBMED   12960173
  REMARK    GeneRIF: QRFP mRNA was highly expressed in the hypothalamus; QRFP
            receptor mRNA was highly expressed in the adrenal gland. Data
            suggests that QRFP and its receptor have a regulatory function in
            the rat adrenal gland.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063140368.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1769568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680416, SAMN06680435
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..124
                     /product="orexigenic neuropeptide QRFP precursor"
                     /note="orexigenic neuropeptide QRFP; P518 precursor
                     protein"
                     /calculated_mol_wt=11745
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1925
     Region          16..124
                     /region_name="RFamide_26RFa"
                     /note="Orexigenic neuropeptide Qrfp/P518; pfam11109"
                     /db_xref="CDD:431659"
     Region          63..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P83860.1)"
     Site            80
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:16648250; propagated from
                     UniProtKB/Swiss-Prot (P83860.1)"
     Site            122
                     /site_type="amidation"
                     /note="Phenylalanine amide.
                     /evidence=ECO:0000269|PubMed:16648250; propagated from
                     UniProtKB/Swiss-Prot (P83860.1)"
     CDS             1..124
                     /gene="Qrfp"
                     /gene_synonym="26RFa; NEWGENE_735020; P518"
                     /coded_by="NM_198200.2:82..456"
                     /db_xref="GeneID:379044"
                     /db_xref="RGD:735020"
ORIGIN      
        1 mrclcswlcl llplsacfpl ldrrgptdig digarmswvq lteghtprsv qsprpqallv
       61 vakeqqasrr ehtgfrlgrq dsgseatgfl ptdsekasgp lgtlaeelss ysrrkggfsf
      121 rfgr
//
LOCUS       NP_001424647             697 aa            linear   ROD 11-APR-2025
DEFINITION  coiled-coil domain-containing protein 116 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424647 XP_017453390
VERSION     NP_001424647.1
DBSOURCE    REFSEQ: accession NM_001437718.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Wang,Y., Wu,W., Zhu,M., Wang,C., Shen,W., Cheng,Y., Geng,L., Li,Z.,
            Zhang,J., Dai,J., Ma,H., Chen,L., Hu,Z., Jin,G. and Shen,H.
  TITLE     Integrating expression-related SNPs into genome-wide gene- and
            pathway-based analyses identified novel lung cancer susceptibility
            genes
  JOURNAL   Int J Cancer 142 (8), 1602-1610 (2018)
   PUBMED   29193083
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Firat-Karalar,E.N., Sante,J., Elliott,S. and Stearns,T.
  TITLE     Proteomic analysis of mammalian sperm cells identifies new
            components of the centrosome
  JOURNAL   J Cell Sci 127 (Pt 19), 4128-4133 (2014)
   PUBMED   25074808
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_017453390.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.204626.1,
                                           SRR26643293.70232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..697
                     /product="coiled-coil domain-containing protein 116
                     isoform 1"
                     /note="coiled-coil domain-containing protein 116; stromal
                     cell-derived factor 2-like 1"
                     /calculated_mol_wt=78077
     Region          18..409
                     /region_name="DUF4702"
                     /note="Domain of unknown function (DUF4702); pfam15774"
                     /db_xref="CDD:464862"
     Region          347..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B5.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8B5.1)"
     CDS             1..697
                     /gene="Ccdc116"
                     /gene_synonym="Sdf2l1"
                     /coded_by="NM_001437718.1:132..2225"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:287936"
                     /db_xref="RGD:1310080"
ORIGIN      
        1 marcrhhsgy laddeaahgt yvarlpkkhl lpemrptckl grvphlpsmn ryserqghqq
       61 nlrrprafgg fldfltegqv ldslqtvveq atecvatmkt eagvplvdvq drvevpnsrh
      121 rsrgrpsint vhrhrarptl caghpnnyps csssmsdshs svtagwlgsr sqdsdlgarg
      181 vgslppmrdk llleknlkrl lrleskgkvl nqhcsqrdsl lwdslgsqss sqptreqpls
      241 wfsgllasts vtpetselgl geqemiflkq elnkeiksll nqptsfnlpt ycplrephrt
      301 ldflsehhlf palqrvvsqa vdklshacrh ngfplfpvts elspvfpgns dlqpsskasl
      361 ptdrearget cysptsassp ktshrkskdr rgspsnavqm atrfrlkspn kflkkkalps
      421 issvsslsyi snpwfeeltn flveqavsll ickykfeesl nkqlgfisfp itevlmdifl
      481 gfkkvkgthi rlssdinwtc llrkleeaem arqalrhvsr sgtsphstsr ivtshhstgp
      541 ssrqpeltrd tdqdqspesh lslhpalpir qvmgprdsri gqkqtantnq searrsvist
      601 agmgsktkev vnieegkdte eeeeeeeeed eeeedeeeed eeedeeedee eeeeeergse
      661 eeetkdfsec ehapspplhe lensvnetti vspgdsq
//
LOCUS       NP_001424643             982 aa            linear   ROD 11-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424643 XP_006248320
VERSION     NP_001424643.1
DBSOURCE    REFSEQ: accession NM_001437714.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Zhang,Z.Y., Bai,H.H., Guo,Z., Li,H.L., Diao,X.T., Zhang,T.Y.,
            Yao,L., Ma,J.J., Cao,Z., Li,Y.X., Bai,X., Chen,H.K., Suo,Z.W.,
            Yang,X. and Hu,X.D.
  TITLE     Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn
  JOURNAL   Sci Signal 13 (638) (2020)
   PUBMED   32606037
  REMARK    GeneRIF: Ubiquitination and functional modification of GluN2B
            subunit-containing NMDA receptors by Cbl-b in the spinal cord
            dorsal horn.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Jeong,J.S., Kim,H.Y., Shin,B.S., Lee,A.R., Yoon,J.H., Hahm,T.S. and
            Lee,J.E.
  TITLE     Increased expression of the Cbl family of E3 ubiquitin ligases
            decreases Interleukin-2 production in a rat model of peripheral
            neuropathy
  JOURNAL   BMC Anesthesiol 18 (1), 87 (2018)
   PUBMED   30021515
  REMARK    GeneRIF: results suggest that ubiquitin and the E3 ubiquitin
            ligases c-Cbl and Cbl-b function as neuroimmune modulators in the
            subacute phase of neuropathic pain after nerve injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Uchida,T., Sakashita,Y., Kitahata,K., Yamashita,Y., Tomida,C.,
            Kimori,Y., Komatsu,A., Hirasaka,K., Ohno,A., Nakao,R.,
            Higashitani,A., Higashibata,A., Ishioka,N., Shimazu,T.,
            Kobayashi,T., Okumura,Y., Choi,I., Oarada,M., Mills,E.M.,
            Teshima-Kondo,S., Takeda,S., Tanaka,E., Tanaka,K., Sokabe,M. and
            Nikawa,T.
  TITLE     Reactive oxygen species upregulate expression of muscle
            atrophy-associated ubiquitin ligase Cbl-b in rat L6 skeletal muscle
            cells
  JOURNAL   Am J Physiol Cell Physiol 314 (6), C721-C731 (2018)
   PUBMED   29513566
  REMARK    GeneRIF: Under microgravity conditions, elevated ROS may be a
            crucial mechanotransducer in skeletal muscle cells, regulating
            muscle mass through Cbl-b expression activated by the ERK-Egr
            signaling pathway.
REFERENCE   4  (residues 1 to 982)
  AUTHORS   Li,P., Liu,H.L., Zhang,Z.Q., Lv,X.D., Chang,Y.X., Wang,H.J., Ma,J.,
            Ma,Z.Y., Qu,X.J. and Teng,Y.E.
  TITLE     Single nucleotide polymorphisms of casitas B-lineage lymphoma
            proto-oncogene-b predict outcomes of patients with advanced
            non-small cell lung cancer after first-line platinum based doublet
            chemotherapy
  JOURNAL   J Thorac Dis 10 (3), 1635-1647 (2018)
   PUBMED   29707316
REFERENCE   5  (residues 1 to 982)
  AUTHORS   Li,P., Liu,H., Zhang,Z., Lv,X., Wang,H., Ma,J., Ma,Z., Qu,X. and
            Teng,Y.E.
  TITLE     Expression and Comparison of Cbl-b in Lung Squamous Cell Carcinoma
            and Adenocarcinoma
  JOURNAL   Med Sci Monit 24, 623-635 (2018)
   PUBMED   29384143
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 982)
  AUTHORS   Thirone,A.C., Carvalheira,J.B., Hirata,A.E., Velloso,L.A. and
            Saad,M.J.
  TITLE     Regulation of Cbl-associated protein/Cbl pathway in muscle and
            adipose tissues of two animal models of insulin resistance
  JOURNAL   Endocrinology 145 (1), 281-293 (2004)
   PUBMED   14525909
  REMARK    GeneRIF: CAP-Cbl pathway may have a role in the modulation of
            adiposity in fasting and in monosodium glutamate treated rats.
REFERENCE   7  (residues 1 to 982)
  AUTHORS   Zhang,W., Shao,Y., Fang,D., Huang,J., Jeon,M.S. and Liu,Y.C.
  TITLE     Negative regulation of T cell antigen receptor-mediated Crk-L-C3G
            signaling and cell adhesion by Cbl-b
  JOURNAL   J Biol Chem 278 (26), 23978-23983 (2003)
   PUBMED   12697763
REFERENCE   8  (residues 1 to 982)
  AUTHORS   Nishio,H., Otsuka,M., Kinoshita,S., Tokuoka,T., Nakajima,M.,
            Noda,Y., Fukuyama,Y. and Suzuki,K.
  TITLE     Phosphorylation of c-Cbl protooncogene product following ethanol
            administration in rat cerebellum: possible involvement of Fyn
            kinase
  JOURNAL   Brain Res 950 (1-2), 203-209 (2002)
   PUBMED   12231245
  REMARK    GeneRIF: c-Cbl protooncogene product is tyrosine- phosphorylated in
            rat cerebellum in response to ethanol administration.
REFERENCE   9  (residues 1 to 982)
  AUTHORS   Yokoi,N., Komeda,K., Wang,H.Y., Yano,H., Kitada,K., Saitoh,Y.,
            Seino,Y., Yasuda,K., Serikawa,T. and Seino,S.
  TITLE     Cblb is a major susceptibility gene for rat type 1 diabetes
            mellitus
  JOURNAL   Nat Genet 31 (4), 391-394 (2002)
   PUBMED   12118252
  REMARK    GeneRIF: we report the positional cloning of Iddm/kdp1 and identify
            a nonsense mutation in Cblb, a member of the Cbl/Sli family of
            ubiquitin-protein ligases.Cblb is a major susceptibility gene for
            rat type 1 diabetes mellitus
REFERENCE   10 (residues 1 to 982)
  AUTHORS   Krawczyk,C., Bachmaier,K., Sasaki,T., Jones,R.G., Snapper,S.B.,
            Bouchard,D., Kozieradzki,I., Ohashi,P.S., Alt,F.W. and
            Penninger,J.M.
  TITLE     Cbl-b is a negative regulator of receptor clustering and raft
            aggregation in T cells
  JOURNAL   Immunity 13 (4), 463-473 (2000)
   PUBMED   11070165
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248320.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.47883.1,
                                           SRR26643429.41005.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..982
                     /product="E3 ubiquitin-protein ligase CBL-B isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; SH3-binding
                     protein CBL-B; signal transduction protein CBL-B; casitas
                     B-lineage lymphoma proto-oncogene b; RING-type E3
                     ubiquitin transferase CBL-B; Casitas B-lineage lymphoma b;
                     Cas-Br-M (murine) ecotropic retroviral transforming
                     sequence b; Cbl proto-oncogene B, E3 ubiquitin protein
                     ligase; Cbl proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=109135
     Region          41..167
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          171..254
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          248..344
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(266,286,288..291,296,308,310)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(311..314,327..329)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          351..426
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(362..363,366,390,409..412)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(366..368,374..377,396,399..400,403,409..410,412)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          931..971
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(933..934,936..938,940..941,946,950)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..982
                     /gene="Cblb"
                     /coded_by="NM_001437714.1:163..3111"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171136"
                     /db_xref="RGD:620535"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr rnltklslif shmlaeikai fpngqfqgdn fritkadaae
      181 fwrkffgdkt ivpwkvfrqc lhevhqissg leamalksti dltcndyisv fefdiftrlf
      241 qpwgsilrnw nflavthpgy mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv
      301 tgdgnilqti phnkplfqal idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy
      361 elycemgstf qlckicaend kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep
      421 iivdpfdprd egsrccsiid pfsipmldld ddddreeslm mnrlasvrkc tdrqnspvts
      481 pgssplaqrr kpqpdplqip hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq
      541 dkplpapppp lrdppppper pppippdsrl srhfhhgegv psrdqpmple awcprdafgt
      601 nqvmgcrilg dgspkpgvta nsnlngrhsr mgsdqvlmrk hrrhdlpseg akvfsnghla
      661 peeydvpprl sppppvtall psikctgpia nclsektrdt veedddeyki psshpvslns
      721 qpshchnvkp pvrscdnghc ilngthgtps emkksnipdl giylkgdvsd sasdpvplpp
      781 arppprdnlk hgssvnrtps dydllipplg edafdalpps lpppppparh sliehskppg
      841 sssrpssgqd lfllpsdpff dpasgqvplp parrapgdgv ksnrasqdyd qlpsssdgsq
      901 aparppkprp rrtapeihhr kphgpeaale nvdakiaklm gegyafeevk raleiaqnnl
      961 evarsilref afpppvsprl nl
//
LOCUS       NP_001099828             476 aa            linear   ROD 11-APR-2025
DEFINITION  doublesex and mab-3 related transcription factor 3 [Rattus
            norvegicus].
ACCESSION   NP_001099828 XP_001078962 XP_219926
VERSION     NP_001099828.1
DBSOURCE    REFSEQ: accession NM_001106358.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Andersson,L.S., Larhammar,M., Memic,F., Wootz,H., Schwochow,D.,
            Rubin,C.J., Patra,K., Arnason,T., Wellbring,L., Hjalm,G.,
            Imsland,F., Petersen,J.L., McCue,M.E., Mickelson,J.R., Cothran,G.,
            Ahituv,N., Roepstorff,L., Mikko,S., Vallstedt,A., Lindgren,G.,
            Andersson,L. and Kullander,K.
  TITLE     Mutations in DMRT3 affect locomotion in horses and spinal circuit
            function in mice
  JOURNAL   Nature 488 (7413), 642-646 (2012)
   PUBMED   22932389
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Konno,D., Iwashita,M., Satoh,Y., Momiyama,A., Abe,T., Kiyonari,H.
            and Matsuzaki,F.
  TITLE     The mammalian DM domain transcription factor Dmrta2 is required for
            early embryonic development of the cerebral cortex
  JOURNAL   PLoS One 7 (10), e46577 (2012)
   PUBMED   23056351
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Ahituv,N., Zhu,Y., Visel,A., Holt,A., Afzal,V., Pennacchio,L.A. and
            Rubin,E.M.
  TITLE     Deletion of ultraconserved elements yields viable mice
  JOURNAL   PLoS Biol 5 (9), e234 (2007)
   PUBMED   17803355
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Murphy,M.W., Zarkower,D. and Bardwell,V.J.
  TITLE     Vertebrate DM domain proteins bind similar DNA sequences and can
            heterodimerize on DNA
  JOURNAL   BMC Mol Biol 8, 58 (2007)
   PUBMED   17605809
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473953.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_219926.4, XP_001078962.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..476
                     /product="doublesex and mab-3 related transcription factor
                     3"
                     /calculated_mol_wt=51313
     Region          25..71
                     /region_name="DM"
                     /note="DM DNA binding domain; pfam00751"
                     /db_xref="CDD:459924"
     Region          89..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     Region          147..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     Region          253..295
                     /region_name="CUE_DMA_DMRTA3"
                     /note="CUE-like DMA domain found in doublesex- and
                     mab-3-related transcription factor 3 (DMRTA3); cd14419"
                     /db_xref="CDD:270602"
     Region          418..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A218.1)"
     CDS             1..476
                     /gene="Dmrt3"
                     /coded_by="NM_001106358.1:253..1683"
                     /db_xref="GeneID:293976"
                     /db_xref="RGD:1306043"
ORIGIN      
        1 mngygspyly mggpvsqppr aplqrtpkca rcrnhgvlsw lkghkrycrf kdctcekcil
       61 iierqrvmaa qvalrrqqan esleslipds lralpgpppp gdaaataata sqsspasqas
      121 qppapprpat elaaaaalrw vaepqpgtlp aqiakpdlte drlgdsssad naaesfsdkd
      181 tdqrsspdvv kskncftpes peivsvdegg yavqknggnp escpdspkyh aeqshllieg
      241 psgtvslpfs lkanrpplev lkkifpnqkp tvlelilkgc ggdlvsavev llssrssaag
      301 aertaeeslv lpssghifeh tlgsypisss kwsvgsafrv pdtlrfsads snvvpnplav
      361 plqhpfpqpp ryplmlrntl arnqsspflp ndvtlwntmt lqqqyqlrsq yvspfpsnst
      421 svfrsspvls srttedpris ipddgcpiva kqsiyteddy dersdssdsr ilntss
//
LOCUS       NP_001291353             113 aa            linear   ROD 11-APR-2025
DEFINITION  sperm associated antigen 11b-like isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001291353 NP_001032939 XP_002728465 XP_008771553
VERSION     NP_001291353.2
DBSOURCE    REFSEQ: accession NM_001304424.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Ribeiro,C.M., Queiroz,D.B., Patrao,M.T., Denadai-Souza,A.,
            Romano,R.M., Silva,E.J. and Avellar,M.C.
  TITLE     Dynamic changes in the spatio-temporal expression of the
            beta-defensin SPAG11C in the developing rat epididymis and its
            regulation by androgens
  JOURNAL   Mol Cell Endocrinol 404, 141-150 (2015)
   PUBMED   25657045
  REMARK    GeneRIF: Results from the spatio-temporal expression, cellular
            distribution showed that SPAG11C may play a role in epididymal
            development and/or sperm function.
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Yenugu,S., Hamil,K.G., French,F.S. and Hall,S.H.
  TITLE     Antimicrobial actions of human and macaque sperm associated antigen
            (SPAG) 11 isoforms: influence of the N-terminal peptide
  JOURNAL   Mol Cell Biochem 284 (1-2), 25-37 (2006)
   PUBMED   16411022
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Patil,A.A., Cai,Y., Sang,Y., Blecha,F. and Zhang,G.
  TITLE     Cross-species analysis of the mammalian beta-defensin gene family:
            presence of syntenic gene clusters and preferential expression in
            the male reproductive tract
  JOURNAL   Physiol Genomics 23 (1), 5-17 (2005)
   PUBMED   16033865
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before May 2, 2024 this sequence version replaced
            NP_001032939.1, NP_001291353.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR23984936.1005444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..113
                     /product="sperm associated antigen 11b-like isoform 2
                     precursor"
                     /note="sperm associated antigen 11C-like; sperm associated
                     antigen 11b-like"
                     /calculated_mol_wt=9934
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2641
     Region          5..72
                     /region_name="Sperm_Ag_HE2"
                     /note="Sperm antigen HE2; pfam05324"
                     /db_xref="CDD:461622"
     CDS             1..113
                     /gene="Spag11b"
                     /gene_synonym="Spag11; Spag11bl; Spag11c"
                     /coded_by="NM_001304424.2:21..362"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:100362580"
                     /db_xref="RGD:1562239"
ORIGIN      
        1 mkrrllpsfv slllaalllp gsssassinh lvteppsspq defpaqggng sgllhhrvkr
       61 fpprtppyhe pgpnyqivnc kknegfcqky cnfmetqvgy cskkkeaccl hpf
//
LOCUS       NP_001424716             460 aa            linear   ROD 11-APR-2025
DEFINITION  rab-3A-interacting protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424716 XP_063119212
VERSION     NP_001424716.1
DBSOURCE    REFSEQ: accession NM_001437787.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vetter,M., Stehle,R., Basquin,C. and Lorentzen,E.
  TITLE     Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3
            and Rabin8 effectors to Rab11
  JOURNAL   Nat Struct Mol Biol 22 (9), 695-702 (2015)
   PUBMED   26258637
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Klip,A., Sun,Y., Chiu,T.T. and Foley,K.P.
  TITLE     Signal transduction meets vesicle traffic: the software and
            hardware of GLUT4 translocation
  JOURNAL   Am J Physiol Cell Physiol 306 (10), C879-C886 (2014)
   PUBMED   24598362
  REMARK    Review article
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Chiba,S., Amagai,Y., Homma,Y., Fukuda,M. and Mizuno,K.
  TITLE     NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by
            switching binding specificity from phosphatidylserine to Sec15
  JOURNAL   EMBO J 32 (6), 874-885 (2013)
   PUBMED   23435566
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Blumer,J., Rey,J., Dehmelt,L., Mazel,T., Wu,Y.W., Bastiaens,P.,
            Goody,R.S. and Itzen,A.
  TITLE     RabGEFs are a major determinant for specific Rab membrane targeting
  JOURNAL   J Cell Biol 200 (3), 287-300 (2013)
   PUBMED   23382462
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Ultanir,S.K., Hertz,N.T., Li,G., Ge,W.P., Burlingame,A.L.,
            Pleasure,S.J., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Chemical genetic identification of NDR1/2 kinase substrates AAK1
            and Rabin8 Uncovers their roles in dendrite arborization and spine
            development
  JOURNAL   Neuron 73 (6), 1127-1142 (2012)
   PUBMED   22445341
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Hattula,K., Furuhjelm,J., Arffman,A. and Peranen,J.
  TITLE     A Rab8-specific GDP/GTP exchange factor is involved in actin
            remodeling and polarized membrane transport
  JOURNAL   Mol Biol Cell 13 (9), 3268-3280 (2002)
   PUBMED   12221131
REFERENCE   7  (residues 1 to 460)
  AUTHORS   de Bruijn,D.R., dos Santos,N.R., Kater-Baats,E., Thijssen,J., van
            den Berk,L., Stap,J., Balemans,M., Schepens,M., Merkx,G. and van
            Kessel,A.G.
  TITLE     The cancer-related protein SSX2 interacts with the human homologue
            of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear
            protein, SSX2IP
  JOURNAL   Genes Chromosomes Cancer 34 (3), 285-298 (2002)
   PUBMED   12007189
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Page,G., Kogel,D., Rangnekar,V. and Scheidtmann,K.H.
  TITLE     Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP
            kinase and Par-4 results in cytoplasmic retention and apoptosis
  JOURNAL   Oncogene 18 (51), 7265-7273 (1999)
   PUBMED   10602480
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Page,G., Lodige,I., Kogel,D. and Scheidtmann,K.H.
  TITLE     AATF, a novel transcription factor that interacts with Dlk/ZIP
            kinase and interferes with apoptosis
  JOURNAL   FEBS Lett 462 (1-2), 187-191 (1999)
   PUBMED   10580117
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Brondyk,W.H., McKiernan,C.J., Fortner,K.A., Stabila,P., Holz,R.W.
            and Macara,I.G.
  TITLE     Interaction cloning of Rabin3, a novel protein that associates with
            the Ras-like GTPase Rab3A
  JOURNAL   Mol Cell Biol 15 (3), 1137-1143 (1995)
   PUBMED   7532276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 9, 2025 this sequence version replaced XP_063119212.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.9967.1,
                                           SRR26643292.29344.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..460
                     /product="rab-3A-interacting protein isoform 1"
                     /note="rab-3A-interacting protein; rabin-3;
                     SSX2-interacting protein; rab3A-interacting protein"
                     /calculated_mol_wt=50901
     Region          97..>240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          173..241
                     /region_name="Sec2p"
                     /note="GDP/GTP exchange factor Sec2p; pfam06428"
                     /db_xref="CDD:428938"
     Region          246..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62739.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          266..458
                     /region_name="Rab11BD_RAB3IP"
                     /note="Rab11 binding domain of Rab-3A-interacting protein
                     (RAB3IP); cd21068"
                     /db_xref="CDD:411032"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            order(351..357,412,415..416,419,423,428..432)
                     /site_type="other"
                     /note="Rab11 binding site [polypeptide binding]"
                     /db_xref="CDD:411032"
     CDS             1..460
                     /gene="Rab3ip"
                     /gene_synonym="RABIN3"
                     /coded_by="NM_001437787.1:179..1561"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:29885"
                     /db_xref="RGD:620650"
ORIGIN      
        1 mandplegfh evnlasptsp dllgvcdpgt qeqttspsvi yrphpstlcs atiqanalnl
       61 sdlptqpvys sprhlncaei snisihvpep assvasevaa gltrftsrkd scnaereflq
      121 gatvteasag nddifglstd slsrlrspsv levrekgyer lkeelakaqr elklkdeece
      181 rlskvrdqlg qeleeltasl feeahkmvre anvkqataek qlkeaqgkid vlqaevaalk
      241 tlvlssspts ptqeplaagk tpfkrghtrn kstssamsgs hqdfsaiqpi vkdcreadls
      301 lynefrswkd eptmdrtcpf ldkiyqedif pcltfaksel asavleaven ntlsiepvgl
      361 qpirfvkasa vecggpkkca ltgqskpckh riklgdsssy yyispvcryr itsvcnffty
      421 iryiqqglvk qqdvdqmfwe vmqlrkemsl aklgyfkeel
//
LOCUS       NP_001424662             153 aa            linear   ROD 11-APR-2025
DEFINITION  transmembrane inner ear expressed protein [Rattus norvegicus].
ACCESSION   NP_001424662 XP_006244058
VERSION     NP_001424662.1
DBSOURCE    REFSEQ: accession NM_001437733.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Shin,M.J., Lee,J.H., Yu,D.H., Kim,H.J., Bae,K.B., Yuh,H.S.,
            Kim,M.O., Hyun,B.H., Lee,S., Park,R. and Ryoo,Z.Y.
  TITLE     Spatiotemporal expression of tmie in the inner ear of rats during
            postnatal development
  JOURNAL   Comp Med 60 (4), 288-294 (2010)
   PUBMED   20819378
  REMARK    GeneRIF: Tmie exists in the cytoplasm and may have a key role in
            the maturation and structure of stereocilia bundles in developing
            hair cells. After hair cell maturation, Tmie is thought to be
            involved in the maintenance of organ of Corti cells.
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Su,M.C., Yang,J.J., Chou,M.Y., Hsin,C.H., Su,C.C. and Li,S.Y.
  TITLE     Expression and localization of Tmie in adult rat cochlea
  JOURNAL   Histochem Cell Biol 130 (1), 119-126 (2008)
   PUBMED   18327602
  REMARK    GeneRIF: Our results point out the presence and localization of
            Tmie products in the cochlea of rat.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Naz,S., Giguere,C.M., Kohrman,D.C., Mitchem,K.L., Riazuddin,S.,
            Morell,R.J., Ramesh,A., Srisailpathy,S., Deshmukh,D., Riazuddin,S.,
            Griffith,A.J., Friedman,T.B., Smith,R.J. and Wilcox,E.R.
  TITLE     Mutations in a novel gene, TMIE, are associated with hearing loss
            linked to the DFNB6 locus
  JOURNAL   Am J Hum Genet 71 (3), 632-636 (2002)
   PUBMED   12145746
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Mitchem,K.L., Hibbard,E., Beyer,L.A., Bosom,K., Dootz,G.A.,
            Dolan,D.F., Johnson,K.R., Raphael,Y. and Kohrman,D.C.
  TITLE     Mutation of the novel gene Tmie results in sensory cell defects in
            the inner ear of spinner, a mouse model of human hearing loss DFNB6
  JOURNAL   Hum Mol Genet 11 (16), 1887-1898 (2002)
   PUBMED   12140191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006244058.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.11848.1,
                                           SRR26643298.46929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..153
                     /product="transmembrane inner ear expressed protein"
                     /calculated_mol_wt=16901
     Region          47..132
                     /region_name="TMIE"
                     /note="TMIE protein; pfam16038"
                     /db_xref="CDD:464987"
     CDS             1..153
                     /gene="Tmie"
                     /gene_synonym="RGD1562523"
                     /coded_by="NM_001437733.1:234..695"
                     /db_xref="GeneID:501061"
                     /db_xref="RGD:1562523"
ORIGIN      
        1 magrqrgsgr lwalggaalg aclagvasql vepstappkp kpppltketv vfwdmrlwhv
       61 vgifslfvls iiitlccvfn crvprtrkei earylqrkaa kmytdkletv pplnelteip
      121 gedkkkkkkd svdtvaikve edekneakkk gek
//
LOCUS       NP_001424715             460 aa            linear   ROD 11-APR-2025
DEFINITION  rab-3A-interacting protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424715 XP_006241422
VERSION     NP_001424715.1
DBSOURCE    REFSEQ: accession NM_001437786.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vetter,M., Stehle,R., Basquin,C. and Lorentzen,E.
  TITLE     Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3
            and Rabin8 effectors to Rab11
  JOURNAL   Nat Struct Mol Biol 22 (9), 695-702 (2015)
   PUBMED   26258637
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Klip,A., Sun,Y., Chiu,T.T. and Foley,K.P.
  TITLE     Signal transduction meets vesicle traffic: the software and
            hardware of GLUT4 translocation
  JOURNAL   Am J Physiol Cell Physiol 306 (10), C879-C886 (2014)
   PUBMED   24598362
  REMARK    Review article
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Chiba,S., Amagai,Y., Homma,Y., Fukuda,M. and Mizuno,K.
  TITLE     NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by
            switching binding specificity from phosphatidylserine to Sec15
  JOURNAL   EMBO J 32 (6), 874-885 (2013)
   PUBMED   23435566
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Blumer,J., Rey,J., Dehmelt,L., Mazel,T., Wu,Y.W., Bastiaens,P.,
            Goody,R.S. and Itzen,A.
  TITLE     RabGEFs are a major determinant for specific Rab membrane targeting
  JOURNAL   J Cell Biol 200 (3), 287-300 (2013)
   PUBMED   23382462
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Ultanir,S.K., Hertz,N.T., Li,G., Ge,W.P., Burlingame,A.L.,
            Pleasure,S.J., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Chemical genetic identification of NDR1/2 kinase substrates AAK1
            and Rabin8 Uncovers their roles in dendrite arborization and spine
            development
  JOURNAL   Neuron 73 (6), 1127-1142 (2012)
   PUBMED   22445341
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Hattula,K., Furuhjelm,J., Arffman,A. and Peranen,J.
  TITLE     A Rab8-specific GDP/GTP exchange factor is involved in actin
            remodeling and polarized membrane transport
  JOURNAL   Mol Biol Cell 13 (9), 3268-3280 (2002)
   PUBMED   12221131
REFERENCE   7  (residues 1 to 460)
  AUTHORS   de Bruijn,D.R., dos Santos,N.R., Kater-Baats,E., Thijssen,J., van
            den Berk,L., Stap,J., Balemans,M., Schepens,M., Merkx,G. and van
            Kessel,A.G.
  TITLE     The cancer-related protein SSX2 interacts with the human homologue
            of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear
            protein, SSX2IP
  JOURNAL   Genes Chromosomes Cancer 34 (3), 285-298 (2002)
   PUBMED   12007189
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Page,G., Kogel,D., Rangnekar,V. and Scheidtmann,K.H.
  TITLE     Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP
            kinase and Par-4 results in cytoplasmic retention and apoptosis
  JOURNAL   Oncogene 18 (51), 7265-7273 (1999)
   PUBMED   10602480
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Page,G., Lodige,I., Kogel,D. and Scheidtmann,K.H.
  TITLE     AATF, a novel transcription factor that interacts with Dlk/ZIP
            kinase and interferes with apoptosis
  JOURNAL   FEBS Lett 462 (1-2), 187-191 (1999)
   PUBMED   10580117
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Brondyk,W.H., McKiernan,C.J., Fortner,K.A., Stabila,P., Holz,R.W.
            and Macara,I.G.
  TITLE     Interaction cloning of Rabin3, a novel protein that associates with
            the Ras-like GTPase Rab3A
  JOURNAL   Mol Cell Biol 15 (3), 1137-1143 (1995)
   PUBMED   7532276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006241422.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.30691.1,
                                           SRR26643291.20287.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..460
                     /product="rab-3A-interacting protein isoform 1"
                     /note="rab-3A-interacting protein; rabin-3;
                     SSX2-interacting protein; rab3A-interacting protein"
                     /calculated_mol_wt=50901
     Region          97..>240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          173..241
                     /region_name="Sec2p"
                     /note="GDP/GTP exchange factor Sec2p; pfam06428"
                     /db_xref="CDD:428938"
     Region          246..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62739.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          266..458
                     /region_name="Rab11BD_RAB3IP"
                     /note="Rab11 binding domain of Rab-3A-interacting protein
                     (RAB3IP); cd21068"
                     /db_xref="CDD:411032"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            order(351..357,412,415..416,419,423,428..432)
                     /site_type="other"
                     /note="Rab11 binding site [polypeptide binding]"
                     /db_xref="CDD:411032"
     CDS             1..460
                     /gene="Rab3ip"
                     /gene_synonym="RABIN3"
                     /coded_by="NM_001437786.1:189..1571"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:29885"
                     /db_xref="RGD:620650"
ORIGIN      
        1 mandplegfh evnlasptsp dllgvcdpgt qeqttspsvi yrphpstlcs atiqanalnl
       61 sdlptqpvys sprhlncaei snisihvpep assvasevaa gltrftsrkd scnaereflq
      121 gatvteasag nddifglstd slsrlrspsv levrekgyer lkeelakaqr elklkdeece
      181 rlskvrdqlg qeleeltasl feeahkmvre anvkqataek qlkeaqgkid vlqaevaalk
      241 tlvlssspts ptqeplaagk tpfkrghtrn kstssamsgs hqdfsaiqpi vkdcreadls
      301 lynefrswkd eptmdrtcpf ldkiyqedif pcltfaksel asavleaven ntlsiepvgl
      361 qpirfvkasa vecggpkkca ltgqskpckh riklgdsssy yyispvcryr itsvcnffty
      421 iryiqqglvk qqdvdqmfwe vmqlrkemsl aklgyfkeel
//
LOCUS       NP_001424649             171 aa            linear   ROD 11-APR-2025
DEFINITION  synaptonemal complex central element protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424649 XP_006255353
VERSION     NP_001424649.1
DBSOURCE    REFSEQ: accession NM_001437720.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Jordan,P.W., Karppinen,J. and Handel,M.A.
  TITLE     Polo-like kinase is required for synaptonemal complex disassembly
            and phosphorylation in mouse spermatocytes
  JOURNAL   J Cell Sci 125 (Pt 21), 5061-5072 (2012)
   PUBMED   22854038
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Modzelewski,A.J., Holmes,R.J., Hilz,S., Grimson,A. and Cohen,P.E.
  TITLE     AGO4 regulates entry into meiosis and influences silencing of sex
            chromosomes in the male mouse germline
  JOURNAL   Dev Cell 23 (2), 251-264 (2012)
   PUBMED   22863743
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Costa,Y., Speed,R., Ollinger,R., Alsheimer,M., Semple,C.A.,
            Gautier,P., Maratou,K., Novak,I., Hoog,C., Benavente,R. and
            Cooke,H.J.
  TITLE     Two novel proteins recruited by synaptonemal complex protein 1
            (SYCP1) are at the centre of meiosis
  JOURNAL   J Cell Sci 118 (Pt 12), 2755-2762 (2005)
   PUBMED   15944401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006255353.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.972263.1,
                                           SRR26360186.875040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..171
                     /product="synaptonemal complex central element protein 2
                     isoform 2"
                     /calculated_mol_wt=19464
     CDS             1..171
                     /gene="Syce2"
                     /gene_synonym="RGD1311867"
                     /coded_by="NM_001437720.1:43..558"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:364976"
                     /db_xref="RGD:1311867"
ORIGIN      
        1 merqgvavpp velkdqeppa ivesgehqqn enheetpssv apsascqlpg pfssldssie
       61 tlkkkaqeli eninesrqkd halmtnfrds lkmkvsdlte kleermyqvy shhskiiqer
      121 lqeftqkmak ishlemelkq vcqtvetmyk dlcvqsevpt seeqnykdge c
//
LOCUS       NP_775164                230 aa            linear   ROD 12-APR-2025
DEFINITION  tissue factor pathway inhibitor 2 precursor [Rattus norvegicus].
ACCESSION   NP_775164 XP_346687 XP_347367
VERSION     NP_775164.2
DBSOURCE    REFSEQ: accession NM_173141.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Xu,Z., Zhu,X., Mu,S., Fan,R., Wang,B., Gao,W. and Kang,T.
  TITLE     FTO overexpression expedites wound healing and alleviates
            depression in burn rats through facilitating keratinocyte migration
            and angiogenesis via mediating TFPI-2 demethylation
  JOURNAL   Mol Cell Biochem 479 (2), 325-335 (2024)
   PUBMED   37074506
  REMARK    GeneRIF: FTO overexpression expedites wound healing and alleviates
            depression in burn rats through facilitating keratinocyte migration
            and angiogenesis via mediating TFPI-2 demethylation.
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Jang,Y.J., Kim,H.K., Choi,B.C., Song,S.J., Park,J.I., Chun,S.Y. and
            Cho,M.K.
  TITLE     Expression of tissue factor and tissue factor pathway inhibitors
            during ovulation in rats: a relevance to the ovarian
            hyperstimulation syndrome
  JOURNAL   Reprod Biol Endocrinol 19 (1), 52 (2021)
   PUBMED   33794911
  REMARK    GeneRIF: Expression of tissue factor and tissue factor pathway
            inhibitors during ovulation in rats: a relevance to the ovarian
            hyperstimulation syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Liu,Z., Zhang,J., Gao,Y., Pei,L., Zhou,J., Gu,L., Zhang,L., Zhu,B.,
            Hattori,N., Ji,J., Yuasa,Y., Kim,W., Ushijima,T., Shi,H. and
            Deng,D.
  TITLE     Large-scale characterization of DNA methylation changes in human
            gastric carcinomas with and without metastasis
  JOURNAL   Clin Cancer Res 20 (17), 4598-4612 (2014)
   PUBMED   25009298
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Jian,P., Yan,W.S., Chao,S.L., Liang,P., Zhen,L., Ling,Q.B.,
            Hong,L.Y., Ping,L.Y., Jian,W., Fang,J.M., Ling,L., Dong,W.X.,
            Ming,Z.X. and Jian,N.
  TITLE     Promoter of TFPI-2 is hypermethylated in Chinese pediatric acute
            myeloid leukemia
  JOURNAL   J Pediatr Hematol Oncol 34 (1), 43-46 (2012)
   PUBMED   22052167
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Ekstrand,J., Razuvaev,A., Folkersen,L., Roy,J. and Hedin,U.
  TITLE     Tissue factor pathway inhibitor-2 is induced by fluid shear stress
            in vascular smooth muscle cells and affects cell proliferation and
            survival
  JOURNAL   J Vasc Surg 52 (1), 167-175 (2010)
   PUBMED   20537494
  REMARK    GeneRIF: TFPI-2 influences smooth muscle cell proliferation and
            apoptosis in vitro in response to fluid shear stress.
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Obata,R., Yanagi,Y., Tamaki,Y., Hozumi,K., Mutoh,M. and Tanaka,Y.
  TITLE     Retinal degeneration is delayed by tissue factor pathway
            inhibitor-2 in RCS rats and a sodium-iodate-induced model in
            rabbits
  JOURNAL   Eye (Lond) 19 (4), 464-468 (2005)
   PUBMED   15184935
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Hisaka,T., Kisiel,W. and Rosenbaum,J.
  TITLE     cDNA cloning and tissue distribution of the rat ortholog of tissue
            factor pathway inhibitor-2
  JOURNAL   Thromb Haemost 88 (2), 356-357 (2002)
   PUBMED   12195712
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Miyagi,Y., Yasumitsu,H., Mizushima,H., Koshikawa,N., Matsuda,Y.,
            Itoh,H., Hori,T.A., Aoki,I., Misugi,K. and Miyazaki,K.
  TITLE     Cloning of the cDNA encoding mouse PP5/TFPI-2 and mapping of the
            gene to chromosome 6
  JOURNAL   DNA Cell Biol 15 (11), 947-954 (1996)
   PUBMED   8945635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Nov 27, 2020 this sequence version replaced NP_775164.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ428954.1, SRR26643285.15233.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q13"
     Protein         1..230
                     /product="tissue factor pathway inhibitor 2 precursor"
                     /calculated_mol_wt=23279
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2866
     Region          32..87
                     /region_name="Kunitz-type"
                     /note="Kunitz/Bovine pancreatic trypsin inhibitor (BPTI)
                     domain; cl00101"
                     /db_xref="CDD:444694"
     Site            order(42..46,48..50,65,69)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438633"
     Region          93..146
                     /region_name="Kunitz-type"
                     /note="Kunitz/Bovine pancreatic trypsin inhibitor (BPTI)
                     domain; cl00101"
                     /db_xref="CDD:444694"
     Site            order(102..106,108..110,125,129)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438633"
     Region          153..206
                     /region_name="Kunitz_TFPI1_TFPI2_3-like"
                     /note="Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or
                     K3) of tissue factor pathway inhibitor (TFPI) and TFPI2,
                     and similar proteins; cd22615"
                     /db_xref="CDD:438658"
     CDS             1..230
                     /gene="Tfpi2"
                     /coded_by="NM_173141.2:53..745"
                     /db_xref="GeneID:286926"
                     /db_xref="RGD:628629"
ORIGIN      
        1 mdpatslrlw nlplllvgsa lglasvsaqg nnleicllpl dmgpckalip kfyydrdqkk
       61 crrfkyggcl gnannfhsrk lcehtcgnke kvpwvcrsav rtypcdkpnt efffnlktmt
      121 ceplrpglcs rttnvfpeea mckslceprk sipsfcsspk deglcsanvt ryyfnsrnka
      181 cetftytgcg gnennfyyld acnracvkal kkpkrrkigd flprfwklrs
//
LOCUS       NP_001424748             450 aa            linear   ROD 13-APR-2025
DEFINITION  sulfide:quinone oxidoreductase, mitochondrial isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424748 XP_006234949
VERSION     NP_001424748.1
DBSOURCE    REFSEQ: accession NM_001437819.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Augustyn,K.D., Jackson,M.R. and Jorns,M.S.
  TITLE     Use of Tissue Metabolite Analysis and Enzyme Kinetics To
            Discriminate between Alternate Pathways for Hydrogen Sulfide
            Metabolism
  JOURNAL   Biochemistry 56 (7), 986-996 (2017)
   PUBMED   28107627
  REMARK    GeneRIF: The role of Sqor in hydrogen sulfide metabolism in the
            heart and liver
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Ackermann,M., Kubitza,M., Hauska,G. and Pina,A.L.
  TITLE     The vertebrate homologue of sulfide-quinone reductase in mammalian
            mitochondria
  JOURNAL   Cell Tissue Res 358 (3), 779-792 (2014)
   PUBMED   25130143
  REMARK    GeneRIF: The present report demonstrates the presence and specific
            localization of SQRDL in various mammalian tissues.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Jackson,M.R., Melideo,S.L. and Jorns,M.S.
  TITLE     Human sulfide:quinone oxidoreductase catalyzes the first step in
            hydrogen sulfide metabolism and produces a sulfane sulfur
            metabolite
  JOURNAL   Biochemistry 51 (34), 6804-6815 (2012)
   PUBMED   22852582
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Ackermann,M., Kubitza,M., Maier,K., Brawanski,A., Hauska,G. and
            Pina,A.L.
  TITLE     The vertebrate homolog of sulfide-quinone reductase is expressed in
            mitochondria of neuronal tissues
  JOURNAL   Neuroscience 199, 1-12 (2011)
   PUBMED   22067608
  REMARK    GeneRIF: we demonstrated that the SQRDL protein is expressed in
            neurons, oligodendrocytes, and endothelial cells
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006234949.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.15126.1,
                                           SRR26643290.12952.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..450
                     /product="sulfide:quinone oxidoreductase, mitochondrial
                     isoform 1"
                     /EC_number="1.8.5.8"
                     /note="sulfide:quinone oxidoreductase, mitochondrial"
                     /calculated_mol_wt=50071
     Region          71..389
                     /region_name="FadH2"
                     /note="NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur
                     reductase, or a related oxidoreductase [Lipid transport
                     and metabolism]; COG0446"
                     /db_xref="CDD:440215"
     CDS             1..450
                     /gene="Sqor"
                     /gene_synonym="Cc2-17; Sqrdl"
                     /coded_by="NM_001437819.1:69..1421"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:691966"
                     /db_xref="RGD:1564504"
ORIGIN      
        1 maplvavvss prarlfacfl rlgtqqagpl qlhtgaccta knhyevlvlg ggsggitmat
       61 rmkrrvgaen vaivepserh fyqpiwtlvg agakelsssd rstlsvipsg vqwiqdrvae
      121 lnpdqncirt dngkeisyry liialgiqld yekikglpeg faypkigsny svktvektwk
      181 alqdfkegna lftfpntpvk cagapqkimy lseayfrktg krskaniifn talgtifgvk
      241 kyadalqeii rernvsvnyk hnlievradk qeavfenldk pgethvihye mlhvtppmss
      301 pdvlkrspva dsagwvdvdk etlqhkkypn vfgigdctnl ptsktaaava aqsgildrti
      361 slimknqtpt kkydgytscp lvtgynrvil aefdytaqpl etfpfdqske rismylmkad
      421 mmpflywnmm lrgywggpaf lrklfhlgls
//
LOCUS       NP_001424814             366 aa            linear   ROD 13-APR-2025
DEFINITION  protein FAM110B [Rattus norvegicus].
ACCESSION   NP_001424814 XP_006237902
VERSION     NP_001424814.1
DBSOURCE    REFSEQ: accession NM_001437885.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006237902.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.52945.1,
                                           SRR26360194.1719172.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..366
                     /product="protein FAM110B"
                     /calculated_mol_wt=40232
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          163..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          214..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          249..357
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC76; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX5.1)"
     Region          313..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJX5.1)"
     CDS             1..366
                     /gene="Fam110b"
                     /coded_by="NM_001437885.1:455..1555"
                     /db_xref="GeneID:500400"
                     /db_xref="RGD:1563403"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpgak rvlgsptlkv fgnhaktesg vqretlklei
      121 lkniinsseg sssgsghkhs srnwpphrdt telhrhsfae slkvyptpgr gspqessshv
      181 srrlleqsae sflhvshsss dirkvtsvkp lkaipcsssa pplppkpkva amkspdadqv
      241 epacgvsrrp slqrsksdls dryfrvdadv erffnycgld peelenlgme nfaransdii
      301 slnfrsasmi ssdceqsqds nsdlrnddsa ndrvpygisa iernariikw lysikqares
      361 qkvshv
//
LOCUS       NP_001424810             332 aa            linear   ROD 13-APR-2025
DEFINITION  PRKC apoptosis WT1 regulator protein [Rattus norvegicus].
ACCESSION   NP_001424810 XP_006241379
VERSION     NP_001424810.1
DBSOURCE    REFSEQ: accession NM_001437881.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Hao,Y., Niu,H., An,S., Wang,M. and Wang,Z.
  TITLE     Downregulation of iNOS, IL-1beta, and P2X7 Expression in Mast Cells
            via Activation of PAR4 Contributes to the Inhibition of Visceral
            Hyperalgesia in Rats
  JOURNAL   J Immunol Res 2018, 3256908 (2018)
   PUBMED   29854833
  REMARK    GeneRIF: this study shows that downregulation of iNOS, IL-1beta,
            and P2X7 expression in mast cells via activation of PAR4
            contributes to the Inhibition of visceral hyperalgesia
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Du,W.W., Li,X., Li,T., Li,H., Khorshidi,A., Liu,F. and Yang,B.B.
  TITLE     The microRNA miR-17-3p inhibits mouse cardiac fibroblast senescence
            by targeting Par4
  JOURNAL   J Cell Sci 128 (2), 293-304 (2015)
   PUBMED   25472717
REFERENCE   3  (residues 1 to 332)
  AUTHORS   de Thonel,A., Hazoume,A., Kochin,V., Isoniemi,K., Jego,G.,
            Fourmaux,E., Hammann,A., Mjahed,H., Filhol,O., Micheau,O.,
            Rocchi,P., Mezger,V., Eriksson,J.E., Rangnekar,V.M. and Garrido,C.
  TITLE     Regulation of the proapoptotic functions of prostate apoptosis
            response-4 (Par-4) by casein kinase 2 in prostate cancer cells
  JOURNAL   Cell Death Dis 5 (1), e1016 (2014)
   PUBMED   24457960
  REMARK    GeneRIF: Phosphorylation by CK2 impairs Par-4 proapoptotic
            functions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Wang,Z., Chen,D., Zhang,R., An,S., Zhang,Z. and Ma,Q.
  TITLE     Interleukin-1beta increased the expression of protease-activated
            receptor 4 mRNA and protein in dorsal root ganglion neurons
  JOURNAL   Neurochem Res 38 (9), 1895-1903 (2013)
   PUBMED   23775412
REFERENCE   5  (residues 1 to 332)
  AUTHORS   MacDonald,J.A., Moffat,L.D., Al-Ghabkari,A., Sutherland,C. and
            Walsh,M.P.
  TITLE     Prostate-apoptosis response-4 phosphorylation in vascular smooth
            muscle
  JOURNAL   Arch Biochem Biophys 535 (1), 84-90 (2013)
   PUBMED   23219599
  REMARK    GeneRIF: Par-4 binding does not block MYPT1 phosphorylation in rat
            caudal arterial smooth muscle.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Duan,W., Rangnekar,V.M. and Mattson,M.P.
  TITLE     Prostate apoptosis response-4 production in synaptic compartments
            following apoptotic and excitotoxic insults: evidence for a pivotal
            role in mitochondrial dysfunction and neuronal degeneration
  JOURNAL   J Neurochem 72 (6), 2312-2322 (1999)
   PUBMED   10349840
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Guo,Q., Fu,W., Xie,J., Luo,H., Sells,S.F., Geddes,J.W., Bondada,V.,
            Rangnekar,V.M. and Mattson,M.P.
  TITLE     Par-4 is a mediator of neuronal degeneration associated with the
            pathogenesis of Alzheimer disease
  JOURNAL   Nat Med 4 (8), 957-962 (1998)
   PUBMED   9701251
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Boghaert,E.R., Sells,S.F., Walid,A.J., Malone,P., Williams,N.M.,
            Weinstein,M.H., Strange,R. and Rangnekar,V.M.
  TITLE     Immunohistochemical analysis of the proapoptotic protein Par-4 in
            normal rat tissues
  JOURNAL   Cell Growth Differ 8 (8), 881-890 (1997)
   PUBMED   9269897
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Johnstone,R.W., See,R.H., Sells,S.F., Wang,J., Muthukkumar,S.,
            Englert,C., Haber,D.A., Licht,J.D., Sugrue,S.P., Roberts,T.,
            Rangnekar,V.M. and Shi,Y.
  TITLE     A novel repressor, par-4, modulates transcription and growth
            suppression functions of the Wilms' tumor suppressor WT1
  JOURNAL   Mol Cell Biol 16 (12), 6945-6956 (1996)
   PUBMED   8943350
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Sells,S.F., Wood,D.P. Jr., Joshi-Barve,S.S., Muthukumar,S.,
            Jacob,R.J., Crist,S.A., Humphreys,S. and Rangnekar,V.M.
  TITLE     Commonality of the gene programs induced by effectors of apoptosis
            in androgen-dependent and -independent prostate cells
  JOURNAL   Cell Growth Differ 5 (4), 457-466 (1994)
   PUBMED   8043520
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006241379.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.38877.1,
                                           SRR26643297.24996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..332
                     /product="PRKC apoptosis WT1 regulator protein"
                     /note="prostate apoptosis response 4 protein;
                     transcriptional repressor Par-4-like protein PAWR; par-4
                     induced by effectors of apoptosis; Prostate apoptosis
                     response protein 4; PRKC, apoptosis, WT1, regulator"
                     /calculated_mol_wt=35722
     Region          1..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          61..65
                     /region_name="B30.2/SPRY domain-binding motif.
                     /evidence=ECO:0000250|UniProtKB:Q96IZ0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          137..195
                     /region_name="Selective for apoptosis induction in cancer
                     cells (SAC)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Region          137..153
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:15657440; propagated from
                     UniProtKB/Swiss-Prot (Q62627.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IZ0; propagated from
                     UniProtKB/Swiss-Prot (Q62627.1)"
     Region          258..325
                     /region_name="Atg16_CCD"
                     /note="Coiled-coiled domain of autophagy-related 16
                     (Atg16) family proteins; cl46300"
                     /db_xref="CDD:480640"
     Site            order(260..261,263..264,267,270..271,274..275,277..278,
                     281..282,285,288..289,292,295..296,298..299,302,305..306,
                     309..310,312..313,316..317,319..320,323..324)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:439196"
     Region          292..332
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62627.1)"
     CDS             1..332
                     /gene="Pawr"
                     /gene_synonym="Par-4; Par4"
                     /coded_by="NM_001437881.1:240..1238"
                     /db_xref="GeneID:64513"
                     /db_xref="RGD:69065"
ORIGIN      
        1 matggyrssg sttdfleewk akrekmrakq npvgpgssgg dpaakspagp laqttaagts
       61 elnhgpagaa apaapgpgal ncahgssalp rgapgsrrpe decpiaagaa gapasrgdee
      121 epdsapekgr ssgpsarkgk gqiekrklre krrstgvvni paaecldeye ddeagqkerk
      181 redaitqqnt iqneaaslpd pgtsylpqdp srtvpgryks ttsapeeeil nryprtdrsg
      241 fsrhnrdtsa panfassstl ekriedleke vlrerqenlr ltrlmqdkee migklkeeid
      301 llnrdlddme deneqlkqen ktllkvvgql tr
//
LOCUS       NP_001100889             995 aa            linear   ROD 13-APR-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100889 XP_001074047 XP_226380
VERSION     NP_001100889.1
DBSOURCE    REFSEQ: accession NM_001107419.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Thompson,P.J., Norton,K.A., Niri,F.H., Dawe,C.E. and McDermid,H.E.
  TITLE     CECR2 is involved in spermatogenesis and forms a complex with SNF2H
            in the testis
  JOURNAL   J Mol Biol 415 (5), 793-806 (2012)
   PUBMED   22154806
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Hargreaves,D.C. and Crabtree,G.R.
  TITLE     ATP-dependent chromatin remodeling: genetics, genomics and
            mechanisms
  JOURNAL   Cell Res 21 (3), 396-420 (2011)
   PUBMED   21358755
  REMARK    Review article
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   4  (residues 1 to 995)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   5  (residues 1 to 995)
  AUTHORS   Torres-Padilla,M.E. and Zernicka-Goetz,M.
  TITLE     Role of TIF1alpha as a modulator of embryonic transcription in the
            mouse zygote
  JOURNAL   J Cell Biol 174 (3), 329-338 (2006)
   PUBMED   16880268
REFERENCE   6  (residues 1 to 995)
  AUTHORS   Loyola,A., Huang,J.Y., LeRoy,G., Hu,S., Wang,Y.H., Donnelly,R.J.,
            Lane,W.S., Lee,S.C. and Reinberg,D.
  TITLE     Functional analysis of the subunits of the chromatin assembly
            factor RSF
  JOURNAL   Mol Cell Biol 23 (19), 6759-6768 (2003)
   PUBMED   12972596
REFERENCE   7  (residues 1 to 995)
  AUTHORS   Bozhenok,L., Wade,P.A. and Varga-Weisz,P.
  TITLE     WSTF-ISWI chromatin remodeling complex targets heterochromatic
            replication foci
  JOURNAL   EMBO J 21 (9), 2231-2241 (2002)
   PUBMED   11980720
  REMARK    Erratum:[EMBO J 2002 Jun 17;21(12):3212]
REFERENCE   8  (residues 1 to 995)
  AUTHORS   Loyola,A., LeRoy,G., Wang,Y.H. and Reinberg,D.
  TITLE     Reconstitution of recombinant chromatin establishes a requirement
            for histone-tail modifications during chromatin assembly and
            transcription
  JOURNAL   Genes Dev 15 (21), 2837-2851 (2001)
   PUBMED   11691835
REFERENCE   9  (residues 1 to 995)
  AUTHORS   Strohner,R., Nemeth,A., Jansa,P., Hofmann-Rohrer,U., Santoro,R.,
            Langst,G. and Grummt,I.
  TITLE     NoRC--a novel member of mammalian ISWI-containing chromatin
            remodeling machines
  JOURNAL   EMBO J 20 (17), 4892-4900 (2001)
   PUBMED   11532953
REFERENCE   10 (residues 1 to 995)
  AUTHORS   LeRoy,G., Orphanides,G., Lane,W.S. and Reinberg,D.
  TITLE     Requirement of RSF and FACT for transcription of chromatin
            templates in vitro
  JOURNAL   Science 282 (5395), 1900-1904 (1998)
   PUBMED   9836642
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_226380.2, XP_001074047.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..995
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     5 isoform 2"
                     /note="SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily A member 5; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin, subfamily a, member 5"
                     /calculated_mol_wt=116524
     Region          12..955
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     CDS             1..995
                     /gene="Smarca5"
                     /coded_by="NM_001107419.1:46..3033"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307766"
                     /db_xref="RGD:1308832"
ORIGIN      
        1 meevfddgsp gkqkeiqepd ptyeekmqtd ranrfeyllk qtelfahfiq paaqktptsp
       61 lkmkpgrprv kkdekqnlls vgdyrhrrte qeedeellte sskatnvctr fedspsyvkw
      121 gklrdyqvrg lnwlislyen gingiladem glgktlqtis llgymkhyrn ipgphmvlvp
      181 kstlhnwmse fkrwvptlrs vcligdkeqr aafvrdvllp gewdvcvtsy emlikeksvf
      241 kkfnwrylvi deahriknek sklseivref kttnrllltg tplqnnlhel wsllnfllpd
      301 vfnsaddfds wfdtnnclgd qklverlhmv lrpfllrrik advekslppk kevkiyvgls
      361 kmqrewytri lmkdidilns agkmdkmrll nilmqlrkcc nhpylfdgae pgppyttdmh
      421 lvtnsgkmvv ldkllpklke qgsrvlifsq mtrvldiled ycmwrnyeyc rldgqtphde
      481 rqdsinayne pnstkfvfml stragglgin latadvvily dsdwnpqvdl qamdrahrig
      541 qtktvrvfrf itdntveeri veraemklrl dsiviqqgrl vdqnlnkigk demlqmirhg
      601 athvfaskes eitdedidgi lergakktae mneklskmge sslrnftmdt essvynfege
      661 dyrekqkiaf tewieppkre rkanyavday frealrvsep kapkaprppk qpnvqdfqff
      721 pprlfellek eilyyrktig ykvprspdlp naaqaqkeeq lkideagpln deeleekekl
      781 ltqgftnwnk rdfnqfikan ekwgrddien iarevegktp eevieysavf wercnelqdi
      841 ekimaqierg eariqrrisi kkaldtkigr ykapfhqlri sygtnkgkny teeedrflic
      901 mlhklgfdke nvydelrqci rnspqfrfdw flksrtamel qrrcntlitl ierenmelee
      961 kekaekkkrg pkpstqkrkm dgapdgrgrk kklkl
//
LOCUS       NP_999623                569 aa            linear   ROD 13-APR-2025
DEFINITION  phosphatase and actin regulator 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_999623 XP_218094
VERSION     NP_999623.2
DBSOURCE    REFSEQ: accession NM_214458.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Chiocco,M.J., Zhu,X., Walther,D., Pletnikova,O., Troncoso,J.C.,
            Uhl,G.R. and Liu,Q.R.
  TITLE     Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative
            splicing patterns, association of 5'UTR trinucleotide repeat with
            addiction vulnerability, and differential isoform expression in
            Alzheimer's disease
  JOURNAL   Subst Use Misuse 45 (11), 1809-1826 (2010)
   PUBMED   20590401
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Goldstein,B.A., Hubbard,A.E., Cutler,A. and Barcellos,L.F.
  TITLE     An application of Random Forests to a genome-wide association
            dataset: methodological considerations & new findings
  JOURNAL   BMC Genet 11, 49 (2010)
   PUBMED   20546594
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Wider,C., Lincoln,S.J., Heckman,M.G., Diehl,N.N., Stone,J.T.,
            Haugarvoll,K., Aasly,J.O., Gibson,J.M., Lynch,T., Rajput,A.,
            Rajput,M.L., Uitti,R.J., Wszolek,Z.K., Farrer,M.J. and Ross,O.A.
  TITLE     Phactr2 and Parkinson's disease
  JOURNAL   Neurosci Lett 453 (1), 9-11 (2009)
   PUBMED   19429005
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Allen,P.B., Greenfield,A.T., Svenningsson,P., Haspeslagh,D.C. and
            Greengard,P.
  TITLE     Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 7187-7192 (2004)
   PUBMED   15107502
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Nov 27, 2020 this sequence version replaced NP_999623.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY500158.1, SRR26643298.147.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..569
                     /product="phosphatase and actin regulator 2 isoform 2"
                     /calculated_mol_wt=62054
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62025.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62025.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75167; propagated from
                     UniProtKB/Swiss-Prot (P62025.1)"
     Region          71..96
                     /region_name="RPEL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P62025.1)"
     Region          73..94
                     /region_name="RPEL"
                     /note="RPEL repeat; pfam02755"
                     /db_xref="CDD:460677"
     Region          98..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62025.1)"
     Region          295..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62025.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62025.1)"
     Region          412..437
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Region          451..475
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P62025.1)"
     Region          488..513
                     /region_name="RPEL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P62025.1)"
     Region          488..513
                     /region_name="RPEL"
                     /note="Repeat in Drosophila CG10860, human KIAA0680 and C.
                     elegans F26H9.2; smart00707"
                     /db_xref="CDD:128947"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75167; propagated from
                     UniProtKB/Swiss-Prot (P62025.1)"
     CDS             1..569
                     /gene="Phactr2"
                     /coded_by="NM_214458.3:181..1890"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308291"
                     /db_xref="RGD:1303141"
ORIGIN      
        1 mgqtsvsals pqpgsvdgld kasiansdgp pagsqtppfk rkgklstigk ifkpwkwrkk
       61 ktsdkfrets avlerkistr qsreelirrg llkelpdqdg dvtvnfensn ghmihigeea
      121 tqeenvgkpe egnvsvcekg ppreeqaeek tagsshpkkt tgskasssps asstsshprg
      181 pkesltgkag avgttrgkkk iskqpaaaas rlspntvtse tsslkgelsd tgveslkpee
      241 tvagaeeeat gkpkavvval ppvtvppssp alplppedpc tialdtpmvl vsdgptlpis
      301 aletsplpgt eepanrttpy sstglggsre qakcfttkdg pgkagpqllt pgqmgdsles
      361 fsapedeapr eyqandsdsd gpilytdddd eedddddstg esalaskirr rdtlaiklgn
      421 rpskkeledk nilqrtseee rqelrqqigt klvrrlsqrp tteeleqrni lkqkneeeeq
      481 eakmelkrrl srklslrptv aelqarrilr fneyvevtds pdydrradkp warltpadka
      541 airkelnefk stemevhees rqftrfhrp
//
LOCUS       NP_001424807             467 aa            linear   ROD 13-APR-2025
DEFINITION  megakaryocyte-associated tyrosine-protein kinase isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424807 XP_063120269
VERSION     NP_001424807.1
DBSOURCE    REFSEQ: accession NM_001437878.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Gunn,N.J., Gorman,M.A., Dobson,R.C., Parker,M.W. and Mulhern,T.D.
  TITLE     Purification, crystallization, small-angle X-ray scattering and
            preliminary X-ray diffraction analysis of the SH2 domain of the
            Csk-homologous kinase
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 336-339
            (2011)
   PUBMED   21393838
  REMARK    GeneRIF: The CHK SH2 was expressed in Escherichia coli and the
            purified protein was characterized as monomeric by synchrotron
            small-angle X-ray scattering in-line with size-exclusion
            chromatography.
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Kuo,S.S., Moran,P., Gripp,J., Armanini,M., Phillips,H.S.,
            Goddard,A. and Caras,I.W.
  TITLE     Identification and characterization of Batk, a predominantly
            brain-specific non-receptor protein tyrosine kinase related to Csk
  JOURNAL   J Neurosci Res 38 (6), 705-715 (1994)
   PUBMED   7807586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063120269.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.794511.1,
                                           SRR26643298.37819.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840109 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..467
                     /product="megakaryocyte-associated tyrosine-protein kinase
                     isoform 1"
                     /EC_number="2.7.10.2"
                     /note="megakaryocyte-associated tyrosine-protein kinase;
                     protein kinase BATK; tyrosine-protein kinase CTK;
                     megakaryocyte-associated tyrosine kinase (non-receptor
                     protein tyrosine kinase); non-receptor protein kinase
                     protein"
                     /calculated_mol_wt=51766
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     Region          9..67
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(16,18,21,25,44..45,60,62..63)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          77..174
                     /region_name="SH2_csk_like"
                     /note="Src homology 2 (SH2) domain found in
                     Carboxyl-Terminal Src Kinase (Csk); cd09937"
                     /db_xref="CDD:198190"
     Site            order(88,106,127,129)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198190"
     Site            order(128,155)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198190"
     Region          187..441
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(200..203,206,208,219,221,248,263..266,311,315..316,
                     318,328..329)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          445..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41243.1)"
     CDS             1..467
                     /gene="Matk"
                     /gene_synonym="Batk"
                     /coded_by="NM_001437878.1:191..1594"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:60450"
                     /db_xref="RGD:69058"
ORIGIN      
        1 mptqrwapgt qcmtkcensr pkpgelafrk gdmvtileac edkswyrakh hssgqeglla
       61 aaalrqreal stdpklslmp wfhgkisgqe aiqqlqpped glflvresar hpgdyvlcvs
      121 fgrdvihyrv lhrdghltid eavcfcnlmd mvehytrdkg aictklvkpk rkqgaksaee
      181 elakagwlld lqhltlgaqi gegefgavlq geylgqkvav knikcdvtaq afldetavmt
      241 klqhrnlvrl lgvilhhgly ivmehvskgn lvnflrtrgr alvstsqllq falhvaegme
      301 yleskklvhr dlaarnilvs edlvakvsdf glakaelrkg ldssrlpvkw tapealkngr
      361 fssksdvwsf gvllwevfsy grapypkmsl kevseavekg yrmeppdscp gpvhtlmgsc
      421 weaepsrrpp frkiveklgr elrsvgvaap aggqeaegsa ptrsqdp
//
LOCUS       NP_001424803             638 aa            linear   ROD 13-APR-2025
DEFINITION  growth hormone receptor isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001424803 XP_008758976
VERSION     NP_001424803.1
DBSOURCE    REFSEQ: accession NM_001437874.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Klammt,J., Shen,S., Kiess,W., Kratzsch,J., Stobbe,H., Vogel,M.,
            Luo,F. and Pfaffle,R.
  TITLE     Clinical and biochemical consequences of an intragenic growth
            hormone receptor (GHR) deletion in a large Chinese pedigree
  JOURNAL   Clin Endocrinol (Oxf) 82 (3), 453-461 (2015)
   PUBMED   25196842
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Deng,H.Z., Deng,H., Cen,C.Q., Chen,K.Y. and Du,M.L.
  TITLE     Post-receptor crosstalk between growth hormone and insulin signal
            in rats born small for gestational age with catch-up growth
  JOURNAL   PLoS One 9 (6), e100459 (2014)
   PUBMED   24963636
  REMARK    GeneRIF: receptor crosstalk between growth hormone and insulin
            signal in rats born small for gestational age with catch-up growth
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Claessen,K.M., Kloppenburg,M., Kroon,H.M., Bijsterbosch,J.,
            Pereira,A.M., Romijn,J.A., van der Straaten,T., Nelissen,R.G.,
            Hofman,A., Uitterlinden,A.G., Duijnisveld,B.J., Lakenberg,N.,
            Beekman,M., van Meurs,J.B., Slagboom,P.E., Biermasz,N.R. and
            Meulenbelt,I.
  TITLE     Relationship between the functional exon 3 deleted growth hormone
            receptor polymorphism and symptomatic osteoarthritis in women
  JOURNAL   Ann Rheum Dis 73 (2), 433-436 (2014)
   PUBMED   23740230
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Enhamre,E., Carlsson,A., Gronbladh,A., Watanabe,H., Hallberg,M. and
            Nyberg,F.
  TITLE     The expression of growth hormone receptor gene transcript in the
            prefrontal cortex is affected in male mice with diabetes-induced
            learning impairments
  JOURNAL   Neurosci Lett 523 (1), 82-86 (2012)
   PUBMED   22750159
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Frick,G.P. and Goodman,H.M.
  TITLE     Characterization of the short isoform of the growth hormone
            receptor synthesized by rat adipocytes
  JOURNAL   Endocrinology 131 (6), 3083-3090 (1992)
   PUBMED   1446642
REFERENCE   7  (residues 1 to 638)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Godowski,P.J., Leung,D.W., Meacham,L.R., Galgani,J.P., Hellmiss,R.,
            Keret,R., Rotwein,P.S., Parks,J.S., Laron,Z. and Wood,W.I.
  TITLE     Characterization of the human growth hormone receptor gene and
            demonstration of a partial gene deletion in two patients with
            Laron-type dwarfism
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8083-8087 (1989)
   PUBMED   2813379
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Baumbach,W.R., Horner,D.L. and Logan,J.S.
  TITLE     The growth hormone-binding protein in rat serum is an alternatively
            spliced form of the rat growth hormone receptor
  JOURNAL   Genes Dev 3 (8), 1199-1205 (1989)
   PUBMED   2792761
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Mathews,L.S., Enberg,B. and Norstedt,G.
  TITLE     Regulation of rat growth hormone receptor gene expression
  JOURNAL   J Biol Chem 264 (17), 9905-9910 (1989)
   PUBMED   2722883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008758976.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.8824.1,
                                           SRR26643285.7354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..638
                     /product="growth hormone receptor isoform 1 precursor"
                     /note="growth hormone receptor/binding protein; GH
                     receptor; somatotropin receptor; growth hormone receptor
                     variant d5-6"
                     /calculated_mol_wt=69187
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=2068
     mat_peptide     19..638
                     /product="Growth hormone receptor. /id=PRO_0000010969"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
                     /calculated_mol_wt=69187
     Region          49..127
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          149..250
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(149,222,239)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          240..244
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000250|UniProtKB:P10912"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            order(240..241,243..244)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            266..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          295..380
                     /region_name="Required for JAK2 binding.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          298..306
                     /region_name="Box 1 motif.
                     /evidence=ECO:0000269|PubMed:8063815"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Region          317..616
                     /region_name="GHBP"
                     /note="Growth hormone receptor binding; pfam12772"
                     /db_xref="CDD:463696"
     Region          341..350
                     /region_name="UbE motif.
                     /evidence=ECO:0000305|PubMed:7615519"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Region          357..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16310.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P10912; propagated from
                     UniProtKB/Swiss-Prot (P16310.1)"
     CDS             1..638
                     /gene="Ghr"
                     /gene_synonym="GHR/BP"
                     /coded_by="NM_001437874.1:241..2157"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:25235"
                     /db_xref="RGD:2687"
ORIGIN      
        1 mdlwrvfltl alavssdmfp gsgatpatlg kaspvlqrin pslresssgk prftkcrspe
       61 letfscywte gddhnlkvpg siqlyyarri ahewtpewke cpdyvsagan scyfnssyts
      121 iwipyciklt tngdlldekc ftvdeivqpd ppiglnwtll nislpgirgd iqvswqppps
      181 advlkgwiil eyeiqykevn etkwktmspi wstsvplysl rldkehevrv rsrqrsfeky
      241 sefsevlrvt fpqmdtlaac eedfrfpwfl iiifgifgva vmlfvvifsk qqrikmlilp
      301 pvpvpkikgi dpdllkegkl eevntilgih dnykpdfynd dswvefield iddadektee
      361 sdtdrllsdd qeksagilga kdddsgrtsc ydpdildtdf htsdmcdgts efaqpqklka
      421 eadllcldqk nlknspydas lgslhpsitl tmedkpqpll gsetesthql pstpmsspvs
      481 lanidfyaqv sditpaggvv lspgqkikag laqgntqlev aapcqenysm nsayfcesda
      541 kkciaaaphm eattcvkpsf nqediyitte sltttarmse tadtapdaep vpdyttvhtv
      601 ksprglilna talplpdkkk flsscgyvst dqlnkimq
//
LOCUS       NP_001424773             445 aa            linear   ROD 13-APR-2025
DEFINITION  transcriptional enhancer factor TEF-4 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424773 XP_006229131
VERSION     NP_001424773.1
DBSOURCE    REFSEQ: accession NM_001437844.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Tamm,C., Bower,N. and Anneren,C.
  TITLE     Regulation of mouse embryonic stem cell self-renewal by a
            Yes-YAP-TEAD2 signaling pathway downstream of LIF
  JOURNAL   J Cell Sci 124 (Pt 7), 1136-1144 (2011)
   PUBMED   21385842
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Tian,W., Yu,J., Tomchick,D.R., Pan,D. and Luo,X.
  TITLE     Structural and functional analysis of the YAP-binding domain of
            human TEAD2
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7293-7298 (2010)
   PUBMED   20368466
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Bhattaram,P., Penzo-Mendez,A., Sock,E., Colmenares,C., Kaneko,K.J.,
            Vassilev,A., Depamphilis,M.L., Wegner,M. and Lefebvre,V.
  TITLE     Organogenesis relies on SoxC transcription factors for the survival
            of neural and mesenchymal progenitors
  JOURNAL   Nat Commun 1 (1), 9 (2010)
   PUBMED   20596238
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Zhang,H., Liu,C.Y., Zha,Z.Y., Zhao,B., Yao,J., Zhao,S., Xiong,Y.,
            Lei,Q.Y. and Guan,K.L.
  TITLE     TEAD transcription factors mediate the function of TAZ in cell
            growth and epithelial-mesenchymal transition
  JOURNAL   J Biol Chem 284 (20), 13355-13362 (2009)
   PUBMED   19324877
  REMARK    Erratum:[J Biol Chem. 2019 Apr 12;294(15):5808. doi:
            10.1074/jbc.AAC119.008436. PMID: 30979850]
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Zhao,B., Ye,X., Yu,J., Li,L., Li,W., Li,S., Yu,J., Lin,J.D.,
            Wang,C.Y., Chinnaiyan,A.M., Lai,Z.C. and Guan,K.L.
  TITLE     TEAD mediates YAP-dependent gene induction and growth control
  JOURNAL   Genes Dev 22 (14), 1962-1971 (2008)
   PUBMED   18579750
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Sawada,A., Nishizaki,Y., Sato,H., Yada,Y., Nakayama,R.,
            Yamamoto,S., Nishioka,N., Kondoh,H. and Sasaki,H.
  TITLE     Tead proteins activate the Foxa2 enhancer in the node in
            cooperation with a second factor
  JOURNAL   Development 132 (21), 4719-4729 (2005)
   PUBMED   16207754
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Kaneko,K.J., Rein,T., Guo,Z.S., Latham,K. and DePamphilis,M.L.
  TITLE     DNA methylation may restrict but does not determine differential
            gene expression at the Sgy/Tead2 locus during mouse development
  JOURNAL   Mol Cell Biol 24 (5), 1968-1982 (2004)
   PUBMED   14966277
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Milewski,R.C., Chi,N.C., Li,J., Brown,C., Lu,M.M. and Epstein,J.A.
  TITLE     Identification of minimal enhancer elements sufficient for Pax3
            expression in neural crest and implication of Tead2 as a regulator
            of Pax3
  JOURNAL   Development 131 (4), 829-837 (2004)
   PUBMED   14736747
  REMARK    Erratum:[Development. 2004 Mar;131(5):1195]
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Yockey,C.E. and Shimizu,N.
  TITLE     cDNA cloning and characterization of mouse DTEF-1 and ETF, members
            of the TEA/ATTS family of transcription factors
  JOURNAL   DNA Cell Biol 17 (2), 187-196 (1998)
   PUBMED   9502435
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Yasunami,M., Suzuki,K., Houtani,T., Sugimoto,T. and Ohkubo,H.
  TITLE     Molecular characterization of cDNA encoding a novel protein related
            to transcriptional enhancer factor-1 from neural precursor cells
  JOURNAL   J Biol Chem 270 (31), 18649-18654 (1995)
   PUBMED   7629195
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006229131.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168947.1, SRR22582416.735549.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..445
                     /product="transcriptional enhancer factor TEF-4 isoform 1"
                     /note="Embryonic TEA domain containing factor; TEA domain
                     family member 2; transcriptional enhancer factor TEF-4"
                     /calculated_mol_wt=48903
     Region          40..107
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          227..442
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..445
                     /gene="Tead2"
                     /coded_by="NM_001437844.1:48..1385"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308582"
                     /db_xref="RGD:1593252"
ORIGIN      
        1 mgdprtgapl ddgggwtgse egseegtggs egvggdgspd aegvwspdie qsfqealaiy
       61 ppcgrrkiil sdegkmygrn eliaryiklr tgktrtrkqv sshiqvlarr ksreiqsklk
      121 dqvskdkafq tmatmssaql isapslqakl gpsgpqatel fqfwsgssgp twnvpdvkpf
      181 sqapfsmslt ppatdlpgye pppalsplpp papsppawqa ralgtarlql vefsafvepp
      241 davdsfqrhl fvhisqqcps pgapplesvd vrqiydkfpe kkgglrelyd rgpphafflv
      301 kfwadlnwgp saeeagnsgg aggfygvssq yesrelmtlt csskvcsfgk qvvekveter
      361 aqleggrfvy rllrspmcey lvnflhklrq lperymmnsv lenftilqvv tnrdtqelll
      421 ctayvfevst sergaqhhiy rlvrd
//
LOCUS       NP_001424549            1072 aa            linear   ROD 13-APR-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424549 XP_063134090
VERSION     NP_001424549.1
DBSOURCE    REFSEQ: accession NM_001437620.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Thompson,P.J., Norton,K.A., Niri,F.H., Dawe,C.E. and McDermid,H.E.
  TITLE     CECR2 is involved in spermatogenesis and forms a complex with SNF2H
            in the testis
  JOURNAL   J Mol Biol 415 (5), 793-806 (2012)
   PUBMED   22154806
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Hargreaves,D.C. and Crabtree,G.R.
  TITLE     ATP-dependent chromatin remodeling: genetics, genomics and
            mechanisms
  JOURNAL   Cell Res 21 (3), 396-420 (2011)
   PUBMED   21358755
  REMARK    Review article
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   4  (residues 1 to 1072)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   5  (residues 1 to 1072)
  AUTHORS   Torres-Padilla,M.E. and Zernicka-Goetz,M.
  TITLE     Role of TIF1alpha as a modulator of embryonic transcription in the
            mouse zygote
  JOURNAL   J Cell Biol 174 (3), 329-338 (2006)
   PUBMED   16880268
REFERENCE   6  (residues 1 to 1072)
  AUTHORS   Loyola,A., Huang,J.Y., LeRoy,G., Hu,S., Wang,Y.H., Donnelly,R.J.,
            Lane,W.S., Lee,S.C. and Reinberg,D.
  TITLE     Functional analysis of the subunits of the chromatin assembly
            factor RSF
  JOURNAL   Mol Cell Biol 23 (19), 6759-6768 (2003)
   PUBMED   12972596
REFERENCE   7  (residues 1 to 1072)
  AUTHORS   Bozhenok,L., Wade,P.A. and Varga-Weisz,P.
  TITLE     WSTF-ISWI chromatin remodeling complex targets heterochromatic
            replication foci
  JOURNAL   EMBO J 21 (9), 2231-2241 (2002)
   PUBMED   11980720
  REMARK    Erratum:[EMBO J 2002 Jun 17;21(12):3212]
REFERENCE   8  (residues 1 to 1072)
  AUTHORS   Loyola,A., LeRoy,G., Wang,Y.H. and Reinberg,D.
  TITLE     Reconstitution of recombinant chromatin establishes a requirement
            for histone-tail modifications during chromatin assembly and
            transcription
  JOURNAL   Genes Dev 15 (21), 2837-2851 (2001)
   PUBMED   11691835
REFERENCE   9  (residues 1 to 1072)
  AUTHORS   Strohner,R., Nemeth,A., Jansa,P., Hofmann-Rohrer,U., Santoro,R.,
            Langst,G. and Grummt,I.
  TITLE     NoRC--a novel member of mammalian ISWI-containing chromatin
            remodeling machines
  JOURNAL   EMBO J 20 (17), 4892-4900 (2001)
   PUBMED   11532953
REFERENCE   10 (residues 1 to 1072)
  AUTHORS   LeRoy,G., Orphanides,G., Lane,W.S. and Reinberg,D.
  TITLE     Requirement of RSF and FACT for transcription of chromatin
            templates in vitro
  JOURNAL   Science 282 (5395), 1900-1904 (1998)
   PUBMED   9836642
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Apr 7, 2025 this sequence version replaced XP_063134090.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.79341.1,
                                           SRR26643297.51389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..1072
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     5 isoform 1"
                     /note="SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily A member 5; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin, subfamily a, member 5"
                     /calculated_mol_wt=123594
     Region          68..1011
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     CDS             1..1072
                     /gene="Smarca5"
                     /coded_by="NM_001437620.1:387..3605"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307766"
                     /db_xref="RGD:1308832"
ORIGIN      
        1 msstaepppp pppesapskp saagaggsss gnkggpegga apaapsatga gpadtemeev
       61 fddgspgkqk eiqepdptye ekmqtdranr feyllkqtel fahfiqpaaq ktptsplkmk
      121 pgrprvkkde kqnllsvgdy rhrrteqeed eelltesska tnvctrfeds psyvkwgklr
      181 dyqvrglnwl islyenging ilademglgk tlqtisllgy mkhyrnipgp hmvlvpkstl
      241 hnwmsefkrw vptlrsvcli gdkeqraafv rdvllpgewd vcvtsyemli keksvfkkfn
      301 wrylvideah riknekskls eivrefkttn rllltgtplq nnlhelwsll nfllpdvfns
      361 addfdswfdt nnclgdqklv erlhmvlrpf llrrikadve kslppkkevk iyvglskmqr
      421 ewytrilmkd idilnsagkm dkmrllnilm qlrkccnhpy lfdgaepgpp yttdmhlvtn
      481 sgkmvvldkl lpklkeqgsr vlifsqmtrv ldiledycmw rnyeycrldg qtphderqds
      541 inaynepnst kfvfmlstra gglginlata dvvilydsdw npqvdlqamd rahrigqtkt
      601 vrvfrfitdn tveerivera emklrldsiv iqqgrlvdqn lnkigkdeml qmirhgathv
      661 faskeseitd edidgilerg akktaemnek lskmgesslr nftmdtessv ynfegedyre
      721 kqkiaftewi eppkrerkan yavdayfrea lrvsepkapk aprppkqpnv qdfqffpprl
      781 fellekeily yrktigykvp rspdlpnaaq aqkeeqlkid eagplndeel eekeklltqg
      841 ftnwnkrdfn qfikanekwg rddieniare vegktpeevi eysavfwerc nelqdiekim
      901 aqiergeari qrrisikkal dtkigrykap fhqlrisygt nkgknyteee drflicmlhk
      961 lgfdkenvyd elrqcirnsp qfrfdwflks rtamelqrrc ntlitliere nmeleekeka
     1021 ekkkrgpkps vstdyvnhtv lgvlctvvcm cmcvciihic mcsnthcvgr rg
//
LOCUS       NP_001424817             683 aa            linear   ROD 13-APR-2025
DEFINITION  U4/U6 small nuclear ribonucleoprotein Prp3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424817 XP_063138242
VERSION     NP_001424817.1
DBSOURCE    REFSEQ: accession NM_001437888.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Agafonov,D.E., Kastner,B., Dybkov,O., Hofele,R.V., Liu,W.T.,
            Urlaub,H., Luhrmann,R. and Stark,H.
  TITLE     Molecular architecture of the human U4/U6.U5 tri-snRNP
  JOURNAL   Science 351 (6280), 1416-1420 (2016)
   PUBMED   26912367
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Long,S.W., Ooi,J.Y., Yau,P.M. and Jones,P.L.
  TITLE     A brain-derived MeCP2 complex supports a role for MeCP2 in RNA
            processing
  JOURNAL   Biosci Rep 31 (5), 333-343 (2011)
   PUBMED   21070191
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Song,E.J., Werner,S.L., Neubauer,J., Stegmeier,F., Aspden,J.,
            Rio,D., Harper,J.W., Elledge,S.J., Kirschner,M.W. and Rape,M.
  TITLE     The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
            reversible ubiquitination at the spliceosome
  JOURNAL   Genes Dev 24 (13), 1434-1447 (2010)
   PUBMED   20595234
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Wahl,M.C., Will,C.L. and Luhrmann,R.
  TITLE     The spliceosome: design principles of a dynamic RNP machine
  JOURNAL   Cell 136 (4), 701-718 (2009)
   PUBMED   19239890
  REMARK    Review article
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Schaffert,N., Hossbach,M., Heintzmann,R., Achsel,T. and Luhrmann,R.
  TITLE     RNAi knockdown of hPrp31 leads to an accumulation of U4/U6
            di-snRNPs in Cajal bodies
  JOURNAL   EMBO J 23 (15), 3000-3009 (2004)
   PUBMED   15257298
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Chakarova,C.F., Hims,M.M., Bolz,H., Abu-Safieh,L., Patel,R.J.,
            Papaioannou,M.G., Inglehearn,C.F., Keen,T.J., Willis,C.,
            Moore,A.T., Rosenberg,T., Webster,A.R., Bird,A.C., Gal,A., Hunt,D.,
            Vithana,E.N. and Bhattacharya,S.S.
  TITLE     Mutations in HPRP3, a third member of pre-mRNA splicing factor
            genes, implicated in autosomal dominant retinitis pigmentosa
  JOURNAL   Hum Mol Genet 11 (1), 87-92 (2002)
   PUBMED   11773002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_063138242.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.9892.1,
                                           SRR26643299.11032.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..683
                     /product="U4/U6 small nuclear ribonucleoprotein Prp3
                     isoform 2"
                     /note="U4/U6 small nuclear ribonucleoprotein Prp3; PRP3
                     pre-mRNA processing factor 3 homolog"
                     /calculated_mol_wt=77310
     Region          3..73
                     /region_name="PWI"
                     /note="domain in splicing factors; smart00311"
                     /db_xref="CDD:214609"
     Region          308..521
                     /region_name="PRP3"
                     /note="pre-mRNA processing factor 3 (PRP3); pfam08572"
                     /db_xref="CDD:462524"
     Region          544..673
                     /region_name="DUF1115"
                     /note="Protein of unknown function (DUF1115); pfam06544"
                     /db_xref="CDD:461943"
     CDS             1..683
                     /gene="Prpf3"
                     /coded_by="NM_001437888.1:87..2138"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361995"
                     /db_xref="RGD:1310555"
ORIGIN      
        1 malskrelde lkpwiektvk rvlgfseptv vtaalncvgk gmdkkkaadh lkpflddstl
       61 rfvdklfeav eegrssrhsk sssdrsrkre lkevfgddse iskessgvkk rriprfeeve
      121 eepevipgpp sespgmltkl qikqmmeaat rqieerkkql sfisppapqp ktpsssqper
      181 lpigntiqps qaatfmndai ekarkaaelq ariqaqlalk pglignanmv glanlhamgi
      241 appkvelkdq tkptplilde qgrtvdatgk evelthrmpt lkaniravkr eqfkqqlkek
      301 psedmesntf fdprvsiaps qrqrrtfkfh dkgkfekiaq rlrtkaqlek lqaeisqaar
      361 ktgihtstrl aliapkkelk egdipeieww dsyiipngfd lteenpkred yfgitnlveh
      421 paqlnppvdn dtpvtlgvyl tkkeqkklrr qtrreaqkel qekvrlgltp ppepkvrisn
      481 lmrvlgteav qdptkveahv raqmakrqka heeanaarkl taeqrkvkkv kklkedisqg
      541 vhisvyrvrn lsnpakkfki eanagqlylt gvvvlhkdvn vvvveggpka qkkfkrlmlh
      601 rikwdeqtsn tkgdddeesd eeavkktnkc vlvwegtakd rsfgemkfkq cptenmareh
      661 fkkhgaehyw dlalsesvle std
//
LOCUS       NP_001424816             116 aa            linear   ROD 13-APR-2025
DEFINITION  cocaine- and amphetamine-regulated transcript protein isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001424816 XP_006231905
VERSION     NP_001424816.1
DBSOURCE    REFSEQ: accession NM_001437887.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Casini,A., Vivacqua,G., Vaccaro,R., Renzi,A., Leone,S.,
            Pannarale,L., Franchitto,A., Onori,P., Mancinelli,R. and Gaudio,E.
  TITLE     Expression and role of cocaine-amphetamine regulated transcript
            (CART) in the proliferation of biliary epithelium
  JOURNAL   Eur J Histochem 67 (4), 3846 (2023)
   PUBMED   37859350
  REMARK    GeneRIF: Expression and role of cocaine-amphetamine regulated
            transcript (CART) in the proliferation of biliary epithelium.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Schuller,J. and Koch,M.
  TITLE     Blockade of the orexin 1-receptors and 'cocaine- and
            amphetamine-regulated transcript' in the nucleus accumbens shell
            alters impulse control in rats
  JOURNAL   Behav Brain Res 440, 114268 (2023)
   PUBMED   36539163
  REMARK    GeneRIF: Blockade of the orexin 1-receptors and 'cocaine- and
            amphetamine-regulated transcript' in the nucleus accumbens shell
            alters impulse control in rats.
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Samson,W.K., Salvemini,D. and Yosten,G.L.C.
  TITLE     Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise
  JOURNAL   Endocrinology 162 (8) (2021)
   PUBMED   34043767
  REMARK    GeneRIF: Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise.
            Review article
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Drott,C.J., Norman,D. and Espes,D.
  TITLE     CART decreases islet blood flow, but has no effect on total
            pancreatic blood flow and glucose tolerance in anesthetized rats
  JOURNAL   Peptides 135, 170431 (2021)
   PUBMED   33098940
  REMARK    GeneRIF: CART decreases islet blood flow, but has no effect on
            total pancreatic blood flow and glucose tolerance in anesthetized
            rats.
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Walker,L.C., Hand,L.J., Letherby,B., Huckstep,K.L., Campbell,E.J.
            and Lawrence,A.J.
  TITLE     Cocaine and amphetamine regulated transcript (CART) signalling in
            the central nucleus of the amygdala modulates stress-induced
            alcohol seeking
  JOURNAL   Neuropsychopharmacology 46 (2), 325-333 (2021)
   PUBMED   32826981
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Walder,K., Morris,C. and Ravussin,E.
  TITLE     A polymorphism in the gene encoding CART is not associated with
            obesity in Pima Indians
  JOURNAL   Int J Obes Relat Metab Disord 24 (4), 520-521 (2000)
   PUBMED   10805512
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Echwald,S.M., Sorensen,T.I., Andersen,T., Hansen,C., Tommerup,N.
            and Pedersen,O.
  TITLE     Sequence variants in the human cocaine and amphetamine-regulated
            transcript (CART) gene in subjects with early onset obesity
  JOURNAL   Obes Res 7 (6), 532-536 (1999)
   PUBMED   10574510
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Thim,L., Nielsen,P.F., Judge,M.E., Andersen,A.S., Diers,I.,
            Egel-Mitani,M. and Hastrup,S.
  TITLE     Purification and characterisation of a new hypothalamic satiety
            peptide, cocaine and amphetamine regulated transcript (CART),
            produced in yeast
  JOURNAL   FEBS Lett 428 (3), 263-268 (1998)
   PUBMED   9654146
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Kristensen,P., Judge,M.E., Thim,L., Ribel,U., Christjansen,K.N.,
            Wulff,B.S., Clausen,J.T., Jensen,P.B., Madsen,O.D., Vrang,N.,
            Larsen,P.J. and Hastrup,S.
  TITLE     Hypothalamic CART is a new anorectic peptide regulated by leptin
  JOURNAL   Nature 393 (6680), 72-76 (1998)
   PUBMED   9590691
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Douglass,J., McKinzie,A.A. and Couceyro,P.
  TITLE     PCR differential display identifies a rat brain mRNA that is
            transcriptionally regulated by cocaine and amphetamine
  JOURNAL   J Neurosci 15 (3 Pt 2), 2471-2481 (1995)
   PUBMED   7891182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006231905.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.5470.1, CB733430.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..116
                     /product="cocaine- and amphetamine-regulated transcript
                     protein isoform 2 precursor"
                     /note="cocaine and amphetamine regulated transcript;
                     cocaine- and amphetamine-regulated transcript protein"
                     /calculated_mol_wt=9956
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2758
     Region          48..116
                     /region_name="CART"
                     /note="Cocaine and amphetamine regulated transcript
                     protein (CART); pfam06373"
                     /db_xref="CDD:461888"
     CDS             1..116
                     /gene="Cartpt"
                     /gene_synonym="Cart"
                     /coded_by="NM_001437887.1:20..370"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29131"
                     /db_xref="RGD:2272"
ORIGIN      
        1 messrlrllp vlgaalllll pllgagaqed aelqpraldi ysavddashe keliealqev
       61 lkklkskrip iyekkygqvp mcdageqcav rkgarigklc dcprgtscns fllkcl
//
LOCUS       NP_001029283             610 aa            linear   ROD 13-APR-2025
DEFINITION  prolactin receptor isoform a precursor [Rattus norvegicus].
ACCESSION   NP_001029283
VERSION     NP_001029283.2
DBSOURCE    REFSEQ: accession NM_001034111.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Ortiz-Perez,A., Limon-Morales,O., Rojas-Castaneda,J.C., Cerbon,M.
            and Picazo,O.
  TITLE     Prolactin prevents the kainic acid-induced neuronal loss in the rat
            hippocampus by inducing prolactin receptor and putatively
            increasing the VGLUT1 overexpression
  JOURNAL   Neurosci Lett 694, 116-123 (2019)
   PUBMED   30500398
  REMARK    GeneRIF: Study indicates that chronic prolactin administration
            before kainic acid induced damage induces hippocampal
            neuroprotection associated with prolactin receptor and VGLUT1
            overexpression.
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Vergara-Castaneda,E., Grattan,D.R., Pasantes-Morales,H.,
            Perez-Dominguez,M., Cabrera-Reyes,E.A., Morales,T. and Cerbon,M.
  TITLE     Prolactin mediates neuroprotection against excitotoxicity in
            primary cell cultures of hippocampal neurons via its receptor
  JOURNAL   Brain Res 1636, 193-199 (2016)
   PUBMED   26874070
  REMARK    GeneRIF: This study demonstrated that the Cultured neurons
            expressed mRNA for both PRL and its receptor (PRLR), and both PRL
            and PRLR expression levels changed after the excitotoxic insult.
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Rojas-Duran,F., Pascual-Mathey,L.I., Serrano,K., Aranda-Abreu,G.E.,
            Manzo,J., Soto-Cid,A.H. and Hernandez,M.E.
  TITLE     Correlation of prolactin levels and PRL-receptor expression with
            Stat and Mapk cell signaling in the prostate of long-term sexually
            active rats
  JOURNAL   Physiol Behav 138, 188-192 (2015)
   PUBMED   25446202
  REMARK    GeneRIF: Results showed that an active sexual life, with constant
            execution of sexual behavior, produces a sustained increase in
            serum PRL, prostate PRL receptors, and the pStat3 signaling pathway
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Arumugam,R., Fleenor,D. and Freemark,M.
  TITLE     Knockdown of prolactin receptors in a pancreatic beta cell line:
            effects on DNA synthesis, apoptosis, and gene expression
  JOURNAL   Endocrine 46 (3), 568-576 (2014)
   PUBMED   24114406
  REMARK    GeneRIF: PRLR signaling is required for DNA synthesis and survival
            of rat insulinoma cells
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Ali,S., Pellegrini,I. and Kelly,P.A.
  TITLE     A prolactin-dependent immune cell line (Nb2) expresses a mutant
            form of prolactin receptor
  JOURNAL   J Biol Chem 266 (30), 20110-20117 (1991)
   PUBMED   1718958
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Shirota,M., Banville,D., Ali,S., Jolicoeur,C., Boutin,J.M.,
            Edery,M., Djiane,J. and Kelly,P.A.
  TITLE     Expression of two forms of prolactin receptor in rat ovary and
            liver
  JOURNAL   Mol Endocrinol 4 (8), 1136-1143 (1990)
   PUBMED   2293022
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Zhang,R., Buczko,E., Tsai-Morris,C.H., Hu,Z.Z. and Dufau,M.L.
  TITLE     Isolation and characterization of two novel rat ovarian lactogen
            receptor cDNA species
  JOURNAL   Biochem Biophys Res Commun 168 (2), 415-422 (1990)
   PUBMED   2159291
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Boutin,J.M., Jolicoeur,C., Okamura,H., Gagnon,J., Edery,M.,
            Shirota,M., Banville,D., Dusanter-Fourt,I., Djiane,J. and
            Kelly,P.A.
  TITLE     Cloning and expression of the rat prolactin receptor, a member of
            the growth hormone/prolactin receptor gene family
  JOURNAL   Cell 53 (1), 69-77 (1988)
   PUBMED   2832068
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Herington,A.C., Harrison,D. and Graystone,J.
  TITLE     Hepatic binding of human and bovine growth hormones and ovine
            prolactin in the dwarf 'little' mouse
  JOURNAL   Endocrinology 112 (6), 2032-2038 (1983)
   PUBMED   6303755
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced NP_001029283.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M57668.1, SRR26643297.6937.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..610
                     /product="prolactin receptor isoform a precursor"
                     /note="PRL-R; lactogen receptor"
                     /calculated_mol_wt=64502
     sig_peptide     1..38
                     /calculated_mol_wt=4116
     Region          19..115
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     mat_peptide     39..610
                     /product="prolactin receptor isoform a"
                     /calculated_mol_wt=64502
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          122..219
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(122,193,208)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05710.2)"
     Region          210..214
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Site            order(210..211,213..214)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            230..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          262..270
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          317..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          458..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     Region          564..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05710.2)"
     CDS             1..610
                     /gene="Prlr"
                     /gene_synonym="RATPRLR"
                     /coded_by="NM_001034111.2:304..2136"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:24684"
                     /db_xref="RGD:3407"
ORIGIN      
        1 mpsalafvll vlnisllkgq sppgkpeihk crspdketft cwwnpgtdgg lptnysltys
       61 kegekttyec pdyktsgpns cffskqytsi wkiyiitvna tnqmgssssd plyvdvtyiv
      121 epepprnltl evkqlkdkkt ylwvkwsppt itdvktgwft meyeirlkpe eaeeweihft
      181 ghqtqfkvfd lypgqkylvq trckpdhgyw srwsqessve mpndftlkdt tvwiivails
      241 aviclimvwa valkgysmmt cifppvpgpk ikgfdthlle kgkseellsa lgcqdfppts
      301 dcedllvefl evddnederl mpshskeypg qgvkpthldp dsdsghgsyd shsllsekce
      361 epqaypptlh ipeitekpen peanipptvd pqstnpnfhv dapksstwpl lpgqhmprsp
      421 yhsvadvckl agspvntlds fldkaeenvl klskaletge eevaeqkgak sfpsdkqntp
      481 wpllqekspt vyvkppdyve ihkvnkdgvl slfpkqrenn qtekpgvpet skeyakvsgi
      541 tdnnilvlvp dsraqntall eesakkapps feadqsekdl asftatssnr rlqlgrldyl
      601 dptcfmhsfh
//
LOCUS       NP_001424784             550 aa            linear   ROD 13-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424784 XP_008768715
VERSION     NP_001424784.1
DBSOURCE    REFSEQ: accession NM_001437855.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Yang,X., Sha,X., Cao,Y., Wang,W. and Shi,J.
  TITLE     Cx43 overexpression reduce the incidence of obstructive sleep apnea
            associated atrial fibrillation via the CaMKgamma/HIF-1 axis
  JOURNAL   Biochem Biophys Res Commun 659, 62-71 (2023)
   PUBMED   37037067
  REMARK    GeneRIF: Cx43 overexpression reduce the incidence of obstructive
            sleep apnea associated atrial fibrillation via the CaMKgamma/HIF-1
            axis.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   He,X., Wang,Y., Zhou,G., Yang,J., Li,J., Li,T., Hu,H. and Ma,H.
  TITLE     A Critical Role for gammaCaMKII in Decoding NMDA Signaling to
            Regulate AMPA Receptors in Putative Inhibitory Interneurons
  JOURNAL   Neurosci Bull 38 (8), 916-926 (2022)
   PUBMED   35290589
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Huang,R. and Bi,G.
  TITLE     MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma facilitates
            vestibular compensation in acute vertigo by promoting protein
            kinase C expression
  JOURNAL   Ann N Y Acad Sci 1475 (1), 78-88 (2020)
   PUBMED   32645222
  REMARK    GeneRIF: MicroRNA-219a-5p-mediated inhibition of CaMKIIgamma
            facilitates vestibular compensation in acute vertigo by promoting
            protein kinase C expression.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Zhao,L., Xiong,L., Hao,Y.H., Li,W.C., Dong,J., Zhang,J., Yao,B.W.,
            Xu,X.P., Wang,L.F., Zhou,H.M. and Peng,R.Y.
  TITLE     Inhibition of MicroRNA 219 Expression Protects Synaptic Plasticity
            via Activating NMDAR1, CaMKIIgamma, and p-CREB after Microwave
            Radiation
  JOURNAL   Biomed Environ Sci 33 (5), 359-364 (2020)
   PUBMED   32553080
  REMARK    GeneRIF: Inhibition of MicroRNA 219 Expression Protects Synaptic
            Plasticity via Activating NMDAR1, CaMKIIgamma, and p-CREB after
            Microwave Radiation.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Liu,Y., Sun,L.Y., Singer,D.V., Ginnan,R., Zhao,W.,
            Jourd'heuil,F.L., Jourd'heuil,D., Long,X. and Singer,H.A.
  TITLE     Thymine DNA glycosylase is a key regulator of CaMKIIgamma
            expression and vascular smooth muscle phenotype
  JOURNAL   Am J Physiol Heart Circ Physiol 317 (5), H969-H980 (2019)
   PUBMED   31518169
  REMARK    GeneRIF: Thymine DNA glycosylase plays a key role in regulating
            CaMKIIgamma expression in vascular smooth muscle cells through
            promoter cytosine methylation/demethylation.
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Hook,S.S. and Means,A.R.
  TITLE     Ca(2+)/CaM-dependent kinases: from activation to function
  JOURNAL   Annu Rev Pharmacol Toxicol 41, 471-505 (2001)
   PUBMED   11264466
  REMARK    Review article
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Haeseleer,F., Sokal,I., Verlinde,C.L., Erdjument-Bromage,H.,
            Tempst,P., Pronin,A.N., Benovic,J.L., Fariss,R.N. and Palczewski,K.
  TITLE     Five members of a novel Ca(2+)-binding protein (CABP) subfamily
            with similarity to calmodulin
  JOURNAL   J Biol Chem 275 (2), 1247-1260 (2000)
   PUBMED   10625670
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Singer,H.A., Benscoter,H.A. and Schworer,C.M.
  TITLE     Novel Ca2+/calmodulin-dependent protein kinase II gamma-subunit
            variants expressed in vascular smooth muscle, brain, and
            cardiomyocytes
  JOURNAL   J Biol Chem 272 (14), 9393-9400 (1997)
   PUBMED   9083077
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Zhou,Z.L. and Ikebe,M.
  TITLE     New isoforms of Ca2+/calmodulin-dependent protein kinase II in
            smooth muscle
  JOURNAL   Biochem J 299 (Pt 2) (Pt 2), 489-495 (1994)
   PUBMED   8172610
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Tobimatsu,T., Kameshita,I. and Fujisawa,H.
  TITLE     Molecular cloning of the cDNA encoding the third polypeptide
            (gamma) of brain calmodulin-dependent protein kinase II
  JOURNAL   J Biol Chem 263 (31), 16082-16086 (1988)
   PUBMED   2846534
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 10, 2025 this sequence version replaced XP_008768715.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2551152.1,
                                           SRR26643298.56234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..550
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 5"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     gamma chain; calcium/calmodulin-dependent protein kinase
                     type II subunit gamma; Ca+2/calmodulin-dependent protein
                     kinase II gamma; caMK-II subunit gamma; caM-kinase II
                     gamma chain; caM kinase II subunit gamma;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II gamma; calcium/calmodulin-dependent protein kinase type
                     II subunit gamma-like"
                     /calculated_mol_wt=61312
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          418..545
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..550
                     /gene="Camk2g"
                     /coded_by="NM_001437855.1:70..1722"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:171140"
                     /db_xref="RGD:621802"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik gstescnttt ededlkvrkq
      421 eiikiteqli eainngdfea ytkicdpglt sfepealgnl vegmdfhkfy fenllsknsk
      481 pihttilnph vhvigedaac iayirltqyi dgqgrprtsq seetrvwhrr dgkwlnvhyh
      541 csgapaaplq
//
LOCUS       NP_001424728             210 aa            linear   ROD 13-APR-2025
DEFINITION  regulator of G-protein signaling 17 [Rattus norvegicus].
ACCESSION   NP_001424728 XP_006227916
VERSION     NP_001424728.1
DBSOURCE    REFSEQ: accession NM_001437799.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Dhukhwa,A., Al Aameri,R.F.H., Sheth,S., Mukherjea,D., Rybak,L. and
            Ramkumar,V.
  TITLE     Regulator of G protein signaling 17 represents a novel target for
            treating cisplatin induced hearing loss
  JOURNAL   Sci Rep 11 (1), 8116 (2021)
   PUBMED   33854102
  REMARK    GeneRIF: Regulator of G protein signaling 17 represents a novel
            target for treating cisplatin induced hearing loss.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Sun,H., Calipari,E.S., Beveridge,T.J., Jones,S.R. and Chen,R.
  TITLE     The brain gene expression profile of dopamine D2/D3 receptors and
            associated signaling proteins following amphetamine
            self-administration
  JOURNAL   Neuroscience 307, 253-261 (2015)
   PUBMED   26321241
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Sokolov,E., Iannitti,D.A., Schrum,L.W. and McKillop,I.H.
  TITLE     Altered expression and function of regulator of G-protein
            signaling-17 (RGS17) in hepatocellular carcinoma
  JOURNAL   Cell Signal 23 (10), 1603-1610 (2011)
   PUBMED   21620966
  REMARK    GeneRIF: RGS17 is differentially expressed in hepatocellular
            carcinoma cells and plays a central role in regulating transformed
            hepatocyte tumorgenicity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006227916.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.334788.1,
                                           SRR26360176.2124595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840109
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..210
                     /product="regulator of G-protein signaling 17"
                     /calculated_mol_wt=24189
     Region          41..197
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     CDS             1..210
                     /gene="Rgs17"
                     /coded_by="NM_001437799.1:155..787"
                     /db_xref="GeneID:308118"
                     /db_xref="RGD:1305515"
ORIGIN      
        1 mrkrqqsqne gtqavsqapg nqrpnntccf cwccccscsc ltvrneergd ssgrpphttk
       61 mesiqvleec qnptadevls wsqnfdkmmk apagrnlfre flrteyseen llfwlacedl
      121 kkeqnkkave ekarmiyedy isilspkevs ldsrvrevin rnllepsphm yedaqlqiyt
      181 lmhrdsfprf lnsqiykafv estasstses
//
LOCUS       NP_001424752             616 aa            linear   ROD 13-APR-2025
DEFINITION  sphingosine kinase 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424752 XP_006229147
VERSION     NP_001424752.1
DBSOURCE    REFSEQ: accession NM_001437823.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Dominguez,G., Maddelein,M.L., Pucelle,M., Nicaise,Y., Maurage,C.A.,
            Duyckaerts,C., Cuvillier,O. and Delisle,M.B.
  TITLE     Neuronal sphingosine kinase 2 subcellular localization is altered
            in Alzheimer's disease brain
  JOURNAL   Acta Neuropathol Commun 6 (1), 25 (2018)
   PUBMED   29615132
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Zhang,R., Li,L., Yuan,L. and Zhao,M.
  TITLE     Hypoxic preconditioning protects cardiomyocytes against
            hypoxia/reoxygenation-induced cell apoptosis via sphingosine kinase
            2 and FAK/AKT pathway
  JOURNAL   Exp Mol Pathol 100 (1), 51-58 (2016)
   PUBMED   26621495
  REMARK    GeneRIF: hypoxic preconditioning significantly increased SphK2
            expression in primary cardiomyocytes
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Sivasubramanian,M., Kanagaraj,N., Dheen,S.T. and Tay,S.S.
  TITLE     Sphingosine kinase 2 and sphingosine-1-phosphate promotes
            mitochondrial function in dopaminergic neurons of mouse model of
            Parkinson's disease and in MPP+ -treated MN9D cells in vitro
  JOURNAL   Neuroscience 290, 636-648 (2015)
   PUBMED   25637806
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Gandy,K.A., Canals,D., Adada,M., Wada,M., Roddy,P., Snider,A.J.,
            Hannun,Y.A. and Obeid,L.M.
  TITLE     Sphingosine 1-phosphate induces filopodia formation through S1PR2
            activation of ERM proteins
  JOURNAL   Biochem J 449 (3), 661-672 (2013)
   PUBMED   23106337
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Hisano,Y., Kobayashi,N., Kawahara,A., Yamaguchi,A. and Nishi,T.
  TITLE     The sphingosine 1-phosphate transporter, SPNS2, functions as a
            transporter of the phosphorylated form of the immunomodulating
            agent FTY720
  JOURNAL   J Biol Chem 286 (3), 1758-1766 (2011)
   PUBMED   21084291
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Mizugishi,K., Yamashita,T., Olivera,A., Miller,G.F., Spiegel,S. and
            Proia,R.L.
  TITLE     Essential role for sphingosine kinases in neural and vascular
            development
  JOURNAL   Mol Cell Biol 25 (24), 11113-11121 (2005)
   PUBMED   16314531
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Maceyka,M., Sankala,H., Hait,N.C., Le Stunff,H., Liu,H., Toman,R.,
            Collier,C., Zhang,M., Satin,L.S., Merrill,A.H. Jr., Milstien,S. and
            Spiegel,S.
  TITLE     SphK1 and SphK2, sphingosine kinase isoenzymes with opposing
            functions in sphingolipid metabolism
  JOURNAL   J Biol Chem 280 (44), 37118-37129 (2005)
   PUBMED   16118219
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Kharel,Y., Lee,S., Snyder,A.H., Sheasley-O'neill,S.L., Morris,M.A.,
            Setiady,Y., Zhu,R., Zigler,M.A., Burcin,T.L., Ley,K., Tung,K.S.,
            Engelhard,V.H., Macdonald,T.L., Pearson-White,S. and Lynch,K.R.
  TITLE     Sphingosine kinase 2 is required for modulation of lymphocyte
            traffic by FTY720
  JOURNAL   J Biol Chem 280 (44), 36865-36872 (2005)
   PUBMED   16093248
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Okada,T., Ding,G., Sonoda,H., Kajimoto,T., Haga,Y.,
            Khosrowbeygi,A., Gao,S., Miwa,N., Jahangeer,S. and Nakamura,S.
  TITLE     Involvement of N-terminal-extended form of sphingosine kinase 2 in
            serum-dependent regulation of cell proliferation and apoptosis
  JOURNAL   J Biol Chem 280 (43), 36318-36325 (2005)
   PUBMED   16103110
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Liu,H., Sugiura,M., Nava,V.E., Edsall,L.C., Kono,K., Poulton,S.,
            Milstien,S., Kohama,T. and Spiegel,S.
  TITLE     Molecular cloning and functional characterization of a novel
            mammalian sphingosine kinase type 2 isoform
  JOURNAL   J Biol Chem 275 (26), 19513-19520 (2000)
   PUBMED   10751414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006229147.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.1933.1,
                                           SRR26643299.2480.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..616
                     /product="sphingosine kinase 2 isoform 1"
                     /EC_number="2.7.1.91"
                     /calculated_mol_wt=65392
     Region          <152..607
                     /region_name="PLN02958"
                     /note="diacylglycerol kinase/D-erythro-sphingosine kinase"
                     /db_xref="CDD:215517"
     CDS             1..616
                     /gene="Sphk2"
                     /coded_by="NM_001437823.1:276..2126"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:308589"
                     /db_xref="RGD:1307757"
ORIGIN      
        1 mapppllpva astpilhgef gsypahgprf altlttqalh iqrlrpkpea rprdglvpld
       61 evsgcgtlqs rspedtaayf ciytyprgrr ggrrratrtf radgaatyve nraeaqrwat
      121 almcllrgvp lsgdqeitpe llprkprlll lvnpfggrgl awqrcmdhvv pmiseaglsf
      181 nliqterqnh arelvqglsl sewegivtvs gdgllyevln glldrpdwed avrmpigvlp
      241 cgsgnalaga vnhhggfeqt vgvdlllncs lllcrggshp ldllsvtlas gsrcfsflsv
      301 awgflsdvdi hserfralgs arftlgavlg latlhtyrgr lsylpattep alpipghglp
      361 rakselalap apapaathsp lhrsvsdlpl plpqpalasp gspeplpdls lngggpeltg
      421 dwggagdapl spdpllpssp nafktaqlsp iaegpsempa sgllppihna peastwgpad
      481 hllpplgspl pqdwvtiege fvlmlailps hlcadlmaap harfddgvvh lcwvrsgisr
      541 aallrillam ehgnhfslgc phlgyaaara frlepltprg vltvdgelve ygpiqaqvhp
      601 slatlltgpa gqkpra
//
LOCUS       NP_001100972             626 aa            linear   ROD 13-APR-2025
DEFINITION  leucine-rich repeat and fibronectin type-III domain-containing
            protein 3 precursor [Rattus norvegicus].
ACCESSION   NP_001100972 XP_001075911 XP_006228833 XP_218483
VERSION     NP_001100972.1
DBSOURCE    REFSEQ: accession NM_001107502.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Lie,E., Ko,J.S., Choi,S.Y., Roh,J.D., Cho,Y.S., Noh,R., Kim,D.,
            Li,Y., Kang,H., Choi,T.Y., Nam,J., Mah,W., Lee,D., Lee,S.G.,
            Kim,H.M., Kim,H., Choi,S.Y., Um,J.W., Kang,M.G., Bae,Y.C., Ko,J.
            and Kim,E.
  TITLE     SALM4 suppresses excitatory synapse development by cis-inhibiting
            trans-synaptic SALM3-LAR adhesion
  JOURNAL   Nat Commun 7, 12328 (2016)
   PUBMED   27480238
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Swanwick,C.C., Shapiro,M.E., Vicini,S. and Wenthold,R.J.
  TITLE     Flotillin-1 mediates neurite branching induced by synaptic
            adhesion-like molecule 4 in hippocampal neurons
  JOURNAL   Mol Cell Neurosci 45 (3), 213-225 (2010)
   PUBMED   20600927
  REMARK    GeneRIF: Data reveal a flotillin-1 signaling pathway for
            hippocampal neurite branching that is regulated by synaptic
            adhesion-like molecule 4.
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Seabold,G.K., Wang,P.Y., Chang,K., Wang,C.Y., Wang,Y.X.,
            Petralia,R.S. and Wenthold,R.J.
  TITLE     The SALM family of adhesion-like molecules forms heteromeric and
            homomeric complexes
  JOURNAL   J Biol Chem 283 (13), 8395-8405 (2008)
   PUBMED   18227064
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Morimura,N., Inoue,T., Katayama,K. and Aruga,J.
  TITLE     Comparative analysis of structure, expression and PSD95-binding
            capacity of Lrfn, a novel family of neuronal transmembrane proteins
  JOURNAL   Gene 380 (2), 72-83 (2006)
   PUBMED   16828986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 10, 2025 this sequence version replaced
            XP_006228833.1, XP_218483.2, XP_001075911.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158862.1, SRR21887620.793209.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN16676787
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..626
                     /product="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 3 precursor"
                     /note="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 3; synaptic adhesion-like
                     molecule 4"
                     /calculated_mol_wt=64438
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1648
     mat_peptide     17..626
                     /product="Leucine-rich repeat and fibronectin type-III
                     domain-containing protein 3. /evidence=ECO:0000255.
                     /id=PRO_0000391358"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
                     /calculated_mol_wt=64438
     Region          63..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <78..>228
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..105
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          108..129
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          109..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          132..153
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          133..157
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          157..178
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          158..181
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          181..202
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          182..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..226
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          206..230
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          242..253
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          249..>281
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          296..383
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          313..317
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          326..330
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B0BNK7.1)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          349..353
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          363..368
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          376..379
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          382..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B0BNK7.1)"
     Region          425..502
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            540..560
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK7.1)"
     CDS             1..626
                     /gene="Lrfn3"
                     /gene_synonym="Salm4"
                     /coded_by="NM_001107502.2:1206..3086"
                     /db_xref="GeneID:308495"
                     /db_xref="RGD:1305567"
ORIGIN      
        1 mavlplllcl lplapasspp qpatsspcpr rcrcqtqslp lsvlcpgagl lfvppsldrr
       61 aaelrladnf iaavrrrdla nmtgllhlsl srntirhvaa gafadlralr alhldgnrlt
      121 slgegqlrgl vnlrhlilsn nqlaalaaga lddcaetled ldlsynnleq lpwealgrlg
      181 nvntlgldhn llasvpagaf srlhklarld mtsnrlttip pdplfsrlpl larprgspas
      241 alvlafggnp lhcncelvwl rrlareddle acasppalgg ryfwavgeee fvceppvvth
      301 rspplavpag rpaalrcrav gdpeprvrwv spqgrllgns srarafpngt lellvteped
      361 ggtftciaan aageataave ltvgpppppq lanstscdpp rdgepdaltp psaasasakv
      421 adtvaptdrg vqvtehgata alvqwpdqrp vpgirmyqiq ynssaddilv yrmipadsrs
      481 flltdlasgr tydlcvlavy edsatgltat rpvgcarfst epalrpcaap hapflggtmi
      541 ialggvivas vlvfifvlll rykvhgvqpp gkakatapvs svcsqtngal gpvpsapape
      601 paaprahtvv qldcepwgps hepagp
//
LOCUS       NP_001100968             687 aa            linear   ROD 13-APR-2025
DEFINITION  protein Smaug homolog 2 [Rattus norvegicus].
ACCESSION   NP_001100968 XP_001073474 XP_001073503 XP_001073537 XP_008757365
            XP_218384
VERSION     NP_001100968.1
DBSOURCE    REFSEQ: accession NM_001107498.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Amadei,G., Zander,M.A., Yang,G., Dumelie,J.G., Vessey,J.P.,
            Lipshitz,H.D., Smibert,C.A., Kaplan,D.R. and Miller,F.D.
  TITLE     A Smaug2-Based Translational Repression Complex Determines the
            Balance between Precursor Maintenance versus Differentiation during
            Mammalian Neurogenesis
  JOURNAL   J Neurosci 35 (47), 15666-15681 (2015)
   PUBMED   26609159
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 10, 2025 this sequence version replaced
            XP_008757365.1, XP_218384.1, XP_001073537.1, XP_001073474.1,
            XP_001073503.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.2251.1,
                                           SRR22582416.745173.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..687
                     /product="protein Smaug homolog 2"
                     /calculated_mol_wt=74781
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     CDS             1..687
                     /gene="Samd4b"
                     /gene_synonym="RGD1305597"
                     /coded_by="NM_001107498.2:378..2441"
                     /db_xref="GeneID:308473"
                     /db_xref="RGD:1305597"
ORIGIN      
        1 mmfrdqvgil aswfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrt rpepsyhsrq gsdewggpae
      181 lapgeagsgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqapgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat ptakdggrge pllpgaeppl
      421 thpgsdkgte akdppaaeny ppppapapsd ssepapapva dgdipsqftr vmgkvctqll
      481 vsrpdeenit sylqliekcl theaftetqk krllswkqqv lkllrtfprk aaldmqsyrq
      541 qkgwafgsns lpiagsvgmg varrtqrqfp mppralppgr mgllspsgig gvsprhalts
      601 pslggqgrqn lwfanpggsn smpsqsrssv qrthslpvhs spqailmfpp dcpvpgpdle
      661 inptleslcl smtehalgdg tdktsti
//
LOCUS       NP_001424806             366 aa            linear   ROD 13-APR-2025
DEFINITION  prostaglandin F2-alpha receptor [Rattus norvegicus].
ACCESSION   NP_001424806 XP_006233548
VERSION     NP_001424806.1
DBSOURCE    REFSEQ: accession NM_001437877.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Fukuda,M., Aoki,T., Manabe,T., Maekawa,A., Shirakawa,T.,
            Kataoka,H., Takagi,Y., Miyamoto,S. and Narumiya,S.
  TITLE     Exacerbation of intracranial aneurysm and aortic dissection in
            hypertensive rat treated with the prostaglandin F-receptor
            antagonist AS604872
  JOURNAL   J Pharmacol Sci 126 (3), 230-242 (2014)
   PUBMED   25341845
  REMARK    GeneRIF: Prostaglandin F-receptor antagonist AS604872 exacerbates
            vascular inflammation in hypertensive animals, facilitating
            intracranial aneurysm formation and aortic dissection.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Anadol,E., Kanca,H., Yar,A.S., Helvacioglu,F., Menevse,S.,
            Calguner,E. and Erdogan,D.
  TITLE     Prostaglandin F receptor expression in intrauterine tissues of
            pregnant rats
  JOURNAL   J Vet Sci 15 (1), 125-131 (2014)
   PUBMED   24136214
  REMARK    GeneRIF: There was an increase rat prostaglandin F receptor
            expression in rat uterus with advancing gestation, a marked
            elevation of expression at term, and a concominant decrease during
            the postpartum period.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Ueno,T. and Fujimori,K.
  TITLE     Novel suppression mechanism operating in early phase of
            adipogenesis by positive feedback loop for enhancement of
            cyclooxygenase-2 expression through prostaglandin F2alpha receptor
            mediated activation of MEK/ERK-CREB cascade
  JOURNAL   FEBS J 278 (16), 2901-2912 (2011)
   PUBMED   21668646
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Suzuki-Yamamoto,T., Toida,K., Sugimoto,Y. and Ishimura,K.
  TITLE     Colocalization of prostaglandin F(2alpha) receptor FP and
            prostaglandin F synthase-I in the spinal cord
  JOURNAL   J Lipid Res 50 (10), 1996-2003 (2009)
   PUBMED   19429887
  REMARK    GeneRIF: Data found that FP localizes in neuronal somata and
            dendrites but not in ependymal cells, tanycytes, or endothelial
            cells. Immunohistochemical analysis of serial sections showed the
            colocalization of FP and PGFS I.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Almirza,W.H., Dernison,M.M., Peters,P.H., van Zoelen,E.J. and
            Theuvenet,A.P.
  TITLE     Role of the prostanoid FP receptor in action potential generation
            and phenotypic transformation of NRK fibroblasts
  JOURNAL   Cell Signal 20 (11), 2022-2029 (2008)
   PUBMED   18703136
  REMARK    GeneRIF: Activity of PGF(2alpha) by putative pacemaker cells
            underlies the generation of calcium action potentials in normal rat
            kidney monolayers.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Yonekura,H., Sakurai,S., Liu,X., Migita,H., Wang,H., Yamagishi,S.,
            Nomura,M., Abedin,M.J., Unoki,H., Yamamoto,Y. and Yamamoto,H.
  TITLE     Placenta growth factor and vascular endothelial growth factor B and
            C expression in microvascular endothelial cells and pericytes.
            Implication in autocrine and paracrine regulation of angiogenesis
  JOURNAL   J Biol Chem 274 (49), 35172-35178 (1999)
   PUBMED   10575000
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Olofsson,J.I., Leung,C.H., Bjurulf,E., Ohno,T., Selstam,G., Peng,C.
            and Leung,P.C.
  TITLE     Characterization and regulation of a mRNA encoding the
            prostaglandin F2alpha receptor in the rat ovary
  JOURNAL   Mol Cell Endocrinol 123 (1), 45-52 (1996)
   PUBMED   8912810
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Orlicky,D.J.
  TITLE     Negative regulatory activity of a prostaglandin F2 alpha receptor
            associated protein (FPRP)
  JOURNAL   Prostaglandins Leukot Essent Fatty Acids 54 (4), 247-259 (1996)
   PUBMED   8804121
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Lake,S., Gullberg,H., Wahlqvist,J., Sjogren,A.M., Kinhult,A.,
            Lind,P., Hellstrom-Lindahl,E. and Stjernschantz,J.
  TITLE     Cloning of the rat and human prostaglandin F2 alpha receptors and
            the expression of the rat prostaglandin F2 alpha receptor
  JOURNAL   FEBS Lett 355 (3), 317-325 (1994)
   PUBMED   7988697
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Kitanaka,J., Hasimoto,H., Sugimoto,Y., Negishi,M., Aino,H.,
            Gotoh,M., Ichikawa,A. and Baba,A.
  TITLE     Cloning and expression of a cDNA for rat prostaglandin F2 alpha
            receptor
  JOURNAL   Prostaglandins 48 (1), 31-41 (1994)
   PUBMED   7972878
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006233548.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.7082.1,
                                           SRR26643289.8015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..366
                     /product="prostaglandin F2-alpha receptor"
                     /note="PGF receptor; prostanoid FP receptor; PGF2-alpha
                     receptor"
                     /calculated_mol_wt=40524
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43118.1)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43118.1)"
     Region          27..316
                     /region_name="7tmA_FP"
                     /note="prostaglandin F2-alpha receptor, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15145"
                     /db_xref="CDD:320273"
     Region          28..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320273"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          66..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320273"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Site            order(88,91..92,108..113,115..116,119,164,166..170,197,
                     200..202,204..206,208..209,262,265..266,268..269,272,
                     282..283,285..287,290,293..294)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320273"
     Region          108..138
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320273"
     Site            110..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          150..172
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320273"
     Site            153..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          197..226
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320273"
     Site            199..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          242..272
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320273"
     Site            251..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     Region          283..308
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320273"
     Site            286..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43118.1)"
     CDS             1..366
                     /gene="Ptgfr"
                     /gene_synonym="PF2AR"
                     /coded_by="NM_001437877.1:250..1350"
                     /db_xref="GeneID:25652"
                     /db_xref="RGD:3436"
ORIGIN      
        1 msinsskqpa ssaagliant tcqtenrlsv ffsiifmtvg ivsnslaiai lmkayqrfrr
       61 kskasfllla sglvitdffg hlinggiavf vyasdkdwir fdqsnilcsv fgismvfsgl
      121 cplflgstma iercigvtnp lfhstkitsk hvkmilsgvc mfavfvallp ilghrdyqiq
      181 asrtwcfynt ehiedwedrf yllffsslgl lalgisfscn avtgvtllrv kfrsqqhrqg
      241 rshhlemviq llaimcvscv cwspflvtma niaingnnsp vtcettlfal rmatwnqild
      301 pwvyillrka vlrnlyklas rccgvniisl hiwelssikn slkvaaises paaekenqqa
      361 sseagl
//
LOCUS       NP_001424746            1682 aa            linear   ROD 13-APR-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH [Rattus norvegicus].
ACCESSION   NP_001424746 XP_006227701
VERSION     NP_001424746.1
DBSOURCE    REFSEQ: accession NM_001437817.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1682)
  AUTHORS   Zeman,M.K., Lin,J.R., Freire,R. and Cimprich,K.A.
  TITLE     DNA damage-specific deubiquitination regulates Rad18 functions to
            suppress mutagenesis
  JOURNAL   J Cell Biol 206 (2), 183-197 (2014)
   PUBMED   25023518
REFERENCE   2  (residues 1 to 1682)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
REFERENCE   3  (residues 1 to 1682)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
REFERENCE   4  (residues 1 to 1682)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006227701.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.54.1, SRR26643292.53.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1682
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..1682
                     /product="E3 ubiquitin-protein ligase SHPRH"
                     /EC_number="2.3.2.27"
                     /note="SNF2 histone linker PHD RING helicase, E3 ubiquitin
                     protein ligase"
                     /calculated_mol_wt=192425
     Region          151..>382
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          298..>414
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            369..375
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          434..502
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          659..705
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(659,672..676,680,700)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <701..902
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          1428..1481
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1507..1632
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1536..1537,1545,1584,1605..1606)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1590..1591,1593,1616,1619)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1682
                     /gene="Shprh"
                     /coded_by="NM_001437817.1:153..5201"
                     /db_xref="GeneID:308282"
                     /db_xref="RGD:1310342"
ORIGIN      
        1 mssrrkrapp mkvdeerqqq lrwnmhedlr neplslteee racwdadssd ciiidddppe
       61 gaahrdkkrc tesvsilnst eketplsval nvtisphpsd dswkaflgdf vlqllpeesl
      121 vehfsertft lmssesssql liyvhsecnn vekeenvlkg pasiygkgir vessfssdml
      181 qdlawlqkrr giklyqrpeg thtikvriyl leagltrldf msdagsrmkk fnqllkrvmg
      241 klyslsipdv leedeeeses epegqdidel yqfvkrthqq eaksvqvdvq hpalipvlrp
      301 yqreavnwml qqeqfrstpa gdnslhflwr eivtpdglnl yynpytgcii rdfphagpql
      361 lggilademg lgktvevlal ilthtrqdvr qdaltlpegk vvnyfipthc prgkvksrei
      421 qntecepkek vhcpptrvmi ltavkemngk kgvsilsiyk yvsstfrydv qrnrsllkrm
      481 lkclifeglv kqikgrgfsg tftlgknyke dvfdktkkqa vgspqkieke lrksvnkdtd
      541 seympsdiyd ddndnddddd ddpyyyycka rksrklkkkp vlltkkekgq pvnldsqvea
      601 paagdcasad ahvsestcvs enrqiqdaed cvespspaam elaqsntasf cetpdyrfec
      661 icgefdqigr kprvqclkch lwqhakcvny eeknlkvkpf ycphclvame pvstratlii
      721 spssichqwv deinrhvrss slrvlvyqgv kkdgflqphf laeqdiviit ydvlrselny
      781 vdiphsnsed grrlrnqkry maipsplvav ewwricldea qmvecptvka aemaqrlsgi
      841 nrwcvsgtpv qrgledlfgl vvflgiepyc vkhwwirlly hpyckknpqh lysfiakimw
      901 rsakkdvidq iqippqteem hwlhfspver hfyhrqhevc cqdavvklrk isdwalklss
      961 ldrrtvssil ypllrlrqac chpqavrgef lplqkstmtm eelltslqkk cgteceeahr
     1021 qlvcalngla gihiikgeya laaelyrevl rsseehkgkl ktdslqrlha thnlmellva
     1081 khpgipptlr dgrleeeakq lrehymskcn tevaeaqqal qpvqqsirel qrkvhsgspw
     1141 wlnvvhrame yavdeelvqr vrneissnyk hqtdklsmse kfrdcrglqf llttqmeelh
     1201 kfqklvreav kklekppsrd viesatvchl rparlplncc vfckadelft eyesklfsnt
     1261 vkgqtaifee miedeeglvd drvptttrgl wavsetersm kailsfarsh rfdveyideg
     1321 svsmdlfeaw kkeykllhey wmtlrnrvsa vdelamater lrvrhpkepk pnppvhhiie
     1381 pheveqnrik lvndkavats qlqkklgqll yltnleksqd ktsgginpep cpicarqlgk
     1441 qwavltcghc fcnectsiii eqysvgshrs sikcaicrqt tshkevsyvf tsekanqedd
     1501 ipvkgshstk veavvrtlmk iqlkdpgaka lvfstwqdvl diiskaltdn nmgftqisri
     1561 ktfqenlsaf kydpqinill lplhtgsngl tiieathvll vepilnpahe lqaigrvhri
     1621 gqtkptivhr flikatieer mqamlktaer shtsssgkhs easaltvadl adlftkesee
     1681 le
//
LOCUS       NP_036651                533 aa            linear   ROD 13-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_036651
VERSION     NP_036651.1
DBSOURCE    REFSEQ: accession NM_012519.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Arias-Chavez,D.J., Mailloux-Salinas,P., Altamirano,J., Huang,F.,
            Gomez-Viquez,N.L. and Bravo,G.
  TITLE     Consumption of combined fructose and sucrose diet exacerbates
            oxidative stress, hypertrophy and CaMKIIdelta oxidation in hearts
            from rats with metabolic syndrome
  JOURNAL   Mol Cell Biochem 477 (4), 1309-1320 (2022)
   PUBMED   35138512
  REMARK    GeneRIF: Consumption of combined fructose and sucrose diet
            exacerbates oxidative stress, hypertrophy and CaMKIIdelta oxidation
            in hearts from rats with metabolic syndrome.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Carlson,C.R., Aronsen,J.M., Bergan-Dahl,A., Moutty,M.C., Lunde,M.,
            Lunde,P.K., Jarstadmarken,H., Wanichawan,P., Pereira,L.,
            Kolstad,T.R.S., Dalhus,B., Subramanian,H., Hille,S.,
            Christensen,G., Muller,O.J., Nikolaev,V., Bers,D.M., Sjaastad,I.,
            Shen,X., Louch,W.E., Klussmann,E. and Sejersted,O.M.
  TITLE     AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR
  JOURNAL   Circ Res 130 (1), 27-44 (2022)
   PUBMED   34814703
  REMARK    GeneRIF: AKAP18delta Anchors and Regulates CaMKII Activity at
            Phospholamban-SERCA2 and RYR.
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Tian,T., Yao,D., Zheng,L., Zhou,Z., Duan,Y., Liu,B., Wang,P. and
            Li,Y.
  TITLE     Sphingosine kinase 1 regulates HMGB1 translocation by directly
            interacting with calcium/calmodulin protein kinase II-delta in
            sepsis-associated liver injury
  JOURNAL   Cell Death Dis 11 (12), 1037 (2020)
   PUBMED   33281190
  REMARK    GeneRIF: Sphingosine kinase 1 regulates HMGB1 translocation by
            directly interacting with calcium/calmodulin protein kinase
            II-delta in sepsis-associated liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Zhang,M., Yang,X., Zimmerman,R.J., Wang,Q., Ross,M.A.,
            Granger,J.M., Luczak,E.D., Bedja,D., Jiang,H. and Feng,N.
  TITLE     CaMKII exacerbates heart failure progression by activating class I
            HDACs
  JOURNAL   J Mol Cell Cardiol 149, 73-81 (2020)
   PUBMED   32971072
  REMARK    GeneRIF: CaMKII exacerbates heart failure progression by activating
            class I HDACs.
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Chen,C.H., Lin,J.W., Huang,C.Y., Yeh,Y.L., Shen,C.Y.,
            Badrealam,K.F., Ho,T.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy
  JOURNAL   J Cell Physiol 235 (4), 3539-3547 (2020)
   PUBMED   31584202
  REMARK    GeneRIF: The combined inhibition of the CaMKIIdelta and calcineurin
            signaling cascade attenuates IGF-IIR-induced cardiac hypertrophy.
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Deng,A.Y., Dene,H. and Rapp,J.P.
  TITLE     Mapping of a quantitative trait locus for blood pressure on rat
            chromosome 2
  JOURNAL   J Clin Invest 94 (1), 431-436 (1994)
   PUBMED   8040284
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Edman,C.F. and Schulman,H.
  TITLE     Identification and characterization of delta B-CaM kinase and delta
            C-CaM kinase from rat heart, two new multifunctional
            Ca2+/calmodulin-dependent protein kinase isoforms
  JOURNAL   Biochim Biophys Acta 1221 (1), 89-101 (1994)
   PUBMED   8130281
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Mayer,P., Mohlig,M., Schatz,H. and Pfeiffer,A.
  TITLE     New isoforms of multifunctional calcium/calmodulin-dependent
            protein kinase II
  JOURNAL   FEBS Lett 333 (3), 315-318 (1993)
   PUBMED   8224201
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Schworer,C.M., Rothblum,L.I., Thekkumkara,T.J. and Singer,H.A.
  TITLE     Identification of novel isoforms of the delta subunit of
            Ca2+/calmodulin-dependent protein kinase II. Differential
            expression in rat brain and aorta
  JOURNAL   J Biol Chem 268 (19), 14443-14449 (1993)
   PUBMED   8390994
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Tobimatsu,T. and Fujisawa,H.
  TITLE     Tissue-specific expression of four types of rat
            calmodulin-dependent protein kinase II mRNAs
  JOURNAL   J Biol Chem 264 (30), 17907-17912 (1989)
   PUBMED   2553697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1621941.1,
                                           SRR26360176.555331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     delta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit delta; caMK-II subunit delta; caM-kinase
                     II delta chain; caM kinase II subunit delta;
                     Ca++/calmodulin-dependent protein kinase II, delta
                     subunit; calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; Ca++/calmodulin-dependent protein kinase
                     2 delta subunit"
                     /calculated_mol_wt=59950
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          337..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15791.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13557; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (P15791.1)"
     CDS             1..533
                     /gene="Camk2d"
                     /gene_synonym="CAMK1; Camk2; Camki; RATCAMKI"
                     /coded_by="NM_012519.3:417..2018"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24246"
                     /db_xref="RGD:2263"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalpki nkpihtiiln phvhlvgdda aciayirltq ymdgngmpkt
      481 mqseetrvwh rrdgkwqnih fhrsgsptvp ikppcipngk enfsggtslw qni
//
LOCUS       NP_001102034            1532 aa            linear   ROD 14-APR-2025
DEFINITION  glycogen debranching enzyme [Rattus norvegicus].
ACCESSION   NP_001102034 XP_001073642 XP_342332
VERSION     NP_001102034.1
DBSOURCE    REFSEQ: accession NM_001108564.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1532)
  AUTHORS   Cheng,A., Zhang,M., Gentry,M.S., Worby,C.A., Dixon,J.E. and
            Saltiel,A.R.
  TITLE     A role for AGL ubiquitination in the glycogen storage disorders of
            Lafora and Cori's disease
  JOURNAL   Genes Dev 21 (19), 2399-2409 (2007)
   PUBMED   17908927
REFERENCE   2  (residues 1 to 1532)
  AUTHORS   Lucchiari,S., Pagliarani,S., Salani,S., Filocamo,M., Di Rocco,M.,
            Melis,D., Rodolico,C., Musumeci,O., Toscano,A., Bresolin,N. and
            Comi,G.P.
  TITLE     Hepatic and neuromuscular forms of glycogenosis type III: nine
            mutations in AGL
  JOURNAL   Hum Mutat 27 (6), 600-601 (2006)
   PUBMED   16705713
REFERENCE   3  (residues 1 to 1532)
  AUTHORS   Lees,S.J., Chen,Y.T. and Williams,J.H.
  TITLE     Glycogen debranching enzyme is associated with rat skeletal muscle
            sarcoplasmic reticulum
  JOURNAL   Acta Physiol Scand 181 (2), 239-245 (2004)
   PUBMED   15180797
REFERENCE   4  (residues 1 to 1532)
  AUTHORS   Becker,K.G., Barnes,K.C., Bright,T.J. and Wang,S.A.
  TITLE     The genetic association database
  JOURNAL   Nat Genet 36 (5), 431-432 (2004)
   PUBMED   15118671
REFERENCE   5  (residues 1 to 1532)
  AUTHORS   Schliselfeld,L.H. and Danon,M.J.
  TITLE     Inverse relationship of skeletal muscle glycogen from wild-type and
            genetically modified mice to their phosphorylase a activity
  JOURNAL   Biochem Biophys Res Commun 290 (2), 874-877 (2002)
   PUBMED   11785984
REFERENCE   6  (residues 1 to 1532)
  AUTHORS   Popova,I.A., Presnova,V.N. and Lavrenova,T.P.
  TITLE     [Effect of biogenic amines on glycogen degradation in isolated rat
            hepatocytes]
  JOURNAL   Vopr Med Khim 38 (2), 30-33 (1992)
   PUBMED   1413626
REFERENCE   7  (residues 1 to 1532)
  AUTHORS   Chen,Y.T., He,J.K., Ding,J.H. and Brown,B.I.
  TITLE     Glycogen debranching enzyme: purification, antibody
            characterization, and immunoblot analyses of type III glycogen
            storage disease
  JOURNAL   Am J Hum Genet 41 (6), 1002-1015 (1987)
   PUBMED   2961257
REFERENCE   8  (residues 1 to 1532)
  AUTHORS   Satoh,K. and Sato,K.
  TITLE     Glycogen-binding protein components of rat tissues
  JOURNAL   Biochem Biophys Res Commun 96 (1), 28-33 (1980)
   PUBMED   6449198
REFERENCE   9  (residues 1 to 1532)
  AUTHORS   Vaillant,R., Bourgeois-Victor,P. and Fairand,A.
  TITLE     [Development and control of liver amylo-1,6-glucosidase activity in
            the fetal rat]
  JOURNAL   Can J Biochem 57 (10), 1245-1249 (1979)
   PUBMED   120213
REFERENCE   10 (residues 1 to 1532)
  AUTHORS   Mannan,A., Noujaim,A.A., Wiebe,L.I., Secord,D.C. and
            Silverberg,D.S.
  TITLE     Carbohydrate metabolism in the chronically uremic rat
  JOURNAL   Clin Biochem 8 (3), 194-198 (1975)
   PUBMED   807434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473952.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342332.3, XP_001073642.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1532
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..1532
                     /product="glycogen debranching enzyme"
                     /note="amylo-1, 6-glucosidase, 4-alpha-glucanotransferase
                     (glycogen debranching enzyme, glycogen storage disease
                     type III); amylo-1,6-glucosidase,
                     4-alpha-glucanotransferase; amylo-alpha-1, 6-glucosidase,
                     4-alpha-glucanotransferase"
                     /calculated_mol_wt=174202
     Region          22..1532
                     /region_name="glyc_debranch"
                     /note="glycogen debranching enzymye; TIGR01531"
                     /db_xref="CDD:273673"
     CDS             1..1532
                     /gene="Agl"
                     /coded_by="NM_001108564.1:544..5142"
                     /db_xref="GeneID:362029"
                     /db_xref="RGD:1306376"
ORIGIN      
        1 mehskqiril llnemeklek tlfrleqgfe lqfrlgptlq gkavtvytny pfpgeafnre
       61 kfrsldwenp tereddsdky ckvhlqqsgs fqyyflqgqe ksgggyivvd pilrvgadnh
      121 vlpldcvtlq tflakclgpf dewesrlrva kesgynmihf tplqalglsr scysladqle
      181 lnpdfsrpnr rytwddvgql veklkrewni lcitdvvynh taanskwihe hpesaynlvn
      241 sphlkpawvl dralwhlscd vadgkyrekg vpaliendhh mncirkiiwe difpriqlwe
      301 ffqvdvqkav eqfrrllsqe nrrvtksepk ehlkiiqdpe frrlgcavdm nialatfiph
      361 dngpaaieec cnwfrkrlee lnsekhhlts chqeqavncl lgnvfyerla ghgpklgpvt
      421 rkyplvtryf tfpfeemals aeesllhrpd kacflmahng wvmgddplrn faepgsnvyl
      481 rrelicwgds vklrygnkpe dcpylwahmk kyteitathf qgvrldnchs tplhvaeyml
      541 daarklqpnl yvvaelftgs edldnifvtr lgisslirea msaynsheeg rlvyryggep
      601 vgsfvqpclr plmpaiahal fmdithdnec pivhrsayda lpsttvvsma ccasgstrgy
      661 delvphqisv vaeerfytkw npgaspsdtg dvsihsgiia arcainrlhq elgakgfiqv
      721 yvdqvdediv avtrhspsih qsvvavsrta frnpktsfys kevpqmcipg kieevvlear
      781 tierntkpyr kdensingmp nmtvelreri qlheskivkq agvatkgpne yiqeiefenl
      841 spgsviifrv sldphaqvav gilrnhltqf sshfksgsla vdnsdpilki pfasiasklt
      901 laelnqvlyr ceseeqedgg gcydipnwss lkyaglqglm svlaeirpkn dlghpfcenl
      961 rsgdwmidyv sgrlisrsgs iaevgkwlqa mffylkqipr ylipcyfdai ligayttlld
     1021 vawkqmssfv qngstfvkhl slgsvqmcgv gkcpclplls pslldvpcrl neitkekeqc
     1081 caslaaglph fssglfrcwg rdtfialrgm llvtgrylea rniilafact lrhglipnll
     1141 gegtyarync rdavwwwlqc iqdyckmvpn gldilkcpvs rmyptddsap lpagtldqpl
     1201 feviqeamqr hmqgiqfrer nagpqidrnm kdegfnitvg vdeetgfvyg gnrfncgtwm
     1261 dkmgesdrar nrgipatprd gsaveivglc ksavrwllel skknifpyhe vrvrrhgkvv
     1321 avsydewnrk iqnsfeklfh vsedpsdpne khpnlvhkrg iykdsygass pwcdyqlrpn
     1381 ftiamvvape lftaekawka leiaegkllg plgmktldpd dmvycgvydn aldndnynla
     1441 rgfnyhqgpe wlwpigyflr aklyfskmmg petaaktvfl vknvlsrhyv hlerspwkgl
     1501 peltnengqy cpfscetqaw smaavletly dl
//
LOCUS       NP_001424913             346 aa            linear   ROD 14-APR-2025
DEFINITION  cyclin-dependent kinase 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424913 XP_006240840
VERSION     NP_001424913.1
DBSOURCE    REFSEQ: accession NM_001437984.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Matveevsky,S., Chassovnikarova,T., Grishaeva,T., Atsaeva,M.,
            Malygin,V., Bakloushinskaya,I. and Kolomiets,O.
  TITLE     Kinase CDK2 in Mammalian Meiotic Prophase I: Screening for Hetero-
            and Homomorphic Sex Chromosomes
  JOURNAL   Int J Mol Sci 22 (4), 1969 (2021)
   PUBMED   33671248
  REMARK    GeneRIF: Kinase CDK2 in Mammalian Meiotic Prophase I: Screening for
            Hetero- and Homomorphic Sex Chromosomes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Peng,T., Peng,J.J., Miao,G.Y., Tan,Z.Q., Liu,B. and Zhou,E.
  TITLE     miR-125/CDK2 axis in cochlear progenitor cell proliferation
  JOURNAL   Mol Med Rep 23 (2) (2021)
   PUBMED   33300064
  REMARK    GeneRIF: miR125/CDK2 axis in cochlear progenitor cell
            proliferation.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Ren,S., Xing,Y., Wang,C., Jiang,F., Liu,G., Li,Z., Jiang,T., Zhu,Y.
            and Piao,D.
  TITLE     Fraxetin inhibits the growth of colon adenocarcinoma cells via the
            Janus kinase 2/signal transducer and activator of transcription 3
            signalling pathway
  JOURNAL   Int J Biochem Cell Biol 125, 105777 (2020)
   PUBMED   32504672
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Lin,Z., Liu,Z., Wang,X., Qiu,C. and Zheng,S.
  TITLE     MiR-21-3p Plays a Crucial Role in Metabolism Alteration of Renal
            Tubular Epithelial Cells during Sepsis Associated Acute Kidney
            Injury via AKT/CDK2-FOXO1 Pathway
  JOURNAL   Biomed Res Int 2019, 2821731 (2019)
   PUBMED   31223614
  REMARK    GeneRIF: MiR-21-3p mediates metabolism and cell fate alterations of
            tubular epithelial cells (TECs) via manipulating AKT/CDK2-FOXO1
            pathway, and that is crucial in the regulation of energy metabolism
            of TECs during Sepsis and associated acute kidney injury.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Beijersbergen,R.L., Carlee,L., Kerkhoven,R.M. and Bernards,R.
  TITLE     Regulation of the retinoblastoma protein-related p107 by G1 cyclin
            complexes
  JOURNAL   Genes Dev 9 (11), 1340-1353 (1995)
   PUBMED   7797074
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Hirai,H., Roussel,M.F., Kato,J.Y., Ashmun,R.A. and Sherr,C.J.
  TITLE     Novel INK4 proteins, p19 and p18, are specific inhibitors of the
            cyclin D-dependent kinases CDK4 and CDK6
  JOURNAL   Mol Cell Biol 15 (5), 2672-2681 (1995)
   PUBMED   7739547
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Kotani,S., Endo,T., Kitagawa,M., Higashi,H. and Onaya,T.
  TITLE     A variant form of cyclin-dependent kinase 2 (Cdk2) in a malignantly
            transformed rat thyroid (FRTL-Tc) cell line
  JOURNAL   Oncogene 10 (4), 663-669 (1995)
   PUBMED   7862443
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Tsai,L.H., Harlow,E. and Meyerson,M.
  TITLE     Isolation of the human cdk2 gene that encodes the cyclin A- and
            adenovirus E1A-associated p33 kinase
  JOURNAL   Nature 353 (6340), 174-177 (1991)
   PUBMED   1653904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240840.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FO803815.1, FO806392.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..346
                     /product="cyclin-dependent kinase 2 isoform 2"
                     /EC_number="2.7.11.22"
                     /note="cell division protein kinase 2; cyclin dependent
                     kinase 2-alpha"
                     /calculated_mol_wt=38903
     Region          3..334
                     /region_name="STKc_CDK2_3"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Cyclin-Dependent protein Kinase 2 and 3; cd07860"
                     /db_xref="CDD:270844"
     Site            order(10..13,18,31,33,50,64,80..83,86,88..89,127,129,
                     131..132,134,145,148,160,162..165,167,253..254)
                     /site_type="active"
                     /db_xref="CDD:270844"
     Site            order(10..13,18,31,33,64,80..83,86,89,131..132,134,145)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270844"
     Site            order(37,41..44,46,49..50,52..53,56..57,71..73,116,
                     119..122,150..152,154..155,157..160,320,324..326)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270844"
     Site            order(50,88,127,129,148,160,162..165,167,253..254)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270844"
     Site            144..167
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270844"
     CDS             1..346
                     /gene="Cdk2"
                     /coded_by="NM_001437984.1:190..1230"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362817"
                     /db_xref="RGD:70486"
ORIGIN      
        1 menfqkveki gegtygvvyk aknkltgevv alkkirldte tegvpstair eisllkelnh
       61 pnivklldvi htenklylvf eflhqdlkkf mdasaltgip lpliksylfq llqglafchs
      121 hrvlhrdlkp qnllinaegs ikladfglar afgvpvrtyt hevvtlwyra peillgckyy
      181 stavdiwslg cifaemhlvc tqhhakccge hrrngrhslc plcsylevaa sqgggmtavs
      241 tpypvtrral fpgdseidql frifrtlgtp devvwpgvts mpdykpsfpk warqdfskvv
      301 ppldedgrsl lsqmlhydpn krisakaala hpffqdvtkp vphlrl
//
LOCUS       NP_001178705             246 aa            linear   ROD 14-APR-2025
DEFINITION  caspase-14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001178705 XP_063119230 XP_234878
VERSION     NP_001178705.1
DBSOURCE    REFSEQ: accession NM_001191776.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Gkegkes,I.D., Aroni,K., Agrogiannis,G., Patsouris,E.S. and
            Konstantinidou,A.E.
  TITLE     Expression of caspase-14 and keratin-19 in the human epidermis and
            appendages during fetal skin development
  JOURNAL   Arch Dermatol Res 305 (5), 379-387 (2013)
   PUBMED   23377137
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Alibardi,L., Tschachler,E. and Eckhart,L.
  TITLE     Distribution of caspase-14 in epidermis and hair follicles is
            evolutionarily conserved among mammals
  JOURNAL   Anat Rec A Discov Mol Cell Evol Biol 286 (2), 962-973 (2005)
   PUBMED   16142807
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_063119230.1, XP_234878.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.27728.1,
                                           SRR26643295.27356.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..246
                     /product="caspase-14 isoform 2"
                     /calculated_mol_wt=28124
     Region          10..246
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cd00032"
                     /db_xref="CDD:237997"
     Site            order(33,94,134,141,180..185,189..190)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(93,136)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(142,165..166,173,176,179,203,211,217,230,235..236,
                     238,241..242)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(143,164)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     CDS             1..246
                     /gene="Casp14"
                     /coded_by="NM_001191776.2:181..921"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:299587"
                     /db_xref="RGD:1311781"
ORIGIN      
        1 mdsetinpqp lqeerydmsg arlaltlcvt karegsevdm dalermfqyl kfestmkrdp
       61 taqqflddmd efqqtienwk epvscafvvl mahgeegflk gedgnmvrle dlfevlnnkn
      121 ckalrgkpkv yiiqacrgeh rdpgeelpgd elavikkknp ptiptytdmi hiystvegfl
      181 syrhdqkgsg fiqtltdvfi hkkgsitell eeitrlmant evmqegkprk vnpeiqstlr
      241 kklylq
//
LOCUS       NP_001127936             126 aa            linear   ROD 14-APR-2025
DEFINITION  protein LLP homolog [Rattus norvegicus].
ACCESSION   NP_001127936 XP_001081031 XP_006241487 XP_216898
VERSION     NP_001127936.1
DBSOURCE    REFSEQ: accession NM_001134464.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Yu,N.K., Kim,H.F., Shim,J., Kim,S., Kim,D.W., Kwak,C., Sim,S.E.,
            Choi,J.H., Ahn,S., Yoo,J., Choi,S.L., Jang,D.J., Lim,C.S.,
            Lee,Y.S., Kang,C., Choi,S.Y. and Kaang,B.K.
  TITLE     A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
            morphogenesis and synaptic transmission
  JOURNAL   Sci Rep 6, 22892 (2016)
   PUBMED   26961175
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_006241487.1, XP_001081031.1, XP_216898.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.19643.1,
                                           SRR26643285.27597.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..126
                     /product="protein LLP homolog"
                     /note="LLP homolog, long-term synaptic facilitation
                     (Aplysia)"
                     /calculated_mol_wt=14802
     Region          3..117
                     /region_name="Laps"
                     /note="Learning-associated protein; pfam10169"
                     /db_xref="CDD:462976"
     CDS             1..126
                     /gene="Llph"
                     /gene_synonym="RGD1308261"
                     /coded_by="NM_001134464.3:66..446"
                     /db_xref="GeneID:299818"
                     /db_xref="RGD:1308261"
ORIGIN      
        1 makslrskwk rkmraekrkk naprelnrlk silkvdgdal mkdveeiatv vvpkhyqekm
       61 qcdvavddek ddmkmeteik rnkktlldqh gqypvwmnqr qrkrlkakre kkrgkskaka
      121 akglaw
//
LOCUS       NP_001424901             298 aa            linear   ROD 14-APR-2025
DEFINITION  AP-1 complex-associated regulatory protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424901 XP_006233353
VERSION     NP_001424901.1
DBSOURCE    REFSEQ: accession NM_001437972.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maritzen,T., Zech,T., Schmidt,M.R., Krause,E., Machesky,L.M. and
            Haucke,V.
  TITLE     Gadkin negatively regulates cell spreading and motility via
            sequestration of the actin-nucleating ARP2/3 complex
  JOURNAL   Proc Natl Acad Sci U S A 109 (26), 10382-10387 (2012)
   PUBMED   22689987
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schmidt,M.R., Maritzen,T., Kukhtina,V., Higman,V.A., Doglio,L.,
            Barak,N.N., Strauss,H., Oschkinat,H., Dotti,C.G. and Haucke,V.
  TITLE     Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin
            KIF5 complex
  JOURNAL   Proc Natl Acad Sci U S A 106 (36), 15344-15349 (2009)
   PUBMED   19706427
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006233353.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1172135.1,
                                           SRR26360181.1980335.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..298
                     /product="AP-1 complex-associated regulatory protein
                     isoform 1"
                     /note="AP-1 complex-associated regulatory protein"
                     /calculated_mol_wt=33605
     Region          24..298
                     /region_name="AP1AR"
                     /note="AP-1 complex-associated regulatory protein;
                     pfam15745"
                     /db_xref="CDD:464841"
     CDS             1..298
                     /gene="Ap1ar"
                     /gene_synonym="RGD1311435"
                     /coded_by="NM_001437972.1:220..1116"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362037"
                     /db_xref="RGD:1311435"
ORIGIN      
        1 mgnccwtqcf gllrreagrl qragggskyf rtcprgehlt iefenlvesd egespgsshr
       61 plteeeivdl qerhydsiae kqkdvdrkiq relalqeekl rleeealyaa qreaaraarq
      121 rklleqekqr iaqryhpssg dcqsvgpedd feaslrniks qyevfrssrl ssdatvltpn
      181 tesscdlmtk tkstsgndds tsldlewede egmnrmlpmr erskteedil raalkcsskk
      241 gsnptsasdd snglewendf vsaemddngn seyagfvnpv lelsesaikq sdtdqqir
//
LOCUS       NP_001424890             462 aa            linear   ROD 14-APR-2025
DEFINITION  midnolin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424890 XP_006240976
VERSION     NP_001424890.1
DBSOURCE    REFSEQ: accession NM_001437961.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Obara,Y. and Ishii,K.
  TITLE     Transcriptome Analysis Reveals That Midnolin Regulates mRNA
            Expression Levels of Multiple Parkinson's Disease Causative Genes
  JOURNAL   Biol Pharm Bull 41 (1), 20-23 (2018)
   PUBMED   29311479
  REMARK    GeneRIF: These findings indicate that MIDN regulates the expression
            of a wide variety of genes, including multiple Parkinson's Disease
            causative genes and is associated with Parkinson's Disease onset.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Obara,Y., Imai,T., Sato,H., Takeda,Y., Kato,T. and Ishii,K.
  TITLE     Midnolin is a novel regulator of parkin expression and is
            associated with Parkinson's Disease
  JOURNAL   Sci Rep 7 (1), 5885 (2017)
   PUBMED   28724963
  REMARK    GeneRIF: MIDN promotes the expression of parkin E3 ubiquitin
            ligase, and that MIDN loss can trigger Parkinson's disease-related
            pathogenic mechanisms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Hofmeister-Brix,A., Kollmann,K., Langer,S., Schultz,J., Lenzen,S.
            and Baltrusch,S.
  TITLE     Identification of the ubiquitin-like domain of midnolin as a new
            glucokinase interaction partner
  JOURNAL   J Biol Chem 288 (50), 35824-35839 (2013)
   PUBMED   24187134
  REMARK    GeneRIF: midnolin plays a role in cellular signaling of adult
            tissues and regulates glucokinase enzyme activity in pancreatic
            beta cells
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Tsukahara,M., Suemori,H., Noguchi,S., Ji,Z.S. and Tsunoo,H.
  TITLE     Novel nucleolar protein, midnolin, is expressed in the
            mesencephalon during mouse development
  JOURNAL   Gene 254 (1-2), 45-55 (2000)
   PUBMED   10974535
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240976.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.24424.1,
                                           SRR26643296.19074.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN09345330,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..462
                     /product="midnolin isoform 1"
                     /note="midbrain nucleolar protein"
                     /calculated_mol_wt=48800
     Region          32..101
                     /region_name="Ubl_midnolin"
                     /note="ubiquitin-like (Ubl) domain found in midnolin and
                     similar proteins; cd01804"
                     /db_xref="CDD:340502"
     CDS             1..462
                     /gene="Midn"
                     /coded_by="NM_001437961.1:475..1863"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314623"
                     /db_xref="RGD:1309629"
ORIGIN      
        1 mepqpggars crrgapggac elsttaesaa pmslaihstt gtrydlsvph detveglrkr
       61 lsqrlkvpke rlallhkdtr lssgklqefg vgdgskltlv ptveaglmsq asrpeqsvmq
      121 alesltetqv sdflsgrspl tlalrvgdhm mfvqlqlaaq haplqhrhvl aaaaaaaaaa
      181 rgdssiatpv sspcrpvssa arvppvsssp sspvspspvt agtfqshaas ttcpeqtdcs
      241 ppassnttst pgssptprsr kpgaviesfv nhapgvfsgt fsgtlhpncq dssgrprrdi
      301 gtilqilndl lsatrhyqgm pasltqlrch aqcspaspap dltpkttsce klatpsllqg
      361 qsqirmckpp gdrlrqtenr atrckverlq lllqqkrlrr karrdargpy hwtpsrkagr
      421 sdssssgggg spseatglgl dfedsvwkpe vnpdiqsefv va
//
LOCUS       NP_001424897             559 aa            linear   ROD 14-APR-2025
DEFINITION  protein LYRIC isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424897 XP_006241585
VERSION     NP_001424897.1
DBSOURCE    REFSEQ: accession NM_001437968.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Xiang,Y., Duan,Y., Peng,Z., Huang,H., Ding,W., Chen,E., Liu,Z.,
            Dou,C., Li,J., Ou,J., Wan,Q., Yang,B. and He,Z.
  TITLE     Microparticles from Hyperphosphatemia-Stimulated Endothelial Cells
            Promote Vascular Calcification Through Astrocyte-Elevated Gene-1
  JOURNAL   Calcif Tissue Int 111 (1), 73-86 (2022)
   PUBMED   35195734
  REMARK    GeneRIF: Microparticles from Hyperphosphatemia-Stimulated
            Endothelial Cells Promote Vascular Calcification Through
            Astrocyte-Elevated Gene-1.
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Wang,Y., Zhang,W., Zhu,X., Wang,Y., Mao,X., Xu,X. and Wang,Y.
  TITLE     Upregulation of AEG-1 Involves in Schwann Cell Proliferation and
            Migration After Sciatic Nerve Crush
  JOURNAL   J Mol Neurosci 60 (2), 248-257 (2016)
   PUBMED   27351433
  REMARK    GeneRIF: AEG-1 was expressed mainly in Schwann cells of the distal
            sciatic nerve segment from injury.  Interference of AEG-1 inhibited
            both proliferation and migration of Schwann cells.
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Watanabe,A., Tatematsu,M., Saeki,K., Shibata,S., Shime,H.,
            Yoshimura,A., Obuse,C., Seya,T. and Matsumoto,M.
  TITLE     Raftlin is involved in the nucleocapture complex to induce
            poly(I:C)-mediated TLR3 activation
  JOURNAL   J Biol Chem 286 (12), 10702-10711 (2011)
   PUBMED   21266579
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Emdad,L., Sarkar,D., Su,Z.Z., Randolph,A., Boukerche,H., Valerie,K.
            and Fisher,P.B.
  TITLE     Activation of the nuclear factor kappaB pathway by astrocyte
            elevated gene-1: implications for tumor progression and metastasis
  JOURNAL   Cancer Res 66 (3), 1509-1516 (2006)
   PUBMED   16452207
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Kang,D.C., Su,Z.Z., Sarkar,D., Emdad,L., Volsky,D.J. and
            Fisher,P.B.
  TITLE     Cloning and characterization of HIV-1-inducible astrocyte elevated
            gene-1, AEG-1
  JOURNAL   Gene 353 (1), 8-15 (2005)
   PUBMED   15927426
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Britt,D.E., Yang,D.F., Yang,D.Q., Flanagan,D., Callanan,H.,
            Lim,Y.P., Lin,S.H. and Hixson,D.C.
  TITLE     Identification of a novel protein, LYRIC, localized to tight
            junctions of polarized epithelial cells
  JOURNAL   Exp Cell Res 300 (1), 134-148 (2004)
   PUBMED   15383321
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Sutherland,H.G., Lam,Y.W., Briers,S., Lamond,A.I. and Bickmore,W.A.
  TITLE     3D3/lyric: a novel transmembrane protein of the endoplasmic
            reticulum and nuclear envelope, which is also present in the
            nucleolus
  JOURNAL   Exp Cell Res 294 (1), 94-105 (2004)
   PUBMED   14980505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006241585.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.29757.1,
                                           SRR26360186.2146692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..559
                     /product="protein LYRIC isoform 2"
                     /note="protein LYRIC; lysine-rich CEACAM1 co-isolated
                     protein; metastasis adhesion protein"
                     /calculated_mol_wt=61538
     Region          6..400
                     /region_name="LYRIC"
                     /note="Lysine-rich CEACAM1 co-isolated protein family;
                     pfam15686"
                     /db_xref="CDD:434858"
     CDS             1..559
                     /gene="Mtdh"
                     /gene_synonym="Lyric"
                     /coded_by="NM_001437968.1:320..1999"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:170910"
                     /db_xref="RGD:620992"
ORIGIN      
        1 maarswqdel aqqaeegsar lrellsvglg flrtelgldl glepkrypsw vilvgtgalg
       61 llllfllgyg waaacagark krrspprkre evtpptpape dpaqlknlrs eeqkkknrkk
      121 lpekpkpngr tveipedevv rtprsitakq ppetdkknek skknkkksks dakavqnssr
      181 hdgkevdega wetkishrek rqqrkrdkvl tdsgsldsti pgientitvt teqlttasfp
      241 vgskknkvss glnenitvng ggwseksvkl ssqlsageek wnsvppasag krkteqsawt
      301 qdpgdtnang kdwgrnwsdr sifsgigsta epvsqsttsd yqwdgsrnqp hiddewsgln
      361 glssadpssd wnapaeewgn wvdedrasll ksqepisndq kdsdddkekg egalptgksk
      421 kkkkkkkkqg ednsitqdte dlekdtreel pvntskarpk qekacslktm stsdpvevli
      481 knsqpiktlp paisaepsvt lskgdsdkss sqvppmlqdt dkpksnakqn svppsqtkse
      541 tnwespkqik kkkkarret
//
LOCUS       NP_001424896            1532 aa            linear   ROD 14-APR-2025
DEFINITION  glycogen debranching enzyme [Rattus norvegicus].
ACCESSION   NP_001424896 XP_006233291
VERSION     NP_001424896.1
DBSOURCE    REFSEQ: accession NM_001437967.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1532)
  AUTHORS   Cheng,A., Zhang,M., Gentry,M.S., Worby,C.A., Dixon,J.E. and
            Saltiel,A.R.
  TITLE     A role for AGL ubiquitination in the glycogen storage disorders of
            Lafora and Cori's disease
  JOURNAL   Genes Dev 21 (19), 2399-2409 (2007)
   PUBMED   17908927
REFERENCE   2  (residues 1 to 1532)
  AUTHORS   Lucchiari,S., Pagliarani,S., Salani,S., Filocamo,M., Di Rocco,M.,
            Melis,D., Rodolico,C., Musumeci,O., Toscano,A., Bresolin,N. and
            Comi,G.P.
  TITLE     Hepatic and neuromuscular forms of glycogenosis type III: nine
            mutations in AGL
  JOURNAL   Hum Mutat 27 (6), 600-601 (2006)
   PUBMED   16705713
REFERENCE   3  (residues 1 to 1532)
  AUTHORS   Lees,S.J., Chen,Y.T. and Williams,J.H.
  TITLE     Glycogen debranching enzyme is associated with rat skeletal muscle
            sarcoplasmic reticulum
  JOURNAL   Acta Physiol Scand 181 (2), 239-245 (2004)
   PUBMED   15180797
REFERENCE   4  (residues 1 to 1532)
  AUTHORS   Becker,K.G., Barnes,K.C., Bright,T.J. and Wang,S.A.
  TITLE     The genetic association database
  JOURNAL   Nat Genet 36 (5), 431-432 (2004)
   PUBMED   15118671
REFERENCE   5  (residues 1 to 1532)
  AUTHORS   Schliselfeld,L.H. and Danon,M.J.
  TITLE     Inverse relationship of skeletal muscle glycogen from wild-type and
            genetically modified mice to their phosphorylase a activity
  JOURNAL   Biochem Biophys Res Commun 290 (2), 874-877 (2002)
   PUBMED   11785984
REFERENCE   6  (residues 1 to 1532)
  AUTHORS   Popova,I.A., Presnova,V.N. and Lavrenova,T.P.
  TITLE     [Effect of biogenic amines on glycogen degradation in isolated rat
            hepatocytes]
  JOURNAL   Vopr Med Khim 38 (2), 30-33 (1992)
   PUBMED   1413626
REFERENCE   7  (residues 1 to 1532)
  AUTHORS   Chen,Y.T., He,J.K., Ding,J.H. and Brown,B.I.
  TITLE     Glycogen debranching enzyme: purification, antibody
            characterization, and immunoblot analyses of type III glycogen
            storage disease
  JOURNAL   Am J Hum Genet 41 (6), 1002-1015 (1987)
   PUBMED   2961257
REFERENCE   8  (residues 1 to 1532)
  AUTHORS   Satoh,K. and Sato,K.
  TITLE     Glycogen-binding protein components of rat tissues
  JOURNAL   Biochem Biophys Res Commun 96 (1), 28-33 (1980)
   PUBMED   6449198
REFERENCE   9  (residues 1 to 1532)
  AUTHORS   Vaillant,R., Bourgeois-Victor,P. and Fairand,A.
  TITLE     [Development and control of liver amylo-1,6-glucosidase activity in
            the fetal rat]
  JOURNAL   Can J Biochem 57 (10), 1245-1249 (1979)
   PUBMED   120213
REFERENCE   10 (residues 1 to 1532)
  AUTHORS   Mannan,A., Noujaim,A.A., Wiebe,L.I., Secord,D.C. and
            Silverberg,D.S.
  TITLE     Carbohydrate metabolism in the chronically uremic rat
  JOURNAL   Clin Biochem 8 (3), 194-198 (1975)
   PUBMED   807434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006233291.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.872952.1,
                                           SRR26360186.2660540.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1532
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..1532
                     /product="glycogen debranching enzyme"
                     /note="amylo-1, 6-glucosidase, 4-alpha-glucanotransferase
                     (glycogen debranching enzyme, glycogen storage disease
                     type III); amylo-1,6-glucosidase,
                     4-alpha-glucanotransferase; amylo-alpha-1, 6-glucosidase,
                     4-alpha-glucanotransferase"
                     /calculated_mol_wt=174202
     Region          22..1532
                     /region_name="glyc_debranch"
                     /note="glycogen debranching enzymye; TIGR01531"
                     /db_xref="CDD:273673"
     CDS             1..1532
                     /gene="Agl"
                     /coded_by="NM_001437967.1:111..4709"
                     /db_xref="GeneID:362029"
                     /db_xref="RGD:1306376"
ORIGIN      
        1 mehskqiril llnemeklek tlfrleqgfe lqfrlgptlq gkavtvytny pfpgeafnre
       61 kfrsldwenp tereddsdky ckvhlqqsgs fqyyflqgqe ksgggyivvd pilrvgadnh
      121 vlpldcvtlq tflakclgpf dewesrlrva kesgynmihf tplqalglsr scysladqle
      181 lnpdfsrpnr rytwddvgql veklkrewni lcitdvvynh taanskwihe hpesaynlvn
      241 sphlkpawvl dralwhlscd vadgkyrekg vpaliendhh mncirkiiwe difpriqlwe
      301 ffqvdvqkav eqfrrllsqe nrrvtksepk ehlkiiqdpe frrlgcavdm nialatfiph
      361 dngpaaieec cnwfrkrlee lnsekhhlts chqeqavncl lgnvfyerla ghgpklgpvt
      421 rkyplvtryf tfpfeemals aeesllhrpd kacflmahng wvmgddplrn faepgsnvyl
      481 rrelicwgds vklrygnkpe dcpylwahmk kyteitathf qgvrldnchs tplhvaeyml
      541 daarklqpnl yvvaelftgs edldnifvtr lgisslirea msaynsheeg rlvyryggep
      601 vgsfvqpclr plmpaiahal fmdithdnec pivhrsayda lpsttvvsma ccasgstrgy
      661 delvphqisv vaeerfytkw npgaspsdtg dvsihsgiia arcainrlhq elgakgfiqv
      721 yvdqvdediv avtrhspsih qsvvavsrta frnpktsfys kevpqmcipg kieevvlear
      781 tierntkpyr kdensingmp nmtvelreri qlheskivkq agvatkgpne yiqeiefenl
      841 spgsviifrv sldphaqvav gilrnhltqf sshfksgsla vdnsdpilki pfasiasklt
      901 laelnqvlyr ceseeqedgg gcydipnwss lkyaglqglm svlaeirpkn dlghpfcenl
      961 rsgdwmidyv sgrlisrsgs iaevgkwlqa mffylkqipr ylipcyfdai ligayttlld
     1021 vawkqmssfv qngstfvkhl slgsvqmcgv gkcpclplls pslldvpcrl neitkekeqc
     1081 caslaaglph fssglfrcwg rdtfialrgm llvtgrylea rniilafact lrhglipnll
     1141 gegtyarync rdavwwwlqc iqdyckmvpn gldilkcpvs rmyptddsap lpagtldqpl
     1201 feviqeamqr hmqgiqfrer nagpqidrnm kdegfnitvg vdeetgfvyg gnrfncgtwm
     1261 dkmgesdrar nrgipatprd gsaveivglc ksavrwllel skknifpyhe vrvrrhgkvv
     1321 avsydewnrk iqnsfeklfh vsedpsdpne khpnlvhkrg iykdsygass pwcdyqlrpn
     1381 ftiamvvape lftaekawka leiaegkllg plgmktldpd dmvycgvydn aldndnynla
     1441 rgfnyhqgpe wlwpigyflr aklyfskmmg petaaktvfl vknvlsrhyv hlerspwkgl
     1501 peltnengqy cpfscetqaw smaavletly dl
//
LOCUS       NP_001424847             530 aa            linear   ROD 14-APR-2025
DEFINITION  S-adenosylhomocysteine hydrolase-like protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424847 XP_008759627
VERSION     NP_001424847.1
DBSOURCE    REFSEQ: accession NM_001437918.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Harvey,K.E., LaVigne,E.K., Dar,M.S., Salyer,A.E., Pratt,E.P.S.,
            Sample,P.A., Aryal,U.K., Gowher,H. and Hockerman,G.H.
  TITLE     RyR2/IRBIT regulates insulin gene transcript, insulin content, and
            secretion in the insulinoma cell line INS-1
  JOURNAL   Sci Rep 12 (1), 7713 (2022)
   PUBMED   35562179
  REMARK    GeneRIF: RyR2/IRBIT regulates insulin gene transcript, insulin
            content, and secretion in the insulinoma cell line INS-1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Borth,H., Weber,N., Meyer,D., Wartenberg,A., Arlt,E., Zierler,S.,
            Breit,A., Wennemuth,G., Gudermann,T. and Boekhoff,I.
  TITLE     The IP3 R Binding Protein Released With Inositol
            1,4,5-Trisphosphate Is Expressed in Rodent Reproductive Tissue and
            Spermatozoa
  JOURNAL   J Cell Physiol 231 (5), 1114-1129 (2016)
   PUBMED   26439876
  REMARK    GeneRIF: The present study documents that IRBIT is expressed in
            Leydig and Sertoli cells.
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Ando,H., Hirose,M., Gainche,L., Kawaai,K., Bonneau,B., Ijuin,T.,
            Itoh,T., Takenawa,T. and Mikoshiba,K.
  TITLE     IRBIT Interacts with the Catalytic Core of Phosphatidylinositol
            Phosphate Kinase Type Ialpha and IIalpha through Conserved
            Catalytic Aspartate Residues
  JOURNAL   PLoS One 10 (10), e0141569 (2015)
   PUBMED   26509711
  REMARK    GeneRIF: IRBIT forms signaling complexes with PIPKIalpha and
            NBCe1-B, whose activity is regulated by PI(4,5)P2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Park,S., Shcheynikov,N., Hong,J.H., Zheng,C., Suh,S.H., Kawaai,K.,
            Ando,H., Mizutani,A., Abe,T., Kiyonari,H., Seki,G., Yule,D.,
            Mikoshiba,K. and Muallem,S.
  TITLE     Irbit mediates synergy between ca(2+) and cAMP signaling pathways
            during epithelial transport in mice
  JOURNAL   Gastroenterology 145 (1), 232-241 (2013)
   PUBMED   23542070
REFERENCE   5  (residues 1 to 530)
  AUTHORS   He,P., Klein,J. and Yun,C.C.
  TITLE     Activation of Na+/H+ exchanger NHE3 by angiotensin II is mediated
            by inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3 (IRBIT) and Ca2+/calmodulin-dependent protein
            kinase II
  JOURNAL   J Biol Chem 285 (36), 27869-27878 (2010)
   PUBMED   20584908
  REMARK    GeneRIF: IRBIT is critically involved in mediating activation of
            NHE3 by ANG II via a Ca(2+)/calmodulin-dependent protein kinases
            II-dependent pathway.
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Ando,H., Mizutani,A. and Mikoshiba,K.
  TITLE     An IRBIT homologue lacks binding activity to inositol
            1,4,5-trisphosphate receptor due to the unique N-terminal appendage
  JOURNAL   J Neurochem 109 (2), 539-550 (2009)
   PUBMED   19220705
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Yang,D., Shcheynikov,N., Zeng,W., Ohana,E., So,I., Ando,H.,
            Mizutani,A., Mikoshiba,K. and Muallem,S.
  TITLE     IRBIT coordinates epithelial fluid and HCO3- secretion by
            stimulating the transporters pNBC1 and CFTR in the murine
            pancreatic duct
  JOURNAL   J Clin Invest 119 (1), 193-202 (2009)
   PUBMED   19033647
REFERENCE   8  (residues 1 to 530)
  AUTHORS   He,P., Zhang,H. and Yun,C.C.
  TITLE     IRBIT, inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3
            activity in response to calcium
  JOURNAL   J Biol Chem 283 (48), 33544-33553 (2008)
   PUBMED   18829453
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Shirakabe,K., Priori,G., Yamada,H., Ando,H., Horita,S., Fujita,T.,
            Fujimoto,I., Mizutani,A., Seki,G. and Mikoshiba,K.
  TITLE     IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
            specifically binds to and activates pancreas-type Na+/HCO3-
            cotransporter 1 (pNBC1)
  JOURNAL   Proc Natl Acad Sci U S A 103 (25), 9542-9547 (2006)
   PUBMED   16769890
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Ando,H., Mizutani,A., Matsu-ura,T. and Mikoshiba,K.
  TITLE     IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
            protein, is released from the IP3 receptor upon IP3 binding to the
            receptor
  JOURNAL   J Biol Chem 278 (12), 10602-10612 (2003)
   PUBMED   12525476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_008759627.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.773629.1,
                                           SRR26360176.321956.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMN06621351 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..530
                     /product="S-adenosylhomocysteine hydrolase-like protein 1
                     isoform 2"
                     /EC_number="3.13.2.1"
                     /note="S-adenosylhomocysteine hydrolase-like 1; putative
                     adenosylhomocysteinase 2; adoHcyase 2;
                     S-adenosyl-L-homocysteine hydrolase 2;
                     S-adenosylhomocysteine hydrolase-like protein 1;
                     IP3R-binding protein released with inositol
                     1,4,5-trisphosphate"
                     /calculated_mol_wt=58821
     Region          106..529
                     /region_name="AdoHcyase"
                     /note="S-adenosyl-L-homocysteine hydrolase; smart00996"
                     /db_xref="CDD:214963"
     Site            order(115,118,122,125..126,260,263..264,280,282,286..287,
                     291,294..295,299,302..303,306..312,320..321,324,333..334,
                     336,341..349,351..354,356..359,362,375..379,389..391,402,
                     419..420,425,449,451,453..454,457,483,489..490,493..494,
                     497,500..501,503..505,507,510..511,514..515)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:240619"
     Site            order(153,155,157..158,229,254..255,284,288,445,450,455,
                     459)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240619"
     Site            order(255..257,289,293,318,320..322,340..343,346,373..376,
                     379,397..399,442,444,450)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240619"
     CDS             1..530
                     /gene="Ahcyl1"
                     /gene_synonym="IRBIT"
                     /coded_by="NM_001437918.1:288..1880"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362013"
                     /db_xref="RGD:1309768"
ORIGIN      
        1 msmpdamplp gvgeelkqak eiedaekysf matvtkapkk qiqfaddmqe ftkfptktgr
       61 rslsrsisqs stdsyssaas ytdssddevs prekqqtnsk gssnfcvkni kqaefgrrei
      121 eiaeqdmsal islrkraqge kplagakivg cthitaqtav lietlcalga qcrwsacniy
      181 stqnevaaal aeagvavfaw kgeseddfww cidrcvnmdg wqanmilddg gdlthwvykk
      241 ypnvfkkirg iveesvtgvh rlyqlskagk lcvpamnvnd svtkqkfdnl yccresildg
      301 lkrttdvmfg gkqvvvcgyg evgkgccaal kalgaivyit eidpicalqa cmdgfrvvkl
      361 nevirqvdvv itctgnknvv trehldrmkn scivcnmghs nteidvtslr tpeltwervr
      421 sqvdhviwpd gkrvvllaeg rllnlscstv ptfvlsitat tqalaliely napegrykqd
      481 vyllpkkmde yvaslhlpsf dahlteltdd qakylglnkn gpfkpnyyry
//
LOCUS       NP_001424872            2099 aa            linear   ROD 14-APR-2025
DEFINITION  dedicator of cytokinesis protein 9 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424872 XP_063130089
VERSION     NP_001424872.1
DBSOURCE    REFSEQ: accession NM_001437943.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2099)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2099)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2099)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 2099)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
REFERENCE   5  (residues 1 to 2099)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063130089.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1847360.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2099
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24-q25"
     Protein         1..2099
                     /product="dedicator of cytokinesis protein 9 isoform 1"
                     /note="dedicator of cytokinesis protein 9; cdc42 guanine
                     nucleotide exchange factor zizimin-1; Thyroid regulating"
                     /calculated_mol_wt=239514
     Region          43..153
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          167..290
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          634..823
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1629..2055
                     /region_name="DHR2_DOCK9"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 9; cd11698"
                     /db_xref="CDD:212571"
     Site            order(1733,1743,1745..1746,1748..1749,1752..1753,
                     1755..1756,1759..1760)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            order(1767..1770,1772,1813..1814,1816..1819,1821..1822,
                     1841..1843,1860,1862,1891,1893,1900..1901,1907,1946..1947,
                     1950,1964,1966,1970,1973..1975,1978..1981,1983..1984,1987,
                     2015,2033..2034,2036..2037,2040)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212571"
     Site            1978..1983
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212571"
     CDS             1..2099
                     /gene="Dock9"
                     /gene_synonym="Trg"
                     /coded_by="NM_001437943.1:138..6437"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:259237"
                     /db_xref="RGD:629617"
ORIGIN      
        1 mqadkyrtsg rndkkelvie splqykdaaq adseaensal akpkliepld yenvivqkkt
       61 qilndclrem llfpyddfqt ailrrqgryv rstvpanaee eaqslfvtec iktynsdwhl
      121 vtyhyedysg efrqlpnkva kldklpvhvy evdeeadkde daaslgsqkg gitkhgwlyk
      181 gnmnsaisvt mrsfkrrffh liqlgdgsyn lnfykdekis kepkgsifld scmgviqnnr
      241 vrrfafelkm qdkssyllaa dseaemeewv tvlnkilqln feaamqekrn gdpheddeqs
      301 klegsgsgld sylpelakst reaeiklkse srvklfyldp dtqkldfssa epevkpfeek
      361 fgkrilvkcn dlsfnlqccv aeneegpttn vepffvtlsl fdikynrkis adfhvdlnhf
      421 svrqmlapas pvlmnggqsp pafqdalqaa mqypkqgifs vtcphpdifl variekvlqg
      481 sithcaepym kssdsskvaq kvlknakqac qrlgqyrmpf awaartlfkd tsgnldknar
      541 fsaiyrqdsn klsnedmlkl ladfrkpekm aklpvilgnl ditidnvscd fpnylnssyi
      601 pmrqfetcsk spitfeveef vpcipkhtqp ytvysnhlyv ypkylrydsq ksfakarnia
      661 iciefkdsde edsqplkciy grpggpvftr salaavlhhq qspefydeik ielpaqlhek
      721 hhllftffhv scdnstkgst kkkdavetqv gfswlpllkd grvltneqhi pvsanlpsgy
      781 lgyqelsmgr hygpevkwve ggkpllkist hlvstvytqd qhlhnffqyc qktesgaqas
      841 gselvkylks lhameghvmi aflptilnql frvltratqe evavnvtrvi ihvvaqchee
      901 gleshlrsyv kfaykaepyi aseyktvhee ltksmttilk psadfltsnk llkyswfffd
      961 vliksmaqhl iennkvkllr nqrfpasyhh avetvvnmlm phitqkfrdn peasknanhs
     1021 lavfikrcft fmdrgfvfkq innyiscfap gdpktlfeyk feflrvvcnh ehyiplnlpm
     1081 pfgkgriqry qdlqldyslt defcrnhflv glllrevgta lqefrevrvi avsvlknlli
     1141 khsfddryts rshqariatl ylplfgllie nvqrinvrdv spfpvnpgsi skdealavpt
     1201 gnplmtpqkg ntldhslhkd llgaisgias pytastpnin svrnadsrgs listdsgnsl
     1261 pdrnpeksns ldkqqsgmlg nsvvrcdkld qseiksllmc flyvlksmsd dalftywnka
     1321 staelmdfft isevclhqfq ymgkryiars qeglgpighd rksqtlpvsr nragmaharl
     1381 qqlgsldnsv tfnhsyghse advahqslle aniatevclt aldtlslftl afknqlladh
     1441 ghnplmkkvf dvylcflqkh qsemalknvf talrsliykf pstfyegrad mcaslcyevl
     1501 kccnsklssi rteasqllyf lmrnnfdytg kksfvrthlq viisvsqlia dvvgiggtrf
     1561 qqslsiinnc ansdrlikht sfssdvkdlt krirtvlmat aqmkehendp emlvdlqysl
     1621 aksyastpel rktwldsmar ihvkngdlse aamcyvhvta lvaeyltrkg mfrqgctafr
     1681 vitpnideea smmedvgmqd vhfnedvlme lleqcadglw kaeryeliad iykliipiye
     1741 krrdferlah lydtlhrays kvtevmhsgr rllgtyfrva ffgqqyqftd setdvegffe
     1801 dedgkeyiyk epkltplsei sqrllklysd kfgsenvkmi qdsgkvnpkd ldskfayiqv
     1861 thvtpffdek elqerktefe rchnirrfmf empftqtgkr qggveeqckr rtiltaihcf
     1921 pyvkkripvm yqhhtdlnpi evaidemskk vaelrqlcss aevdmiklql klqgsvsvqv
     1981 nagplayara flddtntkry pdnkvkllke vfrqfveacg qalavnerli kedqleyqee
     2041 mkanyremak elsdimreqi cpleektsvl pnslhifnai sgtptstvvq gltssssvv
//
LOCUS       NP_001012232             155 aa            linear   ROD 14-APR-2025
DEFINITION  ribonuclease 17 precursor [Rattus norvegicus].
ACCESSION   NP_001012232 XP_008768783
VERSION     NP_001012232.1
DBSOURCE    REFSEQ: accession NM_001012232.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Cho,S., Beintema,J.J. and Zhang,J.
  TITLE     The ribonuclease A superfamily of mammals and birds: identifying
            new members and tracing evolutionary histories
  JOURNAL   Genomics 85 (2), 208-220 (2005)
   PUBMED   15676279
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_008768783.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1662139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..155
                     /product="ribonuclease 17 precursor"
                     /note="ribonuclease 1"
                     /calculated_mol_wt=15544
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2717
     Region          29..155
                     /region_name="RNAse_Pc"
                     /note="Pancreatic ribonuclease; smart00092"
                     /db_xref="CDD:128403"
     Site            order(34..43,46,50,52..54,62,65..70,104,124,148)
                     /site_type="active"
                     /note="dimerization with domain swap [active]"
                     /db_xref="CDD:119387"
     Site            order(38,62,66,93,105,150..151)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:119387"
     Site            order(63,96,107,123,125,127..128,130)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119387"
     CDS             1..155
                     /gene="Rnase17"
                     /gene_synonym="R1; R17"
                     /coded_by="NM_001012232.2:106..573"
                     /db_xref="GeneID:497195"
                     /db_xref="RGD:1359245"
ORIGIN      
        1 mglkllesrl clllllglvl mlascqpptp sqwfeiqhiy nrayprcnda mrhrnrftrh
       61 ckdkntflht sfasvvgvcg nrnipcrnrr yrnchnspyr vsitfcnltt pariytqcry
      121 qttrsrkfyt vgcdprtprd spmypvvpvh ldrif
//
LOCUS       NP_001424880             274 aa            linear   ROD 14-APR-2025
DEFINITION  uncharacterized protein LOC290425 [Rattus norvegicus].
ACCESSION   NP_001424880 XP_006252447
VERSION     NP_001424880.1
DBSOURCE    REFSEQ: accession NM_001437951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006252447.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.876738.1,
                                           SRR26360186.2255443.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..274
                     /product="uncharacterized protein LOC290425"
                     /note="spermatid associated like"
                     /calculated_mol_wt=32094
     Region          <48..>251
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <156..>255
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
     CDS             1..274
                     /gene="Golga6l9"
                     /gene_synonym="RGD1306441; Spertl"
                     /coded_by="NM_001437951.1:149..973"
                     /db_xref="GeneID:290425"
                     /db_xref="RGD:1306441"
ORIGIN      
        1 mnisgskqih krkilrlfsc fsctqnqkkl khksqdvekk lcrenkvlrd enralrkdnk
       61 flwgenkalg renktfrmdn qfirernhil rqqnqllrkv krlisenpkl sgeecnalnt
      121 egrsfwqqnr ameaqitalr qqekafqnea kalheeiksl ceetkalqhq eralrmeeka
      181 llrdgvaael aealtkegaa lemeeqalwk eeqalreenk alreehgalq deevalqeea
      241 rilqewnnll qgkitnnlpe nmnnqdpekc elrm
//
LOCUS       NP_001102198             533 aa            linear   ROD 14-APR-2025
DEFINITION  zinc transporter ZIP5 precursor [Rattus norvegicus].
ACCESSION   NP_001102198 XP_001067058 XP_063119770 XP_343141
VERSION     NP_001102198.1
DBSOURCE    REFSEQ: accession NM_001108728.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Guo,H., Jin,X., Zhu,T., Wang,T., Tong,P., Tian,L., Peng,Y., Sun,L.,
            Wan,A., Chen,J., Liu,Y., Li,Y., Tian,Q., Xia,L., Zhang,L., Pan,Y.,
            Lu,L., Liu,Q., Shen,L., Li,Y., Xiong,W., Li,J., Tang,B., Feng,Y.,
            Zhang,X., Zhang,Z., Pan,Q., Hu,Z. and Xia,K.
  TITLE     SLC39A5 mutations interfering with the BMP/TGF-beta pathway in
            non-syndromic high myopia
  JOURNAL   J Med Genet 51 (8), 518-525 (2014)
   PUBMED   24891338
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Zheng,S., Damoiseaux,R., Chen,L. and Black,D.L.
  TITLE     A broadly applicable high-throughput screening strategy identifies
            new regulators of Dlg4 (Psd-95) alternative splicing
  JOURNAL   Genome Res 23 (6), 998-1007 (2013)
   PUBMED   23636947
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Dufner-Beattie,J., Kuo,Y.M., Gitschier,J. and Andrews,G.K.
  TITLE     The adaptive response to dietary zinc in mice involves the
            differential cellular localization and zinc regulation of the zinc
            transporters ZIP4 and ZIP5
  JOURNAL   J Biol Chem 279 (47), 49082-49090 (2004)
   PUBMED   15358787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_063119770.1, XP_343141.3, XP_001067058.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.28438.1,
                                           SRR26643287.17147.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..533
                     /product="zinc transporter ZIP5 precursor"
                     /note="zinc transporter ZIP5; solute carrier family 39
                     (metal ion transporter), member 5; solute carrier family
                     39 (zinc transporter), member 5"
                     /calculated_mol_wt=53804
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2313
     Region          208..489
                     /region_name="Zip"
                     /note="ZIP Zinc transporter; pfam02535"
                     /db_xref="CDD:396884"
     CDS             1..533
                     /gene="Slc39a5"
                     /coded_by="NM_001108728.2:510..2111"
                     /db_xref="GeneID:362812"
                     /db_xref="RGD:1310322"
ORIGIN      
        1 mgppvhhlla glcvgvalgw vegsvpnlgp aeqeqnhyla qlfglygeng tltagglarl
       61 lhslglgrvq glrlghqepp tgraapmsgd nfthrlqele lsvdvwagmp lspsgwgdqe
      121 dskahdlhgs gpsgldlfhr lllldhslad hlnedclngs qllvnfglsp vapltprqfa
      181 llcpallyqi dsrvciktpa pappgdalsa llhsglavlf lslpapfsll llrllgprll
      241 rpvlgflgal avgtlcgdal lhllphaqgg rhtgpseqae edlgpglsvl gglfllfvle
      301 nalglvrhrg lrprcgrnkr dveepnpdpe dgtgmvlrpl qaasevqgqr ensqslpspa
      361 ppgyqghshe hrggsiawmv llgdclhnlt dglalgaafs dgfssglstt lavfchelph
      421 elgdfamllq eglsfrklll lslvsgvlgl ggaalgvgls lgpvpltpwv fgitagvfly
      481 valvdmlpal lrppeprplp hvllqglgll lggslmftia lleeqllpvv pdg
//
LOCUS       NP_001424860             191 aa            linear   ROD 14-APR-2025
DEFINITION  chromobox protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_001424860 XP_008763929
VERSION     NP_001424860.1
DBSOURCE    REFSEQ: accession NM_001437931.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Gilmore,J.M., Sardiu,M.E., Groppe,B.D., Thornton,J.L., Liu,X.,
            Dayebgadoh,G., Banks,C.A., Slaughter,B.D., Unruh,J.R.,
            Workman,J.L., Florens,L. and Washburn,M.P.
  TITLE     WDR76 Co-Localizes with Heterochromatin Related Proteins and
            Rapidly Responds to DNA Damage
  JOURNAL   PLoS One 11 (6), e0155492 (2016)
   PUBMED   27248496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Whelan,G., Kreidl,E., Wutz,G., Egner,A., Peters,J.M. and Eichele,G.
  TITLE     Cohesin acetyltransferase Esco2 is a cell viability factor and is
            required for cohesion in pericentric heterochromatin
  JOURNAL   EMBO J 31 (1), 71-82 (2012)
   PUBMED   22101327
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Yu,Y.H., Chiou,G.Y., Huang,P.I., Lo,W.L., Wang,C.Y., Lu,K.H.,
            Yu,C.C., Alterovitz,G., Huang,W.C., Lo,J.F., Hsu,H.S. and
            Chiou,S.H.
  TITLE     Network biology of tumor stem-like cells identified a regulatory
            role of CBX5 in lung cancer
  JOURNAL   Sci Rep 2, 584 (2012)
   PUBMED   22900142
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Rosnoblet,C., Vandamme,J., Volkel,P. and Angrand,P.O.
  TITLE     Analysis of the human HP1 interactome reveals novel binding
            partners
  JOURNAL   Biochem Biophys Res Commun 413 (2), 206-211 (2011)
   PUBMED   21888893
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Remboutsika,E., Lutz,Y., Gansmuller,A., Vonesch,J.L., Losson,R. and
            Chambon,P.
  TITLE     The putative nuclear receptor mediator TIF1alpha is tightly
            associated with euchromatin
  JOURNAL   J Cell Sci 112 (Pt 11), 1671-1683 (1999)
   PUBMED   10318760
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Lehming,N., Le Saux,A., Schuller,J. and Ptashne,M.
  TITLE     Chromatin components as part of a putative transcriptional
            repressing complex
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7322-7326 (1998)
   PUBMED   9636147
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Seeler,J.S., Marchio,A., Sitterlin,D., Transy,C. and Dejean,A.
  TITLE     Interaction of SP100 with HP1 proteins: a link between the
            promyelocytic leukemia-associated nuclear bodies and the chromatin
            compartment
  JOURNAL   Proc Natl Acad Sci U S A 95 (13), 7316-7321 (1998)
   PUBMED   9636146
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Le Douarin,B., Nielsen,A.L., Garnier,J.M., Ichinose,H.,
            Jeanmougin,F., Losson,R. and Chambon,P.
  TITLE     A possible involvement of TIF1 alpha and TIF1 beta in the
            epigenetic control of transcription by nuclear receptors
  JOURNAL   EMBO J 15 (23), 6701-6715 (1996)
   PUBMED   8978696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_008763929.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.935915.1,
                                           SRR26360194.731855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /calculated_mol_wt=22055
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="Cbx5"
                     /coded_by="NM_001437931.1:143..718"
                     /db_xref="GeneID:300266"
                     /db_xref="RGD:1306619"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrm vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksegnkr kssfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkekesak s
//
LOCUS       NP_001102031             475 aa            linear   ROD 14-APR-2025
DEFINITION  S-adenosylhomocysteine hydrolase-like protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102031 XP_001068488 XP_342313
VERSION     NP_001102031.1
DBSOURCE    REFSEQ: accession NM_001108561.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Harvey,K.E., LaVigne,E.K., Dar,M.S., Salyer,A.E., Pratt,E.P.S.,
            Sample,P.A., Aryal,U.K., Gowher,H. and Hockerman,G.H.
  TITLE     RyR2/IRBIT regulates insulin gene transcript, insulin content, and
            secretion in the insulinoma cell line INS-1
  JOURNAL   Sci Rep 12 (1), 7713 (2022)
   PUBMED   35562179
  REMARK    GeneRIF: RyR2/IRBIT regulates insulin gene transcript, insulin
            content, and secretion in the insulinoma cell line INS-1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Borth,H., Weber,N., Meyer,D., Wartenberg,A., Arlt,E., Zierler,S.,
            Breit,A., Wennemuth,G., Gudermann,T. and Boekhoff,I.
  TITLE     The IP3 R Binding Protein Released With Inositol
            1,4,5-Trisphosphate Is Expressed in Rodent Reproductive Tissue and
            Spermatozoa
  JOURNAL   J Cell Physiol 231 (5), 1114-1129 (2016)
   PUBMED   26439876
  REMARK    GeneRIF: The present study documents that IRBIT is expressed in
            Leydig and Sertoli cells.
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Ando,H., Hirose,M., Gainche,L., Kawaai,K., Bonneau,B., Ijuin,T.,
            Itoh,T., Takenawa,T. and Mikoshiba,K.
  TITLE     IRBIT Interacts with the Catalytic Core of Phosphatidylinositol
            Phosphate Kinase Type Ialpha and IIalpha through Conserved
            Catalytic Aspartate Residues
  JOURNAL   PLoS One 10 (10), e0141569 (2015)
   PUBMED   26509711
  REMARK    GeneRIF: IRBIT forms signaling complexes with PIPKIalpha and
            NBCe1-B, whose activity is regulated by PI(4,5)P2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Park,S., Shcheynikov,N., Hong,J.H., Zheng,C., Suh,S.H., Kawaai,K.,
            Ando,H., Mizutani,A., Abe,T., Kiyonari,H., Seki,G., Yule,D.,
            Mikoshiba,K. and Muallem,S.
  TITLE     Irbit mediates synergy between ca(2+) and cAMP signaling pathways
            during epithelial transport in mice
  JOURNAL   Gastroenterology 145 (1), 232-241 (2013)
   PUBMED   23542070
REFERENCE   5  (residues 1 to 475)
  AUTHORS   He,P., Klein,J. and Yun,C.C.
  TITLE     Activation of Na+/H+ exchanger NHE3 by angiotensin II is mediated
            by inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3 (IRBIT) and Ca2+/calmodulin-dependent protein
            kinase II
  JOURNAL   J Biol Chem 285 (36), 27869-27878 (2010)
   PUBMED   20584908
  REMARK    GeneRIF: IRBIT is critically involved in mediating activation of
            NHE3 by ANG II via a Ca(2+)/calmodulin-dependent protein kinases
            II-dependent pathway.
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Ando,H., Mizutani,A. and Mikoshiba,K.
  TITLE     An IRBIT homologue lacks binding activity to inositol
            1,4,5-trisphosphate receptor due to the unique N-terminal appendage
  JOURNAL   J Neurochem 109 (2), 539-550 (2009)
   PUBMED   19220705
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Yang,D., Shcheynikov,N., Zeng,W., Ohana,E., So,I., Ando,H.,
            Mizutani,A., Mikoshiba,K. and Muallem,S.
  TITLE     IRBIT coordinates epithelial fluid and HCO3- secretion by
            stimulating the transporters pNBC1 and CFTR in the murine
            pancreatic duct
  JOURNAL   J Clin Invest 119 (1), 193-202 (2009)
   PUBMED   19033647
REFERENCE   8  (residues 1 to 475)
  AUTHORS   He,P., Zhang,H. and Yun,C.C.
  TITLE     IRBIT, inositol 1,4,5-triphosphate (IP3) receptor-binding protein
            released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3
            activity in response to calcium
  JOURNAL   J Biol Chem 283 (48), 33544-33553 (2008)
   PUBMED   18829453
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Shirakabe,K., Priori,G., Yamada,H., Ando,H., Horita,S., Fujita,T.,
            Fujimoto,I., Mizutani,A., Seki,G. and Mikoshiba,K.
  TITLE     IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
            specifically binds to and activates pancreas-type Na+/HCO3-
            cotransporter 1 (pNBC1)
  JOURNAL   Proc Natl Acad Sci U S A 103 (25), 9542-9547 (2006)
   PUBMED   16769890
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Ando,H., Mizutani,A., Matsu-ura,T. and Mikoshiba,K.
  TITLE     IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
            protein, is released from the IP3 receptor upon IP3 binding to the
            receptor
  JOURNAL   J Biol Chem 278 (12), 10602-10612 (2003)
   PUBMED   12525476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473952.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342313.3, XP_001068488.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..475
                     /product="S-adenosylhomocysteine hydrolase-like protein 1
                     isoform 1"
                     /EC_number="3.13.2.1"
                     /note="S-adenosylhomocysteine hydrolase-like 1; putative
                     adenosylhomocysteinase 2; adoHcyase 2;
                     S-adenosyl-L-homocysteine hydrolase 2;
                     S-adenosylhomocysteine hydrolase-like protein 1;
                     IP3R-binding protein released with inositol
                     1,4,5-trisphosphate"
                     /calculated_mol_wt=52765
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Region          18..45
                     /region_name="PEST.
                     /evidence=ECO:0000250|UniProtKB:O43865,
                     ECO:0000250|UniProtKB:Q80SW1"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKD.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80SW1; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     Region          59..442
                     /region_name="AdoHcyase"
                     /note="S-adenosyl-L-homocysteine hydrolase; smart00996"
                     /db_xref="CDD:214963"
     Site            order(68,71,75,78..79,213,216..217,233,235,239..240,244,
                     247..248,252,255..256,259..265,273..274,277,286..287,289,
                     294..302,304..307,309..312,315,328..332,342..344,355,
                     372..373,378,402,404,406..407,410,436,442)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:240619"
     Region          91..154
                     /region_name="Interaction with BCL2L10.
                     /evidence=ECO:0000250|UniProtKB:O43865"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            order(106,108,110..111,182,207..208,237,241,398,403,408,
                     412)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240619"
     Site            order(208..210,242,246,271,273..275,293..296,299,326..329,
                     332,350..352,395,397,403)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240619"
     Region          234..401
                     /region_name="NAD binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFN2.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43865; propagated from
                     UniProtKB/Swiss-Prot (B5DFN2.2)"
     CDS             1..475
                     /gene="Ahcyl1"
                     /gene_synonym="IRBIT"
                     /coded_by="NM_001108561.1:136..1563"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362013"
                     /db_xref="RGD:1309768"
ORIGIN      
        1 mqeftkfptk tgrrslsrsi sqsstdsyss aasytdssdd evsprekqqt nskgssnfcv
       61 knikqaefgr reieiaeqdm salislrkra qgekplagak ivgcthitaq tavlietlca
      121 lgaqcrwsac niystqneva aalaeagvav fawkgesedd fwwcidrcvn mdgwqanmil
      181 ddggdlthwv ykkypnvfkk irgiveesvt gvhrlyqlsk agklcvpamn vndsvtkqkf
      241 dnlyccresi ldglkrttdv mfggkqvvvc gygevgkgcc aalkalgaiv yiteidpica
      301 lqacmdgfrv vklnevirqv dvvitctgnk nvvtrehldr mknscivcnm ghsnteidvt
      361 slrtpeltwe rvrsqvdhvi wpdgkrvvll aegrllnlsc stvptfvlsi tattqalali
      421 elynapegry kqdvyllpkk mdtngritmt spheprnsnr vffkitfiff lllsf
//
LOCUS       NP_001424899             560 aa            linear   ROD 14-APR-2025
DEFINITION  chaperone Ric-8B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424899 XP_006241242
VERSION     NP_001424899.1
DBSOURCE    REFSEQ: accession NM_001437970.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Lopez-Benito,S., Lillo,C., Hernandez-Hernandez,A., Chao,M.V. and
            Arevalo,J.C.
  TITLE     ARMS/Kidins220 and synembryn-B levels regulate NGF-mediated
            secretion
  JOURNAL   J Cell Sci 129 (9), 1866-1877 (2016)
   PUBMED   26966186
  REMARK    GeneRIF: overexpression of ARMS blocked NGF-mediated secretion,
            without affecting basal secretion, a decrease in ARMS resulted in
            potentiation. Similar effects were observed with synembryn-B, a
            protein that interacts directly with ARMS. Downstream of ARMS and
            synembryn-B are Galphaq and Trio proteins, which modulate the
            activity of Rac1 in response to NGF
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Aguilar,R., Grandy,R., Meza,D., Sepulveda,H., Pihan,P., van
            Wijnen,A.J., Lian,J.B., Stein,G.S., Stein,J.L. and Montecino,M.
  TITLE     A functional N-terminal domain in C/EBPbeta-LAP* is required for
            interacting with SWI/SNF and to repress Ric-8B gene transcription
            in osteoblasts
  JOURNAL   J Cell Physiol 229 (10), 1521-1528 (2014)
   PUBMED   24585571
  REMARK    GeneRIF: Results indicate that a functional N-terminus in
            C/EBPbeta-LAP* is required for interacting with SWI/SNF and for
            Ric-8B gene repression in osteoblasts.
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Chan,P., Gabay,M., Wright,F.A. and Tall,G.G.
  TITLE     Ric-8B is a GTP-dependent G protein alphas guanine nucleotide
            exchange factor
  JOURNAL   J Biol Chem 286 (22), 19932-19942 (2011)
   PUBMED   21467038
  REMARK    GeneRIF: Ric-8BFL-catalyzed nucleotide exchange probably proceeds
            in the forward direction to produce Galpha-GTP in cells.
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Klattenhoff,C., Montecino,M., Soto,X., Guzman,L., Romo,X.,
            Garcia,M.A., Mellstrom,B., Naranjo,J.R., Hinrichs,M.V. and Olate,J.
  TITLE     Human brain synembryn interacts with Gsalpha and Gqalpha and is
            translocated to the plasma membrane in response to isoproterenol
            and carbachol
  JOURNAL   J Cell Physiol 195 (2), 151-157 (2003)
   PUBMED   12652642
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Tall,G.G., Krumins,A.M. and Gilman,A.G.
  TITLE     Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein
            guanine nucleotide exchange factor
  JOURNAL   J Biol Chem 278 (10), 8356-8362 (2003)
   PUBMED   12509430
  REMARK    GeneRIF: two mammalian homologs of the Caenorhabditis elegans
            protein Ric-8 were identified: Ric-8A (Ric-8/synembryn) and Ric-8B
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006241242.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.137525.1,
                                           SRR26643429.26098.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..560
                     /product="chaperone Ric-8B isoform 2"
                     /note="synembryn-B; resistance to inhibitors of
                     cholinesterase 8 homolog B; resistance to inhibitors of
                     cholinesterase 8B; heterotrimeric G protein guanine
                     nucleotide exchange factor-like protein Ric-8B; chaperone
                     Ric-8B"
                     /calculated_mol_wt=62929
     Region          66..525
                     /region_name="Ric8"
                     /note="Guanine nucleotide exchange factor synembryn;
                     pfam10165"
                     /db_xref="CDD:462973"
     CDS             1..560
                     /gene="Ric8b"
                     /coded_by="NM_001437970.1:88..1770"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314681"
                     /db_xref="RGD:631419"
ORIGIN      
        1 mdeeralyiv rageagaier vlrdysdkhr atfkfesade dkrkklcegi fkvlvkgvpt
       61 tcqvpclevl rilsrdkkil apvtteenmq illrlaklhe sddslekvse fpviveslkc
      121 lcnivfnsqv aqqlslelnl aaklcnllrk ckdrkfindi kcfdlrllfv lsllhtdirs
      181 qlryelqglp lltqilesaf sikwtdeyes aidhsgppls pqetdcaiea lkalfnvtvd
      241 swkvhkesds hqfrvmaavl rhcllivgpt edkteelhsn avnllsnvpv scldvlicpl
      301 theetaqeaa tldelpgdkt aekdtalkss amvyngmnme aihvllsfme kridkgssyr
      361 egltpvlsll tecsrahrni rkflkdqvlp plrdvtnrpe vgstvrnklv rlmthvdlgv
      421 kqiaaeflfv lckervdsll kytgygnaag llaargllag grgdnwysed edtdteeykn
      481 akpninlitg hleepmpnpi demteeqkey eamklvnmld klsreellkp mglkpdgtit
      541 pleealsqys vieetssdtd
//
LOCUS       NP_001424868             313 aa            linear   ROD 14-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF126 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424868 XP_006240961
VERSION     NP_001424868.1
DBSOURCE    REFSEQ: accession NM_001437939.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Huang,C.Y., Lee,F.L., Peng,S.F., Lin,K.H., Chen,R.J., Ho,T.J.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     HSF1 phosphorylation by ERK/GSK3 suppresses RNF126 to sustain
            IGF-IIR expression for hypertension-induced cardiomyocyte
            hypertrophy
  JOURNAL   J Cell Physiol 233 (2), 979-989 (2018)
   PUBMED   28383811
  REMARK    GeneRIF: Angiotensin II activates ERK/GSK3 to phosphorylate HSF1,
            resulting in RNF126 degradation, which stabilizes IGF-IIR protein
            expression and eventually results in cardiac hypertrophy.
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rodrigo-Brenni,M.C., Gutierrez,E. and Hegde,R.S.
  TITLE     Cytosolic quality control of mislocalized proteins requires RNF126
            recruitment to Bag6
  JOURNAL   Mol Cell 55 (2), 227-237 (2014)
   PUBMED   24981174
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Smith,C.J. and McGlade,C.J.
  TITLE     The ubiquitin ligase RNF126 regulates the retrograde sorting of the
            cation-independent mannose 6-phosphate receptor
  JOURNAL   Exp Cell Res 320 (2), 219-232 (2014)
   PUBMED   24275455
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Smith,C.J., Berry,D.M. and McGlade,C.J.
  TITLE     The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal
            sorting of the epidermal growth factor receptor
  JOURNAL   J Cell Sci 126 (Pt 6), 1366-1380 (2013)
   PUBMED   23418353
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Delker,R.K., Zhou,Y., Strikoudis,A., Stebbins,C.E. and
            Papavasiliou,F.N.
  TITLE     Solubility-based genetic screen identifies RING finger protein 126
            as an E3 ligase for activation-induced cytidine deaminase
  JOURNAL   Proc Natl Acad Sci U S A 110 (3), 1029-1034 (2013)
   PUBMED   23277564
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Zhi,X., Zhao,D., Wang,Z., Zhou,Z., Wang,C., Chen,W., Liu,R. and
            Chen,C.
  TITLE     E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by
            targeting the tumor suppressor p21 for ubiquitin-mediated
            degradation
  JOURNAL   Cancer Res 73 (1), 385-394 (2013)
   PUBMED   23026136
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240961.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.24474.1,
                                           SRR26643285.26715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..313
                     /product="E3 ubiquitin-protein ligase RNF126 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF126"
                     /calculated_mol_wt=33959
     Region          10..40
                     /region_name="zinc_ribbon_9"
                     /note="zinc-ribbon; pfam14369"
                     /db_xref="CDD:433910"
     Region          230..273
                     /region_name="RING-H2_RNF126"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 126 (RNF126) and similar proteins; cd16801"
                     /db_xref="CDD:438453"
     CDS             1..313
                     /gene="Rnf126"
                     /coded_by="NM_001437939.1:61..1002"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314613"
                     /db_xref="RGD:1306011"
ORIGIN      
        1 maeaspqpgr yfchccsvei vprlpdyicp rcesgfieel peetrnteng sapstaptdq
       61 nrqpfenvdq hlftlpqgys qfafgifdds feipafppga qaddgrdpes rrerehqsrh
      121 rygarqprar ltarratgrh egvptlegii qqlvngiisp aavpslglgp wgvlhsnpmd
      181 yawganglda iitqllnqfe ntgpppadke kiqalptvpv teehvgsgle cpvckedyal
      241 gervrqlpcn hlfhdscivp wleqhdscpv crksltgqnt atnppgltgv gfssssssss
      301 ssspsnenat sns
//
LOCUS       NP_001424911             478 aa            linear   ROD 14-APR-2025
DEFINITION  alpha-1,3-mannosyl-glycoprotein
            4-beta-N-acetylglucosaminyltransferase C isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424911 XP_017450226
VERSION     NP_001424911.1
DBSOURCE    REFSEQ: accession NM_001437982.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_017450226.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.833008.1,
                                           SRR26360176.2206032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..478
                     /product="alpha-1,3-mannosyl-glycoprotein
                     4-beta-N-acetylglucosaminyltransferase C isoform 2"
                     /EC_number="2.4.1.145"
                     /note="alpha-1,3-mannosyl-glycoprotein
                     4-beta-N-acetylglucosaminyltransferase C; mannosyl
                     (alpha-1,3-)-glycoprotein
                     beta-1,4-N-acetylglucosaminyltransferase, isozyme C
                     (putative)"
                     /calculated_mol_wt=56084
     Region          64..330
                     /region_name="Glyco_transf_54"
                     /note="N-Acetylglucosaminyltransferase-IV (GnT-IV)
                     conserved region; pfam04666"
                     /db_xref="CDD:461384"
     CDS             1..478
                     /gene="Mgat4c"
                     /gene_synonym="RGD1307871"
                     /coded_by="NM_001437982.1:527..1963"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:299756"
                     /db_xref="RGD:1307871"
ORIGIN      
        1 mfkfyqmkyi fqildkmrcl rkrstvsflg vlvvfllfmn vfiedsyvle gdkqlirets
       61 thqlnseryv htfkdlsnfs gtinvtyryl aatplqrkry ltiglssvkr kkgnylleti
      121 ksifeqssye elkeisvvvh ladfnsswrd amvqditqkf ahhiiagrlm vihapeeyyp
      181 vldglkrnyn dpedrvrfrs kqnvdyafll nfcantsdyy vmleddvrcs rnfltaikkv
      241 iaslegtywv tlefsklgyi gklyhshdlp rlahfllmfy qempcdwllt hfrgllaqkn
      301 virfkpslfq hmgyyssykg tenklkdddf eeesfdipdn ppaslytnmn vfenyeaska
      361 yssvdeyfwg kppstgdtfv ivfenpikik kikvntgted rqndilhhga ldvgeklifs
      421 kqirqcetyl rlgefkngnf emsdvnqkip fdihcmricv tktqkewlii rsisiwts
//
LOCUS       NP_001424833             520 aa            linear   ROD 14-APR-2025
DEFINITION  amphoterin-induced protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001424833 XP_063119439
VERSION     NP_001424833.1
DBSOURCE    REFSEQ: accession NM_001437904.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Li,Z., Khan,M.M., Kuja-Panula,J., Wang,H., Chen,Y., Guo,D.,
            Chen,Z.J., Lahesmaa,R., Rauvala,H. and Tian,L.
  TITLE     AMIGO2 modulates T cell functions and its deficiency in mice
            ameliorates experimental autoimmune encephalomyelitis
  JOURNAL   Brain Behav Immun 62, 110-123 (2017)
   PUBMED   28119027
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Kanda,Y., Osaki,M., Onuma,K., Sonoda,A., Kobayashi,M., Hamada,J.,
            Nicolson,G.L., Ochiya,T. and Okada,F.
  TITLE     Amigo2-upregulation in Tumour Cells Facilitates Their Attachment to
            Liver Endothelial Cells Resulting in Liver Metastases
  JOURNAL   Sci Rep 7, 43567 (2017)
   PUBMED   28272394
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Park,H., Lee,S., Shrestha,P., Kim,J., Park,J.A., Ko,Y., Ban,Y.H.,
            Park,D.Y., Ha,S.J., Koh,G.Y., Hong,V.S., Mochizuki,N., Kim,Y.M.,
            Lee,W. and Kwon,Y.G.
  TITLE     AMIGO2, a novel membrane anchor of PDK1, controls cell survival and
            angiogenesis via Akt activation
  JOURNAL   J Cell Biol 211 (3), 619-637 (2015)
   PUBMED   26553931
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Rabenau,K.E., O'Toole,J.M., Bassi,R., Kotanides,H., Witte,L.,
            Ludwig,D.L. and Pereira,D.S.
  TITLE     DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
            expressed in human gastric adenocarcinoma: effects on ploidy,
            chromosomal stability, cell adhesion/migration and tumorigenicity
  JOURNAL   Oncogene 23 (29), 5056-5067 (2004)
   PUBMED   15107827
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Ono,T., Sekino-Suzuki,N., Kikkawa,Y., Yonekawa,H. and Kawashima,S.
  TITLE     Alivin 1, a novel neuronal activity-dependent gene, inhibits
            apoptosis and promotes survival of cerebellar granule neurons
  JOURNAL   J Neurosci 23 (13), 5887-5896 (2003)
   PUBMED   12843293
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Kuja-Panula,J., Kiiltomaki,M., Yamashiro,T., Rouhiainen,A. and
            Rauvala,H.
  TITLE     AMIGO, a transmembrane protein implicated in axon tract
            development, defines a novel protein family with leucine-rich
            repeats
  JOURNAL   J Cell Biol 160 (6), 963-973 (2003)
   PUBMED   12629050
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119439.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.42069.1,
                                           SRR26643295.29981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840118 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..520
                     /product="amphoterin-induced protein 2 precursor"
                     /note="amphoterin-induced protein 2; alivin 1; AMIGO-2;
                     amphoterin induced gene 2; transmembrane protein AMIGO2;
                     transmembrane protein AMIGO2-like"
                     /calculated_mol_wt=53754
     sig_peptide     1..37
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=4024
     mat_peptide     38..520
                     /product="Amphoterin-induced protein 2.
                     /evidence=ECO:0000255. /id=PRO_0000014512"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
                     /calculated_mol_wt=53754
     Region          50..71
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          68..89
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          <69..>229
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          72..94
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          93..114
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          96..117
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          117..138
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          118..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          141..162
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          142..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          165..186
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          166..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          192..213
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          219..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          297..367
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          305..309
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          319..323
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..341
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          359..364
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          437..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     Region          498..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ4.1)"
     CDS             1..520
                     /gene="Amigo2"
                     /gene_synonym="Ali1"
                     /coded_by="NM_001437904.1:338..1900"
                     /db_xref="GeneID:300186"
                     /db_xref="RGD:727911"
ORIGIN      
        1 mslrfhtlpt lpravkpgcr ellcllviav mvspsssglc ptacicatdi vsctnknlsk
       61 vpgnlfrlik rldlsynrig lldadwipvs fvklstlivr hnnitsistg sfsttpnlkc
      121 ldlssnrlks vksamfqelk vlevlllynn hisyldpaaf gglshlqkly lsgnfltkfp
      181 mdlyvgrfkl adltfldvsy nqiasipmhh inlvpgkqlr giflhgnpfv cdcslysllt
      241 fwyrrhfnsv tdfkhdytcr lwldsrhshq llllqdsfln cshsvingsf halgfiheaq
      301 vgeraivhcd gktgngntdf iwvgpdnrll epdkdtgnfr vfyngslvie npgfedagvy
      361 sciamnrqrl lnetvdimin vsnftinrsh haheafntaf ttlaacvvsi vlvllylylt
      421 pcpckcrdkr qknalnqsna hssilspgpt rdasaedrka gkrvvflepl kdpavgqngk
      481 vklvpsetvi aegilkssra ksdsdsvnsv fsdtpfvast
//
LOCUS       NP_001424840            1087 aa            linear   ROD 14-APR-2025
DEFINITION  ubiquitin-associated protein 2-like isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424840 XP_063138221
VERSION     NP_001424840.1
DBSOURCE    REFSEQ: accession NM_001437911.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Youn,J.Y., Dunham,W.H., Hong,S.J., Knight,J.D.R., Bashkurov,M.,
            Chen,G.I., Bagci,H., Rathod,B., MacLeod,G., Eng,S.W.M., Angers,S.,
            Morris,Q., Fabian,M., Cote,J.F. and Gingras,A.C.
  TITLE     High-Density Proximity Mapping Reveals the Subcellular Organization
            of mRNA-Associated Granules and Bodies
  JOURNAL   Mol Cell 69 (3), 517-532 (2018)
   PUBMED   29395067
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Bordeleau,M.E., Aucagne,R., Chagraoui,J., Girard,S., Mayotte,N.,
            Bonneil,E., Thibault,P., Pabst,C., Bergeron,A., Barabe,F.,
            Hebert,J., Sauvageau,M., Boutonnet,C., Meloche,S. and Sauvageau,G.
  TITLE     UBAP2L is a novel BMI1-interacting protein essential for
            hematopoietic stem cell activity
  JOURNAL   Blood 124 (15), 2362-2369 (2014)
   PUBMED   25185265
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Naz,R.K. and Dhandapani,L.
  TITLE     Identification of human sperm proteins that interact with human
            zona pellucida3 (ZP3) using yeast two-hybrid system
  JOURNAL   J Reprod Immunol 84 (1), 24-31 (2010)
   PUBMED   19945174
REFERENCE   7  (residues 1 to 1087)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063138221.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.8338.1,
                                           SRR26643295.9799.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1087
                     /product="ubiquitin-associated protein 2-like isoform 5"
                     /note="Atpase, class I, type 8B, member 2"
                     /calculated_mol_wt=114379
     Region          50..87
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          496..523
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1087
                     /gene="Ubap2l"
                     /gene_synonym="Atp8b2; EP1"
                     /coded_by="NM_001437911.1:59..3322"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:361984"
                     /db_xref="RGD:1308707"
ORIGIN      
        1 mmtsvgtnra rgnweqpqnq nqtqhkqrpq ataeqirlaq misdhndadf eekvkqlidi
       61 tgknqdecvi alhdcngdvn rainvllegn pdthswemvg kkkgvsgqkd ggqtesneeg
      121 kenrdrdrdy srrrggpprr grgasrgref rgqengldgt ksggpsgrgt drgrrgrgrg
      181 rgssgrrggr fsaqgmgtfn padyaepant ddnygsssgn twnntghfep ddgtsawrta
      241 teewgtedwn edlsetkift asnvssvplp aenvtitagq ridlavllgk tpssmendss
      301 nldpsqapsl aqplvfsnsk qnaisqpasg ntfshhsmvs mlgkgfgdvg eakggsttgs
      361 qfleqfktaq alaqlaaqhs qsgstttssw dmgsttqsps lvqydlksan dstvhspftk
      421 rqaftpsstm mevflqekpp avatstaapp ppssplpsks tsapqmspgs sdnqssspqp
      481 aqqklkqqkk ktsltskipa lavempgsad isglnlqfga lqfgsepvls dyestpttsa
      541 sssqapssly tstasessst vssnqsqesg yqsgpiqstt ytsqnnaqgp lyeqrstqtr
      601 rypssisssp qkdltqakng fssvqatqlq ttqsvegatg savksespst ssipslnetv
      661 paasllttas qhssslsgls hseeipnttt tqhssalstq qntlssstss grtststllh
      721 tsveseanlh sssstfstts stvsapppvv svssslnsgs slglslgsns tvtastrssv
      781 attsgkappn lppgvppllp npyimapgll hayppqvygy ddlqmlqtrf pldyysipfp
      841 tpttpltgrd gslasnpysg dltkfgrgda sspapattla qpqqnqtqth httqqtflnp
      901 alppgysyts lpyytgvpgl pstfqygpav fpvaptsskq hgvnvsvnas atpfqqpsgy
      961 gshgyntgvs vtssntgvpd isgsvysktq qsfekqgfhs gtpaasfnlp salgsggpin
     1021 pataaayppa pfmhiltphq qphsqilhhh lqqdgqtgsg qrsqtssipq kpqtnksayn
     1081 syswgan
//
LOCUS       NP_001424938             663 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001424938 XP_006237940
VERSION     NP_001424938.1
DBSOURCE    REFSEQ: accession NM_001438009.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_006237940.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18284.1,
                                           SRR26643299.21990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..663
                     /product="epithelial splicing regulatory protein 1 isoform
                     2"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=73350
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          310..420
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Site            582
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NXG1; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Region          633..>661
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..663
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438009.1:375..2366"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illlwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki daenlssapq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdldkldvaa maeslnfekn dsmsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcsktel idgntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptapii pvlpqqfvpp tnvrdcvrlr glpyaatied ildflgefst dirthgvhmv
      481 lnhqgrpsgd afiqmkstdr afmaaqkyhk ktmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppcklp clsppsytfp apaaviptea aiyqpsllln pralqpstay ypagtqlfmn
      601 ytayypsppg spnslgyfpt aanlssvppq pgtvvrmqgl ayntgvkeil nffqgyqclk
      661 daw
//
LOCUS       NP_001424944             183 aa            linear   ROD 14-APR-2025
DEFINITION  ras-related protein Rap-2a isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424944
VERSION     NP_001424944.1
DBSOURCE    REFSEQ: accession NM_001438015.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Hu,Y., Hong,X.Y., Yang,X.F., Ma,R.H., Wang,X., Zhang,J.F., Feng,Q.,
            Li,X.G., Sun,D.S., Li,X., Wan,H.L., Li,T., Wang,Q., Ke,D.,
            Wang,J.Z. and Liu,G.P.
  TITLE     Inflammation-dependent ISG15 upregulation mediates MIA-induced
            dendrite damages and depression by disrupting NEDD4/Rap2A signaling
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (6), 1477-1489 (2019)
   PUBMED   30826466
  REMARK    GeneRIF: The data revealed that maternal immune activation impedes
            offspring's dendrite development and causes depressive like
            behaviors by upregulating ISG15 and suppressing NEDD4/Rap2A
            signaling.
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Emery,A.C., Xu,W., Eiden,M.V. and Eiden,L.E.
  TITLE     Guanine nucleotide exchange factor Epac2-dependent activation of
            the GTP-binding protein Rap2A mediates cAMP-dependent growth arrest
            in neuroendocrine cells
  JOURNAL   J Biol Chem 292 (29), 12220-12231 (2017)
   PUBMED   28546426
  REMARK    GeneRIF: Data suggest that Rap2A is the obligate effector for Epac2
            in mediating growth arrest and reversal of neurite extension
            through activation of MAP kinase signaling via protein
            phosphorylation/farnesylation in neuroendocrine cells. (Rap2A = RAS
            oncogene family member Rap2A; Epac2 = guanine nucleotide exchange
            factor Epac2)
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Kawabe,H., Neeb,A., Dimova,K., Young,S.M. Jr., Takeda,M.,
            Katsurabayashi,S., Mitkovski,M., Malakhova,O.A., Zhang,D.E.,
            Umikawa,M., Kariya,K., Goebbels,S., Nave,K.A., Rosenmund,C.,
            Jahn,O., Rhee,J. and Brose,N.
  TITLE     Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls
            neurite development
  JOURNAL   Neuron 65 (3), 358-372 (2010)
   PUBMED   20159449
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Uechi,Y., Bayarjargal,M., Umikawa,M., Oshiro,M., Takei,K.,
            Yamashiro,Y., Asato,T., Endo,S., Misaki,R., Taguchi,T. and
            Kariya,K.
  TITLE     Rap2 function requires palmitoylation and recycling endosome
            localization
  JOURNAL   Biochem Biophys Res Commun 378 (4), 732-737 (2009)
   PUBMED   19061864
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Taira,K., Umikawa,M., Takei,K., Myagmar,B.E., Shinzato,M.,
            Machida,N., Uezato,H., Nonaka,S. and Kariya,K.
  TITLE     The Traf2- and Nck-interacting kinase as a putative effector of
            Rap2 to regulate actin cytoskeleton
  JOURNAL   J Biol Chem 279 (47), 49488-49496 (2004)
   PUBMED   15342639
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Machida,N., Umikawa,M., Takei,K., Sakima,N., Myagmar,B.E.,
            Taira,K., Uezato,H., Ogawa,Y. and Kariya,K.
  TITLE     Mitogen-activated protein kinase kinase kinase kinase 4 as a
            putative effector of Rap2 to activate the c-Jun N-terminal kinase
  JOURNAL   J Biol Chem 279 (16), 15711-15714 (2004)
   PUBMED   14966141
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Menetrey,J. and Cherfils,J.
  TITLE     Structure of the small G protein Rap2 in a non-catalytic complex
            with GTP
  JOURNAL   Proteins 37 (3), 465-473 (1999)
   PUBMED   10591105
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Cherfils,J., Menetrey,J., Le Bras,G., Janoueix-Lerosey,I., de
            Gunzburg,J., Garel,J.R. and Auzat,I.
  TITLE     Crystal structures of the small G protein Rap2A in complex with its
            substrate GTP, with GDP and with GTPgammaS
  JOURNAL   EMBO J 16 (18), 5582-5591 (1997)
   PUBMED   9312017
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Lerosey,I., Chardin,P., de Gunzburg,J. and Tavitian,A.
  TITLE     The product of the rap2 gene, member of the ras superfamily.
            Biochemical characterization and site-directed mutagenesis
  JOURNAL   J Biol Chem 266 (7), 4315-4321 (1991)
   PUBMED   1900290
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.927544.1,
                                           SRR26360181.2350052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24"
     Protein         1..183
                     /product="ras-related protein Rap-2a isoform 1"
                     /EC_number="3.6.5.2"
                     /note="rap2A-like protein; ras-related protein Rap-2a; RAS
                     related protein 2a inverted question mark"
                     /calculated_mol_wt=20511
     Region          16..165
                     /region_name="Rap2"
                     /note="Rap2 family GTPase consists of Rap2a, Rap2b, and
                     Rap2c; cd04176"
                     /db_xref="CDD:133376"
     Site            order(16..18,28..31,116..117,119,146..147)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133376"
     Site            order(17..18,32,34,40..41,54..55,57,59..60,148)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133376"
     Site            order(25,31,33,36..41)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133376"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133376"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133376"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133376"
     Site            order(59..65,68..73,76..77)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133376"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133376"
     Site            146..148
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133376"
     CDS             1..183
                     /gene="Rap2a"
                     /coded_by="NM_001438015.1:273..824"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:114560"
                     /db_xref="RGD:620590"
ORIGIN      
        1 mreykvvvlg sggvgksalt vqfvtgtfie kydptiedfy rkeievdssp svleildtag
       61 teqfasmrdl yikngqgfil vyslvnqqsf qdikpmrdqi irvkryekvp vilvgnkvdl
      121 eserevssne gralaeewgc pfmetsaksk tmvdelfaei vrqmnyaaqp dkddpccsac
      181 niq
//
LOCUS       NP_001424941             436 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001424941 XP_063144265
VERSION     NP_001424941.1
DBSOURCE    REFSEQ: accession NM_001438012.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_063144265.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1089669.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..436
                     /product="epithelial splicing regulatory protein 1 isoform
                     6"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=48412
     Region          44..136
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          138..248
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          272..352
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     CDS             1..436
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438012.1:1505..2815"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 msrygasqve dmgniilami sepynhrfsd pervnykfes gtcsktelid gntvvrargl
       61 pwqssdqdia rffkglniak ggaalclnaq grrngealvr fvseehrdla lqrhkhhmgt
      121 ryievykatg edflkiaggt snevaqflsk enqvivrmrg lpftataeev vaffgqhcpi
      181 tggkegilfv typdgrptgd afvlfaceey aqnalrkhkd llgkryielf rstaaevqqv
      241 lnrfssapli plptapiipv lpqqfvpptn vrdcvrlrgl pyaatiedil dflgefstdi
      301 rthgvhmvln hqgrpsgdaf iqmkstdraf maaqkyhkkt mkdryvevfq csaeemnfvl
      361 mggtlnrngl spppcklpcl sppsytfpap aavipteaai yqpslllnpr alqpstayyp
      421 agtqlfmnyt ayypsv
//
LOCUS       NP_001121036             659 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001121036 XP_001064461 XP_575771
VERSION     NP_001121036.2
DBSOURCE    REFSEQ: accession NM_001127564.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jun 1, 2008 this sequence version replaced NP_001121036.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166735.1, SRR26643295.20643.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760434 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..659
                     /product="epithelial splicing regulatory protein 1 isoform
                     3"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=72909
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          310..420
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Site            578
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NXG1; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Region          629..>657
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..659
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001127564.3:375..2354"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illlwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki daenlssapq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdldkldvaa maeslnfekn dsmsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcsktel idgntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptapii pvlpqqfvpp tnvrdcvrlr glpyaatied ildflgefst dirthgvhmv
      481 lnhqgrpsgd afiqmkstdr afmaaqkyhk ktmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppclsp psytfpapaa vipteaaiyq pslllnpral qpstayypag tqlfmnytay
      601 ypsppgspns lgyfptaanl ssvppqpgtv vrmqglaynt gvkeilnffq gyqclkdaw
//
LOCUS       NP_001424939             607 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001424939 XP_063144262
VERSION     NP_001424939.1
DBSOURCE    REFSEQ: accession NM_001438010.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_063144262.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.515046.1,
                                           SRR26643291.14359.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..607
                     /product="epithelial splicing regulatory protein 1 isoform
                     4"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=67351
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..307
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          309..419
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          443..523
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Site            581
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NXG1; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     CDS             1..607
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438010.1:375..2198"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illlwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki daenlssapq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdldkldvaa maeslnfekn dsmsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtckteli dgntvvrarg lpwqssdqdi
      241 arffkglnia kggaalclna qgrrngealv rfvseehrdl alqrhkhhmg tryievykat
      301 gedflkiagg tsnevaqfls kenqvivrmr glpftataee vvaffgqhcp itggkegilf
      361 vtypdgrptg dafvlfacee yaqnalrkhk dllgkryiel frstaaevqq vlnrfssapl
      421 iplptapiip vlpqqfvppt nvrdcvrlrg lpyaatiedi ldflgefstd irthgvhmvl
      481 nhqgrpsgda fiqmkstdra fmaaqkyhkk tmkdryvevf qcsaeemnfv lmggtlnrng
      541 lspppcklpc lsppsytfpa paavipteaa iyqpslllnp ralqpstayy pagtqlfmny
      601 tayypsv
//
LOCUS       NP_001424940             604 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001424940 XP_063144263
VERSION     NP_001424940.1
DBSOURCE    REFSEQ: accession NM_001438011.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_063144263.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1652073.1,
                                           SRR26643297.18274.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMEA5760476 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..604
                     /product="epithelial splicing regulatory protein 1 isoform
                     5"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=66997
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          310..420
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Site            578
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NXG1; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     CDS             1..604
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438011.1:375..2189"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illlwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki daenlssapq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdldkldvaa maeslnfekn dsmsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcsktel idgntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptapii pvlpqqfvpp tnvrdcvrlr glpyaatied ildflgefst dirthgvhmv
      481 lnhqgrpsgd afiqmkstdr afmaaqkyhk ktmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppclsp psytfpapaa vipteaaiyq pslllnpral qpstayypag tqlfmnytay
      601 ypsv
//
LOCUS       NP_001424942             432 aa            linear   ROD 14-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001424942 XP_063144266
VERSION     NP_001424942.1
DBSOURCE    REFSEQ: accession NM_001438013.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_063144266.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.1157303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..432
                     /product="epithelial splicing regulatory protein 1 isoform
                     7"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=47970
     Region          44..136
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          138..248
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          272..352
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     CDS             1..432
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438013.1:4569..5867"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 msrygasqve dmgniilami sepynhrfsd pervnykfes gtcsktelid gntvvrargl
       61 pwqssdqdia rffkglniak ggaalclnaq grrngealvr fvseehrdla lqrhkhhmgt
      121 ryievykatg edflkiaggt snevaqflsk enqvivrmrg lpftataeev vaffgqhcpi
      181 tggkegilfv typdgrptgd afvlfaceey aqnalrkhkd llgkryielf rstaaevqqv
      241 lnrfssapli plptapiipv lpqqfvpptn vrdcvrlrgl pyaatiedil dflgefstdi
      301 rthgvhmvln hqgrpsgdaf iqmkstdraf maaqkyhkkt mkdryvevfq csaeemnfvl
      361 mggtlnrngl spppclspps ytfpapaavi pteaaiyqps lllnpralqp stayypagtq
      421 lfmnytayyp sv
//
LOCUS       NP_001100776             468 aa            linear   ROD 14-APR-2025
DEFINITION  armadillo repeat-containing protein 6 [Rattus norvegicus].
ACCESSION   NP_001100776 XP_001071122 XP_224735
VERSION     NP_001100776.2
DBSOURCE    REFSEQ: accession NM_001107306.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Apr 14, 2025 this sequence version replaced NP_001100776.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166821.1, SRR26643288.55430.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..468
                     /product="armadillo repeat-containing protein 6"
                     /calculated_mol_wt=50516
     Region          144..182
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          184..226
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          190..224
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          244..278
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(269,273,277,312,316,320,355,359,363)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          286..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          328..364
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..468
                     /gene="Armc6"
                     /coded_by="NM_001107306.2:370..1776"
                     /db_xref="GeneID:306352"
                     /db_xref="RGD:1306691"
ORIGIN      
        1 maskritqet fdaavrenie efemgaeeai reaveqfesq gvdlsnivkt vpkvsldglq
       61 epthdvlqal ndlqqaltgs qlqevsahlv rfcdqckqqk asrylaaqkg aypillaawq
      121 laatsdqgll lqalnalavl tdgqpdlldt qglhllvatl arnaantelt ccgircvrhv
      181 clkheqnrqg lvkagvlpll taaitqhgqh advvreacwa lrvmtfdddi rvpfghaheh
      241 akmivqenrg lkvlieaara fsdnpgvlse lcstlsrlav rnefcqevid lgglgilvtl
      301 ladcndhqdl vkqvlsalra iagnddvkda ivraggtqsi vaamtrhlas pqvceqscaa
      361 lcvlalrkpe nsrviieggg alaalqamka hpqeagvqkq acmlirnlvs rsqvfskpil
      421 dlgaeelilq araahpdced vakaalrdlg crvelrelwt gkkgnlap
//
LOCUS       NP_001128096             330 aa            linear   ROD 14-APR-2025
DEFINITION  leucine-rich repeat-containing protein 69 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001128096 XP_001055887 XP_575777
VERSION     NP_001128096.1
DBSOURCE    REFSEQ: accession NM_001134624.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473962.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_001055887.1, XP_575777.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132301, SAMEA5760383
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..330
                     /product="leucine-rich repeat-containing protein 69
                     isoform 2"
                     /note="leucine-rich repeat-containing protein 69"
                     /calculated_mol_wt=37567
     Region          <8..>233
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          16..38
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          39..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          109..131
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          132..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          155..177
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          178..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          201..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..330
                     /gene="Lrrc69"
                     /coded_by="NM_001134624.1:18..1010"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500415"
                     /db_xref="RGD:1583733"
ORIGIN      
        1 mterllltal kggkstkilt lngkkmskmp saleklpnlr tldlqnnqis kvcpelrtlt
       61 kltllnlgnn llqevpeeik yltslknlhl fgnricriaa gvldglgdlv llnlndnqls
      121 slppeigrlq nltflslnhn kltvipkeic flehlselhi nynritripe eirflqnlqq
      181 lslvrnniee lpeevcqltk lgvldvagnv iqifpagfqd lklrefyceg nplflknpif
      241 apqpkdlwtl reiaarfvls qleeynplim daiecypevk dklskakkca icrkpflsew
      301 lecvyfvpps keeelscwsi sevedsqktf
//
LOCUS       NP_001425026             671 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425026 XP_038937828
VERSION     NP_001425026.1
DBSOURCE    REFSEQ: accession NM_001438097.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937828.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.294242.1,
                                           SRR26643295.1796.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..671
                     /product="proline and serine-rich protein 3 isoform 1"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70181
     Region          <219..514
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          588..>632
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..671
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438097.1:345..2360"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaag
      121 ageptgrsav tgpcptgmss tslasvplqr vkqslnswns amleletlsl qsraakller
      181 skaslsssss spspneasss sfpissdgls pcsvtfnpds nkssspkepv lgaapvpsqa
      241 ipaprpasaq atlkpeedil yqwrqrrkle qslqgagdgt wvlprtpalt tqtpvsavnl
      301 gskgtqpnca ppwgsvaqpp ppqafymerp plsgpsphiw apgthgvlwa pqanpwiplg
      361 mvpttlltst laplaslpvp ptstsaatap isapqvsipg ppasapppct sapastvplp
      421 dnpqgpttpe lsssvhpkkl spkprcvsas srqettgpdt aafespcsql rgalsqvvta
      481 rlfsdsledm ppseadsrkv katssqakvp ppppesrrgs ktesrkskvt lsaeagdpqp
      541 atapkastls evqslefkks tpkkgagdal ttappassha psedllsqaa rllqaaedsd
      601 gsefpedsvl rvlraqrael rqqkrnvdaq lsllldhted pgfssppars psssprmrlr
      661 regaslearr p
//
LOCUS       NP_001425027             671 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425027 XP_006228834
VERSION     NP_001425027.1
DBSOURCE    REFSEQ: accession NM_001438098.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006228834.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1839068.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..671
                     /product="proline and serine-rich protein 3 isoform 1"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70181
     Region          <219..514
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          588..>632
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..671
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438098.1:342..2357"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaag
      121 ageptgrsav tgpcptgmss tslasvplqr vkqslnswns amleletlsl qsraakller
      181 skaslsssss spspneasss sfpissdgls pcsvtfnpds nkssspkepv lgaapvpsqa
      241 ipaprpasaq atlkpeedil yqwrqrrkle qslqgagdgt wvlprtpalt tqtpvsavnl
      301 gskgtqpnca ppwgsvaqpp ppqafymerp plsgpsphiw apgthgvlwa pqanpwiplg
      361 mvpttlltst laplaslpvp ptstsaatap isapqvsipg ppasapppct sapastvplp
      421 dnpqgpttpe lsssvhpkkl spkprcvsas srqettgpdt aafespcsql rgalsqvvta
      481 rlfsdsledm ppseadsrkv katssqakvp ppppesrrgs ktesrkskvt lsaeagdpqp
      541 atapkastls evqslefkks tpkkgagdal ttappassha psedllsqaa rllqaaedsd
      601 gsefpedsvl rvlraqrael rqqkrnvdaq lsllldhted pgfssppars psssprmrlr
      661 regaslearr p
//
LOCUS       NP_001425025             671 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425025 XP_038937827
VERSION     NP_001425025.1
DBSOURCE    REFSEQ: accession NM_001438096.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937827.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3245440.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..671
                     /product="proline and serine-rich protein 3 isoform 1"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70181
     Region          <219..514
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          588..>632
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..671
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438096.1:554..2569"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaag
      121 ageptgrsav tgpcptgmss tslasvplqr vkqslnswns amleletlsl qsraakller
      181 skaslsssss spspneasss sfpissdgls pcsvtfnpds nkssspkepv lgaapvpsqa
      241 ipaprpasaq atlkpeedil yqwrqrrkle qslqgagdgt wvlprtpalt tqtpvsavnl
      301 gskgtqpnca ppwgsvaqpp ppqafymerp plsgpsphiw apgthgvlwa pqanpwiplg
      361 mvpttlltst laplaslpvp ptstsaatap isapqvsipg ppasapppct sapastvplp
      421 dnpqgpttpe lsssvhpkkl spkprcvsas srqettgpdt aafespcsql rgalsqvvta
      481 rlfsdsledm ppseadsrkv katssqakvp ppppesrrgs ktesrkskvt lsaeagdpqp
      541 atapkastls evqslefkks tpkkgagdal ttappassha psedllsqaa rllqaaedsd
      601 gsefpedsvl rvlraqrael rqqkrnvdaq lsllldhted pgfssppars psssprmrlr
      661 regaslearr p
//
LOCUS       NP_001425015             376 aa            linear   ROD 15-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001425015 XP_038937670
VERSION     NP_001425015.1
DBSOURCE    REFSEQ: accession NM_001438086.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937670.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1751427.1,
                                           SRR26360194.1254687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..376
                     /product="vasodilator-stimulated phosphoprotein isoform 3"
                     /calculated_mol_wt=39593
     Region          6..114
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(17,24,72,74,80,82,84)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          216..242
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(223..224,226..227,230,232..236)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          232..235
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          340..372
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..376
                     /gene="Vasp"
                     /coded_by="NM_001438086.1:300..1430"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 msnetvicss ratvmlydds nkrwlpagtg pqafsrvqiy hnptansfrv vgrklqpdqq
       61 vvincaiirg vkynqatpif hqwrdarqvw glnfgskeda aqfaigmana lealegggpp
      121 papappawst qngpspeele qqkrqpehle rrvsnaggpp appaggpppp pgpppppgpp
      181 pppglppsgv sgaghgtgva pppapplpta qgpssggsga pglaaaiaga klrkvskqee
      241 asggplapka ensrgtgggl meemnamlar rrkatqvgek ppkdesasee searipaqse
      301 pvrrpwekns ttlprmksss svttseahps vpsssddsdl ervkqelvee vrkelqkmke
      361 eiievfvqel rkrgsp
//
LOCUS       NP_001425043             463 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425043 XP_006228919
VERSION     NP_001425043.1
DBSOURCE    REFSEQ: accession NM_001438114.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006228919.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.2003.1,
                                           SRR26643298.2488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..463
                     /product="protein LSM14 homolog A isoform 2"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=50475
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          290..400
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..463
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438114.1:142..1533"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqg
      181 rsspqldplr ksptmeqavq tasahlpapa pvgrrspvpa rplpptsqka idnqehrrae
      241 vhkvprpene qlrndskrqv vpgvpsaprr grgghrggrg rfgirrdgpm kfekdfdfes
      301 anaqfnkeei drefhnklkl kedklekqek pvngedkgds gvdtqnsegn adeedplgpn
      361 cyydktksff dniscddnre rrptwaeerr lnaetfgipl rpnrgrggyr grgglgfrgg
      421 rgrgsgrggt ftaprgfrag frgarggref adfeyrktta fgp
//
LOCUS       NP_001425047             404 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 6 [Rattus norvegicus].
ACCESSION   NP_001425047 XP_017444843
VERSION     NP_001425047.1
DBSOURCE    REFSEQ: accession NM_001438118.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_017444843.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1236.1,
                                           SRR26643292.1838.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..404
                     /product="protein LSM14 homolog A isoform 6"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=44108
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          231..341
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..404
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438118.1:142..1356"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqa
      181 evhkvprpen eqlrndskrq vvpgvpsapr rgrgghrggr grfgirrdgp mkfekdfdfe
      241 sanaqfnkee idrefhnklk lkedklekqe kpvngedkgd sgvdtqnseg nadeedplgp
      301 ncyydktksf fdniscddnr errptwaeer rlnaetfgip lrpnrgrggy rgrgglgfrg
      361 grgrgsgrgg tftaprgfra gfrgarggre fadfeyrktt afgp
//
LOCUS       NP_001425033             670 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425033 XP_063122527
VERSION     NP_001425033.1
DBSOURCE    REFSEQ: accession NM_001438104.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122527.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2441413.1,
                                           SRR26360181.3287243.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438104.1:341..2353"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001037732             413 aa            linear   ROD 15-APR-2025
DEFINITION  MAP kinase-interacting serine/threonine-protein kinase 1 [Rattus
            norvegicus].
ACCESSION   NP_001037732 XP_001064399 XP_001064462 XP_575887
VERSION     NP_001037732.1
DBSOURCE    REFSEQ: accession NM_001044267.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Panja,D., Kenney,J.W., D'Andrea,L., Zalfa,F., Vedeler,A.,
            Wibrand,K., Fukunaga,R., Bagni,C., Proud,C.G. and Bramham,C.R.
  TITLE     Two-stage translational control of dentate gyrus LTP consolidation
            is mediated by sustained BDNF-TrkB signaling to MNK
  JOURNAL   Cell Rep 9 (4), 1430-1445 (2014)
   PUBMED   25453757
  REMARK    GeneRIF: Long-term potentiation (LTP) consolidation in the dentate
            gyrus of live rodents requires sustained (hours) BDNF-TrkB
            signaling and from TrkB to MAP-kinase-interacting kinase.
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Niknami,M., Patel,M., Witting,P.K. and Dong,Q.
  TITLE     Molecules in focus: cytosolic phospholipase A2-alpha
  JOURNAL   Int J Biochem Cell Biol 41 (5), 994-997 (2009)
   PUBMED   18761105
  REMARK    Review article
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Chrestensen,C.A., Eschenroeder,A., Ross,W.G., Ueda,T.,
            Watanabe-Fukunaga,R., Fukunaga,R. and Sturgill,T.W.
  TITLE     Loss of MNK function sensitizes fibroblasts to serum-withdrawal
            induced apoptosis
  JOURNAL   Genes Cells 12 (10), 1133-1140 (2007)
   PUBMED   17903173
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Origanti,S. and Shantz,L.M.
  TITLE     Ras transformation of RIE-1 cells activates cap-independent
            translation of ornithine decarboxylase: regulation by the
            Raf/MEK/ERK and phosphatidylinositol 3-kinase pathways
  JOURNAL   Cancer Res 67 (10), 4834-4842 (2007)
   PUBMED   17510413
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Chen,S., Atkins,C.M., Liu,C.L., Alonso,O.F., Dietrich,W.D. and
            Hu,B.R.
  TITLE     Alterations in mammalian target of rapamycin signaling pathways
            after traumatic brain injury
  JOURNAL   J Cereb Blood Flow Metab 27 (5), 939-949 (2007)
   PUBMED   16955078
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Chrestensen,C.A., Shuman,J.K., Eschenroeder,A., Worthington,M.,
            Gram,H. and Sturgill,T.W.
  TITLE     MNK1 and MNK2 regulation in HER2-overexpressing breast cancer lines
  JOURNAL   J Biol Chem 282 (7), 4243-4252 (2007)
   PUBMED   17130135
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Gaestel,M.
  TITLE     MAPKAP kinases - MKs - two's company, three's a crowd
  JOURNAL   Nat Rev Mol Cell Biol 7 (2), 120-130 (2006)
   PUBMED   16421520
  REMARK    Review article
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Fukunaga,R. and Hunter,T.
  TITLE     MNK1, a new MAP kinase-activated protein kinase, isolated by a
            novel expression screening method for identifying protein kinase
            substrates
  JOURNAL   EMBO J 16 (8), 1921-1933 (1997)
   PUBMED   9155018
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Waskiewicz,A.J., Flynn,A., Proud,C.G. and Cooper,J.A.
  TITLE     Mitogen-activated protein kinases activate the serine/threonine
            kinases Mnk1 and Mnk2
  JOURNAL   EMBO J 16 (8), 1909-1920 (1997)
   PUBMED   9155017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_575887.2, XP_001064399.1, XP_001064462.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098754.1, SRR26360194.418492.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..413
                     /product="MAP kinase-interacting serine/threonine-protein
                     kinase 1"
                     /EC_number="2.7.11.1"
                     /note="mnk1; MAP kinase signal-integrating kinase 1; MAPK
                     signal-integrating kinase 1; MAP kinase-interacting
                     serine/threonine kinase 1"
                     /calculated_mol_wt=46083
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:O08605; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:O08605; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Region          34..322
                     /region_name="STKc_Mnk1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase signal-integrating kinase
                     1; cd14174"
                     /db_xref="CDD:271076"
     Site            order(43..47,51,64,66,96,112..115,119,121,157..158,160,
                     162..163,165,178..179,182,204..208,210)
                     /site_type="active"
                     /db_xref="CDD:271076"
     Site            order(43..46,51,64,66,96,112..115,119,162..163,165,
                     178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271076"
     Site            order(47,119,121,157..158,160,162,182,204..208,210)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271076"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            178..208
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271076"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            order(252,256,264,267)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:271076"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     CDS             1..413
                     /gene="Mknk1"
                     /coded_by="NM_001044267.2:64..1305"
                     /db_xref="GeneID:500526"
                     /db_xref="RGD:1559603"
ORIGIN      
        1 mgsseplpiv dsdkrrkkkr ktratdslpg kfedvyqlts ellgegayak vqgavslqsg
       61 keyavkiiek qaghsrsrvf revetlyqcq gnrnilelie ffeddtrfyl vfeklqggsi
      121 lahiqkrkhf neleasrvvr dvataldflh tkgiahrdlk penilcespe kvspvkicdf
      181 dlgsgvklnn sctpittpel ttpcgsaeym apevvevfrd eatfydkrcd lwslgvvlyi
      241 mlsgyppfvg hcgadcgwdr gevcrmcqnk lfesiqegky efpdkdwahi steakdlisk
      301 llvrdakqrl saaqvlqhpw vqgqapergl ptpqvlqrns stmdltlfaa eaialnrqls
      361 qheenelaee healaeglcs mklsppsksr larrralaha greanscstp agl
//
LOCUS       NP_001425045             462 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 4 [Rattus norvegicus].
ACCESSION   NP_001425045 XP_038937975
VERSION     NP_001425045.1
DBSOURCE    REFSEQ: accession NM_001438116.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937975.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.358185.1,
                                           SRR21887620.1432869.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..462
                     /product="protein LSM14 homolog A isoform 4"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=50370
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          290..399
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..462
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438116.1:142..1530"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqg
      181 rsspqldplr ksptmeqavq tasahlpapa pvgrrspvpa rplpptsqka idnqehrrae
      241 vhkvprpene qlrndskrqv vpgvpsaprr grgghrggrg rfgirrdgpm kfekdfdfes
      301 anaqfnkeei drefhnklkl kdklekqekp vngedkgdsg vdtqnsegna deedplgpnc
      361 yydktksffd niscddnrer rptwaeerrl naetfgiplr pnrgrggyrg rgglgfrggr
      421 grgsgrggtf taprgfragf rgarggrefa dfeyrkdnkv aa
//
LOCUS       NP_001101062             758 aa            linear   ROD 15-APR-2025
DEFINITION  lysyl oxidase homolog 4 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001101062 XP_001055686 XP_239059
VERSION     NP_001101062.1
DBSOURCE    REFSEQ: accession NM_001107592.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Ito,H., Akiyama,H., Iguchi,H., Iyama,K., Miyamoto,M., Ohsawa,K. and
            Nakamura,T.
  TITLE     Molecular cloning and biological activity of a novel lysyl
            oxidase-related gene expressed in cartilage
  JOURNAL   J Biol Chem 276 (26), 24023-24029 (2001)
   PUBMED   11292829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_239059.3, XP_001055686.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.7287.1,
                                           SRR26643287.3889.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..758
                     /product="lysyl oxidase homolog 4 isoform 2 precursor"
                     /EC_number="1.4.3.13"
                     /note="lysyl oxidase homolog 4"
                     /calculated_mol_wt=81920
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2841
     Region          33..133
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          177..287
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     Region          313..413
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          447..530
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          535..733
                     /region_name="Lysyl_oxidase"
                     /note="Lysyl oxidase; pfam01186"
                     /db_xref="CDD:460102"
     CDS             1..758
                     /gene="Loxl4"
                     /coded_by="NM_001107592.2:72..2348"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:309380"
                     /db_xref="RGD:1308588"
ORIGIN      
        1 mmwpppptfs vflllllsqv pssrpqspgt kklrlvgpan rpeegrlevl hqgqwgtvcd
       61 ddfalqeatv acrqlgfesa ltwahsakfg qgegpiwldn vrclgtedtl dqcgsngwgv
      121 sdcrhsedvg vvchprrqqg yhsekvsnal gpqgrrleev rlkpilasak rhspvtegav
      181 evryeghwrq vcdqgwtmnn srvvcgmlgf psqapvnshy yrkvwnlkmk dpksrlnglt
      241 kknsfwihrv dclgtephla kcqvqvapgr gklrpacpgg mhavvncvag phfqrqkpkp
      301 krkesgaeqe lkvrlrsgaq vgegrvevlm nrqwgtvcdh rwnlisasvv crqlgfgsar
      361 ealfgaqlgq glgpihlsev rcrgyeqtig dclalegsqn gcqhandaav rcnipdmgfq
      421 nkvrlaggrn seegvvevqv evngvprwgt vcsdhwglte amvtcrqlgl gfanfaikdt
      481 wywqgtpeak evvmsgvrcs gtemalqqcq rhgpvhcshg sgrfsagvac mnsapdlvmn
      541 aqlvqetayl edrplsmlyc aheenclsks adhmdwpygh rrllrfssqi ynlgradfrp
      601 kagrhswiwh qchrhyhsie vfthydlltl ngskvaeghk asfcledtnc psgvqrryac
      661 anfgeqgvav gcwdtyrhdi dcqwvditdv spgdyifqvv vnptndvaes dfsnnmircr
      721 ckydgqrvwl hnchtgdpyr pnaelsleqe qrlrnnli
//
LOCUS       NP_001424990            1890 aa            linear   ROD 15-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424990 XP_063121018
VERSION     NP_001424990.1
DBSOURCE    REFSEQ: accession NM_001438061.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1890)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1890)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1890)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1890)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1890)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1890)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1890)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1890)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1890)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1890)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063121018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.9063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1890
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1890
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 2"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=209661
     Region          <462..>1211
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          732..917
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1758..1888
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1890
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001438061.1:260..5932"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkkispclln tlelssgeqt kalnqlervl
      241 lfknlklkmr aggmsdsskw kkqkrsprpp rhttkvmpgs elptpngaal ssnltggmpf
      301 ieaptsissa sseaastvvs pctdsglels sqatskedlt dleqagspre itttepgste
      361 igvsdqldpq egahvekaqs asvesipevl eectsptdhs dsasvhdmdy vnprgvrftq
      421 ssqkegtalv pyglpcirel frflisltnp hdrhnsevmi hmglhlltva lesapvaqcq
      481 tllglikdem crhlfqllsv erlnlyaasl rvcfllfesm rehlkfqlem yikklmeiit
      541 venpkmpyem kemaleaivq lwripsfvte lyinydcdyy csnlfedltk llsknafpvs
      601 gqlytthlls ldalltvids teahcqakvl ntlnqqekke tarpgfeavd gspdtykser
      661 aasdgkatgv psdapglhfs sggwlstehg kpgcsdleea gdsgvdkktt rkpprfscll
      721 pdprelieik nkkkllitgt eqfnqkpkkg iqflqekgll tipmdnteva qwlrenprld
      781 kkmigefvsd rknmdllesf vstfsfqglr ldealrlyle afrlpgeapv ihrllevfte
      841 hwrscngspf ansdacfala yavimlntdq hnhnvrkqna pmtleefrkn lkgvnggkdf
      901 eqdiledmyh aikneeivmp eeqtglvren yvwsvllhrg atpegiflrv ppgsydldlf
      961 tmtwgptiaa lsyvfdksle etiiqkaisg frkcamisah yglsdvfdnl iislckftal
     1021 ssesienlps vfgsnpkahi aaktvfhlah rhgdilregw knimeamlql fraqllpkam
     1081 vevedfvdpn gkislqreet psnrgestvl sfvswltlsg peqssvrgps tenqeakrva
     1141 ldcikqcdpe kmiteskflq leslqelmka lvsvtpdeet ydeedaafcl emllrivlen
     1201 rdrvgcvwqt vrdhlyhlcv qaqdfcflve ravvgllrla irllrreeis gqvllslril
     1261 llmkpsvlsr vshqvayglh ellktnaani hsgddwatlf tllecigsgv kppdalqata
     1321 radapdagaq sdselpsyhq ndvsldrgyt sdsevytdhg rpgkmhrsat dadmansgwl
     1381 vvgkddidns kpaaglsrpg psplvnqysl tvgldlgphd tksllkcves lsfivrdaah
     1441 itpdnfelcv ktlrifveas lnggcksqdk rgkshkydsk gnrfkkkpke gsmlrrpras
     1501 sqhatraghs deeedegvpa syhtvslqll dlmhtlhtra asiysswaee qrhletggrk
     1561 ieadsrtlwa hcwcpllqgi aclccdarrq vrmqaltylq rallvhdlqk ldalewescf
     1621 nkvlfplltk llenispadv ggmeetrmra stllskvflq hlspllslst faalwltild
     1681 fmdkymhags sdllseavpe slknmllvmd taeifhsada rggspsalwe itweridcfl
     1741 phlrdelfkq tviqdpmpte phsqkplast hltpaagdpr mpghppppei psevgacdpe
     1801 kpestraass sspgspvass pskqspapeg ppplaqppli lqpltsplqv gvppmtlpii
     1861 lnpalieats pvpllatprp tdpiptsevn
//
LOCUS       NP_001121051             671 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001121051 XP_341828
VERSION     NP_001121051.1
DBSOURCE    REFSEQ: accession NM_001127579.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On May 24, 2008 this sequence version replaced XP_341828.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166499.1, SRR26360172.1256701.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..671
                     /product="proline and serine-rich protein 3 isoform 1"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70181
     Region          <219..514
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          588..>632
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..671
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001127579.2:133..2148"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaag
      121 ageptgrsav tgpcptgmss tslasvplqr vkqslnswns amleletlsl qsraakller
      181 skaslsssss spspneasss sfpissdgls pcsvtfnpds nkssspkepv lgaapvpsqa
      241 ipaprpasaq atlkpeedil yqwrqrrkle qslqgagdgt wvlprtpalt tqtpvsavnl
      301 gskgtqpnca ppwgsvaqpp ppqafymerp plsgpsphiw apgthgvlwa pqanpwiplg
      361 mvpttlltst laplaslpvp ptstsaatap isapqvsipg ppasapppct sapastvplp
      421 dnpqgpttpe lsssvhpkkl spkprcvsas srqettgpdt aafespcsql rgalsqvvta
      481 rlfsdsledm ppseadsrkv katssqakvp ppppesrrgs ktesrkskvt lsaeagdpqp
      541 atapkastls evqslefkks tpkkgagdal ttappassha psedllsqaa rllqaaedsd
      601 gsefpedsvl rvlraqrael rqqkrnvdaq lsllldhted pgfssppars psssprmrlr
      661 regaslearr p
//
LOCUS       NP_001424984             340 aa            linear   ROD 15-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424984
VERSION     NP_001424984.1
DBSOURCE    REFSEQ: accession NM_001438055.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR22582419.1807386.1, SRR21887621.940300.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..340
                     /product="LIM domain-binding protein 1 isoform 4"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=38818
     Region          70..271
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     CDS             1..340
                     /gene="Ldb1"
                     /coded_by="NM_001438055.1:259..1281"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 msvgcacpgc ssksfklysp keppngnafp pfhpgtmldr dvgptpmypp tylepgigrh
       61 tpygnqtdyr ifelnkrlqn wteecdnlww daftteffed damltitfcl edgpkrytig
      121 rtlipryfrs ifeggately yvlkhpkeaf hsnfvsldcd qgsmvtqhgk pmftqvcveg
      181 rlylefmfdd mmriktwhfs irqhrelipr silamhaqdp qmldqlskni trcglsnstl
      241 nylrlcvile pmqelmsrhk tyslsprdcl ktclfqkwqr mvappaepar qqpskrrkrk
      301 msggstmssg ggntnnsnsk kkspastfal ssqksqlvni
//
LOCUS       NP_001425036             630 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425036 XP_063122541
VERSION     NP_001425036.1
DBSOURCE    REFSEQ: accession NM_001438107.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122541.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.246566.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..630
                     /product="proline and serine-rich protein 3 isoform 3"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=65680
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..630
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438107.1:133..2025"
                     /note="isoform 3 is encoded by transcript variant 12"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaegmwm
      601 pnypsswttl ktqdfhllqp ghlpvpqecg
//
LOCUS       NP_001101945             376 aa            linear   ROD 15-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001101945 XP_001075571 XP_341800
VERSION     NP_001101945.2
DBSOURCE    REFSEQ: accession NM_001108475.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 4, 2008 this sequence version replaced NP_001101945.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168841.1, SRR21887621.1410644.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..376
                     /product="vasodilator-stimulated phosphoprotein isoform 2"
                     /calculated_mol_wt=39593
     Region          6..114
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(17,24,72,74,80,82,84)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          216..239
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(223..224,226..227,230,232..236)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          232..235
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          340..372
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..376
                     /gene="Vasp"
                     /coded_by="NM_001108475.3:300..1430"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 msnetvicss ratvmlydds nkrwlpagtg pqafsrvqiy hnptansfrv vgrklqpdqq
       61 vvincaiirg vkynqatpif hqwrdarqvw glnfgskeda aqfaigmana lealegggpp
      121 papappawst qngpspeele qqkrqpehle rrvsnaggpp appaggpppp pgpppppgpp
      181 pppglppsgv sgaghgtgva pppapplpta qgpssggsga pglaaaiaga klrkvskeea
      241 sggplapkae nsrgtggglm eemnamlarr rkatqvgekp pkdesasqee searipaqse
      301 pvrrpwekns ttlprmksss svttseahps vpsssddsdl ervkqelvee vrkelqkmke
      361 eiievfvqel rkrgsp
//
LOCUS       NP_001178563            1861 aa            linear   ROD 15-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001178563 XP_219953
VERSION     NP_001178563.1
DBSOURCE    REFSEQ: accession NM_001191634.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1861)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1861)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1861)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1861)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1861)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1861)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1861)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1861)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1861)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1861)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_219953.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5862.1,
                                           SRR26643295.6953.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1861
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1861
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 4"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=206394
     Region          <429..>1178
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          699..884
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1729..1859
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1861
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001191634.2:260..5845"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkklkmragg msdsskwkkq krsprpprht
      241 tkvmpgselp tpngaalssn ltggmpfiea ptsissasse aastvvspct dsglelssqa
      301 tskedltdle qagspreitt tepgsteigv sdqldpqega hvekaqsasv esipevleec
      361 tsptdhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsverl nlyaaslrvc
      481 fllfesmreh lkfqlemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfedltklls knafpvsgql ytthllslda lltvidstea hcqakvlntl
      601 nqqekketar pgfeavdgsp dtykseraas dgkatgvpsd apglhfssgg wlstehgkpg
      661 csdleeagds gvdkkttrkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn mdllesfvst fsfqglrlde
      781 alrlyleafr lpgeapvihr llevftehwr scngspfans dacfalayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik neeivmpeeq tglvrenyvw
      901 svllhrgatp egiflrvppg sydldlftmt wgptiaalsy vfdksleeti iqkaisgfrk
      961 camisahygl sdvfdnliis lckftalsse sienlpsvfg snpkahiaak tvfhlahrhg
     1021 dilregwkni meamlqlfra qllpkamvev edfvdpngki slqreetpsn rgestvlsfv
     1081 swltlsgpeq ssvrgpsten qeakrvaldc ikqcdpekmi teskflqles lqelmkalvs
     1141 vtpdeetyde edaafcleml lrivlenrdr vgcvwqtvrd hlyhlcvqaq dfcflverav
     1201 vgllrlairl lrreeisgqv llslrilllm kpsvlsrvsh qvayglhell ktnaanihsg
     1261 ddwatlftll ecigsgvkpp dalqatarad apdagaqsds elpsyhqndv sldrgytsds
     1321 evytdhgrpg kmhrsatdad mansgwlvvg kddidnskpa aglsrpgpsp lvnqysltvg
     1381 ldlgphdtks llkcveslsf ivrdaahitp dnfelcvktl rifveaslng gcksqdkrgk
     1441 shkydskgnr fkkkpkegsm lrrprassqh atraghsdee edegvpasyh tvslqvsqdl
     1501 ldlmhtlhtr aasiysswae eqrhletggr kieadsrtlw ahcwcpllqg iaclccdarr
     1561 qvrmqaltyl qrallvhdlq kldalewesc fnkvlfpllt kllenispad vggmeetrmr
     1621 astllskvfl qhlspllsls tfaalwltil dfmdkymhag ssdllseavp eslknmllvm
     1681 dtaeifhsad arggspsalw eitweridcf lphlrdelfk qtviqdpmpt ephsqkplas
     1741 thltpaagdp rmpghppppe ipsevgacdp ekpestraas ssspgspvas spskqspape
     1801 gppplaqppl ilqpltsplq vgvppmtlpi ilnpalieat spvpllatpr ptdpiptsev
     1861 n
//
LOCUS       NP_001424973            1383 aa            linear   ROD 15-APR-2025
DEFINITION  inactive cell surface hyaluronidase CEMIP2 [Rattus norvegicus].
ACCESSION   NP_001424973 XP_006231228
VERSION     NP_001424973.1
DBSOURCE    REFSEQ: accession NM_001438044.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1383)
  AUTHORS   Wu,M., Wang,C., Gong,Y., Huang,Y., Jiang,L., Zhang,M., Gao,R. and
            Dang,B.
  TITLE     Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury
  JOURNAL   Int J Mol Med 52 (6) (2023)
   PUBMED   37888730
  REMARK    GeneRIF: Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury.
REFERENCE   2  (residues 1 to 1383)
  AUTHORS   Yamamoto,H., Tobisawa,Y., Inubushi,T., Irie,F., Ohyama,C. and
            Yamaguchi,Y.
  TITLE     A mammalian homolog of the zebrafish transmembrane protein 2
            (TMEM2) is the long-sought-after cell-surface hyaluronidase
  JOURNAL   J Biol Chem 292 (18), 7304-7313 (2017)
   PUBMED   28246172
REFERENCE   3  (residues 1 to 1383)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1383)
  AUTHORS   Zhao,Q., Peng,L., Huang,W., Li,Q., Pei,Y., Yuan,P., Zheng,L.,
            Zhang,Y., Deng,J., Zhong,C., Hu,B., Ding,H., Fang,W., Li,R.,
            Liao,Q., Lin,C., Deng,W., Yan,H., Hou,J., Wu,Q., Xu,T., Liu,J.,
            Hu,L., Peng,T., Chen,S., Lai,K.N., Yuen,M.F., Wang,Y., Maini,M.K.,
            Li,C., Li,M., Wang,J., Zhang,X., Sham,P.C., Wang,J., Gao,Z.L. and
            Wang,Y.
  TITLE     Rare inborn errors associated with chronic hepatitis B virus
            infection
  JOURNAL   Hepatology 56 (5), 1661-1670 (2012)
   PUBMED   22610944
REFERENCE   5  (residues 1 to 1383)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 1383)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231228.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5227.1,
                                           SRR26360186.1614737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1383
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1383
                     /product="inactive cell surface hyaluronidase CEMIP2"
                     /EC_number="3.2.1.35"
                     /note="transmembrane protein 2; cell surface
                     hyaluronidase"
                     /calculated_mol_wt=153824
     Region          132..244
                     /region_name="G8"
                     /note="G8 domain; pfam10162"
                     /db_xref="CDD:462971"
     Region          220..387
                     /region_name="PANDER_like_TMEM2"
                     /note="PANDER-like domain of the transmembrane protein
                     TMEM2; cd13938"
                     /db_xref="CDD:260112"
     Region          1244..1328
                     /region_name="ILEI"
                     /note="Interleukin-like EMT inducer; pfam15711"
                     /db_xref="CDD:464817"
     CDS             1..1383
                     /gene="Cemip2"
                     /gene_synonym="Tmem2"
                     /coded_by="NM_001438044.1:105..4256"
                     /db_xref="GeneID:309400"
                     /db_xref="RGD:1307941"
ORIGIN      
        1 myaagsrghs paflqpqngn ghrspgyvpg kvvpfrpapp pknhasaklt srsqeapatf
       61 afspeeqrtp redrkqkrhk ntficfaits fsffvtlavi lgisskyapd encpdqnprl
      121 rnwdpgqdsa khivikegdm lrltsdatvn siviqdggll vfgddkdgsr nitlrtryil
      181 iqdggalhig aekcryrska titlygksde hesmptfgkk figveaggtl elhgarrtsw
      241 tmlartlhss glpfgsyafe kdfsrglnvr vidqdtarvl ehekfdthey hnesrrlqef
      301 lraqdpgriv aiavgdsavk sllqgtiqmi qdrlgskliq glgyrqawal vgvidggsss
      361 cnesvrnyen hstggkalaq gefytldgqk fsvtaysewi egislsgfrv diadgvklhl
      421 lddvsswgag drivvastdy smyqaeeltl lpcpecsrfq vkvkeipqyl hvgeiidgid
      481 mraevglltr niviqgeted scyadnhcqf fdydtfgghv mieknftsvh lsyvelkhmg
      541 qqhlgrypvh fhlcgdvdsk ggyrvptsvn glsihhsfsr citvhgssgl likdtigfdt
      601 lghcffledg veqrnilfhn lglltkpgtl lptdrnssmc tvmrdgvfgn yipvpttdcm
      661 avstfwiahp nnhlinnaaa gsqdagiwyl fhkeptgess gmqllekpel tplgifynnr
      721 vhsnfkaglf vdkgvkttns sasdpreylc ldnsarfrph qdadpekprv aavidrliaf
      781 knndngawvr ggdiivqnsa fadngkgltf asdgsfpsde gssqevsesl fvgesknygs
      841 qggqnkymgt ggidqkprtl prnrtfpirg fqiydgpihl tkstfkkyvp tpdryssaig
      901 flmknswqtt prnnvslvkf gpqvslnvff gkpgpwfedc eldgdknsif hdidgsvtgy
      961 kdtyvgrmdn ylirhpncvs vtkwnavvcs gtyaqvyvqt wntpnlsmii trdeypshpm
     1021 vlrginqrai spqyqpvvml ekgytihwsg paprttflyl vnfnkddwir vglcypsnts
     1081 fqvtvgflqr qngslsriee yepaqsmeel qkkpserkfy fdsgtgllfl ylrahshrdg
     1141 hsycssqgce rvkiqaatds kdmsncmaka ypqyykkpsa vkrmpamltg fcqgcgthqm
     1201 vfssdphksy lpvrfqspgk aeiqrgepsv isvngtdftf rsagaflliv dacsvpfrlt
     1261 ekrmflsadi shleeylkas ipprsivlls trgeikqmni sdsfvllgla kpahlynkgs
     1321 tvflgfsgnf tpswtrlfts pdvqglgvle qylplqmeey gcsrtssvhr rdlellqqal
     1381 kgl
//
LOCUS       NP_001424982             409 aa            linear   ROD 15-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424982 XP_006231556
VERSION     NP_001424982.1
DBSOURCE    REFSEQ: accession NM_001438053.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231556.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166757.1, SRR22582416.1262732.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..409
                     /product="LIM domain-binding protein 1 isoform 2"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=46175
     Region          70..271
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     Region          334..362
                     /region_name="LID"
                     /note="LIM interaction domain (LID); pfam17916"
                     /db_xref="CDD:465564"
     CDS             1..409
                     /gene="Ldb1"
                     /coded_by="NM_001438053.1:259..1488"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 msvgcacpgc ssksfklysp keppngnafp pfhpgtmldr dvgptpmypp tylepgigrh
       61 tpygnqtdyr ifelnkrlqn wteecdnlww daftteffed damltitfcl edgpkrytig
      121 rtlipryfrs ifeggately yvlkhpkeaf hsnfvsldcd qgsmvtqhgk pmftqvcveg
      181 rlylefmfdd mmriktwhfs irqhrelipr silamhaqdp qmldqlskni trcglsnstl
      241 nylrlcvile pmqelmsrhk tyslsprdcl ktclfqkwqr mvappaepar qqpskrrkrk
      301 msggstmssg ggntnnsnsk kkspastfal ssqdvmvvge ptlmggefgd ederlitrle
      361 ntqfdaangi ddedsfnnsp alganspwns kppssqesks enptsqasq
//
LOCUS       NP_001121024             468 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 7 [Rattus norvegicus].
ACCESSION   NP_001121024 XP_001079562 XP_341842
VERSION     NP_001121024.1
DBSOURCE    REFSEQ: accession NM_001127552.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before May 23, 2008 this sequence version replaced
            XP_341842.2, XP_001079562.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166537.1, SRR21887623.1153182.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676810
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..468
                     /product="protein LSM14 homolog A isoform 7"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=51096
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          290..400
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..468
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001127552.2:142..1548"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqg
      181 rsspqldplr ksptmeqavq tasahlpapa pvgrrspvpa rplpptsqka idnqehrrae
      241 vhkvprpene qlrndskrqv vpgvpsaprr grgghrggrg rfgirrdgpm kfekdfdfes
      301 anaqfnkeei drefhnklkl kedklekqek pvngedkgds gvdtqnsegn adeedplgpn
      361 cyydktksff dniscddnre rrptwaeerr lnaetfgipl rpnrgrggyr grgglgfrgg
      421 rgrgsgrggt ftaprgfrag frgarggref adfeyrttkl lhslqtsl
//
LOCUS       NP_001425017             363 aa            linear   ROD 15-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001425017
VERSION     NP_001425017.1
DBSOURCE    REFSEQ: accession NM_001438088.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.1195.1,
                                           SRR26643298.1771.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..363
                     /product="vasodilator-stimulated phosphoprotein isoform 5"
                     /calculated_mol_wt=38241
     Region          1..100
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(3,10,58,60,66,68,70)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          202..228
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(209..210,212..213,216,218..222)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          218..221
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          327..359
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..363
                     /gene="Vasp"
                     /coded_by="NM_001438088.1:398..1489"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 mlyddsnkrw lpagtgpqaf srvqiyhnpt ansfrvvgrk lqpdqqvvin caiirgvkyn
       61 qatpifhqwr darqvwglnf gskedaaqfa igmanaleal egggpppapa ppawstqngp
      121 speeleqqkr qpehlerrvs naggppappa ggpppppgpp pppgpppppg lppsgvsgag
      181 hgtgvapppa pplptaqgps sggsgapgla aaiagaklrk vskqeeasgg plapkaensr
      241 gtggglmeem namlarrrka tqvgekppkd esasqeesea ripaqsepvr rpweknsttl
      301 prmkssssvt tseahpsvps ssddsdlerv kqelveevrk elqkmkeeii evfvqelrkr
      361 gsp
//
LOCUS       NP_001425044             462 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425044 XP_038937978
VERSION     NP_001425044.1
DBSOURCE    REFSEQ: accession NM_001438115.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937978.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1984193.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..462
                     /product="protein LSM14 homolog A isoform 3"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=50346
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          290..399
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..462
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438115.1:142..1530"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqg
      181 rsspqldplr ksptmeqavq tasahlpapa pvgrrspvpa rplpptsqka idnqehrrae
      241 vhkvprpene qlrndskrqv vpgvpsaprr grgghrggrg rfgirrdgpm kfekdfdfes
      301 anaqfnkeei drefhnklkl kdklekqekp vngedkgdsg vdtqnsegna deedplgpnc
      361 yydktksffd niscddnrer rptwaeerrl naetfgiplr pnrgrggyrg rgglgfrggr
      421 grgsgrggtf taprgfragf rgarggrefa dfeyrkttaf gp
//
LOCUS       NP_001424962             166 aa            linear   ROD 15-APR-2025
DEFINITION  programmed cell death 1 ligand 2 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424962 XP_038935912
VERSION     NP_001424962.1
DBSOURCE    REFSEQ: accession NM_001438033.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Wang,T., Chen,S., Wang,X., Huang,Y., Qiu,J., Fei,Y., Chaulagain,A.,
            Chen,Y., Wang,Y., Lin,L., Yan,B., Wang,Y., Wang,W., Zhao,W. and
            Zhong,Z.
  TITLE     Aberrant PD-1 ligand expression contributes to the myocardial
            inflammatory injury caused by Coxsackievirus B infection
  JOURNAL   Antiviral Res 166, 1-10 (2019)
   PUBMED   30904424
REFERENCE   2  (residues 1 to 166)
  AUTHORS   He,H., Zhou,Y., Zhou,Y., Zhuang,J., He,X., Wang,S. and Lin,W.
  TITLE     Dexmedetomidine Mitigates Microglia-Mediated Neuroinflammation
            through Upregulation of Programmed Cell Death Protein 1 in a Rat
            Spinal Cord Injury Model
  JOURNAL   J Neurotrauma 35 (21), 2591-2603 (2018)
   PUBMED   29665726
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Wilson,J.K., Zhao,Y., Singer,M., Spencer,J. and Shankar-Hari,M.
  TITLE     Lymphocyte subset expression and serum concentrations of PD-1/PD-L1
            in sepsis - pilot study
  JOURNAL   Crit Care 22 (1), 95 (2018)
   PUBMED   29661225
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Singh,A., Mohan,A., Dey,A.B. and Mitra,D.K.
  TITLE     Inhibiting the programmed death 1 pathway rescues Mycobacterium
            tuberculosis-specific interferon gamma-producing T cells from
            apoptosis in patients with pulmonary tuberculosis
  JOURNAL   J Infect Dis 208 (4), 603-615 (2013)
   PUBMED   23661793
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Cao,J., Liu,F.X. and Yu,M.X.
  TITLE     Expression of programmed death 1 and its ligands in the liver of
            autoimmune hepatitis C57BL/6 mice
  JOURNAL   Chin Med J (Engl) 122 (16), 1941-1946 (2009)
   PUBMED   19781375
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Vogt,L., Schmitz,N., Kurrer,M.O., Bauer,M., Hinton,H.I., Behnke,S.,
            Gatto,D., Sebbel,P., Beerli,R.R., Sonderegger,I., Kopf,M.,
            Saudan,P. and Bachmann,M.F.
  TITLE     VSIG4, a B7 family-related protein, is a negative regulator of T
            cell activation
  JOURNAL   J Clin Invest 116 (10), 2817-2826 (2006)
   PUBMED   17016562
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Liang,S.C., Greenwald,R.J., Latchman,Y.E., Rosas,L., Satoskar,A.,
            Freeman,G.J. and Sharpe,A.H.
  TITLE     PD-L1 and PD-L2 have distinct roles in regulating host immunity to
            cutaneous leishmaniasis
  JOURNAL   Eur J Immunol 36 (1), 58-64 (2006)
   PUBMED   16358363
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Brown,J.A., Dorfman,D.M., Ma,F.R., Sullivan,E.L., Munoz,O.,
            Wood,C.R., Greenfield,E.A. and Freeman,G.J.
  TITLE     Blockade of programmed death-1 ligands on dendritic cells enhances
            T cell activation and cytokine production
  JOURNAL   J Immunol 170 (3), 1257-1266 (2003)
   PUBMED   12538684
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Tseng,S.Y., Otsuji,M., Gorski,K., Huang,X., Slansky,J.E., Pai,S.I.,
            Shalabi,A., Shin,T., Pardoll,D.M. and Tsuchiya,H.
  TITLE     B7-DC, a new dendritic cell molecule with potent costimulatory
            properties for T cells
  JOURNAL   J Exp Med 193 (7), 839-846 (2001)
   PUBMED   11283156
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Latchman,Y., Wood,C.R., Chernova,T., Chaudhary,D., Borde,M.,
            Chernova,I., Iwai,Y., Long,A.J., Brown,J.A., Nunes,R.,
            Greenfield,E.A., Bourque,K., Boussiotis,V.A., Carter,L.L.,
            Carreno,B.M., Malenkovich,N., Nishimura,H., Okazaki,T., Honjo,T.,
            Sharpe,A.H. and Freeman,G.J.
  TITLE     PD-L2 is a second ligand for PD-1 and inhibits T cell activation
  JOURNAL   Nat Immunol 2 (3), 261-268 (2001)
   PUBMED   11224527
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038935912.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.4213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..166
                     /product="programmed cell death 1 ligand 2 isoform 2
                     precursor"
                     /note="PD-1 ligand 2; PDCD1 ligand 2; programmed death
                     ligand 2"
                     /calculated_mol_wt=16514
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2114
     Region          25..106
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          50..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          76..80
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          87..92
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          102..105
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..166
                     /gene="Pdcd1lg2"
                     /gene_synonym="PD-L2"
                     /coded_by="NM_001438033.1:287..787"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:309304"
                     /db_xref="RGD:1306403"
ORIGIN      
        1 mlllllilnl ssqlhhiaas yvridtgile vpgtgevqli cqargyplae vswqnvsvpa
       61 ntshirtpeg lyqvtsvlrl kpqpnrnfsc mfwnahmkel tsaiidplsw mepkvprtrs
      121 lhafipactv aliflatvia qrkrlwgkly srkrsepavl gvgkiq
//
LOCUS       NP_001425035             630 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425035 XP_063122544
VERSION     NP_001425035.1
DBSOURCE    REFSEQ: accession NM_001438106.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122544.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2177364.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..630
                     /product="proline and serine-rich protein 3 isoform 3"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=65680
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..630
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438106.1:345..2237"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaegmwm
      601 pnypsswttl ktqdfhllqp ghlpvpqecg
//
LOCUS       NP_001425028             670 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425028 XP_063122529
VERSION     NP_001425028.1
DBSOURCE    REFSEQ: accession NM_001438099.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122529.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.1404.1,
                                           SRR26643299.1996.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438099.1:200..2212"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001425019             362 aa            linear   ROD 15-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001425019
VERSION     NP_001425019.1
DBSOURCE    REFSEQ: accession NM_001438090.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.1300.1,
                                           SRR26643299.1441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..362
                     /product="vasodilator-stimulated phosphoprotein isoform 6"
                     /calculated_mol_wt=38113
     Region          1..100
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(3,10,58,60,66,68,70)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          202..228
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(209..210,212..213,216,218..222)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          218..221
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          326..358
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..362
                     /gene="Vasp"
                     /coded_by="NM_001438090.1:398..1486"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 mlyddsnkrw lpagtgpqaf srvqiyhnpt ansfrvvgrk lqpdqqvvin caiirgvkyn
       61 qatpifhqwr darqvwglnf gskedaaqfa igmanaleal egggpppapa ppawstqngp
      121 speeleqqkr qpehlerrvs naggppappa ggpppppgpp pppgpppppg lppsgvsgag
      181 hgtgvapppa pplptaqgps sggsgapgla aaiagaklrk vskqeeasgg plapkaensr
      241 gtggglmeem namlarrrka tqvgekppkd esaseesear ipaqsepvrr pweknsttlp
      301 rmkssssvtt seahpsvpss sddsdlervk qelveevrke lqkmkeeiie vfvqelrkrg
      361 sp
//
LOCUS       NP_001424993            1858 aa            linear   ROD 15-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424993 XP_006231563
VERSION     NP_001424993.1
DBSOURCE    REFSEQ: accession NM_001438064.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1858)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1858)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1858)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1858)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1858)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1858)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1858)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1858)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1858)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1858)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231563.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5861.1,
                                           SRR26643292.6685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1858
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1858
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 5"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=206092
     Region          <430..>1179
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          700..885
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1726..1856
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1858
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001438064.1:260..5836"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkklkmragg msdsskwkkq krsprpprht
      241 tkvmpgselp tpngaalssn ltggmpfiea ptsissasse aastvvspct dsglelssqa
      301 tskedltdle qagspreitt tepgsteigv sdqldpqqeg ahvekaqsas vesipevlee
      361 ctsptdhsds asvhdmdyvn prgvrftqss qkegtalvpy glpcirelfr flisltnphd
      421 rhnsevmihm glhlltvale sapvaqcqtl lglikdemcr hlfqllsver lnlyaaslrv
      481 cfllfesmre hlkfqlemyi kklmeiitve npkmpyemke maleaivqlw ripsfvtely
      541 inydcdyycs nlfedltkll sknafpvsgq lytthllsld alltvidste ahcqakvlnt
      601 lnqqekketa rpgfeavdgs pdtykseraa sdgkatgvps dapglhfssg gwlstehgkp
      661 gcsdleeagd sgvdkkttrk pprfscllpd prelieiknk kkllitgteq fnqkpkkgiq
      721 flqekgllti pmdntevaqw lrenprldkk migefvsdrk nmdllesfvs tfsfqglrld
      781 ealrlyleaf rlpgeapvih rllevftehw rscngspfan sdacfalaya vimlntdqhn
      841 hnvrkqnapm tleefrknlk gvnggkdfeq diledmyhai kneeivmpee qtglvrenyv
      901 wsvllhrgat pegiflrvpp gsydldlftm twgptiaals yvfdksleet iiqkaisgfr
      961 kcamisahyg lsdvfdnlii slckftalss esienlpsvf gsnpkahiaa ktvfhlahrh
     1021 gdilregwkn imeamlqlfr aqllpkamve vedfvdpngk islqreetps nrgestvlsf
     1081 vswltlsgpe qssvrgpste nqeakrvald cikqcdpekm iteskflqle slqelmkalv
     1141 svtpdeetyd eedaafclem llrivlenrd rvgcvwqtvr dhlyhlcvqa qdfcflvera
     1201 vvgllrlair llrreeisgq vllslrilll mkpsvlsrvs hqvayglhel lktnaanihs
     1261 gddwatlftl lecigsgvkp pdalqatara dapdagaqsd selpsyhqnd vsldrgytsd
     1321 sevytdhgrp gkmhrsatda dmansgwlvv gkddidnskp aaglsrpgps plvnqysltv
     1381 gldlgphdtk sllkcvesls fivrdaahit pdnfelcvkt lrifveasln ggcksqdkrg
     1441 kshkydskgn rfkkkpkegs mlrrprassq hatraghsde eedegvpasy htvslqlldl
     1501 mhtlhtraas iysswaeeqr hletggrkie adsrtlwahc wcpllqgiac lccdarrqvr
     1561 mqaltylqra llvhdlqkld alewescfnk vlfplltkll enispadvgg meetrmrast
     1621 llskvflqhl spllslstfa alwltildfm dkymhagssd llseavpesl knmllvmdta
     1681 eifhsadarg gspsalweit weridcflph lrdelfkqtv iqdpmpteph sqkplasthl
     1741 tpaagdprmp ghppppeips evgacdpekp estraassss pgspvassps kqspapegpp
     1801 plaqpplilq pltsplqvgv ppmtlpiiln palieatspv pllatprptd piptsevn
//
LOCUS       NP_001425016             375 aa            linear   ROD 15-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001425016
VERSION     NP_001425016.1
DBSOURCE    REFSEQ: accession NM_001438087.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.1724454.1,
                                           SRR21887623.3178864.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..375
                     /product="vasodilator-stimulated phosphoprotein isoform 4"
                     /calculated_mol_wt=39464
     Region          6..114
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(17,24,72,74,80,82,84)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          216..239
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(223..224,226..227,230,232..236)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          232..235
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          339..371
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..375
                     /gene="Vasp"
                     /coded_by="NM_001438087.1:300..1427"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 msnetvicss ratvmlydds nkrwlpagtg pqafsrvqiy hnptansfrv vgrklqpdqq
       61 vvincaiirg vkynqatpif hqwrdarqvw glnfgskeda aqfaigmana lealegggpp
      121 papappawst qngpspeele qqkrqpehle rrvsnaggpp appaggpppp pgpppppgpp
      181 pppglppsgv sgaghgtgva pppapplpta qgpssggsga pglaaaiaga klrkvskeea
      241 sggplapkae nsrgtggglm eemnamlarr rkatqvgekp pkdesasees earipaqsep
      301 vrrpweknst tlprmkssss vttseahpsv psssddsdle rvkqelveev rkelqkmkee
      361 iievfvqelr krgsp
//
LOCUS       NP_001425006            1192 aa            linear   ROD 15-APR-2025
DEFINITION  VPS10 domain-containing receptor SorCS1 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001425006 XP_006231583
VERSION     NP_001425006.1
DBSOURCE    REFSEQ: accession NM_001438077.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Yau,B., Blood,Z., An,Y., Su,Z. and Kebede,M.A.
  TITLE     Type 2 diabetes-associated single nucleotide polymorphism in Sorcs1
            gene results in alternative processing of the Sorcs1 protein in
            INS1 beta-cells
  JOURNAL   Sci Rep 9 (1), 19466 (2019)
   PUBMED   31857633
  REMARK    GeneRIF: Type 2 diabetes-associated single nucleotide polymorphism
            in Sorcs1 gene results in alternative processing of the Sorcs1
            protein in INS1 beta-cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Ribeiro,L.F., Verpoort,B., Nys,J., Vennekens,K.M., Wierda,K.D. and
            de Wit,J.
  TITLE     SorCS1-mediated sorting in dendrites maintains neurexin axonal
            surface polarization required for synaptic function
  JOURNAL   PLoS Biol 17 (10), e3000466 (2019)
   PUBMED   31658245
  REMARK    GeneRIF: SorCS1-mediated sorting in dendritic endosomes controls
            Nrxn axonal surface polarization required for proper synapse
            development and function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Lazar,J., O'Meara,C.C., Sarkis,A.B., Prisco,S.Z., Xu,H., Fox,C.S.,
            Chen,M.H., Broeckel,U., Arnett,D.K., Moreno,C., Provoost,A.P. and
            Jacob,H.J.
  TITLE     SORCS1 contributes to the development of renal disease in rats and
            humans
  JOURNAL   Physiol Genomics 45 (16), 720-728 (2013)
   PUBMED   23780848
  REMARK    GeneRIF: The experimental data from the rat combined with
            association results from different ethnic groups indicates a role
            for SORCS1 in maintaining proper renal function.
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Hermey,G., Keat,S.J., Madsen,P., Jacobsen,C., Petersen,C.M. and
            Gliemann,J.
  TITLE     Characterization of sorCS1, an alternatively spliced receptor with
            completely different cytoplasmic domains that mediate different
            trafficking in cells
  JOURNAL   J Biol Chem 278 (9), 7390-7396 (2003)
   PUBMED   12482870
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231583.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.8485.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1192
                     /product="VPS10 domain-containing receptor SorCS1 isoform
                     2 precursor"
                     /note="VPS10 domain-containing receptor SorCS1; VPS10
                     domain receptor protein SORCS 1"
                     /calculated_mol_wt=129799
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3004
     Region          196..793
                     /region_name="VPS10"
                     /note="VPS10 domain; smart00602"
                     /db_xref="CDD:214740"
     Region          807..880
                     /region_name="PKD"
                     /note="PKD domain; pfam00801"
                     /db_xref="CDD:395646"
     Region          836..>973
                     /region_name="COG3291"
                     /note="Uncharacterized conserved protein, PKD repeat
                     domain [Function unknown]"
                     /db_xref="CDD:442520"
     CDS             1..1192
                     /gene="Sorcs1"
                     /coded_by="NM_001438077.1:250..3828"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:309533"
                     /db_xref="RGD:1305910"
ORIGIN      
        1 mgkvgagdgs saalsalltg agllmllapg icsslsccpp qhpsstprwt ltprgfsypg
       61 plgrapatpp plfmrplfav apgdralfle raggsrvsva tasrsgrrrr sgmdpektep
      121 gegtsrsrrd mlrdggqqgp gtgardpdka trfrmeelrl tsttfaltgd sahnqamvhw
      181 sghnssvili ltklydynlg sitesslwrs tdygttyekl ndkvglktil sylyvcptnk
      241 rkimlltdpe iessllissd egatyqkyrl nfyiqsllfh pkqedwilay sqdqklyssa
      301 efgrrwqliq eavvpnrfyw svlgsnkepd lvhleartvd ghsiyltcrm qncteanrnk
      361 pfpgyidpds livqddyvfv qltsggrphy yvsyrrnpfa qmklpkyalp kdmhvistde
      421 nqvfaavqew nqndtynlyi sdtrgvyftl alenvqssrg pegnvmidly evagikgmfl
      481 ankkidnqvk tfitynkgrd wrllqapdad lrgdpvhcll pycslhlhlk vsenpytsgi
      541 iasrdtapsi ivasgnigse lsdsdismfv ssdagntwrq ifeeehsily ldqggvlvam
      601 khtslpirhl wlsfdegrsw skysftsipl fvdgvlgepg eetlimtvfg hfshrsewql
      661 vkvdyksifd rrcaeedyrp wqlhsqgeac imgakriykk rkserkcmqg tyagamesep
      721 cvcteadfdc dygyerhssg qclpafwfnp sslskdcslg qsylnstgyr kvvsnnctdg
      781 vreqytakpq kcpgkaprgl rivtadgklt aeqghnvtlm vqleegdvqr tliqvdfgdg
      841 iavsyvnlss medgikhvyq nvgifrvtvq vdnslgsdsa vlylhvtcpl ehvhlslpfv
      901 ttknkevnat avlwpsqvgt ltyvwwygnn teplitlegs isfkftsegm ntitvqvsag
      961 nailqdtkti avyeefrslr lafspnlddy npdipewrrd isrvikkslv eatgipsqhi
     1021 lvavlpglpt aaelfvlpyq dgarenkrsp edleqisevl ihklnqnlvh felkpgvqvl
     1081 vhaahltaap lvdltpthsg samlmllsvv fvglavfviy kfkrgwrdrs avknigcscr
     1141 gpgfnaqhqq ggsqasvtsv prdttpssdl hghqehtwct dlhpgktpih ik
//
LOCUS       NP_001425031             670 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425031 XP_063122526
VERSION     NP_001425031.1
DBSOURCE    REFSEQ: accession NM_001438102.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122526.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1530787.1,
                                           SRR26360176.2185401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438102.1:342..2354"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001425034             670 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425034 XP_063122534
VERSION     NP_001425034.1
DBSOURCE    REFSEQ: accession NM_001438105.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122534.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1119264.1,
                                           SRR26643296.1165.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438105.1:129..2141"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001424983             342 aa            linear   ROD 15-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424983
VERSION     NP_001424983.1
DBSOURCE    REFSEQ: accession NM_001438054.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR22582419.1807386.1, SRR21887621.940300.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..342
                     /product="LIM domain-binding protein 1 isoform 3"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=39014
     Region          70..271
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     CDS             1..342
                     /gene="Ldb1"
                     /coded_by="NM_001438054.1:259..1287"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 msvgcacpgc ssksfklysp keppngnafp pfhpgtmldr dvgptpmypp tylepgigrh
       61 tpygnqtdyr ifelnkrlqn wteecdnlww daftteffed damltitfcl edgpkrytig
      121 rtlipryfrs ifeggately yvlkhpkeaf hsnfvsldcd qgsmvtqhgk pmftqvcveg
      181 rlylefmfdd mmriktwhfs irqhrelipr silamhaqdp qmldqlskni trcglsnstl
      241 nylrlcvile pmqelmsrhk tyslsprdcl ktclfqkwqr mvappaepar qqpskrrkrk
      301 msggstmssg ggntnnsnsk kkspastfal ssqvpksqlv ni
//
LOCUS       NP_001424963              76 aa            linear   ROD 15-APR-2025
DEFINITION  programmed cell death 1 ligand 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424963
VERSION     NP_001424963.1
DBSOURCE    REFSEQ: accession NM_001438034.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Wang,T., Chen,S., Wang,X., Huang,Y., Qiu,J., Fei,Y., Chaulagain,A.,
            Chen,Y., Wang,Y., Lin,L., Yan,B., Wang,Y., Wang,W., Zhao,W. and
            Zhong,Z.
  TITLE     Aberrant PD-1 ligand expression contributes to the myocardial
            inflammatory injury caused by Coxsackievirus B infection
  JOURNAL   Antiviral Res 166, 1-10 (2019)
   PUBMED   30904424
REFERENCE   2  (residues 1 to 76)
  AUTHORS   He,H., Zhou,Y., Zhou,Y., Zhuang,J., He,X., Wang,S. and Lin,W.
  TITLE     Dexmedetomidine Mitigates Microglia-Mediated Neuroinflammation
            through Upregulation of Programmed Cell Death Protein 1 in a Rat
            Spinal Cord Injury Model
  JOURNAL   J Neurotrauma 35 (21), 2591-2603 (2018)
   PUBMED   29665726
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Wilson,J.K., Zhao,Y., Singer,M., Spencer,J. and Shankar-Hari,M.
  TITLE     Lymphocyte subset expression and serum concentrations of PD-1/PD-L1
            in sepsis - pilot study
  JOURNAL   Crit Care 22 (1), 95 (2018)
   PUBMED   29661225
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Singh,A., Mohan,A., Dey,A.B. and Mitra,D.K.
  TITLE     Inhibiting the programmed death 1 pathway rescues Mycobacterium
            tuberculosis-specific interferon gamma-producing T cells from
            apoptosis in patients with pulmonary tuberculosis
  JOURNAL   J Infect Dis 208 (4), 603-615 (2013)
   PUBMED   23661793
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Cao,J., Liu,F.X. and Yu,M.X.
  TITLE     Expression of programmed death 1 and its ligands in the liver of
            autoimmune hepatitis C57BL/6 mice
  JOURNAL   Chin Med J (Engl) 122 (16), 1941-1946 (2009)
   PUBMED   19781375
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Vogt,L., Schmitz,N., Kurrer,M.O., Bauer,M., Hinton,H.I., Behnke,S.,
            Gatto,D., Sebbel,P., Beerli,R.R., Sonderegger,I., Kopf,M.,
            Saudan,P. and Bachmann,M.F.
  TITLE     VSIG4, a B7 family-related protein, is a negative regulator of T
            cell activation
  JOURNAL   J Clin Invest 116 (10), 2817-2826 (2006)
   PUBMED   17016562
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Liang,S.C., Greenwald,R.J., Latchman,Y.E., Rosas,L., Satoskar,A.,
            Freeman,G.J. and Sharpe,A.H.
  TITLE     PD-L1 and PD-L2 have distinct roles in regulating host immunity to
            cutaneous leishmaniasis
  JOURNAL   Eur J Immunol 36 (1), 58-64 (2006)
   PUBMED   16358363
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Brown,J.A., Dorfman,D.M., Ma,F.R., Sullivan,E.L., Munoz,O.,
            Wood,C.R., Greenfield,E.A. and Freeman,G.J.
  TITLE     Blockade of programmed death-1 ligands on dendritic cells enhances
            T cell activation and cytokine production
  JOURNAL   J Immunol 170 (3), 1257-1266 (2003)
   PUBMED   12538684
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Tseng,S.Y., Otsuji,M., Gorski,K., Huang,X., Slansky,J.E., Pai,S.I.,
            Shalabi,A., Shin,T., Pardoll,D.M. and Tsuchiya,H.
  TITLE     B7-DC, a new dendritic cell molecule with potent costimulatory
            properties for T cells
  JOURNAL   J Exp Med 193 (7), 839-846 (2001)
   PUBMED   11283156
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Latchman,Y., Wood,C.R., Chernova,T., Chaudhary,D., Borde,M.,
            Chernova,I., Iwai,Y., Long,A.J., Brown,J.A., Nunes,R.,
            Greenfield,E.A., Bourque,K., Boussiotis,V.A., Carter,L.L.,
            Carreno,B.M., Malenkovich,N., Nishimura,H., Okazaki,T., Honjo,T.,
            Sharpe,A.H. and Freeman,G.J.
  TITLE     PD-L2 is a second ligand for PD-1 and inhibits T cell activation
  JOURNAL   Nat Immunol 2 (3), 261-268 (2001)
   PUBMED   11224527
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2443027.1,
                                           SRR26643293.8384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..76
                     /product="programmed cell death 1 ligand 2 isoform 3"
                     /note="PD-1 ligand 2; PDCD1 ligand 2; programmed death
                     ligand 2"
                     /calculated_mol_wt=8545
     Region          <1..16
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          12..15
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..76
                     /gene="Pdcd1lg2"
                     /gene_synonym="PD-L2"
                     /coded_by="NM_001438034.1:868..1098"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:309304"
                     /db_xref="RGD:1306403"
ORIGIN      
        1 mfwnahmkel tsaiidplsw mepkvprtrs lhafipactv aliflatvia qrkrlwgkly
       61 srkrsepavl gvgkiq
//
LOCUS       NP_001424972            1383 aa            linear   ROD 15-APR-2025
DEFINITION  inactive cell surface hyaluronidase CEMIP2 [Rattus norvegicus].
ACCESSION   NP_001424972 XP_038936097
VERSION     NP_001424972.1
DBSOURCE    REFSEQ: accession NM_001438043.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1383)
  AUTHORS   Wu,M., Wang,C., Gong,Y., Huang,Y., Jiang,L., Zhang,M., Gao,R. and
            Dang,B.
  TITLE     Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury
  JOURNAL   Int J Mol Med 52 (6) (2023)
   PUBMED   37888730
  REMARK    GeneRIF: Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury.
REFERENCE   2  (residues 1 to 1383)
  AUTHORS   Yamamoto,H., Tobisawa,Y., Inubushi,T., Irie,F., Ohyama,C. and
            Yamaguchi,Y.
  TITLE     A mammalian homolog of the zebrafish transmembrane protein 2
            (TMEM2) is the long-sought-after cell-surface hyaluronidase
  JOURNAL   J Biol Chem 292 (18), 7304-7313 (2017)
   PUBMED   28246172
REFERENCE   3  (residues 1 to 1383)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1383)
  AUTHORS   Zhao,Q., Peng,L., Huang,W., Li,Q., Pei,Y., Yuan,P., Zheng,L.,
            Zhang,Y., Deng,J., Zhong,C., Hu,B., Ding,H., Fang,W., Li,R.,
            Liao,Q., Lin,C., Deng,W., Yan,H., Hou,J., Wu,Q., Xu,T., Liu,J.,
            Hu,L., Peng,T., Chen,S., Lai,K.N., Yuen,M.F., Wang,Y., Maini,M.K.,
            Li,C., Li,M., Wang,J., Zhang,X., Sham,P.C., Wang,J., Gao,Z.L. and
            Wang,Y.
  TITLE     Rare inborn errors associated with chronic hepatitis B virus
            infection
  JOURNAL   Hepatology 56 (5), 1661-1670 (2012)
   PUBMED   22610944
REFERENCE   5  (residues 1 to 1383)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 1383)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038936097.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5228.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1383
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1383
                     /product="inactive cell surface hyaluronidase CEMIP2"
                     /EC_number="3.2.1.35"
                     /note="transmembrane protein 2; cell surface
                     hyaluronidase"
                     /calculated_mol_wt=153824
     Region          132..244
                     /region_name="G8"
                     /note="G8 domain; pfam10162"
                     /db_xref="CDD:462971"
     Region          220..387
                     /region_name="PANDER_like_TMEM2"
                     /note="PANDER-like domain of the transmembrane protein
                     TMEM2; cd13938"
                     /db_xref="CDD:260112"
     Region          1244..1328
                     /region_name="ILEI"
                     /note="Interleukin-like EMT inducer; pfam15711"
                     /db_xref="CDD:464817"
     CDS             1..1383
                     /gene="Cemip2"
                     /gene_synonym="Tmem2"
                     /coded_by="NM_001438043.1:591..4742"
                     /db_xref="GeneID:309400"
                     /db_xref="RGD:1307941"
ORIGIN      
        1 myaagsrghs paflqpqngn ghrspgyvpg kvvpfrpapp pknhasaklt srsqeapatf
       61 afspeeqrtp redrkqkrhk ntficfaits fsffvtlavi lgisskyapd encpdqnprl
      121 rnwdpgqdsa khivikegdm lrltsdatvn siviqdggll vfgddkdgsr nitlrtryil
      181 iqdggalhig aekcryrska titlygksde hesmptfgkk figveaggtl elhgarrtsw
      241 tmlartlhss glpfgsyafe kdfsrglnvr vidqdtarvl ehekfdthey hnesrrlqef
      301 lraqdpgriv aiavgdsavk sllqgtiqmi qdrlgskliq glgyrqawal vgvidggsss
      361 cnesvrnyen hstggkalaq gefytldgqk fsvtaysewi egislsgfrv diadgvklhl
      421 lddvsswgag drivvastdy smyqaeeltl lpcpecsrfq vkvkeipqyl hvgeiidgid
      481 mraevglltr niviqgeted scyadnhcqf fdydtfgghv mieknftsvh lsyvelkhmg
      541 qqhlgrypvh fhlcgdvdsk ggyrvptsvn glsihhsfsr citvhgssgl likdtigfdt
      601 lghcffledg veqrnilfhn lglltkpgtl lptdrnssmc tvmrdgvfgn yipvpttdcm
      661 avstfwiahp nnhlinnaaa gsqdagiwyl fhkeptgess gmqllekpel tplgifynnr
      721 vhsnfkaglf vdkgvkttns sasdpreylc ldnsarfrph qdadpekprv aavidrliaf
      781 knndngawvr ggdiivqnsa fadngkgltf asdgsfpsde gssqevsesl fvgesknygs
      841 qggqnkymgt ggidqkprtl prnrtfpirg fqiydgpihl tkstfkkyvp tpdryssaig
      901 flmknswqtt prnnvslvkf gpqvslnvff gkpgpwfedc eldgdknsif hdidgsvtgy
      961 kdtyvgrmdn ylirhpncvs vtkwnavvcs gtyaqvyvqt wntpnlsmii trdeypshpm
     1021 vlrginqrai spqyqpvvml ekgytihwsg paprttflyl vnfnkddwir vglcypsnts
     1081 fqvtvgflqr qngslsriee yepaqsmeel qkkpserkfy fdsgtgllfl ylrahshrdg
     1141 hsycssqgce rvkiqaatds kdmsncmaka ypqyykkpsa vkrmpamltg fcqgcgthqm
     1201 vfssdphksy lpvrfqspgk aeiqrgepsv isvngtdftf rsagaflliv dacsvpfrlt
     1261 ekrmflsadi shleeylkas ipprsivlls trgeikqmni sdsfvllgla kpahlynkgs
     1321 tvflgfsgnf tpswtrlfts pdvqglgvle qylplqmeey gcsrtssvhr rdlellqqal
     1381 kgl
//
LOCUS       NP_001425046             404 aa            linear   ROD 15-APR-2025
DEFINITION  protein LSM14 homolog A isoform 5 [Rattus norvegicus].
ACCESSION   NP_001425046 XP_038937984
VERSION     NP_001425046.1
DBSOURCE    REFSEQ: accession NM_001438117.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937984.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.2096.1,
                                           SRR26643288.2011.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676810 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..404
                     /product="protein LSM14 homolog A isoform 5"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=44132
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          231..341
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..404
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438117.1:142..1356"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqa
      181 evhkvprpen eqlrndskrq vvpgvpsapr rgrgghrggr grfgirrdgp mkfekdfdfe
      241 sanaqfnkee idrefhnklk lkedklekqe kpvngedkgd sgvdtqnseg nadeedplgp
      301 ncyydktksf fdniscddnr errptwaeer rlnaetfgip lrpnrgrggy rgrgglgfrg
      361 grgrgsgrgg tftaprgfra gfrgarggre fadfeyrkdn kvaa
//
LOCUS       NP_001424991            1862 aa            linear   ROD 15-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424991 XP_006231562
VERSION     NP_001424991.1
DBSOURCE    REFSEQ: accession NM_001438062.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1862)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1862)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1862)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1862)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1862)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1862)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1862)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1862)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1862)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1862)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231562.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.2281.1,
                                           SRR26643296.4646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1862
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1862
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 3"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=206522
     Region          <430..>1179
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          700..885
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1730..1860
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1862
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001438062.1:260..5848"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkklkmragg msdsskwkkq krsprpprht
      241 tkvmpgselp tpngaalssn ltggmpfiea ptsissasse aastvvspct dsglelssqa
      301 tskedltdle qagspreitt tepgsteigv sdqldpqqeg ahvekaqsas vesipevlee
      361 ctsptdhsds asvhdmdyvn prgvrftqss qkegtalvpy glpcirelfr flisltnphd
      421 rhnsevmihm glhlltvale sapvaqcqtl lglikdemcr hlfqllsver lnlyaaslrv
      481 cfllfesmre hlkfqlemyi kklmeiitve npkmpyemke maleaivqlw ripsfvtely
      541 inydcdyycs nlfedltkll sknafpvsgq lytthllsld alltvidste ahcqakvlnt
      601 lnqqekketa rpgfeavdgs pdtykseraa sdgkatgvps dapglhfssg gwlstehgkp
      661 gcsdleeagd sgvdkkttrk pprfscllpd prelieiknk kkllitgteq fnqkpkkgiq
      721 flqekgllti pmdntevaqw lrenprldkk migefvsdrk nmdllesfvs tfsfqglrld
      781 ealrlyleaf rlpgeapvih rllevftehw rscngspfan sdacfalaya vimlntdqhn
      841 hnvrkqnapm tleefrknlk gvnggkdfeq diledmyhai kneeivmpee qtglvrenyv
      901 wsvllhrgat pegiflrvpp gsydldlftm twgptiaals yvfdksleet iiqkaisgfr
      961 kcamisahyg lsdvfdnlii slckftalss esienlpsvf gsnpkahiaa ktvfhlahrh
     1021 gdilregwkn imeamlqlfr aqllpkamve vedfvdpngk islqreetps nrgestvlsf
     1081 vswltlsgpe qssvrgpste nqeakrvald cikqcdpekm iteskflqle slqelmkalv
     1141 svtpdeetyd eedaafclem llrivlenrd rvgcvwqtvr dhlyhlcvqa qdfcflvera
     1201 vvgllrlair llrreeisgq vllslrilll mkpsvlsrvs hqvayglhel lktnaanihs
     1261 gddwatlftl lecigsgvkp pdalqatara dapdagaqsd selpsyhqnd vsldrgytsd
     1321 sevytdhgrp gkmhrsatda dmansgwlvv gkddidnskp aaglsrpgps plvnqysltv
     1381 gldlgphdtk sllkcvesls fivrdaahit pdnfelcvkt lrifveasln ggcksqdkrg
     1441 kshkydskgn rfkkkpkegs mlrrprassq hatraghsde eedegvpasy htvslqvsqd
     1501 lldlmhtlht raasiysswa eeqrhletgg rkieadsrtl wahcwcpllq giaclccdar
     1561 rqvrmqalty lqrallvhdl qkldalewes cfnkvlfpll tkllenispa dvggmeetrm
     1621 rastllskvf lqhlspllsl stfaalwlti ldfmdkymha gssdllseav peslknmllv
     1681 mdtaeifhsa darggspsal weitweridc flphlrdelf kqtviqdpmp tephsqkpla
     1741 sthltpaagd prmpghpppp eipsevgacd pekpestraa sssspgspva sspskqspap
     1801 egppplaqpp lilqpltspl qvgvppmtlp iilnpaliea tspvpllatp rptdpiptse
     1861 vn
//
LOCUS       NP_001424989            1894 aa            linear   ROD 15-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424989 XP_006231559
VERSION     NP_001424989.1
DBSOURCE    REFSEQ: accession NM_001438060.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1894)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1894)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1894)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1894)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1894)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1894)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1894)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1894)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1894)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1894)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231559.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.4647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1894
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1894
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 1"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=210090
     Region          <462..>1211
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          732..917
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1762..1892
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1894
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001438060.1:260..5944"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkkispclln tlelssgeqt kalnqlervl
      241 lfknlklkmr aggmsdsskw kkqkrsprpp rhttkvmpgs elptpngaal ssnltggmpf
      301 ieaptsissa sseaastvvs pctdsglels sqatskedlt dleqagspre itttepgste
      361 igvsdqldpq egahvekaqs asvesipevl eectsptdhs dsasvhdmdy vnprgvrftq
      421 ssqkegtalv pyglpcirel frflisltnp hdrhnsevmi hmglhlltva lesapvaqcq
      481 tllglikdem crhlfqllsv erlnlyaasl rvcfllfesm rehlkfqlem yikklmeiit
      541 venpkmpyem kemaleaivq lwripsfvte lyinydcdyy csnlfedltk llsknafpvs
      601 gqlytthlls ldalltvids teahcqakvl ntlnqqekke tarpgfeavd gspdtykser
      661 aasdgkatgv psdapglhfs sggwlstehg kpgcsdleea gdsgvdkktt rkpprfscll
      721 pdprelieik nkkkllitgt eqfnqkpkkg iqflqekgll tipmdnteva qwlrenprld
      781 kkmigefvsd rknmdllesf vstfsfqglr ldealrlyle afrlpgeapv ihrllevfte
      841 hwrscngspf ansdacfala yavimlntdq hnhnvrkqna pmtleefrkn lkgvnggkdf
      901 eqdiledmyh aikneeivmp eeqtglvren yvwsvllhrg atpegiflrv ppgsydldlf
      961 tmtwgptiaa lsyvfdksle etiiqkaisg frkcamisah yglsdvfdnl iislckftal
     1021 ssesienlps vfgsnpkahi aaktvfhlah rhgdilregw knimeamlql fraqllpkam
     1081 vevedfvdpn gkislqreet psnrgestvl sfvswltlsg peqssvrgps tenqeakrva
     1141 ldcikqcdpe kmiteskflq leslqelmka lvsvtpdeet ydeedaafcl emllrivlen
     1201 rdrvgcvwqt vrdhlyhlcv qaqdfcflve ravvgllrla irllrreeis gqvllslril
     1261 llmkpsvlsr vshqvayglh ellktnaani hsgddwatlf tllecigsgv kppdalqata
     1321 radapdagaq sdselpsyhq ndvsldrgyt sdsevytdhg rpgkmhrsat dadmansgwl
     1381 vvgkddidns kpaaglsrpg psplvnqysl tvgldlgphd tksllkcves lsfivrdaah
     1441 itpdnfelcv ktlrifveas lnggcksqdk rgkshkydsk gnrfkkkpke gsmlrrpras
     1501 sqhatraghs deeedegvpa syhtvslqvs qdlldlmhtl htraasiyss waeeqrhlet
     1561 ggrkieadsr tlwahcwcpl lqgiaclccd arrqvrmqal tylqrallvh dlqkldalew
     1621 escfnkvlfp lltkllenis padvggmeet rmrastllsk vflqhlspll slstfaalwl
     1681 tildfmdkym hagssdllse avpeslknml lvmdtaeifh sadarggsps alweitweri
     1741 dcflphlrde lfkqtviqdp mptephsqkp lasthltpaa gdprmpghpp ppeipsevga
     1801 cdpekpestr aasssspgsp vasspskqsp apegppplaq pplilqplts plqvgvppmt
     1861 lpiilnpali eatspvplla tprptdpipt sevn
//
LOCUS       NP_001424960             965 aa            linear   ROD 15-APR-2025
DEFINITION  fanconi-associated nuclease 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424960 XP_038935867
VERSION     NP_001424960.1
DBSOURCE    REFSEQ: accession NM_001438031.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Wang,R., Persky,N.S., Yoo,B., Ouerfelli,O., Smogorzewska,A.,
            Elledge,S.J. and Pavletich,N.P.
  TITLE     DNA repair. Mechanism of DNA interstrand cross-link processing by
            repair nuclease FAN1
  JOURNAL   Science 346 (6213), 1127-1130 (2014)
   PUBMED   25430771
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Pennell,S., Declais,A.C., Li,J., Haire,L.F., Berg,W.,
            Saldanha,J.W., Taylor,I.A., Rouse,J., Lilley,D.M. and Smerdon,S.J.
  TITLE     FAN1 activity on asymmetric repair intermediates is mediated by an
            atypical monomeric virus-type replication-repair nuclease domain
  JOURNAL   Cell Rep 8 (1), 84-93 (2014)
   PUBMED   24981866
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Smogorzewska,A., Desetty,R., Saito,T.T., Schlabach,M., Lach,F.P.,
            Sowa,M.E., Clark,A.B., Kunkel,T.A., Harper,J.W., Colaiacovo,M.P.
            and Elledge,S.J.
  TITLE     A genetic screen identifies FAN1, a Fanconi anemia-associated
            nuclease necessary for DNA interstrand crosslink repair
  JOURNAL   Mol Cell 39 (1), 36-47 (2010)
   PUBMED   20603073
REFERENCE   4  (residues 1 to 965)
  AUTHORS   Kratz,K., Schopf,B., Kaden,S., Sendoel,A., Eberhard,R.,
            Lademann,C., Cannavo,E., Sartori,A.A., Hengartner,M.O. and
            Jiricny,J.
  TITLE     Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes
            cells to interstrand crosslinking agents
  JOURNAL   Cell 142 (1), 77-88 (2010)
   PUBMED   20603016
REFERENCE   5  (residues 1 to 965)
  AUTHORS   MacKay,C., Declais,A.C., Lundin,C., Agostinho,A., Deans,A.J.,
            MacArtney,T.J., Hofmann,K., Gartner,A., West,S.C., Helleday,T.,
            Lilley,D.M. and Rouse,J.
  TITLE     Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to
            DNA damage by monoubiquitinated FANCD2
  JOURNAL   Cell 142 (1), 65-76 (2010)
   PUBMED   20603015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038935867.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.524325.1,
                                           SRR26360194.2141613.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..965
                     /product="fanconi-associated nuclease 1 isoform 2"
                     /EC_number="3.1.4.1"
                     /note="coiled-coil domain-containing protein MTMR15;
                     myotubularin related protein 15; fanconi-associated
                     nuclease 1; FANCD2/FANCI-associated nuclease 1"
                     /calculated_mol_wt=106267
     Region          376..965
                     /region_name="FAN1-like"
                     /note="repair nuclease FAN1; cd22326"
                     /db_xref="CDD:411730"
     Site            order(376..377,423,427..428,436,439,476..478,495..497,576,
                     579..581,584,623,675,678,681..682,684,709,713,716,
                     720..721,724,742..743,900,928,930,934)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411730"
     CDS             1..965
                     /gene="Fan1"
                     /gene_synonym="Mtmr15; RGD1566323"
                     /coded_by="NM_001438031.1:384..3281"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:309256"
                     /db_xref="RGD:1566323"
ORIGIN      
        1 mmsqksspaq krprkslstg kttksqshsi tsyfnsvppa klacsichkm vprydlirhl
       61 descanngei vqnepaqagl instvptsdl pstpledmtp qklsppkrrl isaqcgsklg
      121 vrqqtspyfk kalvcknqnk lpnqsveirs lgslssklsr ryvkakksls kneglashcp
      181 ptspsppgps lvdncpemdn kdeilnssqk eniyscaple eetaseqkvk sskrmgdgsq
      241 kasggepalt paspeqaptl lssdltlvnn tdsssgdale qegagrvgvg vdeqlaacsh
      301 eevqmtvdae vgtlvsggae snspadnddd dastwsnnpe lreagsalkr qracspleqg
      361 ascvpsvtaq pqpshpyylr sflvvlqail eneedmklfd dqekgviakf yqlsasgqkl
      421 yvrlfqrklt wikvskleye eiasdltpvv eelknlgflq teselqelsd vlellsapel
      481 kalaktfhlv spggqkqqlv daflklarqr svytwgktqp giravilkra kdlagpslrv
      541 ckgpravfcr llllfsltdt medeeaacgg qgqlstvllv nlgrmefpqy sisrktqifr
      601 dredliryaa aahmlsdisa amasgnweea kelsqiakrd wdqlkshpsl ryhealplfl
      661 rcftvgwiyt rissravevl erlhmyeeav kelenllaqk vycpdsrgrw wdrlalnlhq
      721 hlkrleevti tgrlcpqhgm gksvfviegg dptnpttilc sveelaldyy rrsgfdqgih
      781 gegstfstlc glllwdiifm dgipdvfrna yqaspldllt dsffssreqa learlqlihs
      841 apaeslrawv teawqaqqgr aaslvswdrf tslqqaqdlv sclggpvlsg vcrrlaadfr
      901 hcrgglpdlv vwnsqshhck lvevkgpsdr lsckqmiwld elqklgadve vchvvavgak
      961 skglg
//
LOCUS       NP_001425032             670 aa            linear   ROD 15-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425032 XP_063122525
VERSION     NP_001425032.1
DBSOURCE    REFSEQ: accession NM_001438103.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_063122525.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.469754.1,
                                           SRR26360190.2516552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438103.1:345..2357"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001424985             373 aa            linear   ROD 15-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001424985
VERSION     NP_001424985.1
DBSOURCE    REFSEQ: accession NM_001438056.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.419480.1,
                                           SRR21887621.297554.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..373
                     /product="LIM domain-binding protein 1 isoform 5"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=42452
     Region          34..235
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     Region          298..326
                     /region_name="LID"
                     /note="LIM interaction domain (LID); pfam17916"
                     /db_xref="CDD:465564"
     CDS             1..373
                     /gene="Ldb1"
                     /coded_by="NM_001438056.1:675..1796"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 mldrdvgptp mypptylepg igrhtpygnq tdyrifelnk rlqnwteecd nlwwdaftte
       61 ffeddamlti tfcledgpkr ytigrtlipr yfrsifegga telyyvlkhp keafhsnfvs
      121 ldcdqgsmvt qhgkpmftqv cvegrlylef mfddmmrikt whfsirqhre liprsilamh
      181 aqdpqmldql sknitrcgls nstlnylrlc vilepmqelm srhktyslsp rdclktclfq
      241 kwqrmvappa eparqqpskr rkrkmsggst mssgggntnn snskkkspas tfalssqdvm
      301 vvgeptlmgg efgdederli trlentqfda angiddedsf nnspalgans pwnskppssq
      361 esksenptsq asq
//
LOCUS       NP_001178492            1168 aa            linear   ROD 15-APR-2025
DEFINITION  VPS10 domain-containing receptor SorCS1 isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_001178492 XP_002728940
VERSION     NP_001178492.1
DBSOURCE    REFSEQ: accession NM_001191563.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Yau,B., Blood,Z., An,Y., Su,Z. and Kebede,M.A.
  TITLE     Type 2 diabetes-associated single nucleotide polymorphism in Sorcs1
            gene results in alternative processing of the Sorcs1 protein in
            INS1 beta-cells
  JOURNAL   Sci Rep 9 (1), 19466 (2019)
   PUBMED   31857633
  REMARK    GeneRIF: Type 2 diabetes-associated single nucleotide polymorphism
            in Sorcs1 gene results in alternative processing of the Sorcs1
            protein in INS1 beta-cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Ribeiro,L.F., Verpoort,B., Nys,J., Vennekens,K.M., Wierda,K.D. and
            de Wit,J.
  TITLE     SorCS1-mediated sorting in dendrites maintains neurexin axonal
            surface polarization required for synaptic function
  JOURNAL   PLoS Biol 17 (10), e3000466 (2019)
   PUBMED   31658245
  REMARK    GeneRIF: SorCS1-mediated sorting in dendritic endosomes controls
            Nrxn axonal surface polarization required for proper synapse
            development and function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Lazar,J., O'Meara,C.C., Sarkis,A.B., Prisco,S.Z., Xu,H., Fox,C.S.,
            Chen,M.H., Broeckel,U., Arnett,D.K., Moreno,C., Provoost,A.P. and
            Jacob,H.J.
  TITLE     SORCS1 contributes to the development of renal disease in rats and
            humans
  JOURNAL   Physiol Genomics 45 (16), 720-728 (2013)
   PUBMED   23780848
  REMARK    GeneRIF: The experimental data from the rat combined with
            association results from different ethnic groups indicates a role
            for SORCS1 in maintaining proper renal function.
REFERENCE   4  (residues 1 to 1168)
  AUTHORS   Hermey,G., Keat,S.J., Madsen,P., Jacobsen,C., Petersen,C.M. and
            Gliemann,J.
  TITLE     Characterization of sorCS1, an alternatively spliced receptor with
            completely different cytoplasmic domains that mediate different
            trafficking in cells
  JOURNAL   J Biol Chem 278 (9), 7390-7396 (2003)
   PUBMED   12482870
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_002728940.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1168
                     /product="VPS10 domain-containing receptor SorCS1 isoform
                     3 precursor"
                     /note="VPS10 domain-containing receptor SorCS1; VPS10
                     domain receptor protein SORCS 1"
                     /calculated_mol_wt=126984
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3004
     Region          196..793
                     /region_name="VPS10"
                     /note="VPS10 domain; smart00602"
                     /db_xref="CDD:214740"
     Region          807..880
                     /region_name="PKD"
                     /note="PKD domain; pfam00801"
                     /db_xref="CDD:395646"
     Region          836..>973
                     /region_name="COG3291"
                     /note="Uncharacterized conserved protein, PKD repeat
                     domain [Function unknown]"
                     /db_xref="CDD:442520"
     CDS             1..1168
                     /gene="Sorcs1"
                     /coded_by="NM_001191563.1:1..3507"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:309533"
                     /db_xref="RGD:1305910"
ORIGIN      
        1 mgkvgagdgs saalsalltg agllmllapg icsslsccpp qhpsstprwt ltprgfsypg
       61 plgrapatpp plfmrplfav apgdralfle raggsrvsva tasrsgrrrr sgmdpektep
      121 gegtsrsrrd mlrdggqqgp gtgardpdka trfrmeelrl tsttfaltgd sahnqamvhw
      181 sghnssvili ltklydynlg sitesslwrs tdygttyekl ndkvglktil sylyvcptnk
      241 rkimlltdpe iessllissd egatyqkyrl nfyiqsllfh pkqedwilay sqdqklyssa
      301 efgrrwqliq eavvpnrfyw svlgsnkepd lvhleartvd ghsiyltcrm qncteanrnk
      361 pfpgyidpds livqddyvfv qltsggrphy yvsyrrnpfa qmklpkyalp kdmhvistde
      421 nqvfaavqew nqndtynlyi sdtrgvyftl alenvqssrg pegnvmidly evagikgmfl
      481 ankkidnqvk tfitynkgrd wrllqapdad lrgdpvhcll pycslhlhlk vsenpytsgi
      541 iasrdtapsi ivasgnigse lsdsdismfv ssdagntwrq ifeeehsily ldqggvlvam
      601 khtslpirhl wlsfdegrsw skysftsipl fvdgvlgepg eetlimtvfg hfshrsewql
      661 vkvdyksifd rrcaeedyrp wqlhsqgeac imgakriykk rkserkcmqg tyagamesep
      721 cvcteadfdc dygyerhssg qclpafwfnp sslskdcslg qsylnstgyr kvvsnnctdg
      781 vreqytakpq kcpgkaprgl rivtadgklt aeqghnvtlm vqleegdvqr tliqvdfgdg
      841 iavsyvnlss medgikhvyq nvgifrvtvq vdnslgsdsa vlylhvtcpl ehvhlslpfv
      901 ttknkevnat avlwpsqvgt ltyvwwygnn teplitlegs isfkftsegm ntitvqvsag
      961 nailqdtkti avyeefrslr lafspnlddy npdipewrrd isrvikkslv eatgipsqhi
     1021 lvavlpglpt aaelfvlpyq dgarenkrsp edleqisevl ihklnqnlvh felkpgvqvl
     1081 vhaahltaap lvdltpthsg samlmllsvv fvglavfviy kfkrrvalts ppspstqpgd
     1141 sslrlqrprq atppsspkrg sagaqfai
//
LOCUS       NP_001101052             268 aa            linear   ROD 15-APR-2025
DEFINITION  programmed cell death 1 ligand 2 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001101052 XP_001079586 XP_219777
VERSION     NP_001101052.2
DBSOURCE    REFSEQ: accession NM_001107582.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wang,T., Chen,S., Wang,X., Huang,Y., Qiu,J., Fei,Y., Chaulagain,A.,
            Chen,Y., Wang,Y., Lin,L., Yan,B., Wang,Y., Wang,W., Zhao,W. and
            Zhong,Z.
  TITLE     Aberrant PD-1 ligand expression contributes to the myocardial
            inflammatory injury caused by Coxsackievirus B infection
  JOURNAL   Antiviral Res 166, 1-10 (2019)
   PUBMED   30904424
REFERENCE   2  (residues 1 to 268)
  AUTHORS   He,H., Zhou,Y., Zhou,Y., Zhuang,J., He,X., Wang,S. and Lin,W.
  TITLE     Dexmedetomidine Mitigates Microglia-Mediated Neuroinflammation
            through Upregulation of Programmed Cell Death Protein 1 in a Rat
            Spinal Cord Injury Model
  JOURNAL   J Neurotrauma 35 (21), 2591-2603 (2018)
   PUBMED   29665726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Wilson,J.K., Zhao,Y., Singer,M., Spencer,J. and Shankar-Hari,M.
  TITLE     Lymphocyte subset expression and serum concentrations of PD-1/PD-L1
            in sepsis - pilot study
  JOURNAL   Crit Care 22 (1), 95 (2018)
   PUBMED   29661225
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Singh,A., Mohan,A., Dey,A.B. and Mitra,D.K.
  TITLE     Inhibiting the programmed death 1 pathway rescues Mycobacterium
            tuberculosis-specific interferon gamma-producing T cells from
            apoptosis in patients with pulmonary tuberculosis
  JOURNAL   J Infect Dis 208 (4), 603-615 (2013)
   PUBMED   23661793
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Cao,J., Liu,F.X. and Yu,M.X.
  TITLE     Expression of programmed death 1 and its ligands in the liver of
            autoimmune hepatitis C57BL/6 mice
  JOURNAL   Chin Med J (Engl) 122 (16), 1941-1946 (2009)
   PUBMED   19781375
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Vogt,L., Schmitz,N., Kurrer,M.O., Bauer,M., Hinton,H.I., Behnke,S.,
            Gatto,D., Sebbel,P., Beerli,R.R., Sonderegger,I., Kopf,M.,
            Saudan,P. and Bachmann,M.F.
  TITLE     VSIG4, a B7 family-related protein, is a negative regulator of T
            cell activation
  JOURNAL   J Clin Invest 116 (10), 2817-2826 (2006)
   PUBMED   17016562
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Liang,S.C., Greenwald,R.J., Latchman,Y.E., Rosas,L., Satoskar,A.,
            Freeman,G.J. and Sharpe,A.H.
  TITLE     PD-L1 and PD-L2 have distinct roles in regulating host immunity to
            cutaneous leishmaniasis
  JOURNAL   Eur J Immunol 36 (1), 58-64 (2006)
   PUBMED   16358363
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Brown,J.A., Dorfman,D.M., Ma,F.R., Sullivan,E.L., Munoz,O.,
            Wood,C.R., Greenfield,E.A. and Freeman,G.J.
  TITLE     Blockade of programmed death-1 ligands on dendritic cells enhances
            T cell activation and cytokine production
  JOURNAL   J Immunol 170 (3), 1257-1266 (2003)
   PUBMED   12538684
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Tseng,S.Y., Otsuji,M., Gorski,K., Huang,X., Slansky,J.E., Pai,S.I.,
            Shalabi,A., Shin,T., Pardoll,D.M. and Tsuchiya,H.
  TITLE     B7-DC, a new dendritic cell molecule with potent costimulatory
            properties for T cells
  JOURNAL   J Exp Med 193 (7), 839-846 (2001)
   PUBMED   11283156
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Latchman,Y., Wood,C.R., Chernova,T., Chaudhary,D., Borde,M.,
            Chernova,I., Iwai,Y., Long,A.J., Brown,J.A., Nunes,R.,
            Greenfield,E.A., Bourque,K., Boussiotis,V.A., Carter,L.L.,
            Carreno,B.M., Malenkovich,N., Nishimura,H., Okazaki,T., Honjo,T.,
            Sharpe,A.H. and Freeman,G.J.
  TITLE     PD-L2 is a second ligand for PD-1 and inhibits T cell activation
  JOURNAL   Nat Immunol 2 (3), 261-268 (2001)
   PUBMED   11224527
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Aug 14, 2009 this sequence version replaced NP_001101052.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..268
                     /product="programmed cell death 1 ligand 2 isoform 1
                     precursor"
                     /note="PD-1 ligand 2; PDCD1 ligand 2; programmed death
                     ligand 2"
                     /calculated_mol_wt=27904
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2114
     Region          20..119
                     /region_name="IgV_PD-L2"
                     /note="Immunoglobulin Variable (IgV) domain of Programmed
                     death ligand 2 (PD-L2); cd20983"
                     /db_xref="CDD:409575"
     Site            order(20..22,25,28,56,60,67,101,103,105,107..110,112..114)
                     /site_type="other"
                     /note="Receptor-Ligand Binding Site [polypeptide binding]"
                     /db_xref="CDD:409575"
     Region          20..43
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409575"
     Region          22..25
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409575"
     Region          28..32
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409575"
     Region          35..43
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409575"
     Region          44..55
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409575"
     Region          55..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409575"
     Region          56..63
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409575"
     Region          64..71
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409575"
     Region          66..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409575"
     Region          72..104
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409575"
     Region          72..76
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409575"
     Region          84..91
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409575"
     Region          95..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409575"
     Region          105..108
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409575"
     Region          108..119
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409575"
     Region          110..119
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409575"
     Region          127..208
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          139..143
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          189..194
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          204..207
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..268
                     /gene="Pdcd1lg2"
                     /gene_synonym="PD-L2"
                     /coded_by="NM_001107582.4:238..1044"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:309304"
                     /db_xref="RGD:1306403"
ORIGIN      
        1 mlllllilnl ssqlhhiaal ftvtapkevy tvdfgssvsl ecdfdrrect elegiraslq
       61 kvendtssqs qratlleell plgkasfhip svqvrdsgqy rclvicgaaw dykyltvkvk
      121 asyvridtgi levpgtgevq licqargypl aevswqnvsv pantshirtp eglyqvtsvl
      181 rlkpqpnrnf scmfwnahmk eltsaiidpl swmepkvprt rslhafipac tvaliflatv
      241 iaqrkrlwgk lysrkrsepa vlgvgkiq
//
LOCUS       NP_001101071             375 aa            linear   ROD 15-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001101071 XP_001058773 XP_219948
VERSION     NP_001101071.1
DBSOURCE    REFSEQ: accession NM_001107601.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001058773.1, XP_219948.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06621351,
                              SAMN16676786 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..375
                     /product="LIM domain-binding protein 1 isoform 6"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=42648
     Region          34..235
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     Region          300..328
                     /region_name="LID"
                     /note="LIM interaction domain (LID); pfam17916"
                     /db_xref="CDD:465564"
     CDS             1..375
                     /gene="Ldb1"
                     /coded_by="NM_001107601.1:647..1774"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 mldrdvgptp mypptylepg igrhtpygnq tdyrifelnk rlqnwteecd nlwwdaftte
       61 ffeddamlti tfcledgpkr ytigrtlipr yfrsifegga telyyvlkhp keafhsnfvs
      121 ldcdqgsmvt qhgkpmftqv cvegrlylef mfddmmrikt whfsirqhre liprsilamh
      181 aqdpqmldql sknitrcgls nstlnylrlc vilepmqelm srhktyslsp rdclktclfq
      241 kwqrmvappa eparqqpskr rkrkmsggst mssgggntnn snskkkspas tfalssqvpd
      301 vmvvgeptlm ggefgdeder litrlentqf daangidded sfnnspalga nspwnskpps
      361 sqesksenpt sqasq
//
LOCUS       NP_036839                180 aa            linear   ROD 15-APR-2025
DEFINITION  pro-glucagon preproprotein [Rattus norvegicus].
ACCESSION   NP_036839
VERSION     NP_036839.2
DBSOURCE    REFSEQ: accession NM_012707.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Nakamori,H., Niimi,A., Mitsui,R. and Hashitani,H.
  TITLE     Lipopolysaccharide accelerates peristalsis by stimulating
            glucagon-like peptide-1 release from L cells in the rat proximal
            colon
  JOURNAL   J Physiol 602 (19), 4803-4820 (2024)
   PUBMED   39287487
  REMARK    GeneRIF: Lipopolysaccharide accelerates peristalsis by stimulating
            glucagon-like peptide-1 release from L cells in the rat proximal
            colon.
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Ali,I.I., D'Souza,C., Tariq,S. and Adeghate,E.A.
  TITLE     Adropin Is Expressed in Pancreatic Islet Cells and Reduces Glucagon
            Release in Diabetes Mellitus
  JOURNAL   Int J Mol Sci 25 (18), 9824 (2024)
   PUBMED   39337311
  REMARK    GeneRIF: Adropin Is Expressed in Pancreatic Islet Cells and Reduces
            Glucagon Release in Diabetes Mellitus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Randolph,A.B., Zheng,H. and Rinaman,L.
  TITLE     Populations of Hindbrain Glucagon-Like Peptide 1 (GLP1) Neurons
            That Innervate the Hypothalamic PVH, Thalamic PVT, or Limbic
            Forebrain BST Have Axon Collaterals That Reach All Central Regions
            Innervated by GLP1 Neurons
  JOURNAL   J Neurosci 44 (31), e2063232024 (2024)
   PUBMED   38811166
  REMARK    GeneRIF: Populations of Hindbrain Glucagon-Like Peptide 1 (GLP1)
            Neurons That Innervate the Hypothalamic PVH, Thalamic PVT, or
            Limbic Forebrain BST Have Axon Collaterals That Reach All Central
            Regions Innervated by GLP1 Neurons.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Wang,Q.Y., Zhang,W., Zhao,Y., Chen,H.L., Liu,Q., Wang,Z.H.,
            Zeng,L.T., Li,J., Chen,S.J., Wei,L., Iwakuma,T. and Cai,J.P.
  TITLE     Colonic L-cell impairment in aged subjects with type 2 diabetes
            leads to diminished GLP-1 production
  JOURNAL   Diabetes Metab Syndr 17 (12), 102907 (2023)
   PUBMED   37980723
  REMARK    GeneRIF: Colonic L-cell impairment in aged subjects with type 2
            diabetes leads to diminished GLP-1 production.
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Zhu,Y., Tian,J., Shao,Y.W., Zhao,J., Jia,S.H. and Shu,Q.
  TITLE     [Electroacupuncture improves obesity and promotes white adipose
            tissue browning by regulating central glucagon-like peptide-1]
  JOURNAL   Zhen Ci Yan Jiu 48 (8), 727-735 (2023)
   PUBMED   37614130
  REMARK    GeneRIF: [Electroacupuncture improves obesity and promotes white
            adipose tissue browning by regulating central glucagon-like
            peptide-1].
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Mojsov,S., Kopczynski,M.G. and Habener,J.F.
  TITLE     Both amidated and nonamidated forms of glucagon-like peptide I are
            synthesized in the rat intestine and the pancreas
  JOURNAL   J Biol Chem 265 (14), 8001-8008 (1990)
   PUBMED   1692320
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Yamato,E., Noma,Y., Tahara,Y., Ikegami,H., Yamamoto,Y., Cha,T.,
            Yoneda,H., Ogihara,T., Ohboshi,C., Hirota,M. et al.
  TITLE     Suppression of synthesis and release of glucagon by glucagon-like
            peptide-1 (7-36 amide) without affect on mRNA level in isolated rat
            islets
  JOURNAL   Biochem Biophys Res Commun 167 (2), 431-437 (1990)
   PUBMED   2182011
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Mojsov,S., Heinrich,G., Wilson,I.B., Ravazzola,M., Orci,L. and
            Habener,J.F.
  TITLE     Preproglucagon gene expression in pancreas and intestine
            diversifies at the level of post-translational processing
  JOURNAL   J Biol Chem 261 (25), 11880-11889 (1986)
   PUBMED   3528148
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Heinrich,G., Gros,P., Lund,P.K., Bentley,R.C. and Habener,J.F.
  TITLE     Pre-proglucagon messenger ribonucleic acid: nucleotide and encoded
            amino acid sequences of the rat pancreatic complementary
            deoxyribonucleic acid
  JOURNAL   Endocrinology 115 (6), 2176-2181 (1984)
   PUBMED   6548696
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Heinrich,G., Gros,P. and Habener,J.F.
  TITLE     Glucagon gene sequence. Four of six exons encode separate
            functional domains of rat pre-proglucagon
  JOURNAL   J Biol Chem 259 (22), 14082-14087 (1984)
   PUBMED   6094539
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Mar 25, 2010 this sequence version replaced NP_036839.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP480555.1, SRR26643288.13684.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN09345330 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..180
                     /product="pro-glucagon preproprotein"
                     /note="glucagon-like peptide-1; pro-glucagon;
                     glucagon-like peptide 2"
                     /calculated_mol_wt=18592
     sig_peptide     1..20
                     /calculated_mol_wt=2271
     proprotein      21..180
                     /product="glucagon proprotein"
                     /calculated_mol_wt=18592
     mat_peptide     21..89
                     /product="Glicentin.
                     /evidence=ECO:0000250|UniProtKB:P01274.
                     /id=PRO_0000011303"
                     /note="propagated from UniProtKB/Swiss-Prot (P06883.1)"
                     /calculated_mol_wt=8097
     mat_peptide     21..50
                     /product="glicentin-related polypeptide (GRPP)"
                     /calculated_mol_wt=3380
     Region          23..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06883.1)"
     Site            52..53
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P06883.1)"
     mat_peptide     53..89
                     /product="Oxyntomodulin.
                     /evidence=ECO:0000269|PubMed:7937770. /id=PRO_0000011305"
                     /note="propagated from UniProtKB/Swiss-Prot (P06883.1)"
                     /calculated_mol_wt=4450
     mat_peptide     53..81
                     /product="glucagon"
                     /calculated_mol_wt=3483
     Region          53..80
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55095; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     Site            83..84
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK1 and PCSK2.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     Site            91..92
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P06883.1)"
     mat_peptide     92..128
                     /product="Glucagon-like peptide 1.
                     /evidence=ECO:0000250|UniProtKB:P01275.
                     /id=PRO_0000011308"
                     /note="propagated from UniProtKB/Swiss-Prot (P06883.1)"
                     /calculated_mol_wt=4170
     Site            97..98
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P06883.1)"
     mat_peptide     98..128
                     /product="Glucagon-like peptide 1(7-37).
                     /evidence=ECO:0000250|UniProtKB:P01275.
                     /id=PRO_0000011309"
                     /note="propagated from UniProtKB/Swiss-Prot (P06883.1)"
                     /calculated_mol_wt=3356
     mat_peptide     98..127
                     /product="glucagon-like peptide 1 (GLP1)"
                     /calculated_mol_wt=3299
     Region          98..125
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55095; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55095; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     Site            127
                     /site_type="amidation"
                     /note="Arginine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P06883.1)"
     Site            130..131
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P06883.1)"
     Site            145..146
                     /site_type="cleavage"
                     /note="Cleavage, by PCSK1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P06883.1)"
     mat_peptide     146..178
                     /product="glucagon-like peptide 2 (GLP2)"
                     /calculated_mol_wt=3796
     Region          146..173
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55095; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06883.1)"
     CDS             1..180
                     /gene="Gcg"
                     /gene_synonym="GLP-1; Glp1; Glp2"
                     /coded_by="NM_012707.3:94..636"
                     /db_xref="GeneID:24952"
                     /db_xref="RGD:2668"
ORIGIN      
        1 mktvyivagl fvmlvqgswq hapqdteena rsfpasqtep ledpnqined krhsqgtfts
       61 dyskyldsrr aqdfvqwlmn tkrnrnniak rhdeferhae gtftsdvssy legqaakefi
      121 awlvkgrgrr dfpeevaiae elgrrhadgs fsdemntild nlatrdfinw liqtkitdkk
//
LOCUS       NP_001033064            1477 aa            linear   ROD 15-APR-2025
DEFINITION  alpha-1-inhibitor 3 precursor [Rattus norvegicus].
ACCESSION   NP_001033064 XP_216246
VERSION     NP_001033064.2
DBSOURCE    REFSEQ: accession NM_001037975.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1477)
  AUTHORS   Enghild,J.J., Salvesen,G., Thogersen,I.B. and Pizzo,S.V.
  TITLE     Proteinase binding and inhibition by the monomeric
            alpha-macroglobulin rat alpha 1-inhibitor-3
  JOURNAL   J Biol Chem 264 (19), 11428-11435 (1989)
   PUBMED   2472396
REFERENCE   2  (residues 1 to 1477)
  AUTHORS   Northemann,W., Shiels,B.R., Braciak,T.A. and Fey,G.H.
  TITLE     Structure and negative transcriptional regulation by
            glucocorticoids of the acute-phase rat alpha 1-inhibitor III gene
  JOURNAL   Biochemistry 28 (1), 84-95 (1989)
   PUBMED   2495816
REFERENCE   3  (residues 1 to 1477)
  AUTHORS   Braciak,T.A., Northemann,W., Hudson,G.O., Shiels,B.R., Gehring,M.R.
            and Fey,G.H.
  TITLE     Sequence and acute phase regulation of rat alpha 1-inhibitor III
            messenger RNA
  JOURNAL   J Biol Chem 263 (8), 3999-4012 (1988)
   PUBMED   2831216
REFERENCE   4  (residues 1 to 1477)
  AUTHORS   Schweizer,M., Takabayashi,K., Geiger,T., Laux,T., Biermann,G.,
            Buhler,J.M., Gauthier,F., Roberts,L.M. and Heinrich,P.C.
  TITLE     Identification and sequencing of cDNA clones for the rodent
            negative acute-phase protein alpha 1-inhibitor 3
  JOURNAL   Eur J Biochem 164 (2), 375-381 (1987)
   PUBMED   2436907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 4, 2012 this sequence version replaced NP_001033064.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J03552.1, SRR26643286.14756.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1477
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1477
                     /product="alpha-1-inhibitor 3 precursor"
                     /note="murinoglobulin-2-like; alpha-1-inhibitor 3;
                     alpha-1-inhibitor III; murinoglobulin 1 like 1"
                     /calculated_mol_wt=161027
     sig_peptide     1..24
                     /note="propagated from UniProtKB/Swiss-Prot (P14046.1)"
                     /calculated_mol_wt=2713
     mat_peptide     25..1477
                     /product="Alpha-1-inhibitor 3. /id=PRO_0000000061"
                     /note="propagated from UniProtKB/Swiss-Prot (P14046.1)"
                     /calculated_mol_wt=161027
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Region          <129..1349
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Region          601..750
                     /region_name="Bait region (approximate)"
                     /note="propagated from UniProtKB/Swiss-Prot (P14046.1)"
     Site            750
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            777
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            872
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Region          961..1267
                     /region_name="A2M_2"
                     /note="Proteins similar to alpha2-macroglobulin (alpha
                     (2)-M). This group also contains the pregnancy zone
                     protein (PZP). Alpha(2)-M and PZP are broadly specific
                     proteinase inhibitors. Alpha (2)-M is a major carrier
                     protein in serum. The structural thioester...; cd02897"
                     /db_xref="CDD:239227"
     Site            order(975,977..978,981,1021,1031,1034,1088,1090..1091,
                     1251)
                     /site_type="other"
                     /note="surface patch"
                     /db_xref="CDD:239227"
     Site            975..978
                     /site_type="active"
                     /note="thioester region [active]"
                     /db_xref="CDD:239227"
     Site            994
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            order(1077,1081,1083,1091)
                     /site_type="other"
                     /note="specificity defining residues"
                     /db_xref="CDD:239227"
     Site            1143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Site            1314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     Region          1377..1467
                     /region_name="A2M_recep"
                     /note="A-macroglobulin receptor binding domain; pfam07677"
                     /db_xref="CDD:462226"
     Site            1427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14046.1)"
     CDS             1..1477
                     /gene="Mug5"
                     /gene_synonym="A1i3; alpha-1-I3; Mug1l1"
                     /coded_by="NM_001037975.2:80..4513"
                     /db_xref="GeneID:297568"
                     /db_xref="RGD:1584999"
ORIGIN      
        1 mkkdreaqlc lfsallaflp fasllngnsk ymvlvpsqly tetpekiclh lyhlnetvtv
       61 taslisqrgt rklfdelvvd kdlfhcvsft iprlpsseee esldiniega khkfserrvv
      121 lvknkesvvf vqtdkpmykp gqsvkfrvvs mdknlhplne lfplayiedp kmnrimqwqd
      181 vktenglkql sfslsaepiq gpykivilkq sgvkeehsft vmefvlprfg vdvkvpnais
      241 vydeiinvta catytygkpv pghvkislch gnptfssetk sackeedsrl dnngcstqev
      301 nitefqlken ylkmhqafhv natvteegtg sefsgsgrie vertrnkflf lkadshfrhg
      361 ipffvkvrlv dikgdpipne qvlikardag ytnatttdqh glakfsidts gisdyslnik
      421 vyhkeessci hssctaerha eahhtayavy slsksyiyld teagvlpcnq ihtvqahfil
      481 kgqvlgvlqq ivfhylvmaq gsilqtgnht hqvepgesqv qgnfaleipv efsmvpvakm
      541 liytilpdge viadsvkfqv ekclrnkvql sfspsqslpa sqthmrvtas pqslcglrav
      601 dqsvllqkpe aelspsliyd lpgmqdsnfi assndpfede dyclmyqpia rekdvyryvr
      661 etglmaftnl kiklptycnt dydmvplavp avaldsstdr gmyeslpvva vksplpqepp
      721 rkdpppkdpv ietirnyfpe twiwdlvtvn ssgvtelemt vpdtitewka galclsndtg
      781 lglssvasfq afqpffvelt mpysvirgea ftlkatvlny lptslpmavl leaspdftav
      841 pvennqdsyc lgangrhtss wlvtpkslgn vnfsvsaear qspgpcgsev atvpetgrkd
      901 tvvkvlivep egikkehtfs sllcasdael setlslllpp tvvkdsarah fsvmgdilss
      961 aikntqnliq mpygcgeqnm vlfapniyvl kylnetqqlt ekikskalgy lragyqreln
     1021 ykhkdgsysa fgdhngqgqg ntwltafvlk sfaqarafif ideshitdaf twlskqqkds
     1081 gcfrssgsll nnamkggvdd eitlsayitm allesslpdt dpvvskalsc lesswenieq
     1141 ggngsfvytk almayafala gnqekrneil ksldkeaike dnsihwerpq kptksegyly
     1201 tpqassaeve msayvvlarl taqpapsped lalsmgtikw ltkqqnsygg fsstqdtvva
     1261 ldalskygaa tfsksqktps vtvqssgsfs qkfqvdksnr lllqqvslpy ipgnytvsvs
     1321 gegcvyaqtt lrynvplekq qpafalkvqt vpltcnnpkg qnsfqislei sytgsrpasn
     1381 mviadvkmls gfiplkptvk klerlghvsr tevttnnvll yldqvtnqtl sfsfiiqqdi
     1441 pvknlqpaiv kvydyyetde vafaeysspc ssddqnv
//
LOCUS       NP_001171954             319 aa            linear   ROD 15-APR-2025
DEFINITION  iron-sulfur cluster transfer protein NUBPL precursor [Rattus
            norvegicus].
ACCESSION   NP_001171954 XP_001075426 XP_216689
VERSION     NP_001171954.1
DBSOURCE    REFSEQ: accession NM_001185025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Sheftel,A.D., Stehling,O., Pierik,A.J., Netz,D.J., Kerscher,S.,
            Elsasser,H.P., Wittig,I., Balk,J., Brandt,U. and Lill,R.
  TITLE     Human ind1, an iron-sulfur cluster assembly factor for respiratory
            complex I
  JOURNAL   Mol Cell Biol 29 (22), 6059-6073 (2009)
   PUBMED   19752196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP486352.1, CO399813.1 and BF282469.1.
            
            On or before Jun 1, 2010 this sequence version replaced
            XP_216689.4, XP_001075426.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132291,
                              SAMD00132296 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..319
                     /product="iron-sulfur cluster transfer protein NUBPL
                     precursor"
                     /note="iron-sulfur protein NUBPL; nucleotide binding
                     protein-like; iron-sulfur cluster transfer protein NUBPL;
                     NUBP iron-sulfur cluster assembly factor like"
                     /calculated_mol_wt=33952
     Region          65..311
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(76..83,211,213,238..239,275..277,280..281)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(76..78,109..110,112,115..116,157..158,188,190,193,
                     217,220,276,278..279,281)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
     CDS             1..319
                     /gene="Nubpl"
                     /gene_synonym="RGD1307232"
                     /coded_by="NM_001185025.1:11..970"
                     /db_xref="GeneID:299008"
                     /db_xref="RGD:1307232"
ORIGIN      
        1 mgtwrrlllf ggvslrgggv aaalplgcra lgcgrqllga egealkqrrt qimsrglpkq
       61 kpiegvrevi vvasgkggvg ksttavnlal alaandsska vglldvdvyg psipkmmnlk
      121 gnpelspnnl mrpllnygia cmsmgflvee taplvwrglm vmsaiekllr qvdwgqldyl
      181 vvdmppgtgd vqlsvsqnip isgavivstp qdialmdahk gaemfrkvnv pvlglvqnms
      241 vfqcpqckhk thifgadgar klaqtldldv lgdvplhlsi reasdmgqpv vfsqpesdea
      301 kaylniasev vrrlksppe
//
LOCUS       NP_001258305            1485 aa            linear   ROD 15-APR-2025
DEFINITION  C3 and PZP-like, alpha-2-macroglobulin domain containing 8
            precursor [Rattus norvegicus].
ACCESSION   NP_001258305 XP_001060284 XP_003749880 XP_213006
VERSION     NP_001258305.1
DBSOURCE    REFSEQ: accession NM_001271376.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1485)
  AUTHORS   Schweizer,M., Takabayashi,K., Geiger,T., Laux,T., Biermann,G.,
            Buhler,J.M., Gauthier,F., Roberts,L.M. and Heinrich,P.C.
  TITLE     Identification and sequencing of cDNA clones for the rodent
            negative acute-phase protein alpha 1-inhibitor 3
  JOURNAL   Eur J Biochem 164 (2), 375-381 (1987)
   PUBMED   2436907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Sep 21, 2012 this sequence version replaced
            XP_001060284.1, XP_213006.5, XP_003749880.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1485
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1485
                     /product="C3 and PZP-like, alpha-2-macroglobulin domain
                     containing 8 precursor"
                     /note="alpha-1-inhibitor 3-like; C3 and PZP-like,
                     alpha-2-macroglobulin domain containing 8"
                     /calculated_mol_wt=162245
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2687
     Region          <129..1351
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
     Region          749..839
                     /region_name="A2M"
                     /note="Alpha-2-macroglobulin family; pfam00207"
                     /db_xref="CDD:459711"
     Region          969..1275
                     /region_name="A2M_2"
                     /note="Proteins similar to alpha2-macroglobulin (alpha
                     (2)-M). This group also contains the pregnancy zone
                     protein (PZP). Alpha(2)-M and PZP are broadly specific
                     proteinase inhibitors. Alpha (2)-M is a major carrier
                     protein in serum. The structural thioester...; cd02897"
                     /db_xref="CDD:239227"
     Site            order(983,985..986,989,1029,1039,1042,1096,1098..1099,
                     1259)
                     /site_type="other"
                     /note="surface patch"
                     /db_xref="CDD:239227"
     Site            983..986
                     /site_type="active"
                     /note="thioester region [active]"
                     /db_xref="CDD:239227"
     Site            order(1085,1089,1091,1099)
                     /site_type="other"
                     /note="specificity defining residues"
                     /db_xref="CDD:239227"
     Region          1385..1475
                     /region_name="A2M_recep"
                     /note="A-macroglobulin receptor binding domain; pfam07677"
                     /db_xref="CDD:462226"
     CDS             1..1485
                     /gene="Mug6"
                     /gene_synonym="Cpamd8; RGD1566313"
                     /coded_by="NM_001271376.1:1..4458"
                     /db_xref="GeneID:297572"
                     /db_xref="RGD:1566313"
ORIGIN      
        1 mwknreahlc lfsvllallp sassfngnsk ymvlvpsqly tdtpekiclh lyhlnetvtv
       61 taslisqrgt rklfdelvvd kdlfhclsft iprlpsseee esldiniega khkfskrrvv
      121 lvknkesvvf vqtdkpvykp gqsvkfrivs mdknlhplne lfplayiedp kinrimqwqd
      181 iktenglkql sfslsaepiq gpykivilkq sgvkeehsft vmefvlprfg vdvkvpnais
      241 vydeiisvta catytygkpv pgrvkislch gnpsfrsqtk sackeedsel dnngcstqev
      301 nitefrlken ylkvrqafhv natvteegtg sefsgsgrie vkrtrnkflf lkadshfrhg
      361 ipffvkvrlv nikgdpipnq qvfikaqgag ftnatttdqh glakfsidts gisryilnik
      421 vyhkeensci hssctaerha eahhtayavy slsksyiyld teagvlpcnq shtvqahfil
      481 kgqvlgvlpq ivfhylvmaq gsilqtgnht hqvepgespv qgnfaleipv efsmvpmakm
      541 liytilpdge viadsvkfqv ekclrhevhl sfspsqslpa sqthmrvtas pqslcglrav
      601 dqsvlllkpe aelspsliyd lpgmqeskfi prshypfede dgcviyrprv igkltysvpy
      661 grekdvfrym rdtgltaltn lklrtfcfdy dmvplavpaa rssdlfnsdg ygswrsarvk
      721 slppkkaphk dpppkdpvie tirnyfpetw vwdlvtvnss gaaelemtvp dtitewkaga
      781 lclsndtglg lssvatlqaf qpffveltmp ysvirgeaft lkatvmnylp tslpmavqle
      841 aspdftavpv gndqdsyclg angrhtsswl vtpkslgnvn fsvsaeaqqs pepcgsevat
      901 vpetgrkdtv vkvlivepeg ikrehtfssl lcasdaelse tlslllpptv vkdsarahfs
      961 vmgdilssai kntqnliqmp ygcgeqnmvl fapsiyvlky lnetqqltek ikskalgylr
     1021 agyqrelnyk hkdgsysafg dhdgkgqgnt wltafvlksf sqaqafifid eshitdaftw
     1081 lshqqkdsgc frssgslfnn amkggvddei tlsayitval leslppdthp vvskalscle
     1141 sswenieqgg ngsfvytkal mayafalagn qekrneilks ldkeaikedn sihwerpqkp
     1201 mksarslykp qassaevemn ayvilarlta qsapspkdla lsmgtikwlt kqqnsrggfs
     1261 stqdtvvald alskygaatf sksqktpsvt vqssgsffqk fqvdnsnrll lqqvslpdip
     1321 gnytvsvsge gcvyaqtmlr ynlplekqqp afalkvqtvp ltcnnpkgqn sfqisleisy
     1381 tgsrpasnmv iadvkmlsgf iplkptvkkl erlehvsrte vttnnvllyl dqvtnqtlsf
     1441 sfiiqqdipv knlqpaivkv ydyyetdeva faeysspcss dnqnv
//
LOCUS       NP_001100951             667 aa            linear   ROD 15-APR-2025
DEFINITION  paraneoplastic antigen-like protein 8B [Rattus norvegicus].
ACCESSION   NP_001100951 XP_001064185 XP_218352
VERSION     NP_001100951.1
DBSOURCE    REFSEQ: accession NM_001107481.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_218352.3, XP_001064185.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26643296.758.1, SRR26643429.1046.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..667
                     /product="paraneoplastic antigen-like protein 8B"
                     /note="PNMA-like protein 2; PNMA-like 2; paraneoplastic Ma
                     antigen family member 8B; paraneoplastic Ma antigen
                     family-like 2"
                     /calculated_mol_wt=72258
     Region          1..>114
                     /region_name="PNMA"
                     /note="pfam14893"
                     /db_xref="CDD:464357"
     CDS             1..667
                     /gene="Pnma8b"
                     /gene_synonym="Pnmal2; RGD1560435"
                     /coded_by="NM_001107481.2:407..2410"
                     /db_xref="GeneID:308393"
                     /db_xref="RGD:1560435"
ORIGIN      
        1 mtmnllqdwc kelevevhra llitgiperl qqadieatlr pnlqplgnyr lrtvravtke
       61 kaqaalvefg adfdhsaipi hirgengiwk ilskdrgqda rvlrqmrrll lderpmddfr
      121 eiaiplvlea qaqakglgke akkagssega arsgrrgrrg gkrrsrshkl taqkgqkrsr
      181 ggrrarsese dssddslgiv ieeiyaedls vdedqralya tlqaaakelt kkwafrgdqd
      241 egdgprefla lvtvtdkakk eeiekdlpgt esiclnikde ksgvpdlval lavrdtpave
      301 veteveddde eddddddded edededdded ddddgsdses lengeqgkev mdspefvaiv
      361 aytdpadpsa reemlkiasv ietlgwgdkk dkkdvlpqvl svmakdtsgp rvkveeagrq
      421 vdamvlrkae edgnllecis tlaeaencpk gkksglgllr gwtaeghqgg llelvallaa
      481 qdmveavree easrwggggs ggrkcdhsqg glsevlafla sqenlesnee seedsdtese
      541 gdsedtdsee sepgdsvskk prakrartgs kglapagata vstgsrarkt rrggrgrgrg
      601 vtpekkagsg astedhagnn kkkkkkgsag agarvragea kgqpaavpks trgkkarrgp
      661 rrapkcr
//
LOCUS       NP_001094219             232 aa            linear   ROD 15-APR-2025
DEFINITION  max dimerization protein 1 [Rattus norvegicus].
ACCESSION   NP_001094219 XP_001074696 XP_342717
VERSION     NP_001094219.1
DBSOURCE    REFSEQ: accession NM_001100749.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Lin,S.Y. and Elledge,S.J.
  TITLE     Multiple tumor suppressor pathways negatively regulate telomerase
  JOURNAL   Cell 113 (7), 881-889 (2003)
   PUBMED   12837246
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Oh,S., Song,Y.H., Yim,J. and Kim,T.K.
  TITLE     Identification of Mad as a repressor of the human telomerase
            (hTERT) gene
  JOURNAL   Oncogene 19 (11), 1485-1490 (2000)
   PUBMED   10723141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Nov 23, 2008 this sequence version replaced
            XP_342717.2, XP_001074696.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.20065.1,
                                           SRR26643298.23889.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..232
                     /product="max dimerization protein 1"
                     /calculated_mol_wt=25946
     Region          57..136
                     /region_name="bHLHzip_Mad1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max-associated protein 1 (Mad1) and
                     similar proteins; cd18931"
                     /db_xref="CDD:381501"
     Site            order(61..62,65..66,68..69,73,92..94)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381501"
     Site            order(72..73,75..80,82..83,95,98,102,104..106,108..109,
                     111..112,115,119,122..123,125..126,129..130,132..133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381501"
     Site            order(72,75..76,78..79,82..83,95,98,102,104..106,108..109,
                     111..112,115,119,122..123,125..126,129..130,132..133)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381501"
     CDS             1..232
                     /gene="Mxd1"
                     /gene_synonym="Mad-1"
                     /coded_by="NM_001100749.1:134..832"
                     /db_xref="GeneID:362391"
                     /db_xref="RGD:1564525"
ORIGIN      
        1 matavgmniq llleaadyle rrereaehgy asmlpysskd rdafkrrnkp kknstssrst
       61 hnemeknrra hlrlcleklk glvplgpess rhttlslltk aklhikkled cdrkavhqid
      121 qlqreqrhlk rrleklgaer trmdsvgsvv ssersdsdre eldvdvdvdv dvdvdvdves
      181 tdylngdlgw sssvsdsder gsmqslgsde gyssasvkra klqdghkagp gl
//
LOCUS       NP_036843               1151 aa            linear   ROD 15-APR-2025
DEFINITION  integrin alpha-M precursor [Rattus norvegicus].
ACCESSION   NP_036843
VERSION     NP_036843.2
DBSOURCE    REFSEQ: accession NM_012711.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Wang,Y., Pi,Y., Hu,L., Peng,Z., Hu,H., Zhao,J., Zhou,Y. and Wang,D.
  TITLE     Proteomic analysis of foot ulcer tissue reveals novel potential
            therapeutic targets of wound healing in diabetic foot ulcers
  JOURNAL   Comput Biol Med 159, 106858 (2023)
   PUBMED   37087778
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Atcha,H., Meli,V.S., Davis,C.T., Brumm,K.T., Anis,S., Chin,J.,
            Jiang,K., Pathak,M.M. and Liu,W.F.
  TITLE     Crosstalk Between CD11b and Piezo1 Mediates Macrophage Responses to
            Mechanical Cues
  JOURNAL   Front Immunol 12, 689397 (2021)
   PUBMED   34630381
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   Lokki,A.I., Teirila,L., Triebwasser,M., Daly,E., Bhattacharjee,A.,
            Uotila,L., Llort Asens,M., Kurki,M.I., Perola,M., Auro,K.,
            Salmon,J.E., Daly,M., Atkinson,J.P., Laivuori,H., Fagerholm,S. and
            Meri,S.
  CONSRTM   Finnpec
  TITLE     Dysfunction of complement receptors CR3 (CD11b/18) and CR4
            (CD11c/18) in pre-eclampsia: a genetic and functional study
  JOURNAL   BJOG 128 (8), 1282-1291 (2021)
   PUBMED   33539617
REFERENCE   4  (residues 1 to 1151)
  AUTHORS   Zhou,M., Wang,X., Shi,Y., Ding,Y., Li,X., Xie,T., Shi,Z. and Fu,W.
  TITLE     Deficiency of ITGAM Attenuates Experimental Abdominal Aortic
            Aneurysm in Mice
  JOURNAL   J Am Heart Assoc 10 (7), e019900 (2021)
   PUBMED   33749307
REFERENCE   5  (residues 1 to 1151)
  AUTHORS   Shi,F.J., Xie,H., Zhang,C.Y., Qin,H.F., Zeng,X.W., Lou,H.,
            Zhang,L., Xu,G.T., Zhang,J.F. and Xu,G.X.
  TITLE     Is Iba-1 protein expression a sensitive marker for microglia
            activation in experimental diabetic retinopathy?
  JOURNAL   Int J Ophthalmol 14 (2), 200-208 (2021)
   PUBMED   33614447
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1151)
  AUTHORS   Choi,M., Rabb,H., Arnaout,M.A. and Ehrlich,H.P.
  TITLE     Preventing the infiltration of leukocytes by monoclonal antibody
            blocks the development of progressive ischemia in rat burns
  JOURNAL   Plast Reconstr Surg 96 (5), 1177-85 (1995)
   PUBMED   7568496
REFERENCE   7  (residues 1 to 1151)
  AUTHORS   Coombe,D.R., Watt,S.M. and Parish,C.R.
  TITLE     Mac-1 (CD11b/CD18) and CD45 mediate the adhesion of hematopoietic
            progenitor cells to stromal cell elements via recognition of
            stromal heparan sulfate
  JOURNAL   Blood 84 (3), 739-752 (1994)
   PUBMED   8043862
REFERENCE   8  (residues 1 to 1151)
  AUTHORS   Seekamp,A., Mulligan,M.S., Till,G.O., Smith,C.W., Miyasaka,M.,
            Tamatani,T., Todd,R.F. 3rd and Ward,P.A.
  TITLE     Role of beta 2 integrins and ICAM-1 in lung injury following
            ischemia-reperfusion of rat hind limbs
  JOURNAL   Am J Pathol 143 (2), 464-472 (1993)
   PUBMED   8102031
REFERENCE   9  (residues 1 to 1151)
  AUTHORS   Mulligan,M.S., Varani,J., Warren,J.S., Till,G.O., Smith,C.W.,
            Anderson,D.C., Todd,R.F. 3rd and Ward,P.A.
  TITLE     Roles of beta 2 integrins of rat neutrophils in complement- and
            oxygen radical-mediated acute inflammatory injury
  JOURNAL   J Immunol 148 (6), 1847-1857 (1992)
   PUBMED   1347308
REFERENCE   10 (residues 1 to 1151)
  AUTHORS   Tamatani,T., Kotani,M. and Miyasaka,M.
  TITLE     Characterization of the rat leukocyte integrin, CD11/CD18, by the
            use of LFA-1 subunit-specific monoclonal antibodies
  JOURNAL   Eur J Immunol 21 (3), 627-633 (1991)
   PUBMED   1672643
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 13, 2022 this sequence version replaced NP_036843.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF268593.1, SRR26643298.5540.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..1151
                     /product="integrin alpha-M precursor"
                     /note="Integrin alpha-M; integrin, alpha M"
                     /calculated_mol_wt=125422
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1789
     Region          149..324
                     /region_name="vWA_integrins_alpha_subunit"
                     /note="Integrins are a class of adhesion receptors that
                     link the extracellular matrix to the cytoskeleton and
                     cooperate with growth factor receptors to promote celll
                     survival, cell cycle progression and cell migration.
                     Integrins consist of an alpha and a beta...; cd01469"
                     /db_xref="CDD:238746"
     Site            order(149,151,172,252,254,283,313)
                     /site_type="active"
                     /note="integrin inhibitor binding pocket [active]"
                     /db_xref="CDD:238746"
     Site            order(156,158,160,225,258)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238746"
     Site            order(158..160,162,225)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238746"
     Region          453..509
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          516..569
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          581..>605
                     /region_name="Int_alpha"
                     /note="Integrin alpha (beta-propellor repeats);
                     smart00191"
                     /db_xref="CDD:214549"
     Region          615..1031
                     /region_name="Integrin_alpha2"
                     /note="Integrin alpha; pfam08441"
                     /db_xref="CDD:462478"
     Region          1128..1140
                     /region_name="Integrin_alpha"
                     /note="Integrin alpha cytoplasmic region; pfam00357"
                     /db_xref="CDD:459778"
     CDS             1..1151
                     /gene="Itgam"
                     /gene_synonym="Cd11b"
                     /coded_by="NM_012711.2:33..3488"
                     /db_xref="GeneID:25021"
                     /db_xref="RGD:2926"
ORIGIN      
        1 mtlkfllvtv ltlchgfnld tenpmtfqen argfgqsviq lgetrvvvaa pqevkavnqt
       61 galyqcdyst nrcdpiplqv ppeavnmslg lslaattvpp qllacgptvh qnckentyvn
      121 glcylfgsnl lrkpqqfpea lrgcpqqesd iaflidgsgs insidfqkmk efvstvmdqf
      181 qksktlfslm qysdefrthf tfndfkrnpd pkshvrpirq lngrtktasg irkvvrelfq
      241 kingardnaa kilvvitdge kfgdplnyed vipeaeeagi iryvigvgna fhkpqsrrel
      301 dtiaskpagd hvfqvdnfea lntirnqlqe kifaiegtqt gstssfehem sqegfsaait
      361 sngpllgsvg sfdwaggafl ypskdkatfi nttridsdmn daylgyasav isrnrvqslv
      421 lgapryqhig lvvmfkqnfg awephtdikg sqigsyfgas lcsvdmdadg ntnliligap
      481 hhyektrggq vsvcplprgr arwqceailh gdqghpwgrf gaaltvlgdv ngdkltdvai
      541 gapgeqenqg avyifhgasv asistphsqr iagarfspgl qyfgqslsgg kdltmdglmd
      601 lavgaqgrll liraqpvlrl eatmefspkn larsvfacqe evvknkdage vrvclhvrkn
      661 tkdrlregdi qstvtydlal dpgrsvvraf fdetkngilr rirvfgltqk cetlklilpd
      721 cvdnsvspii lrlnytlvge plrssrdlrp vlameaqrif tamfpfeknc gndticqddl
      781 sitvssirvn tlvvgdsrdf dvsvtlrndg edsygtkvtc yypsglsyrk vsasqnqfsk
      841 kpwrviaeps ssegqgvlks tiwdinhpif pansevtfnv tfdvdsdasl gnklllkvvv
      901 tsennvsrtd ktesqlelpv kyaiymvvts gessikylnf tasemtskvi qhqyqfnnlg
      961 qrsfpvsvvf wipvqinkvt iwdppqvtfs qnlssvcrte qkspshskfq delertpvln
     1021 csvavckriq cdipsfnske ifnvtlqgnl lfdwyietsh dhlllvstae ilfndsafal
     1081 lpgqetfvka qtetkvepyk vhnpvplivg ssvgglvlla litaglyklg ffkrqykdmm
     1141 neaapqdgpp q
//
LOCUS       NP_036656                358 aa            linear   ROD 15-APR-2025
DEFINITION  CCAAT/enhancer-binding protein alpha isoform a [Rattus norvegicus].
ACCESSION   NP_036656
VERSION     NP_036656.1
DBSOURCE    REFSEQ: accession NM_012524.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wu,K., Huang,S., Zheng,F. and Liu,Y.
  TITLE     The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway
  JOURNAL   Acta Diabetol 60 (11), 1491-1503 (2023)
   PUBMED   37392202
  REMARK    GeneRIF: The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Xu,Z., Yao,X., Zhao,Y. and Yao,B.
  TITLE     C/EBPalpha involvement in microglial polarization via HDAC1/STAT3
            pathway aggravated sevoflurane-induced cognitive impairment in aged
            rats
  JOURNAL   PeerJ 11, e15466 (2023)
   PUBMED   37361037
  REMARK    GeneRIF: C/EBPalpha involvement in microglial polarization via
            HDAC1/STAT3 pathway aggravated sevoflurane-induced cognitive
            impairment in aged rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Lu,H., Chen,Y., Chen,Y., Huang,L. and Chen,L.
  TITLE     C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A Regulates
            Autophagy, Matrix Metalloproteinase Expression, and Phenotypic of
            Vascular Smooth Muscle Cells in Aortic Dissection
  JOURNAL   J Immunol Res 2022, 7465353 (2022)
   PUBMED   36132983
  REMARK    GeneRIF: C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A
            Regulates Autophagy, Matrix Metalloproteinase Expression, and
            Phenotypic of Vascular Smooth Muscle Cells in Aortic Dissection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Duan,P., Wang,H., Yi,X., Zhang,H., Chen,H. and Pan,Z.
  TITLE     C/EBPalpha regulates the fate of bone marrow mesenchymal stem cells
            and steroid-induced avascular necrosis of the femoral head by
            targeting the PPARgamma signalling pathway
  JOURNAL   Stem Cell Res Ther 13 (1), 342 (2022)
   PUBMED   35883192
  REMARK    GeneRIF: C/EBPalpha regulates the fate of bone marrow mesenchymal
            stem cells and steroid-induced avascular necrosis of the femoral
            head by targeting the PPARgamma signalling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Muller,C., Bremer,A., Schreiber,S., Eichwald,S. and Calkhoven,C.F.
  TITLE     Nucleolar retention of a translational C/EBPalpha isoform
            stimulates rDNA transcription and cell size
  JOURNAL   EMBO J 29 (5), 897-909 (2010)
   PUBMED   20075868
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Calkhoven,C.F., Muller,C. and Leutz,A.
  TITLE     Translational control of C/EBPalpha and C/EBPbeta isoform
            expression
  JOURNAL   Genes Dev 14 (15), 1920-1932 (2000)
   PUBMED   10921906
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Lincoln,A.J., Monczak,Y., Williams,S.C. and Johnson,P.F.
  TITLE     Inhibition of CCAAT/enhancer-binding protein alpha and beta
            translation by upstream open reading frames
  JOURNAL   J Biol Chem 273 (16), 9552-9560 (1998)
   PUBMED   9545285
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Stephens,J.M. and Pekala,P.H.
  TITLE     Transcriptional repression of the C/EBP-alpha and GLUT4 genes in
            3T3-L1 adipocytes by tumor necrosis factor-alpha. Regulations is
            coordinate and independent of protein synthesis
  JOURNAL   J Biol Chem 267 (19), 13580-13584 (1992)
   PUBMED   1618860
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Thomassin,H., Hamel,D., Bernier,D., Guertin,M. and Belanger,L.
  TITLE     Molecular cloning of two C/EBP-related proteins that bind to the
            promoter and the enhancer of the alpha 1-fetoprotein gene. Further
            analysis of C/EBP beta and C/EBP gamma
  JOURNAL   Nucleic Acids Res 20 (12), 3091-3098 (1992)
   PUBMED   1377818
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Samuelsson,L., Stromberg,K., Vikman,K., Bjursell,G. and Enerback,S.
  TITLE     The CCAAT/enhancer binding protein and its role in adipocyte
            differentiation: evidence for direct involvement in terminal
            adipocyte development
  JOURNAL   EMBO J 10 (12), 3787-3793 (1991)
   PUBMED   1935900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Summary: This intronless gene encodes a transcription factor that
            contains a basic leucine zipper (bZIP) domain and recognizes the
            CCAAT motif in the promoters of target genes. The encoded protein
            functions in homodimers and also heterodimers with
            CCAAT/enhancer-binding proteins beta and gamma. Activity of this
            protein can modulate the expression of genes involved in cell cycle
            regulation as well as in body weight homeostasis. The use of
            alternative in-frame non-AUG (CUG) and AUG start codons results in
            protein isoforms with different lengths. Differential translation
            initiation is mediated by an out-of-frame, upstream open reading
            frame which is located between the CUG and the first AUG start
            codons. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (1) can initiate translation from
            an upstream non-AUG (CUG) site, and also from three conserved
            downstream, in-frame AUG sites. The isoform (a) represented in this
            RefSeq results from translation initiation at the first AUG start
            codon. Isoform a has a shorter N-terminus, compared to isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22582416.154041.1,
                                        SRR26643429.1696.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            regulatory uORF        :: PMID: 10921906
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..358
                     /product="CCAAT/enhancer-binding protein alpha isoform a"
                     /note="C/EBP alpha; CAAT/enhancer-binding protein,
                     DNA-binding protein; CCAAT/enhancer binding protein
                     (C/EBP), alpha"
                     /calculated_mol_wt=37240
     Region          1..70
                     /region_name="Required to repress E2F1:TFDP1-mediated
                     transcription, to inhibit cell cycle and to induce
                     adipocyte differentiation.
                     /evidence=ECO:0000269|PubMed:11672531"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Region          15
                     /region_name="alternative AUG start codon; isoform d"
     Region          54..72
                     /region_name="Required for interaction with TRIB1.
                     /evidence=ECO:0000250|UniProtKB:P49715"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Region          118
                     /region_name="alternative AUG start codon; isoform b"
     Region          126..200
                     /region_name="Required to induce adipocyte
                     differentiation. /evidence=ECO:0000269|PubMed:11672531"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Site            159
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P49715; propagated from
                     UniProtKB/Swiss-Prot (P05554.3)"
     Region          176..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Region          180..194
                     /region_name="Required to functionally cooperate with
                     SREBF1 in promoter activation.
                     /evidence=ECO:0000250|UniProtKB:P53566"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53566; propagated from
                     UniProtKB/Swiss-Prot (P05554.3)"
     Region          213..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3.
                     /evidence=ECO:0000250|UniProtKB:P53566; propagated from
                     UniProtKB/Swiss-Prot (P05554.3)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3.
                     /evidence=ECO:0000250|UniProtKB:P53566; propagated from
                     UniProtKB/Swiss-Prot (P05554.3)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3.
                     /evidence=ECO:0000250|UniProtKB:P53566; propagated from
                     UniProtKB/Swiss-Prot (P05554.3)"
     Region          240..358
                     /region_name="Interaction with FOXO1.
                     /evidence=ECO:0000250|UniProtKB:P53566"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Region          280..340
                     /region_name="bZIP_CEBPA"
                     /note="Basic leucine zipper (bZIP) domain of
                     CCAAT/enhancer-binding protein alpha (CEBPA): a
                     DNA-binding and dimerization domain; cd14711"
                     /db_xref="CDD:269859"
     Region          282..340
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269859"
     Site            order(285..286,288..289,291..293,295..296,298..300,302,
                     304)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269859"
     Region          286..313
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     Site            order(307,310,313..314,317..318,320..321,323..325,
                     327..328,331..332,334..335,338..339)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269859"
     Region          317..345
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P05554.3)"
     CDS             1..358
                     /gene="Cebpa"
                     /gene_synonym="DBPCEP"
                     /coded_by="NM_012524.3:122..1198"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24252"
                     /db_xref="RGD:2326"
ORIGIN      
        1 mesadfyeae prppmsshlq spphapsnaa fgfprgagpa pppappaape plggicehet
       61 sidisayidp aafndeflad lfqhsrqqek akaaagpagg ggdfdypgap agpggavmsa
      121 gahgpppgyg caaagyldgr leplyervga palrplvikq epreedeakq lalaglfpyq
      181 pppppppphp haspahlaap hlqfqiahcg qttmhlqpgh ptppptpvps phpapamgaa
      241 glpgpggslk glagphpdlr tgggggggag agkakksvdk nsneyrvrre rnniavrksr
      301 dkakqrnvet qqkvleltsd ndrlrkrveq lsreldtlrg ifrqlpessl vkamgnca
//
LOCUS       NP_001416800             338 aa            linear   ROD 15-APR-2025
DEFINITION  caspase-9 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416800 XP_038966621
VERSION     NP_001416800.1
DBSOURCE    REFSEQ: accession NM_001429871.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Bai,L., Yang,J., Zhang,H., Liao,W. and Cen,Y.
  TITLE     PTB domain and leucine zipper motif 1 (APPL1) inhibits myocardial
            ischemia/hypoxia-reperfusion injury via inactivation of apoptotic
            protease activating factor-1 (APAF-1)/Caspase9 signaling pathway
  JOURNAL   Bioengineered 12 (1), 4385-4396 (2021)
   PUBMED   34304702
  REMARK    GeneRIF: PTB domain and leucine zipper motif 1 (APPL1) inhibits
            myocardial ischemia/hypoxia-reperfusion injury via inactivation of
            apoptotic protease activating factor-1 (APAF-1)/Caspase9 signaling
            pathway.
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Martin,S., Harrington,D.A., Ohlander,S., Stupp,S.I., McVary,K.T.
            and Podlasek,C.A.
  TITLE     Peptide amphiphile nanofiber hydrogel delivery of Sonic hedgehog
            protein to the penis and cavernous nerve suppresses intrinsic and
            extrinsic apoptotic signaling mechanisms, which are an underlying
            cause of erectile dysfunction
  JOURNAL   Nanomedicine 37, 102444 (2021)
   PUBMED   34314869
  REMARK    GeneRIF: Peptide amphiphile nanofiber hydrogel delivery of Sonic
            hedgehog protein to the penis and cavernous nerve suppresses
            intrinsic and extrinsic apoptotic signaling mechanisms, which are
            an underlying cause of erectile dysfunction.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Liu,H., Li,J., Jiang,C., Yuan,T. and Ma,H.
  TITLE     Cellular communication network factor 1 (CCN1) knockdown exerts a
            protective effect for hepatic ischemia/reperfusion injury by
            deactivating the MEK/ERK pathway
  JOURNAL   Clin Res Hepatol Gastroenterol 45 (5), 101737 (2021)
   PUBMED   34144219
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Song,Z., Tian,X. and Shi,Q.
  TITLE     Fas, Caspase-8, and Caspase-9 pathway-mediated bile acid-induced
            fetal cardiomyocyte apoptosis in intrahepatic cholestasis pregnant
            rat models
  JOURNAL   J Obstet Gynaecol Res 47 (7), 2298-2306 (2021)
   PUBMED   33847039
  REMARK    GeneRIF: Fas, Caspase-8, and Caspase-9 pathway-mediated bile
            acid-induced fetal cardiomyocyte apoptosis in intrahepatic
            cholestasis pregnant rat models.
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Zhuang,C., Ni,S., Yang,Z.C. and Liu,R.P.
  TITLE     Oxidative Stress Induces Chondrocyte Apoptosis through
            Caspase-Dependent and Caspase-Independent Mitochondrial Pathways
            and the Antioxidant Mechanism of Angelica Sinensis Polysaccharide
  JOURNAL   Oxid Med Cell Longev 2020, 3240820 (2020)
   PUBMED   33224431
  REMARK    GeneRIF: Oxidative Stress Induces Chondrocyte Apoptosis through
            Caspase-Dependent and Caspase-Independent Mitochondrial Pathways
            and the Antioxidant Mechanism of Angelica Sinensis Polysaccharide.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Vu,C.C., Bortner,C.D. and Cidlowski,J.A.
  TITLE     Differential involvement of initiator caspases in apoptotic volume
            decrease and potassium efflux during Fas- and UV-induced cell death
  JOURNAL   J Biol Chem 276 (40), 37602-37611 (2001)
   PUBMED   11431480
  REMARK    GeneRIF: The activation of caspase-8, but not caspase-9, is
            necessary for Fas-induced apoptosis. Conversely, caspase-9, but not
            caspase-8, is important for UV-mediated shrunken morphology and
            apoptosis progression.
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Angelastro,J.M., Moon,N.Y., Liu,D.X., Yang,A.S., Greene,L.A. and
            Franke,T.F.
  TITLE     Characterization of a novel isoform of caspase-9 that inhibits
            apoptosis
  JOURNAL   J Biol Chem 276 (15), 12190-12200 (2001)
   PUBMED   11278518
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Zaidi,A.U., D'Sa-Eipper,C., Brenner,J., Kuida,K., Zheng,T.S.,
            Flavell,R.A., Rakic,P. and Roth,K.A.
  TITLE     Bcl-X(L)-caspase-9 interactions in the developing nervous system:
            evidence for multiple death pathways
  JOURNAL   J Neurosci 21 (1), 169-175 (2001)
   PUBMED   11150333
REFERENCE   9  (residues 1 to 338)
  AUTHORS   D'Sa-Eipper,C., Leonard,J.R., Putcha,G., Zheng,T.S., Flavell,R.A.,
            Rakic,P., Kuida,K. and Roth,K.A.
  TITLE     DNA damage-induced neural precursor cell apoptosis requires p53 and
            caspase 9 but neither Bax nor caspase 3
  JOURNAL   Development 128 (1), 137-146 (2001)
   PUBMED   11092819
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Kermer,P., Ankerhold,R., Klocker,N., Krajewski,S., Reed,J.C. and
            Bahr,M.
  TITLE     Caspase-9: involvement in secondary death of axotomized rat retinal
            ganglion cells in vivo
  JOURNAL   Brain Res Mol Brain Res 85 (1-2), 144-150 (2000)
   PUBMED   11146116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 30, 2024 this sequence version replaced XP_038966621.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.106984.1,
                                           SRR26643299.25378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..338
                     /product="caspase-9 isoform 2"
                     /EC_number="3.4.22.62"
                     /note="caspase-9-carboxyl-terminal divergent; 25 kDa
                     caspase-9 dominant negative protein; caspase-9 dominant
                     negative form; apoptotic protease Mch-6; Ice-like
                     apoptotic protease 6; apoptotic protease activating factor
                     3; caspase 9, apoptosis-related cysteine peptidase"
                     /calculated_mol_wt=37219
     Region          74..336
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cd00032"
                     /db_xref="CDD:237997"
     Site            order(102,160,207,214,274..279,283..284)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(159,209)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(215,259..260,267,270,273,296,304,310,320,325..326,
                     328,331..332)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(216,258)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     CDS             1..338
                     /gene="Casp9"
                     /gene_synonym="Apaf3; Casp-9-CTD; Casp9_v1; Ice-Lap6;
                     Mch6"
                     /coded_by="NM_001429871.1:278..1294"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:58918"
                     /db_xref="RGD:61867"
ORIGIN      
        1 mglkskeqkv vkldpsqpal gnltpvvlgp eelwptrlrp evltpetprp vdigsgrahd
       61 vctpgkierh admaytldsd pcghcliinn vnfcpssgls trigshvdce klqhrfcwlr
      121 fmvevkndlt akkmvtalme mahrdhrald cfvvvilshg cqashlqfpg avygtdgcsv
      181 sierivnifn gtgcpslggk pklffiqacg geqkdhgfev aftssqdkaf dsdsepdavp
      241 yqegprtldq ldavsslptp sdilvsystf pgfvswrdkk sgswyietld gvleqwarse
      301 dlqslllrva navsekgvyk qipgcfnflr kklffkts
//
LOCUS       NP_001274508             241 aa            linear   ROD 15-APR-2025
DEFINITION  CCAAT/enhancer-binding protein alpha isoform b [Rattus norvegicus].
ACCESSION   NP_001274508
VERSION     NP_001274508.1
DBSOURCE    REFSEQ: accession NM_001287579.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wu,K., Huang,S., Zheng,F. and Liu,Y.
  TITLE     The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway
  JOURNAL   Acta Diabetol 60 (11), 1491-1503 (2023)
   PUBMED   37392202
  REMARK    GeneRIF: The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway.
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Xu,Z., Yao,X., Zhao,Y. and Yao,B.
  TITLE     C/EBPalpha involvement in microglial polarization via HDAC1/STAT3
            pathway aggravated sevoflurane-induced cognitive impairment in aged
            rats
  JOURNAL   PeerJ 11, e15466 (2023)
   PUBMED   37361037
  REMARK    GeneRIF: C/EBPalpha involvement in microglial polarization via
            HDAC1/STAT3 pathway aggravated sevoflurane-induced cognitive
            impairment in aged rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Lu,H., Chen,Y., Chen,Y., Huang,L. and Chen,L.
  TITLE     C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A Regulates
            Autophagy, Matrix Metalloproteinase Expression, and Phenotypic of
            Vascular Smooth Muscle Cells in Aortic Dissection
  JOURNAL   J Immunol Res 2022, 7465353 (2022)
   PUBMED   36132983
  REMARK    GeneRIF: C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A
            Regulates Autophagy, Matrix Metalloproteinase Expression, and
            Phenotypic of Vascular Smooth Muscle Cells in Aortic Dissection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Duan,P., Wang,H., Yi,X., Zhang,H., Chen,H. and Pan,Z.
  TITLE     C/EBPalpha regulates the fate of bone marrow mesenchymal stem cells
            and steroid-induced avascular necrosis of the femoral head by
            targeting the PPARgamma signalling pathway
  JOURNAL   Stem Cell Res Ther 13 (1), 342 (2022)
   PUBMED   35883192
  REMARK    GeneRIF: C/EBPalpha regulates the fate of bone marrow mesenchymal
            stem cells and steroid-induced avascular necrosis of the femoral
            head by targeting the PPARgamma signalling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Muller,C., Bremer,A., Schreiber,S., Eichwald,S. and Calkhoven,C.F.
  TITLE     Nucleolar retention of a translational C/EBPalpha isoform
            stimulates rDNA transcription and cell size
  JOURNAL   EMBO J 29 (5), 897-909 (2010)
   PUBMED   20075868
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Calkhoven,C.F., Muller,C. and Leutz,A.
  TITLE     Translational control of C/EBPalpha and C/EBPbeta isoform
            expression
  JOURNAL   Genes Dev 14 (15), 1920-1932 (2000)
   PUBMED   10921906
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Lincoln,A.J., Monczak,Y., Williams,S.C. and Johnson,P.F.
  TITLE     Inhibition of CCAAT/enhancer-binding protein alpha and beta
            translation by upstream open reading frames
  JOURNAL   J Biol Chem 273 (16), 9552-9560 (1998)
   PUBMED   9545285
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Stephens,J.M. and Pekala,P.H.
  TITLE     Transcriptional repression of the C/EBP-alpha and GLUT4 genes in
            3T3-L1 adipocytes by tumor necrosis factor-alpha. Regulations is
            coordinate and independent of protein synthesis
  JOURNAL   J Biol Chem 267 (19), 13580-13584 (1992)
   PUBMED   1618860
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Thomassin,H., Hamel,D., Bernier,D., Guertin,M. and Belanger,L.
  TITLE     Molecular cloning of two C/EBP-related proteins that bind to the
            promoter and the enhancer of the alpha 1-fetoprotein gene. Further
            analysis of C/EBP beta and C/EBP gamma
  JOURNAL   Nucleic Acids Res 20 (12), 3091-3098 (1992)
   PUBMED   1377818
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Samuelsson,L., Stromberg,K., Vikman,K., Bjursell,G. and Enerback,S.
  TITLE     The CCAAT/enhancer binding protein and its role in adipocyte
            differentiation: evidence for direct involvement in terminal
            adipocyte development
  JOURNAL   EMBO J 10 (12), 3787-3793 (1991)
   PUBMED   1935900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Summary: This intronless gene encodes a transcription factor that
            contains a basic leucine zipper (bZIP) domain and recognizes the
            CCAAT motif in the promoters of target genes. The encoded protein
            functions in homodimers and also heterodimers with
            CCAAT/enhancer-binding proteins beta and gamma. Activity of this
            protein can modulate the expression of genes involved in cell cycle
            regulation as well as in body weight homeostasis. The use of
            alternative in-frame non-AUG (CUG) and AUG start codons results in
            protein isoforms with different lengths. Differential translation
            initiation is mediated by an out-of-frame, upstream open reading
            frame which is located between the CUG and the first AUG start
            codons. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (1) can initiate translation from
            an upstream non-AUG (CUG) site, and also from three conserved
            downstream, in-frame AUG sites. The isoform (b) represented in this
            RefSeq results from translation initiation at the third AUG start
            codon. Isoform b has a shorter N-terminus, compared to isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22582416.154041.1,
                                        SRR26643429.1696.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:10921906)
            regulatory uORF                  :: PMID: 10921906
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..241
                     /product="CCAAT/enhancer-binding protein alpha isoform b"
                     /note="C/EBP alpha; CAAT/enhancer-binding protein,
                     DNA-binding protein; CCAAT/enhancer binding protein
                     (C/EBP), alpha"
                     /calculated_mol_wt=25395
     Region          163..223
                     /region_name="bZIP_CEBPA"
                     /note="Basic leucine zipper (bZIP) domain of
                     CCAAT/enhancer-binding protein alpha (CEBPA): a
                     DNA-binding and dimerization domain; cd14711"
                     /db_xref="CDD:269859"
     Region          165..223
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269859"
     Site            order(168..169,171..172,174..176,178..179,181..183,185,
                     187)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269859"
     Site            order(190,193,196..197,200..201,203..204,206..208,
                     210..211,214..215,217..218,221..222)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269859"
     CDS             1..241
                     /gene="Cebpa"
                     /gene_synonym="DBPCEP"
                     /coded_by="NM_001287579.1:473..1198"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="GeneID:24252"
                     /db_xref="RGD:2326"
ORIGIN      
        1 msagahgppp gygcaaagyl dgrleplyer vgapalrplv ikqepreede akqlalaglf
       61 pyqppppppp phphaspahl aaphlqfqia hcgqttmhlq pghptppptp vpsphpapam
      121 gaaglpgpgg slkglagphp dlrtgggggg gagagkakks vdknsneyrv rrernniavr
      181 ksrdkakqrn vetqqkvlel tsdndrlrkr veqlsreldt lrgifrqlpe sslvkamgnc
      241 a
//
LOCUS       NP_001274507             344 aa            linear   ROD 15-APR-2025
DEFINITION  CCAAT/enhancer-binding protein alpha isoform d [Rattus norvegicus].
ACCESSION   NP_001274507
VERSION     NP_001274507.1
DBSOURCE    REFSEQ: accession NM_001287578.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wu,K., Huang,S., Zheng,F. and Liu,Y.
  TITLE     The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway
  JOURNAL   Acta Diabetol 60 (11), 1491-1503 (2023)
   PUBMED   37392202
  REMARK    GeneRIF: The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Xu,Z., Yao,X., Zhao,Y. and Yao,B.
  TITLE     C/EBPalpha involvement in microglial polarization via HDAC1/STAT3
            pathway aggravated sevoflurane-induced cognitive impairment in aged
            rats
  JOURNAL   PeerJ 11, e15466 (2023)
   PUBMED   37361037
  REMARK    GeneRIF: C/EBPalpha involvement in microglial polarization via
            HDAC1/STAT3 pathway aggravated sevoflurane-induced cognitive
            impairment in aged rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Lu,H., Chen,Y., Chen,Y., Huang,L. and Chen,L.
  TITLE     C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A Regulates
            Autophagy, Matrix Metalloproteinase Expression, and Phenotypic of
            Vascular Smooth Muscle Cells in Aortic Dissection
  JOURNAL   J Immunol Res 2022, 7465353 (2022)
   PUBMED   36132983
  REMARK    GeneRIF: C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A
            Regulates Autophagy, Matrix Metalloproteinase Expression, and
            Phenotypic of Vascular Smooth Muscle Cells in Aortic Dissection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Duan,P., Wang,H., Yi,X., Zhang,H., Chen,H. and Pan,Z.
  TITLE     C/EBPalpha regulates the fate of bone marrow mesenchymal stem cells
            and steroid-induced avascular necrosis of the femoral head by
            targeting the PPARgamma signalling pathway
  JOURNAL   Stem Cell Res Ther 13 (1), 342 (2022)
   PUBMED   35883192
  REMARK    GeneRIF: C/EBPalpha regulates the fate of bone marrow mesenchymal
            stem cells and steroid-induced avascular necrosis of the femoral
            head by targeting the PPARgamma signalling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Muller,C., Bremer,A., Schreiber,S., Eichwald,S. and Calkhoven,C.F.
  TITLE     Nucleolar retention of a translational C/EBPalpha isoform
            stimulates rDNA transcription and cell size
  JOURNAL   EMBO J 29 (5), 897-909 (2010)
   PUBMED   20075868
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Calkhoven,C.F., Muller,C. and Leutz,A.
  TITLE     Translational control of C/EBPalpha and C/EBPbeta isoform
            expression
  JOURNAL   Genes Dev 14 (15), 1920-1932 (2000)
   PUBMED   10921906
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Lincoln,A.J., Monczak,Y., Williams,S.C. and Johnson,P.F.
  TITLE     Inhibition of CCAAT/enhancer-binding protein alpha and beta
            translation by upstream open reading frames
  JOURNAL   J Biol Chem 273 (16), 9552-9560 (1998)
   PUBMED   9545285
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Stephens,J.M. and Pekala,P.H.
  TITLE     Transcriptional repression of the C/EBP-alpha and GLUT4 genes in
            3T3-L1 adipocytes by tumor necrosis factor-alpha. Regulations is
            coordinate and independent of protein synthesis
  JOURNAL   J Biol Chem 267 (19), 13580-13584 (1992)
   PUBMED   1618860
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Thomassin,H., Hamel,D., Bernier,D., Guertin,M. and Belanger,L.
  TITLE     Molecular cloning of two C/EBP-related proteins that bind to the
            promoter and the enhancer of the alpha 1-fetoprotein gene. Further
            analysis of C/EBP beta and C/EBP gamma
  JOURNAL   Nucleic Acids Res 20 (12), 3091-3098 (1992)
   PUBMED   1377818
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Samuelsson,L., Stromberg,K., Vikman,K., Bjursell,G. and Enerback,S.
  TITLE     The CCAAT/enhancer binding protein and its role in adipocyte
            differentiation: evidence for direct involvement in terminal
            adipocyte development
  JOURNAL   EMBO J 10 (12), 3787-3793 (1991)
   PUBMED   1935900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Summary: This intronless gene encodes a transcription factor that
            contains a basic leucine zipper (bZIP) domain and recognizes the
            CCAAT motif in the promoters of target genes. The encoded protein
            functions in homodimers and also heterodimers with
            CCAAT/enhancer-binding proteins beta and gamma. Activity of this
            protein can modulate the expression of genes involved in cell cycle
            regulation as well as in body weight homeostasis. The use of
            alternative in-frame non-AUG (CUG) and AUG start codons results in
            protein isoforms with different lengths. Differential translation
            initiation is mediated by an out-of-frame, upstream open reading
            frame which is located between the CUG and the first AUG start
            codons. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (1) can initiate translation from
            an upstream non-AUG (CUG) site, and also from three conserved
            downstream, in-frame AUG sites. The isoform (d) represented in this
            RefSeq results from translation initiation at the second AUG start
            codon. Isoform d has a shorter N-terminus, compared to isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22582416.154041.1,
                                        SRR26643429.1696.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:10921906)
            regulatory uORF                  :: PMID: 10921906
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..344
                     /product="CCAAT/enhancer-binding protein alpha isoform d"
                     /note="C/EBP alpha; CAAT/enhancer-binding protein,
                     DNA-binding protein; CCAAT/enhancer binding protein
                     (C/EBP), alpha"
                     /calculated_mol_wt=35619
     Region          104
                     /region_name="alternative AUG start codon; isoform b"
     Region          266..326
                     /region_name="bZIP_CEBPA"
                     /note="Basic leucine zipper (bZIP) domain of
                     CCAAT/enhancer-binding protein alpha (CEBPA): a
                     DNA-binding and dimerization domain; cd14711"
                     /db_xref="CDD:269859"
     Region          268..326
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269859"
     Site            order(271..272,274..275,277..279,281..282,284..286,288,
                     290)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269859"
     Site            order(293,296,299..300,303..304,306..307,309..311,
                     313..314,317..318,320..321,324..325)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269859"
     CDS             1..344
                     /gene="Cebpa"
                     /gene_synonym="DBPCEP"
                     /coded_by="NM_001287578.1:164..1198"
                     /note="isoform d is encoded by transcript variant 1"
                     /db_xref="GeneID:24252"
                     /db_xref="RGD:2326"
ORIGIN      
        1 msshlqspph apsnaafgfp rgagpapppa ppaapeplgg icehetsidi sayidpaafn
       61 defladlfqh srqqekakaa agpaggggdf dypgapagpg gavmsagahg pppgygcaaa
      121 gyldgrlepl yervgapalr plvikqepre edeakqlala glfpyqpppp pppphphasp
      181 ahlaaphlqf qiahcgqttm hlqpghptpp ptpvpsphpa pamgaaglpg pggslkglag
      241 phpdlrtggg ggggagagka kksvdknsne yrvrrernni avrksrdkak qrnvetqqkv
      301 leltsdndrl rkrveqlsre ldtlrgifrq lpesslvkam gnca
//
LOCUS       NP_037052                478 aa            linear   ROD 15-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit alpha
            [Rattus norvegicus].
ACCESSION   NP_037052
VERSION     NP_037052.1
DBSOURCE    REFSEQ: accession NM_012920.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Dorovic,D., Lazarevic,V., Arandelovic,J., Stevanovic,V.,
            Paslawski,W., Zhang,X., Velimirovic,M., Petronijevic,N., Puskas,L.,
            Savic,M.M. and Svenningsson,P.
  TITLE     Maternal deprivation causes CaMKII downregulation and modulates
            glutamate, norepinephrine and serotonin in limbic brain areas in a
            rat model of single prolonged stress
  JOURNAL   J Affect Disord 349, 286-296 (2024)
   PUBMED   38199412
  REMARK    GeneRIF: Maternal deprivation causes CaMKII downregulation and
            modulates glutamate, norepinephrine and serotonin in limbic brain
            areas in a rat model of single prolonged stress.
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Obaid,A.A., Almasmoum,H., Almaimani,R.A., El-Boshy,M., Aslam,A.,
            Idris,S., Ghaith,M.M., El-Readi,M.Z., Ahmad,J., Farrash,W.F.,
            Mujalli,A., Eid,S.Y., Elzubier,M.E. and Refaat,B.
  TITLE     Vitamin D and calcium co-therapy mitigates pre-established cadmium
            nephropathy by regulating renal calcium homeostatic molecules and
            improving anti-oxidative and anti-inflammatory activities in rat
  JOURNAL   J Trace Elem Med Biol 79, 127221 (2023)
   PUBMED   37244046
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Yuan,G., Cao,C., Cao,D., Li,B., Li,X., Li,H., Shen,H., Wang,Z. and
            Chen,G.
  TITLE     Receptor-interacting protein 3-phosphorylated Ca2+
            /calmodulin-dependent protein kinase II and mixed lineage kinase
            domain-like protein mediate intracerebral hemorrhage-induced
            neuronal necroptosis
  JOURNAL   J Neurochem 164 (1), 94-114 (2023)
   PUBMED   36424866
  REMARK    GeneRIF: Receptor-interacting protein 3-phosphorylated Ca[2+]
            /calmodulin-dependent protein kinase II and mixed lineage kinase
            domain-like protein mediate intracerebral hemorrhage-induced
            neuronal necroptosis.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Radiske,A., Gonzalez,M.C., Rossato,J.I., Apolinario,G., de
            Oliveira,J.R., Bevilaqua,L.R.M. and Cammarota,M.
  TITLE     Avoidance memory requires CaMKII activity to persist after recall
  JOURNAL   Mol Brain 14 (1), 167 (2021)
   PUBMED   34775982
  REMARK    GeneRIF: Avoidance memory requires CaMKII activity to persist after
            recall.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Yong,X.L.H., Zhang,L., Yang,L., Chen,X., Tan,J.Z.A., Yu,X.,
            Chandra,M., Livingstone,E., Widagdo,J., Vieira,M.M., Roche,K.W.,
            Lynch,J.W., Keramidas,A., Collins,B.M. and Anggono,V.
  TITLE     Regulation of NMDA receptor trafficking and gating by
            activity-dependent CaMKIIalpha phosphorylation of the GluN2A
            subunit
  JOURNAL   Cell Rep 36 (1), 109338 (2021)
   PUBMED   34233182
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Cho,K.O., Hunt,C.A. and Kennedy,M.B.
  TITLE     The rat brain postsynaptic density fraction contains a homolog of
            the Drosophila discs-large tumor suppressor protein
  JOURNAL   Neuron 9 (5), 929-942 (1992)
   PUBMED   1419001
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Benfenati,F., Valtorta,F., Rubenstein,J.L., Gorelick,F.S.,
            Greengard,P. and Czernik,A.J.
  TITLE     Synaptic vesicle-associated Ca2+/calmodulin-dependent protein
            kinase II is a binding protein for synapsin I
  JOURNAL   Nature 359 (6394), 417-420 (1992)
   PUBMED   1328883
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Sunyer,T. and Sahyoun,N.
  TITLE     Sequence analysis and DNA-protein interactions within the 5'
            flanking region of the Ca2+/calmodulin-dependent protein kinase II
            alpha-subunit gene
  JOURNAL   Proc Natl Acad Sci U S A 87 (1), 278-282 (1990)
   PUBMED   2153289
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bulleit,R.F., Bennett,M.K., Molloy,S.S., Hurley,J.B. and
            Kennedy,M.B.
  TITLE     Conserved and variable regions in the subunits of brain type II
            Ca2+/calmodulin-dependent protein kinase
  JOURNAL   Neuron 1 (1), 63-72 (1988)
   PUBMED   2856087
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J02942.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit alpha"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     alpha chain; alpha CaM kinase II; caMK-II subunit alpha;
                     caM-kinase II alpha chain; caM kinase II subunit alpha;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II alpha; Ca2+/calmodulin-dependent protein kinase II
                     alpha; calcium/calmodulin-dependent protein kinase II
                     alpha subunit"
                     /calculated_mol_wt=53984
     Region          11..302
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            order(19..23,27,40,42,73,89..92,96,98,134..135,137,
                     139..140,142,155..156,159,174..178,180)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(19..22,27,40,42,73,89..92,96,139..140,142,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(23,96,98,134..135,137,139,159,174..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(155..165,168..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:2842767; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Region          290..300
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P11275.1)"
     Site            order(293,295..302)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          310..320
                     /region_name="Interaction with BAALC.
                     /evidence=ECO:0000269|PubMed:15659234"
                     /note="propagated from UniProtKB/Swiss-Prot (P11275.1)"
     Region          314..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11275.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11275.1)"
     CDS             1..478
                     /gene="Camk2a"
                     /gene_synonym="PK2CDD; PKCCD"
                     /coded_by="NM_012920.1:42..1478"
                     /db_xref="GeneID:25400"
                     /db_xref="RGD:2261"
ORIGIN      
        1 matitctrft eeyqlfeelg kgafsvvrrc vkvlagqeya akiintkkls ardhqklere
       61 aricrllkhp nivrlhdsis eeghhylifd lvtggelfed ivareyysea dashciqqil
      121 eavlhchqmg vvhrdlkpen lllasklkga avkladfgla ievegeqqaw fgfagtpgyl
      181 spevlrkdpy gkpvdlwacg vilyillvgy ppfwdedqhr lyqqikagay dfpspewdtv
      241 tpeakdlink mltinpskri taaealkhpw ishrstvasc mhrqetvdcl kkfnarrklk
      301 gailttmlat rnfsggksgg nkkndgvkes sestnttied edtkvrkqei ikvteqliea
      361 isngdfesyt kmcdpgmtaf epealgnlve gldfhrfyfe nlwsrnskpv httilnphih
      421 lmgdesacia yiritqylda ggiprtaqse etrvwhrrdg kwqivhfhrs gapsvlph
//
LOCUS       NP_001178528             841 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 9 [Rattus norvegicus].
ACCESSION   NP_001178528 XP_214662
VERSION     NP_001178528.1
DBSOURCE    REFSEQ: accession NM_001191599.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Hadjikyriacou,A., Yang,Y., Espejo,A., Bedford,M.T. and Clarke,S.G.
  TITLE     Unique Features of Human Protein Arginine Methyltransferase 9
            (PRMT9) and Its Substrate RNA Splicing Factor SF3B2
  JOURNAL   J Biol Chem 290 (27), 16723-16743 (2015)
   PUBMED   25979344
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Yang,Y., Hadjikyriacou,A., Xia,Z., Gayatri,S., Kim,D.,
            Zurita-Lopez,C., Kelly,R., Guo,A., Li,W., Clarke,S.G. and
            Bedford,M.T.
  TITLE     PRMT9 is a type II methyltransferase that methylates the splicing
            factor SAP145
  JOURNAL   Nat Commun 6, 6428 (2015)
   PUBMED   25737013
  REMARK    Publication Status: Online-Only
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000019.1.
            
            On Jul 17, 2010 this sequence version replaced XP_214662.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.909746.1,
                                           SRR26360181.281363.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..841
                     /product="protein arginine N-methyltransferase 9"
                     /EC_number="2.1.1.320"
                     /note="putative protein arginine N-methyltransferase 10;
                     putative protein arginine N-methyltransferase 9; protein
                     arginine methyltransferase 10 (putative)"
                     /calculated_mol_wt=93748
     Region          <40..>140
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(68,71..72,75..76,78,102,105..106,109..110,112..113,
                     136,139..140)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          68..95
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          100..130
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..>323
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..841
                     /gene="Prmt9"
                     /gene_synonym="Prmt10; RGD1306157"
                     /coded_by="NM_001191599.1:123..2648"
                     /db_xref="GeneID:291947"
                     /db_xref="RGD:1306157"
ORIGIN      
        1 mpnsrprsrr sagggagtag rdrlvaqslq saehclgdqd fgtayahyll vlslapelke
       61 dvketfqytl fkwaeelhal nriqdllgcy eqalelfpdd evicnsmgeh lfrmgfrdea
      121 agyfhkavkl npdfndaken fyrvanwlve rwhfimlndt krneiynaai qkavrlgskt
      181 vldigagtgi lsmfakkaga hsvyacelsk tmyelacdvv aankmedgir llhmksldle
      241 ipkhipervs lvvtetvdag vfgegivesl ihawehlllq pqtkgesgsw gkygkvipas
      301 avisgmavec aeirrhhrvs akdiagihlp tnvrfqspay asvdpeetve pyttekmsgi
      361 pggyrpltec fqimkvdfnn lqelkslatr kphslsvpav kegtldaimv wfvlqlddeh
      421 slstspseet cweqavypvq aledywiqpg dqvtmeasch dcylriqgis ilhlehemev
      481 iksftkskdl lslgneaelc salanlqtsr pealeqtcvl epteiallnn ipyhegfrta
      541 mrkvlsslap etpsqpmeah cqdmetnles apstsdpfyv ldvsegfsll pilagtlgqv
      601 qpyssvekdq hcialdlise anhfpketle fwlrhiedea avlqrpksdk lwsiiildvi
      661 epsgliqqei mekaaisrcl lqsggkifpq yvlmfgmlve sqtlveesav qgtehtlgln
      721 iapfinqfqv pirvcldlss lpciplsqpv ellrldlmtp ylntsnrevk vrvcrsgrlt
      781 avpfwfhlcl ddevrldtsg eashwkqaav vldnpiqvqa geelvlsveh hksnisitvk
      841 q
//
LOCUS       NP_113820                454 aa            linear   ROD 15-APR-2025
DEFINITION  caspase-9 isoform 1 [Rattus norvegicus].
ACCESSION   NP_113820
VERSION     NP_113820.1
DBSOURCE    REFSEQ: accession NM_031632.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Bai,L., Yang,J., Zhang,H., Liao,W. and Cen,Y.
  TITLE     PTB domain and leucine zipper motif 1 (APPL1) inhibits myocardial
            ischemia/hypoxia-reperfusion injury via inactivation of apoptotic
            protease activating factor-1 (APAF-1)/Caspase9 signaling pathway
  JOURNAL   Bioengineered 12 (1), 4385-4396 (2021)
   PUBMED   34304702
  REMARK    GeneRIF: PTB domain and leucine zipper motif 1 (APPL1) inhibits
            myocardial ischemia/hypoxia-reperfusion injury via inactivation of
            apoptotic protease activating factor-1 (APAF-1)/Caspase9 signaling
            pathway.
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Martin,S., Harrington,D.A., Ohlander,S., Stupp,S.I., McVary,K.T.
            and Podlasek,C.A.
  TITLE     Peptide amphiphile nanofiber hydrogel delivery of Sonic hedgehog
            protein to the penis and cavernous nerve suppresses intrinsic and
            extrinsic apoptotic signaling mechanisms, which are an underlying
            cause of erectile dysfunction
  JOURNAL   Nanomedicine 37, 102444 (2021)
   PUBMED   34314869
  REMARK    GeneRIF: Peptide amphiphile nanofiber hydrogel delivery of Sonic
            hedgehog protein to the penis and cavernous nerve suppresses
            intrinsic and extrinsic apoptotic signaling mechanisms, which are
            an underlying cause of erectile dysfunction.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Liu,H., Li,J., Jiang,C., Yuan,T. and Ma,H.
  TITLE     Cellular communication network factor 1 (CCN1) knockdown exerts a
            protective effect for hepatic ischemia/reperfusion injury by
            deactivating the MEK/ERK pathway
  JOURNAL   Clin Res Hepatol Gastroenterol 45 (5), 101737 (2021)
   PUBMED   34144219
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Song,Z., Tian,X. and Shi,Q.
  TITLE     Fas, Caspase-8, and Caspase-9 pathway-mediated bile acid-induced
            fetal cardiomyocyte apoptosis in intrahepatic cholestasis pregnant
            rat models
  JOURNAL   J Obstet Gynaecol Res 47 (7), 2298-2306 (2021)
   PUBMED   33847039
  REMARK    GeneRIF: Fas, Caspase-8, and Caspase-9 pathway-mediated bile
            acid-induced fetal cardiomyocyte apoptosis in intrahepatic
            cholestasis pregnant rat models.
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Zhuang,C., Ni,S., Yang,Z.C. and Liu,R.P.
  TITLE     Oxidative Stress Induces Chondrocyte Apoptosis through
            Caspase-Dependent and Caspase-Independent Mitochondrial Pathways
            and the Antioxidant Mechanism of Angelica Sinensis Polysaccharide
  JOURNAL   Oxid Med Cell Longev 2020, 3240820 (2020)
   PUBMED   33224431
  REMARK    GeneRIF: Oxidative Stress Induces Chondrocyte Apoptosis through
            Caspase-Dependent and Caspase-Independent Mitochondrial Pathways
            and the Antioxidant Mechanism of Angelica Sinensis Polysaccharide.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Vu,C.C., Bortner,C.D. and Cidlowski,J.A.
  TITLE     Differential involvement of initiator caspases in apoptotic volume
            decrease and potassium efflux during Fas- and UV-induced cell death
  JOURNAL   J Biol Chem 276 (40), 37602-37611 (2001)
   PUBMED   11431480
  REMARK    GeneRIF: The activation of caspase-8, but not caspase-9, is
            necessary for Fas-induced apoptosis. Conversely, caspase-9, but not
            caspase-8, is important for UV-mediated shrunken morphology and
            apoptosis progression.
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Angelastro,J.M., Moon,N.Y., Liu,D.X., Yang,A.S., Greene,L.A. and
            Franke,T.F.
  TITLE     Characterization of a novel isoform of caspase-9 that inhibits
            apoptosis
  JOURNAL   J Biol Chem 276 (15), 12190-12200 (2001)
   PUBMED   11278518
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Zaidi,A.U., D'Sa-Eipper,C., Brenner,J., Kuida,K., Zheng,T.S.,
            Flavell,R.A., Rakic,P. and Roth,K.A.
  TITLE     Bcl-X(L)-caspase-9 interactions in the developing nervous system:
            evidence for multiple death pathways
  JOURNAL   J Neurosci 21 (1), 169-175 (2001)
   PUBMED   11150333
REFERENCE   9  (residues 1 to 454)
  AUTHORS   D'Sa-Eipper,C., Leonard,J.R., Putcha,G., Zheng,T.S., Flavell,R.A.,
            Rakic,P., Kuida,K. and Roth,K.A.
  TITLE     DNA damage-induced neural precursor cell apoptosis requires p53 and
            caspase 9 but neither Bax nor caspase 3
  JOURNAL   Development 128 (1), 137-146 (2001)
   PUBMED   11092819
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Kermer,P., Ankerhold,R., Klocker,N., Krajewski,S., Reed,J.C. and
            Bahr,M.
  TITLE     Caspase-9: involvement in secondary death of axotomized rat retinal
            ganglion cells in vivo
  JOURNAL   Brain Res Mol Brain Res 85 (1-2), 144-150 (2000)
   PUBMED   11146116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF286006.1, SRR26643290.21211.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..454
                     /product="caspase-9 isoform 1"
                     /EC_number="3.4.22.62"
                     /note="caspase-9-carboxyl-terminal divergent; 25 kDa
                     caspase-9 dominant negative protein; caspase-9 dominant
                     negative form; apoptotic protease Mch-6; Ice-like
                     apoptotic protease 6; apoptotic protease activating factor
                     3; caspase 9, apoptosis-related cysteine peptidase"
                     /calculated_mol_wt=50269
     Region          19..90
                     /region_name="CARD_CASP9"
                     /note="Caspase activation and recruitment domain of
                     Caspase-9; cd08326"
                     /db_xref="CDD:176740"
     Region          190..452
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cd00032"
                     /db_xref="CDD:237997"
     Site            order(218,276,323,330,390..395,399..400)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(275,325)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            order(331,375..376,383,386,389,412,420,426,436,441..442,
                     444,447..448)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(332,374)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     CDS             1..454
                     /gene="Casp9"
                     /gene_synonym="Apaf3; Casp-9-CTD; Casp9_v1; Ice-Lap6;
                     Mch6"
                     /coded_by="NM_031632.3:29..1393"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:58918"
                     /db_xref="RGD:61867"
ORIGIN      
        1 meeadrqllr rcrvrlvrel qvaelwdall srelftrdmi ediqragsgs rrdqarqlvi
       61 dletrgrqal prfiscledt gqgslasflq ssgqaakqdp eavtpldhlv pvvlgpmglk
      121 skeqkvvkld psqpalgnlt pvvlgpeelw ptrlrpevlt petprpvdig sgrahdvctp
      181 gkierhadma ytldsdpcgh cliinnvnfc pssglstrig shvdceklqh rfcwlrfmve
      241 vkndltakkm vtalmemahr dhraldcfvv vilshgcqas hlqfpgavyg tdgcsvsier
      301 ivnifngtgc pslggkpklf fiqacggeqk dhgfevafts sqdkafdsds epdavpyqeg
      361 prtldqldav sslptpsdil vsystfpgfv swrdkksgsw yietldgvle qwarsedlqs
      421 lllrvanavs ekgvykqipg cfnflrkklf fkts
//
LOCUS       NP_001102337             637 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 5 [Rattus norvegicus].
ACCESSION   NP_001102337 XP_001054376 XP_344406
VERSION     NP_001102337.2
DBSOURCE    REFSEQ: accession NM_001108867.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Yeh,C.M., Lai,C.Y., Peng,H.Y., Lin,T.B., Chou,D., Wang,H.H.,
            Yang,P.S., Cheng,J.K., Peng,Y.C. and Hsieh,M.C.
  TITLE     Protein Arginine Methyltransferase 5 Contributes to
            Paclitaxel-Induced Neuropathic Pain by Activating Transient
            Receptor Potential Vanilloid 1 Epigenetic Modification in Dorsal
            Root Ganglion
  JOURNAL   Anesth Analg 138 (5), 1107-1119 (2024)
   PUBMED   37390022
  REMARK    GeneRIF: Protein Arginine Methyltransferase 5 Contributes to
            Paclitaxel-Induced Neuropathic Pain by Activating Transient
            Receptor Potential Vanilloid 1 Epigenetic Modification in Dorsal
            Root Ganglion.
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Cai,S., Wang,P., Xie,T., Li,Z., Li,J., Lan,R., Ding,Y., Lu,J.,
            Ye,J., Wang,J., Li,Z. and Liu,P.
  TITLE     Histone H4R3 symmetric di-methylation by Prmt5 protects against
            cardiac hypertrophy via regulation of Filip1L/beta-catenin
  JOURNAL   Pharmacol Res 161, 105104 (2020)
   PUBMED   32739429
  REMARK    GeneRIF: Histone H4R3 symmetric di-methylation by Prmt5 protects
            against cardiac hypertrophy via regulation of Filip1L/beta-catenin.
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Sun,M., Hussain,S., Hu,Y., Yan,J., Min,Z., Lan,X., Guo,Y., Zhao,Y.,
            Huang,H., Feng,M., Han,Y., Zhang,F., Zhu,W., Meng,L., Li,D., Sun,J.
            and Lu,S.
  TITLE     Maintenance of SOX9 stability and ECM homeostasis by
            selenium-sensitive PRMT5 in cartilage
  JOURNAL   Osteoarthritis Cartilage 27 (6), 932-944 (2019)
   PUBMED   30858101
  REMARK    GeneRIF: Maintenance of SOX9 stability and ECM homeostasis by
            selenium-sensitive PRMT5 in cartilage.
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Zhao,D.Y., Gish,G., Braunschweig,U., Li,Y., Ni,Z., Schmitges,F.W.,
            Zhong,G., Liu,K., Li,W., Moffat,J., Vedadi,M., Min,J., Pawson,T.J.,
            Blencowe,B.J. and Greenblatt,J.F.
  TITLE     SMN and symmetric arginine dimethylation of RNA polymerase II
            C-terminal domain control termination
  JOURNAL   Nature 529 (7584), 48-53 (2016)
   PUBMED   26700805
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Lim,Y., Kwon,Y.H., Won,N.H., Min,B.H., Park,I.S., Paik,W.K. and
            Kim,S.
  TITLE     Multimerization of expressed protein-arginine methyltransferases
            during the growth and differentiation of rat liver
  JOURNAL   Biochim Biophys Acta 1723 (1-3), 240-247 (2005)
   PUBMED   15837430
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Bedford,M.T. and Richard,S.
  TITLE     Arginine methylation an emerging regulator of protein function
  JOURNAL   Mol Cell 18 (3), 263-272 (2005)
   PUBMED   15866169
  REMARK    Review article
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Miranda,T.B., Khusial,P., Cook,J.R., Lee,J.H., Gunderson,S.I.,
            Pestka,S., Zieve,G.W. and Clarke,S.
  TITLE     Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically
            dimethylated at arginine residues in the nucleus
  JOURNAL   Biochem Biophys Res Commun 323 (2), 382-387 (2004)
   PUBMED   15369763
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Fabbrizio,E., El Messaoudi,S., Polanowska,J., Paul,C., Cook,J.R.,
            Lee,J.H., Negre,V., Rousset,M., Pestka,S., Le Cam,A. and Sardet,C.
  TITLE     Negative regulation of transcription by the type II arginine
            methyltransferase PRMT5
  JOURNAL   EMBO Rep 3 (7), 641-645 (2002)
   PUBMED   12101096
  REMARK    GeneRIF: These data provide the first direct experimental evidence
            that PRMT5, a type II arginine methylase, is involved in the
            control of transcription and proliferation.
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Friesen,W.J., Wyce,A., Paushkin,S., Abel,L., Rappsilber,J., Mann,M.
            and Dreyfuss,G.
  TITLE     A novel WD repeat protein component of the methylosome binds Sm
            proteins
  JOURNAL   J Biol Chem 277 (10), 8243-8247 (2002)
   PUBMED   11756452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB814013.1, CO573950.1, DY553859.1, CB793692.1, CK845516.1,
            BQ210423.1, BE116721.1 and AI713913.1.
            
            On Apr 21, 2008 this sequence version replaced NP_001102337.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..637
                     /product="protein arginine N-methyltransferase 5"
                     /EC_number="2.1.1.125"
                     /note="SKB1 homolog; HMT1 hnRNP methyltransferase-like 5"
                     /calculated_mol_wt=72564
     Region          37..290
                     /region_name="PRMT5_TIM"
                     /note="PRMT5 TIM barrel domain; pfam17285"
                     /db_xref="CDD:435840"
     Region          295..464
                     /region_name="PRMT5"
                     /note="PRMT5 arginine-N-methyltransferase; pfam05185"
                     /db_xref="CDD:428356"
     Region          468..635
                     /region_name="PRMT5_C"
                     /note="PRMT5 oligomerization domain; pfam17286"
                     /db_xref="CDD:435841"
     CDS             1..637
                     /gene="Prmt5"
                     /gene_synonym="Hrmt1l5; Skb1"
                     /coded_by="NM_001108867.2:15..1928"
                     /db_xref="GeneID:364382"
                     /db_xref="RGD:1309053"
ORIGIN      
        1 maamavggag gsrvssgrdl ncvpeiadtl gavakqgfdf lcmpvfhprf krefiqepak
       61 nrpgpqtrsd lllsgrdwnt livgklspwi hpdskvekir rnseaamlqe lnfgaylglp
      121 afllplnqed ntnlarvltn hihtghhssm fwmrvplvap edlrddvien aptahteeys
      181 geektwlwwh nfrtlcdysk riavaleiga dlpsshvidr wlgepikaai lptsifltnk
      241 kgfpvlskmq qrlifrllkl evqfiitgtn hhsekefcsy lqyleylsqn rpppnayelf
      301 akgyedylqs plqplmdnle sqtyevfekd pikysqyqqa iykclldrvp eeeketnvqv
      361 lmvlgagrgp lvnaslraak qaerrirlya veknpnavvt lenwqfeewg sqvtvvssdm
      421 rewvapekad iivsellgsf adnelspecl dgaqhflkdd gvsipgeyts flapissskl
      481 ynevracrek drdpeaqfem pyvvrlhnfh qlsapqpcft fshpnrdpmi dnnryctlef
      541 pvevntvlhg fagyfetvly rditlsirpe thspgmfswf piffpikqpi tvhegqnicv
      601 rfwrcsnskk vwyewavtap vcssihnptg rsytigl
//
LOCUS       NP_001020315             445 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_001020315 XP_574738
VERSION     NP_001020315.1
DBSOURCE    REFSEQ: accession NM_001025144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Liu,S., Zhang,B., Guo,H., Ding,Z., Hou,W., Hu,X., Wang,Y., Tan,W.
            and Zhou,S.
  TITLE     The antidepressant effects of protein arginine methyltransferase 2
            involve neuroinflammation
  JOURNAL   Neurochem Int 176, 105728 (2024)
   PUBMED   38561150
  REMARK    GeneRIF: The antidepressant effects of protein arginine
            methyltransferase 2 involve neuroinflammation.
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Gayatri,S. and Bedford,M.T.
  TITLE     Readers of histone methylarginine marks
  JOURNAL   Biochim Biophys Acta 1839 (8), 702-710 (2014)
   PUBMED   24583552
  REMARK    Review article
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Di Lorenzo,A. and Bedford,M.T.
  TITLE     Histone arginine methylation
  JOURNAL   FEBS Lett 585 (13), 2024-2031 (2011)
   PUBMED   21074527
  REMARK    Review article
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Iwasaki,H., Kovacic,J.C., Olive,M., Beers,J.K., Yoshimoto,T.,
            Crook,M.F., Tonelli,L.H. and Nabel,E.G.
  TITLE     Disruption of protein arginine N-methyltransferase 2 regulates
            leptin signaling and produces leanness in vivo through loss of
            STAT3 methylation
  JOURNAL   Circ Res 107 (8), 992-1001 (2010)
   PUBMED   20798359
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Yildirim,A.O., Bulau,P., Zakrzewicz,D., Kitowska,K.E.,
            Weissmann,N., Grimminger,F., Morty,R.E. and Eickelberg,O.
  TITLE     Increased protein arginine methylation in chronic hypoxia: role of
            protein arginine methyltransferases
  JOURNAL   Am J Respir Cell Mol Biol 35 (4), 436-443 (2006)
   PUBMED   16690984
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Yoshimoto,T., Boehm,M., Olive,M., Crook,M.F., San,H.,
            Langenickel,T. and Nabel,E.G.
  TITLE     The arginine methyltransferase PRMT2 binds RB and regulates E2F
            function
  JOURNAL   Exp Cell Res 312 (11), 2040-2053 (2006)
   PUBMED   16616919
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Ganesh,L., Yoshimoto,T., Moorthy,N.C., Akahata,W., Boehm,M.,
            Nabel,E.G. and Nabel,G.J.
  TITLE     Protein methyltransferase 2 inhibits NF-kappaB function and
            promotes apoptosis
  JOURNAL   Mol Cell Biol 26 (10), 3864-3874 (2006)
   PUBMED   16648481
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Qi,C., Chang,J., Zhu,Y., Yeldandi,A.V., Rao,S.M. and Zhu,Y.J.
  TITLE     Identification of protein arginine methyltransferase 2 as a
            coactivator for estrogen receptor alpha
  JOURNAL   J Biol Chem 277 (32), 28624-28630 (2002)
   PUBMED   12039952
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Kzhyshkowska,J., Schutt,H., Liss,M., Kremmer,E., Stauber,R.,
            Wolf,H. and Dobner,T.
  TITLE     Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in
            its Arg-Gly-Gly (RGG) box and interacts with human arginine
            methyltransferase HRMT1L1
  JOURNAL   Biochem J 358 (Pt 2), 305-314 (2001)
   PUBMED   11513728
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079112.1.
            
            On Jul 1, 2005 this sequence version replaced XP_574738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079112.1, SRR8487231.110690.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..445
                     /product="protein arginine N-methyltransferase 2"
                     /EC_number="2.1.1.125"
                     /note="HMT1 hnRNP methyltransferase-like 1"
                     /calculated_mol_wt=50356
     Region          46..98
                     /region_name="SH3_PRMT2"
                     /note="Src homology 3 domain of Protein arginine
                     N-methyltransferase 2; cd11806"
                     /db_xref="CDD:212740"
     Site            order(51,53,56,60,78..79,92,94..95)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212740"
     Region          124..>269
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..445
                     /gene="Prmt2"
                     /gene_synonym="Hrmt1l1"
                     /coded_by="NM_001025144.1:105..1442"
                     /db_xref="GeneID:499420"
                     /db_xref="RGD:1565519"
ORIGIN      
        1 meapaedpsh esqvtpapee dpvdygcemq llqdgaqlql qlqpeefvai adytatdetq
       61 lsflrgekil ilrqttadww wgeragccgy ipanhlgkqv eeydpedtwq deeyfdsygt
      121 lklhlemlad qprttkyhsv ilqnkeslkd kvildvgcgt giislfcahh arpkavyave
      181 asdmaqhtgq lvlqngfadt itvfqqkved vvlpekvdvl vsewmgtcll fefmiesily
      241 ardawlkedg iiwpttaalh lvpcsaekdy hskvlfwdna yefnlsalks laikeffsrp
      301 ksnhilkped clsepctilq ldmrtvqvsd letmrgelrf diqkagtlhg ftawfsvhfq
      361 sleegqpqqv lstgplhptt hwkqtlfmmd dpvpvhtgdv vtgsvvlqrn pvwrrhmsvc
      421 lswvvtsavd ptsqragekv fpiwr
//
LOCUS       NP_037200                132 aa            linear   ROD 15-APR-2025
DEFINITION  fatty acid-binding protein, intestinal [Rattus norvegicus].
ACCESSION   NP_037200
VERSION     NP_037200.1
DBSOURCE    REFSEQ: accession NM_013068.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Zenger,S., Demir Piroglu,I., Cevik,A., Ozcabi,Y., Fakioglu,D.,
            Senol,M., Altintas,M.M., Bildik,N. and Yucel,T.
  TITLE     The importance of serum intestinal fatty acid-binding protein for
            the early diagnosis of acute mesenteric ischemia
  JOURNAL   Ulus Travma Acil Cerrahi Derg 27 (3), 278-283 (2021)
   PUBMED   33884597
  REMARK    GeneRIF: The importance of serum intestinal fatty acid-binding
            protein for the early diagnosis of acute mesenteric ischemia.',
            trans 'Akut mezenter iskeminin erken tanisinda serum intestinal yag
            asidi baglayici proteininin onemi.
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Sahin,A., Altay,D.A., Demir,S., Yulug,E., Mentese,A., Tatli,O.,
            Karaca,Y., Ardic,S., Gunduz,A. and Turedi,S.
  TITLE     Comparison of the diagnostic values of vascular adhesion protein-1
            and intestinal fatty acid-binding protein in the diagnosis of acute
            mesenteric ischemia
  JOURNAL   Eur J Trauma Emerg Surg 45 (3), 545-553 (2019)
   PUBMED   29600311
  REMARK    GeneRIF: In acute mesenteric ischemia, Fabp2 levels are
            significantly increased and correlated with ischemic changes.
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Popescu,G.A., Jung,I., Cordos,B.A., Azamfirei,L., Hutanu,A. and
            Gurzu,S.
  TITLE     Intestinal fatty acid-binding protein, as a marker of anastomotic
            leakage after colonic resection in rats
  JOURNAL   Rom J Morphol Embryol 59 (4), 1075-1081 (2018)
   PUBMED   30845287
  REMARK    GeneRIF: The aim of this experimental study was to determine if the
            type of termino-terminal anastomosis of the colon affect the
            process of healing of the intestinal mucosa and if the severity of
            the anastomotic leakage (AL) can be predicted based on the
            circulating level of intestinal fatty acid-binding protein.
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Mandave,P., Khadke,S., Karandikar,M., Pandit,V., Ranjekar,P.,
            Kuvalekar,A. and Mantri,N.
  TITLE     Antidiabetic, Lipid Normalizing, and Nephroprotective Actions of
            the Strawberry: A Potent Supplementary Fruit
  JOURNAL   Int J Mol Sci 18 (1), 124 (2017)
   PUBMED   28085064
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Zhang,H., Li,Y., Hu,J., Shen,W.J., Singh,M., Hou,X., Bittner,A.,
            Bittner,S., Cortez,Y., Tabassum,J., Kraemer,F.B. and Azhar,S.
  TITLE     Effect of Creosote Bush-Derived NDGA on Expression of Genes
            Involved in Lipid Metabolism in Liver of High-Fructose Fed Rats:
            Relevance to NDGA Amelioration of Hypertriglyceridemia and Hepatic
            Steatosis
  JOURNAL   PLoS One 10 (9), e0138203 (2015)
   PUBMED   26394137
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Scapin,G., Gordon,J.I. and Sacchettini,J.C.
  TITLE     Refinement of the structure of recombinant rat intestinal fatty
            acid-binding apoprotein at 1.2-A resolution
  JOURNAL   J Biol Chem 267 (6), 4253-4269 (1992)
   PUBMED   1740465
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Green,R.P., Cohn,S.M., Sacchettini,J.C., Jackson,K.E. and
            Gordon,J.I.
  TITLE     The mouse intestinal fatty acid binding protein gene: nucleotide
            sequence, pattern of developmental and regional expression, and
            proposed structure of its protein product
  JOURNAL   DNA Cell Biol 11 (1), 31-41 (1992)
   PUBMED   1739433
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Sacchettini,J.C., Gordon,J.I. and Banaszak,L.J.
  TITLE     Refined apoprotein structure of rat intestinal fatty acid binding
            protein produced in Escherichia coli
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 7736-7740 (1989)
   PUBMED   2682622
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Sacchettini,J.C., Gordon,J.I. and Banaszak,L.J.
  TITLE     Crystal structure of rat intestinal fatty-acid-binding protein.
            Refinement and analysis of the Escherichia coli-derived protein
            with bound palmitate
  JOURNAL   J Mol Biol 208 (2), 327-339 (1989)
   PUBMED   2671390
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Sweetser,D.A., Birkenmeier,E.H., Klisak,I.J., Zollman,S.,
            Sparkes,R.S., Mohandas,T., Lusis,A.J. and Gordon,J.I.
  TITLE     The human and rodent intestinal fatty acid binding protein genes. A
            comparative analysis of their structure, expression, and linkage
            relationships
  JOURNAL   J Biol Chem 262 (33), 16060-16071 (1987)
   PUBMED   2824476
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M35992.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: K01180.1, M35992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..132
                     /product="fatty acid-binding protein, intestinal"
                     /note="FABPI; I-FABP; intestinal-type fatty acid-binding
                     protein; intestinal fatty acid binding protein; fatty acid
                     binding protein 1; fatty acid binding protein 2,
                     intestinal"
                     /calculated_mol_wt=14993
     Region          2..131
                     /region_name="FABP2"
                     /note="fatty acid-binding protein 2; cd19445"
                     /db_xref="CDD:381220"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:6582489; propagated from
                     UniProtKB/Swiss-Prot (P02693.4)"
     Site            order(3,15,18..19,22,24,28..29,32,37,39,41,48,50,52,59,61,
                     63,71,73,83,90,92,105,107,114,116,118,127,129)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381220"
     CDS             1..132
                     /gene="Fabp2"
                     /gene_synonym="FABP"
                     /coded_by="NM_013068.1:13..411"
                     /db_xref="GeneID:25598"
                     /db_xref="RGD:2591"
ORIGIN      
        1 mafdgtwkvd rnenyekfme kmginvvkrk lgahdnlklt itqegnkftv kessnfrnid
       61 vvfelgvdfa ysladgtelt gtwtmegnkl vgkfkrvdng keliavreis gneliqtyty
      121 egveakrifk ke
//
LOCUS       NP_062038                194 aa            linear   ROD 15-APR-2025
DEFINITION  interleukin-18 [Rattus norvegicus].
ACCESSION   NP_062038 XP_001070641
VERSION     NP_062038.2
DBSOURCE    REFSEQ: accession NM_019165.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Borgonetti,V., Cruz,B., Vozella,V., Khom,S., Steinman,M.Q.,
            Bullard,R., D'Ambrosio,S., Oleata,C.S., Vlkolinsky,R., Bajo,M.,
            Zorrilla,E.P., Kirson,D. and Roberto,M.
  TITLE     IL-18 Signaling in the Rat Central Amygdala Is Disrupted in a
            Comorbid Model of Post-Traumatic Stress and Alcohol Use Disorder
  JOURNAL   Cells 12 (15), 1943 (2023)
   PUBMED   37566022
  REMARK    GeneRIF: IL-18 Signaling in the Rat Central Amygdala Is Disrupted
            in a Comorbid Model of Post-Traumatic Stress and Alcohol Use
            Disorder.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Tavarna,T., Wolfe,B., Wu,X.J. and Reyes,L.
  TITLE     Porphyromonas gingivalis-mediated disruption in spiral artery
            remodeling is associated with altered uterine NK cell populations
            and dysregulated IL-18 and Htra1
  JOURNAL   Sci Rep 12 (1), 14799 (2022)
   PUBMED   36042379
  REMARK    GeneRIF: Porphyromonas gingivalis-mediated disruption in spiral
            artery remodeling is associated with altered uterine NK cell
            populations and dysregulated IL-18 and Htra1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Abu-Risha,S.E., Mousa,M.A. and Elsisi,A.E.
  TITLE     Protective role of irbesartan against cyclophosphamide-induced
            testicular damage in rats via up-regulating PPAR-gamma signaling
            and ameliorating NF-kappaB/NLRP3/IL-18 inflammatory axis
  JOURNAL   Life Sci 289, 120218 (2022)
   PUBMED   34890588
  REMARK    GeneRIF: Protective role of irbesartan against
            cyclophosphamide-induced testicular damage in rats via
            up-regulating PPAR-gamma signaling and ameliorating
            NF-kappaB/NLRP3/IL-18 inflammatory axis.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Simanullang,R.H., Situmorang,P.C., Ginting,L., Tarigan,E.R.,
            Syahputra,R.A., Chairunisa,C. and Maliki,M.F.
  TITLE     PDGF-beta and IL-18 Expressions on Carcinoma Cervical by
            Rhodomyrtus tomentosa
  JOURNAL   Pak J Biol Sci 25 (11), 986-992 (2022)
   PUBMED   36591929
  REMARK    GeneRIF: PDGF-beta and IL-18 Expressions on Carcinoma Cervical by
            Rhodomyrtus tomentosa.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Wang,Y.F., Wang,Y., Zhang,Y., Guo,X., He,X., Zhang,J.L. and
            Rong,P.J.
  TITLE     [Effect of transcutaneous auricular vagus nerve stimulation on the
            expression of TLR4MyD88IL-18 protein in the prefrontal cortex of
            depression rats]
  JOURNAL   Zhen Ci Yan Jiu 46 (7), 580-585 (2021)
   PUBMED   34369678
  REMARK    GeneRIF: [Effect of transcutaneous auricular vagus nerve
            stimulation on the expression of TLR4MyD88IL-18 protein in the
            prefrontal cortex of depression rats].
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Wildbaum,G., Youssef,S., Grabie,N. and Karin,N.
  TITLE     Neutralizing antibodies to IFN-gamma-inducing factor prevent
            experimental autoimmune encephalomyelitis
  JOURNAL   J Immunol 161 (11), 6368-6374 (1998)
   PUBMED   9834127
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Xu,B., Aoyama,K., Yu,S., Kitani,A., Okamura,H., Kurimoto,M.,
            Matsuyama,T. and Matsushita,T.
  TITLE     Expression of interleukin-18 in murine contact hypersensitivity
  JOURNAL   J Interferon Cytokine Res 18 (9), 653-659 (1998)
   PUBMED   9781803
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Culhane,A.C., Hall,M.D., Rothwell,N.J. and Luheshi,G.N.
  TITLE     Cloning of rat brain interleukin-18 cDNA
  JOURNAL   Mol Psychiatry 3 (4), 362-366 (1998)
   PUBMED   9702748
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Conti,B., Jahng,J.W., Tinti,C., Son,J.H. and Joh,T.H.
  TITLE     Induction of interferon-gamma inducing factor in the adrenal cortex
  JOURNAL   J Biol Chem 272 (4), 2035-2037 (1997)
   PUBMED   8999896
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Micallef,M.J., Ohtsuki,T., Kohno,K., Tanabe,F., Ushio,S., Namba,M.,
            Tanimoto,T., Torigoe,K., Fujii,M., Ikeda,M., Fukuda,S. and
            Kurimoto,M.
  TITLE     Interferon-gamma-inducing factor enhances T helper 1 cytokine
            production by stimulated human T cells: synergism with
            interleukin-12 for interferon-gamma production
  JOURNAL   Eur J Immunol 26 (7), 1647-1651 (1996)
   PUBMED   8766574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Nov 20, 2020 this sequence version replaced NP_062038.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY077842.1, CF109780.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760494, SAMN17050747 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..194
                     /product="interleukin-18"
                     /note="interleukin-1 gamma; IFN-gamma-inducing factor;
                     interferon gamma-inducing factor"
                     /calculated_mol_wt=22182
     Site            36..37
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000250|UniProtKB:Q14116; propagated from
                     UniProtKB/Swiss-Prot (P97636.1)"
     mat_peptide     37..194
                     /product="Interleukin-18. /id=PRO_0000015350"
                     /note="propagated from UniProtKB/Swiss-Prot (P97636.1)"
                     /calculated_mol_wt=18279
     Region          42..188
                     /region_name="beta-trefoil_IL18"
                     /note="beta-trefoil domain found in interleukin-18 (IL-18)
                     and similar proteins; cd23298"
                     /db_xref="CDD:466780"
     Site            order(44,87..90,94..97,127,139..141,145..146,148)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:466780"
     Site            order(53,57,65,67..72,89..91,95..96,139..141,145,148,
                     167..168)
                     /site_type="other"
                     /note="receptor interaction site [polypeptide binding]"
                     /db_xref="CDD:466780"
     Site            71..72
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000250|UniProtKB:Q14116; propagated from
                     UniProtKB/Swiss-Prot (P97636.1)"
     Site            order(140,144,147,151,156,159,175..177,179..182,185)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:466780"
     CDS             1..194
                     /gene="Il18"
                     /gene_synonym="IL-1 gamma; IL-18"
                     /coded_by="NM_019165.2:488..1072"
                     /db_xref="GeneID:29197"
                     /db_xref="RGD:2889"
ORIGIN      
        1 maaipeegsc vnfkemmfid ntlylipedn gdlesdhfgr lhcttavmrs indqvlfvdk
       61 rnppvfedmp didrtanesq trliiymykd sevrglavtl svkdgrmstl scknkiisfe
      121 emnppenidd iksdliffqk rvpghnkmef esslyeghfl acqkeddafk lvlkrkdeng
      181 dksvmftltn lhqs
//
LOCUS       NP_445756               1453 aa            linear   ROD 15-APR-2025
DEFINITION  collagen alpha-1(I) chain precursor [Rattus norvegicus].
ACCESSION   NP_445756 XP_001081230 XP_213440
VERSION     NP_445756.1
DBSOURCE    REFSEQ: accession NM_053304.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1453)
  AUTHORS   Cao,Y., Huang,W., Wu,F., Shang,J., Ping,F., Wang,W., Li,Y., Zhao,X.
            and Zhang,X.
  TITLE     ZFP36 protects lungs from intestinal I/R-induced injury and
            fibrosis through the CREBBP/p53/p21/Bax pathway
  JOURNAL   Cell Death Dis 12 (7), 685 (2021)
   PUBMED   34238924
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1453)
  AUTHORS   Lin,G., Wan,X., Liu,D., Wen,Y., Yang,C. and Zhao,C.
  TITLE     COL1A1 as a potential new biomarker and therapeutic target for type
            2 diabetes
  JOURNAL   Pharmacol Res 165, 105436 (2021)
   PUBMED   33497804
  REMARK    GeneRIF: COL1A1 as a potential new biomarker and therapeutic target
            for type 2 diabetes.
REFERENCE   3  (residues 1 to 1453)
  AUTHORS   Xian,S., Chen,A., Wu,X., Lu,C., Wu,Y., Huang,F. and Zeng,Z.
  TITLE     Activation of activin/Smad2 and 3 signaling pathway and
            the&nbsp;potential involvement of endothelial-mesenchymal
            transition in the valvular damage due to rheumatic heart disease
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33179113
REFERENCE   4  (residues 1 to 1453)
  AUTHORS   Yuan,Y., Naito,H., Kitamori,K., Hashimoto,S., Asano,T. and
            Nakajima,T.
  TITLE     The antihypertensive agent hydralazine reduced extracellular matrix
            synthesis and liver fibrosis in nonalcoholic steatohepatitis
            exacerbated by hypertension
  JOURNAL   PLoS One 15 (12), e0243846 (2020)
   PUBMED   33315911
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1453)
  AUTHORS   Kananykhina,E.Y., Shmakova,T.V., Bolshakova,G.B., Rusanov,F.S.,
            Elchaninov,A.V., Nikitina,M.P., Lokhonina,A.V., Makarov,A.V. and
            Fatkhudinov,T.K.
  TITLE     Expression of Metalloproteinases and Type I and III Collagens
            during Healing of Excisional Skin Wound on the Abdomen and Back in
            Rats
  JOURNAL   Bull Exp Biol Med 168 (6), 812-816 (2020)
   PUBMED   32328952
  REMARK    GeneRIF: Expression of Metalloproteinases and Type I and III
            Collagens during Healing of Excisional Skin Wound on the Abdomen
            and Back in Rats.
REFERENCE   6  (residues 1 to 1453)
  AUTHORS   Federspiel,S.J., DiMari,S.J., Howe,A.M., Guerry-Force,M.L. and
            Haralson,M.A.
  TITLE     Extracellular matrix biosynthesis by cultured fetal rat lung
            epithelial cells. IV. Effects of chronic exposure to retinoic acid
            on growth, differentiation, and collagen biosynthesis
  JOURNAL   Lab Invest 65 (4), 441-450 (1991)
   PUBMED   1921334
REFERENCE   7  (residues 1 to 1453)
  AUTHORS   Tsuneyoshi,T., Westerhausen,A., Constantinou,C.D. and Prockop,D.J.
  TITLE     Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of
            type I procollagen in lethal osteogenesis imperfecta. The
            conformational strain on the triple helix introduced by a glycine
            substitution can be transmitted along the helix
  JOURNAL   J Biol Chem 266 (24), 15608-15613 (1991)
   PUBMED   1874719
REFERENCE   8  (residues 1 to 1453)
  AUTHORS   Federspiel,S.J., DiMari,S.J., Howe,A.M., Guerry-Force,M.L. and
            Haralson,M.A.
  TITLE     Extracellular matrix biosynthesis by cultured fetal rat lung
            epithelial cells. III. Effects of chronic exposure to epidermal
            growth factor on growth, differentiation, and collagen biosynthesis
  JOURNAL   Lab Invest 64 (4), 463-473 (1991)
   PUBMED   2016852
REFERENCE   9  (residues 1 to 1453)
  AUTHORS   Annoni,G., Arosio,B., Santambrogio,D., Gagliano,N. and Zern,M.A.
  TITLE     Albumin and procollagen type I gene regulation in alcohol and
            viral-induced human liver disease
  JOURNAL   Boll Ist Sieroter Milan 70 (1-2), 391-397 (1991)
   PUBMED   1670041
REFERENCE   10 (residues 1 to 1453)
  AUTHORS   Kulozik,M., Hogg,A., Lankat-Buttgereit,B. and Krieg,T.
  TITLE     Co-localization of transforming growth factor beta 2 with alpha
            1(I) procollagen mRNA in tissue sections of patients with systemic
            sclerosis
  JOURNAL   J Clin Invest 86 (3), 917-922 (1990)
   PUBMED   1697606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB693258.1, BC133728.1, CB579389.1, CO397981.1 and BQ206338.1.
            
            On or before Oct 27, 2007 this sequence version replaced
            XP_213440.1, XP_001081230.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z78279.1, BC133728.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1453
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..1453
                     /product="collagen alpha-1(I) chain precursor"
                     /note="procollagen type I, alpha 1; collagen alpha-1(I)
                     chain; collagen, type I, alpha 1; alpha-1 type I collagen;
                     collagen, type 1, alpha 1; procollagen, type 1, alpha 1;
                     type I-alpha 1 collagen"
                     /calculated_mol_wt=135570
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2402
     Region          31..86
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          97..1206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     mat_peptide     152..1207
                     /product="Collagen alpha-1(I) chain. /id=PRO_0000043359"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
                     /calculated_mol_wt=94901
     Region          152..167
                     /region_name="Nonhelical region (N-terminal)"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Site            152
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:5777344; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          168..1181
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Site            179
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            182
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            185
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            194
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            197
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            200
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000305|PubMed:4290711; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            215
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          <222..>451
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            230
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            236
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            245
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            251
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            254
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine, alternate.
                     /evidence=ECO:0000269|PubMed:5411206; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            254
                     /site_type="glycosylation"
                     /note="O-linked (Gal...) hydroxylysine, alternate.
                     /evidence=ECO:0000269|PubMed:5411206; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            278
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            281
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            287
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            296
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            302
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            323
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            332
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            335
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          <357..>604
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            362
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            365
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            377
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            383
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            392
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            398
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            401
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            416
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            419
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            425
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            428
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            440
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            449
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            464
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            470
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            479
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            485
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            494
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            503
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            512
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            518
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            524
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            533
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            536
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          <539..>753
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            545
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            554
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            560
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            572
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            581
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            590
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            593
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            611
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            629
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            635
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            641
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            647
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            653
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            659
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            671
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            680
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            692
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            704
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            707
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          <711..>978
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            713
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            719
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            728
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          734..736
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Site            740
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            746
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            761
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            767
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            788
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            794
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            797
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            806
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            812
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            830
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            839
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            848
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            851
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            860
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            866
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            874
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            875
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            884
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            887
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          <897..>1122
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            908
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            917
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            926
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            935
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            953
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            962
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            965
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            971
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            986
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            992
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            998
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1007
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1013
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1022
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1034
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1037
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1040
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          1082..1084
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Site            1085
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1097
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1097
                     /site_type="glycosylation"
                     /note="O-linked (Gal...) hydroxylysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1109
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1112
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1115
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1133
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02457; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1148
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1153
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1154
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1168
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1169
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1171
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1172
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1174
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1175
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          1176..1186
                     /region_name="Major antigenic determinant (of neutral
                     salt-extracted rat skin collagen)"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Site            1178
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Site            1181
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P11087; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     Region          1182..1207
                     /region_name="Nonhelical region (C-terminal)"
                     /note="propagated from UniProtKB/Swiss-Prot (P02454.5)"
     Region          1216..1452
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; pfam01410"
                     /db_xref="CDD:460199"
     Site            1354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02454.5)"
     CDS             1..1453
                     /gene="Col1a1"
                     /gene_synonym="COLIA1"
                     /coded_by="NM_053304.1:112..4473"
                     /db_xref="GeneID:29393"
                     /db_xref="RGD:61817"
ORIGIN      
        1 mfsfvdlrll lllgatallt hgqedipevs cihnglrvpn getwkpdvcl icichngtav
       61 cdgvlckedl dcpnpqkreg eccpfcpeey vspdaevigv egpkgdpgpq gprgpvgppg
      121 qdgipgqpgl pgppgppgpp gppglggnfa sqmsygydek sagvsvpgpm gpsgprglpg
      181 ppgapgpqgf qgppgepgep gasgpmgprg ppgppgkngd dgeagkpgrp gergppgpqg
      241 arglpgtagl pgmkghrgfs gldgakgdtg pagpkgepgs pgengapgqm gprglpgerg
      301 rpgppgsaga rgndgavgaa gppgptgptg ppgfpgaaga kgeagpqgar gsegpqgvrg
      361 epgppgpaga agpagnpgad gqpgakgang apgiagapgf pgargpsgpq gpsgapgpkg
      421 nsgepgapgn kgdtgakgep gpagvqgppg pageegkrga rgepgpsglp gppgerggpg
      481 srgfpgadgv agpkgpager gspgpagpkg spgeagrpge aglpgakglt gspgspgpdg
      541 ktgppgpagq dgrpgpagpp gargqagvmg fpgpkgtage pgkagergvp gppgavgpag
      601 kdgeagaqga pgpagpager geqgpagspg fqglpgpagp pgeagkpgeq gvpgdlgapg
      661 psgargergf pgergvqgpp gpagprgnng apgndgakgd tgapgapgsq gapglqgmpg
      721 ergaaglpgp kgdrgdagpk gadgspgkdg vrgltgpigp pgpagapgdk getgpsgpag
      781 ptgargapgd rgepgppgpa gfagppgadg qpgakgepgd tgvkgdagpp gpagpagppg
      841 pignvgapgp kgsrgaagpp gatgfpgaag rvgppgpsgn agppgppgpv gkeggkgprg
      901 etgpagrpge vgppgppgpa gekgspgadg pagspgtpgp qgiagqrgvv glpgqrgerg
      961 fpglpgpsge pgkqgpsgas gergppgpmg ppglagppge sgregspgae gspgrdgapg
     1021 akgdrgetgp agppgapgap gapgpvgpag kngdrgetgp agpagpigpa gargpagpqg
     1081 prgdkgetge qgdrgikghr gfsglqgppg spgspgeqgp sgasgpagpr gppgsagspg
     1141 kdglnglpgp igppgprgrt gdsgpagppg ppgppgppgp psggydfsfl pqppqeksqd
     1201 ggryyradda nvvrdrdlev dttlkslsqq ienirspegs rknpartcrd lkmchsdwks
     1261 geywidpnqg cnldaikvyc nmetgqtcvf ptqpsvpqkn wyispnpkek khvwfgesmt
     1321 dgfqfeygse gsdpadvaiq ltflrlmste asqnityhck nsvaymdqqt gnlkkslllq
     1381 gsneielrge gnsrftystl vdgctshtgt wgktvieykt tktsrlpiid vapldigapd
     1441 qefgmdigpa cfv
//
LOCUS       NP_001380670            1173 aa            linear   ROD 15-APR-2025
DEFINITION  SRC kinase signaling inhibitor 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001380670
VERSION     NP_001380670.1
DBSOURCE    REFSEQ: accession NM_001393741.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Calipari,E.S., Godino,A., Salery,M., Damez-Werno,D.M., Cahill,M.E.,
            Werner,C.T., Gancarz,A.M., Peck,E.G., Jlayer,Z., Rabkin,J.,
            Landry,J.A., Smith,A.C.W., Defilippi,P., Kenny,P.J., Hurd,Y.L.,
            Neve,R.L., Dietz,D.M. and Nestler,E.J.
  TITLE     Synaptic Microtubule-Associated Protein EB3 and SRC Phosphorylation
            Mediate Structural and Behavioral Adaptations During Withdrawal
            From Cocaine Self-Administration
  JOURNAL   J Neurosci 39 (29), 5634-5646 (2019)
   PUBMED   31092585
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Wang,W., Zhu,X., Du,X., Xu,A., Yuan,X., Zhan,Y., Liu,M. and Wang,S.
  TITLE     MiR-150 promotes angiogensis and proliferation of endothelial
            progenitor cells in deep venous thrombosis by targeting SRCIN1
  JOURNAL   Microvasc Res 123, 35-41 (2019)
   PUBMED   30315850
  REMARK    GeneRIF: Upregulation of miR-150 promoted angiogenesis and
            proliferation of endothelial progenitor cells by targeting SRCIN1
            in vitro and thrombus resolution in vivo.
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Li,M.Y., Miao,W.Y., Wu,Q.Z., He,S.J., Yan,G., Yang,Y., Liu,J.J.,
            Taketo,M.M. and Yu,X.
  TITLE     A Critical Role of Presynaptic Cadherin/Catenin/p140Cap Complexes
            in Stabilizing Spines and Functional Synapses in the Neocortex
  JOURNAL   Neuron 94 (6), 1155-1172 (2017)
   PUBMED   28641114
  REMARK    GeneRIF: Study demonstrates a critical role of presynaptic
            cadherin/catenin/p140Cap cell adhesion complexes in stabilizing
            functional synapses and spines in the developing neocortex.
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Repetto,D., Camera,P., Melani,R., Morello,N., Russo,I.,
            Calcagno,E., Tomasoni,R., Bianchi,F., Berto,G., Giustetto,M.,
            Berardi,N., Pizzorusso,T., Matteoli,M., Di Stefano,P., Missler,M.,
            Turco,E., Di Cunto,F. and Defilippi,P.
  TITLE     p140Cap regulates memory and synaptic plasticity through
            Src-mediated and citron-N-mediated actin reorganization
  JOURNAL   J Neurosci 34 (4), 1542-1553 (2014)
   PUBMED   24453341
  REMARK    GeneRIF: we here demonstrate that p140Cap is a key element for both
            learning and synaptic plasticity
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Di Stefano,P., Damiano,L., Cabodi,S., Aramu,S., Tordella,L.,
            Praduroux,A., Piva,R., Cavallo,F., Forni,G., Silengo,L., Tarone,G.,
            Turco,E. and Defilippi,P.
  TITLE     p140Cap protein suppresses tumour cell properties, regulating Csk
            and Src kinase activity
  JOURNAL   EMBO J 26 (12), 2843-2855 (2007)
   PUBMED   17525734
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Di Stefano,P., Cabodi,S., Boeri Erba,E., Margaria,V., Bergatto,E.,
            Giuffrida,M.G., Silengo,L., Tarone,G., Turco,E. and Defilippi,P.
  TITLE     P130Cas-associated protein (p140Cap) as a new
            tyrosine-phosphorylated protein involved in cell spreading
  JOURNAL   Mol Biol Cell 15 (2), 787-800 (2004)
   PUBMED   14657239
REFERENCE   9  (residues 1 to 1173)
  AUTHORS   Singh,D. and Lampe,P.D.
  TITLE     Identification of connexin-43 interacting proteins
  JOURNAL   Cell Commun Adhes 10 (4-6), 215-220 (2003)
   PUBMED   14681019
REFERENCE   10 (residues 1 to 1173)
  AUTHORS   Chin,L.S., Nugent,R.D., Raynor,M.C., Vavalle,J.P. and Li,L.
  TITLE     SNIP, a novel SNAP-25-interacting protein implicated in regulated
            exocytosis
  JOURNAL   J Biol Chem 275 (2), 1191-1200 (2000)
   PUBMED   10625663
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF156981.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1173
                     /product="SRC kinase signaling inhibitor 1 isoform 3"
                     /note="p130Cas-associated protein; SNAP25-interacting
                     protein"
                     /calculated_mol_wt=126924
     Region          19..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          219..>298
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          319..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            364
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            371
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          501..676
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            535
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          681..731
                     /region_name="Interaction with SNAP25.
                     /evidence=ECO:0000269|PubMed:10625663"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          <720..874
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          891..949
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          983..1065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1094
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          1141..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     CDS             1..1173
                     /gene="Srcin1"
                     /gene_synonym="P140; p140Cap; Snip"
                     /coded_by="NM_001393741.2:34..3555"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:56029"
                     /db_xref="RGD:708439"
ORIGIN      
        1 mqpwqclrrf alawwertae grarspreev gprdpggrge pdperssppm lsaddaeypr
       61 eyrtlggggs ggsggrrfsn vglvhtserr htviaaqsle alsglqkada drkrdafmdh
      121 lkskypqhal alrgqqdrmr eqqpnywsfk trssrhtqga qpgladqaak lsyasaesle
      181 tmseaelplg fsrmnrfrqs lplsrsasqt klrspgvlfl qfgeetrrvh ithevssldt
      241 lhaliahmfp qkltmgmlks pntailikde arnvfyeled vrdiqdrsii kiyrkeplya
      301 afpgshltng dlrremvyas ressptrrln nlspashlas sspppglpsg lpsglpsgsp
      361 srsrlsyagg rppsyagspv hhaaerlgga ptsqgvspsp sailerrdvk pdedlagkag
      421 gmvlvkgegl yadpygllhe grlslaaaag dpfaypgagg lykrgsvrsl stysaaalqs
      481 dledslykag aggplygdgy gfrlppsspq kladvsapsg gpppphspys gppsrgspvr
      541 qsfrkdsgss svfaespggk arstgastag appselfpgp gerslvgfgp pvpakdtetr
      601 ermeamekqi asltglvqsa llrgsepetp sekiegsnga atpsapvcgs gsrssgatpv
      661 sgppppavss tpagqptavs rlqmqmhlrg lqnsasdlrg qlqqlrklql qnqesvrall
      721 krteaelsmr vseaarrqed plqrqrtlve eerlrylnde elitqqlndl eksvekiqrd
      781 vahnhrlvpg peleekalvl kqlgetltel kahfpglqsk mrvvlrveve avkflkeepq
      841 rldgllkrcr vvtdtlaqir rqvdegvwpp pnnllnqspk kvaaetdfsk gldfeippps
      901 pplnlhelsg paegtpltpk sgnptkglda pskrnmdkav sveaaerdwe ekraaltqys
      961 akdinrllee tqaellkaip dldcaskthp gptptpdhkp pkaphgqkaa prtepsgrrg
     1021 sdeltvpryr tekpsksppp ppprrsfpss hgltttrtge vvvtskkdsv fikkaeseel
     1081 eiqkpqvklr ravsevvrpa stppimasai kdeddeerii aelesgggsv ppmkvvtpga
     1141 srlkaaqgpa gspdkgkhgk qrteymriqa qqq
//
LOCUS       NP_445921                 84 aa            linear   ROD 15-APR-2025
DEFINITION  hepcidin precursor [Rattus norvegicus].
ACCESSION   NP_445921
VERSION     NP_445921.1
DBSOURCE    REFSEQ: accession NM_053469.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Flores,S.R.L., Nelson,S., Woloshun,R.R., Wang,X., Ha,J.H.,
            Lee,J.K., Yu,Y., Merlin,D. and Collins,J.F.
  TITLE     Intestinal iron absorption is appropriately modulated to match
            physiological demand for iron in wild-type and iron-loaded Hamp
            (hepcidin) knockout rats during acute colitis
  JOURNAL   PLoS One 16 (6), e0252998 (2021)
   PUBMED   34143808
  REMARK    GeneRIF: Intestinal iron absorption is appropriately modulated to
            match physiological demand for iron in wild-type and iron-loaded
            Hamp (hepcidin) knockout rats during acute colitis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Pourmohammad,P., Alipanah-Moghadam,R., Nemati,A., Malekzadeh,V. and
            Mahmoodzadeh,Y.
  TITLE     Comparison of the effects of zinc oxide and zinc oxide
            nanoparticles on the expression of hepcidin gene in rat liver
  JOURNAL   Horm Mol Biol Clin Investig 42 (1), 43-48 (2020)
   PUBMED   33544508
  REMARK    GeneRIF: Comparison of the effects of zinc oxide and zinc oxide
            nanoparticles on the expression of hepcidin gene in rat liver.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Huang,Y., Zhang,H., Wang,C., Zhou,J., Li,Y. and Hu,C.
  TITLE     DNA methylation suppresses liver Hamp expression in response to
            iron deficiency after bariatric surgery
  JOURNAL   Surg Obes Relat Dis 16 (1), 109-118 (2020)
   PUBMED   31839527
  REMARK    GeneRIF: DNA methylation suppresses liver Hamp expression in
            response to iron deficiency after bariatric surgery.
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Liu,J., Wan,M., Zhang,Y., Zhang,S., Zhang,H. and Wu,S.
  TITLE     Dysfunction of Iron Metabolism and Iron-Regulatory Proteins in the
            Rat Hippocampus After Heat Stroke
  JOURNAL   Shock 51 (6), 780-786 (2019)
   PUBMED   29757912
  REMARK    GeneRIF: ata thereby indicate that heat stroke can decrease
            learning ability and memory in rats. The mechanism may be related
            to changes of iron levels, as well as Fpn1 and hepcidin expression,
            in the hippocampus.
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Marmur,J., Beshara,S., Eggertsen,G., Onelov,L., Albiin,N.,
            Danielsson,O., Hultcrantz,R. and Stal,P.
  TITLE     Hepcidin levels correlate to liver iron content, but not
            steatohepatitis, in non-alcoholic fatty liver disease
  JOURNAL   BMC Gastroenterol 18 (1), 78 (2018)
   PUBMED   29871592
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 84)
  AUTHORS   Nicolas,G., Bennoun,M., Devaux,I., Beaumont,C., Grandchamp,B.,
            Kahn,A. and Vaulont,S.
  TITLE     Lack of hepcidin gene expression and severe tissue iron overload in
            upstream stimulatory factor 2 (USF2) knockout mice
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8780-8785 (2001)
   PUBMED   11447267
REFERENCE   7  (residues 1 to 84)
  AUTHORS   Pigeon,C., Ilyin,G., Courselaud,B., Leroyer,P., Turlin,B.,
            Brissot,P. and Loreal,O.
  TITLE     A new mouse liver-specific gene, encoding a protein homologous to
            human antimicrobial peptide hepcidin, is overexpressed during iron
            overload
  JOURNAL   J Biol Chem 276 (11), 7811-7819 (2001)
   PUBMED   11113132
REFERENCE   8  (residues 1 to 84)
  AUTHORS   Park,C.H., Valore,E.V., Waring,A.J. and Ganz,T.
  TITLE     Hepcidin, a urinary antimicrobial peptide synthesized in the liver
  JOURNAL   J Biol Chem 276 (11), 7806-7810 (2001)
   PUBMED   11113131
REFERENCE   9  (residues 1 to 84)
  AUTHORS   Krause,A., Neitz,S., Magert,H.J., Schulz,A., Forssmann,W.G.,
            Schulz-Knappe,P. and Adermann,K.
  TITLE     LEAP-1, a novel highly disulfide-bonded human peptide, exhibits
            antimicrobial activity
  JOURNAL   FEBS Lett 480 (2-3), 147-150 (2000)
   PUBMED   11034317
REFERENCE   10 (residues 1 to 84)
  AUTHORS   Venta,P.J., Montgomery,J.C., Hewett-Emmett,D., Wiebauer,K. and
            Tashian,R.E.
  TITLE     Structure and exon to protein domain relationships of the mouse
            carbonic anhydrase II gene
  JOURNAL   J Biol Chem 260 (22), 12130-12135 (1985)
   PUBMED   2995362
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF344185.1, AW534367.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..84
                     /product="hepcidin precursor"
                     /calculated_mol_wt=6958
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2346
     Region          32..84
                     /region_name="Hepcidin"
                     /note="pfam06446"
                     /db_xref="CDD:461915"
     mat_peptide     60..84
                     /product="Hepcidin. /id=PRO_0000013386"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MH3.1)"
                     /calculated_mol_wt=2720
     CDS             1..84
                     /gene="Hamp"
                     /gene_synonym="Hepc"
                     /coded_by="NM_053469.2:18..272"
                     /db_xref="GeneID:84604"
                     /db_xref="RGD:70971"
ORIGIN      
        1 malstriqaa cllllllasl ssgaylrqqt rqttalqpwh gaesktddsa llmlkrrkrd
       61 tnfpiclfcc kccknsscgl ccit
//
LOCUS       NP_071613                482 aa            linear   ROD 15-APR-2025
DEFINITION  caspase-8 [Rattus norvegicus].
ACCESSION   NP_071613
VERSION     NP_071613.1
DBSOURCE    REFSEQ: accession NM_022277.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Lu,E., Zhuo,Q., Chen,F., Lin,Q. and Wang,X.
  TITLE     [Role of caspase-8 in stem cell transplantation alleviates rat
            cerebral cortex apoptosis after cardiopulmonary resuscitation]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 34 (12), 1280-1284 (2022)
   PUBMED   36567583
  REMARK    GeneRIF: [Role of caspase-8 in stem cell transplantation alleviates
            rat cerebral cortex apoptosis after cardiopulmonary resuscitation].
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Martin,S., Harrington,D.A., Ohlander,S., Stupp,S.I., McVary,K.T.
            and Podlasek,C.A.
  TITLE     Peptide amphiphile nanofiber hydrogel delivery of Sonic hedgehog
            protein to the penis and cavernous nerve suppresses intrinsic and
            extrinsic apoptotic signaling mechanisms, which are an underlying
            cause of erectile dysfunction
  JOURNAL   Nanomedicine 37, 102444 (2021)
   PUBMED   34314869
  REMARK    GeneRIF: Peptide amphiphile nanofiber hydrogel delivery of Sonic
            hedgehog protein to the penis and cavernous nerve suppresses
            intrinsic and extrinsic apoptotic signaling mechanisms, which are
            an underlying cause of erectile dysfunction.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Song,Z., Tian,X. and Shi,Q.
  TITLE     Fas, Caspase-8, and Caspase-9 pathway-mediated bile acid-induced
            fetal cardiomyocyte apoptosis in intrahepatic cholestasis pregnant
            rat models
  JOURNAL   J Obstet Gynaecol Res 47 (7), 2298-2306 (2021)
   PUBMED   33847039
  REMARK    GeneRIF: Fas, Caspase-8, and Caspase-9 pathway-mediated bile
            acid-induced fetal cardiomyocyte apoptosis in intrahepatic
            cholestasis pregnant rat models.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Yang,X., Zeng,Q. and Tezel,G.
  TITLE     Regulation of distinct caspase-8 functions in retinal ganglion
            cells and astroglia in experimental glaucoma
  JOURNAL   Neurobiol Dis 150, 105258 (2021)
   PUBMED   33434617
  REMARK    GeneRIF: Regulation of distinct caspase-8 functions in retinal
            ganglion cells and astroglia in experimental glaucoma.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Wang,H., Yu,Q., Zhang,Z.L., Ma,H. and Li,X.Q.
  TITLE     Involvement of the miR-137-3p/CAPN-2 Interaction in
            Ischemia-Reperfusion-Induced Neuronal Apoptosis through Modulation
            of p35 Cleavage and Subsequent Caspase-8 Overactivation
  JOURNAL   Oxid Med Cell Longev 2020, 2616871 (2020)
   PUBMED   33456665
  REMARK    GeneRIF: Involvement of the miR-137-3p/CAPN-2 Interaction in
            Ischemia-Reperfusion-Induced Neuronal Apoptosis through Modulation
            of p35 Cleavage and Subsequent Caspase-8 Overactivation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Nakagawa,T., Zhu,H., Morishima,N., Li,E., Xu,J., Yankner,B.A. and
            Yuan,J.
  TITLE     Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and
            cytotoxicity by amyloid-beta
  JOURNAL   Nature 403 (6765), 98-103 (2000)
   PUBMED   10638761
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Estelles,A., Charlton,C.A. and Blau,H.M.
  TITLE     The phosphoprotein protein PEA-15 inhibits Fas- but increases
            TNF-R1-mediated caspase-8 activity and apoptosis
  JOURNAL   Dev Biol 216 (1), 16-28 (1999)
   PUBMED   10588860
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Lin,Y., Devin,A., Rodriguez,Y. and Liu,Z.G.
  TITLE     Cleavage of the death domain kinase RIP by caspase-8 prompts
            TNF-induced apoptosis
  JOURNAL   Genes Dev 13 (19), 2514-2526 (1999)
   PUBMED   10521396
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Sanchez,I., Xu,C.J., Juo,P., Kakizaka,A., Blenis,J. and Yuan,J.
  TITLE     Caspase-8 is required for cell death induced by expanded
            polyglutamine repeats
  JOURNAL   Neuron 22 (3), 623-633 (1999)
   PUBMED   10197541
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Sakamaki,K., Tsukumo,S. and Yonehara,S.
  TITLE     Molecular cloning and characterization of mouse caspase-8
  JOURNAL   Eur J Biochem 253 (2), 399-405 (1998)
   PUBMED   9654089
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF279308.1, SRR26643299.39425.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..482
                     /product="caspase-8"
                     /EC_number="3.4.22.61"
                     /calculated_mol_wt=55208
     Region          3..84
                     /region_name="DED_Caspase_8_r1"
                     /note="Death effector domain, repeat 1, of Caspase-8;
                     cd08333"
                     /db_xref="CDD:260041"
     Site            order(16..17,21,24..25,27..28,64,68)
                     /site_type="other"
                     /note="putative DED1/DED2 interface [polypeptide binding]"
                     /db_xref="CDD:260041"
     Region          98..179
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O89110; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O89110; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Site            218..219
                     /site_type="cleavage"
                     /note="Cleavage, by autocatalytic cleavage.
                     /evidence=ECO:0000250|UniProtKB:Q14790; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Region          227..480
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cd00032"
                     /db_xref="CDD:237997"
     Site            order(262,320,360,367,413..418,422..423)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            order(319,362)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q14790; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Site            order(368,398..399,406,409,412,435,444,450,464,469..470,
                     472,475..476)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(369,397)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     Site            376..377
                     /site_type="cleavage"
                     /note="Cleavage, by CASP6.
                     /evidence=ECO:0000250|UniProtKB:Q14790; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Site            388..389
                     /site_type="cleavage"
                     /note="Cleavage, by autocatalytic cleavage.
                     /evidence=ECO:0000250|UniProtKB:Q14790; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q14790; propagated from
                     UniProtKB/Swiss-Prot (Q9JHX4.1)"
     CDS             1..482
                     /gene="Casp8"
                     /gene_synonym="CASP-8"
                     /coded_by="NM_022277.2:318..1766"
                     /db_xref="GeneID:64044"
                     /db_xref="RGD:620945"
ORIGIN      
        1 mdfhsclydi aerlgneela alkflcldhi pqkkqesind vlvlfqrlqe egmleednls
       61 flkellfhis rrdllsrvlk sspeemvrel qvlgkaqvsa yrvmlfklse dmdkedlksf
      121 kflliteipk cklqdnssll difvemekrt ilaennlvtl ksicfrvnrs llgriddyer
      181 ssterrmste ggeelpvsvl devtikmqdm wdspgeqese slnsdnvyqm kskprgycli
      241 fnnnnfskar edipklsnmr drkgtnydee alsktfkelh feivsfsdct asqihevlvs
      301 yqskdhkgkd cficcilshg dkgivygtdg keasiyelts yftgskcpsl agkpkiffiq
      361 acqgnnfqka vpvpdetgle qehvleedss syknyipdea dfllgmatvk ncvsyrdptr
      421 gtwyiqslcq slrercprge dilsiltgvn ydvsnkdnpr nmgkqmpqpi ftlrkklffp
      481 pn
//
LOCUS       NP_001101224             530 aa            linear   ROD 15-APR-2025
DEFINITION  TNF receptor-associated factor 6 [Rattus norvegicus].
ACCESSION   NP_001101224 XP_001079281 XP_230377
VERSION     NP_001101224.1
DBSOURCE    REFSEQ: accession NM_001107754.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Yang,P., Wang,Y., Ge,W., Jing,Y., Hu,H., Yin,J., Xue,M., Wang,Y.,
            Li,X., Li,X., Shi,Y., Tan,J., Li,Y. and Yan,S.
  TITLE     m6A methyltransferase METTL3 contributes to sympathetic
            hyperactivity post-MI via promoting TRAF6-dependent mitochondrial
            ROS production
  JOURNAL   Free Radic Biol Med 209 (Pt 2), 342-354 (2023)
   PUBMED   37898386
  REMARK    GeneRIF: m6A methyltransferase METTL3 contributes to sympathetic
            hyperactivity post-MI via promoting TRAF6-dependent mitochondrial
            ROS production.
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Wei,B., Su,Z., Yang,H., Feng,Y., Meng,C. and Liang,Z.
  TITLE     Inhibition of TRAF6 improves hyperlipidemic acute pancreatitis by
            alleviating pyroptosis in vitro and in vivo rat models
  JOURNAL   Biol Direct 18 (1), 23 (2023)
   PUBMED   37165439
  REMARK    GeneRIF: Inhibition of TRAF6 improves hyperlipidemic acute
            pancreatitis by alleviating pyroptosis in vitro and in vivo rat
            models.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Xia,P., Marjan,M., Liu,Z., Zhou,W., Zhang,Q., Cheng,C., Zhao,M.,
            Tao,Y., Wang,Z. and Ye,Z.
  TITLE     Chrysophanol postconditioning attenuated cerebral
            ischemia-reperfusion injury induced NLRP3-related pyroptosis in a
            TRAF6-dependent manner
  JOURNAL   Exp Neurol 357, 114197 (2022)
   PUBMED   35932799
  REMARK    GeneRIF: Chrysophanol postconditioning attenuated cerebral
            ischemia-reperfusion injury induced NLRP3-related pyroptosis in a
            TRAF6-dependent manner.
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Zhang,T. and Ge,J.
  TITLE     Mechanism of CREB1 in cardiac function of rats with heart failure
            via regulating the microRNA-376a-3p/TRAF6 axis
  JOURNAL   Mamm Genome 33 (3), 490-501 (2022)
   PUBMED   35217880
  REMARK    GeneRIF: Mechanism of CREB1 in cardiac function of rats with heart
            failure via regulating the microRNA-376a-3p/TRAF6 axis.
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Wei,B., Wu,Q., Yang,X., Lai,C., Su,Z. and Liang,Z.
  TITLE     Effect of TRAF6 in acute pancreatitis-induced intestinal barrier
            injury via TLR4/NF-kappaB signal pathway
  JOURNAL   Tissue Cell 76, 101792 (2022)
   PUBMED   35405432
  REMARK    GeneRIF: Effect of TRAF6 in acute pancreatitis-induced intestinal
            barrier injury via TLR4/NF-kappaB signal pathway.
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Zapata,J.M., Pawlowski,K., Haas,E., Ware,C.F., Godzik,A. and
            Reed,J.C.
  TITLE     A diverse family of proteins containing tumor necrosis factor
            receptor-associated factor domains
  JOURNAL   J Biol Chem 276 (26), 24242-24252 (2001)
   PUBMED   11279055
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Lomaga,M.A., Henderson,J.T., Elia,A.J., Robertson,J., Noyce,R.S.,
            Yeh,W.C. and Mak,T.W.
  TITLE     Tumor necrosis factor receptor-associated factor 6 (TRAF6)
            deficiency results in exencephaly and is required for apoptosis
            within the developing CNS
  JOURNAL   J Neurosci 20 (19), 7384-7393 (2000)
   PUBMED   11007897
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Naito,A., Azuma,S., Tanaka,S., Miyazaki,T., Takaki,S., Takatsu,K.,
            Nakao,K., Nakamura,K., Katsuki,M., Yamamoto,T. and Inoue,J.
  TITLE     Severe osteopetrosis, defective interleukin-1 signalling and lymph
            node organogenesis in TRAF6-deficient mice
  JOURNAL   Genes Cells 4 (6), 353-362 (1999)
   PUBMED   10421844
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Lomaga,M.A., Yeh,W.C., Sarosi,I., Duncan,G.S., Furlonger,C., Ho,A.,
            Morony,S., Capparelli,C., Van,G., Kaufman,S., van der Heiden,A.,
            Itie,A., Wakeham,A., Khoo,W., Sasaki,T., Cao,Z., Penninger,J.M.,
            Paige,C.J., Lacey,D.L., Dunstan,C.R., Boyle,W.J., Goeddel,D.V. and
            Mak,T.W.
  TITLE     TRAF6 deficiency results in osteopetrosis and defective
            interleukin-1, CD40, and LPS signaling
  JOURNAL   Genes Dev 13 (8), 1015-1024 (1999)
   PUBMED   10215628
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Ninomiya-Tsuji,J., Kishimoto,K., Hiyama,A., Inoue,J., Cao,Z. and
            Matsumoto,K.
  TITLE     The kinase TAK1 can activate the NIK-I kappaB as well as the MAP
            kinase cascade in the IL-1 signalling pathway
  JOURNAL   Nature 398 (6724), 252-256 (1999)
   PUBMED   10094049
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168921.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_230377.4, XP_001079281.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168921.1, SRR8487227.172149.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q31"
     Protein         1..530
                     /product="TNF receptor-associated factor 6"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase TRAF6; TNF
                     receptor-associated factor 6, E3 ubiquitin protein ligase;
                     RING-type E3 ubiquitin transferase TRAF6"
                     /calculated_mol_wt=60122
     Region          1..362
                     /region_name="Interaction with TAX1BP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF45.1)"
     Region          67..124
                     /region_name="mRING-HC-C3HC3D_TRAF6"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tumor necrosis factor (TNF) receptor-associated
                     factor 6 (TRAF6) and similar proteins; cd16643"
                     /db_xref="CDD:438305"
     Site            order(67..68,82,84..88,118..122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438305"
     Site            order(69,71..75,97,100..101,106)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438305"
     Region          <132..219
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          157..183
                     /region_name="TRAF6_Z2"
                     /note="TNF receptor-associated factor 6 zinc finger 2;
                     pfam18048"
                     /db_xref="CDD:436235"
     Region          204..261
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          359..508
                     /region_name="MATH_TRAF6"
                     /note="Tumor Necrosis Factor Receptor (TNFR)-Associated
                     Factor (TRAF) family, TRAF6 subfamily, TRAF domain,
                     C-terminal MATH subdomain; composed of proteins with
                     similarity to human TRAF6, including the Drosophila
                     protein DTRAF2. TRAF molecules serve as adapter...;
                     cd03776"
                     /db_xref="CDD:239745"
     Site            order(362,364,392..393,425,428,445)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:239745"
     Region          363..530
                     /region_name="Interaction with TANK.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4K3"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF45.1)"
     Site            order(400,418,464..466,476..480)
                     /site_type="active"
                     /note="TNFR binding site [active]"
                     /db_xref="CDD:239745"
     CDS             1..530
                     /gene="Traf6"
                     /coded_by="NM_001107754.2:191..1783"
                     /db_xref="GeneID:311245"
                     /db_xref="RGD:1306853"
ORIGIN      
        1 msllncensc assqsssdcc aamanscsaa mkddsvsgcv stgnlsssfm eeiqgydvef
       61 dppleskyec piclmalrea vqtpcghrfc kacitksird aghkcpvdne illenqlfpd
      121 nfakreilsl tvkcpnkgcv qkmelrhled hqvhcefalv icpqcqrffq kcqinkhiie
      181 dcprrqvscv ncavpmpyee keihdqscpl aniiceycgt ilireqmpnh ydldcptapv
      241 pctfsvfgch ekmqrnhlar hlqentqlhm rllaqavhnv nlslrpcdas spsrgcrped
      301 pnyeetvkql egrlvrqdhq ireltakmet qsmhvselkr tirsledkva emeaqqcngi
      361 yiwkignfgm hlksqeeerp vvihspgfyt grpgyklcmr lhlqlptaqr canyislfvh
      421 tmqgeydshl pwpfqgtirl tildqseavi rqnheevmda kpellafqrp tiprnpkgfg
      481 yvtfmhleal rqgtfikddt llvrcevstr fdmgglrkeg fqprstdagv
//
LOCUS       NP_001099190             314 aa            linear   ROD 15-APR-2025
DEFINITION  NF-kappa-B inhibitor alpha [Rattus norvegicus].
ACCESSION   NP_001099190 XP_001075778 XP_343066
VERSION     NP_001099190.2
DBSOURCE    REFSEQ: accession NM_001105720.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cui,L. and Ma,J.
  TITLE     NEDD4L Promotes IkappaBalpha Ubiquitination and Degradation in the
            Pathogenesis of Diabetic Retinopathy
  JOURNAL   Curr Eye Res 49 (1), 62-72 (2024)
   PUBMED   37768316
  REMARK    GeneRIF: NEDD4L Promotes IkappaBalpha Ubiquitination and
            Degradation in the Pathogenesis of Diabetic Retinopathy.
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Fan,Y., Wang,J., Feng,Z., Cao,K., Xu,H. and Liu,J.
  TITLE     Pinitol attenuates LPS-induced pneumonia in experimental animals:
            Possible role via inhibition of the TLR-4 and
            NF-kappaB/IkappaBalpha signaling cascade pathway
  JOURNAL   J Biochem Mol Toxicol 35 (1), e22622 (2021)
   PUBMED   32926510
  REMARK    GeneRIF: Pinitol attenuates LPS-induced pneumonia in experimental
            animals: Possible role via inhibition of the TLR-4 and
            NF-kappaB/IkappaBalpha signaling cascade pathway.
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Li,S., Jiang,L., Yang,Y., Cao,J., Zhang,Q., Zhang,J., Wang,R.,
            Deng,X. and Li,Y.
  TITLE     Siglec1 enhances inflammation through miR-1260-dependent
            degradation of IkappaBalpha in COPD
  JOURNAL   Exp Mol Pathol 113, 104398 (2020)
   PUBMED   32007531
  REMARK    GeneRIF: the present study demonstrated that Siglec1 exerts its
            proinflammatory effects through increasing miR-1260, leading to
            decreased expression of IkappaBalpha.
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Liang,W.J., Yang,H.W., Liu,H.N., Qian,W. and Chen,X.L.
  TITLE     HMGB1 upregulates NF-kB by inhibiting IKB-alpha and associates with
            diabetic retinopathy
  JOURNAL   Life Sci 241, 117146 (2020)
   PUBMED   31816325
  REMARK    GeneRIF: High IKB-alpha expression is associated with diabetic
            retinopathy.
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Zabel,U., Henkel,T., Silva,M.S. and Baeuerle,P.A.
  TITLE     Nuclear uptake control of NF-kappa B by MAD-3, an I kappa B protein
            present in the nucleus
  JOURNAL   EMBO J 12 (1), 201-211 (1993)
   PUBMED   7679069
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Tewari,M., Dobrzanski,P., Mohn,K.L., Cressman,D.E., Hsu,J.C.,
            Bravo,R. and Taub,R.
  TITLE     Rapid induction in regenerating liver of RL/IF-1 (an I kappa B that
            inhibits NF-kappa B, RelB-p50, and c-Rel-p50) and PHF, a novel
            kappa B site-binding complex
  JOURNAL   Mol Cell Biol 12 (6), 2898-2908 (1992)
   PUBMED   1588976
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Tewari,M., Mohn,K.L., Yue,F.E. and Taub,R.
  TITLE     Sequence of rat RL/IF-1 encoding an IkappaB, and comparison with
            related proteins containing notch-like repeats [corrected]
  JOURNAL   Nucleic Acids Res 20 (3), 607 (1992)
   PUBMED   1741294
  REMARK    Erratum:[Nucleic Acids Res 1992 Jun 11;20(11):2931]
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Baeuerle,P.A. and Baltimore,D.
  TITLE     I kappa B: a specific inhibitor of the NF-kappa B transcription
            factor
  JOURNAL   Science 242 (4878), 540-546 (1988)
   PUBMED   3140380
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB793714.1, CB316505.1, BF417507.1, CB324027.1 and CA509173.1.
            
            On Nov 15, 2007 this sequence version replaced NP_001099190.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ234262.1, BC166886.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..314
                     /product="NF-kappa-B inhibitor alpha"
                     /note="ikB-alpha; ikappaBalpha; I-kappa-B-alpha; Inhibitor
                     of nuclear factor of kappa light chain gene enhancer in
                     B-cells, alpha; nuclear factor of kappa light chain gene
                     enhancer in B-cells inhibitor, alpha; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells
                     inhibitor, alpha"
                     /calculated_mol_wt=34886
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Region          30..36
                     /region_name="Destruction motif.
                     /evidence=ECO:0000250|UniProtKB:P25963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA and IKKB.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Region          34..>256
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA, IKKB, IKKE and TBK1.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by Tyr-kinases.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Region          45..54
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:P25963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Region          73..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..139
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Region          110..120
                     /region_name="Nuclear import signal.
                     /evidence=ECO:0000250|UniProtKB:P25963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Site            order(143,145,149..150,153..155,157..158,162,165,180,182,
                     184,188..189,192..194,196..197,201,204,213,216,218,
                     222..223,226..228,230..231,235,238)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          143..180
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..172
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Region          182..213
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          182..211
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Site            210
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Region          216..246
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          216..245
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63746.1)"
     Site            244
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25963; propagated from
                     UniProtKB/Swiss-Prot (Q63746.1)"
     CDS             1..314
                     /gene="Nfkbia"
                     /gene_synonym="RL/IF-1"
                     /coded_by="NM_001105720.2:120..1064"
                     /db_xref="GeneID:25493"
                     /db_xref="RGD:3171"
ORIGIN      
        1 mfqpaghgqd wamegprdgl kkerlvddrh dsgldsmkde dyeqmvkelr eirlqpqeap
       61 laaepwkqql tedgdsflhl aiiheektlt mevigqvkgd laflnfqnnl qqtplhlavi
      121 tnqpgiaeal lkagcdpelr dfrgntplhl aceqgclasv avltqtctpq hlhsvlqatn
      181 ynghtclhla sihgylgive hlvtlgadvn aqepcngrta lhlavdlqnp dlvslllkcg
      241 advnrvtyqg yspyqltwgr pstriqqqlg qltlenlqtl pesedeesyd teseftedel
      301 pyddcvfggq rltl
//
LOCUS       NP_062251               1197 aa            linear   ROD 15-APR-2025
DEFINITION  SRC kinase signaling inhibitor 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_062251
VERSION     NP_062251.1
DBSOURCE    REFSEQ: accession NM_019378.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Calipari,E.S., Godino,A., Salery,M., Damez-Werno,D.M., Cahill,M.E.,
            Werner,C.T., Gancarz,A.M., Peck,E.G., Jlayer,Z., Rabkin,J.,
            Landry,J.A., Smith,A.C.W., Defilippi,P., Kenny,P.J., Hurd,Y.L.,
            Neve,R.L., Dietz,D.M. and Nestler,E.J.
  TITLE     Synaptic Microtubule-Associated Protein EB3 and SRC Phosphorylation
            Mediate Structural and Behavioral Adaptations During Withdrawal
            From Cocaine Self-Administration
  JOURNAL   J Neurosci 39 (29), 5634-5646 (2019)
   PUBMED   31092585
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Wang,W., Zhu,X., Du,X., Xu,A., Yuan,X., Zhan,Y., Liu,M. and Wang,S.
  TITLE     MiR-150 promotes angiogensis and proliferation of endothelial
            progenitor cells in deep venous thrombosis by targeting SRCIN1
  JOURNAL   Microvasc Res 123, 35-41 (2019)
   PUBMED   30315850
  REMARK    GeneRIF: Upregulation of miR-150 promoted angiogenesis and
            proliferation of endothelial progenitor cells by targeting SRCIN1
            in vitro and thrombus resolution in vivo.
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Li,M.Y., Miao,W.Y., Wu,Q.Z., He,S.J., Yan,G., Yang,Y., Liu,J.J.,
            Taketo,M.M. and Yu,X.
  TITLE     A Critical Role of Presynaptic Cadherin/Catenin/p140Cap Complexes
            in Stabilizing Spines and Functional Synapses in the Neocortex
  JOURNAL   Neuron 94 (6), 1155-1172 (2017)
   PUBMED   28641114
  REMARK    GeneRIF: Study demonstrates a critical role of presynaptic
            cadherin/catenin/p140Cap cell adhesion complexes in stabilizing
            functional synapses and spines in the developing neocortex.
REFERENCE   4  (residues 1 to 1197)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   5  (residues 1 to 1197)
  AUTHORS   Repetto,D., Camera,P., Melani,R., Morello,N., Russo,I.,
            Calcagno,E., Tomasoni,R., Bianchi,F., Berto,G., Giustetto,M.,
            Berardi,N., Pizzorusso,T., Matteoli,M., Di Stefano,P., Missler,M.,
            Turco,E., Di Cunto,F. and Defilippi,P.
  TITLE     p140Cap regulates memory and synaptic plasticity through
            Src-mediated and citron-N-mediated actin reorganization
  JOURNAL   J Neurosci 34 (4), 1542-1553 (2014)
   PUBMED   24453341
  REMARK    GeneRIF: we here demonstrate that p140Cap is a key element for both
            learning and synaptic plasticity
REFERENCE   6  (residues 1 to 1197)
  AUTHORS   Di Stefano,P., Damiano,L., Cabodi,S., Aramu,S., Tordella,L.,
            Praduroux,A., Piva,R., Cavallo,F., Forni,G., Silengo,L., Tarone,G.,
            Turco,E. and Defilippi,P.
  TITLE     p140Cap protein suppresses tumour cell properties, regulating Csk
            and Src kinase activity
  JOURNAL   EMBO J 26 (12), 2843-2855 (2007)
   PUBMED   17525734
REFERENCE   7  (residues 1 to 1197)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 1197)
  AUTHORS   Di Stefano,P., Cabodi,S., Boeri Erba,E., Margaria,V., Bergatto,E.,
            Giuffrida,M.G., Silengo,L., Tarone,G., Turco,E. and Defilippi,P.
  TITLE     P130Cas-associated protein (p140Cap) as a new
            tyrosine-phosphorylated protein involved in cell spreading
  JOURNAL   Mol Biol Cell 15 (2), 787-800 (2004)
   PUBMED   14657239
REFERENCE   9  (residues 1 to 1197)
  AUTHORS   Singh,D. and Lampe,P.D.
  TITLE     Identification of connexin-43 interacting proteins
  JOURNAL   Cell Commun Adhes 10 (4-6), 215-220 (2003)
   PUBMED   14681019
REFERENCE   10 (residues 1 to 1197)
  AUTHORS   Chin,L.S., Nugent,R.D., Raynor,M.C., Vavalle,J.P. and Li,L.
  TITLE     SNIP, a novel SNAP-25-interacting protein implicated in regulated
            exocytosis
  JOURNAL   J Biol Chem 275 (2), 1191-1200 (2000)
   PUBMED   10625663
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF156982.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1197
                     /product="SRC kinase signaling inhibitor 1 isoform 2"
                     /note="p130Cas-associated protein; SNAP25-interacting
                     protein"
                     /calculated_mol_wt=129614
     Region          19..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          219..>298
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          319..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            364
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            371
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          501..676
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            535
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          681..731
                     /region_name="Interaction with SNAP25.
                     /evidence=ECO:0000269|PubMed:10625663"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          <720..874
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          891..949
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9C0H9; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          983..1065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Site            1094
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QWI6; propagated from
                     UniProtKB/Swiss-Prot (Q9QXY2.1)"
     Region          1141..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXY2.1)"
     CDS             1..1197
                     /gene="Srcin1"
                     /gene_synonym="P140; p140Cap; Snip"
                     /coded_by="NM_019378.3:34..3627"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:56029"
                     /db_xref="RGD:708439"
ORIGIN      
        1 mqpwqclrrf alawwertae grarspreev gprdpggrge pdperssppm lsaddaeypr
       61 eyrtlggggs ggsggrrfsn vglvhtserr htviaaqsle alsglqkada drkrdafmdh
      121 lkskypqhal alrgqqdrmr eqqpnywsfk trssrhtqga qpgladqaak lsyasaesle
      181 tmseaelplg fsrmnrfrqs lplsrsasqt klrspgvlfl qfgeetrrvh ithevssldt
      241 lhaliahmfp qkltmgmlks pntailikde arnvfyeled vrdiqdrsii kiyrkeplya
      301 afpgshltng dlrremvyas ressptrrln nlspashlas sspppglpsg lpsglpsgsp
      361 srsrlsyagg rppsyagspv hhaaerlgga ptsqgvspsp sailerrdvk pdedlagkag
      421 gmvlvkgegl yadpygllhe grlslaaaag dpfaypgagg lykrgsvrsl stysaaalqs
      481 dledslykag aggplygdgy gfrlppsspq kladvsapsg gpppphspys gppsrgspvr
      541 qsfrkdsgss svfaespggk arstgastag appselfpgp gerslvgfgp pvpakdtetr
      601 ermeamekqi asltglvqsa llrgsepetp sekiegsnga atpsapvcgs gsrssgatpv
      661 sgppppavss tpagqptavs rlqmqmhlrg lqnsasdlrg qlqqlrklql qnqesvrall
      721 krteaelsmr vseaarrqed plqrqrtlve eerlrylnde elitqqlndl eksvekiqrd
      781 vahnhrlvpg peleekalvl kqlgetltel kahfpglqsk mrvvlrveve avkflkeepq
      841 rldgllkrcr vvtdtlaqir rqvdegvwpp pnnllnqspk kvaaetdfsk gldfeippps
      901 pplnlhelsg paegtpltpk sgnptkglda pskrnmdkav sveaaerdwe ekraaltqys
      961 akdinrllee tqaellkaip dldcaskthp gptptpdhkp pkaphgqkaa prtepsgrrg
     1021 sdeltvpryr tekpsksppp ppprrsfpss hgltttrtge vvvtskkdsv fikkaeseel
     1081 eiqkpqvklr ravsevvrpa stppimasai kdeddeerii aelesgggsv ppmkvvtpga
     1141 srlkaaqgpa gspdkgkhgk qrteymriqa qqqvrvgyqa prplegctpr lcympls
//
LOCUS       NP_036986                178 aa            linear   ROD 15-APR-2025
DEFINITION  interleukin-10 precursor [Rattus norvegicus].
ACCESSION   NP_036986
VERSION     NP_036986.2
DBSOURCE    REFSEQ: accession NM_012854.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Ren,Z.Y., Wang,J., Xu,F., Gao,Y., He,Q., Pan,B. and Lyu,S.C.
  TITLE     IL-10 dependent modulatory effect of regulatory B10 cells on local
            scar formation following Roux-en-Y choledochojejunostomy in a novel
            rat model
  JOURNAL   Int Immunopharmacol 126, 111309 (2024)
   PUBMED   38048666
  REMARK    GeneRIF: IL-10 dependent modulatory effect of regulatory B10 cells
            on local scar formation following Roux-en-Y choledochojejunostomy
            in a novel rat model.
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Yang,L., Cao,J., Du,Y., Zhang,X., Hong,W., Peng,B., Wu,J., Weng,Q.,
            Wang,J. and Gao,J.
  TITLE     Initial IL-10 production dominates the therapy of mesenchymal stem
            cell scaffold in spinal cord injury
  JOURNAL   Theranostics 14 (2), 879-891 (2024)
   PUBMED   38169599
  REMARK    GeneRIF: Initial IL-10 production dominates the therapy of
            mesenchymal stem cell scaffold in spinal cord injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Kosyreva,A.M., Dzhalilova,D.S., Tsvetkov,I.S., Makarova,M.A. and
            Makarova,O.V.
  TITLE     Ex Vivo Production of IL-1beta and IL-10 by Activated Blood Cells
            of Wistar Rats with Different Resistance to Hypoxia after Systemic
            Inflammatory Response Syndrome
  JOURNAL   Bull Exp Biol Med 176 (2), 290-296 (2023)
   PUBMED   38194074
  REMARK    GeneRIF: Ex Vivo Production of IL-1beta and IL-10 by Activated
            Blood Cells of Wistar Rats with Different Resistance to Hypoxia
            after Systemic Inflammatory Response Syndrome.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Changaei,M., Javidan,M., Ramezani Tehrani,F., Mosaffa,N.,
            Noroozzadeh,M., Hosseinzadeh,R. and Rajaei,S.
  TITLE     Reduced expression of Il10, Stat3, Hoxa10, and Itgb3 in the embryo
            implantation site of rat model with prenatal androgen-induced
            polycystic ovary syndrome
  JOURNAL   Am J Reprod Immunol 90 (1), e13702 (2023)
   PUBMED   37062956
  REMARK    GeneRIF: Reduced expression of Il10, Stat3, Hoxa10, and Itgb3 in
            the embryo implantation site of rat model with prenatal
            androgen-induced polycystic ovary syndrome.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Huynh,T., Reed,C., Blackwell,Z., Phelps,P., Herrera,L.C.P.,
            Almodovar,J., Zaharoff,D.A. and Wolchok,J.
  TITLE     Local IL-10 delivery modulates the immune response and enhances
            repair of volumetric muscle loss muscle injury
  JOURNAL   Sci Rep 13 (1), 1983 (2023)
   PUBMED   36737628
  REMARK    GeneRIF: Local IL-10 delivery modulates the immune response and
            enhances repair of volumetric muscle loss muscle injury.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Berg,D.J., Kuhn,R., Rajewsky,K., Muller,W., Menon,S., Davidson,N.,
            Grunig,G. and Rennick,D.
  TITLE     Interleukin-10 is a central regulator of the response to LPS in
            murine models of endotoxic shock and the Shwartzman reaction but
            not endotoxin tolerance
  JOURNAL   J Clin Invest 96 (5), 2339-2347 (1995)
   PUBMED   7593621
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Stuber,E., Neurath,M., Calderhead,D., Fell,H.P. and Strober,W.
  TITLE     Cross-linking of OX40 ligand, a member of the TNF/NGF cytokine
            family, induces proliferation and differentiation in murine splenic
            B cells
  JOURNAL   Immunity 2 (5), 507-521 (1995)
   PUBMED   7749983
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Goodman,R.E., Oblak,J. and Bell,R.G.
  TITLE     Synthesis and characterization of rat interleukin-10 (IL-10) cDNA
            clones from the RNA of cultured OX8- OX22- thoracic duct T cells
  JOURNAL   Biochem Biophys Res Commun 189 (1), 1-7 (1992)
   PUBMED   1280414
REFERENCE   9  (residues 1 to 178)
  AUTHORS   de Waal Malefyt,R., Abrams,J., Bennett,B., Figdor,C.G. and de
            Vries,J.E.
  TITLE     Interleukin 10(IL-10) inhibits cytokine synthesis by human
            monocytes: an autoregulatory role of IL-10 produced by monocytes
  JOURNAL   J Exp Med 174 (5), 1209-1220 (1991)
   PUBMED   1940799
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Vieira,P., de Waal-Malefyt,R., Dang,M.N., Johnson,K.E.,
            Kastelein,R., Fiorentino,D.F., deVries,J.E., Roncarolo,M.G.,
            Mosmann,T.R. and Moore,K.W.
  TITLE     Isolation and expression of human cytokine synthesis inhibitory
            factor cDNA clones: homology to Epstein-Barr virus open reading
            frame BCRFI
  JOURNAL   Proc Natl Acad Sci U S A 88 (4), 1172-1176 (1991)
   PUBMED   1847510
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L02926.1.
            
            On Jun 10, 2007 this sequence version replaced NP_036986.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L02926.1, X60675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /strain="AO"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..178
                     /product="interleukin-10 precursor"
                     /note="CSIF; IL-10; cytokine synthesis inhibitory factor;
                     interferon 2a"
                     /calculated_mol_wt=18641
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29456.1)"
                     /calculated_mol_wt=1803
     Region          14..174
                     /region_name="IL10"
                     /note="Interleukin 10; pfam00726"
                     /db_xref="CDD:334228"
     mat_peptide     19..178
                     /product="Interleukin-10. /id=PRO_0000015372"
                     /note="propagated from UniProtKB/Swiss-Prot (P29456.1)"
                     /calculated_mol_wt=18641
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29456.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29456.1)"
     CDS             1..178
                     /gene="Il10"
                     /gene_synonym="If2a; IL10X"
                     /coded_by="NM_012854.2:2..538"
                     /db_xref="GeneID:25325"
                     /db_xref="RGD:2886"
ORIGIN      
        1 mpgsallccl lllagvktsk ghsirgdnnc thfpvsqthm lrelraafsq vktffqkkdq
       61 ldnilltdsl lqdfkgylgc qalsemikfy lvevmpqaen hgpeikehln slgeklktlw
      121 iqlrrchrfl pcenkskave qvkndfnklq dkgvykamne fdifinciea yvtlkmkn
//
LOCUS       NP_001274506             395 aa            linear   ROD 15-APR-2025
DEFINITION  CCAAT/enhancer-binding protein alpha isoform c [Rattus norvegicus].
ACCESSION   NP_001274506
VERSION     NP_001274506.1
DBSOURCE    REFSEQ: accession NM_001287577.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Wu,K., Huang,S., Zheng,F. and Liu,Y.
  TITLE     The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway
  JOURNAL   Acta Diabetol 60 (11), 1491-1503 (2023)
   PUBMED   37392202
  REMARK    GeneRIF: The CEBPA-FGF21 regulatory network may participate in the
            T2DM-induced skeletal muscle atrophy by regulating the
            autophagy-lysosomal pathway.
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Xu,Z., Yao,X., Zhao,Y. and Yao,B.
  TITLE     C/EBPalpha involvement in microglial polarization via HDAC1/STAT3
            pathway aggravated sevoflurane-induced cognitive impairment in aged
            rats
  JOURNAL   PeerJ 11, e15466 (2023)
   PUBMED   37361037
  REMARK    GeneRIF: C/EBPalpha involvement in microglial polarization via
            HDAC1/STAT3 pathway aggravated sevoflurane-induced cognitive
            impairment in aged rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Lu,H., Chen,Y., Chen,Y., Huang,L. and Chen,L.
  TITLE     C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A Regulates
            Autophagy, Matrix Metalloproteinase Expression, and Phenotypic of
            Vascular Smooth Muscle Cells in Aortic Dissection
  JOURNAL   J Immunol Res 2022, 7465353 (2022)
   PUBMED   36132983
  REMARK    GeneRIF: C/EBPalpha-Mediated Transcriptional Activation of PIK3C2A
            Regulates Autophagy, Matrix Metalloproteinase Expression, and
            Phenotypic of Vascular Smooth Muscle Cells in Aortic Dissection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Duan,P., Wang,H., Yi,X., Zhang,H., Chen,H. and Pan,Z.
  TITLE     C/EBPalpha regulates the fate of bone marrow mesenchymal stem cells
            and steroid-induced avascular necrosis of the femoral head by
            targeting the PPARgamma signalling pathway
  JOURNAL   Stem Cell Res Ther 13 (1), 342 (2022)
   PUBMED   35883192
  REMARK    GeneRIF: C/EBPalpha regulates the fate of bone marrow mesenchymal
            stem cells and steroid-induced avascular necrosis of the femoral
            head by targeting the PPARgamma signalling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Muller,C., Bremer,A., Schreiber,S., Eichwald,S. and Calkhoven,C.F.
  TITLE     Nucleolar retention of a translational C/EBPalpha isoform
            stimulates rDNA transcription and cell size
  JOURNAL   EMBO J 29 (5), 897-909 (2010)
   PUBMED   20075868
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Calkhoven,C.F., Muller,C. and Leutz,A.
  TITLE     Translational control of C/EBPalpha and C/EBPbeta isoform
            expression
  JOURNAL   Genes Dev 14 (15), 1920-1932 (2000)
   PUBMED   10921906
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Lincoln,A.J., Monczak,Y., Williams,S.C. and Johnson,P.F.
  TITLE     Inhibition of CCAAT/enhancer-binding protein alpha and beta
            translation by upstream open reading frames
  JOURNAL   J Biol Chem 273 (16), 9552-9560 (1998)
   PUBMED   9545285
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Stephens,J.M. and Pekala,P.H.
  TITLE     Transcriptional repression of the C/EBP-alpha and GLUT4 genes in
            3T3-L1 adipocytes by tumor necrosis factor-alpha. Regulations is
            coordinate and independent of protein synthesis
  JOURNAL   J Biol Chem 267 (19), 13580-13584 (1992)
   PUBMED   1618860
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Thomassin,H., Hamel,D., Bernier,D., Guertin,M. and Belanger,L.
  TITLE     Molecular cloning of two C/EBP-related proteins that bind to the
            promoter and the enhancer of the alpha 1-fetoprotein gene. Further
            analysis of C/EBP beta and C/EBP gamma
  JOURNAL   Nucleic Acids Res 20 (12), 3091-3098 (1992)
   PUBMED   1377818
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Samuelsson,L., Stromberg,K., Vikman,K., Bjursell,G. and Enerback,S.
  TITLE     The CCAAT/enhancer binding protein and its role in adipocyte
            differentiation: evidence for direct involvement in terminal
            adipocyte development
  JOURNAL   EMBO J 10 (12), 3787-3793 (1991)
   PUBMED   1935900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            Summary: This intronless gene encodes a transcription factor that
            contains a basic leucine zipper (bZIP) domain and recognizes the
            CCAAT motif in the promoters of target genes. The encoded protein
            functions in homodimers and also heterodimers with
            CCAAT/enhancer-binding proteins beta and gamma. Activity of this
            protein can modulate the expression of genes involved in cell cycle
            regulation as well as in body weight homeostasis. The use of
            alternative in-frame non-AUG (CUG) and AUG start codons results in
            protein isoforms with different lengths. Differential translation
            initiation is mediated by an out-of-frame, upstream open reading
            frame which is located between the CUG and the first AUG start
            codons. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (1) can initiate translation from
            an upstream non-AUG (CUG) site, and also from three conserved
            downstream, in-frame AUG sites. The isoform (c, also known as
            extended) represented in this RefSeq results from translation
            initiation at the upstream CUG start codon. Isoform c is the
            longest isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22582416.154041.1,
                                        SRR26643429.1696.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 20075868
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..395
                     /product="CCAAT/enhancer-binding protein alpha isoform c"
                     /note="C/EBP alpha; CAAT/enhancer-binding protein,
                     DNA-binding protein; CCAAT/enhancer binding protein
                     (C/EBP), alpha"
                     /calculated_mol_wt=41309
     Region          38
                     /region_name="alternative AUG start codon; isoform a"
     Region          52
                     /region_name="alternative AUG start codon; isoform d"
     Region          155
                     /region_name="alternative AUG start codon; isoform b"
     Region          317..377
                     /region_name="bZIP_CEBPA"
                     /note="Basic leucine zipper (bZIP) domain of
                     CCAAT/enhancer-binding protein alpha (CEBPA): a
                     DNA-binding and dimerization domain; cd14711"
                     /db_xref="CDD:269859"
     Region          319..377
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269859"
     Site            order(322..323,325..326,328..330,332..333,335..337,339,
                     341)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269859"
     Site            order(344,347,350..351,354..355,357..358,360..362,
                     364..365,368..369,371..372,375..376)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269859"
     CDS             1..395
                     /gene="Cebpa"
                     /gene_synonym="DBPCEP"
                     /coded_by="NM_001287577.1:11..1198"
                     /note="isoform c is encoded by transcript variant 1;
                     non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:24252"
                     /db_xref="RGD:2326"
ORIGIN      
        1 mrgrgrvgvl ggrrrqrrha qaggrrgspc rensnspmes adfyeaeprp pmsshlqspp
       61 hapsnaafgf prgagpappp appaapeplg gicehetsid isayidpaaf ndefladlfq
      121 hsrqqekaka aagpaggggd fdypgapagp ggavmsagah gpppgygcaa agyldgrlep
      181 lyervgapal rplvikqepr eedeakqlal aglfpyqppp ppppphphas pahlaaphlq
      241 fqiahcgqtt mhlqpghptp pptpvpsphp apamgaaglp gpggslkgla gphpdlrtgg
      301 gggggagagk akksvdknsn eyrvrrernn iavrksrdka kqrnvetqqk vleltsdndr
      361 lrkrveqlsr eldtlrgifr qlpesslvka mgnca
//
LOCUS       NP_112282                360 aa            linear   ROD 15-APR-2025
DEFINITION  mitogen-activated protein kinase 14 [Rattus norvegicus].
ACCESSION   NP_112282
VERSION     NP_112282.2
DBSOURCE    REFSEQ: accession NM_031020.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Tu,Z., Jin,P., Wang,Q., Feng,Y., Chu,X., Fu,L., Hou,S. and Li,W.
  TITLE     Dynamically changed HSP70 after reperfusion following cerebral
            infarction in human and rats: correlation with p38 MAPK
  JOURNAL   Neuroreport 35 (7), 439-446 (2024)
   PUBMED   38597327
  REMARK    GeneRIF: Dynamically changed HSP70 after reperfusion following
            cerebral infarction in human and rats: correlation with p38 MAPK.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Ye,H., He,S., Du,Y., Wang,Y., Hu,Y., Zhao,C., Jin,Y., Liu,F. and
            Guo,Y.
  TITLE     Involvement of CD44 and MAPK14-mediated ferroptosis in hemorrhagic
            shock
  JOURNAL   Apoptosis 29 (1-2), 154-168 (2024)
   PUBMED   37751106
  REMARK    GeneRIF: Involvement of CD44 and MAPK14-mediated ferroptosis in
            hemorrhagic shock.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Zhu,P., Wu,X., Ni,L., Chen,K., Dong,Z., Du,J., Kong,F., Mao,Y.,
            Tao,H., Chu,M., Mao,H., Yang,H., Liu,Q., Gan,M. and Geng,D.
  TITLE     Inhibition of PP2A ameliorates intervertebral disc degeneration by
            reducing annulus fibrosus cells apoptosis via p38/MAPK signal
            pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (1), 166888 (2024)
   PUBMED   37722489
  REMARK    GeneRIF: Inhibition of PP2A ameliorates intervertebral disc
            degeneration by reducing annulus fibrosus cells apoptosis via
            p38/MAPK signal pathway.
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Sase,K., Tsukahara,C., Fujita,N., Arizono,I., Otsubo,M. and
            Kitaoka,Y.
  TITLE     Inhibition of p38 ameliorates axonal loss with modulation of
            autophagy in TNF-induced optic nerve damage
  JOURNAL   Int Ophthalmol 43 (9), 3067-3074 (2023)
   PUBMED   37062014
  REMARK    GeneRIF: Inhibition of p38 ameliorates axonal loss with modulation
            of autophagy in TNF-induced optic nerve damage.
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Muraleva,N.A. and Kolosova,N.G.
  TITLE     P38 MAPK Signaling in the Retina: Effects of Aging and Age-Related
            Macular Degeneration
  JOURNAL   Int J Mol Sci 24 (14), 11586 (2023)
   PUBMED   37511345
  REMARK    GeneRIF: P38 MAPK Signaling in the Retina: Effects of Aging and
            Age-Related Macular Degeneration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Hedges,J.C., Yamboliev,I.A., Ngo,M., Horowitz,B., Adam,L.P. and
            Gerthoffer,W.T.
  TITLE     p38 mitogen-activated protein kinase expression and activation in
            smooth muscle
  JOURNAL   Am J Physiol 275 (2), C527-C534 (1998)
   PUBMED   9688607
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Nemeth,E., Bole-Feysot,C. and Tashima,L.S.
  TITLE     Suppression subtractive hybridization (SSH) identifies prolactin
            stimulation of p38 MAP kinase gene expression in Nb2 T lymphoma
            cells: molecular cloning of rat p38 MAP kinase
  JOURNAL   J Mol Endocrinol 20 (1), 151-156 (1998)
   PUBMED   9513091
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Lee,J.C., Laydon,J.T., McDonnell,P.C., Gallagher,T.F., Kumar,S.,
            Green,D., McNulty,D., Blumenthal,M.J., Heys,J.R., Landvatter,S.W.,
            Strickler,J.E., McLaughlin,M.M., Siemens,I.R., Fisher,S.M.,
            Livi,G.P., White,J.R., Adams,J.L. and Young,P.R.
  TITLE     A protein kinase involved in the regulation of inflammatory
            cytokine biosynthesis
  JOURNAL   Nature 372 (6508), 739-746 (1994)
   PUBMED   7997261
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Han,J., Lee,J.D., Bibbs,L. and Ulevitch,R.J.
  TITLE     A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian
            cells
  JOURNAL   Science 265 (5173), 808-811 (1994)
   PUBMED   7914033
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Williams,A.F., Barclay,A.N., Letarte-Muirhead,M. and Morris,R.J.
  TITLE     Rat thy-1 antigens from thymus and brain: their tissue
            distribution, purification, and chemical composition
  JOURNAL   Cold Spring Harb Symp Quant Biol 41 Pt 1, 51-61 (1977)
   PUBMED   70317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1 and BC092193.1.
            
            On Apr 11, 2005 this sequence version replaced NP_112282.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092193.1, AB000783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..360
                     /product="mitogen-activated protein kinase 14"
                     /EC_number="2.7.11.24"
                     /note="MAP kinase p38 alpha; mitogen-activated protein
                     kinase p38 alpha; MAP kinase 14; p38 mitogen activated
                     protein kinase; MAPK 14; reactive kinase; MAP kinase 2;
                     cytokine-supressive anti-inflammatory drug binding
                     protein; p38alpha Exip; p38 MAP kinase; MAP kinase Mxi2;
                     Csaids binding protein; MAX-interacting protein 2;
                     stress-activated protein kinase 2A; cytokine suppressive
                     anti-inflammatory drug binding protein; mitogen-activated
                     protein kinase 14A"
                     /calculated_mol_wt=41342
     Region          6..350
                     /region_name="STKc_p38alpha"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     p38alpha Mitogen-Activated Protein Kinase (also called
                     MAPK14); cd07877"
                     /db_xref="CDD:143382"
     Site            order(30..33,35,37..38,51,53,70,75,84,86,104,106..109,112,
                     114..115,150,152,154..155,157,167..168,170..171,180,
                     182..185,187,225)
                     /site_type="active"
                     /db_xref="CDD:143382"
     Site            order(30..31,35,37..38,51,53,75,84,86,104,106..109,112,
                     150,152,154..155,167..168,170)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:143382"
     Site            order(70,114,150,152,171,180,182..185,187,225)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:143382"
     Site            order(111,116,119..120,125..126,129,158..162,311)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:143382"
     Site            167..187
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:143382"
     Site            order(191..192,195,197,199..201,236,242,246,249,259,
                     291..294)
                     /site_type="lipid-binding"
                     /note="lipid binding site [chemical binding]"
                     /db_xref="CDD:143382"
     CDS             1..360
                     /gene="Mapk14"
                     /gene_synonym="CRK1; CSBP; Csbp1; Csbp2; CSPB1; Exip; Hog;
                     Mxi2; p38; p38alpha; p38Hog; Prkm14; Prkm15; RK; Sapk2A"
                     /coded_by="NM_031020.3:321..1403"
                     /db_xref="GeneID:81649"
                     /db_xref="RGD:70496"
ORIGIN      
        1 msqerptfyr qelnktvwev peryqnlspv gsgaygsvca afdtktghrv avkklsrpfq
       61 siihakrtyr elrllkhmkh enviglldvf tparsleefn dvylvthlmg adlnnivkcq
      121 kltddhvqfl iyqilrglky ihsadiihrd lkpsnlavne dcelkildfg larhtddemt
      181 gyvatrwyra peimlnwmhy nqtvdiwsvg cimaelltgr tlfpgtdhin qlqqimrltg
      241 tppaylinrm pshearnyiq slaqmpkmnf anvfiganpl avdllekmlv ldsdkritaa
      301 qalahayfaq yhdpddepva dpydqsfesr dllidewksl tydevisfvp ppldqeemes
//
LOCUS       NP_001380788             375 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 6 [Rattus norvegicus].
ACCESSION   NP_001380788 XP_017446270
VERSION     NP_001380788.1
DBSOURCE    REFSEQ: accession NM_001393859.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yan,W.W., Liang,Y.L., Zhang,Q.X., Wang,D., Lei,M.Z., Qu,J.,
            He,X.H., Lei,Q.Y. and Wang,Y.P.
  TITLE     Arginine methylation of SIRT7 couples glucose sensing with
            mitochondria biogenesis
  JOURNAL   EMBO Rep 19 (12) (2018)
   PUBMED   30420520
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Huang,J., Cardamone,M.D., Johnson,H.E., Neault,M., Chan,M.,
            Floyd,Z.E., Mallette,F.A. and Perissi,V.
  TITLE     Exchange Factor TBL1 and Arginine Methyltransferase PRMT6 Cooperate
            in Protecting G Protein Pathway Suppressor 2 (GPS2) from
            Proteasomal Degradation
  JOURNAL   J Biol Chem 290 (31), 19044-19054 (2015)
   PUBMED   26070566
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Casadio,F., Lu,X., Pollock,S.B., LeRoy,G., Garcia,B.A., Muir,T.W.,
            Roeder,R.G. and Allis,C.D.
  TITLE     H3R42me2a is a histone modification with positive transcriptional
            effects
  JOURNAL   Proc Natl Acad Sci U S A 110 (37), 14894-14899 (2013)
   PUBMED   23980157
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Neault,M., Mallette,F.A., Vogel,G., Michaud-Levesque,J. and
            Richard,S.
  TITLE     Ablation of PRMT6 reveals a role as a negative transcriptional
            regulator of the p53 tumor suppressor
  JOURNAL   Nucleic Acids Res 40 (19), 9513-9521 (2012)
   PUBMED   22904064
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Guccione,E., Bassi,C., Casadio,F., Martinato,F., Cesaroni,M.,
            Schuchlautz,H., Luscher,B. and Amati,B.
  TITLE     Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are
            mutually exclusive
  JOURNAL   Nature 449 (7164), 933-937 (2007)
   PUBMED   17898714
REFERENCE   7  (residues 1 to 375)
  AUTHORS   El-Andaloussi,N., Valovka,T., Toueille,M., Steinacher,R., Focke,F.,
            Gehrig,P., Covic,M., Hassa,P.O., Schar,P., Hubscher,U. and
            Hottiger,M.O.
  TITLE     Arginine methylation regulates DNA polymerase beta
  JOURNAL   Mol Cell 22 (1), 51-62 (2006)
   PUBMED   16600869
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Miranda,T.B., Webb,K.J., Edberg,D.D., Reeves,R. and Clarke,S.
  TITLE     Protein arginine methyltransferase 6 specifically methylates the
            nonhistone chromatin protein HMGA1a
  JOURNAL   Biochem Biophys Res Commun 336 (3), 831-835 (2005)
   PUBMED   16157300
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Bedford,M.T. and Richard,S.
  TITLE     Arginine methylation an emerging regulator of protein function
  JOURNAL   Mol Cell 18 (3), 263-272 (2005)
   PUBMED   15866169
  REMARK    Review article
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Frankel,A., Yadav,N., Lee,J., Branscombe,T.L., Clarke,S. and
            Bedford,M.T.
  TITLE     The novel human protein arginine N-methyltransferase PRMT6 is a
            nuclear enzyme displaying unique substrate specificity
  JOURNAL   J Biol Chem 277 (5), 3537-3543 (2002)
   PUBMED   11724789
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Mar 19, 2021 this sequence version replaced XP_017446270.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.9256.1,
                                           SRR26360190.1237519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q41"
     Protein         1..375
                     /product="protein arginine N-methyltransferase 6"
                     /EC_number="2.1.1.125"
                     /note="HMT1 hnRNP methyltransferase-like 6"
                     /calculated_mol_wt=41618
     Region          51..>228
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..375
                     /gene="Prmt6"
                     /gene_synonym="Hrmt1l6"
                     /coded_by="NM_001393859.1:20..1147"
                     /db_xref="GeneID:295384"
                     /db_xref="RGD:1304701"
ORIGIN      
        1 mslskkrkle sgvggaggeg aeeenggeqe aapprprrtk rerdqlyyec ysdvsvheem
       61 iadrvrtday rlgilrnwaa lrgktvldvg agtgilsifc aqagarrvya veasaiwqqa
      121 qevvrlngle drvhilpgpv etvelpeqvd aivsewmgyg llhesmlssv lhartkwlke
      181 gglllpdsae lfvapisdqm lewrlgfwsq vkqhygvdms cmesfatrcl mghseivvqg
      241 lsgedvlarp qrfaqlelar agleqeleag vggrfrcscy gsaplhgfai wfqvtfpggd
      301 sekplvlsts pfhpathwkq allylnepvp veqdtdisge itllpsrdnp rrlrvllryk
      361 vgdheektkd famed
//
LOCUS       NP_001093969             795 aa            linear   ROD 15-APR-2025
DEFINITION  plakophilin-2 [Rattus norvegicus].
ACCESSION   NP_001093969 XP_001065241 XP_213560
VERSION     NP_001093969.1
DBSOURCE    REFSEQ: accession NM_001100499.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   de Paiva Lima,C., da Silva E Silva,D.A., Damasceno,S.,
            Ribeiro,A.F., Rocha,C.S., Berenguer de Matos,A.H., Correia,D.,
            Boerngen-Lacerda,R. and Brunialti Godard,A.L.
  TITLE     Loss of control over the ethanol consumption: differential
            transcriptional regulation in prefrontal cortex
  JOURNAL   J Neurogenet 31 (3), 170-177 (2017)
   PUBMED   28714806
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Moncayo-Arlandi,J., Guasch,E., Sanz-de la Garza,M., Casado,M.,
            Garcia,N.A., Mont,L., Sitges,M., Knoll,R., Buyandelger,B.,
            Campuzano,O., Diez-Juan,A. and Brugada,R.
  TITLE     Molecular disturbance underlies to arrhythmogenic cardiomyopathy
            induced by transgene content, age and exercise in a truncated PKP2
            mouse model
  JOURNAL   Hum Mol Genet 25 (17), 3676-3688 (2016)
   PUBMED   27412010
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Dubash,A.D., Kam,C.Y., Aguado,B.A., Patel,D.M., Delmar,M.,
            Shea,L.D. and Green,K.J.
  TITLE     Plakophilin-2 loss promotes TGF-beta1/p38 MAPK-dependent fibrotic
            gene expression in cardiomyocytes
  JOURNAL   J Cell Biol 212 (4), 425-438 (2016)
   PUBMED   26858265
  REMARK    GeneRIF: Plakophilin-2 loss promotes TGF-beta1/p38 MAPK-dependent
            fibrotic gene expression in cardiomyocytes.
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Fischer-Keso,R., Breuninger,S., Hofmann,S., Henn,M., Rohrig,T.,
            Strobel,P., Stoecklin,G. and Hofmann,I.
  TITLE     Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA
            stability of desmosomal proteins
  JOURNAL   Mol Cell Biol 34 (23), 4244-4256 (2014)
   PUBMED   25225333
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Franke,W.W., Borrmann,C.M., Grund,C. and Pieperhoff,S.
  TITLE     The area composita of adhering junctions connecting heart muscle
            cells of vertebrates. I. Molecular definition in intercalated disks
            of cardiomyocytes by immunoelectron microscopy of desmosomal
            proteins
  JOURNAL   Eur J Cell Biol 85 (2), 69-82 (2006)
   PUBMED   16406610
  REMARK    Erratum:[Eur J Cell Biol. 2006 Jun;85(6):577.]
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Gerull,B., Heuser,A., Wichter,T., Paul,M., Basson,C.T.,
            McDermott,D.A., Lerman,B.B., Markowitz,S.M., Ellinor,P.T.,
            MacRae,C.A., Peters,S., Grossmann,K.S., Drenckhahn,J., Michely,B.,
            Sasse-Klaassen,S., Birchmeier,W., Dietz,R., Breithardt,G.,
            Schulze-Bahr,E. and Thierfelder,L.
  TITLE     Mutations in the desmosomal protein plakophilin-2 are common in
            arrhythmogenic right ventricular cardiomyopathy
  JOURNAL   Nat Genet 36 (11), 1162-1164 (2004)
   PUBMED   15489853
  REMARK    Erratum:[Nat Genet. 2005 Jan;37(1):106]
REFERENCE   8  (residues 1 to 795)
  AUTHORS   Grossmann,K.S., Grund,C., Huelsken,J., Behrend,M., Erdmann,B.,
            Franke,W.W. and Birchmeier,W.
  TITLE     Requirement of plakophilin 2 for heart morphogenesis and cardiac
            junction formation
  JOURNAL   J Cell Biol 167 (1), 149-160 (2004)
   PUBMED   15479741
REFERENCE   9  (residues 1 to 795)
  AUTHORS   Hofmann,I., Mertens,C., Brettel,M., Nimmrich,V., Schnolzer,M. and
            Herrmann,H.
  TITLE     Interaction of plakophilins with desmoplakin and intermediate
            filament proteins: an in vitro analysis
  JOURNAL   J Cell Sci 113 (Pt 13), 2471-2483 (2000)
   PUBMED   10852826
REFERENCE   10 (residues 1 to 795)
  AUTHORS   Gallicano,G.I., Kouklis,P., Bauer,C., Yin,M., Vasioukhin,V.,
            Degenstein,L. and Fuchs,E.
  TITLE     Desmoplakin is required early in development for assembly of
            desmosomes and cytoskeletal linkage
  JOURNAL   J Cell Biol 143 (7), 2009-2022 (1998)
   PUBMED   9864371
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473999.2.
            
            On or before Nov 30, 2008 this sequence version replaced
            XP_001065241.1, XP_213560.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..795
                     /product="plakophilin-2"
                     /calculated_mol_wt=87697
     Region          311..338
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(327,331,337,371,375,379,414,418,422)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          342..382
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          346..382
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          388..423
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          435..479
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          584..625
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          636..670
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          678..716
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..795
                     /gene="Pkp2"
                     /coded_by="NM_001100499.1:38..2425"
                     /db_xref="GeneID:287925"
                     /db_xref="RGD:1306533"
ORIGIN      
        1 maipgslgec gyirtvlgqq ilghldsssl alpsearlrl agssgrgdpv arsqriqeqv
       61 qqtlarrgrs svvggnlhrt ssvpeyvykl hlvendfvgr qspaardydm lkagvtatyg
      121 srwgrgtaqy ssqksveers wrqplrrlei spdssperah yghseyqyaw rshvvpggrl
      181 tlpryarsei lglrqtgtar rapgcgsvsd avfdngplnp tipthppgts hsagslleet
      241 tvrvsqarfq glqsragrss wprssvhstl resgrmlpta gqaavgsgda hrdrsafads
      301 qlgnadlemt leravnmlda dhvplskisa aatfiqhesf qksearkrvn qlqgipkllq
      361 llkvqnedvq ravcgalrnl vfedndnkle vaelngvprl lqvlkqtrdl etkkqitgll
      421 wnlsssdklk hlmiteallt ltesviipfs gwpegdypka nglldfdify nvtgclrnms
      481 sagpdgrkvm rrcdglidsl vhyvrgtiad yqpddkaten cvcilhnlsy qleaelpeky
      541 sqsiymqnrn iqtnsnksig cfgsrsrkvk eqyqdtpmpe erssprgiew lwhsivirmy
      601 lsliakssrn ytqeaslgal qnltagsgpi ptsvarmvvq kenglqhtrk mlhvgdpsvk
      661 ktavsllrnl srnlslqnei aketlpdlvs iipdtvpstd lliettasac ytlnnlmqns
      721 yqnardllnt gglqkimtis igegyapnka skaasvllys lwahtelhna ykkaqfkktd
      781 fvnsrtakas hslkd
//
LOCUS       NP_001178525             366 aa            linear   ROD 15-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 46 [Rattus norvegicus].
ACCESSION   NP_001178525 XP_214034
VERSION     NP_001178525.1
DBSOURCE    REFSEQ: accession NM_001191596.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Jahan,A.S., Lestra,M., Swee,L.K., Fan,Y., Lamers,M.M.,
            Tafesse,F.G., Theile,C.S., Spooner,E., Bruzzone,R., Ploegh,H.L. and
            Sanyal,S.
  TITLE     Usp12 stabilizes the T-cell receptor complex at the cell surface
            during signaling
  JOURNAL   Proc Natl Acad Sci U S A 113 (6), E705-E714 (2016)
   PUBMED   26811477
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Huo,Y., Khatri,N., Hou,Q., Gilbert,J., Wang,G. and Man,H.Y.
  TITLE     The deubiquitinating enzyme USP46 regulates AMPA receptor
            ubiquitination and trafficking
  JOURNAL   J Neurochem 134 (6), 1067-1080 (2015)
   PUBMED   26077708
  REMARK    GeneRIF: USP46-mediated regulation of
            Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor
            ubiquitination and turnover may play an important role in synaptic
            plasticity and brain function.
            Erratum:[J Neurochem. 2017 May;141(3):472. doi: 10.1111/jnc.14023.
            PMID: 28417468]
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Imai,S., Kano,M., Nonoyama,K. and Ebihara,S.
  TITLE     Behavioral characteristics of ubiquitin-specific peptidase
            46-deficient mice
  JOURNAL   PLoS One 8 (3), e58566 (2013)
   PUBMED   23472206
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Imai,S., Mamiya,T., Tsukada,A., Sakai,Y., Mouri,A., Nabeshima,T.
            and Ebihara,S.
  TITLE     Ubiquitin-specific peptidase 46 (Usp46) regulates mouse immobile
            behavior in the tail suspension test through the GABAergic system
  JOURNAL   PLoS One 7 (6), e39084 (2012)
   PUBMED   22720038
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Zhang,W., Tian,Q.B., Li,Q.K., Wang,J.M., Wang,C.N., Liu,T.,
            Liu,D.W. and Wang,M.W.
  TITLE     Lysine 92 amino acid residue of USP46, a gene associated with
            'behavioral despair' in mice, influences the deubiquitinating
            enzyme activity
  JOURNAL   PLoS One 6 (10), e26297 (2011)
   PUBMED   22043315
  REMARK    GeneRIF: results suggest that the Lys 92 deletion of USP46 could
            influence enzyme activity and thereby provide a molecular clue how
            the enzyme regulating the pathogenesis of mental illnesses.
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Tomida,S., Mamiya,T., Sakamaki,H., Miura,M., Aosaki,T., Masuda,M.,
            Niwa,M., Kameyama,T., Kobayashi,J., Iwaki,Y., Imai,S., Ishikawa,A.,
            Abe,K., Yoshimura,T., Nabeshima,T. and Ebihara,S.
  TITLE     Usp46 is a quantitative trait gene regulating mouse immobile
            behavior in the tail suspension and forced swimming tests
  JOURNAL   Nat Genet 41 (6), 688-695 (2009)
   PUBMED   19465912
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jul 17, 2010 this sequence version replaced XP_214034.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211578.1, SRR26643429.46605.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..366
                     /product="ubiquitin carboxyl-terminal hydrolase 46"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 46; ubiquitin
                     thioesterase 46; deubiquitinating enzyme 46;
                     ubiquitin-specific-processing protease 46"
                     /calculated_mol_wt=42284
     Region          36..363
                     /region_name="Peptidase_C19G"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02663"
                     /db_xref="CDD:239128"
     Site            order(39,44,313,329)
                     /site_type="active"
                     /db_xref="CDD:239128"
     CDS             1..366
                     /gene="Usp46"
                     /gene_synonym="RGD1564808"
                     /coded_by="NM_001191596.1:77..1177"
                     /db_xref="GeneID:289584"
                     /db_xref="RGD:1564808"
ORIGIN      
        1 mtvrniasic nmgtnasale kdigpeqfpi nehyfglvnf gntcycnsvl qalyfcrpfr
       61 envlaykaqq kkkenlltcl adlfhsiatq kkkvgvippk kfisrlrken dlfdnymqqd
      121 aheflnylln tiadilqeek kqekqngklk ngnmnepaen skpeltwvhe ifqgtltnet
      181 rclncetvss kdedfldlsv dveqntsith clrdfsntet lcseqkyyce tccskqeaqk
      241 rmrvkklpmi lalhlkrfky meqlhrytkl syrvvfplel rlfntssdav nldrmydlva
      301 vvvhcgsgpn rghyitivks hgfwllfddd ivekidaqai eefygltsdi sknsesgyil
      361 fyqsre
//
LOCUS       NP_001258314             394 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 8 [Rattus norvegicus].
ACCESSION   NP_001258314 XP_001071456 XP_002726479
VERSION     NP_001258314.1
DBSOURCE    REFSEQ: accession NM_001271385.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Zou,Z., Liu,R., Wang,Y., Tan,H., An,G., Zhang,B., Wang,Y. and
            Dong,D.
  TITLE     Protein arginine methyltransferase 8 regulates ferroptosis and
            macrophage polarization in spinal cord injury via glial
            cell-derived neurotrophic factor
  JOURNAL   CNS Neurosci Ther 29 (8), 2145-2161 (2023)
   PUBMED   36914965
  REMARK    GeneRIF: Protein arginine methyltransferase 8 regulates ferroptosis
            and macrophage polarization in spinal cord injury via glial
            cell-derived neurotrophic factor.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Lo,L.H., Dong,R., Lyu,Q. and Lai,K.O.
  TITLE     The Protein Arginine Methyltransferase PRMT8 and Substrate G3BP1
            Control Rac1-PAK1 Signaling and Actin Cytoskeleton for Dendritic
            Spine Maturation
  JOURNAL   Cell Rep 31 (10), 107744 (2020)
   PUBMED   32521269
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Toma-Fukai,S., Kim,J.D., Park,K.E., Kuwabara,N., Shimizu,N.,
            Krayukhina,E., Uchiyama,S., Fukamizu,A. and Shimizu,T.
  TITLE     Novel helical assembly in arginine methyltransferase 8
  JOURNAL   J Mol Biol 428 (6), 1197-1208 (2016)
   PUBMED   26876602
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Pahlich,S., Zakaryan,R.P. and Gehring,H.
  TITLE     Identification of proteins interacting with protein arginine
            methyltransferase 8: the Ewing sarcoma (EWS) protein binds
            independent of its methylation state
  JOURNAL   Proteins 72 (4), 1125-1137 (2008)
   PUBMED   18320585
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Sayegh,J., Webb,K., Cheng,D., Bedford,M.T. and Clarke,S.G.
  TITLE     Regulation of protein arginine methyltransferase 8 (PRMT8) activity
            by its N-terminal domain
  JOURNAL   J Biol Chem 282 (50), 36444-36453 (2007)
   PUBMED   17925405
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Lee,J., Sayegh,J., Daniel,J., Clarke,S. and Bedford,M.T.
  TITLE     PRMT8, a new membrane-bound tissue-specific member of the protein
            arginine methyltransferase family
  JOURNAL   J Biol Chem 280 (38), 32890-32896 (2005)
   PUBMED   16051612
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Sep 21, 2012 this sequence version replaced
            XP_001071456.3, XP_002726479.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2249953.1,
                                           SRR22399492.871561.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..394
                     /product="protein arginine N-methyltransferase 8"
                     /EC_number="2.1.1.319"
                     /calculated_mol_wt=45145
     Region          86..>259
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..394
                     /gene="Prmt8"
                     /coded_by="NM_001271385.1:1..1185"
                     /db_xref="GeneID:688502"
                     /db_xref="RGD:1587677"
ORIGIN      
        1 mgmkhssrcl llrrkmaena vestevssap pqppqpvipa kpvqcvhhvs tqpscpgrgk
       61 mskllnpeem tsrdyyfdsy ahfgiheeml kdevrtltyr nsmyhnkhvf kdkvvldvgs
      121 gtgilsmfaa kagakkvfgi ecssisdyse kiikanhldn vitifkgkve evelpvekvd
      181 iiisewmgyc lfyesmlntv ifardkwlkp gglmfpdraa lyvvaiedrq ykdfkihwwe
      241 nvygfdmtci rdvamkeplv divdpkqvvt naclikevdi ytvkteelsf tsafclqiqr
      301 ndyvhalvty fnieftkchk kmgfstapda pythwkqtvf yledyltvrr geeiygtism
      361 kpnaknvrdl dftvdldfkg qlcetsvsnd ykmr
//
LOCUS       NP_001380669            1216 aa            linear   ROD 15-APR-2025
DEFINITION  SRC kinase signaling inhibitor 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001380669
VERSION     NP_001380669.1
DBSOURCE    REFSEQ: accession NM_001393740.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Calipari,E.S., Godino,A., Salery,M., Damez-Werno,D.M., Cahill,M.E.,
            Werner,C.T., Gancarz,A.M., Peck,E.G., Jlayer,Z., Rabkin,J.,
            Landry,J.A., Smith,A.C.W., Defilippi,P., Kenny,P.J., Hurd,Y.L.,
            Neve,R.L., Dietz,D.M. and Nestler,E.J.
  TITLE     Synaptic Microtubule-Associated Protein EB3 and SRC Phosphorylation
            Mediate Structural and Behavioral Adaptations During Withdrawal
            From Cocaine Self-Administration
  JOURNAL   J Neurosci 39 (29), 5634-5646 (2019)
   PUBMED   31092585
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Wang,W., Zhu,X., Du,X., Xu,A., Yuan,X., Zhan,Y., Liu,M. and Wang,S.
  TITLE     MiR-150 promotes angiogensis and proliferation of endothelial
            progenitor cells in deep venous thrombosis by targeting SRCIN1
  JOURNAL   Microvasc Res 123, 35-41 (2019)
   PUBMED   30315850
  REMARK    GeneRIF: Upregulation of miR-150 promoted angiogenesis and
            proliferation of endothelial progenitor cells by targeting SRCIN1
            in vitro and thrombus resolution in vivo.
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Li,M.Y., Miao,W.Y., Wu,Q.Z., He,S.J., Yan,G., Yang,Y., Liu,J.J.,
            Taketo,M.M. and Yu,X.
  TITLE     A Critical Role of Presynaptic Cadherin/Catenin/p140Cap Complexes
            in Stabilizing Spines and Functional Synapses in the Neocortex
  JOURNAL   Neuron 94 (6), 1155-1172 (2017)
   PUBMED   28641114
  REMARK    GeneRIF: Study demonstrates a critical role of presynaptic
            cadherin/catenin/p140Cap cell adhesion complexes in stabilizing
            functional synapses and spines in the developing neocortex.
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Repetto,D., Camera,P., Melani,R., Morello,N., Russo,I.,
            Calcagno,E., Tomasoni,R., Bianchi,F., Berto,G., Giustetto,M.,
            Berardi,N., Pizzorusso,T., Matteoli,M., Di Stefano,P., Missler,M.,
            Turco,E., Di Cunto,F. and Defilippi,P.
  TITLE     p140Cap regulates memory and synaptic plasticity through
            Src-mediated and citron-N-mediated actin reorganization
  JOURNAL   J Neurosci 34 (4), 1542-1553 (2014)
   PUBMED   24453341
  REMARK    GeneRIF: we here demonstrate that p140Cap is a key element for both
            learning and synaptic plasticity
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Di Stefano,P., Damiano,L., Cabodi,S., Aramu,S., Tordella,L.,
            Praduroux,A., Piva,R., Cavallo,F., Forni,G., Silengo,L., Tarone,G.,
            Turco,E. and Defilippi,P.
  TITLE     p140Cap protein suppresses tumour cell properties, regulating Csk
            and Src kinase activity
  JOURNAL   EMBO J 26 (12), 2843-2855 (2007)
   PUBMED   17525734
REFERENCE   7  (residues 1 to 1216)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 1216)
  AUTHORS   Di Stefano,P., Cabodi,S., Boeri Erba,E., Margaria,V., Bergatto,E.,
            Giuffrida,M.G., Silengo,L., Tarone,G., Turco,E. and Defilippi,P.
  TITLE     P130Cas-associated protein (p140Cap) as a new
            tyrosine-phosphorylated protein involved in cell spreading
  JOURNAL   Mol Biol Cell 15 (2), 787-800 (2004)
   PUBMED   14657239
REFERENCE   9  (residues 1 to 1216)
  AUTHORS   Singh,D. and Lampe,P.D.
  TITLE     Identification of connexin-43 interacting proteins
  JOURNAL   Cell Commun Adhes 10 (4-6), 215-220 (2003)
   PUBMED   14681019
REFERENCE   10 (residues 1 to 1216)
  AUTHORS   Chin,L.S., Nugent,R.D., Raynor,M.C., Vavalle,J.P. and Li,L.
  TITLE     SNIP, a novel SNAP-25-interacting protein implicated in regulated
            exocytosis
  JOURNAL   J Biol Chem 275 (2), 1191-1200 (2000)
   PUBMED   10625663
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1216
                     /product="SRC kinase signaling inhibitor 1 isoform 1"
                     /note="p130Cas-associated protein; SNAP25-interacting
                     protein"
                     /calculated_mol_wt=130618
     Region          218..>297
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     Region          <719..873
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..1216
                     /gene="Srcin1"
                     /gene_synonym="P140; p140Cap; Snip"
                     /coded_by="NM_001393740.2:138..3788"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:56029"
                     /db_xref="RGD:708439"
ORIGIN      
        1 mgnapsqdpe rssppmlsad daeypreyrt lggggsggsg grrfsnvglv htserrhtvi
       61 aaqslealsg lqkadadrkr dafmdhlksk ypqhalalrg qqdrmreqvg gwtvdpvcll
      121 sslcshlhgd stpsgagqpa qqpnywsfkt rssrhtqgaq pgladqaakl syasaeslet
      181 mseaelplgf srmnrfrqsl plsrsasqtk lrspgvlflq fgeetrrvhi thevssldtl
      241 haliahmfpq kltmgmlksp ntailikdea rnvfyeledv rdiqdrsiik iyrkeplyaa
      301 fpgshltngd lrremvyasr essptrrlnn lspashlass spppglpsgl psglpsgsps
      361 rsrlsyaggr ppsyagspvh haaerlggap tsqgvspsps ailerrdvkp dedlagkagg
      421 mvlvkgegly adpygllheg rlslaaaagd pfaypgaggl ykrgsvrsls tysaaalqsd
      481 ledslykaga ggplygdgyg frlppsspqk ladvsapsgg pppphspysg ppsrgspvrq
      541 sfrkdsgsss vfaespggka rstgastaga ppselfpgpg erslvgfgpp vpakdtetre
      601 rmeamekqia sltglvqsal lrgsepetps ekiegsngaa tpsapvcgsg srssgatpvs
      661 gppppavsst pagqptavsr lqmqmhlrgl qnsasdlrgq lqqlrklqlq nqesvrallk
      721 rteaelsmrv seaarrqedp lqrqrtlvee erlrylndee litqqlndle ksvekiqrdv
      781 ahnhrlvpgp eleekalvlk qlgetltelk ahfpglqskm rvvlrvevea vkflkeepqr
      841 ldgllkrcrv vtdtlaqirr qvdegvwppp nnllnqspkk vaaetdfskg ldfeipppsp
      901 plnlhelsgp aegtpltpks gnptkgldap skrnmdkavs veaaerdwee kraaltqysa
      961 kdinrlleet qaellkaipd ldcaskthpg ptptpdhkpp kaphgqkaap rtepsgrrgs
     1021 deltvpryrt ekpskspppp pprrsfpssh gltttrtgev vvtskkdsvf ikkaeseele
     1081 iqkpqvklrr avsevvrpas tppimasaik deddeeriia elesgggsvp pmkvvtpgas
     1141 rlkaaqgpag spdkgkhgkq rteymriqaq qqatkpskem sgpnetsspv sekpsgsrts
     1201 ipvltsfgar nssisf
//
LOCUS       NP_001414204            3006 aa            linear   ROD 15-APR-2025
DEFINITION  protein furry homolog-like [Rattus norvegicus].
ACCESSION   NP_001414204
VERSION     NP_001414204.1
DBSOURCE    REFSEQ: accession NM_001427275.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3006)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   2  (residues 1 to 3006)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3006
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..3006
                     /product="protein furry homolog-like"
                     /note="FRY-like"
                     /calculated_mol_wt=337238
     Region          117..649
                     /region_name="MOR2-PAG1_N"
                     /note="Cell morphogenesis N-terminal; pfam14222"
                     /db_xref="CDD:464107"
     Region          687..1859
                     /region_name="MOR2-PAG1_mid"
                     /note="Cell morphogenesis central region; pfam14228"
                     /db_xref="CDD:433790"
     Region          2001..2254
                     /region_name="MOR2-PAG1_C"
                     /note="Cell morphogenesis C-terminal; pfam14225"
                     /db_xref="CDD:464109"
     Region          2284..3006
                     /region_name="Fry_C"
                     /note="Furry protein C-terminal; pfam19421"
                     /db_xref="CDD:466072"
     CDS             1..3006
                     /gene="Fryl"
                     /gene_synonym="RGD1311309"
                     /coded_by="NM_001427275.1:616..9636"
                     /db_xref="GeneID:364144"
                     /db_xref="RGD:1311309"
ORIGIN      
        1 msnitidpdv kpgeyviksl faefavqaek kievvmaepl ekllsrslqr gedlqfdqli
       61 ssmssvaehc lpsllrtlfd wyrrqngtdd esygyrprss tkskgdeqhr erdyllerrd
      121 lavdfifclv lvevlkqipv hpvpdplvhe vlnlafkhfk hkegysgtnt gnvhiiadly
      181 aevigvlaqs kfqavrkkfv telkelrqke qsphvvqsii slimgmkffr vmmypvedfe
      241 asfqfmqeca qyflevkdkd ikhalaglfv eilipvaaav knevnvpclk nfvemlyqtt
      301 felssrkkhs lalyplitcl lcvsqkqffl nnwhiflqnc lshlknkdpk msrvalesly
      361 rllwvyviri kcesntvtqs rlmsivsalf pkgsrsvvpr dtplnifvki iqfiaqerld
      421 famkeiifdl lsvgksaktf tinpermnig lrvflviads lqqkdgdppm pttgvilpsg
      481 ntlrvkkifl nktltdeeak vigmsvyypq vrraldsilr hldkevgrpm cmtsvqmsnk
      541 epedmitger kpkidlfrtc iaaiprlipd gmsrtdliel larltihmde elralafntl
      601 qalmldfpdw redvlsgfvy fivrevtdvh ptlldnavkm lvqlinqwkq aaqmynrtqd
      661 sqqsisnggp hppplersly stvfhvvegf alvilcssrp atrrlavsvl reiralfall
      721 evpkgdeela idvmdrlsps ilesfihltg adqttllycp ssvdlqtlad wnsspishqf
      781 dvispshiwi fahvtqgqdp wiislssflk qenlpkhcst avsyawmfay trlqllspqv
      841 dinspinakk vstttssdsy vglwrnylil ccsaaaspsp sapagsvrcs ppetlastpd
      901 sgysidskiv gipspsslfk hivpmmrses meiteslvlg lgrtnpgafr elieelhpii
      961 kealerrpen mkrrrrrdil rvqlvrifel ladagvishs asggldneth flnntlleyv
     1021 dltrqlleae nekdsdtlkd irchfsalva niiqnvpvhq rrsifpqqsl rhslfmlfsh
     1081 wagpfsimft pldrysdrnm qinrhqycal kamsavlccg pvadnvglss dgylykwldn
     1141 ildsldkkvh qlgceavtll lelnpdqssl mywavdrcyt gsrrvaagcf raianvfqnr
     1201 dyqcdtvmll nlilfkaads srsiyevamq llqilepkmf ryahklevqr tdgvlsqlsp
     1261 lphlysvsyy qlseelaray peltlaifse isqriqtahp agrqamlhyl lpwmnnielv
     1321 dvrplpsgrr qdeedgslkd relmvtsrrw lrgegwgspq atamvlnnlm ymtakygdel
     1381 awsevenvwt tladgwpknl kiilhflisi cgvnsepsll pyvkkvivyl grdktmqlle
     1441 elvselqltd pvssgvthmd nppyyritsg ckipsvtsgt tsssntmvap tdgnpdskal
     1501 kenfeesfvh ldiygglnsh lnrqhhrles ryssssggsy eeeksdsmpl ysnwrlkvme
     1561 hnqgeplpfp paggcwsplv dyvpetaspg lplhrcsiav illtdliidh svkvewgsyl
     1621 hlllhavfig fdhchpevye hckrlllhll ivmgpnsnir tvasvllrnk efneprvltv
     1681 kptahsdytf tagindftpd yqpspmtdsg lsssstsssi slgnnsaais hlqatllgev
     1741 dlsveqdgkv ktlmefitsr krgplwnhed vssknpsiks adqlttflkh vvsvfkqsna
     1801 egihlerhls evalqtalsc ssrhyagrsf qifralkqpl santlsdvls rlvetvgdpg
     1861 edaqgfviel lltlesaidt laetmkhydl lsalsqtsyh dpvmgnkyaa nrkstgqlnl
     1921 stspinsssh lgcngdtrsn slrlslvgdr rgdrrrsntl ditdgrtnhg gslvrtrsls
     1981 slrekgvydt qpptepgnlm atifwiatsl lesdyeyeyl lalrllskll thlpldkses
     2041 rekiesvqsk lkwsnfpglq qlflkgftsv stqemtvyll sqlisvskht lvdpsqlsgf
     2101 plnilcllph liqhfdnptq fcketasria kvcaeekcpt lvnlahmmsl ysthtysrdc
     2161 anwinvvcry lhdsfseatf slvtylaell ekglasmqqs llqiiyslls hvdlsaapak
     2221 qfnleitkti gkyvqspywk ealnilklvv srsaslvvpn dipkaygvdv gspeisfaki
     2281 fnnvskelpg ktldfhfdis etpiignkyg gqhsaagrng kakviavtrs tsstssgsts
     2341 nalvpvswkr pqlsqrrtre klmsvlslcg pesglpknps vifssnedle vgdqqtslis
     2401 ttediiqeee vavedssseq qfgvfkdfdf ldveledaeg esmdnfnwgv rrrsldsidk
     2461 gdtpslqecp cssstpsltl tnqedtdess eeeaaltasq ilsrtqmlns dcvpddlmpd
     2521 hqdllqsqds assnttedvl qirdetpsle acldnascql pedtssvlke ehvtafedeg
     2581 pyliqdqqdp lvcrgildle etdmpeplap esypesvcee dvtlalkeld erceeeeadf
     2641 sglssqeede qdgfpevqts plptpflsai iaafqpmaye deeeawrchv nqtlsdtdgs
     2701 cavftfhvfs rlfqtiqrkf geitneavgf lgkslqrigt kfksslevmm tcsecptvfv
     2761 daetlmacgl letlkfgvle lqehldtytt kreaaeqwld nckrtfgane didrintnah
     2821 elelcrrlyr lhfqllllfq aycklinqvn aikneaevin mseeltqleg ilkeaeaase
     2881 neetdiskaa qttietaihs lietlknkef vsavaqvkaf rtlwpsdifg scdddpvqtl
     2941 lhiyfhhqtl gqtgsfavig snldmseanc klmelnleir eslrmvqshp llaqakpvgk
     3001 tasagf
//
LOCUS       NP_001414152            1284 aa            linear   ROD 15-APR-2025
DEFINITION  cordon-bleu protein-like 1 [Rattus norvegicus].
ACCESSION   NP_001414152
VERSION     NP_001414152.1
DBSOURCE    REFSEQ: accession NM_001427223.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1284)
  AUTHORS   Xiong,X., Liu,J., He,Q., Dai,R., Zhang,H., Cao,Z., Liao,Y., Liu,B.,
            Zhou,Y., Chen,J., Liu,J. and Chen,M.
  TITLE     Long non-coding RNA NORAD aggravates acute myocardial infarction by
            promoting fibrosis and apoptosis via miR-577/COBLL1 axis
  JOURNAL   Environ Toxicol 36 (11), 2256-2265 (2021)
   PUBMED   34355838
  REMARK    GeneRIF: Long non-coding RNA NORAD aggravates acute myocardial
            infarction by promoting fibrosis and apoptosis via miR-577/COBLL1
            axis.
REFERENCE   2  (residues 1 to 1284)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   3  (residues 1 to 1284)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1284)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.11268.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1284
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..1284
                     /product="cordon-bleu protein-like 1"
                     /note="Cobl-like 1"
                     /calculated_mol_wt=136967
     Region          72..138
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Region          156..234
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          <867..1142
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1233..1258
                     /region_name="WH2"
                     /note="Wiskott-Aldrich Syndrome Homology (WASP) region 2
                     (WH2 motif), and similar proteins; cl41728"
                     /db_xref="CDD:425359"
     Site            order(1237..1238,1240..1242,1244..1246,1254..1257)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409196"
     CDS             1..1284
                     /gene="Cobll1"
                     /coded_by="NM_001427223.1:165..4019"
                     /db_xref="GeneID:311088"
                     /db_xref="RGD:1308954"
ORIGIN      
        1 mdrsardpvp rsaprtpatq sagsagrktk akaplppaem kgmdvssaed pvesipvste
       61 qhdnmidkdi elsvvlpgdv lksttvhgsk pmmdllvflc aqyhlnpssh tinllsaeen
      121 likfkpntpi gmlevekvil kpksldkkkp tpiipektvr vvinfkktqk tivrvsphsp
      181 lqdlapiics kcefdplhtv llkdyqaqep ldltkslndl glrelyamdi srescqishn
      241 pdivkekenk gifsffqrsk kkreqtasap atplvskhrp sftrsntisk pyisntlpsd
      301 apkkrraplp pmptsqgaaq gqerrascve rstsvddtdk sssegfmvrt gslqlsgsts
      361 vgtsslkrtk rkapappskp sltetdegss aaahglpled givpdsisev sspegmsspe
      421 gpgflsqeec svpkpmdeis egpgtpeaav asmtsgvssd ysleeideke elmeaskdqa
      481 gsvksptias astdmiitae ndpdsalsis dgetspgskg ntpegrnpeg qgphhpvecl
      541 ignennvsds ikdlktlspn qesviqnevv vcatstdyvk nrpremeati egeaqkkvgd
      601 veaerlsgsp agrmddvqss renhltaspg pdqksnqprv ektkmqdaai qatpacstfd
      661 gnheahnspd lrvdetaqtl gsststqhss asfqdsvnas revrsqgtst yvqdrlpvke
      721 aactygnnda lspidgsgkn paasslknfp lyrqdnhpkp kpsneitrey ipkigmttyk
      781 ivppkslevv kdwdseaagk kdnqktlava qkhaietmte tavqaealvt sknsqqpqpd
      841 rtpkpssgte hplhrtvssp vgtemnppkp prmttdtgti pfapnledin nileskfrsr
      901 asnpqakpss fflqmqkras ghyvtsaaak svhtapgptp keptikevqr dpqlppeqcl
      961 splserthsa plpniskadd nriqkpaets pppvapkpma lpaetsppav apkpmafpae
     1021 tslppvspkp malpteasss pispkpmapp aeasippvvp kpmappaeas plpvapkpma
     1081 fpaetslppv apkpmalpte aspppvapkp lalpgsqgas lnlktlktfg aprpynssap
     1141 spfalavvkr sqsfskaspe spsedssaqp paaiqdgktq tvnqptvgsq hdgvdkqnkp
     1201 vqnehssqrl tpadgpssft lqrqsslnfq ssdpehirqs lltairsgea aaklkrvtvp
     1261 snrisvngks glsqpmsida qdsc
//
LOCUS       NP_001380787             375 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 6 [Rattus norvegicus].
ACCESSION   NP_001380787
VERSION     NP_001380787.1
DBSOURCE    REFSEQ: accession NM_001393858.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yan,W.W., Liang,Y.L., Zhang,Q.X., Wang,D., Lei,M.Z., Qu,J.,
            He,X.H., Lei,Q.Y. and Wang,Y.P.
  TITLE     Arginine methylation of SIRT7 couples glucose sensing with
            mitochondria biogenesis
  JOURNAL   EMBO Rep 19 (12) (2018)
   PUBMED   30420520
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Damez-Werno,D.M., Sun,H., Scobie,K.N., Shao,N., Rabkin,J., Dias,C.,
            Calipari,E.S., Maze,I., Pena,C.J., Walker,D.M., Cahill,M.E.,
            Chandra,R., Gancarz,A., Mouzon,E., Landry,J.A., Cates,H.,
            Lobo,M.K., Dietz,D., Allis,C.D., Guccione,E., Turecki,G.,
            Defilippi,P., Neve,R.L., Hurd,Y.L., Shen,L. and Nestler,E.J.
  TITLE     Histone arginine methylation in cocaine action in the nucleus
            accumbens
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9623-9628 (2016)
   PUBMED   27506785
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Huang,J., Cardamone,M.D., Johnson,H.E., Neault,M., Chan,M.,
            Floyd,Z.E., Mallette,F.A. and Perissi,V.
  TITLE     Exchange Factor TBL1 and Arginine Methyltransferase PRMT6 Cooperate
            in Protecting G Protein Pathway Suppressor 2 (GPS2) from
            Proteasomal Degradation
  JOURNAL   J Biol Chem 290 (31), 19044-19054 (2015)
   PUBMED   26070566
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Casadio,F., Lu,X., Pollock,S.B., LeRoy,G., Garcia,B.A., Muir,T.W.,
            Roeder,R.G. and Allis,C.D.
  TITLE     H3R42me2a is a histone modification with positive transcriptional
            effects
  JOURNAL   Proc Natl Acad Sci U S A 110 (37), 14894-14899 (2013)
   PUBMED   23980157
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Neault,M., Mallette,F.A., Vogel,G., Michaud-Levesque,J. and
            Richard,S.
  TITLE     Ablation of PRMT6 reveals a role as a negative transcriptional
            regulator of the p53 tumor suppressor
  JOURNAL   Nucleic Acids Res 40 (19), 9513-9521 (2012)
   PUBMED   22904064
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Guccione,E., Bassi,C., Casadio,F., Martinato,F., Cesaroni,M.,
            Schuchlautz,H., Luscher,B. and Amati,B.
  TITLE     Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are
            mutually exclusive
  JOURNAL   Nature 449 (7164), 933-937 (2007)
   PUBMED   17898714
REFERENCE   7  (residues 1 to 375)
  AUTHORS   El-Andaloussi,N., Valovka,T., Toueille,M., Steinacher,R., Focke,F.,
            Gehrig,P., Covic,M., Hassa,P.O., Schar,P., Hubscher,U. and
            Hottiger,M.O.
  TITLE     Arginine methylation regulates DNA polymerase beta
  JOURNAL   Mol Cell 22 (1), 51-62 (2006)
   PUBMED   16600869
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Miranda,T.B., Webb,K.J., Edberg,D.D., Reeves,R. and Clarke,S.
  TITLE     Protein arginine methyltransferase 6 specifically methylates the
            nonhistone chromatin protein HMGA1a
  JOURNAL   Biochem Biophys Res Commun 336 (3), 831-835 (2005)
   PUBMED   16157300
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Bedford,M.T. and Richard,S.
  TITLE     Arginine methylation an emerging regulator of protein function
  JOURNAL   Mol Cell 18 (3), 263-272 (2005)
   PUBMED   15866169
  REMARK    Review article
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Frankel,A., Yadav,N., Lee,J., Branscombe,T.L., Clarke,S. and
            Bedford,M.T.
  TITLE     The novel human protein arginine N-methyltransferase PRMT6 is a
            nuclear enzyme displaying unique substrate specificity
  JOURNAL   J Biol Chem 277 (5), 3537-3543 (2002)
   PUBMED   11724789
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26360194.1647668.1,
                                        SRR26360181.3223959.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q41"
     Protein         1..375
                     /product="protein arginine N-methyltransferase 6"
                     /EC_number="2.1.1.125"
                     /note="HMT1 hnRNP methyltransferase-like 6"
                     /calculated_mol_wt=41618
     Region          51..>228
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..375
                     /gene="Prmt6"
                     /gene_synonym="Hrmt1l6"
                     /coded_by="NM_001393858.1:20..1147"
                     /db_xref="GeneID:295384"
                     /db_xref="RGD:1304701"
ORIGIN      
        1 mslskkrkle sgvggaggeg aeeenggeqe aapprprrtk rerdqlyyec ysdvsvheem
       61 iadrvrtday rlgilrnwaa lrgktvldvg agtgilsifc aqagarrvya veasaiwqqa
      121 qevvrlngle drvhilpgpv etvelpeqvd aivsewmgyg llhesmlssv lhartkwlke
      181 gglllpdsae lfvapisdqm lewrlgfwsq vkqhygvdms cmesfatrcl mghseivvqg
      241 lsgedvlarp qrfaqlelar agleqeleag vggrfrcscy gsaplhgfai wfqvtfpggd
      301 sekplvlsts pfhpathwkq allylnepvp veqdtdisge itllpsrdnp rrlrvllryk
      361 vgdheektkd famed
//
LOCUS       NP_077339                353 aa            linear   ROD 15-APR-2025
DEFINITION  protein arginine N-methyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_077339
VERSION     NP_077339.1
DBSOURCE    REFSEQ: accession NM_024363.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Shen,Q., Xiao,Y., Cheng,B., Sun,Z., Hu,Y., Yang,H. and Luo,Y.
  TITLE     PRMT1 promotes extracellular matrix degradation and apoptosis of
            chondrocytes in temporomandibular joint osteoarthritis via the
            AKT/FOXO1 signaling pathway
  JOURNAL   Int J Biochem Cell Biol 141, 106112 (2021)
   PUBMED   34715362
  REMARK    GeneRIF: PRMT1 promotes extracellular matrix degradation and
            apoptosis of chondrocytes in temporomandibular joint osteoarthritis
            via the AKT/FOXO1 signaling pathway.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Price,O.M., Thakur,A., Ortolano,A., Towne,A., Velez,C., Acevedo,O.
            and Hevel,J.M.
  TITLE     Naturally occurring cancer-associated mutations disrupt
            oligomerization and activity of protein arginine methyltransferase
            1 (PRMT1)
  JOURNAL   J Biol Chem 297 (5), 101336 (2021)
   PUBMED   34688662
  REMARK    GeneRIF: Naturally occurring cancer-associated mutations disrupt
            oligomerization and activity of protein arginine methyltransferase
            1 (PRMT1).
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ma,J., Wu,Y. and He,Y.
  TITLE     Silencing circRNA LRP6 down-regulates PRMT1 to improve the
            streptozocin-induced pancreatic beta-cell injury and insulin
            secretion by sponging miR-9-5p
  JOURNAL   J Bioenerg Biomembr 53 (3), 333-342 (2021)
   PUBMED   33826088
  REMARK    GeneRIF: Silencing circRNA LRP6 down-regulates PRMT1 to improve the
            streptozocin-induced pancreatic beta-cell injury and insulin
            secretion by sponging miR-9-5p.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Zhu,Y., Yu,C. and Zhuang,S.
  TITLE     Protein arginine methyltransferase 1 mediates renal fibroblast
            activation and fibrogenesis through activation of Smad3 signaling
  JOURNAL   Am J Physiol Renal Physiol 318 (2), F375-F387 (2020)
   PUBMED   31813251
  REMARK    GeneRIF: PRMT1 may mediate renal fibroblast activation and renal
            fibrosis development through activation of the TGF-beta/Smad3
            signaling pathway.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Jeong,M.H., Jeong,H.J., Ahn,B.Y., Pyun,J.H., Kwon,I., Cho,H. and
            Kang,J.S.
  TITLE     PRMT1 suppresses ATF4-mediated endoplasmic reticulum response in
            cardiomyocytes
  JOURNAL   Cell Death Dis 10 (12), 903 (2019)
   PUBMED   31787756
  REMARK    GeneRIF: PRMT1 suppresses ATF4-mediated endoplasmic reticulum
            response in cardiomyocytes.
            Erratum:[Cell Death Dis. 2020 Mar 23;11(3):203. doi:
            10.1038/s41419-020-2373-8. PMID: 32251281]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Pawlak,M.R., Scherer,C.A., Chen,J., Roshon,M.J. and Ruley,H.E.
  TITLE     Arginine N-methyltransferase 1 is required for early
            postimplantation mouse development, but cells deficient in the
            enzyme are viable
  JOURNAL   Mol Cell Biol 20 (13), 4859-4869 (2000)
   PUBMED   10848611
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Tang,J., Gary,J.D., Clarke,S. and Herschman,H.R.
  TITLE     PRMT 3, a type I protein arginine N-methyltransferase that differs
            from PRMT1 in its oligomerization, subcellular localization,
            substrate specificity, and regulation
  JOURNAL   J Biol Chem 273 (27), 16935-16945 (1998)
   PUBMED   9642256
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Lin,W.J., Gary,J.D., Yang,M.C., Clarke,S. and Herschman,H.R.
  TITLE     The mammalian immediate-early TIS21 protein and the
            leukemia-associated BTG1 protein interact with a protein-arginine
            N-methyltransferase
  JOURNAL   J Biol Chem 271 (25), 15034-15044 (1996)
   PUBMED   8663146
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Gary,J.D., Lin,W.J., Yang,M.C., Herschman,H.R. and Clarke,S.
  TITLE     The predominant protein-arginine methyltransferase from
            Saccharomyces cerevisiae
  JOURNAL   J Biol Chem 271 (21), 12585-12594 (1996)
   PUBMED   8647869
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U60882.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U60882.1, FQ219843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..353
                     /product="protein arginine N-methyltransferase 1"
                     /EC_number="2.1.1.319"
                     /function="methylates (mono and asymmetric dimethylation)
                     the guanidino nitrogens of arginyl residues present in a
                     glycine and arginine-rich domain; (e.g. can methylate
                     recombinant hnRNPA1 as well as crude histones)"
                     /note="histone-arginine N-methyltransferase PRMT1;
                     heterogeneous nuclear ribonucleoproteins
                     methyltransferase-like 2"
                     /calculated_mol_wt=40391
     Region          45..>218
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIF0; propagated from
                     UniProtKB/Swiss-Prot (Q63009.1)"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIF0; propagated from
                     UniProtKB/Swiss-Prot (Q63009.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99873; propagated from
                     UniProtKB/Swiss-Prot (Q63009.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99873; propagated from
                     UniProtKB/Swiss-Prot (Q63009.1)"
     CDS             1..353
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /coded_by="NM_024363.1:3..1064"
                     /db_xref="GeneID:60421"
                     /db_xref="RGD:62020"
ORIGIN      
        1 maaaeaanci mevscgqaes sekpnaedmt skdyyfdsya hfgiheemlk devrtltyrn
       61 smfhnrhlfk dkvvldvgsg tgilcmfaak agarkvigie cssisdyavk ivkankldhv
      121 vtiikgkvee velpvekvdi iisewmgycl fyesmlntvl hardkwlapd glifpdratl
      181 yvtaiedrqy kdykihwwen vygfdmscik dvaikeplvd vvdpkqlvtn aclikevdiy
      241 tvkvedltft spfclqvkrn dyvhalvayf nieftrchkr tgfstspesp ythwkqtvfy
      301 medyltvktg eeifgtigmr pnaknnrdld ftidldfkgq lcelscstdy rmr
//
LOCUS       NP_446271                217 aa            linear   ROD 15-APR-2025
DEFINITION  metalloproteinase inhibitor 1 precursor [Rattus norvegicus].
ACCESSION   NP_446271
VERSION     NP_446271.1
DBSOURCE    REFSEQ: accession NM_053819.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Xi,X., Yang,Y., Chen,Q., Ma,J., Wang,X., Deng,Y., Wang,X. and Li,Y.
  TITLE     GnT-V-mediated aberrant N-glycosylation of TIMP-1 promotes diabetic
            retinopathy progression
  JOURNAL   Mol Biol Rep 51 (1), 428 (2024)
   PUBMED   38499842
  REMARK    GeneRIF: GnT-V-mediated aberrant N-glycosylation of TIMP-1 promotes
            diabetic retinopathy progression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Ahmadighadykolaei,H., Lambert,J.A. and Raeeszadeh-Sarmazdeh,M.
  TITLE     TIMP-1 Protects Tight Junctions of Brain Endothelial Cells From
            MMP-Mediated Degradation
  JOURNAL   Pharm Res 40 (9), 2121-2131 (2023)
   PUBMED   37700105
  REMARK    GeneRIF: TIMP-1 Protects Tight Junctions of Brain Endothelial Cells
            From MMP-Mediated Degradation.
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Huang,S., Chen,M., Yu,H., Lin,K., Guo,Y. and Zhu,P.
  TITLE     Co-expression of tissue kallikrein 1 and tissue inhibitor of matrix
            metalloproteinase 1 improves myocardial ischemia-reperfusion injury
            by promoting angiogenesis and inhibiting oxidative stress
  JOURNAL   Mol Med Rep 23 (2) (2021)
   PUBMED   33355364
  REMARK    GeneRIF: Coexpression of tissue kallikrein 1 and tissue inhibitor
            of matrix metalloproteinase 1 improves myocardial
            ischemiareperfusion injury by promoting angiogenesis and inhibiting
            oxidative stress.
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Yuan,Y., Naito,H., Kitamori,K., Hashimoto,S., Asano,T. and
            Nakajima,T.
  TITLE     The antihypertensive agent hydralazine reduced extracellular matrix
            synthesis and liver fibrosis in nonalcoholic steatohepatitis
            exacerbated by hypertension
  JOURNAL   PLoS One 15 (12), e0243846 (2020)
   PUBMED   33315911
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Samper Agrelo,I., Schira-Heinen,J., Beyer,F., Groh,J.,
            Butermann,C., Estrada,V., Poschmann,G., Bribian,A., Jadasz,J.J.,
            Lopez-Mascaraque,L., Kremer,D., Martini,R., Muller,H.W.,
            Hartung,H.P., Adjaye,J., Stuhler,K. and Kury,P.
  TITLE     Secretome Analysis of Mesenchymal Stem Cell Factors Fostering
            Oligodendroglial Differentiation of Neural Stem Cells In Vivo
  JOURNAL   Int J Mol Sci 21 (12), 4350 (2020)
   PUBMED   32570968
  REMARK    GeneRIF: Secretome Analysis of Mesenchymal Stem Cell Factors
            Fostering Oligodendroglial Differentiation of Neural Stem Cells In
            Vivo.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Boujrad,N., Ogwuegbu,S.O., Garnier,M., Lee,C.H., Martin,B.M. and
            Papadopoulos,V.
  TITLE     Identification of a stimulator of steroid hormone synthesis
            isolated from testis
  JOURNAL   Science 268 (5217), 1609-1612 (1995)
   PUBMED   7777858
  REMARK    Erratum:[Science 1995 Oct 20;270(5235):365]
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Chun,S.Y., Popliker,M., Reich,R. and Tsafriri,A.
  TITLE     Localization of preovulatory expression of plasminogen activator
            inhibitor type-1 and tissue inhibitor of metalloproteinase type-1
            mRNAs in the rat ovary
  JOURNAL   Biol Reprod 47 (2), 245-253 (1992)
   PUBMED   1327205
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Roswit,W.T., McCourt,D.W., Partridge,N.C. and Jeffrey,J.J.
  TITLE     Purification and sequence analysis of two rat tissue inhibitors of
            metalloproteinases
  JOURNAL   Arch Biochem Biophys 292 (2), 402-410 (1992)
   PUBMED   1309971
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Docherty,A.J., Lyons,A., Smith,B.J., Wright,E.M., Stephens,P.E.,
            Harris,T.J., Murphy,G. and Reynolds,J.J.
  TITLE     Sequence of human tissue inhibitor of metalloproteinases and its
            identity to erythroid-potentiating activity
  JOURNAL   Nature 318 (6041), 66-69 (1985)
   PUBMED   3903517
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Gasson,J.C., Golde,D.W., Kaufman,S.E., Westbrook,C.A., Hewick,R.M.,
            Kaufman,R.J., Wong,G.G., Temple,P.A., Leary,A.C., Brown,E.L. et al.
  TITLE     Molecular characterization and expression of the gene encoding
            human erythroid-potentiating activity
  JOURNAL   Nature 315 (6022), 768-771 (1985)
   PUBMED   3839290
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L31883.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L31883.1, FQ219856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093045, SAMN16093046
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..217
                     /product="metalloproteinase inhibitor 1 precursor"
                     /function="tissue inhibitor of metalloproteinase (type 1)"
                     /note="metalloproteinase inhibitor 1; tissue inhibitor of
                     metalloproteinases 1; tissue inhibitor of
                     metalloproteinase 1; tissue inhibitor of metallopeptidase
                     1"
                     /calculated_mol_wt=21537
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2275
     mat_peptide     24..217
                     /product="metalloproteinase inhibitor 1"
                     /function="tissue inhibitor of metalloproteinase (type 1)"
                     /calculated_mol_wt=21537
     Region          24..199
                     /region_name="NTR"
                     /note="Tissue inhibitor of metalloproteinase family;
                     smart00206"
                     /db_xref="CDD:128502"
     Region          24..27
                     /region_name="Involved in metalloproteinase-binding.
                     /evidence=ECO:0000250|UniProtKB:P16035"
                     /note="propagated from UniProtKB/Swiss-Prot (P30120.2)"
     Site            37
                     /site_type="other"
                     /note="Involved in metalloproteinase-binding.
                     /evidence=ECO:0000250|UniProtKB:P16035; propagated from
                     UniProtKB/Swiss-Prot (P30120.2)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30120.2)"
     Region          90..91
                     /region_name="Involved in metalloproteinase-binding.
                     /evidence=ECO:0000250|UniProtKB:P16035"
                     /note="propagated from UniProtKB/Swiss-Prot (P30120.2)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30120.2)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01033; propagated from
                     UniProtKB/Swiss-Prot (P30120.2)"
     CDS             1..217
                     /gene="Timp1"
                     /gene_synonym="Timp; TIMP-1"
                     /coded_by="NM_053819.1:36..689"
                     /db_xref="GeneID:116510"
                     /db_xref="RGD:621675"
ORIGIN      
        1 mapfaslasg illllslias skacscapth pqtafcnsdl virakfmgsp eiiettlyqr
       61 yeikmtkmlk gfdavgnatg frfaytpame slcgyvhksq nrseefliag rlrngnlhit
      121 acsflvpwhn lspaqqkafv ktysagcgvc tvfpcsaipc klesdshclw tdqilmgsek
      181 gyqsdhfacl prnpdlctwq ylgvsmtrsl plakaea
//
LOCUS       NP_001425124             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425124
VERSION     NP_001425124.1
DBSOURCE    REFSEQ: accession NM_001438195.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.2133.1,
                                           SRR26643290.2961.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438195.1:335..1396"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425147             619 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425147
VERSION     NP_001425147.1
DBSOURCE    REFSEQ: accession NM_001438218.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.359589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093043 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438218.1:1158..3017"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001425069             506 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001425069 XP_006229168
VERSION     NP_001425069.1
DBSOURCE    REFSEQ: accession NM_001438140.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229168.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3151.1,
                                           SRR26360181.756654.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..506
                     /product="tubby-related protein 2 isoform 7"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=55947
     Region          1..>156
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          252..501
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..506
                     /gene="Tulp2"
                     /coded_by="NM_001438140.1:257..1777"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mvqanpdasl rhrrprrgee rfqsdsswgl gvgspflqen vpqahlpsga hsalvtmsyv
       61 gdgsgerapl lsprgavytr gngpavrhlc wlpdssdsdv eevtmedipv isrppkthla
      121 nrrrgwlasp gpgiseeeev epkdarvedk tpspdpdpte nsdrvhgdsa scnmeentak
      181 knietasgig dedpekkeat estetnnalv askvlqgdgd tsnhsawnmt cpmprtpgpr
      241 lgedmeayvl lpaprehmvq crivrnkhgv dkgmfpsyyl yleaedgvav rssplghfll
      301 agrkrkrskt snylisldpk dmsrngnnfv gkvrsnvlgt kftifdngvn pernywipds
      361 arireelgvv cyetnvlgfr gprkmtvilp gmdsrkqrmk vqpqndqdsi lsrvqkgarh
      421 gllllqnkap swsdesgayv lnfhgrvtra svknfqivhp depdhlvlqf grvapniftm
      481 dfryplcplq afaiclssfd gklace
//
LOCUS       NP_001425073             443 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001425073
VERSION     NP_001425073.1
DBSOURCE    REFSEQ: accession NM_001438144.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3164.1,
                                           SRR26360181.1333963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..443
                     /product="tubby-related protein 2 isoform 11"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=49133
     Region          196..438
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..443
                     /gene="Tulp2"
                     /coded_by="NM_001438144.1:213..1544"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 msyvgdgsge rapllsprga vytrgngpav rhlcwlpdss dsdveevtme dipvisrppk
       61 thlanrrrgw laspgpgise eeevepkdar vedktpspdp dptensdrvh gdsascnmee
      121 ntakknieta sgigdedpek keatestetn nalvaskvlq gdgdtsnhsa wnmtcpmprt
      181 pgprlgedme ayvllpapre hmvqcrivrn khgvdkgmfp syylyleaed gvahfllagr
      241 krkrsktsny lisldpkdms rngnnfvgkv rsnvlgtkft ifdngvnper nywipdsari
      301 reelgvvcye tnvlgfrgpr kmtvilpgmd srkqrmkvqp qndqdsilsr vqkgarhgll
      361 llqnkapsws desgayvlnf hgrvtrasvk nfqivhpdep dhlvlqfgrv apniftmdfr
      421 yplcplqafa iclssfdgkl ace
//
LOCUS       NP_001425066             555 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001425066
VERSION     NP_001425066.1
DBSOURCE    REFSEQ: accession NM_001438137.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.2274.1,
                                           SRR26643293.3152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..555
                     /product="tubby-related protein 2 isoform 4"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=62129
     Region          39..>212
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          308..550
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..555
                     /gene="Tulp2"
                     /coded_by="NM_001438137.1:16..1683"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mdregprgpr rgtsqeneqw kketledefs gvrlqkleqq rqlfekkqrr krqeplmvqa
       61 npdaslrhrr prrgeerfqs dsswglgvgs pflqenvpqa hlpsgahsal vtmsyvgdgs
      121 gerapllspr gavytrgngp avrhlcwlpd ssdsdveevt medipvisrp pkthlanrrr
      181 gwlaspgpgi seeeevepkd arvedktpsp dpdptensdr vhgdsascnm eentakknie
      241 tasgigdedp ekkeateste tnnalvaskv lqgdgdtsnh sawnmtcpmp rtpgprlged
      301 meayvllpap rehmvqcriv rnkhgvdkgm fpsyylylea edgvahflla grkrkrskts
      361 nylisldpkd msrngnnfvg kvrsnvlgtk ftifdngvnp ernywipdsa rireelgvvc
      421 yetnvlgfrg prkmtvilpg mdsrkqrmkv qpqndqdsil srvqkgarhg llllqnkaps
      481 wsdesgayvl nfhgrvtras vknfqivhpd epdhlvlqfg rvapniftmd fryplcplqa
      541 faiclssfdg klace
//
LOCUS       NP_001425131             268 aa            linear   ROD 16-APR-2025
DEFINITION  tripartite motif-containing protein 5 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425131 XP_038934094
VERSION     NP_001425131.1
DBSOURCE    REFSEQ: accession NM_001438202.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Zurek,B., Schoultz,I., Neerincx,A., Napolitano,L.M., Birkner,K.,
            Bennek,E., Sellge,G., Lerm,M., Meroni,G., Soderholm,J.D. and
            Kufer,T.A.
  TITLE     TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal
            degradation
  JOURNAL   PLoS One 7 (7), e41255 (2012)
   PUBMED   22829933
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Pertel,T., Hausmann,S., Morger,D., Zuger,S., Guerra,J., Lascano,J.,
            Reinhard,C., Santoni,F.A., Uchil,P.D., Chatel,L., Bisiaux,A.,
            Albert,M.L., Strambio-De-Castillia,C., Mothes,W., Pizzato,M.,
            Grutter,M.G. and Luban,J.
  TITLE     TRIM5 is an innate immune sensor for the retrovirus capsid lattice
  JOURNAL   Nature 472 (7343), 361-365 (2011)
   PUBMED   21512573
REFERENCE   6  (residues 1 to 268)
  AUTHORS   O'Connor,C., Pertel,T., Gray,S., Robia,S.L., Bakowska,J.C.,
            Luban,J. and Campbell,E.M.
  TITLE     p62/sequestosome-1 associates with and sustains the expression of
            retroviral restriction factor TRIM5alpha
  JOURNAL   J Virol 84 (12), 5997-6006 (2010)
   PUBMED   20357094
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038934094.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1964512.1,
                                           SRR26643292.3155.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..268
                     /product="tripartite motif-containing protein 5 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 5"
                     /calculated_mol_wt=30404
     Region          47..264
                     /region_name="SPRY_PRY_TRIM5"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     5 (TRIM5), also known as RING finger protein 88 (RNF88);
                     cd15822"
                     /db_xref="CDD:293994"
     CDS             1..268
                     /gene="Trim5"
                     /gene_synonym="RGD1304579"
                     /coded_by="NM_001438202.1:891..1697"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:308906"
                     /db_xref="RGD:1304579"
ORIGIN      
        1 msilsrgven tikrshtfsm rkpktipkeq rrvfrapdlq gmlqvlqevt eaqrywvqvt
       61 lvesnnpnif itadkrqiry edhqarhfar ptenchagvl gypaiqsgkh ywevdvsgkg
      121 swvlglsdgs ylfnpifrsn aerppnpplf rlnlsndshs rlslsndshy qpkygfwvig
      181 lwgnsvynaf eectftgkps vltlslmvrp crvgifldca agtlsfynis nhgtliyrfc
      241 agsfpdrvfp yfnpmgssep lticwpds
//
LOCUS       NP_001425168             304 aa            linear   ROD 16-APR-2025
DEFINITION  DCN1-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001425168 XP_063119704
VERSION     NP_001425168.1
DBSOURCE    REFSEQ: accession NM_001438239.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ma,T., Shi,T., Huang,J., Wu,L., Hu,F., He,P., Deng,W., Gao,P.,
            Zhang,Y., Song,Q., Ma,D. and Qiu,X.
  TITLE     DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
            progression and cell growth
  JOURNAL   Cancer Sci 99 (11), 2128-2135 (2008)
   PUBMED   18823379
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063119704.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.3630.1,
                                           SRR26360194.2275618.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..304
                     /product="DCN1-like protein 3"
                     /EC_number="3.1.-.-"
                     /note="DCUN1 domain-containing protein 3; defective in
                     cullin neddylation protein 1-like protein 3; DCN1,
                     defective in cullin neddylation 1, domain containing 3"
                     /calculated_mol_wt=34219
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     Region          164..276
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     Region          285..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     CDS             1..304
                     /gene="Dcun1d3"
                     /gene_synonym="DCNL3; RGD1308893"
                     /coded_by="NM_001438239.1:309..1223"
                     /db_xref="GeneID:309035"
                     /db_xref="RGD:1308893"
ORIGIN      
        1 mgqcvtkckn psstlgskng drdpsskshs rrgashreeq vppcgkpagd ilvngtkkae
       61 aateacqlpt ssgdagresk tnaeesslqr leelfrrykd eredaileeg merfcndlcv
      121 dptefrvlll awkfqaatmc kftrkeffdg ckaisadsid gicarfpsll teakqedkfk
      181 dlyrftfqfg ldseegqrsl hreiaialwk lvftqnnppv ldqwlnflte npsgikgisr
      241 dtwnmflnft qvigpdlsny sedeawpslf dtfvewemer rkrevegrga lssgpeglcp
      301 eeqt
//
LOCUS       NP_001425152             630 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425152 XP_038934367
VERSION     NP_001425152.1
DBSOURCE    REFSEQ: accession NM_001438223.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038934367.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.296439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..630
                     /product="zinc finger protein 668 isoform 2"
                     /calculated_mol_wt=69379
     Region          35..55
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(35,38,51,55)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          76..430
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          97..117
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          125..145
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(125,128,141,145)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(181,184,197,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,240,253,257)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(242,244,246,248..249,252..253,256,270,272,276..277,
                     280..281,284,298,300,302,304..305,308..309,312)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          259..609
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(529,532,545,549)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(534,536,538,540..541,544..545,548,562,564,568..569,
                     572..573,576,590,592,594,596..597,600..601,604)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          557..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          585..605
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..630
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438223.1:165..2057"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 mepregllte ameveaaeak spgpcykrsg rrykclfctk tfpnapraar haathtttdc
       61 teevnevqpk vdaepkaeea sgdkvsgsva kprpyacplc pkayktapel rshgrshtge
      121 kpfpcpecgr rfmqpvclrv hlashagelp frcthcpkay gtlsklkihq rghtgerpya
      181 ctdcgksfad psvfrkhrrt haglrpysce rcgkayaelk dlrnhersht gerpflcsec
      241 gksfsrsssl tchqrihaaq kpyrcpacgk gftqlssyqs herthsgekp flcprcgrmf
      301 sdpssfrrhq rahegvkpyr cekcgkdfrq padlamhrrv htgdrpfkcl qcdktfvasw
      361 dlkrhalvhs gqrpfrceec grafaerasl tkhsrmhsge rpfhcnacgk sfvvlsslrk
      421 herthrsnet tgaapqqelv lglalpvgvv gegsaapvag agigdapagl lglppesgsv
      481 vatqwqvvgm tvehvecqda gvgeapstlg dagevggeet dekppqfvcr ecketfstlt
      541 llrrhershp elrpfpctqc gksfsdragl rkhsrthssv rpyscsqcpk aflsasdlrk
      601 herthpvpig tpipleplva llgmpeegsa
//
LOCUS       NP_001425127             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425127 XP_038969136
VERSION     NP_001425127.1
DBSOURCE    REFSEQ: accession NM_001438198.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038969136.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1637476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680431, SAMN06680442
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438198.1:137..1198"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001020057             304 aa            linear   ROD 16-APR-2025
DEFINITION  DCN1-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001020057 XP_219389
VERSION     NP_001020057.1
DBSOURCE    REFSEQ: accession NM_001024886.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ma,T., Shi,T., Huang,J., Wu,L., Hu,F., He,P., Deng,W., Gao,P.,
            Zhang,Y., Song,Q., Ma,D. and Qiu,X.
  TITLE     DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
            progression and cell growth
  JOURNAL   Cancer Sci 99 (11), 2128-2135 (2008)
   PUBMED   18823379
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 17, 2005 this sequence version replaced XP_219389.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097462.1, SRR26360172.162881.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..304
                     /product="DCN1-like protein 3"
                     /EC_number="3.1.-.-"
                     /note="DCUN1 domain-containing protein 3; defective in
                     cullin neddylation protein 1-like protein 3; DCN1,
                     defective in cullin neddylation 1, domain containing 3"
                     /calculated_mol_wt=34219
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     Region          164..276
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     Region          285..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     CDS             1..304
                     /gene="Dcun1d3"
                     /gene_synonym="DCNL3; RGD1308893"
                     /coded_by="NM_001024886.2:314..1228"
                     /db_xref="GeneID:309035"
                     /db_xref="RGD:1308893"
ORIGIN      
        1 mgqcvtkckn psstlgskng drdpsskshs rrgashreeq vppcgkpagd ilvngtkkae
       61 aateacqlpt ssgdagresk tnaeesslqr leelfrrykd eredaileeg merfcndlcv
      121 dptefrvlll awkfqaatmc kftrkeffdg ckaisadsid gicarfpsll teakqedkfk
      181 dlyrftfqfg ldseegqrsl hreiaialwk lvftqnnppv ldqwlnflte npsgikgisr
      241 dtwnmflnft qvigpdlsny sedeawpslf dtfvewemer rkrevegrga lssgpeglcp
      301 eeqt
//
LOCUS       NP_001425166             304 aa            linear   ROD 16-APR-2025
DEFINITION  DCN1-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001425166 XP_038934549
VERSION     NP_001425166.1
DBSOURCE    REFSEQ: accession NM_001438237.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ma,T., Shi,T., Huang,J., Wu,L., Hu,F., He,P., Deng,W., Gao,P.,
            Zhang,Y., Song,Q., Ma,D. and Qiu,X.
  TITLE     DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
            progression and cell growth
  JOURNAL   Cancer Sci 99 (11), 2128-2135 (2008)
   PUBMED   18823379
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038934549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.4109.1,
                                           SRR26643299.4203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..304
                     /product="DCN1-like protein 3"
                     /EC_number="3.1.-.-"
                     /note="DCUN1 domain-containing protein 3; defective in
                     cullin neddylation protein 1-like protein 3; DCN1,
                     defective in cullin neddylation 1, domain containing 3"
                     /calculated_mol_wt=34219
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     Region          164..276
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     Region          285..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     CDS             1..304
                     /gene="Dcun1d3"
                     /gene_synonym="DCNL3; RGD1308893"
                     /coded_by="NM_001438237.1:189..1103"
                     /db_xref="GeneID:309035"
                     /db_xref="RGD:1308893"
ORIGIN      
        1 mgqcvtkckn psstlgskng drdpsskshs rrgashreeq vppcgkpagd ilvngtkkae
       61 aateacqlpt ssgdagresk tnaeesslqr leelfrrykd eredaileeg merfcndlcv
      121 dptefrvlll awkfqaatmc kftrkeffdg ckaisadsid gicarfpsll teakqedkfk
      181 dlyrftfqfg ldseegqrsl hreiaialwk lvftqnnppv ldqwlnflte npsgikgisr
      241 dtwnmflnft qvigpdlsny sedeawpslf dtfvewemer rkrevegrga lssgpeglcp
      301 eeqt
//
LOCUS       NP_001425116            1150 aa            linear   ROD 16-APR-2025
DEFINITION  alpha-mannosidase 2x isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425116 XP_063118711
VERSION     NP_001425116.1
DBSOURCE    REFSEQ: accession NM_001438187.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Akama,T.O., Nakagawa,H., Wong,N.K., Sutton-Smith,M., Dell,A.,
            Morris,H.R., Nakayama,J., Nishimura,S., Pai,A., Moremen,K.W.,
            Marth,J.D. and Fukuda,M.N.
  TITLE     Essential and mutually compensatory roles of {alpha}-mannosidase II
            and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (24), 8983-8988 (2006)
   PUBMED   16754854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063118711.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.3592.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..1150
                     /product="alpha-mannosidase 2x isoform 2"
                     /EC_number="3.2.1.114"
                     /note="alpha-mannosidase 2x; mannosidase 2, alpha 2"
                     /calculated_mol_wt=130307
     Region          140..1149
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     CDS             1..1150
                     /gene="Man2a2"
                     /coded_by="NM_001438187.1:602..4054"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308757"
                     /db_xref="RGD:1310238"
ORIGIN      
        1 mklkkqvtvc gaaifcvavf slylmldrvq hdparhqngg nfprsqisvl qnrieqleql
       61 leenheiish ikdsvlelta naegppallp yhtangswav lpeprpsffs vspedcqfal
      121 ggrgqkpelq mltvsedlpf dnveggvwrq gfdisyspnd wdaedlqvfv vphshndpgw
      181 iktfdkyyte qtqhilnsmv sklqedprrr flwaevsffa kwwdnisaqk raavrrlvgn
      241 gqleiatggw vmpdeanshy falvdqlieg hqwlernlga tprsgwavdp fghsstmpyl
      301 lrranltsml iqrvhyaikk hfaathslef mwrqtwdsds stdifchmmp fysydvphtc
      361 gpdpkiccqf dfkrlpggri ncpwkvppra iteanvadra allldqyrkk srlfrssvll
      421 vplgddfryd kpqewdaqff nyqrlfdfln skpefhvqaq fgtlseyfda lykrtgvepg
      481 arppgfpvls gdffsyadre dhywtgyyts rpfyksldrv lethlrgaev lyslalahar
      541 rsgltgqypl sdyavltear rtlglfqhhd aitgtakeav vvdygvrllr slvslkqvii
      601 naahylvlgd ketysfdpra pflqmddsrv shdalpertv irldssprfv vvfnpleqer
      661 lsvvsllvns prvrvlseeg qplsvqisvq wssatnmvpd vyqvsvpvrl palglgvlql
      721 qpdldgpytl qssvhvylng vklsvsrqtt fplrvvdsgt sdfaisnrym qvwfsgltgl
      781 lksvrrvdee qeqqvdmklf vygtrtskdk sgaylflpdn eakpyvpkkp pvlrvtegpf
      841 fsevaayyeh fhqvirlynl pgveglsldv sfqvdirdyv nkelalriht didsqgtfft
      901 dlngfqvqpr kylkklplqa nfypmpvmay iqdsqrrltl htaqalgvss lgngqlevil
      961 drrlmqddnr glgqglkdnk itcnhfrlll errtlmspev qqerstsyps llshmtsmyl
     1021 ntpplvlpva krestsptlh sfhplasplp cdfhllnlrm lpaedtlpaa daalilhrkg
     1081 fdcgleaknl gfncttsqgk lalgslfhgl dvlflqptsl tllyplasps nstdislepm
     1141 eistfrlrlg
//
LOCUS       NP_001425108            1087 aa            linear   ROD 16-APR-2025
DEFINITION  structural maintenance of chromosomes protein 5 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425108 XP_006231246
VERSION     NP_001425108.1
DBSOURCE    REFSEQ: accession NM_001438179.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Raschle,M., Smeenk,G., Hansen,R.K., Temu,T., Oka,Y., Hein,M.Y.,
            Nagaraj,N., Long,D.T., Walter,J.C., Hofmann,K., Storchova,Z.,
            Cox,J., Bekker-Jensen,S., Mailand,N. and Mann,M.
  TITLE     DNA repair. Proteomics reveals dynamic assembly of repair complexes
            during bypass of DNA cross-links
  JOURNAL   Science 348 (6234), 1253671 (2015)
   PUBMED   25931565
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Brouwer,A.K., Schimmel,J., Wiegant,J.C., Vertegaal,A.C., Tanke,H.J.
            and Dirks,R.W.
  TITLE     Telomeric DNA mediates de novo PML body formation
  JOURNAL   Mol Biol Cell 20 (22), 4804-4815 (2009)
   PUBMED   19793919
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Behlke-Steinert,S., Touat-Todeschini,L., Skoufias,D.A. and
            Margolis,R.L.
  TITLE     SMC5 and MMS21 are required for chromosome cohesion and mitotic
            progression
  JOURNAL   Cell Cycle 8 (14), 2211-2218 (2009)
   PUBMED   19502785
REFERENCE   5  (residues 1 to 1087)
  AUTHORS   Taylor,E.M., Copsey,A.C., Hudson,J.J., Vidot,S. and Lehmann,A.R.
  TITLE     Identification of the proteins, including MAGEG1, that make up the
            human SMC5-6 protein complex
  JOURNAL   Mol Cell Biol 28 (4), 1197-1206 (2008)
   PUBMED   18086888
REFERENCE   6  (residues 1 to 1087)
  AUTHORS   Potts,P.R. and Yu,H.
  TITLE     The SMC5/6 complex maintains telomere length in ALT cancer cells
            through SUMOylation of telomere-binding proteins
  JOURNAL   Nat Struct Mol Biol 14 (7), 581-590 (2007)
   PUBMED   17589526
REFERENCE   7  (residues 1 to 1087)
  AUTHORS   Potts,P.R., Porteus,M.H. and Yu,H.
  TITLE     Human SMC5/6 complex promotes sister chromatid homologous
            recombination by recruiting the SMC1/3 cohesin complex to
            double-strand breaks
  JOURNAL   EMBO J 25 (14), 3377-3388 (2006)
   PUBMED   16810316
REFERENCE   8  (residues 1 to 1087)
  AUTHORS   Taylor,E.M., Moghraby,J.S., Lees,J.H., Smit,B., Moens,P.B. and
            Lehmann,A.R.
  TITLE     Characterization of a novel human SMC heterodimer homologous to the
            Schizosaccharomyces pombe Rad18/Spr18 complex
  JOURNAL   Mol Biol Cell 12 (6), 1583-1594 (2001)
   PUBMED   11408570
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006231246.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.5990.1,
                                           SRR26643429.5244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1087
                     /product="structural maintenance of chromosomes protein 5
                     isoform 2"
                     /note="SMC5 structural maintenance of chromosomes 5-like
                     1; structural maintenance of chromosomes protein 5"
                     /calculated_mol_wt=127350
     Region          51..>196
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          53..1037
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            80..87
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213244"
     Site            178..181
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213244"
     Region          <960..1062
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            976..985
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213244"
     Site            1000..1005
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213244"
     Site            1008..1011
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213244"
     Site            1035..1041
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213244"
     CDS             1..1087
                     /gene="Smc5"
                     /gene_synonym="Smc5l1"
                     /coded_by="NM_001438179.1:86..3349"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293967"
                     /db_xref="RGD:1307492"
ORIGIN      
        1 matpsgkaaa pnpqaskrsl prdassefps krknsnptst lprpsglfve gsivriamen
       61 fltydicevs pgphlnmiig angtgkssiv caiclglagk pafmgradkv gffvkrgcsk
      121 glveielfrt sgnliitrei dviknqsfwf inkkpvtqki veeqvaalni qvgnlcqflp
      181 qdkvgefakl skielleate ksigppemhr yhcelknfre kekqletsck ekteyldkmi
      241 qrnerykqdv erfyerkrhl dliemleakr pwveyenvrq eyegvklvrd rvkeevrklk
      301 egqipmtrri eeierqrrtl evrikekatd ikeasqkckq rqdlierkdr hikelqqalt
      361 vkqneeqdrq krisntrkmi edlqnelrta encenlqpqi daitndlrrv qeekalcege
      421 iidkqrekem lekqkrsvsd hitrfdnlmn qkedklrqry rdtydavlwl rnnrdrfkqr
      481 vcepimltin mkdnknakyv enhissndlr afvfesqedm eiflrevrdn kklrvnavia
      541 pkisyadkap srslnelkqy gffsylrelf dapdpvmsyl ccqyhihevp vgtertreri
      601 erviqetrlk qiytaeekyv lktsfysnkv issntslkva qfltvtvdle qrrhleeqlk
      661 einrkleavd sglvalrdtn rhlelkdnel rlkkkeller ktkkrqleqk issklasirl
      721 meqdtcnlee eerkastkik einvqkaklv teltglvkic tslhiqkvdl ilqnttvise
      781 knkleadyma sssqlrvteq qfielddnrq rllqkckelm krarqvcnls adqavpqefq
      841 tafqdlpntl deidalltee rsrascftgl npsvveeytk reieiqqlte elkgkkveld
      901 eyrenisqvk erwlnplkel vekinekfsn ffssmqcage vdlhteneed ydkygirirv
      961 kfrsstqlhe ltphhqsgge rsvstmlylm alqelnrcpf rvvdeinqgm dpinerrvfe
     1021 mvvntacken tsqyffitpk llqnlpysek mtvlfvyngp hmlepnrwnl kafqrrrrri
     1081 tftqpsq
//
LOCUS       NP_001425119             746 aa            linear   ROD 16-APR-2025
DEFINITION  fibronectin type III and SPRY domain-containing protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001425119
VERSION     NP_001425119.1
DBSOURCE    REFSEQ: accession NM_001438190.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..746
                     /product="fibronectin type III and SPRY domain-containing
                     protein 2"
                     /calculated_mol_wt=84567
     Region          203..>307
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          368..453
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            order(368,436,451)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <369..>558
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(452..453,455..456)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          561..737
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..746
                     /gene="Fsd2"
                     /gene_synonym="RGD1305167"
                     /coded_by="NM_001438190.1:446..2686"
                     /db_xref="GeneID:308779"
                     /db_xref="RGD:1305167"
ORIGIN      
        1 meeeageepg lgrstaprdf hfyhmdlyds edrlqlfpge ssrtrrevtq aeltneprga
       61 gdsknlqkev dalvhlygle dehelggefv dehrlgtlgy pygmrrrdpg reqrdwglsg
      121 eaaeaedlcy gvqgppdqcq dlreayryth graseeyecy vipeeedeee padvfcvtck
      181 tpvrtvekdf dihkehevtp inkalehakd eihknmckle qqiiemenfa shleevfitv
      241 eenfgrqeqn fechyneile tlaqkyeeki qalgekkkek lealygqlvs cgenldacre
      301 lmetieemch eekvdflkda vamtdrlgkf lktktdvels akpefedqtl dfsdveqlmd
      361 sintvpapsa pvinpqapns atgssvrvcw slysddtves yqlsyrpvqd sspgkdqaef
      421 tmtvketycs vknlepntqy efwviaqnrt gpspssehvv ymtapsppsi kteairscee
      481 avlicwesgn lnpvdsytve liqaetpeas gvtesvvgip tcesliqlqp rhsytiyvra
      541 lnvggtsars kpatvhttgs yfqlnkdtch pwltisedgf tvvrsekkrs frrelppska
      601 qfsrcvavmg nlipvrgrhy wevevdehld ytvgvacedv pkqedlganr lswcmrhtfa
      661 strhryeflh ngttpdirit vapkkigvll dyedsklsff nvdiaqhlyt fscplhqfvh
      721 pcfsleksgg lkicngisap khvtff
//
LOCUS       NP_001425145             619 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425145
VERSION     NP_001425145.1
DBSOURCE    REFSEQ: accession NM_001438216.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1066385.1,
                                           SRR26643298.5515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438216.1:286..2145"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001425149             630 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425149
VERSION     NP_001425149.1
DBSOURCE    REFSEQ: accession NM_001438220.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.6045.1,
                                           SRR26360181.1606460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..630
                     /product="zinc finger protein 668 isoform 2"
                     /calculated_mol_wt=69379
     Region          35..55
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(35,38,51,55)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          76..430
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          97..117
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          125..145
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(125,128,141,145)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(181,184,197,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,240,253,257)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(242,244,246,248..249,252..253,256,270,272,276..277,
                     280..281,284,298,300,302,304..305,308..309,312)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          259..609
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(529,532,545,549)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(534,536,538,540..541,544..545,548,562,564,568..569,
                     572..573,576,590,592,594,596..597,600..601,604)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          557..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          585..605
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..630
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438220.1:490..2382"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 mepregllte ameveaaeak spgpcykrsg rrykclfctk tfpnapraar haathtttdc
       61 teevnevqpk vdaepkaeea sgdkvsgsva kprpyacplc pkayktapel rshgrshtge
      121 kpfpcpecgr rfmqpvclrv hlashagelp frcthcpkay gtlsklkihq rghtgerpya
      181 ctdcgksfad psvfrkhrrt haglrpysce rcgkayaelk dlrnhersht gerpflcsec
      241 gksfsrsssl tchqrihaaq kpyrcpacgk gftqlssyqs herthsgekp flcprcgrmf
      301 sdpssfrrhq rahegvkpyr cekcgkdfrq padlamhrrv htgdrpfkcl qcdktfvasw
      361 dlkrhalvhs gqrpfrceec grafaerasl tkhsrmhsge rpfhcnacgk sfvvlsslrk
      421 herthrsnet tgaapqqelv lglalpvgvv gegsaapvag agigdapagl lglppesgsv
      481 vatqwqvvgm tvehvecqda gvgeapstlg dagevggeet dekppqfvcr ecketfstlt
      541 llrrhershp elrpfpctqc gksfsdragl rkhsrthssv rpyscsqcpk aflsasdlrk
      601 herthpvpig tpipleplva llgmpeegsa
//
LOCUS       NP_001425167             304 aa            linear   ROD 16-APR-2025
DEFINITION  DCN1-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001425167
VERSION     NP_001425167.1
DBSOURCE    REFSEQ: accession NM_001438238.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ma,T., Shi,T., Huang,J., Wu,L., Hu,F., He,P., Deng,W., Gao,P.,
            Zhang,Y., Song,Q., Ma,D. and Qiu,X.
  TITLE     DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
            progression and cell growth
  JOURNAL   Cancer Sci 99 (11), 2128-2135 (2008)
   PUBMED   18823379
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3234259.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..304
                     /product="DCN1-like protein 3"
                     /EC_number="3.1.-.-"
                     /note="DCUN1 domain-containing protein 3; defective in
                     cullin neddylation protein 1-like protein 3; DCN1,
                     defective in cullin neddylation 1, domain containing 3"
                     /calculated_mol_wt=34219
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     Region          164..276
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     Region          285..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     CDS             1..304
                     /gene="Dcun1d3"
                     /gene_synonym="DCNL3; RGD1308893"
                     /coded_by="NM_001438238.1:338..1252"
                     /db_xref="GeneID:309035"
                     /db_xref="RGD:1308893"
ORIGIN      
        1 mgqcvtkckn psstlgskng drdpsskshs rrgashreeq vppcgkpagd ilvngtkkae
       61 aateacqlpt ssgdagresk tnaeesslqr leelfrrykd eredaileeg merfcndlcv
      121 dptefrvlll awkfqaatmc kftrkeffdg ckaisadsid gicarfpsll teakqedkfk
      181 dlyrftfqfg ldseegqrsl hreiaialwk lvftqnnppv ldqwlnflte npsgikgisr
      241 dtwnmflnft qvigpdlsny sedeawpslf dtfvewemer rkrevegrga lssgpeglcp
      301 eeqt
//
LOCUS       NP_001425071             479 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 9 [Rattus norvegicus].
ACCESSION   NP_001425071 XP_063122871
VERSION     NP_001425071.1
DBSOURCE    REFSEQ: accession NM_001438142.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122871.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2937614.1,
                                           SRR26643293.3138.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..479
                     /product="tubby-related protein 2 isoform 9"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=52819
     Region          <17..>136
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          232..474
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..479
                     /gene="Tulp2"
                     /coded_by="NM_001438142.1:178..1617"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mpntpphdsl gvgspflqen vpqahlpsga hsalvtmsyv gdgsgerapl lsprgavytr
       61 gngpavrhlc wlpdssdsdv eevtmedipv isrppkthla nrrrgwlasp gpgiseeeev
      121 epkdarvedk tpspdpdpte nsdrvhgdsa scnmeentak knietasgig dedpekkeat
      181 estetnnalv askvlqgdgd tsnhsawnmt cpmprtpgpr lgedmeayvl lpaprehmvq
      241 crivrnkhgv dkgmfpsyyl yleaedgvah fllagrkrkr sktsnylisl dpkdmsrngn
      301 nfvgkvrsnv lgtkftifdn gvnpernywi pdsarireel gvvcyetnvl gfrgprkmtv
      361 ilpgmdsrkq rmkvqpqndq dsilsrvqkg arhgllllqn kapswsdesg ayvlnfhgrv
      421 trasvknfqi vhpdepdhlv lqfgrvapni ftmdfryplc plqafaicls sfdgklace
//
LOCUS       NP_001425123             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425123 XP_038969117
VERSION     NP_001425123.1
DBSOURCE    REFSEQ: accession NM_001438194.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038969117.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.2151.1,
                                           SRR26643294.3239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438194.1:418..1479"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425072             450 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 10 [Rattus norvegicus].
ACCESSION   NP_001425072
VERSION     NP_001425072.1
DBSOURCE    REFSEQ: accession NM_001438143.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3166.1,
                                           SRR26360181.1901616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..450
                     /product="tubby-related protein 2 isoform 10"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=49829
     Region          196..445
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..450
                     /gene="Tulp2"
                     /coded_by="NM_001438143.1:213..1565"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 msyvgdgsge rapllsprga vytrgngpav rhlcwlpdss dsdveevtme dipvisrppk
       61 thlanrrrgw laspgpgise eeevepkdar vedktpspdp dptensdrvh gdsascnmee
      121 ntakknieta sgigdedpek keatestetn nalvaskvlq gdgdtsnhsa wnmtcpmprt
      181 pgprlgedme ayvllpapre hmvqcrivrn khgvdkgmfp syylyleaed gvavrssplg
      241 hfllagrkrk rsktsnylis ldpkdmsrng nnfvgkvrsn vlgtkftifd ngvnpernyw
      301 ipdsariree lgvvcyetnv lgfrgprkmt vilpgmdsrk qrmkvqpqnd qdsilsrvqk
      361 garhgllllq nkapswsdes gayvlnfhgr vtrasvknfq ivhpdepdhl vlqfgrvapn
      421 iftmdfrypl cplqafaicl ssfdgklace
//
LOCUS       NP_001425129             511 aa            linear   ROD 16-APR-2025
DEFINITION  tripartite motif-containing protein 5 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425129
VERSION     NP_001425129.1
DBSOURCE    REFSEQ: accession NM_001438200.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Zurek,B., Schoultz,I., Neerincx,A., Napolitano,L.M., Birkner,K.,
            Bennek,E., Sellge,G., Lerm,M., Meroni,G., Soderholm,J.D. and
            Kufer,T.A.
  TITLE     TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal
            degradation
  JOURNAL   PLoS One 7 (7), e41255 (2012)
   PUBMED   22829933
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Pertel,T., Hausmann,S., Morger,D., Zuger,S., Guerra,J., Lascano,J.,
            Reinhard,C., Santoni,F.A., Uchil,P.D., Chatel,L., Bisiaux,A.,
            Albert,M.L., Strambio-De-Castillia,C., Mothes,W., Pizzato,M.,
            Grutter,M.G. and Luban,J.
  TITLE     TRIM5 is an innate immune sensor for the retrovirus capsid lattice
  JOURNAL   Nature 472 (7343), 361-365 (2011)
   PUBMED   21512573
REFERENCE   6  (residues 1 to 511)
  AUTHORS   O'Connor,C., Pertel,T., Gray,S., Robia,S.L., Bakowska,J.C.,
            Luban,J. and Campbell,E.M.
  TITLE     p62/sequestosome-1 associates with and sustains the expression of
            retroviral restriction factor TRIM5alpha
  JOURNAL   J Virol 84 (12), 5997-6006 (2010)
   PUBMED   20357094
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.3602.1,
                                           SRR26643295.3454.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..511
                     /product="tripartite motif-containing protein 5 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 5"
                     /calculated_mol_wt=58928
     Region          8..78
                     /region_name="RING-HC_TRIM5-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and
                     similar proteins; cd16591"
                     /db_xref="CDD:438253"
     Site            order(16..17,19..20,56..57,59)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438253"
     Region          95..133
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          132..>233
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Region          290..507
                     /region_name="SPRY_PRY_TRIM5"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     5 (TRIM5), also known as RING finger protein 88 (RNF88);
                     cd15822"
                     /db_xref="CDD:293994"
     CDS             1..511
                     /gene="Trim5"
                     /gene_synonym="RGD1304579"
                     /coded_by="NM_001438200.1:161..1696"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:308906"
                     /db_xref="RGD:1304579"
ORIGIN      
        1 masefvmnlk eevtcpicld lmvepvsgdc ghsfcqacit lnyesskcnq deficpvcrv
       61 sylfknlrpn rhvanivqrl kefksspeee pkvlscarhg eklqlfckkd mmpicwlcer
      121 sqehrghqtv lieevvqeyk eklqaalqkl madkkefenw kddlqkerty wqnqiqkdve
      181 nvqsefkgmr dimdseekke lqklmqeked imssleesen eysqqskllg dlildvehql
      241 qcsatemlqg ventikrsht fsmrkpktip keqrrvfrap dlqgmlqvlq evteaqrywv
      301 qvtlvesnnp nifitadkrq iryedhqarh farptencha gvlgypaiqs gkhywevdvs
      361 gkgswvlgls dgsylfnpif rsnaerppnp plfrlnlsnd shsrlslsnd shyqpkygfw
      421 viglwgnsvy nafeectftg kpsvltlslm vrpcrvgifl dcaagtlsfy nisnhgtliy
      481 rfcagsfpdr vfpyfnpmgs seplticwpd s
//
LOCUS       NP_001425074             443 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 11 [Rattus norvegicus].
ACCESSION   NP_001425074 XP_063122881
VERSION     NP_001425074.1
DBSOURCE    REFSEQ: accession NM_001438145.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122881.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.660640.1,
                                           SRR26360181.1685240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..443
                     /product="tubby-related protein 2 isoform 11"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=49133
     Region          196..438
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..443
                     /gene="Tulp2"
                     /coded_by="NM_001438145.1:315..1646"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 msyvgdgsge rapllsprga vytrgngpav rhlcwlpdss dsdveevtme dipvisrppk
       61 thlanrrrgw laspgpgise eeevepkdar vedktpspdp dptensdrvh gdsascnmee
      121 ntakknieta sgigdedpek keatestetn nalvaskvlq gdgdtsnhsa wnmtcpmprt
      181 pgprlgedme ayvllpapre hmvqcrivrn khgvdkgmfp syylyleaed gvahfllagr
      241 krkrsktsny lisldpkdms rngnnfvgkv rsnvlgtkft ifdngvnper nywipdsari
      301 reelgvvcye tnvlgfrgpr kmtvilpgmd srkqrmkvqp qndqdsilsr vqkgarhgll
      361 llqnkapsws desgayvlnf hgrvtrasvk nfqivhpdep dhlvlqfgrv apniftmdfr
      421 yplcplqafa iclssfdgkl ace
//
LOCUS       NP_001425062             198 aa            linear   ROD 16-APR-2025
DEFINITION  transmembrane gamma-carboxyglutamic acid protein 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001425062 XP_008757618
VERSION     NP_001425062.1
DBSOURCE    REFSEQ: accession NM_001438133.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757618.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1446145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..198
                     /product="transmembrane gamma-carboxyglutamic acid protein
                     2 precursor"
                     /note="transmembrane gamma-carboxyglutamic acid protein 2;
                     proline-rich Gla (G-carboxyglutamic acid) polypeptide 2;
                     proline rich Gla (G-carboxyglutamic acid) 2"
                     /calculated_mol_wt=20455
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1892
     Region          33..96
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     CDS             1..198
                     /gene="Prrg2"
                     /coded_by="NM_001438133.1:289..885"
                     /db_xref="GeneID:361570"
                     /db_xref="RGD:1305444"
ORIGIN      
        1 mrshpslllv ymglatcldt lphreqsqvl difldapeaq sflvgrrrfp ranhwdlell
       61 tpgnlerecl eercsweear eyfedntlte rfwesyayng kggrgrvdva glavgltsgi
      121 llivlaglga fwylhyrrrr lrvqesclqe tgliiplspp tplspppppg lptyeqalaa
      181 sgvhdapppp ysslrrph
//
LOCUS       NP_001425070             499 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 8 [Rattus norvegicus].
ACCESSION   NP_001425070
VERSION     NP_001425070.1
DBSOURCE    REFSEQ: accession NM_001438141.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3155.1,
                                           SRR26360181.1491763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..499
                     /product="tubby-related protein 2 isoform 8"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=55250
     Region          1..>156
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          252..494
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..499
                     /gene="Tulp2"
                     /coded_by="NM_001438141.1:257..1756"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mvqanpdasl rhrrprrgee rfqsdsswgl gvgspflqen vpqahlpsga hsalvtmsyv
       61 gdgsgerapl lsprgavytr gngpavrhlc wlpdssdsdv eevtmedipv isrppkthla
      121 nrrrgwlasp gpgiseeeev epkdarvedk tpspdpdpte nsdrvhgdsa scnmeentak
      181 knietasgig dedpekkeat estetnnalv askvlqgdgd tsnhsawnmt cpmprtpgpr
      241 lgedmeayvl lpaprehmvq crivrnkhgv dkgmfpsyyl yleaedgvah fllagrkrkr
      301 sktsnylisl dpkdmsrngn nfvgkvrsnv lgtkftifdn gvnpernywi pdsarireel
      361 gvvcyetnvl gfrgprkmtv ilpgmdsrkq rmkvqpqndq dsilsrvqkg arhgllllqn
      421 kapswsdesg ayvlnfhgrv trasvknfqi vhpdepdhlv lqfgrvapni ftmdfryplc
      481 plqafaicls sfdgklace
//
LOCUS       NP_001425115            1175 aa            linear   ROD 16-APR-2025
DEFINITION  alpha-mannosidase 2x isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425115 XP_008757749
VERSION     NP_001425115.1
DBSOURCE    REFSEQ: accession NM_001438186.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Akama,T.O., Nakagawa,H., Wong,N.K., Sutton-Smith,M., Dell,A.,
            Morris,H.R., Nakayama,J., Nishimura,S., Pai,A., Moremen,K.W.,
            Marth,J.D. and Fukuda,M.N.
  TITLE     Essential and mutually compensatory roles of {alpha}-mannosidase II
            and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (24), 8983-8988 (2006)
   PUBMED   16754854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757749.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3867.1,
                                           SRR26360181.1866834.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..1175
                     /product="alpha-mannosidase 2x isoform 1"
                     /EC_number="3.2.1.114"
                     /note="alpha-mannosidase 2x; mannosidase 2, alpha 2"
                     /calculated_mol_wt=133079
     Region          140..1174
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     CDS             1..1175
                     /gene="Man2a2"
                     /coded_by="NM_001438186.1:607..4134"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308757"
                     /db_xref="RGD:1310238"
ORIGIN      
        1 mklkkqvtvc gaaifcvavf slylmldrvq hdparhqngg nfprsqisvl qnrieqleql
       61 leenheiish ikdsvlelta naegppallp yhtangswav lpeprpsffs vspedcqfal
      121 ggrgqkpelq mltvsedlpf dnveggvwrq gfdisyspnd wdaedlqvfv vphshndpgw
      181 iktfdkyyte qtqhilnsmv sklqedprrr flwaevsffa kwwdnisaqk raavrrlvgn
      241 gqleiatggw vmpdeanshy falvdqlieg hqwlernlga tprsgwavdp fghsstmpyl
      301 lrranltsml iqrvhyaikk hfaathslef mwrqtwdsds stdifchmmp fysydvphtc
      361 gpdpkiccqf dfkrlpggri ncpwkvppra iteanvadra allldqyrkk srlfrssvll
      421 vplgddfryd kpqewdaqff nyqrlfdfln skpefhvqaq fgtlseyfda lykrtgvepg
      481 arppgfpvls gdffsyadre dhywtgyyts rpfyksldrv lethlrgaev lyslalahar
      541 rsgltgqypl sdyavltear rtlglfqhhd aitgtakeav vvdygvrllr slvslkqvii
      601 naahylvlgd ketysfdpra pflqmddsrv shdalpertv irldssprfv vvfnpleqer
      661 lsvvsllvns prvrvlseeg qplsvqisvq wssatnmvpd vyqvsvpvrl palglgvlql
      721 qpdldgpytl qssvhvylng vklsvsrqtt fplrvvdsgt sdfaisnrym qvwfsgltgl
      781 lksvrrvdee qeqqvdmklf vygtrtskdk sgaylflpdn eakpyvpkkp pvlrvtegpf
      841 fsevaayyeh fhqvirlynl pgveglsldv sfqvdirdyv nkelalriht didsqgtfft
      901 dlngfqvqpr kylkklplqa nfypmpvmay iqdsqrrltl htaqalgvss lgngqlevil
      961 drrlmqddnr glgqglkdnk itcnhfrlll errtlmspep gffsklaamf rglifssnti
     1021 rnskvqqers tsypsllshm tsmylntppl vlpvakrest sptlhsfhpl asplpcdfhl
     1081 lnlrmlpaed tlpaadaali lhrkgfdcgl eaknlgfnct tsqgklalgs lfhgldvlfl
     1141 qptsltllyp laspsnstdi slepmeistf rlrlg
//
LOCUS       NP_001425067             551 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001425067 XP_063122834
VERSION     NP_001425067.1
DBSOURCE    REFSEQ: accession NM_001438138.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122834.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3156.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..551
                     /product="tubby-related protein 2 isoform 5"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=61405
     Region          28..>201
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          297..546
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..551
                     /gene="Tulp2"
                     /coded_by="NM_001438138.1:65..1720"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mnsgrktcvs lrtledefsg vrlqkleqqr qlfekkqrrk rqeplmvqan pdaslrhrrp
       61 rrgeerfqsd sswglgvgsp flqenvpqah lpsgahsalv tmsyvgdgsg erapllsprg
      121 avytrgngpa vrhlcwlpds sdsdveevtm edipvisrpp kthlanrrrg wlaspgpgis
      181 eeeevepkda rvedktpspd pdptensdrv hgdsascnme entakkniet asgigdedpe
      241 kkeatestet nnalvaskvl qgdgdtsnhs awnmtcpmpr tpgprlgedm eayvllpapr
      301 ehmvqcrivr nkhgvdkgmf psyylyleae dgvavrsspl ghfllagrkr krsktsnyli
      361 sldpkdmsrn gnnfvgkvrs nvlgtkftif dngvnperny wipdsarire elgvvcyetn
      421 vlgfrgprkm tvilpgmdsr kqrmkvqpqn dqdsilsrvq kgarhgllll qnkapswsde
      481 sgayvlnfhg rvtrasvknf qivhpdepdh lvlqfgrvap niftmdfryp lcplqafaic
      541 lssfdgklac e
//
LOCUS       NP_001425068             544 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001425068 XP_063122856
VERSION     NP_001425068.1
DBSOURCE    REFSEQ: accession NM_001438139.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122856.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3157.1,
                                           SRR26360181.498551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..544
                     /product="tubby-related protein 2 isoform 6"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=60709
     Region          28..>201
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          297..539
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..544
                     /gene="Tulp2"
                     /coded_by="NM_001438139.1:65..1699"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mnsgrktcvs lrtledefsg vrlqkleqqr qlfekkqrrk rqeplmvqan pdaslrhrrp
       61 rrgeerfqsd sswglgvgsp flqenvpqah lpsgahsalv tmsyvgdgsg erapllsprg
      121 avytrgngpa vrhlcwlpds sdsdveevtm edipvisrpp kthlanrrrg wlaspgpgis
      181 eeeevepkda rvedktpspd pdptensdrv hgdsascnme entakkniet asgigdedpe
      241 kkeatestet nnalvaskvl qgdgdtsnhs awnmtcpmpr tpgprlgedm eayvllpapr
      301 ehmvqcrivr nkhgvdkgmf psyylyleae dgvahfllag rkrkrsktsn ylisldpkdm
      361 srngnnfvgk vrsnvlgtkf tifdngvnpe rnywipdsar ireelgvvcy etnvlgfrgp
      421 rkmtvilpgm dsrkqrmkvq pqndqdsils rvqkgarhgl lllqnkapsw sdesgayvln
      481 fhgrvtrasv knfqivhpde pdhlvlqfgr vapniftmdf ryplcplqaf aiclssfdgk
      541 lace
//
LOCUS       NP_001425146             619 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425146
VERSION     NP_001425146.1
DBSOURCE    REFSEQ: accession NM_001438217.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.647744.1,
                                           SRR26360181.2991802.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438217.1:80..1939"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001009965             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001009965 XP_218945
VERSION     NP_001009965.2
DBSOURCE    REFSEQ: accession NM_001009965.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Nov 27, 2020 this sequence version replaced NP_001009965.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100644.1, SRR26643294.3232.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001009965.4:139..1200"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425126             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425126 XP_063118870
VERSION     NP_001425126.1
DBSOURCE    REFSEQ: accession NM_001438197.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063118870.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.1125364.1,
                                           SRR21887620.1723369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN12840116
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438197.1:416..1477"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425125             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425125
VERSION     NP_001425125.1
DBSOURCE    REFSEQ: accession NM_001438196.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1152350.1,
                                           SRR26643288.3317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438196.1:1271..2332"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425092             124 aa            linear   ROD 16-APR-2025
DEFINITION  mth938 domain-containing protein [Rattus norvegicus].
ACCESSION   NP_001425092 XP_006229830
VERSION     NP_001425092.1
DBSOURCE    REFSEQ: accession NM_001438163.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Ma,X., Ding,W., Wang,J., Wu,G., Zhang,H., Yin,J., Zhou,L. and Li,D.
  TITLE     LOC66273 isoform 2, a novel protein highly expressed in white
            adipose tissue, induces adipogenesis in 3T3-L1 cells
  JOURNAL   J Nutr 142 (3), 448-455 (2012)
   PUBMED   22279136
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Wang,H., Ma,X., Zhang,H., Zang,J., Hu,S. and Li,D.
  TITLE     Involvement of LOC66273 isoform 2, a novel Mth938 containing
            protein, in MAPK pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (4), 1241-1248 (2011)
   PUBMED   21622130
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229830.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CV797630.1, BI289587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840121, SAMN16676810
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..124
                     /product="mth938 domain-containing protein"
                     /calculated_mol_wt=13371
     Region          7..122
                     /region_name="Mth938"
                     /note="Mth938 domain. Mth938 is a hypothetical protein
                     encoded by the Methanobacterium thermoautotrophicum (Mth)
                     genome. This protein crystallizes as a dimer, although it
                     is monomeric in solution, with one disulfide bond in each
                     monomer. The function of the...; cd05126"
                     /db_xref="CDD:240162"
     CDS             1..124
                     /gene="Aamdc"
                     /gene_synonym="RGD1561459"
                     /coded_by="NM_001438163.1:90..464"
                     /db_xref="GeneID:361606"
                     /db_xref="RGD:1561459"
ORIGIN      
        1 mlmaspkias lswgqmkvqg stltykdckv wpggsrawdw retgtehspg vqpadvkeva
       61 ekgvqtlvig rgmsealkvp pstveylekq gidvrvlqte qavkeynala argirvggvf
      121 hstc
//
LOCUS       NP_001425075             450 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 10 [Rattus norvegicus].
ACCESSION   NP_001425075 XP_008757620
VERSION     NP_001425075.1
DBSOURCE    REFSEQ: accession NM_001438146.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757620.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2155698.1,
                                           SRR26360186.2519042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..450
                     /product="tubby-related protein 2 isoform 10"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=49829
     Region          196..445
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..450
                     /gene="Tulp2"
                     /coded_by="NM_001438146.1:315..1667"
                     /note="isoform 10 is encoded by transcript variant 13"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 msyvgdgsge rapllsprga vytrgngpav rhlcwlpdss dsdveevtme dipvisrppk
       61 thlanrrrgw laspgpgise eeevepkdar vedktpspdp dptensdrvh gdsascnmee
      121 ntakknieta sgigdedpek keatestetn nalvaskvlq gdgdtsnhsa wnmtcpmprt
      181 pgprlgedme ayvllpapre hmvqcrivrn khgvdkgmfp syylyleaed gvavrssplg
      241 hfllagrkrk rsktsnylis ldpkdmsrng nnfvgkvrsn vlgtkftifd ngvnpernyw
      301 ipdsariree lgvvcyetnv lgfrgprkmt vilpgmdsrk qrmkvqpqnd qdsilsrvqk
      361 garhgllllq nkapswsdes gayvlnfhgr vtrasvknfq ivhpdepdhl vlqfgrvapn
      421 iftmdfrypl cplqafaicl ssfdgklace
//
LOCUS       NP_001099789             748 aa            linear   ROD 16-APR-2025
DEFINITION  cysteine--tRNA ligase, cytoplasmic isoform 2 [Rattus norvegicus].
ACCESSION   NP_001099789 XP_001065753 XP_215134
VERSION     NP_001099789.1
DBSOURCE    REFSEQ: accession NM_001106319.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Liu,C., Gamper,H., Shtivelband,S., Hauenstein,S., Perona,J.J. and
            Hou,Y.M.
  TITLE     Kinetic quality control of anticodon recognition by a eukaryotic
            aminoacyl-tRNA synthetase
  JOURNAL   J Mol Biol 367 (4), 1063-1078 (2007)
   PUBMED   17303165
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Davidson,E., Caffarella,J., Vitseva,O., Hou,Y.M. and King,M.P.
  TITLE     Isolation of two cDNAs encoding functional human cytoplasmic
            cysteinyl-tRNA synthetase
  JOURNAL   Biol Chem 382 (3), 399-406 (2001)
   PUBMED   11347887
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Kim,J.E., Kim,K.H., Lee,S.W., Seol,W., Shiba,K. and Kim,S.
  TITLE     An elongation factor-associating domain is inserted into human
            cysteinyl-tRNA synthetase by alternative splicing
  JOURNAL   Nucleic Acids Res 28 (15), 2866-2872 (2000)
   PUBMED   10908348
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215134.3, XP_001065753.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.5215.1,
                                           SRR26643298.6165.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..748
                     /product="cysteine--tRNA ligase, cytoplasmic isoform 2"
                     /EC_number="6.1.1.16"
                     /note="cysteinyl-tRNA synthetase, cytoplasmic;
                     cysteine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=85463
     Region          1..745
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     CDS             1..748
                     /gene="Cars1"
                     /gene_synonym="Cars"
                     /coded_by="NM_001106319.2:51..2297"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293638"
                     /db_xref="RGD:1310747"
ORIGIN      
        1 magssaeqgk grrvqpqwsp pagtepcrlr lynsltrnkd vfipqdgkkv twyccgptvy
       61 dashmghars yisfdilrrv lrdyfqydvf ycmnitdidd kiirrarqny lfeqyreqkp
      121 saaqllkdvg damkpfsvkl settdpdkrq mleriqnsvk latepleqav hsnpsgeevd
      181 srvqvlleea kdllsdwlds tggsevtdns ifsklpkfwe eefhkdmeal nvlppdvltr
      241 vseyvpeivn fvqkivdngy gyasngsvyf dtakfaasek hsygklvpea vgdqkalqeg
      301 egdlsisadr lsekrspndf alwkaskpge pswpcpwgkg rpgwhiecsa magsllgasm
      361 dihgggfdlr fphhdnelaq seayfendcw vryflhtghl tiagckmsks lknfitikda
      421 lkkhsarqlr laflmhswkd tldyssntme salqyekfmn efflnvkdil rapvditgqf
      481 ekweaeevel nknfydkkta vhealcdnid trtvmeemra lvsqcnlyma arkaarrrpn
      541 ralleniamy lthmlkifga ieeenplgfp vggpgtnlnl estvmpylqv lsefregvrk
      601 iarekkvlev lqlsdalrdd ilpelgvrfe dheglptvvk lvdrdtllke keekkraeee
      661 krrkkeeaar kkqeqeaakl akmktppsem frsetdkysk fdenglpthd tegkelskgq
      721 tkklkklfea qekvykeylq qlqnsslq
//
LOCUS       NP_001425061             198 aa            linear   ROD 16-APR-2025
DEFINITION  transmembrane gamma-carboxyglutamic acid protein 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001425061
VERSION     NP_001425061.1
DBSOURCE    REFSEQ: accession NM_001438132.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.1676.1,
                                           SRR26643294.2327.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..198
                     /product="transmembrane gamma-carboxyglutamic acid protein
                     2 precursor"
                     /note="transmembrane gamma-carboxyglutamic acid protein 2;
                     proline-rich Gla (G-carboxyglutamic acid) polypeptide 2;
                     proline rich Gla (G-carboxyglutamic acid) 2"
                     /calculated_mol_wt=20455
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1892
     Region          33..96
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     CDS             1..198
                     /gene="Prrg2"
                     /coded_by="NM_001438132.1:213..809"
                     /db_xref="GeneID:361570"
                     /db_xref="RGD:1305444"
ORIGIN      
        1 mrshpslllv ymglatcldt lphreqsqvl difldapeaq sflvgrrrfp ranhwdlell
       61 tpgnlerecl eercsweear eyfedntlte rfwesyayng kggrgrvdva glavgltsgi
      121 llivlaglga fwylhyrrrr lrvqesclqe tgliiplspp tplspppppg lptyeqalaa
      181 sgvhdapppp ysslrrph
//
LOCUS       NP_001425148             619 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425148
VERSION     NP_001425148.1
DBSOURCE    REFSEQ: accession NM_001438219.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1937899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680422, SAMN06680425
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438219.1:1189..3048"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001425063             562 aa            linear   ROD 16-APR-2025
DEFINITION  tubby-related protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425063 XP_006229165
VERSION     NP_001425063.1
DBSOURCE    REFSEQ: accession NM_001438134.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229165.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3147.1,
                                           SRR26360181.2188588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..562
                     /product="tubby-related protein 2 isoform 1"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=62888
     Region          39..>212
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          308..557
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..562
                     /gene="Tulp2"
                     /coded_by="NM_001438134.1:16..1704"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mdregprgpr rgtsqeneqw kketledefs gvrlqkleqq rqlfekkqrr krqeplmvqa
       61 npdaslrhrr prrgeerfqs dsswglgvgs pflqenvpqa hlpsgahsal vtmsyvgdgs
      121 gerapllspr gavytrgngp avrhlcwlpd ssdsdveevt medipvisrp pkthlanrrr
      181 gwlaspgpgi seeeevepkd arvedktpsp dpdptensdr vhgdsascnm eentakknie
      241 tasgigdedp ekkeateste tnnalvaskv lqgdgdtsnh sawnmtcpmp rtpgprlged
      301 meayvllpap rehmvqcriv rnkhgvdkgm fpsyylylea edgvavrssp lghfllagrk
      361 rkrsktsnyl isldpkdmsr ngnnfvgkvr snvlgtkfti fdngvnpern ywipdsarir
      421 eelgvvcyet nvlgfrgprk mtvilpgmds rkqrmkvqpq ndqdsilsrv qkgarhglll
      481 lqnkapswsd esgayvlnfh grvtrasvkn fqivhpdepd hlvlqfgrva pniftmdfry
      541 plcplqafai clssfdgkla ff
//
LOCUS       NP_001425130             268 aa            linear   ROD 16-APR-2025
DEFINITION  tripartite motif-containing protein 5 isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001425130 XP_038934094
VERSION     NP_001425130.1
DBSOURCE    REFSEQ: accession NM_001438201.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Zurek,B., Schoultz,I., Neerincx,A., Napolitano,L.M., Birkner,K.,
            Bennek,E., Sellge,G., Lerm,M., Meroni,G., Soderholm,J.D. and
            Kufer,T.A.
  TITLE     TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal
            degradation
  JOURNAL   PLoS One 7 (7), e41255 (2012)
   PUBMED   22829933
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Pertel,T., Hausmann,S., Morger,D., Zuger,S., Guerra,J., Lascano,J.,
            Reinhard,C., Santoni,F.A., Uchil,P.D., Chatel,L., Bisiaux,A.,
            Albert,M.L., Strambio-De-Castillia,C., Mothes,W., Pizzato,M.,
            Grutter,M.G. and Luban,J.
  TITLE     TRIM5 is an innate immune sensor for the retrovirus capsid lattice
  JOURNAL   Nature 472 (7343), 361-365 (2011)
   PUBMED   21512573
REFERENCE   6  (residues 1 to 268)
  AUTHORS   O'Connor,C., Pertel,T., Gray,S., Robia,S.L., Bakowska,J.C.,
            Luban,J. and Campbell,E.M.
  TITLE     p62/sequestosome-1 associates with and sustains the expression of
            retroviral restriction factor TRIM5alpha
  JOURNAL   J Virol 84 (12), 5997-6006 (2010)
   PUBMED   20357094
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.3700.1,
                                           SRR26360190.2710764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..268
                     /product="tripartite motif-containing protein 5 isoform 5"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 5"
                     /calculated_mol_wt=30404
     Region          47..264
                     /region_name="SPRY_PRY_TRIM5"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     5 (TRIM5), also known as RING finger protein 88 (RNF88);
                     cd15822"
                     /db_xref="CDD:293994"
     CDS             1..268
                     /gene="Trim5"
                     /gene_synonym="RGD1304579"
                     /coded_by="NM_001438201.1:765..1571"
                     /note="isoform 5 is encoded by transcript variant 4"
                     /db_xref="GeneID:308906"
                     /db_xref="RGD:1304579"
ORIGIN      
        1 msilsrgven tikrshtfsm rkpktipkeq rrvfrapdlq gmlqvlqevt eaqrywvqvt
       61 lvesnnpnif itadkrqiry edhqarhfar ptenchagvl gypaiqsgkh ywevdvsgkg
      121 swvlglsdgs ylfnpifrsn aerppnpplf rlnlsndshs rlslsndshy qpkygfwvig
      181 lwgnsvynaf eectftgkps vltlslmvrp crvgifldca agtlsfynis nhgtliyrfc
      241 agsfpdrvfp yfnpmgssep lticwpds
//
LOCUS       NP_001014045             511 aa            linear   ROD 16-APR-2025
DEFINITION  tripartite motif-containing protein 5 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001014045 XP_219046
VERSION     NP_001014045.1
DBSOURCE    REFSEQ: accession NM_001014023.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Zurek,B., Schoultz,I., Neerincx,A., Napolitano,L.M., Birkner,K.,
            Bennek,E., Sellge,G., Lerm,M., Meroni,G., Soderholm,J.D. and
            Kufer,T.A.
  TITLE     TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal
            degradation
  JOURNAL   PLoS One 7 (7), e41255 (2012)
   PUBMED   22829933
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Pertel,T., Hausmann,S., Morger,D., Zuger,S., Guerra,J., Lascano,J.,
            Reinhard,C., Santoni,F.A., Uchil,P.D., Chatel,L., Bisiaux,A.,
            Albert,M.L., Strambio-De-Castillia,C., Mothes,W., Pizzato,M.,
            Grutter,M.G. and Luban,J.
  TITLE     TRIM5 is an innate immune sensor for the retrovirus capsid lattice
  JOURNAL   Nature 472 (7343), 361-365 (2011)
   PUBMED   21512573
REFERENCE   6  (residues 1 to 511)
  AUTHORS   O'Connor,C., Pertel,T., Gray,S., Robia,S.L., Bakowska,J.C.,
            Luban,J. and Campbell,E.M.
  TITLE     p62/sequestosome-1 associates with and sustains the expression of
            retroviral restriction factor TRIM5alpha
  JOURNAL   J Virol 84 (12), 5997-6006 (2010)
   PUBMED   20357094
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219046.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078926.1, SRR26643298.4371.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..511
                     /product="tripartite motif-containing protein 5 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 5"
                     /calculated_mol_wt=58928
     Region          8..78
                     /region_name="RING-HC_TRIM5-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and
                     similar proteins; cd16591"
                     /db_xref="CDD:438253"
     Site            order(16..17,19..20,56..57,59)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438253"
     Region          95..133
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          132..>233
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Region          290..507
                     /region_name="SPRY_PRY_TRIM5"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     5 (TRIM5), also known as RING finger protein 88 (RNF88);
                     cd15822"
                     /db_xref="CDD:293994"
     CDS             1..511
                     /gene="Trim5"
                     /gene_synonym="RGD1304579"
                     /coded_by="NM_001014023.2:107..1642"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308906"
                     /db_xref="RGD:1304579"
ORIGIN      
        1 masefvmnlk eevtcpicld lmvepvsgdc ghsfcqacit lnyesskcnq deficpvcrv
       61 sylfknlrpn rhvanivqrl kefksspeee pkvlscarhg eklqlfckkd mmpicwlcer
      121 sqehrghqtv lieevvqeyk eklqaalqkl madkkefenw kddlqkerty wqnqiqkdve
      181 nvqsefkgmr dimdseekke lqklmqeked imssleesen eysqqskllg dlildvehql
      241 qcsatemlqg ventikrsht fsmrkpktip keqrrvfrap dlqgmlqvlq evteaqrywv
      301 qvtlvesnnp nifitadkrq iryedhqarh farptencha gvlgypaiqs gkhywevdvs
      361 gkgswvlgls dgsylfnpif rsnaerppnp plfrlnlsnd shsrlslsnd shyqpkygfw
      421 viglwgnsvy nafeectftg kpsvltlslm vrpcrvgifl dcaagtlsfy nisnhgtliy
      481 rfcagsfpdr vfpyfnpmgs seplticwpd s
//
LOCUS       NP_001425151             630 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425151
VERSION     NP_001425151.1
DBSOURCE    REFSEQ: accession NM_001438222.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2732750.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..630
                     /product="zinc finger protein 668 isoform 2"
                     /calculated_mol_wt=69379
     Region          35..55
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(35,38,51,55)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          76..430
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          97..117
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          125..145
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(125,128,141,145)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(181,184,197,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,240,253,257)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(242,244,246,248..249,252..253,256,270,272,276..277,
                     280..281,284,298,300,302,304..305,308..309,312)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          259..609
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(529,532,545,549)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(534,536,538,540..541,544..545,548,562,564,568..569,
                     572..573,576,590,592,594,596..597,600..601,604)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          557..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          585..605
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..630
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438222.1:129..2021"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 mepregllte ameveaaeak spgpcykrsg rrykclfctk tfpnapraar haathtttdc
       61 teevnevqpk vdaepkaeea sgdkvsgsva kprpyacplc pkayktapel rshgrshtge
      121 kpfpcpecgr rfmqpvclrv hlashagelp frcthcpkay gtlsklkihq rghtgerpya
      181 ctdcgksfad psvfrkhrrt haglrpysce rcgkayaelk dlrnhersht gerpflcsec
      241 gksfsrsssl tchqrihaaq kpyrcpacgk gftqlssyqs herthsgekp flcprcgrmf
      301 sdpssfrrhq rahegvkpyr cekcgkdfrq padlamhrrv htgdrpfkcl qcdktfvasw
      361 dlkrhalvhs gqrpfrceec grafaerasl tkhsrmhsge rpfhcnacgk sfvvlsslrk
      421 herthrsnet tgaapqqelv lglalpvgvv gegsaapvag agigdapagl lglppesgsv
      481 vatqwqvvgm tvehvecqda gvgeapstlg dagevggeet dekppqfvcr ecketfstlt
      541 llrrhershp elrpfpctqc gksfsdragl rkhsrthssv rpyscsqcpk aflsasdlrk
      601 herthpvpig tpipleplva llgmpeegsa
//
LOCUS       NP_001425144             619 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425144 XP_017444705
VERSION     NP_001425144.1
DBSOURCE    REFSEQ: accession NM_001438215.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_017444705.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.848697.1,
                                           SRR26360194.145388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438215.1:1163..3022"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001425106             684 aa            linear   ROD 16-APR-2025
DEFINITION  cysteine--tRNA ligase, cytoplasmic isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425106 XP_038964041
VERSION     NP_001425106.1
DBSOURCE    REFSEQ: accession NM_001438177.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Liu,C., Gamper,H., Shtivelband,S., Hauenstein,S., Perona,J.J. and
            Hou,Y.M.
  TITLE     Kinetic quality control of anticodon recognition by a eukaryotic
            aminoacyl-tRNA synthetase
  JOURNAL   J Mol Biol 367 (4), 1063-1078 (2007)
   PUBMED   17303165
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Davidson,E., Caffarella,J., Vitseva,O., Hou,Y.M. and King,M.P.
  TITLE     Isolation of two cDNAs encoding functional human cytoplasmic
            cysteinyl-tRNA synthetase
  JOURNAL   Biol Chem 382 (3), 399-406 (2001)
   PUBMED   11347887
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Kim,J.E., Kim,K.H., Lee,S.W., Seol,W., Shiba,K. and Kim,S.
  TITLE     An elongation factor-associating domain is inserted into human
            cysteinyl-tRNA synthetase by alternative splicing
  JOURNAL   Nucleic Acids Res 28 (15), 2866-2872 (2000)
   PUBMED   10908348
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038964041.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.4061.1,
                                           SRR26643298.6168.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..684
                     /product="cysteine--tRNA ligase, cytoplasmic isoform 3"
                     /EC_number="6.1.1.16"
                     /note="cysteinyl-tRNA synthetase, cytoplasmic;
                     cysteine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=78340
     Region          1..681
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     CDS             1..684
                     /gene="Cars1"
                     /gene_synonym="Cars"
                     /coded_by="NM_001438177.1:224..2278"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:293638"
                     /db_xref="RGD:1310747"
ORIGIN      
        1 mgharsyisf dilrrvlrdy fqydvfycmn itdiddkiir rarqnylfeq yreqkpsaaq
       61 llkdvgdamk pfsvklsett dpdkrqmler iqnsvklate pleqavhsnp sgeevdsrvq
      121 vlleeakdll sdwldstggs evtdnsifsk lpkfweeefh kdmealnvlp pdvltrvsey
      181 vpeivnfvqk ivdngygyas ngsvyfdtak faasekhsyg klvpeavgdq kalqegegdl
      241 sisadrlsek rspndfalwk askpgepswp cpwgkgrpgw hiecsamags llgasmdihg
      301 ggfdlrfphh dnelaqseay fendcwvryf lhtghltiag ckmskslknf itikdalkkh
      361 sarqlrlafl mhswkdtldy ssntmesalq yekfmneffl nvkdilrapv ditgqfekwe
      421 aeevelnknf ydkktavhea lcdnidtrtv meemralvsq cnlymaarka arrrpnrall
      481 eniamylthm lkifgaieee nplgfpvggp gtnlnlestv mpylqvlsef regvrkiare
      541 kkvlevlqls dalrddilpe lgvrfedheg lptvvklvdr dtllkekeek kraeeekrrk
      601 keeaarkkqe qeaaklakmk tppsemfrse tdkyskfden glpthdtegk elskgqtkkl
      661 kklfeaqekv ykeylqqlqn sslq
//
LOCUS       NP_001425122             353 aa            linear   ROD 16-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425122 XP_006229823
VERSION     NP_001425122.1
DBSOURCE    REFSEQ: accession NM_001438193.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229823.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.3231.1,
                                           SRR26643291.2192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438193.1:238..1299"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001425113             685 aa            linear   ROD 16-APR-2025
DEFINITION  beta-taxilin [Rattus norvegicus].
ACCESSION   NP_001425113 XP_038968359
VERSION     NP_001425113.1
DBSOURCE    REFSEQ: accession NM_001438184.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_038968359.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.88.1, SRR26643295.108.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..685
                     /product="beta-taxilin"
                     /calculated_mol_wt=76826
     Region          146..453
                     /region_name="Taxilin"
                     /note="Myosin-like coiled-coil protein; pfam09728"
                     /db_xref="CDD:462861"
     Region          <527..677
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..685
                     /gene="Txlnb"
                     /gene_synonym="RGD1307979"
                     /coded_by="NM_001438184.1:125..2182"
                     /db_xref="GeneID:308622"
                     /db_xref="RGD:1307979"
ORIGIN      
        1 metnhpdqls veqpnppgds splnqnvpgk qdvqqsstsg qaaeqeasph pekgdhdise
       61 elsrqledii nmygsaaspt gkegtsetke qpqnteapdn edgdyeette etdreptape
      121 epatvkgpvs nkeqklekki lkglgkeanl lmqnlnklqa peekldflfk kyaelldehr
      181 teqkklklll kqqaqtqrek dqlqsehnra ilarsklesl crelqrhnkt lkeetlqrar
      241 eeeekrkeit shfqstltdi qtqieqqser nmklcqente laeklksiid qyelreehld
      301 kifkhrelqq klvdakleea qelmqeaeer hrrekeylln qaaewklqak vlkeqetvlq
      361 aqltlysgrf eefqstltks nevfatfkqe mdnttkkmkk lekdtatwka rfencnkall
      421 dmieekalra keyecfvmki qrlenlcral qeerkelykk irdakmseke dqvqhtsdee
      481 peskvsedkq mdveaangvq navknlataf ailhhpeftp dqsrerqpav ngppggsdlt
      541 hqhtepahln hpnpssvsgs pqppvgsqag seggceaapa ptacctpaea elqsqglsag
      601 nppdpkpqkp eakasgqvpl spaqgslavv eakcdispsp eserdpavvp gceskehppp
      661 evpdiplgpn tglprepdac lngve
//
LOCUS       NP_001425150             630 aa            linear   ROD 16-APR-2025
DEFINITION  zinc finger protein 668 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425150
VERSION     NP_001425150.1
DBSOURCE    REFSEQ: accession NM_001438221.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.570534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..630
                     /product="zinc finger protein 668 isoform 2"
                     /calculated_mol_wt=69379
     Region          35..55
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(35,38,51,55)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          76..430
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          97..117
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          125..145
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(125,128,141,145)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          153..173
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..201
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(181,184,197,201)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          209..229
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          237..257
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,240,253,257)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(242,244,246,248..249,252..253,256,270,272,276..277,
                     280..281,284,298,300,302,304..305,308..309,312)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          259..609
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          265..285
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          293..313
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          321..341
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..369
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          377..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(529,532,545,549)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(534,536,538,540..541,544..545,548,562,564,568..569,
                     572..573,576,590,592,594,596..597,600..601,604)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          557..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          585..605
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..630
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438221.1:641..2533"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 mepregllte ameveaaeak spgpcykrsg rrykclfctk tfpnapraar haathtttdc
       61 teevnevqpk vdaepkaeea sgdkvsgsva kprpyacplc pkayktapel rshgrshtge
      121 kpfpcpecgr rfmqpvclrv hlashagelp frcthcpkay gtlsklkihq rghtgerpya
      181 ctdcgksfad psvfrkhrrt haglrpysce rcgkayaelk dlrnhersht gerpflcsec
      241 gksfsrsssl tchqrihaaq kpyrcpacgk gftqlssyqs herthsgekp flcprcgrmf
      301 sdpssfrrhq rahegvkpyr cekcgkdfrq padlamhrrv htgdrpfkcl qcdktfvasw
      361 dlkrhalvhs gqrpfrceec grafaerasl tkhsrmhsge rpfhcnacgk sfvvlsslrk
      421 herthrsnet tgaapqqelv lglalpvgvv gegsaapvag agigdapagl lglppesgsv
      481 vatqwqvvgm tvehvecqda gvgeapstlg dagevggeet dekppqfvcr ecketfstlt
      541 llrrhershp elrpfpctqc gksfsdragl rkhsrthssv rpyscsqcpk aflsasdlrk
      601 herthpvpig tpipleplva llgmpeegsa
//
LOCUS       NP_001099827            1064 aa            linear   ROD 16-APR-2025
DEFINITION  structural maintenance of chromosomes protein 5 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001099827 XP_001078644 XP_215254
VERSION     NP_001099827.1
DBSOURCE    REFSEQ: accession NM_001106357.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Raschle,M., Smeenk,G., Hansen,R.K., Temu,T., Oka,Y., Hein,M.Y.,
            Nagaraj,N., Long,D.T., Walter,J.C., Hofmann,K., Storchova,Z.,
            Cox,J., Bekker-Jensen,S., Mailand,N. and Mann,M.
  TITLE     DNA repair. Proteomics reveals dynamic assembly of repair complexes
            during bypass of DNA cross-links
  JOURNAL   Science 348 (6234), 1253671 (2015)
   PUBMED   25931565
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Brouwer,A.K., Schimmel,J., Wiegant,J.C., Vertegaal,A.C., Tanke,H.J.
            and Dirks,R.W.
  TITLE     Telomeric DNA mediates de novo PML body formation
  JOURNAL   Mol Biol Cell 20 (22), 4804-4815 (2009)
   PUBMED   19793919
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Behlke-Steinert,S., Touat-Todeschini,L., Skoufias,D.A. and
            Margolis,R.L.
  TITLE     SMC5 and MMS21 are required for chromosome cohesion and mitotic
            progression
  JOURNAL   Cell Cycle 8 (14), 2211-2218 (2009)
   PUBMED   19502785
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Taylor,E.M., Copsey,A.C., Hudson,J.J., Vidot,S. and Lehmann,A.R.
  TITLE     Identification of the proteins, including MAGEG1, that make up the
            human SMC5-6 protein complex
  JOURNAL   Mol Cell Biol 28 (4), 1197-1206 (2008)
   PUBMED   18086888
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Potts,P.R. and Yu,H.
  TITLE     The SMC5/6 complex maintains telomere length in ALT cancer cells
            through SUMOylation of telomere-binding proteins
  JOURNAL   Nat Struct Mol Biol 14 (7), 581-590 (2007)
   PUBMED   17589526
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Potts,P.R., Porteus,M.H. and Yu,H.
  TITLE     Human SMC5/6 complex promotes sister chromatid homologous
            recombination by recruiting the SMC1/3 cohesin complex to
            double-strand breaks
  JOURNAL   EMBO J 25 (14), 3377-3388 (2006)
   PUBMED   16810316
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Taylor,E.M., Moghraby,J.S., Lees,J.H., Smit,B., Moens,P.B. and
            Lehmann,A.R.
  TITLE     Characterization of a novel human SMC heterodimer homologous to the
            Schizosaccharomyces pombe Rad18/Spr18 complex
  JOURNAL   Mol Biol Cell 12 (6), 1583-1594 (2001)
   PUBMED   11408570
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215254.4, XP_001078644.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1064
                     /product="structural maintenance of chromosomes protein 5
                     isoform 3"
                     /note="SMC5 structural maintenance of chromosomes 5-like
                     1; structural maintenance of chromosomes protein 5"
                     /calculated_mol_wt=124323
     Region          51..>196
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          53..1014
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            80..87
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213179"
     Site            178..181
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213179"
     Region          <937..1039
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            953..962
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213179"
     Site            977..982
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213179"
     Site            985..988
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213179"
     Site            1012..1018
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213179"
     CDS             1..1064
                     /gene="Smc5"
                     /gene_synonym="Smc5l1"
                     /coded_by="NM_001106357.2:66..3260"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:293967"
                     /db_xref="RGD:1307492"
ORIGIN      
        1 matpsgkaaa pnpqaskrsl prdassefps krknsnptst lprpsglfve gsivriamen
       61 fltydicevs pgphlnmiig angtgkssiv caiclglagk pafmgradkv gffvkrgcsk
      121 glveielfrt sgnliitrei dviknqsfwf inkkpvtqki veeqvaalni qvgnlcqflp
      181 qdkvgefakl skielleate ksigppemhr yhcelknfre kekqletsck ekteyldkmi
      241 qrnerykqdv erfyerkrhl dliemleakr pwveyenvrq eyegvklvrd rvkeevrklk
      301 egqipmtrri eeierqrrtl evrikekatd ikeasqkckq rqdlierkdr hikelqqalt
      361 vkqneeqdrq krisntrkmi edlqnelrta encenlqpqi daitndlrrv qeekalcege
      421 iidkqrekem lekqkrsvsd hitrfdnlmn qkedklrqry rdtydavlwl rnnrdrfkqr
      481 vcepimltvr dnkklrvnav iapkisyadk apsrslnelk qygffsylre lfdapdpvms
      541 ylccqyhihe vpvgtertre rierviqetr lkqiytaeek yvlktsfysn kvissntslk
      601 vaqfltvtvd leqrrhleeq lkeinrklea vdsglvalrd tnrhlelkdn elrlkkkell
      661 erktkkrqle qkissklasi rlmeqdtcnl eeeerkastk ikeinvqkak lvteltglvk
      721 ictslhiqkv dlilqnttvi seknkleady masssqlrvt eqqfielddn rqrllqkcke
      781 lmkrarqvcn lsadqavpqe fqtqvptipn ghsssppmaf qdlpntldei dallteersr
      841 ascftglnps vveeytkrei eiqqlteelk gkkveldeyr enisqvkerw lnplkelvek
      901 inekfsnffs smqcagevdl hteneedydk ygirirvkfr sstqlheltp hhqsggersv
      961 stmlylmalq elnrcpfrvv deinqgmdpi nerrvfemvv ntackentsq yffitpkllq
     1021 nlpysekmtv lfvyngphml epnrwnlkaf qrrrrritft qpsq
//
LOCUS       NP_001128441             713 aa            linear   ROD 16-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 6 [Rattus norvegicus].
ACCESSION   NP_001128441 XP_001056902 XP_575792
VERSION     NP_001128441.1
DBSOURCE    REFSEQ: accession NM_001134969.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Haribaskar,R., Putz,M., Schupp,B., Skouloudaki,K., Bietenbeck,A.,
            Walz,G. and Schafer,T.
  TITLE     The planar cell polarity (PCP) protein Diversin translocates to the
            nucleus to interact with the transcription factor AF9
  JOURNAL   Biochem Biophys Res Commun 387 (1), 212-217 (2009)
   PUBMED   19591803
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of rat Ankrd6 gene in silico
  JOURNAL   Int J Mol Med 15 (2), 359-363 (2005)
   PUBMED   15647854
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473962.1.
            
            On or before Sep 15, 2008 this sequence version replaced
            XP_001056902.1, XP_575792.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC168675.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..713
                     /product="ankyrin repeat domain-containing protein 6"
                     /calculated_mol_wt=77946
     Region          5..244
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(41,43,47..48,51..53,55..56,60,63,72,74,76,80..81,
                     84..86,88..89,93,96,105,107,109,113..114,117..119,
                     121..122,126,129,138)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          41..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          74..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          107..138
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          141..171
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(142,146..147,150..152,154..155,159,162,171,173,175,
                     179..180,183..185,187..188,192,195,204,206,208,212..213,
                     216..218,220..221,225,228,237)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          173..204
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..237
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <545..706
                     /region_name="PLN02847"
                     /note="triacylglycerol lipase"
                     /db_xref="CDD:178439"
     CDS             1..713
                     /gene="Ankrd6"
                     /coded_by="NM_001134969.1:356..2497"
                     /db_xref="GeneID:500430"
                     /db_xref="RGD:1583731"
ORIGIN      
        1 msqqdavaal serlliaayk gqtenvvqli nkgakvavtk hgrtplhlaa nkghlsvvqi
       61 llkagcdldv qddgdqtalh ratvvgntei ltaliregca ldrqdkdgnt alheaawhgf
      121 sqsakllvka ganvlarnka gntalhlacq nshsqstrvl llggsradlk nnagdtclhv
      181 aarynhlsvv rlllsafcsv heknqagdta lhvaaalnhk kvvkilleag adttlvnnag
      241 qtpletaryh dnpevalllt kapqilrfsr grslrkrrer lkeerraqsv prdevaqskg
      301 svsagdtpss eqavpekeea rrdcppasqe prkderrrks rpevsalsdp tpaadqqpgh
      361 qknlhghhhq kkksrhrcws pppphgfray qlytlyrged gkvmqapikg crceplinkl
      421 enqleaavee lraelgtvqd kvntklghme sksqhqmcvl dklmverlsa erteclnrlq
      481 qhaaaekqeg ekrqmslvde lkswcmlkiq nlelrlsges rtfrakstps psdsspavdq
      541 pvvaagpgaa sdsssqvvrp kdkalnatav prhqqellps dctgsglrkv kapaasrlgd
      601 qqtgscvnrg tqtkksargg qtkhrgqqpt asspsgqqps aassdardas qaleltqyff
      661 eavsaqmekw yerkieears qasqkaqqde atlkehirsl eeevaklrtk mhk
//
LOCUS       NP_001424947             287 aa            linear   ROD 16-APR-2025
DEFINITION  stomatin-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001424947
VERSION     NP_001424947.1
DBSOURCE    REFSEQ: accession NM_001438018.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Morgan,M., Thai,J., Nencini,S., Xu,J. and Ivanusic,J.J.
  TITLE     Stomatin-like protein 3 modulates the responses of Adelta, but not
            C fiber bone afferent neurons to noxious mechanical stimulation in
            an animal model of acute experimental bone pain
  JOURNAL   Mol Pain 19, 17448069231222407 (2023)
   PUBMED   38073226
  REMARK    GeneRIF: Stomatin-like protein 3 modulates the responses of Adelta,
            but not C fiber bone afferent neurons to noxious mechanical
            stimulation in an animal model of acute experimental bone pain.
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Tadenev,A.L., Kulaga,H.M., May-Simera,H.L., Kelley,M.W.,
            Katsanis,N. and Reed,R.R.
  TITLE     Loss of Bardet-Biedl syndrome protein-8 (BBS8) perturbs olfactory
            function, protein localization, and axon targeting
  JOURNAL   Proc Natl Acad Sci U S A 108 (25), 10320-10325 (2011)
   PUBMED   21646512
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wetzel,C., Hu,J., Riethmacher,D., Benckendorff,A., Harder,L.,
            Eilers,A., Moshourab,R., Kozlenkov,A., Labuz,D., Caspani,O.,
            Erdmann,B., Machelska,H., Heppenstall,P.A. and Lewin,G.R.
  TITLE     A stomatin-domain protein essential for touch sensation in the
            mouse
  JOURNAL   Nature 445 (7124), 206-209 (2007)
   PUBMED   17167420
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Kobayakawa,K., Hayashi,R., Morita,K., Miyamichi,K., Oka,Y.,
            Tsuboi,A. and Sakano,H.
  TITLE     Stomatin-related olfactory protein, SRO, specifically expressed in
            the murine olfactory sensory neurons
  JOURNAL   J Neurosci 22 (14), 5931-5937 (2002)
   PUBMED   12122055
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.166874.1,
                                           SRR26360176.1265322.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMN06621351 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..287
                     /product="stomatin-like protein 3"
                     /note="stomatin (Epb7.2)-like 3"
                     /calculated_mol_wt=31546
     Region          69..267
                     /region_name="SPFH_like"
                     /note="core domain of the SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cl19107"
                     /db_xref="CDD:473137"
     CDS             1..287
                     /gene="Stoml3"
                     /coded_by="NM_001438018.1:139..1002"
                     /db_xref="GeneID:295041"
                     /db_xref="RGD:1311090"
ORIGIN      
        1 mdspeklekn nlvgtnksrl gvcgwilffl sfllmlitfp vsiwmclkii keyeravvfr
       61 lgriqadkak gpglilvlpc idvfvkvdlr tvtcnippqe iltrdsvttq vdgvvyyriy
      121 savsavanvn dvhqatflla qttlrnvlgt qtlsqilsgr eeiahsiqtl lddatelwgi
      181 rvarveikdv ripvqlqrsm aaeaeatrea rakvlaaege mnaskslksa smvlaespia
      241 lqlrylqtlt tvateknsti vfplpmnile giggisydnn kkvtaka
//
LOCUS       NP_001424949             354 aa            linear   ROD 16-APR-2025
DEFINITION  leucine-rich repeat-containing protein 69 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424949 XP_017449058
VERSION     NP_001424949.1
DBSOURCE    REFSEQ: accession NM_001438020.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_017449058.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2174156.1,
                                           SRR26360186.2569048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..354
                     /product="leucine-rich repeat-containing protein 69
                     isoform 1"
                     /note="leucine-rich repeat-containing protein 69"
                     /calculated_mol_wt=40308
     Region          <15..>240
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          23..45
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          46..91
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          92..115
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          116..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          139..161
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          162..184
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          185..207
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..229
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..354
                     /gene="Lrrc69"
                     /coded_by="NM_001438020.1:19..1083"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500415"
                     /db_xref="RGD:1583733"
ORIGIN      
        1 mvtsskimte rllltalkgg kstkiltlng kkmskmpsal eklpnlrtld lqnnqiskvc
       61 pelrtltklt llnlgnnllq evpeeikylt slknlhlfgn ricriaagvl dglgdlvlln
      121 lndnqlsslp peigrlqnlt flslnhnklt vipkeicfle hlselhinyn ritripeeir
      181 flqnlqqlsl vrnnieelpe evcqltklgv ldvagnviqi fpagfqdlkl refycegnpl
      241 flknpifapq pkdlwtlrei aarfvlsqle eynplimdai ecypevkdkl skakkcaicr
      301 kpflsewlec vyfvppsknw kisknlqlip lqtlvcsyqc fdrrdpdvfg iake
//
LOCUS       NP_001020926             203 aa            linear   ROD 16-APR-2025
DEFINITION  uncharacterized protein LOC367620 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001020926 XP_006226732 XP_346230
VERSION     NP_001020926.1
DBSOURCE    REFSEQ: accession NM_001025755.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006226732.1, XP_346230.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, longest
                                      protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9"
     Protein         1..203
                     /product="uncharacterized protein LOC367620 isoform 1"
                     /calculated_mol_wt=24052
     Region          47..127
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..203
                     /gene="1700001E04Rikl"
                     /gene_synonym="RGD1563862"
                     /coded_by="NM_001025755.3:46..657"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:367620"
                     /db_xref="RGD:1560404"
ORIGIN      
        1 mfrqllrlfr kesgdqgett prqkeddlls sktgrrksfw grlgfgrkts sqnviseqek
       61 crkeleelkl eiqkckferd elyqildlyi yddwdlrldv elpilqsehe rrmmsmqmmt
      121 nsisdamery keliqanssy rirhsqllre qaqlknkiqi llnekreqlv eqtelpasyv
      181 eakrlceeag mnicvpsakq qqv
//
LOCUS       NP_445951                374 aa            linear   ROD 16-APR-2025
DEFINITION  transcription termination factor 1, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_445951
VERSION     NP_445951.2
DBSOURCE    REFSEQ: accession NM_053499.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Yakubovskaya,E., Mejia,E., Byrnes,J., Hambardjieva,E. and
            Garcia-Diaz,M.
  TITLE     Helix unwinding and base flipping enable human MTERF1 to terminate
            mitochondrial transcription
  JOURNAL   Cell 141 (6), 982-993 (2010)
   PUBMED   20550934
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Bogenhagen,D.F., Rousseau,D. and Burke,S.
  TITLE     The layered structure of human mitochondrial DNA nucleoids
  JOURNAL   J Biol Chem 283 (6), 3665-3675 (2008)
   PUBMED   18063578
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Li,X., Zhang,L.S. and Guan,M.X.
  TITLE     Cloning and characterization of mouse mTERF encoding a
            mitochondrial transcriptional termination factor
  JOURNAL   Biochem Biophys Res Commun 326 (2), 505-510 (2005)
   PUBMED   15582606
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Prieto-Martin,A., Montoya,J. and Martinez-Azorin,F.
  TITLE     Phosphorylation of rat mitochondrial transcription termination
            factor (mTERF) is required for transcription termination but not
            for binding to DNA
  JOURNAL   Nucleic Acids Res 32 (7), 2059-2068 (2004)
   PUBMED   15087485
  REMARK    GeneRIF: The DNA-binding activity of mTERF is unaffected by the
            phosphorylation or dephosphorylation state, however, only the
            phosphorylated form of the protein is active for termination
            activity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Enriquez,J.A., Fernandez-Silva,P., Garrido-Perez,N.,
            Lopez-Perez,M.J., Perez-Martos,A. and Montoya,J.
  TITLE     Direct regulation of mitochondrial RNA synthesis by thyroid hormone
  JOURNAL   Mol Cell Biol 19 (1), 657-670 (1999)
   PUBMED   9858589
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Aug 20, 2024 this sequence version replaced NP_445951.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ292524.1, SRR26360181.1434548.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q13"
     Protein         1..374
                     /product="transcription termination factor 1,
                     mitochondrial"
                     /function="mitochondrial transcription termination"
                     /note="transcription termination factor, mitochondrial"
                     /calculated_mol_wt=38428
     transit_peptide 1..37
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9EPI8.1)"
                     /calculated_mol_wt=4544
     mat_peptide     38..374
                     /product="transcription termination factor 1,
                     mitochondrial"
                     /calculated_mol_wt=38428
     Region          53..366
                     /region_name="mTERF"
                     /note="pfam02536"
                     /db_xref="CDD:460581"
     Site            139
                     /site_type="other"
                     /note="Interaction with DNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Region          146..147
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Site            179
                     /site_type="other"
                     /note="Interaction with DNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Region          224..228
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Region          301..308
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Site            327
                     /site_type="other"
                     /note="Interaction with DNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Region          332..335
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     Region          361..368
                     /region_name="Interaction with DNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPI8.1)"
     CDS             1..374
                     /gene="Mterf1"
                     /gene_synonym="Mterf"
                     /coded_by="NM_053499.2:295..1419"
                     /db_xref="GeneID:85261"
                     /db_xref="RGD:621318"
ORIGIN      
        1 masrniwrvr rnflfdlrgw vpqysaevfl ksisfrpfsv ecnskdgeng dllnnlltmg
       61 vdvdmarrrq pgvfnravtn eqelkmflls kgasdkvigs iisryprait rtpeslskrw
      121 dlwreimasd leivnilers pesffrsnnn lnlennikfl csvglthkcl crlltsaprt
      181 fsnslnlnkq mveflqetgi slghnnptdf vrkiisknps iliqstkrvk tnieflqstf
      241 nldkedllll icgpgarild lsndctkrny tnikkrllsl gcteeevqkf vlsylnmifl
      301 sekkfndkid clleekists qilenprvld ssihtlktri relahagydv stssiallsw
      361 sqrryeaklk rlsg
//
LOCUS       NP_001100962             389 aa            linear   ROD 16-APR-2025
DEFINITION  UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8
            [Rattus norvegicus].
ACCESSION   NP_001100962 XP_001069916 XP_218342
VERSION     NP_001100962.1
DBSOURCE    REFSEQ: accession NM_001107492.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ishida,H., Togayachi,A., Sakai,T., Iwai,T., Hiruma,T., Sato,T.,
            Okubo,R., Inaba,N., Kudo,T., Gotoh,M., Shoda,J., Tanaka,N. and
            Narimatsu,H.
  TITLE     A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which
            synthesizes poly-N-acetyllactosamine, is dramatically upregulated
            in colon cancer
  JOURNAL   FEBS Lett 579 (1), 71-78 (2005)
   PUBMED   15620693
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001069916.1, XP_218342.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB718954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMD00132308
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..389
                     /product="UDP-GlcNAc:betaGal
                     beta-1,3-N-acetylglucosaminyltransferase 8"
                     /note="UDP-Gal:betaGal beta 1,3-galactosyltransferase
                     polypeptide 7"
                     /calculated_mol_wt=43084
     Region          154..341
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..389
                     /gene="B3gnt8"
                     /gene_synonym="B3galt7"
                     /coded_by="NM_001107492.1:484..1653"
                     /db_xref="GeneID:308440"
                     /db_xref="RGD:1305374"
ORIGIN      
        1 mrcrkcqlcl salltllglk vyiewtsesw lkkaeprgal psptppsaep tlptnlsarl
       61 gqtgplssay wnqqqrqlgv lpssdcqtwg svaaseildf ilypqdlrrf llsaacrsfp
      121 lwlpagegsp vascsdkdvp ylllavksep ghfaarqavr etwgspvagt rllfllgspl
      181 gmggpdltsl vtwesrrygd lllwdfldvp ynrtlkdlll ltwlshhcpk vsfvlqvqdn
      241 afvhipalle hlqalpptwa rslylgevft qakplrkpgg pfyvpktffe gdypayasgg
      301 gyvisgrlap wllqaaarva pfpfddvytg fcfralglap rahpgfltaw paertrdpca
      361 vrglllvhpv spqdtiwlwr hlwvpelrc
//
LOCUS       NP_001424912             358 aa            linear   ROD 16-APR-2025
DEFINITION  G-protein coupled receptor 87 [Rattus norvegicus].
ACCESSION   NP_001424912 XP_063137857
VERSION     NP_001424912.1
DBSOURCE    REFSEQ: accession NM_001437983.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063137857.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.9075.1,
                                           SRR26643294.8887.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN13663597,
                                           SAMN13663603 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..358
                     /product="G-protein coupled receptor 87"
                     /calculated_mol_wt=41265
     Region          43..325
                     /region_name="7tmA_GPR87"
                     /note="G protein-coupled receptor 87, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15969"
                     /db_xref="CDD:320635"
     Region          43..70
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320635"
     Region          76..101
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320635"
     Site            order(110,114,118..119,122..123,126,169,172..173,176,180,
                     191..192,196,204,207..208,211,272,275,279,296)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320635"
     Region          114..144
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320635"
     Region          156..178
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320635"
     Region          203..232
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320635"
     Region          245..275
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320635"
     Region          293..318
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320635"
     CDS             1..358
                     /gene="Gpr87"
                     /coded_by="NM_001437983.1:328..1404"
                     /db_xref="GeneID:310443"
                     /db_xref="RGD:1307852"
ORIGIN      
        1 mglnltlakl pgnelysqas htanstiegh gknsthhnef dtiilpvlyl vifvasilln
       61 glavwiffhi rnktsfifyl knivvadlim tltfpfrivr dagfgpwyfe filcrytsvl
      121 fyanmytsiv flglisvdry lkvvkpfgds rmysitftkv lsicvwvima vlslpniilt
      181 ngqptkenih dcmklksplg akwdmavtyv dsclfvavlv iligcyiais ryihkssrqf
      241 isqssrkrkh nqsirvvvav fftcflpyhl cripftfshl drllddsahk ilhyckemtl
      301 flsacnvcld piiyffmcks fsrrlfkksn irtrsesirs lqsvrrsevr iyydytdv
//
LOCUS       NP_001424937             681 aa            linear   ROD 16-APR-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424937 XP_063144260
VERSION     NP_001424937.1
DBSOURCE    REFSEQ: accession NM_001438008.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Rohacek,A.M., Bebee,T.W., Tilton,R.K., Radens,C.M.,
            McDermott-Roe,C., Peart,N., Kaur,M., Zaykaner,M., Cieply,B.,
            Musunuru,K., Barash,Y., Germiller,J.A., Krantz,I.D., Carstens,R.P.
            and Epstein,D.J.
  TITLE     ESRP1 Mutations Cause Hearing Loss due to Defects in Alternative
            Splicing that Disrupt Cochlear Development
  JOURNAL   Dev Cell 43 (3), 318-331 (2017)
   PUBMED   29107558
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Lekva,T., Berg,J.P., Lyle,R., Heck,A., Ringstad,G., Olstad,O.K.,
            Michelsen,A.E., Casar-Borota,O., Bollerslev,J. and Ueland,T.
  TITLE     Epithelial splicing regulator protein 1 and alternative splicing in
            somatotroph adenomas
  JOURNAL   Endocrinology 154 (9), 3331-3343 (2013)
   PUBMED   23825128
  REMARK    GeneRIF: Data suggest that alternative splicing in ESRP1
            transcripts in somatotroph adenoma cells is essential in
            epithelial-mesenchymal transition progression and in response to
            somatostatin analog antineoplastic treatment.
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 14, 2025 this sequence version replaced XP_063144260.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.18270.1,
                                           SRR22582416.813213.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..681
                     /product="epithelial splicing regulatory protein 1 isoform
                     1"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=75375
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          310..420
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Site            582
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NXG1; propagated from
                     UniProtKB/Swiss-Prot (B2RYD2.2)"
     Region          633..>672
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..681
                     /gene="Esrp1"
                     /gene_synonym="RGD1560481"
                     /coded_by="NM_001438008.1:375..2420"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500409"
                     /db_xref="RGD:1560481"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illlwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki daenlssapq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdldkldvaa maeslnfekn dsmsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcsktel idgntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptapii pvlpqqfvpp tnvrdcvrlr glpyaatied ildflgefst dirthgvhmv
      481 lnhqgrpsgd afiqmkstdr afmaaqkyhk ktmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppcklp clsppsytfp apaaviptea aiyqpsllln pralqpstay ypagtqlfmn
      601 ytayypsppg spnslgyfpt aanlssvppq pgtvvrmqgl ayntgvkeil nffqgyqyat
      661 edglvhtndq artlpkewvc i
//
LOCUS       NP_001425254             290 aa            linear   ROD 17-APR-2025
DEFINITION  START domain-containing protein 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425254
VERSION     NP_001425254.1
DBSOURCE    REFSEQ: accession NM_001438325.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ito,M., Yamanashi,Y., Toyoda,Y., Izumi-Nakaseko,H., Oda,S.,
            Sugiyama,A., Kuroda,M., Suzuki,H., Takada,T. and Adachi-Akahane,S.
  TITLE     Disruption of Stard10 gene alters the PPARalpha-mediated bile acid
            homeostasis
  JOURNAL   Biochim Biophys Acta 1831 (2), 459-468 (2013)
   PUBMED   23200860
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.232791.1, EV780436.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..290
                     /product="START domain-containing protein 10 isoform 1"
                     /note="START domain containing 10; PCTP-like protein;
                     StAR-related lipid transfer (START) domain containing 10;
                     START domain-containing protein 10"
                     /calculated_mol_wt=32773
     Region          19..241
                     /region_name="START_STARD10-like"
                     /note="Lipid-binding START domain of mammalian STARD10 and
                     related proteins; cd08871"
                     /db_xref="CDD:176880"
     Site            order(46..47,54,68,70,82,86,92,95..96,98..99,118,120..123,
                     125,128,130,132,147,164,166..169,171,183,185,187,189,191,
                     193,200,202..204,206..208,211..212,215)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176880"
     CDS             1..290
                     /gene="Stard10"
                     /coded_by="NM_001438325.1:437..1309"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:293150"
                     /db_xref="RGD:1306548"
ORIGIN      
        1 mekpaastep qgprpalgre svqvpddqdf rsfrseceae vgwnltyska gvsvwvqave
       61 mdrtlhkikc rmeccdvpae tlydvlhdie yrkkwdsnvi etfdiarltv nadvgyyswr
      121 cpkplknrdv itlrswlpmg adyiimnysv khpkypprkd lvravsiqtg yliqstgpks
      181 cvitylaqvd pkgslpkwvv nkssqflapk amkkmykaci kypewkqkhq phfkpwlhpe
      241 qsplpslals elsvqhadsl enidesavte sreeraggag egsdddtslt
//
LOCUS       NP_001425188            1173 aa            linear   ROD 17-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425188 XP_063138859
VERSION     NP_001425188.1
DBSOURCE    REFSEQ: accession NM_001438259.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138859.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2637327.1,
                                           SRR26643293.9502.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1173
                     /product="tudor domain-containing protein 1 isoform 1"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=129863
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1052
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     Site            order(994,999,1001,1017,1020,1022)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410449"
     CDS             1..1173
                     /gene="Tdrd1"
                     /coded_by="NM_001438259.1:313..3834"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnddfw yraivleasd sdvkvlyady
     1021 gnverlpfsr vqpitashlq lpfriircsl egltelngss sqpvmellrn amlnqsvals
     1081 vkavsknvha vsvekcseng miniaenlvm cglaenlssk resastketp hstdccctel
     1141 qkqiekheqi llfllnnptn qnkfiemkkl lqs
//
LOCUS       NP_001425193             541 aa            linear   ROD 17-APR-2025
DEFINITION  probable tubulin polyglutamylase TTLL2 [Rattus norvegicus].
ACCESSION   NP_001425193 XP_008756973
VERSION     NP_001425193.1
DBSOURCE    REFSEQ: accession NM_001438264.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_008756973.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.452650.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..541
                     /product="probable tubulin polyglutamylase TTLL2"
                     /note="tubulin tyrosine ligase-like family, member 2"
                     /calculated_mol_wt=61829
     Region          98..371
                     /region_name="TTL"
                     /note="Tubulin-tyrosine ligase family; pfam03133"
                     /db_xref="CDD:397308"
     CDS             1..541
                     /gene="Ttll2"
                     /coded_by="NM_001438264.1:176..1801"
                     /db_xref="GeneID:292311"
                     /db_xref="RGD:1305200"
ORIGIN      
        1 mmnglqtlgd vtaeifrlsp egntvqkrqr lrmedeapga alkplvfrvd estpgvvqsv
       61 llergwdkfd eqcqdvedwn lywrsssfrm aeyvnikpwq rlnhhpgtts ltrkdclakh
      121 lahmrrlyge siyeftpltf impsdytkfv akyfkekqdl gtkpsywick paklsqgrgi
      181 iifsdirdlm fkdayvvqky icnpllvgry kcdlriyvcv tgfkpltiym yqeglvrfat
      241 ekfdlsnled yyshltnssi nklgasyeki kevvgqgckw tlsrffsylr nwdvddlllr
      301 rkinhmvilt vlamapsvpv anncfelfgf diliddnlkp wllevnyspa lslecstdvs
      361 vkrslvhdii ellylnglrs eekkcgrtsq gnamvsqarr sqqklcaapa ppsyasliqf
      421 atcskrspaa qhmcpkhtrt sqlremlcrq nklltreaak skprlkawhs prkmlslcas
      481 qslprktkgp tgilpeagnt pnnhagnfvl ifpfnkatfs asrnglnvkr iiqelqklmn
      541 k
//
LOCUS       NP_001425248             526 aa            linear   ROD 17-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 7
            [Rattus norvegicus].
ACCESSION   NP_001425248 XP_063140777
VERSION     NP_001425248.1
DBSOURCE    REFSEQ: accession NM_001438319.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063140777.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.973839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..526
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 7"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=58141
     Region          1..306
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          308..380
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          391..474
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          468..523
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..526
                     /gene="Cpeb1"
                     /coded_by="NM_001438319.1:99..1679"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 mafsleeesg rikdcwdnqe vpalstcsna nifrrinail ddsldfskvc ttpinrgihd
       61 qlpdfqdsee aitsrmlfpt saqesprglp danglclglq slsltgwdrp wstqdsdssa
      121 qsntqsvlsm lqnplgnvlg ktplsflsld plgsdldkfp apsvrgsrld trpildsrss
      181 spsdsdtsgf ssgsdhlsdl isslrisppl pflsmtgngp rdplkmgvgs rmdqeqaala
      241 avapsptsap krwpgtsvwp swdllgapkd pfsierearl hrqaaavnea tctwsgqlpp
      301 rnyknpiysc kvflggvpwd itegyvylvf eleksvrall qacshdplsp dglseyyfkm
      361 ssrrmrckev qvipwvlads nfvwspsqrl dpsrtvfvga lhgmlnaeal aailndlfgg
      421 vvyagidtdk hkypigsgrv tfnnqrsylk avtaafveik ttkftkkvqi dpyledslcl
      481 icssqpgpff crdqvcfkyf crscwhwrhs meglrhhspl mrnqkn
//
LOCUS       NP_001425185             353 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 5 [Rattus norvegicus].
ACCESSION   NP_001425185
VERSION     NP_001425185.1
DBSOURCE    REFSEQ: accession NM_001438256.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.494.1, SRR26643290.406.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..353
                     /product="methionine synthase reductase isoform 5"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=39527
     Region          2..352
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(105..108,123..124,141..144,179,352)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(105,107..108)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(108,305,350,352)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(125..128,199,201,234..235,264..265,279,281,311)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(141,144,147)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(196,200..203,205)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..353
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438256.1:817..1878"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 mdtkkkgasl pqhvpegssl qfiftwclei ravpkkaflr alsdytsdat ekrrlqelcs
       61 kqgaadynrf irdasvclld llltfpscqp plnlllehlp klqprpysca sssllhpdkl
      121 hfvfnivelp snttaaslrk gvctgwlatl vapflqpnte vltadhsdal apeilispra
      181 tnsfhlpddl sapiimvgpg tgvapfvgfl qhreklqeqh pdgnfgamwl ffgcrhkdrd
      241 ylfreelrhf lktgvlthlk vsfsrdaape eeeeapakyv qdnlqhhsqq vartllqeng
      301 yiyvcgdakn makdvhdalv eiiskeagvd kleamktlat lkqekrylqd iws
//
LOCUS       NP_001425189            1150 aa            linear   ROD 17-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425189 XP_063138861
VERSION     NP_001425189.1
DBSOURCE    REFSEQ: accession NM_001438260.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138861.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1978067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1150
                     /product="tudor domain-containing protein 1 isoform 2"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=127190
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1029
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     CDS             1..1150
                     /gene="Tdrd1"
                     /coded_by="NM_001438260.1:149..3601"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnygnv erlpfsrvqp itashlqlpf
     1021 riircslegl telngsssqp vmellrnaml nqsvalsvka vsknvhavsv ekcsengmin
     1081 iaenlvmcgl aenlsskres astketphst dccctelqkq iekheqillf llnnptnqnk
     1141 fiemkkllqs
//
LOCUS       NP_001425249             481 aa            linear   ROD 17-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 8
            [Rattus norvegicus].
ACCESSION   NP_001425249
VERSION     NP_001425249.1
DBSOURCE    REFSEQ: accession NM_001438320.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 481)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 481)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.276718.1,
                                           SRR26360176.1873699.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..481
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 8"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=52945
     Region          <1..231
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          233..335
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          346..429
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          423..478
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..481
                     /gene="Cpeb1"
                     /coded_by="NM_001438320.1:414..1859"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 mlfptsaqes prglpdangl clglqslslt gwdrpwstqd sdssaqsntq svlsmlqnpl
       61 gnvlgktpls flsldplgsd ldkfpapsvr gsrldtrpil dsrssspsds dtsgfssgsd
      121 hlsdlisslr ispplpflsm tgngprdplk mgvgsrmdqe qaalaavaps ptsapkrwpg
      181 tsvwpswdll gapkdpfsie rearlhrqaa avneatctws gqlpprnykn piysckvflg
      241 gvpwditeag lvntfrvfgs lsvewpgkdg khprcppkgy vylvfeleks vrallqacsh
      301 dplspdglse yyfkmssrrm rckevqvipw vladsnfvws psqrldpsrt vfvgalhgml
      361 naealaailn dlfggvvyag idtdkhkypi gsgrvtfnnq rsylkavtaa fveikttkft
      421 kkvqidpyle dslclicssq pgpffcrdqv cfkyfcrscw hwrhsmeglr hhsplmrnqk
      481 n
//
LOCUS       NP_001008304             281 aa            linear   ROD 17-APR-2025
DEFINITION  U1 small nuclear ribonucleoprotein A [Rattus norvegicus].
ACCESSION   NP_001008304 XP_214845
VERSION     NP_001008304.1
DBSOURCE    REFSEQ: accession NM_001008303.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kondo,Y., Oubridge,C., van Roon,A.M. and Nagai,K.
  TITLE     Crystal structure of human U1 snRNP, a small nuclear
            ribonucleoprotein particle, reveals the mechanism of 5' splice site
            recognition
  JOURNAL   Elife 4, e04986 (2015)
   PUBMED   25555158
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Bai,B., Hales,C.M., Chen,P.C., Gozal,Y., Dammer,E.B., Fritz,J.J.,
            Wang,X., Xia,Q., Duong,D.M., Street,C., Cantero,G., Cheng,D.,
            Jones,D.R., Wu,Z., Li,Y., Diner,I., Heilman,C.J., Rees,H.D., Wu,H.,
            Lin,L., Szulwach,K.E., Gearing,M., Mufson,E.J., Bennett,D.A.,
            Montine,T.J., Seyfried,N.T., Wingo,T.S., Sun,Y.E., Jin,P.,
            Hanfelt,J., Willcock,D.M., Levey,A., Lah,J.J. and Peng,J.
  TITLE     U1 small nuclear ribonucleoprotein complex and RNA splicing
            alterations in Alzheimer's disease
  JOURNAL   Proc Natl Acad Sci U S A 110 (41), 16562-16567 (2013)
   PUBMED   24023061
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Pabis,M., Neufeld,N., Steiner,M.C., Bojic,T., Shav-Tal,Y. and
            Neugebauer,K.M.
  TITLE     The nuclear cap-binding complex interacts with the U4/U6.U5
            tri-snRNP and promotes spliceosome assembly in mammalian cells
  JOURNAL   RNA 19 (8), 1054-1063 (2013)
   PUBMED   23793891
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Zhang,L., Li,X. and Zhao,R.
  TITLE     Structural analyses of the pre-mRNA splicing machinery
  JOURNAL   Protein Sci 22 (6), 677-692 (2013)
   PUBMED   23592432
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Novakova,Z., Man,P., Novak,P., Hozak,P. and Hodny,Z.
  TITLE     Separation of nuclear protein complexes by blue native
            polyacrylamide gel electrophoresis
  JOURNAL   Electrophoresis 27 (7), 1277-1287 (2006)
   PUBMED   16502463
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Sinha,K., Perumal,K., Chen,Y. and Reddy,R.
  TITLE     Post-transcriptional adenylation of signal recognition particle RNA
            is carried out by an enzyme different from mRNA Poly(A) polymerase
  JOURNAL   J Biol Chem 274 (43), 30826-30831 (1999)
   PUBMED   10521474
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Nagai,K., Oubridge,C., Jessen,T.H., Li,J. and Evans,P.R.
  TITLE     Crystal structure of the RNA-binding domain of the U1 small nuclear
            ribonucleoprotein A
  JOURNAL   Nature 348 (6301), 515-520 (1990)
   PUBMED   2147232
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Craft,J., Mimori,T., Olsen,T.L. and Hardin,J.A.
  TITLE     The U2 small nuclear ribonucleoprotein particle as an autoantigen.
            Analysis with sera from patients with overlap syndromes
  JOURNAL   J Clin Invest 81 (6), 1716-1724 (1988)
   PUBMED   2968364
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 16, 2004 this sequence version replaced XP_214845.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086331.1, SRR22399484.1559719.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840110 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..281
                     /product="U1 small nuclear ribonucleoprotein A"
                     /calculated_mol_wt=31045
     Region          7..95
                     /region_name="RRM1_U1A"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1A); cd12477"
                     /db_xref="CDD:409906"
     Region          <12..>207
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Site            order(13,15..16,19,44,46,48..54,56,80,83,85..92)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409906"
     Region          196..281
                     /region_name="RRM2_U1A"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A
                     or U1A); cd12480"
                     /db_xref="CDD:409908"
     CDS             1..281
                     /gene="Snrpa"
                     /coded_by="NM_001008303.2:201..1046"
                     /db_xref="GeneID:292729"
                     /db_xref="RGD:1307416"
ORIGIN      
        1 mavpetrpnh tiyinnlnek ikkdelkksl yaifsqfgqi ldilvsrslk mrgqafvifk
       61 evssatnalr smqgfpfydk pmriqyaktd sdiiakmkgt fverdrkrek rkpksqetpa
      121 akkavqggaa apvvgavqpv pgmppmtqap rimhhmpgqp pympppgmip ppglapgqip
      181 pgamppqqlm pgqmppaqpl senppnhilf ltnlpeetne lmlsmlfnqf pgfkevrlvp
      241 grhdiafvef dnevqagaar dalqgfkitq nnamkisfak k
//
LOCUS       NP_001425229             110 aa            linear   ROD 17-APR-2025
DEFINITION  small ribosomal subunit protein uS12m isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425229
VERSION     NP_001425229.1
DBSOURCE    REFSEQ: accession NM_001438300.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2312969.1,
                                           SRR26360176.412975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..110
                     /product="small ribosomal subunit protein uS12m isoform 2"
                     /note="28S ribosomal protein S12, mitochondrial; small
                     ribosomal subunit protein uS12m"
                     /calculated_mol_wt=12206
     Region          3..109
                     /region_name="Ribosomal_S12"
                     /note="S12-like family, 30S ribosomal protein S12
                     subfamily; S12 is located at the interface of the large
                     and small ribosomal subunits of prokaryotes, chloroplasts
                     and mitochondria, where it plays an important role in both
                     tRNA and ribosomal subunit...; cd03368"
                     /db_xref="CDD:239466"
     Site            order(4..5,7..8,11..12)
                     /site_type="other"
                     /note="S17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239466"
     Site            4
                     /site_type="active"
                     /note="S8 interaction site [active]"
                     /db_xref="CDD:239466"
     Site            order(12..14,25,27..28,30,45..46,48..50,57,65,68..69,
                     82..83,87..88,109)
                     /site_type="other"
                     /note="16S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(42..43,87)
                     /site_type="other"
                     /note="streptomycin interaction site [chemical binding]"
                     /db_xref="CDD:239466"
     Site            43..44
                     /site_type="other"
                     /note="23S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(44..49,69..77)
                     /site_type="other"
                     /note="aminoacyl-tRNA interaction site (A-site)
                     [nucleotide binding]"
                     /db_xref="CDD:239466"
     CDS             1..110
                     /gene="Mrps12"
                     /coded_by="NM_001438300.1:58..390"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:292758"
                     /db_xref="RGD:1306221"
ORIGIN      
        1 matlnqmhrl grpkeppkrl gptegrpqlk gvvlrtfirk pkkpnsanrk ccrvrlstgk
       61 eavcfipgeg htlqehhvvl veggrtqdlp gvklkvvrgk ydcghvqkkk
//
LOCUS       NP_001425190            1150 aa            linear   ROD 17-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425190 XP_063138862
VERSION     NP_001425190.1
DBSOURCE    REFSEQ: accession NM_001438261.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138862.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.9497.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1150
                     /product="tudor domain-containing protein 1 isoform 2"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=127190
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1029
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     CDS             1..1150
                     /gene="Tdrd1"
                     /coded_by="NM_001438261.1:86..3538"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnygnv erlpfsrvqp itashlqlpf
     1021 riircslegl telngsssqp vmellrnaml nqsvalsvka vsknvhavsv ekcsengmin
     1081 iaenlvmcgl aenlsskres astketphst dccctelqkq iekheqillf llnnptnqnk
     1141 fiemkkllqs
//
LOCUS       NP_001425228             139 aa            linear   ROD 17-APR-2025
DEFINITION  small ribosomal subunit protein uS12m isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425228 XP_006228713
VERSION     NP_001425228.1
DBSOURCE    REFSEQ: accession NM_001438299.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228713.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM065363.1, SRR26643289.1327.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840109
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..139
                     /product="small ribosomal subunit protein uS12m isoform 1"
                     /note="28S ribosomal protein S12, mitochondrial; small
                     ribosomal subunit protein uS12m"
                     /calculated_mol_wt=15310
     Region          32..138
                     /region_name="Ribosomal_S12"
                     /note="S12-like family, 30S ribosomal protein S12
                     subfamily; S12 is located at the interface of the large
                     and small ribosomal subunits of prokaryotes, chloroplasts
                     and mitochondria, where it plays an important role in both
                     tRNA and ribosomal subunit...; cd03368"
                     /db_xref="CDD:239466"
     Site            order(33..34,36..37,40..41)
                     /site_type="other"
                     /note="S17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239466"
     Site            33
                     /site_type="active"
                     /note="S8 interaction site [active]"
                     /db_xref="CDD:239466"
     Site            order(41..43,54,56..57,59,74..75,77..79,86,94,97..98,
                     111..112,116..117,138)
                     /site_type="other"
                     /note="16S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(71..72,116)
                     /site_type="other"
                     /note="streptomycin interaction site [chemical binding]"
                     /db_xref="CDD:239466"
     Site            72..73
                     /site_type="other"
                     /note="23S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(73..78,98..106)
                     /site_type="other"
                     /note="aminoacyl-tRNA interaction site (A-site)
                     [nucleotide binding]"
                     /db_xref="CDD:239466"
     CDS             1..139
                     /gene="Mrps12"
                     /coded_by="NM_001438299.1:159..578"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:292758"
                     /db_xref="RGD:1306221"
ORIGIN      
        1 mswpgllhgl ttslsrglal apqlwatrsm atlnqmhrlg rpkeppkrlg ptegrpqlkg
       61 vvlrtfirkp kkpnsanrkc crvrlstgke avcfipgegh tlqehhvvlv eggrtqdlpg
      121 vklkvvrgky dcghvqkkk
//
LOCUS       NP_001013087             290 aa            linear   ROD 17-APR-2025
DEFINITION  START domain-containing protein 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001013087 XP_215005
VERSION     NP_001013087.1
DBSOURCE    REFSEQ: accession NM_001013069.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ito,M., Yamanashi,Y., Toyoda,Y., Izumi-Nakaseko,H., Oda,S.,
            Sugiyama,A., Kuroda,M., Suzuki,H., Takada,T. and Adachi-Akahane,S.
  TITLE     Disruption of Stard10 gene alters the PPARalpha-mediated bile acid
            homeostasis
  JOURNAL   Biochim Biophys Acta 1831 (2), 459-468 (2013)
   PUBMED   23200860
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215005.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091411.1, SRR22582416.160633.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..290
                     /product="START domain-containing protein 10 isoform 1"
                     /note="START domain containing 10; PCTP-like protein;
                     StAR-related lipid transfer (START) domain containing 10;
                     START domain-containing protein 10"
                     /calculated_mol_wt=32773
     Region          19..241
                     /region_name="START_STARD10-like"
                     /note="Lipid-binding START domain of mammalian STARD10 and
                     related proteins; cd08871"
                     /db_xref="CDD:176880"
     Site            order(46..47,54,68,70,82,86,92,95..96,98..99,118,120..123,
                     125,128,130,132,147,164,166..169,171,183,185,187,189,191,
                     193,200,202..204,206..208,211..212,215)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176880"
     CDS             1..290
                     /gene="Stard10"
                     /coded_by="NM_001013069.2:280..1152"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:293150"
                     /db_xref="RGD:1306548"
ORIGIN      
        1 mekpaastep qgprpalgre svqvpddqdf rsfrseceae vgwnltyska gvsvwvqave
       61 mdrtlhkikc rmeccdvpae tlydvlhdie yrkkwdsnvi etfdiarltv nadvgyyswr
      121 cpkplknrdv itlrswlpmg adyiimnysv khpkypprkd lvravsiqtg yliqstgpks
      181 cvitylaqvd pkgslpkwvv nkssqflapk amkkmykaci kypewkqkhq phfkpwlhpe
      241 qsplpslals elsvqhadsl enidesavte sreeraggag egsdddtslt
//
LOCUS       NP_001425201             497 aa            linear   ROD 17-APR-2025
DEFINITION  flt3-interacting zinc finger protein 1 [Rattus norvegicus].
ACCESSION   NP_001425201 XP_006228316
VERSION     NP_001425201.1
DBSOURCE    REFSEQ: accession NM_001438272.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Tsuruyama,T., Imai,Y., Takeuchi,H., Hiratsuka,T., Maruyama,Y.,
            Kanaya,K., Kaszynski,R., Jin,G., Okuno,T., Ozeki,M., Nakamura,T.,
            Takakuwa,T., Manabe,T., Tamaki,K. and Hiai,H.
  TITLE     Dual retrovirus integration tagging: identification of new
            signaling molecules Fiz1 and Hipk2 that are involved in the IL-7
            signaling pathway in B lymphoblastic lymphomas
  JOURNAL   J Leukoc Biol 88 (1), 107-116 (2010)
   PUBMED   20360400
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Wolf,I. and Rohrschneider,L.R.
  TITLE     Fiz1, a novel zinc finger protein interacting with the receptor
            tyrosine kinase Flt3
  JOURNAL   J Biol Chem 274 (30), 21478-21484 (1999)
   PUBMED   10409713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228316.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.319.1, SRR26643292.984.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..497
                     /product="flt3-interacting zinc finger protein 1"
                     /note="Flt3 interacting zinc finger protein 1"
                     /calculated_mol_wt=52263
     Region          26..48
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          28..48
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          40..65
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          56..76
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(61,63,65,67..68,71..72,75,89,91,95..96,99..100,103,
                     117,119,121,123..124,127..128)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          68..91
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          84..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          112..130
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(208,210,212,214..215,218..219,222,236,238..240,
                     242..243,247,250)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(422,424,426,428..429,432..433,436,450,452,456..457,
                     460..461,464,478,480,482,484..485,488..489,492)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..454
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          471..493
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          473..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..497
                     /gene="Fiz1"
                     /gene_synonym="RGD1306359"
                     /coded_by="NM_001438272.1:956..2449"
                     /db_xref="GeneID:292584"
                     /db_xref="RGD:1306359"
ORIGIN      
        1 mddpslpvvp aapgpapsat aprvpfhcse cgksfryrsd lrrhfarhta lkphacprcg
       61 kgfkhsfnla nhlrshtger pyrcsacpkg frdstgllhh qvvhtgekpy cclvcelrfs
      121 srsslgrhlk rqhrgtlpsp lqpspglppl sspcsvccnv gpcsvcgggg sgggeglega
      181 gatswglaea aaaaaaslpp facgacarrf dhgrelaahw aahtdvkpfk cprcerdfna
      241 pallerhklt hdlqgssapp tqvwasggap evagegdtae vgatpptwda glllsptgag
      301 vpkleallpe degagnaqap aaaaeassed tlyqcdcgtf fasapalash leahsgpaty
      361 gcghcgalya alaaleehrr ashgkgsgea apdgegeqva ggpgpgsssr gkkifgcsec
      421 eklfrsprdl erhvlvhtge kpfpclecgk ffrhecylkr hrllhgterp fpchicgkgf
      481 itlsnlsrhl klhrgmd
//
LOCUS       NP_001425257             252 aa            linear   ROD 17-APR-2025
DEFINITION  folate receptor beta precursor [Rattus norvegicus].
ACCESSION   NP_001425257 XP_008757925
VERSION     NP_001425257.1
DBSOURCE    REFSEQ: accession NM_001438328.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Pridans,C., Irvine,K.M., Davis,G.M., Lefevre,L., Bush,S.J. and
            Hume,D.A.
  TITLE     Transcriptomic Analysis of Rat Macrophages
  JOURNAL   Front Immunol 11, 594594 (2021)
   PUBMED   33633725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Lu,Y., Parker,N., Kleindl,P.J., Cross,V.A., Wollak,K., Westrick,E.,
            Stinnette,T.W., Gehrke,M.A., Wang,K., Santhapuram,H.K., You,F.,
            Hahn,S.J., Vaughn,J.F., Klein,P.J., Vlahov,I.R., Low,P.S. and
            Leamon,C.P.
  TITLE     Antiinflammatory Activity of a Novel Folic Acid Targeted Conjugate
            of the mTOR Inhibitor Everolimus
  JOURNAL   Mol Med 21 (1), 584-596 (2015)
   PUBMED   26181632
  REMARK    GeneRIF: EC0565 forms micellar aggregates in physiological buffers
            and demonstrates good water solubility as well as strong
            multivalent FR-binding capacity. EC0565 inhibited mTOR signaling in
            rat macrophages at nanomolar concentrations
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Shen,J., Hilgenbrink,A.R., Xia,W., Feng,Y., Dimitrov,D.S.,
            Lockwood,M.B., Amato,R.J. and Low,P.S.
  TITLE     Folate receptor-beta constitutes a marker for human proinflammatory
            monocytes
  JOURNAL   J Leukoc Biol 96 (4), 563-570 (2014)
   PUBMED   25015955
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Watkins,D. and Rosenblatt,D.S.
  TITLE     Update and new concepts in vitamin responsive disorders of folate
            transport and metabolism
  JOURNAL   J Inherit Metab Dis 35 (4), 665-670 (2012)
   PUBMED   22108709
  REMARK    Review article
REFERENCE   5  (residues 1 to 252)
  AUTHORS   van der Heijden,J.W., Oerlemans,R., Dijkmans,B.A., Qi,H., van der
            Laken,C.J., Lems,W.F., Jackman,A.L., Kraan,M.C., Tak,P.P.,
            Ratnam,M. and Jansen,G.
  TITLE     Folate receptor beta as a potential delivery route for novel folate
            antagonists to macrophages in the synovial tissue of rheumatoid
            arthritis patients
  JOURNAL   Arthritis Rheum 60 (1), 12-21 (2009)
   PUBMED   19116913
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Page,S.T., Owen,W.C., Price,K. and Elwood,P.C.
  TITLE     Expression of the human placental folate receptor transcript is
            regulated in human tissues. Organization and full nucleotide
            sequence of the gene
  JOURNAL   J Mol Biol 229 (4), 1175-1183 (1993)
   PUBMED   8445646
  REMARK    Erratum:[J Mol Biol 1994 May 13;238(4):639]
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Antony,A.C., Kane,M.A., Portillo,R.M., Elwood,P.C. and
            Kolhouse,J.F.
  TITLE     Studies of the role of a particulate folate-binding protein in the
            uptake of 5-methyltetrahydrofolate by cultured human KB cells
  JOURNAL   J Biol Chem 260 (28), 14911-14917 (1985)
   PUBMED   4066659
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_008757925.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.891525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..252
                     /product="folate receptor beta precursor"
                     /note="folate receptor 2 (fetal)"
                     /calculated_mol_wt=26904
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2284
     Region          29..204
                     /region_name="Folate_rec"
                     /note="Folate receptor family; pfam03024"
                     /db_xref="CDD:397250"
     CDS             1..252
                     /gene="Folr2"
                     /coded_by="NM_001438328.1:168..926"
                     /db_xref="GeneID:293154"
                     /db_xref="RGD:1308515"
ORIGIN      
        1 mawkqtplll lvymittcsa rdrtdllnvc mdakhhktkp gpedklhdqc spwkrnaccs
       61 vntsqelhkd nsrlynfnwd hcgemtpack rhfiqdacly ecspnlgpwi qqagqswrke
      121 rfldvplcke dcqewweacr tsftckrdwh kgwdwtsgin kcpdtapcrt fqyyfptpas
      181 lceglwshsy kvsnysrgsg qciqmwfdst qgnpneevvk fyasfmtsgt vyhaaillvp
      241 slapvlslwl pd
//
LOCUS       NP_001099672            1173 aa            linear   ROD 17-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099672 XP_001063929 XP_217641
VERSION     NP_001099672.1
DBSOURCE    REFSEQ: accession NM_001106202.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217641.4, XP_001063929.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.9503.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1173
                     /product="tudor domain-containing protein 1 isoform 1"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=129863
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1052
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     Site            order(994,999,1001,1017,1020,1022)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410449"
     CDS             1..1173
                     /gene="Tdrd1"
                     /coded_by="NM_001106202.2:250..3771"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnddfw yraivleasd sdvkvlyady
     1021 gnverlpfsr vqpitashlq lpfriircsl egltelngss sqpvmellrn amlnqsvals
     1081 vkavsknvha vsvekcseng miniaenlvm cglaenlssk resastketp hstdccctel
     1141 qkqiekheqi llfllnnptn qnkfiemkkl lqs
//
LOCUS       NP_001425207             450 aa            linear   ROD 17-APR-2025
DEFINITION  protein tweety homolog 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425207 XP_063139114
VERSION     NP_001425207.1
DBSOURCE    REFSEQ: accession NM_001438278.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kumada,T., Yamanaka,Y., Kitano,A., Shibata,M., Awaya,T., Kato,T.,
            Okawa,K., Abe,T., Oshima,N., Nakahata,T. and Heike,T.
  TITLE     Ttyh1, a Ca(2+)-binding protein localized to the endoplasmic
            reticulum, is required for early embryonic development
  JOURNAL   Dev Dyn 239 (8), 2233-2245 (2010)
   PUBMED   20568244
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yoon,J.C., Ng,A., Kim,B.H., Bianco,A., Xavier,R.J. and Elledge,S.J.
  TITLE     Wnt signaling regulates mitochondrial physiology and insulin
            sensitivity
  JOURNAL   Genes Dev 24 (14), 1507-1518 (2010)
   PUBMED   20634317
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Matthews,C.A., Shaw,J.E., Hooper,J.A., Young,I.G., Crouch,M.F. and
            Campbell,H.D.
  TITLE     Expression and evolution of the mammalian brain gene Ttyh1
  JOURNAL   J Neurochem 100 (3), 693-707 (2007)
   PUBMED   17116230
  REMARK    GeneRIF: These data suggest a role for Ttyh1 in process formation,
            cell adhesion and possibly as a transmembrane receptor.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Collins,M.O., Husi,H., Yu,L., Brandon,J.M., Anderson,C.N.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Molecular characterization and comparison of the components and
            multiprotein complexes in the postsynaptic proteome
  JOURNAL   J Neurochem 97 Suppl 1, 16-23 (2006)
   PUBMED   16635246
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Suzuki,M.
  TITLE     The Drosophila tweety family: molecular candidates for
            large-conductance Ca2+-activated Cl- channels
  JOURNAL   Exp Physiol 91 (1), 141-147 (2006)
   PUBMED   16219661
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063139114.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.1412.1,
                                           SRR26643293.1399.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..450
                     /product="protein tweety homolog 1 isoform 1"
                     /note="protein tweety homolog 1; volume-regulated anion
                     channel subunit Ttyh1"
                     /calculated_mol_wt=48901
     Region          9..441
                     /region_name="Tweety"
                     /note="pfam04906"
                     /db_xref="CDD:461475"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            165
                     /site_type="other"
                     /note="Essential for the formation of the channel-pore.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            355
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            order(371,374)
                     /site_type="active"
                     /note="putative pore region [active]"
                     /db_xref="CDD:143653"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Region          428..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     CDS             1..450
                     /gene="Ttyh1"
                     /coded_by="NM_001438278.1:77..1429"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:292597"
                     /db_xref="RGD:1310103"
ORIGIN      
        1 mgappgyrps awvhllhqlp radfqlrpvp sgfaprdqey qqalllvaal aglglglsli
       61 fiavylirfc ccrppeppga kspppgggcv twsciaallv gcagigigfy gnsetsdgvs
      121 qlssalqhan htlstiddlv letverlgea vrtelttlee vlservelva atrgarrqae
      181 aaaqhlqgla fwqgvslspv qvaedvtfve eyrwlayvll lllvllvclf tllglakqsk
      241 wlvvvmtams llvlvlswgs mgleaatavg lsdfcsnpdt yvlnltqeet gissdilnyy
      301 flcnqavsnp fqqrltlsqr alasihsqlq glereaspqf paaqkpllsl eetlnvters
      361 fhqlvallhc rslhkdygsa lrglcedale gllflmlfsl lsagalattl cslprawalf
      421 ppsddyddtd dddpfnpqes krfvqwqssi
//
LOCUS       NP_001034092             506 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 4 [Rattus norvegicus].
ACCESSION   NP_001034092 XP_225078
VERSION     NP_001034092.1
DBSOURCE    REFSEQ: accession NM_001039003.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 12, 2006 this sequence version replaced XP_225078.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN13663594
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..506
                     /product="methionine synthase reductase isoform 4"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=56400
     Region          6..>50
                     /region_name="Flavodoxin_1"
                     /note="pfam00258"
                     /db_xref="CDD:425562"
     Region          84..505
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(258..261,276..277,294..297,332,505)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(258,260..261)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(261,458,503,505)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(278..281,352,354,387..388,417..418,432,434,464)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(294,297,300)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(349,353..356,358)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..506
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001039003.2:86..1606"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 mrrflllyat qrgqakaiae eiseqalshg fsadlhcvse seksslsipa vspeylevyl
       61 qeslgqdenq asvppsvdpi fqvpiskave lttndaiktt llleldiskv efshqpgdsf
      121 nvicpnsgse vedllqrlql adkqahrvil kikmdtkkkg aslpqhvpeg sslqfiftwc
      181 leiravpkka flralsdyts datekrrlqe lcskqgaady nrfirdasvc lldllltfps
      241 cqpplnllle hlpklqprpy scasssllhp dklhfvfniv elpsnttaas lrkgvctgwl
      301 atlvapflqp ntevltadhs dalapeilis pratnsfhlp ddlsapiimv gpgtgvapfv
      361 gflqhreklq eqhpdgnfga mwlffgcrhk drdylfreel rhflktgvlt hlkvsfsrda
      421 apeeeeeapa kyvqdnlqhh sqqvartllq engyiyvcgd aknmakdvhd alveiiskea
      481 gvdkleamkt latlkqekry lqdiws
//
LOCUS       NP_001425181             577 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425181
VERSION     NP_001425181.1
DBSOURCE    REFSEQ: accession NM_001438252.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.408.1, SRR26643291.357.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..577
                     /product="methionine synthase reductase isoform 2"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=64198
     Region          155..576
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(329..332,347..348,365..368,403,576)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(329,331..332)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(332,529,574,576)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(349..352,423,425,458..459,488..489,503,505,535)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(365,368,371)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(420,424..427,429)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..577
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438252.1:559..2292"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 mfsccgfvlt slelvvepwi dglwpaltkh fkslggqedm sdsdtlaqas daplsmamkp
       61 ellhiqsqve llsledvgkr dselqeqnet nknqpsried fdsslvnsvp plsqsslsip
      121 avspeylevy lqeslgqden qasvppsvdp ifqvpiskav elttndaikt tllleldisk
      181 vefshqpgds fnvicpnsgs evedllqrlq ladkqahrvi lkikmdtkkk gaslpqhvpe
      241 gsslqfiftw cleiravpkk aflralsdyt sdatekrrlq elcskqgaad ynrfirdasv
      301 clldllltfp scqpplnlll ehlpklqprp yscasssllh pdklhfvfni velpsnttaa
      361 slrkgvctgw latlvapflq pntevltadh sdalapeili spratnsfhl pddlsapiim
      421 vgpgtgvapf vgflqhrekl qeqhpdgnfg amwlffgcrh kdrdylfree lrhflktgvl
      481 thlkvsfsrd aapeeeeeap akyvqdnlqh hsqqvartll qengyiyvcg daknmakdvh
      541 dalveiiske agvdkleamk tlatlkqekr ylqdiws
//
LOCUS       NP_001425184             538 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425184 XP_038958835
VERSION     NP_001425184.1
DBSOURCE    REFSEQ: accession NM_001438255.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_038958835.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.521.1, SRR26643296.345.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..538
                     /product="methionine synthase reductase isoform 3"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=59861
     Region          116..537
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(290..293,308..309,326..329,364,537)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(290,292..293)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(293,490,535,537)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(310..313,384,386,419..420,449..450,464,466,496)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(326,329,332)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(381,385..388,390)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..538
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438255.1:558..2174"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 msdsdtlaqa sdaplsmamk pellhiqsqv ellsledvgk rdselqeqne tnknqpsrie
       61 dfdsslvnsv pplsqsslsi pavspeylev ylqeslgqde nqasvppsvd pifqvpiska
      121 velttndaik ttllleldis kvefshqpgd sfnvicpnsg sevedllqrl qladkqahrv
      181 ilkikmdtkk kgaslpqhvp egsslqfift wcleiravpk kaflralsdy tsdatekrrl
      241 qelcskqgaa dynrfirdas vclldllltf pscqpplnll lehlpklqpr pyscasssll
      301 hpdklhfvfn ivelpsntta aslrkgvctg wlatlvapfl qpntevltad hsdalapeil
      361 ispratnsfh lpddlsapii mvgpgtgvap fvgflqhrek lqeqhpdgnf gamwlffgcr
      421 hkdrdylfre elrhflktgv lthlkvsfsr daapeeeeea pakyvqdnlq hhsqqvartl
      481 lqengyiyvc gdaknmakdv hdalveiisk eagvdkleam ktlatlkqek rylqdiws
//
LOCUS       NP_001425230             110 aa            linear   ROD 17-APR-2025
DEFINITION  small ribosomal subunit protein uS12m isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425230
VERSION     NP_001425230.1
DBSOURCE    REFSEQ: accession NM_001438301.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.3644151.1,
                                           SRR26360194.322577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..110
                     /product="small ribosomal subunit protein uS12m isoform 2"
                     /note="28S ribosomal protein S12, mitochondrial; small
                     ribosomal subunit protein uS12m"
                     /calculated_mol_wt=12206
     Region          3..109
                     /region_name="Ribosomal_S12"
                     /note="S12-like family, 30S ribosomal protein S12
                     subfamily; S12 is located at the interface of the large
                     and small ribosomal subunits of prokaryotes, chloroplasts
                     and mitochondria, where it plays an important role in both
                     tRNA and ribosomal subunit...; cd03368"
                     /db_xref="CDD:239466"
     Site            order(4..5,7..8,11..12)
                     /site_type="other"
                     /note="S17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239466"
     Site            4
                     /site_type="active"
                     /note="S8 interaction site [active]"
                     /db_xref="CDD:239466"
     Site            order(12..14,25,27..28,30,45..46,48..50,57,65,68..69,
                     82..83,87..88,109)
                     /site_type="other"
                     /note="16S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(42..43,87)
                     /site_type="other"
                     /note="streptomycin interaction site [chemical binding]"
                     /db_xref="CDD:239466"
     Site            43..44
                     /site_type="other"
                     /note="23S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(44..49,69..77)
                     /site_type="other"
                     /note="aminoacyl-tRNA interaction site (A-site)
                     [nucleotide binding]"
                     /db_xref="CDD:239466"
     CDS             1..110
                     /gene="Mrps12"
                     /coded_by="NM_001438301.1:63..395"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:292758"
                     /db_xref="RGD:1306221"
ORIGIN      
        1 matlnqmhrl grpkeppkrl gptegrpqlk gvvlrtfirk pkkpnsanrk ccrvrlstgk
       61 eavcfipgeg htlqehhvvl veggrtqdlp gvklkvvrgk ydcghvqkkk
//
LOCUS       NP_001425208             454 aa            linear   ROD 17-APR-2025
DEFINITION  protein tweety homolog 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425208 XP_017444382
VERSION     NP_001425208.1
DBSOURCE    REFSEQ: accession NM_001438279.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Kumada,T., Yamanaka,Y., Kitano,A., Shibata,M., Awaya,T., Kato,T.,
            Okawa,K., Abe,T., Oshima,N., Nakahata,T. and Heike,T.
  TITLE     Ttyh1, a Ca(2+)-binding protein localized to the endoplasmic
            reticulum, is required for early embryonic development
  JOURNAL   Dev Dyn 239 (8), 2233-2245 (2010)
   PUBMED   20568244
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Yoon,J.C., Ng,A., Kim,B.H., Bianco,A., Xavier,R.J. and Elledge,S.J.
  TITLE     Wnt signaling regulates mitochondrial physiology and insulin
            sensitivity
  JOURNAL   Genes Dev 24 (14), 1507-1518 (2010)
   PUBMED   20634317
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Matthews,C.A., Shaw,J.E., Hooper,J.A., Young,I.G., Crouch,M.F. and
            Campbell,H.D.
  TITLE     Expression and evolution of the mammalian brain gene Ttyh1
  JOURNAL   J Neurochem 100 (3), 693-707 (2007)
   PUBMED   17116230
  REMARK    GeneRIF: These data suggest a role for Ttyh1 in process formation,
            cell adhesion and possibly as a transmembrane receptor.
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Collins,M.O., Husi,H., Yu,L., Brandon,J.M., Anderson,C.N.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Molecular characterization and comparison of the components and
            multiprotein complexes in the postsynaptic proteome
  JOURNAL   J Neurochem 97 Suppl 1, 16-23 (2006)
   PUBMED   16635246
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Suzuki,M.
  TITLE     The Drosophila tweety family: molecular candidates for
            large-conductance Ca2+-activated Cl- channels
  JOURNAL   Exp Physiol 91 (1), 141-147 (2006)
   PUBMED   16219661
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_017444382.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.1411.1,
                                           SRR26360176.932742.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..454
                     /product="protein tweety homolog 1 isoform 2"
                     /note="protein tweety homolog 1; volume-regulated anion
                     channel subunit Ttyh1"
                     /calculated_mol_wt=48830
     Region          9..424
                     /region_name="Tweety"
                     /note="pfam04906"
                     /db_xref="CDD:461475"
     Site            order(371,374)
                     /site_type="active"
                     /note="putative pore region [active]"
                     /db_xref="CDD:143653"
     CDS             1..454
                     /gene="Ttyh1"
                     /coded_by="NM_001438279.1:77..1441"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:292597"
                     /db_xref="RGD:1310103"
ORIGIN      
        1 mgappgyrps awvhllhqlp radfqlrpvp sgfaprdqey qqalllvaal aglglglsli
       61 fiavylirfc ccrppeppga kspppgggcv twsciaallv gcagigigfy gnsetsdgvs
      121 qlssalqhan htlstiddlv letverlgea vrtelttlee vlservelva atrgarrqae
      181 aaaqhlqgla fwqgvslspv qvaedvtfve eyrwlayvll lllvllvclf tllglakqsk
      241 wlvvvmtams llvlvlswgs mgleaatavg lsdfcsnpdt yvlnltqeet gissdilnyy
      301 flcnqavsnp fqqrltlsqr alasihsqlq glereaspqf paaqkpllsl eetlnvters
      361 fhqlvallhc rslhkdygsa lrglcedale gllflmlfsl lsagalattl cslprawalf
      421 pprnpsalcs gslpseppcq cglpllfgsa llcf
//
LOCUS       NP_001099709             139 aa            linear   ROD 17-APR-2025
DEFINITION  small ribosomal subunit protein uS12m isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001099709 XP_001078443 XP_214890
VERSION     NP_001099709.1
DBSOURCE    REFSEQ: accession NM_001106239.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_214890.1, XP_001078443.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW917069.1, SRR22399489.639410.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..139
                     /product="small ribosomal subunit protein uS12m isoform 1"
                     /note="28S ribosomal protein S12, mitochondrial; small
                     ribosomal subunit protein uS12m"
                     /calculated_mol_wt=15310
     Region          32..138
                     /region_name="Ribosomal_S12"
                     /note="S12-like family, 30S ribosomal protein S12
                     subfamily; S12 is located at the interface of the large
                     and small ribosomal subunits of prokaryotes, chloroplasts
                     and mitochondria, where it plays an important role in both
                     tRNA and ribosomal subunit...; cd03368"
                     /db_xref="CDD:239466"
     Site            order(33..34,36..37,40..41)
                     /site_type="other"
                     /note="S17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239466"
     Site            33
                     /site_type="active"
                     /note="S8 interaction site [active]"
                     /db_xref="CDD:239466"
     Site            order(41..43,54,56..57,59,74..75,77..79,86,94,97..98,
                     111..112,116..117,138)
                     /site_type="other"
                     /note="16S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(71..72,116)
                     /site_type="other"
                     /note="streptomycin interaction site [chemical binding]"
                     /db_xref="CDD:239466"
     Site            72..73
                     /site_type="other"
                     /note="23S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(73..78,98..106)
                     /site_type="other"
                     /note="aminoacyl-tRNA interaction site (A-site)
                     [nucleotide binding]"
                     /db_xref="CDD:239466"
     CDS             1..139
                     /gene="Mrps12"
                     /coded_by="NM_001106239.2:39..458"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292758"
                     /db_xref="RGD:1306221"
ORIGIN      
        1 mswpgllhgl ttslsrglal apqlwatrsm atlnqmhrlg rpkeppkrlg ptegrpqlkg
       61 vvlrtfirkp kkpnsanrkc crvrlstgke avcfipgegh tlqehhvvlv eggrtqdlpg
      121 vklkvvrgky dcghvqkkk
//
LOCUS       NP_001425182             538 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425182 XP_063138783
VERSION     NP_001425182.1
DBSOURCE    REFSEQ: accession NM_001438253.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138783.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1841170.1,
                                           SRR26643289.429.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..538
                     /product="methionine synthase reductase isoform 3"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=59861
     Region          116..537
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(290..293,308..309,326..329,364,537)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(290,292..293)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(293,490,535,537)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(310..313,384,386,419..420,449..450,464,466,496)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(326,329,332)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(381,385..388,390)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..538
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438253.1:300..1916"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 msdsdtlaqa sdaplsmamk pellhiqsqv ellsledvgk rdselqeqne tnknqpsrie
       61 dfdsslvnsv pplsqsslsi pavspeylev ylqeslgqde nqasvppsvd pifqvpiska
      121 velttndaik ttllleldis kvefshqpgd sfnvicpnsg sevedllqrl qladkqahrv
      181 ilkikmdtkk kgaslpqhvp egsslqfift wcleiravpk kaflralsdy tsdatekrrl
      241 qelcskqgaa dynrfirdas vclldllltf pscqpplnll lehlpklqpr pyscasssll
      301 hpdklhfvfn ivelpsntta aslrkgvctg wlatlvapfl qpntevltad hsdalapeil
      361 ispratnsfh lpddlsapii mvgpgtgvap fvgflqhrek lqeqhpdgnf gamwlffgcr
      421 hkdrdylfre elrhflktgv lthlkvsfsr daapeeeeea pakyvqdnlq hhsqqvartl
      481 lqengyiyvc gdaknmakdv hdalveiisk eagvdkleam ktlatlkqek rylqdiws
//
LOCUS       NP_001425195             647 aa            linear   ROD 17-APR-2025
DEFINITION  zinc finger protein 418 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425195
VERSION     NP_001425195.1
DBSOURCE    REFSEQ: accession NM_001438266.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Singh,S.R., Meyer-Jens,M., Alizoti,E., Bacon,W.C., Davis,G.,
            Osinska,H., Gulick,J., Reischmann-Dusener,S., Orthey,E.,
            McLendon,P.M., Molkentin,J.D., Schlossarek,S., Robbins,J. and
            Carrier,L.
  TITLE     A high-throughput screening identifies ZNF418 as a novel regulator
            of the ubiquitin-proteasome system and autophagy-lysosomal pathway
  JOURNAL   Autophagy 17 (10), 3124-3139 (2021)
   PUBMED   33249983
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Pan,L., Sheng,M., Huang,Z., Zhu,Z., Xu,C., Teng,L., He,L., Gu,C.,
            Yi,C. and Li,J.
  TITLE     Zinc-finger protein 418 overexpression protects against cardiac
            hypertrophy and fibrosis
  JOURNAL   PLoS One 12 (10), e0186635 (2017)
   PUBMED   29065170
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.228664.1,
                                           SRR26360176.1957250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..647
                     /product="zinc finger protein 418 isoform 2"
                     /calculated_mol_wt=74997
     Region          11..51
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          277..634
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(370,372,374,376..377,380..381,384,398,400,404..405,
                     408..409,412,426,428,430,432..433,436..437,440)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          393..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(566,568,570,572..573,576..577,580,594,596,600..601,
                     604..605,608,622,624,626,628..629,632..633,636)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          617..637
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..647
                     /gene="Zfp418"
                     /gene_synonym="RGD1311663; ZNF418"
                     /coded_by="NM_001438266.1:178..2121"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:292548"
                     /db_xref="RGD:1311663"
ORIGIN      
        1 maavkhlaqg cvtiedvtvy fsqeewklld eaqrllyldv mlenftliss lvyryeaeae
       61 ektcaqslsq teapqvrtpk qgqlrqkphp sdicitvlkd ilhlndlpgq kpyltevctk
      121 pqdhkhhrak nwlkrdvdsl vkscifhvag npficskige kfpaiwnllq pkdipngekq
      181 nkikrgkafh rdknnsesde ykkssspqhr lheypgvcsa kggfesnsce qdlnkyspap
      241 frmdqtenrp yechvcgkwf gqkatlrihq rrhtgekpyk cgecgksfcq ssnlsehcrv
      301 hsgerpfecl ecgkafgchs sllrhqrtht gewpyecsdc grlfrqivsl ithqrthtte
      361 kpyecgqcek sfshkatltv hqrvhtgekp yhceacgksf sqsanlikhs kihtgekpye
      421 cgecglcfrq ratlmkhqrt htserpyecr ecgkffkqyf yliehrriht ttefyeceqc
      481 gksytqkatl irhqrvhtge spykceecgk afeyksrlkr hqrthtgerp yecakcgkff
      541 resynlaehq kihtkakpyh cdqcgkcfsr radlvkhqrv htgerpytcg ecgktfsrtt
      601 nlvqhrriht gerpyecdqc gksfsqvstl trhqllhtge kpykcsk
//
LOCUS       NP_001425174             281 aa            linear   ROD 17-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-5 [Rattus
            norvegicus].
ACCESSION   NP_001425174
VERSION     NP_001425174.1
DBSOURCE    REFSEQ: accession NM_001438245.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Madarampalli,B., Yuan,Y., Liu,D., Lengel,K., Xu,Y., Li,G., Yang,J.,
            Liu,X., Lu,Z. and Liu,D.X.
  TITLE     ATF5 Connects the Pericentriolar Materials to the Proximal End of
            the Mother Centriole
  JOURNAL   Cell 162 (3), 580-592 (2015)
   PUBMED   26213385
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zhang,Z.Y., Li,S.Z., Zhang,H.H., Wu,Q.R., Gong,J., Liang,T.,
            Gao,L., Xing,N.N., Liu,W.B., Du,R.L. and Zhang,X.D.
  TITLE     Stabilization of ATF5 by TAK1-Nemo-like kinase critically regulates
            the interleukin-1beta-stimulated C/EBP signaling pathway
  JOURNAL   Mol Cell Biol 35 (5), 778-788 (2015)
   PUBMED   25512613
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Zhao,Y., Zhang,Y.D., Zhang,Y.Y., Qian,S.W., Zhang,Z.C., Li,S.F.,
            Guo,L., Liu,Y., Wen,B., Lei,Q.Y., Tang,Q.Q. and Li,X.
  TITLE     p300-dependent acetylation of activating transcription factor 5
            enhances C/EBPbeta transactivation of C/EBPalpha during 3T3-L1
            differentiation
  JOURNAL   Mol Cell Biol 34 (3), 315-324 (2014)
   PUBMED   24216764
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,S.Z., Ou,J., Zhu,L.J. and Green,M.R.
  TITLE     Transcription factor ATF5 is required for terminal differentiation
            and survival of olfactory sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 109 (45), 18589-18594 (2012)
   PUBMED   23090999
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Liu,X., Liu,D., Qian,D., Dai,J., An,Y., Jiang,S., Stanley,B.,
            Yang,J., Wang,B., Liu,X. and Liu,D.X.
  TITLE     Nucleophosmin (NPM1/B23) interacts with activating transcription
            factor 5 (ATF5) protein and promotes proteasome- and
            caspase-dependent ATF5 degradation in hepatocellular carcinoma
            cells
  JOURNAL   J Biol Chem 287 (23), 19599-19609 (2012)
   PUBMED   22528486
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Forgacs,E., Gupta,S.K., Kerry,J.A. and Semmes,O.J.
  TITLE     The bZIP transcription factor ATFx binds human T-cell leukemia
            virus type 1 (HTLV-1) Tax and represses HTLV-1 long terminal
            repeat-mediated transcription
  JOURNAL   J Virol 79 (11), 6932-6939 (2005)
   PUBMED   15890932
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Angelastro,J.M., Mason,J.L., Ignatova,T.N., Kukekov,V.G.,
            Stengren,G.B., Goldman,J.E. and Greene,L.A.
  TITLE     Downregulation of activating transcription factor 5 is required for
            differentiation of neural progenitor cells into astrocytes
  JOURNAL   J Neurosci 25 (15), 3889-3899 (2005)
   PUBMED   15829641
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Angelastro,J.M., Ignatova,T.N., Kukekov,V.G., Steindler,D.A.,
            Stengren,G.B., Mendelsohn,C. and Greene,L.A.
  TITLE     Regulated expression of ATF5 is required for the progression of
            neural progenitor cells to neurons
  JOURNAL   J Neurosci 23 (11), 4590-4600 (2003)
   PUBMED   12805299
  REMARK    GeneRIF: ATF5 blocks the differentiation of neuroprogenitor cells
            into neurons and must be downregulated to permit this process to
            occur.
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Persengiev,S.P., Devireddy,L.R. and Green,M.R.
  TITLE     Inhibition of apoptosis by ATFx: a novel role for a member of the
            ATF/CREB family of mammalian bZIP transcription factors
  JOURNAL   Genes Dev 16 (14), 1806-1814 (2002)
   PUBMED   12130540
REFERENCE   10 (residues 1 to 281)
  AUTHORS   De Graeve,F., Bahr,A., Chatton,B. and Kedinger,C.
  TITLE     A murine ATFa-associated factor with transcriptional repressing
            activity
  JOURNAL   Oncogene 19 (14), 1807-1819 (2000)
   PUBMED   10777215
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.1381.1,
                                           SRR26643297.1627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN16676811
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..281
                     /product="cyclic AMP-dependent transcription factor ATF-5"
                     /note="cAMP-dependent transcription factor ATF-5;
                     transcription factor ATFx"
                     /calculated_mol_wt=30058
     Region          1..21
                     /region_name="Required for protein stabilization induced
                     by IL1B. /evidence=ECO:0000250|UniProtKB:Q9Y2D1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000269|PubMed:21791614; propagated from
                     UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          118..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          119..216
                     /region_name="Interaction with PTP4A1.
                     /evidence=ECO:0000250|UniProtKB:O70191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          166..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          208..270
                     /region_name="bZIP_ATF4"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-4 (ATF-4) and similar proteins: a
                     DNA-binding and dimerization domain; cd14692"
                     /db_xref="CDD:269840"
     Region          209..229
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          210..269
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269840"
     Site            order(213..214,216..218,220..225,227..229)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269840"
     Site            order(232,235,238..239,242..243,245..246,249..250,
                     252..253,256,259..260,263..264,266..267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269840"
     Region          235..249
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D1; propagated from
                     UniProtKB/Swiss-Prot (Q6P788.1)"
     CDS             1..281
                     /gene="Atf5"
                     /coded_by="NM_001438245.1:512..1357"
                     /db_xref="GeneID:282840"
                     /db_xref="RGD:628902"
ORIGIN      
        1 msllatlgle ldrallpasg lgwlvdygkl plapaplgpy evlggalegg lpgggeplag
       61 dgfsdwmter vdftallple aplppgtlpp pspappdlea masllkkele qmedffldap
      121 llpppspppp pppapslplp lplptfdlpq pptldtldll avycrseagp gdsglttlpv
      181 pqqppplapl pspsrpapyp spastrgdrk qkkrdqnksa alryrqrkra egealegecq
      241 glearnrelr eraesverei qyvkdlliev ykarsqrtrs a
//
LOCUS       NP_001425183             538 aa            linear   ROD 17-APR-2025
DEFINITION  methionine synthase reductase isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425183
VERSION     NP_001425183.1
DBSOURCE    REFSEQ: accession NM_001438254.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.570.1, SRR26643297.411.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..538
                     /product="methionine synthase reductase isoform 3"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=59861
     Region          116..537
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(290..293,308..309,326..329,364,537)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(290,292..293)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(293,490,535,537)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(310..313,384,386,419..420,449..450,464,466,496)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(326,329,332)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(381,385..388,390)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..538
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438254.1:454..2070"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 msdsdtlaqa sdaplsmamk pellhiqsqv ellsledvgk rdselqeqne tnknqpsrie
       61 dfdsslvnsv pplsqsslsi pavspeylev ylqeslgqde nqasvppsvd pifqvpiska
      121 velttndaik ttllleldis kvefshqpgd sfnvicpnsg sevedllqrl qladkqahrv
      181 ilkikmdtkk kgaslpqhvp egsslqfift wcleiravpk kaflralsdy tsdatekrrl
      241 qelcskqgaa dynrfirdas vclldllltf pscqpplnll lehlpklqpr pyscasssll
      301 hpdklhfvfn ivelpsntta aslrkgvctg wlatlvapfl qpntevltad hsdalapeil
      361 ispratnsfh lpddlsapii mvgpgtgvap fvgflqhrek lqeqhpdgnf gamwlffgcr
      421 hkdrdylfre elrhflktgv lthlkvsfsr daapeeeeea pakyvqdnlq hhsqqvartl
      481 lqengyiyvc gdaknmakdv hdalveiisk eagvdkleam ktlatlkqek rylqdiws
//
LOCUS       NP_001425253             290 aa            linear   ROD 17-APR-2025
DEFINITION  START domain-containing protein 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425253
VERSION     NP_001425253.1
DBSOURCE    REFSEQ: accession NM_001438324.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ito,M., Yamanashi,Y., Toyoda,Y., Izumi-Nakaseko,H., Oda,S.,
            Sugiyama,A., Kuroda,M., Suzuki,H., Takada,T. and Adachi-Akahane,S.
  TITLE     Disruption of Stard10 gene alters the PPARalpha-mediated bile acid
            homeostasis
  JOURNAL   Biochim Biophys Acta 1831 (2), 459-468 (2013)
   PUBMED   23200860
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.1488085.1, DN948339.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..290
                     /product="START domain-containing protein 10 isoform 1"
                     /note="START domain containing 10; PCTP-like protein;
                     StAR-related lipid transfer (START) domain containing 10;
                     START domain-containing protein 10"
                     /calculated_mol_wt=32773
     Region          19..241
                     /region_name="START_STARD10-like"
                     /note="Lipid-binding START domain of mammalian STARD10 and
                     related proteins; cd08871"
                     /db_xref="CDD:176880"
     Site            order(46..47,54,68,70,82,86,92,95..96,98..99,118,120..123,
                     125,128,130,132,147,164,166..169,171,183,185,187,189,191,
                     193,200,202..204,206..208,211..212,215)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176880"
     CDS             1..290
                     /gene="Stard10"
                     /coded_by="NM_001438324.1:343..1215"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293150"
                     /db_xref="RGD:1306548"
ORIGIN      
        1 mekpaastep qgprpalgre svqvpddqdf rsfrseceae vgwnltyska gvsvwvqave
       61 mdrtlhkikc rmeccdvpae tlydvlhdie yrkkwdsnvi etfdiarltv nadvgyyswr
      121 cpkplknrdv itlrswlpmg adyiimnysv khpkypprkd lvravsiqtg yliqstgpks
      181 cvitylaqvd pkgslpkwvv nkssqflapk amkkmykaci kypewkqkhq phfkpwlhpe
      241 qsplpslals elsvqhadsl enidesavte sreeraggag egsdddtslt
//
LOCUS       NP_001425200             497 aa            linear   ROD 17-APR-2025
DEFINITION  flt3-interacting zinc finger protein 1 [Rattus norvegicus].
ACCESSION   NP_001425200 XP_006228314
VERSION     NP_001425200.1
DBSOURCE    REFSEQ: accession NM_001438271.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Tsuruyama,T., Imai,Y., Takeuchi,H., Hiratsuka,T., Maruyama,Y.,
            Kanaya,K., Kaszynski,R., Jin,G., Okuno,T., Ozeki,M., Nakamura,T.,
            Takakuwa,T., Manabe,T., Tamaki,K. and Hiai,H.
  TITLE     Dual retrovirus integration tagging: identification of new
            signaling molecules Fiz1 and Hipk2 that are involved in the IL-7
            signaling pathway in B lymphoblastic lymphomas
  JOURNAL   J Leukoc Biol 88 (1), 107-116 (2010)
   PUBMED   20360400
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Wolf,I. and Rohrschneider,L.R.
  TITLE     Fiz1, a novel zinc finger protein interacting with the receptor
            tyrosine kinase Flt3
  JOURNAL   J Biol Chem 274 (30), 21478-21484 (1999)
   PUBMED   10409713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228314.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.611884.1,
                                           SRR22582419.767815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..497
                     /product="flt3-interacting zinc finger protein 1"
                     /note="Flt3 interacting zinc finger protein 1"
                     /calculated_mol_wt=52263
     Region          26..48
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          28..48
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          40..65
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          56..76
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(61,63,65,67..68,71..72,75,89,91,95..96,99..100,103,
                     117,119,121,123..124,127..128)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          68..91
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          84..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          112..130
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(208,210,212,214..215,218..219,222,236,238..240,
                     242..243,247,250)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(422,424,426,428..429,432..433,436,450,452,456..457,
                     460..461,464,478,480,482,484..485,488..489,492)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..454
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          471..493
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          473..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..497
                     /gene="Fiz1"
                     /gene_synonym="RGD1306359"
                     /coded_by="NM_001438271.1:259..1752"
                     /db_xref="GeneID:292584"
                     /db_xref="RGD:1306359"
ORIGIN      
        1 mddpslpvvp aapgpapsat aprvpfhcse cgksfryrsd lrrhfarhta lkphacprcg
       61 kgfkhsfnla nhlrshtger pyrcsacpkg frdstgllhh qvvhtgekpy cclvcelrfs
      121 srsslgrhlk rqhrgtlpsp lqpspglppl sspcsvccnv gpcsvcgggg sgggeglega
      181 gatswglaea aaaaaaslpp facgacarrf dhgrelaahw aahtdvkpfk cprcerdfna
      241 pallerhklt hdlqgssapp tqvwasggap evagegdtae vgatpptwda glllsptgag
      301 vpkleallpe degagnaqap aaaaeassed tlyqcdcgtf fasapalash leahsgpaty
      361 gcghcgalya alaaleehrr ashgkgsgea apdgegeqva ggpgpgsssr gkkifgcsec
      421 eklfrsprdl erhvlvhtge kpfpclecgk ffrhecylkr hrllhgterp fpchicgkgf
      481 itlsnlsrhl klhrgmd
//
LOCUS       NP_001425209             458 aa            linear   ROD 17-APR-2025
DEFINITION  protein tweety homolog 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425209 XP_017444381
VERSION     NP_001425209.1
DBSOURCE    REFSEQ: accession NM_001438280.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Kumada,T., Yamanaka,Y., Kitano,A., Shibata,M., Awaya,T., Kato,T.,
            Okawa,K., Abe,T., Oshima,N., Nakahata,T. and Heike,T.
  TITLE     Ttyh1, a Ca(2+)-binding protein localized to the endoplasmic
            reticulum, is required for early embryonic development
  JOURNAL   Dev Dyn 239 (8), 2233-2245 (2010)
   PUBMED   20568244
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Yoon,J.C., Ng,A., Kim,B.H., Bianco,A., Xavier,R.J. and Elledge,S.J.
  TITLE     Wnt signaling regulates mitochondrial physiology and insulin
            sensitivity
  JOURNAL   Genes Dev 24 (14), 1507-1518 (2010)
   PUBMED   20634317
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Matthews,C.A., Shaw,J.E., Hooper,J.A., Young,I.G., Crouch,M.F. and
            Campbell,H.D.
  TITLE     Expression and evolution of the mammalian brain gene Ttyh1
  JOURNAL   J Neurochem 100 (3), 693-707 (2007)
   PUBMED   17116230
  REMARK    GeneRIF: These data suggest a role for Ttyh1 in process formation,
            cell adhesion and possibly as a transmembrane receptor.
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Collins,M.O., Husi,H., Yu,L., Brandon,J.M., Anderson,C.N.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Molecular characterization and comparison of the components and
            multiprotein complexes in the postsynaptic proteome
  JOURNAL   J Neurochem 97 Suppl 1, 16-23 (2006)
   PUBMED   16635246
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Suzuki,M.
  TITLE     The Drosophila tweety family: molecular candidates for
            large-conductance Ca2+-activated Cl- channels
  JOURNAL   Exp Physiol 91 (1), 141-147 (2006)
   PUBMED   16219661
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_017444381.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.537864.1,
                                           SRR26643298.1441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..458
                     /product="protein tweety homolog 1 isoform 3"
                     /note="protein tweety homolog 1; volume-regulated anion
                     channel subunit Ttyh1"
                     /calculated_mol_wt=49460
     Region          9..424
                     /region_name="Tweety"
                     /note="pfam04906"
                     /db_xref="CDD:461475"
     Site            order(371,374)
                     /site_type="active"
                     /note="putative pore region [active]"
                     /db_xref="CDD:143653"
     CDS             1..458
                     /gene="Ttyh1"
                     /coded_by="NM_001438280.1:77..1453"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:292597"
                     /db_xref="RGD:1310103"
ORIGIN      
        1 mgappgyrps awvhllhqlp radfqlrpvp sgfaprdqey qqalllvaal aglglglsli
       61 fiavylirfc ccrppeppga kspppgggcv twsciaallv gcagigigfy gnsetsdgvs
      121 qlssalqhan htlstiddlv letverlgea vrtelttlee vlservelva atrgarrqae
      181 aaaqhlqgla fwqgvslspv qvaedvtfve eyrwlayvll lllvllvclf tllglakqsk
      241 wlvvvmtams llvlvlswgs mgleaatavg lsdfcsnpdt yvlnltqeet gissdilnyy
      301 flcnqavsnp fqqrltlsqr alasihsqlq glereaspqf paaqkpllsl eetlnvters
      361 fhqlvallhc rslhkdygsa lrglcedale gllflmlfsl lsagalattl cslprawalf
      421 pprnpsalcs gslpseppcq cglpllfapf lgcwrrph
//
LOCUS       NP_001425197             633 aa            linear   ROD 17-APR-2025
DEFINITION  zinc finger protein 418 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001425197
VERSION     NP_001425197.1
DBSOURCE    REFSEQ: accession NM_001438268.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Singh,S.R., Meyer-Jens,M., Alizoti,E., Bacon,W.C., Davis,G.,
            Osinska,H., Gulick,J., Reischmann-Dusener,S., Orthey,E.,
            McLendon,P.M., Molkentin,J.D., Schlossarek,S., Robbins,J. and
            Carrier,L.
  TITLE     A high-throughput screening identifies ZNF418 as a novel regulator
            of the ubiquitin-proteasome system and autophagy-lysosomal pathway
  JOURNAL   Autophagy 17 (10), 3124-3139 (2021)
   PUBMED   33249983
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Pan,L., Sheng,M., Huang,Z., Zhu,Z., Xu,C., Teng,L., He,L., Gu,C.,
            Yi,C. and Li,J.
  TITLE     Zinc-finger protein 418 overexpression protects against cardiac
            hypertrophy and fibrosis
  JOURNAL   PLoS One 12 (10), e0186635 (2017)
   PUBMED   29065170
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1959078.1,
                                           SRR26360194.475553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..633
                     /product="zinc finger protein 418 isoform 4"
                     /calculated_mol_wt=73455
     Region          <9..37
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          239..259
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(244,246,248,250..251,254..255,258,272,274,278..279,
                     282..283,286,300,302,304,306..307,310..311,314)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          263..620
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          267..287
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          295..315
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          323..343
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..371
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(356,358,360,362..363,366..367,370,384,386,390..391,
                     394..395,398,412,414,416,418..419,422..423,426)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          379..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          407..427
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          491..511
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          519..539
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          547..567
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(552,554,556,558..559,562..563,566,580,582,586..587,
                     590..591,594,608,610,612,614..615,618..619,622)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          575..595
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          603..623
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..633
                     /gene="Zfp418"
                     /gene_synonym="RGD1311663; ZNF418"
                     /coded_by="NM_001438268.1:178..2079"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:292548"
                     /db_xref="RGD:1311663"
ORIGIN      
        1 maavkhlaqe ewklldeaqr llyldvmlen ftlisslvyr yeaeaeektc aqslsqteap
       61 qvrtpkqgql rqkphpsdic itvlkdilhl ndlpgqkpyl tevctkpqdh khhraknwlk
      121 rdvdslvksc ifhvagnpfi cskigekfpa iwnllqpkdi pngekqnkik rgkafhrdkn
      181 nsesdeykks sspqhrlhey pgvcsakggf esnsceqdln kyspapfrmd qtenrpyech
      241 vcgkwfgqka tlrihqrrht gekpykcgec gksfcqssnl sehcrvhsge rpfeclecgk
      301 afgchssllr hqrthtgewp yecsdcgrlf rqivslithq rthttekpye cgqceksfsh
      361 katltvhqrv htgekpyhce acgksfsqsa nlikhskiht gekpyecgec glcfrqratl
      421 mkhqrthtse rpyecrecgk ffkqyfylie hrrihtttef yeceqcgksy tqkatlirhq
      481 rvhtgespyk ceecgkafey ksrlkrhqrt htgerpyeca kcgkffresy nlaehqkiht
      541 kakpyhcdqc gkcfsrradl vkhqrvhtge rpytcgecgk tfsrttnlvq hrrihtgerp
      601 yecdqcgksf sqvstltrhq llhtgekpyk csk
//
LOCUS       NP_001425221             281 aa            linear   ROD 17-APR-2025
DEFINITION  U1 small nuclear ribonucleoprotein A [Rattus norvegicus].
ACCESSION   NP_001425221
VERSION     NP_001425221.1
DBSOURCE    REFSEQ: accession NM_001438292.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kondo,Y., Oubridge,C., van Roon,A.M. and Nagai,K.
  TITLE     Crystal structure of human U1 snRNP, a small nuclear
            ribonucleoprotein particle, reveals the mechanism of 5' splice site
            recognition
  JOURNAL   Elife 4, e04986 (2015)
   PUBMED   25555158
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Bai,B., Hales,C.M., Chen,P.C., Gozal,Y., Dammer,E.B., Fritz,J.J.,
            Wang,X., Xia,Q., Duong,D.M., Street,C., Cantero,G., Cheng,D.,
            Jones,D.R., Wu,Z., Li,Y., Diner,I., Heilman,C.J., Rees,H.D., Wu,H.,
            Lin,L., Szulwach,K.E., Gearing,M., Mufson,E.J., Bennett,D.A.,
            Montine,T.J., Seyfried,N.T., Wingo,T.S., Sun,Y.E., Jin,P.,
            Hanfelt,J., Willcock,D.M., Levey,A., Lah,J.J. and Peng,J.
  TITLE     U1 small nuclear ribonucleoprotein complex and RNA splicing
            alterations in Alzheimer's disease
  JOURNAL   Proc Natl Acad Sci U S A 110 (41), 16562-16567 (2013)
   PUBMED   24023061
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Pabis,M., Neufeld,N., Steiner,M.C., Bojic,T., Shav-Tal,Y. and
            Neugebauer,K.M.
  TITLE     The nuclear cap-binding complex interacts with the U4/U6.U5
            tri-snRNP and promotes spliceosome assembly in mammalian cells
  JOURNAL   RNA 19 (8), 1054-1063 (2013)
   PUBMED   23793891
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Zhang,L., Li,X. and Zhao,R.
  TITLE     Structural analyses of the pre-mRNA splicing machinery
  JOURNAL   Protein Sci 22 (6), 677-692 (2013)
   PUBMED   23592432
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Novakova,Z., Man,P., Novak,P., Hozak,P. and Hodny,Z.
  TITLE     Separation of nuclear protein complexes by blue native
            polyacrylamide gel electrophoresis
  JOURNAL   Electrophoresis 27 (7), 1277-1287 (2006)
   PUBMED   16502463
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Sinha,K., Perumal,K., Chen,Y. and Reddy,R.
  TITLE     Post-transcriptional adenylation of signal recognition particle RNA
            is carried out by an enzyme different from mRNA Poly(A) polymerase
  JOURNAL   J Biol Chem 274 (43), 30826-30831 (1999)
   PUBMED   10521474
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Nagai,K., Oubridge,C., Jessen,T.H., Li,J. and Evans,P.R.
  TITLE     Crystal structure of the RNA-binding domain of the U1 small nuclear
            ribonucleoprotein A
  JOURNAL   Nature 348 (6301), 515-520 (1990)
   PUBMED   2147232
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Craft,J., Mimori,T., Olsen,T.L. and Hardin,J.A.
  TITLE     The U2 small nuclear ribonucleoprotein particle as an autoantigen.
            Analysis with sera from patients with overlap syndromes
  JOURNAL   J Clin Invest 81 (6), 1716-1724 (1988)
   PUBMED   2968364
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ233559.1, FQ227089.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840110 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..281
                     /product="U1 small nuclear ribonucleoprotein A"
                     /calculated_mol_wt=31045
     Region          7..95
                     /region_name="RRM1_U1A"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1A); cd12477"
                     /db_xref="CDD:409906"
     Region          <12..>207
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Site            order(13,15..16,19,44,46,48..54,56,80,83,85..92)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409906"
     Region          196..281
                     /region_name="RRM2_U1A"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A
                     or U1A); cd12480"
                     /db_xref="CDD:409908"
     CDS             1..281
                     /gene="Snrpa"
                     /coded_by="NM_001438292.1:235..1080"
                     /db_xref="GeneID:292729"
                     /db_xref="RGD:1307416"
ORIGIN      
        1 mavpetrpnh tiyinnlnek ikkdelkksl yaifsqfgqi ldilvsrslk mrgqafvifk
       61 evssatnalr smqgfpfydk pmriqyaktd sdiiakmkgt fverdrkrek rkpksqetpa
      121 akkavqggaa apvvgavqpv pgmppmtqap rimhhmpgqp pympppgmip ppglapgqip
      181 pgamppqqlm pgqmppaqpl senppnhilf ltnlpeetne lmlsmlfnqf pgfkevrlvp
      241 grhdiafvef dnevqagaar dalqgfkitq nnamkisfak k
//
LOCUS       NP_001425231             592 aa            linear   ROD 17-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF220 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425231 XP_063144315
VERSION     NP_001425231.1
DBSOURCE    REFSEQ: accession NM_001438302.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Ma,P., Yang,X., Kong,Q., Li,C., Yang,S., Li,Y. and Mao,B.
  TITLE     The ubiquitin ligase RNF220 enhances canonical Wnt signaling
            through USP7-mediated deubiquitination of beta-catenin
  JOURNAL   Mol Cell Biol 34 (23), 4355-4366 (2014)
   PUBMED   25266658
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Kong,Q., Zeng,W., Wu,J., Hu,W., Li,C. and Mao,B.
  TITLE     RNF220, an E3 ubiquitin ligase that targets Sin3B for
            ubiquitination
  JOURNAL   Biochem Biophys Res Commun 393 (4), 708-713 (2010)
   PUBMED   20170641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063144315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.28543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..592
                     /product="E3 ubiquitin-protein ligase RNF220 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF220"
                     /calculated_mol_wt=65469
     Region          217..470
                     /region_name="RNF220"
                     /note="E3 ubiquitin-protein ligase RNF220; pfam15926"
                     /db_xref="CDD:464946"
     Region          538..589
                     /region_name="RING-HC_RNF220"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 220 (RNF220) and similar proteins; cd16563"
                     /db_xref="CDD:438225"
     CDS             1..592
                     /gene="Rnf220"
                     /coded_by="NM_001438302.1:468..2246"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500532"
                     /db_xref="RGD:1598210"
ORIGIN      
        1 mdlhraafkm enssylpnpl aspalmvlas taeasrdasi pcqqprpfgv pvsvdkdvhi
       61 pftngsytfa smyhrqggvp gtfanrdfpp sllhlhpqfa ppnldctpis mlnhsgvgaf
      121 rpfastedre syqsaftpak rlknchdses phlrfsdadg keydfgtqlp ssspgslkvd
      181 dtgkkifavs glisdretss spedrndrck kkavalfdsq apicpicqvl lrpselqehm
      241 eqeleqlaql pasknsllkd amapgtpksl llsasikreg dsptasphss atedlhhsdr
      301 yqtflrvran rqtrlnarig kmkrrkqdeg qvcplcsrpl agseqemsrh vehclskreg
      361 scvaeddavd iehensnrfe eyewcgqkri rattlleggf rgsgfvmcsg kenpdsdadl
      421 dvdgddtley gkpqyteadv ipctgeepge akerealrga vlnggppstr itpefskwas
      481 dempstsnge sskqeamqkt cknsdiekit edsavttfea lkarvreler qlsrgdrykc
      541 licmdsysmp ltsiqcwhvh ceecwlrtlg akklcpqcnt itapgdlrri yl
//
LOCUS       NP_001011930             432 aa            linear   ROD 17-APR-2025
DEFINITION  pachytene checkpoint protein 2 homolog [Rattus norvegicus].
ACCESSION   NP_001011930 XP_217741
VERSION     NP_001011930.1
DBSOURCE    REFSEQ: accession NM_001011930.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Yost,S., de Wolf,B., Hanks,S., Zachariou,A., Marcozzi,C.,
            Clarke,M., de Voer,R., Etemad,B., Uijttewaal,E., Ramsay,E.,
            Wylie,H., Elliott,A., Picton,S., Smith,A., Smithson,S., Seal,S.,
            Ruark,E., Houge,G., Pines,J., Kops,G.J.P.L. and Rahman,N.
  TITLE     Biallelic TRIP13 mutations predispose to Wilms tumor and chromosome
            missegregation
  JOURNAL   Nat Genet 49 (7), 1148-1151 (2017)
   PUBMED   28553959
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Roig,I., Dowdle,J.A., Toth,A., de Rooij,D.G., Jasin,M. and
            Keeney,S.
  TITLE     Mouse TRIP13/PCH2 is required for recombination and normal
            higher-order chromosome structure during meiosis
  JOURNAL   PLoS Genet 6 (8), e1001062 (2010)
   PUBMED   20711356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Li,X.C. and Schimenti,J.C.
  TITLE     Mouse pachytene checkpoint 2 (trip13) is required for completing
            meiotic recombination but not synapsis
  JOURNAL   PLoS Genet 3 (8), e130 (2007)
   PUBMED   17696610
  REMARK    Erratum:[PLoS Genet. 2007 Sep 7;3(9):e168. Li, Xin [corrected to
            Li, Xin Chenglin]]
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 11, 2005 this sequence version replaced XP_217741.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..432
                     /product="pachytene checkpoint protein 2 homolog"
                     /note="thyroid receptor-interacting protein 13; TRIP-13;
                     TR-interacting protein 13"
                     /calculated_mol_wt=48303
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q15645; propagated from
                     UniProtKB/Swiss-Prot (Q5XHZ9.1)"
     Region          34..>205
                     /region_name="McrB"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, GTP-binding regulatory subunit McrB [Defense
                     mechanisms]; COG1401"
                     /db_xref="CDD:441011"
     Region          121..319
                     /region_name="RecA-like_Pch2-like"
                     /note="ATPase domain of Pachytene checkpoint 2 (Pch2) and
                     similar ATPase domains; cd19508"
                     /db_xref="CDD:410916"
     Site            order(134,151..152,155..156,162..165,167..171,215,
                     217..218,224,311)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:410916"
     Site            order(180,184..186,211,213..214,252..253)
                     /site_type="active"
                     /note="ATP binding site [active]"
                     /db_xref="CDD:410916"
     CDS             1..432
                     /gene="Trip13"
                     /coded_by="NM_001011930.2:128..1426"
                     /db_xref="GeneID:292206"
                     /db_xref="RGD:1308516"
ORIGIN      
        1 mddavgdlkq alpcvaespa vhvevlqrsg stakkedikq svyrllkrhn ivfgdyvwte
       61 fdepfltrnv qsvsivdtel kakdpqpidl sactialhif qlneegpsse nldeetenii
      121 aashwvlpaa efhglwdslv ydvevkshll dyvmttllfs dknvdsnlit wnrvvllhgp
      181 pgtgktslck alaqkltirl ssryrygqli einshslfsk wfsesgklvt kmfqkiqdli
      241 ddkealvfvl idevesltaa rnacragaep sdairvvnav ltqidqikrh snvvilttsn
      301 itekidvafv dradikqyig ppsaaaifki ylscleelmk cqiiyprqql ltlrelemig
      361 fiennvskls lllseisrks eglsgrvlrk lpflahalyi qapsvtiegf lqalslavdk
      421 qfeekkklsa hv
//
LOCUS       NP_001425247             537 aa            linear   ROD 17-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 6
            [Rattus norvegicus].
ACCESSION   NP_001425247 XP_063140774
VERSION     NP_001425247.1
DBSOURCE    REFSEQ: accession NM_001438318.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063140774.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1311007.1,
                                           SRR26643293.3958.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..537
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 6"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=59411
     Region          17..317
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          319..391
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          402..485
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          479..534
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..537
                     /gene="Cpeb1"
                     /coded_by="NM_001438318.1:179..1792"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 mwprgclsaf lsrqgqeees grikdcwdnq evpalstcsn anifrrinai lddsldfskv
       61 cttpinrgih dqlpdfqdse eaitsrmlfp tsaqesprgl pdanglclgl qslsltgwdr
      121 pwstqdsdss aqsntqsvls mlqnplgnvl gktplsflsl dplgsdldkf papsvrgsrl
      181 dtrpildsrs sspsdsdtsg fssgsdhlsd lisslrispp lpflsmtgng prdplkmgvg
      241 srmdqeqaal aavapsptsa pkrwpgtsvw pswdllgapk dpfsierear lhrqaaavne
      301 atctwsgqlp prnyknpiys ckvflggvpw ditegyvylv feleksvral lqacshdpls
      361 pdglseyyfk mssrrmrcke vqvipwvlad snfvwspsqr ldpsrtvfvg alhgmlnaea
      421 laailndlfg gvvyagidtd khkypigsgr vtfnnqrsyl kavtaafvei kttkftkkvq
      481 idpyledslc licssqpgpf fcrdqvcfky fcrscwhwrh smeglrhhsp lmrnqkn
//
LOCUS       NP_001425233             566 aa            linear   ROD 17-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF220 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425233 XP_017449287
VERSION     NP_001425233.1
DBSOURCE    REFSEQ: accession NM_001438304.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Ma,P., Yang,X., Kong,Q., Li,C., Yang,S., Li,Y. and Mao,B.
  TITLE     The ubiquitin ligase RNF220 enhances canonical Wnt signaling
            through USP7-mediated deubiquitination of beta-catenin
  JOURNAL   Mol Cell Biol 34 (23), 4355-4366 (2014)
   PUBMED   25266658
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Kong,Q., Zeng,W., Wu,J., Hu,W., Li,C. and Mao,B.
  TITLE     RNF220, an E3 ubiquitin ligase that targets Sin3B for
            ubiquitination
  JOURNAL   Biochem Biophys Res Commun 393 (4), 708-713 (2010)
   PUBMED   20170641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 17, 2025 this sequence version replaced XP_017449287.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19820.1,
                                           SRR26643298.28542.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..566
                     /product="E3 ubiquitin-protein ligase RNF220 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF220"
                     /calculated_mol_wt=62589
     Region          217..444
                     /region_name="RNF220"
                     /note="E3 ubiquitin-protein ligase RNF220; pfam15926"
                     /db_xref="CDD:464946"
     Region          512..563
                     /region_name="RING-HC_RNF220"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 220 (RNF220) and similar proteins; cd16563"
                     /db_xref="CDD:438225"
     CDS             1..566
                     /gene="Rnf220"
                     /coded_by="NM_001438304.1:464..2164"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:500532"
                     /db_xref="RGD:1598210"
ORIGIN      
        1 mdlhraafkm enssylpnpl aspalmvlas taeasrdasi pcqqprpfgv pvsvdkdvhi
       61 pftngsytfa smyhrqggvp gtfanrdfpp sllhlhpqfa ppnldctpis mlnhsgvgaf
      121 rpfastedre syqsaftpak rlknchdses phlrfsdadg keydfgtqlp ssspgslkvd
      181 dtgkkifavs glisdretss spedrndrck kkavalfdsq apicpicqvl lrpselqehm
      241 eqeleqlaql pasknsllkd amapgtpksl llsasikreg dsptasphss atedlhhsdr
      301 yqtflrvran rqtrlnarig kmkrrkqdeg qregscvaed davdiehens nrfeeyewcg
      361 qkrirattll eggfrgsgfv mcsgkenpds dadldvdgdd tleygkpqyt eadvipctge
      421 epgeakerea lrgavlnggp pstritpefs kwasdempst sngesskqea mqktcknsdi
      481 ekitedsavt tfealkarvr elerqlsrgd rykclicmds ysmpltsiqc whvhceecwl
      541 rtlgakklcp qcntitapgd lrriyl
//
LOCUS       NP_001425186            1173 aa            linear   ROD 17-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425186 XP_063138857
VERSION     NP_001425186.1
DBSOURCE    REFSEQ: accession NM_001438257.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138857.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.437702.1,
                                           SRR26643293.9500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1173
                     /product="tudor domain-containing protein 1 isoform 1"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=129863
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1052
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     Site            order(994,999,1001,1017,1020,1022)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410449"
     CDS             1..1173
                     /gene="Tdrd1"
                     /coded_by="NM_001438257.1:86..3607"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnddfw yraivleasd sdvkvlyady
     1021 gnverlpfsr vqpitashlq lpfriircsl egltelngss sqpvmellrn amlnqsvals
     1081 vkavsknvha vsvekcseng miniaenlvm cglaenlssk resastketp hstdccctel
     1141 qkqiekheqi llfllnnptn qnkfiemkkl lqs
//
LOCUS       NP_001425234             282 aa            linear   ROD 17-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF220 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001425234 XP_008762301
VERSION     NP_001425234.1
DBSOURCE    REFSEQ: accession NM_001438305.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Ma,P., Yang,X., Kong,Q., Li,C., Yang,S., Li,Y. and Mao,B.
  TITLE     The ubiquitin ligase RNF220 enhances canonical Wnt signaling
            through USP7-mediated deubiquitination of beta-catenin
  JOURNAL   Mol Cell Biol 34 (23), 4355-4366 (2014)
   PUBMED   25266658
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Kong,Q., Zeng,W., Wu,J., Hu,W., Li,C. and Mao,B.
  TITLE     RNF220, an E3 ubiquitin ligase that targets Sin3B for
            ubiquitination
  JOURNAL   Biochem Biophys Res Commun 393 (4), 708-713 (2010)
   PUBMED   20170641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 17, 2025 this sequence version replaced XP_008762301.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29546.1,
                                           SRR26643298.28544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..282
                     /product="E3 ubiquitin-protein ligase RNF220 isoform 4"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF220"
                     /calculated_mol_wt=31687
     Region          <15..160
                     /region_name="RNF220"
                     /note="E3 ubiquitin-protein ligase RNF220; pfam15926"
                     /db_xref="CDD:464946"
     Region          228..279
                     /region_name="RING-HC_RNF220"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 220 (RNF220) and similar proteins; cd16563"
                     /db_xref="CDD:438225"
     CDS             1..282
                     /gene="Rnf220"
                     /coded_by="NM_001438305.1:195..1043"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:500532"
                     /db_xref="RGD:1598210"
ORIGIN      
        1 mprarsgrrs reaggreetf lrvranrqtr lnarigkmkr rkqdegqreg scvaeddavd
       61 iehensnrfe eyewcgqkri rattlleggf rgsgfvmcsg kenpdsdadl dvdgddtley
      121 gkpqyteadv ipctgeepge akerealrga vlnggppstr itpefskwas dempstsnge
      181 sskqeamqkt cknsdiekit edsavttfea lkarvreler qlsrgdrykc licmdsysmp
      241 ltsiqcwhvh ceecwlrtlg akklcpqcnt itapgdlrri yl
//
LOCUS       NP_001425196             646 aa            linear   ROD 17-APR-2025
DEFINITION  zinc finger protein 418 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425196
VERSION     NP_001425196.1
DBSOURCE    REFSEQ: accession NM_001438267.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Singh,S.R., Meyer-Jens,M., Alizoti,E., Bacon,W.C., Davis,G.,
            Osinska,H., Gulick,J., Reischmann-Dusener,S., Orthey,E.,
            McLendon,P.M., Molkentin,J.D., Schlossarek,S., Robbins,J. and
            Carrier,L.
  TITLE     A high-throughput screening identifies ZNF418 as a novel regulator
            of the ubiquitin-proteasome system and autophagy-lysosomal pathway
  JOURNAL   Autophagy 17 (10), 3124-3139 (2021)
   PUBMED   33249983
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Pan,L., Sheng,M., Huang,Z., Zhu,Z., Xu,C., Teng,L., He,L., Gu,C.,
            Yi,C. and Li,J.
  TITLE     Zinc-finger protein 418 overexpression protects against cardiac
            hypertrophy and fibrosis
  JOURNAL   PLoS One 12 (10), e0186635 (2017)
   PUBMED   29065170
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212491.1, SRR26360194.1229427.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..646
                     /product="zinc finger protein 418 isoform 3"
                     /calculated_mol_wt=74889
     Region          <21..50
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(257,259,261,263..264,267..268,271,285,287,291..292,
                     295..296,299,313,315,317,319..320,323..324,327)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          276..633
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(369,371,373,375..376,379..380,383,397,399,403..404,
                     407..408,411,425,427,429,431..432,435..436,439)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          560..580
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(565,567,569,571..572,575..576,579,593,595,599..600,
                     603..604,607,621,623,625,627..628,631..632,635)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          588..608
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          616..636
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..646
                     /gene="Zfp418"
                     /gene_synonym="RGD1311663; ZNF418"
                     /coded_by="NM_001438267.1:178..2118"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:292548"
                     /db_xref="RGD:1311663"
ORIGIN      
        1 maavkhlaqi prctetgmic tqeewkllde aqrllyldvm lenftlissl vyryeaeaee
       61 ktcaqslsqt eapqvrtpkq gqlrqkphps dicitvlkdi lhlndlpgqk pyltevctkp
      121 qdhkhhrakn wlkrdvdslv kscifhvagn pficskigek fpaiwnllqp kdipngekqn
      181 kikrgkafhr dknnsesdey kkssspqhrl heypgvcsak ggfesnsceq dlnkyspapf
      241 rmdqtenrpy echvcgkwfg qkatlrihqr rhtgekpykc gecgksfcqs snlsehcrvh
      301 sgerpfecle cgkafgchss llrhqrthtg ewpyecsdcg rlfrqivsli thqrthttek
      361 pyecgqceks fshkatltvh qrvhtgekpy hceacgksfs qsanlikhsk ihtgekpyec
      421 gecglcfrqr atlmkhqrth tserpyecre cgkffkqyfy liehrrihtt tefyeceqcg
      481 ksytqkatli rhqrvhtges pykceecgka feyksrlkrh qrthtgerpy ecakcgkffr
      541 esynlaehqk ihtkakpyhc dqcgkcfsrr adlvkhqrvh tgerpytcge cgktfsrttn
      601 lvqhrrihtg erpyecdqcg ksfsqvstlt rhqllhtgek pykcsk
//
LOCUS       NP_001425245             567 aa            linear   ROD 17-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001425245 XP_063140762
VERSION     NP_001425245.1
DBSOURCE    REFSEQ: accession NM_001438316.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063140762.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.392950.1,
                                           SRR26360172.2087927.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..567
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 3"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=62673
     Region          17..317
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          319..421
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          432..515
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          509..564
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..567
                     /gene="Cpeb1"
                     /coded_by="NM_001438316.1:179..1882"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 mwprgclsaf lsrqgqeees grikdcwdnq evpalstcsn anifrrinai lddsldfskv
       61 cttpinrgih dqlpdfqdse eaitsrmlfp tsaqesprgl pdanglclgl qslsltgwdr
      121 pwstqdsdss aqsntqsvls mlqnplgnvl gktplsflsl dplgsdldkf papsvrgsrl
      181 dtrpildsrs sspsdsdtsg fssgsdhlsd lisslrispp lpflsmtgng prdplkmgvg
      241 srmdqeqaal aavapsptsa pkrwpgtsvw pswdllgapk dpfsierear lhrqaaavne
      301 atctwsgqlp prnyknpiys ckvflggvpw diteaglvnt frvfgslsve wpgkdgkhpr
      361 cppkgyvylv feleksvral lqacshdpls pdglseyyfk mssrrmrcke vqvipwvlad
      421 snfvwspsqr ldpsrtvfvg alhgmlnaea laailndlfg gvvyagidtd khkypigsgr
      481 vtfnnqrsyl kavtaafvei kttkftkkvq idpyledslc licssqpgpf fcrdqvcfky
      541 fcrscwhwrh smeglrhhsp lmrnqkn
//
LOCUS       NP_001425250             408 aa            linear   ROD 17-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 9
            [Rattus norvegicus].
ACCESSION   NP_001425250 XP_063140807
VERSION     NP_001425250.1
DBSOURCE    REFSEQ: accession NM_001438321.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063140807.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.22560.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..408
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 9"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=45789
     Region          17..>182
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          160..262
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          273..356
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          350..405
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..408
                     /gene="Cpeb1"
                     /coded_by="NM_001438321.1:179..1405"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 mwprgclsaf lsrqgqeees grikdcwdnq evpalstcsn anifrrinai lddsldfskv
       61 cttpinrgih dqlpdfqdse eaitsrmlfp tsaqesprgl pdanglclgl qslsltgwdr
      121 pwstqdsdss aqsntqsavn eatctwsgql pprnyknpiy sckvflggvp wditeaglvn
      181 tfrvfgslsv ewpgkdgkhp rcppkgyvyl vfeleksvra llqacshdpl spdglseyyf
      241 kmssrrmrck evqvipwvla dsnfvwspsq rldpsrtvfv galhgmlnae alaailndlf
      301 ggvvyagidt dkhkypigsg rvtfnnqrsy lkavtaafve ikttkftkkv qidpyledsl
      361 clicssqpgp ffcrdqvcfk yfcrscwhwr hsmeglrhhs plmrnqkn
//
LOCUS       NP_001425268             584 aa            linear   ROD 17-APR-2025
DEFINITION  coiled-coil domain-containing protein 17 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425268 XP_038966519
VERSION     NP_001425268.1
DBSOURCE    REFSEQ: accession NM_001438339.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Kang,B.W., Jeon,H.S., Chae,Y.S., Lee,S.J., Park,J.S., Choi,G.S. and
            Kim,J.G.
  TITLE     Impact of Genetic Variation in MicroRNA-binding Site on
            Susceptibility to Colorectal Cancer
  JOURNAL   Anticancer Res 36 (7), 3353-3361 (2016)
   PUBMED   27354594
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Shultz,M.A., Zhang,L., Gu,Y.Z., Baker,G.L., Fannuchi,M.V.,
            Padua,A.M., Gurske,W.A., Morin,D., Penn,S.G., Jovanovich,S.B.,
            Plopper,C.G. and Buckpitt,A.R.
  TITLE     Gene expression analysis in response to lung toxicants: I.
            Sequencing and microarray development
  JOURNAL   Am J Respir Cell Mol Biol 30 (3), 296-310 (2004)
   PUBMED   12947022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 17, 2025 this sequence version replaced XP_038966519.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.145050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..584
                     /product="coiled-coil domain-containing protein 17 isoform
                     2"
                     /note="coiled-coil domain-containing protein 17"
                     /calculated_mol_wt=64674
     CDS             1..584
                     /gene="Ccdc17"
                     /coded_by="NM_001438339.1:146..1900"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500528"
                     /db_xref="RGD:1598211"
ORIGIN      
        1 madysgksgl lpcescdmvf rsrallakht krfciggltp eimaqeqrrs dqeatksslk
       61 rlteekigpw atdtsqtags peerlrdlqg trarrveete aqsralkqrg eelkrrlhsv
      121 agpkgglprp ivlerelrel reeasrtrga lqtlgarvqa lqpqpahqqd akrvvefccl
      181 plrynpetla eeirvlrevy vrgggrdpev ldkilqlqve asalelrrsq nrkekasaas
      241 eealmveaen rileaeilal qkqkvlslsp wgsrdlwrhl srrsdnsllp ppvappmppv
      301 tsstkvqdfh gtskaiingt mtrnlgldlh flpasnvlgp apydpgaglv ifydflrgle
      361 aswiwvqlmt slardgqdtg gatalppalc lpppsasgpi gncailasrq pvprlppspl
      421 lslicklqaw qgvtwtpqpk awaslllfdq slrvlsgrwr lplrvpptts lsfaqmnemp
      481 qvsvegrdwl hpkipmeyhf lcqagqaelf lrlvnardtd aqtlaeinpa saheyqyppm
      541 msssssless ffthssgiad ppppteetfv svedkdehls phqf
//
LOCUS       NP_446193                105 aa            linear   ROD 17-APR-2025
DEFINITION  ras-related protein Rap-2a isoform 2 [Rattus norvegicus].
ACCESSION   NP_446193
VERSION     NP_446193.1
DBSOURCE    REFSEQ: accession NM_053741.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Hu,Y., Hong,X.Y., Yang,X.F., Ma,R.H., Wang,X., Zhang,J.F., Feng,Q.,
            Li,X.G., Sun,D.S., Li,X., Wan,H.L., Li,T., Wang,Q., Ke,D.,
            Wang,J.Z. and Liu,G.P.
  TITLE     Inflammation-dependent ISG15 upregulation mediates MIA-induced
            dendrite damages and depression by disrupting NEDD4/Rap2A signaling
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (6), 1477-1489 (2019)
   PUBMED   30826466
  REMARK    GeneRIF: The data revealed that maternal immune activation impedes
            offspring's dendrite development and causes depressive like
            behaviors by upregulating ISG15 and suppressing NEDD4/Rap2A
            signaling.
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Emery,A.C., Xu,W., Eiden,M.V. and Eiden,L.E.
  TITLE     Guanine nucleotide exchange factor Epac2-dependent activation of
            the GTP-binding protein Rap2A mediates cAMP-dependent growth arrest
            in neuroendocrine cells
  JOURNAL   J Biol Chem 292 (29), 12220-12231 (2017)
   PUBMED   28546426
  REMARK    GeneRIF: Data suggest that Rap2A is the obligate effector for Epac2
            in mediating growth arrest and reversal of neurite extension
            through activation of MAP kinase signaling via protein
            phosphorylation/farnesylation in neuroendocrine cells. (Rap2A = RAS
            oncogene family member Rap2A; Epac2 = guanine nucleotide exchange
            factor Epac2)
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Kawabe,H., Neeb,A., Dimova,K., Young,S.M. Jr., Takeda,M.,
            Katsurabayashi,S., Mitkovski,M., Malakhova,O.A., Zhang,D.E.,
            Umikawa,M., Kariya,K., Goebbels,S., Nave,K.A., Rosenmund,C.,
            Jahn,O., Rhee,J. and Brose,N.
  TITLE     Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls
            neurite development
  JOURNAL   Neuron 65 (3), 358-372 (2010)
   PUBMED   20159449
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Uechi,Y., Bayarjargal,M., Umikawa,M., Oshiro,M., Takei,K.,
            Yamashiro,Y., Asato,T., Endo,S., Misaki,R., Taguchi,T. and
            Kariya,K.
  TITLE     Rap2 function requires palmitoylation and recycling endosome
            localization
  JOURNAL   Biochem Biophys Res Commun 378 (4), 732-737 (2009)
   PUBMED   19061864
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Taira,K., Umikawa,M., Takei,K., Myagmar,B.E., Shinzato,M.,
            Machida,N., Uezato,H., Nonaka,S. and Kariya,K.
  TITLE     The Traf2- and Nck-interacting kinase as a putative effector of
            Rap2 to regulate actin cytoskeleton
  JOURNAL   J Biol Chem 279 (47), 49488-49496 (2004)
   PUBMED   15342639
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Machida,N., Umikawa,M., Takei,K., Sakima,N., Myagmar,B.E.,
            Taira,K., Uezato,H., Ogawa,Y. and Kariya,K.
  TITLE     Mitogen-activated protein kinase kinase kinase kinase 4 as a
            putative effector of Rap2 to activate the c-Jun N-terminal kinase
  JOURNAL   J Biol Chem 279 (16), 15711-15714 (2004)
   PUBMED   14966141
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Menetrey,J. and Cherfils,J.
  TITLE     Structure of the small G protein Rap2 in a non-catalytic complex
            with GTP
  JOURNAL   Proteins 37 (3), 465-473 (1999)
   PUBMED   10591105
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Cherfils,J., Menetrey,J., Le Bras,G., Janoueix-Lerosey,I., de
            Gunzburg,J., Garel,J.R. and Auzat,I.
  TITLE     Crystal structures of the small G protein Rap2A in complex with its
            substrate GTP, with GDP and with GTPgammaS
  JOURNAL   EMBO J 16 (18), 5582-5591 (1997)
   PUBMED   9312017
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Lerosey,I., Chardin,P., de Gunzburg,J. and Tavitian,A.
  TITLE     The product of the rap2 gene, member of the ras superfamily.
            Biochemical characterization and site-directed mutagenesis
  JOURNAL   J Biol Chem 266 (7), 4315-4321 (1991)
   PUBMED   1900290
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR21887622.3512172.1, AY037826.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24"
     Protein         1..105
                     /product="ras-related protein Rap-2a isoform 2"
                     /EC_number="3.6.5.2"
                     /note="rap2A-like protein; ras-related protein Rap-2a; RAS
                     related protein 2a inverted question mark"
                     /calculated_mol_wt=11814
     Region          16..>105
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            38..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(59..60,76..77)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     CDS             1..105
                     /gene="Rap2a"
                     /coded_by="NM_053741.2:273..590"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:114560"
                     /db_xref="RGD:620590"
ORIGIN      
        1 mreykvvvlg sggvgksalt vqfvtgtfie kydptiedfy rkeievdssp svleildtag
       61 teqfasmrdl yikngqgfil vyslvnqqsf qdikpmrdqi irvkr
//
LOCUS       NP_001178891             678 aa            linear   ROD 17-APR-2025
DEFINITION  G-protein-signaling modulator 2 [Rattus norvegicus].
ACCESSION   NP_001178891 XP_008759631 XP_575015
VERSION     NP_001178891.1
DBSOURCE    REFSEQ: accession NM_001191962.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Chiu,C.W.N., Monat,C., Robitaille,M., Lacomme,M., Daulat,A.M.,
            Macleod,G., McNeill,H., Cayouette,M. and Angers,S.
  TITLE     SAPCD2 Controls Spindle Orientation and Asymmetric Divisions by
            Negatively Regulating the Galphai-LGN-NuMA Ternary Complex
  JOURNAL   Dev Cell 36 (1), 50-62 (2016)
   PUBMED   26766442
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Bird,S.L., Heald,R. and Weis,K.
  TITLE     RanGTP and CLASP1 cooperate to position the mitotic spindle
  JOURNAL   Mol Biol Cell 24 (16), 2506-2514 (2013)
   PUBMED   23783028
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Kiyomitsu,T. and Cheeseman,I.M.
  TITLE     Cortical dynein and asymmetric membrane elongation coordinately
            position the spindle in anaphase
  JOURNAL   Cell 154 (2), 391-402 (2013)
   PUBMED   23870127
  REMARK    Erratum:[Cell. 2013 Sep 12;154(6):1401]
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Jia,M., Li,J., Zhu,J., Wen,W., Zhang,M. and Wang,W.
  TITLE     Crystal structures of the scaffolding protein LGN reveal the
            general mechanism by which GoLoco binding motifs inhibit the
            release of GDP from Galphai
  JOURNAL   J Biol Chem 287 (44), 36766-36776 (2012)
   PUBMED   22952234
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Kotak,S., Busso,C. and Gonczy,P.
  TITLE     Cortical dynein is critical for proper spindle positioning in human
            cells
  JOURNAL   J Cell Biol 199 (1), 97-110 (2012)
   PUBMED   23027904
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Walsh,T., Shahin,H., Elkan-Miller,T., Lee,M.K., Thornton,A.M.,
            Roeb,W., Abu Rayyan,A., Loulus,S., Avraham,K.B., King,M.C. and
            Kanaan,M.
  TITLE     Whole exome sequencing and homozygosity mapping identify mutation
            in the cell polarity protein GPSM2 as the cause of nonsyndromic
            hearing loss DFNB82
  JOURNAL   Am J Hum Genet 87 (1), 90-94 (2010)
   PUBMED   20602914
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Izaki,T., Kamakura,S., Kohjima,M. and Sumimoto,H.
  TITLE     Two forms of human Inscuteable-related protein that links Par3 to
            the Pins homologues LGN and AGS3
  JOURNAL   Biochem Biophys Res Commun 341 (4), 1001-1006 (2006)
   PUBMED   16458856
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Sans,N., Wang,P.Y., Du,Q., Petralia,R.S., Wang,Y.X., Nakka,S.,
            Blumer,J.B., Macara,I.G. and Wenthold,R.J.
  TITLE     mPins modulates PSD-95 and SAP102 trafficking and influences NMDA
            receptor surface expression
  JOURNAL   Nat Cell Biol 7 (12), 1179-1190 (2005)
   PUBMED   16299499
  REMARK    Erratum:[Nat Cell Biol. 2006 Jan;8(1):100]
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Du,Q. and Macara,I.G.
  TITLE     Mammalian Pins is a conformational switch that links NuMA to
            heterotrimeric G proteins
  JOURNAL   Cell 119 (4), 503-516 (2004)
   PUBMED   15537540
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Du,Q., Stukenberg,P.T. and Macara,I.G.
  TITLE     A mammalian Partner of inscuteable binds NuMA and regulates mitotic
            spindle organization
  JOURNAL   Nat Cell Biol 3 (12), 1069-1075 (2001)
   PUBMED   11781568
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_008759631.1, XP_575015.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.11018.1,
                                           SRR26643286.8603.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..678
                     /product="G-protein-signaling modulator 2"
                     /note="G-protein signalling modulator 2 (AGS3-like, C.
                     elegans); G-protein signaling modulator 2 (AGS3-like, C.
                     elegans)"
                     /calculated_mol_wt=75318
     Region          27..52
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          64..90
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          65..335
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(66..67,70..71,73,103,106..107,110..111,113..114,143,
                     146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          101..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          203..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(243,246..247,250..251,253,283,286..287,290..291,
                     293..294,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          243..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          281..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          322..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          324..359
                     /region_name="TPR_7"
                     /note="Tetratricopeptide repeat; pfam13176"
                     /db_xref="CDD:433012"
     Region          490..512
                     /region_name="GoLoco"
                     /note="LGN motif, putative GEFs specific for G-alpha
                     GTPases; smart00390"
                     /db_xref="CDD:214645"
     Region          543..564
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          593..615
                     /region_name="GoLoco"
                     /note="LGN motif, putative GEFs specific for G-alpha
                     GTPases; smart00390"
                     /db_xref="CDD:214645"
     Region          628..649
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     CDS             1..678
                     /gene="Gpsm2"
                     /gene_synonym="RGD1560967"
                     /coded_by="NM_001191962.2:508..2544"
                     /db_xref="GeneID:362021"
                     /db_xref="RGD:1560967"
ORIGIN      
        1 megnlmsmre dhsfhvryrm easclelale gerlcksgdc ragvsffeaa vqvgtedlkt
       61 lsaiysqlgn ayfylhdyak aleyhhhdlt lartigdqlg eakasgnlgn tlkvlgnfde
      121 aivccqrhld isrelndkvg earalynlgn vyhakgksfg cpgpqdvgef peevrlalqa
      181 avelyeenls lvtalgdraa qgrafgnlgn thyllgnfrd aviaheqrll iakefgdkaa
      241 erraysnlgn ayiflgefet aseyyrktll larqlkdrav eaqscyslgn tytllqdyek
      301 aieyhlkhla iaqelkdrig egracwslgn aytalgnhdq amhfaekhle isrevgdksg
      361 eltarlnlsd lqmvlglsys tnnsmmseni eidgslhgag tklgrrhsme nmelmkltpe
      421 kvpnwnseil akqkpciaks sakllfvnrl kgkksksgsa stkalhhasn pidhraphaq
      481 kkvgsdavgd egffdllrrl qssrmedqrc hlqenrtasv aassatpkmv kapsasvvsp
      541 ntdefldlla ssqsrrlddq rasfsnlpgl rltegnnqsv lerlmtndkk epdedffdil
      601 vkcqgsrldd qrcapppaat kgptvpdedf fslilrsqak rmdeqrvllq rdpnrdsefg
      661 lkellqnnal lefkhsgk
//
LOCUS       NP_478115                198 aa            linear   ROD 17-APR-2025
DEFINITION  suppressor of cytokine signaling 2 [Rattus norvegicus].
ACCESSION   NP_478115 XP_017450626
VERSION     NP_478115.1
DBSOURCE    REFSEQ: accession NM_058208.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Sheng,M., Huang,Z., Pan,L., Yu,M., Yi,C., Teng,L., He,L., Gu,C.,
            Xu,C. and Li,J.
  TITLE     SOCS2 exacerbates myocardial injury induced by ischemia/reperfusion
            in diabetic mice and H9c2 cells through inhibiting the
            JAK-STAT-IGF-1 pathway
  JOURNAL   Life Sci 188, 101-109 (2017)
   PUBMED   28867579
  REMARK    GeneRIF: research suggests that overexpressed SOCS2 might
            exacerbate myocardial ischemia/reperfusion injury in type 2
            diabetes mellitus by inhibiting the expression of Insulin-like
            Growth Factor-1 via the Janus kinase-signal transducer and
            activator of transcription signaling pathway.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Choi,J.S., Shin,Y.J., Lee,J.Y., Choi,J.Y., Cha,J.H., Chun,M.H. and
            Lee,M.Y.
  TITLE     Enhanced expression of SOCS-2 in the rat hippocampus after
            transient forebrain ischemia
  JOURNAL   J Neurotrauma 26 (11), 2097-2106 (2009)
   PUBMED   19469688
  REMARK    GeneRIF: SOCS-2 may be involved in glial reactions, and possibly
            adult hippocampal neurogenesis during ischemic insults.
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Isshiki,K., He,Z., Maeno,Y., Ma,R.C., Yasuda,Y., Kuroki,T.,
            White,G.S., Patti,M.E., Weir,G.C. and King,G.L.
  TITLE     Insulin regulates SOCS2 expression and the mitogenic effect of
            IGF-1 in mesangial cells
  JOURNAL   Kidney Int 74 (11), 1434-1443 (2008)
   PUBMED   19008912
  REMARK    GeneRIF: insulin can inhibit the mitogenic action of IGF-1 in
            mesangial cells by regulating STAT5/SOCS2 expression.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Hamilton,K.L., Lin,L., Wang,Y. and Knowlton,A.A.
  TITLE     Effect of ovariectomy on cardiac gene expression: inflammation and
            changes in SOCS gene expression
  JOURNAL   Physiol Genomics 32 (2), 254-263 (2008)
   PUBMED   17986523
  REMARK    GeneRIF: Data show that althhough we observed OVX-related increases
            in SOCS2 and SOCS3 mRNA, SOCS2 and SOCS3 protein did not differ
            among groups.
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Haffner,M.C., Petridou,B., Peyrat,J.P., Revillion,F.,
            Muller-Holzner,E., Daxenbichler,G., Marth,C. and Doppler,W.
  TITLE     Favorable prognostic value of SOCS2 and IGF-I in breast cancer
  JOURNAL   BMC Cancer 7, 136 (2007)
   PUBMED   17651480
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Lindeman,G.J., Wittlin,S., Lada,H., Naylor,M.J., Santamaria,M.,
            Zhang,J.G., Starr,R., Hilton,D.J., Alexander,W.S., Ormandy,C.J. and
            Visvader,J.
  TITLE     SOCS1 deficiency results in accelerated mammary gland development
            and rescues lactation in prolactin receptor-deficient mice
  JOURNAL   Genes Dev 15 (13), 1631-1636 (2001)
   PUBMED   11445538
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Johnson,T.S., O'Leary,M., Justice,S.K., Maamra,M.,
            Zarkesh-Esfahani,S.H., Furlanetto,R., Preedy,V.R., Hinds,C.J., El
            Nahas,A.M. and Ross,R.J.
  TITLE     Differential expression of suppressors of cytokine signalling genes
            in response to nutrition and growth hormone in the septic rat
  JOURNAL   J Endocrinol 169 (2), 409-415 (2001)
   PUBMED   11312157
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Horvat,S. and Medrano,J.F.
  TITLE     Lack of Socs2 expression causes the high-growth phenotype in mice
  JOURNAL   Genomics 72 (2), 209-212 (2001)
   PUBMED   11401434
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Mao,Y., Ling,P.R., Fitzgibbons,T.P., McCowen,K.C., Frick,G.P.,
            Bistrian,B.R. and Smith,R.J.
  TITLE     Endotoxin-induced inhibition of growth hormone receptor signaling
            in rat liver in vivo
  JOURNAL   Endocrinology 140 (12), 5505-5515 (1999)
   PUBMED   10579313
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Dey,B.R., Spence,S.L., Nissley,P. and Furlanetto,R.W.
  TITLE     Interaction of human suppressor of cytokine signaling (SOCS)-2 with
            the insulin-like growth factor-I receptor
  JOURNAL   J Biol Chem 273 (37), 24095-24101 (1998)
   PUBMED   9727029
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017450626.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.20038.1,
                                           SRR26643293.39615.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840110,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..198
                     /product="suppressor of cytokine signaling 2"
                     /note="cytokine-inducible SH2 protein 2; cytokine
                     inducible SH2-containing protein 2"
                     /calculated_mol_wt=22248
     Region          1..75
                     /region_name="Interaction with AREL1.
                     /evidence=ECO:0000250|UniProtKB:O14508"
                     /note="propagated from UniProtKB/Swiss-Prot (O88582.1)"
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88582.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14508; propagated from
                     UniProtKB/Swiss-Prot (O88582.1)"
     Region          40..142
                     /region_name="SH2_SOCS2"
                     /note="Src homology 2 (SH2) domain found in suppressor of
                     cytokine signaling (SOCS) proteins; cd10383"
                     /db_xref="CDD:198246"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14508; propagated from
                     UniProtKB/Swiss-Prot (O88582.1)"
     Site            order(55,73,75,83,96)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198246"
     Site            order(106,108,129)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198246"
     Region          158..198
                     /region_name="SOCS"
                     /note="SOCS (suppressors of cytokine signaling) box. The
                     SOCS box is found in the C-terminal region of CIS/SOCS
                     family proteins (in combination with a SH2 domain), ASBs
                     (ankyrin repeat-containing proteins with a SOCS box), SSBs
                     (SPRY domain-containing proteins...; cl02533"
                     /db_xref="CDD:470605"
     Site            order(159..164,170,175,181)
                     /site_type="active"
                     /note="elongin B/C interaction [active]"
                     /db_xref="CDD:239641"
     CDS             1..198
                     /gene="Socs2"
                     /gene_synonym="Cish2; Socs-2"
                     /coded_by="NM_058208.3:410..1006"
                     /db_xref="GeneID:84607"
                     /db_xref="RGD:69273"
ORIGIN      
        1 mtlrclepsg ngadrtrsqw gtagspedqs peaarlakal relsqtgwyw gsmtvneake
       61 klkeapegtf lirdsshsdy lltisvktsa gptnlrieyq dgkfrldsii cvksklkqfd
      121 svvhlidyyv qmckdkrtgp eaprngtvhl yltkplytsa ptlqhfcrls inkctgtirg
      181 lplptrlkdy leeykfqv
//
LOCUS       NP_001425030             670 aa            linear   ROD 17-APR-2025
DEFINITION  proline and serine-rich protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425030 XP_008757390
VERSION     NP_001425030.1
DBSOURCE    REFSEQ: accession NM_001438101.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_008757390.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.1585.1,
                                           SRR26360186.2789992.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..670
                     /product="proline and serine-rich protein 3 isoform 2"
                     /note="proline and serine-rich protein 3; uncharacterized
                     protein C19orf55 homolog"
                     /calculated_mol_wt=70110
     Region          <218..513
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          587..>631
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     CDS             1..670
                     /gene="Proser3"
                     /gene_synonym="RGD1565712"
                     /coded_by="NM_001438101.1:133..2145"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:361541"
                     /db_xref="RGD:1565712"
ORIGIN      
        1 mfpkvdnpld hqeartgatr sqkpqapkat aansaelsee swpsssgtas ppsttegqst
       61 sppltlidne dsvvakyinr frkaqptsre drqpvgptpa dfwwlqpass dlsshlaaga
      121 geptgrsavt gpcptgmsst slasvplqrv kqslnswnsa mleletlslq sraakllers
      181 kaslssssss pspneassss fpissdglsp csvtfnpdsn kssspkepvl gaapvpsqai
      241 paprpasaqa tlkpeedily qwrqrrkleq slqgagdgtw vlprtpaltt qtpvsavnlg
      301 skgtqpncap pwgsvaqppp pqafymerpp lsgpsphiwa pgthgvlwap qanpwiplgm
      361 vpttlltstl aplaslpvpp tstsaatapi sapqvsipgp pasapppcts apastvplpd
      421 npqgpttpel sssvhpkkls pkprcvsass rqettgpdta afespcsqlr galsqvvtar
      481 lfsdsledmp pseadsrkvk atssqakvpp pppesrrgsk tesrkskvtl saeagdpqpa
      541 tapkastlse vqslefkkst pkkgagdalt tappasshap sedllsqaar llqaaedsdg
      601 sefpedsvlr vlraqraelr qqkrnvdaql sllldhtedp gfsspparsp sssprmrlrr
      661 egaslearrp
//
LOCUS       NP_001424588             671 aa            linear   ROD 17-APR-2025
DEFINITION  calcium-responsive transcription factor isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424588
VERSION     NP_001424588.1
DBSOURCE    REFSEQ: accession NM_001437659.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Zheng,F., Zhou,X., Luo,Y., Xiao,H., Wayman,G. and Wang,H.
  TITLE     Regulation of brain-derived neurotrophic factor exon IV
            transcription through calcium responsive elements in cortical
            neurons
  JOURNAL   PLoS One 6 (12), e28441 (2011)
   PUBMED   22174809
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Hasan,M.K., Yaguchi,T., Sugihara,T., Kumar,P.K., Taira,K.,
            Reddel,R.R., Kaul,S.C. and Wadhwa,R.
  TITLE     CARF is a novel protein that cooperates with mouse p19ARF (human
            p14ARF) in activating p53
  JOURNAL   J Biol Chem 277 (40), 37765-37770 (2002)
   PUBMED   12154087
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Tao,X., West,A.E., Chen,W.G., Corfas,G. and Greenberg,M.E.
  TITLE     A calcium-responsive transcription factor, CaRF, that regulates
            neuronal activity-dependent expression of BDNF
  JOURNAL   Neuron 33 (3), 383-395 (2002)
   PUBMED   11832226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.73747.1,
                                           SRR26360176.1574172.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..671
                     /product="calcium-responsive transcription factor isoform
                     1"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 8; calcium-response factor;
                     amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8 protein"
                     /calculated_mol_wt=73651
     Region          201..433
                     /region_name="ALS2CR8"
                     /note="Amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 8; pfam15299"
                     /db_xref="CDD:464625"
     CDS             1..671
                     /gene="Carf"
                     /gene_synonym="Als2cr8"
                     /coded_by="NM_001437659.1:172..2187"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:301446"
                     /db_xref="RGD:1306822"
ORIGIN      
        1 mdsgdpslgq ndpptilpnt vpethdplts qnipetltdt qalheeqfhl ldqngqpiqy
       61 dlqslgnsta qmtgmeqvvi pqesfadvcs ppgvseekpi ggslpavstd aledsassys
      121 lhsqaslvgp rksgtrtlee pllaplqpls cntpmwacrl rscekigdsy rgycvsetel
      181 esvltfhkqq tqtvwgtrqs pspakpatrl mwksqyvpyd gipfvnagsr avvmecqygp
      241 rrkgfqlkki seqesrschl ykatcpariy ikkvqkfpdy rvptdpqidr ktirmeqeka
      301 ftmlkknlvd aggvlrwyvq lptqqahqyh epetpgvpls pspfpmsple eeeaiirden
      361 cvlpsrlhpq vahkiqelvs qgvgqvyavr kqlrkfvere lfkpdevper hnlsffptvn
      421 diknhihevq kslqtgdvvy nseiipatlq wttdsgnilr etvtvtfaeg nllkepitsk
      481 mgtsqtqtsl speplpllsp lssfqpkift hlqalklqpr lsspdgsqal vsvnshpsss
      541 ppgldtagna eannhslllg qsqnlgtdtc lpensstasp mgslpesvqn lvavdqlvgg
      601 edaedagnle gnvkrtllgd ahtipihild shpalveedt lsmnqvkqep neptlsteak
      661 tlldcknvsa t
//
LOCUS       NP_001424971            1383 aa            linear   ROD 17-APR-2025
DEFINITION  inactive cell surface hyaluronidase CEMIP2 [Rattus norvegicus].
ACCESSION   NP_001424971 XP_006231225
VERSION     NP_001424971.1
DBSOURCE    REFSEQ: accession NM_001438042.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1383)
  AUTHORS   Wu,M., Wang,C., Gong,Y., Huang,Y., Jiang,L., Zhang,M., Gao,R. and
            Dang,B.
  TITLE     Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury
  JOURNAL   Int J Mol Med 52 (6) (2023)
   PUBMED   37888730
  REMARK    GeneRIF: Potential mechanism of TMEM2/CD44 in endoplasmic reticulum
            stress-induced neuronal apoptosis in a rat model of traumatic brain
            injury.
REFERENCE   2  (residues 1 to 1383)
  AUTHORS   Yamamoto,H., Tobisawa,Y., Inubushi,T., Irie,F., Ohyama,C. and
            Yamaguchi,Y.
  TITLE     A mammalian homolog of the zebrafish transmembrane protein 2
            (TMEM2) is the long-sought-after cell-surface hyaluronidase
  JOURNAL   J Biol Chem 292 (18), 7304-7313 (2017)
   PUBMED   28246172
REFERENCE   3  (residues 1 to 1383)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1383)
  AUTHORS   Zhao,Q., Peng,L., Huang,W., Li,Q., Pei,Y., Yuan,P., Zheng,L.,
            Zhang,Y., Deng,J., Zhong,C., Hu,B., Ding,H., Fang,W., Li,R.,
            Liao,Q., Lin,C., Deng,W., Yan,H., Hou,J., Wu,Q., Xu,T., Liu,J.,
            Hu,L., Peng,T., Chen,S., Lai,K.N., Yuen,M.F., Wang,Y., Maini,M.K.,
            Li,C., Li,M., Wang,J., Zhang,X., Sham,P.C., Wang,J., Gao,Z.L. and
            Wang,Y.
  TITLE     Rare inborn errors associated with chronic hepatitis B virus
            infection
  JOURNAL   Hepatology 56 (5), 1661-1670 (2012)
   PUBMED   22610944
REFERENCE   5  (residues 1 to 1383)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 1383)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231225.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.6263.1,
                                           SRR26643296.4218.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1383
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1383
                     /product="inactive cell surface hyaluronidase CEMIP2"
                     /EC_number="3.2.1.35"
                     /note="transmembrane protein 2; cell surface
                     hyaluronidase"
                     /calculated_mol_wt=153824
     Region          132..244
                     /region_name="G8"
                     /note="G8 domain; pfam10162"
                     /db_xref="CDD:462971"
     Region          220..387
                     /region_name="PANDER_like_TMEM2"
                     /note="PANDER-like domain of the transmembrane protein
                     TMEM2; cd13938"
                     /db_xref="CDD:260112"
     Region          1244..1328
                     /region_name="ILEI"
                     /note="Interleukin-like EMT inducer; pfam15711"
                     /db_xref="CDD:464817"
     CDS             1..1383
                     /gene="Cemip2"
                     /gene_synonym="Tmem2"
                     /coded_by="NM_001438042.1:453..4604"
                     /db_xref="GeneID:309400"
                     /db_xref="RGD:1307941"
ORIGIN      
        1 myaagsrghs paflqpqngn ghrspgyvpg kvvpfrpapp pknhasaklt srsqeapatf
       61 afspeeqrtp redrkqkrhk ntficfaits fsffvtlavi lgisskyapd encpdqnprl
      121 rnwdpgqdsa khivikegdm lrltsdatvn siviqdggll vfgddkdgsr nitlrtryil
      181 iqdggalhig aekcryrska titlygksde hesmptfgkk figveaggtl elhgarrtsw
      241 tmlartlhss glpfgsyafe kdfsrglnvr vidqdtarvl ehekfdthey hnesrrlqef
      301 lraqdpgriv aiavgdsavk sllqgtiqmi qdrlgskliq glgyrqawal vgvidggsss
      361 cnesvrnyen hstggkalaq gefytldgqk fsvtaysewi egislsgfrv diadgvklhl
      421 lddvsswgag drivvastdy smyqaeeltl lpcpecsrfq vkvkeipqyl hvgeiidgid
      481 mraevglltr niviqgeted scyadnhcqf fdydtfgghv mieknftsvh lsyvelkhmg
      541 qqhlgrypvh fhlcgdvdsk ggyrvptsvn glsihhsfsr citvhgssgl likdtigfdt
      601 lghcffledg veqrnilfhn lglltkpgtl lptdrnssmc tvmrdgvfgn yipvpttdcm
      661 avstfwiahp nnhlinnaaa gsqdagiwyl fhkeptgess gmqllekpel tplgifynnr
      721 vhsnfkaglf vdkgvkttns sasdpreylc ldnsarfrph qdadpekprv aavidrliaf
      781 knndngawvr ggdiivqnsa fadngkgltf asdgsfpsde gssqevsesl fvgesknygs
      841 qggqnkymgt ggidqkprtl prnrtfpirg fqiydgpihl tkstfkkyvp tpdryssaig
      901 flmknswqtt prnnvslvkf gpqvslnvff gkpgpwfedc eldgdknsif hdidgsvtgy
      961 kdtyvgrmdn ylirhpncvs vtkwnavvcs gtyaqvyvqt wntpnlsmii trdeypshpm
     1021 vlrginqrai spqyqpvvml ekgytihwsg paprttflyl vnfnkddwir vglcypsnts
     1081 fqvtvgflqr qngslsriee yepaqsmeel qkkpserkfy fdsgtgllfl ylrahshrdg
     1141 hsycssqgce rvkiqaatds kdmsncmaka ypqyykkpsa vkrmpamltg fcqgcgthqm
     1201 vfssdphksy lpvrfqspgk aeiqrgepsv isvngtdftf rsagaflliv dacsvpfrlt
     1261 ekrmflsadi shleeylkas ipprsivlls trgeikqmni sdsfvllgla kpahlynkgs
     1321 tvflgfsgnf tpswtrlfts pdvqglgvle qylplqmeey gcsrtssvhr rdlellqqal
     1381 kgl
//
LOCUS       NP_001424836             560 aa            linear   ROD 17-APR-2025
DEFINITION  aladin isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424836 XP_008763926
VERSION     NP_001424836.1
DBSOURCE    REFSEQ: accession NM_001437907.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Juhlen,R., Landgraf,D., Huebner,A. and Koehler,K.
  TITLE     Identification of a novel putative interaction partner of the
            nucleoporin ALADIN
  JOURNAL   Biol Open 5 (11), 1697-1705 (2016)
   PUBMED   27754849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Carvalhal,S., Ribeiro,S.A., Arocena,M., Kasciukovic,T., Temme,A.,
            Koehler,K., Huebner,A. and Griffis,E.R.
  TITLE     The nucleoporin ALADIN regulates Aurora A localization to ensure
            robust mitotic spindle formation
  JOURNAL   Mol Biol Cell 26 (19), 3424-3438 (2015)
   PUBMED   26246606
REFERENCE   3  (residues 1 to 560)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Huebner,A., Mann,P., Rohde,E., Kaindl,A.M., Witt,M., Verkade,P.,
            Jakubiczka,S., Menschikowski,M., Stoltenburg-Didinger,G. and
            Koehler,K.
  TITLE     Mice lacking the nuclear pore complex protein ALADIN show female
            infertility but fail to develop a phenotype resembling human triple
            A syndrome
  JOURNAL   Mol Cell Biol 26 (5), 1879-1887 (2006)
   PUBMED   16479006
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Brooks,B.P., Kleta,R., Stuart,C., Tuchman,M., Jeong,A.,
            Stergiopoulos,S.G., Bei,T., Bjornson,B., Russell,L., Chanoine,J.P.,
            Tsagarakis,S., Kalsner,L. and Stratakis,C.
  TITLE     Genotypic heterogeneity and clinical phenotype in triple A
            syndrome: a review of the NIH experience 2000-2005
  JOURNAL   Clin Genet 68 (3), 215-221 (2005)
   PUBMED   16098009
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Storr,H.L., Clark,A.J., Priestley,J.V. and Michael,G.J.
  TITLE     Identification of the sites of expression of triple A syndrome mRNA
            in the rat using in situ hybridisation
  JOURNAL   Neuroscience 131 (1), 113-123 (2005)
   PUBMED   15680696
REFERENCE   8  (residues 1 to 560)
  AUTHORS   Cronshaw,J.M. and Matunis,M.J.
  TITLE     The nuclear pore complex protein ALADIN is mislocalized in triple A
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (10), 5823-5827 (2003)
   PUBMED   12730363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_008763926.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2439328.1,
                                           SRR26643298.42520.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..560
                     /product="aladin isoform 3"
                     /note="achalasia, adrenocortical insufficiency, alacrimia
                     (Allgrove, triple-A)"
                     /calculated_mol_wt=60551
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <172..431
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          211..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..297
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          305..342
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..560
                     /gene="Aaas"
                     /coded_by="NM_001437907.1:143..1825"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300259"
                     /db_xref="RGD:1308701"
ORIGIN      
        1 mcslglfppp pprgqvtlye hnnelvtgns yespppdfrg qvvgvgdaav glqrvwinlp
       61 vlhltkdplk apgrldhgtr aafihhreqv wkrcinvwhd vglfgvlnei anseeevfew
      121 vktasswala lcgrasslhg slfphlslrs edliaefaqv tnwsscclrv fawhphtnkf
      181 avallddsir vynanstivp slkhrlqrnv aalawkplsa svlavacqsc iliwtldpts
      241 lstrpssgca qvlshpghtp vtslawapng gwllsaspvd avilvwdvst etcvplpwfr
      301 gggvtnllws pdgskvlatt psavfrvwea rmwtcegwpt lsgrcqtgcw spdgkrllft
      361 vlgealiysl sfpepcgtek ghvggaksat ivadlsetti qtpdgeerlg geahamvwdp
      421 sgerlavlmk gnprvqdgnp villfrtrns pvfellpcgv iqgepgaqaq lvsfhpafnk
      481 gallsvcwst grithiplyf vnaqfprfsp vlgraqeppa ggggsvhevp lftetsptsa
      541 pwdplpglps aqphsphshl
//
LOCUS       NP_001424882             594 aa            linear   ROD 17-APR-2025
DEFINITION  AT-rich interactive domain-containing protein 3A [Rattus
            norvegicus].
ACCESSION   NP_001424882 XP_006240966
VERSION     NP_001424882.1
DBSOURCE    REFSEQ: accession NM_001437953.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Tidwell,J.A., Schmidt,C., Heaton,P., Wilson,V. and Tucker,P.W.
  TITLE     Characterization of a new ARID family transcription factor
            (Brightlike/ARID3C) that co-activates Bright/ARID3A-mediated
            immunoglobulin gene transcription
  JOURNAL   Mol Immunol 49 (1-2), 260-272 (2011)
   PUBMED   21955986
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Nixon,J.C., Rajaiya,J. and Webb,C.F.
  TITLE     Mutations in the DNA-binding domain of the transcription factor
            Bright act as dominant negative proteins and interfere with
            immunoglobulin transactivation
  JOURNAL   J Biol Chem 279 (50), 52465-52472 (2004)
   PUBMED   15456761
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240966.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.17388.1,
                                           SRR26643299.29827.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..594
                     /product="AT-rich interactive domain-containing protein
                     3A"
                     /note="dead ringer homolog 1; AT rich interactive domain
                     3A (Bright like)"
                     /calculated_mol_wt=63464
     Region          217..349
                     /region_name="ARID_ARID3A"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 3A (ARID3A) and
                     similar proteins; cd16878"
                     /db_xref="CDD:350642"
     Site            order(259..265,290,292..293,296,304..307,309..311,313,
                     343..344)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350642"
     CDS             1..594
                     /gene="Arid3a"
                     /coded_by="NM_001437953.1:424..2208"
                     /db_xref="GeneID:314616"
                     /db_xref="RGD:1305299"
ORIGIN      
        1 mklqavmetl iqrqqrarqe learqpplpp ppepagvqar ttmtdedrep enarmhrtqm
       61 aalaamraaa aglrhpsspg gsededtaqg gtlsspalhg sgqegpghte gdghlmdmgs
      121 dddtkpkwee qeleelgeee eeededdfee eeedeeeegl glpesaslgs aglftrkapp
      181 tqtfrgdggp rmlsgperlg pgpahpshva sqmpppdhgd wtfeeqfkql yeldadpkrk
      241 eflddlfsfm qkrgtpvnri pimakqvldl fmlyvlvtek gglvevinkk lwreitkgln
      301 lptsitsaaf tlrtqymkyl ypyecerrgl sspnelqaai dsnrregrrq sfggslfays
      361 psgahsmlss pklpvtslgl aastngssit ptpkikkeed saipitvpgr lpvslaghpv
      421 vaaqaaavqa aaaqaavaaq aaaleqlrek lesteppekk malvadeqqr lmqravqqsf
      481 lamtaqlpmn irinsqases rqdpavnlts angsnsisms vemngivytg vlfaqppppt
      541 pppasskggv ssigtnntmg nrtgasgsag ssgqvglagv saptmsstsn nslp
//
LOCUS       NP_001425003             855 aa            linear   ROD 17-APR-2025
DEFINITION  leucine-rich repeat and death domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001425003 XP_216085
VERSION     NP_001425003.1
DBSOURCE    REFSEQ: accession NM_001438074.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 15, 2025 this sequence version replaced XP_216085.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3150436.1,
                                           SRR26643293.21698.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q13"
     Protein         1..855
                     /product="leucine-rich repeat and death domain-containing
                     protein 1"
                     /calculated_mol_wt=97144
     Region          162..185
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          167..537
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          186..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          209..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          232..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          255..277
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          278..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          301..323
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          324..346
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          347..392
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          436..780
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          439..461
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          463..484
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          487..507
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          508..530
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          531..553
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          554..576
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          577..599
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          600..648
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          649..671
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          672..694
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          695..717
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..855
                     /gene="Lrrd1"
                     /gene_synonym="RGD1562785"
                     /coded_by="NM_001438074.1:385..2952"
                     /db_xref="GeneID:296836"
                     /db_xref="RGD:1562785"
ORIGIN      
        1 msedgsnvep egltrsesle epefideisd psnetsphsg ntdfnqiyes nssenteqps
       61 asstsqlngn eetnieipfs dtnieevipl snsespqsse ssetneaeey hpvkfpigrk
      121 frgrtfnghh kgfdmesdtf tvhldakglq efpvdivkvk yvkylyldkn qiktfqgadp
      181 gdllgletls lqenglssip qeiqlfhnlk vlnasyneis hipkellqlg nmrqlflnsn
      241 hieslpsgle nlryletlsl gknrlthipd slcglknlkt lnleynqlti fskslcflpk
      301 lvslnltgnm igslpkevre lknlenllmn hnkltflave ifqllkikel hladnkleai
      361 spkienfkel rllnldnnll qslpkkishc vnlesltlsd nnleelpkki rklknlrqlh
      421 anrnkmikma eeishlskih slefsgnqit hvpieiknck eitrvelnyn nimyfpvglc
      481 alqsldylsf ngnyiseipv dlsfskqllh lelnknkiti fsehlcsltn leyldlaknq
      541 irkiphcisa mlslhvlils dnkfeifpke lcslknlqll disenqlhki pseisklkki
      601 qklnlsnnnf thfpaelcql qtledlnisq isgkkltrlp eevsrmtqlk alnisnnaik
      661 eiprnigelr nlitfhasnn qinslpssfl slnvlqsldl ggnnltdlps aiyklsslke
      721 infddnpllr ppmeickgkq mhtitcylqr addrdekile kifhivanni tetkfeflqq
      781 klhmarsens vpvktttpln egiyqallkw ktekrvsfta ialkdqlfra lnmigaydim
      841 dkitalnlyt saikl
//
LOCUS       NP_001425056             413 aa            linear   ROD 17-APR-2025
DEFINITION  MAP kinase-interacting serine/threonine-protein kinase 1 [Rattus
            norvegicus].
ACCESSION   NP_001425056 XP_006238760
VERSION     NP_001425056.1
DBSOURCE    REFSEQ: accession NM_001438127.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Panja,D., Kenney,J.W., D'Andrea,L., Zalfa,F., Vedeler,A.,
            Wibrand,K., Fukunaga,R., Bagni,C., Proud,C.G. and Bramham,C.R.
  TITLE     Two-stage translational control of dentate gyrus LTP consolidation
            is mediated by sustained BDNF-TrkB signaling to MNK
  JOURNAL   Cell Rep 9 (4), 1430-1445 (2014)
   PUBMED   25453757
  REMARK    GeneRIF: Long-term potentiation (LTP) consolidation in the dentate
            gyrus of live rodents requires sustained (hours) BDNF-TrkB
            signaling and from TrkB to MAP-kinase-interacting kinase.
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Niknami,M., Patel,M., Witting,P.K. and Dong,Q.
  TITLE     Molecules in focus: cytosolic phospholipase A2-alpha
  JOURNAL   Int J Biochem Cell Biol 41 (5), 994-997 (2009)
   PUBMED   18761105
  REMARK    Review article
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Chrestensen,C.A., Eschenroeder,A., Ross,W.G., Ueda,T.,
            Watanabe-Fukunaga,R., Fukunaga,R. and Sturgill,T.W.
  TITLE     Loss of MNK function sensitizes fibroblasts to serum-withdrawal
            induced apoptosis
  JOURNAL   Genes Cells 12 (10), 1133-1140 (2007)
   PUBMED   17903173
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Origanti,S. and Shantz,L.M.
  TITLE     Ras transformation of RIE-1 cells activates cap-independent
            translation of ornithine decarboxylase: regulation by the
            Raf/MEK/ERK and phosphatidylinositol 3-kinase pathways
  JOURNAL   Cancer Res 67 (10), 4834-4842 (2007)
   PUBMED   17510413
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Chen,S., Atkins,C.M., Liu,C.L., Alonso,O.F., Dietrich,W.D. and
            Hu,B.R.
  TITLE     Alterations in mammalian target of rapamycin signaling pathways
            after traumatic brain injury
  JOURNAL   J Cereb Blood Flow Metab 27 (5), 939-949 (2007)
   PUBMED   16955078
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Chrestensen,C.A., Shuman,J.K., Eschenroeder,A., Worthington,M.,
            Gram,H. and Sturgill,T.W.
  TITLE     MNK1 and MNK2 regulation in HER2-overexpressing breast cancer lines
  JOURNAL   J Biol Chem 282 (7), 4243-4252 (2007)
   PUBMED   17130135
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Gaestel,M.
  TITLE     MAPKAP kinases - MKs - two's company, three's a crowd
  JOURNAL   Nat Rev Mol Cell Biol 7 (2), 120-130 (2006)
   PUBMED   16421520
  REMARK    Review article
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Fukunaga,R. and Hunter,T.
  TITLE     MNK1, a new MAP kinase-activated protein kinase, isolated by a
            novel expression screening method for identifying protein kinase
            substrates
  JOURNAL   EMBO J 16 (8), 1921-1933 (1997)
   PUBMED   9155018
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Waskiewicz,A.J., Flynn,A., Proud,C.G. and Cooper,J.A.
  TITLE     Mitogen-activated protein kinases activate the serine/threonine
            kinases Mnk1 and Mnk2
  JOURNAL   EMBO J 16 (8), 1909-1920 (1997)
   PUBMED   9155017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006238760.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.17651.1,
                                           SRR26643429.20406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..413
                     /product="MAP kinase-interacting serine/threonine-protein
                     kinase 1"
                     /EC_number="2.7.11.1"
                     /note="mnk1; MAP kinase signal-integrating kinase 1; MAPK
                     signal-integrating kinase 1; MAP kinase-interacting
                     serine/threonine kinase 1"
                     /calculated_mol_wt=46083
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:O08605; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:O08605; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Region          34..322
                     /region_name="STKc_Mnk1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase signal-integrating kinase
                     1; cd14174"
                     /db_xref="CDD:271076"
     Site            order(43..47,51,64,66,96,112..115,119,121,157..158,160,
                     162..163,165,178..179,182,204..208,210)
                     /site_type="active"
                     /db_xref="CDD:271076"
     Site            order(43..46,51,64,66,96,112..115,119,162..163,165,
                     178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271076"
     Site            order(47,119,121,157..158,160,162,182,204..208,210)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271076"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            178..208
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271076"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     Site            order(252,256,264,267)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:271076"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUB5; propagated from
                     UniProtKB/Swiss-Prot (Q4G050.1)"
     CDS             1..413
                     /gene="Mknk1"
                     /coded_by="NM_001438127.1:275..1516"
                     /db_xref="GeneID:500526"
                     /db_xref="RGD:1559603"
ORIGIN      
        1 mgsseplpiv dsdkrrkkkr ktratdslpg kfedvyqlts ellgegayak vqgavslqsg
       61 keyavkiiek qaghsrsrvf revetlyqcq gnrnilelie ffeddtrfyl vfeklqggsi
      121 lahiqkrkhf neleasrvvr dvataldflh tkgiahrdlk penilcespe kvspvkicdf
      181 dlgsgvklnn sctpittpel ttpcgsaeym apevvevfrd eatfydkrcd lwslgvvlyi
      241 mlsgyppfvg hcgadcgwdr gevcrmcqnk lfesiqegky efpdkdwahi steakdlisk
      301 llvrdakqrl saaqvlqhpw vqgqapergl ptpqvlqrns stmdltlfaa eaialnrqls
      361 qheenelaee healaeglcs mklsppsksr larrralaha greanscstp agl
//
LOCUS       NP_001424966             757 aa            linear   ROD 17-APR-2025
DEFINITION  lysyl oxidase homolog 4 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001424966 XP_006231455
VERSION     NP_001424966.1
DBSOURCE    REFSEQ: accession NM_001438037.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Ito,H., Akiyama,H., Iguchi,H., Iyama,K., Miyamoto,M., Ohsawa,K. and
            Nakamura,T.
  TITLE     Molecular cloning and biological activity of a novel lysyl
            oxidase-related gene expressed in cartilage
  JOURNAL   J Biol Chem 276 (26), 24023-24029 (2001)
   PUBMED   11292829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231455.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.5325.1,
                                           SRR21887620.1792440.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..757
                     /product="lysyl oxidase homolog 4 isoform 1 precursor"
                     /EC_number="1.4.3.13"
                     /note="lysyl oxidase homolog 4"
                     /calculated_mol_wt=81792
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2841
     Region          33..133
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          177..287
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     Region          312..412
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          446..529
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          534..732
                     /region_name="Lysyl_oxidase"
                     /note="Lysyl oxidase; pfam01186"
                     /db_xref="CDD:460102"
     CDS             1..757
                     /gene="Loxl4"
                     /coded_by="NM_001438037.1:72..2345"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:309380"
                     /db_xref="RGD:1308588"
ORIGIN      
        1 mmwpppptfs vflllllsqv pssrpqspgt kklrlvgpan rpeegrlevl hqgqwgtvcd
       61 ddfalqeatv acrqlgfesa ltwahsakfg qgegpiwldn vrclgtedtl dqcgsngwgv
      121 sdcrhsedvg vvchprrqqg yhsekvsnal gpqgrrleev rlkpilasak rhspvtegav
      181 evryeghwrq vcdqgwtmnn srvvcgmlgf psqapvnshy yrkvwnlkmk dpksrlnglt
      241 kknsfwihrv dclgtephla kcqvqvapgr gklrpacpgg mhavvncvag phfqrqkpkp
      301 krkesgaeel kvrlrsgaqv gegrvevlmn rqwgtvcdhr wnlisasvvc rqlgfgsare
      361 alfgaqlgqg lgpihlsevr crgyeqtigd clalegsqng cqhandaavr cnipdmgfqn
      421 kvrlaggrns eegvvevqve vngvprwgtv csdhwgltea mvtcrqlglg fanfaikdtw
      481 ywqgtpeake vvmsgvrcsg temalqqcqr hgpvhcshgs grfsagvacm nsapdlvmna
      541 qlvqetayle drplsmlyca heenclsksa dhmdwpyghr rllrfssqiy nlgradfrpk
      601 agrhswiwhq chrhyhsiev fthydlltln gskvaeghka sfcledtncp sgvqrryaca
      661 nfgeqgvavg cwdtyrhdid cqwvditdvs pgdyifqvvv nptndvaesd fsnnmircrc
      721 kydgqrvwlh nchtgdpyrp naelsleqeq rlrnnli
//
LOCUS       NP_059009                460 aa            linear   ROD 17-APR-2025
DEFINITION  rab-3A-interacting protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_059009 XP_006241419
VERSION     NP_059009.2
DBSOURCE    REFSEQ: accession NM_017313.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vetter,M., Stehle,R., Basquin,C. and Lorentzen,E.
  TITLE     Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3
            and Rabin8 effectors to Rab11
  JOURNAL   Nat Struct Mol Biol 22 (9), 695-702 (2015)
   PUBMED   26258637
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Klip,A., Sun,Y., Chiu,T.T. and Foley,K.P.
  TITLE     Signal transduction meets vesicle traffic: the software and
            hardware of GLUT4 translocation
  JOURNAL   Am J Physiol Cell Physiol 306 (10), C879-C886 (2014)
   PUBMED   24598362
  REMARK    Review article
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Chiba,S., Amagai,Y., Homma,Y., Fukuda,M. and Mizuno,K.
  TITLE     NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by
            switching binding specificity from phosphatidylserine to Sec15
  JOURNAL   EMBO J 32 (6), 874-885 (2013)
   PUBMED   23435566
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Blumer,J., Rey,J., Dehmelt,L., Mazel,T., Wu,Y.W., Bastiaens,P.,
            Goody,R.S. and Itzen,A.
  TITLE     RabGEFs are a major determinant for specific Rab membrane targeting
  JOURNAL   J Cell Biol 200 (3), 287-300 (2013)
   PUBMED   23382462
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Ultanir,S.K., Hertz,N.T., Li,G., Ge,W.P., Burlingame,A.L.,
            Pleasure,S.J., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Chemical genetic identification of NDR1/2 kinase substrates AAK1
            and Rabin8 Uncovers their roles in dendrite arborization and spine
            development
  JOURNAL   Neuron 73 (6), 1127-1142 (2012)
   PUBMED   22445341
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Hattula,K., Furuhjelm,J., Arffman,A. and Peranen,J.
  TITLE     A Rab8-specific GDP/GTP exchange factor is involved in actin
            remodeling and polarized membrane transport
  JOURNAL   Mol Biol Cell 13 (9), 3268-3280 (2002)
   PUBMED   12221131
REFERENCE   7  (residues 1 to 460)
  AUTHORS   de Bruijn,D.R., dos Santos,N.R., Kater-Baats,E., Thijssen,J., van
            den Berk,L., Stap,J., Balemans,M., Schepens,M., Merkx,G. and van
            Kessel,A.G.
  TITLE     The cancer-related protein SSX2 interacts with the human homologue
            of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear
            protein, SSX2IP
  JOURNAL   Genes Chromosomes Cancer 34 (3), 285-298 (2002)
   PUBMED   12007189
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Page,G., Kogel,D., Rangnekar,V. and Scheidtmann,K.H.
  TITLE     Interaction partners of Dlk/ZIP kinase: co-expression of Dlk/ZIP
            kinase and Par-4 results in cytoplasmic retention and apoptosis
  JOURNAL   Oncogene 18 (51), 7265-7273 (1999)
   PUBMED   10602480
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Page,G., Lodige,I., Kogel,D. and Scheidtmann,K.H.
  TITLE     AATF, a novel transcription factor that interacts with Dlk/ZIP
            kinase and interferes with apoptosis
  JOURNAL   FEBS Lett 462 (1-2), 187-191 (1999)
   PUBMED   10580117
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Brondyk,W.H., McKiernan,C.J., Fortner,K.A., Stabila,P., Holz,R.W.
            and Macara,I.G.
  TITLE     Interaction cloning of Rabin3, a novel protein that associates with
            the Ras-like GTPase Rab3A
  JOURNAL   Mol Cell Biol 15 (3), 1137-1143 (1995)
   PUBMED   7532276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_006241419.1, NP_059009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.26747.1,
                                           SRR26643297.25083.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..460
                     /product="rab-3A-interacting protein isoform 1"
                     /note="rab-3A-interacting protein; rabin-3;
                     SSX2-interacting protein; rab3A-interacting protein"
                     /calculated_mol_wt=50901
     Region          97..>240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          173..241
                     /region_name="Sec2p"
                     /note="GDP/GTP exchange factor Sec2p; pfam06428"
                     /db_xref="CDD:428938"
     Region          246..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62739.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Region          266..458
                     /region_name="Rab11BD_RAB3IP"
                     /note="Rab11 binding domain of Rab-3A-interacting protein
                     (RAB3IP); cd21068"
                     /db_xref="CDD:411032"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68EF0; propagated from
                     UniProtKB/Swiss-Prot (Q62739.2)"
     Site            order(351..357,412,415..416,419,423,428..432)
                     /site_type="other"
                     /note="Rab11 binding site [polypeptide binding]"
                     /db_xref="CDD:411032"
     CDS             1..460
                     /gene="Rab3ip"
                     /gene_synonym="RABIN3"
                     /coded_by="NM_017313.4:194..1576"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29885"
                     /db_xref="RGD:620650"
ORIGIN      
        1 mandplegfh evnlasptsp dllgvcdpgt qeqttspsvi yrphpstlcs atiqanalnl
       61 sdlptqpvys sprhlncaei snisihvpep assvasevaa gltrftsrkd scnaereflq
      121 gatvteasag nddifglstd slsrlrspsv levrekgyer lkeelakaqr elklkdeece
      181 rlskvrdqlg qeleeltasl feeahkmvre anvkqataek qlkeaqgkid vlqaevaalk
      241 tlvlssspts ptqeplaagk tpfkrghtrn kstssamsgs hqdfsaiqpi vkdcreadls
      301 lynefrswkd eptmdrtcpf ldkiyqedif pcltfaksel asavleaven ntlsiepvgl
      361 qpirfvkasa vecggpkkca ltgqskpckh riklgdsssy yyispvcryr itsvcnffty
      421 iryiqqglvk qqdvdqmfwe vmqlrkemsl aklgyfkeel
//
LOCUS       NP_001100265             546 aa            linear   ROD 17-APR-2025
DEFINITION  aladin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100265 XP_001067255 XP_006242449 XP_217063
VERSION     NP_001100265.1
DBSOURCE    REFSEQ: accession NM_001106795.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Juhlen,R., Landgraf,D., Huebner,A. and Koehler,K.
  TITLE     Identification of a novel putative interaction partner of the
            nucleoporin ALADIN
  JOURNAL   Biol Open 5 (11), 1697-1705 (2016)
   PUBMED   27754849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Carvalhal,S., Ribeiro,S.A., Arocena,M., Kasciukovic,T., Temme,A.,
            Koehler,K., Huebner,A. and Griffis,E.R.
  TITLE     The nucleoporin ALADIN regulates Aurora A localization to ensure
            robust mitotic spindle formation
  JOURNAL   Mol Biol Cell 26 (19), 3424-3438 (2015)
   PUBMED   26246606
REFERENCE   3  (residues 1 to 546)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Huebner,A., Mann,P., Rohde,E., Kaindl,A.M., Witt,M., Verkade,P.,
            Jakubiczka,S., Menschikowski,M., Stoltenburg-Didinger,G. and
            Koehler,K.
  TITLE     Mice lacking the nuclear pore complex protein ALADIN show female
            infertility but fail to develop a phenotype resembling human triple
            A syndrome
  JOURNAL   Mol Cell Biol 26 (5), 1879-1887 (2006)
   PUBMED   16479006
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Brooks,B.P., Kleta,R., Stuart,C., Tuchman,M., Jeong,A.,
            Stergiopoulos,S.G., Bei,T., Bjornson,B., Russell,L., Chanoine,J.P.,
            Tsagarakis,S., Kalsner,L. and Stratakis,C.
  TITLE     Genotypic heterogeneity and clinical phenotype in triple A
            syndrome: a review of the NIH experience 2000-2005
  JOURNAL   Clin Genet 68 (3), 215-221 (2005)
   PUBMED   16098009
REFERENCE   7  (residues 1 to 546)
  AUTHORS   Storr,H.L., Clark,A.J., Priestley,J.V. and Michael,G.J.
  TITLE     Identification of the sites of expression of triple A syndrome mRNA
            in the rat using in situ hybridisation
  JOURNAL   Neuroscience 131 (1), 113-123 (2005)
   PUBMED   15680696
REFERENCE   8  (residues 1 to 546)
  AUTHORS   Cronshaw,J.M. and Matunis,M.J.
  TITLE     The nuclear pore complex protein ALADIN is mislocalized in triple A
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (10), 5823-5827 (2003)
   PUBMED   12730363
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_006242449.1, XP_217063.4, XP_001067255.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3310792.1,
                                           SRR26360186.1616436.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..546
                     /product="aladin isoform 1"
                     /note="achalasia, adrenocortical insufficiency, alacrimia
                     (Allgrove, triple-A)"
                     /calculated_mol_wt=59230
     Region          157..193
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <158..417
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          197..243
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          247..283
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          291..328
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..546
                     /gene="Aaas"
                     /coded_by="NM_001106795.2:143..1783"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300259"
                     /db_xref="RGD:1308701"
ORIGIN      
        1 mcslglfppp pprgqvtlye hnnelvtgns yespppdfrg qwinlpvlhl tkdplkapgr
       61 ldhgtraafi hhreqvwkrc invwhdvglf gvlneianse eevfewvkta sswalalcgr
      121 asslhgslfp hlslrsedli aefaqvtnws scclrvfawh phtnkfaval lddsirvyna
      181 nstivpslkh rlqrnvaala wkplsasvla vacqsciliw tldptslstr pssgcaqvls
      241 hpghtpvtsl awapnggwll saspvdavil vwdvstetcv plpwfrgggv tnllwspdgs
      301 kvlattpsav frvwearmwt cegwptlsgr cqtgcwspdg krllftvlge aliyslsfpe
      361 pcgtekghvg gaksativad lsettiqtpd geerlggeah amvwdpsger lavlmkgnpr
      421 vqdgnpvill frtrnspvfe llpcgviqge pgaqaqlvsf hpafnkgall svcwstgrit
      481 hiplyfvnaq fprfspvlgr aqeppagggg svhevplfte tsptsapwdp lpglpsaqph
      541 sphshl
//
LOCUS       NP_001425005            1198 aa            linear   ROD 17-APR-2025
DEFINITION  VPS10 domain-containing receptor SorCS1 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001425005 XP_006231582
VERSION     NP_001425005.1
DBSOURCE    REFSEQ: accession NM_001438076.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1198)
  AUTHORS   Yau,B., Blood,Z., An,Y., Su,Z. and Kebede,M.A.
  TITLE     Type 2 diabetes-associated single nucleotide polymorphism in Sorcs1
            gene results in alternative processing of the Sorcs1 protein in
            INS1 beta-cells
  JOURNAL   Sci Rep 9 (1), 19466 (2019)
   PUBMED   31857633
  REMARK    GeneRIF: Type 2 diabetes-associated single nucleotide polymorphism
            in Sorcs1 gene results in alternative processing of the Sorcs1
            protein in INS1 beta-cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1198)
  AUTHORS   Ribeiro,L.F., Verpoort,B., Nys,J., Vennekens,K.M., Wierda,K.D. and
            de Wit,J.
  TITLE     SorCS1-mediated sorting in dendrites maintains neurexin axonal
            surface polarization required for synaptic function
  JOURNAL   PLoS Biol 17 (10), e3000466 (2019)
   PUBMED   31658245
  REMARK    GeneRIF: SorCS1-mediated sorting in dendritic endosomes controls
            Nrxn axonal surface polarization required for proper synapse
            development and function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1198)
  AUTHORS   Lazar,J., O'Meara,C.C., Sarkis,A.B., Prisco,S.Z., Xu,H., Fox,C.S.,
            Chen,M.H., Broeckel,U., Arnett,D.K., Moreno,C., Provoost,A.P. and
            Jacob,H.J.
  TITLE     SORCS1 contributes to the development of renal disease in rats and
            humans
  JOURNAL   Physiol Genomics 45 (16), 720-728 (2013)
   PUBMED   23780848
  REMARK    GeneRIF: The experimental data from the rat combined with
            association results from different ethnic groups indicates a role
            for SORCS1 in maintaining proper renal function.
REFERENCE   4  (residues 1 to 1198)
  AUTHORS   Hermey,G., Keat,S.J., Madsen,P., Jacobsen,C., Petersen,C.M. and
            Gliemann,J.
  TITLE     Characterization of sorCS1, an alternatively spliced receptor with
            completely different cytoplasmic domains that mediate different
            trafficking in cells
  JOURNAL   J Biol Chem 278 (9), 7390-7396 (2003)
   PUBMED   12482870
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231582.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.8487.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1198
                     /product="VPS10 domain-containing receptor SorCS1 isoform
                     1 precursor"
                     /note="VPS10 domain-containing receptor SorCS1; VPS10
                     domain receptor protein SORCS 1"
                     /calculated_mol_wt=130699
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3004
     Region          196..793
                     /region_name="VPS10"
                     /note="VPS10 domain; smart00602"
                     /db_xref="CDD:214740"
     Region          807..880
                     /region_name="PKD"
                     /note="PKD domain; pfam00801"
                     /db_xref="CDD:395646"
     Region          836..>973
                     /region_name="COG3291"
                     /note="Uncharacterized conserved protein, PKD repeat
                     domain [Function unknown]"
                     /db_xref="CDD:442520"
     CDS             1..1198
                     /gene="Sorcs1"
                     /coded_by="NM_001438076.1:250..3846"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:309533"
                     /db_xref="RGD:1305910"
ORIGIN      
        1 mgkvgagdgs saalsalltg agllmllapg icsslsccpp qhpsstprwt ltprgfsypg
       61 plgrapatpp plfmrplfav apgdralfle raggsrvsva tasrsgrrrr sgmdpektep
      121 gegtsrsrrd mlrdggqqgp gtgardpdka trfrmeelrl tsttfaltgd sahnqamvhw
      181 sghnssvili ltklydynlg sitesslwrs tdygttyekl ndkvglktil sylyvcptnk
      241 rkimlltdpe iessllissd egatyqkyrl nfyiqsllfh pkqedwilay sqdqklyssa
      301 efgrrwqliq eavvpnrfyw svlgsnkepd lvhleartvd ghsiyltcrm qncteanrnk
      361 pfpgyidpds livqddyvfv qltsggrphy yvsyrrnpfa qmklpkyalp kdmhvistde
      421 nqvfaavqew nqndtynlyi sdtrgvyftl alenvqssrg pegnvmidly evagikgmfl
      481 ankkidnqvk tfitynkgrd wrllqapdad lrgdpvhcll pycslhlhlk vsenpytsgi
      541 iasrdtapsi ivasgnigse lsdsdismfv ssdagntwrq ifeeehsily ldqggvlvam
      601 khtslpirhl wlsfdegrsw skysftsipl fvdgvlgepg eetlimtvfg hfshrsewql
      661 vkvdyksifd rrcaeedyrp wqlhsqgeac imgakriykk rkserkcmqg tyagamesep
      721 cvcteadfdc dygyerhssg qclpafwfnp sslskdcslg qsylnstgyr kvvsnnctdg
      781 vreqytakpq kcpgkaprgl rivtadgklt aeqghnvtlm vqleegdvqr tliqvdfgdg
      841 iavsyvnlss medgikhvyq nvgifrvtvq vdnslgsdsa vlylhvtcpl ehvhlslpfv
      901 ttknkevnat avlwpsqvgt ltyvwwygnn teplitlegs isfkftsegm ntitvqvsag
      961 nailqdtkti avyeefrslr lafspnlddy npdipewrrd isrvikkslv eatgipsqhi
     1021 lvavlpglpt aaelfvlpyq dgarenkrsp edleqisevl ihklnqnlvh felkpgvqvl
     1081 vhaahltaap lvdltpthsg samlmllsvv fvglavfviy kfkrkipgin vyaqmqneke
     1141 qelinpvsht esrptaphpd lrrpgqlvde kveshllgsi sivaenqstk eiptyvnv
//
LOCUS       NP_001425024             205 aa            linear   ROD 17-APR-2025
DEFINITION  V-type proton ATPase 21 kDa proteolipid subunit c'' [Rattus
            norvegicus].
ACCESSION   NP_001425024
VERSION     NP_001425024.1
DBSOURCE    REFSEQ: accession NM_001438095.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Nishi,T., Kawasaki-Nishi,S. and Forgac,M.
  TITLE     Expression and localization of the mouse homologue of the yeast
            V-ATPase 21-kDa Subunit c' (Vma16p)
  JOURNAL   J Biol Chem 276 (36), 34122-34130 (2001)
   PUBMED   11441017
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Sun-Wada,G.H., Murakami,H., Nakai,H., Wada,Y. and Futai,M.
  TITLE     Mouse Atp6f, the gene encoding the 23-kDa proteolipid of vacuolar
            proton translocating ATPase
  JOURNAL   Gene 274 (1-2), 93-99 (2001)
   PUBMED   11675001
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC159422.1, FQ225932.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN16676786,
                                           SAMN16676787 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..205
                     /product="V-type proton ATPase 21 kDa proteolipid subunit
                     c''"
                     /EC_number="7.1.2.2"
                     /note="ATPase, H+ transporting, lysosomal 21kDa, V0
                     subunit b; ATPase, H+ transporting, lysosomal V0 subunit
                     B-like 1; V-type proton ATPase 21 kDa proteolipid subunit
                     c"
                     /calculated_mol_wt=21476
     Region          49..111
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt1"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18177"
                     /db_xref="CDD:349417"
     Region          133..197
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt2"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18178"
                     /db_xref="CDD:349418"
     CDS             1..205
                     /gene="Atp6v0b"
                     /gene_synonym="Atp6v0bl1"
                     /coded_by="NM_001438095.1:146..763"
                     /db_xref="GeneID:298451"
                     /db_xref="RGD:1308303"
ORIGIN      
        1 mtglellylg ifvafwacmi vvgicytifd lgfrfdvawf ltetspfmws nlgiglaisl
       61 svvgaawgiy itgssiiggg vkapriktkn lvsiifceav aiygiimaiv isnmaepfsa
      121 tdpkaighrn yhagysmfga gltvglsnlf cgvcvgivgs gaaladaqnp slfvkilive
      181 ifgsaiglfg vivailqtsr vkmgd
//
LOCUS       NP_001424994            1857 aa            linear   ROD 17-APR-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001424994 XP_006231564
VERSION     NP_001424994.1
DBSOURCE    REFSEQ: accession NM_001438065.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1857)
  AUTHORS   Hansen,M.D., Johnsen,I.B., Stiberg,K.A., Sherstova,T., Wakita,T.,
            Richard,G.M., Kandasamy,R.K., Meurs,E.F. and Anthonsen,M.W.
  TITLE     Hepatitis C virus triggers Golgi fragmentation and autophagy
            through the immunity-related GTPase M
  JOURNAL   Proc Natl Acad Sci U S A 114 (17), E3462-E3471 (2017)
   PUBMED   28389568
REFERENCE   2  (residues 1 to 1857)
  AUTHORS   Lowery,J., Szul,T., Styers,M., Holloway,Z., Oorschot,V.,
            Klumperman,J. and Sztul,E.
  TITLE     The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane
            recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to
            the trans-Golgi network (TGN)
  JOURNAL   J Biol Chem 288 (16), 11532-11545 (2013)
   PUBMED   23386609
REFERENCE   3  (residues 1 to 1857)
  AUTHORS   Mao,L., Li,N., Guo,Y., Xu,X., Gao,L., Xu,Y., Zhou,L. and Liu,W.
  TITLE     AMPK phosphorylates GBF1 for mitotic Golgi disassembly
  JOURNAL   J Cell Sci 126 (Pt 6), 1498-1505 (2013)
   PUBMED   23418352
REFERENCE   4  (residues 1 to 1857)
  AUTHORS   Mazaki,Y., Nishimura,Y. and Sabe,H.
  TITLE     GBF1 bears a novel phosphatidylinositol-phosphate binding module,
            BP3K, to link PI3Kgamma activity with Arf1 activation involved in
            GPCR-mediated neutrophil chemotaxis and superoxide production
  JOURNAL   Mol Biol Cell 23 (13), 2457-2467 (2012)
   PUBMED   22573891
REFERENCE   5  (residues 1 to 1857)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1857)
  AUTHORS   Szul,T., Grabski,R., Lyons,S., Morohashi,Y., Shestopal,S., Lowe,M.
            and Sztul,E.
  TITLE     Dissecting the role of the ARF guanine nucleotide exchange factor
            GBF1 in Golgi biogenesis and protein trafficking
  JOURNAL   J Cell Sci 120 (Pt 22), 3929-3940 (2007)
   PUBMED   17956946
REFERENCE   7  (residues 1 to 1857)
  AUTHORS   Garcia-Mata,R., Szul,T., Alvarez,C. and Sztul,E.
  TITLE     ADP-ribosylation factor/COPI-dependent events at the endoplasmic
            reticulum-Golgi interface are regulated by the guanine nucleotide
            exchange factor GBF1
  JOURNAL   Mol Biol Cell 14 (6), 2250-2261 (2003)
   PUBMED   12808027
REFERENCE   8  (residues 1 to 1857)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
REFERENCE   9  (residues 1 to 1857)
  AUTHORS   Zhao,X., Lasell,T.K. and Melancon,P.
  TITLE     Localization of large ADP-ribosylation factor-guanine nucleotide
            exchange factors to different Golgi compartments: evidence for
            distinct functions in protein traffic
  JOURNAL   Mol Biol Cell 13 (1), 119-133 (2002)
   PUBMED   11809827
REFERENCE   10 (residues 1 to 1857)
  AUTHORS   Claude,A., Zhao,B.P., Kuziemsky,C.E., Dahan,S., Berger,S.J.,
            Yan,J.P., Armold,A.D., Sullivan,E.M. and Melancon,P.
  TITLE     GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide
            exchange factor that displays specificity for ADP-ribosylation
            factor 5
  JOURNAL   J Cell Biol 146 (1), 71-84 (1999)
   PUBMED   10402461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231564.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.7400.1,
                                           SRR26643287.4010.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1857
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 6"
                     /note="golgi-specific brefeldin A-resistance factor 1;
                     Golgi-specific brefeldin A-resistance guanine nucleotide
                     exchange factor 1; golgi-specific brefeldin A resistant
                     guanine nucleotide exchange factor 1"
                     /calculated_mol_wt=205964
     Region          <429..>1178
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          699..884
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1725..1855
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1857
                     /gene="Gbf1"
                     /gene_synonym="RGD1307160"
                     /coded_by="NM_001438065.1:260..5833"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:309451"
                     /db_xref="RGD:1307160"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwsthi pldeerdpll hsfshlkevl nsgtelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflscalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvgt hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepksyvgtn lkklkmragg msdsskwkkq krsprpprht
      241 tkvmpgselp tpngaalssn ltggmpfiea ptsissasse aastvvspct dsglelssqa
      301 tskedltdle qagspreitt tepgsteigv sdqldpqega hvekaqsasv esipevleec
      361 tsptdhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsverl nlyaaslrvc
      481 fllfesmreh lkfqlemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfedltklls knafpvsgql ytthllslda lltvidstea hcqakvlntl
      601 nqqekketar pgfeavdgsp dtykseraas dgkatgvpsd apglhfssgg wlstehgkpg
      661 csdleeagds gvdkkttrkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn mdllesfvst fsfqglrlde
      781 alrlyleafr lpgeapvihr llevftehwr scngspfans dacfalayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik neeivmpeeq tglvrenyvw
      901 svllhrgatp egiflrvppg sydldlftmt wgptiaalsy vfdksleeti iqkaisgfrk
      961 camisahygl sdvfdnliis lckftalsse sienlpsvfg snpkahiaak tvfhlahrhg
     1021 dilregwkni meamlqlfra qllpkamvev edfvdpngki slqreetpsn rgestvlsfv
     1081 swltlsgpeq ssvrgpsten qeakrvaldc ikqcdpekmi teskflqles lqelmkalvs
     1141 vtpdeetyde edaafcleml lrivlenrdr vgcvwqtvrd hlyhlcvqaq dfcflverav
     1201 vgllrlairl lrreeisgqv llslrilllm kpsvlsrvsh qvayglhell ktnaanihsg
     1261 ddwatlftll ecigsgvkpp dalqatarad apdagaqsds elpsyhqndv sldrgytsds
     1321 evytdhgrpg kmhrsatdad mansgwlvvg kddidnskpa aglsrpgpsp lvnqysltvg
     1381 ldlgphdtks llkcveslsf ivrdaahitp dnfelcvktl rifveaslng gcksqdkrgk
     1441 shkydskgnr fkkkpkegsm lrrprassqh atraghsdee edegvpasyh tvslqlldlm
     1501 htlhtraasi ysswaeeqrh letggrkiea dsrtlwahcw cpllqgiacl ccdarrqvrm
     1561 qaltylqral lvhdlqklda lewescfnkv lfplltklle nispadvggm eetrmrastl
     1621 lskvflqhls pllslstfaa lwltildfmd kymhagssdl lseavpeslk nmllvmdtae
     1681 ifhsadargg spsalweitw eridcflphl rdelfkqtvi qdpmptephs qkplasthlt
     1741 paagdprmpg hppppeipse vgacdpekpe straassssp gspvasspsk qspapegppp
     1801 laqpplilqp ltsplqvgvp pmtlpiilnp alieatspvp llatprptdp iptsevn
//
LOCUS       NP_001425042             463 aa            linear   ROD 17-APR-2025
DEFINITION  protein LSM14 homolog A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425042 XP_006228918
VERSION     NP_001425042.1
DBSOURCE    REFSEQ: accession NM_001438113.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Li,Y., Chen,R., Zhou,Q., Xu,Z., Li,C., Wang,S., Mao,A., Zhang,X.,
            He,W. and Shu,H.B.
  TITLE     LSm14A is a processing body-associated sensor of viral nucleic
            acids that initiates cellular antiviral response in the early phase
            of viral infection
  JOURNAL   Proc Natl Acad Sci U S A 109 (29), 11770-11775 (2012)
   PUBMED   22745163
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Tanaka,K.J., Ogawa,K., Takagi,M., Imamoto,N., Matsumoto,K. and
            Tsujimoto,M.
  TITLE     RAP55, a cytoplasmic mRNP component, represses translation in
            Xenopus oocytes
  JOURNAL   J Biol Chem 281 (52), 40096-40106 (2006)
   PUBMED   17074753
  REMARK    Erratum:[J Biol Chem. 2014 Jul 25;289(30):20490]
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Yang,W.H., Yu,J.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     RNA-associated protein 55 (RAP55) localizes to mRNA processing
            bodies and stress granules
  JOURNAL   RNA 12 (4), 547-554 (2006)
   PUBMED   16484376
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006228918.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.1835.1,
                                           SRR26643287.986.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676810 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..463
                     /product="protein LSM14 homolog A isoform 1"
                     /note="LSM14 homolog A; protein LSM14 homolog A; LSM14A,
                     SCD6 homolog A"
                     /calculated_mol_wt=50499
     Region          4..77
                     /region_name="LSm14_N"
                     /note="Like-Sm protein 14, N-terminal domain; cd01736"
                     /db_xref="CDD:212483"
     Site            order(12..18,20..32,35..39)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212483"
     Site            order(30,32,68)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212483"
     Site            64..75
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212483"
     Region          290..400
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     CDS             1..463
                     /gene="Lsm14a"
                     /gene_synonym="RGD1305695"
                     /coded_by="NM_001438113.1:142..1533"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361554"
                     /db_xref="RGD:1305695"
ORIGIN      
        1 msggtpyigs kisliskaei ryegilytid tenstvalak vrsfgtedrp tdrpipprde
       61 vfeyiifrgs dikdltvcep pkpqcslpqd paivqsslgs ssssfqsvgs ygpfgrmpay
      121 sqfspstlvg qqfgavgvag ssltsfgtea snsgtlsqsn avgsaftqdt rsvkpqlaqg
      181 rsspqldplr ksptmeqavq tasahlpapa pvgrrspvpa rplpptsqka idnqehrrae
      241 vhkvprpene qlrndskrqv vpgvpsaprr grgghrggrg rfgirrdgpm kfekdfdfes
      301 anaqfnkeei drefhnklkl kedklekqek pvngedkgds gvdtqnsegn adeedplgpn
      361 cyydktksff dniscddnre rrptwaeerr lnaetfgipl rpnrgrggyr grgglgfrgg
      421 rgrgsgrggt ftaprgfrag frgarggref adfeyrkdnk vaa
//
LOCUS       NP_001425014             377 aa            linear   ROD 17-APR-2025
DEFINITION  vasodilator-stimulated phosphoprotein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425014 XP_038937661
VERSION     NP_001425014.1
DBSOURCE    REFSEQ: accession NM_001438085.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Samuel,S., Zhang,K., Tang,Y.D., Gerdes,A.M. and
            Carrillo-Sepulveda,M.A.
  TITLE     Triiodothyronine Potentiates Vasorelaxation via PKG/VASP Signaling
            in Vascular Smooth Muscle Cells
  JOURNAL   Cell Physiol Biochem 41 (5), 1894-1904 (2017)
   PUBMED   28376489
  REMARK    GeneRIF: findings have uncovered a PKG/VASP signaling pathway in
            Vascular Smooth Muscle Cells as a key molecular mechanism
            underlying T3-induced vascular relaxation.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Basu,S., Kustanovich,I. and Lamprecht,R.
  TITLE     Arp2/3 and VASP Are Essential for Fear Memory Formation in Lateral
            Amygdala
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   27957528
  REMARK    GeneRIF: Study showed that Arp2/3 and VASP, but not formins, are
            needed in lateral amygdala for long-term, but not short-term, fear
            memory formation. Results suggest a mechanism whereby actin
            cytoskeleton remodeling leads to changes in neuronal morphogenesis
            needed for memory consolidation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Li,H., Liu,J., Wang,W., Zhang,Z., Li,D., Lin,K., Chen,Z. and Lin,W.
  TITLE     Matrix Metalloproteinase 9 and Vasodilator-Stimulated
            Phosphoprotein Related to Acute Kidney Injury in Severe Acute
            Pancreatitis Rats
  JOURNAL   Dig Dis Sci 60 (12), 3647-3655 (2015)
   PUBMED   26264698
  REMARK    GeneRIF: In the presence of acute kidney injury in severe, acute
            pancreatitis, the renal expression of MMP-9 and VASP is related to
            damage of endothelial cells in capillaries, which reached a maximum
            at 24 h and declined afterwards.
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: Co-expression of VASP increased the ability of Mena and
            EVL to form mixed oligomers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Zhao,H., Guan,Q., Smith,C.J. and Quilley,J.
  TITLE     Increased phosphodiesterase 3A/4B expression after angioplasty and
            the effect on VASP phosphorylation
  JOURNAL   Eur J Pharmacol 590 (1-3), 29-35 (2008)
   PUBMED   18571642
  REMARK    GeneRIF: Increased phosphodiesterase 3A/4B expression after
            angioplasty and the effect on VASP phosphorylation.
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Ferron,F., Rebowski,G., Lee,S.H. and Dominguez,R.
  TITLE     Structural basis for the recruitment of profilin-actin complexes
            during filament elongation by Ena/VASP
  JOURNAL   EMBO J 26 (21), 4597-4606 (2007)
   PUBMED   17914456
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Menzies,A.S., Aszodi,A., Williams,S.E., Pfeifer,A., Wehman,A.M.,
            Goh,K.L., Mason,C.A., Fassler,R. and Gertler,F.B.
  TITLE     Mena and vasodilator-stimulated phosphoprotein are required for
            multiple actin-dependent processes that shape the vertebrate
            nervous system
  JOURNAL   J Neurosci 24 (37), 8029-8038 (2004)
   PUBMED   15371503
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Mejillano,M.R., Kojima,S., Applewhite,D.A., Gertler,F.B.,
            Svitkina,T.M. and Borisy,G.G.
  TITLE     Lamellipodial versus filopodial mode of the actin nanomachinery:
            pivotal role of the filament barbed end
  JOURNAL   Cell 118 (3), 363-373 (2004)
   PUBMED   15294161
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Tanoue,T. and Takeichi,M.
  TITLE     Mammalian Fat1 cadherin regulates actin dynamics and cell-cell
            contact
  JOURNAL   J Cell Biol 165 (4), 517-528 (2004)
   PUBMED   15148305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_038937661.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.1768.1,
                                           SRR26643297.975.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..377
                     /product="vasodilator-stimulated phosphoprotein isoform 1"
                     /calculated_mol_wt=39721
     Region          6..114
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(17,24,72,74,80,82,84)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          216..242
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(223..224,226..227,230,232..236)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          232..235
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          341..373
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..377
                     /gene="Vasp"
                     /coded_by="NM_001438085.1:300..1433"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361517"
                     /db_xref="RGD:1311542"
ORIGIN      
        1 msnetvicss ratvmlydds nkrwlpagtg pqafsrvqiy hnptansfrv vgrklqpdqq
       61 vvincaiirg vkynqatpif hqwrdarqvw glnfgskeda aqfaigmana lealegggpp
      121 papappawst qngpspeele qqkrqpehle rrvsnaggpp appaggpppp pgpppppgpp
      181 pppglppsgv sgaghgtgva pppapplpta qgpssggsga pglaaaiaga klrkvskqee
      241 asggplapka ensrgtgggl meemnamlar rrkatqvgek ppkdesasqe esearipaqs
      301 epvrrpwekn sttlprmkss ssvttseahp svpsssddsd lervkqelve evrkelqkmk
      361 eeiievfvqe lrkrgsp
//
LOCUS       NP_001424961             268 aa            linear   ROD 17-APR-2025
DEFINITION  programmed cell death 1 ligand 2 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001424961 XP_006231271
VERSION     NP_001424961.1
DBSOURCE    REFSEQ: accession NM_001438032.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wang,T., Chen,S., Wang,X., Huang,Y., Qiu,J., Fei,Y., Chaulagain,A.,
            Chen,Y., Wang,Y., Lin,L., Yan,B., Wang,Y., Wang,W., Zhao,W. and
            Zhong,Z.
  TITLE     Aberrant PD-1 ligand expression contributes to the myocardial
            inflammatory injury caused by Coxsackievirus B infection
  JOURNAL   Antiviral Res 166, 1-10 (2019)
   PUBMED   30904424
REFERENCE   2  (residues 1 to 268)
  AUTHORS   He,H., Zhou,Y., Zhou,Y., Zhuang,J., He,X., Wang,S. and Lin,W.
  TITLE     Dexmedetomidine Mitigates Microglia-Mediated Neuroinflammation
            through Upregulation of Programmed Cell Death Protein 1 in a Rat
            Spinal Cord Injury Model
  JOURNAL   J Neurotrauma 35 (21), 2591-2603 (2018)
   PUBMED   29665726
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Wilson,J.K., Zhao,Y., Singer,M., Spencer,J. and Shankar-Hari,M.
  TITLE     Lymphocyte subset expression and serum concentrations of PD-1/PD-L1
            in sepsis - pilot study
  JOURNAL   Crit Care 22 (1), 95 (2018)
   PUBMED   29661225
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Singh,A., Mohan,A., Dey,A.B. and Mitra,D.K.
  TITLE     Inhibiting the programmed death 1 pathway rescues Mycobacterium
            tuberculosis-specific interferon gamma-producing T cells from
            apoptosis in patients with pulmonary tuberculosis
  JOURNAL   J Infect Dis 208 (4), 603-615 (2013)
   PUBMED   23661793
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Cao,J., Liu,F.X. and Yu,M.X.
  TITLE     Expression of programmed death 1 and its ligands in the liver of
            autoimmune hepatitis C57BL/6 mice
  JOURNAL   Chin Med J (Engl) 122 (16), 1941-1946 (2009)
   PUBMED   19781375
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Vogt,L., Schmitz,N., Kurrer,M.O., Bauer,M., Hinton,H.I., Behnke,S.,
            Gatto,D., Sebbel,P., Beerli,R.R., Sonderegger,I., Kopf,M.,
            Saudan,P. and Bachmann,M.F.
  TITLE     VSIG4, a B7 family-related protein, is a negative regulator of T
            cell activation
  JOURNAL   J Clin Invest 116 (10), 2817-2826 (2006)
   PUBMED   17016562
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Liang,S.C., Greenwald,R.J., Latchman,Y.E., Rosas,L., Satoskar,A.,
            Freeman,G.J. and Sharpe,A.H.
  TITLE     PD-L1 and PD-L2 have distinct roles in regulating host immunity to
            cutaneous leishmaniasis
  JOURNAL   Eur J Immunol 36 (1), 58-64 (2006)
   PUBMED   16358363
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Brown,J.A., Dorfman,D.M., Ma,F.R., Sullivan,E.L., Munoz,O.,
            Wood,C.R., Greenfield,E.A. and Freeman,G.J.
  TITLE     Blockade of programmed death-1 ligands on dendritic cells enhances
            T cell activation and cytokine production
  JOURNAL   J Immunol 170 (3), 1257-1266 (2003)
   PUBMED   12538684
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Tseng,S.Y., Otsuji,M., Gorski,K., Huang,X., Slansky,J.E., Pai,S.I.,
            Shalabi,A., Shin,T., Pardoll,D.M. and Tsuchiya,H.
  TITLE     B7-DC, a new dendritic cell molecule with potent costimulatory
            properties for T cells
  JOURNAL   J Exp Med 193 (7), 839-846 (2001)
   PUBMED   11283156
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Latchman,Y., Wood,C.R., Chernova,T., Chaudhary,D., Borde,M.,
            Chernova,I., Iwai,Y., Long,A.J., Brown,J.A., Nunes,R.,
            Greenfield,E.A., Bourque,K., Boussiotis,V.A., Carter,L.L.,
            Carreno,B.M., Malenkovich,N., Nishimura,H., Okazaki,T., Honjo,T.,
            Sharpe,A.H. and Freeman,G.J.
  TITLE     PD-L2 is a second ligand for PD-1 and inhibits T cell activation
  JOURNAL   Nat Immunol 2 (3), 261-268 (2001)
   PUBMED   11224527
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231271.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.4214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..268
                     /product="programmed cell death 1 ligand 2 isoform 1
                     precursor"
                     /note="PD-1 ligand 2; PDCD1 ligand 2; programmed death
                     ligand 2"
                     /calculated_mol_wt=27904
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2114
     Region          20..119
                     /region_name="IgV_PD-L2"
                     /note="Immunoglobulin Variable (IgV) domain of Programmed
                     death ligand 2 (PD-L2); cd20983"
                     /db_xref="CDD:409575"
     Site            order(20..22,25,28,56,60,67,101,103,105,107..110,112..114)
                     /site_type="other"
                     /note="Receptor-Ligand Binding Site [polypeptide binding]"
                     /db_xref="CDD:409575"
     Region          20..43
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409575"
     Region          22..25
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409575"
     Region          28..32
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409575"
     Region          35..43
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409575"
     Region          44..55
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409575"
     Region          55..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409575"
     Region          56..63
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409575"
     Region          64..71
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409575"
     Region          66..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409575"
     Region          72..104
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409575"
     Region          72..76
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409575"
     Region          84..91
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409575"
     Region          95..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409575"
     Region          105..108
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409575"
     Region          108..119
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409575"
     Region          110..119
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409575"
     Region          127..208
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          139..143
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          189..194
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          204..207
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..268
                     /gene="Pdcd1lg2"
                     /gene_synonym="PD-L2"
                     /coded_by="NM_001438032.1:287..1093"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:309304"
                     /db_xref="RGD:1306403"
ORIGIN      
        1 mlllllilnl ssqlhhiaal ftvtapkevy tvdfgssvsl ecdfdrrect elegiraslq
       61 kvendtssqs qratlleell plgkasfhip svqvrdsgqy rclvicgaaw dykyltvkvk
      121 asyvridtgi levpgtgevq licqargypl aevswqnvsv pantshirtp eglyqvtsvl
      181 rlkpqpnrnf scmfwnahmk eltsaiidpl swmepkvprt rslhafipac tvaliflatv
      241 iaqrkrlwgk lysrkrsepa vlgvgkiq
//
LOCUS       NP_001424631             894 aa            linear   ROD 17-APR-2025
DEFINITION  phosphatidate phosphatase LPIN2 [Rattus norvegicus].
ACCESSION   NP_001424631
VERSION     NP_001424631.1
DBSOURCE    REFSEQ: accession NM_001437702.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Kok,B.P.C., Dyck,J.R.B., Harris,T.E. and Brindley,D.N.
  TITLE     Differential regulation of the expressions of the PGC-1alpha splice
            variants, lipins, and PPARalpha in heart compared to liver
  JOURNAL   J Lipid Res 54 (6), 1662-1677 (2013)
   PUBMED   23505321
  REMARK    GeneRIF: novel differences in the regulation of lipins 1,2,3,
            PPARalpha, and PGC-1alpha splice variants during fasting in heart
            versus liver, even though the ultimate outcome in both tissues is
            to increase FA turnover and oxidation.
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Donkor,J., Zhang,P., Wong,S., O'Loughlin,L., Dewald,J., Kok,B.P.,
            Brindley,D.N. and Reue,K.
  TITLE     A conserved serine residue is required for the phosphatidate
            phosphatase activity but not the transcriptional coactivator
            functions of lipin-1 and lipin-2
  JOURNAL   J Biol Chem 284 (43), 29968-29978 (2009)
   PUBMED   19717560
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Grimsey,N., Han,G.S., O'Hara,L., Rochford,J.J., Carman,G.M. and
            Siniossoglou,S.
  TITLE     Temporal and spatial regulation of the phosphatidate phosphatases
            lipin 1 and 2
  JOURNAL   J Biol Chem 283 (43), 29166-29174 (2008)
   PUBMED   18694939
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Donkor,J., Sariahmetoglu,M., Dewald,J., Brindley,D.N. and Reue,K.
  TITLE     Three mammalian lipins act as phosphatidate phosphatases with
            distinct tissue expression patterns
  JOURNAL   J Biol Chem 282 (6), 3450-3457 (2007)
   PUBMED   17158099
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.35182.1,
                                           SRR26643288.39182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..894
                     /product="phosphatidate phosphatase LPIN2"
                     /EC_number="3.1.3.4"
                     /calculated_mol_wt=99578
     Region          1..107
                     /region_name="Lipin_N"
                     /note="lipin, N-terminal conserved region; pfam04571"
                     /db_xref="CDD:461356"
     Region          <326..483
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          467..559
                     /region_name="Lipin_mid"
                     /note="Lipin/Ned1/Smp2 multi-domain protein middle domain;
                     pfam16876"
                     /db_xref="CDD:465292"
     Region          635..860
                     /region_name="LNS2"
                     /note="LNS2 (Lipin/Ned1/Smp2); pfam08235"
                     /db_xref="CDD:462403"
     Region          873..>891
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     CDS             1..894
                     /gene="Lpin2"
                     /coded_by="NM_001437702.1:202..2886"
                     /db_xref="GeneID:316737"
                     /db_xref="RGD:1304588"
ORIGIN      
        1 mnyvgqlagq vlvtvkelyk ginqatlsgc idvvvvrqqd gsyqcspfhv rfgklgvlrs
       61 kekvidiein gsavdlhmkl gdngeaffve eteeeyeklp aylatspipt edqffkhidp
      121 plvkssgner ppqssdvsht leseavftps svkkkkrrrk kckqdnrkee qaaspvaedv
      181 gdvavssdde kraqaargss naslkeedyk epppfhsgdn yplsdgdwsp letsypqtvc
      241 pksdselevk psesllrses hmewtwggfp estkvskrer ydyhprtati tpsenthfrv
      301 ipsedslire vekdatvedt tctivkpkpr alckqlsdaa stelpesple apqisstlda
      361 dpvpspsaea psepkpaakv dsptkrkgvh krsqhqgpdd iylddlkale pevaalyfpk
      421 sdtdpgsrqw pesdtfsgsq spqsvgsaaa dsgteclsds amdlpdvtls lcgglsenge
      481 iskekfmehi ityhefaenp glidnpnlvi riynryynwa laapmilslq vfqkslpkat
      541 veswvkdkmp kksgrwwfwr kkesmtkqlp etkegksevp pandlpsgte epvsarpaen
      601 dtssdegsqe leetikvdpi smetlshcgt asykkslrls sdqiaklklh dgpndvvfsi
      661 ttqyqgtcrc agtiylwnwn dkviisdidg titksdalgq ilpqlgkdwt hqgiarlyhs
      721 inengykfly csaraigmad mtrgylhwvn dkgtilprgp lmlspsslfs afhreviekk
      781 pekfkiecln diknlfapsr qpfyaafgnr pndvyaytqv gvpdcriftv npkgeliqer
      841 tkgnkssyhr lselvehvfp llnkeqnsaf pcpefssfcy wrdpipdvdl ddla
//
LOCUS       NP_001424981             411 aa            linear   ROD 17-APR-2025
DEFINITION  LIM domain-binding protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424981 XP_006231555
VERSION     NP_001424981.1
DBSOURCE    REFSEQ: accession NM_001438052.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   van Tienen,L.M., Mieszczanek,J., Fiedler,M., Rutherford,T.J. and
            Bienz,M.
  TITLE     Constitutive scaffolding of multiple Wnt enhanceosome components by
            Legless/BCL9
  JOURNAL   Elife 6, e20882 (2017)
   PUBMED   28296634
  REMARK    Erratum:[Elife. 2017 Mar 30;6:e27150. doi: 10.7554/eLife.27150.
            PMID: 28358670]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Costello,I., Nowotschin,S., Sun,X., Mould,A.W., Hadjantonakis,A.K.,
            Bikoff,E.K. and Robertson,E.J.
  TITLE     Lhx1 functions together with Otx2, Foxa2, and Ldb1 to govern
            anterior mesendoderm, node, and midline development
  JOURNAL   Genes Dev 29 (20), 2108-2122 (2015)
   PUBMED   26494787
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Song,S.H., Kim,A., Ragoczy,T., Bender,M.A., Groudine,M. and Dean,A.
  TITLE     Multiple functions of Ldb1 required for beta-globin activation
            during erythroid differentiation
  JOURNAL   Blood 116 (13), 2356-2364 (2010)
   PUBMED   20570862
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Agulnick,A.D., Taira,M., Breen,J.J., Tanaka,T., Dawid,I.B. and
            Westphal,H.
  TITLE     Interactions of the LIM-domain-binding factor Ldb1 with LIM
            homeodomain proteins
  JOURNAL   Nature 384 (6606), 270-272 (1996)
   PUBMED   8918878
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Jurata,L.W., Kenny,D.A. and Gill,G.N.
  TITLE     Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
            protein, is expressed early in neuronal development
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11693-11698 (1996)
   PUBMED   8876198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231555.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.910088.1,
                                           SRR26360190.2736670.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..411
                     /product="LIM domain-binding protein 1 isoform 1"
                     /note="LIM domain-binding protein 1"
                     /calculated_mol_wt=46372
     Region          70..271
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     Region          336..364
                     /region_name="LID"
                     /note="LIM interaction domain (LID); pfam17916"
                     /db_xref="CDD:465564"
     CDS             1..411
                     /gene="Ldb1"
                     /coded_by="NM_001438052.1:259..1494"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309447"
                     /db_xref="RGD:1310359"
ORIGIN      
        1 msvgcacpgc ssksfklysp keppngnafp pfhpgtmldr dvgptpmypp tylepgigrh
       61 tpygnqtdyr ifelnkrlqn wteecdnlww daftteffed damltitfcl edgpkrytig
      121 rtlipryfrs ifeggately yvlkhpkeaf hsnfvsldcd qgsmvtqhgk pmftqvcveg
      181 rlylefmfdd mmriktwhfs irqhrelipr silamhaqdp qmldqlskni trcglsnstl
      241 nylrlcvile pmqelmsrhk tyslsprdcl ktclfqkwqr mvappaepar qqpskrrkrk
      301 msggstmssg ggntnnsnsk kkspastfal ssqvpdvmvv geptlmggef gdederlitr
      361 lentqfdaan giddedsfnn spalganspw nskppssqes ksenptsqas q
//
LOCUS       NP_001425361             404 aa            linear   ROD 18-APR-2025
DEFINITION  activating transcription factor 7-interacting protein 2 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001425361 XP_008765717
VERSION     NP_001425361.1
DBSOURCE    REFSEQ: accession NM_001438432.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 18, 2025 this sequence version replaced XP_008765717.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.35435.1,
                                           SRR26643293.61368.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..404
                     /product="activating transcription factor 7-interacting
                     protein 2 isoform 3"
                     /calculated_mol_wt=45019
     Region          70..278
                     /region_name="ATF7IP_BD"
                     /note="ATF-interacting protein binding domain; pfam16788"
                     /db_xref="CDD:465271"
     CDS             1..404
                     /gene="Atf7ip2"
                     /coded_by="NM_001438432.1:78..1292"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:497859"
                     /db_xref="RGD:1583744"
ORIGIN      
        1 mespdrkrrk vlkakktmpt scrkqmeiln qsknveapkt tvvtnipngn qslgtgfias
       61 hnqkmfsenk envkvmktse qinenaceal erhtalleqv khwirqeict incnlfdkkl
      121 nelnerigkt qcrskheaia gelfikirrl qkriktvlss qgnclepntl psntvckvtd
      181 svnlsvtqrs vksqskrmss vnhtpfnsse kasrkinlps acvefvsesn ddvmlisven
      241 pnlttpiasd pteirkntsr nvssspnars evvpvekkfd fvidltregl ssysigppss
      301 rlhhlriaps aedqafntga fgdhsnsrvq qigtkpstrr kkipvkeken lqqenttrrg
      361 dgggysrvqk seltgtrppg msssssdnrk gfntsflnqn rtlp
//
LOCUS       NP_071784                471 aa            linear   ROD 18-APR-2025
DEFINITION  7-dehydrocholesterol reductase [Rattus norvegicus].
ACCESSION   NP_071784
VERSION     NP_071784.1
DBSOURCE    REFSEQ: accession NM_022389.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Sun,L., Lu,J., Yao,D., Li,X., Cao,Y., Gao,J., Liu,J., Zheng,T.,
            Wang,H. and Zhan,X.
  TITLE     Effect of DHCR7 for the co-occurrence of hypercholesterolemia and
            vitamin D deficiency in type 2 diabetes: Perspective of health
            prevention
  JOURNAL   Prev Med 173, 107576 (2023)
   PUBMED   37329988
  REMARK    GeneRIF: Effect of DHCR7 for the co-occurrence of
            hypercholesterolemia and vitamin D deficiency in type 2 diabetes:
            Perspective of health prevention.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kwak,S.Y., Cho,Y., Oh,H. and Shin,M.J.
  TITLE     Association of circulating 25-hydroxyvitamin D levels with
            hypertension and blood pressure values in Korean adults: A
            Mendelian randomization study on a subset of the Korea National
            Health and Nutrition Survey 2011-2012 population
  JOURNAL   Nutr Res Pract 13 (6), 498-508 (2019)
   PUBMED   31814925
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Fang,J., Hou,S., Xiang,Q., Qi,J., Yu,H., Shi,Y., Zhou,Y.,
            Kijlstra,A. and Yang,P.
  TITLE     Polymorphisms in genetics of vitamin D metabolism confer
            susceptibility to ocular Behcet disease in a Chinese Han population
  JOURNAL   Am J Ophthalmol 157 (2), 488-494 (2014)
   PUBMED   24184224
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bae,S.H., Lee,J.N., Fitzky,B.U., Seong,J. and Paik,Y.K.
  TITLE     Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
            distribution, expression, chromosomal localization, and regulation
            of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz
            syndrome-related protein
  JOURNAL   J Biol Chem 274 (21), 14624-14631 (1999)
   PUBMED   10329655
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Holmer,L., Pezhman,A. and Worman,H.J.
  TITLE     The human lamin B receptor/sterol reductase multigene family
  JOURNAL   Genomics 54 (3), 469-476 (1998)
   PUBMED   9878250
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Shefer,S., Salen,G., Honda,A., Batta,A.K., Nguyen,L.B., Tint,G.S.,
            Ioannou,Y.A. and Desnick,R.
  TITLE     Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase:
            substrate specificity, competitive and non-competitive inhibition,
            and phosphorylation/dephosphorylation
  JOURNAL   J Lipid Res 39 (12), 2471-2476 (1998)
   PUBMED   9831636
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Waterham,H.R., Wijburg,F.A., Hennekam,R.C., Vreken,P.,
            Poll-The,B.T., Dorland,L., Duran,M., Jira,P.E., Smeitink,J.A.,
            Wevers,R.A. and Wanders,R.J.
  TITLE     Smith-Lemli-Opitz syndrome is caused by mutations in the
            7-dehydrocholesterol reductase gene
  JOURNAL   Am J Hum Genet 63 (2), 329-338 (1998)
   PUBMED   9683613
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Moebius,F.F., Fitzky,B.U., Lee,J.N., Paik,Y.K. and Glossmann,H.
  TITLE     Molecular cloning and expression of the human delta7-sterol
            reductase
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1899-1902 (1998)
   PUBMED   9465114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF272393.1, SRR26643429.4225.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680414, SAMN06680437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..471
                     /product="7-dehydrocholesterol reductase"
                     /EC_number="1.3.1.21"
                     /EC_number="3.3.2.11"
                     /note="7-DHC reductase; sterol Delta(7)-reductase;
                     cholesterol-5,6-epoxide hydrolase subunit DHCR7"
                     /calculated_mol_wt=54024
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Region          89..471
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     CDS             1..471
                     /gene="Dhcr7"
                     /coded_by="NM_022389.4:312..1727"
                     /db_xref="GeneID:64191"
                     /db_xref="RGD:621769"
ORIGIN      
        1 masksqhnas kaknhnvkae sqgqwgrawe vdwfslvsvi flllfapfiv yyfimacdqy
       61 scsltapild vatgraslad iwaktppvta kaaqlyalwv sfqvllyswl pdfchrflpg
      121 yvggvqegai tpagivnkye vnglqawlit hflwfvnayl lswfsptiif dnwipllwca
      181 nilgyavstf amikgylfpt saedckftgn ffynymmgie fnprigkwfd fklffngrpg
      241 ivawtlinls faakqqelyg hvtnsmilvn vlqaiyvldf fwnetwylkt idichdhfgw
      301 ylgwgdcvwl pylytlqgly lvyhpvqlst pnalgvlllg lvgyyifrmt nhqkdlfrrt
      361 dghcliwgkk pkaiecsyts adglkhrskl lvsgfwgvar hfnytgdlmg slayclacgg
      421 ghllpyfyii ymtillthrc lrdehrcank ygrdweryva avpyrllpgi f
//
LOCUS       NP_001425338             105 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 8 [Rattus
            norvegicus].
ACCESSION   NP_001425338
VERSION     NP_001425338.1
DBSOURCE    REFSEQ: accession NM_001438409.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.5373.1,
                                           SRR26643298.6868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..105
                     /product="bcl2-associated agonist of cell death isoform 8"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=10807
     Region          43..>104
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     CDS             1..105
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438409.1:419..736"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 mgtpkqpsla pahalglrks dpgirslgsd aggrrwrpaa qsmfqipefe pseqedastt
       61 drglgpslte dqpgpylapg llgsivqqqp gqaannshhg dgagr
//
LOCUS       NP_001425337             116 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001425337
VERSION     NP_001425337.1
DBSOURCE    REFSEQ: accession NM_001438408.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1448324.1,
                                           SRR26360186.864609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..116
                     /product="bcl2-associated agonist of cell death isoform 7"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=13397
     Region          <1..>61
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..116
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438408.1:396..746"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 metrsrhssy pagteedegm eeelspfrgr srsappnlwa aqrygrelrr msdefegsfk
       61 geeltysvef lpvraiameg wpllwsfqsf phtlpptppe vamfplrywt alrrlc
//
LOCUS       NP_001425244             582 aa            linear   ROD 18-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001425244 XP_017444428
VERSION     NP_001425244.1
DBSOURCE    REFSEQ: accession NM_001438315.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_017444428.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2190121.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..582
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 2"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=64244
     Region          42..344
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          346..436
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          447..530
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          524..579
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..582
                     /gene="Cpeb1"
                     /coded_by="NM_001438315.1:652..2400"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 maplklsira pragralsep gevtwlhtfd cfwspspegg pdqeeesgri kdcwdnqevp
       61 alstcsnani frrinaildd sldfskvctt pinrgihdql pdfqdseeai tsrmlfptsa
      121 qesprglpda nglclglqsl sltgwdrpws tqdsdssaqs ntqsvlsmlq nplgnvlgkt
      181 plsflsldpl gsdldkfpap svrgsrldtr pildsrsssp sdsdtsgfss gsdhlsdlis
      241 slrispplpf lsmtgngprd plkmgvgsrm dqeqaalaav apsptsapkr wpgtsvwpsw
      301 dllgapkdpf sierearlhr qaaavneatc twsgqlpprn yknpiysckv flggvpwdit
      361 eaglvntfrv fgslsvewpg yvylvfelek svrallqacs hdplspdgls eyyfkmssrr
      421 mrckevqvip wvladsnfvw spsqrldpsr tvfvgalhgm lnaealaail ndlfggvvya
      481 gidtdkhkyp igsgrvtfnn qrsylkavta afveikttkf tkkvqidpyl edslclicss
      541 qpgpffcrdq vcfkyfcrsc whwrhsmegl rhhsplmrnq kn
//
LOCUS       NP_075227                435 aa            linear   ROD 18-APR-2025
DEFINITION  5-hydroxytryptamine receptor 7 isoform 2 [Rattus norvegicus].
ACCESSION   NP_075227
VERSION     NP_075227.1
DBSOURCE    REFSEQ: accession NM_022938.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Korlatowicz,A., Pabian,P., Solich,J., Kolasa,M., Latocha,K.,
            Dziedzicka-Wasylewska,M. and Faron-Gorecka,A.
  TITLE     Habenula as a Possible Target for Treatment-Resistant Depression
            Phenotype in Wistar Kyoto Rats
  JOURNAL   Mol Neurobiol 60 (2), 643-654 (2023)
   PUBMED   36344870
  REMARK    GeneRIF: Habenula as a Possible Target for Treatment-Resistant
            Depression Phenotype in Wistar Kyoto Rats.
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Slawinska,U., Majczynski,H., Kwasniewska,A., Miazga,K., Cabaj,A.M.,
            Bekisz,M., Jordan,L.M. and Zawadzka,M.
  TITLE     Unusual Quadrupedal Locomotion in Rat during Recovery from Lumbar
            Spinal Blockade of 5-HT7 Receptors
  JOURNAL   Int J Mol Sci 22 (11), 6007 (2021)
   PUBMED   34199392
  REMARK    GeneRIF: Unusual Quadrupedal Locomotion in Rat during Recovery from
            Lumbar Spinal Blockade of 5-HT7 Receptors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Cinar,I., Halici,Z., Dincer,B., Sirin,B. and Cadirci,E.
  TITLE     The role of 5-HT7 receptors on isoproterenol-induced myocardial
            infarction in rats with high-fat diet exacerbated coronary
            endothelial dysfunction
  JOURNAL   Hum Exp Toxicol 39 (8), 1005-1018 (2020)
   PUBMED   32329363
  REMARK    GeneRIF: The role of 5-HT7 receptors on isoproterenol-induced
            myocardial infarction in rats with high-fat diet exacerbated
            coronary endothelial dysfunction.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Hernandez-Abreu,O.I., Garcia-Pedraza,J.A., Rivera-Mancilla,E.,
            Villanueva-Castillo,B., Moran,A., Garcia-Domingo,M.,
            Manrique-Maldonado,G., Altamirano-Espinoza,A.H. and Villalon,C.M.
  TITLE     Blockade of 5-HT2 receptors with sarpogrelate uncovers 5-HT7
            receptors inhibiting the tachycardic sympathetic drive in pithed
            rats
  JOURNAL   Clin Exp Pharmacol Physiol 47 (3), 403-411 (2020)
   PUBMED   31846086
  REMARK    GeneRIF: Blockade of 5-HT2 receptors with sarpogrelate uncovers
            5-HT7 receptors inhibiting the tachycardic sympathetic drive in
            pithed rats.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Seitz,B.M., Demireva,E.Y., Xie,H., Fink,G.D., Krieger-Burke,T.,
            Burke,W.M. and Watts,S.W.
  TITLE     5-HT does not lower blood pressure in the 5-HT7 knockout rat
  JOURNAL   Physiol Genomics 51 (7), 302-310 (2019)
   PUBMED   31125292
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Heidmann,D.E., Metcalf,M.A., Kohen,R. and Hamblin,M.W.
  TITLE     Four 5-hydroxytryptamine7 (5-HT7) receptor isoforms in human and
            rat produced by alternative splicing: species differences due to
            altered intron-exon organization
  JOURNAL   J Neurochem 68 (4), 1372-1381 (1997)
   PUBMED   9084407
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Ruat,M., Traiffort,E., Leurs,R., Tardivel-Lacombe,J., Diaz,J.,
            Arrang,J.M. and Schwartz,J.C.
  TITLE     Molecular cloning, characterization, and localization of a
            high-affinity serotonin receptor (5-HT7) activating cAMP formation
  JOURNAL   Proc Natl Acad Sci U S A 90 (18), 8547-8551 (1993)
   PUBMED   8397408
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Lovenberg,T.W., Baron,B.M., de Lecea,L., Miller,J.D., Prosser,R.A.,
            Rea,M.A., Foye,P.E., Racke,M., Slone,A.L., Siegel,B.W. et al.
  TITLE     A novel adenylyl cyclase-activating serotonin receptor (5-HT7)
            implicated in the regulation of mammalian circadian rhythms
  JOURNAL   Neuron 11 (3), 449-458 (1993)
   PUBMED   8398139
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Shen,Y., Monsma,F.J. Jr., Metcalf,M.A., Jose,P.A., Hamblin,M.W. and
            Sibley,D.R.
  TITLE     Molecular cloning and expression of a 5-hydroxytryptamine7
            serotonin receptor subtype
  JOURNAL   J Biol Chem 268 (24), 18200-18204 (1993)
   PUBMED   8394362
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Meyerhof,W., Obermuller,F., Fehr,S. and Richter,D.
  TITLE     A novel rat serotonin receptor: primary structure, pharmacology,
            and expression pattern in distinct brain regions
  JOURNAL   DNA Cell Biol 12 (5), 401-409 (1993)
   PUBMED   8517926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L22558.1, U68489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..435
                     /product="5-hydroxytryptamine receptor 7 isoform 2"
                     /note="serotonin receptor 7; GPRFO; 5-HT-7; 5-HT-X; 5-HT7;
                     high affinity serotonin receptor (5HT7);
                     5-hydroxytryptamine (serotonin) receptor 7, adenylate
                     cyclase-coupled"
                     /calculated_mol_wt=48297
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32305.2)"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32305.2)"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          100..398
                     /region_name="7tmA_5-HT7"
                     /note="serotonin receptor subtype 7, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15329"
                     /db_xref="CDD:320452"
     Region          119..145
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320452"
     Site            122..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Site            156..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          158..188
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320452"
     Site            order(161..162,165..166,169..170,234,246,250,343,346..347,
                     353,366,369..370,373,377)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320452"
     Region          200..222
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320452"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          239..268
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320452"
     Site            241..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          323..353
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320452"
     Site            330..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          366..391
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320452"
     Site            367..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     CDS             1..435
                     /gene="Htr7"
                     /gene_synonym="5Ht7"
                     /coded_by="NM_022938.3:116..1423"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65032"
                     /db_xref="RGD:71034"
ORIGIN      
        1 mmdvnssgrp dlyghlrsli lpevgrglqd lspdggahpv vsswmphlls gflevtaspa
       61 ptwdappdnv sgcgeqinyg rvekvvigsi ltlitlltia gnclvvisvc fvkklrqpsn
      121 ylivslalad lsvavavmpf vsvtdliggk wifghffcnv fiamdvmcct asimtlcvis
      181 idrylgitrp ltypvrqngk cmakmilsvw llsasitlpp lfgwaqnvnd dkvclisqdf
      241 gytiystava fyipmsvmlf myyqiykaar ksaakhkfpg fprvqpesvi slngvvklqk
      301 eveecanlsr llkherknis ifkreqkaat tlgiivgaft vcwlpfflls tarpficgts
      361 csciplwver tclwlgyans linpfiyaff nrdlrttyrs llqcqyrnin rklsaagmhe
      421 alklaerper sefvl
//
LOCUS       NP_001425324            1231 aa            linear   ROD 18-APR-2025
DEFINITION  centlein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425324
VERSION     NP_001425324.1
DBSOURCE    REFSEQ: accession NM_001438395.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Fang,G., Zhang,D., Yin,H., Zheng,L., Bi,X. and Yuan,L.
  TITLE     Centlein mediates an interaction between C-Nap1 and Cep68 to
            maintain centrosome cohesion
  JOURNAL   J Cell Sci 127 (Pt 8), 1631-1639 (2014)
   PUBMED   24554434
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Makino,K., Umeda,K., Uezu,A., Hiragami,Y., Sakamoto,T., Ihn,H. and
            Nakanishi,H.
  TITLE     Identification and characterization of the novel centrosomal
            protein centlein
  JOURNAL   Biochem Biophys Res Commun 366 (4), 958-962 (2008)
   PUBMED   18086554
  REMARK    GeneRIF: The molecular characterization of a novel protein, named
            centlein (centrosomal protein), is described. Centlein was a
            protein of 721 amino acids with a calculated molecular weight of
            82,717 and possessed coiled-coil domains.[Centlein]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.19560.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..1231
                     /product="centlein isoform 2"
                     /note="centrosomal protein; centlein, centrosomal protein"
                     /calculated_mol_wt=141488
     Region          <105..>727
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <471..1212
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1231
                     /gene="Cntln"
                     /gene_synonym="RGD1308101"
                     /coded_by="NM_001438395.1:168..3863"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:679640"
                     /db_xref="RGD:1308101"
ORIGIN      
        1 maarspsssp psplarrssr ralrvgrgae vhavrseasg lastarevva dksdllwrgk
       61 egsggrrgsg rpgaalapvl sapvgswwpg glssveakat rsqlleeels svkeelaqcq
      121 adkefvwslw krlqatnpdl tqtvslvver ekqkseakdr kvleilqvkd akiqeleqte
      181 avlnrelydl vklktlvdee naflkkefsd lqkkfkdksq eakdakecvq skeeqnrlli
      241 knleeenerv rarctdllnd leklrmqeah wreekhsada kvkvleenli eakkeiessq
      301 srynavslql nskqtellqk dmditlvrke lqelqnlykq nsahtaqqad liqqlqvlnm
      361 dtqkvlrnqe dahtaesity qelynelhic fettksneam lqqrvanlqh qlfqkeqenv
      421 klkeklqesq gtlglsphes dsnhsakepp vkrsrslspk scfmdseelr klkkaerkiq
      481 nlektlqlks qendelrdah ekrkerlqml htnykavreq lkqweedsgm tetrkpkrad
      541 pqqlrredsd avwnelayfk renqelmvqk mnlqdeldel kiymtidktt iqelnrcmae
      601 kreeqlfrhh edagvkkstp eknekaiseq tlekvielen rlksfeknsr klkeeskklk
      661 kendflkshl qhyqedsesr gkelekllrv sssveqdkse lqtkvtaler evttlrrqva
      721 kakalrdene evvnpeekeh cptdkaksem attdvraqhc dckttttkvk fkaakkkcsv
      781 grhhtvlnhs vkvmshvenl skdgwedmse gssdsetqtf qnlgtvivet sqnirpiend
      841 gnqketdqte dsraqqevqt yscedlkapq ntkkmtfqnk sgslqknlhs alparvnrek
      901 cktkpaqkss sntillreri vslqqqnsll qnarkaaess akefkeanek llhqqqisdh
      961 rfqtsrqtik kltldlaelr kekedllkkv esssditsla eevsrimapq iqvttlgpsr
     1021 stdleikqlq cklknatnel tkqsssvksl klellakddh mkamqekmsr merditmkrh
     1081 liedlkfrqk insesnesfn emlgtlekkv ktlteecsnk kvsvdslkqr lsvavkeksq
     1141 yeqmyqkske elekkdlkmn llisklndte tamaqiksaa seqlqglalq seqvlegtqk
     1201 klllanekie eftvfvqgts rlwkrwkghl l
//
LOCUS       NP_001425339             101 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 9 [Rattus
            norvegicus].
ACCESSION   NP_001425339
VERSION     NP_001425339.1
DBSOURCE    REFSEQ: accession NM_001438410.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.864665.1,
                                           SRR22399492.638313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..101
                     /product="bcl2-associated agonist of cell death isoform 9"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=11347
     Region          <1..101
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..101
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438410.1:396..701"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 metrsrhssy pagteedegm eeelspfrgr srsappnlwa aqrygrelrr msdefegsfk
       61 glprpksagt atqmrqsasw triiqswwdr nlgkggstps q
//
LOCUS       NP_001425289             471 aa            linear   ROD 18-APR-2025
DEFINITION  7-dehydrocholesterol reductase [Rattus norvegicus].
ACCESSION   NP_001425289 XP_006230955
VERSION     NP_001425289.1
DBSOURCE    REFSEQ: accession NM_001438360.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Sun,L., Lu,J., Yao,D., Li,X., Cao,Y., Gao,J., Liu,J., Zheng,T.,
            Wang,H. and Zhan,X.
  TITLE     Effect of DHCR7 for the co-occurrence of hypercholesterolemia and
            vitamin D deficiency in type 2 diabetes: Perspective of health
            prevention
  JOURNAL   Prev Med 173, 107576 (2023)
   PUBMED   37329988
  REMARK    GeneRIF: Effect of DHCR7 for the co-occurrence of
            hypercholesterolemia and vitamin D deficiency in type 2 diabetes:
            Perspective of health prevention.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kwak,S.Y., Cho,Y., Oh,H. and Shin,M.J.
  TITLE     Association of circulating 25-hydroxyvitamin D levels with
            hypertension and blood pressure values in Korean adults: A
            Mendelian randomization study on a subset of the Korea National
            Health and Nutrition Survey 2011-2012 population
  JOURNAL   Nutr Res Pract 13 (6), 498-508 (2019)
   PUBMED   31814925
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Fang,J., Hou,S., Xiang,Q., Qi,J., Yu,H., Shi,Y., Zhou,Y.,
            Kijlstra,A. and Yang,P.
  TITLE     Polymorphisms in genetics of vitamin D metabolism confer
            susceptibility to ocular Behcet disease in a Chinese Han population
  JOURNAL   Am J Ophthalmol 157 (2), 488-494 (2014)
   PUBMED   24184224
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bae,S.H., Lee,J.N., Fitzky,B.U., Seong,J. and Paik,Y.K.
  TITLE     Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
            distribution, expression, chromosomal localization, and regulation
            of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz
            syndrome-related protein
  JOURNAL   J Biol Chem 274 (21), 14624-14631 (1999)
   PUBMED   10329655
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Holmer,L., Pezhman,A. and Worman,H.J.
  TITLE     The human lamin B receptor/sterol reductase multigene family
  JOURNAL   Genomics 54 (3), 469-476 (1998)
   PUBMED   9878250
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Shefer,S., Salen,G., Honda,A., Batta,A.K., Nguyen,L.B., Tint,G.S.,
            Ioannou,Y.A. and Desnick,R.
  TITLE     Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase:
            substrate specificity, competitive and non-competitive inhibition,
            and phosphorylation/dephosphorylation
  JOURNAL   J Lipid Res 39 (12), 2471-2476 (1998)
   PUBMED   9831636
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Waterham,H.R., Wijburg,F.A., Hennekam,R.C., Vreken,P.,
            Poll-The,B.T., Dorland,L., Duran,M., Jira,P.E., Smeitink,J.A.,
            Wevers,R.A. and Wanders,R.J.
  TITLE     Smith-Lemli-Opitz syndrome is caused by mutations in the
            7-dehydrocholesterol reductase gene
  JOURNAL   Am J Hum Genet 63 (2), 329-338 (1998)
   PUBMED   9683613
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Moebius,F.F., Fitzky,B.U., Lee,J.N., Paik,Y.K. and Glossmann,H.
  TITLE     Molecular cloning and expression of the human delta7-sterol
            reductase
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1899-1902 (1998)
   PUBMED   9465114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230955.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF071500.1, SRR22399481.722411.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..471
                     /product="7-dehydrocholesterol reductase"
                     /EC_number="1.3.1.21"
                     /EC_number="3.3.2.11"
                     /note="7-DHC reductase; sterol Delta(7)-reductase;
                     cholesterol-5,6-epoxide hydrolase subunit DHCR7"
                     /calculated_mol_wt=54024
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Region          89..471
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     CDS             1..471
                     /gene="Dhcr7"
                     /coded_by="NM_001438360.1:63..1478"
                     /db_xref="GeneID:64191"
                     /db_xref="RGD:621769"
ORIGIN      
        1 masksqhnas kaknhnvkae sqgqwgrawe vdwfslvsvi flllfapfiv yyfimacdqy
       61 scsltapild vatgraslad iwaktppvta kaaqlyalwv sfqvllyswl pdfchrflpg
      121 yvggvqegai tpagivnkye vnglqawlit hflwfvnayl lswfsptiif dnwipllwca
      181 nilgyavstf amikgylfpt saedckftgn ffynymmgie fnprigkwfd fklffngrpg
      241 ivawtlinls faakqqelyg hvtnsmilvn vlqaiyvldf fwnetwylkt idichdhfgw
      301 ylgwgdcvwl pylytlqgly lvyhpvqlst pnalgvlllg lvgyyifrmt nhqkdlfrrt
      361 dghcliwgkk pkaiecsyts adglkhrskl lvsgfwgvar hfnytgdlmg slayclacgg
      421 ghllpyfyii ymtillthrc lrdehrcank ygrdweryva avpyrllpgi f
//
LOCUS       NP_001425288             207 aa            linear   ROD 18-APR-2025
DEFINITION  vascular endothelial growth factor B isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001425288 XP_006230972
VERSION     NP_001425288.1
DBSOURCE    REFSEQ: accession NM_001438359.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Tu,S., Wang,X.Y., Zeng,L.X., Shen,Z.J. and Zhang,Z.H.
  TITLE     LncRNA TINCR improves cardiac hypertrophy by regulating the
            miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway
  JOURNAL   Lab Invest 102 (3), 253-262 (2022)
   PUBMED   34732848
  REMARK    GeneRIF: LncRNA TINCR improves cardiac hypertrophy by regulating
            the miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway.
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Shang,R., Lal,N., Lee,C.S., Zhai,Y., Puri,K., Seira,O.,
            Boushel,R.C., Sultan,I., Rasanen,M., Alitalo,K., Hussein,B. and
            Rodrigues,B.
  TITLE     Cardiac-specific VEGFB overexpression reduces lipoprotein lipase
            activity and improves insulin action in rat heart
  JOURNAL   Am J Physiol Endocrinol Metab 321 (6), E753-E765 (2021)
   PUBMED   34747201
  REMARK    GeneRIF: Cardiac-specific VEGFB overexpression reduces lipoprotein
            lipase activity and improves insulin action in rat heart.
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Lal,N., Chiu,A.P., Wang,F., Zhang,D., Jia,J., Wan,A., Vlodavsky,I.,
            Hussein,B. and Rodrigues,B.
  TITLE     Loss of VEGFB and its signaling in the diabetic heart is associated
            with increased cell death signaling
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (6), H1163-H1175 (2017)
   PUBMED   28314760
  REMARK    GeneRIF: Loss of VEGFB and its downstream signaling is an early
            event following hyperglycemia, is sustained with disease
            progression, and could explain diabetic cardiomyopathy.
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Monastero,R., Garcia-Serrano,S., Lago-Sampedro,A.,
            Rodriguez-Pacheco,F., Colomo,N., Morcillo,S., Martin-Nunez,G.M.,
            Gomez-Zumaquero,J.M., Garcia-Fuentes,E., Soriguer,F.,
            Rojo-Martinez,G. and Garcia-Escobar,E.
  TITLE     Methylation patterns of Vegfb promoter are associated with gene and
            protein expression levels: the effects of dietary fatty acids
  JOURNAL   Eur J Nutr 56 (2), 715-726 (2017)
   PUBMED   26707994
  REMARK    GeneRIF: Data suggest that dietary fatty acids create
            epigenetic/nutrigenomic changes in methylation levels of CpG island
            at Vegfb promoter and changes in Vegfb expression in white
            adipocytes in vivo and in vitro, with particular up-regulation of
            DNA methylation by linoleic acid; Vegfb promoter methylation levels
            are closely related to Vegfb gene expression in visceral and
            subcutaneous adipose tissue.
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Nag,S., Eskandarian,M.R., Davis,J. and Eubanks,J.H.
  TITLE     Differential expression of vascular endothelial growth factor-A
            (VEGF-A) and VEGF-B after brain injury
  JOURNAL   J Neuropathol Exp Neurol 61 (9), 778-788 (2002)
   PUBMED   12230324
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Ikuta,T., Ariga,H. and Matsumoto,K.
  TITLE     Extracellular matrix tenascin-X in combination with vascular
            endothelial growth factor B enhances endothelial cell proliferation
  JOURNAL   Genes Cells 5 (11), 913-927 (2000)
   PUBMED   11122379
REFERENCE   8  (residues 1 to 207)
  AUTHORS   Bellomo,D., Headrick,J.P., Silins,G.U., Paterson,C.A., Thomas,P.S.,
            Gartside,M., Mould,A., Cahill,M.M., Tonks,I.D., Grimmond,S.M.,
            Townson,S., Wells,C., Little,M., Cummings,M.C., Hayward,N.K. and
            Kay,G.F.
  TITLE     Mice lacking the vascular endothelial growth factor-B gene (Vegfb)
            have smaller hearts, dysfunctional coronary vasculature, and
            impaired recovery from cardiac ischemia
  JOURNAL   Circ Res 86 (2), E29-E35 (2000)
   PUBMED   10666423
REFERENCE   9  (residues 1 to 207)
  AUTHORS   Olofsson,B., Pajusola,K., von Euler,G., Chilov,D., Alitalo,K. and
            Eriksson,U.
  TITLE     Genomic organization of the mouse and human genes for vascular
            endothelial growth factor B (VEGF-B) and characterization of a
            second splice isoform
  JOURNAL   J Biol Chem 271 (32), 19310-19317 (1996)
   PUBMED   8702615
REFERENCE   10 (residues 1 to 207)
  AUTHORS   Olofsson,B., Pajusola,K., Kaipainen,A., von Euler,G., Joukov,V.,
            Saksela,O., Orpana,A., Pettersson,R.F., Alitalo,K. and Eriksson,U.
  TITLE     Vascular endothelial growth factor B, a novel growth factor for
            endothelial cells
  JOURNAL   Proc Natl Acad Sci U S A 93 (6), 2576-2581 (1996)
   PUBMED   8637916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230972.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399492.715914.1,
                                           SRR21887623.1257569.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..207
                     /product="vascular endothelial growth factor B isoform 2
                     precursor"
                     /note="VRF; VEGF-B; VEGF-related factor"
                     /calculated_mol_wt=19564
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35485.3)"
                     /calculated_mol_wt=2324
     mat_peptide     22..207
                     /product="Vascular endothelial growth factor B.
                     /id=PRO_0000045174"
                     /note="propagated from UniProtKB/Swiss-Prot (O35485.3)"
                     /calculated_mol_wt=19564
     Region          45..126
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(45..48,82,84..87,102..105)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(47,78,82,89,122,124)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(72,81)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Region          140..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35485.3)"
     CDS             1..207
                     /gene="Vegfb"
                     /coded_by="NM_001438359.1:303..926"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:89811"
                     /db_xref="RGD:619799"
ORIGIN      
        1 mspllrrlll vallqlactq apvsqfdgps hqkkvvswid vyaratcqpr evvvplsmel
       61 mgnvvkqlvp scvtvqrcgg ccpddglecv pigqhqvrmq ilmiqypssq lgemsleehs
      121 qcecrpkrke savkpdrvai phhrpqprsv lswdsapgas spadiihptp apgpsahaap
      181 savsalipgp avaaadaaas siakgga
//
LOCUS       NP_001425334             220 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001425334
VERSION     NP_001425334.1
DBSOURCE    REFSEQ: accession NM_001438405.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 220)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 220)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF279911.1, SRR22399481.1966315.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..220
                     /product="bcl2-associated agonist of cell death isoform 3"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=24147
     Region          1..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Region          43..>165
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            132
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            134
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA, PKB, PAK1, RPS6KA1, RPS6KB1
                     and PKC/PRKCQ. /evidence=ECO:0000250|UniProtKB:Q61337;
                     propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Region          148..162
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     CDS             1..220
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438405.1:419..1081"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 mgtpkqpsla pahalglrks dpgirslgsd aggrrwrpaa qsmfqipefe pseqedastt
       61 drglgpslte dqpgpylapg llgsivqqqp gqaannshhg gagtmetrsr hssypagtee
      121 degmeeelsp frgrsrsapp nlwaaqrygr elrrmsdefe gsfkgeelty sveflpvrai
      181 amegwpllws fqsfphtlpp tppevamfpl rywtalrrlc
//
LOCUS       NP_001425367             487 aa            linear   ROD 18-APR-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Rattus norvegicus].
ACCESSION   NP_001425367 XP_063122088
VERSION     NP_001425367.1
DBSOURCE    REFSEQ: accession NM_001438438.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Shigeta,Y., Kanai,Y., Chairoungdua,A., Ahmed,N., Sakamoto,S.,
            Matsuo,H., Kim,D.K., Fujimura,M., Anzai,N., Mizoguchi,K., Ueda,T.,
            Akakura,K., Ichikawa,T., Ito,H. and Endou,H.
  TITLE     A novel missense mutation of SLC7A9 frequent in Japanese cystinuria
            cases affecting the C-terminus of the transporter
  JOURNAL   Kidney Int 69 (7), 1198-1206 (2006)
   PUBMED   16609684
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Kwak,J.O., Kim,H.W., Jung,S.M., Song,J.H., Hong,S.B., Oh,K.J.,
            Ko,C.B. and Cha,S.H.
  TITLE     Co-localization and interaction of b0,+-type amino acid transporter
            1 (BAT1) with caveolin-1 in rat kidney
  JOURNAL   J Nephrol 18 (6), 681-689 (2005)
   PUBMED   16358225
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Fernandez,E., Carrascal,M., Rousaud,F., Abian,J., Zorzano,A.,
            Palacin,M. and Chillaron,J.
  TITLE     rBAT-b(0,+)AT heterodimer is the main apical reabsorption system
            for cystine in the kidney
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F540-F548 (2002)
   PUBMED   12167606
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Chairoungdua,A., Segawa,H., Kim,J.Y., Miyamoto,K., Haga,H.,
            Fukui,Y., Mizoguchi,K., Ito,H., Takeda,E., Endou,H. and Kanai,Y.
  TITLE     Identification of an amino acid transporter associated with the
            cystinuria-related type II membrane glycoprotein
  JOURNAL   J Biol Chem 274 (41), 28845-28848 (1999)
   PUBMED   10506124
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_063122088.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.1022.1,
                                           SRR26643288.2115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="b(0,+)AT; solute carrier family 7 (amino acid
                     transporter light chain, bo,+ system), member 9;
                     glycoprotein-associated amino acid transporter b0,+AT1;
                     solute carrier family 7 (cationic amino acid transporter,
                     y+ system), member 9; solute carrier family 7
                     (glycoprotein-associated amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53527
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Region          13..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P82252.1)"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     CDS             1..487
                     /gene="Slc7a9"
                     /coded_by="NM_001438438.1:512..1975"
                     /db_xref="GeneID:116726"
                     /db_xref="RGD:619905"
ORIGIN      
        1 meetsprrrr edeksvhste pkttslqkev gllsgiciiv gtiigsgifi spksvlante
       61 svgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meafgpipay lfswtslivm
      121 kpssfaiicl sfseyvcaaf ylgcrppavv vkllaaaail littvnalsv rlgsyvqnvf
      181 taaklvivai iiisglvlla qgnvknfqns fegsqtsvgs islafynglw aydgwnqlny
      241 iteelrnpyr nlpmaivigi plvtvcyilm niayftvmtp tellqsqava vtfgdrvlyp
      301 aswvvplfva fstigaangt cftagrliyv agreghmlkv lsyisvkrlt papalvfygi
      361 iaiiyiipgd inslvnyfsf aawlfygmti lglvvmrftr kdlerpikvp ifipiivilv
      421 svflilapii sspaweylyc vlfilsglif yflfvhykfr waqkisrpit khlqmlmevv
      481 ppekdpe
//
LOCUS       NP_001425292             471 aa            linear   ROD 18-APR-2025
DEFINITION  7-dehydrocholesterol reductase [Rattus norvegicus].
ACCESSION   NP_001425292 XP_006230956
VERSION     NP_001425292.1
DBSOURCE    REFSEQ: accession NM_001438363.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Sun,L., Lu,J., Yao,D., Li,X., Cao,Y., Gao,J., Liu,J., Zheng,T.,
            Wang,H. and Zhan,X.
  TITLE     Effect of DHCR7 for the co-occurrence of hypercholesterolemia and
            vitamin D deficiency in type 2 diabetes: Perspective of health
            prevention
  JOURNAL   Prev Med 173, 107576 (2023)
   PUBMED   37329988
  REMARK    GeneRIF: Effect of DHCR7 for the co-occurrence of
            hypercholesterolemia and vitamin D deficiency in type 2 diabetes:
            Perspective of health prevention.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kwak,S.Y., Cho,Y., Oh,H. and Shin,M.J.
  TITLE     Association of circulating 25-hydroxyvitamin D levels with
            hypertension and blood pressure values in Korean adults: A
            Mendelian randomization study on a subset of the Korea National
            Health and Nutrition Survey 2011-2012 population
  JOURNAL   Nutr Res Pract 13 (6), 498-508 (2019)
   PUBMED   31814925
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Fang,J., Hou,S., Xiang,Q., Qi,J., Yu,H., Shi,Y., Zhou,Y.,
            Kijlstra,A. and Yang,P.
  TITLE     Polymorphisms in genetics of vitamin D metabolism confer
            susceptibility to ocular Behcet disease in a Chinese Han population
  JOURNAL   Am J Ophthalmol 157 (2), 488-494 (2014)
   PUBMED   24184224
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bae,S.H., Lee,J.N., Fitzky,B.U., Seong,J. and Paik,Y.K.
  TITLE     Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
            distribution, expression, chromosomal localization, and regulation
            of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz
            syndrome-related protein
  JOURNAL   J Biol Chem 274 (21), 14624-14631 (1999)
   PUBMED   10329655
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Holmer,L., Pezhman,A. and Worman,H.J.
  TITLE     The human lamin B receptor/sterol reductase multigene family
  JOURNAL   Genomics 54 (3), 469-476 (1998)
   PUBMED   9878250
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Shefer,S., Salen,G., Honda,A., Batta,A.K., Nguyen,L.B., Tint,G.S.,
            Ioannou,Y.A. and Desnick,R.
  TITLE     Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase:
            substrate specificity, competitive and non-competitive inhibition,
            and phosphorylation/dephosphorylation
  JOURNAL   J Lipid Res 39 (12), 2471-2476 (1998)
   PUBMED   9831636
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Waterham,H.R., Wijburg,F.A., Hennekam,R.C., Vreken,P.,
            Poll-The,B.T., Dorland,L., Duran,M., Jira,P.E., Smeitink,J.A.,
            Wevers,R.A. and Wanders,R.J.
  TITLE     Smith-Lemli-Opitz syndrome is caused by mutations in the
            7-dehydrocholesterol reductase gene
  JOURNAL   Am J Hum Genet 63 (2), 329-338 (1998)
   PUBMED   9683613
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Moebius,F.F., Fitzky,B.U., Lee,J.N., Paik,Y.K. and Glossmann,H.
  TITLE     Molecular cloning and expression of the human delta7-sterol
            reductase
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1899-1902 (1998)
   PUBMED   9465114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230956.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.285090.1,
                                           SRR22399481.2497938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..471
                     /product="7-dehydrocholesterol reductase"
                     /EC_number="1.3.1.21"
                     /EC_number="3.3.2.11"
                     /note="7-DHC reductase; sterol Delta(7)-reductase;
                     cholesterol-5,6-epoxide hydrolase subunit DHCR7"
                     /calculated_mol_wt=54024
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Region          89..471
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     CDS             1..471
                     /gene="Dhcr7"
                     /coded_by="NM_001438363.1:83..1498"
                     /db_xref="GeneID:64191"
                     /db_xref="RGD:621769"
ORIGIN      
        1 masksqhnas kaknhnvkae sqgqwgrawe vdwfslvsvi flllfapfiv yyfimacdqy
       61 scsltapild vatgraslad iwaktppvta kaaqlyalwv sfqvllyswl pdfchrflpg
      121 yvggvqegai tpagivnkye vnglqawlit hflwfvnayl lswfsptiif dnwipllwca
      181 nilgyavstf amikgylfpt saedckftgn ffynymmgie fnprigkwfd fklffngrpg
      241 ivawtlinls faakqqelyg hvtnsmilvn vlqaiyvldf fwnetwylkt idichdhfgw
      301 ylgwgdcvwl pylytlqgly lvyhpvqlst pnalgvlllg lvgyyifrmt nhqkdlfrrt
      361 dghcliwgkk pkaiecsyts adglkhrskl lvsgfwgvar hfnytgdlmg slayclacgg
      421 ghllpyfyii ymtillthrc lrdehrcank ygrdweryva avpyrllpgi f
//
LOCUS       NP_001099695             450 aa            linear   ROD 18-APR-2025
DEFINITION  protein tweety homolog 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099695 XP_001070417 XP_218263
VERSION     NP_001099695.1
DBSOURCE    REFSEQ: accession NM_001106225.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kumada,T., Yamanaka,Y., Kitano,A., Shibata,M., Awaya,T., Kato,T.,
            Okawa,K., Abe,T., Oshima,N., Nakahata,T. and Heike,T.
  TITLE     Ttyh1, a Ca(2+)-binding protein localized to the endoplasmic
            reticulum, is required for early embryonic development
  JOURNAL   Dev Dyn 239 (8), 2233-2245 (2010)
   PUBMED   20568244
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yoon,J.C., Ng,A., Kim,B.H., Bianco,A., Xavier,R.J. and Elledge,S.J.
  TITLE     Wnt signaling regulates mitochondrial physiology and insulin
            sensitivity
  JOURNAL   Genes Dev 24 (14), 1507-1518 (2010)
   PUBMED   20634317
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Matthews,C.A., Shaw,J.E., Hooper,J.A., Young,I.G., Crouch,M.F. and
            Campbell,H.D.
  TITLE     Expression and evolution of the mammalian brain gene Ttyh1
  JOURNAL   J Neurochem 100 (3), 693-707 (2007)
   PUBMED   17116230
  REMARK    GeneRIF: These data suggest a role for Ttyh1 in process formation,
            cell adhesion and possibly as a transmembrane receptor.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Collins,M.O., Husi,H., Yu,L., Brandon,J.M., Anderson,C.N.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Molecular characterization and comparison of the components and
            multiprotein complexes in the postsynaptic proteome
  JOURNAL   J Neurochem 97 Suppl 1, 16-23 (2006)
   PUBMED   16635246
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Suzuki,M.
  TITLE     The Drosophila tweety family: molecular candidates for
            large-conductance Ca2+-activated Cl- channels
  JOURNAL   Exp Physiol 91 (1), 141-147 (2006)
   PUBMED   16219661
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001070417.1, XP_218263.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.1406.1,
                                           SRR26360176.2396593.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760434 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..450
                     /product="protein tweety homolog 1 isoform 1"
                     /note="protein tweety homolog 1; volume-regulated anion
                     channel subunit Ttyh1"
                     /calculated_mol_wt=48901
     Region          9..441
                     /region_name="Tweety"
                     /note="pfam04906"
                     /db_xref="CDD:461475"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            165
                     /site_type="other"
                     /note="Essential for the formation of the channel-pore.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            355
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            order(371,374)
                     /site_type="active"
                     /note="putative pore region [active]"
                     /db_xref="CDD:143653"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Region          428..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     CDS             1..450
                     /gene="Ttyh1"
                     /coded_by="NM_001106225.2:77..1429"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:292597"
                     /db_xref="RGD:1310103"
ORIGIN      
        1 mgappgyrps awvhllhqlp radfqlrpvp sgfaprdqey qqalllvaal aglglglsli
       61 fiavylirfc ccrppeppga kspppgggcv twsciaallv gcagigigfy gnsetsdgvs
      121 qlssalqhan htlstiddlv letverlgea vrtelttlee vlservelva atrgarrqae
      181 aaaqhlqgla fwqgvslspv qvaedvtfve eyrwlayvll lllvllvclf tllglakqsk
      241 wlvvvmtams llvlvlswgs mgleaatavg lsdfcsnpdt yvlnltqeet gissdilnyy
      301 flcnqavsnp fqqrltlsqr alasihsqlq glereaspqf paaqkpllsl eetlnvters
      361 fhqlvallhc rslhkdygsa lrglcedale gllflmlfsl lsagalattl cslprawalf
      421 ppsddyddtd dddpfnpqes krfvqwqssi
//
LOCUS       NP_001425311             170 aa            linear   ROD 18-APR-2025
DEFINITION  putative coiled-coil domain-containing protein 196 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001425311 XP_063118382
VERSION     NP_001425311.1
DBSOURCE    REFSEQ: accession NM_001438382.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Apr 18, 2025 this sequence version replaced XP_063118382.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2110128.1,
                                           SRR26360181.464807.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..170
                     /product="putative coiled-coil domain-containing protein
                     196 isoform 3"
                     /note="putative coiled-coil domain-containing protein 196"
                     /calculated_mol_wt=19200
     CDS             1..170
                     /gene="Ccdc196"
                     /gene_synonym="RGD1562540"
                     /coded_by="NM_001438382.1:149..661"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:500678"
                     /db_xref="RGD:1562540"
ORIGIN      
        1 mtsgsnsses glsskrnpkt ydnylkelne dlklrkqell emlkpledkn nlllqklman
       61 leekqrslqi mrqimagrgg dessveelik eaqemkqnlt feseelrgqq kalpkkskad
      121 mqdgkaqkss lslwkvkses ekpdidkvgd irkiflpsgk ateenkmgqi
//
LOCUS       NP_001425310             171 aa            linear   ROD 18-APR-2025
DEFINITION  putative coiled-coil domain-containing protein 196 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001425310 XP_063118381
VERSION     NP_001425310.1
DBSOURCE    REFSEQ: accession NM_001438381.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Apr 18, 2025 this sequence version replaced XP_063118381.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.35860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..171
                     /product="putative coiled-coil domain-containing protein
                     196 isoform 2"
                     /note="putative coiled-coil domain-containing protein 196"
                     /calculated_mol_wt=19328
     CDS             1..171
                     /gene="Ccdc196"
                     /gene_synonym="RGD1562540"
                     /coded_by="NM_001438381.1:264..779"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:500678"
                     /db_xref="RGD:1562540"
ORIGIN      
        1 mtsgsnsses glsskrnpkt ydnylkelne dlklrkqell emlkpledkn nlllqklman
       61 leekqrslqi mrqimagrgg dessveelik eaqemkqnlt feseelrgqq kalpkkskad
      121 mqdgkaqkss lslwkvkses ekpdidkvgd irkkiflpsg kateenkmgq i
//
LOCUS       NP_001425309             171 aa            linear   ROD 18-APR-2025
DEFINITION  putative coiled-coil domain-containing protein 196 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001425309 XP_038968655
VERSION     NP_001425309.1
DBSOURCE    REFSEQ: accession NM_001438380.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Apr 18, 2025 this sequence version replaced XP_038968655.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.860785.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..171
                     /product="putative coiled-coil domain-containing protein
                     196 isoform 2"
                     /note="putative coiled-coil domain-containing protein 196"
                     /calculated_mol_wt=19328
     CDS             1..171
                     /gene="Ccdc196"
                     /gene_synonym="RGD1562540"
                     /coded_by="NM_001438380.1:307..822"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:500678"
                     /db_xref="RGD:1562540"
ORIGIN      
        1 mtsgsnsses glsskrnpkt ydnylkelne dlklrkqell emlkpledkn nlllqklman
       61 leekqrslqi mrqimagrgg dessveelik eaqemkqnlt feseelrgqq kalpkkskad
      121 mqdgkaqkss lslwkvkses ekpdidkvgd irkkiflpsg kateenkmgq i
//
LOCUS       NP_001102210             575 aa            linear   ROD 18-APR-2025
DEFINITION  cytoskeleton-associated protein 4 [Rattus norvegicus].
ACCESSION   NP_001102210 XP_001079545 XP_343190
VERSION     NP_001102210.2
DBSOURCE    REFSEQ: accession NM_001108740.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Zhang,C., Kho,Y.S., Wang,Z., Chiang,Y.T., Ng,G.K., Shaw,P.C.,
            Wang,Y. and Qi,R.Z.
  TITLE     Transmembrane and coiled-coil domain family 1 is a novel protein of
            the endoplasmic reticulum
  JOURNAL   PLoS One 9 (1), e85206 (2014)
   PUBMED   24454821
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Kazi,A.S., Tao,J.Q., Feinstein,S.I., Zhang,L., Fisher,A.B. and
            Bates,S.R.
  TITLE     Role of the PI3-kinase signaling pathway in trafficking of the
            surfactant protein A receptor P63 (CKAP4) on type II pneumocytes
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 299 (6), L794-L807 (2010)
   PUBMED   20870746
  REMARK    GeneRIF: Data demonstrate an important role for the PI3-kinase-Akt
            pathway in intracellular transport of surfactant protein A receptor
            P63.
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Iinuma,T., Aoki,T., Arasaki,K., Hirose,H., Yamamoto,A., Samata,R.,
            Hauri,H.P., Arimitsu,N., Tagaya,M. and Tani,K.
  TITLE     Role of syntaxin 18 in the organization of endoplasmic reticulum
            subdomains
  JOURNAL   J Cell Sci 122 (Pt 10), 1680-1690 (2009)
   PUBMED   19401338
REFERENCE   8  (residues 1 to 575)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 575)
  AUTHORS   Nichols,R.J. and Traktman,P.
  TITLE     Characterization of three paralogous members of the Mammalian
            vaccinia related kinase family
  JOURNAL   J Biol Chem 279 (9), 7934-7946 (2004)
   PUBMED   14645249
REFERENCE   10 (residues 1 to 575)
  AUTHORS   Fujimoto,Y., Itabe,H., Sakai,J., Makita,M., Noda,J., Mori,M.,
            Higashi,Y., Kojima,S. and Takano,T.
  TITLE     Identification of major proteins in the lipid droplet-enriched
            fraction isolated from the human hepatocyte cell line HuH7
  JOURNAL   Biochim Biophys Acta 1644 (1), 47-59 (2004)
   PUBMED   14741744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 18, 2025 this sequence version replaced NP_001102210.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.726787.1,
                                           SRR26643297.24627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..575
                     /product="cytoskeleton-associated protein 4"
                     /calculated_mol_wt=63416
     Region          109..>479
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     CDS             1..575
                     /gene="Ckap4"
                     /coded_by="NM_001108740.2:179..1906"
                     /db_xref="GeneID:362859"
                     /db_xref="RGD:1311989"
ORIGIN      
        1 mpsakqrgsk gghgaaspsd kgahpsggad dvakkpppap qqpqppaphp pqhpqnqahr
       61 gghrgrssta aaaassascs rrlgrllnfl fylslvaaaa fsgwyvhhvl eevqqvrrgh
      121 qdfsrqrdel gqglqgveqk vqslqaavgt fesilrssqh kqdltekavk egeseinris
      181 evlqklqnei lkdlsdgihv vkdarerdft slentveerl teltksindn iaiftdvqkr
      241 sqkeinevkm kvasleeskg drsqdvkvlk eavkevqasm ksrerdieal ksslqtmesd
      301 vytevrelvs lkqeqqafkq aadserlalq altekllqse esssrlpedi rrleeelqql
      361 kvgahgseea vvfrdskafd elqkqmeglg arlqyvedgv ysmqvasash teslesllsk
      421 sqeyeqrlam lqehveslgp isdlastvrs leetqlalss dlkglkqglg elpgtveslq
      481 eqvhlllsqd paqaaglppq dfldrlssld nlkssvsqve sdlkmlrtav dslvaysvki
      541 etnenslesa kgllddlrnd ldrlfvkvek iheki
//
LOCUS       NP_073189                205 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_073189
VERSION     NP_073189.1
DBSOURCE    REFSEQ: accession NM_022698.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.6867.1,
                                           SRR26643297.4443.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..205
                     /product="bcl2-associated agonist of cell death isoform 4"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=22097
     Region          1..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Region          43..205
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            132
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            134
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA, PKB, PAK1, RPS6KA1, RPS6KB1
                     and PKC/PRKCQ. /evidence=ECO:0000250|UniProtKB:Q61337;
                     propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Region          148..162
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     Region          161..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35147.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92934; propagated from
                     UniProtKB/Swiss-Prot (O35147.2)"
     CDS             1..205
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_022698.3:419..1036"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 mgtpkqpsla pahalglrks dpgirslgsd aggrrwrpaa qsmfqipefe pseqedastt
       61 drglgpslte dqpgpylapg llgsivqqqp gqaannshhg gagtmetrsr hssypagtee
      121 degmeeelsp frgrsrsapp nlwaaqrygr elrrmsdefe gsfkglprpk sagtatqmrq
      181 saswtriiqs wwdrnlgkgg stpsq
//
LOCUS       NP_001425336             135 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001425336 XP_063128854
VERSION     NP_001425336.1
DBSOURCE    REFSEQ: accession NM_001438407.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_063128854.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.852746.1,
                                           SRR22582416.1093629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..135
                     /product="bcl2-associated agonist of cell death isoform 6"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=14101
     Region          73..>134
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..135
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438407.1:126..533"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 margvvpkag giqaqkgwrt yqpkqasriq mgtpkqpsla pahalglrks dpgirslgsd
       61 aggrrwrpaa qsmfqipefe pseqedastt drglgpslte dqpgpylapg llgsivqqqp
      121 gqaannshhg dgagr
//
LOCUS       NP_001425358             862 aa            linear   ROD 18-APR-2025
DEFINITION  AP-2 complex subunit alpha-2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425358
VERSION     NP_001425358.1
DBSOURCE    REFSEQ: accession NM_001438429.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Capella,P., Asensio,J., Troncoso,M., Sosa,M.A. and Seltzer,A.M.
  TITLE     Evidence on differential role for alpha 1 and alpha 2 subtypes of
            AP-2 adaptin in the central nervous system
  JOURNAL   Neurosci Lett 808, 137282 (2023)
   PUBMED   37127089
  REMARK    GeneRIF: Evidence on differential role for alpha 1 and alpha 2
            subtypes of AP-2 adaptin in the central nervous system.
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Marcello,E., Saraceno,C., Musardo,S., Vara,H., de la Fuente,A.G.,
            Pelucchi,S., Di Marino,D., Borroni,B., Tramontano,A.,
            Perez-Otano,I., Padovani,A., Giustetto,M., Gardoni,F. and Di
            Luca,M.
  TITLE     Endocytosis of synaptic ADAM10 in neuronal plasticity and
            Alzheimer's disease
  JOURNAL   J Clin Invest 123 (6), 2523-2538 (2013)
   PUBMED   23676497
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Duncker,S.V., Franz,C., Kuhn,S., Schulte,U., Campanelli,D.,
            Brandt,N., Hirt,B., Fakler,B., Blin,N., Ruth,P., Engel,J.,
            Marcotti,W., Zimmermann,U. and Knipper,M.
  TITLE     Otoferlin couples to clathrin-mediated endocytosis in mature
            cochlear inner hair cells
  JOURNAL   J Neurosci 33 (22), 9508-9519 (2013)
   PUBMED   23719817
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Takei,K., Mundigl,O., Daniell,L. and De Camilli,P.
  TITLE     The synaptic vesicle cycle: a single vesicle budding step involving
            clathrin and dynamin
  JOURNAL   J Cell Biol 133 (6), 1237-1250 (1996)
   PUBMED   8682861
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Voglmaier,S.M., Keen,J.H., Murphy,J.E., Ferris,C.D.,
            Prestwich,G.D., Snyder,S.H. and Theibert,A.B.
  TITLE     Inositol hexakisphosphate receptor identified as the clathrin
            assembly protein AP-2
  JOURNAL   Biochem Biophys Res Commun 187 (1), 158-163 (1992)
   PUBMED   1325787
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Bahler,M., Klein,R.L., Wang,J.K., Benfenati,F. and Greengard,P.
  TITLE     A novel synaptic vesicle-associated phosphoprotein: SVAPP-120
  JOURNAL   J Neurochem 57 (2), 423-430 (1991)
   PUBMED   2072093
  REMARK    Erratum:[J Neurochem 1991 Dec;57(6):2155]
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Tucker,K.L., Nathanson,K. and Kirchhausen,T.
  TITLE     Sequence of the rat alpha c large chain of the clathrin associated
            protein complex AP-2
  JOURNAL   Nucleic Acids Res 18 (17), 5306 (1990)
   PUBMED   2402467
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Kirchhausen,T., Nathanson,K.L., Matsui,W., Vaisberg,A., Chow,E.P.,
            Burne,C., Keen,J.H. and Davis,A.E.
  TITLE     Structural and functional division into two domains of the large
            (100- to 115-kDa) chains of the clathrin-associated protein complex
            AP-2
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2612-2616 (1989)
   PUBMED   2495531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1892473.1,
                                           SRR26643284.1607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..862
                     /product="AP-2 complex subunit alpha-2 isoform 3"
                     /note="adaptor protein complex AP-2, alpha 2 subunit; AP-2
                     complex subunit alpha-2; alpha2-adaptin; alpha-adaptin C;
                     100 kDa coated vesicle protein C; adaptor protein complex
                     AP-2 subunit alpha-2; adaptor-related protein complex 2,
                     alpha 2 subunit; adapter-related protein complex 2 alpha-2
                     subunit; clathrin assembly protein complex 2 alpha-C large
                     chain; plasma membrane adaptor HA2/AP2 adaptin alpha C
                     subunit; adapter-related protein complex 2 subunit
                     alpha-2"
                     /calculated_mol_wt=95343
     Region          1..514
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          255..278
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          292..321
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          331..357
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          640..743
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          749..857
                     /region_name="Alpha_adaptin_C"
                     /note="Alpha adaptin AP2, C-terminal domain; pfam02296"
                     /db_xref="CDD:426707"
     CDS             1..862
                     /gene="Ap2a2"
                     /coded_by="NM_001438429.1:555..3143"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:81637"
                     /db_xref="RGD:71015"
ORIGIN      
        1 meavnllssn rytekqigyl fisvlvnsns elirlinnai kndlasrnpt fmglalhcia
       61 nvgsremaea fageipkilv agdtmdsvkq saalcllrly rtspdlvpmg dwtsrvvhll
      121 ndqhlgvvta atslittlaq knpeefktsv slavsrlsri vtsastdlqd ytyyfvpapw
      181 lsvkllrllq cypppdpavr grltecleti lnkaqeppks kkvqhsnakn avlfeaisli
      241 ihhdsepnll vracnqlgqf lqhretnlry lalesmctla ssefsheavk thietvinal
      301 kterdvsvrq ravdllyamc drsnaqqiva emlsyletad ysireeivlk vailaekyav
      361 dytwyvdtil nliriagdyv seevwyrviq ivinrddvqg yaaktvfeal qapachenlv
      421 kvggyilgef gnliagdprs spliqfnllh skfhlcsvpt ralllstyik fvnlfpevka
      481 tiqdvlrsds qlknadvelq qraveylrls tvastdilat vleemppfpe ressilaklk
      541 kkkgpstvtd leetkrersi dvnggpepvp astsaastps psadllglga vppaptgppp
      601 tsgggllvdv fsdsasavap lapgsednfa rfvcknngvl fenqllqigl ksefrqnlgr
      661 mfifygnkts tqflnftptl icaddlqtnl nlqtkpvdpt vdggaqvqqv vniecisdft
      721 eapvlniqfr yggtfqnvsv klpitlnkff qptemasqdf fqrwkqlsnp qqevqnifka
      781 khpmdteitk akiigfgsal leevdpnpan fvgagiihtk ttqigcllrl epnlqaqmyr
      841 ltlrtskdtv sqrlcellse qf
//
LOCUS       NP_446001                186 aa            linear   ROD 18-APR-2025
DEFINITION  vascular endothelial growth factor B isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_446001 XP_342007
VERSION     NP_446001.1
DBSOURCE    REFSEQ: accession NM_053549.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Tu,S., Wang,X.Y., Zeng,L.X., Shen,Z.J. and Zhang,Z.H.
  TITLE     LncRNA TINCR improves cardiac hypertrophy by regulating the
            miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway
  JOURNAL   Lab Invest 102 (3), 253-262 (2022)
   PUBMED   34732848
  REMARK    GeneRIF: LncRNA TINCR improves cardiac hypertrophy by regulating
            the miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway.
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Shang,R., Lal,N., Lee,C.S., Zhai,Y., Puri,K., Seira,O.,
            Boushel,R.C., Sultan,I., Rasanen,M., Alitalo,K., Hussein,B. and
            Rodrigues,B.
  TITLE     Cardiac-specific VEGFB overexpression reduces lipoprotein lipase
            activity and improves insulin action in rat heart
  JOURNAL   Am J Physiol Endocrinol Metab 321 (6), E753-E765 (2021)
   PUBMED   34747201
  REMARK    GeneRIF: Cardiac-specific VEGFB overexpression reduces lipoprotein
            lipase activity and improves insulin action in rat heart.
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Lal,N., Chiu,A.P., Wang,F., Zhang,D., Jia,J., Wan,A., Vlodavsky,I.,
            Hussein,B. and Rodrigues,B.
  TITLE     Loss of VEGFB and its signaling in the diabetic heart is associated
            with increased cell death signaling
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (6), H1163-H1175 (2017)
   PUBMED   28314760
  REMARK    GeneRIF: Loss of VEGFB and its downstream signaling is an early
            event following hyperglycemia, is sustained with disease
            progression, and could explain diabetic cardiomyopathy.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Monastero,R., Garcia-Serrano,S., Lago-Sampedro,A.,
            Rodriguez-Pacheco,F., Colomo,N., Morcillo,S., Martin-Nunez,G.M.,
            Gomez-Zumaquero,J.M., Garcia-Fuentes,E., Soriguer,F.,
            Rojo-Martinez,G. and Garcia-Escobar,E.
  TITLE     Methylation patterns of Vegfb promoter are associated with gene and
            protein expression levels: the effects of dietary fatty acids
  JOURNAL   Eur J Nutr 56 (2), 715-726 (2017)
   PUBMED   26707994
  REMARK    GeneRIF: Data suggest that dietary fatty acids create
            epigenetic/nutrigenomic changes in methylation levels of CpG island
            at Vegfb promoter and changes in Vegfb expression in white
            adipocytes in vivo and in vitro, with particular up-regulation of
            DNA methylation by linoleic acid; Vegfb promoter methylation levels
            are closely related to Vegfb gene expression in visceral and
            subcutaneous adipose tissue.
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Nag,S., Eskandarian,M.R., Davis,J. and Eubanks,J.H.
  TITLE     Differential expression of vascular endothelial growth factor-A
            (VEGF-A) and VEGF-B after brain injury
  JOURNAL   J Neuropathol Exp Neurol 61 (9), 778-788 (2002)
   PUBMED   12230324
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Ikuta,T., Ariga,H. and Matsumoto,K.
  TITLE     Extracellular matrix tenascin-X in combination with vascular
            endothelial growth factor B enhances endothelial cell proliferation
  JOURNAL   Genes Cells 5 (11), 913-927 (2000)
   PUBMED   11122379
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Bellomo,D., Headrick,J.P., Silins,G.U., Paterson,C.A., Thomas,P.S.,
            Gartside,M., Mould,A., Cahill,M.M., Tonks,I.D., Grimmond,S.M.,
            Townson,S., Wells,C., Little,M., Cummings,M.C., Hayward,N.K. and
            Kay,G.F.
  TITLE     Mice lacking the vascular endothelial growth factor-B gene (Vegfb)
            have smaller hearts, dysfunctional coronary vasculature, and
            impaired recovery from cardiac ischemia
  JOURNAL   Circ Res 86 (2), E29-E35 (2000)
   PUBMED   10666423
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Olofsson,B., Pajusola,K., von Euler,G., Chilov,D., Alitalo,K. and
            Eriksson,U.
  TITLE     Genomic organization of the mouse and human genes for vascular
            endothelial growth factor B (VEGF-B) and characterization of a
            second splice isoform
  JOURNAL   J Biol Chem 271 (32), 19310-19317 (1996)
   PUBMED   8702615
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Olofsson,B., Pajusola,K., Kaipainen,A., von Euler,G., Joukov,V.,
            Saksela,O., Orpana,A., Pettersson,R.F., Alitalo,K. and Eriksson,U.
  TITLE     Vascular endothelial growth factor B, a novel growth factor for
            endothelial cells
  JOURNAL   Proc Natl Acad Sci U S A 93 (6), 2576-2581 (1996)
   PUBMED   8637916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Mar 26, 2005 this sequence version replaced XP_342007.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC076395.1, SRR21887622.4094863.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..186
                     /product="vascular endothelial growth factor B isoform 3
                     precursor"
                     /note="VRF; VEGF-B; VEGF-related factor"
                     /calculated_mol_wt=18995
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2125
     Region          45..126
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(45..48,82,84..87,102..105)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(47,78,82,89,122,124)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(72,81)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     CDS             1..186
                     /gene="Vegfb"
                     /coded_by="NM_053549.2:303..863"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:89811"
                     /db_xref="RGD:619799"
ORIGIN      
        1 mspllrrlll vallqlactq apvsqfdgps hqkkvvswid vyaratcqpr evvvplsmel
       61 mgnvvkqlvp scvtvqrcgg ccpddglecv pigqhqvrmq ilmiqypssq lgemsleehs
      121 qcecrpkrke savkpdsprt lcprctqrrq rpdprtcrcr crrrrflhcq grglelnpdt
      181 crsset
//
LOCUS       NP_001425342            1038 aa            linear   ROD 18-APR-2025
DEFINITION  myosin IH [Rattus norvegicus].
ACCESSION   NP_001425342
VERSION     NP_001425342.1
DBSOURCE    REFSEQ: accession NM_001438413.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000012.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..1038
                     /product="myosin IH"
                     /note="unconventional myosin-Ih; unconventional
                     myosin-Ih-like"
                     /calculated_mol_wt=119305
     Region          42..694
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(69..72,77,121..128,168..178,397..402)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(69..72,77)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            121..128
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            168..178
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            397..402
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(426..437,440..447,449)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Site            626..636
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(638..664,681..694)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          <690..>768
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          690..714
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          727..757
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          738..756
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     Region          850..1031
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1038
                     /gene="Myo1h"
                     /gene_synonym="AABR07036550.1"
                     /coded_by="NM_001438413.1:120..3236"
                     /db_xref="GeneID:687866"
                     /db_xref="RGD:1596237"
ORIGIN      
        1 mgskkeevrr khirlhmega ltardkvgvq dfvlldayts esaflenlrk rfrenliyty
       61 igtllvsvnp yqelgiytss qmelyqgvnf felpphvyai adnayrmmcs elnnhfilis
      121 gesgagktea skkilqylav tcpmteslqi ardrlllsip vleafgnakt lrndnssrfg
      181 kymdiqfdfq gvpvgghiis ylieksrvvy qnhgernfhi fyqllaggks erlaslgler
      241 dpqlykflsq ghcarespsn drsdwetvys afsvigftea dlenlfgiia svlhlgnicf
      301 kgdkqgcasi pdtheikwia kllgvcpavl lealthrkie akteevicpl tvelsvyard
      361 amakavygrt ftwlvnkins slvnkdftqk tviglldiyg fevfdkngfe qfcinycnek
      421 lqqlliertl kaeqaeyese giewepvqyf nnkiicdlve erhrgiisil deecirpgpa
      481 tdlsflekle ekvgkhahfq trklagpkgr krigwlefcl lhyagevtyc tkgfleknnd
      541 llyrhlkevl cssknsilre cflvaelenr krpptvgtqf knslssllei liskepsyir
      601 cikpnerkep skfddflish qikylglmeh lrvrragfay rrkyehflqr ykslcpdtwp
      661 hwhgppgegv erlikyigyq pqdyklgktk ifirfprtlf atedafefsk hqlvsriqat
      721 ykgclgrrey vrkrqaatkl eahwrgvlar keikrrkwav qiirrfikgf inrdkplcpd
      781 neeflllvrk nyilnlryhv pknvldkswl rppgilenas nllrrmctrn lvrkycrgis
      841 aerkammqqk avtsglfrgk kegyaeslsq pfassrldeg kinpkvlqll gsekiqygvp
      901 vikydrkgfk arqrqllltl rsaylvefsk ikqkmeysal rgvstsslrd gilvihvspa
      961 dkqqkgdtil qcehifevat klamlikreh vvrvvqgslq fcvspgregt ivfetgeedq
     1021 vykdkngqlr vvsagkkt
//
LOCUS       NP_116005                593 aa            linear   ROD 18-APR-2025
DEFINITION  lipolysis-stimulated lipoprotein receptor isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_116005
VERSION     NP_116005.1
DBSOURCE    REFSEQ: accession NM_032616.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Wang,J., Qin,M., Wu,Q., Yang,H., Wei,B., Xie,J., Qin,Y., Liang,Z.
            and Huang,J.
  TITLE     Effects of Lipolysis-Stimulated Lipoprotein Receptor on Tight
            Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis
  JOURNAL   Biomed Res Int 2022, 4234186 (2022)
   PUBMED   35463981
  REMARK    GeneRIF: Effects of Lipolysis-Stimulated Lipoprotein Receptor on
            Tight Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Sohet,F., Lin,C., Munji,R.N., Lee,S.Y., Ruderisch,N., Soung,A.,
            Arnold,T.D., Derugin,N., Vexler,Z.S., Yen,F.T. and Daneman,R.
  TITLE     LSR/angulin-1 is a tricellular tight junction protein involved in
            blood-brain barrier formation
  JOURNAL   J Cell Biol 208 (6), 703-711 (2015)
   PUBMED   25753034
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Nakatsu,D., Kano,F., Taguchi,Y., Sugawara,T., Nishizono,T.,
            Nishikawa,K., Oda,Y., Furuse,M. and Murata,M.
  TITLE     JNK1/2-dependent phosphorylation of angulin-1/LSR is required for
            the exclusive localization of angulin-1/LSR and tricellulin at
            tricellular contacts in EpH4 epithelial sheet
  JOURNAL   Genes Cells 19 (7), 565-581 (2014)
   PUBMED   24889144
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Furuse,M., Oda,Y., Higashi,T., Iwamoto,N. and Masuda,S.
  TITLE     Lipolysis-stimulated lipoprotein receptor: a novel membrane protein
            of tricellular tight junctions
  JOURNAL   Ann N Y Acad Sci 1257, 54-58 (2012)
   PUBMED   22671589
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Masuda,S., Oda,Y., Sasaki,H., Ikenouchi,J., Higashi,T., Akashi,M.,
            Nishi,E. and Furuse,M.
  TITLE     LSR defines cell corners for tricellular tight junction formation
            in epithelial cells
  JOURNAL   J Cell Sci 124 (Pt 4), 548-555 (2011)
   PUBMED   21245199
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Yagil,C., Hubner,N., Monti,J., Schulz,H., Sapojnikov,M., Luft,F.C.,
            Ganten,D. and Yagil,Y.
  TITLE     Identification of hypertension-related genes through an integrated
            genomic-transcriptomic approach
  JOURNAL   Circ Res 96 (6), 617-625 (2005)
   PUBMED   15731461
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Mesli,S., Javorschi,S., Berard,A.M., Landry,M., Priddle,H.,
            Kivlichan,D., Smith,A.J., Yen,F.T., Bihain,B.E. and Darmon,M.
  TITLE     Distribution of the lipolysis stimulated receptor in adult and
            embryonic murine tissues and lethality of LSR-/- embryos at 12.5 to
            14.5 days of gestation
  JOURNAL   Eur J Biochem 271 (15), 3103-3114 (2004)
   PUBMED   15265030
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Yen,F.T., Masson,M., Clossais-Besnard,N., Andre,P., Grosset,J.M.,
            Bougueleret,L., Dumas,J.B., Guerassimenko,O. and Bihain,B.E.
  TITLE     Molecular cloning of a lipolysis-stimulated remnant receptor
            expressed in the liver
  JOURNAL   J Biol Chem 274 (19), 13390-13398 (1999)
   PUBMED   10224102
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF119667.1, FO794106.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..593
                     /product="lipolysis-stimulated lipoprotein receptor
                     isoform 2 precursor"
                     /note="lipolysis-stimulated remnant receptor;
                     liver-specific bHLH-Zip transcription factor 7;
                     lipolysis-stimulated receptor"
                     /calculated_mol_wt=62334
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
                     /calculated_mol_wt=3461
     mat_peptide     36..593
                     /product="Lipolysis-stimulated lipoprotein receptor.
                     /id=PRO_0000245310"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU74.1)"
                     /calculated_mol_wt=62334
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Region          375..578
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86X29; propagated from
                     UniProtKB/Swiss-Prot (Q9WU74.1)"
     CDS             1..593
                     /gene="Lsr"
                     /gene_synonym="Lisch7"
                     /coded_by="NM_032616.3:202..1983"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:64355"
                     /db_xref="RGD:69236"
ORIGIN      
        1 mapaagacag apdshpatvv fvclfliifc pdpasaiqvt vsdpyhvvil fqpvtlpcty
       61 qmsntltvpi viwkyksfcr driadafspa svdnqlnaql aagnpgynpy vecqdsvrtv
      121 rvvatkqgna vtlgdyyqgr rititgnadl tfeqtawgds gvyycsvvsa qdldgnneay
      181 aelivlgrts eapellpgfr agpledwlfv vvvclaslll flllgicwcq ccphtcccyv
      241 rcpccpdkcc cpealyaagk aatsgvpsiy apsiythlsp aktpppppam ipmgppygyp
      301 gdfdrhssvg ghssqvpllr dvdgsvssev rsgyriqanq qddsmrvlyy mekelanfdp
      361 srpgppngrv eramsevtsl heddwrsrps rapaltpird eewnrhspqs prtweqeplq
      421 eqprggwgsg rprarsvdal ddinrpgste sgrssppssg rrgrayappr srsrddlydp
      481 ddprdlphsr dphyyddirs rdpradprsr qrsrdprdag frsrdpqydg rlleealkkk
      541 gsgerrrvyr eeeeeeegqy ppapppyset dsqasrerrl kknlalsres lvv
//
LOCUS       NP_001425301             525 aa            linear   ROD 18-APR-2025
DEFINITION  lipolysis-stimulated lipoprotein receptor isoform 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_001425301 XP_006228907
VERSION     NP_001425301.1
DBSOURCE    REFSEQ: accession NM_001438372.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Wang,J., Qin,M., Wu,Q., Yang,H., Wei,B., Xie,J., Qin,Y., Liang,Z.
            and Huang,J.
  TITLE     Effects of Lipolysis-Stimulated Lipoprotein Receptor on Tight
            Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis
  JOURNAL   Biomed Res Int 2022, 4234186 (2022)
   PUBMED   35463981
  REMARK    GeneRIF: Effects of Lipolysis-Stimulated Lipoprotein Receptor on
            Tight Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Sohet,F., Lin,C., Munji,R.N., Lee,S.Y., Ruderisch,N., Soung,A.,
            Arnold,T.D., Derugin,N., Vexler,Z.S., Yen,F.T. and Daneman,R.
  TITLE     LSR/angulin-1 is a tricellular tight junction protein involved in
            blood-brain barrier formation
  JOURNAL   J Cell Biol 208 (6), 703-711 (2015)
   PUBMED   25753034
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Nakatsu,D., Kano,F., Taguchi,Y., Sugawara,T., Nishizono,T.,
            Nishikawa,K., Oda,Y., Furuse,M. and Murata,M.
  TITLE     JNK1/2-dependent phosphorylation of angulin-1/LSR is required for
            the exclusive localization of angulin-1/LSR and tricellulin at
            tricellular contacts in EpH4 epithelial sheet
  JOURNAL   Genes Cells 19 (7), 565-581 (2014)
   PUBMED   24889144
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Furuse,M., Oda,Y., Higashi,T., Iwamoto,N. and Masuda,S.
  TITLE     Lipolysis-stimulated lipoprotein receptor: a novel membrane protein
            of tricellular tight junctions
  JOURNAL   Ann N Y Acad Sci 1257, 54-58 (2012)
   PUBMED   22671589
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Masuda,S., Oda,Y., Sasaki,H., Ikenouchi,J., Higashi,T., Akashi,M.,
            Nishi,E. and Furuse,M.
  TITLE     LSR defines cell corners for tricellular tight junction formation
            in epithelial cells
  JOURNAL   J Cell Sci 124 (Pt 4), 548-555 (2011)
   PUBMED   21245199
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Yagil,C., Hubner,N., Monti,J., Schulz,H., Sapojnikov,M., Luft,F.C.,
            Ganten,D. and Yagil,Y.
  TITLE     Identification of hypertension-related genes through an integrated
            genomic-transcriptomic approach
  JOURNAL   Circ Res 96 (6), 617-625 (2005)
   PUBMED   15731461
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Mesli,S., Javorschi,S., Berard,A.M., Landry,M., Priddle,H.,
            Kivlichan,D., Smith,A.J., Yen,F.T., Bihain,B.E. and Darmon,M.
  TITLE     Distribution of the lipolysis stimulated receptor in adult and
            embryonic murine tissues and lethality of LSR-/- embryos at 12.5 to
            14.5 days of gestation
  JOURNAL   Eur J Biochem 271 (15), 3103-3114 (2004)
   PUBMED   15265030
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Yen,F.T., Masson,M., Clossais-Besnard,N., Andre,P., Grosset,J.M.,
            Bougueleret,L., Dumas,J.B., Guerassimenko,O. and Bihain,B.E.
  TITLE     Molecular cloning of a lipolysis-stimulated remnant receptor
            expressed in the liver
  JOURNAL   J Biol Chem 274 (19), 13390-13398 (1999)
   PUBMED   10224102
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006228907.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF119669.1, SRR26643288.1966.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..525
                     /product="lipolysis-stimulated lipoprotein receptor
                     isoform 3 precursor"
                     /note="lipolysis-stimulated remnant receptor;
                     liver-specific bHLH-Zip transcription factor 7;
                     lipolysis-stimulated receptor"
                     /calculated_mol_wt=54797
     sig_peptide     1..36
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3532
     CDS             1..525
                     /gene="Lsr"
                     /gene_synonym="Lisch7"
                     /coded_by="NM_001438372.1:202..1779"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:64355"
                     /db_xref="RGD:69236"
ORIGIN      
        1 mapaagacag apdshpatvv fvclfliifc pdpasaiqvt vsdpyhvvil fqpvtlpcty
       61 qmsntltvpi viwkyksfcr driadafspa svdnqlnaql aagnpgynpy vecqdsvrtv
      121 rvvatkqgna vtlgdyyqgr rititgnadl tfeqtawgds gvyycsvvsa qdldgnneay
      181 aelivlvyaa gkaatsgvps iyapsiythl spaktppppp amipmgppyg ypgdfdrhss
      241 vgghssqvpl lrdvdgsvss evrsgyriqa nqqddsmrvl yymekelanf dpsrpgppng
      301 rveramsevt slheddwrsr psrapaltpi rdeewnrhsp qsprtweqep lqeqprggwg
      361 sgrprarsvd alddinrpgs tesgrsspps sgrrgrayap prsrsrddly dpddprdlph
      421 srdphyyddi rsrdpradpr srqrsrdprd agfrsrdpqy dgrlleealk kkgsgerrrv
      481 yreeeeeeeg qyppapppys etdsqasrer rlkknlalsr eslvv
//
LOCUS       NP_001425291             471 aa            linear   ROD 18-APR-2025
DEFINITION  7-dehydrocholesterol reductase [Rattus norvegicus].
ACCESSION   NP_001425291 XP_038945428
VERSION     NP_001425291.1
DBSOURCE    REFSEQ: accession NM_001438362.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Sun,L., Lu,J., Yao,D., Li,X., Cao,Y., Gao,J., Liu,J., Zheng,T.,
            Wang,H. and Zhan,X.
  TITLE     Effect of DHCR7 for the co-occurrence of hypercholesterolemia and
            vitamin D deficiency in type 2 diabetes: Perspective of health
            prevention
  JOURNAL   Prev Med 173, 107576 (2023)
   PUBMED   37329988
  REMARK    GeneRIF: Effect of DHCR7 for the co-occurrence of
            hypercholesterolemia and vitamin D deficiency in type 2 diabetes:
            Perspective of health prevention.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kwak,S.Y., Cho,Y., Oh,H. and Shin,M.J.
  TITLE     Association of circulating 25-hydroxyvitamin D levels with
            hypertension and blood pressure values in Korean adults: A
            Mendelian randomization study on a subset of the Korea National
            Health and Nutrition Survey 2011-2012 population
  JOURNAL   Nutr Res Pract 13 (6), 498-508 (2019)
   PUBMED   31814925
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Fang,J., Hou,S., Xiang,Q., Qi,J., Yu,H., Shi,Y., Zhou,Y.,
            Kijlstra,A. and Yang,P.
  TITLE     Polymorphisms in genetics of vitamin D metabolism confer
            susceptibility to ocular Behcet disease in a Chinese Han population
  JOURNAL   Am J Ophthalmol 157 (2), 488-494 (2014)
   PUBMED   24184224
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bae,S.H., Lee,J.N., Fitzky,B.U., Seong,J. and Paik,Y.K.
  TITLE     Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
            distribution, expression, chromosomal localization, and regulation
            of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz
            syndrome-related protein
  JOURNAL   J Biol Chem 274 (21), 14624-14631 (1999)
   PUBMED   10329655
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Holmer,L., Pezhman,A. and Worman,H.J.
  TITLE     The human lamin B receptor/sterol reductase multigene family
  JOURNAL   Genomics 54 (3), 469-476 (1998)
   PUBMED   9878250
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Shefer,S., Salen,G., Honda,A., Batta,A.K., Nguyen,L.B., Tint,G.S.,
            Ioannou,Y.A. and Desnick,R.
  TITLE     Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase:
            substrate specificity, competitive and non-competitive inhibition,
            and phosphorylation/dephosphorylation
  JOURNAL   J Lipid Res 39 (12), 2471-2476 (1998)
   PUBMED   9831636
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Waterham,H.R., Wijburg,F.A., Hennekam,R.C., Vreken,P.,
            Poll-The,B.T., Dorland,L., Duran,M., Jira,P.E., Smeitink,J.A.,
            Wevers,R.A. and Wanders,R.J.
  TITLE     Smith-Lemli-Opitz syndrome is caused by mutations in the
            7-dehydrocholesterol reductase gene
  JOURNAL   Am J Hum Genet 63 (2), 329-338 (1998)
   PUBMED   9683613
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Moebius,F.F., Fitzky,B.U., Lee,J.N., Paik,Y.K. and Glossmann,H.
  TITLE     Molecular cloning and expression of the human delta7-sterol
            reductase
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1899-1902 (1998)
   PUBMED   9465114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_038945428.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.4228.1,
                                           SRR26360186.345187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680426, SAMN12840132
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..471
                     /product="7-dehydrocholesterol reductase"
                     /EC_number="1.3.1.21"
                     /EC_number="3.3.2.11"
                     /note="7-DHC reductase; sterol Delta(7)-reductase;
                     cholesterol-5,6-epoxide hydrolase subunit DHCR7"
                     /calculated_mol_wt=54024
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Region          89..471
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     CDS             1..471
                     /gene="Dhcr7"
                     /coded_by="NM_001438362.1:191..1606"
                     /db_xref="GeneID:64191"
                     /db_xref="RGD:621769"
ORIGIN      
        1 masksqhnas kaknhnvkae sqgqwgrawe vdwfslvsvi flllfapfiv yyfimacdqy
       61 scsltapild vatgraslad iwaktppvta kaaqlyalwv sfqvllyswl pdfchrflpg
      121 yvggvqegai tpagivnkye vnglqawlit hflwfvnayl lswfsptiif dnwipllwca
      181 nilgyavstf amikgylfpt saedckftgn ffynymmgie fnprigkwfd fklffngrpg
      241 ivawtlinls faakqqelyg hvtnsmilvn vlqaiyvldf fwnetwylkt idichdhfgw
      301 ylgwgdcvwl pylytlqgly lvyhpvqlst pnalgvlllg lvgyyifrmt nhqkdlfrrt
      361 dghcliwgkk pkaiecsyts adglkhrskl lvsgfwgvar hfnytgdlmg slayclacgg
      421 ghllpyfyii ymtillthrc lrdehrcank ygrdweryva avpyrllpgi f
//
LOCUS       NP_001425366             487 aa            linear   ROD 18-APR-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Rattus norvegicus].
ACCESSION   NP_001425366
VERSION     NP_001425366.1
DBSOURCE    REFSEQ: accession NM_001438437.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Shigeta,Y., Kanai,Y., Chairoungdua,A., Ahmed,N., Sakamoto,S.,
            Matsuo,H., Kim,D.K., Fujimura,M., Anzai,N., Mizoguchi,K., Ueda,T.,
            Akakura,K., Ichikawa,T., Ito,H. and Endou,H.
  TITLE     A novel missense mutation of SLC7A9 frequent in Japanese cystinuria
            cases affecting the C-terminus of the transporter
  JOURNAL   Kidney Int 69 (7), 1198-1206 (2006)
   PUBMED   16609684
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Kwak,J.O., Kim,H.W., Jung,S.M., Song,J.H., Hong,S.B., Oh,K.J.,
            Ko,C.B. and Cha,S.H.
  TITLE     Co-localization and interaction of b0,+-type amino acid transporter
            1 (BAT1) with caveolin-1 in rat kidney
  JOURNAL   J Nephrol 18 (6), 681-689 (2005)
   PUBMED   16358225
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Fernandez,E., Carrascal,M., Rousaud,F., Abian,J., Zorzano,A.,
            Palacin,M. and Chillaron,J.
  TITLE     rBAT-b(0,+)AT heterodimer is the main apical reabsorption system
            for cystine in the kidney
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F540-F548 (2002)
   PUBMED   12167606
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Chairoungdua,A., Segawa,H., Kim,J.Y., Miyamoto,K., Haga,H.,
            Fukui,Y., Mizoguchi,K., Ito,H., Takeda,E., Endou,H. and Kanai,Y.
  TITLE     Identification of an amino acid transporter associated with the
            cystinuria-related type II membrane glycoprotein
  JOURNAL   J Biol Chem 274 (41), 28845-28848 (1999)
   PUBMED   10506124
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098909.1, SRR26643290.1786.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="b(0,+)AT; solute carrier family 7 (amino acid
                     transporter light chain, bo,+ system), member 9;
                     glycoprotein-associated amino acid transporter b0,+AT1;
                     solute carrier family 7 (cationic amino acid transporter,
                     y+ system), member 9; solute carrier family 7
                     (glycoprotein-associated amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53527
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Region          13..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P82252.1)"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     CDS             1..487
                     /gene="Slc7a9"
                     /coded_by="NM_001438437.1:537..2000"
                     /db_xref="GeneID:116726"
                     /db_xref="RGD:619905"
ORIGIN      
        1 meetsprrrr edeksvhste pkttslqkev gllsgiciiv gtiigsgifi spksvlante
       61 svgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meafgpipay lfswtslivm
      121 kpssfaiicl sfseyvcaaf ylgcrppavv vkllaaaail littvnalsv rlgsyvqnvf
      181 taaklvivai iiisglvlla qgnvknfqns fegsqtsvgs islafynglw aydgwnqlny
      241 iteelrnpyr nlpmaivigi plvtvcyilm niayftvmtp tellqsqava vtfgdrvlyp
      301 aswvvplfva fstigaangt cftagrliyv agreghmlkv lsyisvkrlt papalvfygi
      361 iaiiyiipgd inslvnyfsf aawlfygmti lglvvmrftr kdlerpikvp ifipiivilv
      421 svflilapii sspaweylyc vlfilsglif yflfvhykfr waqkisrpit khlqmlmevv
      481 ppekdpe
//
LOCUS       NP_001425335             178 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 5 [Rattus
            norvegicus].
ACCESSION   NP_001425335 XP_006230959
VERSION     NP_001425335.1
DBSOURCE    REFSEQ: accession NM_001438406.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230959.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887621.13046.1,
                                           SRR26360176.984249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..178
                     /product="bcl2-associated agonist of cell death isoform 5"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=19812
     Region          1..>123
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..178
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438406.1:63..599"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 mfqipefeps eqedasttdr glgpsltedq pgpylapgll gsivqqqpgq aannshhgga
       61 gtmetrsrhs sypagteede gmeeelspfr grsrsappnl waaqrygrel rrmsdefegs
      121 fkgeeltysv eflpvraiam egwpllwsfq sfphtlpptp pevamfplry wtalrrlc
//
LOCUS       NP_001425333             235 aa            linear   ROD 18-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425333 XP_038945642
VERSION     NP_001425333.1
DBSOURCE    REFSEQ: accession NM_001438404.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_038945642.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.640818.1,
                                           SRR26360194.1888699.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..235
                     /product="bcl2-associated agonist of cell death isoform 2"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=25391
     Region          73..235
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..235
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438404.1:126..833"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 margvvpkag giqaqkgwrt yqpkqasriq mgtpkqpsla pahalglrks dpgirslgsd
       61 aggrrwrpaa qsmfqipefe pseqedastt drglgpslte dqpgpylapg llgsivqqqp
      121 gqaannshhg gagtmetrsr hssypagtee degmeeelsp frgrsrsapp nlwaaqrygr
      181 elrrmsdefe gsfkglprpk sagtatqmrq saswtriiqs wwdrnlgkgg stpsq
//
LOCUS       NP_001425091             124 aa            linear   ROD 18-APR-2025
DEFINITION  mth938 domain-containing protein [Rattus norvegicus].
ACCESSION   NP_001425091 XP_017444863
VERSION     NP_001425091.1
DBSOURCE    REFSEQ: accession NM_001438162.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Ma,X., Ding,W., Wang,J., Wu,G., Zhang,H., Yin,J., Zhou,L. and Li,D.
  TITLE     LOC66273 isoform 2, a novel protein highly expressed in white
            adipose tissue, induces adipogenesis in 3T3-L1 cells
  JOURNAL   J Nutr 142 (3), 448-455 (2012)
   PUBMED   22279136
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Wang,H., Ma,X., Zhang,H., Zang,J., Hu,S. and Li,D.
  TITLE     Involvement of LOC66273 isoform 2, a novel Mth938 containing
            protein, in MAPK pathway
  JOURNAL   Front Biosci (Elite Ed) 3 (4), 1241-1248 (2011)
   PUBMED   21622130
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_017444863.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.4359.1,
                                           SRR26360181.2887814.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..124
                     /product="mth938 domain-containing protein"
                     /calculated_mol_wt=13371
     Region          7..122
                     /region_name="Mth938"
                     /note="Mth938 domain. Mth938 is a hypothetical protein
                     encoded by the Methanobacterium thermoautotrophicum (Mth)
                     genome. This protein crystallizes as a dimer, although it
                     is monomeric in solution, with one disulfide bond in each
                     monomer. The function of the...; cd05126"
                     /db_xref="CDD:240162"
     CDS             1..124
                     /gene="Aamdc"
                     /gene_synonym="RGD1561459"
                     /coded_by="NM_001438162.1:139..513"
                     /db_xref="GeneID:361606"
                     /db_xref="RGD:1561459"
ORIGIN      
        1 mlmaspkias lswgqmkvqg stltykdckv wpggsrawdw retgtehspg vqpadvkeva
       61 ekgvqtlvig rgmsealkvp pstveylekq gidvrvlqte qavkeynala argirvggvf
      121 hstc
//
LOCUS       NP_001425128             511 aa            linear   ROD 18-APR-2025
DEFINITION  tripartite motif-containing protein 5 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425128 XP_006229974
VERSION     NP_001425128.1
DBSOURCE    REFSEQ: accession NM_001438199.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Zurek,B., Schoultz,I., Neerincx,A., Napolitano,L.M., Birkner,K.,
            Bennek,E., Sellge,G., Lerm,M., Meroni,G., Soderholm,J.D. and
            Kufer,T.A.
  TITLE     TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal
            degradation
  JOURNAL   PLoS One 7 (7), e41255 (2012)
   PUBMED   22829933
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Pertel,T., Hausmann,S., Morger,D., Zuger,S., Guerra,J., Lascano,J.,
            Reinhard,C., Santoni,F.A., Uchil,P.D., Chatel,L., Bisiaux,A.,
            Albert,M.L., Strambio-De-Castillia,C., Mothes,W., Pizzato,M.,
            Grutter,M.G. and Luban,J.
  TITLE     TRIM5 is an innate immune sensor for the retrovirus capsid lattice
  JOURNAL   Nature 472 (7343), 361-365 (2011)
   PUBMED   21512573
REFERENCE   6  (residues 1 to 511)
  AUTHORS   O'Connor,C., Pertel,T., Gray,S., Robia,S.L., Bakowska,J.C.,
            Luban,J. and Campbell,E.M.
  TITLE     p62/sequestosome-1 associates with and sustains the expression of
            retroviral restriction factor TRIM5alpha
  JOURNAL   J Virol 84 (12), 5997-6006 (2010)
   PUBMED   20357094
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Li,X., Gold,B., O'hUigin,C., Diaz-Griffero,F., Song,B., Si,Z.,
            Li,Y., Yuan,W., Stremlau,M., Mische,C., Javanbakht,H., Scally,M.,
            Winkler,C., Dean,M. and Sodroski,J.
  TITLE     Unique features of TRIM5alpha among closely related human TRIM
            family members
  JOURNAL   Virology 360 (2), 419-433 (2007)
   PUBMED   17156811
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229974.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.3157.1,
                                           SRR26360176.427757.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..511
                     /product="tripartite motif-containing protein 5 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 5"
                     /calculated_mol_wt=58928
     Region          8..78
                     /region_name="RING-HC_TRIM5-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and
                     similar proteins; cd16591"
                     /db_xref="CDD:438253"
     Site            order(16..17,19..20,56..57,59)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438253"
     Region          95..133
                     /region_name="Bbox2_TRIM5-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins, TRIM5, TRIM6, TRIM22, TRIM34,
                     TRIM38 and similar proteins; cd19761"
                     /db_xref="CDD:380819"
     Region          132..>233
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Region          290..507
                     /region_name="SPRY_PRY_TRIM5"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     5 (TRIM5), also known as RING finger protein 88 (RNF88);
                     cd15822"
                     /db_xref="CDD:293994"
     CDS             1..511
                     /gene="Trim5"
                     /gene_synonym="RGD1304579"
                     /coded_by="NM_001438199.1:233..1768"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:308906"
                     /db_xref="RGD:1304579"
ORIGIN      
        1 masefvmnlk eevtcpicld lmvepvsgdc ghsfcqacit lnyesskcnq deficpvcrv
       61 sylfknlrpn rhvanivqrl kefksspeee pkvlscarhg eklqlfckkd mmpicwlcer
      121 sqehrghqtv lieevvqeyk eklqaalqkl madkkefenw kddlqkerty wqnqiqkdve
      181 nvqsefkgmr dimdseekke lqklmqeked imssleesen eysqqskllg dlildvehql
      241 qcsatemlqg ventikrsht fsmrkpktip keqrrvfrap dlqgmlqvlq evteaqrywv
      301 qvtlvesnnp nifitadkrq iryedhqarh farptencha gvlgypaiqs gkhywevdvs
      361 gkgswvlgls dgsylfnpif rsnaerppnp plfrlnlsnd shsrlslsnd shyqpkygfw
      421 viglwgnsvy nafeectftg kpsvltlslm vrpcrvgifl dcaagtlsfy nisnhgtliy
      481 rfcagsfpdr vfpyfnpmgs seplticwpd s
//
LOCUS       NP_001425060             198 aa            linear   ROD 18-APR-2025
DEFINITION  transmembrane gamma-carboxyglutamic acid protein 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001425060 XP_008757619
VERSION     NP_001425060.1
DBSOURCE    REFSEQ: accession NM_001438131.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757619.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1517360.1,
                                           SRR26360172.259024.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..198
                     /product="transmembrane gamma-carboxyglutamic acid protein
                     2 precursor"
                     /note="transmembrane gamma-carboxyglutamic acid protein 2;
                     proline-rich Gla (G-carboxyglutamic acid) polypeptide 2;
                     proline rich Gla (G-carboxyglutamic acid) 2"
                     /calculated_mol_wt=20455
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1892
     Region          33..96
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     CDS             1..198
                     /gene="Prrg2"
                     /coded_by="NM_001438131.1:180..776"
                     /db_xref="GeneID:361570"
                     /db_xref="RGD:1305444"
ORIGIN      
        1 mrshpslllv ymglatcldt lphreqsqvl difldapeaq sflvgrrrfp ranhwdlell
       61 tpgnlerecl eercsweear eyfedntlte rfwesyayng kggrgrvdva glavgltsgi
      121 llivlaglga fwylhyrrrr lrvqesclqe tgliiplspp tplspppppg lptyeqalaa
      181 sgvhdapppp ysslrrph
//
LOCUS       NP_001425159             419 aa            linear   ROD 18-APR-2025
DEFINITION  zinc finger protein Pegasus [Rattus norvegicus].
ACCESSION   NP_001425159 XP_006230463
VERSION     NP_001425159.1
DBSOURCE    REFSEQ: accession NM_001438230.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Westman,B.J., Perdomo,J., Matthews,J.M., Crossley,M. and
            Mackay,J.P.
  TITLE     Structural studies on a protein-binding zinc-finger domain of Eos
            reveal both similarities and differences to classical zinc fingers
  JOURNAL   Biochemistry 43 (42), 13318-13327 (2004)
   PUBMED   15491138
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Perdomo,J., Holmes,M., Chong,B. and Crossley,M.
  TITLE     Eos and pegasus, two members of the Ikaros family of proteins with
            distinct DNA binding activities
  JOURNAL   J Biol Chem 275 (49), 38347-38354 (2000)
   PUBMED   10978333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006230463.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.3742.1,
                                           SRR26643292.4384.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840107 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..419
                     /product="zinc finger protein Pegasus"
                     /note="zinc finger protein, subfamily 1A, 5"
                     /calculated_mol_wt=46425
     Region          84..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(89,91,93,95..96,99..100,103,117,119,123..124,
                     127..128,131,145,147,149,151..152,155..156)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          96..121
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          112..132
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          124..148
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          140..158
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          251..>361
                     /region_name="PHA03269"
                     /note="envelope glycoprotein C; Provisional"
                     /db_xref="CDD:165527"
     CDS             1..419
                     /gene="Ikzf5"
                     /gene_synonym="Zfpn1a5"
                     /coded_by="NM_001438230.1:147..1406"
                     /db_xref="GeneID:309031"
                     /db_xref="RGD:1310965"
ORIGIN      
        1 mgekkpepld fvkdfqeylt qqthhvnmis gsvsgdkeae tlqgagtdgd qngldhpsve
       61 vsldensgml vdgfertfdg klkcrycnya skgtarlieh irihtgekph rchlcpfasa
      121 yerhleahmr shtgekpykc elcsfrcsdr snlshhrrrk hkmvpikgtr sslsskkmwg
      181 vlqkktsnlg ysrralinls ppsmvvqkpd ylndftheip niqtdsyetm akttptgglp
      241 rdpqelmvdn plnqlstlag qlsslppenq npaspdvdpc pdekpfmiqq psaqavvsav
      301 sasipqsssp tspdprpshs qrnyspvagp ssepsahtst psignsqpst paptlpvqdp
      361 qllhhcqhcd myfadnilyt ihmgchgyen pfqcnicgck cknkydfach fargqhnqh
//
LOCUS       NP_001425117            1150 aa            linear   ROD 18-APR-2025
DEFINITION  alpha-mannosidase 2x isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425117 XP_008757752
VERSION     NP_001425117.1
DBSOURCE    REFSEQ: accession NM_001438188.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Akama,T.O., Nakagawa,H., Wong,N.K., Sutton-Smith,M., Dell,A.,
            Morris,H.R., Nakayama,J., Nishimura,S., Pai,A., Moremen,K.W.,
            Marth,J.D. and Fukuda,M.N.
  TITLE     Essential and mutually compensatory roles of {alpha}-mannosidase II
            and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (24), 8983-8988 (2006)
   PUBMED   16754854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757752.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.2033.1,
                                           SRR26643298.3591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..1150
                     /product="alpha-mannosidase 2x isoform 2"
                     /EC_number="3.2.1.114"
                     /note="alpha-mannosidase 2x; mannosidase 2, alpha 2"
                     /calculated_mol_wt=130307
     Region          140..1149
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     CDS             1..1150
                     /gene="Man2a2"
                     /coded_by="NM_001438188.1:607..4059"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:308757"
                     /db_xref="RGD:1310238"
ORIGIN      
        1 mklkkqvtvc gaaifcvavf slylmldrvq hdparhqngg nfprsqisvl qnrieqleql
       61 leenheiish ikdsvlelta naegppallp yhtangswav lpeprpsffs vspedcqfal
      121 ggrgqkpelq mltvsedlpf dnveggvwrq gfdisyspnd wdaedlqvfv vphshndpgw
      181 iktfdkyyte qtqhilnsmv sklqedprrr flwaevsffa kwwdnisaqk raavrrlvgn
      241 gqleiatggw vmpdeanshy falvdqlieg hqwlernlga tprsgwavdp fghsstmpyl
      301 lrranltsml iqrvhyaikk hfaathslef mwrqtwdsds stdifchmmp fysydvphtc
      361 gpdpkiccqf dfkrlpggri ncpwkvppra iteanvadra allldqyrkk srlfrssvll
      421 vplgddfryd kpqewdaqff nyqrlfdfln skpefhvqaq fgtlseyfda lykrtgvepg
      481 arppgfpvls gdffsyadre dhywtgyyts rpfyksldrv lethlrgaev lyslalahar
      541 rsgltgqypl sdyavltear rtlglfqhhd aitgtakeav vvdygvrllr slvslkqvii
      601 naahylvlgd ketysfdpra pflqmddsrv shdalpertv irldssprfv vvfnpleqer
      661 lsvvsllvns prvrvlseeg qplsvqisvq wssatnmvpd vyqvsvpvrl palglgvlql
      721 qpdldgpytl qssvhvylng vklsvsrqtt fplrvvdsgt sdfaisnrym qvwfsgltgl
      781 lksvrrvdee qeqqvdmklf vygtrtskdk sgaylflpdn eakpyvpkkp pvlrvtegpf
      841 fsevaayyeh fhqvirlynl pgveglsldv sfqvdirdyv nkelalriht didsqgtfft
      901 dlngfqvqpr kylkklplqa nfypmpvmay iqdsqrrltl htaqalgvss lgngqlevil
      961 drrlmqddnr glgqglkdnk itcnhfrlll errtlmspev qqerstsyps llshmtsmyl
     1021 ntpplvlpva krestsptlh sfhplasplp cdfhllnlrm lpaedtlpaa daalilhrkg
     1081 fdcgleaknl gfncttsqgk lalgslfhgl dvlflqptsl tllyplasps nstdislepm
     1141 eistfrlrlg
//
LOCUS       NP_001012168             486 aa            linear   ROD 18-APR-2025
DEFINITION  tubby-related protein 2 isoform 12 [Rattus norvegicus].
ACCESSION   NP_001012168 XP_341860
VERSION     NP_001012168.1
DBSOURCE    REFSEQ: accession NM_001012168.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC084696.1.
            
            On Feb 11, 2005 this sequence version replaced XP_341860.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084696.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..486
                     /product="tubby-related protein 2 isoform 12"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=53515
     Region          <17..>136
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          232..481
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..486
                     /gene="Tulp2"
                     /coded_by="NM_001012168.1:90..1550"
                     /note="isoform 12 is encoded by transcript variant 14"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mpntpphdsl gvgspflqen vpqahlpsga hsalvtmsyv gdgsgerapl lsprgavytr
       61 gngpavrhlc wlpdssdsdv eevtmedipv isrppkthla nrrrgwlasp gpgiseeeev
      121 epkdarvedk tpspdpdpte nsdrvhgdsa scnmeentak knietasgig dedpekkeat
      181 estetnnalv askvlqgdgd tsnhsawnmt cpmprtpgpr lgedmeayvl lpaprehmvq
      241 crivrnkhgv dkgmfpsyyl yleaedgvav rssplghfll agrkrkrskt snylisldpk
      301 dmsrngnnfv gkvrsnvlgt kftifdngvn pernywipds arireelgvv cyetnvlgfr
      361 gprkmtvilp gmdsrkqrmk vqpqndqdsi lsrvqkgarh gllllqnkap swsdesgayv
      421 lnfhgrvtra svknfqivhp depdhlvlqf grvapniftm dfryplcplq afaiclssfd
      481 gklace
//
LOCUS       NP_446381                487 aa            linear   ROD 18-APR-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Rattus norvegicus].
ACCESSION   NP_446381
VERSION     NP_446381.1
DBSOURCE    REFSEQ: accession NM_053929.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Shigeta,Y., Kanai,Y., Chairoungdua,A., Ahmed,N., Sakamoto,S.,
            Matsuo,H., Kim,D.K., Fujimura,M., Anzai,N., Mizoguchi,K., Ueda,T.,
            Akakura,K., Ichikawa,T., Ito,H. and Endou,H.
  TITLE     A novel missense mutation of SLC7A9 frequent in Japanese cystinuria
            cases affecting the C-terminus of the transporter
  JOURNAL   Kidney Int 69 (7), 1198-1206 (2006)
   PUBMED   16609684
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Kwak,J.O., Kim,H.W., Jung,S.M., Song,J.H., Hong,S.B., Oh,K.J.,
            Ko,C.B. and Cha,S.H.
  TITLE     Co-localization and interaction of b0,+-type amino acid transporter
            1 (BAT1) with caveolin-1 in rat kidney
  JOURNAL   J Nephrol 18 (6), 681-689 (2005)
   PUBMED   16358225
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Fernandez,E., Carrascal,M., Rousaud,F., Abian,J., Zorzano,A.,
            Palacin,M. and Chillaron,J.
  TITLE     rBAT-b(0,+)AT heterodimer is the main apical reabsorption system
            for cystine in the kidney
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F540-F548 (2002)
   PUBMED   12167606
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Chairoungdua,A., Segawa,H., Kim,J.Y., Miyamoto,K., Haga,H.,
            Fukui,Y., Mizoguchi,K., Ito,H., Takeda,E., Endou,H. and Kanai,Y.
  TITLE     Identification of an amino acid transporter associated with the
            cystinuria-related type II membrane glycoprotein
  JOURNAL   J Biol Chem 274 (41), 28845-28848 (1999)
   PUBMED   10506124
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB029559.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB029559.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="b(0,+)AT; solute carrier family 7 (amino acid
                     transporter light chain, bo,+ system), member 9;
                     glycoprotein-associated amino acid transporter b0,+AT1;
                     solute carrier family 7 (cationic amino acid transporter,
                     y+ system), member 9; solute carrier family 7
                     (glycoprotein-associated amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53527
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Region          13..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P82252.1)"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     CDS             1..487
                     /gene="Slc7a9"
                     /coded_by="NM_053929.1:170..1633"
                     /db_xref="GeneID:116726"
                     /db_xref="RGD:619905"
ORIGIN      
        1 meetsprrrr edeksvhste pkttslqkev gllsgiciiv gtiigsgifi spksvlante
       61 svgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meafgpipay lfswtslivm
      121 kpssfaiicl sfseyvcaaf ylgcrppavv vkllaaaail littvnalsv rlgsyvqnvf
      181 taaklvivai iiisglvlla qgnvknfqns fegsqtsvgs islafynglw aydgwnqlny
      241 iteelrnpyr nlpmaivigi plvtvcyilm niayftvmtp tellqsqava vtfgdrvlyp
      301 aswvvplfva fstigaangt cftagrliyv agreghmlkv lsyisvkrlt papalvfygi
      361 iaiiyiipgd inslvnyfsf aawlfygmti lglvvmrftr kdlerpikvp ifipiivilv
      421 svflilapii sspaweylyc vlfilsglif yflfvhykfr waqkisrpit khlqmlmevv
      481 ppekdpe
//
LOCUS       NP_001425111             389 aa            linear   ROD 18-APR-2025
DEFINITION  UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8
            [Rattus norvegicus].
ACCESSION   NP_001425111 XP_063117434
VERSION     NP_001425111.1
DBSOURCE    REFSEQ: accession NM_001438182.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ishida,H., Togayachi,A., Sakai,T., Iwai,T., Hiruma,T., Sato,T.,
            Okubo,R., Inaba,N., Kudo,T., Gotoh,M., Shoda,J., Tanaka,N. and
            Narimatsu,H.
  TITLE     A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which
            synthesizes poly-N-acetyllactosamine, is dramatically upregulated
            in colon cancer
  JOURNAL   FEBS Lett 579 (1), 71-78 (2005)
   PUBMED   15620693
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063117434.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2500783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..389
                     /product="UDP-GlcNAc:betaGal
                     beta-1,3-N-acetylglucosaminyltransferase 8"
                     /note="UDP-Gal:betaGal beta 1,3-galactosyltransferase
                     polypeptide 7"
                     /calculated_mol_wt=43084
     Region          154..341
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..389
                     /gene="B3gnt8"
                     /gene_synonym="B3galt7"
                     /coded_by="NM_001438182.1:443..1612"
                     /db_xref="GeneID:308440"
                     /db_xref="RGD:1305374"
ORIGIN      
        1 mrcrkcqlcl salltllglk vyiewtsesw lkkaeprgal psptppsaep tlptnlsarl
       61 gqtgplssay wnqqqrqlgv lpssdcqtwg svaaseildf ilypqdlrrf llsaacrsfp
      121 lwlpagegsp vascsdkdvp ylllavksep ghfaarqavr etwgspvagt rllfllgspl
      181 gmggpdltsl vtwesrrygd lllwdfldvp ynrtlkdlll ltwlshhcpk vsfvlqvqdn
      241 afvhipalle hlqalpptwa rslylgevft qakplrkpgg pfyvpktffe gdypayasgg
      301 gyvisgrlap wllqaaarva pfpfddvytg fcfralglap rahpgfltaw paertrdpca
      361 vrglllvhpv spqdtiwlwr hlwvpelrc
//
LOCUS       NP_001128102             175 aa            linear   ROD 18-APR-2025
DEFINITION  putative coiled-coil domain-containing protein 196 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001128102 XP_001080862 XP_576055
VERSION     NP_001128102.1
DBSOURCE    REFSEQ: accession NM_001134630.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473947.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_576055.2, XP_001080862.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..175
                     /product="putative coiled-coil domain-containing protein
                     196 isoform 1"
                     /note="putative coiled-coil domain-containing protein 196"
                     /calculated_mol_wt=20483
     CDS             1..175
                     /gene="Ccdc196"
                     /gene_synonym="RGD1562540"
                     /coded_by="NM_001134630.1:75..602"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500678"
                     /db_xref="RGD:1562540"
ORIGIN      
        1 mtsgsnsses glsskrnpkt ydnylkelne dlklrkqell emlkpledkn nlllqklman
       61 leekqrslqi mrqimagrgg dessveelik eaqemkqnle kqqrkikwvk yeeqpnilqg
      121 fhdkvievki ealrnyektn dfelslylqh dfetkqealk llrpqealfs evnar
//
LOCUS       NP_001425105             831 aa            linear   ROD 18-APR-2025
DEFINITION  cysteine--tRNA ligase, cytoplasmic isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425105 XP_006230775
VERSION     NP_001425105.1
DBSOURCE    REFSEQ: accession NM_001438176.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Liu,C., Gamper,H., Shtivelband,S., Hauenstein,S., Perona,J.J. and
            Hou,Y.M.
  TITLE     Kinetic quality control of anticodon recognition by a eukaryotic
            aminoacyl-tRNA synthetase
  JOURNAL   J Mol Biol 367 (4), 1063-1078 (2007)
   PUBMED   17303165
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Davidson,E., Caffarella,J., Vitseva,O., Hou,Y.M. and King,M.P.
  TITLE     Isolation of two cDNAs encoding functional human cytoplasmic
            cysteinyl-tRNA synthetase
  JOURNAL   Biol Chem 382 (3), 399-406 (2001)
   PUBMED   11347887
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Kim,J.E., Kim,K.H., Lee,S.W., Seol,W., Shiba,K. and Kim,S.
  TITLE     An elongation factor-associating domain is inserted into human
            cysteinyl-tRNA synthetase by alternative splicing
  JOURNAL   Nucleic Acids Res 28 (15), 2866-2872 (2000)
   PUBMED   10908348
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006230775.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.4215.1,
                                           SRR26643299.5214.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..831
                     /product="cysteine--tRNA ligase, cytoplasmic isoform 1"
                     /EC_number="6.1.1.16"
                     /note="cysteinyl-tRNA synthetase, cytoplasmic;
                     cysteine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=94748
     Region          4..76
                     /region_name="GST_C_CysRS_N"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of Cysteinyl-tRNA synthetase from higher
                     eukaryotes; cd10310"
                     /db_xref="CDD:198343"
     Site            order(5..7,9..14,16..17,24,27,33..34)
                     /site_type="other"
                     /note="putative protein interface 1 [polypeptide binding]"
                     /db_xref="CDD:198343"
     Site            order(32..36,64..65,67..68,72,75..76)
                     /site_type="other"
                     /note="putative protein interface 2 [polypeptide binding]"
                     /db_xref="CDD:198343"
     Region          91..828
                     /region_name="PTZ00399"
                     /note="cysteinyl-tRNA-synthetase; Provisional"
                     /db_xref="CDD:240402"
     CDS             1..831
                     /gene="Cars1"
                     /gene_synonym="Cars"
                     /coded_by="NM_001438176.1:51..2546"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293638"
                     /db_xref="RGD:1310747"
ORIGIN      
        1 magssaeqaa dyrsilsisd eaarvqaldq hlstrsyiqg yslsqadvdv frqfsappad
       61 srlfhvarwf rhieallggp qgrgepcrlq askgrrvqpq wsppagtepc rlrlynsltr
      121 nkdvfipqdg kkvtwyccgp tvydashmgh arsyisfdil rrvlrdyfqy dvfycmnitd
      181 iddkiirrar qnylfeqyre qkpsaaqllk dvgdamkpfs vklsettdpd krqmleriqn
      241 svklateple qavhsnpsge evdsrvqvll eeakdllsdw ldstggsevt dnsifsklpk
      301 fweeefhkdm ealnvlppdv ltrvseyvpe ivnfvqkivd ngygyasngs vyfdtakfaa
      361 sekhsygklv peavgdqkal qegegdlsis adrlsekrsp ndfalwkask pgepswpcpw
      421 gkgrpgwhie csamagsllg asmdihgggf dlrfphhdne laqseayfen dcwvryflht
      481 ghltiagckm skslknfiti kdalkkhsar qlrlaflmhs wkdtldyssn tmesalqyek
      541 fmnefflnvk dilrapvdit gqfekweaee velnknfydk ktavhealcd nidtrtvmee
      601 mralvsqcnl ymaarkaarr rpnralleni amylthmlki fgaieeenpl gfpvggpgtn
      661 lnlestvmpy lqvlsefreg vrkiarekkv levlqlsdal rddilpelgv rfedheglpt
      721 vvklvdrdtl lkekeekkra eeekrrkkee aarkkqeqea aklakmktpp semfrsetdk
      781 yskfdenglp thdtegkels kgqtkklkkl feaqekvyke ylqqlqnssl q
//
LOCUS       NP_001425112             685 aa            linear   ROD 18-APR-2025
DEFINITION  beta-taxilin [Rattus norvegicus].
ACCESSION   NP_001425112 XP_006227719
VERSION     NP_001425112.1
DBSOURCE    REFSEQ: accession NM_001438183.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006227719.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.103.1, SRR26643289.97.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..685
                     /product="beta-taxilin"
                     /calculated_mol_wt=76826
     Region          146..453
                     /region_name="Taxilin"
                     /note="Myosin-like coiled-coil protein; pfam09728"
                     /db_xref="CDD:462861"
     Region          <527..677
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..685
                     /gene="Txlnb"
                     /gene_synonym="RGD1307979"
                     /coded_by="NM_001438183.1:105..2162"
                     /db_xref="GeneID:308622"
                     /db_xref="RGD:1307979"
ORIGIN      
        1 metnhpdqls veqpnppgds splnqnvpgk qdvqqsstsg qaaeqeasph pekgdhdise
       61 elsrqledii nmygsaaspt gkegtsetke qpqnteapdn edgdyeette etdreptape
      121 epatvkgpvs nkeqklekki lkglgkeanl lmqnlnklqa peekldflfk kyaelldehr
      181 teqkklklll kqqaqtqrek dqlqsehnra ilarsklesl crelqrhnkt lkeetlqrar
      241 eeeekrkeit shfqstltdi qtqieqqser nmklcqente laeklksiid qyelreehld
      301 kifkhrelqq klvdakleea qelmqeaeer hrrekeylln qaaewklqak vlkeqetvlq
      361 aqltlysgrf eefqstltks nevfatfkqe mdnttkkmkk lekdtatwka rfencnkall
      421 dmieekalra keyecfvmki qrlenlcral qeerkelykk irdakmseke dqvqhtsdee
      481 peskvsedkq mdveaangvq navknlataf ailhhpeftp dqsrerqpav ngppggsdlt
      541 hqhtepahln hpnpssvsgs pqppvgsqag seggceaapa ptacctpaea elqsqglsag
      601 nppdpkpqkp eakasgqvpl spaqgslavv eakcdispsp eserdpavvp gceskehppp
      661 evpdiplgpn tglprepdac lngve
//
LOCUS       NP_112270                939 aa            linear   ROD 18-APR-2025
DEFINITION  AP-2 complex subunit alpha-2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_112270
VERSION     NP_112270.2
DBSOURCE    REFSEQ: accession NM_031008.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Capella,P., Asensio,J., Troncoso,M., Sosa,M.A. and Seltzer,A.M.
  TITLE     Evidence on differential role for alpha 1 and alpha 2 subtypes of
            AP-2 adaptin in the central nervous system
  JOURNAL   Neurosci Lett 808, 137282 (2023)
   PUBMED   37127089
  REMARK    GeneRIF: Evidence on differential role for alpha 1 and alpha 2
            subtypes of AP-2 adaptin in the central nervous system.
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Marcello,E., Saraceno,C., Musardo,S., Vara,H., de la Fuente,A.G.,
            Pelucchi,S., Di Marino,D., Borroni,B., Tramontano,A.,
            Perez-Otano,I., Padovani,A., Giustetto,M., Gardoni,F. and Di
            Luca,M.
  TITLE     Endocytosis of synaptic ADAM10 in neuronal plasticity and
            Alzheimer's disease
  JOURNAL   J Clin Invest 123 (6), 2523-2538 (2013)
   PUBMED   23676497
REFERENCE   4  (residues 1 to 939)
  AUTHORS   Duncker,S.V., Franz,C., Kuhn,S., Schulte,U., Campanelli,D.,
            Brandt,N., Hirt,B., Fakler,B., Blin,N., Ruth,P., Engel,J.,
            Marcotti,W., Zimmermann,U. and Knipper,M.
  TITLE     Otoferlin couples to clathrin-mediated endocytosis in mature
            cochlear inner hair cells
  JOURNAL   J Neurosci 33 (22), 9508-9519 (2013)
   PUBMED   23719817
REFERENCE   5  (residues 1 to 939)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 939)
  AUTHORS   Takei,K., Mundigl,O., Daniell,L. and De Camilli,P.
  TITLE     The synaptic vesicle cycle: a single vesicle budding step involving
            clathrin and dynamin
  JOURNAL   J Cell Biol 133 (6), 1237-1250 (1996)
   PUBMED   8682861
REFERENCE   7  (residues 1 to 939)
  AUTHORS   Voglmaier,S.M., Keen,J.H., Murphy,J.E., Ferris,C.D.,
            Prestwich,G.D., Snyder,S.H. and Theibert,A.B.
  TITLE     Inositol hexakisphosphate receptor identified as the clathrin
            assembly protein AP-2
  JOURNAL   Biochem Biophys Res Commun 187 (1), 158-163 (1992)
   PUBMED   1325787
REFERENCE   8  (residues 1 to 939)
  AUTHORS   Bahler,M., Klein,R.L., Wang,J.K., Benfenati,F. and Greengard,P.
  TITLE     A novel synaptic vesicle-associated phosphoprotein: SVAPP-120
  JOURNAL   J Neurochem 57 (2), 423-430 (1991)
   PUBMED   2072093
  REMARK    Erratum:[J Neurochem 1991 Dec;57(6):2155]
REFERENCE   9  (residues 1 to 939)
  AUTHORS   Tucker,K.L., Nathanson,K. and Kirchhausen,T.
  TITLE     Sequence of the rat alpha c large chain of the clathrin associated
            protein complex AP-2
  JOURNAL   Nucleic Acids Res 18 (17), 5306 (1990)
   PUBMED   2402467
REFERENCE   10 (residues 1 to 939)
  AUTHORS   Kirchhausen,T., Nathanson,K.L., Matsui,W., Vaisberg,A., Chow,E.P.,
            Burne,C., Keen,J.H. and Davis,A.E.
  TITLE     Structural and functional division into two domains of the large
            (100- to 115-kDa) chains of the clathrin-associated protein complex
            AP-2
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2612-2616 (1989)
   PUBMED   2495531
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081786.1.
            
            On Dec 8, 2007 this sequence version replaced NP_112270.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081786.1, SRR8487227.332266.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..939
                     /product="AP-2 complex subunit alpha-2 isoform 2"
                     /note="adaptor protein complex AP-2, alpha 2 subunit; AP-2
                     complex subunit alpha-2; alpha2-adaptin; alpha-adaptin C;
                     100 kDa coated vesicle protein C; adaptor protein complex
                     AP-2 subunit alpha-2; adaptor-related protein complex 2,
                     alpha 2 subunit; adapter-related protein complex 2 alpha-2
                     subunit; clathrin assembly protein complex 2 alpha-C large
                     chain; plasma membrane adaptor HA2/AP2 adaptin alpha C
                     subunit; adapter-related protein complex 2 subunit
                     alpha-2"
                     /calculated_mol_wt=104043
     Region          29..591
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          332..355
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          369..398
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          408..434
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          616..682
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18484.3)"
     Region          717..820
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          826..934
                     /region_name="Alpha_adaptin_C"
                     /note="Alpha adaptin AP2, C-terminal domain; pfam02296"
                     /db_xref="CDD:426707"
     CDS             1..939
                     /gene="Ap2a2"
                     /coded_by="NM_031008.2:81..2900"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:81637"
                     /db_xref="RGD:71015"
ORIGIN      
        1 mpavskgegm rglavfisdi rnckskeaei krinkelani rskfkgdkal dgyskkkyvc
       61 kllfifllgh didfghmeav nllssnryte kqigylfisv lvnsnselir linnaikndl
      121 asrnptfmgl alhcianvgs remaeafage ipkilvagdt mdsvkqsaal cllrlyrtsp
      181 dlvpmgdwts rvvhllndqh lgvvtaatsl ittlaqknpe efktsvslav srlsrivtsa
      241 stdlqdytyy fvpapwlsvk llrllqcypp pedpavrgrl tecletilnk aqeppkskkv
      301 qhsnaknavl feaisliihh dsepnllvra cnqlgqflqh retnlrylal esmctlasse
      361 fsheavkthi etvinalkte rdvsvrqrav dllyamcdrs naqqivaeml syletadysi
      421 reeivlkvai laekyavdyt wyvdtilnli riagdyvsee vwyrviqivi nrddvqgyaa
      481 ktvfealqap achenlvkvg gyilgefgnl iagdprsspl iqfnllhskf hlcsvptral
      541 llstyikfvn lfpevkatiq dvlrsdsqlk nadvelqqra veylrlstva stdilatvle
      601 emppfperes silaklkkkk gpstvtdlee tkrersidvn ggpepvpast saastpspsa
      661 dllglgavpp aptgppptsg ggllvdvfsd sasavaplap gsednfarfv cknngvlfen
      721 qllqiglkse frqnlgrmfi fygnktstqf lnftptlica ddlqtnlnlq tkpvdptvdg
      781 gaqvqqvvni ecisdfteap vlniqfrygg tfqnvsvklp itlnkffqpt emasqdffqr
      841 wkqlsnpqqe vqnifkakhp mdteitkaki igfgsallee vdpnpanfvg agiihtkttq
      901 igcllrlepn lqaqmyrltl rtskdtvsqr lcellseqf
//
LOCUS       NP_001425138             713 aa            linear   ROD 18-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 6 [Rattus norvegicus].
ACCESSION   NP_001425138 XP_017449060
VERSION     NP_001425138.1
DBSOURCE    REFSEQ: accession NM_001438209.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Haribaskar,R., Putz,M., Schupp,B., Skouloudaki,K., Bietenbeck,A.,
            Walz,G. and Schafer,T.
  TITLE     The planar cell polarity (PCP) protein Diversin translocates to the
            nucleus to interact with the transcription factor AF9
  JOURNAL   Biochem Biophys Res Commun 387 (1), 212-217 (2009)
   PUBMED   19591803
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of rat Ankrd6 gene in silico
  JOURNAL   Int J Mol Med 15 (2), 359-363 (2005)
   PUBMED   15647854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 16, 2025 this sequence version replaced XP_017449060.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.26755.1,
                                           SRR26643299.22215.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..713
                     /product="ankyrin repeat domain-containing protein 6"
                     /calculated_mol_wt=77946
     Region          5..244
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(41,43,47..48,51..53,55..56,60,63,72,74,76,80..81,
                     84..86,88..89,93,96,105,107,109,113..114,117..119,
                     121..122,126,129,138)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          41..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          74..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          107..138
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          141..171
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(142,146..147,150..152,154..155,159,162,171,173,175,
                     179..180,183..185,187..188,192,195,204,206,208,212..213,
                     216..218,220..221,225,228,237)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          173..204
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..237
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <545..706
                     /region_name="PLN02847"
                     /note="triacylglycerol lipase"
                     /db_xref="CDD:178439"
     CDS             1..713
                     /gene="Ankrd6"
                     /coded_by="NM_001438209.1:271..2412"
                     /db_xref="GeneID:500430"
                     /db_xref="RGD:1583731"
ORIGIN      
        1 msqqdavaal serlliaayk gqtenvvqli nkgakvavtk hgrtplhlaa nkghlsvvqi
       61 llkagcdldv qddgdqtalh ratvvgntei ltaliregca ldrqdkdgnt alheaawhgf
      121 sqsakllvka ganvlarnka gntalhlacq nshsqstrvl llggsradlk nnagdtclhv
      181 aarynhlsvv rlllsafcsv heknqagdta lhvaaalnhk kvvkilleag adttlvnnag
      241 qtpletaryh dnpevalllt kapqilrfsr grslrkrrer lkeerraqsv prdevaqskg
      301 svsagdtpss eqavpekeea rrdcppasqe prkderrrks rpevsalsdp tpaadqqpgh
      361 qknlhghhhq kkksrhrcws pppphgfray qlytlyrged gkvmqapikg crceplinkl
      421 enqleaavee lraelgtvqd kvntklghme sksqhqmcvl dklmverlsa erteclnrlq
      481 qhaaaekqeg ekrqmslvde lkswcmlkiq nlelrlsges rtfrakstps psdsspavdq
      541 pvvaagpgaa sdsssqvvrp kdkalnatav prhqqellps dctgsglrkv kapaasrlgd
      601 qqtgscvnrg tqtkksargg qtkhrgqqpt asspsgqqps aassdardas qaleltqyff
      661 eavsaqmekw yerkieears qasqkaqqde atlkehirsl eeevaklrtk mhk
//
LOCUS       NP_001178556             746 aa            linear   ROD 18-APR-2025
DEFINITION  fibronectin type III and SPRY domain-containing protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001178556 XP_006229502 XP_218860
VERSION     NP_001178556.1
DBSOURCE    REFSEQ: accession NM_001191627.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_006229502.1, XP_218860.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223649.1, SRR26643295.2943.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..746
                     /product="fibronectin type III and SPRY domain-containing
                     protein 2"
                     /calculated_mol_wt=84567
     Region          203..>307
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          368..453
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            order(368,436,451)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <369..>558
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(452..453,455..456)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          561..737
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..746
                     /gene="Fsd2"
                     /gene_synonym="RGD1305167"
                     /coded_by="NM_001191627.2:153..2393"
                     /db_xref="GeneID:308779"
                     /db_xref="RGD:1305167"
ORIGIN      
        1 meeeageepg lgrstaprdf hfyhmdlyds edrlqlfpge ssrtrrevtq aeltneprga
       61 gdsknlqkev dalvhlygle dehelggefv dehrlgtlgy pygmrrrdpg reqrdwglsg
      121 eaaeaedlcy gvqgppdqcq dlreayryth graseeyecy vipeeedeee padvfcvtck
      181 tpvrtvekdf dihkehevtp inkalehakd eihknmckle qqiiemenfa shleevfitv
      241 eenfgrqeqn fechyneile tlaqkyeeki qalgekkkek lealygqlvs cgenldacre
      301 lmetieemch eekvdflkda vamtdrlgkf lktktdvels akpefedqtl dfsdveqlmd
      361 sintvpapsa pvinpqapns atgssvrvcw slysddtves yqlsyrpvqd sspgkdqaef
      421 tmtvketycs vknlepntqy efwviaqnrt gpspssehvv ymtapsppsi kteairscee
      481 avlicwesgn lnpvdsytve liqaetpeas gvtesvvgip tcesliqlqp rhsytiyvra
      541 lnvggtsars kpatvhttgs yfqlnkdtch pwltisedgf tvvrsekkrs frrelppska
      601 qfsrcvavmg nlipvrgrhy wevevdehld ytvgvacedv pkqedlganr lswcmrhtfa
      661 strhryeflh ngttpdirit vapkkigvll dyedsklsff nvdiaqhlyt fscplhqfvh
      721 pcfsleksgg lkicngisap khvtff
//
LOCUS       NP_001100927             104 aa            linear   ROD 18-APR-2025
DEFINITION  KICSTOR complex protein kaptin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100927 XP_001074187 XP_217806
VERSION     NP_001100927.1
DBSOURCE    REFSEQ: accession NM_001107457.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Baple,E.L., Maroofian,R., Chioza,B.A., Izadi,M., Cross,H.E.,
            Al-Turki,S., Barwick,K., Skrzypiec,A., Pawlak,R., Wagner,K.,
            Coblentz,R., Zainy,T., Patton,M.A., Mansour,S., Rich,P.,
            Qualmann,B., Hurles,M.E., Kessels,M.M. and Crosby,A.H.
  TITLE     Mutations in KPTN cause macrocephaly, neurodevelopmental delay, and
            seizures
  JOURNAL   Am J Hum Genet 94 (1), 87-94 (2014)
   PUBMED   24239382
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Bearer,E.L. and Abraham,M.T.
  TITLE     2E4 (kaptin): a novel actin-associated protein from human blood
            platelets found in lamellipodia and the tips of the stereocilia of
            the inner ear
  JOURNAL   Eur J Cell Biol 78 (2), 117-126 (1999)
   PUBMED   10099934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001074187.1, XP_217806.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB734880.1, CB810022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..104
                     /product="KICSTOR complex protein kaptin isoform 2"
                     /note="kaptin-like 1; KICSTOR complex protein kaptin"
                     /calculated_mol_wt=11153
     CDS             1..104
                     /gene="Kptn"
                     /gene_synonym="Kptnl1"
                     /coded_by="NM_001107457.1:75..389"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308107"
                     /db_xref="RGD:1310341"
ORIGIN      
        1 mgeaavaegp cplredsftr fssqsnvygl aggadgrgel laatlkgkvl gfryqdlrqk
       61 irpvakelqf nyipvdaeiv sidtfnkspp krglvvgitf ikvp
//
LOCUS       NP_001425120             604 aa            linear   ROD 18-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 7 [Rattus
            norvegicus].
ACCESSION   NP_001425120
VERSION     NP_001425120.1
DBSOURCE    REFSEQ: accession NM_001438191.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Shi,J.D., Kukar,T., Wang,C.Y., Li,Q.Z., Cruz,P.E.,
            Davoodi-Semiromi,A., Yang,P., Gu,Y., Lian,W., Wu,D.H. and She,J.X.
  TITLE     Molecular cloning and characterization of a novel mammalian
            endo-apyrase (LALP1)
  JOURNAL   J Biol Chem 276 (20), 17474-17478 (2001)
   PUBMED   11278936
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2562402.1,
                                           SRR26643429.5703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..604
                     /product="ectonucleoside triphosphate diphosphohydrolase
                     7"
                     /EC_number="3.6.1.-"
                     /note="bifunctional protein NCOAT-like"
                     /calculated_mol_wt=68751
     Region          82..531
                     /region_name="ASKHA_NBD_NTPDase4-like"
                     /note="nucleotide-binding domain (NBD) of the
                     ectonucleoside triphosphate diphosphohydrolase 4
                     (NTPDase4)-like subfamily; cd24045"
                     /db_xref="CDD:466895"
     CDS             1..604
                     /gene="Entpd7"
                     /coded_by="NM_001438191.1:209..2023"
                     /db_xref="GeneID:309390"
                     /db_xref="RGD:1310638"
ORIGIN      
        1 marisfsylc paswyftvpt vspflrqrva flglffipcl lllllimdlr hwttslprdr
       61 qyerylarvg dleatntedp nlsyglvvdc gssgsrifvy fwprhngnph dlldikqmrd
      121 rnsqpvvkki kpgisamadt pehasdylrp llsfaaahvp vkkhretply ilctagmrll
      181 perqqvaila dlvkdlplef dflfsqsqae visgkqegvy awiginfvlg rfdhedesda
      241 dtsvdsasgr rrtvgildmg gaslqiayev ptsasvlppk qeeaakilla efnlgcdvqh
      301 tehvyrvyvt tflgfggnfa rqryedlvln etlnknrllg qrtglspdnp fldpclpvgl
      361 tdvvernsqv lhfrgkgdwa tcrtmlspll arsntsqasl ngiyqspidf nnsefygfse
      421 ffyctedvlr iggryhgptf akaaqdycgm twsvlaqrfk nglfsshade hrlkyqcfks
      481 awmyevlheg fhfpydypnl qtaqlvydre vqwtlgaily ktrflplrdl rqggvrqahg
      541 swfrlsfvyn hylffactlv vllaivlyll rihrihrrqt rasapldllw ieqvvpmigv
      601 qvgp
//
LOCUS       NP_001425165             304 aa            linear   ROD 18-APR-2025
DEFINITION  DCN1-like protein 3 [Rattus norvegicus].
ACCESSION   NP_001425165 XP_008757972
VERSION     NP_001425165.1
DBSOURCE    REFSEQ: accession NM_001438236.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Ma,T., Shi,T., Huang,J., Wu,L., Hu,F., He,P., Deng,W., Gao,P.,
            Zhang,Y., Song,Q., Ma,D. and Qiu,X.
  TITLE     DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
            progression and cell growth
  JOURNAL   Cancer Sci 99 (11), 2128-2135 (2008)
   PUBMED   18823379
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_008757972.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.4202.1,
                                           SRR26643298.4964.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676785,
                                           SAMN16676807 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..304
                     /product="DCN1-like protein 3"
                     /EC_number="3.1.-.-"
                     /note="DCUN1 domain-containing protein 3; defective in
                     cullin neddylation protein 1-like protein 3; DCN1,
                     defective in cullin neddylation 1, domain containing 3"
                     /calculated_mol_wt=34219
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     Region          164..276
                     /region_name="Cullin_binding"
                     /note="Cullin binding; pfam03556"
                     /db_xref="CDD:460971"
     Region          285..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B2.1)"
     CDS             1..304
                     /gene="Dcun1d3"
                     /gene_synonym="DCNL3; RGD1308893"
                     /coded_by="NM_001438236.1:262..1176"
                     /db_xref="GeneID:309035"
                     /db_xref="RGD:1308893"
ORIGIN      
        1 mgqcvtkckn psstlgskng drdpsskshs rrgashreeq vppcgkpagd ilvngtkkae
       61 aateacqlpt ssgdagresk tnaeesslqr leelfrrykd eredaileeg merfcndlcv
      121 dptefrvlll awkfqaatmc kftrkeffdg ckaisadsid gicarfpsll teakqedkfk
      181 dlyrftfqfg ldseegqrsl hreiaialwk lvftqnnppv ldqwlnflte npsgikgisr
      241 dtwnmflnft qvigpdlsny sedeawpslf dtfvewemer rkrevegrga lssgpeglcp
      301 eeqt
//
LOCUS       NP_001017471             393 aa            linear   ROD 18-APR-2025
DEFINITION  activating transcription factor 7-interacting protein 2 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001017471 XP_573040
VERSION     NP_001017471.1
DBSOURCE    REFSEQ: accession NM_001017471.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083663.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573040.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..393
                     /product="activating transcription factor 7-interacting
                     protein 2 isoform 2"
                     /calculated_mol_wt=43943
     Region          59..267
                     /region_name="ATF7IP_BD"
                     /note="ATF-interacting protein binding domain; pfam16788"
                     /db_xref="CDD:465271"
     CDS             1..393
                     /gene="Atf7ip2"
                     /coded_by="NM_001017471.1:78..1259"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:497859"
                     /db_xref="RGD:1583744"
ORIGIN      
        1 mespdrkrrk vlkakktmpt scrkqmeiln qsknveapkt tvvtnipngh nqkmfsenke
       61 nvkvmktseq inenaceale rhtalleqvk hwirqeicti ncnlfdkkln elnerigktq
      121 crskheaiag elfikirrlq kriktvlssq gnclepntlp sntvckvtds vnlsvtqrsv
      181 ksqskrmssv nhtpfnssek asrkinlpsa cvefvsesnd dvmlisvenp nlttpiasdp
      241 teirkntsrn vssspnarse vvpvekkfdf vidltregls sysigppssr lhhlriapsa
      301 edqafntgaf gdhsnsrvqq igtkpstrrk kipvkekenl qqenttrrgd gggysrvqks
      361 eltgtrppgm sssssdnrkg fntsflnqnr tlp
//
LOCUS       NP_001425143             619 aa            linear   ROD 18-APR-2025
DEFINITION  zinc finger protein 668 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425143 XP_017444707
VERSION     NP_001425143.1
DBSOURCE    REFSEQ: accession NM_001438214.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Kim,S., Elkon,K.B. and Ma,X.
  TITLE     Transcriptional suppression of interleukin-12 gene expression
            following phagocytosis of apoptotic cells
  JOURNAL   Immunity 21 (5), 643-653 (2004)
   PUBMED   15539151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_017444707.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.5514.1,
                                           SRR26643296.2909.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..619
                     /product="zinc finger protein 668 isoform 1"
                     /calculated_mol_wt=68152
     Region          24..44
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          65..419
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          86..106
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          114..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..218
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..246
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(231,233,235,237..238,241..242,245,259,261,265..266,
                     269..270,273,287,289,291,293..294,297..298,301)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          254..274
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          310..330
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          338..358
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          366..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          394..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(523,525,527,529..530,533..534,537,551,553,557..558,
                     561..562,565,579,581,583,585..586,589..590,593)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..619
                     /gene="Zfp668"
                     /gene_synonym="RGD1308623; Znf668"
                     /coded_by="NM_001438214.1:116..1975"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309002"
                     /db_xref="RGD:1308623"
ORIGIN      
        1 meveaaeaks pgpcykrsgr rykclfctkt fpnapraarh aathtttdct eevnevqpkv
       61 daepkaeeas gdkvsgsvak prpyacplcp kayktapelr shgrshtgek pfpcpecgrr
      121 fmqpvclrvh lashagelpf rcthcpkayg tlsklkihqr ghtgerpyac tdcgksfadp
      181 svfrkhrrth aglrpyscer cgkayaelkd lrnhershtg erpflcsecg ksfsrssslt
      241 chqrihaaqk pyrcpacgkg ftqlssyqsh erthsgekpf lcprcgrmfs dpssfrrhqr
      301 ahegvkpyrc ekcgkdfrqp adlamhrrvh tgdrpfkclq cdktfvaswd lkrhalvhsg
      361 qrpfrceecg rafaeraslt khsrmhsger pfhcnacgks fvvlsslrkh erthrsnett
      421 gaapqqelvl glalpvgvvg egsaapvaga gigdapagll glppesgsvv atqwqvvgmt
      481 vehvecqdag vgeapstlgd agevggeetd ekppqfvcre cketfstltl lrrhershpe
      541 lrpfpctqcg ksfsdraglr khsrthssvr pyscsqcpka flsasdlrkh erthpvpigt
      601 pipleplval lgmpeegsa
//
LOCUS       NP_001425121             353 aa            linear   ROD 18-APR-2025
DEFINITION  tsukushi precursor [Rattus norvegicus].
ACCESSION   NP_001425121 XP_006229821
VERSION     NP_001425121.1
DBSOURCE    REFSEQ: accession NM_001438192.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Henke,A., Grace,O.C., Ashley,G.R., Stewart,G.D., Riddick,A.C.,
            Yeun,H., O'Donnell,M., Anderson,R.A. and Thomson,A.A.
  TITLE     Stromal expression of decorin, Semaphorin6D, SPARC, Sprouty1 and
            Tsukushi in developing prostate and decreased levels of decorin in
            prostate cancer
  JOURNAL   PLoS One 7 (8), e42516 (2012)
   PUBMED   22880013
  REMARK    GeneRIF: The spatio-temporal expression of Decorin, Semaphorin6D,
            SPARC, Spry-1 and Tsukushi in developing prostate is described and
            observed similar mesenchymal expression patterns in rat and human.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ohta,K., Ito,A., Kuriyama,S., Lupo,G., Kosaka,M., Ohnuma,S.,
            Nakagawa,S. and Tanaka,H.
  TITLE     Tsukushi functions as a Wnt signaling inhibitor by competing with
            Wnt2b for binding to transmembrane protein Frizzled4
  JOURNAL   Proc Natl Acad Sci U S A 108 (36), 14962-14967 (2011)
   PUBMED   21856951
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Ito,A., Shinmyo,Y., Abe,T., Oshima,N., Tanaka,H. and Ohta,K.
  TITLE     Tsukushi is required for anterior commissure formation in mouse
            brain
  JOURNAL   Biochem Biophys Res Commun 402 (4), 813-818 (2010)
   PUBMED   21055390
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Coffy,S., Decaux,J.F., Girard,J., de Keyzer,Y. and Asfari,M.
  TITLE     Identification of a novel rat hepatic gene induced early by
            insulin, independently of glucose
  JOURNAL   Biochem J 385 (Pt 1), 165-171 (2005)
   PUBMED   15344907
  REMARK    GeneRIF: Tissue distribution of EIIH in adult rats revealed a
            pattern of expression mainly in the liver, intestine and islets of
            Langerhans, closely following that of the Glut2 (glucose
            transporter 2), suggesting that it may play a role in carbohydrate
            metabolism
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006229821.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY533242.1, SRR26643287.1664.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..353
                     /product="tsukushi precursor"
                     /note="leucine-rich repeat-containing protein 54; early
                     insulin-induced hepatic gene protein; hepatic protein
                     EIIH; tsukushin"
                     /calculated_mol_wt=36246
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1850
     mat_peptide     18..353
                     /product="Tsukushi. /id=PRO_0000240409"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
                     /calculated_mol_wt=36246
     Region          60..80
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          63..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          <85..>306
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          86..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          111..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          133..154
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          160..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          160..180
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          186..207
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          187..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          208..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..228
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          231..253
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          232..256
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          256..277
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          257..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..302
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QMY6.1)"
     Region          282..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..353
                     /gene="Tsku"
                     /gene_synonym="Eiih"
                     /coded_by="NM_001438192.1:56..1117"
                     /db_xref="GeneID:308843"
                     /db_xref="RGD:1359311"
ORIGIN      
        1 mlctlfllll algtvqttrp cfpgcqceee tfglfdsfsl irvdcsslgp hivpvpipld
       61 tahldlssnr letvnesvlg gpgyttlagl dlshnlltsi tptafsrlry lesldlshng
      121 laalpaevft ssplsdinls hnrlrevsis aftthsqgra lhvdlshnli hrllpypara
      181 slsaptiqsl nlswnrlrav pnlrdlplry lsldgnplat inpgafmgla glthlslasl
      241 qgilqlpphg frelpglqvl dlsgnpklkw agaevfsglg llqeldlsgs slvplpetll
      301 hhlpalqsvs vgqdvqcrrl vregayhrqp gsspkvvlhc gdtqesargp dil
//
LOCUS       NP_001100997            1164 aa            linear   ROD 20-APR-2025
DEFINITION  alpha-mannosidase 2x isoform 4 [Rattus norvegicus].
ACCESSION   NP_001100997 XP_001066272 XP_218816
VERSION     NP_001100997.1
DBSOURCE    REFSEQ: accession NM_001107527.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Akama,T.O., Nakagawa,H., Wong,N.K., Sutton-Smith,M., Dell,A.,
            Morris,H.R., Nakayama,J., Nishimura,S., Pai,A., Moremen,K.W.,
            Marth,J.D. and Fukuda,M.N.
  TITLE     Essential and mutually compensatory roles of {alpha}-mannosidase II
            and {alpha}-mannosidase IIx in N-glycan processing in vivo in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (24), 8983-8988 (2006)
   PUBMED   16754854
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473980.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_218816.4, XP_001066272.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132261, SAMD00132262
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..1164
                     /product="alpha-mannosidase 2x isoform 4"
                     /EC_number="3.2.1.114"
                     /note="alpha-mannosidase 2x; mannosidase 2, alpha 2"
                     /calculated_mol_wt=131830
     Region          140..1163
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     CDS             1..1164
                     /gene="Man2a2"
                     /coded_by="NM_001107527.1:306..3800"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:308757"
                     /db_xref="RGD:1310238"
ORIGIN      
        1 mklkkqvtvc gaaifcvavf slylmldrvq hdparhqngg nfprsqisvl qnrieqleql
       61 leenheiish ikdsvlelta naegppallp yhtangswav lpeprpsffs vspedcqfal
      121 ggrgqkpelq mltvsedlpf dnveggvwrq gfdisyspnd wdaedlqvfv vphshndpgw
      181 iktfdkyyte qtqhilnsmv sklqedprrr flwaevsffa kwwdnisaqk raavrrlvgn
      241 gqleiatggw vmpdeanshy falvdqlieg hqwlernlga tprsgwavdp fghsstmpyl
      301 lrranltsml iqrvhyaikk hfaathslef mwrqtwdsds stdifchmmp fysydvphtc
      361 gpdpkiccqf dfkrlpggri ncpwkvppra iteanvadra allldqyrkk srlfrssvll
      421 vplgddfryd kpqewdaqff nyqrlfdfln skpefhvqaq fgtlseyfda lykrtgvepg
      481 arppgfpvls gdffsyadre dhywtgyyts rpfyksldrv lethlrgaev lyslalahar
      541 rsgltgqypl sdyavltear rtlglfqhhd aitgtakeav vvdygvrllr slvslkqvii
      601 naahylvlgd ketysfdpra pflqmddsrv shdalpertv irldssprfv vvfnpleqer
      661 lsvvsllvns prvrvlseeg qplsvqisvq wssatnmvpd vyqvsvpvrl palglgvlql
      721 qpdldgpytl qssvhvylng vklsvsrqtt fplrvvdsgt sdfaisnrym qvwfsgltgl
      781 lksvrrvdee qeqqvdmklf vygtrtskdk sgaylflpdn eakpyvpkkp pvlrvtegpf
      841 fsevaayyeh fhqvirlynl pgveglsldv sfqvdirdyv nkelalriht didsqgtfft
      901 dlngfqvqpr kylkklplqa nfypmpvmay iqdsqrrltl htaqalgvss lgngqlevil
      961 drrlmqddnr glgqglkdnk itcnhfrlll errtlmspev qqerstsyps llshmtsmyl
     1021 ntpplvlpva krestsptlh sfhplasplp cdfhllnlrm lpaevsvpvr anphhqaedt
     1081 lpaadaalil hrkgfdcgle aknlgfnctt sqgklalgsl fhgldvlflq ptsltllypl
     1141 aspsnstdis lepmeistfr lrlg
//
LOCUS       NP_001414675             287 aa            linear   ROD 20-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF220 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001414675 XP_038967452
VERSION     NP_001414675.1
DBSOURCE    REFSEQ: accession NM_001427746.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Ma,P., Yang,X., Kong,Q., Li,C., Yang,S., Li,Y. and Mao,B.
  TITLE     The ubiquitin ligase RNF220 enhances canonical Wnt signaling
            through USP7-mediated deubiquitination of beta-catenin
  JOURNAL   Mol Cell Biol 34 (23), 4355-4366 (2014)
   PUBMED   25266658
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kong,Q., Zeng,W., Wu,J., Hu,W., Li,C. and Mao,B.
  TITLE     RNF220, an E3 ubiquitin ligase that targets Sin3B for
            ubiquitination
  JOURNAL   Biochem Biophys Res Commun 393 (4), 708-713 (2010)
   PUBMED   20170641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Feb 2, 2024 this sequence version replaced XP_038967452.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.1502743.1,
                                           SRR21887622.3730119.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..287
                     /product="E3 ubiquitin-protein ligase RNF220 isoform 3"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF220"
                     /calculated_mol_wt=32161
     Region          <12..165
                     /region_name="RNF220"
                     /note="E3 ubiquitin-protein ligase RNF220; pfam15926"
                     /db_xref="CDD:464946"
     Region          233..284
                     /region_name="RING-HC_RNF220"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 220 (RNF220) and similar proteins; cd16563"
                     /db_xref="CDD:438225"
     CDS             1..287
                     /gene="Rnf220"
                     /coded_by="NM_001427746.1:1047..1910"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:500532"
                     /db_xref="RGD:1598210"
ORIGIN      
        1 mvqlfvltev wsrigkmkrr kqdegqvcpl csrplagseq emsrhvehcl skregscvae
       61 ddavdiehen snrfeeyewc gqkrirattl leggfrgsgf vmcsgkenpd sdadldvdgd
      121 dtleygkpqy teadvipctg eepgeakere alrgavlngg ppstritpef skwasdemps
      181 tsngesskqe amqktcknsd iekitedsav ttfealkarv relerqlsrg drykclicmd
      241 sysmpltsiq cwhvhceecw lrtlgakklc pqcntitapg dlrriyl
//
LOCUS       NP_001425256             252 aa            linear   ROD 20-APR-2025
DEFINITION  folate receptor beta precursor [Rattus norvegicus].
ACCESSION   NP_001425256 XP_006229920
VERSION     NP_001425256.1
DBSOURCE    REFSEQ: accession NM_001438327.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Pridans,C., Irvine,K.M., Davis,G.M., Lefevre,L., Bush,S.J. and
            Hume,D.A.
  TITLE     Transcriptomic Analysis of Rat Macrophages
  JOURNAL   Front Immunol 11, 594594 (2021)
   PUBMED   33633725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Lu,Y., Parker,N., Kleindl,P.J., Cross,V.A., Wollak,K., Westrick,E.,
            Stinnette,T.W., Gehrke,M.A., Wang,K., Santhapuram,H.K., You,F.,
            Hahn,S.J., Vaughn,J.F., Klein,P.J., Vlahov,I.R., Low,P.S. and
            Leamon,C.P.
  TITLE     Antiinflammatory Activity of a Novel Folic Acid Targeted Conjugate
            of the mTOR Inhibitor Everolimus
  JOURNAL   Mol Med 21 (1), 584-596 (2015)
   PUBMED   26181632
  REMARK    GeneRIF: EC0565 forms micellar aggregates in physiological buffers
            and demonstrates good water solubility as well as strong
            multivalent FR-binding capacity. EC0565 inhibited mTOR signaling in
            rat macrophages at nanomolar concentrations
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Shen,J., Hilgenbrink,A.R., Xia,W., Feng,Y., Dimitrov,D.S.,
            Lockwood,M.B., Amato,R.J. and Low,P.S.
  TITLE     Folate receptor-beta constitutes a marker for human proinflammatory
            monocytes
  JOURNAL   J Leukoc Biol 96 (4), 563-570 (2014)
   PUBMED   25015955
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Watkins,D. and Rosenblatt,D.S.
  TITLE     Update and new concepts in vitamin responsive disorders of folate
            transport and metabolism
  JOURNAL   J Inherit Metab Dis 35 (4), 665-670 (2012)
   PUBMED   22108709
  REMARK    Review article
REFERENCE   5  (residues 1 to 252)
  AUTHORS   van der Heijden,J.W., Oerlemans,R., Dijkmans,B.A., Qi,H., van der
            Laken,C.J., Lems,W.F., Jackman,A.L., Kraan,M.C., Tak,P.P.,
            Ratnam,M. and Jansen,G.
  TITLE     Folate receptor beta as a potential delivery route for novel folate
            antagonists to macrophages in the synovial tissue of rheumatoid
            arthritis patients
  JOURNAL   Arthritis Rheum 60 (1), 12-21 (2009)
   PUBMED   19116913
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Page,S.T., Owen,W.C., Price,K. and Elwood,P.C.
  TITLE     Expression of the human placental folate receptor transcript is
            regulated in human tissues. Organization and full nucleotide
            sequence of the gene
  JOURNAL   J Mol Biol 229 (4), 1175-1183 (1993)
   PUBMED   8445646
  REMARK    Erratum:[J Mol Biol 1994 May 13;238(4):639]
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Antony,A.C., Kane,M.A., Portillo,R.M., Elwood,P.C. and
            Kolhouse,J.F.
  TITLE     Studies of the role of a particulate folate-binding protein in the
            uptake of 5-methyltetrahydrofolate by cultured human KB cells
  JOURNAL   J Biol Chem 260 (28), 14911-14917 (1985)
   PUBMED   4066659
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006229920.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211323.1, FM095247.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840112,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..252
                     /product="folate receptor beta precursor"
                     /note="folate receptor 2 (fetal)"
                     /calculated_mol_wt=26904
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2284
     Region          29..204
                     /region_name="Folate_rec"
                     /note="Folate receptor family; pfam03024"
                     /db_xref="CDD:397250"
     CDS             1..252
                     /gene="Folr2"
                     /coded_by="NM_001438327.1:134..892"
                     /db_xref="GeneID:293154"
                     /db_xref="RGD:1308515"
ORIGIN      
        1 mawkqtplll lvymittcsa rdrtdllnvc mdakhhktkp gpedklhdqc spwkrnaccs
       61 vntsqelhkd nsrlynfnwd hcgemtpack rhfiqdacly ecspnlgpwi qqagqswrke
      121 rfldvplcke dcqewweacr tsftckrdwh kgwdwtsgin kcpdtapcrt fqyyfptpas
      181 lceglwshsy kvsnysrgsg qciqmwfdst qgnpneevvk fyasfmtsgt vyhaaillvp
      241 slapvlslwl pd
//
LOCUS       NP_001425187            1173 aa            linear   ROD 20-APR-2025
DEFINITION  tudor domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425187 XP_063138858
VERSION     NP_001425187.1
DBSOURCE    REFSEQ: accession NM_001438258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Kuramochi-Miyagawa,S., Watanabe,T., Gotoh,K., Takamatsu,K.,
            Chuma,S., Kojima-Kita,K., Shiromoto,Y., Asada,N., Toyoda,A.,
            Fujiyama,A., Totoki,Y., Shibata,T., Kimura,T., Nakatsuji,N.,
            Noce,T., Sasaki,H. and Nakano,T.
  TITLE     MVH in piRNA processing and gene silencing of retrotransposons
  JOURNAL   Genes Dev 24 (9), 887-892 (2010)
   PUBMED   20439430
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Yamaji,M., Tanaka,T., Shigeta,M., Chuma,S., Saga,Y. and Saitou,M.
  TITLE     Functional reconstruction of NANOS3 expression in the germ cell
            lineage by a novel transgenic reporter reveals distinct subcellular
            localizations of NANOS3
  JOURNAL   Reproduction 139 (2), 381-393 (2010)
   PUBMED   19861488
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Shoji,M., Tanaka,T., Hosokawa,M., Reuter,M., Stark,A., Kato,Y.,
            Kondoh,G., Okawa,K., Chujo,T., Suzuki,T., Hata,K., Martin,S.L.,
            Noce,T., Kuramochi-Miyagawa,S., Nakano,T., Sasaki,H., Pillai,R.S.,
            Nakatsuji,N. and Chuma,S.
  TITLE     The TDRD9-MIWI2 complex is essential for piRNA-mediated
            retrotransposon silencing in the mouse male germline
  JOURNAL   Dev Cell 17 (6), 775-787 (2009)
   PUBMED   20059948
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Aravin,A.A., van der Heijden,G.W., Castaneda,J., Vagin,V.V.,
            Hannon,G.J. and Bortvin,A.
  TITLE     Cytoplasmic compartmentalization of the fetal piRNA pathway in mice
  JOURNAL   PLoS Genet 5 (12), e1000764 (2009)
   PUBMED   20011505
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Reuter,M., Chuma,S., Tanaka,T., Franz,T., Stark,A. and Pillai,R.S.
  TITLE     Loss of the Mili-interacting Tudor domain-containing protein-1
            activates transposons and alters the Mili-associated small RNA
            profile
  JOURNAL   Nat Struct Mol Biol 16 (6), 639-646 (2009)
   PUBMED   19465913
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hosokawa,M., Shoji,M., Kitamura,K., Tanaka,T., Noce,T., Chuma,S.
            and Nakatsuji,N.
  TITLE     Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
            composition, intracellular localization, and function in male germ
            cells in mice
  JOURNAL   Dev Biol 301 (1), 38-52 (2007)
   PUBMED   17141210
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hosokawa,M., Kitamura,K., Kasai,S., Fujioka,M.,
            Hiyoshi,M., Takamune,K., Noce,T. and Nakatsuji,N.
  TITLE     Tdrd1/Mtr-1, a tudor-related gene, is essential for male germ-cell
            differentiation and nuage/germinal granule formation in mice
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15894-15899 (2006)
   PUBMED   17038506
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Chuma,S., Hiyoshi,M., Yamamoto,A., Hosokawa,M., Takamune,K. and
            Nakatsuji,N.
  TITLE     Mouse Tudor Repeat-1 (MTR-1) is a novel component of chromatoid
            bodies/nuages in male germ cells and forms a complex with snRNPs
  JOURNAL   Mech Dev 120 (9), 979-990 (2003)
   PUBMED   14550528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063138858.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.9496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1173
                     /product="tudor domain-containing protein 1 isoform 1"
                     /note="tudor domain-containing protein 1"
                     /calculated_mol_wt=129863
     Region          162..198
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          261..390
                     /region_name="Tudor_TDRD1_rpt1"
                     /note="first Tudor domain found in Tudor domain-containing
                     protein 1 (TDRD1) and similar proteins; cd20408"
                     /db_xref="CDD:410479"
     Site            order(317,324,342,345,347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410479"
     Region          511..592
                     /region_name="Tudor_TDRD1_rpt2"
                     /note="second Tudor domain found in Tudor
                     domain-containing protein 1 (TDRD1) and similar proteins;
                     cd20409"
                     /db_xref="CDD:410480"
     Site            order(546,553,570,573,575)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410480"
     Region          708..824
                     /region_name="TUDOR"
                     /note="Tudor domain; pfam00567"
                     /db_xref="CDD:425754"
     Region          937..1052
                     /region_name="Tudor_SF"
                     /note="Tudor domain superfamily; cl02573"
                     /db_xref="CDD:470623"
     Site            order(994,999,1001,1017,1020,1022)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410449"
     CDS             1..1173
                     /gene="Tdrd1"
                     /coded_by="NM_001438258.1:149..3670"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:292129"
                     /db_xref="RGD:1306140"
ORIGIN      
        1 mmprnnleas tckmaepfnf ekkesklpph dslrspvpqh nhpnfrlksp engnkknnfl
       61 lceqnkqyla sqednsvvss npagingevg gskgdrktlp tgnpvslslg nnsppnqvkt
      121 kpsnavtpek skkshklfen alsvnnpalf nslgpplrst tchrcglfgs lrcsqckqty
      181 ycstacqrrd wsshsticrp vqqslhkled nkspfetkti dvknevacpl gvtkemtaga
      241 ervmfsdlrs lqlrksmeik gtvtefkhpg hfyvqlysse vleymnqlsa slketyanmv
      301 pedgylpvkg evcvakytvd qtwnravveg vdvlqkkahv lyidygneei ipvdrihqls
      361 rsislfppsa ikcyvsgvvp aagewtedcv vavkallfeq ycsikvvdis eeegltcavd
      421 vvlqssgkql dhvlvemgyg vkpdepsskk qsmdpgtsed tgrltaenri gaernalvpt
      481 vltlnvgdef cgvvahiqtp edffcqqlqs ghklaelqes lseycshvtp rsdfyptigd
      541 mccaqfsedd qwyrasvlay aseesvlvgy vdygnfeils lkrlcpiipk lldlpmqaln
      601 cvlagvkpsl gmwtpeaicv mrkavqnrmv tvrvvgmqgt ralvelvdks vaphlsaska
      661 lldsgfaiee kdivadkgss arasnvplav egavevlewt wveftvdetv dvmvcmmhsp
      721 gefychclkd dalkklddln ksladycaqk ppngfkaevg rpccacfagd gnwyralvke
      781 ilpsgnvkvh fvdygnveev ttdqlhaiap qflllpfqgm qcwlvdiqpk nkhwtkeata
      841 rfqacvvglk lqarvveite ngvgveltdl stpypkiisd vlitehlvlr cgspqkdelm
      901 srpankhnqi dsqsvqaspp aeqwktielp vnktvpanvl eiisptlfya ipsempenqe
      961 klcvltaell ehcnaqkgqp pyrprtgeac cakytnddfw yraivleasd sdvkvlyady
     1021 gnverlpfsr vqpitashlq lpfriircsl egltelngss sqpvmellrn amlnqsvals
     1081 vkavsknvha vsvekcseng miniaenlvm cglaenlssk resastketp hstdccctel
     1141 qkqiekheqi llfllnnptn qnkfiemkkl lqs
//
LOCUS       NP_001102742             104 aa            linear   ROD 20-APR-2025
DEFINITION  ciliogenesis and planar polarity effector 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001102742 XP_001072545 XP_575943
VERSION     NP_001102742.1
DBSOURCE    REFSEQ: accession NM_001109272.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_575943.1, XP_001072545.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132273,
                              SAMD00132297 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..104
                     /product="ciliogenesis and planar polarity effector 2
                     isoform 2"
                     /note="REM2 and RAB-like small GTPase 1; ciliogenesis and
                     planar polarity effector 2"
                     /calculated_mol_wt=11768
     CDS             1..104
                     /gene="Cplane2"
                     /gene_synonym="RGD1561421; Rsg1"
                     /coded_by="NM_001109272.1:137..451"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500576"
                     /db_xref="RGD:1561421"
ORIGIN      
        1 marlpmhgsv ivpdwhetve gkeylacilr knrrrefans anrarnmeta hpcqqqlspe
       61 mlltesslrv mpsaghfaqq pcnrvslciq ysllciqyll crpg
//
LOCUS       NP_001425192             388 aa            linear   ROD 20-APR-2025
DEFINITION  beta-1,4-galactosyltransferase 5 [Rattus norvegicus].
ACCESSION   NP_001425192
VERSION     NP_001425192.1
DBSOURCE    REFSEQ: accession NM_001438263.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Yoshihara,T., Satake,H., Nishie,T., Okino,N., Hatta,T., Otani,H.,
            Naruse,C., Suzuki,H., Sugihara,K., Kamimura,E., Tokuda,N.,
            Furukawa,K., Fururkawa,K., Ito,M. and Asano,M.
  TITLE     Lactosylceramide synthases encoded by B4galt5 and 6 genes are
            pivotal for neuronal generation and myelin formation in mice
  JOURNAL   PLoS Genet 14 (8), e1007545 (2018)
   PUBMED   30114188
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Zhang,L., Ren,J., Shi,P., Lu,D., Zhao,C., Su,Y., Zhang,L. and
            Huang,J.
  TITLE     The Immunological Regulation Roles of Porcine beta-1, 4
            Galactosyltransferase V (B4GALT5) in PRRSV Infection
  JOURNAL   Front Cell Infect Microbiol 8, 48 (2018)
   PUBMED   29546034
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Li,S.F., Zhu,C.S., Wang,Y.M., Xie,X.X., Xiao,L.L., Zhang,Z.C.,
            Tang,Q.Q. and Li,X.
  TITLE     Downregulation of beta1,4-galactosyltransferase 5 improves insulin
            resistance by promoting adipocyte commitment and reducing
            inflammation
  JOURNAL   Cell Death Dis 9 (2), 196 (2018)
   PUBMED   29415997
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Mayo,L., Trauger,S.A., Blain,M., Nadeau,M., Patel,B., Alvarez,J.I.,
            Mascanfroni,I.D., Yeste,A., Kivisakk,P., Kallas,K., Ellezam,B.,
            Bakshi,R., Prat,A., Antel,J.P., Weiner,H.L. and Quintana,F.J.
  TITLE     Regulation of astrocyte activation by glycolipids drives chronic
            CNS inflammation
  JOURNAL   Nat Med 20 (10), 1147-1156 (2014)
   PUBMED   25216636
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Yamaji,T. and Hanada,K.
  TITLE     Establishment of HeLa cell mutants deficient in
            sphingolipid-related genes using TALENs
  JOURNAL   PLoS One 9 (2), e88124 (2014)
   PUBMED   24498430
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Nishie,T., Hikimochi,Y., Zama,K., Fukusumi,Y., Ito,M., Yokoyama,H.,
            Naruse,C., Ito,M. and Asano,M.
  TITLE     Beta4-galactosyltransferase-5 is a lactosylceramide synthase
            essential for mouse extra-embryonic development
  JOURNAL   Glycobiology 20 (10), 1311-1322 (2010)
   PUBMED   20574042
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Wei,Y., Zhou,F., Ge,Y., Chen,H., Cui,C., Li,Q., Liu,D., Yang,Z.,
            Wu,G., Sun,S., Gu,J. and Jiang,J.
  TITLE     Beta1,4-galactosyltransferase V regulates self-renewal of
            glioma-initiating cell
  JOURNAL   Biochem Biophys Res Commun 396 (3), 602-607 (2010)
   PUBMED   20417617
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Yan,M., Cheng,C., Ding,F., Jiang,J., Gao,L., Xia,C. and Shen,A.
  TITLE     The expression patterns of beta1,4 galactosyltransferase I and V
            mRNAs, and Galbeta1-4GlcNAc group in rat gastrocnemius muscles post
            sciatic nerve injury
  JOURNAL   Glycoconj J 25 (7), 685-701 (2008)
   PUBMED   18512149
  REMARK    GeneRIF: These results indicated that the expressions of
            beta1,4-GalT I, V mRNAs and Galbeta1-4GlcNAc group were involved in
            the process of denervation and reinnervation.
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Yan,M., Cheng,C., Shao,X., Qian,J., Shen,A. and Xia,C.
  TITLE     Expression change of beta-1,4 galactosyltransferase I, V mRNAs and
            Galbeta1,4GlcNAc group in rat sciatic nerve after crush
  JOURNAL   J Mol Histol 39 (3), 317-328 (2008)
   PUBMED   18320333
  REMARK    GeneRIF: beta1,4-GalT I and V might play important roles in the
            regeneration of the injured sciatic nerve.
            Erratum:[J Mol Histol. 2008 Aug;39(4):469. Xia, Chun [corrected to
            Xia, Chunlin]]
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Yan,M., Xia,C., Niu,S., Shao,X., Cheng,C., Zhao,J. and Shen,A.
  TITLE     The role of TNF-alpha and its receptors in the production of
            beta-1,4 galactosyltransferase I and V mRNAs by rat primary
            astrocytes
  JOURNAL   J Mol Neurosci 33 (2), 155-162 (2007)
   PUBMED   17917074
  REMARK    GeneRIF: These results suggest that an autocrine loop involving
            TNF-alpha, TNFR1 and TNFR2 contributes to the production of
            beta-1,4-GalT I and V mRNA in response to inflammation.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.14680.1,
                                           SRR26643298.20390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760494,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..388
                     /product="beta-1,4-galactosyltransferase 5"
                     /EC_number="2.4.1.38"
                     /note="UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase,
                     polypeptide 5"
                     /calculated_mol_wt=44773
     Region          161..377
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(169,171,173,208,234..236)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(234,236,329)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..388
                     /gene="B4galt5"
                     /coded_by="NM_001438263.1:145..1311"
                     /db_xref="GeneID:362275"
                     /db_xref="RGD:1310062"
ORIGIN      
        1 mrarrgllrl prrsllaalf ffslssslly fvyvapgivn tylfmvqaqg illrdnvrti
       61 gaqvyeqvvr sayakrnssl ndsdypldln hseafppttt flpedftyfa nhpcperlps
      121 mkgpidinms eirmddihel fsrdpairlg ghwkpadcmp rwkvailipf rnrhehlpvl
      181 lrhllpmlqr qrlqfafyvi eqagtqpfnr amlfnvgfqe amkdldwdcl ifhdvdhipe
      241 sdrnyygcgq mprhfatkld kymyllpyte ffggvsgltv eqfrkingfp nafwgwgged
      301 ddlwnrvqna gysvsrpegd tgkyksiphh hrgevqflgr yallrksker qgldglnnls
      361 ysanvtydal yknitvnltp elaqvtey
//
LOCUS       NP_001425220             281 aa            linear   ROD 20-APR-2025
DEFINITION  U1 small nuclear ribonucleoprotein A [Rattus norvegicus].
ACCESSION   NP_001425220 XP_006228626
VERSION     NP_001425220.1
DBSOURCE    REFSEQ: accession NM_001438291.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kondo,Y., Oubridge,C., van Roon,A.M. and Nagai,K.
  TITLE     Crystal structure of human U1 snRNP, a small nuclear
            ribonucleoprotein particle, reveals the mechanism of 5' splice site
            recognition
  JOURNAL   Elife 4, e04986 (2015)
   PUBMED   25555158
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Bai,B., Hales,C.M., Chen,P.C., Gozal,Y., Dammer,E.B., Fritz,J.J.,
            Wang,X., Xia,Q., Duong,D.M., Street,C., Cantero,G., Cheng,D.,
            Jones,D.R., Wu,Z., Li,Y., Diner,I., Heilman,C.J., Rees,H.D., Wu,H.,
            Lin,L., Szulwach,K.E., Gearing,M., Mufson,E.J., Bennett,D.A.,
            Montine,T.J., Seyfried,N.T., Wingo,T.S., Sun,Y.E., Jin,P.,
            Hanfelt,J., Willcock,D.M., Levey,A., Lah,J.J. and Peng,J.
  TITLE     U1 small nuclear ribonucleoprotein complex and RNA splicing
            alterations in Alzheimer's disease
  JOURNAL   Proc Natl Acad Sci U S A 110 (41), 16562-16567 (2013)
   PUBMED   24023061
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Pabis,M., Neufeld,N., Steiner,M.C., Bojic,T., Shav-Tal,Y. and
            Neugebauer,K.M.
  TITLE     The nuclear cap-binding complex interacts with the U4/U6.U5
            tri-snRNP and promotes spliceosome assembly in mammalian cells
  JOURNAL   RNA 19 (8), 1054-1063 (2013)
   PUBMED   23793891
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Zhang,L., Li,X. and Zhao,R.
  TITLE     Structural analyses of the pre-mRNA splicing machinery
  JOURNAL   Protein Sci 22 (6), 677-692 (2013)
   PUBMED   23592432
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Novakova,Z., Man,P., Novak,P., Hozak,P. and Hodny,Z.
  TITLE     Separation of nuclear protein complexes by blue native
            polyacrylamide gel electrophoresis
  JOURNAL   Electrophoresis 27 (7), 1277-1287 (2006)
   PUBMED   16502463
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Sinha,K., Perumal,K., Chen,Y. and Reddy,R.
  TITLE     Post-transcriptional adenylation of signal recognition particle RNA
            is carried out by an enzyme different from mRNA Poly(A) polymerase
  JOURNAL   J Biol Chem 274 (43), 30826-30831 (1999)
   PUBMED   10521474
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Nagai,K., Oubridge,C., Jessen,T.H., Li,J. and Evans,P.R.
  TITLE     Crystal structure of the RNA-binding domain of the U1 small nuclear
            ribonucleoprotein A
  JOURNAL   Nature 348 (6301), 515-520 (1990)
   PUBMED   2147232
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Craft,J., Mimori,T., Olsen,T.L. and Hardin,J.A.
  TITLE     The U2 small nuclear ribonucleoprotein particle as an autoantigen.
            Analysis with sera from patients with overlap syndromes
  JOURNAL   J Clin Invest 81 (6), 1716-1724 (1988)
   PUBMED   2968364
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228626.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.335535.1,
                                           SRR26643299.1724.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840107,
                                           SAMN12840110 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..281
                     /product="U1 small nuclear ribonucleoprotein A"
                     /calculated_mol_wt=31045
     Region          7..95
                     /region_name="RRM1_U1A"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1A); cd12477"
                     /db_xref="CDD:409906"
     Region          <12..>207
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Site            order(13,15..16,19,44,46,48..54,56,80,83,85..92)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409906"
     Region          196..281
                     /region_name="RRM2_U1A"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A
                     or U1A); cd12480"
                     /db_xref="CDD:409908"
     CDS             1..281
                     /gene="Snrpa"
                     /coded_by="NM_001438291.1:198..1043"
                     /db_xref="GeneID:292729"
                     /db_xref="RGD:1307416"
ORIGIN      
        1 mavpetrpnh tiyinnlnek ikkdelkksl yaifsqfgqi ldilvsrslk mrgqafvifk
       61 evssatnalr smqgfpfydk pmriqyaktd sdiiakmkgt fverdrkrek rkpksqetpa
      121 akkavqggaa apvvgavqpv pgmppmtqap rimhhmpgqp pympppgmip ppglapgqip
      181 pgamppqqlm pgqmppaqpl senppnhilf ltnlpeetne lmlsmlfnqf pgfkevrlvp
      241 grhdiafvef dnevqagaar dalqgfkitq nnamkisfak k
//
LOCUS       NP_001425180             700 aa            linear   ROD 20-APR-2025
DEFINITION  methionine synthase reductase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425180 XP_006227875
VERSION     NP_001425180.1
DBSOURCE    REFSEQ: accession NM_001438251.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Cheng,H., Li,H., Bu,Z., Zhang,Q., Bai,B., Zhao,H., Li,R.K.,
            Zhang,T. and Xie,J.
  TITLE     Functional variant in methionine synthase reductase intron-1 is
            associated with pleiotropic congenital malformations
  JOURNAL   Mol Cell Biochem 407 (1-2), 51-56 (2015)
   PUBMED   26045171
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Gherasim,C., Yadav,P.K., Kabil,O., Niu,W.N. and Banerjee,R.
  TITLE     Nitrite reductase activity and inhibition of HS biogenesis by human
            cystathionine ss-synthase
  JOURNAL   PLoS One 9 (1), e85544 (2014)
   PUBMED   24416422
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Padmanabhan,N., Jia,D., Geary-Joo,C., Wu,X., Ferguson-Smith,A.C.,
            Fung,E., Bieda,M.C., Snyder,F.F., Gravel,R.A., Cross,J.C. and
            Watson,E.D.
  TITLE     Mutation in folate metabolism causes epigenetic instability and
            transgenerational effects on development
  JOURNAL   Cell 155 (1), 81-93 (2013)
   PUBMED   24074862
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Lautner-Csorba,O., Gezsi,A., Erdelyi,D.J., Hullam,G., Antal,P.,
            Semsei,A.F., Kutszegi,N., Kovacs,G., Falus,A. and Szalai,C.
  TITLE     Roles of genetic polymorphisms in the folate pathway in childhood
            acute lymphoblastic leukemia evaluated by Bayesian relevance and
            effect size analysis
  JOURNAL   PLoS One 8 (8), e69843 (2013)
   PUBMED   23940529
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Zhao,J.Y., Yang,X.Y., Gong,X.H., Gu,Z.Y., Duan,W.Y., Wang,J.,
            Ye,Z.Z., Shen,H.B., Shi,K.H., Hou,J., Huang,G.Y., Jin,L., Qiao,B.
            and Wang,H.Y.
  TITLE     Functional variant in methionine synthase reductase intron-1
            significantly increases the risk of congenital heart disease in the
            Han Chinese population
  JOURNAL   Circulation 125 (3), 482-490 (2012)
   PUBMED   22179537
REFERENCE   6  (residues 1 to 700)
  AUTHORS   Gemmati,D., Ongaro,A., Scapoli,G.L., Della Porta,M., Tognazzo,S.,
            Serino,M.L., Di Bona,E., Rodeghiero,F., Gilli,G., Reverberi,R.,
            Caruso,A., Pasello,M., Pellati,A. and De Mattei,M.
  TITLE     Common gene polymorphisms in the metabolic folate and methylation
            pathway and the risk of acute lymphoblastic leukemia and
            non-Hodgkin's lymphoma in adults
  JOURNAL   Cancer Epidemiol Biomarkers Prev 13 (5), 787-794 (2004)
   PUBMED   15159311
REFERENCE   7  (residues 1 to 700)
  AUTHORS   Gueant-Rodriguez,R.M., Rendeli,C., Namour,B., Venuti,L., Romano,A.,
            Anello,G., Bosco,P., Debard,R., Gerard,P., Viola,M., Salvaggio,E.
            and Gueant,J.L.
  TITLE     Transcobalamin and methionine synthase reductase mutated
            polymorphisms aggravate the risk of neural tube defects in humans
  JOURNAL   Neurosci Lett 344 (3), 189-192 (2003)
   PUBMED   12812837
REFERENCE   8  (residues 1 to 700)
  AUTHORS   Pietrzyk,J.J., Bik-Multanowski,M., Sanak,M. and Twardowska,M.
  TITLE     Polymorphisms of the 5,10-methylenetetrahydrofolate and the
            methionine synthase reductase genes as independent risk factors for
            spina bifida
  JOURNAL   J Appl Genet 44 (1), 111-113 (2003)
   PUBMED   12590188
REFERENCE   9  (residues 1 to 700)
  AUTHORS   Doolin,M.T., Barbaux,S., McDonnell,M., Hoess,K., Whitehead,A.S. and
            Mitchell,L.E.
  TITLE     Maternal genetic effects, exerted by genes involved in homocysteine
            remethylation, influence the risk of spina bifida
  JOURNAL   Am J Hum Genet 71 (5), 1222-1226 (2002)
   PUBMED   12375236
REFERENCE   10 (residues 1 to 700)
  AUTHORS   Olteanu,H. and Banerjee,R.
  TITLE     Human methionine synthase reductase, a soluble P-450 reductase-like
            dual flavoprotein, is sufficient for NADPH-dependent methionine
            synthase activation
  JOURNAL   J Biol Chem 276 (38), 35558-35563 (2001)
   PUBMED   11466310
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006227875.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.433.1, SRR26643298.569.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..700
                     /product="methionine synthase reductase isoform 1"
                     /EC_number="1.16.1.8"
                     /note="methionine synthase reductase; aqCbl reductase;
                     aquacobalamin reductase"
                     /calculated_mol_wt=77894
     Region          6..142
                     /region_name="Flavodoxin_1"
                     /note="pfam00258"
                     /db_xref="CDD:425562"
     Region          168..247
                     /region_name="Hinge. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498R1.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBK8; propagated from
                     UniProtKB/Swiss-Prot (Q498R1.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBK8; propagated from
                     UniProtKB/Swiss-Prot (Q498R1.2)"
     Region          278..699
                     /region_name="methionine_synthase_red"
                     /note="Human methionine synthase reductase (MSR) restores
                     methionine sythase which is responsible for the
                     regeneration of methionine from homocysteine, as well as
                     the coversion of methyltetrahydrofolate to
                     tetrahydrofolate. In MSR, electrons are transferred...;
                     cd06203"
                     /db_xref="CDD:99800"
     Site            order(452..455,470..471,488..491,526,699)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(452,454..455)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(455,652,697,699)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:99800"
     Site            order(472..475,546,548,581..582,611..612,626,628,658)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99800"
     Site            order(488,491,494)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99800"
     Site            order(543,547..550,552)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99800"
     CDS             1..700
                     /gene="Mtrr"
                     /gene_synonym="MSR"
                     /coded_by="NM_001438251.1:86..2188"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290947"
                     /db_xref="RGD:1308671"
ORIGIN      
        1 mrrflllyat qrgqakaiae eiseqalshg fsadlhcvse sekydlktet gplvmvvstt
       61 gtgdppdtar kfvkeihnkt lptdffahlw ygllglgdse ytyfcnggkv idkrlqelga
      121 qhfydtghad dcvglelvve pwidglwpal tkhfkslggq edmsdsdtla qasdaplsma
      181 mkpellhiqs qvellsledv gkrdselqeq netnknqpsr iedfdsslvn svpplsqssl
      241 sipavspeyl evylqeslgq denqasvpps vdpifqvpis kavelttnda ikttllleld
      301 iskvefshqp gdsfnvicpn sgsevedllq rlqladkqah rvilkikmdt kkkgaslpqh
      361 vpegsslqfi ftwcleirav pkkaflrals dytsdatekr rlqelcskqg aadynrfird
      421 asvclldlll tfpscqppln lllehlpklq prpyscasss llhpdklhfv fnivelpsnt
      481 taaslrkgvc tgwlatlvap flqpntevlt adhsdalape ilispratns fhlpddlsap
      541 iimvgpgtgv apfvgflqhr eklqeqhpdg nfgamwlffg crhkdrdylf reelrhflkt
      601 gvlthlkvsf srdaapeeee eapakyvqdn lqhhsqqvar tllqengyiy vcgdaknmak
      661 dvhdalveii skeagvdkle amktlatlkq ekrylqdiws
//
LOCUS       NP_001425243             594 aa            linear   ROD 20-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001425243 XP_008757732
VERSION     NP_001425243.1
DBSOURCE    REFSEQ: accession NM_001438314.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Xuan,F., Ren,Y., Lu,J., Zhou,W., Jin,R., Chen,A. and Ye,Y.
  TITLE     CPEB1 induces autophagy and promotes apoptosis in ovarian granulosa
            cells of polycystic ovary syndrome
  JOURNAL   Mol Reprod Dev 91 (4), e23741 (2024)
   PUBMED   38616716
  REMARK    GeneRIF: CPEB1 induces autophagy and promotes apoptosis in ovarian
            granulosa cells of polycystic ovary syndrome.
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Takahashi,K., Yi,H., Gu,J., Ikegami,D., Liu,S., Iida,T.,
            Kashiwagi,Y., Dong,C., Kunisawa,T. and Hao,S.
  TITLE     The mitochondrial calcium uniporter contributes to morphine
            tolerance through pCREB and CPEB1 in rat spinal cord dorsal horn
  JOURNAL   Br J Anaesth 123 (2), e226-e238 (2019)
   PUBMED   31253357
  REMARK    GeneRIF: Cytoplasmic polyadenylation element-binding proteins
            (CPEB) are mRNA-binding proteins associated with protein
            translation that play an important role in development, health, and
            disease.
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Shin,J., Paek,K.Y., Ivshina,M., Stackpole,E.E. and Richter,J.D.
  TITLE     Essential role for non-canonical poly(A) polymerase GLD4 in
            cytoplasmic polyadenylation and carbohydrate metabolism
  JOURNAL   Nucleic Acids Res 45 (11), 6793-6804 (2017)
   PUBMED   28383716
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Kim,K.C., Kim,J.W., Choi,C.S., Han,S.Y., Cheong,J.H., Han,S.H.,
            Yang,S.I., Bahn,G.H. and Shin,C.Y.
  TITLE     A role of CPEB1 in the modulation of proliferation and neuronal
            maturation of rat primary neural progenitor cells
  JOURNAL   Neurochem Res 38 (9), 1960-1972 (2013)
   PUBMED   23824559
  REMARK    GeneRIF: Increased NPCs proliferation by down-regulation of CPEB1
            resulted in eventual up-regulation of neuronal differentiation with
            increase in both pre- and post-synaptic proteins
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Alarcon,J.M., Hodgman,R., Theis,M., Huang,Y.S., Kandel,E.R. and
            Richter,J.D.
  TITLE     Selective modulation of some forms of schaffer collateral-CA1
            synaptic plasticity in mice with a disruption of the CPEB-1 gene
  JOURNAL   Learn Mem 11 (3), 318-327 (2004)
   PUBMED   15169862
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Tay,J., Hodgman,R., Sarkissian,M. and Richter,J.D.
  TITLE     Regulated CPEB phosphorylation during meiotic progression suggests
            a mechanism for temporal control of maternal mRNA translation
  JOURNAL   Genes Dev 17 (12), 1457-1462 (2003)
   PUBMED   12815066
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Huang,Y.S., Carson,J.H., Barbarese,E. and Richter,J.D.
  TITLE     Facilitation of dendritic mRNA transport by CPEB
  JOURNAL   Genes Dev 17 (5), 638-653 (2003)
   PUBMED   12629046
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Tay,J. and Richter,J.D.
  TITLE     Germ cell differentiation and synaptonemal complex formation are
            disrupted in CPEB knockout mice
  JOURNAL   Dev Cell 1 (2), 201-213 (2001)
   PUBMED   11702780
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Wu,L., Wells,D., Tay,J., Mendis,D., Abbott,M.A., Barnitt,A.,
            Quinlan,E., Heynen,A., Fallon,J.R. and Richter,J.D.
  TITLE     CPEB-mediated cytoplasmic polyadenylation and the regulation of
            experience-dependent translation of alpha-CaMKII mRNA at synapses
  JOURNAL   Neuron 21 (5), 1129-1139 (1998)
   PUBMED   9856468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_008757732.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3956.1,
                                           SRR26360176.473174.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..594
                     /product="cytoplasmic polyadenylation element-binding
                     protein 1 isoform 1"
                     /note="CPEB; CPEB-1; CPE-BP1; CPE-binding protein 1"
                     /calculated_mol_wt=65546
     Region          42..344
                     /region_name="CEBP1_N"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     1 N-terminus; pfam16368"
                     /db_xref="CDD:465107"
     Region          346..448
                     /region_name="RRM1_CPEB1"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12723"
                     /db_xref="CDD:410122"
     Region          459..542
                     /region_name="RRM2_CPEB1"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein 1 (CPEB-1) and
                     similar proteins; cd12725"
                     /db_xref="CDD:410124"
     Region          536..591
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..594
                     /gene="Cpeb1"
                     /coded_by="NM_001438314.1:652..2436"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293056"
                     /db_xref="RGD:1310421"
ORIGIN      
        1 maplklsira pragralsep gevtwlhtfd cfwspspegg pdqeeesgri kdcwdnqevp
       61 alstcsnani frrinaildd sldfskvctt pinrgihdql pdfqdseeai tsrmlfptsa
      121 qesprglpda nglclglqsl sltgwdrpws tqdsdssaqs ntqsvlsmlq nplgnvlgkt
      181 plsflsldpl gsdldkfpap svrgsrldtr pildsrsssp sdsdtsgfss gsdhlsdlis
      241 slrispplpf lsmtgngprd plkmgvgsrm dqeqaalaav apsptsapkr wpgtsvwpsw
      301 dllgapkdpf sierearlhr qaaavneatc twsgqlpprn yknpiysckv flggvpwdit
      361 eaglvntfrv fgslsvewpg kdgkhprcpp kgyvylvfel eksvrallqa cshdplspdg
      421 lseyyfkmss rrmrckevqv ipwvladsnf vwspsqrldp srtvfvgalh gmlnaealaa
      481 ilndlfggvv yagidtdkhk ypigsgrvtf nnqrsylkav taafveiktt kftkkvqidp
      541 yledslclic ssqpgpffcr dqvcfkyfcr scwhwrhsme glrhhsplmr nqkn
//
LOCUS       NP_001425232             592 aa            linear   ROD 20-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF220 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425232 XP_017449286
VERSION     NP_001425232.1
DBSOURCE    REFSEQ: accession NM_001438303.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Ma,P., Yang,X., Kong,Q., Li,C., Yang,S., Li,Y. and Mao,B.
  TITLE     The ubiquitin ligase RNF220 enhances canonical Wnt signaling
            through USP7-mediated deubiquitination of beta-catenin
  JOURNAL   Mol Cell Biol 34 (23), 4355-4366 (2014)
   PUBMED   25266658
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Kong,Q., Zeng,W., Wu,J., Hu,W., Li,C. and Mao,B.
  TITLE     RNF220, an E3 ubiquitin ligase that targets Sin3B for
            ubiquitination
  JOURNAL   Biochem Biophys Res Commun 393 (4), 708-713 (2010)
   PUBMED   20170641
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 17, 2025 this sequence version replaced XP_017449286.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.28541.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..592
                     /product="E3 ubiquitin-protein ligase RNF220 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF220"
                     /calculated_mol_wt=65469
     Region          217..470
                     /region_name="RNF220"
                     /note="E3 ubiquitin-protein ligase RNF220; pfam15926"
                     /db_xref="CDD:464946"
     Region          538..589
                     /region_name="RING-HC_RNF220"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 220 (RNF220) and similar proteins; cd16563"
                     /db_xref="CDD:438225"
     CDS             1..592
                     /gene="Rnf220"
                     /coded_by="NM_001438303.1:464..2242"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:500532"
                     /db_xref="RGD:1598210"
ORIGIN      
        1 mdlhraafkm enssylpnpl aspalmvlas taeasrdasi pcqqprpfgv pvsvdkdvhi
       61 pftngsytfa smyhrqggvp gtfanrdfpp sllhlhpqfa ppnldctpis mlnhsgvgaf
      121 rpfastedre syqsaftpak rlknchdses phlrfsdadg keydfgtqlp ssspgslkvd
      181 dtgkkifavs glisdretss spedrndrck kkavalfdsq apicpicqvl lrpselqehm
      241 eqeleqlaql pasknsllkd amapgtpksl llsasikreg dsptasphss atedlhhsdr
      301 yqtflrvran rqtrlnarig kmkrrkqdeg qvcplcsrpl agseqemsrh vehclskreg
      361 scvaeddavd iehensnrfe eyewcgqkri rattlleggf rgsgfvmcsg kenpdsdadl
      421 dvdgddtley gkpqyteadv ipctgeepge akerealrga vlnggppstr itpefskwas
      481 dempstsnge sskqeamqkt cknsdiekit edsavttfea lkarvreler qlsrgdrykc
      541 licmdsysmp ltsiqcwhvh ceecwlrtlg akklcpqcnt itapgdlrri yl
//
LOCUS       NP_001425199             497 aa            linear   ROD 20-APR-2025
DEFINITION  flt3-interacting zinc finger protein 1 [Rattus norvegicus].
ACCESSION   NP_001425199 XP_006228315
VERSION     NP_001425199.1
DBSOURCE    REFSEQ: accession NM_001438270.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Tsuruyama,T., Imai,Y., Takeuchi,H., Hiratsuka,T., Maruyama,Y.,
            Kanaya,K., Kaszynski,R., Jin,G., Okuno,T., Ozeki,M., Nakamura,T.,
            Takakuwa,T., Manabe,T., Tamaki,K. and Hiai,H.
  TITLE     Dual retrovirus integration tagging: identification of new
            signaling molecules Fiz1 and Hipk2 that are involved in the IL-7
            signaling pathway in B lymphoblastic lymphomas
  JOURNAL   J Leukoc Biol 88 (1), 107-116 (2010)
   PUBMED   20360400
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Wolf,I. and Rohrschneider,L.R.
  TITLE     Fiz1, a novel zinc finger protein interacting with the receptor
            tyrosine kinase Flt3
  JOURNAL   J Biol Chem 274 (30), 21478-21484 (1999)
   PUBMED   10409713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224110.1, FQ224124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..497
                     /product="flt3-interacting zinc finger protein 1"
                     /note="Flt3 interacting zinc finger protein 1"
                     /calculated_mol_wt=52263
     Region          26..48
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          28..48
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          40..65
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          56..76
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(61,63,65,67..68,71..72,75,89,91,95..96,99..100,103,
                     117,119,121,123..124,127..128)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          68..91
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          84..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          112..130
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          203..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(208,210,212,214..215,218..219,222,236,238..240,
                     242..243,247,250)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(422,424,426,428..429,432..433,436,450,452,456..457,
                     460..461,464,478,480,482,484..485,488..489,492)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..454
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          471..493
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          473..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..497
                     /gene="Fiz1"
                     /gene_synonym="RGD1306359"
                     /coded_by="NM_001438270.1:88..1581"
                     /db_xref="GeneID:292584"
                     /db_xref="RGD:1306359"
ORIGIN      
        1 mddpslpvvp aapgpapsat aprvpfhcse cgksfryrsd lrrhfarhta lkphacprcg
       61 kgfkhsfnla nhlrshtger pyrcsacpkg frdstgllhh qvvhtgekpy cclvcelrfs
      121 srsslgrhlk rqhrgtlpsp lqpspglppl sspcsvccnv gpcsvcgggg sgggeglega
      181 gatswglaea aaaaaaslpp facgacarrf dhgrelaahw aahtdvkpfk cprcerdfna
      241 pallerhklt hdlqgssapp tqvwasggap evagegdtae vgatpptwda glllsptgag
      301 vpkleallpe degagnaqap aaaaeassed tlyqcdcgtf fasapalash leahsgpaty
      361 gcghcgalya alaaleehrr ashgkgsgea apdgegeqva ggpgpgsssr gkkifgcsec
      421 eklfrsprdl erhvlvhtge kpfpclecgk ffrhecylkr hrllhgterp fpchicgkgf
      481 itlsnlsrhl klhrgmd
//
LOCUS       NP_001014089             593 aa            linear   ROD 20-APR-2025
DEFINITION  coiled-coil domain-containing protein 17 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001014089 XP_233417
VERSION     NP_001014089.2
DBSOURCE    REFSEQ: accession NM_001014067.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Kang,B.W., Jeon,H.S., Chae,Y.S., Lee,S.J., Park,J.S., Choi,G.S. and
            Kim,J.G.
  TITLE     Impact of Genetic Variation in MicroRNA-binding Site on
            Susceptibility to Colorectal Cancer
  JOURNAL   Anticancer Res 36 (7), 3353-3361 (2016)
   PUBMED   27354594
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Shultz,M.A., Zhang,L., Gu,Y.Z., Baker,G.L., Fannuchi,M.V.,
            Padua,A.M., Gurske,W.A., Morin,D., Penn,S.G., Jovanovich,S.B.,
            Plopper,C.G. and Buckpitt,A.R.
  TITLE     Gene expression analysis in response to lung toxicants: I.
            Sequencing and microarray development
  JOURNAL   Am J Respir Cell Mol Biol 30 (3), 296-310 (2004)
   PUBMED   12947022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Feb 9, 2008 this sequence version replaced NP_001014089.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1123122.1,
                                           SRR22582419.1266388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..593
                     /product="coiled-coil domain-containing protein 17 isoform
                     1"
                     /note="coiled-coil domain-containing protein 17"
                     /calculated_mol_wt=65728
     Region          <38..>271
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     CDS             1..593
                     /gene="Ccdc17"
                     /coded_by="NM_001014067.3:146..1927"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500528"
                     /db_xref="RGD:1598211"
ORIGIN      
        1 madysgksgl lpcescdmvf rsrallakht krfciggltp eimaqeqrrs dqeatksslk
       61 rlteetellr lslqkigpwa tdtsqtagsp eerlrdlqgt rarrveetea qsralkqrge
      121 elkrrlhsva gpkgglprpi vlerelrelr eeasrtrgal qtlgarvqal qpqpahqqda
      181 krvvefcclp lrynpetlae eirvlrevyv rgggrdpevl dkilqlqvea salelrrsqn
      241 rkekasaase ealmveaenr ileaeilalq kqkvlslspw gsrdlwrhls rrsdnsllpp
      301 pvappmppvt sstkvqdfhg tskaiingtm trnlgldlhf lpasnvlgpa pydpgaglvi
      361 fydflrglea swiwvqlmts lardgqdtgg atalppalcl pppsasgpig ncailasrqp
      421 vprlppspll slicklqawq gvtwtpqpka waslllfdqs lrvlsgrwrl plrvppttsl
      481 sfaqmnempq vsvegrdwlh pkipmeyhfl cqagqaelfl rlvnardtda qtlaeinpas
      541 aheyqyppmm ssssslessf fthssgiadp pppteetfvs vedkdehlsp hqf
//
LOCUS       NP_001425255             363 aa            linear   ROD 20-APR-2025
DEFINITION  START domain-containing protein 10 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425255 XP_063141249
VERSION     NP_001425255.1
DBSOURCE    REFSEQ: accession NM_001438326.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ito,M., Yamanashi,Y., Toyoda,Y., Izumi-Nakaseko,H., Oda,S.,
            Sugiyama,A., Kuroda,M., Suzuki,H., Takada,T. and Adachi-Akahane,S.
  TITLE     Disruption of Stard10 gene alters the PPARalpha-mediated bile acid
            homeostasis
  JOURNAL   Biochim Biophys Acta 1831 (2), 459-468 (2013)
   PUBMED   23200860
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_063141249.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.4558.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..363
                     /product="START domain-containing protein 10 isoform 2"
                     /note="START domain containing 10; PCTP-like protein;
                     StAR-related lipid transfer (START) domain containing 10;
                     START domain-containing protein 10"
                     /calculated_mol_wt=40052
     Region          92..314
                     /region_name="START_STARD10-like"
                     /note="Lipid-binding START domain of mammalian STARD10 and
                     related proteins; cd08871"
                     /db_xref="CDD:176880"
     Site            order(119..120,127,141,143,155,159,165,168..169,171..172,
                     191,193..196,198,201,203,205,220,237,239..242,244,256,258,
                     260,262,264,266,273,275..277,279..281,284..285,288)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176880"
     CDS             1..363
                     /gene="Stard10"
                     /coded_by="NM_001438326.1:122..1213"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:293150"
                     /db_xref="RGD:1306548"
ORIGIN      
        1 mgpraapgrp gsggsgaggr artpaparpg reartgprkv asasaaaptl sepprrtqes
       61 rtrtrapglp tlsmekpaas tepqgprpal gresvqvpdd qdfrsfrsec eaevgwnlty
      121 skagvsvwvq avemdrtlhk ikcrmeccdv paetlydvlh dieyrkkwds nvietfdiar
      181 ltvnadvgyy swrcpkplkn rdvitlrswl pmgadyiimn ysvkhpkypp rkdlvravsi
      241 qtgyliqstg pkscvityla qvdpkgslpk wvvnkssqfl apkamkkmyk acikypewkq
      301 khqphfkpwl hpeqsplpsl alselsvqha dslenidesa vtesreerag gagegsdddt
      361 slt
//
LOCUS       NP_001425206             450 aa            linear   ROD 20-APR-2025
DEFINITION  protein tweety homolog 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425206 XP_006228278
VERSION     NP_001425206.1
DBSOURCE    REFSEQ: accession NM_001438277.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kumada,T., Yamanaka,Y., Kitano,A., Shibata,M., Awaya,T., Kato,T.,
            Okawa,K., Abe,T., Oshima,N., Nakahata,T. and Heike,T.
  TITLE     Ttyh1, a Ca(2+)-binding protein localized to the endoplasmic
            reticulum, is required for early embryonic development
  JOURNAL   Dev Dyn 239 (8), 2233-2245 (2010)
   PUBMED   20568244
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yoon,J.C., Ng,A., Kim,B.H., Bianco,A., Xavier,R.J. and Elledge,S.J.
  TITLE     Wnt signaling regulates mitochondrial physiology and insulin
            sensitivity
  JOURNAL   Genes Dev 24 (14), 1507-1518 (2010)
   PUBMED   20634317
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Matthews,C.A., Shaw,J.E., Hooper,J.A., Young,I.G., Crouch,M.F. and
            Campbell,H.D.
  TITLE     Expression and evolution of the mammalian brain gene Ttyh1
  JOURNAL   J Neurochem 100 (3), 693-707 (2007)
   PUBMED   17116230
  REMARK    GeneRIF: These data suggest a role for Ttyh1 in process formation,
            cell adhesion and possibly as a transmembrane receptor.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Collins,M.O., Husi,H., Yu,L., Brandon,J.M., Anderson,C.N.,
            Blackstock,W.P., Choudhary,J.S. and Grant,S.G.
  TITLE     Molecular characterization and comparison of the components and
            multiprotein complexes in the postsynaptic proteome
  JOURNAL   J Neurochem 97 Suppl 1, 16-23 (2006)
   PUBMED   16635246
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Suzuki,M.
  TITLE     The Drosophila tweety family: molecular candidates for
            large-conductance Ca2+-activated Cl- channels
  JOURNAL   Exp Physiol 91 (1), 141-147 (2006)
   PUBMED   16219661
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228278.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168158.1, SRR26360176.2407213.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760434 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..450
                     /product="protein tweety homolog 1 isoform 1"
                     /note="protein tweety homolog 1; volume-regulated anion
                     channel subunit Ttyh1"
                     /calculated_mol_wt=48901
     Region          9..441
                     /region_name="Tweety"
                     /note="pfam04906"
                     /db_xref="CDD:461475"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            165
                     /site_type="other"
                     /note="Essential for the formation of the channel-pore.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            355
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            order(371,374)
                     /site_type="active"
                     /note="putative pore region [active]"
                     /db_xref="CDD:143653"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Region          428..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5X8.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D3A9; propagated from
                     UniProtKB/Swiss-Prot (P0C5X8.1)"
     CDS             1..450
                     /gene="Ttyh1"
                     /coded_by="NM_001438277.1:77..1429"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292597"
                     /db_xref="RGD:1310103"
ORIGIN      
        1 mgappgyrps awvhllhqlp radfqlrpvp sgfaprdqey qqalllvaal aglglglsli
       61 fiavylirfc ccrppeppga kspppgggcv twsciaallv gcagigigfy gnsetsdgvs
      121 qlssalqhan htlstiddlv letverlgea vrtelttlee vlservelva atrgarrqae
      181 aaaqhlqgla fwqgvslspv qvaedvtfve eyrwlayvll lllvllvclf tllglakqsk
      241 wlvvvmtams llvlvlswgs mgleaatavg lsdfcsnpdt yvlnltqeet gissdilnyy
      301 flcnqavsnp fqqrltlsqr alasihsqlq glereaspqf paaqkpllsl eetlnvters
      361 fhqlvallhc rslhkdygsa lrglcedale gllflmlfsl lsagalattl cslprawalf
      421 ppsddyddtd dddpfnpqes krfvqwqssi
//
LOCUS       NP_001425191             432 aa            linear   ROD 20-APR-2025
DEFINITION  pachytene checkpoint protein 2 homolog [Rattus norvegicus].
ACCESSION   NP_001425191 XP_008756903
VERSION     NP_001425191.1
DBSOURCE    REFSEQ: accession NM_001438262.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Yost,S., de Wolf,B., Hanks,S., Zachariou,A., Marcozzi,C.,
            Clarke,M., de Voer,R., Etemad,B., Uijttewaal,E., Ramsay,E.,
            Wylie,H., Elliott,A., Picton,S., Smith,A., Smithson,S., Seal,S.,
            Ruark,E., Houge,G., Pines,J., Kops,G.J.P.L. and Rahman,N.
  TITLE     Biallelic TRIP13 mutations predispose to Wilms tumor and chromosome
            missegregation
  JOURNAL   Nat Genet 49 (7), 1148-1151 (2017)
   PUBMED   28553959
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Roig,I., Dowdle,J.A., Toth,A., de Rooij,D.G., Jasin,M. and
            Keeney,S.
  TITLE     Mouse TRIP13/PCH2 is required for recombination and normal
            higher-order chromosome structure during meiosis
  JOURNAL   PLoS Genet 6 (8), e1001062 (2010)
   PUBMED   20711356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Li,X.C. and Schimenti,J.C.
  TITLE     Mouse pachytene checkpoint 2 (trip13) is required for completing
            meiotic recombination but not synapsis
  JOURNAL   PLoS Genet 3 (8), e130 (2007)
   PUBMED   17696610
  REMARK    Erratum:[PLoS Genet. 2007 Sep 7;3(9):e168. Li, Xin [corrected to
            Li, Xin Chenglin]]
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_008756903.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.424.1, SRR26643299.401.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..432
                     /product="pachytene checkpoint protein 2 homolog"
                     /note="thyroid receptor-interacting protein 13; TRIP-13;
                     TR-interacting protein 13"
                     /calculated_mol_wt=48303
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q15645; propagated from
                     UniProtKB/Swiss-Prot (Q5XHZ9.1)"
     Region          34..>205
                     /region_name="McrB"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrBC, GTP-binding regulatory subunit McrB [Defense
                     mechanisms]; COG1401"
                     /db_xref="CDD:441011"
     Region          121..319
                     /region_name="RecA-like_Pch2-like"
                     /note="ATPase domain of Pachytene checkpoint 2 (Pch2) and
                     similar ATPase domains; cd19508"
                     /db_xref="CDD:410916"
     Site            order(134,151..152,155..156,162..165,167..171,215,
                     217..218,224,311)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:410916"
     Site            order(180,184..186,211,213..214,252..253)
                     /site_type="active"
                     /note="ATP binding site [active]"
                     /db_xref="CDD:410916"
     CDS             1..432
                     /gene="Trip13"
                     /coded_by="NM_001438262.1:128..1426"
                     /db_xref="GeneID:292206"
                     /db_xref="RGD:1308516"
ORIGIN      
        1 mddavgdlkq alpcvaespa vhvevlqrsg stakkedikq svyrllkrhn ivfgdyvwte
       61 fdepfltrnv qsvsivdtel kakdpqpidl sactialhif qlneegpsse nldeetenii
      121 aashwvlpaa efhglwdslv ydvevkshll dyvmttllfs dknvdsnlit wnrvvllhgp
      181 pgtgktslck alaqkltirl ssryrygqli einshslfsk wfsesgklvt kmfqkiqdli
      241 ddkealvfvl idevesltaa rnacragaep sdairvvnav ltqidqikrh snvvilttsn
      301 itekidvafv dradikqyig ppsaaaifki ylscleelmk cqiiyprqql ltlrelemig
      361 fiennvskls lllseisrks eglsgrvlrk lpflahalyi qapsvtiegf lqalslavdk
      421 qfeekkklsa hv
//
LOCUS       NP_001100350            1128 aa            linear   ROD 20-APR-2025
DEFINITION  inactive phospholipase C-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001100350 XP_001056257 XP_217326
VERSION     NP_001100350.2
DBSOURCE    REFSEQ: accession NM_001106880.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Oue,K., Zhang,J., Harada-Hada,K., Asano,S., Yamawaki,Y.,
            Hayashiuchi,M., Furusho,H., Takata,T., Irifune,M., Hirata,M. and
            Kanematsu,T.
  TITLE     Phospholipase C-related Catalytically Inactive Protein Is a New
            Modulator of Thermogenesis Promoted by beta-Adrenergic Receptors in
            Brown Adipocytes
  JOURNAL   J Biol Chem 291 (8), 4185-4196 (2016)
   PUBMED   26706316
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Kanematsu,T., Yasunaga,A., Mizoguchi,Y., Kuratani,A., Kittler,J.T.,
            Jovanovic,J.N., Takenaka,K., Nakayama,K.I., Fukami,K., Takenawa,T.,
            Moss,S.J., Nabekura,J. and Hirata,M.
  TITLE     Modulation of GABA(A) receptor phosphorylation and membrane
            trafficking by phospholipase C-related inactive protein/protein
            phosphatase 1 and 2A signaling complex underlying brain-derived
            neurotrophic factor-dependent regulation of GABAergic inhibition
  JOURNAL   J Biol Chem 281 (31), 22180-22189 (2006)
   PUBMED   16754670
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Takenaka,K., Fukami,K., Otsuki,M., Nakamura,Y., Kataoka,Y.,
            Wada,M., Tsuji,K., Nishikawa,S., Yoshida,N. and Takenawa,T.
  TITLE     Role of phospholipase C-L2, a novel phospholipase C-like protein
            that lacks lipase activity, in B-cell receptor signaling
  JOURNAL   Mol Cell Biol 23 (20), 7329-7338 (2003)
   PUBMED   14517301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 7, 2025 this sequence version replaced NP_001100350.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.214432.1,
                                           SRR26643298.47663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..1128
                     /product="inactive phospholipase C-like protein 2"
                     /EC_number="3.1.4.11"
                     /calculated_mol_wt=125783
     Region          144..252
                     /region_name="PH_PLC_eta"
                     /note="Phospholipase C-eta (PLC-eta) pleckstrin homology
                     (PH) domain; cd13364"
                     /db_xref="CDD:270170"
     Site            order(149,151,161,178,235)
                     /site_type="other"
                     /note="putative Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270170"
     Site            order(152,154,158,160,162,177..178)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270170"
     Region          272..415
                     /region_name="EFh_PRIP2"
                     /note="EF-hand motif found in phospholipase C-related but
                     catalytically inactive protein 2 (PRIP-2); cd16223"
                     /db_xref="CDD:320053"
     Region          272..301
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320053"
     Region          308..340
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320053"
     Region          344..372
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320053"
     Region          381..415
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320053"
     Region          426..722
                     /region_name="PI-PLCc_PRIP_metazoa"
                     /note="Catalytic domain of metazoan phospholipase C
                     related, but catalytically inactive protein; cd08597"
                     /db_xref="CDD:176539"
     Region          754..882
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(781,805,834,836,841,843)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     CDS             1..1128
                     /gene="Plcl2"
                     /coded_by="NM_001106880.2:228..3614"
                     /db_xref="GeneID:301173"
                     /db_xref="RGD:1305941"
ORIGIN      
        1 maecgrgaag galptspgpa lgakgalkag agegggsggg grlghgrary dsggvsngdc
       61 slgvsgdear aspargprgv alartpspaa gpvprdskpg glprrssiik dgtkqkrerk
      121 ktvsfssmpt ekkissasdc insmvegsel kkvrsnsriy hryflldadm qslrwepskk
      181 dsekakidik sikevrtgkn tdifrsngis eqisedcafs viygenyesl dlvansadva
      241 niwvtglryl isygkhtldm lessqdnmrt cwvsqmfsei dvddlghitl cnavqcirnl
      301 npglktskie lkfkelhksk dktgteitke efvevfhelc trpeiyfllv qfssnkefld
      361 tkdlmmflea eqgvahinee isleiihkye pskegqekgw lsidgftnyl mspdcyifdp
      421 ehkkvcqdmk qplshyfins shntyliedq frgpsditgy iralkmgcrs veldvwdgpd
      481 nepviytght mtsqivfrsv idiinkyaff aseyplilcl enhcsikqqk vmvqhmkkil
      541 gdklyttspn meesylpspd vlkgkilika kklssncsgv egdvtdedeg aemsqrmgke
      601 nveqpnhvpv krfqlckdls elvsicksvq fkefqvsfqv qkywevcsfn evlaskyane
      661 npgdfvnynk rflarvfpsp mridssnmnp qdfwkcgcqi vamnfqtpgl mmdlnigwfr
      721 qngncgyvlr paimreevsf fsantkdsvp gvspqllhik iisgqnfpkp kgsgakgdvv
      781 dpyvyveihg ipadcaeqrt ktvnqngdap mfdesfefqi nlpelamvrf vvldddyigd
      841 efigqytipf eclqtgyrhv plqsltgevl ahaslfvhva itnrrgggkp hkrglsvrkg
      901 kksreyaslr tlwiktvdev fknaqppird atdlrenmqn avvsfkelcg lssvanlmqc
      961 mlavsprflg pdntplvvln lsepyptmel qaivpevlkk ivttydmmiq slkalienad
     1021 avyekivhcq kaamefhehl hsigtkeglk erklqkaves ftwnitilkg qadllkyakn
     1081 etlenlkqih yaavscglnk pgtenseaqk prrslevipe ktsdengd
//
LOCUS       NP_001425198             771 aa            linear   ROD 20-APR-2025
DEFINITION  solute carrier family 7 member 14 [Rattus norvegicus].
ACCESSION   NP_001425198
VERSION     NP_001425198.1
DBSOURCE    REFSEQ: accession NM_001438269.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.10515.1,
                                           SRR26360194.1339752.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..771
                     /product="solute carrier family 7 member 14"
                     /note="probable cationic amino acid transporter; solute
                     carrier family 7 (cationic amino acid transporter, y+
                     system), member 14; solute carrier family 7 (orphan
                     transporter), member 14"
                     /calculated_mol_wt=83879
     Region          43..677
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     CDS             1..771
                     /gene="Slc7a14"
                     /coded_by="NM_001438269.1:487..2802"
                     /db_xref="GeneID:499587"
                     /db_xref="RGD:1594375"
ORIGIN      
        1 msgflssldp rrvqwgaawy amhsrilrtk pvesmlegtg atsahgtkla qvlttvdlis
       61 lgvgscvgtg myvvsglvak emagpgvivs fiiaavasil sgvcyaefgv rvpkttgsay
      121 tysyvtvgef vaffigwnli leyligtaag asalssmfds lanhtisrwm vdtvgtlngl
      181 gkgeesypdl lalviavivt iivalgvkns vgfnnvlnvl nlavwvfimi aglffvngky
      241 waegqflphg wsgvlqgaat cfyafigfdi iattgeeakn pntsipyait aslvicltay
      301 vsvsmiltlm vpyyaidtes plmemfvahg fyaakfvvai gsvagltvsl lgslfpmprv
      361 iyamagdgll frflahvssy tetpvvaciv sgflaallsl lvslrdliem msigtllayt
      421 lvsvcvlllr yqpesdidgf vkflseehtk kkegiladce ketcspvseg eefsspatnt
      481 cgaknlpslg dnemligksd ksaynvnhpn ygtvdmttgi eadeseniyl iklkkligpr
      541 yytmrirlgl pgkmdrptaa tghtvticvl llfilmfifc sfvifgseyi sgqswwaill
      601 vvlmlllitv lvfvilqqpe npkklpymap clpfvpafam lvniylmlkl stitwirfav
      661 wcfvgmliyf gygiwnstle isareqalhq styqrydvdd pfsveegfsy ategesqedw
      721 ggpaedkgfy yqqmsdakan srtsskaksk skhkqnseal iendeldcsp e
//
LOCUS       NP_001013235             364 aa            linear   ROD 20-APR-2025
DEFINITION  tripartite motif-containing protein 54 [Rattus norvegicus].
ACCESSION   NP_001013235 XP_343027
VERSION     NP_001013235.1
DBSOURCE    REFSEQ: accession NM_001013217.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Chen,H., Chen,X., Yang,L., Sheng,S., Yang,J., Lu,Y., Sun,Y.,
            Zhang,X. and Jiang,C.
  TITLE     TRIM54 alleviates inflammation and apoptosis by stabilizing YOD1 in
            rat tendon-derived stem cells
  JOURNAL   J Biol Chem 300 (1), 105510 (2024)
   PUBMED   38042492
  REMARK    GeneRIF: TRIM54 alleviates inflammation and apoptosis by
            stabilizing YOD1 in rat tendon-derived stem cells.
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Spencer,J.A., Eliazer,S., Ilaria,R.L. Jr., Richardson,J.A. and
            Olson,E.N.
  TITLE     Regulation of microtubule dynamics and myogenic differentiation by
            MURF, a striated muscle RING-finger protein
  JOURNAL   J Cell Biol 150 (4), 771-784 (2000)
   PUBMED   10953002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083706.1.
            
            On Apr 20, 2005 this sequence version replaced XP_343027.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..364
                     /product="tripartite motif-containing protein 54"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 30"
                     /calculated_mol_wt=40900
     Region          24..82
                     /region_name="RING-HC_MuRF3"
                     /note="RING finger, HC subclass, found in muscle-specific
                     RING finger protein 3 (MuRF-3) and similar proteins;
                     cd16761"
                     /db_xref="CDD:319675"
     Region          124..166
                     /region_name="Bbox2_MuRF3_C-II"
                     /note="B-box-type 2 zinc finger found in muscle-specific
                     RING finger protein 3 (MuRF-3) and similar proteins;
                     cd19833"
                     /db_xref="CDD:380891"
     Region          168..211
                     /region_name="Mediates microtubule-binding and
                     homooligomerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIH6.1)"
     Region          188..282
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          328..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIH6.1)"
     CDS             1..364
                     /gene="Trim54"
                     /gene_synonym="Rnf30"
                     /coded_by="NM_001013217.1:185..1279"
                     /db_xref="GeneID:362708"
                     /db_xref="RGD:1306453"
ORIGIN      
        1 mnftvgfkpl lgdahnmdnl ekqlicpicl emfskpvvil pcqhnlcrkc andvfqasnp
       61 lwqsrgsttv ssggrfrcps crhevvldrh gvyglqrnll veniidiykq essrplhska
      121 eqhlmceehe dekiniycls cevptcslck vfgahkdcev aplptiykrq kselsdgiam
      181 lvagndrvqa vitqmeevcq tiednsrrqk qllnqkfetl cavleerkge llqalarvqe
      241 eklqrvrsli rqygdhleas sklvesaiqs meepqmalyl qqakelinkv gamskvelag
      301 rpepgyesme qfsvivehva emlrtidfqp gasgdeedde vtldgeegnt gleeerldgp
      361 eglh
//
LOCUS       NP_001425107            1102 aa            linear   ROD 20-APR-2025
DEFINITION  structural maintenance of chromosomes protein 5 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425107 XP_006231245
VERSION     NP_001425107.1
DBSOURCE    REFSEQ: accession NM_001438178.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Raschle,M., Smeenk,G., Hansen,R.K., Temu,T., Oka,Y., Hein,M.Y.,
            Nagaraj,N., Long,D.T., Walter,J.C., Hofmann,K., Storchova,Z.,
            Cox,J., Bekker-Jensen,S., Mailand,N. and Mann,M.
  TITLE     DNA repair. Proteomics reveals dynamic assembly of repair complexes
            during bypass of DNA cross-links
  JOURNAL   Science 348 (6234), 1253671 (2015)
   PUBMED   25931565
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Brouwer,A.K., Schimmel,J., Wiegant,J.C., Vertegaal,A.C., Tanke,H.J.
            and Dirks,R.W.
  TITLE     Telomeric DNA mediates de novo PML body formation
  JOURNAL   Mol Biol Cell 20 (22), 4804-4815 (2009)
   PUBMED   19793919
REFERENCE   4  (residues 1 to 1102)
  AUTHORS   Behlke-Steinert,S., Touat-Todeschini,L., Skoufias,D.A. and
            Margolis,R.L.
  TITLE     SMC5 and MMS21 are required for chromosome cohesion and mitotic
            progression
  JOURNAL   Cell Cycle 8 (14), 2211-2218 (2009)
   PUBMED   19502785
REFERENCE   5  (residues 1 to 1102)
  AUTHORS   Taylor,E.M., Copsey,A.C., Hudson,J.J., Vidot,S. and Lehmann,A.R.
  TITLE     Identification of the proteins, including MAGEG1, that make up the
            human SMC5-6 protein complex
  JOURNAL   Mol Cell Biol 28 (4), 1197-1206 (2008)
   PUBMED   18086888
REFERENCE   6  (residues 1 to 1102)
  AUTHORS   Potts,P.R. and Yu,H.
  TITLE     The SMC5/6 complex maintains telomere length in ALT cancer cells
            through SUMOylation of telomere-binding proteins
  JOURNAL   Nat Struct Mol Biol 14 (7), 581-590 (2007)
   PUBMED   17589526
REFERENCE   7  (residues 1 to 1102)
  AUTHORS   Potts,P.R., Porteus,M.H. and Yu,H.
  TITLE     Human SMC5/6 complex promotes sister chromatid homologous
            recombination by recruiting the SMC1/3 cohesin complex to
            double-strand breaks
  JOURNAL   EMBO J 25 (14), 3377-3388 (2006)
   PUBMED   16810316
REFERENCE   8  (residues 1 to 1102)
  AUTHORS   Taylor,E.M., Moghraby,J.S., Lees,J.H., Smit,B., Moens,P.B. and
            Lehmann,A.R.
  TITLE     Characterization of a novel human SMC heterodimer homologous to the
            Schizosaccharomyces pombe Rad18/Spr18 complex
  JOURNAL   Mol Biol Cell 12 (6), 1583-1594 (2001)
   PUBMED   11408570
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_006231245.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.7543.1,
                                           SRR26643291.4445.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..1102
                     /product="structural maintenance of chromosomes protein 5
                     isoform 1"
                     /note="SMC5 structural maintenance of chromosomes 5-like
                     1; structural maintenance of chromosomes protein 5"
                     /calculated_mol_wt=128881
     Region          51..>196
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          53..1052
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            80..87
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213179"
     Site            178..181
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213179"
     Region          <975..1077
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            991..1000
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213179"
     Site            1015..1020
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213179"
     Site            1023..1026
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213179"
     Site            1050..1056
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213179"
     CDS             1..1102
                     /gene="Smc5"
                     /gene_synonym="Smc5l1"
                     /coded_by="NM_001438178.1:86..3394"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293967"
                     /db_xref="RGD:1307492"
ORIGIN      
        1 matpsgkaaa pnpqaskrsl prdassefps krknsnptst lprpsglfve gsivriamen
       61 fltydicevs pgphlnmiig angtgkssiv caiclglagk pafmgradkv gffvkrgcsk
      121 glveielfrt sgnliitrei dviknqsfwf inkkpvtqki veeqvaalni qvgnlcqflp
      181 qdkvgefakl skielleate ksigppemhr yhcelknfre kekqletsck ekteyldkmi
      241 qrnerykqdv erfyerkrhl dliemleakr pwveyenvrq eyegvklvrd rvkeevrklk
      301 egqipmtrri eeierqrrtl evrikekatd ikeasqkckq rqdlierkdr hikelqqalt
      361 vkqneeqdrq krisntrkmi edlqnelrta encenlqpqi daitndlrrv qeekalcege
      421 iidkqrekem lekqkrsvsd hitrfdnlmn qkedklrqry rdtydavlwl rnnrdrfkqr
      481 vcepimltin mkdnknakyv enhissndlr afvfesqedm eiflrevrdn kklrvnavia
      541 pkisyadkap srslnelkqy gffsylrelf dapdpvmsyl ccqyhihevp vgtertreri
      601 erviqetrlk qiytaeekyv lktsfysnkv issntslkva qfltvtvdle qrrhleeqlk
      661 einrkleavd sglvalrdtn rhlelkdnel rlkkkeller ktkkrqleqk issklasirl
      721 meqdtcnlee eerkastkik einvqkaklv teltglvkic tslhiqkvdl ilqnttvise
      781 knkleadyma sssqlrvteq qfielddnrq rllqkckelm krarqvcnls adqavpqefq
      841 tqvptipngh sssppmafqd lpntldeida llteersras cftglnpsvv eeytkreiei
      901 qqlteelkgk kveldeyren isqvkerwln plkelvekin ekfsnffssm qcagevdlht
      961 eneedydkyg irirvkfrss tqlheltphh qsggersvst mlylmalqel nrcpfrvvde
     1021 inqgmdpine rrvfemvvnt ackentsqyf fitpkllqnl pysekmtvlf vyngphmlep
     1081 nrwnlkafqr rrrritftqp sq
//
LOCUS       NP_001425226             139 aa            linear   ROD 20-APR-2025
DEFINITION  small ribosomal subunit protein uS12m isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425226 XP_006228714
VERSION     NP_001425226.1
DBSOURCE    REFSEQ: accession NM_001438297.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Amunts,A., Brown,A., Toots,J., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Ribosome. The structure of the human mitochondrial ribosome
  JOURNAL   Science 348 (6230), 95-98 (2015)
   PUBMED   25838379
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 17, 2025 this sequence version replaced XP_006228714.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI294944.1, DV728626.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..139
                     /product="small ribosomal subunit protein uS12m isoform 1"
                     /note="28S ribosomal protein S12, mitochondrial; small
                     ribosomal subunit protein uS12m"
                     /calculated_mol_wt=15310
     Region          32..138
                     /region_name="Ribosomal_S12"
                     /note="S12-like family, 30S ribosomal protein S12
                     subfamily; S12 is located at the interface of the large
                     and small ribosomal subunits of prokaryotes, chloroplasts
                     and mitochondria, where it plays an important role in both
                     tRNA and ribosomal subunit...; cd03368"
                     /db_xref="CDD:239466"
     Site            order(33..34,36..37,40..41)
                     /site_type="other"
                     /note="S17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239466"
     Site            33
                     /site_type="active"
                     /note="S8 interaction site [active]"
                     /db_xref="CDD:239466"
     Site            order(41..43,54,56..57,59,74..75,77..79,86,94,97..98,
                     111..112,116..117,138)
                     /site_type="other"
                     /note="16S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(71..72,116)
                     /site_type="other"
                     /note="streptomycin interaction site [chemical binding]"
                     /db_xref="CDD:239466"
     Site            72..73
                     /site_type="other"
                     /note="23S rRNA interaction site [nucleotide binding]"
                     /db_xref="CDD:239466"
     Site            order(73..78,98..106)
                     /site_type="other"
                     /note="aminoacyl-tRNA interaction site (A-site)
                     [nucleotide binding]"
                     /db_xref="CDD:239466"
     CDS             1..139
                     /gene="Mrps12"
                     /coded_by="NM_001438297.1:44..463"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:292758"
                     /db_xref="RGD:1306221"
ORIGIN      
        1 mswpgllhgl ttslsrglal apqlwatrsm atlnqmhrlg rpkeppkrlg ptegrpqlkg
       61 vvlrtfirkp kkpnsanrkc crvrlstgke avcfipgegh tlqehhvvlv eggrtqdlpg
      121 vklkvvrgky dcghvqkkk
//
LOCUS       NP_001425194             289 aa            linear   ROD 20-APR-2025
DEFINITION  Krueppel-like factor 13 [Rattus norvegicus].
ACCESSION   NP_001425194
VERSION     NP_001425194.1
DBSOURCE    REFSEQ: accession NM_001438265.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Gu,M., Wang,J., Wang,Y., Xu,Y., Zhang,Y., Wu,W. and Liao,S.
  TITLE     MiR-147b inhibits cell viability and promotes apoptosis of rat H9c2
            cardiomyocytes via down-regulating KLF13 expression
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 50 (3), 288-297 (2018)
   PUBMED   29377979
  REMARK    GeneRIF: Data show that Kruppel-like factor 1 (KLF13) was a
            downstream target of miR-147b.
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bayoumi,A.S., Park,K.M., Wang,Y., Teoh,J.P., Aonuma,T., Tang,Y.,
            Su,H., Weintraub,N.L. and Kim,I.M.
  TITLE     A carvedilol-responsive microRNA, miR-125b-5p protects the heart
            from acute myocardial infarction by repressing pro-apoptotic bak1
            and klf13 in cardiomyocytes
  JOURNAL   J Mol Cell Cardiol 114, 72-82 (2018)
   PUBMED   29122578
  REMARK    GeneRIF: the improvement of cardiac function and structure elicited
            by miR-125b-5p is in part attributed to repression of the
            pro-apoptotic genes Bak1 and Klf13 in cardiomyocytes.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Gordon,A.R., Outram,S.V., Keramatipour,M., Goddard,C.A.,
            Colledge,W.H., Metcalfe,J.C., Hager-Theodorides,A.L., Crompton,T.
            and Kemp,P.R.
  TITLE     Splenomegaly and modified erythropoiesis in KLF13-/- mice
  JOURNAL   J Biol Chem 283 (18), 11897-11904 (2008)
   PUBMED   18285334
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Martin,K.M., Cooper,W.N., Metcalfe,J.C. and Kemp,P.R.
  TITLE     Mouse BTEB3, a new member of the basic transcription element
            binding protein (BTEB) family, activates expression from GC-rich
            minimal promoter regions
  JOURNAL   Biochem J 345 Pt 3 (Pt 3), 529-533 (2000)
   PUBMED   10642511
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.1569026.1,
                                           SRR22582424.1710311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840112, SAMN12840113
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..289
                     /product="Krueppel-like factor 13"
                     /note="Kruppel-like factor 13"
                     /calculated_mol_wt=30974
     Region          7..169
                     /region_name="KLF13_N"
                     /note="N-terminal domain of Kruppel-like factor 13;
                     cd21571"
                     /db_xref="CDD:409236"
     Region          <163..253
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          170..192
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(177,179,181,183..184,187..188,191,207,209,213..214,
                     217..218,221,235,237,239,241..242,245..246,249)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          200..222
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(200,205,218,222)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          230..250
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..289
                     /gene="Klf13"
                     /gene_synonym="RGD1565099"
                     /coded_by="NM_001438265.1:492..1361"
                     /db_xref="GeneID:499171"
                     /db_xref="RGD:1565099"
ORIGIN      
        1 maaaayvdhf aaeclvsmss ravvhepreg peprpegaaa aaptlprvde rrdgkdsasl
       61 fvvariladl nqqapapapa erregaaark artpcrlppa ppapppgpep aspgqagapa
      121 appspawsep eaalepepgp agsgepglrq rgrrgrsrad lespqrkhkc hyagcekvyg
      181 ksshlkahlr thtgerpfac swqecnkkfa rsdelarhyr thtgekkfsc picekrfmrs
      241 dhltkharrh anfhpgmlqr rgggsrtgsl sdysrsdass ptispassp
//
LOCUS       NP_001425290             471 aa            linear   ROD 21-APR-2025
DEFINITION  7-dehydrocholesterol reductase [Rattus norvegicus].
ACCESSION   NP_001425290 XP_063128807
VERSION     NP_001425290.1
DBSOURCE    REFSEQ: accession NM_001438361.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Sun,L., Lu,J., Yao,D., Li,X., Cao,Y., Gao,J., Liu,J., Zheng,T.,
            Wang,H. and Zhan,X.
  TITLE     Effect of DHCR7 for the co-occurrence of hypercholesterolemia and
            vitamin D deficiency in type 2 diabetes: Perspective of health
            prevention
  JOURNAL   Prev Med 173, 107576 (2023)
   PUBMED   37329988
  REMARK    GeneRIF: Effect of DHCR7 for the co-occurrence of
            hypercholesterolemia and vitamin D deficiency in type 2 diabetes:
            Perspective of health prevention.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Kwak,S.Y., Cho,Y., Oh,H. and Shin,M.J.
  TITLE     Association of circulating 25-hydroxyvitamin D levels with
            hypertension and blood pressure values in Korean adults: A
            Mendelian randomization study on a subset of the Korea National
            Health and Nutrition Survey 2011-2012 population
  JOURNAL   Nutr Res Pract 13 (6), 498-508 (2019)
   PUBMED   31814925
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Fang,J., Hou,S., Xiang,Q., Qi,J., Yu,H., Shi,Y., Zhou,Y.,
            Kijlstra,A. and Yang,P.
  TITLE     Polymorphisms in genetics of vitamin D metabolism confer
            susceptibility to ocular Behcet disease in a Chinese Han population
  JOURNAL   Am J Ophthalmol 157 (2), 488-494 (2014)
   PUBMED   24184224
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bae,S.H., Lee,J.N., Fitzky,B.U., Seong,J. and Paik,Y.K.
  TITLE     Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
            distribution, expression, chromosomal localization, and regulation
            of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz
            syndrome-related protein
  JOURNAL   J Biol Chem 274 (21), 14624-14631 (1999)
   PUBMED   10329655
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Holmer,L., Pezhman,A. and Worman,H.J.
  TITLE     The human lamin B receptor/sterol reductase multigene family
  JOURNAL   Genomics 54 (3), 469-476 (1998)
   PUBMED   9878250
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Shefer,S., Salen,G., Honda,A., Batta,A.K., Nguyen,L.B., Tint,G.S.,
            Ioannou,Y.A. and Desnick,R.
  TITLE     Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase:
            substrate specificity, competitive and non-competitive inhibition,
            and phosphorylation/dephosphorylation
  JOURNAL   J Lipid Res 39 (12), 2471-2476 (1998)
   PUBMED   9831636
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Waterham,H.R., Wijburg,F.A., Hennekam,R.C., Vreken,P.,
            Poll-The,B.T., Dorland,L., Duran,M., Jira,P.E., Smeitink,J.A.,
            Wevers,R.A. and Wanders,R.J.
  TITLE     Smith-Lemli-Opitz syndrome is caused by mutations in the
            7-dehydrocholesterol reductase gene
  JOURNAL   Am J Hum Genet 63 (2), 329-338 (1998)
   PUBMED   9683613
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Moebius,F.F., Fitzky,B.U., Lee,J.N., Paik,Y.K. and Glossmann,H.
  TITLE     Molecular cloning and expression of the human delta7-sterol
            reductase
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1899-1902 (1998)
   PUBMED   9465114
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_063128807.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.6859.1,
                                           SRR22399481.396230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..471
                     /product="7-dehydrocholesterol reductase"
                     /EC_number="1.3.1.21"
                     /EC_number="3.3.2.11"
                     /note="7-DHC reductase; sterol Delta(7)-reductase;
                     cholesterol-5,6-epoxide hydrolase subunit DHCR7"
                     /calculated_mol_wt=54024
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Region          89..471
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2Z8.1)"
     CDS             1..471
                     /gene="Dhcr7"
                     /coded_by="NM_001438361.1:184..1599"
                     /db_xref="GeneID:64191"
                     /db_xref="RGD:621769"
ORIGIN      
        1 masksqhnas kaknhnvkae sqgqwgrawe vdwfslvsvi flllfapfiv yyfimacdqy
       61 scsltapild vatgraslad iwaktppvta kaaqlyalwv sfqvllyswl pdfchrflpg
      121 yvggvqegai tpagivnkye vnglqawlit hflwfvnayl lswfsptiif dnwipllwca
      181 nilgyavstf amikgylfpt saedckftgn ffynymmgie fnprigkwfd fklffngrpg
      241 ivawtlinls faakqqelyg hvtnsmilvn vlqaiyvldf fwnetwylkt idichdhfgw
      301 ylgwgdcvwl pylytlqgly lvyhpvqlst pnalgvlllg lvgyyifrmt nhqkdlfrrt
      361 dghcliwgkk pkaiecsyts adglkhrskl lvsgfwgvar hfnytgdlmg slayclacgg
      421 ghllpyfyii ymtillthrc lrdehrcank ygrdweryva avpyrllpgi f
//
LOCUS       NP_001425300             574 aa            linear   ROD 21-APR-2025
DEFINITION  lipolysis-stimulated lipoprotein receptor isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001425300 XP_006228906
VERSION     NP_001425300.1
DBSOURCE    REFSEQ: accession NM_001438371.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Wang,J., Qin,M., Wu,Q., Yang,H., Wei,B., Xie,J., Qin,Y., Liang,Z.
            and Huang,J.
  TITLE     Effects of Lipolysis-Stimulated Lipoprotein Receptor on Tight
            Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis
  JOURNAL   Biomed Res Int 2022, 4234186 (2022)
   PUBMED   35463981
  REMARK    GeneRIF: Effects of Lipolysis-Stimulated Lipoprotein Receptor on
            Tight Junctions of Pancreatic Ductal Epithelial Cells in
            Hypertriglyceridemic Acute Pancreatitis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Sohet,F., Lin,C., Munji,R.N., Lee,S.Y., Ruderisch,N., Soung,A.,
            Arnold,T.D., Derugin,N., Vexler,Z.S., Yen,F.T. and Daneman,R.
  TITLE     LSR/angulin-1 is a tricellular tight junction protein involved in
            blood-brain barrier formation
  JOURNAL   J Cell Biol 208 (6), 703-711 (2015)
   PUBMED   25753034
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Nakatsu,D., Kano,F., Taguchi,Y., Sugawara,T., Nishizono,T.,
            Nishikawa,K., Oda,Y., Furuse,M. and Murata,M.
  TITLE     JNK1/2-dependent phosphorylation of angulin-1/LSR is required for
            the exclusive localization of angulin-1/LSR and tricellulin at
            tricellular contacts in EpH4 epithelial sheet
  JOURNAL   Genes Cells 19 (7), 565-581 (2014)
   PUBMED   24889144
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Furuse,M., Oda,Y., Higashi,T., Iwamoto,N. and Masuda,S.
  TITLE     Lipolysis-stimulated lipoprotein receptor: a novel membrane protein
            of tricellular tight junctions
  JOURNAL   Ann N Y Acad Sci 1257, 54-58 (2012)
   PUBMED   22671589
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Masuda,S., Oda,Y., Sasaki,H., Ikenouchi,J., Higashi,T., Akashi,M.,
            Nishi,E. and Furuse,M.
  TITLE     LSR defines cell corners for tricellular tight junction formation
            in epithelial cells
  JOURNAL   J Cell Sci 124 (Pt 4), 548-555 (2011)
   PUBMED   21245199
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Yagil,C., Hubner,N., Monti,J., Schulz,H., Sapojnikov,M., Luft,F.C.,
            Ganten,D. and Yagil,Y.
  TITLE     Identification of hypertension-related genes through an integrated
            genomic-transcriptomic approach
  JOURNAL   Circ Res 96 (6), 617-625 (2005)
   PUBMED   15731461
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Mesli,S., Javorschi,S., Berard,A.M., Landry,M., Priddle,H.,
            Kivlichan,D., Smith,A.J., Yen,F.T., Bihain,B.E. and Darmon,M.
  TITLE     Distribution of the lipolysis stimulated receptor in adult and
            embryonic murine tissues and lethality of LSR-/- embryos at 12.5 to
            14.5 days of gestation
  JOURNAL   Eur J Biochem 271 (15), 3103-3114 (2004)
   PUBMED   15265030
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Yen,F.T., Masson,M., Clossais-Besnard,N., Andre,P., Grosset,J.M.,
            Bougueleret,L., Dumas,J.B., Guerassimenko,O. and Bihain,B.E.
  TITLE     Molecular cloning of a lipolysis-stimulated remnant receptor
            expressed in the liver
  JOURNAL   J Biol Chem 274 (19), 13390-13398 (1999)
   PUBMED   10224102
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006228906.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100626.1, AF119668.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..574
                     /product="lipolysis-stimulated lipoprotein receptor
                     isoform 1 precursor"
                     /note="lipolysis-stimulated remnant receptor;
                     liver-specific bHLH-Zip transcription factor 7;
                     lipolysis-stimulated receptor"
                     /calculated_mol_wt=60284
     sig_peptide     1..36
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3532
     CDS             1..574
                     /gene="Lsr"
                     /gene_synonym="Lisch7"
                     /coded_by="NM_001438371.1:202..1926"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:64355"
                     /db_xref="RGD:69236"
ORIGIN      
        1 mapaagacag apdshpatvv fvclfliifc pdpasaiqvt vsdpyhvvil fqpvtlpcty
       61 qmsntltvpi viwkyksfcr driadafspa svdnqlnaql aagnpgynpy vecqdsvrtv
      121 rvvatkqgna vtlgdyyqgr rititgnadl tfeqtawgds gvyycsvvsa qdldgnneay
      181 aelivldwlf vvvvclasll lflllgicwc qccphtcccy vrcpccpdkc ccpealyaag
      241 kaatsgvpsi yapsiythls paktpppppa mipmgppygy pgdfdrhssv gghssqvpll
      301 rdvdgsvsse vrsgyriqan qqddsmrvly ymekelanfd psrpgppngr veramsevts
      361 lheddwrsrp srapaltpir deewnrhspq sprtweqepl qeqprggwgs grprarsvda
      421 lddinrpgst esgrssppss grrgrayapp rsrsrddlyd pddprdlphs rdphyyddir
      481 srdpradprs rqrsrdprda gfrsrdpqyd grlleealkk kgsgerrrvy reeeeeeegq
      541 yppapppyse tdsqasrerr lkknlalsre slvv
//
LOCUS       NP_001425332             163 aa            linear   ROD 21-APR-2025
DEFINITION  bcl2-associated agonist of cell death isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425332 XP_006230960
VERSION     NP_001425332.1
DBSOURCE    REFSEQ: accession NM_001438403.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Bernhem,K., Fontana,J.M., Svensson,D., Zhang,L., Nilsson,L.M.,
            Scott,L., Blom,H., Brismar,H. and Aperia,A.
  TITLE     Super-resolution microscopy reveals that Na+/K+-ATPase signaling
            protects against glucose-induced apoptosis by deactivating Bad
  JOURNAL   Cell Death Dis 12 (8), 739 (2021)
   PUBMED   34315852
  REMARK    GeneRIF: Super-resolution microscopy reveals that Na(+)/K(+)-ATPase
            signaling protects against glucose-induced apoptosis by
            deactivating Bad.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Michurina,S.V., Kolesnikov,S.I., Bochkareva,A.L., Ishchenko,I.Y.
            and Arkhipov,S.A.
  TITLE     Expression of Apoptosis Regulator Proteins Bcl-2 and Bad in Rat
            Ovarian Follicular Apparatus during Recovery after Extreme
            Hypothermia
  JOURNAL   Bull Exp Biol Med 168 (2), 205-209 (2019)
   PUBMED   31784847
  REMARK    GeneRIF: On day 14 after hyperthermia changes in synthesis led to a
            decrease in Bcl-2/Bad index, which attested to weakening of the
            antiapoptotic defense and activation of oocyte apoptosis by the
            mitochondrial pathway.
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yuan,F., Xu,X., Wu,Y., Duan,S. and Wu,H.
  TITLE     Gastrodin Ameliorates Acute Rejection via IRE1alpha/TRAF2/NF-kappaB
            in Rats Receiving Liver Allografts
  JOURNAL   Biomed Res Int 2019, 9276831 (2019)
   PUBMED   31828147
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Wang,Q., Chen,R., Zhang,C., Inam-U-Llah, Piao,F. and Shi,X.
  TITLE     NGF protects bone marrow mesenchymal stem cells against
            2,5-hexanedione-induced apoptosis in vitro via Akt/Bad signal
            pathway
  JOURNAL   Mol Cell Biochem 457 (1-2), 133-143 (2019)
   PUBMED   30911955
  REMARK    GeneRIF: it was found that NGF promoted phosphorylation of Akt and
            Bad, which is TrkA dependent. However, K252a and MK-2206 (TrkA and
            Akt inhibitor, respectively) suppressed the anti-apoptosis of NGF,
            indicating the protective effect of NGF on BMSCs apoptosis via a
            novel Akt/Bad pathway.
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Thangarajan,S., Ramachandran,S. and Krishnamurthy,P.
  TITLE     Chrysin exerts neuroprotective effects against 3-Nitropropionic
            acid induced behavioral despair-Mitochondrial dysfunction and
            striatal apoptosis via upregulating Bcl-2 gene and downregulating
            Bax-Bad genes in male wistar rats
  JOURNAL   Biomed Pharmacother 84, 514-525 (2016)
   PUBMED   27690136
  REMARK    GeneRIF: Chrysin prevents apoptosis by upregulating the Bcl-2 mRNA
            expression and downregulating the pro-apoptotic (Bax, Bad) mRNAs in
            3-nitropropionic acid induced behavioral despair/mitochondrial
            dysfunction/striatal apoptosis.
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Ottilie,S., Diaz,J.L., Horne,W., Chang,J., Wang,Y., Wilson,G.,
            Chang,S., Weeks,S., Fritz,L.C. and Oltersdorf,T.
  TITLE     Dimerization properties of human BAD. Identification of a BH-3
            domain and analysis of its binding to mutant BCL-2 and BCL-XL
            proteins
  JOURNAL   J Biol Chem 272 (49), 30866-30872 (1997)
   PUBMED   9388232
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Kaipia,A., Hsu,S.Y. and Hsueh,A.J.
  TITLE     Expression and function of a proapoptotic Bcl-2 family member
            Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
  JOURNAL   Endocrinology 138 (12), 5497-5504 (1997)
   PUBMED   9389536
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Tzung,S.P., Fausto,N. and Hockenbery,D.M.
  TITLE     Expression of Bcl-2 family during liver regeneration and
            identification of Bcl-x as a delayed early response gene
  JOURNAL   Am J Pathol 150 (6), 1985-1995 (1997)
   PUBMED   9176392
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230960.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.3979.1,
                                           SRR26643287.3009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..163
                     /product="bcl2-associated agonist of cell death isoform 1"
                     /note="bcl2 antagonist of cell death; bcl-2-binding
                     component 6; bcl-xL/Bcl-2-associated death promoter;
                     Bcl2-antagonist of cell death; bcl-2 associated death
                     agonist; bcl2-associated death promoter"
                     /calculated_mol_wt=17762
     Region          1..163
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     CDS             1..163
                     /gene="Bad"
                     /gene_synonym="Bad_v1; Bad_v2"
                     /coded_by="NM_001438403.1:63..554"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64639"
                     /db_xref="RGD:620103"
ORIGIN      
        1 mfqipefeps eqedasttdr glgpsltedq pgpylapgll gsivqqqpgq aannshhgga
       61 gtmetrsrhs sypagteede gmeeelspfr grsrsappnl waaqrygrel rrmsdefegs
      121 fkglprpksa gtatqmrqsa swtriiqsww drnlgkggst psq
//
LOCUS       NP_001425323            1389 aa            linear   ROD 21-APR-2025
DEFINITION  centlein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425323
VERSION     NP_001425323.1
DBSOURCE    REFSEQ: accession NM_001438394.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1389)
  AUTHORS   Fang,G., Zhang,D., Yin,H., Zheng,L., Bi,X. and Yuan,L.
  TITLE     Centlein mediates an interaction between C-Nap1 and Cep68 to
            maintain centrosome cohesion
  JOURNAL   J Cell Sci 127 (Pt 8), 1631-1639 (2014)
   PUBMED   24554434
REFERENCE   2  (residues 1 to 1389)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 1389)
  AUTHORS   Makino,K., Umeda,K., Uezu,A., Hiragami,Y., Sakamoto,T., Ihn,H. and
            Nakanishi,H.
  TITLE     Identification and characterization of the novel centrosomal
            protein centlein
  JOURNAL   Biochem Biophys Res Commun 366 (4), 958-962 (2008)
   PUBMED   18086554
  REMARK    GeneRIF: The molecular characterization of a novel protein, named
            centlein (centrosomal protein), is described. Centlein was a
            protein of 721 amino acids with a calculated molecular weight of
            82,717 and possessed coiled-coil domains.[Centlein]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3051864.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1389
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..1389
                     /product="centlein isoform 1"
                     /note="centrosomal protein; centlein, centrosomal protein"
                     /calculated_mol_wt=159501
     Region          149..>778
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <522..1290
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1389
                     /gene="Cntln"
                     /gene_synonym="RGD1308101"
                     /coded_by="NM_001438394.1:168..4337"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:679640"
                     /db_xref="RGD:1308101"
ORIGIN      
        1 maarspsssp psplarrssr ralrvgrgae vhavrseasg lastarevva dksdllwrgk
       61 egsggrrgsg rpgaalapvl sapvgswwpg glssveakat rsqlleeels svkeelaqcq
      121 adkefvwslw krlqatnpdl tqtvslvver ekqkseakdr kvleilqvkd akiqeleqte
      181 avlnrelydl vklktlvdee naflkkefsd lqkkfkdksq eakdakecvq skeeqnrlli
      241 knleeenerv rarctdllnd leklrmqeah wreekhsada kvkvleenli eakkeiessq
      301 srynavslql nskqtellqk dmditlvrke lqelqnlykq nsahtaqqad liqqlqvlnm
      361 dtqkvlrnqe dahtaesity qelynelhic fettksneam lqqrvanlqh qlfqkeqenv
      421 klkeklqesq gtlglsphes dsnhsakapl ssletlmisq kseieylqkk lkvaneklme
      481 nrscdqelse kgtegkrtep pvkrsrslsp kscfmdseel rklkkaerki qnlektlqlk
      541 sqendelrda hekrkerlqm lhtnykavre qlkqweedsg mtetrkpkra dpqqlrreds
      601 davwnelayf krenqelmvq kmnlqdelde lkiymtidkt tiqelnrcma ekreeqlfrh
      661 hedagvkkst peknekaise qtlekviele nrlksfekns rklkeeskkl kkendflksh
      721 lqhyqedses rgkelekllr vsssveqdks elqtkvtale revttlrrqv akakalrden
      781 eevvnpeeke hcptdkakse mattdvraqh cdckttttkv kfkaakkkcs vgrhhtvlnh
      841 svkvmshven lskdgwedms egssdsetqt fqnlgtvive tsqnirpien dgnqketdqt
      901 edsraqqevq tyscedlkap qntkkmtfqn ksgslqknlh salparvnre kcktkpaqks
      961 ssntillrer ivslqqqnsl lqnarkaaes sakefkeane kllhqqqisd hrfqtsrqti
     1021 kkltldlael rkekedllkk vesssditsl aeevsrimap qiqvttlgps rstdleikql
     1081 qcklknatne ltkqsssvks lklellakdd hmkamqekms rmerditmkr hliedlkfrq
     1141 kinsesnesf nemlgtlekk vktlteecsn kkvsvdslkq rlsvavkeks qyeqmyqksk
     1201 eelekkdlkm nllisklndt etamaqiksa aseqlqglal qseqvlegtq kklllaneki
     1261 eeftvfvqal vnelqsdahr trqqvrelrq tqksrhackt sthkaqtlaa silnisrsdl
     1321 eeilhtgdem eiektkidae ndkdwmlyiq kllqgqlpfa sylleavlgk ikenkklteg
     1381 yftvmkdik
//
LOCUS       NP_001425348             448 aa            linear   ROD 21-APR-2025
DEFINITION  5-hydroxytryptamine receptor 7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425348 XP_006231369
VERSION     NP_001425348.1
DBSOURCE    REFSEQ: accession NM_001438419.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Korlatowicz,A., Pabian,P., Solich,J., Kolasa,M., Latocha,K.,
            Dziedzicka-Wasylewska,M. and Faron-Gorecka,A.
  TITLE     Habenula as a Possible Target for Treatment-Resistant Depression
            Phenotype in Wistar Kyoto Rats
  JOURNAL   Mol Neurobiol 60 (2), 643-654 (2023)
   PUBMED   36344870
  REMARK    GeneRIF: Habenula as a Possible Target for Treatment-Resistant
            Depression Phenotype in Wistar Kyoto Rats.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Slawinska,U., Majczynski,H., Kwasniewska,A., Miazga,K., Cabaj,A.M.,
            Bekisz,M., Jordan,L.M. and Zawadzka,M.
  TITLE     Unusual Quadrupedal Locomotion in Rat during Recovery from Lumbar
            Spinal Blockade of 5-HT7 Receptors
  JOURNAL   Int J Mol Sci 22 (11), 6007 (2021)
   PUBMED   34199392
  REMARK    GeneRIF: Unusual Quadrupedal Locomotion in Rat during Recovery from
            Lumbar Spinal Blockade of 5-HT7 Receptors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Cinar,I., Halici,Z., Dincer,B., Sirin,B. and Cadirci,E.
  TITLE     The role of 5-HT7 receptors on isoproterenol-induced myocardial
            infarction in rats with high-fat diet exacerbated coronary
            endothelial dysfunction
  JOURNAL   Hum Exp Toxicol 39 (8), 1005-1018 (2020)
   PUBMED   32329363
  REMARK    GeneRIF: The role of 5-HT7 receptors on isoproterenol-induced
            myocardial infarction in rats with high-fat diet exacerbated
            coronary endothelial dysfunction.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Hernandez-Abreu,O.I., Garcia-Pedraza,J.A., Rivera-Mancilla,E.,
            Villanueva-Castillo,B., Moran,A., Garcia-Domingo,M.,
            Manrique-Maldonado,G., Altamirano-Espinoza,A.H. and Villalon,C.M.
  TITLE     Blockade of 5-HT2 receptors with sarpogrelate uncovers 5-HT7
            receptors inhibiting the tachycardic sympathetic drive in pithed
            rats
  JOURNAL   Clin Exp Pharmacol Physiol 47 (3), 403-411 (2020)
   PUBMED   31846086
  REMARK    GeneRIF: Blockade of 5-HT2 receptors with sarpogrelate uncovers
            5-HT7 receptors inhibiting the tachycardic sympathetic drive in
            pithed rats.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Seitz,B.M., Demireva,E.Y., Xie,H., Fink,G.D., Krieger-Burke,T.,
            Burke,W.M. and Watts,S.W.
  TITLE     5-HT does not lower blood pressure in the 5-HT7 knockout rat
  JOURNAL   Physiol Genomics 51 (7), 302-310 (2019)
   PUBMED   31125292
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Heidmann,D.E., Metcalf,M.A., Kohen,R. and Hamblin,M.W.
  TITLE     Four 5-hydroxytryptamine7 (5-HT7) receptor isoforms in human and
            rat produced by alternative splicing: species differences due to
            altered intron-exon organization
  JOURNAL   J Neurochem 68 (4), 1372-1381 (1997)
   PUBMED   9084407
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Ruat,M., Traiffort,E., Leurs,R., Tardivel-Lacombe,J., Diaz,J.,
            Arrang,J.M. and Schwartz,J.C.
  TITLE     Molecular cloning, characterization, and localization of a
            high-affinity serotonin receptor (5-HT7) activating cAMP formation
  JOURNAL   Proc Natl Acad Sci U S A 90 (18), 8547-8551 (1993)
   PUBMED   8397408
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Lovenberg,T.W., Baron,B.M., de Lecea,L., Miller,J.D., Prosser,R.A.,
            Rea,M.A., Foye,P.E., Racke,M., Slone,A.L., Siegel,B.W. et al.
  TITLE     A novel adenylyl cyclase-activating serotonin receptor (5-HT7)
            implicated in the regulation of mammalian circadian rhythms
  JOURNAL   Neuron 11 (3), 449-458 (1993)
   PUBMED   8398139
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Shen,Y., Monsma,F.J. Jr., Metcalf,M.A., Jose,P.A., Hamblin,M.W. and
            Sibley,D.R.
  TITLE     Molecular cloning and expression of a 5-hydroxytryptamine7
            serotonin receptor subtype
  JOURNAL   J Biol Chem 268 (24), 18200-18204 (1993)
   PUBMED   8394362
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Meyerhof,W., Obermuller,F., Fehr,S. and Richter,D.
  TITLE     A novel rat serotonin receptor: primary structure, pharmacology,
            and expression pattern in distinct brain regions
  JOURNAL   DNA Cell Biol 12 (5), 401-409 (1993)
   PUBMED   8517926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006231369.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X69663.1, SRR26360176.274686.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..448
                     /product="5-hydroxytryptamine receptor 7 isoform 1"
                     /note="serotonin receptor 7; GPRFO; 5-HT-7; 5-HT-X; 5-HT7;
                     high affinity serotonin receptor (5HT7);
                     5-hydroxytryptamine (serotonin) receptor 7, adenylate
                     cyclase-coupled"
                     /calculated_mol_wt=49706
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32305.2)"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32305.2)"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          100..398
                     /region_name="7tmA_5-HT7"
                     /note="serotonin receptor subtype 7, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15329"
                     /db_xref="CDD:320452"
     Region          119..145
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320452"
     Site            122..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Site            156..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          158..188
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320452"
     Site            order(161..162,165..166,169..170,234,246,250,343,346..347,
                     353,366,369..370,373,377)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320452"
     Region          200..222
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320452"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          239..268
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320452"
     Site            241..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          323..353
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320452"
     Site            330..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     Region          366..391
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320452"
     Site            367..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32305.2)"
     CDS             1..448
                     /gene="Htr7"
                     /gene_synonym="5Ht7"
                     /coded_by="NM_001438419.1:116..1462"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65032"
                     /db_xref="RGD:71034"
ORIGIN      
        1 mmdvnssgrp dlyghlrsli lpevgrglqd lspdggahpv vsswmphlls gflevtaspa
       61 ptwdappdnv sgcgeqinyg rvekvvigsi ltlitlltia gnclvvisvc fvkklrqpsn
      121 ylivslalad lsvavavmpf vsvtdliggk wifghffcnv fiamdvmcct asimtlcvis
      181 idrylgitrp ltypvrqngk cmakmilsvw llsasitlpp lfgwaqnvnd dkvclisqdf
      241 gytiystava fyipmsvmlf myyqiykaar ksaakhkfpg fprvqpesvi slngvvklqk
      301 eveecanlsr llkherknis ifkreqkaat tlgiivgaft vcwlpfflls tarpficgts
      361 csciplwver tclwlgyans linpfiyaff nrdlrttyrs llqcqyrnin rklsaagmhe
      421 alklaerper sefvlqnsdh cgkkghdt
//
LOCUS       NP_001425357             938 aa            linear   ROD 21-APR-2025
DEFINITION  AP-2 complex subunit alpha-2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425357 XP_008758232
VERSION     NP_001425357.1
DBSOURCE    REFSEQ: accession NM_001438428.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Capella,P., Asensio,J., Troncoso,M., Sosa,M.A. and Seltzer,A.M.
  TITLE     Evidence on differential role for alpha 1 and alpha 2 subtypes of
            AP-2 adaptin in the central nervous system
  JOURNAL   Neurosci Lett 808, 137282 (2023)
   PUBMED   37127089
  REMARK    GeneRIF: Evidence on differential role for alpha 1 and alpha 2
            subtypes of AP-2 adaptin in the central nervous system.
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Marcello,E., Saraceno,C., Musardo,S., Vara,H., de la Fuente,A.G.,
            Pelucchi,S., Di Marino,D., Borroni,B., Tramontano,A.,
            Perez-Otano,I., Padovani,A., Giustetto,M., Gardoni,F. and Di
            Luca,M.
  TITLE     Endocytosis of synaptic ADAM10 in neuronal plasticity and
            Alzheimer's disease
  JOURNAL   J Clin Invest 123 (6), 2523-2538 (2013)
   PUBMED   23676497
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Duncker,S.V., Franz,C., Kuhn,S., Schulte,U., Campanelli,D.,
            Brandt,N., Hirt,B., Fakler,B., Blin,N., Ruth,P., Engel,J.,
            Marcotti,W., Zimmermann,U. and Knipper,M.
  TITLE     Otoferlin couples to clathrin-mediated endocytosis in mature
            cochlear inner hair cells
  JOURNAL   J Neurosci 33 (22), 9508-9519 (2013)
   PUBMED   23719817
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Saheki,Y. and De Camilli,P.
  TITLE     Synaptic vesicle endocytosis
  JOURNAL   Cold Spring Harb Perspect Biol 4 (9), a005645 (2012)
   PUBMED   22763746
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Takei,K., Mundigl,O., Daniell,L. and De Camilli,P.
  TITLE     The synaptic vesicle cycle: a single vesicle budding step involving
            clathrin and dynamin
  JOURNAL   J Cell Biol 133 (6), 1237-1250 (1996)
   PUBMED   8682861
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Voglmaier,S.M., Keen,J.H., Murphy,J.E., Ferris,C.D.,
            Prestwich,G.D., Snyder,S.H. and Theibert,A.B.
  TITLE     Inositol hexakisphosphate receptor identified as the clathrin
            assembly protein AP-2
  JOURNAL   Biochem Biophys Res Commun 187 (1), 158-163 (1992)
   PUBMED   1325787
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Bahler,M., Klein,R.L., Wang,J.K., Benfenati,F. and Greengard,P.
  TITLE     A novel synaptic vesicle-associated phosphoprotein: SVAPP-120
  JOURNAL   J Neurochem 57 (2), 423-430 (1991)
   PUBMED   2072093
  REMARK    Erratum:[J Neurochem 1991 Dec;57(6):2155]
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Tucker,K.L., Nathanson,K. and Kirchhausen,T.
  TITLE     Sequence of the rat alpha c large chain of the clathrin associated
            protein complex AP-2
  JOURNAL   Nucleic Acids Res 18 (17), 5306 (1990)
   PUBMED   2402467
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Kirchhausen,T., Nathanson,K.L., Matsui,W., Vaisberg,A., Chow,E.P.,
            Burne,C., Keen,J.H. and Davis,A.E.
  TITLE     Structural and functional division into two domains of the large
            (100- to 115-kDa) chains of the clathrin-associated protein complex
            AP-2
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2612-2616 (1989)
   PUBMED   2495531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_008758232.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.4146.1,
                                           SRR26643299.5110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..938
                     /product="AP-2 complex subunit alpha-2 isoform 1"
                     /note="adaptor protein complex AP-2, alpha 2 subunit; AP-2
                     complex subunit alpha-2; alpha2-adaptin; alpha-adaptin C;
                     100 kDa coated vesicle protein C; adaptor protein complex
                     AP-2 subunit alpha-2; adaptor-related protein complex 2,
                     alpha 2 subunit; adapter-related protein complex 2 alpha-2
                     subunit; clathrin assembly protein complex 2 alpha-C large
                     chain; plasma membrane adaptor HA2/AP2 adaptin alpha C
                     subunit; adapter-related protein complex 2 subunit
                     alpha-2"
                     /calculated_mol_wt=103914
     Region          29..590
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          331..354
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          368..397
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          407..433
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          615..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18484.3)"
     Region          716..819
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          825..933
                     /region_name="Alpha_adaptin_C"
                     /note="Alpha adaptin AP2, C-terminal domain; pfam02296"
                     /db_xref="CDD:426707"
     CDS             1..938
                     /gene="Ap2a2"
                     /coded_by="NM_001438428.1:124..2940"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:81637"
                     /db_xref="RGD:71015"
ORIGIN      
        1 mpavskgegm rglavfisdi rnckskeaei krinkelani rskfkgdkal dgyskkkyvc
       61 kllfifllgh didfghmeav nllssnryte kqigylfisv lvnsnselir linnaikndl
      121 asrnptfmgl alhcianvgs remaeafage ipkilvagdt mdsvkqsaal cllrlyrtsp
      181 dlvpmgdwts rvvhllndqh lgvvtaatsl ittlaqknpe efktsvslav srlsrivtsa
      241 stdlqdytyy fvpapwlsvk llrllqcypp pdpavrgrlt ecletilnka qeppkskkvq
      301 hsnaknavlf eaisliihhd sepnllvrac nqlgqflqhr etnlrylale smctlassef
      361 sheavkthie tvinalkter dvsvrqravd llyamcdrsn aqqivaemls yletadysir
      421 eeivlkvail aekyavdytw yvdtilnlir iagdyvseev wyrviqivin rddvqgyaak
      481 tvfealqapa chenlvkvgg yilgefgnli agdprsspli qfnllhskfh lcsvptrall
      541 lstyikfvnl fpevkatiqd vlrsdsqlkn advelqqrav eylrlstvas tdilatvlee
      601 mppfperess ilaklkkkkg pstvtdleet krersidvng gpepvpasts aastpspsad
      661 llglgavppa ptgppptsgg gllvdvfsds asavaplapg sednfarfvc knngvlfenq
      721 llqiglksef rqnlgrmfif ygnktstqfl nftptlicad dlqtnlnlqt kpvdptvdgg
      781 aqvqqvvnie cisdfteapv lniqfryggt fqnvsvklpi tlnkffqpte masqdffqrw
      841 kqlsnpqqev qnifkakhpm dteitkakii gfgsalleev dpnpanfvga giihtkttqi
      901 gcllrlepnl qaqmyrltlr tskdtvsqrl cellseqf
//
LOCUS       NP_001425287             188 aa            linear   ROD 21-APR-2025
DEFINITION  vascular endothelial growth factor B isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001425287 XP_006230974
VERSION     NP_001425287.1
DBSOURCE    REFSEQ: accession NM_001438358.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Tu,S., Wang,X.Y., Zeng,L.X., Shen,Z.J. and Zhang,Z.H.
  TITLE     LncRNA TINCR improves cardiac hypertrophy by regulating the
            miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway
  JOURNAL   Lab Invest 102 (3), 253-262 (2022)
   PUBMED   34732848
  REMARK    GeneRIF: LncRNA TINCR improves cardiac hypertrophy by regulating
            the miR-211-3p-VEGFB-SDF-1alpha-CXCR4 pathway.
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Shang,R., Lal,N., Lee,C.S., Zhai,Y., Puri,K., Seira,O.,
            Boushel,R.C., Sultan,I., Rasanen,M., Alitalo,K., Hussein,B. and
            Rodrigues,B.
  TITLE     Cardiac-specific VEGFB overexpression reduces lipoprotein lipase
            activity and improves insulin action in rat heart
  JOURNAL   Am J Physiol Endocrinol Metab 321 (6), E753-E765 (2021)
   PUBMED   34747201
  REMARK    GeneRIF: Cardiac-specific VEGFB overexpression reduces lipoprotein
            lipase activity and improves insulin action in rat heart.
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Lal,N., Chiu,A.P., Wang,F., Zhang,D., Jia,J., Wan,A., Vlodavsky,I.,
            Hussein,B. and Rodrigues,B.
  TITLE     Loss of VEGFB and its signaling in the diabetic heart is associated
            with increased cell death signaling
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (6), H1163-H1175 (2017)
   PUBMED   28314760
  REMARK    GeneRIF: Loss of VEGFB and its downstream signaling is an early
            event following hyperglycemia, is sustained with disease
            progression, and could explain diabetic cardiomyopathy.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Monastero,R., Garcia-Serrano,S., Lago-Sampedro,A.,
            Rodriguez-Pacheco,F., Colomo,N., Morcillo,S., Martin-Nunez,G.M.,
            Gomez-Zumaquero,J.M., Garcia-Fuentes,E., Soriguer,F.,
            Rojo-Martinez,G. and Garcia-Escobar,E.
  TITLE     Methylation patterns of Vegfb promoter are associated with gene and
            protein expression levels: the effects of dietary fatty acids
  JOURNAL   Eur J Nutr 56 (2), 715-726 (2017)
   PUBMED   26707994
  REMARK    GeneRIF: Data suggest that dietary fatty acids create
            epigenetic/nutrigenomic changes in methylation levels of CpG island
            at Vegfb promoter and changes in Vegfb expression in white
            adipocytes in vivo and in vitro, with particular up-regulation of
            DNA methylation by linoleic acid; Vegfb promoter methylation levels
            are closely related to Vegfb gene expression in visceral and
            subcutaneous adipose tissue.
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Rintala,J.M., Savikko,J., Palin,N., Rintala,S.E., Koskinen,P.K. and
            von Willebrand,E.
  TITLE     Oral Platelet-Derived Growth Factor and Vascular Endothelial Growth
            Factor Inhibitor Sunitinib Prevents Chronic Allograft Injury in
            Experimental Kidney Transplantation Model
  JOURNAL   Transplantation 100 (1), 103-110 (2016)
   PUBMED   26262503
  REMARK    GeneRIF: Combined inhibition of PGDF and VEGF with sunitinib
            prevents chronic rejection changes in experimental kidney
            transplantation.
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Nag,S., Eskandarian,M.R., Davis,J. and Eubanks,J.H.
  TITLE     Differential expression of vascular endothelial growth factor-A
            (VEGF-A) and VEGF-B after brain injury
  JOURNAL   J Neuropathol Exp Neurol 61 (9), 778-788 (2002)
   PUBMED   12230324
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Ikuta,T., Ariga,H. and Matsumoto,K.
  TITLE     Extracellular matrix tenascin-X in combination with vascular
            endothelial growth factor B enhances endothelial cell proliferation
  JOURNAL   Genes Cells 5 (11), 913-927 (2000)
   PUBMED   11122379
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Bellomo,D., Headrick,J.P., Silins,G.U., Paterson,C.A., Thomas,P.S.,
            Gartside,M., Mould,A., Cahill,M.M., Tonks,I.D., Grimmond,S.M.,
            Townson,S., Wells,C., Little,M., Cummings,M.C., Hayward,N.K. and
            Kay,G.F.
  TITLE     Mice lacking the vascular endothelial growth factor-B gene (Vegfb)
            have smaller hearts, dysfunctional coronary vasculature, and
            impaired recovery from cardiac ischemia
  JOURNAL   Circ Res 86 (2), E29-E35 (2000)
   PUBMED   10666423
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Olofsson,B., Pajusola,K., von Euler,G., Chilov,D., Alitalo,K. and
            Eriksson,U.
  TITLE     Genomic organization of the mouse and human genes for vascular
            endothelial growth factor B (VEGF-B) and characterization of a
            second splice isoform
  JOURNAL   J Biol Chem 271 (32), 19310-19317 (1996)
   PUBMED   8702615
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Olofsson,B., Pajusola,K., Kaipainen,A., von Euler,G., Joukov,V.,
            Saksela,O., Orpana,A., Pettersson,R.F., Alitalo,K. and Eriksson,U.
  TITLE     Vascular endothelial growth factor B, a novel growth factor for
            endothelial cells
  JOURNAL   Proc Natl Acad Sci U S A 93 (6), 2576-2581 (1996)
   PUBMED   8637916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006230974.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.3893.1,
                                           SRR22399484.1309898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..188
                     /product="vascular endothelial growth factor B isoform 1
                     precursor"
                     /note="VRF; VEGF-B; VEGF-related factor"
                     /calculated_mol_wt=19404
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2125
     Region          45..126
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(45..48,82,84..87,102..105)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(47,78,82,89,122,124)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(72,81)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     CDS             1..188
                     /gene="Vegfb"
                     /coded_by="NM_001438358.1:303..869"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:89811"
                     /db_xref="RGD:619799"
ORIGIN      
        1 mspllrrlll vallqlactq apvsqfdgps hqkkvvswid vyaratcqpr evvvplsmel
       61 mgnvvkqlvp scvtvqrcgg ccpddglecv pigqhqvrmq ilmiqypssq lgemsleehs
      121 qcecrpkrke savkpdsprt lcprctqrrq rpdprtcrcr crrrrflhcq grglelnpdt
      181 crcrklrr
//
LOCUS       NP_001425467             161 aa            linear   ROD 21-APR-2025
DEFINITION  sterile alpha motif domain-containing protein 12 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001425467
VERSION     NP_001425467.1
DBSOURCE    REFSEQ: accession NM_001438538.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840130,
                              SAMN16676787 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..161
                     /product="sterile alpha motif domain-containing protein 12
                     isoform 2"
                     /note="sterile alpha motif domain-containing protein 12"
                     /calculated_mol_wt=18112
     Region          72..146
                     /region_name="SAM_aveugle-like"
                     /note="SAM domain of aveugle-like subfamily; cd09510"
                     /db_xref="CDD:188909"
     Site            order(102..106,109..110,113,118,121..122)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188909"
     CDS             1..161
                     /gene="Samd12"
                     /gene_synonym="RGD1561402"
                     /coded_by="NM_001438538.1:42..527"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362910"
                     /db_xref="RGD:1561402"
ORIGIN      
        1 mavealhcgl npqsidhpah adgiklqieg egvesqsikn rnfqkvsdqk gtpkrlqgea
       61 etaksatvkl skpvalwtqq dvckwlkkhc pnqyhiyses fkqhditgra llrltdkkle
      121 rmgvaqenqr qhilqqvlql kvreevrnlq lltqastdcs p
//
LOCUS       NP_001100562             557 aa            linear   ROD 21-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001100562 XP_001062923 XP_221420
VERSION     NP_001100562.1
DBSOURCE    REFSEQ: accession NM_001107092.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473967.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_221420.2, XP_001062923.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..557
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 3"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=64005
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <293..>408
                     /region_name="COG5022"
                     /note="Myosin heavy chain [General function prediction
                     only]"
                     /db_xref="CDD:227355"
     Region          <385..>430
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..557
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001107092.1:116..1789"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqravlkf lakcrkkkkl faswhglqel tdarrvelkq qvddyvkrhp gsqmsdvasr
      481 elhaqaqerl qhyfmgraie eraqqhreal maqistnieq lmsmlyiclc fingithard
      541 vaskifrsat nslyssp
//
LOCUS       NP_001424693             598 aa            linear   ROD 21-APR-2025
DEFINITION  IQ calmodulin-binding motif-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001424693 XP_006248459
VERSION     NP_001424693.1
DBSOURCE    REFSEQ: accession NM_001437764.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Polymorphic variation of RPGRIP1L and IQCB1 as modifiers of
            X-linked retinitis pigmentosa caused by mutations in RPGR
  JOURNAL   Adv Exp Med Biol 723, 313-320 (2012)
   PUBMED   22183348
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Wang,X., Wang,H., Cao,M., Li,Z., Chen,X., Patenia,C., Gore,A.,
            Abboud,E.B., Al-Rajhi,A.A., Lewis,R.A., Lupski,J.R., Mardon,G.,
            Zhang,K., Muzny,D., Gibbs,R.A. and Chen,R.
  TITLE     Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
            mutations in patients with Leber congenital amaurosis
  JOURNAL   Hum Mutat 32 (12), 1450-1459 (2011)
   PUBMED   21901789
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Stone,E.M., Cideciyan,A.V., Aleman,T.S., Scheetz,T.E., Sumaroka,A.,
            Ehlinger,M.A., Schwartz,S.B., Fishman,G.A., Traboulsi,E.I.,
            Lam,B.L., Fulton,A.B., Mullins,R.F., Sheffield,V.C. and
            Jacobson,S.G.
  TITLE     Variations in NPHP5 in patients with nonsyndromic leber congenital
            amaurosis and Senior-Loken syndrome
  JOURNAL   Arch Ophthalmol 129 (1), 81-87 (2011)
   PUBMED   21220633
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Fahim,A.T., Bowne,S.J., Sullivan,L.S., Webb,K.D., Williams,J.T.,
            Wheaton,D.K., Birch,D.G. and Daiger,S.P.
  TITLE     Allelic heterogeneity and genetic modifier loci contribute to
            clinical variation in males with X-linked retinitis pigmentosa due
            to RPGR mutations
  JOURNAL   PLoS One 6 (8), e23021 (2011)
   PUBMED   21857984
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Otto,E.A., Helou,J., Allen,S.J., O'Toole,J.F., Wise,E.L.,
            Ashraf,S., Attanasio,M., Zhou,W., Wolf,M.T. and Hildebrandt,F.
  TITLE     Mutation analysis in nephronophthisis using a combined approach of
            homozygosity mapping, CEL I endonuclease cleavage, and direct
            sequencing
  JOURNAL   Hum Mutat 29 (3), 418-426 (2008)
   PUBMED   18076122
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Otto,E.A., Loeys,B., Khanna,H., Hellemans,J., Sudbrak,R., Fan,S.,
            Muerb,U., O'Toole,J.F., Helou,J., Attanasio,M., Utsch,B.,
            Sayer,J.A., Lillo,C., Jimeno,D., Coucke,P., De Paepe,A.,
            Reinhardt,R., Klages,S., Tsuda,M., Kawakami,I., Kusakabe,T.,
            Omran,H., Imm,A., Tippens,M., Raymond,P.A., Hill,J., Beales,P.,
            He,S., Kispert,A., Margolis,B., Williams,D.S., Swaroop,A. and
            Hildebrandt,F.
  TITLE     Nephrocystin-5, a ciliary IQ domain protein, is mutated in
            Senior-Loken syndrome and interacts with RPGR and calmodulin
  JOURNAL   Nat Genet 37 (3), 282-288 (2005)
   PUBMED   15723066
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_006248459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.476807.1,
                                           SRR26360186.1336005.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..598
                     /product="IQ calmodulin-binding motif-containing protein 1
                     isoform 1"
                     /note="IQ calmodulin-binding motif-containing protein 1;
                     IQ calmodulin-binding motif containing 1; nephrocystin 5"
                     /calculated_mol_wt=68499
     Region          239..>430
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          239..258
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          273..282
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          290..>316
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          294..314
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          323..369
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          392..410
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     CDS             1..598
                     /gene="Iqcb1"
                     /gene_synonym="NPHP5"
                     /coded_by="NM_001437764.1:123..1919"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:303915"
                     /db_xref="RGD:1310069"
ORIGIN      
        1 mkpagtdpri lslaaevaks peqnvpvill klkeiinntp lgsselkkvk qdiycydliq
       61 ycllvlsqds sriqggwsti sqltqilshc cvglepgedg eefykellps aaenflvlgr
      121 rlqtcfinat kgeeqdkllh ffqivtdslf wllgghiqli qnvlqsdhfl hllqtdnvqi
      181 gatvmtllqn ilqinsgnll kiegkalhsi ldeilfklls tpspvirsta tklllvlaes
      241 hqeilillrl sacykglrsl lnkqetltef srelrqlvdl ltpkiqqeve eqklhkaacl
      301 iqaywkgfqt rkrlkklpsa vialqrsfra krtkmlleln rqkeeedlrl rlqlqkqram
      361 rlsresrlsm leiihpgqve kynreieeks altiqkhwrg yrerknfrqq rpslteykaa
      421 vtlqravlkf lakcrkkkkl faswhglqel tdarrvelkq qvddyvkrhp gsqmsdvasr
      481 elhaqaqerl qhyfmgraie eraqqhreal maqistnieq lmkapslkea egkepeqfls
      541 rsrpvaakak qahlttlkhi qapwwkklge epgdemdvpk delsidlgtl figgtkpp
//
LOCUS       NP_001425118             480 aa            linear   ROD 22-APR-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 4 [Rattus
            norvegicus].
ACCESSION   NP_001425118 XP_063133019
VERSION     NP_001425118.1
DBSOURCE    REFSEQ: accession NM_001438189.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063133019.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2060846.1,
                                           SRR26360186.2096928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..480
                     /product="zinc finger protein with KRAB and SCAN domains
                     4"
                     /note="zinc finger protein 307; zinc finger protein with
                     KRAB and SCAN domains 4-like"
                     /calculated_mol_wt=54130
     Region          47..156
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          253..275
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          255..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(255,258,271,275)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          268..290
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          281..303
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          283..303
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <307..471
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          311..331
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(311,314,327,331)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(316,318,320,322..323,326..327,330,344,346,350..351,
                     354..355,358,372,374,376,378..379,382..383,386)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          339..359
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          367..387
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(422,425,438,442)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..480
                     /gene="Zkscan4"
                     /gene_synonym="Zfp307; Znf307"
                     /coded_by="NM_001438189.1:248..1690"
                     /db_xref="GeneID:291164"
                     /db_xref="RGD:1309004"
ORIGIN      
        1 marepgacaa lnapsaeegt gflvvkvepe easqlaeeps wlgspgpdrs rqrfrafryp
       61 daagprqals rlrelcrqwl rpdmhskeqi lellvleqfl tilpgelqaw vreqhpdsge
      121 evvalleyld rqldetppqv ptgewsrell cckvalvtss qdsqsshsqa mkslfkhesq
      181 eslecsplqa rglemkpetr glplaeeyke qkpeqtvwfl gedtvqists teaseqegkl
      241 qttqknatgn rrfychecgk sfaqssgltk hkrihtgekp yecedcgktf igssalvihq
      301 rvhtgekpye ceecgkvfsh ssnlikhqrt htgekpyecd dcgktftqsc sllehhkiht
      361 gekpfqcnlc gkafrrsshl lrhqrihgdk aapkllhget wegqsrvasl gdiveapety
      421 qcnecersft rsrsliehkk ihtgekpyqc dacgkgftrt sylvqhrrsh vgkklshsdl
//
LOCUS       NP_001178549             660 aa            linear   ROD 22-APR-2025
DEFINITION  zinc finger protein 418 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178549 XP_218208
VERSION     NP_001178549.1
DBSOURCE    REFSEQ: accession NM_001191620.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Singh,S.R., Meyer-Jens,M., Alizoti,E., Bacon,W.C., Davis,G.,
            Osinska,H., Gulick,J., Reischmann-Dusener,S., Orthey,E.,
            McLendon,P.M., Molkentin,J.D., Schlossarek,S., Robbins,J. and
            Carrier,L.
  TITLE     A high-throughput screening identifies ZNF418 as a novel regulator
            of the ubiquitin-proteasome system and autophagy-lysosomal pathway
  JOURNAL   Autophagy 17 (10), 3124-3139 (2021)
   PUBMED   33249983
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Pan,L., Sheng,M., Huang,Z., Zhu,Z., Xu,C., Teng,L., He,L., Gu,C.,
            Yi,C. and Li,J.
  TITLE     Zinc-finger protein 418 overexpression protects against cardiac
            hypertrophy and fibrosis
  JOURNAL   PLoS One 12 (10), e0186635 (2017)
   PUBMED   29065170
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_218208.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.1218.1,
                                           SRR26360172.2032105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation, longest
                                                protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..660
                     /product="zinc finger protein 418 isoform 1"
                     /calculated_mol_wt=76432
     Region          24..64
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(271,273,275,277..278,281..282,285,299,301,305..306,
                     309..310,313,327,329,331,333..334,337..338,341)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          290..647
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(383,385,387,389..390,393..394,397,411,413,417..418,
                     421..422,425,439,441,443,445..446,449..450,453)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          546..566
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          574..594
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(579,581,583,585..586,589..590,593,607,609,613..614,
                     617..618,621,635,637,639,641..642,645..646,649)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          602..622
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          630..650
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..660
                     /gene="Zfp418"
                     /gene_synonym="RGD1311663; ZNF418"
                     /coded_by="NM_001191620.2:178..2160"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:292548"
                     /db_xref="RGD:1311663"
ORIGIN      
        1 maavkhlaqi prctetgmic tqgcvtiedv tvyfsqeewk lldeaqrlly ldvmlenftl
       61 isslvyryea eaeektcaqs lsqteapqvr tpkqgqlrqk phpsdicitv lkdilhlndl
      121 pgqkpyltev ctkpqdhkhh raknwlkrdv dslvkscifh vagnpficsk igekfpaiwn
      181 llqpkdipng ekqnkikrgk afhrdknnse sdeykksssp qhrlheypgv csakggfesn
      241 sceqdlnkys papfrmdqte nrpyechvcg kwfgqkatlr ihqrrhtgek pykcgecgks
      301 fcqssnlseh crvhsgerpf eclecgkafg chssllrhqr thtgewpyec sdcgrlfrqi
      361 vslithqrth ttekpyecgq ceksfshkat ltvhqrvhtg ekpyhceacg ksfsqsanli
      421 khskihtgek pyecgecglc frqratlmkh qrthtserpy ecrecgkffk qyfyliehrr
      481 ihtttefyec eqcgksytqk atlirhqrvh tgespykcee cgkafeyksr lkrhqrthtg
      541 erpyecakcg kffresynla ehqkihtkak pyhcdqcgkc fsrradlvkh qrvhtgerpy
      601 tcgecgktfs rttnlvqhrr ihtgerpyec dqcgksfsqv stltrhqllh tgekpykcsk
//
LOCUS       NP_001425158             961 aa            linear   ROD 22-APR-2025
DEFINITION  SPOC domain containing 1 [Rattus norvegicus].
ACCESSION   NP_001425158
VERSION     NP_001425158.1
DBSOURCE    REFSEQ: accession NM_001438229.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2457133.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..961
                     /product="SPOC domain containing 1"
                     /note="SPOC domain containing 1, pseudogene 1; SPOC
                     domain-containing protein 1"
                     /calculated_mol_wt=105274
     Region          354..463
                     /region_name="TFIIS_M"
                     /note="Transcription factor S-II (TFIIS), central domain;
                     pfam07500"
                     /db_xref="CDD:462184"
     Region          631..767
                     /region_name="SPOC_SF"
                     /note="SPOC (Spen paralog and ortholog C-terminal) domain
                     superfamily; cl45902"
                     /db_xref="CDD:459247"
     CDS             1..961
                     /gene="Spocd1"
                     /gene_synonym="RGD1560989; Spocd1-ps1"
                     /coded_by="NM_001438229.1:658..3543"
                     /db_xref="GeneID:313060"
                     /db_xref="RGD:1560989"
ORIGIN      
        1 megasspslr qaitvegmvs pkgdgrvpth skeglsekdl ppspvlpprr srrkcrkcsi
       61 cpqdeeesyf slklgqrpsg dcqpvqgppe rappeafagp qsllsskntg leepagswae
      121 calesevenm ffakdvlppd sldhlfefpg lfageplslv tqdppqspal ypevltgdst
      181 kqqkaqsgfv vgspgtpphp erpedkaqpg srmelgqgla tpadfcassl eplggldgas
      241 qeqrrpkhvn krpwgspdns sqdhpeeark ndcsrpvcsg sgikllgavs srqpgqtepm
      301 eelkassarr krkpmtahpa ccqsdpseae nvqplqqrae dpgereimpl dvgvrstvvr
      361 amqevlwtrt qelpnlelre devegiaegi eaalfhltqd tnlrykskyr nllfnlrdpr
      421 ndlflkvahc dvtpkdlvqm ssiqlapkel srwrdqekrr sldiieqqqk epyrlpaskl
      481 thkgeveipr dsdqmltled lmepmvprec slqalttple dttdwhqhhl cdsscqictg
      541 gkggrkadsg sqpelqagis hsmdqksstk lpafspaamn eeentiqkap spvpvsspem
      601 lkvgktppke pqdrlqmpag pkpvppsppp wegsldmfsi khfrtkaqli sghscqlvqg
      661 lpevirsagr lppnhiwdll dsmgpsrakd icvvrlsphg srdiqnyrll ysylndkqch
      721 clatvhhvkm vlmplpafep lparlrplgg pgletahtsl llavlfpede lpdtalsspv
      781 wskapktvsf skkverirys sedrrseatp rgpspheeep kqslaqgnla prsvcapqsl
      841 srgrgsepgw gqwsseagwh ysqhysqhpn pagpmfpgis rgqhlhrasc fhhdlhqhlk
      901 vlvtmshqfq aslrpqgqds clpstvvsvv pdppgsssgp ldgggsgcpl pegpdplelp
      961 e
//
LOCUS       NP_001418756             253 aa            linear   ROD 22-APR-2025
DEFINITION  ankyrin repeat domain 53 [Rattus norvegicus].
ACCESSION   NP_001418756
VERSION     NP_001418756.1
DBSOURCE    REFSEQ: accession NM_001431827.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Kim,S. and Jang,C.Y.
  TITLE     ANKRD53 interacts with DDA3 and regulates chromosome integrity
            during mitosis
  JOURNAL   Biochem Biophys Res Commun 470 (3), 484-491 (2016)
   PUBMED   26820536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160898.1, SRR26643293.23664.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..253
                     /product="ankyrin repeat domain 53"
                     /note="ankyrin repeat domain-containing protein 53"
                     /calculated_mol_wt=29315
     CDS             1..253
                     /gene="Ankrd53"
                     /gene_synonym="RGD1561200"
                     /coded_by="NM_001431827.1:921..1682"
                     /db_xref="GeneID:500230"
                     /db_xref="RGD:1561200"
ORIGIN      
        1 mwkhdkkvfa remerlktlk kkltimeyry ltefqkeqqi mredlfrkwl qskvlartlg
       61 savskqnasv qpwslasktl ehqiiksfqy psieaqlksl pspmvppkpv ykqskisrpk
      121 iwncsanpsr pritdighpq girlgvhpep ykehdfcrfl emtrnklgga clrtvdcqlv
      181 kpvpqlpfev mirvlypgtr pyrmkvpqgf yardilkvpq krhlgdtctn tvamslrdtf
      241 depflaslea cqt
//
LOCUS       NP_001416630             360 aa            linear   ROD 22-APR-2025
DEFINITION  cannabinoid receptor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001416630 XP_063144399
VERSION     NP_001416630.1
DBSOURCE    REFSEQ: accession NM_001429701.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Smereczanska,M., Domian,N., Lewandowska,A. and Kasacka,I.
  TITLE     Comparative assessment of CacyBP/SIP, beta-catenin and cannabinoid
            receptors in the adrenals of hypertensive rats
  JOURNAL   J Cell Mol Med 28 (10), e18376 (2024)
   PUBMED   38780511
  REMARK    GeneRIF: Comparative assessment of CacyBP/SIP, beta-catenin and
            cannabinoid receptors in the adrenals of hypertensive rats.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Uzuneser,T.C., Szkudlarek,H.J., Jones,M.J., Nashed,M.G.,
            Clement,T., Wang,H., Ojima,I., Rushlow,W.J. and Laviolette,S.R.
  TITLE     Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex
  JOURNAL   Cereb Cortex 33 (6), 2470-2484 (2023)
   PUBMED   35650684
  REMARK    GeneRIF: Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Kang,H., Jiang,S., Song,Q. and Zhang,Y.
  TITLE     [Activation of cannabinoid receptor 2 alleviates acute lung injury
            in rats with lipopolysaccharide-induced sepsis]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (9), 1374-1380 (2022)
   PUBMED   36210711
  REMARK    GeneRIF: [Activation of cannabinoid receptor 2 alleviates acute
            lung injury in rats with lipopolysaccharide-induced sepsis].
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Karan,A.A., Spivak,Y.S., Gerasimov,K.A., Suleymanova,E.M.,
            Volobueva,M.N., Kvichansky,A.A., Vinogradova,L.V. and
            Bolshakov,A.P.
  TITLE     CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex
  JOURNAL   Mol Neurobiol 58 (8), 4028-4037 (2021)
   PUBMED   33907944
  REMARK    GeneRIF: CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex.
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Gigante,I., Tutino,V., Russo,F., De Nunzio,V., Coletta,S.,
            Armentano,R., Crovace,A., Caruso,M.G., Orlando,A. and
            Notarnicola,M.
  TITLE     Cannabinoid Receptors Overexpression in a Rat Model of Irritable
            Bowel Syndrome (IBS) after Treatment with a Ketogenic Diet
  JOURNAL   Int J Mol Sci 22 (6), 2880 (2021)
   PUBMED   33809047
  REMARK    GeneRIF: Cannabinoid Receptors Overexpression in a Rat Model of
            Irritable Bowel Syndrome (IBS) after Treatment with a Ketogenic
            Diet.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Esposito,G., Ligresti,A., Izzo,A.A., Bisogno,T., Ruvo,M., Di
            Rosa,M., Di Marzo,V. and Iuvone,T.
  TITLE     The endocannabinoid system protects rat glioma cells against HIV-1
            Tat protein-induced cytotoxicity. Mechanism and regulation
  JOURNAL   J Biol Chem 277 (52), 50348-50354 (2002)
   PUBMED   12388547
  REMARK    GeneRIF: protects rat glioma cells against HIV-1 Tat
            protein-induced cytotoxicity
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Brown,S.M., Wager-Miller,J. and Mackie,K.
  TITLE     Cloning and molecular characterization of the rat CB2 cannabinoid
            receptor
  JOURNAL   Biochim Biophys Acta 1576 (3), 255-264 (2002)
   PUBMED   12084572
  REMARK    GeneRIF: The rat peripheral cannabinoid receptor (rCB2) was cloned
            from a Sprague-Dawley rat spleen cDNA library and when translated,
            encodes a protein of 410 amino acids.
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Clayton,N., Marshall,F.H., Bountra,C. and O'Shaughnessy,C.T.
  TITLE     CB1 and CB2 cannabinoid receptors are implicated in inflammatory
            pain
  JOURNAL   Pain 96 (3), 253-260 (2002)
   PUBMED   11972997
  REMARK    GeneRIF: CB1 and CB2 cannabinoid receptors are implicated in
            inflammatory pain.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Carlisle,S.J., Marciano-Cabral,F., Staab,A., Ludwick,C. and
            Cabral,G.A.
  TITLE     Differential expression of the CB2 cannabinoid receptor by rodent
            macrophages and macrophage-like cells in relation to cell
            activation
  JOURNAL   Int Immunopharmacol 2 (1), 69-82 (2002)
   PUBMED   11789671
  REMARK    GeneRIF: levels of the cannabinoid receptor type 2 in cells of
            macrophage lineage undergo major modulatory changes in relation to
            cell activation
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Griffin,G., Tao,Q. and Abood,M.E.
  TITLE     Cloning and pharmacological characterization of the rat CB(2)
            cannabinoid receptor
  JOURNAL   J Pharmacol Exp Ther 292 (3), 886-894 (2000)
   PUBMED   10688601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 25, 2024 this sequence version replaced XP_063144399.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.8168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..360
                     /product="cannabinoid receptor 2 isoform 1"
                     /note="peripheral cannabinoid receptor; CB2 receptor;
                     cannabinoid receptor 2 (macrophage)"
                     /calculated_mol_wt=39228
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          34..310
                     /region_name="7tmA_CB2"
                     /note="cannabinoid receptor subtype 2, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15341"
                     /db_xref="CDD:320463"
     Site            34..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320463"
     Region          69..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320463"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            order(90,109..110,113..114,117,194,258,265,282,285)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320463"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320463"
     Region          148..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320463"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          186..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320463"
     Site            189..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          238..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320463"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          278..303
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320463"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          327..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34972; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     CDS             1..360
                     /gene="Cnr2"
                     /gene_synonym="CB-2; CB2; CB2C; CNR2C; rCB2"
                     /coded_by="NM_001429701.1:366..1448"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:57302"
                     /db_xref="RGD:619713"
ORIGIN      
        1 magcrelelt ngsngglefn pmkeymilsd aqqiavavlc tlmgllsale nvavlylils
       61 sqrlrrkpsy lfigslagad flasvifacn fvifhvfhgv dsrnifllki gsvtmtftas
      121 vgsllltavd rylclcyppt ykalvtrgra lvalgvmwvl salisylplm gwtccpspcs
      181 elfplipndy llgwllfiai lfsgiiytyg yvlwkahqhv aslaehqdrq vpgiarmrld
      241 vrlaktlglv mavllicwfp alalmghslv ttlsdkvkea fafcsmlclv nsminpiiya
      301 lrsgeirsaa qhcltgwkky lqglgsegke eapkssvtet eaevktttgp gsrtpgcsnc
//
LOCUS       NP_001157614             360 aa            linear   ROD 22-APR-2025
DEFINITION  cannabinoid receptor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001157614
VERSION     NP_001157614.1
DBSOURCE    REFSEQ: accession NM_001164142.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Smereczanska,M., Domian,N., Lewandowska,A. and Kasacka,I.
  TITLE     Comparative assessment of CacyBP/SIP, beta-catenin and cannabinoid
            receptors in the adrenals of hypertensive rats
  JOURNAL   J Cell Mol Med 28 (10), e18376 (2024)
   PUBMED   38780511
  REMARK    GeneRIF: Comparative assessment of CacyBP/SIP, beta-catenin and
            cannabinoid receptors in the adrenals of hypertensive rats.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Uzuneser,T.C., Szkudlarek,H.J., Jones,M.J., Nashed,M.G.,
            Clement,T., Wang,H., Ojima,I., Rushlow,W.J. and Laviolette,S.R.
  TITLE     Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex
  JOURNAL   Cereb Cortex 33 (6), 2470-2484 (2023)
   PUBMED   35650684
  REMARK    GeneRIF: Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Kang,H., Jiang,S., Song,Q. and Zhang,Y.
  TITLE     [Activation of cannabinoid receptor 2 alleviates acute lung injury
            in rats with lipopolysaccharide-induced sepsis]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (9), 1374-1380 (2022)
   PUBMED   36210711
  REMARK    GeneRIF: [Activation of cannabinoid receptor 2 alleviates acute
            lung injury in rats with lipopolysaccharide-induced sepsis].
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Karan,A.A., Spivak,Y.S., Gerasimov,K.A., Suleymanova,E.M.,
            Volobueva,M.N., Kvichansky,A.A., Vinogradova,L.V. and
            Bolshakov,A.P.
  TITLE     CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex
  JOURNAL   Mol Neurobiol 58 (8), 4028-4037 (2021)
   PUBMED   33907944
  REMARK    GeneRIF: CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex.
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Gigante,I., Tutino,V., Russo,F., De Nunzio,V., Coletta,S.,
            Armentano,R., Crovace,A., Caruso,M.G., Orlando,A. and
            Notarnicola,M.
  TITLE     Cannabinoid Receptors Overexpression in a Rat Model of Irritable
            Bowel Syndrome (IBS) after Treatment with a Ketogenic Diet
  JOURNAL   Int J Mol Sci 22 (6), 2880 (2021)
   PUBMED   33809047
  REMARK    GeneRIF: Cannabinoid Receptors Overexpression in a Rat Model of
            Irritable Bowel Syndrome (IBS) after Treatment with a Ketogenic
            Diet.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Esposito,G., Ligresti,A., Izzo,A.A., Bisogno,T., Ruvo,M., Di
            Rosa,M., Di Marzo,V. and Iuvone,T.
  TITLE     The endocannabinoid system protects rat glioma cells against HIV-1
            Tat protein-induced cytotoxicity. Mechanism and regulation
  JOURNAL   J Biol Chem 277 (52), 50348-50354 (2002)
   PUBMED   12388547
  REMARK    GeneRIF: protects rat glioma cells against HIV-1 Tat
            protein-induced cytotoxicity
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Brown,S.M., Wager-Miller,J. and Mackie,K.
  TITLE     Cloning and molecular characterization of the rat CB2 cannabinoid
            receptor
  JOURNAL   Biochim Biophys Acta 1576 (3), 255-264 (2002)
   PUBMED   12084572
  REMARK    GeneRIF: The rat peripheral cannabinoid receptor (rCB2) was cloned
            from a Sprague-Dawley rat spleen cDNA library and when translated,
            encodes a protein of 410 amino acids.
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Clayton,N., Marshall,F.H., Bountra,C. and O'Shaughnessy,C.T.
  TITLE     CB1 and CB2 cannabinoid receptors are implicated in inflammatory
            pain
  JOURNAL   Pain 96 (3), 253-260 (2002)
   PUBMED   11972997
  REMARK    GeneRIF: CB1 and CB2 cannabinoid receptors are implicated in
            inflammatory pain.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Carlisle,S.J., Marciano-Cabral,F., Staab,A., Ludwick,C. and
            Cabral,G.A.
  TITLE     Differential expression of the CB2 cannabinoid receptor by rodent
            macrophages and macrophage-like cells in relation to cell
            activation
  JOURNAL   Int Immunopharmacol 2 (1), 69-82 (2002)
   PUBMED   11789671
  REMARK    GeneRIF: levels of the cannabinoid receptor type 2 in cells of
            macrophage lineage undergo major modulatory changes in relation to
            cell activation
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Griffin,G., Tao,Q. and Abood,M.E.
  TITLE     Cloning and pharmacological characterization of the rat CB(2)
            cannabinoid receptor
  JOURNAL   J Pharmacol Exp Ther 292 (3), 886-894 (2000)
   PUBMED   10688601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.8170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..360
                     /product="cannabinoid receptor 2 isoform 1"
                     /note="peripheral cannabinoid receptor; CB2 receptor;
                     cannabinoid receptor 2 (macrophage)"
                     /calculated_mol_wt=39228
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          34..310
                     /region_name="7tmA_CB2"
                     /note="cannabinoid receptor subtype 2, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15341"
                     /db_xref="CDD:320463"
     Site            34..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320463"
     Region          69..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320463"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            order(90,109..110,113..114,117,194,258,265,282,285)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320463"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320463"
     Region          148..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320463"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          186..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320463"
     Site            189..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          238..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320463"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          278..303
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320463"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          327..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34972; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     CDS             1..360
                     /gene="Cnr2"
                     /gene_synonym="CB-2; CB2; CB2C; CNR2C; rCB2"
                     /coded_by="NM_001164142.4:173..1255"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:57302"
                     /db_xref="RGD:619713"
ORIGIN      
        1 magcrelelt ngsngglefn pmkeymilsd aqqiavavlc tlmgllsale nvavlylils
       61 sqrlrrkpsy lfigslagad flasvifacn fvifhvfhgv dsrnifllki gsvtmtftas
      121 vgsllltavd rylclcyppt ykalvtrgra lvalgvmwvl salisylplm gwtccpspcs
      181 elfplipndy llgwllfiai lfsgiiytyg yvlwkahqhv aslaehqdrq vpgiarmrld
      241 vrlaktlglv mavllicwfp alalmghslv ttlsdkvkea fafcsmlclv nsminpiiya
      301 lrsgeirsaa qhcltgwkky lqglgsegke eapkssvtet eaevktttgp gsrtpgcsnc
//
LOCUS       NP_001157615             360 aa            linear   ROD 22-APR-2025
DEFINITION  cannabinoid receptor 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001157615
VERSION     NP_001157615.1
DBSOURCE    REFSEQ: accession NM_001164143.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Smereczanska,M., Domian,N., Lewandowska,A. and Kasacka,I.
  TITLE     Comparative assessment of CacyBP/SIP, beta-catenin and cannabinoid
            receptors in the adrenals of hypertensive rats
  JOURNAL   J Cell Mol Med 28 (10), e18376 (2024)
   PUBMED   38780511
  REMARK    GeneRIF: Comparative assessment of CacyBP/SIP, beta-catenin and
            cannabinoid receptors in the adrenals of hypertensive rats.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Uzuneser,T.C., Szkudlarek,H.J., Jones,M.J., Nashed,M.G.,
            Clement,T., Wang,H., Ojima,I., Rushlow,W.J. and Laviolette,S.R.
  TITLE     Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex
  JOURNAL   Cereb Cortex 33 (6), 2470-2484 (2023)
   PUBMED   35650684
  REMARK    GeneRIF: Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Kang,H., Jiang,S., Song,Q. and Zhang,Y.
  TITLE     [Activation of cannabinoid receptor 2 alleviates acute lung injury
            in rats with lipopolysaccharide-induced sepsis]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (9), 1374-1380 (2022)
   PUBMED   36210711
  REMARK    GeneRIF: [Activation of cannabinoid receptor 2 alleviates acute
            lung injury in rats with lipopolysaccharide-induced sepsis].
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Karan,A.A., Spivak,Y.S., Gerasimov,K.A., Suleymanova,E.M.,
            Volobueva,M.N., Kvichansky,A.A., Vinogradova,L.V. and
            Bolshakov,A.P.
  TITLE     CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex
  JOURNAL   Mol Neurobiol 58 (8), 4028-4037 (2021)
   PUBMED   33907944
  REMARK    GeneRIF: CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex.
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Gigante,I., Tutino,V., Russo,F., De Nunzio,V., Coletta,S.,
            Armentano,R., Crovace,A., Caruso,M.G., Orlando,A. and
            Notarnicola,M.
  TITLE     Cannabinoid Receptors Overexpression in a Rat Model of Irritable
            Bowel Syndrome (IBS) after Treatment with a Ketogenic Diet
  JOURNAL   Int J Mol Sci 22 (6), 2880 (2021)
   PUBMED   33809047
  REMARK    GeneRIF: Cannabinoid Receptors Overexpression in a Rat Model of
            Irritable Bowel Syndrome (IBS) after Treatment with a Ketogenic
            Diet.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Esposito,G., Ligresti,A., Izzo,A.A., Bisogno,T., Ruvo,M., Di
            Rosa,M., Di Marzo,V. and Iuvone,T.
  TITLE     The endocannabinoid system protects rat glioma cells against HIV-1
            Tat protein-induced cytotoxicity. Mechanism and regulation
  JOURNAL   J Biol Chem 277 (52), 50348-50354 (2002)
   PUBMED   12388547
  REMARK    GeneRIF: protects rat glioma cells against HIV-1 Tat
            protein-induced cytotoxicity
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Brown,S.M., Wager-Miller,J. and Mackie,K.
  TITLE     Cloning and molecular characterization of the rat CB2 cannabinoid
            receptor
  JOURNAL   Biochim Biophys Acta 1576 (3), 255-264 (2002)
   PUBMED   12084572
  REMARK    GeneRIF: The rat peripheral cannabinoid receptor (rCB2) was cloned
            from a Sprague-Dawley rat spleen cDNA library and when translated,
            encodes a protein of 410 amino acids.
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Clayton,N., Marshall,F.H., Bountra,C. and O'Shaughnessy,C.T.
  TITLE     CB1 and CB2 cannabinoid receptors are implicated in inflammatory
            pain
  JOURNAL   Pain 96 (3), 253-260 (2002)
   PUBMED   11972997
  REMARK    GeneRIF: CB1 and CB2 cannabinoid receptors are implicated in
            inflammatory pain.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Carlisle,S.J., Marciano-Cabral,F., Staab,A., Ludwick,C. and
            Cabral,G.A.
  TITLE     Differential expression of the CB2 cannabinoid receptor by rodent
            macrophages and macrophage-like cells in relation to cell
            activation
  JOURNAL   Int Immunopharmacol 2 (1), 69-82 (2002)
   PUBMED   11789671
  REMARK    GeneRIF: levels of the cannabinoid receptor type 2 in cells of
            macrophage lineage undergo major modulatory changes in relation to
            cell activation
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Griffin,G., Tao,Q. and Abood,M.E.
  TITLE     Cloning and pharmacological characterization of the rat CB(2)
            cannabinoid receptor
  JOURNAL   J Pharmacol Exp Ther 292 (3), 886-894 (2000)
   PUBMED   10688601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760494,
                              SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..360
                     /product="cannabinoid receptor 2 isoform 1"
                     /note="peripheral cannabinoid receptor; CB2 receptor;
                     cannabinoid receptor 2 (macrophage)"
                     /calculated_mol_wt=39228
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          34..310
                     /region_name="7tmA_CB2"
                     /note="cannabinoid receptor subtype 2, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15341"
                     /db_xref="CDD:320463"
     Site            34..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320463"
     Region          69..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320463"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            order(90,109..110,113..114,117,194,258,265,282,285)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320463"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320463"
     Region          148..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320463"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          186..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320463"
     Site            189..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          238..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320463"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          278..303
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320463"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          327..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34972; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     CDS             1..360
                     /gene="Cnr2"
                     /gene_synonym="CB-2; CB2; CB2C; CNR2C; rCB2"
                     /coded_by="NM_001164143.3:271..1353"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:57302"
                     /db_xref="RGD:619713"
ORIGIN      
        1 magcrelelt ngsngglefn pmkeymilsd aqqiavavlc tlmgllsale nvavlylils
       61 sqrlrrkpsy lfigslagad flasvifacn fvifhvfhgv dsrnifllki gsvtmtftas
      121 vgsllltavd rylclcyppt ykalvtrgra lvalgvmwvl salisylplm gwtccpspcs
      181 elfplipndy llgwllfiai lfsgiiytyg yvlwkahqhv aslaehqdrq vpgiarmrld
      241 vrlaktlglv mavllicwfp alalmghslv ttlsdkvkea fafcsmlclv nsminpiiya
      301 lrsgeirsaa qhcltgwkky lqglgsegke eapkssvtet eaevktttgp gsrtpgcsnc
//
LOCUS       NP_076460                871 aa            linear   ROD 22-APR-2025
DEFINITION  transient receptor potential cation channel subfamily V member 4
            [Rattus norvegicus].
ACCESSION   NP_076460
VERSION     NP_076460.1
DBSOURCE    REFSEQ: accession NM_023970.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Chen,Z., Liu,B., Zhou,D., Lei,M., Yang,J., Hu,Z. and Duan,W.
  TITLE     AQP4 regulates ferroptosis and oxidative stress of Muller cells in
            diabetic retinopathy by regulating TRPV4
  JOURNAL   Exp Cell Res 439 (1), 114087 (2024)
   PUBMED   38735619
  REMARK    GeneRIF: AQP4 regulates ferroptosis and oxidative stress of Muller
            cells in diabetic retinopathy by regulating TRPV4.
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Bihari,S., Costell,M.H., Bouchier,T., Behm,D.J., Burgert,M., Ye,G.,
            Bersten,A.D., Puukila,S., Cavallaro,E., Sprecher,D.L. and
            Dixon,D.L.
  TITLE     Evaluation of GSK2789917-induced TRPV4 inhibition in animal models
            of fluid induced lung injury
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 397 (5), 3461-3475 (2024)
   PUBMED   37966569
  REMARK    GeneRIF: Evaluation of GSK2789917-induced TRPV4 inhibition in
            animal models of fluid induced lung injury.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Philip,N., Yun,X., Pi,H., Murray,S., Hill,Z., Fonticella,J.,
            Perez,P., Zhang,C., Pathmasiri,W., Sumner,S., Servinsky,L.,
            Jiang,H., Huetsch,J.C., Oldham,W.M., Visovatti,S., Leary,P.J.,
            Gharib,S.A., Brittain,E., Simpson,C.E., Le,A., Shimoda,L.A. and
            Suresh,K.
  TITLE     Fatty acid metabolism promotes TRPV4 activity in lung microvascular
            endothelial cells in pulmonary arterial hypertension
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 326 (3), L252-L265 (2024)
   PUBMED   38226418
  REMARK    GeneRIF: Fatty acid metabolism promotes TRPV4 activity in lung
            microvascular endothelial cells in pulmonary arterial hypertension.
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Li,X., Lu,K., Guo,S., Xue,S. and Lian,F.
  TITLE     TRPV4 blockade alleviates endoplasmic reticulum stress mediated
            apoptosis in hypoxia-induced cardiomyocyte injury
  JOURNAL   Cell Signal 114, 110973 (2024)
   PUBMED   37981067
  REMARK    GeneRIF: TRPV4 blockade alleviates endoplasmic reticulum stress
            mediated apoptosis in hypoxia-induced cardiomyocyte injury.
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Shen,X., Zhang,H., Chen,D.T. and Cao,Y.L.
  TITLE     [Preliminary study of TRPV4 affects chondrocyte degeneration]
  JOURNAL   Zhongguo Gu Shang 36 (10), 990-995 (2023)
   PUBMED   37881934
  REMARK    GeneRIF: [Preliminary study of TRPV4 affects chondrocyte
            degeneration].
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Strotmann,R., Schultz,G. and Plant,T.D.
  TITLE     Ca2+-dependent potentiation of the nonselective cation channel
            TRPV4 is mediated by a C-terminal calmodulin binding site
  JOURNAL   J Biol Chem 278 (29), 26541-26549 (2003)
   PUBMED   12724311
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mizuno,A., Matsumoto,N., Imai,M. and Suzuki,M.
  TITLE     Impaired osmotic sensation in mice lacking TRPV4
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C96-C101 (2003)
   PUBMED   12777254
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Xu,H., Zhao,H., Tian,W., Yoshida,K., Roullet,J.B. and Cohen,D.M.
  TITLE     Regulation of a transient receptor potential (TRP) channel by
            tyrosine phosphorylation. SRC family kinase-dependent tyrosine
            phosphorylation of TRPV4 on TYR-253 mediates its response to
            hypotonic stress
  JOURNAL   J Biol Chem 278 (13), 11520-11527 (2003)
   PUBMED   12538589
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Liedtke,W., Choe,Y., Marti-Renom,M.A., Bell,A.M., Denis,C.S.,
            Sali,A., Hudspeth,A.J., Friedman,J.M. and Heller,S.
  TITLE     Vanilloid receptor-related osmotically activated channel (VR-OAC),
            a candidate vertebrate osmoreceptor
  JOURNAL   Cell 103 (3), 525-535 (2000)
   PUBMED   11081638
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Strotmann,R., Harteneck,C., Nunnenmacher,K., Schultz,G. and
            Plant,T.D.
  TITLE     OTRPC4, a nonselective cation channel that confers sensitivity to
            extracellular osmolarity
  JOURNAL   Nat Cell Biol 2 (10), 695-702 (2000)
   PUBMED   11025659
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF263521.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF263521.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..871
                     /product="transient receptor potential cation channel
                     subfamily V member 4"
                     /note="transient receptor potential cation channel,
                     subfamily 5, member 4; VR-OAC; osm-9-like TRP channel 4;
                     vanilloid receptor-related osmotically-activated channel;
                     osmosensitive transient receptor potential channel 4;
                     vanilloid receptor-related osmotically activated channel
                     (Vroac); transient receptor potential cation channel subf
                     V memb 4"
                     /calculated_mol_wt=97879
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          103..834
                     /region_name="TRPV4"
                     /note="Transient Receptor Potential channel, Vanilloid
                     subfamily (TRPV), type 4; cd22195"
                     /db_xref="CDD:411979"
     Region          110..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPK8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          191..231
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(237,239,243..244,247..249,251..252,256,259,268,284,
                     286,290..291,294..296,298..299,303,306,318,320,322,
                     326..327,330..332,343..344,348)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          237..268
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          237..266
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            order(247,249,272..273,281..282,284,294,331,338,341,409,
                     411..414,490,548,551..552,555,573,575,577,579..580,
                     583..584,587,602..603,606,610,614,620,624,628,631,
                     634..635,671,674..675,678,680,688,692,694..696,698..700,
                     705,707..708,710..712,715,718..719,721..723,725,785,788)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:411979"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPK8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          284..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          284..313
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          369..398
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            470..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            508..534
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            548..568
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            573..593
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            609..636
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          679..682
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:O35433"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            694..722
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPK8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Region          812..831
                     /region_name="Interaction with calmodulin and ITPR3.
                     /evidence=ECO:0000250|UniProtKB:Q9HBA0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPK8; propagated from
                     UniProtKB/Swiss-Prot (Q9ERZ8.1)"
     CDS             1..871
                     /gene="Trpv4"
                     /gene_synonym="Otrpc4; Vroac"
                     /coded_by="NM_023970.1:94..2709"
                     /db_xref="GeneID:66026"
                     /db_xref="RGD:69337"
ORIGIN      
        1 madpgdgpra apgdvaeppg desgtsggea fplsslanlf egeegsssls pvdasrpagp
       61 gdgrpnlrmk fqgafrkgvp npidllestl yessvvpgpk kapmdslfdy gtyrhhpsdn
      121 krwrrkvvek qpqspkapap qpppilkvfn rpilfdivsr gstadldgll syllthkkrl
      181 tdeefrepst gktclpkall nlsngrndti pvlldiaert gnmrefinsp frdiyyrgqt
      241 alhiaierrc khyvellvaq gadvhaqarg rffqpkdegg yfyfgelpls laactnqphi
      301 vnyltenphk kadmrrqdsr gntvlhalva iadntrentk fvtkmydlll lkcsrlfpds
      361 nletvlnndg lsplmmaakt gkigvfqhii rrevtdedtr hlsrkfkdwa ygpvysslyd
      421 lssldtcgee vsvleilvyn skienrheml avepinellr dkwrkfgavs fyinvvsylc
      481 amviftltay yqplegtppy pyrttvdylr lagevitllt gvlffftsik dlfmkkcpgv
      541 nslfvdgsfq llyfiysvlv vvsaalylag ieaylavmvf alvlgwmnal yftrglkltg
      601 tysimiqkil fkdlfrfllv yllfmigyas alvtllnpct nmkvcnedqs nctvpsypac
      661 rdsetfsafl ldlfkltigm gdlemlssak ypvvfilllv tyiiltfvll lnmlialmge
      721 tvgqvskesk hiwklqwatt ildiersfpv flrkafrsge mvtvgkssdg tpdrrwcfrv
      781 devnwshwnq nlgiinedpg kseiyqyygf shtmgrlrrd rwssvvprvv elnknsgtde
      841 vvvpldnlgn pncdghqqgy apkwraedap l
//
LOCUS       NP_001101302             384 aa            linear   ROD 22-APR-2025
DEFINITION  prostaglandin E synthase 2 [Rattus norvegicus].
ACCESSION   NP_001101302 XP_001078154 XP_231144
VERSION     NP_001101302.1
DBSOURCE    REFSEQ: accession NM_001107832.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Shah,M.D., Gnanaraj,C., Khan,M.S. and Iqbal,M.
  TITLE     Dillenia suffruticosa L. Impedes Carbon Tetrachloride-Induced
            Hepatic Damage by Modulating Oxidative Stress and Inflammatory
            Markers in Rats
  JOURNAL   J Environ Pathol Toxicol Oncol 34 (2), 133-152 (2015)
   PUBMED   26081032
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Majed,B.H. and Khalil,R.A.
  TITLE     Molecular mechanisms regulating the vascular prostacyclin pathways
            and their adaptation during pregnancy and in the newborn
  JOURNAL   Pharmacol Rev 64 (3), 540-582 (2012)
   PUBMED   22679221
  REMARK    Review article
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Hirata,T. and Narumiya,S.
  TITLE     Prostanoids as regulators of innate and adaptive immunity
  JOURNAL   Adv Immunol 116, 143-174 (2012)
   PUBMED   23063076
  REMARK    Review article
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Jiang,H., Deng,C.S., Zhang,M. and Xia,J.
  TITLE     Curcumin-attenuated trinitrobenzene sulphonic acid induces chronic
            colitis by inhibiting expression of cyclooxygenase-2
  JOURNAL   World J Gastroenterol 12 (24), 3848-3853 (2006)
   PUBMED   16804969
  REMARK    GeneRIF: Curcumin has therapeutic effects on TNBS acid-induced
            colitis, the mechanisms seem to be related to COX-2 inhibition and
            PGE(2) improvement.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Leppilampi,M., Parkkila,S., Karttunen,T., Gut,M.O., Gros,G. and
            Sjoblom,M.
  TITLE     Carbonic anhydrase isozyme-II-deficient mice lack the duodenal
            bicarbonate secretory response to prostaglandin E2
  JOURNAL   Proc Natl Acad Sci U S A 102 (42), 15247-15252 (2005)
   PUBMED   16217040
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Giannico,G., Mendez,M. and LaPointe,M.C.
  TITLE     Regulation of the membrane-localized prostaglandin E synthases
            mPGES-1 and mPGES-2 in cardiac myocytes and fibroblasts
  JOURNAL   Am J Physiol Heart Circ Physiol 288 (1), H165-H174 (2005)
   PUBMED   15358613
  REMARK    GeneRIF: Prostaglandin E synthase(PGES)-1 and -2 are colocalized
            with COX-2 in cardiac myocytes and fibroblasts.
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Watanabe,K., Ohkubo,H., Niwa,H., Tanikawa,N., Koda,N., Ito,S. and
            Ohmiya,Y.
  TITLE     Essential 110Cys in active site of membrane-associated
            prostaglandin E synthase-2
  JOURNAL   Biochem Biophys Res Commun 306 (2), 577-581 (2003)
   PUBMED   12804604
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Hu,J., Meng,Q., Roy,S.K., Raha,A., Hu,J., Zhang,J., Hashimoto,K.
            and Kalvakolanu,D.V.
  TITLE     A novel transactivating factor that regulates
            interferon-gamma-dependent gene expression
  JOURNAL   J Biol Chem 277 (33), 30253-30263 (2002)
   PUBMED   12050152
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474001.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001078154.1, XP_231144.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ231959.1, SRR8487226.130213.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..384
                     /product="prostaglandin E synthase 2"
                     /EC_number="5.3.99.3"
                     /calculated_mol_wt=43321
     Region          100..176
                     /region_name="GST_N_mPGES2"
                     /note="GST_N family; microsomal Prostaglandin E synthase
                     Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored
                     dimeric protein containing a CXXC motif which catalyzes
                     the isomerization of PGH2 to PGE2. Unlike cytosolic PGE
                     synthase (cPGES) and microsomal...; cd03040"
                     /db_xref="CDD:239338"
     Site            order(106,108..112)
                     /site_type="active"
                     /note="GRX-like active site [active]"
                     /db_xref="CDD:239338"
     Site            order(107..109,113..114,116..117,121,132..134,138,165,169)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239338"
     Site            order(146,162..163,165..166,169)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239338"
     Region          223..371
                     /region_name="GST_C_mPGES2"
                     /note="C-terminal, alpha helical domain of microsomal
                     Prostaglandin E synthase Type 2; cd03197"
                     /db_xref="CDD:198306"
     Site            order(224,228,235,240,295,297)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198306"
     Site            order(234,238,262..263,266,329,338,341..342)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198306"
     Site            order(245..246,249..250,259,262..263,342,346)
                     /site_type="active"
                     /note="GRX-like active site [active]"
                     /db_xref="CDD:198306"
     CDS             1..384
                     /gene="Ptges2"
                     /coded_by="NM_001107832.1:512..1666"
                     /db_xref="GeneID:311865"
                     /db_xref="RGD:1310836"
ORIGIN      
        1 maqaarvawv lgssrcalse glltrpwtql saqsragftr aaagnrgasi rkgsprllgv
       61 aalalggalg lyhtvrwhlr sqdlhaersa vqlslsnrlq ltlyqyktcp fcskvrafld
      121 fhslpyqvve vnpvrrteik fssyrkvpil vaqegdslqq lndssviisa lktylvsgqp
      181 leeiityypp mkamndqgke vtefgnkywl mldqkeaqqm yggkeartee mkwrqwaddw
      241 lvhlispnvy rtpaealasf dyivregkfg aveatmakyv gaaamyfisk rlksrhhlqd
      301 dvrvdlyeaa nkwvtavgkd rpfmggqkpn ladlavygvl rvmegleafd dlmrhshiqp
      361 wylrmeraik eassmhcmhp nckd
//
LOCUS       NP_037164                523 aa            linear   ROD 22-APR-2025
DEFINITION  excitatory amino acid transporter 3 [Rattus norvegicus].
ACCESSION   NP_037164 XP_346584
VERSION     NP_037164.3
DBSOURCE    REFSEQ: accession NM_013032.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Wang,J., Zielewicz,L., Dong,Y. and Grewer,C.
  TITLE     Pre-Steady-State Kinetics and Reverse Transport in Rat Glutamate
            Transporter EAAC1 with an Immobilized Transport Domain
  JOURNAL   Neurochem Res 47 (1), 148-162 (2022)
   PUBMED   33550531
  REMARK    GeneRIF: Pre-Steady-State Kinetics and Reverse Transport in Rat
            Glutamate Transporter EAAC1 with an Immobilized Transport Domain.
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Magi,S., Piccirillo,S., Maiolino,M., Lariccia,V. and Amoroso,S.
  TITLE     NCX1 and EAAC1 transporters are involved in the protective action
            of glutamate in an in vitro Alzheimer's disease-like model
  JOURNAL   Cell Calcium 91, 102268 (2020)
   PUBMED   32827867
  REMARK    GeneRIF: NCX1 and EAAC1 transporters are involved in the protective
            action of glutamate in an in vitro Alzheimer's disease-like model.
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Malik,A.R., Szydlowska,K., Nizinska,K., Asaro,A., van Vliet,E.A.,
            Popp,O., Dittmar,G., Fritsche-Guenther,R., Kirwan,J.A., Nykjaer,A.,
            Lukasiuk,K., Aronica,E. and Willnow,T.E.
  TITLE     SorCS2 Controls Functional Expression of Amino Acid Transporter
            EAAT3 and Protects Neurons from Oxidative Stress and
            Epilepsy-Induced Pathology
  JOURNAL   Cell Rep 26 (10), 2792-2804 (2019)
   PUBMED   30840898
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Ottestad-Hansen,S., Hu,Q.X., Follin-Arbelet,V.V., Bentea,E.,
            Sato,H., Massie,A., Zhou,Y. and Danbolt,N.C.
  TITLE     The cystine-glutamate exchanger (xCT, Slc7a11) is expressed in
            significant concentrations in a subpopulation of astrocytes in the
            mouse brain
  JOURNAL   Glia 66 (5), 951-970 (2018)
   PUBMED   29350434
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Wei,Y.B., Melas,P.A., Villaescusa,J.C., Liu,J.J., Xu,N.,
            Christiansen,S.H., Elbrond-Bek,H., Woldbye,D.P., Wegener,G.,
            Mathe,A.A. and Lavebratt,C.
  TITLE     MicroRNA 101b Is Downregulated in the Prefrontal Cortex of a
            Genetic Model of Depression and Targets the Glutamate Transporter
            SLC1A1 (EAAT3) in Vitro
  JOURNAL   Int J Neuropsychopharmacol 19 (12) (2016)
   PUBMED   27507301
  REMARK    GeneRIF: miR-101b targets the neuronal glutamate transporter
            SLC1A1.  Both mRNA and protein levels of SLC1A1 were found to be
            upregulated in the prefrontal cortex of rats genetically
            predisposed to develop major depressive disorder.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Palos,T.P., Ramachandran,B., Boado,R. and Howard,B.D.
  TITLE     Rat C6 and human astrocytic tumor cells express a neuronal type of
            glutamate transporter
  JOURNAL   Brain Res Mol Brain Res 37 (1-2), 297-303 (1996)
   PUBMED   8738164
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Kiryu,S., Yao,G.L., Morita,N., Kato,H. and Kiyama,H.
  TITLE     Nerve injury enhances rat neuronal glutamate transporter
            expression: identification by differential display PCR
  JOURNAL   J Neurosci 15 (12), 7872-7878 (1995)
   PUBMED   8613726
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Kanai,Y., Bhide,P.G., DiFiglia,M. and Hediger,M.A.
  TITLE     Neuronal high-affinity glutamate transport in the rat central
            nervous system
  JOURNAL   Neuroreport 6 (17), 2357-2362 (1995)
   PUBMED   8747153
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Kanai,Y., Stelzner,M., Nussberger,S., Khawaja,S., Hebert,S.C.,
            Smith,C.P. and Hediger,M.A.
  TITLE     The neuronal and epithelial human high affinity glutamate
            transporter. Insights into structure and mechanism of transport
  JOURNAL   J Biol Chem 269 (32), 20599-20606 (1994)
   PUBMED   7914198
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061743.1.
            
            On Jun 10, 2007 this sequence version replaced NP_037164.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061743.1, U39555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..523
                     /product="excitatory amino acid transporter 3"
                     /note="excitatory amino-acid carrier 1; sodium-dependent
                     glutamate/aspartate transporter 3; Solute carrier family 1
                     A1 (brain glutamate transporter); solute carrier family 1
                     (neuronal/epithelial high affinity glutamate transporter,
                     system Xag), member 1"
                     /calculated_mol_wt=56641
     Site            19..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Region          51..467
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51907.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51907.1)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51907.1)"
     Site            205..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            238..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            286..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            353..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            440..461
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51907.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51906; propagated from
                     UniProtKB/Swiss-Prot (P51907.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51906; propagated from
                     UniProtKB/Swiss-Prot (P51907.1)"
     CDS             1..523
                     /gene="Slc1a1"
                     /gene_synonym="Eaac1; Eaat3; REAAC1"
                     /coded_by="NM_013032.3:90..1661"
                     /db_xref="GeneID:25550"
                     /db_xref="RGD:3696"
ORIGIN      
        1 mgkptssgcd wrrflrnhwl llstvaavvl givvgvlvrg hselsnldkf yfafpgeilm
       61 rmlklvilpl iissmitgva aldsnvsgki glravvyyfs ttviavilgi vlvvsikpgv
      121 tqkvneinrt gktpevstvd amldlirnmf penlvqacfq qyktkreevk pasdpggnqt
      181 evsvttamtt msenktkeyk ivglysdgin vlgliifclv fglvigkmge kgqilvdffn
      241 alsdatmkiv qiimcympig ilfliagkii evedweifrk lglymatvls glaihslvvl
      301 pliyfivvrk npfrfalgma qalltalmis sssatlpvtf rcaeeknhvd kritrfvlpv
      361 gatinmdgta lyeavaavfi aqlngmdlsi gqiitisita taasigaagv pqaglvtmvi
      421 vlsavglpae dvtliiavdw lldrfrtmvn vlgdafgtgi veklskkele qvdvssevni
      481 vnpfalepti ldnedsdtkk syvnggfsvd ksdtisftqt sqf
//
LOCUS       NP_036717                422 aa            linear   ROD 22-APR-2025
DEFINITION  5-hydroxytryptamine receptor 1A [Rattus norvegicus].
ACCESSION   NP_036717
VERSION     NP_036717.2
DBSOURCE    REFSEQ: accession NM_012585.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Zhu,C.P., Liu,S.Q., Wang,K.Q., Xiong,H.L., Aristu-Zabalza,P.,
            Boyer-Diaz,Z., Feng,J.F., Song,S.H., Luo,C., Chen,W.S., Zhang,X.,
            Dong,W.H., Gracia-Sancho,J. and Xie,W.F.
  TITLE     Targeting 5-Hydroxytryptamine Receptor 1A in the Portal Vein to
            Decrease Portal Hypertension
  JOURNAL   Gastroenterology 167 (5), 993-1007 (2024)
   PUBMED   38906512
  REMARK    GeneRIF: Targeting 5-Hydroxytryptamine Receptor 1A in the Portal
            Vein to Decrease Portal Hypertension.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Nikolaus,S., Chao,O.Y., Henke,J., Beu,M., Fazari,B., Almeida,F.R.,
            Abdel-Hafiz,L., Antke,C., Hautzel,H., Mamlins,E., Muller,H.W.,
            Huston,J.P., von Gall,C. and Giesel,F.L.
  TITLE     5-HT1A and 5-HT2A receptor effects on recognition memory,
            motor/exploratory behaviors, emotionality and regional dopamine
            transporter binding in the rat
  JOURNAL   Behav Brain Res 469, 115051 (2024)
   PUBMED   38777263
  REMARK    GeneRIF: 5-HT1A and 5-HT2A receptor effects on recognition memory,
            motor/exploratory behaviors, emotionality and regional dopamine
            transporter binding in the rat.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Malheiros,J., Amaral,C., da Silva,L.S., Guinsburg,R. and Covolan,L.
  TITLE     Neonatal nociceptive stimulation results in pain sensitization,
            reduction of hippocampal 5-HT1A receptor, and p-CREB expression in
            adult female rats
  JOURNAL   Behav Brain Res 466, 114975 (2024)
   PUBMED   38552745
  REMARK    GeneRIF: Neonatal nociceptive stimulation results in pain
            sensitization, reduction of hippocampal 5-HT1A receptor, and p-CREB
            expression in adult female rats.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Valipour,H., Jahromi,G.P., Mohammadi,A. and Meftahi,G.H.
  TITLE     Effects of the suppression of 5-HT1A receptors in the left, right,
            or bilateral basolateral amygdala on memory consolidation in
            chronic stress in male rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 397 (5), 3049-3064 (2024)
   PUBMED   37874340
  REMARK    GeneRIF: Effects of the suppression of 5-HT1A receptors in the
            left, right, or bilateral basolateral amygdala on memory
            consolidation in chronic stress in male rats.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Munawar,N., Bitar,M.S. and Masocha,W.
  TITLE     Activation of 5-HT1A Receptors Normalizes the Overexpression of
            Presynaptic 5-HT1A Receptors and Alleviates Diabetic Neuropathic
            Pain
  JOURNAL   Int J Mol Sci 24 (18), 14334 (2023)
   PUBMED   37762636
  REMARK    GeneRIF: Activation of 5-HT1A Receptors Normalizes the
            Overexpression of Presynaptic 5-HT1A Receptors and Alleviates
            Diabetic Neuropathic Pain.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Charest,A., Wainer,B.H. and Albert,P.R.
  TITLE     Cloning and differentiation-induced expression of a murine
            serotonin1A receptor in a septal cell line
  JOURNAL   J Neurosci 13 (12), 5164-5171 (1993)
   PUBMED   8254366
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Penington,N.J., Kelly,J.S. and Fox,A.P.
  TITLE     Whole-cell recordings of inwardly rectifying K+ currents activated
            by 5-HT1A receptors on dorsal raphe neurones of the adult rat
  JOURNAL   J Physiol 469, 387-405 (1993)
   PUBMED   8271204
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Aune,T.M., McGrath,K.M., Sarr,T., Bombara,M.P. and Kelley,K.A.
  TITLE     Expression of 5HT1a receptors on activated human T cells.
            Regulation of cyclic AMP levels and T cell proliferation by
            5-hydroxytryptamine
  JOURNAL   J Immunol 151 (3), 1175-1183 (1993)
   PUBMED   8393041
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Albert,P.R., Zhou,Q.Y., Van Tol,H.H., Bunzow,J.R. and Civelli,O.
  TITLE     Cloning, functional expression, and mRNA tissue distribution of the
            rat 5-hydroxytryptamine1A receptor gene
  JOURNAL   J Biol Chem 265 (10), 5825-5832 (1990)
   PUBMED   2156831
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Verge,D., Daval,G., Marcinkiewicz,M., Patey,A., el Mestikawy,S.,
            Gozlan,H. and Hamon,M.
  TITLE     Quantitative autoradiography of multiple 5-HT1 receptor subtypes in
            the brain of control or 5,7-dihydroxytryptamine-treated rats
  JOURNAL   J Neurosci 6 (12), 3474-3482 (1986)
   PUBMED   2947981
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Oct 3, 2022 this sequence version replaced NP_036717.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR26360194.1822363.1,
                                        SRR26643298.9522.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..422
                     /product="5-hydroxytryptamine receptor 1A"
                     /note="5-HT1A; 5-HT-1A; serotonin receptor 1A;
                     5-hydroxytryptamine (serotonin) receptor 1A, G
                     protein-coupled; serotonin 1A receptor; serotonin 5-HT1A
                     receptor"
                     /calculated_mol_wt=46325
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19327.1)"
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19327.1)"
     Site            24
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19327.1)"
     Region          37..411
                     /region_name="7tmA_5-HT1A_vertebrates"
                     /note="serotonin receptor subtype 1A from vertebrates,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15330"
                     /db_xref="CDD:320453"
     Region          38..64
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320453"
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          71..97
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320453"
     Site            74..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Site            108..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          109..139
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320453"
     Site            order(112..113,116..117,120..121,187,199,203,358,361..362,
                     368,379,382..383,386,390)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320453"
     Region          133..135
                     /region_name="DRY motif, important for ligand-induced
                     conformation changes.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          151..173
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320453"
     Site            153..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          192..221
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320453"
     Site            194..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          235..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          338..368
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320453"
     Site            347..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          379..404
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320453"
     Site            379..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     Region          396..400
                     /region_name="NPxxY motif, important for ligand-induced
                     conformation changes and signaling.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P19327.1)"
     CDS             1..422
                     /gene="Htr1a"
                     /gene_synonym="5HT1A; RAT5HT1A"
                     /coded_by="NM_012585.2:713..1981"
                     /db_xref="GeneID:24473"
                     /db_xref="RGD:2845"
ORIGIN      
        1 mdvfsfgqgn nttasqepfg tggnvtsisd vtfsyqvits lllgtlifca vlgnacvvaa
       61 ialerslqnv anyligslav tdlmvsvlvl pmaalyqvln kwtlgqvtcd lfialdvlcc
      121 tssilhlcai aldrywaitd pidyvnkrtp rraaalislt wligflisip pmlgwrtped
      181 rsdpdactis kdhgytiyst fgafyiplll mlvlygrifr aarfrirktv rkvekkgagt
      241 slgtssappp kkslngqpgs gdwrrcaenr avgtpctnga vrqgddeatl evievhrvgn
      301 skehlplpse sgsnsyapac lerknernae akrkmalare rktvktlgii mgtfilcwlp
      361 ffivalvlpf censchmpal lgaiinwlgy snsllnpviy ayfnkdfqna fkkiikckfc
      421 rr
//
LOCUS       NP_065418                410 aa            linear   ROD 22-APR-2025
DEFINITION  cannabinoid receptor 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_065418
VERSION     NP_065418.3
DBSOURCE    REFSEQ: accession NM_020543.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Smereczanska,M., Domian,N., Lewandowska,A. and Kasacka,I.
  TITLE     Comparative assessment of CacyBP/SIP, beta-catenin and cannabinoid
            receptors in the adrenals of hypertensive rats
  JOURNAL   J Cell Mol Med 28 (10), e18376 (2024)
   PUBMED   38780511
  REMARK    GeneRIF: Comparative assessment of CacyBP/SIP, beta-catenin and
            cannabinoid receptors in the adrenals of hypertensive rats.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Uzuneser,T.C., Szkudlarek,H.J., Jones,M.J., Nashed,M.G.,
            Clement,T., Wang,H., Ojima,I., Rushlow,W.J. and Laviolette,S.R.
  TITLE     Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex
  JOURNAL   Cereb Cortex 33 (6), 2470-2484 (2023)
   PUBMED   35650684
  REMARK    GeneRIF: Identification of a novel fatty acid binding protein-5-CB2
            receptor-dependent mechanism regulating anxiety behaviors in the
            prefrontal cortex.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kang,H., Jiang,S., Song,Q. and Zhang,Y.
  TITLE     [Activation of cannabinoid receptor 2 alleviates acute lung injury
            in rats with lipopolysaccharide-induced sepsis]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (9), 1374-1380 (2022)
   PUBMED   36210711
  REMARK    GeneRIF: [Activation of cannabinoid receptor 2 alleviates acute
            lung injury in rats with lipopolysaccharide-induced sepsis].
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Karan,A.A., Spivak,Y.S., Gerasimov,K.A., Suleymanova,E.M.,
            Volobueva,M.N., Kvichansky,A.A., Vinogradova,L.V. and
            Bolshakov,A.P.
  TITLE     CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex
  JOURNAL   Mol Neurobiol 58 (8), 4028-4037 (2021)
   PUBMED   33907944
  REMARK    GeneRIF: CB2 receptors modulate seizure-induced expression of
            pro-inflammatory cytokines in the hippocampus but not neocortex.
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Gigante,I., Tutino,V., Russo,F., De Nunzio,V., Coletta,S.,
            Armentano,R., Crovace,A., Caruso,M.G., Orlando,A. and
            Notarnicola,M.
  TITLE     Cannabinoid Receptors Overexpression in a Rat Model of Irritable
            Bowel Syndrome (IBS) after Treatment with a Ketogenic Diet
  JOURNAL   Int J Mol Sci 22 (6), 2880 (2021)
   PUBMED   33809047
  REMARK    GeneRIF: Cannabinoid Receptors Overexpression in a Rat Model of
            Irritable Bowel Syndrome (IBS) after Treatment with a Ketogenic
            Diet.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Esposito,G., Ligresti,A., Izzo,A.A., Bisogno,T., Ruvo,M., Di
            Rosa,M., Di Marzo,V. and Iuvone,T.
  TITLE     The endocannabinoid system protects rat glioma cells against HIV-1
            Tat protein-induced cytotoxicity. Mechanism and regulation
  JOURNAL   J Biol Chem 277 (52), 50348-50354 (2002)
   PUBMED   12388547
  REMARK    GeneRIF: protects rat glioma cells against HIV-1 Tat
            protein-induced cytotoxicity
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Brown,S.M., Wager-Miller,J. and Mackie,K.
  TITLE     Cloning and molecular characterization of the rat CB2 cannabinoid
            receptor
  JOURNAL   Biochim Biophys Acta 1576 (3), 255-264 (2002)
   PUBMED   12084572
  REMARK    GeneRIF: The rat peripheral cannabinoid receptor (rCB2) was cloned
            from a Sprague-Dawley rat spleen cDNA library and when translated,
            encodes a protein of 410 amino acids.
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Clayton,N., Marshall,F.H., Bountra,C. and O'Shaughnessy,C.T.
  TITLE     CB1 and CB2 cannabinoid receptors are implicated in inflammatory
            pain
  JOURNAL   Pain 96 (3), 253-260 (2002)
   PUBMED   11972997
  REMARK    GeneRIF: CB1 and CB2 cannabinoid receptors are implicated in
            inflammatory pain.
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Carlisle,S.J., Marciano-Cabral,F., Staab,A., Ludwick,C. and
            Cabral,G.A.
  TITLE     Differential expression of the CB2 cannabinoid receptor by rodent
            macrophages and macrophage-like cells in relation to cell
            activation
  JOURNAL   Int Immunopharmacol 2 (1), 69-82 (2002)
   PUBMED   11789671
  REMARK    GeneRIF: levels of the cannabinoid receptor type 2 in cells of
            macrophage lineage undergo major modulatory changes in relation to
            cell activation
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Griffin,G., Tao,Q. and Abood,M.E.
  TITLE     Cloning and pharmacological characterization of the rat CB(2)
            cannabinoid receptor
  JOURNAL   J Pharmacol Exp Ther 292 (3), 886-894 (2000)
   PUBMED   10688601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Aug 13, 2009 this sequence version replaced NP_065418.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF218846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN06680444
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..410
                     /product="cannabinoid receptor 2 isoform 2"
                     /note="peripheral cannabinoid receptor; CB2 receptor;
                     cannabinoid receptor 2 (macrophage)"
                     /calculated_mol_wt=45032
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          34..310
                     /region_name="7tmA_CB2"
                     /note="cannabinoid receptor subtype 2, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15341"
                     /db_xref="CDD:320463"
     Site            34..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320463"
     Region          69..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320463"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            order(90,109..110,113..114,117,194,258,265,282,285)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320463"
     Site            105..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320463"
     Region          148..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320463"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          186..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320463"
     Site            189..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          238..268
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320463"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Region          278..303
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320463"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47936; propagated from
                     UniProtKB/Swiss-Prot (Q9QZN9.3)"
     CDS             1..410
                     /gene="Cnr2"
                     /gene_synonym="CB-2; CB2; CB2C; CNR2C; rCB2"
                     /coded_by="NM_020543.4:1..1233"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:57302"
                     /db_xref="RGD:619713"
ORIGIN      
        1 magcrelelt ngsngglefn pmkeymilsd aqqiavavlc tlmgllsale nvavlylils
       61 sqrlrrkpsy lfigslagad flasvifacn fvifhvfhgv dsrnifllki gsvtmtftas
      121 vgsllltavd rylclcyppt ykalvtrgra lvalgvmwvl salisylplm gwtccpspcs
      181 elfplipndy llgwllfiai lfsgiiytyg yvlwkahqhv aslaehqdrq vpgiarmrld
      241 vrlaktlglv mavllicwfp alalmghslv ttlsdkvkea fafcsmlclv nsminpiiya
      301 lrsgeirsaa qhcltgwkky lqglgsegke eapkssvtet eaetlvlkdk qelggdcllr
      361 tssihspmls ladsanrqdv rphcpeeltw wcsvrrpisl pnkagqstll
//
LOCUS       NP_062259                686 aa            linear   ROD 23-APR-2025
DEFINITION  protein-glutamine gamma-glutamyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_062259
VERSION     NP_062259.3
DBSOURCE    REFSEQ: accession NM_019386.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Da Silva Lodge,M., Pullen,N., Pereira,M. and Johnson,T.S.
  TITLE     Urinary levels of pro-fibrotic transglutaminase 2 (TG2) may help
            predict progression of chronic kidney disease
  JOURNAL   PLoS One 17 (1), e0262104 (2022)
   PUBMED   35041708
  REMARK    GeneRIF: Urinary levels of pro-fibrotic transglutaminase 2 (TG2)
            may help predict progression of chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Orr,A.N., Thompson,J.M., Lyttle,J.M. and Watts,S.W.
  TITLE     Transglutaminases Are Active in Perivascular Adipose Tissue
  JOURNAL   Int J Mol Sci 22 (5), 2649 (2021)
   PUBMED   33808023
  REMARK    GeneRIF: Transglutaminases Are Active in Perivascular Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Shi,W., Que,Y., Lv,D., Bi,S., Xu,Z., Wang,D. and Zhang,Z.
  TITLE     Overexpression of TG2 enhances the differentiation of
            ectomesenchymal stem cells into neuron-like cells and promotes
            functional recovery in adult rats following spinal cord injury
  JOURNAL   Mol Med Rep 20 (3), 2763-2773 (2019)
   PUBMED   31322240
  REMARK    GeneRIF: Immunofluorescence staining and western blot analyses
            demonstrated that Tgm2 overexpression had beneficial effects on the
            rate of Ectomesenchymal stem cells (EMSCs) neurogenesis, and that
            the proliferative capacity of Tgm2 EMSCs was higher than that of
            controls.
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Li,Z.Y., Xiao,L., Lin,G., Tang,J., Chen,Y., Chen,L., Li,B., Wu,M.,
            Liu,S., Huang,C., Ferrandon,D. and Li,Z.
  TITLE     Contribution of tissue transglutaminase to the severity of hepatic
            fibrosis resulting from Schistosoma japonicum infection through the
            regulation of IL-33/ST2 expression
  JOURNAL   Parasit Vectors 12 (1), 302 (2019)
   PUBMED   31200771
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Serrano,R.L., Yu,W., Graham,R.M., Bryan,R.L. and Terkeltaub,R.
  TITLE     A vascular smooth muscle cell X-box binding protein 1 and
            transglutaminase 2 regulatory circuit limits neointimal hyperplasia
  JOURNAL   PLoS One 14 (4), e0212235 (2019)
   PUBMED   30943188
  REMARK    GeneRIF: Cultured Xbp1-deficient vascular smooth muscle cells
            (VSMCs) demonstrated decreased levels of TG2 protein, in
            association with increased TG2 polyubiquitination. Moreover,
            IRE1alpha, and TG2-specific transamidation cross-links were
            increased in carotid artery neointima in Xbp1fl/fl SM22alpha-CRE+
            mice. Cultured TG2-deficient VSMCs had decreased Xbp1 associated
            with increased IRE1alpha, and increased migration in respons...
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Citron,B.A., SantaCruz,K.S., Davies,P.J. and Festoff,B.W.
  TITLE     Intron-exon swapping of transglutaminase mRNA and neuronal Tau
            aggregation in Alzheimer's disease
  JOURNAL   J Biol Chem 276 (5), 3295-3301 (2001)
   PUBMED   11013236
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Ou,H., Haendeler,J., Aebly,M.R., Kelly,L.A., Cholewa,B.C.,
            Koike,G., Kwitek-Black,A., Jacob,H.J., Berk,B.C. and Miano,J.M.
  TITLE     Retinoic acid-induced tissue transglutaminase and apoptosis in
            vascular smooth muscle cells
  JOURNAL   Circ Res 87 (10), 881-887 (2000)
   PUBMED   11073883
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Nakaoka,H., Perez,D.M., Baek,K.J., Das,T., Husain,A., Misono,K.,
            Im,M.J. and Graham,R.M.
  TITLE     Gh: a GTP-binding protein with transglutaminase activity and
            receptor signaling function
  JOURNAL   Science 264 (5165), 1593-1596 (1994)
   PUBMED   7911253
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Phillips,M.A., Qin,Q., Mehrpouyan,M. and Rice,R.H.
  TITLE     Keratinocyte transglutaminase membrane anchorage: analysis of
            site-directed mutants
  JOURNAL   Biochemistry 32 (41), 11057-11063 (1993)
   PUBMED   8105889
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Thacher,S.M. and Rice,R.H.
  TITLE     Keratinocyte-specific transglutaminase of cultured human epidermal
            cells: relation to cross-linked envelope formation and terminal
            differentiation
  JOURNAL   Cell 40 (3), 685-695 (1985)
   PUBMED   2578891
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Nov 27, 2020 this sequence version replaced NP_062259.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062062.1, SRR22582416.1518996.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..686
                     /product="protein-glutamine gamma-glutamyltransferase 2"
                     /EC_number="2.3.2.13"
                     /EC_number="3.5.1.44"
                     /note="tissue-type transglutaminase; transglutaminase 2, C
                     polypeptide; glutamine gamma-glutamyltransferase 2;
                     tTgase; TGase 2; TGase II; protein G(h); isopeptidase
                     TGM2; protein G alpha(h); transglutaminase II; tissue
                     transglutaminase; protein-glutamine deamidase TGM2;
                     protein-glutamine dopaminyltransferase TGM2;
                     protein-glutamine serotonyltransferase TGM2;
                     protein-glutamine histaminyltransferase TGM2;
                     protein-glutamine noradrenalinyltransferase TGM2"
                     /calculated_mol_wt=76804
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P21980; propagated from
                     UniProtKB/Swiss-Prot (Q9WVJ6.1)"
     Region          8..122
                     /region_name="Transglut_N"
                     /note="Transglutaminase family; pfam00868"
                     /db_xref="CDD:459971"
     Region          269..361
                     /region_name="TGc"
                     /note="Transglutaminase/protease-like homologues;
                     smart00460"
                     /db_xref="CDD:214673"
     Site            468
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P21981; propagated from
                     UniProtKB/Swiss-Prot (Q9WVJ6.1)"
     Region          473..572
                     /region_name="Transglut_C"
                     /note="Transglutaminase family, C-terminal ig like domain;
                     pfam00927"
                     /db_xref="CDD:460002"
     Site            516
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P52181; propagated from
                     UniProtKB/Swiss-Prot (Q9WVJ6.1)"
     Region          586..685
                     /region_name="Transglut_C"
                     /note="Transglutaminase family, C-terminal ig like domain;
                     pfam00927"
                     /db_xref="CDD:460002"
     CDS             1..686
                     /gene="Tgm2"
                     /gene_synonym="TgaseII; TGII; tTG"
                     /coded_by="NM_019386.3:57..2117"
                     /db_xref="GeneID:56083"
                     /db_xref="RGD:621081"
ORIGIN      
        1 maeelnlerc dleiqangrd hhtadlcqqk lvlrrgqrfr ltlyfegrgy easvdrltfg
       61 avtgpdpsee agtkarfsls ddveegswsa svldqqdnvl slqlctpana pvgqyrlsle
      121 tstgyqgssf mlghfillfn awcpaddvyl dseaerreyv ltqqgfiyqg svkfiksvpw
      181 nfgqfedgil daclmlldvn pkflkdrsrd csrrsspiyv grvvsgmvnc nddqgvllgr
      241 wdnnygdgis pmawigsvdi lrrwkehgcq qvkygqcwvf aavactvlrc lgiptrvvtn
      301 ynsahdqnsn llieyfrney gelesnksem iwnfhcwves wmtrpdlqpg yegwqaidpt
      361 pqeksegtyc cgpvsvraik egdlstkyda sfvfaevnad vvdwirqsdg svlksinnsl
      421 vvgqkistks vgrddredit ytykypegsp eerevftran hlnklaekee tgvamrirvg
      481 dgmslgndfd vfahigndts esrecrlllc artvsyngvl gpecgtedin ltldpysens
      541 iplrilyeky sgcltesnli kvrgllvepa ansyllaerd lylenpeiki rilgepkqnr
      601 klvaevslkn plsdslydcv ftvegagltk eqksvevsdp vpagdavkvr vdlfptdigl
      661 hklvvnfqcd klksvkgyrn iiigpa
//
LOCUS       NP_001425368             487 aa            linear   ROD 24-APR-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Rattus norvegicus].
ACCESSION   NP_001425368 XP_008757325
VERSION     NP_001425368.1
DBSOURCE    REFSEQ: accession NM_001438439.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Shigeta,Y., Kanai,Y., Chairoungdua,A., Ahmed,N., Sakamoto,S.,
            Matsuo,H., Kim,D.K., Fujimura,M., Anzai,N., Mizoguchi,K., Ueda,T.,
            Akakura,K., Ichikawa,T., Ito,H. and Endou,H.
  TITLE     A novel missense mutation of SLC7A9 frequent in Japanese cystinuria
            cases affecting the C-terminus of the transporter
  JOURNAL   Kidney Int 69 (7), 1198-1206 (2006)
   PUBMED   16609684
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Kwak,J.O., Kim,H.W., Jung,S.M., Song,J.H., Hong,S.B., Oh,K.J.,
            Ko,C.B. and Cha,S.H.
  TITLE     Co-localization and interaction of b0,+-type amino acid transporter
            1 (BAT1) with caveolin-1 in rat kidney
  JOURNAL   J Nephrol 18 (6), 681-689 (2005)
   PUBMED   16358225
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Fernandez,E., Carrascal,M., Rousaud,F., Abian,J., Zorzano,A.,
            Palacin,M. and Chillaron,J.
  TITLE     rBAT-b(0,+)AT heterodimer is the main apical reabsorption system
            for cystine in the kidney
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F540-F548 (2002)
   PUBMED   12167606
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Chairoungdua,A., Segawa,H., Kim,J.Y., Miyamoto,K., Haga,H.,
            Fukui,Y., Mizoguchi,K., Ito,H., Takeda,E., Endou,H. and Kanai,Y.
  TITLE     Identification of an amino acid transporter associated with the
            cystinuria-related type II membrane glycoprotein
  JOURNAL   J Biol Chem 274 (41), 28845-28848 (1999)
   PUBMED   10506124
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 18, 2025 this sequence version replaced XP_008757325.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.1020.1,
                                           SRR26360186.993030.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="b(0,+)AT; solute carrier family 7 (amino acid
                     transporter light chain, bo,+ system), member 9;
                     glycoprotein-associated amino acid transporter b0,+AT1;
                     solute carrier family 7 (cationic amino acid transporter,
                     y+ system), member 9; solute carrier family 7
                     (glycoprotein-associated amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53527
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Region          13..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P82252.1)"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82252.1)"
     CDS             1..487
                     /gene="Slc7a9"
                     /coded_by="NM_001438439.1:343..1806"
                     /db_xref="GeneID:116726"
                     /db_xref="RGD:619905"
ORIGIN      
        1 meetsprrrr edeksvhste pkttslqkev gllsgiciiv gtiigsgifi spksvlante
       61 svgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meafgpipay lfswtslivm
      121 kpssfaiicl sfseyvcaaf ylgcrppavv vkllaaaail littvnalsv rlgsyvqnvf
      181 taaklvivai iiisglvlla qgnvknfqns fegsqtsvgs islafynglw aydgwnqlny
      241 iteelrnpyr nlpmaivigi plvtvcyilm niayftvmtp tellqsqava vtfgdrvlyp
      301 aswvvplfva fstigaangt cftagrliyv agreghmlkv lsyisvkrlt papalvfygi
      361 iaiiyiipgd inslvnyfsf aawlfygmti lglvvmrftr kdlerpikvp ifipiivilv
      421 svflilapii sspaweylyc vlfilsglif yflfvhykfr waqkisrpit khlqmlmevv
      481 ppekdpe
//
LOCUS       NP_001425458            1012 aa            linear   ROD 24-APR-2025
DEFINITION  cilia and flagella associated protein 91 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001425458 XP_008766990
VERSION     NP_001425458.1
DBSOURCE    REFSEQ: accession NM_001438529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 21, 2025 this sequence version replaced XP_008766990.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1566181.1,
                                           SRR26360181.41094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..1012
                     /product="cilia and flagella associated protein 91 isoform
                     4"
                     /note="MYCBP/AMY-1-associated, testis expressed 1;
                     MYCBP-associated, testis expressed 1; MYCBP associated and
                     testis expressed 1"
                     /calculated_mol_wt=114314
     Region          190..342
                     /region_name="CFAP91"
                     /note="Cilia- and flagella-associated protein 91;
                     pfam14738"
                     /db_xref="CDD:464290"
     Region          <515..>697
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          <756..1002
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..1012
                     /gene="Cfap91"
                     /gene_synonym="Maats1; RGD1305539"
                     /coded_by="NM_001438529.1:74..3112"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:303920"
                     /db_xref="RGD:1305539"
ORIGIN      
        1 msqtvtiqep rtnvpgflfq crdvlrakgr satrvydfly dplfivsser dhaqaniqat
       61 lvrsrlkkvp nfrsmfsnlf hhprysmyws ksdpvpphvs rewrgqeakh kevlrlraav
      121 dasfqkpeek yedadvsgkn rykffdrpfl pflqplplnv vlstaktgpl llspesskys
      181 imptkstvgt qtdyrdadiq tdpyspeyvv cqdtipellt lanltwgrgl paglaevemi
      241 erarekrawe atlpplsdsl qaekrrkmmn amerkewafr egeieklqel rlevlkqllk
      301 rreenqnemd mrhlnnqwce lqekkeakvs qihhrhvsni rklvgkgkni egklqrrdii
      361 rdysnfasqv ygplsrlgrf pdnnsedfvv rnhylntyeg lmelesslpd fvtqpriqap
      421 kpkvittkag flkrmartdy elaeihkall dkknkgpegp kplrflqknp ipqprlptps
      481 lemtsyeege iemaiiylqk llrgrvvqnm mfegkekrle limelrtsha lqeddklvkk
      541 aekqvtlalq rqrnlhedkl svienhlgdl egrvladmfd flskelvrlq eerrihafam
      601 laerqrrmre aeesgrrqve qrrlkqedqi fmevikvhqs tvtsyledii ltteertaee
      661 qareeiekia qeinniayem enrrtnlqse eivaelvysf lipevqkdfv kekvrnaqrk
      721 hilaahqiih sntesmlhqh aieeeqrsfl eqtetsnsdv ptlsvsdapt lsisdaptls
      781 vsdaptlsvs daptlsvsda ptlsvsdmpa ltvsdappis vsdepppsvs dkpppsvsde
      841 ppppvsvepp ppvsdeppps vsdeppppvs deppppvsde pppsvsdepp ppvsdeppps
      901 vsdepppsvs deppppvsde ppppvsdepp psvsdepppp vsdepppsvs depplpvsde
      961 pppsvsdepp psvsdepppp vsdeppppvs deppisasds etvkhtqdee eg
//
LOCUS       NP_001014050             288 aa            linear   ROD 24-APR-2025
DEFINITION  alpha/beta hydrolase domain-containing protein 17B [Rattus
            norvegicus].
ACCESSION   NP_001014050 XP_219895
VERSION     NP_001014050.1
DBSOURCE    REFSEQ: accession NM_001014028.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Tortosa,E., Adolfs,Y., Fukata,M., Pasterkamp,R.J., Kapitein,L.C.
            and Hoogenraad,C.C.
  TITLE     Dynamic Palmitoylation Targets MAP6 to the Axon to Promote
            Microtubule Stabilization during Neuronal Polarization
  JOURNAL   Neuron 94 (4), 809-825 (2017)
   PUBMED   28521134
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Yokoi,N., Fukata,Y., Sekiya,A., Murakami,T., Kobayashi,K. and
            Fukata,M.
  TITLE     Identification of PSD-95 Depalmitoylating Enzymes
  JOURNAL   J Neurosci 36 (24), 6431-6444 (2016)
   PUBMED   27307232
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Lin,D.T. and Conibear,E.
  TITLE     ABHD17 proteins are novel protein depalmitoylases that regulate
            N-Ras palmitate turnover and subcellular localization
  JOURNAL   Elife 4, e11306 (2015)
   PUBMED   26701913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219895.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079229.1, SRR26360186.1387896.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..288
                     /product="alpha/beta hydrolase domain-containing protein
                     17B"
                     /EC_number="3.1.2.22"
                     /note="abhydrolase domain-containing protein FAM108B1;
                     family with sequence similarity 108, member B1;
                     abhydrolase domain-containing protein 17B; protein
                     ABHD17B"
                     /calculated_mol_wt=32070
     Region          58..285
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY17.1)"
     CDS             1..288
                     /gene="Abhd17b"
                     /gene_synonym="Cgi67l; Fam108b1; RGD1305246"
                     /coded_by="NM_001014028.2:725..1591"
                     /db_xref="GeneID:309399"
                     /db_xref="RGD:1305246"
ORIGIN      
        1 mnnlsfselc clfccppcpg kiasklaflp pdptytlmcd esgsrwtlhl seradwqyss
       61 rekdaiecfm trtskgnria cmfvrcspna kytllfshgn avdlgqmssf yiglgsrinc
      121 nifsydysgy gassgkptek nlyadveaaw lalrtrygir penviiygqs igtvpsvdla
      181 aryesaavil hspltsgmrv afpdtkktyc fdafpnidki skitspvlii hgtedevidf
      241 shglalferc qrpveplwve gaghndvely gqylerlkqf vsqelvnl
//
LOCUS       NP_001425114             430 aa            linear   ROD 24-APR-2025
DEFINITION  KICSTOR complex protein kaptin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425114
VERSION     NP_001425114.1
DBSOURCE    REFSEQ: accession NM_001438185.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Baple,E.L., Maroofian,R., Chioza,B.A., Izadi,M., Cross,H.E.,
            Al-Turki,S., Barwick,K., Skrzypiec,A., Pawlak,R., Wagner,K.,
            Coblentz,R., Zainy,T., Patton,M.A., Mansour,S., Rich,P.,
            Qualmann,B., Hurles,M.E., Kessels,M.M. and Crosby,A.H.
  TITLE     Mutations in KPTN cause macrocephaly, neurodevelopmental delay, and
            seizures
  JOURNAL   Am J Hum Genet 94 (1), 87-94 (2014)
   PUBMED   24239382
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Bearer,E.L. and Abraham,M.T.
  TITLE     2E4 (kaptin): a novel actin-associated protein from human blood
            platelets found in lamellipodia and the tips of the stereocilia of
            the inner ear
  JOURNAL   Eur J Cell Biol 78 (2), 117-126 (1999)
   PUBMED   10099934
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166768.1, SRR26643296.719.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..430
                     /product="KICSTOR complex protein kaptin isoform 1"
                     /note="kaptin-like 1; KICSTOR complex protein kaptin"
                     /calculated_mol_wt=47409
     Region          316..379
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     CDS             1..430
                     /gene="Kptn"
                     /gene_synonym="Kptnl1"
                     /coded_by="NM_001438185.1:75..1367"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308107"
                     /db_xref="RGD:1310341"
ORIGIN      
        1 mgeaavaegp cplredsftr fssqsnvygl aggadgrgel laatlkgkvl gfryqdlrqk
       61 irpvakelqf nyipvdaeiv sidtfnkspp krglvvgitf ikdsgdkgsp flniycdyep
      121 gseynldsia esclnlelqf tpfqlchaev qvgdqletvf llsgndpaih lykeneglhq
      181 feeqpvenlf peltnltssv lwldvhnlpg ssqrlsalgc qsgyvrvahv dqknreilqt
      241 wtiqqdgpis rvivfrpsts eatkdspqqe gysllvasml epavvywdll nkglddqlll
      301 pgsdqfdsvl cglvtdvdld gqpevlvaty gqellcykyh glpeasrgfr llwrrsfasp
      361 llamahvdlt gdglrelavv slkgvhilqh sliqaselvl trlrhqveqr khqqglgdka
      421 gprpeeppas
//
LOCUS       NP_758839                281 aa            linear   ROD 24-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-5 [Rattus
            norvegicus].
ACCESSION   NP_758839 XP_006229042
VERSION     NP_758839.3
DBSOURCE    REFSEQ: accession NM_172336.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Madarampalli,B., Yuan,Y., Liu,D., Lengel,K., Xu,Y., Li,G., Yang,J.,
            Liu,X., Lu,Z. and Liu,D.X.
  TITLE     ATF5 Connects the Pericentriolar Materials to the Proximal End of
            the Mother Centriole
  JOURNAL   Cell 162 (3), 580-592 (2015)
   PUBMED   26213385
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zhang,Z.Y., Li,S.Z., Zhang,H.H., Wu,Q.R., Gong,J., Liang,T.,
            Gao,L., Xing,N.N., Liu,W.B., Du,R.L. and Zhang,X.D.
  TITLE     Stabilization of ATF5 by TAK1-Nemo-like kinase critically regulates
            the interleukin-1beta-stimulated C/EBP signaling pathway
  JOURNAL   Mol Cell Biol 35 (5), 778-788 (2015)
   PUBMED   25512613
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Zhao,Y., Zhang,Y.D., Zhang,Y.Y., Qian,S.W., Zhang,Z.C., Li,S.F.,
            Guo,L., Liu,Y., Wen,B., Lei,Q.Y., Tang,Q.Q. and Li,X.
  TITLE     p300-dependent acetylation of activating transcription factor 5
            enhances C/EBPbeta transactivation of C/EBPalpha during 3T3-L1
            differentiation
  JOURNAL   Mol Cell Biol 34 (3), 315-324 (2014)
   PUBMED   24216764
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,S.Z., Ou,J., Zhu,L.J. and Green,M.R.
  TITLE     Transcription factor ATF5 is required for terminal differentiation
            and survival of olfactory sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 109 (45), 18589-18594 (2012)
   PUBMED   23090999
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Liu,X., Liu,D., Qian,D., Dai,J., An,Y., Jiang,S., Stanley,B.,
            Yang,J., Wang,B., Liu,X. and Liu,D.X.
  TITLE     Nucleophosmin (NPM1/B23) interacts with activating transcription
            factor 5 (ATF5) protein and promotes proteasome- and
            caspase-dependent ATF5 degradation in hepatocellular carcinoma
            cells
  JOURNAL   J Biol Chem 287 (23), 19599-19609 (2012)
   PUBMED   22528486
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Forgacs,E., Gupta,S.K., Kerry,J.A. and Semmes,O.J.
  TITLE     The bZIP transcription factor ATFx binds human T-cell leukemia
            virus type 1 (HTLV-1) Tax and represses HTLV-1 long terminal
            repeat-mediated transcription
  JOURNAL   J Virol 79 (11), 6932-6939 (2005)
   PUBMED   15890932
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Angelastro,J.M., Mason,J.L., Ignatova,T.N., Kukekov,V.G.,
            Stengren,G.B., Goldman,J.E. and Greene,L.A.
  TITLE     Downregulation of activating transcription factor 5 is required for
            differentiation of neural progenitor cells into astrocytes
  JOURNAL   J Neurosci 25 (15), 3889-3899 (2005)
   PUBMED   15829641
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Angelastro,J.M., Ignatova,T.N., Kukekov,V.G., Steindler,D.A.,
            Stengren,G.B., Mendelsohn,C. and Greene,L.A.
  TITLE     Regulated expression of ATF5 is required for the progression of
            neural progenitor cells to neurons
  JOURNAL   J Neurosci 23 (11), 4590-4600 (2003)
   PUBMED   12805299
  REMARK    GeneRIF: ATF5 blocks the differentiation of neuroprogenitor cells
            into neurons and must be downregulated to permit this process to
            occur.
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Persengiev,S.P., Devireddy,L.R. and Green,M.R.
  TITLE     Inhibition of apoptosis by ATFx: a novel role for a member of the
            ATF/CREB family of mammalian bZIP transcription factors
  JOURNAL   Genes Dev 16 (14), 1806-1814 (2002)
   PUBMED   12130540
REFERENCE   10 (residues 1 to 281)
  AUTHORS   De Graeve,F., Bahr,A., Chatton,B. and Kedinger,C.
  TITLE     A murine ATFa-associated factor with transcriptional repressing
            activity
  JOURNAL   Oncogene 19 (14), 1807-1819 (2000)
   PUBMED   10777215
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 17, 2025 this sequence version replaced
            XP_006229042.1, NP_758839.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061786.1, SRR26643299.2303.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN12840129
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..281
                     /product="cyclic AMP-dependent transcription factor ATF-5"
                     /note="cAMP-dependent transcription factor ATF-5;
                     transcription factor ATFx"
                     /calculated_mol_wt=30058
     Region          1..21
                     /region_name="Required for protein stabilization induced
                     by IL1B. /evidence=ECO:0000250|UniProtKB:Q9Y2D1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000269|PubMed:21791614; propagated from
                     UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          118..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          119..216
                     /region_name="Interaction with PTP4A1.
                     /evidence=ECO:0000250|UniProtKB:O70191"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          166..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          208..270
                     /region_name="bZIP_ATF4"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-4 (ATF-4) and similar proteins: a
                     DNA-binding and dimerization domain; cd14692"
                     /db_xref="CDD:269840"
     Region          209..229
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Region          210..269
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269840"
     Site            order(213..214,216..218,220..225,227..229)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269840"
     Site            order(232,235,238..239,242..243,245..246,249..250,
                     252..253,256,259..260,263..264,266..267)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269840"
     Region          235..249
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P788.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D1; propagated from
                     UniProtKB/Swiss-Prot (Q6P788.1)"
     CDS             1..281
                     /gene="Atf5"
                     /coded_by="NM_172336.5:312..1157"
                     /db_xref="GeneID:282840"
                     /db_xref="RGD:628902"
ORIGIN      
        1 msllatlgle ldrallpasg lgwlvdygkl plapaplgpy evlggalegg lpgggeplag
       61 dgfsdwmter vdftallple aplppgtlpp pspappdlea masllkkele qmedffldap
      121 llpppspppp pppapslplp lplptfdlpq pptldtldll avycrseagp gdsglttlpv
      181 pqqppplapl pspsrpapyp spastrgdrk qkkrdqnksa alryrqrkra egealegecq
      241 glearnrelr eraesverei qyvkdlliev ykarsqrtrs a
//
LOCUS       NP_001424995             898 aa            linear   ROD 24-APR-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit [Rattus norvegicus].
ACCESSION   NP_001424995 XP_006231565
VERSION     NP_001424995.1
DBSOURCE    REFSEQ: accession NM_001438066.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Qiu,J., Yuan,H., Chen,S., Zhou,Y., Song,D. and Chen,R.
  TITLE     TNFalpha up-regulates COX-2 in chronic progressive nephropathy
            through nuclear accumulation of RelB and NF-kappaB2
  JOURNAL   Arch Physiol Biochem 122 (2), 88-93 (2016)
   PUBMED   26824492
  REMARK    GeneRIF: TNFalpha-RelB/p52 pathway may be involved in the early
            stages of renal damage, in part by stimulating COX-2 and
            inflammatory responses
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Burkitt,M.D., Williams,J.M., Duckworth,C.A., O'Hara,A., Hanedi,A.,
            Varro,A., Caamano,J.H. and Pritchard,D.M.
  TITLE     Signaling mediated by the NF-kappaB sub-units NF-kappaB1,
            NF-kappaB2 and c-Rel differentially regulate Helicobacter
            felis-induced gastric carcinogenesis in C57BL/6 mice
  JOURNAL   Oncogene 32 (50), 5563-5573 (2013)
   PUBMED   23975431
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Manecka,D.L., Mahmood,S.F., Grumolato,L., Lihrmann,I. and Anouar,Y.
  TITLE     Pituitary adenylate cyclase-activating polypeptide (PACAP) promotes
            both survival and neuritogenesis in PC12 cells through activation
            of nuclear factor kappaB (NF-kappaB) pathway: involvement of
            extracellular signal-regulated kinase (ERK), calcium, and c-REL
  JOURNAL   J Biol Chem 288 (21), 14936-14948 (2013)
   PUBMED   23564451
  REMARK    GeneRIF: PACAP promotes both survival and neuritogenesis in PC12
            cells by activating NF-kappaB pathway, most likely via classical
            and alternative signaling cascades involving ERK1/2 kinases,
            Ca(2+), and c-Rel/p52 dimers.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Vogel,K.U., Edelmann,S.L., Jeltsch,K.M., Bertossi,A., Heger,K.,
            Heinz,G.A., Zoller,J., Warth,S.C., Hoefig,K.P., Lohs,C., Neff,F.,
            Kremmer,E., Schick,J., Repsilber,D., Geerlof,A., Blum,H., Wurst,W.,
            Heikenwalder,M., Schmidt-Supprian,M. and Heissmeyer,V.
  TITLE     Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40
            costimulator mRNAs and control follicular helper T cell
            differentiation
  JOURNAL   Immunity 38 (4), 655-668 (2013)
   PUBMED   23583643
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Droebner,K., Klein,B., Paxian,S., Schmid,R., Stitz,L. and Planz,O.
  TITLE     The alternative NF-kappaB signalling pathway is a prerequisite for
            an appropriate immune response against lymphocytic choriomeningitis
            virus infection
  JOURNAL   Viral Immunol 23 (3), 295-308 (2010)
   PUBMED   20565293
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Medicherla,R., Leers-Sucheta,S., Luo,Y. and Azhar,S.
  TITLE     Age-dependent modulation of NF-kappaB expression in rat adrenal
            gland
  JOURNAL   Mech Ageing Dev 123 (9), 1211-1227 (2002)
   PUBMED   12020944
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Poljak,L., Carlson,L., Cunningham,K., Kosco-Vilbois,M.H. and
            Siebenlist,U.
  TITLE     Distinct activities of p52/NF-kappa B required for proper secondary
            lymphoid organ microarchitecture: functions enhanced by Bcl-3
  JOURNAL   J Immunol 163 (12), 6581-6588 (1999)
   PUBMED   10586052
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Muggia,A., Teesalu,T., Neri,A., Blasi,F. and Talarico,D.
  TITLE     Trophoblast giant cells express NF-kappa B2 during early mouse
            development
  JOURNAL   Dev Genet 25 (1), 23-30 (1999)
   PUBMED   10402669
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Bundy,D.L. and McKeithan,T.W.
  TITLE     Diverse effects of BCL3 phosphorylation on its modulation of
            NF-kappaB p52 homodimer binding to DNA
  JOURNAL   J Biol Chem 272 (52), 33132-33139 (1997)
   PUBMED   9407099
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231565.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ226161.1, SRR22582419.2573737.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..898
                     /product="nuclear factor NF-kappa-B p100 subunit"
                     /note="nuclear factor of kappa light polypeptide gene
                     enhancer in B-cells 2, p49/p100"
                     /calculated_mol_wt=96608
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          435..705
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(486,488,492..493,496..498,500..501,505,511,523,525,
                     527,531..532,535..537,539..540,544,547,556,558,560,
                     564..565,568..570,574..575,579,582)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          486..523
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          525..556
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          558..585
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(598,600,604..605,608..610,612..613,617,620,629,632,
                     634,638..639,642..644,646..647,651,654,664,666,668,
                     672..673,676..678,680..681,685,688,697)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          598..629
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          632..664
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          666..697
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          773..847
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     CDS             1..898
                     /gene="Nfkb2"
                     /gene_synonym="RGD1307189"
                     /coded_by="NM_001438066.1:137..2833"
                     /db_xref="GeneID:309452"
                     /db_xref="RGD:1307189"
ORIGIN      
        1 mdrcydpgld gipeyddfef spsivepkdp apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgvc
      121 avsvgpkdmt aqfnnlgvlh vtkknmmeim iqklqrqrlr skpqglteae rreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggsaggygga ggggslgffs sfayspyqsg aapmgcfpgg gggaqmagsg rdaeageaee
      421 qprapseapq seqqaldtlq rareynarlf glaqrsaral ldygvtadar allagqrhll
      481 maqdengdtp lhlaiihgqt gvieqiaqvi yhaqylgvin ltnhlhqtpl hlavitgqtr
      541 vvsfllqvga dptlldrhgd savhlalrag aaapdllqav lhsgahalpq mlhmpdfegl
      601 ypvhlavhar specldllvd cgaeveaaer qggrtplhla temeelglvt hlvtklhanv
      661 nartfagntp lhlaaglgsp tltrlllkag adihaeneep lcplpsppts gsdsdsegpe
      721 tdtqrnfrgh tpldltrstk vktlllnaaq nttepplapp spagpglslg daalqnleql
      781 ldgpeaqgsw aelaerlglr slvdtyrktp spsgsllrsy klaggdlvgl lealsdmglh
      841 egvrllkape trdklpstev kedsaygsqs veqeaeklcp ppeppgglch ghpqpqvh
//
LOCUS       NP_001425628            2218 aa            linear   ROD 24-APR-2025
DEFINITION  zinc finger protein 318 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001425628 XP_038940748
VERSION     NP_001425628.1
DBSOURCE    REFSEQ: accession NM_001438699.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2218)
  AUTHORS   Tao,R.H., Kawate,H., Ohnaka,K., Ishizuka,M., Hagiwara,H. and
            Takayanagi,R.
  TITLE     Opposite effects of alternative TZF spliced variants on androgen
            receptor
  JOURNAL   Biochem Biophys Res Commun 341 (2), 515-521 (2006)
   PUBMED   16446156
REFERENCE   2  (residues 1 to 2218)
  AUTHORS   Ishizuka,M., Ohshima,H., Tamura,N., Nakada,T., Inoue,A., Hirose,S.
            and Hagiwara,H.
  TITLE     Molecular cloning and characteristics of a novel zinc finger
            protein and its splice variant whose transcripts are expressed
            during spermatogenesis
  JOURNAL   Biochem Biophys Res Commun 301 (4), 1079-1085 (2003)
   PUBMED   12589823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 22, 2025 this sequence version replaced XP_038940748.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.49176.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..2218
                     /product="zinc finger protein 318 isoform 1"
                     /calculated_mol_wt=244349
     Region          <17..>141
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <892..1060
                     /region_name="PRK00409"
                     /note="recombination and DNA strand exchange inhibitor
                     protein; Reviewed"
                     /db_xref="CDD:234750"
     Region          1078..1112
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1148..1182
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     CDS             1..2218
                     /gene="Zfp318"
                     /coded_by="NM_001438699.1:112..6768"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:685082"
                     /db_xref="RGD:1583221"
ORIGIN      
        1 myrsgsrssv sshrpkdgga sgpppgrpvg assgparrps spppscsslr lparrhrsps
       61 ghrgrwasps pprgrrgsps pprgrrasps pprgrrasps pprgrrvsps pprarrgsps
      121 pprsrrhypp glggfrgsir gesradfard grgdhpgdsg srrrspglcs dssleqslri
      181 tvgndhfcvs taerrrlsdr lgspvdgled mdrddltdds vftrssqcsr gleryisree
      241 gplspflgql dedyptretf lnrseyspqs rchdellrgt ernrdklkss sysvrseers
      301 reakrprydn lekahstggd hsgftsgtrn yrqrrsspsp rfldpefrel dlarrkreee
      361 eeqskslsqe lvgvddgqtg csipglsgvl ttaepgyslh rseeipvmpk ksilkkriev
      421 dmkpslqles fssgtssced rplysehspl plsdaiaaft seienkgttv eadlkepqsn
      481 lyqwgplrei pkdnsekfds flcfkekldl kaegleqqtd fllpherasq dgsgfsrils
      541 mladptstqe krrrsfpdie deekflygde eeediksesp pksledaest gtrqksnslp
      601 stpavklesl eesnpeyaki hdllktigld igvaeigkla artqerlhgk kpssrssadr
      661 rssadrhfsa drcssvdhsf ttdwhssdph rpesreahhs stqspevshp hpaslvdsyl
      721 rtknsppflk sdrpvghvsg aevvgsgfqs svavrcmlps apstpirlph saalsqfhip
      781 rasqfaatri spnyqgtvip pasfdayrhy mayaasrwpm ypasqppshp lsdphrlipv
      841 tkqatrsrpn lrviptvtpa kpkqeipvlg sisvkripvr vsipsliryn pkkisdeknr
      901 asqkqkviee rerlkteqea rqkkmfylrt elerlhkqqg emlrkkrrek dghkdpllme
      961 vsrlqegimk diaelhkete eagkkqseld kvaqilgidi fdkslksand skestekpek
     1021 ekskspekel spsnpssnnk eskvneksyi kspssteilq ptakhpdepv aayeyydagn
     1081 hwckdcntic gtmfdffthm hnkkhtqtld pynrpwaskt qseakqdtvk rtdkitvpak
     1141 gseflipitg fycqlceefl gdpisgeqhv kghqhnekyk kyveenplye errnldrqag
     1201 lavvleterr rqnelkrkln ekpkeekiek kakivkeake ddkasgeled qlsegrdspe
     1261 kgdskrnasl kpqvkeevkk esstasfgkf swkkpekeee knslvtpgap kedtvetnkd
     1321 rdegkaevgk akpikiklsg ktvvahtspw tpvvttsaqt kirpnlpips talrksgsat
     1381 vskpaplntf lsikssgasa kplpvvkess sdlllppdvi skafggeevv lkgspeekve
     1441 laeknepsqi peqmlallpp pppppppppp ppppplvvpq lsapspaqan avltpvksns
     1501 vvsqtfslgf qgpnilnpgl pvafmaseqp aaipcdetap gvsesdrdqt lismlvrppp
     1561 plssvfseqa kklekrnscl atanakdlyd ifyssggkga hetklssspl angessslsr
     1621 tessdissts alkssvsped lpqdvalata teisnlenpi skgvesigkw sivdqidpkg
     1681 rdstfsflqp ltrlyqnrpy emvspktdtl amwtsgsfqn dtdkdrpsev kikfdqgepa
     1741 ppatdstshp sdehcqtngs qklveinlmd nqdknqevyq sedcresegk rntelkgkva
     1801 aeeganiglq siedsnsnyg nrntwegepk lstidkeaeq ssrlmtghen tssivielsq
     1861 clpskrtkid sfpsllqnpk gmpellllsp agsgmclkrq etwerpekpe veaeelqgth
     1921 pegtvktese gsesldtthv everfatlrn lgdthaefcn sqieqtrrsp talsqkisee
     1981 nsvssvvcnp sspsdvepvp sfsgfplesp kilvlnfete gahsssnsrn gritsnslet
     2041 ghpmenvdhd lggerthqal dllaggmlse evkepsplqk dllrmesttv spsghgpspc
     2101 lpdlvdfvtr tpgvpkekpr splsepddfl kcsslemgsp ppeilnvsvs evavpqased
     2161 cdnalnlvkp ptsgspsrgq vvggsvssqe mpeqeaavdv ipdhrkssvy ncqdylng
//
LOCUS       NP_001425494             594 aa            linear   ROD 24-APR-2025
DEFINITION  Fc receptor-like 5 precursor [Rattus norvegicus].
ACCESSION   NP_001425494 XP_017446788
VERSION     NP_001425494.1
DBSOURCE    REFSEQ: accession NM_001438565.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Zhu,Z., Li,R., Li,H., Zhou,T. and Davis,R.S.
  TITLE     FCRL5 exerts binary and compartment-specific influence on
            innate-like B-cell receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 110 (14), E1282-E1290 (2013)
   PUBMED   23509253
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Polson,A.G., Zheng,B., Elkins,K., Chang,W., Du,C., Dowd,P., Yen,L.,
            Tan,C., Hongo,J.A., Koeppen,H. and Ebens,A.
  TITLE     Expression pattern of the human FcRH/IRTA receptors in normal
            tissue and in B-chronic lymphocytic leukemia
  JOURNAL   Int Immunol 18 (9), 1363-1373 (2006)
   PUBMED   16849395
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 21, 2025 this sequence version replaced XP_017446788.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760400, SAMEA5760434
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..594
                     /product="Fc receptor-like 5 precursor"
                     /note="Fc receptor-like protein 5; Fc receptor-like 3;
                     rCG62831-like"
                     /calculated_mol_wt=63579
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2738
     Region          34..109
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          51..55
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          65..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          77..81
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..96
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          102..105
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          114..196
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          128..132
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          142..146
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          159..163
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          173..178
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          189..192
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          202..284
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Region          304..372
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          315..319
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          329..333
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..354
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          364..369
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          378..381
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          392..466
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     CDS             1..594
                     /gene="Fcrl5"
                     /gene_synonym="Fcrl3"
                     /coded_by="NM_001438565.1:132..1916"
                     /db_xref="GeneID:680697"
                     /db_xref="RGD:1589379"
ORIGIN      
        1 mpgsfscgva ftqlwltllv vtpvngqhea vlqsvvylqp pwttffqgek vtlfcygfgf
       61 ylpqktkwyr knktqrqlrs tstlevresg eywcqadnfl psmhvhldfr qdslvlqapp
      121 avfegdsvvl rchtrediaa eslkfykngk alelsgpsse lhihhanred ngqytctgrk
      181 nwhlkytpsn tvrvqvqell prpvlmatps qpidgspvtl tcqiqlpaqr snvqlqfcfl
      241 knlqalesgc snssefhipa iwteestwyq craetvnsqt ekqsialkip vqraladfqt
      301 yimpasklvy egqslllncs vngvpgplkf swykrdmlnk kanipkssga evkiskvnvs
      361 dageyyceak nsrrrfvsra vpitikvpvs qpvltlssgk tqalegdlmt lhcksqrgsp
      421 yilyefyhen vslgnsstls gegggasfnf smstersgny hctadnglga qnseaiwisv
      481 aemtnnrsap viagitvgll itavgvflsy cwfsrqaggk pasdesrsps daepqeptyy
      541 nmpacielqp vysndpkeav iyteirrtqp kpkpkravke sesprsrcqm aekn
//
LOCUS       NP_001178562            1020 aa            linear   ROD 24-APR-2025
DEFINITION  fanconi-associated nuclease 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178562 XP_006229401 XP_219706
VERSION     NP_001178562.1
DBSOURCE    REFSEQ: accession NM_001191633.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Wang,R., Persky,N.S., Yoo,B., Ouerfelli,O., Smogorzewska,A.,
            Elledge,S.J. and Pavletich,N.P.
  TITLE     DNA repair. Mechanism of DNA interstrand cross-link processing by
            repair nuclease FAN1
  JOURNAL   Science 346 (6213), 1127-1130 (2014)
   PUBMED   25430771
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   Pennell,S., Declais,A.C., Li,J., Haire,L.F., Berg,W.,
            Saldanha,J.W., Taylor,I.A., Rouse,J., Lilley,D.M. and Smerdon,S.J.
  TITLE     FAN1 activity on asymmetric repair intermediates is mediated by an
            atypical monomeric virus-type replication-repair nuclease domain
  JOURNAL   Cell Rep 8 (1), 84-93 (2014)
   PUBMED   24981866
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Smogorzewska,A., Desetty,R., Saito,T.T., Schlabach,M., Lach,F.P.,
            Sowa,M.E., Clark,A.B., Kunkel,T.A., Harper,J.W., Colaiacovo,M.P.
            and Elledge,S.J.
  TITLE     A genetic screen identifies FAN1, a Fanconi anemia-associated
            nuclease necessary for DNA interstrand crosslink repair
  JOURNAL   Mol Cell 39 (1), 36-47 (2010)
   PUBMED   20603073
REFERENCE   4  (residues 1 to 1020)
  AUTHORS   Kratz,K., Schopf,B., Kaden,S., Sendoel,A., Eberhard,R.,
            Lademann,C., Cannavo,E., Sartori,A.A., Hengartner,M.O. and
            Jiricny,J.
  TITLE     Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes
            cells to interstrand crosslinking agents
  JOURNAL   Cell 142 (1), 77-88 (2010)
   PUBMED   20603016
REFERENCE   5  (residues 1 to 1020)
  AUTHORS   MacKay,C., Declais,A.C., Lundin,C., Agostinho,A., Deans,A.J.,
            MacArtney,T.J., Hofmann,K., Gartner,A., West,S.C., Helleday,T.,
            Lilley,D.M. and Rouse,J.
  TITLE     Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to
            DNA damage by monoubiquitinated FANCD2
  JOURNAL   Cell 142 (1), 65-76 (2010)
   PUBMED   20603015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_006229401.1, XP_219706.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.1271.1,
                                           SRR26643292.2298.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1020
                     /product="fanconi-associated nuclease 1 isoform 1"
                     /EC_number="3.1.4.1"
                     /note="coiled-coil domain-containing protein MTMR15;
                     myotubularin related protein 15; fanconi-associated
                     nuclease 1; FANCD2/FANCI-associated nuclease 1"
                     /calculated_mol_wt=112624
     Region          376..1020
                     /region_name="FAN1-like"
                     /note="repair nuclease FAN1; cd22326"
                     /db_xref="CDD:411730"
     Site            order(376..377,423,427..428,436,439,476..478,495..497,576,
                     579..581,584,623,675,678,681..682,684,709,713,716,
                     720..721,745,752,755,797..798,955,983,985,989)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411730"
     CDS             1..1020
                     /gene="Fan1"
                     /gene_synonym="Mtmr15; RGD1566323"
                     /coded_by="NM_001191633.2:384..3446"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309256"
                     /db_xref="RGD:1566323"
ORIGIN      
        1 mmsqksspaq krprkslstg kttksqshsi tsyfnsvppa klacsichkm vprydlirhl
       61 descanngei vqnepaqagl instvptsdl pstpledmtp qklsppkrrl isaqcgsklg
      121 vrqqtspyfk kalvcknqnk lpnqsveirs lgslssklsr ryvkakksls kneglashcp
      181 ptspsppgps lvdncpemdn kdeilnssqk eniyscaple eetaseqkvk sskrmgdgsq
      241 kasggepalt paspeqaptl lssdltlvnn tdsssgdale qegagrvgvg vdeqlaacsh
      301 eevqmtvdae vgtlvsggae snspadnddd dastwsnnpe lreagsalkr qracspleqg
      361 ascvpsvtaq pqpshpyylr sflvvlqail eneedmklfd dqekgviakf yqlsasgqkl
      421 yvrlfqrklt wikvskleye eiasdltpvv eelknlgflq teselqelsd vlellsapel
      481 kalaktfhlv spggqkqqlv daflklarqr svytwgktqp giravilkra kdlagpslrv
      541 ckgpravfcr llllfsltdt medeeaacgg qgqlstvllv nlgrmefpqy sisrktqifr
      601 dredliryaa aahmlsdisa amasgnweea kelsqiakrd wdqlkshpsl ryhealplfl
      661 rcftvgwiyt rissravevl erlhmyeeav kelenllaqk vycpdsrgrw wdrlalnlhq
      721 hlkrleeaiw cikegladpq vrtghrlsly qravrlresp sckkyrhlfs qlpevtvgdv
      781 khvtitgrlc pqhgmgksvf vieggdptnp ttilcsveel aldyyrrsgf dqgihgegst
      841 fstlcglllw diifmdgipd vfrnayqasp ldlltdsffs sreqalearl qlihsapaes
      901 lrawvteawq aqqgraaslv swdrftslqq aqdlvsclgg pvlsgvcrrl aadfrhcrgg
      961 lpdlvvwnsq shhcklvevk gpsdrlsckq miwldelqkl gadvevchvv avgakskglg
//
LOCUS       NP_001425258             258 aa            linear   ROD 24-APR-2025
DEFINITION  ciliogenesis and planar polarity effector 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425258
VERSION     NP_001425258.1
DBSOURCE    REFSEQ: accession NM_001438329.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..258
                     /product="ciliogenesis and planar polarity effector 2
                     isoform 1"
                     /note="REM2 and RAB-like small GTPase 1; ciliogenesis and
                     planar polarity effector 2"
                     /calculated_mol_wt=28341
     Region          62..>180
                     /region_name="Ras_like_GTPase"
                     /note="Rat sarcoma (Ras)-like superfamily of small
                     guanosine triphosphatases (GTPases); cd00882"
                     /db_xref="CDD:206648"
     Site            62..69
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            87
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            91..93
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            175..178
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     CDS             1..258
                     /gene="Cplane2"
                     /gene_synonym="RGD1561421; Rsg1"
                     /coded_by="NM_001438329.1:137..913"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500576"
                     /db_xref="RGD:1561421"
ORIGIN      
        1 marlpmhgsv ivpdwhetve gkeylacilr knrrrefgll erpvlppsvv idtasykifv
       61 sgksgvgkta lvaklaglev pvvhhettgi qttvvfwpak lkasgrvvmf rfefwdcges
      121 alkkfdhilp ackekadafl flfsftdras fedlpgqlsr vageapgvvk ivigskfdqy
      181 mhtdvperdl tafrqawelp lfrvksvpgr rladgrtldg ragladtahv lnglaeqlwh
      241 qdqvaagllp sspenapg
//
LOCUS       NP_001008350             898 aa            linear   ROD 24-APR-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit [Rattus norvegicus].
ACCESSION   NP_001008350 XP_219954 XP_347196
VERSION     NP_001008350.1
DBSOURCE    REFSEQ: accession NM_001008349.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Qiu,J., Yuan,H., Chen,S., Zhou,Y., Song,D. and Chen,R.
  TITLE     TNFalpha up-regulates COX-2 in chronic progressive nephropathy
            through nuclear accumulation of RelB and NF-kappaB2
  JOURNAL   Arch Physiol Biochem 122 (2), 88-93 (2016)
   PUBMED   26824492
  REMARK    GeneRIF: TNFalpha-RelB/p52 pathway may be involved in the early
            stages of renal damage, in part by stimulating COX-2 and
            inflammatory responses
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Burkitt,M.D., Williams,J.M., Duckworth,C.A., O'Hara,A., Hanedi,A.,
            Varro,A., Caamano,J.H. and Pritchard,D.M.
  TITLE     Signaling mediated by the NF-kappaB sub-units NF-kappaB1,
            NF-kappaB2 and c-Rel differentially regulate Helicobacter
            felis-induced gastric carcinogenesis in C57BL/6 mice
  JOURNAL   Oncogene 32 (50), 5563-5573 (2013)
   PUBMED   23975431
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Manecka,D.L., Mahmood,S.F., Grumolato,L., Lihrmann,I. and Anouar,Y.
  TITLE     Pituitary adenylate cyclase-activating polypeptide (PACAP) promotes
            both survival and neuritogenesis in PC12 cells through activation
            of nuclear factor kappaB (NF-kappaB) pathway: involvement of
            extracellular signal-regulated kinase (ERK), calcium, and c-REL
  JOURNAL   J Biol Chem 288 (21), 14936-14948 (2013)
   PUBMED   23564451
  REMARK    GeneRIF: PACAP promotes both survival and neuritogenesis in PC12
            cells by activating NF-kappaB pathway, most likely via classical
            and alternative signaling cascades involving ERK1/2 kinases,
            Ca(2+), and c-Rel/p52 dimers.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Vogel,K.U., Edelmann,S.L., Jeltsch,K.M., Bertossi,A., Heger,K.,
            Heinz,G.A., Zoller,J., Warth,S.C., Hoefig,K.P., Lohs,C., Neff,F.,
            Kremmer,E., Schick,J., Repsilber,D., Geerlof,A., Blum,H., Wurst,W.,
            Heikenwalder,M., Schmidt-Supprian,M. and Heissmeyer,V.
  TITLE     Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40
            costimulator mRNAs and control follicular helper T cell
            differentiation
  JOURNAL   Immunity 38 (4), 655-668 (2013)
   PUBMED   23583643
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Droebner,K., Klein,B., Paxian,S., Schmid,R., Stitz,L. and Planz,O.
  TITLE     The alternative NF-kappaB signalling pathway is a prerequisite for
            an appropriate immune response against lymphocytic choriomeningitis
            virus infection
  JOURNAL   Viral Immunol 23 (3), 295-308 (2010)
   PUBMED   20565293
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Medicherla,R., Leers-Sucheta,S., Luo,Y. and Azhar,S.
  TITLE     Age-dependent modulation of NF-kappaB expression in rat adrenal
            gland
  JOURNAL   Mech Ageing Dev 123 (9), 1211-1227 (2002)
   PUBMED   12020944
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Poljak,L., Carlson,L., Cunningham,K., Kosco-Vilbois,M.H. and
            Siebenlist,U.
  TITLE     Distinct activities of p52/NF-kappa B required for proper secondary
            lymphoid organ microarchitecture: functions enhanced by Bcl-3
  JOURNAL   J Immunol 163 (12), 6581-6588 (1999)
   PUBMED   10586052
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Muggia,A., Teesalu,T., Neri,A., Blasi,F. and Talarico,D.
  TITLE     Trophoblast giant cells express NF-kappa B2 during early mouse
            development
  JOURNAL   Dev Genet 25 (1), 23-30 (1999)
   PUBMED   10402669
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Bundy,D.L. and McKeithan,T.W.
  TITLE     Diverse effects of BCL3 phosphorylation on its modulation of
            NF-kappaB p52 homodimer binding to DNA
  JOURNAL   J Biol Chem 272 (52), 33132-33139 (1997)
   PUBMED   9407099
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Dec 16, 2004 this sequence version replaced
            XP_219954.2, XP_347196.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085800.1, SRR26643287.4013.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..898
                     /product="nuclear factor NF-kappa-B p100 subunit"
                     /note="nuclear factor of kappa light polypeptide gene
                     enhancer in B-cells 2, p49/p100"
                     /calculated_mol_wt=96608
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          435..705
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(486,488,492..493,496..498,500..501,505,511,523,525,
                     527,531..532,535..537,539..540,544,547,556,558,560,
                     564..565,568..570,574..575,579,582)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          486..523
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          525..556
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          558..585
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(598,600,604..605,608..610,612..613,617,620,629,632,
                     634,638..639,642..644,646..647,651,654,664,666,668,
                     672..673,676..678,680..681,685,688,697)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          598..629
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          632..664
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          666..697
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          773..847
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     CDS             1..898
                     /gene="Nfkb2"
                     /gene_synonym="RGD1307189"
                     /coded_by="NM_001008349.2:298..2994"
                     /db_xref="GeneID:309452"
                     /db_xref="RGD:1307189"
ORIGIN      
        1 mdrcydpgld gipeyddfef spsivepkdp apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgvc
      121 avsvgpkdmt aqfnnlgvlh vtkknmmeim iqklqrqrlr skpqglteae rreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggsaggygga ggggslgffs sfayspyqsg aapmgcfpgg gggaqmagsg rdaeageaee
      421 qprapseapq seqqaldtlq rareynarlf glaqrsaral ldygvtadar allagqrhll
      481 maqdengdtp lhlaiihgqt gvieqiaqvi yhaqylgvin ltnhlhqtpl hlavitgqtr
      541 vvsfllqvga dptlldrhgd savhlalrag aaapdllqav lhsgahalpq mlhmpdfegl
      601 ypvhlavhar specldllvd cgaeveaaer qggrtplhla temeelglvt hlvtklhanv
      661 nartfagntp lhlaaglgsp tltrlllkag adihaeneep lcplpsppts gsdsdsegpe
      721 tdtqrnfrgh tpldltrstk vktlllnaaq nttepplapp spagpglslg daalqnleql
      781 ldgpeaqgsw aelaerlglr slvdtyrktp spsgsllrsy klaggdlvgl lealsdmglh
      841 egvrllkape trdklpstev kedsaygsqs veqeaeklcp ppeppgglch ghpqpqvh
//
LOCUS       NP_001414645            1147 aa            linear   ROD 24-APR-2025
DEFINITION  zinc finger protein 318 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001414645 XP_038940749
VERSION     NP_001414645.1
DBSOURCE    REFSEQ: accession NM_001427716.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Tao,R.H., Kawate,H., Ohnaka,K., Ishizuka,M., Hagiwara,H. and
            Takayanagi,R.
  TITLE     Opposite effects of alternative TZF spliced variants on androgen
            receptor
  JOURNAL   Biochem Biophys Res Commun 341 (2), 515-521 (2006)
   PUBMED   16446156
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Ishizuka,M., Ohshima,H., Tamura,N., Nakada,T., Inoue,A., Hirose,S.
            and Hagiwara,H.
  TITLE     Molecular cloning and characteristics of a novel zinc finger
            protein and its splice variant whose transcripts are expressed
            during spermatogenesis
  JOURNAL   Biochem Biophys Res Commun 301 (4), 1079-1085 (2003)
   PUBMED   12589823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Feb 2, 2024 this sequence version replaced XP_038940749.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..1147
                     /product="zinc finger protein 318 isoform 2"
                     /calculated_mol_wt=128294
     Region          <17..>141
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <892..1060
                     /region_name="PRK00409"
                     /note="recombination and DNA strand exchange inhibitor
                     protein; Reviewed"
                     /db_xref="CDD:234750"
     Region          1078..1107
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     CDS             1..1147
                     /gene="Zfp318"
                     /coded_by="NM_001427716.2:322..3765"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:685082"
                     /db_xref="RGD:1583221"
ORIGIN      
        1 myrsgsrssv sshrpkdgga sgpppgrpvg assgparrps spppscsslr lparrhrsps
       61 ghrgrwasps pprgrrgsps pprgrrasps pprgrrasps pprgrrvsps pprarrgsps
      121 pprsrrhypp glggfrgsir gesradfard grgdhpgdsg srrrspglcs dssleqslri
      181 tvgndhfcvs taerrrlsdr lgspvdgled mdrddltdds vftrssqcsr gleryisree
      241 gplspflgql dedyptretf lnrseyspqs rchdellrgt ernrdklkss sysvrseers
      301 reakrprydn lekahstggd hsgftsgtrn yrqrrsspsp rfldpefrel dlarrkreee
      361 eeqskslsqe lvgvddgqtg csipglsgvl ttaepgyslh rseeipvmpk ksilkkriev
      421 dmkpslqles fssgtssced rplysehspl plsdaiaaft seienkgttv eadlkepqsn
      481 lyqwgplrei pkdnsekfds flcfkekldl kaegleqqtd fllpherasq dgsgfsrils
      541 mladptstqe krrrsfpdie deekflygde eeediksesp pksledaest gtrqksnslp
      601 stpavklesl eesnpeyaki hdllktigld igvaeigkla artqerlhgk kpssrssadr
      661 rssadrhfsa drcssvdhsf ttdwhssdph rpesreahhs stqspevshp hpaslvdsyl
      721 rtknsppflk sdrpvghvsg aevvgsgfqs svavrcmlps apstpirlph saalsqfhip
      781 rasqfaatri spnyqgtvip pasfdayrhy mayaasrwpm ypasqppshp lsdphrlipv
      841 tkqatrsrpn lrviptvtpa kpkqeipvlg sisvkripvr vsipsliryn pkkisdeknr
      901 asqkqkviee rerlkteqea rqkkmfylrt elerlhkqqg emlrkkrrek dghkdpllme
      961 vsrlqegimk diaelhkete eagkkqseld kvaqilgidi fdkslksand skestekpek
     1021 ekskspekel spsnpssnnk eskvneksyi kspssteilq ptakhpdepv aayeyydagn
     1081 hwckdcntic gtmfdffthm hnkkhtqgqs qksshfpkeg lqqtfllqec rdrnhkdygn
     1141 nvrpcgq
//
LOCUS       NP_001162607             541 aa            linear   ROD 24-APR-2025
DEFINITION  probable tubulin polyglutamylase TTLL2 [Rattus norvegicus].
ACCESSION   NP_001162607 XP_001070106 XP_006227981 XP_217869
VERSION     NP_001162607.2
DBSOURCE    REFSEQ: accession NM_001169136.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Apr 17, 2025 this sequence version replaced
            XP_006227981.1, NP_001162607.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3319768.1,
                                           SRR26643293.883.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..541
                     /product="probable tubulin polyglutamylase TTLL2"
                     /note="tubulin tyrosine ligase-like family, member 2"
                     /calculated_mol_wt=61829
     Region          98..371
                     /region_name="TTL"
                     /note="Tubulin-tyrosine ligase family; pfam03133"
                     /db_xref="CDD:397308"
     CDS             1..541
                     /gene="Ttll2"
                     /coded_by="NM_001169136.2:173..1798"
                     /db_xref="GeneID:292311"
                     /db_xref="RGD:1305200"
ORIGIN      
        1 mmnglqtlgd vtaeifrlsp egntvqkrqr lrmedeapga alkplvfrvd estpgvvqsv
       61 llergwdkfd eqcqdvedwn lywrsssfrm aeyvnikpwq rlnhhpgtts ltrkdclakh
      121 lahmrrlyge siyeftpltf impsdytkfv akyfkekqdl gtkpsywick paklsqgrgi
      181 iifsdirdlm fkdayvvqky icnpllvgry kcdlriyvcv tgfkpltiym yqeglvrfat
      241 ekfdlsnled yyshltnssi nklgasyeki kevvgqgckw tlsrffsylr nwdvddlllr
      301 rkinhmvilt vlamapsvpv anncfelfgf diliddnlkp wllevnyspa lslecstdvs
      361 vkrslvhdii ellylnglrs eekkcgrtsq gnamvsqarr sqqklcaapa ppsyasliqf
      421 atcskrspaa qhmcpkhtrt sqlremlcrq nklltreaak skprlkawhs prkmlslcas
      481 qslprktkgp tgilpeagnt pnnhagnfvl ifpfnkatfs asrnglnvkr iiqelqklmn
      541 k
//
LOCUS       NP_001417715             448 aa            linear   ROD 24-APR-2025
DEFINITION  cilia and flagella associated protein 91 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001417715
VERSION     NP_001417715.1
DBSOURCE    REFSEQ: accession NM_001430786.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2104679.1,
                                           SRR22582416.126975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..448
                     /product="cilia and flagella associated protein 91 isoform
                     1"
                     /note="MYCBP/AMY-1-associated, testis expressed 1;
                     MYCBP-associated, testis expressed 1; MYCBP associated and
                     testis expressed 1"
                     /calculated_mol_wt=52048
     Region          190..342
                     /region_name="CFAP91"
                     /note="Cilia- and flagella-associated protein 91;
                     pfam14738"
                     /db_xref="CDD:464290"
     CDS             1..448
                     /gene="Cfap91"
                     /gene_synonym="Maats1; RGD1305539"
                     /coded_by="NM_001430786.1:74..1420"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303920"
                     /db_xref="RGD:1305539"
ORIGIN      
        1 msqtvtiqep rtnvpgflfq crdvlrakgr satrvydfly dplfivsser dhaqaniqat
       61 lvrsrlkkvp nfrsmfsnlf hhprysmyws ksdpvpphvs rewrgqeakh kevlrlraav
      121 dasfqkpeek yedadvsgkn rykffdrpfl pflqplplnv vlstaktgpl llspesskys
      181 imptkstvgt qtdyrdadiq tdpyspeyvv cqdtipellt lanltwgrgl paglaevemi
      241 erarekrawe atlpplsdsl qaekrrkmmn amerkewafr egeieklqel rlevlkqllk
      301 rreenqnemd mrhlnnqwce lqekkeakvs qihhrhvsni rklvgkgkni egklqrrdii
      361 rdysnfasqv ygplsrlgrf pdnnsedfvv rnhylntyeg lmelesslpd fvtqpriqap
      421 kpkvittkag flkrmartdy elaeihkv
//
LOCUS       NP_001425422             496 aa            linear   ROD 24-APR-2025
DEFINITION  fibronectin type III and SPRY domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001425422
VERSION     NP_001425422.1
DBSOURCE    REFSEQ: accession NM_001438493.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Manabe,Ri., Whitmore,L., Weiss,J.M. and Horwitz,A.R.
  TITLE     Identification of a novel microtubule-associated protein that
            regulates microtubule organization and cytokinesis by using a
            GFP-screening strategy
  JOURNAL   Curr Biol 12 (22), 1946-1951 (2002)
   PUBMED   12445389
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Stein,P.A., Toret,C.P., Salic,A.N., Rolls,M.M. and Rapoport,T.A.
  TITLE     A novel centrosome-associated protein with affinity for
            microtubules
  JOURNAL   J Cell Sci 115 (Pt 17), 3389-3402 (2002)
   PUBMED   12154070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160924.1, SRR26643293.48486.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..496
                     /product="fibronectin type III and SPRY domain-containing
                     protein 1"
                     /note="fibronectin type 3 and SPRY domain-containing
                     protein; fibronectin type 3 and SPRY domain-containing
                     protein-like1"
                     /calculated_mol_wt=55496
     Region          4..120
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          165..265
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(165,237,253)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(254..255,257..258)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          270..476
                     /region_name="SPRY_PRY_FSD1"
                     /note="Fibronectin type III and SPRY containing 1 (FSD1)
                     domain includes PRY at the N-terminus; cd12901"
                     /db_xref="CDD:293958"
     CDS             1..496
                     /gene="Fsd1"
                     /gene_synonym="Fsd1l1"
                     /coded_by="NM_001438493.1:154..1644"
                     /db_xref="GeneID:301506"
                     /db_xref="RGD:1583850"
ORIGIN      
        1 medqrealrk ivttlamkne etqtfiyslk qmllnveans akvqedleae fqsltsvlee
       61 lresmlmkik qerasrtyel qnqltactra lesseellet anqtlqaadr edfpqaakqi
      121 kdgvtmapaf rlslkakvsd nmshlmvdft qerqmlqalk flpvpsapii nlaeslvadn
      181 cvtlvwhmpe edskidhyvl eyrrtnfegp prlkedhpwm vvegirhtec tltglkfdmk
      241 ymnvrvkacn kavagefsep vtletpafmf rldgstshqn lrveglsvew damggkvqdi
      301 karekegkgr taspvnspar gtpspkrtas grggrdrfta esytvlgdtp idsgehywev
      361 rfepdskafg lgvayrslgr feqlgktaas wclhannwlq asftakhank vkvldspvpd
      421 clgvhcdfhq gllsfynart kqllhtfktk ftqpllpaft vwcgsfqvtt glqvpsavrc
      481 lqkrgsatss sntslt
//
LOCUS       NP_001424968             288 aa            linear   ROD 24-APR-2025
DEFINITION  alpha/beta hydrolase domain-containing protein 17B [Rattus
            norvegicus].
ACCESSION   NP_001424968 XP_006231224
VERSION     NP_001424968.1
DBSOURCE    REFSEQ: accession NM_001438039.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Tortosa,E., Adolfs,Y., Fukata,M., Pasterkamp,R.J., Kapitein,L.C.
            and Hoogenraad,C.C.
  TITLE     Dynamic Palmitoylation Targets MAP6 to the Axon to Promote
            Microtubule Stabilization during Neuronal Polarization
  JOURNAL   Neuron 94 (4), 809-825 (2017)
   PUBMED   28521134
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Yokoi,N., Fukata,Y., Sekiya,A., Murakami,T., Kobayashi,K. and
            Fukata,M.
  TITLE     Identification of PSD-95 Depalmitoylating Enzymes
  JOURNAL   J Neurosci 36 (24), 6431-6444 (2016)
   PUBMED   27307232
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Lin,D.T. and Conibear,E.
  TITLE     ABHD17 proteins are novel protein depalmitoylases that regulate
            N-Ras palmitate turnover and subcellular localization
  JOURNAL   Elife 4, e11306 (2015)
   PUBMED   26701913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 15, 2025 this sequence version replaced XP_006231224.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.1233629.1,
                                           SRR26360172.118024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..288
                     /product="alpha/beta hydrolase domain-containing protein
                     17B"
                     /EC_number="3.1.2.22"
                     /note="abhydrolase domain-containing protein FAM108B1;
                     family with sequence similarity 108, member B1;
                     abhydrolase domain-containing protein 17B; protein
                     ABHD17B"
                     /calculated_mol_wt=32070
     Region          58..285
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY17.1)"
     CDS             1..288
                     /gene="Abhd17b"
                     /gene_synonym="Cgi67l; Fam108b1; RGD1305246"
                     /coded_by="NM_001438039.1:409..1275"
                     /db_xref="GeneID:309399"
                     /db_xref="RGD:1305246"
ORIGIN      
        1 mnnlsfselc clfccppcpg kiasklaflp pdptytlmcd esgsrwtlhl seradwqyss
       61 rekdaiecfm trtskgnria cmfvrcspna kytllfshgn avdlgqmssf yiglgsrinc
      121 nifsydysgy gassgkptek nlyadveaaw lalrtrygir penviiygqs igtvpsvdla
      181 aryesaavil hspltsgmrv afpdtkktyc fdafpnidki skitspvlii hgtedevidf
      241 shglalferc qrpveplwve gaghndvely gqylerlkqf vsqelvnl
//
LOCUS       NP_001128098             292 aa            linear   ROD 24-APR-2025
DEFINITION  coiled-coil domain-containing protein 24 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001128098 XP_001072060 XP_575895
VERSION     NP_001128098.1
DBSOURCE    REFSEQ: accession NM_001134626.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_575895.2, XP_001072060.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1295283.1,
                                           SRR22582424.1122401.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..292
                     /product="coiled-coil domain-containing protein 24 isoform
                     2"
                     /note="coiled-coil domain-containing protein 24"
                     /calculated_mol_wt=32422
     Region          21..216
                     /region_name="CCDC24"
                     /note="Coiled-coil domain-containing protein 24 family;
                     pfam15669"
                     /db_xref="CDD:464792"
     CDS             1..292
                     /gene="Ccdc24"
                     /gene_synonym="RGD1562911"
                     /coded_by="NM_001134626.2:311..1189"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500534"
                     /db_xref="RGD:1562911"
ORIGIN      
        1 mpgdspalwe lveehvplpe rpevkrilge aavdlslelr eevamlkall qdlqssqvsd
       61 spsllapppl lrdlmrqelr qllqglrlka isegrdqtqm waqysprvlr faleeprses
      121 tqqdpfpmra geprtgmsst ervtltspvs scprdltvik dqlnvsnidq vvrhlrslle
      181 eechmlqkei ahlqhcleme qmqvhqpske almptlggkd prraprvpsp lplphtvhtt
      241 vytpeeagai spvpfhrdkg seegngtgat dlsgaflfsc qaqvhqttgw av
//
LOCUS       NP_077335                826 aa            linear   ROD 25-APR-2025
DEFINITION  hypoxia-inducible factor 1-alpha [Rattus norvegicus].
ACCESSION   NP_077335
VERSION     NP_077335.2
DBSOURCE    REFSEQ: accession NM_024359.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Kong,F., Xia,P., Shi,Y., Ye,Z., Zhang,X., Yu,C., Cheng,K. and Li,X.
  TITLE     Ultrasound-targeted microbubble destruction facilitates cartilage
            repair through increased the migration of mesenchymal stem cells
            via HIF-1alpha-mediated glycolysis pathway in rats
  JOURNAL   Biochem Biophys Res Commun 726, 150229 (2024)
   PUBMED   38908346
  REMARK    GeneRIF: Ultrasound-targeted microbubble destruction facilitates
            cartilage repair through increased the migration of mesenchymal
            stem cells via HIF-1alpha-mediated glycolysis pathway in rats.
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Xiaoshan,Z., Huan,C., Zhilin,G., Liwen,M., Yan,Z. and Yue,C.
  TITLE     Hypoxia-inducible factor-1alpha attenuates renal podocyte injury in
            male rats in a simulated high-altitude environment by upregulating
            Kruppel-like factor 4 expression
  JOURNAL   Exp Physiol 109 (7), 1188-1198 (2024)
   PUBMED   38774964
  REMARK    GeneRIF: Hypoxia-inducible factor-1alpha attenuates renal podocyte
            injury in male rats in a simulated high-altitude environment by
            upregulating Kruppel-like factor 4 expression.
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Xu,L., Yang,M., Wei,A., Wei,Z., Qin,Y., Wang,K., Li,B., Chen,K.,
            Liu,C., Li,C. and Wang,T.
  TITLE     Aerobic exercise-induced HIF-1alpha upregulation in heart failure:
            exploring potential impacts on MCT1 and MPC1 regulation
  JOURNAL   Mol Med 30 (1), 83 (2024)
   PUBMED   38867145
  REMARK    GeneRIF: Aerobic exercise-induced HIF-1alpha upregulation in heart
            failure: exploring potential impacts on MCT1 and MPC1 regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 826)
  AUTHORS   Mao,C., Huang,J., Liu,H., Liu,Y., Hu,Z. and Xu,R.
  TITLE     Nur77 induced by HIF-1alpha mediates vascular remodeling in hypoxic
            pulmonary hypertension
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (6), 233-237 (2024)
   PUBMED   38836656
  REMARK    GeneRIF: Nur77 induced by HIF-1alpha mediates vascular remodeling
            in hypoxic pulmonary hypertension.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 826)
  AUTHORS   Wang,G.L., Jiang,B.H., Rue,E.A. and Semenza,G.L.
  TITLE     Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS
            heterodimer regulated by cellular O2 tension
  JOURNAL   Proc Natl Acad Sci U S A 92 (12), 5510-5514 (1995)
   PUBMED   7539918
REFERENCE   7  (residues 1 to 826)
  AUTHORS   Semenza,G.L., Roth,P.H., Fang,H.M. and Wang,G.L.
  TITLE     Transcriptional regulation of genes encoding glycolytic enzymes by
            hypoxia-inducible factor 1
  JOURNAL   J Biol Chem 269 (38), 23757-23763 (1994)
   PUBMED   8089148
REFERENCE   8  (residues 1 to 826)
  AUTHORS   Wang,G.L. and Semenza,G.L.
  TITLE     General involvement of hypoxia-inducible factor 1 in
            transcriptional response to hypoxia
  JOURNAL   Proc Natl Acad Sci U S A 90 (9), 4304-4308 (1993)
   PUBMED   8387214
REFERENCE   9  (residues 1 to 826)
  AUTHORS   Obara,N. and Takeda,M.
  TITLE     Expression of neural cell adhesion molecule (NCAM) during the first
            molar development in the mouse
  JOURNAL   Anat Embryol (Berl) 187 (3), 209-219 (1993)
   PUBMED   8470821
REFERENCE   10 (residues 1 to 826)
  AUTHORS   Semenza,G.L. and Wang,G.L.
  TITLE     A nuclear factor induced by hypoxia via de novo protein synthesis
            binds to the human erythropoietin gene enhancer at a site required
            for transcriptional activation
  JOURNAL   Mol Cell Biol 12 (12), 5447-5454 (1992)
   PUBMED   1448077
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Mar 15, 2021 this sequence version replaced NP_077335.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF057308.1, SRR26643285.24954.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..826
                     /product="hypoxia-inducible factor 1-alpha"
                     /note="hypoxia-inducible factor 1, alpha subunit (basic
                     helix-loop-helix transcription factor); hypoxia inducible
                     factor 1 alpha subunit; HIF1 alpha"
                     /calculated_mol_wt=92348
     Region          14..84
                     /region_name="bHLH-PAS_HIF1a_PASD8"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in hypoxia-inducible factor 1-alpha (HIF1a)
                     and similar proteins; cd19727"
                     /db_xref="CDD:381570"
     Site            order(19..20,22..24,27..28,30..31,56..57)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381570"
     Region          22..31
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            order(33..34,36..37,40..41,44..45,56..58,61..62,65,68..69,
                     72)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381570"
     Region          94..149
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          171..192
                     /region_name="Required for heterodimer formation with
                     ARNT. /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          255..340
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(256,260,266,279..282,308,313)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(276,280,288,291..292,320,322)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          402..603
                     /region_name="ODD"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            403
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          493..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Region          531..575
                     /region_name="NTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            532
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          551..580
                     /region_name="HIF-1"
                     /note="Hypoxia-inducible factor-1; pfam11413"
                     /db_xref="CDD:463274"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Site            564
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          576..785
                     /region_name="ID"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          580..603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          640..>788
                     /region_name="PLN03113"
                     /note="DNA ligase 1; Provisional"
                     /db_xref="CDD:215584"
     Region          655..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     Region          718..722
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Region          786..826
                     /region_name="CTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (O35800.1)"
     Region          789..825
                     /region_name="HIF-1a_CTAD"
                     /note="HIF-1 alpha C terminal transactivation domain;
                     pfam08778"
                     /db_xref="CDD:430212"
     Site            803
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine.
                     /evidence=ECO:0000250|UniProtKB:Q16665; propagated from
                     UniProtKB/Swiss-Prot (O35800.1)"
     CDS             1..826
                     /gene="Hif1a"
                     /gene_synonym="HIF1-alpha; MOP1"
                     /coded_by="NM_024359.2:327..2807"
                     /db_xref="GeneID:29560"
                     /db_xref="RGD:61928"
ORIGIN      
        1 megaggenek knrmsserrk eksrdaarsr rskesevfye lahqlplphn vsshldkasv
       61 mrltisylrv rklldagdld iedemkaqmn cfylkaldgf vmvltddgdm iyisdnvnky
      121 mgltqfeltg hsvfdfthpc dheemremlt hrngpvrkgk eqntqrsffl rmkctltsrg
      181 rtmniksatw kvlhctghih vydtssnqpq cgykkppmtc lvlicepiph psnieiplds
      241 ktflsrhsld mkfsycderi telmgyepee llgrsiyeyy haldsdhltk thhdmftkgq
      301 vttgqyrmla krggyvwvet qatviyntkn sqpqcivcvn yvvsgiiqhd lifslqqtes
      361 vlkpvessdm kmtqlftkve sedtsclfdk lkkepdaltl lapaagdtii sldfgsddte
      421 tedqqledvp lyndvmfpss neklninlam splpasetpk plrssadpal nqevalkles
      481 speslglsft mpqiqdqpas psdgstrqss pepnspseyc fdvdsdmvnv fklelveklf
      541 aedteaknpf saqdtdldle mlapyipmdd dfqlrsfdql splesnspsp psvstvtgfq
      601 qtqlqkptit vtaatattat ttdeskavtk dniedikili asppstqvpq emttakasay
      661 sgthsrttsp dragkrviek tdkahprsln lsvtlnqrnt vpeeelnpkt ialqnaqrkr
      721 kmehdgslfq aagigtllqq pgdraptmsl swkrvkgyis seqdgmeqkt iflipsdlac
      781 rllgqsmdes glpqltsydc evnapiqgsr nllqgeellr aldqvn
//
LOCUS       NP_001407186              51 aa            linear   ROD 25-APR-2025
DEFINITION  peroxisomal testis-specific protein 1 [Rattus norvegicus].
ACCESSION   NP_001407186
VERSION     NP_001407186.1
DBSOURCE    REFSEQ: accession NM_001420257.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Kaczmarek,K., Studencka,M., Meinhardt,A., Wieczerzak,K., Thoms,S.,
            Engel,W. and Grzmil,P.
  TITLE     Overexpression of peroxisomal testis-specific 1 protein induces
            germ cell apoptosis and leads to infertility in male mice
  JOURNAL   Mol Biol Cell 22 (10), 1766-1779 (2011)
   PUBMED   21460186
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Kaczmarek,K., Niedzialkowska,E., Studencka,M., Schulz,Y. and
            Grzmil,P.
  TITLE     Ccdc33, a predominantly testis-expressed gene, encodes a putative
            peroxisomal protein
  JOURNAL   Cytogenet Genome Res 126 (3), 243-252 (2009)
   PUBMED   20068295
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Grzmil,P., Burfeind,C., Preuss,T., Dixkens,C., Wolf,S., Engel,W.
            and Burfeind,P.
  TITLE     The putative peroxisomal gene Pxt1 is exclusively expressed in the
            testis
  JOURNAL   Cytogenet Genome Res 119 (1-2), 74-82 (2007)
   PUBMED   18160785
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.744304.1,
                                           SRR26360181.1396951.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..51
                     /product="peroxisomal testis-specific protein 1"
                     /note="small testis-specific peroxisomal protein;
                     peroxisomal, testis specific 1"
                     /calculated_mol_wt=5952
     Region          1..51
                     /region_name="PXT1"
                     /note="Peroxisomal testis-specific protein 1; pfam15214"
                     /db_xref="CDD:464566"
     CDS             1..51
                     /gene="Pxt1"
                     /coded_by="NM_001420257.1:132..287"
                     /db_xref="GeneID:100360640"
                     /db_xref="RGD:2321717"
ORIGIN      
        1 mqlrhigdsv nhrmiqehfp qevgnvlvpl valmfmrgqv llrffwnnhl l
//
LOCUS       NP_037328                468 aa            linear   ROD 25-APR-2025
DEFINITION  peroxisome proliferator-activated receptor alpha [Rattus
            norvegicus].
ACCESSION   NP_037328
VERSION     NP_037328.1
DBSOURCE    REFSEQ: accession NM_013196.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Hu,T., Yu,W.P., Wang,X.Q., Wang,Z.Y., Xu,Z.Q., Hu,F.J., Liu,J.C.,
            Yu,F. and Wang,L.J.
  TITLE     Activation of PPAR-alpha attenuates myocardial ischemia/reperfusion
            injury by inhibiting ferroptosis and mitochondrial injury via
            upregulating 14-3-3eta
  JOURNAL   Sci Rep 14 (1), 15246 (2024)
   PUBMED   38956068
  REMARK    GeneRIF: Activation of PPAR-alpha attenuates myocardial
            ischemia/reperfusion injury by inhibiting ferroptosis and
            mitochondrial injury via upregulating 14-3-3eta.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhu,L., Yao,X., Mo,Y., Chen,M.W., Li,S.C., Liu,J.Q. and Liu,H.Y.
  TITLE     miR-4433a-3p promotes granulosa cell apoptosis by targeting
            peroxisome proliferator-activated receptor alpha and inducing
            immune cell infiltration in polycystic ovarian syndrome
  JOURNAL   J Assist Reprod Genet 40 (6), 1447-1459 (2023)
   PUBMED   37204637
  REMARK    GeneRIF: miR-4433a-3p promotes granulosa cell apoptosis by
            targeting peroxisome proliferator-activated receptor alpha and
            inducing immune cell infiltration in polycystic ovarian syndrome.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Shen,W., Yang,L., Yang,Y., Wang,P., Tao,X., Shen,Y., Wang,S. and
            Shen,Y.
  TITLE     PRDX6 Promotes Fatty Acid Oxidation via PLA2-Dependent PPARalpha
            Activation in Rats Fed High-Fat Diet
  JOURNAL   Antioxid Redox Signal 38 (16-18), 1184-1200 (2023)
   PUBMED   36401357
  REMARK    GeneRIF: PRDX6 Promotes Fatty Acid Oxidation via PLA2-Dependent
            PPARalpha Activation in Rats Fed High-Fat Diet.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Zhao,H.X., Zhang,Z., Hu,F., Wei,Q.F., Yu,Y.S. and Zhao,H.D.
  TITLE     Swimming exercise activates peroxisome proliferator-activated
            receptor-alpha and mitigates age-related renal fibrosis in rats
  JOURNAL   Mol Cell Biochem 478 (5), 1109-1116 (2023)
   PUBMED   36219352
  REMARK    GeneRIF: Swimming exercise activates peroxisome
            proliferator-activated receptor-alpha and mitigates age-related
            renal fibrosis in rats.
REFERENCE   5  (residues 1 to 468)
  AUTHORS   DeFronzo,R.A.
  TITLE     Chiglitazar: a novel pan-PPAR agonist
  JOURNAL   Sci Bull (Beijing) 66 (15), 1497-1498 (2021)
   PUBMED   36654276
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Kliewer,S.A., Sundseth,S.S., Jones,S.A., Brown,P.J., Wisely,G.B.,
            Koble,C.S., Devchand,P., Wahli,W., Willson,T.M., Lenhard,J.M. and
            Lehmann,J.M.
  TITLE     Fatty acids and eicosanoids regulate gene expression through direct
            interactions with peroxisome proliferator-activated receptors alpha
            and gamma
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4318-4323 (1997)
   PUBMED   9113987
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Chu,R., Lin,Y., Rao,M.S. and Reddy,J.K.
  TITLE     Cloning and identification of rat deoxyuridine triphosphatase as an
            inhibitor of peroxisome proliferator-activated receptor alpha
  JOURNAL   J Biol Chem 271 (44), 27670-27676 (1996)
   PUBMED   8910358
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Shalev,A., Siegrist-Kaiser,C.A., Yen,P.M., Wahli,W., Burger,A.G.,
            Chin,W.W. and Meier,C.A.
  TITLE     The peroxisome proliferator-activated receptor alpha is a
            phosphoprotein: regulation by insulin
  JOURNAL   Endocrinology 137 (10), 4499-4502 (1996)
   PUBMED   8828512
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Kliewer,S.A., Forman,B.M., Blumberg,B., Ong,E.S., Borgmeyer,U.,
            Mangelsdorf,D.J., Umesono,K. and Evans,R.M.
  TITLE     Differential expression and activation of a family of murine
            peroxisome proliferator-activated receptors
  JOURNAL   Proc Natl Acad Sci U S A 91 (15), 7355-7359 (1994)
   PUBMED   8041794
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Gottlicher,M., Widmark,E., Li,Q. and Gustafsson,J.A.
  TITLE     Fatty acids activate a chimera of the clofibric acid-activated
            receptor and the glucocorticoid receptor
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4653-4657 (1992)
   PUBMED   1316614
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M88592.1, SRR26643287.18982.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..468
                     /product="peroxisome proliferator-activated receptor
                     alpha"
                     /note="PPAR-alpha; nuclear receptor subfamily 1 group C
                     member 1"
                     /calculated_mol_wt=52246
     Region          101..184
                     /region_name="NR_DBD_Ppar"
                     /note="DNA-binding domain of peroxisome
                     proliferator-activated receptors (PPAR) is composed of two
                     C4-type zinc fingers; cd06965"
                     /db_xref="CDD:143523"
     Site            order(102,105,119,122,138,143,153,156)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143523"
     Site            order(110..114,120..121,123,125,127..128,131,150..151,154,
                     157,168,171..175,177)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143523"
     Site            order(148..149,151..152)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143523"
     Region          201..467
                     /region_name="NR_LBD_PPAR"
                     /note="The ligand binding domain of peroxisome
                     proliferator-activated receptors; cd06932"
                     /db_xref="CDD:132730"
     Site            order(275..276,280,314,318,321,330,332,355,440)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132730"
     Site            order(285,288,292,297,302..303,305..306,309..310)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132730"
     Region          304..433
                     /region_name="Required for heterodimerization with RXRA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P37230.1)"
     Site            order(364,386,389,398,421,425,428,430..431,434..435,442)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:132730"
     Site            433
                     /site_type="other"
                     /note="Essential for heterodimerization with RXRA.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P37230.1)"
     CDS             1..468
                     /gene="Ppara"
                     /gene_synonym="PPAR"
                     /coded_by="NM_013196.2:378..1784"
                     /db_xref="GeneID:25747"
                     /db_xref="RGD:3369"
ORIGIN      
        1 mvdtespicp lspleaddle splseeflqe mgniqeisqs lgeessgsfs fadyqylgsc
       61 pgsegsvitd tlspasspss vscpavptst despgnalni ecricgdkas gyhygvhace
      121 gckgffrrti rlklaydkcd rsckiqkknr nkcqycrfhk clsvgmshna irfgrmprse
      181 kaklkaeilt cehdlkdset adlkslakri heaylknfnm nkvkarvila gktsnnppfv
      241 ihdmetlcma ektlvakmva ngvenkeaev rffhccqcms vetvteltef akaipgfanl
      301 dlndqvtllk ygvyeaiftm lsslmnkdgm liaygngfit reflknlrkp fcdimepkfd
      361 famkfnalel ddsdislfva aiiccgdrpg llnigyiekl qegivhvlkl hlqsnhpddt
      421 flfpkllqkm vdlrqlvteh aqlvqvikkt esdaalhpll qeiyrdmy
//
LOCUS       NP_112637                796 aa            linear   ROD 25-APR-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator
            1-alpha [Rattus norvegicus].
ACCESSION   NP_112637
VERSION     NP_112637.1
DBSOURCE    REFSEQ: accession NM_031347.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Tian,Z., Li,J., Tang,H., Liu,W., Hou,H., Wang,C., Li,D., Chen,G.,
            Xia,T. and Wang,A.
  TITLE     ZLN005 alleviates PBDE-47 induced impairment of mitochondrial
            translation and neurotoxicity through PGC-1alpha/ERRalpha axis
  JOURNAL   J Hazard Mater 471, 134331 (2024)
   PUBMED   38677116
  REMARK    GeneRIF: ZLN005 alleviates PBDE-47 induced impairment of
            mitochondrial translation and neurotoxicity through
            PGC-1alpha/ERRalpha axis.
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Figarola-Centurion,I., Escoto-Delgadillo,M.,
            Gonzalez-Enriquez,G.V., Gutierrez-Sevilla,J.E., Vazquez-Valls,E.,
            Cardenas-Bedoya,J. and Torres-Mendoza,B.M.
  TITLE     HIV-1 Tat Induces Dysregulation of PGC1-Alpha and Sirtuin 3
            Expression in Neurons: The Role of Mitochondrial Biogenesis in
            HIV-Associated Neurocognitive Disorder (HAND)
  JOURNAL   Int J Mol Sci 24 (24), 17566 (2023)
   PUBMED   38139395
  REMARK    GeneRIF: HIV-1 Tat Induces Dysregulation of PGC1-Alpha and Sirtuin
            3 Expression in Neurons: The Role of Mitochondrial Biogenesis in
            HIV-Associated Neurocognitive Disorder (HAND).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Hoshino,D., Wada,R., Mori,Y., Takeda,R., Nonaka,Y., Kano,R.,
            Takagi,R. and Kano,Y.
  TITLE     Cooling of male rat skeletal muscle during endurance-like
            contraction attenuates contraction-induced PGC-1alpha mRNA
            expression
  JOURNAL   Physiol Rep 11 (21), e15867 (2023)
   PUBMED   37962014
  REMARK    GeneRIF: Cooling of male rat skeletal muscle during endurance-like
            contraction attenuates contraction-induced PGC-1alpha mRNA
            expression.
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Zou,Y., Wu,S., Wen,F., Ge,Y. and Luo,S.
  TITLE     PGC-1alpha Inhibits Schwann Cell Dedifferentiation and Delays
            Peripheral Nerve Degeneration by Targeting PON1
  JOURNAL   Cell Mol Neurobiol 43 (7), 3767-3781 (2023)
   PUBMED   37526811
  REMARK    GeneRIF: PGC-1alpha Inhibits Schwann Cell Dedifferentiation and
            Delays Peripheral Nerve Degeneration by Targeting PON1.
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Mu,N., Zhang,T., Zhu,Y., Lu,B., Zheng,Q. and Duan,J.
  TITLE     The mechanism by which miR-494-3p regulates PGC1-alpha-mediated
            inhibition of mitophagy in cardiomyocytes and alleviation of
            myocardial ischemia-reperfusion injury
  JOURNAL   BMC Cardiovasc Disord 23 (1), 204 (2023)
   PUBMED   37085803
  REMARK    GeneRIF: The mechanism by which miR-494-3p regulates
            PGC1-alpha-mediated inhibition of mitophagy in cardiomyocytes and
            alleviation of myocardial ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Louet,J.F., Hayhurst,G., Gonzalez,F.J., Girard,J. and Decaux,J.F.
  TITLE     The coactivator PGC-1 is involved in the regulation of the liver
            carnitine palmitoyltransferase I gene expression by cAMP in
            combination with HNF4 alpha and cAMP-response element-binding
            protein (CREB)
  JOURNAL   J Biol Chem 277 (41), 37991-38000 (2002)
   PUBMED   12107181
  REMARK    GeneRIF: Results show that CREB and HNF4alpha bind the CPT
            promoter, that PGC-1 is involved in liver carnitine
            palmitoyltransferase I (CPT) gene activation by cylic AMP, and that
            PGC-1 acts to coordinate the process of metabolic adaptation in the
            liver.
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Lane,R.H., MacLennan,N.K., Hsu,J.L., Janke,S.M. and Pham,T.D.
  TITLE     Increased hepatic peroxisome proliferator-activated receptor-gamma
            coactivator-1 gene expression in a rat model of intrauterine growth
            retardation and subsequent insulin resistance
  JOURNAL   Endocrinology 143 (7), 2486-2490 (2002)
   PUBMED   12072378
  REMARK    GeneRIF: increased PGC-1 expression and subsequent hepatic glucose
            production contribute to the insulin resistance observed in the
            intrauterine growth retardation juvenile rat
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Oberkofler,H., Esterbauer,H., Linnemayr,V., Strosberg,A.D.,
            Krempler,F. and Patsch,W.
  TITLE     Peroxisome proliferator-activated receptor (PPAR) gamma
            coactivator-1 recruitment regulates PPAR subtype specificity
  JOURNAL   J Biol Chem 277 (19), 16750-16757 (2002)
   PUBMED   11875072
  REMARK    GeneRIF: Peroxisome proliferator-activated receptor (PPAR) gamma
            coactivator-1 recruitment regulates PPAR subtype specificity.
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Kakuma,T., Wang,Z.W., Pan,W., Unger,R.H. and Zhou,Y.T.
  TITLE     Role of leptin in peroxisome proliferator-activated receptor gamma
            coactivator-1 expression
  JOURNAL   Endocrinology 141 (12), 4576-4582 (2000)
   PUBMED   11108270
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Goto,M., Terada,S., Kato,M., Katoh,M., Yokozeki,T., Tabata,I. and
            Shimokawa,T.
  TITLE     cDNA Cloning and mRNA analysis of PGC-1 in epitrochlearis muscle in
            swimming-exercised rats
  JOURNAL   Biochem Biophys Res Commun 274 (2), 350-354 (2000)
   PUBMED   10913342
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB025784.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB025784.1, AY237127.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rattus norvegicus"
                     /strain="Z"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..796
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-alpha"
                     /note="PGC-1-alpha; PPARGC-1-alpha; PPAR-gamma coactivator
                     1-alpha; peroxisome proliferative activated receptor,
                     gamma, coactivator 1 alpha; PGC-1alpha; PPAR gamma
                     coactivator 1alpha variant form-1; Ppargc1a-vf1;
                     peroxisome proliferative activated receptor gamma
                     coactivator 1"
                     /calculated_mol_wt=90491
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          98..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          142..146
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          211..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            252
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            269
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            276
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          288..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          291..337
                     /region_name="Interaction with PPARG.
                     /evidence=ECO:0000250|UniProtKB:Q9UBK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            345
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          348..796
                     /region_name="Mediates interaction with RNF34.
                     /evidence=ECO:0000250|UniProtKB:Q9UBK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            411
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            440
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            449
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          541..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          611..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Region          673..763
                     /region_name="RRM_PPARGC1A"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-alpha
                     (PGC-1alpha, or PPARGC-1-alpha) and similar proteins;
                     cd12623"
                     /db_xref="CDD:410034"
     Site            756
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     Site            777
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9QYK2.1)"
     CDS             1..796
                     /gene="Ppargc1a"
                     /gene_synonym="LRPGC1; PGC-1v; PGCvf; PGCvf-1; PGCvf1;
                     Ppargc1"
                     /coded_by="NM_031347.1:42..2432"
                     /db_xref="GeneID:83516"
                     /db_xref="RGD:620925"
ORIGIN      
        1 mawdmcsqds vwsdiecaal vgedqplcpd lpeldlseld vndldtdsfl gglkwcsdqs
       61 eiisnqynne panifekide eneanllavl tetldslpvd edglpsfdal tdgdvttdne
      121 aspssmpdgt pppqeaeeps llkklllapa ntqlsynecs glstqnhanh thrirtnpai
      181 vktenswsnk aksicqqqkp qrrpcsellk ylttnddpph tkptenrnss rdkcaskkks
      241 htqpqsqhaq akpttlslpl tpespndpkg spfenktier tlsvelsgta gltppttpph
      301 kanqdnpfka spklkpsckt vvppptkrar ysecsgtqgs hstkkgpeqs elyaqlskss
      361 vlsrgheerk tkrpslrlfg dhdycqsvns ktdilinisq elqdsrqldf kdascdwqgh
      421 icsstdssqc ylretleask qvspcstrkq lqdqeirael nkhfghpsqa vfddkvdkts
      481 elrdgnfsne qfsklpvfin sglamdglfd dsedendkls ypwdgtqsys lfdvspscss
      541 fnspcrdsvs ppkslfsqrp qrmrsrsrsf srhrscsrsp ysrsrsrspg srsssrscyy
      601 yesshyrhrt hrnsplyvrs rsrspysrrp rydsyeaneh erlkrdeyrr eyekresera
      661 kqrerqkqka ieerrviyvg kirpdttrte lrdrfevfge ieectvnlrd dgdsygfity
      721 rytcdafaal engytlrrsn etdfelyfcg rkqffksnya dldsnsddfd pastkskyds
      781 ldfdsllkea qrslrr
//
LOCUS       NP_001102273             183 aa            linear   ROD 27-APR-2025
DEFINITION  2-acylglycerol O-acyltransferase 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001102273 XP_001059515 XP_343603
VERSION     NP_001102273.1
DBSOURCE    REFSEQ: accession NM_001108803.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Yen,C.L., Stone,S.J., Cases,S., Zhou,P. and Farese,R.V. Jr.
  TITLE     Identification of a gene encoding MGAT1, a monoacylglycerol
            acyltransferase
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8512-8517 (2002)
   PUBMED   12077311
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474004.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001059515.1, XP_343603.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMD00132274, SAMD00132292
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..183
                     /product="2-acylglycerol O-acyltransferase 1 isoform 2"
                     /EC_number="2.3.1.22"
                     /note="2-acylglycerol O-acyltransferase 1"
                     /calculated_mol_wt=20247
     Region          <1..126
                     /region_name="LPLAT"
                     /note="Lysophospholipid acyltransferases (LPLATs) of
                     glycerophospholipid biosynthesis; cl17185"
                     /db_xref="CDD:473073"
     CDS             1..183
                     /gene="Mogat1"
                     /coded_by="NM_001108803.1:52..603"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363261"
                     /db_xref="RGD:1311644"
ORIGIN      
        1 mskegggnis viviggakel lesfpgrysl cllqrkgfvk ialthgahlv pvfsfgenel
       61 ysqvdnpkgs wlrtaqdkvy nltglalplf yargifqnsf glmpyrkliy tvaavgtaar
      121 ltqksnhqnd ssvsaekgns ficcqvgwcd rdrqplaaps lfrrlctrpq srlmscirrt
      181 wrs
//
LOCUS       NP_001425880             315 aa            linear   ROD 27-APR-2025
DEFINITION  coiled-coil domain-containing protein 24 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001425880 XP_006238771
VERSION     NP_001425880.1
DBSOURCE    REFSEQ: accession NM_001438951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 25, 2025 this sequence version replaced XP_006238771.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.29586.1,
                                           SRR26360181.657856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..315
                     /product="coiled-coil domain-containing protein 24 isoform
                     1"
                     /note="coiled-coil domain-containing protein 24"
                     /calculated_mol_wt=35348
     Region          21..220
                     /region_name="CCDC24"
                     /note="Coiled-coil domain-containing protein 24 family;
                     pfam15669"
                     /db_xref="CDD:464792"
     CDS             1..315
                     /gene="Ccdc24"
                     /gene_synonym="RGD1562911"
                     /coded_by="NM_001438951.1:311..1258"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500534"
                     /db_xref="RGD:1562911"
ORIGIN      
        1 mpgdspalwe lveehvplpe rpevkrilge aavdlslelr eelslqvaml kallqdlqss
       61 qvsdspslla pppllrdlmr qelrqllqgl rlkaisegrd qtqmwaqysp rvlrfaleep
      121 rsestqqdpf pmrageprtg msstervtlt spvsscprdl tvikdqlnvs nidqvvrhlr
      181 slleeechml qkeiahlqhc lemeqmqvhq pskealmptl geikdqkkam eqelqislgp
      241 sysaakhrqk slrpsipgpr plpclhgymp tppsercphp qgqastrrwg rqlrysycke
      301 tastsvssaa sqapt
//
LOCUS       NP_001032268            1166 aa            linear   ROD 27-APR-2025
DEFINITION  tectonin beta-propeller repeat-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001032268 XP_221926
VERSION     NP_001032268.1
DBSOURCE    REFSEQ: accession NM_001037191.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1166)
  AUTHORS   Chen,D., Fan,W., Lu,Y., Ding,X., Chen,S. and Zhong,Q.
  TITLE     A mammalian autophagosome maturation mechanism mediated by TECPR1
            and the Atg12-Atg5 conjugate
  JOURNAL   Mol Cell 45 (5), 629-641 (2012)
   PUBMED   22342342
REFERENCE   2  (residues 1 to 1166)
  AUTHORS   Ogawa,M., Yoshikawa,Y., Kobayashi,T., Mimuro,H., Fukumatsu,M.,
            Kiga,K., Piao,Z., Ashida,H., Yoshida,M., Kakuta,S., Koyama,T.,
            Goto,Y., Nagatake,T., Nagai,S., Kiyono,H., Kawalec,M.,
            Reichhart,J.M. and Sasakawa,C.
  TITLE     A Tecpr1-dependent selective autophagy pathway targets bacterial
            pathogens
  JOURNAL   Cell Host Microbe 9 (5), 376-389 (2011)
   PUBMED   21575909
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC103478.1.
            
            On Nov 18, 2005 this sequence version replaced XP_221926.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1166
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..1166
                     /product="tectonin beta-propeller repeat-containing
                     protein 1"
                     /calculated_mol_wt=130056
     Region          64..125
                     /region_name="DysFN"
                     /note="Dysferlin domain, N-terminal region; smart00693"
                     /db_xref="CDD:214777"
     Region          169..375
                     /region_name="Tectonin"
                     /note="Tectonin domain; pfam19193"
                     /db_xref="CDD:465992"
     Region          209..240
                     /region_name="TECPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          254..285
                     /region_name="TECPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          301..332
                     /region_name="TECPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          344..376
                     /region_name="TECPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          403..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          609..729
                     /region_name="PH1_TECPR1"
                     /note="Tectonin beta-propeller repeat-containing protein 1
                     Pleckstrin homology (PH) domain, repeat 1; cd13300"
                     /db_xref="CDD:270112"
     Region          734..761
                     /region_name="TECPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          766..799
                     /region_name="TECPR"
                     /note="Beta propeller repeats in Physarum polycephalum
                     tectonins, Limulus lectin L-6 and animal hypothetical
                     proteins; smart00706"
                     /db_xref="CDD:214782"
     Region          821..882
                     /region_name="DysFN"
                     /note="Dysferlin domain, N-terminal region; smart00693"
                     /db_xref="CDD:214777"
     Region          893..926
                     /region_name="DysFC"
                     /note="Dysferlin domain, C-terminal region; smart00694"
                     /db_xref="CDD:128935"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z6L1; propagated from
                     UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          <950..1097
                     /region_name="Tectonin"
                     /note="Tectonin domain; pfam19193"
                     /db_xref="CDD:465992"
     Region          958..989
                     /region_name="TECPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          1003..1034
                     /region_name="TECPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          1049..1080
                     /region_name="TECPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          1092..1132
                     /region_name="TECPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     Region          1147..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZBA0.1)"
     CDS             1..1166
                     /gene="Tecpr1"
                     /gene_synonym="RGD1306873"
                     /coded_by="NM_001037191.1:58..3558"
                     /db_xref="GeneID:304285"
                     /db_xref="RGD:1306873"
ORIGIN      
        1 mptsmlwavd lfgrvytlst agqywelckd vqlefkrvsa atqccwgiac dnqvylyvcs
       61 sdvpirhree ayenqrwnpm ggfcekllps drwswsdvsg lqhrpldgva lpspywewes
      121 dwyvdenfgg eptekggwty amdfpatytr dkkwnscvrr rkwiryrryk srdtwakips
      181 kddpkelpdp fndlsvggwe iteepvgrls vwavslqgkv wyrenvshpn pegsswslvd
      241 tpgevvqisc gphdliwatl wegqalvreg icrnnpkgns wsiveppgse ngimhvsagv
      301 svvwaitkdr kvwfrrgvns hnpcgtswie mvgemtmvnv glndqvwgis cedravyfrq
      361 gvtpselsgk twkaivvgre sdrshsgsss sllsagcffg eevrgsgtes apsdtdasse
      421 verqgpersl pkesldnsrn lkgssskghe strntedpme naclaegqak apktsgpdec
      481 hgpaptpael pwtnidlkep kkasnqpaag fpetsglssl glfpmgmeep ygaddhplwa
      541 wvsgggcave agsalkwftv qsglspsvqt lslsitpaqt aawrkqifqq ltertkrele
      601 sfrhyeqave qsvwvktgal qwwcdwkphk wvdvrvaleq ftghdgards ilfiyyvvhe
      661 ekkylhvfln evtvlvpvln eakhsfalyt pertrqrwpv rlaatteqdm ndwltllsls
      721 ccesrkvhgr pslqaiwsvt ckgdifvsep spdleahehl lpcdqmfwrq mgghlriiea
      781 nsrgvvwgig ydhtawvytg gygggcfqgl asstsniytq sdvksvyiye nqrwnpvtgy
      841 tsrglptdry mwsdvtglqe ctkagtkpps lqwtwvsdwy vdfsvlggtd qegwqyasdf
      901 pasyhgyktm kdfvrrrcwa rkcklvtsgp wlevapials dvsiipesad angrghnial
      961 wavsdkgdvl crlgvselnp agsswlhvgt dqpfasvsig acyqvwavar dgsafyrgsv
     1021 spsqpagdcw yhipsppkqk ltqvsvgqts vyaldengnl wyragitpsy pqgsswehvs
     1081 nnvrkvsvgp ldqvwviank vqgshglsrg tvcrrmgvqp repkgqgwdy gigggwdhis
     1141 vranatrapr nmsrdqeahg pgpvcc
//
LOCUS       NP_001120966             431 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase 24 [Rattus norvegicus].
ACCESSION   NP_001120966 XP_001078875 XP_341378
VERSION     NP_001120966.1
DBSOURCE    REFSEQ: accession NM_001127494.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Lu,T.J., Chan,C.H., Ling,P., Chao,Y.M., Bao,B.Y., Chiang,C.Y.,
            Lee,T.H., Weng,Y.P., Kan,W.C. and Lu,T.L.
  TITLE     MST3 (mammalian Ste20-like protein kinase 3), a novel gene involved
            in ion homeostasis and renal regulation of blood pressure in
            spontaneous hypertensive rats
  JOURNAL   Int Urol Nephrol 50 (12), 2299-2307 (2018)
   PUBMED   30328087
  REMARK    GeneRIF: This is the first study reporting that MST3, a Ste20-like
            kinase, exerts a conserved regulatory role in sodium homeostasis
            after high-salt diet and in the development of hypertension.
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Mardakheh,F.K., Self,A. and Marshall,C.J.
  TITLE     RHO binding to FAM65A regulates Golgi reorientation during cell
            migration
  JOURNAL   J Cell Sci 129 (24), 4466-4479 (2016)
   PUBMED   27807006
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Zhang,Y., Hu,H., Tian,T., Zhang,L., Zhao,D., Wu,Q., Chang,Y.,
            Wang,Q., Zhou,S., Feng,G. and Huang,F.
  TITLE     Mst3b promotes spinal cord neuronal regeneration by promoting
            growth cone branching out in spinal cord injury rats
  JOURNAL   Mol Neurobiol 51 (3), 1144-1157 (2015)
   PUBMED   24990316
  REMARK    GeneRIF: Mst3b was identified as a powerful regulator for promoting
            spinal cord injury recovery.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Fidalgo,M., Guerrero,A., Fraile,M., Iglesias,C., Pombo,C.M. and
            Zalvide,J.
  TITLE     Adaptor protein cerebral cavernous malformation 3 (CCM3) mediates
            phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin
            by mammalian Ste20-4 to protect cells from oxidative stress
  JOURNAL   J Biol Chem 287 (14), 11556-11565 (2012)
   PUBMED   22291017
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Lu,T.J., Lai,W.Y., Huang,C.Y., Hsieh,W.J., Yu,J.S., Hsieh,Y.J.,
            Chang,W.T., Leu,T.H., Chang,W.C., Chuang,W.J., Tang,M.J.,
            Chen,T.Y., Lu,T.L. and Lai,M.D.
  TITLE     Inhibition of cell migration by autophosphorylated mammalian
            sterile 20-like kinase 3 (MST3) involves paxillin and
            protein-tyrosine phosphatase-PEST
  JOURNAL   J Biol Chem 281 (50), 38405-38417 (2006)
   PUBMED   17046825
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Irwin,N., Li,Y.M., O'Toole,J.E. and Benowitz,L.I.
  TITLE     Mst3b, a purine-sensitive Ste20-like protein kinase, regulates axon
            outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18320-18325 (2006)
   PUBMED   17114295
  REMARK    GeneRIF: Mst3b, a neuron-specific homolog of the yeast kinase
            Ste20, is critical for axon outgrowth. Mst3b is activated in
            response to trophic factors, and suppressing its expression
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stegert,M.R., Hergovich,A., Tamaskovic,R., Bichsel,S.J. and
            Hemmings,B.A.
  TITLE     Regulation of NDR protein kinase by hydrophobic motif
            phosphorylation mediated by the mammalian Ste20-like kinase MST3
  JOURNAL   Mol Cell Biol 25 (24), 11019-11029 (2005)
   PUBMED   16314523
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Huang,C.Y., Wu,Y.M., Hsu,C.Y., Lee,W.S., Lai,M.D., Lu,T.J.,
            Huang,C.L., Leu,T.H., Shih,H.M., Fang,H.I., Robinson,D.R.,
            Kung,H.J. and Yuan,C.J.
  TITLE     Caspase activation of mammalian sterile 20-like kinase 3 (Mst3).
            Nuclear translocation and induction of apoptosis
  JOURNAL   J Biol Chem 277 (37), 34367-34374 (2002)
   PUBMED   12107159
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EU371958.1.
            
            On or before May 22, 2008 this sequence version replaced
            XP_341378.3, XP_001078875.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU371958.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q24"
     Protein         1..431
                     /product="serine/threonine-protein kinase 24"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 24 (STE20 homolog, yeast);
                     STE20-like kinase MST3; mammalian STE20-like protein
                     kinase 3"
                     /calculated_mol_wt=47859
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q99KH8; propagated from
                     UniProtKB/Swiss-Prot (B0LT89.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99KH8; propagated from
                     UniProtKB/Swiss-Prot (B0LT89.1)"
     Region          22..295
                     /region_name="STKc_MST3_like"
                     /note="Catalytic domain of Mammalian Ste20-like protein
                     kinase 3-like Serine/Threonine Kinases; cd06609"
                     /db_xref="CDD:270786"
     Site            order(30..34,38,51,53,83,99..102,105..106,109,144,
                     146..149,151,161..162,165,179..182,184,211,220)
                     /site_type="active"
                     /db_xref="CDD:270786"
     Site            order(30..34,38,51,53,70,83,99..102,105..106,109,148..149,
                     151,162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270786"
     Site            order(33..34,144,146..148,165,179..182,184,211,220)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270786"
     Site            order(161..172,174..184)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270786"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6E0; propagated from
                     UniProtKB/Swiss-Prot (B0LT89.1)"
     Region          266..280
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B0LT89.1)"
     Region          297..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0LT89.1)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6E0; propagated from
                     UniProtKB/Swiss-Prot (B0LT89.1)"
     Site            313..314
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3, caspase-7 and caspase-8.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (B0LT89.1)"
     Region          323..374
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B0LT89.1)"
     CDS             1..431
                     /gene="Stk24"
                     /gene_synonym="MST-3; Mst3b; RGD1561742"
                     /coded_by="NM_001127494.1:1..1296"
                     /db_xref="GeneID:361092"
                     /db_xref="RGD:1561742"
ORIGIN      
        1 mahspvqsgl pgmqtlkadp eelftkleki gkgsfgevfk gidnrtqkvv aikiidleea
       61 edeiediqqe itvlsqcdsp yvtkyygsyl kdtklwiime ylgggsaldl lepgpldeiq
      121 iatilreilk gldylhsekk ihrdikaanv llsehgevkl adfgvagqlt dtqikrntfv
      181 gtpfwmapev ikqsaydska diwslgitai elakgepphs elhpmkvlfl ipknnpptle
      241 gsysrplkef veaclnkeps frptakellk hkfiirnakk tsyltelidr ykrwkaeqsh
      301 edsssedsdv etdsqasggs dsgdwiftir ekdpknleng tlqpsdlern kmkdfpkrpf
      361 sqclstiisp lfaelkeksq acggnlgsie elrgaiylae eacpgisdtm vaqlvqrlqr
      421 yslsgggasa h
//
LOCUS       NP_599227                328 aa            linear   ROD 27-APR-2025
DEFINITION  deoxynucleotidyltransferase terminal-interacting protein 1 [Rattus
            norvegicus].
ACCESSION   NP_599227 XP_215927
VERSION     NP_599227.2
DBSOURCE    REFSEQ: accession NM_134400.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Itoh,T., Fairall,L., Muskett,F.W., Milano,C.P., Watson,P.J.,
            Arnaudo,N., Saleh,A., Millard,C.J., El-Mezgueldi,M., Martino,F. and
            Schwabe,J.W.
  TITLE     Structural and functional characterization of a cell cycle
            associated HDAC1/2 complex reveals the structural basis for complex
            assembly and nucleosome targeting
  JOURNAL   Nucleic Acids Res 43 (4), 2033-2044 (2015)
   PUBMED   25653165
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Fujisaki,S., Sato,A., Toyomoto,T., Hayano,T., Sugai,M., Kubota,T.
            and Koiwai,O.
  TITLE     Direct binding of TReP-132 with TdT results in reduction of TdT
            activity
  JOURNAL   Genes Cells 11 (1), 47-57 (2006)
   PUBMED   16371131
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Yamashita,N., Shimazaki,N., Ibe,S., Kaneko,R., Tanabe,A.,
            Toyomoto,T., Fujita,K., Hasegawa,T., Toji,S., Tamai,K., Yamamoto,H.
            and Koiwai,O.
  TITLE     Terminal deoxynucleotidyltransferase directly interacts with a
            novel nuclear protein that is homologous to p65
  JOURNAL   Genes Cells 6 (7), 641-652 (2001)
   PUBMED   11473582
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanausek,M., Szemraj,J., Adams,A.K. and Walaszek,Z.
  TITLE     The oncofetal protein p65: a new member of the steroid/thyroid
            receptor superfamily
  JOURNAL   Cancer Detect Prev 20 (2), 94-102 (1996)
   PUBMED   8706045
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC100640.1.
            
            On Jun 14, 2007 this sequence version replaced NP_599227.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100640.1, AF348701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..328
                     /product="deoxynucleotidyltransferase terminal-interacting
                     protein 1"
                     /note="tdIF1; tdT-interacting factor 1; terminal
                     deoxynucleotidyltransferase-interacting factor 1"
                     /calculated_mol_wt=36724
     Region          65..132
                     /region_name="DNTTIP1_dimer"
                     /note="DNTTIP1 dimerization domain; pfam18192"
                     /db_xref="CDD:408020"
     CDS             1..328
                     /gene="Dnttip1"
                     /coded_by="NM_134400.2:54..1040"
                     /db_xref="GeneID:171437"
                     /db_xref="RGD:621627"
ORIGIN      
        1 mgatgdteqp rgpggaergg lelgdagaag qpvltnpwni mikhrqvqrr grrsqmttsf
       61 tdpaismdll ravlqpsine eiqsvfnkym kffqkaalnv rdnvgeevda eqliqeacrs
      121 cleqakllfs dgekviprla helpgikrgr qaeeeshrgs pipkkrkgrp pghvlsndra
      181 aagmvwkpks cepirregpk wdparlnest tfvlgsrank algmggtrgr iyikhphlfk
      241 yaadpqdkhw laeqhhmrat ggkmayllie edirdlaasd dyrgcldlkl eelksfvlps
      301 wmvekmrkym etlrtenehr aaeatpqt
//
LOCUS       NP_001103456             168 aa            linear   ROD 27-APR-2025
DEFINITION  DNA damage-inducible transcript 3 protein [Rattus norvegicus].
ACCESSION   NP_001103456
VERSION     NP_001103456.1
DBSOURCE    REFSEQ: accession NM_001109986.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Mou,L., Sun,D., Qu,J., Tan,X., Wang,S., Zeng,Q. and Liu,C.
  TITLE     GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline
  JOURNAL   J Hazard Mater 476, 135101 (2024)
   PUBMED   39002476
  REMARK    GeneRIF: GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline.
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Ishteyaque,S., Yadav,K.S., Verma,S., Washimkar,K.R. and Mugale,M.N.
  TITLE     CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit apoptosis
            and promotes progression of hepatocellular carcinoma
  JOURNAL   Arch Biochem Biophys 745, 109701 (2023)
   PUBMED   37499993
  REMARK    GeneRIF: CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit
            apoptosis and promotes progression of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Wang,S., Duan,J., Liao,J., Wang,Y., Xiao,X., Li,L., Liu,Y., Gu,H.,
            Yang,P., Fu,D., Du,J., Li,X. and Shao,M.
  TITLE     LncRNA H19 inhibits ER stress induced apoptosis and improves
            diabetic cardiomyopathy by regulating PI3K/AKT/mTOR axis
  JOURNAL   Aging (Albany NY) 14 (16), 6809-6828 (2022)
   PUBMED   36044268
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Yuan,Z., Xiao-Wei,L., Juan,W., Xiu-Juan,L., Nian-Yun,Z. and Lei,S.
  TITLE     HIIT and MICT attenuate high-fat diet-induced hepatic lipid
            accumulation and ER stress via the PERK-ATF4-CHOP signaling pathway
  JOURNAL   J Physiol Biochem 78 (3), 641-652 (2022)
   PUBMED   35315506
  REMARK    GeneRIF: HIIT and MICT attenuate high-fat diet-induced hepatic
            lipid accumulation and ER stress via the PERK-ATF4-CHOP signaling
            pathway.
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Zhan,W., Chen,L., Liu,H., Long,C., Liu,J., Ding,S., Wu,Q. and
            Chen,S.
  TITLE     Pcsk6 Deficiency Promotes Cardiomyocyte Senescence by Modulating
            Ddit3-Mediated ER Stress
  JOURNAL   Genes (Basel) 13 (4), 711 (2022)
   PUBMED   35456517
  REMARK    GeneRIF: Pcsk6 Deficiency Promotes Cardiomyocyte Senescence by
            Modulating Ddit3-Mediated ER Stress.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Jousse,C., Bruhat,A., Carraro,V., Urano,F., Ferrara,M., Ron,D. and
            Fafournoux,P.
  TITLE     Inhibition of CHOP translation by a peptide encoded by an open
            reading frame localized in the chop 5'UTR
  JOURNAL   Nucleic Acids Res 29 (21), 4341-4351 (2001)
   PUBMED   11691921
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Sylvester,S.L., ap Rhys,C.M., Luethy-Martindale,J.D. and
            Holbrook,N.J.
  TITLE     Induction of GADD153, a CCAAT/enhancer-binding protein
            (C/EBP)-related gene, during the acute phase response in rats.
            Evidence for the involvement of C/EBPs in regulating its expression
  JOURNAL   J Biol Chem 269 (31), 20119-20125 (1994)
   PUBMED   8051100
  REMARK    Erratum:[J Biol Chem. 1995 Jun 16;270(24):14842. PMID: 7782352]
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Aman,P., Ron,D., Mandahl,N., Fioretos,T., Heim,S., Arheden,K.,
            Willen,H., Rydholm,A. and Mitelman,F.
  TITLE     Rearrangement of the transcription factor gene CHOP in myxoid
            liposarcomas with t(12;16)(q13;p11)
  JOURNAL   Genes Chromosomes Cancer 5 (4), 278-285 (1992)
   PUBMED   1283316
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Ron,D. and Habener,J.F.
  TITLE     CHOP, a novel developmentally regulated nuclear protein that
            dimerizes with transcription factors C/EBP and LAP and functions as
            a dominant-negative inhibitor of gene transcription
  JOURNAL   Genes Dev 6 (3), 439-453 (1992)
   PUBMED   1547942
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Kesterton,D.B.
  TITLE     A projectionist speaks
  JOURNAL   Med Biol Illus 27 (1), 15-19 (1977)
   PUBMED   70575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CF977695.1, AW916370.1, BC100664.1 and BF282473.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100664.1, U36994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..168
                     /product="DNA damage-inducible transcript 3 protein"
                     /note="C/EBP homologous protein; DDIT-3; growth arrest and
                     DNA-damage-inducible protein GADD153; c/EBP-homologous
                     protein 10; C/EBP zeta; CCAAT/enhancer-binding protein
                     homologous protein"
                     /calculated_mol_wt=18897
     Region          10..26
                     /region_name="N-terminal. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Region          10..18
                     /region_name="Interaction with TRIB3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Region          34..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Region          100..160
                     /region_name="BRLZ"
                     /note="basic region leucin zipper; smart00338"
                     /db_xref="CDD:197664"
     Region          100..129
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Region          101..152
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269861"
     Site            order(104..105,107..109,111..116,118..120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269861"
     Site            order(119,122..123,126..127,129..130,133..134,136..137,
                     140..141,143..144,147..148,150..151)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269861"
     Region          133..147
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     CDS             1..168
                     /gene="Ddit3"
                     /gene_synonym="CHOP; CHOP-10; Chop10; Gadd153; RM4"
                     /coded_by="NM_001109986.1:167..673"
                     /db_xref="GeneID:29467"
                     /db_xref="RGD:62391"
ORIGIN      
        1 maaeslpfaf etvsswelea wyedlqevls sdeiggtyis spgneeeesk tfttldpasl
       61 awlteepgpa evtstsqspr spdssqssma qeeeeedqgr trkrkqsgqc aaragkqrmk
      121 ekeqenerkv aqlaeenerl kqeierltre vettrralid rmvslhqa
//
LOCUS       NP_001007724             300 aa            linear   ROD 27-APR-2025
DEFINITION  7-methylguanosine phosphate-specific 5'-nucleotidase [Rattus
            norvegicus].
ACCESSION   NP_001007724 XP_340904
VERSION     NP_001007724.2
DBSOURCE    REFSEQ: accession NM_001007723.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078963.1 and AW527524.1.
            
            On Aug 31, 2007 this sequence version replaced NP_001007724.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..300
                     /product="7-methylguanosine phosphate-specific
                     5'-nucleotidase"
                     /EC_number="3.1.3.5"
                     /EC_number="3.1.3.91"
                     /note="cytosolic 5'-nucleotidase III-like protein;
                     cN-III-like protein; 5'-nucleotidase, cytosolic III-like;
                     cytosolic 5'-nucleotidase 3B; 7-methylguanosine
                     nucleotidase; N(7)-methylguanylate 5'-phosphatase;
                     cytosolic 5-nucleotidase III-like protein-like"
                     /calculated_mol_wt=34405
     Region          17..289
                     /region_name="HAD_5NT"
                     /note="haloacid dehalogenase (HAD)-like 5'-nucleotidases
                     similar to human cytosolic IIIA and IIIB; cd07504"
                     /db_xref="CDD:319807"
     Site            order(41..45,60,81,85,88,105..106,109,156..158,202,205,
                     229..230,233..234)
                     /site_type="active"
                     /db_xref="CDD:319807"
     Site            256
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q969T7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYP7.2)"
     CDS             1..300
                     /gene="Nt5c3b"
                     /gene_synonym="Nt5c3l"
                     /coded_by="NM_001007723.2:326..1228"
                     /db_xref="GeneID:360629"
                     /db_xref="RGD:1359229"
ORIGIN      
        1 maeevsslmk atvlmrqpgr vqeivsalrr gggdrlqvis dfdmtlsrfa yngqrcpssh
       61 nildnskiis edcrkeltel fhhyypieid phrtikeklp hmvqwwskah sllcqqriqk
      121 fqiaqvvges tamlregykm ffdtlyhnni plfifsagig dileeiirqm kvfhpnihiv
      181 snymdfsedg flkgfkgqli htynknssvc enssyfqqlr nktniillgd sigdltmadg
      241 vpgvqnilki gflndkveer rerymdsydi vlekdetldv vngllqhilr qgdcvelqgs
//
LOCUS       NP_001013105             356 aa            linear   ROD 27-APR-2025
DEFINITION  ELMO domain-containing protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001013105
VERSION     NP_001013105.1
DBSOURCE    REFSEQ: accession NM_001013087.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083623.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083623.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..356
                     /product="ELMO domain-containing protein 3 isoform 2"
                     /note="ELMO domain-containing protein 3; RNA-binding motif
                     and ELMO domain-containing protein 1; potassium channel
                     modulatory factor 1; RNA binding motif and ELMO domain 1;
                     ELMO/CED-12 domain containing 3"
                     /calculated_mol_wt=39883
     Region          154..313
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..356
                     /gene="Elmod3"
                     /gene_synonym="Kcmf1; Rbed1"
                     /coded_by="NM_001013087.1:277..1347"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:297342"
                     /db_xref="RGD:1306408"
ORIGIN      
        1 msetscsfli ekefqdgqve svsaglspsy kdngalmafr gipiselknh gilqvltaet
       61 ngwqpgvvsa emlraqeewe vvdtihpdie sgvssqqpgq fisfnealeh fqtvdlssfk
      121 kriqptiqrt glaalrhclf gppklhqglq eerdlvltia qcgldsqnpt hgrvlqtiyk
      181 kltgskfdca lhgdhwedlg fqganpatdl rgtgflallh llylvmdskt llmaqeilrl
      241 shhhiqqfpf clmsvnitri aiqalreecl srecnrrrkv ipvvnsfyaa tflhlarmwr
      301 tqhntildsg fvlkelgiep ralrsigkrs taelnpqpap aflvwdysra fmhgsr
//
LOCUS       NP_001032437             370 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 830 [Rattus norvegicus].
ACCESSION   NP_001032437 XP_573159
VERSION     NP_001032437.1
DBSOURCE    REFSEQ: accession NM_001037360.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Vandormael-Pournin,S., Guigon,C.J., Ishaq,M., Coudouel,N., Ave,P.,
            Huerre,M., Magre,S., Cohen-Tannoudji,J. and Cohen-Tannoudji,M.
  TITLE     Oocyte-specific inactivation of Omcg1 leads to DNA damage and
            c-Abl/TAp63-dependent oocyte death associated with dramatic
            remodeling of ovarian somatic cells
  JOURNAL   Cell Death Differ 22 (1), 108-117 (2015)
   PUBMED   25168238
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Leguillier,T., Vandormael-Pournin,S., Artus,J., Houlard,M.,
            Picard,C., Bernex,F., Robine,S. and Cohen-Tannoudji,M.
  TITLE     Omcg1 is critically required for mitosis in rapidly dividing mouse
            intestinal progenitors and embryonic stem cells
  JOURNAL   Biol Open 1 (7), 648-657 (2012)
   PUBMED   23213458
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Houlard,M., Artus,J., Leguillier,T., Vandormael-Pournin,S. and
            Cohen-Tannoudji,M.
  TITLE     DNA-RNA hybrids contribute to the replication dependent genomic
            instability induced by Omcg1 deficiency
  JOURNAL   Cell Cycle 10 (1), 108-117 (2011)
   PUBMED   21191184
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Artus,J., Vandormael-Pournin,S., Frodin,M., Nacerddine,K.,
            Babinet,C. and Cohen-Tannoudji,M.
  TITLE     Impaired mitotic progression and preimplantation lethality in mice
            lacking OMCG1, a new evolutionarily conserved nuclear protein
  JOURNAL   Mol Cell Biol 25 (14), 6289-6302 (2005)
   PUBMED   15988037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC104717.1.
            
            On Nov 25, 2005 this sequence version replaced XP_573159.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC104717.1, SRR8487230.70651.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..370
                     /product="zinc finger protein 830"
                     /note="coiled-coil domain-containing protein 16;
                     coiled-coil domain containing 16"
                     /calculated_mol_wt=41485
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHS2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96NB3; propagated from
                     UniProtKB/Swiss-Prot (Q3MHS2.1)"
     Region          18..>144
                     /region_name="PRP11"
                     /note="Splicing factor 3a, subunit 2 [RNA processing and
                     modification]; COG5246"
                     /db_xref="CDD:227571"
     Region          49..82
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          75..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHS2.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96NB3; propagated from
                     UniProtKB/Swiss-Prot (Q3MHS2.1)"
     Region          <224..>362
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MHS2.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96NB3; propagated from
                     UniProtKB/Swiss-Prot (Q3MHS2.1)"
     CDS             1..370
                     /gene="Zfp830"
                     /gene_synonym="Ccdc16; Znf830"
                     /coded_by="NM_001037360.1:8..1120"
                     /db_xref="GeneID:497967"
                     /db_xref="RGD:1562573"
ORIGIN      
        1 masstsartp agkrvvnqee lrrlmkekqr lstnrkries pfakynrlgq lscalcntpv
       61 ksellwqthv lgkqhrerva elkgakgatq gpsagtapqp tkrkttdves qdakkakasv
      121 dqvqpstsas sanfeksgke atrvassktg lgllpdyeee eeeeeeeelg ggeerrdssk
      181 hlpdaqgreh slaspretts nvlpndpfnt nppkaplvph sgsiekaeih ekvverrent
      241 aealpegffd dpevdakvrk vdapkdqmdk ewdefqkamr qvntiseaiv aeedeegrld
      301 rqigeideqi ecyrrveklr nrqdeiknkl kevltikelq kkeeenvdsd degelqdlls
      361 qdwrvkgall
//
LOCUS       NP_598240                141 aa            linear   ROD 27-APR-2025
DEFINITION  ATP synthase F(0) complex subunit C2, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_598240
VERSION     NP_598240.1
DBSOURCE    REFSEQ: accession NM_133556.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Bruggemann,M., Gromes,A., Poss,M., Schmidt,D., Klumper,N.,
            Tolkach,Y., Dietrich,D., Kristiansen,G., Muller,S.C. and
            Ellinger,J.
  TITLE     Systematic Analysis of the Expression of the Mitochondrial ATP
            Synthase (Complex V) Subunits in Clear Cell Renal Cell Carcinoma
  JOURNAL   Transl Oncol 10 (4), 661-668 (2017)
   PUBMED   28672194
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Campo,G., Morciano,G., Pavasini,R., Bonora,M., Sbano,L.,
            Biscaglia,S., Bovolenta,M., Pinotti,M., Punzetti,S., Rizzo,P.,
            Aquila,G., Giorgi,C., Ferrari,R. and Pinton,P.
  TITLE     Fo ATP synthase C subunit serum levels in patients with ST-segment
            Elevation Myocardial Infarction: Preliminary findings
  JOURNAL   Int J Cardiol 221, 993-997 (2016)
   PUBMED   27441480
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Kitchen,M.O., Bryan,R.T., Emes,R.D., Glossop,J.R., Luscombe,C.,
            Cheng,K.K., Zeegers,M.P., James,N.D., Devall,A.J., Mein,C.A.,
            Gommersall,L., Fryer,A.A. and Farrell,W.E.
  TITLE     Quantitative genome-wide methylation analysis of high-grade
            non-muscle invasive bladder cancer
  JOURNAL   Epigenetics 11 (3), 237-246 (2016)
   PUBMED   26929985
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Xie,X., Man,X., Zhu,Z., Yuan,D. and Huang,S.
  TITLE     Tumor suppressor RIZ1 in obesity and the PI3K/AKT/mTOR pathway
  JOURNAL   Obesity (Silver Spring) 24 (2), 389-397 (2016)
   PUBMED   26709097
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   7  (residues 1 to 141)
  AUTHORS   Li,H.S., Zhang,J.Y., Thompson,B.S., Deng,X.Y., Ford,M.E.,
            Wood,P.G., Stolz,D.B., Eagon,P.K. and Whitcomb,D.C.
  TITLE     Rat mitochondrial ATP synthase ATP5G3: cloning and upregulation in
            pancreas after chronic ethanol feeding
  JOURNAL   Physiol Genomics 6 (2), 91-98 (2001)
   PUBMED   11459924
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 141)
  AUTHORS   McGeoch,J.E. and Guidotti,G.
  TITLE     Batten disease and the control of the Fo subunit c pore by cGMP and
            calcium
  JOURNAL   Eur J Paediatr Neurol 5 Suppl A, 147-150 (2001)
   PUBMED   11588987
REFERENCE   9  (residues 1 to 141)
  AUTHORS   Andersson,U., Houstek,J. and Cannon,B.
  TITLE     ATP synthase subunit c expression: physiological regulation of the
            P1 and P2 genes
  JOURNAL   Biochem J 323 (Pt 2) (Pt 2), 379-385 (1997)
   PUBMED   9163327
REFERENCE   10 (residues 1 to 141)
  AUTHORS   Higuti,T., Kuroiwa,K., Kawamura,Y., Morimoto,K. and Tsujita,H.
  TITLE     Molecular cloning and sequence of cDNAs for the import precursors
            of oligomycin sensitivity conferring protein, ATPase inhibitor
            protein, and subunit c of H(+)-ATP synthase in rat mitochondria
  JOURNAL   Biochim Biophys Acta 1172 (3), 311-314 (1993)
   PUBMED   8448208
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128726.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128726.1, FQ209535.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132301, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial precursor"
                     /note="ATP synthase lipid-binding protein, mitochondrial;
                     ATPase protein 9; ATPase subunit c; ATP synthase
                     proteolipid P2; ATP synthase, H+ transporting,
                     mitochondrial Fo complex, subunit C2 (subunit 9); ATP
                     synthase, H+ transporting, mitochondrial F0 complex,
                     subunit c (subunit 9); ATP synthase, H+ transporting,
                     mitochondrial F0 complex, subunit C2 (subunit 9); ATP
                     synthase F(0) complex subunit C2, mitochondrial"
                     /calculated_mol_wt=7608
     transit_peptide 1..66
                     /note="Mitochondrion; propagated from UniProtKB/Swiss-Prot
                     (Q06646.1)"
                     /calculated_mol_wt=7328
     mat_peptide     67..141
                     /product="ATP synthase F(0) complex subunit C2,
                     mitochondrial. /id=PRO_0000002566"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06646.1)"
                     /calculated_mol_wt=7608
     Region          67..141
                     /region_name="ATP9"
                     /note="ATP synthase F0 subunit 9; Provisional; MTH00222"
                     /db_xref="CDD:164765"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06646.1)"
     Site            109
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:30530489; propagated from
                     UniProtKB/Swiss-Prot (Q06646.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06646.1)"
     Site            124
                     /site_type="other"
                     /note="Reversibly protonated during proton transport.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q06646.1)"
     CDS             1..141
                     /gene="Atp5mc2"
                     /gene_synonym="Atp5g2"
                     /coded_by="NM_133556.2:49..474"
                     /db_xref="GeneID:171082"
                     /db_xref="RGD:620051"
ORIGIN      
        1 myacskfvst rslirstsql lsrplsavel krpqmptdeg lsclavrrpl tslipsrsfq
       61 tsaisrdidt aakfigagaa tvgvagsgag igtvfgslii gyarnpslkq qlfsyailgf
      121 alseamglfc lmvaflilfa m
//
LOCUS       NP_001041508             120 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 230 [Rattus norvegicus].
ACCESSION   NP_001041508 XP_001063827 XP_001063869 XP_001079817 XP_001079827
VERSION     NP_001041508.1
DBSOURCE    REFSEQ: accession NM_001048043.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Deng,H.X., Shi,Y., Yang,Y., Ahmeti,K.B., Miller,N., Huang,C.,
            Cheng,L., Zhai,H., Deng,S., Nuytemans,K., Corbett,N.J., Kim,M.J.,
            Deng,H., Tang,B., Yang,Z., Xu,Y., Chan,P., Huang,B., Gao,X.P.,
            Song,Z., Liu,Z., Fecto,F., Siddique,N., Foroud,T., Jankovic,J.,
            Ghetti,B., Nicholson,D.A., Krainc,D., Melen,O., Vance,J.M.,
            Pericak-Vance,M.A., Ma,Y.C., Rajput,A.H. and Siddique,T.
  TITLE     Identification of TMEM230 mutations in familial Parkinson's disease
  JOURNAL   Nat Genet 48 (7), 733-739 (2016)
   PUBMED   27270108
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105614.1.
            
            On or before Feb 10, 2007 this sequence version replaced
            XP_001063827.1, XP_001063869.1, XP_001079817.1, XP_001079827.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105614.1, EX490848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..120
                     /product="transmembrane protein 230"
                     /note="HSPC274 protein; UPF0414 transmembrane protein
                     C20orf30 homolog"
                     /calculated_mol_wt=13073
     Region          2..118
                     /region_name="TMEM_230_134"
                     /note="Transmembrane proteins 230/134; pfam05915"
                     /db_xref="CDD:399128"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96A57; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP5.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96A57; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP5.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP5.1)"
     Site            46..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJP5.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJP5.1)"
     CDS             1..120
                     /gene="Tmem230"
                     /gene_synonym="RGD1307399"
                     /coded_by="NM_001048043.1:224..586"
                     /db_xref="GeneID:681315"
                     /db_xref="RGD:1307399"
ORIGIN      
        1 mmpsrtnlat gipsskvkys rlsstddgyi dlqfkksppk ipykaialat vlfligtfli
       61 iigslllsgy iskggadrav pvliigilvf lpgfyhlria yyaskgyrgy syddipdfdd
//
LOCUS       NP_001037761             212 aa            linear   ROD 27-APR-2025
DEFINITION  amelotin precursor [Rattus norvegicus].
ACCESSION   NP_001037761 XP_001070666
VERSION     NP_001037761.1
DBSOURCE    REFSEQ: accession NM_001044296.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Abbarin,N., San Miguel,S., Holcroft,J., Iwasaki,K. and Ganss,B.
  TITLE     The enamel protein amelotin is a promoter of hydroxyapatite
            mineralization
  JOURNAL   J Bone Miner Res 30 (5), 775-785 (2015)
   PUBMED   25407797
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nishio,C., Wazen,R., Kuroda,S., Moffatt,P. and Nanci,A.
  TITLE     Expression pattern of odontogenic ameloblast-associated and
            amelotin during formation and regeneration of the junctional
            epithelium
  JOURNAL   Eur Cell Mater 20, 393-402 (2010)
   PUBMED   21154245
  REMARK    GeneRIF: ODAM and AMTN have a role at the cell-tooth interface, and
            that ODAM is likely also implicated in cellular events during
            formation and regeneration of the junctional epithelium.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Trueb,B., Taeschler,S., Schild,C. and Lang,N.P.
  TITLE     Expression of phosphoproteins and amelotin in teeth
  JOURNAL   Int J Mol Med 19 (1), 49-54 (2007)
   PUBMED   17143547
  REMARK    GeneRIF: The amino acid sequence of rat amelotin showed 62%
            identity with the sequence from humans. It was expressed
            considerably later than the other enamel proteins, suggesting that
            amelotin may serve a different function.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Moffatt,P., Smith,C.E., St-Arnaud,R., Simmons,D., Wright,J.T. and
            Nanci,A.
  TITLE     Cloning of rat amelotin and localization of the protein to the
            basal lamina of maturation stage ameloblasts and junctional
            epithelium
  JOURNAL   Biochem J 399 (1), 37-46 (2006)
   PUBMED   16787391
  REMARK    GeneRIF: The isolation and characterization of amelotin at the
            expression and localization levels from the rat is reported.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Moffatt,P., Smith,C.E., Sooknanan,R., St-Arnaud,R. and Nanci,A.
  TITLE     Identification of secreted and membrane proteins in the rat incisor
            enamel organ using a signal-trap screening approach
  JOURNAL   Eur J Oral Sci 114 Suppl 1, 139-46 (2006)
   PUBMED   16674676
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Iwasaki,K., Bajenova,E., Somogyi-Ganss,E., Miller,M., Nguyen,V.,
            Nourkeyhani,H., Gao,Y., Wendel,M. and Ganss,B.
  TITLE     Amelotin--a Novel Secreted, Ameloblast-specific Protein
  JOURNAL   J Dent Res 84 (12), 1127-1132 (2005)
   PUBMED   16304441
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ198381.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001070666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ198381.1, AM231717.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840111,
                                           SAMN12840121 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..212
                     /product="amelotin precursor"
                     /calculated_mol_wt=20422
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1676
     mat_peptide     17..212
                     /product="Amelotin.
                     /evidence=ECO:0000250|UniProtKB:Q6UX39.
                     /id=PRO_5000140668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS82.1)"
                     /calculated_mol_wt=20422
     Region          17..210
                     /region_name="Amelotin"
                     /note="pfam15757"
                     /db_xref="CDD:464850"
     Region          23..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS82.1)"
     Region          141..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS82.1)"
     CDS             1..212
                     /gene="Amtn"
                     /coded_by="NM_001044296.1:93..731"
                     /db_xref="GeneID:689404"
                     /db_xref="RGD:1592356"
ORIGIN      
        1 mktvvlllcl lgsaqslprq lspalgapat kptpgqvtpl tqqqpnqvfp sislipltql
       61 ltlgsdlplf npatmphgtq tlpftlgpln gqqqlqpqml piivaqlgaq gallsseelp
      121 lasqiftgll ihplfpgaiq psgqtgakpd vqngalptrq agaspanqat tpghttpavt
      181 ddddyemstp aglqrathtt egttmdppnr tk
//
LOCUS       NP_001101957             332 aa            linear   ROD 27-APR-2025
DEFINITION  apoptosis-enhancing nuclease [Rattus norvegicus].
ACCESSION   NP_001101957 XP_001064302 XP_341875
VERSION     NP_001101957.1
DBSOURCE    REFSEQ: accession NM_001108487.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Kawase,T., Ichikawa,H., Ohta,T., Nozaki,N., Tashiro,F., Ohki,R. and
            Taya,Y.
  TITLE     p53 target gene AEN is a nuclear exonuclease required for
            p53-dependent apoptosis
  JOURNAL   Oncogene 27 (27), 3797-3810 (2008)
   PUBMED   18264133
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Lee,J.H., Koh,Y.A., Cho,C.K., Lee,S.J., Lee,Y.S. and Bae,S.
  TITLE     Identification of a novel ionizing radiation-induced nuclease, AEN,
            and its functional characterization in apoptosis
  JOURNAL   Biochem Biophys Res Commun 337 (1), 39-47 (2005)
   PUBMED   16171785
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166435.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064302.1, XP_341875.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166435.1, SRR8487226.50006.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..332
                     /product="apoptosis-enhancing nuclease"
                     /EC_number="3.1.-.-"
                     /note="interferon stimulated exonuclease gene 20-like 1;
                     interferon-stimulated 20 kDa exonuclease-like 1"
                     /calculated_mol_wt=36930
     Region          1..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUW6.1)"
     Region          21..29
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8WTP8"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUW6.1)"
     Region          106..262
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            order(109..112,188..189,191..193,253)
                     /site_type="active"
                     /db_xref="CDD:99852"
     Site            order(109,111,193,253)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99852"
     Site            order(110..112,188..189,191..192,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99852"
     Region          160..183
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8WTP8"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUW6.1)"
     Region          272..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUW6.1)"
     CDS             1..332
                     /gene="Aen"
                     /gene_synonym="Isg20l1; RGD1305051"
                     /coded_by="NM_001108487.2:357..1355"
                     /db_xref="GeneID:361594"
                     /db_xref="RGD:1305051"
ORIGIN      
        1 mvprevpess ltslktkdva rrrhkrrsrq hqrfmarkal lqeqeslsmv pgpglcplps
       61 ptqtpagtea sgnrkqrtka rsgskglcsk rpvpreapss gpskyvaidc emvgtgpqgr
      121 vselarcsvv sysgdvlydk yirpempivd yrtrwsgitr qhmhkaipfq vaqkeilkll
      181 kgkvvvghal hndfqalkyv hpgsqirdtt yvpnllsqps sltrarvslk dlalnllhkk
      241 iqvghhghss vedamtamel yqlvevqweq qvastakahp edrgpdsstd veqymddqyw
      301 pedlaqstrg dtreaqdrqe geegqgarsa pp
//
LOCUS       NP_001099495             467 aa            linear   ROD 27-APR-2025
DEFINITION  putative protein MSS51 homolog, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001099495 XP_001056023 XP_214130
VERSION     NP_001099495.1
DBSOURCE    REFSEQ: accession NM_001106025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Liu,C.M., Fann,C.S., Chen,C.Y., Liu,Y.L., Oyang,Y.J., Yang,W.C.,
            Chang,C.C., Wen,C.C., Chen,W.J., Hwang,T.J., Hsieh,M.H., Liu,C.C.,
            Faraone,S.V., Tsuang,M.T. and Hwu,H.G.
  TITLE     ANXA7, PPP3CB, DNAJC9, and ZMYND17 genes at chromosome 10q22
            associated with the subgroup of schizophrenia with deficits in
            attention and executive function
  JOURNAL   Biol Psychiatry 70 (1), 51-58 (2011)
   PUBMED   21531385
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474061.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001056023.1, XP_214130.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..467
                     /product="putative protein MSS51 homolog, mitochondrial"
                     /note="zinc finger MYND domain-containing protein 17; zinc
                     finger, MYND domain containing 17; zinc finger, MYND-type
                     containing 17; MSS51 mitochondrial translational activator
                     homolog"
                     /calculated_mol_wt=52152
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZKV9.1)"
     Region          104..148
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Region          242..422
                     /region_name="MSS51_C"
                     /note="MSS51 C-terminal domain; pfam20179"
                     /db_xref="CDD:466330"
     CDS             1..467
                     /gene="Mss51"
                     /gene_synonym="Zmynd17"
                     /coded_by="NM_001106025.1:71..1474"
                     /db_xref="GeneID:289904"
                     /db_xref="RGD:1309408"
ORIGIN      
        1 maprsrrrkh kkpppvtpmp dipptdvsav rpalpepgps idalgfiald sdvpglpqri
       61 lqrlnmksye eyklvidggt pvpsfgfrcq qemfqrmedt frfcayckal phglssckvl
      121 rhckrcrnvy ycdaecqrsd wpahrkvcge lrlvavdrvm ewllvtgdfv lpsgpwpwlp
      181 eeiqnwdtwf smrglqlest lnallgsham tmlwaslgrp rpdpdvlhgs lkrlmtdvls
      241 rpltlglgir tlaidvgktg gstlhvvgas hvetflirsg dydelgymfp enlgfrvimv
      301 gvdvsadllq sssslplepg tvqlsghral yhdfweeqie tgnlahpdlv aafhpgfhas
      361 pglmeawlpt llllrdyeip tlitvysqqe leaslqvlvn ldthiiacga npfaslkpeq
      421 vyskpnkqpv yssayyivfr gcsscqldkq qveeepdefs vvesnpn
//
LOCUS       NP_001029244             281 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.10br [Rattus norvegicus].
ACCESSION   NP_001029244
VERSION     NP_001029244.1
DBSOURCE    REFSEQ: accession NM_001034072.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB787774.1, M34135.1,
            AF372217.1 and BE118215.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.10, also known as variant 5)
            contains a different 3' exon compared to variant 1. The resulting
            protein (isoform Tpm1.10br, also referred to as TMBr-1) is shorter
            and has a distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M34135.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..281
                     /product="tropomyosin alpha-1 chain isoform Tpm1.10br"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32364
     Region          48..280
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..281
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034072.1:107..952"
                     /note="isoform Tpm1.10br is encoded by transcript variant
                     Tpm1.10"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledql yhqleqnrrl tnelklalne d
//
LOCUS       NP_001001507             546 aa            linear   ROD 27-APR-2025
DEFINITION  oncoprotein-induced transcript 3 protein precursor [Rattus
            norvegicus].
ACCESSION   NP_001001507 XP_228352
VERSION     NP_001001507.1
DBSOURCE    REFSEQ: accession NM_001001507.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Yan,B., Zhang,Z.Z., Huang,L.Y., Shen,H.L. and Han,Z.G.
  TITLE     OIT3 deficiency impairs uric acid reabsorption in renal tubule
  JOURNAL   FEBS Lett 586 (6), 760-765 (2012)
   PUBMED   22306318
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Shen,H.L., Xu,Z.G., Huang,L.Y., Liu,D., Lin,D.H., Cao,J.B.,
            Zhang,X., Wang,Z.Q., Wang,W.H., Yang,P.Y. and Han,Z.G.
  TITLE     Liver-specific ZP domain-containing protein (LZP) as a new partner
            of Tamm-Horsfall protein harbors on renal tubules
  JOURNAL   Mol Cell Biochem 321 (1-2), 73-83 (2009)
   PUBMED   18830570
  REMARK    GeneRIF: The finding that LZP might act as a new partner of THP
            would provide novel insights into renal functions related to THP
            and LZP, such as the urothelial permeability barrier and the host
            defense against the adhesion of pathogens.
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Xu,Z.G., Du,J.J., Cui,S.J., Wang,Z.Q., Huo,K.K., Li,Y.Y. and
            Han,Z.G.
  TITLE     Identification of LZP gene from Mus musculus and Rattus norvegicus
            coding for a novel liver-specific ZP domain-containing secretory
            protein
  JOURNAL   DNA Seq 15 (2), 81-87 (2004)
   PUBMED   15346761
  REMARK    GeneRIF: Sequence analysis revealed that human, rat and mouse LZP
            proteins are highly conserved.
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Xu,Z.G., Du,J.J., Zhang,X., Cheng,Z.H., Ma,Z.Z., Xiao,H.S., Yu,L.,
            Wang,Z.Q., Li,Y.Y., Huo,K.K. and Han,Z.G.
  TITLE     A novel liver-specific zona pellucida domain containing protein
            that is expressed rarely in hepatocellular carcinoma
  JOURNAL   Hepatology 38 (3), 735-744 (2003)
   PUBMED   12939600
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY353853.1.
            
            On Aug 30, 2004 this sequence version replaced XP_228352.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY353853.1, AY356356.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..546
                     /product="oncoprotein-induced transcript 3 protein
                     precursor"
                     /note="oncoprotein-induced transcript 3 protein;
                     liver-specific zona pellucida domain-containing protein"
                     /calculated_mol_wt=58461
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V0K7.1)"
                     /calculated_mol_wt=1736
     mat_peptide     17..546
                     /product="Oncoprotein-induced transcript 3 protein.
                     /id=PRO_0000298933"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V0K7.1)"
                     /calculated_mol_wt=58461
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V0K7.1)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V0K7.1)"
     Region          186..221
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          227..262
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          268..514
                     /region_name="Zona_pellucida"
                     /note="Zona pellucida-like domain; pfam00100"
                     /db_xref="CDD:459673"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6V0K7.1)"
     Region          524..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6V0K7.1)"
     CDS             1..546
                     /gene="Oit3"
                     /gene_synonym="Lzp"
                     /coded_by="NM_001001507.1:106..1746"
                     /db_xref="GeneID:294559"
                     /db_xref="RGD:735082"
ORIGIN      
        1 mplslllacl fttvtlqspv vldpcsayis lnepwrntdh qfdesqsqpl cdnhmdgewy
       61 rftgmagdam ptfcipenhc gthapvwlng shplegdgiv qrqacasfkg ncclwnttve
      121 vkacpggyyv yrlakpsvcf hiycghfydi cdedchgscl dttecacspg tslgpdgqtc
      181 fdenecehnn ggcseicvnl knshrcacgv grvlrsdgkt cediegchsn nggcshsclg
      241 sekgyqcecp rglvlsednh tcqvpvlcks saievsvpre lvgglelflt ntscrgvsng
      301 thvniifslk tcgtvvdvvn dkivasnlvt glpkqtpgss gdiiirtskl lipvtcefpr
      361 lytisegyvp nlrnapleir srnhgifpft leifkdhefe epyretlptl klrdslyfgi
      421 eplvhvsgle slvescfatp takvdeilky ylirdgcvsd dsvkqyssrd hlakhfqvpv
      481 fkfvgkdhke vflhcrvlvc gvldersrca qgchrrvrre agededsagl qsqtltggpi
      541 sidwee
//
LOCUS       NP_071974                146 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL23m [Rattus norvegicus].
ACCESSION   NP_071974
VERSION     NP_071974.1
DBSOURCE    REFSEQ: accession NM_022529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U62635.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U62635.1, BC059936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..146
                     /product="large ribosomal subunit protein uL23m"
                     /note="39S ribosomal protein L23, mitochondrial; L23mt;
                     MRP-L23; L23 mitochondrial-related protein; ribosomal
                     protein L23-related product homolog"
                     /calculated_mol_wt=16919
     Region          <42..105
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     Region          108..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63750.1)"
     CDS             1..146
                     /gene="Mrpl23"
                     /gene_synonym="rL23MRP; Rpl23-rs; Rpl23l"
                     /coded_by="NM_022529.1:16..456"
                     /db_xref="GeneID:64360"
                     /db_xref="RGD:68343"
ORIGIN      
        1 marnvlyply qlggpqlrvf rtnffiqlvr pgtaqpedtv qfripmemtr vdlrnyleqi
       61 ynvpvaavrt rvqhgsnrrr dhknvrikkp dykvayvqla hgqtftfpdl fpekeptspd
      121 pleeelpqqr qssdprcpgi pswfgl
//
LOCUS       NP_001106187             919 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor ionotropic, kainate 3 isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001106187
VERSION     NP_001106187.1
DBSOURCE    REFSEQ: accession NM_001112716.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Kumari,J., Vinnakota,R. and Kumar,J.
  TITLE     Structural and Functional Insights into GluK3-kainate Receptor
            Desensitization and Recovery
  JOURNAL   Sci Rep 9 (1), 10254 (2019)
   PUBMED   31311973
  REMARK    GeneRIF: Structural and Functional Insights into GluK3-kainate
            Receptor Desensitization and Recovery.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Fujikawa,T., Petralia,R.S., Fitzgerald,T.S., Wang,Y.X., Millis,B.,
            Morgado-Diaz,J.A., Kitamura,K. and Kachar,B.
  TITLE     Localization of kainate receptors in inner and outer hair cell
            synapses
  JOURNAL   Hear Res 314, 20-32 (2014)
   PUBMED   24858010
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Zhou,W., Zhou,L.Q., Zhang,S.L., Liu,B., Leng,Y.M., Zhou,R.H. and
            Kong,W.J.
  TITLE     The changes in mGluR2 and mGluR7 expression in rat medial
            vestibular nucleus and flocculus following unilateral
            labyrinthectomy
  JOURNAL   Int J Mol Sci 14 (11), 22857-22875 (2013)
   PUBMED   24264036
  REMARK    GeneRIF: Our results suggest that mGluR2 and mGluR7 may contribute
            to the early rebalancing of spontaneous resting activity in the MVN
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Veran,J., Kumar,J., Pinheiro,P.S., Athane,A., Mayer,M.L.,
            Perrais,D. and Mulle,C.
  TITLE     Zinc potentiates GluK3 glutamate receptor function by stabilizing
            the ligand binding domain dimer interface
  JOURNAL   Neuron 76 (3), 565-578 (2012)
   PUBMED   23141068
  REMARK    GeneRIF: Zinc binding stabilizes the labile GluK3 dimer interface,
            slows desensitization and potentiates currents.
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Schiffer,H.H., Swanson,G.T. and Heinemann,S.F.
  TITLE     Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are
            functional kainate receptor subunits with a low sensitivity to
            glutamate
  JOURNAL   Neuron 19 (5), 1141-1146 (1997)
   PUBMED   9390526
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Flor,P.J., Van Der Putten,H., Ruegg,D., Lukic,S., Leonhardt,T.,
            Bence,M., Sansig,G., Knopfel,T. and Kuhn,R.
  TITLE     A novel splice variant of a metabotropic glutamate receptor, human
            mGluR7b
  JOURNAL   Neuropharmacology 36 (2), 153-159 (1997)
   PUBMED   9144652
REFERENCE   8  (residues 1 to 919)
  AUTHORS   Nutt,S.L., Hoo,K.H., Rampersad,V., Deverill,R.M., Elliott,C.E.,
            Fletcher,E.J., Adams,S.L., Korczak,B., Foldes,R.L. and Kamboj,R.K.
  TITLE     Molecular characterization of the human EAA5 (GluR7) receptor: a
            high-affinity kainate receptor with novel potential RNA editing
            sites
  JOURNAL   Recept Channels 2 (4), 315-326 (1994)
   PUBMED   7719709
REFERENCE   9  (residues 1 to 919)
  AUTHORS   Lomeli,H., Wisden,W., Kohler,M., Keinanen,K., Sommer,B. and
            Seeburg,P.H.
  TITLE     High-affinity kainate and domoate receptors in rat brain
  JOURNAL   FEBS Lett 307 (2), 139-143 (1992)
   PUBMED   1322826
REFERENCE   10 (residues 1 to 919)
  AUTHORS   Bettler,B., Egebjerg,J., Sharma,G., Pecht,G., Hermans-Borgmeyer,I.,
            Moll,C., Stevens,C.F. and Heinemann,S.
  TITLE     Cloning of a putative glutamate receptor: a low affinity
            kainate-binding subunit
  JOURNAL   Neuron 8 (2), 257-265 (1992)
   PUBMED   1371217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z11716.1, JAXUCZ010000005.1 and
            M83552.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. Compared to other kainate or AMPA receptors, this subunit
            exhibits a lower sensitivity to glutamate, and thus may play a
            unique role in neurotransmission in the brain. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1, also known as GluR7a) encodes
            the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z11716.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..919
                     /product="glutamate receptor ionotropic, kainate 3 isoform
                     1 precursor"
                     /note="glutamate receptor subunit kainate subtype;
                     glutamate receptor 7; glutamate receptor, ionotropic,
                     kainate 3"
                     /calculated_mol_wt=100328
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3771
     mat_peptide     32..919
                     /product="Glutamate receptor ionotropic, kainate 3.
                     /id=PRO_0000011548"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
                     /calculated_mol_wt=100328
     Region          37..417
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            order(90..92,96,127,179,182,186,189,192..193,203..206)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142,
                     ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Region          433..801
                     /region_name="PBP2_iGluR_Kainate_GluR7"
                     /note="GluR7 subtype of kainate receptor, type 2
                     periplasmic-binding fold superfamily; cd13723"
                     /db_xref="CDD:270441"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            order(491,518..520,525)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270441"
     Site            order(521..523,526..527,531..534,537,695,761..762,
                     776..777,780..782,784..785,787..790)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270441"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     Site            637..657
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     Site            752
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            821..841
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13002; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     CDS             1..919
                     /gene="Grik3"
                     /gene_synonym="GluK3; gluR-7; GluR7"
                     /coded_by="NM_001112716.1:132..2891"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:298521"
                     /db_xref="RGD:71027"
ORIGIN      
        1 mtapwrrlrs lvweywagfl vcafwipdsr gmphvirigg ifeyadgpna qvmnaeehaf
       61 rfsaniinrn rtllpnttlt ydiqrihfhd sfeatkkacd qlalgvvaif gpsqgsctna
      121 vqsicnalev phiqlrwkhh pldnkdtfyv nlypdyasls haildlvqsl kwrsatvvyd
      181 dstglirlqe limapsryni rlkirqlpid sddsrpllke mkrgrefrii fdcshtmaaq
      241 ilkqamamgm mteyyhfift tldlyaldle pyrysgvnlt gfrilnvdnp hvsaivekws
      301 merlqaapra esglldgvmm tdaallydav hivsvcyqra pqmtvnslqc hrhkawrfgg
      361 rfmnfikeaq wegltgrivf nktsglrtdf dldiislked glekvgvwsp adglniteva
      421 kgrgpnvtds ltnrslivtt lleepfvmfr ksdrtlygnd rfegycidll kelahilgfs
      481 yeirlvedgk ygaqddkgqw ngmvkelidh kadlavaplt ithvrekaid fskpfmtlgv
      541 silyrkpngt npsvfsflnp lspdiwmyvl laylgvscvl fviarfspye wydahpcnpg
      601 sevvennftl lnsfwfgmgs lmqqgselmp kalstriigg iwwfftliii ssytanlaaf
      661 ltvermespi dsaddlakqt kieygavkdg atmtffkksk istfekmwaf msskpsalvk
      721 nneegiqrtl tadyallmes ttieyitqrn cnltqiggli dskgygigtp mgspyrdkit
      781 iailqlqeed klhimkekww rgsgcpeeen keasalgiqk iggifivlaa glvlsvlvav
      841 gefiyklrkt aereqrsfcs tvadeirfsl tcqrrlkhkp qppmmvktda vinmhtfndr
      901 rlpgkdsmsc stslapvfp
//
LOCUS       NP_036915                272 aa            linear   ROD 27-APR-2025
DEFINITION  basigin isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_036915 XP_579350
VERSION     NP_036915.1
DBSOURCE    REFSEQ: accession NM_012783.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Zhu,X., Tang,Z., Li,W., Li,X., Iwakiri,Y. and Liu,F.
  TITLE     S-nitrosylation of EMMPRIN influences the migration of HSCs and MMP
            activity in liver fibrosis
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1640-1649 (2023)
   PUBMED   37700592
  REMARK    GeneRIF: S-nitrosylation of EMMPRIN influences the migration of
            HSCs and MMP activity in liver fibrosis.
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Chen,Y., Luan,J., Jiang,T., Cai,D., Sun,C., Wang,X., Zhao,X. and
            Gou,X.
  TITLE     Knockdown of EMMPRIN (OX47) in MRMT-1 Carcinoma Cells Inhibits
            Tumor Growth and Decreases Cancer-Induced Bone Destruction and Pain
  JOURNAL   Cancer Res Treat 53 (2), 576-583 (2021)
   PUBMED   33138345
  REMARK    GeneRIF: Knockdown of EMMPRIN (OX47) in MRMT-1 Carcinoma Cells
            Inhibits Tumor Growth and Decreases Cancer-Induced Bone Destruction
            and Pain.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Wang,Q., Xu,B., Fan,K., Wu,J. and Wang,T.
  TITLE     Inflammation suppression by dexamethasone via inhibition of
            CD147-mediated NF-kappaB pathway in collagen-induced arthritis rats
  JOURNAL   Mol Cell Biochem 473 (1-2), 63-76 (2020)
   PUBMED   32594339
  REMARK    GeneRIF: Inflammation suppression by dexamethasone via inhibition
            of CD147-mediated NF-kappaB pathway in collagen-induced arthritis
            rats.
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Wang,Q., Xu,B., Fan,K., Wu,J. and Wang,T.
  TITLE     CypB-CD147 Signaling Is Involved in Crosstalk between Cartilage and
            FLS in Collagen-Induced Arthritis
  JOURNAL   Mediators Inflamm 2020, 6473858 (2020)
   PUBMED   32908452
  REMARK    GeneRIF: CypB-CD147 Signaling Is Involved in Crosstalk between
            Cartilage and FLS in Collagen-Induced Arthritis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Forero-Quintero,L.S., Ames,S., Schneider,H.P., Thyssen,A.,
            Boone,C.D., Andring,J.T., McKenna,R., Casey,J.R., Deitmer,J.W. and
            Becker,H.M.
  TITLE     Membrane-anchored carbonic anhydrase IV interacts with
            monocarboxylate transporters via their chaperones CD147 and GP70
  JOURNAL   J Biol Chem 294 (2), 593-607 (2019)
   PUBMED   30446621
  REMARK    GeneRIF: This study analyzed the direct interaction between CAIV
            and the two Monocarboxylate transporters (MCTs) chaperones basigin
            (CD147) and embigin (GP70). In rat CD147, binding of CAIV was
            mediated by by the positively charged Lys-73.
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Kuno,N., Kadomatsu,K., Fan,Q.W., Hagihara,M., Senda,T., Mizutani,S.
            and Muramatsu,T.
  TITLE     Female sterility in mice lacking the basigin gene, which encodes a
            transmembrane glycoprotein belonging to the immunoglobulin
            superfamily
  JOURNAL   FEBS Lett 425 (2), 191-194 (1998)
   PUBMED   9559645
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Naruhashi,K., Kadomatsu,K., Igakura,T., Fan,Q.W., Kuno,N.,
            Muramatsu,H., Miyauchi,T., Hasegawa,T., Itoh,A., Muramatsu,T. and
            Nabeshima,T.
  TITLE     Abnormalities of sensory and memory functions in mice lacking Bsg
            gene
  JOURNAL   Biochem Biophys Res Commun 236 (3), 733-737 (1997)
   PUBMED   9245724
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Polette,M., Gilles,C., Marchand,V., Lorenzato,M., Toole,B.,
            Tournier,J.M., Zucker,S. and Birembaut,P.
  TITLE     Tumor collagenase stimulatory factor (TCSF) expression and
            localization in human lung and breast cancers
  JOURNAL   J Histochem Cytochem 45 (5), 703-709 (1997)
   PUBMED   9154157
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Nehme,C.L., Cesario,M.M., Myles,D.G., Koppel,D.E. and Bartles,J.R.
  TITLE     Breaching the diffusion barrier that compartmentalizes the
            transmembrane glycoprotein CE9 to the posterior-tail plasma
            membrane domain of the rat spermatozoon
  JOURNAL   J Cell Biol 120 (3), 687-694 (1993)
   PUBMED   8425897
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Fossum,S., Mallett,S. and Barclay,A.N.
  TITLE     The MRC OX-47 antigen is a member of the immunoglobulin superfamily
            with an unusual transmembrane sequence
  JOURNAL   Eur J Immunol 21 (3), 671-679 (1991)
   PUBMED   2009910
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV119278.1, BC059145.1 and BQ199464.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579350.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The resulting
            isoform (2) has a shorter N-terminus when compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ227451.1, FQ212838.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..272
                     /product="basigin isoform 2 precursor"
                     /note="OX-47 antigen; glycoprotein CE9; neurothelin;
                     basigin (Ok blood group); Basigin (Ox47 antigen or CE-9)
                     (EMMPRIN in human) (neurothelin HT7 or 5A11 in avian);
                     Basignin (Ox47 antigen or CE-9) (EMMPRIN in human)
                     (neurothelin HT7 or 5A11 in avian)"
                     /calculated_mol_wt=27563
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2040
     Region          112..205
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          137..141
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          154..174
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          185..190
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          198..201
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..272
                     /gene="Bsg"
                     /gene_synonym="5A11; basignin; CE9; EMMPRIN; HT7; Ox47R"
                     /coded_by="NM_012783.3:92..910"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:25246"
                     /db_xref="RGD:2220"
ORIGIN      
        1 maaalllala ftflsgqgac aaagtivtsv qevdsktqlt cflnssgidi vghrwmrggk
       61 vlqedtlpdl qmkytvdadd rsgeyscifl pepvgrgnin vegpprikvg kksehasege
      121 fvklicksea shppvdewvw fktsdtgdqt isngteansk yviistpels eliisdldmn
      181 vdpgtyvcna tnsqgsaret islrvrsrla alwpflgiva evlvlvtiif iyekrrkpdq
      241 tldeddpgaa plkgsgshln dkdknvrqrn at
//
LOCUS       NP_001012480             776 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase SUPV3L1, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_001012480 XP_215393
VERSION     NP_001012480.1
DBSOURCE    REFSEQ: accession NM_001012462.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Pietras,Z., Wojcik,M.A., Borowski,L.S., Szewczyk,M., Kulinski,T.M.,
            Cysewski,D., Stepien,P.P., Dziembowski,A. and Szczesny,R.J.
  TITLE     Dedicated surveillance mechanism controls G-quadruplex forming
            non-coding RNAs in human mitochondria
  JOURNAL   Nat Commun 9 (1), 2558 (2018)
   PUBMED   29967381
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Szczesny,R.J., Borowski,L.S., Brzezniak,L.K., Dmochowska,A.,
            Gewartowski,K., Bartnik,E. and Stepien,P.P.
  TITLE     Human mitochondrial RNA turnover caught in flagranti: involvement
            of hSuv3p helicase in RNA surveillance
  JOURNAL   Nucleic Acids Res 38 (1), 279-298 (2010)
   PUBMED   19864255
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Wang,D.D., Shu,Z., Lieser,S.A., Chen,P.L. and Lee,W.H.
  TITLE     Human mitochondrial SUV3 and polynucleotide phosphorylase form a
            330-kDa heteropentamer to cooperatively degrade double-stranded RNA
            with a 3'-to-5' directionality
  JOURNAL   J Biol Chem 284 (31), 20812-20821 (2009)
   PUBMED   19509288
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Khidr,L., Wu,G., Davila,A., Procaccio,V., Wallace,D. and Lee,W.H.
  TITLE     Role of SUV3 helicase in maintaining mitochondrial homeostasis in
            human cells
  JOURNAL   J Biol Chem 283 (40), 27064-27073 (2008)
   PUBMED   18678873
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Bogenhagen,D.F., Rousseau,D. and Burke,S.
  TITLE     The layered structure of human mitochondrial DNA nucleoids
  JOURNAL   J Biol Chem 283 (6), 3665-3675 (2008)
   PUBMED   18063578
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Pereira,M., Mason,P., Szczesny,R.J., Maddukuri,L., Dziwura,S.,
            Jedrzejczak,R., Paul,E., Wojcik,A., Dybczynska,L., Tudek,B.,
            Bartnik,E., Klysik,J., Bohr,V.A. and Stepien,P.P.
  TITLE     Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss
            of the SUV3 gene results in mouse embryonic lethality
  JOURNAL   Mech Ageing Dev 128 (11-12), 609-617 (2007)
   PUBMED   17961633
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Szczesny,R.J., Obriot,H., Paczkowska,A., Jedrzejczak,R.,
            Dmochowska,A., Bartnik,E., Formstecher,P., Polakowska,R. and
            Stepien,P.P.
  TITLE     Down-regulation of human RNA/DNA helicase SUV3 induces apoptosis by
            a caspase- and AIF-dependent pathway
  JOURNAL   Biol Cell 99 (6), 323-332 (2007)
   PUBMED   17352692
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Minczuk,M., Piwowarski,J., Papworth,M.A., Awiszus,K.,
            Schalinski,S., Dziembowski,A., Dmochowska,A., Bartnik,E.,
            Tokatlidis,K., Stepien,P.P. and Borowski,P.
  TITLE     Localisation of the human hSuv3p helicase in the mitochondrial
            matrix and its preferential unwinding of dsDNA
  JOURNAL   Nucleic Acids Res 30 (23), 5074-5086 (2002)
   PUBMED   12466530
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089883.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215393.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089883.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..776
                     /product="ATP-dependent RNA helicase SUPV3L1,
                     mitochondrial precursor"
                     /EC_number="3.6.4.13"
                     /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial;
                     SUV3-like helicase; SUV3-like protein 1; suppressor of
                     var1 3-like protein 1"
                     /calculated_mol_wt=82717
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5EBA1.1)"
                     /calculated_mol_wt=4007
     mat_peptide     41..776
                     /product="ATP-dependent RNA helicase SUPV3L1,
                     mitochondrial. /id=PRO_0000310547"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA1.1)"
                     /calculated_mol_wt=82717
     Region          62..179
                     /region_name="Suv3_N"
                     /note="Suv3 helical N-terminal domain; pfam18114"
                     /db_xref="CDD:436283"
     Site            99
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8IYB8; propagated from
                     UniProtKB/Swiss-Prot (Q5EBA1.1)"
     Region          200..345
                     /region_name="DEXQc_Suv3"
                     /note="DEXQ-box helicase domain of Suv3; cd17913"
                     /db_xref="CDD:350671"
     Site            order(209..215,291)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350671"
     Region          349..487
                     /region_name="SF2_C_suv3"
                     /note="C-terminal helicase domain of ATP-dependent RNA
                     helicase; cd18805"
                     /db_xref="CDD:350192"
     Site            order(429,432,466,470,473..474)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350192"
     Region          558..598
                     /region_name="Suv3_C_1"
                     /note="Suv3 C-terminal domain 1; pfam18147"
                     /db_xref="CDD:436308"
     Region          626..672
                     /region_name="SUV3_C"
                     /note="Mitochondrial degradasome RNA helicase subunit C
                     terminal; pfam12513"
                     /db_xref="CDD:463616"
     Region          650..776
                     /region_name="Interaction with LAMTOR5, important for
                     protein stability. /evidence=ECO:0000250|UniProtKB:Q8IYB8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA1.1)"
     Region          689..733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA1.1)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IYB8; propagated from
                     UniProtKB/Swiss-Prot (Q5EBA1.1)"
     Region          751..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA1.1)"
     CDS             1..776
                     /gene="Supv3l1"
                     /coded_by="NM_001012462.1:16..2346"
                     /db_xref="GeneID:294385"
                     /db_xref="RGD:1305565"
ORIGIN      
        1 mslprcallw arlpagrgag praapcsalr alvgsfpgas grvpclaass sasggskapn
       61 tslfvpltvk pqgpsadgdv gaeltrpldk nevkkildkf ykrqeiqkls adygldarlf
      121 hqafisfrny imqshsldvd ihivlndicf saahvddlfp fflrhakqif pvleckddlr
      181 qisdlrrppn wypearaiqr kiifhsgptn sgktyhaiqr ylsatsgvyc gplkllahei
      241 feksnaagvp cdlvtgeerl tvepegkqat hvsctvemcn vatpyevavi deiqmirdpa
      301 rgwawtrall glcaeevhlc gesaaidlvt ellyttgeev evqkyerltp isvldrales
      361 ldnlrpgdci vcfskndiys vsrqieirgl esaviygslp pgtklaqark fndpndpcki
      421 lvatdaigmg lnlsirriif yslikpsine kgekelepit tsqalqiagr agrfsshfke
      481 gevttmhrdd lallkeilnr pvdpiqaagl hptaeqiemf ayhlpettls nlidifvdfa
      541 qvdgqyfvcn mddfkfsael iqhiplslrv ryvfctapin kkqpfvcssl lqfarqysrn
      601 epltfawlrr yikwpllppk nikdlmdlea vhdvfdlylw lsyrfidmfp dssfvrslqk
      661 eldviiqegv hnitklikis eshkllnlep sgsqsrlpga sksparrtrg tktgnkaaep
      721 pspsdkelpl asrlvqqgll tadmlkqlqk ewltqrpeqg kekvgtrrkk kdpnsd
//
LOCUS       NP_112404                412 aa            linear   ROD 27-APR-2025
DEFINITION  double C2-like domain-containing protein beta [Rattus norvegicus].
ACCESSION   NP_112404
VERSION     NP_112404.1
DBSOURCE    REFSEQ: accession NM_031142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Brouwer,I., Giniatullina,A., Laurens,N., van Weering,J.R.T.,
            Bald,D., Wuite,G.J.L. and Groffen,A.J.
  TITLE     Direct quantitative detection of Doc2b-induced hemifusion in
            optically trapped membranes
  JOURNAL   Nat Commun 6, 8387 (2015)
   PUBMED   26395669
  REMARK    GeneRIF: acts directly on membranes and stabilizes hemifusion
            intermediate in cell-free system
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Xue,R., Gaffaney,J.D. and Chapman,E.R.
  TITLE     Structural elements that underlie Doc2beta function during
            asynchronous synaptic transmission
  JOURNAL   Proc Natl Acad Sci U S A 112 (31), E4316-E4325 (2015)
   PUBMED   26195798
  REMARK    GeneRIF: these data reveal the key determinants of Doc2beta that
            underlie its function during the slow phase of synaptic
            transmission.
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Gaffaney,J.D., Xue,R. and Chapman,E.R.
  TITLE     Mutations that disrupt Ca(2)-binding activity endow Doc2beta with
            novel functional properties during synaptic transmission
  JOURNAL   Mol Biol Cell 25 (4), 481-494 (2014)
   PUBMED   24356452
  REMARK    GeneRIF: Mutations that disrupt Ca(2)-binding activity endow
            Doc2beta with novel functional properties during synaptic
            transmission.
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Yu,H., Rathore,S.S., Davis,E.M., Ouyang,Y. and Shen,J.
  TITLE     Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated
            fusion reaction in a calcium- and membrane bending-dependent manner
  JOURNAL   Mol Biol Cell 24 (8), 1176-1184 (2013)
   PUBMED   23427263
  REMARK    GeneRIF: Doc2b exocytotic functions appear to be distinct from how
            synaptotagmin-1 promotes synaptic neurotransmitter release.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Yao,J., Gaffaney,J.D., Kwon,S.E. and Chapman,E.R.
  TITLE     Doc2 is a Ca2+ sensor required for asynchronous neurotransmitter
            release
  JOURNAL   Cell 147 (3), 666-677 (2011)
   PUBMED   22036572
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Ke,B., Oh,E. and Thurmond,D.C.
  TITLE     Doc2beta is a novel Munc18c-interacting partner and positive
            effector of syntaxin 4-mediated exocytosis
  JOURNAL   J Biol Chem 282 (30), 21786-21797 (2007)
   PUBMED   17548353
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Korteweg,N., Denekamp,F.A., Verhage,M. and Burbach,J.P.
  TITLE     Different spatiotemporal expression of DOC2 genes in the developing
            rat brain argues for an additional, nonsynaptic role of DOC2B in
            early development
  JOURNAL   Eur J Neurosci 12 (1), 165-171 (2000)
   PUBMED   10651871
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Nagano,F., Orita,S., Sasaki,T., Naito,A., Sakaguchi,G., Maeda,M.,
            Watanabe,T., Kominami,E., Uchiyama,Y. and Takai,Y.
  TITLE     Interaction of Doc2 with tctex-1, a light chain of cytoplasmic
            dynein. Implication in dynein-dependent vesicle transport
  JOURNAL   J Biol Chem 273 (46), 30065-30068 (1998)
   PUBMED   9804756
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Verhage,M., de Vries,K.J., Roshol,H., Burbach,J.P., Gispen,W.H. and
            Sudhof,T.C.
  TITLE     DOC2 proteins in rat brain: complementary distribution and proposed
            function as vesicular adapter proteins in early stages of secretion
  JOURNAL   Neuron 18 (3), 453-461 (1997)
   PUBMED   9115738
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Kojima,T., Fukuda,M., Aruga,J. and Mikoshiba,K.
  TITLE     Calcium-dependent phospholipid binding to the C2A domain of a
            ubiquitous form of double C2 protein (Doc2 beta)
  JOURNAL   J Biochem 120 (3), 671-676 (1996)
   PUBMED   8902635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U70778.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U70778.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..412
                     /product="double C2-like domain-containing protein beta"
                     /function="probably functions in vesicular trafficking"
                     /note="doc2-beta; double C2, beta; double C2-like domains,
                     beta"
                     /calculated_mol_wt=45710
     Region          1..90
                     /region_name="Mediates interaction with DYNLT1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P70610.2)"
     Region          1..36
                     /region_name="Negatively regulates targeting to plasma
                     membrane. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P70610.2)"
     Region          21..>86
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          38..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70610.2)"
     Region          127..250
                     /region_name="C2A_Rabphilin_Doc2"
                     /note="C2 domain first repeat present in Rabphilin and
                     Double C2 domain; cd04035"
                     /db_xref="CDD:176000"
     Site            order(157,163,218,220,226)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176000"
     Region          257..375
                     /region_name="Mediates interaction with STXBP3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P70610.2)"
     Region          269..401
                     /region_name="C2B_Rabphilin_Doc2"
                     /note="C2 domain second repeat present in Rabphilin and
                     Double C2 domain; cd08384"
                     /db_xref="CDD:176030"
     Site            order(297,303,357,359,365)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176030"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70610.2)"
     CDS             1..412
                     /gene="Doc2b"
                     /coded_by="NM_031142.1:156..1394"
                     /db_xref="GeneID:81820"
                     /db_xref="RGD:620519"
ORIGIN      
        1 mtlrrrgeka tisiqehmai dvcpgpirpi kqisdyfprf prglpptaap rasappdapa
       61 rspaatagpr spsdgarddd edvdqlfgay gaspgpspgp spvrppakpp edepdadgye
      121 sddctalgtl dfsllydqen nalhctiska kglkpmdhng ladpyvklhl lpgaskankl
      181 rtktlrntln pswnetltyy gitdedmirk tlrisvcded kfrhnefige trvplkklkp
      241 nhtktfsicl ekqlpvdkae dksleergri lislkyssqk qgllvgivrc ahlaamdang
      301 ysdpyvktyl kpdvdkkskh ktavkkktln pefneefcye ikhgdlakkt levtvwdydi
      361 gksndfiggv vlginakger lkhwfdclkn kdkrierwht ltneipgavl sd
//
LOCUS       NP_543173                228 aa            linear   ROD 27-APR-2025
DEFINITION  vesicle transport protein SEC20 [Rattus norvegicus].
ACCESSION   NP_543173
VERSION     NP_543173.1
DBSOURCE    REFSEQ: accession NM_080897.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wang,P., Wu,Y., Li,Y., Zheng,J. and Tang,J.
  TITLE     A novel RING finger E3 ligase RNF186 regulate ER stress-mediated
            apoptosis through interaction with BNip1
  JOURNAL   Cell Signal 25 (11), 2320-2333 (2013)
   PUBMED   23896122
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Cho,B., Choi,S.Y., Park,O.H., Sun,W. and Geum,D.
  TITLE     Differential expression of BNIP family members of BH3-only proteins
            during the development and after axotomy in the rat
  JOURNAL   Mol Cells 33 (6), 605-610 (2012)
   PUBMED   22639046
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Tang,F., Wang,B., Li,N., Wu,Y., Jia,J., Suo,T., Chen,Q., Liu,Y.J.
            and Tang,J.
  TITLE     RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates
            autophagy through interaction with BNIP1
  JOURNAL   PLoS One 6 (9), e24367 (2011)
   PUBMED   21931693
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Lomonosova,E. and Chinnadurai,G.
  TITLE     BH3-only proteins in apoptosis and beyond: an overview
  JOURNAL   Oncogene 27 Suppl 1 (Suppl 1), S2-S19 (2008)
   PUBMED   19641503
  REMARK    Review article
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Verrier,S.E., Willmann,M., Wenzel,D., Winter,U., von Mollard,G.F.
            and Soling,H.D.
  TITLE     Members of a mammalian SNARE complex interact in the endoplasmic
            reticulum in vivo and are found in COPI vesicles
  JOURNAL   Eur J Cell Biol 87 (11), 863-878 (2008)
   PUBMED   18834646
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Chung,I.H., Lee,S.H., Lee,K.W., Park,S.H., Cha,K.Y., Kim,N.S.,
            Yoo,H.S., Kim,Y.S. and Lee,S.
  TITLE     Gene expression analysis of cultured amniotic fluid cell with Down
            syndrome by DNA microarray
  JOURNAL   J Korean Med Sci 20 (1), 82-87 (2005)
   PUBMED   15716609
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Nakajima,K., Hirose,H., Taniguchi,M., Kurashina,H., Arasaki,K.,
            Nagahama,M., Tani,K., Yamamoto,A. and Tagaya,M.
  TITLE     Involvement of BNIP1 in apoptosis and endoplasmic reticulum
            membrane fusion
  JOURNAL   EMBO J 23 (16), 3216-3226 (2004)
   PUBMED   15272311
REFERENCE   8  (residues 1 to 228)
  AUTHORS   Heon,S., Bernier,M., Servant,N., Dostanic,S., Wang,C., Kirby,G.M.,
            Alpert,L. and Chalifour,L.E.
  TITLE     Dexrazoxane does not protect against doxorubicin-induced damage in
            young rats
  JOURNAL   Am J Physiol Heart Circ Physiol 285 (2), H499-H506 (2003)
   PUBMED   12714334
REFERENCE   9  (residues 1 to 228)
  AUTHORS   Boyd,J.M., Malstrom,S., Subramanian,T., Venkatesh,L.K.,
            Schaeper,U., Elangovan,B., D'Sa-Eipper,C. and Chinnadurai,G.
  TITLE     Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set
            of cellular proteins
  JOURNAL   Cell 79 (2), 341-351 (1994)
   PUBMED   7954800
  REMARK    Erratum:[Cell. 1994 Dec 16;79(6):1121. PMID: 8001138]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF454391.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF454391.1, FQ218385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..228
                     /product="vesicle transport protein SEC20"
                     /note="BCL2/adenovirus E1B 19kDa-interacting protein 1;
                     BCL2/adenovirus E1B interacting protein 1-like 1"
                     /calculated_mol_wt=26039
     Region          132..224
                     /region_name="SNARE_SEC20"
                     /note="SNARE motif of SEC20; cd15865"
                     /db_xref="CDD:277218"
     Site            order(137..139,141..146,148..149,152..153,155..160,
                     162..163,165..167,169..174,176..177,179..181,183..184,
                     186..188,190..191,193)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277218"
     Site            166
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277218"
     Site            200..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHI8.1)"
     CDS             1..228
                     /gene="Bnip1"
                     /gene_synonym="Bnip1l1"
                     /coded_by="NM_080897.1:12..698"
                     /db_xref="GeneID:140932"
                     /db_xref="RGD:620799"
ORIGIN      
        1 maapqdvhvr icnqeivkfd levkaliqdi rdcsgplsel telntkvkek fqqlkhriqe
       61 leqsakeqdk esekqlllqe venhkkqmls nqtswrkanl tcklaidnle kaellqggds
      121 lrqrkttkes laqtsstite slmgisrmms qqvqqseeam qtlvsssrtl ldaneefksm
      181 sgtiqlgrkl itkynrrelt dklliflala lflatvlyiv kkrlfpfl
//
LOCUS       NP_001020584             425 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 184A [Rattus norvegicus].
ACCESSION   NP_001020584 XP_221955
VERSION     NP_001020584.1
DBSOURCE    REFSEQ: accession NM_001025413.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Pugh,R.J., Slee,J.B., Farwell,S.L., Li,Y., Barthol,T., Patton,W.A.
            and Lowe-Krentz,L.J.
  TITLE     Transmembrane Protein 184A Is a Receptor Required for Vascular
            Smooth Muscle Cell Responses to Heparin
  JOURNAL   J Biol Chem 291 (10), 5326-5341 (2016)
   PUBMED   26769966
  REMARK    GeneRIF: TMEM184A is a heparin receptor in vascular cells.
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Best,D. and Adams,I.R.
  TITLE     Sdmg1 is a component of secretory granules in mouse secretory
            exocrine tissues
  JOURNAL   Dev Dyn 238 (1), 223-231 (2009)
   PUBMED   19097053
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Best,D., Sahlender,D.A., Walther,N., Peden,A.A. and Adams,I.R.
  TITLE     Sdmg1 is a conserved transmembrane protein associated with germ
            cell sex determination and germline-soma interactions in mice
  JOURNAL   Development 135 (8), 1415-1425 (2008)
   PUBMED   18321981
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098056.1.
            
            On Jul 15, 2005 this sequence version replaced XP_221955.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098056.1, BC083910.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..425
                     /product="transmembrane protein 184A"
                     /calculated_mol_wt=46748
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Region          58..332
                     /region_name="Solute_trans_a"
                     /note="Organic solute transporter Ostalpha; pfam03619"
                     /db_xref="CDD:460991"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     Region          375..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS1.1)"
     CDS             1..425
                     /gene="Tmem184a"
                     /gene_synonym="RGD1306702"
                     /coded_by="NM_001025413.1:7..1284"
                     /db_xref="GeneID:304325"
                     /db_xref="RGD:1306702"
ORIGIN      
        1 mrnasgflkt agaplvsatw lppspppamp mvaagpqmer vdngsqgapq lfltsalarg
       61 vsgvfvwtal lltghqiysh lrsytvpreq rfvirllfiv piyafdswls llllgghpyy
      121 vyfdsvrdcy eafviysflt lcfqylgges aimaeirgkp irsscfygtc clrgmsysit
      181 flrfckqatl qfcivkpvma litiilqafd kyhdgdfnih sgylyvtlvy nasvslalya
      241 lflfyfatrd llrpfepvlk fltikaiifl sfwqgmllai lercgvipev qavdgtrvga
      301 gtlaagyqnf liciemlfas lalryafpsq vysekknspa ppapmqsiss glketispqd
      361 ivqdaihnfs payqqytqqs theapgpgqg ghpspsthpg pasgsgggkk srniekrmli
      421 psedl
//
LOCUS       NP_001100666             656 aa            linear   ROD 27-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-6 alpha [Rattus
            norvegicus].
ACCESSION   NP_001100666 XP_001076843 XP_222871
VERSION     NP_001100666.1
DBSOURCE    REFSEQ: accession NM_001107196.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Liang,T., Xu,S., Liu,R. and Xia,X.
  TITLE     Activating transcription factor 6 alleviates secondary brain injury
            by increasing cystathionine gamma-lyase expression in a rat model
            of intracerebral hemorrhage
  JOURNAL   Aging (Albany NY) 16 (8), 6990-7008 (2024)
   PUBMED   38613810
  REMARK    GeneRIF: Activating transcription factor 6 alleviates secondary
            brain injury by increasing cystathionine gamma-lyase expression in
            a rat model of intracerebral hemorrhage.
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Ishteyaque,S., Yadav,K.S., Verma,S., Washimkar,K.R. and Mugale,M.N.
  TITLE     CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit apoptosis
            and promotes progression of hepatocellular carcinoma
  JOURNAL   Arch Biochem Biophys 745, 109701 (2023)
   PUBMED   37499993
  REMARK    GeneRIF: CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit
            apoptosis and promotes progression of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Zhang,Q., Liu,G., Liu,R., Liu,J., Zeng,X., Ren,D., Yan,X. and
            Yuan,X.
  TITLE     Dual role of endoplasmic reticulum stress-ATF-6 activation in
            autophagy and apoptosis induced by cyclic stretch in myoblast
  JOURNAL   Apoptosis 28 (5-6), 796-809 (2023)
   PUBMED   36881290
  REMARK    GeneRIF: Dual role of endoplasmic reticulum stress-ATF-6 activation
            in autophagy and apoptosis induced by cyclic stretch in myoblast.
            Erratum:[Apoptosis. 2023 Oct;28(9-10):1501. doi:
            10.1007/s10495-023-01864-y. PMID: 37439923]
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Wang,S., Duan,J., Liao,J., Wang,Y., Xiao,X., Li,L., Liu,Y., Gu,H.,
            Yang,P., Fu,D., Du,J., Li,X. and Shao,M.
  TITLE     LncRNA H19 inhibits ER stress induced apoptosis and improves
            diabetic cardiomyopathy by regulating PI3K/AKT/mTOR axis
  JOURNAL   Aging (Albany NY) 14 (16), 6809-6828 (2022)
   PUBMED   36044268
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Xia,H., Zhao,H., Yang,W., Luo,X., Wei,J. and Xia,H.
  TITLE     MiR-195-5p represses inflammation, apoptosis, oxidative stress, and
            endoplasmic reticulum stress in sepsis-induced myocardial injury by
            targeting activating transcription factor 6
  JOURNAL   Cell Biol Int 46 (2), 243-254 (2022)
   PUBMED   34816499
  REMARK    GeneRIF: MiR-195-5p represses inflammation, apoptosis, oxidative
            stress, and endoplasmic reticulum stress in sepsis-induced
            myocardial injury by targeting activating transcription factor 6.
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Yoshida,H., Matsui,T., Yamamoto,A., Okada,T. and Mori,K.
  TITLE     XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER
            stress to produce a highly active transcription factor
  JOURNAL   Cell 107 (7), 881-891 (2001)
   PUBMED   11779464
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Haze,K., Okada,T., Yoshida,H., Yanagi,H., Yura,T., Negishi,M. and
            Mori,K.
  TITLE     Identification of the G13 (cAMP-response-element-binding
            protein-related protein) gene product related to activating
            transcription factor 6 as a transcriptional activator of the
            mammalian unfolded protein response
  JOURNAL   Biochem J 355 (Pt 1), 19-28 (2001)
   PUBMED   11256944
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Ye,J., Rawson,R.B., Komuro,R., Chen,X., Dave,U.P., Prywes,R.,
            Brown,M.S. and Goldstein,J.L.
  TITLE     ER stress induces cleavage of membrane-bound ATF6 by the same
            proteases that process SREBPs
  JOURNAL   Mol Cell 6 (6), 1355-1364 (2000)
   PUBMED   11163209
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Haze,K., Yoshida,H., Yanagi,H., Yura,T. and Mori,K.
  TITLE     Mammalian transcription factor ATF6 is synthesized as a
            transmembrane protein and activated by proteolysis in response to
            endoplasmic reticulum stress
  JOURNAL   Mol Biol Cell 10 (11), 3787-3799 (1999)
   PUBMED   10564271
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Yoshida,H., Haze,K., Yanagi,H., Yura,T. and Mori,K.
  TITLE     Identification of the cis-acting endoplasmic reticulum stress
            response element responsible for transcriptional induction of
            mammalian glucose-regulated proteins. Involvement of basic leucine
            zipper transcription factors
  JOURNAL   J Biol Chem 273 (50), 33741-33749 (1998)
   PUBMED   9837962
  REMARK    Erratum:[J Biol Chem 1999 Jan 22;274(4):2592]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473958.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_222871.4, XP_001076843.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168890.1, SRR8487227.299522.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..656
                     /product="cyclic AMP-dependent transcription factor ATF-6
                     alpha"
                     /note="ATF6-alpha; activating transcription factor 6
                     alpha; cAMP-dependent transcription factor ATF-6 alpha"
                     /calculated_mol_wt=72535
     Region          1..137
                     /region_name="Transcription activation.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Region          81..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Region          295..326
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Region          296..347
                     /region_name="bZIP_ATF6"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-6 (ATF-6) and similar proteins: a
                     DNA-binding and dimerization domain; cd14700"
                     /db_xref="CDD:269848"
     Region          296..347
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269848"
     Site            order(299..300,302..304,306..311,313..315)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269848"
     Site            order(314,317..318,321..322,324..325,328..329,331..332,
                     335..336,338..339,342..343,345..346)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269848"
     Region          335..342
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Site            378..398
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Site            406..407
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS1.
                     /evidence=ECO:0000250|UniProtKB:P18850; propagated from
                     UniProtKB/Swiss-Prot (G3V909.1)"
     Region          455..575
                     /region_name="Interaction with THBS4.
                     /evidence=ECO:0000250|UniProtKB:P18850"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V909.1)"
     Site            570
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V909.1)"
     Site            629
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V909.1)"
     Region          632..656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V909.1)"
     CDS             1..656
                     /gene="Atf6"
                     /coded_by="NM_001107196.1:71..2041"
                     /db_xref="GeneID:304962"
                     /db_xref="RGD:1305471"
ORIGIN      
        1 mespfspvlp hgpgedwest lfaelgyftd tddvqfdaah etyennfdhl nfdldlmpwe
       61 sdiwspsshf csdikaepqp lspassscsv ssprstdscs stqhvpeeld llsssqspls
      121 lygdschsps saeplkeekp vtgpgnkteh gltpkkkiqm sskpsvqpkp lllpaapktp
      181 anasvpakti iiqtlpalmp lakqqsiisi qpaptkgqtv llsqpavvql qtpgvlpsaq
      241 pvlavtggat qlpnhvvnvv papvvnspvn gklcvtkpvl qsstrstgsd iavlrrqqrm
      301 iknresacqs rkkkkeymlg learlkaals eneqlkkeng slkrqldqvv senqrlkvps
      361 pkrravcvmi vlafimlnyg pmsmleqdsr rvkpsvspan qrrhllefsa kevkdtsdgd
      421 nqknsyrydh svsndkalmv lseepllyip pppcqplint teslrlnhel rgwvhrheve
      481 rtksrrmtns qqktrilqga leqgsnsqlm avqytettsi srnsgselqv yyaspgsyqg
      541 ffdairrrgd tfyvvsfrrd hlllpatthn kttrpkmsiv lpainindnv ingqdyevmm
      601 qidcqvmdtr ilhiksssvp pylrdhqrnq tstffgsppt atetthvvst lpesvq
//
LOCUS       NP_058950                471 aa            linear   ROD 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 2A [Rattus norvegicus].
ACCESSION   NP_058950 NP_068634
VERSION     NP_058950.1
DBSOURCE    REFSEQ: accession NM_017254.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Chen,X., Lv,R., Li,M., Zhang,L., Sun,Y., Cao,N. and Gu,B.
  TITLE     The serotonin(5-HT)2A receptor is involved in the hypersensitivity
            of bladder afferent neurons in cyclophosphamide-induced cystitis
  JOURNAL   Eur J Pharmacol 982, 176909 (2024)
   PUBMED   39154826
  REMARK    GeneRIF: The serotonin(5-HT)2A receptor is involved in the
            hypersensitivity of bladder afferent neurons in
            cyclophosphamide-induced cystitis.
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Nikolaus,S., Chao,O.Y., Henke,J., Beu,M., Fazari,B., Almeida,F.R.,
            Abdel-Hafiz,L., Antke,C., Hautzel,H., Mamlins,E., Muller,H.W.,
            Huston,J.P., von Gall,C. and Giesel,F.L.
  TITLE     5-HT1A and 5-HT2A receptor effects on recognition memory,
            motor/exploratory behaviors, emotionality and regional dopamine
            transporter binding in the rat
  JOURNAL   Behav Brain Res 469, 115051 (2024)
   PUBMED   38777263
  REMARK    GeneRIF: 5-HT1A and 5-HT2A receptor effects on recognition memory,
            motor/exploratory behaviors, emotionality and regional dopamine
            transporter binding in the rat.
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Farias,C.P., Leite,A.K.O., Schmidt,B.E., de Carvalho Myskiw,J. and
            Wyse,A.T.S.
  TITLE     The 5-HT2A, 5-HT5A, and 5-HT6 serotonergic receptors in the medial
            prefrontal cortex behave differently in extinction learning: Does
            social support play a role?
  JOURNAL   Behav Brain Res 463, 114922 (2024)
   PUBMED   38408524
  REMARK    GeneRIF: The 5-HT2A, 5-HT5A, and 5-HT6 serotonergic receptors in
            the medial prefrontal cortex behave differently in extinction
            learning: Does social support play a role?
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Rohn,T.T., Radin,D., Brandmeyer,T., Seidler,P.G., Linder,B.J.,
            Lytle,T., Mee,J.L. and Macciardi,F.
  TITLE     Intranasal delivery of shRNA to knockdown the 5HT-2A receptor
            enhances memory and alleviates anxiety
  JOURNAL   Transl Psychiatry 14 (1), 154 (2024)
   PUBMED   38509093
  REMARK    GeneRIF: Intranasal delivery of shRNA to knockdown the 5HT-2A
            receptor enhances memory and alleviates anxiety.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Ercan,Z., Bulmus,O., Kacar,E., Serhatlioglu,I., Zorlu,G. and
            Kelestimur,H.
  TITLE     Treadmill Exercise Improves Behavioral and Neurobiological
            Alterations in Restraint-Stressed Rats
  JOURNAL   J Mol Neurosci 73 (9-10), 831-842 (2023)
   PUBMED   37794307
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Bonhaus,D.W., Bach,C., DeSouza,A., Salazar,F.H., Matsuoka,B.D.,
            Zuppan,P., Chan,H.W. and Eglen,R.M.
  TITLE     The pharmacology and distribution of human 5-hydroxytryptamine2B
            (5-HT2B) receptor gene products: comparison with 5-HT2A and 5-HT2C
            receptors
  JOURNAL   Br J Pharmacol 115 (4), 622-628 (1995)
   PUBMED   7582481
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Du,Y.L., Wilcox,B.D., Teitler,M. and Jeffrey,J.J.
  TITLE     Isolation and characterization of the rat 5-hydroxytryptamine type
            2 receptor promoter: constitutive and inducible activity in
            myometrial smooth muscle cells
  JOURNAL   Mol Pharmacol 45 (6), 1125-1131 (1994)
   PUBMED   8022406
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Liu,J., Chen,Y., Kozak,C.A. and Yu,L.
  TITLE     The 5-HT2 serotonin receptor gene Htr-2 is tightly linked to Es-10
            on mouse chromosome 14
  JOURNAL   Genomics 11 (1), 231-234 (1991)
   PUBMED   1765383
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Julius,D., Huang,K.N., Livelli,T.J., Axel,R. and Jessell,T.M.
  TITLE     The 5HT2 receptor defines a family of structurally distinct but
            functionally conserved serotonin receptors
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 928-932 (1990)
   PUBMED   2300586
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Pritchett,D.B., Bach,A.W., Wozny,M., Taleb,O., Dal Toso,R.,
            Shih,J.C. and Seeburg,P.H.
  TITLE     Structure and functional expression of cloned rat serotonin 5HT-2
            receptor
  JOURNAL   EMBO J 7 (13), 4135-4140 (1988)
   PUBMED   2854054
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M30705.1.
            
            On Oct 1, 2003 this sequence version replaced NP_068634.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M30705.1, M64867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..471
                     /product="5-hydroxytryptamine receptor 2A"
                     /note="serotonin 5HT-2 receptor; 5-HT-2; 5-HT-2A;
                     serotonin receptor 2A; 5-hydroxytryptamine (serotonin)
                     receptor 2A, G protein-coupled"
                     /calculated_mol_wt=52719
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Region          75..391
                     /region_name="7tmA_5-HT2A"
                     /note="serotonin receptor subtype 2A, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15304"
                     /db_xref="CDD:341345"
     Region          76..102
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341345"
     Site            81..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Region          109..135
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341345"
     Site            112..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Site            147..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Region          148..178
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341345"
     Site            order(152,155..156,159..160,227,234..235,238,242,336,
                     339..340,343,346,359,362..363,366,370)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:341345"
     Region          172..174
                     /region_name="DRY motif, important for ligand-induced
                     conformation changes.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Region          190..213
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341345"
     Site            192..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Site            229
                     /site_type="other"
                     /note="Hydrophobic barrier that decreases the speed of
                     ligand binding and dissociation.
                     /evidence=ECO:0000250|UniProtKB:P28223; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Region          231..260
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341345"
     Site            233..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28223; propagated from
                     UniProtKB/Swiss-Prot (P14842.1)"
     Region          316..346
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341345"
     Site            323..348
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Site            357..382
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Region          359..384
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341345"
     Region          376..380
                     /region_name="NPxxY motif, important for ligand-induced
                     conformation changes and signaling.
                     /evidence=ECO:0000250|UniProtKB:P41595"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     Region          469..471
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:P28223"
                     /note="propagated from UniProtKB/Swiss-Prot (P14842.1)"
     CDS             1..471
                     /gene="Htr2a"
                     /gene_synonym="5-HT2A; 5Ht-2"
                     /coded_by="NM_017254.1:60..1475"
                     /db_xref="GeneID:29595"
                     /db_xref="RGD:61800"
ORIGIN      
        1 meilcednis lssipnslmq lgdgprlyhn dfnsrdants easnwtidae nrtnlscegy
       61 lpptclsilh lqeknwsall ttvviiltia gnilvimavs lekklqnatn yflmslaiad
      121 mllgflvmpv smltilygyr wplpsklcai wiyldvlfst asimhlcais ldryvaiqnp
      181 ihhsrfnsrt kaflkiiavw tisvgismpi pvfglqddsk vfkegsclla ddnfvligsf
      241 vaffipltim vityfltiks lqkeatlcvs dlstraklas fsflpqssls seklfqrsih
      301 repgsyagrr tmqsisneqk ackvlgivff lfvvmwcpff itnimavick escnenviga
      361 llnvfvwigy lssavnplvy tlfnktyrsa fsryiqcqyk enrkplqlil vntipalayk
      421 ssqlqvgqkk nsqedaeqtv ddcsmvtlgk qqseenctdn ietvnekvsc v
//
LOCUS       NP_112639                377 aa            linear   ROD 27-APR-2025
DEFINITION  apelin receptor [Rattus norvegicus].
ACCESSION   NP_112639
VERSION     NP_112639.1
DBSOURCE    REFSEQ: accession NM_031349.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Lei,J., Zheng,F., Chen,L., Zhang,R., Yang,Y., Yin,Z. and Luo,L.
  TITLE     Gstp1 negatively regulates blood pressure in hypertensive rat via
            promoting APLNR ubiquitination degradation mediated by Nedd4
  JOURNAL   Clin Sci (Lond) 138 (14), 883-900 (2024)
   PUBMED   38959295
  REMARK    GeneRIF: Gstp1 negatively regulates blood pressure in hypertensive
            rat via promoting APLNR ubiquitination degradation mediated by
            Nedd4.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Gemici,B., Birsen,I. and Izgut-Uysal,V.N.
  TITLE     The apelin-apela receptor APJ is necessary for formation and
            healing of ischemia reperfusion-induced gastric ulcer in rats
  JOURNAL   Peptides 166, 171027 (2023)
   PUBMED   37245722
  REMARK    GeneRIF: The apelin-apela receptor APJ is necessary for formation
            and healing of ischemia reperfusion-induced gastric ulcer in rats.
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Xi,Y., Li,Y., Ren,W., Bo,W., Ma,Y., Pan,S., Gong,D.W. and Tian,Z.
  TITLE     ELABELA-APJ-Akt/YAP Signaling Axis: A Novel Mechanism of Aerobic
            Exercise in Cardioprotection of Myocardial Infarction Rats
  JOURNAL   Med Sci Sports Exerc 55 (7), 1172-1183 (2023)
   PUBMED   36878020
  REMARK    GeneRIF: ELABELA-APJ-Akt/YAP Signaling Axis: A Novel Mechanism of
            Aerobic Exercise in Cardioprotection of Myocardial Infarction Rats.
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Akkan,S.S., Izgut-Uysal,V.N., Cakir,T., Ozbey,O. and Ustunel,I.
  TITLE     The effect of experimental varicocele on the apelin and APJ
            expressions in rat testis tissue
  JOURNAL   Tissue Cell 63, 101318 (2020)
   PUBMED   32223946
  REMARK    GeneRIF: The effect of experimental varicocele on the apelin and
            APJ expressions in rat testis tissue.
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Zhao,Y., Li,Y., Li,Z., Xu,B., Chen,P. and Yang,X.
  TITLE     Superoxide anions modulate the performance of apelin in the
            paraventricular nucleus on sympathetic activity and blood pressure
            in spontaneously hypertensive rats
  JOURNAL   Peptides 121, 170051 (2019)
   PUBMED   30582943
  REMARK    GeneRIF: The enhanced activity of endogenous apelin and APJ
            receptor in paraventricular nucleus contributes to sympathetic
            activation in hypertension.
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Medhurst,A.D., Jennings,C.A., Robbins,M.J., Davis,R.P., Ellis,C.,
            Winborn,K.Y., Lawrie,K.W., Hervieu,G., Riley,G., Bolaky,J.E.,
            Herrity,N.C., Murdock,P. and Darker,J.G.
  TITLE     Pharmacological and immunohistochemical characterization of the APJ
            receptor and its endogenous ligand apelin
  JOURNAL   J Neurochem 84 (5), 1162-1172 (2003)
   PUBMED   12603839
  REMARK    GeneRIF: Organ specificity of APJ receptor mRNA and distribution of
            the APJ receptor in rat brain and spinal cord was determined
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Reaux,A., De Mota,N., Skultetyova,I., Lenkei,Z., El Messari,S.,
            Gallatz,K., Corvol,P., Palkovits,M. and Llorens-Cortes,C.
  TITLE     Physiological role of a novel neuropeptide, apelin, and its
            receptor in the rat brain
  JOURNAL   J Neurochem 77 (4), 1085-1096 (2001)
   PUBMED   11359874
REFERENCE   8  (residues 1 to 377)
  AUTHORS   De Mota,N., Lenkei,Z. and Llorens-Cortes,C.
  TITLE     Cloning, pharmacological characterization and brain distribution of
            the rat apelin receptor
  JOURNAL   Neuroendocrinology 72 (6), 400-407 (2000)
   PUBMED   11146423
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Hosoya,M., Kawamata,Y., Fukusumi,S., Fujii,R., Habata,Y.,
            Hinuma,S., Kitada,C., Honda,S., Kurokawa,T., Onda,H., Nishimura,O.
            and Fujino,M.
  TITLE     Molecular and functional characteristics of APJ. Tissue
            distribution of mRNA and interaction with the endogenous ligand
            apelin
  JOURNAL   J Biol Chem 275 (28), 21061-21067 (2000)
   PUBMED   10777510
REFERENCE   10 (residues 1 to 377)
  AUTHORS   O'Carroll,A.M., Selby,T.L., Palkovits,M. and Lolait,S.J.
  TITLE     Distribution of mRNA encoding B78/apj, the rat homologue of the
            human APJ receptor, and its endogenous ligand apelin in brain and
            peripheral tissues
  JOURNAL   Biochim Biophys Acta 1492 (1), 72-80 (2000)
   PUBMED   11004481
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072494.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC072494.1, AB033170.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..377
                     /product="apelin receptor"
                     /note="B78; GPCR34; G-protein coupled receptor APJ;
                     angiotensin receptor-like 1"
                     /calculated_mol_wt=42218
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          17..318
                     /region_name="7tmA_Apelin_R"
                     /note="apelin receptor, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15190"
                     /db_xref="CDD:341340"
     Site            order(18..22,83,86..87,89,91,108,166,171..175,181,183,196,
                     262,266,269,289,293,297)
                     /site_type="other"
                     /note="peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:341340"
     Region          28..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341340"
     Site            29..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          62..87
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341340"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Site            83
                     /site_type="other"
                     /note="Required for APELA and APLN/apelin-13 interaction
                     and signaling. /evidence=ECO:0000250|UniProtKB:P35414;
                     propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Site            98..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          100..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341340"
     Region          143..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341340"
     Site            145..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Site            166
                     /site_type="other"
                     /note="Required for APELA and APLN/apelin-13 interaction
                     and signaling. /evidence=ECO:0000250|UniProtKB:P35414;
                     propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          196..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341340"
     Site            197..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          239..269
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341340"
     Site            245..268
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          286..311
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341340"
     Site            288..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     Region          335..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHG3.1)"
     CDS             1..377
                     /gene="Aplnr"
                     /gene_synonym="Agtrl1; Apj"
                     /coded_by="NM_031349.2:224..1357"
                     /db_xref="GeneID:83518"
                     /db_xref="RGD:621645"
ORIGIN      
        1 meddgynyyg adnqsecdya dwtpsgalip aiyilvfllg ttgnglvlwt vfwssrekrr
       61 sadifiasla vadltfvvtl plwatytyre fdwpfgtfsc klssylifvn myasvfcltg
      121 lsfdrylaiv rpvanarlrl rvsgavatav lwvlaallav pvmvfrstdi penstktqcy
      181 mdysmvatsn sewawevglg vsstavgfvv pfiimltcyf fiaqtiaghf rkerieglrk
      241 rrrllsiivv lvvtfalcwm pyhlvktlym lgnllhwpcd fdsflmnvfp yctcisyvns
      301 clnpflyaff dprfrracts mlccdqsgck gsphsssaek sasyssghsq gpgpnmckgg
      361 epmheksipy sqetlvd
//
LOCUS       NP_001129464             267 aa            linear   ROD 27-APR-2025
DEFINITION  Fc gamma receptor 2A like 1 [Rattus norvegicus].
ACCESSION   NP_001129464
VERSION     NP_001129464.1
DBSOURCE    REFSEQ: accession NM_001135992.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Farber,D.L. and Sears,D.W.
  TITLE     Rat CD16 is defined by a family of class III Fc gamma receptors
            requiring co-expression of heteroprotein subunits
  JOURNAL   J Immunol 146 (12), 4352-4361 (1991)
   PUBMED   1710249
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Zeger,D.L., Hogarth,P.M. and Sears,D.W.
  TITLE     Characterization and expression of an Fc gamma receptor cDNA cloned
            from rat natural killer cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3425-3429 (1990)
   PUBMED   1692135
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC159405.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC159405.1, M32062.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132264,
                                           SAMD00132265 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..267
                     /product="Fc gamma receptor 2A like 1"
                     /note="Fc-gamma RIIIB-alpha; Fc-gamma RIIIC-alpha;
                     Fc-gamma RIIID-alpha; low affinity immunoglobulin gamma Fc
                     region receptor III-like; Fc gamma receptor II beta"
                     /calculated_mol_wt=30153
     Region          41..119
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          58..62
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409410"
     Region          72..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409410"
     Region          89..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409410"
     Region          101..106
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409410"
     Region          112..115
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409410"
     Region          123..205
                     /region_name="Ig2_FcgammaR_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     Fcgamma-receptors (FcgammaRs), and similar domains;
                     cd05753"
                     /db_xref="CDD:409411"
     Site            order(123,146,152..153)
                     /site_type="other"
                     /note="Fc binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          123..127
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409411"
     Region          132..134
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409411"
     Site            order(136..138,147,152,191)
                     /site_type="other"
                     /note="pentraxin binding site [polypeptide binding]"
                     /db_xref="CDD:409411"
     Region          138..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409411"
     Region          152..158
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409411"
     Region          161..166
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409411"
     Region          170..174
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409411"
     Region          184..189
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409411"
     Region          195..205
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409411"
     CDS             1..267
                     /gene="Fcgr2al1"
                     /coded_by="NM_001135992.1:97..900"
                     /db_xref="GeneID:498276"
                     /db_xref="RGD:1594388"
ORIGIN      
        1 mtletqmfqn ahsgsqwllp pltmlllfaf adrqtgdllk avvkrdppwi qvlkddtvtl
       61 tcegthnpgn sstqwfhnqs stwgqvqasy tfkatvndsg eyrcrmahts lsdpihlevi
      121 sdwlllqtpq lvfeegetit lrchswknkq ltkvllfqng kpvryyyqss nfsipkanhs
      181 hsgnyyckay lgrtmhvskp vtitvqgsat astsslvwfh aafclvmcll favdtglyfc
      241 vrrnlqtsge dwrkslsvgk ykapqdk
//
LOCUS       NP_001020868             524 aa            linear   ROD 27-APR-2025
DEFINITION  hydroxysteroid dehydrogenase-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001020868 XP_232942
VERSION     NP_001020868.1
DBSOURCE    REFSEQ: accession NM_001025697.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Kowalik,D., Haller,F., Adamski,J. and Moeller,G.
  TITLE     In search for function of two human orphan SDR enzymes:
            hydroxysteroid dehydrogenase like 2 (HSDL2) and short-chain
            dehydrogenase/reductase-orphan (SDR-O)
  JOURNAL   J Steroid Biochem Mol Biol 117 (4-5), 117-124 (2009)
   PUBMED   19703561
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097407.1.
            
            On Jul 22, 2005 this sequence version replaced XP_232942.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097407.1, SRR8487226.183875.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..524
                     /product="hydroxysteroid dehydrogenase-like protein 2"
                     /calculated_mol_wt=58213
     Region          8..248
                     /region_name="HSDL2_SDR_c"
                     /note="human hydroxysteroid dehydrogenase-like protein 2
                     (HSDL2), classical (c) SDRs; cd09762"
                     /db_xref="CDD:187663"
     Site            order(17,19..22,41..43,50,73..75,101..103,124,151,168,172,
                     196,200..201,203..205)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187663"
     Site            order(78,113,115,118..119,122,127,130,134,137,155,157,159,
                     166,170,177..178,180..182,184..185)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187663"
     Site            116
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q2TPA8; propagated from
                     UniProtKB/Swiss-Prot (Q4V8F9.1)"
     Site            order(125,153,168,172)
                     /site_type="active"
                     /db_xref="CDD:187663"
     Region          283..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8F9.1)"
     Region          424..517
                     /region_name="SCP2"
                     /note="SCP-2 sterol transfer family; pfam02036"
                     /db_xref="CDD:460423"
     CDS             1..524
                     /gene="Hsdl2"
                     /gene_synonym="RGD1305387"
                     /coded_by="NM_001025697.1:116..1690"
                     /db_xref="GeneID:313200"
                     /db_xref="RGD:1305387"
ORIGIN      
        1 mlpntgklag ctvfitgasr gigkaialka akdganivia akttqrhpkl lgtiytaaee
       61 ieaaggkalp cvvdvrdeqq insavekave rfggidilvn nasaisltnt letptkrvdl
      121 mmsvntrgty ltskacipfl kkskvahiln lspplnlnpm wfkqhcayti akygmsmcvl
      181 gmaeefrgei avnalwprta ihtaamdmlg gagvesqcrk vdiiadaays ifkrpksftg
      241 nfiidenilk eegikdfdiy aitpghpllp dffldehpda vmeekesydp vpevkeeklq
      301 lqeqpqlqeq pqlqekpqlq eqpqlqekpq lqeqpqlqeq pqlqeqpqqq pqlqeqpqlq
      361 ekpqlqeqpq qqekpqpqqq pqqqpqqrpq qrpqpqpqpq pllqsvlppk phfgaveetf
      421 rivkdslsde vvratqavyq felsgedggt wfldlkskgg kvghgepsdr advvmsmate
      481 dfvkmfsgkl kptmafmsgk lkikgniala ikleklmthm nsrl
//
LOCUS       NP_001028888             652 aa            linear   ROD 27-APR-2025
DEFINITION  calpastatin isoform c [Rattus norvegicus].
ACCESSION   NP_001028888
VERSION     NP_001028888.1
DBSOURCE    REFSEQ: accession NM_001033716.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Gritsyna,Y.V., Salmov,N.N., Bobylev,A.G., Ulanova,A.D.,
            Kukushkin,N.I., Podlubnaya,Z.A. and Vikhlyantsev,I.M.
  TITLE     Increased Autolysis of mu-Calpain in Skeletal Muscles of Chronic
            Alcohol-Fed Rats
  JOURNAL   Alcohol Clin Exp Res 41 (10), 1686-1694 (2017)
   PUBMED   28800153
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Manfredi,L.H., Lustrino,D., Machado,J., Silveira,W.A., Zanon,N.M.,
            Navegantes,L.C. and Kettelhut,I.C.
  TITLE     Adrenodemedullation activates the Ca2+-dependent proteolysis in
            soleus muscles from rats exposed to cold
  JOURNAL   J Appl Physiol (1985) 122 (2), 317-326 (2017)
   PUBMED   27765842
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Mochida,S., Hida,Y., Tanifuji,S., Hagiwara,A., Hamada,S., Abe,M.,
            Ma,H., Yasumura,M., Kitajima,I., Sakimura,K. and Ohtsuka,T.
  TITLE     SAD-B Phosphorylation of CAST Controls Active Zone Vesicle
            Recycling for Synaptic Depression
  JOURNAL   Cell Rep 16 (11), 2901-2913 (2016)
   PUBMED   27626661
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 652)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 652)
  AUTHORS   Yasuoka,H., Sugano,Y., Oka,T., Watanabe,C., Kaneko,Y., Nojima,T.,
            Matsumura,M., Fujii,T. and Mimori,T.
  TITLE     [Antigenic epitopes recognized by autoantibodies to calpastatin in
            patients with rheumatoid arthritis and their clinical significance]
  JOURNAL   Ryumachi 37 (3), 458-466 (1997)
   PUBMED   9256029
REFERENCE   7  (residues 1 to 652)
  AUTHORS   Despres,N., Talbot,G., Plouffe,B., Boire,G. and Menard,H.A.
  TITLE     Detection and expression of a cDNA clone that encodes a polypeptide
            containing two inhibitory domains of human calpastatin and its
            recognition by rheumatoid arthritis sera
  JOURNAL   J Clin Invest 95 (4), 1891-1896 (1995)
   PUBMED   7706496
REFERENCE   8  (residues 1 to 652)
  AUTHORS   Lee,W.J., Hatanaka,M. and Maki,M.
  TITLE     Multiple forms of rat calpastatin cDNA in the coding region of
            functionally unknown amino-terminal domain
  JOURNAL   Biochim Biophys Acta 1129 (2), 251-253 (1992)
   PUBMED   1730065
REFERENCE   9  (residues 1 to 652)
  AUTHORS   Ishida,S., Emori,Y. and Suzuki,K.
  TITLE     Rat calpastatin has diverged primary sequence from other mammalian
            calpastatins but retains functionally important sequences
  JOURNAL   Biochim Biophys Acta 1088 (3), 436-438 (1991)
   PUBMED   2015306
REFERENCE   10 (residues 1 to 652)
  AUTHORS   Uemori,T., Shimojo,T., Asada,K., Asano,T., Kimizuka,F., Kato,I.,
            Maki,M., Hatanaka,M., Murachi,T., Hanzawa,H. et al.
  TITLE     Characterization of a functional domain of human calpastatin
  JOURNAL   Biochem Biophys Res Commun 166 (3), 1485-1493 (1990)
   PUBMED   2407243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091239.1, AF346597.1 and Y13589.1.
            
            Transcript Variant: This variant (3) lacks two in-frame exons
            compared to variant 1. The resulting isoform (c) has the same N-
            and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ186625.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q11"
     Protein         1..652
                     /product="calpastatin isoform c"
                     /note="calpain inhibitor"
                     /calculated_mol_wt=70426
     Region          <133..197
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          208..330
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          344..440
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          455..577
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     CDS             1..652
                     /gene="Cast"
                     /coded_by="NM_001033716.1:148..2106"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:25403"
                     /db_xref="RGD:2278"
ORIGIN      
        1 msrpgpkpaa ssrprrgaaa shtqehvnek nigssskpae kkgsdevtas saatgtsprm
       61 sttgakavki eseksqssep pvihekkpkg kpkegsetkf qdapsadges vaggvtvata
      121 sdkvvvksgv naalddlidt lgecedtnkd dppytgpvvl dpmdstylea lgikegtipp
      181 eyrkllekne aitgplpdsp kpmgidhaid alssdftcss ptgkqtekek stgesskaqs
      241 agvtrsavpp qekkrkveee vmndqalqal sdslgtrqpd pqshlrqakq vkeakakeer
      301 qekcgededt vpaeyrlkpa kdkdgkpllp epeetskcls eseligelsa dfvqptyqek
      361 psmpaakikk gvvpddavet larslgtrke dpedekslvd kvkekakeed heklgekeet
      421 ippdyrleiv kdkdgkpllp keaeeqlppl sddflldals qdfsspanil slgfedakls
      481 aavsetvsqv papsnhtaap ppgterrdke lddaldelsd slgqrqpdpd enkplddkvk
      541 ekikaehsek lgerddtipp eyrhlldndg kdkpekpltk ntekpgqdqd pidalsedld
      601 scppttetsq nttkekgkkt ssskasknee ktkdsskkte evpkpkvded at
//
LOCUS       NP_001013055             413 aa            linear   ROD 27-APR-2025
DEFINITION  probable inactive allantoicase [Rattus norvegicus].
ACCESSION   NP_001013055 XP_216673
VERSION     NP_001013055.1
DBSOURCE    REFSEQ: accession NM_001013037.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Vigetti,D., Binelli,G., Monetti,C., Prati,M., Bernardini,G. and
            Gornati,R.
  TITLE     Selective pressure on the allantoicase gene during vertebrate
            evolution
  JOURNAL   J Mol Evol 57 (6), 650-658 (2003)
   PUBMED   14745534
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Vigetti,D., Monetti,C., Prati,M., Gornati,R. and Bernardini,G.
  TITLE     Genomic organization and chromosome localization of the murine and
            human allantoicase gene
  JOURNAL   Gene 289 (1-2), 13-17 (2002)
   PUBMED   12036579
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078971.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216673.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078971.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..413
                     /product="probable inactive allantoicase"
                     /EC_number="3.5.3.4"
                     /note="probable allantoicase; allantoate amidinohydrolase"
                     /calculated_mol_wt=45907
     Region          18..385
                     /region_name="allantoicase"
                     /note="TIGR02961"
                     /db_xref="CDD:274363"
     CDS             1..413
                     /gene="Allc"
                     /coded_by="NM_001013037.1:154..1395"
                     /db_xref="GeneID:246758"
                     /db_xref="RGD:621804"
ORIGIN      
        1 madtpkegkl trfldftqli dlasecvggk vlfatddffg paenliksnn psfkeneyte
       61 fgkwvdgwet rrkripghdw cviqlgiqgi irgidvdisy fsgnyaprms iqaanlsedt
      121 vtnipprgvk mgaaatseef vaitelkshs wdylvpmsel kpgdpdsshn yffvnsqqrw
      181 thirlnifpd ggvarlrvyg tgqrdwaald stepvdlvai afggvcvgfs nahfghpnnm
      241 igvgdpksia dgwetarrld rppvlegnen gflqvpgcew avfrlahpgv itqieidtky
      301 fkgnspdsck vdgcilttle eedmirqkws lpahkwkpll pvtkltpnqn hlldsltlel
      361 qdvitharit iapdggvsrl rlkgfpssic llrplrekpm lrfslkagfr anl
//
LOCUS       NP_001014014             395 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 385D [Rattus norvegicus].
ACCESSION   NP_001014014 XP_223794
VERSION     NP_001014014.1
DBSOURCE    REFSEQ: accession NM_001013992.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079278.1.
            
            On Apr 20, 2005 this sequence version replaced XP_223794.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079278.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..395
                     /product="zinc finger protein 385D"
                     /note="zinc finger protein 659"
                     /calculated_mol_wt=42349
     Region          82..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          82..104
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          204..228
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          206..268
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(213..215,217..218,222,253,274,277..281,283..284)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          267..291
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          269..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          282..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXX3.1)"
     CDS             1..395
                     /gene="Zfp385d"
                     /gene_synonym="Znf385d"
                     /coded_by="NM_001013992.1:276..1463"
                     /db_xref="GeneID:305691"
                     /db_xref="RGD:1359606"
ORIGIN      
        1 mrkimyfggt cqspalpali hppapplqps ldikpflpfp ldtaatvnlf pnfnamdpiq
       61 kavinhtfgf plphrkkqii scnicqlrfn sdsqaaahyk gtkhakklka lesmknkqks
      121 vtakdsaktt ftsittnpit tssdktesta gtqviarsad mrkssevtte ltsnaekslt
      181 aavaagnnss ppteteeeka krllycslck vavnsasqle ahnsgtkhkt mlearngsgt
      241 ikafpragmk gkgpvnkgnt glqnktfhce icdvhvnset qlkqhissrr hkdrasgkpp
      301 kpkyspynkl qkaahplgvk lvfskepskp ltprilpnpl aaaaaaaava vnspfslrta
      361 paatlfqtsa lppallrpap gpirtthtpv lfspy
//
LOCUS       NP_001013178             499 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 [Rattus norvegicus].
ACCESSION   NP_001013178 XP_230524
VERSION     NP_001013178.1
DBSOURCE    REFSEQ: accession NM_001013160.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091171.1.
            
            On Apr 20, 2005 this sequence version replaced XP_230524.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..499
                     /product="E3 ubiquitin-protein ligase TRIM69"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 69; ring finger
                     protein 36; RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=57084
     Region          1..152
                     /region_name="Necessary for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK82.1)"
     Region          35..93
                     /region_name="RING-HC_TRIM69_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 69 (TRIM69) and similar proteins;
                     cd16611"
                     /db_xref="CDD:438273"
     Region          115..>141
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <152..>299
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Region          311..496
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BK82.1)"
     CDS             1..499
                     /gene="Trim69"
                     /gene_synonym="Rnf36"
                     /coded_by="NM_001013160.1:55..1554"
                     /db_xref="GeneID:311373"
                     /db_xref="RGD:1305074"
ORIGIN      
        1 mevssrppsn fdpgnyvevs dpsthlpskv viqdittelh cplcndwfrd plmltcghnf
       61 cqaciqnywk mqaketfcpe ckmlcqysnc tfnlvleklv ekikrlpllk ghpqcpehge
      121 nlklfskpdg kmicfqckda rlsmgqskdf lqiseavrff teelaiyqsq lqttlkelqs
      181 lrtmqkdaia aykdnkiqlq qnlsleflkl hqflhnkekd ilndlrdegk vlneemdanl
      241 nqiqeqclla kdmlaniqar meqqnsfdfl tditkllenm ekgmktlvpr qliskklslg
      301 rfkgpiqyti wremqsilsp gpsqltldpk tahpnlvlsn srtsvchgdv kqvmpddper
      361 fdssvavlgs kgftsgkwyw eievakktkw tigivresii rkgscpltpe qgfwllrlrn
      421 qtdlkaldlp scslnlgdlr rvgvyldyeg gqvsfynatn mthlytftsv fleklfpylc
      481 pclndggenk eplhivhpq
//
LOCUS       NP_001101508            2542 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger FYVE domain-containing protein 26 [Rattus norvegicus].
ACCESSION   NP_001101508 XP_001080898 XP_234335
VERSION     NP_001101508.1
DBSOURCE    REFSEQ: accession NM_001108038.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2542)
  AUTHORS   Slabicki,M., Theis,M., Krastev,D.B., Samsonov,S., Mundwiller,E.,
            Junqueira,M., Paszkowski-Rogacz,M., Teyra,J., Heninger,A.K.,
            Poser,I., Prieur,F., Truchetto,J., Confavreux,C., Marelli,C.,
            Durr,A., Camdessanche,J.P., Brice,A., Shevchenko,A.,
            Pisabarro,M.T., Stevanin,G. and Buchholz,F.
  TITLE     A genome-scale DNA repair RNAi screen identifies SPG48 as a novel
            gene associated with hereditary spastic paraplegia
  JOURNAL   PLoS Biol 8 (6), e1000408 (2010)
   PUBMED   20613862
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2542)
  AUTHORS   Sagona,A.P., Nezis,I.P., Pedersen,N.M., Liestol,K., Poulton,J.,
            Rusten,T.E., Skotheim,R.I., Raiborg,C. and Stenmark,H.
  TITLE     PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment
            of FYVE-CENT to the midbody
  JOURNAL   Nat Cell Biol 12 (4), 362-371 (2010)
   PUBMED   20208530
REFERENCE   3  (residues 1 to 2542)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473947.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001080898.1, XP_234335.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2542
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..2542
                     /product="zinc finger FYVE domain-containing protein 26"
                     /note="zinc finger, FYVE domain containing 26"
                     /calculated_mol_wt=284086
     Region          591..658
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Region          740..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68DK2; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Region          1273..1292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DU37; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Region          1746..1807
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            1761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68DK2; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            1783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DU37; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Site            1785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DU37; propagated from
                     UniProtKB/Swiss-Prot (D4A8G9.1)"
     Region          1812..1872
                     /region_name="FYVE_ZFY26"
                     /note="FYVE domain found in FYVE domain-containing protein
                     26 (ZFY26 or ZFYVE26); cd15724"
                     /db_xref="CDD:277263"
     Site            order(1812,1815,1834..1839,1841..1842,1865..1867)
                     /site_type="other"
                     /note="putative phosphatidylinositol 3-phosphate binding
                     site [chemical binding]"
                     /db_xref="CDD:277263"
     CDS             1..2542
                     /gene="Zfyve26"
                     /coded_by="NM_001108038.1:157..7785"
                     /db_xref="GeneID:314265"
                     /db_xref="RGD:1307820"
ORIGIN      
        1 msypfgkeet ttekqlfeff ceclrrgdwe laqacvpqlq rgqgeipqkv edilqalvqc
       61 pillrcgpdi npqrlawlwl lvlekwlppe kkllstvfrr kleflflsed lqggipetil
      121 kelfetlaqg pagctsdrsq rwesgapqls peavsmlwnl lkqapgpaqa llellleerh
      181 saslchsslq kslldlirka lqtlrdpasq pagvtdavcg alqalcctae lpegewhvlc
      241 eelletcrte gsplkeerll gcllhkagrs llslyghtya ekvaerppka slsgkdhpdp
      301 eramlalfst pdpahawkma ffyclsnnkh fleqilvtal tllkeedfps lgylldrefr
      361 plshllvllg wthcqslesa krllqtlyrn qdqghdellr daceglwahl evlewcvqqs
      421 sslipkrell chlhggdshs vlyslhhltn lpalreeevl kllqkvptkd lqgehdthda
      481 svpehlsqcq sltlyqgfca mkyavyalcv nshqhsqcpd crdsasseel alvepgrdsl
      541 pspgashlfp tylarcrqyl qripdslcle ilenifslll itsadlhpep hlpedyaedd
      601 diegkgpwgl wspsespqhi aaterrsera smgprdlapt gpgcpkgepk dnspgphths
      661 fldlkhftss lsgfladefa igaflsliqe qlnelsshrt peetelledq scwaardglq
      721 grlhrfskvl seaqwrykvv tsnqsseeqp srryrptakr hsslrrgrrt rrtradgrer
      781 gsnpslegts selststseg slsavsgqve adnrfqpqpq ssiipmmfsp pesllascil
      841 rgnfaeahqv vlmfnlkssp sagelmfver yqeviqelar vehkienqns dggnntvrrt
      901 gsgrstlqai gsaaaagmvf ysisdvtdkl lspsedpipt lqedfwinaa ltetntplrg
      961 vledlsppam aafdlaccqc qlwktckqll etaerrlsss legrgrrldq vvlnpdgmrg
     1021 fpfvlqqisk ilsypltvtg ltksetleer gggaprcsis ellqmcwpsl tedciashts
     1081 lsqqldqalq slrealtlse pkstpltclv eqaaqkapea eahpvhiqsq llqktlgkqt
     1141 lagprqtdyv gaffsycssl akvllrslss dpdnvevkvg npfvllqqss sqlvshllle
     1201 rqvppdrlaa llaqehlnls vpqvivsccc epltlclsrq sqqassltah lgmlaqghas
     1261 hlldglplsv lgsprpsenp saerksdssp kdslpaftas alaflksrsk ilamvaclra
     1321 srgtkvsrps lswkelrgrr eapltaekva qecehlleqf pvfeaallan weplqqases
     1381 rpslaaslcg qarlstvllg lhstlaqdvv teafeealva rdwpralqli dvygqdsddl
     1441 ssvrdsvltc atvcdkegwq ylfpvkdasl rsqlalrfvd kwplesclei laycvsdmav
     1501 peelkselqr kltelrvyqk ilglqdppvw cdwqtlrscc aedpstvmdm mlgsqeyelc
     1561 eewgclypip rehlvslhhk hllyllerre yekalqllqr ipdptmclev tersldqhps
     1621 latshflany ltshfygelt tdrhheiqal ymgskvlltl peqhrasyah lssspllmle
     1681 qllmnmkvdw attavqtlqq llagqdigft ldevdsllsr yagkaldlpy plrekrsdsm
     1741 ihlqepvhqa sdpetlsrss saefsaaaaa papaapgsal vcspspkera fpqtqpplef
     1801 vppetppard qwvpdetesm cmvccrehft mfnrrhhcrr cgrlvcgscs tkkmvvegcr
     1861 enptrvcdqc ysyynkdape espcqsevpd saknespsys avvripkate vewilslnee
     1921 enelvrsefy yeqapsaslc iailnlhrds iacghqlieh ccrlsrgltn pevdagllid
     1981 imkqllfsak mmfvkagqsq dlalcdsyis kvdvlhilva aayrhmpsld qilqpasvtr
     2041 lrnqlleaey yqlgvevstk tgldstgawh awgmaclkag nltaarekfs rclkppldln
     2101 qlshgsrlvq dvveylestv rplvslqddd yfatlrelea tlrtqslfle aipdgkimnn
     2161 tyyqeclfyl hnystnlaii sfymrhnclr eallhllnke spaevfiegi fqpsyksgkl
     2221 htlenllesi dptleswgay liaacqhlqk knyyhilyel qqfmkdqvra amtcirffsh
     2281 kaksytelge klswllkakd hlkiylqens rssgrkkttf frkkmaaadv srhmntlqlq
     2341 mevtrflhrc esartsqitt lplptlfgnn hmkmevacqv mlggknvedg fgiafrvlqd
     2401 fqldaavtyc raarqlveke kygeirqllk cvsesgmaak sdgdtillnc leafkrippq
     2461 elegliqaih sddnkvrayl tccklrsayl iavkqehtqa aalvqqvqqa akssgdsvvq
     2521 dicaqwllts hsrgahgsgs rk
//
LOCUS       NP_001029255              88 aa            linear   ROD 27-APR-2025
DEFINITION  stannin [Rattus norvegicus].
ACCESSION   NP_001029255 XP_001052997
VERSION     NP_001029255.1
DBSOURCE    REFSEQ: accession NM_001034083.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Buck-Koehntop,B.A., Mascioni,A., Buffy,J.J. and Veglia,G.
  TITLE     Structure, dynamics, and membrane topology of stannin: a mediator
            of neuronal cell apoptosis induced by trimethyltin chloride
  JOURNAL   J Mol Biol 354 (3), 652-665 (2005)
   PUBMED   16246365
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Davidson,C.E., Reese,B.E., Billingsley,M.L. and Yun,J.K.
  TITLE     The protein stannin binds 14-3-3zeta and modulates
            mitogen-activated protein kinase signaling
  JOURNAL   Brain Res Mol Brain Res 138 (2), 256-263 (2005)
   PUBMED   15923056
  REMARK    GeneRIF: Together, these findings indicate a role of Stannin in
            modulation of MAPK signaling pathways through its interactions with
            14-3-3zeta
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Dejneka,N.S., Patanow,C.M., Polavarapu,R., Toggas,S.M., Krady,J.K.
            and Billingsley,M.L.
  TITLE     Localization and characterization of stannin: relationship to
            cellular sensitivity to organotin compounds
  JOURNAL   Neurochem Int 31 (6), 801-815 (1997)
   PUBMED   9413842
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Toggas,S.M., Krady,J.K. and Billingsley,M.L.
  TITLE     Molecular neurotoxicology of trimethyltin: identification of
            stannin, a novel protein expressed in trimethyltin-sensitive cells
  JOURNAL   Mol Pharmacol 42 (1), 44-56 (1992)
   PUBMED   1635553
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100111.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001052997.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100111.1, M81639.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..88
                     /product="stannin"
                     /calculated_mol_wt=9370
     Region          4..88
                     /region_name="Stannin"
                     /note="cd20257"
                     /db_xref="CDD:380774"
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P61808.1)"
     Site            39..45
                     /site_type="other"
                     /note="putative 14-3-3zeta binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380774"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61807; propagated from
                     UniProtKB/Swiss-Prot (P61808.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61808.1)"
     CDS             1..88
                     /gene="Snn"
                     /coded_by="NM_001034083.1:165..431"
                     /db_xref="GeneID:29140"
                     /db_xref="RGD:3730"
ORIGIN      
        1 msimdhsptt gvvtvivili aiaalgalil gcwcylrlqr isqsedeesi vgdgetkepf
       61 llvqysakgp cverkaklmt anspevhg
//
LOCUS       NP_001020593             624 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-1 receptor-associated kinase-like 2 [Rattus
            norvegicus].
ACCESSION   NP_001020593 XP_342740
VERSION     NP_001020593.1
DBSOURCE    REFSEQ: accession NM_001025422.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Liu,Z., Zhao,N., Zhu,H., Zhu,S., Pan,S., Xu,J., Zhang,X., Zhang,Y.
            and Wang,J.
  TITLE     Circulating interleukin-1beta promotes endoplasmic reticulum
            stress-induced myocytes apoptosis in diabetic cardiomyopathy via
            interleukin-1 receptor-associated kinase-2
  JOURNAL   Cardiovasc Diabetol 14, 125 (2015)
   PUBMED   26394923
  REMARK    GeneRIF: Elevated circulating IL-1beta contributed to promote ER
            stress- induced myocytes apoptosis by affecting IRAK-2/CHOP pathway
            in diabetic cardiomyopathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Kumar,H., Kawai,T. and Akira,S.
  TITLE     Pathogen recognition by the innate immune system
  JOURNAL   Int Rev Immunol 30 (1), 16-34 (2011)
   PUBMED   21235323
  REMARK    Review article
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Weber,A., Wasiliew,P. and Kracht,M.
  TITLE     Interleukin-1 (IL-1) pathway
  JOURNAL   Sci Signal 3 (105), cm1 (2010)
   PUBMED   20086235
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Bailey,M.J., Coon,S.L., Carter,D.A., Humphries,A., Kim,J.S.,
            Shi,Q., Gaildrat,P., Morin,F., Ganguly,S., Hogenesch,J.B.,
            Weller,J.L., Rath,M.F., Moller,M., Baler,R., Sugden,D.,
            Rangel,Z.G., Munson,P.J. and Klein,D.C.
  TITLE     Night/day changes in pineal expression of >600 genes: central role
            of adrenergic/cAMP signaling
  JOURNAL   J Biol Chem 284 (12), 7606-7622 (2009)
   PUBMED   19103603
  REMARK    GeneRIF: Expression of Irak2 increases ~ 15-fold at night in the
            rat pineal gland, as a result of adrenergic-cyclic AMP signalling.
            Night time levels are >15-fold greater than median expression
            levels in other tissues.
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Elzinga,B.M., Twomey,C., Powell,J.C., Harte,F. and McCarthy,J.V.
  TITLE     Interleukin-1 receptor type 1 is a substrate for
            gamma-secretase-dependent regulated intramembrane proteolysis
  JOURNAL   J Biol Chem 284 (3), 1394-1409 (2009)
   PUBMED   18996842
  REMARK    GeneRIF: TRAF6 and interleukin receptor-associated kinase 2 are
            novel binding partners for PS1, and IL-1R1 is a new substrate for
            presenilin-dependent gamma-secretase cleavage
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Hardy,M.P. and O'Neill,L.A.
  TITLE     The murine IRAK2 gene encodes four alternatively spliced isoforms,
            two of which are inhibitory
  JOURNAL   J Biol Chem 279 (26), 27699-27708 (2004)
   PUBMED   15082713
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Rosati,O. and Martin,M.U.
  TITLE     Identification and characterization of murine IRAK-2
  JOURNAL   Biochem Biophys Res Commun 297 (1), 52-58 (2002)
   PUBMED   12220507
REFERENCE   8  (residues 1 to 624)
  AUTHORS   Mamidipudi,V., Li,X. and Wooten,M.W.
  TITLE     Identification of interleukin 1 receptor-associated kinase as a
            conserved component in the p75-neurotrophin receptor activation of
            nuclear factor-kappa B
  JOURNAL   J Biol Chem 277 (31), 28010-28018 (2002)
   PUBMED   12034707
REFERENCE   9  (residues 1 to 624)
  AUTHORS   Wesche,H., Gao,X., Li,X., Kirschning,C.J., Stark,G.R. and Cao,Z.
  TITLE     IRAK-M is a novel member of the Pelle/interleukin-1
            receptor-associated kinase (IRAK) family
  JOURNAL   J Biol Chem 274 (27), 19403-19410 (1999)
   PUBMED   10383454
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098060.1.
            
            On Jul 15, 2005 this sequence version replaced XP_342740.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098060.1, SRR8487227.155940.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..624
                     /product="interleukin-1 receptor-associated kinase-like 2"
                     /note="IRAK-2"
                     /calculated_mol_wt=69106
     Region          3..91
                     /region_name="Death_IRAK2"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-2; cd08795"
                     /db_xref="CDD:176773"
     Site            order(5..6,8..11,44,52..53,58..59,62..68,73)
                     /site_type="other"
                     /note="IRAK2-IRAK4 interaction site [polypeptide binding]"
                     /db_xref="CDD:176773"
     Region          216..504
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(216..219,222,224,235,237,270,286..289,335,339..340,
                     342,352..353)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          508..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS0.1)"
     Region          549..593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQS0.1)"
     CDS             1..624
                     /gene="Irak2"
                     /coded_by="NM_001025422.1:36..1910"
                     /db_xref="GeneID:362418"
                     /db_xref="RGD:1309584"
ORIGIN      
        1 macyiyqlps wvlddlcrni dtlsewdwmq fasyvitdlt qlrkiksmer vqgvsitrel
       61 lwwwsmrqat vqqlvdllch lelyraaqiv lswkpapdsl splsafpeav kpgpvatsgr
      121 nlkddqkkgq pvkpcsflss gttmagaqqq ascqrpceed apcslktdvp dslqskycst
      181 sipkqeklln lpgdrlfwse adivqatedf dqshrisegt fadiyrgqrn gvafafkrlr
      241 evtgsspgsm drflqaemql clrcchpnil pllgfctgrq fhsliypyma ngslqdrlwa
      301 qgdsdmlswp qrasicsgll lavehlhsld iihsnvksan vlldqhlnpk lahpvahpcp
      361 tnkktkytvm kthlfqasaa ylpenfirvg qltkqvdifs cgivlaevlt gipamdkdrs
      421 pvylkdllls eipsntssvh srktsmgkvv vkeicqkhle rkagllpeac aetwatavsv
      481 clrrreasle earvsmagve eqlrgqlslp wsrvsedtgs ssntpeetdd vdnsslsvps
      541 svmvvscarv sspppsmgng taqpstsgrq eadssseaca gpqppqeate tswkieinea
      601 krrlmenill ykeekldsve lfgp
//
LOCUS       NP_112383                709 aa            linear   ROD 27-APR-2025
DEFINITION  FACT complex subunit SSRP1 [Rattus norvegicus].
ACCESSION   NP_112383 XP_342458
VERSION     NP_112383.1
DBSOURCE    REFSEQ: accession NM_031121.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Charles Richard,J.L., Shukla,M.S., Menoni,H., Ouararhni,K.,
            Lone,I.N., Roulland,Y., Papin,C., Ben Simon,E., Kundu,T.,
            Hamiche,A., Angelov,D. and Dimitrov,S.
  TITLE     FACT Assists Base Excision Repair by Boosting the Remodeling
            Activity of RSC
  JOURNAL   PLoS Genet 12 (7), e1006221 (2016)
   PUBMED   27467129
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Burgess,R.J. and Zhang,Z.
  TITLE     Histone chaperones in nucleosome assembly and human disease
  JOURNAL   Nat Struct Mol Biol 20 (1), 14-22 (2013)
   PUBMED   23288364
  REMARK    Review article
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Kwak,H. and Lis,J.T.
  TITLE     Control of transcriptional elongation
  JOURNAL   Annu Rev Genet 47, 483-508 (2013)
   PUBMED   24050178
  REMARK    Review article
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Vethantham,V., Yang,Y., Bowman,C., Asp,P., Lee,J.H., Skalnik,D.G.
            and Dynlacht,B.D.
  TITLE     Dynamic loss of H2B ubiquitylation without corresponding changes in
            H3K4 trimethylation during myogenic differentiation
  JOURNAL   Mol Cell Biol 32 (6), 1044-1055 (2012)
   PUBMED   22252316
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Winkler,D.D. and Luger,K.
  TITLE     The histone chaperone FACT: structural insights and mechanisms for
            nucleosome reorganization
  JOURNAL   J Biol Chem 286 (21), 18369-18374 (2011)
   PUBMED   21454601
  REMARK    Review article
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Todd,R.C. and Lippard,S.J.
  TITLE     Inhibition of transcription by platinum antitumor compounds
  JOURNAL   Metallomics 1 (4), 280-291 (2009)
   PUBMED   20046924
  REMARK    Review article
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Spencer,J.A., Baron,M.H. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by serum response factor and
            the high mobility group protein SSRP1
  JOURNAL   J Biol Chem 274 (22), 15686-15693 (1999)
   PUBMED   10336466
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Wang,L., Precht,P., Balakir,R. and Horton,W.E. Jr.
  TITLE     Rat and chick cDNA clones encoding HMG-like proteins
  JOURNAL   Nucleic Acids Res 21 (6), 1493 (1993)
   PUBMED   8464746
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083588.1.
            
            On Oct 11, 2004 this sequence version replaced XP_342458.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..709
                     /product="FACT complex subunit SSRP1"
                     /note="T160; recombination signal sequence recognition
                     protein 1; facilitates chromatin transcription complex
                     subunit SSRP1"
                     /calculated_mol_wt=80784
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Region          21..480
                     /region_name="POB3"
                     /note="Nucleosome-binding factor SPN, POB3 subunit
                     [Transcription / DNA replication, recombination, and
                     repair / Chromatin structure and dynamics]; COG5165"
                     /db_xref="CDD:227494"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            413
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            450..451
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and/or caspase-7.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Region          458..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04931.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            542
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Region          549..615
                     /region_name="HMG-box_SSRP1-like"
                     /note="high mobility group (HMG)-box found in
                     structure-specific recognition protein 1 (SSRP1) and
                     similar proteins; cd21994"
                     /db_xref="CDD:438810"
     Site            order(549,551..552,554..555,558..559,562,566,574..575,
                     578..579,582,585..586,607,611,615)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438810"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q08945; propagated from
                     UniProtKB/Swiss-Prot (Q04931.2)"
     CDS             1..709
                     /gene="Ssrp1"
                     /coded_by="NM_031121.1:294..2423"
                     /db_xref="GeneID:81785"
                     /db_xref="RGD:621143"
ORIGIN      
        1 maetlefndi fqevkgsmnd grlrlsrqgi ifknsktgkv dniqagelte giwrrvalgh
       61 glklltkngh vykydgfres efeklsdffk thyrlelmek dlcvkgwnwg tvkfggqlls
      121 fdigdqpvfe iplsnvsqct tgknevtlef hqnddaevsl mevrfyvppt qedgvdpvea
      181 faqnvlskad viqatgdaic ifrelqcltp rgrydiriyp tflhlhgktf dykipyttvl
      241 rlfllphkdq rqmffvisld ppikqgqtry hflillfskd edisltlnmn eeevekrfeg
      301 rltknmsgsl yemvsrvmka lvnrkitvpg nfqghsgaqc itcsykassg llyplergfi
      361 yvhkppvhir fdeisfvnfa rgttttrsfd feietkqgtq ytfssieree ygklfdfvna
      421 kklniknrgl keginpgydd yadsdedqhd aylermkeeg kireenands sddsgeetde
      481 sfnpgeeeed vaeefdsnas assssnegds dreekkrkql krakmakdrk srkkssegkk
      541 gkdpnapkrp msaymlwlna srekiksdhp gisitdlskk ageiwkgmsk ekkeewdrka
      601 edarreyeka mkeyeggrgd sskrdkskkk kkvkaklekk stpsrgsssk sssrqlsdsf
      661 kskefvssde sssgenkskk krrrsedsde eelastppss edsasgsde
//
LOCUS       NP_695221                465 aa            linear   ROD 27-APR-2025
DEFINITION  ribosomal oxygenase 2 [Rattus norvegicus].
ACCESSION   NP_695221
VERSION     NP_695221.1
DBSOURCE    REFSEQ: accession NM_153309.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Okamoto,M., Van Stry,M., Chung,L., Koyanagi,M., Sun,X., Suzuki,Y.,
            Ohara,O., Kitamura,H., Hijikata,A., Kubo,M. and Bix,M.
  TITLE     Mina, an Il4 repressor, controls T helper type 2 bias
  JOURNAL   Nat Immunol 10 (8), 872-879 (2009)
   PUBMED   19561615
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Tsuneoka,M., Koda,Y., Soejima,M., Teye,K. and Kimura,H.
  TITLE     A novel myc target gene, mina53, that is involved in cell
            proliferation
  JOURNAL   J Biol Chem 277 (38), 35450-35459 (2002)
   PUBMED   12091391
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087650.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087650.1, SRR8487227.79474.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q12"
     Protein         1..465
                     /product="ribosomal oxygenase 2"
                     /EC_number="1.14.11.79"
                     /note="Mina-53; histone lysine demethylase MINA;
                     bifunctional lysine-specific demethylase and
                     histidyl-hydroxylase MINA; MYC-induced nuclear antigen;
                     myc induced nuclear antigen"
                     /calculated_mol_wt=53085
     Region          136..261
                     /region_name="JmjC_2"
                     /note="JmjC domain; pfam08007"
                     /db_xref="CDD:462340"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IUF8; propagated from
                     UniProtKB/Swiss-Prot (Q8CFC1.1)"
     Region          332..428
                     /region_name="ROXA-like_wH"
                     /note="ROXA-like winged helix; pfam20514"
                     /db_xref="CDD:466663"
     CDS             1..465
                     /gene="Riox2"
                     /gene_synonym="Mina53"
                     /coded_by="NM_153309.2:47..1444"
                     /db_xref="GeneID:266670"
                     /db_xref="RGD:708521"
ORIGIN      
        1 mpkkvkptgd eneeesvpck qvkeelpntl svlnfdspss ffeslispik vetffkefwe
       61 qkplliqrdd pslaayyqsl fslsdlrslc sqglyygrdv nvcrciggkk kvlnkdgkaq
      121 flqlrkdfdq kratiqfhqp qrfkdelwri qeklecyfgs lvgsnvymtp agsqglpphy
      181 ddvevfilql egrkrwrlys ptvplareys vepedrigtp thdfllkpgd llyfprgtih
      241 qaetpsglah sihltistyq nnswgdylld sisglvfdia kedvalrtgm prrmlmnvet
      301 padvtrklsg flrtladqle grkellssdm kkdfvmhrlp pfcvgngtes mnpggklprl
      361 nsivrlqfkd hivltvgpdq nqsdeaqqkv vyiyhslkne rqthmmgkev eteiyglrfp
      421 lsyvdalkqi wcgspvrvkd lklgtdeeke nlavslwtec lvhvl
//
LOCUS       NP_058698                507 aa            linear   ROD 27-APR-2025
DEFINITION  erythropoietin receptor precursor [Rattus norvegicus].
ACCESSION   NP_058698
VERSION     NP_058698.2
DBSOURCE    REFSEQ: accession NM_017002.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Papic,M., Zivanovic,S., Vucicevic,T., Papic,M.V., Zdravkovic,D.,
            Milivojevic,N., Virijevic,K., Zivanovic,M., Mircic,A., Ljujic,B.,
            Lukic,M.L. and Popovic,M.
  TITLE     Pulpal expression of erythropoietin and erythropoietin receptor
            after direct pulp capping in rat
  JOURNAL   Eur J Oral Sci 130 (5), e12888 (2022)
   PUBMED   35917324
  REMARK    GeneRIF: Pulpal expression of erythropoietin and erythropoietin
            receptor after direct pulp capping in rat.
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Zhu,L., Huang,L., Wen,Q., Wang,T., Qiao,L. and Jiang,L.
  TITLE     Recombinant human erythropoietin offers neuroprotection through
            inducing endogenous erythropoietin receptor and neuroglobin in a
            neonatal rat model of periventricular white matter damage
  JOURNAL   Neurosci Lett 650, 12-17 (2017)
   PUBMED   28359933
  REMARK    GeneRIF: In conclusion, this study shows that EPOR and Ngb were
            upregulated, and both of them act as important coordinated
            neuroprotectors in rh-EPO treatment of PWMD. However, the two
            proteins exhibit different expression patterns.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Zhong,C. and Zhang,X.
  TITLE     Age-associated expression of erythropoietin and its receptor in rat
            spiral ganglion neurons and its association with neuronal apoptosis
            and hearing alterations
  JOURNAL   Mol Med Rep 15 (1), 228-234 (2017)
   PUBMED   27959434
  REMARK    GeneRIF: The present study aimed to determine the expression of
            erythropoietin (EPO) and the EPO receptor (EPOR) in spiral ganglion
            neurons (SGNs) in the inner ear of rats of various ages, and the
            associated neuronal apoptosis and hearing alterations.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Liu,F., Wei,W., Ding,J., Chen,Y., Feng,T.T., Ji,L.H. and Shi,J.Y.
  TITLE     [Influence of HIF- 2alpha on the expression of GATA- 1 in bone
            marrow CD71(+) cell of high altitude polycythemia rat model]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 37 (8), 696-701 (2016)
   PUBMED   27587253
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Hertzberg-Bigelman,E., Barashi,R., Levy,R., Cohen,L.,
            Ben-Shoshan,J., Keren,G. and Entin-Meer,M.
  TITLE     Down-Regulation of Cardiac Erythropoietin Receptor and its
            Downstream Activated Signal Transducer Phospho-STAT-5 in a Rat
            Model of Chronic Kidney Disease
  JOURNAL   Isr Med Assoc J 18 (6), 326-330 (2016)
   PUBMED   27468524
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Fujita,M., Takahashi,R., Kitada,K., Watanabe,R., Kitazawa,S.,
            Ashoori,F., Liang,P., Saya,H., Serikawa,T. and Maeda,S.
  TITLE     Alternative splicing of the erythropoietin receptor gene correlates
            with erythroid differentiation in rat hematopoietic and leukemic
            cells
  JOURNAL   Cancer Lett 112 (1), 47-55 (1997)
   PUBMED   9029168
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Longmore,G.D., Pharr,P., Neumann,D. and Lodish,H.F.
  TITLE     Both megakaryocytopoiesis and erythropoiesis are induced in mice
            infected with a retrovirus expressing an oncogenic erythropoietin
            receptor
  JOURNAL   Blood 82 (8), 2386-2395 (1993)
   PUBMED   8400289
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Masuda,S., Nagao,M., Takahata,K., Konishi,Y., Gallyas,F. Jr.,
            Tabira,T. and Sasaki,R.
  TITLE     Functional erythropoietin receptor of the cells with neural
            characteristics. Comparison with receptor properties of erythroid
            cells
  JOURNAL   J Biol Chem 268 (15), 11208-11216 (1993)
   PUBMED   7684373
REFERENCE   9  (residues 1 to 507)
  AUTHORS   de la Chapelle,A., Traskelin,A.L. and Juvonen,E.
  TITLE     Truncated erythropoietin receptor causes dominantly inherited
            benign human erythrocytosis
  JOURNAL   Proc Natl Acad Sci U S A 90 (10), 4495-4499 (1993)
   PUBMED   8506290
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Jones,S.S., D'Andrea,A.D., Haines,L.L. and Wong,G.G.
  TITLE     Human erythropoietin receptor: cloning, expression, and biologic
            characterization
  JOURNAL   Blood 76 (1), 31-35 (1990)
   PUBMED   2163696
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089810.1.
            
            On Feb 13, 2005 this sequence version replaced NP_058698.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089810.1, D13566.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..507
                     /product="erythropoietin receptor precursor"
                     /note="EPO-R"
                     /calculated_mol_wt=52776
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
                     /calculated_mol_wt=2723
     mat_peptide     25..507
                     /product="Erythropoietin receptor. /id=PRO_0000010871"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
                     /calculated_mol_wt=52776
     Region          37..139
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Site            116
                     /site_type="other"
                     /note="Required for ligand binding.
                     /evidence=ECO:0000250|UniProtKB:P19235; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Region          145..243
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          232..236
                     /region_name="WSXWS motif.
                     /evidence=ECO:0000250|UniProtKB:P14753"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Site            order(232..233,235..236)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            250..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Region          281..289
                     /region_name="Box 1 motif.
                     /evidence=ECO:0000250|UniProtKB:P16310"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Region          384..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Region          451..456
                     /region_name="ITIM motif.
                     /evidence=ECO:0000250|UniProtKB:P14753"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Region          466..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07303.1)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000250|UniProtKB:P14753; propagated from
                     UniProtKB/Swiss-Prot (Q07303.1)"
     CDS             1..507
                     /gene="Epor"
                     /coded_by="NM_017002.2:83..1606"
                     /db_xref="GeneID:24336"
                     /db_xref="RGD:2560"
ORIGIN      
        1 mdqlrvarwp rvsplcllla gaawasspsl pdpkfeskaa llasrgseel lcftqrledl
       61 vcfweeaans gmgfnysfsy qlegesrksc rlhqaptvrg smrfwcslpt adtssfvple
      121 lqvteasgsp ryhriihine vvlldapagl larraeegsh vvlrwlpppg apmtthirye
      181 vdvsagnrag gtqrvevleg rtecvlsnlr ggtrytfavr armaepsfsg fwsawsepas
      241 lltasdldpl iltlslilvl isllltvlal lshrralrqk iwpgipspen efeglftthk
      301 gnfqlwllqr dgclwwspss pfpedppahl evlserhwgv tqagdagaed kgpllepvgs
      361 eraqdtylvl dewllprcpc senlsgpgds vdpatmdegs etsscpsdla skprpegtsp
      421 ssfeytildp sskllcpral ppelpptpph lkylylvvsd sgistdyssg gsqgvhgdss
      481 dgpyshpyen slvpdteplr psyvacs
//
LOCUS       NP_001012762             477 aa            linear   ROD 27-APR-2025
DEFINITION  ectonucleotide pyrophosphatase/phosphodiesterase family member 5
            precursor [Rattus norvegicus].
ACCESSION   NP_001012762 XP_236956
VERSION     NP_001012762.1
DBSOURCE    REFSEQ: accession NM_001012744.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Ohe,Y., Ohnishi,H., Okazawa,H., Tomizawa,K., Kobayashi,H., Okawa,K.
            and Matozaki,T.
  TITLE     Characterization of nucleotide pyrophosphatase-5 as an
            oligomannosidic glycoprotein in rat brain
  JOURNAL   Biochem Biophys Res Commun 308 (4), 719-725 (2003)
   PUBMED   12927778
  REMARK    GeneRIF: NPP-5 is a neural oligomannosidic glycoprotein that may
            participate in neural cell communications.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090331.1.
            
            On Apr 20, 2005 this sequence version replaced XP_236956.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMD00132299
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..477
                     /product="ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 5 precursor"
                     /EC_number="3.6.1.29"
                     /note="NPP-5; E-NPP5; ectonucleotide
                     pyrophosphatase/phosphodiesterase 5"
                     /calculated_mol_wt=51736
     sig_peptide     1..24
                     /note="/evidence=ECO:0000269|PubMed:12927778; propagated
                     from UniProtKB/Swiss-Prot (P84039.2)"
                     /calculated_mol_wt=2572
     mat_peptide     25..477
                     /product="Ectonucleotide pyrophosphatase/phosphodiesterase
                     family member 5. /id=PRO_0000188572"
                     /note="propagated from UniProtKB/Swiss-Prot (P84039.2)"
                     /calculated_mol_wt=51736
     Region          28..382
                     /region_name="Enpp"
                     /note="Ectonucleotide pyrophosphatase/phosphodiesterase,
                     also called autotaxin; cd16018"
                     /db_xref="CDD:293742"
     Site            order(36,71..72,93,191,195,238..239,339)
                     /site_type="active"
                     /db_xref="CDD:293742"
     Site            order(36,71..72,93,191,195,239,339)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293742"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            364..366
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293742"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:12927778; propagated from
                     UniProtKB/Swiss-Prot (P84039.2)"
     Site            432..452
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P84039.2)"
     CDS             1..477
                     /gene="Enpp5"
                     /gene_synonym="E-NPP 5; Npp5"
                     /coded_by="NM_001012744.1:99..1532"
                     /db_xref="GeneID:316249"
                     /db_xref="RGD:1359199"
ORIGIN      
        1 mipeflvvsc tlaalchsvp lslqteqqkv lvvsfdgfrw dylykvptph fhyvmkngvh
       61 vkqvtnvfit ktypnhytlv tglfaenhgi vandmfdpvl nksfslehmn iydskfweea
      121 tplwitnqra ghasgaamwp gtdvkihesy pthylpynes vsfedrvaki iewftakdpi
      181 nlgflyweep ddtghdvgpd splmgpvisd idhklgylik mlkkaklwnn inlivtsdhg
      241 mtqcskervi eldqyldkeh ytlidhspva ailpkegkfn evydalanah pnltvykkee
      301 iperwhykhs drvqpivava degwyilqnk sdefllgnhg ydnalaemhp iflahgpafr
      361 knftkeamns tdlyslvchl lnvtalphng sfrnvqdlls saapkaipyt qsttlplgsa
      421 kpgeyeqees ypyyigislg sliaivffvv likhlirsqm htlqymqvev aqpllqa
//
LOCUS       NP_037300                361 aa            linear   ROD 27-APR-2025
DEFINITION  porphobilinogen deaminase [Rattus norvegicus].
ACCESSION   NP_037300
VERSION     NP_037300.2
DBSOURCE    REFSEQ: accession NM_013168.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Loskove,Y., Yasuda,M., Chen,B., Nazarenko,I., Cody,N. and
            Desnick,R.J.
  TITLE     Acute hepatic porphyrias: Identification of 46 hydroxymethylbilane
            synthase, 11 coproporphyrinogen oxidase, and 20 protoporphyrinogen
            oxidase novel mutations
  JOURNAL   Mol Genet Metab 128 (3), 352-357 (2019)
   PUBMED   30385147
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Yasuda,M., Gan,L., Chen,B., Yu,C., Zhang,J., Gama-Sosa,M.A.,
            Pollak,D.D., Berger,S., Phillips,J.D., Edelmann,W. and Desnick,R.J.
  TITLE     Homozygous hydroxymethylbilane synthase knock-in mice provide
            pathogenic insights into the severe neurological impairments
            present in human homozygous dominant acute intermittent porphyria
  JOURNAL   Hum Mol Genet 28 (11), 1755-1767 (2019)
   PUBMED   30615115
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Jiang,L., Berraondo,P., Jerico,D., Guey,L.T., Sampedro,A.,
            Frassetto,A., Benenato,K.E., Burke,K., Santamaria,E., Alegre,M.,
            Pejenaute,A., Kalariya,M., Butcher,W., Park,J.S., Zhu,X.,
            Sabnis,S., Kumarasinghe,E.S., Salerno,T., Kenney,M., Lukacs,C.M.,
            Avila,M.A., Martini,P.G.V. and Fontanellas,A.
  TITLE     Systemic messenger RNA as an etiological treatment for acute
            intermittent porphyria
  JOURNAL   Nat Med 24 (12), 1899-1909 (2018)
   PUBMED   30297912
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Serrano-Mendioroz,I., Sampedro,A., Alegre,M., Enriquez de
            Salamanca,R., Berraondo,P. and Fontanellas,A.
  TITLE     An Inducible Promoter Responsive to Different Porphyrinogenic
            Stimuli Improves Gene Therapy Vectors for Acute Intermittent
            Porphyria
  JOURNAL   Hum Gene Ther 29 (4), 480-491 (2018)
   PUBMED   28990424
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Barupala,D.P., Dzul,S.P., Riggs-Gelasco,P.J. and Stemmler,T.L.
  TITLE     Synthesis, delivery and regulation of eukaryotic heme and Fe-S
            cluster cofactors
  JOURNAL   Arch Biochem Biophys 592, 60-75 (2016)
   PUBMED   26785297
  REMARK    Review article
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Van Hillegersberg,R., Van den Berg,J.W., Kort,W.J., Terpstra,O.T.
            and Wilson,J.H.
  TITLE     Selective accumulation of endogenously produced porphyrins in a
            liver metastasis model in rats
  JOURNAL   Gastroenterology 103 (2), 647-651 (1992)
   PUBMED   1386052
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Piper,W.N. and Van Lier,B.L.
  TITLE     Pteridine regulation of inhibition of hepatic uroporphyrinogen L
            synthetase activity by lead chloride
  JOURNAL   Mol Pharmacol 13 (6), 1126-1135 (1977)
   PUBMED   593266
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Anderson,K.E., Sassa,S., Peterson,C.M. and Kappas,A.
  TITLE     Increased erythrocyte uroporphyrinogen-l-synthetase,
            delta-aminolevulinic acid dehydratase and protoporphyrin in
            hemolytic anemias
  JOURNAL   Am J Med 63 (3), 359-364 (1977)
   PUBMED   900140
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Piper,W.N. and Van Lier,R.B.
  TITLE     Isolation of a factor that protects against lead inhibition of
            hepatic and erythrocytic uroporphyrinogen I synthetase activity
  JOURNAL   Life Sci 19 (8), 1225-1234 (1976)
   PUBMED   994723
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Woods,J.S.
  TITLE     Developmental aspects of hepatic heme biosynthetic capability and
            hematotoxicity
  JOURNAL   Biochem Pharmacol 25 (19), 2147-2152 (1976)
   PUBMED   971328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC088162.1.
            
            On Oct 28, 2005 this sequence version replaced NP_037300.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088162.1, SRR8487226.42182.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..361
                     /product="porphobilinogen deaminase"
                     /EC_number="2.5.1.61"
                     /note="alternative name: porphobilinogen deaminase;
                     pre-uroporphyrinogen synthase; uroporphyrinogen I
                     synthase"
                     /calculated_mol_wt=39230
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P08397; propagated from
                     UniProtKB/Swiss-Prot (P19356.2)"
     Region          20..299
                     /region_name="PBP2_HuPBGD_like"
                     /note="Human porphobilinogen deaminase possess type 2
                     periplasmic binding protein fold; cd13645"
                     /db_xref="CDD:270363"
     Site            order(26,30,77,98..99,145..147,149..150,166..170,173,214,
                     261)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270363"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08397; propagated from
                     UniProtKB/Swiss-Prot (P19356.2)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P22907; propagated from
                     UniProtKB/Swiss-Prot (P19356.2)"
     Site            order(116,194,203,205,271..272)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270363"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08397; propagated from
                     UniProtKB/Swiss-Prot (P19356.2)"
     CDS             1..361
                     /gene="Hmbs"
                     /gene_synonym="hemC; PBG-D; PBGD; URO-S"
                     /coded_by="NM_013168.2:131..1216"
                     /db_xref="GeneID:25709"
                     /db_xref="RGD:2801"
ORIGIN      
        1 msgnggaatt aeengsmmrv irvgtrksql ariqtdtvva mlktlypgiq feiiamsttg
       61 dkildtalsk igekslftke lenaleknev dlvvhslkdv ptilppgfti gaickrenpc
      121 davvfhpkfi gktletlpek savgtsslrr vaqlqrkfph lefksirgnl ntrlrkldel
      181 qefsaiilav aglqrmgwqn rvgqilhpee cmyavgqgal avevrakdqd ildlvgvlhd
      241 petllrciae raflrhlegg csvpvavhtv mkdgqlyltg gvwsldgsds mqetmqatiq
      301 vpvqqedgpe ddpqlvgita rniprgaqla aenlgislas lllnkgakni ldvarqlndv
      361 r
//
LOCUS       NP_001139314             524 aa            linear   ROD 27-APR-2025
DEFINITION  progranulin isoform b precursor [Rattus norvegicus].
ACCESSION   NP_001139314
VERSION     NP_001139314.1
DBSOURCE    REFSEQ: accession NM_001145842.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Liao,A., Zheng,W., Wang,S., Wang,N., Li,Y., Chen,D. and Wang,Y.
  TITLE     Sortilin is associated with progranulin deficiency and autism-like
            behaviors in valproic acid-induced autism rats
  JOURNAL   CNS Neurosci Ther 30 (9), e70015 (2024)
   PUBMED   39218796
  REMARK    GeneRIF: Sortilin is associated with progranulin deficiency and
            autism-like behaviors in valproic acid-induced autism rats.
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Horinokita,I., Hayashi,H., Oteki,R., Mizumura,R., Yamaguchi,T.,
            Usui,A., Yuan,B. and Takagi,N.
  TITLE     Involvement of Progranulin and Granulin Expression in Inflammatory
            Responses after Cerebral Ischemia
  JOURNAL   Int J Mol Sci 20 (20), 5210 (2019)
   PUBMED   31640144
  REMARK    GeneRIF: Study demonstrated that the level of PGRN protein in the
            cerebral cortex was significantly increased after
            microsphere-induced cerebral embolism (ME). Furthermore, PGRN was
            expressed in the microglia of the ipsilateral hemisphere after ME.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Wang,S., Wei,J., Fan,Y., Ding,H., Tian,H., Zhou,X. and Cheng,L.
  TITLE     Progranulin Is Positively Associated with Intervertebral Disc
            Degeneration by Interaction with IL-10 and IL-17 Through TNF
            Pathways
  JOURNAL   Inflammation 41 (5), 1852-1863 (2018)
   PUBMED   29992506
  REMARK    GeneRIF: PGRN is associated with intervertebral disc degeneration
            through interfering with IL-10 and IL-17
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Chen,L., Li,Q., Wang,J., Jin,S., Zheng,H., Lin,J., He,F., Zhang,H.,
            Ma,S., Mei,J. and Yu,J.
  TITLE     MiR-29b-3p promotes chondrocyte apoptosis and facilitates the
            occurrence and development of osteoarthritis by targeting PGRN
  JOURNAL   J Cell Mol Med 21 (12), 3347-3359 (2017)
   PUBMED   28609022
  REMARK    GeneRIF: MiR-29b-3p promotes chondrocyte apoptosis and facilitates
            the occurrence and development of osteoarthritis by targeting PGRN.
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Lee,C.W., Stankowski,J.N., Chew,J., Cook,C.N., Lam,Y.W.,
            Almeida,S., Carlomagno,Y., Lau,K.F., Prudencio,M., Gao,F.B.,
            Bogyo,M., Dickson,D.W. and Petrucelli,L.
  TITLE     The lysosomal protein cathepsin L is a progranulin protease
  JOURNAL   Mol Neurodegener 12 (1), 55 (2017)
   PUBMED   28743268
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Suzuki,M., Bannai,M., Matsumuro,M., Furuhata,Y., Ikemura,R.,
            Kuranaga,E., Kaneda,Y., Nishihara,M. and Takahashi,M.
  TITLE     Suppression of copulatory behavior by intracerebroventricular
            infusion of antisense oligodeoxynucleotide of granulin in neonatal
            male rats
  JOURNAL   Physiol Behav 68 (5), 707-713 (2000)
   PUBMED   10764901
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Bhandari,V., Giaid,A. and Bateman,A.
  TITLE     The complementary deoxyribonucleic acid sequence, tissue
            distribution, and cellular localization of the rat granulin
            precursor
  JOURNAL   Endocrinology 133 (6), 2682-2689 (1993)
   PUBMED   8243292
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Plowman,G.D., Green,J.M., Neubauer,M.G., Buckley,S.D.,
            McDonald,V.L., Todaro,G.J. and Shoyab,M.
  TITLE     The epithelin precursor encodes two proteins with opposing
            activities on epithelial cell growth
  JOURNAL   J Biol Chem 267 (18), 13073-13078 (1992)
   PUBMED   1618805
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Bateman,A., Belcourt,D., Bennett,H., Lazure,C. and Solomon,S.
  TITLE     Granulins, a novel class of peptide from leukocytes
  JOURNAL   Biochem Biophys Res Commun 173 (3), 1161-1168 (1990)
   PUBMED   2268320
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Shoyab,M., McDonald,V.L., Byles,C., Todaro,G.J. and Plowman,G.D.
  TITLE     Epithelins 1 and 2: isolation and characterization of two
            cysteine-rich growth-modulating proteins
  JOURNAL   Proc Natl Acad Sci U S A 87 (20), 7912-7916 (1990)
   PUBMED   2236009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB731349.1 and BC072469.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The resulting
            isoform (b) is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072469.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..524
                     /product="progranulin isoform b precursor"
                     /note="granulins; acrogranin; progranulin; proepithelin;
                     prostate cancer cell-derived growth factor; epithelin"
                     /calculated_mol_wt=53150
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3517
     Region          79..125
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          140..190
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          222..272
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          296..346
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          388..429
                     /region_name="Granulin"
                     /note="pfam00396"
                     /db_xref="CDD:459799"
     Region          463..504
                     /region_name="Granulin"
                     /note="pfam00396"
                     /db_xref="CDD:459799"
     CDS             1..524
                     /gene="Grn"
                     /gene_synonym="PEPI; PGRN"
                     /coded_by="NM_001145842.1:18..1592"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29143"
                     /db_xref="RGD:61983"
ORIGIN      
        1 mpprergprr rqtmwilvsw lalvarlvag tqcpdgqfcp vaccldqgga nysccnplld
       61 twpiitsrrl dgscqirdhc pdgysclltv sgtssccpfs egvscddgqh ccprgfhcsv
      121 dgkscsqisd sllgavqcpg sqfecpdsat ccimidgswg ccpmpqascc edrvhccphg
      181 ascdlvhtrc isptgthpll kkfpaqrtnr avafpfsvvc pdaktqcpdd stccelptgk
      241 ygccpmpnai ccsdhlhccp qdtvcdliqs kciskdyttd lmtklpgypv nevkcdlevs
      301 cpdgytccrl ntgawgccpf tkavccedhi hccpagfqch tetgtcelgv lqvpwmkkvt
      361 aslslpdpqi lkndvpcddf sscpsnntcc rlssgdwgcc pipeavcced rqhccpagyt
      421 cnvkartcek dagsvqpsmd ltfgskvgnv ecgaghfchd nqscckdsqg gwaccpyvkg
      481 vccrdgrhcc pigfhcsakg tkclrkktpr wdillrdpap rpll
//
LOCUS       NP_001013975             202 aa            linear   ROD 27-APR-2025
DEFINITION  dynein regulatory complex protein 12 [Rattus norvegicus].
ACCESSION   NP_001013975 XP_238539
VERSION     NP_001013975.1
DBSOURCE    REFSEQ: accession NM_001013953.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089910.1.
            
            On Apr 20, 2005 this sequence version replaced XP_238539.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089910.1, CF115111.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..202
                     /product="dynein regulatory complex protein 12"
                     /note="coiled-coil domain-containing protein 153;
                     coiled-coil domain containing 153"
                     /calculated_mol_wt=23276
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVL4.1)"
     Region          <28..>158
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..202
                     /gene="Drc12"
                     /gene_synonym="Ccdc153; RGD1305351"
                     /coded_by="NM_001013953.1:316..924"
                     /db_xref="GeneID:300663"
                     /db_xref="RGD:1305351"
ORIGIN      
        1 mppktkgkgr kaatrkkkkn sspgveaeak hrlvllekel lqdhlalqre eacrakased
       61 rlkqrlqgle aelertqseg ravyaemsrq rqalqkelgt rskrleeevr glrerletcq
      121 reaktareea eralreqdgt ltelrahvah meakyeeilh dnlncllakl ravkpqwdaa
      181 tlrlhtrhke qlrrfglnpl dl
//
LOCUS       NP_067686                333 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction alpha-4 protein [Rattus norvegicus].
ACCESSION   NP_067686
VERSION     NP_067686.1
DBSOURCE    REFSEQ: accession NM_021654.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Taylor,S.Z., Jacobsen,N.L., Pontifex,T.K., Langlais,P. and
            Burt,J.M.
  TITLE     Serine 319 phosphorylation is necessary and sufficient to induce a
            Cx37 conformation that leads to arrested cell cycling
  JOURNAL   J Cell Sci 133 (12) (2020)
   PUBMED   32350069
  REMARK    GeneRIF: Serine 319 phosphorylation is necessary and sufficient to
            induce a Cx37 conformation that leads to arrested cell cycling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Guo,S., Yang,Y., Yang,Z., You,H., Shi,Y., Hu,Z., Meng,Z. and
            Xiao,J.
  TITLE     Improving myocardial fractional flow reserve in coronary
            atherosclerosis via CX37 gene silence: a preclinical validation
            study in pigs
  JOURNAL   Interact Cardiovasc Thorac Surg 26 (1), 139-145 (2018)
   PUBMED   29049831
  REMARK    GeneRIF: FFR levels increased along with decreased doses of siRNA
            CX37 lentivirus, indicating that siRNA CX37 lentivirus may reduce
            the risk of coronary atherosclerosis and provide a potential
            approach to treat coronary heart disease.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Jacobsen,N.L., Pontifex,T.K., Li,H., Solan,J.L., Lampe,P.D.,
            Sorgen,P.L. and Burt,J.M.
  TITLE     Regulation of Cx37 channel and growth-suppressive properties by
            phosphorylation
  JOURNAL   J Cell Sci 130 (19), 3308-3321 (2017)
   PUBMED   28818996
  REMARK    GeneRIF: Substituting alanine at serine residues 275, 302 and 328
            eliminated Cx37-induced cell death, supported proliferation and
            reduced the GJCh closed state probability.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Good,M.E., Ek-Vitorin,J.F. and Burt,J.M.
  TITLE     Structural determinants and proliferative consequences of connexin
            37 hemichannel function in insulinoma cells
  JOURNAL   J Biol Chem 289 (44), 30379-30386 (2014)
   PUBMED   25217644
  REMARK    GeneRIF: Cx37-N55I and -Q58L mutations formed hemichannels with
            behavior and permeation properties similar to Cx37-WT (especially
            Q58L), but none of the mutants suppressed rat insulinoma cell
            proliferation.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Ganesan,S. and Keating,A.F.
  TITLE     Impact of 7,12-dimethylbenz[a]anthracene exposure on connexin gap
            junction proteins in cultured rat ovaries
  JOURNAL   Toxicol Appl Pharmacol 274 (2), 209-214 (2014)
   PUBMED   24269759
  REMARK    GeneRIF: 7,12-Dimethylbenz[a]anthracene increases Cx37 and Cx43
            expression prior to follicle loss and during follicle loss both
            Cx37 and Cx43 expressions are reduced in cultured rat ovaries.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Lin,S.H., Lu,C.Y., Muhammad,R., Chou,W.Y., Lin,F.C., Wu,P.C.,
            Lin,C.R. and Yang,L.C.
  TITLE     Induction of connexin 37 expression in a rat model of neuropathic
            pain
  JOURNAL   Brain Res Mol Brain Res 99 (2), 134-140 (2002)
   PUBMED   11978404
  REMARK    GeneRIF: Upregulation of connexin 37 mRNA after sciatic nerve
            injury causes thermal hyperalgesia; gap junctions thus may be
            responsible for this hyperexcitability.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Yeh,H.I., Lai,Y.J., Chang,H.M., Ko,Y.S., Severs,N.J. and Tsai,C.H.
  TITLE     Multiple connexin expression in regenerating arterial endothelial
            gap junctions
  JOURNAL   Arterioscler Thromb Vasc Biol 20 (7), 1753-1762 (2000)
   PUBMED   10894813
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Yeh,H.I., Rothery,S., Dupont,E., Coppen,S.R. and Severs,N.J.
  TITLE     Individual gap junction plaques contain multiple connexins in
            arterial endothelium
  JOURNAL   Circ Res 83 (12), 1248-1263 (1998)
   PUBMED   9851942
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Vrionis,F.D., Wu,J.K., Qi,P., Waltzman,M., Cherington,V. and
            Spray,D.C.
  TITLE     The bystander effect exerted by tumor cells expressing the herpes
            simplex virus thymidine kinase (HSVtk) gene is dependent on
            connexin expression and cell communication via gap junctions
  JOURNAL   Gene Ther 4 (6), 577-585 (1997)
   PUBMED   9231074
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Haefliger,J.A., Bruzzone,R., Jenkins,N.A., Gilbert,D.J.,
            Copeland,N.G. and Paul,D.L.
  TITLE     Four novel members of the connexin family of gap junction proteins.
            Molecular cloning, expression, and chromosome mapping
  JOURNAL   J Biol Chem 267 (3), 2057-2064 (1992)
   PUBMED   1370487
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078837.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078837.1, EX490393.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN16093043
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..333
                     /product="gap junction alpha-4 protein"
                     /note="cx37; connexin-37; Gap junction membrane channel,
                     protein alpha 4 (connexin 37); connexin h1; gap junction
                     membrane channel protein alpha 4"
                     /calculated_mol_wt=37425
     Region          3..220
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03190.2)"
     Site            77..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03190.2)"
     Site            149..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03190.2)"
     Site            209..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03190.2)"
     Region          292..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03190.2)"
     CDS             1..333
                     /gene="Gja4"
                     /gene_synonym="CXN37; Cxnh1"
                     /coded_by="NM_021654.2:78..1079"
                     /db_xref="GeneID:25655"
                     /db_xref="RGD:2691"
ORIGIN      
        1 mgdwgflekl ldqvqehstv vgkiwltvlf ifrililgla gesvwgdeqs dfecntaqpg
       61 ctnvcydqaf pishirywvl qflfvstptl iylghviyls rreerlrqke gelralpskd
      121 phveralaai ehqmakisva edgrlrirga lmgtyvisvl cksvleagfl ygqwrlygwt
      181 mepvfvcqra pcphvvdcyv srptektifi ifmlvvgvis lvlnllelvh llcrcvsrei
      241 karrdhdtrp aqgsasdpyp eqvffylpmg egpssppcpt ynglssteqn wanltteerl
      301 tstrpppfvn aapqggqkss srpnssaskk qyv
//
LOCUS       NP_001099604             254 aa            linear   ROD 27-APR-2025
DEFINITION  SKA complex subunit 1 [Rattus norvegicus].
ACCESSION   NP_001099604 XP_001053750 XP_214527
VERSION     NP_001099604.1
DBSOURCE    REFSEQ: accession NM_001106134.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Yao,C., Wang,Q., Wang,Y., Wu,J., Cao,X., Lu,Y., Chen,Y., Feng,W.,
            Gu,X., Dun,X.P. and Yu,B.
  TITLE     Loc680254 regulates Schwann cell proliferation through Psrc1 and
            Ska1 as a microRNA sponge following sciatic nerve injury
  JOURNAL   Glia 69 (10), 2391-2403 (2021)
   PUBMED   34115425
  REMARK    GeneRIF: Loc680254 regulates Schwann cell proliferation through
            Psrc1 and Ska1 as a microRNA sponge following sciatic nerve injury.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Welburn,J.P., Grishchuk,E.L., Backer,C.B., Wilson-Kubalek,E.M.,
            Yates,J.R. 3rd and Cheeseman,I.M.
  TITLE     The human kinetochore Ska1 complex facilitates microtubule
            depolymerization-coupled motility
  JOURNAL   Dev Cell 16 (3), 374-385 (2009)
   PUBMED   19289083
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Rines,D.R., Gomez-Ferreria,M.A., Zhou,Y., DeJesus,P., Grob,S.,
            Batalov,S., Labow,M., Huesken,D., Mickanin,C., Hall,J.,
            Reinhardt,M., Natt,F., Lange,J., Sharp,D.J., Chanda,S.K. and
            Caldwell,J.S.
  TITLE     Whole genome functional analysis identifies novel components
            required for mitotic spindle integrity in human cells
  JOURNAL   Genome Biol 9 (2), R44 (2008)
   PUBMED   18302737
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Hanisch,A., Sillje,H.H. and Nigg,E.A.
  TITLE     Timely anaphase onset requires a novel spindle and kinetochore
            complex comprising Ska1 and Ska2
  JOURNAL   EMBO J 25 (23), 5504-5515 (2006)
   PUBMED   17093495
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474095.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001053750.1, XP_214527.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158659.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..254
                     /product="SKA complex subunit 1"
                     /note="spindle and kinetochore-associated protein 1"
                     /calculated_mol_wt=29290
     Site            order(3..5,8)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:214021"
     Site            order(5,8..9,12,16,19..20,23,26..27,34,37..38,41,44..45,
                     47..48,51..52,54..55,58,61..62,65,69,72,76)
                     /site_type="other"
                     /note="SKA3 interface [polypeptide binding]"
                     /db_xref="CDD:214021"
     Site            order(11,15,18..19,22..23,25..26,29,41,45,48..49,52..53,
                     55..56,59,62,66,69..70,72..73,76)
                     /site_type="other"
                     /note="SKA2 interface [polypeptide binding]"
                     /db_xref="CDD:214021"
     Region          15..247
                     /region_name="SKA1"
                     /note="Spindle and kinetochore-associated protein 1;
                     pfam07160"
                     /db_xref="CDD:462107"
     Region          91..131
                     /region_name="Flexiple loop that anchors MAPRE1.
                     /evidence=ECO:0000250|UniProtKB:Q96BD8"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN28.1)"
     Region          92..95
                     /region_name="SXLP motif, mediates interaction with
                     MAPRE1, targeting to microtubule plus ends, stabilization
                     on kinetochores and is required for proper chromosome
                     alignment to the metaphase plate.
                     /evidence=ECO:0000250|UniProtKB:Q96BD8"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN28.1)"
     Region          97..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN28.1)"
     Region          131..254
                     /region_name="Binds microtubules and protein phosphatase
                     PP1 subunit PPP1CA.
                     /evidence=ECO:0000250|UniProtKB:Q96BD8"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN28.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96BD8; propagated from
                     UniProtKB/Swiss-Prot (B0BN28.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BD8; propagated from
                     UniProtKB/Swiss-Prot (B0BN28.1)"
     CDS             1..254
                     /gene="Ska1"
                     /gene_synonym="RGD1310784"
                     /coded_by="NM_001106134.1:196..960"
                     /db_xref="GeneID:291441"
                     /db_xref="RGD:1310784"
ORIGIN      
        1 masdleqlcs yvnekienik kilslrklgq dptlkttlsk igdeiitvne llnqfeleiq
       61 yqeqtnsslk elcksleeef kdvehlkehi pshlpqvtvt qssthkpdld pkesvkaeep
      121 vlpkkppkeq rvikemhfit tdefsgvpay mksrltycqi ndvikeinka vvskykiihq
      181 pkasmssvkr nlyqrfinee tkdtkgrhfi veadikeftt lkvdkkfhvi mnilrhcqrl
      241 sevrgggltr yvit
//
LOCUS       NP_476480                798 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein U [Rattus norvegicus].
ACCESSION   NP_476480 XP_346452
VERSION     NP_476480.2
DBSOURCE    REFSEQ: accession NM_057139.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Liu,J., Ma,X., Guo,W., Lu,B., Yue,Y., Yang,X., Wang,R., Wu,C.,
            Zhang,B., Li,X. and Luo,X.
  TITLE     Deacetylation of HnRNP U mediated by sirtuin1 ameliorates aged rat
            with liver fibrosis via inhibiting p53-related senescence and
            NLRP3-related inflammation
  JOURNAL   Int Immunopharmacol 141, 113026 (2024)
   PUBMED   39216234
  REMARK    GeneRIF: Deacetylation of HnRNP U mediated by sirtuin1 ameliorates
            aged rat with liver fibrosis via inhibiting p53-related senescence
            and NLRP3-related inflammation.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Miyaji,M., Kawano,S., Furuta,R., Murakami,E., Ikeda,S.,
            Tsutsui,K.M. and Tsutsui,K.
  TITLE     Selective DNA-binding of SP120 (rat ortholog of human hnRNP U) is
            mediated by arginine-glycine rich domain and modulated by RNA
  JOURNAL   PLoS One 18 (8), e0289599 (2023)
   PUBMED   37540655
  REMARK    GeneRIF: Selective DNA-binding of SP120 (rat ortholog of human
            hnRNP U) is mediated by arginine-glycine rich domain and modulated
            by RNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Qu,J., Xiong,X., Hujie,G., Ren,J., Yan,L. and Ma,L.
  TITLE     MicroRNA-132-3p alleviates neuron apoptosis and impairments of
            learning and memory abilities in Alzheimer's disease by
            downregulation of HNRNPU stabilized BACE1
  JOURNAL   Cell Cycle 20 (21), 2309-2320 (2021)
   PUBMED   34585626
  REMARK    GeneRIF: MicroRNA-132-3p alleviates neuron apoptosis and
            impairments of learning and memory abilities in Alzheimer's disease
            by downregulation of HNRNPU stabilized BACE1.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Majewski,L., Nowak,J., Sobczak,M., Karatsai,O., Havrylov,S.,
            Lenartowski,R., Suszek,M., Lenartowska,M. and Redowicz,M.J.
  TITLE     Myosin VI in the nucleus of neurosecretory PC12 cells:
            Stimulation-dependent nuclear translocation and interaction with
            nuclear proteins
  JOURNAL   Nucleus 9 (1), 125-141 (2018)
   PUBMED   29293066
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Li,S., Mi,L., Yu,L., Yu,Q., Liu,T., Wang,G.X., Zhao,X.Y., Wu,J. and
            Lin,J.D.
  TITLE     Zbtb7b engages the long noncoding RNA Blnc1 to drive brown and
            beige fat development and thermogenesis
  JOURNAL   Proc Natl Acad Sci U S A 114 (34), E7111-E7120 (2017)
   PUBMED   28784777
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Malik,K.F., Jaffe,H., Brady,J. and Young,W.S. 3rd.
  TITLE     The class III POU factor Brn-4 interacts with other class III POU
            factors and the heterogeneous nuclear ribonucleoprotein U
  JOURNAL   Brain Res Mol Brain Res 45 (1), 99-107 (1997)
   PUBMED   9105675
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Jordan,P., Heid,H., Kinzel,V. and Kubler,D.
  TITLE     Major cell surface-located protein substrates of an ecto-protein
            kinase are homologs of known nuclear proteins
  JOURNAL   Biochemistry 33 (49), 14696-14706 (1994)
   PUBMED   7993898
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Fackelmayer,F.O. and Richter,A.
  TITLE     Purification of two isoforms of hnRNP-U and characterization of
            their nucleic acid binding activity
  JOURNAL   Biochemistry 33 (34), 10416-10422 (1994)
   PUBMED   8068679
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Fackelmayer,F.O., Dahm,K., Renz,A., Ramsperger,U. and Richter,A.
  TITLE     Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix
            protein which binds DNA and RNA in vivo and in vitro
  JOURNAL   Eur J Biochem 221 (2), 749-757 (1994)
   PUBMED   8174554
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Kiledjian,M. and Dreyfuss,G.
  TITLE     Primary structure and binding activity of the hnRNP U protein:
            binding RNA through RGG box
  JOURNAL   EMBO J 11 (7), 2655-2664 (1992)
   PUBMED   1628625
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072529.1.
            
            On Jun 10, 2007 this sequence version replaced NP_476480.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072529.1, D14048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q25"
     Protein         1..798
                     /product="heterogeneous nuclear ribonucleoprotein U"
                     /note="system N1 Na+ and H+-coupled glutamine transporter;
                     transporter protein; transporter protein; system N1 Na+
                     and H+-coupled glutamine transporter; scaffold-attachment
                     factor A"
                     /calculated_mol_wt=87602
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          8..42
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          41..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            94..95
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          262..437
                     /region_name="SPRY_hnRNP"
                     /note="SPRY domain in heterogeneous nuclear
                     ribonucleoprotein U-like (hnRNP) protein 1; cd12884"
                     /db_xref="CDD:293942"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          462..646
                     /region_name="ATPase domain.
                     /evidence=ECO:0000250|UniProtKB:Q00839"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          473..617
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Site            490
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            498
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            525
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            539
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          585..600
                     /region_name="Actin-binding.
                     /evidence=ECO:0000250|UniProtKB:Q00839"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            609
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          645..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            676
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          688..713
                     /region_name="RNA-binding RGG-box.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            689
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            694
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            701
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            707
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8VEK3; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            713
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            728
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            735
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Region          743..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY8.1)"
     Site            787
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q00839; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY8.1)"
     CDS             1..798
                     /gene="Hnrnpu"
                     /gene_synonym="hnRNP U; Hnrpu; SAF-A; SN1; SP120"
                     /coded_by="NM_057139.2:168..2564"
                     /db_xref="GeneID:117280"
                     /db_xref="RGD:620372"
ORIGIN      
        1 mssspvnvkk lkvselkeel kkrrlsdkgl kadlmdrlqa aldneaggrp amepgngsld
       61 lggdaagrsg agleqeaaag aeddeeeegi aaldgdqmel geengaagaa dagameeeea
      121 asedengddq gfqegedelg deeegagden ghgeqqsqpp aaaqqasqqr gpgkeaagks
      181 sgptslfavt vappgarqgq qqaggdgkte qkagdkkrgv krpredhgrg yfeyieenky
      241 srakspqppv eeedehfddt vvcldtyncd lhfkisrdrl sassltmesf aflwaggras
      301 ygvskgkvcf emkvtekipv rhlytkdidi hevrigwslt tsgmllgeee fsygyslkgi
      361 ktcncetedy gekfdendvi tcfanfetde velsyakngq dlgvafkisk evladrplfp
      421 hvlchncave fnfgqkekpy fpipedctfi qnvpledrvr gpkgpeekkd cevvmmiglp
      481 gagkttwvtk haaenpgkyn ilgtntimdk mmvagfkkqm adtgklntll qrapqclgkf
      541 ieiaarkkrn fildqtnvsa aaqrrkmclf agfqrkavvv cpkdedykqr tqkkaevegk
      601 dlpehavlkm kgnftlpeva ecfdeityve lqkeeaqkll eqykeeskka lppekkqntg
      661 skksnknksg knqfnrgggh rgrggfnmrg gnfrggapgn rggynrrgnm pqrgggggsg
      721 gigypyprgp vfpgrggysn rgnynrggmp nrgnynqnfr grgnnrgykn qsqgynqwqq
      781 gqfwgqkpws qhyhqgyy
//
LOCUS       NP_001028825            1607 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 12 isoform beta [Rattus norvegicus].
ACCESSION   NP_001028825
VERSION     NP_001028825.1
DBSOURCE    REFSEQ: accession NM_001033653.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1607)
  AUTHORS   Selvaraju,V., Suresh,S.C., Thirunavukkarasu,M., Mannu,J.,
            Foye,J.L.C., Mathur,P.P., Palesty,J.A., Sanchez,J.A., McFadden,D.W.
            and Maulik,N.
  TITLE     Regulation of A-Kinase-Anchoring Protein 12 by Heat Shock Protein
            A12B to Prevent Ventricular Dysfunction Following Acute Myocardial
            Infarction in Diabetic Rats
  JOURNAL   J Cardiovasc Transl Res 10 (2), 209-220 (2017)
   PUBMED   28281242
  REMARK    GeneRIF: HSPA12B overexpression interacts with AKAP12 and
            downregulate TXNIP in diabetic rats following acute myocardial
            infarction.
REFERENCE   2  (residues 1 to 1607)
  AUTHORS   Wilhelm,T., Lipka,D.B., Witte,T., Wierzbinska,J.A., Fluhr,S.,
            Helf,M., Mucke,O., Claus,R., Konermann,C., Nollke,P.,
            Niemeyer,C.M., Flotho,C. and Plass,C.
  TITLE     Epigenetic silencing of AKAP12 in juvenile myelomonocytic leukemia
  JOURNAL   Epigenetics 11 (2), 110-119 (2016)
   PUBMED   26891149
REFERENCE   3  (residues 1 to 1607)
  AUTHORS   Kritzer,M.D., Li,J., Passariello,C.L., Gayanilo,M., Thakur,H.,
            Dayan,J., Dodge-Kafka,K. and Kapiloff,M.S.
  TITLE     The scaffold protein muscle A-kinase anchoring protein beta
            orchestrates cardiac myocyte hypertrophic signaling required for
            the development of heart failure
  JOURNAL   Circ Heart Fail 7 (4), 663-672 (2014)
   PUBMED   24812305
REFERENCE   4  (residues 1 to 1607)
  AUTHORS   Yan,M., Zhao,J., Zhu,S., Shao,X., Zhang,L., Gao,H. and Yao,D.
  TITLE     Expression of SRC suppressed C kinase substrate in rat neural
            tissues during inflammation
  JOURNAL   Neurochem Res 39 (4), 748-757 (2014)
   PUBMED   24623461
  REMARK    GeneRIF: SSeCKS play an important role in sciatic nerve fibers and
            neurons in spinal cord and dorsal root ganglion during
            inflammation.
REFERENCE   5  (residues 1 to 1607)
  AUTHORS   You,T., Fan,Y., Li,Q., Gao,Y., Yang,Y., Zhao,Z. and Wang,C.
  TITLE     Increased SSeCKS expression in rat hepatic stellate cells upon
            activation in vitro and in vivo
  JOURNAL   Inflammation 36 (6), 1415-1423 (2013)
   PUBMED   23925424
REFERENCE   6  (residues 1 to 1607)
  AUTHORS   Xia,W. and Gelman,I.H.
  TITLE     Mitogen-induced, FAK-dependent tyrosine phosphorylation of the
            SSeCKS scaffolding protein
  JOURNAL   Exp Cell Res 277 (2), 139-151 (2002)
   PUBMED   12083796
  REMARK    GeneRIF: a role in mitogen-induced cytoskeletal reorganization
REFERENCE   7  (residues 1 to 1607)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   8  (residues 1 to 1607)
  AUTHORS   Siegel,S.M., Grove,B.D. and Carr,P.A.
  TITLE     SSeCKS immunolabeling in rat primary sensory neurons
  JOURNAL   Brain Res 926 (1-2), 126-136 (2002)
   PUBMED   11814414
REFERENCE   9  (residues 1 to 1607)
  AUTHORS   Chapline,C., Mousseau,B., Ramsay,K., Duddy,S., Li,Y., Kiley,S.C.
            and Jaken,S.
  TITLE     Identification of a major protein kinase C-binding protein and
            substrate in rat embryo fibroblasts. Decreased expression in
            transformed cells
  JOURNAL   J Biol Chem 271 (11), 6417-6422 (1996)
   PUBMED   8626441
REFERENCE   10 (residues 1 to 1607)
  AUTHORS   Lin,X., Nelson,P.J., Frankfort,B., Tombler,E., Johnson,R. and
            Gelman,I.H.
  TITLE     Isolation and characterization of a novel mitogenic regulatory
            gene, 322, which is transcriptionally suppressed in cells
            transformed by src and ras
  JOURNAL   Mol Cell Biol 15 (5), 2754-2762 (1995)
   PUBMED   7739556
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY695057.1 and BG664488.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY695057.1, SRR8487230.55492.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1607
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..1607
                     /product="A-kinase anchor protein 12 isoform beta"
                     /note="A kinase (PRKA) anchor protein (gravin) 12; SSeCKS,
                     Gravin, AKAP250; A kinase (PRKA) anchor protein 12;
                     AKAP-12"
                     /calculated_mol_wt=172934
     Region          512..540
                     /region_name="WSK"
                     /note="WSK motif; pfam03832"
                     /db_xref="CDD:461069"
     Region          704..729
                     /region_name="WSK"
                     /note="WSK motif; pfam03832"
                     /db_xref="CDD:461069"
     Region          <1005..1266
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     CDS             1..1607
                     /gene="Akap12"
                     /gene_synonym="AKAP12A; AKAP12B; AKAP12G"
                     /coded_by="NM_001033653.1:168..4991"
                     /note="isoform beta is encoded by transcript variant 2"
                     /db_xref="GeneID:83425"
                     /db_xref="RGD:70988"
ORIGIN      
        1 mlgtititvg qresedvrek drveemaans taveditkdg qeetseiieq ipasesnvee
       61 mvqpaesqan dvgfkkvfkf vgfkftvkkd kneksdtvql ltvkkdegeg aeasvgagdh
      121 qepsvetavg esaskeselk qstekqegtl kqeqssteip lqaesdqaae eeakdegeek
      181 qekeptkspe spsspvsset tssfkkffth gwagwrkkts fkkskeddle taekrkeqea
      241 ekvdeeekek tepaseeqep aedtdqarls adyekvelpl edqvgdleas seekcaplat
      301 evfdekmeah qevvaevhvs tvekteeeqg gggeaeggvv vegtgeslpp eklaepqevp
      361 qeaepaeelm ksremcvsgg dhtqltdlsp eektlpkhpe givsevemls sqerikvqgs
      421 plkklfsssg lkklsgkkqk gkrggggdee pgeyqhihte spesadeqkg essasspeep
      481 eettclekgp leapqdgeae egttsdgekk regitpwasf kkmvtpkkrv rrpsesdkee
      541 elekvksatl sstdstvsem qdevktvgee qkpeepkrrv dtsvsweali cvgsskkrar
      601 kasssddegg prtlggdshr aeeaskdkea gtdavpastq eqdqaqgsss pepagspseg
      661 egvstwesfk rlvtprkksk skleekaeds sveqlsteie psreeswvsi kkfipgrrkk
      721 radgkqeqat vedsgpvein eddpdvpavv plseydaver ekmeaqgnae lpqllgavyv
      781 seelsktlvh tvsvavidgt ravtsveers pswisasvte plehtageam ppveevtekd
      841 iiaeetpvlt qtlpegkdah ddmvtsevdf tseavtatet sealrteevt easgaeettd
      901 mvsavsqltd spdtteeatp vqeveggvld teeeerqtqa ilqavadkvk eesqvpatqt
      961 vqrtgskale kveeveedse vlasekekdv mpkgpvqeag aehlaqgset gqatpeslev
     1021 pevtadvdhv atcqviklqq lmeqavapes setltdsetn gstpladsdt adgtqqdeti
     1081 dsqdskataa vrqsqvteee aataqkeeps tlpnnvpaqe ehgeepgrdv leptqqelaa
     1141 aavpvlakte vgqegevdwl dgekvkeeqe vfvhsgpnsq kaadvtydse vmgvagcqek
     1201 estevqslsl eegemetdve kekretkpeq vseegeqeta apehegtygk pvltldmpss
     1261 ergkalgslg gspslpdqdk agcievqvqs ldttvtqtae avekvietvv isetgespec
     1321 vgahllpaek ssatgghwtl qhaedtvplg pesqaesipi ivtpapestl hpdlqgeisa
     1381 sqrerseeed kpdagpdadg kestaiekvl kaepeilele sksnkivlnv iqtavdqfar
     1441 tetapethay dsqtqvpamq adsqgaqqml dknescqdet psaaaqrgla spdrsggmgs
     1501 asemlaalav esagvkvsie klppqpkdqk ehaadgpqlq slaqaeasas gnltkespdt
     1561 ngpklteegd apkvevqeee mstksvkenk aqaeedlqep kgdlaes
//
LOCUS       NP_001004082             724 aa            linear   ROD 27-APR-2025
DEFINITION  heat shock protein HSP 90-beta [Rattus norvegicus].
ACCESSION   NP_001004082 XP_217339
VERSION     NP_001004082.3
DBSOURCE    REFSEQ: accession NM_001004082.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Liang,T., Hu,X., Zeng,L., Zhou,Z., Zhang,J., Xu,Z., Zeng,J. and
            Xu,P.
  TITLE     HSP90beta regulates EAAT2 expression and participates in
            ischemia-reperfusion injury in rats
  JOURNAL   Mol Med Rep 29 (1) (2024)
   PUBMED   37975223
  REMARK    GeneRIF: HSP90beta regulates EAAT2 expression and participates in
            ischemia-reperfusion injury in rats.
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Oroz,J., Chang,B.J., Wysoczanski,P., Lee,C.T., Perez-Lara,A.,
            Chakraborty,P., Hofele,R.V., Baker,J.D., Blair,L.J., Biernat,J.,
            Urlaub,H., Mandelkow,E., Dickey,C.A. and Zweckstetter,M.
  TITLE     Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau
            complex
  JOURNAL   Nat Commun 9 (1), 4532 (2018)
   PUBMED   30382094
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Krzemien-Ojak,L., Goral,A., Joachimiak,E., Filipek,A. and
            Fabczak,H.
  TITLE     Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein
            Hsp90
  JOURNAL   J Cell Biochem 118 (2), 420-429 (2017)
   PUBMED   27496612
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Okabe,T., Chavan,R., Fonseca Costa,S.S., Brenna,A., Ripperger,J.A.
            and Albrecht,U.
  TITLE     REV-ERBalpha influences the stability and nuclear localization of
            the glucocorticoid receptor
  JOURNAL   J Cell Sci 129 (21), 4143-4154 (2016)
   PUBMED   27686098
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Haslbeck,V., Eckl,J.M., Drazic,A., Rutz,D.A., Lorenz,O.R.,
            Zimmermann,K., Kriehuber,T., Lindemann,C., Madl,T. and Richter,K.
  TITLE     The activity of protein phosphatase 5 towards native clients is
            modulated by the middle- and C-terminal domains of Hsp90
  JOURNAL   Sci Rep 5, 17058 (2015)
   PUBMED   26593036
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Rallu,M., Loones,M., Lallemand,Y., Morimoto,R., Morange,M. and
            Mezger,V.
  TITLE     Function and regulation of heat shock factor 2 during mouse
            embryogenesis
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2392-2397 (1997)
   PUBMED   9122205
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Sepehrnia,B., Paz,I.B., Dasgupta,G. and Momand,J.
  TITLE     Heat shock protein 84 forms a complex with mutant p53 protein
            predominantly within a cytoplasmic compartment of the cell
  JOURNAL   J Biol Chem 271 (25), 15084-15090 (1996)
   PUBMED   8663025
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Nemoto,T., Ohara-Nemoto,Y., Ota,M., Takagi,T. and Yokoyama,K.
  TITLE     Mechanism of dimer formation of the 90-kDa heat-shock protein
  JOURNAL   Eur J Biochem 233 (1), 1-8 (1995)
   PUBMED   7588731
REFERENCE   9  (residues 1 to 724)
  AUTHORS   McGuire,J.A., Poellinger,L., Wikstrom,A.C. and Gustafsson,J.A.
  TITLE     Cloning and regulation by glucocorticoid receptor ligands of a rat
            hsp90
  JOURNAL   J Steroid Biochem Mol Biol 42 (8), 813-822 (1992)
   PUBMED   1525042
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Denis,M.
  TITLE     Two-step purification and N-terminal amino acid sequence analysis
            of the rat Mr 90,000 heat shock protein
  JOURNAL   Anal Biochem 173 (2), 405-411 (1988)
   PUBMED   3189818
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY695392.1.
            
            On Jun 10, 2007 this sequence version replaced NP_001004082.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY695392.1, BC082009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..724
                     /product="heat shock protein HSP 90-beta"
                     /note="HSP 84; HSP84; heat shock 84 kDa; heat shock
                     protein 90kDa alpha (cytosolic), class B member 1; heat
                     shock 90kDa protein 1, beta; heat shock protein 90 alpha
                     (cytosolic), class B member 1; heat shock protein 90kDa
                     alpha family class B member 1"
                     /calculated_mol_wt=83150
     Region          2..527
                     /region_name="Interaction with TP53.
                     /evidence=ECO:0000250|UniProtKB:P08238"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Region          2..214
                     /region_name="Interaction with BIRC2.
                     /evidence=ECO:0000250|UniProtKB:P08238"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Region          9..231
                     /region_name="Interaction with NR3C1.
                     /evidence=ECO:0000250|UniProtKB:P11499"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Region          14..724
                     /region_name="HSP90"
                     /note="Hsp90 protein; cl46693"
                     /db_xref="CDD:481033"
     Site            126..127
                     /site_type="other"
                     /note="Cleaved under oxidative stress.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Region          215..552
                     /region_name="Interaction with AHSA1.
                     /evidence=ECO:0000250|UniProtKB:P08238"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Region          222..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Region          264..608
                     /region_name="Interaction with NR3C1.
                     /evidence=ECO:0000250|UniProtKB:P11499"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11499; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            434
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            435
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            452
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            481
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11499; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            531
                     /site_type="methylation"
                     /note="N6-methylated lysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            574
                     /site_type="methylation"
                     /note="N6-methylated lysine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Region          620..723
                     /region_name="Interaction with NR1D1.
                     /evidence=ECO:0000250|UniProtKB:P11499"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            624
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11499; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Region          694..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2 and PLK3.
                     /evidence=ECO:0000250|UniProtKB:P08238; propagated from
                     UniProtKB/Swiss-Prot (P34058.4)"
     Region          720..724
                     /region_name="TPR repeat-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P34058.4)"
     CDS             1..724
                     /gene="Hsp90ab1"
                     /gene_synonym="HSP90-BETA; HSP90B; HSPC2; Hspcb"
                     /coded_by="NM_001004082.3:46..2220"
                     /db_xref="GeneID:301252"
                     /db_xref="RGD:1303075"
ORIGIN      
        1 mpeevhhgee evetfafqae iaqlmsliin tfysnkeifl relisnasda ldkiryeslt
       61 dpskldsgke lkidiipnpq ertltlvdtg igmtkadlin nlgtiaksgt kafmealqag
      121 adismigqfg vgfysaylva ekvvvitkhn ddeqyawess aggsftvrad hgepigrgtk
      181 vilhlkedqt eyleerrvke vvkkhsqfig ypitlyleke rekeisddea eeekgekeee
      241 dkedeekpki edvgsdeedd sgkdkkkktk kikekyidqe elnktkpiwt rnpdditqee
      301 ygefyksltn dwedhlavkh fsvegqlefr allfiprrap fdlfenkkkk nniklyvrrv
      361 fimdscdeli peylnfirgv vdsedlplni sremlqqski lkvirknivk kclelfsela
      421 edkenykkfy eafsknlklg ihedstnrrr lsellryhts qsgdemtsls eyvsrmketq
      481 ksiyyitges keqvansafv ervrkrgfev vymtepidey cvqqlkefdg kslvsvtkeg
      541 lelpedeeek kkmeeskakf enlcklmkei ldkkvekvti snrlvsspcc ivtstygwta
      601 nmerimkaqa lrdnstmgym makkhleinp dhpivetlrq kaeadkndka vkdlvvllfe
      661 tallssgfsl edpqthsnri yrmiklglgi dedevtaeep saavpdeipp legdedasrm
      721 eevd
//
LOCUS       NP_077376                967 aa            linear   ROD 27-APR-2025
DEFINITION  A disintegrin and metalloproteinase with thrombospondin motifs 1
            precursor [Rattus norvegicus].
ACCESSION   NP_077376
VERSION     NP_077376.2
DBSOURCE    REFSEQ: accession NM_024400.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Tatar,M., Uslu,S. and Oner,J.
  TITLE     Expression of placental growth factor and a disintegrin and
            metalloprotease with a thrombospondin type motifs 1-4-8 during the
            three trimesters of rat pregnancy at the maternal-fetal interface
  JOURNAL   Anat Histol Embryol 52 (5), 805-814 (2023)
   PUBMED   37424113
  REMARK    GeneRIF: Expression of placental growth factor and a disintegrin
            and metalloprotease with a thrombospondin type motifs 1-4-8 during
            the three trimesters of rat pregnancy at the maternal-fetal
            interface.
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Li,M., Liu,Q., Lei,J., Wang,X., Chen,X. and Ding,Y.
  TITLE     MiR-362-3p inhibits the proliferation and migration of vascular
            smooth muscle cells in atherosclerosis by targeting ADAMTS1
  JOURNAL   Biochem Biophys Res Commun 493 (1), 270-276 (2017)
   PUBMED   28890348
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Roet,K.C., Franssen,E.H., de Bree,F.M., Essing,A.H., Zijlstra,S.J.,
            Fagoe,N.D., Eggink,H.M., Eggers,R., Smit,A.B., van Kesteren,R.E.
            and Verhaagen,J.
  TITLE     A multilevel screening strategy defines a molecular fingerprint of
            proregenerative olfactory ensheathing cells and identifies SCARB2,
            a protein that improves regenerative sprouting of injured sensory
            spinal axons
  JOURNAL   J Neurosci 33 (27), 11116-11135 (2013)
   PUBMED   23825416
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Oveland,E., Karlsen,T.V., Haslene-Hox,H., Semaeva,E., Janaczyk,B.,
            Tenstad,O. and Wiig,H.
  TITLE     Proteomic evaluation of inflammatory proteins in rat spleen
            interstitial fluid and lymph during LPS-induced systemic
            inflammation reveals increased levels of ADAMST1
  JOURNAL   J Proteome Res 11 (11), 5338-5349 (2012)
   PUBMED   23025351
  REMARK    GeneRIF: A disintegrin and metalloproteinase with thrombospondin
            motifs 1 (ADAMTS1) was detected by proteomics (the pro- region) in
            lymph only after LPS
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Wang,Y., Huang,C.X., Zhou,Y.F., Cheng,J.S., Wang,H., Wu,W.J.,
            Liao,W.Q., Wen,J.Y., Ke,Y.N. and Zheng,J.G.
  TITLE     ADAMTS-1 expression in rat myocardium after ischemic
            preconditioning: age-associated differences
  JOURNAL   Chin Med J (Engl) 124 (1), 95-99 (2011)
   PUBMED   21362315
  REMARK    GeneRIF: Cardioprotection with IPC is attenuated in the older
            heart. ADAMTS-1 expression induced by IPC is greater in old rats.
            Over-expression of anti-angiogenic factors might be a potential
            mechanism behind reduced protection after IPC associated with
            aging.
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Diamantis,I., Luthi,M., Hosli,M. and Reichen,J.
  TITLE     Cloning of the rat ADAMTS-1 gene and its down regulation in
            endothelial cells in cirrhotic rats
  JOURNAL   Liver 20 (2), 165-172 (2000)
   PUBMED   10847486
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Espey,L.L., Yoshioka,S., Russell,D.L., Robker,R.L., Fujii,S. and
            Richards,J.S.
  TITLE     Ovarian expression of a disintegrin and metalloproteinase with
            thrombospondin motifs during ovulation in the gonadotropin-primed
            immature rat
  JOURNAL   Biol Reprod 62 (4), 1090-1095 (2000)
   PUBMED   10727282
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Vazquez,F., Hastings,G., Ortega,M.A., Lane,T.F., Oikemus,S.,
            Lombardo,M. and Iruela-Arispe,M.L.
  TITLE     METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a
            new family of proteins with angio-inhibitory activity
  JOURNAL   J Biol Chem 274 (33), 23349-23357 (1999)
   PUBMED   10438512
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Kuno,K. and Matsushima,K.
  TITLE     ADAMTS-1 protein anchors at the extracellular matrix through the
            thrombospondin type I motifs and its spacing region
  JOURNAL   J Biol Chem 273 (22), 13912-13917 (1998)
   PUBMED   9593739
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Kuno,K., Kanada,N., Nakashima,E., Fujiki,F., Ichimura,F. and
            Matsushima,K.
  TITLE     Molecular cloning of a gene encoding a new type of
            metalloproteinase-disintegrin family protein with thrombospondin
            motifs as an inflammation associated gene
  JOURNAL   J Biol Chem 272 (1), 556-562 (1997)
   PUBMED   8995297
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC080237.1.
            
            On Jun 10, 2007 this sequence version replaced NP_077376.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC080237.1, AF149118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..967
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 1 precursor"
                     /note="ADAM-TS1; ADAMTS-1; ADAM-TS 1; a disintegrin and
                     metalloproteinase with thrombospondin motifs 1 (ADAMTS-1);
                     a disintegrin-like and metalloprotease (reprolysin type)
                     with thrombospondin type 1 motif, 1; a disintegrin-like
                     and metallopeptidase (reprolysin type) with thrombospondin
                     type 1 motif, 1; a disintegrin-like and metallopeptidse
                     (reprolysin type) with thrombospondin type 1 motif, 1"
                     /calculated_mol_wt=99900
     sig_peptide     1..54
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
                     /calculated_mol_wt=5766
     Region          67..166
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          198..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Region          203..210
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     mat_peptide     253..967
                     /product="A disintegrin and metalloproteinase with
                     thrombospondin motifs 1. /id=PRO_0000029155"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WUQ1.1)"
                     /calculated_mol_wt=78570
     Region          258..463
                     /region_name="ZnMc_ADAMTS_like"
                     /note="Zinc-dependent metalloprotease, ADAMTS_like
                     subgroup. ADAMs (A Disintegrin And Metalloprotease) are
                     glycoproteins, which play roles in cell signaling, cell
                     fusion, and cell-cell interactions. This particular
                     subfamily represents domain architectures that...;
                     cd04273"
                     /db_xref="CDD:239801"
     Site            order(401..402,405,411)
                     /site_type="active"
                     /db_xref="CDD:239801"
     Region          478..546
                     /region_name="ADAMTS_CR_2"
                     /note="ADAMTS cysteine-rich domain 2; pfam17771"
                     /db_xref="CDD:465496"
     Site            547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Region          562..614
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          621..724
                     /region_name="ADAMTS_CR_3"
                     /note="ADAMTS cysteine-rich domain; pfam19236"
                     /db_xref="CDD:437068"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Region          725..857
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Region          726..842
                     /region_name="ADAMTS_spacer1"
                     /note="ADAM-TS Spacer 1; pfam05986"
                     /db_xref="CDD:461796"
     Site            764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     Region          858..909
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Region          912..966
                     /region_name="TSP1_ADAMTS"
                     /note="Thrombospondin type 1 domain; pfam19030"
                     /db_xref="CDD:465950"
     Site            945
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WUQ1.1)"
     CDS             1..967
                     /gene="Adamts1"
                     /coded_by="NM_024400.2:382..3285"
                     /db_xref="GeneID:79252"
                     /db_xref="RGD:621241"
ORIGIN      
        1 mqpevplgsg klkpcsdmgd iqraakfrss qsahmlllll asitmllcvr gahgrpteed
       61 eelvlpsler arghgsttll rldafgqqlh lklqpdsgfl apgftlqtvg rspgseaqhl
      121 dptgdlahcf ysgtvngdps saaalslceg vrgafylqge effiqpapav aterlvpaep
      181 keesiapprf hilrrrrrgs ggakcgvmde etlptsnsgr esqntpdqwp lrnptpqgag
      241 kptgpgsirk krfvsspryv etmlvadqsm adfhgsglkh ylltlfsvaa rfykhpsirn
      301 sislvvvkil viyeeqkgpe vtsnaaltlr nfcswqkqhn spsdrdpehy dtailftrqd
      361 lcgshtcdtl gmadvgtvcd psrscsvied dglqaaftta helghvfnmp hddakhcasf
      421 ngvsgdshlm asmlssldhs qpwspcsaym vtsfldnghg eclmdkpqnp iklpsdlpgt
      481 lydanrqcqf tfgeesthcp daastcstlw ctgtsggllv cqtkhfpwad gtscgegkwc
      541 vsgkcvnktd mkhfatpvhg swgpwgpwgd csrtcgggvq ytmrecdnpv pknggkyceg
      601 krvryrscni edcpdnngkt freeqceahn efskasfgne ptvewtpkya gvspkdrckl
      661 tceakgigyf fvlqpkvvdg tpcspdstsv cvqgqcvkag cdriidskkk fdkcgvcggn
      721 gstckkisgt vtstrpgyhd ivtipagatn ievkhrnprg srnngsflai raadgtyiln
      781 gnftlstleq dltykgtvlr ysgssaaler irsfsplkep ltiqvlmvgh alrpkikyty
      841 fmkkktepfn aiptfsewvi eewgecsktc gsgwqrrvve crdinghpas ecakevkpas
      901 trpcadlpcp rwqvgdwspc sktcgkgykk rtlkclshdg gvlsnescdp lkkpkhyidf
      961 ciltqcs
//
LOCUS       NP_001103374             800 aa            linear   ROD 27-APR-2025
DEFINITION  fibroblast growth factor receptor 4 precursor [Rattus norvegicus].
ACCESSION   NP_001103374 XP_001066753 XP_001066809 XP_344571
VERSION     NP_001103374.1
DBSOURCE    REFSEQ: accession NM_001109904.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Sootome,H., Fujita,H., Ito,K., Ochiiwa,H., Fujioka,Y., Ito,K.,
            Miura,A., Sagara,T., Ito,S., Ohsawa,H., Otsuki,S., Funabashi,K.,
            Yashiro,M., Matsuo,K., Yonekura,K. and Hirai,H.
  TITLE     Futibatinib Is a Novel Irreversible FGFR 1-4 Inhibitor That Shows
            Selective Antitumor Activity against FGFR-Deregulated Tumors
  JOURNAL   Cancer Res 80 (22), 4986-4997 (2020)
   PUBMED   32973082
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Yamauchi,M., Ono,A., Ishikawa,A., Kodama,K., Uchikawa,S.,
            Hatooka,H., Zhang,P., Teraoka,Y., Morio,K., Fujino,H., Nakahara,T.,
            Murakami,E., Miki,D., Kawaoka,T., Tsuge,M., Hiramatsu,A.,
            Imamura,M., Hayes,C.N., Fujita,M., Nakagawa,H., Yasui,W., Aikata,H.
            and Chayama,K.
  TITLE     Tumor Fibroblast Growth Factor Receptor 4 Level Predicts the
            Efficacy of Lenvatinib in Patients With Advanced Hepatocellular
            Carcinoma
  JOURNAL   Clin Transl Gastroenterol 11 (5), e00179 (2020)
   PUBMED   32677805
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Quintanal-Villalonga,A., Ojeda-Marquez,L., Marrugal,A., Yague,P.,
            Ponce-Aix,S., Salinas,A., Carnero,A., Ferrer,I., Molina-Pinelo,S.
            and Paz-Ares,L.
  TITLE     The FGFR4-388arg Variant Promotes Lung Cancer Progression by
            N-Cadherin Induction
  JOURNAL   Sci Rep 8 (1), 2394 (2018)
   PUBMED   29402970
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Leifheit-Nestler,M., Grabner,A., Hermann,L., Richter,B.,
            Schmitz,K., Fischer,D.C., Yanucil,C., Faul,C. and Haffner,D.
  TITLE     Vitamin D treatment attenuates cardiac FGF23/FGFR4 signaling and
            hypertrophy in uremic rats
  JOURNAL   Nephrol Dial Transplant 32 (9), 1493-1503 (2017)
   PUBMED   28339837
  REMARK    GeneRIF: High FGFr4 expression is associated with cardiac
            hypertrophy.
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Shi,S., Li,X., You,B., Shan,Y., Cao,X. and You,Y.
  TITLE     High Expression of FGFR4 Enhances Tumor Growth and Metastasis in
            Nasopharyngeal Carcinoma
  JOURNAL   J Cancer 6 (12), 1245-1254 (2015)
   PUBMED   26535066
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Xie,M.H., Holcomb,I., Deuel,B., Dowd,P., Huang,A., Vagts,A.,
            Foster,J., Liang,J., Brush,J., Gu,Q., Hillan,K., Goddard,A. and
            Gurney,A.L.
  TITLE     FGF-19, a novel fibroblast growth factor with unique specificity
            for FGFR4
  JOURNAL   Cytokine 11 (10), 729-735 (1999)
   PUBMED   10525310
REFERENCE   7  (residues 1 to 800)
  AUTHORS   Szpirer,C., Szpirer,J., Van Vooren,P., Tissir,F., Simon,J.S.,
            Koike,G., Jacob,H.J., Lander,E.S., Helou,K., Klinga-Levan,K. and
            Levan,G.
  TITLE     Gene-based anchoring of the rat genetic linkage and cytogenetic
            maps: new regional localizations, orientation of the linkage
            groups, and insights into mammalian chromosome evolution
  JOURNAL   Mamm Genome 9 (9), 721-734 (1998)
   PUBMED   9716657
REFERENCE   8  (residues 1 to 800)
  AUTHORS   Weinstein,M., Xu,X., Ohyama,K. and Deng,C.X.
  TITLE     FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in
            the murine lung
  JOURNAL   Development 125 (18), 3615-3623 (1998)
   PUBMED   9716527
REFERENCE   9  (residues 1 to 800)
  AUTHORS   Ornitz,D.M., Xu,J., Colvin,J.S., McEwen,D.G., MacArthur,C.A.,
            Coulier,F., Gao,G. and Goldfarb,M.
  TITLE     Receptor specificity of the fibroblast growth factor family
  JOURNAL   J Biol Chem 271 (25), 15292-15297 (1996)
   PUBMED   8663044
REFERENCE   10 (residues 1 to 800)
  AUTHORS   Horlick,R.A., Stack,S.L. and Cooke,G.M.
  TITLE     Cloning, expression and tissue distribution of the gene encoding
            rat fibroblast growth factor receptor subtype 4
  JOURNAL   Gene 120 (2), 291-295 (1992)
   PUBMED   1398143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB743466.1 and BC100260.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_344571.3, XP_001066753.1, XP_001066809.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC100260.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..800
                     /product="fibroblast growth factor receptor 4 precursor"
                     /EC_number="2.7.10.1"
                     /note="FGFR-4"
                     /calculated_mol_wt=86880
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
                     /calculated_mol_wt=1846
     mat_peptide     17..800
                     /product="Fibroblast growth factor receptor 4.
                     /id=PRO_0000227548"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498D6.1)"
                     /calculated_mol_wt=86880
     Region          33..101
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..85
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          95..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Region          143..237
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          164..168
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          203..207
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          217..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          230..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          245..347
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Region          263..267
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..280
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Region          312..316
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          326..331
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          339..342
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498D6.1)"
     Region          452..765
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(471..474,477,479,499,501,532,548..551,610,614..615,
                     617,627..628)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22455; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P22455; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P22455; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P22455; propagated from
                     UniProtKB/Swiss-Prot (Q498D6.1)"
     Region          768..800
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498D6.1)"
     CDS             1..800
                     /gene="Fgfr4"
                     /coded_by="NM_001109904.1:176..2578"
                     /db_xref="GeneID:25114"
                     /db_xref="RGD:2612"
ORIGIN      
        1 mwlllallsi fqetpafsle aseemeqepc papiseqqeq vltvalgqpv rlccgrterg
       61 rhwykegsrl asagrvrgwr grleiasflp edagrylcla rgsmtvvhnl tlimddslps
      121 innedpktls ssssghsylq qapywthpqr mekklhavpa gntvkfrcpa agnpmptihw
      181 lkngqafhge nriggirlrh qhwslvmesv vpsdrgtytc lvenslgsir ysylldvler
      241 sphrpilqag lpanttavvg snvellckvy sdaqphiqwl khivingssf gadgfpyvqv
      301 lkttdinsse vevlylrnvs aedageytcl agnsiglsyq sawltvlpae eedlawttat
      361 searytdiil yvsgslalvl llllagvyhr qaihghhsrq pvtvqklsrf plarqfsles
      421 rssgksslsl vrgvrlsssg pplltglvsl dlpldplwef prdrlvlgkp lgegcfgqvv
      481 raealgmdss rpdqtstvav kmlkdnasdk dladliseme mmkligrhkn iinllgvctq
      541 egplyvivey aakgnlrefl rarrppgpdl spdgprsseg plsfpalvsc ayqvargmqy
      601 lesrkcihrd laarnvlvte ddvmkiadfg largvhhidy ykktsngrlp vkwmapealf
      661 drvythqsdv wsfgillwei ftlggspypg ipveelfsll reghrmerpp ncpselyglm
      721 recwhaapsq rptfkqlvea ldkvllavse eyldlrltfg pyspnngdas stcsssdsvf
      781 shdplpleps pfpfpeaqtt
//
LOCUS       NP_036712                289 aa            linear   ROD 27-APR-2025
DEFINITION  heme oxygenase 1 [Rattus norvegicus].
ACCESSION   NP_036712
VERSION     NP_036712.1
DBSOURCE    REFSEQ: accession NM_012580.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Liu,H.L., Wu,T., Zeng,X., Cao,W.Y. and Wu,S.K.
  TITLE     Acupoint Autohemotherapy Alleviates Airway Inflammation in
            Asthmatic Rats via Upregulating Expression of Hemeoxygenase-1
  JOURNAL   J Acupunct Meridian Stud 17 (5), 149-157 (2024)
   PUBMED   39444099
  REMARK    GeneRIF: Acupoint Autohemotherapy Alleviates Airway Inflammation in
            Asthmatic Rats via Upregulating Expression of Hemeoxygenase-1.
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Xiao,B., Zhu,Y., Liu,M., Chen,M., Huang,C., Xu,D., Wang,F., Sun,S.,
            Huang,J., Sun,N. and Yang,F.
  TITLE     miR-340-3p-modified bone marrow mesenchymal stem cell-derived
            exosomes inhibit ferroptosis through METTL3-mediated m6A
            modification of HMOX1 to promote recovery of injured rat uterus
  JOURNAL   Stem Cell Res Ther 15 (1), 224 (2024)
   PUBMED   39075530
  REMARK    GeneRIF: miR-340-3p-modified bone marrow mesenchymal stem
            cell-derived exosomes inhibit ferroptosis through METTL3-mediated
            m[6]A modification of HMOX1 to promote recovery of injured rat
            uterus.
            Erratum:[Stem Cell Res Ther. 2024 Oct 10;15(1):357. doi:
            10.1186/s13287-024-03985-w. PMID: 39390524]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Li,M. and Zheng,N.
  TITLE     The Role of Heme Oxygenase 1 in Rheumatoid Arthritis and IL-1
            Induced Inflammatory Cell Model
  JOURNAL   Ann Clin Lab Sci 54 (4), 446-451 (2024)
   PUBMED   39293832
  REMARK    GeneRIF: The Role of Heme Oxygenase 1 in Rheumatoid Arthritis and
            IL-1 Induced Inflammatory Cell Model.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Tao,W., Lu,Y., Xiao,R., Zhang,J., Hu,P., Zhao,N., Peng,W., Qian,K.
            and Liu,F.
  TITLE     LncRNA HMOX1 alleviates renal ischemia-reperfusion-induced
            ferroptotic injury via the miR-3587/HMOX1 axis
  JOURNAL   Cell Signal 119, 111165 (2024)
   PUBMED   38583746
  REMARK    GeneRIF: LncRNA HMOX1 alleviates renal ischemia-reperfusion-induced
            ferroptotic injury via the miR-3587/HMOX1 axis.
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Wang,Y., Qiu,J., Yan,H., Zhang,N., Gao,S., Xu,N., Wang,C. and
            Lou,H.
  TITLE     The Bach1/HO-1 pathway regulates oxidative stress and contributes
            to ferroptosis in doxorubicin-induced cardiomyopathy in H9c2 cells
            and mice
  JOURNAL   Arch Toxicol 98 (6), 1781-1794 (2024)
   PUBMED   38573338
  REMARK    GeneRIF: The Bach1/HO-1 pathway regulates oxidative stress and
            contributes to ferroptosis in doxorubicin-induced cardiomyopathy in
            H9c2 cells and mice.
REFERENCE   6  (residues 1 to 289)
  AUTHORS   McCoubrey,W.K. Jr., Ewing,J.F. and Maines,M.D.
  TITLE     Human heme oxygenase-2: characterization and expression of a
            full-length cDNA and evidence suggesting that the two HO-2
            transcripts may differ by choice of polyadenylation signal
  JOURNAL   Arch Biochem Biophys 295 (1), 13-20 (1992)
   PUBMED   1575508
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Ishikawa,K., Sato,M. and Yoshida,T.
  TITLE     Expression of rat heme oxygenase in Escherichia coli as a
            catalytically active, full-length form that binds to bacterial
            membranes
  JOURNAL   Eur J Biochem 202 (1), 161-165 (1991)
   PUBMED   1935972
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Yoshida,T. and Sato,M.
  TITLE     Posttranslational and direct integration of heme oxygenase into
            microsomes
  JOURNAL   Biochem Biophys Res Commun 163 (2), 1086-1092 (1989)
   PUBMED   2783112
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Muller,R.M., Taguchi,H. and Shibahara,S.
  TITLE     Nucleotide sequence and organization of the rat heme oxygenase gene
  JOURNAL   J Biol Chem 262 (14), 6795-6802 (1987)
   PUBMED   3032976
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Shibahara,S., Muller,R., Taguchi,H. and Yoshida,T.
  TITLE     Cloning and expression of cDNA for rat heme oxygenase
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7865-7869 (1985)
   PUBMED   3865203
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091164.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091164.1, EV768426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..289
                     /product="heme oxygenase 1"
                     /EC_number="1.14.14.18"
                     /note="heme oxygenase (decyclizing) 1; heme oxygenase
                     (decycling) 1"
                     /calculated_mol_wt=32875
     Region          11..216
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(18,25,28..29,34,38,134..136,142..143,147,179,183,
                     207,210,214)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350856"
     Region          127..154
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350856"
     Site            140
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P09601; propagated from
                     UniProtKB/Swiss-Prot (P06762.1)"
     Region          225..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06762.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09601; propagated from
                     UniProtKB/Swiss-Prot (P06762.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06762.1)"
     Site            267..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P06762.1)"
     CDS             1..289
                     /gene="Hmox1"
                     /gene_synonym="Heox; HEOXG; Hmox; Ho-1; Ho1; hsp32"
                     /coded_by="NM_012580.2:117..986"
                     /db_xref="GeneID:24451"
                     /db_xref="RGD:2806"
ORIGIN      
        1 merpqldsms qdlsealkea tkevhiraen sefmrnfqkg qvsregfklv maslyhiyta
       61 leeeiernkq npvyaplyfp eelhrraale qdmafwygph wqeaipytpa tqhyvkrlhe
      121 vggthpellv ahaytrylgd lsggqvlkki aqkamalpss geglafftfp sidnptkfkq
      181 lyrarmntle mtpevkhrvt eeaktaflln ielfeelqal lteehkdqsp sqteflrqrp
      241 aslvqdttsa etprgksqis tsssqtpllr wvltlsflla tvavgiyam
//
LOCUS       NP_001020190             223 aa            linear   ROD 27-APR-2025
DEFINITION  N-terminal Xaa-Pro-Lys N-methyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_001020190
VERSION     NP_001020190.1
DBSOURCE    REFSEQ: accession NM_001025019.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wu,R., Yue,Y., Zheng,X. and Li,H.
  TITLE     Molecular basis for histone N-terminal methylation by NRMT1
  JOURNAL   Genes Dev 29 (22), 2337-2342 (2015)
   PUBMED   26543159
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Tooley,C.E., Petkowski,J.J., Muratore-Schroeder,T.L.,
            Balsbaugh,J.L., Shabanowitz,J., Sabat,M., Minor,W., Hunt,D.F. and
            Macara,I.G.
  TITLE     NRMT is an alpha-N-methyltransferase that methylates RCC1 and
            retinoblastoma protein
  JOURNAL   Nature 466 (7310), 1125-1128 (2010)
   PUBMED   20668449
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Webb,K.J., Lipson,R.S., Al-Hadid,Q., Whitelegge,J.P. and
            Clarke,S.G.
  TITLE     Identification of protein N-terminal methyltransferases in yeast
            and humans
  JOURNAL   Biochemistry 49 (25), 5225-5235 (2010)
   PUBMED   20481588
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091294.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091294.1, DN933978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..223
                     /product="N-terminal Xaa-Pro-Lys N-methyltransferase 1"
                     /EC_number="2.1.1.244"
                     /note="methyltransferase-like protein 11A; alpha
                     N-terminal protein methyltransferase 1A; X-Pro-Lys
                     N-terminal protein methyltransferase 1A; methyltransferase
                     like 11A"
                     /calculated_mol_wt=25333
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BV86; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX0.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in N-terminal Xaa-Pro-Lys
                     N-methyltransferase 1, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:Q9BV86; propagated from
                     UniProtKB/Swiss-Prot (Q5BJX0.3)"
     Region          8..223
                     /region_name="Methyltransf_PK"
                     /note="AdoMet dependent proline di-methyltransferase;
                     pfam05891"
                     /db_xref="CDD:461771"
     CDS             1..223
                     /gene="Ntmt1"
                     /gene_synonym="Mettl11a; NTM1A; RGD1306582"
                     /coded_by="NM_001025019.1:168..839"
                     /db_xref="GeneID:362103"
                     /db_xref="RGD:1306582"
ORIGIN      
        1 mtseviedek qfyskaktyw kqipptvdgm lggyghisni dlnssrkflq rflregpnkt
       61 gtscaldcga gigritkrll lplfrvvdmv dvtedflaka ktylgeegkr vrnyfccglq
      121 dfspepssyd viwiqwvigh ltdqhlaefl rrcrrglrpn giivikdnma qegvilddvd
      181 ssvcrdlevv rriirsagls llaeerqenl pdeiyhvysf alr
//
LOCUS       NP_001029245             248 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.8cy [Rattus norvegicus].
ACCESSION   NP_001029245
VERSION     NP_001029245.1
DBSOURCE    REFSEQ: accession NM_001034073.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB585296.1, M60668.1 and
            BC078780.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.8, also known as variant 7)
            has multiple differences in the coding region compared to variant
            1. These differences result in an isoform (Tpm1.8cy, also referred
            to as TM-5a) that is shorter and has distinct N- and C-termini
            compared to isoform a. Isoform Tpm1.8cy is the same length as
            isoforms Tpm1.9cy and Tpm1.13 but is the product of alternate
            splicing and contains short regions of sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform Tpm1.8cy"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=28426
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034073.1:152..898"
                     /note="isoform Tpm1.8cy is encoded by transcript variant
                     Tpm1.8"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeerags lqreldqerk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedkyeeeik vlsdklkeae traefaersv tkleksiddl eekvahakee nlsmhqmldq
      241 tllelnnm
//
LOCUS       NP_071551                349 aa            linear   ROD 27-APR-2025
DEFINITION  glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic [Rattus
            norvegicus].
ACCESSION   NP_071551
VERSION     NP_071551.2
DBSOURCE    REFSEQ: accession NM_022215.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Orr,A.L., Quinlan,C.L., Perevoshchikova,I.V. and Brand,M.D.
  TITLE     A refined analysis of superoxide production by mitochondrial
            sn-glycerol 3-phosphate dehydrogenase
  JOURNAL   J Biol Chem 287 (51), 42921-42935 (2012)
   PUBMED   23124204
  REMARK    GeneRIF: These results clarify the maximum rate and mechanism of
            superoxide production by mGPDH.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Rauchova,H., Mracek,T., Novak,P., Vokurkova,M. and Soukup,T.
  TITLE     Glycerol-3-phosphate dehydrogenase expression and oxygen
            consumption in liver mitochondria of female and male rats with
            chronic alteration of thyroid status
  JOURNAL   Horm Metab Res 43 (1), 43-47 (2011)
   PUBMED   20886417
  REMARK    GeneRIF: GPDH expression was significantly increased in the
            hyperthyroid and decreased in the hyporthyroid status in both
            sexes.
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Mracek,T., Pecinova,A., Vrbacky,M., Drahota,Z. and Houstek,J.
  TITLE     High efficiency of ROS production by glycerophosphate dehydrogenase
            in mammalian mitochondria
  JOURNAL   Arch Biochem Biophys 481 (1), 30-36 (2009)
   PUBMED   18952046
  REMARK    GeneRIF: high efficiency of mGPDH-dependent ROS production in
            mammalian mitochondria with a low content of mGPDH and suggest its
            endogenous inhibition in BAT.
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Ying,W.
  TITLE     NAD+/NADH and NADP+/NADPH in cellular functions and cell death:
            regulation and biological consequences
  JOURNAL   Antioxid Redox Signal 10 (2), 179-206 (2008)
   PUBMED   18020963
  REMARK    Review article
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Daikoku,T., Shinohara,Y., Shima,A., Yamazaki,N. and Terada,H.
  TITLE     Dramatic enhancement of the specific expression of the heart-type
            fatty acid binding protein in rat brown adipose tissue by cold
            exposure
  JOURNAL   FEBS Lett 410 (2-3), 383-386 (1997)
   PUBMED   9237667
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Brand,I.A. and Heinickel,A.
  TITLE     Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa
            Zn(2+)-binding protein (parathymosin)
  JOURNAL   J Biol Chem 266 (31), 20984-20989 (1991)
   PUBMED   1834654
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Dobson,D.E., Groves,D.L. and Spiegelman,B.M.
  TITLE     Nucleotide sequence and hormonal regulation of mouse
            glycerophosphate dehydrogenase mRNA during adipocyte and muscle
            cell differentiation
  JOURNAL   J Biol Chem 262 (4), 1804-1809 (1987)
   PUBMED   3027100
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Preston,S.L. and McMorris,F.A.
  TITLE     Normal myelin composition and phospholipid synthesis in
            adrenalectomized rats with reduced brain myelin and glycerol
            3-phosphate dehydrogenase activity
  JOURNAL   J Neurochem 45 (6), 1771-1778 (1985)
   PUBMED   2997397
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Kozak,L.P. and Ratner,P.L.
  TITLE     Genetic regulation of translatable mRNA levels for mouse
            sn-glycerol-3-phosphate dehydrogenase during development of the
            cerebellum
  JOURNAL   J Biol Chem 255 (16), 7589-7594 (1980)
   PUBMED   6105153
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088396.1.
            
            On Jan 12, 2005 this sequence version replaced NP_071551.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088396.1, AB002558.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..349
                     /product="glycerol-3-phosphate dehydrogenase [NAD(+)],
                     cytoplasmic"
                     /EC_number="1.1.1.8"
                     /note="glycerol-3-phosphate dehydrogenase [NAD+],
                     cytoplasmic; GPD-C; GPDH-C; glycerol 3-phosphate
                     dehydrogenase; glycerol-3-phosphate dehydrogenase 1
                     (soluble)"
                     /calculated_mol_wt=37322
     Region          5..342
                     /region_name="glycerol3P_DH"
                     /note="glycerol-3-phosphate dehydrogenase (NAD(+));
                     TIGR03376"
                     /db_xref="CDD:274551"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21695; propagated from
                     UniProtKB/Swiss-Prot (O35077.4)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35077.4)"
     CDS             1..349
                     /gene="Gpd1"
                     /gene_synonym="Gpd3; GPDH"
                     /coded_by="NM_022215.2:13..1062"
                     /db_xref="GeneID:60666"
                     /db_xref="RGD:621381"
ORIGIN      
        1 magkkvcivg sgnwgsaiak ivgsnasqla hfdprvtmwv feediggrkl teiintqhen
       61 vkylpghklp pnvvavpdvv qaatgadilv fvvphqfigk icdqlkghlk antigislik
      121 gidegpnglk lisevigesl gipmsvlmga niasevaeek fcettigckd paqgqllkel
      181 mqtpnfritv vqevdtveic galknivavg agfcdglgfg dntkaavirl glmemiafak
      241 lfcsgsvssa tflescgvad littcyggrn rkvaeafart gksieqleke mlngqklqgp
      301 qtarelhsil qhkglvdkfp lftavykvcy egqpvgefic clqnhpehm
//
LOCUS       NP_036663                264 aa            linear   ROD 27-APR-2025
DEFINITION  catechol O-methyltransferase [Rattus norvegicus].
ACCESSION   NP_036663
VERSION     NP_036663.1
DBSOURCE    REFSEQ: accession NM_012531.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Zhou,Y., Song,Z., Chen,S., Yao,F., Liu,J., Ouyang,Z. and Liao,Z.
  TITLE     Mechanism of Catechol-O-methyltransferase Regulating Orofacial Pain
            Induced by Tooth Movement
  JOURNAL   Biomed Res Int 2021, 4229491 (2021)
   PUBMED   34725639
  REMARK    GeneRIF: Mechanism of Catechol-O-methyltransferase Regulating
            Orofacial Pain Induced by Tooth Movement.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Oyaci,Y., Aytac,H.M., Pasin,O., Cetinay Aydin,P. and Pehlivan,S.
  TITLE     Detection of altered methylation of MB-COMT promotor and DRD2 gene
            in cannabinoid or synthetic cannabinoid use disorder regarding gene
            variants and clinical parameters
  JOURNAL   J Addict Dis 39 (4), 526-536 (2021)
   PUBMED   33781176
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Su,Y., DePasquale,M., Liao,G., Buchler,I., Zhang,G., Byers,S.,
            Carr,G.V., Barrow,J. and Wei,H.
  TITLE     Membrane bound catechol-O-methytransferase is the dominant isoform
            for dopamine metabolism in PC12 cells and rat brain
  JOURNAL   Eur J Pharmacol 896, 173909 (2021)
   PUBMED   33503461
  REMARK    GeneRIF: Membrane bound catechol-O-methytransferase is the dominant
            isoform for dopamine metabolism in PC12 cells and rat brain.
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Deji,C., Li,Y., Chen,Y., Lai,J. and Wei,S.
  TITLE     Association study of Catechol-o-methyltransferase and
            Alpha-1-adrenergic receptor gene polymorphisms with multiple
            phenotypes of heroin use disorder
  JOURNAL   Neurosci Lett 748, 135677 (2021)
   PUBMED   33577997
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Sonia,J.A., Kabir,T., Islam,M.M.T. and Kabir,Y.
  TITLE     Catechol-O-methyltransferase and dopamine receptor D4 gene
            variants: Possible association with substance abuse in Bangladeshi
            male
  JOURNAL   PLoS One 16 (2), e0246462 (2021)
   PUBMED   33544778
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Ulmanen,I. and Lundstrom,K.
  TITLE     Cell-free synthesis of rat and human catechol O-methyltransferase.
            Insertion of the membrane-bound form into microsomal membranes in
            vitro
  JOURNAL   Eur J Biochem 202 (3), 1013-1020 (1991)
   PUBMED   1765063
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Salminen,M., Lundstrom,K., Tilgmann,C., Savolainen,R., Kalkkinen,N.
            and Ulmanen,I.
  TITLE     Molecular cloning and characterization of rat liver
            catechol-O-methyltransferase
  JOURNAL   Gene 93 (2), 241-247 (1990)
   PUBMED   2227437
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Amin,A.M., Creveling,C.R. and Lowe,M.C.
  TITLE     Immunohistochemical localization of catechol methyltransferase in
            normal and cancerous breast tissues of mice and rats
  JOURNAL   J Natl Cancer Inst 70 (2), 337-342 (1983)
   PUBMED   6337293
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Pazmino,P.A. and Weinshilboum,R.M.
  TITLE     Methyl conjugation in uraemia: catechol-O-methyltransferase
  JOURNAL   Br J Clin Pharmacol 10 (5), 509-518 (1980)
   PUBMED   7437264
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Parvez,H., Ismahan,G., Parvez,S. and Youdim,M.B.
  TITLE     Developmental changes in the activity of catechol-O-methyl
            transferase in rat and rabbit fetuses
  JOURNAL   J Neural Transm 44 (1-2), 65-75 (1979)
   PUBMED   438804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK478774.1 and BC081850.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081850.1, EV762632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..264
                     /product="catechol O-methyltransferase"
                     /EC_number="2.1.1.6"
                     /note="catecholamine-O-methyltransferase"
                     /calculated_mol_wt=29466
     Site            3..19
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22734.2)"
     Region          90..235
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22734.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22734.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22734.2)"
     CDS             1..264
                     /gene="Comt"
                     /coded_by="NM_012531.2:168..962"
                     /db_xref="GeneID:24267"
                     /db_xref="RGD:2379"
ORIGIN      
        1 mplaavslgl lllalllllr hlgwglvtif wfeyvlqpvh nlimgdtkeq rilryvqqna
       61 kpgdpqsvle aidtyctqke wamnvgdakg qimdavirey spslvlelga ycgysavrma
      121 rllqpgarll tmemnpdyaa itqqmlnfag lqdkvtilng asqdlipqlk kkydvdtldm
      181 vfldhwkdry lpdtlllekc gllrkgtvll adnvivpgtp dflayvrgss sfecthyssy
      241 leymkvvdgl ekaiyqgpss pdks
//
LOCUS       NP_001004447             685 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis-associated protein 21 [Rattus norvegicus].
ACCESSION   NP_001004447 XP_345596
VERSION     NP_001004447.1
DBSOURCE    REFSEQ: accession NM_001004447.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Iida,H., Yamashita,H., Doiguchi,M. and Kaneko,T.
  TITLE     Molecular cloning of rat Spergen-3, a spermatogenic cell-specific
            gene-3, encoding a novel 75-kDa protein bearing EF-hand motifs
  JOURNAL   J Androl 25 (6), 885-892 (2004)
   PUBMED   15477360
  REMARK    GeneRIF: Potential role of Spergen-3, a new member of EF-hand
            family, in differentiation of haploid spermatids in testis.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB168097.1.
            
            On Sep 17, 2004 this sequence version replaced XP_345596.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB168097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..685
                     /product="spermatogenesis-associated protein 21"
                     /note="spergen-3; spermatogenic cell-specific gene 3
                     protein"
                     /calculated_mol_wt=75695
     Region          1..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68A65.1)"
     Region          <36..397
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          302..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68A65.1)"
     Region          439..498
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(447,449,456,481,483,485,492)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Region          656..685
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68A65.1)"
     CDS             1..685
                     /gene="Spata21"
                     /gene_synonym="Spergen3"
                     /coded_by="NM_001004447.1:265..2322"
                     /db_xref="GeneID:366491"
                     /db_xref="RGD:1302954"
ORIGIN      
        1 menrnththp enkaeaptvq sssglsstkk ktdleaavaa gqngradate rdsrkkpaap
       61 rgpekeprht assqersgep qtqeqrpsar skttqdgpre lqtgqeqarp sgdfvasegr
      121 pqpamqtkdq qkrwqsaeak dvqstescqg ntdhdlgkpc tsdsrshpqk tnslseggrp
      181 qarlqepmpa pssgthkdnp qeavppkpkv taeekkappv lptvprthkd rgeaveskas
      241 prppppppsp ppppppeerd vekkelgqgq kqrqpalaaa gtqgpgnfrr gfmkclleve
      301 eqeeathrrt lksraltarr spktvtsvpt sgpvnssvpp lpptlhepst sapatvpswv
      361 kppapgqapi pmgtpssvlp tpaqdqswrw pellpqgner nlnyaktrqe seehglfkly
      421 qnweerteeh ltlkqeeafr syfdifngpg evdarslkni llligftftp aqveealmsa
      481 dvngdghvdf kdflavmtdt krffcsveqn vlmdmsppnp ytlffeilsl lvemlalpev
      541 aleeitnyyq kklkegsska remetamggi rqrkkipyss qqvenlevpe rrvlrilsrl
      601 kqqnyaanlq spyaqvpcip lcprldkkav rrkqashnhs vldqcvptsl gpdlhgfflq
      661 pgqqgsrehs sdsrkwlssv parth
//
LOCUS       NP_001026817             258 aa            linear   ROD 27-APR-2025
DEFINITION  axonemal dynein light intermediate polypeptide 1 [Rattus
            norvegicus].
ACCESSION   NP_001026817 XP_233519
VERSION     NP_001026817.1
DBSOURCE    REFSEQ: accession NM_001031647.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Whitfield,M., Thomas,L., Bequignon,E., Schmitt,A., Stouvenel,L.,
            Montantin,G., Tissier,S., Duquesnoy,P., Copin,B., Chantot,S.,
            Dastot,F., Faucon,C., Barbotin,A.L., Loyens,A., Siffroi,J.P.,
            Papon,J.F., Escudier,E., Amselem,S., Mitchell,V., Toure,A. and
            Legendre,M.
  TITLE     Mutations in DNAH17, Encoding a Sperm-Specific Axonemal Outer
            Dynein Arm Heavy Chain, Cause Isolated Male Infertility Due to
            Asthenozoospermia
  JOURNAL   Am J Hum Genet 105 (1), 198-212 (2019)
   PUBMED   31178125
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Mali,G.R., Yeyati,P.L., Mizuno,S., Dodd,D.O., Tennant,P.A.,
            Keighren,M.A., Zur Lage,P., Shoemark,A., Garcia-Munoz,A.,
            Shimada,A., Takeda,H., Edlich,F., Takahashi,S., von Kreigsheim,A.,
            Jarman,A.P. and Mill,P.
  TITLE     ZMYND10 functions in a chaperone relay during axonemal dynein
            assembly
  JOURNAL   Elife 7, e34389 (2018)
   PUBMED   29916806
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Abdelhamed,Z., Vuong,S.M., Hill,L., Shula,C., Timms,A., Beier,D.,
            Campbell,K., Mangano,F.T., Stottmann,R.W. and Goto,J.
  TITLE     A mutation in Ccdc39 causes neonatal hydrocephalus with abnormal
            motile cilia development in mice
  JOURNAL   Development 145 (1) (2018)
   PUBMED   29317443
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Jeanson,L., Thomas,L., Copin,B., Coste,A., Sermet-Gaudelus,I.,
            Dastot-Le Moal,F., Duquesnoy,P., Montantin,G., Collot,N.,
            Tissier,S., Papon,J.F., Clement,A., Louis,B., Escudier,E.,
            Amselem,S. and Legendre,M.
  TITLE     Mutations in GAS8, a Gene Encoding a Nexin-Dynein Regulatory
            Complex Subunit, Cause Primary Ciliary Dyskinesia with Axonemal
            Disorganization
  JOURNAL   Hum Mutat 37 (8), 776-785 (2016)
   PUBMED   27120127
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Dougherty,G.W., Loges,N.T., Klinkenbusch,J.A., Olbrich,H.,
            Pennekamp,P., Menchen,T., Raidt,J., Wallmeier,J., Werner,C.,
            Westermann,C., Ruckert,C., Mirra,V., Hjeij,R., Memari,Y.,
            Durbin,R., Kolb-Kokocinski,A., Praveen,K., Kashef,M.A., Kashef,S.,
            Eghtedari,F., Haffner,K., Valmari,P., Baktai,G., Aviram,M.,
            Bentur,L., Amirav,I., Davis,E.E., Katsanis,N., Brueckner,M.,
            Shaposhnykov,A., Pigino,G., Dworniczak,B. and Omran,H.
  TITLE     DNAH11 Localization in the Proximal Region of Respiratory Cilia
            Defines Distinct Outer Dynein Arm Complexes
  JOURNAL   Am J Respir Cell Mol Biol 55 (2), 213-224 (2016)
   PUBMED   26909801
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Hjeij,R., Lindstrand,A., Francis,R., Zariwala,M.A., Liu,X., Li,Y.,
            Damerla,R., Dougherty,G.W., Abouhamed,M., Olbrich,H., Loges,N.T.,
            Pennekamp,P., Davis,E.E., Carvalho,C.M., Pehlivan,D., Werner,C.,
            Raidt,J., Kohler,G., Haffner,K., Reyes-Mugica,M., Lupski,J.R.,
            Leigh,M.W., Rosenfeld,M., Morgan,L.C., Knowles,M.R., Lo,C.W.,
            Katsanis,N. and Omran,H.
  TITLE     ARMC4 mutations cause primary ciliary dyskinesia with randomization
            of left/right body asymmetry
  JOURNAL   Am J Hum Genet 93 (2), 357-367 (2013)
   PUBMED   23849778
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Loges,N.T., Olbrich,H., Becker-Heck,A., Haffner,K., Heer,A.,
            Reinhard,C., Schmidts,M., Kispert,A., Zariwala,M.A., Leigh,M.W.,
            Knowles,M.R., Zentgraf,H., Seithe,H., Nurnberg,G., Nurnberg,P.,
            Reinhardt,R. and Omran,H.
  TITLE     Deletions and point mutations of LRRC50 cause primary ciliary
            dyskinesia due to dynein arm defects
  JOURNAL   Am J Hum Genet 85 (6), 883-889 (2009)
   PUBMED   19944400
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Rashid,S., Breckle,R., Hupe,M., Geisler,S., Doerwald,N. and
            Neesen,J.
  TITLE     The murine Dnali1 gene encodes a flagellar protein that interacts
            with the cytoplasmic dynein heavy chain 1
  JOURNAL   Mol Reprod Dev 73 (6), 784-794 (2006)
   PUBMED   16496424
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099087.1.
            
            On Aug 12, 2005 this sequence version replaced XP_233519.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            23 bp suspected to be vector contamination from the 5' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..258
                     /product="axonemal dynein light intermediate polypeptide
                     1"
                     /note="inner dynein arm light chain, axonemal; dynein,
                     axonemal, light intermediate polypeptide 1"
                     /calculated_mol_wt=29491
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZV3.1)"
     Region          66..252
                     /region_name="Ax_dynein_light"
                     /note="Axonemal dynein light chain; pfam10211"
                     /db_xref="CDD:463000"
     Region          202..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZV3.1)"
     CDS             1..258
                     /gene="Dnali1"
                     /coded_by="NM_001031647.1:3..779"
                     /db_xref="GeneID:298524"
                     /db_xref="RGD:1309260"
ORIGIN      
        1 mippadsllk ydtpvlvsrn tekrspkarp lkvtvqqpgp sgagpqppka klpstscvpd
       61 ptkqaeeiln ailpprewve dtqlwiqqvs stpstrmdvv hlqeqldlkl qqrqaretgi
      121 cpvrrelysq cfdelirevt incaerglll lrvrdeirmt iaayqtlyes svafgmrkal
      181 qaeqgksdme rkiteletek rdlerqvneq kakceatekr eserrqveek khneeiqflk
      241 rtnqqlkaql egiiapkk
//
LOCUS       NP_001012765             216 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 12 [Rattus norvegicus].
ACCESSION   NP_001012765 XP_343286
VERSION     NP_001012765.1
DBSOURCE    REFSEQ: accession NM_001012747.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Henras,A.K., Plisson-Chastang,C., O'Donohue,M.F., Chakraborty,A.
            and Gleizes,P.E.
  TITLE     An overview of pre-ribosomal RNA processing in eukaryotes
  JOURNAL   Wiley Interdiscip Rev RNA 6 (2), 225-242 (2015)
   PUBMED   25346433
  REMARK    Review article
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Sloan,K.E., Mattijssen,S., Lebaron,S., Tollervey,D., Pruijn,G.J.
            and Watkins,N.J.
  TITLE     Both endonucleolytic and exonucleolytic cleavage mediate ITS1
            removal during human ribosomal RNA processing
  JOURNAL   J Cell Biol 200 (5), 577-588 (2013)
   PUBMED   23439679
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Fujiwara,T., Suzuki,S., Kanno,M., Sugiyama,H., Takahashi,H. and
            Tanaka,J.
  TITLE     Mapping a nucleolar targeting sequence of an RNA binding nucleolar
            protein, Nop25
  JOURNAL   Exp Cell Res 312 (10), 1703-1712 (2006)
   PUBMED   16515785
  REMARK    GeneRIF: These data suggest that the nucleolar targeting sequence
            might play an important role in the binding of Nop25 to RNA
            molecules and that the RNA binding of Nop25 might be essential for
            the nucleolar localization of Nop25.
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Suzuki,S., Kanno,M., Fujiwara,T., Sugiyama,H., Yokoyama,A.,
            Takahashi,H. and Tanaka,J.
  TITLE     Molecular cloning and characterization of Nop25, a novel nucleolar
            RNA binding protein, highly conserved in vertebrate species
  JOURNAL   Exp Cell Res 312 (7), 1031-1041 (2006)
   PUBMED   16430885
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC103643.1.
            
            On Apr 20, 2005 this sequence version replaced XP_343286.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103643.1, AY917132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..216
                     /product="nucleolar protein 12"
                     /note="nucleolar protein, 25 kDa; 25 kDa nucleolar
                     protein"
                     /calculated_mol_wt=25055
     Region          20..>67
                     /region_name="Nop25"
                     /note="Nucleolar protein 12 (25kDa); pfam09805"
                     /db_xref="CDD:430839"
     Region          120..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5D1Z3.1)"
     CDS             1..216
                     /gene="Nol12"
                     /gene_synonym="Nop25; RGD1305327"
                     /coded_by="NM_001012747.2:23..673"
                     /db_xref="GeneID:362955"
                     /db_xref="RGD:1305327"
ORIGIN      
        1 mgrnkkkkrd gddrrprlil nfdeekrrey ltgfhkrkve rkkaaieeik qrlkqeqkkl
       61 reerhqeylk mlaereeale eadelerlvt aktesvqydh pnhtvtvttv sdldlsgarl
      121 lglplpeqgd qdgsqeeevs smekptkalp kkskdpllsq rissltatlh ahsrkkvkrk
      181 hprraqdstk kppsatrtsk tqrrrrmtgk arhnge
//
LOCUS       NP_446433                427 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 12 [Rattus
            norvegicus].
ACCESSION   NP_446433
VERSION     NP_446433.2
DBSOURCE    REFSEQ: accession NM_053981.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Seyler,C., Scherer,D., Kopple,C., Kulzer,M., Korkmaz,S.,
            Xynogalos,P., Thomas,D., Kaya,Z., Scholz,E., Backs,J., Karle,C.,
            Katus,H.A. and Zitron,E.
  TITLE     Role of plasma membrane-associated AKAPs for the regulation of
            cardiac IK1 current by protein kinase A
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 390 (5), 493-503 (2017)
   PUBMED   28331977
  REMARK    GeneRIF: Report coupling of cardiac Kir2.1 and Kir2.2 subunits with
            the plasma membrane-bound AKAPs 15 and 79. Cardiac
            membrane-associated AKAPs are a functionally essential part of the
            regulatory cascade determining IK1 current function.
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Matamoros,M., Perez-Hernandez,M., Guerrero-Serna,G., Amoros,I.,
            Barana,A., Nunez,M., Ponce-Balbuena,D., Sacristan,S., Gomez,R.,
            Tamargo,J., Caballero,R., Jalife,J. and Delpon,E.
  TITLE     Nav1.5 N-terminal domain binding to alpha1-syntrophin increases
            membrane density of human Kir2.1, Kir2.2 and Nav1.5 channels
  JOURNAL   Cardiovasc Res 110 (2), 279-290 (2016)
   PUBMED   26786162
  REMARK    GeneRIF: Nav1.5 N-terminal domain binding to alpha1-syntrophin
            increases membrane density of human Kir2.1, Kir2.2 and Nav1.5
            channels
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Murata,Y., Yasaka,T., Takano,M. and Ishihara,K.
  TITLE     Neuronal and glial expression of inward rectifier potassium channel
            subunits Kir2.x in rat dorsal root ganglion and spinal cord
  JOURNAL   Neurosci Lett 617, 59-65 (2016)
   PUBMED   26854211
  REMARK    GeneRIF: Kir2 channels composed of Kir2.1-2.3 subunits are
            expressed in neuronal and glial cells in the DRG and spinal cord,
            contributing to sensory transduction and motor control.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Li,J., Blankenship,M.L. and Baccei,M.L.
  TITLE     Inward-rectifying potassium (Kir) channels regulate pacemaker
            activity in spinal nociceptive circuits during early life
  JOURNAL   J Neurosci 33 (8), 3352-3362 (2013)
   PUBMED   23426663
  REMARK    GeneRIF: Immunohistochemical analysis reveals the expression of
            Kir2.1, Kir2.2, and Kir2.3 within spontaneously bursting neurons
            that regulate the level of pacemaker activity within the developing
            superficial dorsal horn.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Hansen,S.B., Tao,X. and MacKinnon,R.
  TITLE     Structural basis of PIP2 activation of the classical inward
            rectifier K+ channel Kir2.2
  JOURNAL   Nature 477 (7365), 495-498 (2011)
   PUBMED   21874019
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Chwalisz,W.T., Koelsch,B.U., Kindler-Rohrborn,A., Hedrich,H.J. and
            Wedekind,D.
  TITLE     The circling behavior of the deafblind LEW-ci2 rat is linked to a
            segment of RNO10 containing Myo15 and Kcnj12
  JOURNAL   Mamm Genome 14 (9), 620-627 (2003)
   PUBMED   14629112
  REMARK    GeneRIF: Myo15 and Kcnj12 can be regarded as candidate genes for
            the deafblind phenotype of the LEW-ci2 rat.
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Pruss,H., Wenzel,M., Eulitz,D., Thomzig,A., Karschin,A. and
            Veh,R.W.
  TITLE     Kir2 potassium channels in rat striatum are strategically localized
            to control basal ganglia function
  JOURNAL   Brain Res Mol Brain Res 110 (2), 203-219 (2003)
   PUBMED   12591157
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Chen,L., Kawano,T., Bajic,S., Kaziro,Y., Itoh,H., Art,J.J.,
            Nakajima,Y. and Nakajima,S.
  TITLE     A glutamate residue at the C terminus regulates activity of inward
            rectifier K+ channels: implication for Andersen's syndrome
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8430-8435 (2002)
   PUBMED   12034888
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Leonoudakis,D., Mailliard,W., Wingerd,K., Clegg,D. and
            Vandenberg,C.
  TITLE     Inward rectifier potassium channel Kir2.2 is associated with
            synapse-associated protein SAP97
  JOURNAL   J Cell Sci 114 (Pt 5), 987-998 (2001)
   PUBMED   11181181
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Koyama,H., Morishige,K., Takahashi,N., Zanelli,J.S., Fass,D.N. and
            Kurachi,Y.
  TITLE     Molecular cloning, functional expression and localization of a
            novel inward rectifier potassium channel in the rat brain
  JOURNAL   FEBS Lett 341 (2-3), 303-307 (1994)
   PUBMED   8137958
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127487.1.
            
            On Nov 13, 2006 this sequence version replaced NP_446433.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127487.1, DY319566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..427
                     /product="ATP-sensitive inward rectifier potassium channel
                     12"
                     /note="inward rectifier K(+) channel Kir2.2; potassium
                     channel, inwardly rectifying subfamily J member 12; IRK-2;
                     potassium voltage-gated channel subfamily J member 12"
                     /calculated_mol_wt=48283
     Region          2..46
                     /region_name="IRK_N"
                     /note="Inward rectifier potassium channel N-terminal;
                     pfam08466"
                     /db_xref="CDD:462486"
     Region          47..187
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            78..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52188.1)"
     Region          143..148
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:F1NHE9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52188.1)"
     Site            156..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P52188.1)"
     Site            173
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P52188.1)"
     Region          194..366
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Region          387..427
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52188.1)"
     Region          425..427
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P52188.1)"
     CDS             1..427
                     /gene="Kcnj12"
                     /gene_synonym="IRK2; Kir2.1; Kir2.2"
                     /coded_by="NM_053981.2:333..1616"
                     /db_xref="GeneID:117052"
                     /db_xref="RGD:621660"
ORIGIN      
        1 mtaasranpy sivsseedgl hlvtmsgang fgngkvhtrr rcrnrfvkkn gqcniefanm
       61 deksqrylad mfttcvdirw rymllifsla flaswllfgi ifwviavahg dlepaegrgr
      121 tpcvlqvhgf maaflfsiet qttigyglrc vteecpvavf mvvaqsivgc iidsfmigai
      181 makmarpkkr aqtllfshna vvalrdgklc lmwrvgnlrk shiveahvra qlikprvtee
      241 geyipldqid idvgfdkgld riflvspiti lheideaspl fgisrqdlet ddfeivvile
      301 gmveatamtt qarssylane ilwghrfepv lfeeknqyki dyshfhktye vpstprcsak
      361 dlvenkfllp sansfcyene laflsrdeed evatdrdgrs pqpehdfdrl qassgalerp
      421 yrresei
//
LOCUS       NP_001099187             572 aa            linear   ROD 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 2 [Rattus norvegicus].
ACCESSION   NP_001099187 XP_001067745 XP_573810
VERSION     NP_001099187.1
DBSOURCE    REFSEQ: accession NM_001105717.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Rahamim,N., Liran,M., Aronovici,C., Flumin,H., Gordon,T.,
            Urshansky,N. and Barak,S.
  TITLE     Inhibition of ERK1/2 or CRMP2 Disrupts Alcohol Memory
            Reconsolidation and Prevents Relapse in Rats
  JOURNAL   Int J Mol Sci 25 (10), 5478 (2024)
   PUBMED   38791516
  REMARK    GeneRIF: Inhibition of ERK1/2 or CRMP2 Disrupts Alcohol Memory
            Reconsolidation and Prevents Relapse in Rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Martinez-Alonso,E., Escobar-Peso,A., Guerra-Perez,N., Roca,M.,
            Masjuan,J. and Alcazar,A.
  TITLE     Dihydropyrimidinase-Related Protein 2 Is a New Partner in the
            Binding between 4E-BP2 and eIF4E Related to Neuronal Death after
            Cerebral Ischemia
  JOURNAL   Int J Mol Sci 24 (9), 8246 (2023)
   PUBMED   37175950
  REMARK    GeneRIF: Dihydropyrimidinase-Related Protein 2 Is a New Partner in
            the Binding between 4E-BP2 and eIF4E Related to Neuronal Death
            after Cerebral Ischemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Li,Y., Tong,F., Zhang,Y., Cai,Y., Ding,J., Wang,Q. and Wang,X.
  TITLE     Neuropilin-2 Signaling Modulates Mossy Fiber Sprouting by
            Regulating Axon Collateral Formation Through CRMP2 in a Rat Model
            of Epilepsy
  JOURNAL   Mol Neurobiol 59 (11), 6817-6833 (2022)
   PUBMED   36044155
  REMARK    GeneRIF: Neuropilin-2 Signaling Modulates Mossy Fiber Sprouting by
            Regulating Axon Collateral Formation Through CRMP2 in a Rat Model
            of Epilepsy.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Li,Y., Tong,F., Liu,L., Su,Z., Ding,J., Wang,Q. and Wang,X.
  TITLE     CRMP2 modulates mossy fiber sprouting in dentate gyrus of
            pilocarpine induced rat model of epilepsy
  JOURNAL   Biochem Biophys Res Commun 605, 141-147 (2022)
   PUBMED   35334412
  REMARK    GeneRIF: CRMP2 modulates mossy fiber sprouting in dentate gyrus of
            pilocarpine induced rat model of epilepsy.
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Fazil,M.H.U.T., Prasannan,P., Wong,B.H.S., Kottaiswamy,A.,
            Salim,N.S.B.M., Sze,S.K. and Verma,N.K.
  TITLE     GSK3beta Interacts With CRMP2 and Notch1 and Controls T-Cell
            Motility
  JOURNAL   Front Immunol 12, 680071 (2021)
   PUBMED   34975828
  REMARK    GeneRIF: GSK3beta Interacts With CRMP2 and Notch1 and Controls
            T-Cell Motility.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Wong,C.C. and Leung,M.S.
  TITLE     Effects of neonatal hypothyroidism on the expressions of growth
            cone proteins and axon guidance molecules related genes in the
            hippocampus
  JOURNAL   Mol Cell Endocrinol 184 (1-2), 143-150 (2001)
   PUBMED   11694350
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Gu,Y., Hamajima,N. and Ihara,Y.
  TITLE     Neurofibrillary tangle-associated collapsin response mediator
            protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518,
            and Ser-522
  JOURNAL   Biochemistry 39 (15), 4267-4275 (2000)
   PUBMED   10757975
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Wang,L.H. and Strittmatter,S.M.
  TITLE     Brain CRMP forms heterotetramers similar to liver
            dihydropyrimidinase
  JOURNAL   J Neurochem 69 (6), 2261-2269 (1997)
   PUBMED   9375656
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Geschwind,D.H., Kelly,G.M., Fryer,H., Feeser-Bhatt,H. and
            Hockfield,S.
  TITLE     Identification and characterization of novel developmentally
            regulated proteins in rat spinal cord
  JOURNAL   Brain Res Dev Brain Res 97 (1), 62-75 (1996)
   PUBMED   8946055
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Minturn,J.E., Fryer,H.J., Geschwind,D.H. and Hockfield,S.
  TITLE     TOAD-64, a gene expressed early in neuronal differentiation in the
            rat, is related to unc-33, a C. elegans gene involved in axon
            outgrowth
  JOURNAL   J Neurosci 15 (10), 6757-6766 (1995)
   PUBMED   7472434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB749736.1, JAXUCZ010000015.1, CB729753.1, CA510768.1 and
            CB577285.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001067745.1, XP_573810.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.52343.1,
                                           SRR26643291.37161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..572
                     /product="dihydropyrimidinase-related protein 2"
                     /note="DRP-2; CRMP-2; turned on after division, 64 kDa
                     protein; collapsin response mediator protein 2"
                     /calculated_mol_wt=62147
     Region          17..466
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(28..29,31,44..45,180,201,204,207,230,234,238,241,
                     268..269,271..272,390,395,400)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000250|UniProtKB:Q16555; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            order(73,75,165,198,254,332)
                     /site_type="active"
                     /db_xref="CDD:238639"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            486
                     /site_type="other"
                     /note="Not phosphorylated; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:10757975, ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Region          512..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47942.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16555; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10757975; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10757975; Phosphoserine, by
                     DYRK2. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:O02675; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     Site            565
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O08553; propagated from
                     UniProtKB/Swiss-Prot (P47942.1)"
     CDS             1..572
                     /gene="Dpysl2"
                     /gene_synonym="Crmp2; TOAD-64"
                     /coded_by="NM_001105717.2:225..1943"
                     /db_xref="GeneID:25416"
                     /db_xref="RGD:2517"
ORIGIN      
        1 msyqgkknip ritsdrllik ggkivnddqs fyadiymedg likqigenli vpggvktiea
       61 hsrmvipggi dvhtrfqmpd qgmtsaddff qgtkaalagg ttmiidhvvp epgtsllaaf
      121 dqwrewadsk sccdyslhvd itewhkgiqe emealvkdhg vnsflvymaf kdrfqltdsq
      181 iyevlsvird igaiaqvhae ngdiiaeeqq rildlgitgp eghvlsrpee veaeavnrsi
      241 tianqtncpl yvtkvmsksa aeviaqarkk gtvvygepit aslgtdgshy wsknwakaaa
      301 fvtspplspd pttpdflnsl lscgdlqvtg sahctfntaq kavgkdnftl ipegtngtee
      361 rmsviwdkav vtgkmdenqf vavtstnaak vfnlyprkgr isvgsdadlv iwdpdsvkti
      421 sakthnsale ynifegmecr gsplvvisqg kivledgtlh vtegsgryip rkpfpdfvyk
      481 rikarsrlae lrgvprglyd gpvcevsvtp ktvtpassak tspakqqapp vrnlhqsgfs
      541 lsgaqiddni prrttqriva ppggranits lg
//
LOCUS       NP_001012141             443 aa            linear   ROD 27-APR-2025
DEFINITION  transcriptional adapter 2-alpha [Rattus norvegicus].
ACCESSION   NP_001012141 XP_340863
VERSION     NP_001012141.1
DBSOURCE    REFSEQ: accession NM_001012141.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Krebs,A.R., Demmers,J., Karmodiya,K., Chang,N.C., Chang,A.C. and
            Tora,L.
  TITLE     ATAC and Mediator coactivators form a stable complex and regulate a
            set of non-coding RNA genes
  JOURNAL   EMBO Rep 11 (7), 541-547 (2010)
   PUBMED   20508642
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Saad,Y., Garrett,M.R., Manickavasagam,E., Yerga-Woolwine,S.,
            Farms,P., Radecki,T. and Joe,B.
  TITLE     Fine-mapping and comprehensive transcript analysis reveals
            nonsynonymous variants within a novel 1.17 Mb blood pressure QTL
            region on rat chromosome 10
  JOURNAL   Genomics 89 (3), 343-353 (2007)
   PUBMED   17218081
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079084.1.
            
            On Feb 11, 2005 this sequence version replaced XP_340863.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079084.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..443
                     /product="transcriptional adapter 2-alpha"
                     /note="ADA2-like protein"
                     /calculated_mol_wt=51268
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75478; propagated from
                     UniProtKB/Swiss-Prot (Q6AYE3.1)"
     Region          28..440
                     /region_name="COG5114"
                     /note="Histone acetyltransferase complex SAGA/ADA, subunit
                     ADA2 [Chromatin structure and dynamics]"
                     /db_xref="CDD:227445"
     CDS             1..443
                     /gene="Tada2a"
                     /gene_synonym="Tada2l"
                     /coded_by="NM_001012141.1:162..1493"
                     /db_xref="GeneID:360581"
                     /db_xref="RGD:1309959"
ORIGIN      
        1 mdrlgsfsnd psdkppcrgc ssylmepyik caecgpppff lclqcftrgf eykkhqsdht
       61 yeimtsdfpv ldpswtaqee malleavmdc gfgnwqdvan qmctktkeec ekhymkhfin
      121 nplfastlln lkqaeaakta dtaipfhsad dpprpafdsl lsrdmagymp aradfieefd
      181 nyaewdlrdi dfveddsdil halkmavvdi yhsrlkerqr rkkiirdhgl vnlrkfrlme
      241 rrypkevqdl yetmrrfari vgpvehdkfi eshalefelr reikrlqeyr tagitnfcsa
      301 rtydhlkktr eeerlkrtml sevlqyiqds sacqqwlrrq adidsglsps vlmasnsgrr
      361 sapplnltgl pgteklneke kelcqvvrlv pgayleyksa llnechkqgg lrlaqarali
      421 kidvnktrki ydfliregyi tka
//
LOCUS       NP_612552                534 aa            linear   ROD 27-APR-2025
DEFINITION  high affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
            [Rattus norvegicus].
ACCESSION   NP_612552
VERSION     NP_612552.1
DBSOURCE    REFSEQ: accession NM_138543.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Dungan,J.R., Qin,X., Gregory,S.G., Cooper-Dehoff,R., Duarte,J.D.,
            Qin,H., Gulati,M., Taylor,J.Y., Pepine,C.J., Hauser,E.R. and
            Kraus,W.E.
  TITLE     Sex-dimorphic gene effects on survival outcomes in people with
            coronary artery disease
  JOURNAL   Am Heart J Plus 17 (2022)
   PUBMED   35959094
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Mishra,S., Sadagopan,N., Dunkerly-Eyring,B., Rodriguez,S.,
            Sarver,D.C., Ceddia,R.P., Murphy,S.A., Knutsdottir,H., Jani,V.P.,
            Ashok,D., Oeing,C.U., O'Rourke,B., Gangoiti,J.A., Sears,D.D.,
            Wong,G.W., Collins,S. and Kass,D.A.
  TITLE     Inhibition of phosphodiesterase type 9 reduces obesity and
            cardiometabolic syndrome in mice
  JOURNAL   J Clin Invest 131 (21) (2021)
   PUBMED   34618683
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Besler,C., Rommel,K.P., Kresoja,K.P., Morbitz,J., Kirsten,H.,
            Scholz,M., Klingel,K., Thiery,J., Burkhardt,R., Buttner,P.,
            Adams,V., Thiele,H. and Lurz,P.
  TITLE     Evaluation of phosphodiesterase 9A as a novel biomarker in heart
            failure with preserved ejection fraction
  JOURNAL   ESC Heart Fail 8 (3), 1861-1872 (2021)
   PUBMED   33787083
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Richards,D.A., Aronovitz,M.J., Liu,P., Martin,G.L., Tam,K.,
            Pande,S., Karas,R.H., Bloomfield,D.M., Mendelsohn,M.E. and
            Blanton,R.M.
  TITLE     CRD-733, a Novel PDE9 (Phosphodiesterase 9) Inhibitor, Reverses
            Pressure Overload-Induced Heart Failure
  JOURNAL   Circ Heart Fail 14 (1), e007300 (2021)
   PUBMED   33464954
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Huan,X., Oumei,C., Hongmei,Q., Junxia,Y., Xiaojiao,M. and
            Qingsong,J.
  TITLE     PDE9 inhibition promotes proliferation of neural stem cells via
            cGMP-PKG pathway following oxygen-glucose deprivation/reoxygenation
            injury in vitro
  JOURNAL   Neurochem Int 133, 104630 (2020)
   PUBMED   31821840
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Kruse,L.S., Moller,M., Tibaek,M., Gammeltoft,S., Olesen,J. and
            Kruuse,C.
  TITLE     PDE9A, PDE10A, and PDE11A expression in rat trigeminovascular pain
            signalling system
  JOURNAL   Brain Res 1281, 25-34 (2009)
   PUBMED   19445908
  REMARK    GeneRIF: We here present, for the first time, the expression of
            PDE9A, PDE10A, and PDE11A in the trigeminovascular system;
            localisation indicates that they may have a role in pain pathways
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 534)
  AUTHORS   van Staveren,W.C., Glick,J., Markerink-van Ittersum,M., Shimizu,M.,
            Beavo,J.A., Steinbusch,H.W. and de Vente,J.
  TITLE     Cloning and localization of the cGMP-specific phosphodiesterase
            type 9 in the rat brain
  JOURNAL   J Neurocytol 31 (8-9), 729-741 (2002)
   PUBMED   14501210
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Fisher,D.A., Smith,J.F., Pillar,J.S., St Denis,S.H. and Cheng,J.B.
  TITLE     Isolation and characterization of PDE9A, a novel human
            cGMP-specific phosphodiesterase
  JOURNAL   J Biol Chem 273 (25), 15559-15564 (1998)
   PUBMED   9624146
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Soderling,S.H., Bayuga,S.J. and Beavo,J.A.
  TITLE     Identification and characterization of a novel family of cyclic
            nucleotide phosphodiesterases
  JOURNAL   J Biol Chem 273 (25), 15553-15558 (1998)
   PUBMED   9624145
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF372654.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF372654.1, BC161837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..534
                     /product="high affinity cGMP-specific 3',5'-cyclic
                     phosphodiesterase 9A"
                     /EC_number="3.1.4.35"
                     /calculated_mol_wt=61625
     Region          250..478
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q8QZV1.1)"
     Region          500..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8QZV1.1)"
     CDS             1..534
                     /gene="Pde9a"
                     /coded_by="NM_138543.1:43..1647"
                     /db_xref="GeneID:191569"
                     /db_xref="RGD:621035"
ORIGIN      
        1 mgagsssyrp kaiyldidgr iqkvvfskyc nssdimdlfc iatglprntt isllttddam
       61 vsidptmpan sertpykvrp vavkqvsere elvqgvlaqv aeqfsrafki nelkaevanh
      121 lamlekrvel eglkvveiek cksdikkmre elaarnnrtn cpckysfldn kkltprrdvp
      181 typkyllspe tiealrkptf dvwlwepnem lsclehmyhd lglvrdfsin pitlrrwllc
      241 vhdnyrsnpf hnfrhcfcvt qmmysmvwlc glqekfsqmd ilvlmtaaic hdldhpgynn
      301 tyqinartel avryndispl enhhcaiafq ilarpecnif asvppegfrq irqgmitlil
      361 atdmarhaei mdsfkekmen fdysneehlt llkmilikcc disnevrpme vaepwvdcll
      421 eeyfmqsdre kseglpvapf mdrdkvtkat aqigfikfvl ipmfetvtkl fpiveetmlr
      481 plwesrehye elkqlddamk elqkktenlt sgatenapek trdakdnedr sppn
//
LOCUS       NP_703195                440 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction alpha-8 protein [Rattus norvegicus].
ACCESSION   NP_703195
VERSION     NP_703195.2
DBSOURCE    REFSEQ: accession NM_153465.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Seda,O., Liska,F., Pravenec,M., Vernerova,Z., Kazdova,L.,
            Krenova,D., Zidek,V., Sedova,L., Krupkova,M. and Kren,V.
  TITLE     Connexin 50 mutation lowers blood pressure in spontaneously
            hypertensive rat
  JOURNAL   Physiol Res 66 (1), 15-28 (2017)
   PUBMED   27782748
  REMARK    GeneRIF: The connexin 50 mutation lowers blood pressure in the
            spontaneously hypertensive rat.
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Seda,O., Krenova,D., Oliyarnyk,O., Sedova,L., Krupkova,M.,
            Liska,F., Chylikova,B., Kazdova,L. and Kren,V.
  TITLE     Heterozygous connexin 50 mutation affects metabolic syndrome
            attributes in spontaneously hypertensive rat
  JOURNAL   Lipids Health Dis 15 (1), 199 (2016)
   PUBMED   27871290
  REMARK    GeneRIF: Gja8 mutation L7Q in heterozygous state affects the lipid
            profile and the oxidative stress parameters in the spontaneously
            hypertensive rat strain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Rodriguez-Jimenez,F.J., Alastrue,A., Stojkovic,M., Erceg,S. and
            Moreno-Manzano,V.
  TITLE     Connexin 50 modulates Sox2 expression in spinal-cord-derived
            ependymal stem/progenitor cells
  JOURNAL   Cell Tissue Res 365 (2), 295-307 (2016)
   PUBMED   27221278
  REMARK    GeneRIF: Cx50 might constitute an interesting mechanism for Sox2
            induction to modulate the endogenous regenerative potential of
            neuronal tissue with a potential application in regenerative
            therapies.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Pinto,B.I., Garcia,I.E., Pupo,A., Retamal,M.A., Martinez,A.D.,
            Latorre,R. and Gonzalez,C.
  TITLE     Charged Residues at the First Transmembrane Region Contribute to
            the Voltage Dependence of the Slow Gate of Connexins
  JOURNAL   J Biol Chem 291 (30), 15740-15752 (2016)
   PUBMED   27143357
  REMARK    GeneRIF: the role of the charged residues at the end of TM-1 in
            voltage sensing in Cx26, Cx46, and Cx50.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Rodriguez-Jimenez,F.J., Alastrue-Agudo,A., Stojkovic,M., Erceg,S.
            and Moreno-Manzano,V.
  TITLE     Connexin 50 Expression in Ependymal Stem Progenitor Cells after
            Spinal Cord Injury Activation
  JOURNAL   Int J Mol Sci 16 (11), 26608-26618 (2015)
   PUBMED   26561800
  REMARK    GeneRIF: Upon ependymal stem cells differentiation, Cx50 expression
            favors glial cell fate, since higher expression levels, endogenous
            or by over-expression of Cx50, augmented the expression of the
            astrocyte marker GFAP and impaired the neuronal marker Tuj1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Zampighi,G.A.
  TITLE     Distribution of connexin50 channels and hemichannels in lens
            fibers: a structural approach
  JOURNAL   Cell Commun Adhes 10 (4-6), 265-270 (2003)
   PUBMED   14681027
  REMARK    GeneRIF: In lens fibers, Cx50 hemichannels are inserted via
            exocytosis and are rapidly assembled into channels assembled in gap
            junction plaques.
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Yamashita,S., Furumoto,K., Nobukiyo,A., Kamohara,M., Ushijima,T.
            and Furukawa,T.
  TITLE     Mapping of A gene responsible for cataract formation and its
            modifier in the UPL rat
  JOURNAL   Invest Ophthalmol Vis Sci 43 (10), 3153-3159 (2002)
   PUBMED   12356818
  REMARK    GeneRIF: A candidate gene for formation of cataracts in UPL rats
            was mapped to rat chr 2, and the Cx50 gene was a strong candidate.
            A potential modifier gene was mapped on chr 5.
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Rong,P., Wang,X., Niesman,I., Wu,Y., Benedetti,L.E., Dunia,I.,
            Levy,E. and Gong,X.
  TITLE     Disruption of Gja8 (alpha8 connexin) in mice leads to
            microphthalmia associated with retardation of lens growth and lens
            fiber maturation
  JOURNAL   Development 129 (1), 167-174 (2002)
   PUBMED   11782410
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Gao,Y. and Spray,D.C.
  TITLE     Structural changes in lenses of mice lacking the gap junction
            protein connexin43
  JOURNAL   Invest Ophthalmol Vis Sci 39 (7), 1198-1209 (1998)
   PUBMED   9620080
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Favor,J.
  TITLE     A comparison of the dominant cataract and recessive specific-locus
            mutation rates induced by treatment of male mice with
            ethylnitrosourea
  JOURNAL   Mutat Res 110 (2), 367-382 (1983)
   PUBMED   6877261
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EU445788.1.
            
            On Jul 11, 2008 this sequence version replaced NP_703195.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /strain="SHR-dca"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..440
                     /product="gap junction alpha-8 protein"
                     /note="connexin-50; gap junction membrane channel protein
                     alpha 8; connexin l"
                     /calculated_mol_wt=49299
     Region          3..235
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Region          111..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Site            162..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Site            211..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Region          267..333
                     /region_name="Connexin50"
                     /note="Gap junction alpha-8 protein (Cx50); pfam03509"
                     /db_xref="CDD:460951"
     Region          334..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4Q9.1)"
     Region          <419..440
                     /region_name="Connexin40_C"
                     /note="Connexin 40 C-terminal domain; cl46284"
                     /db_xref="CDD:480624"
     CDS             1..440
                     /gene="Gja8"
                     /gene_synonym="Cx50; Cxnl"
                     /coded_by="NM_153465.2:78..1400"
                     /db_xref="GeneID:29601"
                     /db_xref="RGD:628890"
ORIGIN      
        1 mgdwsfqgni leevnehstv igrvwltvlf ifrililgta aefvwgdeqs dfvcntqqpg
       61 cenvcydeaf pishirlwvl qiifvstpsl myvghavhhv rmeekrkdre aeelcqqsrs
      121 nggervpiap dqasirksss sskgtkkfrl egtllrtyvc hiifktlfev gfivghyfly
      181 gfrilplyrc srwpcpnvvd cfvsrptekt ifilfmlsva fvslflnime mshlgmkgir
      241 safkrpaeqp lgeiaekslh siavssiqka kgyqlleeek ivshyfplte vgmvetspls
      301 akpfsqfeek igtgpladms rgyqetlpsy aqvgaqever eeqpveeave pelgekkqea
      361 ekvapegqet vavpdgekve tpgvgkddek eelqaekvtk qglsaekapt lcpelttddn
      421 rplsrlskas srarsddlti
//
LOCUS       NP_001013901             624 aa            linear   ROD 27-APR-2025
DEFINITION  uncharacterized protein C19orf44 homolog [Rattus norvegicus].
ACCESSION   NP_001013901 XP_214317
VERSION     NP_001013901.1
DBSOURCE    REFSEQ: accession NM_001013879.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079430.1.
            
            On Apr 20, 2005 this sequence version replaced XP_214317.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079430.1, SRR8487231.143936.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..624
                     /product="uncharacterized protein C19orf44 homolog"
                     /calculated_mol_wt=68113
     Region          108..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP1.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6X5; propagated from
                     UniProtKB/Swiss-Prot (Q6AXP1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXP1.1)"
     Region          217..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP1.1)"
     Region          305..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP1.1)"
     Region          428..581
                     /region_name="DUF4614"
                     /note="Domain of unknown function (DUF4614); pfam15391"
                     /db_xref="CDD:464698"
     CDS             1..624
                     /gene="C16h19orf44"
                     /gene_synonym="RGD1311847"
                     /coded_by="NM_001013879.1:60..1934"
                     /db_xref="GeneID:290615"
                     /db_xref="RGD:1311847"
ORIGIN      
        1 mastrrpfgp phgafdfrdm ffdsskmeei rnvqarslgq mapgqsrilk rnqtmdekyl
       61 lpkeealagt gvrlslrppt issksrasea lrklaqietk ilkrrqvpta wsgmesdsta
      121 serslpqrtd ttsvssqypl rtfqkqvckt svvgddgqsg kgsrflkkke lpaearspvl
      181 aaetekqvll ptqreparky dapdsdeeem kvllgslmes sgekerngnq elpgtrsdlg
      241 kvfldltpdq pgvlcllsad qsslkstsvs lraqslqtrs ggdpasltts psilrddfsr
      301 sasskrecik lasspsrmet esseepvsea aadslhdfri nilsiddlvl adgyksdgeq
      361 kgvttvvede edltteheis ehpgasstaa vwshsmssar smetptalsv spvysedfeq
      421 fsgplalees ldrtldtlsk fssgeqtdtv srqplsrtew grgvtrvvke tavqtldpaf
      481 ayqwtkaggm aaigptlggg yvdpvpiash iisadaieal tayspavlal ndmlkqqlsl
      541 tqqfieashh lhhsllrsld edsfhyhtle eakeyirchr papltmeaal qevrkelevh
      601 ldindshvea skaaalpaep idgl
//
LOCUS       NP_001014041             449 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein H2 [Rattus norvegicus].
ACCESSION   NP_001014041 XP_218703
VERSION     NP_001014041.1
DBSOURCE    REFSEQ: accession NM_001014019.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Grammatikakis,I., Zhang,P., Panda,A.C., Kim,J., Maudsley,S.,
            Abdelmohsen,K., Yang,X., Martindale,J.L., Motino,O.,
            Hutchison,E.R., Mattson,M.P. and Gorospe,M.
  TITLE     Alternative Splicing of Neuronal Differentiation Factor TRF2
            Regulated by HNRNPH1/H2
  JOURNAL   Cell Rep 15 (5), 926-934 (2016)
   PUBMED   27117401
  REMARK    GeneRIF: HNRNPH is a splicing regulator of Trf2 pre-mRNA that
            prevents the expression of TRF2-S, a factor implicated in neuronal
            differentiation.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Maggi,L.B. Jr., Kuchenruether,M., Dadey,D.Y., Schwope,R.M.,
            Grisendi,S., Townsend,R.R., Pandolfi,P.P. and Weber,J.D.
  TITLE     Nucleophosmin serves as a rate-limiting nuclear export chaperone
            for the Mammalian ribosome
  JOURNAL   Mol Cell Biol 28 (23), 7050-7065 (2008)
   PUBMED   18809582
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Mauger,D.M., Lin,C. and Garcia-Blanco,M.A.
  TITLE     hnRNP H and hnRNP F complex with Fox2 to silence fibroblast growth
            factor receptor 2 exon IIIc
  JOURNAL   Mol Cell Biol 28 (17), 5403-5419 (2008)
   PUBMED   18573884
  REMARK    GeneRIF: These results establish hnRNP H and hnRNP F as being
            repressors of exon inclusion and suggest that Fox proteins enhance
            their ability to antagonize ASF/SF2.
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Li,K.W., Hornshaw,M.P., Van Der Schors,R.C., Watson,R., Tate,S.,
            Casetta,B., Jimenez,C.R., Gouwenberg,Y., Gundelfinger,E.D.,
            Smalla,K.H. and Smit,A.B.
  TITLE     Proteomics analysis of rat brain postsynaptic density. Implications
            of the diverse protein functional groups for the integration of
            synaptic physiology
  JOURNAL   J Biol Chem 279 (2), 987-1002 (2004)
   PUBMED   14532281
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079240.1.
            
            On Apr 20, 2005 this sequence version replaced XP_218703.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079240.1, EV769547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..449
                     /product="heterogeneous nuclear ribonucleoprotein H2"
                     /note="hnRNP H'; hnRNP H2; heterogeneous nuclear
                     ribonucleoprotein H'; heterogeneous nuclear
                     ribonucleoprotein H2 (H')"
                     /calculated_mol_wt=49163
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein H2, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70333; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            233
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P31943;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P55795; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Region          234..433
                     /region_name="2 X 16 AA Gly-rich approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY09.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31943; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Region          257..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Region          289..364
                     /region_name="RRM3_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12734"
                     /db_xref="CDD:410133"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55795; propagated from
                     UniProtKB/Swiss-Prot (Q6AY09.1)"
     Region          354..392
                     /region_name="2 X 19 AA perfect repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY09.1)"
     CDS             1..449
                     /gene="Hnrnph2"
                     /gene_synonym="Hnrph2"
                     /coded_by="NM_001014019.1:225..1574"
                     /db_xref="GeneID:308650"
                     /db_xref="RGD:1549784"
ORIGIN      
        1 mmlstegreg fvvkvrglpw scsaeevmrf fsdckiqngt sgvrfiytre grpsgeafve
       61 lesedevkla lkkdretmgh ryvevfksns vemdwvlkht gpnspdtand gfvrlrglpf
      121 gcskeeivqf fsgleivpng mtlpvdfqgr stgeafvqfa sqeiaekalk khkerighry
      181 ieifkssrae vrthydpprk lmtmqrpgpy drpgagrgyn sigrgagfer mrrgaygggy
      241 ggyddyggyn dgygfgsdrf grdlnycfsg msdhrygdgg ssfqsttghc vhmrglpyra
      301 tendiynffs plnpmrvhie igpdgrvtge advefathed avaamakdka nmqhryvelf
      361 lnstagtsgg aydhsyvelf lnstagasgg aygsqmmggm glsnqssygg pasqqlsagy
      421 gggyggqssm sgydqvlqen ssdyqsnla
//
LOCUS       NP_112274                965 aa            linear   ROD 27-APR-2025
DEFINITION  aminopeptidase N precursor [Rattus norvegicus].
ACCESSION   NP_112274
VERSION     NP_112274.1
DBSOURCE    REFSEQ: accession NM_031012.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 965)
  AUTHORS   Cheng,R., Xu,X., Yang,S., Mi,Z., Zhao,Y., Wang,C., Shi,X., Gao,J.,
            Yu,F. and Ren,X.
  TITLE     The effect of APN, hs-CRP and APN/hs-CRP in periodontitis with DAA
  JOURNAL   BMC Oral Health 23 (1), 85 (2023)
   PUBMED   36765308
  REMARK    GeneRIF: The effect of APN, hs-CRP and APN/hs-CRP in periodontitis
            with DAA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 965)
  AUTHORS   Minocha,E., Chaturvedi,C.P. and Nityanand,S.
  TITLE     Renogenic characterization and in vitro differentiation of rat
            amniotic fluid stem cells into renal proximal tubular- and
            juxtaglomerular-like cells
  JOURNAL   In Vitro Cell Dev Biol Anim 55 (2), 138-147 (2019)
   PUBMED   30645697
REFERENCE   3  (residues 1 to 965)
  AUTHORS   Dominguez-Vias,G., Aretxaga-Maza,G., Prieto,I., Segarra,A.B.,
            Luna,J.D., Gasparo,M. and Ramirez-Sanchez,M.
  TITLE     Light-dark influence on enkephalinase activity in hypothalamus and
            pituitary
  JOURNAL   Neuro Endocrinol Lett 39 (4), 277-280 (2018)
   PUBMED   30531704
  REMARK    GeneRIF: In standard light/dark conditions, the results
            demonstrated an opposite daily rhythm in hypothalamus and
            pituitary. While the highest levels of AlaAP or enkephalinase
            activities were measured in hypothalamus during the dark period,
            they were the highest in the pituitary during the light one.
REFERENCE   4  (residues 1 to 965)
  AUTHORS   Byzia,A., Szeffler,A., Kalinowski,L. and Drag,M.
  TITLE     Activity profiling of aminopeptidases in cell lysates using a
            fluorogenic substrate library
  JOURNAL   Biochimie 122, 31-37 (2016)
   PUBMED   26449746
  REMARK    GeneRIF: Data indicate that fluorogenic substrates can be
            successfully used to identify aminopeptidase N and to measure their
            activity in cell lysates.
REFERENCE   5  (residues 1 to 965)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   6  (residues 1 to 965)
  AUTHORS   Yeager,C.L., Ashmun,R.A., Williams,R.K., Cardellichio,C.B.,
            Shapiro,L.H., Look,A.T. and Holmes,K.V.
  TITLE     Human aminopeptidase N is a receptor for human coronavirus 229E
  JOURNAL   Nature 357 (6377), 420-422 (1992)
   PUBMED   1350662
REFERENCE   7  (residues 1 to 965)
  AUTHORS   Funkhouser,J.D., Tangada,S.D., Jones,M., O,S.J. and Peterson,R.D.
  TITLE     p146 type II alveolar epithelial cell antigen is identical to
            aminopeptidase N
  JOURNAL   Am J Physiol 260 (4 Pt 1), L274-L279 (1991)
   PUBMED   1673322
REFERENCE   8  (residues 1 to 965)
  AUTHORS   Malfroy,B., Kado-Fong,H., Gros,C., Giros,B., Schwartz,J.C. and
            Hellmiss,R.
  TITLE     Molecular cloning and amino acid sequence of rat kidney
            aminopeptidase M: a member of a super family of
            zinc-metallohydrolases
  JOURNAL   Biochem Biophys Res Commun 161 (1), 236-241 (1989)
   PUBMED   2567164
REFERENCE   9  (residues 1 to 965)
  AUTHORS   Watt,V.M. and Yip,C.C.
  TITLE     Amino acid sequence deduced from a rat kidney cDNA suggests it
            encodes the Zn-peptidase aminopeptidase N
  JOURNAL   J Biol Chem 264 (10), 5480-5487 (1989)
   PUBMED   2564389
REFERENCE   10 (residues 1 to 965)
  AUTHORS   Look,A.T., Ashmun,R.A., Shapiro,L.H. and Peiper,S.C.
  TITLE     Human myeloid plasma membrane glycoprotein CD13 (gp150) is
            identical to aminopeptidase N
  JOURNAL   J Clin Invest 83 (4), 1299-1307 (1989)
   PUBMED   2564851
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M25073.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M25073.1, M26710.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132280,
                                           SAMD00132282 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..965
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..965
                     /product="aminopeptidase N precursor"
                     /EC_number="3.4.11.2"
                     /note="leucine arylaminopeptidase 1; aminopeptidase N;
                     cluster of differentiation antigen 13 (CD13);
                     aminopeptidase M; kidney Zn peptidase; microsomal
                     aminopeptidase; membrane alanine aminopeptidase; kidney
                     aminopeptidase M; alanyl (membrane) aminopeptidase"
                     /calculated_mol_wt=109449
     Site            9..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P15684.2)"
     sig_peptide     11..32
                     /note="kidney Zn-peptidase signal peptide"
                     /calculated_mol_wt=2109
     mat_peptide     33..965
                     /product="aminopeptidase N"
                     /calculated_mol_wt=106231
     Region          33..68
                     /region_name="Cytosolic Ser/Thr-rich junction"
                     /note="propagated from UniProtKB/Swiss-Prot (P15684.2)"
     Region          44..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15684.2)"
     Region          69..965
                     /region_name="Metalloprotease"
                     /note="propagated from UniProtKB/Swiss-Prot (P15684.2)"
     Region          84..545
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            176
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P15684.2)"
     Site            order(211,213,351..354,387..388,391,410,414,471,476)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Site            234
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            476
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            555
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            606
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Region          618..945
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
     Site            624
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            780
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97449; propagated from
                     UniProtKB/Swiss-Prot (P15684.2)"
     CDS             1..965
                     /gene="Anpep"
                     /gene_synonym="AP-M; AP-N; Apm; Apn; KZP; Lap1; rAPN"
                     /coded_by="NM_031012.1:20..2917"
                     /db_xref="GeneID:81641"
                     /db_xref="RGD:2991"
ORIGIN      
        1 makgfyiskt lgilgillgv aavctiials vvyaqeknrn aensaiaptl pgstsattst
       61 tnpaideskp wnqyrlpktl ipdsyqvtlr pyltpneqgl yifkgsstvr ftcnettnvi
      121 iihskklnyt nkgnhrvalr algdtpapni dttelverte ylvvhlqgsl vkghqyemds
      181 efqgeladdl agfyrseyme ggnkkvvatt qmqaadarks fpcfdepamk asfnitlihp
      241 nnltalsnml pkdsrtlqed pswnvtefhp tpkmstylla yivsefkyve avspnrvqir
      301 iwarpsaide ghgdyalqvt gpilnffaqh yntaypleks dqialpdfna gamenwglvt
      361 yresalvfdp qsssisnker vvtviahela hqwfgnlvtv dwwndlwlne gfasyveflg
      421 adyaeptwnl kdlivlndvy rvmavdalas shplsspane vntpaqisel fdsityskga
      481 svlrmlssfl tedlfkkgls sylhtfqysn tiyldlwehl qqavdsqtai klpasvstim
      541 drwilqmgfp vitvntstge iyqehflldp tskptrpsdf nylwivpipy lkngkedhyw
      601 leteknqsae fqtssnewll lninvtgyyq vnydennwrk iqnqlqtdls vipvinraqi
      661 ihdsfnlasa gklsitlpls ntlflasete ympweaalss lnyfklmfdr sevygpmkry
      721 lkkqvtplfa yfkiktnnwl drpptlmeqy neinaistac ssgleecrdl vvglysqwmn
      781 nsdnnpihpn lrstvycnai afggeeewnf aweqfrkatl vneadklrsa lacsnevwil
      841 nrylsytlnp dyirkqdats tivsiannvv gqtlvwdfvr snwkklfedy gggsfsfanl
      901 iqgvtrrfss efelqqleqf kednsatgfg sgtraleqal ektkanikwv kenkdvvlkw
      961 ftens
//
LOCUS       NP_001100580             277 aa            linear   ROD 27-APR-2025
DEFINITION  carbonyl reductase [NADPH] 3 [Rattus norvegicus].
ACCESSION   NP_001100580 XP_001055098 XP_221641
VERSION     NP_001100580.1
DBSOURCE    REFSEQ: accession NM_001107110.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Karanges,E.A., Kashem,M.A., Sarker,R., Ahmed,E.U., Ahmed,S., Van
            Nieuwenhuijzen,P.S., Kemp,A.H. and McGregor,I.S.
  TITLE     Hippocampal protein expression is differentially affected by
            chronic paroxetine treatment in adolescent and adult rats: a
            possible mechanism of 'paradoxical' antidepressant responses in
            young persons
  JOURNAL   Front Pharmacol 4, 86 (2013)
   PUBMED   23847536
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Swaminathan,S., Huentelman,M.J., Corneveaux,J.J., Myers,A.J.,
            Faber,K.M., Foroud,T., Mayeux,R., Shen,L., Kim,S., Turk,M.,
            Hardy,J., Reiman,E.M. and Saykin,A.J.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative  and  NIA-LOAD/NCRAD
            Family Study Group
  TITLE     Analysis of copy number variation in Alzheimer's disease in a
            cohort of clinically characterized and neuropathologically verified
            individuals
  JOURNAL   PLoS One 7 (12), e50640 (2012)
   PUBMED   23227193
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Thorn,C.F., Oshiro,C., Marsh,S., Hernandez-Boussard,T., McLeod,H.,
            Klein,T.E. and Altman,R.B.
  TITLE     Doxorubicin pathways: pharmacodynamics and adverse effects
  JOURNAL   Pharmacogenet Genomics 21 (7), 440-446 (2011)
   PUBMED   21048526
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Miura,T., Itoh,Y., Takada,M., Tsutsui,H., Yukimura,T., Nishinaka,T.
            and Terada,T.
  TITLE     Investigation of the role of the amino acid residue at position 230
            for catalysis in monomeric carbonyl reductase 3
  JOURNAL   Chem Biol Interact 178 (1-3), 211-214 (2009)
   PUBMED   18983987
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Mordente,A., Meucci,E., Silvestrini,A., Martorana,G.E. and
            Giardina,B.
  TITLE     New developments in anthracycline-induced cardiotoxicity
  JOURNAL   Curr Med Chem 16 (13), 1656-1672 (2009)
   PUBMED   19442138
  REMARK    Review article
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Miura,T., Nishinaka,T. and Terada,T.
  TITLE     Different functions between human monomeric carbonyl reductase 3
            and carbonyl reductase 1
  JOURNAL   Mol Cell Biochem 315 (1-2), 113-121 (2008)
   PUBMED   18493841
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Ohkura-Hada,S., Kondoh,N., Hada,A., Arai,M., Yamazaki,Y.,
            Shindoh,M., Kitagawa,Y., Takahashi,M., Ando,T., Sato,Y. and
            Yamamoto,M.
  TITLE     Carbonyl Reductase 3 (CBR3) Mediates 9-cis-Retinoic Acid-Induced
            Cytostatis and is a Potential Prognostic Marker for Oral Malignancy
  JOURNAL   Open Dent J 2, 78-88 (2008)
   PUBMED   19088887
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474083.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001055098.1, XP_221641.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ234106.1, BC166553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..277
                     /product="carbonyl reductase [NADPH] 3"
                     /EC_number="1.1.1.184"
                     /EC_number="1.6.5.10"
                     /note="quinone reductase CBR3; monomeric carbonyl
                     reductase 3"
                     /calculated_mol_wt=30710
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P16152; propagated from
                     UniProtKB/Swiss-Prot (B2GV72.1)"
     Region          6..277
                     /region_name="carb_red_PTCR-like_SDR_c"
                     /note="Porcine testicular carbonyl reductase (PTCR)-like,
                     classical (c) SDRs; cd05324"
                     /db_xref="CDD:187585"
     Site            order(12,14..17,38,42,62..64,90..93,113,138..140,194,198,
                     227..231,233..236)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187585"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48758; propagated from
                     UniProtKB/Swiss-Prot (B2GV72.1)"
     Site            order(94..95,140..142,145,194,227,229..230,235..236)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187585"
     Site            order(114,140,194,198)
                     /site_type="active"
                     /db_xref="CDD:187585"
     CDS             1..277
                     /gene="Cbr3"
                     /coded_by="NM_001107110.1:112..945"
                     /db_xref="GeneID:304078"
                     /db_xref="RGD:1309728"
ORIGIN      
        1 msscsrvalv tgankgigfa itrdlcrkfs gdvvltarde argraavkql qaeglsprfh
       61 qldidnpqsi ralrdflrke ygglnvlvnn agiafrmddp tpfdvqaevt lktnffatrn
      121 vctellpimk phgrvvnvss lqglkalenc sedlqerfrc dtltegdlvd lmkkfvedtk
      181 nevheregwp dsaygvsklg vtvltrilar qldekrkadr illnaccpgw vktdmardqg
      241 srtveegaet pvylallppd atephgqlvr dkvvqtw
//
LOCUS       NP_598238                465 aa            linear   ROD 27-APR-2025
DEFINITION  sodium-dependent phosphate transport protein 1 [Rattus norvegicus].
ACCESSION   NP_598238
VERSION     NP_598238.2
DBSOURCE    REFSEQ: accession NM_133554.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Sakiyama,M., Matsuo,H., Nagamori,S., Ling,W., Kawamura,Y.,
            Nakayama,A., Higashino,T., Chiba,T., Ichida,K., Kanai,Y. and
            Shinomiya,N.
  TITLE     Expression of a human NPT1/SLC17A1 missense variant which increases
            urate export
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 35 (10-12), 536-542 (2016)
   PUBMED   27906618
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Kolz,M., Johnson,T., Sanna,S., Teumer,A., Vitart,V., Perola,M.,
            Mangino,M., Albrecht,E., Wallace,C., Farrall,M., Johansson,A.,
            Nyholt,D.R., Aulchenko,Y., Beckmann,J.S., Bergmann,S., Bochud,M.,
            Brown,M., Campbell,H., Connell,J., Dominiczak,A., Homuth,G.,
            Lamina,C., McCarthy,M.I., Meitinger,T., Mooser,V., Munroe,P.,
            Nauck,M., Peden,J., Prokisch,H., Salo,P., Salomaa,V., Samani,N.J.,
            Schlessinger,D., Uda,M., Volker,U., Waeber,G., Waterworth,D.,
            Wang-Sattler,R., Wright,A.F., Adamski,J., Whitfield,J.B.,
            Gyllensten,U., Wilson,J.F., Rudan,I., Pramstaller,P., Watkins,H.,
            Doering,A., Wichmann,H.E., Spector,T.D., Peltonen,L., Volzke,H.,
            Nagaraja,R., Vollenweider,P., Caulfield,M., Illig,T. and Gieger,C.
  CONSRTM   EUROSPAN Consortium; ENGAGE Consortium; PROCARDIS Consortium; KORA
            Study; WTCCC
  TITLE     Meta-analysis of 28,141 individuals identifies common variants
            within five new loci that influence uric acid concentrations
  JOURNAL   PLoS Genet 5 (6), e1000504 (2009)
   PUBMED   19503597
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Hinojos,C.A., Boerwinkle,E., Fornage,M. and Doris,P.A.
  TITLE     Combined genealogical, mapping, and expression approaches to
            identify spontaneously hypertensive rat hypertension candidate
            genes
  JOURNAL   Hypertension 45 (4), 698-704 (2005)
   PUBMED   15710778
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Alvarez,F.J., Villalba,R.M., Zerda,R. and Schneider,S.P.
  TITLE     Vesicular glutamate transporters in the spinal cord, with special
            reference to sensory primary afferent synapses
  JOURNAL   J Comp Neurol 472 (3), 257-280 (2004)
   PUBMED   15065123
  REMARK    GeneRIF: VGLUT1 localization (most abundant in LIII/LIV and medial
            LV of sponal cord) is consistent with an origin from cutaneous and
            muscle mechanoreceptors and disappeared after rhizotomy.
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Landry,M., Bouali-Benazzouz,R., El Mestikawy,S., Ravassard,P. and
            Nagy,F.
  TITLE     Expression of vesicular glutamate transporters in rat lumbar spinal
            cord, with a note on dorsal root ganglia
  JOURNAL   J Comp Neurol 468 (3), 380-394 (2004)
   PUBMED   14681932
  REMARK    GeneRIF: VGLUT1 and VGLUT2 transcripts are colocalized in most
            sensory neurons of the dorsal root ganglia, as well as in motor
            neurons of the ventral horn.
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Li,J.L., Xiong,K.H., Dong,Y.L., Fujiyama,F., Kaneko,T. and
            Mizuno,N.
  TITLE     Vesicular glutamate transporters, VGluT1 and VGluT2, in the
            trigeminal ganglion neurons of the rat, with special reference to
            coexpression
  JOURNAL   J Comp Neurol 463 (2), 212-220 (2003)
   PUBMED   12815758
  REMARK    GeneRIF: More than 80% of trigeminal ganglion neurons express
            vesicular glutamate transporter (VGluT)1 and VGluT2. VGluT1 is
            coexpressed with VGluT2 in the cell bodies and axon terminals in
            most trigeminal ganglion neurons.
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Li,J.L., Fujiyama,F., Kaneko,T. and Mizuno,N.
  TITLE     Expression of vesicular glutamate transporters, VGluT1 and VGluT2,
            in axon terminals of nociceptive primary afferent fibers in the
            superficial layers of the medullary and spinal dorsal horns of the
            rat
  JOURNAL   J Comp Neurol 457 (3), 236-249 (2003)
   PUBMED   12541308
  REMARK    GeneRIF: Both VGluT1 and VGluT2 were expressed in axon terminals of
            primary afferent fibers, including SP-containing nociceptive fibers
            and that VGluT in unmyelinated primary afferent fibers terminating
            in lamina II was primarily VGluT2.
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Minelli,A., Edwards,R.H., Manzoni,T. and Conti,F.
  TITLE     Postnatal development of the glutamate vesicular transporter VGLUT1
            in rat cerebral cortex
  JOURNAL   Brain Res Dev Brain Res 140 (2), 309-314 (2003)
   PUBMED   12586437
  REMARK    GeneRIF: VGLUT is localized to puncta coexpressing synaptophysin.
            Faint at birth, increases in subplate during first postnatal week,
            invades supragranular layers in second week and reaches adult
            pattern at P20-P30.
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Hioki,H., Fujiyama,F., Taki,K., Tomioka,R., Furuta,T., Tamamaki,N.
            and Kaneko,T.
  TITLE     Differential distribution of vesicular glutamate transporters in
            the rat cerebellar cortex
  JOURNAL   Neuroscience 117 (1), 1-6 (2003)
   PUBMED   12605886
  REMARK    GeneRIF: In the cerebellar granular layer, vesicular glutamate
            transporter 1 (Slc17a1) immunoreactivity is found in mossy fiber
            terminals and in single-axon terminals and in most brainstem
            precerebellar nuclei sending mossy fibers.
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Li,H. and Xie,Z.
  TITLE     Molecular cloning of two rat Na+/Pi cotransporters: evidence for
            differential tissue expression of transcripts
  JOURNAL   Cell Mol Biol Res 41 (5), 451-460 (1995)
   PUBMED   8867793
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078748.1.
            
            On Aug 8, 2004 this sequence version replaced NP_598238.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..465
                     /product="sodium-dependent phosphate transport protein 1"
                     /note="solute carrier family 17 vesicular glutamate
                     transporter), member 1; sodium/phosphate cotransporter 1;
                     renal sodium-phosphate transport protein 1; renal
                     Na(+)-dependent phosphate cotransporter 1; solute carrier
                     family 17 (sodium phosphate), member 1; renal
                     sodium-dependent phosphate transport protein 1; Na(+)/PI
                     cotransporter 1; solute carrier family 17 (organic anion
                     transporter), member 1"
                     /calculated_mol_wt=51266
     Region          1..464
                     /region_name="2A0114euk"
                     /note="Na(+)-dependent inorganic phosphate cotransporter;
                     TIGR00894"
                     /db_xref="CDD:129972"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62795.1)"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62795.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62795.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            337..357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            363..383
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            399..419
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     Site            431..451
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62795.1)"
     CDS             1..465
                     /gene="Slc17a1"
                     /gene_synonym="Napi-1"
                     /coded_by="NM_133554.2:145..1542"
                     /db_xref="GeneID:171080"
                     /db_xref="RGD:620099"
ORIGIN      
        1 menrclpkkv pgfcsfrygl aillhfcniv imaqrvclnl tmvamvnkte pphlsnksva
       61 emldnvknpv hswsldiqgl ilssvflgmv viqvpvgyls gaypmkkiig sslflssvls
      121 llippaaqvg aalvivcrvl qgiaqgavst gqhgiwvkwa pplergrlts mtlsgfvmgp
      181 fiallvsgfi cdllgwpmvf yifgivgcvl slfwfilffd dpnnhpymss sekdyitssl
      241 mqqvhsgrqs lpikamlksl plwaiilnsf afiwsnnllv tytptfistt lhvnvrengl
      301 lsslpyllay icgivagqms dfllsrkifs vvavrklftt lgifcpvifv vcllylsynf
      361 ystvifltla nstlsfsfcg qlinaldiap ryygflkavt aligifggli sstlagliln
      421 qdpeyawhkn fflmaginvt clafyllfak gdiqdwaket kttrl
//
LOCUS       NP_077380                353 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein D0 isoform a [Rattus
            norvegicus].
ACCESSION   NP_077380
VERSION     NP_077380.2
DBSOURCE    REFSEQ: accession NM_024404.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Yan,J., Du,F., Li,S.D., Yuan,Y., Jiang,J.Y., Li,S., Li,X.Y. and
            Du,Z.X.
  TITLE     AUF1 modulates TGF-beta signal in renal tubular epithelial cells
            via post-transcriptional regulation of Nedd4L expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (1), 48-56 (2018)
   PUBMED   28986222
  REMARK    GeneRIF: AUF1 might be a potential player in renal
            tubulointerstitial fibrosis through modulation of TGF-beta signal
            transduction via posttranscriptional regulation of Nedd4L.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Castellanos-Rubio,A., Fernandez-Jimenez,N., Kratchmarov,R., Luo,X.,
            Bhagat,G., Green,P.H., Schneider,R., Kiledjian,M., Bilbao,J.R. and
            Ghosh,S.
  TITLE     A long noncoding RNA associated with susceptibility to celiac
            disease
  JOURNAL   Science 352 (6281), 91-95 (2016)
   PUBMED   27034373
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Lee,K.H., Kim,S.H., Kim,H.J., Kim,W., Lee,H.R., Jung,Y., Choi,J.H.,
            Hong,K.Y., Jang,S.K. and Kim,K.T.
  TITLE     AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
            translation
  JOURNAL   Nucleic Acids Res 42 (6), 3590-3606 (2014)
   PUBMED   24423872
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Raineri,I., Wegmueller,D., Gross,B., Certa,U. and Moroni,C.
  TITLE     Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover
            studied by RNA interference
  JOURNAL   Nucleic Acids Res 32 (4), 1279-1288 (2004)
   PUBMED   14976220
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Arao,Y., Kikuchi,A., Ikeda,K., Nomoto,S., Horiguchi,H. and
            Kayama,F.
  TITLE     A+U-rich-element RNA-binding factor 1/heterogeneous nuclear
            ribonucleoprotein D gene expression is regulated by oestrogen in
            the rat uterus
  JOURNAL   Biochem J 361 (Pt 1), 125-132 (2002)
   PUBMED   11742537
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Ehrenman,K., Long,L., Wagner,B.J. and Brewer,G.
  TITLE     Characterization of cDNAs encoding the murine A+U-rich RNA-binding
            protein AUF1
  JOURNAL   Gene 149 (2), 315-319 (1994)
   PUBMED   7959009
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Ishikawa,F., Matunis,M.J., Dreyfuss,G. and Cech,T.R.
  TITLE     Nuclear proteins that bind the pre-mRNA 3' splice site sequence
            r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
  JOURNAL   Mol Cell Biol 13 (7), 4301-4310 (1993)
   PUBMED   8321232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO567918.1, AB046615.1 and CB798484.1.
            
            On Mar 9, 2007 this sequence version replaced NP_077380.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB046615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..353
                     /product="heterogeneous nuclear ribonucleoprotein D0
                     isoform a"
                     /note="heterogeneous nuclear ribonucleoprotein D0; hnRNP
                     D0; AU-rich element RNA-binding protein 1; AU-rich element
                     RNA-binding factor 1; RNA binding protein p45AUF1"
                     /calculated_mol_wt=38087
     Region          1..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Region          <55..76
                     /region_name="CBFNT"
                     /note="CBFNT (NUC161) domain; pfam08143"
                     /db_xref="CDD:311868"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Region          97..170
                     /region_name="RRM1_hnRNPD"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12756"
                     /db_xref="CDD:410150"
     Site            117
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Region          181..255
                     /region_name="RRM2_hnRNPD"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12583"
                     /db_xref="CDD:241027"
     Site            order(181,183,185..186,210..213,215..216,219..221,223,225,
                     242,249..251,253..255)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:241027"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60668; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            276
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            278
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            280
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q60668; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     Site            343
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60668; Dimethylated
                     arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q14103;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q14103; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ54.2)"
     CDS             1..353
                     /gene="Hnrnpd"
                     /gene_synonym="Auf1; Hnrpd"
                     /coded_by="NM_024404.2:286..1347"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:79256"
                     /db_xref="RGD:620365"
ORIGIN      
        1 mseeqfggdg aaaaataavg gsageqegam vaaaqgaaaa agsgsgggsa pggteggste
       61 aegakidask needeghsns sprhteaata qreewkmfig glswdttkkd lkdyfskfgd
      121 vvdctlkldp itgrsrgfgf vlfkesesvd kvmdqkehkl ngkvidpkra kamktkepvk
      181 kifvgglspd tpeekireyf ggfgevesie lpmdnktnkr rgfcfitfke eepvkkimek
      241 kyhnvglskc eikvamskeq yqqqqqwgsr ggfagrargr gggpsqnwnq gysnywnqgy
      301 gsygynsqgy ggyggydytg ynsyygygdy snqqsgygkv srrgghqnsy kpy
//
LOCUS       NP_001006982             454 aa            linear   ROD 27-APR-2025
DEFINITION  dihydrolipoyllysine-residue succinyltransferase component of
            2-oxoglutarate dehydrogenase complex, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001006982 XP_216753
VERSION     NP_001006982.2
DBSOURCE    REFSEQ: accession NM_001006981.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Remacha,L., Pirman,D., Mahoney,C.E., Coloma,J., Calsina,B.,
            Curras-Freixes,M., Leton,R., Torres-Perez,R., Richter,S., Pita,G.,
            Herraez,B., Cianchetta,G., Honrado,E., Maestre,L., Urioste,M.,
            Aller,J., Garcia-Uriarte,O., Galvez,M.A., Luque,R.M., Lahera,M.,
            Moreno-Rengel,C., Eisenhofer,G., Montero-Conde,C.,
            Rodriguez-Antona,C., Llorca,O., Smolen,G.A., Robledo,M. and
            Cascon,A.
  TITLE     Recurrent Germline DLST Mutations in Individuals with Multiple
            Pheochromocytomas and Paragangliomas
  JOURNAL   Am J Hum Genet 104 (4), 651-664 (2019)
   PUBMED   30929736
  REMARK    Erratum:[Am J Hum Genet. 2019 May 2;104(5):1008-1010. doi:
            10.1016/j.ajhg.2019.04.010. PMID: 31051110]
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Wang,Y., Guo,Y.R., Liu,K., Yin,Z., Liu,R., Xia,Y., Tan,L., Yang,P.,
            Lee,J.H., Li,X.J., Hawke,D., Zheng,Y., Qian,X., Lyu,J., He,J.,
            Xing,D., Tao,Y.J. and Lu,Z.
  TITLE     KAT2A coupled with the alpha-KGDH complex acts as a histone H3
            succinyltransferase
  JOURNAL   Nature 552 (7684), 273-277 (2017)
   PUBMED   29211711
REFERENCE   3  (residues 1 to 454)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Sheu,K.F. and Blass,J.P.
  TITLE     The alpha-ketoglutarate dehydrogenase complex
  JOURNAL   Ann N Y Acad Sci 893, 61-78 (1999)
   PUBMED   10672230
  REMARK    Review article
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Bruschi,S.A., Lindsay,J.G. and Crabb,J.W.
  TITLE     Mitochondrial stress protein recognition of inactivated
            dehydrogenases during mammalian cell death
  JOURNAL   Proc Natl Acad Sci U S A 95 (23), 13413-13418 (1998)
   PUBMED   9811814
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Matuda,S., Kodama,J., Goshi,N., Takase,C., Nakano,K., Nakagawa,S.
            and Ohta,S.
  TITLE     A polypeptide derived from mitochondrial dihydrolipoamide
            succinyltransferase is located on the plasma membrane in skeletal
            muscle
  JOURNAL   Biochem Biophys Res Commun 241 (1), 151-156 (1997)
   PUBMED   9405249
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Nakano,K., Matuda,S., Yamanaka,T., Tsubouchi,H., Nakagawa,S.,
            Titani,K., Ohta,S. and Miyata,T.
  TITLE     Purification and molecular cloning of succinyltransferase of the
            rat alpha-ketoglutarate dehydrogenase complex. Absence of a
            sequence motif of the putative E3 and/or E1 binding site
  JOURNAL   J Biol Chem 266 (28), 19013-19017 (1991)
   PUBMED   1918017
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB807447.1, BC083858.1, CK355938.1 and CK845707.1.
            
            On Aug 6, 2008 this sequence version replaced NP_001006982.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083858.1, D90401.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..454
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial"
                     /EC_number="2.3.1.61"
                     /note="E2; E2K; dihydrolipoamide succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex;
                     2-oxoglutarate dehydrogenase complex component E2;
                     dihydrolipoamide S-succinyltransferase (E2 component of
                     2-oxo-glutarate complex); OGDC-E2"
                     /calculated_mol_wt=41442
     transit_peptide 1..68
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:1918017, ECO:0000269|Ref.3;
                     propagated from UniProtKB/Swiss-Prot (Q01205.2)"
                     /calculated_mol_wt=7476
     mat_peptide     69..454
                     /product="Dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial. /id=PRO_0000020475"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01205.2)"
                     /calculated_mol_wt=41442
     Region          72..454
                     /region_name="sucB"
                     /note="2-oxoglutarate dehydrogenase complex
                     dihydrolipoamide succinyltransferase (E2 component);
                     TIGR01347"
                     /db_xref="CDD:273565"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Region          148..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01205.2)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Site            268
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Site            274
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Site            278
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     Site            308
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (Q01205.2)"
     CDS             1..454
                     /gene="Dlst"
                     /coded_by="NM_001006981.2:44..1408"
                     /db_xref="GeneID:299201"
                     /db_xref="RGD:1359615"
ORIGIN      
        1 mlsrsrcvsr afsrslsafq kgncplgrrs lpgvslcqgp gypdsrkmvi nnssvfsvrf
       61 fqttavcknd vitvqtpafa esvtegdvrw ekavgdavae devvceietd ktsvqvpspa
      121 ngiieallvp dggkveggtp lftlrktgaa pakakpaeap atahkaapea paappppvap
      181 vptqmppvps psqppsskpv saikptaapp laeagaakgl rsehrekmnr mrqriaqrlk
      241 eaqntcamlt tfnevdmsni qemrarhkda flkkhnlklg fmsafvkasa falqeqpvvn
      301 aviddatkev vyrdyidisv avatprglvv pvirnvetmn yadiertine lgekarknel
      361 aiedmdggtf tisnggvfgs lfgtpiinpp qsailgmhgi fdrpvavggk vevrpmmyva
      421 ltydhrlidg reavtflrki kaavedprvl lldl
//
LOCUS       NP_001007635             385 aa            linear   ROD 27-APR-2025
DEFINITION  protein pelota homolog [Rattus norvegicus].
ACCESSION   NP_001007635 XP_215478
VERSION     NP_001007635.1
DBSOURCE    REFSEQ: accession NM_001007634.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Nyamsuren,G., Kata,A., Xu,X., Raju,P., Dressel,R., Engel,W.,
            Pantakani,D.V. and Adham,I.M.
  TITLE     Pelota regulates the development of extraembryonic endoderm through
            activation of bone morphogenetic protein (BMP) signaling
  JOURNAL   Stem Cell Res 13 (1), 61-74 (2014)
   PUBMED   24835669
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Franckenberg,S., Becker,T. and Beckmann,R.
  TITLE     Structural view on recycling of archaeal and eukaryotic ribosomes
            after canonical termination and ribosome rescue
  JOURNAL   Curr Opin Struct Biol 22 (6), 786-796 (2012)
   PUBMED   23031510
  REMARK    Review article
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Adham,I.M., Sallam,M.A., Steding,G., Korabiowska,M., Brinck,U.,
            Hoyer-Fender,S., Oh,C. and Engel,W.
  TITLE     Disruption of the pelota gene causes early embryonic lethality and
            defects in cell cycle progression
  JOURNAL   Mol Cell Biol 23 (4), 1470-1476 (2003)
   PUBMED   12556505
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083637.1.
            
            On Nov 29, 2004 this sequence version replaced XP_215478.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083637.1, FQ214039.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..385
                     /product="protein pelota homolog"
                     /note="pelota homolog"
                     /calculated_mol_wt=43276
     Region          1..370
                     /region_name="aRF1/eRF1"
                     /note="peptide chain release factor 1, archaeal and
                     eukaryotic forms; cl42864"
                     /db_xref="CDD:456209"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIP1.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIP1.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIP1.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIP1.1)"
     CDS             1..385
                     /gene="Pelo"
                     /coded_by="NM_001007634.1:156..1313"
                     /db_xref="GeneID:294754"
                     /db_xref="RGD:1359591"
ORIGIN      
        1 mklvrkdiek dnagqvtlvp eepedmwhty nlvqvgdslr astirkvqte sstgsvgsnr
       61 vrttltlcve aidfdsqacq lrvkgtniqe neyvkmgayh tielepnrqf tlakkqwdsv
      121 vlerieqacd pawsadvaav vmqeglahvc lvtpsmtltr akvevniprk rkgncsqhdr
      181 alerfyeqvv qaiqrhinfe vvkcilvasp gfvreqfcdy mfqqavktdn kvllenrskf
      241 lqvhassghk yslkevlcdp tvasrlsdtk aagevkaldd fykmlqhepd rafyglkqve
      301 ranealaidt llisdelfrh qdvatrsryv rlvdsvkena gtvrifsslh vsgeqlgqlt
      361 gvaailrfpv pelsdqedds sseed
//
LOCUS       NP_036959                408 aa            linear   ROD 27-APR-2025
DEFINITION  bone morphogenetic protein 4 precursor [Rattus norvegicus].
ACCESSION   NP_036959
VERSION     NP_036959.2
DBSOURCE    REFSEQ: accession NM_012827.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Shen,S., Nan,W., Zhang,W., Wu,H. and Zhang,Y.
  TITLE     Bone morphogenetic protein 4 inhibits corneal neovascularization by
            blocking NETs-induced disruption to corneal epithelial barrier
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113023 (2024)
   PUBMED   39217886
  REMARK    GeneRIF: Bone morphogenetic protein 4 inhibits corneal
            neovascularization by blocking NETs-induced disruption to corneal
            epithelial barrier.
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Li,Q., Li,Z., Li,J., Qin,X., Wu,F. and Chen,C.
  TITLE     Bone Morphogenetic Protein-4 Promotes Phenotypic Modulation via
            SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells
  JOURNAL   J Vasc Res 61 (3), 99-108 (2024)
   PUBMED   38151007
  REMARK    GeneRIF: Bone Morphogenetic Protein-4 Promotes Phenotypic
            Modulation via SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Zhou,Y., Yang,Y., Dong,R. and Huang,Y.
  TITLE     Regulation of Shh/Bmp4 Signaling Pathway by DNA Methylation in
            Rectal Nervous System Development of Fetal Rats with Anorectal
            Malformation
  JOURNAL   J Pediatr Surg 58 (7), 1317-1321 (2023)
   PUBMED   36906487
  REMARK    GeneRIF: Regulation of Shh/Bmp4 Signaling Pathway by DNA
            Methylation in Rectal Nervous System Development of Fetal Rats with
            Anorectal Malformation.
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Gao,L.T., Yuan,J.Q., Zhang,Z.Y., Zhao,H.M. and Gao,L.
  TITLE     Hypermethylation of the Bmp4 promoter dampens binding of HIF-1alpha
            and impairs its cardiac protective effects from oxidative stress in
            prenatally GC-exposed offspring
  JOURNAL   Cell Mol Life Sci 80 (3), 58 (2023)
   PUBMED   36746787
  REMARK    GeneRIF: Hypermethylation of the Bmp4 promoter dampens binding of
            HIF-1alpha and impairs its cardiac protective effects from
            oxidative stress in prenatally GC-exposed offspring.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Li,Q., Kou,X., Qin,X., Li,Z., Li,J. and Chen,C.
  TITLE     BMP-4 impedes endothelial cell migration in neointimal hyperplasia
            via FoXO-3 specific modulation of reactive oxygen species
  JOURNAL   Atherosclerosis 351, 9-17 (2022)
   PUBMED   35605369
  REMARK    GeneRIF: BMP-4 impedes endothelial cell migration in neointimal
            hyperplasia via FoXO-3 specific modulation of reactive oxygen
            species.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Winnier,G., Blessing,M., Labosky,P.A. and Hogan,B.L.
  TITLE     Bone morphogenetic protein-4 is required for mesoderm formation and
            patterning in the mouse
  JOURNAL   Genes Dev 9 (17), 2105-2116 (1995)
   PUBMED   7657163
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Johansson,B.M. and Wiles,M.V.
  TITLE     Evidence for involvement of activin A and bone morphogenetic
            protein 4 in mammalian mesoderm and hematopoietic development
  JOURNAL   Mol Cell Biol 15 (1), 141-151 (1995)
   PUBMED   7799920
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Yamaji,N., Celeste,A.J., Thies,R.S., Song,J.J., Bernier,S.M.,
            Goltzman,D., Lyons,K.M., Nove,J., Rosen,V. and Wozney,J.M.
  TITLE     A mammalian serine/threonine kinase receptor specifically binds
            BMP-2 and BMP-4
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1944-1951 (1994)
   PUBMED   7811286
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Phelan,J.P.
  TITLE     Genetic variability and rodent models of human aging
  JOURNAL   Exp Gerontol 27 (2), 147-159 (1992)
   PUBMED   1521591
  REMARK    Review article
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Wozney,J.M., Rosen,V., Celeste,A.J., Mitsock,L.M., Whitters,M.J.,
            Kriz,R.W., Hewick,R.M. and Wang,E.A.
  TITLE     Novel regulators of bone formation: molecular clones and activities
  JOURNAL   Science 242 (4885), 1528-1534 (1988)
   PUBMED   3201241
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078901.1.
            
            On Jun 10, 2007 this sequence version replaced NP_036959.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078901.1, CK478915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676806 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..408
                     /product="bone morphogenetic protein 4 precursor"
                     /note="BMP-4; BMP-2B; bone morphogenetic protein 2B"
                     /calculated_mol_wt=44447
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
                     /calculated_mol_wt=2101
     Region          43..276
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; pfam00688"
                     /db_xref="CDD:459906"
     Region          91..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06826.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12644; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
     Region          281..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06826.1)"
     mat_peptide     293..408
                     /product="Bone morphogenetic protein 4.
                     /id=PRO_0000033863"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06826.1)"
                     /calculated_mol_wt=13155
     Region          302..408
                     /region_name="TGF_beta_BMP4_BMP2B"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in bone morphogenetic protein 4 (BMP-4) and
                     similar proteins; cd19391"
                     /db_xref="CDD:381661"
     Site            order(313,315,319..320,322,332,334..336,353..354,357..358,
                     360..361,364,367..369,372,374..375,378,398..400,402,408)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381661"
     Site            350
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
     Site            365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06826.1)"
     CDS             1..408
                     /gene="Bmp4"
                     /gene_synonym="BOMPR4A"
                     /coded_by="NM_012827.2:139..1365"
                     /db_xref="GeneID:25296"
                     /db_xref="RGD:2213"
ORIGIN      
        1 mipgnrmlmv vllcqvllgg ashaslipet gkkkvaeiqg haggrrsgqs hellrdfeat
       61 llqmfglrrr pqpsksavip dymrdlyrlq sgeeeeeeqs qgtgleyper pasrantvrs
      121 fhheehleni pgtsessafr fffnlssipe nevissaelr lfreqvdqgp dweqgfhrin
      181 iyevmkppae mvpghlitrl ldtrlvhhnv trwetfdvsp avlrwtrekq pnyglaievt
      241 hlhqtrthqg qhvrisrslp qgsgnwaqlr pllvtfghdg rghtltrrra krspkhhpqr
      301 srkknkncrr hslyvdfsdv gwndwivapp gyqafychgd cpfpladhln stnhaivqtl
      361 vnsvnssipk accvptelsa ismlyldeyd kvvlknyqem vvegcgcr
//
LOCUS       NP_620186                514 aa            linear   ROD 27-APR-2025
DEFINITION  monocarboxylate transporter 10 [Rattus norvegicus].
ACCESSION   NP_620186
VERSION     NP_620186.1
DBSOURCE    REFSEQ: accession NM_138831.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Chen,Z., Gao,Y., Huang,X., Yao,Y., Chen,K., Zeng,S. and Mao,W.
  TITLE     Tissue-based metabolomics reveals metabolic biomarkers and
            potential therapeutic targets for esophageal squamous cell
            carcinoma
  JOURNAL   J Pharm Biomed Anal 197, 113937 (2021)
   PUBMED   33609949
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Muller,J., Mayerl,S., Visser,T.J., Darras,V.M., Boelen,A.,
            Frappart,L., Mariotta,L., Verrey,F. and Heuer,H.
  TITLE     Tissue-specific alterations in thyroid hormone homeostasis in
            combined Mct10 and Mct8 deficiency
  JOURNAL   Endocrinology 155 (1), 315-325 (2014)
   PUBMED   24248460
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Kim,D.K., Kanai,Y., Chairoungdua,A., Matsuo,H., Cha,S.H. and
            Endou,H.
  TITLE     Expression cloning of a Na+-independent aromatic amino acid
            transporter with structural similarity to H+/monocarboxylate
            transporters
  JOURNAL   J Biol Chem 276 (20), 17221-17228 (2001)
   PUBMED   11278508
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB047324.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB047324.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..514
                     /product="monocarboxylate transporter 10"
                     /note="MCT 10; aromatic amino acid transporter 1; solute
                     carrier family 16 (monocarboxylic acid transporters),
                     member 10; solute carrier family 16, member 10 (aromatic
                     amino acid transporter); T-type amino acid transporter 1;
                     solute carrier family 16 (aromatic amino acid
                     transporter), member 10"
                     /calculated_mol_wt=55533
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Region          69..469
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(80..81,84..85,88,128,179..180,182..184,187,206,
                     209..210,213,299,302..303,306..308,311,338,342,394..395,
                     399,403,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            200..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            329..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            419..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            451..471
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF71; propagated from
                     UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U9N9; propagated from
                     UniProtKB/Swiss-Prot (Q91Y77.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91Y77.2)"
     CDS             1..514
                     /gene="Slc16a10"
                     /gene_synonym="Tat1"
                     /coded_by="NM_138831.1:192..1736"
                     /db_xref="GeneID:170566"
                     /db_xref="RGD:69197"
ORIGIN      
        1 mvpsleepaa aeretneaqp pgpapsddap lpvpgpsdvs dgsvekveve ltrstgnqep
       61 peppeggwgw lvmlaamwcn gsvfgiqnay gvlfvsmlet fgakdddnma fkaawvgsls
      121 mgmiffccpi vsvftdmfgc rrtavlgaav gfvglmsssf vssieplyft ygvvfacgcs
      181 fayqpslvil ghyfkkrlgl vngivtagss vftillplll gnltstvglc ytlrilcifm
      241 fvlflagfty rplvpsskek esedsrssff srrklsppkk ifnfalfket ayavwaagip
      301 lalfgyfvpy vhlmnhvker fkdvnnkevl fmcigvtsgv grllfgriad ylpgvkkvyl
      361 qvlsfffigl tsmmiplcsv fgalialcli mglfdgcfis imapiafelv gpqdasqaig
      421 fllgfmsipm tvgppvagll hdklgsydla fylagippfi ggavlclipw ihskkqreis
      481 kntggekmek mlanqsslls sssgifkkes dsii
//
LOCUS       NP_640354                357 aa            linear   ROD 27-APR-2025
DEFINITION  hsp70-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_640354
VERSION     NP_640354.1
DBSOURCE    REFSEQ: accession NM_139261.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Al-Ramahi,I., Lam,Y.C., Chen,H.K., de Gouyon,B., Zhang,M.,
            Perez,A.M., Branco,J., de Haro,M., Patterson,C., Zoghbi,H.Y. and
            Botas,J.
  TITLE     CHIP protects from the neurotoxicity of expanded and wild-type
            ataxin-1 and promotes their ubiquitination and degradation
  JOURNAL   J Biol Chem 281 (36), 26714-26724 (2006)
   PUBMED   16831871
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Arndt,V., Daniel,C., Nastainczyk,W., Alberti,S. and Hohfeld,J.
  TITLE     BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin
            ligase CHIP
  JOURNAL   Mol Biol Cell 16 (12), 5891-5900 (2005)
   PUBMED   16207813
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Raynes,D.A. and Guerriero,V.
  TITLE     Isolation and characterization of isoforms of HspBP1, inhibitors of
            Hsp70
  JOURNAL   Biochim Biophys Acta 1490 (1-2), 203-207 (2000)
   PUBMED   10786638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF187860.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF187860.1, BC072541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..357
                     /product="hsp70-binding protein 1"
                     /function="Hsp70 inhibitor"
                     /note="hsp70-interacting protein 1; HSPA binding protein,
                     cytoplasmic cochaperone 1; heat shock protein-binding
                     protein 1; HSPA (heat shock 70kDa) binding protein,
                     cytoplasmic cochaperone 1; HSPA (heat shock 70) binding
                     protein, cytoplasmic cochaperone 1"
                     /calculated_mol_wt=39046
     Region          1..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Region          43..137
                     /region_name="Fes1"
                     /note="Nucleotide exchange factor Fes1; pfam08609"
                     /db_xref="CDD:462534"
     Site            order(119,123,127,161,165,169,204,208,212)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          130..172
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Region          135..172
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          175..215
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Region          178..213
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          218..257
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Region          231..255
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          260..299
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Region          263..299
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMX7.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZL4; propagated from
                     UniProtKB/Swiss-Prot (Q6IMX7.1)"
     CDS             1..357
                     /gene="Hspbp1"
                     /coded_by="NM_139261.1:124..1197"
                     /db_xref="GeneID:246146"
                     /db_xref="RGD:628677"
ORIGIN      
        1 madkgsggsr lplalppasq gcssgssgss aggsgnprlp rnlqgllqma itagseepdp
       61 ppepmseerr qwlqeamsaa frgqreeveq mknclrvlsq atpptageae latdqqereg
      121 alelladlce nmdnaadfcq lsgmhllvgr yleagaaglr wraaqligtc sqnvaaiqeq
      181 vlglgalrkl lrlldrdscd tvrvnalfai sclvreqeag llqflrldgf svlmramqqq
      241 vqklkvksaf llqnllvghp ehkgtlcsmg mvqqlvalvr tehspfhehv lgalcslvtd
      301 fpqgvrecre pelgleellr hrcqllqqhe eyqeelefce kllqtcfssp tddsmdr
//
LOCUS       NP_620232                301 aa            linear   ROD 27-APR-2025
DEFINITION  NADH-cytochrome b5 reductase 3 [Rattus norvegicus].
ACCESSION   NP_620232
VERSION     NP_620232.1
DBSOURCE    REFSEQ: accession NM_138877.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Diaz-Ruiz,A., Lanasa,M., Garcia,J., Mora,H., Fan,F.,
            Martin-Montalvo,A., Di Francesco,A., Calvo-Rubio,M.,
            Salvador-Pascual,A., Aon,M.A., Fishbein,K.W., Pearson,K.J.,
            Villalba,J.M., Navas,P., Bernier,M. and de Cabo,R.
  TITLE     Overexpression of CYB5R3 and NQO1, two NAD+ -producing enzymes,
            mimics aspects of caloric restriction
  JOURNAL   Aging Cell 17 (4), e12767 (2018)
   PUBMED   29706024
  REMARK    GeneRIF: results highlight the importance of CYB5R3 and NQO1, two
            NAD(+) producers, for the promotion of health and extended lifespan
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Samhan-Arias,A.K., Lopez-Sanchez,C., Marques-da-Silva,D., Lagoa,R.,
            Garcia-Lopez,V., Garcia-Martinez,V. and Gutierrez-Merino,C.
  TITLE     High expression of cytochrome b 5 reductase isoform 3/cytochrome b
            5 system in the cerebellum and pyramidal neurons of adult rat brain
  JOURNAL   Brain Struct Funct 221 (4), 2147-2162 (2016)
   PUBMED   25850901
  REMARK    GeneRIF: Results point out the enrichment of cytochrome b 5
            reductase isoform 3/cytochrome b 5 system in neuronal cells and
            structures of the cerebellum and brain stem.
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Lund,R.R., Leth-Larsen,R., Caterino,T.D., Terp,M.G., Nissen,J.,
            Laenkholm,A.V., Jensen,O.N. and Ditzel,H.J.
  TITLE     NADH-Cytochrome b5 Reductase 3 Promotes Colonization and Metastasis
            Formation and Is a Prognostic Marker of Disease-Free and Overall
            Survival in Estrogen Receptor-Negative Breast Cancer
  JOURNAL   Mol Cell Proteomics 14 (11), 2988-2999 (2015)
   PUBMED   26351264
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Blanke,K.L., Sacco,J.C., Millikan,R.C., Olshan,A.F., Luo,J. and
            Trepanier,L.A.
  TITLE     Polymorphisms in the carcinogen detoxification genes CYB5A and
            CYB5R3 and breast cancer risk in African American women
  JOURNAL   Cancer Causes Control 25 (11), 1513-1521 (2014)
   PUBMED   25225034
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Mota Vieira,L., Kaplan,J.C., Kahn,A. and Leroux,A.
  TITLE     Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts
            resulting from multiple alternative first exons
  JOURNAL   Eur J Biochem 220 (3), 729-737 (1994)
   PUBMED   8143727
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Pietrini,G., Aggujaro,D., Carrera,P., Malyszko,J., Vitale,A. and
            Borgese,N.
  TITLE     A single mRNA, transcribed from an alternative, erythroid-specific,
            promoter, codes for two non-myristylated forms of NADH-cytochrome
            b5 reductase
  JOURNAL   J Cell Biol 117 (5), 975-986 (1992)
   PUBMED   1577871
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Zenno,S., Hattori,M., Misumi,Y., Yubisui,T. and Sakaki,Y.
  TITLE     Molecular cloning of a cDNA encoding rat NADH-cytochrome b5
            reductase and the corresponding gene
  JOURNAL   J Biochem 107 (6), 810-816 (1990)
   PUBMED   2391344
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Murakami,K., Yubisui,T., Takeshita,M. and Miyata,T.
  TITLE     The NH2-terminal structures of human and rat liver microsomal
            NADH-cytochrome b5 reductases
  JOURNAL   J Biochem 105 (2), 312-317 (1989)
   PUBMED   2498303
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Pietrini,G., Carrera,P. and Borgese,N.
  TITLE     Two transcripts encode rat cytochrome b5 reductase
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7246-7250 (1988)
   PUBMED   3174630
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D00636.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062066.1, J03867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..301
                     /product="NADH-cytochrome b5 reductase 3"
                     /EC_number="1.6.2.2"
                     /note="B5R; diaphorase-1; Diaphorase (NADH) (cytochrome
                     b-5 reductase)"
                     /calculated_mol_wt=34044
     Region          <38..301
                     /region_name="PLN02252"
                     /note="nitrate reductase [NADPH]"
                     /db_xref="CDD:215141"
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (P20070.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (P20070.2)"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCN2; propagated from
                     UniProtKB/Swiss-Prot (P20070.2)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCN2; propagated from
                     UniProtKB/Swiss-Prot (P20070.2)"
     CDS             1..301
                     /gene="Cyb5r3"
                     /gene_synonym="Dia1; Nadhcb5; RNNADHCB5"
                     /coded_by="NM_138877.1:39..944"
                     /db_xref="GeneID:25035"
                     /db_xref="RGD:2502"
ORIGIN      
        1 mgaqlstlsr vvlspvwfvy slfmklfqrs spaitlenpd ikyplrlidk eiishdtrrf
       61 rfalpspqhi lglpigqhiy lstridgnlv irpytpvssd ddkgfvdlvv kvyfkdthpk
      121 fpaggkmsqy lenmnigdti efrgpngllv yqgkgkfair adkksnpvvr tvksvgmiag
      181 gtgitpmlqv iravlkdpnd htvcyllfan qsekdillrp eleelrnehs srfklwytvd
      241 kapdawdysq gfvneemird hlpppgeetl ilmcgpppmi qfaclpnler vghpkercft
      301 f
//
LOCUS       NP_001007629             316 aa            linear   ROD 27-APR-2025
DEFINITION  CXXC-type zinc finger protein 5 [Rattus norvegicus].
ACCESSION   NP_001007629 XP_214577
VERSION     NP_001007629.1
DBSOURCE    REFSEQ: accession NM_001007628.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Aras,S., Pak,O., Sommer,N., Finley,R. Jr., Huttemann,M.,
            Weissmann,N. and Grossman,L.I.
  TITLE     Oxygen-dependent expression of cytochrome c oxidase subunit 4-2
            gene expression is mediated by transcription factors RBPJ, CXXC5
            and CHCHD2
  JOURNAL   Nucleic Acids Res 41 (4), 2255-2266 (2013)
   PUBMED   23303788
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Andersson,T., Sodersten,E., Duckworth,J.K., Cascante,A., Fritz,N.,
            Sacchetti,P., Cervenka,I., Bryja,V. and Hermanson,O.
  TITLE     CXXC5 is a novel BMP4-regulated modulator of Wnt signaling in
            neural stem cells
  JOURNAL   J Biol Chem 284 (6), 3672-3681 (2009)
   PUBMED   19001364
  REMARK    GeneRIF: CXXC5 expression overlapped with BMP4 adjacent to Wnt3a
            expression in the dorsal regions of the telencephalon, including
            the developing choroid plexus.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083622.1, DV723039.1 and BE114271.1.
            
            On Nov 29, 2004 this sequence version replaced XP_214577.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK365729.1, BP482957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..316
                     /product="CXXC-type zinc finger protein 5"
                     /note="CXXC finger 5"
                     /calculated_mol_wt=32495
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIQ3.1)"
     Region          249..290
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          251..256
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIQ3.1)"
     CDS             1..316
                     /gene="Cxxc5"
                     /coded_by="NM_001007628.2:137..1087"
                     /db_xref="GeneID:291670"
                     /db_xref="RGD:1359466"
ORIGIN      
        1 msslgggsqd aggsssssnt ssssgsgqka ggtdksatva atapasvadd appperrnks
       61 giiseplnks lrrsrplshy ssfgssggag smmggesadk aaaaaaslla nghdlaaama
      121 vdksnptskh ksgavaslls kaeratelaa egqltlqqfa qstemlkrvv qehlplmsea
      181 gaglpdmeav agaealngqs dfpylgafpi npglfimtpa gvflaesalh maglaeypmq
      241 gelasaissg kkkrkrcgmc apcrrrince qcsscrnrkt ghqickfrkc eelkkkpsaa
      301 lekvmlpsga afrwfq
//
LOCUS       NP_599233                961 aa            linear   ROD 27-APR-2025
DEFINITION  phosphofurin acidic cluster sorting protein 1 [Rattus norvegicus].
ACCESSION   NP_599233
VERSION     NP_599233.1
DBSOURCE    REFSEQ: accession NM_134406.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Kottgen,M., Benzing,T., Simmen,T., Tauber,R., Buchholz,B.,
            Feliciangeli,S., Huber,T.B., Schermer,B., Kramer-Zucker,A.,
            Hopker,K., Simmen,K.C., Tschucke,C.C., Sandford,R., Kim,E.,
            Thomas,G. and Walz,G.
  TITLE     Trafficking of TRPP2 by PACS proteins represents a novel mechanism
            of ion channel regulation
  JOURNAL   EMBO J 24 (4), 705-716 (2005)
   PUBMED   15692563
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Huang,Z., Philippin,B., O'Leary,E., Bonventre,J.V., Kriz,W. and
            Witzgall,R.
  TITLE     Expression of the transcriptional repressor protein Kid-1 leads to
            the disintegration of the nucleolus
  JOURNAL   J Biol Chem 274 (12), 7640-7648 (1999)
   PUBMED   10075651
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Wan,L., Molloy,S.S., Thomas,L., Liu,G., Xiang,Y., Rybak,S.L. and
            Thomas,G.
  TITLE     PACS-1 defines a novel gene family of cytosolic sorting proteins
            required for trans-Golgi network localization
  JOURNAL   Cell 94 (2), 205-216 (1998)
   PUBMED   9695949
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF076183.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF076183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..961
                     /product="phosphofurin acidic cluster sorting protein 1"
                     /note="cytosolic sorting protein PACS-1"
                     /calculated_mol_wt=104570
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8K212; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Region          260..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     Region          375..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Region          475..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VY07; propagated from
                     UniProtKB/Swiss-Prot (O88588.1)"
     Region          546..958
                     /region_name="Pacs-1"
                     /note="PACS-1 cytosolic sorting protein; pfam10254"
                     /db_xref="CDD:463027"
     Region          758..802
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88588.1)"
     CDS             1..961
                     /gene="Pacs1"
                     /gene_synonym="Pacs-1"
                     /coded_by="NM_134406.1:101..2986"
                     /db_xref="GeneID:171444"
                     /db_xref="RGD:620579"
ORIGIN      
        1 maerggaggg pggagggssq rgsgvaqspq qqppqqpsqp qqptppklaq atssssstsa
       61 aaasssssst stsmavavas gsappggpgp grtpapvqmn lyatwevdrs ssscvprlfs
      121 ltlkklvmlk emdkdlnsvv iavklqgskr ilrsneiilp asglvetelq ltfslqyphf
      181 lkrdanklqi mlqrrkrykn rtilgyktla vglinmaevm qhpnegalvl glhsnvkdvs
      241 vpvaeikiys lssqpidheg iksklsdrsp didnyseeee esfsseqegs ddplhgqdlf
      301 yededlrkvk ktrrkltsts aitrqpnikq kfvallkrfk vsdevgfgle hvsreqirev
      361 eedldelyds lemynpsdsg pemeetesil stpkpklkpf fegmsqsssq teigslnskg
      421 slgkdttspm elaalekvks twiknqddsl tetdtleitd qdmfgdasts lvvpekvktp
      481 mksskadlqg saspskvegt htprqkrstp lkerqlskpl sertnssdse rspdlghstq
      541 iprkvvydql nqilvsdaal penvilvntt dwqgqyvael lqdqrkpvvc tcstvevqav
      601 lsalltriqr ycncnssmpr pvkvaavgsq sylssilrff vkslasktpd wlghmrfliv
      661 plgshpvaky lgsvdsryss tfldsawrdl fsrseppvse pldvvgrvmq yvngattthq
      721 lpvaeamltc rhkfpdedsy qkfipfigvv kvglvedsps tagdgddspv vsltvpstsp
      781 psssglsrda tatppsspsm ssalaivgsp nspygdvigl qvdywlghpg errregdkrd
      841 asskntlksv frsvqvsrlp hageaqlsgt mamtvvtkek nkkvptifls kkprekevds
      901 ksqviegisr licsakqqqt mlrvsidgve wsdikffqla aqwpthvkhf pvglfsgskp
      961 t
//
LOCUS       NP_001116824             297 aa            linear   ROD 27-APR-2025
DEFINITION  palmitoyl-protein thioesterase ABHD10, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_001116824 XP_001064579
VERSION     NP_001116824.1
DBSOURCE    REFSEQ: accession NM_001123352.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Iwamura,A., Fukami,T., Higuchi,R., Nakajima,M. and Yokoi,T.
  TITLE     Human alpha/beta hydrolase domain containing 10 (ABHD10) is
            responsible enzyme for deglucuronidation of mycophenolic acid
            acyl-glucuronide in liver
  JOURNAL   J Biol Chem 287 (12), 9240-9249 (2012)
   PUBMED   22294686
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161919.1.
            
            On Apr 13, 2008 this sequence version replaced XP_001064579.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161919.1, CO568709.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..297
                     /product="palmitoyl-protein thioesterase ABHD10,
                     mitochondrial precursor"
                     /EC_number="3.1.2.22"
                     /EC_number="3.1.1.93"
                     /note="abhydrolase domain-containing protein 10,
                     mitochondrial; alpha/beta hydrolase domain-containing
                     protein 10, mitochondrial; mycophenolic acid
                     acyl-glucuronide esterase, mitochondrial; acyl-protein
                     thioesterase ABHD10; palmitoyl-protein thioesterase
                     ABHD10, mitochondrial"
                     /calculated_mol_wt=28177
     transit_peptide 1..43
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5I0K5.2)"
                     /calculated_mol_wt=4994
     mat_peptide     44..297
                     /product="Palmitoyl-protein thioesterase ABHD10,
                     mitochondrial. /id=PRO_0000280736"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0K5.2)"
                     /calculated_mol_wt=28177
     Region          62..293
                     /region_name="YvaK"
                     /note="Esterase/lipase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1647"
                     /db_xref="CDD:441253"
     CDS             1..297
                     /gene="Abhd10"
                     /gene_synonym="RGD1308084"
                     /coded_by="NM_001123352.1:6..899"
                     /db_xref="GeneID:303953"
                     /db_xref="RGD:1308084"
ORIGIN      
        1 maawvpcrkw gwaavsfgrh rgliaslark ppwawwlsac rqkttlsflk rpelpslayk
       61 rlkgknpgii fipgylsnmn gkkavaieef cksighafir fdysgvgssd gnlaecsvgk
      121 wrkdvlsild diaegpqilv gsslggwlml haaiarpekv ialigiasat dgvvtqfhsl
      181 pvemqkeiem kgewslpsky nkegyysipy sfikeaahhc llhspipvtc pvrllhgmkd
      241 eivpwhrslq vadrvvspdv dvilrkhsdh rmketadihl lictiddlid klstvth
//
LOCUS       NP_001029042             415 aa            linear   ROD 27-APR-2025
DEFINITION  casein kinase I isoform gamma-2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001029042
VERSION     NP_001029042.1
DBSOURCE    REFSEQ: accession NM_001033870.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Chia,R., Haddock,S., Beilina,A., Rudenko,I.N., Mamais,A.,
            Kaganovich,A., Li,Y., Kumaran,R., Nalls,M.A. and Cookson,M.R.
  TITLE     Phosphorylation of LRRK2 by casein kinase 1alpha regulates
            trans-Golgi clustering via differential interaction with ARHGEF7
  JOURNAL   Nat Commun 5, 5827 (2014)
   PUBMED   25500533
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Zhai,L., Graves,P.R., Robinson,L.C., Italiano,M., Culbertson,M.R.,
            Rowles,J., Cobb,M.H., DePaoli-Roach,A.A. and Roach,P.J.
  TITLE     Casein kinase I gamma subfamily. Molecular cloning, expression, and
            characterization of three mammalian isoforms and complementation of
            defects in the Saccharomyces cerevisiae YCK genes
  JOURNAL   J Biol Chem 270 (21), 12717-12724 (1995)
   PUBMED   7759525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072533.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..415
                     /product="casein kinase I isoform gamma-2 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="CKI-gamma 2; casein kinase I"
                     /calculated_mol_wt=47505
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62762.2)"
     Region          45..332
                     /region_name="STKc_CK1_gamma"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, Casein Kinase 1 gamma; cd14126"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,119..123,125,127,165,167,169..170,
                     172,188,191,214..217)
                     /site_type="active"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,119..123,167,169..170,172,188)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271028"
     Site            order(56,125,127,165,167,169,191,214..217)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271028"
     Site            187..217
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271028"
     Region          332..385
                     /region_name="CK1gamma_C"
                     /note="Casein kinase 1 gamma C terminal; pfam12605"
                     /db_xref="CDD:463640"
     Region          369..415
                     /region_name="Phospho-regulated basic and hydrophobic
                     (PRBH) motif. /evidence=ECO:0000250|UniProtKB:P78368"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62762.2)"
     CDS             1..415
                     /gene="Csnk1g2"
                     /coded_by="NM_001033870.1:459..1706"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65278"
                     /db_xref="RGD:621407"
ORIGIN      
        1 mdfdkkggkg eleegrrmsk tgtnrsnhgv rnsgtssgvl mvgpnfrvgk kigcgnfgel
       61 rlgknlytne yvaiklepik srapqlhley rfykqlstte gvpqvyyfgp cgkynamvle
      121 llgpsledlf dlcdrtftlk tvlmiaiqli trmeyvhtks liyrdvkpen flvgrpgskr
      181 qhsihiidfg lakeyidpet kkhipyrehk sltgtaryms inthlgkeqs rrddlealgh
      241 mfmyflrgsl pwqglkadtl keryqkigdt kratpievlc esfpeematy lryvrrldff
      301 ekpdydylrk lftdlfdrsg yvfdyeydwa gkplptpigt vhpdvpsqpp hrdkaqlhtk
      361 nqalnstnge lntddptagh snapiaapae vevadetkcc cffkrrkrks lqrhk
//
LOCUS       NP_001012224             373 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor NF-E2 45 kDa subunit [Rattus norvegicus].
ACCESSION   NP_001012224 XP_345884
VERSION     NP_001012224.1
DBSOURCE    REFSEQ: accession NM_001012224.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Zhang,Y., Wan,J., Liu,S., Hua,T. and Sun,Q.
  TITLE     Exercise induced improvements in insulin sensitivity are concurrent
            with reduced NFE2/miR-432-5p and increased FAM3A
  JOURNAL   Life Sci 207, 23-29 (2018)
   PUBMED   29802941
  REMARK    GeneRIF: NFE2/miR432-5p is reduced and FAM3a is increased with
            exercise in a rat model of insulin sensitivity
            Erratum:[Life Sci. 2020 Nov 1;260:118515. doi:
            10.1016/j.lfs.2020.118515. PMID: 33039124]
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Yang,W., Wang,J., Chen,Z., Chen,J., Meng,Y., Chen,L., Chang,Y.,
            Geng,B., Sun,L., Dou,L., Li,J., Guan,Y., Cui,Q. and Yang,J.
  TITLE     NFE2 Induces miR-423-5p to Promote Gluconeogenesis and
            Hyperglycemia by Repressing the Hepatic FAM3A-ATP-Akt Pathway
  JOURNAL   Diabetes 66 (7), 1819-1832 (2017)
   PUBMED   28411267
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Khalifeh,S., Oryan,S., Digaleh,H., Shaerzadeh,F., Khodagholi,F.,
            Maghsoudi,N. and Zarrindast,M.R.
  TITLE     Involvement of Nrf2 in development of anxiety-like behavior by
            linking Bcl2 to oxidative phosphorylation: estimation in rat
            hippocampus, amygdala, and prefrontal cortex
  JOURNAL   J Mol Neurosci 55 (2), 492-499 (2015)
   PUBMED   25007950
  REMARK    GeneRIF: Nrf2 silencing induced anxiety-related behavior in rats.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Kashif,M., Hellwig,A., Kolleker,A., Shahzad,K., Wang,H., Lang,S.,
            Wolter,J., Thati,M., Vinnikov,I., Bierhaus,A., Nawroth,P.P. and
            Isermann,B.
  TITLE     p45NF-E2 represses Gcm1 in trophoblast cells to regulate syncytium
            formation, placental vascularization and embryonic growth
  JOURNAL   Development 138 (11), 2235-2247 (2011)
   PUBMED   21558372
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Zhao,Q., Zhou,W., Rank,G., Sutton,R., Wang,X., Cumming,H.,
            Cerruti,L., Cunningham,J.M. and Jane,S.M.
  TITLE     Repression of human gamma-globin gene expression by a short isoform
            of the NF-E4 protein is associated with loss of NF-E2 and RNA
            polymerase II recruitment to the promoter
  JOURNAL   Blood 107 (5), 2138-2145 (2006)
   PUBMED   16263792
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Wang,D., Li,Y. and Shen,B.
  TITLE     A novel erythroid differentiation related gene EDRF1 upregulating
            globin gene expression in HEL cells
  JOURNAL   Chin Med J (Engl) 115 (11), 1701-1705 (2002)
   PUBMED   12609092
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Gavva,N.R., Wen,S.C., Daftari,P., Moniwa,M., Yang,W.M.,
            Yang-Feng,L.P., Seto,E., Davie,J.R. and Shen,C.K.
  TITLE     NAPP2, a peroxisomal membrane protein, is also a transcriptional
            corepressor
  JOURNAL   Genomics 79 (3), 423-431 (2002)
   PUBMED   11863372
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Li,Y.J., Higgins,R.R., Pak,B.J., Shivdasani,R.A., Ney,P.A.,
            Archer,M. and Ben-David,Y.
  TITLE     p45(NFE2) is a negative regulator of erythroid proliferation which
            contributes to the progression of Friend virus-induced
            erythroleukemias
  JOURNAL   Mol Cell Biol 21 (1), 73-80 (2001)
   PUBMED   11113182
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Ney,P.A., Farina,S.F., Bodine,D.M., Andrews,N.C., Orkin,S.H. and
            Neinhuis,A.W.
  TITLE     Microcytic anemia in mk/mk mice is not corrected by
            retroviral-mediated gene transfer of wild-type p45 NF-E2
  JOURNAL   Exp Hematol 23 (1), 74-80 (1995)
   PUBMED   7995373
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078925.1.
            
            On Feb 11, 2005 this sequence version replaced XP_345884.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078925.1, FQ234994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..373
                     /product="transcription factor NF-E2 45 kDa subunit"
                     /note="p45 NF-E2; leucine zipper protein NF-E2; nuclear
                     factor, erythroid-derived 2 45 kDa subunit; nuclear
                     factor, erythroid derived 2"
                     /calculated_mol_wt=41365
     Region          1..206
                     /region_name="Transactivation domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          1..83
                     /region_name="Required for interaction with MAPK8.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          40..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          61..65
                     /region_name="PXY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          79..83
                     /region_name="PXY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          131..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:Q07279; propagated from
                     UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q07279; propagated from
                     UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          206..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Region          263..330
                     /region_name="bZIP_NFE2-like"
                     /note="Basic leucine zipper (bZIP) domain of Nuclear
                     Factor, Erythroid-derived 2 (NFE2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14720"
                     /db_xref="CDD:269868"
     Region          264..326
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269868"
     Region          268..287
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     Site            order(272..273,275..277,279..284,286..288)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269868"
     Site            order(287,290..291,294..295,297..298,301..302,304..305,
                     308..309,311..312,315..316,318..319)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269868"
     Region          291..298
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYT2.1)"
     CDS             1..373
                     /gene="Nfe2"
                     /coded_by="NM_001012224.1:309..1430"
                     /db_xref="GeneID:366998"
                     /db_xref="RGD:1306888"
ORIGIN      
        1 mppcppqpnr nrlpqlptge lgemeltwqe imsitelqgl nvpsepsfep qaptpypgpl
       61 ppptycpcsi hpdagftlpp ppyelpastp hapdlpysyg niaipvskpl tlsgllnepl
      121 pdplalldig lpvgqpkpqe dpesdsglsl nysdaeslel egteagrrrs eyvdmypvey
      181 pyslmpnsla hpnytlppte tplvlesssg pvrakpavrg eagsrderra lamkipfptd
      241 kivnlpvddf nellaqyplt esqlalvrdi rrrgknkvaa qncrkrklet ivqlereler
      301 lgsererllr argeadrtle vmrqqltely hdifqhlrde sgnsyspeey vlqqaadgai
      361 flvprgtkme atd
//
LOCUS       NP_001020841             457 aa            linear   ROD 27-APR-2025
DEFINITION  glycerol-3-phosphate acyltransferase 3 [Rattus norvegicus].
ACCESSION   NP_001020841 XP_223200
VERSION     NP_001020841.1
DBSOURCE    REFSEQ: accession NM_001025670.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Sukumaran,S., Barnes,R.I., Garg,A. and Agarwal,A.K.
  TITLE     Functional characterization of the human
            1-acylglycerol-3-phosphate-O-acyltransferase isoform
            10/glycerol-3-phosphate acyltransferase isoform 3
  JOURNAL   J Mol Endocrinol 42 (6), 469-478 (2009)
   PUBMED   19318427
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Cao,J., Li,J.L., Li,D., Tobin,J.F. and Gimeno,R.E.
  TITLE     Molecular identification of microsomal
            acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de
            novo triacylglycerol synthesis
  JOURNAL   Proc Natl Acad Sci U S A 103 (52), 19695-19700 (2006)
   PUBMED   17170135
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Tang,W., Yuan,J., Chen,X., Gu,X., Luo,K., Li,J., Wan,B., Wang,Y.
            and Yu,L.
  TITLE     Identification of a novel human lysophosphatidic acid
            acyltransferase, LPAAT-theta, which activates mTOR pathway
  JOURNAL   J Biochem Mol Biol 39 (5), 626-635 (2006)
   PUBMED   17002884
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097362.1.
            
            On Jul 22, 2005 this sequence version replaced XP_223200.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097362.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..457
                     /product="glycerol-3-phosphate acyltransferase 3"
                     /EC_number="2.3.1.51"
                     /EC_number="2.3.1.15"
                     /note="1-AGPAT 9; LPAAT-theta; 1-AGP acyltransferase 9;
                     lysophosphatidic acid acyltransferase theta; GPAT-3;
                     1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9;
                     1-acylglycerol-3-phosphate O-acyltransferase 9;
                     1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10"
                     /calculated_mol_wt=50881
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53EU6; propagated from
                     UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Region          199..408
                     /region_name="LPLAT_LPCAT1-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: LPCAT1-like; cd07991"
                     /db_xref="CDD:153253"
     Site            order(229,232,234,248..251,304..306)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153253"
     Region          229..234
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q9D517"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8J4.1)"
     Region          429..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8J4.1)"
     CDS             1..457
                     /gene="Gpat3"
                     /gene_synonym="AGPAT 10; Agpat9"
                     /coded_by="NM_001025670.1:302..1675"
                     /db_xref="GeneID:305166"
                     /db_xref="RGD:1565703"
ORIGIN      
        1 megtdlvvkl lstwltlvgs lillpsafgl slgiseiymk ilvktlewat lriekgapke
       61 svlkspasmg iiqrdespme kglsglrgrd felsdvfyfs kkgleaived evtqrfssee
      121 lvswnlltrt nvnfhyispk ltivwvlgvl vrycfllplr vtlafigisl liigttlvgq
      181 lpdsslknwl selvhltccr icvrslsgti hyhnkqyrpq kggicvanht spidvlilat
      241 dgcyamvgqv hgglmgiiqr amvkacphvw ferseikdrh lvtkrlkehi adkkklpili
      301 fpegtcinnt svmmfkkgsf eiggtiypva ikynpqfgda fwnsskynlv syllrimtsw
      361 aivcdvwymp pmtreegeda vqfanrvksa iavqggltel pwdgglkrak vkdtfkeeqq
      421 ktyskmivgn gspslaldss tvdnhgspep afrsesl
//
LOCUS       NP_001011970             565 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane 7 superfamily member 3 precursor [Rattus norvegicus].
ACCESSION   NP_001011970 XP_216312
VERSION     NP_001011970.1
DBSOURCE    REFSEQ: accession NM_001011970.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Isaac,R., Goldstein,I., Furth,N., Zilber,N., Streim,S.,
            Boura-Halfon,S., Elhanany,E., Rotter,V., Oren,M. and Zick,Y.
  TITLE     TM7SF3, a novel p53-regulated homeostatic factor, attenuates
            cellular stress and the subsequent induction of the unfolded
            protein response
  JOURNAL   Cell Death Differ 24 (1), 132-143 (2017)
   PUBMED   27740623
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Beck,A., Isaac,R., Lavelin,I., Hart,Y., Volberg,T.,
            Shatz-Azoulay,H., Geiger,B. and Zick,Y.
  TITLE     An siRNA screen identifies transmembrane 7 superfamily member 3
            (TM7SF3), a seven transmembrane orphan receptor, as an inhibitor of
            cytokine-induced death of pancreatic beta cells
  JOURNAL   Diabetologia 54 (11), 2845-2855 (2011)
   PUBMED   21853325
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Akashi,H., Han,H.J., Iizaka,M., Nakajima,Y., Furukawa,Y.,
            Sugano,S., Imai,K. and Nakamura,Y.
  TITLE     Isolation and characterization of a novel gene encoding a putative
            seven-span transmembrane protein, TM7SF3
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 305-309 (2000)
   PUBMED   10828615
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090030.1.
            
            On Feb 11, 2005 this sequence version replaced XP_216312.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090030.1, SRR8487226.198147.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..565
                     /product="transmembrane 7 superfamily member 3 precursor"
                     /calculated_mol_wt=61363
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF4.1)"
                     /calculated_mol_wt=2240
     mat_peptide     22..565
                     /product="Transmembrane 7 superfamily member 3.
                     /id=PRO_0000045329"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
                     /calculated_mol_wt=61363
     Site            22
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Region          291..498
                     /region_name="DUF4203"
                     /note="Domain of unknown function (DUF4203); pfam13886"
                     /db_xref="CDD:464018"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            341..361
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            402..422
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            427..447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF4.1)"
     CDS             1..565
                     /gene="Tm7sf3"
                     /coded_by="NM_001011970.1:97..1794"
                     /db_xref="GeneID:297725"
                     /db_xref="RGD:1306752"
ORIGIN      
        1 mwrlrllvla vlaagsaeaq anssdgflef svgkftyfvl srrfpqeavl rhissnvtfl
       61 lfqihsqyqn ttvsytktll pstsgtgndr glvfilrpeq tvctwylete dtkpvqsvav
      121 tlsyserdpi pggcnlefdl didpniyldy nffettikfa panigyaraa epppcdvstg
      181 qesrwrlryh vyqyflpegd lteasllqhl qrmaqvvqvm asavkvvtlt addktvvsfs
      241 slpgqgviyn vivwdpslnt saayvpvhty acsfdsvdgn cvppgrvstk vfstlfallg
      301 lftcffghrf wktelffvgf iflgfffyil itrltalkye vrlvltavag sigglllvas
      361 wwrfgiltlc mlcvglvlgf lvssgtfftp lgnlnvfhdd gvfwvtfsci allvpviflg
      421 clrilnilac givgsysvvl ainsymftsl syitlnvlrr alnadfrgaf irvpfqtndy
      481 iilavwgmla vtgitlqirr ergrppfpph pyklwkqere rrvtnildps hhipplrerl
      541 ygwvarikel fqkeqpager tplll
//
LOCUS       NP_001020054             349 aa            linear   ROD 27-APR-2025
DEFINITION  protein O-mannose kinase [Rattus norvegicus].
ACCESSION   NP_001020054 XP_224953
VERSION     NP_001020054.1
DBSOURCE    REFSEQ: accession NM_001024883.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yoshida-Moriguchi,T., Willer,T., Anderson,M.E., Venzke,D.,
            Whyte,T., Muntoni,F., Lee,H., Nelson,S.F., Yu,L. and Campbell,K.P.
  TITLE     SGK196 is a glycosylation-specific O-mannose kinase required for
            dystroglycan function
  JOURNAL   Science 341 (6148), 896-899 (2013)
   PUBMED   23929950
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Vogel,P., Read,R.W., Hansen,G.M., Payne,B.J., Small,D., Sands,A.T.
            and Zambrowicz,B.P.
  TITLE     Congenital hydrocephalus in genetically engineered mice
  JOURNAL   Vet Pathol 49 (1), 166-181 (2012)
   PUBMED   21746835
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097466.1.
            
            On Jun 17, 2005 this sequence version replaced XP_224953.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097466.1, FQ125227.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.4"
     Protein         1..349
                     /product="protein O-mannose kinase"
                     /EC_number="2.7.1.183"
                     /note="sugen kinase 196; probable inactive protein
                     kinase-like protein SgK196"
                     /calculated_mol_wt=39923
     Site            20..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A9.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A9.1)"
     Region          104..>194
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A9.1)"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A9.1)"
     CDS             1..349
                     /gene="Pomk"
                     /gene_synonym="RGD1310810; Sgk196"
                     /coded_by="NM_001024883.1:289..1338"
                     /db_xref="GeneID:306549"
                     /db_xref="RGD:1310810"
ORIGIN      
        1 mgqqhgarng lthrelprgm glllamalmn vvlyvcldhl fispgrated prrcppgyfr
       61 mgrmrncsrw lsceelrtev rqlklvgega vkrvflsewn ehkvalsrlt rlemkedflh
      121 glrmltslqs qhvvtlagfc eedgtiltey hplgslsnle etlnlskyrd vntwqhrlrl
      181 aveyvsiiny lhhsplgtrv mcdsndlpkt lsqylltsnf sivandldal plvdhgsrvl
      241 vkcghrelhg dfvapeqlwp ygedtpfqdd lmppydekid iwkipdvssf llghvegsdm
      301 vrfhlfdihk acknqfpaer ptaqnvlday qkvfhslrdt vmsqtkeml
//
LOCUS       NP_001006996             397 aa            linear   ROD 27-APR-2025
DEFINITION  acetyl-CoA acetyltransferase, cytosolic [Rattus norvegicus].
ACCESSION   NP_001006996 XP_217796
VERSION     NP_001006996.1
DBSOURCE    REFSEQ: accession NM_001006995.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Ichigo,Y., Takeshita,A., Hibino,M., Nakagawa,T., Hayakawa,T.,
            Patel,D., Field,C.J. and Shimada,M.
  TITLE     High-Fructose Diet-Induced Hypertriglyceridemia Is Associated With
            Enhanced Hepatic Expression of ACAT2 in Rats
  JOURNAL   Physiol Res 68 (6), 1021-1026 (2019)
   PUBMED   31647302
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhai,S., Zhao,M., Zhou,C., Lu,F., Zhang,H., Na,L., Feng,S.,
            Qiang,X. and Du,Y.
  TITLE     The association and significance of H3K27me3 and a folate metabolic
            gene ACat2 in neural tube defects
  JOURNAL   Nutr J 15 (1), 95 (2016)
   PUBMED   27809850
  REMARK    GeneRIF: The increased H3K27me3 expression might cause a disorder
            of folate metabolic pathway by silencing ACat2 expression, leading
            to reduced proliferation and differentiation of neural stem cells,
            and ultimately the occurrence of neural tube defects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Cote,I., Chapados,N.A. and Lavoie,J.M.
  TITLE     Impaired VLDL assembly: a novel mechanism contributing to hepatic
            lipid accumulation following ovariectomy and
            high-fat/high-cholesterol diets?
  JOURNAL   Br J Nutr 112 (10), 1592-1600 (2014)
   PUBMED   25263431
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Morris,A.A.
  TITLE     Cerebral ketone body metabolism
  JOURNAL   J Inherit Metab Dis 28 (2), 109-121 (2005)
   PUBMED   15877199
  REMARK    Review article
REFERENCE   5  (residues 1 to 397)
  AUTHORS   McCarthy,J.J., Meyer,J., Moliterno,D.J., Newby,L.K., Rogers,W.J.
            and Topol,E.J.
  CONSRTM   GenQuest multicenter study
  TITLE     Evidence for substantial effect modification by gender in a
            large-scale genetic association study of the metabolic syndrome
            among coronary heart disease patients
  JOURNAL   Hum Genet 114 (1), 87-98 (2003)
   PUBMED   14557872
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Antonenkov,V.D., Croes,K., Waelkens,E., Van Veldhoven,P.P. and
            Mannaerts,G.P.
  TITLE     Identification, purification and characterization of an
            acetoacetyl-CoA thiolase from rat liver peroxisomes
  JOURNAL   Eur J Biochem 267 (10), 2981-2990 (2000)
   PUBMED   10806397
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Song,X.Q., Fukao,T., Yamaguchi,S., Miyazawa,S., Hashimoto,T. and
            Orii,T.
  TITLE     Molecular cloning and nucleotide sequence of complementary DNA for
            human hepatic cytosolic acetoacetyl-coenzyme A thiolase
  JOURNAL   Biochem Biophys Res Commun 201 (1), 478-485 (1994)
   PUBMED   7911016
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Middleton,B.
  TITLE     The acetoacetyl-coenzyme A thiolases of rat brain and their
            relative activities during postnatal development
  JOURNAL   Biochem J 132 (4), 731-737 (1973)
   PUBMED   4721608
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Lockwood,E.A. and Bailey,E.
  TITLE     The course of ketosis and the activity of key enzymes of
            ketogenesis and ketone-body utilization during development of the
            postnatal rat
  JOURNAL   Biochem J 124 (1), 249-254 (1971)
   PUBMED   5166591
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Page,M.A., Krebs,H.A. and Williamson,D.H.
  TITLE     Activities of enzymes of ketone-body utilization in brain and other
            tissues of suckling rats
  JOURNAL   Biochem J 121 (1), 49-53 (1971)
   PUBMED   5116556
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083872.1.
            
            On Nov 22, 2004 this sequence version replaced XP_217796.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083872.1, FQ210374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..397
                     /product="acetyl-CoA acetyltransferase, cytosolic"
                     /EC_number="2.3.1.9"
                     /note="cytosolic acetoacetyl-CoA thiolase; acetyl-Coenzyme
                     A acetyltransferase 2; acetyl-Coenzyme A acetyltransferase
                     3"
                     /calculated_mol_wt=40977
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWD1; propagated from
                     UniProtKB/Swiss-Prot (Q5XI22.1)"
     Region          8..396
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWD1; propagated from
                     UniProtKB/Swiss-Prot (Q5XI22.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWD1; propagated from
                     UniProtKB/Swiss-Prot (Q5XI22.1)"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWD1; propagated from
                     UniProtKB/Swiss-Prot (Q5XI22.1)"
     Site            353
                     /site_type="other"
                     /note="Increases nucleophilicity of active site Cys.
                     /evidence=ECO:0000250|UniProtKB:P42765; propagated from
                     UniProtKB/Swiss-Prot (Q5XI22.1)"
     CDS             1..397
                     /gene="Acat2"
                     /gene_synonym="Ab2-076; Acat3"
                     /coded_by="NM_001006995.1:27..1220"
                     /db_xref="GeneID:308100"
                     /db_xref="RGD:1359366"
ORIGIN      
        1 mnagsdpvvi isaartaigs fngalstvpv hnlgttvike vlqrakvape evsevifghv
       61 ltagcgqnpt rqasvgagip ysvpawscqm icgsglkavc laaqsiamgd stivvaggme
      121 nmskaphlah lrsgvkmgev pladsilcdg ltdafhnyhm gitaenvakk wqvsreaqdk
      181 vavvsqnrae haqkaghfdk eivpvhvssr kgltevkide fprhgsnlea msklkpyflt
      241 dgtgtvtpan asgmndgaaa vvlmkkteae srmlkplaqv vswsqagvep svmgvgpipa
      301 ikqavakagw sledvdvfei neafaavsaa iakelglspe kvnidggaia lghplgasgc
      361 rilvtllhtl ervggtrgva alcigggmgi amcvqrg
//
LOCUS       NP_001014122             254 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase NEURL3 [Rattus norvegicus].
ACCESSION   NP_001014122 XP_237084
VERSION     NP_001014122.1
DBSOURCE    REFSEQ: accession NM_001014100.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Hu,Y., Nguyen,T.T., Bui,K.C., Demello,D.E. and Smith,J.B.
  TITLE     A novel inflammation-induced ubiquitin E3 ligase in alveolar type
            II cells
  JOURNAL   Biochem Biophys Res Commun 333 (1), 253-263 (2005)
   PUBMED   15936721
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088198.1.
            
            On Apr 20, 2005 this sequence version replaced XP_237084.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088198.1, CO566844.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN06680432,
                                           SAMN16093042 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..254
                     /product="E3 ubiquitin-protein ligase NEURL3"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase LINCR; lung-inducible
                     neuralized-related C3CH4 RING domain protein;
                     neuralized-like protein 3; lung-inducible
                     neuralized-related C3HC4 RING domain protein; neuralized
                     homolog 3; RING-type E3 ubiquitin transferase NEURL3"
                     /calculated_mol_wt=27883
     Region          20..173
                     /region_name="Neuralized"
                     /note="pfam07177"
                     /db_xref="CDD:462112"
     Region          194..243
                     /region_name="RING-HC_NEURL3"
                     /note="RING finger, HC subclass, found in neuralized-like
                     protein 3 (NEURL3) and similar proteins; cd16552"
                     /db_xref="CDD:438214"
     CDS             1..254
                     /gene="Neurl3"
                     /gene_synonym="Lincr"
                     /coded_by="NM_001014100.1:219..983"
                     /db_xref="GeneID:316326"
                     /db_xref="RGD:1359633"
ORIGIN      
        1 mgsrlspean aevprealsf hgdatgaqvh lddqrstarr rstfhdgivf sqrpvwpger
       61 valrvlrhed gwcgglrvgf trldpaqvaa sclppfvcpd leeqsptwaa llpegfvrag
      121 nvvcfwvnrr gwlfakvnag rplllrkdvl vqgaplwavm dvygttkaie lldpkanawi
      181 tsgepmpese vtsgeecvic fhntantrlm pcghsqfcgs cawhifkdta rcpmcrwqie
      241 evavepsvks gegs
//
LOCUS       NP_001009964             517 aa            linear   ROD 27-APR-2025
DEFINITION  T-box transcription factor TBX5 [Rattus norvegicus].
ACCESSION   NP_001009964 XP_222201
VERSION     NP_001009964.1
DBSOURCE    REFSEQ: accession NM_001009964.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Jia,Y., Chang,Y., Guo,Z. and Li,H.
  TITLE     Transcription factor Tbx5 promotes cardiomyogenic differentiation
            of cardiac fibroblasts treated with 5-azacytidine
  JOURNAL   J Cell Biochem 120 (10), 16503-16515 (2019)
   PUBMED   31265161
  REMARK    GeneRIF: Transcription factor Tbx5 promotes cardiomyogenic
            differentiation of cardiac fibroblasts treated with 5-azacytidine.
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Li,M., Zhang,Y.L., Huang,H. and Xiong,Y.
  TITLE     MicroRNA-10-5p regulates differentiation of bone marrow mesenchymal
            stem cells into cardiomyocytes by targeting TBX5
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (2), 479-485 (2019)
   PUBMED   30720154
  REMARK    GeneRIF: The MicroRNA-10-5p regulates BMSCs differentiation into
            cardiomyocytes by binding to TBX5.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Ono,A., Hirooka,K., Nakano,Y., Nitta,E., Nishiyama,A. and
            Tsujikawa,A.
  TITLE     Gene expression changes in the retina after systemic administration
            of aldosterone
  JOURNAL   Jpn J Ophthalmol 62 (4), 499-507 (2018)
   PUBMED   29713904
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Ghosh,T.K., Aparicio-Sanchez,J.J., Buxton,S., Ketley,A.,
            Mohamed,T., Rutland,C.S., Loughna,S. and Brook,J.D.
  TITLE     Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb
            development
  JOURNAL   J Mol Cell Cardiol 114, 185-198 (2018)
   PUBMED   29174768
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Wang,D., Zhai,G., Ji,Y. and Jing,H.
  TITLE     microRNA-10a Targets T-box 5 to Inhibit the Development of Cardiac
            Hypertrophy
  JOURNAL   Int Heart J 58 (1), 100-106 (2017)
   PUBMED   28100873
  REMARK    GeneRIF: miR-10a may inhibit cardiac hypertrophy via targeting
            Tbx5.
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Ghosh,T.K., Packham,E.A., Bonser,A.J., Robinson,T.E., Cross,S.J.
            and Brook,J.D.
  TITLE     Characterization of the TBX5 binding site and analysis of mutations
            that cause Holt-Oram syndrome
  JOURNAL   Hum Mol Genet 10 (18), 1983-1994 (2001)
   PUBMED   11555635
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Hiroi,Y., Kudoh,S., Monzen,K., Ikeda,Y., Yazaki,Y., Nagai,R. and
            Komuro,I.
  TITLE     Tbx5 associates with Nkx2-5 and synergistically promotes
            cardiomyocyte differentiation
  JOURNAL   Nat Genet 28 (3), 276-280 (2001)
   PUBMED   11431700
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Hatcher,C.J., Kim,M.S., Mah,C.S., Goldstein,M.M., Wong,B.,
            Mikawa,T. and Basson,C.T.
  TITLE     TBX5 transcription factor regulates cell proliferation during
            cardiogenesis
  JOURNAL   Dev Biol 230 (2), 177-188 (2001)
   PUBMED   11161571
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Basson,C.T., Bachinsky,D.R., Lin,R.C., Levi,T., Elkins,J.A.,
            Soults,J., Grayzel,D., Kroumpouzou,E., Traill,T.A.,
            Leblanc-Straceski,J., Renault,B., Kucherlapati,R., Seidman,J.G. and
            Seidman,C.E.
  TITLE     Mutations in human TBX5 [corrected] cause limb and cardiac
            malformation in Holt-Oram syndrome
  JOURNAL   Nat Genet 15 (1), 30-35 (1997)
   PUBMED   8988165
  REMARK    Erratum:[Nat Genet 1997 Apr;15(4):411]
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Li,Q.Y., Newbury-Ecob,R.A., Terrett,J.A., Wilson,D.I., Curtis,A.R.,
            Yi,C.H., Gebuhr,T., Bullen,P.J., Robson,S.C., Strachan,T.,
            Bonnet,D., Lyonnet,S., Young,I.D., Raeburn,J.A., Buckler,A.J.,
            Law,D.J. and Brook,J.D.
  TITLE     Holt-Oram syndrome is caused by mutations in TBX5, a member of the
            Brachyury (T) gene family
  JOURNAL   Nat Genet 15 (1), 21-29 (1997)
   PUBMED   8988164
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY859491.1.
            
            On Jan 22, 2005 this sequence version replaced XP_222201.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY859491.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..517
                     /product="T-box transcription factor TBX5"
                     /note="T-box protein 5; T-box 5"
                     /calculated_mol_wt=57614
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I2P1.1)"
     Region          54..238
                     /region_name="T-box_TBX4_5-like"
                     /note="DNA-binding domain of T-box transcription factor 4
                     and 5, and related T-box proteins; cd20189"
                     /db_xref="CDD:410315"
     Site            order(81..82,159,162,175..176,215,217,223,226..227,
                     230..236)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410315"
     Site            order(101,108..109,128,131,133,135,137,141..142,182,184,
                     187,199..201)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:410315"
     Site            order(140..142,150)
                     /site_type="other"
                     /note="NKX2.5 interface [polypeptide binding]"
                     /db_xref="CDD:410315"
     Region          270..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I2P1.1)"
     Region          331..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I2P1.1)"
     Site            338
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99593; propagated from
                     UniProtKB/Swiss-Prot (Q5I2P1.1)"
     CDS             1..517
                     /gene="Tbx5"
                     /coded_by="NM_001009964.1:21..1574"
                     /db_xref="GeneID:304514"
                     /db_xref="RGD:1305702"
ORIGIN      
        1 madadegfgl artplepdsk drscdskpes algapsksps spqaaftqqg megikvflhe
       61 relwlkfhev gtemiitkag rqmfpsykvk vtglnpktky illmdivpad dhrykfadnk
      121 wsvtgkaepa mpgrlyvhpd spatgahwmr qlvsfqklkl tnnhldpfgh iilnsmhkyq
      181 prlhivkade nngfgsknta fcthvfpeta fiavtsyqnh kitqlkienn pfakgfrgsd
      241 dlelhrmsrm rskeypvvpr stvrhkvanh spfssetral stssnlgsqy qcengvsgps
      301 qdllpppnpy plaqehsqiy hctkrkdeec sstehpykkp ymetspseed tfyrsgypqq
      361 qglstsyrte saqrqacmya ssappsepvp slediscntw psmpsyssct vttvqpmdrl
      421 pyqhfsahft sgplvprlag manhgspqlg egmfqhqtsv thqpvvrqcg pqtglqspgs
      481 lqppeflyth gvprtlsphq yhsvhgvgmv pewsens
//
LOCUS       NP_068607                334 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Jun [Rattus norvegicus].
ACCESSION   NP_068607
VERSION     NP_068607.1
DBSOURCE    REFSEQ: accession NM_021835.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Li,Q., Li,S., Xu,C., Zhao,J., Hou,L., Jiang,F., Zhu,Z., Wang,Y. and
            Tian,L.
  TITLE     microRNA-149-5p mediates the PM2.5-induced inflammatory response by
            targeting TAB2 via MAPK and NF-kappaB signaling pathways in vivo
            and in vitro
  JOURNAL   Cell Biol Toxicol 39 (3), 703-717 (2023)
   PUBMED   34331613
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shi,H., Duan,L., Lan,Y., He,Q., Pu,P. and Tang,H.
  TITLE     RING Finger Protein 10 Regulates AP-1/Meox2 to Mediate
            Pirarubicin-Induced Cardiomyocyte Apoptosis
  JOURNAL   Oxid Med Cell Longev 2023, 7872193 (2023)
   PUBMED   36713029
  REMARK    GeneRIF: RING Finger Protein 10 Regulates AP-1/Meox2 to Mediate
            Pirarubicin-Induced Cardiomyocyte Apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Ramesh,R., Manurung,Y., Ma,K.H., Blakely,T. Jr., Won,S.,
            Moreno-Ramos,O.A., Wyatt,E., Awatramani,R. and Svaren,J.
  TITLE     JUN Regulation of Injury-Induced Enhancers in Schwann Cells
  JOURNAL   J Neurosci 42 (34), 6506-6517 (2022)
   PUBMED   35906072
  REMARK    GeneRIF: JUN Regulation of Injury-Induced Enhancers in Schwann
            Cells.
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Alam,M. and Mishra,R.
  TITLE     Bcl-xL expression and regulation in the progression, recurrence,
            and cisplatin resistance of oral cancer
  JOURNAL   Life Sci 280, 119705 (2021)
   PUBMED   34111459
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Tan,Y., Cao,H., Li,Q. and Sun,J.
  TITLE     The role of transcription factor Ap1 in the activation of the
            Nrf2/ARE pathway through TET1 in diabetic nephropathy
  JOURNAL   Cell Biol Int 45 (8), 1654-1665 (2021)
   PUBMED   33760331
  REMARK    GeneRIF: The role of transcription factor Ap1 in the activation of
            the Nrf2/ARE pathway through TET1 in diabetic nephropathy.
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Pravenec,M., Gauguier,D., Schott,J.J., Buard,J., Kren,V., Bila,V.,
            Szpirer,C., Szpirer,J., Wang,J.M., Huang,H. et al.
  TITLE     Mapping of quantitative trait loci for blood pressure and cardiac
            mass in the rat by genome scanning of recombinant inbred strains
  JOURNAL   J Clin Invest 96 (4), 1973-1978 (1995)
   PUBMED   7560090
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Kitabayashi,I., Kawakami,Z., Chiu,R., Ozawa,K., Matsuoka,T.,
            Toyoshima,S., Umesono,K., Evans,R.M., Gachelin,G. and Yokoyama,K.
  TITLE     Transcriptional regulation of the c-jun gene by retinoic acid and
            E1A during differentiation of F9 cells
  JOURNAL   EMBO J 11 (1), 167-175 (1992)
   PUBMED   1310930
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Kitabayashi,I., Saka,F., Gachelin,G. and Yokoyama,K.
  TITLE     Nucleotide sequence of rat c-jun protooncogene
  JOURNAL   Nucleic Acids Res 18 (11), 3400 (1990)
   PUBMED   2113275
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Sakai,M., Okuda,A., Hatayama,I., Sato,K., Nishi,S. and Muramatsu,M.
  TITLE     Structure and expression of the rat c-jun messenger RNA: tissue
            distribution and increase during chemical hepatocarcinogenesis
  JOURNAL   Cancer Res 49 (20), 5633-5637 (1989)
   PUBMED   2507134
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Mermod,N., Williams,T.J. and Tjian,R.
  TITLE     Enhancer binding factors AP-4 and AP-1 act in concert to activate
            SV40 late transcription in vitro
  JOURNAL   Nature 332 (6164), 557-561 (1988)
   PUBMED   2833704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB740532.1, BE113912.1, BC078738.1, CK475341.1 and BF414978.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..334
                     /product="transcription factor Jun"
                     /note="transcription factor AP-1; AP1; activator protein
                     1; proto-oncogene c-jun; V-jun avian sarcoma virus 17
                     oncogene homolog; v-jun sarcoma virus 17 oncogene homolog;
                     Avian sarcoma virus 17 (v-jun) oncogene homolog; Jun
                     oncogene; transcription factor AP-1 subunit Jun"
                     /calculated_mol_wt=35870
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Region          6..243
                     /region_name="Jun"
                     /note="Jun-like transcription factor; pfam03957"
                     /db_xref="CDD:461108"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05627; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and PLK3.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and PLK3.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Region          150..226
                     /region_name="Interaction with PAGE4.
                     /evidence=ECO:0000250|UniProtKB:P05412"
                     /note="propagated from UniProtKB/Swiss-Prot (P17325.1)"
     Region          184..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17325.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2 and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Region          255..282
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P17325.1)"
     Region          257..317
                     /region_name="bZIP_Jun"
                     /note="Basic leucine zipper (bZIP) domain of Jun proteins
                     and similar proteins: a DNA-binding and dimerization
                     domain; cd14696"
                     /db_xref="CDD:269844"
     Region          258..309
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269844"
     Site            order(262,264..266,268..273,275..277)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269844"
     Site            274
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            275
                     /site_type="other"
                     /note="Necessary for synergistic transcriptional activity
                     with SMAD3. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     Site            order(276..277,279..280,282..284,286..287,290..291,
                     293..294,296..298,300..301,304..305,308,311,314..317)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269844"
     Region          283..311
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P17325.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK2.
                     /evidence=ECO:0000250|UniProtKB:P05412; propagated from
                     UniProtKB/Swiss-Prot (P17325.1)"
     CDS             1..334
                     /gene="Jun"
                     /coded_by="NM_021835.3:859..1863"
                     /db_xref="GeneID:24516"
                     /db_xref="RGD:2943"
ORIGIN      
        1 mtakmettfy ddalnasflq sesgaygysn pkilkqsmtl nladpvgnlk phlraknsdl
       61 ltspdvgllk laspelerli iqssnghitt tptptqflcp knvtdeqegf aegfvralae
      121 lhsqntlpsv tsaaqpvsga gmvapavasv agagggggys aslhseppvy anlsnfnpga
      181 lssgggapsy gatglafpsq pqqqqqppqp phhlpqqipv qhprlqalke epqtvpempg
      241 etpplspidm esqerikaer krmrnriaas kcrkrkleri arleekvktl kaqnselast
      301 anmlreqvaq lkqkvmnhvn sgcqlmltqq lqtf
//
LOCUS       NP_001005892             271 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor PU.1 [Rattus norvegicus].
ACCESSION   NP_001005892 XP_345403
VERSION     NP_001005892.1
DBSOURCE    REFSEQ: accession NM_001005892.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Yu,M., Ou,Y., Wang,H. and Gu,W.
  TITLE     PU.1 interaction with p50 promotes microglial-mediated inflammation
            in secondary spinal cord injury in SCI rats
  JOURNAL   Int J Neurosci 133 (4), 389-402 (2023)
   PUBMED   33970748
  REMARK    GeneRIF: PU.1 interaction with p50 promotes microglial-mediated
            inflammation in secondary spinal cord injury in SCI rats.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Cai,X., Hong,L., Liu,Y., Huang,X., Lai,H. and Shao,L.
  TITLE     Salmonella pathogenicity island 1 knockdown confers protection
            against myocardial fibrosis and inflammation in uremic
            cardiomyopathy via down-regulation of S100 Calcium Binding Protein
            A8/A9 transcription
  JOURNAL   Ren Fail 44 (1), 1819-1832 (2022)
   PUBMED   36299239
  REMARK    GeneRIF: Salmonella pathogenicity island 1 knockdown confers
            protection against myocardial fibrosis and inflammation in uremic
            cardiomyopathy via down-regulation of S100 Calcium Binding Protein
            A8/A9 transcription.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Lipponen,A., El-Osta,A., Kaspi,A., Ziemann,M., Khurana,I., Kn,H.,
            Navarro-Ferrandis,V., Puhakka,N., Paananen,J. and Pitkanen,A.
  TITLE     Transcription factors Tp73, Cebpd, Pax6, and Spi1 rather than DNA
            methylation regulate chronic transcriptomics changes after
            experimental traumatic brain injury
  JOURNAL   Acta Neuropathol Commun 6 (1), 17 (2018)
   PUBMED   29482641
  REMARK    GeneRIF: Four upregulated transcription factors Pax6, Tp73, Cebpd,
            and Spi1, appeared as potent regulators of chronic post-traumatic
            brain injury (TBI) gene expression. They regulate molecular
            networks contributing to post-injury secondary damage, including
            apoptosis and inflammation, strengthening the feasibility of
            therapeutically targeting these molecular networks even after the
            acute post-TBI period.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Staitieh,B.S., Fan,X., Neveu,W. and Guidot,D.M.
  TITLE     Nrf2 regulates PU.1 expression and activity in the alveolar
            macrophage
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 308 (10), L1086-L1093 (2015)
   PUBMED   25840997
  REMARK    GeneRIF: Nrf2 regulates the expression and activity of PU.1 and
            that antioxidant response and immune activation are coordinately
            regulated within the AM.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Delatte,B., Deplus,R. and Fuks,F.
  TITLE     Playing TETris with DNA modifications
  JOURNAL   EMBO J 33 (11), 1198-1211 (2014)
   PUBMED   24825349
  REMARK    Review article
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Guerriero,A., Langmuir,P.B., Spain,L.M. and Scott,E.W.
  TITLE     PU.1 is required for myeloid-derived but not lymphoid-derived
            dendritic cells
  JOURNAL   Blood 95 (3), 879-885 (2000)
   PUBMED   10648399
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Egan,B.S., Lane,K.B. and Shepherd,V.L.
  TITLE     PU.1 and USF are required for macrophage-specific mannose receptor
            promoter activity
  JOURNAL   J Biol Chem 274 (13), 9098-9107 (1999)
   PUBMED   10085160
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Scott,E.W., Fisher,R.C., Olson,M.C., Kehrli,E.W., Simon,M.C. and
            Singh,H.
  TITLE     PU.1 functions in a cell-autonomous manner to control the
            differentiation of multipotential lymphoid-myeloid progenitors
  JOURNAL   Immunity 6 (4), 437-447 (1997)
   PUBMED   9133423
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Borras,F.E., Lloberas,J., Maki,R.A. and Celada,A.
  TITLE     Repression of I-A beta gene expression by the transcription factor
            PU.1
  JOURNAL   J Biol Chem 270 (41), 24385-24391 (1995)
   PUBMED   7592651
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Hagman,J. and Grosschedl,R.
  TITLE     An inhibitory carboxyl-terminal domain in Ets-1 and Ets-2 mediates
            differential binding of ETS family factors to promoter sequences of
            the mb-1 gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 8889-8893 (1992)
   PUBMED   1409581
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091185.1.
            
            On Oct 22, 2004 this sequence version replaced XP_345403.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091185.1, AB154364.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..271
                     /product="transcription factor PU.1"
                     /note="hematopoietic transcription factor PU.1; SFFV
                     proviral integration 1; spleen focus forming virus
                     proviral integration oncogene spi1; spleen focus forming
                     virus (SFFV) proviral integration oncogene spi1"
                     /calculated_mol_wt=30958
     Region          124..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS1.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17947; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS1.1)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17947; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS1.1)"
     Region          172..253
                     /region_name="Ets"
                     /note="Ets-domain; pfam00178"
                     /db_xref="CDD:459700"
     CDS             1..271
                     /gene="Spi1"
                     /gene_synonym="Pu.1; Sfpi1"
                     /coded_by="NM_001005892.2:156..971"
                     /db_xref="GeneID:366126"
                     /db_xref="RGD:1359607"
ORIGIN      
        1 mlqackmegf plvappsdel vtyeselyqr qthdyyslig gdgdshsdhy wdfsthhvhs
       61 efesfpenhf telqsvqppq lqqlyrhmel eqmhvldtpm apphaslshq vsymprvcfp
      121 ypplspahqq ssdeeegerq spplevsdge adglepgpgl lhgetgskkk irlyqflldl
      181 lrsgdmkdsi wwvdkdkgtf qfsskhkeal ahrwgiqkgn rkkmtyqkma ralrnygktg
      241 evkkvkkklt yqfsgevlgr gglaerrlpp h
//
LOCUS       NP_062057                500 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2C11 [Rattus norvegicus].
ACCESSION   NP_062057
VERSION     NP_062057.2
DBSOURCE    REFSEQ: accession NM_019184.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Navarro-Mabarak,C., Loaiza-Zuluaga,M., Hernandez-Ojeda,S.L.,
            Camacho-Carranza,R. and Espinosa-Aguirre,J.J.
  TITLE     Neuroinflammation is able to downregulate cytochrome P450
            epoxygenases 2J3 and 2C11 in the rat brain
  JOURNAL   Brain Res Bull 163, 57-64 (2020)
   PUBMED   32707261
  REMARK    GeneRIF: Neuroinflammation is able to downregulate cytochrome P450
            epoxygenases 2J3 and 2C11 in the rat brain.
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Navarro-Mabarak,C., Mitre-Aguilar,I.B., Camacho-Carranza,R.,
            Arias,C., Zentella-Dehesa,A. and Espinosa-Aguirre,J.J.
  TITLE     Role of NF-kappaB in cytochrome P450 epoxygenases down-regulation
            during an inflammatory process in astrocytes
  JOURNAL   Neurochem Int 129, 104499 (2019)
   PUBMED   31271766
  REMARK    GeneRIF: Inflammation in astrocytes could down-regulate CYP2C11
            mRNA, protein and activity.Inhibition of NF-kappaB partially
            prevented the down-regulation of CYP2C11 mRNA and protein.NF-kappaB
            is able to bind to at least two response elements in the promoter
            of Cyp2c11.
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Wei,Y., Yang,L., Zhang,X., Sui,D., Wang,C., Wang,K., Shan,M.,
            Guo,D. and Wang,H.
  TITLE     Generation and Characterization of a CYP2C11-Null Rat Model by
            Using the CRISPR/Cas9 Method
  JOURNAL   Drug Metab Dispos 46 (5), 525-531 (2018)
   PUBMED   29444903
  REMARK    GeneRIF: A CYP2C11-null rat model was successfully generated and is
            a valuable tool to study the in vivo function of CYP2C11.
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Raish,M., Ahmad,A., Alkharfy,K.M., Jan,B.L., Mohsin,K., Ahad,A.,
            Al-Jenoobi,F.I. and Al-Mohizea,A.M.
  TITLE     Effects of Paeonia emodi on hepatic cytochrome P450 (CYP3A2 and
            CYP2C11) expression and pharmacokinetics of carbamazepine in rats
  JOURNAL   Biomed Pharmacother 90, 694-698 (2017)
   PUBMED   28419964
  REMARK    GeneRIF: The PE extract also showed a significant potential to
            reduce CYP3A and CYP2C protein expression by approximately 50%.
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Xu,M., Tang,H., Rong,Q., Zhang,Y., Li,Y., Zhao,L., Ye,G., Shi,F.
            and Lv,C.
  TITLE     The Effects of Formaldehyde on Cytochrome P450 Isoform Activity in
            Rats
  JOURNAL   Biomed Res Int 2017, 6525474 (2017)
   PUBMED   28555194
  REMARK    GeneRIF: acute Formaldehyde (FA) poisoning suppressed the
            activities of CYP2C11, CYP2E1, and CYP3A2 and induced the activity
            of CYP1A2 in rats. And the change of CYP450 activity caused by
            acute FA poisoning may be associated with FA potential carcinogenic
            effects on the airways.
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Strom,A., Mode,A., Zaphiropoulos,P., Nilsson,A.G., Morgan,E. and
            Gustafsson,J.A.
  TITLE     Cloning and pretranslational hormonal regulation of testosterone 16
            alpha-hydroxylase (P-45016 alpha) in male rat liver
  JOURNAL   Acta Endocrinol (Copenh) 118 (2), 314-320 (1988)
   PUBMED   2455430
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Zaphiropoulos,P.G., Mode,A., Strom,A., Husman,B., Andersson,G. and
            Gustafsson,J.A.
  TITLE     Sequence and regulation of two growth-hormone-controlled,
            sex-specific isozymes of cytochrome P-450 in rat liver,
            P-450(15)beta and P-450(16)alpha
  JOURNAL   Acta Med Scand Suppl 723, 161-167 (1988)
   PUBMED   3164963
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Morishima,N., Yoshioka,H., Higashi,Y., Sogawa,K. and
            Fujii-Kuriyama,Y.
  TITLE     Gene structure of cytochrome P-450(M-1) specifically expressed in
            male rat liver
  JOURNAL   Biochemistry 26 (25), 8279-8285 (1987)
   PUBMED   2894840
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Yoshioka,H., Morohashi,K., Sogawa,K., Miyata,T., Kawajiri,K.,
            Hirose,T., Inayama,S., Fujii-Kuriyama,Y. and Omura,T.
  TITLE     Structural analysis and specific expression of microsomal
            cytochrome P-450(M-1) mRNA in male rat livers
  JOURNAL   J Biol Chem 262 (4), 1706-1711 (1987)
   PUBMED   3805049
  REMARK    Erratum:[J Biol Chem 1987 Jun 15;262(17):8438]
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Matsumoto,T., Emi,Y., Kawabata,S. and Omura,T.
  TITLE     Purification and characterization of three male-specific and one
            female-specific forms of cytochrome P-450 from rat liver microsomes
  JOURNAL   J Biochem 100 (5), 1359-1371 (1986)
   PUBMED   2434473
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J02657.1.
            
            On Jan 25, 2008 this sequence version replaced NP_062057.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02657.1, U33173.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..500
                     /product="cytochrome P450 2C11"
                     /EC_number="1.14.14.1"
                     /note="UT-2; P450H; CYPIIC11; P450-UT-A; P-450(M-1);
                     cytochrome P450H; cytochrome P450-UT-2; cytochrome
                     P450-UT-A; cytochrome P-450(M-1); cytochrome P450, 2c29;
                     cytochrome P450, subfamily IIC (mephenytoin
                     4-hydroxylase), polypeptide 11; cytochrome P450 2C11-like"
                     /calculated_mol_wt=57050
     Region          61..484
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(97,112..113,120,124,294,297..298,301..302,305,356,
                     361..362,365..366,368,427..429,433,435..437,441,444)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(108,113..114,204..205,208,214,233,237,240,292..293,
                     296..297,300..301,362,366,476..477)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     CDS             1..500
                     /gene="Cyp2c11"
                     /gene_synonym="Cyp2c; Cyp2c11l; CYP2CII"
                     /coded_by="NM_019184.2:21..1523"
                     /db_xref="GeneID:29277"
                     /db_xref="RGD:2469"
ORIGIN      
        1 mdpvlvlvlt lssllllslw rqsfgrgklp pgptplpiig ntlqiymkdi gqsikkfskv
       61 ygpiftlylg mkpfvvlhgy eavkealvdl geefsgrgsf pvservnkgl gvifsngmqw
      121 keirrfsimt lrtfgmgkrt iedriqeeaq clveelrksk gapfdptfil gcapcnvics
      181 iifqnrfdyk dptflnlmhr fnenfrlfss pwlqvcntfp aiidyfpgsh nqvlknffyi
      241 knyvlekvke hqesldkdnp rdfidcflnk meqekhnpqs eftleslvat vtdmfgagte
      301 ttsttlrygl llllkhvdvt akvqeeierv igrnrspcmk drsqmpytda vvheiqryid
      361 lvptnlphlv trdikfrnyf ipkgtnvivs lssilhddke fpnpekfdpg hfldergnfk
      421 ksdyfmpfsa gkricageal artelflfft tilqnfnlks lvdvkdidtt paisgfghlp
      481 pfyeacfipv qradslsshl
//
LOCUS       NP_997679                142 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import receptor subunit TOM22 homolog [Rattus
            norvegicus].
ACCESSION   NP_997679 XP_216977
VERSION     NP_997679.1
DBSOURCE    REFSEQ: accession NM_212514.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Bose,H.S., Whittal,R.M., Marshall,B., Rajapaksha,M., Wang,N.P.,
            Bose,M., Perry,E.W., Zhao,Z.Q. and Miller,W.L.
  TITLE     A Novel Mitochondrial Complex of Aldosterone Synthase,
            Steroidogenic Acute Regulatory Protein, and Tom22 Synthesizes
            Aldosterone in the Rat Heart
  JOURNAL   J Pharmacol Exp Ther 377 (1), 108-120 (2021)
   PUBMED   33526603
  REMARK    GeneRIF: A Novel Mitochondrial Complex of Aldosterone Synthase,
            Steroidogenic Acute Regulatory Protein, and Tom22 Synthesizes
            Aldosterone in the Rat Heart.
            Erratum:[J Pharmacol Exp Ther. 2021 Apr;377(1):200. doi:
            10.1124/jpet.120.000365err. PMID: 33757981]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Ellenrieder,L., Martensson,C.U. and Becker,T.
  TITLE     Biogenesis of mitochondrial outer membrane proteins, problems and
            diseases
  JOURNAL   Biol Chem 396 (11), 1199-1213 (2015)
   PUBMED   25980382
  REMARK    Review article
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Wenz,L.S., Opalinski,L., Wiedemann,N. and Becker,T.
  TITLE     Cooperation of protein machineries in mitochondrial protein sorting
  JOURNAL   Biochim Biophys Acta 1853 (5), 1119-1129 (2015)
   PUBMED   25633533
  REMARK    Review article
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Schulz,C., Schendzielorz,A. and Rehling,P.
  TITLE     Unlocking the presequence import pathway
  JOURNAL   Trends Cell Biol 25 (5), 265-275 (2015)
   PUBMED   25542066
  REMARK    Review article
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Humphries,A.D., Streimann,I.C., Stojanovski,D., Johnston,A.J.,
            Yano,M., Hoogenraad,N.J. and Ryan,M.T.
  TITLE     Dissection of the mitochondrial import and assembly pathway for
            human Tom40
  JOURNAL   J Biol Chem 280 (12), 11535-11543 (2005)
   PUBMED   15644312
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Nakamura,Y., Suzuki,H., Sakaguchi,M. and Mihara,K.
  TITLE     Targeting and assembly of rat mitochondrial translocase of outer
            membrane 22 (TOM22) into the TOM complex
  JOURNAL   J Biol Chem 279 (20), 21223-21232 (2004)
   PUBMED   14985332
  REMARK    GeneRIF: Analysis of signals that target rat TOM22 to the
            mitochondrial outer membrane and assembly into the TOM complex in
            cultured mammalian cells.
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Johnston,A.J., Hoogenraad,J., Dougan,D.A., Truscott,K.N., Yano,M.,
            Mori,M., Hoogenraad,N.J. and Ryan,M.T.
  TITLE     Insertion and assembly of human tom7 into the preprotein
            translocase complex of the outer mitochondrial membrane
  JOURNAL   J Biol Chem 277 (44), 42197-42204 (2002)
   PUBMED   12198123
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Suzuki,H., Maeda,M. and Mihara,K.
  TITLE     Characterization of rat TOM70 as a receptor of the preprotein
            translocase of the mitochondrial outer membrane
  JOURNAL   J Cell Sci 115 (Pt 9), 1895-1905 (2002)
   PUBMED   11956321
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098639.1.
            
            On Aug 30, 2004 this sequence version replaced XP_216977.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098639.1, EV776729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..142
                     /product="mitochondrial import receptor subunit TOM22
                     homolog"
                     /note="translocase of outer membrane 22 kDa subunit
                     homolog; translocase of outer mitochondrial membrane 22
                     homolog"
                     /calculated_mol_wt=15360
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NS69; propagated from
                     UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q75Q41.1)"
     Region          41..50
                     /region_name="Import sequence, necessary for mitochondrion
                     outer membrane localization and integration in the TOM
                     complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NS69; propagated from
                     UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CPQ3; propagated from
                     UniProtKB/Swiss-Prot (Q75Q41.1)"
     Region          49..105
                     /region_name="TOM22"
                     /note="Mitochondrial import receptor subunit TOM22 and
                     similar proteins; cd22884"
                     /db_xref="CDD:439375"
     Region          83..103
                     /region_name="TMD, necessary for mitochondrion outer
                     membrane localization and integration in the TOM complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q41.1)"
     Site            order(86..87,90..91,93..95,97..98,101..102,105)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:439375"
     Site            order(90,93,97..98,101,105)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:439375"
     Region          123..142
                     /region_name="C-tail signal, necessary for mitochondrion
                     outer membrane localization and integration in the TOM
                     complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q41.1)"
     CDS             1..142
                     /gene="Tomm22"
                     /gene_synonym="rTOM22; TOM22"
                     /coded_by="NM_212514.2:14..442"
                     /db_xref="GeneID:300075"
                     /db_xref="RGD:1303260"
ORIGIN      
        1 maaavaaaga geplspeelv pkaeaekaee dleeddddel detlserlwg ltemfpervr
       61 saagatfdls lfvaqkmyrf sraalwigtt sfmilvlpvv feteklqmeq qqqlqqrqil
      121 lgpntglsgg mpgalpplpg ki
//
LOCUS       NP_001014047             444 aa            linear   ROD 27-APR-2025
DEFINITION  ATPase PAAT [Rattus norvegicus].
ACCESSION   NP_001014047 XP_219322
VERSION     NP_001014047.1
DBSOURCE    REFSEQ: accession NM_001014025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Yang,X., Yang,J., Li,L., Sun,L., Yi,X., Han,X., Si,W., Yan,R.,
            Chen,Z., Xie,G., Li,W., Shang,Y. and Liang,J.
  TITLE     PAAT, a novel ATPase and trans-regulator of mitochondrial ABC
            transporters, is critically involved in the maintenance of
            mitochondrial homeostasis
  JOURNAL   FASEB J 28 (11), 4821-4834 (2014)
   PUBMED   25063848
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083846.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219322.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083846.1, SRR8487226.68813.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..444
                     /product="ATPase PAAT"
                     /EC_number="3.6.1.3"
                     /note="uncharacterized protein C10orf88 homolog; protein
                     associated with ABC transporters"
                     /calculated_mol_wt=48689
     Region          59..198
                     /region_name="PAAT-like"
                     /note="ATPase PAAT-like; pfam14958"
                     /db_xref="CDD:464404"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8K7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI46.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8K7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI46.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8K7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI46.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8K7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI46.1)"
     Region          424..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI46.1)"
     CDS             1..444
                     /gene="C1h10orf88"
                     /gene_synonym="PAAT; RGD1305014"
                     /coded_by="NM_001014025.1:3..1337"
                     /db_xref="GeneID:309029"
                     /db_xref="RGD:1305014"
ORIGIN      
        1 metaiedagl drgptltssw daacgaltqs lfltrtgpra qdldfeqlla ppaqgpdlvs
       61 lksslsprde npcfiylkcg pnggeeilsv gilssarnme vylgeeycgt srgknvctvl
      121 dnsehekill ykkylklesp thackiklls fgeeqcvlis kvvvhlrprs akpspsspal
      181 gsridldniq timesmgskl spgaqqlmdm irfqqqnclp irdqlqsvlg taghkhlmal
      241 qsspssgvvd kasstpfpfr tgltpsaite nlkalidkst qpsgegnttn hnechlmpqn
      301 hslesdlkna vssflpkkas gsssvpnsel lpflqnlcsq vnhlrvghna rwqenvskpr
      361 egtvgvplee qpvcsyleki lsknmevmek klmkhideri yqlqehidak mallvdllrs
      421 pnspspgmpl rhydsrerls nger
//
LOCUS       NP_001019407             309 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription factor IIH subunit 3 [Rattus norvegicus].
ACCESSION   NP_001019407 XP_213778
VERSION     NP_001019407.1
DBSOURCE    REFSEQ: accession NM_001024236.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   He,Y., Yan,C., Fang,J., Inouye,C., Tjian,R., Ivanov,I. and
            Nogales,E.
  TITLE     Near-atomic resolution visualization of human transcription
            promoter opening
  JOURNAL   Nature 533 (7603), 359-365 (2016)
   PUBMED   27193682
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Egly,J.M. and Coin,F.
  TITLE     A history of TFIIH: two decades of molecular biology on a pivotal
            transcription/repair factor
  JOURNAL   DNA Repair (Amst) 10 (7), 714-721 (2011)
   PUBMED   21592869
  REMARK    Review article
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Kershnar,E., Wu,S.Y. and Chiang,C.M.
  TITLE     Immunoaffinity purification and functional characterization of
            human transcription factor IIH and RNA polymerase II from clonal
            cell lines that conditionally express epitope-tagged subunits of
            the multiprotein complexes
  JOURNAL   J Biol Chem 273 (51), 34444-34453 (1998)
   PUBMED   9852112
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Iyer,N., Reagan,M.S., Wu,K.J., Canagarajah,B. and Friedberg,E.C.
  TITLE     Interactions involving the human RNA polymerase II
            transcription/nucleotide excision repair complex TFIIH, the
            nucleotide excision repair protein XPG, and Cockayne syndrome group
            B (CSB) protein
  JOURNAL   Biochemistry 35 (7), 2157-2167 (1996)
   PUBMED   8652557
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC093380.1.
            
            On May 27, 2005 this sequence version replaced XP_213778.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093380.1, SRR8487230.117016.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..309
                     /product="general transcription factor IIH subunit 3"
                     /note="general transcription factor IIH, polypeptide 3"
                     /calculated_mol_wt=34147
     Region          7..290
                     /region_name="tfb4"
                     /note="transcription factor tfb4; TIGR00627"
                     /db_xref="CDD:273181"
     CDS             1..309
                     /gene="Gtf2h3"
                     /coded_by="NM_001024236.1:25..954"
                     /db_xref="GeneID:288651"
                     /db_xref="RGD:1305494"
ORIGIN      
        1 maadedelnl lviivdtnpi wwgkqalkes qftlskcmda vmvlanahlf mnrsnqlavi
       61 ashiqesrfl ypgkngrlgd ffgdpgnalp dcnpsgskdg kyelltaane viaeeikdlm
      121 tksdikgqht etllagslak alcyihrask avkdnqemks rilvikaaed salqymnfmn
      181 vifaaqkqni lidacvldsd sgllqqacdi tgglylkvpq mpsllqyllw vflpdqdqrs
      241 qlilpppihv dyraacfchr slieigyvcs vclsifcnfs picttcetaf kislppvlka
      301 kkkkqkvsl
//
LOCUS       NP_001100734             901 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear factor of activated T-cells, cytoplasmic 4 [Rattus
            norvegicus].
ACCESSION   NP_001100734 XP_001061815 XP_240184
VERSION     NP_001100734.1
DBSOURCE    REFSEQ: accession NM_001107264.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Li,M., Fang,X.Z., Liu,X.T., Zheng,Y.F., Xie,Y.B., Ma,X.D., Xia,Y.
            and Shao,D.H.
  TITLE     Inhibition of calcineurin/NFATc4 signaling attenuates
            ventilator-induced lung injury
  JOURNAL   Mol Med Rep 21 (2), 607-614 (2020)
   PUBMED   31789412
  REMARK    GeneRIF: Inhibition of calcineurin/NFATc4 signaling attenuates
            ventilatorinduced lung injury.
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Su,Q., Liu,M., Jiang,M., Wang,Y., Ma,X., Li,S. and Xie,J.
  TITLE     Involvement of calcineurin/NFATc4 pathway in a single-prolonged
            stress-based rat model of post-traumatic stress disorder
  JOURNAL   Mol Biol Rep 46 (6), 6197-6204 (2019)
   PUBMED   31486013
  REMARK    GeneRIF: Our results show that CaN/NFATc4 pathway were involved in
            the development of PTSD model, which suggested that the changes of
            CaN/NFATc4 pathway may be one of the pathological molecular
            mechanism in the dysfunction of hippocampus in PTSD.
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Kuwata,H., Yuzurihara,C., Kinoshita,N., Taki,Y., Ikegami,Y.,
            Washio,S., Hirakawa,Y., Yoda,E., Aiuchi,T., Itabe,H., Nakatani,Y.
            and Hara,S.
  TITLE     The group VIA calcium-independent phospholipase A2 and NFATc4
            pathway mediates IL-1beta-induced expression of chemokines CCL2 and
            CXCL10 in rat fibroblasts
  JOURNAL   FEBS J 285 (11), 2056-2070 (2018)
   PUBMED   29637744
  REMARK    GeneRIF: the transcriptional activation of nuclear factor of
            activated T-cell proteins (NFATs), but not nuclear factor-kappaB,
            by IL-1beta stimulation was markedly attenuated by the iPLA2
            inhibitor bromoenol lactone, and NFATc4 knockdown markedly
            attenuated the IL-1beta-induced expression of both CCL2 and CXCL10.
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Li,M., He,H.P., Gong,H.Q., Zhang,J., Ma,W.J., Zhou,H., Cao,D.S.,
            Wang,N. and Zhang,T.C.
  TITLE     NFATc4 and myocardin synergistically up-regulate the expression of
            LTCC alpha1C in ET-1-induced cardiomyocyte hypertrophy
  JOURNAL   Life Sci 155, 11-20 (2016)
   PUBMED   27155398
  REMARK    GeneRIF: results suggest a novel mechanism of the transcriptional
            regulation of LTCC alpha1C by synergistic activities of NFATc4 and
            myocardin in ET-1-induced cardiomyocyte hypertrophy
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Asadi,F., Razmi,A., Dehpour,A.R. and Shafiei,M.
  TITLE     Tropisetron inhibits high glucose-induced calcineurin/NFAT
            hypertrophic pathway in H9c2 myocardial cells
  JOURNAL   J Pharm Pharmacol 68 (4), 485-493 (2016)
   PUBMED   26945895
  REMARK    GeneRIF: Tropisetron may have protective effects against high
            glucose-induced cardiomyocyte hypertrophy. The mechanism
            responsible for this beneficial effect seems to be, at least in
            part, blockade of calcineurin/NFATc4 signalling pathway.
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Bushdid,P.B., Osinska,H., Waclaw,R.R., Molkentin,J.D. and
            Yutzey,K.E.
  TITLE     NFATc3 and NFATc4 are required for cardiac development and
            mitochondrial function
  JOURNAL   Circ Res 92 (12), 1305-1313 (2003)
   PUBMED   12750314
REFERENCE   7  (residues 1 to 901)
  AUTHORS   Wilkins,B.J., De Windt,L.J., Bueno,O.F., Braz,J.C., Glascock,B.J.,
            Kimball,T.F. and Molkentin,J.D.
  TITLE     Targeted disruption of NFATc3, but not NFATc4, reveals an intrinsic
            defect in calcineurin-mediated cardiac hypertrophic growth
  JOURNAL   Mol Cell Biol 22 (21), 7603-7613 (2002)
   PUBMED   12370307
REFERENCE   8  (residues 1 to 901)
  AUTHORS   Hunton,D.L., Lucchesi,P.A., Pang,Y., Cheng,X., Dell'Italia,L.J. and
            Marchase,R.B.
  TITLE     Capacitative calcium entry contributes to nuclear factor of
            activated T-cells nuclear translocation and hypertrophy in
            cardiomyocytes
  JOURNAL   J Biol Chem 277 (16), 14266-14273 (2002)
   PUBMED   11827959
  REMARK    GeneRIF: Capacitative calcium entry contributes to nuclear factor
            of activated T-cells nuclear translocation and hypertrophy in
            cardiomyocytes.
REFERENCE   9  (residues 1 to 901)
  AUTHORS   Graef,I.A., Chen,F., Chen,L., Kuo,A. and Crabtree,G.R.
  TITLE     Signals transduced by Ca(2+)/calcineurin and NFATc3/c4 pattern the
            developing vasculature
  JOURNAL   Cell 105 (7), 863-875 (2001)
   PUBMED   11439183
REFERENCE   10 (residues 1 to 901)
  AUTHORS   Molkentin,J.D., Lu,J.R., Antos,C.L., Markham,B., Richardson,J.,
            Robbins,J., Grant,S.R. and Olson,E.N.
  TITLE     A calcineurin-dependent transcriptional pathway for cardiac
            hypertrophy
  JOURNAL   Cell 93 (2), 215-228 (1998)
   PUBMED   9568714
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474049.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_240184.2, XP_001061815.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132291,
                              SAMD00132296 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..901
                     /product="nuclear factor of activated T-cells, cytoplasmic
                     4"
                     /note="nuclear factor of activated T-cells, cytoplasmic,
                     calcineurin-dependent 4; T-cell transcription factor
                     NFAT3"
                     /calculated_mol_wt=95633
     Region          1..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          <40..407
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          114..119
                     /region_name="Calcineurin-binding.
                     /evidence=ECO:0000250|UniProtKB:Q14934"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K120; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K120; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          203..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          213..293
                     /region_name="2 approximate SP repeats.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14934; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14934; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          268..270
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K120; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14934; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14934; propagated from
                     UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          407..580
                     /region_name="RHD-n_NFAT"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of activated T-cells (NFAT)
                     proteins; cd07881"
                     /db_xref="CDD:143641"
     Site            order(430,433,435..436,438..440,487,528,530..531,545..546,
                     548,579)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143641"
     Region          585..685
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(609,673)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     Region          672..674
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          697..721
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     Region          791..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z9H7.1)"
     CDS             1..901
                     /gene="Nfatc4"
                     /gene_synonym="NF-AT3; NF-ATc4"
                     /coded_by="NM_001107264.1:138..2843"
                     /db_xref="GeneID:305897"
                     /db_xref="RGD:1310749"
ORIGIN      
        1 mgaascedee lefklvfgee keapplgpgg pgeeldseda ppccrlalge plpygaapig
       61 iprpppprpg mhsppprpap spgtwesqpp rsvrlggpgg taggtgggrv lecpsirits
      121 isptpdppts ledapetwgd gsprdypppe gfggyreagg qgggaffsps pgssslssws
      181 ffsdasdeaa lyaacdeves elneaasrfg lssplpspra sprpwtpedp wslygpssgg
      241 rapedswlll sapgpipasp rpaspcgkrr ysssgtpssa spalsrrgsl geegpepppp
      301 pplplvrdps ssgpfdyvga pptesvpqkt rrtsseqava lprseepasc ngklpsgted
      361 svaapgalrk emagmdylav psplawskar igghspifrt salppldwpl psqyeqlelr
      421 ievqprahhr ahyetegsrg avkaapgghp vvkllgynek pltlqmfigt aderslrpha
      481 fyqvhritgk mvatasyeav vsgtkvlemt llpennmaan idcagilklr nsdielrkge
      541 tdigrkntrv rlvfrvhvpq gggkvvsvqa asvpiecsqr saqelpqvea yspsacsvrg
      601 geelvltgsn flpdskvvfi ergpdgklqw eeeaavnrlq ssevtltlti peysnkrvsr
      661 pvqvyfyvsn grrkrsptqs fkflpvifke eplpdsslrg fpstsgppfg pdmdfspprp
      721 pypsyphedp ayetpylseg fgystpalyp qtgpppsyrs glrmfpetgg ttgcarlpsv
      781 sflprpfpgd qyggqgssfp lglpfsppap frpplpsspp ledpfnpqsa vhplpaegyn
      841 evgpgytpge gaseqeksrg gygsgfrdnv piqgitleev seiigrdlsg fparpgeepp
      901 a
//
LOCUS       NP_001037739             278 aa            linear   ROD 27-APR-2025
DEFINITION  odontogenic ameloblast-associated protein precursor [Rattus
            norvegicus].
ACCESSION   NP_001037739 XP_001071185 XP_001074023
VERSION     NP_001037739.1
DBSOURCE    REFSEQ: accession NM_001044274.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lee,H.K., Ji,S., Park,S.J., Choung,H.W., Choi,Y., Lee,H.J.,
            Park,S.Y. and Park,J.C.
  TITLE     Odontogenic Ameloblast-associated Protein (ODAM) Mediates
            Junctional Epithelium Attachment to Teeth via Integrin-ODAM-Rho
            Guanine Nucleotide Exchange Factor 5 (ARHGEF5)-RhoA Signaling
  JOURNAL   J Biol Chem 290 (23), 14740-14753 (2015)
   PUBMED   25911094
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Lee,H.K., Park,S.J., Oh,H.J., Kim,J.W., Bae,H.S. and Park,J.C.
  TITLE     Expression pattern, subcellular localization, and functional
            implications of ODAM in ameloblasts, odontoblasts, osteoblasts, and
            various cancer cells
  JOURNAL   Gene Expr Patterns 12 (3-4), 102-108 (2012)
   PUBMED   22387195
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Nishio,C., Wazen,R., Kuroda,S., Moffatt,P. and Nanci,A.
  TITLE     Expression pattern of odontogenic ameloblast-associated and
            amelotin during formation and regeneration of the junctional
            epithelium
  JOURNAL   Eur Cell Mater 20, 393-402 (2010)
   PUBMED   21154245
  REMARK    GeneRIF: ODAM and AMTN have a role at the cell-tooth interface, and
            that ODAM is likely also implicated in cellular events during
            formation and regeneration of the junctional epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Yang,I.S., Lee,D.S., Park,J.T., Kim,H.J., Son,H.H. and Park,J.C.
  TITLE     Tertiary dentin formation after direct pulp capping with
            odontogenic ameloblast-associated protein in rat teeth
  JOURNAL   J Endod 36 (12), 1956-1962 (2010)
   PUBMED   21092812
  REMARK    GeneRIF: accelerates reactionary dentin formation close to the pulp
            exposure area
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Moffatt,P., Smith,C.E., St-Arnaud,R. and Nanci,A.
  TITLE     Characterization of Apin, a secreted protein highly expressed in
            tooth-associated epithelia
  JOURNAL   J Cell Biochem 103 (3), 941-956 (2008)
   PUBMED   17647262
  REMARK    GeneRIF: The protein sequences deduced from the cloned cDNA for
            rat, mouse, pig, and human were aligned together with those
            obtained from four other mammal genomes. Apin is highly conserved
            in mammals.
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Moffatt,P., Smith,C.E., Sooknanan,R., St-Arnaud,R. and Nanci,A.
  TITLE     Identification of secreted and membrane proteins in the rat incisor
            enamel organ using a signal-trap screening approach
  JOURNAL   Eur J Oral Sci 114 Suppl 1, 139-46 (2006)
   PUBMED   16674676
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Khoo,J.P., Nicoli,T., Alp,N.J., Fullerton,J., Flint,J. and
            Channon,K.M.
  TITLE     Congenic mapping and genotyping of the
            tetrahydrobiopterin-deficient hph-1 mouse
  JOURNAL   Mol Genet Metab 82 (3), 251-254 (2004)
   PUBMED   15234340
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Solomon,A., Murphy,C.L., Weaver,K., Weiss,D.T., Hrncic,R.,
            Eulitz,M., Donnell,R.L., Sletten,K., Westermark,G. and
            Westermark,P.
  TITLE     Calcifying epithelial odontogenic (Pindborg) tumor-associated
            amyloid consists of a novel human protein
  JOURNAL   J Lab Clin Med 142 (5), 348-355 (2003)
   PUBMED   14647039
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ198380.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_001071185.1, XP_001074023.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ198380.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..278
                     /product="odontogenic ameloblast-associated protein
                     precursor"
                     /note="odontogenic ameloblast-associated protein; APIN;
                     odontogenic, ameloblast asssociated"
                     /calculated_mol_wt=28931
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1530
     mat_peptide     16..278
                     /product="Odontogenic ameloblast-associated protein.
                     /id=PRO_5000140667"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS83.1)"
                     /calculated_mol_wt=28931
     Region          16..278
                     /region_name="ODAM"
                     /note="Odontogenic ameloblast-associated family;
                     pfam15424"
                     /db_xref="CDD:464710"
     Region          103..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            116
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            120
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     Region          126..128
                     /region_name="Interaction with ARHGEF5.
                     /evidence=ECO:0000250|UniProtKB:A1E959"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS83.1)"
     Region          230..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            240
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            243
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            249
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     Site            254
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3HS83.1)"
     CDS             1..278
                     /gene="Odam"
                     /gene_synonym="Apin"
                     /coded_by="NM_001044274.1:54..890"
                     /db_xref="GeneID:641555"
                     /db_xref="RGD:1561883"
ORIGIN      
        1 mkiiillgli gatssaplit qrllsasnsh elllnlnngq llplqfqsaf nswippfpgl
       61 lqqqqqqaqv sghpqfplst lesfaglfpn qipfsrqvgf aqggqagqpd fsqqqtpsqt
      121 qqaspmsyvv pvkvpqdqtq mfqyypvyml lpweqpqqtv tsspqqtgqq lyeeqipfyn
      181 qfgfvpqqae pgvpggqqhl vldsfvgtap etpgmpaveg plypqkepig fkqdnvgvst
      241 pstspkpdtg nfftseinpt iapllpeqkv nadslrep
//
LOCUS       NP_001099834             376 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-centractin [Rattus norvegicus].
ACCESSION   NP_001099834 XP_001059244 XP_238177
VERSION     NP_001099834.1
DBSOURCE    REFSEQ: accession NM_001106364.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Garifulin,O.M., Kykot,V.O., Gridina,N.Y., Kiyamova,R.G., Gout,I.T.
            and Filonenko,V.V.
  TITLE     Application of serex-analysis for identification of human colon
            cancer antigens
  JOURNAL   Exp Oncol 37 (3), 173-180 (2015)
   PUBMED   26422100
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kiyomitsu,T. and Cheeseman,I.M.
  TITLE     Chromosome- and spindle-pole-derived signals generate an intrinsic
            code for spindle position and orientation
  JOURNAL   Nat Cell Biol 14 (3), 311-317 (2012)
   PUBMED   22327364
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Schroer,T.A.
  TITLE     Dynactin
  JOURNAL   Annu Rev Cell Dev Biol 20, 759-779 (2004)
   PUBMED   15473859
  REMARK    Review article
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Gulesserian,T., Kim,S.H., Fountoulakis,M. and Lubec,G.
  TITLE     Aberrant expression of centractin and capping proteins, integral
            constituents of the dynactin complex, in fetal down syndrome brain
  JOURNAL   Biochem Biophys Res Commun 291 (1), 62-67 (2002)
   PUBMED   11829462
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Fouquet,J., Kann,M., Soues,S. and Melki,R.
  TITLE     ARP1 in Golgi organisation and attachment of manchette microtubules
            to the nucleus during mammalian spermatogenesis
  JOURNAL   J Cell Sci 113 (Pt 5), 877-886 (2000)
   PUBMED   10671377
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Heimann,K., Percival,J.M., Weinberger,R., Gunning,P. and Stow,J.L.
  TITLE     Specific isoforms of actin-binding proteins on distinct populations
            of Golgi-derived vesicles
  JOURNAL   J Biol Chem 274 (16), 10743-10750 (1999)
   PUBMED   10196146
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_238177.4, XP_001059244.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..376
                     /product="alpha-centractin"
                     /note="centractin; ARP1 actin-related protein 1 homolog A,
                     centractin alpha; ARP1 actin related protein 1 homolog A"
                     /calculated_mol_wt=42483
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61163; propagated from
                     UniProtKB/Swiss-Prot (P85515.1)"
     Region          9..375
                     /region_name="ASKHA_NBD_Arp1"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein 1 (Arp1) and similar proteins; cd10216"
                     /db_xref="CDD:466820"
     CDS             1..376
                     /gene="Actr1a"
                     /coded_by="NM_001106364.1:65..1195"
                     /db_xref="GeneID:294010"
                     /db_xref="RGD:1307025"
ORIGIN      
        1 mesydvianq pvvidngsgv ikagfagdqi pkycfpnyvg rpkhvrvmag alegdifigp
       61 kaeehrglls irypmehgiv kdwndmeriw qyvyskdqlq tfseehpvll teaplnprkn
      121 reraaevffe tfnvpalfis mqavlslyat grttgvvlds gdgvthavpi yegfamphsi
      181 mridiagrdv srflrlylrk egydfhssse feivkaiker acylsinpqk detletekaq
      241 yylpdgstie igpsrfrape llfrpdlige esegihevlv faiqksdmdl rrtlfsnivl
      301 sggstlfkgf gdrllsevkk lapkdvkiri sapqerlyst wiggsilasl dtfkkmwvsk
      361 keyeedgars ihrktf
//
LOCUS       NP_001008802             625 aa            linear   ROD 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 1 [Rattus norvegicus].
ACCESSION   NP_001008802
VERSION     NP_001008802.2
DBSOURCE    REFSEQ: accession NM_001008802.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Zhang,L., Zeng,X.X., Li,Y.M., Chen,S.K., Tang,L.Y., Wang,N.,
            Yang,X. and Lin,M.J.
  TITLE     Keratin 1 attenuates hypoxic pulmonary artery hypertension by
            suppressing pulmonary artery media smooth muscle expansion
  JOURNAL   Acta Physiol (Oxf) 231 (2), e13558 (2021)
   PUBMED   32920982
  REMARK    GeneRIF: Keratin 1 attenuates hypoxic pulmonary artery hypertension
            by suppressing pulmonary artery media smooth muscle expansion.
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Bunick,C.G. and Milstone,L.M.
  TITLE     The X-Ray Crystal Structure of the Keratin 1-Keratin 10 Helix 2B
            Heterodimer Reveals Molecular Surface Properties and Biochemical
            Insights into Human Skin Disease
  JOURNAL   J Invest Dermatol 137 (1), 142-150 (2017)
   PUBMED   27595935
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Soteriou,D., Iskender,B., Byron,A., Humphries,J.D.,
            Borg-Bartolo,S., Haddock,M.C., Baxter,M.A., Knight,D.,
            Humphries,M.J. and Kimber,S.J.
  TITLE     Comparative proteomic analysis of supportive and unsupportive
            extracellular matrix substrates for human embryonic stem cell
            maintenance
  JOURNAL   J Biol Chem 288 (26), 18716-18731 (2013)
   PUBMED   23658023
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Roth,W., Kumar,V., Beer,H.D., Richter,M., Wohlenberg,C., Reuter,U.,
            Thiering,S., Staratschek-Jox,A., Hofmann,A., Kreusch,F.,
            Schultze,J.L., Vogl,T., Roth,J., Reichelt,J., Hausser,I. and
            Magin,T.M.
  TITLE     Keratin 1 maintains skin integrity and participates in an
            inflammatory network in skin through interleukin-18
  JOURNAL   J Cell Sci 125 (Pt 22), 5269-5279 (2012)
   PUBMED   23132931
REFERENCE   6  (residues 1 to 625)
  AUTHORS   van Niel,G., Raposo,G., Candalh,C., Boussac,M., Hershberg,R.,
            Cerf-Bensussan,N. and Heyman,M.
  TITLE     Intestinal epithelial cells secrete exosome-like vesicles
  JOURNAL   Gastroenterology 121 (2), 337-349 (2001)
   PUBMED   11487543
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Mahdi,F., Shariat-Madar,Z., Todd,R.F. 3rd, Figueroa,C.D. and
            Schmaier,A.H.
  TITLE     Expression and colocalization of cytokeratin 1 and urokinase
            plasminogen activator receptor on endothelial cells
  JOURNAL   Blood 97 (8), 2342-2350 (2001)
   PUBMED   11290596
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Sprecher,E., Ishida-Yamamoto,A., Becker,O.M., Marekov,L.,
            Miller,C.J., Steinert,P.M., Neldner,K. and Richard,G.
  TITLE     Evidence for novel functions of the keratin tail emerging from a
            mutation causing ichthyosis hystrix
  JOURNAL   J Invest Dermatol 116 (4), 511-519 (2001)
   PUBMED   11286616
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Steinert,P.M. and Marekov,L.N.
  TITLE     The proteins elafin, filaggrin, keratin intermediate filaments,
            loricrin, and small proline-rich proteins 1 and 2 are isodipeptide
            cross-linked components of the human epidermal cornified cell
            envelope
  JOURNAL   J Biol Chem 270 (30), 17702-17711 (1995)
   PUBMED   7543090
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Itoh,N., Yonehara,S., Schreurs,J., Gorman,D.M., Maruyama,K.,
            Ishii,A., Yahara,I., Arai,K. and Miyajima,A.
  TITLE     Cloning of an interleukin-3 receptor gene: a member of a distinct
            receptor gene family
  JOURNAL   Science 247 (4940), 324-327 (1990)
   PUBMED   2404337
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127464.1.
            
            On Dec 31, 2006 this sequence version replaced NP_001008802.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127464.1, BK001580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132264 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..625
                     /product="keratin, type II cytoskeletal 1"
                     /note="K1; CK-1; cytokeratin-1; type-II keratin Kb1;
                     keratin 1, type II"
                     /calculated_mol_wt=64626
     Region          1..178
                     /region_name="Head. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04264; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            51
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04264; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          <144..175
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          178..491
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          179..214
                     /region_name="Coil 1A. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          215..233
                     /region_name="Linker 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          234..325
                     /region_name="Coil 1B. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            275
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04264; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          326..349
                     /region_name="Linker 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          350..488
                     /region_name="Coil 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            432
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          489..625
                     /region_name="Tail. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          496..525
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            517
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Region          560..625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            574
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     Site            596
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04104; propagated from
                     UniProtKB/Swiss-Prot (Q6IMF3.1)"
     CDS             1..625
                     /gene="Krt1"
                     /gene_synonym="Kb1"
                     /coded_by="NM_001008802.2:49..1926"
                     /db_xref="GeneID:300250"
                     /db_xref="RGD:1359664"
ORIGIN      
        1 msfqcssrsl crsggggggr nfssgsaglv sfqrrstsss mrrsgggggg rfsgggfcgs
       61 sgggfgsksl vnlgggrsis isvagggssy gggfgggsyg ggsfgggsfg ggvgggfggg
      121 gfggggfgsg ggfgggrfgg gfgpvcppgg iqevtinqsl lqplnvevdp qiqkvksqer
      181 eqikslndkf asfidkvrfl eqqnqvlqtk wellqqvdts trtqnldpff esyisnlrrq
      241 vdslkndqsr mdselknmqd lveeyrtkye deinkrtnae nefvtikkdv dsaymnkael
      301 qarvdnlqqd idffstlyqm elsqmqtqis etnvvlsmdn nrtldldgii aevkaqydsi
      361 cqrskaeaet fyqskyeelq itagkhgdsv kntkmeisel nrviqrlrse idsvkkqisq
      421 mqqnisdaeq rgekalkdaq nklneiedal tqakeeltrl lrdyqelmnt klaldmeiat
      481 yrkllegeei rmsgectpnv svsvstshts msgsssrggg rygsgggggg gsygggsrgg
      541 sygggsgggs ygggssgggs gggsygggss gghrggsggg ggssggsygg ssgggrggss
      601 sgggvkssgs ssvkfvstty srgtn
//
LOCUS       NP_599242                260 aa            linear   ROD 27-APR-2025
DEFINITION  ribosome biogenesis protein NSA2 homolog [Rattus norvegicus].
ACCESSION   NP_599242 XP_231263
VERSION     NP_599242.2
DBSOURCE    REFSEQ: accession NM_134415.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Shahni,R., Gnudi,L., King,A., Jones,P. and Malik,A.N.
  TITLE     Elevated levels of renal and circulating Nop-7-associated 2 (NSA2)
            in rat and mouse models of diabetes, in mesangial cells in vitro
            and in patients with diabetic nephropathy
  JOURNAL   Diabetologia 55 (3), 825-834 (2012)
   PUBMED   22095236
  REMARK    GeneRIF: Data suggest that renal and circulating NSA2 levels are
            increased in hyperglycemia in experimental models of diabetes, and
            that circulating NSA2 is elevated in diabetic nephropathy patients
            with albuminuria.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Sandhu,H., Dehnen,W., Roller,M., Abel,J. and Unfried,K.
  TITLE     mRNA expression patterns in different stages of asbestos-induced
            carcinogenesis in rats
  JOURNAL   Carcinogenesis 21 (5), 1023-1029 (2000)
   PUBMED   10783328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CR473148.1, BC098657.1, BP486932.1 and BP485557.1.
            
            On Mar 10, 2007 this sequence version replaced NP_599242.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ226635.1, FQ214845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN16093042
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..260
                     /product="ribosome biogenesis protein NSA2 homolog"
                     /note="TGF beta-inducible nuclear protein;
                     TGF-beta-inducible nuclear protein 1; NSA2 ribosome
                     biogenesis homolog"
                     /calculated_mol_wt=29905
     Region          4..260
                     /region_name="NSA2"
                     /note="pre-ribosomal protein NSA2 (Nop seven-associated
                     2); cd11381"
                     /db_xref="CDD:211393"
     Region          11..18
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU7.2)"
     Region          20..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU7.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95478; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU7.2)"
     CDS             1..260
                     /gene="Nsa2"
                     /gene_synonym="Cdk105; Tinp1"
                     /coded_by="NM_134415.2:99..881"
                     /db_xref="GeneID:171456"
                     /db_xref="RGD:621335"
ORIGIN      
        1 mpqneyielh rkrygyrldy hekkrkkegr eaherskkak kmiglkakly hkqrhaekiq
       61 mkktikmhek rntkqkddek tpqgavpayl ldregqsrak vlsnmikqkr kekagkwevp
      121 lpkvraqget evlkvirtgk rkkkawkrmv tkvcfvgdgf trkppkyerf irpmglrfkk
      181 ahvthpelka tfclpilgvk knpssplytt lgvitkgtvi evnvselglv tqggkviwgk
      241 yaqvtnnpen dgcinavllv
//
LOCUS       NP_001028240            1407 aa            linear   ROD 27-APR-2025
DEFINITION  enhancer of mRNA-decapping protein 4 [Rattus norvegicus].
ACCESSION   NP_001028240 XP_341680
VERSION     NP_001028240.3
DBSOURCE    REFSEQ: accession NM_001033068.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1407)
  AUTHORS   Jonas,S. and Izaurralde,E.
  TITLE     The role of disordered protein regions in the assembly of decapping
            complexes and RNP granules
  JOURNAL   Genes Dev 27 (24), 2628-2641 (2013)
   PUBMED   24352420
  REMARK    Review article
REFERENCE   2  (residues 1 to 1407)
  AUTHORS   Marnef,A., Maldonado,M., Bugaut,A., Balasubramanian,S., Kress,M.,
            Weil,D. and Standart,N.
  TITLE     Distinct functions of maternal and somatic Pat1 protein paralogs
  JOURNAL   RNA 16 (11), 2094-2107 (2010)
   PUBMED   20826699
REFERENCE   3  (residues 1 to 1407)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 1407)
  AUTHORS   Bloch,D.B., Rabkina,D., Quertermous,T. and Bloch,K.D.
  TITLE     The immunoreactive region in a novel autoantigen contains a nuclear
            localization sequence
  JOURNAL   Clin Immunol Immunopathol 72 (3), 380-389 (1994)
   PUBMED   7520377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Sep 16, 2008 this sequence version replaced NP_001028240.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103628.1, SRR26643296.38816.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1407
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..1407
                     /product="enhancer of mRNA-decapping protein 4"
                     /calculated_mol_wt=152465
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          114..440
                     /region_name="Ge1_WD40"
                     /note="WD40 region of Ge1, enhancer of mRNA-decapping
                     protein; pfam16529"
                     /db_xref="CDD:465162"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          174..214
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          230..277
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          295..334
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          304..343
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          342..393
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          349..396
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          604..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          673..745
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          787..817
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            850
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Region          875..951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            877
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     Site            1386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P2E9; propagated from
                     UniProtKB/Swiss-Prot (Q3ZAV8.1)"
     CDS             1..1407
                     /gene="Edc4"
                     /gene_synonym="LRRG00115; Nrn1l; RGD1309136"
                     /coded_by="NM_001033068.3:175..4398"
                     /db_xref="GeneID:361399"
                     /db_xref="RGD:1562009"
ORIGIN      
        1 mascasidie datqhlrdil kldrpaggsn vesqrpssay ngdlngllvp dplssgdgns
       61 tskpgirtmp pinlqekqvi clsgddsstc igilakevei vassdssiss kargsnkvki
      121 qpvakydweq kyyygnliav snsflayair aanngsamvr visvstsert llkgftgsva
      181 dlafahlnsp qlacldeagd lfvwrlalvk gkiqeeilvh irqpegtpln hfrriiwcpf
      241 ipeesedcce essptvallh edraevwdld mlrsshstwp vdvsqikqgf ivvkghstcl
      301 segalspdgt vlatashdgf vkfwqiyieg qdeprclhew kphdgrplsc llfcdnhkkq
      361 dpevpfwrfl itgadqnrel kmwctvswtc lqtirfspdi fssvsvppsl kvcldlsaey
      421 lilsdvqrkv lyvmellqnq degracfssi sefllthpvl sfgiqvvsrc rlrhtevlpa
      481 eeesdslgte sshgagtles aagvliklfc vhtkalqdvq irfqpqlnpd vvaplsthta
      541 hedftfgesr pelgseglas aphgsqpdlr rivelpapad flslssetkp klmtpdafmt
      601 ptaslqqisa spssssssss ssssssssss sssltavsav ssssamdpsl psrppeeltl
      661 spklqldgsl tissssslqa sprsllpgll pgpadklipk gpgqvssgts alsldlqeve
      721 plglpqasps rtrspdviss astalsqdip eiasealsrg fgssvpegli epdsmasaas
      781 alhllsprpr qgpelssqlg ldggpgdgdr hstpslleaa ltqevatsds qvwptapdit
      841 retcstltes prnglqekhk slafhrppyh llqqhdsqdt saeqsdhdde vaslasasgg
      901 fgskiptprl pakdwktkgs prtspklkrk skkddgdsav gsrltehqvv eppedwpali
      961 wqqqrelael whnqeellqr lcaqleglqs tvtdhveral etrheqeqrr leralaegqq
     1021 rggqlqeqlt qqlsqalssa vagrlersir deikktvppc vsrslepvag qlsnsvatkl
     1081 tavegsmken iskllksknl tdaiaraaad tlqgpmqaay reafqsvvlp afekscqamf
     1141 qqindsfrlg tqeylqqlds hmksrkareq earepvlaql rglvstlqna teqmaatvss
     1201 svraevqhql hvavgslqes ilaqvqrivk gevsvalkeq qatvtssimq amrsaagtpv
     1261 psahldcqaq qahilqllqq ghlnqafqqa ltaadlnlvl yvcetvdpaq vfgqppcpls
     1321 qpvllsliqq lasdlgtrsd lklsyleeav mhldhsdpit rdhmgsvmaq vrqklfqflq
     1381 adphnslgka arrlslmlhg lvtpslp
//
LOCUS       NP_001103355             747 aa            linear   ROD 27-APR-2025
DEFINITION  protein Niban 2 [Rattus norvegicus].
ACCESSION   NP_001103355 XP_342418
VERSION     NP_001103355.1
DBSOURCE    REFSEQ: accession NM_001109885.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Chen,S., Evans,H.G. and Evans,D.R.
  TITLE     FAM129B/MINERVA, a novel adherens junction-associated protein,
            suppresses apoptosis in HeLa cells
  JOURNAL   J Biol Chem 286 (12), 10201-10209 (2011)
   PUBMED   21148485
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Zhang,X., Gejman,R., Mahta,A., Zhong,Y., Rice,K.A., Zhou,Y.,
            Cheunsuchon,P., Louis,D.N. and Klibanski,A.
  TITLE     Maternally expressed gene 3, an imprinted noncoding RNA gene, is
            associated with meningioma pathogenesis and progression
  JOURNAL   Cancer Res 70 (6), 2350-2358 (2010)
   PUBMED   20179190
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Zhang,X., Rice,K., Wang,Y., Chen,W., Zhong,Y., Nakayama,Y., Zhou,Y.
            and Klibanski,A.
  TITLE     Maternally expressed gene 3 (MEG3) noncoding ribonucleic acid:
            isoform structure, expression, and functions
  JOURNAL   Endocrinology 151 (3), 939-947 (2010)
   PUBMED   20032057
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Gejman,R., Batista,D.L., Zhong,Y., Zhou,Y., Zhang,X.,
            Swearingen,B., Stratakis,C.A., Hedley-Whyte,E.T. and Klibanski,A.
  TITLE     Selective loss of MEG3 expression and intergenic differentially
            methylated region hypermethylation in the MEG3/DLK1 locus in human
            clinically nonfunctioning pituitary adenomas
  JOURNAL   J Clin Endocrinol Metab 93 (10), 4119-4125 (2008)
   PUBMED   18628527
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Zhou,Y., Zhong,Y., Wang,Y., Zhang,X., Batista,D.L., Gejman,R.,
            Ansell,P.J., Zhao,J., Weng,C. and Klibanski,A.
  TITLE     Activation of p53 by MEG3 non-coding RNA
  JOURNAL   J Biol Chem 282 (34), 24731-24742 (2007)
   PUBMED   17569660
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Zhang,X., Zhou,Y., Mehta,K.R., Danila,D.C., Scolavino,S.,
            Johnson,S.R. and Klibanski,A.
  TITLE     A pituitary-derived MEG3 isoform functions as a growth suppressor
            in tumor cells
  JOURNAL   J Clin Endocrinol Metab 88 (11), 5119-5126 (2003)
   PUBMED   14602737
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 10, 2007 this sequence version replaced XP_342418.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168248.1, SRR22582424.118807.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..747
                     /product="protein Niban 2"
                     /note="niban-like protein 1; family with sequence
                     similarity 129, member B"
                     /calculated_mol_wt=84600
     Region          9..557
                     /region_name="Niban-like"
                     /note="Niban-like protein; cd23949"
                     /db_xref="CDD:469558"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96TA1; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96TA1; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Region          589..747
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96TA1; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Region          606..>735
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96TA1; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96TA1; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B4F7E8.1)"
     CDS             1..747
                     /gene="Niban2"
                     /gene_synonym="Fam129b; Meg-3; RGD1307018"
                     /coded_by="NM_001109885.1:192..2435"
                     /db_xref="GeneID:362115"
                     /db_xref="RGD:1307018"
ORIGIN      
        1 mgdvlsthld darrqniaek tekilreflr fyedqygvsl fnsmrheieg tgppqaqllw
       61 rkvplderii fsgnlfqyqe dnkkwrnrfs lvphnyglvl yenkvayerq ippravinsa
      121 gykvltsldq ylelvgnslp gttsksgstp ilkcptqfpl ilwhpyarhy yfcmmteaeq
      181 dkwqavlqdc vrhcnngipe nskvegpaft dairmyrqsk eqygtwemlc gnevqilsnl
      241 vmeelgpalk telgprlkgk pqerqrqwiq isdavyrlvf eqakvhfeev lcklqlarpa
      301 meavirtdmd qiitskehla skirafilpk aevcvrnhvq pyipsileal mvptsqgfte
      361 vrdvffkevt dmnlnvineg gidklgeyme klsqlayhpl kmqscyekme plrldglqqr
      421 fdvsstsvfk qraqihmreq mdnavytfet llhqelgkgp tkeelcksiq rilervlkky
      481 dydsssvrkr ffreallqit ipfllkklap tckselprfq elifedfarf ilventyeev
      541 vlqtvmkdil qavkeaavqr khnlyrdsvv lhnsdpnlhl laegapidwg eqygdggdgs
      601 dsggspcpse aatltekrrr akqvvsvvqd eesglpfeag seppspaspd nvtelrglla
      661 qdlqaesspp aspllngapv qespqpmtvl easppasplr hlppgkavdl eppkpsdqet
      721 gekvsspgsr ppihttteds agvqtef
//
LOCUS       NP_001012116             893 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 1 [Rattus norvegicus].
ACCESSION   NP_001012116 XP_235372
VERSION     NP_001012116.1
DBSOURCE    REFSEQ: accession NM_001012116.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Neesse,A., Gangeswaran,R., Luettges,J., Feakins,R., Weeks,M.E.,
            Lemoine,N.R. and Crnogorac-Jurcevic,T.
  TITLE     Sperm-associated antigen 1 is expressed early in pancreatic
            tumorigenesis and promotes motility of cancer cells
  JOURNAL   Oncogene 26 (11), 1533-1545 (2007)
   PUBMED   16983343
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Lin,W., Zhou,X., Zhang,M., Li,Y., Miao,S., Wang,L., Zong,S. and
            Koide,S.S.
  TITLE     Expression and function of the HSD-3.8 gene encoding a
            testis-specific protein
  JOURNAL   Mol Hum Reprod 7 (9), 811-818 (2001)
   PUBMED   11517287
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085828.1.
            
            On Feb 11, 2005 this sequence version replaced XP_235372.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085828.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..893
                     /product="sperm-associated antigen 1"
                     /note="HSD-3.8; infertility-related sperm protein Spag-1"
                     /calculated_mol_wt=100485
     Region          112..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          213..246
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            order(217..218,221..222,224,247,250..251,254..255,
                     257..258,281,284..285,288..289,292)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          217..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          218..>336
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          246..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..279
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          280..313
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          280..308
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          324..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          349..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          373..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          429..463
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          <432..>569
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          432..458
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(433..434,437..438,440,468,475..476,479..480,
                     482..483,506,509..510,513..514,517)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          466..500
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          471..504
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          505..533
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          506..538
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          601..>713
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          605..638
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            order(606,609..610,613..614,616,640,643..644,647..648,
                     650..651,674,677..678,681..682,685)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          606..633
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          638..668
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          639..672
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          704..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07617; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X2.1)"
     Region          770..861
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..893
                     /gene="Spag1"
                     /coded_by="NM_001012116.1:290..2971"
                     /db_xref="GeneID:315033"
                     /db_xref="RGD:1310702"
ORIGIN      
        1 mtakvkdhpp lwgfgttktf kipiehldfk yiencsdvkq lekilcvlrs geegyypelt
       61 efcekrltgl aprsralrkd kpaatassfs aeewekidsd lkswvseikr eentrhfhdp
      121 ekhpgvedpl ppvrgsnscp rggketssks ktakkriprd yaewdkfdve kecskidedy
      181 kektvinnka hlskietkid tagltekekn flanrekgkg neafysgdye eavmyytrsl
      241 salptatayn nraqaeiklq rwssaledce kalelepgni kallrratty khqnkfleav
      301 ddlrkvlqae pdndlakktl severelkns epaselqtkg krmvieeven sgdeggkgde
      361 ddheddgvdm aamgniqkkl mvrsqggrrs rrartpmpga eqqegqpetg tastsdnhdl
      421 eerraadspg dlksrgnelf rggqfaeaav qysgaiaqle ptgsenadel silysnraac
      481 ylkegncrgc iqdcdralel qpfavkpllr ramayetleq yrsayvdyit vlkidcriql
      541 asdsvnritr ilteldgpkw rerlppipav paseplrvwh paaetpdqdp cpnsctptit
      601 dekmfqalke egnqlvkdkn ykdaiskyne clkinskaca iytnralcyl klgqfeeakl
      661 dcdkalqids knvkasyrle laqkglencr ervadpsqvv llspdsseaa rhldtkndta
      721 ppsrererrr ieiqevddss deeperpaea saveegwsae ragkievckp rnayefgqvl
      781 stisarkdee acaqllvfta pqdlpvllsn klegdmllli mqslkshlva kdpslvckhl
      841 lylskaerfe mmlaltskdq keqmaqlfdd lsdaqadclt aediqalrrq yvl
//
LOCUS       NP_068507                542 aa            linear   ROD 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_068507
VERSION     NP_068507.2
DBSOURCE    REFSEQ: accession NM_021739.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Yang,C., Zhang,M., Li,S., Yi,F., Huang,H., Xie,H., Liu,H., Huang,R.
            and Zhou,J.
  TITLE     Effects of Camk2b Overexpression and Underexpression on the
            Proteome of Rat Hippocampal Neurons
  JOURNAL   Neuroscience 503, 58-68 (2022)
   PUBMED   36041587
  REMARK    GeneRIF: Effects of Camk2b Overexpression and Underexpression on
            the Proteome of Rat Hippocampal Neurons.
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Liu,W., Li,L., Kuang,H., Xia,Y., Wang,Z., Liu,S. and Yin,D.
  TITLE     Proteomic Profile of Carbonylated Proteins Screen Regulation of
            Apoptosis via CaMK Signaling in Response to Regular Aerobic
            Exercise
  JOURNAL   Biomed Res Int 2018, 2828143 (2018)
   PUBMED   30662904
  REMARK    GeneRIF: Significantly upregulated the expression levels of
            CaMKIIbeta.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Yamazaki,H., Sasagawa,Y., Yamamoto,H., Bito,H. and Shirao,T.
  TITLE     CaMKIIbeta is localized in dendritic spines as both
            drebrin-dependent and drebrin-independent pools
  JOURNAL   J Neurochem 146 (2), 145-159 (2018)
   PUBMED   29675826
  REMARK    GeneRIF: This study provides the first evidence to show that
            CaMKIIbeta interacts with drebrin in dendritic spines.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Kury,S., van Woerden,G.M., Besnard,T., Proietti Onori,M.,
            Latypova,X., Towne,M.C., Cho,M.T., Prescott,T.E., Ploeg,M.A.,
            Sanders,S., Stessman,H.A.F., Pujol,A., Distel,B., Robak,L.A.,
            Bernstein,J.A., Denomme-Pichon,A.S., Lesca,G., Sellars,E.A.,
            Berg,J., Carre,W., Busk,O.L., van Bon,B.W.M., Waugh,J.L.,
            Deardorff,M., Hoganson,G.E., Bosanko,K.B., Johnson,D.S., Dabir,T.,
            Holla,O.L., Sarkar,A., Tveten,K., de Bellescize,J., Braathen,G.J.,
            Terhal,P.A., Grange,D.K., van Haeringen,A., Lam,C., Mirzaa,G.,
            Burton,J., Bhoj,E.J., Douglas,J., Santani,A.B., Nesbitt,A.I.,
            Helbig,K.L., Andrews,M.V., Begtrup,A., Tang,S., van Gassen,K.L.I.,
            Juusola,J., Foss,K., Enns,G.M., Moog,U., Hinderhofer,K.,
            Paramasivam,N., Lincoln,S., Kusako,B.H., Lindenbaum,P.,
            Charpentier,E., Nowak,C.B., Cherot,E., Simonet,T.,
            Ruivenkamp,C.A.L., Hahn,S., Brownstein,C.A., Xia,F., Schmitt,S.,
            Deb,W., Bonneau,D., Nizon,M., Quinquis,D., Chelly,J., Rudolf,G.,
            Sanlaville,D., Parent,P., Gilbert-Dussardier,B., Toutain,A.,
            Sutton,V.R., Thies,J., Peart-Vissers,L.E.L.M., Boisseau,P.,
            Vincent,M., Grabrucker,A.M., Dubourg,C., Tan,W.H., Verbeek,N.E.,
            Granzow,M., Santen,G.W.E., Shendure,J., Isidor,B., Pasquier,L.,
            Redon,R., Yang,Y., State,M.W., Kleefstra,T., Cogne,B.,
            Petrovski,S., Retterer,K., Eichler,E.E., Rosenfeld,J.A.,
            Agrawal,P.B., Bezieau,S., Odent,S., Elgersma,Y. and Mercier,S.
  CONSRTM   Undiagnosed Diseases Network; GEM HUGO; Deciphering Developmental
            Disorders Study
  TITLE     De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause
            Intellectual Disability
  JOURNAL   Am J Hum Genet 101 (5), 768-788 (2017)
   PUBMED   29100089
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Yan,X., Liu,J., Ye,Z., Huang,J., He,F., Xiao,W., Hu,X. and Luo,Z.
  TITLE     CaMKII-Mediated CREB Phosphorylation Is Involved in Ca2+-Induced
            BDNF mRNA Transcription and Neurite Outgrowth Promoted by
            Electrical Stimulation
  JOURNAL   PLoS One 11 (9), e0162784 (2016)
   PUBMED   27611779
  REMARK    GeneRIF: these data establish a potential signaling pathway of
            Ca2+-CaMKII-CREB in neuronal activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Bayer,K.U., Harbers,K. and Schulman,H.
  TITLE     alphaKAP is an anchoring protein for a novel CaM kinase II isoform
            in skeletal muscle
  JOURNAL   EMBO J 17 (19), 5598-5605 (1998)
   PUBMED   9755160
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Urquidi,V. and Ashcroft,S.J.
  TITLE     A novel pancreatic beta-cell isoform of
            calcium/calmodulin-dependent protein kinase II (beta 3 isoform)
            contains a proline-rich tandem repeat in the association domain
  JOURNAL   FEBS Lett 358 (1), 23-26 (1995)
   PUBMED   7821422
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Ochiishi,T., Terashima,T. and Yamauchi,T.
  TITLE     Specific distribution of Ca2+/calmodulin-dependent protein kinase
            II alpha and beta isoforms in some structures of the rat forebrain
  JOURNAL   Brain Res 659 (1-2), 179-193 (1994)
   PUBMED   7820660
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Malinow,R., Schulman,H. and Tsien,R.W.
  TITLE     Inhibition of postsynaptic PKC or CaMKII blocks induction but not
            expression of LTP
  JOURNAL   Science 245 (4920), 862-866 (1989)
   PUBMED   2549638
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB616255.1, M16112.1, CO395982.1 and JAXUCZ010000014.1.
            
            On Jun 12, 2006 this sequence version replaced NP_068507.1.
            
            Transcript Variant: This variant (2) has multiple differences in
            the coding region, compared to variant 1. The resulting protein
            (isoform 2) is shorter when it is compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M16112.1, SRR26360194.2450487.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..542
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     beta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit beta; caMK-II subunit beta; caM-kinase II
                     beta chain; caM kinase II subunit beta;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II beta; Ca++/calmodulin-dependent protein kinase II beta
                     subunit"
                     /calculated_mol_wt=60330
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P08413.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17272343; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Region          291..301
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P08413.1)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Region          349..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08413.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P28652; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08413.1)"
     Region          410..537
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..542
                     /gene="Camk2b"
                     /gene_synonym="Ck2b"
                     /coded_by="NM_021739.2:83..1711"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24245"
                     /db_xref="RGD:2262"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsvgrqt tapatmstaa sgttmglveq aksllnkkad gvkpqtnstk
      361 nssaitspkg slppaalepq ttvihnpvdg ikessdstnt tiededakar kqeiiktteq
      421 lieavnngdf eayakicdpg ltsfepealg nlvegmdfhr fyfenllakn skpihttiln
      481 phvhvigeda aciayirltq yidgqgrprt sqseetrvwh rrdgkwqnvh fhcsgapvap
      541 lq
//
LOCUS       NP_001013961             748 aa            linear   ROD 27-APR-2025
DEFINITION  ribonucleoprotein PTB-binding 1 [Rattus norvegicus].
ACCESSION   NP_001013961 XP_216612
VERSION     NP_001013961.1
DBSOURCE    REFSEQ: accession NM_001013939.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Gromak,N., Rideau,A., Southby,J., Scadden,A.D., Gooding,C.,
            Huttelmaier,S., Singer,R.H. and Smith,C.W.
  TITLE     The PTB interacting protein raver1 regulates alpha-tropomyosin
            alternative splicing
  JOURNAL   EMBO J 22 (23), 6356-6364 (2003)
   PUBMED   14633994
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083865.1.
            
            On Apr 20, 2005 this sequence version replaced XP_216612.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083865.1, SRR8487230.154767.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..748
                     /product="ribonucleoprotein PTB-binding 1"
                     /note="protein raver-1; RAVER1 homolog"
                     /calculated_mol_wt=79158
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8IY67; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IY67; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          45..60
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          59..129
                     /region_name="RRM1_RAVER1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12663"
                     /db_xref="CDD:410064"
     Site            order(67..69,91..93,117,119..121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410064"
     Region          133..209
                     /region_name="RRM2_RAVER1"
                     /note="RNA recognition motif 2 (RRM2) found found in
                     vertebrate ribonucleoprotein PTB-binding 1 (raver-1);
                     cd12665"
                     /db_xref="CDD:410066"
     Region          219..306
                     /region_name="RRM3_RAVER1"
                     /note="RNA recognition motif 3 (RRM3) found in vertebrate
                     ribonucleoprotein PTB-binding 1 (raver-1); cd12667"
                     /db_xref="CDD:410068"
     Region          307..401
                     /region_name="Interaction with PTBP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          390..505
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IY67; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IY67; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          525..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CW46; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          672..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CW46; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CW46; propagated from
                     UniProtKB/Swiss-Prot (Q5XI28.1)"
     Region          743..746
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI28.1)"
     CDS             1..748
                     /gene="Raver1"
                     /gene_synonym="Raver1h"
                     /coded_by="NM_001013939.1:17..2263"
                     /db_xref="GeneID:298705"
                     /db_xref="RGD:1359190"
ORIGIN      
        1 maadvsvthr pplspeaeae aetpetvdrr tpeqelppld peeirkrleh terqfrnrrk
       61 ilirglpgdv tnqevhdlls dyelkycfvd kykgtafvtl lngeqaeaai ntfhqsrlre
      121 relsvqlqpt dallcvanlp psltqaqfee lvrpfgsler cflvysertg hskgygfaey
      181 mkkdsaarak sdllgkplgp rtlyvhwtda gqltpallhs rclcvdhlpp gfndvdalrq
      241 alsavytptf cqlasgqdgq lkgfavleye taemaeaaqq radglalggs hlrvsfcapg
      301 ppgrsmlaal iaaqatalnr gkgllpepni lqllnnlgps aslqlllnpl lhggasgkqg
      361 llgappampl lsgpalstal lqlalqsqnq sqsqsqkkpg ilgdsplgtl qagaqpsnsl
      421 lgelsagggl apelpprrgk pqpllppllg psggdrepmg lgppasqltp ppapmglrgs
      481 slrglpkdsg plptppgvsl lgeppkdyri plnpylnlhs llpssnlagk etrgwggsgr
      541 grrpaepplp spavpgggna snngskafpm kprllspias nrlppepglp dsysfdyptd
      601 vgprrlfshp resnlgahgp srhkmsppps sfseprsggg sggplshfys gsptsyftsg
      661 lqaglkqshl nkavgsspmg ssegllglgp gpnghshllk tplggqkrsf shllpspeps
      721 pegsyvgqhs qglgghyads ylkrkrif
//
LOCUS       NP_001007675             318 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial thiamine pyrophosphate carrier [Rattus norvegicus].
ACCESSION   NP_001007675 XP_221118
VERSION     NP_001007675.1
DBSOURCE    REFSEQ: accession NM_001007674.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Ramamoorthy,K., Sabui,S., Manzon,K.I., Balamurugan,A.N. and
            Said,H.M.
  TITLE     miR-122-5p is involved in posttranscriptional regulation of the
            mitochondrial thiamin pyrophosphate transporter (SLC25A19) in
            pancreatic acinar cells
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 325 (4), G347-G355 (2023)
   PUBMED   37529835
  REMARK    GeneRIF: miR-122-5p is involved in posttranscriptional regulation
            of the mitochondrial thiamin pyrophosphate transporter (SLC25A19)
            in pancreatic acinar cells.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Lindhurst,M.J., Fiermonte,G., Song,S., Struys,E., De Leonardis,F.,
            Schwartzberg,P.L., Chen,A., Castegna,A., Verhoeven,N.,
            Mathews,C.K., Palmieri,F. and Biesecker,L.G.
  TITLE     Knockout of Slc25a19 causes mitochondrial thiamine pyrophosphate
            depletion, embryonic lethality, CNS malformations, and anemia
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15927-15932 (2006)
   PUBMED   17035501
  REMARK    GeneRIF: mitochondria of Slc25a19(-/-) and Amish lethal
            microcephaly cells have undetectable and markedly reduced thiamine
            pyrophosphate content, respectively
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Rosenberg,M.J., Agarwala,R., Bouffard,G., Davis,J., Fiermonte,G.,
            Hilliard,M.S., Koch,T., Kalikin,L.M., Makalowska,I., Morton,D.H.,
            Petty,E.M., Weber,J.L., Palmieri,F., Kelley,R.I., Schaffer,A.A. and
            Biesecker,L.G.
  TITLE     Mutant deoxynucleotide carrier is associated with congenital
            microcephaly
  JOURNAL   Nat Genet 32 (1), 175-179 (2002)
   PUBMED   12185364
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Iacobazzi,V., Ventura,M., Fiermonte,G., Prezioso,G., Rocchi,M. and
            Palmieri,F.
  TITLE     Genomic organization and mapping of the gene (SLC25A19) encoding
            the human mitochondrial deoxynucleotide carrier (DNC)
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 40-42 (2001)
   PUBMED   11474176
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079002.1.
            
            On Nov 29, 2004 this sequence version replaced XP_221118.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079002.1, SRR8487226.104023.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..318
                     /product="mitochondrial thiamine pyrophosphate carrier"
                     /note="mitochondrial uncoupling protein 1; solute carrier
                     family 25 (mitochondrial deoxynucleotide carrier), member
                     19; solute carrier family 25 (mitochondrial thiamine
                     pyrophosphate carrier), member 19"
                     /calculated_mol_wt=35507
     Region          13..106
                     /region_name="Solcar 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Region          16..108
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Region          116..202
                     /region_name="Solcar 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Region          118..203
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Region          212..311
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          214..309
                     /region_name="Solcar 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Site            220..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL0.1)"
     CDS             1..318
                     /gene="Slc25a19"
                     /coded_by="NM_001007674.1:72..1028"
                     /db_xref="GeneID:303676"
                     /db_xref="RGD:1359554"
ORIGIN      
        1 mvgydakada rsnsklevav agsvsgfvtr alispldvik irfqlqlerv cpsdpnakyh
       61 gilqaakqil qeegprafwk ghvpaqilsi gygavqflaf eeltellyqa nlyqthqfsa
      121 hfvcgglsag tatltvhpvd vlrtrlaaqg epkiysnlre airtmyrteg pfvfykgltp
      181 tviaifpyag lqfscyrslk raydwimppd gkqtgnlknl lcgcgsgvis ktltypldlf
      241 kkrlqvrgfe harsafgqvr syrglldlaq qvlqhegtrg ffkglspslm kaalstgfmf
      301 fwyelfcnlf hcirredr
//
LOCUS       NP_001030096             791 aa            linear   ROD 27-APR-2025
DEFINITION  splicing factor, suppressor of white-apricot homolog isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001030096 XP_222111
VERSION     NP_001030096.1
DBSOURCE    REFSEQ: accession NM_001034924.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Wang,J., Gao,Q.S., Wang,Y., Lafyatis,R., Stamm,S. and Andreadis,A.
  TITLE     Tau exon 10, whose missplicing causes frontotemporal dementia, is
            regulated by an intricate interplay of cis elements and trans
            factors
  JOURNAL   J Neurochem 88 (5), 1078-1090 (2004)
   PUBMED   15009664
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Sarkissian,M., Winne,A. and Lafyatis,R.
  TITLE     The mammalian homolog of suppressor-of-white-apricot regulates
            alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS
  JOURNAL   J Biol Chem 271 (49), 31106-31114 (1996)
   PUBMED   8940107
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105868.1.
            
            On Oct 21, 2005 this sequence version replaced XP_222111.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105868.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q13"
     Protein         1..791
                     /product="splicing factor, suppressor of white-apricot
                     homolog isoform 2"
                     /note="splicing factor, arginine/serine-rich 8
                     (suppressor-of-white-apricot homolog, Drosophila);
                     serine/arginine-rich splicing factor 8; splicing factor
                     SWAP homolog; suppressor of white apricot protein homolog;
                     splicing factor, suppressor of white-apricot family;
                     splicing factor, suppressor of white-apricot homolog"
                     /calculated_mol_wt=87261
     Region          83..136
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          334..381
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     CDS             1..791
                     /gene="Sfswap"
                     /gene_synonym="Sfrs8; Srsf8"
                     /coded_by="NM_001034924.1:435..2810"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304431"
                     /db_xref="RGD:1305004"
ORIGIN      
        1 mkreeeykrl sealaedgny savgftygsd yydpseptee eepskqreks eaenleenee
       61 pfiaplglsv psdvelppta kmhaiierta nfvckqgaqf eimlkakqar nsqfdflrfd
      121 hylnpyykfi qkamkegryt vlaeskseek kksgptsdne eeddeedgsy lhpslfaskk
      181 ssrleelmkp lkvvdpdhpl aalvrkaqad ssapapptad gtpaqpsqve ytadstvaam
      241 yysyymlpdg tyclappppg idvatyystl pagvtvsssp gvtttvpppp gttppppptt
      301 aesssgvtst ttttsalapv aiippppdiq pvidklaeyv arnglkfets vrakndqrfe
      361 flqpwhqyna yyefkkqffl qkegggstqa astaeeapte taveesseag edgapeasfa
      421 pisfaikake ndllpleknr vkldddseed eesrecqest ssvanpspaa appsavveek
      481 kpqltqeele akqakqkled rlaaaarekl aqaskeskek qlqaerkrka alflqtlknp
      541 lpdaevgkle estfgveetg vmpcpllvgg rtlpmlegkp perpssrcrd ppreeerekk
      601 kkkhkkrsrt rsrspkyhss skprsrshsk akhslpsayr tvrrsrsrsr sprrrahspe
      661 rrredrsvpt ayrmsgspgv srkrtrsrsp hekkkkrrsr srtkakarsq stspskqaaq
      721 rpsahsahsa sispvesrgs sqersrgvsq ekdgqissai vssvqskitq dlmakvraml
      781 aasknlqtsa s
//
LOCUS       NP_058685                175 aa            linear   ROD 27-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide precursor
            [Rattus norvegicus].
ACCESSION   NP_058685 XP_346861
VERSION     NP_058685.1
DBSOURCE    REFSEQ: accession NM_016989.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Maugeri,G., D'Amico,A.G., Magri,B., Giunta,S., Saccone,S.,
            Federico,C., Bucolo,C., Musumeci,G. and D'Agata,V.
  TITLE     Protective effect of pituitary adenylate cyclase activating
            polypeptide in diabetic keratopathy
  JOURNAL   Peptides 170, 171107 (2023)
   PUBMED   37775045
  REMARK    GeneRIF: Protective effect of pituitary adenylate cyclase
            activating polypeptide in diabetic keratopathy.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Chen,Q., Zhang,X.Y., Wang,Y.P., Fu,Y.J., Cao,F., Xu,Y.N.,
            Kong,J.G., Tian,N.X., Xu,Y. and Wang,Y.
  TITLE     Unveiling adcyap1 as a protective factor linking pain and nerve
            regeneration through single-cell RNA sequencing of rat dorsal root
            ganglion neurons
  JOURNAL   BMC Biol 21 (1), 235 (2023)
   PUBMED   37880634
  REMARK    GeneRIF: Unveiling adcyap1 as a protective factor linking pain and
            nerve regeneration through single-cell RNA sequencing of rat dorsal
            root ganglion neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Broome,S.T., Mandwie,M., Gorrie,C.A., Musumeci,G., Marzagalli,R.
            and Castorina,A.
  TITLE     Early Alterations of PACAP and VIP Expression in the Female Rat
            Brain Following Spinal Cord Injury
  JOURNAL   J Mol Neurosci 73 (9-10), 724-737 (2023)
   PUBMED   37646964
  REMARK    GeneRIF: Early Alterations of PACAP and VIP Expression in the
            Female Rat Brain Following Spinal Cord Injury.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Liu,M., He,F., Shao,M., Li,T., Wang,L., Wang,Y. and Xu,W.
  TITLE     PACAP inhibition alleviates neuropathic pain by modulating Nav1.7
            through the MAPK/ERK signaling pathway in a rat model of chronic
            constriction injury
  JOURNAL   Neuropeptides 99, 102327 (2023)
   PUBMED   36842389
  REMARK    GeneRIF: PACAP inhibition alleviates neuropathic pain by modulating
            Nav1.7 through the MAPK/ERK signaling pathway in a rat model of
            chronic constriction injury.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Hurley,J.D., Gardiner,J.V., Jones,P.M. and Bloom,S.R.
  TITLE     Cloning and molecular characterization of complementary
            deoxyribonucleic acid corresponding to a novel form of pituitary
            adenylate cyclase-activating polypeptide messenger ribonucleic acid
            in the rat testis
  JOURNAL   Endocrinology 136 (2), 550-557 (1995)
   PUBMED   7835287
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Nguyen,T.D., Heintz,G.G. and Wolfe,M.S.
  TITLE     Structural characterization of PACAP receptors on rat liver plasma
            membranes
  JOURNAL   Am J Physiol 265 (5 Pt 1), G811-G818 (1993)
   PUBMED   8238511
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Gaylinn,B.D., Harrison,J.K., Zysk,J.R., Lyons,C.E., Lynch,K.R. and
            Thorner,M.O.
  TITLE     Molecular cloning and expression of a human anterior pituitary
            receptor for growth hormone-releasing hormone
  JOURNAL   Mol Endocrinol 7 (1), 77-84 (1993)
   PUBMED   7680413
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Ogi,K., Kimura,C., Onda,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and characterization of cDNA for the precursor of
            rat pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   Biochem Biophys Res Commun 173 (3), 1271-1279 (1990)
   PUBMED   2268329
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Miyata,A., Arimura,A., Dahl,R.R., Minamino,N., Uehara,A., Jiang,L.,
            Culler,M.D. and Coy,D.H.
  TITLE     Isolation of a novel 38 residue-hypothalamic polypeptide which
            stimulates adenylate cyclase in pituitary cells
  JOURNAL   Biochem Biophys Res Commun 164 (1), 567-574 (1989)
   PUBMED   2803320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB786482.1, M63006.1 and BG664825.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346861.1.
            
            Sequence Note: The sequence M63006.1 is from a chimeric clone. Only
            the adenylate cyclase activating polypeptide 1 sequence region was
            propagated into this RefSeq record.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389,
                              SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..175
                     /product="pituitary adenylate cyclase-activating
                     polypeptide precursor"
                     /note="pituitary adenylate cyclase activating polypeptide
                     1; pituitary adenylate cyclase-activating polypeptide
                     precursor (Pacap); adenylate cyclase activating
                     polypeptide 1 (pituitary)"
                     /calculated_mol_wt=17004
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2571
     Region          83..109
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     Region          131..158
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     Region          149..157
                     /region_name="Important for receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P18509"
                     /note="propagated from UniProtKB/Swiss-Prot (P13589.2)"
     Site            157
                     /site_type="amidation"
                     /note="Leucine amide.
                     /evidence=ECO:0000250|UniProtKB:P18509; propagated from
                     UniProtKB/Swiss-Prot (P13589.2)"
     Site            168
                     /site_type="amidation"
                     /note="Lysine amide. /evidence=ECO:0000269|PubMed:2803320;
                     propagated from UniProtKB/Swiss-Prot (P13589.2)"
     CDS             1..175
                     /gene="Adcyap1"
                     /gene_synonym="Pacap"
                     /coded_by="NM_016989.2:297..824"
                     /db_xref="GeneID:24166"
                     /db_xref="RGD:2037"
ORIGIN      
        1 mtmcsgarla llvygiimhn svscspaagl sfpgirpeee aydqdgnplq dfydwdppga
       61 gspasalrda yalyypadrr dvaheilnea yrkvldqlsa rkylqsmvar gmgenlaaaa
      121 vddrapltkr hsdgiftdsy sryrkqmavk kylaavlgkr ykqrvknkgr riayl
//
LOCUS       NP_001007727             619 aa            linear   ROD 27-APR-2025
DEFINITION  dynein axonemal intermediate chain 2 [Rattus norvegicus].
ACCESSION   NP_001007727 XP_340932
VERSION     NP_001007727.1
DBSOURCE    REFSEQ: accession NM_001007726.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Mali,G.R., Yeyati,P.L., Mizuno,S., Dodd,D.O., Tennant,P.A.,
            Keighren,M.A., Zur Lage,P., Shoemark,A., Garcia-Munoz,A.,
            Shimada,A., Takeda,H., Edlich,F., Takahashi,S., von Kreigsheim,A.,
            Jarman,A.P. and Mill,P.
  TITLE     ZMYND10 functions in a chaperone relay during axonemal dynein
            assembly
  JOURNAL   Elife 7, e34389 (2018)
   PUBMED   29916806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Hjeij,R., Lindstrand,A., Francis,R., Zariwala,M.A., Liu,X., Li,Y.,
            Damerla,R., Dougherty,G.W., Abouhamed,M., Olbrich,H., Loges,N.T.,
            Pennekamp,P., Davis,E.E., Carvalho,C.M., Pehlivan,D., Werner,C.,
            Raidt,J., Kohler,G., Haffner,K., Reyes-Mugica,M., Lupski,J.R.,
            Leigh,M.W., Rosenfeld,M., Morgan,L.C., Knowles,M.R., Lo,C.W.,
            Katsanis,N. and Omran,H.
  TITLE     ARMC4 mutations cause primary ciliary dyskinesia with randomization
            of left/right body asymmetry
  JOURNAL   Am J Hum Genet 93 (2), 357-367 (2013)
   PUBMED   23849778
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Knowles,M.R., Leigh,M.W., Ostrowski,L.E., Huang,L., Carson,J.L.,
            Hazucha,M.J., Yin,W., Berg,J.S., Davis,S.D., Dell,S.D.,
            Ferkol,T.W., Rosenfeld,M., Sagel,S.D., Milla,C.E., Olivier,K.N.,
            Turner,E.H., Lewis,A.P., Bamshad,M.J., Nickerson,D.A., Shendure,J.
            and Zariwala,M.A.
  CONSRTM   Genetic Disorders of Mucociliary Clearance Consortium
  TITLE     Exome sequencing identifies mutations in CCDC114 as a cause of
            primary ciliary dyskinesia
  JOURNAL   Am J Hum Genet 92 (1), 99-106 (2013)
   PUBMED   23261302
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Loges,N.T., Olbrich,H., Fenske,L., Mussaffi,H., Horvath,J.,
            Fliegauf,M., Kuhl,H., Baktai,G., Peterffy,E., Chodhari,R.,
            Chung,E.M., Rutman,A., O'Callaghan,C., Blau,H., Tiszlavicz,L.,
            Voelkel,K., Witt,M., Zietkiewicz,E., Neesen,J., Reinhardt,R.,
            Mitchison,H.M. and Omran,H.
  TITLE     DNAI2 mutations cause primary ciliary dyskinesia with defects in
            the outer dynein arm
  JOURNAL   Am J Hum Genet 83 (5), 547-558 (2008)
   PUBMED   18950741
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Yang,Z. and Wu,J.
  TITLE     Mouse dynein axonemal intermediate chain 2: cloning and expression
  JOURNAL   DNA Cell Biol 27 (9), 479-488 (2008)
   PUBMED   18547164
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Pennarun,G., Chapelin,C., Escudier,E., Bridoux,A.M., Dastot,F.,
            Cacheux,V., Goossens,M., Amselem,S. and Duriez,B.
  TITLE     The human dynein intermediate chain 2 gene (DNAI2): cloning,
            mapping, expression pattern, and evaluation as a candidate for
            primary ciliary dyskinesia
  JOURNAL   Hum Genet 107 (6), 642-649 (2000)
   PUBMED   11153919
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081920.1.
            
            On Nov 29, 2004 this sequence version replaced XP_340932.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..619
                     /product="dynein axonemal intermediate chain 2"
                     /note="dynein intermediate chain 2, axonemal; axonemal
                     dynein intermediate chain 2; dynein, axonemal,
                     intermediate polypeptide 2"
                     /calculated_mol_wt=70187
     Region          165..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..472
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(180,197,201..202,215,234,238,244..245,261..262,281,
                     286,292..293,311,336,346,362..363,381,385,391,393,
                     405..406,424,429,435..436,448..449,469)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          214..254
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     Region          220..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..302
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     Region          266..361
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          318..347
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          362..401
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     Region          367..403
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          405..445
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     Region          410..435
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          450..489
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     Region          566..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HC9.1)"
     CDS             1..619
                     /gene="Dnai2"
                     /gene_synonym="Dnaic2"
                     /coded_by="NM_001007726.1:361..2220"
                     /db_xref="GeneID:360654"
                     /db_xref="RGD:1359602"
ORIGIN      
        1 meivyvyvkk rsefgkqcnf sdrqaelnid ispnpelaal yvernpvdtg iqcsasmseh
       61 eanterfeme ncgvnhvegg wpkdvnpqel eqtirfrkkv ekdenyinav mqlgsimehc
      121 ikqnnaidiy eeyfddeeav evteeapsak tinvfrdpqe ikrtathlsw hpdgnkklav
      181 aysclqfqrs pmgmshdsyi wdlenpnrpe ialkpsspli tleynpkdsh vllggcyngq
      241 iacwdtrkgs lvaelstief shrdpvygti wlqsktgtec fsastdgqvm wwdirkisep
      301 tevvimditr keqlenalga islefestlp tkfmvgteqg iviscnrkak tpaekivctf
      361 sghhgpiyal qrnpfypknf ltvgdwaari wseesressi mwtryhmayl sdgawspvrp
      421 avffttkmdg tldiwdlvfk qcdpalslkv cddplfclrv qdtgcliacg selgtttlle
      481 vssslstlqr nerniassif eretrrekil earhremrlk ekgkaegrdd dqkeeetald
      541 ldelvnkaee effevifael krkeaealkk kpkpkkasie vegedeledi ageeeesgii
      601 mgedtgeddm dekneggap
//
LOCUS       NP_001101838             215 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity phosphatase 29 [Rattus norvegicus].
ACCESSION   NP_001101838 XP_001057815 XP_341279
VERSION     NP_001101838.1
DBSOURCE    REFSEQ: accession NM_001108368.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Lountos,G.T., Tropea,J.E. and Waugh,D.S.
  TITLE     Structure of human dual-specificity phosphatase 27 at 2.38 A
            resolution
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 5), 471-479 (2011)
   PUBMED   21543850
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Friedberg,I., Nika,K., Tautz,L., Saito,K., Cerignoli,F.,
            Friedberg,I., Godzik,A. and Mustelin,T.
  TITLE     Identification and characterization of DUSP27, a novel
            dual-specific protein phosphatase
  JOURNAL   FEBS Lett 581 (13), 2527-2533 (2007)
   PUBMED   17498703
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474061.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057815.1, XP_341279.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW918423.1, AW918455.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..215
                     /product="dual specificity phosphatase 29"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="dual specificity phosphatase DUPD1; dual
                     specificity phosphatase and pro isomerase domain
                     containing 1"
                     /calculated_mol_wt=23942
     Region          44..203
                     /region_name="DUPD1"
                     /note="dual specificity phosphatase and pro isomerase
                     domain containing 1; cd14575"
                     /db_xref="CDD:350423"
     CDS             1..215
                     /gene="Dusp29"
                     /gene_synonym="Dupd1"
                     /coded_by="NM_001108368.1:105..752"
                     /db_xref="GeneID:361003"
                     /db_xref="RGD:1310229"
ORIGIN      
        1 masgdtktsv khahpcaerl slqqeegeae dyctpgafel erlfwkgspq ythvnevwpr
       61 lhvgdeatal dryglqkagf thvlnaahgr wnvdtgpdyy rdmaieyhgv eaddvptfdl
      121 siffysaaaf idsalqddhs kilvhcamgr srsatlvlay lmihknmtlv daiqqvaknr
      181 cvlpnrgflk qlreldkqlv kqrrqagpga gelgl
//
LOCUS       NP_001025082            2055 aa            linear   ROD 27-APR-2025
DEFINITION  citron rho-interacting kinase [Rattus norvegicus].
ACCESSION   NP_001025082 XP_573407
VERSION     NP_001025082.1
DBSOURCE    REFSEQ: accession NM_001029911.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2055)
  AUTHORS   Basit,S., Al-Harbi,K.M., Alhijji,S.A., Albalawi,A.M., Alharby,E.,
            Eldardear,A. and Samman,M.I.
  TITLE     CIT, a gene involved in neurogenic cytokinesis, is mutated in human
            primary microcephaly
  JOURNAL   Hum Genet 135 (10), 1199-1207 (2016)
   PUBMED   27519304
REFERENCE   2  (residues 1 to 2055)
  AUTHORS   Shaheen,R., Hashem,A., Abdel-Salam,G.M., Al-Fadhli,F., Ewida,N. and
            Alkuraya,F.S.
  TITLE     Mutations in CIT, encoding citron rho-interacting serine/threonine
            kinase, cause severe primary microcephaly in humans
  JOURNAL   Hum Genet 135 (10), 1191-1197 (2016)
   PUBMED   27503289
REFERENCE   3  (residues 1 to 2055)
  AUTHORS   Li,H., Bielas,S.L., Zaki,M.S., Ismail,S., Farfara,D., Um,K.,
            Rosti,R.O., Scott,E.C., Tu,S., Chi,N.C., Gabriel,S.,
            Erson-Omay,E.Z., Ercan-Sencicek,A.G., Yasuno,K., Caglayan,A.O.,
            Kaymakcalan,H., Ekici,B., Bilguvar,K., Gunel,M. and Gleeson,J.G.
  TITLE     Biallelic Mutations in Citron Kinase Link Mitotic Cytokinesis to
            Human Primary Microcephaly
  JOURNAL   Am J Hum Genet 99 (2), 501-510 (2016)
   PUBMED   27453578
REFERENCE   4  (residues 1 to 2055)
  AUTHORS   Karunakaran,D.K., Chhaya,N., Lemoine,C., Congdon,S., Black,A. and
            Kanadia,R.
  TITLE     Loss of citron kinase affects a subset of progenitor cells that
            alters late but not early neurogenesis in the developing rat retina
  JOURNAL   Invest Ophthalmol Vis Sci 56 (2), 787-798 (2015)
   PUBMED   25593024
  REMARK    GeneRIF: CitK is not required for a subset of RPCs before E14, but
            is necessary for RPC survival post E14.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2055)
  AUTHORS   Ahmed,Z., Douglas,M.R., Read,M.L., Berry,M. and Logan,A.
  TITLE     Citron kinase regulates axon growth through a pathway that
            converges on cofilin downstream of RhoA
  JOURNAL   Neurobiol Dis 41 (2), 421-429 (2011)
   PUBMED   20971191
  REMARK    GeneRIF: Citron-K regulates actin polymerization downstream of RhoA
            and may offer a potentially novel therapeutic approach for
            promoting central nervous system axon regeneration.
REFERENCE   6  (residues 1 to 2055)
  AUTHORS   Di Cunto,F., Imarisio,S., Hirsch,E., Broccoli,V., Bulfone,A.,
            Migheli,A., Atzori,C., Turco,E., Triolo,R., Dotto,G.P., Silengo,L.
            and Altruda,F.
  TITLE     Defective neurogenesis in citron kinase knockout mice by altered
            cytokinesis and massive apoptosis
  JOURNAL   Neuron 28 (1), 115-127 (2000)
   PUBMED   11086988
REFERENCE   7  (residues 1 to 2055)
  AUTHORS   Sarkisian,M.R., Rattan,S., D'Mello,S.R. and LoTurco,J.J.
  TITLE     Characterization of seizures in the flathead rat: a new genetic
            model of epilepsy in early postnatal development
  JOURNAL   Epilepsia 40 (4), 394-400 (1999)
   PUBMED   10219263
REFERENCE   8  (residues 1 to 2055)
  AUTHORS   Zhang,W., Vazquez,L., Apperson,M. and Kennedy,M.B.
  TITLE     Citron binds to PSD-95 at glutamatergic synapses on inhibitory
            neurons in the hippocampus
  JOURNAL   J Neurosci 19 (1), 96-108 (1999)
   PUBMED   9870942
REFERENCE   9  (residues 1 to 2055)
  AUTHORS   Di Cunto,F., Calautti,E., Hsiao,J., Ong,L., Topley,G., Turco,E. and
            Dotto,G.P.
  TITLE     Citron rho-interacting kinase, a novel tissue-specific ser/thr
            kinase encompassing the Rho-Rac-binding protein Citron
  JOURNAL   J Biol Chem 273 (45), 29706-29711 (1998)
   PUBMED   9792683
REFERENCE   10 (residues 1 to 2055)
  AUTHORS   Madaule,P., Eda,M., Watanabe,N., Fujisawa,K., Matsuoka,T., Bito,H.,
            Ishizaki,T. and Narumiya,S.
  TITLE     Role of citron kinase as a target of the small GTPase Rho in
            cytokinesis
  JOURNAL   Nature 394 (6692), 491-494 (1998)
   PUBMED   9697773
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jul 28, 2005 this sequence version replaced XP_573407.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2055
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..2055
                     /product="citron rho-interacting kinase"
                     /EC_number="2.7.11.1"
                     /note="citron kinase; citron (rho-interacting,
                     serine/threonine kinase 21); citron-K kinase; postsynaptic
                     density protein (citron); rho-interacting,
                     serine/threonine-protein kinase 21"
                     /calculated_mol_wt=235180
     Region          96..421
                     /region_name="STKc_CRIK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Citron Rho-interacting kinase; cd05601"
                     /db_xref="CDD:270752"
     Site            order(103..107,111,124,126,158,174..175,177,181,183,221,
                     223,225..226,228,238..239,242,256..261,294,300,303)
                     /site_type="active"
                     /db_xref="CDD:270752"
     Site            order(103..107,111,124,126,158,175..177,181,221,223,
                     225..226,228,238..239)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270752"
     Site            order(107,181,183,221,223,225,242,256..261,294,300,303)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270752"
     Site            order(238..250,251..261)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270752"
     Region          375..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSL7.1)"
     Site            415..420
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270752"
     Region          530..1327
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1349..1376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSL7.1)"
     Region          1385..1440
                     /region_name="CRIK"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in citron Rho-interacting kinase (CRIK) and similar
                     proteins; cd20814"
                     /db_xref="CDD:410364"
     Region          1470..1589
                     /region_name="PH"
                     /note="PH domain; pfam00169"
                     /db_xref="CDD:459697"
     Region          1619..1915
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     Region          1932..2040
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSL7.1)"
     CDS             1..2055
                     /gene="Cit"
                     /gene_synonym="CRIK"
                     /coded_by="NM_001029911.1:111..6278"
                     /db_xref="GeneID:83620"
                     /db_xref="RGD:70878"
ORIGIN      
        1 mlkfkygvrn pseasapepi asrasrlnlf fqgkpplmtq qqmsalsreg vldalfvlle
       61 ecsqpalmki khvssfvrky sdtiaelrel qpsvrdfevr slvgcghfae vqvvrekatg
      121 dvyamkimkk aalraqeqvs ffeeernils qstspwipql qyafqdknnl ylvmeyqpgg
      181 dllsllnrye dqldenmiqf ylaelilavh svhqmgyvhr dikpenilid rtghiklvdf
      241 gsaakmnsnk vdaklpigtp dymapevltv mnedrrgtyg ldcdwwsvgv vayemlygkt
      301 pftegtsart fnnimnfqrf lkfpddpkvs selldliqsl lcvqkerlkf eglcchpffa
      361 rtdwnnirns pppfvptlks dddtsnfdep eknswvsssp cqlspsgfsg eelpfvgfsy
      421 skalgylgrs esvvsgldsp akissmekkl likskelqds qdkchkmeqe marlhrrvse
      481 veavlsqkev elkasetqrs lleqdlatyi tecsslkrsl eqarmevsqe ddkalqllhd
      541 ireqsrklqe ikeqeyqaqv eemrlmmnql eedlvsarrr sdlyeselre srlaaeefkr
      601 kanecqhklm kakdlgkpev gecsrlekin aeqqlkiqel qeklekavka steatellqn
      661 irqakeraer eleklhnred ssegikkklv eaeerrhsle nkvkrletme rrenrlkddi
      721 qtkseqiqqm adkileleek hreaqvsaqh levhlkqkeq hyeekikvld nqikkdladk
      781 esletmmqrh eeeahekgki lseqkamina mdskirsleq rivelseank laansslftq
      841 rnmkaqeemi selrqqkfyl etqagkleaq nrkleeqlek ishqdhsdkn rlleletrlr
      901 evsleheeqk lelkrqltel qlslqeresq ltalqaaraa lesqlrqakt eleettaeae
      961 eeiqaltahr deiqrkfdal rnsctvitdl eeqlnqlted naelnnqnfy lskqldeasg
     1021 andeivqlrs evdhlrreit eremqltsqk qtmealkttc tmleeqvmdl ealndellek
     1081 erqweawrsv lgdeksqfec rvrelqrmld tekqsrarad qritesrqvv elavkehkae
     1141 ilalqqalke qklkaeslsd klndlekkha mlemnarslq qkleterelk qrlleeqakl
     1201 qqqmdlqknh ifrltqglqe aldradllkt ersdleyqle niqvlyshek vkmegtisqq
     1261 tklidflqak mdqpakkkkv plqynelkla lekekarcae leealqktri elrsareeaa
     1321 hrkatdhphp stpatarqqi amsaivrspe hqpsamslla ppssrrkeas tpeefsrrlk
     1381 ermhhniphr fnvglnmrat kcavcldtvh fgrqaskcle cqvmchpkcs tclpatcglp
     1441 aeyathftea fcrdkvsspg lqskepsssl hlegwmkvpr nnkrgqqgwd rkyivlegsk
     1501 vliydneare agqrpveefe lclpdgdvsi hgavgasela ntakadvpyi lkmeshphtt
     1561 cwpgrtlyll apsfpdkqrw vtalesvvag grvsrekaea dakllgnsll klegddrldm
     1621 nctlpfsdqv vlvgteegly alnvlknslt hipgigavfq iyiikdlekl lmiageeral
     1681 clvdvkkvkq slaqshlpaq pdvspnifea vkgchlfaag kienslcica ampskvvilr
     1741 yndnlskfci rkeietsepc scihftnysi ligtnkfyei dmkqytleef ldkndhslap
     1801 avfasstnsf pvsivqanst gqreeyllcf hefgvfvdsy grrsrtddlk wsrlplafay
     1861 repylfvthf nslevieiqa rsslgtpara yleipnpryl gpaissgaiy lassyqdklr
     1921 vicckgnlvk esgteqhrvp stsrsspnkr gpptynehit krvasspapp egpshpreps
     1981 tphryrdreg rtelrrdksp grplereksp grmlstrrer spgrlfedss rgrlpagavr
     2041 tplsqvnkvw dqssv
//
LOCUS       NP_001009633             405 aa            linear   ROD 27-APR-2025
DEFINITION  BRCA1-A complex subunit Abraxas 1 [Rattus norvegicus].
ACCESSION   NP_001009633 XP_214001
VERSION     NP_001009633.1
DBSOURCE    REFSEQ: accession NM_001009633.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wang,B., Hurov,K., Hofmann,K. and Elledge,S.J.
  TITLE     NBA1, a new player in the Brca1 A complex, is required for DNA
            damage resistance and checkpoint control
  JOURNAL   Genes Dev 23 (6), 729-739 (2009)
   PUBMED   19261749
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Feng,L., Huang,J. and Chen,J.
  TITLE     MERIT40 facilitates BRCA1 localization and DNA damage repair
  JOURNAL   Genes Dev 23 (6), 719-728 (2009)
   PUBMED   19261748
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Shao,G., Patterson-Fortin,J., Messick,T.E., Feng,D., Shanbhag,N.,
            Wang,Y. and Greenberg,R.A.
  TITLE     MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to
            DNA double-strand breaks
  JOURNAL   Genes Dev 23 (6), 740-754 (2009)
   PUBMED   19261746
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Liu,Z., Wu,J. and Yu,X.
  TITLE     CCDC98 targets BRCA1 to DNA damage sites
  JOURNAL   Nat Struct Mol Biol 14 (8), 716-720 (2007)
   PUBMED   17643121
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Wang,B., Matsuoka,S., Ballif,B.A., Zhang,D., Smogorzewska,A.,
            Gygi,S.P. and Elledge,S.J.
  TITLE     Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
            damage response
  JOURNAL   Science 316 (5828), 1194-1198 (2007)
   PUBMED   17525340
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088408.1.
            
            On Jan 13, 2005 this sequence version replaced XP_214001.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088408.1, SRR8487227.155437.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132300, SAMD00132303
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..405
                     /product="BRCA1-A complex subunit Abraxas 1"
                     /note="coiled-coil domain-containing protein 98;
                     coiled-coil domain containing 98; family with sequence
                     similarity 175, member A"
                     /calculated_mol_wt=45559
     Region          2..378
                     /region_name="Abraxas_1"
                     /note="BRCA1-A complex subunit Abraxas 1; cd23523"
                     /db_xref="CDD:467803"
     Site            order(11..13,15..17,19..20,23..28,45..47,49,62..66,68..71,
                     76,87,91,101,103..109,111..114,116,139..140,144..152,
                     163..165,168..177,179..184,186,188..191,195,199,202..203,
                     207..209,211..213,215..216,218..219,222..223,225..227,
                     229..230,233..234,236..241,243..244,246..247,250..251,253,
                     255,273..275,277..278,281..282,285..286,292,295..305,
                     319..323,325..327)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467803"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPZ8; propagated from
                     UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Site            170
                     /site_type="active"
                     /note="BRCC36 activation site [active]"
                     /db_xref="CDD:467803"
     Region          333..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6UWZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6UWZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Region          402..405
                     /region_name="pSXXF motif. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0F1.1)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6UWZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5I0F1.1)"
     CDS             1..405
                     /gene="Abraxas1"
                     /gene_synonym="Ccdc98; Fam175a; RGD1305287"
                     /coded_by="NM_001009633.1:50..1267"
                     /db_xref="GeneID:289468"
                     /db_xref="RGD:1305287"
ORIGIN      
        1 megestlgvl sgfvlgaltf qhlntdsdte glllgemkge aknsitdsqm dsvkvvytid
       61 iqkyipcyrl fsfynslgev nehalkkils nvkktvvgwy kfrrhsdqim tfreqllhrn
      121 lqthlsspel vfllltpsit tesccthcle hglykpqsgl fhkvplvvtn lgmsdqlgyk
      181 tesvsctstv fsravrtyss qffnedgslk evrkinemya aiqeelktic qkveqserev
      241 ekllmdvnrl kevrkkqqaq akgageksqn hpqenillcq alrtffpesr vlhscvislk
      301 nrhishsgcn tdhhldvvdk ltlmveyvys peaspapaap lskrkaldtq dqwpakrprl
      361 lesesrpgpa frgshqdkas sssldidtev gspeddtdyp rsptf
//
LOCUS       NP_598232                669 aa            linear   ROD 27-APR-2025
DEFINITION  hepatoma-derived growth factor-related protein 2 [Rattus
            norvegicus].
ACCESSION   NP_598232
VERSION     NP_598232.1
DBSOURCE    REFSEQ: accession NM_133548.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Zhuang,Z., Mei,G., Liu,W., Chen,Y., Zeng,J., Zhang,W., Yao,G. and
            Wang,X.
  TITLE     Hepatoma-derived growth factor-2 is highly expressed during
            development and in spinal cord injury
  JOURNAL   Mol Med Rep 12 (4), 6140-6144 (2015)
   PUBMED   26252862
  REMARK    GeneRIF: HDGF-2 expression was significantly upregulated in the
            embryonic spinal cord and injured spinal cord.
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Gao,K., Xu,C., Jin,X., Wumaier,R., Ma,J., Peng,J., Wang,Y.,
            Tang,Y., Yu,L. and Zhang,P.
  TITLE     HDGF-related protein-2 (HRP-2) acts as an oncogene to promote cell
            growth in hepatocellular carcinoma
  JOURNAL   Biochem Biophys Res Commun 458 (4), 849-855 (2015)
   PUBMED   25689719
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Thakar,K., Votteler,I., Kelkar,D., Shidore,T., Gupta,S., Kelm,S.
            and Dietz,F.
  TITLE     Interaction of HRP-2 isoforms with HDGF: chromatin binding of a
            specific heteromer
  JOURNAL   FEBS J 279 (5), 737-751 (2012)
   PUBMED   22212508
REFERENCE   4  (residues 1 to 669)
  AUTHORS   El-Tahir,H.M., Dietz,F., Dringen,R., Schwabe,K., Strenge,K.,
            Kelm,S., Abouzied,M.M., Gieselmann,V. and Franken,S.
  TITLE     Expression of hepatoma-derived growth factor family members in the
            adult central nervous system
  JOURNAL   BMC Neurosci 7, 6 (2006)
   PUBMED   16430771
  REMARK    GeneRIF: HRP-2 was strongly expressed in neurons, astrocytes and
            oligodendrocytes in the thalamus, prefrontal and parietal cortex,
            neurohypophysis, and the cerebellum.
            Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF355102.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF355102.1, BC071178.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..669
                     /product="hepatoma-derived growth factor-related protein
                     2"
                     /note="HRP-2; hepatoma-derived growth factor 3; HDGF-3"
                     /calculated_mol_wt=73871
     Region          5..88
                     /region_name="PWWP_HDGFL2"
                     /note="PWWP domain found in Hepatoma-derived growth
                     factor-related protein 2 (HDGFL2); cd20149"
                     /db_xref="CDD:438977"
     Site            order(14,16..17,19,72,74)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438977"
     Site            order(18,21,44)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438977"
     Site            19..22
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438977"
     Region          92..469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Region          466..548
                     /region_name="Interaction with DPF3/BAF45C isoform 2.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925G1.2)"
     Region          468..565
                     /region_name="LEDGF"
                     /note="Lens epithelium-derived growth factor (LEDGF);
                     pfam11467"
                     /db_xref="CDD:463284"
     Region          558..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z4V5; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMU9; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMU9; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMU9; propagated from
                     UniProtKB/Swiss-Prot (Q925G1.2)"
     CDS             1..669
                     /gene="Hdgfl2"
                     /gene_synonym="Hdgf2; Hdgfrp2"
                     /coded_by="NM_133548.1:5..2014"
                     /db_xref="GeneID:171073"
                     /db_xref="RGD:621013"
ORIGIN      
        1 mphafkpgdl vfakmkgyph wpariddiad gavkpppnky pifffgthet aflgpkdlfp
       61 ydkckdkygk pnkrkgfneg lweiqnnpha sysaplpvss sdseapeadl gggsdadkek
      121 earrvmtvta vtttatsgrt esdsdsdkns dhsglkrktp vlkmsvskra rkassdldqa
      181 svspseedse spsesektsd qdftpekkti araprraplg grkkkkvpsa sdsdsradsd
      241 gakeepvvta qpspssasss ssssasdsdv sikkpprgrk paekpppkpr grrskperpp
      301 stsssdsdsd sgevdrisew krrdeerrre learrrreqe eelrrlreqe reekerrker
      361 aerggssgee ledeepvkkr srkargrgtp sssdsepege lgkegkklak ksqlqgsesa
      421 rkpgqkekrg rpdekprarp vkvertrkrs eglsldrkge kkkepsveer lqklhseikf
      481 alkvdnpdvr rclsaleelg tlqvtsqilq kntdvvatlk kirrykankd vmakaaevyt
      541 rlksrvlgpk vealqkvnka gaekeradge kveeqpgeqa prelaedeps tdrsapvnge
      601 aasqkgente dgaqedgqdl edgprggsse elhdspqdss dparpgnehq dhermqlase
      661 saddddeds
//
LOCUS       NP_001099908              93 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A5 [Rattus norvegicus].
ACCESSION   NP_001099908 XP_001075383 XP_215608
VERSION     NP_001099908.1
DBSOURCE    REFSEQ: accession NM_001106438.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Tadenev,A.L., Kulaga,H.M., May-Simera,H.L., Kelley,M.W.,
            Katsanis,N. and Reed,R.R.
  TITLE     Loss of Bardet-Biedl syndrome protein-8 (BBS8) perturbs olfactory
            function, protein localization, and axon targeting
  JOURNAL   Proc Natl Acad Sci U S A 108 (25), 10320-10325 (2011)
   PUBMED   21646512
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Bertini,I., Das Gupta,S., Hu,X., Karavelas,T., Luchinat,C.,
            Parigi,G. and Yuan,J.
  TITLE     Solution structure and dynamics of S100A5 in the apo and Ca2+-bound
            states
  JOURNAL   J Biol Inorg Chem 14 (7), 1097-1107 (2009)
   PUBMED   19536568
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Hsieh,H.L., Schafer,B.W., Cox,J.A. and Heizmann,C.W.
  TITLE     S100A13 and S100A6 exhibit distinct translocation pathways in
            endothelial cells
  JOURNAL   J Cell Sci 115 (Pt 15), 3149-3158 (2002)
   PUBMED   12118070
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Schafer,B.W., Fritschy,J.M., Murmann,P., Troxler,H., Durussel,I.,
            Heizmann,C.W. and Cox,J.A.
  TITLE     Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding
            protein of the EF-hand superfamily
  JOURNAL   J Biol Chem 275 (39), 30623-30630 (2000)
   PUBMED   10882717
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473976.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215608.3, XP_001075383.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BF548433.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..93
                     /product="protein S100-A5"
                     /calculated_mol_wt=10681
     Region          3..88
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(3..20,26..28,37..38,40..42,68..71,73..74,76..79,
                     81..88)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(20,25,28,33..34,61,63,65,67,69,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     CDS             1..93
                     /gene="S100a5"
                     /coded_by="NM_001106438.1:33..314"
                     /db_xref="GeneID:295211"
                     /db_xref="RGD:1308996"
ORIGIN      
        1 metplekalt tmvttfhkys gregskltls rkelkelikt elslaekmke ssidnlmksl
       61 dknsdqeidf keysvflttl cmayndffle dnk
//
LOCUS       NP_970617                216 aa            linear   ROD 27-APR-2025
DEFINITION  sperm microtubule inner protein 8 [Rattus norvegicus].
ACCESSION   NP_970617 XP_214634
VERSION     NP_970617.1
DBSOURCE    REFSEQ: accession NM_201655.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Bera,T.K., Hahn,Y., Lee,B. and Pastan,I.H.
  TITLE     TEPP, a new gene specifically expressed in testis, prostate, and
            placenta and well conserved in chordates
  JOURNAL   Biochem Biophys Res Commun 312 (4), 1209-1215 (2003)
   PUBMED   14652002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BK001512.1.
            
            On Mar 22, 2004 this sequence version replaced XP_214634.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001512.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..216
                     /product="sperm microtubule inner protein 8"
                     /note="testis, prostate and placenta-expressed protein;
                     testis/prostate/placenta-expressed protein; testis,
                     prostate and placenta expressed"
                     /calculated_mol_wt=24934
     CDS             1..216
                     /gene="Spmip8"
                     /gene_synonym="Tepp"
                     /coded_by="NM_201655.1:185..835"
                     /db_xref="GeneID:291850"
                     /db_xref="RGD:735198"
ORIGIN      
        1 mariidlvpw decsahlyas pailiplerv rrplagvkhq lyhpglpslr rmdmdsvkgc
       61 lsdehcqsst yytkddfnea hftllgvpnk plhcldftat gqklchkyrd gkmipivpgi
      121 qradwpcftr aiedwsqfvs ksgefklpca nrrvegfsgy avrylkpelt qnwryclnqn
      181 psldrygqkp lpfntlnsfr rfgshysrin yltpwh
//
LOCUS       NP_001014213             291 aa            linear   ROD 27-APR-2025
DEFINITION  trimeric intracellular cation channel type B [Rattus norvegicus].
ACCESSION   NP_001014213 XP_342840
VERSION     NP_001014213.1
DBSOURCE    REFSEQ: accession NM_001014191.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Zhao,C., Ichimura,A., Qian,N., Iida,T., Yamazaki,D., Noma,N.,
            Asagiri,M., Yamamoto,K., Komazaki,S., Sato,C., Aoyama,F.,
            Sawaguchi,A., Kakizawa,S., Nishi,M. and Takeshima,H.
  TITLE     Mice lacking the intracellular cation channel TRIC-B have
            compromised collagen production and impaired bone mineralization
  JOURNAL   Sci Signal 9 (428), ra49 (2016)
   PUBMED   27188440
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Yamazaki,D., Komazaki,S., Nakanishi,H., Mishima,A., Nishi,M.,
            Yazawa,M., Yamazaki,T., Taguchi,R. and Takeshima,H.
  TITLE     Essential role of the TRIC-B channel in Ca2+ handling of alveolar
            epithelial cells and in perinatal lung maturation
  JOURNAL   Development 136 (14), 2355-2361 (2009)
   PUBMED   19515693
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Yazawa,M., Ferrante,C., Feng,J., Mio,K., Ogura,T., Zhang,M.,
            Lin,P.H., Pan,Z., Komazaki,S., Kato,K., Nishi,M., Zhao,X.,
            Weisleder,N., Sato,C., Ma,J. and Takeshima,H.
  TITLE     TRIC channels are essential for Ca2+ handling in intracellular
            stores
  JOURNAL   Nature 448 (7149), 78-82 (2007)
   PUBMED   17611541
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079336.1.
            
            On Apr 1, 2005 this sequence version replaced XP_342840.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079336.1, FQ229075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..291
                     /product="trimeric intracellular cation channel type B"
                     /note="TRICB; TRIC-B"
                     /calculated_mol_wt=32314
     Site            17..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Region          39..222
                     /region_name="TRIC"
                     /note="TRIC channel; pfam05197"
                     /db_xref="CDD:461583"
     Site            48..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Site            81..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Site            104..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Site            139..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Site            180..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Site            207..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     Region          254..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV1.1)"
     CDS             1..291
                     /gene="Tmem38b"
                     /gene_synonym="RGD1305703"
                     /coded_by="NM_001014191.1:29..904"
                     /db_xref="GeneID:362521"
                     /db_xref="RGD:1305703"
ORIGIN      
        1 meypwddltl afsrtsmfpf fdiahylvsv malkqrpgav aaawsnplss wlsamlhcfg
       61 ggilscilla epplkfltnh tnillassiw yivffcprdl vsqgysyqpi qllaagmkev
      121 trtwkivggv ahangyyrng wivmiavgwa rgaggaiita ceqllkgdwk pegdewlkms
      181 fpckvtllgs imftfqhtrh laiskhdlmf lytiflvtik vtmmmtkdaa vtltpfedtl
      241 trmlfgrqqq qfslsekkae vkpssngsas saskrgtepp ssakrhakke d
//
LOCUS       NP_001029310             597 aa            linear   ROD 27-APR-2025
DEFINITION  protein Spindly [Rattus norvegicus].
ACCESSION   NP_001029310 XP_220305
VERSION     NP_001029310.1
DBSOURCE    REFSEQ: accession NM_001034138.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Chan,Y.W., Fava,L.L., Uldschmid,A., Schmitz,M.H., Gerlich,D.W.,
            Nigg,E.A. and Santamaria,A.
  TITLE     Mitotic control of kinetochore-associated dynein and spindle
            orientation by human Spindly
  JOURNAL   J Cell Biol 185 (5), 859-874 (2009)
   PUBMED   19468067
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105812.1.
            
            On Oct 14, 2005 this sequence version replaced XP_220305.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105812.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..597
                     /product="protein Spindly"
                     /note="coiled-coil domain containing 99; coiled-coil
                     domain-containing protein 99; spindle apparatus
                     coiled-coil domain-containing protein 1"
                     /calculated_mol_wt=68981
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96EA4; propagated from
                     UniProtKB/Swiss-Prot (Q3KR99.1)"
     Region          <2..>277
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EA4; propagated from
                     UniProtKB/Swiss-Prot (Q3KR99.1)"
     Region          531..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR99.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923A2; propagated from
                     UniProtKB/Swiss-Prot (Q3KR99.1)"
     CDS             1..597
                     /gene="Spdl1"
                     /gene_synonym="Ccdc99; RGD1306908"
                     /coded_by="NM_001034138.1:145..1938"
                     /db_xref="GeneID:303037"
                     /db_xref="RGD:1306908"
ORIGIN      
        1 meaditnlrn klkecederl kaaqyglqll erqtelqsql dkcheemmtt aenynqekya
       61 lqrevelksr mleslscece alrqqqkaql eqlemqlhrs hrqevhglrn klenlkveld
      121 earlsekqlk qkldhqgell shkseelrll seqralssvs sellslqtel teaegvknal
      181 reevnelqck qeqleclnas llhqvdrlke ekeerekeav syynalekar venqdlqvql
      241 ghalqqaadp nskgnslfae vedrrvamer rlnlmkdkyq slkkqnaftr dqmnkmklqi
      301 stllrmrgsq tefeqqerlf amleqkngei khllgeinkl ekfknlyenm esksstsdsa
      361 caledstyyt dllqlkldkl nkenestkge lsiqrmkalf esqrtldier klfanerhlq
      421 lsesenlklr akldelklky epeerievpv lkrrrevlpl nintpeetaa asatgedvsr
      481 lplerkeesc ldnlkdntvq wkqpaslsph kslpldtqpk kekcvtlvas pastevlheq
      541 sgntpssprl teesrlptkv kerkeatskl ekgaskksht imyvsskstp emqcpqq
//
LOCUS       NP_001030131             187 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome b-245 chaperone 1 [Rattus norvegicus].
ACCESSION   NP_001030131
VERSION     NP_001030131.1
DBSOURCE    REFSEQ: accession NM_001034959.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Thomas,D.C., Clare,S., Sowerby,J.M., Pardo,M., Juss,J.K.,
            Goulding,D.A., van der Weyden,L., Storisteanu,D., Prakash,A.,
            Espeli,M., Flint,S., Lee,J.C., Hoenderdos,K., Kane,L., Harcourt,K.,
            Mukhopadhyay,S., Umrania,Y., Antrobus,R., Nathan,J.A., Adams,D.J.,
            Bateman,A., Choudhary,J.S., Lyons,P.A., Condliffe,A.M.,
            Chilvers,E.R., Dougan,G. and Smith,K.G.
  TITLE     Eros is a novel transmembrane protein that controls the phagocyte
            respiratory burst and is essential for innate immunity
  JOURNAL   J Exp Med 214 (4), 1111-1128 (2017)
   PUBMED   28351984
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079126.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079126.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..187
                     /product="cytochrome b-245 chaperone 1"
                     /note="uncharacterized protein C17orf62 homolog; eros;
                     essential for reactive oxygen species protein"
                     /calculated_mol_wt=20763
     Region          2..183
                     /region_name="Cybc1_Eros"
                     /note="Cytochrome b-245 chaperone 1 / Eros; pfam15169"
                     /db_xref="CDD:405793"
     Site            20..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYA6.1)"
     Region          167..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYA6.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA6.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA6.1)"
     CDS             1..187
                     /gene="Cybc1"
                     /coded_by="NM_001034959.1:281..844"
                     /db_xref="GeneID:619574"
                     /db_xref="RGD:1562022"
ORIGIN      
        1 mymqvetrts trlhlkrapg irswsllvgi lstglaaayy sgdslgwklf yvtgclfvav
       61 qnledweeai fnkstgkvil ktfslykkll tllraghdqv vvllkdiqdv nveeekvryf
      121 gkgymvvlrf atgfshpltq savmgrrsdv eaiaklitsf lelhrlesps ersqssdsep
      181 dgpggqs
//
LOCUS       NP_036771                648 aa            linear   ROD 27-APR-2025
DEFINITION  RAF proto-oncogene serine/threonine-protein kinase [Rattus
            norvegicus].
ACCESSION   NP_036771 XP_003749868
VERSION     NP_036771.1
DBSOURCE    REFSEQ: accession NM_012639.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Yu,W., Zheng,Z., Wei,W., Li,L., Zhang,Y., Sun,Y., Cao,J., Zang,W.
            and Shao,J.
  TITLE     Raf1 interacts with OIP5 to participate in oxaliplatin-induced
            neuropathic pain
  JOURNAL   Life Sci 281, 119804 (2021)
   PUBMED   34229010
  REMARK    GeneRIF: Raf1 interacts with OIP5 to participate in
            oxaliplatin-induced neuropathic pain.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Chen,S., Tang,C., Ding,H., Wang,Z., Liu,X., Chai,Y., Jiang,W.,
            Han,Y. and Zeng,H.
  TITLE     Maf1 Ameliorates Sepsis-Associated Encephalopathy by Suppressing
            the NF-kB/NLRP3 Inflammasome Signaling Pathway
  JOURNAL   Front Immunol 11, 594071 (2020)
   PUBMED   33424842
  REMARK    GeneRIF: Maf1 Ameliorates Sepsis-Associated Encephalopathy by
            Suppressing the NF-kB/NLRP3 Inflammasome Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Feng,D., Sheng-Dong,L., Tong,W. and Zhen-Xian,D.
  TITLE     O-GlcNAcylation of RAF1 increases its stabilization and induces the
            renal fibrosis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (3), 165556 (2020)
   PUBMED   31521821
  REMARK    GeneRIF: O-GlcNAcylation suppressed the ubiquitination of RAF1.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Kamemura,N., Murakami,S., Komatsu,H., Sawanoi,M., Miyamoto,K.,
            Ishidoh,K., Kishimoto,K., Tsuji,A. and Yuasa,K.
  TITLE     Type II cGMP-dependent protein kinase negatively regulates
            fibroblast growth factor signaling by phosphorylating Raf-1 at
            serine 43 in rat chondrosarcoma cells
  JOURNAL   Biochem Biophys Res Commun 483 (1), 82-87 (2017)
   PUBMED   28057484
  REMARK    GeneRIF: Wild-type PKGII phosphorylated Raf-1 at Ser-43 in a
            cGMP-dependent manner, but a PKGII D412A/R415A mutant, which has a
            low affinity for cGMP, did not.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Zhang,J., Xu,X., Zhou,D., Li,H., You,W., Wang,Z. and Chen,G.
  TITLE     Possible Role of Raf-1 Kinase in the Development of Cerebral
            Vasospasm and Early Brain Injury After Experimental Subarachnoid
            Hemorrhage in Rats
  JOURNAL   Mol Neurobiol 52 (3), 1527-1539 (2015)
   PUBMED   25367879
  REMARK    GeneRIF: Raf-1 kinase contributes to cerebral vasospasm and early
            brain injury after subarachnoid hemorrhage by enhancing the
            activation of the Raf-1/ERK1/2 and Raf-1/NF-kappaB signaling
            pathways.
            Erratum:[Mol Neurobiol. 2024 Oct;61(10):8490. doi:
            10.1007/s12035-024-04153-0. PMID: 38625621]
REFERENCE   6  (residues 1 to 648)
  AUTHORS   York,R.D., Yao,H., Dillon,T., Ellig,C.L., Eckert,S.P.,
            McCleskey,E.W. and Stork,P.J.
  TITLE     Rap1 mediates sustained MAP kinase activation induced by nerve
            growth factor
  JOURNAL   Nature 392 (6676), 622-626 (1998)
   PUBMED   9560161
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Seko,Y., Tobe,K., Ueki,K., Kadowaki,T. and Yazaki,Y.
  TITLE     Hypoxia and hypoxia/reoxygenation activate Raf-1, mitogen-activated
            protein kinase kinase, mitogen-activated protein kinases, and S6
            kinase in cultured rat cardiac myocytes
  JOURNAL   Circ Res 78 (1), 82-90 (1996)
   PUBMED   8603510
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Silverman,J.A., Kuhlmann,E.T., Zurlo,J., Yager,J.D. and
            Longnecker,D.S.
  TITLE     Expression of c-myc, c-raf-1, and c-Ki-ras in azaserine-induced
            pancreatic carcinomas and growing pancreas in rats
  JOURNAL   Mol Carcinog 3 (6), 379-386 (1990)
   PUBMED   2278633
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Ishikawa,F., Takaku,F., Nagao,M. and Sugimura,T.
  TITLE     Rat c-raf oncogene activation by a rearrangement that produces a
            fused protein
  JOURNAL   Mol Cell Biol 7 (3), 1226-1232 (1987)
   PUBMED   3550433
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Williams,A.F., Barclay,A.N., Letarte-Muirhead,M. and Morris,R.J.
  TITLE     Rat thy-1 antigens from thymus and brain: their tissue
            distribution, purification, and chemical composition
  JOURNAL   Cold Spring Harb Symp Quant Biol 41 Pt 1, 51-61 (1977)
   PUBMED   70317
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062071.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003749868.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062071.1, SRR8487231.90257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..648
                     /product="RAF proto-oncogene serine/threonine-protein
                     kinase"
                     /EC_number="2.7.11.1"
                     /note="murine leukemia viral (v-raf-1) oncogene homolog 1
                     (3611-MSV); cRaf; C-RAF; proto-oncogene c-RAF; v-raf-1
                     murine leukemia viral oncogene homolog 1; v-raf-leukemia
                     viral oncogene 1"
                     /calculated_mol_wt=72797
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q99N57; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Region          55..131
                     /region_name="RBD_CRAF"
                     /note="Ras-binding domain (RBD) found in RAF
                     proto-oncogene serine/threonine-protein kinase RAF1/CRAF;
                     cd17135"
                     /db_xref="CDD:340655"
     Site            order(57,59,64..69,71,84,88..90)
                     /site_type="other"
                     /note="RBD_Raf-Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340655"
     Site            order(57,64,66..69,84,87..90)
                     /site_type="other"
                     /note="putative RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340655"
     Site            125
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:340655"
     Region          136..187
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Region          217..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11345.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q99N57; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Region          331..349
                     /region_name="Interaction with PEBP1/RKIP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11345.1)"
     Region          336..618
                     /region_name="STKc_C-Raf"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; cd14149"
                     /db_xref="CDD:271051"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1, PAK2, PAK3 and PAK5.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1, PAK2 and PAK3.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            order(340,342,367,369..370,397..403,407..409,454,457..458,
                     461..462,478,480,607)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271051"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            order(355..359,363,373,375,406,421..424,428,430,468,470,
                     472..473,475,486,489,507..510)
                     /site_type="active"
                     /db_xref="CDD:271051"
     Site            order(355..359,363,373,375,406,421..424,428,468,470,
                     472..473,475,486)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271051"
     Site            order(359,428,430,468,470,472,489,507..510)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271051"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            485..510
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271051"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            563
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P04049; propagated from
                     UniProtKB/Swiss-Prot (P11345.1)"
     CDS             1..648
                     /gene="Raf1"
                     /coded_by="NM_012639.2:297..2243"
                     /db_xref="GeneID:24703"
                     /db_xref="RGD:3531"
ORIGIN      
        1 mehiqgawkt isngfglkda vfdgsscisp tivqqfgyqr rasddgkltd ssktsntirv
       61 flpnkqrtvv nvrngmslhd clmkalkvrg lqpeccavfr llqehkgkka rldwntdaas
      121 ligeelqvdf ldhvpltthn farktflkla fcdicqkfll ngfrcqtcgy kfhehcstkv
      181 ptmcvdwsni rqlllfpnst asdsgvpapp sftmrrmres vsrmpassqh rystphaftf
      241 ntsspssegs lsqrqrstst pnvhmvsttl pvdsrmieda irshsesasp salssspnnl
      301 sptgwsqpkt pvpaqrerap gsgtqeknki rprgqrdssy yweieasevm lstrigsgsf
      361 gtvykgkwhg dvavkilkvv dptpeqlqaf rnevavlrkt rhvnillfmg ymtkdnlaiv
      421 tqwcegssly khlhvqetkf qmfqlidiar qtaqgmdylh akniihrdmk snniflhegl
      481 tvkigdfgla tvksrwsgsq qveqptgsvl wmapevirmq dnnpfsfqsd vysygivlye
      541 lmtgelpysh innrdqiifm vgrgyaspdl srlykncpka mkrlvadcvk kvkeerplfp
      601 qilssiellq hslpkinrsa sepslhraah tedinactlt tsprlpvf
//
LOCUS       NP_001017378             458 aa            linear   ROD 27-APR-2025
DEFINITION  histone acetyltransferase KAT8 [Rattus norvegicus].
ACCESSION   NP_001017378 XP_226893
VERSION     NP_001017378.1
DBSOURCE    REFSEQ: accession NM_001017378.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Li,L., Ghorbani,M., Weisz-Hubshman,M., Rousseau,J., Thiffault,I.,
            Schnur,R.E., Breen,C., Oegema,R., Weiss,M.M., Waisfisz,Q.,
            Welner,S., Kingston,H., Hills,J.A., Boon,E.M., Basel-Salmon,L.,
            Konen,O., Goldberg-Stern,H., Bazak,L., Tzur,S., Jin,J., Bi,X.,
            Bruccoleri,M., McWalter,K., Cho,M.T., Scarano,M., Schaefer,G.B.,
            Brooks,S.S., Hughes,S.S., van Gassen,K.L.I., van Hagen,J.M.,
            Pandita,T.K., Agrawal,P.B., Campeau,P.M. and Yang,X.J.
  TITLE     Lysine acetyltransferase 8 is involved in cerebral development and
            syndromic intellectual disability
  JOURNAL   J Clin Invest 130 (3), 1431-1445 (2020)
   PUBMED   31794431
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Qiao,W., Zhang,W., Gai,Y., Zhao,L. and Fan,J.
  TITLE     The histone acetyltransferase MOF overexpression blunts cardiac
            hypertrophy by targeting ROS in mice
  JOURNAL   Biochem Biophys Res Commun 448 (4), 379-384 (2014)
   PUBMED   24802406
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Fullgrabe,J., Lynch-Day,M.A., Heldring,N., Li,W., Struijk,R.B.,
            Ma,Q., Hermanson,O., Rosenfeld,M.G., Klionsky,D.J. and Joseph,B.
  TITLE     The histone H4 lysine 16 acetyltransferase hMOF regulates the
            outcome of autophagy
  JOURNAL   Nature 500 (7463), 468-471 (2013)
   PUBMED   23863932
  REMARK    Erratum:[Nature. 2017 Mar 30;543(7647):742. doi:
            10.1038/nature22027. PMID: 28297710]
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Wang,Y., Zhang,R., Wu,D., Lu,Z., Sun,W., Cai,Y., Wang,C. and Jin,J.
  TITLE     Epigenetic change in kidney tumor: downregulation of histone
            acetyltransferase MYST1 in human renal cell carcinoma
  JOURNAL   J Exp Clin Cancer Res 32 (1), 8 (2013)
   PUBMED   23394073
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Patani,N., Jiang,W.G., Newbold,R.F. and Mokbel,K.
  TITLE     Histone-modifier gene expression profiles are associated with
            pathological and clinical outcomes in human breast cancer
  JOURNAL   Anticancer Res 31 (12), 4115-4125 (2011)
   PUBMED   22199269
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Kruse,J.P. and Gu,W.
  TITLE     Modes of p53 regulation
  JOURNAL   Cell 137 (4), 609-622 (2009)
   PUBMED   19450511
  REMARK    Review article
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Pelletier,N., Champagne,N., Stifani,S. and Yang,X.J.
  TITLE     MOZ and MORF histone acetyltransferases interact with the
            Runt-domain transcription factor Runx2
  JOURNAL   Oncogene 21 (17), 2729-2740 (2002)
   PUBMED   11965546
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Kitabayashi,I., Aikawa,Y., Nguyen,L.A., Yokoyama,A. and Ohki,M.
  TITLE     Activation of AML1-mediated transcription by MOZ and inhibition by
            the MOZ-CBP fusion protein
  JOURNAL   EMBO J 20 (24), 7184-7196 (2001)
   PUBMED   11742995
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083891.1.
            
            On Apr 22, 2005 this sequence version replaced XP_226893.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083891.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..458
                     /product="histone acetyltransferase KAT8"
                     /EC_number="2.3.1.48"
                     /note="probable histone acetyltransferase MYST1; MYST
                     protein 1; MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1; K
                     (lysine) acetyltransferase 8; MYST-1; MYST histone
                     acetyltransferase 1; protein acetyltransferase KAT8;
                     protein propionyltransferase KAT8"
                     /calculated_mol_wt=52501
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI06.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     Region          21..449
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     Site            113
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     Region          140..149
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI06.1)"
     Region          174..458
                     /region_name="Sufficient for interaction with KANSL1.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI06.1)"
     Site            274
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H7Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5XI06.1)"
     CDS             1..458
                     /gene="Kat8"
                     /gene_synonym="Myst1"
                     /coded_by="NM_001017378.1:6..1382"
                     /db_xref="GeneID:310194"
                     /db_xref="RGD:1311512"
ORIGIN      
        1 maaqgataav aattsgivge gepgpgents vegparspgr vspptparge pevtveiget
       61 ylcrrpdstw hsaeviqsrv ndqegreefy vhyvgfnrrl dewvdknrla ltktvkdavq
      121 knsekylsel aeqperkitr nqkrkhdein hvqktyaemd pttaalekeh eaitkvkyvd
      181 kihignyeid awyfspfped ygkqpklwlc eyclkymkfe ksyrfhlgqc qwrqppgkei
      241 yrksnisvye vdgkdhkiyc qnlcllaklf ldhktlyfdv epfvfyilte vdrqgahivg
      301 yfskekespd gnnvaciltl ppyqrrgygk fliafsyels klestvgspe kplsdlgkls
      361 yrsywswvll eilrdfrgtl sikdlsqmts itqndiistl qslnmvkywk gqhvicvtpk
      421 lveehlksaq ykkppitvds vclkwappkh kqvklskk
//
LOCUS       NP_001004228             250 aa            linear   ROD 27-APR-2025
DEFINITION  endomucin precursor [Rattus norvegicus].
ACCESSION   NP_001004228 XP_215710
VERSION     NP_001004228.1
DBSOURCE    REFSEQ: accession NM_001004228.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shuwen,H., Xi,Y., Miao,D., Jiamin,X., Jing,Z. and Weili,G.
  TITLE     Nine Genes Mediate the Therapeutic Effects of Iodine-131
            Radiotherapy in Thyroid Carcinoma Patients
  JOURNAL   Dis Markers 2020, 9369341 (2020)
   PUBMED   32626543
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Morgan,S.M., Samulowitz,U., Darley,L., Simmons,D.L. and
            Vestweber,D.
  TITLE     Biochemical characterization and molecular cloning of a novel
            endothelial-specific sialomucin
  JOURNAL   Blood 93 (1), 165-175 (1999)
   PUBMED   9864158
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079155.1.
            
            On Sep 10, 2004 this sequence version replaced XP_215710.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079155.1, EV765755.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q43"
     Protein         1..250
                     /product="endomucin precursor"
                     /note="sialomucin"
                     /calculated_mol_wt=24251
     Region          1..250
                     /region_name="Endomucin"
                     /note="pfam07010"
                     /db_xref="CDD:429246"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2283
     mat_peptide     21..250
                     /product="Endomucin. /id=PRO_0000249727"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY82.1)"
                     /calculated_mol_wt=24251
     Region          24..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY82.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY82.1)"
     Region          105..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY82.1)"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY82.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY82.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY82.1)"
     Region          210..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY82.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0H2; propagated from
                     UniProtKB/Swiss-Prot (Q6AY82.1)"
     CDS             1..250
                     /gene="Emcn"
                     /coded_by="NM_001004228.1:92..844"
                     /db_xref="GeneID:295490"
                     /db_xref="RGD:1303218"
ORIGIN      
        1 mrllqvtalf fllsnslcrg enskaltets ttkasattpd mvsitnkstg gtppkgttns
       61 atpktplmpa ldspttpkhe tttrgvikne vstikttvan ptisnavstl sspqnktenq
      121 ssirtteisg tnqlpddqkp kttetpsasl ttaktisqiq dtedgkitat tsttpsyssv
      181 ilpvvialiv itvlvftlvg lyricwkrdp gtpesgndqp qsdkesvkll tvktishesg
      241 ehsaqgkakn
//
LOCUS       NP_001029242             284 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.7cy [Rattus norvegicus].
ACCESSION   NP_001029242
VERSION     NP_001029242.1
DBSOURCE    REFSEQ: accession NM_001034070.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB787774.1, CK483405.1,
            M60667.1 and BC078780.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.7, also known as variant 3)
            has multiple differences in the coding region, compared to variant
            1, resulting in a shorter protein (isoform Tpm1.7cy, also referred
            to as TM-3). Isoform Tpm1.7cy is the same length as isoforms
            Tpm1.6cy and Tpm1.3sm but is the product of alternate splicing and
            contains short regions of sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60667.1, SRR8487230.79325.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111, SAMN12840127
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.7cy"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32717
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034070.1:107..961"
                     /note="isoform Tpm1.7cy is encoded by transcript variant
                     Tpm1.7"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddleekv ahakeenlsm hqmldqtlle lnnm
//
LOCUS       NP_077062                317 aa            linear   ROD 27-APR-2025
DEFINITION  DNA repair nuclease/redox regulator APEX1 [Rattus norvegicus].
ACCESSION   NP_077062
VERSION     NP_077062.1
DBSOURCE    REFSEQ: accession NM_024148.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Fan,J., Liu,M., Li,X., Gao,S., Wang,Y., Li,A., Chen,L., Zhou,D.,
            Chen,H., Xu,Z., Wu,Z. and Wu,K.
  TITLE     Apurinic/apyrimidinic endonuclease 1 regulates palmitic
            acid-mediated apoptosis in cardiomyocytes via endoplasmic reticulum
            stress
  JOURNAL   Biochem Biophys Res Commun 650, 123-131 (2023)
   PUBMED   36791545
  REMARK    GeneRIF: Apurinic/apyrimidinic endonuclease 1 regulates palmitic
            acid-mediated apoptosis in cardiomyocytes via endoplasmic reticulum
            stress.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Sadek,K., Abouzed,T., Nasr,S. and Shoukry,M.
  TITLE     Licochalcone B Ameliorates Liver Cancer via Targeting of Apoptotic
            Genes, DNA Repair Systems, and Cell Cycle Control
  JOURNAL   Iran J Pharm Res 19 (4), 372-386 (2020)
   PUBMED   33841550
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Tang,W., Lin,D., Chen,M., Li,Z., Zhang,W., Hu,W. and Li,F.
  TITLE     PTEN-mediated mitophagy and APE1 overexpression protects against
            cardiac hypoxia/reoxygenation injury
  JOURNAL   In Vitro Cell Dev Biol Anim 55 (9), 741-748 (2019)
   PUBMED   31432320
  REMARK    GeneRIF: Our findings provide an insight into the PTEN and APE1
            overexpression protects against cardiac hypoxia/reoxygenation
            injury, which may be through inducing the PINK1/Parkin-mediated
            mitophagy.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Zaky,A., Bouali-Benazzouz,R., Favereaux,A., Tell,G. and Landry,M.
  TITLE     APE1/Ref-1 redox function contributes to inflammatory pain
            sensitization
  JOURNAL   Exp Neurol 307, 1-11 (2018)
   PUBMED   29772245
  REMARK    GeneRIF: Changes in APE1 expression and sub-cellular distribution
            are implicated in inflammatory pain mechanisms mediated by APE1
            redox functions.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Fehrenbacher,J.C., Guo,C., Kelley,M.R. and Vasko,M.R.
  TITLE     DNA damage mediates changes in neuronal sensitivity induced by the
            inflammatory mediators, MCP-1 and LPS, and can be reversed by
            enhancing the DNA repair function of APE1
  JOURNAL   Neuroscience 366, 23-35 (2017)
   PUBMED   28965839
  REMARK    GeneRIF: Study shows that genetically enhancing
            apurinic/apyrimidinic endonuclease expression or treatment with the
            small molecule, E3330, increases DNA repair.
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Walton,M., Lawlor,P., Sirimanne,E., Williams,C., Gluckman,P. and
            Dragunow,M.
  TITLE     Loss of Ref-1 protein expression precedes DNA fragmentation in
            apoptotic neurons
  JOURNAL   Brain Res Mol Brain Res 44 (1), 167-170 (1997)
   PUBMED   9030714
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Yacoub,A., Kelley,M.R. and Deutsch,W.A.
  TITLE     Drosophila ribosomal protein PO contains apurinic/apyrimidinic
            endonuclease activity
  JOURNAL   Nucleic Acids Res 24 (21), 4298-4303 (1996)
   PUBMED   8932386
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Tan,Y., Nakagawa,Y., Akiyama,K., Wakabayashi,H., Sarker,A.H. and
            Seki,S.
  TITLE     cDNA cloning of rat major AP endonuclease (APEX nuclease) and
            analyses of its mRNA expression in rat tissues
  JOURNAL   Acta Med Okayama 50 (1), 53-60 (1996)
   PUBMED   8701782
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Akiyama,K., Seki,S., Oshida,T. and Yoshida,M.C.
  TITLE     Structure, promoter analysis and chromosomal assignment of the
            human APEX gene
  JOURNAL   Biochim Biophys Acta 1219 (1), 15-25 (1994)
   PUBMED   8086453
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Wilson,T.M., Carney,J.P. and Kelley,M.R.
  TITLE     Cloning of the multifunctional rat apurinic/apyrimidinic
            endonuclease (rAPEN)/redox factor from an immature T cell line
  JOURNAL   Nucleic Acids Res 22 (3), 530-531 (1994)
   PUBMED   7510394
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D44495.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D44495.1, BC078816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..317
                     /product="DNA repair nuclease/redox regulator APEX1"
                     /EC_number="3.1.11.2"
                     /note="apurinic/apyrimidinic endonuclease 1; APEX nuclease
                     1; DNA-(apurinic or apyrimidinic site) lyase; APEN; AP
                     endonuclease 1; DNA-(apurinic or apyrimidinic site)
                     endonuclease; redox factor-1; APEX nuclease
                     (multifunctional DNA repair enzyme) 1"
                     /calculated_mol_wt=35407
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Region          1..32
                     /region_name="Necessary for interaction with YBX1, binding
                     to RNA, association together with NPM1 to rRNA,
                     endoribonuclease activity on abasic RNA and localization
                     in the nucleoli. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Region          8..12
                     /region_name="Nuclear localization signal (NLS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Region          22..32
                     /region_name="Necessary for interaction with NPM1 and for
                     efficient rRNA binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            26
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            30..31
                     /site_type="cleavage"
                     /note="Cleavage, by granzyme A. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            31
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Region          61..315
                     /region_name="Ape1-like_AP-endo"
                     /note="Human Ape1-like subfamily of the ExoIII family
                     apurinic/apyrimidinic (AP) endonucleases; cd09087"
                     /db_xref="CDD:197321"
     Region          63..79
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            order(67,69..73,77,95,97,102,126..127,170,173,209,211,221,
                     223,225,228..229,265,267..269,275,277,279,281..282,308)
                     /site_type="active"
                     /db_xref="CDD:197321"
     Site            order(67,69..73,77,95,97,102,126..127,170,173,209,211,221,
                     223,225,228..229,265,267..269,275,277,279,281,308)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197321"
     Site            order(67,95,170,173,209,211,308)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197321"
     Site            order(67,95,170,209,211,282,307..308)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197321"
     Site            order(69,95,307)
                     /site_type="metal-binding"
                     /note="metal binding site A [ion binding]"
                     /db_xref="CDD:197321"
     Site            order(170,173,209,211,229,265,279,281,308)
                     /site_type="other"
                     /note="AP binding site [nucleotide binding]"
                     /db_xref="CDD:197321"
     Site            196
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27695; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            order(209,211,308)
                     /site_type="metal-binding"
                     /note="metal binding site B [ion binding]"
                     /db_xref="CDD:197321"
     Site            211
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:P28352; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Site            282
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     Region          288..317
                     /region_name="Mitochondrial targeting sequence (MTS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P43138.2)"
     Site            308
                     /site_type="other"
                     /note="Interaction with DNA substrate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P43138.2)"
     CDS             1..317
                     /gene="Apex1"
                     /gene_synonym="APE; Apex; REF-1"
                     /coded_by="NM_024148.1:108..1061"
                     /db_xref="GeneID:79116"
                     /db_xref="RGD:2126"
ORIGIN      
        1 mpkrgkraaa edgeepksep etkkskgaak ktekeaageg pvlyedppdq ktsasgksat
       61 lkicswnvdg lrawikkkgl dwvkeeapdi lclqetkcse nklpaelqel pglthqywsa
      121 psdkegysgv gllsrqcplk vsygigeeeh dqegrvivae fesfilvtay vpnagrglvr
      181 leyrqrwdea frkflkdlas rkplvlcgdl nvaheeidlr npkgnkknag ftpqerqgfg
      241 emlqavplad sfrhlypnta yaytfwtymm narsknvgwr ldyfllshsl lpalcdskir
      301 skalgsdhcp itlylal
//
LOCUS       NP_075590                414 aa            linear   ROD 27-APR-2025
DEFINITION  casein kinase I isoform gamma-2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_075590 XP_001071924 XP_001071962 XP_001071997 XP_001072038
VERSION     NP_075590.2
DBSOURCE    REFSEQ: accession NM_023102.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Chia,R., Haddock,S., Beilina,A., Rudenko,I.N., Mamais,A.,
            Kaganovich,A., Li,Y., Kumaran,R., Nalls,M.A. and Cookson,M.R.
  TITLE     Phosphorylation of LRRK2 by casein kinase 1alpha regulates
            trans-Golgi clustering via differential interaction with ARHGEF7
  JOURNAL   Nat Commun 5, 5827 (2014)
   PUBMED   25500533
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Zhai,L., Graves,P.R., Robinson,L.C., Italiano,M., Culbertson,M.R.,
            Rowles,J., Cobb,M.H., DePaoli-Roach,A.A. and Roach,P.J.
  TITLE     Casein kinase I gamma subfamily. Molecular cloning, expression, and
            characterization of three mammalian isoforms and complementation of
            defects in the Saccharomyces cerevisiae YCK genes
  JOURNAL   J Biol Chem 270 (21), 12717-12724 (1995)
   PUBMED   7759525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072533.1 and U22297.1.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001072038.1, XP_001071962.1, XP_001071924.1, XP_001071997.1,
            NP_075590.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: U22297.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..414
                     /product="casein kinase I isoform gamma-2 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="CKI-gamma 2; casein kinase I"
                     /calculated_mol_wt=47376
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62762.2)"
     Region          45..331
                     /region_name="STKc_CK1_gamma"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, Casein Kinase 1 gamma; cd14126"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,118..122,124,126,164,166,168..169,
                     171,187,190,213..216)
                     /site_type="active"
                     /db_xref="CDD:271028"
     Site            order(52..58,60,73,75,118..122,166,168..169,171,187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271028"
     Site            order(56,124,126,164,166,168,190,213..216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271028"
     Site            186..216
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271028"
     Region          331..384
                     /region_name="CK1gamma_C"
                     /note="Casein kinase 1 gamma C terminal; pfam12605"
                     /db_xref="CDD:463640"
     Region          368..414
                     /region_name="Phospho-regulated basic and hydrophobic
                     (PRBH) motif. /evidence=ECO:0000250|UniProtKB:P78368"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62762.2)"
     CDS             1..414
                     /gene="Csnk1g2"
                     /coded_by="NM_023102.2:459..1703"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65278"
                     /db_xref="RGD:621407"
ORIGIN      
        1 mdfdkkggkg eleegrrmsk tgtnrsnhgv rnsgtssgvl mvgpnfrvgk kigcgnfgel
       61 rlgknlytne yvaiklepik srapqlhley rfykqlsttg vpqvyyfgpc gkynamvlel
      121 lgpsledlfd lcdrtftlkt vlmiaiqlit rmeyvhtksl iyrdvkpenf lvgrpgskrq
      181 hsihiidfgl akeyidpetk khipyrehks ltgtarymsi nthlgkeqsr rddlealghm
      241 fmyflrgslp wqglkadtlk eryqkigdtk ratpievlce sfpeematyl ryvrrldffe
      301 kpdydylrkl ftdlfdrsgy vfdyeydwag kplptpigtv hpdvpsqpph rdkaqlhtkn
      361 qalnstngel ntddptaghs napiaapaev evadetkccc ffkrrkrksl qrhk
//
LOCUS       NP_001128163              37 aa            linear   ROD 27-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit 4 [Rattus norvegicus].
ACCESSION   NP_001128163
VERSION     NP_001128163.1
DBSOURCE    REFSEQ: accession NM_001134691.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 37)
  AUTHORS   Dumax-Vorzet,A., Roboti,P. and High,S.
  TITLE     OST4 is a subunit of the mammalian oligosaccharyltransferase
            required for efficient N-glycosylation
  JOURNAL   J Cell Sci 126 (Pt 12), 2595-2606 (2013)
   PUBMED   23606741
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI298452.1, CB706964.1 and BI277067.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW918924.1, FQ124330.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..37
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..37
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 4"
                     /note="oligosaccharyltransferase 4 homolog"
                     /calculated_mol_wt=4062
     Region          1..34
                     /region_name="Ost4"
                     /note="Oligosaccaryltransferase; pfam10215"
                     /db_xref="CDD:431142"
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BLS0.1)"
     CDS             1..37
                     /gene="Ost4"
                     /coded_by="NM_001134691.1:71..184"
                     /db_xref="GeneID:100188932"
                     /db_xref="RGD:2300150"
ORIGIN      
        1 mitdvqlaif anmlgvslfl lvvlyhyvav nnpkkqe
//
LOCUS       NP_001012048             422 aa            linear   ROD 27-APR-2025
DEFINITION  SH2 domain-containing protein 4A [Rattus norvegicus].
ACCESSION   NP_001012048 XP_224758
VERSION     NP_001012048.1
DBSOURCE    REFSEQ: accession NM_001012048.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Patrakka,J., Xiao,Z., Nukui,M., Takemoto,M., He,L., Oddsson,A.,
            Perisic,L., Kaukinen,A., Szigyarto,C.A., Uhlen,M., Jalanko,H.,
            Betsholtz,C. and Tryggvason,K.
  TITLE     Expression and subcellular distribution of novel
            glomerulus-associated proteins dendrin, ehd3, sh2d4a, plekhh2, and
            2310066E14Rik
  JOURNAL   J Am Soc Nephrol 18 (3), 689-697 (2007)
   PUBMED   17251388
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079100.1.
            
            On Feb 11, 2005 this sequence version replaced XP_224758.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..422
                     /product="SH2 domain-containing protein 4A"
                     /calculated_mol_wt=48391
     Region          <32..>243
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D7V1; propagated from
                     UniProtKB/Swiss-Prot (Q6AYC8.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H788; propagated from
                     UniProtKB/Swiss-Prot (Q6AYC8.1)"
     Region          141..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC8.1)"
     Region          202..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYC8.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H788; propagated from
                     UniProtKB/Swiss-Prot (Q6AYC8.1)"
     Region          308..410
                     /region_name="SH2_SH2D4A"
                     /note="Src homology 2 domain found in the SH2 domain
                     containing protein 4A (SH2D4A); cd10350"
                     /db_xref="CDD:198213"
     Site            order(323,341,361,363)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198213"
     Site            order(362,391)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198213"
     CDS             1..422
                     /gene="Sh2d4a"
                     /coded_by="NM_001012048.1:229..1497"
                     /db_xref="GeneID:306376"
                     /db_xref="RGD:1307991"
ORIGIN      
        1 mlrqilsemf idpdllaels eeqkqilfyk mreeqirrwk ereaamerke slpvksrpkk
       61 engksvhwkl gadkqvwvwv mgehhldkpy dvlcdeilae rehlraakda elrkaqslqf
      121 tnslkvksln cdlqavkkte pqnvtrkaaa eeatdqgpra iptkkddkaq tkdltkkkds
      181 eelkqtedek tkqiyknwke dsewqaslrk skaadekrrs lakqaredyk rlsqrgrsgd
      241 glqnpltgpq kpkrpplppk pqflqplgsp pkslgnqgvi rtktsstqed iirwfkeeql
      301 pfragyqkns dtiapwfhgi ltlkkanell stgmpgsfli rvsekikgya lsylseegck
      361 hflidasans ysflgvdqlq hatladlvey hkeepitslg kelllfpcgq qdkppdylel
      421 fq
//
LOCUS       NP_036940                297 aa            linear   ROD 27-APR-2025
DEFINITION  thiosulfate sulfurtransferase [Rattus norvegicus].
ACCESSION   NP_036940 XP_343285
VERSION     NP_036940.1
DBSOURCE    REFSEQ: accession NM_012808.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Smirnov,A., Entelis,N., Martin,R.P. and Tarassov,I.
  TITLE     Biological significance of 5S rRNA import into human mitochondria:
            role of ribosomal protein MRP-L18
  JOURNAL   Genes Dev 25 (12), 1289-1305 (2011)
   PUBMED   21685364
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Buhrke,T., Lengler,I. and Lampen,A.
  TITLE     Analysis of proteomic changes induced upon cellular differentiation
            of the human intestinal cell line Caco-2
  JOURNAL   Dev Growth Differ 53 (3), 411-426 (2011)
   PUBMED   21492153
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Smirnov,A., Comte,C., Mager-Heckel,A.M., Addis,V.,
            Krasheninnikov,I.A., Martin,R.P., Entelis,N. and Tarassov,I.
  TITLE     Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA
            import into human mitochondria
  JOURNAL   J Biol Chem 285 (40), 30792-30803 (2010)
   PUBMED   20663881
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Nagahara,N., Okazaki,T. and Nishino,T.
  TITLE     Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily
            related to mitochondrial rhodanese. Striking similarity in active
            site amino acid sequence and the increase in the mercaptopyruvate
            sulfurtransferase activity of rhodanese by site-directed
            mutagenesis
  JOURNAL   J Biol Chem 270 (27), 16230-16235 (1995)
   PUBMED   7608189
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Weiland,K.L. and Dooley,T.P.
  TITLE     Molecular cloning, sequencing and characterization of cDNA to rat
            liver rhodanese, a thiosulphate sulphurtransferase
  JOURNAL   Biochem J 275 (Pt 1) (Pt 1), 227-231 (1991)
   PUBMED   2018478
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088449.1.
            
            On Jan 13, 2005 this sequence version replaced XP_343285.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088449.1, FQ216517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..297
                     /product="thiosulfate sulfurtransferase"
                     /EC_number="2.8.1.1"
                     /note="rhodanese; Thiosulfate sulphurtransferase
                     (rhodanese); thiosulfate sulfurtransferase, mitochondrial"
                     /calculated_mol_wt=33276
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q16762; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Region          27..279
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
     Site            35
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24098488; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            136
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Region          144..159
                     /region_name="Hinge"
                     /note="propagated from UniProtKB/Swiss-Prot (P24329.3)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            175
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            236
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     Site            237
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52196; propagated from
                     UniProtKB/Swiss-Prot (P24329.3)"
     CDS             1..297
                     /gene="Tst"
                     /gene_synonym="RHODAN"
                     /coded_by="NM_012808.1:32..925"
                     /db_xref="GeneID:25274"
                     /db_xref="RGD:3913"
ORIGIN      
        1 mvhqvlyral vstkwlaesi rsgkvgpslr vldaswyspg trqarkeyqe rhvpgasffd
       61 ieecrdttsp yemmlpseah fgdyvgnlgi sndthvvvyd gddlgsfyap rvwwmfrvfg
      121 hrtvsvlngg frnwlkeghp vtsepsrpep avfkatlnrs llktyeqvle nlqskrfqlv
      181 dsraqgrylg tqpepdavgl dsghirgsvn vpfmnflted gfekspeelr aifqdkkvdl
      241 sqpliatcrk gvtachiala aylcgkpdva vydgswsewf rrappetrvs qgksgka
//
LOCUS       NP_808789                491 aa            linear   ROD 27-APR-2025
DEFINITION  nicotinamide phosphoribosyltransferase [Rattus norvegicus].
ACCESSION   NP_808789
VERSION     NP_808789.1
DBSOURCE    REFSEQ: accession NM_177928.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Li,D., Chen,Y., Wang,Y., Liu,J., Chai,L., Zhang,Q., Qiu,Y.,
            Chen,H., Shen,N., Shi,X. and Li,M.
  TITLE     NAMPT mediates PDGF-induced pulmonary arterial smooth muscle cell
            proliferation by TLR4/NF-kappaB/PLK4 signaling pathway
  JOURNAL   Eur J Pharmacol 961, 176151 (2023)
   PUBMED   37914064
  REMARK    GeneRIF: NAMPT mediates PDGF-induced pulmonary arterial smooth
            muscle cell proliferation by TLR4/NF-kappaB/PLK4 signaling pathway.
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Miao,J., He,X., Hu,J. and Cai,W.
  TITLE     Emodin inhibits NF-kappaB signaling pathway to protect obese
            asthmatic rats from pathological damage via Visfatin
  JOURNAL   Tissue Cell 74, 101713 (2022)
   PUBMED   34952398
  REMARK    GeneRIF: Emodin inhibits NF-kappaB signaling pathway to protect
            obese asthmatic rats from pathological damage via Visfatin.
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Lei,M., Tao,M.Q., Wu,Y.J., Xu,L., Yang,Z., Li,Y., Olatunji,O.J.,
            Wang,X.W. and Zuo,J.
  TITLE     Metabolic Enzyme Triosephosphate Isomerase 1 and Nicotinamide
            Phosphoribosyltransferase, Two Independent Inflammatory Indicators
            in Rheumatoid Arthritis: Evidences From Collagen-Induced Arthritis
            and Clinical Samples
  JOURNAL   Front Immunol 12, 795626 (2022)
   PUBMED   35111160
  REMARK    GeneRIF: Metabolic Enzyme Triosephosphate Isomerase 1 and
            Nicotinamide Phosphoribosyltransferase, Two Independent
            Inflammatory Indicators in Rheumatoid Arthritis: Evidences From
            Collagen-Induced Arthritis and Clinical Samples.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Zhang,H., Wang,L., Xiang,Y., Wang,Y. and Li,H.
  TITLE     Nampt promotes fibroblast extracellular matrix degradation in
            stress urinary incontinence by inhibiting autophagy
  JOURNAL   Bioengineered 13 (1), 481-495 (2022)
   PUBMED   34967693
  REMARK    GeneRIF: Nampt promotes fibroblast extracellular matrix degradation
            in stress urinary incontinence by inhibiting autophagy.
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Sun,Y., Li,X., Yang,X., Chen,B. and Zhang,W.
  TITLE     Small Extracellular Vesicles Derived from Adipocytes Attenuate
            Intervertebral Disc Degeneration in Rats by Rejuvenating Senescent
            Nucleus Pulposus Cells and Endplate Cells by Delivering Exogenous
            NAMPT
  JOURNAL   Oxid Med Cell Longev 2021, 9955448 (2021)
   PUBMED   34434488
  REMARK    GeneRIF: Small Extracellular Vesicles Derived from Adipocytes
            Attenuate Intervertebral Disc Degeneration in Rats by Rejuvenating
            Senescent Nucleus Pulposus Cells and Endplate Cells by Delivering
            Exogenous NAMPT.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Wang,T., Zhang,X., Bheda,P., Revollo,J.R., Imai,S. and Wolberger,C.
  TITLE     Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic
            enzyme
  JOURNAL   Nat Struct Mol Biol 13 (7), 661-662 (2006)
   PUBMED   16783373
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Kloting,N. and Kloting,I.
  TITLE     Visfatin: gene expression in isolated adipocytes and sequence
            analysis in obese WOKW rats compared with lean control rats
  JOURNAL   Biochem Biophys Res Commun 332 (4), 1070-1072 (2005)
   PUBMED   15922301
  REMARK    GeneRIF: relative visfatin gene expression is not associated with
            the metabolic syndrome in WOKW rats [Pbef, also called visfatin]
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Revollo,J.R., Grimm,A.A. and Imai,S.
  TITLE     The NAD biosynthesis pathway mediated by nicotinamide
            phosphoribosyltransferase regulates Sir2 activity in mammalian
            cells
  JOURNAL   J Biol Chem 279 (49), 50754-50763 (2004)
   PUBMED   15381699
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Kitani,T., Okuno,S. and Fujisawa,H.
  TITLE     Growth phase-dependent changes in the subcellular localization of
            pre-B-cell colony-enhancing factor
  JOURNAL   FEBS Lett 544 (1-3), 74-78 (2003)
   PUBMED   12782293
  REMARK    GeneRIF: PBEF is not a cytokine-like secreted protein but an
            intracellular protein associated with the cell cycle
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Dietrich,L.S. and Muniz,O.
  TITLE     Inhibition of nicotinamide phosphoribosyltransferase by pyridine
            nucleotides
  JOURNAL   Biochemistry 11 (9), 1691-1695 (1972)
   PUBMED   4402158
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085681.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085681.1, AB081730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..491
                     /product="nicotinamide phosphoribosyltransferase"
                     /EC_number="2.4.2.12"
                     /note="visfatin; NAmPRTase; pre-B-cell colony-enhancing
                     factor 1 homolog; pre-B-cell colony enhancing factor 1"
                     /calculated_mol_wt=55307
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P43490; propagated from
                     UniProtKB/Swiss-Prot (Q80Z29.1)"
     Region          12..428
                     /region_name="PBEF_like"
                     /note="pre-B-cell colony-enhancing factor (PBEF)-like. The
                     mammalian members of this group of nicotinate
                     phosphoribosyltransferases (NAPRTases) were originally
                     identified as genes whose expression is upregulated upon
                     activation in lymphoid cells. In general; cd01569"
                     /db_xref="CDD:238803"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P43490; propagated from
                     UniProtKB/Swiss-Prot (Q80Z29.1)"
     Site            order(195..197,220..221,313,352..353,381,383..384,387)
                     /site_type="active"
                     /db_xref="CDD:238803"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43490; propagated from
                     UniProtKB/Swiss-Prot (Q80Z29.1)"
     CDS             1..491
                     /gene="Nampt"
                     /gene_synonym="Pbef; Pbef1"
                     /coded_by="NM_177928.3:28..1503"
                     /db_xref="GeneID:297508"
                     /db_xref="RGD:631365"
ORIGIN      
        1 mnaaaeaefn illatdsykv thykqyppnt skvysyfecr ekktenskvr kvkyeetvfy
       61 glqyilnkyl kgkvvtkeki qeakevyreh fqddvfnerg wnyilekydg hlpievkavp
      121 egsviprgnv lftventdpe cywltnwiet ilvqswypit vatnsreqkk ilakyllets
      181 gnldgleykl hdfgyrgvss qetagigasa hlvnfkgtdt vagialikky ygtkdpvpgy
      241 svpaaehsti tawgkdhekd afehivtqfs svpvsvvsds ydiynaceki wgedlrhliv
      301 srsteaplii rpdsgnpldt vlkvldilgk kfpvsenskg ykllppylrv iqgdgvdint
      361 lqeivegmkq kkwsienvsf gsggallqkl trdllncsfk csyvvtnglg vnvfkdpvad
      421 pnkrskkgrl slhrtpagtf vtleegkgdl eeyghdllht vfkngkvtks ysfdevrkna
      481 qlnmeqdvap h
//
LOCUS       NP_001004255             378 aa            linear   ROD 27-APR-2025
DEFINITION  protein DEK [Rattus norvegicus].
ACCESSION   NP_001004255 XP_225209
VERSION     NP_001004255.1
DBSOURCE    REFSEQ: accession NM_001004255.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Cheung,T.H., Quach,N.L., Charville,G.W., Liu,L., Park,L.,
            Edalati,A., Yoo,B., Hoang,P. and Rando,T.A.
  TITLE     Maintenance of muscle stem-cell quiescence by microRNA-489
  JOURNAL   Nature 482 (7386), 524-528 (2012)
   PUBMED   22358842
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Kavanaugh,G.M., Wise-Draper,T.M., Morreale,R.J., Morrison,M.A.,
            Gole,B., Schwemberger,S., Tichy,E.D., Lu,L., Babcock,G.F.,
            Wells,J.M., Drissi,R., Bissler,J.J., Stambrook,P.J.,
            Andreassen,P.R., Wiesmuller,L. and Wells,S.I.
  TITLE     The human DEK oncogene regulates DNA damage response signaling and
            repair
  JOURNAL   Nucleic Acids Res 39 (17), 7465-7476 (2011)
   PUBMED   21653549
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Hollenbach,A.D., McPherson,C.J., Mientjes,E.J., Iyengar,R. and
            Grosveld,G.
  TITLE     Daxx and histone deacetylase II associate with chromatin through an
            interaction with core histones and the chromatin-associated protein
            Dek
  JOURNAL   J Cell Sci 115 (Pt 16), 3319-3330 (2002)
   PUBMED   12140263
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079344.1.
            
            On Sep 10, 2004 this sequence version replaced XP_225209.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079344.1, SRR8487231.33871.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132292
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..378
                     /product="protein DEK"
                     /note="DEK oncogene (DNA binding)"
                     /calculated_mol_wt=42761
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Region          151..185
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Region          186..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Region          207..223
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35659; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS3.1)"
     Region          323..377
                     /region_name="DEK_C"
                     /note="DEK C terminal domain; pfam08766"
                     /db_xref="CDD:462592"
     CDS             1..378
                     /gene="Dek"
                     /coded_by="NM_001004255.1:106..1242"
                     /db_xref="GeneID:306817"
                     /db_xref="RGD:1303246"
ORIGIN      
        1 msaaaapaae gedtptppas ekepempgpr eeseeeeeed dddedeeeek ekslivegkr
       61 ekrkverltm qvsslqrepf tiaqgkgqkl ceierihffl skkktdelrn lhkllynrpg
      121 tvsslkknvg qfsgfpfekg stqykkkeem lkkyrnamlk sicevldler sgvnselvkr
      181 ilnflmhpkp sgkplpkskk ssskgskker nssgttrksk qtkcpeilsd esssdedekk
      241 nkdessedee keseeeqppk ktskkekakq kattkskksv ksanvkkads sttkknqnss
      301 kkesgsedss ddeplikklk kpptdeelke tvkklladan leevtmkqic kevyenypay
      361 dlterkdfik ttvkelis
//
LOCUS       NP_076473                648 aa            linear   ROD 27-APR-2025
DEFINITION  cell surface glycoprotein MUC18 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_076473 XP_346824
VERSION     NP_076473.2
DBSOURCE    REFSEQ: accession NM_023983.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Yamchi,N.N., Rahbarghazi,R., Bedate,A.M., Mahdipour,M., Nouri,M.
            and Khanbabaee,R.
  TITLE     Menstrual blood CD146+ mesenchymal stem cells reduced fibrosis rate
            in the rat model of premature ovarian failure
  JOURNAL   Cell Biochem Funct 39 (8), 998-1008 (2021)
   PUBMED   34477225
  REMARK    GeneRIF: Menstrual blood CD146(+) mesenchymal stem cells reduced
            fibrosis rate in the rat model of premature ovarian failure.
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Marr,N., Meeson,R., Kelly,E.F., Fang,Y., Peffers,M.J.,
            Pitsillides,A.A., Dudhia,J. and Thorpe,C.T.
  TITLE     CD146 Delineates an Interfascicular Cell Sub-Population in Tendon
            That Is Recruited during Injury through Its Ligand Laminin-alpha4
  JOURNAL   Int J Mol Sci 22 (18), 9729 (2021)
   PUBMED   34575887
  REMARK    GeneRIF: CD146 Delineates an Interfascicular Cell Sub-Population in
            Tendon That Is Recruited during Injury through Its Ligand
            Laminin-alpha4.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Obara,M., Sato,S., Takahashi,K., Kondo,Y., Hirose,M., Nata,K. and
            Taira,E.
  TITLE     Expression of cell adhesion molecule, Gicerin/CD146 during the
            formation of heart and in the cardiac hypertrophy
  JOURNAL   Mol Cell Biochem 476 (5), 2021-2028 (2021)
   PUBMED   33515199
  REMARK    GeneRIF: Expression of cell adhesion molecule, Gicerin/CD146 during
            the formation of heart and in the cardiac hypertrophy.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Liu,G., Sun,X., Bian,J., Wu,R., Guan,X., Ouyang,B., Huang,Y.,
            Xiao,H., Luo,D., Atala,A., Zhang,Y. and Deng,C.
  TITLE     Correction of diabetic erectile dysfunction with adipose derived
            stem cells modified with the vascular endothelial growth factor
            gene in a rodent diabetic model
  JOURNAL   PLoS One 8 (8), e72790 (2013)
   PUBMED   24023647
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Taira,E., Kohama,K., Tsukamoto,Y., Okumura,S. and Miki,N.
  TITLE     Gicerin/CD146 is involved in neurite extension of NGF-treated PC12
            cells
  JOURNAL   J Cell Physiol 204 (2), 632-637 (2005)
   PUBMED   15880440
  REMARK    GeneRIF: Increase of gicerin expression by NGF promotes the
            gicerin-gicerin homophilic interaction resulting in the neurite
            extension.
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Taira,E., Kohama,K., Tsukamoto,Y., Okumura,S. and Miki,N.
  TITLE     Characterization of Gicerin/MUC18/CD146 in the rat nervous system
  JOURNAL   J Cell Physiol 198 (3), 377-387 (2004)
   PUBMED   14755543
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Okumura,S., Kohama,K., Kim,S., Iwao,H., Miki,N. and Taira,E.
  TITLE     Induction of gicerin/CD146 in the rat carotid artery after balloon
            injury
  JOURNAL   Biochem Biophys Res Commun 313 (4), 902-906 (2004)
   PUBMED   14706627
  REMARK    GeneRIF: expression of gicerin was increased in the rat carotid
            arteries after balloon injury. Gicerin might be involved in the
            arteriosclerotic neointima formation in the artery.
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Tsukamoto,Y., Egawa,M., Hiroi,S., Furuya,M., Tsuchiya,S.,
            Sasaki,F., Miki,N. and Taira,E.
  TITLE     Gicerin, an Ig-superfamily cell adhesion molecule, promotes the
            invasive and metastatic activities of a mouse fibroblast cell line
  JOURNAL   J Cell Physiol 197 (1), 103-109 (2003)
   PUBMED   12942546
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Li,B.S., Su,Q.N., Kiyama,H., Miki,N., Robinow,D.R. and Zhang,L.
  TITLE     Expression of gicerin, a novel cell adhesion molecule, is
            upregulated in the astrocytes after hypoglossal nerve injury in
            rats
  JOURNAL   Neurosci Lett 260 (3), 149-152 (1999)
   PUBMED   10076889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070916.1 and AB035506.1.
            
            On Oct 6, 2005 this sequence version replaced NP_076473.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB035506.1, SRR8487230.91818.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..648
                     /product="cell surface glycoprotein MUC18 isoform 1
                     precursor"
                     /note="cell surface glycoprotein MUC18; gicerin;
                     melanoma-associated antigen MUC18; l-gicerin"
                     /calculated_mol_wt=68951
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2394
     mat_peptide     24..648
                     /product="Cell surface glycoprotein MUC18.
                     /id=PRO_0000045461"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
                     /calculated_mol_wt=68951
     Region          43..120
                     /region_name="CD19_double_Ig"
                     /note="CD19 (Cluster of Differentiation 19), a unique
                     double immunoglobulin (Ig)-fold domain; cl49627"
                     /db_xref="CDD:483967"
     Region          43..50
                     /region_name="strand B"
                     /note="strand B [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(45,47,49,81,102,104,106,111)
                     /site_type="other"
                     /note="CD81 binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          51..60
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:467824"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          60..67
                     /region_name="strand C"
                     /note="strand C [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(67,117)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          76..80
                     /region_name="strand C'"
                     /note="strand C' [structural motif]"
                     /db_xref="CDD:467824"
     Region          81..90
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:467824"
     Region          90..120
                     /region_name="protodomain 2+4"
                     /note="protodomain 2+4 [structural motif]"
                     /db_xref="CDD:467824"
     Region          90..94
                     /region_name="strand D"
                     /note="strand D [structural motif]"
                     /db_xref="CDD:467824"
     Region          101..106
                     /region_name="strand E"
                     /note="strand E [structural motif]"
                     /db_xref="CDD:467824"
     Region          112..120
                     /region_name="strand F"
                     /note="strand F [structural motif]"
                     /db_xref="CDD:467824"
     Region          141..236
                     /region_name="C2-set_2"
                     /note="CD80-like C2-set immunoglobulin domain; pfam08205"
                     /db_xref="CDD:400489"
     Region          173..177
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          264..323
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          282..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          348..412
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          <452..508
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          463..467
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          488..491
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          499..503
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          527..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Site            561..581
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R2Y2; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43121; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          626..648
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     CDS             1..648
                     /gene="Mcam"
                     /gene_synonym="CD146; Muc18"
                     /coded_by="NM_023983.3:19..1965"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:78967"
                     /db_xref="RGD:620463"
ORIGIN      
        1 mglprlvcaf lfaaccccrs atgvpgeekq ptptpdpvev evgntallkc gpahpsgnfs
       61 qvewflihke rqipifrvhq gkgqsepgey ehrlslhgpg atlalsqvtp hddrmflcks
      121 kqprpqdhyv qlqvykapee ptiqanvlgi hvdiqelkev atcvgrngyp ipqviwykng
      181 rplqeeenrv hiqssqtves sglytlksvl sarlvkedkd aqfycelsyr lpsgnrmkes
      241 kevtvpvlyp aekvwvevep vgllkegdhv kircltdgnp qphftinkkn psteemeees
      301 tdengllsle paqkhhsgvy qcqsldlett vmlssdplel lvnyvsdvqv dptapevqeg
      361 dsltltckae snqdlefewl rdktgqllgk gpilqlnnvk reaggrylcv asvpsvpgln
      421 rtrrvsvgif gspwmaaker kvwaqenaml nlsceasghp qptiswning satewnpdpq
      481 tvvstlnvlv tpelletgae ctasnslgsn ttviilklvt lttltpdssq ttglstptvs
      541 phsranstst ekklpqqesk gvvivavivc tlvlavlgat lyyfykkgkl pcgrsgkqei
      601 tlpptrksef vvevksdklp eemallqgsn gdkrapgdqg ekyidlrh
//
LOCUS       NP_001037738             525 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor GTPase-activating protein 3 [Rattus
            norvegicus].
ACCESSION   NP_001037738 XP_001077733
VERSION     NP_001037738.1
DBSOURCE    REFSEQ: accession NM_001044273.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Liu,X., Zhang,C., Xing,G., Chen,Q. and He,F.
  TITLE     Functional characterization of novel human ARFGAP3
  JOURNAL   FEBS Lett 490 (1-2), 79-83 (2001)
   PUBMED   11172815
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099081.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001077733.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099081.1, SRR8487226.95886.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..525
                     /product="ADP-ribosylation factor GTPase-activating
                     protein 3"
                     /note="ADP-ribosylation factor GTPase activating protein
                     3; ARF GAP 3"
                     /calculated_mol_wt=57540
     Region          1..488
                     /region_name="PLN03114"
                     /note="ADP-ribosylation factor GTPase-activating protein
                     AGD10; Provisional"
                     /db_xref="CDD:178661"
     Region          4..123
                     /region_name="ArfGap_ArfGap3"
                     /note="Arf1 GTPase-activating protein 3; cd09028"
                     /db_xref="CDD:350085"
     Site            order(25,28,45,48,53)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350085"
     Site            order(25,28,45,48)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350085"
     Region          160..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Region          249..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Region          293..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Region          377..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP61; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN7.1)"
     CDS             1..525
                     /gene="Arfgap3"
                     /coded_by="NM_001044273.1:64..1641"
                     /db_xref="GeneID:503165"
                     /db_xref="RGD:1560066"
ORIGIN      
        1 mgdpskqdil aifkrlrsvp tnkvcfdcga knpswasisy gvflcidcsg shrslgvhls
       61 firsteldsn wswfqlrcmq vggnanassf fhqhgcatkd tnakynsraa qlyrekiktl
      121 atqatrrhgt dlwldscaap paspppkeed ffashaslev sgatqasaqp epasstpwgl
      181 ettpekhegg pgqgpsvegl ntpgktapae vssiikkkpn qakkglgakk gslgaqkltn
      241 tsfteiekqa qavdkrkeqe dlargtpkee sivsslrlay kdleihkkqd erlnlsgqkk
      301 aeaerlgmgf gscrggishs vtsdmqtieq esptlakprr kyqedpedsy fsssskwseq
      361 sssryfddpm elrsshfssw ddsadsywkk dssrdpepat kstgssdrps srrkpeyepv
      421 gntdeaqkkf gnvkaissdm yfgiqsqtdf etrarlerls tsssissadl fdeqrkqttg
      481 nynlsnvlpn apdmaqfkqg vrsvagklsv fangvmtsiq drygs
//
LOCUS       NP_445832                695 aa            linear   ROD 27-APR-2025
DEFINITION  sodium-dependent phosphate transport protein 2B [Rattus
            norvegicus].
ACCESSION   NP_445832 XP_346463
VERSION     NP_445832.1
DBSOURCE    REFSEQ: accession NM_053380.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Pastor-Arroyo,E.M., Rodriguez,J.M.M., Pellegrini,G., Bettoni,C.,
            Levi,M., Hernando,N. and Wagner,C.A.
  TITLE     Constitutive depletion of Slc34a2/NaPi-IIb in rats causes perinatal
            mortality
  JOURNAL   Sci Rep 11 (1), 7943 (2021)
   PUBMED   33846411
  REMARK    GeneRIF: Constitutive depletion of Slc34a2/NaPi-IIb in rats causes
            perinatal mortality.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Ratcliffe,S., Jugdaohsingh,R., Vivancos,J., Marron,A., Deshmukh,R.,
            Ma,J.F., Mitani-Ueno,N., Robertson,J., Wills,J., Boekschoten,M.V.,
            Muller,M., Mawhinney,R.C., Kinrade,S.D., Isenring,P., Belanger,R.R.
            and Powell,J.J.
  TITLE     Identification of a mammalian silicon transporter
  JOURNAL   Am J Physiol Cell Physiol 312 (5), C550-C561 (2017)
   PUBMED   28179233
  REMARK    GeneRIF: This is the first evidence of an active Si transport
            protein in mammals and points towards an important role for Si in
            vertebrates and explains interactions between dietary phosphate and
            silicon.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Giral,H., Cranston,D., Lanzano,L., Caldas,Y., Sutherland,E.,
            Rachelson,J., Dobrinskikh,E., Weinman,E.J., Doctor,R.B., Gratton,E.
            and Levi,M.
  TITLE     NHE3 regulatory factor 1 (NHERF1) modulates intestinal
            sodium-dependent phosphate transporter (NaPi-2b) expression in
            apical microvilli
  JOURNAL   J Biol Chem 287 (42), 35047-35056 (2012)
   PUBMED   22904329
  REMARK    GeneRIF: that NHERF1 associates with NaPi-2b in enterocytes and
            regulates NaPi-2b adaptation.
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Suyama,T., Okada,S., Ishijima,T., Iida,K., Abe,K. and Nakai,Y.
  TITLE     High phosphorus diet-induced changes in NaPi-IIb phosphate
            transporter expression in the rat kidney: DNA microarray analysis
  JOURNAL   PLoS One 7 (1), e29483 (2012)
   PUBMED   22235299
  REMARK    GeneRIF: NaPi-IIb is upregulated in the kidney in response to the
            active excretion of phosphate in HP diet-fed rats
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Prie,D., Torres,P.U. and Friedlander,G.
  TITLE     Phosphate handling: new genes, new molecules
  JOURNAL   Horm Res Paediatr 76 Suppl 1, 71-75 (2011)
   PUBMED   21778753
  REMARK    Review article
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Miyoshi,K., Shillingford,J.M., Smith,G.H., Grimm,S.L., Wagner,K.U.,
            Oka,T., Rosen,J.M., Robinson,G.W. and Hennighausen,L.
  TITLE     Signal transducer and activator of transcription (Stat) 5 controls
            the proliferation and differentiation of mammary alveolar
            epithelium
  JOURNAL   J Cell Biol 155 (4), 531-542 (2001)
   PUBMED   11706048
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Hashimoto,M., Wang,D.Y., Kamo,T., Zhu,Y., Tsujiuchi,T., Konishi,Y.,
            Tanaka,M. and Sugimura,H.
  TITLE     Isolation and localization of type IIb Na/Pi cotransporter in the
            developing rat lung
  JOURNAL   Am J Pathol 157 (1), 21-27 (2000)
   PUBMED   10880371
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Xu,H., Bai,L., Collins,J.F. and Ghishan,F.K.
  TITLE     Molecular cloning, functional characterization, tissue
            distribution, and chromosomal localization of a human, small
            intestinal sodium-phosphate (Na+-Pi) transporter (SLC34A2)
  JOURNAL   Genomics 62 (2), 281-284 (1999)
   PUBMED   10610722
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Feild,J.A., Zhang,L., Brun,K.A., Brooks,D.P. and Edwards,R.M.
  TITLE     Cloning and functional characterization of a sodium-dependent
            phosphate transporter expressed in human lung and small intestine
  JOURNAL   Biochem Biophys Res Commun 258 (3), 578-582 (1999)
   PUBMED   10329428
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Hilfiker,H., Hattenhauer,O., Traebert,M., Forster,I., Murer,H. and
            Biber,J.
  TITLE     Characterization of a murine type II sodium-phosphate cotransporter
            expressed in mammalian small intestine
  JOURNAL   Proc Natl Acad Sci U S A 95 (24), 14564-14569 (1998)
   PUBMED   9826740
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070898.1.
            
            On Jan 7, 2005 this sequence version replaced XP_346463.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070898.1, AF157026.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..695
                     /product="sodium-dependent phosphate transport protein 2B"
                     /note="naPi-2b; sodium/phosphate cotransporter 2B;
                     sodium-phosphate transport protein 2B; Na(+)/Pi
                     cotransporter 2B; Na(+)-dependent phosphate cotransporter
                     2B; rNaPi IIb; type IIb sodium-phosphate transporter;
                     solute carrier family 34 (sodium phosphate), member 2;
                     solute carrier family 34 (type II sodium/phosphate
                     contransporter), member 2; solute carrier family 34 (type
                     II sodium/phosphate cotransporter), member 2"
                     /calculated_mol_wt=75862
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Region          105..604
                     /region_name="2a58"
                     /note="Phosphate:Na+ Symporter (PNaS) Family; TIGR01013"
                     /db_xref="CDD:162157"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            409..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            487..507
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            527..547
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     Site            552..572
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ09.1)"
     CDS             1..695
                     /gene="Slc34a2"
                     /coded_by="NM_053380.2:32..2119"
                     /db_xref="GeneID:84395"
                     /db_xref="RGD:620889"
ORIGIN      
        1 mapwpelena hpnpnkfieg asgpqssipd kdkgtsktnd sgtpvakiel lpsysalvli
       61 eeppegndpw dlpelqdngi kwserdskgk ilcifqgigk filllgflyl fvcsldvlss
      121 afqlvggkma gqffsnnsim snpvaglvig vlvtvmvqss stsssiivsm vassllsvra
      181 aipiimgani gtsitntiva lmqagdrnef rrafagatvh dffnwlsvlv llpleaathy
      241 lekltnlvle tfsfqngeda pdilkvitdp ftkliiqldk kviqqiamgd seaqnkslik
      301 iwcktisnvi eenvtvpspd nctspsycwt dgiqtwtiqn vtekeniakc qhifvnfslp
      361 dlavgiillt vsllilcgcl imivkllgsv lrgqvatvik ktlntdfpfp fawltgylai
      421 lvgagmtfiv qsssvftsam tpligigvis ieraypltlg snigttttai laalaspgnt
      481 lrsslqialc hfffnisgil lwypipftrl pirlakglgn isakyrwfav fylifffllt
      541 pltvfglsla gwpvlvgvgv piillillvl clrmlqarcp rilplklrdw nflplwmhsl
      601 kpwdniisla tscfqrrccc ccrvccrvcc mvcgckccrc skccknleee ekeqdvpvka
      661 sggfdntams kecqdegkgq vevlgmkals nttvf
//
LOCUS       NP_001004258             357 aa            linear   ROD 27-APR-2025
DEFINITION  acyl-coenzyme A diphosphatase NUDT19 precursor [Rattus norvegicus].
ACCESSION   NP_001004258 XP_218512
VERSION     NP_001004258.1
DBSOURCE    REFSEQ: accession NM_001004258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079088.1.
            
            On Sep 10, 2004 this sequence version replaced XP_218512.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079088.1, FQ215228.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..357
                     /product="acyl-coenzyme A diphosphatase NUDT19 precursor"
                     /EC_number="3.6.1.77"
                     /note="nucleoside diphosphate-linked moiety X motif 19,
                     mitochondrial; nudix motif 19; nudix (nucleoside
                     diphosphate linked moiety X)-type motif 19; acyl-coenzyme
                     A diphosphatase NUDT19"
                     /calculated_mol_wt=39808
     Region          9..246
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
     Site            34
                     /site_type="other"
                     /note="Important for coenzyme A binding.
                     /evidence=ECO:0000250|UniProtKB:P11930; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD9.1)"
     Site            40
                     /site_type="other"
                     /note="Important for coenzyme A binding.
                     /evidence=ECO:0000250|UniProtKB:P11930; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD9.1)"
     Region          97..118
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD9.1)"
     Site            189
                     /site_type="other"
                     /note="Important for coenzyme A binding.
                     /evidence=ECO:0000250|UniProtKB:P11930; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD9.1)"
     Region          355..357
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD9.1)"
     CDS             1..357
                     /gene="Nudt19"
                     /coded_by="NM_001004258.1:53..1126"
                     /db_xref="GeneID:308518"
                     /db_xref="RGD:1302935"
ORIGIN      
        1 msgpsswrra atvmlaagws haspagfrll llqraqnqrf mpgahvfpgg vldaadsspd
       61 wvslfaprht pprfglgpep prqpsfpglf hgdadgaalp ddvalricai retfeeagvl
      121 llrprdsara sqepsialsp pagladwrsr vrsdprcflq lcahldctpd iwalhdwggw
      181 ltpygrssrr fdttfllccl retprvepdl aevvgykwls pseatecfls keiwlappqf
      241 yevrrlenfa slsalyrfcl dhplevpekw lpivlltsdg sihllpgdel yvkgsdflek
      301 nmsidkktee ivtegkvvnr ivihsphlye iymtltskse hgypksytak ksctarl
//
LOCUS       NP_476444               1687 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 12 isoform alpha [Rattus norvegicus].
ACCESSION   NP_476444
VERSION     NP_476444.2
DBSOURCE    REFSEQ: accession NM_057103.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1687)
  AUTHORS   Selvaraju,V., Suresh,S.C., Thirunavukkarasu,M., Mannu,J.,
            Foye,J.L.C., Mathur,P.P., Palesty,J.A., Sanchez,J.A., McFadden,D.W.
            and Maulik,N.
  TITLE     Regulation of A-Kinase-Anchoring Protein 12 by Heat Shock Protein
            A12B to Prevent Ventricular Dysfunction Following Acute Myocardial
            Infarction in Diabetic Rats
  JOURNAL   J Cardiovasc Transl Res 10 (2), 209-220 (2017)
   PUBMED   28281242
  REMARK    GeneRIF: HSPA12B overexpression interacts with AKAP12 and
            downregulate TXNIP in diabetic rats following acute myocardial
            infarction.
REFERENCE   2  (residues 1 to 1687)
  AUTHORS   Wilhelm,T., Lipka,D.B., Witte,T., Wierzbinska,J.A., Fluhr,S.,
            Helf,M., Mucke,O., Claus,R., Konermann,C., Nollke,P.,
            Niemeyer,C.M., Flotho,C. and Plass,C.
  TITLE     Epigenetic silencing of AKAP12 in juvenile myelomonocytic leukemia
  JOURNAL   Epigenetics 11 (2), 110-119 (2016)
   PUBMED   26891149
REFERENCE   3  (residues 1 to 1687)
  AUTHORS   Kritzer,M.D., Li,J., Passariello,C.L., Gayanilo,M., Thakur,H.,
            Dayan,J., Dodge-Kafka,K. and Kapiloff,M.S.
  TITLE     The scaffold protein muscle A-kinase anchoring protein beta
            orchestrates cardiac myocyte hypertrophic signaling required for
            the development of heart failure
  JOURNAL   Circ Heart Fail 7 (4), 663-672 (2014)
   PUBMED   24812305
REFERENCE   4  (residues 1 to 1687)
  AUTHORS   Yan,M., Zhao,J., Zhu,S., Shao,X., Zhang,L., Gao,H. and Yao,D.
  TITLE     Expression of SRC suppressed C kinase substrate in rat neural
            tissues during inflammation
  JOURNAL   Neurochem Res 39 (4), 748-757 (2014)
   PUBMED   24623461
  REMARK    GeneRIF: SSeCKS play an important role in sciatic nerve fibers and
            neurons in spinal cord and dorsal root ganglion during
            inflammation.
REFERENCE   5  (residues 1 to 1687)
  AUTHORS   You,T., Fan,Y., Li,Q., Gao,Y., Yang,Y., Zhao,Z. and Wang,C.
  TITLE     Increased SSeCKS expression in rat hepatic stellate cells upon
            activation in vitro and in vivo
  JOURNAL   Inflammation 36 (6), 1415-1423 (2013)
   PUBMED   23925424
REFERENCE   6  (residues 1 to 1687)
  AUTHORS   Xia,W. and Gelman,I.H.
  TITLE     Mitogen-induced, FAK-dependent tyrosine phosphorylation of the
            SSeCKS scaffolding protein
  JOURNAL   Exp Cell Res 277 (2), 139-151 (2002)
   PUBMED   12083796
  REMARK    GeneRIF: a role in mitogen-induced cytoskeletal reorganization
REFERENCE   7  (residues 1 to 1687)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   8  (residues 1 to 1687)
  AUTHORS   Siegel,S.M., Grove,B.D. and Carr,P.A.
  TITLE     SSeCKS immunolabeling in rat primary sensory neurons
  JOURNAL   Brain Res 926 (1-2), 126-136 (2002)
   PUBMED   11814414
REFERENCE   9  (residues 1 to 1687)
  AUTHORS   Chapline,C., Mousseau,B., Ramsay,K., Duddy,S., Li,Y., Kiley,S.C.
            and Jaken,S.
  TITLE     Identification of a major protein kinase C-binding protein and
            substrate in rat embryo fibroblasts. Decreased expression in
            transformed cells
  JOURNAL   J Biol Chem 271 (11), 6417-6422 (1996)
   PUBMED   8626441
REFERENCE   10 (residues 1 to 1687)
  AUTHORS   Lin,X., Nelson,P.J., Frankfort,B., Tombler,E., Johnson,R. and
            Gelman,I.H.
  TITLE     Isolation and characterization of a novel mitogenic regulatory
            gene, 322, which is transcriptionally suppressed in cells
            transformed by src and ras
  JOURNAL   Mol Cell Biol 15 (5), 2754-2762 (1995)
   PUBMED   7739556
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY695056.1 and BG664488.1.
            
            On Sep 20, 2005 this sequence version replaced NP_476444.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY695056.1, U41453.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1687
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..1687
                     /product="A-kinase anchor protein 12 isoform alpha"
                     /note="A kinase (PRKA) anchor protein (gravin) 12; SSeCKS,
                     Gravin, AKAP250; A kinase (PRKA) anchor protein 12;
                     AKAP-12"
                     /calculated_mol_wt=180980
     Region          1..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          175..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          254..544
                     /region_name="Involved in PKC-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          298..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          402..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          496..828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          592..620
                     /region_name="WSK"
                     /note="WSK motif; pfam03832"
                     /db_xref="CDD:461069"
     Region          594..614
                     /region_name="AKAP CaM-binding 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01241"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          743..763
                     /region_name="AKAP CaM-binding 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01241"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          784..809
                     /region_name="WSK"
                     /note="WSK motif; pfam03832"
                     /db_xref="CDD:461069"
     Region          784..804
                     /region_name="AKAP CaM-binding 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01241"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            873
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          959..981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1035..1105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1059
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          <1085..1346
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          1125..1221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1277..1361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1443..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1498..1511
                     /region_name="RII-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1522..1582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02952; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     Region          1599..1687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QD51.1)"
     Site            1637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTQ5; propagated from
                     UniProtKB/Swiss-Prot (Q5QD51.1)"
     CDS             1..1687
                     /gene="Akap12"
                     /gene_synonym="AKAP12A; AKAP12B; AKAP12G"
                     /coded_by="NM_057103.2:157..5220"
                     /note="isoform alpha is encoded by transcript variant 1"
                     /db_xref="GeneID:83425"
                     /db_xref="RGD:70988"
ORIGIN      
        1 mgagssteqr speqpagsdt pselvlsghg paaeasgaag dpadadpatk lpqkngqlst
       61 vngvaeqgdv hvqeenqegq eeevvdedvg qresedvrek drveemaans taveditkdg
      121 qeetseiieq ipasesnvee mvqpaesqan dvgfkkvfkf vgfkftvkkd kneksdtvql
      181 ltvkkdegeg aeasvgagdh qepsvetavg esaskeselk qstekqegtl kqeqssteip
      241 lqaesdqaae eeakdegeek qekeptkspe spsspvsset tssfkkffth gwagwrkkts
      301 fkkskeddle taekrkeqea ekvdeeekek tepaseeqep aedtdqarls adyekvelpl
      361 edqvgdleas seekcaplat evfdekmeah qevvaevhvs tvekteeeqg gggeaeggvv
      421 vegtgeslpp eklaepqevp qeaepaeelm ksremcvsgg dhtqltdlsp eektlpkhpe
      481 givsevemls sqerikvqgs plkklfsssg lkklsgkkqk gkrggggdee pgeyqhihte
      541 spesadeqkg essasspeep eettclekgp leapqdgeae egttsdgekk regitpwasf
      601 kkmvtpkkrv rrpsesdkee elekvksatl sstdstvsem qdevktvgee qkpeepkrrv
      661 dtsvsweali cvgsskkrar kasssddegg prtlggdshr aeeaskdkea gtdavpastq
      721 eqdqaqgsss pepagspseg egvstwesfk rlvtprkksk skleekaeds sveqlsteie
      781 psreeswvsi kkfipgrrkk radgkqeqat vedsgpvein eddpdvpavv plseydaver
      841 ekmeaqgnae lpqllgavyv seelsktlvh tvsvavidgt ravtsveers pswisasvte
      901 plehtageam ppveevtekd iiaeetpvlt qtlpegkdah ddmvtsevdf tseavtatet
      961 sealrteevt easgaeettd mvsavsqltd spdtteeatp vqeveggvld teeeerqtqa
     1021 ilqavadkvk eesqvpatqt vqrtgskale kveeveedse vlasekekdv mpkgpvqeag
     1081 aehlaqgset gqatpeslev pevtadvdhv atcqviklqq lmeqavapes setltdsetn
     1141 gstpladsdt adgtqqdeti dsqdskataa vrqsqvteee aataqkeeps tlpnnvpaqe
     1201 ehgeepgrdv leptqqelaa aavpvlakte vgqegevdwl dgekvkeeqe vfvhsgpnsq
     1261 kaadvtydse vmgvagcqek estevqslsl eegemetdve kekretkpeq vseegeqeta
     1321 apehegtygk pvltldmpss ergkalgslg gspslpdqdk agcievqvqs ldttvtqtae
     1381 avekvietvv isetgespec vgahllpaek ssatgghwtl qhaedtvplg pesqaesipi
     1441 ivtpapestl hpdlqgeisa sqrerseeed kpdagpdadg kestaiekvl kaepeilele
     1501 sksnkivlnv iqtavdqfar tetapethay dsqtqvpamq adsqgaqqml dknescqdet
     1561 psaaaqrgla spdrsggmgs asemlaalav esagvkvsie klppqpkdqk ehaadgpqlq
     1621 slaqaeasas gnltkespdt ngpklteegd apkvevqeee mstksvkenk aqaeedlqep
     1681 kgdlaes
//
LOCUS       NP_955421                419 aa            linear   ROD 27-APR-2025
DEFINITION  synaptosomal-associated protein 47 [Rattus norvegicus].
ACCESSION   NP_955421 XP_220560
VERSION     NP_955421.1
DBSOURCE    REFSEQ: accession NM_199389.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Munster-Wandowski,A., Heilmann,H., Bolduan,F., Trimbuch,T.,
            Yanagawa,Y. and Vida,I.
  TITLE     Distinct Localization of SNAP47 Protein in GABAergic and
            Glutamatergic Neurons in the Mouse and the Rat Hippocampus
  JOURNAL   Front Neuroanat 11, 56 (2017)
   PUBMED   28751858
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Jurado,S., Goswami,D., Zhang,Y., Molina,A.J., Sudhof,T.C. and
            Malenka,R.C.
  TITLE     LTP requires a unique postsynaptic SNARE fusion machinery
  JOURNAL   Neuron 77 (3), 542-558 (2013)
   PUBMED   23395379
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Ghiani,C.A., Starcevic,M., Rodriguez-Fernandez,I.A., Nazarian,R.,
            Cheli,V.T., Chan,L.N., Malvar,J.S., de Vellis,J., Sabatti,C. and
            Dell'Angelica,E.C.
  TITLE     The dysbindin-containing complex (BLOC-1) in brain: developmental
            regulation, interaction with SNARE proteins and role in neurite
            outgrowth
  JOURNAL   Mol Psychiatry 15 (2), 115 (2010)
   PUBMED   19546860
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Holt,M., Varoqueaux,F., Wiederhold,K., Takamori,S., Urlaub,H.,
            Fasshauer,D. and Jahn,R.
  TITLE     Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous
            expression
  JOURNAL   J Biol Chem 281 (25), 17076-17083 (2006)
   PUBMED   16621800
  REMARK    GeneRIF: SNAP-47, a novel Qbc-SNARE with ubiquitous expression
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062056.1.
            
            On Jan 12, 2004 this sequence version replaced XP_220560.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062056.1, SRR8487231.37868.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..419
                     /product="synaptosomal-associated protein 47"
                     /note="synaptosomal-associated 47 kDa protein;
                     synaptosomal-associated protein, 47"
                     /calculated_mol_wt=46911
     Region          12..98
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          106..170
                     /region_name="SNARE_SNAP47N"
                     /note="N-terminal SNARE motif of SNAP47; cd15888"
                     /db_xref="CDD:277241"
     Site            order(108,111..116,118..123,125..126,129..130,132..137,
                     139..140,142..144,146..151,153..154,156..158,160..161,
                     163..165,167..168,170)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277241"
     Site            143
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277241"
     Region          359..417
                     /region_name="SNARE_SNAP47C"
                     /note="C-terminal SNARE motif of SNAP47; cd15854"
                     /db_xref="CDD:277207"
     Site            order(363..366,368..370,372..374,376..377,379..384,
                     386..387,389..390,393..394,396..398,400..402,404..405,
                     407..408,411..412,414..415,417)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277207"
     Site            390
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277207"
     CDS             1..419
                     /gene="Snap47"
                     /gene_synonym="RGD735194; SNAP-47"
                     /coded_by="NM_199389.1:129..1388"
                     /db_xref="GeneID:303183"
                     /db_xref="RGD:735194"
ORIGIN      
        1 mssdvrvhtw pcsyyldlek qwlpgkltlt prslkfsvdk aeevlvglpl ssiteirket
       61 slfifsaitv lekgqakhwf sslrpsrnvv fniiehfwre lllsqpgtaa nptspmtrgq
      121 elmglmassq rrmedtakvl hhqgeqldsv mrglekmesd ldvadrllte letpswwpfs
      181 akfwktpvea kprdsvsvap cepfgkegvv irvpavvsqr teshskpgkl tvlvsgleih
      241 dssslllhrf ekedvddikv hspyevsirq rfigkpdvay rlisakmpev ipilevqfsk
      301 kielledalv lrsrgraspa eggcsirhaa srlmgctthq elptggqegq qsqlqkdwpl
      361 lsegeaqelt qilsklkgla ldteaelerq daaldgitva vdratltvdk hnrrmrkll
//
LOCUS       NP_579839                418 aa            linear   ROD 27-APR-2025
DEFINITION  AP-3 complex subunit mu-2 [Rattus norvegicus].
ACCESSION   NP_579839
VERSION     NP_579839.1
DBSOURCE    REFSEQ: accession NM_133305.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Larimore,J., Tornieri,K., Ryder,P.V., Gokhale,A., Zlatic,S.A.,
            Craige,B., Lee,J.D., Talbot,K., Pare,J.F., Smith,Y. and Faundez,V.
  TITLE     The schizophrenia susceptibility factor dysbindin and its
            associated complex sort cargoes from cell bodies to the synapse
  JOURNAL   Mol Biol Cell 22 (24), 4854-4867 (2011)
   PUBMED   21998198
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Nangaku,M., Miyata,T., Suzuki,D., Umezono,T., Hashimoto,T.,
            Wada,T., Yagi,M., Nagano,N., Inagi,R. and Kurokawa,K.
  TITLE     Cloning of rodent megsin revealed its up-regulation in
            mesangioproliferative nephritis
  JOURNAL   Kidney Int 60 (2), 641-652 (2001)
   PUBMED   11473647
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Pevsner,J., Volknandt,W., Wong,B.R. and Scheller,R.H.
  TITLE     Two rat homologs of clathrin-associated adaptor proteins
  JOURNAL   Gene 146 (2), 279-283 (1994)
   PUBMED   8076832
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086993.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086993.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132264, SAMD00155316
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..418
                     /product="AP-3 complex subunit mu-2"
                     /note="adaptor-related protein complex 3, mu 2 subunit;
                     P47B; mu3B-adaptin; HA1 47 kDa subunit homolog 2; golgi
                     adaptor AP-1 47 kDa protein homolog 2; clathrin coat
                     assembly protein AP47 homolog 2; adapter-related protein
                     complex 3 mu-2 subunit; clathrin coat-associated protein
                     AP47 homolog 2; clathrin assembly protein assembly protein
                     complex 1 medium chain homolog 2; adapter-related protein
                     complex 3 subunit mu-2; clathrin assembly protein assembly
                     protein complex 3 mu-2 medium chain"
                     /calculated_mol_wt=46743
     Region          3..141
                     /region_name="AP3_Mu_N"
                     /note="AP-3 complex subunit mu N-terminal domain; cd14837"
                     /db_xref="CDD:341441"
     Site            order(18,21,46..47,55,57,59,71..73,75..77,80,84,110..111,
                     114..115,117..119,121..124,133,135..136)
                     /site_type="other"
                     /note="putative AP-3 beta interface [polypeptide binding]"
                     /db_xref="CDD:341441"
     Region          165..418
                     /region_name="AP_MHD_Cterm"
                     /note="C-terminal domain of adaptor protein (AP) complexes
                     medium mu subunits and its homologs (MHD); cl10970"
                     /db_xref="CDD:472082"
     CDS             1..418
                     /gene="Ap3m2"
                     /coded_by="NM_133305.2:209..1465"
                     /db_xref="GeneID:140667"
                     /db_xref="RGD:70969"
ORIGIN      
        1 mihslflins agdiflekhw ksvvsrsvcd yffeaqerat eaenvppvip tphhyllsvy
       61 rhkiffvavi qtevpplfvi eflhrvvdtf qdyfgvcsep vikdnvvvvy evleemldng
      121 fplatesnil kelikpptil rtvvntitgs tnvgdqlptg qlsvvpwrrt gvkytnneay
      181 fdvveeidai idksgstvta eiqgvidacv kltgmpdltl sfmnprlldd vsfhpcvrfk
      241 rweserilsf ippdgnfrll syhvsaqnlv aipvyvkhsi sfrdsgslgr feitvgpkqt
      301 mgktiegvtv tsqmpkgvln msltpsqgth tfdpvtkmls wdvgkinpqk lpslkgtmgl
      361 qvgaskpden ptinlqfkiq qlaisglkvn rldmygekyk pfkgikymtk agkfqvrt
//
LOCUS       NP_001012350             190 aa            linear   ROD 27-APR-2025
DEFINITION  membrane protein FAM174A precursor [Rattus norvegicus].
ACCESSION   NP_001012350 XP_217476
VERSION     NP_001012350.1
DBSOURCE    REFSEQ: accession NM_001012350.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089835.1.
            
            On Feb 18, 2005 this sequence version replaced XP_217476.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089835.1, CB716000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..190
                     /product="membrane protein FAM174A precursor"
                     /note="membrane protein FAM174A; transmembrane protein
                     157"
                     /calculated_mol_wt=17145
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3101
     Region          10..190
                     /region_name="DUF1180"
                     /note="Protein of unknown function (DUF1180); pfam06679"
                     /db_xref="CDD:429067"
     Site            27
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ7.1)"
     mat_peptide     30..190
                     /product="Membrane protein FAM174A. /id=PRO_0000263652"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ7.1)"
                     /calculated_mol_wt=17145
     Region          37..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ7.1)"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ7.1)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ7.1)"
     Region          168..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ7.1)"
     CDS             1..190
                     /gene="Fam174a"
                     /gene_synonym="Fam174; RGD1309973; Tmem157"
                     /coded_by="NM_001012350.1:64..636"
                     /db_xref="GeneID:301634"
                     /db_xref="RGD:1309973"
ORIGIN      
        1 mptrrgcsgp chflasafvl lllpalnqsv vlpstvprav qeskplepgp rtlsplppgp
       61 taaqprgqaq segagprgae srngsipgaa seadgpegka gesslggsla vspnpsdkpm
      121 tqraltvlvv vsaavlvyfv vrtvrmrrrn rktrrygvld tnienmeltp leqddedddn
      181 tlfdanhprr
//
LOCUS       NP_001019938             586 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 3
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001019938 XP_222607
VERSION     NP_001019938.1
DBSOURCE    REFSEQ: accession NM_001024767.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Rai,A.K., Chen,J.X., Selbach,M. and Pelkmans,L.
  TITLE     Kinase-controlled phase transition of membraneless organelles in
            mitosis
  JOURNAL   Nature 559 (7713), 211-216 (2018)
   PUBMED   29973724
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Kim,K., Cha,J.S., Cho,Y.S., Kim,H., Chang,N., Kim,H.J. and Cho,H.S.
  TITLE     Crystal Structure of Human Dual-Specificity Tyrosine-Regulated
            Kinase 3 Reveals New Structural Features and Insights into its
            Auto-phosphorylation
  JOURNAL   J Mol Biol 430 (10), 1521-1530 (2018)
   PUBMED   29634919
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Wippich,F., Bodenmiller,B., Trajkovska,M.G., Wanka,S., Aebersold,R.
            and Pelkmans,L.
  TITLE     Dual specificity kinase DYRK3 couples stress granule
            condensation/dissolution to mTORC1 signaling
  JOURNAL   Cell 152 (4), 791-805 (2013)
   PUBMED   23415227
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Guo,X., Williams,J.G., Schug,T.T. and Li,X.
  TITLE     DYRK1A and DYRK3 promote cell survival through phosphorylation and
            activation of SIRT1
  JOURNAL   J Biol Chem 285 (17), 13223-13232 (2010)
   PUBMED   20167603
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Wojchowski,D.M., Menon,M.P., Sathyanarayana,P., Fang,J., Karur,V.,
            Houde,E., Kapelle,W. and Bogachev,O.
  TITLE     Erythropoietin-dependent erythropoiesis: New insights and questions
  JOURNAL   Blood Cells Mol Dis 36 (2), 232-238 (2006)
   PUBMED   16524748
  REMARK    Review article
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Li,K., Zhao,S., Karur,V. and Wojchowski,D.M.
  TITLE     DYRK3 activation, engagement of protein kinase A/cAMP response
            element-binding protein, and modulation of progenitor cell survival
  JOURNAL   J Biol Chem 277 (49), 47052-47060 (2002)
   PUBMED   12356771
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Lord,K.A., Creasy,C.L., King,A.G., King,C., Burns,B.M., Lee,J.C.
            and Dillon,S.B.
  TITLE     REDK, a novel human regulatory erythroid kinase
  JOURNAL   Blood 95 (9), 2838-2846 (2000)
   PUBMED   10779429
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097474.1.
            
            On Jun 10, 2005 this sequence version replaced XP_222607.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097474.1, CV115198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132286, SAMD00132299
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..586
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 3 isoform 1"
                     /EC_number="2.7.12.1"
                     /note="dual-specificity tyrosine-(Y)-phosphorylation
                     regulated kinase 3"
                     /calculated_mol_wt=65380
     Region          1..187
                     /region_name="Disordered.
                     /evidence=ECO:0000250|UniProtKB:O43781"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A3.1)"
     Region          142..521
                     /region_name="PKc_DYRK2_3"
                     /note="Catalytic domain of the protein kinases,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinases 2 and 3; cd14224"
                     /db_xref="CDD:271126"
     Site            order(214..218,222,235,237,251,271,287..290,293,295..296,
                     334,336,338..339,341,354,357,366,368..371,373,410)
                     /site_type="active"
                     /db_xref="CDD:271126"
     Site            order(214..218,222,235,237,271,287..290,293,334,336,
                     338..339,341,354)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271126"
     Site            order(251,295,334,336,357,366,368..371,373,410)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271126"
     Site            353..373
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271126"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q922Y0; propagated from
                     UniProtKB/Swiss-Prot (Q4V8A3.1)"
     Region          467..480
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O43781"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8A3.1)"
     CDS             1..586
                     /gene="Dyrk3"
                     /coded_by="NM_001024767.1:119..1879"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304775"
                     /db_xref="RGD:1310924"
ORIGIN      
        1 mggaarergr kdaalpgagl ppqqrrlgdg vydtfmmide tkcppytntl cnpseapvsr
       61 rlnittepft rghtqhfvsg gvmkveqlfq efgsrrtstl qsdgvsnsek sspasqgkss
      121 dslgtvkcsl ssrpskvlpl tpeqalkqyk hhltayekle iisypeiyfv gpnakkrqgv
      181 iggpnnggyd dadgayihvp rdhlayryev lkiigkgsfg qvarvydhkl rqyvalkmvr
      241 nekrfhrqaa eeirilehlk kqdktgsmnv ihmlesftfr nhvcmafell sidlyelikk
      301 nkfqgfsvql vrkfaqsilq sldalhknki ihcdlkpeni llkhhgrsat kvidfgsscf
      361 eyqklytyiq srfyrapeii lgcrystpid iwsfgcilae lltgqplfpg edegdqlacm
      421 mellgmppqk lleqskraky finskglpry csvttqtdgr vvllggrsrr gkkrgppgsk
      481 dwaaalkgcd dylfieflkr clqwdpsarl tpaqalrhpw isksaprplt tdkvsgkrvv
      541 nptnafqglg sklppvvgia sklkanlmse tsgsiplcsv lpklis
//
LOCUS       NP_001020892             742 aa            linear   ROD 27-APR-2025
DEFINITION  collectin-12 [Rattus norvegicus].
ACCESSION   NP_001020892 XP_341575
VERSION     NP_001020892.1
DBSOURCE    REFSEQ: accession NM_001025721.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Toma,V.A., Tigu,A.B., Farcas,A.D., Sevastre,B., Taulescu,M.,
            Gherman,A.M.R., Roman,I., Fischer-Fodor,E. and Parvu,M.
  TITLE     New Aspects Towards a Molecular Understanding of the Allicin
            Immunostimulatory Mechanism via Colec12, MARCO, and SCARB1
            Receptors
  JOURNAL   Int J Mol Sci 20 (15), 3627 (2019)
   PUBMED   31344978
  REMARK    GeneRIF: The molecular docking revealed that
            S-allyl-mercapto-glutathione interacting with Colec12, MARCO (class
            A), and SCARB1 (class B) scavenger receptors in in vitro tests
            demonstrates a direct stimulation of immunoglobulin secretion by
            S-allylmercaptoglutathione (GSSA) in CD19+ B lymphocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Fork,C., Hitzel,J., Nichols,B.J., Tikkanen,R. and Brandes,R.P.
  TITLE     Flotillin-1 facilitates toll-like receptor 3 signaling in human
            endothelial cells
  JOURNAL   Basic Res Cardiol 109 (6), 439 (2014)
   PUBMED   25204797
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Ohtani,K., Suzuki,Y., Eda,S., Kawai,T., Kase,T., Keshi,H.,
            Sakai,Y., Fukuoh,A., Sakamoto,T., Itabe,H., Suzutani,T.,
            Ogasawara,M., Yoshida,I. and Wakamiya,N.
  TITLE     The membrane-type collectin CL-P1 is a scavenger receptor on
            vascular endothelial cells
  JOURNAL   J Biol Chem 276 (47), 44222-44228 (2001)
   PUBMED   11564734
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Nakamura,K., Funakoshi,H., Tokunaga,F. and Nakamura,T.
  TITLE     Molecular cloning of a mouse scavenger receptor with C-type lectin
            (SRCL)(1), a novel member of the scavenger receptor family
  JOURNAL   Biochim Biophys Acta 1522 (1), 53-58 (2001)
   PUBMED   11718900
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097495.1.
            
            On Jul 22, 2005 this sequence version replaced XP_341575.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097495.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..742
                     /product="collectin-12"
                     /note="CL-P1; collectin placenta protein 1; nurse cell
                     scavenger receptor 2"
                     /calculated_mol_wt=81416
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V885.1)"
     Region          85..>307
                     /region_name="PRK11281"
                     /note="mechanosensitive channel MscK; cl46976"
                     /db_xref="CDD:481316"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V885.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V885.1)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4V885.1)"
     Region          439..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V885.1)"
     Region          455..563
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          607..732
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(663,694,696,706,712..713,718..721)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(670,674,697,706..707)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(674,707)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     CDS             1..742
                     /gene="Colec12"
                     /coded_by="NM_001025721.1:88..2316"
                     /db_xref="GeneID:361289"
                     /db_xref="RGD:735039"
ORIGIN      
        1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi illyvlcall titvailgyk
       61 vvekmdtvtd gmetsrqtyd nkliavesdl kklgdqtgkk alstnselst frsdildlrq
      121 qlqeitekts knkdmleklq angdslvdrq sqlketlqnn sflittvnkt lqayngyvtn
      181 lqqdtsvlqg nlqsqmysqn vvimnlnnln ltqvqqrnli tnlqrsvddt slaiqqiknd
      241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnnql ssftgqmdni
      301 ttisqaneqs mkdlqdlhkd tenrtavkfs qleerfqvfe tdivniinni sytahhlrtl
      361 tsnlndvrtt ctdtltrhtd dltslnntlv nirldsislr mqqdmmrsrl dtevanlsvv
      421 meemklvdsk hgqliknfti lqgppgprgp kgdrgsqgpp gptgnkgqkg ekgepgppgp
      481 agergtigpv gppgergskg skgsqgpkgs rgspgkpgpq gpsgdpgppg ppgkdglpgp
      541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgame plalqneptp
      601 asevngcpph wknftdkcyy fsvekeifed aklfcedkss hlvfinsree qqwikkqtmg
      661 reshwigltd seqesewkwl dgtpvdyknw kagqpdnwgs ghgpgedcag liyagqwndf
      721 qcdeinnfic ekereavpss il
//
LOCUS       NP_446238                349 aa            linear   ROD 27-APR-2025
DEFINITION  replication factor C subunit 2 [Rattus norvegicus].
ACCESSION   NP_446238 XP_341063 XP_347154
VERSION     NP_446238.1
DBSOURCE    REFSEQ: accession NM_053786.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Vannier,J.B., Sandhu,S., Petalcorin,M.I., Wu,X., Nabi,Z., Ding,H.
            and Boulton,S.J.
  TITLE     RTEL1 is a replisome-associated helicase that promotes telomere and
            genome-wide replication
  JOURNAL   Science 342 (6155), 239-242 (2013)
   PUBMED   24115439
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Hedglin,M., Kumar,R. and Benkovic,S.J.
  TITLE     Replication clamps and clamp loaders
  JOURNAL   Cold Spring Harb Perspect Biol 5 (4), a010165 (2013)
   PUBMED   23545418
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Li,G.M.
  TITLE     Mechanisms and functions of DNA mismatch repair
  JOURNAL   Cell Res 18 (1), 85-98 (2008)
   PUBMED   18157157
  REMARK    Review article
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Bermudez,V.P., Maniwa,Y., Tappin,I., Ozato,K., Yokomori,K. and
            Hurwitz,J.
  TITLE     The alternative Ctf18-Dcc1-Ctf8-replication factor C complex
            required for sister chromatid cohesion loads proliferating cell
            nuclear antigen onto DNA
  JOURNAL   Proc Natl Acad Sci U S A 100 (18), 10237-10242 (2003)
   PUBMED   12930902
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Chim,S.S., Fung,K., Waye,M.M., Lee,C. and Tsui,S.K.
  TITLE     Expression of replication factor C 40-kDa subunit is down-regulated
            during neonatal development in rat ventricular myocardium
  JOURNAL   J Cell Biochem 78 (4), 533-540 (2000)
   PUBMED   10861850
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Ellison,V. and Stillman,B.
  TITLE     Reconstitution of recombinant human replication factor C (RFC) and
            identification of an RFC subcomplex possessing DNA-dependent ATPase
            activity
  JOURNAL   J Biol Chem 273 (10), 5979-5987 (1998)
   PUBMED   9488738
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082110.1.
            
            On or before Nov 26, 2004 this sequence version replaced
            XP_341063.1, XP_347154.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082110.1, SRR8487227.147001.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..349
                     /product="replication factor C subunit 2"
                     /note="activator 1 subunit C2; replication factor C
                     (activator 1) 2"
                     /calculated_mol_wt=38526
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W4.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P35250; propagated from
                     UniProtKB/Swiss-Prot (Q641W4.1)"
     Region          31..343
                     /region_name="PLN03025"
                     /note="replication factor C subunit; Provisional"
                     /db_xref="CDD:178596"
     Site            158
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35250; propagated from
                     UniProtKB/Swiss-Prot (Q641W4.1)"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35250; propagated from
                     UniProtKB/Swiss-Prot (Q641W4.1)"
     CDS             1..349
                     /gene="Rfc2"
                     /coded_by="NM_053786.1:38..1087"
                     /db_xref="GeneID:116468"
                     /db_xref="RGD:621198"
ORIGIN      
        1 mevqesgsgs aesgtqepsp vpskttghye lpwvekyrpv klneivgned tvsrlevfar
       61 egnvpniiia gppgtgktts ilclarallg palkdavlel nasndrgidv vrnkikmfaq
      121 qkvtlpkgrh kiiildeads mtdgaqqalr rtmeiysktt rfalacnasd kiiepiqsrc
      181 avlrytkltd aqvlsrlmnv iekekvpytd dgleaiifta qgdmrqalnn lqstfsgfgy
      241 insenvfkvc dephpllvke miqhcvdani deaykilahl whlgyspedv ignifrvckt
      301 fpmaeylkle fikeigythm kvaegvnsll qmagllarlc qktmapvas
//
LOCUS       NP_001028879             520 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor GTPase-activating protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001028879 XP_342463
VERSION     NP_001028879.1
DBSOURCE    REFSEQ: accession NM_001033707.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Weimer,C., Beck,R., Eckert,P., Reckmann,I., Moelleken,J.,
            Brugger,B. and Wieland,F.
  TITLE     Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI
            trafficking
  JOURNAL   J Cell Biol 183 (4), 725-735 (2008)
   PUBMED   19015319
  REMARK    GeneRIF: Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in
            COPI trafficking
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC101917.1.
            
            On Sep 25, 2005 this sequence version replaced XP_342463.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101917.1, FQ218185.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..520
                     /product="ADP-ribosylation factor GTPase-activating
                     protein 2"
                     /note="ARF GAP 2; ADP-ribosylation factor GTPase
                     activating protein 2; GTPase-activating protein ZNF289;
                     zinc finger protein 289"
                     /calculated_mol_wt=56425
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Region          5..124
                     /region_name="ArfGap_ArfGap2"
                     /note="Arf1 GTPase-activating protein 2; cd09029"
                     /db_xref="CDD:350086"
     Region          12..470
                     /region_name="PLN03114"
                     /note="ADP-ribosylation factor GTPase-activating protein
                     AGD10; Provisional"
                     /db_xref="CDD:178661"
     Site            order(26,29,46,49,54)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350086"
     Site            order(26,29,46,49)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350086"
     Region          97..520
                     /region_name="Required for interaction with coatomer.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Region          163..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Region          <242..>304
                     /region_name="YqiK"
                     /note="Uncharacterized membrane protein YqiK, contains
                     Band7/PHB/SPFH domain [Function unknown]; COG2268"
                     /db_xref="CDD:441869"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N6H7; propagated from
                     UniProtKB/Swiss-Prot (Q3MID3.1)"
     CDS             1..520
                     /gene="Arfgap2"
                     /gene_synonym="Zfp289"
                     /coded_by="NM_001033707.1:49..1611"
                     /db_xref="GeneID:362162"
                     /db_xref="RGD:1306177"
ORIGIN      
        1 maagpsksei qtlfkrlrai ptnkacfdcg akspswasit ygvflcidcs gvhrslgvhl
       61 sfirstelds nwswlqlrcm qvggnanata ffrqhgclan dantkynsra aqmyrekirq
      121 lgstalarhg tdlwidnmns apshspekkd sdfftehtqa pawdtaatdp sgtqqpalps
      181 essslaqpep gpntdllgts pqaslelkss iigkkkpaaa kkglgakkgl gaqkvsnqsf
      241 teierqaqva eklreqqaad akkqaeesmv asmrlayqel qidrkkeekk lqnlegkkre
      301 qaerlgmglv srssishsvl semqmieqet plsakssrsq ldlfddvgtf asgppkykdn
      361 pfslgetfgs rwdsdaawgm drveekepev tissirpise rttsrreves risglessea
      421 rqkfagakai ssdmffgrev dseyearsrl qqlsgssais ssdlfgdvdg ahgggtvslg
      481 nvlptadiaq fkqgvksvag kmavlangvm nslqdrygsy
//
LOCUS       NP_446328                690 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein M isoform b [Rattus
            norvegicus].
ACCESSION   NP_446328 XP_343181
VERSION     NP_446328.2
DBSOURCE    REFSEQ: accession NM_053876.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Chen,S., Zhang,J., Duan,L., Zhang,Y., Li,C., Liu,D., Ouyang,C.,
            Lu,F. and Liu,X.
  TITLE     Identification of HnRNP M as a novel biomarker for colorectal
            carcinoma by quantitative proteomics
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 306 (5), G394-G403 (2014)
   PUBMED   24381081
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Soteriou,D., Iskender,B., Byron,A., Humphries,J.D.,
            Borg-Bartolo,S., Haddock,M.C., Baxter,M.A., Knight,D.,
            Humphries,M.J. and Kimber,S.J.
  TITLE     Comparative proteomic analysis of supportive and unsupportive
            extracellular matrix substrates for human embryonic stem cell
            maintenance
  JOURNAL   J Biol Chem 288 (26), 18716-18731 (2013)
   PUBMED   23658023
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 690)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 690)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   7  (residues 1 to 690)
  AUTHORS   Bajenova,O.V., Zimmer,R., Stolper,E., Salisbury-Rowswell,J.,
            Nanji,A. and Thomas,P.
  TITLE     Heterogeneous RNA-binding protein M4 is a receptor for
            carcinoembryonic antigen in Kupffer cells
  JOURNAL   J Biol Chem 276 (33), 31067-31073 (2001)
   PUBMED   11406629
REFERENCE   8  (residues 1 to 690)
  AUTHORS   Kafasla,P., Patrinou-Georgoula,M. and Guialis,A.
  TITLE     The 72/74-kDa polypeptides of the 70-110 S large heterogeneous
            nuclear ribonucleoprotein complex (LH-nRNP) represent a discrete
            subset of the hnRNP M protein family
  JOURNAL   Biochem J 350 Pt 2 (Pt 2), 495-503 (2000)
   PUBMED   10947964
REFERENCE   9  (residues 1 to 690)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   10 (residues 1 to 690)
  AUTHORS   Cuervo,A.M., Dice,J.F. and Knecht,E.
  TITLE     A population of rat liver lysosomes responsible for the selective
            uptake and degradation of cytosolic proteins
  JOURNAL   J Biol Chem 272 (9), 5606-5615 (1997)
   PUBMED   9038169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV774465.1, U32577.2 and BC088317.1.
            
            On Oct 12, 2007 this sequence version replaced NP_446328.1.
            
            Transcript Variant: This variant (2) lacks an in-frame segment in
            the coding region, compared to variant 1, which results in shorter
            protein (isoform b) when compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U32577.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..690
                     /product="heterogeneous nuclear ribonucleoprotein M
                     isoform b"
                     /note="hnRNP M; M4 protein"
                     /calculated_mol_wt=73591
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62826.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Region          40..69
                     /region_name="HnRNP_M_NLS"
                     /note="HnRNP M nuclear localization signal; pfam11532"
                     /db_xref="CDD:463289"
     Region          71..146
                     /region_name="RRM1_hnRNPM"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12657"
                     /db_xref="CDD:410058"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            133
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9D0E1; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Region          164..239
                     /region_name="RRM2_hnRNPM"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12659"
                     /db_xref="CDD:410060"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            237
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Region          360..568
                     /region_name="27 X 6 AA repeats of
                     [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62826.4)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            456
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Region          614..690
                     /region_name="RRM3_hnRNPM"
                     /note="RNA recognition motif 3 (RRM3) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12661"
                     /db_xref="CDD:410062"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            632
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0E1; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            658
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52272; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62826.4)"
     CDS             1..690
                     /gene="Hnrnpm"
                     /gene_synonym="Hnrpm; Hnrpm4"
                     /coded_by="NM_053876.2:22..2094"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:116655"
                     /db_xref="RGD:620369"
ORIGIN      
        1 maagveaaae vaatepkmee esgapcvpsg ngapvpkgee rptqnekrke knikrggnrf
       61 epyanptkry rafitnipfd vkwqslkdlv kekvgevtyv ellmdaegks rgcavvefkm
      121 eesmkkaaev lnkhslsgrp lkvkedpdge harramqkag rlgstvfvan ldykvgwkkl
      181 kevfsmagvv vradiledkd gksrgigtvt feqsieavqa ismfngqllf drpmhvkmde
      241 ralpkgdffp perpqqlphg lggigmglgp ggqpidanhl nkgigmgnlg pagmgmegig
      301 fginkiggme gpfgggmenm grfgsgmnmg rineilsnal krgeiiakqg gggaggsvpg
      361 iermgpgidr isgagmermg aglghgmdrv gseiermglv mdrmgsverm gsgiermgpl
      421 gldhmassie rmgqtmerig sgvermgagm gfglermaap idrvgqtier mgsgvermgp
      481 aiermglsmd rmvptgmgag lermgpvmdr matglermga nnlermgler mganslermg
      541 lermgansle rmgpamgpal gagiermgla mggaggasfd raiemergnf ggsfagsfgg
      601 agghapgvar kacqifvrnl pfdftwkmlk dkfnecghvl yadikmengk skgcgvvkfe
      661 spevaeracr mmngmklsgr eidvridrna
//
LOCUS       NP_001019527             418 aa            linear   ROD 27-APR-2025
DEFINITION  testis-specific H1 histone [Rattus norvegicus].
ACCESSION   NP_001019527 XP_576337
VERSION     NP_001019527.1
DBSOURCE    REFSEQ: accession NM_001024356.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Shalini,V., Bhaduri,U., Ravikkumar,A.C., Rengarajan,A. and
            Satyanarayana,R.M.R.
  TITLE     Genome-wide occupancy reveals the localization of H1T2 (H1fnt) to
            repeat regions and a subset of transcriptionally active chromatin
            domains in rat spermatids
  JOURNAL   Epigenetics Chromatin 14 (1), 3 (2021)
   PUBMED   33407810
  REMARK    GeneRIF: Genome-wide occupancy reveals the localization of H1T2
            (H1fnt) to repeat regions and a subset of transcriptionally active
            chromatin domains in rat spermatids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Tang,M.C., Jacobs,S.A., Mattiske,D.M., Soh,Y.M., Graham,A.N.,
            Tran,A., Lim,S.L., Hudson,D.F., Kalitsis,P., O'Bryan,M.K.,
            Wong,L.H. and Mann,J.R.
  TITLE     Contribution of the two genes encoding histone variant h3.3 to
            viability and fertility in mice
  JOURNAL   PLoS Genet 11 (2), e1004964 (2015)
   PUBMED   25675407
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 418)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Govin,J., Escoffier,E., Rousseaux,S., Kuhn,L., Ferro,M.,
            Thevenon,J., Catena,R., Davidson,I., Garin,J., Khochbin,S. and
            Caron,C.
  TITLE     Pericentric heterochromatin reprogramming by new histone variants
            during mouse spermiogenesis
  JOURNAL   J Cell Biol 176 (3), 283-294 (2007)
   PUBMED   17261847
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Catena,R., Ronfani,L., Sassone-Corsi,P. and Davidson,I.
  TITLE     Changes in intranuclear chromatin architecture induce bipolar
            nuclear localization of histone variant H1T2 in male haploid
            spermatids
  JOURNAL   Dev Biol 296 (1), 231-238 (2006)
   PUBMED   16765935
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Martianov,I., Brancorsini,S., Catena,R., Gansmuller,A., Kotaja,N.,
            Parvinen,M., Sassone-Corsi,P. and Davidson,I.
  TITLE     Polar nuclear localization of H1T2, a histone H1 variant, required
            for spermatid elongation and DNA condensation during spermiogenesis
  JOURNAL   Proc Natl Acad Sci U S A 102 (8), 2808-2813 (2005)
   PUBMED   15710904
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085950.1.
            
            On May 27, 2005 this sequence version replaced XP_576337.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC085950.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..418
                     /product="testis-specific H1 histone"
                     /note="histone H1t2; haploid germ cell-specific nuclear
                     protein 1; H1 histone family, member N, testis-specific;
                     histone H1.7"
                     /calculated_mol_wt=46942
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG3.1)"
     Region          114..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG3.1)"
     Region          344..418
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG3.1)"
     CDS             1..418
                     /gene="H1f7"
                     /gene_synonym="H1-7; H1fnt"
                     /coded_by="NM_001024356.1:26..1282"
                     /db_xref="GeneID:500928"
                     /db_xref="RGD:1560024"
ORIGIN      
        1 maeaaqptge sqgaeltiqi qqpveralrt pvrrgaqsvl rvsqlllrai aghqrltlaa
       61 lkkelgnagy evrrkisshq agdstrseky tllrvsgsda agyfrvwkis kprrkaprsr
      121 ltlgshshgk tvlksprplr prsrrkaakk arevwrrkar alkarsrrar slarsmvrsr
      181 assrassrar srarsrarsr arsrarsras srarssarss arssarssvr ssvrssarss
      241 arssirsrar srartrarsr akdlvrskar eqartrareq ahararthdc vrakaqeyvr
      301 akeqqyvsak eqeyvrtkeq ecakareqmr igameearik aidnrvqttm edtspwstde
      361 mrsrtkpree krqeperpvk qtnqkpavvk vdnapsrqgk tctksstksg hpgcsgts
//
LOCUS       NP_001009455             926 aa            linear   ROD 27-APR-2025
DEFINITION  armadillo repeat-containing protein 5 [Rattus norvegicus].
ACCESSION   NP_001009455 XP_341934
VERSION     NP_001009455.1
DBSOURCE    REFSEQ: accession NM_001009455.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Assie,G., Libe,R., Espiard,S., Rizk-Rabin,M., Guimier,A.,
            Luscap,W., Barreau,O., Lefevre,L., Sibony,M., Guignat,L.,
            Rodriguez,S., Perlemoine,K., Rene-Corail,F., Letourneur,F.,
            Trabulsi,B., Poussier,A., Chabbert-Buffet,N., Borson-Chazot,F.,
            Groussin,L., Bertagna,X., Stratakis,C.A., Ragazzon,B. and
            Bertherat,J.
  TITLE     ARMC5 mutations in macronodular adrenal hyperplasia with Cushing's
            syndrome
  JOURNAL   N Engl J Med 369 (22), 2105-2114 (2013)
   PUBMED   24283224
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087086.1.
            
            On Jan 7, 2005 this sequence version replaced XP_341934.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087086.1, SRR8487231.50594.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..926
                     /product="armadillo repeat-containing protein 5"
                     /calculated_mol_wt=96454
     Region          82..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          139..179
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          142..179
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          181..221
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          185..219
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          223..263
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          267..306
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          307..354
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C12; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          355..399
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          401..440
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          467..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP9.1)"
     Region          744..839
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     CDS             1..926
                     /gene="Armc5"
                     /coded_by="NM_001009455.1:208..2988"
                     /db_xref="GeneID:361653"
                     /db_xref="RGD:1306553"
ORIGIN      
        1 maaarpaltd slsfclaqlt aaagegpggg kdpatnetal grvllalrtr hikaaegier
       61 frargglrpl vallrrtaaa gpapsqaasg sappsvasag sspgpapaae spltlsapmr
      121 lrktldlals ilancctega crsevrrigg ilplvtilqc vridsiqnrt aralgnlame
      181 pescgdihsa gavpflvesl tacqdsqclq sivralrnla dspqhrlala qqgavrplae
      241 llatapdpal tsalvralle lsrgcsraca eqlslggglg plvslashpk raireaaili
      301 lanlcaqglv rpalgnaggv evllgelrrr rgpsgsssas qqplvravcl lcreainrar
      361 lrdagglell mgllqdpgas awhprvvaal vgflydtgal gklqalglvp llarqlcgea
      421 geeeeegvea aswdfpeert sgqpeggsfr slrlwliseg yaagpgdisp dwspercpmp
      481 epsesvsptp gqtsmstprt lrklgrvpaa tteepwgqeg pallllsrfs qapdpsgalv
      541 tgpalcglla yvtgapgppn pralrilarl tcnpacleaf vrsygaallr awlvlgvspd
      601 dwpvpharpv hrsqhrelge mllqnltvqa espfgvgalt hlllsgsped rvacaltvpf
      661 icrkptlwrr llldqgglrl lltaltqpap hplflffaad slsclqglvs psaspvplpd
      721 lpleldspsp clykpllgpa papapdlhfv ldsglqlpaq raasaaaspf frallsgsfa
      781 eaqmnlvplr glspsaawpv lhhlhgcrgc gaalgpippp gqpllgskae ealeaagrfl
      841 lpaleeelee avgrihlspq ggpesvgevf rlgrprlaah carwtlepgq cprkralalt
      901 glveaageea gplteallav vmgves
//
LOCUS       NP_058801                468 aa            linear   ROD 27-APR-2025
DEFINITION  bone morphogenetic protein 3 precursor [Rattus norvegicus].
ACCESSION   NP_058801
VERSION     NP_058801.1
DBSOURCE    REFSEQ: accession NM_017105.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Song,B., Li,X., Xu,Q., Yin,S., Wu,S., Meng,X., Huang,C. and Li,J.
  TITLE     Inhibition of BMP3 increases the inflammatory response of
            fibroblast-like synoviocytes in rheumatoid arthritis
  JOURNAL   Aging (Albany NY) 12 (12), 12305-12323 (2020)
   PUBMED   32568738
  REMARK    GeneRIF: Inhibition of BMP3 increases the inflammatory response of
            fibroblast-like synoviocytes in rheumatoid arthritis.
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Yamashita,K., Mikawa,S. and Sato,K.
  TITLE     BMP3 expression in the adult rat CNS
  JOURNAL   Brain Res 1643, 35-50 (2016)
   PUBMED   27130896
  REMARK    GeneRIF: Data indicate that bone morphogenetic protein-3 (BMP3) is
            widely expressed throughout the adult central nervous system, and
            its abundant expression in the adult brain strongly supports the
            idea that BMP3 plays important roles in the adult brain.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Grgurevic,L., Macek,B., Healy,D.R., Brault,A.L., Erjavec,I.,
            Cipcic,A., Grgurevic,I., Rogic,D., Galesic,K., Brkljacic,J.,
            Stern-Padovan,R., Paralkar,V.M. and Vukicevic,S.
  TITLE     Circulating bone morphogenetic protein 1-3 isoform increases renal
            fibrosis
  JOURNAL   J Am Soc Nephrol 22 (4), 681-692 (2011)
   PUBMED   21415150
  REMARK    GeneRIF: Circulating bone morphogenetic protein 1-3 isoform
            increases renal fibrosis.
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Nahar,N.N., Missana,L.R., Garimella,R., Tague,S.E. and
            Anderson,H.C.
  TITLE     Matrix vesicles are carriers of bone morphogenetic proteins (BMPs),
            vascular endothelial growth factor (VEGF), and noncollagenous
            matrix proteins
  JOURNAL   J Bone Miner Metab 26 (5), 514-519 (2008)
   PUBMED   18758911
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Takahashi,H. and Ikeda,T.
  TITLE     Transcripts for two members of the transforming growth factor-beta
            superfamily BMP-3 and BMP-7 are expressed in developing rat embryos
  JOURNAL   Dev Dyn 207 (4), 439-449 (1996)
   PUBMED   8950518
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Takao,M., Hino,J., Takeshita,N., Konno,Y., Nishizawa,T., Matsuo,H.
            and Kangawa,K.
  TITLE     Identification of rat bone morphogenetic protein-3b (BMP-3b), a new
            member of BMP-3
  JOURNAL   Biochem Biophys Res Commun 219 (2), 656-662 (1996)
   PUBMED   8605043
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Chen,D., Feng,J.Q., Feng,M., Harris,M.A., Mahy,P., Mundy,G.R. and
            Harris,S.E.
  TITLE     Sequence and expression of bone morphogenetic protein 3 mRNA in
            prolonged cultures of fetal rat calvarial osteoblasts and in rat
            prostate adenocarcinoma PA III cells
  JOURNAL   DNA Cell Biol 14 (3), 235-239 (1995)
   PUBMED   7880444
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Yamaji,N., Celeste,A.J., Thies,R.S., Song,J.J., Bernier,S.M.,
            Goltzman,D., Lyons,K.M., Nove,J., Rosen,V. and Wozney,J.M.
  TITLE     A mammalian serine/threonine kinase receptor specifically binds
            BMP-2 and BMP-4
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1944-1951 (1994)
   PUBMED   7811286
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Ohta,S., Hiraki,Y., Shigeno,C., Suzuki,F., Kasai,R., Ikeda,T.,
            Kohno,H., Lee,K., Kikuchi,H., Konishi,J. et al.
  TITLE     Bone morphogenetic proteins (BMP-2 and BMP-3) induce the late phase
            expression of the proto-oncogene c-fos in murine osteoblastic
            MC3T3-E1 cells
  JOURNAL   FEBS Lett 314 (3), 356-360 (1992)
   PUBMED   1468569
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D63860.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D63860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..468
                     /product="bone morphogenetic protein 3 precursor"
                     /note="BMP-3"
                     /calculated_mol_wt=50383
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2311
     Region          27..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49002.1)"
     Region          46..>203
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Region          72..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49002.1)"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49002.1)"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49002.1)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49002.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49002.1)"
     Region          316..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49002.1)"
     mat_peptide     359..468
                     /product="Bone morphogenetic protein 3.
                     /id=PRO_0000033841"
                     /note="propagated from UniProtKB/Swiss-Prot (P49002.1)"
                     /calculated_mol_wt=12381
     Region          359..468
                     /region_name="TGF_beta_BMP3"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in bone morphogenetic protein 3 (BMP-3) and
                     similar proteins; cd19393"
                     /db_xref="CDD:381663"
     Site            order(371,373,377..378,380,390,392..394,411..412,415..416,
                     418..419,422,425,427..429,432,434..435,438,458..460,462,
                     468)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381663"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49002.1)"
     CDS             1..468
                     /gene="Bmp3"
                     /gene_synonym="PBMP3"
                     /coded_by="NM_017105.1:605..2011"
                     /db_xref="GeneID:25667"
                     /db_xref="RGD:2212"
ORIGIN      
        1 magargllcl wlgcfclnla qgqrpnlhlp glrgtessdr mtgggpspdl rphdkvsehm
       61 lwlydrysgs nraqatrtpg sqlpgpqplr ggntvrsfra aaagtlqrkg lhtfnltslt
      121 ksenilsatl yfyigelvnt svncpesqgc shdsqrqhiq idlsawtlqs nqsqllghls
      181 vdtakpyrds mswlskditq llrkakqdee fligfnitsr ahelpkrmll fpepyilvya
      241 ndaaicepes vvsslqrhrd ftagtvprld shvrealsve rrkkrstgil lplqnnelpg
      301 aeyqykeagv weerkpyksl qtqppeksrs kkkqrkgphq kgqtlqfdeq tlkkarrkqw
      361 ieprncarry lkvdfadigw sewiispksf dayycsgacq fpmpkslkps nhatiqsivr
      421 avgvvsgipe pccvpekmss lsilffdenk nvvlkvypnm tvdscacr
//
LOCUS       NP_001020214             547 aa            linear   ROD 27-APR-2025
DEFINITION  inositol 1,4,5-trisphosphate receptor-interacting protein-like 1
            precursor [Rattus norvegicus].
ACCESSION   NP_001020214 XP_575230
VERSION     NP_001020214.1
DBSOURCE    REFSEQ: accession NM_001025043.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082013.1.
            
            On Jun 25, 2005 this sequence version replaced XP_575230.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082013.1, CK469179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676789 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..547
                     /product="inositol 1,4,5-trisphosphate
                     receptor-interacting protein-like 1 precursor"
                     /note="inositol 1,4,5-triphosphate receptor-interacting
                     protein-like 1; inositol 1,4,5-trisphosphate receptor
                     interacting protein-like 1"
                     /calculated_mol_wt=60760
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H52.1)"
                     /calculated_mol_wt=1806
     mat_peptide     17..547
                     /product="Inositol 1,4,5-trisphosphate
                     receptor-interacting protein-like 1. /id=PRO_0000320568"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H52.1)"
                     /calculated_mol_wt=60760
     Region          <26..>65
                     /region_name="MAT1"
                     /note="CDK-activating kinase assembly factor MAT1;
                     pfam06391"
                     /db_xref="CDD:461894"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H52.1)"
     Region          413..514
                     /region_name="Mab-21_C"
                     /note="Mab-21 protein HhH/H2TH-like domain; pfam20266"
                     /db_xref="CDD:466416"
     CDS             1..547
                     /gene="Itpripl1"
                     /coded_by="NM_001025043.1:204..1847"
                     /db_xref="GeneID:499885"
                     /db_xref="RGD:1564158"
ORIGIN      
        1 mavisllfla vmyvvhhplm vsdrmdldtl arsrqlekrm seemrqleie feersraaee
       61 kqkaenfwrg dtsndqlvlg kkdmrwpfqa sgqdggplgw mlgnlwnagl fclflifell
      121 rqnmqhepaf essseeeeee irvvpvssyt wlsgfpsqea lesfykhyiq nairdlpctc
      181 efvesfvddl ieacrvlsrr eahpqledcl gigaafekwg tlhetqkfdv lvpivppqgt
      241 mfilemrdpt lgrrcgcvkv dsecvcknek llgdvlclvh hrdhsamlsk ctssikaalc
      301 tsshldvykt vqwfrnmvsn awalvahkyd fkltlppstt tcklrldyrs grslsislvl
      361 gvqredtlvy lvsqapereq ftsvdwpesf aacehlflkl vgrfapdntc hlkclqiils
      421 lqdhqtlppg asrpiltsyh fktalmhlll rlpltdwqhr mlsqrlqdll wflgrslqqr
      481 slhhflignt hlpltipipk afrnaepvnl fqhlvlnpva hsqaveefhn llaqvktlpc
      541 splaggl
//
LOCUS       NP_001032881              99 aa            linear   ROD 27-APR-2025
DEFINITION  small integral membrane protein 14 [Rattus norvegicus].
ACCESSION   NP_001032881 XP_344242
VERSION     NP_001032881.1
DBSOURCE    REFSEQ: accession NM_001037792.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Jun,M.H., Jun,Y.W., Kim,K.H., Lee,J.A. and Jang,D.J.
  TITLE     Characterization of the cellular localization of C4orf34 as a novel
            endoplasmic reticulum resident protein
  JOURNAL   BMB Rep 47 (10), 563-568 (2014)
   PUBMED   24499674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100271.1.
            
            On Dec 16, 2005 this sequence version replaced XP_344242.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100271.1, FQ229969.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..99
                     /product="small integral membrane protein 14"
                     /note="uncharacterized protein C4orf34 homolog"
                     /calculated_mol_wt=10553
     Region          3..97
                     /region_name="DUF2615"
                     /note="Protein of unknown function (DUF2615); pfam11027"
                     /db_xref="CDD:402563"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498C7.1)"
     Region          77..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498C7.1)"
     CDS             1..99
                     /gene="Smim14"
                     /gene_synonym="RGD1311122"
                     /coded_by="NM_001037792.1:126..425"
                     /db_xref="GeneID:364154"
                     /db_xref="RGD:1311122"
ORIGIN      
        1 maeggfdpce cicshehamr rlinllrqsq syctdteclr elpgpsgdsg isitvilmaw
       61 mviavllfll rppnlrgssl pgkpssphsg qdppappvd
//
LOCUS       NP_001014066             185 aa            linear   ROD 27-APR-2025
DEFINITION  TRAF-interacting protein with FHA domain-containing protein A
            [Rattus norvegicus].
ACCESSION   NP_001014066 XP_227712
VERSION     NP_001014066.1
DBSOURCE    REFSEQ: accession NM_001014044.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Zhou,P., She,Y., Dong,N., Li,P., He,H., Borio,A., Wu,Q., Lu,S.,
            Ding,X., Cao,Y., Xu,Y., Gao,W., Dong,M., Ding,J., Wang,D.C.,
            Zamyatina,A. and Shao,F.
  TITLE     Alpha-kinase 1 is a cytosolic innate immune receptor for bacterial
            ADP-heptose
  JOURNAL   Nature 561 (7721), 122-126 (2018)
   PUBMED   30111836
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Zimmermann,S., Pfannkuch,L., Al-Zeer,M.A., Bartfeld,S., Koch,M.,
            Liu,J., Rechner,C., Soerensen,M., Sokolova,O., Zamyatina,A.,
            Kosma,P., Maurer,A.P., Glowinski,F., Pleissner,K.P., Schmid,M.,
            Brinkmann,V., Karlas,A., Naumann,M., Rother,M., Machuy,N. and
            Meyer,T.F.
  TITLE     ALPK1- and TIFA-Dependent Innate Immune Response Triggered by the
            Helicobacter pylori Type IV Secretion System
  JOURNAL   Cell Rep 20 (10), 2384-2395 (2017)
   PUBMED   28877472
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Milivojevic,M., Dangeard,A.S., Kasper,C.A., Tschon,T.,
            Emmenlauer,M., Pique,C., Schnupf,P., Guignot,J. and Arrieumerlou,C.
  TITLE     ALPK1 controls TIFA/TRAF6-dependent innate immunity against
            heptose-1,7-bisphosphate of gram-negative bacteria
  JOURNAL   PLoS Pathog 13 (2), e1006224 (2017)
   PUBMED   28222186
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Gaudet,R.G., Sintsova,A., Buckwalter,C.M., Leung,N., Cochrane,A.,
            Li,J., Cox,A.D., Moffat,J. and Gray-Owen,S.D.
  TITLE     INNATE IMMUNITY. Cytosolic detection of the bacterial metabolite
            HBP activates TIFA-dependent innate immunity
  JOURNAL   Science 348 (6240), 1251-1255 (2015)
   PUBMED   26068852
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Huang,C.C., Weng,J.H., Wei,T.Y., Wu,P.Y., Hsu,P.H., Chen,Y.H.,
            Wang,S.C., Qin,D., Hung,C.C., Chen,S.T., Wang,A.H., Shyy,J.Y. and
            Tsai,M.D.
  TITLE     Intermolecular binding between TIFA-FHA and TIFA-pT mediates tumor
            necrosis factor alpha stimulation and NF-kappaB activation
  JOURNAL   Mol Cell Biol 32 (14), 2664-2673 (2012)
   PUBMED   22566686
  REMARK    Erratum:[Mol Cell Biol. 2012 Sep;32(18):3800]
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Kanamori,M., Suzuki,H., Saito,R., Muramatsu,M. and Hayashizaki,Y.
  TITLE     T2BP, a novel TRAF2 binding protein, can activate NF-kappaB and
            AP-1 without TNF stimulation
  JOURNAL   Biochem Biophys Res Commun 290 (3), 1108-1113 (2002)
   PUBMED   11798190
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083765.1.
            
            On Apr 20, 2005 this sequence version replaced XP_227712.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083765.1, DN933168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132295, SAMD00132301
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..185
                     /product="TRAF-interacting protein with FHA
                     domain-containing protein A"
                     /note="TRAF2-binding protein; Traf2 binding protein"
                     /calculated_mol_wt=21417
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96CG3; propagated from
                     UniProtKB/Swiss-Prot (Q5XIB9.1)"
     Region          13..147
                     /region_name="FHA_TIFA"
                     /note="forkhead associated (FHA) domain found in
                     TRAF-interacting protein with FHA domain-containing
                     protein A (TIFA) and similar proteins; cd22714"
                     /db_xref="CDD:438766"
     Site            order(52..54,62,64..65,67..68,95)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438766"
     CDS             1..185
                     /gene="Tifa"
                     /gene_synonym="Ab2-389; T2bp"
                     /coded_by="NM_001014044.1:278..835"
                     /db_xref="GeneID:310877"
                     /db_xref="RGD:1359151"
ORIGIN      
        1 mstfedadte etvtclqmti yhpgqlqsgi fksirfcske kfpsievvkf grnsnmcqyt
       61 fqdkqvsrvq falqpfkqfn ssvlsfeikn mskktslmvd nqelgylnkm dlpykcmlrf
      121 geyqfllqke dgesvesfet qfilsprpll qennwptqsp ipedgvyssy fthrsspaem
      181 denel
//
LOCUS       NP_001012060             355 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF146 [Rattus norvegicus].
ACCESSION   NP_001012060 XP_217722
VERSION     NP_001012060.2
DBSOURCE    REFSEQ: accession NM_001012060.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Mu,Q., Zhou,H., Xu,Y., He,Q., Luo,X., Zhang,W. and Li,H.
  TITLE     NPD1 inhibits excessive autophagy by targeting RNF146 and
            wnt/beta-catenin pathway in cerebral ischemia-reperfusion injury
  JOURNAL   J Recept Signal Transduct Res 40 (5), 456-463 (2020)
   PUBMED   32326811
  REMARK    GeneRIF: NPD1 inhibits excessive autophagy by targeting RNF146 and
            wnt/beta-catenin pathway in cerebral ischemia-reperfusion injury.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Yang,X., Cheng,J., Gao,Y., Ding,J. and Ni,X.
  TITLE     Downregulation of Iduna is associated with AIF nuclear
            translocation in neonatal brain after hypoxia-ischemia
  JOURNAL   Neuroscience 346, 74-80 (2017)
   PUBMED   28108258
  REMARK    GeneRIF: Results suggest that apoptosis-inducing factor nuclear
            translocation and neuronal cell death are associated with Iduna
            loss after severe hypoxic-ischemic in the immature brain.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Gero,D. and Szabo,C.
  TITLE     Salvage of nicotinamide adenine dinucleotide plays a critical role
            in the bioenergetic recovery of post-hypoxic cardiomyocytes
  JOURNAL   Br J Pharmacol 172 (20), 4817-4832 (2015)
   PUBMED   26218637
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Gero,D., Szoleczky,P., Chatzianastasiou,A., Papapetropoulos,A. and
            Szabo,C.
  TITLE     Modulation of poly(ADP-ribose) polymerase-1 (PARP-1)-mediated
            oxidative cell injury by ring finger protein 146 (RNF146) in
            cardiac myocytes
  JOURNAL   Mol Med 20 (1), 313-328 (2014)
   PUBMED   24842055
  REMARK    GeneRIF: Modulation of PARP-1-mediated oxidative cell injury by
            ring finger protein 146 (RNF146) in cardiac myocytes
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   7  (residues 1 to 355)
  AUTHORS   von Rotz,R.C., Kins,S., Hipfel,R., von der Kammer,H. and
            Nitsch,R.M.
  TITLE     The novel cytosolic RING finger protein dactylidin is up-regulated
            in brains of patients with Alzheimer's disease
  JOURNAL   Eur J Neurosci 21 (5), 1289-1298 (2005)
   PUBMED   15813938
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083675.1 and CK845087.1.
            
            On Oct 30, 2007 this sequence version replaced NP_001012060.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083675.1, CV105582.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..355
                     /product="E3 ubiquitin-protein ligase RNF146"
                     /EC_number="2.3.2.27"
                     /note="iduna; RING-type E3 ubiquitin transferase RNF146"
                     /calculated_mol_wt=38485
     Region          37..86
                     /region_name="RING-HC_RNF146"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 146 (RNF146) and similar proteins; cd16546"
                     /db_xref="CDD:438208"
     Site            order(40..41,43,72,74..75)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438208"
     Region          106..178
                     /region_name="WWE"
                     /note="Domain in Deltex and TRIP12 homologues. Possibly
                     involved in regulation of ubiquitin-mediated proteolysis;
                     smart00678"
                     /db_xref="CDD:128922"
     CDS             1..355
                     /gene="Rnf146"
                     /coded_by="NM_001012060.2:146..1213"
                     /db_xref="GeneID:308051"
                     /db_xref="RGD:1306482"
ORIGIN      
        1 memmagcgei dhslnmlptn kkasetcsnt apsltvpeca iclqtcvhpv slpckhvfcy
       61 lcvkgaswlg krcalcrqei pedfldkptl lspeelkaas rgngeyvwyy egrngwwqyd
      121 ertsreleda fskgkkntem liagflyvad lenmvqyrrn ehgrrrkikr diidipkkgv
      181 aglrldcdsn tvnlaressa dgadsgsaht gasvqlpvps strpltsvdg qltspvtpsp
      241 dagasledsf ahlqlsgdsi aershrgege edhespssgr vpdtsteete sdassdieda
      301 pvvvaqhslt qqrllvssan qtvaersdrp vagggtmsvn vrsrrpdgqc tvtev
//
LOCUS       NP_058896                302 aa            linear   ROD 27-APR-2025
DEFINITION  tissue factor pathway inhibitor isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_058896
VERSION     NP_058896.1
DBSOURCE    REFSEQ: accession NM_017200.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Muto,M., Chakraborty,D., Varberg,K.M., Moreno-Irusta,A., Iqbal,K.,
            Scott,R.L., McNally,R.P., Choudhury,R.H., Aplin,J.D., Okae,H.,
            Arima,T., Matsumoto,S., Ema,M., Mast,A.E., Grundberg,E. and
            Soares,M.J.
  TITLE     Intersection of regulatory pathways controlling hemostasis and
            hemochorial placentation
  JOURNAL   Proc Natl Acad Sci U S A 118 (50) (2021)
   PUBMED   34876522
  REMARK    GeneRIF: Intersection of regulatory pathways controlling hemostasis
            and hemochorial placentation.
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Smith,S.A., Travers,R.J. and Morrissey,J.H.
  TITLE     How it all starts: Initiation of the clotting cascade
  JOURNAL   Crit Rev Biochem Mol Biol 50 (4), 326-336 (2015)
   PUBMED   26018600
  REMARK    Review article
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Parunov,L.A., Soshitova,N.P., Fadeeva,O.A., Balandina,A.N.,
            Kopylov,K.G., Kumskova,M.A., Gilbert,J.C., Schaub,R.G.,
            McGinness,K.E., Ataullakhanov,F.I. and Panteleev,M.A.
  TITLE     Drug-drug interaction of the anti-TFPI aptamer BAX499 and factor
            VIII: studies of spatial dynamics of fibrin clot formation in
            hemophilia A
  JOURNAL   Thromb Res 133 (1), 112-119 (2014)
   PUBMED   24263002
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Ogiwara,K., Nogami,K., Matsumoto,T. and Shima,M.
  TITLE     Tissue factor pathway inhibitor in activated prothrombin complex
            concentrates (aPCC) moderates the effectiveness of therapy in some
            severe hemophilia A patients with inhibitor
  JOURNAL   Int J Hematol 99 (5), 577-587 (2014)
   PUBMED   24687919
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Mukai,Y. and Sato,S.
  TITLE     Effect of nitric oxide deficiency on tissue-type plasminogen
            activator expression in the umbilical cord in a pregnancy-induced
            hypertension rat model
  JOURNAL   Pregnancy Hypertens 2 (1), 53-58 (2012)
   PUBMED   26104991
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Elsayed,Y.A., Nakagawa,K., Kamikubo,Y.I., Enjyoji,K.I., Kato,H. and
            Sueishi,K.
  TITLE     Effects of recombinant human tissue factor pathway inhibitor on
            thrombus formation and its in vivo distribution in a rat DIC model
  JOURNAL   Am J Clin Pathol 106 (5), 574-583 (1996)
   PUBMED   8929465
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Saito,M., Morishita,E., Asakura,H., Jokaji,H., Uotani,C.,
            Kumabashiri,I., Yamazaki,M., Aoshima,K. and Matsuda,T.
  TITLE     [Analysis of behaviors of plasma tissue factor and tissue factor
            pathway inhibitor in patients with various diseases]
  JOURNAL   Rinsho Ketsueki 37 (9), 794-798 (1996)
   PUBMED   8914465
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Kobayashi,M., Wada,H., Wakita,Y., Shimura,M., Nakase,T.,
            Hiyoyama,K., Nagaya,S., Minami,N., Nakano,T. and Shiku,H.
  TITLE     Decreased plasma tissue factor pathway inhibitor levels in patients
            with thrombotic thrombocytopenic purpura
  JOURNAL   Thromb Haemost 73 (1), 10-14 (1995)
   PUBMED   7740478
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Bregengard,C., Nordfang,O., Wildgoose,P., Svendsen,O., Hedner,U.
            and Diness,V.
  TITLE     The effect of two-domain tissue factor pathway inhibitor on
            endotoxin-induced disseminated intravascular coagulation in rabbits
  JOURNAL   Blood Coagul Fibrinolysis 4 (5), 699-706 (1993)
   PUBMED   8292719
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Enjyoji,K., Emi,M., Mukai,T. and Kato,H.
  TITLE     cDNA cloning and expression of rat tissue factor pathway inhibitor
            (TFPI)
  JOURNAL   J Biochem 111 (5), 681-687 (1992)
   PUBMED   1639767
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D10926.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D10926.1, SRR8487231.148988.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676809 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..302
                     /product="tissue factor pathway inhibitor isoform 1
                     precursor"
                     /note="EPI; LACI; extrinsic pathway inhibitor;
                     lipoprotein-associated coagulation inhibitor"
                     /calculated_mol_wt=31432
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3140
     mat_peptide     29..302
                     /product="tissue factor pathway inhibitor isoform 1"
                     /calculated_mol_wt=31432
     Region          50..104
                     /region_name="Kunitz_TFPI1_1-like"
                     /note="Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or
                     K1) of tissue factor pathway inhibitor (TFPI); cd22613"
                     /db_xref="CDD:438656"
     Site            order(51..52,62,64,66,68,83..90,92..95,98,101..102)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            order(59..68,82..87,92)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            63..64
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02445.1)"
     Region          120..175
                     /region_name="Kunitz_TFPI1_2-like"
                     /note="Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or
                     K2) of tissue factor pathway inhibitor (TFPI); cd22614"
                     /db_xref="CDD:438657"
     Site            order(132..136,155,157..158)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438657"
     Site            134..135
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02445.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02445.1)"
     Region          219..272
                     /region_name="Kunitz_TFPI1_TFPI2_3-like"
                     /note="Kunitz protease inhibitor (KPI) domain 3 (KPI-3 or
                     K3) of tissue factor pathway inhibitor (TFPI) and TFPI2,
                     and similar proteins; cd22615"
                     /db_xref="CDD:438658"
     Site            232..233
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02445.1)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02445.1)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02445.1)"
     CDS             1..302
                     /gene="Tfpi"
                     /coded_by="NM_017200.1:89..997"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29436"
                     /db_xref="RGD:61914"
ORIGIN      
        1 mtnklkkdha fwaavcllls ivpellnalp eedddtintd selrpmkplh tfcamkaedg
       61 pckamirsyy fnmnshqcee fiyggcrgnk nrfdtleecr ktcipgykkt tikttsgaek
      121 pdfcfleedp gicrgfmtry fynnqskqce qfkyggclgn snnfetleec rntcedpvne
      181 vqkgdyvtnq itvtdrttvn nvvipqatka psqwdydgps wclepadsgl ckasekrfyy
      241 npaigkcrqf nytgcggnnn nfttkqdcnr ackkdsskks skraktqrrr ksfvkvmyen
      301 ih
//
LOCUS       NP_001009419             432 aa            linear   ROD 27-APR-2025
DEFINITION  N-acylneuraminate cytidylyltransferase [Rattus norvegicus].
ACCESSION   NP_001009419 XP_232513
VERSION     NP_001009419.1
DBSOURCE    REFSEQ: accession NM_001009419.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087599.1.
            
            On Jan 7, 2005 this sequence version replaced XP_232513.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..432
                     /product="N-acylneuraminate cytidylyltransferase"
                     /EC_number="2.7.7.43"
                     /note="CMP-NeuNAc synthetase; CMP-N-acetylneuraminic acid
                     synthetase; CMP-NeuNAc synthase; CMP-N-acetylneuraminic
                     acid synthase; cytidine monophospho-N-acetylneuraminic
                     acid synthetase; cytidine 5'-monophosphate
                     N-acetylneuraminic acid synthetase"
                     /calculated_mol_wt=48009
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P69060.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFW8; propagated from
                     UniProtKB/Swiss-Prot (P69060.1)"
     Region          15..31
                     /region_name="BC1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P69060.1)"
     Site            35
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99KK2; propagated from
                     UniProtKB/Swiss-Prot (P69060.1)"
     Region          42..257
                     /region_name="CMP-NeuAc_Synthase"
                     /note="CMP-NeuAc_Synthase activates N-acetylneuraminic
                     acid by adding CMP moiety; cd02513"
                     /db_xref="CDD:133006"
     Site            order(48..50,54,60,109,113,120,141,143,211,216,247)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133006"
     Site            50
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99KK2; propagated from
                     UniProtKB/Swiss-Prot (P69060.1)"
     Site            order(63,65..66,168,172..173,208..211,216,233,235,247,
                     250..251,254,257)
                     /site_type="active"
                     /note="tetramer interface [active]"
                     /db_xref="CDD:133006"
     Region          198..204
                     /region_name="BC2 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P69060.1)"
     Region          267..274
                     /region_name="BC3 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P69060.1)"
     Region          273..417
                     /region_name="HAD_KDO-like"
                     /note="haloacid dehalogenase-like (HAD) hydrolase, similar
                     to Escherichia coli 3-deoxy-D-manno-octulosonate
                     8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout
                     N-acylneuraminate cytidylyltransferase; cd01630"
                     /db_xref="CDD:319769"
     Site            order(279..283,323..324,348,370..371,374..375)
                     /site_type="active"
                     /db_xref="CDD:319769"
     Site            order(281,286..293,295,297..304,307,311,325,329..330,
                     333..334,337,346,371..374,376..377,390,394,409,413,417)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:319769"
     CDS             1..432
                     /gene="Cmas"
                     /coded_by="NM_001009419.1:6..1304"
                     /db_xref="GeneID:312826"
                     /db_xref="RGD:1310911"
ORIGIN      
        1 mdalekgaat sgpaprgrps rgrppklqrs rgagrglekp phlaalvlar ggskgiplkn
       61 ikrlagvpli gwvlraalda gvfqsvwvst dhdeienvak qfgaqvhrrs setskdssts
      121 ldaiveflny hnevdivgni qatspclhpt dlqkvaemir eegydsvfsv vrrhqfrwse
      181 iqkgvrevte plnlnpakrp rrqdwdgely engsfyfakr hliemgylqg gkmayyemra
      241 ehsvdidvdi dwpiaeqrvl rfgyfgkekl keikllvcni dgcltnghiy vsgdqkeiis
      301 ydvkdaigis llkksgievr liseracskq tlsalkldck tevsvsdkla ivdewrkemg
      361 lcwkevaylg nevsdeeclk raglsavpad acsraqkavg yickcnggrg airefaehif
      421 lllekvnnsc qk
//
LOCUS       NP_001004072             390 aa            linear   ROD 27-APR-2025
DEFINITION  pyruvate dehydrogenase E1 component subunit alpha, somatic form,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_001004072 XP_343788
VERSION     NP_001004072.2
DBSOURCE    REFSEQ: accession NM_001004072.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Sharkia,I., Hadad Erlich,T., Landolina,N., Assayag,M., Motzik,A.,
            Rachmin,I., Kay,G., Porat,Z., Tshori,S., Berkman,N.,
            Levi-Schaffer,F. and Razin,E.
  TITLE     Pyruvate dehydrogenase has a major role in mast cell function, and
            its activity is regulated by mitochondrial microphthalmia
            transcription factor
  JOURNAL   J Allergy Clin Immunol 140 (1), 204-214 (2017)
   PUBMED   27871875
  REMARK    GeneRIF: The association of mitochondrial microphthalmia-associated
            transcription factor (MITF) with pyruvate dehydrogenase (PDH)
            emerges as an important regulator of mast cell function. Our
            findings indicate that PDH could arise as a new target for the
            manipulation of allergic diseases.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Terzenidou,M.E., Segklia,A., Kano,T., Papastefanaki,F.,
            Karakostas,A., Charalambous,M., Ioakeimidis,F., Papadaki,M.,
            Kloukina,I., Chrysanthou-Piterou,M., Samiotaki,M., Panayotou,G.,
            Matsas,R. and Douni,E.
  TITLE     Novel insights into SLC25A46-related pathologies in a genetic mouse
            model
  JOURNAL   PLoS Genet 13 (4), e1006656 (2017)
   PUBMED   28376086
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Bunik,V.I., Artiukhov,A., Kazantsev,A., Goncalves,R., Daloso,D.,
            Oppermann,H., Kulakovskaya,E., Lukashev,N., Fernie,A., Brand,M. and
            Gaunitz,F.
  TITLE     Specific inhibition by synthetic analogs of pyruvate reveals that
            the pyruvate dehydrogenase reaction is essential for metabolism and
            viability of glioblastoma cells
  JOURNAL   Oncotarget 6 (37), 40036-40052 (2015)
   PUBMED   26503465
  REMARK    GeneRIF: Data indicate that catalytic transformation of pyruvate by
            pyruvate dehydrogenase is essential for the metabolism and
            viability of glioblastoma cell lines.
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Akhmedov,D., De Marchi,U., Wollheim,C.B. and Wiederkehr,A.
  TITLE     Pyruvate dehydrogenase E1alpha phosphorylation is induced by
            glucose but does not control metabolism-secretion coupling in
            INS-1E clonal beta-cells
  JOURNAL   Biochim Biophys Acta 1823 (10), 1815-1824 (2012)
   PUBMED   22809973
  REMARK    GeneRIF: Although glucose stimulates E1alpha phosphorylation and
            therefore inhibits PDH activity, this control mechanism by itself
            does not alter metabolism-secretion coupling in INS-1E clonal
            beta-cells.
REFERENCE   5  (residues 1 to 390)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Johnson,M.T., Mahmood,S., Hyatt,S.L., Yang,H.S., Soloway,P.D.,
            Hanson,R.W. and Patel,M.S.
  TITLE     Inactivation of the murine pyruvate dehydrogenase (Pdha1) gene and
            its effect on early embryonic development
  JOURNAL   Mol Genet Metab 74 (3), 293-302 (2001)
   PUBMED   11708858
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Lissens,W., De Meirleir,L., Seneca,S., Liebaers,I., Brown,G.K.,
            Brown,R.M., Ito,M., Naito,E., Kuroda,Y., Kerr,D.S., Wexler,I.D.,
            Patel,M.S., Robinson,B.H. and Seyda,A.
  TITLE     Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit
            gene (PDHA1) in patients with a pyruvate dehydrogenase complex
            deficiency
  JOURNAL   Hum Mutat 15 (3), 209-219 (2000)
   PUBMED   10679936
  REMARK    Review article
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Maury,J., Kerbey,A.L., Priestman,D.A., Patel,M.S., Girard,J. and
            Ferre,P.
  TITLE     Pretranslational regulation of pyruvate dehydrogenase complex
            subunits in white adipose tissue during the suckling-weaning
            transition in the rat
  JOURNAL   Biochem J 311 (Pt 2) (Pt 2), 531-535 (1995)
   PUBMED   7487891
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Cullingford,T.E., Clark,J.B. and Phillips,I.R.
  TITLE     The pyruvate dehydrogenase complex: cloning of the rat somatic E1
            alpha subunit and its coordinate expression with the mRNAs for the
            E1 beta, E2, and E3 catalytic subunits in developing rat brain
  JOURNAL   J Neurochem 62 (5), 1682-1690 (1994)
   PUBMED   8158120
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Matuda,S., Nakano,K., Ohta,S., Saheki,T., Kawanishi,Y. and
            Miyata,T.
  TITLE     The alpha-ketoacid dehydrogenase complexes. Sequence similarity of
            rat pyruvate dehydrogenase with Escherichia coli and Azotobacter
            vinelandii alpha-ketoglutarate dehydrogenase
  JOURNAL   Biochim Biophys Acta 1089 (1), 1-7 (1991)
   PUBMED   2025639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC098897.1.
            
            On Feb 3, 2007 this sequence version replaced NP_001004072.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098897.1, BC079369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq14"
     Protein         1..390
                     /product="pyruvate dehydrogenase E1 component subunit
                     alpha, somatic form, mitochondrial precursor"
                     /EC_number="1.2.4.1"
                     /note="pyruvate dehydrogenase E1 component subunit alpha,
                     somatic form, mitochondrial; PDHE1-A type I; pyruvate
                     dehydrogenase E1alpha subunit; pyruvate dehydrogenase
                     (lipoamide) alpha 1; pyruvate dehydrogenase alpha 1;
                     pyruvate dehydrogenase E1 alpha 1 subunit"
                     /calculated_mol_wt=40181
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P26284.2)"
                     /calculated_mol_wt=3053
     mat_peptide     30..390
                     /product="Pyruvate dehydrogenase E1 component subunit
                     alpha, somatic form, mitochondrial. /id=PRO_0000020445"
                     /note="propagated from UniProtKB/Swiss-Prot (P26284.2)"
                     /calculated_mol_wt=40181
     Region          58..370
                     /region_name="PDH_E1_alph_y"
                     /note="pyruvate dehydrogenase E1 component, alpha subunit;
                     TIGR03182"
                     /db_xref="CDD:274473"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            order(88,140,165..166,197,199..202,205,209,213,228..231,
                     245,296,300)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            order(118..119,165,167,195..198,225,227,292)
                     /site_type="other"
                     /note="TPP-binding site [chemical binding]"
                     /db_xref="CDD:238958"
     Site            order(160,162,164,169,172..173,176..177,179..180,183,
                     202..203,209..210,213)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:238958"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            order(287..293,295..305,314..316)
                     /site_type="phosphorylation"
                     /note="phosphorylation loop region [posttranslational
                     modification]"
                     /db_xref="CDD:238958"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1, PDK2, PDK3 and PDK4.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDK1, PDK2, PDK3 and PDK4.
                     /evidence=ECO:0000269|PubMed:19341700; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            313
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08559; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     Site            336
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35486; propagated from
                     UniProtKB/Swiss-Prot (P26284.2)"
     CDS             1..390
                     /gene="Pdha1"
                     /coded_by="NM_001004072.2:39..1211"
                     /db_xref="GeneID:29554"
                     /db_xref="RGD:3286"
ORIGIN      
        1 mrkmlaavsr vlagaaqkpa srvlvasrnf andatfeikk cdlhrleegp pvttvltred
       61 glkyyrmmqt vrrmelkadq lykqkiirgf chlcdgqeac cvgleaginp tdhlitayra
      121 hgftftrglp vrailaeltg rrggcakgkg gsmhmyaknf yggngivgaq vplgagiala
      181 ckyngkdevc ltlygdgaan qgqifeaynm aalwklpcif icennrygmg tsveraaast
      241 dyykrgdfip glrvdgmdil cvreatkfaa aycrsgkgpi lmelqtyryh ghsmsdpgvs
      301 yrtreeiqev rsksdpimll kdrmvnsnla sveelkeidv evrkeiedaa qfatadpepp
      361 leelgyhiys sdppfevrga nqwikfksvs
//
LOCUS       NP_058774                467 aa            linear   ROD 27-APR-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-5 [Rattus
            norvegicus].
ACCESSION   NP_058774
VERSION     NP_058774.2
DBSOURCE    REFSEQ: accession NM_017078.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Hopkins,R.J., Duan,F., Gamble,G.D., Chiles,C., Cavadino,A.,
            Billings,P., Aberle,D. and Young,R.P.
  TITLE     Chr15q25 genetic variant (rs16969968) independently confers risk of
            lung cancer, COPD and smoking intensity in a prospective study of
            high-risk smokers
  JOURNAL   Thorax 76 (3), 272-280 (2021)
   PUBMED   33419953
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Forget,B., Icick,R., Robert,J., Correia,C., Prevost,M.S.,
            Gielen,M., Corringer,P.J., Bellivier,F., Vorspan,F., Besson,M. and
            Maskos,U.
  TITLE     Alterations in nicotinic receptor alpha5 subunit gene
            differentially impact early and later stages of cocaine addiction:
            a translational study in transgenic rats and patients
  JOURNAL   Prog Neurobiol 197, 101898 (2021)
   PUBMED   32841724
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Besson,M., Forget,B., Correia,C., Blanco,R. and Maskos,U.
  TITLE     Profound alteration in reward processing due to a human
            polymorphism in CHRNA5: a role in alcohol dependence and feeding
            behavior
  JOURNAL   Neuropsychopharmacology 44 (11), 1906-1916 (2019)
   PUBMED   31288250
  REMARK    GeneRIF: Rats expressing the alpha5SNP consume more alcohol, and
            exhibit increased relapse to alcohol seeking after abstinence.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Perez-Morales,R., Gonzalez-Zamora,A., Gonzalez-Delgado,M.F.,
            Calleros Rincon,E.Y., Olivas Calderon,E.H., Martinez-Ramirez,O.C.
            and Rubio,J.
  TITLE     CHRNA3 rs1051730 and CHRNA5 rs16969968 polymorphisms are associated
            with heavy smoking, lung cancer, and chronic obstructive pulmonary
            disease in a mexican population
  JOURNAL   Ann Hum Genet 82 (6), 415-424 (2018)
   PUBMED   29993116
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Forget,B., Scholze,P., Langa,F., Morel,C., Pons,S., Mondoloni,S.,
            Besson,M., Durand-de Cuttoli,R., Hay,A., Tricoire,L., Lambolez,B.,
            Mourot,A., Faure,P. and Maskos,U.
  TITLE     A Human Polymorphism in CHRNA5 Is Linked to Relapse to Nicotine
            Seeking in Transgenic Rats
  JOURNAL   Curr Biol 28 (20), 3244-3253 (2018)
   PUBMED   30293722
  REMARK    GeneRIF: The alpha5SNP polymorphism is a major risk factor for
            nicotine intake at high doses and for relapse to nicotine seeking
            in rats, a dual effect that reflects the human condition. The
            results also suggest an important role for the IPN in the higher
            relapse to nicotine seeking observed in alpha5SNP rats.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Oshikawa,J., Toya,Y., Fujita,T., Egawa,M., Kawabe,J., Umemura,S.
            and Ishikawa,Y.
  TITLE     Nicotinic acetylcholine receptor alpha 7 regulates cAMP signal
            within lipid rafts
  JOURNAL   Am J Physiol Cell Physiol 285 (3), C567-C574 (2003)
   PUBMED   12748066
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Voitenko,L.P., Voitenko,S.V., Skok,M.V., Purnyn,H.E. and Skok,V.I.
  TITLE     Nicotinic acetylcholine receptor subtypes in rat superior cervical
            ganglion neurons as studied by sequential application of two
            alpha-subunit-specific antibodies
  JOURNAL   Neurosci Lett 303 (1), 37-40 (2001)
   PUBMED   11297818
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Stitzel,J.A., Blanchette,J.M. and Collins,A.C.
  TITLE     Sensitivity to the seizure-inducing effects of nicotine is
            associated with strain-specific variants of the alpha 5 and alpha 7
            nicotinic receptor subunit genes
  JOURNAL   J Pharmacol Exp Ther 284 (3), 1104-1111 (1998)
   PUBMED   9495872
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Chini,B., Clementi,F., Hukovic,N. and Sher,E.
  TITLE     Neuronal-type alpha-bungarotoxin receptors and the alpha
            5-nicotinic receptor subunit gene are expressed in neuronal and
            nonneuronal human cell lines
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1572-1576 (1992)
   PUBMED   1542648
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Boulter,J., O'Shea-Greenfield,A., Duvoisin,R.M., Connolly,J.G.,
            Wada,E., Jensen,A., Gardner,P.D., Ballivet,M., Deneris,E.S.,
            McKinnon,D. et al.
  TITLE     Alpha 3, alpha 5, and beta 4: three members of the rat neuronal
            nicotinic acetylcholine receptor-related gene family form a gene
            cluster
  JOURNAL   J Biol Chem 265 (8), 4472-4482 (1990)
   PUBMED   1689727
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 23, 2007 this sequence version replaced NP_058774.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY574255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN12840131
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..467
                     /product="neuronal acetylcholine receptor subunit alpha-5"
                     /note="acetylcholine receptor alpha 5; cholinergic
                     receptor, nicotinic, alpha polypeptide 5; cholinergic
                     receptor, nicotinic, alpha 5 (neuronal)"
                     /calculated_mol_wt=53408
     Region          45..251
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(82,84,90..91,98,120,122,131..132,134,136..137,
                     147..149,151,161,163,165,169,191,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     Region          257..446
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     CDS             1..467
                     /gene="Chrna5"
                     /coded_by="NM_017078.2:58..1461"
                     /db_xref="GeneID:25102"
                     /db_xref="RGD:2347"
ORIGIN      
        1 mavrgsrrra lrlllmvqll agrwrptgaa rgtrgglpel ssaakhedsl frdlfedyer
       61 wvrpvehlsd kikikfglai sqlvdvdekn qlmttnvwlk qewidvklrw npddyggiki
      121 irvpsdslwi pdivlfdnad grfegastkt vvryngtvtw tqpanykssc tidvtffpfd
      181 lqncsmkfgs wtydgsqvdi iledqdvdrt dffdngewei msamgskgnr tdsccwypyi
      241 tysfvikrlp lfytlfliip ciglsfltvv vfylpsnege kislctsvlv sltvfllvie
      301 eiipssskvi pligeylvft mifvtlsimv tvfainihhr sssthnamap wvrkiflhkl
      361 pkllcmrsha dryftqreea esgagpksrn tleaaldcir yitrhvvken dvrevvedwk
      421 fiaqvldrmf lwtfllvsii gtlglfvpvi ykwaniivpv higntik
//
LOCUS       NP_001102036             149 aa            linear   ROD 27-APR-2025
DEFINITION  oligosaccharyltransferase complex subunit OSTC [Rattus norvegicus].
ACCESSION   NP_001102036 XP_001076989 XP_342342
VERSION     NP_001102036.1
DBSOURCE    REFSEQ: accession NM_001108566.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Shibatani,T., David,L.L., McCormack,A.L., Frueh,K. and Skach,W.R.
  TITLE     Proteomic analysis of mammalian oligosaccharyltransferase reveals
            multiple subcomplexes that contain Sec61, TRAP, and two potential
            new subunits
  JOURNAL   Biochemistry 44 (16), 5982-5992 (2005)
   PUBMED   15835887
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473952.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342342.3, XP_001076989.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM052106.1, FQ219812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132293, SAMD00132304
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q43"
     Protein         1..149
                     /product="oligosaccharyltransferase complex subunit OSTC"
                     /note="oligosaccharyltransferase complex subunit
                     (non-catalytic)"
                     /calculated_mol_wt=16684
     Region          <17..146
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0K025.1)"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0K025.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0K025.1)"
     CDS             1..149
                     /gene="Ostc"
                     /gene_synonym="Dc2; RGD1560708"
                     /coded_by="NM_001108566.1:45..494"
                     /db_xref="GeneID:362040"
                     /db_xref="RGD:1560708"
ORIGIN      
        1 metlyrvpfl vlecpnlklk kppwvhmpsa mtvyalvvvs yflitggiiy dviveppsvg
       61 smtdehghqr pvaflayrvn gqyimeglas sflftmgglg fiildrsnap nipklnrfll
      121 lfigfvcvll sffmarvfmr mklpgylmg
//
LOCUS       NP_075223                397 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily A member 1 [Rattus norvegicus].
ACCESSION   NP_075223
VERSION     NP_075223.1
DBSOURCE    REFSEQ: accession NM_022934.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Meshalkina,D.A., Shevtsov,M.A., Dobrodumov,A.V., Komarova,E.Y.,
            Voronkina,I.V., Lazarev,V.F., Margulis,B.A. and Guzhova,I.V.
  TITLE     Knock-down of Hdj2/DNAJA1 co-chaperone results in an unexpected
            burst of tumorigenicity of C6 glioblastoma cells
  JOURNAL   Oncotarget 7 (16), 22050-22063 (2016)
   PUBMED   26959111
  REMARK    GeneRIF: The results of this study uncover a completely new role
            for the Hdj2 co-chaperone in tumorigenicity
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Roder,K., Werdich,A.A., Li,W., Liu,M., Kim,T.Y.,
            Organ-Darling,L.E., Moshal,K.S., Hwang,J.M., Lu,Y., Choi,B.R.,
            MacRae,C.A. and Koren,G.
  TITLE     RING finger protein RNF207, a novel regulator of cardiac excitation
  JOURNAL   J Biol Chem 289 (49), 33730-33740 (2014)
   PUBMED   25281747
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Stark,J.L., Mehla,K., Chaika,N., Acton,T.B., Xiao,R., Singh,P.K.,
            Montelione,G.T. and Powers,R.
  TITLE     Structure and function of human DnaJ homologue subfamily a member 1
            (DNAJA1) and its relationship to pancreatic cancer
  JOURNAL   Biochemistry 53 (8), 1360-1372 (2014)
   PUBMED   24512202
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Rauch,J.N. and Gestwicki,J.E.
  TITLE     Binding of human nucleotide exchange factors to heat shock protein
            70 (Hsp70) generates functionally distinct complexes in vitro
  JOURNAL   J Biol Chem 289 (3), 1402-1414 (2014)
   PUBMED   24318877
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Slater,L.H., Hett,E.C., Clatworthy,A.E., Mark,K.G. and Hung,D.T.
  TITLE     CCT chaperonin complex is required for efficient delivery of
            anthrax toxin into the cytosol of host cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (24), 9932-9937 (2013)
   PUBMED   23716698
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Marschang,P., Brich,J., Weeber,E.J., Sweatt,J.D., Shelton,J.M.,
            Richardson,J.A., Hammer,R.E. and Herz,J.
  TITLE     Normal development and fertility of knockout mice lacking the tumor
            suppressor gene LRP1b suggest functional compensation by LRP1
  JOURNAL   Mol Cell Biol 24 (9), 3782-3793 (2004)
   PUBMED   15082773
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Gotoh,T., Terada,K., Oyadomari,S. and Mori,M.
  TITLE     hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced
            apoptosis by inhibiting translocation of Bax to mitochondria
  JOURNAL   Cell Death Differ 11 (4), 390-402 (2004)
   PUBMED   14752510
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Imai,Y., Soda,M., Hatakeyama,S., Akagi,T., Hashikawa,T.,
            Nakayama,K.I. and Takahashi,R.
  TITLE     CHIP is associated with Parkin, a gene responsible for familial
            Parkinson's disease, and enhances its ubiquitin ligase activity
  JOURNAL   Mol Cell 10 (1), 55-67 (2002)
   PUBMED   12150907
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Pei,L.
  TITLE     Pituitary tumor-transforming gene protein associates with ribosomal
            protein S10 and a novel human homologue of DnaJ in testicular cells
  JOURNAL   J Biol Chem 274 (5), 3151-3158 (1999)
   PUBMED   9915854
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Leng,C.H., Brodsky,J.L. and Wang,C.
  TITLE     Isolation and characterization of a DnaJ-like protein in rats: the
            C-terminal 10-kDa domain of hsc70 is not essential for stimulating
            the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein
  JOURNAL   Protein Sci 7 (5), 1186-1194 (1998)
   PUBMED   9605323
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U53922.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U53922.1, FQ216722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..397
                     /product="dnaJ homolog subfamily A member 1"
                     /note="DnaJ-like protein 2; dnaJ-like protein 1; HSJ-2;
                     heat shock protein J2; DnaJ (Hsp40) homolog, subfamily A,
                     member 1"
                     /calculated_mol_wt=44737
     mat_peptide     1..394
                     /product="DnaJ homolog subfamily A member 1.
                     /id=PRO_0000071010"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
                     /calculated_mol_wt=44552
     Region          2..394
                     /region_name="PTZ00037"
                     /note="DnaJ_C chaperone protein; Provisional"
                     /db_xref="CDD:240236"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P31689; propagated from
                     UniProtKB/Swiss-Prot (P63036.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63036.1)"
     Region          134..141
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
     Region          150..157
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
     Region          177..184
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
     Region          193..200
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63036.1)"
     Region          352..397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63036.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31689; propagated from
                     UniProtKB/Swiss-Prot (P63036.1)"
     Site            394
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P63036.1)"
     CDS             1..397
                     /gene="Dnaja1"
                     /gene_synonym="Hsj2"
                     /coded_by="NM_022934.1:122..1315"
                     /db_xref="GeneID:65028"
                     /db_xref="RGD:620942"
ORIGIN      
        1 mvkettyydv lgvkpnatqe elkkayrkla lkyhpdknpn egekfkqisq ayevladskk
       61 relydkggeq aikeggaggg fgspmdifdm ffggggrmqr errgknvvhq lsvtledlyn
      121 gatrklalqk nvicdkcegr ggkkgavecc pncrgtgmqi rihqigpgmv qqiqsvcmec
      181 qghgerispk drckscngrk ivrekkilev hidkgmkdgq kitfhgegdq epglepgdii
      241 ivldqkdhav ftrrgedlfm cmdiqlveal cgfqkpistl dnrtivitsh pgqivkhgdi
      301 kcvlnegmpi yrrpyekgrl iiefkvnfpe ngflspdkls llekllperk eveetdemdq
      361 velvdfdpnq errrhyngea yeddehhprg gvqcqts
//
LOCUS       NP_036775               1115 aa            linear   ROD 27-APR-2025
DEFINITION  proto-oncogene tyrosine-protein kinase receptor Ret isoform a
            precursor [Rattus norvegicus].
ACCESSION   NP_036775
VERSION     NP_036775.2
DBSOURCE    REFSEQ: accession NM_012643.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Kasanga,E.A., Han,Y., Navarrete,W., McManus,R., Shifflet,M.K.,
            Parry,C., Barahona,A., Manfredsson,F.P., Nejtek,V.A.,
            Richardson,J.R. and Salvatore,M.F.
  TITLE     Differential expression of RET and GDNF family receptor,
            GFR-alpha1, between striatum and substantia nigra following
            nigrostriatal lesion: A case for diminished GDNF-signaling
  JOURNAL   Exp Neurol 366, 114435 (2023)
   PUBMED   37178997
  REMARK    GeneRIF: Differential expression of RET and GDNF family receptor,
            GFR-alpha1, between striatum and substantia nigra following
            nigrostriatal lesion: A case for diminished GDNF-signaling.
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Kearon,J.E., Kocherry,S.C., Zoumboulakis,D., Rivera,D.,
            Lourenssen,S.R. and Blennerhassett,M.G.
  TITLE     GDNF requires HIF-1alpha and RET activation for suppression of
            programmed cell death of enteric neurons by metabolic challenge
  JOURNAL   Mol Cell Neurosci 115, 103655 (2021)
   PUBMED   34273501
  REMARK    GeneRIF: GDNF requires HIF-1alpha and RET activation for
            suppression of programmed cell death of enteric neurons by
            metabolic challenge.
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Hu,X.B., Fu,S.H., Luo,Q.I., He,J.Z., Qiu,Y.F., Lai,W. and Zhong,M.
  TITLE     Down-regulation of microRNA-216a confers protection against yttrium
            aluminium garnet laser-induced retinal injury via the GDNF-mediated
            GDNF/GFRalpha1/RET signalling pathway
  JOURNAL   J Biosci 43 (5), 985-1000 (2018)
   PUBMED   30541958
  REMARK    GeneRIF: The findings demonstrate that elevated GDNF levels can
            reduce the retinal injury, whereby down-regulated miR-216a
            aggravates the YAG laser-induced retinal injury by targeting the
            GDNF level through the GDNF/GFRa1/RET signaling pathway.
REFERENCE   4  (residues 1 to 1115)
  AUTHORS   Pertile,R.A.N., Cui,X., Hammond,L. and Eyles,D.W.
  TITLE     Vitamin D regulation of GDNF/Ret signaling in dopaminergic neurons
  JOURNAL   FASEB J 32 (2), 819-828 (2018)
   PUBMED   29018141
  REMARK    GeneRIF: the inverse relationship between GFRalpha1 and C-Ret, as
            knocking down C-Ret led to increases in GFRalpha1 expression.
REFERENCE   5  (residues 1 to 1115)
  AUTHORS   Hsu,J.Y., Crawley,S., Chen,M., Ayupova,D.A., Lindhout,D.A.,
            Higbee,J., Kutach,A., Joo,W., Gao,Z., Fu,D., To,C., Mondal,K.,
            Li,B., Kekatpure,A., Wang,M., Laird,T., Horner,G., Chan,J.,
            McEntee,M., Lopez,M., Lakshminarasimhan,D., White,A., Wang,S.P.,
            Yao,J., Yie,J., Matern,H., Solloway,M., Haldankar,R., Parsons,T.,
            Tang,J., Shen,W.D., Alice Chen,Y., Tian,H. and Allan,B.B.
  TITLE     Non-homeostatic body weight regulation through a
            brainstem-restricted receptor for GDF15
  JOURNAL   Nature 550 (7675), 255-259 (2017)
   PUBMED   28953886
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24481. PMID: 29144449]
REFERENCE   6  (residues 1 to 1115)
  AUTHORS   Kitagawa,H., Sasaki,C., Zhang,W.R., Sakai,K., Shiro,Y., Warita,H.,
            Mitsumoto,Y., Mori,T. and Abe,K.
  TITLE     Induction of glial cell line-derived neurotrophic factor receptor
            proteins in cerebral cortex and striatum after permanent middle
            cerebral artery occlusion in rats
  JOURNAL   Brain Res 834 (1-2), 190-195 (1999)
   PUBMED   10407114
REFERENCE   7  (residues 1 to 1115)
  AUTHORS   Natarajan,D., Grigoriou,M., Marcos-Gutierrez,C.V., Atkins,C. and
            Pachnis,V.
  TITLE     Multipotential progenitors of the mammalian enteric nervous system
            capable of colonising aganglionic bowel in organ culture
  JOURNAL   Development 126 (1), 157-168 (1999)
   PUBMED   9834195
REFERENCE   8  (residues 1 to 1115)
  AUTHORS   Baloh,R.H., Gorodinsky,A., Golden,J.P., Tansey,M.G., Keck,C.L.,
            Popescu,N.C., Johnson,E.M. Jr. and Milbrandt,J.
  TITLE     GFRalpha3 is an orphan member of the GDNF/neurturin/persephin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 95 (10), 5801-5806 (1998)
   PUBMED   9576965
REFERENCE   9  (residues 1 to 1115)
  AUTHORS   Burazin,T.C. and Gundlach,A.L.
  TITLE     Up-regulation of GDNFR-alpha and c-ret mRNA in facial motor neurons
            following facial nerve injury in the rat
  JOURNAL   Brain Res Mol Brain Res 55 (2), 331-336 (1998)
   PUBMED   9582449
REFERENCE   10 (residues 1 to 1115)
  AUTHORS   Canzian,F., Ushijima,T., Nagao,M., Matera,I., Romeo,G. and
            Ceccherini,I.
  TITLE     Genetic mapping of the RET protooncogene on rat chromosome 4
  JOURNAL   Mamm Genome 6 (6), 433-435 (1995)
   PUBMED   7647468
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 23, 2007 this sequence version replaced NP_036775.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.17263.1,
                                           SRR26643298.24942.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1115
                     /product="proto-oncogene tyrosine-protein kinase receptor
                     Ret isoform a precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine kinase; Ret proto-oncogene
                     (multiple endocrine neoplasia MEN2A MEN2B and medullary
                     thyroid carcinoma 1 Hirschsprung disease); proto-oncogene
                     tyrosine-protein kinase receptor Ret; Ret gene for
                     receptor tyrosin"
                     /calculated_mol_wt=121945
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
                     /calculated_mol_wt=2311
     mat_peptide     24..1115
                     /product="Proto-oncogene tyrosine-protein kinase receptor
                     Ret. /id=PRO_0000424874"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
                     /calculated_mol_wt=121945
     Region          29..154
                     /region_name="RET_CLD1"
                     /note="RET Cadherin like domain 1; pfam17756"
                     /db_xref="CDD:465485"
     Region          29..153
                     /region_name="Cadherin-like region 1 (CLD1).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          173..248
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(178..179,230,232,265,267..268)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          266..380
                     /region_name="Cadherin-like region 3 (CLD3).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          266..380
                     /region_name="RET_CLD3"
                     /note="RET Cadherin like domain 3; pfam17812"
                     /db_xref="CDD:465516"
     Site            378
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            395
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          406..507
                     /region_name="Cadherin-like region 4 (CLD4).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          408..507
                     /region_name="RET_CLD4"
                     /note="RET Cadherin like domain 4; pfam17813"
                     /db_xref="CDD:465517"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            469
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            555
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            638..658
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            689
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            708..709
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          724..1013
                     /region_name="PTKc_RET"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     REarranged during Transfection protein; cd05045"
                     /db_xref="CDD:173631"
     Site            order(731..735,739,757,759,805..806,808,812,875,879..880,
                     882,893,911..915,924,958)
                     /site_type="active"
                     /db_xref="CDD:173631"
     Site            order(731..734,739,757,759,805..806,808,812,882,893)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173631"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            order(875,879,911..915,924,958)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173631"
     Site            892..917
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173631"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            982
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1018..1019
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1063
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1097
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     CDS             1..1115
                     /gene="Ret"
                     /coded_by="NM_012643.2:14..3361"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:24716"
                     /db_xref="RGD:3556"
ORIGIN      
        1 makarsgaag lglklflllp llgeaplgly fsrdaywerl yvdqpagtpl lyvhalrdap
       61 gevpsfrlgq ylygvyrtrl hendwihids gtgllylnqs ldhssweqls irnggfpllt
      121 vflqvflgst aqregechwp gcarvyfsfi ndtfpncssf kardlctpet gvsfrirenr
      181 ppgtfyqfrm lpvqflcpni svkykllegd glpfrcdpdc levstrwald relqekyvle
      241 aecavagpga nkekvavsfp vtvydeddsp ptfsggvgta savvefkrke gtvvatlqvf
      301 dadvvpasge lvrrytstll sgdswaqqtf rvehtpnetl vqsnnnsvra tmhnyklvln
      361 rslsisesrv lqlvvlvnds dfqgpgsgvl flhfnvsvlp vtlnlpmays fpvnrrarry
      421 aqigkvcven cqefsgvsiq yklqpsstnc salgvvtste dtsgtlyvnd tealrrpect
      481 elqytvvatd rqtrrqtqas lvvtvegtyi aeevgcpksc avnkrrpece ecgglgsptg
      541 rcewrqgdgk gitrnfstcs pstrtcpdgh cdalesrdin icpqdclrgp ivggherger
      601 qgikagygic ncfpdekkcf cepedsqgpl cdelcrtvit aavlfsfiis vllstfcihr
      661 yhkhahkppi asaemtfcrp aqgfpisyss sgtrrpslds menqvsvdsf kipedpkwef
      721 prknlvlgkt lgegefgkvv katafrlkgr agyttvavkm lkenasqsel rdllsefnll
      781 kqvnhphvik lygacsqdgp llliveyaky gslrgflrds rkigpayvss ggsrnsssld
      841 hpdervltmg dlisfawqis rgmqylaemk lvhrdlaarn ilvaegrkmk isdfglsrdv
      901 yeedsyvkks kgripvkwma ieslfdhiyt tqsdvwsfgv llweivtlgg npypgipper
      961 lfnllktghr merpdncsee myrlmlqcwk qepdkrpvfa diskdlekmm vksrdyldla
     1021 astpsdslly ddglseeetp lvdcnsaplp rslpstwien klygmsdpnw pgespvpltr
     1081 adgtstgfpr yandsvyanw mvspsaaklm dtfds
//
LOCUS       NP_036842                414 aa            linear   ROD 27-APR-2025
DEFINITION  seminal vesicle secretory protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_036842
VERSION     NP_036842.2
DBSOURCE    REFSEQ: accession NM_012710.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   O'Rand,M.G. and Widgren,E.E.
  TITLE     Loss of calcium in human spermatozoa via EPPIN, the semenogelin
            receptor
  JOURNAL   Biol Reprod 86 (2), 55 (2012)
   PUBMED   22075473
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Mitra,A., Richardson,R.T. and O'Rand,M.G.
  TITLE     Analysis of recombinant human semenogelin as an inhibitor of human
            sperm motility
  JOURNAL   Biol Reprod 82 (3), 489-496 (2010)
   PUBMED   19889947
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Edstrom,A.M., Malm,J., Frohm,B., Martellini,J.A., Giwercman,A.,
            Morgelin,M., Cole,A.M. and Sorensen,O.E.
  TITLE     The major bactericidal activity of human seminal plasma is
            zinc-dependent and derived from fragmentation of the semenogelins
  JOURNAL   J Immunol 181 (5), 3413-3421 (2008)
   PUBMED   18714013
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Zhao,H., Lee,W.H., Shen,J.H., Li,H. and Zhang,Y.
  TITLE     Identification of novel semenogelin I-derived antimicrobial peptide
            from liquefied human seminal plasma
  JOURNAL   Peptides 29 (4), 505-511 (2008)
   PUBMED   18314226
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Kise,H., Nishioka,J., Kawamura,J. and Suzuki,K.
  TITLE     Characterization of semenogelin II and its molecular interaction
            with prostate-specific antigen and protein C inhibitor
  JOURNAL   Eur J Biochem 238 (1), 88-96 (1996)
   PUBMED   8665956
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Malm,J., Hellman,J., Magnusson,H., Laurell,C.B. and Lilja,H.
  TITLE     Isolation and characterization of the major gel proteins in human
            semen, semenogelin I and semenogelin II
  JOURNAL   Eur J Biochem 238 (1), 48-53 (1996)
   PUBMED   8665951
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Harris,S.E., Harris,M.A., Johnson,C.M., Bean,M.F., Dodd,J.G.,
            Matusik,R.J., Carr,S.A. and Crabb,J.W.
  TITLE     Structural characterization of the rat seminal vesicle secretion II
            protein and gene
  JOURNAL   J Biol Chem 265 (17), 9896-9903 (1990)
   PUBMED   2351680
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Lilja,H., Abrahamsson,P.A. and Lundwall,A.
  TITLE     Semenogelin, the predominant protein in human semen. Primary
            structure and identification of closely related proteins in the
            male accessory sex glands and on the spermatozoa
  JOURNAL   J Biol Chem 264 (3), 1894-1900 (1989)
   PUBMED   2912989
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Maffei,A., Paonessa,G., Abrescia,P., Metafora,S. and Guardiola,J.
  TITLE     Polymorphism of rat seminal vesicle secretory proteins:
            characterization of svp-1 and svp-2 and their identification with
            the major secretory proteins IV and V
  JOURNAL   Biochem Genet 22 (5-6), 567-576 (1984)
   PUBMED   6466291
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061977.1.
            
            On Jan 1, 2004 this sequence version replaced NP_036842.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676811 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..414
                     /product="seminal vesicle secretory protein 2 precursor"
                     /note="seminal vesicle protein, secretion 1; seminal
                     vesicle protein, secretion 2; SVS II; seminal vesicle
                     secretory protein II; seminal vesicle secretory protein 2;
                     semenogelin I"
                     /calculated_mol_wt=43135
     sig_peptide     1..22
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
                     /calculated_mol_wt=2436
     mat_peptide     23..414
                     /product="Seminal vesicle secretory protein 2.
                     /id=PRO_0000022451"
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
                     /calculated_mol_wt=43135
     Site            23
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:2351680; propagated from
                     UniProtKB/Swiss-Prot (P22006.1)"
     Region          <64..>265
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          108..311
                     /region_name="13 X 13 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
     Region          170..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
     Region          240..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
     Region          306..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22006.1)"
     CDS             1..414
                     /gene="Semg1"
                     /gene_synonym="RATSVPIIA; Svp1; SVPIIA; Svs2; SVS2P;
                     Svs2p2"
                     /coded_by="NM_012710.2:10..1254"
                     /db_xref="GeneID:25013"
                     /db_xref="RGD:3790"
ORIGIN      
        1 mkssifilsl flllerqaav vgqyggtkgh fqssssgfml gqkghlnfgl kggseeaaee
       61 sifmqsqhqm fgqdggdmaq tsvsqehtgv kgaaicrkgq vsqlksqesq iksfrqvkss
      121 gqlksggsql ksfgqvksse sqlksfgqvk asgsqlksfg qvkasgsqlk sygqmkssgs
      181 qvksfgqmks sgsqvksfgq mkasesqiks fgqrksqggq lqsygqmksy gqtkslesqa
      241 ksfgqvksqs gqmkssygqr ksygeetqlk sfdqdaqlks ygqqksqkqs sfsqvksqsa
      301 qlksfgqqks lkgfsqqtqq kgfamdedls qvrkqfdddd lsvqqkstqq mkteedlsqf
      361 gqqrqfgqer sqsykgylaq yrkklqeqqq qknfnqdnff tkggaglyqa qlkg
//
LOCUS       NP_579832                572 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane glycoprotein NMB precursor [Rattus norvegicus].
ACCESSION   NP_579832
VERSION     NP_579832.1
DBSOURCE    REFSEQ: accession NM_133298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Hou,X., Xiao,S., Xu,X., Qin,M., Cheng,X. and Xu,X.
  TITLE     Glycoprotein Non-metastatic Melanoma Protein B (GPNMB) Protects
            Against Neuroinflammation and Neuronal Loss in Pilocarpine-induced
            Epilepsy via the Regulation of Microglial Polarization
  JOURNAL   Neuroscience 551, 166-176 (2024)
   PUBMED   38782114
  REMARK    GeneRIF: Glycoprotein Non-metastatic Melanoma Protein B (GPNMB)
            Protects Against Neuroinflammation and Neuronal Loss in
            Pilocarpine-induced Epilepsy via the Regulation of Microglial
            Polarization.
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Li,X., Xu,J., Su,W., Su,L., Chen,X., Yang,J., Lin,X. and Yang,L.
  TITLE     GPNMB Modulates Autophagy to Enhance Functional Recovery After
            Spinal Cord Injury in Rats
  JOURNAL   Cell Transplant 33, 9636897241233040 (2024)
   PUBMED   38400732
  REMARK    GeneRIF: GPNMB Modulates Autophagy to Enhance Functional Recovery
            After Spinal Cord Injury in Rats.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Zheng,Y., Huang,C., Yang,X. and Zhang,Z.
  TITLE     Altered expression of glycoprotein non-metastatic melanoma protein
            B in the distal sciatic nerve following injury
  JOURNAL   Int J Mol Med 45 (6), 1909-1917 (2020)
   PUBMED   32236569
  REMARK    GeneRIF: Altered expression of glycoprotein nonmetastatic melanoma
            protein B in the distal sciatic nerve following injury.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Ma,J., Baker,A.R., Calabro,A. and Derwin,K.A.
  TITLE     Exploratory study on the effect of osteoactivin on muscle
            regeneration in a rat volumetric muscle loss model
  JOURNAL   PLoS One 12 (4), e0175853 (2017)
   PUBMED   28426701
  REMARK    GeneRIF: objective of this study is to investigate the potential
            regenerative effect of OA embedded and delivered via a cross-linked
            gelatin hydrogel within a volumetric tibialis anterior muscle
            defect in a rat model
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Jarve,A., Muhlstedt,S., Qadri,F., Nickl,B., Schulz,H., Hubner,N.,
            Ozcelik,C. and Bader,M.
  TITLE     Adverse left ventricular remodeling by glycoprotein nonmetastatic
            melanoma protein B in myocardial infarction
  JOURNAL   FASEB J 31 (2), 556-568 (2017)
   PUBMED   28148779
  REMARK    GeneRIF: This is the first experimental study to show that GPNMB
            adversely influences myocardial remodeling.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Onaga,M., Ido,A., Hasuike,S., Uto,H., Moriuchi,A., Nagata,K.,
            Hori,T., Hayash,K. and Tsubouchi,H.
  TITLE     Osteoactivin expressed during cirrhosis development in rats fed a
            choline-deficient, L-amino acid-defined diet, accelerates motility
            of hepatoma cells
  JOURNAL   J Hepatol 39 (5), 779-785 (2003)
   PUBMED   14568261
  REMARK    GeneRIF: results indicate that osteoactivin is a novel factor
            involved in the progression of hepatocellular carcinoma via
            stimulation of tumor invasiveness and metastatic potential
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Bandari,P.S., Qian,J., Yehia,G., Joshi,D.D., Maloof,P.B.,
            Potian,J., Oh,H.S., Gascon,P., Harrison,J.S. and Rameshwar,P.
  TITLE     Hematopoietic growth factor inducible neurokinin-1 type: a
            transmembrane protein that is similar to neurokinin 1 interacts
            with substance P
  JOURNAL   Regul Pept 111 (1-3), 169-178 (2003)
   PUBMED   12609765
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Bachner,D., Schroder,D. and Gross,G.
  TITLE     mRNA expression of the murine glycoprotein (transmembrane) nmb
            (Gpnmb) gene is linked to the developing retinal pigment epithelium
            and iris
  JOURNAL   Brain Res Gene Expr Patterns 1 (3-4), 159-165 (2002)
   PUBMED   12638126
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Shikano,S., Bonkobara,M., Zukas,P.K. and Ariizumi,K.
  TITLE     Molecular cloning of a dendritic cell-associated transmembrane
            protein, DC-HIL, that promotes RGD-dependent adhesion of
            endothelial cells through recognition of heparan sulfate
            proteoglycans
  JOURNAL   J Biol Chem 276 (11), 8125-8134 (2001)
   PUBMED   11114299
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Safadi,F.F., Xu,J., Smock,S.L., Rico,M.C., Owen,T.A. and
            Popoff,S.N.
  TITLE     Cloning and characterization of osteoactivin, a novel cDNA
            expressed in osteoblasts
  JOURNAL   J Cell Biochem 84 (1), 12-26 (2001)
   PUBMED   11746512
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF184983.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF184983.2, BC061725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132281, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..572
                     /product="transmembrane glycoprotein NMB precursor"
                     /note="transmembrane glycoprotein NMB; osteoactivin;
                     glycoprotein (transmembrane) nmb"
                     /calculated_mol_wt=61561
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
                     /calculated_mol_wt=2230
     mat_peptide     23..572
                     /product="Transmembrane glycoprotein NMB.
                     /id=PRO_0000024711"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7C7.1)"
                     /calculated_mol_wt=61561
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Region          263..316
                     /region_name="PKD"
                     /note="polycystic kidney disease I (PKD) domain; similar
                     to other cell-surface modules, with an IG-like fold;
                     domain probably functions as a ligand binding site in
                     protein-protein or protein-carbohydrate interactions; a
                     single instance of the repeat is...; cd00146"
                     /db_xref="CDD:238084"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            306
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Region          321..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Region          417..467
                     /region_name="PKAT_KLD"
                     /note="PKAT, KLD domain; pfam20433"
                     /db_xref="CDD:466582"
     Site            461
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            469
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            501..521
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99P91; propagated from
                     UniProtKB/Swiss-Prot (Q6P7C7.1)"
     Region          556..558
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7C7.1)"
     CDS             1..572
                     /gene="Gpnmb"
                     /coded_by="NM_133298.1:115..1833"
                     /db_xref="GeneID:113955"
                     /db_xref="RGD:71008"
ORIGIN      
        1 meslcgvlvf lllaaglplq aakrfrdvlg heqypdhmre nnqlrgwssd enewdeqlyp
       61 vwrrgegrwk dsweggrvqa altsdspalv gsnitfvvnl vfprcqkeda ngnivyernc
      121 rsdlelasdp yvynwttgad dedwedntsq gqhlrfpdgk pfprphgrkk wnfvyvfhtl
      181 gqyfqklgqc sarvsintvn ltvgpqvmev ivfrrhgray ipiskvkdvy vitdqipifv
      241 tmyqkndrns sdetflrdlp iffdvlihdp shflnysais ykwnfgdntg lfvsnnhtln
      301 htyvlngtfn fnltvqtavp gpcpsptpsp ssstspspas spsptlstps pslmptgyks
      361 melsdisnen crinrygyfr atitivdgil evniiqvadv piptlqpdns lmdfivtckg
      421 atpteactii sdptcqiaqn rvcspvavde lcllsvrraf ngsgtycvnf tlgddaslal
      481 tsalisipgk dlgsplrtvn gvlisigcla mfvtmvtill ykkhktykpi gnctrnvvkg
      541 kglsvflsha kapfsrgdre kdpllqdkpw ml
//
LOCUS       NP_001030084             480 aa            linear   ROD 27-APR-2025
DEFINITION  reticulophagy regulator 1 [Rattus norvegicus].
ACCESSION   NP_001030084
VERSION     NP_001030084.1
DBSOURCE    REFSEQ: accession NM_001034912.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Luo,R., Li,G., Zhang,W., Liang,H., Lu,S., Cheung,J.P.Y., Zhang,T.,
            Tu,J., Liu,H., Liao,Z., Ke,W., Wang,B., Song,Y. and Yang,C.
  TITLE     O-GlcNAc transferase regulates intervertebral disc degeneration by
            targeting FAM134B-mediated ER-phagy
  JOURNAL   Exp Mol Med 54 (9), 1472-1485 (2022)
   PUBMED   36056188
  REMARK    GeneRIF: O-GlcNAc transferase regulates intervertebral disc
            degeneration by targeting FAM134B-mediated ER-phagy.
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Wang,C., Li,Y., Li,Y., Du,L., Zhang,J., Li,N., Hu,X., Zhang,W.,
            Xie,N. and Ming,L.
  TITLE     FAM134B-Mediated ER-Phagy in Mg2+-Free Solution-Induced
            Mitochondrial Calcium Homeostasis and Cell Death in Epileptic
            Hippocampal Neurons
  JOURNAL   Neurochem Res 46 (9), 2485-2494 (2021)
   PUBMED   34212292
  REMARK    GeneRIF: FAM134B-Mediated ER-Phagy in Mg(2+)-Free Solution-Induced
            Mitochondrial Calcium Homeostasis and Cell Death in Epileptic
            Hippocampal Neurons.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Xie,N., Li,Y., Wang,C., Lian,Y., Zhang,H., Li,Y., Meng,X. and Du,L.
  TITLE     FAM134B Attenuates Seizure-Induced Apoptosis and Endoplasmic
            Reticulum Stress in Hippocampal Neurons by Promoting Autophagy
  JOURNAL   Cell Mol Neurobiol 40 (8), 1297-1305 (2020)
   PUBMED   32086669
  REMARK    GeneRIF: FAM134B Attenuates Seizure-Induced Apoptosis and
            Endoplasmic Reticulum Stress in Hippocampal Neurons by Promoting
            Autophagy.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Cinque,L., De Leonibus,C., Iavazzo,M., Krahmer,N., Intartaglia,D.,
            Salierno,F.G., De Cegli,R., Di Malta,C., Svelto,M., Lanzara,C.,
            Maddaluno,M., Wanderlingh,L.G., Huebner,A.K., Cesana,M., Bonn,F.,
            Polishchuk,E., Hubner,C.A., Conte,I., Dikic,I., Mann,M.,
            Ballabio,A., Sacco,F., Grumati,P. and Settembre,C.
  TITLE     MiT/TFE factors control ER-phagy via transcriptional regulation of
            FAM134B
  JOURNAL   EMBO J 39 (17), e105696 (2020)
   PUBMED   32716134
  REMARK    GeneRIF: MiT/TFE factors control ER-phagy via transcriptional
            regulation of FAM134B.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Khaminets,A., Heinrich,T., Mari,M., Grumati,P., Huebner,A.K.,
            Akutsu,M., Liebmann,L., Stolz,A., Nietzsche,S., Koch,N., Mauthe,M.,
            Katona,I., Qualmann,B., Weis,J., Reggiori,F., Kurth,I., Hubner,C.A.
            and Dikic,I.
  TITLE     Regulation of endoplasmic reticulum turnover by selective autophagy
  JOURNAL   Nature 522 (7556), 354-358 (2015)
   PUBMED   26040720
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Kurth,I., Pamminger,T., Hennings,J.C., Soehendra,D., Huebner,A.K.,
            Rotthier,A., Baets,J., Senderek,J., Topaloglu,H., Farrell,S.A.,
            Nurnberg,G., Nurnberg,P., De Jonghe,P., Gal,A., Kaether,C.,
            Timmerman,V. and Hubner,C.A.
  TITLE     Mutations in FAM134B, encoding a newly identified Golgi protein,
            cause severe sensory and autonomic neuropathy
  JOURNAL   Nat Genet 41 (11), 1179-1181 (2009)
   PUBMED   19838196
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089887.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089887.1, SRR8487231.59863.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q22"
     Protein         1..480
                     /product="reticulophagy regulator 1"
                     /note="protein FAM134B; reticulophagy receptor FAM134B;
                     reticulophagy receptor 1; family with sequence similarity
                     134, member B"
                     /calculated_mol_wt=52651
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Region          50..242
                     /region_name="RETR1_RHD"
                     /note="N-terminal reticulon-homology domain of
                     Reticulophagy regulator 1; cd22560"
                     /db_xref="CDD:411699"
     Region          67..216
                     /region_name="Reticulon homology domain.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK2B.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Region          <253..>362
                     /region_name="rad2"
                     /note="DNA excision repair protein (rad2); TIGR00600"
                     /db_xref="CDD:273166"
     Region          302..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Region          436..441
                     /region_name="LIR motif.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     Region          450..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM3.1)"
     CDS             1..480
                     /gene="Retreg1"
                     /gene_synonym="Fam134b"
                     /coded_by="NM_001034912.1:88..1530"
                     /db_xref="GeneID:619558"
                     /db_xref="RGD:1565003"
ORIGIN      
        1 maspapeeha tqgcpateeq eprpgvpgee agpegagpqv eeaagrvaaa ltwllgepvl
       61 wlgwradell swkrplrsll aflganllfw flaltpwrvy hlisvmilgr vimqiikdmv
      121 lsrargaqlw rslseswevi nskpderprl shciaeswmn fsiflqemsl fkqqspgkfc
      181 llvcsvctff tilgsyipgv ilsyllllfa flcplfkcnd igqkiyskvk sillkldfgi
      241 geyinqkkre rseadkeksh kddseidfsa lcpkisltva akelsvsdtd vsevswtdng
      301 tfnlsegytp qtdtsddldr pseevfsrdl sdfpslenga gtndedelsl glptelktkk
      361 qqlnsahrps kdrqsaagls lplksdqalh lmsnlagdvi taamtaaikd qlegarqala
      421 qaaptpgddt dteegddfel ldqaeldqie selgltqdqg aeaqqskkss gflsnllggh
//
LOCUS       NP_110489                199 aa            linear   ROD 27-APR-2025
DEFINITION  MARCKS-related protein [Rattus norvegicus].
ACCESSION   NP_110489
VERSION     NP_110489.1
DBSOURCE    REFSEQ: accession NM_030862.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Bjorkblom,B., Padzik,A., Mohammad,H., Westerlund,N., Komulainen,E.,
            Hollos,P., Parviainen,L., Papageorgiou,A.C., Iljin,K.,
            Kallioniemi,O., Kallajoki,M., Courtney,M.J., Magard,M., James,P.
            and Coffey,E.T.
  TITLE     c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines
            actin stability and migration in neurons and in cancer cells
  JOURNAL   Mol Cell Biol 32 (17), 3513-3526 (2012)
   PUBMED   22751924
  REMARK    GeneRIF: c-Jun N-terminal kinase phosphorylation of MARCKSL1
            enables it to bundle and stabilize F-actin, increase filopodium
            numbers and dynamics, and retard migration in neurons.
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Zhao,J., Izumi,T., Nunomura,K., Satoh,S. and Watanabe,S.
  TITLE     MARCKS-like protein, a membrane protein identified for its
            expression in developing neural retina, plays a role in regulating
            retinal cell proliferation
  JOURNAL   Biochem J 408 (1), 51-59 (2007)
   PUBMED   17688421
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Bertaso,F., Lill,Y., Airas,J.M., Espeut,J., Blahos,J., Bockaert,J.,
            Fagni,L., Betz,H. and El-Far,O.
  TITLE     MacMARCKS interacts with the metabotropic glutamate receptor type 7
            and modulates G protein-mediated constitutive inhibition of calcium
            channels
  JOURNAL   J Neurochem 99 (1), 288-298 (2006)
   PUBMED   16987251
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Yang,H., Wang,X., Sumners,C. and Raizada,M.K.
  TITLE     Obligatory role of protein kinase Cbeta and MARCKS in vesicular
            trafficking in living neurons
  JOURNAL   Hypertension 39 (2 Pt 2), 567-572 (2002)
   PUBMED   11882609
  REMARK    GeneRIF: PKCbeta-MARCKS signaling may be a general mechanism for
            the stimulation of vesicular trafficking in brain neurons.
REFERENCE   6  (residues 1 to 199)
  AUTHORS   McNamara,R.K. and Lenox,R.H.
  TITLE     Differential regulation of primary protein kinase C substrate
            (MARCKS, MLP, GAP-43, RC3) mRNAs in the hippocampus during kainic
            acid-induced seizures and synaptic reorganization
  JOURNAL   J Neurosci Res 62 (3), 416-426 (2000)
   PUBMED   11054811
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Chang,S., Hemmings,H.C. Jr. and Aderem,A.
  TITLE     Stimulus-dependent phosphorylation of MacMARCKS, a protein kinase C
            substrate, in nerve termini and PC12 cells
  JOURNAL   J Biol Chem 271 (2), 1174-1178 (1996)
   PUBMED   8557647
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081789.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081789.1, AJ301677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..199
                     /product="MARCKS-related protein"
                     /note="macMARCKS; mac-MARCKS; brain protein F52;
                     MARCKS-like protein 1; macrophage myristoylated
                     alanine-rich C kinase substrate; MARCKS-related
                     protein-like"
                     /calculated_mol_wt=19716
     Region          1..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Region          5..>193
                     /region_name="MARCKS"
                     /note="MARCKS family; pfam02063"
                     /db_xref="CDD:460433"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Region          87..110
                     /region_name="Effector domain involved in lipid-binding
                     and calmodulin-binding.
                     /evidence=ECO:0000250|UniProtKB:P28667"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49006; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P28667; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH2.3)"
     CDS             1..199
                     /gene="Marcksl1"
                     /gene_synonym="F52; Mlp"
                     /coded_by="NM_030862.2:183..782"
                     /db_xref="GeneID:81520"
                     /db_xref="RGD:621197"
ORIGIN      
        1 mgsqsskapr gdvtaeeaag aspakangqe nghvksngdl tpkgegespp vngadeaaga
       61 tgdaiepapp sqeaeakgev apketpkkkk kfsfkkpfkl sglsfkrnrk egggdssass
      121 pteeeqeqge isacsdegta qegkaaatpe sqepqakgae asavskggda eeeagpqaae
      181 pstpsgpesg pasasaene
//
LOCUS       NP_001004081             423 aa            linear   ROD 27-APR-2025
DEFINITION  mannose-6-phosphate isomerase [Rattus norvegicus].
ACCESSION   NP_001004081 XP_217168
VERSION     NP_001004081.1
DBSOURCE    REFSEQ: accession NM_001004081.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Harada,Y., Nakajima,K., Masahara-Negishi,Y., Freeze,H.H.,
            Angata,T., Taniguchi,N. and Suzuki,T.
  TITLE     Metabolically programmed quality control system for dolichol-linked
            oligosaccharides
  JOURNAL   Proc Natl Acad Sci U S A 110 (48), 19366-19371 (2013)
   PUBMED   24218558
REFERENCE   2  (residues 1 to 423)
  AUTHORS   DeRossi,C., Bode,L., Eklund,E.A., Zhang,F., Davis,J.A.,
            Westphal,V., Wang,L., Borowsky,A.D. and Freeze,H.H.
  TITLE     Ablation of mouse phosphomannose isomerase (Mpi) causes mannose
            6-phosphate accumulation, toxicity, and embryonic lethality
  JOURNAL   J Biol Chem 281 (9), 5916-5927 (2006)
   PUBMED   16339137
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Niehues,R., Hasilik,M., Alton,G., Korner,C., Schiebe-Sukumar,M.,
            Koch,H.G., Zimmer,K.P., Wu,R., Harms,E., Reiter,K., von Figura,K.,
            Freeze,H.H., Harms,H.K. and Marquardt,T.
  TITLE     Carbohydrate-deficient glycoprotein syndrome type Ib.
            Phosphomannose isomerase deficiency and mannose therapy
  JOURNAL   J Clin Invest 101 (7), 1414-1420 (1998)
   PUBMED   9525984
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Otto,J. and von Deimling,O.H.
  TITLE     Esterase-17 (ES-17): characterization and genetic location on
            chromosome 9 of a bis-p-nitrophenyl phosphate-resistant esterase of
            the house mouse (Mus musculus)
  JOURNAL   Biochem Genet 21 (1-2), 37-48 (1983)
   PUBMED   6838491
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Stallings,R.L. and Siciliano,M.J.
  TITLE     Confirmational, provisional, and/or regional assignment of 15
            enzyme loci onto Chinese hamster autosomes 1, 2, and 7
  JOURNAL   Somatic Cell Genet 7 (6), 683-698 (1981)
   PUBMED   7323947
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Schafer,R., Doehmer,J., Rademacher,I. and Willecke,K.
  TITLE     Assignment of the gene for cytoplasmic glutamate-oxaloacetate
            transaminase to mouse chromosome 19 using chinese hamster x mouse
            somatic cell hybrids
  JOURNAL   Somatic Cell Genet 6 (6), 709-717 (1980)
   PUBMED   7444718
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for thymidine kinase and galactokinase to
            Mus musculus chromosome 11 and the preferential segregation of this
            chromosome in Chinese hamster/mouse somatic cell hybrids
  JOURNAL   Somatic Cell Genet 3 (2), 121-133 (1977)
   PUBMED   204065
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Kozak,C., Nichols,E. and Ruddle,F.H.
  TITLE     Gene linkage analysis in the mouse by somatic cell hybridization:
            assignment of adenine phosphoribosyltransferase to chromosome 8 and
            alpha-galactosidase to the X chromosome
  JOURNAL   Somatic Cell Genet 1 (4), 371-382 (1975)
   PUBMED   1235912
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Nichols,E.A., Chapman,V.M. and Ruddle,F.H.
  TITLE     Polymorphism and linkage for mannosephosphate isomerase in Mus
            musculus
  JOURNAL   Biochem Genet 8 (1), 47-53 (1973)
   PUBMED   4693062
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079111.1.
            
            On Sep 3, 2004 this sequence version replaced XP_217168.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079111.1, SRR8487226.156089.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..423
                     /product="mannose-6-phosphate isomerase"
                     /EC_number="5.3.1.8"
                     /note="PMI; phosphohexomutase; phosphomannose isomerase"
                     /calculated_mol_wt=46293
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P34949; propagated from
                     UniProtKB/Swiss-Prot (Q68FX1.1)"
     Region          9..404
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Site            order(18,48,50,99,107..108,110,112,135,137,139,276,278,
                     285,287,291,295)
                     /site_type="active"
                     /db_xref="CDD:380414"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34949; propagated from
                     UniProtKB/Swiss-Prot (Q68FX1.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34949; propagated from
                     UniProtKB/Swiss-Prot (Q68FX1.1)"
     CDS             1..423
                     /gene="Mpi"
                     /coded_by="NM_001004081.1:11..1282"
                     /db_xref="GeneID:300741"
                     /db_xref="RGD:3107"
ORIGIN      
        1 manprvfpls cvvqqyawgk vgsksevacl lacsdpltqi sedkpyaelw mgahprgdak
       61 ildnrisqkt lgqwiaenqn slgqkvkdtf ngklpflfkv lsvetalsiq ahpnkelaek
      121 lhlqapehyp danhkpemai altpfqglcg frpveeivtf lkkvpefqsl igedataqlk
      181 ksmnegsgam asalkncfsh lmksekkvvv eqlnllvkri sqqisngnsm ddicgelllq
      241 lhqqypgdig cfaiyllnli tlkpgeamfl eanvphaylk gdcvecmacs dntvragltp
      301 kfidvstlce mldytpspsk drlfaptlsq ddpylsiydp pvpdftvmki evpgsvteyk
      361 vltldsasil llvqgtvtai ipsvqgeipl srggvlfiga netvllkltv pknllifrac
      421 cll
//
LOCUS       NP_001004257             509 aa            linear   ROD 27-APR-2025
DEFINITION  heat shock 70 kDa protein 14 [Rattus norvegicus].
ACCESSION   NP_001004257 XP_225576
VERSION     NP_001004257.1
DBSOURCE    REFSEQ: accession NM_001004257.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Hageman,J., van Waarde,M.A., Zylicz,A., Walerych,D. and
            Kampinga,H.H.
  TITLE     The diverse members of the mammalian HSP70 machine show distinct
            chaperone-like activities
  JOURNAL   Biochem J 435 (1), 127-142 (2011)
   PUBMED   21231916
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Otto,H., Conz,C., Maier,P., Wolfle,T., Suzuki,C.K., Jeno,P.,
            Rucknagel,P., Stahl,J. and Rospert,S.
  TITLE     The chaperones MPP11 and Hsp70L1 form the mammalian
            ribosome-associated complex
  JOURNAL   Proc Natl Acad Sci U S A 102 (29), 10064-10069 (2005)
   PUBMED   16002468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079118.1.
            
            On Sep 10, 2004 this sequence version replaced XP_225576.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079118.1, SRR8487227.53443.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..509
                     /product="heat shock 70 kDa protein 14"
                     /note="heat shock protein hsp70-related protein; heat
                     shock 70kDa protein 14; heat shock protein 14; heat shock
                     protein family A, member 14"
                     /calculated_mol_wt=54332
     Region          2..378
                     /region_name="ASKHA_NBD_HSP70_HSPA14"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 14 (HSPA14) and similar proteins; cd10238"
                     /db_xref="CDD:466836"
     CDS             1..509
                     /gene="Hspa14"
                     /coded_by="NM_001004257.1:68..1597"
                     /db_xref="GeneID:307133"
                     /db_xref="RGD:1303296"
ORIGIN      
        1 maaigvhlgc tsacvavykd gradvvanda gdrvtpavva ysereqvvgl aakqsrirni
       61 sstvvkvkqi lgrstadpqa qkyiseskcl viekngklqy eidtgeetkl vspedvarli
      121 fskmketahs vlgsdandvv vtvpfdfgek qksalgeaag aagfnvlrli hepsaallay
      181 gigqdcptgk snvlvfklgg tslslsimev nsgmyrvlst ntsdniggvh ftdslaqyla
      241 sefqrlfkhd vrgsarammk lmnsaevakh slstlgsanc fvdslyegqd fdcnvsrarf
      301 ellcsplfnk cieavrallq qsgftaddin kvvlcggssr iprlqqlikd lfpagdllns
      361 ippdevipig aaieagilvg kestsgddsv liecsardil vkgvdesgan rftvlfpsgt
      421 plparrqhtl qapgsissvc lelyesegkn svkeetkfaq vvlqdldkke nglrdilavl
      481 tmkrdgslqv tctdqetgkc eaitvevas
//
LOCUS       NP_001019469             243 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 174 [Rattus norvegicus].
ACCESSION   NP_001019469 XP_574840
VERSION     NP_001019469.1
DBSOURCE    REFSEQ: accession NM_001024298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Miyazaki-Anzai,S., Keenan,A.L., Blaine,J. and Miyazaki,M.
  TITLE     Targeted Disruption of a Proximal Tubule-Specific TMEM174 Gene in
            Mice Causes Hyperphosphatemia and Vascular Calcification
  JOURNAL   J Am Soc Nephrol 33 (8), 1477-1486 (2022)
   PUBMED   35459732
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079357.1.
            
            On May 27, 2005 this sequence version replaced XP_574840.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079357.1, CK481830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..243
                     /product="transmembrane protein 174"
                     /calculated_mol_wt=26347
     Region          9..241
                     /region_name="TMEM174"
                     /note="Transmembrane protein 174; pfam15029"
                     /db_xref="CDD:434404"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FU0.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FU0.1)"
     Region          205..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FU0.1)"
     CDS             1..243
                     /gene="Tmem174"
                     /coded_by="NM_001024298.1:28..759"
                     /db_xref="GeneID:499516"
                     /db_xref="RGD:1561129"
ORIGIN      
        1 meqssnrped fplnvfsvtp ytpstadiqv sdddkagatl lfsgiflglv gitftvmgwi
       61 kyqgvshfew tqllgpills vgvtfilisv ckfkmlscql ctdneervld sdqtsggqsf
      121 vftginqpit fhgatvvqyi pppygsqepl gmnttylqpm mnpcglvpss gavaatpspp
      181 qyytiypqdn aafvesegfs pfvgaghdrp ssdadqlegt qmgeeervcf spppyeeiya
      241 lpr
//
LOCUS       NP_075211                249 aa            linear   ROD 27-APR-2025
DEFINITION  triosephosphate isomerase [Rattus norvegicus].
ACCESSION   NP_075211
VERSION     NP_075211.2
DBSOURCE    REFSEQ: accession NM_022922.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Lei,M., Tao,M.Q., Wu,Y.J., Xu,L., Yang,Z., Li,Y., Olatunji,O.J.,
            Wang,X.W. and Zuo,J.
  TITLE     Metabolic Enzyme Triosephosphate Isomerase 1 and Nicotinamide
            Phosphoribosyltransferase, Two Independent Inflammatory Indicators
            in Rheumatoid Arthritis: Evidences From Collagen-Induced Arthritis
            and Clinical Samples
  JOURNAL   Front Immunol 12, 795626 (2022)
   PUBMED   35111160
  REMARK    GeneRIF: Metabolic Enzyme Triosephosphate Isomerase 1 and
            Nicotinamide Phosphoribosyltransferase, Two Independent
            Inflammatory Indicators in Rheumatoid Arthritis: Evidences From
            Collagen-Induced Arthritis and Clinical Samples.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Martins-de-Souza,D., Alsaif,M., Ernst,A., Harris,L.W., Aerts,N.,
            Lenaerts,I., Peeters,P.J., Amess,B., Rahmoune,H., Bahn,S. and
            Guest,P.C.
  TITLE     The application of selective reaction monitoring confirms
            dysregulation of glycolysis in a preclinical model of schizophrenia
  JOURNAL   BMC Res Notes 5, 146 (2012)
   PUBMED   22420779
  REMARK    GeneRIF: Data show statistically significant altered levels of Tpi1
            and alteration of Hk1, Aldoc, Pgam1 and Gapdh with borderline
            significance in phencyclidine (PCP) rats compared to controls.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 249)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Brand,I.A. and Heinickel,A.
  TITLE     Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa
            Zn(2+)-binding protein (parathymosin)
  JOURNAL   J Biol Chem 266 (31), 20984-20989 (1991)
   PUBMED   1834654
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Merkle,S. and Pretsch,W.
  TITLE     Characterization of triosephosphate isomerase mutants with reduced
            enzyme activity in Mus musculus
  JOURNAL   Genetics 123 (4), 837-844 (1989)
   PUBMED   2693209
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Minna,J.D., Bruns,G.A., Krinsky,A.H., Lalley,P.A., Francke,U. and
            Gerald,P.S.
  TITLE     Assignment of a Mus musculus gene for triosephosphate isomerase to
            chromosome 6 and for glyoxalase-I to chromosome 17 using somatic
            cell hybrids
  JOURNAL   Somatic Cell Genet 4 (2), 241-252 (1978)
   PUBMED   566476
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Leinwand,L.A., Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for triose phosphate isomerase to
            chromosome 6 and tripeptidase-1 to chromosome 10 in Mus musculus by
            somatic cell hybridization
  JOURNAL   Somatic Cell Genet 4 (2), 233-240 (1978)
   PUBMED   566475
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for thymidine kinase and galactokinase to
            Mus musculus chromosome 11 and the preferential segregation of this
            chromosome in Chinese hamster/mouse somatic cell hybrids
  JOURNAL   Somatic Cell Genet 3 (2), 121-133 (1977)
   PUBMED   204065
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC126087.1.
            
            On Nov 13, 2006 this sequence version replaced NP_075211.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK356973.1, FQ212675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..249
                     /product="triosephosphate isomerase"
                     /EC_number="5.3.1.1"
                     /EC_number="4.2.3.3"
                     /note="TIM; triose-phosphate isomerase; methylglyoxal
                     synthase; triosephosphate isomerase-like"
                     /calculated_mol_wt=26718
     Region          2..247
                     /region_name="PTZ00333"
                     /note="triosephosphate isomerase; Provisional"
                     /db_xref="CDD:240365"
     Site            order(12,14,96,166,172,212,231,233..234)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238190"
     Site            order(12,15,46..48,50,53,65,83,86..87,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238190"
     Site            order(14,96,166)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238190"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            156
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P17751; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P17751; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            194
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            194
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60174; propagated from
                     UniProtKB/Swiss-Prot (P48500.2)"
     CDS             1..249
                     /gene="Tpi1"
                     /gene_synonym="Tpi"
                     /coded_by="NM_022922.2:25..774"
                     /db_xref="GeneID:24849"
                     /db_xref="RGD:3896"
ORIGIN      
        1 mapsrkffvg gnwkmngrkk clgelictln aaklpadtev vcapptayid farqkldpki
       61 avaaqncykv tngaftgeis pgmikdlgat wvvlghserr hifgesdeli gqkvnhalse
      121 glgviacige kldereagit ekvvfeqtka iadnvkdwck vvlayepvwa igtgktatpq
      181 qaqevheklr gwlkcnvseg vaqctriiyg gsvtgatcke lasqpdvdgf lvggaslkpe
      241 fvdiinakq
//
LOCUS       NP_067605                356 aa            linear   ROD 27-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF1 [Rattus
            norvegicus].
ACCESSION   NP_067605
VERSION     NP_067605.1
DBSOURCE    REFSEQ: accession NM_021594.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Tachikawa,M., Yokoyama,R., Akanuma,S.I. and Hosoya,K.I.
  TITLE     Assembly of Taurine Transporter (Slc6a6) with Na+-H+ Exchanger
            Regulatory Factor 1 (Slc9a3r1) Improves GABA Transport Activity by
            Increasing the Maximum Transport Velocity
  JOURNAL   Biol Pharm Bull 41 (3), 338-341 (2018)
   PUBMED   29491210
  REMARK    GeneRIF: The purpose of this study was to clarify the assembly of
            taurine transporter (TauT/Slc6a6) and PSD-95/Disc-large/Zo-1 (PDZ)
            domain of Slc9a3r1 as a regulatory mechanism of Slc6a6-mediated
            GABA transport activity
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Lu,X., He,L., Zhou,Q., Wang,M., Shen,W.J., Azhar,S., Pan,F., Guo,Z.
            and Hu,Z.
  TITLE     NHERF1 and NHERF2 regulation of SR-B1 stability via ubiquitination
            and proteasome degradation
  JOURNAL   Biochem Biophys Res Commun 490 (4), 1168-1175 (2017)
   PUBMED   28669731
  REMARK    GeneRIF: The results suggest that NHERF1 and NHERF2 down-regulated
            SR-B1 at least in part via the ubiquitin/proteasome pathway.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Barati,M.T., Ketchem,C.J., Merchant,M.L., Kusiak,W.B., Jose,P.A.,
            Weinman,E.J., LeBlanc,A.J., Lederer,E.D. and Khundmiri,S.J.
  TITLE     Loss of NHERF-1 expression prevents dopamine-mediated Na-K-ATPase
            regulation in renal proximal tubule cells from rat models of
            hypertension: aged F344 rats and spontaneously hypertensive rats
  JOURNAL   Am J Physiol Cell Physiol 313 (2), C197-C206 (2017)
   PUBMED   28515088
  REMARK    GeneRIF: These results suggest that decreased renal NHERF-1
            expression contributes to the impaired dopamine-mediated inhibition
            of NKA in PTCs from animal models of hypertension.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Ritter-Makinson,S.L., Paquet,M., Bogenpohl,J.W., Rodin,R.E., Chris
            Yun,C., Weinman,E.J., Smith,Y. and Hall,R.A.
  TITLE     Group II metabotropic glutamate receptor interactions with NHERF
            scaffold proteins: Implications for receptor localization in brain
  JOURNAL   Neuroscience 353, 58-75 (2017)
   PUBMED   28392297
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Briffa,J.F., Grinfeld,E., Jenkin,K.A., Mathai,M.L., Poronnik,P.,
            McAinch,A.J. and Hryciw,D.H.
  TITLE     Diet induced obesity in rats reduces NHE3 and Na(+) /K(+) -ATPase
            expression in the kidney
  JOURNAL   Clin Exp Pharmacol Physiol 42 (10), 1118-1126 (2015)
   PUBMED   26173747
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Shenolikar,S., Voltz,J.W., Minkoff,C.M., Wade,J.B. and Weinman,E.J.
  TITLE     Targeted disruption of the mouse NHERF-1 gene promotes
            internalization of proximal tubule sodium-phosphate cotransporter
            type IIa and renal phosphate wasting
  JOURNAL   Proc Natl Acad Sci U S A 99 (17), 11470-11475 (2002)
   PUBMED   12169661
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Bonilha,V.L. and Rodriguez-Boulan,E.
  TITLE     Polarity and developmental regulation of two PDZ proteins in the
            retinal pigment epithelium
  JOURNAL   Invest Ophthalmol Vis Sci 42 (13), 3274-3282 (2001)
   PUBMED   11726633
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Takeda,T., McQuistan,T., Orlando,R.A. and Farquhar,M.G.
  TITLE     Loss of glomerular foot processes is associated with uncoupling of
            podocalyxin from the actin cytoskeleton
  JOURNAL   J Clin Invest 108 (2), 289-301 (2001)
   PUBMED   11457882
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Fouassier,L., Yun,C.C., Fitz,J.G. and Doctor,R.B.
  TITLE     Evidence for ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50)
            self-association through PDZ-PDZ interactions
  JOURNAL   J Biol Chem 275 (32), 25039-25045 (2000)
   PUBMED   10859298
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Hall,R.A., Premont,R.T., Chow,C.W., Blitzer,J.T., Pitcher,J.A.,
            Claing,A., Stoffel,R.H., Barak,L.S., Shenolikar,S., Weinman,E.J.,
            Grinstein,S. and Lefkowitz,R.J.
  TITLE     The beta2-adrenergic receptor interacts with the Na+/H+-exchanger
            regulatory factor to control Na+/H+ exchange
  JOURNAL   Nature 392 (6676), 626-630 (1998)
   PUBMED   9560162
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF154336.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF154336.1, FQ213792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..356
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF1"
                     /note="EBP50; NHERF-1; regulatory cofactor of Na(+)/H(+)
                     exchanger; sodium-hydrogen exchanger regulatory factor 1;
                     ezrin-radixin-moesin-binding phosphoprotein 50; solute
                     carrier family 9, subfamily A (NHE3, cation proton
                     antiporter 3), member 3 regulator 1; solute carrier family
                     9 (sodium/hydrogen exchanger), member 3 regulator 1;
                     ERM-binding phosphoprotein; SLC9A3 regulator 1"
                     /calculated_mol_wt=38699
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O14745; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Region          13..92
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(23..29,40,43,72,76,79..80)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14745; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Region          113..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Region          150..229
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(160..166,177,180,209,213,216..217)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          232..356
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     Region          265..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14745; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ19.3)"
     CDS             1..356
                     /gene="Nherf1"
                     /gene_synonym="Slc9a3r1"
                     /coded_by="NM_021594.1:70..1140"
                     /db_xref="GeneID:59114"
                     /db_xref="RGD:708538"
ORIGIN      
        1 msadaaagep lprlcclekg pngygfhlhg ekgkvgqfir lvepgspaek sgllagdrlv
       61 evngenveke thqqvvsrir aalnavrllv vdpetdeqlk klgvpireel lraqekseht
      121 eppaaadtkk agdqneaeks hlercelrpr lctmkkgpng ygfnlhsdks kpgqfiravd
      181 pdspaeasgl raqdrivevn gvcmegkqhg dvvsaikagg deakllvvdk etdeffkkcr
      241 vtpsqehldg plpepfsnge iqkensreal vepasesprp alarsassdt seelnaqdsp
      301 krhdstepss tssssdpild fnislavake rahqkrsskr apqmdwskkn elfsnl
//
LOCUS       NP_001020067             330 aa            linear   ROD 27-APR-2025
DEFINITION  inactive hydroxysteroid dehydrogenase-like protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001020067 XP_341697
VERSION     NP_001020067.1
DBSOURCE    REFSEQ: accession NM_001024896.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Meier,M., Tokarz,J., Haller,F., Mindnich,R. and Adamski,J.
  TITLE     Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1)
            proteins are inactive enzymes but conserved among species
  JOURNAL   Chem Biol Interact 178 (1-3), 197-205 (2009)
   PUBMED   19026618
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097457.1.
            
            On Jun 17, 2005 this sequence version replaced XP_341697.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097457.1, CR755461.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155336, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..330
                     /product="inactive hydroxysteroid dehydrogenase-like
                     protein 1"
                     /calculated_mol_wt=36777
     Region          2..82
                     /region_name="Required for mitochondria translocation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q3SXM5; propagated from
                     UniProtKB/Swiss-Prot (Q4V8B7.1)"
     Region          67..309
                     /region_name="17beta-HSD1_like_SDR_c"
                     /note="17-beta-hydroxysteroid dehydrogenases (17beta-HSDs)
                     types -1, -3, and -12, -like, classical (c) SDRs; cd05356"
                     /db_xref="CDD:187614"
     Site            order(74,76..79,98..100,123..125,151..153,176,203..205,
                     218,222,248..251,253..254)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187614"
     Site            order(177,205,218,222)
                     /site_type="active"
                     /db_xref="CDD:187614"
     CDS             1..330
                     /gene="Hsdl1"
                     /gene_synonym="RGD1308433"
                     /coded_by="NM_001024896.1:325..1317"
                     /db_xref="GeneID:361418"
                     /db_xref="RGD:1308433"
ORIGIN      
        1 maavdsfyll yreiarscsc yvealalvga wytarksipv icdfyslvrl hfiprlgsrp
       61 dlikqygrwa visgatdgig kayaeelash glniilisqe eeklqavakh iadtyrvetl
      121 vlvadfsrgr eiyapireal rdrdigilvn dvgafypypq yfsqvpedti wdivnvniaa
      181 aslmvhivlp gmverkkgai vtvssgscck ptpqlaafsa skayldhfsr alqyeyaskg
      241 ifvqslipfy vtssvtapgs flrrcpwlap sprvyaqhav stlgiskrtt gywshsiqfl
      301 faqympewlw vwganllnrs lrkealssqa
//
LOCUS       NP_742038                422 aa            linear   ROD 27-APR-2025
DEFINITION  potassium channel subfamily K member 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_742038
VERSION     NP_742038.2
DBSOURCE    REFSEQ: accession NM_172041.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Li,T., Fei,J., Yu,H., Wang,X., Li,D. and Yin,Z.
  TITLE     Prolonged stretching of rat uteri causes hypoxia and inhibits
            contractility via potassium channel TREK1
  JOURNAL   Reproduction 166 (1), 55-64 (2023)
   PUBMED   37184053
  REMARK    GeneRIF: Prolonged stretching of rat uteri causes hypoxia and
            inhibits contractility via potassium channel TREK1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Kanda,H., Noguchi,K. and Dai,Y.
  TITLE     Axonal membrane stretch suppresses neuronal excitability by
            activating mechanosensitive K2P channels at the node of Ranvier
  JOURNAL   Mol Brain 16 (1), 8 (2023)
   PUBMED   36650581
  REMARK    GeneRIF: Axonal membrane stretch suppresses neuronal excitability
            by activating mechanosensitive K2P channels at the node of Ranvier.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Ulkumen,B., Artunc Ulkumen,B., Batir,M.B., Cam,S. and Vatansever,S.
  TITLE     The Role of TREK-1 and AQP5 in Gonadocorticoid-Related Voice
            Disorders
  JOURNAL   J Voice 36 (2), 150-155 (2022)
   PUBMED   32439217
  REMARK    GeneRIF: The Role of TREK-1 and AQP5 in Gonadocorticoid-Related
            Voice Disorders.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Garcia,G., Mendez-Resendiz,K.A., Oviedo,N. and Murbartian,J.
  TITLE     PKC- and PKA-dependent phosphorylation modulates TREK-1 function in
            naive and neuropathic rats
  JOURNAL   J Neurochem 157 (6), 2039-2054 (2021)
   PUBMED   33006141
  REMARK    GeneRIF: PKC- and PKA-dependent phosphorylation modulates TREK-1
            function in naive and neuropathic rats.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Li,R., Zhao,K., Ruan,Q., Meng,C. and Yin,F.
  TITLE     The transcription factor Foxd3 induces spinal cord
            ischemia-reperfusion injury by potentiating microRNA-214-dependent
            inhibition of Kcnk2
  JOURNAL   Exp Mol Med 52 (1), 118-129 (2020)
   PUBMED   31959866
  REMARK    GeneRIF: The transcription factor Foxd3 induces spinal cord
            ischemia-reperfusion injury by potentiating microRNA-214-dependent
            inhibition of Kcnk2.
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Koh,S.D., Monaghan,K., Sergeant,G.P., Ro,S., Walker,R.L.,
            Sanders,K.M. and Horowitz,B.
  TITLE     TREK-1 regulation by nitric oxide and cGMP-dependent protein
            kinase. An essential role in smooth muscle inhibitory
            neurotransmission
  JOURNAL   J Biol Chem 276 (47), 44338-44346 (2001)
   PUBMED   11560940
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Terrenoire,C., Lauritzen,I., Lesage,F., Romey,G. and Lazdunski,M.
  TITLE     A TREK-1-like potassium channel in atrial cells inhibited by
            beta-adrenergic stimulation and activated by volatile anesthetics
  JOURNAL   Circ Res 89 (4), 336-342 (2001)
   PUBMED   11509450
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Bockenhauer,D., Zilberberg,N. and Goldstein,S.A.
  TITLE     KCNK2: reversible conversion of a hippocampal potassium leak into a
            voltage-dependent channel
  JOURNAL   Nat Neurosci 4 (5), 486-491 (2001)
   PUBMED   11319556
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Hervieu,G.J., Cluderay,J.E., Gray,C.W., Green,P.J., Ranson,J.L.,
            Randall,A.D. and Meadows,H.J.
  TITLE     Distribution and expression of TREK-1, a two-pore-domain potassium
            channel, in the adult rat CNS
  JOURNAL   Neuroscience 103 (4), 899-919 (2001)
   PUBMED   11301200
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Bearzatto,B., Lesage,F., Reyes,R., Lazdunski,M. and Laduron,P.M.
  TITLE     Axonal transport of TREK and TRAAK potassium channels in rat
            sciatic nerves
  JOURNAL   Neuroreport 11 (5), 927-930 (2000)
   PUBMED   10790857
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ403851.1.
            
            On Mar 24, 2007 this sequence version replaced NP_742038.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ403851.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..422
                     /product="potassium channel subfamily K member 2 isoform
                     1"
                     /note="tandem-pore-domain potassium channel TREK-1; ion
                     transport membrane protein; arachidonic acid sensitive
                     tandem pore domain potassium channel; potassium channel,
                     two pore domain subfamily K, member 2; TREK-1 K(+) channel
                     subunit; two pore potassium channel TPKC1; two pore domain
                     potassium channel TREK-1; stretch-activated potassium
                     channel TREK-1; outward rectifying potassium channel
                     protein TREK-1; potassium channel subfamily K member 2"
                     /calculated_mol_wt=46667
     Region          <134..192
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          230..308
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     CDS             1..422
                     /gene="Kcnk2"
                     /gene_synonym="rTREK1d; Trek-1"
                     /coded_by="NM_172041.2:68..1336"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:170899"
                     /db_xref="RGD:621448"
ORIGIN      
        1 mmnprakrsv ylaapdlldp ksaaqnskpr lsfsakptvl asrvesdsai nvmkwktvst
       61 iflvvvlyli igatvfkale qpqeisqrtt iviqkqnfia qhacvnstel deliqqivta
      121 inagiiplgn nsnqvshwdl gssfffagtv ittigfgnis prteggkifc iiyallgipl
      181 fgfllagvgd qlgtifgkgi akvedtfikw nvsqtkirii stiifilfgc vlfvalpavi
      241 fkhiegwsal daiyfvvitl ttigfgdyva ggsdieyldf ykpvvwfwil vglayfaavl
      301 smigdwlrvi skktkeevge frahaaewta nvtaefketr rrlsveiydk fqratsvkrk
      361 lsaelagnhn qeltpcrrtl svnhltsere vlppllkaes iylngltphc arediavien
      421 mk
//
LOCUS       NP_001020316             408 aa            linear   ROD 27-APR-2025
DEFINITION  protein ZNF365 [Rattus norvegicus].
ACCESSION   NP_001020316 XP_574746
VERSION     NP_001020316.1
DBSOURCE    REFSEQ: accession NM_001025145.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Koyama,Y., Hattori,T., Nishida,T., Hori,O. and Tohyama,M.
  TITLE     Alterations in dendrite and spine morphology of cortical pyramidal
            neurons in DISC1-binding zinc finger protein (DBZ) knockout mice
  JOURNAL   Front Neuroanat 9, 52 (2015)
   PUBMED   25983680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Shimizu,S., Koyama,Y., Hattori,T., Tachibana,T., Yoshimi,T.,
            Emoto,H., Matsumoto,Y., Miyata,S., Katayama,T., Ito,A. and
            Tohyama,M.
  TITLE     DBZ, a CNS-specific DISC1 binding protein, positively regulates
            oligodendrocyte differentiation
  JOURNAL   Glia 62 (5), 709-724 (2014)
   PUBMED   24481677
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Koyama,Y., Hattori,T., Shimizu,S., Taniguchi,M., Yamada,K.,
            Takamura,H., Kumamoto,N., Matsuzaki,S., Ito,A., Katayama,T. and
            Tohyama,M.
  TITLE     DBZ (DISC1-binding zinc finger protein)-deficient mice display
            abnormalities in basket cells in the somatosensory cortices
  JOURNAL   J Chem Neuroanat 53, 1-10 (2013)
   PUBMED   23912123
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Zhang,Y., Park,E., Kim,C.S. and Paik,J.H.
  TITLE     ZNF365 promotes stalled replication forks recovery to maintain
            genome stability
  JOURNAL   Cell Cycle 12 (17), 2817-2828 (2013)
   PUBMED   23966166
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Zhang,Y., Shin,S.J., Liu,D., Ivanova,E., Foerster,F., Ying,H.,
            Zheng,H., Xiao,Y., Chen,Z., Protopopov,A., Depinho,R.A. and
            Paik,J.H.
  TITLE     ZNF365 promotes stability of fragile sites and telomeres
  JOURNAL   Cancer Discov 3 (7), 798-811 (2013)
   PUBMED   23776040
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Hattori,T., Baba,K., Matsuzaki,S., Honda,A., Miyoshi,K., Inoue,K.,
            Taniguchi,M., Hashimoto,H., Shintani,N., Baba,A., Shimizu,S.,
            Yukioka,F., Kumamoto,N., Yamaguchi,A., Tohyama,M. and Katayama,T.
  TITLE     A novel DISC1-interacting partner DISC1-Binding Zinc-finger
            protein: implication in the modulation of DISC1-dependent neurite
            outgrowth
  JOURNAL   Mol Psychiatry 12 (4), 398-407 (2007)
   PUBMED   17389905
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Wang,Q., Du,X., Meinkoth,J., Hirohashi,Y., Zhang,H., Liu,Q.,
            Richter,M. and Greene,M.I.
  TITLE     Characterization of Su48, a centrosome protein essential for cell
            division
  JOURNAL   Proc Natl Acad Sci U S A 103 (17), 6512-6517 (2006)
   PUBMED   16617106
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087056.1.
            
            On Jul 1, 2005 this sequence version replaced XP_574746.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087056.1, SRR8487227.221551.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132274, SAMD00132284
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p11"
     Protein         1..408
                     /product="protein ZNF365"
                     /note="DISC1-binding zinc-finger protein"
                     /calculated_mol_wt=46837
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS2.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS2.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG89; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS2.1)"
     Region          <170..>291
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS2.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS2.1)"
     CDS             1..408
                     /gene="Zfp365"
                     /gene_synonym="Znf365"
                     /coded_by="NM_001025145.1:222..1448"
                     /db_xref="GeneID:499425"
                     /db_xref="RGD:1565986"
ORIGIN      
        1 mqqttfeesr yrwqdslenv avclpfrcpr cgdhtrfrsl sslrahlefs hsyeertllt
       61 kcsllpslkd tdllrsselp kqgkllrgha kvtkqkpsyv nlysishghs kdpkpfemva
      121 erpvsyvqty tavdiradsl daprsssglp tqdtkaafea hvrekfnrmv eavdrtiekr
      181 idkltkelaq ktaellevra afvqltqkkq evqrreralh kqvdvavemi avlkqrltes
      241 eeellrkeee vvtfnhflea aaekevqgka rlqdfienll qrvelaekql eyyqsqqasg
      301 fshdtsehml tdisssrksr clsrghqhsv cnhpelkahf hlkgrsylkk akderagmqp
      361 akaiheqaes preffrpakk gehlglsrkg nfrpkmakkk ptaivnii
//
LOCUS       NP_001099692             285 aa            linear   ROD 27-APR-2025
DEFINITION  ret finger protein-like 4A [Rattus norvegicus].
ACCESSION   NP_001099692 XP_001072525 XP_218194
VERSION     NP_001099692.1
DBSOURCE    REFSEQ: accession NM_001106222.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Suzumori,N., Burns,K.H., Yan,W. and Matzuk,M.M.
  TITLE     RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
            degradation pathway
  JOURNAL   Proc Natl Acad Sci U S A 100 (2), 550-555 (2003)
   PUBMED   12525704
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474075.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_218194.3, XP_001072525.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..285
                     /product="ret finger protein-like 4A"
                     /note="ret finger protein-like 4"
                     /calculated_mol_wt=32352
     Region          9..56
                     /region_name="vRING-HC-C4C4_RFPL"
                     /note="Variant RING finger, HC subclass (C4C4-type), found
                     in Ret finger protein-like (RFPL) family; cd16621"
                     /db_xref="CDD:438283"
     Region          54..95
                     /region_name="RDM"
                     /note="RFPL defining motif (RDM); pfam11002"
                     /db_xref="CDD:463205"
     Region          94..270
                     /region_name="SPRY_PRY_RFPL"
                     /note="Ret finger protein-like (RFPL), includes RFP1, 2,
                     3, 4; cd15821"
                     /db_xref="CDD:293993"
     CDS             1..285
                     /gene="Rfpl4a"
                     /gene_synonym="Rfpl4"
                     /coded_by="NM_001106222.1:271..1128"
                     /db_xref="GeneID:292583"
                     /db_xref="RGD:1307409"
ORIGIN      
        1 mahffkenss cyfcfrylen pvylncgyic cfqcldslek spegdgvlcp ncsvvslked
       61 irhakqlrnl vttvkdlepq lnfiltmdps mkifqvnmil dvdtaqnnli isedlrsvyh
      121 tsqtqdrkkc aerfdpspcv lgssrftsgc hywevvvgts kewdigicke sinrqevvyl
      181 sekkgfwtvg vrneevyaas tdpltvllvn prlhrvgifl dlleksvsfw dlgdgshiyt
      241 fleipdtepf rpffspanty pdeeqvisic pvmnpsifgl pvnpv
//
LOCUS       NP_001019503             186 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 8B [Rattus norvegicus].
ACCESSION   NP_001019503 XP_575632
VERSION     NP_001019503.1
DBSOURCE    REFSEQ: accession NM_001024332.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Vukoja,A., Rey,U., Petzoldt,A.G., Ott,C., Vollweiter,D.,
            Quentin,C., Puchkov,D., Reynolds,E., Lehmann,M., Hohensee,S.,
            Rosa,S., Lipowsky,R., Sigrist,S.J. and Haucke,V.
  TITLE     Presynaptic Biogenesis Requires Axonal Transport of
            Lysosome-Related Vesicles
  JOURNAL   Neuron 99 (6), 1216-1232 (2018)
   PUBMED   30174114
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Pu,J., Schindler,C., Jia,R., Jarnik,M., Backlund,P. and
            Bonifacino,J.S.
  TITLE     BORC, a multisubunit complex that regulates lysosome positioning
  JOURNAL   Dev Cell 33 (2), 176-188 (2015)
   PUBMED   25898167
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Schiefermeier,N., Scheffler,J.M., de Araujo,M.E., Stasyk,T.,
            Yordanov,T., Ebner,H.L., Offterdinger,M., Munck,S., Hess,M.W.,
            Wickstrom,S.A., Lange,A., Wunderlich,W., Fassler,R., Teis,D. and
            Huber,L.A.
  TITLE     The late endosomal p14-MP1 (LAMTOR2/3) complex regulates focal
            adhesion dynamics during cell migration
  JOURNAL   J Cell Biol 205 (4), 525-540 (2014)
   PUBMED   24841562
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Okai,T., Araki,Y., Tada,M., Tateno,T., Kontani,K. and Katada,T.
  TITLE     Novel small GTPase subfamily capable of associating with tubulin is
            required for chromosome segregation
  JOURNAL   J Cell Sci 117 (Pt 20), 4705-4715 (2004)
   PUBMED   15331635
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Secombe,J. and Parkhurst,S.M.
  TITLE     Drosophila Topors is a RING finger-containing protein that
            functions as a ubiquitin-protein isopeptide ligase for the hairy
            basic helix-loop-helix repressor protein
  JOURNAL   J Biol Chem 279 (17), 17126-17133 (2004)
   PUBMED   14871887
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081947.1.
            
            On May 27, 2005 this sequence version replaced XP_575632.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081947.1, FQ214780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q41"
     Protein         1..186
                     /product="ADP-ribosylation factor-like protein 8B"
                     /EC_number="3.6.5.2"
                     /note="ADP-ribosylation factor-like 8B; ADP-ribosylation
                     factor like GTPase 8B"
                     /calculated_mol_wt=21408
     Region          22..180
                     /region_name="Arl10_like"
                     /note="Arf-like 9 (Arl9) and 10 (Arl10) GTPases; cd04159"
                     /db_xref="CDD:206724"
     Site            27..34
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206724"
     Site            order(29..30,34,38,51..58,80,85)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206724"
     Site            order(30..35,130..131,133..134,163..165)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206724"
     Site            order(39..42,45..55)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206724"
     Site            order(52..56,61,71,75,81,83..85)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206724"
     Site            52
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206724"
     Site            order(53..60,70,81,84..85)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206724"
     Site            order(56..63,65..70)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206724"
     Site            71..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206724"
     Site            71..74
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206724"
     Site            130..133
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206724"
     Site            163..165
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206724"
     CDS             1..186
                     /gene="Arl8b"
                     /coded_by="NM_001024332.1:184..744"
                     /db_xref="GeneID:500282"
                     /db_xref="RGD:1562830"
ORIGIN      
        1 mlalisrlld wfrslfwkee meltlvglqy sgkttfvnvi asgqfsedmi ptvgfnmrkv
       61 tkgnvtikiw diggqprfrs mwerycrgvn aivymidaad rekieasrne lhnlldkpql
      121 qgipvlvlgn krdlpnalde kqliekmnls aiqdreiccy sisckekdni ditlqwliqh
      181 sksrrs
//
LOCUS       NP_445924                172 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 4 isoform 2, mitochondrial isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_445924
VERSION     NP_445924.1
DBSOURCE    REFSEQ: accession NM_053472.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Hao,Y.H., Zhang,J., Wang,H., Wang,H.Y., Dong,J., Xu,X.P., Yao,B.W.,
            Wang,L.F., Zhou,H.M., Zhao,L. and Peng,R.Y.
  TITLE     HIF-1alpha regulates COXIV subunits, a potential mechanism of
            self-protective response to microwave induced mitochondrial damages
            in neurons
  JOURNAL   Sci Rep 8 (1), 10403 (2018)
   PUBMED   29991768
  REMARK    GeneRIF: microwave induced mitochondrial ROS production activated
            HIF-1alpha and regulated COXIV-1 expression to restore mitochondria
            functions. Therefore, HIF-1alpha might be a potential target to
            impair microwave induced injuries.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Aras,S., Pak,O., Sommer,N., Finley,R. Jr., Huttemann,M.,
            Weissmann,N. and Grossman,L.I.
  TITLE     Oxygen-dependent expression of cytochrome c oxidase subunit 4-2
            gene expression is mediated by transcription factors RBPJ, CXXC5
            and CHCHD2
  JOURNAL   Nucleic Acids Res 41 (4), 2255-2266 (2013)
   PUBMED   23303788
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Acin-Perez,R., Gatti,D.L., Bai,Y. and Manfredi,G.
  TITLE     Protein phosphorylation and prevention of cytochrome oxidase
            inhibition by ATP: coupled mechanisms of energy metabolism
            regulation
  JOURNAL   Cell Metab 13 (6), 712-719 (2011)
   PUBMED   21641552
  REMARK    GeneRIF: mitochondrial energy metabolism regulation by
            phosphorylation of COXIV-1 is coupled with prevention of COX
            allosteric inhibition by ATP
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Singh,S., Misiak,M., Beyer,C. and Arnold,S.
  TITLE     Cytochrome c oxidase isoform IV-2 is involved in 3-nitropropionic
            acid-induced toxicity in striatal astrocytes
  JOURNAL   Glia 57 (14), 1480-1491 (2009)
   PUBMED   19306371
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Prior,L.J., Velkoska,E., Watts,R., Cameron-Smith,D. and Morris,M.J.
  TITLE     Undernutrition during suckling in rats elevates plasma adiponectin
            and its receptor in skeletal muscle regardless of diet composition:
            a protective effect?
  JOURNAL   Int J Obes (Lond) 32 (10), 1585-1594 (2008)
   PUBMED   18725894
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Lombard,D.B., Alt,F.W., Cheng,H.L., Bunkenborg,J., Streeper,R.S.,
            Mostoslavsky,R., Kim,J., Yancopoulos,G., Valenzuela,D., Murphy,A.,
            Yang,Y., Chen,Y., Hirschey,M.D., Bronson,R.T., Haigis,M.,
            Guarente,L.P., Farese,R.V. Jr., Weissman,S., Verdin,E. and
            Schwer,B.
  TITLE     Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine
            acetylation
  JOURNAL   Mol Cell Biol 27 (24), 8807-8814 (2007)
   PUBMED   17923681
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Putcha,G.V., Harris,C.A., Moulder,K.L., Easton,R.M., Thompson,C.B.
            and Johnson,E.M. Jr.
  TITLE     Intrinsic and extrinsic pathway signaling during neuronal
            apoptosis: lessons from the analysis of mutant mice
  JOURNAL   J Cell Biol 157 (3), 441-453 (2002)
   PUBMED   11980919
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Huttemann,M., Kadenbach,B. and Grossman,L.I.
  TITLE     Mammalian subunit IV isoforms of cytochrome c oxidase
  JOURNAL   Gene 267 (1), 111-123 (2001)
   PUBMED   11311561
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF255347.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF255347.1, FM069824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..172
                     /product="cytochrome c oxidase subunit 4 isoform 2,
                     mitochondrial isoform 2 precursor"
                     /EC_number="7.1.1.9"
                     /note="COX IV-2; cytochrome c oxidase, subunit 4b;
                     cytochrome c oxidase, subunit IVb; cytochrome c oxidase
                     subunit IV"
                     /calculated_mol_wt=18176
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y94.1)"
     transit_peptide 1..18
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q91Y94.1)"
                     /calculated_mol_wt=2012
     Region          41..165
                     /region_name="Cyt_c_Oxidase_IV"
                     /note="Cytochrome c oxidase subunit IV. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00922"
                     /db_xref="CDD:238462"
     Site            order(43,45,47..50,69,71,73,81,85..86,88..89,91..94,97)
                     /site_type="other"
                     /note="Subunit IV/Va interface [polypeptide binding]"
                     /db_xref="CDD:238462"
     Site            order(44..46,102,109,113,117,121,130,132,135..136)
                     /site_type="other"
                     /note="Subunit IV/I interface [polypeptide binding]"
                     /db_xref="CDD:238462"
     Site            order(45,147..148,151,155,157..159)
                     /site_type="other"
                     /note="Subunit IV/II interface [polypeptide binding]"
                     /db_xref="CDD:238462"
     Site            order(45,98,100,102..103)
                     /site_type="other"
                     /note="putative ATP/ADP binding site [chemical binding]"
                     /db_xref="CDD:238462"
     Site            102..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y94.1)"
     Site            order(104..105,111..112,114..116,118..119,136,139,
                     142..143,146,150,159,163)
                     /site_type="other"
                     /note="Subunit IV/VIIb interface [polypeptide binding]"
                     /db_xref="CDD:238462"
     Site            order(152,157)
                     /site_type="other"
                     /note="Subunit IV/VIc interface [polypeptide binding]"
                     /db_xref="CDD:238462"
     CDS             1..172
                     /gene="Cox4i2"
                     /gene_synonym="Cox4b; CoxIV-2"
                     /coded_by="NM_053472.1:23..541"
                     /db_xref="GeneID:84683"
                     /db_xref="RGD:69422"
ORIGIN      
        1 mfsratrslv mktgglrtqg thspgsaass sqrrmtpyvd cyaqrsypmp depyctelse
       61 eqralkekek gswaqlsqae kvalyrlqfh etfaemnhrs newktvmgcv fffigftalv
      121 iwwqrvyvfp kkvvtlteer kaqqlqrlld mksnpiqgls ahwdyekkew kk
//
LOCUS       NP_001020068             543 aa            linear   ROD 27-APR-2025
DEFINITION  EH domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001020068 XP_341795
VERSION     NP_001020068.1
DBSOURCE    REFSEQ: accession NM_001024897.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Yang,H.Q., Jana,K., Rindler,M.J. and Coetzee,W.A.
  TITLE     The trafficking protein, EHD2, positively regulates cardiac
            sarcolemmal KATP channel surface expression: role in
            cardioprotection
  JOURNAL   FASEB J 32 (3), 1613-1625 (2018)
   PUBMED   29133341
  REMARK    GeneRIF: EHD2 may be cardioprotective as a dominant-negative EHD2
            mutant sensitized cardiomyocytes to ischemic damage. Our findings
            highlight EHD2 as a potential pharmacologic target in the treatment
            of diseases with KATP channel trafficking defects
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Shah,C., Hegde,B.G., Moren,B., Behrmann,E., Mielke,T., Moenke,G.,
            Spahn,C.M.T., Lundmark,R., Daumke,O. and Langen,R.
  TITLE     Structural insights into membrane interaction and caveolar
            targeting of dynamin-like EHD2
  JOURNAL   Structure 22 (3), 409-420 (2014)
   PUBMED   24508342
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Ke,K., Rui,Y., Li,L., Zheng,H., Xu,W., Tan,X., Cao,J., Wu,X.,
            Cui,G. and Cao,M.
  TITLE     Upregulation of EHD2 after intracerebral hemorrhage in adult rats
  JOURNAL   J Mol Neurosci 54 (2), 171-180 (2014)
   PUBMED   24664435
  REMARK    GeneRIF: EHD2 expression was upregulated in the perihematomal
            caudate in adult rats after intracerebral hemorrhage.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Ludwig,A., Howard,G., Mendoza-Topaz,C., Deerinck,T., Mackey,M.,
            Sandin,S., Ellisman,M.H. and Nichols,B.J.
  TITLE     Molecular composition and ultrastructure of the caveolar coat
            complex
  JOURNAL   PLoS Biol 11 (8), e1001640 (2013)
   PUBMED   24013648
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Posey,A.D. Jr., Pytel,P., Gardikiotes,K., Demonbreun,A.R.,
            Rainey,M., George,M., Band,H. and McNally,E.M.
  TITLE     Endocytic recycling proteins EHD1 and EHD2 interact with
            fer-1-like-5 (Fer1L5) and mediate myoblast fusion
  JOURNAL   J Biol Chem 286 (9), 7379-7388 (2011)
   PUBMED   21177873
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Guilherme,A., Soriano,N.A., Furcinitti,P.S. and Czech,M.P.
  TITLE     Role of EHD1 and EHBP1 in perinuclear sorting and insulin-regulated
            GLUT4 recycling in 3T3-L1 adipocytes
  JOURNAL   J Biol Chem 279 (38), 40062-40075 (2004)
   PUBMED   15247266
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Park,S.Y., Ha,B.G., Choi,G.H., Ryu,J., Kim,B., Jung,C.Y. and Lee,W.
  TITLE     EHD2 interacts with the insulin-responsive glucose transporter
            (GLUT4) in rat adipocytes and may participate in insulin-induced
            GLUT4 recruitment
  JOURNAL   Biochemistry 43 (23), 7552-7562 (2004)
   PUBMED   15182197
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Guilherme,A., Soriano,N.A., Bose,S., Holik,J., Bose,A.,
            Pomerleau,D.P., Furcinitti,P., Leszyk,J., Corvera,S. and Czech,M.P.
  TITLE     EHD2 and the novel EH domain binding protein EHBP1 couple
            endocytosis to the actin cytoskeleton
  JOURNAL   J Biol Chem 279 (11), 10593-10605 (2004)
   PUBMED   14676205
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Suzuki,K., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L9
  JOURNAL   Gene 93 (2), 297-300 (1990)
   PUBMED   2227441
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097385.1.
            
            On Jun 17, 2005 this sequence version replaced XP_341795.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097385.1, SRR8487231.63233.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..543
                     /product="EH domain-containing protein 2"
                     /note="putative eps protein"
                     /calculated_mol_wt=61107
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          25..56
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BH64; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          60..300
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          65..72
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            65..72
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(70..73,153,220,222,256..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          91..92
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            98..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          153..156
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            153..156
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(155..156,183..184)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          219..222
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            219..222
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          243
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            256..258
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          288..394
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Region          320..340
                     /region_name="Mediates membrane-binding.
                     /evidence=ECO:0000250|UniProtKB:Q8BH64"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          443..536
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZN4; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZN4; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8H8.1)"
     Region          521..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8H8.1)"
     CDS             1..543
                     /gene="Ehd2"
                     /gene_synonym="MGEPS"
                     /coded_by="NM_001024897.1:84..1715"
                     /db_xref="GeneID:361512"
                     /db_xref="RGD:1560856"
ORIGIN      
        1 mfswlkkgga rgqrseairt vtsslkelyr tkllpleehy rfgsfhspal edadfdgkpm
       61 vlvagqystg ktsfiqylle qevpgsrvgp epttdcfvav mhgetegtvp gnalvvdpek
      121 pfrklnpfgn tflnrfmcaq lpnqvlesis iidtpgilsg akqrvsrgyd fpavlrwfae
      181 rvdliillfd ahkleisdef seaigalrgh edkirvvlnk admvetqqlm rvygalmwal
      241 gkvvgtpevl rvyigsfwsq pllvpdnrrl feleeqdlfr diqglprhaa lrklndlvkr
      301 arlvrvhayi isylkkemps vfgkenkkkq lifklpvifa kiqlehhisp gdfpdcqkmq
      361 ellmahdftk fhslkpklle aldemlthdi aklmpllrqe elesveagvq ggafegtrmg
      421 pfvergpdea iedgeegsed daewvvtkdk skydeifynl apadgklsgs kaktwmvgtk
      481 lpnsvlgriw klsdvdrdgm lddeefalas hlieaklegh glptnlprrl vppskrrqkg
      541 sae
//
LOCUS       NP_598292                723 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier organic anion transporter family member 4A1 [Rattus
            norvegicus].
ACCESSION   NP_598292
VERSION     NP_598292.2
DBSOURCE    REFSEQ: accession NM_133608.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Fujiwara,K., Adachi,H., Nishio,T., Unno,M., Tokui,T., Okabe,M.,
            Onogawa,T., Suzuki,T., Asano,N., Tanemoto,M., Seki,M., Shiiba,K.,
            Suzuki,M., Kondo,Y., Nunoki,K., Shimosegawa,T., Iinuma,K., Ito,S.,
            Matsuno,S. and Abe,T.
  TITLE     Identification of thyroid hormone transporters in humans: different
            molecules are involved in a tissue-specific manner
  JOURNAL   Endocrinology 142 (5), 2005-2012 (2001)
   PUBMED   11316767
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097285.1.
            
            On Jun 12, 2005 this sequence version replaced NP_598292.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097285.1, BC097286.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132307, SAMD00155322
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..723
                     /product="solute carrier organic anion transporter family
                     member 4A1"
                     /note="solute carrier family 21 member 12; organic
                     anion-transporting polypeptide E; sodium-independent
                     organic anion transporter E; solute carrier family 21
                     (organic anion transporter), member 12"
                     /calculated_mol_wt=77556
     Region          23..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BD0; propagated from
                     UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BD0; propagated from
                     UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BD0; propagated from
                     UniProtKB/Swiss-Prot (Q99N01.1)"
     Region          101..606
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            order(115..116,119..120,123,156,246..247,249..251,254,274,
                     277..278,281,394,397..398,401..403,406,435,439,479..480,
                     484,488,550,553..554,557..558,561)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     Site            143..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            170..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            228..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            313..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            381..402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            423..446
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            451..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            566
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            583..605
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            615..640
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Site            674..691
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     Region          700..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99N01.1)"
     CDS             1..723
                     /gene="Slco4a1"
                     /gene_synonym="OATP-E; Slc21a12"
                     /coded_by="NM_133608.2:167..2338"
                     /db_xref="GeneID:171144"
                     /db_xref="RGD:620228"
ORIGIN      
        1 mpqhamgdkh flslpkhlft stssttdsgc dtppssrasp aslrsahgal gsssqplfep
       61 qvekrssqaa revqylssgp qstlcgwqsf tpkclqvfnt pkgflfflca asflqgmtvn
      121 gfintvitsi errfdlhsyq sgliassydi aaclcltfvs yfggnghkpr wlgwgalvlg
      181 igslvfalph ftagryevei ddeglgtetg tcltnqsqve ckdrasglss yrlifmlgql
      241 lhgvgatply tlgvtylden vkssyspiyi aifytaailg paagyligga mlnvytevgq
      301 rtelttdspl wvgawwigfl gagiaaflia ipilgyprql pgsqryvvmr aaetqqlkdh
      361 srdnpafgkt vrdlplsvwi llrnptfill clagateatl iagmstfgpk ffeaqfslsa
      421 seaatlfgyl vvpaggggtl lggflvnkfk lrgsgiirfc lfctltslla ffvflmhcpn
      481 vhmagvttgy vgsllpkgql dlkaacnaly ccqprhyspl cgsdgtmyys pcyagcpega
      541 vtgpggqkvy rgcscileka ssgwgnatag kcastcqskp lllvlvfvvi iftflssipa
      601 ltatlrcvcd rqrsfalgiq wivvrtlgsi pgpiafgwvi dkacllwqdq cghqgscfvy
      661 kneamsryll iagltfkvlg flffvaayfl ykspsvssdg leaslpsqss asdspteqlq
      721 snv
//
LOCUS       NP_001020823             431 aa            linear   ROD 27-APR-2025
DEFINITION  tRNA (adenine(37)-N6)-methyltransferase [Rattus norvegicus].
ACCESSION   NP_001020823 XP_216401
VERSION     NP_001020823.1
DBSOURCE    REFSEQ: accession NM_001025652.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kimura,S., Miyauchi,K., Ikeuchi,Y., Thiaville,P.C.,
            Crecy-Lagard,Vd. and Suzuki,T.
  TITLE     Discovery of the beta-barrel-type RNA methyltransferase responsible
            for N6-methylation of N6-threonylcarbamoyladenosine in tRNAs
  JOURNAL   Nucleic Acids Res 42 (14), 9350-9365 (2014)
   PUBMED   25063302
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097981.1.
            
            On Jul 22, 2005 this sequence version replaced XP_216401.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132292
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..431
                     /product="tRNA (adenine(37)-N6)-methyltransferase"
                     /note="nef-associated protein 1; thioesterase NAP1"
                     /calculated_mol_wt=47464
     Site            order(32..33,73..75,77,84,88,112..117,121,123,125,
                     154..159)
                     /site_type="other"
                     /note="homodimer interaction site [polypeptide binding]"
                     /db_xref="CDD:187753"
     Region          45..164
                     /region_name="TrmO"
                     /note="tRNA-methyltransferase O; pfam01980"
                     /db_xref="CDD:460402"
     Site            order(87,89..90,117,125,127,146,151)
                     /site_type="active"
                     /note="cofactor binding site [active]"
                     /db_xref="CDD:187753"
     Region          167..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7E0.1)"
     Region          201..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7E0.1)"
     Region          325..393
                     /region_name="TrmO_C"
                     /note="TrmO C-terminal domain; pfam18389"
                     /db_xref="CDD:465738"
     CDS             1..431
                     /gene="Trmo"
                     /gene_synonym="Nap1; RGD1305420"
                     /coded_by="NM_001025652.1:58..1353"
                     /db_xref="GeneID:298072"
                     /db_xref="RGD:1305420"
ORIGIN      
        1 mrglekqgps ataapcgcaq paletgnllt epigylescf sakigtprqp sicsqsracl
       61 kirksifnnp ehslmgleqf shvwilfvfh knghlnykak vqpprlngak tgvfstrsph
      121 rpnaigltla klekveggav ylsgidmihg tpvldikpyi adydspqnle pqtkhhklra
      181 agpsdatans cdqqllsgce kaqpchstke kpkcrehrts densqkfrdt seiqhtlped
      241 reravdlale ssreetmdep edqlgpqelk sfleegtdrp rkvegalvlr gssaetrwda
      301 schartadrv pcsvvpswvk eapvatlqvr ftphaemdlr klssggasqt sfkyfhsaee
      361 akcaieamls adprsvyrrk lcedrlffft vdiahvtcwf gdgfaevlri klasepveva
      421 dpeeslvalg s
//
LOCUS       NP_001028887             675 aa            linear   ROD 27-APR-2025
DEFINITION  calpastatin isoform b [Rattus norvegicus].
ACCESSION   NP_001028887
VERSION     NP_001028887.1
DBSOURCE    REFSEQ: accession NM_001033715.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Gritsyna,Y.V., Salmov,N.N., Bobylev,A.G., Ulanova,A.D.,
            Kukushkin,N.I., Podlubnaya,Z.A. and Vikhlyantsev,I.M.
  TITLE     Increased Autolysis of mu-Calpain in Skeletal Muscles of Chronic
            Alcohol-Fed Rats
  JOURNAL   Alcohol Clin Exp Res 41 (10), 1686-1694 (2017)
   PUBMED   28800153
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Manfredi,L.H., Lustrino,D., Machado,J., Silveira,W.A., Zanon,N.M.,
            Navegantes,L.C. and Kettelhut,I.C.
  TITLE     Adrenodemedullation activates the Ca2+-dependent proteolysis in
            soleus muscles from rats exposed to cold
  JOURNAL   J Appl Physiol (1985) 122 (2), 317-326 (2017)
   PUBMED   27765842
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Mochida,S., Hida,Y., Tanifuji,S., Hagiwara,A., Hamada,S., Abe,M.,
            Ma,H., Yasumura,M., Kitajima,I., Sakimura,K. and Ohtsuka,T.
  TITLE     SAD-B Phosphorylation of CAST Controls Active Zone Vesicle
            Recycling for Synaptic Depression
  JOURNAL   Cell Rep 16 (11), 2901-2913 (2016)
   PUBMED   27626661
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Yasuoka,H., Sugano,Y., Oka,T., Watanabe,C., Kaneko,Y., Nojima,T.,
            Matsumura,M., Fujii,T. and Mimori,T.
  TITLE     [Antigenic epitopes recognized by autoantibodies to calpastatin in
            patients with rheumatoid arthritis and their clinical significance]
  JOURNAL   Ryumachi 37 (3), 458-466 (1997)
   PUBMED   9256029
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Despres,N., Talbot,G., Plouffe,B., Boire,G. and Menard,H.A.
  TITLE     Detection and expression of a cDNA clone that encodes a polypeptide
            containing two inhibitory domains of human calpastatin and its
            recognition by rheumatoid arthritis sera
  JOURNAL   J Clin Invest 95 (4), 1891-1896 (1995)
   PUBMED   7706496
REFERENCE   8  (residues 1 to 675)
  AUTHORS   Lee,W.J., Hatanaka,M. and Maki,M.
  TITLE     Multiple forms of rat calpastatin cDNA in the coding region of
            functionally unknown amino-terminal domain
  JOURNAL   Biochim Biophys Acta 1129 (2), 251-253 (1992)
   PUBMED   1730065
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Ishida,S., Emori,Y. and Suzuki,K.
  TITLE     Rat calpastatin has diverged primary sequence from other mammalian
            calpastatins but retains functionally important sequences
  JOURNAL   Biochim Biophys Acta 1088 (3), 436-438 (1991)
   PUBMED   2015306
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Uemori,T., Shimojo,T., Asada,K., Asano,T., Kimizuka,F., Kato,I.,
            Maki,M., Hatanaka,M., Murachi,T., Hanzawa,H. et al.
  TITLE     Characterization of a functional domain of human calpastatin
  JOURNAL   Biochem Biophys Res Commun 166 (3), 1485-1493 (1990)
   PUBMED   2407243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091239.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon
            compared to variant 1. The resulting isoform (b) has the same N-
            and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091239.1, DQ186627.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q11"
     Protein         1..675
                     /product="calpastatin isoform b"
                     /note="calpain inhibitor"
                     /calculated_mol_wt=73025
     Region          <156..220
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          231..353
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          367..463
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Region          478..600
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     CDS             1..675
                     /gene="Cast"
                     /coded_by="NM_001033715.1:148..2175"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:25403"
                     /db_xref="RGD:2278"
ORIGIN      
        1 msrpgpkpaa ssrprrgaaa shtqehvnek nigssskpae kkgsdevtas saatgtsprm
       61 sttgakavki eseksqssep pvihekkpkg kpkegsetkf qdapsadges vaggvtvata
      121 sdkvvvkkke kksltptlpm estlnklsdk sgvnaalddl idtlgecedt nkddppytgp
      181 vvldpmdsty lealgikegt ippeyrklle kneaitgplp dspkpmgidh aidalssdft
      241 cssptgkqte kekstgessk aqsagvtrsa vppqekkrkv eeevmndqal qalsdslgtr
      301 qpdpqshlrq akqvkeakak eerqekcged edtvpaeyrl kpakdkdgkp llpepeetsk
      361 clseselige lsadfvqpty qekpsmpaak ikkgvvpdda vetlarslgt rkedpedeks
      421 lvdkvkekak eedheklgek eetippdyrl eivkdkdgkp llpkeaeeql pplsddflld
      481 alsqdfsspa nilslgfeda klsaavsetv sqvpapsnht aapppgterr dkelddalde
      541 lsdslgqrqp dpdenkpldd kvkekikaeh seklgerddt ippeyrhlld ndgkdkpekp
      601 ltkntekpgq dqdpidalse dldscpptte tsqnttkekg kktssskask neektkdssk
      661 kteevpkpkv dedat
//
LOCUS       NP_640347                450 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin beta-3 chain [Rattus norvegicus].
ACCESSION   NP_640347 XP_346523
VERSION     NP_640347.2
DBSOURCE    REFSEQ: accession NM_139254.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Shao,Q., Yang,T., Huang,H., Alarmanazi,F. and Liu,G.
  TITLE     Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
            Netrin-1 Repulsion
  JOURNAL   J Neurosci 37 (23), 5620-5633 (2017)
   PUBMED   28483977
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Gumy,L.F., Katrukha,E.A., Grigoriev,I., Jaarsma,D., Kapitein,L.C.,
            Akhmanova,A. and Hoogenraad,C.C.
  TITLE     MAP2 Defines a Pre-axonal Filtering Zone to Regulate KIF1- versus
            KIF5-Dependent Cargo Transport in Sensory Neurons
  JOURNAL   Neuron 94 (2), 347-362 (2017)
   PUBMED   28426968
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Cao,S., Du,J., Lv,Y., Lin,H., Mao,Z., Xu,M., Liu,M. and Liu,Y.
  TITLE     PAX3 inhibits beta-Tubulin-III expression and neuronal
            differentiation of neural stem cell
  JOURNAL   Biochem Biophys Res Commun 485 (2), 307-311 (2017)
   PUBMED   28223217
  REMARK    GeneRIF: PAX3 could inhibit the neuronal differentiation of neural
            stem celland the expression of TUBB3.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Rodriguez-Jimenez,F.J., Alastrue-Agudo,A., Stojkovic,M., Erceg,S.
            and Moreno-Manzano,V.
  TITLE     Connexin 50 Expression in Ependymal Stem Progenitor Cells after
            Spinal Cord Injury Activation
  JOURNAL   Int J Mol Sci 16 (11), 26608-26618 (2015)
   PUBMED   26561800
  REMARK    GeneRIF: Upon ependymal stem cells differentiation, Cx50 expression
            favors glial cell fate, since higher expression levels, endogenous
            or by over-expression of Cx50, augmented the expression of the
            astrocyte marker GFAP and impaired the neuronal marker Tubb3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Serinagaoglu,Y., Pare,J., Giovannini,M. and Cao,X.
  TITLE     Nf2-Yap signaling controls the expansion of DRG progenitors and
            glia during DRG development
  JOURNAL   Dev Biol 398 (1), 97-109 (2015)
   PUBMED   25433207
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Farkas,R.H., Qian,J., Goldberg,J.L., Quigley,H.A. and Zack,D.J.
  TITLE     Gene expression profiling of purified rat retinal ganglion cells
  JOURNAL   Invest Ophthalmol Vis Sci 45 (8), 2503-2513 (2004)
   PUBMED   15277470
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Kuvbachieva,A., Bestel,A.M., Tissir,F., Maloum,I., Guimiot,F.,
            Ramoz,N., Bourgeois,F., Moalic,J.M., Goffinet,A.M. and Simonneau,M.
  TITLE     Identification of a novel brain-specific and Reelin-regulated gene
            that encodes a protein colocalized with synapsin
  JOURNAL   Eur J Neurosci 20 (3), 603-610 (2004)
   PUBMED   15255972
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Lawoko-Kerali,G., Rivolta,M.N., Lawlor,P., Cacciabue-Rivolta,D.I.,
            Langton-Hewer,C., van Doorninck,J.H. and Holley,M.C.
  TITLE     GATA3 and NeuroD distinguish auditory and vestibular neurons during
            development of the mammalian inner ear
  JOURNAL   Mech Dev 121 (3), 287-299 (2004)
   PUBMED   15003631
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Olave,I., Wang,W., Xue,Y., Kuo,A. and Crabtree,G.R.
  TITLE     Identification of a polymorphic, neuron-specific chromatin
            remodeling complex
  JOURNAL   Genes Dev 16 (19), 2509-2517 (2002)
   PUBMED   12368262
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Dennis,K., Uittenbogaard,M., Chiaramello,A. and Moody,S.A.
  TITLE     Cloning and characterization of the 5'-flanking region of the rat
            neuron-specific Class III beta-tubulin gene
  JOURNAL   Gene 294 (1-2), 269-277 (2002)
   PUBMED   12234689
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CF976541.1 and BC097281.1.
            
            On Apr 27, 2007 this sequence version replaced NP_640347.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097281.1, CV117201.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..450
                     /product="tubulin beta-3 chain"
                     /note="neuron-specific class III beta-tubulin"
                     /calculated_mol_wt=50288
     Region          1..447
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QRB4.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q13509; propagated from
                     UniProtKB/Swiss-Prot (Q4QRB4.1)"
     Region          422..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QRB4.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2T9S0; propagated from
                     UniProtKB/Swiss-Prot (Q4QRB4.1)"
     CDS             1..450
                     /gene="Tubb3"
                     /coded_by="NM_139254.2:50..1402"
                     /db_xref="GeneID:246118"
                     /db_xref="RGD:628595"
ORIGIN      
        1 mreivhiqag qcgnqigakf wevisdehgi dpsgnyvgds dlqlerisvy yneasshkyv
       61 prailvdlep gtmdsvrsga fghlfrpdnf ifgqsgagnn wakghytega elvdsvldvv
      121 rkecencdcl qgfqlthslg ggtgsgmgtl liskvreeyp drimntfsvv pspkvsdtvv
      181 epynatlsih qlventdety cidnealydi cfrtlklatp tygdlnhlvs atmsgvttsl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltargsqq yraltvpelt qqmfdaknmm
      301 aacdprhgry ltvatvfrgr msmkevdeqm laiqsknssy fvewipnnvk vavcdipprg
      361 lkmsstfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata eeegemyedd deeseaqgpk
//
LOCUS       NP_001032281             453 aa            linear   ROD 27-APR-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            A [Rattus norvegicus].
ACCESSION   NP_001032281 XP_341168
VERSION     NP_001032281.1
DBSOURCE    REFSEQ: accession NM_001037204.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     TFIIB-related factors in RNA polymerase I transcription
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 265-273 (2013)
   PUBMED   22960599
  REMARK    Review article
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Schneider,D.A.
  TITLE     RNA polymerase I activity is regulated at multiple steps in the
            transcription cycle: recent insights into factors that influence
            transcription elongation
  JOURNAL   Gene 493 (2), 176-184 (2012)
   PUBMED   21893173
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107466.1.
            
            On Nov 18, 2005 this sequence version replaced XP_341168.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..453
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit A"
                     /note="TBP-associated factor 1A; TATA box-binding
                     protein-associated factor 1A; transcription initiation
                     factor SL1/TIF-IB subunit A; TATA box binding protein
                     (Tbp)-associated factor, RNA polymerase I, A"
                     /calculated_mol_wt=52890
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U2.1)"
     Region          64..424
                     /region_name="TAF1_subA"
                     /note="TAF RNA Polymerase I subunit A; pfam14929"
                     /db_xref="CDD:434323"
     CDS             1..453
                     /gene="Taf1a"
                     /coded_by="NM_001037204.1:87..1448"
                     /db_xref="GeneID:360893"
                     /db_xref="RGD:1305698"
ORIGIN      
        1 mmsdfseelt klagaednpe tsefsktrmh fpwlqkhiea vvtggkkrkd faqttsacls
       61 flqeallkhq wcraaeymhs ylqtledsdt yrkqaapeii wklgseilfy hpksnvetfs
      121 sfadrmknig vlnylkislq halyllhhgm ledanrnlse aetwrygeks asqevliklv
      181 qaykgllqhy swskkkmels eldeddyayt aksrnmlsqs sktstnictl iktpgvwdpf
      241 vksyvemlef ygdqdgarel ltnyaydekf psnpnahvyl yeflkrekap raklisvlki
      301 lheivpshsl mlefhtllrk seteehrklg lavlfevldf sgctknitaw kylakylkqt
      361 lmeshrewve eewksrrnww pafhfsffwa ksdwkadael acekafvagi llgkgcryfr
      421 yilkqdhetl kkkikrmkks vkkytivnpg vht
//
LOCUS       NP_001103074             226 aa            linear   ROD 27-APR-2025
DEFINITION  lysoplasmalogenase TMEM86B [Rattus norvegicus].
ACCESSION   NP_001103074 XP_001064677 XP_001064738
VERSION     NP_001103074.1
DBSOURCE    REFSEQ: accession NM_001109604.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wu,L.C., Pfeiffer,D.R., Calhoon,E.A., Madiai,F., Marcucci,G.,
            Liu,S. and Jurkowitz,M.S.
  TITLE     Purification, identification, and cloning of lysoplasmalogenase,
            the enzyme that catalyzes hydrolysis of the vinyl ether bond of
            lysoplasmalogen
  JOURNAL   J Biol Chem 286 (28), 24916-24930 (2011)
   PUBMED   21515882
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474075.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064677.1, XP_001064738.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210876.1, FQ219460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..226
                     /product="lysoplasmalogenase TMEM86B"
                     /EC_number="3.3.2.2"
                     /note="lysoplasmalogenase"
                     /calculated_mol_wt=25026
     Region          48..217
                     /region_name="YhhN"
                     /note="YhhN family; pfam07947"
                     /db_xref="CDD:429751"
     CDS             1..226
                     /gene="Tmem86b"
                     /coded_by="NM_001109604.1:94..774"
                     /db_xref="GeneID:690610"
                     /db_xref="RGD:1593455"
ORIGIN      
        1 mdarkeglsl eilfsdqypq vrrwlapfiv acslyfllwi pedqpswvsa lvkcqpilcl
       61 vlflwavapg gsytwllqga ltcsavgdac liwpeaffyg mavfsvahll ylwafglspl
      121 qpglllcttl asltyysfll lhlepnmvlp vaayglilnt mlwrglvlgr sagwgavlfi
      181 fsdgvlawdt fvytlpfarl vtmstyyaaq llltlsalrs pglkth
//
LOCUS       NP_001020151             495 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 34A [Rattus norvegicus].
ACCESSION   NP_001020151
VERSION     NP_001020151.1
DBSOURCE    REFSEQ: accession NM_001024980.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091343.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091343.1, CO405513.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..495
                     /product="ankyrin repeat domain-containing protein 34A"
                     /note="ankyrin repeat domain 34"
                     /calculated_mol_wt=52325
     Region          4..33
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Region          <8..>133
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          8..35
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(10..11,14..16,18..19,23,26,35,37,39,43..44,47..49,
                     51..52,62,65,74,76,78,83..84,87..89,91..92,96,99,108)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Site            15
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000250|UniProtKB:Q69YU3; propagated from
                     UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Region          37..74
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          37..72
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Region          76..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          76..106
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Region          110..139
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Region          110..136
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          147..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJT1.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BJT1.1)"
     CDS             1..495
                     /gene="Ankrd34a"
                     /gene_synonym="Ankrd34; RGD1308412"
                     /coded_by="NM_001024980.1:165..1652"
                     /db_xref="GeneID:295283"
                     /db_xref="RGD:1308412"
ORIGIN      
        1 mlhteghall ravgqgklrl arllleggay vnegdaqget almaacrary ddpqnkarmv
       61 rylleqgadp niadrlgrta lmhacagggg aavaslllah gadpsvrdha gasalvhald
      121 rgdretlatl ldackakgte viiittdtsp sgtkktrqyl nsppspgved papappspgv
      181 ctspsevqlq tagggrglls praqeeeekr dvfefplpks pddpspsepl pkpprhppkp
      241 lkrlnsepwg lvappqpvpp aegrpglerl aaefngltlt grprlsrrhs tegpedpppw
      301 aekvtgggpl srrntapeaq esglpsglrq klsrmesvel dtpghfcpds pessrlsler
      361 rrysaspltl ppagsvsspr qsqeslpgav splsgrrrsp gllerrgsgt llldhisqtr
      421 pgflpplnvs phppipdirp qpggrapslp apphsgapgs prtkrklvrr hsmqteqirl
      481 lggfqslggp gepgr
//
LOCUS       NP_001013077             221 aa            linear   ROD 27-APR-2025
DEFINITION  NEDD4 family-interacting protein 1 [Rattus norvegicus].
ACCESSION   NP_001013077 XP_214564
VERSION     NP_001013077.1
DBSOURCE    REFSEQ: accession NM_001013059.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Low,L.H., Chow,Y.L., Li,Y., Goh,C.P., Putz,U., Silke,J., Ouchi,T.,
            Howitt,J. and Tan,S.S.
  TITLE     Nedd4 family interacting protein 1 (Ndfip1) is required for
            ubiquitination and nuclear trafficking of BRCA1-associated ATM
            activator 1 (BRAT1) during the DNA damage response
  JOURNAL   J Biol Chem 290 (11), 7141-7150 (2015)
   PUBMED   25631046
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Lackovic,J., Howitt,J., Callaway,J.K., Silke,J., Bartlett,P. and
            Tan,S.S.
  TITLE     Differential regulation of Nedd4 ubiquitin ligases and their
            adaptor protein Ndfip1 in a rat model of ischemic stroke
  JOURNAL   Exp Neurol 235 (1), 326-335 (2012)
   PUBMED   22417925
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Oliver,P.M., Cao,X., Worthen,G.S., Shi,P., Briones,N., MacLeod,M.,
            White,J., Kirby,P., Kappler,J., Marrack,P. and Yang,B.
  TITLE     Ndfip1 protein promotes the function of itch ubiquitin ligase to
            prevent T cell activation and T helper 2 cell-mediated inflammation
  JOURNAL   Immunity 25 (6), 929-940 (2006)
   PUBMED   17137798
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Harvey,K.F., Shearwin-Whyatt,L.M., Fotia,A., Parton,R.G. and
            Kumar,S.
  TITLE     N4WBP5, a potential target for ubiquitination by the Nedd4 family
            of proteins, is a novel Golgi-associated protein
  JOURNAL   J Biol Chem 277 (11), 9307-9317 (2002)
   PUBMED   11748237
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085887.1.
            
            On Apr 20, 2005 this sequence version replaced XP_214564.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085887.1, FQ229568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..221
                     /product="NEDD4 family-interacting protein 1"
                     /calculated_mol_wt=24782
     Region          2..41
                     /region_name="Interaction with UBE2L3.
                     /evidence=ECO:0000250|UniProtKB:Q8R0W6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BT67; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Region          15..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Region          16..221
                     /region_name="NDFIP1"
                     /note="NEDD4 family-interacting protein 1; cd22305"
                     /db_xref="CDD:412069"
     Region          39..42
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Region          42..76
                     /region_name="Interaction with ITCH.
                     /evidence=ECO:0000250|UniProtKB:Q8R0W6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Region          64..67
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Region          74..76
                     /region_name="PPxY motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S1.1)"
     CDS             1..221
                     /gene="Ndfip1"
                     /coded_by="NM_001013059.1:135..800"
                     /db_xref="GeneID:291609"
                     /db_xref="RGD:1310053"
ORIGIN      
        1 malalaalaa vepacgtgyq qlqneeepge reqtagdapp pyssisaesa ayfdykdesg
       61 fpkppsynva ttlpsydeae rtkaeatipl vpgrdedfvg rddfddadql rigndgifml
      121 tffmaflfnw igfflsfclt tsaagrygai sgfglslikw ilivrfstyf pgyfdgqywl
      181 wwvflvlgfl lflrgfinya kvrkmpetfs nlprtrvlfi y
//
LOCUS       NP_001014181             478 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 42 [Rattus norvegicus].
ACCESSION   NP_001014181 XP_341832
VERSION     NP_001014181.2
DBSOURCE    REFSEQ: accession NM_001014159.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Zheng,S., Damoiseaux,R., Chen,L. and Black,D.L.
  TITLE     A broadly applicable high-throughput screening strategy identifies
            new regulators of Dlg4 (Psd-95) alternative splicing
  JOURNAL   Genome Res 23 (6), 998-1007 (2013)
   PUBMED   23636947
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP504208.1, BC079321.1 and BI273871.1.
            
            On Mar 12, 2009 this sequence version replaced NP_001014181.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079321.1, SRR8487227.155205.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..478
                     /product="RNA-binding protein 42"
                     /calculated_mol_wt=50135
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTD8; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            151
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTD8; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            156
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTD8; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            166
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTD8; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Region          171..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Site            179
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTD8; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Region          234..478
                     /region_name="Necessary for interaction with HNRNPK.
                     /evidence=ECO:0000269|PubMed:19170760"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Region          317..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT7.2)"
     Region          373..455
                     /region_name="RRM_RBM42"
                     /note="RNA recognition motif (RRM) found in RNA-binding
                     protein 42 (RBM42) and similar proteins; cd12383"
                     /db_xref="CDD:409817"
     CDS             1..478
                     /gene="Rbm42"
                     /gene_synonym="RGD1306184"
                     /coded_by="NM_001014159.2:96..1532"
                     /db_xref="GeneID:361545"
                     /db_xref="RGD:1306184"
ORIGIN      
        1 masamagagp apglpvaggp vvpgpgvgip gksgeerlke meaemalfeq evlgapvtgi
       61 ptavpavptv eamqvppapv irpiiatnty qqvqqtlear aaaaatvvpp mvggppfvgp
      121 vgfgpadrsh ldspeaream flrraavapq rapilrpafv phvlqradsa lssaaggprp
      181 malrpphqal vgpplpgppg ppmmlppmar apgpplgsma alrppleepa aprdlglglg
      241 lglkekeeav vaaaagleea saavavgagg apagpavigp slplalampl pepeplplpl
      301 evvrgllppl ripellslrp rprpprpepp pglmalevpe plgedkkkgk peklkrcirt
      361 aagsswedps llewdaddfr ifcgdlgnev nddilarafs rfpsflkakv irdkrtgktk
      421 gygfvsfkdp sdyvramrem ngkyvgsrpi klrksmwkdr nldvvrkkqk ekkklglr
//
LOCUS       NP_446142                703 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 14 [Rattus norvegicus].
ACCESSION   NP_446142
VERSION     NP_446142.2
DBSOURCE    REFSEQ: accession NM_053690.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Bermak,J.C., Li,M., Bullock,C. and Zhou,Q.Y.
  TITLE     Regulation of transport of the dopamine D1 receptor by a new
            membrane-associated ER protein
  JOURNAL   Nat Cell Biol 3 (5), 492-498 (2001)
   PUBMED   11331877
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083549.1, BP502976.1 and AA957791.1.
            
            On Dec 5, 2007 this sequence version replaced NP_446142.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083549.1, AF351783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..703
                     /product="dnaJ homolog subfamily C member 14"
                     /note="dopamine receptor-interacting protein of 78 kDa;
                     dopamine receptor interacting protein; DnaJ (Hsp40)
                     homolog, subfamily C, member 14; dnaJ homolog subfamily C
                     member 14-like"
                     /calculated_mol_wt=78887
     Region          1..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Region          164..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Region          444..505
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(472..474,482,485..486,489..490)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          533..621
                     /region_name="Jiv90"
                     /note="Cleavage inducing molecular chaperone; pfam14901"
                     /db_xref="CDD:464360"
     Region          622..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     Region          659..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX0.1)"
     CDS             1..703
                     /gene="Dnajc14"
                     /gene_synonym="Drip78"
                     /coded_by="NM_053690.2:107..2218"
                     /db_xref="GeneID:114481"
                     /db_xref="RGD:620489"
ORIGIN      
        1 maqkhpgerg lcgvhhsggs slitsgssvd peilsfsglr dsketapngt rclkehsdpk
       61 ctqppnpahw sdpshgpprg pgppreggyp desetcsees gvdqelsren etgyqedgsp
      121 sflpipsacn cqgspgvpeg tcseegdgss ssfchhctsp algedeelee eyddeeplkf
      181 psdfsrvssg kkppsrrqrh rfltkedvrd sgrrdpkapg rhrlarkrsq tdkrrglglw
      241 gveelcqlgq agfwwliell vlvgeyvetc gyliyacrkl kgsdldlfri wvgvwarrlg
      301 gwarvmfqfl sqsffsvagl firllrvvga flllalalfl gclqlgwrfl vglgdrlgwr
      361 gkaawlfswl dspalhhflt llkdsrpwqq lvrviqwgwl elpwvkqrtq rqgtahvasg
      421 rycqpeeeva rlltmagvpe delnpfhvlg veatasdiel kkayrqlavm vhpdknhhpr
      481 aeeafkvlra awdivsnper rkeyemkrma enelsrsvne flsklqddlk eamntmmcsr
      541 cqgkhrrfem drepksaryc aecnrlhpae egdfwaessm lglkityfal mdgkvydite
      601 wagcqrvgis pdthrvpyhi sfgsrvpgts grqratpesp padlqdflsr ifqvppgpms
      661 ngnffaaphp gpgttstsrp nssvpkgeak pkrrkkvrrp fqr
//
LOCUS       NP_058937                920 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_058937
VERSION     NP_058937.1
DBSOURCE    REFSEQ: accession NM_017241.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Jack,A., Hamad,M.I.K., Gonda,S., Gralla,S., Pahl,S., Hollmann,M.
            and Wahle,P.
  TITLE     Development of Cortical Pyramidal Cell and Interneuronal Dendrites:
            a Role for Kainate Receptor Subunits and NETO1
  JOURNAL   Mol Neurobiol 56 (7), 4960-4979 (2019)
   PUBMED   30421168
  REMARK    GeneRIF: Gluk1 and NETO1 specifically promote dendrite growth of
            interneurons in the visual cortex.
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Duan,G.F., Ye,Y., Xu,S., Tao,W., Zhao,S., Jin,T., Nicoll,R.A.,
            Shi,Y.S. and Sheng,N.
  TITLE     Signal peptide represses GluK1 surface and synaptic trafficking
            through binding to amino-terminal domain
  JOURNAL   Nat Commun 9 (1), 4879 (2018)
   PUBMED   30451858
  REMARK    GeneRIF: Signal peptide represses GluK1 surface and synaptic
            trafficking through binding to amino-terminal domain.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Sheng,N., Shi,Y.S. and Nicoll,R.A.
  TITLE     Amino-terminal domains of kainate receptors determine the
            differential dependence on Neto auxiliary subunits for trafficking
  JOURNAL   Proc Natl Acad Sci U S A 114 (5), 1159-1164 (2017)
   PUBMED   28100490
  REMARK    GeneRIF: In the CA1 hippocampal pyramidal cell, GluK1 had no effect
            on synaptic transmission. GluK1 which requires the auxiliary
            subunits Neto1 and Neto2 for surface and synaptic trafficking. It
            is the amino-terminal domains of GluK1 and GluK2 that control their
            strikingly different trafficking properties.
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Fisher,M.T. and Fisher,J.L.
  TITLE     Contributions of different kainate receptor subunits to the
            properties of recombinant homomeric and heteromeric receptors
  JOURNAL   Neuroscience 278, 70-80 (2014)
   PUBMED   25139762
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Sailer,A., Swanson,G.T., Perez-Otano,I., O'Leary,L., Malkmus,S.A.,
            Dyck,R.H., Dickinson-Anson,H., Schiffer,H.H., Maron,C., Yaksh,T.L.,
            Gage,F.H., O'Gorman,S. and Heinemann,S.F.
  TITLE     Generation and analysis of GluR5(Q636R) kainate receptor mutant
            mice
  JOURNAL   J Neurosci 19 (20), 8757-8764 (1999)
   PUBMED   10516295
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Brakeman,P.R., Lanahan,A.A., O'Brien,R., Roche,K., Barnes,C.A.,
            Huganir,R.L. and Worley,P.F.
  TITLE     Homer: a protein that selectively binds metabotropic glutamate
            receptors
  JOURNAL   Nature 386 (6622), 284-288 (1997)
   PUBMED   9069287
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Lomeli,H., Wisden,W., Kohler,M., Keinanen,K., Sommer,B. and
            Seeburg,P.H.
  TITLE     High-affinity kainate and domoate receptors in rat brain
  JOURNAL   FEBS Lett 307 (2), 139-143 (1992)
   PUBMED   1322826
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Sommer,B., Burnashev,N., Verdoorn,T.A., Keinanen,K., Sakmann,B. and
            Seeburg,P.H.
  TITLE     A glutamate receptor channel with high affinity for domoate and
            kainate
  JOURNAL   EMBO J 11 (4), 1651-1656 (1992)
   PUBMED   1373382
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Bettler,B., Boulter,J., Hermans-Borgmeyer,I., O'Shea-Greenfield,A.,
            Deneris,E.S., Moll,C., Borgmeyer,U., Hollmann,M. and Heinemann,S.
  TITLE     Cloning of a novel glutamate receptor subunit, GluR5: expression in
            the nervous system during development
  JOURNAL   Neuron 5 (5), 583-595 (1990)
   PUBMED   1977421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M83560.1, JAXUCZ010000011.1 and
            AI145540.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) is missing an in-frame coding
            exon at the 3' end compared to transcript variant 1, resulting in a
            shorter isoform (2) lacking a 29 aa segment, compared to isoform 1.
            RNA editing (CAG->CGG) changes Gln636Arg.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M83560.1, Z11713.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 10516295
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..920
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     2"
                     /note="glutamate receptor 5; glutamate receptor
                     ionotropic, kainate 1"
                     /calculated_mol_wt=104397
     Region          38..431
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Region          446..815
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..920
                     /gene="Grik1"
                     /gene_synonym="GluK1; GluR5"
                     /coded_by="NM_017241.2:186..2948"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29559"
                     /db_xref="RGD:2732"
ORIGIN      
        1 merstvliqp glwtrdtswt llyflcyilp qtspqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dsrdlfyinl ypdyaaisra vldlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlppank dakpllkemk kskefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltgritfnk tdglrkdfdl diislkeegt ekasgevskh lykvwkkigi
      421 wnsnsglnmt dgnrdrsnni tdslanrtli vttileepyv myrksdkply gndrfegycl
      481 dllkelsnil gflydvklvp dgkygaqndk gewngmvkel idhradlava pltityvrek
      541 vidfskpfmt lgisilyrkp ngtnpgvfsf lnplspdiwm yvllaclgvs cvlfviarft
      601 pyewynphpc npdsdvvenn ftllnsfwfg vgalmqqgse lmpkalstri vggiwwfftl
      661 iiissytanl aafltverme spidsaddla kqtkieygav rdgstmtffk kskistyekm
      721 wafmssrqqs alvknsdegi qrvlttdyal lmestsieyv tqrncnltqi gglidskgyg
      781 vgtpigspyr dkitiailql qeegklhmmk ekwwrgngcp eedskeasal gveniggifi
      841 vlaaglvlsv fvaigeflyk srknndveqc lsfnaimeel gislknqkkl kkksrtkgks
      901 sftsiltchq rrtqrketva
//
LOCUS       NP_110468                494 aa            linear   ROD 27-APR-2025
DEFINITION  neuronal pentraxin receptor precursor [Rattus norvegicus].
ACCESSION   NP_110468
VERSION     NP_110468.2
DBSOURCE    REFSEQ: accession NM_030841.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Lee,S.J., Wei,M., Zhang,C., Maxeiner,S., Pak,C., Calado Botelho,S.,
            Trotter,J., Sterky,F.H. and Sudhof,T.C.
  TITLE     Presynaptic Neuronal Pentraxin Receptor Organizes Excitatory and
            Inhibitory Synapses
  JOURNAL   J Neurosci 37 (5), 1062-1080 (2017)
   PUBMED   27986928
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Bilousova,T., Taylor,K., Emirzian,A., Gylys,R., Frautschy,S.A.,
            Cole,G.M. and Teng,E.
  TITLE     Parallel age-associated changes in brain and plasma neuronal
            pentraxin receptor levels in a transgenic APP/PS1 rat model of
            Alzheimer's disease
  JOURNAL   Neurobiol Dis 74, 32-40 (2015)
   PUBMED   25449907
  REMARK    GeneRIF: Results indicate that cerebral accumulation of NPR and
            Abeta occurs with similar temporal and regional patterns in the
            APP/PS1 model, and suggest that a 26 kDa plasma NPR fragment may
            represent a peripheral biomarker of this process
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Anantharam,V., Lehrmann,E., Kanthasamy,A., Yang,Y., Banerjee,P.,
            Becker,K.G., Freed,W.J. and Kanthasamy,A.G.
  TITLE     Microarray analysis of oxidative stress regulated genes in
            mesencephalic dopaminergic neuronal cells: relevance to oxidative
            damage in Parkinson's disease
  JOURNAL   Neurochem Int 50 (6), 834-847 (2007)
   PUBMED   17397968
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Andersson,K.B., Florholmen,G., Winer,L.H., Tonnessen,T. and
            Christensen,G.
  TITLE     Regulation of neuronal type genes in congestive heart failure rats
  JOURNAL   Acta Physiol (Oxf) 186 (1), 17-27 (2006)
   PUBMED   16497176
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Chen,B. and Bixby,J.L.
  TITLE     A novel substrate of receptor tyrosine phosphatase PTPRO is
            required for nerve growth factor-induced process outgrowth
  JOURNAL   J Neurosci 25 (4), 880-888 (2005)
   PUBMED   15673668
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Kim,Y.D., Sohn,N.W., Kang,C. and Soh,Y.
  TITLE     DNA array reveals altered gene expression in response to focal
            cerebral ischemia
  JOURNAL   Brain Res Bull 58 (5), 491-498 (2002)
   PUBMED   12242102
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Kirkpatrick,L.L., Matzuk,M.M., Dodds,D.C. and Perin,M.S.
  TITLE     Biochemical interactions of the neuronal pentraxins. Neuronal
            pentraxin (NP) receptor binds to taipoxin and taipoxin-associated
            calcium-binding protein 49 via NP1 and NP2
  JOURNAL   J Biol Chem 275 (23), 17786-17792 (2000)
   PUBMED   10748068
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Dodds,D.C., Omeis,I.A., Cushman,S.J., Helms,J.A. and Perin,M.S.
  TITLE     Neuronal pentraxin receptor, a novel putative integral membrane
            pentraxin that interacts with neuronal pentraxin 1 and 2 and
            taipoxin-associated calcium-binding protein 49
  JOURNAL   J Biol Chem 272 (34), 21488-21494 (1997)
   PUBMED   9261167
  REMARK    GeneRIF: non-AUG translation initiation site. Comparison of rat
            determined N-terminal amino acid sequence with cDNA sequence
            indicates that a CUG codon is used as an initiator codon and codes
            for a methionine. The CTG is present in cDNAs of mouse, rat, and
            human.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1 and
            BG380575.1.
            
            On Sep 26, 2003 this sequence version replaced NP_110468.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein, and functions as a neuronal receptor. It is thought to
            mediate neuronal uptake of the snake venom toxin, taipoxin, and its
            transport into the synapses. Studies in rat indicate that
            translation of this mRNA initiates at a non-AUG (CUG) codon. This
            site is also conserved in human and mouse. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no quality transcript was available
            for the full length of the gene. The extent of this transcript and
            the encoded protein are supported by transcript alignment and
            orthologous mouse data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.40939.1,
                                           SRR21887623.650003.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 9261167
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..494
                     /product="neuronal pentraxin receptor precursor"
                     /calculated_mol_wt=48804
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3471
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35764.1)"
     Region          37..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35764.1)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35764.1)"
     Region          <106..>277
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (O35764.1)"
     Region          282..488
                     /region_name="PTX"
                     /note="Pentraxin / C-reactive protein / pentaxin family;
                     smart00159"
                     /db_xref="CDD:128463"
     Site            order(341,419,421,428,431)
                     /site_type="active"
                     /note="calcium mediated ligand binding site [active]"
                     /db_xref="CDD:238086"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35764.1)"
     CDS             1..494
                     /gene="Nptxr"
                     /gene_synonym="Npr"
                     /coded_by="NM_030841.3:115..1599"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:81005"
                     /db_xref="RGD:628898"
ORIGIN      
        1 mkflavllaa gmlaflgavi ciiasvplaa sparalpggt dnasaasaag apgpqrslsa
       61 lqgaggsagp svlpgepaas vfppppgpll srflctplaa acpsgaeqgd aageraelll
      121 lqstaeqlrq talqqearir adrdtirelt gklgrcesgl prglqdagpr rdtmadgawd
      181 spallvelen avralrdrie rieqelparg nlsssapapa vptalhskmd elegqllakv
      241 lalekeraal shgshqqrqe vekeldalqg rvaelehgss aysppdafkv sipirnnymy
      301 arvrkavpel yaftacmwlr srsggsgqgt pfsysvpgqa neivlleagl epmellindk
      361 vaqlplslkd snwhhiciaw ttrdglwsay qdgelrgsgd nlaawhpikp hgililgqeq
      421 dtlggrfdat qafvgdiaqf nlwdhaltpa qvlgianctg plmgnvlpwe dklveafgga
      481 kkaafdvckg raka
//
LOCUS       NP_997684                610 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import receptor subunit TOM70 [Rattus norvegicus].
ACCESSION   NP_997684 XP_221530
VERSION     NP_997684.1
DBSOURCE    REFSEQ: accession NM_212519.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Kang,C., Qin,J., Osei,W. and Hu,K.
  TITLE     Regulation of protein kinase C-epsilon and its age-dependence
  JOURNAL   Biochem Biophys Res Commun 482 (4), 1201-1206 (2017)
   PUBMED   27919679
  REMARK    GeneRIF: adenosine-induced translocation of PKCepsilon to
            mitochondria is mediated by a caveolin-3-dependent mechanism and
            this process is age-related, possibly in part, through regulation
            of HSP90 and TOM70 expression
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Ellenrieder,L., Martensson,C.U. and Becker,T.
  TITLE     Biogenesis of mitochondrial outer membrane proteins, problems and
            diseases
  JOURNAL   Biol Chem 396 (11), 1199-1213 (2015)
   PUBMED   25980382
  REMARK    Review article
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Wenz,L.S., Opalinski,L., Wiedemann,N. and Becker,T.
  TITLE     Cooperation of protein machineries in mitochondrial protein sorting
  JOURNAL   Biochim Biophys Acta 1853 (5), 1119-1129 (2015)
   PUBMED   25633533
  REMARK    Review article
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Schulz,C., Schendzielorz,A. and Rehling,P.
  TITLE     Unlocking the presequence import pathway
  JOURNAL   Trends Cell Biol 25 (5), 265-275 (2015)
   PUBMED   25542066
  REMARK    Review article
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Anandatheerthavarada,H.K., Sepuri,N.B.V. and Avadhani,N.G.
  TITLE     Mitochondrial targeting of cytochrome P450 proteins containing
            NH2-terminal chimeric signals involves an unusual TOM20/TOM22
            bypass mechanism
  JOURNAL   J Biol Chem 284 (25), 17352-17363 (2009)
   PUBMED   19401463
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Suzuki,H., Maeda,M. and Mihara,K.
  TITLE     Characterization of rat TOM70 as a receptor of the preprotein
            translocase of the mitochondrial outer membrane
  JOURNAL   J Cell Sci 115 (Pt 9), 1895-1905 (2002)
   PUBMED   11956321
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Alvarez-Dolado,M., Gonzalez-Moreno,M., Valencia,A., Zenke,M.,
            Bernal,J. and Munoz,A.
  TITLE     Identification of a mammalian homologue of the fungal Tom70
            mitochondrial precursor protein import receptor as a thyroid
            hormone-regulated gene in specific brain regions
  JOURNAL   J Neurochem 73 (6), 2240-2249 (1999)
   PUBMED   10582581
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098640.1.
            
            On Aug 30, 2004 this sequence version replaced XP_221530.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098640.1, FQ228582.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q12"
     Protein         1..610
                     /product="mitochondrial import receptor subunit TOM70"
                     /note="translocase of outer membrane 70 kDa subunit;
                     mitochondrial precursor proteins import receptor;
                     translocase of outer mitochondrial membrane protein 70"
                     /calculated_mol_wt=67314
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O94826; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          69..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            74
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O94826; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94826; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZW5; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94826; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          <116..603
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          116..149
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          116..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(117,120..121,124..125,127,151,159..160,163..164,
                     166..167,190,193..194,197..198,201)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          149..184
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..188
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Site            187
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O94826; propagated from
                     UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          296..329
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          331..364
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          331..359
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(332,335..336,339..340,342,370,373..374,377..378,
                     380..381,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          364..398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          369..402
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          403..436
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          403..431
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          444..477
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          446..472
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          478..511
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          478..506
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(479,482..483,486..487,489,513,516..517,520..521,
                     523..524,548,551..552,555..556,559)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          511..542
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          513..546
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          547..580
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75Q39.1)"
     Region          547..574
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..610
                     /gene="Tomm70"
                     /gene_synonym="TOM70; Tomm70a"
                     /coded_by="NM_212519.2:138..1970"
                     /db_xref="GeneID:304017"
                     /db_xref="RGD:1303049"
ORIGIN      
        1 maaskpveaa maaaaapasg ngvgssggta apgsgagtlp rwhvalaiga plllgagamy
       61 lwsrrrrrre aggrgdasgl krnserktpe graspalgsg pdgsgdslem ssldraqaak
      121 nkgnkyfkag kyeqaiqcyt eaislcptek nadlstfyqn raaafeqlqk wkevaqdctk
      181 avelnpkyvk alfrrakahe kldnkkecle dvtavcileg fqneqsmlla dkvlkllgke
      241 nakekyknre plmpspqfik syfssftddi isqpmlkgek sdedkdkege alevkensgy
      301 lkakqymeee nydkiisecs keidaqgkym aealllratf ylligsanaa kpdldkvisl
      361 keanvklran alikrgtmcm qqqqpmlstq dfnmaaeidp mnsdvyhhrg qlkilldlve
      421 eavadfdaci rlrpkfalaq aqkcfalyrq aytannssqv qaamkgfeev ikkfprcaeg
      481 yalyaqaltd qqqfgkadem ydkcidlepd nattyvhkgl lqlqwkqdld kgleliskai
      541 eidnkcdfay etmgtievqr gnmekaidmf nkainlakse memahlyslc daahaqteva
      601 kkyglkpptl
//
LOCUS       NP_001004207             369 aa            linear   ROD 27-APR-2025
DEFINITION  deoxyhypusine synthase [Rattus norvegicus].
ACCESSION   NP_001004207 XP_213837
VERSION     NP_001004207.1
DBSOURCE    REFSEQ: accession NM_001004207.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Lemay,S.E., Grobs,Y., Romanet,C., Martineau,S., Salem,M.,
            Shimauchi,T., Breuils-Bonnet,S., Bourgeois,A., Theberge,C.,
            Pelletier,A., Potus,F., Provencher,S., Bonnet,S. and Boucherat,O.
  TITLE     Hypusine Signaling Promotes Pulmonary Vascular Remodeling in
            Pulmonary Arterial Hypertension
  JOURNAL   Am J Respir Crit Care Med 209 (11), 1376-1391 (2024)
   PUBMED   38261723
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Ganapathi,M., Padgett,L.R., Yamada,K., Devinsky,O., Willaert,R.,
            Person,R., Au,P.B., Tagoe,J., McDonald,M., Karlowicz,D., Wolf,B.,
            Lee,J., Shen,Y., Okur,V., Deng,L., LeDuc,C.A., Wang,J., Hanner,A.,
            Mirmira,R.G., Park,M.H., Mastracci,T.L. and Chung,W.K.
  TITLE     Recessive Rare Variants in Deoxyhypusine Synthase, an Enzyme
            Involved in the Synthesis of Hypusine, Are Associated with a
            Neurodevelopmental Disorder
  JOURNAL   Am J Hum Genet 104 (2), 287-298 (2019)
   PUBMED   30661771
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Colvin,S.C., Maier,B., Morris,D.L., Tersey,S.A. and Mirmira,R.G.
  TITLE     Deoxyhypusine synthase promotes differentiation and proliferation
            of T helper type 1 (Th1) cells in autoimmune diabetes
  JOURNAL   J Biol Chem 288 (51), 36226-36235 (2013)
   PUBMED   24196968
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Nguyen,S., Jones,D.C., Wyllie,S., Fairlamb,A.H. and Phillips,M.A.
  TITLE     Allosteric activation of trypanosomatid deoxyhypusine synthase by a
            catalytically dead paralog
  JOURNAL   J Biol Chem 288 (21), 15256-15267 (2013)
   PUBMED   23525104
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Umland,T.C., Wolff,E.C., Park,M.H. and Davies,D.R.
  TITLE     A new crystal structure of deoxyhypusine synthase reveals the
            configuration of the active enzyme and of an enzyme.NAD.inhibitor
            ternary complex
  JOURNAL   J Biol Chem 279 (27), 28697-28705 (2004)
   PUBMED   15100216
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Wolff,E.C., Folk,J.E. and Park,M.H.
  TITLE     Enzyme-substrate intermediate formation at lysine 329 of human
            deoxyhypusine synthase
  JOURNAL   J Biol Chem 272 (25), 15865-15871 (1997)
   PUBMED   9188485
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Bevec,D., Kappel,B., Jaksche,H., Csonga,R., Hauber,J., Klier,H. and
            Steinkasserer,A.
  TITLE     Molecular characterization of a cDNA encoding functional human
            deoxyhypusine synthase and chromosomal mapping of the corresponding
            gene locus
  JOURNAL   FEBS Lett 378 (2), 195-198 (1996)
   PUBMED   8549832
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Joe,Y.A., Wolff,E.C. and Park,M.H.
  TITLE     Cloning and expression of human deoxyhypusine synthase cDNA.
            Structure-function studies with the recombinant enzyme and mutant
            proteins
  JOURNAL   J Biol Chem 270 (38), 22386-22392 (1995)
   PUBMED   7673224
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Wolff,E.C., Lee,Y.B., Chung,S.I., Folk,J.E. and Park,M.H.
  TITLE     Deoxyhypusine synthase from rat testis: purification and
            characterization
  JOURNAL   J Biol Chem 270 (15), 8660-8666 (1995)
   PUBMED   7721768
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079188.1.
            
            On Sep 10, 2004 this sequence version replaced XP_213837.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079188.1, FQ214612.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..369
                     /product="deoxyhypusine synthase"
                     /EC_number="2.5.1.46"
                     /note="DHS"
                     /calculated_mol_wt=40574
     Region          44..354
                     /region_name="DS"
                     /note="Deoxyhypusine synthase; pfam01916"
                     /db_xref="CDD:460382"
     CDS             1..369
                     /gene="Dhps"
                     /coded_by="NM_001004207.1:75..1184"
                     /db_xref="GeneID:288923"
                     /db_xref="RGD:1303326"
ORIGIN      
        1 megtpsgaap ssalaavlkh ssalppesaq vqgydfnrgv dyhalleayg ttgfqatnfg
       61 ravqqvnami ekkleplavd edhhedltqs rrpltgctif lgytsnliss giretirylv
      121 qhnmvdvlvt taggveedli kclaptylge fslrgkelre nginrignll vpndnyckfe
      181 dwlmpildqm vqeqntegvk wtpskmisrl gkeinnpesv yywahknhip vlspaltdgs
      241 lgdmiffhsy knpglvldiv edlrlinmqa ifakrtgmii lgggvvkhhi ananlmrnga
      301 dyavyintaq efdgsdsgar pdeavswgki rmdaqpvkvy adaslvfpll vaetfaqkad
      361 afraekned
//
LOCUS       NP_612544               1043 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor-interacting protein 2 [Rattus norvegicus].
ACCESSION   NP_612544
VERSION     NP_612544.2
DBSOURCE    REFSEQ: accession NM_138535.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Fouillade,C., Baron-Menguy,C., Domenga-Denier,V., Thibault,C.,
            Takamiya,K., Huganir,R. and Joutel,A.
  TITLE     Transcriptome analysis for Notch3 target genes identifies Grip2 as
            a novel regulator of myogenic response in the cerebrovasculature
  JOURNAL   Arterioscler Thromb Vasc Biol 33 (1), 76-86 (2013)
   PUBMED   23117660
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Mao,L., Takamiya,K., Thomas,G., Lin,D.T. and Huganir,R.L.
  TITLE     GRIP1 and 2 regulate activity-dependent AMPA receptor recycling via
            exocyst complex interactions
  JOURNAL   Proc Natl Acad Sci U S A 107 (44), 19038-19043 (2010)
   PUBMED   20956289
  REMARK    GeneRIF: GRIP1 and 2 regulate activity-dependent AMPA receptor
            recycling via exocyst complex interactions.
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Misra,C., Restituito,S., Ferreira,J., Rameau,G.A., Fu,J. and
            Ziff,E.B.
  TITLE     Regulation of synaptic structure and function by palmitoylated AMPA
            receptor binding protein
  JOURNAL   Mol Cell Neurosci 43 (4), 341-352 (2010)
   PUBMED   20083202
  REMARK    GeneRIF: postsynaptic palmitoylated ABP induces pre and
            postsynaptic changes that are dependent on palmitoylation and
            likely achieved through ABP association with a multi-molecular cell
            surface signaling complex.
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Marsden,K.C., Beattie,J.B., Friedenthal,J. and Carroll,R.C.
  TITLE     NMDA receptor activation potentiates inhibitory transmission
            through GABA receptor-associated protein-dependent exocytosis of
            GABA(A) receptors
  JOURNAL   J Neurosci 27 (52), 14326-14337 (2007)
   PUBMED   18160640
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Lu,W. and Ziff,E.B.
  TITLE     PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
  JOURNAL   Neuron 47 (3), 407-421 (2005)
   PUBMED   16055064
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Dong,H., Zhang,P., Song,I., Petralia,R.S., Liao,D. and Huganir,R.L.
  TITLE     Characterization of the glutamate receptor-interacting proteins
            GRIP1 and GRIP2
  JOURNAL   J Neurosci 19 (16), 6930-6941 (1999)
   PUBMED   10436050
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   Wyszynski,M., Valtschanoff,J.G., Naisbitt,S., Dunah,A.W., Kim,E.,
            Standaert,D.G., Weinberg,R. and Sheng,M.
  TITLE     Association of AMPA receptors with a subset of glutamate
            receptor-interacting protein in vivo
  JOURNAL   J Neurosci 19 (15), 6528-6537 (1999)
   PUBMED   10414981
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Bruckner,K., Pablo Labrador,J., Scheiffele,P., Herb,A.,
            Seeburg,P.H. and Klein,R.
  TITLE     EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
            membrane microdomains
  JOURNAL   Neuron 22 (3), 511-524 (1999)
   PUBMED   10197531
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   Srivastava,S., Osten,P., Vilim,F.S., Khatri,L., Inman,G.,
            States,B., Daly,C., DeSouza,S., Abagyan,R., Valtschanoff,J.G.,
            Weinberg,R.J. and Ziff,E.B.
  TITLE     Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA
            receptor-binding protein ABP
  JOURNAL   Neuron 21 (3), 581-591 (1998)
   PUBMED   9768844
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Nishimune,A., Isaac,J.T., Molnar,E., Noel,J., Nash,S.R., Tagaya,M.,
            Collingridge,G.L., Nakanishi,S. and Henley,J.M.
  TITLE     NSF binding to GluR2 regulates synaptic transmission
  JOURNAL   Neuron 21 (1), 87-97 (1998)
   PUBMED   9697854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF205193.1 and JAXUCZ010000004.1.
            
            On Oct 10, 2007 this sequence version replaced NP_612544.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF205193.1, AF072509.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..1043
                     /product="glutamate receptor-interacting protein 2"
                     /note="AMPA receptor-interacting protein GRIP2; GRIP-2;
                     AMPA receptor binding protein"
                     /calculated_mol_wt=112358
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WTW1.1)"
     Region          52..134
                     /region_name="PDZ1_GRIP1-2-like"
                     /note="PDZ domain 1 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06687"
                     /db_xref="CDD:467175"
     Site            order(63..69,81,84,114,118,121..122)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467175"
     Region          150..238
                     /region_name="PDZ2_GRIP1-2-like"
                     /note="PDZ domain 2 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06681"
                     /db_xref="CDD:467169"
     Site            order(162..168,184,187,217,221,224..225)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467169"
     Region          250..335
                     /region_name="PDZ3_GRIP1-2-like"
                     /note="PDZ domain 3 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06684"
                     /db_xref="CDD:467172"
     Site            order(263..269,282,285,315,319,322..323)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467172"
     Region          371..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW1.1)"
     Region          450..550
                     /region_name="PDZ4_GRIP1-2-like"
                     /note="PDZ domain 4 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06686"
                     /db_xref="CDD:467174"
     Site            order(455..458,499..500,502..504,543,545..550)
                     /site_type="other"
                     /note="PDZ5 interface [polypeptide binding]"
                     /db_xref="CDD:467174"
     Site            order(468..474,490,493,523,527,530..531)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467174"
     Region          558..641
                     /region_name="PDZ5_GRIP1-2-like"
                     /note="PDZ domain 5 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06682"
                     /db_xref="CDD:467170"
     Site            order(569..575,588,591,621,625,628..629)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467170"
     Region          654..738
                     /region_name="PDZ6_GRIP1-2-like"
                     /note="PDZ domain 6 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06683"
                     /db_xref="CDD:467171"
     Site            order(667..673,685,688,718,722,725..726)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467171"
     Region          745..769
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW1.1)"
     Region          786..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTW1.1)"
     Region          938..1022
                     /region_name="PDZ7_GRIP1-2-like"
                     /note="PDZ domain 7 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06685"
                     /db_xref="CDD:467173"
     Site            order(953..959,970,973,1002,1006,1009..1010)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     Site            order(992,995,1000,1003..1004,1007..1008)
                     /site_type="other"
                     /note="GRASP-1 binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     CDS             1..1043
                     /gene="Grip2"
                     /gene_synonym="Abp"
                     /coded_by="NM_138535.2:97..3228"
                     /db_xref="GeneID:171571"
                     /db_xref="RGD:621668"
ORIGIN      
        1 mlavslkwrl gvvrrrpkdd gpyskggkdt agtdgalvcr rqsipeefrg itmvelikre
       61 gstlgltisg gtdkdgkprv snlrpgglaa rsdllnvgdy irsvngirlt rlrhdeiitl
      121 lknvgervvl eveyelpppa pennpriisk tvdvslykeg nsfgfvlrgg ahedlhksrp
      181 lvltyvrpgg padregslkv gdrllsidgi plhgashata iatlqqcshe alfqveydva
      241 tpdtvanasg plvveiaktp gsalgisltt gshrnkpait idrikpasvv drsgalhagd
      301 hilaidgtst ehcslveatk llasvtekvr leilpapqsr rplkppeavr iqrseqlhhw
      361 dpcvpschsp rpshcraptw apggqdqsrs vsstpfsspt mnpafpcana stlprgpmsp
      421 rttagrrrqr rkehrsslsl asstvgpggq ivhtettevv lcgdplsgfg lqlqggifat
      481 etlsspplvr fiepdspaer cgllqvgdrv laingiated gtmeeanqll rdaalarkvv
      541 leiefdvaes vipssgtfhv klpkrrgvel gitissasrk rgepliisdi kkgsvahrtg
      601 tlepgdklla idnirldhcp meyavqilrq cedlvklkir kdednsdeqe ssgavsytve
      661 lkryggplgi tisgteepfd piiisgltkr glaertgaih vgdrilains vslkgrplse
      721 aihllqvage tvtlkikkql drpllprqsg slseasdvde dppealkggl ltthfspavp
      781 svdsaveswg ssateggfgg sgsytpqvav rsvtpqewrs srlksspppl eprrtsytpg
      841 ptdesfpeee egdweppmsp apgpareegf wrvlgealed lescgqsell releasimtg
      901 tvqsvavdgr pgsrpwrrsr evgtspedlq elllptplem hrvtlhkdpv rndfgfsvsd
      961 gllekgvyvh tvridgpaqh gglqpfdrll qvnhvrtrdf dcclavplla eagdilelvv
     1021 srnplaqsrr tpgapgpssp qmi
//
LOCUS       NP_612523                490 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2C13, male-specific [Rattus norvegicus].
ACCESSION   NP_612523
VERSION     NP_612523.1
DBSOURCE    REFSEQ: accession NM_138514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Eguchi,H., Westin,S., Strom,A., Gustafsson,J.A. and
            Zaphiropoulos,P.G.
  TITLE     Gene structure and expression of the rat cytochrome P450IIC13, a
            polymorphic, male-specific cytochrome in the P450IIC subfamily
  JOURNAL   Biochemistry 30 (45), 10844-10849 (1991)
   PUBMED   1834171
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Yeowell,H.N., McClellan-Green,P.D., Negishi,M. and Goldstein,J.A.
  TITLE     Characterization of a cDNA for the unexpressed form of cytochrome
            P-450g from the (-g) rat and differentiation of its mRNA from that
            of the (+g) phenotype using specific oligoprobes
  JOURNAL   Biochemistry 29 (3), 713-718 (1990)
   PUBMED   2337591
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Zaphiropoulos,P.G., Strom,A., Robertson,J.A. and Gustafsson,J.A.
  TITLE     Structural and regulatory analysis of the male-specific rat liver
            cytochrome P-450 g: repression by continuous growth hormone
            administration
  JOURNAL   Mol Endocrinol 4 (1), 53-58 (1990)
   PUBMED   2325668
REFERENCE   4  (residues 1 to 490)
  AUTHORS   McClellan-Green,P.D., Negishi,M. and Goldstein,J.A.
  TITLE     Characterization of a cDNA for rat P-450g, a highly polymorphic,
            male-specific cytochrome in the P-450IIC subfamily
  JOURNAL   Biochemistry 28 (14), 5832-5839 (1989)
   PUBMED   2775738
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Matsumoto,T., Emi,Y., Kawabata,S. and Omura,T.
  TITLE     Purification and characterization of three male-specific and one
            female-specific forms of cytochrome P-450 from rat liver microsomes
  JOURNAL   J Biochem 100 (5), 1359-1371 (1986)
   PUBMED   2434473
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M32277.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02861.1, M32277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..490
                     /product="cytochrome P450 2C13, male-specific"
                     /EC_number="1.14.14.1"
                     /note="cytochrome P450, 2c38; UT-5; P-450g; P450-G;
                     CYPIIC13; cytochrome P-450g; cytochrome P450-G; cytochrome
                     P450-UT-5; CYP2C13 (+); cytochrome P450 g (+); cytochrome
                     P450 2C13, male-specific-like"
                     /calculated_mol_wt=55709
     Region          61..485
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(97,112..113,120,124,294,297..298,301..302,305,356,
                     361..362,365..366,368,427..429,433,435..437,441,444)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(108,113..114,204..205,208,214,233,237,240,292..293,
                     296..297,300..301,362,366,476..477)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     CDS             1..490
                     /gene="Cyp2c13"
                     /gene_synonym="Cyp2c38"
                     /coded_by="NM_138514.1:12..1484"
                     /db_xref="GeneID:171521"
                     /db_xref="RGD:620363"
ORIGIN      
        1 mdpvvvllls lffllflslw rlssgrgklp pgptplpiig nffqvdmkdi rqsltnfskt
       61 ygpvytlyvg sqptvvlhgy ealkealvdh geefsgrgrl picekvakgq giafshgnvw
      121 katrhftvkt lrnlgmgkgt iedkvqeeak wlvkelkktn gspcdpqfim gcapgnvicc
      181 iilqnrfdye dkdflnliek vneavkiiss pgiqvfnifp illdycpgnh niylknytwv
      241 ksyllekike heesldvsnp rdfidyflie rnqenanqwm nytlehlaim vtdlffagie
      301 tvsstmrfal lllmkyphvt akvqeeidhv igrhrspsmq drshmpytna mvhevqryid
      361 igpngllhdv tcdtkfrnyf ipkgtavlts ltsvlhdske fpnpemfdpg hfldengnfk
      421 ksdyfipfsa gkrmclgesl armelflflt tilqnfklks lvdpkdintt picsslssvp
      481 ptfqmrfipl
//
LOCUS       NP_113940                624 aa            linear   ROD 27-APR-2025
DEFINITION  basal cell adhesion molecule precursor [Rattus norvegicus].
ACCESSION   NP_113940
VERSION     NP_113940.1
DBSOURCE    REFSEQ: accession NM_031752.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Liu,M., Liao,L., Gao,Y., Yin,Y., Wei,X., Xu,Q., Gao,L. and Zhou,R.
  TITLE     BCAM Deficiency May Contribute to Preeclampsia by Suppressing the
            PIK3R6/p-STAT3 Signaling
  JOURNAL   Hypertension 79 (12), 2830-2842 (2022)
   PUBMED   36252138
  REMARK    GeneRIF: BCAM Deficiency May Contribute to Preeclampsia by
            Suppressing the PIK3R6/p-STAT3 Signaling.
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Piteau,M., Papatheodorou,P., Schwan,C., Schlosser,A., Aktories,K.
            and Schmidt,G.
  TITLE     Lu/BCAM adhesion glycoprotein is a receptor for Escherichia coli
            Cytotoxic Necrotizing Factor 1 (CNF1)
  JOURNAL   PLoS Pathog 10 (1), e1003884 (2014)
   PUBMED   24453976
  REMARK    Erratum:[PLoS Pathog. 2014 Jan;10(1).
            doi:10.1371/annotation/6eec6403-e090-4283-aa34-34cc58ca0bbb]
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Akiyama,H., Iwahana,Y., Suda,M., Yoshimura,A., Kogai,H.,
            Nagashima,A., Ohtsuka,H., Komiya,Y. and Tashiro,F.
  TITLE     The FBI1/Akirin2 target gene, BCAM, acts as a suppressive oncogene
  JOURNAL   PLoS One 8 (11), e78716 (2013)
   PUBMED   24223164
  REMARK    GeneRIF: Data indicate that the 14-3-3beta-FBI1/Akirin2 complex
            bound to the basal cell adhesion molecule (BCAM) promoter and
            repressed transcription.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Vainionpaa,N., Kikkawa,Y., Lounatmaa,K., Miner,J.H., Rousselle,P.
            and Virtanen,I.
  TITLE     Laminin-10 and Lutheran blood group glycoproteins in adhesion of
            human endothelial cells
  JOURNAL   Am J Physiol Cell Physiol 290 (3), C764-C775 (2006)
   PUBMED   16236823
REFERENCE   8  (residues 1 to 624)
  AUTHORS   Moulson,C.L., Li,C. and Miner,J.H.
  TITLE     Localization of Lutheran, a novel laminin receptor, in normal,
            knockout, and transgenic mice suggests an interaction with laminin
            alpha5 in vivo
  JOURNAL   Dev Dyn 222 (1), 101-114 (2001)
   PUBMED   11507772
REFERENCE   9  (residues 1 to 624)
  AUTHORS   El Nemer,W., Gane,P., Colin,Y., D'Ambrosio,A.M., Callebaut,I.,
            Cartron,J.P. and Van Kim,C.L.
  TITLE     Characterization of the laminin binding domains of the Lutheran
            blood group glycoprotein
  JOURNAL   J Biol Chem 276 (26), 23757-23762 (2001)
   PUBMED   11319237
REFERENCE   10 (residues 1 to 624)
  AUTHORS   Rahuel,C., Colin,Y., Goossens,D., Gane,P., El Nemer,W.,
            Cartron,J.P. and Le Van Kim,C.
  TITLE     Characterization of a mouse liminin receptor gene homologous to the
            human blood group Lutheran gene
  JOURNAL   Immunogenetics 50 (5-6), 271-277 (1999)
   PUBMED   10630290
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072479.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072479.1, AB035510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..624
                     /product="basal cell adhesion molecule precursor"
                     /note="Lutheran blood group (Auberger b antigen included);
                     lutheran antigen; B-CAM cell surface glycoprotein"
                     /calculated_mol_wt=64899
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2631
     Region          25..137
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     mat_peptide     26..624
                     /product="Basal cell adhesion molecule.
                     /id=PRO_0000383339"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESS6.1)"
                     /calculated_mol_wt=64899
     Region          43..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          58..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          100..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          116..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          130..133
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          145..242
                     /region_name="C2-set_2"
                     /note="CD80-like C2-set immunoglobulin domain; pfam08205"
                     /db_xref="CDD:400489"
     Region          163..166
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          176..180
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          214..218
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          228..233
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          265..334
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Region          <377..439
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            378
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Region          452..522
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          477..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Region          574..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50895; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50895; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50895; propagated from
                     UniProtKB/Swiss-Prot (Q9ESS6.1)"
     CDS             1..624
                     /gene="Bcam"
                     /gene_synonym="Lu"
                     /coded_by="NM_031752.2:10..1884"
                     /db_xref="GeneID:78958"
                     /db_xref="RGD:68378"
ORIGIN      
        1 meppdaragl lwltlllsgy sgaqaelhvs vpprvevmrg eqialdctpr ehpenyvlew
       61 llvdasgarh rlasvepqgs eflgtihnsr grrppykids lgrlviaeaq vgderdyvcv
      121 vkagaagtse atssvrvfat peatevapnk gtlsvmeqfa qeiatcssnn gnpvpritwy
      181 qngqrldvpm elnskgymts rtvreasgly sltstlylrl hkedrdasfh caahydlpsg
      241 qhgrldshtf rltlhypteh vefwvgspst tegwvregda vqllcqgdgs pspeysffre
      301 qgnqeeqlnv nlkgnltleg vhrsqsgiyg crvedydade evqlvkklkl hvayldplel
      361 svpeefsvfl nssgtvvncs arglpapivr wtkdsvtvad gpilsldsvt fdsagtytce
      421 astptvplls rtqsfqlvvq gapelkpnei kpksgtswte gdevmltcsa rgfpepkltw
      481 sqrgdttpae ppfegrgwms ssltlkvtsa lsregvscea snihgknghv fhfgsvapqt
      541 aqagvavmav avsvgllllv vaafycmrrk grpgccqrae kgapparepe lshsgserpe
      601 htgllmggps gggrggnggf gdec
//
LOCUS       NP_001004133            1252 aa            linear   ROD 27-APR-2025
DEFINITION  SH3 and multiple ankyrin repeat domains protein 2 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001004133 XP_003749075
VERSION     NP_001004133.1
DBSOURCE    REFSEQ: accession NM_001004133.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1252)
  AUTHORS   Li,N., Ren,C., Li,S., Yu,W., Jin,K. and Ji,X.
  TITLE     Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway
  JOURNAL   Prog Neurobiol 230, 102514 (2023)
   PUBMED   37574039
  REMARK    GeneRIF: Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway.
REFERENCE   2  (residues 1 to 1252)
  AUTHORS   Fu,Y., Liu,D., Guo,J., Long,H., Xiao,W., Xiao,W., Feng,L., Luo,Z.
            and Xiao,B.
  TITLE     Dynamic Change of Shanks Gene mRNA Expression and DNA Methylation
            in Epileptic Rat Model and Human Patients
  JOURNAL   Mol Neurobiol 57 (9), 3712-3726 (2020)
   PUBMED   32564287
  REMARK    GeneRIF: Dynamic Change of Shanks Gene mRNA Expression and DNA
            Methylation in Epileptic Rat Model and Human Patients.
REFERENCE   3  (residues 1 to 1252)
  AUTHORS   Ishida,H., Skorobogatov,A., Yamniuk,A.P. and Vogel,H.J.
  TITLE     Solution structures of the SH3 domains from Shank scaffold proteins
            and their interactions with Cav1.3 calcium channels
  JOURNAL   FEBS Lett 592 (16), 2786-2797 (2018)
   PUBMED   30058071
REFERENCE   4  (residues 1 to 1252)
  AUTHORS   Modi,M.E., Brooks,J.M., Guilmette,E.R., Beyna,M., Graf,R., Reim,D.,
            Schmeisser,M.J., Boeckers,T.M., O'Donnell,P. and Buhl,D.L.
  TITLE     Hyperactivity and Hypermotivation Associated With Increased
            Striatal mGluR1 Signaling in a Shank2 Rat Model of Autism
  JOURNAL   Front Mol Neurosci 11, 107 (2018)
   PUBMED   29970986
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1252)
  AUTHORS   Shi,R., Redman,P., Ghose,D., Hwang,H., Liu,Y., Ren,X., Ding,L.J.,
            Liu,M., Jones,K.J. and Xu,W.
  TITLE     Shank Proteins Differentially Regulate Synaptic Transmission
  JOURNAL   eNeuro 4 (6) (2017)
   PUBMED   29250591
  REMARK    GeneRIF: Loss of scaffold proteins via knockdown of Shank1 or
            Shank2, but not Shank3, led to a reduction of the number but not
            the unitary response of AMPAR-containing synapses. Only when both
            Shank1 and Shank2 were knocked down, were both the number and the
            unitary response of active synapses reduced. This reduction was
            accompanied by a decrease in NMDAR-mediated synaptic response.
            Erratum:[eNeuro. 2018 Mar 19;5(1):ENEURO.0073-18.2018. doi:
            10.1523/ENEURO.0073-18.2018. PMID: 29569864]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1252)
  AUTHORS   Boeckers,T.M., Winter,C., Smalla,K.H., Kreutz,M.R., Bockmann,J.,
            Seidenbecher,C., Garner,C.C. and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated proteins ProSAP1 and ProSAP2
            interact with synaptic proteins of the SAPAP/GKAP family
  JOURNAL   Biochem Biophys Res Commun 264 (1), 247-252 (1999)
   PUBMED   10527873
REFERENCE   7  (residues 1 to 1252)
  AUTHORS   Lim,S., Naisbitt,S., Yoon,J., Hwang,J.I., Suh,P.G., Sheng,M. and
            Kim,E.
  TITLE     Characterization of the Shank family of synaptic proteins. Multiple
            genes, alternative splicing, and differential expression in brain
            and development
  JOURNAL   J Biol Chem 274 (41), 29510-29518 (1999)
   PUBMED   10506216
REFERENCE   8  (residues 1 to 1252)
  AUTHORS   Boeckers,T.M., Kreutz,M.R., Winter,C., Zuschratter,W., Smalla,K.H.,
            Sanmarti-Vila,L., Wex,H., Langnaese,K., Bockmann,J., Garner,C.C.
            and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated protein-1/cortactin binding protein
            1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the
            postsynaptic density
  JOURNAL   J Neurosci 19 (15), 6506-6518 (1999)
   PUBMED   10414979
REFERENCE   9  (residues 1 to 1252)
  AUTHORS   Zitzer,H., Richter,D. and Kreienkamp,H.J.
  TITLE     Agonist-dependent interaction of the rat somatostatin receptor
            subtype 2 with cortactin-binding protein 1
  JOURNAL   J Biol Chem 274 (26), 18153-18156 (1999)
   PUBMED   10373412
REFERENCE   10 (residues 1 to 1252)
  AUTHORS   Du,Y., Weed,S.A., Xiong,W.C., Marshall,T.D. and Parsons,J.T.
  TITLE     Identification of a novel cortactin SH3 domain-binding protein and
            its localization to growth cones of cultured neurons
  JOURNAL   Mol Cell Biol 18 (10), 5838-5851 (1998)
   PUBMED   9742101
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF060116.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003749075.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF060116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155322, SAMD00155324
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1252
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..1252
                     /product="SH3 and multiple ankyrin repeat domains protein
                     2 isoform b"
                     /note="SH3 and multiple ankyrin repeat domains protein 2;
                     GKAP/SAPAP-interacting protein; proline-rich
                     synapse-associated protein 1; cortactin-binding protein 1;
                     SH3 and multiple ankyrin repeat domains protein 2-like;
                     SH3/ankyrin domain gene 2"
                     /calculated_mol_wt=134151
     Region          30..131
                     /region_name="PDZ_SHANK1_3-like"
                     /note="PDZ domain of SH3 and multiple ankyrin repeat
                     domains protein 1 (SHANK1), SHANK2, SHANK3, and related
                     domains; cd06746"
                     /db_xref="CDD:467228"
     Site            order(30..35,65..68,103,105,128)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467228"
     Site            order(47..53,77,80,109,113,116..117)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467228"
     Region          <471..880
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1185..1250
                     /region_name="SAM_Shank1,2,3"
                     /note="SAM domain of Shank1,2,3 family proteins; cd09506"
                     /db_xref="CDD:188905"
     Site            order(1188..1190,1192,1206..1207,1220)
                     /site_type="other"
                     /note="polymer interface (interfiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     Site            order(1205..1206,1238)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188905"
     Site            order(1229,1231,1236)
                     /site_type="other"
                     /note="polymer interface (intrafiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     CDS             1..1252
                     /gene="Shank2"
                     /gene_synonym="CortBP1; ProSAP1; Shank2E; Spank-3"
                     /coded_by="NM_001004133.1:425..4183"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:171093"
                     /db_xref="RGD:628772"
ORIGIN      
        1 mmsvpgggaa tvmmtgynng ryprnslysd ciiedktvvl qkkdnegfgf vlrgakadtp
       61 ieeftptpaf palqylesvd eggvawqagl rtgdflievn nenvvkvghr qvvnmirqgg
      121 nhlvlkvvtv trnldpddta rkkappppkr apttaltvrs ksmtaeleel vdkdkpeeiv
      181 paskpsrtae nvaiesrvat ikqrptsrcf paasdvnsvy erqgiavmtp tvpgspkgpf
      241 lglprgtmrr qksidsrifl sgiteeerqf lappmlkftr slsmpdtsed ippppqsvpp
      301 sppppsptty ncprsptprv ygtikpafnq npvakvppat rsdtvatmmr ekgmfyrrel
      361 drfsldsedv ysrspapqaa frtkrgqmpe npysevgkia skavyvpakp arrkgmlvkq
      421 snvedspekt csipiptiiv kepstsssgk ssqgssmeid pqatepgqlr pddsltvssp
      481 faaaiagavr drekrlearr nspaflstdl gdedvglgpp aprmqpskfp eeggfgdede
      541 teqpllptpg aaprelenhf lgggeagaqg eaggplssts kakgpesgpa aalkssspas
      601 penyvhpltg rlldpsspla lalsardram qesqqghkge apkadlnkpl yidtkmrpsv
      661 esgfppvtrq ntrgplrrqe tenkyetdls kdrraddkkn mlinivdtaq qksagllmvh
      721 tvdipvagpp leeeedredg dtkpdhspst vpegvpkteg alqisaapep aaapgrtiva
      781 agsveeavil pfrippppla svdldedflf teplppplef ansfdipddr aasvpaladl
      841 vkqkksdtpq ppslnssqpa nstdskkpag isnclpssfl pppesfdavt dsgieevdsr
      901 sssdhhlett stistvssis tlsseggesm dtctvyadgq afvvdkppvp pkpkmkpivh
      961 ksnalyqdtl peedtdgfvi pppapppppg saqagvakvi qprtsklwgd vtevkspils
     1021 gpkanvisel nsilqqmnrg ksvkpgegle lpvgaksanl aprspevmst vsgtrsttvt
     1081 ftvrpgtsqp itlqsrppdy esrtsgprra pspvvsptel skeilptpps aaaaspsptl
     1141 sdvfslpsqs pagdlfglnp agrsrspsps ilqqpisnkp fttkpvhlwt kpdvadwles
     1201 lnlgehketf mdneidgshl pnlqkedlid lgvtrvghrm nieralkqll dr
//
LOCUS       NP_446070                721 aa            linear   ROD 27-APR-2025
DEFINITION  BBSome complex member BBS2 [Rattus norvegicus].
ACCESSION   NP_446070
VERSION     NP_446070.1
DBSOURCE    REFSEQ: accession NM_053618.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Shevach,E., Ali,M., Mizrahi-Meissonnier,L., McKibbin,M.,
            El-Asrag,M., Watson,C.M., Inglehearn,C.F., Ben-Yosef,T.,
            Blumenfeld,A., Jalas,C., Banin,E. and Sharon,D.
  TITLE     Association between missense mutations in the BBS2 gene and
            nonsyndromic retinitis pigmentosa
  JOURNAL   JAMA Ophthalmol 133 (3), 312-318 (2015)
   PUBMED   25541840
REFERENCE   2  (residues 1 to 721)
  AUTHORS   May-Simera,H.L., Petralia,R.S., Montcouquiol,M., Wang,Y.X.,
            Szarama,K.B., Liu,Y., Lin,W., Deans,M.R., Pazour,G.J. and
            Kelley,M.W.
  TITLE     Ciliary proteins Bbs8 and Ift20 promote planar cell polarity in the
            cochlea
  JOURNAL   Development 142 (3), 555-566 (2015)
   PUBMED   25605782
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Chamling,X., Seo,S., Searby,C.C., Kim,G., Slusarski,D.C. and
            Sheffield,V.C.
  TITLE     The centriolar satellite protein AZI1 interacts with BBS4 and
            regulates ciliary trafficking of the BBSome
  JOURNAL   PLoS Genet 10 (2), e1004083 (2014)
   PUBMED   24550735
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Zhang,Q., Yu,D., Seo,S., Stone,E.M. and Sheffield,V.C.
  TITLE     Intrinsic protein-protein interaction-mediated and
            chaperonin-assisted sequential assembly of stable bardet-biedl
            syndrome protein complex, the BBSome
  JOURNAL   J Biol Chem 287 (24), 20625-20635 (2012)
   PUBMED   22500027
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Gascue,C., Tan,P.L., Cardenas-Rodriguez,M., Libisch,G.,
            Fernandez-Calero,T., Liu,Y.P., Astrada,S., Robello,C., Naya,H.,
            Katsanis,N. and Badano,J.L.
  TITLE     Direct role of Bardet-Biedl syndrome proteins in transcriptional
            regulation
  JOURNAL   J Cell Sci 125 (Pt 2), 362-375 (2012)
   PUBMED   22302990
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Forti,E., Aksanov,O. and Birk,R.Z.
  TITLE     Temporal expression pattern of Bardet-Biedl syndrome genes in
            adipogenesis
  JOURNAL   Int J Biochem Cell Biol 39 (5), 1055-1062 (2007)
   PUBMED   17379567
REFERENCE   7  (residues 1 to 721)
  AUTHORS   Benzinou,M., Walley,A., Lobbens,S., Charles,M.A., Jouret,B.,
            Fumeron,F., Balkau,B., Meyre,D. and Froguel,P.
  TITLE     Bardet-Biedl syndrome gene variants are associated with both
            childhood and adult common obesity in French Caucasians
  JOURNAL   Diabetes 55 (10), 2876-2882 (2006)
   PUBMED   17003356
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Nishimura,D.Y., Fath,M., Mullins,R.F., Searby,C., Andrews,M.,
            Davis,R., Andorf,J.L., Mykytyn,K., Swiderski,R.E., Yang,B.,
            Carmi,R., Stone,E.M. and Sheffield,V.C.
  TITLE     Bbs2-null mice have neurosensory deficits, a defect in social
            dominance, and retinopathy associated with mislocalization of
            rhodopsin
  JOURNAL   Proc Natl Acad Sci U S A 101 (47), 16588-16593 (2004)
   PUBMED   15539463
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Nishimura,D.Y., Searby,C.C., Carmi,R., Elbedour,K., Van
            Maldergem,L., Fulton,A.B., Lam,B.L., Powell,B.R., Swiderski,R.E.,
            Bugge,K.E., Haider,N.B., Kwitek-Black,A.E., Ying,L., Duhl,D.M.,
            Gorman,S.W., Heon,E., Iannaccone,A., Bonneau,D., Biesecker,L.G.,
            Jacobson,S.G., Stone,E.M. and Sheffield,V.C.
  TITLE     Positional cloning of a novel gene on chromosome 16q causing
            Bardet-Biedl syndrome (BBS2)
  JOURNAL   Hum Mol Genet 10 (8), 865-874 (2001)
   PUBMED   11285252
REFERENCE   10 (residues 1 to 721)
  AUTHORS   Kwitek-Black,A.E., Carmi,R., Duyk,G.M., Buetow,K.H., Elbedour,K.,
            Parvari,R., Yandava,C.N., Stone,E.M. and Sheffield,V.C.
  TITLE     Linkage of Bardet-Biedl syndrome to chromosome 16q and evidence for
            non-allelic genetic heterogeneity
  JOURNAL   Nat Genet 5 (4), 392-396 (1993)
   PUBMED   8298649
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF342738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF342738.1, SRR8487231.40588.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..721
                     /product="BBSome complex member BBS2"
                     /note="bardet-Biedl syndrome 2 protein homolog;
                     Bardet-Biedl syndrome 2 homolog"
                     /calculated_mol_wt=79787
     Region          20..126
                     /region_name="BBS2_N"
                     /note="Ciliary BBSome complex subunit 2, N-terminal;
                     pfam14781"
                     /db_xref="CDD:464314"
     Region          165..272
                     /region_name="BBS2_Mid"
                     /note="Ciliary BBSome complex subunit 2, middle region;
                     pfam14783"
                     /db_xref="CDD:405473"
     Region          276..715
                     /region_name="BBS2_C"
                     /note="Ciliary BBSome complex subunit 2, C-terminal;
                     pfam14782"
                     /db_xref="CDD:464315"
     CDS             1..721
                     /gene="Bbs2"
                     /coded_by="NM_053618.1:99..2264"
                     /db_xref="GeneID:113948"
                     /db_xref="RGD:71091"
ORIGIN      
        1 mllpvftlkl rhkisprmva igrydgthpc laaatqagkv fihnphmrsq hfstsrvfqs
       61 plesdvslln inqtvsclga gvlnpelgyd tllvgtqtsl laydiynnsd lfyrevadga
      121 nalvlgtlgd iapplaiigg ncalqgfdhe gndlfwtvtg dnvhslalcd fdgdgksell
      181 vgsedfdirv fkedeivaem teteivtslc pmygsrfgya lsngtvgvyd ktarywriks
      241 knhamsihaf dinsdgvcel itgwsngkvd arsdrtgevi fkdnfssava gvvegdyrmd
      301 ghvqliccsv dgeirgylpg taemkgnlld tsveqglire lsqkkqnlll elrnyeentk
      361 aelssplnea dgqkgiipan tklhtalsvn lgndaqdaha elristsndt iiravlifae
      421 gifageshvv hpsthnlsss irvpitppkd vpvdlhlktf vgyrsstqfh vfelirqlpr
      481 ftmyaltspd aasepvsfvn fivveraqrm vtwlnqnfll pedsniqnap fhvcftslrn
      541 ggqlyikmkp sgeitvntdd idlagdiiqs masffaiedl qveadfpvyf eelrkvllkv
      601 deyhsvhqkl sanmadnsnl irsllvraed arlmrdmktm ktrymelydl nkdllngyki
      661 rcnnhtellg nlkavnqaiq ragrlrvgkp knqvisacrd airsnnintl frimrvgtap
      721 s
//
LOCUS       NP_001012051             340 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 367 [Rattus norvegicus].
ACCESSION   NP_001012051 XP_225104
VERSION     NP_001012051.1
DBSOURCE    REFSEQ: accession NM_001012051.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Asano,H., Murate,T., Naoe,T., Saito,H. and Stamatoyannopoulos,G.
  TITLE     Molecular cloning and characterization of ZFF29: a protein
            containing a unique Cys2His2 zinc-finger motif
  JOURNAL   Biochem J 384 (Pt 3), 647-653 (2004)
   PUBMED   15344908
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085804.1.
            
            On Feb 11, 2005 this sequence version replaced XP_225104.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..340
                     /product="zinc finger protein 367"
                     /calculated_mol_wt=37341
     Region          96..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z0.1)"
     Region          157..>230
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          159..179
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(164,166,168,170..171,174..175,178,194,196,200..201,
                     204..205,208,224,226,228,248..249,252..253,256)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          187..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          217..256
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          280..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z0.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7RTV3; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z0.1)"
     CDS             1..340
                     /gene="Zfp367"
                     /gene_synonym="Znf367"
                     /coded_by="NM_001012051.1:190..1212"
                     /db_xref="GeneID:306695"
                     /db_xref="RGD:1307136"
ORIGIN      
        1 mirgapapma epppvifchd spkrvlvsvi rttpatppcs svgepepppp lvptspgfsd
       61 fmvypwrwge nahnvtlspg aaggvvsagl paatelptlr gappssasva avsggedeee
      121 asspdsghlk dgirrgrpra dtvrdlineg ehsssrircn icnrvfprek slqahkrtht
      181 gerpylcdyp dcgkafvqsg qlkthqrlht gekpfvcsen gclsrfthan rhcpkhpyar
      241 lkreeptdtl skhqstdnka aaewlakywe mreqrtptlk gklvqkadqe qqdpleylqs
      301 deeddeksga qrrlqeqrer lhgalaliel anltgaplrq
//
LOCUS       NP_112648                390 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 11 [Rattus
            norvegicus].
ACCESSION   NP_112648
VERSION     NP_112648.2
DBSOURCE    REFSEQ: accession NM_031358.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Li,Y., Ba,M., Du,Y., Xia,C., Tan,S., Ng,K.P. and Ma,G.
  TITLE     Abeta1-42 increases the expression of neural KATP subunits
            Kir6.2/SUR1 via the NF-kappaB, p38 MAPK and PKC signal pathways in
            rat primary cholinergic neurons
  JOURNAL   Hum Exp Toxicol 38 (6), 665-674 (2019)
   PUBMED   30868916
  REMARK    GeneRIF: Our findings suggest that the NF-kappaB, p38 MAPK, and PKC
            signal pathways are partially involved in the upregulation of KATP
            subunits Kir6.2/SUR1 expression induced by Abeta1-42 cytotoxicity
            in neurons, which supports a potential theoretical basis of
            targeting these signal pathways in the treatment of Alzheimer's
            disease.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Wang,X. and Fitts,R.H.
  TITLE     Effects of regular exercise on ventricular myocyte biomechanics and
            KATP channel function
  JOURNAL   Am J Physiol Heart Circ Physiol 315 (4), H885-H896 (2018)
   PUBMED   30074836
  REMARK    GeneRIF: Up-regulation of the KATP channel accelerates
            repolarization and shortens action potential duration during stress
            and exercise.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Cooper,P.E., McClenaghan,C., Chen,X., Stary-Weinzinger,A. and
            Nichols,C.G.
  TITLE     Conserved functional consequences of disease-associated mutations
            in the slide helix of Kir6.1 and Kir6.2 subunits of the
            ATP-sensitive potassium channel
  JOURNAL   J Biol Chem 292 (42), 17387-17398 (2017)
   PUBMED   28842488
  REMARK    GeneRIF: both Kir6.1(V65M) and Kir6.2(V64M) mutations essentially
            abolish high-affinity sensitivity to the KATP blocker glibenclamide
            in both intact cells and excised patches. This raises the
            possibility that, at least for some CS mutations, sulfonylurea
            therapy may not prove to be successful and highlights the need for
            detailed pharmacogenomic analyses of CS mutations.
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Feng,Y., Liu,J., Wang,M., Liu,M., Shi,L., Yuan,W., Ye,J., Hu,D. and
            Wan,J.
  TITLE     The E23K variant of the Kir6.2 subunit of the ATP-sensitive
            potassium channel increases susceptibility to ventricular
            arrhythmia in response to ischemia in rats
  JOURNAL   Int J Cardiol 232, 192-198 (2017)
   PUBMED   28082085
  REMARK    GeneRIF: The E23K variant of the KATP channel increased the
            susceptibility to ventricular arrhythmia under acute ischemia
            stress.
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Martin,G.M., Yoshioka,C., Rex,E.A., Fay,J.F., Xie,Q., Whorton,M.R.,
            Chen,J.Z. and Shyng,S.L.
  TITLE     Cryo-EM structure of the ATP-sensitive potassium channel
            illuminates mechanisms of assembly and gating
  JOURNAL   Elife 6, e24149 (2017)
   PUBMED   28092267
  REMARK    GeneRIF: Intricate interactions between TMD0, the loop following
            TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP
            density is observed, suggest SUR1 may contribute to ATP and PIP2
            binding to enhance Kir6.2 sensitivity to both.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Moritz,W., Leech,C.A., Ferrer,J. and Habener,J.F.
  TITLE     Regulated expression of adenosine triphosphate-sensitive potassium
            channel subunits in pancreatic beta-cells
  JOURNAL   Endocrinology 142 (1), 129-138 (2001)
   PUBMED   11145575
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Thomas,P., Ye,Y. and Lightner,E.
  TITLE     Mutation of the pancreatic islet inward rectifier Kir6.2 also leads
            to familial persistent hyperinsulinemic hypoglycemia of infancy
  JOURNAL   Hum Mol Genet 5 (11), 1809-1812 (1996)
   PUBMED   8923010
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Isomoto,S., Kondo,C., Yamada,M., Matsumoto,S., Higashiguchi,O.,
            Horio,Y., Matsuzawa,Y. and Kurachi,Y.
  TITLE     A novel sulfonylurea receptor forms with BIR (Kir6.2) a smooth
            muscle type ATP-sensitive K+ channel
  JOURNAL   J Biol Chem 271 (40), 24321-24324 (1996)
   PUBMED   8798681
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Inagaki,N., Gonoi,T., Clement,J.P., Wang,C.Z., Aguilar-Bryan,L.,
            Bryan,J. and Seino,S.
  TITLE     A family of sulfonylurea receptors determines the pharmacological
            properties of ATP-sensitive K+ channels
  JOURNAL   Neuron 16 (5), 1011-1017 (1996)
   PUBMED   8630239
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Tokuyama,Y., Fan,Z., Furuta,H., Makielski,J.C., Polonsky,K.S.,
            Bell,G.I. and Yano,H.
  TITLE     Rat inwardly rectifying potassium channel Kir6.2: cloning
            electrophysiological characterization, and decreased expression in
            pancreatic islets of male Zucker diabetic fatty rats
  JOURNAL   Biochem Biophys Res Commun 220 (3), 532-538 (1996)
   PUBMED   8607800
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D61687.1, D86039.1, AB043638.1, BF565039.1 and AW527189.1.
            
            On Apr 4, 2002 this sequence version replaced NP_112648.1.
            
            Sequence Note: This RefSeq record was created using sequences from
            two different strains, W and Sprague-Dawley, because no single
            transcript from the same strain was available for the full length
            of the gene.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..390
                     /product="ATP-sensitive inward rectifier potassium channel
                     11"
                     /note="BIR; inward rectifier K(+) channel Kir6.2;
                     potassium channel, inwardly rectifying subfamily J member
                     11; potassium voltage-gated channel subfamily J member 11"
                     /calculated_mol_wt=43477
     Region          36..174
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            67..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70673.1)"
     Region          130..135
                     /region_name="Selectivity filter. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P70673.1)"
     Site            143..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70673.1)"
     Site            160
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P70673.1)"
     Region          181..354
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q14654; propagated from
                     UniProtKB/Swiss-Prot (P70673.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q14654; propagated from
                     UniProtKB/Swiss-Prot (P70673.1)"
     CDS             1..390
                     /gene="Kcnj11"
                     /gene_synonym="Kir6.2"
                     /coded_by="NM_031358.3:237..1409"
                     /db_xref="GeneID:83535"
                     /db_xref="RGD:69247"
ORIGIN      
        1 mlsrkgiipe eyvltrlaed ptepryrtre rrarfvskkg ncnvahknir eqgrflqdvf
       61 ttlvdlkwph tlliftmsfl cswllfamvw wliafahgdl apgegtnvpc vtsihsfssa
      121 flfsievqvt igfggrmvte ecplailili vqnivglmin aimlgcifmk taqahrraet
      181 lifskhavit lrhgrlcfml rvgdlrksmi isatihmqvv rkttspegev vplhqvdipm
      241 engvggnsif lvapliiyhv idsnsplydl apsdlhhhqd leiivilegv vettgittqa
      301 rtsyladeil wgqrfvpiva eedgrysvdy skfgntvkvp tplctarqld edrslldalt
      361 lassrgplrk rsvavakakp kfsispdsls
//
LOCUS       NP_742018                613 aa            linear   ROD 27-APR-2025
DEFINITION  TANK-binding kinase 1-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_742018
VERSION     NP_742018.2
DBSOURCE    REFSEQ: accession NM_172021.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Liebau,S., Proepper,C., Schmidt,T., Schoen,M., Bockmann,J. and
            Boeckers,T.M.
  TITLE     ProSAPiP2, a novel postsynaptic density protein that interacts with
            ProSAP2/Shank3
  JOURNAL   Biochem Biophys Res Commun 385 (3), 460-465 (2009)
   PUBMED   19481056
  REMARK    GeneRIF: a novel interaction partner of ProSAP2/Shank3, named
            ProSAP interacting protein 2 (ProSAPiP2) that does not show any
            close homology to other known proteins, was characterized
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC076503.1.
            
            On Jul 18, 2004 this sequence version replaced NP_742018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC076503.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..613
                     /product="TANK-binding kinase 1-binding protein 1"
                     /calculated_mol_wt=67024
     Region          1..280
                     /region_name="Homodimerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DG50.1)"
     Region          <50..333
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Region          281..330
                     /region_name="Interaction with TBK1 and IKBKE.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DG50.1)"
     Region          289..342
                     /region_name="TBD"
                     /note="TBD domain; pfam12845"
                     /db_xref="CDD:463729"
     Region          328..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A7MCY6; propagated from
                     UniProtKB/Swiss-Prot (Q6DG50.1)"
     CDS             1..613
                     /gene="Tbkbp1"
                     /gene_synonym="Prosapip2"
                     /coded_by="NM_172021.2:122..1963"
                     /db_xref="GeneID:266764"
                     /db_xref="RGD:631328"
ORIGIN      
        1 mesmfeddis iltqealgps evwldgpgdp slggdmcsas hfalitaygd ikerlggler
       61 enatlrrrlk vyeikyplit dfgeehgfpl yeikdgslle vekvslqqrl nqfqhelqkn
      121 keqeeqlgem iqayeklcve ksdletelge mralvethlr qicglekqlq qqqglrdaaf
      181 sslsppavpa tacpdldlhy lalrggpalg hagwpgptsv svselerrrl eealeaaqge
      241 argaqlreeq lqaecerlqg elkqlqetra qdlasnqsec gmawvkrvgd dqvnlalayt
      301 elteelgrlr elsslqgril rtllqeqarn agqrhsplsq rhspapacps pspparpppc
      361 apcqspaaqr rspvppcpsp qqrrspasps cpspvpqrrs pvppscqsps pqrrspvpps
      421 cpapqprppp ppgertlaer ayakppshha kagfqgrrsy selaegaaya aaspawlqae
      481 aatlpkpray ggelygpgrp lsprrafegi rlrfekqpse eeewampasp pspeastirc
      541 asfcagfpip espaatayah aehaqswpsi nllmetvgsd irscplcqlg fpvgypddal
      601 ikhidshlen ski
//
LOCUS       NP_113703                188 aa            linear   ROD 27-APR-2025
DEFINITION  GTPase KRas [Rattus norvegicus].
ACCESSION   NP_113703
VERSION     NP_113703.1
DBSOURCE    REFSEQ: accession NM_031515.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Hong,J.H., Ding,Y.Y., Li,J.M., Pan,X.C., Liu,Y. and Zhang,H.G.
  TITLE     Self-limiting bidirectional positive feedback between P53 and P21
            is involved in cardiac hypertrophy
  JOURNAL   Eur J Pharmacol 932, 175239 (2022)
   PUBMED   36044972
  REMARK    GeneRIF: Self-limiting bidirectional positive feedback between P53
            and P21 is involved in cardiac hypertrophy.
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Cao,Y., Huang,W., Wu,F., Shang,J., Ping,F., Wang,W., Li,Y., Zhao,X.
            and Zhang,X.
  TITLE     ZFP36 protects lungs from intestinal I/R-induced injury and
            fibrosis through the CREBBP/p53/p21/Bax pathway
  JOURNAL   Cell Death Dis 12 (7), 685 (2021)
   PUBMED   34238924
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Park,E.S., Kim,S., Huang,S., Yoo,J.Y., Korbelin,J., Lee,T.J.,
            Kaur,B., Dash,P.K., Chen,P.R. and Kim,E.
  TITLE     Selective Endothelial Hyperactivation of Oncogenic KRAS Induces
            Brain Arteriovenous Malformations in Mice
  JOURNAL   Ann Neurol 89 (5), 926-941 (2021)
   PUBMED   33675084
  REMARK    GeneRIF: Selective Endothelial Hyperactivation of Oncogenic KRAS
            Induces Brain Arteriovenous Malformations in Mice.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Feng,F., Wu,X., Shi,X., Gao,Q., Wu,Y., Yu,Y., Cheng,Q., Li,B.,
            Yi,B., Liu,C., Hao,Q., Zhang,L., Gao,C. and Jiang,X.
  TITLE     Comprehensive analysis of genomic alterations of Chinese hilar
            cholangiocarcinoma patients
  JOURNAL   Int J Clin Oncol 26 (4), 717-727 (2021)
   PUBMED   33387086
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Iida,K., Naiki,T., Naiki-Ito,A., Suzuki,S., Kato,H., Nozaki,S.,
            Nagai,T., Etani,T., Nagayasu,Y., Ando,R., Kawai,N., Yasui,T. and
            Takahashi,S.
  TITLE     Luteolin suppresses bladder cancer growth via regulation of
            mechanistic target of rapamycin pathway
  JOURNAL   Cancer Sci 111 (4), 1165-1179 (2020)
   PUBMED   31994822
  REMARK    GeneRIF: teolin, and in particular its metabolized product, may
            represent another natural product-derived therapeutic agent that
            acts against bladder cancer by upregulating p21 and inhibiting mTOR
            signaling
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Jansen,H., van Tol,A., Auwerx,J., Skretting,G. and Staels,B.
  TITLE     Opposite regulation of hepatic lipase and lecithin: cholesterol
            acyltransferase by glucocorticoids in rats
  JOURNAL   Biochim Biophys Acta 1128 (2-3), 181-185 (1992)
   PUBMED   1420288
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Palejwala,S. and Goldsmith,L.T.
  TITLE     Ovarian expression of cellular Ki-ras p21 varies with physiological
            status
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 4202-4206 (1992)
   PUBMED   1570348
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Chan,S.O., Wong,S.S. and Yeung,D.C.
  TITLE     Expression of c-Ki-ras in developing rat liver
  JOURNAL   Comp Biochem Physiol B 102 (1), 111-117 (1992)
   PUBMED   1526114
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Grimmond,S.M., Raghavan,D. and Russell,P.J.
  TITLE     Detection of a rare point mutation in Ki-ras of a human bladder
            cancer xenograft by polymerase chain reaction and direct sequencing
  JOURNAL   Urol Res 20 (2), 121-126 (1992)
   PUBMED   1553789
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Leibovitch,S.A., Leibovitch,M.P., Guillier,M., Hillion,J. and
            Harel,J.
  TITLE     Differential expression of protooncogenes related to transformation
            and cancer progression in rat myoblasts
  JOURNAL   Cancer Res 46 (8), 4097-4103 (1986)
   PUBMED   2425941
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U09793.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09793.1, BC126086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="Noble"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..188
                     /product="GTPase KRas"
                     /EC_number="3.6.5.2"
                     /note="c-K-ras2 protein; c-Kirsten-ras proto-oncogene;
                     ki-Ras; K-Ras 2; Kirsten rat sarcoma viral oncogene
                     homologue 2 (active); v-Ki-ras2 Kirsten rat sarcoma viral
                     oncogene homolog"
                     /calculated_mol_wt=21364
     Region          3..164
                     /region_name="H_N_K_Ras_like"
                     /note="Ras GTPase family containing H-Ras,N-Ras and
                     K-Ras4A/4B; cd04138"
                     /db_xref="CDD:133338"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133338"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133338"
     Site            order(12..18,28..30,32,35,60,116..117,119..120,145..146)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133338"
     Site            order(17..18,30..32,34,37,40..41,54..55,57,59..61,63..65,
                     67,69..71,73,102..103,147)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:133338"
     Site            order(25,37..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133338"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133338"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133338"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133338"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133338"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133338"
     Site            145..147
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133338"
     CDS             1..188
                     /gene="Kras"
                     /gene_synonym="c-Ki-ras; K-ras; Kras2; p21"
                     /coded_by="NM_031515.3:1..567"
                     /db_xref="GeneID:24525"
                     /db_xref="RGD:2981"
ORIGIN      
        1 mteyklvvvg aggvgksalt iqliqnhfvd eydptiedsy rkqvvidget clldildtag
       61 qeeysamrdq ymrtgegflc vfainntksf edihhyreqi krvkdsedvp mvlvgnkcdl
      121 psrtvdtkqa qelarsygip fietsaktrq gvddafytlv reirkhkekm skdgkkkkkk
      181 srtrcivm
//
LOCUS       NP_001020910             167 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL5 [Rattus norvegicus].
ACCESSION   NP_001020910 XP_342950
VERSION     NP_001020910.1
DBSOURCE    REFSEQ: accession NM_001025739.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Slomnicki,L.P., Hallgren,J., Vashishta,A., Smith,S.C., Ellis,S.R.
            and Hetman,M.
  TITLE     Proapoptotic Requirement of Ribosomal Protein L11 in Ribosomal
            Stress-Challenged Cortical Neurons
  JOURNAL   Mol Neurobiol 55 (1), 538-553 (2018)
   PUBMED   27975169
  REMARK    GeneRIF: knockdown of the RP L11, which in nonneuronal systems
            mediates p53 activation downstream of ribosomal stress, protected
            neurons against inhibition of ribosomal biogenesis.
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Morgado-Palacin,L., Varetti,G., Llanos,S., Gomez-Lopez,G.,
            Martinez,D. and Serrano,M.
  TITLE     Partial Loss of Rpl11 in Adult Mice Recapitulates Diamond-Blackfan
            Anemia and Promotes Lymphomagenesis
  JOURNAL   Cell Rep 13 (4), 712-722 (2015)
   PUBMED   26489471
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Smetanina,N.S., Mersiyanova,I.V., Kurnikova,M.A.,
            Ovsyannikova,G.S., Hachatryan,L.A., Bobrynina,V.O., Maschan,M.A.,
            Novichkova,G.A., Lipton,J.M. and Maschan,A.A.
  TITLE     Clinical and genomic heterogeneity of Diamond Blackfan anemia in
            the Russian Federation
  JOURNAL   Pediatr Blood Cancer 62 (9), 1597-1600 (2015)
   PUBMED   25946618
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Voorhees,R.M., Fernandez,I.S., Scheres,S.H. and Hegde,R.S.
  TITLE     Structure of the mammalian ribosome-Sec61 complex to 3.4 A
            resolution
  JOURNAL   Cell 157 (7), 1632-1643 (2014)
   PUBMED   24930395
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Peng,J., Kim,M.J., Cheng,D., Duong,D.M., Gygi,S.P. and Sheng,M.
  TITLE     Semiquantitative proteomic analysis of rat forebrain postsynaptic
            density fractions by mass spectrometry
  JOURNAL   J Biol Chem 279 (20), 21003-21011 (2004)
   PUBMED   15020595
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Chan,Y.L., Olvera,J., Paz,V. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L11
  JOURNAL   Biochem Biophys Res Commun 185 (1), 356-362 (1992)
   PUBMED   1599472
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Uchiumi,T., Kikuchi,M. and Ogata,K.
  TITLE     Cross-linking study on protein neighborhoods at the subunit
            interface of rat liver ribosomes with 2-iminothiolane
  JOURNAL   J Biol Chem 261 (21), 9663-9667 (1986)
   PUBMED   3733691
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Uchiumi,T., Kikuchi,M., Terao,K. and Ogata,K.
  TITLE     Neighboring proteins in rat liver 60 S ribosomal subunits
            disulfide-linked by hydrogen peroxide oxidation or cross-linked
            with dithiobis(succinimidyl propionate)
  JOURNAL   J Biol Chem 260 (9), 5669-5674 (1985)
   PUBMED   3988767
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097372.1.
            
            On Jul 22, 2005 this sequence version replaced XP_342950.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097372.1, CV108281.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..167
                     /product="large ribosomal subunit protein uL5"
                     /note="60S ribosomal protein L11"
                     /calculated_mol_wt=18893
     Region          1..164
                     /region_name="PTZ00156"
                     /note="60S ribosomal protein L11; Provisional"
                     /db_xref="CDD:185485"
     CDS             1..167
                     /gene="Rpl11"
                     /coded_by="NM_001025739.1:370..873"
                     /db_xref="GeneID:362631"
                     /db_xref="RGD:1308681"
ORIGIN      
        1 mrelrirklc lnicvgesgd rltraakvle qltgqtpvfs karytvrsfg irrnekiavh
       61 ctvrgakaee ilekglkvre yelrknnfsd tgnfgfgiqe hidlgikydp sigiygldfy
      121 vvlgrpgfsi adkkrrtgci gakhriskee amrwfqqkyd giilpgk
//
LOCUS       NP_671486                698 aa            linear   ROD 27-APR-2025
DEFINITION  protein artemis [Rattus norvegicus].
ACCESSION   NP_671486
VERSION     NP_671486.2
DBSOURCE    REFSEQ: accession NM_147145.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Volk,T., Pannicke,U., Reisli,I., Bulashevska,A., Ritter,J.,
            Bjorkman,A., Schaffer,A.A., Fliegauf,M., Sayar,E.H., Salzer,U.,
            Fisch,P., Pfeifer,D., Di Virgilio,M., Cao,H., Yang,F.,
            Zimmermann,K., Keles,S., Caliskaner,Z., Guner,S.U., Schindler,D.,
            Hammarstrom,L., Rizzi,M., Hummel,M., Pan-Hammarstrom,Q., Schwarz,K.
            and Grimbacher,B.
  TITLE     DCLRE1C (ARTEMIS) mutations causing phenotypes ranging from
            atypical severe combined immunodeficiency to mere antibody
            deficiency
  JOURNAL   Hum Mol Genet 24 (25), 7361-7372 (2015)
   PUBMED   26476407
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Craxton,A., Somers,J., Munnur,D., Jukes-Jones,R., Cain,K. and
            Malewicz,M.
  TITLE     XLS (c9orf142) is a new component of mammalian DNA double-stranded
            break repair
  JOURNAL   Cell Death Differ 22 (6), 890-897 (2015)
   PUBMED   25941166
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Lee,B.S., Gapud,E.J., Zhang,S., Dorsett,Y., Bredemeyer,A.,
            George,R., Callen,E., Daniel,J.A., Osipovich,O., Oltz,E.M.,
            Bassing,C.H., Nussenzweig,A., Lees-Miller,S., Hammel,M., Chen,B.P.
            and Sleckman,B.P.
  TITLE     Functional intersection of ATM and DNA-dependent protein kinase
            catalytic subunit in coding end joining during V(D)J recombination
  JOURNAL   Mol Cell Biol 33 (18), 3568-3579 (2013)
   PUBMED   23836881
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Rooney,S., Alt,F.W., Lombard,D., Whitlow,S., Eckersdorff,M.,
            Fleming,J., Fugmann,S., Ferguson,D.O., Schatz,D.G. and Sekiguchi,J.
  TITLE     Defective DNA repair and increased genomic instability in
            Artemis-deficient murine cells
  JOURNAL   J Exp Med 197 (5), 553-565 (2003)
   PUBMED   12615897
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Rooney,S., Sekiguchi,J., Zhu,C., Cheng,H.L., Manis,J., Whitlow,S.,
            DeVido,J., Foy,D., Chaudhuri,J., Lombard,D. and Alt,F.W.
  TITLE     Leaky Scid phenotype associated with defective V(D)J coding end
            processing in Artemis-deficient mice
  JOURNAL   Mol Cell 10 (6), 1379-1390 (2002)
   PUBMED   12504013
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Ma,Y., Pannicke,U., Schwarz,K. and Lieber,M.R.
  TITLE     Hairpin opening and overhang processing by an Artemis/DNA-dependent
            protein kinase complex in nonhomologous end joining and V(D)J
            recombination
  JOURNAL   Cell 108 (6), 781-794 (2002)
   PUBMED   11955432
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Moshous,D., Callebaut,I., de Chasseval,R., Corneo,B.,
            Cavazzana-Calvo,M., Le Deist,F., Tezcan,I., Sanal,O., Bertrand,Y.,
            Philippe,N., Fischer,A. and de Villartay,J.P.
  TITLE     Artemis, a novel DNA double-strand break repair/V(D)J recombination
            protein, is mutated in human severe combined immune deficiency
  JOURNAL   Cell 105 (2), 177-186 (2001)
   PUBMED   11336668
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083546.1.
            
            On Dec 7, 2007 this sequence version replaced NP_671486.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083546.1, AF395746.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..698
                     /product="protein artemis"
                     /note="SNM1-like protein; DNA cross-link repair 1C
                     protein"
                     /calculated_mol_wt=78058
     Region          1..171
                     /region_name="artemis-SNM1C-like_MBL-fold"
                     /note="artemis-SNM1C and related proteins; MBL-fold
                     metallo-hydrolase domain; cd16297"
                     /db_xref="CDD:293855"
     Site            order(33,35,37..38,115..116,136,166)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293855"
     Region          239..343
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K4J0; propagated from
                     UniProtKB/Swiss-Prot (Q5XIX3.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIX3.1)"
     Region          445..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX3.1)"
     Region          505..595
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX3.1)"
     Region          620..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIX3.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000250|UniProtKB:Q96SD1; propagated from
                     UniProtKB/Swiss-Prot (Q5XIX3.1)"
     CDS             1..698
                     /gene="Dclre1c"
                     /gene_synonym="Snm1l"
                     /coded_by="NM_147145.2:24..2120"
                     /db_xref="GeneID:259171"
                     /db_xref="RGD:708574"
ORIGIN      
        1 mssfqgqmee yptisidrfd renlkarayf lshchkdhmk glrapsmkrr lecslkvfly
       61 cspvtkelll tspkykfwen riiaieietp tqvslvdeas gekeevvvtl lpaghcpgsv
      121 mflfqgsngt vlytgdfrla kgevsrmell hsggrvkdiq svyldttfcd prfyqipsre
      181 eclrgvlelv rswitrspkh vvwlnckaay gyeylftnls eelgvqvhvd kldmfknmpd
      241 ilhhlttdrn tqihacrhpk aeeyfqwnkl pcgmasktkt vlhtisikps tmwfgertrk
      301 tnvivrtges syracfsfhs syseikdfls yicpvnaypn vipigltvdk vmdflkplcr
      361 ssqcaepkyk plgklkrart vhldseeddd lfddpllths rrkvpyqvtl hpevfsmkal
      421 pldqpelgqs pgcckaesmp spslanfvdc desnsdsege letppslqgg lgpttlpqqn
      481 adpdvdvprw evffkrkdei tdeclenlps sietggsqsp krfsdspklg sdsdgesthi
      541 ssqnssqsth itdqgsqgwd sqcdtvllss qeksggdsts lnkdtykpkp kdsisasqie
      601 qnalcpqdth cdlksgaevn gvpcieepdt vsgrksspek tsltstqads qsssdfeips
      661 tpeaelpkpe hlqflygkla tgesivlkke nvhsqifk
//
LOCUS       NP_598208                649 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor E2-alpha isoform a [Rattus norvegicus].
ACCESSION   NP_598208
VERSION     NP_598208.2
DBSOURCE    REFSEQ: accession NM_133524.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Guo,Q., Liu,Y., Sun,R., Yang,F., Qiao,P., Zhang,R., Song,L., E,L.
            and Liu,H.
  TITLE     Mechanical stimulation induced osteogenic differentiation of BMSCs
            through TWIST/E2A/p21 axis
  JOURNAL   Biosci Rep 40 (5) (2020)
   PUBMED   32309849
  REMARK    GeneRIF: Mechanical stimulation induced osteogenic differentiation
            of BMSCs through TWIST/E2A/p21 axis.
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Siu,M.K., Chen,W.Y., Tsai,H.Y., Chen,H.Y., Yin,J.J., Chen,C.L.,
            Tsai,Y.C. and Liu,Y.N.
  TITLE     TCF7 is suppressed by the androgen receptor via microRNA-1-mediated
            downregulation and is involved in the development of resistance to
            androgen deprivation in prostate cancer
  JOURNAL   Prostate Cancer Prostatic Dis 20 (2), 172-178 (2017)
   PUBMED   28220803
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Wang,Z., Kim,J., Teng,Y., Ding,H.F., Zhang,J., Hai,T., Cowell,J.K.
            and Yan,C.
  TITLE     Loss of ATF3 promotes hormone-induced prostate carcinogenesis and
            the emergence of CK5(+)CK8(+) epithelial cells
  JOURNAL   Oncogene 35 (27), 3555-3564 (2016)
   PUBMED   26522727
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Udayakumar,T.S., Stoyanova,R., Shareef,M.M., Mu,Z., Philip,S.,
            Burnstein,K.L. and Pollack,A.
  TITLE     Edelfosine Promotes Apoptosis in Androgen-Deprived Prostate Tumors
            by Increasing ATF3 and Inhibiting Androgen Receptor Activity
  JOURNAL   Mol Cancer Ther 15 (6), 1353-1363 (2016)
   PUBMED   26944919
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Zhu,G., Li,X., Guo,B., Ke,Q., Dong,M. and Li,F.
  TITLE     PAK5-mediated E47 phosphorylation promotes epithelial-mesenchymal
            transition and metastasis of colon cancer
  JOURNAL   Oncogene 35 (15), 1943-1954 (2016)
   PUBMED   26212009
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Metz,R. and Ziff,E.
  TITLE     The helix-loop-helix protein rE12 and the C/EBP-related factor
            rNFIL-6 bind to neighboring sites within the c-fos serum response
            element
  JOURNAL   Oncogene 6 (12), 2165-2178 (1991)
   PUBMED   1766666
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Nelson,C., Shen,L.P., Meister,A., Fodor,E. and Rutter,W.J.
  TITLE     Pan: a transcriptional regulator that binds chymotrypsin, insulin,
            and AP-4 enhancer motifs
  JOURNAL   Genes Dev 4 (6), 1035-1043 (1990)
   PUBMED   2200736
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
REFERENCE   10 (residues 1 to 649)
  AUTHORS   Murre,C., McCaw,P.S., Vaessin,H., Caudy,M., Jan,L.Y., Jan,Y.N.,
            Cabrera,C.V., Buskin,J.N., Hauschka,S.D., Lassar,A.B. et al.
  TITLE     Interactions between heterologous helix-loop-helix proteins
            generate complexes that bind specifically to a common DNA sequence
  JOURNAL   Cell 58 (3), 537-544 (1989)
   PUBMED   2503252
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X54549.1, BC078750.1 and BQ192196.1.
            
            On Oct 28, 2005 this sequence version replaced NP_598208.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ973227.1, X54549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132268
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..649
                     /product="transcription factor E2-alpha isoform a"
                     /note="transcription factor E2-alpha; TCF-3; transcription
                     regulator Pan; pancreas specific transcription factor 1c;
                     immunoglobulin enhancer-binding factor E12/E47;
                     transcription factor E2a; transcription factor E2a-like"
                     /calculated_mol_wt=67452
     Region          37..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Region          132..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15923; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15923; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Region          171..177
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Region          296..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Region          339..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15806; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15923; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Site            367
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P15806; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15923; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Region          385..420
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Region          435..547
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21677.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15923; propagated from
                     UniProtKB/Swiss-Prot (P21677.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P21677.1)"
     Region          538..622
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(546,550,552..554,556,561,582..583)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(559..560,563..564,566..567,570,574,584,587,591,594,
                     597..602)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..649
                     /gene="Tcf3"
                     /gene_synonym="Pan2; Tcfe2a"
                     /coded_by="NM_133524.2:74..2023"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:171046"
                     /db_xref="RGD:620914"
ORIGIN      
        1 mmnqsqrmap vgsdkelsdl ldfsmmfplp vangkgrpas lagtqfagsg ledrpssgsw
       61 gnseqnsssf dpsraysega hfsdshsslp pstflgaglg gkgsernaya tfgrdtsvgt
      121 lsqagflpge lglsspgpls psgvksssqy ytsfpsnprr raadggldtq pkkvrkvppg
      181 lpssvypsss gdnysrdata ypsaktpssa ypspfyvadg slhpsaelws ppgqvgfgpm
      241 lgdgsaplpl apgsssvssg afgglqqqdr mgyqlhgsev ngtlpavssf saapgtysgt
      301 sghtppvsga dsllgtrgtt asssgdalgk alasiyspdh ssnnfspsps tpvgspqglp
      361 gtsqwpraga psalspnyda glhglskmed rldeaihvlr shavgtasel hgllpghstl
      421 ttsfagpmsl ggrhaglvsg shpedgltsg asllhnhasl psqpsslpdl sqrppdsfsg
      481 lgragvtaga seikreeked eevtsvadae edkkdlkvpr trtspdeded dllppeqkae
      541 rekerrvann arerlrvrdi neafkelgrm cqlhlstekp qtkllilhqa vavilsleqq
      601 vrernlnpka aclkrreeek vsgvvgdpql alsaahpglg eahnpaghl
//
LOCUS       NP_001007648             165 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF181 [Rattus norvegicus].
ACCESSION   NP_001007648 XP_216174
VERSION     NP_001007648.1
DBSOURCE    REFSEQ: accession NM_001007647.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Pedersen,S.M., Chan,W., Jattani,R.P., Mackie,d.S. and
            Pomerantz,J.L.
  TITLE     Negative Regulation of CARD11 Signaling and Lymphoma Cell Survival
            by the E3 Ubiquitin Ligase RNF181
  JOURNAL   Mol Cell Biol 36 (5), 794-808 (2015)
   PUBMED   26711259
  REMARK    Erratum:[Mol Cell Biol. 2016 Mar 31;36(8):1322. doi:
            10.1128/MCB.00106-16. PMID: 27034408]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Lee,Y.I., Giovinazzo,D., Kang,H.C., Lee,Y., Jeong,J.S.,
            Doulias,P.T., Xie,Z., Hu,J., Ghasemi,M., Ischiropoulos,H., Qian,J.,
            Zhu,H., Blackshaw,S., Dawson,V.L. and Dawson,T.M.
  TITLE     Protein microarray characterization of the S-nitrosoproteome
  JOURNAL   Mol Cell Proteomics 13 (1), 63-72 (2014)
   PUBMED   24105792
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079313.1.
            
            On Nov 29, 2004 this sequence version replaced XP_216174.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..165
                     /product="E3 ubiquitin-protein ligase RNF181"
                     /EC_number="2.3.2.27"
                     /note="RING-type E3 ubiquitin transferase RNF181"
                     /calculated_mol_wt=19157
     Region          87..132
                     /region_name="RING-H2_RNF181"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 181 (RNF181) and similar proteins; cd16669"
                     /db_xref="CDD:438331"
     Region          136..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU4.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0P0; propagated from
                     UniProtKB/Swiss-Prot (Q6AXU4.1)"
     CDS             1..165
                     /gene="Rnf181"
                     /coded_by="NM_001007647.1:411..908"
                     /db_xref="GeneID:297337"
                     /db_xref="RGD:1359698"
ORIGIN      
        1 masyfdehdc eplnperear nnmllelarr vrgawswapg srslfnrmdf edlglvdweh
       61 hlpppaakav veslprtvir sskaelkcpv cllefeeeet viempchhlf hsncilpwls
      121 ktnscplcrh elptdddsye ehkkdkarrq qqqhrlenlh gamyt
//
LOCUS       NP_001019931             301 aa            linear   ROD 27-APR-2025
DEFINITION  intraflagellar transport protein 46 homolog [Rattus norvegicus].
ACCESSION   NP_001019931 XP_217120
VERSION     NP_001019931.1
DBSOURCE    REFSEQ: accession NM_001024760.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Liew,G.M., Ye,F., Nager,A.R., Murphy,J.P., Lee,J.S., Aguiar,M.,
            Breslow,D.K., Gygi,S.P. and Nachury,M.V.
  TITLE     The intraflagellar transport protein IFT27 promotes BBSome exit
            from cilia through the GTPase ARL6/BBS3
  JOURNAL   Dev Cell 31 (3), 265-278 (2014)
   PUBMED   25443296
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Ishikawa,H., Ide,T., Yagi,T., Jiang,X., Hirono,M., Sasaki,H.,
            Yanagisawa,H., Wemmer,K.A., Stainier,D.Y., Qin,H., Kamiya,R. and
            Marshall,W.F.
  TITLE     TTC26/DYF13 is an intraflagellar transport protein required for
            transport of motility-related proteins into flagella
  JOURNAL   Elife 3, e01566 (2014)
   PUBMED   24596149
  REMARK    Erratum:[Elife. 2014 Apr 01;3:e02897. doi: 10.7554/eLife.02897.
            PMID: 24692455]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Lai,C.K., Gupta,N., Wen,X., Rangell,L., Chih,B., Peterson,A.S.,
            Bazan,J.F., Li,L. and Scales,S.J.
  TITLE     Functional characterization of putative cilia genes by high-content
            analysis
  JOURNAL   Mol Biol Cell 22 (7), 1104-1119 (2011)
   PUBMED   21289087
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Follit,J.A., Xu,F., Keady,B.T. and Pazour,G.J.
  TITLE     Characterization of mouse IFT complex B
  JOURNAL   Cell Motil Cytoskeleton 66 (8), 457-468 (2009)
   PUBMED   19253336
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Gouttenoire,J., Valcourt,U., Bougault,C., Aubert-Foucher,E.,
            Arnaud,E., Giraud,L. and Mallein-Gerin,F.
  TITLE     Knockdown of the intraflagellar transport protein IFT46 stimulates
            selective gene expression in mouse chondrocytes and affects early
            development in zebrafish
  JOURNAL   J Biol Chem 282 (42), 30960-30973 (2007)
   PUBMED   17720815
  REMARK    GeneRIF: Characterization of a similar gene in mouse and zebrafish.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Hou,Y., Qin,H., Follit,J.A., Pazour,G.J., Rosenbaum,J.L. and
            Witman,G.B.
  TITLE     Functional analysis of an individual IFT protein: IFT46 is required
            for transport of outer dynein arms into flagella
  JOURNAL   J Cell Biol 176 (5), 653-665 (2007)
   PUBMED   17312020
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097954.1.
            
            On Jun 13, 2005 this sequence version replaced XP_217120.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097954.1, BC079388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..301
                     /product="intraflagellar transport protein 46 homolog"
                     /note="intraflagellar transport protein IFT46;
                     intraflagellar transport 46 homolog"
                     /calculated_mol_wt=33901
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXQ9.2)"
     Region          62..264
                     /region_name="IFT46_B_C"
                     /note="Intraflagellar transport complex B protein 46 C
                     terminal; pfam12317"
                     /db_xref="CDD:463532"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9DB07; propagated from
                     UniProtKB/Swiss-Prot (Q6AXQ9.2)"
     CDS             1..301
                     /gene="Ift46"
                     /gene_synonym="RGD1307682"
                     /coded_by="NM_001024760.1:347..1252"
                     /db_xref="GeneID:300675"
                     /db_xref="RGD:1307682"
ORIGIN      
        1 madnssdeye ednkekkkps qltpqqgfse ndddddddss etdsdddddd eehgaplega
       61 ydpadyehlp vsaeikelfe yisrytpqli dldhklkpfi pdfipavgdi daflkvprpd
      121 gkpdhlgllv ldepstkqsd ptvlslwlte nskqhnitqh mkvksledae knpkaidtwi
      181 esiselhrsk ppatvhytrp mpdidtlmqe wspefeellg kvslptveid cslaeyidmi
      241 caildipfyk sriqslhllf slysefknsq hfkalaegkk tftppsnsas qagdaetlsf
      301 l
//
LOCUS       NP_001012104             441 aa            linear   ROD 27-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48
            kDa subunit precursor [Rattus norvegicus].
ACCESSION   NP_001012104 XP_233581
VERSION     NP_001012104.1
DBSOURCE    REFSEQ: accession NM_001012104.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Poulsen,M.W., Andersen,J.M., Hedegaard,R.V., Madsen,A.N.,
            Krath,B.N., Monosik,R., Bak,M.J., Nielsen,J., Holst,B.,
            Skibsted,L.H., Larsen,L.H. and Dragsted,L.O.
  TITLE     Short-term effects of dietary advanced glycation end products in
            rats
  JOURNAL   Br J Nutr 115 (4), 629-636 (2016)
   PUBMED   26824730
  REMARK    GeneRIF: Data suggest expression of Rage (advanced glycosylation
            end product-specific receptor) and Ager1/Ddost can be altered by
            dietary factors; diet high in AGE (advanced glycation end products)
            up-regulates expression of Rage and Ager1/Ddost after 2 weeks.
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Roboti,P. and High,S.
  TITLE     The oligosaccharyltransferase subunits OST48, DAD1 and KCP2
            function as ubiquitous and selective modulators of mammalian
            N-glycosylation
  JOURNAL   J Cell Sci 125 (Pt 14), 3474-3484 (2012)
   PUBMED   22467853
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kumar,V., Heinemann,F.S. and Ozols,J.
  TITLE     Interleukin-2 induces N-glycosylation in T-cells: characterization
            of human lymphocyte oligosaccharyltransferase
  JOURNAL   Biochem Biophys Res Commun 247 (2), 524-529 (1998)
   PUBMED   9642163
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Yamagata,T., Tsuru,T., Momoi,M.Y., Suwa,K., Nozaki,Y., Mukasa,T.,
            Ohashi,H., Fukushima,Y. and Momoi,T.
  TITLE     Genome organization of human 48-kDa oligosaccharyltransferase
            (DDOST)
  JOURNAL   Genomics 45 (3), 535-540 (1997)
   PUBMED   9367678
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082075.1.
            
            On Feb 11, 2005 this sequence version replaced XP_233581.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082075.1, FQ228905.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..441
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase 48 kDa subunit precursor"
                     /EC_number="2.4.99.18"
                     /note="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase 48 kDa subunit;
                     dolichyl-di-phosphooligosaccharide-protein
                     glycotransferase; DDOST 48 kDa subunit; oligosaccharyl
                     transferase 48 kDa subunit;
                     dolichyl-diphosphooligosaccharide-protein
                     glycosyltransferase;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit (non-catalytic)"
                     /calculated_mol_wt=45970
     sig_peptide     1..28
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q641Y0.1)"
                     /calculated_mol_wt=2944
     mat_peptide     29..441
                     /product="Dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase 48 kDa subunit. /id=PRO_0000357447"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y0.1)"
                     /calculated_mol_wt=45970
     Region          31..435
                     /region_name="DDOST_48kD"
                     /note="Oligosaccharyltransferase 48 kDa subunit beta;
                     pfam03345"
                     /db_xref="CDD:460890"
     Site            413..432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y0.1)"
     CDS             1..441
                     /gene="Ddost"
                     /coded_by="NM_001012104.1:2..1327"
                     /db_xref="GeneID:313648"
                     /db_xref="RGD:1308970"
ORIGIN      
        1 mkmvprlavr awplcgllla algcvcasgp rtlvlldnln vrdthslffr slkdrgfelt
       61 fktaddpsls likygeflyd nliifspsve dfggninvet isafidgggs vlvaassdig
      121 dplrelgsec giefdeekta vidhhnydvs dlgqhtliva dtenllkapt ivgksslnpi
      181 lfrgvgmvad pdnplvldil tgsstsysff pdkpitqyph avgrntllia glqarnnarv
      241 ifsgsldffs daffnsavqk aapgaqrysq tgnyelaval srwvfkeegv lrvgpvshhr
      301 vgetappnay tvtdlveysi vieqlsngkw vpfdgddiql efvridpfvr tflkrkggky
      361 svqfklpdvy gvfqfkvdyn rlgythlyss tqvsvrplqh tqyerfipsa ypyyasafsm
      421 maglflfsvv flhmkekeks d
//
LOCUS       NP_001019431             502 aa            linear   ROD 27-APR-2025
DEFINITION  nostrin [Rattus norvegicus].
ACCESSION   NP_001019431 XP_229998
VERSION     NP_001019431.1
DBSOURCE    REFSEQ: accession NM_001024260.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Kim,H.W., Choi,Y.J., Kim,J.A., Bae,S.H., Kim,K.R. and Park,S.S.
  TITLE     Mouse disabled 2 interacting protein 2 functions as a
            transcriptional repressor through direct binding onto its own
            promoter
  JOURNAL   Biochem Biophys Res Commun 337 (1), 75-81 (2005)
   PUBMED   16171775
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Kirsch,T., Wellner,M., Luft,F.C., Haller,H. and Lippoldt,A.
  TITLE     Altered gene expression in cerebral capillaries of stroke-prone
            spontaneously hypertensive rats
  JOURNAL   Brain Res 910 (1-2), 106-115 (2001)
   PUBMED   11489260
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088446.1.
            
            On May 27, 2005 this sequence version replaced XP_229998.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088446.1, FQ226667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..502
                     /product="nostrin"
                     /note="BM247; eNOS-trafficking inducer; nitric oxide
                     synthase trafficker"
                     /calculated_mol_wt=57221
     Region          8..250
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(13,16..17,21,23..24,27..28,30..31,41..42,44..45,
                     48..49,51..52,55,81,84..85,209,212..213,215,217,220..221,
                     223..224,227..228,231..232,234..235,238..239,241..242)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153271"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5I0D6.1)"
     Region          413..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0D6.1)"
     Region          443..494
                     /region_name="SH3_Nostrin"
                     /note="Src homology 3 domain of Nitric Oxide Synthase
                     TRaffic INducer; cd11823"
                     /db_xref="CDD:212757"
     Site            order(447,449,452,456,474..475,488,490..491)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212757"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ7; propagated from
                     UniProtKB/Swiss-Prot (Q5I0D6.1)"
     CDS             1..502
                     /gene="Nostrin"
                     /coded_by="NM_001024260.1:49..1557"
                     /db_xref="GeneID:311111"
                     /db_xref="RGD:727920"
ORIGIN      
        1 mrdpltdcsy nkvykslkef aqngdnfckq itsvlqqran leisyakglq klavklskal
       61 qstkknclst awawasesmk saadlhqklg kaieleaikp thqvlsmqek krksldneve
      121 ksanlvinnw nqqikakkkl mmstkkheal fhliesskqs mtqkekqkll nklkkstekl
      181 ekedesyyqk nmagystrlk westlekcyk smlelekeri qllcnnlnqy sqhislfgqt
      241 lttchtqihc aiskvdvekd iqalmeetav lslenksell ladyfeedpk npmdkerrks
      301 likpklwrlq kdiekasrdk egleqklkal assasfsdak sqkdaetlmd enslkldllq
      361 ansyklstvl adleqrpkpc hpcsncifkw kekehshsyv kisrplltkr lekaeskapa
      421 geqnnpsssr pgssvsqgnn qlckalytfq arqddelnle kgdivtihek keegwwfgsl
      481 ngkkghfpaa yveelppkag qa
//
LOCUS       NP_596917                433 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNG3 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_596917
VERSION     NP_596917.2
DBSOURCE    REFSEQ: accession NM_133426.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Mederos Y Schnitzler,M., Rinne,S., Skrobek,L., Renigunta,V.,
            Schlichthorl,G., Derst,C., Gudermann,T., Daut,J. and
            Preisig-Muller,R.
  TITLE     Mutation of histidine 105 in the T1 domain of the potassium channel
            Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4
  JOURNAL   J Biol Chem 284 (7), 4695-4704 (2009)
   PUBMED   19074135
  REMARK    GeneRIF: Mutation of histidine 105 in the T1 domain of the
            potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and
            Kv6.4.
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Vega-Saenz de Miera,E.C.
  TITLE     Modification of Kv2.1 K+ currents by the silent Kv10 subunits
  JOURNAL   Brain Res Mol Brain Res 123 (1-2), 91-103 (2004)
   PUBMED   15046870
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Ottschytsch,N., Raes,A., Van Hoorick,D. and Snyders,D.J.
  TITLE     Obligatory heterotetramerization of three previously
            uncharacterized Kv channel alpha-subunits identified in the human
            genome
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7986-7991 (2002)
   PUBMED   12060745
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Sano,Y., Mochizuki,S., Miyake,A., Kitada,C., Inamura,K., Yokoi,H.,
            Nozawa,K., Matsushime,H. and Furuichi,K.
  TITLE     Molecular cloning and characterization of Kv6.3, a novel modulatory
            subunit for voltage-gated K(+) channel Kv2.1
  JOURNAL   FEBS Lett 512 (1-3), 230-234 (2002)
   PUBMED   11852086
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF454550.1.
            
            On Oct 4, 2005 this sequence version replaced NP_596917.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF454550.1, AB070605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..433
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNG3 isoform 1"
                     /note="potassium voltage-gated channel, subfamily G,
                     memeber 3; potassium voltage-gated channel, subfamily G,
                     member 3; voltage-gated potassium channel subunit Kv6.3;
                     voltage-gated potassium channel subunit Kv10.1; potassium
                     channel, voltage gated modifier subfamily G, member 3;
                     voltage-gated potassium channel 6.3; voltage-gated
                     potassium channel regulatory subunit KCNG3"
                     /calculated_mol_wt=49160
     Region          11..122
                     /region_name="BTB_POZ_KCNG3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily G member 3 (KCNG3);
                     cd18422"
                     /db_xref="CDD:349729"
     Site            order(14,16..23,26,62,64..65,68,71,75,78,82,84,92..93,96)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349729"
     Site            166..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Region          210..417
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            218..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Site            318..339
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Region          370..375
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     Site            385..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R523.2)"
     CDS             1..433
                     /gene="Kcng3"
                     /gene_synonym="Kv10.1; Kv6.3"
                     /coded_by="NM_133426.2:43..1344"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171011"
                     /db_xref="RGD:628832"
ORIGIN      
        1 mtfgrggaas vvlnvggary slsrellkdf plrrvsrlhg crserdvlev cddydrerne
       61 yffdrhseaf gfillyvrgh gklrfaprmc elsfynemiy wglegahley ccqrrlddrm
      121 sdthtfhaae elgreqprpt gpeaapsrrw lermrrtfee ptsslaaqil asvsvvfviv
      181 smvvlcastl pdwraaaadn rslddrsrys aspgrepsgi ieaicigwft aecivrfivs
      241 knkcefvkrp lniidllait pyyisvlmtv ftgensqlqr agvtlrvlrm mrifwvikla
      301 rhfiglqtlg ltlkrcyrem vmllvficva maifsalsql lehgldlets nkdfasipaa
      361 cwwviismtt vgygdmypit vpgrilggvc vvsgivllal pitfiyhsfv qcyhelkfrs
      421 arysrslsae fln
//
LOCUS       NP_001004075             381 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF34 [Rattus norvegicus].
ACCESSION   NP_001004075 XP_341083
VERSION     NP_001004075.1
DBSOURCE    REFSEQ: accession NM_001004075.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Yamaoka,S., Oshima,Y., Horiuchi,H., Morino,T., Hino,M., Miura,H.
            and Ogata,T.
  TITLE     Altered Gene Expression of RNF34 and PACAP Possibly Involved in
            Mechanism of Exercise-Induced Analgesia for Neuropathic Pain in
            Rats
  JOURNAL   Int J Mol Sci 18 (9), 1962 (2017)
   PUBMED   28902127
  REMARK    GeneRIF: Results suggest that exercise therapy possibly involves
            pain relief in SNL rats by suppressing Rnf34 and Pacap expression
            in the spinal cord.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Jin,H., Chiou,T.T., Serwanski,D.R., Miralles,C.P., Pinal,N. and De
            Blas,A.L.
  TITLE     Ring finger protein 34 (RNF34) interacts with and promotes
            gamma-aminobutyric acid type-A receptor degradation via
            ubiquitination of the gamma2 subunit
  JOURNAL   J Biol Chem 289 (42), 29420-29436 (2014)
   PUBMED   25193658
  REMARK    GeneRIF: RNF34 regulates postsynaptic gamma2-GABAAR clustering and
            GABAergic synaptic innervation by interacting with and
            ubiquitinating the gamma2-GABAAR subunit promoting GABAAR
            degradation
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Zhang,R., Zhao,J., Song,Y., Wang,X., Wang,L., Xu,J., Song,C. and
            Liu,F.
  TITLE     The E3 ligase RNF34 is a novel negative regulator of the NOD1
            pathway
  JOURNAL   Cell Physiol Biochem 33 (6), 1954-1962 (2014)
   PUBMED   25012219
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Wei,P., Pan,D., Mao,C. and Wang,Y.X.
  TITLE     RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and
            modulates brown fat cell metabolism
  JOURNAL   Mol Cell Biol 32 (2), 266-275 (2012)
   PUBMED   22064484
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Yang,W., Dicker,D.T., Chen,J. and El-Deiry,W.S.
  TITLE     CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
            MDM2
  JOURNAL   Cell Cycle 7 (5), 670-682 (2008)
   PUBMED   18382127
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Yang,W., Rozan,L.M., McDonald,E.R. 3rd, Navaraj,A., Liu,J.J.,
            Matthew,E.M., Wang,W., Dicker,D.T. and El-Deiry,W.S.
  TITLE     CARPs are ubiquitin ligases that promote MDM2-independent p53 and
            phospho-p53ser20 degradation
  JOURNAL   J Biol Chem 282 (5), 3273-3281 (2007)
   PUBMED   17121812
REFERENCE   7  (residues 1 to 381)
  AUTHORS   McDonald,E.R. 3rd and El-Deiry,W.S.
  TITLE     Suppression of caspase-8- and -10-associated RING proteins results
            in sensitization to death ligands and inhibition of tumor cell
            growth
  JOURNAL   Proc Natl Acad Sci U S A 101 (16), 6170-6175 (2004)
   PUBMED   15069192
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Araki,K., Kawamura,M., Suzuki,T., Matsuda,N., Kanbe,D., Ishii,K.,
            Ichikawa,T., Kumanishi,T., Chiba,T., Tanaka,K. and Nawa,H.
  TITLE     A palmitoylated RING finger ubiquitin ligase and its homologue in
            the brain membranes
  JOURNAL   J Neurochem 86 (3), 749-762 (2003)
   PUBMED   12859687
  REMARK    GeneRIF: identified two novel Ub ligases, Momo and Sakura, carrying
            double zinc finger motif and RING finger domain; momo expression is
            enriched in the brain gray matter and testis
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079044.1.
            
            On Sep 3, 2004 this sequence version replaced XP_341083.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079044.1, SRR8487231.120655.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..381
                     /product="E3 ubiquitin-protein ligase RNF34"
                     /EC_number="2.3.2.27"
                     /note="RING finger protein MOMO; ring finger protein 34,
                     E3 ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase RNF34"
                     /calculated_mol_wt=42550
     Region          59..105
                     /region_name="FYVE_CARP1"
                     /note="FYVE-like domain found in caspase regulator CARP1
                     and similar proteins; cd15769"
                     /db_xref="CDD:277308"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Region          216..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            241..242
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969K3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99KR6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH3.1)"
     Region          328..381
                     /region_name="RING-HC_CARP1"
                     /note="RING finger, HC subclass, found in caspases-8 and
                     -10-associated RING finger protein 1 (CARP1) and similar
                     proteins; cd16706"
                     /db_xref="CDD:438366"
     CDS             1..381
                     /gene="Rnf34"
                     /gene_synonym="Momo"
                     /coded_by="NM_001004075.1:96..1241"
                     /db_xref="GeneID:282845"
                     /db_xref="RGD:628636"
ORIGIN      
        1 mkagatsmwa sccgllnevm gtgavrgqqa gfpgstgpfr ftpssdfpty ppaategpni
       61 vckacglsfs vfrkkhvccd ckkdfcslcs vsqenlrrcs tchllqetaf qrpqlmrlkv
      121 kdlrqylllr nvptdtcrek edlvdlvlch rglgsgdgld srslsssrsq tssfftqsyf
      181 snytppsatv ssfqgelmdr egtfrsevlt qvqselasan tddedgeedd dddddddded
      241 ddeqeenlee qnpglskkka raslsdlssl eevegmsvrq lkeilarnfv nysgccekwe
      301 lvekvnrlyk eneenqksyg ermqlqdeed dslcricmda vidcvllecg hmvtctkcgk
      361 rmsecpicrq yvvravhvfk s
//
LOCUS       NP_001093940            1468 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear pore complex protein Nup153 [Rattus norvegicus].
ACCESSION   NP_001093940 XP_001056084 XP_341509
VERSION     NP_001093940.1
DBSOURCE    REFSEQ: accession NM_001100470.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1468)
  AUTHORS   Vollmer,B., Lorenz,M., Moreno-Andres,D., Bodenhofer,M., De
            Magistris,P., Astrinidis,S.A., Schooley,A., Flotenmeyer,M.,
            Leptihn,S. and Antonin,W.
  TITLE     Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear
            Membrane for Interphasic Nuclear Pore Complex Assembly
  JOURNAL   Dev Cell 33 (6), 717-728 (2015)
   PUBMED   26051542
REFERENCE   2  (residues 1 to 1468)
  AUTHORS   Bonnet,A. and Palancade,B.
  TITLE     Regulation of mRNA trafficking by nuclear pore complexes
  JOURNAL   Genes (Basel) 5 (3), 767-791 (2014)
   PUBMED   25184662
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1468)
  AUTHORS   Milles,S., Huy Bui,K., Koehler,C., Eltsov,M., Beck,M. and
            Lemke,E.A.
  TITLE     Facilitated aggregation of FG nucleoporins under molecular crowding
            conditions
  JOURNAL   EMBO Rep 14 (2), 178-183 (2013)
   PUBMED   23238392
REFERENCE   4  (residues 1 to 1468)
  AUTHORS   Rajanala,K. and Nandicoori,V.K.
  TITLE     Localization of nucleoporin Tpr to the nuclear pore complex is
            essential for Tpr mediated regulation of the export of unspliced
            RNA
  JOURNAL   PLoS One 7 (1), e29921 (2012)
   PUBMED   22253824
REFERENCE   5  (residues 1 to 1468)
  AUTHORS   Krull,S., Dorries,J., Boysen,B., Reidenbach,S., Magnius,L.,
            Norder,H., Thyberg,J. and Cordes,V.C.
  TITLE     Protein Tpr is required for establishing nuclear pore-associated
            zones of heterochromatin exclusion
  JOURNAL   EMBO J 29 (10), 1659-1673 (2010)
   PUBMED   20407419
REFERENCE   6  (residues 1 to 1468)
  AUTHORS   Bodoor,K., Shaikh,S., Salina,D., Raharjo,W.H., Bastos,R., Lohka,M.
            and Burke,B.
  TITLE     Sequential recruitment of NPC proteins to the nuclear periphery at
            the end of mitosis
  JOURNAL   J Cell Sci 112 (Pt 13), 2253-2264 (1999)
   PUBMED   10362555
REFERENCE   7  (residues 1 to 1468)
  AUTHORS   Shah,S., Tugendreich,S. and Forbes,D.
  TITLE     Major binding sites for the nuclear import receptor are the
            internal nucleoporin Nup153 and the adjacent nuclear filament
            protein Tpr
  JOURNAL   J Cell Biol 141 (1), 31-49 (1998)
   PUBMED   9531546
REFERENCE   8  (residues 1 to 1468)
  AUTHORS   Ewald,A., Kossner,U., Scheer,U. and Dabauvalle,M.C.
  TITLE     A biochemical and immunological comparison of nuclear and
            cytoplasmic pore complexes
  JOURNAL   J Cell Sci 109 (Pt 7), 1813-1824 (1996)
   PUBMED   8832404
REFERENCE   9  (residues 1 to 1468)
  AUTHORS   Radu,A., Blobel,G. and Moore,M.S.
  TITLE     Identification of a protein complex that is required for nuclear
            protein import and mediates docking of import substrate to distinct
            nucleoporins
  JOURNAL   Proc Natl Acad Sci U S A 92 (5), 1769-1773 (1995)
   PUBMED   7878057
REFERENCE   10 (residues 1 to 1468)
  AUTHORS   Sukegawa,J. and Blobel,G.
  TITLE     A nuclear pore complex protein that contains zinc finger motifs,
            binds DNA, and faces the nucleoplasm
  JOURNAL   Cell 72 (1), 29-38 (1993)
   PUBMED   8422679
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L06821.1, CV117688.1, CO574678.1 and AA818240.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_001056084.1, XP_341509.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L06821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1468
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..1468
                     /product="nuclear pore complex protein Nup153"
                     /note="nucleoporin Nup153; 153 kDa nucleoporin;
                     nucleoporin 153kD"
                     /calculated_mol_wt=152703
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          78..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          114..621
                     /region_name="Nup153"
                     /note="Nucleoporin Nup153-like; pfam08604"
                     /db_xref="CDD:462533"
     Region          172..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          237..1411
                     /region_name="29 X 2 AA repeats of F-G.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            385
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          387..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            534
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            544
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          661..687
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          662..681
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          693..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            717
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          722..750
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          725..744
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          789..818
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          793..812
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Region          846..875
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          850..869
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            902
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            947
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Region          960..985
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            1106
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Region          1121..1145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Region          1190..1209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Region          1231..1260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Region          1308..1380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Region          1378..1468
                     /region_name="Nup_retrotrp_bd"
                     /note="Retro-transposon transporting motif; pfam10599"
                     /db_xref="CDD:371156"
     Region          1414..1468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49791.1)"
     Site            1450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            1454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49790; propagated from
                     UniProtKB/Swiss-Prot (P49791.1)"
     CDS             1..1468
                     /gene="Nup153"
                     /gene_synonym="NUCZINK"
                     /coded_by="NM_001100470.1:535..4941"
                     /db_xref="GeneID:25281"
                     /db_xref="RGD:3216"
ORIGIN      
        1 masgaggigg gggggkirtr rchqgpvkpy qqgrpqhqgi lsrvtesvkn ivpgwlqryf
       61 nksenacscs vnadevprwp enredereiy vdentntddg rttpeptgsn teepsttsta
      121 snypdvltrp slhrshlnfs vlespalhcq pstssafpig ssgfslvkei kdstsqhddd
      181 nisttsgfss rasekdiavs kntslpplws peaershsls qhtaisskkp afnlsafgtl
      241 stslgnssil ktsqlgdspf ypgkttygga aaavrqnkvr stpyqapvrr qmkakqlnaq
      301 sygvtsstar rilqslekms spladakrip savssplnsp ldrsgidstv fqakkekvds
      361 qyppvqrlmt pkpvsiatnr tvyfkpsltp sgdlrktnqr idkknstvde knisrqnreq
      421 esgfsypnfs ipaanglssg vgggggkmrr ertthfvask pseeeevevp llpqislpis
      481 ssslptfnfs spaisaasss svspsqplsn kvqmtslgst gnpvftfssp ivkstqadvl
      541 ppasigftfs vplaktelsg pnsssetvls ssvtaqdntv vnsssskkrs apcedpftpa
      601 kilregsvld ilktpgfmsp kvdspalqpt ttssivytrp aistfsssgv efgeslkags
      661 swqcdtcllq nkvtdnkcia cqaaklplke takqtgigtp sksdkpasts gtgfgdkfkp
      721 aigtwdcdtc lvqnkpeavk cvacetpkpg tgvkralplt vasespvtas ssttvttgtl
      781 gfgdkfkrpv gswecpvccv snkaedsrcv sctsekpglv sasssnpvpv slpsggclgl
      841 dkfkkpegsw dcevclvqnk adstkciace sakpgtksef kgfgtsssln papsafkfgi
      901 pssssglsqt ftstgnfkfg dqggfklgts sdsgstntmn tnfkfpkptg dfkfgvlpds
      961 kpeeikndsk ndnfqfgpss glsnpassap fqfgvstlgq qekkeelpqs ssagfsfgag
     1021 vanpssaaid ttvtsenksg fnfgtidtks vsvtpftykt teakkedasa tkggftfgkv
     1081 dsaalsspsm fvlgrteekq qepvtstslv fgkkadneep kcqpvfsfgn seqtkdesss
     1141 kptfsfsvak psvkesdqla katfafgnqt ntttdqgaak pafsflnsss sssstpatss
     1201 sasifgssts sssppvaafv fgqasnpvss safgnsaess tsqpllfpqd gkpattssta
     1261 saappfvfgt gassnstvss gftfgattts sssgsffvfg tghsapsasp afganqtptf
     1321 gqsqgasqpn ppsfgsisss talfsagsqp vppptfgtvs sssqppvfgq qpsqsafgsg
     1381 tanassvfqf gssttnfnft nnnpsgvftf gaspstpaaa aqpsgsggfs fsqspasftv
     1441 gsngknmfss sgtsvsgrki ktavrrkk
//
LOCUS       NP_001019939             395 aa            linear   ROD 27-APR-2025
DEFINITION  ETS-related transcription factor Elf-3 [Rattus norvegicus].
ACCESSION   NP_001019939 XP_222659
VERSION     NP_001019939.1
DBSOURCE    REFSEQ: accession NM_001024768.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Wang,J., Shen,X., Liu,J., Chen,W., Wu,F., Wu,W., Meng,Z., Zhu,M.
            and Miao,C.
  TITLE     High glucose mediates NLRP3 inflammasome activation via
            upregulation of ELF3 expression
  JOURNAL   Cell Death Dis 11 (5), 383 (2020)
   PUBMED   32439949
  REMARK    GeneRIF: High glucose mediates NLRP3 inflammasome activation via
            upregulation of ELF3 expression.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Kageyama,S., Liu,H., Nagata,M. and Aoki,F.
  TITLE     The role of ETS transcription factors in transcription and
            development of mouse preimplantation embryos
  JOURNAL   Biochem Biophys Res Commun 344 (2), 675-679 (2006)
   PUBMED   16630543
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Brown,C., Gaspar,J., Pettit,A., Lee,R., Gu,X., Wang,H., Manning,C.,
            Voland,C., Goldring,S.R., Goldring,M.B., Libermann,T.A.,
            Gravallese,E.M. and Oettgen,P.
  TITLE     ESE-1 is a novel transcriptional mediator of angiopoietin-1
            expression in the setting of inflammation
  JOURNAL   J Biol Chem 279 (13), 12794-12803 (2004)
   PUBMED   14715662
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Cabral,A., Fischer,D.F., Vermeij,W.P. and Backendorf,C.
  TITLE     Distinct functional interactions of human Skn-1 isoforms with Ese-1
            during keratinocyte terminal differentiation
  JOURNAL   J Biol Chem 278 (20), 17792-17799 (2003)
   PUBMED   12624109
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Kim,J.H., Wilder,P.J., Hou,J., Nowling,T. and Rizzino,A.
  TITLE     Activation of the murine type II transforming growth factor-beta
            receptor gene: up-regulation and function of the transcription
            factor Elf-3/Ert/Esx/Ese-1
  JOURNAL   J Biol Chem 277 (20), 17520-17530 (2002)
   PUBMED   11893733
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Ng,A.Y., Waring,P., Ristevski,S., Wang,C., Wilson,T., Pritchard,M.,
            Hertzog,P. and Kola,I.
  TITLE     Inactivation of the transcription factor Elf3 in mice results in
            dysmorphogenesis and altered differentiation of intestinal
            epithelium
  JOURNAL   Gastroenterology 122 (5), 1455-1466 (2002)
   PUBMED   11984530
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Brembeck,F.H., Opitz,O.G., Libermann,T.A. and Rustgi,A.K.
  TITLE     Dual function of the epithelial specific ets transcription factor,
            ELF3, in modulating differentiation
  JOURNAL   Oncogene 19 (15), 1941-1949 (2000)
   PUBMED   10773884
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Neve,R., Chang,C.H., Scott,G.K., Wong,A., Friis,R.R., Hynes,N.E.
            and Benz,C.C.
  TITLE     The epithelium-specific ets transcription factor ESX is associated
            with mammary gland development and involution
  JOURNAL   FASEB J 12 (14), 1541-1550 (1998)
   PUBMED   9806763
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Oettgen,P., Alani,R.M., Barcinski,M.A., Brown,L., Akbarali,Y.,
            Boltax,J., Kunsch,C., Munger,K. and Libermann,T.A.
  TITLE     Isolation and characterization of a novel epithelium-specific
            transcription factor, ESE-1, a member of the ets family
  JOURNAL   Mol Cell Biol 17 (8), 4419-4433 (1997)
   PUBMED   9234700
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097980.1.
            
            On Jun 10, 2005 this sequence version replaced XP_222659.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097980.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..395
                     /product="ETS-related transcription factor Elf-3"
                     /note="E74-like factor 3"
                     /calculated_mol_wt=44390
     Region          78..155
                     /region_name="SAM_PNT-ESE-1-like"
                     /note="Sterile alpha motif (SAM)/Pointed domain of ESE-1
                     like ETS transcriptional regulators; cd08537"
                     /db_xref="CDD:188880"
     Region          200..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7E1.1)"
     Region          296..383
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..395
                     /gene="Elf3"
                     /coded_by="NM_001024768.1:96..1283"
                     /db_xref="GeneID:304815"
                     /db_xref="RGD:1310687"
ORIGIN      
        1 maatceisnv fsnyfnamys sedptlapap lttfgtedfv ltlnnqhmsp egpvgcvgpq
       61 trsqrdrtep pavlhlaeka swtgerpqfw sktqvldwis yqveknkyda ssidfsrcdm
      121 dgatlcncal eelrlvfgpl gdqlhaqlrd ltssssdels wiiellekdg mtfqeglgds
      181 gpfdqgspfa qellddgrqa spyygssygp gapspgssdf stsgtdtpqs shssdsggsd
      241 vdldltdskv fprdgfpdyk kgepkhgkrk rgrprklske ywdclegkks khaprgthlw
      301 efirdilihp elneglmkwe nrhegvfkfl rseavaqlwg qkkknsnmty eklsramryy
      361 ykreilervd grrlvykfgk nssgwkeeev gesqn
//
LOCUS       NP_001037714             576 aa            linear   ROD 27-APR-2025
DEFINITION  anthrax toxin receptor 1 precursor [Rattus norvegicus].
ACCESSION   NP_001037714 XP_001074844 XP_342719
VERSION     NP_001037714.1
DBSOURCE    REFSEQ: accession NM_001044249.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Cheng,B., Liu,Y., Zhao,Y., Li,Q., Liu,Y., Wang,J., Chen,Y. and
            Zhang,M.
  TITLE     The role of anthrax toxin protein receptor 1 as a new mechanosensor
            molecule and its mechanotransduction in BMSCs under hydrostatic
            pressure
  JOURNAL   Sci Rep 9 (1), 12642 (2019)
   PUBMED   31477767
  REMARK    GeneRIF: The role of anthrax toxin protein receptor 1 as a new
            mechanosensor molecule and its mechanotransduction in BMSCs under
            hydrostatic pressure.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Besschetnova,T.Y., Ichimura,T., Katebi,N., St Croix,B.,
            Bonventre,J.V. and Olsen,B.R.
  TITLE     Regulatory mechanisms of anthrax toxin receptor 1-dependent
            vascular and connective tissue homeostasis
  JOURNAL   Matrix Biol 42, 56-73 (2015)
   PUBMED   25572963
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Stranecky,V., Hoischen,A., Hartmannova,H., Zaki,M.S., Chaudhary,A.,
            Zudaire,E., Noskova,L., Baresova,V., Pristoupilova,A., Hodanova,K.,
            Sovova,J., Hulkova,H., Piherova,L., Hehir-Kwa,J.Y., de Silva,D.,
            Senanayake,M.P., Farrag,S., Zeman,J., Martasek,P., Baxova,A.,
            Afifi,H.H., St Croix,B., Brunner,H.G., Temtamy,S. and Kmoch,S.
  TITLE     Mutations in ANTXR1 cause GAPO syndrome
  JOURNAL   Am J Hum Genet 92 (5), 792-799 (2013)
   PUBMED   23602711
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Opoku-Darko,M., Yuen,C., Gratton,K., Sampson,E. and Bathe,O.F.
  TITLE     Tumor endothelial marker 8 overexpression in breast cancer cells
            enhances tumor growth and metastasis
  JOURNAL   Cancer Invest 29 (10), 676-682 (2011)
   PUBMED   22085271
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Gutwein,L.G., Al-Quran,S.Z., Fernando,S., Fletcher,B.S.,
            Copeland,E.M. and Grobmyer,S.R.
  TITLE     Tumor endothelial marker 8 expression in triple-negative breast
            cancer
  JOURNAL   Anticancer Res 31 (10), 3417-3422 (2011)
   PUBMED   21965755
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Fernando,S. and Fletcher,B.S.
  TITLE     Targeting tumor endothelial marker 8 in the tumor vasculature of
            colorectal carcinomas in mice
  JOURNAL   Cancer Res 69 (12), 5126-5132 (2009)
   PUBMED   19528090
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Ruan,Z., Yang,Z., Wang,Y., Wang,H., Chen,Y., Shang,X., Yang,C.,
            Guo,S., Han,J., Liang,H. and Wu,Y.
  TITLE     DNA vaccine against tumor endothelial marker 8 inhibits tumor
            angiogenesis and growth
  JOURNAL   J Immunother 32 (5), 486-491 (2009)
   PUBMED   19609240
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Davies,G., Rmali,K.A., Watkins,G., Mansel,R.E., Mason,M.D. and
            Jiang,W.G.
  TITLE     Elevated levels of tumour endothelial marker-8 in human breast
            cancer and its clinical significance
  JOURNAL   Int J Oncol 29 (5), 1311-1317 (2006)
   PUBMED   17016666
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Werner,E., Kowalczyk,A.P. and Faundez,V.
  TITLE     Anthrax toxin receptor 1/tumor endothelium marker 8 mediates cell
            spreading by coupling extracellular ligands to the actin
            cytoskeleton
  JOURNAL   J Biol Chem 281 (32), 23227-23236 (2006)
   PUBMED   16762926
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC131853.1.
            
            On or before Aug 28, 2006 this sequence version replaced
            XP_342719.3, XP_001074844.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC131853.1, DQ789143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..576
                     /product="anthrax toxin receptor 1 precursor"
                     /note="tumor endothelial marker 8; anthrax toxin receptor
                     1"
                     /calculated_mol_wt=59865
     sig_peptide     1..39
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4032
     Region          51..235
                     /region_name="vWA_ATR"
                     /note="ATR (Anthrax Toxin Receptor): Anthrax toxin is a
                     key virulence factor for Bacillus anthracis, the causative
                     agent of anthrax. ATR is the cellular receptor for the
                     anthrax protective antigen and facilitates entry of the
                     toxin into cells. The VWA domain in...; cd01474"
                     /db_xref="CDD:238751"
     Site            order(62,64,66,130,162)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238751"
     Region          230..331
                     /region_name="Anth_Ig"
                     /note="Anthrax receptor extracellular domain; pfam05587"
                     /db_xref="CDD:461684"
     Region          408..500
                     /region_name="Ant_C"
                     /note="Anthrax receptor C-terminus region; pfam05586"
                     /db_xref="CDD:461683"
     CDS             1..576
                     /gene="Antxr1"
                     /coded_by="NM_001044249.2:352..2082"
                     /db_xref="GeneID:362393"
                     /db_xref="RGD:1307144"
ORIGIN      
        1 mshgrqrgqr sscsmdragr lgtglrglcv aalvlvcagq ggrredggpa cyggfdlyfi
       61 ldksgsvlhh wneiyyfveq lahrfispql rmsfivfstr gttlmklted reqirqglee
      121 lqkvlpggdt ymhegferas eqiyyensqg yrtasviial tdgelhedlf fysereanrs
      181 rdlgaivycv gvkdfnetql ariadskdhv fpvndgfqal qgiihsilkk scieilaaep
      241 sticagesfq vvvrgngfrh arnvdrvlcs fkindsvtln ekpfavedty llcpapilke
      301 vgmkaalqvs mndglsfiss sviittthcs dgsilaiall ilflllalal lwwfwplcct
      361 viikevpppp veeseeeddd glpkkkwptv dasyyggrgv ggikrmevrw gekgsteega
      421 klekaknarv kmpeqeyefp eprnlnnnmr rpssprkwys pikgkldalw vllrkgydrv
      481 svmrpqpgdt grcinftrvk nsqpakypln nsyhsssppp apiytppppa phcpppapsa
      541 ptppipspps tlppppqapp pnrapppsrp pprpsv
//
LOCUS       NP_001138613             510 aa            linear   ROD 27-APR-2025
DEFINITION  uncharacterized protein CXorf49 homolog [Rattus norvegicus].
ACCESSION   NP_001138613 XP_001069659 XP_576276
VERSION     NP_001138613.1
DBSOURCE    REFSEQ: accession NM_001145141.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC105880.1.
            
            On or before Feb 13, 2009 this sequence version replaced
            XP_001069659.1, XP_576276.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC105880.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..510
                     /product="uncharacterized protein CXorf49 homolog"
                     /calculated_mol_wt=54817
     Region          1..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR64.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3KR64.2)"
     Region          79..500
                     /region_name="DUF4641"
                     /note="Domain of unknown function (DUF4641); pfam15483"
                     /db_xref="CDD:464741"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D454; propagated from
                     UniProtKB/Swiss-Prot (Q3KR64.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D454; propagated from
                     UniProtKB/Swiss-Prot (Q3KR64.2)"
     Region          208..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR64.2)"
     Region          234..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR64.2)"
     Region          368..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR64.2)"
     CDS             1..510
                     /gene="4933412E24Rikl"
                     /coded_by="NM_001145141.1:12..1544"
                     /db_xref="GeneID:500876"
                     /db_xref="RGD:1564901"
ORIGIN      
        1 mgspeeqsvp gddfneestd pnknlslvsg padsnegeir lpspkgsnlp lvsqqdtsea
       61 psvvlwtggc wpdslvseee rlgspedekm dgldflsqps veteqqvanp etpgakeqps
      121 sesfcaetet gsnrrapqas gseeakaasa atflpkgleq srawvsprks ttsrmlisen
      181 vhhppsepel seelnevqmm rvticlkdgn hgnqaknsgp aetgdlarhs nvqtresfmr
      241 mpsslltttr gltsgmerqt skelepfssk kkqgilwgkg gsksnyaeaa agvgalpkag
      301 prkkmtqkkk plwdasavtl gkafhqwgqr lksapaepat fppisgvglp grsnkcsllp
      361 lrpkqcknfy tgkrsgakrt kelqlvaked tdstrdpgsq vqfptcraep pcqsvhqefs
      421 sgdintrslq dpgnsqssgl sqrgilskks tpsgdqeepv gppapdseil qlhgtqgcpr
      481 cpelqkeied lrkqlsalqa vgekfqthst
//
LOCUS       NP_036914                446 aa            linear   ROD 27-APR-2025
DEFINITION  2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_036914 XP_341806
VERSION     NP_036914.1
DBSOURCE    REFSEQ: accession NM_012782.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Ogawa,T., Kouzu,H., Osanami,A., Tatekoshi,Y., Sato,T., Kuno,A.,
            Fujita,Y., Ino,S., Shimizu,M., Toda,Y., Ohwada,W., Yano,T.,
            Tanno,M., Miki,T. and Miura,T.
  TITLE     Downregulation of extramitochondrial BCKDH and its uncoupling from
            AMP deaminase in type 2 diabetic OLETF rat hearts
  JOURNAL   Physiol Rep 11 (4), e15608 (2023)
   PUBMED   36802195
  REMARK    GeneRIF: Downregulation of extramitochondrial BCKDH and its
            uncoupling from AMP deaminase in type 2 diabetic OLETF rat hearts.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Gordeev,S.A., Bykova,T.V., Zubova,S.G., Aksenov,N.D. and
            Pospelova,T.V.
  TITLE     [Antiapoptotic gene bcl-2 prevents cellular senescence program
            reactivation induced by histone deacetylase inhibitor sodium
            butyrate in E1A and cHa-ras transformed rat fibroblasts]
  JOURNAL   Tsitologiia 57 (2), 135-143 (2015)
   PUBMED   26035971
  REMARK    GeneRIF: It has been found that NaBut reduces proliferation rate of
            ERasBcl (E1A, cHa-ras and bcl-2 ) cells significantly weaker than
            of ERas transformed cells
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Knapik-Czajka,M.
  TITLE     Simvastatin increases liver branched-chain alpha-ketoacid
            dehydrogenase activity in rats fed with low protein diet
  JOURNAL   Toxicology 325, 107-114 (2014)
   PUBMED   25193403
  REMARK    GeneRIF: Simvastatin stimulates liver BCKDH activity and BCAAs
            degradation in rats fed with the low protein diet.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Chuang,J.L., Davie,J.R., Chinsky,J.M., Wynn,R.M., Cox,R.P. and
            Chuang,D.T.
  TITLE     Molecular and biochemical basis of intermediate maple syrup urine
            disease. Occurrence of homozygous G245R and F364C mutations at the
            E1 alpha locus of Hispanic-Mexican patients
  JOURNAL   J Clin Invest 95 (3), 954-963 (1995)
   PUBMED   7883996
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Chicco,A.G., Adibi,S.A., Liu,W.Q., Morris,S.M. Jr. and Paul,H.S.
  TITLE     Regulation of gene expression of branched-chain keto acid
            dehydrogenase complex in primary cultured hepatocytes by
            dexamethasone and a cAMP analog
  JOURNAL   J Biol Chem 269 (30), 19427-19434 (1994)
   PUBMED   8034710
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Zhang,B., Zhao,Y., Harris,R.A. and Crabb,D.W.
  TITLE     Molecular defects in the E1 alpha subunit of the branched-chain
            alpha-ketoacid dehydrogenase complex that cause maple syrup urine
            disease
  JOURNAL   Mol Biol Med 8 (1), 39-47 (1991)
   PUBMED   1943689
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Zhang,B., Kuntz,M.J., Goodwin,G.W., Harris,R.A. and Crabb,D.W.
  TITLE     Molecular cloning of a cDNA for the E1 alpha subunit of rat liver
            branched chain alpha-ketoacid dehydrogenase
  JOURNAL   J Biol Chem 262 (31), 15220-15224 (1987)
   PUBMED   2822716
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Shimomura,Y., Paxton,R., Ozawa,T. and Harris,R.A.
  TITLE     Purification of branched chain alpha-ketoacid dehydrogenase complex
            from rat liver
  JOURNAL   Anal Biochem 163 (1), 74-78 (1987)
   PUBMED   3619032
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB579195.1, J02827.1 and BC089915.1.
            
            On Oct 17, 2005 this sequence version replaced XP_341806.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161819.1, J02827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..446
                     /product="2-oxoisovalerate dehydrogenase subunit alpha,
                     mitochondrial"
                     /EC_number="1.2.4.4"
                     /note="branched chain alpha-ketoacid dehydrogenase subunit
                     E1 alpha; BCKDH E1-alpha; branched-chain alpha-keto acid
                     dehydrogenase E1 component alpha chain; BCKDE1A; branched
                     chain keto acid dehydrogenase subunit E1, alpha
                     polypeptide; branched chain ketoacid dehydrogenase E1,
                     alpha polypeptide"
                     /calculated_mol_wt=50537
     Region          81..430
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
     CDS             1..446
                     /gene="Bckdha"
                     /gene_synonym="BCKDA; E1a"
                     /coded_by="NM_012782.1:2..1342"
                     /db_xref="GeneID:25244"
                     /db_xref="RGD:2196"
ORIGIN      
        1 mavamsaaki wrpsrglrqa allllgrpga rglarfhpsr qqqqqfpsld dkpqfpgasa
       61 efvdklefiq pnvisgipiy rvmdrqgqii npsedphlpq eevlklyrsm tllntmdril
      121 yesqrqgris fymtnygeeg thvgsaaale rtdlvfgqyr eagvlmyrdy plelfmaqcy
      181 gnvsdpgkgr qmpvhygcke rhfvtisspl atqipqavga ayaakranan qivicyfgeg
      241 aasegdahag fnfaatlecp iiffcrnngy aistptseqy rgdgiaargp gygimsirvd
      301 gndvfavyna tkearrrava enqpflieam tyrighhsts ddssayrsvd evnywdkqdh
      361 pisrlrqyll nqgwwdeeqe kawrkqsrkk vmeafeqaer klkpnpsllf sdvyqempaq
      421 lrrqqeslar hlqtygehyp ldhfdk
//
LOCUS       NP_071977                604 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase A-Raf isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_071977
VERSION     NP_071977.1
DBSOURCE    REFSEQ: accession NM_022532.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Huang,L.E., Cohen,A.L., Colman,H., Jensen,R.L., Fults,D.W. and
            Couldwell,W.T.
  TITLE     IGFBP2 expression predicts IDH-mutant glioma patient survival
  JOURNAL   Oncotarget 8 (1), 191-202 (2017)
   PUBMED   27852048
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Gan,X., Wang,J., Wang,C., Sommer,E., Kozasa,T., Srinivasula,S.,
            Alessi,D., Offermanns,S., Simon,M.I. and Wu,D.
  TITLE     PRR5L degradation promotes mTORC2-mediated PKC-delta
            phosphorylation and cell migration downstream of Galpha12
  JOURNAL   Nat Cell Biol 14 (7), 686-696 (2012)
   PUBMED   22609986
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Roskoski,R. Jr.
  TITLE     MEK1/2 dual-specificity protein kinases: structure and regulation
  JOURNAL   Biochem Biophys Res Commun 417 (1), 5-10 (2012)
   PUBMED   22177953
  REMARK    Review article
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Polzien,L., Baljuls,A., Rennefahrt,U.E.E., Fischer,A., Schmitz,W.,
            Zahedi,R.P., Sickmann,A., Metz,R., Albert,S., Benz,R., Hekman,M.
            and Rapp,U.R.
  TITLE     Identification of novel in vivo phosphorylation sites of the human
            proapoptotic protein BAD: pore-forming activity of BAD is regulated
            by phosphorylation
  JOURNAL   J Biol Chem 284 (41), 28004-28020 (2009)
   PUBMED   19667065
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Yokoyama,T., Takano,K., Yoshida,A., Katada,F., Sun,P., Takenawa,T.,
            Andoh,T. and Endo,T.
  TITLE     DA-Raf1, a competent intrinsic dominant-negative antagonist of the
            Ras-ERK pathway, is required for myogenic differentiation
  JOURNAL   J Cell Biol 177 (5), 781-793 (2007)
   PUBMED   17535970
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Gruppuso,P.A. and Boylan,J.M.
  TITLE     Hepatic epidermal growth factor-regulated mitogen-activated protein
            kinase kinase kinase activity in the rat: lack of identity with
            known forms of raf and MEKK
  JOURNAL   FEBS Lett 466 (1), 200-204 (2000)
   PUBMED   10648842
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Kim,S.O., Irwin,P., Katz,S. and Pelech,S.L.
  TITLE     Expression of mitogen-activated protein kinase pathways during
            postnatal development of rat heart
  JOURNAL   J Cell Biochem 71 (2), 286-301 (1998)
   PUBMED   9779826
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Ishikawa,F., Takaku,F., Nagao,M. and Sugimura,T.
  TITLE     The complete primary structure of the rat A-raf cDNA coding region:
            conservation of the putative regulatory regions present in rat
            c-raf
  JOURNAL   Oncogene Res 1 (3), 243-253 (1987)
   PUBMED   3449797
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Huleihel,M., Goldsborough,M., Cleveland,J., Gunnell,M., Bonner,T.
            and Rapp,U.R.
  TITLE     Characterization of murine A-raf, a new oncogene related to the
            v-raf oncogene
  JOURNAL   Mol Cell Biol 6 (7), 2655-2662 (1986)
   PUBMED   3491291
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Williams,A.F., Barclay,A.N., Letarte-Muirhead,M. and Morris,R.J.
  TITLE     Rat thy-1 antigens from thymus and brain: their tissue
            distribution, purification, and chemical composition
  JOURNAL   Cold Spring Harb Symp Quant Biol 41 Pt 1, 51-61 (1977)
   PUBMED   70317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO572305.1, X06942.1 and AI712552.1.
            
            Sequence Note: This RefSeq record was created using sequences from
            two different strains, F344 and Sprague-Dawley, because no single
            transcript from the same strain was available for the full length
            of the gene.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X06942.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..604
                     /product="serine/threonine-protein kinase A-Raf isoform 1"
                     /EC_number="2.7.11.1"
                     /note="v-raf murine sarcoma 3611 viral oncogene homolog 1;
                     v-raf oncogene homolog 1 (murine sarcoma 3611 virus); Raf
                     related protein; A-Raf proto-oncogene
                     serine/threonine-protein kinase; Ras-binding protein;
                     serine/threonine-protein kinase A-Raf; proto-oncogene
                     A-Raf; proto-oncogene A-Raf-1"
                     /calculated_mol_wt=67421
     Region          19..91
                     /region_name="RBD_ARAF"
                     /note="Ras-binding domain (RBD) found in
                     serine/threonine-protein kinase ARAF; cd17133"
                     /db_xref="CDD:340653"
     Site            order(20,22,27..32,34,47,51..53)
                     /site_type="other"
                     /note="putative RBD_Raf-Ras interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            order(20,27,29..32,47,50..53)
                     /site_type="other"
                     /note="RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            85
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:340653"
     Region          96..147
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Region          178..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14056.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Region          241..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14056.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Region          307..571
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(314..317,320,322,332,334,365,380..383,427,431..432,
                     434,444..445)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     CDS             1..604
                     /gene="Araf"
                     /gene_synonym="Araf1"
                     /coded_by="NM_022532.2:111..1925"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64363"
                     /db_xref="RGD:2148"
ORIGIN      
        1 mepprgppas gaepsravgt vkvylpnkqr tvvtvrdgms vydsldkalk vrglnqdccv
       61 vyrlikgrkt vtawdtaiap ldgeelivev ledvpltmhn fvrktffsla fcdfclkflf
      121 hgfrcqtcgy kfhqhcsskv ptvcvdmstn rrqfyhsiqd lsggsrqqev psnlsvnell
      181 tpqgpspftq qrdqehfsfp apanpplqri rststpnvhm vsttapmdss lmqftaqsfs
      241 tdaagrggdg aprgspspas vssgrksphs klpaeqrerk sladekkkvk nlgyrdsgyy
      301 wevppsevql lkrigtgsfg tvfrgrwhgd vavkvlkvaq ptaeqaqafk nemqvlrktr
      361 hvnillfmgf mtrpgfaiit qwcegsslyh hlhvadtrfd mvqlidvarq taqgmdylha
      421 kniihrdlks nniflheglt vkigdfglat vktrwsgaqp leqpsgsvlw maaevirmqd
      481 pnpysfqsdv yaygvvlyel mtgslpyshi gsrdqiifmv grgylspdls kifsncpkam
      541 rrlltdclkf qreerplfpq ilatiellqr slpkiersas epslhrtqad elpacllsaa
      601 rlvp
//
LOCUS       NP_001028844             284 aa            linear   ROD 27-APR-2025
DEFINITION  bcl-2-like protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001028844
VERSION     NP_001028844.1
DBSOURCE    REFSEQ: accession NM_001033672.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Perez-Serna,A.A., Dos Santos,R.S., Ripoll,C., Nadal,A.,
            Eizirik,D.L. and Marroqui,L.
  TITLE     BCL-XL Overexpression Protects Pancreatic beta-Cells against
            Cytokine- and Palmitate-Induced Apoptosis
  JOURNAL   Int J Mol Sci 24 (6), 5657 (2023)
   PUBMED   36982731
  REMARK    GeneRIF: BCL-XL Overexpression Protects Pancreatic beta-Cells
            against Cytokine- and Palmitate-Induced Apoptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Alam,M. and Mishra,R.
  TITLE     Bcl-xL expression and regulation in the progression, recurrence,
            and cisplatin resistance of oral cancer
  JOURNAL   Life Sci 280, 119705 (2021)
   PUBMED   34111459
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Rozier,R., Paul,R., Madji Hounoum,B., Villa,E., Mhaidly,R.,
            Chiche,J., Verhoeyen,E., Marchetti,S., Vandenberghe,A.,
            Raucoules,M., Carles,M. and Ricci,J.E.
  TITLE     Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism
  JOURNAL   FEBS J 288 (11), 3547-3569 (2021)
   PUBMED   33340237
  REMARK    GeneRIF: Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Liang,J.R. and Yang,H.
  TITLE     Ginkgolic acid (GA) suppresses gastric cancer growth by inducing
            apoptosis and suppressing STAT3/JAK2 signaling regulated by ROS
  JOURNAL   Biomed Pharmacother 125, 109585 (2020)
   PUBMED   32106377
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Sadek,K., Abouzed,T., Nasr,S. and Shoukry,M.
  TITLE     Licochalcone B Ameliorates Liver Cancer via Targeting of Apoptotic
            Genes, DNA Repair Systems, and Cell Cycle Control
  JOURNAL   Iran J Pharm Res 19 (4), 372-386 (2020)
   PUBMED   33841550
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Chao,D.T., Linette,G.P., Boise,L.H., White,L.S., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bcl-XL and Bcl-2 repress a common pathway of cell death
  JOURNAL   J Exp Med 182 (3), 821-828 (1995)
   PUBMED   7650488
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Gonzalez-Garcia,M., Garcia,I., Ding,L., O'Shea,S., Boise,L.H.,
            Thompson,C.B. and Nunez,G.
  TITLE     bcl-x is expressed in embryonic and postnatal neural tissues and
            functions to prevent neuronal cell death
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4304-4308 (1995)
   PUBMED   7753802
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Tilly,J.L., Tilly,K.I., Kenton,M.L. and Johnson,A.L.
  TITLE     Expression of members of the bcl-2 gene family in the immature rat
            ovary: equine chorionic gonadotropin-mediated inhibition of
            granulosa cell apoptosis is associated with decreased bax and
            constitutive bcl-2 and bcl-xlong messenger ribonucleic acid levels
  JOURNAL   Endocrinology 136 (1), 232-241 (1995)
   PUBMED   7828536
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Gonzalez-Garcia,M., Perez-Ballestero,R., Ding,L., Duan,L.,
            Boise,L.H., Thompson,C.B. and Nunez,G.
  TITLE     bcl-XL is the major bcl-x mRNA form expressed during murine
            development and its product localizes to mitochondria
  JOURNAL   Development 120 (10), 3033-3042 (1994)
   PUBMED   7607090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY141038.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1 and 2 both encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY141038.1, CO555623.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..284
                     /product="bcl-2-like protein 1 isoform 1"
                     /note="bcl-2-like protein 1; B cell lymphoma like X;
                     bcl2-L-1; apoptosis regulator Bcl-X; B cell lymphoma 2
                     like"
                     /calculated_mol_wt=31645
     Region          1..>188
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Region          27..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     CDS             1..284
                     /gene="Bcl2l1"
                     /gene_synonym="bcl-X; Bcl-xl; Bcl2l; Bclx"
                     /coded_by="NM_001033672.1:336..1190"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24888"
                     /db_xref="RGD:2200"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapee teperetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaswm atylndhlep
      181 wiqenggwvr ttplvcpplv clssveipnc pfwspgmvve didysgdipg ftlipgvnfg
      241 niddpvfkep vffilatlva pqfhsfvpis rqrktacvft wlkt
//
LOCUS       NP_114468                412 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily A member 2 [Rattus norvegicus].
ACCESSION   NP_114468
VERSION     NP_114468.2
DBSOURCE    REFSEQ: accession NM_032079.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Rauch,J.N. and Gestwicki,J.E.
  TITLE     Binding of human nucleotide exchange factors to heat shock protein
            70 (Hsp70) generates functionally distinct complexes in vitro
  JOURNAL   J Biol Chem 289 (3), 1402-1414 (2014)
   PUBMED   24318877
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Hageman,J., van Waarde,M.A., Zylicz,A., Walerych,D. and
            Kampinga,H.H.
  TITLE     The diverse members of the mammalian HSP70 machine show distinct
            chaperone-like activities
  JOURNAL   Biochem J 435 (1), 127-142 (2011)
   PUBMED   21231916
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Rosales-Hernandez,A., Beck,K.E., Zhao,X., Braun,A.P. and Braun,J.E.
  TITLE     RDJ2 (DNAJA2) chaperones neural G protein signaling pathways
  JOURNAL   Cell Stress Chaperones 14 (1), 71-82 (2009)
   PUBMED   18595009
  REMARK    GeneRIF: Rdj2 modulates G protein signaling and further suggest
            that chaperoning G proteins is an emerging theme of the J protein
            network.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Smith,D.F. and Toft,D.O.
  TITLE     Minireview: the intersection of steroid receptors with molecular
            chaperones: observations and questions
  JOURNAL   Mol Endocrinol 22 (10), 2229-2240 (2008)
   PUBMED   18451092
  REMARK    Review article
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Prescott,J. and Coetzee,G.A.
  TITLE     Molecular chaperones throughout the life cycle of the androgen
            receptor
  JOURNAL   Cancer Lett 231 (1), 12-19 (2006)
   PUBMED   16356826
  REMARK    Review article
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Lee,K.J., Terada,K., Oyadomari,S., Inomata,Y., Mori,M. and Gotoh,T.
  TITLE     Induction of molecular chaperones in carbon tetrachloride-treated
            rat liver: implications in protection against liver damage
  JOURNAL   Cell Stress Chaperones 9 (1), 58-68 (2004)
   PUBMED   15270078
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Terada,K. and Mori,M.
  TITLE     Human DnaJ homologs dj2 and dj3, and bag-1 are positive
            cochaperones of hsc70
  JOURNAL   J Biol Chem 275 (32), 24728-24734 (2000)
   PUBMED   10816573
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Andres,D.A., Shao,H., Crick,D.C. and Finlin,B.S.
  TITLE     Expression cloning of a novel farnesylated protein, RDJ2, encoding
            a DnaJ protein homologue
  JOURNAL   Arch Biochem Biophys 346 (1), 113-124 (1997)
   PUBMED   9328291
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087010.1.
            
            On Dec 26, 2004 this sequence version replaced NP_114468.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087010.1, U95727.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..412
                     /product="dnaJ homolog subfamily A member 2"
                     /note="DnaJ (Hsp40) homolog, subfamily A, member 2"
                     /calculated_mol_wt=45615
     mat_peptide     1..409
                     /product="DnaJ homolog subfamily A member 2.
                     /id=PRO_0000071013"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
                     /calculated_mol_wt=45410
     Region          4..412
                     /region_name="PTZ00037"
                     /note="DnaJ_C chaperone protein; Provisional"
                     /db_xref="CDD:240236"
     Site            39
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYJ0; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60884; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Region          143..150
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
     Site            152
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYJ0; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Region          159..166
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
     Region          186..193
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
     Region          202..209
                     /region_name="CXXCXGXG motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
     Region          365..412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35824.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O60884; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60884; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60884; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     Site            409
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:O60884; propagated from
                     UniProtKB/Swiss-Prot (O35824.1)"
     CDS             1..412
                     /gene="Dnaja2"
                     /gene_synonym="Cpr3; Dj3; DjA2; Dnj3; Hirip4; Rdj2"
                     /coded_by="NM_032079.2:21..1259"
                     /db_xref="GeneID:84026"
                     /db_xref="RGD:71001"
ORIGIN      
        1 manvadtkly dilgvppgas enelkkayrk lakeyhpdkn pnagdkfkei sfayevlsnp
       61 ekrelydryg eqglregsgg gggmddifsh ifggglfgfm gnqsrsrngr rrgedmmhpl
      121 kvsledlyng kttklqlskn vlcsacsgqg gksgavqkcs acrgrgvrim irqlapgmvq
      181 qmqsvcsdcn gegevinekd rckkcegkkv ikevkilevh vdkgmkhgqr itftgeadqa
      241 pgvepgdivl llqekehevf qrdgndlhmt ykiglvealc gfqftfkhld arqivvkypp
      301 gkviepgcvr vvrgegmpqy rnpfekgdly ikfdvqfpen nwinpdklse ledllpsrpe
      361 vpnvigetee velqefdstr gsgggqrrea yndssdeess shhgpgvqca hq
//
LOCUS       NP_001019528             345 aa            linear   ROD 27-APR-2025
DEFINITION  myb/SANT-like DNA-binding domain-containing protein 4 [Rattus
            norvegicus].
ACCESSION   NP_001019528 XP_576351
VERSION     NP_001019528.1
DBSOURCE    REFSEQ: accession NM_001024357.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC096000.1.
            
            On May 27, 2005 this sequence version replaced XP_576351.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC096000.1, FQ121521.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q11"
     Protein         1..345
                     /product="myb/SANT-like DNA-binding domain-containing
                     protein 4"
                     /note="Myb/SANT-like DNA-binding domain containing 4 with
                     coiled-coils"
                     /calculated_mol_wt=41102
     Region          8..86
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q501L3.1)"
     Region          141..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501L3.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCY6; propagated from
                     UniProtKB/Swiss-Prot (Q501L3.1)"
     Region          <206..>341
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..345
                     /gene="Msantd4"
                     /coded_by="NM_001024357.1:196..1233"
                     /db_xref="GeneID:500941"
                     /db_xref="RGD:1565380"
ORIGIN      
        1 mkqlkrkrks nfsvqetqtl lkeitkrkev ifskqlntti nvmkrmawee iaqcvnavge
       61 geqrtgtevk rryldwralm krkrmkanmk lvgsgfplpt sdlddslted idekiafrnd
      121 anfdwqnvad frdaggslte vkveeeerdp qspefeieee eemlssvipd srrenelpdf
      181 phidefftln stpsrptyde phllmniekq klelekrrld ieaerlqvek erlqiekerl
      241 rhldleherl qlekerlqie rekwrlqlvs tekpalenel gqgeksmlqp qdieaeklkl
      301 ererlqlekd rlqflkfese klqiekerlq vekerlriqk eghlp
//
LOCUS       NP_598241                610 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell immunomodulatory protein precursor [Rattus norvegicus].
ACCESSION   NP_598241 XP_346519
VERSION     NP_598241.2
DBSOURCE    REFSEQ: accession NM_133557.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Principe,S., Jones,E.E., Kim,Y., Sinha,A., Nyalwidhe,J.O.,
            Brooks,J., Semmes,O.J., Troyer,D.A., Lance,R.S., Kislinger,T. and
            Drake,R.R.
  TITLE     In-depth proteomic analyses of exosomes isolated from expressed
            prostatic secretions in urine
  JOURNAL   Proteomics 13 (10-11), 1667-1671 (2013)
   PUBMED   23533145
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085706.1.
            
            On May 23, 2007 this sequence version replaced NP_598241.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085706.1, AF480856.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..610
                     /product="T-cell immunomodulatory protein precursor"
                     /note="CDA08-like protein; linkin; integrin-alpha FG-GAP
                     repeat-containing protein 1; T-cell immunomodulatory
                     protein; hypothetical protein CDA08"
                     /calculated_mol_wt=64317
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3074
     mat_peptide     33..610
                     /product="T-cell immunomodulatory protein.
                     /id=PRO_0000034356"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R4E1.1)"
                     /calculated_mol_wt=64317
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Region          54..117
                     /region_name="FG-GAP_3"
                     /note="FG-GAP-like repeat; pfam13517"
                     /db_xref="CDD:433275"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Region          98..135
                     /region_name="FG-GAP 1, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            123
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Region          153..183
                     /region_name="FG-GAP 2, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Region          256..291
                     /region_name="FG-GAP 3, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            351
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q8R4E1.1)"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R4E1.1)"
     CDS             1..610
                     /gene="Itfg1"
                     /gene_synonym="Cda08"
                     /coded_by="NM_133557.2:144..1976"
                     /db_xref="GeneID:171083"
                     /db_xref="RGD:619898"
ORIGIN      
        1 maagllpsar avlallflgl allsvgpapa qalhnvtael fggeawgtla afgdlnsdkq
       61 tdlfvlrern dlivfladqs apyfkpkvkv slknfsalvt svvpgdydgd sqmdvlltyf
      121 pqnhsnnelg avifwgqnqt ldpknmtiln rtfhdqplim dfngdlipdv faitnessqp
      181 qillggdlsw hpalttkskm rdphshafid ltedftadlf lttlsasntf qfeiwenlgg
      241 nfsirsvfek pknlvvvgqs afadfdgdgh mdhllpgced kdcqksaiyl mrsgtgqwap
      301 vlqdfsnkgt lwgfvpfvhe erptaipvpl tlhigdynmd gypdalailk ntsgsnqqaf
      361 llenvpcnna sceevhrmfk vywdlaglnl ikdamvatff diyedgildi ivlskgytks
      421 dvaihtlknn feadayfvkv ivlsglcssd cprkitpfgv nqpgpyimyt tvdangylkn
      481 gsagqlsqsa hlalqlpynv lglgrsanfl dhlfvgiprp sgeksirkqe wtaiipnsql
      541 ivipyphsvp rswsaklylt psnivlltav altgvcvfil aiiailhwqe kkaddrekrq
      601 eahrfhfdam
//
LOCUS       NP_445806               1621 aa            linear   ROD 27-APR-2025
DEFINITION  DNA (cytosine-5)-methyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_445806
VERSION     NP_445806.3
DBSOURCE    REFSEQ: accession NM_053354.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1621)
  AUTHORS   Ding,X., Lin,Y., Chen,C., Yan,B., Liu,Q., Zheng,H., Wu,Y. and
            Zhou,C.
  TITLE     DNMT1 Mediates Chronic Pain-Related Depression by Inhibiting
            GABAergic Neuronal Activation in the Central Amygdala
  JOURNAL   Biol Psychiatry 94 (8), 672-684 (2023)
   PUBMED   37001844
  REMARK    GeneRIF: DNMT1 Mediates Chronic Pain-Related Depression by
            Inhibiting GABAergic Neuronal Activation in the Central Amygdala.
REFERENCE   2  (residues 1 to 1621)
  AUTHORS   Zhang,S., Xie,H., Du,Y., Wang,B., Lan,B. and Wang,H.
  TITLE     DNMT1-induced miR-133b suppression via methylation promotes
            myocardial fibrosis after myocardial infarction
  JOURNAL   Gen Physiol Biophys 42 (5), 417-429 (2023)
   PUBMED   37702447
  REMARK    GeneRIF: DNMT1-induced miR-133b suppression via methylation
            promotes myocardial fibrosis after myocardial infarction.
REFERENCE   3  (residues 1 to 1621)
  AUTHORS   Wu,Q., Xie,J., Zhu,X. and He,J.
  TITLE     Runt-related transcription factor 3, mediated by
            DNA-methyltransferase 1, regulated Schwann cell proliferation and
            myelination during peripheral nerve regeneration via JAK/STAT
            signaling pathway
  JOURNAL   Neurosci Res 192, 1-10 (2023)
   PUBMED   36690210
  REMARK    GeneRIF: Runt-related transcription factor 3, mediated by
            DNA-methyltransferase 1, regulated Schwann cell proliferation and
            myelination during peripheral nerve regeneration via JAK/STAT
            signaling pathway.
REFERENCE   4  (residues 1 to 1621)
  AUTHORS   Wang,H.J., Zhang,F.C., Xu,T.W., Xu,Y.C., Tian,Y.Q., Wu,Y.Y.,
            Xu,J.T., Hu,S. and Xu,G.Y.
  TITLE     DNMT1 involved in the analgesic effect of folic acid on gastric
            hypersensitivity through downregulating ASIC1 in adult offspring
            rats with prenatal maternal stress
  JOURNAL   CNS Neurosci Ther 29 (6), 1678-1689 (2023)
   PUBMED   36852448
  REMARK    GeneRIF: DNMT1 involved in the analgesic effect of folic acid on
            gastric hypersensitivity through downregulating ASIC1 in adult
            offspring rats with prenatal maternal stress.
REFERENCE   5  (residues 1 to 1621)
  AUTHORS   Hou,Y., Shi,J., Guo,Y. and Shi,G.
  TITLE     DNMT1 regulates polarization of macrophage-induced intervertebral
            disc degeneration by modulating SIRT6 expression and promoting
            pyroptosis in vivo
  JOURNAL   Aging (Albany NY) 15 (10), 4288-4303 (2023)
   PUBMED   37199639
  REMARK    GeneRIF: DNMT1 regulates polarization of macrophage-induced
            intervertebral disc degeneration by modulating SIRT6 expression and
            promoting pyroptosis in vivo.
REFERENCE   6  (residues 1 to 1621)
  AUTHORS   Deng,J. and Szyf,M.
  TITLE     Multiple isoforms of DNA methyltransferase are encoded by the
            vertebrate cytosine DNA methyltransferase gene
  JOURNAL   J Biol Chem 273 (36), 22869-22872 (1998)
   PUBMED   9722504
REFERENCE   7  (residues 1 to 1621)
  AUTHORS   Hollnagel,A., Schroder,D. and Gross,G.
  TITLE     Domain-specific gene activation by parathyroid hormone in
            osteoblastic ROS17/2.8 cells
  JOURNAL   J Biol Chem 271 (36), 21870-21877 (1996)
   PUBMED   8702988
REFERENCE   8  (residues 1 to 1621)
  AUTHORS   Ohsawa,K., Imai,Y., Ito,D. and Kohsaka,S.
  TITLE     Molecular cloning and characterization of annexin V-binding
            proteins with highly hydrophilic peptide structure
  JOURNAL   J Neurochem 67 (1), 89-97 (1996)
   PUBMED   8667030
REFERENCE   9  (residues 1 to 1621)
  AUTHORS   Li,E., Bestor,T.H. and Jaenisch,R.
  TITLE     Targeted mutation of the DNA methyltransferase gene results in
            embryonic lethality
  JOURNAL   Cell 69 (6), 915-926 (1992)
   PUBMED   1606615
REFERENCE   10 (residues 1 to 1621)
  AUTHORS   Farrance,I.K. and Ivarie,R.
  TITLE     Ethylation of poly(dC-dG).poly(dC-dG) by ethyl methanesulfonate
            stimulates the activity of mammalian DNA methyltransferase in vitro
  JOURNAL   Proc Natl Acad Sci U S A 82 (4), 1045-1049 (1985)
   PUBMED   3856245
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473993.2.
            
            On Nov 25, 2008 this sequence version replaced NP_445806.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1621
                     /product="DNA (cytosine-5)-methyltransferase 1"
                     /EC_number="2.1.1.37"
                     /note="MCMT; m.RnoIP; DNA MTase RnoIP; DNA
                     methyltransferase I; DNA methyltransferase (cytosine-5) 1;
                     DNA (cytosine-5-)-methyltransferase 1"
                     /calculated_mol_wt=182909
     Region          16..106
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          109..>327
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          405..540
                     /region_name="DNMT1-RFD"
                     /note="Cytosine specific DNA methyltransferase replication
                     foci domain; pfam12047"
                     /db_xref="CDD:463444"
     Region          649..695
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          759..881
                     /region_name="BAH_Dnmt1_I"
                     /note="BAH, or Bromo Adjacent Homology domain, first copy
                     present in DNA (Cytosine-5)-methyltransferases from
                     Bilateria, Dnmt1 and similar proteins. DNA methylation, or
                     the covalent addition of a methyl group to cytosine within
                     the context of the CpG...; cd04760"
                     /db_xref="CDD:240107"
     Region          969..1105
                     /region_name="BAH_Dnmt1_II"
                     /note="BAH, or Bromo Adjacent Homology domain, second copy
                     present in DNA (Cytosine-5)-methyltransferases from
                     Bilateria, Dnmt1 and similar proteins. DNA methylation, or
                     the covalent addition of a methyl group to cytosine within
                     the context of the CpG...; cd04711"
                     /db_xref="CDD:240062"
     Region          1141..1599
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     CDS             1..1621
                     /gene="Dnmt1"
                     /coded_by="NM_053354.3:81..4946"
                     /db_xref="GeneID:84350"
                     /db_xref="RGD:620979"
ORIGIN      
        1 mpartaparv palaspagsl pdhvrrrlkd lerdglteke cvkeklnllh eflqteiksq
       61 lcdletklhk eelseegyla kvktllnkdl clengtlslt qkangcpang srptwkaema
      121 dsnrsprsrp kprgprrsks dsetmieass ssvatrrttr qttitshfkg pakrkpkeds
      181 ekgnanesaa eerdqdkkrr vagtesrasr agesvekper vrpgtqlcqe eqgeqeddrr
      241 prrqtrelas rrksredpdr earpgthldv ddddekdkrs srprsqprdl atkrrpkeev
      301 eqitpeppeg kdedereekr rkttrkkpep lsipvqsrve rkasqgkasa ipklnppqcp
      361 ecgqylddpd lkyqqhpvda vdepqmltne alsvfdsnss wfetydsspm hkftffsvyc
      421 srghlcpvdt glieknvely fsgvakaihe enpsveggvn gknlgpinqw wisgfdggek
      481 aligfstafa eyflmepspe yapifglmqe kiyiskivve flqsnpdavy edlinkiett
      541 vppsainvnr ftedsllrha qfvvsqvesy ddakdddetp iflspcmrsl ihlagvslgq
      601 rratrrtvin sakvkrkgpt katttklvyq ifdtffseqi ekddkedken tmkrrrcgvc
      661 evcqqpecgk ckackdmvkf ggtgrskqac lkrrcpnlav keadedeead ddipelpspk
      721 klhqgkkkkq nkdriswlge pvkieenrty ywkvsideet levgdcvsvi pddpskplyl
      781 arvtalwedk ngqmfhahwf cagtdtvlga tsdplelflv gecenmqlsy ihskvkviyr
      841 gpspnwameg gmdpeamlpg aedgktyfyq fwysqdyarf esppktqpte dnkhkfclsc
      901 irlaelrqke mpkvleqlee vdgrvycssi tkngvvyrlg dsvylppeaf tfnikmaspm
      961 krskrdpvne nlypehyrky sdyikgsnld apepyrigri keihcgkkkg gkvneadiki
     1021 rlykfyrpen thksiqatyh adinllywsd eeavvdfsdv qgrctveyge dllesiqdys
     1081 qggpdrfyfl eaynsktksf edppnharsp gnkgkgkgkg kgkgkpqvse pkepeaaikl
     1141 pklrtldvfs gcggltegfh qagisetlwa iemwepaaqa frlnnpgttv ftedcnvllk
     1201 lvmagevtns lgqrlpqkgd vemlcggppc qgfsgmnrfn srtyskfkns lvvsflsycd
     1261 yyrprfflle nvrnfvsfrr smvlkltlrc lvrmgyqctf gvlqagqygv aqtrrraiil
     1321 aaapgeklpl fpeplhvfap racqlsvvvd dkkfvsnitr lssgpfrtit vrdtmsdlpe
     1381 iqngasapei syngepqswf qrqlrgshyq pilrdhickd msalvaarmr hiplspgsdw
     1441 rdlpniqvrl rdgvitnklr ytfhdtkngc sstgalrgvc scaegktcdp asrqfntlip
     1501 wclphtgnrh nhwaglygrl ewdgffsttv tnpepmgkqg rvlhpeqhrv vsvrecarsq
     1561 gfpdtyrlfg nildrhrqvg navppplaka igleiklcll asaqesasaa vkgkeettte
     1621 d
//
LOCUS       NP_001094232             282 aa            linear   ROD 27-APR-2025
DEFINITION  hepatitis A virus cellular receptor 2 homolog precursor [Rattus
            norvegicus].
ACCESSION   NP_001094232 XP_001069084 XP_343882
VERSION     NP_001094232.1
DBSOURCE    REFSEQ: accession NM_001100762.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Ramirez Hernandez,E., Hernandez Zimbron,L.F., Segura Perez,E.,
            Sanchez Salgado,J.L., Pereyra Morales,M.A. and Zenteno,E.
  TITLE     Galectin-9 and Tim-3 are upregulated in response to microglial
            activation induced by the peptide Amyloid-beta (25-35)
  JOURNAL   Neuropeptides 105, 102426 (2024)
   PUBMED   38527407
  REMARK    GeneRIF: Galectin-9 and Tim-3 are upregulated in response to
            microglial activation induced by the peptide Amyloid-beta (25-35).
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Hu,X.H., Li,Z.H., Muyayalo,K.P., Wang,L.L., Liu,C.Y., Mor,G. and
            Liao,A.H.
  TITLE     A newly intervention strategy in preeclampsia: Targeting PD-1/Tim-3
            signaling pathways to modulate the polarization of decidual
            macrophages
  JOURNAL   FASEB J 36 (1), e22073 (2022)
   PUBMED   34847253
  REMARK    GeneRIF: A newly intervention strategy in preeclampsia: Targeting
            PD-1/Tim-3 signaling pathways to modulate the polarization of
            decidual macrophages.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Guo,S., Li,Y., Wei,B., Liu,W., Li,R., Cheng,W., Zhang,X., He,X.,
            Li,X. and Duan,C.
  TITLE     Tim-3 deteriorates neuroinflammatory and neurocyte apoptosis after
            subarachnoid hemorrhage through the Nrf2/HMGB1 signaling pathway in
            rats
  JOURNAL   Aging (Albany NY) 12 (21), 21161-21185 (2020)
   PUBMED   33168786
  REMARK    GeneRIF: Tim-3 deteriorates neuroinflammatory and neurocyte
            apoptosis after subarachnoid hemorrhage through the Nrf2/HMGB1
            signaling pathway in rats.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Chen,Z.Q., Yu,H., Li,H.Y., Shen,H.T., Li,X., Zhang,J.Y.,
            Zhang,Z.W., Wang,Z. and Chen,G.
  TITLE     Negative regulation of glial Tim-3 inhibits the secretion of
            inflammatory factors and modulates microglia to antiinflammatory
            phenotype after experimental intracerebral hemorrhage in rats
  JOURNAL   CNS Neurosci Ther 25 (6), 674-684 (2019)
   PUBMED   30677253
  REMARK    GeneRIF: Negative regulation of glial Tim-3 inhibits the secretion
            of inflammatory factors and modulates microglia to antiinflammatory
            phenotype after experimental intracerebral hemorrhage in rats.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Li,Z., Li,N., Li,F., Zhou,Z., Sang,J., Jin,Z., Liu,H., Han,Q.,
            Lv,Y. and Liu,Z.
  TITLE     Genetic polymorphisms of immune checkpoint proteins PD-1 and TIM-3
            are associated with survival of patients with hepatitis B
            virus-related hepatocellular carcinoma
  JOURNAL   Oncotarget 7 (18), 26168-26180 (2016)
   PUBMED   27034168
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Graves,P.E., Siroux,V., Guerra,S., Klimecki,W.T. and Martinez,F.D.
  TITLE     Association of atopy and eczema with polymorphisms in T-cell
            immunoglobulin domain and mucin domain-IL-2-inducible T-cell kinase
            gene cluster in chromosome 5 q 33
  JOURNAL   J Allergy Clin Immunol 116 (3), 650-656 (2005)
   PUBMED   16159638
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Gielen,A.W., Lobell,A., Lidman,O., Khademi,M., Olsson,T. and
            Piehl,F.
  TITLE     Expression of T cell immunoglobulin- and mucin-domain-containing
            molecules-1 and -3 (TIM-1 and -3) in the rat nervous and immune
            systems
  JOURNAL   J Neuroimmunol 164 (1-2), 93-104 (2005)
   PUBMED   15913792
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Wefer,J., Harris,R.A. and Lobell,A.
  TITLE     Protective DNA vaccination against experimental autoimmune
            encephalomyelitis is associated with induction of IFNbeta
  JOURNAL   J Neuroimmunol 149 (1-2), 66-76 (2004)
   PUBMED   15020066
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Sabatos,C.A., Chakravarti,S., Cha,E., Schubart,A.,
            Sanchez-Fueyo,A., Zheng,X.X., Coyle,A.J., Strom,T.B., Freeman,G.J.
            and Kuchroo,V.K.
  TITLE     Interaction of Tim-3 and Tim-3 ligand regulates T helper type 1
            responses and induction of peripheral tolerance
  JOURNAL   Nat Immunol 4 (11), 1102-1110 (2003)
   PUBMED   14556006
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Monney,L., Sabatos,C.A., Gaglia,J.L., Ryu,A., Waldner,H.,
            Chernova,T., Manning,S., Greenfield,E.A., Coyle,A.J., Sobel,R.A.,
            Freeman,G.J. and Kuchroo,V.K.
  TITLE     Th1-specific cell surface protein Tim-3 regulates macrophage
            activation and severity of an autoimmune disease
  JOURNAL   Nature 415 (6871), 536-541 (2002)
   PUBMED   11823861
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Oct 20, 2007 this sequence version replaced
            XP_343882.3, XP_001069084.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2381871.1,
                                           SRR26360194.441971.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..282
                     /product="hepatitis A virus cellular receptor 2 homolog
                     precursor"
                     /note="hepatitis A virus cellular receptor 2 homolog; T
                     cell immunoglobulin mucin-3; TIM-3; TIMD-3; HAVcr-2;
                     T-cell membrane protein 3; T-cell immunoglobulin and mucin
                     domain-containing protein 3; T-cell immunoglobulin mucin
                     receptor 3"
                     /calculated_mol_wt=28268
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2391
     mat_peptide     22..282
                     /product="Hepatitis A virus cellular receptor 2 homolog.
                     /id=PRO_0000072703"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0K5.2)"
                     /calculated_mol_wt=28268
     Region          24..130
                     /region_name="IgV_TIM-3_like"
                     /note="Immunoglobulin Variable (IgV) domain of T cell
                     Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and
                     similar domains; cd20982"
                     /db_xref="CDD:409574"
     Region          24..39
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409574"
     Region          24..28
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409574"
     Region          31..39
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409574"
     Region          40..48
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409574"
     Region          49..55
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409574"
     Region          50..63
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409574"
     Region          65..80
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409574"
     Region          66..71
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409574"
     Region          74..77
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409574"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C0K5.2)"
     Region          82..113
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409574"
     Region          82..86
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409574"
     Region          93..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409574"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C0K5.2)"
     Region          104..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409574"
     Region          114..121
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409574"
     Region          121..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409574"
     Region          122..130
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409574"
     Region          138..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0K5.2)"
     Site            147
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:Q8TDQ0; propagated from
                     UniProtKB/Swiss-Prot (P0C0K5.2)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P0C0K5.2)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0K5.2)"
     Region          253..271
                     /region_name="Interaction with BAG6.
                     /evidence=ECO:0000250|UniProtKB:Q8VIM0"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0K5.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ITK.
                     /evidence=ECO:0000250|UniProtKB:Q8TDQ0; propagated from
                     UniProtKB/Swiss-Prot (P0C0K5.2)"
     CDS             1..282
                     /gene="Havcr2"
                     /gene_synonym="tim3"
                     /coded_by="NM_001100762.1:71..919"
                     /db_xref="GeneID:363578"
                     /db_xref="RGD:1305233"
ORIGIN      
        1 mfswlpfsca llllqplpar slenaytaev gknaylpcsy tvpapgtlvp icwgkgscpl
       61 lqcasvvlrt detnvtyrks rryqlkgnfy kgdmsltikn vtladsgtyc criqfpgpmn
      121 deklelklsi tepakvipag tahgdsttas prtlttegsg setqtlvtlh dnngtkistw
      181 adeikdsget irtavhigvg vsaglalali lgvlilkwys skkkklqdls litlansppg
      241 glvnagagri rseeniytie eniyemensn eyycyvssqq ps
//
LOCUS       NP_001004283             548 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit D [Rattus
            norvegicus].
ACCESSION   NP_001004283 XP_343284
VERSION     NP_001004283.1
DBSOURCE    REFSEQ: accession NM_001004283.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Lee,A.S., Kranzusch,P.J., Doudna,J.A. and Cate,J.H.
  TITLE     eIF3d is an mRNA cap-binding protein that is required for
            specialized translation initiation
  JOURNAL   Nature 536 (7614), 96-99 (2016)
   PUBMED   27462815
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Lee,A.S., Kranzusch,P.J. and Cate,J.H.
  TITLE     eIF3 targets cell-proliferation messenger RNAs for translational
            activation or repression
  JOURNAL   Nature 522 (7554), 111-114 (2015)
   PUBMED   25849773
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Hinnebusch,A.G.
  TITLE     The scanning mechanism of eukaryotic translation initiation
  JOURNAL   Annu Rev Biochem 83, 779-812 (2014)
   PUBMED   24499181
  REMARK    Review article
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Villa,N., Do,A., Hershey,J.W. and Fraser,C.S.
  TITLE     Human eukaryotic initiation factor 4G (eIF4G) protein binds to
            eIF3c, -d, and -e to promote mRNA recruitment to the ribosome
  JOURNAL   J Biol Chem 288 (46), 32932-32940 (2013)
   PUBMED   24092755
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Zeng,L., Wan,Y., Li,D., Wu,J., Shao,M., Chen,J., Hui,L., Ji,H. and
            Zhu,X.
  TITLE     The m subunit of murine translation initiation factor eIF3
            maintains the integrity of the eIF3 complex and is required for
            embryonic development, homeostasis, and organ size control
  JOURNAL   J Biol Chem 288 (42), 30087-30093 (2013)
   PUBMED   24003236
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Zhou,M., Sandercock,A.M., Fraser,C.S., Ridlova,G., Stephens,E.,
            Schenauer,M.R., Yokoi-Fong,T., Barsky,D., Leary,J.A., Hershey,J.W.,
            Doudna,J.A. and Robinson,C.V.
  TITLE     Mass spectrometry reveals modularity and a complete subunit
            interaction map of the eukaryotic translation factor eIF3
  JOURNAL   Proc Natl Acad Sci U S A 105 (47), 18139-18144 (2008)
   PUBMED   18599441
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     Reconstitution reveals the functional core of mammalian eIF3
  JOURNAL   EMBO J 26 (14), 3373-3383 (2007)
   PUBMED   17581632
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Damoc,E., Fraser,C.S., Zhou,M., Videler,H., Mayeur,G.L.,
            Hershey,J.W., Doudna,J.A., Robinson,C.V. and Leary,J.A.
  TITLE     Structural characterization of the human eukaryotic initiation
            factor 3 protein complex by mass spectrometry
  JOURNAL   Mol Cell Proteomics 6 (7), 1135-1146 (2007)
   PUBMED   17322308
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079005.1.
            
            On Sep 10, 2004 this sequence version replaced XP_343284.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079005.1, SRR8487230.72996.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..548
                     /product="eukaryotic translation initiation factor 3
                     subunit D"
                     /note="eIF-3-zeta; eukaryotic translation initiation
                     factor 3, subunit 7 (zeta); eukaryotic translation
                     initiation factor 3 subunit 7"
                     /calculated_mol_wt=63858
     Region          4..521
                     /region_name="eIF-3_zeta"
                     /note="Eukaryotic translation initiation factor 3 subunit
                     7 (eIF-3); pfam05091"
                     /db_xref="CDD:461547"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70194; propagated from
                     UniProtKB/Swiss-Prot (Q6AYK8.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15371; propagated from
                     UniProtKB/Swiss-Prot (Q6AYK8.1)"
     Region          285..299
                     /region_name="RNA gate.
                     /evidence=ECO:0000250|UniProtKB:K7IM66"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYK8.1)"
     Region          523..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYK8.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYK8.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYK8.1)"
     CDS             1..548
                     /gene="Eif3d"
                     /gene_synonym="Eif3s7"
                     /coded_by="NM_001004283.1:90..1736"
                     /db_xref="GeneID:362952"
                     /db_xref="RGD:1303255"
ORIGIN      
        1 makfmtpviq dnpsgwgpca vpeqfrdmpy qpfskgdrlg kvadwtgaty qdkrytnkys
       61 sqfgggsqya yfheedetsf qlvdtartqk tayqrnrmrf aqrnlrrdkd rrnmvqfnlq
      121 tlpksakqke rerirlqkkf qkqfgvrqkw dqksqkprds svevrsdwev keemdfpqlm
      181 kmrylevsep qdieccgale yydkafdrit trsekplrsi krifhtvttt ddpvirklak
      241 tqgnvfatda ilatlmsctr svyswdivvq rvgsklffdk rdnsdfdllt vsetaneppq
      301 degnsfnspr nlameatyin hnfsqqclrm grerynfpnp npfveddmdk neiasvayry
      361 rrwklgddid livrcehdgv mtgangevsf iniktlnewd srhcngvdwr qkldsqrgav
      421 iatelknnsy klarwtccal lagseylklg yvsryhvkds srhvilgtqq fkpnefasqi
      481 nlsvenawgi lrcvidicmk leegkylilk dpnkqvirvy slpdgtfsse edeedeeeee
      541 eeeeeeet
//
LOCUS       NP_001032585             523 aa            linear   ROD 27-APR-2025
DEFINITION  OTU domain-containing protein 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001032585 XP_343775
VERSION     NP_001032585.1
DBSOURCE    REFSEQ: accession NM_001037496.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Rutz,S., Kayagaki,N., Phung,Q.T., Eidenschenk,C., Noubade,R.,
            Wang,X., Lesch,J., Lu,R., Newton,K., Huang,O.W., Cochran,A.G.,
            Vasser,M., Fauber,B.P., DeVoss,J., Webster,J., Diehl,L.,
            Modrusan,Z., Kirkpatrick,D.S., Lill,J.R., Ouyang,W. and Dixit,V.M.
  TITLE     Deubiquitinase DUBA is a post-translational brake on interleukin-17
            production in T cells
  JOURNAL   Nature 518 (7539), 417-421 (2015)
   PUBMED   25470037
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Mevissen,T.E., Hospenthal,M.K., Geurink,P.P., Elliott,P.R.,
            Akutsu,M., Arnaudo,N., Ekkebus,R., Kulathu,Y., Wauer,T., El
            Oualid,F., Freund,S.M., Ovaa,H. and Komander,D.
  TITLE     OTU deubiquitinases reveal mechanisms of linkage specificity and
            enable ubiquitin chain restriction analysis
  JOURNAL   Cell 154 (1), 169-184 (2013)
   PUBMED   23827681
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Huang,O.W., Ma,X., Yin,J., Flinders,J., Maurer,T., Kayagaki,N.,
            Phung,Q., Bosanac,I., Arnott,D., Dixit,V.M., Hymowitz,S.G.,
            Starovasnik,M.A. and Cochran,A.G.
  TITLE     Phosphorylation-dependent activity of the deubiquitinase DUBA
  JOURNAL   Nat Struct Mol Biol 19 (2), 171-175 (2012)
   PUBMED   22245969
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Kayagaki,N., Phung,Q., Chan,S., Chaudhari,R., Quan,C.,
            O'Rourke,K.M., Eby,M., Pietras,E., Cheng,G., Bazan,J.F., Zhang,Z.,
            Arnott,D. and Dixit,V.M.
  TITLE     DUBA: a deubiquitinase that regulates type I interferon production
  JOURNAL   Science 318 (5856), 1628-1632 (2007)
   PUBMED   17991829
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC110054.1.
            
            On Nov 30, 2005 this sequence version replaced XP_343775.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110054.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..523
                     /product="OTU domain-containing protein 5 isoform 2"
                     /EC_number="3.4.19.12"
                     /note="OTU domain-containing protein 5; DUBA;
                     deubiquinating enzyme A; deubiquitinating enzyme A; OTU
                     domain containing 5"
                     /calculated_mol_wt=56403
     Region          169..292
                     /region_name="OTU_OTUD5-like"
                     /note="OTU (ovarian tumor) domain of OTU domain-containing
                     protein 5 and similar proteins; cd22752"
                     /db_xref="CDD:438589"
     Site            order(177..178,181,214,217..218,220,236..239,242..243,264,
                     266,281,284..287)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438589"
     CDS             1..523
                     /gene="Otud5"
                     /coded_by="NM_001037496.1:105..1676"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363452"
                     /db_xref="RGD:1563027"
ORIGIN      
        1 mtilpkkkpp ppdadpanep pppgplppap rrgggvgvgg ggtgvggger drdsgvvgar
       61 praspppqgp lpgppgalhr walavppgav agprpqqasp ppcggpggpg ggpgdalvgg
      121 aspereevga gynsedeyea aaarieamdp atveqqehwf ekalrdkkgf iikqmkedga
      181 clfravadqv ygdqdmhevv rkhcmdylmk nadyfsnyvt edfttyinrk rknnchgnhi
      241 emqamaemyn rpvevyqyst epintfhgih qnedepirvs yhrnihynsv vnpnkatigv
      301 glglpsfkpg faeqslmkna iktseeswie qqmledkkra tdweatneai eeqvaresyl
      361 qwlrdqekqa rqvrgpsqpr kasatcssat aaassgleew tsrsprqrss asspehpelh
      421 aelgikppsp gtvlalakpp spcapgtssq fsagadrats plvslypale craliqqmsp
      481 safglndwdd deilasvlav sqqeyldsmk knkvhrdppp dks
//
LOCUS       NP_001030334             312 aa            linear   ROD 27-APR-2025
DEFINITION  ubiquinone biosynthesis protein COQ9, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_001030334 XP_574198
VERSION     NP_001030334.1
DBSOURCE    REFSEQ: accession NM_001035257.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lohman,D.C., Forouhar,F., Beebe,E.T., Stefely,M.S., Minogue,C.E.,
            Ulbrich,A., Stefely,J.A., Sukumar,S., Luna-Sanchez,M., Jochem,A.,
            Lew,S., Seetharaman,J., Xiao,R., Wang,H., Westphall,M.S.,
            Wrobel,R.L., Everett,J.K., Mitchell,J.C., Lopez,L.C., Coon,J.J.,
            Tong,L. and Pagliarini,D.J.
  TITLE     Mitochondrial COQ9 is a lipid-binding protein that associates with
            COQ7 to enable coenzyme Q biosynthesis
  JOURNAL   Proc Natl Acad Sci U S A 111 (44), E4697-E4705 (2014)
   PUBMED   25339443
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Garcia-Corzo,L., Luna-Sanchez,M., Doerrier,C., Garcia,J.A.,
            Guaras,A., Acin-Perez,R., Bullejos-Peregrin,J., Lopez,A.,
            Escames,G., Enriquez,J.A., Acuna-Castroviejo,D. and Lopez,L.C.
  TITLE     Dysfunctional Coq9 protein causes predominant encephalomyopathy
            associated with CoQ deficiency
  JOURNAL   Hum Mol Genet 22 (6), 1233-1248 (2013)
   PUBMED   23255162
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Kucharska,J., Gvozdjakova,A. and Simko,F.
  TITLE     Simvastatin decreased coenzyme Q in the left ventricle and skeletal
            muscle but not in the brain and liver in L-NAME-induced
            hypertension
  JOURNAL   Physiol Res 56 Suppl 2, S49-S54 (2007)
   PUBMED   17824807
  REMARK    GeneRIF: Administration of simvastatin under the condition of
            nitric oxide-deficiency reduced the level of coenzyme Q9/10 in the
            heart and skeletal muscle.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK600220.1 and BC104702.1.
            
            On Oct 31, 2005 this sequence version replaced XP_574198.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127449.1, SRR8487226.40572.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..312
                     /product="ubiquinone biosynthesis protein COQ9,
                     mitochondrial precursor"
                     /note="ubiquinone biosynthesis protein COQ9,
                     mitochondrial; coenzyme Q9 homolog"
                     /calculated_mol_wt=30185
     transit_peptide 1..45
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q68FT1.2)"
                     /calculated_mol_wt=4979
     Region          17..32
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000250|UniProtKB:O75208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FT1.2)"
     Region          43..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FT1.2)"
     mat_peptide     46..312
                     /product="Ubiquinone biosynthesis protein COQ9,
                     mitochondrial. /id=PRO_0000228639"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FT1.2)"
                     /calculated_mol_wt=30185
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FT1.2)"
     Region          96..275
                     /region_name="COQ9"
                     /note="cl21709"
                     /db_xref="CDD:473940"
     Site            169
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1Z0; propagated from
                     UniProtKB/Swiss-Prot (Q68FT1.2)"
     CDS             1..312
                     /gene="Coq9"
                     /coded_by="NM_001035257.1:10..948"
                     /db_xref="GeneID:498909"
                     /db_xref="RGD:1586040"
ORIGIN      
        1 maataavsgv lrrlgwrllq lrclpvarcq splmprafht avgfrsseeq rqqpphssqq
       61 hsetqgpefs rppprytdqs geeeedyese eqiqhrilta alefvpdhgw taeaiaegaq
      121 slglssaaas mfgsdgseli lhfvtqcnar lnhvleeeqk lvqlgqaekr ktdqflrdav
      181 etrlrmlipy iehwpralsi lllpqnipps lslltsmvdd mwhyagdqst dfnwytrrav
      241 lagiynttel vmmqdsspdf edtwrfldnr indamnmght akqvkstgea lvqglmgaav
      301 tlknltglnq rr
//
LOCUS       NP_445950                455 aa            linear   ROD 27-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 6 [Rattus
            norvegicus].
ACCESSION   NP_445950
VERSION     NP_445950.1
DBSOURCE    REFSEQ: accession NM_053498.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   O'Keeffe,M.G., Thorne,P.R., Housley,G.D., Robson,S.C. and
            Vlajkovic,S.M.
  TITLE     Hair cell specific NTPDase6 immunolocalisation in vestibular end
            organs: potential role of purinergic signaling in vestibular
            sensory transduction
  JOURNAL   J Vestib Res 22 (5-6), 213-219 (2012)
   PUBMED   23302703
  REMARK    GeneRIF: NTPDase6 immunolocalisation in the vestibular end organ
            could be linked to the regulation of P2 receptor signalling and
            sensory transduction, including maintenance of vestibular hair
            bundles.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Ivanenkov,V.V., Murphy-Piedmonte,D.M. and Kirley,T.L.
  TITLE     Bacterial expression, characterization, and disulfide bond
            determination of soluble human NTPDase6 (CD39L2) nucleotidase:
            implications for structure and function
  JOURNAL   Biochemistry 42 (40), 11726-11735 (2003)
   PUBMED   14529283
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Hicks-Berger,C.A., Chadwick,B.P., Frischauf,A.M. and Kirley,T.L.
  TITLE     Expression and characterization of soluble and membrane-bound human
            nucleoside triphosphate diphosphohydrolase 6 (CD39L2)
  JOURNAL   J Biol Chem 275 (44), 34041-34045 (2000)
   PUBMED   10948193
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Braun,N., Fengler,S., Ebeling,C., Servos,J. and Zimmermann,H.
  TITLE     Sequencing, functional expression and characterization of rat
            NTPDase6, a nucleoside diphosphatase and novel member of the
            ecto-nucleoside triphosphate diphosphohydrolase family
  JOURNAL   Biochem J 351 Pt 3 (Pt 3), 639-647 (2000)
   PUBMED   11042118
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ277748.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ277748.1, SRR8487231.76011.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132287, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..455
                     /product="ectonucleoside triphosphate diphosphohydrolase
                     6"
                     /EC_number="3.6.1.6"
                     /function="ecto-nucleoside triphosphate
                     diphosphohydrolase"
                     /note="NTPDase 6; CD39 antigen-like 2"
                     /calculated_mol_wt=49768
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ER31.1)"
     Region          72..444
                     /region_name="ASKHA_NBD_NTPDase6"
                     /note="nucleotide-binding domain (NBD) of ectonucleoside
                     triphosphate diphosphohydrolase 6 (NTPDase6) and similar
                     proteins; cd24115"
                     /db_xref="CDD:466965"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ER31.1)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ER31.1)"
     CDS             1..455
                     /gene="Entpd6"
                     /coded_by="NM_053498.1:129..1496"
                     /db_xref="GeneID:85260"
                     /db_xref="RGD:619725"
ORIGIN      
        1 mrkipnhgtl rmtkvayplg lcvglfiyva yikwhrasaa qafftiagaa sgvrwtqqaf
       61 sspdsatrgh evfygimfda gstgtrihvf qfarppgetp tlthetfkal kpglsayadd
      121 veksaqgiqe llnvakqhip ydfwkatplv lkataglrll pgekaqkllq kvkevfkasp
      181 flvgddcvsi mngtdegvsa witvnfltgs lktpgsssvg mldlgggstq itflprvegt
      241 lqasppghlt alqmfnrtfk lysysylglg lmsarlailg gvegkpaedd kelvspclsp
      301 rfrgkwehae vtyrisgqka vglyelcasr vsevlrnkvh rteeaqhvdf yafsyyydla
      361 asfglidaek ggslvvgdfe iaakyvcrtl etqppsspfa cmdltyisll lhefgfpgdk
      421 vlklarkidn vetswalgai fhyidslkrq kvpal
//
LOCUS       NP_077373                481 aa            linear   ROD 27-APR-2025
DEFINITION  abl interactor 1 [Rattus norvegicus].
ACCESSION   NP_077373 XP_346506
VERSION     NP_077373.2
DBSOURCE    REFSEQ: accession NM_024397.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Chazeau,A., Mehidi,A., Nair,D., Gautier,J.J., Leduc,C., Chamma,I.,
            Kage,F., Kechkar,A., Thoumine,O., Rottner,K., Choquet,D.,
            Gautreau,A., Sibarita,J.B. and Giannone,G.
  TITLE     Nanoscale segregation of actin nucleation and elongation factors
            determines dendritic spine protrusion
  JOURNAL   EMBO J 33 (23), 2745-2764 (2014)
   PUBMED   25293574
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Jia,J.M., Hu,Z., Nordman,J. and Li,Z.
  TITLE     The schizophrenia susceptibility gene dysbindin regulates dendritic
            spine dynamics
  JOURNAL   J Neurosci 34 (41), 13725-13736 (2014)
   PUBMED   25297099
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Verpelli,C., Dvoretskova,E., Vicidomini,C., Rossi,F.,
            Chiappalone,M., Schoen,M., Di Stefano,B., Mantegazza,R.,
            Broccoli,V., Bockers,T.M., Dityatev,A. and Sala,C.
  TITLE     Importance of Shank3 protein in regulating metabotropic glutamate
            receptor 5 (mGluR5) expression and signaling at synapses
  JOURNAL   J Biol Chem 286 (40), 34839-34850 (2011)
   PUBMED   21795692
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Proepper,C., Steinestel,K., Schmeisser,M.J., Heinrich,J.,
            Steinestel,J., Bockmann,J., Liebau,S. and Boeckers,T.M.
  TITLE     Heterogeneous nuclear ribonucleoprotein k interacts with Abi-1 at
            postsynaptic sites and modulates dendritic spine morphology
  JOURNAL   PLoS One 6 (11), e27045 (2011)
   PUBMED   22102872
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Garcia-Garcia,M.J., Eggenschwiler,J.T., Caspary,T., Alcorn,H.L.,
            Wyler,M.R., Huangfu,D., Rakeman,A.S., Lee,J.D., Feinberg,E.H.,
            Timmer,J.R. and Anderson,K.V.
  TITLE     Analysis of mouse embryonic patterning and morphogenesis by forward
            genetics
  JOURNAL   Proc Natl Acad Sci U S A 102 (17), 5913-5919 (2005)
   PUBMED   15755804
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Tani,K., Sato,S., Sukezane,T., Kojima,H., Hirose,H., Hanafusa,H.
            and Shishido,T.
  TITLE     Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
            enabled (Mena) by c-Abl kinase
  JOURNAL   J Biol Chem 278 (24), 21685-21692 (2003)
   PUBMED   12672821
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Stradal,T., Courtney,K.D., Rottner,K., Hahne,P., Small,J.V. and
            Pendergast,A.M.
  TITLE     The Abl interactor proteins localize to sites of actin
            polymerization at the tips of lamellipodia and filopodia
  JOURNAL   Curr Biol 11 (11), 891-895 (2001)
   PUBMED   11516653
REFERENCE   9  (residues 1 to 481)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   10 (residues 1 to 481)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB725283.1 and BC129092.1.
            
            On Mar 8, 2007 this sequence version replaced NP_077373.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129092.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..481
                     /product="abl interactor 1"
                     /note="abi-1; abelson interactor 1; eps8-binding protein;
                     eps8 SH3 domain-binding protein; eps8 binding protein
                     (e3B1), alternatively spliced"
                     /calculated_mol_wt=52201
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17304222; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8CBW3; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Region          317..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Region          361..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Region          423..481
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(428,430,433,437,455..456,469,471..472)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8CBW3; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZP0; propagated from
                     UniProtKB/Swiss-Prot (Q9QZM5.3)"
     CDS             1..481
                     /gene="Abi1"
                     /gene_synonym="E3b1"
                     /coded_by="NM_024397.2:65..1510"
                     /db_xref="GeneID:79249"
                     /db_xref="RGD:621008"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkwlkakh gnnqpartgt lsrtnpptqk
      181 ppsppvsgrg tlgrntpykt lepvkpptvp ndymtsparl gsqhspgrta slnqrprths
      241 gssggsgsre nsgsssigip iavptpsppt agpaapgaap gsqygtmtrq isrhnsttss
      301 tssggyrrtp svtaqfsaqp hvnggplysq nsisiapppp pmpqltpqip ltgfvarvqe
      361 niadsptppp ppppddipmf ddsppppppp pvdyedeeaa vvqysdpyad gdpawapkny
      421 iekvvaiydy tkdkddelsf kegaiiyvik knddgwfegv cnrvtglfpg nyvesimhyt
      481 d
//
LOCUS       NP_001004284             440 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger MYND domain-containing protein 10 [Rattus norvegicus].
ACCESSION   NP_001004284 XP_343477
VERSION     NP_001004284.1
DBSOURCE    REFSEQ: accession NM_001004284.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Mali,G.R., Yeyati,P.L., Mizuno,S., Dodd,D.O., Tennant,P.A.,
            Keighren,M.A., Zur Lage,P., Shoemark,A., Garcia-Munoz,A.,
            Shimada,A., Takeda,H., Edlich,F., Takahashi,S., von Kreigsheim,A.,
            Jarman,A.P. and Mill,P.
  TITLE     ZMYND10 functions in a chaperone relay during axonemal dynein
            assembly
  JOURNAL   Elife 7, e34389 (2018)
   PUBMED   29916806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Cho,K.J., Noh,S.H., Han,S.M., Choi,W.I., Kim,H.Y., Yu,S., Lee,J.S.,
            Rim,J.H., Lee,M.G., Hildebrandt,F. and Gee,H.Y.
  TITLE     ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic
            pre-assembly of dynein arms
  JOURNAL   PLoS Genet 14 (3), e1007316 (2018)
   PUBMED   29601588
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Moore,D.J., Onoufriadis,A., Shoemark,A., Simpson,M.A., zur
            Lage,P.I., de Castro,S.C., Bartoloni,L., Gallone,G., Petridi,S.,
            Woollard,W.J., Antony,D., Schmidts,M., Didonna,T.,
            Makrythanasis,P., Bevillard,J., Mongan,N.P., Djakow,J., Pals,G.,
            Lucas,J.S., Marthin,J.K., Nielsen,K.G., Santoni,F., Guipponi,M.,
            Hogg,C., Antonarakis,S.E., Emes,R.D., Chung,E.M., Greene,N.D.,
            Blouin,J.L., Jarman,A.P. and Mitchison,H.M.
  TITLE     Mutations in ZMYND10, a gene essential for proper axonemal assembly
            of inner and outer dynein arms in humans and flies, cause primary
            ciliary dyskinesia
  JOURNAL   Am J Hum Genet 93 (2), 346-356 (2013)
   PUBMED   23891471
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Zariwala,M.A., Gee,H.Y., Kurkowiak,M., Al-Mutairi,D.A., Leigh,M.W.,
            Hurd,T.W., Hjeij,R., Dell,S.D., Chaki,M., Dougherty,G.W., Adan,M.,
            Spear,P.C., Esteve-Rudd,J., Loges,N.T., Rosenfeld,M., Diaz,K.A.,
            Olbrich,H., Wolf,W.E., Sheridan,E., Batten,T.F., Halbritter,J.,
            Porath,J.D., Kohl,S., Lovric,S., Hwang,D.Y., Pittman,J.E.,
            Burns,K.A., Ferkol,T.W., Sagel,S.D., Olivier,K.N., Morgan,L.C.,
            Werner,C., Raidt,J., Pennekamp,P., Sun,Z., Zhou,W., Airik,R.,
            Natarajan,S., Allen,S.J., Amirav,I., Wieczorek,D., Landwehr,K.,
            Nielsen,K., Schwerk,N., Sertic,J., Kohler,G., Washburn,J., Levy,S.,
            Fan,S., Koerner-Rettberg,C., Amselem,S., Williams,D.S.,
            Mitchell,B.J., Drummond,I.A., Otto,E.A., Omran,H., Knowles,M.R. and
            Hildebrandt,F.
  TITLE     ZMYND10 is mutated in primary ciliary dyskinesia and interacts with
            LRRC6
  JOURNAL   Am J Hum Genet 93 (2), 336-345 (2013)
   PUBMED   23891469
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079255.1.
            
            On Sep 10, 2004 this sequence version replaced XP_343477.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..440
                     /product="zinc finger MYND domain-containing protein 10"
                     /note="zinc finger, MYND domain-containing 10"
                     /calculated_mol_wt=50545
     Region          394..430
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..440
                     /gene="Zmynd10"
                     /coded_by="NM_001004284.1:104..1426"
                     /db_xref="GeneID:363139"
                     /db_xref="RGD:1303250"
ORIGIN      
        1 mgdlelllpg eaevlvqglh sfqlremgse gwskqhenle klnmqailda tvsqaepiqe
       61 llvthgkipt lveeliavem wkqkvfpvlc rledfkpqnt fpiymvvhhe asiinlletv
      121 ffhkevcesa ddtvldlvdy chrklillva rkgggdlsee erfqdstpmq elqkqaemme
      181 feislkalsv lryitdcmds lslstlnrml tthnlpcllv ellehspwsr reggklqhfe
      241 sgrwqtvaps ehqklnkldg qvwialynll lspeartryc ltnfakgqll klqafltdtl
      301 ldqlpnladl ksflahlalv etqppkkdlv leqipeiwdr lerenkgkwq aiakhqlqhv
      361 fslsekdlrq qaqrwaetyr ldvleavape rprcaycsae askrcsrcqk vwyccrecqv
      421 khwekhgktc vlaaqgdrak
//
LOCUS       NP_001004267             275 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 106B [Rattus norvegicus].
ACCESSION   NP_001004267 XP_231500
VERSION     NP_001004267.1
DBSOURCE    REFSEQ: accession NM_001004267.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Zhou,X., Sun,L., Bastos de Oliveira,F., Qi,X., Brown,W.J.,
            Smolka,M.B., Sun,Y. and Hu,F.
  TITLE     Prosaposin facilitates sortilin-independent lysosomal trafficking
            of progranulin
  JOURNAL   J Cell Biol 210 (6), 991-1002 (2015)
   PUBMED   26370502
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Stagi,M., Klein,Z.A., Gould,T.J., Bewersdorf,J. and
            Strittmatter,S.M.
  TITLE     Lysosome size, motility and stress response regulated by
            fronto-temporal dementia modifier TMEM106B
  JOURNAL   Mol Cell Neurosci 61, 226-240 (2014)
   PUBMED   25066864
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Schwenk,B.M., Lang,C.M., Hogl,S., Tahirovic,S., Orozco,D.,
            Rentzsch,K., Lichtenthaler,S.F., Hoogenraad,C.C., Capell,A.,
            Haass,C. and Edbauer,D.
  TITLE     The FTLD risk factor TMEM106B and MAP6 control dendritic
            trafficking of lysosomes
  JOURNAL   EMBO J 33 (5), 450-467 (2014)
   PUBMED   24357581
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079127.1.
            
            On Sep 10, 2004 this sequence version replaced XP_231500.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079127.1, EV769119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q21"
     Protein         1..275
                     /product="transmembrane protein 106B"
                     /calculated_mol_wt=31021
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Region          28..259
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUM4; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYA5.1)"
     CDS             1..275
                     /gene="Tmem106b"
                     /gene_synonym="LRRGT00101"
                     /coded_by="NM_001004267.1:122..949"
                     /db_xref="GeneID:312132"
                     /db_xref="RGD:1303037"
ORIGIN      
        1 mgkslshlpl hsnkedgydg vtstdnmrng lvssevrned grsgdvsqfp yveftgrdsv
       61 tcptcqgtgr iprgqenqlv alipysdqrl rprrtklyvm asvfvcllls glavfflfpr
      121 sidvkyigvk sayvsydsqk rmiylnitnt lnitnnnyys vevenitaqv qfsktvigka
      181 rlsnitnigp ldmkqidytv ptviaeemsy mydfctlpsi kvhnivlmmq vtvttayfgh
      241 seqisqeryq yvdcgrntty qlaqseylnv lqpqq
//
LOCUS       NP_001071149             253 aa            linear   ROD 27-APR-2025
DEFINITION  testis-expressed protein 47 [Rattus norvegicus].
ACCESSION   NP_001071149 XP_001063160 XP_575348
VERSION     NP_001071149.1
DBSOURCE    REFSEQ: accession NM_001077681.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127528.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_575348.1, XP_001063160.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127528.1, CK653310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..253
                     /product="testis-expressed protein 47"
                     /note="uncharacterized protein C7orf62 homolog"
                     /calculated_mol_wt=29470
     CDS             1..253
                     /gene="Tex47"
                     /gene_synonym="RGD1564345"
                     /coded_by="NM_001077681.1:94..855"
                     /db_xref="GeneID:499993"
                     /db_xref="RGD:1564345"
ORIGIN      
        1 msfivhnrrs skkqfqvdpl lmpkvpriny lhiqeekhrl qlkkfllhrl flvgyiqant
       61 ekkeiseyye qlfqsilkhh lgevvtglfl iypssflhil essngtlfri lldyvaheks
      121 erefmiqnmk iivashnipt rlfmqwhisi ikvpvlyldd dtqsqsveev ttdfltlthk
      181 lalhlyktvk lggkgpgdnl hqlapelilp ektikylcka tefmdpasfl smynrpihit
      241 mdsdivwpap srf
//
LOCUS       NP_001120813             487 aa            linear   ROD 27-APR-2025
DEFINITION  tumor protein 63 isoform c [Rattus norvegicus].
ACCESSION   NP_001120813
VERSION     NP_001120813.1
DBSOURCE    REFSEQ: accession NM_001127341.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Wang,Y., Wu,W., Zhu,M., Wang,C., Shen,W., Cheng,Y., Geng,L., Li,Z.,
            Zhang,J., Dai,J., Ma,H., Chen,L., Hu,Z., Jin,G. and Shen,H.
  TITLE     Integrating expression-related SNPs into genome-wide gene- and
            pathway-based analyses identified novel lung cancer susceptibility
            genes
  JOURNAL   Int J Cancer 142 (8), 1602-1610 (2018)
   PUBMED   29193083
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Liao,W., Liu,H., Zhang,Y., Jung,J.H., Chen,J., Su,X., Kim,Y.C.,
            Flores,E.R., Wang,S.M., Czarny-Ratajczak,M., Li,W., Zeng,S.X. and
            Lu,H.
  TITLE     Ccdc3: A New P63 Target Involved in Regulation Of Liver Lipid
            Metabolism
  JOURNAL   Sci Rep 7 (1), 9020 (2017)
   PUBMED   28827783
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Alves,L.U., Pardono,E., Otto,P.A. and Mingroni Netto,R.C.
  TITLE     A novel c.1037C > G (p.Ala346Gly) mutation in TP63 as cause of the
            ectrodactyly-ectodermal dysplasia and cleft lip/palate (EEC)
            syndrome
  JOURNAL   Genet Mol Biol 38 (1), 37-41 (2015)
   PUBMED   25983622
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Eisenkraft,A., Pode-Shakked,B., Goldstein,N., Shpirer,Z., van
            Bokhoven,H. and Anikster,Y.
  TITLE     Clinical Variability in a Family with an Ectodermal Dysplasia
            Syndrome and a Nonsense Mutation in the TP63 Gene
  JOURNAL   Fetal Pediatr Pathol 34 (6), 400-406 (2015)
   PUBMED   26470833
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Bamberger,C. and Schmale,H.
  TITLE     Identification and tissue distribution of novel KET/p63 splice
            variants
  JOURNAL   FEBS Lett 501 (2-3), 121-126 (2001)
   PUBMED   11470269
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Davison,T.S., Vagner,C., Kaghad,M., Ayed,A., Caput,D. and
            Arrowsmith,C.H.
  TITLE     p73 and p63 are homotetramers capable of weak heterotypic
            interactions with each other but not with p53
  JOURNAL   J Biol Chem 274 (26), 18709-18714 (1999)
   PUBMED   10373484
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Yang,A., Schweitzer,R., Sun,D., Kaghad,M., Walker,N., Bronson,R.T.,
            Tabin,C., Sharpe,A., Caput,D., Crum,C. and McKeon,F.
  TITLE     p63 is essential for regenerative proliferation in limb,
            craniofacial and epithelial development
  JOURNAL   Nature 398 (6729), 714-718 (1999)
   PUBMED   10227294
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Mills,A.A., Zheng,B., Wang,X.J., Vogel,H., Roop,D.R. and Bradley,A.
  TITLE     p63 is a p53 homologue required for limb and epidermal
            morphogenesis
  JOURNAL   Nature 398 (6729), 708-713 (1999)
   PUBMED   10227293
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Yang,A., Kaghad,M., Wang,Y., Gillett,E., Fleming,M.D., Dotsch,V.,
            Andrews,N.C., Caput,D. and McKeon,F.
  TITLE     p63, a p53 homolog at 3q27-29, encodes multiple products with
            transactivating, death-inducing, and dominant-negative activities
  JOURNAL   Mol Cell 2 (3), 305-316 (1998)
   PUBMED   9774969
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Schmale,H. and Bamberger,C.
  TITLE     A novel protein with strong homology to the tumor suppressor p53
  JOURNAL   Oncogene 15 (11), 1363-1367 (1997)
   PUBMED   9315105
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y10258.2 and AJ277449.1.
            
            Summary: This gene encodes tumor protein p63, a member of the p53
            family of transcription factors involved in cellular responses to
            stress and development. The family members include p53, p63, and
            p73, which have high sequence similarity to one another. This
            similarity allows p63 and p73 to transactivate p53-responsive genes
            causing cell cycle arrest and apoptosis. The family members can
            interact with each other in many ways, including direct and
            indirect protein interactions. This results in mutual regulation of
            target gene promoters. Both alternative splicing and the use of
            alternative promoters result in multiple transcript variants
            encoding different protein isoforms.[provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (3) lacks several 3' exons but has
            an alternate 3' exon, as compared to variant 1. The resulting
            isoform (c, also known as TA2KETgamma) has a shorter and different
            C-terminus, as compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ277449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..487
                     /product="tumor protein 63 isoform c"
                     /note="tumor protein 63 kDa; transformation related
                     protein 63; keratinocyte transcription factor KET"
                     /calculated_mol_wt=55368
     Region          1..107
                     /region_name="Transcription activation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJP6.1)"
     Region          122..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJP6.1)"
     Region          177..358
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(244,247,308,312)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(245..247,249)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(309,311,318,343,345..347,350)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          351..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJP6.1)"
     Region          352..388
                     /region_name="Interaction with HIPK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJP6.1)"
     Region          391..431
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     Region          394..443
                     /region_name="Oligomerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJP6.1)"
     CDS             1..487
                     /gene="Tp63"
                     /gene_synonym="Ket; P73l; Tp73l; Trp63"
                     /coded_by="NM_001127341.1:148..1611"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:246334"
                     /db_xref="RGD:620863"
ORIGIN      
        1 mnfetsrcat lqycpdpyiq rfietpshfs wkesyyrsam sqstqtsefl spevfqhiwd
       61 fleqpicsvq pidlnfvdep sengatnkie ismdcirmqd sdlsdpmwpq ytnlgllngm
      121 dqqiqngsss tspyntdhaq nsvtapspya qpsstfdals pspaipsntd ypgphsfdvs
      181 fqqsstaksa twtystelkk lycqiaktcp iqikvmtppp qgavirampv ykkaehvtev
      241 vkrcpnhels refnegqiap pshlirvegn shaqyvedpi tgrqsvlvpy eppqvgteft
      301 tvlynfmcns scvggmnrrp iliivtletr dgqvlgrrcf earicacpgr drkadedsir
      361 kqqvsdsakn gdgtkrpfrq nthgiqmtsi kkrrspddel lylpvrgret yemllkikes
      421 lelmqylpqh tietyrqqqq qqhqhllqkh llsacfrnel vesrreaptq sdvffrhsnp
      481 pnhsvyp
//
LOCUS       NP_446258                313 aa            linear   ROD 27-APR-2025
DEFINITION  potassium channel subfamily K member 6 [Rattus norvegicus].
ACCESSION   NP_446258 XP_215230
VERSION     NP_446258.2
DBSOURCE    REFSEQ: accession NM_053806.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Bobak,N., Feliciangeli,S., Chen,C.C., Ben Soussia,I., Bittner,S.,
            Pagnotta,S., Ruck,T., Biel,M., Wahl-Schott,C., Grimm,C., Meuth,S.G.
            and Lesage,F.
  TITLE     Recombinant tandem of pore-domains in a Weakly Inward rectifying K+
            channel 2 (TWIK2) forms active lysosomal channels
  JOURNAL   Sci Rep 7 (1), 649 (2017)
   PUBMED   28381826
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Lloyd,E.E., Pandit,L.M., Crossland,R.F., Marrelli,S.P. and
            Bryan,R.M. Jr.
  TITLE     Endothelium-dependent relaxations in the aorta from K(2p)6.1
            knockout mice
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 305 (1), R60-R67 (2013)
   PUBMED   23637138
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Buga,A.M., Scholz,C.J., Kumar,S., Herndon,J.G., Alexandru,D.,
            Cojocaru,G.R., Dandekar,T. and Popa-Wagner,A.
  TITLE     Identification of new therapeutic targets by genome-wide analysis
            of gene expression in the ipsilateral cortex of aged rats after
            stroke
  JOURNAL   PLoS One 7 (12), e50985 (2012)
   PUBMED   23251410
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Lloyd,E.E., Crossland,R.F., Phillips,S.C., Marrelli,S.P.,
            Reddy,A.K., Taffet,G.E., Hartley,C.J. and Bryan,R.M. Jr.
  TITLE     Disruption of K(2P)6.1 produces vascular dysfunction and
            hypertension in mice
  JOURNAL   Hypertension 58 (4), 672-678 (2011)
   PUBMED   21876070
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Lloyd,E.E., Marrelli,S.P. and Bryan,R.M. Jr.
  TITLE     cGMP does not activate two-pore domain K+ channels in
            cerebrovascular smooth muscle
  JOURNAL   Am J Physiol Heart Circ Physiol 296 (6), H1774-H1780 (2009)
   PUBMED   19363137
  REMARK    GeneRIF: Although K(2P) channels are highly expressed, K(2P)
            currents are not activated via the NO/cGMP pathway in rat middle
            cerebral artery smooth muscle, despite the presence of numerous
            putative PKG phosphorylation sites
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Popper,P., Winkler,J., Erbe,C.B., Lerch-Gaggl,A., Siebeneich,W. and
            Wackym,P.A.
  TITLE     Distribution of two-pore-domain potassium channels in the adult rat
            vestibular periphery
  JOURNAL   Hear Res 246 (1-2), 1-8 (2008)
   PUBMED   18838117
  REMARK    GeneRIF: K(2P)6.1 (TWIK 2) immunoreactivity was detected in nerve
            terminals, blood vessels hair cells and transitional cells of the
            crista ampullaris and in the somata and neuron fibers of Scarpa's
            ganglia.
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Patel,A.J., Maingret,F., Magnone,V., Fosset,M., Lazdunski,M. and
            Honore,E.
  TITLE     TWIK-2, an inactivating 2P domain K+ channel
  JOURNAL   J Biol Chem 275 (37), 28722-28730 (2000)
   PUBMED   10887187
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF281304.1, JAXUCZ010000001.1 and BF405813.1.
            
            On Oct 11, 2007 this sequence version replaced NP_446258.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.436353.1, AF281304.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840110,
                                           SAMN16676789 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..313
                     /product="potassium channel subfamily K member 6"
                     /note="potassium inwardly-rectifying channel, subfamily K,
                     member 6; potassium channel, two pore domain subfamily K,
                     member 6; potassium channel, subfamily K, member 6;
                     potassium channel subfamily K member 6-like"
                     /calculated_mol_wt=34052
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc) asparagine.
                     /evidence=ECO:0000269|PubMed:28381826; propagated from
                     UniProtKB/Swiss-Prot (G3V8R8.1)"
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc) asparagine.
                     /evidence=ECO:0000269|PubMed:28381826; propagated from
                     UniProtKB/Swiss-Prot (G3V8R8.1)"
     Region          <89..146
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          106..111
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Region          180..259
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          214..219
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:P57789"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Region          282..290
                     /region_name="Lysosomal targeting signal.
                     /evidence=ECO:0000269|PubMed:28381826"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     Region          308..312
                     /region_name="Lysosomal targeting signal.
                     /evidence=ECO:0000269|PubMed:28381826"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8R8.1)"
     CDS             1..313
                     /gene="Kcnk6"
                     /gene_synonym="Twik-2; Twik2"
                     /coded_by="NM_053806.2:1..942"
                     /db_xref="GeneID:116491"
                     /db_xref="RGD:621450"
ORIGIN      
        1 mrrgallasa lvayagylal gallvarler phearlrael gtlreqllrh spcvaahald
       61 afvervlaag rlgravlana sgpanasdpa wdfasalffa stlvttvgyg yttpltdagk
      121 afsivfallg vpitmlllta saqrlslllt haplswlslr wgwhpqraar whlvallmvi
      181 vaifflipaa vfayleeaws fldafyfcfi slstiglgdy vpgeapgqpy rslykvlvta
      241 ylflglvamv lvlqtfrrvs dlhgltelil lpdpdparlh qdeddqvdil dartdlhqhl
      301 saashanyas ipr
//
LOCUS       NP_062123                895 aa            linear   ROD 27-APR-2025
DEFINITION  ral guanine nucleotide dissociation stimulator isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_062123 XP_001079127
VERSION     NP_062123.2
DBSOURCE    REFSEQ: accession NM_019250.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Kawai,M., Kawashima,S., Sakoda,T., Toh,R., Kikuchi,A.,
            Yamauchi-Takihara,K., Kunisada,K. and Yokoyama,M.
  TITLE     Ral GDP dissociation stimulator and Ral GTPase are involved in
            myocardial hypertrophy
  JOURNAL   Hypertension 41 (4), 956-962 (2003)
   PUBMED   12642511
  REMARK    GeneRIF: Ral GDP dissociation stimulator is involved in myocardial
            hypertrophy.
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Huang,L., Weng,X., Hofer,F., Martin,G.S. and Kim,S.H.
  TITLE     Three-dimensional structure of the Ras-interacting domain of RalGDS
  JOURNAL   Nat Struct Biol 4 (8), 609-615 (1997)
   PUBMED   9253406
  REMARK    Erratum:[Nat Struct Biol 1997 Oct;4(10):840]
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Hofer,F., Fields,S., Schneider,C. and Martin,G.S.
  TITLE     Activated Ras interacts with the Ral guanine nucleotide
            dissociation stimulator
  JOURNAL   Proc Natl Acad Sci U S A 91 (23), 11089-11093 (1994)
   PUBMED   7972015
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Albright,C.F., Giddings,B.W., Liu,J., Vito,M. and Weinberg,R.A.
  TITLE     Characterization of a guanine nucleotide dissociation stimulator
            for a ras-related GTPase
  JOURNAL   EMBO J 12 (1), 339-347 (1993)
   PUBMED   8094051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L07925.1, JAXUCZ010000003.1, CB775259.1 and CO561927.1.
            
            On Oct 20, 2007 this sequence version replaced NP_062123.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.12879.1,
                                           SRR26643429.10920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..895
                     /product="ral guanine nucleotide dissociation stimulator
                     isoform 1"
                     /note="ralGEF; ral guanine nucleotide exchange factor"
                     /calculated_mol_wt=98659
     Region          112..236
                     /region_name="RasGEFN"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal motif; smart00229"
                     /db_xref="CDD:214571"
     Site            order(131,179,183..184,187,190..191,228..229,232,239)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:100121"
     Region          <241..>348
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          301..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03386.1)"
     Region          363..625
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases. Small GTP-binding proteins of the Ras
                     superfamily function as molecular switches in fundamental
                     events such as signal transduction, cytoskeleton dynamics
                     and intracellular trafficking; cd00155"
                     /db_xref="CDD:238087"
     Site            order(396..398,411..412,414..416,418..419,422..423,426,
                     461,464..465,467..469,471..474,476..477,497,500,505..507,
                     510,547..549,552..554,556..558,560..563,578,582,617,
                     620..621)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          708..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03386.1)"
     Region          779..864
                     /region_name="RA_RalGDS"
                     /note="Ras-associating (RA) domain found in Ral guanine
                     nucleotide dissociation stimulator (RalGDS) and similar
                     proteins; cd17209"
                     /db_xref="CDD:340729"
     Site            order(779..782,784,791..799,803..804,812,815..816,818)
                     /site_type="other"
                     /note="RA-Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340729"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q12967; propagated from
                     UniProtKB/Swiss-Prot (Q03386.1)"
     CDS             1..895
                     /gene="Ralgds"
                     /gene_synonym="Rgds"
                     /coded_by="NM_019250.2:202..2889"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29622"
                     /db_xref="RGD:3533"
ORIGIN      
        1 mvqrmwaeas gpiggaeplf pgsrrsrsvw davrlevgvp dscpvvlhsf tqldpdlprl
       61 esstqeigee lingviysis lrkvqlhpga tkgqrwlgce nesalnlyet ckvrtvkagt
      121 leklvehlvp afqgsdlsyv tvflctyraf tttqqvldll fkrygcilpy ssedggpqdq
      181 lknaissilg twldqysedf cqppdfpclk qlvayvqlnm pgsdlerrah lllaqledle
      241 psevepeals papvlslkpa sqlepapall ltpsravast pvrepapvpv lasspvvapa
      301 selepalepp ldpeptlapa peldptvsqs lhlepapvpa palepswplp ettenglcak
      361 phlllfppdl vaeqftlmda elfkkvvpyh clgsiwsqrd kkgkehlapt iratvaqfnn
      421 vancvittcl gdqsmkasdr arvvehwiev arecrvlknf sslyailsal qsnaihrlkk
      481 tweevsrgsf rvfqklseif sdennyslsr ellikegtsk fatlemnprr tqrrqketgv
      541 iqgtvpylgt fltdlvmldt amkdylygrl infekrrkef eviaqikllq sacnnysivp
      601 eehfgawfra mgrlseaesy nlscelepps esasntlrsk kstaivkrws drqapstels
      661 tsssahsksc dqlrcspyls sgditdalsv hsagssssdv eeinmsfvpe spdgqekkfw
      721 esasqsspet sgissassst ssssasttpv sttrthkrsv sgvcsysssl plynqqvgdc
      781 ciirvsldvd ngnmyksilv tsqdkaptvi rkamdkhnld edepedyell qiisedhklk
      841 ipenanvfya mnsaanydfi lkkraftkga kvkhgasstl prmkqkglri argif
//
LOCUS       NP_072121                145 aa            linear   ROD 27-APR-2025
DEFINITION  synaptojanin-2-binding protein [Rattus norvegicus].
ACCESSION   NP_072121
VERSION     NP_072121.2
DBSOURCE    REFSEQ: accession NM_022599.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Adam,M.G., Berger,C., Feldner,A., Yang,W.J., Wustehube-Lausch,J.,
            Herberich,S.E., Pinder,M., Gesierich,S., Hammes,H.P., Augustin,H.G.
            and Fischer,A.
  TITLE     Synaptojanin-2 binding protein stabilizes the Notch ligands DLL1
            and DLL4 and inhibits sprouting angiogenesis
  JOURNAL   Circ Res 113 (11), 1206-1218 (2013)
   PUBMED   24025447
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Serasinghe,M.N. and Yoon,Y.
  TITLE     The mitochondrial outer membrane protein hFis1 regulates
            mitochondrial morphology and fission through self-interaction
  JOURNAL   Exp Cell Res 314 (19), 3494-3507 (2008)
   PUBMED   18845145
  REMARK    Erratum:[Exp Cell Res. 2009 Mar 10;315(5):899]
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Liu,Z.H., Tsuchida,K., Matsuzaki,T., Bao,Y.L., Kurisaki,A. and
            Sugino,H.
  TITLE     Characterization of isoforms of activin receptor-interacting
            protein 2 that augment activin signaling
  JOURNAL   J Endocrinol 189 (2), 409-421 (2006)
   PUBMED   16648306
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Cestra,G., Toomre,D., Chang,S. and De Camilli,P.
  TITLE     The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of
            multiple regulatory mechanisms converging on the actin cytoskeleton
  JOURNAL   Proc Natl Acad Sci U S A 102 (5), 1731-1736 (2005)
   PUBMED   15659545
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Matsuzaki,T., Hanai,S., Kishi,H., Liu,Z., Bao,Y., Kikuchi,A.,
            Tsuchida,K. and Sugino,H.
  TITLE     Regulation of endocytosis of activin type II receptors by a novel
            PDZ protein through Ral/Ral-binding protein 1-dependent pathway
  JOURNAL   J Biol Chem 277 (21), 19008-19018 (2002)
   PUBMED   11882656
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Nemoto,Y., Wenk,M.R., Watanabe,M., Daniell,L., Murakami,T.,
            Ringstad,N., Yamada,H., Takei,K. and De Camilli,P.
  TITLE     Identification and characterization of a synaptojanin 2 splice
            isoform predominantly expressed in nerve terminals
  JOURNAL   J Biol Chem 276 (44), 41133-41142 (2001)
   PUBMED   11498538
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Nemoto,Y. and De Camilli,P.
  TITLE     Recruitment of an alternatively spliced form of synaptojanin 2 to
            mitochondria by the interaction with the PDZ domain of a
            mitochondrial outer membrane protein
  JOURNAL   EMBO J 18 (11), 2991-3006 (1999)
   PUBMED   10357812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF260258.1 and JAXUCZ010000006.1.
            
            On Oct 14, 2005 this sequence version replaced NP_072121.1.
            
            Sequence Note: This RefSeq record was created using sequences from
            two different strains, Sprague-Dawley and BN/SsNHsdMCW, because no
            single transcript from the same strain was available for the full
            length of the gene.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF260258.1, SRR26643294.26152.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..145
                     /product="synaptojanin-2-binding protein"
                     /note="NPW16; mitochondrial outer membrane protein 25"
                     /calculated_mol_wt=15694
     Region          12..97
                     /region_name="PDZ_SYNJ2BP-like"
                     /note="PDZ domain of synaptojanin-2-binding protein
                     (SYNJ2BP), and related domains; cd06709"
                     /db_xref="CDD:467193"
     Site            order(22..28,45,48,78,82,85..86)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467193"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVJ4.2)"
     CDS             1..145
                     /gene="Synj2bp"
                     /gene_synonym="Omp25"
                     /coded_by="NM_022599.2:85..522"
                     /db_xref="GeneID:64531"
                     /db_xref="RGD:69400"
ORIGIN      
        1 mngrvdylvs eeeinltrgp sglgfnivgg tdqqyvsnds giyvsriked gaaardgrlq
       61 egdkilsvng qdlknllhqd avdlfrnagy avslrvqhrl pvqngpivhr gdgepsgvpv
      121 avvllpvfal tlvavwafvr yrkql
//
LOCUS       NP_001005871            1169 aa            linear   ROD 27-APR-2025
DEFINITION  plasma membrane calcium-transporting ATPase 4 [Rattus norvegicus].
ACCESSION   NP_001005871 XP_341123
VERSION     NP_001005871.1
DBSOURCE    REFSEQ: accession NM_001005871.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1169)
  AUTHORS   Miya,V., Kumar,C., Breed,A.A., Idicula-Thomas,S. and Pathak,B.R.
  TITLE     Mammalian cysteine-rich secretory proteins interact with plasma
            membrane Ca2+ exporter PMCA4b
  JOURNAL   Andrology 12 (5), 1096-1110 (2024)
   PUBMED   37882330
  REMARK    GeneRIF: Mammalian cysteine-rich secretory proteins interact with
            plasma membrane Ca[2+] exporter PMCA4b.
REFERENCE   2  (residues 1 to 1169)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   3  (residues 1 to 1169)
  AUTHORS   Ho,P.W., Pang,S.Y., Li,M., Tse,Z.H., Kung,M.H., Sham,P.C. and
            Ho,S.L.
  TITLE     PMCA4 (ATP2B4) mutation in familial spastic paraplegia causes delay
            in intracellular calcium extrusion
  JOURNAL   Brain Behav 5 (4), e00321 (2015)
   PUBMED   25798335
REFERENCE   4  (residues 1 to 1169)
  AUTHORS   Baggott,R.R., Alfranca,A., Lopez-Maderuelo,D., Mohamed,T.M.,
            Escolano,A., Oller,J., Ornes,B.C., Kurusamy,S., Rowther,F.B.,
            Brown,J.E., Oceandy,D., Cartwright,E.J., Wang,W., Gomez-del
            Arco,P., Martinez-Martinez,S., Neyses,L., Redondo,J.M. and
            Armesilla,A.L.
  TITLE     Plasma membrane calcium ATPase isoform 4 inhibits vascular
            endothelial growth factor-mediated angiogenesis through interaction
            with calcineurin
  JOURNAL   Arterioscler Thromb Vasc Biol 34 (10), 2310-2320 (2014)
   PUBMED   25147342
REFERENCE   5  (residues 1 to 1169)
  AUTHORS   Afroze,T., Yang,G., Khoshbin,A., Tanwir,M., Tabish,T., Momen,A. and
            Husain,M.
  TITLE     Calcium efflux activity of plasma membrane Ca2+ ATPase-4 (PMCA4)
            mediates cell cycle progression in vascular smooth muscle cells
  JOURNAL   J Biol Chem 289 (10), 7221-7231 (2014)
   PUBMED   24448801
REFERENCE   6  (residues 1 to 1169)
  AUTHORS   Adamo,H.P., Filoteo,A.G., Enyedi,A. and Penniston,J.T.
  TITLE     Mutants in the putative nucleotide-binding region of the plasma
            membrane Ca(2+)-pump. A reduction in activity due to slow
            dephosphorylation
  JOURNAL   J Biol Chem 270 (50), 30111-30114 (1995)
   PUBMED   8530416
REFERENCE   7  (residues 1 to 1169)
  AUTHORS   Keeton,T.P. and Shull,G.E.
  TITLE     Primary structure of rat plasma membrane Ca(2+)-ATPase isoform 4
            and analysis of alternative splicing patterns at splice site A
  JOURNAL   Biochem J 306 (Pt 3) (Pt 3), 779-785 (1995)
   PUBMED   7702574
REFERENCE   8  (residues 1 to 1169)
  AUTHORS   Howard,A., Barley,N.F., Legon,S. and Walters,J.R.
  TITLE     Plasma-membrane calcium-pump isoforms in human and rat liver
  JOURNAL   Biochem J 303 (Pt 1) (Pt 1), 275-279 (1994)
   PUBMED   7945253
REFERENCE   9  (residues 1 to 1169)
  AUTHORS   Howard,A., Legon,S. and Walters,J.R.
  TITLE     Human and rat intestinal plasma membrane calcium pump isoforms
  JOURNAL   Am J Physiol 265 (5 Pt 1), G917-G925 (1993)
   PUBMED   7694502
REFERENCE   10 (residues 1 to 1169)
  AUTHORS   Keeton,T.P., Burk,S.E. and Shull,G.E.
  TITLE     Alternative splicing of exons encoding the calmodulin-binding
            domains and C termini of plasma membrane Ca(2+)-ATPase isoforms 1,
            2, 3, and 4
  JOURNAL   J Biol Chem 268 (4), 2740-2748 (1993)
   PUBMED   8428948
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U15408.1.
            
            On Oct 22, 2004 this sequence version replaced XP_341123.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U15408.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1169
                     /organism="Rattus norvegicus"
                     /strain="CD"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..1169
                     /product="plasma membrane calcium-transporting ATPase 4"
                     /EC_number="7.2.2.10"
                     /note="plasma membrane calcium pump; ATPase, Ca++
                     transporting, plasma membrane 4; plasma membrane calcium
                     ATPase; plasma membrane Ca2+-ATPases 4"
                     /calculated_mol_wt=128660
     Region          16..1052
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Region          1089..>1126
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     CDS             1..1169
                     /gene="Atp2b4"
                     /gene_synonym="PMCA4"
                     /coded_by="NM_001005871.1:168..3677"
                     /db_xref="GeneID:29600"
                     /db_xref="RGD:621305"
ORIGIN      
        1 mtnpsghnlp ansvaesyeg efgctlmdlr klmelraada vtqisahygs vqeicarlkt
       61 spveglsgnp adlekrrlvf gknmippkkp ktflelvwea lqdvtliile iaaiislvls
      121 fyrppggene icghivsnpe edeegetgwi egaailasvi ivvfvtafnd wskekqfrgl
      181 qsrieleqkf siirngqliq lpvaeivvgd iaqvkygdll padgiliqgn dlkidesslt
      241 gesdhvkktl dkdpmllsgt hvmegsgrmv vtavginsqt giiftllgan eeeddekkkk
      301 gkkqgvsenr nkaktqdgva leiqplnsqe gldseekekk askgpkkeks vlqgkltrla
      361 vqigkaglim siltvlilil yfvvdnfviq rrawlpectp vyiqyfvkff iigvtvlvva
      421 vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl tmnrmtvvqa
      481 yiggthyrqi pkpddlppnv ldlivnsici nsaytskilp pekegglprq vgnktecgll
      541 gfvtdlkqdy qavrsempee klfkvytfns vrksmstvir kpeggfrvfs kgaseimlrk
      601 cdrilnkegg ivpfktkdrd nmvrnviepm aseglrtigi ayrdfdgeep sweneneift
      661 glvciavvgi edpvrpevpd ainkckragi tvrmvtgdnv ntaraiatkc giltpgddfl
      721 clegkefnrl irnekgeveq ekldkvwprl rvlarssptd khtlvkgiid snigeqrqvv
      781 avtgdgtndg palkkadvgf amgiagtdva keasdiiltd dnftsivkav mwgrnvydsi
      841 skflqfqltv nvvavivafs gacitqdspl kavqmlwvnl imdtfaslal atepptdsll
      901 rrrpygrnkp lisrtmmkni lghavyqlgi vfllvfagdk lfdidsgrka plnsppsqhy
      961 tivfntfvlm qlfneinsrk ihgeknvfag vyrniifcsv vlgtffcqil ivevggkpfs
     1021 ctnltmeqwm wclfigigel lwgqvisaip tkslkflkea ghgsdkeeis kdaegleeid
     1081 haemelrrgq ilwvrglnri qtqievinkf qtgasfkgvl rrqnlsqqld vklvpssyse
     1141 avasvrtsps tssavtpppv gnqsgqsis
//
LOCUS       NP_742044                262 aa            linear   ROD 27-APR-2025
DEFINITION  ELL-associated factor 2 [Rattus norvegicus].
ACCESSION   NP_742044
VERSION     NP_742044.1
DBSOURCE    REFSEQ: accession NM_172047.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Luo,Z., Lin,C. and Shilatifard,A.
  TITLE     The super elongation complex (SEC) family in transcriptional
            control
  JOURNAL   Nat Rev Mol Cell Biol 13 (9), 543-547 (2012)
   PUBMED   22895430
  REMARK    Review article
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Xiao,W., Zhang,Q., Habermacher,G., Yang,X., Zhang,A.Y., Cai,X.,
            Hahn,J., Liu,J., Pins,M., Doglio,L., Dhir,R., Gingrich,J. and
            Wang,Z.
  TITLE     U19/Eaf2 knockout causes lung adenocarcinoma, B-cell lymphoma,
            hepatocellular carcinoma and prostatic intraepithelial neoplasia
  JOURNAL   Oncogene 27 (11), 1536-1544 (2008)
   PUBMED   17873910
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Xiao,W., Jiang,F. and Wang,Z.
  TITLE     ELL binding regulates U19/Eaf2 intracellular localization,
            stability, and transactivation
  JOURNAL   Prostate 66 (1), 1-12 (2006)
   PUBMED   16114057
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Xiao,W., Zhang,Q., Jiang,F., Pins,M., Kozlowski,J.M. and Wang,Z.
  TITLE     Suppression of prostate tumor growth by U19, a novel
            testosterone-regulated apoptosis inducer
  JOURNAL   Cancer Res 63 (15), 4698-4704 (2003)
   PUBMED   12907652
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Saso,K., Ito,T., Natori,S. and Sekimizu,K.
  TITLE     Identification of a novel tissue-specific transcriptional activator
            FESTA as a protein that interacts with the transcription elongation
            factor S-II
  JOURNAL   J Biochem 133 (4), 493-500 (2003)
   PUBMED   12761297
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY049022.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY049022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..262
                     /product="ELL-associated factor 2"
                     /note="transcription factor; testosterone-regulated
                     apoptosis inducer and tumor suppressor protein;
                     testosterone regulated apoptosis inducer and tumor
                     suppressor"
                     /calculated_mol_wt=28802
     Region          17..113
                     /region_name="EAF"
                     /note="RNA polymerase II transcription elongation factor;
                     pfam09816"
                     /db_xref="CDD:462913"
     Region          17..104
                     /region_name="Necessary for interaction with ELL.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q811X5.1)"
     Region          124..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q811X5.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96CJ1; propagated from
                     UniProtKB/Swiss-Prot (Q811X5.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96CJ1; propagated from
                     UniProtKB/Swiss-Prot (Q811X5.1)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96CJ1; propagated from
                     UniProtKB/Swiss-Prot (Q811X5.1)"
     Region          170..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q811X5.1)"
     Region          177..262
                     /region_name="Necessary for transactivation activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q811X5.1)"
     Region          248..262
                     /region_name="Necessary for interaction with TCEA1 and
                     transactivation activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q811X5.1)"
     CDS             1..262
                     /gene="Eaf2"
                     /gene_synonym="Traits"
                     /coded_by="NM_172047.1:129..917"
                     /db_xref="GeneID:266787"
                     /db_xref="RGD:628879"
ORIGIN      
        1 mngpaglayl drrerilklg esfekqprca fhtvrydfkp asvdascegn levgkgeqvt
       61 itlpniegst ppvtvfkgsk rpylkecili inhdtgecrl eklssnitvk ktrgegsski
      121 qcrleqqqqq mwnpprtsnl vqhspsedkl sptslmddie relkaeaslm dqmsscdsss
      181 dsrsssssss edsssdsedd drsspsgprr yssehpsvsa gpqyrtsdad ttcnrlydns
      241 allmstlrsd lqlsesdsds ed
//
LOCUS       NP_001014202             295 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 [Rattus
            norvegicus].
ACCESSION   NP_001014202 XP_342470
VERSION     NP_001014202.1
DBSOURCE    REFSEQ: accession NM_001014180.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Li,X., Xiong,X., Wang,K., Wang,L., Shu,X., Ma,S. and Yi,C.
  TITLE     Transcriptome-wide mapping reveals reversible and dynamic
            N(1)-methyladenosine methylome
  JOURNAL   Nat Chem Biol 12 (5), 311-316 (2016)
   PUBMED   26863410
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Dominissini,D., Nachtergaele,S., Moshitch-Moshkovitz,S., Peer,E.,
            Kol,N., Ben-Haim,M.S., Dai,Q., Di Segni,A., Salmon-Divon,M.,
            Clark,W.C., Zheng,G., Pan,T., Solomon,O., Eyal,E., Hershkovitz,V.,
            Han,D., Dore,L.C., Amariglio,N., Rechavi,G. and He,C.
  TITLE     The dynamic N(1)-methyladenosine methylome in eukaryotic messenger
            RNA
  JOURNAL   Nature 530 (7591), 441-446 (2016)
   PUBMED   26863196
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Dango,S., Mosammaparast,N., Sowa,M.E., Xiong,L.J., Wu,F., Park,K.,
            Rubin,M., Gygi,S., Harper,J.W. and Shi,Y.
  TITLE     DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
            alkylation repair and cancer cell proliferation
  JOURNAL   Mol Cell 44 (3), 373-384 (2011)
   PUBMED   22055184
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Sundheim,O., Vagbo,C.B., Bjoras,M., Sousa,M.M., Talstad,V.,
            Aas,P.A., Drablos,F., Krokan,H.E., Tainer,J.A. and Slupphaug,G.
  TITLE     Human ABH3 structure and key residues for oxidative demethylation
            to reverse DNA/RNA damage
  JOURNAL   EMBO J 25 (14), 3389-3397 (2006)
   PUBMED   16858410
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Lee,D.H., Jin,S.G., Cai,S., Chen,Y., Pfeifer,G.P. and O'Connor,T.R.
  TITLE     Repair of methylation damage in DNA and RNA by mammalian AlkB
            homologues
  JOURNAL   J Biol Chem 280 (47), 39448-39459 (2005)
   PUBMED   16174769
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083756.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342470.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083756.1, FQ229710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q31"
     Protein         1..295
                     /product="alpha-ketoglutarate-dependent dioxygenase alkB
                     homolog 3"
                     /EC_number="1.14.11.33"
                     /EC_number="1.14.11.54"
                     /note="alkylated DNA repair protein alkB homolog 3; alkB,
                     alkylation repair homolog 3; alkylation repair-like
                     protein 3"
                     /calculated_mol_wt=33880
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC8.1)"
     Region          90..279
                     /region_name="AlkB"
                     /note="Alkylated DNA repair dioxygenase AlkB [Replication,
                     recombination and repair]; COG3145"
                     /db_xref="CDD:442379"
     Site            177
                     /site_type="hydroxylation"
                     /note="(4R)-5-hydroxyleucine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96Q83; propagated from
                     UniProtKB/Swiss-Prot (Q5XIC8.1)"
     CDS             1..295
                     /gene="Alkbh3"
                     /coded_by="NM_001014180.1:132..1019"
                     /db_xref="GeneID:362169"
                     /db_xref="RGD:1359731"
ORIGIN      
        1 mgdkrqrarv qgawatptks qsaarpatpa rsrpsqtpgp swrskeqqqc drrfvfkepq
       61 lvvraapepr vidregvyei slsptgvsrv clypgfvdlk eadwilerlc qdvpwkqrmg
      121 ireditypqp rltawygelp ytysrvtmep nphwlpvlwt lksrieentg htfnsllcnf
      181 yrdekdsvdw hsddepslgs cpviaslsfg atrtfemrkk pppeengdyt yvervkipld
      241 hgtllimega tqadwqhrvp keyhsrerrv nltfrtvypd prgapgdtsa elplr
//
LOCUS       NP_445744               1264 aa            linear   ROD 27-APR-2025
DEFINITION  valine--tRNA ligase [Rattus norvegicus].
ACCESSION   NP_445744 XP_001076616
VERSION     NP_445744.1
DBSOURCE    REFSEQ: accession NM_053292.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Vilalta,A., Donovan,D., Wood,L., Vogeli,G. and Yang,D.C.
  TITLE     Cloning, sequencing and expression of a cDNA encoding mammalian
            valyl-tRNA synthetase
  JOURNAL   Gene 123 (2), 181-186 (1993)
   PUBMED   8428657
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883045.1.
            
            On Oct 13, 2007 this sequence version replaced XP_001076616.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..1264
                     /product="valine--tRNA ligase"
                     /EC_number="6.1.1.9"
                     /note="valyl-tRNA synthetase 2; valRS"
                     /calculated_mol_wt=140238
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P26640; propagated from
                     UniProtKB/Swiss-Prot (Q04462.2)"
     Region          92..213
                     /region_name="GST_C_family"
                     /note="C-terminal, alpha helical domain of the Glutathione
                     S-transferase family; cl02776"
                     /db_xref="CDD:470672"
     Site            order(97,104,159,162..163,166,170)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198286"
     Site            order(97..98,101..102,105,141)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198286"
     Site            order(104,108..109,167,170)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198286"
     Region          218..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04462.2)"
     Region          282..1264
                     /region_name="PTZ00419"
                     /note="valyl-tRNA synthetase-like protein; Provisional"
                     /db_xref="CDD:240411"
     Region          344..354
                     /region_name="'HIGH' region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04462.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26640; propagated from
                     UniProtKB/Swiss-Prot (Q04462.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26640; propagated from
                     UniProtKB/Swiss-Prot (Q04462.2)"
     Site            645
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P26640; propagated from
                     UniProtKB/Swiss-Prot (Q04462.2)"
     Region          862..866
                     /region_name="'KMSKS' region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04462.2)"
     CDS             1..1264
                     /gene="Vars1"
                     /gene_synonym="Bat6; G7a; TrsVal; Vars; Vars2"
                     /coded_by="NM_053292.1:121..3915"
                     /db_xref="GeneID:25009"
                     /db_xref="RGD:3950"
ORIGIN      
        1 msilyvsphp dafpslrali aarygeagdg pgwggphpri clqpppssrt pfppprlpal
       61 eqgpgglwvw gapavaqllw paglggpggs raavlvqqwv syadteltpa acgatlpalg
      121 lrgpgqdpqa algalgkaln pleewlrlht ylagdaptla dlaavtalll pfryvldpsa
      181 rriwgnvtrw fntcvrqpef ravlgevvly sgarsvtqqp gseitapqkt aaqlkkeakk
      241 reklekfqqk qktqqqqpah gekkpkpekk ekrdpgvity dlptppgekk dvsgtmpdsy
      301 spqyveaawy pwwerqgffk peygrpsvsa pnprgvfmmc ipppnvtgsl hlghaltnai
      361 qdsltrwhrm rgettlwnpg cdhagiatqv vvekklwker glnrhqlgre aflqevwkwk
      421 aekgdriyhq lkklgssldw dracftmdpk lsatvteafv rlheegviyr strlvnwsct
      481 lnsaisdiev dkkeltgrtl lsvpgykekv efgvlvsfay kvqgsdsdee vvvattriet
      541 mlgdvavavh pkdpryqhlk gksvvhpfls rslpivfddf vdmefgtgav kitpahdqnd
      601 yevgqrhrle aisimdskga lvnvpppflg lprfearkav laalkeqglf rgikdnpmvv
      661 plcnrskdvv epllrpqwyv rcgemaqaas aavtrgdlri lpeahqrtwh swmdnirdwc
      721 isrqlwwghr ipayfitvhd pavppgedpd grywvsgrte aearekaare fgvspdkisl
      781 qqdedvldtw fssglfpfsi fgwpnqsedl svfypgtlle tghdilffwv armvmlglkl
      841 teklpfrevy lhaivrdahg rkmskslgnv idpldvihgv slqglhdqll nsnldpseve
      901 kakegqradf pagipecgtd alrfglcayt sqgrdinldv nrilgyrhfc nklwnatkfa
      961 lrglgkgfvp sptskpeghe slvdrwirsr laeavrlsne gfqaydfpav ttaqysfwly
     1021 elcdvylecl kpvlngvdqv aadcarqtly tcldvglrll spfmpfvtee lfqrlprrtp
     1081 napaslcvtp ypepsecswk dpeaeaalel alsitravrs lradynltrt rpdcflevad
     1141 eatgalasav sayvqtlasa gvvavlalga papqgcavav asdrcsihlq lqglvdpare
     1201 lgklqakrse aqrqaqrlqe rraasgysak vplevqeade vklqqteael rkvdeaialf
     1261 qkml
//
LOCUS       NP_001008359             260 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 106C [Rattus norvegicus].
ACCESSION   NP_001008359 XP_235617
VERSION     NP_001008359.1
DBSOURCE    REFSEQ: accession NM_001008358.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086606.1.
            
            On Dec 16, 2004 this sequence version replaced XP_235617.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086606.1, DY316426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..260
                     /product="transmembrane protein 106C"
                     /calculated_mol_wt=28777
     Region          15..246
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RJK0.1)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5RJK0.1)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RJK0.1)"
     CDS             1..260
                     /gene="Tmem106c"
                     /gene_synonym="RGD1311532"
                     /coded_by="NM_001008358.1:86..868"
                     /db_xref="GeneID:315286"
                     /db_xref="RGD:1311532"
ORIGIN      
        1 mgsqhssalt fcqrkkddnp edllaerdqe eaiaqfpyve ftgrnsitch tcqgagyipe
       61 eqvnklvali phsdqrlrpq rtkqyvllsv llcllasglv ffflfphsvl vddngirvsn
      121 vtfnkqdslv vldvtatlki rnsnfypvav tnlfsqvqym kavvgsytaa nvslipprse
      181 hlvnftvkae vggpssyvyf yctlpailvh nivifmrtsv qisyightsq stleaqhnvd
      241 cgenstavqs lllvpwgphl
//
LOCUS       NP_058947                283 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction beta-1 protein [Rattus norvegicus].
ACCESSION   NP_058947
VERSION     NP_058947.1
DBSOURCE    REFSEQ: accession NM_017251.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Chen,L., Fang,H., Li,X., Yu,P., Guan,Y., Xiao,C., Deng,Z., Hei,Z.,
            Chen,C. and Luo,C.
  TITLE     Connexin32 gap junction channels deliver miR155-3p to mediate
            pyroptosis in renal ischemia-reperfusion injury
  JOURNAL   Cell Commun Signal 22 (1), 121 (2024)
   PUBMED   38347637
  REMARK    GeneRIF: Connexin32 gap junction channels deliver miR155-3p to
            mediate pyroptosis in renal ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Guo,H., Liu,Y., Gu,J., Luo,J., Ma,Y. and Xiao,F.
  TITLE     GJB1 mutations c.212T>G and c.311A>C induce apoptosis and inwardly
            rectifying potassium current changes in X-linked
            Charcot-Marie-Tooth type 1
  JOURNAL   Biochem Biophys Res Commun 582, 8-15 (2021)
   PUBMED   34678594
  REMARK    GeneRIF: GJB1 mutations c.212T>G and c.311A>C induce apoptosis and
            inwardly rectifying potassium current changes in X-linked
            Charcot-Marie-Tooth type 1.
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Moscato,S., Cabiati,M., Bianchi,F., Panetta,D., Burchielli,S.,
            Massimetti,G., Del Ry,S. and Mattii,L.
  TITLE     Heart and liver connexin expression related to the first stage of
            aging: A study on naturally aged animals
  JOURNAL   Acta Histochem 122 (8), 151651 (2020)
   PUBMED   33171391
  REMARK    GeneRIF: Heart and liver connexin expression related to the first
            stage of aging: A study on naturally aged animals.
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Chen,C., Yao,W., Wu,S., Zhou,S., Ge,M., Gu,Y., Li,X., Chen,G.,
            Bellanti,J.A., Zheng,S.G., Yuan,D. and Hei,Z.
  TITLE     Crosstalk Between Connexin32 and Mitochondrial Apoptotic Signaling
            Pathway Plays a Pivotal Role in Renal Ischemia Reperfusion-Induced
            Acute Kidney Injury
  JOURNAL   Antioxid Redox Signal 30 (12), 1521-1538 (2019)
   PUBMED   29790387
  REMARK    GeneRIF: Crosstalk Between Connexin32 and Mitochondrial Apoptotic
            Signaling Pathway Plays a Pivotal Role in Renal Ischemia
            Reperfusion-Induced Acute Kidney Injury.
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Alaei,S.R., Abrams,C.K., Bulinski,J.C., Hertzberg,E.L. and
            Freidin,M.M.
  TITLE     Acetylation of C-terminal lysines modulates protein turnover and
            stability of Connexin-32
  JOURNAL   BMC Cell Biol 19 (1), 22 (2018)
   PUBMED   30268116
  REMARK    GeneRIF: these results highlight the role of post translational
            modifications and lysines in the C-terminal tail of Cx32 in the
            fine-tuning of Cx32 protein stability and channel-independent
            functions.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Sakamoto,H., Oyamada,M., Enomoto,K. and Mori,M.
  TITLE     Differential changes in expression of gap junction proteins
            connexin 26 and 32 during hepatocarcinogenesis in rats
  JOURNAL   Jpn J Cancer Res 83 (11), 1210-1215 (1992)
   PUBMED   1336494
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Rahman,S. and Evans,W.H.
  TITLE     Topography of connexin32 in rat liver gap junctions. Evidence for
            an intramolecular disulphide linkage connecting the two
            extracellular peptide loops
  JOURNAL   J Cell Sci 100 (Pt 3), 567-578 (1991)
   PUBMED   1667015
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Miller,T., Dahl,G. and Werner,R.
  TITLE     Structure of a gap junction gene: rat connexin-32
  JOURNAL   Biosci Rep 8 (5), 455-464 (1988)
   PUBMED   2852976
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Paul,D.L.
  TITLE     Molecular cloning of cDNA for rat liver gap junction protein
  JOURNAL   J Cell Biol 103 (1), 123-134 (1986)
   PUBMED   3013898
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Nicholson,B.J., Gros,D.B., Kent,S.B., Hood,L.E. and Revel,J.P.
  TITLE     The Mr 28,000 gap junction proteins from rat heart and liver are
            different but related
  JOURNAL   J Biol Chem 260 (11), 6514-6517 (1985)
   PUBMED   2987225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK476084.1 and BC078868.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210131.1, FQ218820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..283
                     /product="gap junction beta-1 protein"
                     /note="gap junction membrane channel protein beta 1;
                     connexin-32; GAP junction 28 kDa liver protein; connexin
                     g"
                     /calculated_mol_wt=31872
     Region          2..214
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08033.1)"
     Site            76..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08033.1)"
     Site            131..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08033.1)"
     Site            192..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08033.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08033.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08033.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08033.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08034; propagated from
                     UniProtKB/Swiss-Prot (P08033.1)"
     CDS             1..283
                     /gene="Gjb1"
                     /gene_synonym="Cx32; Cxng"
                     /coded_by="NM_017251.2:86..937"
                     /db_xref="GeneID:29584"
                     /db_xref="RGD:61926"
ORIGIN      
        1 mnwtglytll sgvnrhstai grvwlsvifi frimvlvvaa esvwgdekss ficntlqpgc
       61 nsvcydhffp ishvrlwslq lilvstpall vamhvahqqh iekkmlrleg hgdplhleev
      121 krhkvhisgt lwwtyvisvv frllfeavfm yvfyllypgy amvrlvkcea fpcpntvdcf
      181 vsrptektvf tvfmlaasgi ciilnvaevv yliiracarr aqrrsnppsr kgsgfghrls
      241 peykqneink llseqdgslk dilrrspgtg aglaeksdrc sac
//
LOCUS       NP_062140                390 aa            linear   ROD 27-APR-2025
DEFINITION  2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
            precursor [Rattus norvegicus].
ACCESSION   NP_062140 XP_001062965 XP_343440
VERSION     NP_062140.1
DBSOURCE    REFSEQ: accession NM_019267.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Knapik-Czajka,M.
  TITLE     Simvastatin increases liver branched-chain alpha-ketoacid
            dehydrogenase activity in rats fed with low protein diet
  JOURNAL   Toxicology 325, 107-114 (2014)
   PUBMED   25193403
  REMARK    GeneRIF: Simvastatin stimulates liver BCKDH activity and BCAAs
            degradation in rats fed with the low protein diet.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Doering,C.B., Coursey,C., Spangler,W. and Danner,D.J.
  TITLE     Murine branched chain alpha-ketoacid dehydrogenase kinase; cDNA
            cloning, tissue distribution, and temporal expression during
            embryonic development
  JOURNAL   Gene 212 (2), 213-219 (1998)
   PUBMED   9611264
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Lombardo,Y.B., Thamotharan,M., Bawani,S.Z., Paul,H.S. and
            Adibi,S.A.
  TITLE     Posttranscriptional alterations in protein masses of hepatic
            branched-chain keto acid dehydrogenase and its associated kinase in
            diabetes
  JOURNAL   Proc Assoc Am Physicians 110 (1), 40-49 (1998)
   PUBMED   9460082
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Zhao,Y., Kuntz,M.J., Harris,R.A. and Crabb,D.W.
  TITLE     Molecular cloning of the E1 beta subunit of the rat branched chain
            alpha-ketoacid dehydrogenase
  JOURNAL   Biochim Biophys Acta 1260 (2), 243 (1995)
   PUBMED   7841205
  REMARK    Correction to:[Biochim Biophys Acta. 1992 Sep 24;1132(2):207-10.
            doi: 10.1016/0167-4781(92)90014-q. PMID: 1390893]
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Zhao,Y., Kuntz,M.J., Harris,R.A. and Crabb,D.W.
  TITLE     Molecular cloning of the E1 beta subunit of the rat branched chain
            alpha-ketoacid dehydrogenase
  JOURNAL   Biochim Biophys Acta 1132 (2), 207-210 (1992)
   PUBMED   1390893
  REMARK    Erratum:[Biochim Biophys Acta. 1995 Jan 25;1260(2):243. PMID:
            7841205]
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Popov,K.M., Zhao,Y., Shimomura,Y., Kuntz,M.J. and Harris,R.A.
  TITLE     Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular
            cloning, expression, and sequence similarity with histidine protein
            kinases
  JOURNAL   J Biol Chem 267 (19), 13127-13130 (1992)
   PUBMED   1377677
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Nobukuni,Y., Mitsubuchi,H., Akaboshi,I., Indo,Y., Endo,F.,
            Yoshioka,A. and Matsuda,I.
  TITLE     Maple syrup urine disease. Complete defect of the E1 beta subunit
            of the branched chain alpha-ketoacid dehydrogenase complex due to a
            deletion of an 11-bp repeat sequence which encodes a mitochondrial
            targeting leader peptide in a family with the disease
  JOURNAL   J Clin Invest 87 (5), 1862-1866 (1991)
   PUBMED   2022752
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Shimomura,Y., Paxton,R., Ozawa,T. and Harris,R.A.
  TITLE     Purification of branched chain alpha-ketoacid dehydrogenase complex
            from rat liver
  JOURNAL   Anal Biochem 163 (1), 74-78 (1987)
   PUBMED   3619032
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK473898.1, M94040.1, CB547976.1, BM385109.1 and DV215445.1.
            
            On or before Oct 28, 2007 this sequence version replaced
            XP_001062965.1, XP_343440.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158861.1, FQ226240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..390
                     /product="2-oxoisovalerate dehydrogenase subunit beta,
                     mitochondrial precursor"
                     /EC_number="1.2.4.4"
                     /note="2-oxoisovalerate dehydrogenase beta subunit;
                     branched chain keto acid dehydrogenase E1 beta;
                     2-oxoisovalerate dehydrogenase subunit beta,
                     mitochondrial; BCKDH E1-beta; branched-chain alpha-keto
                     acid dehydrogenase E1 component beta chain; branched chain
                     keto acid dehydrogenase E1, beta polypeptide"
                     /calculated_mol_wt=37809
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P35738.3)"
                     /calculated_mol_wt=5033
     mat_peptide     49..390
                     /product="2-oxoisovalerate dehydrogenase subunit beta,
                     mitochondrial. /id=PRO_0000020471"
                     /note="propagated from UniProtKB/Swiss-Prot (P35738.3)"
                     /calculated_mol_wt=37809
     Region          64..388
                     /region_name="PTZ00182"
                     /note="3-methyl-2-oxobutanate dehydrogenase; Provisional"
                     /db_xref="CDD:185502"
     Site            230
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P3A8; propagated from
                     UniProtKB/Swiss-Prot (P35738.3)"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P21953; propagated from
                     UniProtKB/Swiss-Prot (P35738.3)"
     CDS             1..390
                     /gene="Bckdhb"
                     /gene_synonym="BCKDE1B"
                     /coded_by="NM_019267.1:29..1201"
                     /db_xref="GeneID:29711"
                     /db_xref="RGD:2197"
ORIGIN      
        1 maavaaragg llrlgaagae rrrrglrcaa lvqgflqpav ddasqkrrva hftfqpdpes
       61 lqygqtqkmn lfqsitsald nslakdptav ifgedvafgg vfrctvglrd kygkdrvfnt
      121 plceqgivgf gigiavtgat aiaeiqfady ifpafdqivn eaakyryrsg dlfncgslti
      181 rapwgcvghg alyhsqspea ffahcpgikv viprspfqak glllsciedk npciffepki
      241 lyraaveqvp vepykiplsq aeviqegsdv tlvawgtqvh virevasmaq eklgvscevi
      301 dlrtivpwdv dtvcksvikt grllisheap ltggfaseis stvqeecfln leapisrvcg
      361 ydtpfphife pfyipdkwkc ydalrkminy
//
LOCUS       NP_036853                389 aa            linear   ROD 27-APR-2025
DEFINITION  P2X purinoceptor 6 [Rattus norvegicus].
ACCESSION   NP_036853
VERSION     NP_036853.2
DBSOURCE    REFSEQ: accession NM_012721.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Padilla,K., Gonzalez-Mendoza,D., Berumen,L.C., Escobar,J.E.,
            Miledi,R. and Garcia-Alcocer,G.
  TITLE     Differential gene expression patterns and colocalization of
            ATP-gated P2X6/P2X4 ion channels during rat small intestine
            ontogeny
  JOURNAL   Gene Expr Patterns 21 (2), 81-88 (2016)
   PUBMED   27545450
  REMARK    GeneRIF: P2X4 and P2X6 proteins were expressed in a different way
            during rat small intestine development, showing a higher
            colocalization coefficient at age P30 in both intestine regions.
            Those results suggest that purinergic receptors may play a role in
            intestinal maturation, which is associated with age and intestinal
            region.
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Liu,Y., Tian,X., Wu,Y., Chen,L., Yi,C.L., Li,Z.W., Zhang,Y. and
            Li,C.Y.
  TITLE     Phenotypes of ATP-activated current associated with their genotypes
            of P2X1-6 subunits in neurons innervating tooth-pulp
  JOURNAL   Biochem Biophys Res Commun 458 (3), 596-600 (2015)
   PUBMED   25680470
  REMARK    GeneRIF: The study explores the association of the phenotype of
            ATP-activated current with the genotype of P2X1-6 subunits in
            neurons innervating tooth-pulp.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Antonio,L.S., Stewart,A.P., Varanda,W.A. and Edwardson,J.M.
  TITLE     Identification of P2X2/P2X4/P2X6 heterotrimeric receptors using
            atomic force microscopy (AFM) imaging
  JOURNAL   FEBS Lett 588 (12), 2125-2128 (2014)
   PUBMED   24815693
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Garcia-Alcocer,G., Padilla,K., Rodriguez,A., Miledi,R. and
            Berumen,L.C.
  TITLE     Distribution of the purinegic receptors P2X(4) and P2X(6) during
            rat gut development
  JOURNAL   Neurosci Lett 509 (2), 92-95 (2012)
   PUBMED   22230887
  REMARK    GeneRIF: P2X(4) and P2X(6) purinoreceptors are present in the gut
            from birth and that they are differentially distributed among
            regions
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Aoyama,R., Okada,Y., Yokota,S., Yasui,Y., Fukuda,K., Shinozaki,Y.,
            Yoshida,H., Nakamura,M., Chiba,K., Yasui,Y., Kato,F. and Toyama,Y.
  TITLE     Spatiotemporal and anatomical analyses of P2X receptor-mediated
            neuronal and glial processing of sensory signals in the rat dorsal
            horn
  JOURNAL   Pain 152 (9), 2085-2097 (2011)
   PUBMED   21669492
  REMARK    GeneRIF: The P2X6 receptor subunit is widely expressed in neuropils
            in the whole gray matter except for the dorsal superficial layer of
            the dorsal horn.
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Bobanovic,L.K., Royle,S.J. and Murrell-Lagnado,R.D.
  TITLE     P2X receptor trafficking in neurons is subunit specific
  JOURNAL   J Neurosci 22 (12), 4814-4824 (2002)
   PUBMED   12077178
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Glass,R., Loesch,A., Bodin,P. and Burnstock,G.
  TITLE     P2X4 and P2X6 receptors associate with VE-cadherin in human
            endothelial cells
  JOURNAL   Cell Mol Life Sci 59 (5), 870-881 (2002)
   PUBMED   12088286
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Rubio,M.E. and Soto,F.
  TITLE     Distinct Localization of P2X receptors at excitatory postsynaptic
            specializations
  JOURNAL   J Neurosci 21 (2), 641-653 (2001)
   PUBMED   11160443
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Soto,F., Garcia-Guzman,M., Karschin,C. and Stuhmer,W.
  TITLE     Cloning and tissue distribution of a novel P2X receptor from rat
            brain
  JOURNAL   Biochem Biophys Res Commun 223 (2), 456-460 (1996)
   PUBMED   8670303
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Collo,G., North,R.A., Kawashima,E., Merlo-Pich,E., Neidhart,S.,
            Surprenant,A. and Buell,G.
  TITLE     Cloning OF P2X5 and P2X6 receptors and the distribution and
            properties of an extended family of ATP-gated ion channels
  JOURNAL   J Neurosci 16 (8), 2495-2507 (1996)
   PUBMED   8786426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X97376.1, CO554543.1 and X92070.1.
            
            On Apr 21, 2009 this sequence version replaced NP_036853.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X92070.1, X97376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..389
                     /product="P2X purinoceptor 6"
                     /note="purinergic receptor P2X6; P2XM; ATP receptor;
                     purinergic receptor P2X-like 1 orphan receptor; P2X6
                     receptor; purinergic receptor P2X, ligand-gated ion
                     channel, 6"
                     /calculated_mol_wt=43291
     Region          22..376
                     /region_name="P2X"
                     /note="cation transporter protein; TIGR00863"
                     /db_xref="CDD:273307"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51579.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O15547; propagated from
                     UniProtKB/Swiss-Prot (P51579.2)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51579.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51579.2)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51579.2)"
     Site            336..356
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51579.2)"
     CDS             1..389
                     /gene="P2rx6"
                     /gene_synonym="P2rxl1; P2x6; Rnap2x6"
                     /coded_by="NM_012721.2:103..1272"
                     /db_xref="GeneID:25041"
                     /db_xref="RGD:3243"
ORIGIN      
        1 mqlqpagtgs masavaaalv swgfldykte kyvmtrncwv gisqrllqlg vvvyvigwal
       61 lakkgyqewd mdpqisvitk lkgvsvtqvk elekrlwdva dfvrpsqgen vfflvtnflv
      121 tpaqvqgrcp ehpsvplanc wadedcpege mgtyshgikt gqcvafngth rtceiwswcp
      181 vessavprkp llaqaknftl fikntvtfnk fnfsrtnald twdntyfkyc lydslsspyc
      241 pvfrigdlva mtggdfedla llggavgini hwdcnldtkg sdcspqysfq lqergynfrt
      301 anywwaasgv esrsllklyg irfdilvtgq agkfalipta itvgtgaawl gmvtflcdll
      361 llyvdreagf ywrtkyeear apkattnsa
//
LOCUS       NP_001035813             589 aa            linear   ROD 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001035813
VERSION     NP_001035813.1
DBSOURCE    REFSEQ: accession NM_001042354.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Yang,C., Zhang,M., Li,S., Yi,F., Huang,H., Xie,H., Liu,H., Huang,R.
            and Zhou,J.
  TITLE     Effects of Camk2b Overexpression and Underexpression on the
            Proteome of Rat Hippocampal Neurons
  JOURNAL   Neuroscience 503, 58-68 (2022)
   PUBMED   36041587
  REMARK    GeneRIF: Effects of Camk2b Overexpression and Underexpression on
            the Proteome of Rat Hippocampal Neurons.
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Liu,W., Li,L., Kuang,H., Xia,Y., Wang,Z., Liu,S. and Yin,D.
  TITLE     Proteomic Profile of Carbonylated Proteins Screen Regulation of
            Apoptosis via CaMK Signaling in Response to Regular Aerobic
            Exercise
  JOURNAL   Biomed Res Int 2018, 2828143 (2018)
   PUBMED   30662904
  REMARK    GeneRIF: Significantly upregulated the expression levels of
            CaMKIIbeta.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Yamazaki,H., Sasagawa,Y., Yamamoto,H., Bito,H. and Shirao,T.
  TITLE     CaMKIIbeta is localized in dendritic spines as both
            drebrin-dependent and drebrin-independent pools
  JOURNAL   J Neurochem 146 (2), 145-159 (2018)
   PUBMED   29675826
  REMARK    GeneRIF: This study provides the first evidence to show that
            CaMKIIbeta interacts with drebrin in dendritic spines.
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Kury,S., van Woerden,G.M., Besnard,T., Proietti Onori,M.,
            Latypova,X., Towne,M.C., Cho,M.T., Prescott,T.E., Ploeg,M.A.,
            Sanders,S., Stessman,H.A.F., Pujol,A., Distel,B., Robak,L.A.,
            Bernstein,J.A., Denomme-Pichon,A.S., Lesca,G., Sellars,E.A.,
            Berg,J., Carre,W., Busk,O.L., van Bon,B.W.M., Waugh,J.L.,
            Deardorff,M., Hoganson,G.E., Bosanko,K.B., Johnson,D.S., Dabir,T.,
            Holla,O.L., Sarkar,A., Tveten,K., de Bellescize,J., Braathen,G.J.,
            Terhal,P.A., Grange,D.K., van Haeringen,A., Lam,C., Mirzaa,G.,
            Burton,J., Bhoj,E.J., Douglas,J., Santani,A.B., Nesbitt,A.I.,
            Helbig,K.L., Andrews,M.V., Begtrup,A., Tang,S., van Gassen,K.L.I.,
            Juusola,J., Foss,K., Enns,G.M., Moog,U., Hinderhofer,K.,
            Paramasivam,N., Lincoln,S., Kusako,B.H., Lindenbaum,P.,
            Charpentier,E., Nowak,C.B., Cherot,E., Simonet,T.,
            Ruivenkamp,C.A.L., Hahn,S., Brownstein,C.A., Xia,F., Schmitt,S.,
            Deb,W., Bonneau,D., Nizon,M., Quinquis,D., Chelly,J., Rudolf,G.,
            Sanlaville,D., Parent,P., Gilbert-Dussardier,B., Toutain,A.,
            Sutton,V.R., Thies,J., Peart-Vissers,L.E.L.M., Boisseau,P.,
            Vincent,M., Grabrucker,A.M., Dubourg,C., Tan,W.H., Verbeek,N.E.,
            Granzow,M., Santen,G.W.E., Shendure,J., Isidor,B., Pasquier,L.,
            Redon,R., Yang,Y., State,M.W., Kleefstra,T., Cogne,B.,
            Petrovski,S., Retterer,K., Eichler,E.E., Rosenfeld,J.A.,
            Agrawal,P.B., Bezieau,S., Odent,S., Elgersma,Y. and Mercier,S.
  CONSRTM   Undiagnosed Diseases Network; GEM HUGO; Deciphering Developmental
            Disorders Study
  TITLE     De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause
            Intellectual Disability
  JOURNAL   Am J Hum Genet 101 (5), 768-788 (2017)
   PUBMED   29100089
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Yan,X., Liu,J., Ye,Z., Huang,J., He,F., Xiao,W., Hu,X. and Luo,Z.
  TITLE     CaMKII-Mediated CREB Phosphorylation Is Involved in Ca2+-Induced
            BDNF mRNA Transcription and Neurite Outgrowth Promoted by
            Electrical Stimulation
  JOURNAL   PLoS One 11 (9), e0162784 (2016)
   PUBMED   27611779
  REMARK    GeneRIF: these data establish a potential signaling pathway of
            Ca2+-CaMKII-CREB in neuronal activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Bayer,K.U., Harbers,K. and Schulman,H.
  TITLE     alphaKAP is an anchoring protein for a novel CaM kinase II isoform
            in skeletal muscle
  JOURNAL   EMBO J 17 (19), 5598-5605 (1998)
   PUBMED   9755160
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Urquidi,V. and Ashcroft,S.J.
  TITLE     A novel pancreatic beta-cell isoform of
            calcium/calmodulin-dependent protein kinase II (beta 3 isoform)
            contains a proline-rich tandem repeat in the association domain
  JOURNAL   FEBS Lett 358 (1), 23-26 (1995)
   PUBMED   7821422
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Ochiishi,T., Terashima,T. and Yamauchi,T.
  TITLE     Specific distribution of Ca2+/calmodulin-dependent protein kinase
            II alpha and beta isoforms in some structures of the rat forebrain
  JOURNAL   Brain Res 659 (1-2), 179-193 (1994)
   PUBMED   7820660
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Malinow,R., Schulman,H. and Tsien,R.W.
  TITLE     Inhibition of postsynaptic PKC or CaMKII blocks induction but not
            expression of LTP
  JOURNAL   Science 245 (4920), 862-866 (1989)
   PUBMED   2549638
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB616255.1, X83375.1, CO395982.1, CO406099.1 and JAXUCZ010000014.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X83375.1, SRR26643290.45023.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..589
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     beta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit beta; caMK-II subunit beta; caM-kinase II
                     beta chain; caM kinase II subunit beta;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II beta; Ca++/calmodulin-dependent protein kinase II beta
                     subunit"
                     /calculated_mol_wt=64904
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          457..584
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..589
                     /gene="Camk2b"
                     /gene_synonym="Ck2b"
                     /coded_by="NM_001042354.1:83..1852"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24245"
                     /db_xref="RGD:2262"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsaaksl lnkkadgvkp qtnstknssa itspkgslpp aalessdstn
      361 ttiededaka prisdilnsv rrgcgtpeae gplsvgpppc lspgllgplp tpsprisdil
      421 nsvrrgsgtp eaeglppvgp ppcpsptlpg plptpsrkqe iiktteqlie avnngdfeay
      481 akicdpglts fepealgnlv egmdfhrfyf enllaknskp ihttilnphv hvigedaaci
      541 ayirltqyid gqgrprtsqs eetrvwhrrd gkwqnvhfhc sgapvaplq
//
LOCUS       NP_001026810             797 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit B [Rattus
            norvegicus].
ACCESSION   NP_001026810 XP_221957
VERSION     NP_001026810.1
DBSOURCE    REFSEQ: accession NM_001031640.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Lee,A.S., Kranzusch,P.J., Doudna,J.A. and Cate,J.H.
  TITLE     eIF3d is an mRNA cap-binding protein that is required for
            specialized translation initiation
  JOURNAL   Nature 536 (7614), 96-99 (2016)
   PUBMED   27462815
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Lee,A.S., Kranzusch,P.J. and Cate,J.H.
  TITLE     eIF3 targets cell-proliferation messenger RNAs for translational
            activation or repression
  JOURNAL   Nature 522 (7554), 111-114 (2015)
   PUBMED   25849773
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Milochau,A., Lagree,V., Benassy,M.N., Chaignepain,S., Papin,J.,
            Garcia-Arcos,I., Lajoix,A., Monterrat,C., Coudert,L.,
            Schmitter,J.M., Ochoa,B. and Lang,J.
  TITLE     Synaptotagmin 11 interacts with components of the RNA-induced
            silencing complex RISC in clonal pancreatic beta-cells
  JOURNAL   FEBS Lett 588 (14), 2217-2222 (2014)
   PUBMED   24882364
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Hinnebusch,A.G.
  TITLE     The scanning mechanism of eukaryotic translation initiation
  JOURNAL   Annu Rev Biochem 83, 779-812 (2014)
   PUBMED   24499181
  REMARK    Review article
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Zeng,L., Wan,Y., Li,D., Wu,J., Shao,M., Chen,J., Hui,L., Ji,H. and
            Zhu,X.
  TITLE     The m subunit of murine translation initiation factor eIF3
            maintains the integrity of the eIF3 complex and is required for
            embryonic development, homeostasis, and organ size control
  JOURNAL   J Biol Chem 288 (42), 30087-30093 (2013)
   PUBMED   24003236
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Damoc,E., Fraser,C.S., Zhou,M., Videler,H., Mayeur,G.L.,
            Hershey,J.W., Doudna,J.A., Robinson,C.V. and Leary,J.A.
  TITLE     Structural characterization of the human eukaryotic initiation
            factor 3 protein complex by mass spectrometry
  JOURNAL   Mol Cell Proteomics 6 (7), 1135-1146 (2007)
   PUBMED   17322308
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098728.1.
            
            On Aug 12, 2005 this sequence version replaced XP_221957.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098728.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..797
                     /product="eukaryotic translation initiation factor 3
                     subunit B"
                     /note="eukaryotic translation initiation factor 3, subunit
                     9 (eta); eIF-3-eta; eukaryotic translation initiation
                     factor 3 subunit 9"
                     /calculated_mol_wt=90780
     Region          1..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P55884,
                     ECO:0000255|HAMAP-Rule:MF_03001; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          <22..162
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZQ9; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZQ9,
                     ECO:0000255|HAMAP-Rule:MF_03001; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZQ9; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZQ9; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZQ9; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          107..396
                     /region_name="Sufficient for interaction with EIF3E.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          153..257
                     /region_name="Sufficient for interaction with EIF3J.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          167..247
                     /region_name="RRM_eIF3B"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     translation initiation factor 3 subunit B (eIF-3B) and
                     similar proteins; cd12278"
                     /db_xref="CDD:409720"
     Site            order(169,171,173..174,204,213,215,217,245,247)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409720"
     Site            order(172,175,182,185..186,188..190,192..193,196,232..235,
                     237..238,243..244)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409720"
     Site            192
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55884; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55884,
                     ECO:0000255|HAMAP-Rule:MF_03001; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Site            271
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55884; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          291..790
                     /region_name="COG5354"
                     /note="Uncharacterized protein, contains Trp-Asp (WD)
                     repeat [General function prediction only]"
                     /db_xref="CDD:227657"
     Region          321..354
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            347
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55884; propagated from
                     UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          355..400
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          359..406
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          404..442
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          412..446
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          450..489
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          497..528
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          539..587
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          543..584
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          595..630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          632..677
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G061.1)"
     Region          637..667
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..797
                     /gene="Eif3b"
                     /gene_synonym="Eif3s9"
                     /coded_by="NM_001031640.1:29..2422"
                     /db_xref="GeneID:288516"
                     /db_xref="RGD:1309018"
ORIGIN      
        1 mqdaenvaap eaaeeraepa rqqpvsespp tdeaagsggs evgrtedaee daearpepev
       61 rakpaaqsee etaaspaasp tpqsaqepsa pgkaeaggeq arhpsaraee eggsdgsaae
      121 aepralenge adepsfsdpe dfvddvseee llgdvlkdrp qeadgidsvi vvdnvpqvgp
      181 drleklknvi hkifskfgki indyypeedg ktkgyifley aspahavdav knadgykldk
      241 qhtfrvnlft dfdkymtisd ewdipekqpf kdlgnlrywl eeaecrdqys vifesgdrts
      301 ifwndvkdpv sieerarwte tyvrwspkgt ylatfhqrgi alwggdkfkq iqrfshqgvq
      361 lidfspcery lvtfsplmdt qddpqaiiiw diltghkkrg fhcessahwp ifkwshdgkf
      421 farmtldtls iyetpsmgll dkkslkisgi kdfswspggn iiafwvpedk diparvtlmq
      481 lptrqeirvr nlfnvvdckl hwqkngdylc vkvdrtpkgt qgvvtnfeif rmrekqvpvd
      541 vvemketiia fawepngskf avlhgeapri svsfyhvksn gkielikmfd kqqantifws
      601 pqgqfvvlag lrsmngalaf vdtsdctvmn iaehymasdv ewdptgryvv tsvswwshkv
      661 dnaywlwtfq grllqknnkd rfcqllwrpr pptllsqdqi kqikkdlkky skifeqkdrl
      721 sqskaskelv errrtmmedf rqyrkmaqel ymkqknerle lrggvdtdel dsnvddweee
      781 tieffvteev iplgsqe
//
LOCUS       NP_001010963             426 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCCH domain-containing protein 15 [Rattus norvegicus].
ACCESSION   NP_001010963 XP_342455
VERSION     NP_001010963.1
DBSOURCE    REFSEQ: accession NM_001010963.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Perez-Arellano,I., Spinola-Amilibia,M. and Bravo,J.
  TITLE     Human Drg1 is a potassium-dependent GTPase enhanced by Lerepo4
  JOURNAL   FEBS J 280 (15), 3647-3657 (2013)
   PUBMED   23711155
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Heese,K.
  TITLE     Establishing an in vivo p48ZnF bioluminescence mouse brain imaging
            model
  JOURNAL   Neurosci Lett 542, 97-101 (2013)
   PUBMED   23470633
  REMARK    GeneRIF: p48ZnF' cellular location of action depends on the cell's
            differentiation status: nuclear in proliferating cells and
            cytoplasmic in differentiated neurons.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Heese,K., Nagai,Y. and Sawada,T.
  TITLE     Nerve growth factor (NGF) induces mRNA expression of the new
            transcription factor protein p48ZnF
  JOURNAL   Exp Mol Med 36 (2), 130-134 (2004)
   PUBMED   15150441
  REMARK    GeneRIF: p48ZnF is up-regulated in rat neuronal PC12 cells upon
            stimulation with the neurotrophic factor NGF
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Gregory,R.C., Lord,K.A., Panek,L.B., Gaines,P., Dillon,S.B. and
            Wojchowski,D.M.
  TITLE     Subtraction cloning and initial characterization of novel
            epo-immediate response genes
  JOURNAL   Cytokine 12 (7), 845-857 (2000)
   PUBMED   10880228
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088438.1.
            
            On Jan 28, 2005 this sequence version replaced XP_342455.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088438.1, AY377983.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..426
                     /product="zinc finger CCCH domain-containing protein 15"
                     /note="brain zinc finger protein; p48ZnF"
                     /calculated_mol_wt=48168
     Region          1..325
                     /region_name="COG5252"
                     /note="Uncharacterized conserved protein, contains
                     CCCH-type Zn-finger protein [General function prediction
                     only]"
                     /db_xref="CDD:227577"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Region          53..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Region          236..260
                     /region_name="Required for interaction with DRG1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Region          302..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WU90; propagated from
                     UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Region          359..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WU90; propagated from
                     UniProtKB/Swiss-Prot (Q6U6G5.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WU90; propagated from
                     UniProtKB/Swiss-Prot (Q6U6G5.1)"
     CDS             1..426
                     /gene="Zc3h15"
                     /coded_by="NM_001010963.1:45..1325"
                     /db_xref="GeneID:362154"
                     /db_xref="RGD:1359234"
ORIGIN      
        1 mppkkqaqag gskkaeqkkk ekiiedktfg lknkkgakqq kfikavthqv kfgqqnprqv
       61 aqseaekklk kddkkkelqe lnelfkpvva aqkiskgadp ksvvcaffkq gqctkgdkck
      121 fshdltlerk cekrsvyida rdeelekdtm dnwdekklee vvnkkhgeae kkkpktqivc
      181 rhfleaienn kygwfwvcpg ggdncmyrha lppgfvlkkd kkkeekedei sledlierer
      241 salgpnvtki tlesflawkk rkrqekidkl eqdmerrkad fkagkalvis grevfefrpe
      301 lvndddeead dtryiqgtgg devddsvgvn didlslyvpr dveetgitva slerfstyas
      361 dkdenklsea sgglaenger sdldedsggg gqengsidav pvdenlftge dldeleeeln
      421 tldlee
//
LOCUS       NP_001017478             247 aa            linear   ROD 27-APR-2025
DEFINITION  C-X-C motif chemokine 16 precursor [Rattus norvegicus].
ACCESSION   NP_001017478 XP_573130
VERSION     NP_001017478.1
DBSOURCE    REFSEQ: accession NM_001017478.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,C., Wu,M., Qu,J., Huang,X., Zeng,Q. and Ha,M.
  TITLE     JNK and Jag1/Notch2 co-regulate CXCL16 to facilitate
            cypermethrin-induced kidney damage
  JOURNAL   Ecotoxicol Environ Saf 238, 113582 (2022)
   PUBMED   35512476
  REMARK    GeneRIF: JNK and Jag1/Notch2 co-regulate CXCL16 to facilitate
            cypermethrin-induced kidney damage.
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Blanco-Melo,D., Nilsson-Payant,B.E., Liu,W.C., Uhl,S., Hoagland,D.,
            Moller,R., Jordan,T.X., Oishi,K., Panis,M., Sachs,D., Wang,T.T.,
            Schwartz,R.E., Lim,J.K., Albrecht,R.A. and tenOever,B.R.
  TITLE     Imbalanced Host Response to SARS-CoV-2 Drives Development of
            COVID-19
  JOURNAL   Cell 181 (5), 1036-1045 (2020)
   PUBMED   32416070
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Wu,J., He,Y., Luo,Y., Zhang,L., Lin,H., Liu,X., Liu,B., Liang,C.,
            Zhou,Y. and Zhou,J.
  TITLE     MiR-145-5p inhibits proliferation and inflammatory responses of RMC
            through regulating AKT/GSK pathway by targeting CXCL16
  JOURNAL   J Cell Physiol 233 (4), 3648-3659 (2018)
   PUBMED   29030988
  REMARK    GeneRIF: miR-145-5p inhibited proliferation and inflammatory
            responses of RMCs through regulation of AKT/GSK pathway by
            targeting CXCL16
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Rabquer,B.J., Tsou,P.S., Hou,Y., Thirunavukkarasu,E., Haines,G.K.
            3rd, Impens,A.J., Phillips,K., Kahaleh,B., Seibold,J.R. and
            Koch,A.E.
  TITLE     Dysregulated expression of MIG/CXCL9, IP-10/CXCL10 and CXCL16 and
            their receptors in systemic sclerosis
  JOURNAL   Arthritis Res Ther 13 (1), R18 (2011)
   PUBMED   21303517
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Dahl,C.P., Husberg,C., Gullestad,L., Waehre,A., Damas,J.K.,
            Vinge,L.E., Finsen,A.V., Ueland,T., Florholmen,G., Aakhus,S.,
            Halvorsen,B., Aukrust,P., Oie,E., Yndestad,A. and Christensen,G.
  TITLE     Increased production of CXCL16 in experimental and clinical heart
            failure: a possible role in extracellular matrix remodeling
  JOURNAL   Circ Heart Fail 2 (6), 624-632 (2009)
   PUBMED   19919988
  REMARK    GeneRIF: Report increased production of CXCL16 in experimental
            heart failure: a possible role in extracellular matrix remodeling.
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Schramme,A., Abdel-Bakky,M.S., Kampfer-Kolb,N., Pfeilschifter,J.
            and Gutwein,P.
  TITLE     The role of CXCL16 and its processing metalloproteinases ADAM10 and
            ADAM17 in the proliferation and migration of human mesangial cells
  JOURNAL   Biochem Biophys Res Commun 370 (2), 311-316 (2008)
   PUBMED   18373975
REFERENCE   8  (residues 1 to 247)
  AUTHORS   Chandrasekar,B., Mummidi,S., Valente,A.J., Patel,D.N., Bailey,S.R.,
            Freeman,G.L., Hatano,M., Tokuhisa,T. and Jensen,L.E.
  TITLE     The pro-atherogenic cytokine interleukin-18 induces CXCL16
            expression in rat aortic smooth muscle cells via MyD88,
            interleukin-1 receptor-associated kinase, tumor necrosis factor
            receptor-associated factor 6, c-Src, phosphatidylinositol 3-kinase,
            Akt, c-Jun N-terminal kinase, and activator protein-1 signaling
  JOURNAL   J Biol Chem 280 (28), 26263-26277 (2005)
   PUBMED   15890643
  REMARK    GeneRIF: IL-18 induces CXCL16 expression via a MyD88,
            IRAK1-IRAK4-TRAF6, c-Src, PI3K, Akt, JNK, AP-1 pathway
REFERENCE   9  (residues 1 to 247)
  AUTHORS   Shimaoka,T., Kume,N., Minami,M., Hayashida,K., Kataoka,H., Kita,T.
            and Yonehara,S.
  TITLE     Molecular cloning of a novel scavenger receptor for oxidized low
            density lipoprotein, SR-PSOX, on macrophages
  JOURNAL   J Biol Chem 275 (52), 40663-40666 (2000)
   PUBMED   11060282
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Matloubian,M., David,A., Engel,S., Ryan,J.E. and Cyster,J.G.
  TITLE     A transmembrane CXC chemokine is a ligand for HIV-coreceptor Bonzo
  JOURNAL   Nat Immunol 1 (4), 298-304 (2000)
   PUBMED   11017100
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079312.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573130.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079312.1, DQ025528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..247
                     /product="C-X-C motif chemokine 16 precursor"
                     /note="C-X-C motif chemokine 16; small-inducible cytokine
                     B16; transmembrane chemokine CXCL16; chemokine (C-X-C
                     motif) ligand 16"
                     /calculated_mol_wt=24343
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2871
     mat_peptide     27..247
                     /product="C-X-C motif chemokine 16. /id=PRO_0000378193"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU5.1)"
                     /calculated_mol_wt=24343
     Region          120..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU5.1)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU5.1)"
     CDS             1..247
                     /gene="Cxcl16"
                     /coded_by="NM_001017478.1:287..1030"
                     /db_xref="GeneID:497942"
                     /db_xref="RGD:1562928"
ORIGIN      
        1 mrrgfgplal tlflfffall tlpgdgnqgs vagscycdrt ipsgtqippa tlnhmrkylk
       61 tfhrcqffir fqlqsksvcg gsqdqwvrel vncfehkqcg ighgqsfhhq khvpqastri
      121 peategkppd tstavqfqst qqstfpsgap slnkeltrhw ettilpsgyg learpvaean
      181 ekqhkqqkep gagagtqalv pvlsllaivf flvaamvcvl cnrrvtrqss sglqlcytpv
      241 eprpqgl
//
LOCUS       NP_001103381             729 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein M isoform a [Rattus
            norvegicus].
ACCESSION   NP_001103381
VERSION     NP_001103381.1
DBSOURCE    REFSEQ: accession NM_001109911.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Chen,S., Zhang,J., Duan,L., Zhang,Y., Li,C., Liu,D., Ouyang,C.,
            Lu,F. and Liu,X.
  TITLE     Identification of HnRNP M as a novel biomarker for colorectal
            carcinoma by quantitative proteomics
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 306 (5), G394-G403 (2014)
   PUBMED   24381081
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Soteriou,D., Iskender,B., Byron,A., Humphries,J.D.,
            Borg-Bartolo,S., Haddock,M.C., Baxter,M.A., Knight,D.,
            Humphries,M.J. and Kimber,S.J.
  TITLE     Comparative proteomic analysis of supportive and unsupportive
            extracellular matrix substrates for human embryonic stem cell
            maintenance
  JOURNAL   J Biol Chem 288 (26), 18716-18731 (2013)
   PUBMED   23658023
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Bajenova,O.V., Zimmer,R., Stolper,E., Salisbury-Rowswell,J.,
            Nanji,A. and Thomas,P.
  TITLE     Heterogeneous RNA-binding protein M4 is a receptor for
            carcinoembryonic antigen in Kupffer cells
  JOURNAL   J Biol Chem 276 (33), 31067-31073 (2001)
   PUBMED   11406629
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Kafasla,P., Patrinou-Georgoula,M. and Guialis,A.
  TITLE     The 72/74-kDa polypeptides of the 70-110 S large heterogeneous
            nuclear ribonucleoprotein complex (LH-nRNP) represent a discrete
            subset of the hnRNP M protein family
  JOURNAL   Biochem J 350 Pt 2 (Pt 2), 495-503 (2000)
   PUBMED   10947964
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Cuervo,A.M., Dice,J.F. and Knecht,E.
  TITLE     A population of rat liver lysosomes responsible for the selective
            uptake and degradation of cytosolic proteins
  JOURNAL   J Biol Chem 272 (9), 5606-5615 (1997)
   PUBMED   9038169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV774465.1, AY724543.1 and BC088317.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY724543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..729
                     /product="heterogeneous nuclear ribonucleoprotein M
                     isoform a"
                     /note="hnRNP M; M4 protein"
                     /calculated_mol_wt=77499
     Region          40..69
                     /region_name="HnRNP_M_NLS"
                     /note="HnRNP M nuclear localization signal; pfam11532"
                     /db_xref="CDD:463289"
     Region          71..146
                     /region_name="RRM1_hnRNPM"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12657"
                     /db_xref="CDD:410058"
     Region          203..278
                     /region_name="RRM2_hnRNPM"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12659"
                     /db_xref="CDD:410060"
     Region          653..729
                     /region_name="RRM3_hnRNPM"
                     /note="RNA recognition motif 3 (RRM3) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein M (hnRNP M);
                     cd12661"
                     /db_xref="CDD:410062"
     CDS             1..729
                     /gene="Hnrnpm"
                     /gene_synonym="Hnrpm; Hnrpm4"
                     /coded_by="NM_001109911.1:22..2211"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:116655"
                     /db_xref="RGD:620369"
ORIGIN      
        1 maagveaaae vaatepkmee esgapcvpsg ngapvpkgee rptqnekrke knikrggnrf
       61 epyanptkry rafitnipfd vkwqslkdlv kekvgevtyv ellmdaegks rgcavvefkm
      121 eesmkkaaev lnkhslsgrp lkvkedpdge harramqkvm attggmgmgp ggpgminipp
      181 silnnpnipn eiihalqagr lgstvfvanl dykvgwkklk evfsmagvvv radiledkdg
      241 ksrgigtvtf eqsieavqai smfngqllfd rpmhvkmder alpkgdffpp erpqqlphgl
      301 ggigmglgpg gqpidanhln kgigmgnlgp agmgmegigf ginkiggmeg pfgggmenmg
      361 rfgsgmnmgr ineilsnalk rgeiiakqgg ggaggsvpgi ermgpgidri sgagmermga
      421 glghgmdrvg seiermglvm drmgsvermg sgiermgplg ldhmassier mgqtmerigs
      481 gvermgagmg fglermaapi drvgqtierm gsgvermgpa iermglsmdr mvptgmgagl
      541 ermgpvmdrm atglermgan nlermglerm ganslermgl ermgansler mgpamgpalg
      601 agiermglam ggaggasfdr aiemergnfg gsfagsfgga gghapgvark acqifvrnlp
      661 fdftwkmlkd kfnecghvly adikmengks kgcgvvkfes pevaeracrm mngmklsgre
      721 idvridrna
//
LOCUS       NP_001012208             320 aa            linear   ROD 27-APR-2025
DEFINITION  pyrroline-5-carboxylate reductase 2 [Rattus norvegicus].
ACCESSION   NP_001012208 XP_344181
VERSION     NP_001012208.1
DBSOURCE    REFSEQ: accession NM_001012208.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Nakayama,T., Al-Maawali,A., El-Quessny,M., Rajab,A., Khalil,S.,
            Stoler,J.M., Tan,W.H., Nasir,R., Schmitz-Abe,K., Hill,R.S.,
            Partlow,J.N., Al-Saffar,M., Servattalab,S., LaCoursiere,C.M.,
            Tambunan,D.E., Coulter,M.E., Elhosary,P.C., Gorski,G.,
            Barkovich,A.J., Markianos,K., Poduri,A. and Mochida,G.H.
  TITLE     Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2,
            Cause Microcephaly and Hypomyelination
  JOURNAL   Am J Hum Genet 96 (5), 709-719 (2015)
   PUBMED   25865492
REFERENCE   2  (residues 1 to 320)
  AUTHORS   De Ingeniis,J., Ratnikov,B., Richardson,A.D., Scott,D.A.,
            Aza-Blanc,P., De,S.K., Kazanov,M., Pellecchia,M., Ronai,Z.,
            Osterman,A.L. and Smith,J.W.
  TITLE     Functional specialization in proline biosynthesis of melanoma
  JOURNAL   PLoS One 7 (9), e45190 (2012)
   PUBMED   23024808
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079222.1.
            
            On Feb 11, 2005 this sequence version replaced XP_344181.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079222.1, SRR8487227.205113.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..320
                     /product="pyrroline-5-carboxylate reductase 2"
                     /EC_number="1.5.1.2"
                     /note="P5CR 2; P5C reductase 2; pyrroline-5-carboxylate
                     reductase family, member 2"
                     /calculated_mol_wt=33542
     Region          1..268
                     /region_name="ProC"
                     /note="Pyrroline-5-carboxylate reductase [Amino acid
                     transport and metabolism]; COG0345"
                     /db_xref="CDD:440114"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C36; propagated from
                     UniProtKB/Swiss-Prot (Q6AY23.1)"
     Region          293..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY23.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C36; propagated from
                     UniProtKB/Swiss-Prot (Q6AY23.1)"
     CDS             1..320
                     /gene="Pycr2"
                     /coded_by="NM_001012208.1:116..1078"
                     /db_xref="GeneID:364064"
                     /db_xref="RGD:1310074"
ORIGIN      
        1 msvgfigagq lacalargft aagvlsahki iasspemdlp tvsalrkmgv nltrsnkdtv
       61 rhsdvlflav kphiipfild eigadvqerh ivvscaagvt issvekklma fqpapkvirc
      121 mtntpvvvre gatvyatgth alvedgklle qlmssvgfct eveedlidai tglsgsgpay
      181 afmaldalad ggvkmgvprr lavrlgaqal lgaakmllds edhpgqlkdn vcspggatih
      241 alhflesggf rsllinavea scirtrelqs madqekvspa alkktlldrv klesptvstl
      301 appssgkllt rnpaqgskre
//
LOCUS       NP_001094222             377 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9,
            mitochondrial [Rattus norvegicus].
ACCESSION   NP_001094222 XP_001064382
VERSION     NP_001094222.1
DBSOURCE    REFSEQ: accession NM_001100752.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Moutaoufik,M.T., Malty,R., Amin,S., Zhang,Q., Phanse,S.,
            Gagarinova,A., Zilocchi,M., Hoell,L., Minic,Z., Gagarinova,M.,
            Aoki,H., Stockwell,J., Jessulat,M., Goebels,F., Broderick,K.,
            Scott,N.E., Vlasblom,J., Musso,G., Prasad,B., Lamantea,E.,
            Garavaglia,B., Rajput,A., Murayama,K., Okazaki,Y., Foster,L.J.,
            Bader,G.D., Cayabyab,F.S. and Babu,M.
  TITLE     Rewiring of the Human Mitochondrial Interactome during Neuronal
            Reprogramming Reveals Regulators of the Respirasome and
            Neurogenesis
  JOURNAL   iScience 19, 1114-1132 (2019)
   PUBMED   31536960
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Lin,R., Mo,Y., Zha,H., Qu,Z., Xie,P., Zhu,Z.J., Xu,Y., Xiong,Y. and
            Guan,K.L.
  TITLE     CLOCK Acetylates ASS1 to Drive Circadian Rhythm of Ureagenesis
  JOURNAL   Mol Cell 68 (1), 198-209 (2017)
   PUBMED   28985504
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168777.1.
            
            On Sep 7, 2008 this sequence version replaced XP_001064382.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168777.1, FQ225095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..377
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 9, mitochondrial"
                     /EC_number="7.1.1.2"
                     /note="CI-39kD; complex I-39kD; NADH-ubiquinone
                     oxidoreductase 39 kDa subunit; sperm flagella protein 3;
                     NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 9"
                     /calculated_mol_wt=38872
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q5BK63.2)"
                     /calculated_mol_wt=3705
     mat_peptide     36..377
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 9, mitochondrial. /id=PRO_0000308374"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK63.2)"
                     /calculated_mol_wt=38872
     Region          54..326
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(60,62..65,84..86,129..131,144,167..169,180,184,
                     203..206)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(180,184)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DC69; propagated from
                     UniProtKB/Swiss-Prot (Q5BK63.2)"
     Site            370
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DC69; propagated from
                     UniProtKB/Swiss-Prot (Q5BK63.2)"
     CDS             1..377
                     /gene="Ndufa9"
                     /coded_by="NM_001100752.1:14..1147"
                     /db_xref="GeneID:362440"
                     /db_xref="RGD:1307307"
ORIGIN      
        1 maaavrfqvv ralpmsrpai saaatsvfcs sshrqlhhav iphgkggrss vsgvvatvfg
       61 atgflgryvv nhlgrmgsqv iipyrcdiyd tmhlrlmgdl gqliflewda rdkdsirkav
      121 qhsnvvinli grewetrnfd fedvfvnipr aiaqaskeag verfihvshl nasmkssaks
      181 lrskavgeke vrtvfpdaii irpsdmfgre drflnhfany rwflavplvs lgfktvkqpv
      241 yvadvskgia natknpdaig ktfaftgpnr yllfhlvkyi fgmthrtfip yplprfvysw
      301 igrlfglspf epwttkdkve rihisdvmat dlpgledlgv qptplelksi evlrrhrtyr
      361 wlsseieetk paktvny
//
LOCUS       NP_001012028             464 aa            linear   ROD 27-APR-2025
DEFINITION  kinetochore protein Nuf2 [Rattus norvegicus].
ACCESSION   NP_001012028 XP_222860
VERSION     NP_001012028.1
DBSOURCE    REFSEQ: accession NM_001012028.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Sun,Z.Y., Wang,W., Gao,H. and Chen,Q.F.
  TITLE     Potential therapeutic targets of the nuclear division cycle 80
            (NDC80) complexes genes in lung adenocarcinoma
  JOURNAL   J Cancer 11 (10), 2921-2934 (2020)
   PUBMED   32226507
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Wang,Y., Tan,P.Y., Handoko,Y.A., Sekar,K., Shi,M., Xie,C.,
            Jiang,X.D., Dong,Q.Z., Goh,B.K.P., Ooi,L.L., Gao,Z. and Hui,K.M.
  TITLE     NUF2 is a valuable prognostic biomarker to predict early recurrence
            of hepatocellular carcinoma after surgical resection
  JOURNAL   Int J Cancer 145 (3), 662-670 (2019)
   PUBMED   30653265
  REMARK    Erratum:[Int J Cancer. 2021 Mar 15;148(6):E7. doi:
            10.1002/ijc.33440. PMID: 33398879]
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Xu,W., Wang,Y., Wang,Y., Lv,S., Xu,X. and Dong,X.
  TITLE     Screening of differentially expressed genes and identification of
            NUF2 as a prognostic marker in breast cancer
  JOURNAL   Int J Mol Med 44 (2), 390-404 (2019)
   PUBMED   31198978
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Sun,J., Chen,J., Wang,Z., Deng,Y., Liu,L. and Liu,X.
  TITLE     [Expression of NUF2 in breast cancer and its clinical significance]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 39 (5), 591-597 (2019)
   PUBMED   31140425
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Chen,X., Li,W., Xiao,L. and Liu,L.
  TITLE     Nuclear division cycle 80 complex is associated with malignancy and
            predicts poor survival of hepatocellular carcinoma
  JOURNAL   Int J Clin Exp Pathol 12 (4), 1233-1247 (2019)
   PUBMED   31933938
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Kaneko,N., Miura,K., Gu,Z., Karasawa,H., Ohnuma,S., Sasaki,H.,
            Tsukamoto,N., Yokoyama,S., Yamamura,A., Nagase,H., Shibata,C.,
            Sasaki,I. and Horii,A.
  TITLE     siRNA-mediated knockdown against CDCA1 and KNTC2, both frequently
            overexpressed in colorectal and gastric cancers, suppresses cell
            proliferation and induces apoptosis
  JOURNAL   Biochem Biophys Res Commun 390 (4), 1235-1240 (2009)
   PUBMED   19878654
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Ohnuma,S., Miura,K., Horii,A., Fujibuchi,W., Kaneko,N., Gotoh,O.,
            Nagasaki,H., Mizoi,T., Tsukamoto,N., Kobayashi,T., Kinouchi,M.,
            Okabe,M., Sasaki,H., Shiiba,K., Miyagawa,K. and Sasaki,I.
  TITLE     Cancer-associated splicing variants of the CDCA1 and MSMB genes
            expressed in cancer cell lines and surgically resected gastric
            cancer tissues
  JOURNAL   Surgery 145 (1), 57-68 (2009)
   PUBMED   19081476
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Hayama,S., Daigo,Y., Kato,T., Ishikawa,N., Yamabuki,T.,
            Miyamoto,M., Ito,T., Tsuchiya,E., Kondo,S. and Nakamura,Y.
  TITLE     Activation of CDCA1-KNTC2, members of centromere protein complex,
            involved in pulmonary carcinogenesis
  JOURNAL   Cancer Res 66 (21), 10339-10348 (2006)
   PUBMED   17079454
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Bharadwaj,R., Qi,W. and Yu,H.
  TITLE     Identification of two novel components of the human NDC80
            kinetochore complex
  JOURNAL   J Biol Chem 279 (13), 13076-13085 (2004)
   PUBMED   14699129
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078993.1.
            
            On Feb 11, 2005 this sequence version replaced XP_222860.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078993.1, SRR8487231.104770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..464
                     /product="kinetochore protein Nuf2"
                     /note="cell division cycle-associated protein 1; NDC80
                     kinetochore complex component NUF2; cell division cycle
                     associated 1; NUF2, NDC80 kinetochore complex component,
                     homolog"
                     /calculated_mol_wt=54425
     Region          1..385
                     /region_name="Interaction with the N-terminus of NDC80.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL9.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZD4; propagated from
                     UniProtKB/Swiss-Prot (Q6AYL9.1)"
     Region          3..146
                     /region_name="Nuf2"
                     /note="Nuf2 family; pfam03800"
                     /db_xref="CDD:461057"
     Region          <150..447
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZD4; propagated from
                     UniProtKB/Swiss-Prot (Q6AYL9.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZD4; propagated from
                     UniProtKB/Swiss-Prot (Q6AYL9.1)"
     Region          386..464
                     /region_name="Interaction with the C-terminus of NDC80 and
                     the SPBC24-SPBC25 subcomplex. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL9.1)"
     CDS             1..464
                     /gene="Nuf2"
                     /gene_synonym="Cdca1"
                     /coded_by="NM_001012028.1:131..1525"
                     /db_xref="GeneID:304951"
                     /db_xref="RGD:1307952"
ORIGIN      
        1 metlsfpryn iaeivvhirn klltgadgkn lsksdflpnp kpevlymiym ralqlvygvr
       61 lehfymmpvn ievmyphime gflpvsnlff hldsfmpicr vndfeiadil ypkanrtsrf
      121 lsgiinfihf retclekyee fllqnkssvd kiqqlsnahq ealmklekln svpveeqeef
      181 kqlkddiqel qhllnqdfrq kttllqeryt kmksdfsekt khvnelklsv vslkevqdsl
      241 kskivdspek lknykekmkd tvqklrsare evmekydiyr dsvdclpscq levqlyqkks
      301 qdladnrekl ssilkeslnl egqidsdsse lkklkteens lirlmtlkke rlatmqfkin
      361 kkqedvkqyk rtmiedcnkv qekrdavceq vtainqdihk iksgiqqlrd aekreklksq
      421 eilvdlksal ekyhegiekt teecctrigg ktaelkrrmf kmpp
//
LOCUS       NP_001019513             705 aa            linear   ROD 27-APR-2025
DEFINITION  dynein axonemal intermediate chain 1 [Rattus norvegicus].
ACCESSION   NP_001019513 XP_575804
VERSION     NP_001019513.1
DBSOURCE    REFSEQ: accession NM_001024342.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Gao,F.J., Shi,L., Hines,T., Hebbar,S., Neufeld,K.L. and Smith,D.S.
  TITLE     Insulin signaling regulates a functional interaction between
            adenomatous polyposis coli and cytoplasmic dynein
  JOURNAL   Mol Biol Cell 28 (5), 587-599 (2017)
   PUBMED   28057765
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Jeanson,L., Thomas,L., Copin,B., Coste,A., Sermet-Gaudelus,I.,
            Dastot-Le Moal,F., Duquesnoy,P., Montantin,G., Collot,N.,
            Tissier,S., Papon,J.F., Clement,A., Louis,B., Escudier,E.,
            Amselem,S. and Legendre,M.
  TITLE     Mutations in GAS8, a Gene Encoding a Nexin-Dynein Regulatory
            Complex Subunit, Cause Primary Ciliary Dyskinesia with Axonemal
            Disorganization
  JOURNAL   Hum Mutat 37 (8), 776-785 (2016)
   PUBMED   27120127
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Li,Y., Klena,N.T., Gabriel,G.C., Liu,X., Kim,A.J., Lemke,K.,
            Chen,Y., Chatterjee,B., Devine,W., Damerla,R.R., Chang,C., Yagi,H.,
            San Agustin,J.T., Thahir,M., Anderton,S., Lawhead,C., Vescovi,A.,
            Pratt,H., Morgan,J., Haynes,L., Smith,C.L., Eppig,J.T.,
            Reinholdt,L., Francis,R., Leatherbury,L., Ganapathiraju,M.K.,
            Tobita,K., Pazour,G.J. and Lo,C.W.
  TITLE     Global genetic analysis in mice unveils central role for cilia in
            congenital heart disease
  JOURNAL   Nature 521 (7553), 520-524 (2015)
   PUBMED   25807483
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Nakhleh,N., Francis,R., Giese,R.A., Tian,X., Li,Y., Zariwala,M.A.,
            Yagi,H., Khalifa,O., Kureshi,S., Chatterjee,B., Sabol,S.L.,
            Swisher,M., Connelly,P.S., Daniels,M.P., Srinivasan,A., Kuehl,K.,
            Kravitz,N., Burns,K., Sami,I., Omran,H., Barmada,M., Olivier,K.,
            Chawla,K.K., Leigh,M., Jonas,R., Knowles,M., Leatherbury,L. and
            Lo,C.W.
  TITLE     High prevalence of respiratory ciliary dysfunction in congenital
            heart disease patients with heterotaxy
  JOURNAL   Circulation 125 (18), 2232-2242 (2012)
   PUBMED   22499950
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Ikegami,K., Sato,S., Nakamura,K., Ostrowski,L.E. and Setou,M.
  TITLE     Tubulin polyglutamylation is essential for airway ciliary function
            through the regulation of beating asymmetry
  JOURNAL   Proc Natl Acad Sci U S A 107 (23), 10490-10495 (2010)
   PUBMED   20498047
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Kennedy,M.P., Omran,H., Leigh,M.W., Dell,S., Morgan,L.,
            Molina,P.L., Robinson,B.V., Minnix,S.L., Olbrich,H., Severin,T.,
            Ahrens,P., Lange,L., Morillas,H.N., Noone,P.G., Zariwala,M.A. and
            Knowles,M.R.
  TITLE     Congenital heart disease and other heterotaxic defects in a large
            cohort of patients with primary ciliary dyskinesia
  JOURNAL   Circulation 115 (22), 2814-2821 (2007)
   PUBMED   17515466
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Zariwala,M.A., Leigh,M.W., Ceppa,F., Kennedy,M.P., Noone,P.G.,
            Carson,J.L., Hazucha,M.J., Lori,A., Horvath,J., Olbrich,H.,
            Loges,N.T., Bridoux,A.M., Pennarun,G., Duriez,B., Escudier,E.,
            Mitchison,H.M., Chodhari,R., Chung,E.M., Morgan,L.C., de
            Iongh,R.U., Rutland,J., Pradal,U., Omran,H., Amselem,S. and
            Knowles,M.R.
  TITLE     Mutations of DNAI1 in primary ciliary dyskinesia: evidence of
            founder effect in a common mutation
  JOURNAL   Am J Respir Crit Care Med 174 (8), 858-866 (2006)
   PUBMED   16858015
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Utton,M.A., Noble,W.J., Hill,J.E., Anderton,B.H. and Hanger,D.P.
  TITLE     Molecular motors implicated in the axonal transport of tau and
            alpha-synuclein
  JOURNAL   J Cell Sci 118 (Pt 20), 4645-4654 (2005)
   PUBMED   16176937
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Fliegauf,M., Olbrich,H., Horvath,J., Wildhaber,J.H., Zariwala,M.A.,
            Kennedy,M., Knowles,M.R. and Omran,H.
  TITLE     Mislocalization of DNAH5 and DNAH9 in respiratory cells from
            patients with primary ciliary dyskinesia
  JOURNAL   Am J Respir Crit Care Med 171 (12), 1343-1349 (2005)
   PUBMED   15750039
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Guichard,C., Harricane,M.C., Lafitte,J.J., Godard,P., Zaegel,M.,
            Tack,V., Lalau,G. and Bouvagnet,P.
  TITLE     Axonemal dynein intermediate-chain gene (DNAI1) mutations result in
            situs inversus and primary ciliary dyskinesia (Kartagener syndrome)
  JOURNAL   Am J Hum Genet 68 (4), 1030-1035 (2001)
   PUBMED   11231901
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083662.1.
            
            On May 27, 2005 this sequence version replaced XP_575804.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083662.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..705
                     /product="dynein axonemal intermediate chain 1"
                     /note="dynein intermediate chain 1, axonemal; axonemal
                     dynein intermediate chain 1"
                     /calculated_mol_wt=79943
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          122..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          340..386
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <358..616
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          386..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          392..433
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          435..478
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          440..494
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          505..542
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          543..583
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          548..587
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          585..625
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     Region          590..631
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          633..672
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL8.1)"
     CDS             1..705
                     /gene="Dnai1"
                     /gene_synonym="Dnaic1"
                     /coded_by="NM_001024342.1:111..2228"
                     /db_xref="GeneID:500442"
                     /db_xref="RGD:1565671"
ORIGIN      
        1 mpskqirkqs viltrgarkr eedsgtdvge gaddwaqska avrppdqlel tdaelkeeft
       61 riltannpha pqnivrysfk ertykligfv nqmaihfsqv gnlipkdsde grrqhyrdel
      121 vagsqesvkv vtsdteilee eeepkegege gegeaegeae agsqtdvpaa aettekviee
      181 elmapvqpke rkltnqfnfs erasqtfnnp lrdrecqmep pprtnfsata nqweiydayv
      241 deleklektk ekektktpva kktekmamrk ltsmesqsdd itkvtqaaki vermvnqnty
      301 ddvaqdfkyy edaadeyrdq egtllplwkf qndkakrlav talcwnpkyk dlfavghgsy
      361 dfmkqsrgml llysmknpsf peymfssesg imcldmhmdh pylvvvgyyd gnvaiynlkk
      421 phsqpcfrst sksgkhtdpv wqvkwqkddm dhnlnffsvs sdgrivswtl vkselvhidv
      481 iklkdegstt eipeglqlht vgcgtafdfh keidylflvg teegkiykcs ksyssqfldt
      541 ydahnmavda vlwnpyharv fiscssdwtv kiwdhaiktp mfiydlnaav gdvawapyss
      601 tvfaavttdg kahvfdlavn kyeaicnqpv vakkknkith vqfnpihpii ivgddrghit
      661 clklspnlrk mpkekkgqev qkgpaveiak ldkllnlvre vktkt
//
LOCUS       NP_775165                305 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase 16 [Rattus norvegicus].
ACCESSION   NP_775165
VERSION     NP_775165.1
DBSOURCE    REFSEQ: accession NM_173142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Eswaran,J., Bernad,A., Ligos,J.M., Guinea,B., Debreczeni,J.E.,
            Sobott,F., Parker,S.A., Najmanovich,R., Turk,B.E. and Knapp,S.
  TITLE     Structure of the human protein kinase MPSK1 reveals an atypical
            activation loop architecture
  JOURNAL   Structure 16 (1), 115-124 (2008)
   PUBMED   18184589
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Guinea,B., Ligos,J.M., Lain de Lera,T., Martin-Caballero,J.,
            Flores,J., Gonzalez de la Pena,M., Garcia-Castro,J. and Bernad,A.
  TITLE     Nucleocytoplasmic shuttling of STK16 (PKL12), a Golgi-resident
            serine/threonine kinase involved in VEGF expression regulation
  JOURNAL   Exp Cell Res 312 (2), 135-144 (2006)
   PUBMED   16310770
  REMARK    GeneRIF: The STK16 overexpression in several cell lines enhances
            their capacity to produce and secrete VEGF.
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Ohta,S., Takeuchi,M., Deguchi,M., Tsuji,T., Gahara,Y. and Nagata,K.
  TITLE     A novel transcriptional factor with Ser/Thr kinase activity
            involved in the transforming growth factor (TGF)-beta signalling
            pathway
  JOURNAL   Biochem J 350 Pt 2 (Pt 2), 395-404 (2000)
   PUBMED   10947953
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Ligos,J.M., Gerwin,N., Fernandez,P., Gutierrez-Ramos,J.C. and
            Bernad,A.
  TITLE     Cloning, expression analysis, and functional characterization of
            PKL12, a member of a new subfamily of ser/thr kinases
  JOURNAL   Biochem Biophys Res Commun 249 (2), 380-384 (1998)
   PUBMED   9712705
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D86220.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86220.1, FQ213827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..305
                     /product="serine/threonine-protein kinase 16"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="MPSK; TSF-1; protein kinase PKL12;
                     TGF-beta-stimulated factor 1; myristoylated and
                     palmitoylated serine/threonine-protein kinase;
                     tyrosine-protein kinase STK16"
                     /calculated_mol_wt=34278
     Region          19..295
                     /region_name="STKc_16"
                     /note="Catalytic domain of Serine/Threonine Kinase 16;
                     cd13986"
                     /db_xref="CDD:270888"
     Site            order(26..30,34,47,49,78,98..101,105,107,148,150,152..153,
                     155,166,169,194..197)
                     /site_type="active"
                     /db_xref="CDD:270888"
     Site            order(26..30,34,47,49,78,98..101,105,148,150,152..153,155,
                     166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270888"
     Site            order(30,105,107,148,150,152,169,194..197)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270888"
     Site            order(165..191,193..197)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270888"
     Region          166..202
                     /region_name="Activation loop. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P57760.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O75716; propagated from
                     UniProtKB/Swiss-Prot (P57760.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O75716; propagated from
                     UniProtKB/Swiss-Prot (P57760.2)"
     CDS             1..305
                     /gene="Stk16"
                     /gene_synonym="F52; PKL12"
                     /coded_by="NM_173142.1:285..1202"
                     /db_xref="GeneID:286927"
                     /db_xref="RGD:629474"
ORIGIN      
        1 mghalcvcsr gtviidnkry lfvqklgegg fsyvdlvegl hdghfyalkr ilcheqqdqe
       61 eaqreadmhr lfqhpnilrl mayslkerga kheawlllpf fkrgtlwnei erlkdqgnfl
      121 tedqilplll gicrgleaih akgyahrdlk ptnillgdeg qpvlmdlgsm nqaciqvegs
      181 rqalalqdwa aqrctisyra pelfsvqshc vidertdvws lgcvlyammf gegpydmvfq
      241 kgdsvalavq ndlsipqspr hssalrqlla smmtvdpqqr phipvllsql ealqppapgq
      301 httqi
//
LOCUS       NP_113900                523 aa            linear   ROD 27-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF3 [Rattus
            norvegicus].
ACCESSION   NP_113900
VERSION     NP_113900.1
DBSOURCE    REFSEQ: accession NM_031712.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Chi,J., Li,W., Xu,Y., Li,X., Zhang,X., Shi,Z., Liu,C., Liu,W.,
            Zhao,M., Meng,Y. and Zhao,D.
  TITLE     PDZK1 improves ventricular remodeling in hypertensive rats by
            regulating the stability of the Mas receptor
  JOURNAL   Amino Acids 55 (11), 1573-1585 (2023)
   PUBMED   37696999
  REMARK    GeneRIF: PDZK1 improves ventricular remodeling in hypertensive rats
            by regulating the stability of the Mas receptor.
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Ferreira,C., Hagen,P., Stern,M., Hussner,J., Zimmermann,U.,
            Grube,M. and Meyer Zu Schwabedissen,H.E.
  TITLE     The scaffold protein PDZK1 modulates expression and function of the
            organic anion transporting polypeptide 2B1
  JOURNAL   Eur J Pharm Sci 120, 181-190 (2018)
   PUBMED   29752999
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Giral,H., Cranston,D., Lanzano,L., Caldas,Y., Sutherland,E.,
            Rachelson,J., Dobrinskikh,E., Weinman,E.J., Doctor,R.B., Gratton,E.
            and Levi,M.
  TITLE     NHE3 regulatory factor 1 (NHERF1) modulates intestinal
            sodium-dependent phosphate transporter (NaPi-2b) expression in
            apical microvilli
  JOURNAL   J Biol Chem 287 (42), 35047-35056 (2012)
   PUBMED   22904329
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Tanimura,A., Yamada,F., Saito,A., Ito,M., Kimura,T., Anzai,N.,
            Horie,D., Yamamoto,H., Miyamoto,K., Taketani,Y. and Takeda,E.
  TITLE     Analysis of different complexes of type IIa sodium-dependent
            phosphate transporter in rat renal cortex using blue-native
            polyacrylamide gel electrophoresis
  JOURNAL   J Med Invest 58 (1-2), 140-147 (2011)
   PUBMED   21372499
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Wang,P., Wang,J.J., Xiao,Y., Murray,J.W., Novikoff,P.M.,
            Angeletti,R.H., Orr,G.A., Lan,D., Silver,D.L. and Wolkoff,A.W.
  TITLE     Interaction with PDZK1 is required for expression of organic anion
            transporting protein 1A1 on the hepatocyte surface
  JOURNAL   J Biol Chem 280 (34), 30143-30149 (2005)
   PUBMED   15994332
  REMARK    GeneRIF: oligomerization of Oatp1a1 with PDZK1 is critical for its
            proper subcellular localization and function
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Kato,Y., Sai,Y., Yoshida,K., Watanabe,C., Hirata,T. and Tsuji,A.
  TITLE     PDZK1 directly regulates the function of organic cation/carnitine
            transporter OCTN2
  JOURNAL   Mol Pharmacol 67 (3), 734-743 (2005)
   PUBMED   15523054
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Ikemoto,M., Arai,H., Feng,D., Tanaka,K., Aoki,J., Dohmae,N.,
            Takio,K., Adachi,H., Tsujimoto,M. and Inoue,K.
  TITLE     Identification of a PDZ-domain-containing protein that interacts
            with the scavenger receptor class B type I
  JOURNAL   Proc Natl Acad Sci U S A 97 (12), 6538-6543 (2000)
   PUBMED   10829064
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Kocher,O., Comella,N., Tognazzi,K. and Brown,L.F.
  TITLE     Identification and partial characterization of PDZK1: a novel
            protein containing PDZ interaction domains
  JOURNAL   Lab Invest 78 (1), 117-125 (1998)
   PUBMED   9461128
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Custer,M., Spindler,B., Verrey,F., Murer,H. and Biber,J.
  TITLE     Identification of a new gene product (diphor-1) regulated by
            dietary phosphate
  JOURNAL   Am J Physiol 273 (5), F801-F806 (1997)
   PUBMED   9374845
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF116896.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF116896.1, BC078788.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..523
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF3"
                     /note="C-terminal linking and modulating protein; NHERF-3;
                     diphor-1; naPi-Cap1; dietary Pi-regulated RNA-1; PDZ
                     domain-containing protein 1; sodium-hydrogen exchanger
                     regulatory factor 3; Na(+)/H(+) exchanger regulatory
                     factor 3; na/Pi cotransporter C-terminal-associated
                     protein 1"
                     /calculated_mol_wt=56757
     Region          8..88
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(19..25,36,39,68,72,75..76)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Region          134..213
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(144..150,161,164,193,197,200..201)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T2W1; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Region          242..321
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            order(252..258,269,272,301,305,308..309)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Region          377..456
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(387..393,404,407,436,440,443..444)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Region          479..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIL4; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ40.2)"
     CDS             1..523
                     /gene="Pdzk1"
                     /gene_synonym="Clamp"
                     /coded_by="NM_031712.1:73..1644"
                     /db_xref="GeneID:65144"
                     /db_xref="RGD:70924"
ORIGIN      
        1 mastfnprec klskkegqny gfflriekdt dghlvrviee gspaekagll dgdrvlring
       61 vfvdkeehaq vvdlvrksgn svtllvldgd syekavkhqv dlkeldqspr epalnekkpd
      121 lgmnggvetc aqprlcylvk egnsfgfslk tiqgkkgvfl tditpqgvam kagvladdhl
      181 ievngenven asheevvekv tksgsrimfl lvdketarch seqktpfkre taslkllphq
      241 prvvvikkgs ngygfylrag peqkgqiikd iepgspaeaa glknndlvva vngesveald
      301 hdsvvemirn ggdqttllvl dkeadriysl arfspllycq sqelpngsvk eapapisapl
      361 eapgsatted vgdhkpklcr likeddsygf hlnairgqpg sfvkevqqgg padkaglene
      421 diiievngen vqdepydrvv erikssgehv tllvcgkvay syfqakkipi lssladplva
      481 gpdekgeteh dsaestkdss hpardrtlsa ashsssnsed tvm
//
LOCUS       NP_001014265             520 aa            linear   ROD 27-APR-2025
DEFINITION  nonsense-mediated mRNA decay factor SMG9 [Rattus norvegicus].
ACCESSION   NP_001014265 XP_344870
VERSION     NP_001014265.1
DBSOURCE    REFSEQ: accession NM_001014243.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Jin,X., Yin,J., Zhu,H., Li,W., Yu,K., Liu,M., Zhang,X., Lu,M.,
            Wan,Z. and Huang,X.
  TITLE     SMG9 Serves as an Oncogene to Promote the Tumor Progression via EMT
            and Wnt/beta-Catenin Signaling Pathway in Hepatocellular Carcinoma
  JOURNAL   Front Pharmacol 12, 701454 (2021)
   PUBMED   34456727
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Shaheen,R., Anazi,S., Ben-Omran,T., Seidahmed,M.Z., Caddle,L.B.,
            Palmer,K., Ali,R., Alshidi,T., Hagos,S., Goodwin,L., Hashem,M.,
            Wakil,S.M., Abouelhoda,M., Colak,D., Murray,S.A. and Alkuraya,F.S.
  TITLE     Mutations in SMG9, Encoding an Essential Component of
            Nonsense-Mediated Decay Machinery, Cause a Multiple Congenital
            Anomaly Syndrome in Humans and Mice
  JOURNAL   Am J Hum Genet 98 (4), 643-652 (2016)
   PUBMED   27018474
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Fernandez,I.S., Yamashita,A., Arias-Palomo,E., Bamba,Y.,
            Bartolome,R.A., Canales,M.A., Teixido,J., Ohno,S. and Llorca,O.
  TITLE     Characterization of SMG-9, an essential component of the
            nonsense-mediated mRNA decay SMG1C complex
  JOURNAL   Nucleic Acids Res 39 (1), 347-358 (2011)
   PUBMED   20817927
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Yamashita,A., Izumi,N., Kashima,I., Ohnishi,T., Saari,B.,
            Katsuhata,Y., Muramatsu,R., Morita,T., Iwamatsu,A., Hachiya,T.,
            Kurata,R., Hirano,H., Anderson,P. and Ohno,S.
  TITLE     SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
            remodeling of the mRNA surveillance complex during
            nonsense-mediated mRNA decay
  JOURNAL   Genes Dev 23 (9), 1091-1105 (2009)
   PUBMED   19417104
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087051.1.
            
            On Apr 20, 2005 this sequence version replaced XP_344870.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132296
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..520
                     /product="nonsense-mediated mRNA decay factor SMG9"
                     /note="protein SMG9; protein smg-9 homolog"
                     /calculated_mol_wt=57502
     Region          1..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H0W8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H0W8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H0W8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Region          107..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS6.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H0W8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS6.1)"
     CDS             1..520
                     /gene="Smg9"
                     /gene_synonym="RGD1309888"
                     /coded_by="NM_001014243.1:76..1638"
                     /db_xref="GeneID:365215"
                     /db_xref="RGD:1309888"
ORIGIN      
        1 msesghsqpg lygierrrrw kepgssgpqn lsgpggrerd yiapwererr dgsedpstnv
       61 mqktpiilsk ppaerskqpp pstapaappa paplekpivl mkpreegkgp vaatgastpe
      121 gtapppptap appkgekegq rptqpvyqiq nrgmgtaapt amdpvvgqak llppermkhs
      181 iklvddqmnw cdsaieylld qtdvlvvgvl glqgtgksmv msllsantpe edqrayvfra
      241 qsaemkergg nqtsgidffi tqerivfldt qpilspsild hlinndrklp peynlphtyv
      301 emqslqiaaf lftvchvviv vqdwftdlsl yrflqtaemv kpstpspshe sssaagsdeg
      361 teyyphlvfl qnkarredfc prklrqmhlm idqlmahshl rykgtlsmlq cnifpglppd
      421 fldaevnlfl vpfmdseaen enppragpgs splfsllpgy rghpsfqslv sklrsqvmsm
      481 arpqlshtil teknwfhyaa riwdgvkkss alaeysrlla
//
LOCUS       NP_001102720             601 aa            linear   ROD 27-APR-2025
DEFINITION  kelch repeat and BTB domain-containing protein 8 [Rattus
            norvegicus].
ACCESSION   NP_001102720 XP_001076969 XP_575612
VERSION     NP_001102720.2
DBSOURCE    REFSEQ: accession NM_001109250.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Werner,A., Iwasaki,S., McGourty,C.A., Medina-Ruiz,S.,
            Teerikorpi,N., Fedrigo,I., Ingolia,N.T. and Rape,M.
  TITLE     Cell-fate determination by ubiquitin-dependent regulation of
            translation
  JOURNAL   Nature 525 (7570), 523-527 (2015)
   PUBMED   26399832
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC160902.1 and CR467699.1.
            
            On Apr 25, 2009 this sequence version replaced NP_001102720.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160902.1, SRR8487230.13242.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132268, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..601
                     /product="kelch repeat and BTB domain-containing protein
                     8"
                     /note="kelch repeat and BTB (POZ) domain containing 8"
                     /calculated_mol_wt=68709
     Region          27..155
                     /region_name="BTB_POZ_KBTBD8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 8 (KBTBD8); cd18274"
                     /db_xref="CDD:349583"
     Region          50..516
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          147..243
                     /region_name="BACK_KBTBD8"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 8 (KBTBD8);
                     cd18483"
                     /db_xref="CDD:350558"
     Region          330..376
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          380..428
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          431..467
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          461..>575
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          519..571
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..601
                     /gene="Kbtbd8"
                     /gene_synonym="RGD1563166"
                     /coded_by="NM_001109250.3:40..1845"
                     /db_xref="GeneID:500262"
                     /db_xref="RGD:1563166"
ORIGIN      
        1 maasadlsks sptpngipss dtandtmdpf hacsilkqlk tmydegqltd ivvevdhgkt
       61 fschrnvlaa ispyfrsmft sgltestqke vriigveaes mglvlnyayt srvilteanv
      121 qalfttasif qipsiqdqca kymishldpq nsigvfifad hyghqelgdr skeyirkkfl
      181 cvtkeqeflq ltkdqlisil dsddlnvdre ehvyesiirw feheqnerev hlpeifakci
      241 rfplmedafi ekipprfaqa ivkscgekgp sntngctqrl gmtasemiic fdaahkhsgk
      301 kqtvpcldiv tgrvfklckp pndlrevgil vspdndiyia ggyrpsssev sidhkaendf
      361 wmydhstnrw lskpsllrar igcklvyccg kmyaiggrvy egdgrnslks vecydsrenc
      421 wmtvcampva mefhnavehk ekiyvlqgef flfyepqkdy wgfltpmtvp riqglaavyk
      481 dsiyyiagtc gnhqrvftve aydielnkwt rkkdfpcdqs inpylklvlf qnklhlfvra
      541 tqvtveehif rtsrknslyq yddiadqwmk vyetpdrlwd lgrhfecava klypqclqkv
      601 l
//
LOCUS       NP_620221                716 aa            linear   ROD 27-APR-2025
DEFINITION  translation initiation factor eIF2B subunit epsilon [Rattus
            norvegicus].
ACCESSION   NP_620221
VERSION     NP_620221.2
DBSOURCE    REFSEQ: accession NM_138866.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Kashiwagi,K., Shigeta,T., Imataka,H., Ito,T. and Yokoyama,S.
  TITLE     Expression, purification, and crystallization of
            Schizosaccharomyces pombe eIF2B
  JOURNAL   J Struct Funct Genomics 17 (1), 33-38 (2016)
   PUBMED   27023709
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Hinnebusch,A.G. and Lorsch,J.R.
  TITLE     The mechanism of eukaryotic translation initiation: new insights
            and challenges
  JOURNAL   Cold Spring Harb Perspect Biol 4 (10), a011544 (2012)
   PUBMED   22815232
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Tuckow,A.P., Vary,T.C., Kimball,S.R. and Jefferson,L.S.
  TITLE     Ectopic expression of eIF2Bepsilon in rat skeletal muscle rescues
            the sepsis-induced reduction in guanine nucleotide exchange
            activity and protein synthesis
  JOURNAL   Am J Physiol Endocrinol Metab 299 (2), E241-E248 (2010)
   PUBMED   20484009
  REMARK    GeneRIF: modulation of eIF2Bepsilon expression may be sufficient to
            correct deficits in skeletal muscle protein synthesis associated
            with sepsis and other muscle-wasting conditions
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Kantor,L., Pinchasi,D., Mintz,M., Hathout,Y., Vanderver,A. and
            Elroy-Stein,O.
  TITLE     A point mutation in translation initiation factor 2B leads to a
            continuous hyper stress state in oligodendroglial-derived cells
  JOURNAL   PLoS One 3 (11), e3783 (2008)
   PUBMED   19023445
  REMARK    GeneRIF: oligodendroglial-derived cells expressing a mutated eIF2B5
            constantly use their stress response mechanism as an adaptation
            mean in order to survive
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Kubica,N., Crispino,J.L., Gallagher,J.W., Kimball,S.R. and
            Jefferson,L.S.
  TITLE     Activation of the mammalian target of rapamycin complex 1 is both
            necessary and sufficient to stimulate eukaryotic initiation factor
            2Bvarepsilon mRNA translation and protein synthesis
  JOURNAL   Int J Biochem Cell Biol 40 (11), 2522-2533 (2008)
   PUBMED   18556237
  REMARK    GeneRIF: Data show that activation of mTORC1 is necessary and
            sufficient to stimulate eIF2Bepsilon mRNA translation.
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Fabian,J.R., Kimball,S.R., Heinzinger,N.K. and Jefferson,L.S.
  TITLE     Subunit assembly and guanine nucleotide exchange activity of
            eukaryotic initiation factor-2B expressed in Sf9 cells
  JOURNAL   J Biol Chem 272 (19), 12359-12365 (1997)
   PUBMED   9139680
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Flowers,K.M., Mellor,H., Matts,R.L., Kimball,S.R. and
            Jefferson,L.S.
  TITLE     Cloning and characterization of complementary and genomic DNAs
            encoding the epsilon-subunit of rat translation initiation
            factor-2B
  JOURNAL   Biochim Biophys Acta 1307 (3), 318-324 (1996)
   PUBMED   8688467
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Gilligan,M., Welsh,G.I., Flynn,A., Bujalska,I., Diggle,T.A.,
            Denton,R.M., Proud,C.G. and Docherty,K.
  TITLE     Glucose stimulates the activity of the guanine nucleotide-exchange
            factor eIF-2B in isolated rat islets of Langerhans
  JOURNAL   J Biol Chem 271 (4), 2121-2125 (1996)
   PUBMED   8567668
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Karinch,A.M., Kimball,S.R., Vary,T.C. and Jefferson,L.S.
  TITLE     Regulation of eukaryotic initiation factor-2B activity in muscle of
            diabetic rats
  JOURNAL   Am J Physiol 264 (1 Pt 1), E101-E108 (1993)
   PUBMED   8430778
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085698.1.
            
            On Nov 15, 2004 this sequence version replaced NP_620221.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085698.1, U19516.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..716
                     /product="translation initiation factor eIF2B subunit
                     epsilon"
                     /note="translation initiation factor eIF-2B subunit
                     epsilon; eIF-2B GDP-GTP exchange factor subunit epsilon;
                     initiation factor eIF-2Be; eukaryotic translation
                     initiation factor 2B subunit 5 epsilon; eIF2B GDP-GTP
                     exchange factor subunit epsilon"
                     /calculated_mol_wt=80076
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64350.2)"
     Site            18
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CHW4; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23707720; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Region          38..252
                     /region_name="eIF-2B_epsilon_N"
                     /note="The N-terminal domain of epsilon subunit of the
                     eIF-2B is a subfamily of glycosyltransferase 2; cd04197"
                     /db_xref="CDD:133040"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23707720; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Region          <317..>391
                     /region_name="glgC"
                     /note="glucose-1-phosphate adenylyltransferase;
                     Provisional; PRK02862"
                     /db_xref="CDD:179486"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23707720; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Region          356..434
                     /region_name="LbH_eIF2B_epsilon"
                     /note="eIF-2B epsilon subunit, central Left-handed
                     parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic
                     translation initiator, a guanine nucleotide exchange
                     factor (GEF) composed of five different subunits (alpha,
                     beta, gamma, delta and epsilon). eIF2B is...; cd05787"
                     /db_xref="CDD:100061"
     Region          443..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64350.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13144; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13144; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13144; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Region          517..539
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64350.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2.
                     /evidence=ECO:0000269|PubMed:11311121,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     Region          543..713
                     /region_name="W2_eIF2B_epsilon"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 2B epsilon; cd11558"
                     /db_xref="CDD:211396"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13144; propagated from
                     UniProtKB/Swiss-Prot (Q64350.2)"
     CDS             1..716
                     /gene="Eif2b5"
                     /coded_by="NM_138866.2:37..2187"
                     /db_xref="GeneID:192234"
                     /db_xref="RGD:708380"
ORIGIN      
        1 maataavpsa vggrankrgg gsggggtqga eeepppplqa vlvadsfdrr ffpiskdqpr
       61 vllplanval idytleflta tgvqetfvfc cwkaaqikeh lqkskwchpt slnvvriits
      121 dlyrslgdvl rdvdakalvr sdflliygdv vsniniskal eehrlrrkle knvsvmtmvf
      181 kesspshptr chednvvlav dsttnrilhf qktqglrhfs fplglfqgsl dgveirydll
      241 dchisicspq vaqlftdnfd yqtrddfvrg llvneeilgn qihlhvtsre ygarvsnlhm
      301 ysavcadvir rwvypltpev nftdsstqsy thsrhniyrg pevslghgsv leenvllgag
      361 tvvgsncsit nsvigpnchi gdnvvldqay lwqgvrvaag aqihqsllcd raevkervil
      421 kphcvltsqv vvgpdiilpe gsvislhppd aeededdgqf sddsgadqek ekvklkgynp
      481 aevgpegqgy lwkaedvdek edeelrqslw glminmeees etesersvdp eeldsragsp
      541 qlddirvfqn evlgtlqrgr eeniscdnlv leinslkyay nislkevmqv lshvvlefpl
      601 qqvdgvldpn rycalllpll kawspvfrny ikraadhlea laaiedffle hetlvpslak
      661 vlmafyqlei laeetilswf sqrditdkgq qlrknqqlqr fiqwlreaee essddd
//
LOCUS       NP_599211                154 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis-associated protein 19, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_599211 XP_579633
VERSION     NP_599211.1
DBSOURCE    REFSEQ: accession NM_134384.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Doiguchi,M., Yamashita,H., Ichinose,J., Mori,T., Shibata,Y. and
            Iida,H.
  TITLE     Complementary DNA cloning and characterization of rat spergen-1, a
            spermatogenic cell-specific gene-1, containing a
            mitochondria-targeting signal
  JOURNAL   Biol Reprod 66 (5), 1462-1470 (2002)
   PUBMED   11967211
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB057408.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579633.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB057408.1, BC081729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..154
                     /product="spermatogenesis-associated protein 19,
                     mitochondrial precursor"
                     /note="spermatogenesis-associated protein 19,
                     mitochondrial; spermatogenic cell-specific gene 1 protein;
                     spermatogenic specific-gene1"
                     /calculated_mol_wt=15242
     transit_peptide 1..24
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q920Q3.1)"
                     /calculated_mol_wt=2818
     mat_peptide     25..154
                     /product="Spermatogenesis-associated protein 19,
                     mitochondrial. /evidence=ECO:0000250. /id=PRO_0000251611"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920Q3.1)"
                     /calculated_mol_wt=15242
     Region          25..154
                     /region_name="SPATA19"
                     /note="Spermatogenesis-associated protein 19,
                     mitochondrial; pfam15212"
                     /db_xref="CDD:291866"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q3.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q3.1)"
     CDS             1..154
                     /gene="Spata19"
                     /gene_synonym="Spas1; spergen-1"
                     /coded_by="NM_134384.1:25..489"
                     /db_xref="GeneID:171403"
                     /db_xref="RGD:620628"
ORIGIN      
        1 miittwimyi larksiglpf pprvnsdiev eeteavsvvq hwlnkteeea srsikekisi
       61 ndpctqghdi hvtrdlvkhr lskcdmltdp nqevleertr iqfirwshtr ifqvpsemmd
      121 dviqeridqv rrsvshlrcd sssdpcyrns csec
//
LOCUS       NP_001071150             409 aa            linear   ROD 27-APR-2025
DEFINITION  sperm equatorial segment protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001071150 XP_001073992 XP_576422
VERSION     NP_001071150.1
DBSOURCE    REFSEQ: accession NM_001077682.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Suryavathi,V., Panneerdoss,S., Wolkowicz,M.J., Shetty,J.,
            Sherman,N.E., Flickinger,C.J. and Herr,J.C.
  TITLE     Dynamic Changes in Equatorial Segment Protein 1 (SPESP1)
            Glycosylation During Mouse Spermiogenesis
  JOURNAL   Biol Reprod 92 (5), 129 (2015)
   PUBMED   25761597
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Fujihara,Y., Murakami,M., Inoue,N., Satouh,Y., Kaseda,K., Ikawa,M.
            and Okabe,M.
  TITLE     Sperm equatorial segment protein 1, SPESP1, is required for fully
            fertile sperm in mouse
  JOURNAL   J Cell Sci 123 (Pt 9), 1531-1536 (2010)
   PUBMED   20375058
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127527.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_576422.1, XP_001073992.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127527.1, CK468918.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..409
                     /product="sperm equatorial segment protein 1 precursor"
                     /calculated_mol_wt=43798
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A0JPP4.1)"
                     /calculated_mol_wt=2100
     mat_peptide     19..409
                     /product="Sperm equatorial segment protein 1.
                     /evidence=ECO:0000255. /id=PRO_0000274537"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP4.1)"
                     /calculated_mol_wt=43798
     Region          20..381
                     /region_name="SPESP1"
                     /note="Sperm equatorial segment protein 1; pfam15754"
                     /db_xref="CDD:464848"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A0JPP4.1)"
     Region          141..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP4.1)"
     CDS             1..409
                     /gene="Spesp1"
                     /gene_synonym="RGD1563468"
                     /coded_by="NM_001077682.1:151..1380"
                     /db_xref="GeneID:501010"
                     /db_xref="RGD:1563468"
ORIGIN      
        1 mkpvvlvall wlwpssflay ptatvlpdee qnlnhyvqil qnlimsvptk eqgfgrkfrs
       61 srtvdgaear slssemlltp glvsaqevtt petevmltsm vekttfpssg ftmesekrrt
      121 hskafwsiqp nnvsivlhte epyiekepep epeleteees rrlatepepe pesesapete
      181 trqtaeseee vetstaqnkv rtgtsrmstv itqttntqgt pntvtvktin nldvstesed
      241 vpqlsgqsei lnvedlpghh slstrhenil rkisninsqi hqgllsdhss paykefikas
      301 rehlkrslal aaaaehklqq mygsnvfldg htsdpdddme viinmlynsr sklsdyftin
      361 hvpselreka tvviavlkki lcvdqvemqs lirkllsnnm kilnilnvp
//
LOCUS       NP_620782                260 aa            linear   ROD 27-APR-2025
DEFINITION  BMP and activin membrane-bound inhibitor homolog precursor [Rattus
            norvegicus].
ACCESSION   NP_620782
VERSION     NP_620782.1
DBSOURCE    REFSEQ: accession NM_139082.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Zhu,K., Hu,X., Chen,H., Li,F., Yin,N., Liu,A.L., Shan,K., Qin,Y.W.,
            Huang,X., Chang,Q., Xu,G.Z. and Wang,Z.
  TITLE     Downregulation of circRNA DMNT3B contributes to diabetic retinal
            vascular dysfunction through targeting miR-20b-5p and BAMBI
  JOURNAL   EBioMedicine 49, 341-353 (2019)
   PUBMED   31636010
  REMARK    GeneRIF: Downregulation of circDNMT3B contributes to vascular
            dysfunction in diabetic retinas through regulating miR-20b-5p and
            BAMBI, providing a potential treatment strategy for diabetic
            retinopathy
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Sun,L., Xiu,M., Wang,S., Brigstock,D.R., Li,H., Qu,L. and Gao,R.
  TITLE     Lipopolysaccharide enhances TGF-beta1 signalling pathway and rat
            pancreatic fibrosis
  JOURNAL   J Cell Mol Med 22 (4), 2346-2356 (2018)
   PUBMED   29424488
  REMARK    GeneRIF: These findings indicate that LPS increases TGF-beta1
            production through paracrine and autocrine mechanisms and that LPS
            enhances TGF-beta1 signalling in PSCs by repressing BAMBI via
            TLR4/MyD88/NF-kB activation.
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Yang,Y., Guo,C., Liao,B., Cao,J., Liang,C. and He,X.
  TITLE     BAMBI inhibits inflammation through the activation of autophagy in
            experimental spinal cord injury
  JOURNAL   Int J Mol Med 39 (2), 423-429 (2017)
   PUBMED   28035406
  REMARK    GeneRIF: BAMBI plays a neuroprotective role by decreasing
            inflammation and activating autophagy in rats with SCI.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Zhang,J.C., Chen,G., Chen,L., Meng,Z.J., Xiong,X.Z., Liu,H.J.,
            Jin,Y., Tao,X.N., Wu,J.H. and Sun,S.W.
  TITLE     TGF-beta/BAMBI pathway dysfunction contributes to peripheral
            Th17/Treg imbalance in chronic obstructive pulmonary disease
  JOURNAL   Sci Rep 6, 31911 (2016)
   PUBMED   27549738
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   He,Y., Ou,Z., Chen,X., Zu,X., Liu,L., Li,Y., Cao,Z., Chen,M.,
            Chen,Z., Chen,H., Qi,L. and Wang,L.
  TITLE     LPS/TLR4 Signaling Enhances TGF-beta Response Through
            Downregulating BAMBI During Prostatic Hyperplasia
  JOURNAL   Sci Rep 6, 27051 (2016)
   PUBMED   27243216
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Lin,Z., Gao,C., Ning,Y., He,X., Wu,W. and Chen,Y.G.
  TITLE     The pseudoreceptor BMP and activin membrane-bound inhibitor
            positively modulates Wnt/beta-catenin signaling
  JOURNAL   J Biol Chem 283 (48), 33053-33058 (2008)
   PUBMED   18838381
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Togo,N., Ohwada,S., Sakurai,S., Toya,H., Sakamoto,I., Yamada,T.,
            Nakano,T., Muroya,K., Takeyoshi,I., Nakajima,T., Sekiya,T.,
            Yamazumi,Y., Nakamura,T. and Akiyama,T.
  TITLE     Prognostic significance of BMP and activin membrane-bound inhibitor
            in colorectal cancer
  JOURNAL   World J Gastroenterol 14 (31), 4880-4888 (2008)
   PUBMED   18756595
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Sekiya,T., Adachi,S., Kohu,K., Yamada,T., Higuchi,O., Furukawa,Y.,
            Nakamura,Y., Nakamura,T., Tashiro,K., Kuhara,S., Ohwada,S. and
            Akiyama,T.
  TITLE     Identification of BMP and activin membrane-bound inhibitor (BAMBI),
            an inhibitor of transforming growth factor-beta signaling, as a
            target of the beta-catenin pathway in colorectal tumor cells
  JOURNAL   J Biol Chem 279 (8), 6840-6846 (2004)
   PUBMED   14660579
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Loveland,K.L., Bakker,M., Meehan,T., Christy,E., von Schonfeldt,V.,
            Drummond,A. and de Kretser,D.
  TITLE     Expression of Bambi is widespread in juvenile and adult rat tissues
            and is regulated in male germ cells
  JOURNAL   Endocrinology 144 (9), 4180-4186 (2003)
   PUBMED   12933693
  REMARK    GeneRIF: Regulated Bambi mRNA synthesis may contribute to TGF beta
            superfamily signaling modulation in several organs, as suggested by
            its discrete expression switch in male germ cells.
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF387513.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF387513.1, BC070516.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..260
                     /product="BMP and activin membrane-bound inhibitor homolog
                     precursor"
                     /note="kinase-deficient TGFbeta superfamily receptor
                     subunit; BMP and activin membrane-bound inhibitor,
                     homolog"
                     /calculated_mol_wt=26121
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3040
     Region          4..111
                     /region_name="BAMBI"
                     /note="BMP and activin membrane-bound inhibitor (BAMBI)
                     N-terminal domain; pfam06211"
                     /db_xref="CDD:283793"
     mat_peptide     27..260
                     /product="BMP and activin membrane-bound inhibitor
                     homolog. /id=PRO_0000020781"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XN4.1)"
                     /calculated_mol_wt=26121
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XN4.1)"
     Region          123..260
                     /region_name="BAMBI_C"
                     /note="BMP and activin membrane-bound inhibitor homolog
                     C-terminus; pfam19337"
                     /db_xref="CDD:437169"
     Site            153..173
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XN4.1)"
     CDS             1..260
                     /gene="Bambi"
                     /coded_by="NM_139082.3:12..794"
                     /db_xref="GeneID:83837"
                     /db_xref="RGD:621831"
ORIGIN      
        1 mdrhssyifi wlqlelcama vlltkgeirc ycdaahcvat gymckselsa cfsrlldpqn
       61 tnsplthgcl dslastadic rakqaqnhsg ptmptlecch edmcnyrglh dvlsppksea
      121 sgqgnryqhd ssrnlitkvq eltsskelwf raaviavpia gglilvllim lalrmlrsen
      181 krlqdqrqqm lsrlhysfhg hhskkgqvak ldlecmvpvs gqenccltcd kmrqadlsne
      241 kilslvhwgm ysghgklefv
//
LOCUS       NP_001007680             350 aa            linear   ROD 27-APR-2025
DEFINITION  proton-activated chloride channel [Rattus norvegicus].
ACCESSION   NP_001007680 XP_223071
VERSION     NP_001007680.1
DBSOURCE    REFSEQ: accession NM_001007679.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082061.1.
            
            On Nov 29, 2004 this sequence version replaced XP_223071.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082061.1, FQ228821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..350
                     /product="proton-activated chloride channel"
                     /note="transmembrane protein 206"
                     /calculated_mol_wt=39942
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H813; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Region          55..349
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H28.1)"
     Site            302..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H28.1)"
     CDS             1..350
                     /gene="Pacc1"
                     /gene_synonym="PAC; RGD1359339; Tmem206"
                     /coded_by="NM_001007679.1:68..1120"
                     /db_xref="GeneID:305070"
                     /db_xref="RGD:1359339"
ORIGIN      
        1 mirqdlstsy qelseeleqv venseqader dkelvqvqgp gvvpgvdnes asssirfska
       61 clknvfsvll iliylllmav avflvyqtit dfreklkhpv msvsykevdr ydapgialyp
      121 gqaqllsckh hyevipplas pgqpgdrnct tqrinythpf snhtmqsali vqgpqevkkr
      181 elvflqfrln qsdedfsaid yllfssfref mqspdkagfm qacesayssw kfsggfrtwv
      241 kmslvktkee dgreavefrq etsvvnyidq rpaaekstql ffvvfewkdp fiqkvqdiit
      301 anpwntiall cgaflalfka aefaklsvkw mikirkrylk rrgqatnhis
//
LOCUS       NP_001108507             325 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit I [Rattus
            norvegicus].
ACCESSION   NP_001108507 XP_001061306
VERSION     NP_001108507.1
DBSOURCE    REFSEQ: accession NM_001115035.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Lee,A.S., Kranzusch,P.J. and Cate,J.H.
  TITLE     eIF3 targets cell-proliferation messenger RNAs for translational
            activation or repression
  JOURNAL   Nature 522 (7554), 111-114 (2015)
   PUBMED   25849773
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Hinnebusch,A.G.
  TITLE     The scanning mechanism of eukaryotic translation initiation
  JOURNAL   Annu Rev Biochem 83, 779-812 (2014)
   PUBMED   24499181
  REMARK    Review article
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Zeng,L., Wan,Y., Li,D., Wu,J., Shao,M., Chen,J., Hui,L., Ji,H. and
            Zhu,X.
  TITLE     The m subunit of murine translation initiation factor eIF3
            maintains the integrity of the eIF3 complex and is required for
            embryonic development, homeostasis, and organ size control
  JOURNAL   J Biol Chem 288 (42), 30087-30093 (2013)
   PUBMED   24003236
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Du,J., Teng,R.J., Lawrence,M., Guan,T., Xu,H., Ge,Y. and Shi,Y.
  TITLE     The protein partners of GTP cyclohydrolase I in rat organs
  JOURNAL   PLoS One 7 (3), e33991 (2012)
   PUBMED   22479495
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Zhou,M., Sandercock,A.M., Fraser,C.S., Ridlova,G., Stephens,E.,
            Schenauer,M.R., Yokoi-Fong,T., Barsky,D., Leary,J.A., Hershey,J.W.,
            Doudna,J.A. and Robinson,C.V.
  TITLE     Mass spectrometry reveals modularity and a complete subunit
            interaction map of the eukaryotic translation factor eIF3
  JOURNAL   Proc Natl Acad Sci U S A 105 (47), 18139-18144 (2008)
   PUBMED   18599441
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     Reconstitution reveals the functional core of mammalian eIF3
  JOURNAL   EMBO J 26 (14), 3373-3383 (2007)
   PUBMED   17581632
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Damoc,E., Fraser,C.S., Zhou,M., Videler,H., Mayeur,G.L.,
            Hershey,J.W., Doudna,J.A., Robinson,C.V. and Leary,J.A.
  TITLE     Structural characterization of the human eukaryotic initiation
            factor 3 protein complex by mass spectrometry
  JOURNAL   Mol Cell Proteomics 6 (7), 1135-1146 (2007)
   PUBMED   17322308
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Sheu,T.J., Schwarz,E.M., Martinez,D.A., O'Keefe,R.J., Rosier,R.N.,
            Zuscik,M.J. and Puzas,J.E.
  TITLE     A phage display technique identifies a novel regulator of cell
            differentiation
  JOURNAL   J Biol Chem 278 (1), 438-443 (2003)
   PUBMED   12403789
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473968.1.
            
            On Mar 2, 2008 this sequence version replaced XP_001061306.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158821.1, FQ220584.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..325
                     /product="eukaryotic translation initiation factor 3
                     subunit I"
                     /note="eIF3 p36; eIF-3-beta; eukaryotic translation
                     initiation factor 3 subunit 2"
                     /calculated_mol_wt=36330
     Region          <5..311
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          8..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          14..50
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          50..91
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          55..91
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          144..183
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          150..185
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          186..225
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          191..226
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          232..272
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            264
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13347; propagated from
                     UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          283..324
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA7.1)"
     Region          288..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13347; propagated from
                     UniProtKB/Swiss-Prot (B0BNA7.1)"
     CDS             1..325
                     /gene="Eif3i"
                     /gene_synonym="Eif3s2; TRIP-1"
                     /coded_by="NM_001115035.1:39..1016"
                     /db_xref="GeneID:682390"
                     /db_xref="RGD:1584560"
ORIGIN      
        1 mkpillqghe rsitqikynr egdllftvak dpivnvwysv ngerlgtymg htgavwcvda
       61 dwdtkhvltg sadnscrlwd cetgkqlall ktnsavrtcg fdfggniimf stdkqmgyqc
      121 fvsffdlrdp sqidsnepym kipcndskit savwgplgec iiaghesgel nqysaksgev
      181 lvnvkehsrq indiqlsrdm tmfvtaskdn taklfdstsl ehqktfrter pvnsaalspn
      241 ydhvvlgggq eamdvtttst rigkfearff hlafeeefgr vkghfgpins vafhpdgksy
      301 ssggedgyvr ihyfdpqyfe fefea
//
LOCUS       NP_001004268             397 aa            linear   ROD 27-APR-2025
DEFINITION  keratinocyte differentiation factor 1 [Rattus norvegicus].
ACCESSION   NP_001004268 XP_232747
VERSION     NP_001004268.1
DBSOURCE    REFSEQ: accession NM_001004268.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Lee,S., Kong,Y. and Weatherbee,S.D.
  TITLE     Forward genetics identifies Kdf1/1810019J16Rik as an essential
            regulator of the proliferation-differentiation decision in
            epidermal progenitor cells
  JOURNAL   Dev Biol 383 (2), 201-213 (2013)
   PUBMED   24075906
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079148.1.
            
            On Sep 10, 2004 this sequence version replaced XP_232747.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..397
                     /product="keratinocyte differentiation factor 1"
                     /note="uncharacterized protein C1orf172 homolog"
                     /calculated_mol_wt=43314
     Region          1..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY88.1)"
     Region          48..397
                     /region_name="DUF4656"
                     /note="Domain of unknown function (DUF4656); pfam15551"
                     /db_xref="CDD:464761"
     Region          124..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY88.1)"
     Region          191..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY88.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A9F4; propagated from
                     UniProtKB/Swiss-Prot (Q6AY88.1)"
     Region          304..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY88.1)"
     Region          361..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY88.1)"
     CDS             1..397
                     /gene="Kdf1"
                     /gene_synonym="RGD1303271"
                     /coded_by="NM_001004268.1:73..1266"
                     /db_xref="GeneID:313018"
                     /db_xref="RGD:1303271"
ORIGIN      
        1 mprpgqprps sgpprlgpwe rptelcletn dersqpppgr rtrrpdpkdp ghhgpesitf
       61 isgsaepane pptccllwrp wgwdwcraaf cfrrcrdclq rcgacvrscs pclsagdpie
      121 gsseaawake hngvppspdr appsrrdgqk lktsmgssfs ypdvklkgip vypyrhatsp
      181 vpdadsccke pladppptrh slpstftssp rgseeyysfh esdldlpemg sgsmssreid
      241 vlifkkltel fsvhqidela kctsdtvfle ktskisdlis sitqdyhlde qdaegrlvrg
      301 iiristrksr srpqtsegrs arstapaaap dsghetmvgs glsqdeltvq isqettadai
      361 arklrpygap gypasqdssf qgtdtdssga pllqvyc
//
LOCUS       NP_001033069             335 aa            linear   ROD 27-APR-2025
DEFINITION  transcriptional adapter 1 [Rattus norvegicus].
ACCESSION   NP_001033069 XP_341151
VERSION     NP_001033069.2
DBSOURCE    REFSEQ: accession NM_001037980.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Kurabe,N., Katagiri,K., Komiya,Y., Ito,R., Sugiyama,A., Kawasaki,Y.
            and Tashiro,F.
  TITLE     Deregulated expression of a novel component of TFTC/STAGA histone
            acetyltransferase complexes, rat SGF29, in hepatocellular
            carcinoma: possible implication for the oncogenic potential of
            c-Myc
  JOURNAL   Oncogene 26 (38), 5626-5634 (2007)
   PUBMED   17334388
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158713.1.
            
            On May 30, 2008 this sequence version replaced NP_001033069.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158713.1, SRR8487231.43484.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..335
                     /product="transcriptional adapter 1"
                     /note="transcriptional adaptor 1- like; transcriptional
                     adapter 1-like protein; transcriptional adaptor 1 (HFI1
                     homolog, yeast) like"
                     /calculated_mol_wt=37345
     Region          7..193
                     /region_name="SAGA-Tad1"
                     /note="Transcriptional regulator of RNA polII, SAGA,
                     subunit; pfam12767"
                     /db_xref="CDD:463692"
     Region          145..227
                     /region_name="HFD_TADA1"
                     /note="histone-fold domain found in transcriptional
                     adapter 1 (TADA1) and similar proteins; cd22934"
                     /db_xref="CDD:467058"
     CDS             1..335
                     /gene="Tada1"
                     /gene_synonym="RGD1306774; Tada1l"
                     /coded_by="NM_001037980.2:103..1110"
                     /db_xref="GeneID:360874"
                     /db_xref="RGD:1306774"
ORIGIN      
        1 matfvselea akknlsealg dnvkqywanl klwfkqkisk eefdleahrl ltqdnvhshn
       61 dfllailtrc qilvstpega gslpwtggsa akpgkpkgkk klssvrqkfd hrfqpqnpls
      121 gaqqfvakdp qddddlklcs htmmlptrgq legrmivtay ehgldnvtee avsavvyave
      181 nhlkdiltsv vsrrkayrvr dghfkyafgs nvtpqpylkn svvaynnlve gppafpapca
      241 sqnpashpht ddaeqqaafl lacsgdtlpa slppvnmydl fealqvhrev ipthtvyaln
      301 ieriimklwh pnheelqqdk vhrqrlaake glllc
//
LOCUS       NP_001029280             246 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF2 [Rattus norvegicus].
ACCESSION   NP_001029280 XP_576195
VERSION     NP_001029280.1
DBSOURCE    REFSEQ: accession NM_001034108.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Fukuda,H., Nakamura,N. and Hirose,S.
  TITLE     MARCH-III Is a novel component of endosomes with properties similar
            to those of MARCH-II
  JOURNAL   J Biochem 139 (1), 137-145 (2006)
   PUBMED   16428329
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Nakamura,N., Fukuda,H., Kato,A. and Hirose,S.
  TITLE     MARCH-II is a syntaxin-6-binding protein involved in endosomal
            trafficking
  JOURNAL   Mol Biol Cell 16 (4), 1696-1710 (2005)
   PUBMED   15689499
  REMARK    GeneRIF: Depletion of MARCH-II by small interfering RNA perturbed
            the trans-Golgi network (TGN) localization of syntaxin 6 and
            TGN38/46
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI578941.1 and BC088286.1.
            
            On Oct 14, 2005 this sequence version replaced XP_576195.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC088286.1, AB048838.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5756307, SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..246
                     /product="E3 ubiquitin-protein ligase MARCHF2"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase MARCH2;
                     syntaxin-6-binding protein; membrane associated RING-CH
                     finger protein II; membrane-associated RING-CH protein II;
                     membrane-associated RING finger protein 2;
                     membrane-associated ring finger (C3HC4) 2, E3 ubiquitin
                     protein ligase; RING-type E3 ubiquitin transferase MARCH2;
                     RING-type E3 ubiquitin transferase MARCHF2; RING finger
                     protein 172"
                     /calculated_mol_wt=27038
     Region          62..113
                     /region_name="RING_CH-C4HC3_MARCH2"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH2 (MARCH2); cd16808"
                     /db_xref="CDD:319722"
     Region          121..246
                     /region_name="Required for interaction with IKBKG.
                     /evidence=ECO:0000250|UniProtKB:Q9P0N8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0I2.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0I2.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0I2.1)"
     CDS             1..246
                     /gene="Marchf2"
                     /gene_synonym="MARCH-II; March2; RGD1306395; RNF172"
                     /coded_by="NM_001034108.1:80..820"
                     /db_xref="GeneID:362849"
                     /db_xref="RGD:1306395"
ORIGIN      
        1 mttgdcchlp gslcdcsssp afskvveatg lgppqyvaqv tsrdgrllst viraldtpsd
       61 cpfcricheg angenllspc gctgtlgavh ksclekwlss sntsycelch tefavekrpr
      121 pltewlkdpg prtekrtlcc dmvcfvfitp laaisgwlcl rgaqdhlrlh srleavglia
      181 ltialftiyv lwtlvsfryh cqlysewrkt nqkvrlkire adgsedphhs llatgllkkv
      241 aeetpv
//
LOCUS       NP_037189                295 aa            linear   ROD 27-APR-2025
DEFINITION  tissue factor precursor [Rattus norvegicus].
ACCESSION   NP_037189
VERSION     NP_037189.2
DBSOURCE    REFSEQ: accession NM_013057.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wu,D., Lin,Y., Yang,M., Li,H., Wang,W., Wu,Q., Chen,M., Shao,N. and
            Deng,C.
  TITLE     Tissue factor regulates autophagy in pulmonary artery endothelial
            cells from chronic thromboembolic pulmonary hypertension rats via
            the p38 MAPK-FoxO1 pathway
  JOURNAL   Respir Res 25 (1), 261 (2024)
   PUBMED   38943142
  REMARK    GeneRIF: Tissue factor regulates autophagy in pulmonary artery
            endothelial cells from chronic thromboembolic pulmonary
            hypertension rats via the p38 MAPK-FoxO1 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Jang,Y.J., Kim,H.K., Choi,B.C., Song,S.J., Park,J.I., Chun,S.Y. and
            Cho,M.K.
  TITLE     Expression of tissue factor and tissue factor pathway inhibitors
            during ovulation in rats: a relevance to the ovarian
            hyperstimulation syndrome
  JOURNAL   Reprod Biol Endocrinol 19 (1), 52 (2021)
   PUBMED   33794911
  REMARK    GeneRIF: Expression of tissue factor and tissue factor pathway
            inhibitors during ovulation in rats: a relevance to the ovarian
            hyperstimulation syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Ramlall,V., Thangaraj,P.M., Meydan,C., Foox,J., Butler,D., Kim,J.,
            May,B., De Freitas,J.K., Glicksberg,B.S., Mason,C.E.,
            Tatonetti,N.P. and Shapira,S.D.
  TITLE     Immune complement and coagulation dysfunction in adverse outcomes
            of SARS-CoV-2 infection
  JOURNAL   Nat Med 26 (10), 1609-1615 (2020)
   PUBMED   32747830
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Wan,S., Xiang,Y., Fang,W., Zheng,Y., Li,B., Hu,Y., Lang,C.,
            Huang,D., Sun,Q., Xiong,Y., Huang,X., Lv,J., Luo,Y., Shen,L.,
            Yang,H., Huang,G. and Yang,R.
  TITLE     Clinical features and treatment of COVID-19 patients in northeast
            Chongqing
  JOURNAL   J Med Virol 92 (7), 797-806 (2020)
   PUBMED   32198776
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Chen,F., Jiang,Y., Liu,S.L., Zou,L.H., Cao,Y. and Zhu,Y.M.
  TITLE     The expression changes and correlation analysis of high mobility
            group box-1 and tissue factor in the serum of rats with sepsis
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (4), 1634-1640 (2019)
   PUBMED   30840287
  REMARK    GeneRIF: expression levels of HMGB-1 and tissue factor (TF) of the
            rats with sepsis gradually increased with time, and the level of
            HMGB-1 was positively correlated with the level of TF
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Bauer,K.A., Conway,E.M., Bach,R., Konigsberg,W.H., Griffin,J.D. and
            Demetri,G.
  TITLE     Tissue factor gene expression in acute myeloblastic leukemia
  JOURNAL   Thromb Res 56 (3), 425-430 (1989)
   PUBMED   2617479
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Wilcox,J.N., Smith,K.M., Schwartz,S.M. and Gordon,D.
  TITLE     Localization of tissue factor in the normal vessel wall and in the
            atherosclerotic plaque
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2839-2843 (1989)
   PUBMED   2704749
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Andoh,K., Kubota,T., Takada,M., Tanaka,H., Kobayashi,N. and
            Maekawa,T.
  TITLE     Tissue factor activity in leukemia cells. Special reference to
            disseminated intravascular coagulation
  JOURNAL   Cancer 59 (4), 748-754 (1987)
   PUBMED   3802033
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Guha,A., Bach,R., Konigsberg,W. and Nemerson,Y.
  TITLE     Affinity purification of human tissue factor: interaction of factor
            VII and tissue factor in detergent micelles
  JOURNAL   Proc Natl Acad Sci U S A 83 (2), 299-302 (1986)
   PUBMED   3455766
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Zacharski,L.R., Rosenstein,R., Cornwell,G.G. 3rd, Davis,W.M. and
            McIntyre,O.R.
  TITLE     Reduced tissue factor (thromboplastin) activity in von Willebrand's
            disease
  JOURNAL   Am J Med 57 (1), 102-107 (1974)
   PUBMED   4546024
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081846.1.
            
            On Sep 16, 2004 this sequence version replaced NP_037189.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081846.1, U07619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132292
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..295
                     /product="tissue factor precursor"
                     /note="tissue factor; coagulation factor 3; coagulation
                     factor III (thromboplastin, tissue factor)"
                     /calculated_mol_wt=30567
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2953
     Region          13..111
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     mat_peptide     29..295
                     /product="Tissue factor. /id=PRO_0000033641"
                     /note="propagated from UniProtKB/Swiss-Prot (P42533.1)"
                     /calculated_mol_wt=30567
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Region          139..246
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; pfam09294"
                     /db_xref="CDD:462746"
     Site            170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42533.1)"
     Region          246..248
                     /region_name="WKS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42533.1)"
     Site            253..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42533.1)"
     CDS             1..295
                     /gene="F3"
                     /gene_synonym="TF"
                     /coded_by="NM_013057.2:97..984"
                     /db_xref="GeneID:25584"
                     /db_xref="RGD:2587"
ORIGIN      
        1 maipmrprll aalaptflgf lllqvaagag tppgkafnlt wistdfktil ewqpkptnyt
       61 ytvqisdrsr nwkykctgtt dtecdltdei vkdvnwtyea rvlsvpwrns thgketlfgt
      121 hgeeppftna rkflpyrdtk igqpviqkye qdgtklkvtv kdsftlvrkn gtfltlrqvf
      181 gndlgyilty rkdsstgrkt ntthtnefli dvekgvsycf fvqavifsrk tnhkspesit
      241 kcteqwksvl getliivgav vflvtvfiil ltislckrrk nragqkrknt psrla
//
LOCUS       NP_001029247             248 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.13 [Rattus norvegicus].
ACCESSION   NP_001029247
VERSION     NP_001029247.1
DBSOURCE    REFSEQ: accession NM_001034075.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO562261.1, AF372215.1,
            X02412.1 and AA899493.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.13, also known as variant 9)
            has multiple differences in the coding region, compared to variant
            1. These differences result in an isoform (Tpm1.13) that is shorter
            and has distinct N- and C- termini compared to isoform a. Isoform
            Tpm1.13 is the same length as isoforms Tpm1.8cy and Tpm1.9cy but is
            the product of alternate splicing and contains short regions of
            sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF372215.1, SRR8487226.183075.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform Tpm1.13"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=28398
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034075.1:152..898"
                     /note="isoform Tpm1.13 is encoded by transcript variant
                     Tpm1.13"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeerags lqreldqerk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedkyeeeik vlsdklkeae traefaersv tkleksiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_001104584             905 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001104584
VERSION     NP_001104584.1
DBSOURCE    REFSEQ: accession NM_001111114.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Jack,A., Hamad,M.I.K., Gonda,S., Gralla,S., Pahl,S., Hollmann,M.
            and Wahle,P.
  TITLE     Development of Cortical Pyramidal Cell and Interneuronal Dendrites:
            a Role for Kainate Receptor Subunits and NETO1
  JOURNAL   Mol Neurobiol 56 (7), 4960-4979 (2019)
   PUBMED   30421168
  REMARK    GeneRIF: Gluk1 and NETO1 specifically promote dendrite growth of
            interneurons in the visual cortex.
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Duan,G.F., Ye,Y., Xu,S., Tao,W., Zhao,S., Jin,T., Nicoll,R.A.,
            Shi,Y.S. and Sheng,N.
  TITLE     Signal peptide represses GluK1 surface and synaptic trafficking
            through binding to amino-terminal domain
  JOURNAL   Nat Commun 9 (1), 4879 (2018)
   PUBMED   30451858
  REMARK    GeneRIF: Signal peptide represses GluK1 surface and synaptic
            trafficking through binding to amino-terminal domain.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 905)
  AUTHORS   Sheng,N., Shi,Y.S. and Nicoll,R.A.
  TITLE     Amino-terminal domains of kainate receptors determine the
            differential dependence on Neto auxiliary subunits for trafficking
  JOURNAL   Proc Natl Acad Sci U S A 114 (5), 1159-1164 (2017)
   PUBMED   28100490
  REMARK    GeneRIF: In the CA1 hippocampal pyramidal cell, GluK1 had no effect
            on synaptic transmission. GluK1 which requires the auxiliary
            subunits Neto1 and Neto2 for surface and synaptic trafficking. It
            is the amino-terminal domains of GluK1 and GluK2 that control their
            strikingly different trafficking properties.
REFERENCE   5  (residues 1 to 905)
  AUTHORS   Fisher,M.T. and Fisher,J.L.
  TITLE     Contributions of different kainate receptor subunits to the
            properties of recombinant homomeric and heteromeric receptors
  JOURNAL   Neuroscience 278, 70-80 (2014)
   PUBMED   25139762
REFERENCE   6  (residues 1 to 905)
  AUTHORS   Sailer,A., Swanson,G.T., Perez-Otano,I., O'Leary,L., Malkmus,S.A.,
            Dyck,R.H., Dickinson-Anson,H., Schiffer,H.H., Maron,C., Yaksh,T.L.,
            Gage,F.H., O'Gorman,S. and Heinemann,S.F.
  TITLE     Generation and analysis of GluR5(Q636R) kainate receptor mutant
            mice
  JOURNAL   J Neurosci 19 (20), 8757-8764 (1999)
   PUBMED   10516295
REFERENCE   7  (residues 1 to 905)
  AUTHORS   Brakeman,P.R., Lanahan,A.A., O'Brien,R., Roche,K., Barnes,C.A.,
            Huganir,R.L. and Worley,P.F.
  TITLE     Homer: a protein that selectively binds metabotropic glutamate
            receptors
  JOURNAL   Nature 386 (6622), 284-288 (1997)
   PUBMED   9069287
REFERENCE   8  (residues 1 to 905)
  AUTHORS   Lomeli,H., Wisden,W., Kohler,M., Keinanen,K., Sommer,B. and
            Seeburg,P.H.
  TITLE     High-affinity kainate and domoate receptors in rat brain
  JOURNAL   FEBS Lett 307 (2), 139-143 (1992)
   PUBMED   1322826
REFERENCE   9  (residues 1 to 905)
  AUTHORS   Sommer,B., Burnashev,N., Verdoorn,T.A., Keinanen,K., Sakmann,B. and
            Seeburg,P.H.
  TITLE     A glutamate receptor channel with high affinity for domoate and
            kainate
  JOURNAL   EMBO J 11 (4), 1651-1656 (1992)
   PUBMED   1373382
REFERENCE   10 (residues 1 to 905)
  AUTHORS   Bettler,B., Boulter,J., Hermans-Borgmeyer,I., O'Shea-Greenfield,A.,
            Deneris,E.S., Moll,C., Borgmeyer,U., Hollmann,M. and Heinemann,S.
  TITLE     Cloning of a novel glutamate receptor subunit, GluR5: expression in
            the nervous system during development
  JOURNAL   Neuron 5 (5), 583-595 (1990)
   PUBMED   1977421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M83561.1, JAXUCZ010000011.1 and
            AI145540.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) is missing two in-frame coding
            exons compared to transcript variant 1, resulting in a shorter
            isoform (3) lacking two protein segments of 15 aa and 29 aa,
            compared to isoform 1. RNA editing (CAG->CGG) changes Gln621Arg.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M83561.1, SRR26643298.66033.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            undergoes RNA editing  :: PMID: 10516295
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..905
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     3"
                     /note="glutamate receptor 5; glutamate receptor
                     ionotropic, kainate 1"
                     /calculated_mol_wt=102655
     Region          38..416
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Region          431..800
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..905
                     /gene="Grik1"
                     /gene_synonym="GluK1; GluR5"
                     /coded_by="NM_001111114.1:186..2903"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:29559"
                     /db_xref="RGD:2732"
ORIGIN      
        1 merstvliqp glwtrdtswt llyflcyilp qtspqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dsrdlfyinl ypdyaaisra vldlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlppank dakpllkemk kskefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltgritfnk tdglrkdfdl diislkeegt ekigiwnsns glnmtdgnrd
      421 rsnnitdsla nrtlivttil eepyvmyrks dkplygndrf egycldllke lsnilgflyd
      481 vklvpdgkyg aqndkgewng mvkelidhra dlavapltit yvrekvidfs kpfmtlgisi
      541 lyrkpngtnp gvfsflnpls pdiwmyvlla clgvscvlfv iarftpyewy nphpcnpdsd
      601 vvennftlln sfwfgvgalm qqgselmpka lstrivggiw wfftliiiss ytanlaaflt
      661 vermespids addlakqtki eygavrdgst mtffkkskis tyekmwafms srqqsalvkn
      721 sdegiqrvlt tdyallmest sieyvtqrnc nltqigglid skgygvgtpi gspyrdkiti
      781 ailqlqeegk lhmmkekwwr gngcpeedsk easalgveni ggifivlaag lvlsvfvaig
      841 eflyksrknn dveqclsfna imeelgislk nqkklkkksr tkgkssftsi ltchqrrtqr
      901 ketva
//
LOCUS       NP_001037762             418 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 61 [Rattus norvegicus].
ACCESSION   NP_001037762 XP_001073284
VERSION     NP_001037762.1
DBSOURCE    REFSEQ: accession NM_001044297.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082099.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001073284.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082099.1, CK603586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..418
                     /product="ankyrin repeat domain-containing protein 61"
                     /calculated_mol_wt=46189
     Region          27..57
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          74..103
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          <78..>118
                     /region_name="PHA03095"
                     /note="ankyrin-like protein; Provisional"
                     /db_xref="CDD:222980"
     Region          78..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          107..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          131..160
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          136..334
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          166..195
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Site            order(168,172..173,176..178,180..181,185,188,197,199,201,
                     205..206,232..234,257..258,262,265,274,276,278,282..283,
                     286..288,290..291,295,298)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          168..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..274
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          199..228
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          233..272
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          276..305
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          276..305
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     Region          309..342
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641X1.1)"
     CDS             1..418
                     /gene="Ankrd61"
                     /coded_by="NM_001044297.1:41..1297"
                     /db_xref="GeneID:689907"
                     /db_xref="RGD:1586393"
ORIGIN      
        1 mgnitkrgsr dfaadsavll egslatalhs rlyeaiiked cdtirtllrn hpvnqpltll
       61 asstgyrfls qqtqpifpih laaeyrkpqs llcllqhgad pevrdaqglt tlhlmllnwp
      121 vtsttwtkps triqkiltdi qnnavlclri lcdhgaqvna rvdnsnkhsp lhlaitygty
      181 pvlsflaqng aqvnainess mtplhmaadi lnknmietli acganvncai sstgntalkl
      241 avctasskag rllaagvgci rlllnhgaqv naqdhegqta lheacfggre viinlllefe
      301 anvniltrng espiymylqr ssnirdvtll arllyrtypl rlsnkqgalp agimlpefhl
      361 lretliklsk kpltleaick rnirnvygek ykfqlkkllp aklwnsiygi ydftyllk
//
LOCUS       NP_001007599             192 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL6 [Rattus norvegicus].
ACCESSION   NP_001007599 XP_341214
VERSION     NP_001007599.3
DBSOURCE    REFSEQ: accession NM_001007598.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 192)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Angelastro,J.M., Torocsik,B. and Greene,L.A.
  TITLE     Nerve growth factor selectively regulates expression of transcripts
            encoding ribosomal proteins
  JOURNAL   BMC Neurosci 3, 3 (2002)
   PUBMED   11922865
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Monach,P.A., Meredith,S.C., Siegel,C.T. and Schreiber,H.
  TITLE     A unique tumor antigen produced by a single amino acid substitution
  JOURNAL   Immunity 2 (1), 45-59 (1995)
   PUBMED   7600302
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Suzuki,K., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L9
  JOURNAL   Gene 93 (2), 297-300 (1990)
   PUBMED   2227441
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Tsurugi,K., Collatz,E., Wool,E.G. and Lin,A.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 60 S ribosomal subunit proteins L4, L5, L7,
            L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37,
            and L39
  JOURNAL   J Biol Chem 251 (24), 7940-7946 (1976)
   PUBMED   1002715
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC060589.1 and BC086561.1.
            
            On Apr 13, 2007 this sequence version replaced NP_001007599.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060589.1, CB314568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..192
                     /product="large ribosomal subunit protein uL6"
                     /note="60S ribosomal protein L9"
                     /calculated_mol_wt=21762
     Region          1..189
                     /region_name="PTZ00027"
                     /note="60S ribosomal protein L6; Provisional"
                     /db_xref="CDD:240234"
     Site            121
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P32969; propagated from
                     UniProtKB/Swiss-Prot (P17077.1)"
     CDS             1..192
                     /gene="Rpl9"
                     /coded_by="NM_001007598.3:25..603"
                     /db_xref="GeneID:29257"
                     /db_xref="RGD:62049"
ORIGIN      
        1 mktilsnqtv dipenvditl kgrtvivkgp rgtlrrdfnh invelsllgk kkkrlrvdkw
       61 wgnrkelatv rticshvqnm ikgvtlgfry kmrsvyahfp invviqengs lveirnflge
      121 kyirrvrmrt gvacsvsqaq kdelilegnd ielvsnsaal iqqattvknk dirkfldgiy
      181 vsekgtvqqp de
//
LOCUS       NP_001028835             186 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase A-Raf isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001028835
VERSION     NP_001028835.1
DBSOURCE    REFSEQ: accession NM_001033663.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Huang,L.E., Cohen,A.L., Colman,H., Jensen,R.L., Fults,D.W. and
            Couldwell,W.T.
  TITLE     IGFBP2 expression predicts IDH-mutant glioma patient survival
  JOURNAL   Oncotarget 8 (1), 191-202 (2017)
   PUBMED   27852048
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Gan,X., Wang,J., Wang,C., Sommer,E., Kozasa,T., Srinivasula,S.,
            Alessi,D., Offermanns,S., Simon,M.I. and Wu,D.
  TITLE     PRR5L degradation promotes mTORC2-mediated PKC-delta
            phosphorylation and cell migration downstream of Galpha12
  JOURNAL   Nat Cell Biol 14 (7), 686-696 (2012)
   PUBMED   22609986
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Roskoski,R. Jr.
  TITLE     MEK1/2 dual-specificity protein kinases: structure and regulation
  JOURNAL   Biochem Biophys Res Commun 417 (1), 5-10 (2012)
   PUBMED   22177953
  REMARK    Review article
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Polzien,L., Baljuls,A., Rennefahrt,U.E.E., Fischer,A., Schmitz,W.,
            Zahedi,R.P., Sickmann,A., Metz,R., Albert,S., Benz,R., Hekman,M.
            and Rapp,U.R.
  TITLE     Identification of novel in vivo phosphorylation sites of the human
            proapoptotic protein BAD: pore-forming activity of BAD is regulated
            by phosphorylation
  JOURNAL   J Biol Chem 284 (41), 28004-28020 (2009)
   PUBMED   19667065
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Yokoyama,T., Takano,K., Yoshida,A., Katada,F., Sun,P., Takenawa,T.,
            Andoh,T. and Endo,T.
  TITLE     DA-Raf1, a competent intrinsic dominant-negative antagonist of the
            Ras-ERK pathway, is required for myogenic differentiation
  JOURNAL   J Cell Biol 177 (5), 781-793 (2007)
   PUBMED   17535970
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Gruppuso,P.A. and Boylan,J.M.
  TITLE     Hepatic epidermal growth factor-regulated mitogen-activated protein
            kinase kinase kinase activity in the rat: lack of identity with
            known forms of raf and MEKK
  JOURNAL   FEBS Lett 466 (1), 200-204 (2000)
   PUBMED   10648842
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Kim,S.O., Irwin,P., Katz,S. and Pelech,S.L.
  TITLE     Expression of mitogen-activated protein kinase pathways during
            postnatal development of rat heart
  JOURNAL   J Cell Biochem 71 (2), 286-301 (1998)
   PUBMED   9779826
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Ishikawa,F., Takaku,F., Nagao,M. and Sugimura,T.
  TITLE     The complete primary structure of the rat A-raf cDNA coding region:
            conservation of the putative regulatory regions present in rat
            c-raf
  JOURNAL   Oncogene Res 1 (3), 243-253 (1987)
   PUBMED   3449797
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Huleihel,M., Goldsborough,M., Cleveland,J., Gunnell,M., Bonner,T.
            and Rapp,U.R.
  TITLE     Characterization of murine A-raf, a new oncogene related to the
            v-raf oncogene
  JOURNAL   Mol Cell Biol 6 (7), 2655-2662 (1986)
   PUBMED   3491291
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Williams,A.F., Barclay,A.N., Letarte-Muirhead,M. and Morris,R.J.
  TITLE     Rat thy-1 antigens from thymus and brain: their tissue
            distribution, purification, and chemical composition
  JOURNAL   Cold Spring Harb Symp Quant Biol 41 Pt 1, 51-61 (1977)
   PUBMED   70317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO572305.1, AB158253.1, AI060060.1 and DV728203.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EV764730.1, FQ081576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132307, SAMEA5756307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..186
                     /product="serine/threonine-protein kinase A-Raf isoform 2"
                     /EC_number="2.7.11.1"
                     /note="v-raf murine sarcoma 3611 viral oncogene homolog 1;
                     v-raf oncogene homolog 1 (murine sarcoma 3611 virus); Raf
                     related protein; A-Raf proto-oncogene
                     serine/threonine-protein kinase; Ras-binding protein;
                     serine/threonine-protein kinase A-Raf; proto-oncogene
                     A-Raf; proto-oncogene A-Raf-1"
                     /calculated_mol_wt=20740
     Region          19..91
                     /region_name="RBD_ARAF"
                     /note="Ras-binding domain (RBD) found in
                     serine/threonine-protein kinase ARAF; cd17133"
                     /db_xref="CDD:340653"
     Site            order(20,22,27..32,34,47,51..53)
                     /site_type="other"
                     /note="putative RBD_Raf-Ras interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            order(20,27,29..32,47,50..53)
                     /site_type="other"
                     /note="RBD_Raf-KRas interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340653"
     Site            85
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:340653"
     Region          96..147
                     /region_name="C1_A_C-Raf"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma)
                     kinases, and similar proteins; cd20870"
                     /db_xref="CDD:410420"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10398; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14056.1)"
     CDS             1..186
                     /gene="Araf"
                     /gene_synonym="Araf1"
                     /coded_by="NM_001033663.2:111..671"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64363"
                     /db_xref="RGD:2148"
ORIGIN      
        1 mepprgppas gaepsravgt vkvylpnkqr tvvtvrdgms vydsldkalk vrglnqdccv
       61 vyrlikgrkt vtawdtaiap ldgeelivev ledvpltmhn fvrktffsla fcdfclkflf
      121 hgfrcqtcgy kfhqhcsskv ptvcvdmstn rrqfyhsiqd lsggsrqqev psnlsvnell
      181 tpqgpr
//
LOCUS       NP_542428                 89 aa            linear   ROD 27-APR-2025
DEFINITION  dynein light chain 2, cytoplasmic [Rattus norvegicus].
ACCESSION   NP_542428
VERSION     NP_542428.1
DBSOURCE    REFSEQ: accession NM_080697.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Suyama,S., Kodaira-Hirano,M., Otgon-Uul,Z., Ueta,Y., Nakata,M. and
            Yada,T.
  TITLE     Fasted/fed states regulate postsynaptic hub protein DYNLL2 and
            glutamatergic transmission in oxytocin neurons in the hypothalamic
            paraventricular nucleus
  JOURNAL   Neuropeptides 56, 115-123 (2016)
   PUBMED   26344333
  REMARK    GeneRIF: Results suggest that feeding increases excitatory synaptic
            input on paraventricular nucleus oxytocin neurons via mechanisms
            involving DYNLL2 upregulation and NMDA receptor-mediated synaptic
            reorganization.
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Goggolidou,P., Stevens,J.L., Agueci,F., Keynton,J., Wheway,G.,
            Grimes,D.T., Patel,S.H., Hilton,H., Morthorst,S.K., DiPaolo,A.,
            Williams,D.J., Sanderson,J., Khoronenkova,S.V., Powles-Glover,N.,
            Ermakov,A., Esapa,C.T., Romero,R., Dianov,G.L., Briscoe,J.,
            Johnson,C.A., Pedersen,L.B. and Norris,D.P.
  TITLE     ATMIN is a transcriptional regulator of both lung morphogenesis and
            ciliogenesis
  JOURNAL   Development 141 (20), 3966-3977 (2014)
   PUBMED   25294941
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Du,H., Grob,S.R., Zhao,L., Lee,J., El-Sahn,M., Hughes,G., Luo,J.,
            Schaf,K., Duan,Y., Quach,J., Wei,X., Shaw,P., Granet,D. and
            Zhang,K.
  TITLE     Myotonia congenita with strabismus in a large family with a
            mutation in the SCN4A gene
  JOURNAL   Eye (Lond) 26 (8), 1039-1043 (2012)
   PUBMED   22653516
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Moutin,E., Raynaud,F., Fagni,L. and Perroy,J.
  TITLE     GKAP-DLC2 interaction organizes the postsynaptic scaffold complex
            to enhance synaptic NMDA receptor activity
  JOURNAL   J Cell Sci 125 (Pt 8), 2030-2040 (2012)
   PUBMED   22328512
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Allan,V.J.
  TITLE     Cytoplasmic dynein
  JOURNAL   Biochem Soc Trans 39 (5), 1169-1178 (2011)
   PUBMED   21936784
  REMARK    Review article
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Day,C.L., Puthalakath,H., Skea,G., Strasser,A., Barsukov,I.,
            Lian,L.Y., Huang,D.C. and Hinds,M.G.
  TITLE     Localization of dynein light chains 1 and 2 and their pro-apoptotic
            ligands
  JOURNAL   Biochem J 377 (Pt 3), 597-605 (2004)
   PUBMED   14561217
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Wang,W., Lo,K.W., Kan,H.M., Fan,J.S. and Zhang,M.
  TITLE     Structure of the monomeric 8-kDa dynein light chain and mechanism
            of the domain-swapped dimer assembly
  JOURNAL   J Biol Chem 278 (42), 41491-41499 (2003)
   PUBMED   12904292
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Fuhrmann,J.C., Kins,S., Rostaing,P., El Far,O., Kirsch,J.,
            Sheng,M., Triller,A., Betz,H. and Kneussel,M.
  TITLE     Gephyrin interacts with Dynein light chains 1 and 2, components of
            motor protein complexes
  JOURNAL   J Neurosci 22 (13), 5393-5402 (2002)
   PUBMED   12097491
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Naisbitt,S., Valtschanoff,J., Allison,D.W., Sala,C., Kim,E.,
            Craig,A.M., Weinberg,R.J. and Sheng,M.
  TITLE     Interaction of the postsynaptic density-95/guanylate kinase
            domain-associated protein complex with a light chain of myosin-V
            and dynein
  JOURNAL   J Neurosci 20 (12), 4524-4534 (2000)
   PUBMED   10844022
REFERENCE   10 (residues 1 to 89)
  AUTHORS   King,S.M., Barbarese,E., Dillman,J.F. 3rd, Patel-King,R.S.,
            Carson,J.H. and Pfister,K.K.
  TITLE     Brain cytoplasmic and flagellar outer arm dyneins share a highly
            conserved Mr 8,000 light chain
  JOURNAL   J Biol Chem 271 (32), 19358-19366 (1996)
   PUBMED   8702622
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061874.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061874.1, BU671206.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132281, SAMD00132305
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..89
                     /product="dynein light chain 2, cytoplasmic"
                     /note="dynein light chain-2"
                     /calculated_mol_wt=10219
     Region          5..88
                     /region_name="DLC-like_DYNLL1_DYNLL2"
                     /note="dynein light chain (DLC)-like domain found in the
                     cytoplasmic dynein light chain 1 (DYNLL1) family; cd21452"
                     /db_xref="CDD:412000"
     Site            41
                     /site_type="other"
                     /note="Interaction with myosin V motor complex.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q78P75.1)"
     CDS             1..89
                     /gene="Dynll2"
                     /gene_synonym="Dlc2"
                     /coded_by="NM_080697.2:260..529"
                     /db_xref="GeneID:140734"
                     /db_xref="RGD:619860"
ORIGIN      
        1 msdrkavikn admsedmqqd avdcatqame kyniekdiaa yikkefdkky nptwhcivgr
       61 nfgsyvthet khfiyfylgq vaillfksg
//
LOCUS       NP_954546                405 aa            linear   ROD 27-APR-2025
DEFINITION  angiopoietin-related protein 4 precursor [Rattus norvegicus].
ACCESSION   NP_954546 XP_343183
VERSION     NP_954546.1
DBSOURCE    REFSEQ: accession NM_199115.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Kondo,S., Kojima,K., Nakamura,N., Miyabe,M., Kikuchi,T., Ohno,T.,
            Sawada,N., Minato,T., Saiki,T., Ito,M., Sasajima,S., Matsubara,T.,
            Mitani,A. and Naruse,K.
  TITLE     Increased expression of angiopoietin-like protein 4 regulates
            matrix metalloproteinase-13 expression in Porphyromonas gingivalis
            lipopolysaccharides-stimulated gingival fibroblasts and
            ligature-induced experimental periodontitis
  JOURNAL   J Periodontal Res 58 (1), 43-52 (2023)
   PUBMED   36409042
  REMARK    GeneRIF: Increased expression of angiopoietin-like protein 4
            regulates matrix metalloproteinase-13 expression in Porphyromonas
            gingivalis lipopolysaccharides-stimulated gingival fibroblasts and
            ligature-induced experimental periodontitis.
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Qiu,W., Huang,L., Li,Y., Liu,Q. and Lv,Y.
  TITLE     Dysregulation of Angiopoietin-like-4 Associated with
            Hyperlipidemia-induced Renal Injury by AMPK/ACC Pathway
  JOURNAL   Curr Pharm Des 29 (4), 300-309 (2023)
   PUBMED   36537603
  REMARK    GeneRIF: Dysregulation of Angiopoietin-like-4 Associated with
            Hyperlipidemia-induced Renal Injury by AMPK/ACC Pathway.
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Shen,X., Zhang,Y., Lin,C., Weng,C., Wang,Y., Feng,S., Wang,C.,
            Shao,X., Lin,W., Li,B., Wang,H., Chen,J. and Jiang,H.
  TITLE     Calcineurin inhibitors ameliorate PAN-induced podocyte injury
            through the NFAT-Angptl4 pathway
  JOURNAL   J Pathol 252 (3), 227-238 (2020)
   PUBMED   32686149
  REMARK    GeneRIF: Calcineurin inhibitors ameliorate PAN-induced podocyte
            injury through the NFAT-Angptl4 pathway.
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Guo,K., Pan,P., Wu,M., Ma,Y., Lu,J. and Chen,H.
  TITLE     Hyposialylated angiopoietin-like-4 induces apoptosis of podocytes
            via beta1 Integrin/FAK signaling in diabetic nephropathy
  JOURNAL   Mol Cell Endocrinol 505, 110730 (2020)
   PUBMED   31981598
  REMARK    GeneRIF: Hyposialylated angiopoietin-like-4 induces apoptosis of
            podocytes via beta1 Integrin/FAK signaling in diabetic nephropathy.
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Yang,X., Cao,J., Du,Y., Gong,Q., Cheng,Y. and Su,G.
  TITLE     Angiopoietin-Like Protein 4 (ANGPTL4) Induces Retinal Pigment
            Epithelial Barrier Breakdown by Activating Signal Transducer and
            Activator of Transcription 3 (STAT3): Evidence from ARPE-19 Cells
            Under Hypoxic Condition and Diabetic Rats
  JOURNAL   Med Sci Monit 25, 6742-6754 (2019)
   PUBMED   31494661
  REMARK    GeneRIF: ANGPTL4 partially modulates STAT3 and could serve as an
            effective diabetic retinopathy treatment strategy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Xu,A., Lam,M.C., Chan,K.W., Wang,Y., Zhang,J., Hoo,R.L., Xu,J.Y.,
            Chen,B., Chow,W.S., Tso,A.W. and Lam,K.S.
  TITLE     Angiopoietin-like protein 4 decreases blood glucose and improves
            glucose tolerance but induces hyperlipidemia and hepatic steatosis
            in mice
  JOURNAL   Proc Natl Acad Sci U S A 102 (17), 6086-6091 (2005)
   PUBMED   15837923
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Ge,H., Yang,G., Huang,L., Motola,D.L., Pourbahrami,T. and Li,C.
  TITLE     Oligomerization and regulated proteolytic processing of
            angiopoietin-like protein 4
  JOURNAL   J Biol Chem 279 (3), 2038-2045 (2004)
   PUBMED   14570927
REFERENCE   8  (residues 1 to 405)
  AUTHORS   Yoshida,K., Shimizugawa,T., Ono,M. and Furukawa,H.
  TITLE     Angiopoietin-like protein 4 is a potent hyperlipidemia-inducing
            factor in mice and inhibitor of lipoprotein lipase
  JOURNAL   J Lipid Res 43 (11), 1770-1772 (2002)
   PUBMED   12401877
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Yoon,J.C., Chickering,T.W., Rosen,E.D., Dussault,B., Qin,Y.,
            Soukas,A., Friedman,J.M., Holmes,W.E. and Spiegelman,B.M.
  TITLE     Peroxisome proliferator-activated receptor gamma target gene
            encoding a novel angiopoietin-related protein associated with
            adipose differentiation
  JOURNAL   Mol Cell Biol 20 (14), 5343-5349 (2000)
   PUBMED   10866690
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Kim,I., Kim,H.G., Kim,H., Kim,H.H., Park,S.K., Uhm,C.S., Lee,Z.H.
            and Koh,G.Y.
  TITLE     Hepatic expression, synthesis and secretion of a novel
            fibrinogen/angiopoietin-related protein that prevents
            endothelial-cell apoptosis
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 603-610 (2000)
   PUBMED   10698685
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078944.1.
            
            On Jan 1, 2004 this sequence version replaced XP_343183.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078944.1, AY393999.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..405
                     /product="angiopoietin-related protein 4 precursor"
                     /note="angiopoietin-related protein 4; HFARP; hepatic
                     fibrinogen/angiopoietin-related protein; angiopoietin-like
                     protein 4"
                     /calculated_mol_wt=42836
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6TMA8.1)"
                     /calculated_mol_wt=2133
     mat_peptide     24..405
                     /product="Angiopoietin-related protein 4.
                     /id=PRO_0000009126"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TMA8.1)"
                     /calculated_mol_wt=42836
     Site            163..164
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q9BY76;
                     propagated from UniProtKB/Swiss-Prot (Q6TMA8.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6TMA8.1)"
     Region          182..399
                     /region_name="FReD"
                     /note="Fibrinogen-related domains (FReDs); C terminal
                     globular domain of fibrinogen. Fibrinogen is involved in
                     blood clotting, being activated by thrombin to assemble
                     into fibrin clots. The N-termini of 2 times 3 chains come
                     together to form a globular...; cd00087"
                     /db_xref="CDD:238040"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6TMA8.1)"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6TMA8.1)"
     Site            300
                     /site_type="other"
                     /note="gamma-gamma dimer interface [polypeptide binding]"
                     /db_xref="CDD:238040"
     Site            order(331,333,335)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238040"
     Site            order(340,343..344,353..354)
                     /site_type="active"
                     /note="polymerization pocket [active]"
                     /db_xref="CDD:238040"
     CDS             1..405
                     /gene="Angptl4"
                     /coded_by="NM_199115.2:141..1358"
                     /db_xref="GeneID:362850"
                     /db_xref="RGD:735058"
ORIGIN      
        1 mrcaptagaa lvlcaatagl lsaqgrpaqp epprfaswde mnllahgllq lghglrehve
       61 rtrgqlgale rrmaacgnac qgpkgtdpkd rvpegqapet lqslqtqlka qnskiqqlfq
      121 kvaqqqryls kqnlriqnlq sqidlltpth ldngvdktsr gkrlpkmaql igltpnatrl
      181 hrpprdcqel fqegerhsgl fqiqplgspp flvncemtsd ggwtviqrrl ngsvdfnqsw
      241 eaykdgfgdp qgefwlglek mhsitgdrgs qlavqlqdwd gnakllqfpi hlggedtays
      301 lqlteptane lgatnvspng lslpfstwdq dhdlrgdlnc akslsggwwf gtcshsnlng
      361 qyfhsiprqr qqrkkgifwk twkgryyplq attlliqpme ataas
//
LOCUS       NP_445961                617 aa            linear   ROD 27-APR-2025
DEFINITION  zona pellucida sperm-binding protein 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_445961 XP_001074922 XP_001075428
VERSION     NP_445961.1
DBSOURCE    REFSEQ: accession NM_053509.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Lv,C., Huang,H.L., Yi,D.J., Peng,T.L., Tan,H.J., Quan,R.P.,
            Deng,H.W. and Xiao,H.M.
  TITLE     Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the zona
            pellucida, resulting in zona absence and female infertility in
            ratsdagger
  JOURNAL   Biol Reprod 104 (6), 1262-1270 (2021)
   PUBMED   33624742
  REMARK    GeneRIF: Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the
            zona pellucida, resulting in zona absence and female infertility in
            ratsdagger.
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Dai,C., Hu,L., Gong,F., Tan,Y., Cai,S., Zhang,S., Dai,J., Lu,C.,
            Chen,J., Chen,Y., Lu,G., Du,J. and Lin,G.
  TITLE     ZP2 pathogenic variants cause in vitro fertilization failure and
            female infertility
  JOURNAL   Genet Med 21 (2), 431-440 (2019)
   PUBMED   29895852
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Boja,E.S., Hoodbhoy,T., Garfield,M. and Fales,H.M.
  TITLE     Structural conservation of mouse and rat zona pellucida
            glycoproteins. Probing the native rat zona pellucida proteome by
            mass spectrometry
  JOURNAL   Biochemistry 44 (50), 16445-16460 (2005)
   PUBMED   16342937
REFERENCE   4  (residues 1 to 617)
  AUTHORS   El-Mestrah,M., Castle,P.E., Borossa,G. and Kan,F.W.
  TITLE     Subcellular distribution of ZP1, ZP2, and ZP3 glycoproteins during
            folliculogenesis and demonstration of their topographical
            disposition within the zona matrix of mouse ovarian oocytes
  JOURNAL   Biol Reprod 66 (4), 866-876 (2002)
   PUBMED   11906903
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Akatsuka,K., Yoshida-Komiya,H., Tulsiani,D.R., Orgebin-Crist,M.C.,
            Hiroi,M. and Araki,Y.
  TITLE     Rat zona pellucida glycoproteins: molecular cloning and
            characterization of the three major components
  JOURNAL   Mol Reprod Dev 51 (4), 454-467 (1998)
   PUBMED   9820205
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB000928.1.
            
            On or before Oct 23, 2008 this sequence version replaced
            XP_001074922.1, XP_001075428.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00155321,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..617
                     /product="zona pellucida sperm-binding protein 1
                     precursor"
                     /note="zona pellucida sperm-binding protein 1; zp-1; zona
                     pellucida glycoprotein 1 (sperm receptor)"
                     /calculated_mol_wt=65729
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2143
     mat_peptide     21..544
                     /product="Zona pellucida sperm-binding protein 1.
                     /id=PRO_0000041681"
                     /note="propagated from UniProtKB/Swiss-Prot (O54766.1)"
                     /calculated_mol_wt=57998
     Site            21
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54766.1)"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54766.1)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54766.1)"
     Region          179..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54766.1)"
     Region          224..266
                     /region_name="PD"
                     /note="P or trefoil or TFF domain; smart00018"
                     /db_xref="CDD:197472"
     Site            order(238,258..259)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(253,258)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     Region          269..539
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            369
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54766.1)"
     Site            589..609
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O54766.1)"
     CDS             1..617
                     /gene="Zp1"
                     /gene_synonym="ZP1-202"
                     /coded_by="NM_053509.1:36..1889"
                     /db_xref="GeneID:85271"
                     /db_xref="RGD:620604"
ORIGIN      
        1 mawgcfvvll llvaaplrlg qhlhlkpgfq ysydcgvqgm qllvfprpnq tiqfkvldef
       61 gnrfevnncs icyhwvisea qkpavfsady kgchvlekqd grfhlrvfiq avlpngrvdt
      121 aqdvtlicpk pdhiltpesy lappttpqpf iphtfalhpi sghtlagsgh tglttlypet
      181 hptpappsse pgpvgptvpq sqwgtlgswe lteldsigth llqercqvas ghipcmvkgs
      241 seeacqqagc cydntkempc yygntvtlqc frsgyftlvm sqetalthgv mldnvhlaya
      301 pngcpptqkt safvvfhvpl tlcgtaiqvv gkqlvyenql vsnievqtgp qgsitrdgvf
      361 rlhvrcifna sdflpirasi fspqppapvt rsgplrlelr iatdktfssy yqgsdyplvr
      421 llqepvyiev rllqrtdpgl almlhqcwat psaspfeqpq wpilsdgcpf kgdnyrtqmv
      481 aadratlpfw shyqrftiat ftlldsssqn alrgqvyffc sasachpvgs etcsttcdse
      541 iarhrrssgh hnstiraldi vsspgavgfe dapklepsgs trnsgsrpll wvlqllaltl
      601 vlgdgvlvgl swawawa
//
LOCUS       NP_113747                773 aa            linear   ROD 27-APR-2025
DEFINITION  carnitine O-palmitoyltransferase 1, liver isoform [Rattus
            norvegicus].
ACCESSION   NP_113747
VERSION     NP_113747.2
DBSOURCE    REFSEQ: accession NM_031559.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Yan,J., Song,K., Bai,Z. and Ge,R.L.
  TITLE     WY14643 improves left ventricular myocardial mitochondrial and
            systolic functions in obese rats under chronic persistent hypoxia
            via the PPARalpha pathway
  JOURNAL   Life Sci 266, 118888 (2021)
   PUBMED   33310031
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Lin,L., Hao,Z., Zhang,S., Shi,L., Lu,B., Xu,H. and Ji,L.
  TITLE     Study on the protection of water extracts of Polygoni Multiflori
            Radix and Polygoni Multiflori Radix Praeparata against NAFLD and
            its mechanism
  JOURNAL   J Ethnopharmacol 252, 112577 (2020)
   PUBMED   31953200
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Liu,M.E., Chou,C.H., Li,L., Wu,Y.S., Lin,Y.L., Tu,D.G. and
            Chen,Y.C.
  TITLE     Modulation effects of black-vinegar-based supplement against a
            high-fat dietary habit: antiobesity/hypolipidemic, antioxidative,
            and energy-metabolism effects
  JOURNAL   J Sci Food Agric 100 (6), 2380-2388 (2020)
   PUBMED   31901136
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Huo,X., Meng,X., Zhang,J. and Zhao,Y.
  TITLE     Hepatoprotective effect of different combinations of 18alpha-and
            18beta-Glycyrrhizic acid against CCl4-induced liver injury in rats
  JOURNAL   Biomed Pharmacother 122, 109354 (2020)
   PUBMED   31918260
REFERENCE   5  (residues 1 to 773)
  AUTHORS   Wu,Z., Zhang,Y., Gong,X., Cheng,G., Pu,S. and Cai,S.
  TITLE     The preventive effect of phenolic-rich extracts from Chinese sumac
            fruits against nonalcoholic fatty liver disease in rats induced by
            a high-fat diet
  JOURNAL   Food Funct 11 (1), 799-812 (2020)
   PUBMED   31930271
REFERENCE   6  (residues 1 to 773)
  AUTHORS   Esser,V., Brown,N.F., Cowan,A.T., Foster,D.W. and McGarry,J.D.
  TITLE     Expression of a cDNA isolated from rat brown adipose tissue and
            heart identifies the product as the muscle isoform of carnitine
            palmitoyltransferase I (M-CPT I). M-CPT I is the predominant CPT I
            isoform expressed in both white (epididymal) and brown adipocytes
  JOURNAL   J Biol Chem 271 (12), 6972-6977 (1996)
   PUBMED   8636126
REFERENCE   7  (residues 1 to 773)
  AUTHORS   Britton,C.H., Schultz,R.A., Zhang,B., Esser,V., Foster,D.W. and
            McGarry,J.D.
  TITLE     Human liver mitochondrial carnitine palmitoyltransferase I:
            characterization of its cDNA and chromosomal localization and
            partial analysis of the gene
  JOURNAL   Proc Natl Acad Sci U S A 92 (6), 1984-1988 (1995)
   PUBMED   7892212
REFERENCE   8  (residues 1 to 773)
  AUTHORS   Kolodziej,M.P. and Zammit,V.A.
  TITLE     Mature carnitine palmitoyltransferase I retains the N-terminus of
            the nascent protein in rat liver
  JOURNAL   FEBS Lett 327 (3), 294-296 (1993)
   PUBMED   8348957
REFERENCE   9  (residues 1 to 773)
  AUTHORS   Esser,V., Britton,C.H., Weis,B.C., Foster,D.W. and McGarry,J.D.
  TITLE     Cloning, sequencing, and expression of a cDNA encoding rat liver
            carnitine palmitoyltransferase I. Direct evidence that a single
            polypeptide is involved in inhibitor interaction and catalytic
            function
  JOURNAL   J Biol Chem 268 (8), 5817-5822 (1993)
   PUBMED   8449948
REFERENCE   10 (residues 1 to 773)
  AUTHORS   Esser,V., Kuwajima,M., Britton,C.H., Krishnan,K., Foster,D.W. and
            McGarry,J.D.
  TITLE     Inhibitors of mitochondrial carnitine palmitoyltransferase I limit
            the action of proteases on the enzyme. Isolation and partial amino
            acid analysis of a truncated form of the rat liver isozyme
  JOURNAL   J Biol Chem 268 (8), 5810-5816 (1993)
   PUBMED   8449947
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072522.1 and AA875270.1.
            
            On Dec 11, 2007 this sequence version replaced NP_113747.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072522.1, L07736.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..773
                     /product="carnitine O-palmitoyltransferase 1, liver
                     isoform"
                     /EC_number="2.3.1.21"
                     /note="CPT I; CPT1-L; CPTI-L; carnitine
                     palmitoyltransferase 1, liver; carnitine
                     palmitoyltransferase 1a, liver; succinyltransferase CPT1A"
                     /calculated_mol_wt=87995
     Region          1..47
                     /region_name="CPT_N"
                     /note="Carnitine O-palmitoyltransferase N-terminus;
                     pfam16484"
                     /db_xref="CDD:465132"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:17478130; propagated from
                     UniProtKB/Swiss-Prot (P32198.2)"
     Site            48..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32198.2)"
     Site            103..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32198.2)"
     Region          174..756
                     /region_name="Carn_acyltransf"
                     /note="Choline/Carnitine o-acyltransferase; pfam00755"
                     /db_xref="CDD:459926"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17478130; propagated from
                     UniProtKB/Swiss-Prot (P32198.2)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17478130; propagated from
                     UniProtKB/Swiss-Prot (P32198.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17478130; propagated from
                     UniProtKB/Swiss-Prot (P32198.2)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17478130; propagated from
                     UniProtKB/Swiss-Prot (P32198.2)"
     CDS             1..773
                     /gene="Cpt1a"
                     /gene_synonym="CPT-Ia"
                     /coded_by="NM_031559.2:49..2370"
                     /db_xref="GeneID:25757"
                     /db_xref="RGD:2396"
ORIGIN      
        1 maeahqavaf qftvtpdgid lrlshealkq iclsglhswk kkfirfkngi itgvfpanps
       61 swlivvvgvi ssmhakvdps lgmiakisrt ldttgrmssq tknivsgvlf gtglwvavim
      121 tmryslkvll syhgwmfaeh gkmsrstkiw mamvkvlsgr kpmlysfqts lprlpvpavk
      181 dtvsrylesv rplmkeedfq rmtalaqdfa vnlgpklqwy lklkswwatn yvsdwweeyi
      241 ylrgrgplmv nsnyyameml yitpthiqaa ragntihail lyrrtldree lkpirllgst
      301 iplcsaqwer lfntsripge etdtiqhikd srhivvyhrg ryfkvwlyhd grllrprele
      361 qqmqqilddp sepqpgeakl aaltaadrvp wakcrqtyfa rgknkqslda vekaaffvtl
      421 deseqgyree dpeasidsya ksllhgrcfd rwfdksitfv vfknskigin aehswadapv
      481 vghlweyvma tdvfqlgyse dghckgdtnp nipkptrlqw dipgecqevi daslssasll
      541 andvdlhsfp fdsfgkglik kcrtspdafi qlalqlahyk dmgkfcltye asmtrlfreg
      601 rtetvrsctm escnfvqamm dpkstaeqrl klfkiacekh qhlyrlamtg agidrhlfcl
      661 yvvskylavd spflkevlse pwrlstsqtp qqqvelfdfe knpdyvscgg gfgpvaddgy
      721 gvsyiivgen fihfhisskf sspetdshrf gkhlrqammd iitlfgltin skk
//
LOCUS       NP_077331                838 aa            linear   ROD 27-APR-2025
DEFINITION  axin-2 [Rattus norvegicus].
ACCESSION   NP_077331 XP_001081593
VERSION     NP_077331.1
DBSOURCE    REFSEQ: accession NM_024355.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Qiu,Z., Chen,W., Liu,Y., Jiang,B., Yin,L. and Chen,X.
  TITLE     LncRNA AC061961.2 overexpression inhibited endoplasmic reticulum
            stress induced apoptosis in dilated cardiomyopathy rats and
            cardiomyocytes via activating wnt/beta-catenin pathway
  JOURNAL   J Recept Signal Transduct Res 41 (5), 494-503 (2021)
   PUBMED   33092439
REFERENCE   2  (residues 1 to 838)
  AUTHORS   An,Y.Z., Cho,E., Ling,J. and Zhang,X.
  TITLE     The Axin2-snail axis promotes bone invasion by activating
            cancer-associated fibroblasts in oral squamous cell carcinoma
  JOURNAL   BMC Cancer 20 (1), 987 (2020)
   PUBMED   33046030
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Wu,Z., Liang,Y. and Yu,S.
  TITLE     Downregulation of microRNA-103a reduces microvascular endothelial
            cell injury in a rat model of cerebral ischemia by targeting AXIN2
  JOURNAL   J Cell Physiol 235 (5), 4720-4733 (2020)
   PUBMED   31650542
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Otero,L., Lacunza,E., Vasquez,V., Arbelaez,V., Cardier,F. and
            Gonzalez,F.
  TITLE     Variations in AXIN2 predict risk and prognosis of colorectal cancer
  JOURNAL   BDJ Open 5, 13 (2019)
   PUBMED   31632692
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Mishra,A., Singh,S., Tiwari,V., Chaturvedi,S., Wahajuddin,M. and
            Shukla,S.
  TITLE     Dopamine receptor activation mitigates mitochondrial dysfunction
            and oxidative stress to enhance dopaminergic neurogenesis in 6-OHDA
            lesioned rats: A role of Wnt signalling
  JOURNAL   Neurochem Int 129, 104463 (2019)
   PUBMED   31078578
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Leung,J.Y., Kolligs,F.T., Wu,R., Zhai,Y., Kuick,R., Hanash,S.,
            Cho,K.R. and Fearon,E.R.
  TITLE     Activation of AXIN2 expression by beta-catenin-T cell factor. A
            feedback repressor pathway regulating Wnt signaling
  JOURNAL   J Biol Chem 277 (24), 21657-21665 (2002)
   PUBMED   11940574
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Lustig,B., Jerchow,B., Sachs,M., Weiler,S., Pietsch,T., Karsten,U.,
            van de Wetering,M., Clevers,H., Schlag,P.M., Birchmeier,W. and
            Behrens,J.
  TITLE     Negative feedback loop of Wnt signaling through upregulation of
            conductin/axin2 in colorectal and liver tumors
  JOURNAL   Mol Cell Biol 22 (4), 1184-1193 (2002)
   PUBMED   11809809
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Liu,W., Dong,X., Mai,M., Seelan,R.S., Taniguchi,K.,
            Krishnadath,K.K., Halling,K.C., Cunningham,J.M., Boardman,L.A.,
            Qian,C., Christensen,E., Schmidt,S.S., Roche,P.C., Smith,D.I. and
            Thibodeau,S.N.
  TITLE     Mutations in AXIN2 cause colorectal cancer with defective mismatch
            repair by activating beta-catenin/TCF signalling
  JOURNAL   Nat Genet 26 (2), 146-147 (2000)
   PUBMED   11017067
  REMARK    Erratum:[Nat Genet 2000 Dec;26(4):501]
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Yamamoto,H., Kishida,S., Uochi,T., Ikeda,S., Koyama,S., Asashima,M.
            and Kikuchi,A.
  TITLE     Axil, a member of the Axin family, interacts with both glycogen
            synthase kinase 3beta and beta-catenin and inhibits axis formation
            of Xenopus embryos
  JOURNAL   Mol Cell Biol 18 (5), 2867-2875 (1998)
   PUBMED   9566905
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Behrens,J., Jerchow,B.A., Wurtele,M., Grimm,J., Asbrand,C.,
            Wirtz,R., Kuhl,M., Wedlich,D. and Birchmeier,W.
  TITLE     Functional interaction of an axin homolog, conductin, with
            beta-catenin, APC, and GSK3beta
  JOURNAL   Science 280 (5363), 596-599 (1998)
   PUBMED   9554852
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF017757.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001081593.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF017757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..838
                     /product="axin-2"
                     /note="conductin; axin-like protein; axis inhibition
                     protein 2"
                     /calculated_mol_wt=92817
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          10..75
                     /region_name="AXIN1_TNKS_BD"
                     /note="Axin-1 tankyrase binding domain; pfam16646"
                     /db_xref="CDD:465215"
     Region          21..30
                     /region_name="Tankyrase-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          82..198
                     /region_name="RGS_Axin"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the Axin protein; cd08707"
                     /db_xref="CDD:188662"
     Site            order(86..89,92,109,112..113,116..117,119,129..130,
                     132..134,136..137)
                     /site_type="other"
                     /note="APC binding site [polypeptide binding]"
                     /db_xref="CDD:188662"
     Region          300..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          327..413
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          398..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          413..476
                     /region_name="Interaction with beta-catenin.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          433..468
                     /region_name="Axin_b-cat_bind"
                     /note="Axin beta-catenin binding motif; pfam08833"
                     /db_xref="CDD:462616"
     Region          450..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          568..682
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          712..744
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70240.1)"
     Region          756..838
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     CDS             1..838
                     /gene="Axin2"
                     /gene_synonym="axil; axin-2"
                     /coded_by="NM_024355.1:85..2601"
                     /db_xref="GeneID:29134"
                     /db_xref="RGD:69259"
ORIGIN      
        1 mssavlvtll pdpsssfred aprppvpgee getppcqpsv gkvqstkpmp vssnarrned
       61 glgepegras pdspltrwtk slhsllgdqd gaylfrtfle rekcvdtldf wfacngfrqm
      121 nlkdtktlrv akaiykryie nnsvvskqlk patktyirdg ikkqqigsvm fdqaqteiqa
      181 vmeenayqvf ltsdiyleyv rsggentaym sngglgslkv lcgylptlne eeewtcadlk
      241 cklsptvvgl ssktlratas vrstetaeng frsfkrsepv npyhvgsgyv fapatsands
      301 elssdaltdd smsmtdssvd gippyrmgsk kqlqremhrs vkangqvslp hfprthrlpk
      361 emtpvepaaf aaelisrlek lklelesrhs leerlqqire deekegseqa lssrdgapvq
      421 hplallpsgs yeedpqtild dhlsrvlktp gcqspgvgry sprsrspdhh hhhhqqchal
      481 lptggklppe aacpllggks fltkqttkhv hhhyihhhav pktkeeieae atqrvrclcp
      541 ggtdyycysk ckshskppep lpgeqfcgsr ggtlpkrntk gtepglalpa reggmssaag
      601 apqlpgeegd rsqdvwqwml eserqskskp hstqsirksy plesarappg ervsrhhllg
      661 asghprsaar ahpftqdpam ppltppntla qleeacrrla evskpqkqrc cvasqqrdrn
      721 hpatgqagpt sfsnpslase dhkepkrlas vhalqaseli vtyffcgeei pyrrmlkaqs
      781 ltlghfkeql skkgnyryyf kkasdefacg avfeeiwdde tvlpmyegri lgkverid
//
LOCUS       NP_001006978             619 aa            linear   ROD 27-APR-2025
DEFINITION  adenosine deaminase domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001006978 XP_227046
VERSION     NP_001006978.2
DBSOURCE    REFSEQ: accession NM_001006977.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Connolly,C.M., Dearth,A.T. and Braun,R.E.
  TITLE     Disruption of murine Tenr results in teratospermia and male
            infertility
  JOURNAL   Dev Biol 278 (1), 13-21 (2005)
   PUBMED   15649457
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Schumacher,J.M., Lee,K., Edelhoff,S. and Braun,R.E.
  TITLE     Distribution of Tenr, an RNA-binding protein, in a lattice-like
            network within the spermatid nucleus in the mouse
  JOURNAL   Biol Reprod 52 (6), 1274-1283 (1995)
   PUBMED   7543294
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083595.1 and CV126304.1.
            
            On Apr 6, 2005 this sequence version replaced NP_001006978.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083595.1, BC105906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q25"
     Protein         1..619
                     /product="adenosine deaminase domain-containing protein 1"
                     /note="testis nuclear RNA-binding protein; adenosine
                     deaminase domain containing 1 (testis specific)"
                     /calculated_mol_wt=67685
     Region          28..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR54.1)"
     Region          137..205
                     /region_name="DSRM_ADAD1"
                     /note="double-stranded RNA binding motif of adenosine
                     deaminase domain-containing protein 1 (ADAD1) and similar
                     proteins; cd19905"
                     /db_xref="CDD:380734"
     Site            order(137,139..140,143..144,147..148,153..154,164..168,
                     170,187..190,193..194)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380734"
     Region          246..618
                     /region_name="ADEAMc"
                     /note="tRNA-specific and double-stranded RNA adenosine
                     deaminase (RNA-specific editase); smart00552"
                     /db_xref="CDD:214718"
     CDS             1..619
                     /gene="Adad1"
                     /gene_synonym="Tenr"
                     /coded_by="NM_001006977.2:13..1872"
                     /db_xref="GeneID:294979"
                     /db_xref="RGD:1359309"
ORIGIN      
        1 mataggsrra pvpgprlglp laahlpaslg gegakdslgg ektsgnndwf qssrvpsfaq
       61 mlkknlpvqs saqtvtlptg yssescslsn maskvtqvtg nfpepllskg lssisnpvlp
      121 pkkipkefim kyrrgeinpv salhqfaqmq rvqldlketv ttgnvmgpyf afcavvdgiq
      181 yktglgqnkk esrsnaakla ldellqldep epralepagp ppipaepivt peaayiskvq
      241 yegrqvqyak isqlvketfs qlisshsqyl kcssslaafi iergghhevv aigtgeynys
      301 qcikpngrvl hdthavvtar rsllryfyrq lllfysknpa mmeksifcte pasnlltlkq
      361 ninlylymnq lpkgsaqiks qlrlnphsis afeaneelsl hvavegkiyl tvycsadgvn
      421 rvnsmsssdk ltrwevlgvq gallshfiqp vyissilvgd gncndtrgle iainqrvdda
      481 ltsklpmfyl vnrphislvp tayplqinld hkslslnwaq gdnsleivdg lsgkitessp
      541 fksglsmasr lckaamlsrf nllakeaktd dlleartyha akclsgpyqe akallkaylq
      601 qhgygswivk spcieqfsm
//
LOCUS       NP_001019537             395 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 13A [Rattus norvegicus].
ACCESSION   NP_001019537 XP_577016
VERSION     NP_001019537.1
DBSOURCE    REFSEQ: accession NM_001024366.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079325.1.
            
            On May 27, 2005 this sequence version replaced XP_577016.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079325.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..395
                     /product="ADP-ribosylation factor-like protein 13A"
                     /note="ADP-ribosylation factor-like 13A; ADP ribosylation
                     factor like GTPase 13A"
                     /calculated_mol_wt=45336
     Region          23..189
                     /region_name="Arl2l1_Arl13_like"
                     /note="Arl2-like protein 1 (Arl2l1) and Arl13; cd04161"
                     /db_xref="CDD:133361"
     Site            28..35
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133361"
     Site            order(30..36,51..52,74,130..131,133,166..168)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133361"
     Site            order(30..31,35,39,51..58,80,85)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133361"
     Site            order(40..43,45..55)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133361"
     Site            order(52..56,61,71,75,81,83..85)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133361"
     Site            52
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133361"
     Site            order(53..60,70,81,84..85)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133361"
     Site            order(56..62,65..70)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:133361"
     Site            71..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133361"
     Site            71..74
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133361"
     Site            130..133
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133361"
     Site            166..168
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133361"
     CDS             1..395
                     /gene="Arl13a"
                     /coded_by="NM_001024366.1:155..1342"
                     /db_xref="GeneID:501617"
                     /db_xref="RGD:1562947"
ORIGIN      
        1 mfrlltacws rqkategkqr nvtiivigld nsgkshlvaa fqrlipskmh semrptqttl
       61 llddyqvsvy dltgdlkgre kwpnyyaeah glvfvvdssd iariqevkii ltrlmfdkrv
      121 sgkpililan kqdkkdallp cdiieyllle rlvnetksmc rvepcstirn lpkrhqqpiv
      181 iglrwllaai gdrydelctr hqtpsmsnis ssknirgcge rcssdslstr gvgvvrnnhr
      241 qhfekrqhle hrqhveqrhf ekrqhfesrq hliqrsldar plkpilqkdg frirpkknms
      301 vtfaldvime egecsrkiga pniskpcnsq cydtktpaps adanlfkarr pkkrietwdt
      361 eemfledprg eafrscvtgh ssrssrntqs lyftg
//
LOCUS       NP_037321                355 aa            linear   ROD 27-APR-2025
DEFINITION  guanine nucleotide-binding protein G(z) subunit alpha [Rattus
            norvegicus].
ACCESSION   NP_037321
VERSION     NP_037321.1
DBSOURCE    REFSEQ: accession NM_013189.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wainford,R.D., Kurtz,K. and Kapusta,D.R.
  TITLE     Central G-alpha subunit protein-mediated control of cardiovascular
            function, urine output, and vasopressin secretion in conscious
            Sprague-Dawley rats
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 295 (2), R535-R542 (2008)
   PUBMED   18525017
  REMARK    GeneRIF: Central Galphaz (inhibitory) and Galphaq (stimulatory)
            activity differentially modulates AVP release to control the
            pattern of diuresis to intracerebroventricular nociceptin.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Mannoury la Cour,C., El Mestikawy,S., Hanoun,N., Hamon,M. and
            Lanfumey,L.
  TITLE     Regional differences in the coupling of 5-hydroxytryptamine-1A
            receptors to G proteins in the rat brain
  JOURNAL   Mol Pharmacol 70 (3), 1013-1021 (2006)
   PUBMED   16772521
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Kimple,M.E., Nixon,A.B., Kelly,P., Bailey,C.L., Young,K.H.,
            Fields,T.A. and Casey,P.J.
  TITLE     A role for G(z) in pancreatic islet beta-cell biology
  JOURNAL   J Biol Chem 280 (36), 31708-31713 (2005)
   PUBMED   16157560
  REMARK    GeneRIF: An endogenous receptor-mediated signaling process in
            pancreatic beta-cells is dependent on G alpha(z) function.
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Andric,S.A., Zivadinovic,D., Gonzalez-Iglesias,A.E., Lachowicz,A.,
            Tomic,M. and Stojilkovic,S.S.
  TITLE     Endothelin-induced, long lasting, and Ca2+ influx-independent
            blockade of intrinsic secretion in pituitary cells by Gz subunits
  JOURNAL   J Biol Chem 280 (29), 26896-26903 (2005)
   PUBMED   15919662
  REMARK    GeneRIF: endothelin-1 in picomolar concentrations can interrupt
            prolactin release for several hours downstream of spontaneous and
            high K+-stimulated voltage-gated Ca2+ influx. This action occurred
            through the Gz signaling pathway.
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Carrasco,G.A., Damjanoska,K.J., D'Souza,D.N., Zhang,Y., Garcia,F.,
            Battaglia,G., Muma,N.A. and Van de Kar,L.D.
  TITLE     Short-term cocaine treatment causes neuroadaptive changes in
            Galphaq and Galpha11 proteins in rats undergoing withdrawal
  JOURNAL   J Pharmacol Exp Ther 311 (1), 349-355 (2004)
   PUBMED   15175423
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Carrasco,G.A., Zhang,Y., Damjanoska,K.J., D'Souza,D.N., Garcia,F.,
            Battaglia,G., Muma,N.A. and Van de Kar,L.D.
  TITLE     A region-specific increase in Galphaq and Galpha11 proteins in
            brains of rats during cocaine withdrawal
  JOURNAL   J Pharmacol Exp Ther 307 (3), 1012-1019 (2003)
   PUBMED   14534355
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Schuller,U., Lamp,E.C. and Schilling,K.
  TITLE     Developmental expression of heterotrimeric G-proteins in the murine
            cerebellar cortex
  JOURNAL   Histochem Cell Biol 116 (2), 149-159 (2001)
   PUBMED   11685543
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Yang,J., Wu,J., Kowalska,M.A., Dalvi,A., Prevost,N., O'Brien,P.J.,
            Manning,D., Poncz,M., Lucki,I., Blendy,J.A. and Brass,L.F.
  TITLE     Loss of signaling through the G protein, Gz, results in abnormal
            platelet activation and altered responses to psychoactive drugs
  JOURNAL   Proc Natl Acad Sci U S A 97 (18), 9984-9989 (2000)
   PUBMED   10954748
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Lounsbury,K.M., Casey,P.J., Brass,L.F. and Manning,D.R.
  TITLE     Phosphorylation of Gz in human platelets. Selectivity and site of
            modification
  JOURNAL   J Biol Chem 266 (32), 22051-22056 (1991)
   PUBMED   1939224
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Matsuoka,M., Itoh,H., Kozasa,T. and Kaziro,Y.
  TITLE     Sequence analysis of cDNA and genomic DNA for a putative pertussis
            toxin-insensitive guanine nucleotide-binding regulatory protein
            alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 85 (15), 5384-5388 (1988)
   PUBMED   2456569
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J03773.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J03773.1, BP486875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..355
                     /product="guanine nucleotide-binding protein G(z) subunit
                     alpha"
                     /note="gz-alpha; g(x) alpha chain; guanine nucleotide
                     binding protein (G protein), alpha z polypeptide; Guanine
                     nucleotide binding protein alpha; guanine nucleotide
                     binding protein, alpha z polypeptide; guanine nucleotide
                     binding protein, alpha z subunit; heterotrimeric guanine
                     nucleotide-binding protein 1h"
                     /calculated_mol_wt=40749
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Region          34..349
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          35..48
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Site            order(40,45..47,182,201,204,270..271,273,326..327)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            40..47
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(41..43,71,75,79,82,85..86,104,107,150,179,204,212,
                     216)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          174..182
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Site            177..185
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            182
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(183,185,187,198,200,204..206,208,211..212,214..217)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(185,210,213..214,217)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          197..206
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Site            201..204
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            202..218
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          266..273
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Site            270..273
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(318..329,331..334)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          325..330
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P19627.3)"
     Site            326..328
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..355
                     /gene="Gnaz"
                     /gene_synonym="GXA; Hg1h"
                     /coded_by="NM_013189.2:15..1082"
                     /db_xref="GeneID:25740"
                     /db_xref="RGD:2717"
ORIGIN      
        1 mgcrqsseek eaarrsrrid rhlrsesqrq rreikllllg tsnsgkstiv kqmkiihsgg
       61 fnleackeyk pliiynaids ltriiralaa lkidfhnpdr aydavqlfal tgpaeskgei
      121 tpellgvmrr lwadpgaqac fgrsseyhle dnaayylndl eriaapdyip tvedilrsrd
      181 mttgivenkf tfkeltfkmv dvggqrserk kwihcfegvt aiifcvelsg ydlklyednq
      241 tsrmaeslrl fdsicnnnwf intslilfln kkdllsekir riplsvcfpe ykgqntyeea
      301 avyiqrqfed lnrnketkei yshftcatdt sniqfvfdav tdviiqnnlk yiglc
//
LOCUS       NP_077359                166 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor HES-5 [Rattus norvegicus].
ACCESSION   NP_077359
VERSION     NP_077359.1
DBSOURCE    REFSEQ: accession NM_024383.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Chen,X., Zhou,W., Hu,Q. and Huang,L.
  TITLE     Exploration of the Notch3-HES5 signal pathway in
            monocrotaline-induced pulmonary hypertension using rat model
  JOURNAL   Congenit Heart Dis 14 (3), 396-402 (2019)
   PUBMED   30811836
  REMARK    GeneRIF: Monocrotaline-induced pulmonary hypertension rats had high
            expressions of the Notch3-HES5 signal pathway in the pulmonary
            arterioles.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Zheng,X., Narayanan,S., Sunkari,V.G., Eliasson,S., Botusan,I.R.,
            Grunler,J., Catrina,A.I., Radtke,F., Xu,C., Zhao,A., Ekberg,N.R.,
            Lendahl,U. and Catrina,S.B.
  TITLE     Triggering of a Dll4-Notch1 loop impairs wound healing in diabetes
  JOURNAL   Proc Natl Acad Sci U S A 116 (14), 6985-6994 (2019)
   PUBMED   30886104
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Li,W., Wu,J., Yang,J., Sun,S., Chai,R., Chen,Z.Y. and Li,H.
  TITLE     Notch inhibition induces mitotically generated hair cells in
            mammalian cochleae via activating the Wnt pathway
  JOURNAL   Proc Natl Acad Sci U S A 112 (1), 166-171 (2015)
   PUBMED   25535395
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Zhang,X., Huang,G., Liu,H., Chang,H. and Wilson,J.X.
  TITLE     Folic acid enhances Notch signaling, hippocampal neurogenesis, and
            cognitive function in a rat model of cerebral ischemia
  JOURNAL   Nutr Neurosci 15 (2), 55-61 (2012)
   PUBMED   22334042
  REMARK    GeneRIF: Folic acid stimulated the expression of Notch1, Hes1, and
            Hes5 proteins, and this effect increased with folic acid dose in
            the rat middle cerebral artery occlusion model of stroke.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Tateya,T., Imayoshi,I., Tateya,I., Ito,J. and Kageyama,R.
  TITLE     Cooperative functions of Hes/Hey genes in auditory hair cell and
            supporting cell development
  JOURNAL   Dev Biol 352 (2), 329-340 (2011)
   PUBMED   21300049
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Ohtsuka,T., Sakamoto,M., Guillemot,F. and Kageyama,R.
  TITLE     Roles of the basic helix-loop-helix genes Hes1 and Hes5 in
            expansion of neural stem cells of the developing brain
  JOURNAL   J Biol Chem 276 (32), 30467-30474 (2001)
   PUBMED   11399758
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Hojo,M., Ohtsuka,T., Hashimoto,N., Gradwohl,G., Guillemot,F. and
            Kageyama,R.
  TITLE     Glial cell fate specification modulated by the bHLH gene Hes5 in
            mouse retina
  JOURNAL   Development 127 (12), 2515-2522 (2000)
   PUBMED   10821751
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Cau,E., Gradwohl,G., Casarosa,S., Kageyama,R. and Guillemot,F.
  TITLE     Hes genes regulate sequential stages of neurogenesis in the
            olfactory epithelium
  JOURNAL   Development 127 (11), 2323-2332 (2000)
   PUBMED   10804175
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Ohtsuka,T., Ishibashi,M., Gradwohl,G., Nakanishi,S., Guillemot,F.
            and Kageyama,R.
  TITLE     Hes1 and Hes5 as notch effectors in mammalian neuronal
            differentiation
  JOURNAL   EMBO J 18 (8), 2196-2207 (1999)
   PUBMED   10205173
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Akazawa,C., Sasai,Y., Nakanishi,S. and Kageyama,R.
  TITLE     Molecular characterization of a rat negative regulator with a basic
            helix-loop-helix structure predominantly expressed in the
            developing nervous system
  JOURNAL   J Biol Chem 267 (30), 21879-21885 (1992)
   PUBMED   1400497
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D12516.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D12516.1, AI548772.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132276, SAMD00132289
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..166
                     /product="transcription factor HES-5"
                     /note="hairy and enhancer of split 5"
                     /calculated_mol_wt=18321
     Region          18..76
                     /region_name="bHLH-O_HES5"
                     /note="basic helix-loop-helix-orange (bHLH-O) domain found
                     in transcription factor HES-5 and similar proteins;
                     cd11461"
                     /db_xref="CDD:381467"
     Site            order(21,28..29,31..33,35..36,38..39,42..43,46,55,57..59,
                     62..63,65..66,68..70,72..73,76)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381467"
     Site            order(21..23,26,28..29,33,57..58)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381467"
     Region          86..128
                     /region_name="ORANGE"
                     /note="Orange domain; smart00511"
                     /db_xref="CDD:128787"
     Region          125..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03062.1)"
     Region          163..166
                     /region_name="WRPW motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03062.1)"
     CDS             1..166
                     /gene="Hes5"
                     /coded_by="NM_024383.1:53..553"
                     /db_xref="GeneID:79225"
                     /db_xref="RGD:621340"
ORIGIN      
        1 mapstvavem lspkeknrlr kpvvekmrrd rinssieqlk llleqefarh qpnsklekad
       61 ilemavsylk hskafaaaag pkslhqdyse gyswclqeav qfltlhaasd tqmkllyhfq
      121 rppapaapvk etptpgaapq parsstkaaa svstsrqsac glwrpw
//
LOCUS       NP_001004199             813 aa            linear   ROD 27-APR-2025
DEFINITION  tax1-binding protein 1 homolog [Rattus norvegicus].
ACCESSION   NP_001004199 XP_342688
VERSION     NP_001004199.1
DBSOURCE    REFSEQ: accession NM_001004199.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Sarraf,S.A., Shah,H.V., Kanfer,G., Pickrell,A.M., Holtzclaw,L.A.,
            Ward,M.E. and Youle,R.J.
  TITLE     Loss of TAX1BP1-Directed Autophagy Results in Protein Aggregate
            Accumulation in the Brain
  JOURNAL   Mol Cell 80 (5), 779-795 (2020)
   PUBMED   33207181
  REMARK    GeneRIF: Loss of TAX1BP1-Directed Autophagy Results in Protein
            Aggregate Accumulation in the Brain.
            Erratum:[Mol Cell. 2022 Apr 7;82(7):1383-1385. doi:
            10.1016/j.molcel.2022.03.020. PMID: 35395199]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Chen,J. and Chen,Z.J.
  TITLE     Regulation of NF-kappaB by ubiquitination
  JOURNAL   Curr Opin Immunol 25 (1), 4-12 (2013)
   PUBMED   23312890
  REMARK    Review article
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Mesentier-Louro,L.A., Coronel,J., Zaverucha-do-Valle,C.,
            Mencalha,A., Paredes,B.D., Abdelhay,E., Mendez-Otero,R. and
            Santiago,M.F.
  TITLE     Cell therapy modulates expression of Tax1-binding protein 1 and
            synaptotagmin IV in a model of optic nerve lesion
  JOURNAL   Invest Ophthalmol Vis Sci 53 (8), 4720-4729 (2012)
   PUBMED   22695963
  REMARK    GeneRIF: The increased expression of Tax1BP1 in optic nerve crush
            eyes displays the possible neuroprotective effect of bone marrow
            mononuclear cell treatment
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Harhaj,E.W. and Dixit,V.M.
  TITLE     Deubiquitinases in the regulation of NF-kappaB signaling
  JOURNAL   Cell Res 21 (1), 22-39 (2011)
   PUBMED   21119682
  REMARK    Review article
REFERENCE   5  (residues 1 to 813)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   6  (residues 1 to 813)
  AUTHORS   Shembade,N., Harhaj,N.S., Parvatiyar,K., Copeland,N.G.,
            Jenkins,N.A., Matesic,L.E. and Harhaj,E.W.
  TITLE     The E3 ligase Itch negatively regulates inflammatory signaling
            pathways by controlling the function of the ubiquitin-editing
            enzyme A20
  JOURNAL   Nat Immunol 9 (3), 254-262 (2008)
   PUBMED   18246070
REFERENCE   7  (residues 1 to 813)
  AUTHORS   Iha,H., Peloponese,J.M., Verstrepen,L., Zapart,G., Ikeda,F.,
            Smith,C.D., Starost,M.F., Yedavalli,V., Heyninck,K., Dikic,I.,
            Beyaert,R. and Jeang,K.T.
  TITLE     Inflammatory cardiac valvulitis in TAX1BP1-deficient mice through
            selective NF-kappaB activation
  JOURNAL   EMBO J 27 (4), 629-641 (2008)
   PUBMED   18239685
REFERENCE   8  (residues 1 to 813)
  AUTHORS   Ulrich,M., Seeber,S., Becker,C.M. and Enz,R.
  TITLE     Tax1-binding protein 1 is expressed in the retina and interacts
            with the GABA(C) receptor rho1 subunit
  JOURNAL   Biochem J 401 (2), 429-436 (2007)
   PUBMED   16999686
  REMARK    GeneRIF: C-terminal region of Tax1BP1 bound to an intracellular
            domain of the rho1 subunit, but not to other subunits of GABA(C),
            GABA(A) or glycine receptors. Tax1BP1 & GABA(C) receptors were
            co-expressed in both synaptic layers of the retina.
REFERENCE   9  (residues 1 to 813)
  AUTHORS   De Valck,D., Jin,D.Y., Heyninck,K., Van de Craen,M., Contreras,R.,
            Fiers,W., Jeang,K.T. and Beyaert,R.
  TITLE     The zinc finger protein A20 interacts with a novel anti-apoptotic
            protein which is cleaved by specific caspases
  JOURNAL   Oncogene 18 (29), 4182-4190 (1999)
   PUBMED   10435631
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081949.1.
            
            On Sep 10, 2004 this sequence version replaced XP_342688.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081949.1, SRR8487231.170348.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..813
                     /product="tax1-binding protein 1 homolog"
                     /note="TRAF6-binding protein homolog; liver
                     regeneration-related protein 2; Tax1 (human T-cell
                     leukemia virus type I) binding protein 1; liver
                     regeneration-related protein LRRG004"
                     /calculated_mol_wt=93066
     Region          17..120
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UKC1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Region          125..>460
                     /region_name="CALCOCO1"
                     /note="Calcium binding and coiled-coil domain (CALCOCO1)
                     like; pfam07888"
                     /db_xref="CDD:462303"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86VP1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86VP1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Region          320..420
                     /region_name="Oligomerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HA4.1)"
     Region          332..>630
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000250|UniProtKB:Q86VP1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UKC1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Region          667..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HA4.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000250|UniProtKB:Q86VP1; propagated from
                     UniProtKB/Swiss-Prot (Q66HA4.1)"
     Region          752..778
                     /region_name="Zn-C2H2_12"
                     /note="Autophagy receptor zinc finger-C2H2 domain;
                     pfam18112"
                     /db_xref="CDD:407946"
     Region          779..805
                     /region_name="Zn-C2H2_TAX1BP1_rpt2"
                     /note="second C2H2-type zinc binding domain found in
                     tax1-binding protein 1 (TAX1BP1) and similar proteins;
                     cd21970"
                     /db_xref="CDD:412016"
     CDS             1..813
                     /gene="Tax1bp1"
                     /gene_synonym="Aa1076"
                     /coded_by="NM_001004199.1:85..2526"
                     /db_xref="GeneID:246244"
                     /db_xref="RGD:708579"
ORIGIN      
        1 mtsfqevplq tsnfahvifq nvaksylpna hlechytltp yihphskdwv gifkvgwsta
       61 rdyytflwsp mpeqyvegst vncvlafqgy ylpnddgefy qfcyvthkge irgastpfqf
      121 raaspveell tmedegnsdm lvvttkagll elkiektlke keellklvsv leketaqlre
      181 qvgrmerels heksrceqlq aeqkgllevs qslrveneef mkrysdatsk ahqleedivs
      241 vthkaveket eldslkdklr kaqqekeqle cqlktekdek elykvhlknt eientklvse
      301 iqtlknvdgn kesmithfke eigklqscla dkenlhrall lttsnkedtl llkeqlrkae
      361 eqvqatrqel iflakelsda vnvrdktmad lhtarlener vkkqladtla elqlhavktd
      421 qektdtlehe lrrevedlkl rlqmaadhyk ekfkecqrlq kqinklsdqs assngvftkr
      481 mgsqqkvnda sintdpaasa savdvkpaas caaetdfdms akdhvcevtk emaekvekyn
      541 kckqllqdek akcnkyadel aqmelkwkeq vriaenvkle laeledsysl qlaekdkein
      601 clasflenls rekeltksle dqkgrkmegq spqqvsrcln tcseqsgllp tlpaaqpvlq
      661 ygnpytahet rdgadgafyp deiqrppvrg pswednvvcs qparnlsrpd gledpedsre
      721 denvpippdp anqhlrghga gfcfdssfdv hkkcplcelm fppnydqikf eehveshwkv
      781 cpmcseqfpp dydqqgferh vqthfdqnvl nfd
//
LOCUS       NP_001014098             688 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar protein 10 [Rattus norvegicus].
ACCESSION   NP_001014098 XP_233988
VERSION     NP_001014098.1
DBSOURCE    REFSEQ: accession NM_001014076.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Staub,E., Fiziev,P., Rosenthal,A. and Hinzmann,B.
  TITLE     Insights into the evolution of the nucleolus by an analysis of its
            protein domain repertoire
  JOURNAL   Bioessays 26 (5), 567-581 (2004)
   PUBMED   15112237
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081954.1.
            
            On Apr 20, 2005 this sequence version replaced XP_233988.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081954.1, SRR8487227.281906.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..688
                     /product="nucleolar protein 10"
                     /calculated_mol_wt=80108
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSC4; propagated from
                     UniProtKB/Swiss-Prot (Q66H99.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSC4; propagated from
                     UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          50..90
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          55..95
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..219
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          174..213
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          <182..339
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          228..268
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          228..266
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          270..308
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          275..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          310..349
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSC4; propagated from
                     UniProtKB/Swiss-Prot (Q66H99.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSC4; propagated from
                     UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          482..508
                     /region_name="NUC153"
                     /note="NUC153 domain; pfam08159"
                     /db_xref="CDD:462385"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSC4; propagated from
                     UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          528..561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          <555..>670
                     /region_name="CCDC34"
                     /note="Coiled-coil domain-containing protein 3; pfam13904"
                     /db_xref="CDD:464032"
     Region          570..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     Region          644..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H99.1)"
     CDS             1..688
                     /gene="Nol10"
                     /coded_by="NM_001014076.1:74..2140"
                     /db_xref="GeneID:313981"
                     /db_xref="RGD:1359447"
ORIGIN      
        1 mqvsslnevk iyslscgksl pewlsdrkkr alqkkdvdvr rrieliqdfe mptvcttikv
       61 skdgqyilat gtykprvrcy dtyqlslkfe rcldsevvtf eilsddyski vflhndryie
      121 fhsqsgfyyk tripkfgrdf syhypscdly fvgassevyr lnleqgryln plqtdaaenn
      181 vcdintvhgl fatgtiegrv ecwdprvrkr vgvldcalns vtadseinsl ptisalkfng
      241 alsmavgtst gqvllydlrs dkpllvkdhq yglpiksvhf qdsldlvlsa dsrivkmwnk
      301 dsgkiftsle pehdlndvcl ypssgmilta nespkmgiyy ipvlgpaprw csfldnltee
      361 leenpestvy ddykfvtkkd lenlglthli gspflraymh gffmdirlyh kvklmvnpfa
      421 yeeyrkdkir qkieetraqr vqlkklpkvn kelalkliee eeekqkstlk kkvkslpnil
      481 tddrfkvmfe npdfqvdeds eefrllnplv srisekrkkq lrlleqqeql kneeeeepeg
      541 kpsdaesses sddekdwvee vrkqrrllqq eervkrqeql kedqqtvlkp qfyeikagee
      601 frsfkesatk qklmnktled rlkleakhgt lsvsdttvgs kqltftlkrs eqqkkqqeae
      661 klhrqerkkl rrsashlrsr prrgrpfh
//
LOCUS       NP_001007707             290 aa            linear   ROD 27-APR-2025
DEFINITION  tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A
            [Rattus norvegicus].
ACCESSION   NP_001007707 XP_234552
VERSION     NP_001007707.1
DBSOURCE    REFSEQ: accession NM_001007706.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Li,X., Xiong,X., Zhang,M., Wang,K., Chen,Y., Zhou,J., Mao,Y.,
            Lv,J., Yi,D., Chen,X.W., Wang,C., Qian,S.B. and Yi,C.
  TITLE     Base-Resolution Mapping Reveals Distinct m1A Methylome in Nuclear-
            and Mitochondrial-Encoded Transcripts
  JOURNAL   Mol Cell 68 (5), 993-1005 (2017)
   PUBMED   29107537
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Safra,M., Sas-Chen,A., Nir,R., Winkler,R., Nachshon,A.,
            Bar-Yaacov,D., Erlacher,M., Rossmanith,W., Stern-Ginossar,N. and
            Schwartz,S.
  TITLE     The m1A landscape on cytosolic and mitochondrial mRNA at
            single-base resolution
  JOURNAL   Nature 551 (7679), 251-255 (2017)
   PUBMED   29072297
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Ozanick,S., Krecic,A., Andersland,J. and Anderson,J.T.
  TITLE     The bipartite structure of the tRNA m1A58 methyltransferase from S.
            cerevisiae is conserved in humans
  JOURNAL   RNA 11 (8), 1281-1290 (2005)
   PUBMED   16043508
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079198.1.
            
            On Nov 29, 2004 this sequence version replaced XP_234552.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079198.1, CK596541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..290
                     /product="tRNA (adenine(58)-N(1))-methyltransferase
                     catalytic subunit TRMT61A"
                     /EC_number="2.1.1.220"
                     /note="tRNA(m1A58)-methyltransferase subunit TRM61; tRNA
                     (adenine-N(1)-)-methyltransferase catalytic subunit TRM61;
                     tRNA(m1A58)MTase subunit TRM61; tRNA
                     (adenine-N(1)-)-methyltransferase catalytic subunit
                     TRMT61A; tRNA(m1A58)MTase subunit TRMT61A;
                     tRNA(m1A58)-methyltransferase subunit TRMT61A; GCD14 and
                     PCMT domain containing protein RGD1359191; GCD14/PCMT
                     domain containing protein RGD1359191; tRNA
                     methyltransferase 61 homolog A; mRNA
                     methyladenosine-N(1)-methyltransferase catalytic subunit
                     TRMT61A"
                     /calculated_mol_wt=31488
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7; propagated from
                     UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          20..22
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          <23..58
                     /region_name="GCD14_N"
                     /note="tRNA methyltransferase complex GCD14 subunit
                     N-term; pfam14801"
                     /db_xref="CDD:434222"
     Region          35..42
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          64..287
                     /region_name="GCD14"
                     /note="tRNA methyltransferase complex GCD14 subunit;
                     pfam08704"
                     /db_xref="CDD:312288"
     Region          64..65
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          85..89
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          110..117
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          180..183
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     Region          205..212
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:Q96FX7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY46.1)"
     CDS             1..290
                     /gene="Trmt61a"
                     /gene_synonym="Gcd14; RGD1359191; Trm61"
                     /coded_by="NM_001007706.1:64..936"
                     /db_xref="GeneID:314462"
                     /db_xref="RGD:1359191"
ORIGIN      
        1 msfvayeeli kegdtailsl ghgsmvavrv qrgaqtqtrh gvlrhsvdli grpfgskvtc
       61 srggwvyvlh ptpelwtvnl phrtqilyst dialitmmle lrpgsvvces gtgsgsvsha
      121 iirsiaptgh lhtvefhqqr adkareefqq hrvsqwvtvh tqdvcrsgfg vvhvadavfl
      181 dipspweavg hawdalkveg grfcsfspci eqvqrtcqal aahgftelst levlpqvynv
      241 rtvslplpdl gaddlegnvg sdatpfrsgt pmketvghtg yltfatktpg
//
LOCUS       NP_001013161             393 aa            linear   ROD 27-APR-2025
DEFINITION  telomeric repeat-binding factor 2-interacting protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001013161 XP_226486
VERSION     NP_001013161.1
DBSOURCE    REFSEQ: accession NM_001013143.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Li,C.X., Lo,C.M., Lian,Q., Ng,K.T., Liu,X.B., Ma,Y.Y., Qi,X.,
            Yeung,O.W., Tergaonkar,V., Yang,X.X., Liu,H., Liu,J., Shao,Y. and
            Man,K.
  TITLE     Repressor and activator protein accelerates hepatic ischemia
            reperfusion injury by promoting neutrophil inflammatory response
  JOURNAL   Oncotarget 7 (19), 27711-27723 (2016)
   PUBMED   27050284
  REMARK    GeneRIF: Rap1 may induce hepatic ischemia reperfusion injury (IRI)
            through promoting neutrophils inflammatory response. Rap1 may be
            the potential therapeutic target of attenuating hepatic IRI.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Chang,C.W., Cheong,M.L., Chang,G.D., Tsai,M.S. and Chen,H.
  TITLE     Involvement of Epac1/Rap1/CaMKI/HDAC5 signaling cascade in the
            regulation of placental cell fusion
  JOURNAL   Mol Hum Reprod 19 (11), 745-755 (2013)
   PUBMED   23867755
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Doksani,Y., Wu,J.Y., de Lange,T. and Zhuang,X.
  TITLE     Super-resolution fluorescence imaging of telomeres reveals
            TRF2-dependent T-loop formation
  JOURNAL   Cell 155 (2), 345-356 (2013)
   PUBMED   24120135
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Horn,H.F., Kim,D.I., Wright,G.D., Wong,E.S., Stewart,C.L., Burke,B.
            and Roux,K.J.
  TITLE     A mammalian KASH domain protein coupling meiotic chromosomes to the
            cytoskeleton
  JOURNAL   J Cell Biol 202 (7), 1023-1039 (2013)
   PUBMED   24062341
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   6  (residues 1 to 393)
  AUTHORS   O'Connor,M.S., Safari,A., Liu,D., Qin,J. and Songyang,Z.
  TITLE     The human Rap1 protein complex and modulation of telomere length
  JOURNAL   J Biol Chem 279 (27), 28585-28591 (2004)
   PUBMED   15100233
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Liu,D., Safari,A., O'Connor,M.S., Chan,D.W., Laegeler,A., Qin,J.
            and Songyang,Z.
  TITLE     PTOP interacts with POT1 and regulates its localization to
            telomeres
  JOURNAL   Nat Cell Biol 6 (7), 673-680 (2004)
   PUBMED   15181449
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Tarsounas,M., Munoz,P., Claas,A., Smiraldo,P.G., Pittman,D.L.,
            Blasco,M.A. and West,S.C.
  TITLE     Telomere maintenance requires the RAD51D recombination/repair
            protein
  JOURNAL   Cell 117 (3), 337-347 (2004)
   PUBMED   15109494
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Li,B. and de Lange,T.
  TITLE     Rap1 affects the length and heterogeneity of human telomeres
  JOURNAL   Mol Biol Cell 14 (12), 5060-5068 (2003)
   PUBMED   14565979
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Loayza,D. and De Lange,T.
  TITLE     POT1 as a terminal transducer of TRF1 telomere length control
  JOURNAL   Nature 423 (6943), 1013-1018 (2003)
   PUBMED   12768206
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090335.1.
            
            On Apr 20, 2005 this sequence version replaced XP_226486.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090335.1, CB745139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..393
                     /product="telomeric repeat-binding factor 2-interacting
                     protein 1"
                     /note="RAP1 homolog; TRF2-interacting telomeric protein 1;
                     TERF2-interacting telomeric protein 1; repressor/activator
                     protein 1 homolog; telomeric repeat binding factor 2,
                     interacting protein"
                     /calculated_mol_wt=43287
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          17..99
                     /region_name="BRCT_2"
                     /note="BRCT domain, a BRCA1 C-terminus domain; pfam16589"
                     /db_xref="CDD:465186"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          104..132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          129..193
                     /region_name="Myb_DNA-bind_2"
                     /note="Rap1 Myb domain; pfam08914"
                     /db_xref="CDD:286058"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          194..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYB0; propagated from
                     UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          272..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EAN7.1)"
     Region          300..393
                     /region_name="rap1_RCT"
                     /note="C-terminal domain of RAP1 recruits proteins to
                     telomeres; cd11653"
                     /db_xref="CDD:212167"
     Site            order(300,305,308..309,312,323..324,327..328,330..331,
                     334..336,390)
                     /site_type="other"
                     /note="recruitment target interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212167"
     Region          377..393
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EAN7.1)"
     CDS             1..393
                     /gene="Terf2ip"
                     /coded_by="NM_001013143.1:51..1232"
                     /db_xref="GeneID:307861"
                     /db_xref="RGD:1309684"
ORIGIN      
        1 maevmdlgkd pngpthsstl fvredgsams fyvrpssakr rlstlilhgg gilcrvqkpg
       61 avllaqpgea laeasgdfis tqyildcver nekleleayr lglteqasdp kpgasaegst
      121 epepqpltgr iaytdaddva iltyvkenar spssvtgnal wkameksslt qhswqslkdr
      181 ylkhlqgqeh kyllgnapvs pssqklkrka eqdpeaadsg epqnkrtpdl peeecvkget
      241 kengeadnkl feeatpelge avvdespdfe ihitmcdgdp ptpeedsetq pdeeeeepkv
      301 stqevgtaik iirqlmekfn ldlstvtqal lknsgeleat ssflesgrrp dgfpiwcrqd
      361 dldlqkdddd trnalvkkyg aqnvarrief rkk
//
LOCUS       NP_001006987             434 aa            linear   ROD 27-APR-2025
DEFINITION  evolutionarily conserved signaling intermediate in Toll pathway,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_001006987 XP_217092
VERSION     NP_001006987.1
DBSOURCE    REFSEQ: accession NM_001006986.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kondo,T., Watanabe,M. and Hatakeyama,S.
  TITLE     TRIM59 interacts with ECSIT and negatively regulates NF-kappaB and
            IRF-3/7-mediated signal pathways
  JOURNAL   Biochem Biophys Res Commun 422 (3), 501-507 (2012)
   PUBMED   22588174
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Vogel,R.O., Janssen,R.J., van den Brand,M.A., Dieteren,C.E.,
            Verkaart,S., Koopman,W.J., Willems,P.H., Pluk,W., van den
            Heuvel,L.P., Smeitink,J.A. and Nijtmans,L.G.
  TITLE     Cytosolic signaling protein Ecsit also localizes to mitochondria
            where it interacts with chaperone NDUFAF1 and functions in complex
            I assembly
  JOURNAL   Genes Dev 21 (5), 615-624 (2007)
   PUBMED   17344420
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Xiao,C., Shim,J.H., Kluppel,M., Zhang,S.S., Dong,C., Flavell,R.A.,
            Fu,X.Y., Wrana,J.L., Hogan,B.L. and Ghosh,S.
  TITLE     Ecsit is required for Bmp signaling and mesoderm formation during
            mouse embryogenesis
  JOURNAL   Genes Dev 17 (23), 2933-2949 (2003)
   PUBMED   14633973
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Kopp,E., Medzhitov,R., Carothers,J., Xiao,C., Douglas,I.,
            Janeway,C.A. and Ghosh,S.
  TITLE     ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1
            signal transduction pathway
  JOURNAL   Genes Dev 13 (16), 2059-2071 (1999)
   PUBMED   10465784
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083762.1.
            
            On Nov 22, 2004 this sequence version replaced XP_217092.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083762.1, FQ209658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..434
                     /product="evolutionarily conserved signaling intermediate
                     in Toll pathway, mitochondrial precursor"
                     /note="evolutionarily conserved signaling intermediate in
                     Toll pathway, mitochondrial; ECSIT signalling integrator;
                     ECSIT homolog"
                     /calculated_mol_wt=44459
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5XIC2.1)"
                     /calculated_mol_wt=5179
     mat_peptide     49..434
                     /product="Evolutionarily conserved signaling intermediate
                     in Toll pathway, mitochondrial. /id=PRO_0000291988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC2.1)"
                     /calculated_mol_wt=44459
     Region          72..265
                     /region_name="ECSIT"
                     /note="Evolutionarily conserved signalling intermediate in
                     Toll pathway; pfam06239"
                     /db_xref="CDD:461857"
     Region          125..170
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          268..392
                     /region_name="ECSIT_C"
                     /note="C-terminal domain of the ECSIT protein; pfam14784"
                     /db_xref="CDD:464316"
     Region          403..434
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC2.1)"
     CDS             1..434
                     /gene="Ecsit"
                     /coded_by="NM_001006986.1:75..1379"
                     /db_xref="GeneID:300447"
                     /db_xref="RGD:1359488"
ORIGIN      
        1 mswvqvnlla rglsrgwgsi crtvlsgtpf aqpslqargl hcsavthkdd vwlvprpsep
       61 qkkpikvpam hedlfrpsgn geqdkasfln avrsfgehnv rkrghvdfiy lalrkmpefg
      121 verdlsvynl lldvfpkevf rprnaiqrif vhyprqqecg vavleqmerh gvmpntetef
      181 lliqvfghks ypmlkflrmk lwftrfknin pypvprdlpq dpldlaklgl rhmepdlsak
      241 vtvyqmslps estgiedptq phivgiqspd qqaalarhnp srpvfvegpf plwlrnkcvy
      301 yhilradlpp peeetveeip eewnlyypmq ldleysrsaw dnyefdmdev tegpvfamcm
      361 tgahdqatlv kwiqglqetn ptlaqipvvf rlarstgell attrlegqsp phsppkgpee
      421 ddeaiqaqqr qgqs
//
LOCUS       NP_001103352             388 aa            linear   ROD 27-APR-2025
DEFINITION  basigin isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001103352
VERSION     NP_001103352.1
DBSOURCE    REFSEQ: accession NM_001109882.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Zhu,X., Tang,Z., Li,W., Li,X., Iwakiri,Y. and Liu,F.
  TITLE     S-nitrosylation of EMMPRIN influences the migration of HSCs and MMP
            activity in liver fibrosis
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1640-1649 (2023)
   PUBMED   37700592
  REMARK    GeneRIF: S-nitrosylation of EMMPRIN influences the migration of
            HSCs and MMP activity in liver fibrosis.
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Chen,Y., Luan,J., Jiang,T., Cai,D., Sun,C., Wang,X., Zhao,X. and
            Gou,X.
  TITLE     Knockdown of EMMPRIN (OX47) in MRMT-1 Carcinoma Cells Inhibits
            Tumor Growth and Decreases Cancer-Induced Bone Destruction and Pain
  JOURNAL   Cancer Res Treat 53 (2), 576-583 (2021)
   PUBMED   33138345
  REMARK    GeneRIF: Knockdown of EMMPRIN (OX47) in MRMT-1 Carcinoma Cells
            Inhibits Tumor Growth and Decreases Cancer-Induced Bone Destruction
            and Pain.
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Wang,Q., Xu,B., Fan,K., Wu,J. and Wang,T.
  TITLE     Inflammation suppression by dexamethasone via inhibition of
            CD147-mediated NF-kappaB pathway in collagen-induced arthritis rats
  JOURNAL   Mol Cell Biochem 473 (1-2), 63-76 (2020)
   PUBMED   32594339
  REMARK    GeneRIF: Inflammation suppression by dexamethasone via inhibition
            of CD147-mediated NF-kappaB pathway in collagen-induced arthritis
            rats.
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Wang,Q., Xu,B., Fan,K., Wu,J. and Wang,T.
  TITLE     CypB-CD147 Signaling Is Involved in Crosstalk between Cartilage and
            FLS in Collagen-Induced Arthritis
  JOURNAL   Mediators Inflamm 2020, 6473858 (2020)
   PUBMED   32908452
  REMARK    GeneRIF: CypB-CD147 Signaling Is Involved in Crosstalk between
            Cartilage and FLS in Collagen-Induced Arthritis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Forero-Quintero,L.S., Ames,S., Schneider,H.P., Thyssen,A.,
            Boone,C.D., Andring,J.T., McKenna,R., Casey,J.R., Deitmer,J.W. and
            Becker,H.M.
  TITLE     Membrane-anchored carbonic anhydrase IV interacts with
            monocarboxylate transporters via their chaperones CD147 and GP70
  JOURNAL   J Biol Chem 294 (2), 593-607 (2019)
   PUBMED   30446621
  REMARK    GeneRIF: This study analyzed the direct interaction between CAIV
            and the two Monocarboxylate transporters (MCTs) chaperones basigin
            (CD147) and embigin (GP70). In rat CD147, binding of CAIV was
            mediated by by the positively charged Lys-73.
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Kuno,N., Kadomatsu,K., Fan,Q.W., Hagihara,M., Senda,T., Mizutani,S.
            and Muramatsu,T.
  TITLE     Female sterility in mice lacking the basigin gene, which encodes a
            transmembrane glycoprotein belonging to the immunoglobulin
            superfamily
  JOURNAL   FEBS Lett 425 (2), 191-194 (1998)
   PUBMED   9559645
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Naruhashi,K., Kadomatsu,K., Igakura,T., Fan,Q.W., Kuno,N.,
            Muramatsu,H., Miyauchi,T., Hasegawa,T., Itoh,A., Muramatsu,T. and
            Nabeshima,T.
  TITLE     Abnormalities of sensory and memory functions in mice lacking Bsg
            gene
  JOURNAL   Biochem Biophys Res Commun 236 (3), 733-737 (1997)
   PUBMED   9245724
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Polette,M., Gilles,C., Marchand,V., Lorenzato,M., Toole,B.,
            Tournier,J.M., Zucker,S. and Birembaut,P.
  TITLE     Tumor collagenase stimulatory factor (TCSF) expression and
            localization in human lung and breast cancers
  JOURNAL   J Histochem Cytochem 45 (5), 703-709 (1997)
   PUBMED   9154157
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Nehme,C.L., Cesario,M.M., Myles,D.G., Koppel,D.E. and Bartles,J.R.
  TITLE     Breaching the diffusion barrier that compartmentalizes the
            transmembrane glycoprotein CE9 to the posterior-tail plasma
            membrane domain of the rat spermatozoon
  JOURNAL   J Cell Biol 120 (3), 687-694 (1993)
   PUBMED   8425897
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Fossum,S., Mallett,S. and Barclay,A.N.
  TITLE     The MRC OX-47 antigen is a member of the immunoglobulin superfamily
            with an unusual transmembrane sequence
  JOURNAL   Eur J Immunol 21 (3), 671-679 (1991)
   PUBMED   2009910
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV119278.1, AY120888.1 and BQ199464.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY120888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676808 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..388
                     /product="basigin isoform 1 precursor"
                     /note="OX-47 antigen; glycoprotein CE9; neurothelin;
                     basigin (Ok blood group); Basigin (Ox47 antigen or CE-9)
                     (EMMPRIN in human) (neurothelin HT7 or 5A11 in avian);
                     Basignin (Ox47 antigen or CE-9) (EMMPRIN in human)
                     (neurothelin HT7 or 5A11 in avian)"
                     /calculated_mol_wt=40342
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
                     /calculated_mol_wt=2112
     mat_peptide     23..388
                     /product="Basigin. /id=PRO_0000014521"
                     /note="propagated from UniProtKB/Swiss-Prot (P26453.2)"
                     /calculated_mol_wt=40342
     Region          23..138
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          40..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..95
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          105..110
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          129..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
     Region          228..321
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
     Region          270..290
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
     Region          314..317
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26453.2)"
     Region          355..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26453.2)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P26453.2)"
     CDS             1..388
                     /gene="Bsg"
                     /gene_synonym="5A11; basignin; CE9; EMMPRIN; HT7; Ox47R"
                     /coded_by="NM_001109882.1:92..1258"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25246"
                     /db_xref="RGD:2220"
ORIGIN      
        1 maaalllala ftflsgqgac aaagflkapm sqeqwaggsv vlhceavgsp mpeiqwwfeg
       61 nepndscsql wdgarldrvh ihatyrqhaa stlsvdglaa edtgtyecra ssdpdrnhlt
      121 rpprvkwvra qasvvvlepg tivtsvqevd sktqltcfln ssgidivghr wmrggkvlqe
      181 dtlpdlqmky tvdaddrsge ysciflpepv grgninvegp prikvgkkse hasegefvkl
      241 ickseashpp vdewvwfkts dtgdqtisng teanskyvii stpelselii sdldmnvdpg
      301 tyvcnatnsq gsaretislr vrsrlaalwp flgivaevlv lvtiifiyek rrkpdqtlde
      361 ddpgaaplkg sgshlndkdk nvrqrnat
//
LOCUS       NP_001017988             607 aa            linear   ROD 27-APR-2025
DEFINITION  homologous recombination OB-fold protein [Rattus norvegicus].
ACCESSION   NP_001017988 XP_220994
VERSION     NP_001017988.1
DBSOURCE    REFSEQ: accession NM_001017988.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Hustedt,N., Saito,Y., Zimmermann,M., Alvarez-Quilon,A.,
            Setiaputra,D., Adam,S., McEwan,A., Yuan,J.Y., Olivieri,M., Zhao,Y.,
            Kanemaki,M.T., Jurisicova,A. and Durocher,D.
  TITLE     Control of homologous recombination by the HROB-MCM8-MCM9 pathway
  JOURNAL   Genes Dev 33 (19-20), 1397-1415 (2019)
   PUBMED   31467087
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Iwanaga,R., Komori,H., Ishida,S., Okamura,N., Nakayama,K.,
            Nakayama,K.I. and Ohtani,K.
  TITLE     Identification of novel E2F1 target genes regulated in cell
            cycle-dependent and independent manners
  JOURNAL   Oncogene 25 (12), 1786-1798 (2006)
   PUBMED   16288221
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY623030.1, AY623029.1 and BE114522.1.
            
            On May 13, 2005 this sequence version replaced XP_220994.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY623030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155311, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..607
                     /product="homologous recombination OB-fold protein"
                     /note="uncharacterized protein C17orf53 homolog;
                     E2F1-inducible"
                     /calculated_mol_wt=65029
     Region          25..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GX86.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3J3; propagated from
                     UniProtKB/Swiss-Prot (Q6GX86.1)"
     Region          84..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GX86.1)"
     Region          196..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GX86.1)"
     Region          <198..357
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            281
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3J3; propagated from
                     UniProtKB/Swiss-Prot (Q6GX86.1)"
     Region          441..522
                     /region_name="HROB"
                     /note="Homologous recombination OB-fold protein;
                     pfam15072"
                     /db_xref="CDD:464486"
     Region          531..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GX86.1)"
     CDS             1..607
                     /gene="Hrob"
                     /coded_by="NM_001017988.1:223..2046"
                     /db_xref="GeneID:303566"
                     /db_xref="RGD:1305385"
ORIGIN      
        1 mdflsalena enhivsalpg davclrpnss rpqetpqahs sklspsypas nrsvlglcfp
       61 tsrmpetike ppckgamflr pvsisssssg sqqrmtgtkv sqessgrqss aahsgfifes
      121 cqhgigdfet ldqdefdkal asmefegagl epevnrgasq ilpakhcedp vlakkarvad
      181 lsgsfqegpi vhcrkpwpsl rpttatgglp vpatsdists hqrgspvpap qyspvagrtl
      241 qngpqnyvpg qplqspraws sgkprfsgpq cphsssaafc rgpspsrapv ssvespfstp
      301 rststtvtqp alqtpvvtnh lvqlvtatnr tpqqpsrpsi raktrrfpgp agllphqhsg
      361 enleeimvst pqtpthgala kfqteivtss qgsveedfgr gpwltmksal gldegdptcf
      421 lytysivmvl rkaalkqlpr nkvpnmavmi ksltrstmda svvfkdptge mlgtvhrvll
      481 ethqnelkpg svlllkqigv fspslrnhyl nvtpnnlvhi ysldsgdgdf lkppqplpkd
      541 lgnshgslqp dvaaeptqgl rtaqnppasp eeelpeaddl dgllselped ffcepsgwsc
      601 lktghpp
//
LOCUS       NP_058838               1248 aa            linear   ROD 27-APR-2025
DEFINITION  adenylate cyclase type 8 [Rattus norvegicus].
ACCESSION   NP_058838
VERSION     NP_058838.1
DBSOURCE    REFSEQ: accession NM_017142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1248)
  AUTHORS   Falcon,D., Calderon-Sanchez,E.M., Mayoral-Gonzalez,I.,
            Martin-Bornez,M., Dominguez-Rodriguez,A., Gutierrez-Carretero,E.,
            Ordonez-Fernandez,A., Rosado,J.A. and Smani,T.
  TITLE     Inhibition of adenylyl cyclase 8 prevents the upregulation of Orai1
            channel, which improves cardiac function after myocardial
            infarction
  JOURNAL   Mol Ther 32 (3), 646-662 (2024)
   PUBMED   38291755
  REMARK    GeneRIF: Inhibition of adenylyl cyclase 8 prevents the upregulation
            of Orai1 channel, which improves cardiac function after myocardial
            infarction.
REFERENCE   2  (residues 1 to 1248)
  AUTHORS   Vallin,B., Legueux-Cajgfinger,Y., Clement,N., Glorian,M., Duca,L.,
            Vincent,P., Limon,I. and Blaise,R.
  TITLE     Novel short isoforms of adenylyl cyclase as negative regulators of
            cAMP production
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (9), 1326-1340 (2018)
   PUBMED   29940197
  REMARK    GeneRIF: Data show that the IL-1beta-dependent transdifferentiation
            of VSMCs is associated with the de novo expression of a new family
            of AC8 isoforms. These isoforms are catalytically inactive with
            dominant-negative effects, decreasing total cAMP production. The
            inhibitory effect of AC8E on adenylyl cyclases (ACs) activity is
            accompanied by the formation of heterodimers between AC8E and
            functional ACs.
REFERENCE   3  (residues 1 to 1248)
  AUTHORS   Bernabucci,M. and Zhuo,M.
  TITLE     Calcium activated adenylyl cyclase AC8 but not AC1 is required for
            prolonged behavioral anxiety
  JOURNAL   Mol Brain 9 (1), 60 (2016)
   PUBMED   27234425
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1248)
  AUTHORS   Raoux,M., Vacher,P., Papin,J., Picard,A., Kostrzewa,E., Devin,A.,
            Gaitan,J., Limon,I., Kas,M.J., Magnan,C. and Lang,J.
  TITLE     Multilevel control of glucose homeostasis by adenylyl cyclase 8
  JOURNAL   Diabetologia 58 (4), 749-757 (2015)
   PUBMED   25403481
REFERENCE   5  (residues 1 to 1248)
  AUTHORS   Dou,H., Wang,C., Wu,X., Yao,L., Zhang,X., Teng,S., Xu,H., Liu,B.,
            Wu,Q., Zhang,Q., Hu,M., Wang,Y., Wang,L., Wu,Y., Shang,S., Kang,X.,
            Zheng,L., Zhang,J., Raoux,M., Lang,J., Li,Q., Su,J., Yu,X., Chen,L.
            and Zhou,Z.
  TITLE     Calcium influx activates adenylyl cyclase 8 for sustained insulin
            secretion in rat pancreatic beta cells
  JOURNAL   Diabetologia 58 (2), 324-333 (2015)
   PUBMED   25381556
REFERENCE   6  (residues 1 to 1248)
  AUTHORS   Parkinson,N.A. and Bolsover,S.R.
  TITLE     A nuclear location for Ca2+-activated adenylyl cyclases I and III
            in neurones
  JOURNAL   Brain Res Mol Brain Res 91 (1-2), 43-49 (2001)
   PUBMED   11457491
REFERENCE   7  (residues 1 to 1248)
  AUTHORS   Schaefer,M.L., Wong,S.T., Wozniak,D.F., Muglia,L.M., Liauw,J.A.,
            Zhuo,M., Nardi,A., Hartman,R.E., Vogt,S.K., Luedke,C.E., Storm,D.R.
            and Muglia,L.J.
  TITLE     Altered stress-induced anxiety in adenylyl cyclase type
            VIII-deficient mice
  JOURNAL   J Neurosci 20 (13), 4809-4820 (2000)
   PUBMED   10864938
REFERENCE   8  (residues 1 to 1248)
  AUTHORS   Wong,S.T., Athos,J., Figueroa,X.A., Pineda,V.V., Schaefer,M.L.,
            Chavkin,C.C., Muglia,L.J. and Storm,D.R.
  TITLE     Calcium-stimulated adenylyl cyclase activity is critical for
            hippocampus-dependent long-term memory and late phase LTP
  JOURNAL   Neuron 23 (4), 787-798 (1999)
   PUBMED   10482244
REFERENCE   9  (residues 1 to 1248)
  AUTHORS   Cali,J.J., Parekh,R.S. and Krupinski,J.
  TITLE     Splice variants of type VIII adenylyl cyclase. Differences in
            glycosylation and regulation by Ca2+/calmodulin
  JOURNAL   J Biol Chem 271 (2), 1089-1095 (1996)
   PUBMED   8557635
REFERENCE   10 (residues 1 to 1248)
  AUTHORS   Cali,J.J., Zwaagstra,J.C., Mons,N., Cooper,D.M. and Krupinski,J.
  TITLE     Type VIII adenylyl cyclase. A Ca2+/calmodulin-stimulated enzyme
            expressed in discrete regions of rat brain
  JOURNAL   J Biol Chem 269 (16), 12190-12195 (1994)
   PUBMED   8163524
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L26986.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L26986.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132276,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1248
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..1248
                     /product="adenylate cyclase type 8"
                     /EC_number="4.6.1.1"
                     /note="ATP pyrophosphate-lyase 8; adenylate cyclase type
                     VIII; ca(2+)/calmodulin-activated adenylyl cyclase; type
                     VIII adenylyl cyclase; adenylate cyclase 8 (brain);
                     adenylyl cyclase 8"
                     /calculated_mol_wt=139692
     Region          1..179
                     /region_name="Involved in ORAI1, STIM1, PPP2CA and PPP2R1A
                     interaction. /evidence=ECO:0000269|PubMed:16258073,
                     ECO:0000269|PubMed:22494970, ECO:0000269|PubMed:22976297"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          1..106
                     /region_name="Involved in AKAP5 and PRKAR2A interaction.
                     /evidence=ECO:0000269|PubMed:22976297"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          38..40
                     /region_name="Essential for CALM1 interaction.
                     /evidence=ECO:0000269|PubMed:16258073"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          49..51
                     /region_name="Essential for CALM1 interaction.
                     /evidence=ECO:0000269|PubMed:16258073"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          51..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            55
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P97490; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          211..564
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          402..586
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(414,416..421,456,458..460,463,525..527,531..532,
                     535..536,570)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(416,460)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(421,433,436..437,440,444,456..457,513,516,526..529,
                     532,570)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97490; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Region          614..709
                     /region_name="Adcy_cons_dom"
                     /note="Adenylate cyclase, conserved domain; pfam06327"
                     /db_xref="CDD:461877"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            713..733
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            735..755
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            784..804
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            814
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            818
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            828..848
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            858..878
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            885
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            891..911
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Region          970..1169
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(982,984..989,1031,1033..1035,1038,1106..1108,
                     1112..1113,1116..1117,1153)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(984,1035)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(989,1005,1008..1009,1012,1016,1031..1032,1094,1097,
                     1107..1110,1113,1153)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          1106..1248
                     /region_name="Involved in CALM1 interaction.
                     /evidence=ECO:0000269|PubMed:16258073"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            1196
                     /site_type="other"
                     /note="Essential for autoinhibition maintenance by
                     promoting interaction of the N and C termini.
                     /evidence=ECO:0000269|PubMed:19305019; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Region          1197..1212
                     /region_name="Required for both calcium stimulation and
                     maintenance of autoinhibition.
                     /evidence=ECO:0000269|PubMed:19305019"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     Site            1197
                     /site_type="other"
                     /note="Essential for autoinhibition maintenance.
                     /evidence=ECO:0000269|PubMed:19305019; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            1200
                     /site_type="other"
                     /note="Essential for autoinhibition maintenance by
                     promoting interaction of the N and C termini.
                     /evidence=ECO:0000269|PubMed:19305019; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            1202
                     /site_type="other"
                     /note="Essential for CALM1 interaction.
                     /evidence=ECO:0000269|PubMed:19305019; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Site            1204
                     /site_type="other"
                     /note="Essential for CALM1 interaction.
                     /evidence=ECO:0000269|PubMed:19305019; propagated from
                     UniProtKB/Swiss-Prot (P40146.1)"
     Region          1220..1248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40146.1)"
     CDS             1..1248
                     /gene="Adcy8"
                     /gene_synonym="Ac8"
                     /coded_by="NM_017142.1:777..4523"
                     /db_xref="GeneID:29241"
                     /db_xref="RGD:2036"
ORIGIN      
        1 melsdvhcls gseelytihp tppaadggsg srpqrllwqt avrhiteqrf ihghrggggg
       61 gsrkasnpag sgpnhhapql ssdsvlplys lgsgerahnt ggtkvfpers gsgsasgsgg
      121 ggdlgflhld capsnsdffl nggysyrgvi fptlrnsfks rdlerlyqry flgqrrksev
      181 vmnvldvltk ltllvlhlsl asapmdplkg illgfftgie vvicalvvvr kdttshtylq
      241 ysgvvtwvam ttqilaaglg ygllgdgigy vlftlfatys mlplpltwai laglgtsllq
      301 vtlqvliprl avfsinqvla qvvlfmcmnt agifisylsd raqrqaflet rrcvearlrl
      361 etenqrqerl vlsvlprfvv lemindmtnv edehlqhqfh riyihryenv silfadvkgf
      421 tnlsttlsaq elvrmlnelf arfdrlaheh hclrikilgd cyycvsglpe prqdhahccv
      481 emglsmikti rfvrsrtkhd vdmrigihsg svlcgvlglr kwqfdvwswd vdianklesg
      541 gipgrihisk atldclsgdy nveeghgker neflrkhnie tylikqpees llslpedivk
      601 esvscsdrrn sgatftegsw spelpfdniv gkqntlaalt rnsinllpnh laqalhvqsg
      661 peeinkrieh tidlrsgdkl rrehikpfsl mfkdsslehk ysqmrdevfk snlvcafivl
      721 lfitaiqsll pssrlmpmti qfsilimlhs alvlittaed ykclplilrk tccwinetyl
      781 arnviifasi linflgavin ilwcdfdksi plknltfnss avftdicsyp eyfvftgvla
      841 mvtcavflrl nsvlklavll imiaiyallt etiyaglfls ydnlnhsged flgtkeasll
      901 lmamfllavf yhgqqleyta rldflwrvqa keeinemkdl rehnenmlrn ilpghvarhf
      961 lekdrdneel ysqsydavgv mfasipgfad fysqtemnnq gveclrllne iiadfdellg
     1021 edrfqdieki ktigstymav sglspekqqc edkwghlcal adfslaltes iqeinkhsfn
     1081 nfelrigish gsvvagviga kkpqydiwgk tvnlasrmds tgvsgriqvp eetylilkdq
     1141 gfafdyrgei yvkgiseqeg kiktyfllgr vqpnpfilpp rrlpgqysla avvlglvqsl
     1201 nrqrqkqlln ensnsgiiks hynrrtlltp sgpepgaqae gtdksdlp
//
LOCUS       NP_001101377             427 aa            linear   ROD 27-APR-2025
DEFINITION  terminal nucleotidyltransferase 5B [Rattus norvegicus].
ACCESSION   NP_001101377 XP_001065098 XP_232748
VERSION     NP_001101377.1
DBSOURCE    REFSEQ: accession NM_001107907.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158863.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232748.2, XP_001065098.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158863.1, DN933876.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..427
                     /product="terminal nucleotidyltransferase 5B"
                     /EC_number="2.7.7.19"
                     /note="Protein FAM46B; putative nucleotidyltransferase
                     FAM46B; family with sequence similarity 46, member B;
                     non-canonical poly(A) polymerase FAM46B"
                     /calculated_mol_wt=46885
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNK8.1)"
     Region          52..371
                     /region_name="NTP_transf_7"
                     /note="Nucleotidyltransferase; pfam07984"
                     /db_xref="CDD:462329"
     CDS             1..427
                     /gene="Tent5b"
                     /gene_synonym="Fam46b; RGD1308967"
                     /coded_by="NM_001107907.2:155..1438"
                     /db_xref="GeneID:313019"
                     /db_xref="RGD:1308967"
ORIGIN      
        1 mmpsesgdes leqpaaqvgt gaasavatag aagggpdlea ssaslgrhqs rlswpqvkrl
       61 dallkepipi hgrgnfptls vqpqqivqvv rssleeqglh vhsvrlhgsa ashvlhpesg
      121 lgykdldlvf qmdlqseasf qltkavvlac lldflpagvs rakitpltlk eayvqklvkv
      181 ctdldrwsli slsnksgknv elkfvdsvrr qfefsidsfq iildslllfg qcsstpmsea
      241 fhptvtgesl ygdfaealeh lqhrviatrs peeirgggll kychllvrgf rprpstdvra
      301 lqrymcsrff idfpdpveqr rileryleah fggaeaarry aclvtlhrvv nestvclmsh
      361 errqtldlit mlalqalaeq gpaamaalaw rrpgsdgvvp atvnyyvtpm qpllprahsy
      421 ptwlpcn
//
LOCUS       NP_446078                346 aa            linear   ROD 27-APR-2025
DEFINITION  D-amino-acid oxidase [Rattus norvegicus].
ACCESSION   NP_446078 XP_001080433
VERSION     NP_446078.1
DBSOURCE    REFSEQ: accession NM_053626.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Fukushima,T., Kansaku,A., Umino,M., Sakamoto,T. and Onozato,M.
  TITLE     Evaluation of D-amino acid oxidase activity in rat kidney using a
            D-kynurenine derivative, 6-methylthio-D-kynurenine: An in vivo
            microdialysis study
  JOURNAL   Drug Discov Ther 17 (6), 434-439 (2024)
   PUBMED   38044118
  REMARK    GeneRIF: Evaluation of D-amino acid oxidase activity in rat kidney
            using a D-kynurenine derivative, 6-methylthio-D-kynurenine: An in
            vivo microdialysis study.
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Jiang,H., Zhang,H., Jiang,X. and Wu,S.
  TITLE     Overexpression of D-amino acid oxidase prevents retinal
            neurovascular pathologies in diabetic rats
  JOURNAL   Diabetologia 64 (3), 693-706 (2021)
   PUBMED   33319325
  REMARK    GeneRIF: Overexpression of D-amino acid oxidase prevents retinal
            neurovascular pathologies in diabetic rats.
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Shimizu,Y., Ishii,C., Yanobu-Takanashi,R., Nakano,K., Imaike,A.,
            Mita,M., Hamase,K. and Okamura,T.
  TITLE     d-Amino acid oxidase deficiency is caused by a large deletion in
            the Dao gene in LEA rats
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1868 (9), 140463 (2020)
   PUBMED   32512180
  REMARK    GeneRIF: d-Amino acid oxidase deficiency is caused by a large
            deletion in the Dao gene in LEA rats.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Luks,L., Sacchi,S., Pollegioni,L. and Dietrich,D.R.
  TITLE     Novel insights into renal D-amino acid oxidase accumulation:
            propiverine changes DAAO localization and peroxisomal size in vivo
  JOURNAL   Arch Toxicol 91 (1), 427-437 (2017)
   PUBMED   26961980
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Paul,P., Murphy,T., Oseni,Z., Sivalokanathan,S. and de
            Belleroche,J.S.
  TITLE     Pathogenic effects of amyotrophic lateral sclerosis-linked mutation
            in D-amino acid oxidase are mediated by D-serine
  JOURNAL   Neurobiol Aging 35 (4), 876-885 (2014)
   PUBMED   24138986
  REMARK    GeneRIF: Its toxic effect on motor neurons can be mediated by
            expression in motor neurons and it promotes autophagy.
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Schumacher,J., Jamra,R.A., Freudenberg,J., Becker,T., Ohlraun,S.,
            Otte,A.C., Tullius,M., Kovalenko,S., Bogaert,A.V., Maier,W.,
            Rietschel,M., Propping,P., Nothen,M.M. and Cichon,S.
  TITLE     Examination of G72 and D-amino-acid oxidase as genetic risk factors
            for schizophrenia and bipolar affective disorder
  JOURNAL   Mol Psychiatry 9 (2), 203-207 (2004)
   PUBMED   14966479
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Chumakov,I., Blumenfeld,M., Guerassimenko,O., Cavarec,L.,
            Palicio,M., Abderrahim,H., Bougueleret,L., Barry,C., Tanaka,H., La
            Rosa,P., Puech,A., Tahri,N., Cohen-Akenine,A., Delabrosse,S.,
            Lissarrague,S., Picard,F.P., Maurice,K., Essioux,L., Millasseau,P.,
            Grel,P., Debailleul,V., Simon,A.M., Caterina,D., Dufaure,I.,
            Malekzadeh,K., Belova,M., Luan,J.J., Bouillot,M., Sambucy,J.L.,
            Primas,G., Saumier,M., Boubkiri,N., Martin-Saumier,S., Nasroune,M.,
            Peixoto,H., Delaye,A., Pinchot,V., Bastucci,M., Guillou,S.,
            Chevillon,M., Sainz-Fuertes,R., Meguenni,S., Aurich-Costa,J.,
            Cherif,D., Gimalac,A., Van Duijn,C., Gauvreau,D., Ouellette,G.,
            Fortier,I., Raelson,J., Sherbatich,T., Riazanskaia,N., Rogaev,E.,
            Raeymaekers,P., Aerssens,J., Konings,F., Luyten,W., Macciardi,F.,
            Sham,P.C., Straub,R.E., Weinberger,D.R., Cohen,N. and Cohen,D.
  TITLE     Genetic and physiological data implicating the new human gene G72
            and the gene for D-amino acid oxidase in schizophrenia
  JOURNAL   Proc Natl Acad Sci U S A 99 (21), 13675-13680 (2002)
   PUBMED   12364586
  REMARK    Erratum:[Proc Natl Acad Sci U S A 2002 Dec 24;99(26):17221.
            Ouelette, G [corrected to Ouellette, G]; Realson, J [corrected to
            Raelson, J]]
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Konno,R.
  TITLE     Rat D-amino-acid oxidase cDNA: rat D-amino-acid oxidase as an
            intermediate form between mouse and other mammalian D-amino-acid
            oxidases
  JOURNAL   Biochim Biophys Acta 1395 (2), 165-170 (1998)
   PUBMED   9473656
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Wanders,R.J., Romeyn,G.J., Schutgens,R.B. and Tager,J.M.
  TITLE     L-pipecolate oxidase: a distinct peroxisomal enzyme in man
  JOURNAL   Biochem Biophys Res Commun 164 (1), 550-555 (1989)
   PUBMED   2572224
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Angermuller,S. and Fahimi,H.D.
  TITLE     Heterogenous staining of D-amino acid oxidase in peroxisomes of rat
            liver and kidney. A light and electron microscopic study
  JOURNAL   Histochemistry 88 (3-6), 277-285 (1988)
   PUBMED   2896644
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB003400.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001080433.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB003400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..346
                     /product="D-amino-acid oxidase"
                     /EC_number="1.4.3.3"
                     /note="DAAO; DAMOX; D-amino acid oxidase 1"
                     /calculated_mol_wt=38689
     Region          1..16
                     /region_name="Required for protein stability.
                     /evidence=ECO:0000250|UniProtKB:P14920"
                     /note="propagated from UniProtKB/Swiss-Prot (O35078.1)"
     Region          2..328
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
     Region          215..227
                     /region_name="Active site lid that may open upon
                     substrate/product migration in and out of the active site
                     and close to increase the hydrophobicity of the active
                     site, to make the hydride transfer reaction more
                     efficient. /evidence=ECO:0000250|UniProtKB:P00371"
                     /note="propagated from UniProtKB/Swiss-Prot (O35078.1)"
     Region          344..346
                     /region_name="Microbody targeting signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O35078.1)"
     CDS             1..346
                     /gene="Dao"
                     /gene_synonym="Dao1"
                     /coded_by="NM_053626.1:97..1137"
                     /db_xref="GeneID:114027"
                     /db_xref="RGD:621138"
ORIGIN      
        1 mrvavigagv iglstalcih eryhpaqplh mkiyadrftp fttsdvaagl wqpylsdpsn
       61 pqeaewnqqt fdhlqsclhs pnaekmglal isgynlfrde vpdpfwkstv lgfrkltpse
      121 ldmfpdysyg wfntsllleg ksylswlter ltergvkfih rkvasfeevv rggvdviinc
      181 tgvwagalqa daslqpgrgq iiqveapwik hfilthdpsl giynspyiip gsktvtlggv
      241 fqlgnwseln svhdhntiwk sccqleptlk narimgeltg frpvrpqvrl ererlrfgss
      301 saevihnygh ggygltihwg cameaanlfg kileeknlsr mppshl
//
LOCUS       NP_062235                553 aa            linear   ROD 27-APR-2025
DEFINITION  STE20/SPS1-related proline-alanine-rich protein kinase [Rattus
            norvegicus].
ACCESSION   NP_062235 XP_001057901
VERSION     NP_062235.1
DBSOURCE    REFSEQ: accession NM_019362.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Liu,J., Shelton,E.L., Crescenzi,R., Colvin,D.C., Kirabo,A.,
            Zhong,J., Delpire,E.J., Yang,H.C. and Kon,V.
  TITLE     Kidney Injury Causes Accumulation of Renal Sodium That Modulates
            Renal Lymphatic Dynamics
  JOURNAL   Int J Mol Sci 23 (3), 1428 (2022)
   PUBMED   35163352
  REMARK    GeneRIF: Kidney Injury Causes Accumulation of Renal Sodium That
            Modulates Renal Lymphatic Dynamics.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Gong,Y., Wu,M., Gao,F., Shi,M., Gu,H., Gao,R., Dang,B.Q. and
            Chen,G.
  TITLE     Inhibition of the p-SPAK/p-NKCC1 signaling pathway protects the
            blood-brain barrier and reduces neuronal apoptosis in a rat model
            of surgical brain injury
  JOURNAL   Mol Med Rep 24 (4) (2021)
   PUBMED   34396440
  REMARK    GeneRIF: Inhibition of the pSPAK/pNKCC1 signaling pathway protects
            the bloodbrain barrier and reduces neuronal apoptosis in a rat
            model of surgical brain injury.
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Zhang,J., Gao,G., Begum,G., Wang,J., Khanna,A.R., Shmukler,B.E.,
            Daubner,G.M., de Los Heros,P., Davies,P., Varghese,J.,
            Bhuiyan,M.I., Duan,J., Zhang,J., Duran,D., Alper,S.L., Sun,D.,
            Elledge,S.J., Alessi,D.R. and Kahle,K.T.
  TITLE     Functional kinomics establishes a critical node of volume-sensitive
            cation-Cl- cotransporter regulation in the mammalian brain
  JOURNAL   Sci Rep 6, 35986 (2016)
   PUBMED   27782176
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Kochl,R., Thelen,F., Vanes,L., Brazao,T.F., Fountain,K., Xie,J.,
            Huang,C.L., Lyck,R., Stein,J.V. and Tybulewicz,V.L.
  TITLE     WNK1 kinase balances T cell adhesion versus migration in vivo
  JOURNAL   Nat Immunol 17 (9), 1075-1083 (2016)
   PUBMED   27400149
  REMARK    Erratum:[Nat Immunol. 2017 Jan 19;18(2):246. doi:
            10.1038/ni0217-246a. PMID: 28102214]
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Fezai,M., Elvira,B., Borras,J., Ben-Attia,M., Hoseinzadeh,Z. and
            Lang,F.
  TITLE     Negative regulation of the creatine transporter SLC6A8 by SPAK and
            OSR1
  JOURNAL   Kidney Blood Press Res 39 (6), 546-554 (2014)
   PUBMED   25531585
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Vitari,A.C., Deak,M., Morrice,N.A. and Alessi,D.R.
  TITLE     The WNK1 and WNK4 protein kinases that are mutated in Gordon's
            hypertension syndrome phosphorylate and activate SPAK and OSR1
            protein kinases
  JOURNAL   Biochem J 391 (Pt 1), 17-24 (2005)
   PUBMED   16083423
  REMARK    GeneRIF: WNK1 and WNK4 both interacted with SPAK as well as a
            closely related kinase, termed oxidative stress response kinase-1
            (OSR1).
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Dowd,B.F. and Forbush,B.
  TITLE     PASK (proline-alanine-rich STE20-related kinase), a regulatory
            kinase of the Na-K-Cl cotransporter (NKCC1)
  JOURNAL   J Biol Chem 278 (30), 27347-27353 (2003)
   PUBMED   12740379
  REMARK    GeneRIF: roles in phosphorylation and activation of the Na-K-Cl
            cotransporter (NKCC1)
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Piechotta,K., Lu,J. and Delpire,E.
  TITLE     Cation chloride cotransporters interact with the stress-related
            kinases Ste20-related proline-alanine-rich kinase (SPAK) and
            oxidative stress response 1 (OSR1)
  JOURNAL   J Biol Chem 277 (52), 50812-50819 (2002)
   PUBMED   12386165
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Johnston,A.M., Naselli,G., Gonez,L.J., Martin,R.M., Harrison,L.C.
            and DeAizpurua,H.J.
  TITLE     SPAK, a STE20/SPS1-related kinase that activates the p38 pathway
  JOURNAL   Oncogene 19 (37), 4290-4297 (2000)
   PUBMED   10980603
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Ushiro,H., Tsutsumi,T., Suzuki,K., Kayahara,T. and Nakano,K.
  TITLE     Molecular cloning and characterization of a novel Ste20-related
            protein kinase enriched in neurons and transporting epithelia
  JOURNAL   Arch Biochem Biophys 355 (2), 233-240 (1998)
   PUBMED   9675032
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D88190.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001057901.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D88190.1, AF099990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..553
                     /product="STE20/SPS1-related proline-alanine-rich protein
                     kinase"
                     /EC_number="2.7.11.1"
                     /function="Ste20-related protein kinase"
                     /note="PS/TK; PSTK1; ste-20-related kinase;
                     serine/threonine-protein kinase 39; pancreatic
                     serine/threonine-protein kinase; Ste-20 related kinase"
                     /calculated_mol_wt=59920
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Region          70..346
                     /region_name="STKc_OSR1_SPAK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Oxidative stress response kinase and Ste20-related proline
                     alanine-rich kinase; cd06610"
                     /db_xref="CDD:270787"
     Site            order(78..82,86,99,101,131,147..150,153..154,157,201,
                     203..206,208,218..219,222,241..244,246,274,283)
                     /site_type="active"
                     /db_xref="CDD:270787"
     Site            order(78..82,86,99,101,131,147..150,153..154,157,203,
                     205..206,208,219)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270787"
     Site            order(81..82,201,203..205,222,241..244,246,274,283)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270787"
     Site            order(202..203,227..229,242..255,257..259,263,266..267,
                     270..271,274,280,287,290..292,294..295,329,331..332,334)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270787"
     Site            order(218..231,238..246)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270787"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by WNK1.
                     /evidence=ECO:0000269|PubMed:16083423; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1W9; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCQ.
                     /evidence=ECO:0000250|UniProtKB:Q9UEW8; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Region          319..544
                     /region_name="Interaction with RELT.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1W9"
                     /note="propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Site            358
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEW8; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Region          369..375
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Region          370..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEW8; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by WNK1.
                     /evidence=ECO:0000269|PubMed:16083423,
                     ECO:0000269|PubMed:16263722, ECO:0000269|PubMed:22544747;
                     propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Region          396..400
                     /region_name="Caspase cleavage related site"
                     /note="propagated from UniProtKB/Swiss-Prot (O88506.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1W9; propagated from
                     UniProtKB/Swiss-Prot (O88506.2)"
     Region          460..517
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     CDS             1..553
                     /gene="Stk39"
                     /gene_synonym="Spak"
                     /coded_by="NM_019362.1:417..2078"
                     /db_xref="GeneID:54348"
                     /db_xref="RGD:621643"
ORIGIN      
        1 maepsgspvh vqlpqqaapv taaaaapaaa tsapapapap aapaapapap aaapapapaa
       61 qavgwpicrd ayelqevigs gatavvqaal ckprqervai krinlekcqt smdellkeiq
      121 amsqcshpnv vtyytsfvvk delwlvmkll sggsmldiik yivnrgehkn gvleeaiiat
      181 ilkevlegld ylhrngqihr dlkagnillg edgsvqiadf gvsaflatgg dvtrnkvrkt
      241 fvgtpcwmap evmeqvrgyd fkadmwsfgi taielatgaa pyhkyppmkv lmltlqndpp
      301 tletgvedke mmkkygksfr kllslclqkd pskrptaael lkckffqkak nreyliekll
      361 trtpdiaqra kkvrrvpgss ghlhktedgd wewsddemde kseegkaaas qeksrrvkee
      421 npeisvnagg ipeqiqslsv hdsqgqpnan edyregpcav nlvlrlrnsr kelndirfef
      481 tpgrdtadgv sqelfsaglv dghdvvivaa nlqkivddpk alktltfkla sgcdgaeipd
      541 evkligfaql svs
//
LOCUS       NP_001093644             566 aa            linear   ROD 27-APR-2025
DEFINITION  homeobox protein ARX [Rattus norvegicus].
ACCESSION   NP_001093644 XP_001064618 XP_228590
VERSION     NP_001093644.1
DBSOURCE    REFSEQ: accession NM_001100174.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Navik,U., Rawat,K. and Tikoo,K.
  TITLE     L-Methionine prevents beta-cell damage by modulating the expression
            of Arx, MafA and regulation of FOXO1 in type 1 diabetic rats
  JOURNAL   Acta Histochem 124 (1), 151820 (2022)
   PUBMED   34871948
  REMARK    GeneRIF: L-Methionine prevents beta-cell damage by modulating the
            expression of Arx, MafA and regulation of FOXO1 in type 1 diabetic
            rats.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Curie,A., Nazir,T., Brun,A., Paulignan,Y., Reboul,A., Delange,K.,
            Cheylus,A., Bertrand,S., Rochefort,F., Bussy,G., Marignier,S.,
            Lacombe,D., Chiron,C., Cossee,M., Leheup,B., Philippe,C.,
            Laugel,V., De Saint Martin,A., Sacco,S., Poirier,K., Bienvenu,T.,
            Souville,I., Gilbert-Dussardier,B., Bieth,E., Kauffmann,D.,
            Briot,P., de Freminville,B., Prieur,F., Till,M., Rooryck-Thambo,C.,
            Mortemousque,I., Bobillier-Chaumont,I., Toutain,A., Touraine,R.,
            Sanlaville,D., Chelly,J., Freeman,S., Kong,J., Hadjikhani,N.,
            Gollub,R.L., Roy,A. and des Portes,V.
  TITLE     The c.429_452 duplication of the ARX gene: a unique
            developmental-model of limb kinetic apraxia
  JOURNAL   Orphanet J Rare Dis 9, 25 (2014)
   PUBMED   24528893
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Poeta,L., Fusco,F., Drongitis,D., Shoubridge,C., Manganelli,G.,
            Filosa,S., Paciolla,M., Courtney,M., Collombat,P., Lioi,M.B.,
            Gecz,J., Ursini,M.V. and Miano,M.G.
  TITLE     A regulatory path associated with X-linked intellectual disability
            and epilepsy links KDM5C to the polyalanine expansions in ARX
  JOURNAL   Am J Hum Genet 92 (1), 114-125 (2013)
   PUBMED   23246292
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Du,A., McCracken,K.W., Walp,E.R., Terry,N.A., Klein,T.J., Han,A.,
            Wells,J.M. and May,C.L.
  TITLE     Arx is required for normal enteroendocrine cell development in mice
            and humans
  JOURNAL   Dev Biol 365 (1), 175-188 (2012)
   PUBMED   22387004
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Quille,M.L., Carat,S., Quemener-Redon,S., Hirchaud,E., Baron,D.,
            Benech,C., Guihot,J., Placet,M., Mignen,O., Ferec,C., Houlgatte,R.
            and Friocourt,G.
  TITLE     High-throughput analysis of promoter occupancy reveals new targets
            for Arx, a gene mutated in mental retardation and
            interneuronopathies
  JOURNAL   PLoS One 6 (9), e25181 (2011)
   PUBMED   21966449
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Yoshihara,S., Omichi,K., Yanazawa,M., Kitamura,K. and Yoshihara,Y.
  TITLE     Arx homeobox gene is essential for development of mouse olfactory
            system
  JOURNAL   Development 132 (4), 751-762 (2005)
   PUBMED   15677725
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Poirier,K., Van Esch,H., Friocourt,G., Saillour,Y., Bahi,N.,
            Backer,S., Souil,E., Castelnau-Ptakhine,L., Beldjord,C.,
            Francis,F., Bienvenu,T. and Chelly,J.
  TITLE     Neuroanatomical distribution of ARX in brain and its localisation
            in GABAergic neurons
  JOURNAL   Brain Res Mol Brain Res 122 (1), 35-46 (2004)
   PUBMED   14992814
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Kitamura,K., Yanazawa,M., Sugiyama,N., Miura,H., Iizuka-Kogo,A.,
            Kusaka,M., Omichi,K., Suzuki,R., Kato-Fukui,Y., Kamiirisa,K.,
            Matsuo,M., Kamijo,S., Kasahara,M., Yoshioka,H., Ogata,T.,
            Fukuda,T., Kondo,I., Kato,M., Dobyns,W.B., Yokoyama,M. and
            Morohashi,K.
  TITLE     Mutation of ARX causes abnormal development of forebrain and testes
            in mice and X-linked lissencephaly with abnormal genitalia in
            humans
  JOURNAL   Nat Genet 32 (3), 359-369 (2002)
   PUBMED   12379852
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Scheffer,I.E., Wallace,R.H., Phillips,F.L., Hewson,P., Reardon,K.,
            Parasivam,G., Stromme,P., Berkovic,S.F., Gecz,J. and Mulley,J.C.
  TITLE     X-linked myoclonic epilepsy with spasticity and intellectual
            disability: mutation in the homeobox gene ARX
  JOURNAL   Neurology 59 (3), 348-356 (2002)
   PUBMED   12177367
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Bienvenu,T., Poirier,K., Friocourt,G., Bahi,N., Beaumont,D.,
            Fauchereau,F., Ben Jeema,L., Zemni,R., Vinet,M.C., Francis,F.,
            Couvert,P., Gomot,M., Moraine,C., van Bokhoven,H., Kalscheuer,V.,
            Frints,S., Gecz,J., Ohzaki,K., Chaabouni,H., Fryns,J.P.,
            Desportes,V., Beldjord,C. and Chelly,J.
  TITLE     ARX, a novel Prd-class-homeobox gene highly expressed in the
            telencephalon, is mutated in X-linked mental retardation
  JOURNAL   Hum Mol Genet 11 (8), 981-991 (2002)
   PUBMED   11971879
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EF638804.1.
            
            On or before Jul 29, 2007 this sequence version replaced
            XP_228590.4, XP_001064618.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF638804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..566
                     /product="homeobox protein ARX"
                     /calculated_mol_wt=58516
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6YP92.1)"
     Region          50..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6YP92.1)"
     Region          119..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6YP92.1)"
     Region          286..319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6YP92.1)"
     Region          333..389
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          530..548
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          534..547
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (A6YP92.1)"
     CDS             1..566
                     /gene="Arx"
                     /gene_synonym="RGD1562672"
                     /coded_by="NM_001100174.1:197..1897"
                     /db_xref="GeneID:317268"
                     /db_xref="RGD:1562672"
ORIGIN      
        1 msnqyqeegc serpecksks ptllssycid silgrrspck mrllgaaqsl paplasrtdq
       61 ekamqgspkg ssapfeaelh lppklrrlyg pgggrllqga aaaaaaaaaa aaaaatatgt
      121 agprgevppp pppaarpger qdsagavaaa aaaawdtlki sqapqvsisr sksyrengap
      181 fvppppalde lggpggvahp eerlsaasgp gsapaagggt gteedeeell edeededeee
      241 elleddeeel leddarallk eprrcsvatt gtvaaaaaaa aaaaavateg gelspkeell
      301 lhpedaegkd gedsvclsag sdseegllkr kqrryrttft syqleelera fqkthypdvf
      361 treelamrld ltearvqvwf qnrrakwrkr ekagaqthpp glpfpgplsa thplspylda
      421 spfpphhpal dsawtaaaaa aaaafpslpp ppgsaslpps gaplglstfl gaavfrhpaf
      481 ispafgrlfs tmapltsast aaallrqptp avegavasga ladpataaad rrassiaalr
      541 lkakehaaql tqlnilpgts tgkevc
//
LOCUS       NP_853664                421 aa            linear   ROD 27-APR-2025
DEFINITION  probable G-protein coupled receptor 151 [Rattus norvegicus].
ACCESSION   NP_853664
VERSION     NP_853664.1
DBSOURCE    REFSEQ: accession NM_181633.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Mashiko,M., Kurosawa,A., Tani,Y., Tsuji,T. and Takeda,S.
  TITLE     GPR31 and GPR151 are activated under acidic conditions
  JOURNAL   J Biochem 166 (4), 317-322 (2019)
   PUBMED   31119277
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Broms,J., Antolin-Fontes,B., Tingstrom,A. and Ibanez-Tallon,I.
  TITLE     Conserved expression of the GPR151 receptor in habenular axonal
            projections of vertebrates
  JOURNAL   J Comp Neurol 523 (3), 359-380 (2015)
   PUBMED   25116430
  REMARK    GeneRIF: This study demonstrated that GPR151 expression in the rats
            brain is restricted to habenular neurons projecting to the
            interpeduncular nucleus,Rostromedial tegmental nucleus, rhabdoid
            nucleus, mesencephalic raphe nuclei, and dorsal tegmental nucleus.
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Ignatov,A., Hermans-Borgmeyer,I. and Schaller,H.C.
  TITLE     Cloning and characterization of a novel G-protein-coupled receptor
            with homology to galanin receptors
  JOURNAL   Neuropharmacology 46 (8), 1114-1120 (2004)
   PUBMED   15111018
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Berthold,M., Collin,M., Sejlitz,T., Meister,B. and Lind,P.
  TITLE     Cloning of a novel orphan G protein-coupled receptor (GPCR-2037):
            in situ hybridization reveals high mRNA expression in rat brain
            restricted to neurons of the habenular complex
  JOURNAL   Brain Res Mol Brain Res 120 (1), 22-29 (2003)
   PUBMED   14667573
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ564168.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AJ564168.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..421
                     /product="probable G-protein coupled receptor 151"
                     /note="GPCR-2037; putative G protein-coupled receptor
                     nGPCR-2037"
                     /calculated_mol_wt=46593
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          41..320
                     /region_name="7tmA_GPR151"
                     /note="G protein-coupled receptor 151, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15002"
                     /db_xref="CDD:320133"
     Region          41..67
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320133"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Site            75..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          76..101
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320133"
     Site            order(98,101..102,114..119,121..122,125,169,171..175,202,
                     205..207,209..211,213..214,266,269..270,272..273,276,
                     287..288,290..292,295,298..299)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320133"
     Region          113..143
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320133"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          156..177
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320133"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          202..231
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320133"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          246..276
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320133"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          288..313
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320133"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          346..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     Region          394..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSN5.1)"
     CDS             1..421
                     /gene="Gpr151"
                     /gene_synonym="nGPCR-2037"
                     /coded_by="NM_181633.2:44..1309"
                     /db_xref="GeneID:307475"
                     /db_xref="RGD:727873"
ORIGIN      
        1 mgkatlavfa dsdssnmnes fahlhfaggy lpsdskgwrt iipsllaavc lvgfvgnlcv
       61 iglllhgvwk rkpsmihsli lnlsladisl llfsapvrat ayvkgvwdlg wfvckssdwf
      121 thmcmaaksl tfvvvakvcf myasdpakpv gthnctiwsl lgaiwvvasl lplpewffst
      181 trhhagvemc lvdvpavaae fmslfgklyp llvfclplll agfyfwrayn qckircaktq
      241 nlrnqmrskq ltvmllstav tsallwlpew iawlwvwhlk aggpmppqgf ialsqvlmfs
      301 istvnplifl mmseefkagl kgiwkwmitr kpvvtsevqe vpagnietlp gkapspetqt
      361 cipdtdrcgs pdsskettdk vmvpilpdve qfwherdvgp saqdndpipw ehegqetkgc
      421 n
//
LOCUS       NP_001032392             290 aa            linear   ROD 27-APR-2025
DEFINITION  arylamine N-acetyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_001032392
VERSION     NP_001032392.1
DBSOURCE    REFSEQ: accession NM_001037315.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,Y.J., Meng,F.T., Wang,L.L., Zhang,L.F., Cheng,X.P. and
            Zhou,J.N.
  TITLE     Apolipoprotein E influences melatonin biosynthesis by regulating
            NAT and MAOA expression in C6 cells
  JOURNAL   J Pineal Res 52 (4), 397-402 (2012)
   PUBMED   22225631
  REMARK    GeneRIF: A higher level of melatonin was demonstrated in cultured
            ApoE4-C6 cells than in ApoE3-C6 cells. NAT was up-regulated in
            ApoE4-C6 cells compared with ApoE3-C6 cells, and MAOA and MAOB
            expression decreased in ApoE4-C6 cells.
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Potts,L.F., Cambon,A.C., Ross,O.A., Rademakers,R., Dickson,D.W.,
            Uitti,R.J., Wszolek,Z.K., Rai,S.N., Farrer,M.J., Hein,D.W. and
            Litvan,I.
  TITLE     Polymorphic genes of detoxification and mitochondrial enzymes and
            risk for progressive supranuclear palsy: a case control study
  JOURNAL   BMC Med Genet 13, 16 (2012)
   PUBMED   22424094
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Blomeke,B., Brans,R., Coenraads,P.J., Dickel,H., Bruckner,T.,
            Hein,D.W., Heesen,M., Merk,H.F. and Kawakubo,Y.
  TITLE     Para-phenylenediamine and allergic sensitization: risk modification
            by N-acetyltransferase 1 and 2 genotypes
  JOURNAL   Br J Dermatol 161 (5), 1130-1135 (2009)
   PUBMED   19663877
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Dai,Y., Leng,S., Li,L., Niu,Y., Huang,H., Liu,Q., Duan,H.,
            Cheng,J., Liu,Q. and Zheng,Y.
  TITLE     Effects of genetic polymorphisms of N-Acetyltransferase on
            trichloroethylene-induced hypersensitivity dermatitis among exposed
            workers
  JOURNAL   Ind Health 47 (5), 479-486 (2009)
   PUBMED   19834256
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Barker,D.F., Walraven,J.M., Ristagno,E.H., Doll,M.A., States,J.C.
            and Hein,D.W.
  TITLE     Quantitative tissue and gene-specific differences and developmental
            changes in Nat1, Nat2, and Nat3 mRNA expression in the rat
  JOURNAL   Drug Metab Dispos 36 (12), 2445-2451 (2008)
   PUBMED   18799802
  REMARK    GeneRIF: Results demonstrate differential tissue-specific and
            developmental regulation of the rat Nat1 and Nat2 genes.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Jones,R.F., Land,S.J. and King,C.M.
  TITLE     Recombinant rat and hamster N-acetyltransferases-1 and -2: relative
            rates of N-acetylation of arylamines and N,O-acyltransfer with
            arylhydroxamic acids
  JOURNAL   Carcinogenesis 17 (8), 1729-1733 (1996)
   PUBMED   8761433
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Ebisawa,T., Sasaki,Y. and Deguchi,T.
  TITLE     Complementary DNAs for two arylamine N-acetyltransferases with
            identical 5' non-coding regions from rat pineal gland
  JOURNAL   Eur J Biochem 228 (1), 129-137 (1995)
   PUBMED   7882993
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Vatsis,K.P., Weber,W.W., Bell,D.A., Dupret,J.M., Evans,D.A.,
            Grant,D.M., Hein,D.W., Lin,H.J., Meyer,U.A., Relling,M.V. et al.
  TITLE     Nomenclature for N-acetyltransferases
  JOURNAL   Pharmacogenetics 5 (1), 1-17 (1995)
   PUBMED   7773298
  REMARK    Review article
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Kelly,S.L. and Sim,E.
  TITLE     Arylamine N-acetyltransferase in Balb/c mice: identification of a
            novel mouse isoenzyme by cloning and expression in vitro
  JOURNAL   Biochem J 302 (Pt 2) (Pt 2), 347-353 (1994)
   PUBMED   7545952
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Omura,G.A.
  TITLE     Combination therapy with 5-azacytidine plus
            beta-2'-deoxythioguanosine in adult acute leukemia
  JOURNAL   Cancer Treat Rep 61 (5), 915-917 (1977)
   PUBMED   70273
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U01343.1 and BC078765.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U01343.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..290
                     /product="arylamine N-acetyltransferase 1"
                     /EC_number="2.3.1.5"
                     /note="AT-1; NAT-1; arylamide acetylase 1;
                     N-acetyltransferase type 1; N-acetyltransferase 1
                     (arylamine N-acetyltransferase); N-acetyltransferase
                     (arylamine N-acetyltransferase)"
                     /calculated_mol_wt=33306
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P18440; propagated from
                     UniProtKB/Swiss-Prot (P50297.1)"
     Region          20..280
                     /region_name="Acetyltransf_2"
                     /note="N-acetyltransferase; pfam00797"
                     /db_xref="CDD:395644"
     CDS             1..290
                     /gene="Nat1"
                     /gene_synonym="Nat"
                     /coded_by="NM_001037315.1:325..1197"
                     /db_xref="GeneID:116631"
                     /db_xref="RGD:70490"
ORIGIN      
        1 mdieayferi gyknsvnkld latltevlqh qmravpfenl smhcgeamcl gleatfdhiv
       61 rkkrggwclq vnhllywalt kmgfettmlg gyvyitpvnk yssemvhllv qvtisdrnyi
      121 vdsaygssyq mwepleltsg kdqpqvpaif rlteengtwy ldqirreqdv pnqefvnsdl
      181 lekskyrkiy sftleprtie dfeyvntylq tspasvfvst sfcslqtseg vccligstlt
      241 srrfsykdnv dlvefkslte eeiedvlktt fgislekkfv pkhgelvfti
//
LOCUS       NP_665721                451 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin gamma-1 chain [Rattus norvegicus].
ACCESSION   NP_665721 XP_001081447 XP_001081448 XP_001081449
VERSION     NP_665721.1
DBSOURCE    REFSEQ: accession NM_145778.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hehnly,H. and Doxsey,S.
  TITLE     Rab11 endosomes contribute to mitotic spindle organization and
            orientation
  JOURNAL   Dev Cell 28 (5), 497-507 (2014)
   PUBMED   24561039
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Vaz Meirelles,G., Ferreira Lanza,D.C., da Silva,J.C., Santana
            Bernachi,J., Paes Leme,A.F. and Kobarg,J.
  TITLE     Characterization of hNek6 interactome reveals an important role for
            its short N-terminal domain and colocalization with proteins at the
            centrosome
  JOURNAL   J Proteome Res 9 (12), 6298-6316 (2010)
   PUBMED   20873783
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Di Fiore,B., Ciciarello,M., Mangiacasale,R., Palena,A.,
            Tassin,A.M., Cundari,E. and Lavia,P.
  TITLE     Mammalian RanBP1 regulates centrosome cohesion during mitosis
  JOURNAL   J Cell Sci 116 (Pt 16), 3399-3411 (2003)
   PUBMED   12840069
  REMARK    Erratum:[J Cell Sci. 2003 Sep 1;116(Pt 17):3659]
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Fleming,S.L., Shank,P.R. and Boekelheide,K.
  TITLE     gamma-Tubulin overexpression in Sertoli cells in vivo: I.
            Localization to sites of spermatid head attachment and alterations
            in Sertoli cell microtubule distribution
  JOURNAL   Biol Reprod 69 (1), 310-321 (2003)
   PUBMED   12672673
  REMARK    GeneRIF: gamma-tubulin overexpression caused redistribution of
            Sertoli cell microtubule networks, and a gamma-tubulin-enhanced
            green fluorescent protein fusion protein localized to the site of
            elongate spermatid head attachment to the seminiferous epithelium.
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Fleming,S.L., Shank,P.R. and Boekelheide,K.
  TITLE     gamma-Tubulin overexpression in Sertoli cells in vivo. II:
            Retention of spermatids, residual bodies, and germ cell apoptosis
  JOURNAL   Biol Reprod 69 (1), 322-330 (2003)
   PUBMED   12672672
  REMARK    GeneRIF: gamma-tubulin overexpression disrupts the Sertoli cell
            microtubule network,leads to gross disorganization of the
            seminiferous epithelium, inducing retention of spermatids and
            residual bodies; and causes germ cell apoptosis.
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Nakadai,T., Okada,N., Makino,Y. and Tamura,T.
  TITLE     Structure of rat gamma-tubulin and its binding to HP33
  JOURNAL   DNA Res 6 (3), 207-209 (1999)
   PUBMED   10470852
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Tassin,A.M., Celati,C., Moudjou,M. and Bornens,M.
  TITLE     Characterization of the human homologue of the yeast spc98p and its
            association with gamma-tubulin
  JOURNAL   J Cell Biol 141 (3), 689-701 (1998)
   PUBMED   9566969
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070957.1.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001081448.1, XP_001081449.1, XP_001081447.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070957.1, AB015946.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..451
                     /product="tubulin gamma-1 chain"
                     /note="GCP-1; gamma-1-tubulin; gamma-tubulin complex
                     component 1"
                     /calculated_mol_wt=50970
     Region          3..435
                     /region_name="gamma_tubulin"
                     /note="The gamma-tubulin family; cd02188"
                     /db_xref="CDD:276957"
     Site            order(3,47,133,252,254,258,261..262,264..265,330..331,
                     333..334,337..338,341,353..354,357..358,430,433..434)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:276957"
     Site            order(11..13,16,102,140,142..146,171,173,207,225,228..229)
                     /site_type="other"
                     /note="nucleotide binding site [chemical binding]"
                     /db_xref="CDD:276957"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BRSK1.
                     /evidence=ECO:0000250|UniProtKB:P83887; propagated from
                     UniProtKB/Swiss-Prot (P83888.1)"
     CDS             1..451
                     /gene="Tubg1"
                     /coded_by="NM_145778.2:114..1469"
                     /db_xref="GeneID:252921"
                     /db_xref="RGD:628606"
ORIGIN      
        1 mpreiitlql gqcgnqigfe fwkqlcaehg ispegiveef ategtdrkdv ffyqaddehy
       61 ipravlldle prvihsilns syaklynpen iylsehggga gnnwasgfsq gekihedifd
      121 iidreadgsd slegfvlchs iaggtgsglg syllerlndr ypkklvqtys vfpnqdemsd
      181 vvvqpynsll tlkrltqnad cvvvldntal nliatdrlhi qnpsfsqinq lvstimsast
      241 ttlrypgymn ndligliasl iptprlhflm tgytplttdq svasvrkttv ldvmrrllqp
      301 knvmvstgrd rqtnhcyiai lniiqgevdp tqvhkslqri rerklanfip wgpasiqval
      361 srkspylpsa hrvsglmman htsisslfer tcrqfdklrk reafmeqfrk edifkdnfde
      421 mdtsreivqq lideyhaatr pdyiswgtqe q
//
LOCUS       NP_775429               1642 aa            linear   ROD 27-APR-2025
DEFINITION  cholesterol transporter ABCA5 [Rattus norvegicus].
ACCESSION   NP_775429
VERSION     NP_775429.1
DBSOURCE    REFSEQ: accession NM_173307.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1642)
  AUTHORS   Ye,D., Meurs,I., Ohigashi,M., Calpe-Berdiel,L., Habets,K.L.,
            Zhao,Y., Kubo,Y., Yamaguchi,A., Van Berkel,T.J., Nishi,T. and Van
            Eck,M.
  TITLE     Macrophage ABCA5 deficiency influences cellular cholesterol efflux
            and increases susceptibility to atherosclerosis in female LDLr
            knockout mice
  JOURNAL   Biochem Biophys Res Commun 395 (3), 387-394 (2010)
   PUBMED   20382126
REFERENCE   2  (residues 1 to 1642)
  AUTHORS   Petry,F., Ritz,V., Meineke,C., Middel,P., Kietzmann,T.,
            Schmitz-Salue,C. and Hirsch-Ernst,K.I.
  TITLE     Subcellular localization of rat Abca5, a rat ATP-binding-cassette
            transporter expressed in Leydig cells, and characterization of its
            splice variant apparently encoding a half-transporter
  JOURNAL   Biochem J 393 (Pt 1), 79-87 (2006)
   PUBMED   16162093
  REMARK    GeneRIF: Expression of rAbca5 mRNA in Leydig cells, intracellular
            localization of rAbca5-EGFP/rAbca5-V5 and involvement of
            rAbca5-related proteins in lipid transport suggest that rAbca5 may
            participate in intracellular sterol/steroid trafficking.
REFERENCE   3  (residues 1 to 1642)
  AUTHORS   Kubo,Y., Sekiya,S., Ohigashi,M., Takenaka,C., Tamura,K., Nada,S.,
            Nishi,T., Yamamoto,A. and Yamaguchi,A.
  TITLE     ABCA5 resides in lysosomes, and ABCA5 knockout mice develop
            lysosomal disease-like symptoms
  JOURNAL   Mol Cell Biol 25 (10), 4138-4149 (2005)
   PUBMED   15870284
  REMARK    Erratum:[Mol Cell Biol. 2005 Jul;25(13):5786]
REFERENCE   4  (residues 1 to 1642)
  AUTHORS   Petry,F., Kotthaus,A. and Hirsch-Ernst,K.I.
  TITLE     Cloning of human and rat ABCA5/Abca5 and detection of a human
            splice variant
  JOURNAL   Biochem Biophys Res Commun 300 (2), 343-350 (2003)
   PUBMED   12504089
  REMARK    GeneRIF: Molecular cloning of Abca5.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ426052.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ426052.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1642
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..1642
                     /product="cholesterol transporter ABCA5"
                     /function="transporter"
                     /note="ATP-binding cassette sub-family A member 5;
                     ATP-binding cassette, sub-family A (ABC1), member 5;
                     ATP-binding cassette, subfamily A (ABC1), member 5"
                     /calculated_mol_wt=185680
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CF82.1)"
     Region          <107..1618
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            220..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            327..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            866..886
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            919
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            967..987
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            996
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1021..1041
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1071..1091
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1102..1122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1139..1159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1164..1184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     Site            1207..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CF82.1)"
     CDS             1..1642
                     /gene="Abca5"
                     /coded_by="NM_173307.1:36..4964"
                     /db_xref="GeneID:286970"
                     /db_xref="RGD:628661"
ORIGIN      
        1 matairdvgv wrqtrtlllk nylvkcrtkk ssvqeilfpl fflfwlilis mmhpnkkyee
       61 vsdielspmd ksilsnlilg ytpvtnttss vmqrvstdhl pdvlvteeya sekellassl
      121 skpsnfvgvv fkdvmsyelr ffpdmvpvss vymdsragcs kscdaaqyws sgftalqasi
      181 daaiiqlktn vslwrelest kavimgeaav veidtfprgv iliylviafs pfgyflaihi
      241 vaekekrlke flkimglhdt afwlswvlly tsliflmsll maviatassl fpqsssivif
      301 llfflyglss vffalmltpl fkkskhvgvv effvtvvfgf vgllivlves fprslvwlfs
      361 plcqcaflig iaqvmhledf negalfsslt egpypliitl tmlaldsvfy allavyldqv
      421 ipgefglrrs slyflkpsyw sknkrnykel segningnis lneivepvss efigkeairi
      481 sgiqkayrkk netvealrnl sfdiyegqit allghsgtgk stlmnilcgl cppsdgfasi
      541 yghrvseide mfearkmigi cpqsdmnfdv ltveenlsil asvkgipann iiqevqkvll
      601 dldmqaikdn qakklsggqk rklslgiavl gnpkilllde ptagmdpcsr hivwnllkyr
      661 kanrvtvfst hfmdeadila drkavisqgm lkcvgssifl kskwgigyrl smyidrycat
      721 eslsslvrqh ipaaallqqn dqqivyslpf kdmdkfsglf saldihsnlg visygvsmtt
      781 ledvflklev eaeidqadys vftqqpreee tdsksfdeme qsllilsetk aslvstmslw
      841 kqqvstiakf hflslkresk svrsvlllll iffavqifmf lvhhsfknav vpiklvpdly
      901 flkpgdkphk yktslllqns tdsdindlid fftqqniiva mfndsdyvsa aphsaalnvv
      961 qsekdyvfta vfnstmvysl pvmmniisny ylyhlnvtdt iqiwstpfiq eitdivfkve
     1021 lyfqaallgi ivtamppyfa menaenhkik aytqlklsgl lpsaywigqa vvdiplffvv
     1081 ltlmlgslfa fhhglyfypv kflavvfcli ayvpsvilft yiasftfkki lntkefwsfi
     1141 ysvtalacva vteitfflgy gvtavfhytf ciaipiypll gclisfikgs wknipktena
     1201 ynpwdrllva vimpylqcvl wifllqhyek khggrsirkd plfralsqka khkkfpeppi
     1261 nedededvka erlkvkelmg cqcceekpai mvynlhkeyd dkkdflhsrk ttkvatkyvs
     1321 fcvkkgeilg llgpngagks tiinilvgdv eptsgkiflg dygshsnedd estkcmgycp
     1381 qtnplwpdit lqehfeiyga vkgmssgdmk evisritkal dlkehlqktv kklpagikrk
     1441 lcfalsmlgn pqvtlldeps tgmdprakqh mwrairtafk nkkraalltt hymeeaeavc
     1501 drvaimvsgq lrcigtvqhl kskfgkgyfl eiklkdwien leidrlqrei qyifpnasrq
     1561 esfssilayk ipkedvqsls qsfakleeak htfaieeysf sqatleqvfv eltkeqeeed
     1621 nscgtlnstl wwerrqedrv vf
//
LOCUS       NP_001012120             415 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-N-acetylgalactosaminidase precursor [Rattus norvegicus].
ACCESSION   NP_001012120 XP_235515
VERSION     NP_001012120.1
DBSOURCE    REFSEQ: accession NM_001012120.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Clark,N.E. and Garman,S.C.
  TITLE     The 1.9 a structure of human alpha-N-acetylgalactosaminidase: The
            molecular basis of Schindler and Kanzaki diseases
  JOURNAL   J Mol Biol 393 (2), 435-447 (2009)
   PUBMED   19683538
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Asfaw,B., Schindler,D., Ledvinova,J., Cerny,B., Smid,F. and
            Conzelmann,E.
  TITLE     Degradation of blood group A glycolipid A-6-2 by normal and mutant
            human skin fibroblasts
  JOURNAL   J Lipid Res 39 (9), 1768-1780 (1998)
   PUBMED   9741689
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Wang,A.M., Kanzaki,T. and Desnick,R.J.
  TITLE     The molecular lesion in the alpha-N-acetylgalactosaminidase gene
            that causes angiokeratoma corporis diffusum with glycopeptiduria
  JOURNAL   J Clin Invest 94 (2), 839-845 (1994)
   PUBMED   8040340
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Wang,A.M., Schindler,D. and Desnick,R.
  TITLE     Schindler disease: the molecular lesion in the
            alpha-N-acetylgalactosaminidase gene that causes an infantile
            neuroaxonal dystrophy
  JOURNAL   J Clin Invest 86 (5), 1752-1756 (1990)
   PUBMED   2243144
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082084.1.
            
            On Feb 11, 2005 this sequence version replaced XP_235515.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082084.1, SRR8487231.20403.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..415
                     /product="alpha-N-acetylgalactosaminidase precursor"
                     /EC_number="3.2.1.49"
                     /note="alpha-galactosidase B; N-acetyl galactosaminidase,
                     alpha"
                     /calculated_mol_wt=45005
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1884
     mat_peptide     18..415
                     /product="Alpha-N-acetylgalactosaminidase.
                     /id=PRO_0000001020"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H12.1)"
                     /calculated_mol_wt=45005
     Region          25..308
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Site            order(33,78..79,119,154,156,188,213,217)
                     /site_type="active"
                     /db_xref="CDD:269893"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     Region          311..394
                     /region_name="Melibiase_2_C"
                     /note="Alpha galactosidase A C-terminal beta sandwich
                     domain; pfam17450"
                     /db_xref="CDD:407508"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17050; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17050; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H12.1)"
     CDS             1..415
                     /gene="Naga"
                     /coded_by="NM_001012120.1:53..1300"
                     /db_xref="GeneID:315165"
                     /db_xref="RGD:1306025"
ORIGIN      
        1 mlqktvllla lvaqvlmlen gllrtppmgw lawerfrcni nceedpknci serlfmemad
       61 rlaqdgwrdl gyvylniddc wiggrdatgr lipdpkrfph giafladyah slglklgiye
      121 dmgkmtcmgy pgttldkvel daatfaewkv dmlkldgcys tpkeraegyp kmaaalnatg
      181 rpiafscswp ayegglppkv nytevagtcn lwrnykdiqd swksvlsild wfvkhqdilq
      241 pvsgpghwnd pdmllignfg lsfdesraqm alwtvlaapl fmstdlrtis pqnidilqnp
      301 llikinqdpl giqgrlifks kshievfkrn lsddasalvf fsrrtdmpyh fhcsllelny
      361 pkgsvyegqn vftgdiisgl hpetnftvii npsgvvmwyl ypvkglgiyt mmsql
//
LOCUS       NP_073636                243 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
            [Rattus norvegicus].
ACCESSION   NP_073636 XP_002726866 XP_003750300
VERSION     NP_073636.1
DBSOURCE    REFSEQ: accession NM_022799.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Parplys,A.C., Zhao,W., Sharma,N., Groesser,T., Liang,F.,
            Maranon,D.G., Leung,S.G., Grundt,K., Dray,E., Idate,R.,
            Ostvold,A.C., Schild,D., Sung,P. and Wiese,C.
  TITLE     NUCKS1 is a novel RAD51AP1 paralog important for homologous
            recombination and genome stability
  JOURNAL   Nucleic Acids Res 43 (20), 9817-9834 (2015)
   PUBMED   26323318
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Qiu,B., Shi,X., Zhou,Q., Chen,H.S., Lim,J., Han,W. and
            Tergaonkar,V.
  TITLE     Hypothalamic NUCKS regulates peripheral glucose homoeostasis
  JOURNAL   Biochem J 469 (3), 391-398 (2015)
   PUBMED   26205492
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kim,H.Y., Choi,B.S., Kim,S.S., Roh,T.Y., Park,J. and Yoon,C.H.
  TITLE     NUCKS1, a novel Tat coactivator, plays a crucial role in HIV-1
            replication by increasing Tat-mediated viral transcription on the
            HIV-1 LTR promoter
  JOURNAL   Retrovirology 11, 67 (2014)
   PUBMED   25116364
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Qiu,B., Shi,X., Wong,E.T., Lim,J., Bezzi,M., Low,D., Zhou,Q.,
            Akincilar,S.C., Lakshmanan,M., Swa,H.L., Tham,J.M., Gunaratne,J.,
            Cheng,K.K., Hong,W., Lam,K.S., Ikawa,M., Guccione,E., Xu,A., Han,W.
            and Tergaonkar,V.
  TITLE     NUCKS is a positive transcriptional regulator of insulin signaling
  JOURNAL   Cell Rep 7 (6), 1876-1886 (2014)
   PUBMED   24931609
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Drosos,Y., Kouloukoussa,M., Ostvold,A.C., Havaki,S., Katsantoni,E.,
            Marinos,E. and Aleporou-Marinou,V.
  TITLE     Dynamic expression of the vertebrate-specific protein Nucks during
            rodent embryonic development
  JOURNAL   Gene Expr Patterns 14 (1), 19-29 (2014)
   PUBMED   24140890
  REMARK    GeneRIF: Results show that Nucks expression increased during the
            initial stages of embryonic development, and then gradually
            decreased until birth in all tissues except the nervous tissue and
            muscle fibers.
            GeneRIF: The expression of Nucks in both proliferating and
            quiescent cells and its correlation with Bax levels and apoptosis
            strongly suggest that Nucks plays complex roles in cell
            homeostasis.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Yu,S., Wang,H., Davis,A. and Ahmed,K.
  TITLE     Consequences of CK2 signaling to the nuclear matrix
  JOURNAL   Mol Cell Biochem 227 (1-2), 67-71 (2001)
   PUBMED   11827176
  REMARK    GeneRIF: Consequences of CK2 signaling to the nuclear matrix.
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Ostvold,A.C., Norum,J.H., Mathiesen,S., Wanvik,B., Sefland,I. and
            Grundt,K.
  TITLE     Molecular cloning of a mammalian nuclear phosphoprotein NUCKS,
            which serves as a substrate for Cdk1 in vivo
  JOURNAL   Eur J Biochem 268 (8), 2430-2440 (2001)
   PUBMED   11298763
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Ostvold,A.C., Hullstein,I. and Laland,S.G.
  TITLE     The phosphate groups of the high mobility group like protein P1
            strengthens its affinity for DNA
  JOURNAL   Biochem Biophys Res Commun 185 (3), 1091-1097 (1992)
   PUBMED   1627131
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Omeke,B.C. and Onuora,G.I.
  TITLE     Genital lesions and histopathology of male guinea-pigs infected
            with trypanosomes
  JOURNAL   Rev Elev Med Vet Pays Trop 45 (1), 27-30 (1992)
   PUBMED   1298022
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Ostvold,A.C., Holtlund,J. and Laland,S.G.
  TITLE     A novel, highly phosphorylated protein, of the high-mobility group
            type, present in a variety of proliferating and non-proliferating
            mammalian cells
  JOURNAL   Eur J Biochem 153 (3), 469-475 (1985)
   PUBMED   3000779
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078818.1.
            
            On or before Sep 8, 2012 this sequence version replaced
            XP_002726866.1, XP_003750300.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078818.1, AJ237669.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..243
                     /product="nuclear ubiquitous casein and cyclin-dependent
                     kinase substrate 1"
                     /note="nuclear ubiquitous casein and cyclin-dependent
                     kinases substrate; nuclear ubiquitous casein kinase and
                     cyclin-dependent kinase substrate; nuclear ubiquitous
                     casein kinase 2; nuclear ubiquitous casein and
                     cyclin-dependent kinases substrate-like"
                     /calculated_mol_wt=27009
     Region          1..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80XU3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1E3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1E3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1E3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1E3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1E3; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9EPJ0.1)"
     CDS             1..243
                     /gene="Nucks1"
                     /gene_synonym="Nucks"
                     /coded_by="NM_022799.2:176..907"
                     /db_xref="GeneID:64709"
                     /db_xref="RGD:620993"
ORIGIN      
        1 msrpvrnrkv vdysqfqesd dadedygrds gppakkirss preaknkrrs gknsqedsed
       61 seekdvktkk ddshsaedse dekddhksvr qqrqaaskaa skqremlled vgseeepeed
      121 deapfqekds gsdedflmed dddsdygssk kknkkmvkks kperkekkmp kprlkatvtp
      181 spvkgkgkvg rptasktske ktpspkeede eaesppekkt sasppleksg degsedeaas
      241 ged
//
LOCUS       NP_001020587             480 aa            linear   ROD 27-APR-2025
DEFINITION  docking protein 1 [Rattus norvegicus].
ACCESSION   NP_001020587 XP_232106
VERSION     NP_001020587.1
DBSOURCE    REFSEQ: accession NM_001025416.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Goel,R.K., Miah,S., Black,K., Kalra,N., Dai,C. and Lukong,K.E.
  TITLE     The unique N-terminal region of SRMS regulates enzymatic activity
            and phosphorylation of its novel substrate docking protein 1
  JOURNAL   FEBS J 280 (18), 4539-4559 (2013)
   PUBMED   23822091
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Berger,A.H., Niki,M., Morotti,A., Taylor,B.S., Socci,N.D.,
            Viale,A., Brennan,C., Szoke,J., Motoi,N., Rothman,P.B.,
            Teruya-Feldstein,J., Gerald,W.L., Ladanyi,M. and Pandolfi,P.P.
  TITLE     Identification of DOK genes as lung tumor suppressors
  JOURNAL   Nat Genet 42 (3), 216-223 (2010)
   PUBMED   20139980
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Hiragun,T., Peng,Z. and Beaven,M.A.
  TITLE     Dexamethasone up-regulates the inhibitory adaptor protein Dok-1 and
            suppresses downstream activation of the mitogen-activated protein
            kinase pathway in antigen-stimulated RBL-2H3 mast cells
  JOURNAL   Mol Pharmacol 67 (3), 598-603 (2005)
   PUBMED   15608142
  REMARK    GeneRIF: Dok-1 is the mediator of the antiallergic actions of
            dexamethasone and as a negative regulator of the MAP kinase pathway
            and downstream release of inflammatory mediators.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Abramson,J., Rozenblum,G. and Pecht,I.
  TITLE     Dok protein family members are involved in signaling mediated by
            the type 1 Fcepsilon receptor
  JOURNAL   Eur J Immunol 33 (1), 85-91 (2003)
   PUBMED   12594836
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Berg,K.L., Siminovitch,K.A. and Stanley,E.R.
  TITLE     SHP-1 regulation of p62(DOK) tyrosine phosphorylation in
            macrophages
  JOURNAL   J Biol Chem 274 (50), 35855-35865 (1999)
   PUBMED   10585470
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Yamanashi,Y. and Baltimore,D.
  TITLE     Identification of the Abl- and rasGAP-associated 62 kDa protein as
            a docking protein, Dok
  JOURNAL   Cell 88 (2), 205-211 (1997)
   PUBMED   9008161
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097972.1.
            
            On Jul 15, 2005 this sequence version replaced XP_232106.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097972.1, CV115728.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..480
                     /product="docking protein 1"
                     /note="downstream of tyrosine kinase 1"
                     /calculated_mol_wt=52039
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Region          6..119
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Region          151..253
                     /region_name="PTB_DOK1_DOK2_DOK3"
                     /note="Downstream of tyrosine kinase 1, 2, and 3 proteins
                     phosphotyrosine-binding domain (PTBi); cd01203"
                     /db_xref="CDD:269914"
     Site            order(161,167)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269914"
     Site            order(203..211,217,221..222,242,249,252)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:269914"
     Region          253..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97465; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97465; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by INSR.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by INSR.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Region          398..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99704; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97465; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97465; propagated from
                     UniProtKB/Swiss-Prot (Q4QQV2.1)"
     CDS             1..480
                     /gene="Dok1"
                     /gene_synonym="Dok-1"
                     /coded_by="NM_001025416.1:9..1451"
                     /db_xref="GeneID:312477"
                     /db_xref="RGD:1309499"
ORIGIN      
        1 mdgalmegpl flqsqrfgtk rwkktwavly pasphgvarl effdhkgsss gggrggsrrl
       61 dckmirlaec vsvvpvtves ppepgasafr ldtaqrshll aadaasstaw vqilcrtafp
      121 kggwalaqte nppkfsalem lenslysptw egsqfwvtsq kteasercgl qgsyvlrvea
      181 ekltlltlga qsqilepllf wpytllrryg rdkvmfsfea grrcpsgpgt ftfqtaqgnd
      241 ifqaveaaiq qqkaqgkvgq gqditrtdsh dgetegkmap tpvpqeplgs ppalyaepld
      301 slrippgpsq dslysdplgs tpagagegvq rkkplywdly ghvqqqllkt klidskedpi
      361 ydepeglapa plrglydlpq epkdawwcqa rlkeegyelp ynpatddyav ppprsskptp
      421 apkpqglilp esgttagsgs kgsdtalysq vqksgtpgrw dcglsrvgnd rvgvksegst
//
LOCUS       NP_001138941             166 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein-signaling modulator 1 isoform b [Rattus norvegicus].
ACCESSION   NP_001138941
VERSION     NP_001138941.1
DBSOURCE    REFSEQ: accession NM_001145469.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Conley,J.M. and Watts,V.J.
  TITLE     Differential effects of AGS3 expression on D(2L) dopamine
            receptor-mediated adenylyl cyclase signaling
  JOURNAL   Cell Mol Neurobiol 33 (4), 551-558 (2013)
   PUBMED   23504261
  REMARK    GeneRIF: AGS3 reduced D(2L)DR-mediated sensitization of AC1 and
            AC2.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Wang,W., Li,Q., Zou,F., Yu,Z., Wang,Y., Lu,T., Hu,T. and Cui,G.
  TITLE     Increased expression of AGS3 in rat brain cortex after traumatic
            brain injury
  JOURNAL   J Neurosci Res 91 (5), 726-736 (2013)
   PUBMED   23404409
  REMARK    GeneRIF: This study demonistrated that the ags3 expression
            increassing in rat brain cortex after traumatic brain injury.
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Regner,K.R., Nozu,K., Lanier,S.M., Blumer,J.B., Avner,E.D.,
            Sweeney,W.E. Jr. and Park,F.
  TITLE     Loss of activator of G-protein signaling 3 impairs renal tubular
            regeneration following acute kidney injury in rodents
  JOURNAL   FASEB J 25 (6), 1844-1855 (2011)
   PUBMED   21343176
  REMARK    GeneRIF: These data suggest that Gpsm1 acts through a novel
            receptor-independent mechanism to facilitate renal tubular
            epithelial cell proliferation and renal tubular regeneration.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Xu,Z., Xia,B., Gong,Q., Bailey,J., Groves,B., Radeke,M., Wood,S.A.,
            Szumlinski,K.K. and Ma,D.
  TITLE     Identification of a deubiquitinating enzyme as a novel
            AGS3-interacting protein
  JOURNAL   PLoS One 5 (3), e9725 (2010)
   PUBMED   20305814
  REMARK    GeneRIF: levels of AGS3 and USP9x are co-regulated in the
            prefrontal cortex of rats withdrawn from repeated cocaine treatment
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Bernard,M.L., Peterson,Y.K., Chung,P., Jourdan,J. and Lanier,S.M.
  TITLE     Selective interaction of AGS3 with G-proteins and the influence of
            AGS3 on the activation state of G-proteins
  JOURNAL   J Biol Chem 276 (2), 1585-1593 (2001)
   PUBMED   11042168
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Natochin,M., Lester,B., Peterson,Y.K., Bernard,M.L., Lanier,S.M.
            and Artemyev,N.O.
  TITLE     AGS3 inhibits GDP dissociation from galpha subunits of the Gi
            family and rhodopsin-dependent activation of transducin
  JOURNAL   J Biol Chem 275 (52), 40981-40985 (2000)
   PUBMED   11024022
REFERENCE   8  (residues 1 to 166)
  AUTHORS   De Vries,L., Fischer,T., Tronchere,H., Brothers,G.M.,
            Strockbine,B., Siderovski,D.P. and Farquhar,M.G.
  TITLE     Activator of G protein signaling 3 is a guanine dissociation
            inhibitor for Galpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14364-14369 (2000)
   PUBMED   11121039
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Peterson,Y.K., Bernard,M.L., Ma,H., Hazard,S. 3rd, Graber,S.G. and
            Lanier,S.M.
  TITLE     Stabilization of the GDP-bound conformation of Gialpha by a peptide
            derived from the G-protein regulatory motif of AGS3
  JOURNAL   J Biol Chem 275 (43), 33193-33196 (2000)
   PUBMED   10969064
  REMARK    GeneRIF: The GPR motif in this protein and other proteins is
            actually associated with activity as a GDI - guanine nucleotide
            dissociation inhibitor and not GTPase activator as initially
            suggested.
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Takesono,A., Cismowski,M.J., Ribas,C., Bernard,M., Chung,P.,
            Hazard,S. 3rd, Duzic,E. and Lanier,S.M.
  TITLE     Receptor-independent activators of heterotrimeric G-protein
            signaling pathways
  JOURNAL   J Biol Chem 274 (47), 33202-33205 (1999)
   PUBMED   10559191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC086535.1.
            
            Transcript Variant: This variant (2, also known as AGS3-SHORT-1)
            differs in the 5' UTR, lacks several exons in the 5' coding region
            and uses a downstream translational start codon, compared to
            variant 1. The resulting isoform (b) is shorter at the N-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086535.1, CK359069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132308, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..166
                     /product="G-protein-signaling modulator 1 isoform b"
                     /note="activator of G-protein signaling 3; G-protein
                     signalling modulator 1 (AGS3-like, C. elegans); G-protein
                     signaling modulator 1 (AGS3-like, C. elegans)"
                     /calculated_mol_wt=17987
     Region          40..60
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          88..108
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          122..143
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     CDS             1..166
                     /gene="Gpsm1"
                     /gene_synonym="Ags3"
                     /coded_by="NM_001145469.1:200..700"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:246254"
                     /db_xref="RGD:628682"
ORIGIN      
        1 mddqrcplee gqagaaeata aptleeraaq psvtaspqte effdliassq srrlddqras
       61 vgslpglrit lnnvghlrgd gdpqepgdef fnmlikyqss riddqrcppp dvlprgptmp
      121 dedffsliqr vqakrmdeqr vdlagspdqe asglpdprqq cppgas
//
LOCUS       NP_001007655             160 aa            linear   ROD 27-APR-2025
DEFINITION  type-1 angiotensin II receptor-associated protein [Rattus
            norvegicus].
ACCESSION   NP_001007655 XP_216588
VERSION     NP_001007655.1
DBSOURCE    REFSEQ: accession NM_001007654.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Sotozawa,M., Kinguchi,S., Wakui,H., Azushima,K., Funakoshi,K.,
            Nakajima,W., Miyazaki,T., Takahashi,T. and Tamura,K.
  TITLE     Enhancement of angiotensin II type 1 receptor-associated protein in
            the paraventricular nucleus suppresses angiotensin II-dependent
            hypertension
  JOURNAL   Hypertens Res 47 (1), 67-77 (2024)
   PUBMED   37884662
  REMARK    GeneRIF: Enhancement of angiotensin II type 1 receptor-associated
            protein in the paraventricular nucleus suppresses angiotensin
            II-dependent hypertension.
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Huang,H., Zhou,J., Cui,Z., Wang,B. and Hu,Y.
  TITLE     Angiotensin II type 1 receptor-associated protein plays a role in
            regulating the local renin-angiotensin system in HSC-T6 cells
  JOURNAL   Mol Med Rep 12 (3), 3763-3768 (2015)
   PUBMED   26018598
  REMARK    GeneRIF: A single dose of angiotensin(17) at the same concentration
            as angiotensin II induced Agtrap gene expression.
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Flister,M.J., Tsaih,S.W., O'Meara,C.C., Endres,B., Hoffman,M.J.,
            Geurts,A.M., Dwinell,M.R., Lazar,J., Jacob,H.J. and Moreno,C.
  TITLE     Identifying multiple causative genes at a single GWAS locus
  JOURNAL   Genome Res 23 (12), 1996-2002 (2013)
   PUBMED   24006081
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Granado,M., Fernandez,N., Monge,L., Figueras,J.C.,
            Carreno-Tarragona,G., Amor,S. and Garcia-Villalon,A.L.
  TITLE     Effects of coronary ischemia-reperfusion in a rat model of early
            overnutrition. Role of angiotensin receptors
  JOURNAL   PLoS One 8 (2), e54984 (2013)
   PUBMED   23383303
  REMARK    GeneRIF: The expression of both angiotensin AGTRa and AGTR2
            receptors was increased in the myocardium of overfed rats, and
            ischemia-reperfusion increased the expression of both receptors in
            control rats but reduced it in overfed rats.
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Wenzel,K., Rajakumar,A., Haase,H., Geusens,N., Hubner,N.,
            Schulz,H., Brewer,J., Roberts,L., Hubel,C.A., Herse,F., Hering,L.,
            Qadri,F., Lindschau,C., Wallukat,G., Pijnenborg,R., Heidecke,H.,
            Riemekasten,G., Luft,F.C., Muller,D.N., Lamarca,B. and Dechend,R.
  TITLE     Angiotensin II type 1 receptor antibodies and increased angiotensin
            II sensitivity in pregnant rats
  JOURNAL   Hypertension 58 (1), 77-84 (2011)
   PUBMED   21576625
  REMARK    GeneRIF: AT(1)-AB induces Ang II sensitivity. Our mechanistic study
            supports the existence of an 'autoimmune-activating receptor' that
            could contribute to Ang II sensitivity and possible to
            preeclampsia.
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Gustavsson,M., Mallard,C., Vannucci,S.J., Wilson,M.A.,
            Johnston,M.V. and Hagberg,H.
  TITLE     Vascular response to hypoxic preconditioning in the immature brain
  JOURNAL   J Cereb Blood Flow Metab 27 (5), 928-938 (2007)
   PUBMED   17033689
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Tanaka,Y., Tamura,K., Koide,Y., Sakai,M., Tsurumi,Y., Noda,Y.,
            Umemura,M., Ishigami,T., Uchino,K., Kimura,K., Horiuchi,M. and
            Umemura,S.
  TITLE     The novel angiotensin II type 1 receptor (AT1R)-associated protein
            ATRAP downregulates AT1R and ameliorates cardiomyocyte hypertrophy
  JOURNAL   FEBS Lett 579 (7), 1579-1586 (2005)
   PUBMED   15757644
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Cui,T., Nakagami,H., Iwai,M., Takeda,Y., Shiuchi,T., Tamura,K.,
            Daviet,L. and Horiuchi,M.
  TITLE     ATRAP, novel AT1 receptor associated protein, enhances
            internalization of AT1 receptor and inhibits vascular smooth muscle
            cell growth
  JOURNAL   Biochem Biophys Res Commun 279 (3), 938-941 (2000)
   PUBMED   11162453
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Akishita,M., Yamada,H., Dzau,V.J. and Horiuchi,M.
  TITLE     Increased vasoconstrictor response of the mouse lacking angiotensin
            II type 2 receptor
  JOURNAL   Biochem Biophys Res Commun 261 (2), 345-349 (1999)
   PUBMED   10425188
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Daviet,L., Lehtonen,J.Y., Tamura,K., Griese,D.P., Horiuchi,M. and
            Dzau,V.J.
  TITLE     Cloning and characterization of ATRAP, a novel protein that
            interacts with the angiotensin II type 1 receptor
  JOURNAL   J Biol Chem 274 (24), 17058-17062 (1999)
   PUBMED   10358057
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082019.1.
            
            On Nov 29, 2004 this sequence version replaced XP_216588.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082019.1, DN933749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132301, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..160
                     /product="type-1 angiotensin II receptor-associated
                     protein"
                     /note="AT1 receptor-associated protein; angiotensin II,
                     type I receptor-associated protein"
                     /calculated_mol_wt=17267
     Region          1..160
                     /region_name="AGTRAP"
                     /note="Angiotensin II, type I receptor-associated protein;
                     smart00805"
                     /db_xref="CDD:197883"
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A2.1)"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A2.1)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A2.1)"
     Region          110..122
                     /region_name="Interaction with AGTR1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A2.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6RW13; propagated from
                     UniProtKB/Swiss-Prot (Q642A2.1)"
     Region          128..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A2.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6RW13; propagated from
                     UniProtKB/Swiss-Prot (Q642A2.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6RW13; propagated from
                     UniProtKB/Swiss-Prot (Q642A2.1)"
     CDS             1..160
                     /gene="Agtrap"
                     /coded_by="NM_001007654.1:42..524"
                     /db_xref="GeneID:298646"
                     /db_xref="RGD:1359346"
ORIGIN      
        1 melpavnlkv illvhwlltt wgclafsgsy awgnftilal gvwavaqrds vdaigmflgg
       61 lvatifldii yisifyssva vgdtgrfsag maifslllkp fscclvyhmh rerggelplr
      121 sdffgpsqeh sayqtidssd spadplasle nkgqaaprgy
//
LOCUS       NP_775446                619 aa            linear   ROD 27-APR-2025
DEFINITION  TOX high mobility group box family member 4 [Rattus norvegicus].
ACCESSION   NP_775446
VERSION     NP_775446.2
DBSOURCE    REFSEQ: accession NM_173324.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Lee,J.H., You,J., Dobrota,E. and Skalnik,D.G.
  TITLE     Identification and characterization of a novel human PP1
            phosphatase complex
  JOURNAL   J Biol Chem 285 (32), 24466-24476 (2010)
   PUBMED   20516061
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081696.1.
            
            On Sep 16, 2004 this sequence version replaced NP_775446.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081696.1, FQ212245.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..619
                     /product="TOX high mobility group box family member 4"
                     /note="epidermal Langerhans cell protein LCP1"
                     /calculated_mol_wt=65867
     Region          140..>306
                     /region_name="NHP6B"
                     /note="Chromatin-associated proteins containing the HMG
                     domain [Chromatin structure and dynamics]; COG5648"
                     /db_xref="CDD:227935"
     Region          155..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BU11; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Region          213..218
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PM1.1)"
     Region          224..293
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(224..225,227..231,234..235,242,254..255,258,
                     261..262,269,273,276,280,283)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     Region          304..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Region          436..458
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PM1.1)"
     Region          <464..530
                     /region_name="Peptidase_S21"
                     /note="Assemblin (Peptidase family S21); cl25932"
                     /db_xref="CDD:330753"
     Site            479
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94842; propagated from
                     UniProtKB/Swiss-Prot (Q99PM1.1)"
     CDS             1..619
                     /gene="Tox4"
                     /gene_synonym="RGD708449"
                     /coded_by="NM_173324.2:57..1916"
                     /db_xref="GeneID:286990"
                     /db_xref="RGD:708449"
ORIGIN      
        1 mefpggndny ltitgpshpf lsgaetfhtp slgdeefeip pisldsdpsl avsdvvghfd
       61 dladpsssqd gsfsaqygvq tldmpvgmth glmeqgggll sggltmdldh sigtqysanp
      121 pvtidvpmtd mtsglmghsq lttidqsels sqlglslggg tilppaqspe drlsttpspt
      181 nslhedgvdd frrqlpaqkt vvvetgkkqk apkkrkkkdp nepqkpvsay alffrdtqaa
      241 ikgqnpnatf gevskivasm wdslgeeqkq vykrkteaak keylkalaay kdnqecqatv
      301 etveldpvpq sqtpspppvt tadpaspapa stespalspc ivvnstlssy vanqassgpg
      361 gqpnitklii tkqmlpssit msqggmvtvi patvvtsrgl qlgqtstati qpsqqaqivt
      421 rsvlqaaaaa aasmqlpppr lqppplqqmp qpptqqqvti lqqppplqam qqpppqkvri
      481 nlqqqppplq skivpppalk mqatvlpptv esspeqpmns speahtveat speticemia
      541 dvvpevesps qmdvelvsgs pvtlspqprc vrsgcenppv iskdwdneyc snecvvkhcr
      601 dvflawvasr npnsvvfvk
//
LOCUS       NP_001034111             327 aa            linear   ROD 27-APR-2025
DEFINITION  2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
            precursor [Rattus norvegicus].
ACCESSION   NP_001034111 XP_222227
VERSION     NP_001034111.1
DBSOURCE    REFSEQ: accession NM_001039022.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nguyen,T.P., Casarin,A., Desbats,M.A., Doimo,M., Trevisson,E.,
            Santos-Ocana,C., Navas,P., Clarke,C.F. and Salviati,L.
  TITLE     Molecular characterization of the human COQ5 C-methyltransferase in
            coenzyme Q10 biosynthesis
  JOURNAL   Biochim Biophys Acta 1841 (11), 1628-1638 (2014)
   PUBMED   25152161
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098719.1.
            
            On Jan 12, 2006 this sequence version replaced XP_222227.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098719.1, FQ219423.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132303, SAMD00155314
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..327
                     /product="2-methoxy-6-polyprenyl-1,4-benzoquinol
                     methylase, mitochondrial precursor"
                     /EC_number="2.1.1.201"
                     /note="ubiquinone biosynthesis methyltransferase COQ5,
                     mitochondrial; 2-methoxy-6-polyprenyl-1,4-benzoquinol
                     methylase, mitochondrial; coenzyme Q5 homolog,
                     methyltransferase"
                     /calculated_mol_wt=31866
     transit_peptide 1..49
                     /note="Mitochondrion.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03191; propagated from
                     UniProtKB/Swiss-Prot (Q4G064.1)"
                     /calculated_mol_wt=5453
     mat_peptide     50..327
                     /product="2-methoxy-6-polyprenyl-1,4-benzoquinol
                     methylase, mitochondrial. /id=PRO_0000228631"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G064.1)"
                     /calculated_mol_wt=31866
     Region          56..327
                     /region_name="ubiE"
                     /note="bifunctional demethylmenaquinone
                     methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol
                     methylase UbiE; PRK00216"
                     /db_xref="CDD:234689"
     CDS             1..327
                     /gene="Coq5"
                     /gene_synonym="RGD1310857"
                     /coded_by="NM_001039022.1:4..987"
                     /db_xref="GeneID:304542"
                     /db_xref="RGD:1310857"
ORIGIN      
        1 maaprscvlw sycghgwsrl agdcrlpgfr rswlgatlsa rslsqekraa ethfgfetvs
       61 ekekggkvyq vfqsvarkyd lmndmmslgi hrawkdllir kmhplpgtql ldvaggtgdi
      121 afrflsyvqt qherkqrrql rtrqnlswee iarkyqsked plggslvmvc dinremlkvg
      181 kqkalarght aglawvlgda eelpfdddrf dvytiafgir nvthidralq eahrvlkpgg
      241 rflclefsqv ndplisrlyd lysfqvipvi geviagdwks yqylvesirk fpnqeefkdm
      301 iedagfqkvt yesltsgiva ihsgfkl
//
LOCUS       NP_001012345             388 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol O-acyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_001012345 XP_341888
VERSION     NP_001012345.1
DBSOURCE    REFSEQ: accession NM_001012345.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Ma,Z., Onorato,J.M., Chen,L., Nelson,D.W., Yen,C.E. and Cheng,D.
  TITLE     Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid
            acyltransferases
  JOURNAL   J Lipid Res 58 (6), 1091-1099 (2017)
   PUBMED   28420705
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Brandt,C., McFie,P.J. and Stone,S.J.
  TITLE     Biochemical characterization of human acyl coenzyme A:
            2-monoacylglycerol acyltransferase-3 (MGAT3)
  JOURNAL   Biochem Biophys Res Commun 475 (3), 264-270 (2016)
   PUBMED   27184406
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Zhang,H., Li,Y., Hu,J., Shen,W.J., Singh,M., Hou,X., Bittner,A.,
            Bittner,S., Cortez,Y., Tabassum,J., Kraemer,F.B. and Azhar,S.
  TITLE     Effect of Creosote Bush-Derived NDGA on Expression of Genes
            Involved in Lipid Metabolism in Liver of High-Fructose Fed Rats:
            Relevance to NDGA Amelioration of Hypertriglyceridemia and Hepatic
            Steatosis
  JOURNAL   PLoS One 10 (9), e0138203 (2015)
   PUBMED   26394137
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Cote,I., Chapados,N.A. and Lavoie,J.M.
  TITLE     Impaired VLDL assembly: a novel mechanism contributing to hepatic
            lipid accumulation following ovariectomy and
            high-fat/high-cholesterol diets?
  JOURNAL   Br J Nutr 112 (10), 1592-1600 (2014)
   PUBMED   25263431
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Jin,Y., McFie,P.J., Banman,S.L., Brandt,C. and Stone,S.J.
  TITLE     Diacylglycerol acyltransferase-2 (DGAT2) and monoacylglycerol
            acyltransferase-2 (MGAT2) interact to promote triacylglycerol
            synthesis
  JOURNAL   J Biol Chem 289 (41), 28237-28248 (2014)
   PUBMED   25164810
  REMARK    GeneRIF: The interaction of DGAT2 and MGAT2 serves to channel lipid
            substrates efficiently for triacylglycerol biosynthesis.
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Stone,S.J., Myers,H.M., Watkins,S.M., Brown,B.E., Feingold,K.R.,
            Elias,P.M. and Farese,R.V. Jr.
  TITLE     Lipopenia and skin barrier abnormalities in DGAT2-deficient mice
  JOURNAL   J Biol Chem 279 (12), 11767-11776 (2004)
   PUBMED   14668353
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Wakimoto,K., Chiba,H., Michibata,H., Seishima,M., Kawasaki,S.,
            Okubo,K., Mitsui,H., Torii,H. and Imai,Y.
  TITLE     A novel diacylglycerol acyltransferase (DGAT2) is decreased in
            human psoriatic skin and increased in diabetic mice
  JOURNAL   Biochem Biophys Res Commun 310 (2), 296-302 (2003)
   PUBMED   14521909
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Waterman,I.J., Price,N.T. and Zammit,V.A.
  TITLE     Distinct ontogenic patterns of overt and latent DGAT activities of
            rat liver microsomes
  JOURNAL   J Lipid Res 43 (9), 1555-1562 (2002)
   PUBMED   12235188
  REMARK    GeneRIF: ontogeny of the two functional diacylglycerol
            acyltransferase (DGAT) activities (overt and latent) during
            postnatal development in rat liver
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Yen,C.L., Stone,S.J., Cases,S., Zhou,P. and Farese,R.V. Jr.
  TITLE     Identification of a gene encoding MGAT1, a monoacylglycerol
            acyltransferase
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8512-8517 (2002)
   PUBMED   12077311
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Cases,S., Stone,S.J., Zhou,P., Yen,E., Tow,B., Lardizabal,K.D.,
            Voelker,T. and Farese,R.V. Jr.
  TITLE     Cloning of DGAT2, a second mammalian diacylglycerol
            acyltransferase, and related family members
  JOURNAL   J Biol Chem 276 (42), 38870-38876 (2001)
   PUBMED   11481335
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089846.1.
            
            On Feb 18, 2005 this sequence version replaced XP_341888.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089846.1, SRR8487231.101396.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..388
                     /product="diacylglycerol O-acyltransferase 2"
                     /EC_number="2.3.1.20"
                     /EC_number="2.3.1.76"
                     /note="diglyceride acyltransferase 2; retinol
                     O-fatty-acyltransferase; acyl-CoA retinol
                     O-fatty-acyltransferase"
                     /calculated_mol_wt=43664
     Site            70..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVP8.1)"
     Region          92..388
                     /region_name="DAGAT"
                     /note="Diacylglycerol acyltransferase; pfam03982"
                     /db_xref="CDD:112781"
     Site            93..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVP8.1)"
     Site            order(163,166,189..192,240..242)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
     CDS             1..388
                     /gene="Dgat2"
                     /gene_synonym="ARAT"
                     /coded_by="NM_001012345.1:178..1344"
                     /db_xref="GeneID:252900"
                     /db_xref="RGD:620329"
ORIGIN      
        1 mktliaaysg vlrgerraea arsenknkgs alsregsgrw gtgssilsal qdifsvtwln
       61 rskvekhlqv isvlqwvlsf lvlgvacsvi lmytfctdcw liaalyftwl afdwntpkkg
      121 grrsqwvrnw avwryfrdyf piqlvkthnl lttrnyifgy hphgimglga fcnfsteate
      181 vskkfpgirp ylatlagnfr mpvlreylms ggicpvnrdt idyllskngs gnaivivvgg
      241 aaeslssmpg knavtlrnrk gfvklalrhg adlvptysfg enevykqvif eegswgrwvq
      301 kkfqkyigfa pcifhgrglf ssdtwglvpy skpittvvge pitvpklehp tqkdidlyht
      361 mymealvklf dnhktkfglp etevlevn
//
LOCUS       NP_001014217             685 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 214 [Rattus norvegicus].
ACCESSION   NP_001014217
VERSION     NP_001014217.2
DBSOURCE    REFSEQ: accession NM_001014195.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC129115.1.
            
            On Jan 14, 2007 this sequence version replaced NP_001014217.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..685
                     /product="transmembrane protein 214"
                     /calculated_mol_wt=76435
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1L2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6NUQ4; propagated from
                     UniProtKB/Swiss-Prot (A1L1L2.1)"
     Region          8..679
                     /region_name="TMEM214"
                     /note="C-terminal, caspase 4 activator; pfam10151"
                     /db_xref="CDD:462966"
     Region          66..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1L2.1)"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A1L1L2.1)"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A1L1L2.1)"
     Site            479..499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1L2.1)"
     Site            612..632
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1L2.1)"
     CDS             1..685
                     /gene="Tmem214"
                     /gene_synonym="RGD1311324"
                     /coded_by="NM_001014195.2:52..2109"
                     /db_xref="GeneID:362711"
                     /db_xref="RGD:1311324"
ORIGIN      
        1 maaraagsgg wevvkrsrrp gassggrggg gdrralgean gvwkydlssp iqptstlyer
       61 gfekimkrqn keqvpppaae skkpvnkkqp kkvtavasqn qkqgpfrsle dalkaldvaa
      121 lqkeldksqs vftgnpsvwl kdlasylnyk lqtprmeptl sqyphdypys lvsrelrgii
      181 rglltkaags velffdhclf tmlqeldktp geslhgyric iqailqdkpk ivtsnldkfl
      241 ellrshqsrp akcltimwal gqagftnlte glkvwlgiml pvlgikslsp faiayldrll
      301 lmypnltkgf gmigpkdffp lldfaympnn slspslqeql cqlfprlkvl afgakpessl
      361 htyfpsflsr atpscpaamk kellasltqc ltvdplstsv wrqlypkhls qsslllehll
      421 tsweqipkka rkclqetiqs ftltnqellk kgsgsnehvv tcdtackgll qqargprppw
      481 arllllllvf avgflchdlr shssfqaslt grllqssgll pvaqqvcakl ysyslqsynw
      541 lqetlpacgs yllavvqpsl qlawtyiyat fsflsaycas ylaffsdsla gvlqrvqlpe
      601 alhqlfhslk ellllfyhsv llpmwhllla alaqvqehch eacrgemtwd ciktqfstaa
      661 hwtwlclqdv tvafldwalt misqq
//
LOCUS       NP_001012210             407 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM13 [Rattus norvegicus].
ACCESSION   NP_001012210 XP_344418
VERSION     NP_001012210.1
DBSOURCE    REFSEQ: accession NM_001012210.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Uchil,P.D., Hinz,A., Siegel,S., Coenen-Stass,A., Pertel,T.,
            Luban,J. and Mothes,W.
  TITLE     TRIM protein-mediated regulation of inflammatory and innate immune
            signaling and its association with antiretroviral activity
  JOURNAL   J Virol 87 (1), 257-272 (2013)
   PUBMED   23077300
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Tomar,D., Singh,R., Singh,A.K., Pandya,C.D. and Singh,R.
  TITLE     TRIM13 regulates ER stress induced autophagy and clonogenic ability
            of the cells
  JOURNAL   Biochim Biophys Acta 1823 (2), 316-326 (2012)
   PUBMED   22178386
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Joo,H.M., Kim,J.Y., Jeong,J.B., Seong,K.M., Nam,S.Y., Yang,K.H.,
            Kim,C.S., Kim,H.S., Jeong,M., An,S. and Jin,Y.W.
  TITLE     Ret finger protein 2 enhances ionizing radiation-induced apoptosis
            via degradation of AKT and MDM2
  JOURNAL   Eur J Cell Biol 90 (5), 420-431 (2011)
   PUBMED   21333377
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Lerner,M., Corcoran,M., Cepeda,D., Nielsen,M.L., Zubarev,R.,
            Ponten,F., Uhlen,M., Hober,S., Grander,D. and Sangfelt,O.
  TITLE     The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3
            ubiquitin ligase involved in ERAD
  JOURNAL   Mol Biol Cell 18 (5), 1670-1682 (2007)
   PUBMED   17314412
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088425.1.
            
            On Feb 11, 2005 this sequence version replaced XP_344418.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088425.1, CK479217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..407
                     /product="E3 ubiquitin-protein ligase TRIM13"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 13; ret finger protein 2;
                     tripartite motif-containing protein 13; putative tumor
                     suppressor RFP2; RING-type E3 ubiquitin transferase
                     TRIM13"
                     /calculated_mol_wt=46684
     Region          5..61
                     /region_name="RING-HC_TRIM13_C-V"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 13 (TRIM13) and similar proteins;
                     cd16762"
                     /db_xref="CDD:438418"
     Region          92..133
                     /region_name="Bbox2_TRIM13_C-XI"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 13 (TRIM13) and similar proteins;
                     cd19767"
                     /db_xref="CDD:380825"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V1.1)"
     CDS             1..407
                     /gene="Trim13"
                     /coded_by="NM_001012210.1:127..1350"
                     /db_xref="GeneID:364398"
                     /db_xref="RGD:1307609"
ORIGIN      
        1 melleedltc piccslfddp rvlpcshnfc kkcleglleg nvrnslwrps pfkcptcrke
       61 tsatgvnslq vnyslkgive kynkikispk mpvckehlgq plnifcvtdm qlicgvcatr
      121 gshtkhvfss iedaytqerd afeflfqsfe twrrgdalsr ldtletnkrk slqlltkdsd
      181 kvkeffeklq htldqkknei lsdfetmkla vmqtydpein klnsilqeqr mafniaeafk
      241 dvsepiiflq qmqefrekik viketplpps nlptsplmkn fdtsqwedik lvdvdklslp
      301 qdtgvltsrs pwhpclllma vvllgllvff gptvflewsp leelatwkdc lssfnsyltk
      361 sadfveqsvf yweqmtdglf vfservknvs lvalnnvaef vckykll
//
LOCUS       NP_001007266             666 aa            linear   ROD 27-APR-2025
DEFINITION  protein OS-9 precursor [Rattus norvegicus].
ACCESSION   NP_001007266 XP_343219
VERSION     NP_001007266.1
DBSOURCE    REFSEQ: accession NM_001007265.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Zhong,Y., Shen,H., Wang,Y., Yang,Y., Yang,P. and Fang,S.
  TITLE     Identification of ERAD components essential for dislocation of the
            null Hong Kong variant of alpha-1-antitrypsin (NHK)
  JOURNAL   Biochem Biophys Res Commun 458 (2), 424-428 (2015)
   PUBMED   25660456
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Iida,Y., Fujimori,T., Okawa,K., Nagata,K., Wada,I. and Hosokawa,N.
  TITLE     SEL1L protein critically determines the stability of the HRD1-SEL1L
            endoplasmic reticulum-associated degradation (ERAD) complex to
            optimize the degradation kinetics of ERAD substrates
  JOURNAL   J Biol Chem 286 (19), 16929-16939 (2011)
   PUBMED   21454652
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Hosokawa,N., Kamiya,Y., Kamiya,D., Kato,K. and Nagata,K.
  TITLE     Human OS-9, a lectin required for glycoprotein endoplasmic
            reticulum-associated degradation, recognizes mannose-trimmed
            N-glycans
  JOURNAL   J Biol Chem 284 (25), 17061-17068 (2009)
   PUBMED   19346256
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Semenza,G.L.
  TITLE     Regulation of oxygen homeostasis by hypoxia-inducible factor 1
  JOURNAL   Physiology (Bethesda) 24, 97-106 (2009)
   PUBMED   19364912
  REMARK    Review article
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Pan,K., Dai,A.G. and Hu,R.C.
  TITLE     [The cooperation of OS-9 and PHDs in hypoxia-induced pulmonary
            hypertension of rats]
  JOURNAL   Zhongguo Ying Yong Sheng Li Xue Za Zhi 25 (1), 1-6 (2009)
   PUBMED   21186601
  REMARK    GeneRIF: HIF-1alpha, procollagen-proline dioxygenases and OS-9 are
            all involved in the pathogenesis of hypoxic pulmonary hypertension
            in rats.
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Alcock,F. and Swanton,E.
  TITLE     Mammalian OS-9 is upregulated in response to endoplasmic reticulum
            stress and facilitates ubiquitination of misfolded glycoproteins
  JOURNAL   J Mol Biol 385 (4), 1032-1042 (2009)
   PUBMED   19084021
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Bernasconi,R., Pertel,T., Luban,J. and Molinari,M.
  TITLE     A dual task for the Xbp1-responsive OS-9 variants in the mammalian
            endoplasmic reticulum: inhibiting secretion of misfolded protein
            conformers and enhancing their disposal
  JOURNAL   J Biol Chem 283 (24), 16446-16454 (2008)
   PUBMED   18417469
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Christianson,J.C., Shaler,T.A., Tyler,R.E. and Kopito,R.R.
  TITLE     OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
            ubiquitin ligase complex for ERAD
  JOURNAL   Nat Cell Biol 10 (3), 272-282 (2008)
   PUBMED   18264092
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Litovchick,L., Friedmann,E. and Shaltiel,S.
  TITLE     A selective interaction between OS-9 and the carboxyl-terminal tail
            of meprin beta
  JOURNAL   J Biol Chem 277 (37), 34413-34423 (2002)
   PUBMED   12093806
  REMARK    GeneRIF: characterized alternatively spliced form and found that
            only the non-spliced form binds to meprin beta, suggesting the
            possible mechanism of the regulation of OS-9 function.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085907.1.
            
            On Nov 26, 2004 this sequence version replaced XP_343219.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..666
                     /product="protein OS-9 precursor"
                     /note="protein OS-9; osteosarcoma amplified 9, endoplasmic
                     reticulum lectin; amplified in osteosarcoma"
                     /calculated_mol_wt=72448
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5RKH6.1)"
                     /calculated_mol_wt=2936
     mat_peptide     31..666
                     /product="Protein OS-9. /id=PRO_0000386450"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKH6.1)"
                     /calculated_mol_wt=72448
     Region          110..181
                     /region_name="PRKCSH"
                     /note="Glucosidase II beta subunit-like protein;
                     pfam07915"
                     /db_xref="CDD:400321"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5RKH6.1)"
     Region          <259..643
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          261..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKH6.1)"
     Region          370..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKH6.1)"
     Region          505..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKH6.1)"
     Region          631..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKH6.1)"
     CDS             1..666
                     /gene="Os9"
                     /gene_synonym="Os-9"
                     /coded_by="NM_001007265.1:30..2030"
                     /db_xref="GeneID:362891"
                     /db_xref="RGD:1359574"
ORIGIN      
        1 maaeallssl lgllflglll pahltggvgs lnleelsemr ygiqilplpv mggqsqasdv
       61 vvvsskykqr yecrlpagai hfqrereeet payqgpgipe llspmrdapc llktkdwwty
      121 efcygrhiqq yhmedseikg dvlylgyyqs afnwddetak askqhrlkry hsqtygngsk
      181 cdlngkprea evrflcdega gisgdyidrv depfscsyvl sirtsrlcph pllrppasaa
      241 pqailchpal qpdeymaylq rqaeskqhee kvteevqdtd hqvwsgskaa gappkkedvs
      301 ptkedkesef wkmlqepeeq atgteeaqag eqdlnheaaa dpapapptdf qnnvqvklir
      361 spadlirlie elkgaekgkp svrqeqpgdd tteapqreae akgkggeprg lveeedgdee
      421 eedededeqq llgefekele gmllpsdrer lrsevkagme releniiqet ekeldpeglr
      481 kesereqail altstldkli krlqesqspe lvqkykkrrv vpqkpppsph pteeepehrv
      541 rvrvtklrhg gpnqdltvle mnrenpqlkq ieglvtevle regltaegki eikivrpgae
      601 gkeedtrwlt dedtrnlkei ffnilvqgae eankerqrqs elesnyrrvw gspggedtgd
      661 ldefdf
//
LOCUS       NP_631931                358 aa            linear   ROD 27-APR-2025
DEFINITION  acyl-CoA desaturase 1 [Rattus norvegicus].
ACCESSION   NP_631931
VERSION     NP_631931.2
DBSOURCE    REFSEQ: accession NM_139192.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Zhu,Y.L., Meng,L.L., Ma,J.H., Yuan,X., Chen,S.W., Yi,X.R., Li,X.Y.,
            Wang,Y., Tang,Y.S., Xue,M., Zhu,M.Z., Peng,J., Lu,X.J., Huang,J.Z.,
            Song,Z.C., Wu,C., Zheng,K.Z., Dai,Q.Q., Huang,F. and Fang,H.S.
  TITLE     Loss of LBP triggers lipid metabolic disorder through H3K27
            acetylation-mediated C/EBPbeta- SCD activation in non-alcoholic
            fatty liver disease
  JOURNAL   Zool Res 45 (1), 79-94 (2024)
   PUBMED   38114435
  REMARK    GeneRIF: Loss of LBP triggers lipid metabolic disorder through
            H3K27 acetylation-mediated C/EBPbeta- SCD activation in
            non-alcoholic fatty liver disease.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Zhang,Y., Gu,Y., Chen,Y., Huang,Z., Li,M., Jiang,W., Chen,J.,
            Rao,W., Luo,S., Chen,Y., Chen,J., Li,L., Jia,Y., Liu,M. and Zhou,F.
  TITLE     Dingxin Recipe IV attenuates atherosclerosis by regulating lipid
            metabolism through LXR-alpha/SREBP1 pathway and modulating the gut
            microbiota in ApoE-/- mice fed with HFD
  JOURNAL   J Ethnopharmacol 266, 113436 (2021)
   PUBMED   33011372
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Chen,M., Xu,J., Wang,Y., Wang,Z., Guo,L., Li,X. and Huang,L.
  TITLE     Arctium lappa L. polysaccharide can regulate lipid metabolism in
            type 2 diabetic rats through the SREBP-1/SCD-1 axis
  JOURNAL   Carbohydr Res 494, 108055 (2020)
   PUBMED   32535406
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Gopal Reddy,M.R., Kumar,M.S., Acharya,V., Venkata,S.M., Putcha,U.K.
            and Jeyakumar,S.M.
  TITLE     Vitamin A deficiency increases the oleic acid (C18:1) levels in the
            kidney of high fructose diet-fed rats
  JOURNAL   Indian J Med Res 150 (6), 620-629 (2019)
   PUBMED   32048626
  REMARK    GeneRIF: Feeding of VAD diet either alone or under HFr condition
            increased the kidney oleic acid (C18:1) levels and thus total MUFA,
            which corroborated with elevated SCD1 activity index, without
            affecting its expression status
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Hao,C.L., Lin,H.L., Ke,L.Y., Yen,H.W. and Shen,K.P.
  TITLE     Pre-germinated brown rice extract ameliorates high-fat diet-induced
            metabolic syndrome
  JOURNAL   J Food Biochem 43 (3), e12769 (2019)
   PUBMED   31353547
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Sundberg,J.P., Boggess,D., Sundberg,B.A., Eilertsen,K., Parimoo,S.,
            Filippi,M. and Stenn,K.
  TITLE     Asebia-2J (Scd1(ab2J)): a new allele and a model for scarring
            alopecia
  JOURNAL   Am J Pathol 156 (6), 2067-2075 (2000)
   PUBMED   10854228
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Shanklin,J., Whittle,E. and Fox,B.G.
  TITLE     Eight histidine residues are catalytically essential in a
            membrane-associated iron enzyme, stearoyl-CoA desaturase, and are
            conserved in alkane hydroxylase and xylene monooxygenase
  JOURNAL   Biochemistry 33 (43), 12787-12794 (1994)
   PUBMED   7947684
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Mihara,K.
  TITLE     Structure and regulation of rat liver microsomal stearoyl-CoA
            desaturase gene
  JOURNAL   J Biochem 108 (6), 1022-1029 (1990)
   PUBMED   1982442
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Strittmatter,P., Thiede,M.A., Hackett,C.S. and Ozols,J.
  TITLE     Bacterial synthesis of active rat stearyl-CoA desaturase lacking
            the 26-residue amino-terminal amino acid sequence
  JOURNAL   J Biol Chem 263 (5), 2532-2535 (1988)
   PUBMED   2892838
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Thiede,M.A., Ozols,J. and Strittmatter,P.
  TITLE     Construction and sequence of cDNA for rat liver stearyl coenzyme A
            desaturase
  JOURNAL   J Biol Chem 261 (28), 13230-13235 (1986)
   PUBMED   2428815
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF509569.1.
            
            On Jun 10, 2007 this sequence version replaced NP_631931.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF509568.1, AF509569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..358
                     /product="acyl-CoA desaturase 1"
                     /EC_number="1.14.19.1"
                     /note="delta(9)-desaturase 1; fatty acid desaturase 1;
                     stearoyl-CoA desaturase 1; stearoyl-Coenzyme A desaturase
                     1"
                     /calculated_mol_wt=41336
     Region          8..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Region          99..336
                     /region_name="Delta9-FADS-like"
                     /note="The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like
                     CD includes the delta-9 and delta-11 acyl CoA desaturases
                     found in various eukaryotes including vertebrates,
                     insects, higher plants, and fungi. The delta-9 acyl-lipid
                     desaturases are found in a wide...; cd03505"
                     /db_xref="CDD:239582"
     Site            order(119,124,156,159..160,297,300..301)
                     /site_type="other"
                     /note="Di-iron ligands [ion binding]"
                     /db_xref="CDD:239582"
     Region          119..124
                     /region_name="Histidine box-1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Region          156..160
                     /region_name="Histidine box-2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Site            217..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Site            241..262
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     Region          297..301
                     /region_name="Histidine box-3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P07308.2)"
     CDS             1..358
                     /gene="Scd"
                     /gene_synonym="Scd1"
                     /coded_by="NM_139192.2:49..1125"
                     /db_xref="GeneID:246074"
                     /db_xref="RGD:621176"
ORIGIN      
        1 mpahmlqeis ssytttttit eppsgnlqng rekmkkvply leedirpemr edihdpsyqd
       61 eegpppkley vwrniilmal lhvgalygit lipsskvytl lwgifyylis algitagahr
      121 lwshrtykar lplrifliia ntmafqndvy ewardhrahh kfsethadph nsrrgfffsh
      181 vgwllvrkhp avkekggkld msdlkaeklv mfqrryykpg lllmcfilpt lvpwycwget
      241 flhslfvstf lrytlvlnat wlvnsaahly gyrpydkniq srenilvslg avgegfhnyh
      301 hafpydysas eyrwhinftt ffidcmaalg laydrkkvsk aavlarikrt gdgshkss
//
LOCUS       NP_001003958             908 aa            linear   ROD 27-APR-2025
DEFINITION  DNA (cytosine-5)-methyltransferase 3A isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001003958 XP_233941
VERSION     NP_001003958.1
DBSOURCE    REFSEQ: accession NM_001003958.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Cheng,P., Wei,H.Z., Chen,H.W., Wang,Z.Q., Mao,P. and Zhang,H.H.
  TITLE     DNMT3a-mediated methylation of PPARgamma promote intervertebral
            disc degeneration by regulating the NF-kappaB pathway
  JOURNAL   J Cell Mol Med 28 (2), e18048 (2024)
   PUBMED   37986543
  REMARK    GeneRIF: DNMT3a-mediated methylation of PPARgamma promote
            intervertebral disc degeneration by regulating the NF-kappaB
            pathway.
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Gu,Y.H., Wang,J., Lu,W.C., Cheng,Y., Tao,R., Zhang,S.J., Xu,T.,
            Zhai,K.W., Luo,S.X. and Xin,W.J.
  TITLE     POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment
  JOURNAL   Neurochem Res 48 (12), 3652-3664 (2023)
   PUBMED   37592110
  REMARK    GeneRIF: POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment.
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Kuang,J., Xu,M., Xu,C., Wang,Y., Ni,C., Wei,S., Liu,Z., Kong,M.,
            Zhou,Q., Yao,M. and Ni,H.
  TITLE     miR-199a-3p mediates bone cancer pain through upregulation of
            dnmt3a expression in spinal dorsal horn neurons
  JOURNAL   Biochem Biophys Res Commun 682, 97-103 (2023)
   PUBMED   37804593
  REMARK    GeneRIF: miR-199a-3p mediates bone cancer pain through upregulation
            of dnmt3a expression in spinal dorsal horn neurons.
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Frances,R., Mata-Garrido,J., de la Fuente,R., Carcelen,M.,
            Lafarga,M., Berciano,M.T., Garcia,R., Hurle,M.A. and Tramullas,M.
  TITLE     Identification of Epigenetic Interactions between MicroRNA-30c-5p
            and DNA Methyltransferases in Neuropathic Pain
  JOURNAL   Int J Mol Sci 23 (22), 13994 (2022)
   PUBMED   36430472
  REMARK    GeneRIF: Identification of Epigenetic Interactions between
            MicroRNA-30c-5p and DNA Methyltransferases in Neuropathic Pain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Wei,J., Cheng,J., Waddell,N.J., Wang,Z.J., Pang,X., Cao,Q., Liu,A.,
            Chitaman,J.M., Abreu,K., Jasrotia,R.S., Duffney,L.J., Zhang,J.,
            Dietz,D.M., Feng,J. and Yan,Z.
  TITLE     DNA Methyltransferase 3A Is Involved in the Sustained Effects of
            Chronic Stress on Synaptic Functions and Behaviors
  JOURNAL   Cereb Cortex 31 (4), 1998-2012 (2021)
   PUBMED   33230530
  REMARK    GeneRIF: DNA Methyltransferase 3A Is Involved in the Sustained
            Effects of Chronic Stress on Synaptic Functions and Behaviors.
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Hata,K., Okano,M., Lei,H. and Li,E.
  TITLE     Dnmt3L cooperates with the Dnmt3 family of de novo DNA
            methyltransferases to establish maternal imprints in mice
  JOURNAL   Development 129 (8), 1983-1993 (2002)
   PUBMED   11934864
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Gowher,H. and Jeltsch,A.
  TITLE     Enzymatic properties of recombinant Dnmt3a DNA methyltransferase
            from mouse: the enzyme modifies DNA in a non-processive manner and
            also methylates non-CpG [correction of non-CpA] sites
  JOURNAL   J Mol Biol 309 (5), 1201-1208 (2001)
   PUBMED   11399089
  REMARK    Erratum:[J Mol Biol 2001 Jul 20;310(4):951]
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Mizuno,S., Chijiwa,T., Okamura,T., Akashi,K., Fukumaki,Y., Niho,Y.
            and Sasaki,H.
  TITLE     Expression of DNA methyltransferases DNMT1, 3A, and 3B in normal
            hematopoiesis and in acute and chronic myelogenous leukemia
  JOURNAL   Blood 97 (5), 1172-1179 (2001)
   PUBMED   11222358
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Okano,M., Bell,D.W., Haber,D.A. and Li,E.
  TITLE     DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
            methylation and mammalian development
  JOURNAL   Cell 99 (3), 247-257 (1999)
   PUBMED   10555141
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Okano,M., Xie,S. and Li,E.
  TITLE     Cloning and characterization of a family of novel mammalian DNA
            (cytosine-5) methyltransferases
  JOURNAL   Nat Genet 19 (3), 219-220 (1998)
   PUBMED   9662389
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000395.1.
            
            On Apr 19, 2005 this sequence version replaced XP_233941.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..908
                     /product="DNA (cytosine-5)-methyltransferase 3A isoform 1"
                     /EC_number="2.1.1.37"
                     /note="DNA methyltransferase 3A; DNA
                     (cytosine-5)-methyltransferase 3A; DNA
                     (cytosine-5-)-methyltransferase 3 alpha; cysteine
                     methyltransferase DNMT3A"
                     /calculated_mol_wt=101538
     Region          1..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          <1..>121
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            167
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88508; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          195..399
                     /region_name="Interaction with DNMT1 and DNMT3B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          226..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6K1; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          281..414
                     /region_name="PWWP_DNMT3A"
                     /note="PWWP domain found in DNA
                     (cytosine-5)-methyltransferase 3A (DNMT3A); cd20154"
                     /db_xref="CDD:438982"
     Site            order(297,299,302,314,326,329,331..333)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438982"
     Site            300..303
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438982"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88508; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88508; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          443..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Region          483..610
                     /region_name="ADDz_Dnmt3a"
                     /note="ADDz domain found in DNA (cytosine-5)
                     methyltransferases (C5-MTases) 3a (Dnmt3a); cd11729"
                     /db_xref="CDD:277255"
     Region          490..582
                     /region_name="Interaction with the PRC2/EED-EZH2 complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1LZ53.1)"
     Site            order(525,527,529..532,537..544,571..572,574,577)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:277255"
     Region          627..905
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Site            706
                     /site_type="methylation"
                     /note="S-methylcysteine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O88508; propagated from
                     UniProtKB/Swiss-Prot (Q1LZ53.1)"
     CDS             1..908
                     /gene="Dnmt3a"
                     /coded_by="NM_001003958.1:172..2898"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:444984"
                     /db_xref="RGD:1303336"
ORIGIN      
        1 mpssgpgdts isslereddr kegeeqeenr gkeerqepsa tarkvgrpgr krkhppvess
       61 dtpkdpavtt ksqptaqdsg psdllpngdl ekrsepqpee gspaagqkgg apaegegtet
      121 ppeasraven gccvtkegrg asagegkeqk qtniesmkme gsrgrlrggl gwesslrqrp
      181 mprltfqagd pyyiskrkrd ewlarwkrea ekkakviavm naveesqasg esqkveeasp
      241 pavqqptdpa sptvattpep vgadagdkna tkaaddepey edgrgfgige lvwgklrgfs
      301 wwpgrivsww mtgrsraaeg trwvmwfgdg kfsvvcvekl mplssfcsaf hqatynkqpm
      361 yrkaiyevlq vassragklf pachdsdesd tgkavevqnk qmiewalggf qpsgpkglep
      421 peeeknpyke vytdmwvepe aaayappppa kkprksttek pkvkeiider trerlvyevr
      481 qkcrniedic iscgslnvtl ehplfiggmc qnckncflec ayqydddgyq sycticcggr
      541 evlmcgnnnc crcfcvecvd llvgpgaaqa aikedpwncy mcghkgtygl lrrredwpsr
      601 lqmffannhd qefdppkvyp pvpaekrkpi rvlslfdgia tgllvlkdlg iqvdryiase
      661 vcedsitvgm vrhqgkimyv gdvrsvtqkh iqewgpfdlv iggspcndls ivnparkgly
      721 egtgrlffef yrllhdarpk egddrpffwl fenvvamgvs dkrdisrfle snpvmidake
      781 vsaahraryf wgnlpgmnrp lastvndkle lqeclehgri akfskvrtit trsnsikqgk
      841 dqhfpvfmne kedilwctem ervfgfpvhy tdvsnmsrla rqrllgrsws vpvirhlfap
      901 lkeyfacv
//
LOCUS       NP_001009618             127 aa            linear   ROD 27-APR-2025
DEFINITION  activated RNA polymerase II transcriptional coactivator p15 [Rattus
            norvegicus].
ACCESSION   NP_001009618 XP_342201
VERSION     NP_001009618.1
DBSOURCE    REFSEQ: accession NM_001009618.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Lopez,C.R., Singh,S., Hambarde,S., Griffin,W.C., Gao,J., Chib,S.,
            Yu,Y., Ira,G., Raney,K.D. and Kim,N.
  TITLE     Yeast Sub1 and human PC4 are G-quadruplex binding proteins that
            suppress genome instability at co-transcriptionally formed G4 DNA
  JOURNAL   Nucleic Acids Res 45 (10), 5850-5862 (2017)
   PUBMED   28369605
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Moir,R.D. and Willis,I.M.
  TITLE     Regulation of pol III transcription by nutrient and stress
            signaling pathways
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 361-375 (2013)
   PUBMED   23165150
  REMARK    Review article
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Dieci,G., Bosio,M.C., Fermi,B. and Ferrari,R.
  TITLE     Transcription reinitiation by RNA polymerase III
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 331-341 (2013)
   PUBMED   23128323
  REMARK    Review article
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Redshaw,N., Camps,C., Sharma,V., Motallebipour,M., Guzman-Ayala,M.,
            Oikonomopoulos,S., Thymiakou,E., Ragoussis,J. and Episkopou,V.
  TITLE     TGF-beta/Smad2/3 signaling directly regulates several miRNAs in
            mouse ES cells and early embryos
  JOURNAL   PLoS One 8 (1), e55186 (2013)
   PUBMED   23390484
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Jeong,Y., Leskow,F.C., El-Jaick,K., Roessler,E., Muenke,M.,
            Yocum,A., Dubourg,C., Li,X., Geng,X., Oliver,G. and Epstein,D.J.
  TITLE     Regulation of a remote Shh forebrain enhancer by the Six3
            homeoprotein
  JOURNAL   Nat Genet 40 (11), 1348-1353 (2008)
   PUBMED   18836447
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Werten,S. and Moras,D.
  TITLE     A global transcription cofactor bound to juxtaposed strands of
            unwound DNA
  JOURNAL   Nat Struct Mol Biol 13 (2), 181-182 (2006)
   PUBMED   16415882
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Shakib,K., Norman,J.T., Fine,L.G., Brown,L.R. and
            Godovac-Zimmermann,J.
  TITLE     Proteomics profiling of nuclear proteins for kidney fibroblasts
            suggests hypoxia, meiosis, and cancer may meet in the nucleus
  JOURNAL   Proteomics 5 (11), 2819-2838 (2005)
   PUBMED   15942958
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     Purification, cloning, and characterization of a human coactivator,
            PC4, that mediates transcriptional activation of class II genes
  JOURNAL   Cell 78 (3), 513-523 (1994)
   PUBMED   8062391
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Soma,G., Kitahara,N. and Andoh,T.
  TITLE     Molecular cloning and characterization of a cDNA clone for a
            protein specifically expressed in embryo as well as in a chemically
            induced pancreatic B cell tumor of rat
  JOURNAL   Biochem Biophys Res Commun 124 (1), 164-171 (1984)
   PUBMED   6208900
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088346.1.
            
            On Jan 13, 2005 this sequence version replaced XP_342201.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088346.1, EV773683.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..127
                     /product="activated RNA polymerase II transcriptional
                     coactivator p15"
                     /note="PC4; p14; positive cofactor 4; pR-ET2 encoded
                     oncodevelopmental protein; RNA polymerase II
                     transcriptional coactivator; SUB1 homolog, transcriptional
                     regulator"
                     /calculated_mol_wt=14310
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63396.3)"
     Region          1..50
                     /region_name="Regulatory. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63396.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            50..51
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11031; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Region          64..115
                     /region_name="PC4"
                     /note="Transcriptional Coactivator p15 (PC4); pfam02229"
                     /db_xref="CDD:460501"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     Region          77..101
                     /region_name="Interaction with ssDNA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63396.3)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53999; propagated from
                     UniProtKB/Swiss-Prot (Q63396.3)"
     CDS             1..127
                     /gene="Sub1"
                     /gene_synonym="Rpo2tc1"
                     /coded_by="NM_001009618.1:124..507"
                     /db_xref="GeneID:192269"
                     /db_xref="RGD:621582"
ORIGIN      
        1 mpkskelvss sssgsdsdse vekklkrkkq vvpekpvkkq kpgessrala sskqssssrd
       61 dnmfqigkmr yvsvrdfkgk ilidireywm dsegemkpgr kgislnmeqw sqlkeqisdi
      121 ddavrkl
//
LOCUS       NP_001012097             698 aa            linear   ROD 27-APR-2025
DEFINITION  ubiquitin-like modifier-activating enzyme ATG7 [Rattus norvegicus].
ACCESSION   NP_001012097 XP_232276
VERSION     NP_001012097.1
DBSOURCE    REFSEQ: accession NM_001012097.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Sun,Y., Zhao,Y., Lu,Y., Li,H., Xiang,J., Yang,D., Wang,J., Gao,X.
            and Wang,Y.
  TITLE     Urinary stem cell-derived exocrine circRNA ATG7 regulates the
            SOCS1/STAT3 signaling pathway through miR-4500, inhibits M1
            macrophage polarization, and alleviates the progression of diabetes
            nephropathy
  JOURNAL   Int Urol Nephrol 56 (4), 1449-1463 (2024)
   PUBMED   37815664
  REMARK    GeneRIF: Urinary stem cell-derived exocrine circRNA ATG7 regulates
            the SOCS1/STAT3 signaling pathway through miR-4500, inhibits M1
            macrophage polarization, and alleviates the progression of diabetes
            nephropathy.
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Liu,X., Lv,J., Tang,W., Hu,Y., Wen,Y. and Shen,H.
  TITLE     METTL3-mediated maturation of miR-192-5p targets ATG7 to prevent
            Schwann cell autophagy in peripheral nerve injury
  JOURNAL   J Neuropathol Exp Neurol 82 (12), 1010-1019 (2023)
   PUBMED   37964653
  REMARK    GeneRIF: METTL3-mediated maturation of miR-192-5p targets ATG7 to
            prevent Schwann cell autophagy in peripheral nerve injury.
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Fan,W., Rong,J., Shi,W., Liu,W., Wang,J., Tan,J., Yu,B. and Tong,J.
  TITLE     GATA6 Inhibits Neuronal Autophagy and Ferroptosis in Cerebral
            ischemia-reperfusion Injury Through a miR-193b/ATG7 axis-dependent
            Mechanism
  JOURNAL   Neurochem Res 48 (8), 2552-2567 (2023)
   PUBMED   37059928
  REMARK    GeneRIF: GATA6 Inhibits Neuronal Autophagy and Ferroptosis in
            Cerebral ischemia-reperfusion Injury Through a miR-193b/ATG7
            axis-dependent Mechanism.
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Dong,L., Sun,Q., Qiu,H., Yang,K., Xiao,B., Xia,T., Wang,A., Gao,H.
            and Zhang,S.
  TITLE     Melatonin protects against developmental PBDE-47 neurotoxicity by
            targeting the AMPK/mitophagy axis
  JOURNAL   J Pineal Res 75 (1), e12871 (2023)
   PUBMED   37042059
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Zhang,X.X., Lang,Y.F., Li,X., Li,Z., Xu,Y.Q. and Chu,H.Q.
  TITLE     The protective effect of puerarin-loaded mesoporous silicon
            nanoparticles on alcoholic hepatitis through mTOR-mediated
            autophagy pathway
  JOURNAL   Biomed Microdevices 24 (4), 37 (2022)
   PUBMED   36308627
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Fortun,J., Dunn,W.A. Jr., Joy,S., Li,J. and Notterpek,L.
  TITLE     Emerging role for autophagy in the removal of aggresomes in Schwann
            cells
  JOURNAL   J Neurosci 23 (33), 10672-10680 (2003)
   PUBMED   14627652
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Nemoto,T., Tanida,I., Tanida-Miyake,E., Minematsu-Ikeguchi,N.,
            Yokota,M., Ohsumi,M., Ueno,T. and Kominami,E.
  TITLE     The mouse APG10 homologue, an E2-like enzyme for Apg12p
            conjugation, facilitates MAP-LC3 modification
  JOURNAL   J Biol Chem 278 (41), 39517-39526 (2003)
   PUBMED   12890687
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Mizushima,N., Yoshimori,T. and Ohsumi,Y.
  TITLE     Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the
            conjugation-mediated yeast two-hybrid method
  JOURNAL   FEBS Lett 532 (3), 450-454 (2002)
   PUBMED   12482611
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Nishitani,T., Komatsu,M., Yamazaki,H.,
            Ueno,T. and Kominami,E.
  TITLE     Murine Apg12p has a substrate preference for murine Apg7p over
            three Apg8p homologs
  JOURNAL   Biochem Biophys Res Commun 292 (1), 256-262 (2002)
   PUBMED   11890701
REFERENCE   10 (residues 1 to 698)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Ueno,T. and Kominami,E.
  TITLE     The human homolog of Saccharomyces cerevisiae Apg7p is a
            Protein-activating enzyme for multiple substrates including human
            Apg12p, GATE-16, GABARAP, and MAP-LC3
  JOURNAL   J Biol Chem 276 (3), 1701-1706 (2001)
   PUBMED   11096062
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082059.1.
            
            On Feb 11, 2005 this sequence version replaced XP_232276.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082059.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132264, SAMD00132272
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..698
                     /product="ubiquitin-like modifier-activating enzyme ATG7"
                     /note="autophagy-related protein 7; ubiquitin-activating
                     enzyme E1-like protein; ATG7 autophagy related 7 homolog;
                     ATG12-activating enzyme E1 ATG7; autophagy 7-like"
                     /calculated_mol_wt=77305
     Region          11..697
                     /region_name="E1_like_apg7"
                     /note="E1-like protein-activating enzyme Gsa7p/Apg7p;
                     TIGR01381"
                     /db_xref="CDD:273590"
     Region          11..13
                     /region_name="FAP motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y5.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95352; propagated from
                     UniProtKB/Swiss-Prot (Q641Y5.1)"
     CDS             1..698
                     /gene="Atg7"
                     /gene_synonym="Apg7l"
                     /coded_by="NM_001012097.1:16..2112"
                     /db_xref="GeneID:312647"
                     /db_xref="RGD:1304817"
ORIGIN      
        1 mgdpglsklq fapfnsaldv gfwheltqkk lneyrldeap kdikgyyyng dsaglptrlt
       61 lefsafdmsa ptparccpam gtlhntntle afktadkkll leqsaneiwe aiksgaalen
      121 pmllnkflll tfadlkkyhf yywfccpalc lpesiplirg pvgldqrlsp kqiqalehay
      181 ddlcrtegvt alpyflfkyd ddtvlvsllk hysdffqgqr tkltvgvydp cnltqhpgwp
      241 lrnflvlaah rwsgsfqsve vlcfrdrtmq gardvthsii fevklpemaf spdcpkavgw
      301 eknqkggmgp rmvnlsgcmd pkrlaessvd lnlklmcwrl vptldldkvv svkclllgag
      361 tlgcnvartl mgwgvrhvtf vdnakisysn pvrqplyefe dclgggkpka laaaerlqki
      421 fpgvnasgfn msipmpghpv nfsdvtmeqa rrdveqleel idshdvifll mdtresrwlp
      481 tviaaskrkl vinaalgfdt fvvmrhglkk pkqqgagdlc pshlvapadl gsslfanipg
      541 yklgcyfcnd vvapgdstrd rtldqqctvs rpglaviaga lavelmvsvl qhpeggyaia
      601 sssddrmnep ptslglvphq irgflsrfdn vlpvslafdk ctacsskvld qyeqegftfl
      661 akvfnsshsf ledltgltll hqetqaaeiw dmsdeetv
//
LOCUS       NP_596883                371 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase 17B [Rattus norvegicus].
ACCESSION   NP_596883
VERSION     NP_596883.1
DBSOURCE    REFSEQ: accession NM_133392.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kuwahara,H., Nishizaki,M. and Kanazawa,H.
  TITLE     Nuclear localization signal and phosphorylation of Serine350
            specify intracellular localization of DRAK2
  JOURNAL   J Biochem 143 (3), 349-358 (2008)
   PUBMED   18084041
  REMARK    GeneRIF: These results suggest that phosphorylation of Ser350 plays
            an essential role in regulating translocation of DRAK2 to the
            nucleus from the cytoplasm, possibly by affecting the activity of
            the nuclear localization signal.
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Kuwahara,H., Kamei,J., Nakamura,N., Matsumoto,M., Inoue,H. and
            Kanazawa,H.
  TITLE     The apoptosis-inducing protein kinase DRAK2 is inhibited in a
            calcium-dependent manner by the calcium-binding protein CHP
  JOURNAL   J Biochem 134 (2), 245-250 (2003)
   PUBMED   12966074
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Matsumoto,M., Miyake,Y., Nagita,M., Inoue,H., Shitakubo,D.,
            Takemoto,K., Ohtsuka,C., Murakami,H., Nakamura,N. and Kanazawa,H.
  TITLE     A serine/threonine kinase which causes apoptosis-like cell death
            interacts with a calcineurin B-like protein capable of binding
            Na(+)/H(+) exchanger
  JOURNAL   J Biochem 130 (2), 217-225 (2001)
   PUBMED   11481038
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Sanjo,H., Kawai,T. and Akira,S.
  TITLE     DRAKs, novel serine/threonine kinases related to death-associated
            protein kinase that trigger apoptosis
  JOURNAL   J Biol Chem 273 (44), 29066-29071 (1998)
   PUBMED   9786912
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Praloran,V. and Bartocci,A.
  TITLE     CFU-C in Agar
  JOURNAL   Methods Mol Biol 5, 323-330 (1990)
   PUBMED   21374135
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB070349.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB070349.1, SRR8487227.145907.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..371
                     /product="serine/threonine-protein kinase 17B"
                     /EC_number="2.7.11.1"
                     /note="DAP kinase-related apoptosis-inducing protein
                     kinase 2; serine/threonine kinase 17b
                     (apoptosis-inducing); death-associated protein
                     kinase-related 2"
                     /calculated_mol_wt=42002
     Region          24..293
                     /region_name="STKc_DRAK2"
                     /note="The catalytic domain of the Serine/Threonine
                     Kinase, Death-associated protein kinase-Related
                     Apoptosis-inducing protein Kinase 2; cd14198"
                     /db_xref="CDD:271100"
     Site            order(39..43,45,47,60,62,94,110..111,113,117,119,158,160,
                     162..163,165,178..179,182,197..200)
                     /site_type="active"
                     /db_xref="CDD:271100"
     Site            order(39..43,45,47,60,62,94,110..111,113,117,162..163,165,
                     178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271100"
     Site            order(43,117,119,158,160,162,182,197..200)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271100"
     Site            178..200
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271100"
     Region          308..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XS8.1)"
     CDS             1..371
                     /gene="Stk17b"
                     /gene_synonym="Drak2"
                     /coded_by="NM_133392.1:168..1283"
                     /db_xref="GeneID:170904"
                     /db_xref="RGD:620457"
ORIGIN      
        1 msrrrfdcrs isglltttpq tpmktenfnn fytltpkelg rgkfavvrqc iskstgqeya
       61 akflkkrrrg qdcraeilhe iavlelarsc phvinlhevy etateiilvl eyaaggeifn
      121 lclpelaemv sendvirlik qilegvhylh qnnivhldlk pqnillssiy plgdikivdf
      181 gmsrkignas elreimgtpe ylapeilnyd pittatdmwn igiiaymllt htspfvgedn
      241 qetylnisqv nvdyseemfs svsqlatdfi qsllvknpek rptaesclsh swlqqwdfgs
      301 lfhpeetses sqtqdlslrs sedktpkscn gscgdredke nipeddslls krfrfddslp
      361 sphelvpdlf c
//
LOCUS       NP_001101192             825 aa            linear   ROD 27-APR-2025
DEFINITION  breast cancer anti-estrogen resistance protein 3 homolog [Rattus
            norvegicus].
ACCESSION   NP_001101192 XP_001074184 XP_227657
VERSION     NP_001101192.1
DBSOURCE    REFSEQ: accession NM_001107722.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Oh,M.J., Yi,S.J., Kim,H.S., Kim,J.H., Jeong,Y.H., van Agthoven,T.
            and Jhun,B.H.
  TITLE     Functional roles of BCAR3 in the signaling pathways of insulin
            leading to DNA synthesis, membrane ruffling and GLUT4 translocation
  JOURNAL   Biochem Biophys Res Commun 441 (4), 911-916 (2013)
   PUBMED   24216110
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Sun,G., Cheng,S.Y., Chen,M., Lim,C.J. and Pallen,C.J.
  TITLE     Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3
            to position Cas for activation at integrin-mediated focal adhesions
  JOURNAL   Mol Cell Biol 32 (18), 3776-3789 (2012)
   PUBMED   22801373
  REMARK    GeneRIF: study described a molecular complex of
            PTPalpha-BCAR3-Cas-Src; this complex forms in response to PTPalpha
            Tyr789 phosphorylation and mediates Cas localization to focal
            adhesions and Cas downstream signaling to promote cell migration
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Rufanova,V.A., Alexanian,A., Wakatsuki,T., Lerner,A. and Sorokin,A.
  TITLE     Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and
            regulates human glomerular mesangial cell adhesion and spreading
  JOURNAL   J Cell Physiol 219 (1), 45-56 (2009)
   PUBMED   19086031
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Near,R.I., Smith,R.S., Toselli,P.A., Freddo,T.F., Bloom,A.B.,
            Vanden Borre,P., Seldin,D.C. and Lerner,A.
  TITLE     Loss of AND-34/BCAR3 expression in mice results in rupture of the
            adult lens
  JOURNAL   Mol Vis 15, 685-699 (2009)
   PUBMED   19365570
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Oh,M.J., van Agthoven,T., Choi,J.E., Jeong,Y.J., Chung,Y.H.,
            Kim,C.M. and Jhun,B.H.
  TITLE     BCAR3 regulates EGF-induced DNA synthesis in normal human breast
            MCF-12A cells
  JOURNAL   Biochem Biophys Res Commun 375 (3), 430-434 (2008)
   PUBMED   18722344
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473952.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001074184.1, XP_227657.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760384 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..825
                     /product="breast cancer anti-estrogen resistance protein 3
                     homolog"
                     /note="breast cancer anti-estrogen resistance 3; BCAR3,
                     NSP family adaptor protein 3; novel SH2-containing protein
                     2; p130Cas-binding protein AND-34; SH2 domain-containing
                     protein 3B; BCAR3 adapter protein, NSP family member"
                     /calculated_mol_wt=92347
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Region          40..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Region          148..282
                     /region_name="SH2_BCAR3"
                     /note="Src homology 2 (SH2) domain in the Breast Cancer
                     Anti-estrogen Resistance protein 3; cd10337"
                     /db_xref="CDD:198200"
     Site            order(161,177,198,200)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198200"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            order(199,234)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198200"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Region          300..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            334
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK2; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            442
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O75815; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK2; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Region          544..819
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases. Small GTP-binding proteins of the Ras
                     superfamily function as molecular switches in fundamental
                     events such as signal transduction, cytoskeleton dynamics
                     and intracellular trafficking; cl02485"
                     /db_xref="CDD:470590"
     Site            order(579..581,595..596,598..600,602..603,606..607,610,
                     645,648..649,651..653,655..658,660..661,678,683..685,688,
                     709..711,714..716,718..720,722..725,739,743,784,787..788)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          744..748
                     /region_name="Mediates the interaction with BCAR1/p130CAS.
                     /evidence=ECO:0000250|UniProtKB:O75815"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     Site            748
                     /site_type="other"
                     /note="Required for interaction with NEDD9.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK2; propagated from
                     UniProtKB/Swiss-Prot (D3ZAZ5.1)"
     CDS             1..825
                     /gene="Bcar3"
                     /coded_by="NM_001107722.1:425..2902"
                     /db_xref="GeneID:310838"
                     /db_xref="RGD:1311688"
ORIGIN      
        1 maagkfaslp rhmpvnhqfp lassmdllss ksplaehrte aypdvsihgt lprkkkgppp
       61 irscdsashm gtlphskspr qsspltqdli lekplpdwkg dsfafrdpyl ldptleyvkf
      121 skerhimdrt perlkkelee elllssedlr shawyhgrip rqvsenlvqr dgdflvrdsl
      181 sspgnfvltc qwknlaqhfk inrtvlrlse aysrvqyqfe mesfdsipgl vrcyvgnrrp
      241 isqqsgaiif qpinrtvplw cleerygtsp grgregsfae grpdvvkrls lttggiqard
      301 hslprgnllr nkdksgsqpa cldhvqdrka atlkahqses hlpigcklpp qspsvdtspc
      361 pnspvfrtgs eptlspalvr rfssdarage alrgsdsqlc pkpppkpckv pflkvppsps
      421 pwlnseanyc elnpafavgc drgakllsqa ldshemllta kqngasgprn sginysildg
      481 ddqgrhwdpl avqtdegqed etkfvppvme tvssfrpndf eskllppenk pletamlkha
      541 kelftnhdar viaqhmlsvd ckvarilevs edmkrsmgvs sglelitlph grqlrldiie
      601 rhntmaigia vdilgctgtl enragtlnki iqvamelkdt mgdlysfsai mkalempqit
      661 rlektwtalr hhytqtaily ekqlkpfski lhegrestyv passvsvpll mplvtlmerq
      721 avtfegtdmw ekndesceim lshlatarfm aeasesyrmn aervladfqp deemteilkt
      781 efqmrllwgs kgaevnqner ydkfnqilta lsrkleppsg kqael
//
LOCUS       NP_776209                193 aa            linear   ROD 27-APR-2025
DEFINITION  bcl-2-binding component 3 [Rattus norvegicus].
ACCESSION   NP_776209
VERSION     NP_776209.1
DBSOURCE    REFSEQ: accession NM_173837.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Das,A.K. and Biswas,S.C.
  TITLE     Cdc25A phosphatase is activated and mediates neuronal cell death by
            PUMA via pRb/E2F1 pathway in a model of Parkinson's disease
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119848 (2024)
   PUBMED   39305937
  REMARK    GeneRIF: Cdc25A phosphatase is activated and mediates neuronal cell
            death by PUMA via pRb/E2F1 pathway in a model of Parkinson's
            disease.
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Guo,J., Li,Z.D., Xiao,C.S. and Bian,Y.F.
  TITLE     [Effects of PUMA knockout on the apoptosis of H9C2 cardiomyocytes
            induced by high glucose]
  JOURNAL   Zhongguo Ying Yong Sheng Li Xue Za Zhi 38 (5), 504-509 (2022)
   PUBMED   37088760
  REMARK    GeneRIF: [Effects of PUMA knockout on the apoptosis of H9C2
            cardiomyocytes induced by high glucose].
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Zhou,X.B., Lai,L.F., Xie,G.B., Ding,C., Xu,X. and Wang,Y.
  TITLE     LncRNAGAS5 sponges miRNA-221 to promote neurons apoptosis by
            up-regulated PUMA under hypoxia condition
  JOURNAL   Neurol Res 42 (1), 8-16 (2020)
   PUBMED   31878844
  REMARK    GeneRIF: LncRNAGAS5 sponges miRNA-221 to promote neurons apoptosis
            by up-regulated PUMA under hypoxia condition.
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Shi,S.Y., Luk,C.T., Schroer,S.A., Kim,M.J., Dodington,D.W.,
            Sivasubramaniyam,T., Lin,L., Cai,E.P., Lu,S.Y., Wagner,K.U.,
            Bazinet,R.P. and Woo,M.
  TITLE     Janus Kinase 2 (JAK2) Dissociates Hepatosteatosis from
            Hepatocellular Carcinoma in Mice
  JOURNAL   J Biol Chem 292 (9), 3789-3799 (2017)
   PUBMED   28100771
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Omori,K., Kobayashi,E., Komatsu,H., Rawson,J., Agrawal,G.,
            Parimi,M., Oancea,A.R., Valiente,L., Ferreri,K., Al-Abdullah,I.H.,
            Kandeel,F., Takahashi,M. and Mullen,Y.
  TITLE     Involvement of a proapoptotic gene (BBC3) in islet injury mediated
            by cold preservation and rewarming
  JOURNAL   Am J Physiol Endocrinol Metab 310 (11), E1016-E1026 (2016)
   PUBMED   27117005
  REMARK    GeneRIF: These results demonstrated the involvement of BBC3/Bbc3 in
            cold preservation/rewarming-mediated islet injury, possibly through
            modulating HMGB1- and oxidative stress-mediated injury to islets.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Villunger,A., Michalak,E.M., Coultas,L., Mullauer,F., Bock,G.,
            Ausserlechner,M.J., Adams,J.M. and Strasser,A.
  TITLE     p53- and drug-induced apoptotic responses mediated by BH3-only
            proteins puma and noxa
  JOURNAL   Science 302 (5647), 1036-1038 (2003)
   PUBMED   14500851
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Reimertz,C., Kogel,D., Rami,A., Chittenden,T. and Prehn,J.H.
  TITLE     Gene expression during ER stress-induced apoptosis in neurons:
            induction of the BH3-only protein Bbc3/PUMA and activation of the
            mitochondrial apoptosis pathway
  JOURNAL   J Cell Biol 162 (4), 587-597 (2003)
   PUBMED   12913114
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Itoh,T., Itoh,A. and Pleasure,D.
  TITLE     Bcl-2-related protein family gene expression during
            oligodendroglial differentiation
  JOURNAL   J Neurochem 85 (6), 1500-1512 (2003)
   PUBMED   12787069
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Nakano,K. and Vousden,K.H.
  TITLE     PUMA, a novel proapoptotic gene, is induced by p53
  JOURNAL   Mol Cell 7 (3), 683-694 (2001)
   PUBMED   11463392
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Yu,J., Zhang,L., Hwang,P.M., Kinzler,K.W. and Vogelstein,B.
  TITLE     PUMA induces the rapid apoptosis of colorectal cancer cells
  JOURNAL   Mol Cell 7 (3), 673-682 (2001)
   PUBMED   11463391
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY157758.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY157758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..193
                     /product="bcl-2-binding component 3"
                     /note="p53 up-regulated modulator of apoptosis"
                     /calculated_mol_wt=20587
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG6.1)"
     Region          2..193
                     /region_name="PUMA"
                     /note="Bcl-2-binding component 3, p53 upregulated
                     modulator of apoptosis; pfam15826"
                     /db_xref="CDD:374148"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BXH1; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG6.1)"
     Region          71..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG6.1)"
     Region          137..151
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG6.1)"
     CDS             1..193
                     /gene="Bbc3"
                     /gene_synonym="Puma"
                     /coded_by="NM_173837.2:279..860"
                     /db_xref="GeneID:317673"
                     /db_xref="RGD:631434"
ORIGIN      
        1 mararqegss pepveglard sprpfplgrl mpsavscglc epglpaapaa pallpaaylc
       61 aptappavta alggprwpgg hrsrprgprp dgpqpslspa qqhlespvps apealaggpt
      121 qaapgvrvee eewareigaq lrrmaddlna qyerrrqeeq hrhrpspwrv mynlfmgllp
      181 lprdpgapem epn
//
LOCUS       NP_001013144             305 aa            linear   ROD 27-APR-2025
DEFINITION  NADH-cytochrome b5 reductase 1 [Rattus norvegicus].
ACCESSION   NP_001013144 XP_222644
VERSION     NP_001013144.1
DBSOURCE    REFSEQ: accession NM_001013126.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Samhan-Arias,A.K., Marques-da-Silva,D., Yanamala,N. and
            Gutierrez-Merino,C.
  TITLE     Stimulation and clustering of cytochrome b5 reductase in
            caveolin-rich lipid microdomains is an early event in oxidative
            stress-mediated apoptosis of cerebellar granule neurons
  JOURNAL   J Proteomics 75 (10), 2934-2949 (2012)
   PUBMED   22200675
  REMARK    GeneRIF: Stimulation and clustering of cytochrome b5 reductase in
            caveolin-rich lipid microdomains is an early event in oxidative
            stress-mediated apoptosis.
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089945.1.
            
            On Apr 20, 2005 this sequence version replaced XP_222644.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089945.1, SRR8487227.28346.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..305
                     /product="NADH-cytochrome b5 reductase 1"
                     /EC_number="1.6.2.2"
                     /note="b5R.1; NAD(P)H:quinone oxidoreductase type 3,
                     polypeptide A2"
                     /calculated_mol_wt=34092
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB81.1)"
     Region          <42..300
                     /region_name="PLN02252"
                     /note="nitrate reductase [NADPH]"
                     /db_xref="CDD:215141"
     CDS             1..305
                     /gene="Cyb5r1"
                     /gene_synonym="Nqo3a2"
                     /coded_by="NM_001013126.1:45..962"
                     /db_xref="GeneID:304805"
                     /db_xref="RGD:1306084"
ORIGIN      
        1 mgiqpspvll aslgvglftl fglalgtylv rrsrrpqvtl qdpdekyllr lldkttvshn
       61 trrfrfalpt ahhilglpvg khvylsarid gsqvirpytp vtsdedqgyv dlvikvylkg
      121 vhpkfseggk msqyldslki gdvvefrgps gllsyagkgn fniqpnkksp pelrvakklg
      181 miaggtgitp mlqlirailk vpedptqcfl lfanqtekdi ilredleelq aqypirfklw
      241 ftldyppedw tyskgfvtad miqehlpapa edvllllcgp ppmvqlachp nldklgysqk
      301 mrfty
//
LOCUS       NP_001029200             998 aa            linear   ROD 27-APR-2025
DEFINITION  hypoxia up-regulated protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001029200
VERSION     NP_001029200.1
DBSOURCE    REFSEQ: accession NM_001034028.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Abu El-Asrar,A.M., Ahmad,A., Alam,K., Bittoun,E., Siddiquei,M.M.,
            Mohammad,G., Mousa,A., De Hertogh,G. and Opdenakker,G.
  TITLE     Association of 150-kDa oxygen-regulated protein with vascular
            endothelial growth factor in proliferative diabetic retinopathy
  JOURNAL   Acta Ophthalmol 96 (4), e460-e467 (2018)
   PUBMED   29098793
  REMARK    GeneRIF: 150-kDa oxygen-regulated protein (ORP150) levels were
            significantly increased in rat retinas after induction of diabetes.
            Vascular endothelial growth factor (VEGF) and the pro-inflammatory
            cytokines interleukin-6 (IL-6) and tumour necrosis factor-alpha
            (TNF-alpha) induced upregulation of ORP150 in HRMEC.
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cunningham,C.N., He,K., Arunagiri,A., Paton,A.W., Paton,J.C.,
            Arvan,P. and Tsai,B.
  TITLE     Chaperone-Driven Degradation of a Misfolded Proinsulin Mutant in
            Parallel With Restoration of Wild-Type Insulin Secretion
  JOURNAL   Diabetes 66 (3), 741-753 (2017)
   PUBMED   28028074
  REMARK    GeneRIF: Data reveal that Grp170 participates in preparing mutant
            proinsulin for degradation while enabling wild-type proinsulin
            escape from the endoplasmic reticulum.
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,H., Wang,F., Wang,X., Yang,J., Li,Z., Cong,X. and Chen,X.
  TITLE     Lysophosphatidic acid promotes secretion of VEGF by increasing
            expression of 150-kD Oxygen-regulated protein (ORP150) in
            mesenchymal stem cells
  JOURNAL   Biochim Biophys Acta 1831 (8), 1426-1434 (2013)
   PUBMED   23707263
  REMARK    GeneRIF: LPA promotes VEGF secretion at the post-translation level
            by up-regulating ORP150 expression.
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Jansen,G., Maattanen,P., Denisov,A.Y., Scarffe,L., Schade,B.,
            Balghi,H., Dejgaard,K., Chen,L.Y., Muller,W.J., Gehring,K. and
            Thomas,D.Y.
  TITLE     An interaction map of endoplasmic reticulum chaperones and foldases
  JOURNAL   Mol Cell Proteomics 11 (9), 710-723 (2012)
   PUBMED   22665516
REFERENCE   5  (residues 1 to 998)
  AUTHORS   Deng,W.H., Chen,C., Wang,W.X., Yu,J., Li,J.Y. and Liu,L.
  TITLE     Effects of ORP150 on appearance and function of pancreatic beta
            cells following acute necrotizing pancreatitis
  JOURNAL   Pathol Res Pract 207 (6), 370-376 (2011)
   PUBMED   21536389
  REMARK    GeneRIF: Results imply a probable role of ORP150 in the changes in
            appearance and function of pancreatic beta cells following acute
            necrotizing pancreatitis, through the pathway of endoplasmic
            reticulum stress.
REFERENCE   6  (residues 1 to 998)
  AUTHORS   Bando,Y., Ogawa,S., Yamauchi,A., Kuwabara,K., Ozawa,K., Hori,O.,
            Yanagi,H., Tamatani,M. and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) functions as a novel
            molecular chaperone in MDCK cells
  JOURNAL   Am J Physiol Cell Physiol 278 (6), C1172-C1182 (2000)
   PUBMED   10837345
REFERENCE   7  (residues 1 to 998)
  AUTHORS   Ozawa,K., Kuwabara,K., Tamatani,M., Takatsuji,K., Tsukamoto,Y.,
            Kaneda,S., Yanagi,H., Stern,D.M., Eguchi,Y., Tsujimoto,Y., Ogawa,S.
            and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) suppresses
            hypoxia-induced apoptotic cell death
  JOURNAL   J Biol Chem 274 (10), 6397-6404 (1999)
   PUBMED   10037731
REFERENCE   8  (residues 1 to 998)
  AUTHORS   Matsushita,K., Matsuyama,T., Nishimura,H., Takaoka,T., Kuwabara,K.,
            Tsukamoto,Y., Sugita,M. and Ogawa,S.
  TITLE     Marked, sustained expression of a novel 150-kDa oxygen-regulated
            stress protein, in severely ischemic mouse neurons
  JOURNAL   Brain Res Mol Brain Res 60 (1), 98-106 (1998)
   PUBMED   9748521
REFERENCE   9  (residues 1 to 998)
  AUTHORS   Ikeda,J., Kaneda,S., Kuwabara,K., Ogawa,S., Kobayashi,T.,
            Matsumoto,M., Yura,T. and Yanagi,H.
  TITLE     Cloning and expression of cDNA encoding the human 150 kDa
            oxygen-regulated protein, ORP150
  JOURNAL   Biochem Biophys Res Commun 230 (1), 94-99 (1997)
   PUBMED   9020069
REFERENCE   10 (residues 1 to 998)
  AUTHORS   Kuwabara,K., Matsumoto,M., Ikeda,J., Hori,O., Ogawa,S., Maeda,Y.,
            Kitagawa,K., Imuta,N., Kinoshita,T., Stern,D.M., Yanagi,H. and
            Kamada,T.
  TITLE     Purification and characterization of a novel stress protein, the
            150-kDa oxygen-regulated protein (ORP150), from cultured rat
            astrocytes and its expression in ischemic mouse brain
  JOURNAL   J Biol Chem 271 (9), 5025-5032 (1996)
   PUBMED   8617779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB691248.1 and BC065310.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC065310.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..998
                     /product="hypoxia up-regulated protein 1 precursor"
                     /note="hypoxia up-regulated protein 1; 150 kDa
                     oxygen-regulated protein; ORP-150; oxygen regulated
                     protein (150kD)"
                     /calculated_mol_wt=107645
     sig_peptide     1..32
                     /note="/evidence=ECO:0000269|PubMed:8617779,
                     ECO:0000269|PubMed:9020069; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
                     /calculated_mol_wt=3593
     Region          34..424
                     /region_name="ASKHA_NBD_HSP70_HYOU1"
                     /note="nucleotide-binding domain (NBD) of hypoxia
                     up-regulated protein 1 (HYOU1) and similar proteins;
                     cd10230"
                     /db_xref="CDD:466828"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          564..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63617.1)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4L1; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          <586..>691
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          <592..>800
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            830
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            862
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            869
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            883
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKR6; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            922
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            931
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          995..998
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63617.1)"
     CDS             1..998
                     /gene="Hyou1"
                     /gene_synonym="Cab140; Orp150"
                     /coded_by="NM_001034028.1:51..3047"
                     /db_xref="GeneID:192235"
                     /db_xref="RGD:621146"
ORIGIN      
        1 maatvrrqrp rrllcwalva vlladllals dtlavmsvdl gsesmkvaiv kpgvpmeivl
       61 nkesrrktpv tvtlkenerf lgdsaagmai knpkatlryf qhllgkqadn phvalyrsrf
      121 pehelnvdpq rqtvrfqisp qlqfspeevl gmvlnysrsl aedfaeqpik davitvpaff
      181 nqaerravlq aarmaglkvl qlindntata lsygvfrrkd instaqnimf ydmgsgstvc
      241 tivtyqtvkt keagtqpqlq irgvgfdrtl gglemelrlr ehlaklfneq rkgqkakdvr
      301 enpramakll reanrlktvl sanadhmaqi eglmddvdfk akvtrvefee lcadlfdrvp
      361 gpvqqalqsa emsldqieqv ilvggatrvp kvqevllkav gkeelgknin adeaaamgav
      421 yqaaalskaf kvkpfvvrda viypilveft reveeepglr slkhnkrvlf srmgpypqrk
      481 vitfnryshd fnfhinygdl gflgpedlrv fgsqnlttvk lkgvgesfkk ypdyeskgik
      541 ahfnldesgv lsldrvesvf etlvedspee estltklgnt isslfgggts sdakengtda
      601 vqeeeespae gskdepaeqg elkeeaeapm edtsqpppse pkgdaarege tpdekesgdk
      661 seaqkpnekg qagpegvppa peeekkqkpa rkqkmveeig velavldlpd lpedelahsv
      721 qkledltlrd lekqerekaa nsleafifet qdklyqpeyq evsteeqree isgklsatst
      781 wledegfgat tvmlkdklae lrklcqglff rveerrkwpe rlsaldnlln hssiflkgar
      841 lipemdqift dvemttlekv indtwtwkna tlaeqaklpa tekpvllskd ieakmmaldr
      901 evqyllnkak ftkprprpkd kngtrteppl nasagdqeek vipptgqtee akpilepdke
      961 tgtepadsep lelggpgaes eqaeqtagqk rplkndel
//
LOCUS       NP_001028843             170 aa            linear   ROD 27-APR-2025
DEFINITION  bcl-2-like protein 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001028843
VERSION     NP_001028843.1
DBSOURCE    REFSEQ: accession NM_001033671.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Perez-Serna,A.A., Dos Santos,R.S., Ripoll,C., Nadal,A.,
            Eizirik,D.L. and Marroqui,L.
  TITLE     BCL-XL Overexpression Protects Pancreatic beta-Cells against
            Cytokine- and Palmitate-Induced Apoptosis
  JOURNAL   Int J Mol Sci 24 (6), 5657 (2023)
   PUBMED   36982731
  REMARK    GeneRIF: BCL-XL Overexpression Protects Pancreatic beta-Cells
            against Cytokine- and Palmitate-Induced Apoptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Alam,M. and Mishra,R.
  TITLE     Bcl-xL expression and regulation in the progression, recurrence,
            and cisplatin resistance of oral cancer
  JOURNAL   Life Sci 280, 119705 (2021)
   PUBMED   34111459
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Rozier,R., Paul,R., Madji Hounoum,B., Villa,E., Mhaidly,R.,
            Chiche,J., Verhoeyen,E., Marchetti,S., Vandenberghe,A.,
            Raucoules,M., Carles,M. and Ricci,J.E.
  TITLE     Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism
  JOURNAL   FEBS J 288 (11), 3547-3569 (2021)
   PUBMED   33340237
  REMARK    GeneRIF: Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism.
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Liang,J.R. and Yang,H.
  TITLE     Ginkgolic acid (GA) suppresses gastric cancer growth by inducing
            apoptosis and suppressing STAT3/JAK2 signaling regulated by ROS
  JOURNAL   Biomed Pharmacother 125, 109585 (2020)
   PUBMED   32106377
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Sadek,K., Abouzed,T., Nasr,S. and Shoukry,M.
  TITLE     Licochalcone B Ameliorates Liver Cancer via Targeting of Apoptotic
            Genes, DNA Repair Systems, and Cell Cycle Control
  JOURNAL   Iran J Pharm Res 19 (4), 372-386 (2020)
   PUBMED   33841550
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Chao,D.T., Linette,G.P., Boise,L.H., White,L.S., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bcl-XL and Bcl-2 repress a common pathway of cell death
  JOURNAL   J Exp Med 182 (3), 821-828 (1995)
   PUBMED   7650488
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Gonzalez-Garcia,M., Garcia,I., Ding,L., O'Shea,S., Boise,L.H.,
            Thompson,C.B. and Nunez,G.
  TITLE     bcl-x is expressed in embryonic and postnatal neural tissues and
            functions to prevent neuronal cell death
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4304-4308 (1995)
   PUBMED   7753802
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Tilly,J.L., Tilly,K.I., Kenton,M.L. and Johnson,A.L.
  TITLE     Expression of members of the bcl-2 gene family in the immature rat
            ovary: equine chorionic gonadotropin-mediated inhibition of
            granulosa cell apoptosis is associated with decreased bax and
            constitutive bcl-2 and bcl-xlong messenger ribonucleic acid levels
  JOURNAL   Endocrinology 136 (1), 232-241 (1995)
   PUBMED   7828536
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Gonzalez-Garcia,M., Perez-Ballestero,R., Ding,L., Duan,L.,
            Boise,L.H., Thompson,C.B. and Nunez,G.
  TITLE     bcl-XL is the major bcl-x mRNA form expressed during murine
            development and its product localizes to mitochondria
  JOURNAL   Development 120 (10), 3033-3042 (1994)
   PUBMED   7607090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U72349.1, AF279286.1 and BC094213.1.
            
            Transcript Variant: This variant (4) differs in the 3' UTR and 3'
            coding sequence compared to variant 1. The resulting isoform (3)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF136230.1, AF279286.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..170
                     /product="bcl-2-like protein 1 isoform 3"
                     /note="bcl-2-like protein 1; B cell lymphoma like X;
                     bcl2-L-1; apoptosis regulator Bcl-X; B cell lymphoma 2
                     like"
                     /calculated_mol_wt=18856
     Region          1..170
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Region          27..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     CDS             1..170
                     /gene="Bcl2l1"
                     /gene_synonym="bcl-X; Bcl-xl; Bcl2l; Bclx"
                     /coded_by="NM_001033671.1:113..625"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:24888"
                     /db_xref="RGD:2200"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapee teperetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqdtfvd lygnnaaaes rkgqerfnrw fltgmtvagv vllgslfsrk
//
LOCUS       NP_001119774             420 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 42 [Rattus
            norvegicus].
ACCESSION   NP_001119774 XP_001078808
VERSION     NP_001119774.1
DBSOURCE    REFSEQ: accession NM_001126302.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Patel,N., Smith,L.L., Faqeih,E., Mohamed,J., Gupta,V.A. and
            Alkuraya,F.S.
  TITLE     ZBTB42 mutation defines a novel lethal congenital contracture
            syndrome (LCCS6)
  JOURNAL   Hum Mol Genet 23 (24), 6584-6593 (2014)
   PUBMED   25055871
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Devaney,S.A., Mate,S.E., Devaney,J.M. and Hoffman,E.P.
  TITLE     Characterization of the ZBTB42 gene in humans and mice
  JOURNAL   Hum Genet 129 (4), 433-441 (2011)
   PUBMED   21193930
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Takahashi,A., Hirai,S., Ohtaka-Maruyama,C., Miwa,A., Hata,Y.,
            Okabe,S. and Okado,H.
  TITLE     Co-localization of a novel transcriptional repressor simiRP58 with
            RP58
  JOURNAL   Biochem Biophys Res Commun 368 (3), 637-642 (2008)
   PUBMED   18262495
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161864.1.
            
            On May 7, 2008 this sequence version replaced XP_001078808.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161864.1, CK366187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..420
                     /product="zinc finger and BTB domain-containing protein
                     42"
                     /calculated_mol_wt=46497
     Region          1..129
                     /region_name="BTB_POZ_ZBTB42"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 42 (ZBTB42); cd18956"
                     /db_xref="CDD:349737"
     Region          174..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBS3.1)"
     Region          216..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBS3.1)"
     Region          294..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..>388
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(339,341,343,345..346,349..350,353,367,369,373..374,
                     377..378,381,395,397,399,401..402,405..406)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          347..369
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          390..408
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..420
                     /gene="Zbtb42"
                     /coded_by="NM_001126302.1:117..1379"
                     /db_xref="GeneID:691556"
                     /db_xref="RGD:1582758"
ORIGIN      
        1 mefpehgvrl lgrlrqqrel gflcdctvlv gdarfpahra vlaacsvyfh lfyrdqpass
       61 rdtvrlngdi vtvpafsrll dfmyegrldl hslpvedvla aasylhmydi vkvckgrlrk
      121 kdpdletrtl gtelpgqtph plpswppafc qatpkakpps lgvkavhplp kfgppswqvs
      181 eessgaldls lkpgprpeqa hppcllqtsq cssiqqgaqp lvkaeqdsfs eqdssspqsa
      241 drspppvcas aarglavnle plhiqgtgsq qlglhaepvv dsedlgpgrh lcicplcckl
      301 fpsthalqph lsahfrerds vrtrlspega vptcplcskt fsctytlkrh erthsgekpy
      361 tcvqcgksfq yshnlsrhav vhtrekphac rwcerrftqs gdlyrhvrkf hyglvkpllv
//
LOCUS       NP_671738                214 aa            linear   ROD 27-APR-2025
DEFINITION  beta-galactoside alpha-2,6-sialyltransferase 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_671738 XP_341007
VERSION     NP_671738.2
DBSOURCE    REFSEQ: accession NM_147205.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Meng,L., Forouhar,F., Thieker,D., Gao,Z., Ramiah,A., Moniz,H.,
            Xiang,Y., Seetharaman,J., Milaninia,S., Su,M., Bridger,R.,
            Veillon,L., Azadi,P., Kornhaber,G., Wells,L., Montelione,G.T.,
            Woods,R.J., Tong,L. and Moremen,K.W.
  TITLE     Enzymatic basis for N-glycan sialylation: structure of rat
            alpha2,6-sialyltransferase (ST6GAL1) reveals conserved and unique
            features for glycan sialylation
  JOURNAL   J Biol Chem 288 (48), 34680-34698 (2013)
   PUBMED   24155237
  REMARK    GeneRIF: Comparisons of the structure with pig ST3GAL1 and a
            bacterial sialyltransferase revealed a similar positioning of
            donor, acceptor, and catalytic residues that provide a common
            structural framework for catalysis
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kuhn,B., Benz,J., Greif,M., Engel,A.M., Sobek,H. and Rudolph,M.G.
  TITLE     The structure of human alpha-2,6-sialyltransferase reveals the
            binding mode of complex glycans
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 9), 1826-1838 (2013)
   PUBMED   23999306
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Hirano,Y., Suzuki,T., Matsumoto,T., Ishihara,Y., Takaki,Y.,
            Kono,M., Dohmae,N. and Tsuji,S.
  TITLE     Disulphide linkage in mouse ST6Gal-I: determination of linkage
            positions and mutant analysis
  JOURNAL   J Biochem 151 (2), 197-203 (2012)
   PUBMED   22039275
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Liu,Z., Swindall,A.F., Kesterson,R.A., Schoeb,T.R., Bullard,D.C.
            and Bellis,S.L.
  TITLE     ST6Gal-I regulates macrophage apoptosis via alpha2-6 sialylation of
            the TNFR1 death receptor
  JOURNAL   J Biol Chem 286 (45), 39654-39662 (2011)
   PUBMED   21930713
  REMARK    GeneRIF: ST6Gal-I regulates macrophage apoptosis via alpha2-6
            sialylation of the TNFR1 death receptor.
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Maksimovic,J., Sharp,J.A., Nicholas,K.R., Cocks,B.G. and Savin,K.
  TITLE     Conservation of the ST6Gal I gene and its expression in the mammary
            gland
  JOURNAL   Glycobiology 21 (4), 467-481 (2011)
   PUBMED   21098517
  REMARK    GeneRIF: rat ST6GAL1 mRNA possess an L exon, suggesting
            conservation of this regulatory element in rodents
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Wen,D.X., Svensson,E.C. and Paulson,J.C.
  TITLE     Tissue-specific alternative splicing of the beta-galactoside alpha
            2,6-sialyltransferase gene
  JOURNAL   J Biol Chem 267 (4), 2512-2518 (1992)
   PUBMED   1733948
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Svensson,E.C., Soreghan,B. and Paulson,J.C.
  TITLE     Organization of the beta-galactoside alpha 2,6-sialyltransferase
            gene. Evidence for the transcriptional regulation of terminal
            glycosylation
  JOURNAL   J Biol Chem 265 (34), 20863-20868 (1990)
   PUBMED   2249992
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Wang,X.C., Smith,T.J. and Lau,J.T.
  TITLE     Transcriptional regulation of the liver beta-galactoside alpha
            2,6-sialyltransferase by glucocorticoids
  JOURNAL   J Biol Chem 265 (29), 17849-17853 (1990)
   PUBMED   2211665
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Wang,X., O'Hanlon,T.P., Young,R.F. and Lau,J.T.
  TITLE     Rat beta-galactoside alpha 2,6-sialyltransferase genomic
            organization: alternate promoters direct the synthesis of liver and
            kidney transcripts
  JOURNAL   Glycobiology 1 (1), 25-31 (1990)
   PUBMED   1983783
REFERENCE   10 (residues 1 to 214)
  AUTHORS   O'Hanlon,T.P., Lau,K.M., Wang,X.C. and Lau,J.T.
  TITLE     Tissue-specific expression of beta-galactoside
            alpha-2,6-sialyltransferase. Transcript heterogeneity predicts a
            divergent polypeptide
  JOURNAL   J Biol Chem 264 (29), 17389-17394 (1989)
   PUBMED   2793863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M83143.1, JAXUCZ010000011.1 and BF418553.1.
            
            On Jan 9, 2008 this sequence version replaced NP_671738.1.
            
            Transcript Variant: This variant (2) has an alternate 5' sequence,
            as compared to variant 1. The resulting isoform (2) has a shorter
            and distinct N-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M83143.1, SRR26643287.27262.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760476,
                                           SAMN16676786 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..214
                     /product="beta-galactoside alpha-2,6-sialyltransferase 1
                     isoform 2"
                     /EC_number="2.4.3.1"
                     /note="beta-galactoside alpha-2,6-sialyltransferase 1;
                     ST6Gal I; ST6 beta-galactosamide
                     alpha-2,6-sialyltranferase 1;
                     CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,
                     6-sialyltransferase 1; ST6GalI; alpha 2,6-ST 1;
                     Sialyltransferase 1 (beta-galactoside
                     alpha-2,6-sialytransferase); Sialyltransferase 1
                     (beta-galactoside alpha-26-sialytransferase)"
                     /calculated_mol_wt=25093
     Region          <45..209
                     /region_name="GT29"
                     /note="glycosyltransferase family 29; cl45931"
                     /db_xref="CDD:480271"
     CDS             1..214
                     /gene="St6gal1"
                     /gene_synonym="Siat1"
                     /coded_by="NM_147205.2:105..749"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25197"
                     /db_xref="RGD:3676"
ORIGIN      
        1 mryllfwygl phsysqcvch wtpasgifen epllslllll lgklvttekr flkdslyteg
       61 ilivwdpsvy hadipkwyqk pdynffetyk syrrlnpsqp fyilkpqmpw elwdiiqeis
      121 adliqpnpps sgmlgiiimm tlcdqvdiye flpskrktdv cyyhqkffds actmgayhpl
      181 lfeknmvkhl negtdediyl fgkatlsgfr nirc
//
LOCUS       NP_001012356             476 aa            linear   ROD 27-APR-2025
DEFINITION  non-POU domain-containing octamer-binding protein [Rattus
            norvegicus].
ACCESSION   NP_001012356 XP_228554
VERSION     NP_001012356.1
DBSOURCE    REFSEQ: accession NM_001012356.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Lei,Y.Q., Ye,Z.J., Wei,Y.L., Zhu,L.P., Zhuang,X.D., Wang,X.R. and
            Cao,H.
  TITLE     Nono deficiency impedes the proliferation and adhesion of H9c2
            cardiomyocytes through Pi3k/Akt signaling pathway
  JOURNAL   Sci Rep 13 (1), 7134 (2023)
   PUBMED   37130848
  REMARK    GeneRIF: Nono deficiency impedes the proliferation and adhesion of
            H9c2 cardiomyocytes through Pi3k/Akt signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Itai,T., Sugie,A., Nitta,Y., Maki,R., Suzuki,T., Shinkai,Y.,
            Watanabe,Y., Nakano,Y., Ichikawa,K., Okamoto,N., Utsuno,Y.,
            Koshimizu,E., Fujita,A., Hamanaka,K., Uchiyama,Y., Tsuchida,N.,
            Miyake,N., Misawa,K., Mizuguchi,T., Miyatake,S. and Matsumoto,N.
  TITLE     A novel NONO variant that causes developmental delay and cardiac
            phenotypes
  JOURNAL   Sci Rep 13 (1), 975 (2023)
   PUBMED   36653413
  REMARK    Erratum:[Sci Rep. 2023 Mar 9;13(1):3954. doi:
            10.1038/s41598-023-30968-3. PMID: 36894578]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Fu,W., Ren,H., Shou,J., Liao,Q., Li,L., Shi,Y., Jose,P.A., Zeng,C.
            and Wang,W.E.
  TITLE     Loss of NPPA-AS1 promotes heart regeneration by stabilizing
            SFPQ-NONO heteromer-induced DNA repair
  JOURNAL   Basic Res Cardiol 117 (1), 10 (2022)
   PUBMED   35247074
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Zhang,J., Rui,Y., Gao,M., Wang,L. and Yan,B.C.
  TITLE     Expression of Long Non-coding RNA RGD1566344 in the Brain Cortex of
            Male Mice After Focal Cerebral Ischemia-Reperfusion and the
            Neuroprotective Effect of a Non-coding RNA RGD1566344 Inhibitor
  JOURNAL   Cell Mol Neurobiol 41 (4), 705-716 (2021)
   PUBMED   32424772
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Xu,(.). X, Xu,(.). X, Mao,(.). Y, Lu,(.). L, Ma,(.). J, Zheng,(.).
            T, Zhang,(.). J, Zhang,(.). M, Meng,(.). L, Ma,(.). L, Cheng,(.).
            J, Chen,(.). W, Jiang,(.). H, Zhang,(.). Y and Zhang,(.). C.
  TITLE     Knockout of the NONO Gene Inhibits Neointima Formation in a Mouse
            Model of Vascular Injury
  JOURNAL   Arterioscler Thromb Vasc Biol 41 (4), 1428-1445 (2021)
   PUBMED   33626912
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Bianconcini,A., Lupo,A., Capone,S., Quadro,L., Monti,M., Zurlo,D.,
            Fucci,A., Sabatino,L., Brunetti,A., Chiefari,E., Gottesman,M.E.,
            Blaner,W.S. and Colantuoni,V.
  TITLE     Transcriptional activity of the murine retinol-binding protein gene
            is regulated by a multiprotein complex containing HMGA1, p54
            nrb/NonO, protein-associated splicing factor (PSF) and
            steroidogenic factor 1 (SF1)/liver receptor homologue 1 (LRH-1)
  JOURNAL   Int J Biochem Cell Biol 41 (11), 2189-2203 (2009)
   PUBMED   19389484
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Clemson,C.M., Hutchinson,J.N., Sara,S.A., Ensminger,A.W., Fox,A.H.,
            Chess,A. and Lawrence,J.B.
  TITLE     An architectural role for a nuclear noncoding RNA: NEAT1 RNA is
            essential for the structure of paraspeckles
  JOURNAL   Mol Cell 33 (6), 717-726 (2009)
   PUBMED   19217333
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Fox,A.H., Bond,C.S. and Lamond,A.I.
  TITLE     P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles
            in an RNA-dependent manner
  JOURNAL   Mol Biol Cell 16 (11), 5304-5315 (2005)
   PUBMED   16148043
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Xu,J., Zhong,N., Wang,H., Elias,J.E., Kim,C.Y., Woldman,I.,
            Pifl,C., Gygi,S.P., Geula,C. and Yankner,B.A.
  TITLE     The Parkinson's disease-associated DJ-1 protein is a
            transcriptional co-activator that protects against neuronal
            apoptosis
  JOURNAL   Hum Mol Genet 14 (9), 1231-1241 (2005)
   PUBMED   15790595
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Brown,S.A., Ripperger,J., Kadener,S., Fleury-Olela,F., Vilbois,F.,
            Rosbash,M. and Schibler,U.
  TITLE     PERIOD1-associated proteins modulate the negative limb of the
            mammalian circadian oscillator
  JOURNAL   Science 308 (5722), 693-696 (2005)
   PUBMED   15860628
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089880.1.
            
            On Feb 18, 2005 this sequence version replaced XP_228554.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089880.1, SRR8487227.186763.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..476
                     /product="non-POU domain-containing octamer-binding
                     protein"
                     /calculated_mol_wt=54794
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Region          60..379
                     /region_name="DBHS. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Region          78..148
                     /region_name="RRM1_p54nrb"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     54 kDa nuclear RNA- and DNA-binding protein (p54nrb);
                     cd12588"
                     /db_xref="CDD:410001"
     Site            order(124..125,128..129,131..133)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410001"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Region          154..233
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Site            203
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Region          224..316
                     /region_name="NOPS_p54nrb_PSF_PSPC1"
                     /note="NOPS domain, including C-terminal coiled-coil
                     region, in p54nrb/PSF/PSPC1 family proteins; cd12946"
                     /db_xref="CDD:240581"
     Site            order(224..226,228,268..269,271..273,275..277,279..280,
                     282..283,286..287,290..291,293..294,297..298,301..302,
                     304..305,308..309,312)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:240581"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            300
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            376
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Region          448..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     Site            461
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q15233; propagated from
                     UniProtKB/Swiss-Prot (Q5FVM4.3)"
     CDS             1..476
                     /gene="Nono"
                     /coded_by="NM_001012356.1:125..1555"
                     /db_xref="GeneID:317259"
                     /db_xref="RGD:1549738"
ORIGIN      
        1 mqsnktfnle kqnhtprkhh qhhhqqhhqq qqqqqqqqqq qppppipang qqassqnegl
       61 tidlknfrkp gektftqrsr lfvgnlppdi teeemrklfe kygkagevfi hkdkgfgfir
      121 letrtlaeia kveldnmplr gkqlrvrfac hsasltvrnl pqyvsnelle eafsvfgqve
      181 ravvivddrg rpsgkgivef sgkpaarkal drcsegsfll ttfprpvtve pmdqlddeeg
      241 lpeklviknq qfhkereqpp rfaqpgsfey eyamrwkali emekqqqdqv drnikearek
      301 lememeaarh ehqvmlmrqd lmrrqeelrr meelhnqevq krkqlelrqe eerrrreeem
      361 rrqqeemmrr qqegfkgtfp dareqeirmg qmamggamgi nnrgamppap vppgtpappg
      421 paammpdgtl gltpptterf gqaatmegig aiggtppafn rpapgaefap nkrrry
//
LOCUS       NP_076471                566 aa            linear   ROD 27-APR-2025
DEFINITION  macrophage colony-stimulating factor 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_076471
VERSION     NP_076471.3
DBSOURCE    REFSEQ: accession NM_023981.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Liu,F., Shen,X., Su,S., Cui,H., Fang,Y., Wang,T., Zhang,L.,
            Huang,Y. and Ma,C.
  TITLE     Fcgamma Receptor I-Coupled Signaling in Peripheral Nociceptors
            Mediates Joint Pain in a Rat Model of Rheumatoid Arthritis
  JOURNAL   Arthritis Rheumatol 72 (10), 1668-1678 (2020)
   PUBMED   32510872
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Fraser,D.D., Cepinskas,G., Slessarev,M., Martin,C., Daley,M.,
            Miller,M.R., O'Gorman,D.B., Gill,S.E., Patterson,E.K. and Dos
            Santos,C.C.
  TITLE     Inflammation Profiling of Critically Ill Coronavirus Disease 2019
            Patients
  JOURNAL   Crit Care Explor 2 (6), e0144 (2020)
   PUBMED   32696007
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Wlodarczyk,A., Benmamar-Badel,A., Cedile,O., Jensen,K.N.,
            Kramer,I., Elsborg,N.B. and Owens,T.
  TITLE     CSF1R Stimulation Promotes Increased Neuroprotection by CD11c+
            Microglia in EAE
  JOURNAL   Front Cell Neurosci 12, 523 (2019)
   PUBMED   30687013
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Hoshino,S., Kurotani,R., Miyano,Y., Sakahara,S., Koike,K.,
            Maruyama,M., Ishikawa,F., Sakatai,I., Abe,H. and Sakai,T.
  TITLE     Macrophage colony-stimulating factor induces prolactin expression
            in rat pituitary gland
  JOURNAL   Zoolog Sci 31 (6), 390-397 (2014)
   PUBMED   24882100
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Weir,E.C., Horowitz,M.C., Baron,R., Centrella,M., Kacinski,B.M. and
            Insogna,K.L.
  TITLE     Macrophage colony-stimulating factor release and receptor
            expression in bone cells
  JOURNAL   J Bone Miner Res 8 (12), 1507-1518 (1993)
   PUBMED   8304053
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Clinton,S.K., Underwood,R., Hayes,L., Sherman,M.L., Kufe,D.W. and
            Libby,P.
  TITLE     Macrophage colony-stimulating factor gene expression in vascular
            cells and in experimental and human atherosclerosis
  JOURNAL   Am J Pathol 140 (2), 301-316 (1992)
   PUBMED   1739124
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Manos,M.M.
  TITLE     Expression and processing of a recombinant human macrophage
            colony-stimulating factor in mouse cells
  JOURNAL   Mol Cell Biol 8 (11), 5035-5039 (1988)
   PUBMED   3264878
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Cerretti,D.P., Wignall,J., Anderson,D., Tushinski,R.J.,
            Gallis,B.M., Stya,M., Gillis,S., Urdal,D.L. and Cosman,D.
  TITLE     Human macrophage-colony stimulating factor: alternative RNA and
            protein processing from a single gene
  JOURNAL   Mol Immunol 25 (8), 761-770 (1988)
   PUBMED   2460758
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Sherr,C.J., Rettenmier,C.W., Sacca,R., Roussel,M.F., Look,A.T. and
            Stanley,E.R.
  TITLE     The c-fms proto-oncogene product is related to the receptor for the
            mononuclear phagocyte growth factor, CSF-1
  JOURNAL   Cell 41 (3), 665-676 (1985)
   PUBMED   2408759
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC074007.1.
            
            On Jul 8, 2004 this sequence version replaced NP_076471.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC074007.1, AF515736.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132263,
                                           SAMD00132264 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..566
                     /product="macrophage colony-stimulating factor 1
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="macrophage colony-stimulating factor 1; MCSF;
                     CSF-1; colony stimulating factor 1 (macrophage);
                     proteoglycan macrophage colony-stimulating factor"
                     /calculated_mol_wt=58820
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3351
     mat_peptide     33..566
                     /product="Macrophage colony-stimulating factor 1.
                     /id=PRO_0000005859"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZQ0.1)"
                     /calculated_mol_wt=58820
     Region          40..179
                     /region_name="CSF-1"
                     /note="Macrophage colony stimulating factor-1 (CSF-1);
                     pfam05337"
                     /db_xref="CDD:398810"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Region          <193..311
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
     Region          197..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            302
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P09603; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            355
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P09603; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            357
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P09603; propagated from
                     UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Region          434..484
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Site            509..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     Region          538..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8JZQ0.1)"
     CDS             1..566
                     /gene="Csf1"
                     /gene_synonym="PG-M-CSF"
                     /coded_by="NM_023981.4:161..1861"
                     /db_xref="GeneID:78965"
                     /db_xref="RGD:621063"
ORIGIN      
        1 mtargaagrc psstwmgsrl llvcllvsrs vaevsehcsh mignghlqil qqlidsqmet
       61 aclieykfvd qeqlddpvcy lkkafvlvqv iieetmrfkd ntpnanater lqelsmklns
      121 cfikdykeqn eacvqtykes plrllekikn ffnetknfle kdwnifsknc ndslakcssr
      181 dvvtkpdcnc lypkatpssd lasasphqpp apsmapladl awddsqrteg ssllpsdlpl
      241 riedpgsakq rpprstcqtl esteqpnhed pqphpsagap ipgvediies smgtnwvlee
      301 asgeasegfl tqerkfspsn pvggsiqaet drpwarsass pfpkltedqq ptnitdtplt
      361 evnpmrptgq tlnntpektd gsstlredqq eprsphfatl npqrvgnsat pyakllppks
      421 hswgivlplg elegkkstrd rrspaelkgg pasegaarpv aqstrdrrsp aelkggpase
      481 gaarpvarfn sipltdtgss iqdpqtsafv fwvlgiilvl lavggllfys wkrrshrdpr
      541 tldssvgrpe gsslaqdedr qvelpv
//
LOCUS       NP_001017505             494 aa            linear   ROD 27-APR-2025
DEFINITION  integrin beta-like protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001017505 XP_573839
VERSION     NP_001017505.1
DBSOURCE    REFSEQ: accession NM_001017505.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Chen,X., Li,X., Wu,X., Ding,Y., Li,Y., Zhou,G., Wei,Y., Chen,S.,
            Lu,X., Xu,J., Liu,S., Li,J. and Cai,L.
  TITLE     Integrin beta-like 1 mediates fibroblast-cardiomyocyte crosstalk to
            promote cardiac fibrosis and hypertrophy
  JOURNAL   Cardiovasc Res 119 (10), 1928-1941 (2023)
   PUBMED   37395147
  REMARK    GeneRIF: Integrin beta-like 1 mediates fibroblast-cardiomyocyte
            crosstalk to promote cardiac fibrosis and hypertrophy.
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087076.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573839.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087076.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q25"
     Protein         1..494
                     /product="integrin beta-like protein 1 precursor"
                     /note="integrin beta-like protein 1; integrin, beta-like
                     1"
                     /calculated_mol_wt=51387
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2536
     mat_peptide     24..494
                     /product="Integrin beta-like protein 1.
                     /id=PRO_0000323024"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQQ8.1)"
                     /calculated_mol_wt=51387
     Region          51..494
                     /region_name="Cysteine-rich tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQQ8.1)"
     Site            405
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5PQQ8.1)"
     CDS             1..494
                     /gene="Itgbl1"
                     /coded_by="NM_001017505.1:93..1577"
                     /db_xref="GeneID:498564"
                     /db_xref="RGD:1560635"
ORIGIN      
        1 mhppgfknfl llvsslffig lsaapqsfsp slrslsgapc rlsraeserr crapgqppgs
       61 alchdrgrce cgvcichvte pgtyfgplce chdwvcetyd gktcaghgtc dcgkckcdvg
      121 wsgeacqypt kcdltkkisn qmcknsqdvi csnagtchcg rckcdnsdgh gliygkfcec
      181 ddreciddet eeicgghgkc ycgncyceag whgdkcefqc ditpweskrr ctspdgkvcs
      241 nrgtcvcgec schdvdptgd wgdihgdtce cderdcravy drysddfcsg hgqcncgrcd
      301 cragwygkkc ehpkncplsa eestrkcqgs sdlpcsgrgr cecgrctcyp pgdsrvygkt
      361 cecddrrced ldgvvcggrg tcscgrcvce kgwfgklcqh prkcnmteeq srslcesadg
      421 tlcsgkgsch cgkcicsgee wyisgefcdc ddrdcdkhdg lictgngics cgncecwdgw
      481 ngnaceiwlg teyp
//
LOCUS       NP_037118                889 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4 [Rattus norvegicus].
ACCESSION   NP_037118 XP_001053672 XP_343428
VERSION     NP_037118.1
DBSOURCE    REFSEQ: accession NM_012986.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Lei,J., Zheng,F., Chen,L., Zhang,R., Yang,Y., Yin,Z. and Luo,L.
  TITLE     Gstp1 negatively regulates blood pressure in hypertensive rat via
            promoting APLNR ubiquitination degradation mediated by Nedd4
  JOURNAL   Clin Sci (Lond) 138 (14), 883-900 (2024)
   PUBMED   38959295
  REMARK    GeneRIF: Gstp1 negatively regulates blood pressure in hypertensive
            rat via promoting APLNR ubiquitination degradation mediated by
            Nedd4.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Liu,Y., Yang,H., Zeng,R., He,L., Xiao,T., Peng,X., Kuang,Z. and
            Wu,L.
  TITLE     NEDD4-2 and the CLC-2 channel regulate neuronal excitability in the
            pathogenesis of mesial temporal lobe epilepsy
  JOURNAL   Sci Rep 14 (1), 4835 (2024)
   PUBMED   38418461
  REMARK    GeneRIF: NEDD4-2 and the CLC-2 channel regulate neuronal
            excitability in the pathogenesis of mesial temporal lobe epilepsy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Zou,Z., Zhao,T., Zeng,Z. and An,Y.
  TITLE     Serum and glucocorticoid inducible kinase 1 modulates mitochondrial
            dysfunction and oxidative stress in doxorubicin-induced
            cardiomyocytes by regulating Hippo pathway via Neural precursor
            cell-expressed developmentally down-regulated 4 type 2
  JOURNAL   Hum Exp Toxicol 42, 9603271231158039 (2023)
   PUBMED   36781297
  REMARK    GeneRIF: Serum and glucocorticoid inducible kinase 1 modulates
            mitochondrial dysfunction and oxidative stress in
            doxorubicin-induced cardiomyocytes by regulating Hippo pathway via
            Neural precursor cell-expressed developmentally down-regulated 4
            type 2.
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Shao,Y., Jiang,Z., He,D. and Shen,J.
  TITLE     NEDD4 attenuates phosgene-induced acute lung injury through the
            inhibition of Notch1 activation
  JOURNAL   J Cell Mol Med 26 (10), 2831-2840 (2022)
   PUBMED   35355403
  REMARK    GeneRIF: NEDD4 attenuates phosgene-induced acute lung injury
            through the inhibition of Notch1 activation.
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Hu,Y., Hong,X.Y., Yang,X.F., Ma,R.H., Wang,X., Zhang,J.F., Feng,Q.,
            Li,X.G., Sun,D.S., Li,X., Wan,H.L., Li,T., Wang,Q., Ke,D.,
            Wang,J.Z. and Liu,G.P.
  TITLE     Inflammation-dependent ISG15 upregulation mediates MIA-induced
            dendrite damages and depression by disrupting NEDD4/Rap2A signaling
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (6), 1477-1489 (2019)
   PUBMED   30826466
  REMARK    GeneRIF: The data revealed that maternal immune activation impedes
            offspring's dendrite development and causes depressive like
            behaviors by upregulating ISG15 and suppressing NEDD4/Rap2A
            signaling.
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Hatakeyama,S., Jensen,J.P. and Weissman,A.M.
  TITLE     Subcellular localization and ubiquitin-conjugating enzyme (E2)
            interactions of mammalian HECT family ubiquitin protein ligases
  JOURNAL   J Biol Chem 272 (24), 15085-15092 (1997)
   PUBMED   9182527
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Staub,O., Yeger,H., Plant,P.J., Kim,H., Ernst,S.A. and Rotin,D.
  TITLE     Immunolocalization of the ubiquitin-protein ligase Nedd4 in tissues
            expressing the epithelial Na+ channel (ENaC)
  JOURNAL   Am J Physiol 272 (6 Pt 1), C1871-C1880 (1997)
   PUBMED   9227416
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Imhof,M.O. and McDonnell,D.P.
  TITLE     Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent
            activation of transcription by human progesterone and
            glucocorticoid receptors
  JOURNAL   Mol Cell Biol 16 (6), 2594-2605 (1996)
   PUBMED   8649367
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Staub,O., Dho,S., Henry,P., Correa,J., Ishikawa,T., McGlade,J. and
            Rotin,D.
  TITLE     WW domains of Nedd4 bind to the proline-rich PY motifs in the
            epithelial Na+ channel deleted in Liddle's syndrome
  JOURNAL   EMBO J 15 (10), 2371-2380 (1996)
   PUBMED   8665844
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK365888.1, U50842.1, CB615796.1, CB568921.1, DY312717.1,
            BQ191927.1, EV775947.1, DY318090.1, CF110862.1 and CB326200.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_343428.3, XP_001053672.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..889
                     /product="E3 ubiquitin-protein ligase NEDD4"
                     /EC_number="2.3.2.26"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated 4, E3 ubiquitin protein ligase; neural
                     precursor cell expressed, developmentally down-regulated
                     gene 4A; HECT-type E3 ubiquitin transferase NEDD4"
                     /calculated_mol_wt=102624
     Region          79..210
                     /region_name="C2_NEDD4_NEDD4L"
                     /note="C2 domain present in the Human neural precursor
                     cell-expressed, developmentally down-regulated 4 (NEDD4)
                     and NEDD4-like (NEDD4L/NEDD42); cd04033"
                     /db_xref="CDD:175999"
     Site            order(100,152,154,159)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175999"
     Region          254..282
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(266,277)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          407..436
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          463..495
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(479,490)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(538,569,580,642,815,850..851,854..858,878,885)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          556..885
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(670,673..674,676..677,680,685,687,691..692,693,699,
                     704,721,725)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..889
                     /gene="Nedd4"
                     /gene_synonym="Nedd4a"
                     /coded_by="NM_012986.1:66..2735"
                     /db_xref="GeneID:25489"
                     /db_xref="RGD:3157"
ORIGIN      
        1 mssdmaaddt eapvlsedev wefcldknee gggspgsdvt dtceppcgcw elnpssleee
       61 hvlftadpyl elhnddtrvv rvkviagigl akkdilgasd pyvrvtlydp msgvltsvqt
      121 ktikkslnpk wneeilfrvl pqqhrilfev fdenrltrdd flgqvdvply plptenprme
      181 rpytfkdfvl hprshksrvk gylrlkmtyl pkngsddena dqaeelepgw vvldqpdaat
      241 hlqhppepsp lppgweerqd vlgrtyyvnh esrttqwkrp speddltdde ngdiqlqaqr
      301 afttrrqise dvdgpdnhes penweivred entmysgqav qsppsghpdv qvrlaeeldt
      361 rltmygnpat sqpvtssnhs srggssqtci feeqptlpvl lptssglppg weekqddrgr
      421 syyvdhnskt ttwskptmqd dprskipahl rgktpvdsnd lgplppgwee rthtdgrvff
      481 inhnikktqw edprmqnvai tgpavpysrd ykrkyeffrr klkkqtdipn kfemklrran
      541 iledsyrrim gvkradflka rlwiefdgek gldyggvare wffliskemf npyyglfeys
      601 atdnytlqin pnsglcnedh lsyfkfigrv agmavyhgkl ldgffirpfy kmmlqklitl
      661 hdmesvdsey ysslrwilen dpteldlrfi ideelfgqth qhelktggse vvvtnknkke
      721 yiylviqwrf vnriqkqmaa fkegffelip qdlikifden elellmcglg dvdvndwreh
      781 tkykngysln hqvihwfwka vlmmdsekri rllqfvtgts rvpmngfael ygsngpqsft
      841 veqwgtpdkl prahtcfnrl dlppyesfde lwdklqmaie ntqgfdgvd
//
LOCUS       NP_112342                482 aa            linear   ROD 27-APR-2025
DEFINITION  high affinity 3',5'-cyclic-AMP phosphodiesterase 7A [Rattus
            norvegicus].
ACCESSION   NP_112342 XP_001053781 XP_001055271 XP_001055326 XP_215540
VERSION     NP_112342.1
DBSOURCE    REFSEQ: accession NM_031080.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Morales-Garcia,J.A., Echeverry-Alzate,V., Alonso-Gil,S.,
            Sanz-SanCristobal,M., Lopez-Moreno,J.A., Gil,C., Martinez,A.,
            Santos,A. and Perez-Castillo,A.
  TITLE     Phosphodiesterase7 Inhibition Activates Adult Neurogenesis in
            Hippocampus and Subventricular Zone In Vitro and In Vivo
  JOURNAL   Stem Cells 35 (2), 458-472 (2017)
   PUBMED   27538853
  REMARK    GeneRIF: PDE7 inhibition controls stem cell expansion in the
            subgranular zone of the dentate gyrus of the hippocampus (SGZ) and
            the subventricular zone (SVZ) in the adult rat brain.
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Conti,M. and Beavo,J.
  TITLE     Biochemistry and physiology of cyclic nucleotide
            phosphodiesterases: essential components in cyclic nucleotide
            signaling
  JOURNAL   Annu Rev Biochem 76, 481-511 (2007)
   PUBMED   17376027
  REMARK    Review article
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yamamoto,S., Sugahara,S., Ikeda,K. and Shimizu,Y.
  TITLE     Pharmacological profile of a novel phosphodiesterase 7A and -4 dual
            inhibitor, YM-393059, on acute and chronic inflammation models
  JOURNAL   Eur J Pharmacol 550 (1-3), 166-172 (2006)
   PUBMED   17010967
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Miro,X., Perez-Torres,S., Palacios,J.M., Puigdomenech,P. and
            Mengod,G.
  TITLE     Differential distribution of cAMP-specific phosphodiesterase 7A
            mRNA in rat brain and peripheral organs
  JOURNAL   Synapse 40 (3), 201-214 (2001)
   PUBMED   11304758
  REMARK    GeneRIF: results are consistent with PDE7A being involved in the
            regulation of cAMP signaling in many brain functions.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Hoffmann,R., Abdel'Al,S. and Engels,P.
  TITLE     Differential distribution of rat PDE-7 mRNA in embryonic and adult
            rat brain
  JOURNAL   Cell Biochem Biophys 28 (2-3), 103-113 (1998)
   PUBMED   9515162
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Bloom,T.J. and Beavo,J.A.
  TITLE     Identification and tissue-specific expression of PDE7
            phosphodiesterase splice variants
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 14188-14192 (1996)
   PUBMED   8943082
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Nov 23, 2008 this sequence version replaced
            XP_215540.3, XP_001053781.1, XP_001055326.1, XP_001055271.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.9050.1,
                                           SRR26643294.8444.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..482
                     /product="high affinity 3',5'-cyclic-AMP phosphodiesterase
                     7A"
                     /EC_number="3.1.4.53"
                     /note="high affinity cAMP-specific 3',5'-cyclic
                     phosphodiesterase 7A; rolipram-insensitive
                     phosphodiesterase type 7; cAMP-specific phosphodiesterase
                     7A"
                     /calculated_mol_wt=55295
     Region          211..431
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     CDS             1..482
                     /gene="Pde7a"
                     /gene_synonym="PDE7-1"
                     /coded_by="NM_031080.1:129..1577"
                     /db_xref="GeneID:81744"
                     /db_xref="RGD:68391"
ORIGIN      
        1 mevcyqlpvl pldrpvpqhv lsrrgaisfs sssalfgcph prqlsqrrga isydssdqta
       61 lyirmlgdvr vrsragfete rrgshpyidf rifhaqseie asvsarnirr llsfqrylrs
      121 srffrgatvc rslnildedy ngqakcmlek vgnwnfdifl fdrltngnsl vsltfhlfsl
      181 hglieyfhld mvklrrflvm iqedyhsqnp yhnavhaadv tqamhcylke pklansvtpw
      241 dillsliaaa thdldhpgvn qpfliktnhy latlykntsv lenhhwrsav gllresglfs
      301 hlplesrhem eaqigalila tdisrqneyl slfrshldkg dlhlddgrhr hlvlqmalkc
      361 adicnpcrnw elskqwsekv teeffhqgdi ekkyhlgvsp lcdrqtesia niqigfmtyl
      421 veplftewar fsdtrlsqtm lghvglnkas wkglqrqqps sedasaafel nsqlltqenr
      481 ls
//
LOCUS       NP_001005530             428 aa            linear   ROD 27-APR-2025
DEFINITION  monocarboxylate transporter 13 [Rattus norvegicus].
ACCESSION   NP_001005530 XP_213359
VERSION     NP_001005530.1
DBSOURCE    REFSEQ: accession NM_001005530.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Williams,A.L., Jacobs,S.B., Moreno-Macias,H., Huerta-Chagoya,A.,
            Churchhouse,C., Marquez-Luna,C., Garcia-Ortiz,H.,
            Gomez-Vazquez,M.J., Burtt,N.P., Aguilar-Salinas,C.A.,
            Gonzalez-Villalpando,C., Florez,J.C., Orozco,L., Haiman,C.A.,
            Tusie-Luna,T. and Altshuler,D.
  CONSRTM   SIGMA Type 2 Diabetes Consortium
  TITLE     Sequence variants in SLC16A11 are a common risk factor for type 2
            diabetes in Mexico
  JOURNAL   Nature 506 (7486), 97-101 (2014)
   PUBMED   24390345
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Halestrap,A.P. and Meredith,D.
  TITLE     The SLC16 gene family-from monocarboxylate transporters (MCTs) to
            aromatic amino acid transporters and beyond
  JOURNAL   Pflugers Arch 447 (5), 619-628 (2004)
   PUBMED   12739169
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081902.1.
            
            On Oct 8, 2004 this sequence version replaced XP_213359.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081902.1, SRR8487227.23720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..428
                     /product="monocarboxylate transporter 13"
                     /note="MCT 13; solute carrier family 16 (monocarboxylic
                     acid transporters), member 13; solute carrier family 16,
                     member 13 (monocarboxylic acid transporter 13)"
                     /calculated_mol_wt=44862
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Region          13..392
                     /region_name="MFS_MCT11_13"
                     /note="Monocarboxylate transporters 11 and 13 of the Major
                     Facilitator Superfamily of transporters; cd17423"
                     /db_xref="CDD:340981"
     Site            order(24..25,28..29,32,67,118..119,121..123,126,145,
                     148..149,152,223,226..227,230..232,235,262,266,317..318,
                     322,326,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340981"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            309..329
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            338..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     Site            374..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE2.1)"
     CDS             1..428
                     /gene="Slc16a13"
                     /coded_by="NM_001005530.1:286..1572"
                     /db_xref="GeneID:287451"
                     /db_xref="RGD:1359138"
ORIGIN      
        1 mvhrteppdg gwgwmvvlsa ffqsalvfgv lrsfgvffve fvaafeeqaa rvswiasigi
       61 avqqfgspig salstklgpr pvvmtggila algmllasfa tslthlylsi gllsgsgwal
      121 tftptlacls ryfsqrrsla mglaltgvgi ssfafaplfq wllnnyawrg alllvsalsl
      181 hlvacgallr plsltedtav ggpwaqitsl lchgpflryt valtlintgy fipyvhlvah
      241 lqdlgwdplp aafllsvaai sdlvgrvasg wlgdavpgpv arllmlwttl tgvslalfpv
      301 aqasttlvvl avaygftsga ltpvafsvip elvgtgriyc glglvqmies vggllgapls
      361 gylrdvtgny tasfvvagaf llagsgvlit lphffscisl stsrpqdlvi eapdtkiplp
      421 keeglgen
//
LOCUS       NP_446179                462 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear factor interleukin-3-regulated protein [Rattus norvegicus].
ACCESSION   NP_446179
VERSION     NP_446179.2
DBSOURCE    REFSEQ: accession NM_053727.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Zhang,T., Yu,F., Guo,L., Chen,M., Yuan,X. and Wu,B.
  TITLE     Small Heterodimer Partner Regulates Circadian Cytochromes p450 and
            Drug-Induced Hepatotoxicity
  JOURNAL   Theranostics 8 (19), 5246-5258 (2018)
   PUBMED   30555544
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhao,M., Zhang,T., Yu,F., Guo,L. and Wu,B.
  TITLE     E4bp4 regulates carboxylesterase 2 enzymes through repression of
            the nuclear receptor Rev-erbalpha in mice
  JOURNAL   Biochem Pharmacol 152, 293-301 (2018)
   PUBMED   29653076
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Lin,K.H., Kuo,C.H., Kuo,W.W., Ho,T.J., Pai,P., Chen,W.K., Pan,L.F.,
            Wang,C.C., Padma,V.V. and Huang,C.Y.
  TITLE     NFIL3 suppresses hypoxia-induced apoptotic cell death by targeting
            the insulin-like growth factor 2 receptor
  JOURNAL   J Cell Biochem 116 (6), 1113-1120 (2015)
   PUBMED   25536374
  REMARK    GeneRIF: results demonstrate that NFIL3 is an important negative
            transcription factor, which through binding to the promoter of
            IGF2R, suppresses the apoptosis induced by IGF2R signaling in H9c2
            cardiomyoblast cells under hypoxic conditions.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   van der Kallen,L.R., Eggers,R., Ehlert,E.M., Verhaagen,J.,
            Smit,A.B. and van Kesteren,R.E.
  TITLE     Genetic Deletion of the Transcriptional Repressor NFIL3 Enhances
            Axon Growth In Vitro but Not Axonal Repair In Vivo
  JOURNAL   PLoS One 10 (5), e0127163 (2015)
   PUBMED   25993115
  REMARK    GeneRIF: removal of NFIL3 in vivo does not recapitulate the
            regeneration-promoting effects that were previously observed in
            vitro.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Yamajuku,D., Shibata,Y., Kitazawa,M., Katakura,T., Urata,H.,
            Kojima,T., Takayasu,S., Nakata,O. and Hashimoto,S.
  TITLE     Cellular DBP and E4BP4 proteins are critical for determining the
            period length of the circadian oscillator
  JOURNAL   FEBS Lett 585 (14), 2217-2222 (2011)
   PUBMED   21635892
  REMARK    GeneRIF: Data show that knockdown of DBP, D-box positive regulator,
            led to a short-period phenotype, and overexpression of DBP produced
            a long-period rhythm, while knockdown and overexpression of E4BP4,
            D-box negative regulator, had the opposite effect of DBP.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Kong,S.L., Chui,P., Lim,B. and Salto-Tellez,M.
  TITLE     Elucidating the molecular physiopathology of acute respiratory
            distress syndrome in severe acute respiratory syndrome patients
  JOURNAL   Virus Res 145 (2), 260-269 (2009)
   PUBMED   19635508
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Junghans,D., Chauvet,S., Buhler,E., Dudley,K., Sykes,T. and
            Henderson,C.E.
  TITLE     The CES-2-related transcription factor E4BP4 is an intrinsic
            regulator of motoneuron growth and survival
  JOURNAL   Development 131 (18), 4425-4434 (2004)
   PUBMED   15306565
  REMARK    GeneRIF: Pathways regulated by E4BP4 are of potential interest both
            for understanding neuromuscular development and for promoting
            neuronal survival and regeneration in pathological situations
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Newman,J.R. and Keating,A.E.
  TITLE     Comprehensive identification of human bZIP interactions with
            coiled-coil arrays
  JOURNAL   Science 300 (5628), 2097-2101 (2003)
   PUBMED   12805554
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Nishimura,Y. and Tanaka,T.
  TITLE     Calcium-dependent activation of nuclear factor regulated by
            interleukin 3/adenovirus E4 promoter-binding protein gene
            expression by calcineurin/nuclear factor of activated T cells and
            calcium/calmodulin-dependent protein kinase signaling
  JOURNAL   J Biol Chem 276 (23), 19921-19928 (2001)
   PUBMED   11262393
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Chu,C.C. and Paul,W.E.
  TITLE     Expressed genes in interleukin-4 treated B cells identified by cDNA
            representational difference analysis
  JOURNAL   Mol Immunol 35 (8), 487-502 (1998)
   PUBMED   9798653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072527.1.
            
            On Jun 13, 2004 this sequence version replaced NP_446179.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            regulator that binds as a homodimer to activating transcription
            factor (ATF) sites in many cellular and viral promoters. The
            encoded protein represses Per1 and Per2 expression and therefore
            plays a role in the regulation of circadian rhythm. [provided by
            RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072527.1, CK364644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..462
                     /product="nuclear factor interleukin-3-regulated protein"
                     /note="E4 promoter-binding protein 4"
                     /calculated_mol_wt=50650
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Region          72..131
                     /region_name="bZIP_NFIL3"
                     /note="Basic leucine zipper (bZIP) domain of Nuclear
                     factor interleukin-3-regulated protein (NFIL3): a
                     DNA-binding and dimerization domain; cd14694"
                     /db_xref="CDD:269842"
     Region          73..131
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269842"
     Region          79..95
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Site            order(79..80,82..84,86..91,93..95)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269842"
     Site            order(94,97..98,101..102,104..105,108..109,111..112,
                     115..116,118..119,122..123,125..126)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269842"
     Region          99..106
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Region          130..461
                     /region_name="Vert_IL3-reg_TF"
                     /note="Vertebrate interleukin-3 regulated transcription
                     factor; pfam06529"
                     /db_xref="CDD:368956"
     Region          188..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Region          259..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16649; propagated from
                     UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16649; propagated from
                     UniProtKB/Swiss-Prot (Q6IMZ0.1)"
     CDS             1..462
                     /gene="Nfil3"
                     /gene_synonym="E4BP4"
                     /coded_by="NM_053727.2:291..1679"
                     /db_xref="GeneID:114519"
                     /db_xref="RGD:620972"
ORIGIN      
        1 mqlrkmqaik kepasldptg ssdkmlllns alaevaedla sgedlllneg smgknkssac
       61 rrkrefipde kkdamywekr rknneaakrs rekrrlndlv lenklialge enatlkaell
      121 slklkfglis stvyaqeiqk lsnstavyfq dyqtskaavs syvdehepam vagscisvik
      181 hspqsslsdv sevssvehtq espaqggcrs penkfpvikq epvelesfar esreergays
      241 asiyqsymgs sfstyshspp llqvhgstsn sprtseadeg vvgkssdged eqqvpkgpih
      301 spvelqrvha tvvkvpevnp salphklrik akamqvkvea ldsefegmqk lsspadalak
      361 rhfdlekhga sgtahsslpp fsvqvtniqd wslrsehwhh kelggktqgt fktgvvevkd
      421 sgykvseaen lylkqgvanl saevvslkrf iatqpisasd sr
//
LOCUS       NP_001103382            1050 aa            linear   ROD 27-APR-2025
DEFINITION  TSC22 domain family protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001103382 XP_001072618 XP_001072656 XP_573819
VERSION     NP_001103382.1
DBSOURCE    REFSEQ: accession NM_001109912.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Yan,X., Zhang,J., Pan,L., Wang,P., Xue,H., Zhang,L., Gao,X.,
            Zhao,X., Ning,Y. and Chen,Y.G.
  TITLE     TSC-22 promotes transforming growth factor beta-mediated cardiac
            myofibroblast differentiation by antagonizing Smad7 activity
  JOURNAL   Mol Cell Biol 31 (18), 3700-3709 (2011)
   PUBMED   21791611
  REMARK    GeneRIF: TSC-22 can promote the differentiation of cardiac
            myofibroblasts by increasing expression of the fibrotic genes for
            alpha-smooth muscle actin, PAI-1, fibronectin, and collagen I.
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Huser,C.A., Pringle,M.A., Heath,V.J., Bell,A.K., Kendrick,H.,
            Smalley,M.J., Crighton,D., Ryan,K.M., Gusterson,B.A. and Stein,T.
  TITLE     TSC-22D1 isoforms have opposing roles in mammary epithelial cell
            survival
  JOURNAL   Cell Death Differ 17 (2), 304-315 (2010)
   PUBMED   19745830
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Ohta,S., Shimekake,Y. and Nagata,K.
  TITLE     Molecular cloning and characterization of a transcription factor
            for the C-type natriuretic peptide gene promoter
  JOURNAL   Eur J Biochem 242 (3), 460-466 (1996)
   PUBMED   9022669
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Hamil,K.G. and Hall,S.H.
  TITLE     Cloning of rat Sertoli cell follicle-stimulating hormone primary
            response complementary deoxyribonucleic acid: regulation of TSC-22
            gene expression
  JOURNAL   Endocrinology 134 (3), 1205-1212 (1994)
   PUBMED   8161377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_001072656.1, XP_001072618.1, XP_573819.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.60638.1,
                                           SRR26643298.58066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..1050
                     /product="TSC22 domain family protein 1 isoform 1"
                     /note="TSC22 domain family protein 1; regulatory protein
                     TSC-22; TGFB-stimulated clone 22 homolog; transforming
                     growth factor beta-1-induced transcript 4 protein;
                     Transforming growth factor beta stimulated clone 22;
                     transforming growth factor beta 1 induced transcript 4"
                     /calculated_mol_wt=106656
     Region          1..99
                     /region_name="Required for interaction with TGFBR1 and
                     promotion of TGF-beta signaling.
                     /evidence=ECO:0000250|UniProtKB:Q15714"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          22..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          126..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15714; propagated from
                     UniProtKB/Swiss-Prot (P62501.2)"
     Region          445..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          511..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          <541..826
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          581..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          720..740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          795..847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          879..919
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          960..1038
                     /region_name="ZIP_TSC22D1"
                     /note="leucine zipper domain found in TSC22 domain family
                     protein 1; cd21938"
                     /db_xref="CDD:409278"
     Site            order(978..980,983,986..987,990..991,993..994,997..998,
                     1000..1001,1004..1005,1008,1012)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409278"
     Region          983..1004
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     Region          1015..1050
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62501.2)"
     CDS             1..1050
                     /gene="Tsc22d1"
                     /gene_synonym="Tgfb1i4; TS22A; TSC-22"
                     /coded_by="NM_001109912.1:338..3490"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:498545"
                     /db_xref="RGD:3850"
ORIGIN      
        1 mhqppestaa aaaaadisar kmahpamfpr rgsgggsasa lsaagtgvsg aapssedfpp
       61 pssllqpppp aasstqgpqp pppqslnlls qaqlqgqpla pggtqmkkks gfqitsvtpa
      121 qisasissnn siaedtesyd dldeshtedl ssseildvsl sratdlgepe rssseetlnn
      181 fqeaetpgav spnqphlpqp hlphlpqqnv vingnahphh lhhhhhihhg hhlhhghhhs
      241 shaavastsv pggppptspv srklstagss dggvpvppts avssaglpas vmtsirapst
      301 pgsigvnsvt gtnatnnvni aavggfspgv ansvhpnavs isggpgvtsg vnvnvlsgmg
      361 ngtisspvln aaagitvgvv ssqqqqpqqp pptvntsrfr vvkldstsep fkkgrwtcte
      421 fyerenavpg pegvainkvv etvkqtptea ssserestsg ssvsssvstl shytesvgsg
      481 emgaptvvvq qqqplppapp glqgvalqql dfsspgpqsi sqsqmsqvql qpqelsfqqk
      541 pnlqpvplqa tmsaatgiqp spvnvvgvts avgqqpsiss laqpqlpypq pappvqtplp
      601 gappqqlqyg qqqpmvptqi apghgqpatq nppseyaqqq pifqaamssg qssstgtgas
      661 vipvaqpqgi qlpvqptavq aqpagatgqp igqaptavst vpaggqiasi gqqaniptav
      721 qppstqvtps vvqqgappss qvvlpaptgi ihqgvqtsap slpqqlviap qstmvavppq
      781 tqgveavahg vvshqlptgs plpsastisv tsqvssagps gmssvptnlv ppqniaqppa
      841 tqngslvqsv sqspliatni nlplaqqipl sstqfstqsl aqaigsqmed trrpaepssg
      901 glpqtlsgds ggvsavsdgs ssslaasasl fplkvlpltt plvdgedess gasvvaidnk
      961 ieqamdlvks hlmyavreev evlkeqikel ieknsqleqe nnllktlasp eqlaqfqaql
     1021 qtgsppattq pqgttqppaq pasqgsgsta
//
LOCUS       NP_001102793             381 aa            linear   ROD 27-APR-2025
DEFINITION  40-kDa huntingtin-associated protein [Rattus norvegicus].
ACCESSION   NP_001102793 XP_001053469 XP_577058
VERSION     NP_001102793.1
DBSOURCE    REFSEQ: accession NM_001109323.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Huang,Z.N. and Her,L.S.
  TITLE     The Ubiquitin Receptor ADRM1 Modulates HAP40-Induced Proteasome
            Activity
  JOURNAL   Mol Neurobiol 54 (9), 7382-7400 (2017)
   PUBMED   27815841
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Milman,P. and Woulfe,J.
  TITLE     Novel variant of neuronal intranuclear rodlet immunoreactive for 40
            kDa huntingtin associated protein and ubiquitin in the mouse brain
  JOURNAL   J Comp Neurol 521 (16), 3832-3846 (2013)
   PUBMED   23749422
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Pal,A., Severin,F., Lommer,B., Shevchenko,A. and Zerial,M.
  TITLE     Huntingtin-HAP40 complex is a novel Rab5 effector that regulates
            early endosome motility and is up-regulated in Huntington's disease
  JOURNAL   J Cell Biol 172 (4), 605-618 (2006)
   PUBMED   16476778
  REMARK    GeneRIF: We have identified Huntingtin (Htt)-associated protein 40
            (HAP40) as a novel effector of the small guanosine triphosphatase
            Rab5, a key regulator of endocytosis. HAP40 mediates the
            recruitment of Htt by Rab5 onto early endosomes.
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Peters,M.F. and Ross,C.A.
  TITLE     Isolation of a 40-kDa Huntingtin-associated protein
  JOURNAL   J Biol Chem 276 (5), 3188-3194 (2001)
   PUBMED   11035034
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474110.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001053469.1, XP_577058.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..381
                     /product="40-kDa huntingtin-associated protein"
                     /note="factor 8-associated gene A; factor VIII intron 22
                     protein; coagulation factor VIII-associated (intronic
                     transcript) 1; huntingtin-associated protein 40"
                     /calculated_mol_wt=40413
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P23610; propagated from
                     UniProtKB/Swiss-Prot (M0RDU0.1)"
     Region          34..36
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q00558"
                     /note="propagated from UniProtKB/Swiss-Prot (M0RDU0.1)"
     Region          213..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0RDU0.1)"
     CDS             1..381
                     /gene="F8a1"
                     /gene_synonym="F8a; Hap40; RGD1566014"
                     /coded_by="NM_001109323.1:51..1196"
                     /db_xref="GeneID:501661"
                     /db_xref="RGD:1566014"
ORIGIN      
        1 maagsasslg ggswpgseag dflaryrqvs nklkkrflrk pnvaeageqf aqlarelraq
       61 eclpyaawcq lavarcqqal fhgpgealal teaarlflrq ecdarqrlgc paaygeplqa
      121 aasalgaavr lhlelgqpaa aaalclelaa alravgqpaa aaghfqraaq lhlplmplaa
      181 lqalgdaasc qllardytga lavftrmqrl arehgghpvq qpelpqqlps vpqpslpgpq
      241 prpvlgstlp lplppdhapg svaqspgtlg afadvlvrce vsrvllllll qpppakllpe
      301 haqtlekysw eafdghgqds sgqlpeelfl llqslvmaah ekdtegikkl qvemwpllta
      361 eqnhllhlvl qetispsgqg v
//
LOCUS       NP_113846                625 aa            linear   ROD 27-APR-2025
DEFINITION  mesothelin precursor [Rattus norvegicus].
ACCESSION   NP_113846
VERSION     NP_113846.1
DBSOURCE    REFSEQ: accession NM_031658.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Yin,D.D., You,L.H., Yuan,Q.X., Liang,X.D., Wang,N., Wang,L.T.,
            Yuan,L., Wang,K.M. and De,W.
  TITLE     Mesothelin promotes cell proliferation in the remodeling of
            neonatal rat pancreas
  JOURNAL   World J Gastroenterol 20 (22), 6884-6896 (2014)
   PUBMED   24944479
  REMARK    GeneRIF: Mesothelin may have an important role in the remodeling of
            the endocrine pancreas in neonatal rats.
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Takata,A., Yamauchi,H., Toya,T., Miyamoto-Kohno,S., Iwatatsu,Y.,
            Teranaka,I., Aminaka,M., Yamashita,K. and Kohyama,N.
  TITLE     Effectiveness of serum megakaryocyte potentiating factor in
            evaluating the effects of chrysotile and its heated products on
            respiratory organs
  JOURNAL   Toxicol Appl Pharmacol 252 (2), 123-129 (2011)
   PUBMED   20933535
  REMARK    GeneRIF: Megakaryocyte potentiating factor is a useful serum
            biomarker for the effects of chrysotile exposure on respiratory
            organs.
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Fukamachi,K., Tanaka,H., Hagiwara,Y., Ohara,H., Joh,T., Iigo,M.,
            Alexander,D.B., Xu,J., Long,N., Takigahira,M., Yanagihara,K.,
            Hino,O., Saito,I. and Tsuda,H.
  TITLE     An animal model of preclinical diagnosis of pancreatic ductal
            adenocarcinomas
  JOURNAL   Biochem Biophys Res Commun 390 (3), 636-641 (2009)
   PUBMED   19818733
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Johnston,F.M., Tan,M.C., Tan,B.R. Jr., Porembka,M.R., Brunt,E.M.,
            Linehan,D.C., Simon,P.O. Jr., Plambeck-Suess,S., Eberlein,T.J.,
            Hellstrom,K.E., Hellstrom,I., Hawkins,W.G. and Goedegebuure,P.
  TITLE     Circulating mesothelin protein and cellular antimesothelin immunity
            in patients with pancreatic cancer
  JOURNAL   Clin Cancer Res 15 (21), 6511-6518 (2009)
   PUBMED   19843662
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Zhao,H., Davydova,L., Mandich,D., Cartun,R.W. and Ligato,S.
  TITLE     S100A4 protein and mesothelin expression in dysplasia and carcinoma
            of the extrahepatic bile duct
  JOURNAL   Am J Clin Pathol 127 (3), 374-379 (2007)
   PUBMED   17276942
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Jhala,N., Jhala,D., Vickers,S.M., Eltoum,I., Batra,S.K., Manne,U.,
            Eloubeidi,M., Jones,J.J. and Grizzle,W.E.
  TITLE     Biomarkers in Diagnosis of pancreatic carcinoma in fine-needle
            aspirates
  JOURNAL   Am J Clin Pathol 126 (4), 572-579 (2006)
   PUBMED   17019794
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Hassan,R., Laszik,Z.G., Lerner,M., Raffeld,M., Postier,R. and
            Brackett,D.
  TITLE     Mesothelin is overexpressed in pancreaticobiliary adenocarcinomas
            but not in normal pancreas and chronic pancreatitis
  JOURNAL   Am J Clin Pathol 124 (6), 838-845 (2005)
   PUBMED   16416732
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Sato,N., Maitra,A., Fukushima,N., van Heek,N.T., Matsubayashi,H.,
            Iacobuzio-Donahue,C.A., Rosty,C. and Goggins,M.
  TITLE     Frequent hypomethylation of multiple genes overexpressed in
            pancreatic ductal adenocarcinoma
  JOURNAL   Cancer Res 63 (14), 4158-4166 (2003)
   PUBMED   12874021
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Yamashita,Y., Yokoyama,M., Kobayashi,E., Takai,S. and Hino,O.
  TITLE     Mapping and determination of the cDNA sequence of the Erc gene
            preferentially expressed in renal cell carcinoma in the Tsc2 gene
            mutant (Eker) rat model
  JOURNAL   Biochem Biophys Res Commun 275 (1), 134-140 (2000)
   PUBMED   10944454
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D87351.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D87351.1, BC070934.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132301,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Rattus norvegicus"
                     /strain="Eker rat"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..625
                     /product="mesothelin precursor"
                     /note="protein expressed in renal carcinoma;
                     pre-pro-megakaryocyte-potentiating factor; ERC/mesothelin"
                     /calculated_mol_wt=65188
     Region          1..624
                     /region_name="Mesothelin"
                     /note="Pre-pro-megakaryocyte potentiating factor precursor
                     (Mesothelin); pfam06060"
                     /db_xref="CDD:368727"
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERA7.2)"
                     /calculated_mol_wt=3683
     mat_peptide     36..600
                     /product="Mesothelin. /id=PRO_0000253566"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERA7.2)"
                     /calculated_mol_wt=62652
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13421; propagated from
                     UniProtKB/Swiss-Prot (Q9ERA7.2)"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERA7.2)"
     Site            488
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERA7.2)"
     Site            517
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERA7.2)"
     CDS             1..625
                     /gene="Msln"
                     /coded_by="NM_031658.1:91..1968"
                     /db_xref="GeneID:60333"
                     /db_xref="RGD:69333"
ORIGIN      
        1 malptaqpll gscgspicsr sflllllslg wlpllqtqtt rtsqeaallh avtgtvdfas
       61 lptglflglt cdevsglsmg hakelamavr qknivlqvhq lrclarrlpk hltneeldal
      121 pldlllflnp amfpgqqaca hffsliskan vnvlprrsle rqrlltgalk cqgvygfqvs
      181 etdaralggl acdlpgefva kssevllpwl arcggpldqg qakavrevlr sgrapygpps
      241 twsvstldal qgllvvldes ivhsipkdvi tewlqgisre psrlgskwtv thprfrrdte
      301 qkacppgkep nvvdenlify qnweleacvd gtllagqmdl vneipftyeq lsifkhkldk
      361 typqgypesl ikqlghffry vspedirqwn vtspdtvntl lkvskgqkmd aqvialvacy
      421 lrgggklded ivkaldnipl sylcdfspqd lhaipssvmw lvglhdldkc sqrhlgilyq
      481 kacsafqnvs gleyfekirt flggasredl ralsqhnvsm diatfkklqv dalvglsvae
      541 vqkllgphig dlkteedksp vrdwlfrqqq kdldslglgl qggipngyli ldfnvreafs
      601 sgapllgpgf vfawipalls alrls
//
LOCUS       NP_001012071             248 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione S-transferase omega-2 [Rattus norvegicus].
ACCESSION   NP_001012071 XP_006231651 XP_219980
VERSION     NP_001012071.1
DBSOURCE    REFSEQ: accession NM_001012071.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Polimanti,R., Piacentini,S., Moscatelli,B., Pellicciotti,L.,
            Manfellotto,D. and Fuciarelli,M.
  TITLE     GSTA1, GSTO1 and GSTO2 gene polymorphisms in Italian asthma
            patients
  JOURNAL   Clin Exp Pharmacol Physiol 37 (8), 870-872 (2010)
   PUBMED   20374258
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Wahner,A.D., Glatt,C.E., Bronstein,J.M. and Ritz,B.
  TITLE     Glutathione S-transferase mu, omega, pi, and theta class variants
            and smoking in Parkinson's disease
  JOURNAL   Neurosci Lett 413 (3), 274-278 (2007)
   PUBMED   17194543
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ozturk,A., Desai,P.P., Minster,R.L., Dekosky,S.T. and Kamboh,M.I.
  TITLE     Three SNPs in the GSTO1, GSTO2 and PRSS11 genes on chromosome 10
            are not associated with age-at-onset of Alzheimer's disease
  JOURNAL   Neurobiol Aging 26 (8), 1161-1165 (2005)
   PUBMED   15917099
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Schmuck,E.M., Board,P.G., Whitbread,A.K., Tetlow,N.,
            Cavanaugh,J.A., Blackburn,A.C. and Masoumi,A.
  TITLE     Characterization of the monomethylarsonate reductase and
            dehydroascorbate reductase activities of Omega class glutathione
            transferase variants: implications for arsenic metabolism and the
            age-at-onset of Alzheimer's and Parkinson's diseases
  JOURNAL   Pharmacogenet Genomics 15 (7), 493-501 (2005)
   PUBMED   15970797
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Li,Y.J., Oliveira,S.A., Xu,P., Martin,E.R., Stenger,J.E.,
            Scherzer,C.R., Hauser,M.A., Scott,W.K., Small,G.W., Nance,M.A.,
            Watts,R.L., Hubble,J.P., Koller,W.C., Pahwa,R., Stern,M.B.,
            Hiner,B.C., Jankovic,J., Goetz,C.G., Mastaglia,F., Middleton,L.T.,
            Roses,A.D., Saunders,A.M., Schmechel,D.E., Gullans,S.R.,
            Haines,J.L., Gilbert,J.R., Vance,J.M., Pericak-Vance,M.A.,
            Hulette,C. and Welsh-Bohmer,K.A.
  TITLE     Glutathione S-transferase omega-1 modifies age-at-onset of
            Alzheimer disease and Parkinson disease
  JOURNAL   Hum Mol Genet 12 (24), 3259-3267 (2003)
   PUBMED   14570706
  REMARK    Erratum:[Hum Mol Genet. 2004 Mar 1;13(5):573]
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Strange,R.C., Jones,P.W. and Fryer,A.A.
  TITLE     Glutathione S-transferase: genetics and role in toxicology
  JOURNAL   Toxicol Lett 112-113, 357-363 (2000)
   PUBMED   10720752
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079295.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006231651.1, XP_219980.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079295.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..248
                     /product="glutathione S-transferase omega-2"
                     /EC_number="2.5.1.18"
                     /EC_number="1.8.5.1"
                     /EC_number="1.20.4.2"
                     /note="GSTO-2; MMA(V) reductase; monomethylarsonic acid
                     reductase; glutathione S-transferase omega 2-2;
                     glutathione-dependent dehydroascorbate reductase"
                     /calculated_mol_wt=28548
     Region          7..94
                     /region_name="GST_N_Omega"
                     /note="GST_N family, Class Omega subfamily; GSTs are
                     cytosolic dimeric proteins involved in cellular
                     detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of endogenous and
                     xenobiotic alkylating agents, including carcinogens;
                     cd03055"
                     /db_xref="CDD:239353"
     Site            order(7..8,29..31,33,36..37,39..41,43..44,55,57)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239353"
     Site            order(32,34,59,71..73,85..86)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:239353"
     Site            32
                     /site_type="active"
                     /note="active site cysteine [active]"
                     /db_xref="CDD:239353"
     Site            order(71,84..85,87..88,91)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239353"
     Region          108..230
                     /region_name="GST_C_Omega"
                     /note="C-terminal, alpha helical domain of Class Omega
                     Glutathione S-transferases; cd03184"
                     /db_xref="CDD:198293"
     Site            order(114..115,118..119,122,153)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198293"
     Site            order(121,124..125,128..129,181,184,223)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198293"
     Site            order(173,176..177,180,183..184,212,216,226,230)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198293"
     CDS             1..248
                     /gene="Gsto2"
                     /gene_synonym="GSTO 2-2"
                     /coded_by="NM_001012071.1:499..1245"
                     /db_xref="GeneID:309465"
                     /db_xref="RGD:1310764"
ORIGIN      
        1 msgdltrclg kgscppgpvp egviriysmr fcpyshrtrl vlkaksirhe iininlknkp
       61 dwyytkhpfg qvpvlensqc qliyesviac eylddvfpgr klfpydpyer arqkmllelf
      121 ckvpqlskec lvalrcgrdc tdlkvalrqe lcnleeiley qnttffggds ismidylvwp
      181 wferldvygl adcvnhtpml rlwissmkqd pavcalhidk niflgflnly fqnnpcafdf
      241 glcgpivr
//
LOCUS       NP_001013267            1194 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DHX30 [Rattus norvegicus].
ACCESSION   NP_001013267 XP_345986
VERSION     NP_001013267.1
DBSOURCE    REFSEQ: accession NM_001013249.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Lessel,D., Schob,C., Kury,S., Reijnders,M.R.F., Harel,T.,
            Eldomery,M.K., Coban-Akdemir,Z., Denecke,J., Edvardson,S.,
            Colin,E., Stegmann,A.P.A., Gerkes,E.H., Tessarech,M., Bonneau,D.,
            Barth,M., Besnard,T., Cogne,B., Revah-Politi,A., Strom,T.M.,
            Rosenfeld,J.A., Yang,Y., Posey,J.E., Immken,L., Oundjian,N.,
            Helbig,K.L., Meeks,N., Zegar,K., Morton,J., Schieving,J.H.,
            Claasen,A., Huentelman,M., Narayanan,V., Ramsey,K., Brunner,H.G.,
            Elpeleg,O., Mercier,S., Bezieau,S., Kubisch,C., Kleefstra,T.,
            Kindler,S., Lupski,J.R. and Kreienkamp,H.J.
  CONSRTM   DDD study; C4RCD Research Group
  TITLE     De Novo Missense Mutations in DHX30 Impair Global Translation and
            Cause a Neurodevelopmental Disorder
  JOURNAL   Am J Hum Genet 101 (5), 716-724 (2017)
   PUBMED   29100085
  REMARK    Erratum:[Am J Hum Genet. 2018 Jan 4;102(1):196. doi:
            10.1016/j.ajhg.2017.12.016. PMID: 29304375]
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Antonicka,H. and Shoubridge,E.A.
  TITLE     Mitochondrial RNA Granules Are Centers for Posttranscriptional RNA
            Processing and Ribosome Biogenesis
  JOURNAL   Cell Rep 10 (6), 920-932 (2015)
   PUBMED   25683715
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Zheng,H.J., Tsukahara,M., Liu,E., Ye,L., Xiong,H., Noguchi,S.,
            Suzuki,K. and Ji,Z.S.
  TITLE     The novel helicase helG (DHX30) is expressed during gastrulation in
            mice and has a structure similar to a human DExH box helicase
  JOURNAL   Stem Cells Dev 24 (3), 372-383 (2015)
   PUBMED   25219788
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Watanabe,A., Tatematsu,M., Saeki,K., Shibata,S., Shime,H.,
            Yoshimura,A., Obuse,C., Seya,T. and Matsumoto,M.
  TITLE     Raftlin is involved in the nucleocapture complex to induce
            poly(I:C)-mediated TLR3 activation
  JOURNAL   J Biol Chem 286 (12), 10702-10711 (2011)
   PUBMED   21266579
REFERENCE   7  (residues 1 to 1194)
  AUTHORS   Ye,P., Liu,S., Zhu,Y., Chen,G. and Gao,G.
  TITLE     DEXH-Box protein DHX30 is required for optimal function of the
            zinc-finger antiviral protein
  JOURNAL   Protein Cell 1 (10), 956-964 (2010)
   PUBMED   21204022
REFERENCE   8  (residues 1 to 1194)
  AUTHORS   Bogenhagen,D.F., Rousseau,D. and Burke,S.
  TITLE     The layered structure of human mitochondrial DNA nucleoids
  JOURNAL   J Biol Chem 283 (6), 3665-3675 (2008)
   PUBMED   18063578
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091359.1.
            
            On Apr 20, 2005 this sequence version replaced XP_345986.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091359.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1194
                     /product="ATP-dependent RNA helicase DHX30"
                     /EC_number="3.6.4.13"
                     /note="putative ATP-dependent RNA helicase DHX30; DEAH box
                     protein 30; DEAH (Asp-Glu-Ala-His) box polypeptide 30;
                     DEAH (Asp-Glu-Ala-His) box helicase 30; DEAH-box helicase
                     30"
                     /calculated_mol_wt=133867
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L2E3; propagated from
                     UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Region          153..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L2E3; propagated from
                     UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Region          426..>958
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          559..562
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJS0.1)"
     Region          1015..1102
                     /region_name="OB_NTP_bind"
                     /note="Oligonucleotide/oligosaccharide-binding (OB)-fold;
                     pfam07717"
                     /db_xref="CDD:400182"
     CDS             1..1194
                     /gene="Dhx30"
                     /coded_by="NM_001013249.1:170..3754"
                     /db_xref="GeneID:367172"
                     /db_xref="RGD:1308888"
ORIGIN      
        1 mftldsfrkd rtqhrqrqck lppprlppmc vnpapggtis rasrdllkef pqpknllnsv
       61 igralgisha kdklvyvhtn gpkkkkvtlh ikwpksveve gygskkidae rqaaaaacql
      121 fkgwgllgpr nelfdaakyr vladrfgspa dswwrpeptm pptswrqlnp enirpagtgg
      181 lsrslgreee edeeeeleeg tidvteflsm tqqdshnplr dsrggsfemt dddsairalt
      241 qfplpknlla kviqiatsss taknlmqfht vgtktklatl tllwpcpmtf vakgrrkaea
      301 enkaaalack klkslglvdr nneplthamy nlaslrelge tqrrpctiqv pepilrkiea
      361 flshypvdss wispelrlqs ddilplgkds gplsdpitgk pymplseaee vrlsqsllel
      421 wrrrgpiwqe apqlpvdphr dtilsaieqh pvvvisgdtg cgkttripql lleryvtegr
      481 garcnviitq prrisavsva qrvshelgps lrrnvgfqvr leskppargg allfctvgil
      541 lrklqsnpsl egvshvivde vherdvntdf llillkglqr lnpalrlvlm satgdnerfs
      601 ryfggcpvik vpgfmypvke hyledilakl gkhqyphrhr hhesedecal dldlvtdlvl
      661 hidargepgg ilcflpgwqe ikgvqqrlqe algmheskyl ilpvhsnipm mdqkaifqqp
      721 plgvrkivla tniaetsitv ndivhvvdsg lhkeerydlk tkvscletvw vsranviqrr
      781 gragrcqsgf ayhlfprsrl ekmvpfqvpe ilrtplenlv lqakihmpek taveflskav
      841 dspnikavde avillqeigv ldqreylttl gqrlahistd prlakaivla aifrclhpll
      901 vvvscltrdp fssslqnrae vdkvkallsh dsgsdhlafv ravagweevl rwqdrtsren
      961 yleenllyap slrfihglik qfseniyeaf lvgkpsdctl psaqcneyse eeelvkgvlm
     1021 aglypnliqv rqgkvtrqgk fkpnsvtyrt ksgnillhks tinreatrlr srwltyfmav
     1081 ksngsvfvrd ssqvhplavl lltdgdvhir ddgrratisl sdsdllrleg dsrtvrllre
     1141 lrralgrmve rslrselaal plsvqqehgq llallaellr gpcgsfdvrk tadd
//
LOCUS       NP_067088                635 aa            linear   ROD 27-APR-2025
DEFINITION  MAGUK p55 subfamily member 4 [Rattus norvegicus].
ACCESSION   NP_067088
VERSION     NP_067088.2
DBSOURCE    REFSEQ: accession NM_021265.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Aartsen,W.M., Kantardzhieva,A., Klooster,J., van Rossum,A.G., van
            de Pavert,S.A., Versteeg,I., Cardozo,B.N., Tonagel,F., Beck,S.C.,
            Tanimoto,N., Seeliger,M.W. and Wijnholds,J.
  TITLE     Mpp4 recruits Psd95 and Veli3 towards the photoreceptor synapse
  JOURNAL   Hum Mol Genet 15 (8), 1291-1302 (2006)
   PUBMED   16520334
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Kantardzhieva,A., Gosens,I., Alexeeva,S., Punte,I.M., Versteeg,I.,
            Krieger,E., Neefjes-Mol,C.A., den Hollander,A.I., Letteboer,S.J.,
            Klooster,J., Cremers,F.P., Roepman,R. and Wijnholds,J.
  TITLE     MPP5 recruits MPP4 to the CRB1 complex in photoreceptors
  JOURNAL   Invest Ophthalmol Vis Sci 46 (6), 2192-2201 (2005)
   PUBMED   15914641
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Conte,I., Lestingi,M., den Hollander,A., Miano,M.G., Alfano,G.,
            Circolo,D., Pugliese,M., Testa,F., Simonelli,F., Rinaldi,E.,
            Baiget,M., Banfi,S. and Ciccodicola,A.
  TITLE     Characterization of MPP4, a gene highly expressed in photoreceptor
            cells, and mutation analysis in retinitis pigmentosa
  JOURNAL   Gene 297 (1-2), 33-38 (2002)
   PUBMED   12384283
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Inagaki,H., Maeda,S., Lin,K.H., Shimizu,N. and Saito,T.
  TITLE     rDLG6: a novel homolog of Drosophila DLG expressed in rat brain
  JOURNAL   Biochem Biophys Res Commun 265 (2), 462-468 (1999)
   PUBMED   10558890
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Oct 16, 2007 this sequence version replaced NP_067088.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..635
                     /product="MAGUK p55 subfamily member 4"
                     /note="discs large homolog 6; rDLG6; membrane protein,
                     palmitoylated 4 (MAGUK p55 subfamily member 4); membrane
                     palmitoylated protein 4"
                     /calculated_mol_wt=71856
     Region          <47..82
                     /region_name="L27"
                     /note="domain in receptor targeting proteins Lin-2 and
                     Lin-7; smart00569"
                     /db_xref="CDD:197794"
     Region          89..135
                     /region_name="L27"
                     /note="L27 domain; pfam02828"
                     /db_xref="CDD:460717"
     Region          154..232
                     /region_name="PDZ_MPP3-MPP4-MPP7-like"
                     /note="PDZ domain of membrane palmitoylated proteins 3
                     (MPP3), MPP4, and MPP7, and related domains; cd06799"
                     /db_xref="CDD:467260"
     Site            order(162..168,179,182,212,216,219..220)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467260"
     Region          245..305
                     /region_name="SH3_MPP4"
                     /note="Src Homology 3 domain of Membrane Protein,
                     Palmitoylated 4 (or MAGUK p55 subfamily member 4);
                     cd12034"
                     /db_xref="CDD:212967"
     Site            order(247,271..272)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212967"
     Site            order(250,252,255,266,284..285,302,304..305)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212967"
     Region          427..617
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..635
                     /gene="Mpp4"
                     /gene_synonym="Dlg6"
                     /coded_by="NM_021265.3:1..1908"
                     /db_xref="GeneID:58808"
                     /db_xref="RGD:620016"
ORIGIN      
        1 mrqsdrgael tdedralsta pnpenglsgi lrlllqelsl fysrdvhglc llydllhspw
       61 lqallkvydc lqkfkekklv patthaqils cevlellpka ssspeiqelr qvlqaphcka
      121 llrahdtvaq kdfepllppl pdnipdseea mrtvclvknq qplgatikrh eitgdilvar
      181 vihgglvers gllyagdklv evngvpvegl dpeqvihila mscgtimfkv ipvsappvss
      241 qttvyvrami dywpqedpdi pcmdaglpfl kgdilqivdq sdalwwqark isdlaicagl
      301 ipsnhllkrk qrefwwsqpy qphtclkstr slsveeedsm kidekcvead eetfeseela
      361 eakeefvgdg qqffiagfrr smrlcrrksh fsqlhanmrc tcscysavga pyeevvryqr
      421 qpadkhrliv lvgpsgvgvn elrrqligcn pscfqsavph ttrspksyem dgreyhyvsr
      481 etfeslmygh rmlefgeykg hlygtsvnav lavldegkic vmdlepqdiq lartrelkpy
      541 vifikppsms smrhsrrnak iitdyfvdmk fkdedlqeme elaqkmesqf gqffdhvivn
      601 dnlqdaraql lsaiqkaeee lqwvpeawvs pgaes
//
LOCUS       NP_476489                361 aa            linear   ROD 27-APR-2025
DEFINITION  septin-2 [Rattus norvegicus].
ACCESSION   NP_476489
VERSION     NP_476489.1
DBSOURCE    REFSEQ: accession NM_057148.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Kuo,Y.C., Shen,Y.R., Chen,H.I., Lin,Y.H., Wang,Y.Y., Chen,Y.R.,
            Wang,C.Y. and Kuo,P.L.
  TITLE     SEPT12 orchestrates the formation of mammalian sperm annulus by
            organizing core octameric complexes with other SEPT proteins
  JOURNAL   J Cell Sci 128 (5), 923-934 (2015)
   PUBMED   25588830
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Lu,Y., Cai,G., Cui,S., Geng,W., Chen,D., Wen,J., Zhang,Y.,
            Zhang,F., Xie,Y., Fu,B. and Chen,X.
  TITLE     FHL2-driven molecular network mediated Septin2 knockdown inducing
            apoptosis in mesangial cell
  JOURNAL   Proteomics 14 (21-22), 2485-2497 (2014)
   PUBMED   25103794
  REMARK    GeneRIF: This study illustrated the FHL2-driven molecular network
            controlling SEPT2-mediated apoptosis in mesangial cell and their
            potential roles in mesangial proliferative nephritis.
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Cui,C., Chatterjee,B., Lozito,T.P., Zhang,Z., Francis,R.J.,
            Yagi,H., Swanhart,L.M., Sanker,S., Francis,D., Yu,Q., San
            Agustin,J.T., Puligilla,C., Chatterjee,T., Tansey,T., Liu,X.,
            Kelley,M.W., Spiliotis,E.T., Kwiatkowski,A.V., Tuan,R.,
            Pazour,G.J., Hukriede,N.A. and Lo,C.W.
  TITLE     Wdpcp, a PCP protein required for ciliogenesis, regulates
            directional cell migration and cell polarity by direct modulation
            of the actin cytoskeleton
  JOURNAL   PLoS Biol 11 (11), e1001720 (2013)
   PUBMED   24302887
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Ghossoub,R., Hu,Q., Failler,M., Rouyez,M.C., Spitzbarth,B.,
            Mostowy,S., Wolfrum,U., Saunier,S., Cossart,P., Jamesnelson,W. and
            Benmerah,A.
  TITLE     Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the
            primary cilium and control ciliary length
  JOURNAL   J Cell Sci 126 (Pt 12), 2583-2594 (2013)
   PUBMED   23572511
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Kinoshita,N., Kimura,K., Matsumoto,N., Watanabe,M., Fukaya,M. and
            Ide,C.
  TITLE     Mammalian septin Sept2 modulates the activity of GLAST, a glutamate
            transporter in astrocytes
  JOURNAL   Genes Cells 9 (1), 1-14 (2004)
   PUBMED   14723703
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Vega,I.E. and Hsu,S.C.
  TITLE     The septin protein Nedd5 associates with both the exocyst complex
            and microtubules and disruption of its GTPase activity promotes
            aberrant neurite sprouting in PC12 cells
  JOURNAL   Neuroreport 14 (1), 31-37 (2003)
   PUBMED   12544826
  REMARK    GeneRIF: Nedd5 may be required for polarized neurite outgrowth,
            perhaps, by facilitating the exocyst complex function during
            neuronal differentiation.
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Peng,X.R., Jia,Z., Zhang,Y., Ware,J. and Trimble,W.S.
  TITLE     The septin CDCrel-1 is dispensable for normal development and
            neurotransmitter release
  JOURNAL   Mol Cell Biol 22 (1), 378-387 (2002)
   PUBMED   11739749
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Beites,C.L., Xie,H., Bowser,R. and Trimble,W.S.
  TITLE     The septin CDCrel-1 binds syntaxin and inhibits exocytosis
  JOURNAL   Nat Neurosci 2 (5), 434-439 (1999)
   PUBMED   10321247
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081745.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..361
                     /product="septin-2"
                     /note="vascular endothelial cell specific protein 11"
                     /calculated_mol_wt=41462
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P42208; propagated from
                     UniProtKB/Swiss-Prot (Q91Y81.1)"
     Region          35..306
                     /region_name="Septin"
                     /note="pfam00735"
                     /db_xref="CDD:395596"
     Region          44..51
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            44..51
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(46..52,101,104,182..183,185,241..242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            76..84
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            78
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          101..104
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            101..104
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(103..138,139..148)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            156
                     /site_type="other"
                     /note="Important for dimerization. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q91Y81.1)"
     Region          182..185
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            182..185
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q15019; propagated from
                     UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q15019; propagated from
                     UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91Y81.1)"
     Site            241..243
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Region          260..270
                     /region_name="Important for dimerization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91Y81.1)"
     CDS             1..361
                     /gene="Septin2"
                     /gene_synonym="Nedd5; Sept2; Vesp11"
                     /coded_by="NM_057148.2:66..1151"
                     /db_xref="GeneID:117515"
                     /db_xref="RGD:620056"
ORIGIN      
        1 mskqqptqfi npetpgyvgf anlpnqvhrk svkkgfeftl mvvgesglgk stlinslflt
       61 dlyperiipg aaekiertvq ieastveiee rgvklrltvv dtpgygdain srdcfktiis
      121 yideqferyl hdesglnrrh iidnrvhccf yfispfghgl kpldvafmka ihnkvnivpv
      181 iakadtltlk ererlkkril deieehsiki yhlpdaesde dedfkeqtrl lkasipfsvv
      241 gsnqlieakg kkvrgrlypw gvvevenpeh ndflklrtml ithmqdlqev tqdlhyenfr
      301 serlkrggrk venedmnkdq illekeaelr rmqemiarmq aqmqmqmqgg dtdsstlghh
      361 v
//
LOCUS       NP_001032363             415 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein F [Rattus norvegicus].
ACCESSION   NP_001032363
VERSION     NP_001032363.1
DBSOURCE    REFSEQ: accession NM_001037286.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Lo,C.S., Shi,Y., Chenier,I., Ghosh,A., Wu,C.H., Cailhier,J.F.,
            Ethier,J., Lattouf,J.B., Filep,J.G., Ingelfinger,J.R., Zhang,S.L.
            and Chan,J.S.D.
  TITLE     Heterogeneous Nuclear Ribonucleoprotein F Stimulates Sirtuin-1 Gene
            Expression and Attenuates Nephropathy Progression in Diabetic Mice
  JOURNAL   Diabetes 66 (7), 1964-1978 (2017)
   PUBMED   28424160
  REMARK    GeneRIF: hnRNP F protects kidneys against oxidative stress and
            nephropathy via stimulation of Sirtuin-1 expression and signaling
            in diabetes.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dominguez,C., Fisette,J.F., Chabot,B. and Allain,F.H.
  TITLE     Structural basis of G-tract recognition and encaging by hnRNP F
            quasi-RRMs
  JOURNAL   Nat Struct Mol Biol 17 (7), 853-861 (2010)
   PUBMED   20526337
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Wei,C.C., Zhang,S.L., Chen,Y.W., Guo,D.F., Ingelfinger,J.R.,
            Bomsztyk,K. and Chan,J.S.
  TITLE     Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen
            gene expression in kidney cells
  JOURNAL   J Biol Chem 281 (35), 25344-25355 (2006)
   PUBMED   16837467
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Wei,C.C., Guo,D.F., Zhang,S.L., Ingelfinger,J.R. and Chan,J.S.
  TITLE     Heterogenous nuclear ribonucleoprotein F modulates angiotensinogen
            gene expression in rat kidney proximal tubular cells
  JOURNAL   J Am Soc Nephrol 16 (3), 616-628 (2005)
   PUBMED   15659559
  REMARK    GeneRIF: hnRNP F binds to rANG-IRE and modulates renal ANG gene
            expression, implicating that dysregulation of hnRNP F might affect
            renin-angiotensin system activation and, subsequently, kidney
            injury in diabetes
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Yoshida,T., Makino,Y. and Tamura,T.
  TITLE     Association of the rat heterogeneous nuclear RNA-ribonucleoprotein
            F with TATA-binding protein
  JOURNAL   FEBS Lett 457 (2), 251-254 (1999)
   PUBMED   10471789
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Gamberi,C., Izaurralde,E., Beisel,C. and Mattaj,I.W.
  TITLE     Interaction between the human nuclear cap-binding protein complex
            and hnRNP F
  JOURNAL   Mol Cell Biol 17 (5), 2587-2597 (1997)
   PUBMED   9111328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK359545.1 and BC103634.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK359545.1, EV769167.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..415
                     /product="heterogeneous nuclear ribonucleoprotein F"
                     /note="hnRNP F; ribonucleoprotein F"
                     /calculated_mol_wt=45599
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein F, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            16
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            20
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            52
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            75
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          81..86
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            116
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            120
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            150
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            173
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          179..184
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X1; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          255..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          289..363
                     /region_name="RRM3_hnRNPH_CRSF1_like"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H protein
                     family, G-rich sequence factor 1 (GRSF-1) and similar
                     proteins; cd12506"
                     /db_xref="CDD:409929"
     Site            294
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            298
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            326
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            349
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          355..360
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     CDS             1..415
                     /gene="Hnrnpf"
                     /gene_synonym="Hnrpf"
                     /coded_by="NM_001037286.1:365..1612"
                     /db_xref="GeneID:64200"
                     /db_xref="RGD:620366"
ORIGIN      
        1 mmlgpeggeg yvvklrglpw scsiedvqnf lsdctihdgv agvhfiytre grqsgeafve
       61 leseddvkla lkkdresmgh ryievfkshr temdwvlkhs gpnsadsand gfvrlrglpf
      121 gctkeeivqf fsgleivpng itlpvdpegk itgeafvqfa sqelaekalg khkerighry
      181 ievfkssqee vrsysdpplk fmsvqrpgpy drpgtarryi givkqagldr mrsgaysagy
      241 ggyeeysgls dgygfttdlf grdlsyclsg mydhrygdse ftvqsttghc vhmrglpyka
      301 tendiynffs plnpvrvhie igpdgrvtge advefathee avaamskdra nmqhryielf
      361 lnsttgasng ayssqvmqgm gvsaaqatys glesqsvsgc ygagysgqns mggyd
//
LOCUS       NP_001028842             233 aa            linear   ROD 27-APR-2025
DEFINITION  bcl-2-like protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001028842
VERSION     NP_001028842.1
DBSOURCE    REFSEQ: accession NM_001033670.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Perez-Serna,A.A., Dos Santos,R.S., Ripoll,C., Nadal,A.,
            Eizirik,D.L. and Marroqui,L.
  TITLE     BCL-XL Overexpression Protects Pancreatic beta-Cells against
            Cytokine- and Palmitate-Induced Apoptosis
  JOURNAL   Int J Mol Sci 24 (6), 5657 (2023)
   PUBMED   36982731
  REMARK    GeneRIF: BCL-XL Overexpression Protects Pancreatic beta-Cells
            against Cytokine- and Palmitate-Induced Apoptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Alam,M. and Mishra,R.
  TITLE     Bcl-xL expression and regulation in the progression, recurrence,
            and cisplatin resistance of oral cancer
  JOURNAL   Life Sci 280, 119705 (2021)
   PUBMED   34111459
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Rozier,R., Paul,R., Madji Hounoum,B., Villa,E., Mhaidly,R.,
            Chiche,J., Verhoeyen,E., Marchetti,S., Vandenberghe,A.,
            Raucoules,M., Carles,M. and Ricci,J.E.
  TITLE     Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism
  JOURNAL   FEBS J 288 (11), 3547-3569 (2021)
   PUBMED   33340237
  REMARK    GeneRIF: Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Liang,J.R. and Yang,H.
  TITLE     Ginkgolic acid (GA) suppresses gastric cancer growth by inducing
            apoptosis and suppressing STAT3/JAK2 signaling regulated by ROS
  JOURNAL   Biomed Pharmacother 125, 109585 (2020)
   PUBMED   32106377
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Sadek,K., Abouzed,T., Nasr,S. and Shoukry,M.
  TITLE     Licochalcone B Ameliorates Liver Cancer via Targeting of Apoptotic
            Genes, DNA Repair Systems, and Cell Cycle Control
  JOURNAL   Iran J Pharm Res 19 (4), 372-386 (2020)
   PUBMED   33841550
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Chao,D.T., Linette,G.P., Boise,L.H., White,L.S., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bcl-XL and Bcl-2 repress a common pathway of cell death
  JOURNAL   J Exp Med 182 (3), 821-828 (1995)
   PUBMED   7650488
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Gonzalez-Garcia,M., Garcia,I., Ding,L., O'Shea,S., Boise,L.H.,
            Thompson,C.B. and Nunez,G.
  TITLE     bcl-x is expressed in embryonic and postnatal neural tissues and
            functions to prevent neuronal cell death
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4304-4308 (1995)
   PUBMED   7753802
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Tilly,J.L., Tilly,K.I., Kenton,M.L. and Johnson,A.L.
  TITLE     Expression of members of the bcl-2 gene family in the immature rat
            ovary: equine chorionic gonadotropin-mediated inhibition of
            granulosa cell apoptosis is associated with decreased bax and
            constitutive bcl-2 and bcl-xlong messenger ribonucleic acid levels
  JOURNAL   Endocrinology 136 (1), 232-241 (1995)
   PUBMED   7828536
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Gonzalez-Garcia,M., Perez-Ballestero,R., Ding,L., Duan,L.,
            Boise,L.H., Thompson,C.B. and Nunez,G.
  TITLE     bcl-XL is the major bcl-x mRNA form expressed during murine
            development and its product localizes to mitochondria
  JOURNAL   Development 120 (10), 3033-3042 (1994)
   PUBMED   7607090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC094213.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, 3' UTR,
            and 3' coding sequence compared to variant 1. The resulting isoform
            (2) has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094213.1, SRR8487231.164919.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform 2"
                     /note="bcl-2-like protein 1; B cell lymphoma like X;
                     bcl2-L-1; apoptosis regulator Bcl-X; B cell lymphoma 2
                     like"
                     /calculated_mol_wt=26027
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Region          27..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     CDS             1..233
                     /gene="Bcl2l1"
                     /gene_synonym="bcl-X; Bcl-xl; Bcl2l; Bclx"
                     /coded_by="NM_001033670.1:179..880"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:24888"
                     /db_xref="RGD:2200"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapee teperetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaswm atylndhlep
      181 wiqenggwdt fvdlygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_695222               1044 aa            linear   ROD 27-APR-2025
DEFINITION  suppression of tumorigenicity 18 protein [Rattus norvegicus].
ACCESSION   NP_695222
VERSION     NP_695222.2
DBSOURCE    REFSEQ: accession NM_153310.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Henry,C., Close,A.F. and Buteau,J.
  TITLE     A critical role for the neural zinc factor ST18 in pancreatic
            beta-cell apoptosis
  JOURNAL   J Biol Chem 289 (12), 8413-8419 (2014)
   PUBMED   24509857
  REMARK    GeneRIF: ST18 expression and activity are increased in cytotoxic
            conditions in pancreatic beta-cells. Overexpression of ST18 causes
            apoptosis.
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Yang,J., Siqueira,M.F., Behl,Y., Alikhani,M. and Graves,D.T.
  TITLE     The transcription factor ST18 regulates proapoptotic and
            proinflammatory gene expression in fibroblasts
  JOURNAL   FASEB J 22 (11), 3956-3967 (2008)
   PUBMED   18676404
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Jandrig,B., Seitz,S., Hinzmann,B., Arnold,W., Micheel,B.,
            Koelble,K., Siebert,R., Schwartz,A., Ruecker,K., Schlag,P.M.,
            Scherneck,S. and Rosenthal,A.
  TITLE     ST18 is a breast cancer tumor suppressor gene at human chromosome
            8q11.2
  JOURNAL   Oncogene 23 (57), 9295-9302 (2004)
   PUBMED   15489893
REFERENCE   4  (residues 1 to 1044)
  AUTHORS   Yee,K.S. and Yu,V.C.
  TITLE     Isolation and characterization of a novel member of the neural zinc
            finger factor/myelin transcription factor family with
            transcriptional repression activity
  JOURNAL   J Biol Chem 273 (9), 5366-5374 (1998)
   PUBMED   9478997
REFERENCE   5  (residues 1 to 1044)
  AUTHORS   Bellefroid,E.J., Bourguignon,C., Hollemann,T., Ma,Q.,
            Anderson,D.J., Kintner,C. and Pieler,T.
  TITLE     X-MyT1, a Xenopus C2HC-type zinc finger protein with a regulatory
            function in neuronal differentiation
  JOURNAL   Cell 87 (7), 1191-1202 (1996)
   PUBMED   8980226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U67080.1, AF031942.1 and CO394514.1.
            
            On Oct 13, 2005 this sequence version replaced NP_695222.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U67080.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..1044
                     /product="suppression of tumorigenicity 18 protein"
                     /note="suppression of tumorigenicity protein 18; NZF-3;
                     C2-HC type zinc finger protein r-MyT3; neural zinc finger
                     factor 3; ST18, C2H2C-type zinc finger"
                     /calculated_mol_wt=114453
     Region          364..390
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          408..436
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          477..712
                     /region_name="MYT1"
                     /note="Myelin transcription factor 1; pfam08474"
                     /db_xref="CDD:462489"
     Region          720..748
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          764..792
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          812..840
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          866..892
                     /region_name="zf-C2HC"
                     /note="Zinc finger, C2HC type; pfam01530"
                     /db_xref="CDD:460240"
     Region          887..>1042
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          <920..969
                     /region_name="Atg16_CCD"
                     /note="Coiled-coiled domain of autophagy-related 16
                     (Atg16) family proteins; cl46300"
                     /db_xref="CDD:480640"
     CDS             1..1044
                     /gene="St18"
                     /gene_synonym="Nzf3; r-MyT3"
                     /coded_by="NM_153310.2:141..3275"
                     /db_xref="GeneID:266680"
                     /db_xref="RGD:708566"
ORIGIN      
        1 mdaevedkal htlskgtevp mdslipelrv aydcsmakkr raeeqalgvp vnkrksllmk
       61 prhyspdmdc kenpdnrned dgletndhst adeivvkpmd ktlhlpaqes slpkedqyac
      121 ypelmvkslm hlgkfeeses vqtvgenlng ngiqslkaec deanecfmvh sddgrdkvhh
      181 sqppfcssgd sesdsdnten gwgsgsnsse dtdthkgpkr kltynrkdll evpeikaedd
      241 kfipcenrcd sdtsgrdpqn shmeplavkv qpsfpevees eslatviaes aevekakgsl
      301 slleqaialq aergsvfhht ykeldrflld hlarqrrqpk vtdasgrqif nnkhsprper
      361 reakcpipgc dgtghvtgly phhrslsgcp hkvrvpleil amhenvlkcp tpgctgrghv
      421 nsnrnthrsl sgcpiaaaek lamtqdksql dssqtgqgpe qahrvnlvkq iefnfrsqai
      481 tsprasaske qekfgkvpfd yasfdaqvfg krpllqtgqg qkappfpesk hfsnpvkfsn
      541 glpsagahtq stvrassygh gqysedthia aaaailnlst rcreatdils nkpqslrakg
      601 aeievdengt ldlsmkkhri ldksipptss httiatpsss pfkassllvn aafyqalcdq
      661 egwnvpinys kshgkteeek ekdpvnslen leekkfagea sipspkpklh trdlkkelit
      721 cptpgcdgsg hvtgnyashr svsgcpladk tlkslmaans qelkcptpgc dgsghvtgny
      781 ashrslsgcp rarkggikmt ptkeekedse lrcpvigcdg qghisgkyts hrtasgcpla
      841 akrqkenpln gtplswklnk qelphcplpg cnglghvnnv fvthrslsgc plnaqaikkv
      901 kvseelmtik lkatggiegd eeirhldeei kelnesnlki eadmmklqtq itsmesnlkt
      961 ieeenklieq snesllkela glsqalissl adiqlpqmgp ineqnfeayv ntltdmysnl
     1021 erdyspecka llesikqavk gihv
//
LOCUS       NP_705890                802 aa            linear   ROD 27-APR-2025
DEFINITION  neuronal PAS domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_705890
VERSION     NP_705890.1
DBSOURCE    REFSEQ: accession NM_153626.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Louis Sam Titus,A.S.C., Sharma,D., Kim,M.S. and D'Mello,S.R.
  TITLE     The Bdnf and Npas4 genes are targets of HDAC3-mediated
            transcriptional repression
  JOURNAL   BMC Neurosci 20 (1), 65 (2019)
   PUBMED   31883511
  REMARK    GeneRIF: In healthy cerebellar granule neurons HDAC3 associates
            weakly with the Npas4 promoter, however, this association is
            robustly increased in neurons primed to die. Study found that HDAC3
            also associates differentially with the Bdnfr gene promoter, with
            higher association in dying neurons. Overexpression of HDAC3 leads
            to a suppression of Npas4 and Bdnf expression in cortical neurons.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Wu,H., Huang,Y., Tian,X., Zhang,Z., Zhang,Y., Mao,Y., Wang,C.,
            Yang,S., Liu,Y., Zhang,W. and Ma,Z.
  TITLE     Preoperative anxiety-induced glucocorticoid signaling reduces
            GABAergic markers in spinal cord and promotes postoperative
            hyperalgesia by affecting neuronal PAS domain protein 4
  JOURNAL   Mol Pain 15, 1744806919850383 (2019)
   PUBMED   31041873
  REMARK    GeneRIF: preoperative anxiety led to GABAergic system impairment in
            spinal cord and thus caused hyperalgesia due to
            glucocorticoid-induced downregulation of neuronal PAS domain
            protein 4.
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Greb-Markiewicz,B., Zarebski,M. and Ozyhar,A.
  TITLE     Multiple sequences orchestrate subcellular trafficking of neuronal
            PAS domain-containing protein 4 (NPAS4)
  JOURNAL   J Biol Chem 293 (29), 11255-11270 (2018)
   PUBMED   29899116
  REMARK    GeneRIF: The presence of multiple localization signals and the
            differentiated localization of NPAS4 suggest a precise,
            multifactor-dependent regulation of NPAS4 trafficking, potentially
            crucial for its ability to act as a cellular stress sensor and
            transcription factor.
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Drouet,J.B., Peinnequin,A., Faure,P., Denis,J., Fidier,N.,
            Maury,R., Buguet,A., Cespuglio,R. and Canini,F.
  TITLE     Stress-induced hippocampus Npas4 mRNA expression relates to
            specific psychophysiological patterns of stress response
  JOURNAL   Brain Res 1679, 75-83 (2018)
   PUBMED   29196218
  REMARK    GeneRIF: The main discovery of this study is that the spontaneously
            expressed hippocampus Npas4 mRNA level under stressful conditions
            is associated with differences in hippocampus activation and
            behavior
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Taniguchi,M., Carreira,M.B., Cooper,Y.A., Bobadilla,A.C.,
            Heinsbroek,J.A., Koike,N., Larson,E.B., Balmuth,E.A., Hughes,B.W.,
            Penrod,R.D., Kumar,J., Smith,L.N., Guzman,D., Takahashi,J.S.,
            Kim,T.K., Kalivas,P.W., Self,D.W., Lin,Y. and Cowan,C.W.
  TITLE     HDAC5 and Its Target Gene, Npas4, Function in the Nucleus Accumbens
            to Regulate Cocaine-Conditioned Behaviors
  JOURNAL   Neuron 96 (1), 130-144 (2017)
   PUBMED   28957664
  REMARK    GeneRIF: nuclear histone deacetylase 5 (HDAC5) in the nucleus
            accumbens (NAc) reduced cocaine reward-context associations and
            relapse-like behaviors in a cocaine self-administration model. We
            also discovered that HDAC5 associates with an activity-sensitive
            enhancer of the Npas4 gene and negatively regulates NPAS4
            expression.
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Ooe,N., Kobayashi,K., Motonaga,K., Saito,K. and Kaneko,H.
  TITLE     Dynamic regulation of bHLH-PAS-type transcription factor NXF gene
            expression and neurotrophin dependent induction of the
            transcriptional control activity
  JOURNAL   Biochem Biophys Res Commun 378 (4), 761-765 (2009)
   PUBMED   19083991
  REMARK    GeneRIF: NXF, is a new member genes under the control of
            neurotrophin BDNF.
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Ooe,N., Motonaga,K., Kobayashi,K., Saito,K. and Kaneko,H.
  TITLE     Functional characterization of basic helix-loop-helix-PAS type
            transcription factor NXF in vivo: putative involvement in an 'on
            demand' neuroprotection system
  JOURNAL   J Biol Chem 284 (2), 1057-1063 (2009)
   PUBMED   19001414
  REMARK    GeneRIF: NXF gene could be induced in response to several
            neurodegenerative stimuli/excitations for the cell protection, and
            thus provide an 'on demand' cell-protection system in nervous
            tissue
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Lin,Y., Bloodgood,B.L., Hauser,J.L., Lapan,A.D., Koon,A.C.,
            Kim,T.K., Hu,L.S., Malik,A.N. and Greenberg,M.E.
  TITLE     Activity-dependent regulation of inhibitory synapse development by
            Npas4
  JOURNAL   Nature 455 (7217), 1198-1204 (2008)
   PUBMED   18815592
REFERENCE   9  (residues 1 to 802)
  AUTHORS   Moser,M., Knoth,R., Bode,C. and Patterson,C.
  TITLE     LE-PAS, a novel Arnt-dependent HLH-PAS protein, is expressed in
            limbic tissues and transactivates the CNS midline enhancer element
  JOURNAL   Brain Res Mol Brain Res 128 (2), 141-149 (2004)
   PUBMED   15363889
REFERENCE   10 (residues 1 to 802)
  AUTHORS   Ooe,N., Saito,K., Mikami,N., Nakatuka,I. and Kaneko,H.
  TITLE     Identification of a novel basic helix-loop-helix-PAS factor, NXF,
            reveals a Sim2 competitive, positive regulatory role in
            dendritic-cytoskeleton modulator drebrin gene expression
  JOURNAL   Mol Cell Biol 24 (2), 608-616 (2004)
   PUBMED   14701734
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB050103.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB050103.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132263,
                                           SAMD00132288 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..802
                     /product="neuronal PAS domain-containing protein 4"
                     /note="bHLH-PAS type transcription factor NXF; neuronal
                     PAS4; HLH-PAS transcription factor NXF"
                     /calculated_mol_wt=87187
     Region          1..13
                     /region_name="Basic motif, degenerate.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00981"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJH6.1)"
     Region          2..57
                     /region_name="bHLH-PAS_NPAS4_PASD10"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 4
                     (NPAS4) and similar proteins; cd19697"
                     /db_xref="CDD:381540"
     Site            order(4..6,10,12..13,17,38..39)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381540"
     Region          14..53
                     /region_name="Helix-loop-helix motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00981"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJH6.1)"
     Site            order(15..16,19..20,22..23,40,43,47,49..50,54,56)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381540"
     Region          72..135
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          230..>298
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(232,236,242,255..258,286,291)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Region          472..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJH6.1)"
     CDS             1..802
                     /gene="Npas4"
                     /gene_synonym="Nxf"
                     /coded_by="NM_153626.1:35..2443"
                     /db_xref="GeneID:266734"
                     /db_xref="RGD:628866"
ORIGIN      
        1 myrstkgask arrdqinaei rnlkellpla eadkvrlsyl himslaciyt rkgvffaggt
       61 plagptglls aqeledivaa lpgfllvfta egkllylses vsehlghsmv dlvaqgdsiy
      121 diidpadhlt vrqqltmpsa ldadrlfrcr fntskslrrq sagnklvlir grfhahppga
      181 ywagnpvfta fcapleprpr pgpgpgpgpg paslflamfq srhakdlall disesvliyl
      241 gfersellck swygllhped lahassqhyr llaengdiqa emvvrlqakh ggwtwiycml
      301 ysdgpegpit annypisdte awslrqqlns entqaayvlg tpavlpsfse nvfsqehcsn
      361 plftpalgtp rsasfprape lgvistseel aqpskeldfs ylpfparpep slqadlskdl
      421 vctppytphq pggcaflfsl hepfqthlpp pssslqeqlt pstvtfseql tpssatfpdp
      481 ltsslqgqlt essarsfeeq ltpctstfpd qllpstatfp eplgsptheq ltppstafqa
      541 hlnspsqtfp eqlspnptkt yfaqegcsfl yeklppspss pgngdctlla laqlrgplsv
      601 dvplvpegll tpeaspvkqs ffhytekeqn eidrliqqis qlaqgmdrpf saeagtggle
      661 plggleplnp nlslsgagpp vlsldlkpwk cqeldflvdp dnlfleetpv edifmdlstp
      721 dpngewgsgd peaevpggtl spcnnlsped hsfledlaty etafetgvst fpyegfadel
      781 hqlqsqvqds fhedgsggep tf
//
LOCUS       NP_001011939             534 aa            linear   ROD 27-APR-2025
DEFINITION  EH domain-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001011939 XP_215154
VERSION     NP_001011939.1
DBSOURCE    REFSEQ: accession NM_001011939.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Martins-Marques,T., Catarino,S., Goncalves,A., Miranda-Silva,D.,
            Goncalves,L., Antunes,P., Coutinho,G., Leite Moreira,A., Falcao
            Pires,I. and Girao,H.
  TITLE     EHD1 Modulates Cx43 Gap Junction Remodeling Associated With Cardiac
            Diseases
  JOURNAL   Circ Res 126 (10), e97-e113 (2020)
   PUBMED   32138615
  REMARK    GeneRIF: EHD1 Modulates Cx43 Gap Junction Remodeling Associated
            With Cardiac Diseases.
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Wu,C., Bao,G., Xu,G., Sun,Y., Wang,L., Chen,J., Zhang,J., Chen,C.,
            Zhu,Q. and Cui,Z.
  TITLE     Triad1 regulates the expression and distribution of EHD1
            contributing to the neurite outgrowth of neurons after spinal cord
            injury
  JOURNAL   J Cell Biochem 120 (4), 5355-5366 (2019)
   PUBMED   30320922
  REMARK    GeneRIF: Our data delineate a novel interaction between Triad1 and
            EHD1 that may contribute to the regulation of neurite outgrowth for
            neurons after the spinal cord injury.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Wu,C., Cui,Z., Liu,Y., Zhang,J., Ding,W., Wang,S., Bao,G., Xu,G.,
            Sun,Y. and Chen,J.
  TITLE     The importance of EHD1 in neurite outgrowth contributing to the
            functional recovery after spinal cord injury
  JOURNAL   Int J Dev Neurosci 52, 24-32 (2016)
   PUBMED   27211346
  REMARK    GeneRIF: This study demonstrated that EHD1 was up-regulated in rat
            spinal cord injury model.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Lu,Q., Insinna,C., Ott,C., Stauffer,J., Pintado,P.A., Rahajeng,J.,
            Baxa,U., Walia,V., Cuenca,A., Hwang,Y.S., Daar,I.O., Lopes,S.,
            Lippincott-Schwartz,J., Jackson,P.K., Caplan,S. and Westlake,C.J.
  TITLE     Early steps in primary cilium assembly require EHD1/EHD3-dependent
            ciliary vesicle formation
  JOURNAL   Nat Cell Biol 17 (3), 228-240 (2015)
   PUBMED   25686250
  REMARK    Erratum:[Nat Cell Biol. 2015 Apr;17(4):531. doi: 10.1038/ncb3155.
            PMID: 25812525]
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Gallon,M. and Cullen,P.J.
  TITLE     Retromer and sorting nexins in endosomal sorting
  JOURNAL   Biochem Soc Trans 43 (1), 33-47 (2015)
   PUBMED   25619244
  REMARK    Review article
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Guilherme,A., Soriano,N.A., Furcinitti,P.S. and Czech,M.P.
  TITLE     Role of EHD1 and EHBP1 in perinuclear sorting and insulin-regulated
            GLUT4 recycling in 3T3-L1 adipocytes
  JOURNAL   J Biol Chem 279 (38), 40062-40075 (2004)
   PUBMED   15247266
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Naslavsky,N., Boehm,M., Backlund,P.S. Jr. and Caplan,S.
  TITLE     Rabenosyn-5 and EHD1 interact and sequentially regulate protein
            recycling to the plasma membrane
  JOURNAL   Mol Biol Cell 15 (5), 2410-2422 (2004)
   PUBMED   15020713
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Galperin,E., Benjamin,S., Rapaport,D., Rotem-Yehudar,R.,
            Tolchinsky,S. and Horowitz,M.
  TITLE     EHD3: a protein that resides in recycling tubular and vesicular
            membrane structures and interacts with EHD1
  JOURNAL   Traffic 3 (8), 575-589 (2002)
   PUBMED   12121420
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Lin,S.X., Grant,B., Hirsh,D. and Maxfield,F.R.
  TITLE     Rme-1 regulates the distribution and function of the endocytic
            recycling compartment in mammalian cells
  JOURNAL   Nat Cell Biol 3 (6), 567-572 (2001)
   PUBMED   11389441
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV120970.1, BC082030.1, CO571196.1 and BQ192279.1.
            
            On Feb 11, 2005 this sequence version replaced XP_215154.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160908.1, SRR8487230.65133.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..534
                     /product="EH domain-containing protein 1"
                     /calculated_mol_wt=60472
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4M9; propagated from
                     UniProtKB/Swiss-Prot (Q641Z6.1)"
     Region          24..56
                     /region_name="EHD_N"
                     /note="N-terminal EH-domain containing protein; pfam16880"
                     /db_xref="CDD:465295"
     Region          60..300
                     /region_name="EHD"
                     /note="Eps15 homology domain (EHD), C-terminal domain;
                     cd09913"
                     /db_xref="CDD:206740"
     Region          65..72
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z6.1)"
     Site            65..72
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206740"
     Site            order(70..73,153,220,222,256..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206740"
     Region          91..92
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z6.1)"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206740"
     Site            98..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206740"
     Region          153..156
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z6.1)"
     Site            153..156
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206740"
     Site            order(155..156,183..184)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206740"
     Region          219..222
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z6.1)"
     Site            219..222
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206740"
     Region          243
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z6.1)"
     Site            256..258
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206740"
     Region          288..394
                     /region_name="DUF5600"
                     /note="Domain of unknown function (DUF5600); pfam18150"
                     /db_xref="CDD:465667"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4M9; propagated from
                     UniProtKB/Swiss-Prot (Q641Z6.1)"
     Region          438..531
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q641Z6.1)"
     CDS             1..534
                     /gene="Ehd1"
                     /gene_synonym="RGD1306960"
                     /coded_by="NM_001011939.2:74..1678"
                     /db_xref="GeneID:293692"
                     /db_xref="RGD:1309017"
ORIGIN      
        1 mfswvskdar rkkepelfqt vaeglrqlya qkllpleehy rfhefhspal edadfdnkpm
       61 vllvgqystg kttfirhlie qdfpgmrigp epttdsfiav mhgptegvvp gnalvvdprr
      121 pfrklnafgn aflnrfmcaq lpnpvldsis iidtpgilsg ekqrisrgyd faavlewfae
      181 rvdriillfd ahkldisdef sevikalknh edkirvvlnk adqietqqlm rvygalmwsl
      241 gkiintpevv rvyigsfwsh pllipdnrkl feaeeqdlfk diqslprnaa lrklndlikr
      301 arlakvhayi isslkkempn vfgkeskkke lvnnlgeiyq kierehqiss gdfpslrkmq
      361 ellqtqdfsk fqalkpklld tvddmlandi arlmvmvrqe eslmpsqavk ggafdgtmng
      421 pfghgygega gegiddvewv vgkdkptyde ifytlspvng kitganakke mvksklpntv
      481 lgkiwkladv dkdgllddee falanhlikv kleghelpad lpphlippsk rrhe
//
LOCUS       NP_001029159             448 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 5 isoform
            a [Rattus norvegicus].
ACCESSION   NP_001029159 XP_579403
VERSION     NP_001029159.1
DBSOURCE    REFSEQ: accession NM_001033987.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Stankiewicz,T.R., Ramaswami,S.A., Bouchard,R.J., Aktories,K. and
            Linseman,D.A.
  TITLE     Neuronal apoptosis induced by selective inhibition of Rac GTPase
            versus global suppression of Rho family GTPases is mediated by
            alterations in distinct mitogen-activated protein kinase signaling
            cascades
  JOURNAL   J Biol Chem 290 (15), 9363-9376 (2015)
   PUBMED   25666619
  REMARK    GeneRIF: Data indicate that NSC23766-mediated Rac inhibition
            induces cerebellar granule neurons (CGNs) apoptosis through
            deactivation of prosurvival MAP Kinase Kinase 5 MEK5/ERK5 kinase
            signaling.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Woo,C.H., Le,N.T., Shishido,T., Chang,E., Lee,H., Heo,K.S.,
            Mickelsen,D.M., Lu,Y., McClain,C., Spangenberg,T., Yan,C.,
            Molina,C.A., Yang,J., Patterson,C. and Abe,J.
  TITLE     Novel role of C terminus of Hsc70-interacting protein (CHIP)
            ubiquitin ligase on inhibiting cardiac apoptosis and dysfunction
            via regulating ERK5-mediated degradation of inducible cAMP early
            repressor
  JOURNAL   FASEB J 24 (12), 4917-4928 (2010)
   PUBMED   20724525
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Ohnesorge,N., Viemann,D., Schmidt,N., Czymai,T., Spiering,D.,
            Schmolke,M., Ludwig,S., Roth,J., Goebeler,M. and Schmidt,M.
  TITLE     Erk5 activation elicits a vasoprotective endothelial phenotype via
            induction of Kruppel-like factor 4 (KLF4)
  JOURNAL   J Biol Chem 285 (34), 26199-26210 (2010)
   PUBMED   20551324
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Haines,J.D., Fang,J., Mushynski,W.E. and Almazan,G.
  TITLE     Mitogen-activated protein kinase activated protein kinase 2 (MK2)
            participates in p38 MAPK regulated control of oligodendrocyte
            differentiation
  JOURNAL   Glia 58 (11), 1384-1393 (2010)
   PUBMED   20607863
  REMARK    GeneRIF: The p38-mitogen-activated protein kinase activated protein
            kinase 2 (MK2) pathway is a component of the signaling cascade
            regulating oligodendrocyte differentiation.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Gerits,N., Shiryaev,A., Kostenko,S., Klenow,H., Shiryaeva,O.,
            Johannessen,M. and Moens,U.
  TITLE     The transcriptional regulation and cell-specific expression of the
            MAPK-activated protein kinase MK5
  JOURNAL   Cell Mol Biol Lett 14 (4), 548-574 (2009)
   PUBMED   19484198
  REMARK    GeneRIF: Several binding motifs for heat shock factor are dispersed
            in the mouse and rat promoter, and temperature shock transiently
            enhanced the MAP-kinase-activated kinase 5 transcript levels.
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Thomas,J.A., Haudek,S.B., Koroglu,T., Tsen,M.F., Bryant,D.D.,
            White,D.J., Kusewitt,D.F., Horton,J.W. and Giroir,B.P.
  TITLE     IRAK1 deletion disrupts cardiac Toll/IL-1 signaling and protects
            against contractile dysfunction
  JOURNAL   Am J Physiol Heart Circ Physiol 285 (2), H597-H606 (2003)
   PUBMED   12860565
  REMARK    Erratum:[Am J Physiol Heart Circ Physiol. 2004 Jan;286(1):H477]
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Mehta,P.B., Jenkins,B.L., McCarthy,L., Thilak,L., Robson,C.N.,
            Neal,D.E. and Leung,H.Y.
  TITLE     MEK5 overexpression is associated with metastatic prostate cancer,
            and stimulates proliferation, MMP-9 expression and invasion
  JOURNAL   Oncogene 22 (9), 1381-1389 (2003)
   PUBMED   12618764
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Watson,F.L., Heerssen,H.M., Bhattacharyya,A., Klesse,L., Lin,M.Z.
            and Segal,R.A.
  TITLE     Neurotrophins use the Erk5 pathway to mediate a retrograde survival
            response
  JOURNAL   Nat Neurosci 4 (10), 981-988 (2001)
   PUBMED   11544482
  REMARK    Erratum:[Nat Neurosci 2002 Oct;5(10):1017]
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Nicol,R.L., Frey,N., Pearson,G., Cobb,M., Richardson,J. and
            Olson,E.N.
  TITLE     Activated MEK5 induces serial assembly of sarcomeres and eccentric
            cardiac hypertrophy
  JOURNAL   EMBO J 20 (11), 2757-2767 (2001)
   PUBMED   11387209
REFERENCE   10 (residues 1 to 448)
  AUTHORS   English,J.M., Vanderbilt,C.A., Xu,S., Marcus,S. and Cobb,M.H.
  TITLE     Isolation of MEK5 and differential expression of alternatively
            spliced forms
  JOURNAL   J Biol Chem 270 (48), 28897-28902 (1995)
   PUBMED   7499418
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078860.1.
            
            On Oct 9, 2005 this sequence version replaced XP_579403.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078860.1, U37462.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..448
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 5 isoform a"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 5; MAPKK 5; MAPK/ERK kinase 5; MAP kinase kinase 5;
                     MEK 5"
                     /calculated_mol_wt=50067
     Region          17..107
                     /region_name="PB1_Map2k5"
                     /note="PB1 domain is essential part of the
                     mitogen-activated protein kinase kinase 5 (Map2k5, alias
                     MEK5) one of the key member of the signaling kinases
                     cascade which involved in angiogenesis and early
                     cardiovascular development. The PB1 domain of Map2k5...;
                     cd06395"
                     /db_xref="CDD:99717"
     Region          18..25
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62862.1)"
     Site            order(64,66,68,77)
                     /site_type="other"
                     /note="PB1 interaction surface [polypeptide binding]"
                     /db_xref="CDD:99717"
     Region          64..68
                     /region_name="Interaction with MAP3K2/MAP3K3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62862.1)"
     Region          116..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62862.1)"
     Region          117..131
                     /region_name="Interaction with MAPK7.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62862.1)"
     Region          164..442
                     /region_name="PKc_MKK5"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-activated protein Kinase Kinase 5;
                     cd06619"
                     /db_xref="CDD:132950"
     Site            order(172..176,180,193,195,225,241..244,247..248,251,283,
                     285..288,290,300..301,304,316..319,321,348,357)
                     /site_type="active"
                     /db_xref="CDD:132950"
     Site            order(172..176,178,180,193,195,225,241..244,247..248,
                     250..251,285,287..288,290,301)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132950"
     Site            order(175..176,283,285..287,304,316..319,321,348,357)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:132950"
     Site            300..321
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:132950"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13163; propagated from
                     UniProtKB/Swiss-Prot (Q62862.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13163; propagated from
                     UniProtKB/Swiss-Prot (Q62862.1)"
     CDS             1..448
                     /gene="Map2k5"
                     /gene_synonym="Mek5"
                     /coded_by="NM_001033987.1:600..1946"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:29568"
                     /db_xref="RGD:61890"
ORIGIN      
        1 mlwlalgpfr amenqvlvir ikipnsgavd wtvhsgpqll frdvldvigq vlpeatttaf
       61 eyededgdri tvrsdeemka mlsyyystvm eqqvngqlie plqifprack ppgernihgl
      121 kvntragpsq htspvvsdsl psnslkkssa elrkilangq mneqdiryrd tlghgnggtv
      181 ykayhvpsgk ilavkvilld itlelqkqim seleilykcd ssyiigfyga ffvenrisic
      241 tefmdggsld vyrkipehvl griavavvkg ltylwslkil hrdvkpsnml vntsgqvklc
      301 dfgvstqlvn siaktyvgtn aymaperisg eqygihsdvw slgisfmela lgrfpypqiq
      361 knqgslmplq llqcivdeds pvlplgefse pfvhfitqcm rkqpkerpap eelmghpfiv
      421 qfndgnatvv smwvcralee rrsqqgpp
//
LOCUS       NP_036635                284 aa            linear   ROD 27-APR-2025
DEFINITION  asialoglycoprotein receptor 1 isoform a [Rattus norvegicus].
ACCESSION   NP_036635
VERSION     NP_036635.1
DBSOURCE    REFSEQ: accession NM_012503.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Li,Y., Yang,C.F., Zuo,H., Li,A., Das,S.K. and Yu,J.H.
  TITLE     Asialoglycoprotein Receptor-Targeted Superparamagnetic
            Perfluorooctylbromide Nanoparticles
  JOURNAL   Contrast Media Mol Imaging 2021, 5510071 (2021)
   PUBMED   34131415
  REMARK    GeneRIF: Asialoglycoprotein Receptor-Targeted Superparamagnetic
            Perfluorooctylbromide Nanoparticles.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Park,E.I., Mi,Y., Unverzagt,C., Gabius,H.J. and Baenziger,J.U.
  TITLE     The asialoglycoprotein receptor clears glycoconjugates terminating
            with sialic acid alpha 2,6GalNAc
  JOURNAL   Proc Natl Acad Sci U S A 102 (47), 17125-17129 (2005)
   PUBMED   16286643
  REMARK    GeneRIF: Asialoglycoprotein receptor functions to help regulate the
            concentration of glycoproteins bearing sialic acid alpha 2,6GalNAc
            in the blood.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Casey,C.A., McVicker,B.L., Donohue,T.M. Jr., McFarland,M.A.,
            Wiegert,R.L. and Nanji,A.A.
  TITLE     Liver asialoglycoprotein receptor levels correlate with severity of
            alcoholic liver damage in rats
  JOURNAL   J Appl Physiol (1985) 96 (1), 76-80 (2004)
   PUBMED   12949020
  REMARK    GeneRIF: a correlation exists between the progression of
            alcohol-associated liver injury, as defined by the severity of
            liver pathology, and an ethanol-induced decline in ASGP-R content.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Deng,A.Y. and Rapp,J.P.
  TITLE     Locus for the inducible, but not a constitutive, nitric oxide
            synthase cosegregates with blood pressure in the Dahl
            salt-sensitive rat
  JOURNAL   J Clin Invest 95 (5), 2170-2177 (1995)
   PUBMED   7537756
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Ishibashi,S., Hammer,R.E. and Herz,J.
  TITLE     Asialoglycoprotein receptor deficiency in mice lacking the minor
            receptor subunit
  JOURNAL   J Biol Chem 269 (45), 27803-27806 (1994)
   PUBMED   7961705
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Reddy,N.S., Roth,W.W., Bragg,P.W. and Wahba,A.J.
  TITLE     Isolation and mapping of a gene for protein synthesis initiation
            factor 4A and its expression during differentiation of murine
            erythroleukemia cells
  JOURNAL   Gene 70 (2), 231-243 (1988)
   PUBMED   3215517
REFERENCE   7  (residues 1 to 284)
  AUTHORS   McPhaul,M. and Berg,P.
  TITLE     Identification and characterization of cDNA clones encoding two
            homologous proteins that are part of the asialoglycoprotein
            receptor
  JOURNAL   Mol Cell Biol 7 (5), 1841-1847 (1987)
   PUBMED   3600647
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Watts,C.
  TITLE     Isolation and expression of cDNA clones for a rat liver
            asialoglycoprotein receptor
  JOURNAL   Biosci Rep 6 (6), 527-534 (1986)
   PUBMED   2945599
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Leung,J.O., Holland,E.C. and Drickamer,K.
  TITLE     Characterization of the gene encoding the major rat liver
            asialoglycoprotein receptor
  JOURNAL   J Biol Chem 260 (23), 12523-12527 (1985)
   PUBMED   2995379
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Holland,E.C., Leung,J.O. and Drickamer,K.
  TITLE     Rat liver asialoglycoprotein receptor lacks a cleavable
            NH2-terminal signal sequence
  JOURNAL   Proc Natl Acad Sci U S A 81 (23), 7338-7342 (1984)
   PUBMED   6095287
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC088154.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088154.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..284
                     /product="asialoglycoprotein receptor 1 isoform a"
                     /note="RHL-1; ASGPR 1; ASGP-R 1; HL-1; hepatic lectin 1,
                     RHL1; Asialoglycoprotein receptor 1 (hepatic lectin);
                     asialoglycoprotein receptor (RHL1)"
                     /calculated_mol_wt=32718
     Region          4..143
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:461106"
     Region          5..8
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02706.2)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02706.2)"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02706.2)"
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02706.2)"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02706.2)"
     Region          153..278
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(208,239,241,252,258..259,264..267)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(215,242,252..253)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     CDS             1..284
                     /gene="Asgr1"
                     /gene_synonym="ASGR; RATRHL1; RHL1"
                     /coded_by="NM_012503.2:66..920"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24210"
                     /db_xref="RGD:2160"
ORIGIN      
        1 mtkdyqdfqh ldnendhhql qrgpppaprl lqrlcsgfrl fllslglsil llvvvcvits
       61 qnsqlredlr vlrqnfsnft vstedqvkal ttqgervgrk mklvesqlek hqedlredhs
      121 rlllhvkqlv sdvrslscqm aalrgngser iccpinwvey egscywfsss vkpwteadky
      181 cqlenahlvv vtsweeqrfv qqhmgplntw igltdqngpw kwvdgtdyet gfknwrpgqp
      241 ddwyghglgg gedcahfttd ghwnddvcrr pyrwvcetel gkan
//
LOCUS       NP_852050                361 aa            linear   ROD 27-APR-2025
DEFINITION  zygote arrest protein 1 [Rattus norvegicus].
ACCESSION   NP_852050
VERSION     NP_852050.1
DBSOURCE    REFSEQ: accession NM_181385.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Hu,J., Wang,F., Zhu,X., Yuan,Y., Ding,M. and Gao,S.
  TITLE     Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing
            components and its dominant-negative mutant caused two-cell-stage
            embryonic arrest
  JOURNAL   Dev Dyn 239 (2), 407-424 (2010)
   PUBMED   20014101
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Wu,X., Wang,P., Brown,C.A., Zilinski,C.A. and Matzuk,M.M.
  TITLE     Zygote arrest 1 (Zar1) is an evolutionarily conserved gene
            expressed in vertebrate ovaries
  JOURNAL   Biol Reprod 69 (3), 861-867 (2003)
   PUBMED   12773403
  REMARK    GeneRIF: The carboxyl-termini of these ZAR1 proteins contain an
            important functional domain that is conserved through vertebrate
            evolution and that may be necessary for normal female reproduction
            in the transition from oocyte to embryonic life.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY283175.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY283175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..361
                     /product="zygote arrest protein 1"
                     /note="oocyte-specific maternal effect factor"
                     /calculated_mol_wt=40226
     Region          68..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSX9.1)"
     Region          <120..>250
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          142..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSX9.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80SU3; propagated from
                     UniProtKB/Swiss-Prot (Q7TSX9.1)"
     Region          264..346
                     /region_name="zf-3CxxC"
                     /note="Zinc-binding domain; pfam13695"
                     /db_xref="CDD:463958"
     CDS             1..361
                     /gene="Zar1"
                     /coded_by="NM_181385.2:28..1113"
                     /db_xref="GeneID:353228"
                     /db_xref="RGD:727972"
ORIGIN      
        1 mfpastphpc phpypptaak agdgwrfgar gcrpeppsfl pgyrqlmaae yfdsyqraql
       61 mallsrmgpr pvssrdaavq vnprrdasvq cslgrrtlqp grrraspdar pgscqprspa
      121 ragrpprswr tvalyspvtf gglsssleva gdrqtptkge grpaptgtre pepgevavmk
      181 avpqpqseeg dvqaegqdgq eqppredpds vaamqsepgs eepppavema qdpsdvaasr
      241 draspqsteq dkerlrfqfl eqkygyyhck dcnirwesay vwcvqgtskv yfkqfcrvce
      301 ksynpyrved itcqsckrtr cacpvrlrhv dpkrphrqdl cgrckdkrls cdstfsfkyi
      361 i
//
LOCUS       NP_955408                465 aa            linear   ROD 27-APR-2025
DEFINITION  nucleotide exchange factor SIL1 precursor [Rattus norvegicus].
ACCESSION   NP_955408 XP_214586
VERSION     NP_955408.1
DBSOURCE    REFSEQ: accession NM_199376.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhao,L., Longo-Guess,C., Harris,B.S., Lee,J.W. and Ackerman,S.L.
  TITLE     Protein accumulation and neurodegeneration in the woozy mutant
            mouse is caused by disruption of SIL1, a cochaperone of BiP
  JOURNAL   Nat Genet 37 (9), 974-979 (2005)
   PUBMED   16116427
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Chung,K.T., Shen,Y. and Hendershot,L.M.
  TITLE     BAP, a mammalian BiP-associated protein, is a nucleotide exchange
            factor that regulates the ATPase activity of BiP
  JOURNAL   J Biol Chem 277 (49), 47557-47563 (2002)
   PUBMED   12356756
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062050.1.
            
            On Jan 11, 2004 this sequence version replaced XP_214586.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062050.1, SRR8487227.171200.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..465
                     /product="nucleotide exchange factor SIL1 precursor"
                     /note="nucleotide exchange factor SIL1; SIL1 homolog,
                     endoplasmic reticulum chaperone"
                     /calculated_mol_wt=49066
     Region          1..260
                     /region_name="Interaction with HSPA5 and localization to
                     the endoplasmic reticulum.
                     /evidence=ECO:0000250|UniProtKB:Q9EPK6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6S4.1)"
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3302
     mat_peptide     32..465
                     /product="Nucleotide exchange factor SIL1.
                     /id=PRO_0000223356"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6S4.1)"
                     /calculated_mol_wt=49066
     Region          39..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6S4.1)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P6S4.1)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P6S4.1)"
     CDS             1..465
                     /gene="Sil1"
                     /coded_by="NM_199376.1:82..1479"
                     /db_xref="GeneID:291673"
                     /db_xref="RGD:735103"
ORIGIN      
        1 mapqhlpstr mapqgmllgl llascltfcl scqnsnnfal tnpeksthed sdtketrree
       61 eldaevlevl nptqewqalq pgqavpagsh vrmnlqtgvn evklqqedkf qsnwkgfkrg
      121 rrldintnty tsqdlksala kfkegtemen skdelarqat vkqlfrpiee lkkefdelnv
      181 vletdmqimv rlinkfnsss ssleekvaal fdleyyvhqm dnaqdllsfg glqvvingln
      241 steplvkeya afvlgaafss npkvqveaie ggalqkllvi lateqplpak kkvlfalcsl
      301 lrhfpyaqqq flklgglqvl rslvqeksak vlavrvvtll ydlvtekmfa eeeaeltqes
      361 speklqqyrq vqllpglreq gwceitaqll alpehdarek vlqtlgalla tcrdryrqdl
      421 elsrtlgslq aeyqalasle lqegeddgyf rellasidsl vkelr
//
LOCUS       NP_058804               1087 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated inwardly rectifying potassium channel KCNH3 [Rattus
            norvegicus].
ACCESSION   NP_058804 XP_001063471
VERSION     NP_058804.1
DBSOURCE    REFSEQ: accession NM_017108.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1087)
  AUTHORS   Wulfsen,I., Hauber,H.P., Schiemann,D., Bauer,C.K. and Schwarz,J.R.
  TITLE     Expression of mRNA for voltage-dependent and inward-rectifying K
            channels in GH3/B6 cells and rat pituitary
  JOURNAL   J Neuroendocrinol 12 (3), 263-272 (2000)
   PUBMED   10718922
REFERENCE   2  (residues 1 to 1087)
  AUTHORS   Miyake,A., Mochizuki,S., Yokoi,H., Kohda,M. and Furuichi,K.
  TITLE     New ether-a-go-go K(+) channel family members localized in human
            telencephalon
  JOURNAL   J Biol Chem 274 (35), 25018-25025 (1999)
   PUBMED   10455180
REFERENCE   3  (residues 1 to 1087)
  AUTHORS   Engeland,B., Neu,A., Ludwig,J., Roeper,J. and Pongs,O.
  TITLE     Cloning and functional expression of rat ether-a-go-go-like K+
            channel genes
  JOURNAL   J Physiol 513 (Pt 3) (Pt 3), 647-654 (1998)
   PUBMED   9824707
REFERENCE   4  (residues 1 to 1087)
  AUTHORS   Shi,W., Wang,H.S., Pan,Z., Wymore,R.S., Cohen,I.S., McKinnon,D. and
            Dixon,J.E.
  TITLE     Cloning of a mammalian elk potassium channel gene and EAG mRNA
            distribution in rat sympathetic ganglia
  JOURNAL   J Physiol 511 (Pt 3) (Pt 3), 675-682 (1998)
   PUBMED   9714851
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB022697.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001063471.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB022697.1, AJ007627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1087
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..1087
                     /product="voltage-gated inwardly rectifying potassium
                     channel KCNH3"
                     /note="rElk2; ELK channel 2; brain-specific eag-like
                     channel 1; ether-a-go-go-like potassium channel 2;
                     voltage-gated potassium channel subunit Kv12.2; potassium
                     voltage-gated channel, subfamily H (eag-related), member
                     3; potassium channel, voltage gated eag related subfamily
                     H, member 3"
                     /calculated_mol_wt=117450
     Region          40..135
                     /region_name="PAS_9"
                     /note="PAS domain; pfam13426"
                     /db_xref="CDD:463873"
     Region          137..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Region          227..>654
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            332..352
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            362..382
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Region          416..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O89047.1)"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O89047.1)"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O89047.1)"
     Region          468..473
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Site            483..503
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Region          <609..704
                     /region_name="cyc_nuc_ocin"
                     /note="bacteriocin-type transport-associated protein;
                     TIGR03896"
                     /db_xref="CDD:274839"
     Region          733..813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     Region          975..1061
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89047.1)"
     CDS             1..1087
                     /gene="Kcnh3"
                     /gene_synonym="Bec1; Elk2"
                     /coded_by="NM_017108.1:156..3419"
                     /db_xref="GeneID:27150"
                     /db_xref="RGD:71070"
ORIGIN      
        1 mpamrgllap qntfldtiat rfdgthsnfv lgnaqvaglf pvvycsdgfc dltgfsraev
       61 mqrgcacsfl ygpdtselvr qqirkaldeh kefkaelily rksglpfwcl ldvipiknek
      121 gevalflvsh kdisetknrg gpdnwkergg grrrygrags kgfnanrrrs ravlyhlsgh
      181 lqkqpkgkhk lnkgvfgekp nlpeykvaai rkspfillhc galratwdgf illatlyvav
      241 tvpysvcvst arepsaargp psvcdlavev lfildivlnf rttfvsksgq vvfapksicl
      301 hyvttwflld viaalpfdll hafkvnvyvg ahllktvrll rllrllprld rysqysavvl
      361 tllmavfall ahwvacvwfy igqqeiense selpeigwlq elarrletpy ylvsrspdgg
      421 nssgqsencs ssgggseang tglellggps lrsayitsly falssltsvg fgnvsantdt
      481 ekifsictml igalmhavvf gnvtaiiqrm yarrflyhsr trdlrdyiri hripkplkqr
      541 mleyfqatwa vnngidttel lqslpdelra diamhlhkev lqlplfeaas rgclralsla
      601 lrpafctpge ylihqgdalq alyfvcsgsm evlkggtvla ilgkgdligc elpqreqvvk
      661 anadvkglty cvlqclqlag lheslalype faprfsrglr gelsynlgag gvsaevdtss
      721 lsgdntlmst leeketdgeq ghtispapad epsspllspg ctssssaakl lsprrtaprp
      781 rlggrgrpsr agvlkpeagp sahprtldgl qlppmpwnvp pdlsprvvdg iedgcgsdqh
      841 kfsfrvgqsg pecssspspg tesglltvpl vpsearntdt ldklrqavte lseqvlqmre
      901 glqslrqavq lilvpqgegq cprvsgegpc patasgllqp lrvdtgassy clqppagsvl
      961 sgtwphprpg hppplmapwp wgppasqssp wpratalwts tsdseppgsg dlcsepstpa
     1021 sppppeegar tgtpapvsqa eatstgeppp gsggralpwd phslemvlig chgpgsvqwt
     1081 qeegtgv
//
LOCUS       NP_001035815             503 aa            linear   ROD 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_001035815
VERSION     NP_001035815.1
DBSOURCE    REFSEQ: accession NM_001042356.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Yang,C., Zhang,M., Li,S., Yi,F., Huang,H., Xie,H., Liu,H., Huang,R.
            and Zhou,J.
  TITLE     Effects of Camk2b Overexpression and Underexpression on the
            Proteome of Rat Hippocampal Neurons
  JOURNAL   Neuroscience 503, 58-68 (2022)
   PUBMED   36041587
  REMARK    GeneRIF: Effects of Camk2b Overexpression and Underexpression on
            the Proteome of Rat Hippocampal Neurons.
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Liu,W., Li,L., Kuang,H., Xia,Y., Wang,Z., Liu,S. and Yin,D.
  TITLE     Proteomic Profile of Carbonylated Proteins Screen Regulation of
            Apoptosis via CaMK Signaling in Response to Regular Aerobic
            Exercise
  JOURNAL   Biomed Res Int 2018, 2828143 (2018)
   PUBMED   30662904
  REMARK    GeneRIF: Significantly upregulated the expression levels of
            CaMKIIbeta.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Yamazaki,H., Sasagawa,Y., Yamamoto,H., Bito,H. and Shirao,T.
  TITLE     CaMKIIbeta is localized in dendritic spines as both
            drebrin-dependent and drebrin-independent pools
  JOURNAL   J Neurochem 146 (2), 145-159 (2018)
   PUBMED   29675826
  REMARK    GeneRIF: This study provides the first evidence to show that
            CaMKIIbeta interacts with drebrin in dendritic spines.
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Kury,S., van Woerden,G.M., Besnard,T., Proietti Onori,M.,
            Latypova,X., Towne,M.C., Cho,M.T., Prescott,T.E., Ploeg,M.A.,
            Sanders,S., Stessman,H.A.F., Pujol,A., Distel,B., Robak,L.A.,
            Bernstein,J.A., Denomme-Pichon,A.S., Lesca,G., Sellars,E.A.,
            Berg,J., Carre,W., Busk,O.L., van Bon,B.W.M., Waugh,J.L.,
            Deardorff,M., Hoganson,G.E., Bosanko,K.B., Johnson,D.S., Dabir,T.,
            Holla,O.L., Sarkar,A., Tveten,K., de Bellescize,J., Braathen,G.J.,
            Terhal,P.A., Grange,D.K., van Haeringen,A., Lam,C., Mirzaa,G.,
            Burton,J., Bhoj,E.J., Douglas,J., Santani,A.B., Nesbitt,A.I.,
            Helbig,K.L., Andrews,M.V., Begtrup,A., Tang,S., van Gassen,K.L.I.,
            Juusola,J., Foss,K., Enns,G.M., Moog,U., Hinderhofer,K.,
            Paramasivam,N., Lincoln,S., Kusako,B.H., Lindenbaum,P.,
            Charpentier,E., Nowak,C.B., Cherot,E., Simonet,T.,
            Ruivenkamp,C.A.L., Hahn,S., Brownstein,C.A., Xia,F., Schmitt,S.,
            Deb,W., Bonneau,D., Nizon,M., Quinquis,D., Chelly,J., Rudolf,G.,
            Sanlaville,D., Parent,P., Gilbert-Dussardier,B., Toutain,A.,
            Sutton,V.R., Thies,J., Peart-Vissers,L.E.L.M., Boisseau,P.,
            Vincent,M., Grabrucker,A.M., Dubourg,C., Tan,W.H., Verbeek,N.E.,
            Granzow,M., Santen,G.W.E., Shendure,J., Isidor,B., Pasquier,L.,
            Redon,R., Yang,Y., State,M.W., Kleefstra,T., Cogne,B.,
            Petrovski,S., Retterer,K., Eichler,E.E., Rosenfeld,J.A.,
            Agrawal,P.B., Bezieau,S., Odent,S., Elgersma,Y. and Mercier,S.
  CONSRTM   Undiagnosed Diseases Network; GEM HUGO; Deciphering Developmental
            Disorders Study
  TITLE     De Novo Mutations in Protein Kinase Genes CAMK2A and CAMK2B Cause
            Intellectual Disability
  JOURNAL   Am J Hum Genet 101 (5), 768-788 (2017)
   PUBMED   29100089
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Yan,X., Liu,J., Ye,Z., Huang,J., He,F., Xiao,W., Hu,X. and Luo,Z.
  TITLE     CaMKII-Mediated CREB Phosphorylation Is Involved in Ca2+-Induced
            BDNF mRNA Transcription and Neurite Outgrowth Promoted by
            Electrical Stimulation
  JOURNAL   PLoS One 11 (9), e0162784 (2016)
   PUBMED   27611779
  REMARK    GeneRIF: these data establish a potential signaling pathway of
            Ca2+-CaMKII-CREB in neuronal activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Bayer,K.U., Harbers,K. and Schulman,H.
  TITLE     alphaKAP is an anchoring protein for a novel CaM kinase II isoform
            in skeletal muscle
  JOURNAL   EMBO J 17 (19), 5598-5605 (1998)
   PUBMED   9755160
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Urquidi,V. and Ashcroft,S.J.
  TITLE     A novel pancreatic beta-cell isoform of
            calcium/calmodulin-dependent protein kinase II (beta 3 isoform)
            contains a proline-rich tandem repeat in the association domain
  JOURNAL   FEBS Lett 358 (1), 23-26 (1995)
   PUBMED   7821422
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Ochiishi,T., Terashima,T. and Yamauchi,T.
  TITLE     Specific distribution of Ca2+/calmodulin-dependent protein kinase
            II alpha and beta isoforms in some structures of the rat forebrain
  JOURNAL   Brain Res 659 (1-2), 179-193 (1994)
   PUBMED   7820660
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Malinow,R., Schulman,H. and Tsien,R.W.
  TITLE     Inhibition of postsynaptic PKC or CaMKII blocks induction but not
            expression of LTP
  JOURNAL   Science 245 (4920), 862-866 (1989)
   PUBMED   2549638
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB616255.1, M16112.1, CB728582.1, CB692429.1 and JAXUCZ010000014.1.
            
            Transcript Variant: This variant (3) lacks two alternate, in-frame
            exons in the 3' coding region, compared to variant 1. The resulting
            protein (isoform 3) is shorter when it is compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2353185.1,
                                           SRR26360194.1536397.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..503
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 3"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type II
                     beta chain; calcium/calmodulin-dependent protein kinase
                     type II subunit beta; caMK-II subunit beta; caM-kinase II
                     beta chain; caM kinase II subunit beta;
                     calcium/calmodulin-dependent protein kinase (CaM kinase)
                     II beta; Ca++/calmodulin-dependent protein kinase II beta
                     subunit"
                     /calculated_mol_wt=56322
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          371..498
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..503
                     /gene="Camk2b"
                     /gene_synonym="Ck2b"
                     /coded_by="NM_001042356.1:83..1594"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24245"
                     /db_xref="RGD:2262"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsaaksl lnkkadgvkp qtnstknssa itspkgslpp aalessdstn
      361 ttiededaka rkqeiiktte qlieavnngd feayakicdp gltsfepeal gnlvegmdfh
      421 rfyfenllak nskpihttil nphvhviged aaciayirlt qyidgqgrpr tsqseetrvw
      481 hrrdgkwqnv hfhcsgapva plq
//
LOCUS       NP_786934                539 aa            linear   ROD 27-APR-2025
DEFINITION  neutral amino acid transporter B(0) [Rattus norvegicus].
ACCESSION   NP_786934 NP_714945
VERSION     NP_786934.1
DBSOURCE    REFSEQ: accession NM_175758.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Chen,Z., Gao,Y., Huang,X., Yao,Y., Chen,K., Zeng,S. and Mao,W.
  TITLE     Tissue-based metabolomics reveals metabolic biomarkers and
            potential therapeutic targets for esophageal squamous cell
            carcinoma
  JOURNAL   J Pharm Biomed Anal 197, 113937 (2021)
   PUBMED   33609949
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Ndaru,E., Garibsingh,R.A., Zielewicz,L., Schlessinger,A. and
            Grewer,C.
  TITLE     Interaction of the neutral amino acid transporter ASCT2 with basic
            amino acids
  JOURNAL   Biochem J 477 (8), 1443-1457 (2020)
   PUBMED   32242892
  REMARK    GeneRIF: Interaction of the neutral amino acid transporter ASCT2
            with basic amino acids.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Garaeva,A.A., Oostergetel,G.T., Gati,C., Guskov,A., Paulino,C. and
            Slotboom,D.J.
  TITLE     Cryo-EM structure of the human neutral amino acid transporter ASCT2
  JOURNAL   Nat Struct Mol Biol 25 (6), 515-521 (2018)
   PUBMED   29872227
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Foster,A.C., Farnsworth,J., Lind,G.E., Li,Y.X., Yang,J.Y., Dang,V.,
            Penjwini,M., Viswanath,V., Staubli,U. and Kavanaugh,M.P.
  TITLE     D-Serine Is a Substrate for Neutral Amino Acid Transporters
            ASCT1/SLC1A4 and ASCT2/SLC1A5, and Is Transported by Both Subtypes
            in Rat Hippocampal Astrocyte Cultures
  JOURNAL   PLoS One 11 (6), e0156551 (2016)
   PUBMED   27272177
  REMARK    GeneRIF: the selectivity profile of D-serine uptake in cultured rat
            hippocampal astrocytes is consistent with uptake mediated by both
            ASCT1 and ASCT2. Together these data suggest that SLC1A4 (ASCT1)
            may represent an important route of Na-dependent D-serine flux in
            the brain that has the ability to regulate extracellular D-serine
            and thereby NMDA receptor activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Honjo,H., Kaira,K., Miyazaki,T., Yokobori,T., Kanai,Y.,
            Nagamori,S., Oyama,T., Asao,T. and Kuwano,H.
  TITLE     Clinicopathological significance of LAT1 and ASCT2 in patients with
            surgically resected esophageal squamous cell carcinoma
  JOURNAL   J Surg Oncol 113 (4), 381-389 (2016)
   PUBMED   26936531
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Yamamoto,T., Nishizaki,I., Furuya,S., Hirabayashi,Y., Takahashi,K.,
            Okuyama,S. and Yamamoto,H.
  TITLE     Characterization of rapid and high-affinity uptake of L-serine in
            neurons and astrocytes in primary culture
  JOURNAL   FEBS Lett 548 (1-3), 69-73 (2003)
   PUBMED   12885409
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Pollard,M., Meredith,D. and McGivan,J.D.
  TITLE     Identification of a plasma membrane glutamine transporter from the
            rat hepatoma cell line H4-IIE-C3
  JOURNAL   Biochem J 368 (Pt 1), 371-375 (2002)
   PUBMED   12171599
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Marin,M., Tailor,C.S., Nouri,A. and Kabat,D.
  TITLE     Sodium-dependent neutral amino acid transporter type 1 is an
            auxiliary receptor for baboon endogenous retrovirus
  JOURNAL   J Virol 74 (17), 8085-8093 (2000)
   PUBMED   10933718
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Broer,A., Wagner,C., Lang,F. and Broer,S.
  TITLE     Neutral amino acid transporter ASCT2 displays substrate-induced Na+
            exchange and a substrate-gated anion conductance
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 705-710 (2000)
   PUBMED   10698697
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Broer,A., Brookes,N., Ganapathy,V., Dimmer,K.S., Wagner,C.A.,
            Lang,F. and Broer,S.
  TITLE     The astroglial ASCT2 amino acid transporter as a mediator of
            glutamine efflux
  JOURNAL   J Neurochem 73 (5), 2184-2194 (1999)
   PUBMED   10537079
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC080242.1.
            
            On Oct 20, 2005 this sequence version replaced NP_714945.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC080242.1, AJ132846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..539
                     /product="neutral amino acid transporter B(0)"
                     /note="H4-system ASC-like transporter; solute carrier
                     family 1, member 7; CAZ-associated structural protein;
                     sodium-dependent neutral amino acid transporter ASCT2;
                     solute carrier family 1 (neutral amino acid transporter),
                     member 5; insulin-activated amino acid transporter;
                     sodium-dependent neutral amino acid transporter type 2;
                     ASC-like Na(+)-dependent neutral amino acid transporter
                     ASCT2"
                     /calculated_mol_wt=56624
     Region          81..477
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..539
                     /gene="Slc1a5"
                     /gene_synonym="Asct2; ATB(0); H4-ASCT2; Slc1a7"
                     /coded_by="NM_175758.3:392..2011"
                     /db_xref="GeneID:292657"
                     /db_xref="RGD:708512"
ORIGIN      
        1 mavdppkadp kgvvavdpta ncgsglksre dqgakaggcc ssrdqvcrcl ranllvlltv
       61 aaavagvvlg lgvsaaggae algharftaf afpgelllrl lemiilplvv csliggaasl
      121 dpsalgrlga wallfflvtt llssalgval alalkpgaaf aainssvvds svhraptkev
      181 ldsflellrn mfpsnlvsas aafripcgac pqrsnatmdq phcemkmnil glvvfaivfg
      241 valrklgpeg ellirffnsf ndatmvlvsw imwyapigil flvagkivem kdirqlfigl
      301 gkyivccllg haihgllvlp liyflftrkn pyrflwgivt platafgtss ssatlplmmk
      361 cveekngvak hisrfilpig atvnmdgaal fqcvaavfia qlngmsldfv kiitilvtat
      421 assvgaagip aggvltlaii leaislpvkd islilavdwl vdrsctvlnv egdafgagll
      481 qsyvdrtkmp ssepeliqvk ndvslkplpl ateegnpllk qcrepsgdss atcekesvm
//
LOCUS       NP_001036084             373 aa            linear   ROD 27-APR-2025
DEFINITION  3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
            [Rattus norvegicus].
ACCESSION   NP_001036084 XP_001061878 XP_001061941
VERSION     NP_001036084.1
DBSOURCE    REFSEQ: accession NM_001042619.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Zurvarra,F.M., Salvetti,N.R., Mason,J.I., Velazquez,M.M.,
            Alfaro,N.S. and Ortega,H.H.
  TITLE     Disruption in the expression and immunolocalisation of steroid
            receptors and steroidogenic enzymes in letrozole-induced polycystic
            ovaries in rat
  JOURNAL   Reprod Fertil Dev 21 (7), 827-839 (2009)
   PUBMED   19698287
  REMARK    GeneRIF: Letrozole-induced polycystic ovaries showed increased
            3beta-HSD expression.
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Naville,D., Keeney,D.S., Jenkin,G., Murry,B.A., Head,J.R. and
            Mason,J.I.
  TITLE     Regulation of expression of male-specific rat liver microsomal 3
            beta-hydroxysteroid dehydrogenase
  JOURNAL   Mol Endocrinol 5 (8), 1090-1100 (1991)
   PUBMED   1944305
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Zhao,H.F., Labrie,C., Simard,J., de Launoit,Y., Trudel,C.,
            Martel,C., Rheaume,E., Dupont,E., Luu-The,V., Pelletier,G. et al.
  TITLE     Characterization of rat 3 beta-hydroxysteroid dehydrogenase/delta
            5-delta 4 isomerase cDNAs and differential tissue-specific
            expression of the corresponding mRNAs in steroidogenic and
            peripheral tissues
  JOURNAL   J Biol Chem 266 (1), 583-593 (1991)
   PUBMED   1985917
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Lachance,Y., Luu-The,V., Labrie,C., Simard,J., Dumont,M., de
            Launoit,Y., Guerin,S., Leblanc,G. and Labrie,F.
  TITLE     Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta
            5-delta 4-isomerase gene and its expression in mammalian cells
  JOURNAL   J Biol Chem 265 (33), 20469-20475 (1990)
   PUBMED   2243100
  REMARK    Erratum:[J Biol Chem. 1992 Feb 15;267(5):3551. PMID: 1737804]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M38179.1.
            
            On or before Jul 30, 2006 this sequence version replaced
            XP_001061941.1, XP_001061878.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M38179.1, EX488740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..373
                     /product="3 beta-hydroxysteroid dehydrogenase/Delta
                     5-->4-isomerase type 2"
                     /EC_number="1.1.1.145"
                     /EC_number="5.3.3.1"
                     /note="3-beta-HSD II; 3 beta-hydroxysteroid
                     dehydrogenase/Delta 5-->4-isomerase type II; 3
                     beta-hydroxysteroid dehydrogenase/delta-5-delta-4
                     isomerase type II; 3 beta-hydroxysteroid
                     dehydrogenase/delta-5-delta-4 isomerase type 3"
                     /calculated_mol_wt=42146
     Region          5..357
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(10,12..13,15,36..38,82..84,123..125,155,159,
                     187..190)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187671"
     Site            order(101,125,155,159)
                     /site_type="active"
                     /db_xref="CDD:187671"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22072.3)"
     CDS             1..373
                     /gene="Hsd3b3"
                     /gene_synonym="Hsd3b"
                     /coded_by="NM_001042619.1:153..1274"
                     /db_xref="GeneID:682974"
                     /db_xref="RGD:1592771"
ORIGIN      
        1 mpgwsclvtg aggfvgqrii rmlvqekelq evraldkvfr petkeefskl qtkakvtmle
       61 gdildaqylr racqgisvvi htasvmdfsr vlprqtildv nlkgtqnlle agihasvpaf
      121 iycstvdvag pnsykktiln greeehhest wsnpypyskk maekavlaan gsilknggtl
      181 htcalrpmyi ygergqflsr iiimalknkg vlnvtgkfsi vnpvyvgnva wahilaargl
      241 rdpkksqniq gqfyyisddt phqsyddlnc tlskewglrl dsswslplpl lywlafllet
      301 vsfllrpfyn yrppfnchlv tlsnskftfs ykkaqrdlgy eplvsweeak qktsewigtl
      361 veqhretldt ksq
//
LOCUS       NP_071948                 83 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 7A2, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_071948
VERSION     NP_071948.1
DBSOURCE    REFSEQ: accession NM_022503.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Zong,S., Wu,M., Gu,J., Liu,T., Guo,R. and Yang,M.
  TITLE     Structure of the intact 14-subunit human cytochrome c oxidase
  JOURNAL   Cell Res 28 (10), 1026-1034 (2018)
   PUBMED   30030519
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   6  (residues 1 to 83)
  AUTHORS   Schagger,H., Noack,H., Halangk,W., Brandt,U. and von Jagow,G.
  TITLE     Cytochrome-c oxidase in developing rat heart. Enzymic properties
            and amino-terminal sequences suggest identity of the fetal heart
            and the adult liver isoform
  JOURNAL   Eur J Biochem 230 (1), 235-241 (1995)
   PUBMED   7601105
REFERENCE   7  (residues 1 to 83)
  AUTHORS   Enders,C., Schlerf,A., Mell,O., Grossman,L.I. and Kadenbach,B.
  TITLE     Nucleotide sequence of cDNA encoding subunit VIIa of rat liver
            cytochrome c oxidase
  JOURNAL   Nucleic Acids Res 18 (23), 7143 (1990)
   PUBMED   2175887
REFERENCE   8  (residues 1 to 83)
  AUTHORS   Kennaway,N.G., Carrero-Valenzuela,R.D., Ewart,G., Balan,V.K.,
            Lightowlers,R., Zhang,Y.Z., Powell,B.R., Capaldi,R.A. and
            Buist,N.R.
  TITLE     Isoforms of mammalian cytochrome c oxidase: correlation with human
            cytochrome c oxidase deficiency
  JOURNAL   Pediatr Res 28 (5), 529-535 (1990)
   PUBMED   2175025
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG668415.1 and AW521400.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ229035.1, FQ230547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..83
                     /product="cytochrome c oxidase subunit 7A2, mitochondrial
                     precursor"
                     /EC_number="7.1.1.9"
                     /note="cytochrome c oxidase subunit VIIa 3; cytochrome c
                     oxidase polypeptide 7A2, mitochondrial; cytochrome c
                     oxidase subunit 7A2, mitochondrial; cytochrome c oxidase
                     subunit VIIa-L; cytochrome c oxidase polypeptide
                     VIIa-liver/heart; cytochrome c oxidase subunit
                     VIIa-liver/heart; cytochrome c oxidase, subunit VIIa 2;
                     cytochrome c oxidase, subunit 7a 3; cytochrome c oxidase
                     subunit VIIa polypeptide 2"
                     /calculated_mol_wt=6649
     transit_peptide 1..23
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:2175025,
                     ECO:0000269|PubMed:7601105; propagated from
                     UniProtKB/Swiss-Prot (P35171.1)"
                     /calculated_mol_wt=2722
     mat_peptide     24..83
                     /product="Cytochrome c oxidase subunit 7A2, mitochondrial.
                     /id=PRO_0000006147"
                     /note="propagated from UniProtKB/Swiss-Prot (P35171.1)"
                     /calculated_mol_wt=6649
     Region          24..78
                     /region_name="Cyt_c_Oxidase_VIIa"
                     /note="Cytochrome c oxidase subunit VIIa. Cytochrome c
                     oxidase (CcO), the terminal oxidase in the respiratory
                     chains of eukaryotes and most bacteria, is a multi-chain
                     transmembrane protein located in the inner membrane of
                     mitochondria and the cell membrane of...; cd00928"
                     /db_xref="CDD:238468"
     Site            order(26,28,32,36)
                     /site_type="other"
                     /note="Subunit VIIa/Vb interface [polypeptide binding]"
                     /db_xref="CDD:238468"
     Site            order(28,31..32,35..36,43..44,51,54,58)
                     /site_type="other"
                     /note="Subunit VIIa/III interface [polypeptide binding]"
                     /db_xref="CDD:238468"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48771; propagated from
                     UniProtKB/Swiss-Prot (P35171.1)"
     Site            49..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35171.1)"
     Site            order(73,77)
                     /site_type="other"
                     /note="Subunit VIIa/I interface [polypeptide binding]"
                     /db_xref="CDD:238468"
     Site            77
                     /site_type="other"
                     /note="Subunit VIIa/VIIc interface [polypeptide binding]"
                     /db_xref="CDD:238468"
     CDS             1..83
                     /gene="Cox7a2"
                     /gene_synonym="Cox7a3"
                     /coded_by="NM_022503.2:83..334"
                     /db_xref="GeneID:29507"
                     /db_xref="RGD:68365"
ORIGIN      
        1 mlrnvlalrq iaqrtistts rrhfenkvpe kqklfqedng mpvhlkggts dallyratml
       61 ltvggtayai ymlamaafpk kqn
//
LOCUS       NP_058957                883 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor 2 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_058957
VERSION     NP_058957.1
DBSOURCE    REFSEQ: accession NM_017261.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Zhang,J., Liu,Z., Liu,X., Wang,X. and Yu,L.
  TITLE     Intravenous Injection of GluR2-3Y Inhibits Repeated Morphine-Primed
            Reinstatement of Drug Seeking in Rats
  JOURNAL   Brain Sci 13 (4), 590 (2023)
   PUBMED   37190555
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Han,J.X., Wen,C.X., Sun,R., Tang,M.Y., Li,X.M. and Lian,H.
  TITLE     The dorsal hippocampal CA3 regulates spatial reference memory
            through the CtBP2/GluR2 pathway
  JOURNAL   FASEB J 36 (9), e22456 (2022)
   PUBMED   35969153
  REMARK    GeneRIF: The dorsal hippocampal CA3 regulates spatial reference
            memory through the CtBP2/GluR2 pathway.
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Herguedas,B., Kohegyi,B.K., Dohrke,J.N., Watson,J.F., Zhang,D.,
            Ho,H., Shaikh,S.A., Lape,R., Krieger,J.M. and Greger,I.H.
  TITLE     Mechanisms underlying TARP modulation of the GluA1/2-gamma8 AMPA
            receptor
  JOURNAL   Nat Commun 13 (1), 734 (2022)
   PUBMED   35136046
  REMARK    GeneRIF: Mechanisms underlying TARP modulation of the
            GluA1/2-gamma8 AMPA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Schwarz,A.P., Kovalenko,A.A., Zakharova,M.V. and Zaitsev,A.V.
  TITLE     The application of the self-probing primer PCR for quantitative
            expression analysis of R607Q (un)edited GluA2 AMPA receptor mRNA
  JOURNAL   Biochem Biophys Res Commun 569, 174-178 (2021)
   PUBMED   34252589
  REMARK    GeneRIF: The application of the self-probing primer PCR for
            quantitative expression analysis of R607Q (un)edited GluA2 AMPA
            receptor mRNA.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Pereyra,M., de Landeta,A.B., Dalto,J.F., Katche,C. and Medina,J.H.
  TITLE     AMPA Receptor Expression Requirement During Long-Term Memory
            Retrieval and Its Association with mTORC1 Signaling
  JOURNAL   Mol Neurobiol 58 (4), 1711-1722 (2021)
   PUBMED   33244735
  REMARK    GeneRIF: AMPA Receptor Expression Requirement During Long-Term
            Memory Retrieval and Its Association with mTORC1 Signaling.
REFERENCE   6  (residues 1 to 883)
  AUTHORS   Hume,R.I., Dingledine,R. and Heinemann,S.F.
  TITLE     Identification of a site in glutamate receptor subunits that
            controls calcium permeability
  JOURNAL   Science 253 (5023), 1028-1031 (1991)
   PUBMED   1653450
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Nakanishi,N., Shneider,N.A. and Axel,R.
  TITLE     A family of glutamate receptor genes: evidence for the formation of
            heteromultimeric receptors with distinct channel properties
  JOURNAL   Neuron 5 (5), 569-581 (1990)
   PUBMED   1699567
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Sommer,B., Keinanen,K., Verdoorn,T.A., Wisden,W., Burnashev,N.,
            Herb,A., Kohler,M., Takagi,T., Sakmann,B. and Seeburg,P.H.
  TITLE     Flip and flop: a cell-specific functional switch in
            glutamate-operated channels of the CNS
  JOURNAL   Science 249 (4976), 1580-1585 (1990)
   PUBMED   1699275
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Boulter,J., Hollmann,M., O'Shea-Greenfield,A., Hartley,M.,
            Deneris,E., Maron,C. and Heinemann,S.
  TITLE     Molecular cloning and functional expression of glutamate receptor
            subunit genes
  JOURNAL   Science 249 (4972), 1033-1037 (1990)
   PUBMED   2168579
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Keinanen,K., Wisden,W., Sommer,B., Werner,P., Herb,A.,
            Verdoorn,T.A., Sakmann,B. and Seeburg,P.H.
  TITLE     A family of AMPA-selective glutamate receptors
  JOURNAL   Science 249 (4968), 556-560 (1990)
   PUBMED   2166337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M38061.1, AF164344.1,
            CO400088.1 and JAXUCZ010000002.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to a family of glutamate receptors that are
            sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate
            (AMPA), and function as ligand-activated cation channels. These
            channels are assembled from 4 related subunits, Gria1-4. The
            subunit encoded by this gene (Gria2) is subject to RNA editing (Q/R
            and R/G), which is thought to render the channels impermeable to
            Ca(2+), and to affect the kinetic aspects of these channels in rat
            brain. Alternative splicing, resulting in transcript variants
            encoding different isoforms (flip and flop), has been noted for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1 (also known
            as the flip isoform). RNA editing changes Gln607Arg (CAG->CGG) and
            Arg764Gly (AGA->GGA).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF164344.1, X54655.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            undergoes RNA editing  :: PMID: 7992055, 12045112
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q33"
     Protein         1..883
                     /product="glutamate receptor 2 isoform 1 precursor"
                     /note="glutamate receptor B; AMPA-selective glutamate
                     receptor 2; glutamate receptor, ionotropic, AMPA 2"
                     /calculated_mol_wt=96135
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     Region          28..398
                     /region_name="PBP1_iGluR_AMPA_GluR2"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the GluR2 subunit of the
                     AMPA receptor; cd06389"
                     /db_xref="CDD:380612"
     Site            order(69..71,74..75,78,98..99,102..103,106,152,162,
                     165..166,169..170,177,179,198,329..331,333,335)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380612"
     Site            order(69..71,74..75,78,98..99,102..103,106,152,162,
                     165..166,169..170,177,179,198,329..331,333,335)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380612"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21317873; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            370
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19946266,
                     ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Region          413..794
                     /region_name="PBP2_iGluR_AMPA"
                     /note="The ligand-binding domain of the AMPA
                     (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic
                     acid) subtypes of ionotropic glutamate receptors, a member
                     of the type 2 periplasmic binding fold protein
                     superfamily; cd13715"
                     /db_xref="CDD:270433"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            order(452,456,503..504,507,512..515,750,768..769,772..777,
                     779,782)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            order(471,499..501,506,671,674..676,725..726,729,753)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            474
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            order(514..518,772,775,780..781,784)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270433"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            617..637
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            654
                     /site_type="other"
                     /note="Crucial to convey clamshell closure to channel
                     opening. /evidence=ECO:0000269|PubMed:25103405; propagated
                     from UniProtKB/Swiss-Prot (P19491.2)"
     Site            681
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:8848293; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG.
                     /evidence=ECO:0000269|PubMed:8848293; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            773
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            813..833
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            863
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Region          867..877
                     /region_name="Required for interaction with IQSEC1.
                     /evidence=ECO:0000269|PubMed:20547133"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:15240807,
                     ECO:0000269|PubMed:20547133; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     CDS             1..883
                     /gene="Gria2"
                     /gene_synonym="GluA2; gluR-B; GluR-K2; GluR2"
                     /coded_by="NM_017261.2:431..3082"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29627"
                     /db_xref="RGD:61862"
ORIGIN      
        1 mqkimhisvl lspvlwglif gvssnsiqig glfprgadqe ysafrvgmvq fstsefrltp
       61 hidnlevans favtnafcsq fsrgvyaifg fydkksvnti tsfcgtlhvs fitpsfptdg
      121 thpfviqmrp dlkgallsli eyyqwdkfay lydsdrglst lqavldsaae kkwqvtainv
      181 gninndkkde tyrslfqdle lkkerrvild cerdkvndiv dqvitigkhv kgyhyiianl
      241 gftdgdllki qfgganvsgf qivdyddslv skfierwstl eekeypgaht atikytsalt
      301 ydavqvmtea frnlrkqrie isrrgnagdc lanpavpwgq gveieralkq vqveglsgni
      361 kfdqngkrin ytinimelkt ngprkigyws evdkmvvtlt elpsgndtsg lenktvvvtt
      421 ilespyvmmk knhemlegne ryegycvdla aeiakhcgfk ykltivgdgk ygardadtki
      481 wngmvgelvy gkadiaiapl titlvreevi dfskpfmslg isimikkpqk skpgvfsfld
      541 playeiwmci vfayigvsvv lflvsrfspy ewhteefedg retqssestn efgifnslwf
      601 slgafmrqgc disprslsgr ivggvwwfft liiissytan laafltverm vspiesaedl
      661 skqteiaygt ldsgstkeff rrskiavfdk mwtymrsaep svfvrttaeg varvrkskgk
      721 yayllestmn eyieqrkpcd tmkvggnlds kgygiatpkg sslgtpvnla vlklseqgvl
      781 dklknkwwyd kgecgakdsg skektsalsl snvagvfyil vgglglamlv aliefcyksr
      841 aeakrmkvak npqninpsss qnsqnfatyk egynvygies vki
//
LOCUS       NP_001007015             357 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 4B [Rattus norvegicus].
ACCESSION   NP_001007015 XP_215168
VERSION     NP_001007015.2
DBSOURCE    REFSEQ: accession NM_001007014.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Kojima,S., Matsumoto,K., Hirose,M., Shimada,M., Nagano,M.,
            Shigeyoshi,Y., Hoshino,S., Ui-Tei,K., Saigo,K., Green,C.B.,
            Sakaki,Y. and Tei,H.
  TITLE     LARK activates posttranscriptional expression of an essential
            mammalian clock protein, PERIOD1
  JOURNAL   Proc Natl Acad Sci U S A 104 (6), 1859-1864 (2007)
   PUBMED   17264215
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Guo,D., Ling,J., Wang,M.H., She,J.X., Gu,J. and Wang,C.Y.
  TITLE     Physical interaction and functional coupling between ACDP4 and the
            intracellular ion chaperone COX11, an implication of the role of
            ACDP4 in essential metal ion transport and homeostasis
  JOURNAL   Mol Pain 1, 15 (2005)
   PUBMED   15840172
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Ishii,H., Vecchione,A., Furukawa,Y., Croce,C.M., Huebner,K. and
            Fong,L.Y.
  TITLE     Differentially expressed genes execute zinc-induced apoptosis in
            precancerous esophageal epithelium of zinc-deficient rats
  JOURNAL   Oncogene 23 (49), 8040-8048 (2004)
   PUBMED   15361827
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086416.1.
            
            On or before Jan 12, 2005 this sequence version replaced
            XP_215168.1, NP_001007015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086416.1, AY303541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..357
                     /product="RNA-binding protein 4B"
                     /note="RNA-binding protein 30; zinc-responsive protein
                     ZD7; RNA-binding motif protein 30"
                     /calculated_mol_wt=39860
     Region          2..68
                     /region_name="RRM1_RBM4"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 4 (RBM4); cd12606"
                     /db_xref="CDD:410018"
     Region          78..144
                     /region_name="RRM2_RBM4"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 4 (RBM4); cd12607"
                     /db_xref="CDD:410019"
     Region          <145..>181
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          161..176
                     /region_name="ZnF_C2HC"
                     /note="zinc finger; smart00343"
                     /db_xref="CDD:197667"
     Region          196..357
                     /region_name="Interaction with TNPO3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64LC9.2)"
     CDS             1..357
                     /gene="Rbm4b"
                     /coded_by="NM_001007014.2:117..1190"
                     /db_xref="GeneID:474154"
                     /db_xref="RGD:1359343"
ORIGIN      
        1 mvklfignlp reateqeirs lfeqygkvle cdiiknygfv hiedktaaed airnlhhykl
       61 hgvninveas knkskastkl hvgnisptct nqelrakfee ygpviecdiv kdyafvhmer
      121 aedaveairg ldntefqgkr mhvqlstsrl rtapgmgdqs gcyrcgkegh wskecpvdrt
      181 grvadfteqy neqygavrtp ytmgygesmy yndaygaldy ykryrvrsye avaaaaaasa
      241 ynyaeqtmsh lpqvqssavp shlnstsvdp ydrhllqnsg saatsaamaa aasssyygrd
      301 rsplrrnaav lptvgegygy gpesemsqas aatrnslydm aryereqyvd rarysaf
//
LOCUS       NP_001012175             227 aa            linear   ROD 27-APR-2025
DEFINITION  AN1-type zinc finger protein 3 [Rattus norvegicus].
ACCESSION   NP_001012175 XP_342110
VERSION     NP_001012175.1
DBSOURCE    REFSEQ: accession NM_001012175.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085956.1.
            
            On Feb 11, 2005 this sequence version replaced XP_342110.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085956.1, CK367635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..227
                     /product="AN1-type zinc finger protein 3"
                     /note="testis-expressed sequence 27; testis expressed gene
                     27; zinc finger, AN1-type domain 3; testis-expressed
                     protein 27"
                     /calculated_mol_wt=24951
     Region          <19..36
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          41..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2M7.1)"
     Region          174..>194
                     /region_name="CUZ1"
                     /note="CDC48-associated ubiquitin-like protein CUZ1,
                     contains AN1-type Zn-finger (protection from As/Sb
                     toxicity) [Defense mechanisms]; COG3582"
                     /db_xref="CDD:442801"
     CDS             1..227
                     /gene="Zfand3"
                     /gene_synonym="Tex27"
                     /coded_by="NM_001012175.1:122..805"
                     /db_xref="GeneID:361816"
                     /db_xref="RGD:1307113"
ORIGIN      
        1 mgdagsersk apslpprcpc gfwgssktmn lcskcfadfq kkqpdddstp stsnsqsdlf
       61 seettsdnnn tsvttptlsp sqqslpteln vtspseeecg pctdtahvsl itptkrscga
      121 dsqseseasp vkrprlvenp erpeesgrsk qksrrrcfqc qtklelvqqe lgscrcgyvf
      181 cmlhrlpeqh dctfdhmgrg reeaimkmvk ldrkvgrscq rigegcs
//
LOCUS       NP_620222                998 aa            linear   ROD 27-APR-2025
DEFINITION  hypoxia up-regulated protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_620222
VERSION     NP_620222.2
DBSOURCE    REFSEQ: accession NM_138867.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Abu El-Asrar,A.M., Ahmad,A., Alam,K., Bittoun,E., Siddiquei,M.M.,
            Mohammad,G., Mousa,A., De Hertogh,G. and Opdenakker,G.
  TITLE     Association of 150-kDa oxygen-regulated protein with vascular
            endothelial growth factor in proliferative diabetic retinopathy
  JOURNAL   Acta Ophthalmol 96 (4), e460-e467 (2018)
   PUBMED   29098793
  REMARK    GeneRIF: 150-kDa oxygen-regulated protein (ORP150) levels were
            significantly increased in rat retinas after induction of diabetes.
            Vascular endothelial growth factor (VEGF) and the pro-inflammatory
            cytokines interleukin-6 (IL-6) and tumour necrosis factor-alpha
            (TNF-alpha) induced upregulation of ORP150 in HRMEC.
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Cunningham,C.N., He,K., Arunagiri,A., Paton,A.W., Paton,J.C.,
            Arvan,P. and Tsai,B.
  TITLE     Chaperone-Driven Degradation of a Misfolded Proinsulin Mutant in
            Parallel With Restoration of Wild-Type Insulin Secretion
  JOURNAL   Diabetes 66 (3), 741-753 (2017)
   PUBMED   28028074
  REMARK    GeneRIF: Data reveal that Grp170 participates in preparing mutant
            proinsulin for degradation while enabling wild-type proinsulin
            escape from the endoplasmic reticulum.
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Wei,H., Wang,F., Wang,X., Yang,J., Li,Z., Cong,X. and Chen,X.
  TITLE     Lysophosphatidic acid promotes secretion of VEGF by increasing
            expression of 150-kD Oxygen-regulated protein (ORP150) in
            mesenchymal stem cells
  JOURNAL   Biochim Biophys Acta 1831 (8), 1426-1434 (2013)
   PUBMED   23707263
  REMARK    GeneRIF: LPA promotes VEGF secretion at the post-translation level
            by up-regulating ORP150 expression.
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Jansen,G., Maattanen,P., Denisov,A.Y., Scarffe,L., Schade,B.,
            Balghi,H., Dejgaard,K., Chen,L.Y., Muller,W.J., Gehring,K. and
            Thomas,D.Y.
  TITLE     An interaction map of endoplasmic reticulum chaperones and foldases
  JOURNAL   Mol Cell Proteomics 11 (9), 710-723 (2012)
   PUBMED   22665516
REFERENCE   5  (residues 1 to 998)
  AUTHORS   Deng,W.H., Chen,C., Wang,W.X., Yu,J., Li,J.Y. and Liu,L.
  TITLE     Effects of ORP150 on appearance and function of pancreatic beta
            cells following acute necrotizing pancreatitis
  JOURNAL   Pathol Res Pract 207 (6), 370-376 (2011)
   PUBMED   21536389
  REMARK    GeneRIF: Results imply a probable role of ORP150 in the changes in
            appearance and function of pancreatic beta cells following acute
            necrotizing pancreatitis, through the pathway of endoplasmic
            reticulum stress.
REFERENCE   6  (residues 1 to 998)
  AUTHORS   Bando,Y., Ogawa,S., Yamauchi,A., Kuwabara,K., Ozawa,K., Hori,O.,
            Yanagi,H., Tamatani,M. and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) functions as a novel
            molecular chaperone in MDCK cells
  JOURNAL   Am J Physiol Cell Physiol 278 (6), C1172-C1182 (2000)
   PUBMED   10837345
REFERENCE   7  (residues 1 to 998)
  AUTHORS   Ozawa,K., Kuwabara,K., Tamatani,M., Takatsuji,K., Tsukamoto,Y.,
            Kaneda,S., Yanagi,H., Stern,D.M., Eguchi,Y., Tsujimoto,Y., Ogawa,S.
            and Tohyama,M.
  TITLE     150-kDa oxygen-regulated protein (ORP150) suppresses
            hypoxia-induced apoptotic cell death
  JOURNAL   J Biol Chem 274 (10), 6397-6404 (1999)
   PUBMED   10037731
REFERENCE   8  (residues 1 to 998)
  AUTHORS   Matsushita,K., Matsuyama,T., Nishimura,H., Takaoka,T., Kuwabara,K.,
            Tsukamoto,Y., Sugita,M. and Ogawa,S.
  TITLE     Marked, sustained expression of a novel 150-kDa oxygen-regulated
            stress protein, in severely ischemic mouse neurons
  JOURNAL   Brain Res Mol Brain Res 60 (1), 98-106 (1998)
   PUBMED   9748521
REFERENCE   9  (residues 1 to 998)
  AUTHORS   Ikeda,J., Kaneda,S., Kuwabara,K., Ogawa,S., Kobayashi,T.,
            Matsumoto,M., Yura,T. and Yanagi,H.
  TITLE     Cloning and expression of cDNA encoding the human 150 kDa
            oxygen-regulated protein, ORP150
  JOURNAL   Biochem Biophys Res Commun 230 (1), 94-99 (1997)
   PUBMED   9020069
REFERENCE   10 (residues 1 to 998)
  AUTHORS   Kuwabara,K., Matsumoto,M., Ikeda,J., Hori,O., Ogawa,S., Maeda,Y.,
            Kitagawa,K., Imuta,N., Kinoshita,T., Stern,D.M., Yanagi,H. and
            Kamada,T.
  TITLE     Purification and characterization of a novel stress protein, the
            150-kDa oxygen-regulated protein (ORP150), from cultured rat
            astrocytes and its expression in ischemic mouse brain
  JOURNAL   J Biol Chem 271 (9), 5025-5032 (1996)
   PUBMED   8617779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U41853.1 and BC065310.1.
            
            On Oct 9, 2005 this sequence version replaced NP_620222.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC065310.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..998
                     /product="hypoxia up-regulated protein 1 precursor"
                     /note="hypoxia up-regulated protein 1; 150 kDa
                     oxygen-regulated protein; ORP-150; oxygen regulated
                     protein (150kD)"
                     /calculated_mol_wt=107645
     sig_peptide     1..32
                     /note="/evidence=ECO:0000269|PubMed:8617779,
                     ECO:0000269|PubMed:9020069; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
                     /calculated_mol_wt=3593
     Region          34..424
                     /region_name="ASKHA_NBD_HSP70_HYOU1"
                     /note="nucleotide-binding domain (NBD) of hypoxia
                     up-regulated protein 1 (HYOU1) and similar proteins;
                     cd10230"
                     /db_xref="CDD:466828"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          564..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63617.1)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4L1; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          <586..>691
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          <592..>800
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            830
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            862
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            869
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            883
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKR6; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            922
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Site            931
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q63617.1)"
     Region          995..998
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63617.1)"
     CDS             1..998
                     /gene="Hyou1"
                     /gene_synonym="Cab140; Orp150"
                     /coded_by="NM_138867.2:203..3199"
                     /db_xref="GeneID:192235"
                     /db_xref="RGD:621146"
ORIGIN      
        1 maatvrrqrp rrllcwalva vlladllals dtlavmsvdl gsesmkvaiv kpgvpmeivl
       61 nkesrrktpv tvtlkenerf lgdsaagmai knpkatlryf qhllgkqadn phvalyrsrf
      121 pehelnvdpq rqtvrfqisp qlqfspeevl gmvlnysrsl aedfaeqpik davitvpaff
      181 nqaerravlq aarmaglkvl qlindntata lsygvfrrkd instaqnimf ydmgsgstvc
      241 tivtyqtvkt keagtqpqlq irgvgfdrtl gglemelrlr ehlaklfneq rkgqkakdvr
      301 enpramakll reanrlktvl sanadhmaqi eglmddvdfk akvtrvefee lcadlfdrvp
      361 gpvqqalqsa emsldqieqv ilvggatrvp kvqevllkav gkeelgknin adeaaamgav
      421 yqaaalskaf kvkpfvvrda viypilveft reveeepglr slkhnkrvlf srmgpypqrk
      481 vitfnryshd fnfhinygdl gflgpedlrv fgsqnlttvk lkgvgesfkk ypdyeskgik
      541 ahfnldesgv lsldrvesvf etlvedspee estltklgnt isslfgggts sdakengtda
      601 vqeeeespae gskdepaeqg elkeeaeapm edtsqpppse pkgdaarege tpdekesgdk
      661 seaqkpnekg qagpegvppa peeekkqkpa rkqkmveeig velavldlpd lpedelahsv
      721 qkledltlrd lekqerekaa nsleafifet qdklyqpeyq evsteeqree isgklsatst
      781 wledegfgat tvmlkdklae lrklcqglff rveerrkwpe rlsaldnlln hssiflkgar
      841 lipemdqift dvemttlekv indtwtwkna tlaeqaklpa tekpvllskd ieakmmaldr
      901 evqyllnkak ftkprprpkd kngtrteppl nasagdqeek vipptgqtee akpilepdke
      961 tgtepadsep lelggpgaes eqaeqtagqk rplkndel
//
LOCUS       NP_001124044            1367 aa            linear   ROD 27-APR-2025
DEFINITION  tonsoku-like protein [Rattus norvegicus].
ACCESSION   NP_001124044 XP_001075280 XP_345851
VERSION     NP_001124044.1
DBSOURCE    REFSEQ: accession NM_001130572.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1367)
  AUTHORS   Chang,H.R., Cho,S.Y., Lee,J.H., Lee,E., Seo,J., Lee,H.R.,
            Cavalcanti,D.P., Makitie,O., Valta,H., Girisha,K.M., Lee,C.,
            Neethukrishna,K., Bhavani,G.S., Shukla,A., Nampoothiri,S.,
            Phadke,S.R., Park,M.J., Ikegawa,S., Wang,Z., Higgs,M.R.,
            Stewart,G.S., Jung,E., Lee,M.S., Park,J.H., Lee,E.A., Kim,H.,
            Myung,K., Jeon,W., Lee,K., Kim,D., Kim,O.H., Choi,M., Lee,H.W.,
            Kim,Y. and Cho,T.J.
  TITLE     Hypomorphic Mutations in TONSL Cause SPONASTRIME Dysplasia
  JOURNAL   Am J Hum Genet 104 (3), 439-453 (2019)
   PUBMED   30773278
REFERENCE   2  (residues 1 to 1367)
  AUTHORS   O'Connell,B.C., Adamson,B., Lydeard,J.R., Sowa,M.E., Ciccia,A.,
            Bredemeyer,A.L., Schlabach,M., Gygi,S.P., Elledge,S.J. and
            Harper,J.W.
  TITLE     A genome-wide camptothecin sensitivity screen identifies a
            mammalian MMS22L-NFKBIL2 complex required for genomic stability
  JOURNAL   Mol Cell 40 (4), 645-657 (2010)
   PUBMED   21055985
REFERENCE   3  (residues 1 to 1367)
  AUTHORS   Duro,E., Lundin,C., Ask,K., Sanchez-Pulido,L., MacArtney,T.J.,
            Toth,R., Ponting,C.P., Groth,A., Helleday,T. and Rouse,J.
  TITLE     Identification of the MMS22L-TONSL complex that promotes homologous
            recombination
  JOURNAL   Mol Cell 40 (4), 632-644 (2010)
   PUBMED   21055984
REFERENCE   4  (residues 1 to 1367)
  AUTHORS   O'Donnell,L., Panier,S., Wildenhain,J., Tkach,J.M., Al-Hakim,A.,
            Landry,M.C., Escribano-Diaz,C., Szilard,R.K., Young,J.T., Munro,M.,
            Canny,M.D., Kolas,N.K., Zhang,W., Harding,S.M., Ylanko,J.,
            Mendez,M., Mullin,M., Sun,T., Habermann,B., Datti,A., Bristow,R.G.,
            Gingras,A.C., Tyers,M.D., Brown,G.W. and Durocher,D.
  TITLE     The MMS22L-TONSL complex mediates recovery from replication stress
            and homologous recombination
  JOURNAL   Mol Cell 40 (4), 619-631 (2010)
   PUBMED   21055983
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473950.2.
            
            On or before Jul 28, 2008 this sequence version replaced
            XP_345851.2, XP_001075280.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1367
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..1367
                     /product="tonsoku-like protein"
                     /note="ikappaBR; I-kappa-B-related protein; inhibitor of
                     kappa B-related protein; NF-kappa-B inhibitor-like protein
                     2; nuclear factor of kappa light polypeptide gene enhancer
                     in B-cells inhibitor-like 2"
                     /calculated_mol_wt=151703
     Region          25..>234
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          27..60
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          27..55
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(28,31..32,35..36,38,68,71..72,75..76,78..79,108,
                     111..112,115..116,119)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          66..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..100
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          101..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          107..147
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          162..195
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Site            order(163,166..167,170..171,173,203,206..207,210..211,
                     213..214,243,246..247,250..251,254)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          163..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          195..237
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          197..450
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          202..235
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          242..275
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          242..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..344
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Site            order(316,319..320,322,353,356..357,360..361,363..364,391,
                     394..395,398..399,402)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          316..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          351..381
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          352..385
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          390..424
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          390..417
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          460..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          <523..>635
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(528,530,534..535,538..540,542..543,547,550,559,561,
                     563,567..568,571..573,575..576,580,583,592,597,599,
                     603..604,607..609,611..612,616,619)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          528..559
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          528..557
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          561..592
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          561..590
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          597..627
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          597..626
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          660..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          726..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Site            797
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZL6; propagated from
                     UniProtKB/Swiss-Prot (D4A615.1)"
     Region          798..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          841..910
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          <1055..1331
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          1062..1086
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1065..1092
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1090..1118
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1093..1124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1121..1144
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1125..1147
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1152..1183
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1181..1205
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1184..1208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1209..1242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1240..1263
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1243..1270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1268..1293
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     Region          1271..1293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1294..1321
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1324..1347
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A615.1)"
     CDS             1..1367
                     /gene="Tonsl"
                     /gene_synonym="Nfkbil2"
                     /coded_by="NM_001130572.1:68..4171"
                     /db_xref="GeneID:366953"
                     /db_xref="RGD:1307483"
ORIGIN      
        1 mtleqelrql skakaraqrn gqlceeavcc hqlgellash grfqealeeh qqelhllesv
       61 qdtlgcavah rkigerlaem enysaalkhq hlyldlagsl snhtelqraw atigrthldv
      121 ydhcqsrdsl lqaqaafeks laivdekleg mltqrelsem rtrlylnlgl tceslqqtaq
      181 cnnyfkksif laeqnhlyed lfrarynlga ihwrggqhsq amrclegare caramkmrfm
      241 eseccmlvsq vlqdlgdfla akralkkayr lgsqkpnqrv aicqslkyvl avvrlqqqlq
      301 eaegndlqga maiceqlgdl fskaddfpka seayqkqlhf aellnrpdle laviheslat
      361 tlgdmkdyhk avhhyeeelr lrkgnaleea ktwfniglar eeagdayell apcfqkafgc
      421 aqqaqryqlq rqilqhlytv qlklqpqear dteirlqels makdteeeee eeeeeeeeas
      481 ealetsemel seseddadgl sqqleeeeel qgcvgrrkin kwnrrndmge tllhracieg
      541 qlrrvqdlvk qghplnprdy cgwtplheac nyghleivrf lldhgaavdd pggqgcdgit
      601 plhdalncgh fevaellier gasvtlrtrk glspletlqq wvklyfrdld letrqkaasm
      661 errlqmassg qashsspalq tipnnhlfdp etsppsspcp kppsytprpp easpapakvf
      721 leetvsavcr prknrhrpas sssssedddd ntnpcrpsqk rlrhstqqge aktpdpsksr
      781 etaissacra ayqaairgvg saqsrrlvps lprgsnevpa pktalipeee flaeewlevd
      841 tpltrsssss rpstsisdye rcparprtra kqsrpasldg wctrtkaada sltaeptens
      901 smprttgpnk encaagqpll lvqpppirvr vqiqdnlfli pvphsdvhsv awlaeqaaqr
      961 yfqtcgllpr ltlrkdgall apqdpipdvl qsndevmaev tswdlpplkd ryrracqslg
     1021 qgehqqvlqa mehqssspsf sacslalcqa qltpllralk lhtalrelrl sgnrlgdpca
     1081 tellatlgtm pnlvlldlss nhlgpeglrq lvegslgqta fqnveeldls mnplgdgcaq
     1141 alasllrtcp vlrtlrlqac gfspsfflsh qaalgsafkd aehlktlsls yntlgapala
     1201 rvlqslptct llhlelssva asksnsslie pvikyltkeg calahltlsa nclsdkavre
     1261 lsrclpscps ltsldlsanp evscagleel lsalqerpqg lsffdlsgcs iqgplnsdlw
     1321 dkilsqlqel qlcskdlttk drdtlcqrlp agactlnqgs klffkcl
//
LOCUS       NP_808792                848 aa            linear   ROD 27-APR-2025
DEFINITION  origin recognition complex subunit 1 [Rattus norvegicus].
ACCESSION   NP_808792
VERSION     NP_808792.1
DBSOURCE    REFSEQ: accession NM_177931.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Shen,Z., Sathyan,K.M., Geng,Y., Zheng,R., Chakraborty,A.,
            Freeman,B., Wang,F., Prasanth,K.V. and Prasanth,S.G.
  TITLE     A WD-repeat protein stabilizes ORC binding to chromatin
  JOURNAL   Mol Cell 40 (1), 99-111 (2010)
   PUBMED   20932478
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Shu,M.Q., Qin,Y.L. and Jiang,M.H.
  TITLE     RNA interference targeting ORC1 gene suppresses the proliferation
            of vascular smooth muscle cells in rats
  JOURNAL   Exp Mol Pathol 84 (3), 206-212 (2008)
   PUBMED   18499104
  REMARK    GeneRIF: ORC1 gene silencing causes rat VSMCs to enter a reversible
            G(0) quiescent, growth arrested state; thus, ORC1 gene may be an
            important new target for suppressing VSMCs proliferation.
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Siddiqui,K. and Stillman,B.
  TITLE     ATP-dependent assembly of the human origin recognition complex
  JOURNAL   J Biol Chem 282 (44), 32370-32383 (2007)
   PUBMED   17716973
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Minami,H., Takahashi,J., Suto,A., Saitoh,Y. and Tsutsumi,K.
  TITLE     Binding of AlF-C, an Orc1-binding transcriptional regulator,
            enhances replicator activity of the rat aldolase B origin
  JOURNAL   Mol Cell Biol 26 (23), 8770-8780 (2006)
   PUBMED   16982680
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Miyake,Y., Mizuno,T., Yanagi,K. and Hanaoka,F.
  TITLE     Novel splicing variant of mouse Orc1 is deficient in nuclear
            translocation and resistant for proteasome-mediated degradation
  JOURNAL   J Biol Chem 280 (13), 12643-12652 (2005)
   PUBMED   15634681
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Natale,D.A., Li,C.J., Sun,W.H. and DePamphilis,M.L.
  TITLE     Selective instability of Orc1 protein accounts for the absence of
            functional origin recognition complexes during the M-G(1)
            transition in mammals
  JOURNAL   EMBO J 19 (11), 2728-2738 (2000)
   PUBMED   10835370
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB105378.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB105378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132296, SAMD00132297
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..848
                     /product="origin recognition complex subunit 1"
                     /calculated_mol_wt=95629
     Region          43..169
                     /region_name="BAH_Orc1p_animal"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1
                     is part of the Yeast Sir1-origin recognition complex. The
                     Orc1p BAH doman functions in epigenetic silencing. In
                     vertebrates, a similar ORC...; cd04719"
                     /db_xref="CDD:240070"
     Site            93
                     /site_type="other"
                     /note="Histone H4K20me2 binding.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          189..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          261..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            314
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1N2; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          344..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          388..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13415; propagated from
                     UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          426..>536
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Region          <482..773
                     /region_name="PTZ00112"
                     /note="origin recognition complex 1 protein; Provisional"
                     /db_xref="CDD:240274"
     Region          488..848
                     /region_name="Necessary and sufficient for ORC complex
                     assembly. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80Z32.1)"
     Region          765..844
                     /region_name="Cdc6_C"
                     /note="CDC6, C terminal winged helix domain; pfam09079"
                     /db_xref="CDD:462672"
     CDS             1..848
                     /gene="Orc1"
                     /gene_synonym="Orc1l"
                     /coded_by="NM_177931.2:1..2547"
                     /db_xref="GeneID:313479"
                     /db_xref="RGD:631435"
ORIGIN      
        1 mpsyvtrqkt rqtfswvgrp lpnrkqfyqm ykeicmking cseihikvgq fvliqgednq
       61 kpyvakliel fengsevppk kyarvqwfvr fceipipkrh llgrrpsaqe ifwydcsdcd
      121 ndihvetiig pvqvvalape deipvnqkse etlfvklswn kknfaplppe elaalrrlec
      181 qkpleaktks vkspswstae qevkriessh stsrsyqdpa htvtpnamks lecggftrkp
      241 nmrlsrkilc dsldsqktck rraafsetts ppkkpqpgei ktssaletlg knghtqpffa
      301 kssmvlrtrg tavkttkltv esalspvrsr srysvapsvg ltpqyigrka keqethkepi
      361 htslrarrrs slltlkrikq qlwlldddks dqeeeesiss vevsdsssee edesvpsppt
      421 gkpvgqsrtr rtaskpssqt pskspkktfr prpplhatpq irdrnlavqe pasvleearl
      481 rlhvsavpds lpcreqefqd iysfveskll dgtggcmyis gvpgtgktat vhevirclqq
      541 aaqtndvppf eyvevngmkl tephqvyvqi lqkltgqkat anhaaellak qfcsrgsqke
      601 ttvllvdeld llwthkqdvl ynlfdwpthk garlvvltia ntmdlperim mnrvasrlgl
      661 trmsfqpysh sqlkqilvsr lkhlkafedd avqlvarkva alsgdarrcl dicrrateic
      721 evshqrgdsq clvtvahlme aidemfsssy itaiknssvl eqsflraiia efrrsgleea
      781 tfqqiysqhv alcrmeglpy ptmsetmavc srlgscrill vepsrndlll rvrlnvsqnd
      841 vlyalkee
//
LOCUS       NP_001007693             414 aa            linear   ROD 27-APR-2025
DEFINITION  NFATC2-interacting protein [Rattus norvegicus].
ACCESSION   NP_001007693 XP_219329
VERSION     NP_001007693.1
DBSOURCE    REFSEQ: accession NM_001007692.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Zhao,L., Qian,X., Ren,Z. and Wang,A.
  TITLE     miR-31-5p suppresses myocardial hypertrophy by targeting Nfatc2ip
  JOURNAL   J Cell Mol Med 28 (12), e18413 (2024)
   PUBMED   38894694
  REMARK    GeneRIF: miR-31-5p suppresses myocardial hypertrophy by targeting
            Nfatc2ip.
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Bettelli,E., Dastrange,M. and Oukka,M.
  TITLE     Foxp3 interacts with nuclear factor of activated T cells and
            NF-kappa B to repress cytokine gene expression and effector
            functions of T helper cells
  JOURNAL   Proc Natl Acad Sci U S A 102 (14), 5138-5143 (2005)
   PUBMED   15790681
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Rengarajan,J., Mittelstadt,P.R., Mages,H.W., Gerth,A.J.,
            Kroczek,R.A., Ashwell,J.D. and Glimcher,L.H.
  TITLE     Sequential involvement of NFAT and Egr transcription factors in
            FasL regulation
  JOURNAL   Immunity 12 (3), 293-300 (2000)
   PUBMED   10755616
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hodge,M.R., Chun,H.J., Rengarajan,J., Alt,A., Lieberson,R. and
            Glimcher,L.H.
  TITLE     NF-AT-Driven interleukin-4 transcription potentiated by NIP45
  JOURNAL   Science 274 (5294), 1903-1905 (1996)
   PUBMED   8943202
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079050.1.
            
            On Nov 29, 2004 this sequence version replaced XP_219329.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..414
                     /product="NFATC2-interacting protein"
                     /note="nuclear factor of activated T-cells, cytoplasmic
                     2-interacting protein; nuclear factor of activated
                     T-cells, cytoplasmic, calcineurin-dependent 2 interacting
                     protein"
                     /calculated_mol_wt=45299
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Region          63..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09130; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Region          139..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Region          258..330
                     /region_name="Ubl_SLD1_NFATC2ip"
                     /note="SUMO-like domain 1 (SLD1), structurally similar to
                     a beta-grasp ubiquitin-like fold, found in nuclear factor
                     of activated T-cells 2 interacting protein (NFATC2ip) and
                     similar proteins; cd17078"
                     /db_xref="CDD:340598"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Region          341..413
                     /region_name="Ubl_SLD2_NFATC2ip"
                     /note="SUMO-like domain 2 (SLD2), structurally similar to
                     a beta-grasp ubiquitin-like fold, found in nuclear factor
                     of activated T-cells 2 interacting protein (NFATC2ip) and
                     similar proteins; cd17079"
                     /db_xref="CDD:340599"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NCF5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG7.1)"
     CDS             1..414
                     /gene="Nfatc2ip"
                     /coded_by="NM_001007692.1:122..1366"
                     /db_xref="GeneID:308983"
                     /db_xref="RGD:1359096"
ORIGIN      
        1 maeplrrrgp rsrggrasrg arraraargr cpraprsptr lipdtvlvdl vsdsdeevle
       61 vvadpgevpv arlpapaape qdsdsdsega aegpagaprt lvrrrrrlld pgeapvvpvy
      121 sgkvqsslnl ipdnssllkl cpsepedead ltdsgsppse dalppgspwk kklrkkheke
      181 ekkmeefpdq displpqpss rnksrkhtea lqklrevnkr lqdlrsclsp kqhqspalqn
      241 tddevvlveg svlpqnprlf tlkircradl vrlpvktsep lqnvvdhmas hlgvspnril
      301 llfgetelsp tatprtlklg vadiidcvvl asssedtets qelrlrvqgk ekhqmleisl
      361 spdsplkvlm shyeeamgls ghklsfffdg tklsgkelpt dlglesgdli evwg
//
LOCUS       NP_997706                707 aa            linear   ROD 27-APR-2025
DEFINITION  choline transporter-like protein 4 [Rattus norvegicus].
ACCESSION   NP_997706 XP_215344
VERSION     NP_997706.1
DBSOURCE    REFSEQ: accession NM_212541.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Ma,Z., Xia,W., Liu,F., Ma,J., Sun,S., Zhang,J., Jiang,N., Wang,X.,
            Hu,J. and Ma,D.
  TITLE     SLC44A4 mutation causes autosomal dominant hereditary postlingual
            non-syndromic mid-frequency hearing loss
  JOURNAL   Hum Mol Genet 26 (2), 383-394 (2017)
   PUBMED   28013291
  REMARK    Erratum:[Hum Mol Genet. 2017 Aug 15;26(16):3234. doi:
            10.1093/hmg/ddx232. PMID: 28859437]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Nabokina,S.M., Inoue,K., Subramanian,V.S., Valle,J.E., Yuasa,H. and
            Said,H.M.
  TITLE     Molecular identification and functional characterization of the
            human colonic thiamine pyrophosphate transporter
  JOURNAL   J Biol Chem 289 (7), 4405-4416 (2014)
   PUBMED   24379411
  REMARK    Erratum:[J Biol Chem. 2017 Oct 6;292(40):16526. doi:
            10.1074/jbc.A113.528257. PMID: 28986434]
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Song,P., Rekow,S.S., Singleton,C.A., Sekhon,H.S., Dissen,G.A.,
            Zhou,M., Campling,B., Lindstrom,J. and Spindel,E.R.
  TITLE     Choline transporter-like protein 4 (CTL4) links to non-neuronal
            acetylcholine synthesis
  JOURNAL   J Neurochem 126 (4), 451-461 (2013)
   PUBMED   23651124
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Traiffort,E., Ruat,M., O'Regan,S. and Meunier,F.M.
  TITLE     Molecular characterization of the family of choline
            transporter-like proteins and their splice variants
  JOURNAL   J Neurochem 92 (5), 1116-1125 (2005)
   PUBMED   15715662
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883045.1.
            
            On Aug 30, 2004 this sequence version replaced XP_215344.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079178.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..707
                     /product="choline transporter-like protein 4"
                     /note="thiamine pyrophosphate transporter 1"
                     /calculated_mol_wt=78606
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q53GD3; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q53GD3; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            308..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Region          312..672
                     /region_name="Choline_transpo"
                     /note="Plasma-membrane choline transporter; pfam04515"
                     /db_xref="CDD:461337"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q53GD3; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q53GD3; propagated from
                     UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            453..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            499..519
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            558..578
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            595..615
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     Site            636..656
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG71.1)"
     CDS             1..707
                     /gene="Slc44a4"
                     /gene_synonym="Ng22"
                     /coded_by="NM_212541.1:8..2131"
                     /db_xref="GeneID:294255"
                     /db_xref="RGD:1303167"
ORIGIN      
        1 mgkkqkenea ygnsakydps frgpiknrgc tdiiccvlfl vfilgyivvg lvawvygdpr
       61 qvlyprnstg aycgvgdnkd kpyvlyfnil scaaainvis iaenglqcpt pqvcvsscpq
      121 tpwvvegfql sntvgdvyke yrnfcvpavs pdmvvmdslq kglcpsfllp stpalgrcfp
      181 lpninftlpe qlqinnttvs kgisglldsi nardvsvkif edfaqswywi lvalgvalvl
      241 sllfilllrl vaaplvllli vgvlavlayg iyhcwqqyre lrdqgvsitq lgftanlsay
      301 qnvketwlaa liilavlegv lllmliflrq ririaiallk easravgqmm stmfyplvtf
      361 vllvicigyw avtalylats gqpqyvywvh ntstpgcekv lvnvscdpma plnsscpelk
      421 ctftgysssg laqrslfnlq iygilglfwt vnwvlalgqc vlagafasfy wafhkprdip
      481 tfplssafir tlryhtgsla fgaliltlvq iarvileyid hklrgsqnpv arciiccfkc
      541 clwclekfik flnrnayimi aiygknfcvs aknafmllmr nvvrvvvldk vtdlllffgk
      601 llvvggvgvl sffffsgrik glgkdfknpd lnyywlpimt simgayvias gffsvfgmcv
      661 dtlflcfled lerndgsqer pyympkallk ilgkknevpt ggknrkk
//
LOCUS       NP_001012018             344 aa            linear   ROD 27-APR-2025
DEFINITION  beta-1,4-galactosyltransferase 4 [Rattus norvegicus].
ACCESSION   NP_001012018 XP_221439
VERSION     NP_001012018.1
DBSOURCE    REFSEQ: accession NM_001012018.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081866.1.
            
            On Feb 11, 2005 this sequence version replaced XP_221439.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081866.1, SRR8487227.81253.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..344
                     /product="beta-1,4-galactosyltransferase 4"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.275"
                     /note="b4Gal-T4; beta4Gal-T4; beta-1,4-GalTase 4;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 4; UDP-Gal:betaGlcNAc beta
                     1,4-galactosyltransferase, polypeptide 4; nal synthase;
                     N-acetyllactosamine synthase; lactotriaosylceramide
                     beta-1,4-galactosyltransferase;
                     beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=39576
     Site            13..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HH1.1)"
     Region          122..339
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(129,131,133,168,194..196)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(194,196,289)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66HH1.1)"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66HH1.1)"
     CDS             1..344
                     /gene="B4galt4"
                     /coded_by="NM_001012018.1:242..1276"
                     /db_xref="GeneID:303923"
                     /db_xref="RGD:1307880"
ORIGIN      
        1 mgcnppylls yrlrllllft lcltvlgwat snyfvgaiqv ipraknfmat lhkvmylgne
       61 etlghgaamk kaelancpsv spnlrgqnkl vfkpdltlee vqaknpkvsr gryrpeecka
      121 lqrvavliph rnrekhliyl lehlhpflqr qqldygiyvi hqtgskkfnr akllnvgyle
      181 alkeenwdcf ifhdvdlvpe ndfnlytcgd qpkhlvvgrn stgyrlrysk yfggvtalsr
      241 eqffkvngfs nnywgwgged ddlrlrvelh kmkisrpkpd vgkytmifht rdkgnevngs
      301 rmkllqqmsr vwktdglssc syrllsvehn plyanitvdf wtaa
//
LOCUS       NP_847900                503 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 184C [Rattus norvegicus].
ACCESSION   NP_847900
VERSION     NP_847900.1
DBSOURCE    REFSEQ: accession NM_178330.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY228474.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY228474.1, BC089112.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..503
                     /product="transmembrane protein 184C"
                     /note="transmembrane protein 34; DNA sequence AY228474"
                     /calculated_mol_wt=57786
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Region          44..330
                     /region_name="DUF300 domain"
     Region          48..317
                     /region_name="Solute_trans_a"
                     /note="Organic solute transporter Ostalpha; pfam03619"
                     /db_xref="CDD:460991"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Region          358..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     Region          479..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810F5.1)"
     CDS             1..503
                     /gene="Tmem184c"
                     /gene_synonym="Tmem34"
                     /coded_by="NM_178330.1:457..1968"
                     /db_xref="GeneID:291946"
                     /db_xref="RGD:727852"
ORIGIN      
        1 mpcacnrnnw rkwirpllil lyalailvtv pvciwefqkl kvgihtkvwf iagiflllti
       61 pvsmcgilqh lvhytqpelq kpiirilwmv piysldswva lkypkiaiyv dtwrecyeay
      121 viynfmiflt nyltirfpnl mlhleakdqq nhlpplcccp pwamgemllf rcklgvlqyt
      181 vvrpittvts lvceilgvyd egnfsfsnaw tylvilnnls qlfamyclll fykvlkeels
      241 piqpvgkflc vklvvfvsfw qavliallvk vgvisekrtw ewqsaeavat glqdfiicie
      301 mffaaiahhy tfsykpyvhe aeegpcfdsf lamwdvsdir ediseqvrrv grtmrgypkk
      361 kcfpgdpdhn ehssllsass qdsskpsspv glyqgfgqti tsqspisian lyeeilneip
      421 eeqqrlysgq ditmdipeeq prhdtgqdvv hlpyrqelpy knhyqdhiqt vtsryllssp
      481 kpsddividf sdspegsdss tds
//
LOCUS       NP_062171                517 aa            linear   ROD 27-APR-2025
DEFINITION  acetylcholine receptor subunit delta precursor [Rattus norvegicus].
ACCESSION   NP_062171
VERSION     NP_062171.1
DBSOURCE    REFSEQ: accession NM_019298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Witzemann,V., Chevessier,F., Pacifici,P.G. and Yampolsky,P.
  TITLE     The neuromuscular junction: selective remodeling of synaptic
            regulators at the nerve/muscle interface
  JOURNAL   Mech Dev 130 (6-8), 402-411 (2013)
   PUBMED   23032192
  REMARK    Review article
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Rasoulpour,R.J., Ellis-Hutchings,R.G., Terry,C., Millar,N.S.,
            Zablotny,C.L., Gibb,A., Marshall,V., Collins,T., Carney,E.W. and
            Billington,R.
  TITLE     A novel mode-of-action mediated by the fetal muscle nicotinic
            acetylcholine receptor resulting in developmental toxicity in rats
  JOURNAL   Toxicol Sci 127 (2), 522-534 (2012)
   PUBMED   22461452
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Alberola-Die,A., Martinez-Pinna,J., Gonzalez-Ros,J.M., Ivorra,I.
            and Morales,A.
  TITLE     Multiple inhibitory actions of lidocaine on Torpedo nicotinic
            acetylcholine receptors transplanted to Xenopus oocytes
  JOURNAL   J Neurochem 117 (6), 1009-1019 (2011)
   PUBMED   21480901
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Albuquerque,E.X., Pereira,E.F., Alkondon,M. and Rogers,S.W.
  TITLE     Mammalian nicotinic acetylcholine receptors: from structure to
            function
  JOURNAL   Physiol Rev 89 (1), 73-120 (2009)
   PUBMED   19126755
  REMARK    Review article
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Michalk,A., Stricker,S., Becker,J., Rupps,R., Pantzar,T.,
            Miertus,J., Botta,G., Naretto,V.G., Janetzki,C., Yaqoob,N.,
            Ott,C.E., Seelow,D., Wieczorek,D., Fiebig,B., Wirth,B.,
            Hoopmann,M., Walther,M., Korber,F., Blankenburg,M., Mundlos,S.,
            Heller,R. and Hoffmann,K.
  TITLE     Acetylcholine receptor pathway mutations explain various fetal
            akinesia deformation sequence disorders
  JOURNAL   Am J Hum Genet 82 (2), 464-476 (2008)
   PUBMED   18252226
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Keller,S.H., Lindstrom,J. and Taylor,P.
  TITLE     Involvement of the chaperone protein calnexin and the acetylcholine
            receptor beta-subunit in the assembly and cell surface expression
            of the receptor
  JOURNAL   J Biol Chem 271 (37), 22871-22877 (1996)
   PUBMED   8798466
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Chahine,K.G., Walke,W. and Goldman,D.
  TITLE     A 102 base pair sequence of the nicotinic acetylcholine receptor
            delta-subunit gene confers regulation by muscle electrical activity
  JOURNAL   Development 115 (1), 213-219 (1992)
   PUBMED   1638981
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Witzemann,V., Stein,E., Barg,B., Konno,T., Koenen,M., Kues,W.,
            Criado,M., Hofmann,M. and Sakmann,B.
  TITLE     Primary structure and functional expression of the alpha-, beta-,
            gamma-, delta- and epsilon-subunits of the acetylcholine receptor
            from rat muscle
  JOURNAL   Eur J Biochem 194 (2), 437-448 (1990)
   PUBMED   1702709
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Gu,Y., Franco,A. Jr., Gardner,P.D., Lansman,J.B., Forsayeth,J.R.
            and Hall,Z.W.
  TITLE     Properties of embryonic and adult muscle acetylcholine receptors
            transiently expressed in COS cells
  JOURNAL   Neuron 5 (2), 147-157 (1990)
   PUBMED   2383398
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Porter,C.W., Barnard,E.A. and Chiu,T.H.
  TITLE     The ultrastructural localization and quantitation of cholinergic
            receptors at the mouse motor endplate
  JOURNAL   J Membr Biol 14 (4), 383-402 (1973)
   PUBMED   4781450
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X74835.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X74835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..517
                     /product="acetylcholine receptor subunit delta precursor"
                     /note="cholinergic receptor, nicotinic, delta polypeptide;
                     nicotinic acetylcholine receptor delta-subunit;
                     acetylcholine receptor subunit delta; cholinergic
                     receptor, nicotinic, delta (muscle); cholinergic receptor,
                     nicotinic delta"
                     /calculated_mol_wt=56890
     sig_peptide     1..21
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P25110.1)"
                     /calculated_mol_wt=2012
     mat_peptide     22..517
                     /product="acetylcholine receptor subunit delta"
                     /calculated_mol_wt=56890
     Region          26..246
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(62,64,70..71,78,100,102,111..112,114,116..117,
                     128..130,132,142,144,146,150,172,245)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349829"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25110.1)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25110.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25110.1)"
     Site            246..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25110.1)"
     Region          253..489
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            278..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25110.1)"
     Site            312..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25110.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by Tyr-kinases.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P25110.1)"
     Site            472..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25110.1)"
     CDS             1..517
                     /gene="Chrnd"
                     /coded_by="NM_019298.1:1..1554"
                     /db_xref="GeneID:54240"
                     /db_xref="RGD:2352"
ORIGIN      
        1 magpvptlgl laalvvcgsw glneeqrliq hlfeekgynk elrpvarked ivdvalsltl
       61 snlislkeve etlttnvwid hawidsrlqw nanefgnitv lrlpsdmvwl peivlennnd
      121 gsfqisyacn vlvsdsghvt wlppaifrss cpisvtyfpf dwqncslkfs slkytakeir
      181 lslkqeeedn rsypiewiii dpegftenge weivhraakv nvdpsvpmds tnhqdvtfyl
      241 iirrkplfyi inilvpcvli sfminlvfyl pgdcgektsv aisvllaqsv fllliskrlp
      301 atsmaiplvg kfllfgmvlv tmvvvicviv lnihfrtpst hvlsegvkkf fletlpkllh
      361 msrpeeedpg pralirrtss lgyiskaeey fslksrsdlm fekqserhgl arrlttarkp
      421 passeqvqqe lfnemkpavd ganfivnhmr dqnsyneekd nwnqvartvd rlclfvvtpv
      481 mvvgtawifl qgvynqpppq pfpgdpfsyd eqdrrfi
//
LOCUS       NP_955787                509 aa            linear   ROD 27-APR-2025
DEFINITION  DAP3-binding cell death enhancer 1 [Rattus norvegicus].
ACCESSION   NP_955787 XP_225996
VERSION     NP_955787.1
DBSOURCE    REFSEQ: accession NM_199493.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Harada,T., Iwai,A. and Miyazaki,T.
  TITLE     Identification of DELE, a novel DAP3-binding protein which is
            crucial for death receptor-mediated apoptosis induction
  JOURNAL   Apoptosis 15 (10), 1247-1255 (2010)
   PUBMED   20563667
  REMARK    GeneRIF: Functionally characterizes the human homolog as a
            DAP3-binding protein involved in apoptosis mediated by death
            receptors.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC064660.1.
            
            On Jan 23, 2004 this sequence version replaced XP_225996.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064660.1, FQ211991.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 20563667
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..509
                     /product="DAP3-binding cell death enhancer 1"
                     /note="death ligand signal enhancer; SEL1 domain
                     containing protein RGD735029; DAP3-binding cell death
                     enhancer 1, long form"
                     /calculated_mol_wt=52717
     transit_peptide 1..23
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P60924.2)"
                     /calculated_mol_wt=2551
     Region          19..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     mat_peptide     102..509
                     /product="DAP3-binding cell death enhancer 1.
                     /id=PRO_0000050723"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
                     /calculated_mol_wt=44151
     Region          143..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          213..245
                     /region_name="TPR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          246..278
                     /region_name="TPR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          <261..418
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          261..290
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          279..313
                     /region_name="TPR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          297..326
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          307..326
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000250|UniProtKB:Q14154"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          314..351
                     /region_name="TPR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          352..385
                     /region_name="TPR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          369..398
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          386..423
                     /region_name="TPR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     Region          470..498
                     /region_name="TPR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P60924.2)"
     CDS             1..509
                     /gene="Dele1"
                     /gene_synonym="Dele; DELE1(L); RGD735029"
                     /coded_by="NM_199493.1:42..1571"
                     /db_xref="GeneID:307480"
                     /db_xref="RGD:735029"
ORIGIN      
        1 mwrltgilgr alprllgpgf rgitpkptss dgpqttsttl llprvnfdrs gshgskrnrd
       61 pkccgwkeaf hwmsahvspn tlrdavswgt lavlalhlar qihfhaplva gpqsaercsw
      121 hsplyrflss swwhphsslr ryvlpspdcp aprntglrep rlgqeepaar sqglpsdssl
      181 kpgllnlpee epsdfgflna srdftsqaka aeagppggkn eqdkpkalpl eeavtsiqql
      241 fqlsvaiafn flgteniktg dytaafsyfq kaadrgyska qynvglcleh grgtprdlsk
      301 avlfyhlaav qghslaqyry arcllqspgs msdperqrav sllkqaadsg lteaqaflgv
      361 lftkephlde qkavkyfwla asngdsqsrf hlgicyekgl gvqrnlgeav kcyqksaamg
      421 nepaqerlrt lfnveaagps hlaiglksfs spslcslntf lagasglpha sstgnlgllc
      481 rsghlgtshg apsrampsle rslvrlgfg
//
LOCUS       NP_036724                424 aa            linear   ROD 27-APR-2025
DEFINITION  isovaleryl-CoA dehydrogenase, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_036724
VERSION     NP_036724.1
DBSOURCE    REFSEQ: accession NM_012592.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Liu,X., Wu,L., Deng,G., Chen,G., Li,N., Chu,X. and Li,D.
  TITLE     Comparative studies of Acyl-CoA dehydrogenases for monomethyl
            branched chain substrates in amino acid metabolism
  JOURNAL   Bioorg Chem 47, 1-8 (2013)
   PUBMED   23474214
  REMARK    GeneRIF: Isovaleryl-CoA dehydrogenase has relatively broader
            substrate specificity than those of the other two enzymes in
            accommodating various substrate analogs.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Vockley,J., Rogan,P.K., Anderson,B.D., Willard,J., Seelan,R.S.,
            Smith,D.I. and Liu,W.
  TITLE     Exon skipping in IVD RNA processing in isovaleric acidemia caused
            by point mutations in the coding region of the IVD gene
  JOURNAL   Am J Hum Genet 66 (2), 356-367 (2000)
   PUBMED   10677295
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Tiffany,K.A., Roberts,D.L., Wang,M., Paschke,R., Mohsen,A.W.,
            Vockley,J. and Kim,J.J.
  TITLE     Structure of human isovaleryl-CoA dehydrogenase at 2.6 A
            resolution: structural basis for substrate specificity,
  JOURNAL   Biochemistry 36 (28), 8455-8464 (1997)
   PUBMED   9214289
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Mohsen,A.W. and Vockley,J.
  TITLE     Identification of the active site catalytic residue in human
            isovaleryl-CoA dehydrogenase
  JOURNAL   Biochemistry 34 (32), 10146-10152 (1995)
   PUBMED   7640268
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Vockley,J., Parimoo,B. and Tanaka,K.
  TITLE     Molecular characterization of four different classes of mutations
            in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric
            acidemia
  JOURNAL   Am J Hum Genet 49 (1), 147-157 (1991)
   PUBMED   2063866
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Matsubara,Y., Indo,Y., Naito,E., Ozasa,H., Glassberg,R.,
            Vockley,J., Ikeda,Y., Kraus,J. and Tanaka,K.
  TITLE     Molecular cloning and nucleotide sequence of cDNAs encoding the
            precursors of rat long chain acyl-coenzyme A, short chain
            acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence
            homology of four enzymes of the acyl-CoA dehydrogenase family
  JOURNAL   J Biol Chem 264 (27), 16321-16331 (1989)
   PUBMED   2777793
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Kraus,J.P., Matsubara,Y., Barton,D., Yang-Feng,T.L., Glassberg,R.,
            Ito,M., Ikeda,Y., Mole,J., Francke,U. and Tanaka,K.
  TITLE     Isolation of cDNA clones coding for rat isovaleryl-CoA
            dehydrogenase and assignment of the gene to human chromosome 15
  JOURNAL   Genomics 1 (3), 264-269 (1987)
   PUBMED   3446585
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Finocchiaro,G., Ito,M. and Tanaka,K.
  TITLE     Purification and properties of short chain acyl-CoA, medium chain
            acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver
  JOURNAL   J Biol Chem 262 (17), 7982-7989 (1987)
   PUBMED   3597357
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Ikeda,Y., Keese,S.M., Fenton,W.A. and Tanaka,K.
  TITLE     Biosynthesis of four rat liver mitochondrial acyl-CoA
            dehydrogenases: in vitro synthesis, import into mitochondria, and
            processing of their precursors in a cell-free system and in
            cultured cells
  JOURNAL   Arch Biochem Biophys 252 (2), 662-674 (1987)
   PUBMED   3813556
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088401.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088401.1, J05031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..424
                     /product="isovaleryl-CoA dehydrogenase, mitochondrial
                     precursor"
                     /EC_number="1.3.8.4"
                     /EC_number="1.3.8.1"
                     /note="isovaleryl-CoA dehydrogenase, mitochondrial;
                     isovaleryl coenzyme A dehydrogenase; butyryl-CoA
                     dehydrogenase"
                     /calculated_mol_wt=43098
     transit_peptide 1..30
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:2777793; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
                     /calculated_mol_wt=3356
     mat_peptide     31..424
                     /product="Isovaleryl-CoA dehydrogenase, mitochondrial.
                     /id=PRO_0000000534"
                     /note="propagated from UniProtKB/Swiss-Prot (P12007.2)"
                     /calculated_mol_wt=43098
     Region          42..421
                     /region_name="IVD"
                     /note="Isovaleryl-CoA dehydrogenase; cd01156"
                     /db_xref="CDD:173845"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JHI5; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
     Site            65
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JHI5; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
     Site            76
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P26440; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
     Site            order(125,129,133,172,198,221,275,282,285,288,400..401,
                     404..406)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:173845"
     Site            order(163,165..166,171..172,196,198,407,409)
                     /site_type="other"
                     /note="FAD binding site [chemical binding]"
                     /db_xref="CDD:173845"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHI5; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JHI5; propagated from
                     UniProtKB/Swiss-Prot (P12007.2)"
     Site            284
                     /site_type="active"
                     /note="catalytic base [active]"
                     /db_xref="CDD:173845"
     CDS             1..424
                     /gene="Ivd"
                     /coded_by="NM_012592.2:6..1280"
                     /db_xref="GeneID:24513"
                     /db_xref="RGD:2936"
ORIGIN      
        1 matavrllgr rvsswrlrpl psplavpqra hsmlpvdddi nglneeqkql rhtiskfvqe
       61 nlapkaqeid qsndfknlre fwkqlgslgv lgitapvqyg gsglgylehv lvmeeisras
      121 aavglsygah snlcinqivr ngneaqkeky lpklisgefi galamsepna gsdvvsmrlk
      181 aekkgdhyvl ngnkfwitng pdadvlvvya ktdltavpas rgitafivek dmpgfstskk
      241 ldklgmrgsn tcelvfedck vpaanilsqe skgvyvlmsg ldlerlvlag gplgimqavl
      301 dhtipylhvr eafgqkigqf qlmqgkmadm ytrlmacrqy vynvaracde ghitakdcag
      361 vilytaecat qvaldgiqcl ggngyindfp mgrflrdakl yeigggtsev rrlvigrafn
      421 adfr
//
LOCUS       NP_446305                290 aa            linear   ROD 27-APR-2025
DEFINITION  arylamine N-acetyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_446305
VERSION     NP_446305.1
DBSOURCE    REFSEQ: accession NM_053853.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,Y.J., Meng,F.T., Wang,L.L., Zhang,L.F., Cheng,X.P. and
            Zhou,J.N.
  TITLE     Apolipoprotein E influences melatonin biosynthesis by regulating
            NAT and MAOA expression in C6 cells
  JOURNAL   J Pineal Res 52 (4), 397-402 (2012)
   PUBMED   22225631
  REMARK    GeneRIF: A higher level of melatonin was demonstrated in cultured
            ApoE4-C6 cells than in ApoE3-C6 cells. NAT was up-regulated in
            ApoE4-C6 cells compared with ApoE3-C6 cells, and MAOA and MAOB
            expression decreased in ApoE4-C6 cells.
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Potts,L.F., Cambon,A.C., Ross,O.A., Rademakers,R., Dickson,D.W.,
            Uitti,R.J., Wszolek,Z.K., Rai,S.N., Farrer,M.J., Hein,D.W. and
            Litvan,I.
  TITLE     Polymorphic genes of detoxification and mitochondrial enzymes and
            risk for progressive supranuclear palsy: a case control study
  JOURNAL   BMC Med Genet 13, 16 (2012)
   PUBMED   22424094
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Blomeke,B., Brans,R., Coenraads,P.J., Dickel,H., Bruckner,T.,
            Hein,D.W., Heesen,M., Merk,H.F. and Kawakubo,Y.
  TITLE     Para-phenylenediamine and allergic sensitization: risk modification
            by N-acetyltransferase 1 and 2 genotypes
  JOURNAL   Br J Dermatol 161 (5), 1130-1135 (2009)
   PUBMED   19663877
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Dai,Y., Leng,S., Li,L., Niu,Y., Huang,H., Liu,Q., Duan,H.,
            Cheng,J., Liu,Q. and Zheng,Y.
  TITLE     Effects of genetic polymorphisms of N-Acetyltransferase on
            trichloroethylene-induced hypersensitivity dermatitis among exposed
            workers
  JOURNAL   Ind Health 47 (5), 479-486 (2009)
   PUBMED   19834256
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Barker,D.F., Walraven,J.M., Ristagno,E.H., Doll,M.A., States,J.C.
            and Hein,D.W.
  TITLE     Quantitative tissue and gene-specific differences and developmental
            changes in Nat1, Nat2, and Nat3 mRNA expression in the rat
  JOURNAL   Drug Metab Dispos 36 (12), 2445-2451 (2008)
   PUBMED   18799802
  REMARK    GeneRIF: Results demonstrate differential tissue-specific and
            developmental regulation of the rat Nat1 and Nat2 genes.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Jones,R.F., Land,S.J. and King,C.M.
  TITLE     Recombinant rat and hamster N-acetyltransferases-1 and -2: relative
            rates of N-acetylation of arylamines and N,O-acyltransfer with
            arylhydroxamic acids
  JOURNAL   Carcinogenesis 17 (8), 1729-1733 (1996)
   PUBMED   8761433
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Ebisawa,T., Sasaki,Y. and Deguchi,T.
  TITLE     Complementary DNAs for two arylamine N-acetyltransferases with
            identical 5' non-coding regions from rat pineal gland
  JOURNAL   Eur J Biochem 228 (1), 129-137 (1995)
   PUBMED   7882993
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Vatsis,K.P., Weber,W.W., Bell,D.A., Dupret,J.M., Evans,D.A.,
            Grant,D.M., Hein,D.W., Lin,H.J., Meyer,U.A., Relling,M.V. et al.
  TITLE     Nomenclature for N-acetyltransferases
  JOURNAL   Pharmacogenetics 5 (1), 1-17 (1995)
   PUBMED   7773298
  REMARK    Review article
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Kelly,S.L. and Sim,E.
  TITLE     Arylamine N-acetyltransferase in Balb/c mice: identification of a
            novel mouse isoenzyme by cloning and expression in vitro
  JOURNAL   Biochem J 302 (Pt 2) (Pt 2), 347-353 (1994)
   PUBMED   7545952
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Omura,G.A.
  TITLE     Combination therapy with 5-azacytidine plus
            beta-2'-deoxythioguanosine in adult acute leukemia
  JOURNAL   Cancer Treat Rep 61 (5), 915-917 (1977)
   PUBMED   70273
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB580886.1 and BC078765.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..290
                     /product="arylamine N-acetyltransferase 1"
                     /EC_number="2.3.1.5"
                     /note="AT-1; NAT-1; arylamide acetylase 1;
                     N-acetyltransferase type 1; N-acetyltransferase 1
                     (arylamine N-acetyltransferase); N-acetyltransferase
                     (arylamine N-acetyltransferase)"
                     /calculated_mol_wt=33306
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P18440; propagated from
                     UniProtKB/Swiss-Prot (P50297.1)"
     Region          20..280
                     /region_name="Acetyltransf_2"
                     /note="N-acetyltransferase; pfam00797"
                     /db_xref="CDD:395644"
     CDS             1..290
                     /gene="Nat1"
                     /gene_synonym="Nat"
                     /coded_by="NM_053853.2:478..1350"
                     /db_xref="GeneID:116631"
                     /db_xref="RGD:70490"
ORIGIN      
        1 mdieayferi gyknsvnkld latltevlqh qmravpfenl smhcgeamcl gleatfdhiv
       61 rkkrggwclq vnhllywalt kmgfettmlg gyvyitpvnk yssemvhllv qvtisdrnyi
      121 vdsaygssyq mwepleltsg kdqpqvpaif rlteengtwy ldqirreqdv pnqefvnsdl
      181 lekskyrkiy sftleprtie dfeyvntylq tspasvfvst sfcslqtseg vccligstlt
      241 srrfsykdnv dlvefkslte eeiedvlktt fgislekkfv pkhgelvfti
//
LOCUS       NP_113741                207 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear transcription factor Y subunit beta [Rattus norvegicus].
ACCESSION   NP_113741
VERSION     NP_113741.1
DBSOURCE    REFSEQ: accession NM_031553.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Muller,P.A. and Vousden,K.H.
  TITLE     p53 mutations in cancer
  JOURNAL   Nat Cell Biol 15 (1), 2-8 (2013)
   PUBMED   23263379
  REMARK    Review article
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Freed-Pastor,W.A. and Prives,C.
  TITLE     Mutant p53: one name, many proteins
  JOURNAL   Genes Dev 26 (12), 1268-1286 (2012)
   PUBMED   22713868
  REMARK    Review article
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Chang,M., Jin,W. and Sun,S.C.
  TITLE     Peli1 facilitates TRIF-dependent Toll-like receptor signaling and
            proinflammatory cytokine production
  JOURNAL   Nat Immunol 10 (10), 1089-1095 (2009)
   PUBMED   19734906
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Stros,M., Polanska,E., Struncova,S. and Pospisilova,S.
  TITLE     HMGB1 and HMGB2 proteins up-regulate cellular expression of human
            topoisomerase IIalpha
  JOURNAL   Nucleic Acids Res 37 (7), 2070-2086 (2009)
   PUBMED   19223331
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Niimi,T., Hayashi,Y., Futaki,S. and Sekiguchi,K.
  TITLE     SOX7 and SOX17 regulate the parietal endoderm-specific enhancer
            activity of mouse laminin alpha1 gene
  JOURNAL   J Biol Chem 279 (36), 38055-38061 (2004)
   PUBMED   15220343
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Haze,K., Okada,T., Yoshida,H., Yanagi,H., Yura,T., Negishi,M. and
            Mori,K.
  TITLE     Identification of the G13 (cAMP-response-element-binding
            protein-related protein) gene product related to activating
            transcription factor 6 as a transcriptional activator of the
            mammalian unfolded protein response
  JOURNAL   Biochem J 355 (Pt 1), 19-28 (2001)
   PUBMED   11256944
REFERENCE   8  (residues 1 to 207)
  AUTHORS   Sinha,S., Maity,S.N., Lu,J. and de Crombrugghe,B.
  TITLE     Recombinant rat CBF-C, the third subunit of CBF/NFY, allows
            formation of a protein-DNA complex with CBF-A and CBF-B and with
            yeast HAP2 and HAP3
  JOURNAL   Proc Natl Acad Sci U S A 92 (5), 1624-1628 (1995)
   PUBMED   7878029
REFERENCE   9  (residues 1 to 207)
  AUTHORS   Vuorio,T., Maity,S.N. and de Crombrugghe,B.
  TITLE     Purification and molecular cloning of the 'A' chain of a rat
            heteromeric CCAAT-binding protein. Sequence identity with the yeast
            HAP3 transcription factor
  JOURNAL   J Biol Chem 265 (36), 22480-22486 (1990)
   PUBMED   2266139
REFERENCE   10 (residues 1 to 207)
  AUTHORS   Hooft van Huijsduijnen,R., Li,X.Y., Black,D., Matthes,H.,
            Benoist,C. and Mathis,D.
  TITLE     Co-evolution from yeast to mouse: cDNA cloning of the two NF-Y
            (CP-1/CBF) subunits
  JOURNAL   EMBO J 9 (10), 3119-3127 (1990)
   PUBMED   1698608
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089791.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089791.1, CO561802.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..207
                     /product="nuclear transcription factor Y subunit beta"
                     /note="CBF-A; NF-YB; nuclear transcription factor Y
                     subunit B; CCAAT-binding transcription factor subunit A;
                     CAAT box DNA-binding protein subunit B; nuclear
                     transcription factor - Y beta; CCAAT binding transcription
                     factor of CBF-B/NFY-B; CCAAT-binding transcription factor
                     subunit B; nuclear transcription factor-Y beta"
                     /calculated_mol_wt=22656
     Region          1..52
                     /region_name="A domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P63140.1)"
     Region          27..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63140.1)"
     Region          52..142
                     /region_name="HFD_NFYB"
                     /note="histone-fold domain found in nuclear transcription
                     factor Y subunit beta (NF-YB) and similar proteins;
                     cd22907"
                     /db_xref="CDD:467032"
     Site            order(52,54..55,58,84,87..88,92,95..96,99..100,103,
                     123..125,127)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:467032"
     Region          53..142
                     /region_name="B domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P63140.1)"
     Site            order(55..60,63,67..68,71..73,76..79,82,85..86,89..94,
                     96..99,102,111..115,118,122,126..127,130,134,137,141..142)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467032"
     Site            order(55,60..63,66,69,77..80,83,111..112)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467032"
     Region          86..97
                     /region_name="Subunit association domain (SAD).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P63140.1)"
     Region          143..207
                     /region_name="C domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P63140.1)"
     CDS             1..207
                     /gene="Nfyb"
                     /gene_synonym="CBF-B; CBFB; Nfya"
                     /coded_by="NM_031553.2:214..837"
                     /db_xref="GeneID:25336"
                     /db_xref="RGD:3172"
ORIGIN      
        1 mtmdgdsstt dasqlgisad yiggshyviq phddtedsmn dhedtngske sfreqdiylp
       61 ianvarimkn aipqtgkiak dakecvqecv sefisfitse aserchqekr ktingedilf
      121 amstlgfdsy veplklylqk freamkgekg iggavsatdg lseelteeaf tnqlpaglit
      181 adgqqqnvmv yttsyqqisg vqqiqfs
//
LOCUS       NP_598271               2013 aa            linear   ROD 27-APR-2025
DEFINITION  cell adhesion molecule DSCAM precursor [Rattus norvegicus].
ACCESSION   NP_598271 XP_346414
VERSION     NP_598271.1
DBSOURCE    REFSEQ: accession NM_133587.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2013)
  AUTHORS   Purohit,A.A., Li,W., Qu,C., Dwyer,T., Shao,Q., Guan,K.L. and Liu,G.
  TITLE     Down syndrome cell adhesion molecule (DSCAM) associates with
            uncoordinated-5C (UNC5C) in netrin-1-mediated growth cone collapse
  JOURNAL   J Biol Chem 287 (32), 27126-27138 (2012)
   PUBMED   22685302
REFERENCE   2  (residues 1 to 2013)
  AUTHORS   Shen,L., Xiao,Z., Pan,Y., Fang,M., Li,C., Chen,D., Wang,L., Xi,Z.,
            Xiao,F. and Wang,X.
  TITLE     Altered expression of Dscam in temporal lobe tissue from human and
            experimental animals
  JOURNAL   Synapse 65 (10), 975-982 (2011)
   PUBMED   21360594
  REMARK    GeneRIF: Dscam is highly expressed in rat brain during the
            different phases of experimental epilepsy.
REFERENCE   3  (residues 1 to 2013)
  AUTHORS   Fuerst,P.G., Bruce,F., Tian,M., Wei,W., Elstrott,J., Feller,M.B.,
            Erskine,L., Singer,J.H. and Burgess,R.W.
  TITLE     DSCAM and DSCAML1 function in self-avoidance in multiple cell types
            in the developing mouse retina
  JOURNAL   Neuron 64 (4), 484-497 (2009)
   PUBMED   19945391
REFERENCE   4  (residues 1 to 2013)
  AUTHORS   Wang,M.C., Jia,Y.J., Wen,Q.Q., Guan,W.J., Zhao,E.Y., Wang,L.D. and
            Zhang,B.A.
  TITLE     [Effects of DSCAM on differentiation of rat marrow mesenchymal stem
            cells into neurons in vitro]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 11 (6), 486-489 (2009)
   PUBMED   19558816
  REMARK    GeneRIF: DSCAM may play an important role in mesenchymal stem cells
            (MSCs) differentiation into neural cells.
REFERENCE   5  (residues 1 to 2013)
  AUTHORS   Liu,G., Li,W., Wang,L., Kar,A., Guan,K.L., Rao,Y. and Wu,J.Y.
  TITLE     DSCAM functions as a netrin receptor in commissural axon
            pathfinding
  JOURNAL   Proc Natl Acad Sci U S A 106 (8), 2951-2956 (2009)
   PUBMED   19196994
REFERENCE   6  (residues 1 to 2013)
  AUTHORS   Ly,A., Nikolaev,A., Suresh,G., Zheng,Y., Tessier-Lavigne,M. and
            Stein,E.
  TITLE     DSCAM is a netrin receptor that collaborates with DCC in mediating
            turning responses to netrin-1
  JOURNAL   Cell 133 (7), 1241-1254 (2008)
   PUBMED   18585357
REFERENCE   7  (residues 1 to 2013)
  AUTHORS   Fuerst,P.G., Koizumi,A., Masland,R.H. and Burgess,R.W.
  TITLE     Neurite arborization and mosaic spacing in the mouse retina require
            DSCAM
  JOURNAL   Nature 451 (7177), 470-474 (2008)
   PUBMED   18216855
REFERENCE   8  (residues 1 to 2013)
  AUTHORS   Barlow,G.M., Chen,X.N., Shi,Z.Y., Lyons,G.E., Kurnit,D.M.,
            Celle,L., Spinner,N.B., Zackai,E., Pettenati,M.J., Van Riper,A.J.,
            Vekemans,M.J., Mjaatvedt,C.H. and Korenberg,J.R.
  TITLE     Down syndrome congenital heart disease: a narrowed region and a
            candidate gene
  JOURNAL   Genet Med 3 (2), 91-101 (2001)
   PUBMED   11280955
REFERENCE   9  (residues 1 to 2013)
  AUTHORS   Barlow,G.M., Micales,B., Lyons,G.E. and Korenberg,J.R.
  TITLE     Down syndrome cell adhesion molecule is conserved in mouse and
            highly expressed in the adult mouse brain
  JOURNAL   Cytogenet Cell Genet 94 (3-4), 155-162 (2001)
   PUBMED   11856873
REFERENCE   10 (residues 1 to 2013)
  AUTHORS   Yamakawa,K., Huot,Y.K., Haendelt,M.A., Hubert,R., Chen,X.N.,
            Lyons,G.E. and Korenberg,J.R.
  TITLE     DSCAM: a novel member of the immunoglobulin superfamily maps in a
            Down syndrome region and is involved in the development of the
            nervous system
  JOURNAL   Hum Mol Genet 7 (2), 227-237 (1998)
   PUBMED   9426258
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF334385.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346414.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF334385.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2013
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..2013
                     /product="cell adhesion molecule DSCAM precursor"
                     /note="Down syndrome cell adhesion molecule homolog; cell
                     adhesion molecule DSCAM"
                     /calculated_mol_wt=220299
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1974
     mat_peptide     18..2013
                     /product="Cell adhesion molecule DSCAM.
                     /id=PRO_0000392479"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ8.1)"
                     /calculated_mol_wt=220299
     Region          26..121
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          42..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          79..83
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          99..104
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          112..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          125..210
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          235..310
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          242..246
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          255..259
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          290..295
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..395
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          331..335
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          344..348
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          368..372
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          382..387
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          406..501
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          424..428
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          437..441
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          467..471
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          481..486
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          494..497
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          504..593
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          521..525
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          534..538
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          557..561
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          572..577
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          586..589
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          596..686
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          613..617
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          627..631
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          652..656
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          666..671
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          679..682
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          689..784
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig)-like domain of Down Syndrome
                     Cell Adhesion molecule (DSCAM); cd05734"
                     /db_xref="CDD:409397"
     Region          689..693
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409397"
     Region          698..702
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409397"
     Region          704..714
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409397"
     Region          720..726
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409397"
     Region          733..736
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409397"
     Region          744..747
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409397"
     Region          749..755
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409397"
     Region          762..770
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409397"
     Region          775..784
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409397"
     Region          785..884
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig) domain of Down Syndrome Cell
                     Adhesion molecule (DSCAM); cd05735"
                     /db_xref="CDD:409398"
     Region          785..788
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409398"
     Region          796..800
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409398"
     Region          803..810
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409398"
     Region          818..824
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409398"
     Region          833..836
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409398"
     Region          842..846
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409398"
     Region          848..854
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409398"
     Region          861..869
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409398"
     Region          872..882
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409398"
     Region          885..978
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(885,952,967)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <937..1300
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(968..969,971..972)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Site            1250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          1287..1363
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          1380..1470
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1380,1443,1458)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1459..1460,1462..1463)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1486..1555
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1595..1615
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          1616..2013
                     /region_name="Required for netrin-mediated axon repulsion
                     of neuronal growth cones.
                     /evidence=ECO:0000250|UniProtKB:Q9ERC8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          1718..1809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     Region          1920..2013
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ8.1)"
     CDS             1..2013
                     /gene="Dscam"
                     /coded_by="NM_133587.1:477..6518"
                     /db_xref="GeneID:171119"
                     /db_xref="RGD:619992"
ORIGIN      
        1 mwilalslfq sfanvfseep hsslyfvnas lqevvfasts gtlvpcpaag ippvtlrwyl
       61 atgeeiydvp girhvhpngt lqifpfppss fstlihdnty yctaenpsgk irsqdvhika
      121 vlrepytvrv edqktmrgnv avfkciipss veayvtvvsw ekdtvslvsg srflitstga
      181 lyikdvqned glynyrcitr hrytgetrqs nsarlfvsdp ansapsildg fdhrkamagq
      241 rvelpckalg hpepdyrwlk dnmplelsgr fqktvtglli ensrpsdsgs yvcevsnryg
      301 takvigrlyv kqplkatisp rkvkssvgsq vslscsvtgn edqelswyrn geilnpgknv
      361 ritglnhanl imdhmvksdg gayqcfvrkd klsaqdyvqv vledgtpkii safsekvvsp
      421 aepvslvcnv kgtplptvtw tldddpilkg sghrisqmit segnvvsyln isssqvrdgg
      481 vyrctannsa gvvlyqarin vrgpasirpm knitaiagrd tyihcrvigy pyysikwykn
      541 anllpfnhrq vafenngtlk lsdvqkevde geytcnvlvq pqlstsqsvh vtvkvppfiq
      601 pfefprfsig qrvfipcvvv sgdlpititw qkdgrpipas lgvtidnidf tsslrisnls
      661 lmhngnytci arneaaaveh qsqlivrvpp kfvvqprdqd giygkaviln csaegypvpt
      721 ivwkfskgag vpqfqpialn griqvlsngs llikhvveed sgyylckvsn dvgadvsksm
      781 yltvkipami tsypnttlat qgqrkemsct ahgekpiivr wekedriinp emarylvstk
      841 evgeevistl qilptvreds gffschains ygedrgiiql tvqeppdppe ieikdvkart
      901 itlrwtmgfd gnspitgydi ecknksdswd saqrtkdvsp qlnsatiidi hpsstysirm
      961 yaknrigkse psneititad eaapdgppqe vhleptssqs irvtwkapkk hlqngiirgy
     1021 qigyreystg gnfqfniisi dttgdsevyt ldnlnkftqy glvvqacnra gtgpssqeii
     1081 tttledvpsy ppenvqaiat spesisisws tlskealngi lqgfrviywa nlidgelgei
     1141 knvtttqpsl eldglekytn ysiqvlaftr agdgvrseqi ftrtkedvpg ppagvkaaaa
     1201 sasmvfvswl pplklngiir kytvfcshpy ptvisefeas pdsfsyripn lsrnrqysvw
     1261 vvavtsagrg nsseiitvep lakaparilt fsgtvttpwm kdivlpckav gdpspavkwm
     1321 kdsngtpslv tidgrrsifs ngsfvirtvk aedsgyyscv annnwgsdei ilnlqvqvpp
     1381 dqprltvskt tsssitlswl pgdnggssir gyilqysedn seqwgsfpis psersyrlen
     1441 lkcgtwykft ltaqngvgpg riseiieakt lgkepqfske qelfasintt rvrlnligwn
     1501 dggcpitsft leyrpfgttv wttaqrtsls ksyilydlqe atwyelqmrv cnsagcaekq
     1561 anfatlnydg stippliksv vqseeglttn eglkilvtis cilvgvlllf vlllvvrrrr
     1621 reqrlkrlrd akslaemlms kntrtsdtls kqqqtlrmhi dipraqllie erdtmetidd
     1681 rstvlltdad fgeaakqksl tvthtvhyqs vsqatgplvd vsdarpgtnp ttrrnakagp
     1741 tarnryasqw tlnrphptis ahtlttdwrl ptpratgsvd kesdsysvsp sqdtdrarss
     1801 mvstesasst yeelarayeh akmeeqlrha kftitecfis dtsseqltag tneytdslts
     1861 stpsesgicr ftasppkpqd ggrvvnmavp kahrpgdlih lppylrmdfl lnrgapgtsr
     1921 dlslgqacle pqksrtlkrp tvleptpmea ssstsstreg qqswqqgava tlpqregael
     1981 gqaakmsssq eslldsrghl kgnnpyaksy tlv
//
LOCUS       NP_001009268             394 aa            linear   ROD 27-APR-2025
DEFINITION  actin-related protein 2 [Rattus norvegicus].
ACCESSION   NP_001009268 XP_214109
VERSION     NP_001009268.1
DBSOURCE    REFSEQ: accession NM_001009268.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Zhao,H., Wang,L., Yan,Y., Zhao,Q.H., He,J., Jiang,R., Luo,C.J.,
            Qiu,H.L., Miao,Y.Q., Gong,S.G., Yuan,P. and Wu,W.H.
  TITLE     Identification of the shared gene signatures between pulmonary
            fibrosis and pulmonary hypertension using bioinformatics analysis
  JOURNAL   Front Immunol 14, 1197752 (2023)
   PUBMED   37731513
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Schrank,B.R., Aparicio,T., Li,Y., Chang,W., Chait,B.T.,
            Gundersen,G.G., Gottesman,M.E. and Gautier,J.
  TITLE     Nuclear ARP2/3 drives DNA break clustering for homology-directed
            repair
  JOURNAL   Nature 559 (7712), 61-66 (2018)
   PUBMED   29925947
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Rao,J., Ashraf,S., Tan,W., van der Ven,A.T., Gee,H.Y., Braun,D.A.,
            Feher,K., George,S.P., Esmaeilniakooshkghazi,A., Choi,W.I.,
            Jobst-Schwan,T., Schneider,R., Schmidt,J.M., Widmeier,E.,
            Warejko,J.K., Hermle,T., Schapiro,D., Lovric,S., Shril,S., Daga,A.,
            Nayir,A., Shenoy,M., Tse,Y., Bald,M., Helmchen,U., Mir,S.,
            Berdeli,A., Kari,J.A., El Desoky,S., Soliman,N.A., Bagga,A.,
            Mane,S., Jairajpuri,M.A., Lifton,R.P., Khurana,S., Martins,J.C. and
            Hildebrandt,F.
  TITLE     Advillin acts upstream of phospholipase C 1 in steroid-resistant
            nephrotic syndrome
  JOURNAL   J Clin Invest 127 (12), 4257-4269 (2017)
   PUBMED   29058690
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Singer,B.F., Bubula,N., Przybycien-Szymanska,M.M., Li,D. and
            Vezina,P.
  TITLE     Stimuli associated with the presence or absence of amphetamine
            regulate cytoskeletal signaling and behavior
  JOURNAL   Eur Neuropsychopharmacol 26 (11), 1836-1842 (2016)
   PUBMED   27720500
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Jilek,J.L., Sant,K.E., Cho,K.H., Reed,M.S., Pohl,J., Hansen,J.M.
            and Harris,C.
  TITLE     Ethanol Attenuates Histiotrophic Nutrition Pathways and Alters the
            Intracellular Redox Environment and Thiol Proteome during Rat
            Organogenesis
  JOURNAL   Toxicol Sci 147 (2), 475-489 (2015)
   PUBMED   26185205
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Cai,L., Holoweckyj,N., Schaller,M.D. and Bear,J.E.
  TITLE     Phosphorylation of coronin 1B by protein kinase C regulates
            interaction with Arp2/3 and cell motility
  JOURNAL   J Biol Chem 280 (36), 31913-31923 (2005)
   PUBMED   16027158
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Peng,J., Kim,M.J., Cheng,D., Duong,D.M., Gygi,S.P. and Sheng,M.
  TITLE     Semiquantitative proteomic analysis of rat forebrain postsynaptic
            density fractions by mass spectrometry
  JOURNAL   J Biol Chem 279 (20), 21003-21011 (2004)
   PUBMED   15020595
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Otsubo,T., Iwaya,K., Mukai,Y., Mizokami,Y., Serizawa,H.,
            Matsuoka,T. and Mukai,K.
  TITLE     Involvement of Arp2/3 complex in the process of colorectal
            carcinogenesis
  JOURNAL   Mod Pathol 17 (4), 461-467 (2004)
   PUBMED   14990971
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Rombouts,K., Knittel,T., Machesky,L., Braet,F., Wielant,A.,
            Hellemans,K., De Bleser,P., Gelman,I., Ramadori,G. and Geerts,A.
  TITLE     Actin filament formation, reorganization and migration are impaired
            in hepatic stellate cells under influence of trichostatin A, a
            histone deacetylase inhibitor
  JOURNAL   J Hepatol 37 (6), 788-796 (2002)
   PUBMED   12445420
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Gournier,H., Goley,E.D., Niederstrasser,H., Trinh,T. and Welch,M.D.
  TITLE     Reconstitution of human Arp2/3 complex reveals critical roles of
            individual subunits in complex structure and activity
  JOURNAL   Mol Cell 8 (5), 1041-1052 (2001)
   PUBMED   11741539
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088442.1.
            
            On Jan 7, 2005 this sequence version replaced XP_214109.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088442.1, FQ233785.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..394
                     /product="actin-related protein 2"
                     /note="actin-like protein 2; ARP2 actin related protein 2
                     homolog"
                     /calculated_mol_wt=44603
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (Q5M7U6.1)"
     Region          7..388
                     /region_name="ASKHA_NBD_Arp2"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein2 (Arp2) and similar proteins; cd10220"
                     /db_xref="CDD:466821"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (Q5M7U6.1)"
     Site            322
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61160; propagated from
                     UniProtKB/Swiss-Prot (Q5M7U6.1)"
     CDS             1..394
                     /gene="Actr2"
                     /coded_by="NM_001009268.1:65..1249"
                     /db_xref="GeneID:289820"
                     /db_xref="RGD:1310826"
ORIGIN      
        1 mdsqgrkvvv cdngtgfvkc gyagsnfpeh ifpalvgrpi irsttkvgni eikdlmvgde
       61 aselrsmlev nypmengivr nwddmkhlwd ytfgpeklni dtrsckillt eppmnptknr
      121 ekivevmfet yqfsgvyvai qavltlyaqg lltgvvvdsg dgvthicpvy egfslphltr
      181 rldiagrdit rylikllllr gyafnhsadf etvrmikekl cyvgynieqe qklalettvl
      241 vesytlpdgr iikvggerfe apealfqphl invegvgvae llfntiqaad idtrsefykh
      301 ivlsggstmy pglpsrlere lkqlylervl kgdveklskf kiriedpprr khmvflggav
      361 ladimkdkdn fwmtrqeyqe kgvrvleklg vtvr
//
LOCUS       NP_001008292             837 aa            linear   ROD 27-APR-2025
DEFINITION  tuftelin-interacting protein 11 [Rattus norvegicus].
ACCESSION   NP_001008292 XP_213801
VERSION     NP_001008292.1
DBSOURCE    REFSEQ: accession NM_001008291.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Tannukit,S., Crabb,T.L., Hertel,K.J., Wen,X., Jans,D.A. and
            Paine,M.L.
  TITLE     Identification of a novel nuclear localization signal and
            speckle-targeting sequence of tuftelin-interacting protein 11, a
            splicing factor involved in spliceosome disassembly
  JOURNAL   Biochem Biophys Res Commun 390 (3), 1044-1050 (2009)
   PUBMED   19857462
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Yoshimoto,R., Kataoka,N., Okawa,K. and Ohno,M.
  TITLE     Isolation and characterization of post-splicing lariat-intron
            complexes
  JOURNAL   Nucleic Acids Res 37 (3), 891-902 (2009)
   PUBMED   19103666
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Ji,Q., Huang,C.H., Peng,J., Hashmi,S., Ye,T. and Chen,Y.
  TITLE     Characterization of STIP, a multi-domain nuclear protein, highly
            conserved in metazoans, and essential for embryogenesis in
            Caenorhabditis elegans
  JOURNAL   Exp Cell Res 313 (7), 1460-1472 (2007)
   PUBMED   17289020
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Herrmann,G., Kais,S., Hoffbauer,J., Shah-Hosseini,K.,
            Bruggenolte,N., Schober,H., Fasi,M. and Schar,P.
  TITLE     Conserved interactions of the splicing factor Ntr1/Spp382 with
            proteins involved in DNA double-strand break repair and telomere
            metabolism
  JOURNAL   Nucleic Acids Res 35 (7), 2321-2332 (2007)
   PUBMED   17389648
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Paine,C.T., Paine,M.L., Luo,W., Okamoto,C.T., Lyngstadaas,S.P. and
            Snead,M.L.
  TITLE     A tuftelin-interacting protein (TIP39) localizes to the apical
            secretory pole of mouse ameloblasts
  JOURNAL   J Biol Chem 275 (29), 22284-22292 (2000)
   PUBMED   10806191
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085809.1.
            
            On Dec 16, 2004 this sequence version replaced XP_213801.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085809.1, DQ342031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..837
                     /product="tuftelin-interacting protein 11"
                     /note="STIP-1; septin and tuftelin-interacting protein 1"
                     /calculated_mol_wt=96021
     Region          1..50
                     /region_name="Required for interaction with DHX15.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          18..104
                     /region_name="TIP_N"
                     /note="Tuftelin interacting protein N terminal; pfam12457"
                     /db_xref="CDD:463593"
     Region          34..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB9; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          85..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBB9; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          149..193
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          183..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          397..666
                     /region_name="GCFC"
                     /note="GC-rich sequence DNA-binding factor-like protein;
                     pfam07842"
                     /db_xref="CDD:400273"
     Region          700..705
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     Region          710..734
                     /region_name="Required for nuclear speckle localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y6.1)"
     CDS             1..837
                     /gene="Tfip11"
                     /coded_by="NM_001008291.1:271..2784"
                     /db_xref="GeneID:288718"
                     /db_xref="RGD:1311449"
ORIGIN      
        1 mslshlyrdg eghlddddde renfeitdwd lqnefnpnrq rhwqtkeeat ygvwaerdsd
       61 eerpsfggkr ardysapvnf isaglkkgaa eeadsedsda eekpvkqedf pkdlgpkklk
      121 tggnfkpsqk gfaggtksfm dfgswerhtk gigqkllqkm gyvpgrglgk naqgiinpie
      181 akqrkgkgav gaygserttq slqdfpvads eeeaeeefqk elsqwrkdps gskkkpkysy
      241 ktveelkakg rvskkltapq kelsqvkvid mtgreqkvyy sysqishkhs vpdegvplla
      301 qlpptagkea kvpgfalpel ehnlqllier teqeiiqsdr qlqyerdmvv slshelekta
      361 evlaheervi snlskvlalv eecehrmqph gadpltldec arifetlqdk yyeeyrladr
      421 adlavaivyp lvkdyfkdwh pledsnygtq iiskwkslle ndqllshssq dlssdafhrl
      481 mwevwmpfvr nvvaqwqprn cepmvdflds wahiipvwil dnildqlifp klqkevdnwn
      541 pltdtvpihs wihpwlplmq arleplyspv rsklssalqk whpsdasakl ilqpwkevlt
      601 pgsweafmlr nivpklgmcl gelvinphqq hmdafywvmd wegmisvssl vgllekhffp
      661 kwlqvlcswl snspnyeeit kwylgwksmf sdqvlahpsv kdkfnealdi mnravssnvg
      721 aymqpgaren iaylthterr kdfqyeamqe rreaenmaqr gigvaassvp mnfkdlietk
      781 aeehnivfmp vigkrhegkq lytfgriviy idrgvvfvqg ektwvptslq slidmak
//
LOCUS       NP_620187                485 aa            linear   ROD 27-APR-2025
DEFINITION  sodium-coupled neutral amino acid symporter 1 [Rattus norvegicus].
ACCESSION   NP_620187
VERSION     NP_620187.1
DBSOURCE    REFSEQ: accession NM_138832.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Nusken,E., Gellhaus,A., Kuhnel,E., Swoboda,I., Wohlfarth,M.,
            Vohlen,C., Schneider,H., Dotsch,J. and Nusken,K.D.
  TITLE     Increased Rat Placental Fatty Acid, but Decreased Amino Acid and
            Glucose Transporters Potentially Modify Intrauterine Programming
  JOURNAL   J Cell Biochem 117 (7), 1594-1603 (2016)
   PUBMED   26590355
  REMARK    GeneRIF: Increased Rat Placental Fatty Acid, but Decreased Amino
            Acid and Glucose Transporters Potentially Modify Intrauterine
            Programming
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Takarada,T., Ogura,M., Nakamichi,N., Kakuda,T., Nakazato,R.,
            Kokubo,H., Ikeno,S., Nakamura,S., Kutsukake,T., Hinoi,E. and
            Yoneda,Y.
  TITLE     Upregulation of Slc38a1 Gene Along with Promotion of Neurosphere
            Growth and Subsequent Neuronal Specification in Undifferentiated
            Neural Progenitor Cells Exposed to Theanine
  JOURNAL   Neurochem Res 41 (1-2), 5-15 (2016)
   PUBMED   25957749
  REMARK    GeneRIF: Overexpression of X-box binding protein-1 led to a marked
            increase in luciferase activity in P19 cells transfected with the
            Slc38a1 reporter plasmid. These results suggest that theanine
            accelerates cellular proliferation and subsequent neuronal
            specification through a mechanism relevant to upregulation of
            Slc38a1 gene in undifferentiated neural progenitor cells
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Park,Y.Y., Sohn,B.H., Johnson,R.L., Kang,M.H., Kim,S.B., Shim,J.J.,
            Mangala,L.S., Kim,J.H., Yoo,J.E., Rodriguez-Aguayo,C., Pradeep,S.,
            Hwang,J.E., Jang,H.J., Lee,H.S., Rupaimoole,R., Lopez-Berestein,G.,
            Jeong,W., Park,I.S., Park,Y.N., Sood,A.K., Mills,G.B. and Lee,J.S.
  TITLE     Yes-associated protein 1 and transcriptional coactivator with
            PDZ-binding motif activate the mammalian target of rapamycin
            complex 1 pathway by regulating amino acid transporters in
            hepatocellular carcinoma
  JOURNAL   Hepatology 63 (1), 159-172 (2016)
   PUBMED   26389641
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Doi,T., Ueda,Y., Takaki,M. and Willmore,L.J.
  TITLE     Differential molecular regulation of glutamate in kindling
            resistant rats
  JOURNAL   Brain Res 1375, 1-6 (2011)
   PUBMED   21138736
REFERENCE   5  (residues 1 to 485)
  AUTHORS   King,N., Lin,H. and Suleiman,M.S.
  TITLE     Oxidative stress increases SNAT1 expression and stimulates cysteine
            uptake in freshly isolated rat cardiomyocytes
  JOURNAL   Amino Acids 40 (2), 517-526 (2011)
   PUBMED   20602128
  REMARK    GeneRIF: Oxidative stress increases SNAT1 expression and stimulates
            cysteine uptake in rat cardiomyocytes.
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Mackenzie,B., Schafer,M.K., Erickson,J.D., Hediger,M.A., Weihe,E.
            and Varoqui,H.
  TITLE     Functional properties and cellular distribution of the system A
            glutamine transporter SNAT1 support specialized roles in central
            neurons
  JOURNAL   J Biol Chem 278 (26), 23720-23730 (2003)
   PUBMED   12684517
  REMARK    GeneRIF: distribution of SNAT1 in central nervous system neurons
            and characterization of its transport properties
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Chaudhry,F.A., Schmitz,D., Reimer,R.J., Larsson,P., Gray,A.T.,
            Nicoll,R., Kavanaugh,M. and Edwards,R.H.
  TITLE     Glutamine uptake by neurons: interaction of protons with system a
            transporters
  JOURNAL   J Neurosci 22 (1), 62-72 (2002)
   PUBMED   11756489
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Albers,A., Broer,A., Wagner,C.A., Setiawan,I., Lang,P.A.,
            Kranz,E.U., Lang,F. and Broer,S.
  TITLE     Na+ transport by the neural glutamine transporter ATA1
  JOURNAL   Pflugers Arch 443 (1), 92-101 (2001)
   PUBMED   11692272
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Gu,S., Roderick,H.L., Camacho,P. and Jiang,J.X.
  TITLE     Characterization of an N-system amino acid transporter expressed in
            retina and its involvement in glutamine transport
  JOURNAL   J Biol Chem 276 (26), 24137-24144 (2001)
   PUBMED   11325958
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Varoqui,H., Zhu,H., Yao,D., Ming,H. and Erickson,J.D.
  TITLE     Cloning and functional identification of a neuronal glutamine
            transporter
  JOURNAL   J Biol Chem 275 (6), 4049-4054 (2000)
   PUBMED   10660562
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF075704.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF075704.1, BC097283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..485
                     /product="sodium-coupled neutral amino acid symporter 1"
                     /note="contains 11 putative transmembrane domains;
                     sodium-coupled neutral amino acid transporter 1; rATA1;
                     glutamine transporter; system A transporter 2; amino acid
                     transporter A1; N-system amino acid transporter 2; system
                     A amino acid transporter 1; system N amino acid
                     transporter 1; amino acid transporter system A1"
                     /calculated_mol_wt=53716
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2P7; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2P7; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2H9; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2H9; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2H9; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Region          69..472
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            75..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            189..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            349..369
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            392..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     Site            451..471
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM15.1)"
     CDS             1..485
                     /gene="Slc38a1"
                     /gene_synonym="Ata1; GlnT; Sat1; Snat1"
                     /coded_by="NM_138832.1:234..1691"
                     /db_xref="GeneID:170567"
                     /db_xref="RGD:69645"
ORIGIN      
        1 mmhfksglel telqnmtvpe ddnvsndsnd ftevengqin skfisdresr rsltnshlek
       61 rkcdeyipgt tslgmsvfnl snaimgsgil glafalantg illflillts vtllsiysin
      121 lllicsketg cmvyeklgeq vfgttgklvi fgatslqntg amlsylfivk nelpsaiksl
      181 mgeeetfsaw yvdgrvlvvm vtfgiilplc llknlgylgy tsgfslscmv fflivviykk
      241 fqipcmngeq nstvsanvtd actpkyvtfn sktvyalpti afafvchpsv lpiyselkdr
      301 sqkkmqmvsn isffamfvmy fltaifgylt fyekvqsdll hkyqstgdil iltvrlaviv
      361 aviltvpvlf ftvrsslfel akktkfhlcr hvlvtiillv iinllvifip smkdifgvvg
      421 vtsanmlifi lpsslylkit nqdgdkntqr iwaalflalg vlfslisipl viydwacsss
      481 ngegh
//
LOCUS       NP_001101677             655 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 21 precursor
            [Rattus norvegicus].
ACCESSION   NP_001101677 XP_001067689 XP_236992
VERSION     NP_001101677.1
DBSOURCE    REFSEQ: accession NM_001108207.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Zhang,D., Cao,X., Li,J. and Zhao,G.
  TITLE     MiR-210 inhibits NF-kappaB signaling pathway by targeting DR6 in
            osteoarthritis
  JOURNAL   Sci Rep 5, 12775 (2015)
   PUBMED   26244598
  REMARK    GeneRIF: The results demonstrated that miR-210 decreased
            inflammation in articular cavity in OA rats by targeting DR6 and
            inhibiting NF-kappaB signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Wang,Y., Zhao,D., Pan,B., Song,Z., Shah,S.Z.A., Yin,X., Zhou,X. and
            Yang,L.
  TITLE     Death Receptor 6 and Caspase-6 Regulate Prion Peptide-Induced
            Axonal Degeneration in Rat Spinal Neurons
  JOURNAL   J Mol Neurosci 56 (4), 966-976 (2015)
   PUBMED   25898930
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Hu,Y., Lee,X., Shao,Z., Apicco,D., Huang,G., Gong,B.J.,
            Pepinsky,R.B. and Mi,S.
  TITLE     A DR6/p75(NTR) complex is responsible for beta-amyloid-induced
            cortical neuron death
  JOURNAL   Cell Death Dis 4 (4), e579 (2013)
   PUBMED   23559013
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Zeng,L., Li,T., Xu,D.C., Liu,J., Mao,G., Cui,M.Z., Fu,X. and Xu,X.
  TITLE     Death receptor 6 induces apoptosis not through type I or type II
            pathways, but via a unique mitochondria-dependent pathway by
            interacting with Bax protein
  JOURNAL   J Biol Chem 287 (34), 29125-29133 (2012)
   PUBMED   22761420
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Mi,S., Lee,X., Hu,Y., Ji,B., Shao,Z., Yang,W., Huang,G., Walus,L.,
            Rhodes,K., Gong,B.J., Miller,R.H. and Pepinsky,R.B.
  TITLE     Death receptor 6 negatively regulates oligodendrocyte survival,
            maturation and myelination
  JOURNAL   Nat Med 17 (7), 816-821 (2011)
   PUBMED   21725297
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Klima,M., Zajedova,J., Doubravska,L. and Andera,L.
  TITLE     Functional analysis of the posttranslational modifications of the
            death receptor 6
  JOURNAL   Biochim Biophys Acta 1793 (10), 1579-1587 (2009)
   PUBMED   19654028
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Schmidt,C.S., Liu,J., Zhang,T., Song,H.Y., Sandusky,G., Mintze,K.,
            Benschop,R.J., Glasebrook,A., Yang,D.D. and Na,S.
  TITLE     Enhanced B cell expansion, survival, and humoral responses by
            targeting death receptor 6
  JOURNAL   J Exp Med 197 (1), 51-62 (2003)
   PUBMED   12515813
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Liu,J., Na,S., Glasebrook,A., Fox,N., Solenberg,P.J., Zhang,Q.,
            Song,H.Y. and Yang,D.D.
  TITLE     Enhanced CD4+ T cell proliferation and Th2 cytokine production in
            DR6-deficient mice
  JOURNAL   Immunity 15 (1), 23-34 (2001)
   PUBMED   11485735
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473987.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_236992.4, XP_001067689.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5756307, SAMEA5760383
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..655
                     /product="tumor necrosis factor receptor superfamily
                     member 21 precursor"
                     /note="death receptor 6; tumor necrosis factor receptor
                     superfamily, member 21"
                     /calculated_mol_wt=67958
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3930
     mat_peptide     42..655
                     /product="Tumor necrosis factor receptor superfamily
                     member 21. /id=PRO_0000425729"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
                     /calculated_mol_wt=67958
     Region          50..88
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          53..211
                     /region_name="TNFRSF21"
                     /note="Tumor necrosis factor receptor superfamily member
                     21 (TNFRSF21), also known as death receptor (DR6);
                     cd10583"
                     /db_xref="CDD:276909"
     Region          67..88
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276909"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          90..131
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          91..131
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..186
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..167
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          170..211
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          214..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZF92.1)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZF92.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          318..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZF92.1)"
     Region          414..497
                     /region_name="Death_TNFRSF21"
                     /note="Death domain of tumor necrosis factor receptor
                     superfamily member 21; cd08778"
                     /db_xref="CDD:176756"
     Region          594..655
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     CDS             1..655
                     /gene="Tnfrsf21"
                     /coded_by="NM_001108207.1:448..2415"
                     /db_xref="GeneID:316256"
                     /db_xref="RGD:1307308"
ORIGIN      
        1 mgtsassita lascsriagq vgatmvagsl lllgflstit aqpeqktlsl tgtyrhvdrt
       61 tgqvltcdkc pagtyvsehc tntslrvcss cpsgtftrhe ngierchdcs qpcprpmier
      121 lpcaaltdre cicppgmyqs ngtcaphtvc pvgwgvrkkg tenedvrckq cargtfsdvp
      181 ssvmkcraht dclgqnlmvv kqgtketdnv cgvhlsssst tpsspgiatf shpehteshd
      241 vpsstyepqg mnstdsnsta svrtkvpsdi qeetvpdnts stsgkestnr tlpnppqlth
      301 qqgphhrhil kllpssmeat geksstaika pkrghprqnp hkhfdinehl pwmivlflll
      361 vlvlivvcsi rkssrtlkkg prqdpsaime kaglkksltp tqnrekwiyy rnghgidilk
      421 lvaaqvgsqw kdiyqflcna serevaafsn gytadheray aalqhwtirg peaslaqlis
      481 alrqhrrndv vekirglmed ttqletdkla lpmspsplsp spipspnvkl enstlltvep
      541 spldknkgff vdesepllrc dstssgssal srngsfitke kkdtvlrqvr ldpcdlqpif
      601 ddmlhilnpe elrvieeipq aedkldrlfe iigvksqeas qtlldsvysh lpdll
//
LOCUS       NP_599203                957 aa            linear   ROD 27-APR-2025
DEFINITION  calsyntenin-3 precursor [Rattus norvegicus].
ACCESSION   NP_599203 XP_346721
VERSION     NP_599203.1
DBSOURCE    REFSEQ: accession NM_134376.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Pettem,K.L., Yokomaku,D., Luo,L., Linhoff,M.W., Prasad,T.,
            Connor,S.A., Siddiqui,T.J., Kawabe,H., Chen,F., Zhang,L.,
            Rudenko,G., Wang,Y.T., Brose,N. and Craig,A.M.
  TITLE     The specific alpha-neurexin interactor calsyntenin-3 promotes
            excitatory and inhibitory synapse development
  JOURNAL   Neuron 80 (1), 113-128 (2013)
   PUBMED   24094106
  REMARK    GeneRIF: The transmembrane form of calsyntenin-3 can trigger
            excitatory and inhibitory presynapse differentiation in contacting
            axons.
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Rindler,M.J., Xu,C.F., Gumper,I., Cen,C., Sonderegger,P. and
            Neubert,T.A.
  TITLE     Calsyntenins are secretory granule proteins in anterior pituitary
            gland and pancreatic islet alpha cells
  JOURNAL   J Histochem Cytochem 56 (4), 381-388 (2008)
   PUBMED   18158283
  REMARK    GeneRIF: Results indicate that calsyntenins function outside the
            nervous system and potentially are modulators of endocrine
            function.
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Hintsch,G., Zurlinden,A., Meskenaite,V., Steuble,M.,
            Fink-Widmer,K., Kinter,J. and Sonderegger,P.
  TITLE     The calsyntenins--a family of postsynaptic membrane proteins with
            distinct neuronal expression patterns
  JOURNAL   Mol Cell Neurosci 21 (3), 393-409 (2002)
   PUBMED   12498782
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ431642.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346721.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ431642.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Rattus norvegicus"
                     /strain="OFA"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..957
                     /product="calsyntenin-3 precursor"
                     /note="alc-beta; alcadein-beta"
                     /calculated_mol_wt=103991
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1972
     mat_peptide     20..957
                     /product="Calsyntenin-3. /id=PRO_0000004028"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R553.1)"
                     /calculated_mol_wt=103991
     Region          32..140
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(39..40,98,100,137,139..140)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          150..239
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R553.1)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R553.1)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R553.1)"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R553.1)"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R553.1)"
     Region          555..914
                     /region_name="CLSTN_C"
                     /note="Calsyntenin C-terminal; pfam19699"
                     /db_xref="CDD:466150"
     Site            741
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8R553.1)"
     Site            849..869
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R553.1)"
     Region          916..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R553.1)"
     CDS             1..957
                     /gene="Clstn3"
                     /gene_synonym="Cs3; Cstn3"
                     /coded_by="NM_134376.1:142..3015"
                     /db_xref="GeneID:171393"
                     /db_xref="RGD:621153"
ORIGIN      
        1 mtlllvslll asllqissgn kankhkpwie aeyqgivmen dntvllnppl faldkdaplr
       61 yageicgfrl hgsgvpfkav ildkatgegl irakepvdce aqkehtfttq aydcvdgpdg
      121 antkkshkat vhvrvndvne fapvfverly raavtegkly drilrveaid gdcspqysqi
      181 cyyeiltpnt pflidndgni enteklqysg eklykftvta ydcgkkraad daeveiqvkp
      241 tckpswqgwn krieyapgag slalfpgirl etcdeplwni qatielqtsh vakgcdrdny
      301 seralrklcg aatgevdllp mpgpnanwta glsvhysqds sliywfngtq avqvplggpa
      361 glgsgpqdgl sdhftlsfwm khsvtpskgk keeetivcnt iqnedgyshy sltvhgcria
      421 flywpllesa rpvkflwkle qvcddewhhy alnlefptvt lytdgisfdp alihdnglih
      481 pprrepalmi gacwseeknk ekekggenst dttsgdplpi hhyfhgylag fsvrsgrles
      541 revieclyac regldyrdfe slgkgmkvhv npsqslltle gddvetfnha lqhvaymntl
      601 rfatpgvrpl rlttavkcfs eescvsipev egyvvvlqpd apqillsgta hfarpavdfe
      661 gpegvplfpd lqitcsishq veakadeswq gtvtdtrmsd eivhnldgce islvgddldp
      721 eresllldma slqqrglelt nrsayltiag vetitvyeei lrqaryqlrh gaalyarkfr
      781 lscsemngry ssnefivevn vlhsmnrvah pshvlssqqf lhrghqpppe maghslassh
      841 rnsmvpsaat liivvcvgfl vlmvilglvr ihslhrrvsg tggpsgasad pkdpdlfwdd
      901 saltiivnpm esyqnqqtgv agvaggqqee edssdseaad spssderrii espphry
//
LOCUS       NP_113980                444 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-associated antigen 4 protein [Rattus norvegicus].
ACCESSION   NP_113980
VERSION     NP_113980.1
DBSOURCE    REFSEQ: accession NM_031792.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Shao,X., Tarnasky,H.A., Lee,J.P., Oko,R. and van der Hoorn,F.A.
  TITLE     Spag4, a novel sperm protein, binds outer dense-fiber protein Odf1
            and localizes to microtubules of manchette and axoneme
  JOURNAL   Dev Biol 211 (1), 109-123 (1999)
   PUBMED   10373309
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Tarnasky,H., Gill,D., Murthy,S., Shao,X., Demetrick,D.J. and van
            der Hoorn,F.A.
  TITLE     A novel testis-specific gene, SPAG4, whose product interacts
            specifically with outer dense fiber protein ODF27, maps to human
            chromosome 20q11.2
  JOURNAL   Cytogenet Cell Genet 81 (1), 65-67 (1998)
   PUBMED   9691178
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF043345.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043345.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..444
                     /product="sperm-associated antigen 4 protein"
                     /note="outer dense fiber-associated protein SPAG4; SUN
                     domain-containing protein 4; sperm antigen 4;
                     sperm-associated antigen 4 protein-like"
                     /calculated_mol_wt=48562
     Region          1..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O55034.2)"
     Site            137..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O55034.2)"
     Site            166..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O55034.2)"
     Region          293..426
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..444
                     /gene="Spag4"
                     /coded_by="NM_031792.1:105..1439"
                     /db_xref="GeneID:83623"
                     /db_xref="RGD:620151"
ORIGIN      
        1 mrrnprpgsa asshnhtpnf ysensnsshs atsgdsngrr sagpelgepd grmargsscg
       61 epalssgvpg gdtwagssrp klaprshngq tacgaatvrg gasepsgspa vleeqlnllp
      121 ildlrqempp ppvsksflsl ffqvlsvfls lvadglvcvy reicsirflf tavsllsifl
      181 aalwwgllyl ipplenepke mltlsqyhhr vhsqgqqlqq lqaelsklhk evtsvraahs
      241 ervaklvfqr lnedfvrkpd yalssvgasi dlektssdye drntayfwnr lsfwnyarpp
      301 svilepdvfp gncwafegeq gqvvirlpgh vqlsditlqh ppptvahtgg assaprdfav
      361 fglqadddet evflgkfife vqkseiqtfh lqndppsafp kvkiqilsnw ghprftclyr
      421 vrahgvrise saednamgvt ggph
//
LOCUS       NP_001007631             223 aa            linear   ROD 27-APR-2025
DEFINITION  AN1-type zinc finger protein 6 [Rattus norvegicus].
ACCESSION   NP_001007631 XP_214987
VERSION     NP_001007631.1
DBSOURCE    REFSEQ: accession NM_001007630.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Zhan,J., Qin,W., Zhang,Y., Jiang,J., Ma,H., Li,Q. and Luo,Y.
  TITLE     Upregulation of neuronal zinc finger protein A20 expression is
            required for electroacupuncture to attenuate the cerebral
            inflammatory injury mediated by the nuclear factor-kB signaling
            pathway in cerebral ischemia/reperfusion rats
  JOURNAL   J Neuroinflammation 13 (1), 258 (2016)
   PUBMED   27716383
  REMARK    GeneRIF: This study demonstrated that the Ischemia/reperfusion
            cortical neurons in MCAO rats are the main cell types that express
            A20, and there is a correlation between A20 expression and the
            suppression of neuroinflammation and the resulting neuroprotective
            effects.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Dai,F.Z., Yang,J., Chen,X.B. and Xu,M.Q.
  TITLE     Zinc finger protein A20 inhibits maturation of dendritic cells
            resident in rat liver allograft
  JOURNAL   J Surg Res 183 (2), 885-893 (2013)
   PUBMED   23481562
  REMARK    GeneRIF: Zinc finger protein A20 inhibits maturation of dendritic
            cells resident in rat liver allograft.
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Peluffo,H., Gonzalez,P., Acarin,L., Aris,A., Beyaert,R.,
            Villaverde,A. and Gonzalez,B.
  TITLE     Overexpression of the nuclear factor kappaB inhibitor A20 is
            neurotoxic after an excitotoxic injury to the immature rat brain
  JOURNAL   Neurol Res 35 (3), 308-319 (2013)
   PUBMED   23336395
  REMARK    GeneRIF: A20 is expressed in astrocytes after brain damage, and its
            overexpression is neurotoxic for cortical neurons in basal mixed
            neuron-glia culture conditions and exacerbates postnatal brain
            excitotoxic damage.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Miyata,N., Okumoto,K., Mukai,S., Noguchi,M. and Fujiki,Y.
  TITLE     AWP1/ZFAND6 functions in Pex5 export by interacting with
            cys-monoubiquitinated Pex5 and Pex6 AAA ATPase
  JOURNAL   Traffic 13 (1), 168-183 (2012)
   PUBMED   21980954
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Chang,E.J., Ha,J., Kang,S.S., Lee,Z.H. and Kim,H.H.
  TITLE     AWP1 binds to tumor necrosis factor receptor-associated factor 2
            (TRAF2) and is involved in TRAF2-mediated nuclear factor-kappaB
            signaling
  JOURNAL   Int J Biochem Cell Biol 43 (11), 1612-1620 (2011)
   PUBMED   21810480
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Lutz,J., Luong le,A., Strobl,M., Deng,M., Huang,H., Anton,M.,
            Zakkar,M., Enesa,K., Chaudhury,H., Haskard,D.O., Baumann,M.,
            Boyle,J., Harten,S., Maxwell,P.H., Pusey,C., Heemann,U. and
            Evans,P.C.
  TITLE     The A20 gene protects kidneys from ischaemia/reperfusion injury by
            suppressing pro-inflammatory activation
  JOURNAL   J Mol Med (Berl) 86 (12), 1329-1339 (2008)
   PUBMED   18813897
  REMARK    GeneRIF: It was observed that A20 was induced in rat kidneys
            exposed to ischaemia/reperfusion.
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Duan,W., Sun,B., Li,T.W., Tan,B.J., Lee,M.K. and Teo,T.S.
  TITLE     Cloning and characterization of AWP1, a novel protein that
            associates with serine/threonine kinase PRK1 in vivo
  JOURNAL   Gene 256 (1-2), 113-121 (2000)
   PUBMED   11054541
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC076394.1.
            
            On Nov 29, 2004 this sequence version replaced XP_214987.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK473343.1, CK481082.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..223
                     /product="AN1-type zinc finger protein 6"
                     /note="zinc finger A20 domain-containing protein 3; zinc
                     finger, A20 domain containing 3; protein associated with
                     PRK1; zinc finger, AN1-type domain 6"
                     /calculated_mol_wt=23870
     Region          12..35
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          41..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DGF4.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6FIF0; propagated from
                     UniProtKB/Swiss-Prot (Q6DGF4.1)"
     Region          164..201
                     /region_name="ZnF_AN1"
                     /note="AN1-like Zinc finger; smart00154"
                     /db_xref="CDD:197545"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCH6; propagated from
                     UniProtKB/Swiss-Prot (Q6DGF4.1)"
     CDS             1..223
                     /gene="Zfand6"
                     /gene_synonym="Za20d3; zgc:101121"
                     /coded_by="NM_001007630.1:110..781"
                     /db_xref="GeneID:293067"
                     /db_xref="RGD:1359317"
ORIGIN      
        1 maqetnhsqa pmlcstgcgf ygnprtngmc svcykehlqr qnssngrisp paasvsslse
       61 slpvqcadgs vpdaqsalds tsssmqpgpv snqsllsesv apsqvdstsv dkavsetedl
      121 qgpraeglvp lecdppssvs dttqqpseeq skslekpkqk knrcfmcrkk vgltgfecrc
      181 gnvycgvhry sdvhncsyny kadaaekirk enpvvvgeki qki
//
LOCUS       NP_001026814             782 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription and DNA repair factor IIH
            helicase/translocase subunit XPB [Rattus norvegicus].
ACCESSION   NP_001026814 XP_214601
VERSION     NP_001026814.1
DBSOURCE    REFSEQ: accession NM_001031644.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   He,Y., Yan,C., Fang,J., Inouye,C., Tjian,R., Ivanov,I. and
            Nogales,E.
  TITLE     Near-atomic resolution visualization of human transcription
            promoter opening
  JOURNAL   Nature 533 (7603), 359-365 (2016)
   PUBMED   27193682
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Sullivan,I., Salazar,J., Majem,M., Pallares,C., Del Rio,E.,
            Paez,D., Baiget,M. and Barnadas,A.
  TITLE     Pharmacogenetics of the DNA repair pathways in advanced non-small
            cell lung cancer patients treated with platinum-based chemotherapy
  JOURNAL   Cancer Lett 353 (2), 160-166 (2014)
   PUBMED   25069034
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Nonnekens,J., Perez-Fernandez,J., Theil,A.F., Gadal,O., Bonnart,C.
            and Giglia-Mari,G.
  TITLE     Mutations in TFIIH causing trichothiodystrophy are responsible for
            defects in ribosomal RNA production and processing
  JOURNAL   Hum Mol Genet 22 (14), 2881-2893 (2013)
   PUBMED   23562818
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Kamileri,I., Karakasilioti,I. and Garinis,G.A.
  TITLE     Nucleotide excision repair: new tricks with old bricks
  JOURNAL   Trends Genet 28 (11), 566-573 (2012)
   PUBMED   22824526
  REMARK    Review article
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Compe,E. and Egly,J.M.
  TITLE     TFIIH: when transcription met DNA repair
  JOURNAL   Nat Rev Mol Cell Biol 13 (6), 343-354 (2012)
   PUBMED   22572993
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2012 Jul;13(7):476]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Hwang,J.R., Moncollin,V., Vermeulen,W., Seroz,T., van Vuuren,H.,
            Hoeijmakers,J.H. and Egly,J.M.
  TITLE     A 3' --> 5' XPB helicase defect in repair/transcription factor
            TFIIH of xeroderma pigmentosum group B affects both DNA repair and
            transcription
  JOURNAL   J Biol Chem 271 (27), 15898-15904 (1996)
   PUBMED   8663148
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Iyer,N., Reagan,M.S., Wu,K.J., Canagarajah,B. and Friedberg,E.C.
  TITLE     Interactions involving the human RNA polymerase II
            transcription/nucleotide excision repair complex TFIIH, the
            nucleotide excision repair protein XPG, and Cockayne syndrome group
            B (CSB) protein
  JOURNAL   Biochemistry 35 (7), 2157-2167 (1996)
   PUBMED   8652557
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Serizawa,H., Conaway,R.C. and Conaway,J.W.
  TITLE     Multifunctional RNA polymerase II initiation factor delta from rat
            liver. Relationship between carboxyl-terminal domain kinase,
            ATPase, and DNA helicase activities
  JOURNAL   J Biol Chem 268 (23), 17300-17308 (1993)
   PUBMED   8394338
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Weeda,G., Ma,L., van Ham,R.C., Bootsma,D., van der Eb,A.J. and
            Hoeijmakers,J.H.
  TITLE     Characterization of the mouse homolog of the XPBC/ERCC-3 gene
            implicated in xeroderma pigmentosum and Cockayne's syndrome
  JOURNAL   Carcinogenesis 12 (12), 2361-2368 (1991)
   PUBMED   1747940
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Weeda,G., van Ham,R.C., Vermeulen,W., Bootsma,D., van der Eb,A.J.
            and Hoeijmakers,J.H.
  TITLE     A presumed DNA helicase encoded by ERCC-3 is involved in the human
            repair disorders xeroderma pigmentosum and Cockayne's syndrome
  JOURNAL   Cell 62 (4), 777-791 (1990)
   PUBMED   2167179
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098856.1.
            
            On Aug 12, 2005 this sequence version replaced XP_214601.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098856.1, SRR8487231.5306.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..782
                     /product="general transcription and DNA repair factor IIH
                     helicase/translocase subunit XPB"
                     /EC_number="5.6.2.4"
                     /note="TFIIH basal transcription factor complex helicase
                     XPB subunit; DNA excision repair protein ERCC-3; excision
                     repair cross-complementing rodent repair deficiency,
                     complementation group 3; excision repair
                     cross-complementation group 3; TFIIH subunit XPB; general
                     transcription and DNA repair factor IIH helicase subunit
                     XPB; DNA 3'-5' helicase/translocase XPB"
                     /calculated_mol_wt=88969
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G005.1)"
     Region          6..18
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G005.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G005.1)"
     Region          60..779
                     /region_name="rad25"
                     /note="DNA repair helicase rad25; TIGR00603"
                     /db_xref="CDD:273168"
     Region          442..445
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G005.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19447; propagated from
                     UniProtKB/Swiss-Prot (Q4G005.1)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P19447; propagated from
                     UniProtKB/Swiss-Prot (Q4G005.1)"
     CDS             1..782
                     /gene="Ercc3"
                     /coded_by="NM_001031644.1:39..2387"
                     /db_xref="GeneID:291703"
                     /db_xref="RGD:1307139"
ORIGIN      
        1 mgkrdrvdrd kkkskkrqye eeeededdap gnesqeavps aagkqvdess tkvdeygakd
       61 yrqqmplkgd htsrplwvap dghifleafs pvykyaqdfl vaiaepvcrp thvheyklta
      121 yslyaavsvg lqtsditeyl rklsktgvpd giiqfiklct vsygkvklvl khnryfvess
      181 hpdviqhllq dpvirecrlr naegeateli tetftsksai sktvegsgga stsqgvdaqa
      241 ksdipkdlfd fyeqmdkdee eeeetqtvsf evkqemieel qkrcicleyp llaeydfrnd
      301 slnpdinidl kptavlrpyq ekslrkmfgn grarsgvivl pcgagkslvg vtaactvrkr
      361 clvlgnsavs veqwkaqfkm wstiddsqic rftsdakdkp igcsiaisty smlghttkrs
      421 weaervmewl ktqewglmil devhtipakm frrvltivqa hcklgltatl vreddkivdl
      481 nfligpklye anwmelqnng yiakvqcaev wcpmspefyr eyvaiktkkr illytmnpnk
      541 fracqflikf herrndkiiv fadnvfalke yairlnkpyi ygptsqgerm qilqnfkhnp
      601 kintifiskv gdtsfdlpea nvliqisshg gsrrqeaqrl grvlrakkgm vaeeynaffy
      661 slvsqdtqem aystkrqrfl vdqgysfkvi tklagmeeee lafstkeeqq qllqkvlaat
      721 dldaeeevva gefgsrsgqa srrfgtmssl sgaddtvyme yhssrnkast khvhplfkrf
      781 rk
//
LOCUS       NP_570100                190 aa            linear   ROD 27-APR-2025
DEFINITION  cytoglobin [Rattus norvegicus].
ACCESSION   NP_570100
VERSION     NP_570100.1
DBSOURCE    REFSEQ: accession NM_130744.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Liu,X., El-Mahdy,M.A., Boslett,J., Varadharaj,S., Hemann,C.,
            Abdelghany,T.M., Ismail,R.S., Little,S.C., Zhou,D., Thuy,L.T.,
            Kawada,N. and Zweier,J.L.
  TITLE     Cytoglobin regulates blood pressure and vascular tone through
            nitric oxide metabolism in the vascular wall
  JOURNAL   Nat Commun 8, 14807 (2017)
   PUBMED   28393874
  REMARK    GeneRIF: Cygb has a critical role in the regulation of vascular
            tone and disease. We suggest that modulation of the expression and
            NOD activity of Cygb represents a strategy for the treatment of
            cardiovascular disease
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Ferreira,J.C., Marcondes,M.F., Icimoto,M.Y., Cardoso,T.H.,
            Tofanello,A., Pessoto,F.S., Miranda,E.G., Prieto,T.,
            Nascimento,O.R., Oliveira,V. and Nantes,I.L.
  TITLE     Intermediate Tyrosyl Radical and Amyloid Structure in
            Peroxide-Activated Cytoglobin
  JOURNAL   PLoS One 10 (8), e0136554 (2015)
   PUBMED   26312997
  REMARK    GeneRIF: This result suggests that Cygb possibly participates in
            the development of degenerative diseases; our findings also support
            the possible biological role of Cygb related to peroxidase
            activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Tian,S.F., Yang,H.H., Xiao,D.P., Huang,Y.J., He,G.Y., Ma,H.R.,
            Xia,F. and Shi,X.C.
  TITLE     Mechanisms of neuroprotection from hypoxia-ischemia (HI) brain
            injury by up-regulation of cytoglobin (CYGB) in a neonatal rat
            model
  JOURNAL   J Biol Chem 288 (22), 15988-16003 (2013)
   PUBMED   23585565
  REMARK    GeneRIF: The reduction of neonatal HI injury by CYGB may be due in
            part to antioxidant and antiapoptotic mechanisms and by promoting
            angiogenesis.
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Tanaka,F., Tominaga,K., Sasaki,E., Sogawa,M., Yamagami,H.,
            Tanigawa,T., Shiba,M., Watanabe,K., Watanabe,T., Fujiwara,Y.,
            Kawada,N., Yoshizato,K. and Arakawa,T.
  TITLE     Cytoglobin may be involved in the healing process of gastric
            mucosal injuries in the late phase without angiogenesis
  JOURNAL   Dig Dis Sci 58 (5), 1198-1206 (2013)
   PUBMED   23306842
  REMARK    GeneRIF: may be involved in the healing process of gastric mucosal
            injuries in the late phase without angiogenesis
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Nishi,H., Inagi,R., Kawada,N., Yoshizato,K., Mimura,I., Fujita,T.
            and Nangaku,M.
  TITLE     Cytoglobin, a novel member of the globin family, protects kidney
            fibroblasts against oxidative stress under ischemic conditions
  JOURNAL   Am J Pathol 178 (1), 128-139 (2011)
   PUBMED   21224051
  REMARK    GeneRIF: These findings show for the first that Cygb serves as a
            defensive mechanism against oxidative stress both in vitro and in
            vivo.
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Xu,R., Harrison,P.M., Chen,M., Li,L., Tsui,T.Y., Fung,P.C.,
            Cheung,P.T., Wang,G., Li,H., Diao,Y., Krissansen,G.W., Xu,S. and
            Farzaneh,F.
  TITLE     Cytoglobin overexpression protects against damage-induced fibrosis
  JOURNAL   Mol Ther 13 (6), 1093-1100 (2006)
   PUBMED   16581302
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Schmidt,M., Gerlach,F., Avivi,A., Laufs,T., Wystub,S.,
            Simpson,J.C., Nevo,E., Saaler-Reinhardt,S., Reuss,S., Hankeln,T.
            and Burmester,T.
  TITLE     Cytoglobin is a respiratory protein in connective tissue and
            neurons, which is up-regulated by hypoxia
  JOURNAL   J Biol Chem 279 (9), 8063-8069 (2004)
   PUBMED   14660570
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Nakatani,K., Okuyama,H., Shimahara,Y., Saeki,S., Kim,D.H.,
            Nakajima,Y., Seki,S., Kawada,N. and Yoshizato,K.
  TITLE     Cytoglobin/STAP, its unique localization in splanchnic
            fibroblast-like cells and function in organ fibrogenesis
  JOURNAL   Lab Invest 84 (1), 91-101 (2004)
   PUBMED   14647402
REFERENCE   9  (residues 1 to 190)
  AUTHORS   Burmester,T., Ebner,B., Weich,B. and Hankeln,T.
  TITLE     Cytoglobin: a novel globin type ubiquitously expressed in
            vertebrate tissues
  JOURNAL   Mol Biol Evol 19 (4), 416-421 (2002)
   PUBMED   11919282
REFERENCE   10 (residues 1 to 190)
  AUTHORS   Kawada,N., Kristensen,D.B., Asahina,K., Nakatani,K., Minamiyama,Y.,
            Seki,S. and Yoshizato,K.
  TITLE     Characterization of a stellate cell activation-associated protein
            (STAP) with peroxidase activity found in rat hepatic stellate cells
  JOURNAL   J Biol Chem 276 (27), 25318-25323 (2001)
   PUBMED   11320098
  REMARK    Erratum:[J Biol Chem 2001 Dec 14;276(50):47744-5]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088455.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088455.1, AJ245663.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676808 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.2"
     Protein         1..190
                     /product="cytoglobin"
                     /EC_number="1.15.1.1"
                     /note="HGb; histoglobin; stellate cell
                     activation-associated protein; globin f; pseudoperoxidase
                     CYGB; nitrite reductase CYGB; superoxide dismutase CYGB;
                     nitric oxygen dioxygenase CYGB"
                     /calculated_mol_wt=21366
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q921A4.1)"
     Region          22..171
                     /region_name="Cygb"
                     /note="Cytoglobin and related globins; cd08924"
                     /db_xref="CDD:271275"
     Site            order(48,51..55,123,125..126,129,132..133,137,155)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:271275"
     Site            order(49,56,59..60,77,80..81,84..85,88..89,109,112..113,
                     116..117,119,123..124,127)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:271275"
     Site            order(89,105,124,127,131,151,154,157)
                     /site_type="other"
                     /note="apolar cavity"
                     /db_xref="CDD:271275"
     CDS             1..190
                     /gene="Cygb"
                     /gene_synonym="Glnf; Staap; Stap"
                     /coded_by="NM_130744.2:171..743"
                     /db_xref="GeneID:170520"
                     /db_xref="RGD:69415"
ORIGIN      
        1 mekvpgdmei errerneels eaerkavqat warlyanced vgvailvrff vnfpsakqyf
       61 sqfkhmedpl emerspqlrk hacrvmgaln tvvenlhdpd kvssvlalvg kahalkhkve
      121 pmyfkilsgv ildviaeefa ndfpvetqka wtklrgliys hvtaaykevg wvqqvpnttt
      181 lpatlpssgp
//
LOCUS       NP_001009541             221 aa            linear   ROD 27-APR-2025
DEFINITION  immediate early response gene 2 protein [Rattus norvegicus].
ACCESSION   NP_001009541
VERSION     NP_001009541.1
DBSOURCE    REFSEQ: accession NM_001009541.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Izquierdo,A.G., Boughanem,H., Diaz-Lagares,A., Arranz-Salas,I.,
            Esteller,M., Tinahones,F.J., Casanueva,F.F., Macias-Gonzalez,M. and
            Crujeiras,A.B.
  TITLE     DNA methylome in visceral adipose tissue can discriminate patients
            with and without colorectal cancer
  JOURNAL   Epigenetics 17 (6), 665-676 (2022)
   PUBMED   34311674
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Kyjacova,L., Saup,R., Ronsch,K., Wallbaum,S., Dukowic-Schulze,S.,
            Foss,A., Scherer,S.D., Rothley,M., Neeb,A., Grau,N., Thiele,W.,
            Thaler,S., Cremers,N., Sticht,C., Gretz,N., Garvalov,B.K.,
            Utikal,J. and Sleeman,J.P.
  TITLE     IER2-induced senescence drives melanoma invasion through
            osteopontin
  JOURNAL   Oncogene 40 (47), 6494-6512 (2021)
   PUBMED   34611309
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Liu,X., Liu,X., Cai,M., Luo,A., He,Y., Liu,S., Zhang,X., Yang,X.,
            Xu,L. and Jiang,H.
  TITLE     CircRNF220, not its linear cognate gene RNF220, regulates cell
            growth and is associated with relapse in pediatric acute myeloid
            leukemia
  JOURNAL   Mol Cancer 20 (1), 139 (2021)
   PUBMED   34702297
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Xu,X., Zhou,W., Chen,Y., Wu,K., Wang,H., Zhang,J., Zhou,Y.,
            Zeng,J., Yang,J., Deng,Z., Zhang,Y. and Shen,W.
  TITLE     Immediate early response protein 2 promotes the migration and
            invasion of hepatocellular carcinoma cells via regulating the
            activity of Rho GTPases
  JOURNAL   Neoplasma 67 (3), 614-622 (2020)
   PUBMED   32009420
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Neeb,A., Wallbaum,S., Novac,N., Dukovic-Schulze,S., Scholl,I.,
            Schreiber,C., Schlag,P., Moll,J., Stein,U. and Sleeman,J.P.
  TITLE     The immediate early gene Ier2 promotes tumor cell motility and
            metastasis, and predicts poor survival of colorectal cancer
            patients
  JOURNAL   Oncogene 31 (33), 3796-3806 (2012)
   PUBMED   22120713
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Takaya,T., Kasatani,K., Noguchi,S. and Nikawa,J.
  TITLE     Functional analyses of immediate early gene ETR101 expressed in
            yeast
  JOURNAL   Biosci Biotechnol Biochem 73 (7), 1653-1660 (2009)
   PUBMED   19584537
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Park,J.B., Kim,E.J., Yang,E.J., Seo,S.R. and Chung,K.C.
  TITLE     JNK- and Rac1-dependent induction of immediate early gene pip92
            suppresses neuronal differentiation
  JOURNAL   J Neurochem 100 (2), 555-566 (2007)
   PUBMED   17156131
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Charles,C.H., Simske,J.S., O'Brien,T.P. and Lau,L.F.
  TITLE     Pip92: a short-lived, growth factor-inducible protein in BALB/c 3T3
            and PC12 cells
  JOURNAL   Mol Cell Biol 10 (12), 6769-6774 (1990)
   PUBMED   2247083
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061717.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC061717.1, CK366536.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..221
                     /product="immediate early response gene 2 protein"
                     /calculated_mol_wt=24465
     Region          1..>100
                     /region_name="IER"
                     /note="Immediate early response protein (IER); pfam05760"
                     /db_xref="CDD:461732"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BTL4; propagated from
                     UniProtKB/Swiss-Prot (Q6P7D3.1)"
     Region          54..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7D3.1)"
     CDS             1..221
                     /gene="Ier2"
                     /coded_by="NM_001009541.1:89..754"
                     /db_xref="GeneID:494344"
                     /db_xref="RGD:1359581"
ORIGIN      
        1 mevqkeaqri mtlsvwkmyh srmqrgglrl hrslqlslvm rsarelylsa kvethqpefp
       61 psrraldprl hpprepeaam eaatpdveqp pepmdtqeev lrvqetpalc dppparvsrk
      121 rrsssdlsdg sdaglvpskk arleevegea tsevsnrlql ppaqtegafp nlarvlqrrf
      181 ssllncgpav ppptpptcea kpacrpadnm lnvlvrtvva f
//
LOCUS       NP_001019509             326 aa            linear   ROD 27-APR-2025
DEFINITION  apoptosis facilitator Bcl-2-like protein 14 [Rattus norvegicus].
ACCESSION   NP_001019509 XP_575700
VERSION     NP_001019509.1
DBSOURCE    REFSEQ: accession NM_001024338.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Lin,M.L., Park,J.H., Nishidate,T., Nakamura,Y. and Katagiri,T.
  TITLE     Involvement of maternal embryonic leucine zipper kinase (MELK) in
            mammary carcinogenesis through interaction with Bcl-G, a
            pro-apoptotic member of the Bcl-2 family
  JOURNAL   Breast Cancer Res 9 (1), R17 (2007)
   PUBMED   17280616
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kibel,A.S., Huagen,J., Guo,C., Isaacs,W.B., Yan,Y., Pienta,K.J. and
            Goodfellow,P.J.
  TITLE     Expression mapping at 12p12-13 in advanced prostate carcinoma
  JOURNAL   Int J Cancer 109 (5), 668-672 (2004)
   PUBMED   14999772
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Guo,B., Godzik,A. and Reed,J.C.
  TITLE     Bcl-G, a novel pro-apoptotic member of the Bcl-2 family
  JOURNAL   J Biol Chem 276 (4), 2780-2785 (2001)
   PUBMED   11054413
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079010.1.
            
            On May 27, 2005 this sequence version replaced XP_575700.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079010.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q43"
     Protein         1..326
                     /product="apoptosis facilitator Bcl-2-like protein 14"
                     /note="bcl2-L-14; Bcl2-like 14 (apoptosis facilitator)"
                     /calculated_mol_wt=36760
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYK4.1)"
     Region          99..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYK4.1)"
     Region          211..225
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYK4.1)"
     Region          <291..320
                     /region_name="Bcl-2_like"
                     /note="Apoptosis regulator proteins of the Bcl-2 family,
                     named after B-cell lymphoma 2. This alignment model spans
                     what have been described as Bcl-2 homology regions BH1,
                     BH2, BH3, and BH4. Many members of this family have an
                     additional C-terminal transmembrane...; cl02575"
                     /db_xref="CDD:470624"
     Region          307..314
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYK4.1)"
     CDS             1..326
                     /gene="Bcl2l14"
                     /coded_by="NM_001024338.1:221..1201"
                     /db_xref="GeneID:500348"
                     /db_xref="RGD:1562777"
ORIGIN      
        1 mcstsvydle dipledddpn siefkilafy arhhvfkstp avfspklsrt rslsqkalgt
       61 wstdswtqis lpcrdslsse khislgkkks swrtlfrvte keeeppsspk eihaqgpfpv
      121 erqgrnqhws rslssveqcl eseavdskva cianrvaeiv yswpppddsq sqgggkfkes
      181 vpkilhfelq gpqlrpcdsk kdgedqiinr ivellkysgd qlgreikrdk alvsifqegl
      241 sysvfrtitd lflrdvdtrg eseikaqgfk aalaidaiak ltaidnhpmn rmlgfgtkyl
      301 reyfspwvqq nggwekilgl sheevd
//
LOCUS       NP_001006984             310 aa            linear   ROD 27-APR-2025
DEFINITION  alpha/beta hydrolase domain-containing protein 17A [Rattus
            norvegicus].
ACCESSION   NP_001006984 XP_216853
VERSION     NP_001006984.1
DBSOURCE    REFSEQ: accession NM_001006983.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Tortosa,E., Adolfs,Y., Fukata,M., Pasterkamp,R.J., Kapitein,L.C.
            and Hoogenraad,C.C.
  TITLE     Dynamic Palmitoylation Targets MAP6 to the Axon to Promote
            Microtubule Stabilization during Neuronal Polarization
  JOURNAL   Neuron 94 (4), 809-825 (2017)
   PUBMED   28521134
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Yokoi,N., Fukata,Y., Sekiya,A., Murakami,T., Kobayashi,K. and
            Fukata,M.
  TITLE     Identification of PSD-95 Depalmitoylating Enzymes
  JOURNAL   J Neurosci 36 (24), 6431-6444 (2016)
   PUBMED   27307232
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Lin,D.T. and Conibear,E.
  TITLE     ABHD17 proteins are novel protein depalmitoylases that regulate
            N-Ras palmitate turnover and subcellular localization
  JOURNAL   Elife 4, e11306 (2015)
   PUBMED   26701913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083686.1.
            
            On Nov 22, 2004 this sequence version replaced XP_216853.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083686.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..310
                     /product="alpha/beta hydrolase domain-containing protein
                     17A"
                     /EC_number="3.1.2.22"
                     /note="abhydrolase domain-containing protein FAM108A;
                     family with sequence similarity 108, member A1;
                     abhydrolase domain-containing protein 17A; protein
                     ABHD17A"
                     /calculated_mol_wt=33863
     Region          38..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIJ5.1)"
     Region          100..305
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96GS6; propagated from
                     UniProtKB/Swiss-Prot (Q5XIJ5.1)"
     CDS             1..310
                     /gene="Abhd17a"
                     /gene_synonym="Fam108a; Fam108a1; RGD1359682; upf0227"
                     /coded_by="NM_001006983.1:333..1265"
                     /db_xref="GeneID:299617"
                     /db_xref="RGD:1359682"
ORIGIN      
        1 mnglsvselc clfccppcpg riaaklaflp peptyslvpe pepgpggaga apsgplrtsa
       61 atpgrwkihl teradfqygq reldtievfv tksaranria cmyvrcvpga rytvlfshgn
      121 avdlgqmcsf yvglgtrigc nifsydysgy gissgrpsek nlyadidaaw qalrtrygis
      181 pdsiilygqs igtvptvdla sryecaavvl hspltsgmrv afpdtkktyc fdafpniekv
      241 skitspvlii hgtedevidf shglalyerc pkaveplwve gaghndiely sqylerlrrf
      301 isqelpsqrt
//
LOCUS       NP_001099612             767 aa            linear   ROD 27-APR-2025
DEFINITION  actin filament-associated protein 1-like 1 [Rattus norvegicus].
ACCESSION   NP_001099612 XP_001058822 XP_238021
VERSION     NP_001099612.1
DBSOURCE    REFSEQ: accession NM_001106142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473971.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001058822.1, XP_238021.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132270, SAMD00132273
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..767
                     /product="actin filament-associated protein 1-like 1"
                     /note="actin filament-associated protein, 110 kDa;
                     AFAP1-like protein 1"
                     /calculated_mol_wt=86744
     Region          83..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZI0; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          164..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          209..314
                     /region_name="PH1_AFAP"
                     /note="Actin filament associated protein family Pleckstrin
                     homology (PH) domain, repeat 1; cd13306"
                     /db_xref="CDD:270116"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZI0; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          341..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZI0; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          418..517
                     /region_name="PH2_AFAP"
                     /note="Actin filament associated protein family Pleckstrin
                     homology (PH) domain, repeat 2; cd13307"
                     /db_xref="CDD:270117"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZI0; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          <561..>702
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          563..605
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AB98.1)"
     Region          704..767
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AB98.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZI0; propagated from
                     UniProtKB/Swiss-Prot (D4AB98.1)"
     CDS             1..767
                     /gene="Afap1l1"
                     /gene_synonym="RGD1311580"
                     /coded_by="NM_001106142.1:99..2402"
                     /db_xref="GeneID:291565"
                     /db_xref="RGD:1311580"
ORIGIN      
        1 mdrsrvleql ipeltrllsl ldheylsdst lekkmavasl lqslqplpak evsflyvnta
       61 dlhsgpsfve slfeefdcdl gdlrdmsddg erskeaspep ikspslrsta dvppplpnkp
      121 ppedyyeeal plgpgkspey isshngcspa qsivdgyyed adssypttrm ngeskssynd
      181 sdamsssyes ydeeeeeekg rqpkhqwpse easmhlvrdc ricafllrkk rfgqwakqlt
      241 vikeeqllcy ksskdrqphl rlpldvctvv yvpkdsrhkr helrfsqgat evlvlalqsr
      301 eqaeewlkvi revsrpigga eslevprspv ilckldqdkr lsqekqnsds dslgmndsss
      361 tlsrreaceh gkgkknslae lkdsmsraag rkitriisfs kkkalsedlq tfssedeapc
      421 cgylnvlvnh gwkerwcrlr cntlyfhkdr tdlhthvnai alrgcevapg fgprhpfafr
      481 ilrnrqevai leascsedmg rwlglllvem gskvtpealh ydyvdvetlt sivsagrnsf
      541 lyaqscqdqw pepriydevp yekvqdeepq rptgaqvkrh asscsekshr adpqvkvkrh
      601 assanqykyg knraeedarr ylvekerlek eketirtelt alrqekkelk eairnnpgak
      661 lkaleeavat ldaqcrakee qridlelklv avkerlqqsl aggpalglsv ssksksqett
      721 nkpqssvpeq slpvncvsem rkrspsivts nqgrvlqkak ewemkkt
//
LOCUS       NP_001012522             289 aa            linear   ROD 27-APR-2025
DEFINITION  protein SET [Rattus norvegicus].
ACCESSION   NP_001012522 XP_226569
VERSION     NP_001012522.1
DBSOURCE    REFSEQ: accession NM_001012504.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Milochau,A., Lagree,V., Benassy,M.N., Chaignepain,S., Papin,J.,
            Garcia-Arcos,I., Lajoix,A., Monterrat,C., Coudert,L.,
            Schmitter,J.M., Ochoa,B. and Lang,J.
  TITLE     Synaptotagmin 11 interacts with components of the RNA-induced
            silencing complex RISC in clonal pancreatic beta-cells
  JOURNAL   FEBS Lett 588 (14), 2217-2222 (2014)
   PUBMED   24882364
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Avet,C., Garrel,G., Denoyelle,C., Laverriere,J.N., Counis,R.,
            Cohen-Tannoudji,J. and Simon,V.
  TITLE     SET protein interacts with intracellular domains of the
            gonadotropin-releasing hormone receptor and differentially
            regulates receptor signaling to cAMP and calcium in gonadotrope
            cells
  JOURNAL   J Biol Chem 288 (4), 2641-2654 (2013)
   PUBMED   23233674
  REMARK    GeneRIF: SET protein interacts with intracellular domains of the
            gonadotropin-releasing hormone receptor and differentially
            regulates receptor signaling to cAMP and calcium in gonadotrope
            cells
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Wang,X., Blanchard,J., Kohlbrenner,E., Clement,N., Linden,R.M.,
            Radu,A., Grundke-Iqbal,I. and Iqbal,K.
  TITLE     The carboxy-terminal fragment of inhibitor-2 of protein
            phosphatase-2A induces Alzheimer disease pathology and cognitive
            impairment
  JOURNAL   FASEB J 24 (11), 4420-4432 (2010)
   PUBMED   20651003
  REMARK    GeneRIF: induced expression of the C-terminal fragment (I(2CTF)) of
            I(2)(PP2A), also called SET, in rat brain, decrease in protein
            phosphatase 2A (PP2A) activity, abnormal hyperphosphorylation of
            tau, and neurodegeneration
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Kajiwara,Y., Akram,A., Katsel,P., Haroutunian,V., Schmeidler,J.,
            Beecham,G., Haines,J.L., Pericak-Vance,M.A. and Buxbaum,J.D.
  TITLE     FE65 binds Teashirt, inhibiting expression of the primate-specific
            caspase-4
  JOURNAL   PLoS One 4 (4), e5071 (2009)
   PUBMED   19343227
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Liu,Z., Jang,S.W., Liu,X., Cheng,D., Peng,J., Yepes,M., Li,X.J.,
            Matthews,S., Watts,C., Asano,M., Hara-Nishimura,I., Luo,H.R. and
            Ye,K.
  TITLE     Neuroprotective actions of PIKE-L by inhibition of SET proteolytic
            degradation by asparagine endopeptidase
  JOURNAL   Mol Cell 29 (6), 665-678 (2008)
   PUBMED   18374643
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Fan,Z., Beresford,P.J., Zhang,D. and Lieberman,J.
  TITLE     HMG2 interacts with the nucleosome assembly protein SET and is a
            target of the cytotoxic T-lymphocyte protease granzyme A
  JOURNAL   Mol Cell Biol 22 (8), 2810-2820 (2002)
   PUBMED   11909973
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Beresford,P.J., Zhang,D., Oh,D.Y., Fan,Z., Greer,E.L., Russo,M.L.,
            Jaju,M. and Lieberman,J.
  TITLE     Granzyme A activates an endoplasmic reticulum-associated
            caspase-independent nuclease to induce single-stranded DNA nicks
  JOURNAL   J Biol Chem 276 (46), 43285-43293 (2001)
   PUBMED   11555662
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Fukukawa,C., Shima,H., Tanuma,N., Ogawa,K. and Kikuchi,K.
  TITLE     Up-regulation of I-2(PP2A)/SET gene expression in rat primary
            hepatomas and regenerating livers
  JOURNAL   Cancer Lett 161 (1), 89-95 (2000)
   PUBMED   11078917
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Misawa,K., Nosaka,T., Morita,S., Kaneko,A., Nakahata,T., Asano,S.
            and Kitamura,T.
  TITLE     A method to identify cDNAs based on localization of green
            fluorescent protein fusion products
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3062-3066 (2000)
   PUBMED   10716735
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Kim,E.G., Choi,M.E. and Ballermann,B.J.
  TITLE     Spatially restricted expression of set mRNA in developing rat
            kidney
  JOURNAL   Am J Physiol 266 (1 Pt 2), F155-F161 (1994)
   PUBMED   7508204
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY325137.1, BQ782936.1 and BU758850.1.
            
            On Apr 21, 2005 this sequence version replaced XP_226569.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..289
                     /product="protein SET"
                     /note="TAF-I; SET nuclear proto-oncogene; I-2PP2A;
                     template-activating factor I; phosphatase 2A inhibitor
                     I2PP2A; liver regeneration-related protein LRRGR00002; SET
                     translocation; SET nuclear oncogene"
                     /calculated_mol_wt=33251
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQU5; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01105; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQU5; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01105; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Region          31..77
                     /region_name="Dimerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63945.2)"
     Region          44..233
                     /region_name="NAP"
                     /note="Nucleosome assembly protein (NAP); pfam00956"
                     /db_xref="CDD:460010"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01105; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Site            67
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQU5; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Region          78..224
                     /region_name="Earmuff domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQU5; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Site            149
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01105; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Region          157..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63945.2)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01105; propagated from
                     UniProtKB/Swiss-Prot (Q63945.2)"
     Region          235..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63945.2)"
     CDS             1..289
                     /gene="Setsip"
                     /gene_synonym="Ab1-115; Set"
                     /coded_by="NM_001012504.1:1..870"
                     /db_xref="GeneID:307947"
                     /db_xref="RGD:1307467"
ORIGIN      
        1 mapkrqsail pqpkkprpva apkledksas pglpkgekeq qeaiehidev qneidrlneq
       61 aseeilkveq kynklrqpff qkrselitki pnfwvttfvn hpqvsallge edeealhylt
      121 rvevtefedi ksgyridfyf denpyfenkv lskefhlnes gdpsskstei kwksgkdltk
      181 cssqtqnkas rkrqheepes fftwftdhsd agadelgevi kddiwpnplq yylvpdmdde
      241 egeaeddddd deeeegledi deegdedege edndedegee geedegedd
//
LOCUS       NP_001099323             973 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent DNA helicase Q5 [Rattus norvegicus].
ACCESSION   NP_001099323 XP_001081701 XP_237812
VERSION     NP_001099323.1
DBSOURCE    REFSEQ: accession NM_001105853.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Kim,T.M., Son,M.Y., Dodds,S., Hu,L., Luo,G. and Hasty,P.
  TITLE     RECQL5 and BLM exhibit divergent functions in cells defective for
            the Fanconi anemia pathway
  JOURNAL   Nucleic Acids Res 43 (2), 893-903 (2015)
   PUBMED   25520194
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Kassube,S.A., Jinek,M., Fang,J., Tsutakawa,S. and Nogales,E.
  TITLE     Structural mimicry in transcription regulation of human RNA
            polymerase II by the DNA helicase RECQL5
  JOURNAL   Nat Struct Mol Biol 20 (7), 892-899 (2013)
   PUBMED   23748380
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Tadokoro,T., Ramamoorthy,M., Popuri,V., May,A., Tian,J., Sykora,P.,
            Rybanska,I., Wilson,D.M. 3rd, Croteau,D.L. and Bohr,V.A.
  TITLE     Human RECQL5 participates in the removal of endogenous DNA damage
  JOURNAL   Mol Biol Cell 23 (21), 4273-4285 (2012)
   PUBMED   22973052
REFERENCE   4  (residues 1 to 973)
  AUTHORS   Ramamoorthy,M., Tadokoro,T., Rybanska,I., Ghosh,A.K., Wersto,R.,
            May,A., Kulikowicz,T., Sykora,P., Croteau,D.L. and Bohr,V.A.
  TITLE     RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation
            and cell cycle progression
  JOURNAL   Nucleic Acids Res 40 (4), 1621-1635 (2012)
   PUBMED   22013166
REFERENCE   5  (residues 1 to 973)
  AUTHORS   Ni,Z., Olsen,J.B., Guo,X., Zhong,G., Ruan,E.D., Marcon,E.,
            Young,P., Guo,H., Li,J., Moffat,J., Emili,A. and Greenblatt,J.F.
  TITLE     Control of the RNA polymerase II phosphorylation state in promoter
            regions by CTD interaction domain-containing proteins RPRD1A and
            RPRD1B
  JOURNAL   Transcription 2 (5), 237-242 (2011)
   PUBMED   22231121
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001081701.1, XP_237812.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..973
                     /product="ATP-dependent DNA helicase Q5"
                     /EC_number="5.6.2.4"
                     /note="DNA helicase, RecQ-like type 5; RecQ protein-like
                     5; RecQ helicase-like 5; DNA 3'-5' helicase RecQ5"
                     /calculated_mol_wt=107091
     Region          12..449
                     /region_name="RecQ"
                     /note="Superfamily II DNA helicase RecQ [Replication,
                     recombination and repair]; COG0514"
                     /db_xref="CDD:440280"
     Region          157..160
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4ACP5.1)"
     Region          491..621
                     /region_name="Interaction with POLR2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4ACP5.1)"
     Region          518..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VID5; propagated from
                     UniProtKB/Swiss-Prot (D4ACP5.1)"
     Region          626..816
                     /region_name="RecQ5"
                     /note="RecQ helicase protein-like 5 (RecQ5); pfam06959"
                     /db_xref="CDD:399738"
     Region          653..726
                     /region_name="Interaction with RAD51.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     Region          679..795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:O94762; propagated from
                     UniProtKB/Swiss-Prot (D4ACP5.1)"
     Region          822..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP5.1)"
     CDS             1..973
                     /gene="Recql5"
                     /gene_synonym="RecQ5"
                     /coded_by="NM_001105853.1:549..3470"
                     /db_xref="GeneID:287834"
                     /db_xref="RGD:1310823"
ORIGIN      
        1 msarpfstpf drerrvrstl kkvfgfdsfk tplqesaima vvkgdkdvfv cmptgagksl
       61 cyqlpavlak gitivvspli aliqdqvdhl lalkvqvssl nsklsvqerk ellsdlerdk
      121 prtkllyitp emaasasfqp tlnsllsrnl lsylvvdeah cvsqwghdfr pdylrlgalr
      181 srlahapcva ltatatpqvq edvfaalhlk qpvasfktpc franlfydvq fkelipdvyg
      241 nlrdfclkal gqkadngsss gcgivycrtr eaceqlaiel ssrgvnakay haglkasert
      301 qvqnewmeek vpvivatisf gmgvdkanvr fvahwniaks magyyqesgr agrdgkpswc
      361 rlyysrndrd qvsflirkel aklqekrgnk psdkatllaf dalvtfceev gcrhaaiaky
      421 fgdappacak gcdccqspaa irkkldaleh ssswgktcig psqgdgfdpe lyeggrrgyg
      481 gfsrydegsg gsgdegrdea hkrewnlfyq rqmslrkgke akpeeftppg edcplrdass
      541 rkipkltvka rehclrllee alnsnhqaag sthgadlqak avelehetfr sakmvnlyka
      601 svlkkvaeih kaskdgqlyd messtkscga iaellepsdy dipptshlys lkpkrvgagf
      661 skgpcpfqta tellgksqte klapeaales eqepsgwvcd pqdgdrskpc lgyqeeapgs
      721 rtncgdpspe krtkgssqgs akaraskrqq llataarkds qsitrflrqr tecpppaasv
      781 pssedaspcg dvpgkcteev gaqghlvavf qtecprerls tcsledqslp kgqpsplket
      841 qaekrprpqq esqekraqkr lrpstnssal asdpstenrv arepcqlsap gislkeaadi
      901 vvryltpfyk egrfiskdlf kgfarhlshl laqklspgrs vkeeaqslik qffhnrarce
      961 seadwhglcg pqr
//
LOCUS       NP_445849                224 aa            linear   ROD 27-APR-2025
DEFINITION  artemin precursor [Rattus norvegicus].
ACCESSION   NP_445849 XP_342892
VERSION     NP_445849.1
DBSOURCE    REFSEQ: accession NM_053397.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Nencini,S., Ringuet,M., Kim,D.H., Greenhill,C. and Ivanusic,J.J.
  TITLE     GDNF, Neurturin, and Artemin Activate and Sensitize Bone Afferent
            Neurons and Contribute to Inflammatory Bone Pain
  JOURNAL   J Neurosci 38 (21), 4899-4911 (2018)
   PUBMED   29712778
  REMARK    GeneRIF: We have shown evidence of a role for GDNF, neurturin, and
            artemin in the activation and sensitization of bone afferent
            neurons, and that sequestering these ligands reduces pain behavior
            in a model of inflammatory bone pain
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Shang,H., Wang,Y., Chao,X., Sun,G., Bai,X., Xu,L., Han,Y., Li,J.,
            Wang,H. and Fan,Z.
  TITLE     Artemin transiently increases iNOS expression in primary cultured
            trigeminal ganglion neurons
  JOURNAL   Neurosci Lett 660, 34-38 (2017)
   PUBMED   28899786
  REMARK    GeneRIF: Results indicate a previously unknown role of artemin in
            regulating inducible form of nitric oxide synthase (iNOS)
            expression in primary cultured TGNs, and regulation of iNOS might
            be involved in the mechanism through which artemin participates in
            the trigeminal pain pathway.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Wong,L.E., Gibson,M.E., Arnold,H.M., Pepinsky,B. and Frank,E.
  TITLE     Artemin promotes functional long-distance axonal regeneration to
            the brainstem after dorsal root crush
  JOURNAL   Proc Natl Acad Sci U S A 112 (19), 6170-6175 (2015)
   PUBMED   25918373
  REMARK    GeneRIF: artemin has a role in robust regeneration of large,
            myelinated sensory axons to the brainstem and in promoting
            functional reinnervation of the cuneate nucleus
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Ikeda-Miyagawa,Y., Kobayashi,K., Yamanaka,H., Okubo,M., Wang,S.,
            Dai,Y., Yagi,H., Hirose,M. and Noguchi,K.
  TITLE     Peripherally increased artemin is a key regulator of TRPA1/V1
            expression in primary afferent neurons
  JOURNAL   Mol Pain 11, 8 (2015)
   PUBMED   25889103
  REMARK    GeneRIF: indicate the important roles of peripherally-derived
            artemin on the regulation of TRPV1/A1 in DRG neurons in
            pathological conditions such as inflammatory and neuropathic pain
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Albers,K.M., Zhang,X.L., Diges,C.M., Schwartz,E.S., Yang,C.I.,
            Davis,B.M. and Gold,M.S.
  TITLE     Artemin growth factor increases nicotinic cholinergic receptor
            subunit expression and activity in nociceptive sensory neurons
  JOURNAL   Mol Pain 10, 31 (2014)
   PUBMED   24886596
  REMARK    GeneRIF: This study suggest that Artn regulates the expression and
            composition of nAChRs in GFRalpha3 nociceptors and that these
            changes contribute to the thermal hypersensitivity that develops in
            response to Artn injection and perhaps to inflammation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Zihlmann,K.B., Ducray,A.D., Schaller,B., Huber,A.W., Krebs,S.H.,
            Andres,R.H., Seiler,R.W., Meyer,M. and Widmer,H.R.
  TITLE     The GDNF family members neurturin, artemin and persephin promote
            the morphological differentiation of cultured ventral mesencephalic
            dopaminergic neurons
  JOURNAL   Brain Res Bull 68 (1-2), 42-53 (2005)
   PUBMED   16325003
  REMARK    GeneRIF: ARTN acts as potent neurotrophic factor that may play an
            important role in the structural development and plasticity of
            ventral mesencephalic dopaminergic neurons
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Bolon,B., Jing,S., Asuncion,F., Scully,S., Pisegna,M., Van,G.Y.,
            Hu,Z., Yu,Y.B., Min,H., Wild,K., Rosenfeld,R.D., Tarpley,J.,
            Carnahan,J., Duryea,D., Hill,D., Kaufman,S., Yan,X.Q., Juan,T.,
            Christensen,K., McCabe,J. and Simonet,W.S.
  TITLE     The candidate neuroprotective agent artemin induces autonomic
            neural dysplasia without preventing peripheral nerve dysfunction
  JOURNAL   Toxicol Pathol 32 (3), 275-294 (2004)
   PUBMED   15204970
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Honma,Y., Araki,T., Gianino,S., Bruce,A., Heuckeroth,R., Johnson,E.
            and Milbrandt,J.
  TITLE     Artemin is a vascular-derived neurotropic factor for developing
            sympathetic neurons
  JOURNAL   Neuron 35 (2), 267-282 (2002)
   PUBMED   12160745
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Stover,T., Gong,T.L., Cho,Y., Altschuler,R.A. and Lomax,M.I.
  TITLE     Expression of the GDNF family members and their receptors in the
            mature rat cochlea
  JOURNAL   Brain Res Mol Brain Res 76 (1), 25-35 (2000)
   PUBMED   10719212
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Baloh,R.H., Tansey,M.G., Lampe,P.A., Fahrner,T.J., Enomoto,H.,
            Simburger,K.S., Leitner,M.L., Araki,T., Johnson,E.M. Jr. and
            Milbrandt,J.
  TITLE     Artemin, a novel member of the GDNF ligand family, supports
            peripheral and central neurons and signals through the
            GFRalpha3-RET receptor complex
  JOURNAL   Neuron 21 (6), 1291-1302 (1998)
   PUBMED   9883723
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079078.1.
            
            On Apr 19, 2005 this sequence version replaced XP_342892.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079078.1, CK476025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN16093042
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..224
                     /product="artemin precursor"
                     /calculated_mol_wt=19473
     sig_peptide     1..39
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4201
     Region          41..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYE8.1)"
     mat_peptide     112..224
                     /product="Artemin. /id=PRO_0000240291"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYE8.1)"
                     /calculated_mol_wt=12105
     Region          126..223
                     /region_name="TGF_beta_Artemin"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in Artemin and similar proteins; cd19381"
                     /db_xref="CDD:381651"
     Site            order(130,132..134,138..141,146..148,150..157,164..166,
                     168,171..172,177..179,181..182,186..187,189..191,193..194,
                     197,199,201,203,206..207,209..211,214..217,223)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381651"
     Site            order(130,132,134,138..141,151..157,164..166,168..169,
                     171..172,177..179,181..182,186..191,193,197,214..217)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381651"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYE8.1)"
     CDS             1..224
                     /gene="Artn"
                     /coded_by="NM_053397.1:258..932"
                     /db_xref="GeneID:362572"
                     /db_xref="RGD:621427"
ORIGIN      
        1 melglgepta lshclrprwq palwptlaal allssvteas ldpmsrspas rdvpspvlap
       61 ptdylpgght ahlcseralr pppqspqpap pppgpalqsp paalrgaraa ragtrssrar
      121 atdargcrlr sqlvpvsalg lghssdelir frfcsgscrr arsphdlsla slldagalrs
      181 ppgsrpisqp ccrptryeav sfmdvnstwr tvdhlsatac gclg
//
LOCUS       NP_113723                284 aa            linear   ROD 27-APR-2025
DEFINITION  bcl-2-like protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_113723
VERSION     NP_113723.2
DBSOURCE    REFSEQ: accession NM_031535.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Perez-Serna,A.A., Dos Santos,R.S., Ripoll,C., Nadal,A.,
            Eizirik,D.L. and Marroqui,L.
  TITLE     BCL-XL Overexpression Protects Pancreatic beta-Cells against
            Cytokine- and Palmitate-Induced Apoptosis
  JOURNAL   Int J Mol Sci 24 (6), 5657 (2023)
   PUBMED   36982731
  REMARK    GeneRIF: BCL-XL Overexpression Protects Pancreatic beta-Cells
            against Cytokine- and Palmitate-Induced Apoptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Alam,M. and Mishra,R.
  TITLE     Bcl-xL expression and regulation in the progression, recurrence,
            and cisplatin resistance of oral cancer
  JOURNAL   Life Sci 280, 119705 (2021)
   PUBMED   34111459
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Rozier,R., Paul,R., Madji Hounoum,B., Villa,E., Mhaidly,R.,
            Chiche,J., Verhoeyen,E., Marchetti,S., Vandenberghe,A.,
            Raucoules,M., Carles,M. and Ricci,J.E.
  TITLE     Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism
  JOURNAL   FEBS J 288 (11), 3547-3569 (2021)
   PUBMED   33340237
  REMARK    GeneRIF: Pharmacological preconditioning protects from
            ischemia/reperfusion-induced apoptosis by modulating Bcl-xL
            expression through a ROS-dependent mechanism.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Liang,J.R. and Yang,H.
  TITLE     Ginkgolic acid (GA) suppresses gastric cancer growth by inducing
            apoptosis and suppressing STAT3/JAK2 signaling regulated by ROS
  JOURNAL   Biomed Pharmacother 125, 109585 (2020)
   PUBMED   32106377
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Sadek,K., Abouzed,T., Nasr,S. and Shoukry,M.
  TITLE     Licochalcone B Ameliorates Liver Cancer via Targeting of Apoptotic
            Genes, DNA Repair Systems, and Cell Cycle Control
  JOURNAL   Iran J Pharm Res 19 (4), 372-386 (2020)
   PUBMED   33841550
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Chao,D.T., Linette,G.P., Boise,L.H., White,L.S., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bcl-XL and Bcl-2 repress a common pathway of cell death
  JOURNAL   J Exp Med 182 (3), 821-828 (1995)
   PUBMED   7650488
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Gonzalez-Garcia,M., Garcia,I., Ding,L., O'Shea,S., Boise,L.H.,
            Thompson,C.B. and Nunez,G.
  TITLE     bcl-x is expressed in embryonic and postnatal neural tissues and
            functions to prevent neuronal cell death
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4304-4308 (1995)
   PUBMED   7753802
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Tilly,J.L., Tilly,K.I., Kenton,M.L. and Johnson,A.L.
  TITLE     Expression of members of the bcl-2 gene family in the immature rat
            ovary: equine chorionic gonadotropin-mediated inhibition of
            granulosa cell apoptosis is associated with decreased bax and
            constitutive bcl-2 and bcl-xlong messenger ribonucleic acid levels
  JOURNAL   Endocrinology 136 (1), 232-241 (1995)
   PUBMED   7828536
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Gonzalez-Garcia,M., Perez-Ballestero,R., Ding,L., Duan,L.,
            Boise,L.H., Thompson,C.B. and Nunez,G.
  TITLE     bcl-XL is the major bcl-x mRNA form expressed during murine
            development and its product localizes to mitochondria
  JOURNAL   Development 120 (10), 3033-3042 (1994)
   PUBMED   7607090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U72349.1 and AY141038.1.
            
            On Sep 21, 2005 this sequence version replaced NP_113723.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U72349.1, BF523847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093050 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..284
                     /product="bcl-2-like protein 1 isoform 1"
                     /note="bcl-2-like protein 1; B cell lymphoma like X;
                     bcl2-L-1; apoptosis regulator Bcl-X; B cell lymphoma 2
                     like"
                     /calculated_mol_wt=31645
     Region          1..>188
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Region          27..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q07817; propagated from
                     UniProtKB/Swiss-Prot (P53563.2)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (P53563.2)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     CDS             1..284
                     /gene="Bcl2l1"
                     /gene_synonym="bcl-X; Bcl-xl; Bcl2l; Bclx"
                     /coded_by="NM_031535.2:164..1018"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:24888"
                     /db_xref="RGD:2200"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapee teperetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaswm atylndhlep
      181 wiqenggwvr ttplvcpplv clssveipnc pfwspgmvve didysgdipg ftlipgvnfg
      241 niddpvfkep vffilatlva pqfhsfvpis rqrktacvft wlkt
//
LOCUS       NP_073637                343 aa            linear   ROD 27-APR-2025
DEFINITION  P2Y purinoceptor 12 [Rattus norvegicus].
ACCESSION   NP_073637
VERSION     NP_073637.1
DBSOURCE    REFSEQ: accession NM_022800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Zou,L., Liu,S., Li,L., Yang,R., Xu,X., Li,G., Zhang,C., Li,G. and
            Liang,S.
  TITLE     Implication of P2Y12 receptor in uc.48+-mediated abnormal
            sympathoexcitatory reflex via superior cervical ganglia in
            myocardial ischemic rats
  JOURNAL   Eur J Pharmacol 927, 175049 (2022)
   PUBMED   35644421
  REMARK    GeneRIF: Implication of P2Y12 receptor in uc.48+-mediated abnormal
            sympathoexcitatory reflex via superior cervical ganglia in
            myocardial ischemic rats.
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wu,G., Xue,P., Jin,H., Zhang,M., Gui,C., Bao,G., Xu,G., Jiang,J.,
            Zhang,J., Cui,S., Cui,Z. and Sun,Y.
  TITLE     Upregulation of P2Y12 inhibits chondrocyte apoptosis in lumbar
            osteoarthritis through the PI3K/AKT signaling pathway
  JOURNAL   Mol Biol Rep 49 (7), 6459-6466 (2022)
   PUBMED   35581507
  REMARK    GeneRIF: Upregulation of P2Y12 inhibits chondrocyte apoptosis in
            lumbar osteoarthritis through the PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Wang,L., Li,N., Wang,F. and Cui,L.
  TITLE     P2Y12 inhibition in macrophages reduces ventricular arrhythmias in
            rats after myocardial ischemia-reperfusion
  JOURNAL   Adv Clin Exp Med 30 (4), 413-420 (2021)
   PUBMED   33908199
  REMARK    GeneRIF: P2Y12 inhibition in macrophages reduces ventricular
            arrhythmias in rats after myocardial ischemia-reperfusion.
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Cohen,E.M., Mohammed,S., Kavurma,M., Nedoboy,P.E., Cartland,S.,
            Farnham,M.M.J. and Pilowsky,P.M.
  TITLE     Microglia in the RVLM of SHR have reduced P2Y12R and CX3CR1
            expression, shorter processes, and lower cell density
  JOURNAL   Auton Neurosci 216, 9-16 (2019)
   PUBMED   30598122
  REMARK    GeneRIF: gene expression of the metabotropic purinergic receptor
            P2Y12 and the fractalkine receptor CX3CR1 was downregulated in the
            Medulla oblongata of Spontaneously Hypertensive Rats compared to
            Wistar kyoto rats (by 37.3% and 30.9% respectively).
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Guo,J., Sheng,X., Dan,Y., Xu,Y., Zhang,Y., Ji,H., Wang,J., Xu,Z.,
            Che,H., Li,G., Liang,S. and Li,G.
  TITLE     Involvement of P2Y12 receptor of stellate ganglion in diabetic
            cardiovascular autonomic neuropathy
  JOURNAL   Purinergic Signal 14 (4), 345-357 (2018)
   PUBMED   30084083
  REMARK    GeneRIF: that P2Y12 receptor in the stellate ganglia may
            participate in developing diabetic autonomic neuropathy
            Erratum:[Purinergic Signal. 2021 Mar;17(1):163. doi:
            10.1007/s11302-020-09741-y. PMID: 33185789]
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Cattaneo,M., Zighetti,M.L., Lombardi,R., Martinez,C., Lecchi,A.,
            Conley,P.B., Ware,J. and Ruggeri,Z.M.
  TITLE     Molecular bases of defective signal transduction in the platelet
            P2Y12 receptor of a patient with congenital bleeding
  JOURNAL   Proc Natl Acad Sci U S A 100 (4), 1978-1983 (2003)
   PUBMED   12578987
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Simon,J., Filippov,A.K., Goransson,S., Wong,Y.H., Frelin,C.,
            Michel,A.D., Brown,D.A. and Barnard,E.A.
  TITLE     Characterization and channel coupling of the P2Y(12) nucleotide
            receptor of brain capillary endothelial cells
  JOURNAL   J Biol Chem 277 (35), 31390-31400 (2002)
   PUBMED   12080041
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Foster,C.J., Prosser,D.M., Agans,J.M., Zhai,Y., Smith,M.D.,
            Lachowicz,J.E., Zhang,F.L., Gustafson,E., Monsma,F.J. Jr.,
            Wiekowski,M.T., Abbondanzo,S.J., Cook,D.N., Bayne,M.L., Lira,S.A.
            and Chintala,M.S.
  TITLE     Molecular identification and characterization of the platelet ADP
            receptor targeted by thienopyridine antithrombotic drugs
  JOURNAL   J Clin Invest 107 (12), 1591-1598 (2001)
   PUBMED   11413167
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Zhang,F.L., Luo,L., Gustafson,E., Lachowicz,J., Smith,M., Qiao,X.,
            Liu,Y.H., Chen,G., Pramanik,B., Laz,T.M., Palmer,K., Bayne,M. and
            Monsma,F.J. Jr.
  TITLE     ADP is the cognate ligand for the orphan G protein-coupled receptor
            SP1999
  JOURNAL   J Biol Chem 276 (11), 8608-8615 (2001)
   PUBMED   11104774
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Hollopeter,G., Jantzen,H.M., Vincent,D., Li,G., England,L.,
            Ramakrishnan,V., Yang,R.B., Nurden,P., Nurden,A., Julius,D. and
            Conley,P.B.
  TITLE     Identification of the platelet ADP receptor targeted by
            antithrombotic drugs
  JOURNAL   Nature 409 (6817), 202-207 (2001)
   PUBMED   11196645
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF313450.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF313450.1, H31419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..343
                     /product="P2Y purinoceptor 12"
                     /note="P2Y12 platelet ADP receptor; purinergic receptor
                     P2Y, G-protein coupled, 12"
                     /calculated_mol_wt=38916
     Site            7
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          32..316
                     /region_name="7tmA_P2Y12"
                     /note="P2Y purinoceptor 12, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd15150"
                     /db_xref="CDD:341326"
     Region          32..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341326"
     Site            34..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          65..90
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341326"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Site            order(99,103,107..108,111..112,115,158,161..162,165,169,
                     180..181,185,193,196..197,200,262,265,269,286)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:341326"
     Region          103..133
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341326"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          145..167
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341326"
     Site            149..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          192..221
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341326"
     Site            192..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Site            240..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          241..269
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341326"
     Region          282..306
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341326"
     Site            285..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     Region          324..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPX4.1)"
     CDS             1..343
                     /gene="P2ry12"
                     /gene_synonym="P2y12"
                     /coded_by="NM_022800.1:124..1155"
                     /db_xref="GeneID:64803"
                     /db_xref="RGD:621681"
ORIGIN      
        1 mevpganats anttsipgts tlcsrdykit qvlfpllytv lffaglitns lamriffqir
       61 sksnfiiflk ntvisdllmi ltfpfkilsd aklgaghlrt lvcqvtsvtf yftmyisisf
      121 lglitidryl kttrpfktss psnllgakil svaiwafmfl lslpnmiltn rrpkdkditk
      181 csflksefgl vwheivnyic qvifwinfli vivcyslitk elyrsyvrtr gsakapkkrv
      241 nikvfiiiav fficfvpfhf aripytlsqt ravfdcnaen tlfyvkestl wltslnacld
      301 pfiyfflcks frnslmsmlr cstsgankkk gqeggdpsee tpm
//
LOCUS       NP_001020313             515 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM35 [Rattus norvegicus].
ACCESSION   NP_001020313 XP_573809
VERSION     NP_001020313.2
DBSOURCE    REFSEQ: accession NM_001025142.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Uchil,P.D., Quinlan,B.D., Chan,W.T., Luna,J.M. and Mothes,W.
  TITLE     TRIM E3 ligases interfere with early and late stages of the
            retroviral life cycle
  JOURNAL   PLoS Pathog 4 (2), e16 (2008)
   PUBMED   18248090
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Lalonde,J.P., Lim,R., Ingley,E., Tilbrook,P.A., Thompson,M.J.,
            McCulloch,R., Beaumont,J.G., Wicking,C., Eyre,H.J.,
            Sutherland,G.R., Howe,K., Solomon,E., Williams,J.H. and
            Klinken,S.P.
  TITLE     HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member
            isolated from a hemopoietic lineage switch, is a candidate tumor
            suppressor
  JOURNAL   J Biol Chem 279 (9), 8181-8189 (2004)
   PUBMED   14662771
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kimura,F., Suzu,S., Nakamura,Y., Nakata,Y., Yamada,M., Kuwada,N.,
            Matsumura,T., Yamashita,T., Ikeda,T., Sato,K. and Motoyoshi,K.
  TITLE     Cloning and characterization of a novel RING-B-box-coiled-coil
            protein with apoptotic function
  JOURNAL   J Biol Chem 278 (27), 25046-25054 (2003)
   PUBMED   12692137
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CB743135.1 and
            BC085942.1.
            
            On Mar 16, 2007 this sequence version replaced NP_001020313.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224662.1, FQ094961.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..515
                     /product="E3 ubiquitin-protein ligase TRIM35"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif-containing protein 35; tripartite
                     motif protein 35"
                     /calculated_mol_wt=58414
     Region          29..94
                     /region_name="RING-HC_TRIM35_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 35 (TRIM35) and similar proteins;
                     cd16599"
                     /db_xref="CDD:438261"
     Region          110..153
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <144..>260
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          317..503
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..515
                     /gene="Trim35"
                     /coded_by="NM_001025142.2:8..1555"
                     /db_xref="GeneID:498538"
                     /db_xref="RGD:1564642"
ORIGIN      
        1 mkaaasvvta aapamepgps vspgpsrsfk eellcavcyd pfrdavtlrc ghnfcrrcvs
       61 gcwevqttps cpvckeravp gelrtnhtln nlvetllree aegarwtgrr sprpcrahra
      121 pltlfcvedk ellccacqad arhqehrvqp ikdtaqdfra kcknmehvlr ekaksfwalr
      181 rtyeaiakhn evqttwlegr irdefdklrd flrveeqatv damkeesrkk hllaeekmkq
      241 laeqtealar eierlqmemk eddmtflmkh ksrkrrlfct vepaplqpgl lmdackyles
      301 lqyrvwkkml gsvesvpfsl dpntaagwlk vaddltsvin hgyrvqvenp erfssapcll
      361 gsqvfskgsh swevdvgglp swrvgvvrvq ahaqaqaqad vggeghshsc yhdtrsgfwy
      421 lcrtqgvdgd hcmtsdtata plvqamprrl rveleceege lsfydserhc hlytfhahfg
      481 evrpyfylga srgdgppepl richlrvsik eeldi
//
LOCUS       NP_001106828             382 aa            linear   ROD 27-APR-2025
DEFINITION  neuropeptide Y receptor type 1 [Rattus norvegicus].
ACCESSION   NP_001106828
VERSION     NP_001106828.1
DBSOURCE    REFSEQ: accession NM_001113357.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Borroto-Escuela,D., Serrano-Castro,P., Sanchez-Perez,J.A.,
            Barbancho-Fernandez,M.A., Fuxe,K. and Narvaez,M.
  TITLE     Enhanced neuronal survival and BDNF elevation via long-term
            co-activation of galanin 2 (GALR2) and neuropeptide Y1 receptors
            (NPY1R): potential therapeutic targets for major depressive
            disorder
  JOURNAL   Expert Opin Ther Targets 28 (4), 295-308 (2024)
   PUBMED   38622072
  REMARK    GeneRIF: Enhanced neuronal survival and BDNF elevation via
            long-term co-activation of galanin 2 (GALR2) and neuropeptide Y1
            receptors (NPY1R): potential therapeutic targets for major
            depressive disorder.
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Sanchez-Marin,L., Flores-Lopez,M., Pastor,A., Gavito,A.L.,
            Suarez,J., de la Torre,R., Pavon,F.J., Rodriguez de Fonseca,F. and
            Serrano,A.
  TITLE     Acute stress and alcohol exposure during adolescence result in an
            anxious phenotype in adulthood: Role of altered
            glutamate/endocannabinoid transmission mechanisms
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 113, 110460 (2022)
   PUBMED   34695542
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Peles,E., Levran,O., Randesi,M., Ott,J., Kreek,M.J. and Adelson,M.
  TITLE     Polymorphisms in Stress-Related Genes Are Associated with Reduced
            Cocaine Abuse and Longer Retention in Methadone Maintenance
            Treatment for Opioid Use Disorder
  JOURNAL   Eur Addict Res 27 (3), 198-205 (2021)
   PUBMED   33242852
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Chen,F., Zhou,Y., Yang,K., Shen,M. and Wang,Y.
  TITLE     NPY stimulates cholesterol synthesis acutely by activating the
            SREBP2-HMGCR pathway through the Y1 and Y5 receptors in murine
            hepatocytes
  JOURNAL   Life Sci 262, 118478 (2020)
   PUBMED   32976883
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Randesi,M., Levran,O., van den Brink,W., Blanken,P., van Ree,J.M.,
            Ott,J. and Kreek,M.J.
  TITLE     Further evidence for the association of GAL, GALR1 and NPY1R
            variants with opioid dependence
  JOURNAL   Pharmacogenomics 21 (13), 903-917 (2020)
   PUBMED   32757697
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Pesini,P., Kopp,J., Wong,H., Walsh,J.H., Grant,G. and Hokfelt,T.
  TITLE     An immunohistochemical marker for Wallerian degeneration of fibers
            in the central and peripheral nervous system
  JOURNAL   Brain Res 828 (1-2), 41-59 (1999)
   PUBMED   10320723
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Kushi,A., Sasai,H., Koizumi,H., Takeda,N., Yokoyama,M. and
            Nakamura,M.
  TITLE     Obesity and mild hyperinsulinemia found in neuropeptide Y-Y1
            receptor-deficient mice
  JOURNAL   Proc Natl Acad Sci U S A 95 (26), 15659-15664 (1998)
   PUBMED   9861026
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Prieto,D., Garcia-Sacristan,A. and Simonsen,U.
  TITLE     Characterization of NPY receptors mediating contraction in rat
            intramyocardial coronary arteries
  JOURNAL   Regul Pept 75-76, 155-160 (1998)
   PUBMED   9802404
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Pedrazzini,T., Seydoux,J., Kunstner,P., Aubert,J.F., Grouzmann,E.,
            Beermann,F. and Brunner,H.R.
  TITLE     Cardiovascular response, feeding behavior and locomotor activity in
            mice lacking the NPY Y1 receptor
  JOURNAL   Nat Med 4 (6), 722-726 (1998)
   PUBMED   9623984
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Eva,C., Keinanen,K., Monyer,H., Seeburg,P. and Sprengel,R.
  TITLE     Molecular cloning of a novel G protein-coupled receptor that may
            belong to the neuropeptide receptor family
  JOURNAL   FEBS Lett 271 (1-2), 81-84 (1990)
   PUBMED   2172008
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.50432.1,
                                           SRR26360186.1168127.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840117, SAMN12840129
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..382
                     /product="neuropeptide Y receptor type 1"
                     /note="FC5; NPY1-R; Neuropepetide Y1 Receptor;
                     neuropeptide Y1 receptor"
                     /calculated_mol_wt=43972
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21555.3)"
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21555.3)"
     Site            17
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21555.3)"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Region          40..330
                     /region_name="7tmA_NPY1R"
                     /note="neuropeptide Y receptor type 1, member of the class
                     A family of seven-transmembrane G protein-coupled
                     receptors; cd15395"
                     /db_xref="CDD:320517"
     Region          41..67
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320517"
     Region          74..99
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320517"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Site            order(96,99..100,112..117,119..120,123,166,168..172,207,
                     210..212,214..216,218..219,275,278..279,281..282,285,
                     297..298,300..302,305,308..309)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320517"
     Region          112..142
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320517"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Region          153..174
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320517"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Region          207..236
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320517"
     Site            211..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Region          255..285
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320517"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Region          298..323
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320517"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21555.3)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P21555.3)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04573; propagated from
                     UniProtKB/Swiss-Prot (P21555.3)"
     CDS             1..382
                     /gene="Npy1r"
                     /gene_synonym="NPY-1"
                     /coded_by="NM_001113357.1:173..1321"
                     /db_xref="GeneID:29358"
                     /db_xref="RGD:3198"
ORIGIN      
        1 mnstlfsrve nysvhynvse nspflafend dchlplavif tlalaygavi ilgvsgnlal
       61 iiiilkqkem rnvtnilivn lsfsdllvav mclpftfvyt lmdhwvfget mcklnpfvqc
      121 vsitvsifsl vliaverhql iinprgwrpn nrhayigitv iwvlavassl pfviyqiltd
      181 epfqnvslaa fkdkyvcfdk fpsdshrlsy ttlllvlqyf gplcfificy fkiyvrlkrr
      241 nnmmdkirds kyrssetkri nvmllsivva favcwlplti fntvfdwnhq iiatcnhnll
      301 fllchltami stcvnpifyg flnknfqrdl qfffnfcdfr srdddyetia mstmhtdvsk
      361 tslkqaspva fkkismndne ki
//
LOCUS       NP_001070896             396 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription factor IIH subunit 2 [Rattus norvegicus].
ACCESSION   NP_001070896 XP_001062050 XP_215466
VERSION     NP_001070896.1
DBSOURCE    REFSEQ: accession NM_001077428.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Melis,J.P., Luijten,M., Mullenders,L.H. and van Steeg,H.
  TITLE     The role of XPC: implications in cancer and oxidative DNA damage
  JOURNAL   Mutat Res 728 (3), 107-117 (2011)
   PUBMED   21763452
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Egly,J.M. and Coin,F.
  TITLE     A history of TFIIH: two decades of molecular biology on a pivotal
            transcription/repair factor
  JOURNAL   DNA Repair (Amst) 10 (7), 714-721 (2011)
   PUBMED   21592869
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC126097.1.
            
            On or before Oct 29, 2006 this sequence version replaced
            XP_215466.2, XP_001062050.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC126097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..396
                     /product="general transcription factor IIH subunit 2"
                     /note="BTF2-p44; basic transcription factor 2 44 kDa
                     subunit; TFIIH basal transcription factor complex p44
                     subunit; general transcription factor IIH, polypeptide 2"
                     /calculated_mol_wt=44572
     Region          11..386
                     /region_name="SSL1"
                     /note="RNA polymerase II transcription
                     initiation/nucleotide excision repair factor TFIIH,
                     subunit SSL1 [Transcription / DNA replication,
                     recombination, and repair]; COG5151"
                     /db_xref="CDD:227480"
     Region          56..240
                     /region_name="vWA_transcription_factor_IIH_type"
                     /note="Transcription factors IIH type: TFIIH is a
                     multiprotein complex that is one of the five general
                     transcription factors that binds RNA polymerase II
                     holoenzyme. Orthologues of these genes are found in all
                     completed eukaryotic genomes and all these proteins...;
                     cd01453"
                     /db_xref="CDD:238730"
     Site            order(66,68,144,178)
                     /site_type="active"
                     /note="partial metal ion-dependent adhesion site (MIDAS)
                     [active]"
                     /db_xref="CDD:238730"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (A0JN27.1)"
     CDS             1..396
                     /gene="Gtf2h2"
                     /gene_synonym="BTF2 p44"
                     /coded_by="NM_001077428.1:64..1254"
                     /db_xref="GeneID:294693"
                     /db_xref="RGD:1310499"
ORIGIN      
        1 mdeepertkr weggyertwe ilkedesgsl katiedilfk akrkrvfehh gqvrlgmmrh
       61 lyvvvdgsrt medqdlkpnr ltctlklley fveeyfdqnp isqigiivtk skraekltel
      121 sgnprkhits lkkavdmtch gepslynsls mamqtlkhmp ghtsrevlii fsslttcdps
      181 niydliktlk takirvsvig lsaevrvctv laretggtyh vildethyke llarhvsppp
      241 assgsecsli rmgfpqhtia slsdqdakps fsmahldnns tepgltlggy fcpqcrakyc
      301 elpveckicg ltlvsaphla rsyhhlfpld afqeipleey kgerfcygcq gelkdqhvyv
      361 ctvcrnvfcv dcdvfvhdsl hccpgcvhki ptqsgv
//
LOCUS       NP_954515                551 aa            linear   ROD 27-APR-2025
DEFINITION  RCC1 and BTB domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_954515 XP_214224
VERSION     NP_954515.1
DBSOURCE    REFSEQ: accession NM_199084.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Wang,J., Teves,M.E., Shen,X., Nagarkatti-Gude,D.R., Hess,R.A.,
            Henderson,S.C., Strauss,J.F. 3rd and Zhang,Z.
  TITLE     Mouse RC/BTB2, a member of the RCC1 superfamily, localizes to
            spermatid acrosomal vesicles
  JOURNAL   PLoS One 7 (6), e39846 (2012)
   PUBMED   22768142
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Devilder,M.C., Cadoret,E., Cherel,M., Moreau,I., Rondeau,G.,
            Bezieau,S. and Moisan,J.P.
  TITLE     cDNA cloning, gene characterization and 13q14.3 chromosomal
            assignment of CHC1-L, a chromosome condensation regulator-like
            guanine nucleotide exchange factor
  JOURNAL   Genomics 54 (1), 99-106 (1998)
   PUBMED   9806834
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061766.1.
            
            On Jan 1, 2004 this sequence version replaced XP_214224.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061766.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..551
                     /product="RCC1 and BTB domain-containing protein 2"
                     /note="regulator of chromosome condensation (RCC1) and BTB
                     (POZ) domain containing protein 2; regulator of chromosome
                     condensation and BTB domain-containing protein 2"
                     /calculated_mol_wt=59992
     Region          64..115
                     /region_name="RCC1 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          <71..335
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          117..169
                     /region_name="RCC1 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          171..222
                     /region_name="RCC1 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          223..274
                     /region_name="RCC1 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          276..326
                     /region_name="RCC1 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          328..382
                     /region_name="RCC1 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P798.1)"
     Region          374..490
                     /region_name="BTB_POZ_RCBTB2_CHC1L"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in RCC1 and BTB
                     domain-containing protein 2 (RCBTB2); cd18354"
                     /db_xref="CDD:349663"
     Region          487..551
                     /region_name="BACK_RCBTB2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     RCC1 and BTB domain-containing protein 2 (RCBTB2);
                     cd18529"
                     /db_xref="CDD:350604"
     CDS             1..551
                     /gene="Rcbtb2"
                     /gene_synonym="Chc1l"
                     /coded_by="NM_199084.1:229..1884"
                     /db_xref="GeneID:290363"
                     /db_xref="RGD:735048"
ORIGIN      
        1 meeevpgfyg esgksvqatl sslkmldvgk wpifslcsee elqlirqacv fgtagnevly
       61 ttvndeifvl gtncsgclgv gdiqstiepr rldsltgkki aslsygsgph ivlattdgev
      121 ftwghnaysq lgngttnhgl vpchistnls nkqvievacg syhslvltsd gevfawgynn
      181 sgqvgsgsta nqpiprrvtg clqnkvvmsi acgqmcsmav vdtgevyvwg yngngqlglg
      241 ssgnqptpcr vaalqgirvq rvacgyahtl vltdegqiya wgansygqlg tgnksnqsyp
      301 tpvvvekdri ieiaachsah tsaaksqggh vymwgqcrgq svilphlthf cctddvfacf
      361 atpavtwrll svepddhltv aeslkrefdn pdtadlkflv dgkyiyahkv llkircehfr
      421 ssledseddi vemsefsypv frafleylyt dnislppeea vglldlatfy setrlkklcq
      481 qtikqgicee naiallsaav kydaqdleef cfrfcinhlt vvtqtsgfae mdhdllknfi
      541 skasrvgafk n
//
LOCUS       NP_001020138             261 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 106A [Rattus norvegicus].
ACCESSION   NP_001020138 XP_213459
VERSION     NP_001020138.1
DBSOURCE    REFSEQ: accession NM_001024967.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Dai,H., Xu,D., Su,J., Jang,J. and Chen,Y.
  TITLE     Transmembrane protein 106a activates mouse peritoneal macrophages
            via the MAPK and NF-kappaB signaling pathways
  JOURNAL   Sci Rep 5, 12461 (2015)
   PUBMED   26215746
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091170.1.
            
            On Jun 25, 2005 this sequence version replaced XP_213459.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132271, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..261
                     /product="transmembrane protein 106A"
                     /calculated_mol_wt=29005
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK83.1)"
     Region          24..251
                     /region_name="DUF1356"
                     /note="Protein of unknown function (DUF1356); pfam07092"
                     /db_xref="CDD:462088"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK83.1)"
     CDS             1..261
                     /gene="Tmem106a"
                     /gene_synonym="RGD1309043"
                     /coded_by="NM_001024967.1:307..1092"
                     /db_xref="GeneID:287722"
                     /db_xref="RGD:1309043"
ORIGIN      
        1 mgkafsqlts qkdedksilp dnpamaskaa nyfstgnrkp shscvpceka astsfvtcpt
       61 cqgngeipqe lekqlvalip ygdqrlkprr tklsvflavt icllifslti fflyprnivv
      121 hpvglnsstv afdethvqln mtnvlnitns nfypvtvtql taevlhqtsv vgqvtsslrl
      181 higplaskqm pyevasrild entykictwp kirvhhilvn iqgaltcsyl thpqqlpfes
      241 feyvdcrenm smphlelprp a
//
LOCUS       NP_075586                525 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear pore glycoprotein p62 [Rattus norvegicus].
ACCESSION   NP_075586 XP_218620
VERSION     NP_075586.1
DBSOURCE    REFSEQ: accession NM_023098.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Huang,X., Yao,J., Liu,L., Chen,J., Mei,L., Huangfu,J., Luo,D.,
            Wang,X., Lin,C., Chen,X., Yang,Y., Ouyang,S., Wei,F., Wang,Z.,
            Zhang,S., Xiang,T., Neculai,D., Sun,Q., Kong,E., Tate,E.W. and
            Yang,A.
  TITLE     S-acylation of p62 promotes p62 droplet recruitment into
            autophagosomes in mammalian autophagy
  JOURNAL   Mol Cell 83 (19), 3485-3501 (2023)
   PUBMED   37802024
  REMARK    GeneRIF: S-acylation of p62 promotes p62 droplet recruitment into
            autophagosomes in mammalian autophagy.
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Chung,H., Choi,J. and Park,S.
  TITLE     Ghrelin protects adult rat hippocampal neural stem cells from
            excessive autophagy during oxygen-glucose deprivation
  JOURNAL   Endocr J 65 (1), 63-73 (2018)
   PUBMED   29057768
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Dewangan,P.S., Sonawane,P.J., Chouksey,A.R. and Chauhan,R.
  TITLE     The Nup62 Coiled-Coil Motif Provides Plasticity for Triple-Helix
            Bundle Formation
  JOURNAL   Biochemistry 56 (22), 2803-2811 (2017)
   PUBMED   28406021
  REMARK    GeneRIF: complexes of Nup62 suggest the crucial role of the
            coiled-coil motifs in providing plasticity to various modular
            assemblies
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Sharma,A., Solmaz,S.R., Blobel,G. and Melcak,I.
  TITLE     Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58
            Form Dynamic Complexes in Solution
  JOURNAL   J Biol Chem 290 (30), 18370-18378 (2015)
   PUBMED   26025361
  REMARK    GeneRIF: we carried out solution analysis utilizing the entire
            ordered regions of Nup62, Nup54, and Nup58, and demonstrate that
            they form a dynamic 'triple complex'
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Kinoshita,Y., Hunter,R.G., Gray,J.D., Mesias,R., McEwen,B.S.,
            Benson,D.L. and Kohtz,D.S.
  TITLE     Role for NUP62 depletion and PYK2 redistribution in dendritic
            retraction resulting from chronic stress
  JOURNAL   Proc Natl Acad Sci U S A 111 (45), 16130-16135 (2014)
   PUBMED   25349423
  REMARK    GeneRIF: Role for NUP62 depletion and PYK2 redistribution in
            dendritic retraction resulting from chronic stress
REFERENCE   6  (residues 1 to 525)
  AUTHORS   D'Onofrio,M., Lee,M.D., Starr,C.M., Miller,M. and Hanover,J.A.
  TITLE     The gene encoding rat nuclear pore glycoprotein p62 is intronless
  JOURNAL   J Biol Chem 266 (18), 11980-11985 (1991)
   PUBMED   2050692
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Cordes,V., Waizenegger,I. and Krohne,G.
  TITLE     Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse:
            cDNA cloning and identification of its glycosylated region
  JOURNAL   Eur J Cell Biol 55 (1), 31-47 (1991)
   PUBMED   1915419
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Carmo-Fonseca,M., Kern,H. and Hurt,E.C.
  TITLE     Human nucleoporin p62 and the essential yeast nuclear pore protein
            NSP1 show sequence homology and a similar domain organization
  JOURNAL   Eur J Cell Biol 55 (1), 17-30 (1991)
   PUBMED   1915414
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Starr,C.M., D'Onofrio,M., Park,M.K. and Hanover,J.A.
  TITLE     Primary sequence and heterologous expression of nuclear pore
            glycoprotein p62
  JOURNAL   J Cell Biol 110 (6), 1861-1871 (1990)
   PUBMED   2190987
REFERENCE   10 (residues 1 to 525)
  AUTHORS   D'Onofrio,M., Starr,C.M., Park,M.K., Holt,G.D., Haltiwanger,R.S.,
            Hart,G.W. and Hanover,J.A.
  TITLE     Partial cDNA sequence encoding a nuclear pore protein modified by
            O-linked N-acetylglucosamine
  JOURNAL   Proc Natl Acad Sci U S A 85 (24), 9595-9599 (1988)
   PUBMED   3200844
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK600248.1 and BC128709.1.
            
            On Aug 8, 2005 this sequence version replaced XP_218620.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK600248.1, FN802488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..525
                     /product="nuclear pore glycoprotein p62"
                     /note="62 kDa nucleoporin; nucleoporin Nup62; nuclear pore
                     glycoprotein 62"
                     /calculated_mol_wt=53266
     Region          1..>188
                     /region_name="Nucleoporin_FG2"
                     /note="Nucleoporin FG repeated region; pfam15967"
                     /db_xref="CDD:435043"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P37198; propagated from
                     UniProtKB/Swiss-Prot (P17955.1)"
     Region          6..144
                     /region_name="5 X 2 AA repeats of F-G.
                     /evidence=ECO:0000250|UniProtKB:P37198"
                     /note="propagated from UniProtKB/Swiss-Prot (P17955.1)"
     Region          260..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17955.1)"
     Region          318..432
                     /region_name="Nsp1_C"
                     /note="Nsp1-like C-terminal region; pfam05064"
                     /db_xref="CDD:461540"
     Region          331..461
                     /region_name="Required for centrosome localization.
                     /evidence=ECO:0000250|UniProtKB:P37198"
                     /note="propagated from UniProtKB/Swiss-Prot (P17955.1)"
     Region          346..>525
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P17955.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37198; propagated from
                     UniProtKB/Swiss-Prot (P17955.1)"
     Site            471
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:3200844; propagated from
                     UniProtKB/Swiss-Prot (P17955.1)"
     CDS             1..525
                     /gene="Nup62"
                     /gene_synonym="Np62"
                     /coded_by="NM_023098.2:136..1713"
                     /db_xref="GeneID:65274"
                     /db_xref="RGD:619938"
ORIGIN      
        1 msgfnfggtg apaggftfgt aktatttpat gfsfsasgtg tggfnfgtps qpaattpsts
       61 lfslatqtst tqtpgfnfgt tpasggtgfs lgistpklsl sstaatpata ntgsfglgss
      121 tltnaisgas tssqgtaptg fvfgssttsa pstgttgfsf tsgsasqpga sgfnigsvgs
      181 laqptalsgs pftpatlatt tagatqpaaa tptaattsag stlfasiaaa passsttvls
      241 lsapattaat ptagtlgfsl kapgaapgas ttsttttttt ttttastsss ttttgfalsl
      301 kplvpagpss vaatalpass tavgtttgpa mtyaqlesli nkwsleledq erhflqqatq
      361 vnawdrtlie ngekitslhr evekvkldqk rldqeldfil sqqkeledll spleesvkeq
      421 sgtiylqhad eerektykla enidaqlkrm aqdlkdiieh lnmaggpadt sdplqqicki
      481 lnahmdslqw vdqssallqr rveeasrvce srrkeqersl riafd
//
LOCUS       NP_071782                229 aa            linear   ROD 27-APR-2025
DEFINITION  platelet-activating factor acetylhydrolase IB subunit alpha2
            [Rattus norvegicus].
ACCESSION   NP_071782 XP_346825
VERSION     NP_071782.1
DBSOURCE    REFSEQ: accession NM_022387.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Kim,G.R., Zhao,T., Kee,H.J., Kee,S.J. and Jeong,M.H.
  TITLE     MicroRNA-212-5p and its target PAFAH1B2 suppress vascular
            proliferation and contraction via the downregulation of RhoA
  JOURNAL   PLoS One 16 (3), e0249146 (2021)
   PUBMED   33760887
  REMARK    GeneRIF: MicroRNA-212-5p and its target PAFAH1B2 suppress vascular
            proliferation and contraction via the downregulation of RhoA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Zhang,G., Assadi,A.H., McNeil,R.S., Beffert,U., Wynshaw-Boris,A.,
            Herz,J., Clark,G.D. and D'Arcangelo,G.
  TITLE     The Pafah1b complex interacts with the reelin receptor VLDLR
  JOURNAL   PLoS One 2 (2), e252 (2007)
   PUBMED   17330141
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Bonin,F., Ryan,S.D., Migahed,L., Mo,F., Lallier,J., Franks,D.J.,
            Arai,H. and Bennett,S.A.
  TITLE     Anti-apoptotic actions of the platelet-activating factor
            acetylhydrolase I alpha2 catalytic subunit
  JOURNAL   J Biol Chem 279 (50), 52425-52436 (2004)
   PUBMED   15456758
  REMARK    GeneRIF: the PAF receptor-independent death pathway is regulated by
            PAF-AH I alpha2
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Arai,H., Koizumi,H., Aoki,J. and Inoue,K.
  TITLE     Platelet-activating factor acetylhydrolase (PAF-AH)
  JOURNAL   J Biochem 131 (5), 635-640 (2002)
   PUBMED   11983068
  REMARK    Review article
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Kitagawa,M., Umezu,M., Aoki,J., Koizumi,H., Arai,H. and Inoue,K.
  TITLE     Direct association of LIS1, the lissencephaly gene product, with a
            mammalian homologue of a fungal nuclear distribution protein, rNUDE
  JOURNAL   FEBS Lett 479 (1-2), 57-62 (2000)
   PUBMED   10940388
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Shmueli,O., Cahana,A. and Reiner,O.
  TITLE     Platelet-activating factor (PAF) acetylhydrolase activity, LIS1
            expression, and seizures
  JOURNAL   J Neurosci Res 57 (2), 176-184 (1999)
   PUBMED   10398295
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Manya,H., Aoki,J., Watanabe,M., Adachi,T., Asou,H., Inoue,Y.,
            Arai,H. and Inoue,K.
  TITLE     Switching of platelet-activating factor acetylhydrolase catalytic
            subunits in developing rat brain
  JOURNAL   J Biol Chem 273 (29), 18567-18572 (1998)
   PUBMED   9660828
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Watanabe,M., Aoki,J., Manya,H., Arai,H. and Inoue,K.
  TITLE     Molecular cloning of cDNAs encoding alpha1, alpha2, and beta
            subunits of rat brain platelet-activating factor acetylhydrolase
  JOURNAL   Biochim Biophys Acta 1401 (1), 73-79 (1998)
   PUBMED   9459487
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081714.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346825.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081714.1, FQ212439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..229
                     /product="platelet-activating factor acetylhydrolase IB
                     subunit alpha2"
                     /EC_number="3.1.1.47"
                     /note="platelet-activating factor acetylhydrolase IB
                     subunit beta; PAF-AH alpha 2; PAFAH subunit beta; PAF-AH
                     subunit beta; PAF-AH 30 kDa subunit; PAF acetylhydrolase
                     30 kDa subunit; platelet-activating factor acetylhydrolase
                     alpha 2 subunit (PAF-AH alpha 2)"
                     /calculated_mol_wt=25450
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P68402; propagated from
                     UniProtKB/Swiss-Prot (O35264.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35264.1)"
     Region          8..217
                     /region_name="PAF_acetylesterase_like"
                     /note="PAF_acetylhydrolase (PAF-AH)_like subfamily of
                     SGNH-hydrolases. Platelet-activating factor (PAF) and
                     PAF-AH are key players in inflammation and in
                     atherosclerosis. PAF-AH is a calcium independent
                     phospholipase A2 which exhibits strong substrate...;
                     cd01820"
                     /db_xref="CDD:238858"
     Site            order(48,75,105,193,196)
                     /site_type="active"
                     /db_xref="CDD:238858"
     Site            order(48,193,196)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238858"
     Site            order(48,75,105)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238858"
     Site            order(49,104,195)
                     /site_type="active"
                     /note="specificity pocket [active]"
                     /db_xref="CDD:238858"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35264.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35264.1)"
     CDS             1..229
                     /gene="Pafah1b2"
                     /coded_by="NM_022387.3:126..815"
                     /db_xref="GeneID:64189"
                     /db_xref="RGD:620332"
ORIGIN      
        1 msqgdsnpaa iphaaediqg ddrwmsqhnr fvldckdkep dvlfvgdsmv qlmqqyeiwr
       61 elfsplhaln fgiggdttrh vlwrlkngel enikpkvivv wvgtnnhent aeevaggiea
      121 ivqlintrqp qakiivlgll prgekpnplr qknakvnqll kvslpklanv qlldidggfv
      181 hsdgaischd mfdflhltgg gyakickplh elimqlleet peekqttia
//
LOCUS       NP_112412                695 aa            linear   ROD 27-APR-2025
DEFINITION  zona pellucida sperm-binding protein 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_112412
VERSION     NP_112412.1
DBSOURCE    REFSEQ: accession NM_031150.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Dai,C., Hu,L., Gong,F., Tan,Y., Cai,S., Zhang,S., Dai,J., Lu,C.,
            Chen,J., Chen,Y., Lu,G., Du,J. and Lin,G.
  TITLE     ZP2 pathogenic variants cause in vitro fertilization failure and
            female infertility
  JOURNAL   Genet Med 21 (2), 431-440 (2019)
   PUBMED   29895852
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Louros,N.N., Chrysina,E.D., Baltatzis,G.E., Patsouris,E.S.,
            Hamodrakas,S.J. and Iconomidou,V.A.
  TITLE     A common 'aggregation-prone' interface possibly participates in the
            self-assembly of human zona pellucida proteins
  JOURNAL   FEBS Lett 590 (5), 619-630 (2016)
   PUBMED   26879157
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Burkart,A.D., Xiong,B., Baibakov,B., Jimenez-Movilla,M. and Dean,J.
  TITLE     Ovastacin, a cortical granule protease, cleaves ZP2 in the zona
            pellucida to prevent polyspermy
  JOURNAL   J Cell Biol 197 (1), 37-44 (2012)
   PUBMED   22472438
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Jose,O., Hernandez-Hernandez,O., Chirinos,M.,
            Gonzalez-Gonzalez,M.E., Larrea,F., Almanza,A., Felix,R., Darszon,A.
            and Trevino,C.L.
  TITLE     Recombinant human ZP3-induced sperm acrosome reaction: evidence for
            the involvement of T- and L-type voltage-gated calcium channels
  JOURNAL   Biochem Biophys Res Commun 395 (4), 530-534 (2010)
   PUBMED   20394732
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Hoodbhoy,T., Aviles,M., Baibakov,B., Epifano,O.,
            Jimenez-Movilla,M., Gauthier,L. and Dean,J.
  TITLE     ZP2 and ZP3 traffic independently within oocytes prior to assembly
            into the extracellular zona pellucida
  JOURNAL   Mol Cell Biol 26 (21), 7991-7998 (2006)
   PUBMED   17047254
REFERENCE   6  (residues 1 to 695)
  AUTHORS   El-Mestrah,M., Castle,P.E., Borossa,G. and Kan,F.W.
  TITLE     Subcellular distribution of ZP1, ZP2, and ZP3 glycoproteins during
            folliculogenesis and demonstration of their topographical
            disposition within the zona matrix of mouse ovarian oocytes
  JOURNAL   Biol Reprod 66 (4), 866-876 (2002)
   PUBMED   11906903
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Bray,C., Son,J.H., Kumar,P., Harris,J.D. and Meizel,S.
  TITLE     A role for the human sperm glycine receptor/Cl(-) channel in the
            acrosome reaction initiated by recombinant ZP3
  JOURNAL   Biol Reprod 66 (1), 91-97 (2002)
   PUBMED   11751269
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Howes,E., Pascall,J.C., Engel,W. and Jones,R.
  TITLE     Interactions between mouse ZP2 glycoprotein and proacrosin; a
            mechanism for secondary binding of sperm to the zona pellucida
            during fertilization
  JOURNAL   J Cell Sci 114 (Pt 22), 4127-4136 (2001)
   PUBMED   11739644
REFERENCE   9  (residues 1 to 695)
  AUTHORS   O'Toole,C.M., Arnoult,C., Darszon,A., Steinhardt,R.A. and
            Florman,H.M.
  TITLE     Ca(2+) entry through store-operated channels in mouse sperm is
            initiated by egg ZP3 and drives the acrosome reaction
  JOURNAL   Mol Biol Cell 11 (5), 1571-1584 (2000)
   PUBMED   10793136
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Akatsuka,K., Yoshida-Komiya,H., Tulsiani,D.R., Orgebin-Crist,M.C.,
            Hiroi,M. and Araki,Y.
  TITLE     Rat zona pellucida glycoproteins: molecular cloning and
            characterization of the three major components
  JOURNAL   Mol Reprod Dev 51 (4), 454-467 (1998)
   PUBMED   9820205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB000929.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000929.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..695
                     /product="zona pellucida sperm-binding protein 2
                     precursor"
                     /note="zona pellucida sperm-binding protein 2; zona
                     pellucida protein A; zona pellucida glycoprotein ZP2; zona
                     pellucida 2 glycoprotein; zona pellucida glycoprotein 2
                     (sperm receptor)"
                     /calculated_mol_wt=75518
     sig_peptide     1..24
                     /note="/evidence=ECO:0000269|PubMed:16342937; propagated
                     from UniProtKB/Swiss-Prot (O54767.1)"
                     /calculated_mol_wt=2945
     mat_peptide     25..619
                     /product="Zona pellucida sperm-binding protein 2.
                     /id=PRO_0000041699"
                     /note="propagated from UniProtKB/Swiss-Prot (O54767.1)"
                     /calculated_mol_wt=67438
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            156..157
                     /site_type="cleavage"
                     /note="Cleavage, by ASTL.
                     /evidence=ECO:0000250|UniProtKB:P20239; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Region          354..614
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            444
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Region          451..473
                     /region_name="Disordered.
                     /evidence=ECO:0000250|UniProtKB:P20239"
                     /note="propagated from UniProtKB/Swiss-Prot (O54767.1)"
     Site            563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (O54767.1)"
     Site            619..620
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:P20239;
                     propagated from UniProtKB/Swiss-Prot (O54767.1)"
     Site            665..685
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O54767.1)"
     CDS             1..695
                     /gene="Zp2"
                     /gene_synonym="Zp-2"
                     /coded_by="NM_031150.1:20..2107"
                     /db_xref="GeneID:81828"
                     /db_xref="RGD:620605"
ORIGIN      
        1 marwqrvywl rslffalvts vnslslpqse npafpgtlic dkdevrvefs srfdmekwnp
       61 slvdtfgnei snctyaldle kfilkfpyet ctikviggyq vnirvqdtna dvsykddvhh
      121 ffcpaiqaei hevseivvcm edlisfsfpq lfsrladenq nvsemgwiik igngtrvhtl
      181 plkdaivqgf nllidsqkit lhvpanatgv ahyvqessyl ytvqlkllfs spgqkitfss
      241 qaicapdlsv acnvthmslt ipefpgklks vgfgqrnipe dqwhangidk eatnglrlhf
      301 rksllktkps ekcpfyqfyf ssleltfnfq gdmlstvidp echcespvsi delctrdgfm
      361 dfevyshqtk palnlesllv gnsscqpifk vqslglarfh iplngcgtrq kfegdkviye
      421 neihalwenp psniifrnse frmtvrchyi rdsmllrahi kshsspvasv kpgplalvlq
      481 typdisyqrp yrkneyplvr ylrqpiymev tvlnrndpni klvlddcwat tfedpasvpq
      541 wqiimdgcey eldnyrttfh aanssaahsg hyqrfdvktf afvsesrgls sliyfhcsal
      601 icnqasplcs vtcpaplrnk reaskegtmt vslpgpiill sddssskgvm npdsyeitkd
      661 iasktlgava alvgsaviig ficylhkkri vrfns
//
LOCUS       NP_062018                519 aa            linear   ROD 27-APR-2025
DEFINITION  acetylcholine receptor subunit gamma precursor [Rattus norvegicus].
ACCESSION   NP_062018
VERSION     NP_062018.1
DBSOURCE    REFSEQ: accession NM_019145.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Witzemann,V., Chevessier,F., Pacifici,P.G. and Yampolsky,P.
  TITLE     The neuromuscular junction: selective remodeling of synaptic
            regulators at the nerve/muscle interface
  JOURNAL   Mech Dev 130 (6-8), 402-411 (2013)
   PUBMED   23032192
  REMARK    Review article
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Rasoulpour,R.J., Ellis-Hutchings,R.G., Terry,C., Millar,N.S.,
            Zablotny,C.L., Gibb,A., Marshall,V., Collins,T., Carney,E.W. and
            Billington,R.
  TITLE     A novel mode-of-action mediated by the fetal muscle nicotinic
            acetylcholine receptor resulting in developmental toxicity in rats
  JOURNAL   Toxicol Sci 127 (2), 522-534 (2012)
   PUBMED   22461452
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Alberola-Die,A., Martinez-Pinna,J., Gonzalez-Ros,J.M., Ivorra,I.
            and Morales,A.
  TITLE     Multiple inhibitory actions of lidocaine on Torpedo nicotinic
            acetylcholine receptors transplanted to Xenopus oocytes
  JOURNAL   J Neurochem 117 (6), 1009-1019 (2011)
   PUBMED   21480901
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Albuquerque,E.X., Pereira,E.F., Alkondon,M. and Rogers,S.W.
  TITLE     Mammalian nicotinic acetylcholine receptors: from structure to
            function
  JOURNAL   Physiol Rev 89 (1), 73-120 (2009)
   PUBMED   19126755
  REMARK    Review article
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Yumoto,N., Wakatsuki,S. and Sehara-Fujisawa,A.
  TITLE     The acetylcholine receptor gamma-to-epsilon switch occurs in
            individual endplates
  JOURNAL   Biochem Biophys Res Commun 331 (4), 1522-1527 (2005)
   PUBMED   15883046
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Marchand,S., Devillers-Thiery,A., Pons,S., Changeux,J.P. and
            Cartaud,J.
  TITLE     Rapsyn escorts the nicotinic acetylcholine receptor along the
            exocytic pathway via association with lipid rafts
  JOURNAL   J Neurosci 22 (20), 8891-8901 (2002)
   PUBMED   12388596
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Keller,S.H., Lindstrom,J. and Taylor,P.
  TITLE     Involvement of the chaperone protein calnexin and the acetylcholine
            receptor beta-subunit in the assembly and cell surface expression
            of the receptor
  JOURNAL   J Biol Chem 271 (37), 22871-22877 (1996)
   PUBMED   8798466
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Witzemann,V., Stein,E., Barg,B., Konno,T., Koenen,M., Kues,W.,
            Criado,M., Hofmann,M. and Sakmann,B.
  TITLE     Primary structure and functional expression of the alpha-, beta-,
            gamma-, delta- and epsilon-subunits of the acetylcholine receptor
            from rat muscle
  JOURNAL   Eur J Biochem 194 (2), 437-448 (1990)
   PUBMED   1702709
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Gu,Y., Franco,A. Jr., Gardner,P.D., Lansman,J.B., Forsayeth,J.R.
            and Hall,Z.W.
  TITLE     Properties of embryonic and adult muscle acetylcholine receptors
            transiently expressed in COS cells
  JOURNAL   Neuron 5 (2), 147-157 (1990)
   PUBMED   2383398
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Witzemann,V., Barg,B., Nishikawa,Y., Sakmann,B. and Numa,S.
  TITLE     Differential regulation of muscle acetylcholine receptor gamma- and
            epsilon-subunit mRNAs
  JOURNAL   FEBS Lett 223 (1), 104-112 (1987)
   PUBMED   3666131
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X74834.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X74834.1, SRR8487230.73989.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..519
                     /product="acetylcholine receptor subunit gamma precursor"
                     /note="acetylcholine receptor subunit gamma; cholinergic
                     receptor, nicotinic, gamma (muscle); cholinergic receptor,
                     nicotinic gamma; cholinergic receptor, nicotinic, gamma
                     polypeptide; AChR gamma subunit"
                     /calculated_mol_wt=56418
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2222
     mat_peptide     23..519
                     /product="acetylcholine receptor subunit gamma"
                     /calculated_mol_wt=56418
     Region          49..241
                     /region_name="LGIC_ECD_nAChR_G"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit gamma (CHRNG); cd19029"
                     /db_xref="CDD:349830"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18916.2)"
     Site            order(61,69,97,99,101,103,111,119,121,129,141..143,149,
                     171..172,177,202)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349830"
     Region          150..164
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349830"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18916.2)"
     Site            241..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18916.2)"
     Region          248..494
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            274..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18916.2)"
     Site            308..329
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18916.2)"
     Site            477..497
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18916.2)"
     CDS             1..519
                     /gene="Chrng"
                     /gene_synonym="ACHRG"
                     /coded_by="NM_019145.1:133..1692"
                     /db_xref="GeneID:25753"
                     /db_xref="RGD:2354"
ORIGIN      
        1 mhggqgpqll llllatclga qsrnqeerll adlmrnydph lrpaerdsdv vnvslkltlt
       61 nlislneree alttnvwiem qwcdyrlrwd pkdyeglwil rvpstmvwqp divlgnnvdg
      121 vfevalycnv lvspdgciyw lppaifrssc sisvtyfpfd wqncslvfqs qtystseinl
      181 qlsqedgqai ewifidpeaf tengewairh rpakmlldpv tpaeeaghqk vvfylliqrk
      241 plfyviniiv pcvlissvai liyflpakag gqkctvatnv llaqtvflfl vakkvpetsq
      301 avpliskylt flmvvtiliv vnsvvvlnvs lrsphthsma rgvrkvflrl lpqllrmhvh
      361 prapaavqda rlrlqngsss gwpimtreeg dlclprsell frqrqrnglv qavlekleng
      421 pemrqsqefc gslkqaspai qacvdacnlm ararhqqshf dsgneewllv grvldrvcfl
      481 amlslficgt agiflmahyn qvpdlpfpgd prpylplpd
//
LOCUS       NP_001014087             401 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC domain-containing protein 12 [Rattus norvegicus].
ACCESSION   NP_001014087 XP_233280
VERSION     NP_001014087.1
DBSOURCE    REFSEQ: accession NM_001014065.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Cho,G., Lim,Y. and Golden,J.A.
  TITLE     XLMR candidate mouse gene, Zcchc12 (Sizn1) is a novel marker of
            Cajal-Retzius cells
  JOURNAL   Gene Expr Patterns 11 (3-4), 216-220 (2011)
   PUBMED   21172456
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Cho,G., Lim,Y. and Golden,J.A.
  TITLE     SUMO interaction motifs in Sizn1 are required for promyelocytic
            leukemia protein nuclear body localization and for transcriptional
            activation
  JOURNAL   J Biol Chem 284 (29), 19592-19600 (2009)
   PUBMED   19416967
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089115.1 and BF405776.1.
            
            On Apr 20, 2005 this sequence version replaced XP_233280.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089115.1, CO404055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132267, SAMD00132270
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq34"
     Protein         1..401
                     /product="zinc finger CCHC domain-containing protein 12"
                     /note="zinc finger, CCHC domain containing 12"
                     /calculated_mol_wt=45023
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HZA3.1)"
     Region          <9..212
                     /region_name="PNMA"
                     /note="pfam14893"
                     /db_xref="CDD:464357"
     Region          270..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HZA3.1)"
     CDS             1..401
                     /gene="Zcchc12"
                     /coded_by="NM_001014065.2:383..1588"
                     /db_xref="GeneID:313436"
                     /db_xref="RGD:1359439"
ORIGIN      
        1 masilsrmgn srgqnsplpp wahsmlrslg rslgplmasm aernmklfsg raepaqgeet
       61 fenwlsqvta vlpdwhmpee ekvrrlmrtl rgparevmrl lqaanpcldv edflramklv
      121 fgesessvta hskfvntvqe pgekpslyvi rlevqlqnai qagvfaerea nqarlhqllv
      181 gaemstdlrf rlksllrvya neperlpnfl elirmireee eweeafihpk rprrsqsver
      241 alsptfqssp pvmissidcn vieiddspdd sdedvilvep ddpplpsssa gpsflgravs
      301 edqvlviesp nifeiqapst ssgagrknnn nfgelrrark rkhtvhcshc geeghsketc
      361 dnesdrgqvf enliitlqel thteerarei fgeaiglsel h
//
LOCUS       NP_037072                543 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 1B1 [Rattus norvegicus].
ACCESSION   NP_037072 XP_346760
VERSION     NP_037072.1
DBSOURCE    REFSEQ: accession NM_012940.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Zuo,C., Fan,P., Yang,Y. and Hu,C.
  TITLE     MiR-488-3p facilitates wound healing through CYP1B1-mediated
            Wnt/beta-catenin signaling pathway by targeting MeCP2
  JOURNAL   J Diabetes Investig 15 (2), 145-158 (2024)
   PUBMED   37961023
  REMARK    GeneRIF: MiR-488-3p facilitates wound healing through
            CYP1B1-mediated Wnt/beta-catenin signaling pathway by targeting
            MeCP2.
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Lidin,E., Skold,M.K., Angeria,M., Davidsson,J. and Risling,M.
  TITLE     Hippocampal Expression of Cytochrome P450 1B1 in Penetrating
            Traumatic Brain Injury
  JOURNAL   Int J Mol Sci 23 (2), 722 (2022)
   PUBMED   35054909
  REMARK    GeneRIF: Hippocampal Expression of Cytochrome P450 1B1 in
            Penetrating Traumatic Brain Injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Kulas,J., Tucovic,D., Zeljkovic,M., Popovic,D., Popov
            Aleksandrov,A., Kataranovski,M. and Mirkov,I.
  TITLE     Aryl Hydrocarbon Receptor is Involved in the Proinflammatory
            Cytokine Response to Cadmium
  JOURNAL   Biomed Environ Sci 34 (3), 192-202 (2021)
   PUBMED   33766215
  REMARK    GeneRIF: Aryl Hydrocarbon Receptor is Involved in the
            Proinflammatory Cytokine Response to Cadmium.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Han,Y., Dong,B., Chen,M. and Yao,C.
  TITLE     LncRNA H19 suppresses pyroptosis of cardiomyocytes to attenuate
            myocardial infarction in a PBX3/CYP1B1-dependent manner
  JOURNAL   Mol Cell Biochem 476 (3), 1387-1400 (2021)
   PUBMED   33389498
  REMARK    GeneRIF: LncRNA H19 suppresses pyroptosis of cardiomyocytes to
            attenuate myocardial infarction in a PBX3/CYP1B1-dependent manner.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Alghamdi,A., Aldossary,W., Albahkali,S., Alotaibi,B. and
            Alrfaei,B.M.
  TITLE     The loss of microglia activities facilitates glaucoma progression
            in association with CYP1B1 gene mutation (p.Gly61Glu)
  JOURNAL   PLoS One 15 (11), e0241902 (2020)
   PUBMED   33170892
  REMARK    GeneRIF: The loss of microglia activities facilitates glaucoma
            progression in association with CYP1B1 gene mutation (p.Gly61Glu).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Stoilov,I., Akarsu,A.N. and Sarfarazi,M.
  TITLE     Identification of three different truncating mutations in
            cytochrome P4501B1 (CYP1B1) as the principal cause of primary
            congenital glaucoma (Buphthalmos) in families linked to the GLC3A
            locus on chromosome 2p21
  JOURNAL   Hum Mol Genet 6 (4), 641-647 (1997)
   PUBMED   9097971
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Christou,M., Savas,U., Schroeder,S., Shen,X., Thompson,T.,
            Gould,M.N. and Jefcoate,C.R.
  TITLE     Cytochromes CYP1A1 and CYP1B1 in the rat mammary gland:
            cell-specific expression and regulation by polycyclic aromatic
            hydrocarbons and hormones
  JOURNAL   Mol Cell Endocrinol 115 (1), 41-50 (1995)
   PUBMED   8674863
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Walker,N.J., Gastel,J.A., Costa,L.T., Clark,G.C., Lucier,G.W. and
            Sutter,T.R.
  TITLE     Rat CYP1B1: an adrenal cytochrome P450 that exhibits sex-dependent
            expression in livers and kidneys of TCDD-treated animals
  JOURNAL   Carcinogenesis 16 (6), 1319-1327 (1995)
   PUBMED   7788849
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Bhattacharyya,K.K., Brake,P.B., Eltom,S.E., Otto,S.A. and
            Jefcoate,C.R.
  TITLE     Identification of a rat adrenal cytochrome P450 active in
            polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a
            unique tissue-specific pattern of hormonal and aryl hydrocarbon
            receptor-linked regulation
  JOURNAL   J Biol Chem 270 (19), 11595-11602 (1995)
   PUBMED   7744798
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Pottenger,L.H., Christou,M. and Jefcoate,C.R.
  TITLE     Purification and immunological characterization of a novel
            cytochrome P450 from C3H/10T1/2 cells
  JOURNAL   Arch Biochem Biophys 286 (2), 488-497 (1991)
   PUBMED   1910294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U09540.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346760.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09540.1, SRR8487227.95902.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..543
                     /product="cytochrome P450 1B1"
                     /EC_number="1.14.14.1"
                     /EC_number="4.2.1.152"
                     /note="CYPIB1; P450RAP; cytochrome P450RAP; cytochrome
                     P450, subfamily 1B, polypeptide 1; hydroperoxy
                     icosatetraenoate dehydratase"
                     /calculated_mol_wt=60426
     Region          81..518
                     /region_name="CYP1B1-like"
                     /note="cytochrome P450 family 1, subfamily B, polypeptide
                     1 and similar cytochrome P450s; cd20675"
                     /db_xref="CDD:410768"
     Site            order(117,132..133,141,145,152,327,330..331,334..335,
                     394..395,398..399,401,424,462..464,468,470..472,476)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410768"
     Site            order(126..127,131,133..134,228,231,264..265,268,326,
                     329..330,333..334,395,399,509..510)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410768"
     Site            395
                     /site_type="other"
                     /note="Major determinant of CYP1B1 17beta-estradiol
                     hydroxylation regiospecificity; propagated from
                     UniProtKB/Swiss-Prot (Q64678.1)"
     CDS             1..543
                     /gene="Cyp1b1"
                     /coded_by="NM_012940.2:372..2003"
                     /db_xref="GeneID:25426"
                     /db_xref="RGD:2460"
ORIGIN      
        1 matslsadsp qqlsslstqq tillllvsvl aivhlgqwll rqwrrkpwss ppgpfpwpli
       61 gnaasvgras hlyfarlarr ygdvfqirlg scpvvvlnge saihqalvqq ggvfadrppf
      121 asfrvvsggr slafghyser wkerrraayg tmrafstrhp rsrgllegha lgearelvav
      181 lvrrcaggac ldptqpiiva vanvmsavcf gcrynhddae flellshnee fgrtvgagsl
      241 vdvmpwlqlf pnpvrtifre feqinrnfsn fvldkflrhr eslvpgaapr dmmdafilsa
      301 ekkatgdpgd spsgldledv patitdifga sqdtlstall wllilftryp dvqarvqael
      361 dqvvgrdrlp cmsdqpnlpy vmaflyesmr ftsflpvtlp hattantfvl gyyipkntvv
      421 fvnqwsvnhd pakwsnpedf dparfldkdg finkalassv mifsvgkrrc igeelsktll
      481 flfisilahq cnfkanqnep snmsfsygls ikpksfkihv slresmklld saveklqaee
      541 acq
//
LOCUS       NP_001001514             573 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001001514 XP_341237
VERSION     NP_001001514.1
DBSOURCE    REFSEQ: accession NM_001001514.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Barrientos,T., Frank,D., Kuwahara,K., Bezprozvannaya,S.,
            Pipes,G.C., Bassel-Duby,R., Richardson,J.A., Katus,H.A., Olson,E.N.
            and Frey,N.
  TITLE     Two novel members of the ABLIM protein family, ABLIM-2 and -3,
            associate with STARS and directly bind F-actin
  JOURNAL   J Biol Chem 282 (11), 8393-8403 (2007)
   PUBMED   17194709
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Klimov,E., Rud'ko,O., Rakhmanaliev,E. and Sulimova,G.
  TITLE     Genomic organisation and tissue specific expression of ABLIM2 gene
            in human, mouse and rat
  JOURNAL   Biochim Biophys Acta 1730 (1), 1-9 (2005)
   PUBMED   16005990
  REMARK    GeneRIF: The highest expression of both isoforms was observed in
            rat brain and eye and in mouse embryos. ABLIM2 protein was
            necessary for the normal functioning of neurons.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ703893.2.
            
            On Aug 30, 2004 this sequence version replaced XP_341237.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            two-exon segment in the 3' coding region, compared to variant 1.
            The resulting isoform (b) lacks an internal segment, compared to
            isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ703893.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..573
                     /product="actin-binding LIM protein 2 isoform b"
                     /note="abLIM-2; actin-binding LIM protein 2"
                     /calculated_mol_wt=63669
     Region          24..75
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(24,27,44,47,50,53,71,74)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          80..135
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(83,86,103,106,109,112,131,134)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          153..204
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(153,156,174,177,180,183,200,203)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          212..267
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(212,215,232,235,238,241,260,263)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          276..523
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          538..573
                     /region_name="VHP"
                     /note="Villin headpiece domain; pfam02209"
                     /db_xref="CDD:460493"
     CDS             1..573
                     /gene="Ablim2"
                     /coded_by="NM_001001514.2:159..1880"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:360958"
                     /db_xref="RGD:1303094"
ORIGIN      
        1 msavsqpqaa haplekpast ailcntcgnv ckgevlrvqn khfhircfvc kacgcdlaeg
       61 gffvrqgehi ctrdyqrlyg trcfscdcfi egevvsalgk tyhpdcfvca vcrlpfppgd
      121 rvtfngkdcm cqkcspptlv gnsahvaqgl rscggcglei kngqalvald khwhlgcfkc
      181 ktcgkllnae yiskdglpyc eadyhtkfgi rcdgcekyit grvleagekh yhpscalcvr
      241 cgqmfsegee mylqgssiwh pacrqaarte dksketrtss esivsvpass tsgspsrviy
      301 aklgdeildy rdlaalpknk aiynidrpdm isyspyishs avgdrqsyge gdqddrsykq
      361 crtsspssag svslghytpt srspqhysrp gsesgrstps lsvhsdsrpp sstyqqaprh
      421 fhvpdtgvkd niyrkppiyk qhaarrldve dssfdqdsrk kttwlllkgd adtrtnspdl
      481 dsqslslssg adqeplqrmp gdslysqyki ypydslivtn rirvklpkdv drtrlerhls
      541 peefqevfgm sieefdrlal wkrndlkkka llf
//
LOCUS       NP_001014038             463 aa            linear   ROD 27-APR-2025
DEFINITION  interferon-inducible GTPase 5 [Rattus norvegicus].
ACCESSION   NP_001014038 XP_218443
VERSION     NP_001014038.1
DBSOURCE    REFSEQ: accession NM_001014016.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079061.1.
            
            On Apr 20, 2005 this sequence version replaced XP_218443.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079061.1, CK600500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..463
                     /product="interferon-inducible GTPase 5"
                     /note="immunity-related GTPase cinema 1; immunity-related
                     GTPase family, cinema 1; interferon-gamma-inducible GTPase
                     Ifgge protein"
                     /calculated_mol_wt=50425
     Region          <17..>75
                     /region_name="YlqF_related_GTPase"
                     /note="Circularly permuted YlqF-related GTPases; cl49605"
                     /db_xref="CDD:483945"
     Site            37..39
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206746"
     Region          53..249
                     /region_name="p47_IIGP_like"
                     /note="p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47,
                     GTPI, LRG-47, and IIGP1; cd04104"
                     /db_xref="CDD:206690"
     Site            60..67
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206690"
     Site            60..67
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206746"
     Site            order(63..68,86..87,168,170..171,215..217)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206690"
     Site            88..98
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206690"
     Site            92
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206690"
     Site            110..113
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206690"
     Site            order(112..130,132..135)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206690"
     Site            order(152..153,156..157,159,162)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206690"
     Site            167..170
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206690"
     Site            215..217
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206690"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF9.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF9.1)"
     Region          409..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF9.1)"
     CDS             1..463
                     /gene="Irgc"
                     /gene_synonym="Ifgge; Irgc1; RGD1311107"
                     /coded_by="NM_001014016.1:233..1624"
                     /db_xref="GeneID:308428"
                     /db_xref="RGD:1311107"
ORIGIN      
        1 matsrlpavp eeettilmak eelealrtaf esgdipqaas rlrellatte ttrlevgvtg
       61 esgagkssli nalrgvgaed pgaaltgvve ttmqpspyph pqfpdvtlwd lpgagspgcs
      121 adkylkevdf grydffllvs prrcgavetr laseilrqgk kfyfvrtkvd edlaatrnqr
      181 psgfseaavl qeirdhcaer lraaglsdpr iflvsnlspn rydfpmlvtt wehdlpahrr
      241 hagllslpdi slealqkkkd mlqeqvlkta lvsgviqalp vpglaaaydd allirslrgy
      301 hrsfglddds laklaeqvgk qagdlrsvir splanevspe tvlrlysqss dgamrvaraf
      361 ergipvfgtl vaggisfgtv ytmlqgclne maedaqrvri kaleedetqg evsleaagdn
      421 avekrssgeg tseeaplstr rklglllkyi ldswkrrdls edk
//
LOCUS       NP_071587                945 aa            linear   ROD 27-APR-2025
DEFINITION  glutamyl aminopeptidase [Rattus norvegicus].
ACCESSION   NP_071587 XP_578082
VERSION     NP_071587.2
DBSOURCE    REFSEQ: accession NM_022251.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Berillo,O., Ouerd,S., Idris-Khodja,N., Rehman,A., Richer,C.,
            Sinnett,D., Kwitek,A.E., Paradis,P. and Schiffrin,E.L.
  TITLE     Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive Rats and
            RNA Sequencing Identified Enpep and Hs2st1 as Vascular Inflammatory
            Modulators
  JOURNAL   Hypertension 77 (1), 178-189 (2021)
   PUBMED   33161775
  REMARK    GeneRIF: Chromosome 2 Fragment Substitutions in Dahl Salt-Sensitive
            Rats and RNA Sequencing Identified Enpep and Hs2st1 as Vascular
            Inflammatory Modulators.
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Wangensteen,R., Segarra,A.B., Ramirez-Sanchez,M., Gasparo,M.D.,
            Dominguez,G., Banegas,I., Vargas,F., Vives,F. and Prieto,I.
  TITLE     Influence of thyroid disorders on the kidney expression and plasma
            activity of aminopeptidase A
  JOURNAL   Endocr Regul 49 (2), 68-72 (2015)
   PUBMED   25960007
  REMARK    GeneRIF: A discrepancy between the high expression of AP-A in
            kidney of hyperthyroid rats and the low activity of AP-A measured
            in plasma and kidney of hyperthyroid animals was found.
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Yang,Y., Liu,C., Lin,Y.L. and Li,F.
  TITLE     Structural insights into central hypertension regulation by human
            aminopeptidase A
  JOURNAL   J Biol Chem 288 (35), 25638-25645 (2013)
   PUBMED   23888046
REFERENCE   4  (residues 1 to 945)
  AUTHORS   Ishii,M., Hattori,A., Numaguchi,Y., Ma,X., Nagasaka,T.,
            Tsujimoto,M., Murohara,T., Kobayashi,H. and Mizutani,S.
  TITLE     The effect of recombinant aminopeptidase A (APA) on hypertension in
            pregnant spontaneously hypertensive rats (SHRs)
  JOURNAL   Early Hum Dev 85 (9), 589-594 (2009)
   PUBMED   19608358
REFERENCE   5  (residues 1 to 945)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 945)
  AUTHORS   Troyanovskaya,M., Song,L., Jayaraman,G. and Healy,D.P.
  TITLE     Expression of aminopeptidase A, an angiotensinase, in glomerular
            mesangial cells
  JOURNAL   Hypertension 27 (3 Pt 2), 518-522 (1996)
   PUBMED   8613196
REFERENCE   7  (residues 1 to 945)
  AUTHORS   Wenger,R.H., Kopf,M., Nitschke,L., Lamers,M.C., Kohler,G. and
            Nielsen,P.J.
  TITLE     B-cell maturation in chimaeric mice deficient for the heat stable
            antigen (HSA/mouse CD24)
  JOURNAL   Transgenic Res 4 (3), 173-183 (1995)
   PUBMED   7795661
REFERENCE   8  (residues 1 to 945)
  AUTHORS   Song,L., Ye,M., Troyanovskaya,M., Wilk,E., Wilk,S. and Healy,D.P.
  TITLE     Rat kidney glutamyl aminopeptidase (aminopeptidase A): molecular
            identity and cellular localization
  JOURNAL   Am J Physiol 267 (4 Pt 2), F546-F557 (1994)
   PUBMED   7943354
REFERENCE   9  (residues 1 to 945)
  AUTHORS   Li,L., Wang,J. and Cooper,M.D.
  TITLE     cDNA cloning and expression of human glutamyl aminopeptidase
            (aminopeptidase A)
  JOURNAL   Genomics 17 (3), 657-664 (1993)
   PUBMED   8244382
REFERENCE   10 (residues 1 to 945)
  AUTHORS   Nanus,D.M., Engelstein,D., Gastl,G.A., Gluck,L., Vidal,M.J.,
            Morrison,M., Finstad,C.L., Bander,N.H. and Albino,A.P.
  TITLE     Molecular cloning of the human kidney differentiation antigen
            gp160: human aminopeptidase A
  JOURNAL   Proc Natl Acad Sci U S A 90 (15), 7069-7073 (1993)
   PUBMED   8346219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF146044.1, CK481363.1, BC066663.1, CB747518.1 and AF214568.1.
            
            On Apr 5, 2007 this sequence version replaced NP_071587.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF214568.1, BC066663.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..945
                     /product="glutamyl aminopeptidase"
                     /EC_number="3.4.11.7"
                     /note="EAP; AP-A; aminopeptidase A"
                     /calculated_mol_wt=107866
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50123.2)"
     Region          45..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50123.2)"
     Region          92..531
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            order(213,215,349..352,385..386,389,408,412,466,471)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Site            213
                     /site_type="other"
                     /note="Binds calcium which modulates its enzyme activity.
                     /evidence=ECO:0000250|UniProtKB:Q07075; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            471
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q07075; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            584
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            601
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Region          607..925
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
     Site            640
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            669
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            754
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     Site            792
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50123.2)"
     CDS             1..945
                     /gene="Enpep"
                     /coded_by="NM_022251.2:422..3259"
                     /db_xref="GeneID:64017"
                     /db_xref="RGD:621228"
ORIGIN      
        1 mnfaeeepsk kycikgkhva iicatvvavg livglsvglt rscepgttpa psnppphtst
       61 alppqdqnvc pdsddesgew knfrlpdfiq pvhydlevkv lmeedrytgi vsisvnlskd
      121 trdlwlhire tritklpelr rpsgeqvpir rcfeykkqey vviqaeedla atsgdsvyrl
      181 tiefegwlng slvgfyrtty tedgqtksia atdheptdar ksfpcfdepn kkatynisli
      241 hpkeysalsn mpvekeetld ndwkkttfmk svpmstylvc favhqftsiq rtsrsgkplt
      301 vyvqpnqkqt aeyaanitka vfdffedyfa meyslpkldk iaipdfgtga menwglvtyr
      361 etnllydpll sassnqqrva svvahelvhq wfgnivtmdw wddlwlnegf asffeflgvn
      421 haeadwqmls qvlledvlpv qeddslmssh pvvvtvstpa eitsvfdgis yskgasilrm
      481 lqdwitpekf qkgcqiylen fkfknaktsd fwdslekasn qpvkevmdtw tsqmgypvvt
      541 vsgkqnvtqk rflldykadp sqppsalgyt wnipikwten gnsnitvyyr snregitlna
      601 nlsgdgflki npdhigfyrv nyeaetwdwi aetlssnhmn fssadrssfi ddafalaraq
      661 lldyekalnl tryltsekdf lpwervisav syiismfedd relypliety frsqvkpiad
      721 slgwqdtgsh itkllrasvl gfackmgage algnasqlfe awlkgnesip vnlrllvyry
      781 gmqnsgneaa wnytleqyqk tslaqekekl lyglasvkdv tllaryleml kdpniiktqd
      841 vftviryisy nsygksmawn wiqlnwdylv nrftindryl grivtiaepf ntelqlwqmq
      901 sffakypnag agakpreqvl etvknniewl klnrksisew ftsmp
//
LOCUS       NP_001013236             211 aa            linear   ROD 27-APR-2025
DEFINITION  receptor expression-enhancing protein 6 [Rattus norvegicus].
ACCESSION   NP_001013236 XP_343164
VERSION     NP_001013236.1
DBSOURCE    REFSEQ: accession NM_001013218.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Sun,Y., Chen,L., Xu,T., Gou,B., Mai,J.W., Luo,D.X., Xin,W.J. and
            Wu,J.Y.
  TITLE     MiR-672-5p-Mediated Upregulation of REEP6 in Spinal Dorsal Horn
            Participates in Bortezomib-Induced Neuropathic Pain in Rats
  JOURNAL   Neurochem Res 48 (1), 229-237 (2023)
   PUBMED   36064821
  REMARK    GeneRIF: MiR-672-5p-Mediated Upregulation of REEP6 in Spinal Dorsal
            Horn Participates in Bortezomib-Induced Neuropathic Pain in Rats.
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Arno,G., Agrawal,S.A., Eblimit,A., Bellingham,J., Xu,M., Wang,F.,
            Chakarova,C., Parfitt,D.A., Lane,A., Burgoyne,T., Hull,S.,
            Carss,K.J., Fiorentino,A., Hayes,M.J., Munro,P.M., Nicols,R.,
            Pontikos,N., Holder,G.E., Asomugha,C., Raymond,F.L., Moore,A.T.,
            Plagnol,V., Michaelides,M., Hardcastle,A.J., Li,Y., Cukras,C.,
            Webster,A.R., Cheetham,M.E. and Chen,R.
  CONSRTM   UKIRDC
  TITLE     Mutations in REEP6 Cause Autosomal-Recessive Retinitis Pigmentosa
  JOURNAL   Am J Hum Genet 99 (6), 1305-1315 (2016)
   PUBMED   27889058
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Hao,H., Veleri,S., Sun,B., Kim,D.S., Keeley,P.W., Kim,J.W.,
            Yang,H.J., Yadav,S.P., Manjunath,S.H., Sood,R., Liu,P., Reese,B.E.
            and Swaroop,A.
  TITLE     Regulation of a novel isoform of Receptor Expression Enhancing
            Protein REEP6 in rod photoreceptors by bZIP transcription factor
            NRL
  JOURNAL   Hum Mol Genet 23 (16), 4260-4271 (2014)
   PUBMED   24691551
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Bjork,S., Hurt,C.M., Ho,V.K. and Angelotti,T.
  TITLE     REEPs are membrane shaping adapter proteins that modulate specific
            g protein-coupled receptor trafficking by affecting ER cargo
            capacity
  JOURNAL   PLoS One 8 (10), e76366 (2013)
   PUBMED   24098485
  REMARK    Erratum:[PLoS One. 2013;8(12).
            doi:10.1371/annotation/6f86410c-63c3-4fcd-b1cb-9fd8d2ea95d0]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Krolewski,R.C., Packard,A., Jang,W., Wildner,H. and Schwob,J.E.
  TITLE     Ascl1 (Mash1) knockout perturbs differentiation of nonneuronal
            cells in olfactory epithelium
  JOURNAL   PLoS One 7 (12), e51737 (2012)
   PUBMED   23284756
REFERENCE   6  (residues 1 to 211)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Sato,H., Tomita,H., Nakazawa,T., Wakana,S. and Tamai,M.
  TITLE     Deleted in polyposis 1-like 1 gene (Dp1l1): a novel gene richly
            expressed in retinal ganglion cells
  JOURNAL   Invest Ophthalmol Vis Sci 46 (3), 791-796 (2005)
   PUBMED   15728532
  REMARK    GeneRIF: TB2-like 1 is a membrane protein that belongs to the
            YOP1/TB2/DP1/HVA22 family, and it probably plays an important role
            in intracellular membrane trafficking in RGCs
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083830.1.
            
            On Apr 20, 2005 this sequence version replaced XP_343164.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083830.1, CK469420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..211
                     /product="receptor expression-enhancing protein 6"
                     /note="polyposis locus protein 1-like 1; deleted in
                     polyposis 1-like 1"
                     /calculated_mol_wt=23182
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI60.1)"
     Region          66..143
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI60.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI60.1)"
     Region          188..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI60.1)"
     CDS             1..211
                     /gene="Reep6"
                     /gene_synonym="Dp1l1"
                     /coded_by="NM_001013218.1:28..663"
                     /db_xref="GeneID:362835"
                     /db_xref="RGD:1309508"
ORIGIN      
        1 mdglrqrfer fleqknvatd algaleartg vekrylaaga ltllglyllf gygasllcnv
       61 igfvypayas vkaiespnke ddtvwltywv vyalfglvef fsdlllfwfp fyyagkcafl
      121 lfcmtpgpwn galllyhrvi rplflkhhva ldsaasqlsg raldiaagit rdvlqalarg
      181 rtlvtpasas espaalepdp kssqttllkh k
//
LOCUS       NP_001020226             542 aa            linear   ROD 27-APR-2025
DEFINITION  NXPE family member 4 precursor [Rattus norvegicus].
ACCESSION   NP_001020226 XP_576405
VERSION     NP_001020226.1
DBSOURCE    REFSEQ: accession NM_001025055.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083798.1.
            
            On Jun 25, 2005 this sequence version replaced XP_576405.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083798.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..542
                     /product="NXPE family member 4 precursor"
                     /note="protein FAM55D; NXPE family member 4; family with
                     sequence similarity 55, member B"
                     /calculated_mol_wt=58439
     sig_peptide     1..26
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI89.1)"
                     /calculated_mol_wt=3195
     mat_peptide     27..542
                     /product="NXPE family member 4. /id=PRO_0000019555"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI89.1)"
                     /calculated_mol_wt=58439
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI89.1)"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI89.1)"
     Region          <127..255
                     /region_name="Neurexophilin"
                     /note="pfam06312"
                     /db_xref="CDD:428882"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI89.1)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI89.1)"
     CDS             1..542
                     /gene="Nxpe4"
                     /gene_synonym="Fam55b; Fam55d"
                     /coded_by="NM_001025055.1:384..2012"
                     /db_xref="GeneID:500991"
                     /db_xref="RGD:1560781"
ORIGIN      
        1 mkmmasrksl wvllfivifw isftvfrnpv klwavfklpa sfnqwdlimk sscpkvplnp
       61 svsptetelr ireileklnk qipprpfahl nnttsathsi atilnpqdty cvgdqldilv
      121 eardhlrnrk gyggdflrar msspalkaga sgkvtdfnng tylvsftlfw egqvslsill
      181 mhpsegvsal wrarnqgydr iifsghfvsg asqvhtdcal vlnssvelcq yldaqdqeaf
      241 ycvkppnvpc aaithmhskn kdisylsqqe rslfersnia veimgksnvi svskcnkavp
      301 vkkkckfgma saiptghvwk ntwnpascsl apikmkdclr gklvhlmgds tmrqwmeyfk
      361 skintlrpvd lhetgrlqhq lavdldekin iqwqkhgfpl igslvysvke ientariidr
      421 iggekntviv fslgqhfrpf pidvfirral svhralqrll lrspdtlvvl ktentrelnn
      481 dmerfsdfhg ytqylalkni fqdlrvgvid awdmtvaygt ndvhppeevv rseiniflny
      541 ic
//
LOCUS       NP_001014091             389 aa            linear   ROD 27-APR-2025
DEFINITION  smad nuclear interacting protein 1 [Rattus norvegicus].
ACCESSION   NP_001014091 XP_233518
VERSION     NP_001014091.1
DBSOURCE    REFSEQ: accession NM_001014069.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Yu,B., Bi,L., Zheng,B., Ji,L., Chevalier,D., Agarwal,M.,
            Ramachandran,V., Li,W., Lagrange,T., Walker,J.C. and Chen,X.
  TITLE     The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans
            act in small RNA biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (29), 10073-10078 (2008)
   PUBMED   18632581
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Kim,R.H., Flanders,K.C., Birkey Reffey,S., Anderson,L.A.,
            Duckett,C.S., Perkins,N.D. and Roberts,A.B.
  TITLE     SNIP1 inhibits NF-kappa B signaling by competing for its binding to
            the C/H1 domain of CBP/p300 transcriptional co-activators
  JOURNAL   J Biol Chem 276 (49), 46297-46304 (2001)
   PUBMED   11567019
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Kim,R.H., Wang,D., Tsang,M., Martin,J., Huff,C., de
            Caestecker,M.P., Parks,W.T., Meng,X., Lechleider,R.J., Wang,T. and
            Roberts,A.B.
  TITLE     A novel smad nuclear interacting protein, SNIP1, suppresses
            p300-dependent TGF-beta signal transduction
  JOURNAL   Genes Dev 14 (13), 1605-1616 (2000)
   PUBMED   10887155
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087118.1.
            
            On Apr 20, 2005 this sequence version replaced XP_233518.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087118.1, SRR8487231.77247.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..389
                     /product="smad nuclear interacting protein 1"
                     /calculated_mol_wt=44792
     Region          1..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Region          2..>199
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TAD8; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Region          215..363
                     /region_name="FHA_SNIP1"
                     /note="forkhead associated (FHA) domain found in Smad
                     nuclear-interacting protein 1 (SNIP1) and similar
                     proteins; cd22718"
                     /db_xref="CDD:438770"
     Site            order(223,252..254,287)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438770"
     Site            order(275..277,291..292,294,324,326..327)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438770"
     Region          363..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G6.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TAD8; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G6.1)"
     CDS             1..389
                     /gene="Snip1"
                     /coded_by="NM_001014069.1:34..1203"
                     /db_xref="GeneID:313588"
                     /db_xref="RGD:1359268"
ORIGIN      
        1 mkagkserer ssrrrhrsgd alatvvvkqe rlspepvahr rpdapaaspp ppaaesgsag
       61 hrgsrargas rspakkksks sgrrsksprt krsrsphyst vkvkqeredh prrgredrqh
      121 relseqehrr arnserdrhr gharqrrssd erpvsgqgrd rdsqilqaqe eerdfnnarr
      181 rehrqqnesa gaeaqevipr pagnknkevp vkekpsfels galledtntf rgvvikysep
      241 pearipkkrw rlypfkndev lpvmyihrqs ayllgrhrri adipidhpsc skqhavfqyr
      301 lveytradgt vgrrvkpyii dlgsgngtfl nnkriepqry yelkekdvlk fgfssreyvl
      361 lhessdtsel drkededeee eeemvsdss
//
LOCUS       NP_620190                421 aa            linear   ROD 27-APR-2025
DEFINITION  synaptotagmin-12 [Rattus norvegicus].
ACCESSION   NP_620190
VERSION     NP_620190.1
DBSOURCE    REFSEQ: accession NM_138835.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Kaeser-Woo,Y.J., Younts,T.J., Yang,X., Zhou,P., Wu,D.,
            Castillo,P.E. and Sudhof,T.C.
  TITLE     Synaptotagmin-12 phosphorylation by cAMP-dependent protein kinase
            is essential for hippocampal mossy fiber LTP
  JOURNAL   J Neurosci 33 (23), 9769-9780 (2013)
   PUBMED   23739973
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Maximov,A., Shin,O.H., Liu,X. and Sudhof,T.C.
  TITLE     Synaptotagmin-12, a synaptic vesicle phosphoprotein that modulates
            spontaneous neurotransmitter release
  JOURNAL   J Cell Biol 176 (1), 113-124 (2007)
   PUBMED   17190793
  REMARK    GeneRIF: These data suggest that spontaneous synaptic-vesicle
            exocytosis is selectively modulated by a Ca(2+)-independent
            synaptotagmin isoform, synaptotagmin-12, which is controlled by
            cyclic AMP-dependent phosphorylation.
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Thompson,C.C.
  TITLE     Thyroid hormone-responsive genes in developing cerebellum include a
            novel synaptotagmin and a hairless homolog
  JOURNAL   J Neurosci 16 (24), 7832-7840 (1996)
   PUBMED   8987811
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U71294.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U71294.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132264 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..421
                     /product="synaptotagmin-12"
                     /note="sytXII; synaptotagmin-related gene 1 protein;
                     synaptotagmin XII"
                     /calculated_mol_wt=46477
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97610.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:17190793,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97610.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97610.1)"
     Region          152..263
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97610.1)"
     Region          284..419
                     /region_name="C2B_Synaptotagmin-12"
                     /note="C2 domain second repeat present in Synaptotagmin
                     12; cd08406"
                     /db_xref="CDD:176051"
     CDS             1..421
                     /gene="Syt12"
                     /gene_synonym="Srg1"
                     /coded_by="NM_138835.1:221..1486"
                     /db_xref="GeneID:191595"
                     /db_xref="RGD:621876"
ORIGIN      
        1 mavdvteyhl sviksppgwe vgvyaagala llgiaavslw klwtsgsfps pspfpnydyr
       61 ylqqkygeay veaklkrvpp wnaqrtttrg ppsrkgslsi edtfesisel gplelmgrel
      121 dlapygtlrk sqsadslnsi ssvsntfgqd ftlgqvevsm dydgashtlh vavlqgkdll
      181 ereeatfesc fmrvsllpde qivgisriqr naysiffdek fsvpldptal eekslrfsvf
      241 gidedernvs tgvvelklsv ldlplqpfsg wlylqdqnka adavgeills lsylptaerl
      301 tvvvvkaknl iwtndkttad pfvkvyllqd grkmskkkta vkrddpnpvf neamifsvpa
      361 ivlqdlslrv tvaesssdgr gdnvghviig pgasgmgtth wnqmlatlrr pvsmwhpvrr
      421 n
//
LOCUS       NP_001102089             548 aa            linear   ROD 27-APR-2025
DEFINITION  inosine-5'-monophosphate dehydrogenase 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102089 XP_001063757 XP_342651
VERSION     NP_001102089.1
DBSOURCE    REFSEQ: accession NM_001108619.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Tam,L.C., Kiang,A.S., Kennan,A., Kenna,P.F., Chadderton,N.,
            Ader,M., Palfi,A., Aherne,A., Ayuso,C., Campbell,M., Reynolds,A.,
            McKee,A., Humphries,M.M., Farrar,G.J. and Humphries,P.
  TITLE     Therapeutic benefit derived from RNAi-mediated ablation of IMPDH1
            transcripts in a murine model of autosomal dominant retinitis
            pigmentosa (RP10)
  JOURNAL   Hum Mol Genet 17 (14), 2084-2100 (2008)
   PUBMED   18385099
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Watanabe,M., Yamamoto,T., Kakuhata,R., Okada,N., Kajimoto,K.,
            Yamazaki,N., Kataoka,M., Baba,Y., Tamaki,T. and Shinohara,Y.
  TITLE     Synchronized changes in transcript levels of genes activating cold
            exposure-induced thermogenesis in brown adipose tissue of
            experimental animals
  JOURNAL   Biochim Biophys Acta 1777 (1), 104-112 (2008)
   PUBMED   18036333
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Gunter,J.H., Thomas,E.C., Lengefeld,N., Kruger,S.J., Worton,L.,
            Gardiner,E.M., Jones,A., Barnett,N.L. and Whitehead,J.P.
  TITLE     Characterisation of inosine monophosphate dehydrogenase expression
            during retinal development: differences between variants and
            isoforms
  JOURNAL   Int J Biochem Cell Biol 40 (9), 1716-1728 (2008)
   PUBMED   18295529
REFERENCE   4  (residues 1 to 548)
  AUTHORS   McLean,J.E., Hamaguchi,N., Belenky,P., Mortimer,S.E., Stanton,M.
            and Hedstrom,L.
  TITLE     Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro
            and in vivo
  JOURNAL   Biochem J 379 (Pt 2), 243-251 (2004)
   PUBMED   14766016
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Aherne,A., Kennan,A., Kenna,P.F., McNally,N., Lloyd,D.G.,
            Alberts,I.L., Kiang,A.S., Humphries,M.M., Ayuso,C., Engel,P.C.,
            Gu,J.J., Mitchell,B.S., Farrar,G.J. and Humphries,P.
  TITLE     On the molecular pathology of neurodegeneration in IMPDH1-based
            retinitis pigmentosa
  JOURNAL   Hum Mol Genet 13 (6), 641-650 (2004)
   PUBMED   14981049
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Gu,J.J., Tolin,A.K., Jain,J., Huang,H., Santiago,L. and
            Mitchell,B.S.
  TITLE     Targeted disruption of the inosine 5'-monophosphate dehydrogenase
            type I gene in mice
  JOURNAL   Mol Cell Biol 23 (18), 6702-6712 (2003)
   PUBMED   12944494
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Bowne,S.J., Sullivan,L.S., Blanton,S.H., Cepko,C.L., Blackshaw,S.,
            Birch,D.G., Hughbanks-Wheaton,D., Heckenlively,J.R. and Daiger,S.P.
  TITLE     Mutations in the inosine monophosphate dehydrogenase 1 gene
            (IMPDH1) cause the RP10 form of autosomal dominant retinitis
            pigmentosa
  JOURNAL   Hum Mol Genet 11 (5), 559-568 (2002)
   PUBMED   11875050
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Kennan,A., Aherne,A., Palfi,A., Humphries,M., McKee,A., Stitt,A.,
            Simpson,D.A., Demtroder,K., Orntoft,T., Ayuso,C., Kenna,P.F.,
            Farrar,G.J. and Humphries,P.
  TITLE     Identification of an IMPDH1 mutation in autosomal dominant
            retinitis pigmentosa (RP10) revealed following comparative
            microarray analysis of transcripts derived from retinas of
            wild-type and Rho(-/-) mice
  JOURNAL   Hum Mol Genet 11 (5), 547-557 (2002)
   PUBMED   11875049
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Hager,P.W., Collart,F.R., Huberman,E. and Mitchell,B.S.
  TITLE     Recombinant human inosine monophosphate dehydrogenase type I and
            type II proteins. Purification and characterization of inhibitor
            binding
  JOURNAL   Biochem Pharmacol 49 (9), 1323-1329 (1995)
   PUBMED   7763314
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473959.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342651.3, XP_001063757.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..548
                     /product="inosine-5'-monophosphate dehydrogenase 1 isoform
                     1"
                     /EC_number="1.1.1.205"
                     /note="inosine 5'-phosphate dehydrogenase 1; IMP (inosine
                     monophosphate) dehydrogenase 1; IMP dehydrogenase 1; IMP
                     (inosine 5'-monophosphate) dehydrogenase 1;
                     inosine-5'-monophosphate dehydrogenase 1"
                     /calculated_mol_wt=58478
     Region          71..544
                     /region_name="PTZ00314"
                     /note="inosine-5'-monophosphate dehydrogenase;
                     Provisional"
                     /db_xref="CDD:240355"
     CDS             1..548
                     /gene="Impdh1"
                     /gene_synonym="IMPD 1; IMPDH 1"
                     /coded_by="NM_001108619.1:37..1683"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362329"
                     /db_xref="RGD:1311108"
ORIGIN      
        1 meeplspppe sgllspllqg ggaaaapepg arqhpgheta aqrysarllq agyepesmad
       61 ylisggtgyv pedgltaqql fanadgltyn dflilpgfid fiadevdlts altrkitlkt
      121 plisspmdtv teadmaiama lmggigfihh nctpefqane vrkvkkfeqg fitdpvvlsp
      181 shtvgdvlea kiqhgfsgip itatgtmgsk lvmtprielv vapagvtlke aneilqrskk
      241 gklpivndqd elvaiiartd lkknrdypla skdshkqllc gaavgtredd kyrldlltqa
      301 gadvivldss qgnsvyqiam vhyikqkyph lqviggnvvt aaqaknlida gvdglrvgmg
      361 cgsicitqev macgrpqgta vykvaeyarr fgvpviadgg iqtvghvvka lalgastvmm
      421 gsllaattea pgeyffsdgv rlkkyrgmgs ldamekssss qkryfsegdk vkiaqgvsgs
      481 iqdkgsiqkf vpyliagiqh gcqdigaqsl svlrsmmysg elkfekrtms aqieggvhgl
      541 hsyekrly
//
LOCUS       NP_001029073             866 aa            linear   ROD 27-APR-2025
DEFINITION  speckle targeted PIP5K1A-regulated poly(A) polymerase [Rattus
            norvegicus].
ACCESSION   NP_001029073 XP_574615
VERSION     NP_001029073.1
DBSOURCE    REFSEQ: accession NM_001033901.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Sudheesh,A.P., Mohan,N., Francis,N., Laishram,R.S. and
            Anderson,R.A.
  TITLE     Star-PAP controlled alternative polyadenylation coupled poly(A)
            tail length regulates protein expression in hypertrophic heart
  JOURNAL   Nucleic Acids Res 47 (20), 10771-10787 (2019)
   PUBMED   31598705
  REMARK    GeneRIF: The loss of NQO1 during hypertrophy was rescued by ectopic
            expression of the distal- but not the proximal- or middle-specific
            NQO1 mRNA isoforms in the presence of Star-PAP expression, and
            reverses molecular events of hypertrophy in cardiomyocytes.
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Yamashita,S., Takagi,Y., Nagaike,T. and Tomita,K.
  TITLE     Crystal structures of U6 snRNA-specific terminal
            uridylyltransferase
  JOURNAL   Nat Commun 8, 15788 (2017)
   PUBMED   28589955
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Laishram,R.S. and Anderson,R.A.
  TITLE     The poly A polymerase Star-PAP controls 3'-end cleavage by
            promoting CPSF interaction and specificity toward the pre-mRNA
  JOURNAL   EMBO J 29 (24), 4132-4145 (2010)
   PUBMED   21102410
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Gonzales,M.L., Mellman,D.L. and Anderson,R.A.
  TITLE     CKIalpha is associated with and phosphorylates star-PAP and is also
            required for expression of select star-PAP target messenger RNAs
  JOURNAL   J Biol Chem 283 (18), 12665-12673 (2008)
   PUBMED   18305108
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Mellman,D.L., Gonzales,M.L., Song,C., Barlow,C.A., Wang,P.,
            Kendziorski,C. and Anderson,R.A.
  TITLE     A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls
            expression of select mRNAs
  JOURNAL   Nature 451 (7181), 1013-1017 (2008)
   PUBMED   18288197
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Mullen,T.E. and Marzluff,W.F.
  TITLE     Degradation of histone mRNA requires oligouridylation followed by
            decapping and simultaneous degradation of the mRNA both 5' to 3'
            and 3' to 5'
  JOURNAL   Genes Dev 22 (1), 50-65 (2008)
   PUBMED   18172165
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Trippe,R., Guschina,E., Hossbach,M., Urlaub,H., Luhrmann,R. and
            Benecke,B.J.
  TITLE     Identification, cloning, and functional analysis of the human U6
            snRNA-specific terminal uridylyl transferase
  JOURNAL   RNA 12 (8), 1494-1504 (2006)
   PUBMED   16790842
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC104695.1.
            
            On Sep 30, 2005 this sequence version replaced XP_574615.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC104695.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..866
                     /product="speckle targeted PIP5K1A-regulated poly(A)
                     polymerase"
                     /EC_number="2.7.7.19"
                     /EC_number="2.7.7.52"
                     /note="U6 snRNA-specific terminal uridylyltransferase 1;
                     U6-TUTase; RNA-binding protein 21; RNA-binding motif
                     protein 21; star-PAP"
                     /calculated_mol_wt=94247
     Region          16..40
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          54..127
                     /region_name="RRM_TUT1"
                     /note="RNA recognition motif (RRM) found in speckle
                     targeted PIP5K1A-regulated poly(A) polymerase (Star-PAP)
                     and similar proteins; cd12279"
                     /db_xref="CDD:409721"
     Region          116..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          223..249
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          267..321
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          <331..401
                     /region_name="NT_PAP_TUTase"
                     /note="Nucleotidyltransferase (NT) domain of poly(A)
                     polymerases and terminal uridylyl transferases; cd05402"
                     /db_xref="CDD:143392"
     Region          <358..>566
                     /region_name="TRF4"
                     /note="DNA polymerase sigma [Replication, recombination
                     and repair]; COG5260"
                     /db_xref="CDD:227585"
     Site            order(366,369,371,382,389..390)
                     /site_type="active"
                     /note="putative primer-binding pocket [active]"
                     /db_xref="CDD:143392"
     Region          599..866
                     /region_name="KA1, binds the bulging loops of U6 snRNA but
                     is dispensable for terminal uridylyltransferase activity.
                     /evidence=ECO:0000250|UniProtKB:Q9H6E5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          638..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3F9; propagated from
                     UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          728..755
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MHT4.1)"
     Region          773..792
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHT4.1)"
     CDS             1..866
                     /gene="Tut1"
                     /coded_by="NM_001033901.1:13..2613"
                     /db_xref="GeneID:499314"
                     /db_xref="RGD:1561043"
ORIGIN      
        1 maavdsdvvs lprgrfrccl cdvttanrps ldahlkgrkh rdlvqlratr kaqglrsvfv
       61 sgfprdvgsa qlseyfqtfg pvanivmdkd kgvfaivemg disareavls qpkhslgght
      121 lrvrpreqke fqspaskspk gvdsnshqla qalaeaadvg aqmvklvelr elseaerqlr
      181 tlvvalmqev fteffpgcvv hpfgssvnsf dvhgcdldlf ldlgdmeepq pdpqtpklpe
      241 assldstlas sldpqvlact pasldslspt slqdsealdf etpsslapqt pdsalgsdtv
      301 tspqslppvs pleedrgegk hrkelelaea skdekeeata vlelvgsilr gcvpgvyrvq
      361 tvpsarrpvv kfchrpsglh gdislsnrla lynsrflnlc semdsrvrpl vytlrcwaqh
      421 nglsgggpll nnyaltllvi yflqtrdppv lptvaqltqr sgegeqvevd gwdcsfpkda
      481 srlepstnve plssllaqff scvscwdlsg sllslregqa lmvagglpsd lweglrlgpm
      541 nlqdpfdlsh nvaanvtsrv akrlqsscga aasycrslqy qqrssrgrdw gllpllqpss
      601 pssllsakli plpsapfpqi italvsvlre algchieqgt krrrsegars kdsplggank
      661 rprlsgqeks ceegkeepqg cagdhsenev eemvielret pqdwallhcg ppgelplmta
      721 kcldktaeqn pmepegageg spgetekeas hpssvswrca lwhqiwqgrr rarrrfqqqt
      781 keegrggpst gaewlavear vtqelkgpks eqqrlqgepl ltfvasasqa eqtltvaplq
      841 dpqglfpglh hflqvfipqa lknllk
//
LOCUS       NP_001100806             444 aa            linear   ROD 27-APR-2025
DEFINITION  docking protein 3 [Rattus norvegicus].
ACCESSION   NP_001100806 XP_001069255 XP_225170
VERSION     NP_001100806.1
DBSOURCE    REFSEQ: accession NM_001107336.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kang,B.W., Jeon,H.S., Chae,Y.S., Lee,S.J., Park,J.S., Choi,G.S. and
            Kim,J.G.
  TITLE     Impact of Genetic Variation in MicroRNA-binding Site on
            Susceptibility to Colorectal Cancer
  JOURNAL   Anticancer Res 36 (7), 3353-3361 (2016)
   PUBMED   27354594
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Berger,A.H., Niki,M., Morotti,A., Taylor,B.S., Socci,N.D.,
            Viale,A., Brennan,C., Szoke,J., Motoi,N., Rothman,P.B.,
            Teruya-Feldstein,J., Gerald,W.L., Ladanyi,M. and Pandolfi,P.P.
  TITLE     Identification of DOK genes as lung tumor suppressors
  JOURNAL   Nat Genet 42 (3), 216-223 (2010)
   PUBMED   20139980
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Cong,F., Yuan,B. and Goff,S.P.
  TITLE     Characterization of a novel member of the DOK family that binds and
            modulates Abl signaling
  JOURNAL   Mol Cell Biol 19 (12), 8314-8325 (1999)
   PUBMED   10567556
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474032.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225170.3, XP_001069255.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166772.1, FQ235097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132301, SAMD00132307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..444
                     /product="docking protein 3"
                     /note="downstream of tyrosine kinase 3"
                     /calculated_mol_wt=48059
     Region          9..123
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          47..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RYG7.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L591; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     Region          157..255
                     /region_name="PTB_DOK1_DOK2_DOK3"
                     /note="Downstream of tyrosine kinase 1, 2, and 3 proteins
                     phosphotyrosine-binding domain (PTBi); cd01203"
                     /db_xref="CDD:269914"
     Site            order(167,173)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269914"
     Site            order(205..213,219,223..224,244,251,254)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:269914"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK7; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK7; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK7; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     Region          354..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RYG7.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZK7; propagated from
                     UniProtKB/Swiss-Prot (B2RYG7.1)"
     CDS             1..444
                     /gene="Dok3"
                     /coded_by="NM_001107336.1:25..1359"
                     /db_xref="GeneID:306760"
                     /db_xref="RGD:1311840"
ORIGIN      
        1 mesvetpvkd gllyqqhmkf gkkcwrkvwa llyaggpsgv arleswdvrd gglgpggdrp
       61 agpgrrgerr iirladcvsv lpadgescpr dtgaflittt ershllaaqh rqswmdpicq
      121 lafpstgecs sgsgqaespk rgfvpmeens iysswqevae fpvvvqrtea ttrcqlkgpy
      181 llvlgqddiq lretskpqac yswpyrflrk fgsdkgvfsf eagrrcdsge glfafsspra
      241 pdicgavaaa iarqrerlpe lamsppcplp ralslpslep pgelrevape yelapsrklp
      301 ltdpgpqslp lllsptqdgt asslyasvck qtskhkatve hlyenvfmle aspglsnggp
      361 eaqegppggr splgspiyhn seelswpgsa hdsnleaqyr rlleleldda ggagrpgaqt
      421 gikaklvtll trerkkgpap cdrp
//
LOCUS       NP_001013261             388 aa            linear   ROD 27-APR-2025
DEFINITION  probable proton-coupled zinc antiporter SLC30A3 [Rattus
            norvegicus].
ACCESSION   NP_001013261 XP_345643
VERSION     NP_001013261.1
DBSOURCE    REFSEQ: accession NM_001013243.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Nishida,K., Bansho,S., Ikukawa,A., Kubota,T., Ohishi,A. and
            Nagasawa,K.
  TITLE     Expression profile of the zinc transporter ZnT3 in taste cells of
            rat circumvallate papillae and its role in zinc release, a
            potential mechanism for taste stimulation
  JOURNAL   Eur J Histochem 66 (4), 3534 (2022)
   PUBMED   36373349
  REMARK    GeneRIF: Expression profile of the zinc transporter ZnT3 in taste
            cells of rat circumvallate papillae and its role in zinc release, a
            potential mechanism for taste stimulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Qin,W., Li,L., Wang,T., Huang,H. and Gao,Y.
  TITLE     Urine Proteome Changes in a TNBS-Induced Colitis Rat Model
  JOURNAL   Proteomics Clin Appl 13 (5), e1800100 (2019)
   PUBMED   31095872
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Ni,H., Chen,S.H., Li,L.L. and Jin,M.F.
  TITLE     Alterations in the Neurobehavioral Phenotype and ZnT3/CB-D28k
            Expression in the Cerebral Cortex Following
            Lithium-Pilocarpine-Induced Status Epilepticus: the Ameliorative
            Effect of Leptin
  JOURNAL   Biol Trace Elem Res 187 (1), 100-106 (2019)
   PUBMED   29687372
  REMARK    GeneRIF: The ZnT3/CB-D28k-associated Zn (2+)/Ca(2+) signaling might
            be involved in neonatal SE-induced long-term brain damage in the
            aspects of neurobehavioral impairment.
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hildebrand,M.S., Phillips,A.M., Mullen,S.A., Adlard,P.A.,
            Hardies,K., Damiano,J.A., Wimmer,V., Bellows,S.T., McMahon,J.M.,
            Burgess,R., Hendrickx,R., Weckhuysen,S., Suls,A., De Jonghe,P.,
            Scheffer,I.E., Petrou,S., Berkovic,S.F. and Reid,C.A.
  TITLE     Loss of synaptic Zn2+ transporter function increases risk of
            febrile seizures
  JOURNAL   Sci Rep 5, 17816 (2015)
   PUBMED   26647834
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Tian,T., Ni,H. and Sun,B.L.
  TITLE     Neurobehavioral Deficits in a Rat Model of Recurrent Neonatal
            Seizures Are Prevented by a Ketogenic Diet and Correlate with
            Hippocampal Zinc/Lipid Transporter Signals
  JOURNAL   Biol Trace Elem Res 167 (2), 251-258 (2015)
   PUBMED   25778834
  REMARK    GeneRIF: rats treated with KD (EXP2) showed a significant
            down-regulated expression of ZnT-3, MT-3, ApoE, clusterin, and
            ACAT-1 in hippocampus
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Salazar,G., Falcon-Perez,J.M., Harrison,R. and Faundez,V.
  TITLE     SLC30A3 (ZnT3) oligomerization by dityrosine bonds regulates its
            subcellular localization and metal transport capacity
  JOURNAL   PLoS One 4 (6), e5896 (2009)
   PUBMED   19521526
  REMARK    GeneRIF: SLC30A3 (ZnT3) oligomerization by dityrosine bonds
            regulates its subcellular localization and metal transport capacity
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Ni,H., Jiang,Y.W., Tao,L.Y., Jin,M.F. and Wu,X.R.
  TITLE     ZnT-1, ZnT-3, CaMK II, PRG-1 expressions in hippocampus following
            neonatal seizure-induced cognitive deficit in rats
  JOURNAL   Toxicol Lett 184 (3), 145-150 (2009)
   PUBMED   19059322
  REMARK    GeneRIF: ZnT-1, ZnT-3, CaMK II, PRG-1 expressions in hippocampus
            following neonatal seizure-induced cognitive deficit in rats.
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Salazar,G., Craige,B., Love,R., Kalman,D. and Faundez,V.
  TITLE     Vglut1 and ZnT3 co-targeting mechanisms regulate vesicular zinc
            stores in PC12 cells
  JOURNAL   J Cell Sci 118 (Pt 9), 1911-1921 (2005)
   PUBMED   15860731
  REMARK    GeneRIF: the coupling of zinc transporter 3 and Vglut1 transport
            mechanisms regulates neurotransmitter content in secretory vesicles
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Cole,T.B., Wenzel,H.J., Kafer,K.E., Schwartzkroin,P.A. and
            Palmiter,R.D.
  TITLE     Elimination of zinc from synaptic vesicles in the intact mouse
            brain by disruption of the ZnT3 gene
  JOURNAL   Proc Natl Acad Sci U S A 96 (4), 1716-1721 (1999)
   PUBMED   9990090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY538655.1.
            
            On Apr 20, 2005 this sequence version replaced XP_345643.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY538655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..388
                     /product="probable proton-coupled zinc antiporter SLC30A3"
                     /note="solute carrier family 30 protein; zinc transporter
                     3; znT-3; zinc transporter ZnT-3; solute carrier family 30
                     (zinc transporter), member 3"
                     /calculated_mol_wt=41767
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Region          50..370
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QIX3.1)"
     CDS             1..388
                     /gene="Slc30a3"
                     /gene_synonym="ZnT3"
                     /coded_by="NM_001013243.1:81..1247"
                     /db_xref="GeneID:366568"
                     /db_xref="RGD:1359689"
ORIGIN      
        1 mepspasggs ettrlvsprd rssaggglrl kslftepsep lpegpklegm afhhchknrv
       61 sqsglspera qarrqlyaac vvcfifmage vvggylahsl aimtdaahll adigsmmasl
      121 fslwlstrpa trtmtfgwhr setlgalasv vslwivtgil lylaflrllh sdyhieagam
      181 lltasiavca nmimafvlhq tgaphshgpr gaeyapleeg hghplslgnt svraafvhvl
      241 gdllqslgvl aasiliyfkp qykvadpist flfsicalgs taptlrdvll vlmegaprsv
      301 efepvrdtll svpgvrathd lhlwaltlty hvasahlaid stadpeaila eassrlysrf
      361 gfssctlqve kyrsemahcl rcreppka
//
LOCUS       NP_072169                127 aa            linear   ROD 27-APR-2025
DEFINITION  histone H2B type 1-A [Rattus norvegicus].
ACCESSION   NP_072169
VERSION     NP_072169.1
DBSOURCE    REFSEQ: accession NM_022643.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Mahadevan,I.A., Pentakota,S., Roy,R., Bhaduri,U. and Satyanarayana
            Rao,M.R.
  TITLE     TH2BS11ph histone mark is enriched in the unsynapsed axes of the XY
            body and predominantly associates with H3K4me3-containing genomic
            regions in mammalian spermatocytes
  JOURNAL   Epigenetics Chromatin 12 (1), 53 (2019)
   PUBMED   31493790
  REMARK    GeneRIF: TH2BS11ph is predominantly associated with H3K4me3
            positive genomic regions like gene promoters, etc. TH2BS11ph
            modification could act alone or in concert with other histone
            modifications to recruit the appropriate transcription or XY body
            recombination protein machinery at specific genomic loci.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Barral,S., Morozumi,Y., Tanaka,H., Montellier,E., Govin,J., de
            Dieuleveult,M., Charbonnier,G., Coute,Y., Puthier,D., Buchou,T.,
            Boussouar,F., Urahama,T., Fenaille,F., Curtet,S., Hery,P.,
            Fernandez-Nunez,N., Shiota,H., Gerard,M., Rousseaux,S.,
            Kurumizaka,H. and Khochbin,S.
  TITLE     Histone Variant H2A.L.2 Guides Transition Protein-Dependent
            Protamine Assembly in Male Germ Cells
  JOURNAL   Mol Cell 66 (1), 89-101 (2017)
   PUBMED   28366643
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Pentakota,S.K., Sandhya,S., P Sikarwar,A., Chandra,N. and
            Satyanarayana Rao,M.R.
  TITLE     Mapping post-translational modifications of mammalian testicular
            specific histone variant TH2B in tetraploid and haploid germ cells
            and their implications on the dynamics of nucleosome structure
  JOURNAL   J Proteome Res 13 (12), 5603-5617 (2014)
   PUBMED   25252820
  REMARK    GeneRIF: Testis specific histone TH2B undergoes multiple post
            translational amino acid modification, suggesting the possibility
            of chromatin regulation.
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Urahama,T., Horikoshi,N., Osakabe,A., Tachiwana,H. and
            Kurumizaka,H.
  TITLE     Structure of human nucleosome containing the testis-specific
            histone variant TSH2B
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 4), 444-449 (2014)
   PUBMED   24699735
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Shinagawa,T., Takagi,T., Tsukamoto,D., Tomaru,C., Huynh,L.M.,
            Sivaraman,P., Kumarevel,T., Inoue,K., Nakato,R., Katou,Y., Sado,T.,
            Takahashi,S., Ogura,A., Shirahige,K. and Ishii,S.
  TITLE     Histone variants enriched in oocytes enhance reprogramming to
            induced pluripotent stem cells
  JOURNAL   Cell Stem Cell 14 (2), 217-227 (2014)
   PUBMED   24506885
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Golebiowski,F. and Kasprzak,K.S.
  TITLE     Inhibition of core histones acetylation by carcinogenic nickel(II)
  JOURNAL   Mol Cell Biochem 279 (1-2), 133-139 (2005)
   PUBMED   16283522
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Walter,L., Klinga-Levan,K., Helou,K., Albig,W., Drabent,B.,
            Doenecke,D., Gunther,E. and Levan,G.
  TITLE     Chromosome mapping of rat histone genes H1fv, H1d, H1t, Th2a and
            Th2b
  JOURNAL   Cytogenet Cell Genet 75 (2-3), 136-139 (1996)
   PUBMED   9040779
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Huh,N.E., Hwang,I.W., Lim,K., You,K.H. and Chae,C.B.
  TITLE     Presence of a bi-directional S phase-specific transcription
            regulatory element in the promoter shared by testis-specific TH2A
            and TH2B histone genes
  JOURNAL   Nucleic Acids Res 19 (1), 93-98 (1991)
   PUBMED   2011515
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Hwang,I. and Chae,C.B.
  TITLE     S-phase-specific transcription regulatory elements are present in a
            replication-independent testis-specific H2B histone gene
  JOURNAL   Mol Cell Biol 9 (3), 1005-1013 (1989)
   PUBMED   2725487
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Kim,Y.J., Hwang,I., Tres,L.L., Kierszenbaum,A.L. and Chae,C.B.
  TITLE     Molecular cloning and differential expression of somatic and
            testis-specific H2B histone genes during rat spermatogenesis
  JOURNAL   Dev Biol 124 (1), 23-34 (1987)
   PUBMED   3666307
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M18046.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M18046.1, M18045.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..127
                     /product="histone H2B type 1-A"
                     /note="histone H2B, testis; testis-specific histone H2B;
                     testis-specific histone 2b; histone 1, H2ba; histone
                     cluster 1, H2ba; histone cluster 1 H2B family member a"
                     /calculated_mol_wt=14094
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00729.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylproline.
                     /evidence=ECO:0000250|UniProtKB:P23527; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522,
                     ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522,
                     ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            18
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            22
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16283522,
                     ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            25
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P33778; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Region          31..124
                     /region_name="HFD_H2B"
                     /note="histone-fold domain found in histone H2B and
                     similar proteins; cd22910"
                     /db_xref="CDD:467035"
     Site            order(32,34,37,39,41..43,45..47,50..57,59..60,63..64,
                     67..68,70..72,74..76,80,90..91,93,96..97,100,103..105,108,
                     111..113,115..116,119..120,123..124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            order(32..38,41..42,44,55..57,90)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467035"
     Site            order(36,40..42,44..45,48..50,55..57,61,97,101,110..111,
                     113..114,117..118,120..121,124)
                     /site_type="other"
                     /note="Hif1 binding site [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64475; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            48
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            59
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            order(63,66..67,69..70,73,78,81,84..86,94..95,98,102..103)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467035"
     Site            81
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            87
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            87
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            88
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            94
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q96A08; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            110
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62807; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     Site            118
                     /site_type="methylation"
                     /note="N6-methylated lysine, alternate.
                     /evidence=ECO:0000269|PubMed:19346237; propagated from
                     UniProtKB/Swiss-Prot (Q00729.2)"
     CDS             1..127
                     /gene="H2bc1"
                     /gene_synonym="Hist1h2ba; histone; Th2b"
                     /coded_by="NM_022643.1:42..425"
                     /db_xref="GeneID:24829"
                     /db_xref="RGD:3855"
ORIGIN      
        1 mpevsakgtt iskkgfkkav tktqkkegrk rkrcreesys iyiykvlkqv hpdtgisska
       61 msimnsfvtd iferiageas rlahynkrst itsreiqtav rlllpgelak havsegtkav
      121 tkytssk
//
LOCUS       NP_001007690             309 aa            linear   ROD 27-APR-2025
DEFINITION  anamorsin [Rattus norvegicus].
ACCESSION   NP_001007690 XP_226244
VERSION     NP_001007690.1
DBSOURCE    REFSEQ: accession NM_001007689.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Cai,X., Wang,S., Hong,L., Yu,S., Li,B., Zeng,H., Yang,X., Zhang,P.
            and Shao,L.
  TITLE     Inhibition of miR-322-5p Protects Cardiac Myoblast Cells Against
            Hypoxia-Induced Apoptosis and Injury Through Regulating CIAPIN1
  JOURNAL   J Cardiovasc Pharmacol 77 (2), 200-207 (2021)
   PUBMED   33538533
  REMARK    GeneRIF: Inhibition of miR-322-5p Protects Cardiac Myoblast Cells
            Against Hypoxia-Induced Apoptosis and Injury Through Regulating
            CIAPIN1.
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Zhang,H.J., Zhang,Y.N. and Teng,Z.Y.
  TITLE     Downregulation of miR-16 protects H9c2(2-1) cells against
            hypoxia/reoxygenation damage by targeting CIAPIN1 and regulating
            the NF-kappaB pathway
  JOURNAL   Mol Med Rep 20 (4), 3113-3122 (2019)
   PUBMED   31432171
  REMARK    GeneRIF: The present study illustrates that downregulation of miR16
            may protect against H/Rinduced injury partially by targeting
            CIAPIN1 and the NFkappaB signaling pathway.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Zhang,Y., Fang,J. and Ma,H.
  TITLE     Inhibition of miR-182-5p protects cardiomyocytes from
            hypoxia-induced apoptosis by targeting CIAPIN1
  JOURNAL   Biochem Cell Biol 96 (5), 646-654 (2018)
   PUBMED   29671338
  REMARK    GeneRIF: the knockdown of CIAPIN1 with small interfering RNAs
            (siRNAs) efficiently abolished the protective effects of miR-182-5p
            inhibitor on HICA, demonstrating that miR-182-5p plays a
            pro-apoptotic role in cardiomyocytes under hypoxic conditions by
            downregulating CIAPIN1.
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Frey,A.G., Palenchar,D.J., Wildemann,J.D. and Philpott,C.C.
  TITLE     A Glutaredoxin.BolA Complex Serves as an Iron-Sulfur Cluster
            Chaperone for the Cytosolic Cluster Assembly Machinery
  JOURNAL   J Biol Chem 291 (43), 22344-22356 (2016)
   PUBMED   27519415
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Paul,V.D. and Lill,R.
  TITLE     Biogenesis of cytosolic and nuclear iron-sulfur proteins and their
            role in genome stability
  JOURNAL   Biochim Biophys Acta 1853 (6), 1528-1539 (2015)
   PUBMED   25583461
  REMARK    Review article
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hao,Z., Li,X., Qiao,T., Du,R., Zhang,G. and Fan,D.
  TITLE     Subcellular localization of CIAPIN1
  JOURNAL   J Histochem Cytochem 54 (12), 1437-1444 (2006)
   PUBMED   16957168
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Shibayama,H., Takai,E., Matsumura,I., Kouno,M., Morii,E.,
            Kitamura,Y., Takeda,J. and Kanakura,Y.
  TITLE     Identification of a cytokine-induced antiapoptotic molecule
            anamorsin essential for definitive hematopoiesis
  JOURNAL   J Exp Med 199 (4), 581-592 (2004)
   PUBMED   14970183
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083753.1.
            
            On Nov 29, 2004 this sequence version replaced XP_226244.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083753.1, SRR8487226.144213.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..309
                     /product="anamorsin"
                     /note="fe-S cluster assembly protein DRE2 homolog"
                     /calculated_mol_wt=32911
     Region          6..172
                     /region_name="N-terminal SAM-like domain.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Region          <21..96
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cd02440"
                     /db_xref="CDD:100107"
     Region          173..222
                     /region_name="Linker.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6FI81; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6FI81; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     Region          233..301
                     /region_name="CIAPIN1"
                     /note="Cytokine-induced anti-apoptosis inhibitor 1, Fe-S
                     biogenesis; pfam05093"
                     /db_xref="CDD:398662"
     Region          235..249
                     /region_name="Fe-S binding site A.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WTY4; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     Region          271..285
                     /region_name="Fe-S binding site B.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Region          271..274
                     /region_name="Cx2C motif 1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Region          282..285
                     /region_name="Cx2C motif 2.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6FI81; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6FI81; propagated from
                     UniProtKB/Swiss-Prot (Q5XID1.1)"
     CDS             1..309
                     /gene="Ciapin1"
                     /coded_by="NM_001007689.1:313..1242"
                     /db_xref="GeneID:307649"
                     /db_xref="RGD:1549737"
ORIGIN      
        1 maefgispgq lvavfcdkss seealkklvg rvqgltgseg qvfvenitql lqsahkessf
       61 dvilsgivpg stslhspeal admarilrpg gclflkepve ttgvnndkik tasklcsalt
      121 lsglveikel qrealspeea qsmqehlgyh sdsllsvhvt gkkpnfevgs ssqlkllhkk
      181 sssvkpvvdp ataklwtlsa ndmeddsmdl idsdelldpe dlkkpdpasl kapscgegkk
      241 rkacknctcg laeelekeqs kaqssqpksa cgncylgdaf rcancpylgm pafkpgeqvl
      301 lsssnlqda
//
LOCUS       NP_001012074            1057 aa            linear   ROD 27-APR-2025
DEFINITION  probable E3 ubiquitin-protein ligase HERC4 [Rattus norvegicus].
ACCESSION   NP_001012074 XP_228147
VERSION     NP_001012074.1
DBSOURCE    REFSEQ: accession NM_001012074.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Sun,X., Sun,B., Cui,M. and Zhou,Z.
  TITLE     HERC4 exerts an anti-tumor role through destabilizing the
            oncoprotein Smo
  JOURNAL   Biochem Biophys Res Commun 513 (4), 1013-1018 (2019)
   PUBMED   31010679
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Rodriguez,C.I. and Stewart,C.L.
  TITLE     Disruption of the ubiquitin ligase HERC4 causes defects in
            spermatozoon maturation and impaired fertility
  JOURNAL   Dev Biol 312 (2), 501-508 (2007)
   PUBMED   17967448
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087104.1.
            
            On Feb 11, 2005 this sequence version replaced XP_228147.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087104.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p11"
     Protein         1..1057
                     /product="probable E3 ubiquitin-protein ligase HERC4"
                     /EC_number="2.3.2.26"
                     /note="HECT domain and RCC1-like domain-containing protein
                     4; hect domain and RLD 4; HECT-type E3 ubiquitin
                     transferase HERC4"
                     /calculated_mol_wt=118409
     Region          1..51
                     /region_name="RCC1 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          3..338
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          52..101
                     /region_name="RCC1 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          102..154
                     /region_name="RCC1 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          156..207
                     /region_name="RCC1 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          208..259
                     /region_name="RCC1 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          261..311
                     /region_name="RCC1 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          313..366
                     /region_name="RCC1 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN1.1)"
     Region          709..1055
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(715,745,756,813,990,1019..1020,1023..1027,1047,1054)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(841,844..845,847..848,851,860,862,866..867,869,874,
                     879,896,900)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..1057
                     /gene="Herc4"
                     /coded_by="NM_001012074.1:427..3600"
                     /db_xref="GeneID:309758"
                     /db_xref="RGD:1310971"
ORIGIN      
        1 mlcwgnasyg qlglggidee ivleprksdf fvnkkvrdvg cglrhtvfvl ddgtvytcgc
       61 ndlgqlghek srkkpeqvva ldaqnivavs cgeahtlaln dkgqvyawgl dsdgqlglqg
      121 seecirvprn ikslsdiqiv qvacgyyhsl alskasevfc wgqnkygqlg lgiecqkqts
      181 pqliksllgi pfmqvaagga hsfvltlsga ifgwgrnkfg qlglndendr yvpnllkslr
      241 sqkivyiccg edhtaaltke ggvftfgagg ygqlghnsts heinprkvfe lmgsivtqia
      301 cgrqhtsafv pssgriysfg lggngqlgtg stsnrkspft vkgnwfsyng qcpqdigsed
      361 yfcvkrifsg gdqsfshyss pqscgppddf rrsdpskqiw tvnealiqkw lsypsgrfpv
      421 eianeidgtf sssgclngsf lavsnddhyr tgtrfsgvdm naarllfhrl iqpdhpqisq
      481 qvaasleknl ipkltsslpd vealrfyltl pecplmsdcn nfttiaipfg talvnlekap
      541 lkvlenwwsv lepplflkiv elfkevvvhl lklykigipp serrifnsfl htalkvleil
      601 hrvnertgql iqydkfyihe vqelidirnd yinwvqqqay gvdvshgite ladipvtict
      661 ypfvfdaqak ttllqtdavl qmqmaidqah rqnvsslflp viesvnpcli lvvrrenivg
      721 damevlrktk nidykkplkv ifvgedavda ggvrkeffll imrelldpky gmfryyedsr
      781 liwfsdktfe dsdlfhligv icglaiynft ivdlhfplal ykkllkrkps lddlkelmpd
      841 vgrsmqqlld ypeddieetf clnftitven fgatevkelv lngadtavnk qnrqefvday
      901 vdyifnksva slfdafhagf hkvcggkvll lfqpnelqam vigntnydwk eleknteykg
      961 eywaehptik ifwevfhelp lekkkqfllf ltgsdripil gmkslklviq stgggesylp
     1021 vshtcfnlld lpkyteketl rckliqaidh negfsli
//
LOCUS       NP_445811                 68 aa            linear   ROD 27-APR-2025
DEFINITION  copper transport protein ATOX1 [Rattus norvegicus].
ACCESSION   NP_445811
VERSION     NP_445811.1
DBSOURCE    REFSEQ: accession NM_053359.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Chen,X., Xiang,W., Li,L. and Xu,K.
  TITLE     Copper Chaperone Atox1 Protected the Cochlea From Cisplatin by
            Regulating the Copper Transport Family and Cell Cycle
  JOURNAL   Int J Toxicol 43 (2), 134-145 (2024)
   PUBMED   37859596
  REMARK    GeneRIF: Copper Chaperone Atox1 Protected the Cochlea From
            Cisplatin by Regulating the Copper Transport Family and Cell Cycle.
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Palm-Espling,M.E., Andersson,C.D., Bjorn,E., Linusson,A. and
            Wittung-Stafshede,P.
  TITLE     Determinants for simultaneous binding of copper and platinum to
            human chaperone Atox1: hitchhiking not hijacking
  JOURNAL   PLoS One 8 (7), e70473 (2013)
   PUBMED   23936210
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Kohno,T., Urao,N., Ashino,T., Sudhahar,V., McKinney,R.D.,
            Hamakubo,T., Iwanari,H., Ushio-Fukai,M. and Fukai,T.
  TITLE     Novel role of copper transport protein antioxidant-1 in neointimal
            formation after vascular injury
  JOURNAL   Arterioscler Thromb Vasc Biol 33 (4), 805-813 (2013)
   PUBMED   23349186
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Monnot,A.D., Zheng,G. and Zheng,W.
  TITLE     Mechanism of copper transport at the blood-cerebrospinal fluid
            barrier: influence of iron deficiency in an in vitro model
  JOURNAL   Exp Biol Med (Maywood) 237 (3), 327-333 (2012)
   PUBMED   22442359
  REMARK    GeneRIF: these results suggest that Ctr1, DMT1, ATOX1 and ATP7A
            contribute to Cu transport at the blood-CSF barrier
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Tokuda,E., Okawa,E. and Ono,S.
  TITLE     Dysregulation of intracellular copper trafficking pathway in a
            mouse model of mutant copper/zinc superoxide dismutase-linked
            familial amyotrophic lateral sclerosis
  JOURNAL   J Neurochem 111 (1), 181-191 (2009)
   PUBMED   19656261
REFERENCE   6  (residues 1 to 68)
  AUTHORS   Hamza,I., Faisst,A., Prohaska,J., Chen,J., Gruss,P. and Gitlin,J.D.
  TITLE     The metallochaperone Atox1 plays a critical role in perinatal
            copper homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6848-6852 (2001)
   PUBMED   11391006
REFERENCE   7  (residues 1 to 68)
  AUTHORS   Kelner,G.S., Lee,M., Clark,M.E., Maciejewski,D., McGrath,D.,
            Rabizadeh,S., Lyons,T., Bredesen,D., Jenner,P. and Maki,R.A.
  TITLE     The copper transport protein Atox1 promotes neuronal survival
  JOURNAL   J Biol Chem 275 (1), 580-584 (2000)
   PUBMED   10617654
REFERENCE   8  (residues 1 to 68)
  AUTHORS   Hiromura,M. and Sakurai,H.
  TITLE     Molecular cloning of rat ATX1 homologue protein
  JOURNAL   Biochem Biophys Res Commun 265 (2), 509-512 (1999)
   PUBMED   10558899
REFERENCE   9  (residues 1 to 68)
  AUTHORS   Larin,D., Mekios,C., Das,K., Ross,B., Yang,A.S. and Gilliam,T.C.
  TITLE     Characterization of the interaction between the Wilson and Menkes
            disease proteins and the cytoplasmic copper chaperone, HAH1p
  JOURNAL   J Biol Chem 274 (40), 28497-28504 (1999)
   PUBMED   10497213
REFERENCE   10 (residues 1 to 68)
  AUTHORS   Naeve,G.S., Vana,A.M., Eggold,J.R., Kelner,G.S., Maki,R.,
            Desouza,E.B. and Foster,A.C.
  TITLE     Expression profile of the copper homeostasis gene, rAtox1, in the
            rat brain
  JOURNAL   Neuroscience 93 (3), 1179-1187 (1999)
   PUBMED   10473283
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI281905.1, AF177671.1 and BM392393.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058458.1, FQ220104.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..68
                     /product="copper transport protein ATOX1"
                     /EC_number="6.2.1.2"
                     /note="ATX1 homolog protein Rah1; metal transport protein
                     ATX1; ATX1 (antioxidant protein 1) homolog 1; ATX1
                     antioxidant protein 1 homolog"
                     /calculated_mol_wt=7161
     Region          5..63
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(10..12,15)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00244; propagated from
                     UniProtKB/Swiss-Prot (Q9WUC4.1)"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O08997; propagated from
                     UniProtKB/Swiss-Prot (Q9WUC4.1)"
     CDS             1..68
                     /gene="Atox1"
                     /gene_synonym="Atx1"
                     /coded_by="NM_053359.2:99..305"
                     /db_xref="GeneID:84355"
                     /db_xref="RGD:621684"
ORIGIN      
        1 mpkhefsvdm tcggcaeavs rvlnklggve fnidlpnkkv ciesehssdi llatlnktgk
       61 avsylgpk
//
LOCUS       NP_001034093             227 aa            linear   ROD 27-APR-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 5 [Rattus
            norvegicus].
ACCESSION   NP_001034093
VERSION     NP_001034093.1
DBSOURCE    REFSEQ: accession NM_001039004.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Brumbaugh,J., Di Stefano,B., Wang,X., Borkent,M., Forouzmand,E.,
            Clowers,K.J., Ji,F., Schwarz,B.A., Kalocsay,M., Elledge,S.J.,
            Chen,Y., Sadreyev,R.I., Gygi,S.P., Hu,G., Shi,Y. and
            Hochedlinger,K.
  TITLE     Nudt21 Controls Cell Fate by Connecting Alternative Polyadenylation
            to Chromatin Signaling
  JOURNAL   Cell 172 (1-2), 106-120 (2018)
   PUBMED   29249356
  REMARK    Erratum:[Cell. 2018 Jan 25;172(3):629-631. doi:
            10.1016/j.cell.2017.12.035. PMID: 29373832]
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Zhu,Y., Wang,X., Forouzmand,E., Jeong,J., Qiao,F., Sowd,G.A.,
            Engelman,A.N., Xie,X., Hertel,K.J. and Shi,Y.
  TITLE     Molecular Mechanisms for CFIm-Mediated Regulation of mRNA
            Alternative Polyadenylation
  JOURNAL   Mol Cell 69 (1), 62-74 (2018)
   PUBMED   29276085
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Means to an end: mechanisms of alternative polyadenylation of
            messenger RNA precursors
  JOURNAL   Wiley Interdiscip Rev RNA 5 (2), 183-196 (2014)
   PUBMED   24243805
  REMARK    Review article
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Gruber,A.R., Martin,G., Keller,W. and Zavolan,M.
  TITLE     Cleavage factor Im is a key regulator of 3' UTR length
  JOURNAL   RNA Biol 9 (12), 1405-1412 (2012)
   PUBMED   23187700
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Fukumitsu,H., Soumiya,H. and Furukawa,S.
  TITLE     Knockdown of pre-mRNA cleavage factor Im 25 kDa promotes neurite
            outgrowth
  JOURNAL   Biochem Biophys Res Commun 425 (4), 848-853 (2012)
   PUBMED   22898046
  REMARK    GeneRIF: Taken together, these results indicate that endogenous
            CFIm may promote neuritogenesis in developing neurons by
            coordinating events upstream of NGF-induced RhoA inactivation.
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Shimazu,T., Horinouchi,S. and Yoshida,M.
  TITLE     Multiple histone deacetylases and the CREB-binding protein regulate
            pre-mRNA 3'-end processing
  JOURNAL   J Biol Chem 282 (7), 4470-4478 (2007)
   PUBMED   17172643
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Kubo,T., Wada,T., Yamaguchi,Y., Shimizu,A. and Handa,H.
  TITLE     Knock-down of 25 kDa subunit of cleavage factor Im in Hela cells
            alters alternative polyadenylation within 3'-UTRs
  JOURNAL   Nucleic Acids Res 34 (21), 6264-6271 (2006)
   PUBMED   17098938
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Venkataraman,K., Brown,K.M. and Gilmartin,G.M.
  TITLE     Analysis of a noncanonical poly(A) site reveals a tripartite
            mechanism for vertebrate poly(A) site recognition
  JOURNAL   Genes Dev 19 (11), 1315-1327 (2005)
   PUBMED   15937220
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Dettwiler,S., Aringhieri,C., Cardinale,S., Keller,W. and
            Barabino,S.M.
  TITLE     Distinct sequence motifs within the 68-kDa subunit of cleavage
            factor Im mediate RNA binding, protein-protein interactions, and
            subcellular localization
  JOURNAL   J Biol Chem 279 (34), 35788-35797 (2004)
   PUBMED   15169763
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Ruegsegger,U., Beyer,K. and Keller,W.
  TITLE     Purification and characterization of human cleavage factor Im
            involved in the 3' end processing of messenger RNA precursors
  JOURNAL   J Biol Chem 271 (11), 6107-6113 (1996)
   PUBMED   8626397
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098748.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098748.1, FQ229498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..227
                     /product="cleavage and polyadenylation specificity factor
                     subunit 5"
                     /note="nudix motif 21; nucleoside diphosphate-linked
                     moiety X motif 21; cleavage and polyadenylation specific
                     factor 5; nudix (nucleoside diphosphate linked moiety
                     X)-type motif 21"
                     /calculated_mol_wt=26109
     Region          2..147
                     /region_name="Necessary for RNA-binding.
                     /evidence=ECO:0000250|UniProtKB:O43809"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            15
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Region          39..221
                     /region_name="NUDIX_Cfim25_Nudt21"
                     /note="25 kDa subunit of cleavage factor Im; cd18871"
                     /db_xref="CDD:467583"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            55
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            56
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Site            63
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000250|UniProtKB:O43809; propagated from
                     UniProtKB/Swiss-Prot (Q4KM65.1)"
     Region          81..160
                     /region_name="Necessary for interactions with PAPOLA and
                     PABPN1. /evidence=ECO:0000250|UniProtKB:O43809"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM65.1)"
     Region          102..104
                     /region_name="Interaction with RNA.
                     /evidence=ECO:0000250|UniProtKB:O43809"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM65.1)"
     Region          109..130
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM65.1)"
     CDS             1..227
                     /gene="Nudt21"
                     /gene_synonym="Cpsf5"
                     /coded_by="NM_001039004.1:82..765"
                     /db_xref="GeneID:291877"
                     /db_xref="RGD:1305766"
ORIGIN      
        1 msvvppnrsq tgwprgvnqf gnkyiqqtkp ltlertinly pltnytfgtk eplyekdssv
       61 aarfqrmree fdkigmrrtv egvlivhehr lphvlllqlg ttffklpgge lnpgedeveg
      121 lkrlmteilg rqdgvlqdwv iddcignwwr pnfeppqypy ipahitkpke hkklflvqlq
      181 ekalfavpkn yklvaaplfe lydnapgygp iisslpqlls rfnfiyn
//
LOCUS       NP_113875                128 aa            linear   ROD 27-APR-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein [Rattus
            norvegicus].
ACCESSION   NP_113875
VERSION     NP_113875.1
DBSOURCE    REFSEQ: accession NM_031687.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Tiwari,S., Singh,A., Gupta,P., K,A. and Singh,S.
  TITLE     UBA52 Attunes VDAC1-Mediated Mitochondrial Dysfunction and
            Dopaminergic Neuronal Death
  JOURNAL   ACS Chem Neurosci 14 (5), 839-850 (2023)
   PUBMED   36755387
  REMARK    GeneRIF: UBA52 Attunes VDAC1-Mediated Mitochondrial Dysfunction and
            Dopaminergic Neuronal Death.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Devulapalli,R., Jones,N., Farrell,K., Musaus,M., Kugler,H.,
            McFadden,T., Orsi,S.A., Martin,K., Nelsen,J., Navabpour,S.,
            O'Donnell,M., McCoig,E. and Jarome,T.J.
  TITLE     Males and females differ in the regulation and engagement of, but
            not requirement for, protein degradation in the amygdala during
            fear memory formation
  JOURNAL   Neurobiol Learn Mem 180, 107404 (2021)
   PUBMED   33609735
  REMARK    GeneRIF: Males and females differ in the regulation and engagement
            of, but not requirement for, protein degradation in the amygdala
            during fear memory formation.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Vincenzetti,S., Nasuti,C., Fedeli,D., Ricciutelli,M.,
            Pucciarelli,S. and Gabbianelli,R.
  TITLE     Proteomic analysis for early neurodegenerative biomarker detection
            in an animal model
  JOURNAL   Biochimie 121, 79-86 (2016)
   PUBMED   26631339
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Voorhees,R.M., Fernandez,I.S., Scheres,S.H. and Hegde,R.S.
  TITLE     Structure of the mammalian ribosome-Sec61 complex to 3.4 A
            resolution
  JOURNAL   Cell 157 (7), 1632-1643 (2014)
   PUBMED   24930395
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Redman,K.L. and Burris,G.W.
  TITLE     The cDNA for the ubiquitin-52-amino-acid fusion protein from rat
            encodes a previously unidentified 60 S ribosomal subunit protein
  JOURNAL   Biochem J 315 (Pt 1) (Pt 1), 315-321 (1996)
   PUBMED   8670124
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Barnard,G.F., Mori,M., Staniunas,R.J., Begum,N.A., Bao,S.,
            Puder,M., Cobb,J., Redman,K.L., Steele,G.D. Jr. and Chen,L.B.
  TITLE     Ubiquitin fusion proteins are overexpressed in colon cancer but not
            in gastric cancer
  JOURNAL   Biochim Biophys Acta 1272 (3), 147-153 (1995)
   PUBMED   8541345
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Chan,Y.L., Suzuki,K. and Wool,I.G.
  TITLE     The carboxyl extensions of two rat ubiquitin fusion proteins are
            ribosomal proteins S27a and L40
  JOURNAL   Biochem Biophys Res Commun 215 (2), 682-690 (1995)
   PUBMED   7488009
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Hubbard,M.J. and Carne,A.
  TITLE     Differential feeding-related regulation of ubiquitin and
            calbindin9kDa in rat duodenum
  JOURNAL   Biochim Biophys Acta 1200 (2), 191-196 (1994)
   PUBMED   8031840
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Hayashi,T., Noga,M. and Matsuda,M.
  TITLE     Nucleotide sequence and expression of the rat polyubiquitin mRNA
  JOURNAL   Biochim Biophys Acta 1218 (2), 232-234 (1994)
   PUBMED   8018730
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP480615.1, BC061544.1 and BP492585.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217153.1, FQ222440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..128
                     /product="ubiquitin-ribosomal protein eL40 fusion protein"
                     /note="60S ribosomal protein L40; ubiquitin-60S ribosomal
                     protein L40; CEP52"
                     /calculated_mol_wt=14597
     Region          1..76
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(6..9,11,34..37,40,42,44,46..49,68..76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(8..12,31..35,40,42,44,46..49,68,70..76)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            54
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62986.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000250|UniProtKB:P62987; propagated from
                     UniProtKB/Swiss-Prot (P62986.2)"
     Site            68
                     /site_type="other"
                     /note="Essential for function; propagated from
                     UniProtKB/Swiss-Prot (P62986.2)"
     Site            72
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62986.2)"
     Region          79..126
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     Site            98
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:9219540; propagated from
                     UniProtKB/Swiss-Prot (P62986.2)"
     CDS             1..128
                     /gene="Uba52"
                     /gene_synonym="Rps27a; Ubb"
                     /coded_by="NM_031687.3:50..436"
                     /db_xref="GeneID:64156"
                     /db_xref="RGD:68344"
ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggiiep slrqlaqkyn cdkmicrkcy arlhpravnc rkkkcghtnn
      121 lrpkkkvk
//
LOCUS       NP_579845                183 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-24 precursor [Rattus norvegicus].
ACCESSION   NP_579845
VERSION     NP_579845.1
DBSOURCE    REFSEQ: accession NM_133311.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Gao,R., Li,Z., Ai,D., Ma,J., Chen,C. and Liu,X.
  TITLE     Interleukin-24 as a Pulmonary Target Cytokine in Bronchopulmonary
            Dysplasia
  JOURNAL   Cell Biochem Biophys 79 (2), 311-320 (2021)
   PUBMED   33683657
  REMARK    GeneRIF: Interleukin-24 as a Pulmonary Target Cytokine in
            Bronchopulmonary Dysplasia.
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Pap,D., Sziksz,E., Kiss,Z., Rokonay,R., Veres-Szekely,A.,
            Lippai,R., Takacs,I.M., Kis,E., Fekete,A., Reusz,G., Szabo,A.J. and
            Vannay,A.
  TITLE     Microarray Analysis Reveals Increased Expression of Matrix
            Metalloproteases and Cytokines of Interleukin-20 Subfamily in the
            Kidneys of Neonate Rats Underwent Unilateral Ureteral Obstruction:
            A Potential Role of IL-24 in the Regulation of Inflammation and
            Tissue Remodeling
  JOURNAL   Kidney Blood Press Res 42 (1), 16-32 (2017)
   PUBMED   28253513
  REMARK    GeneRIF: In studies of Congenital obstructive nephropathy in rat,
            it was found that il24 was upregulated and that il24 decreases the
            expression of IL-6 and MMP-3 in the renal epithelial cells.
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Zhao,Y., Tian,L., Sheng,W., Miao,J. and Yang,J.
  TITLE     Hypalgesia effect of IL-24, a quite new mechanism for IL-24
            application in cancer treatment
  JOURNAL   J Interferon Cytokine Res 33 (10), 606-611 (2013)
   PUBMED   23869901
  REMARK    GeneRIF: IL-24 has a potential treatment effect on cancers not only
            by inhibiting tumor proliferation, but also by the promotion of
            beta-endorphin synthesis, inhibition of IL-6 secretion to relieve
            cancer pain.
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Li,Y., Messina,C., Bendaoud,M., Fine,D.H., Schreiner,H. and
            Tsiagbe,V.K.
  TITLE     Adaptive immune response in osteoclastic bone resorption induced by
            orally administered Aggregatibacter actinomycetemcomitans in a rat
            model of periodontal disease
  JOURNAL   Mol Oral Microbiol 25 (4), 275-292 (2010)
   PUBMED   20618701
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Bastonero,S., Le Priol,Y., Armand,M., Bernard,C.S.,
            Reynaud-Gaubert,M., Olive,D., Parzy,D., de Bentzmann,S., Capo,C.
            and Mege,J.L.
  TITLE     New microbicidal functions of tracheal glands: defective
            anti-infectious response to Pseudomonas aeruginosa in cystic
            fibrosis
  JOURNAL   PLoS One 4 (4), e5357 (2009)
   PUBMED   19399182
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Shinohara,S. and Rothstein,J.L.
  TITLE     Interleukin 24 is induced by the RET/PTC3 oncoprotein and is an
            autocrine growth factor for epithelial cells
  JOURNAL   Oncogene 23 (45), 7571-7579 (2004)
   PUBMED   15326486
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Garn,H., Schmidt,A., Grau,V., Stumpf,S., Kaufmann,A., Becker,M.,
            Gemsa,D. and Siese,A.
  TITLE     IL-24 is expressed by rat and human macrophages
  JOURNAL   Immunobiology 205 (3), 321-334 (2002)
   PUBMED   12182458
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Schaefer,G., Venkataraman,C. and Schindler,U.
  TITLE     Cutting edge: FISP (IL-4-induced secreted protein), a novel
            cytokine-like molecule secreted by Th2 cells
  JOURNAL   J Immunol 166 (10), 5859-5863 (2001)
   PUBMED   11342597
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Zhang,R., Tan,Z. and Liang,P.
  TITLE     Identification of a novel ligand-receptor pair constitutively
            activated by ras oncogenes
  JOURNAL   J Biol Chem 275 (32), 24436-24443 (2000)
   PUBMED   10825166
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Soo,C., Shaw,W.W., Freymiller,E., Longaker,M.T., Bertolami,C.N.,
            Chiu,R., Tieu,A. and Ting,K.
  TITLE     Cutaneous rat wounds express c49a, a novel gene with homology to
            the human melanoma differentiation associated gene, mda-7
  JOURNAL   J Cell Biochem 74 (1), 1-10 (1999)
   PUBMED   10381256
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF269251.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF269251.1, AF004774.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..183
                     /product="interleukin-24 precursor"
                     /note="cytokine-like protein Mob-5; IL-24; interferon 2e"
                     /calculated_mol_wt=18011
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3103
     mat_peptide     29..183
                     /product="Interleukin-24. /id=PRO_0000015388"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI24.1)"
                     /calculated_mol_wt=18011
     Region          <50..177
                     /region_name="IL10"
                     /note="Interleukin 10; cl02501"
                     /db_xref="CDD:413341"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JI24.1)"
     CDS             1..183
                     /gene="Il24"
                     /gene_synonym="If2e; Mda-7; Mda7"
                     /coded_by="NM_133311.1:232..783"
                     /db_xref="GeneID:170819"
                     /db_xref="RGD:621484"
ORIGIN      
        1 mqtslrqqil pglslillvl nqvpelqgqe frfgpcqvtg vvlpelweaf wtvkntvktq
       61 deltsvrllk pqvlqnvsda escylahsll kfylntvfkn yhskivkfkv lksfstlann
      121 flvimsklqp skdnamlpis dsarrrflly hrtfkqldie valakafgev dillawmqnf
      181 yql
//
LOCUS       NP_001106815             403 aa            linear   ROD 27-APR-2025
DEFINITION  beta-galactoside alpha-2,6-sialyltransferase 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001106815
VERSION     NP_001106815.1
DBSOURCE    REFSEQ: accession NM_001113344.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Meng,L., Forouhar,F., Thieker,D., Gao,Z., Ramiah,A., Moniz,H.,
            Xiang,Y., Seetharaman,J., Milaninia,S., Su,M., Bridger,R.,
            Veillon,L., Azadi,P., Kornhaber,G., Wells,L., Montelione,G.T.,
            Woods,R.J., Tong,L. and Moremen,K.W.
  TITLE     Enzymatic basis for N-glycan sialylation: structure of rat
            alpha2,6-sialyltransferase (ST6GAL1) reveals conserved and unique
            features for glycan sialylation
  JOURNAL   J Biol Chem 288 (48), 34680-34698 (2013)
   PUBMED   24155237
  REMARK    GeneRIF: Comparisons of the structure with pig ST3GAL1 and a
            bacterial sialyltransferase revealed a similar positioning of
            donor, acceptor, and catalytic residues that provide a common
            structural framework for catalysis
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Kuhn,B., Benz,J., Greif,M., Engel,A.M., Sobek,H. and Rudolph,M.G.
  TITLE     The structure of human alpha-2,6-sialyltransferase reveals the
            binding mode of complex glycans
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 9), 1826-1838 (2013)
   PUBMED   23999306
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Hirano,Y., Suzuki,T., Matsumoto,T., Ishihara,Y., Takaki,Y.,
            Kono,M., Dohmae,N. and Tsuji,S.
  TITLE     Disulphide linkage in mouse ST6Gal-I: determination of linkage
            positions and mutant analysis
  JOURNAL   J Biochem 151 (2), 197-203 (2012)
   PUBMED   22039275
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Liu,Z., Swindall,A.F., Kesterson,R.A., Schoeb,T.R., Bullard,D.C.
            and Bellis,S.L.
  TITLE     ST6Gal-I regulates macrophage apoptosis via alpha2-6 sialylation of
            the TNFR1 death receptor
  JOURNAL   J Biol Chem 286 (45), 39654-39662 (2011)
   PUBMED   21930713
  REMARK    GeneRIF: ST6Gal-I regulates macrophage apoptosis via alpha2-6
            sialylation of the TNFR1 death receptor.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Maksimovic,J., Sharp,J.A., Nicholas,K.R., Cocks,B.G. and Savin,K.
  TITLE     Conservation of the ST6Gal I gene and its expression in the mammary
            gland
  JOURNAL   Glycobiology 21 (4), 467-481 (2011)
   PUBMED   21098517
  REMARK    GeneRIF: rat ST6GAL1 mRNA possess an L exon, suggesting
            conservation of this regulatory element in rodents
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Wen,D.X., Svensson,E.C. and Paulson,J.C.
  TITLE     Tissue-specific alternative splicing of the beta-galactoside alpha
            2,6-sialyltransferase gene
  JOURNAL   J Biol Chem 267 (4), 2512-2518 (1992)
   PUBMED   1733948
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Svensson,E.C., Soreghan,B. and Paulson,J.C.
  TITLE     Organization of the beta-galactoside alpha 2,6-sialyltransferase
            gene. Evidence for the transcriptional regulation of terminal
            glycosylation
  JOURNAL   J Biol Chem 265 (34), 20863-20868 (1990)
   PUBMED   2249992
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Wang,X.C., Smith,T.J. and Lau,J.T.
  TITLE     Transcriptional regulation of the liver beta-galactoside alpha
            2,6-sialyltransferase by glucocorticoids
  JOURNAL   J Biol Chem 265 (29), 17849-17853 (1990)
   PUBMED   2211665
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Wang,X., O'Hanlon,T.P., Young,R.F. and Lau,J.T.
  TITLE     Rat beta-galactoside alpha 2,6-sialyltransferase genomic
            organization: alternate promoters direct the synthesis of liver and
            kidney transcripts
  JOURNAL   Glycobiology 1 (1), 25-31 (1990)
   PUBMED   1983783
REFERENCE   10 (residues 1 to 403)
  AUTHORS   O'Hanlon,T.P., Lau,K.M., Wang,X.C. and Lau,J.T.
  TITLE     Tissue-specific expression of beta-galactoside
            alpha-2,6-sialyltransferase. Transcript heterogeneity predicts a
            divergent polypeptide
  JOURNAL   J Biol Chem 264 (29), 17389-17394 (1989)
   PUBMED   2793863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M18769.1 and JAXUCZ010000011.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M18769.1, FQ224146.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..403
                     /product="beta-galactoside alpha-2,6-sialyltransferase 1
                     isoform 1"
                     /EC_number="2.4.3.1"
                     /note="beta-galactoside alpha-2,6-sialyltransferase 1;
                     ST6Gal I; ST6 beta-galactosamide
                     alpha-2,6-sialyltranferase 1;
                     CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,
                     6-sialyltransferase 1; ST6GalI; alpha 2,6-ST 1;
                     Sialyltransferase 1 (beta-galactoside
                     alpha-2,6-sialytransferase); Sialyltransferase 1
                     (beta-galactoside alpha-26-sialytransferase)"
                     /calculated_mol_wt=46623
     Site            10..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13721.2)"
     Region          63..403
                     /region_name="Catalytic (soluble form).
                     /evidence=ECO:0000305|PubMed:3121604"
                     /note="propagated from UniProtKB/Swiss-Prot (P13721.2)"
     Region          134..398
                     /region_name="GT29_ST6GAL1"
                     /note="beta-galactoside alpha-2,6-sialyltransferase 1;
                     cd23985"
                     /db_xref="CDD:467713"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24155237,
                     ECO:0007744|PDB:4MPS; propagated from UniProtKB/Swiss-Prot
                     (P13721.2)"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24155237,
                     ECO:0007744|PDB:4MPS; propagated from UniProtKB/Swiss-Prot
                     (P13721.2)"
     Site            order(185..187,208..209,230,319..321,339..340,349..351,
                     367)
                     /site_type="active"
                     /db_xref="CDD:467713"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P15907; propagated from
                     UniProtKB/Swiss-Prot (P13721.2)"
     CDS             1..403
                     /gene="St6gal1"
                     /gene_synonym="Siat1"
                     /coded_by="NM_001113344.1:182..1393"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25197"
                     /db_xref="RGD:3676"
ORIGIN      
        1 mihtnlkkkf slfilvfllf avicvwkkgs dyealtlqak efqmpksqek vamgsasqvv
       61 fsnskqdpke dipilsyhrv takvkpqpsf qvwdkdstys klnprllkiw rnylnmnkyk
      121 vsykgpgpgv kfsvealrch lrdhvnvsmi eatdfpfntt ewegylpken frtkvgpwqr
      181 cavvssagsl knsqlgreid nhdavlrfng aptdnfqqdv gskttirlmn sqlvttekrf
      241 lkdslytegi livwdpsvyh adipkwyqkp dynffetyks yrrlnpsqpf yilkpqmpwe
      301 lwdiiqeisa dliqpnppss gmlgiiimmt lcdqvdiyef lpskrktdvc yyhqkffdsa
      361 ctmgayhpll feknmvkhln egtdediylf gkatlsgfrn irc
//
LOCUS       NP_001011891             271 aa            linear   ROD 27-APR-2025
DEFINITION  cytosolic Fe-S cluster assembly factor NUBP2 [Rattus norvegicus].
ACCESSION   NP_001011891 XP_213239
VERSION     NP_001011891.1
DBSOURCE    REFSEQ: accession NM_001011891.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Paul,V.D. and Lill,R.
  TITLE     Biogenesis of cytosolic and nuclear iron-sulfur proteins and their
            role in genome stability
  JOURNAL   Biochim Biophys Acta 1853 (6), 1528-1539 (2015)
   PUBMED   25583461
  REMARK    Review article
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Christodoulou,A., Lederer,C.W., Surrey,T., Vernos,I. and Santama,N.
  TITLE     Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is
            implicated in the regulation of centrosome duplication
  JOURNAL   J Cell Sci 119 (Pt 10), 2035-2047 (2006)
   PUBMED   16638812
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079386.1.
            
            On Feb 11, 2005 this sequence version replaced XP_213239.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079386.1, FQ213066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155302, SAMD00155323
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..271
                     /product="cytosolic Fe-S cluster assembly factor NUBP2"
                     /note="NBP 2; nucleotide binding protein 2"
                     /calculated_mol_wt=28795
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5Y2,
                     ECO:0000255|HAMAP-Rule:MF_03039; propagated from
                     UniProtKB/Swiss-Prot (Q68FS1.1)"
     Region          12..263
                     /region_name="ParA"
                     /note="NUBPL iron-transfer P-loop NTPase; pfam10609"
                     /db_xref="CDD:431392"
     Site            order(23..30,163,165,190..191,227..229,232..233)
                     /site_type="active"
                     /db_xref="CDD:349757"
     Site            order(23..25,54..55,57,60..61,106..107,137,139,142,169,
                     172,228,230..231,233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349757"
     CDS             1..271
                     /gene="Nubp2"
                     /coded_by="NM_001011891.1:28..843"
                     /db_xref="GeneID:287125"
                     /db_xref="RGD:1305113"
ORIGIN      
        1 meaaaepgnl agvrhiilvl sgkggvgkst istelalalr hqgkkvgild vdlcgpsiph
       61 mlhaqgkavh qcdsgwvpvf vdqeqsislm svgfllenpd eavvwrgpkk halikqfvsd
      121 vawgeldylv vdtppgtsde hmatvealrp ykplgalvvt tpqavsigdv rreltfckkt
      181 glqvigvien msgfacphca ectnvfssgg geelarlagv pflgsvpldp qltrsleegr
      241 dfiqefpkst aysaltsiah kvlhqmpalc s
//
LOCUS       NP_001103569            1073 aa            linear   ROD 27-APR-2025
DEFINITION  proto-oncogene tyrosine-protein kinase receptor Ret isoform b
            precursor [Rattus norvegicus].
ACCESSION   NP_001103569
VERSION     NP_001103569.1
DBSOURCE    REFSEQ: accession NM_001110099.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Kasanga,E.A., Han,Y., Navarrete,W., McManus,R., Shifflet,M.K.,
            Parry,C., Barahona,A., Manfredsson,F.P., Nejtek,V.A.,
            Richardson,J.R. and Salvatore,M.F.
  TITLE     Differential expression of RET and GDNF family receptor,
            GFR-alpha1, between striatum and substantia nigra following
            nigrostriatal lesion: A case for diminished GDNF-signaling
  JOURNAL   Exp Neurol 366, 114435 (2023)
   PUBMED   37178997
  REMARK    GeneRIF: Differential expression of RET and GDNF family receptor,
            GFR-alpha1, between striatum and substantia nigra following
            nigrostriatal lesion: A case for diminished GDNF-signaling.
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Kearon,J.E., Kocherry,S.C., Zoumboulakis,D., Rivera,D.,
            Lourenssen,S.R. and Blennerhassett,M.G.
  TITLE     GDNF requires HIF-1alpha and RET activation for suppression of
            programmed cell death of enteric neurons by metabolic challenge
  JOURNAL   Mol Cell Neurosci 115, 103655 (2021)
   PUBMED   34273501
  REMARK    GeneRIF: GDNF requires HIF-1alpha and RET activation for
            suppression of programmed cell death of enteric neurons by
            metabolic challenge.
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Hu,X.B., Fu,S.H., Luo,Q.I., He,J.Z., Qiu,Y.F., Lai,W. and Zhong,M.
  TITLE     Down-regulation of microRNA-216a confers protection against yttrium
            aluminium garnet laser-induced retinal injury via the GDNF-mediated
            GDNF/GFRalpha1/RET signalling pathway
  JOURNAL   J Biosci 43 (5), 985-1000 (2018)
   PUBMED   30541958
  REMARK    GeneRIF: The findings demonstrate that elevated GDNF levels can
            reduce the retinal injury, whereby down-regulated miR-216a
            aggravates the YAG laser-induced retinal injury by targeting the
            GDNF level through the GDNF/GFRa1/RET signaling pathway.
REFERENCE   4  (residues 1 to 1073)
  AUTHORS   Pertile,R.A.N., Cui,X., Hammond,L. and Eyles,D.W.
  TITLE     Vitamin D regulation of GDNF/Ret signaling in dopaminergic neurons
  JOURNAL   FASEB J 32 (2), 819-828 (2018)
   PUBMED   29018141
  REMARK    GeneRIF: the inverse relationship between GFRalpha1 and C-Ret, as
            knocking down C-Ret led to increases in GFRalpha1 expression.
REFERENCE   5  (residues 1 to 1073)
  AUTHORS   Hsu,J.Y., Crawley,S., Chen,M., Ayupova,D.A., Lindhout,D.A.,
            Higbee,J., Kutach,A., Joo,W., Gao,Z., Fu,D., To,C., Mondal,K.,
            Li,B., Kekatpure,A., Wang,M., Laird,T., Horner,G., Chan,J.,
            McEntee,M., Lopez,M., Lakshminarasimhan,D., White,A., Wang,S.P.,
            Yao,J., Yie,J., Matern,H., Solloway,M., Haldankar,R., Parsons,T.,
            Tang,J., Shen,W.D., Alice Chen,Y., Tian,H. and Allan,B.B.
  TITLE     Non-homeostatic body weight regulation through a
            brainstem-restricted receptor for GDF15
  JOURNAL   Nature 550 (7675), 255-259 (2017)
   PUBMED   28953886
  REMARK    Erratum:[Nature. 2017 Nov 16;551(7680):398. doi:
            10.1038/nature24481. PMID: 29144449]
REFERENCE   6  (residues 1 to 1073)
  AUTHORS   Kitagawa,H., Sasaki,C., Zhang,W.R., Sakai,K., Shiro,Y., Warita,H.,
            Mitsumoto,Y., Mori,T. and Abe,K.
  TITLE     Induction of glial cell line-derived neurotrophic factor receptor
            proteins in cerebral cortex and striatum after permanent middle
            cerebral artery occlusion in rats
  JOURNAL   Brain Res 834 (1-2), 190-195 (1999)
   PUBMED   10407114
REFERENCE   7  (residues 1 to 1073)
  AUTHORS   Natarajan,D., Grigoriou,M., Marcos-Gutierrez,C.V., Atkins,C. and
            Pachnis,V.
  TITLE     Multipotential progenitors of the mammalian enteric nervous system
            capable of colonising aganglionic bowel in organ culture
  JOURNAL   Development 126 (1), 157-168 (1999)
   PUBMED   9834195
REFERENCE   8  (residues 1 to 1073)
  AUTHORS   Baloh,R.H., Gorodinsky,A., Golden,J.P., Tansey,M.G., Keck,C.L.,
            Popescu,N.C., Johnson,E.M. Jr. and Milbrandt,J.
  TITLE     GFRalpha3 is an orphan member of the GDNF/neurturin/persephin
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 95 (10), 5801-5806 (1998)
   PUBMED   9576965
REFERENCE   9  (residues 1 to 1073)
  AUTHORS   Burazin,T.C. and Gundlach,A.L.
  TITLE     Up-regulation of GDNFR-alpha and c-ret mRNA in facial motor neurons
            following facial nerve injury in the rat
  JOURNAL   Brain Res Mol Brain Res 55 (2), 331-336 (1998)
   PUBMED   9582449
REFERENCE   10 (residues 1 to 1073)
  AUTHORS   Canzian,F., Ushijima,T., Nagao,M., Matera,I., Romeo,G. and
            Ceccherini,I.
  TITLE     Genetic mapping of the RET protooncogene on rat chromosome 4
  JOURNAL   Mamm Genome 6 (6), 433-435 (1995)
   PUBMED   7647468
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and unique C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ299017.1, SRR26643288.20313.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1073
                     /product="proto-oncogene tyrosine-protein kinase receptor
                     Ret isoform b precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine kinase; Ret proto-oncogene
                     (multiple endocrine neoplasia MEN2A MEN2B and medullary
                     thyroid carcinoma 1 Hirschsprung disease); proto-oncogene
                     tyrosine-protein kinase receptor Ret; Ret gene for
                     receptor tyrosin"
                     /calculated_mol_wt=117073
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2778
     Region          29..154
                     /region_name="RET_CLD1"
                     /note="RET Cadherin like domain 1; pfam17756"
                     /db_xref="CDD:465485"
     Region          29..153
                     /region_name="Cadherin-like region 1 (CLD1).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          173..248
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(178..179,230,232,265,267..268)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          266..380
                     /region_name="Cadherin-like region 3 (CLD3).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          266..380
                     /region_name="RET_CLD3"
                     /note="RET Cadherin like domain 3; pfam17812"
                     /db_xref="CDD:465516"
     Site            378
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            395
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          406..507
                     /region_name="Cadherin-like region 4 (CLD4).
                     /evidence=ECO:0000250|UniProtKB:P07949"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          408..507
                     /region_name="RET_CLD4"
                     /note="RET Cadherin like domain 4; pfam17813"
                     /db_xref="CDD:465517"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            469
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            555
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            638..658
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            689
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            708..709
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Region          724..1013
                     /region_name="PTKc_RET"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     REarranged during Transfection protein; cd05045"
                     /db_xref="CDD:173631"
     Site            order(731..735,739,757,759,805..806,808,812,875,879..880,
                     882,893,911..915,924,958)
                     /site_type="active"
                     /db_xref="CDD:173631"
     Site            order(731..734,739,757,759,805..806,808,812,882,893)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173631"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            order(875,879,911..915,924,958)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173631"
     Site            892..917
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173631"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            982
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1018..1019
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     Site            1063
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P07949; propagated from
                     UniProtKB/Swiss-Prot (G3V9H8.1)"
     CDS             1..1073
                     /gene="Ret"
                     /coded_by="NM_001110099.1:14..3235"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:24716"
                     /db_xref="RGD:3556"
ORIGIN      
        1 makarsgaag lglklflllp llgeaplgly fsrdaywerl yvdqpagtpl lyvhalrdap
       61 gevpsfrlgq ylygvyrtrl hendwihids gtgllylnqs ldhssweqls irnggfpllt
      121 vflqvflgst aqregechwp gcarvyfsfi ndtfpncssf kardlctpet gvsfrirenr
      181 ppgtfyqfrm lpvqflcpni svkykllegd glpfrcdpdc levstrwald relqekyvle
      241 aecavagpga nkekvavsfp vtvydeddsp ptfsggvgta savvefkrke gtvvatlqvf
      301 dadvvpasge lvrrytstll sgdswaqqtf rvehtpnetl vqsnnnsvra tmhnyklvln
      361 rslsisesrv lqlvvlvnds dfqgpgsgvl flhfnvsvlp vtlnlpmays fpvnrrarry
      421 aqigkvcven cqefsgvsiq yklqpsstnc salgvvtste dtsgtlyvnd tealrrpect
      481 elqytvvatd rqtrrqtqas lvvtvegtyi aeevgcpksc avnkrrpece ecgglgsptg
      541 rcewrqgdgk gitrnfstcs pstrtcpdgh cdalesrdin icpqdclrgp ivggherger
      601 qgikagygic ncfpdekkcf cepedsqgpl cdelcrtvit aavlfsfiis vllstfcihr
      661 yhkhahkppi asaemtfcrp aqgfpisyss sgtrrpslds menqvsvdsf kipedpkwef
      721 prknlvlgkt lgegefgkvv katafrlkgr agyttvavkm lkenasqsel rdllsefnll
      781 kqvnhphvik lygacsqdgp llliveyaky gslrgflrds rkigpayvss ggsrnsssld
      841 hpdervltmg dlisfawqis rgmqylaemk lvhrdlaarn ilvaegrkmk isdfglsrdv
      901 yeedsyvkks kgripvkwma ieslfdhiyt tqsdvwsfgv llweivtlgg npypgipper
      961 lfnllktghr merpdncsee myrlmlqcwk qepdkrpvfa diskdlekmm vksrdyldla
     1021 astpsdslly ddglseeetp lvdcnsaplp rslpstwien klygrishaf trf
//
LOCUS       NP_036676               1313 aa            linear   ROD 27-APR-2025
DEFINITION  angiotensin-converting enzyme precursor [Rattus norvegicus].
ACCESSION   NP_036676
VERSION     NP_036676.1
DBSOURCE    REFSEQ: accession NM_012544.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1313)
  AUTHORS   Ferreira-Duarte,M., Oliveira,L.C.G., Quintas,C.,
            Esteves-Monteiro,M., Duarte-Araujo,M., Sousa,T., Casarini,D.E. and
            Morato,M.
  TITLE     ACE and ACE2 catalytic activity in the fecal content along the gut
  JOURNAL   Neurogastroenterol Motil 35 (9), e14598 (2023)
   PUBMED   37052403
  REMARK    GeneRIF: ACE and ACE2 catalytic activity in the fecal content along
            the gut.
REFERENCE   2  (residues 1 to 1313)
  AUTHORS   Lin,Y., Li,Y.Q., Wang,H., Wu,H.J., Bai,B.L., Ma,L.J., Zou,J.Z.,
            Zhang,Q. and Shi,L.
  TITLE     Increasing angiotensin-converting enzyme 1 regulated by histone 3
            lysine 27 hyperacetylation in high-fat diet-induced hypertensive
            rat kidney
  JOURNAL   J Hypertens 40 (10), 1969-1978 (2022)
   PUBMED   35969203
  REMARK    GeneRIF: Increasing angiotensin-converting enzyme 1 regulated by
            histone 3 lysine 27 hyperacetylation in high-fat diet-induced
            hypertensive rat kidney.
REFERENCE   3  (residues 1 to 1313)
  AUTHORS   Saadat,M.
  TITLE     No significant correlation between ACE Ins/Del genetic polymorphism
            and COVID-19 infection
  JOURNAL   Clin Chem Lab Med 58 (7), 1127-1128 (2020)
   PUBMED   32386188
REFERENCE   4  (residues 1 to 1313)
  AUTHORS   Delanghe,J.R., Speeckaert,M.M. and De Buyzere,M.L.
  TITLE     COVID-19 infections are also affected by human ACE1 D/I
            polymorphism
  JOURNAL   Clin Chem Lab Med 58 (7), 1125-1126 (2020)
   PUBMED   32286246
REFERENCE   5  (residues 1 to 1313)
  AUTHORS   Shu,Y., Cao,X.Y. and Chen,J.
  TITLE     Preparation and antagonistic effect of ACE inhibitory peptide from
            cashew
  JOURNAL   J Sci Food Agric 99 (15), 6822-6832 (2019)
   PUBMED   31385307
REFERENCE   6  (residues 1 to 1313)
  AUTHORS   Weinreb,R.N., O'Donnell,J.J., Sandman,R., Char,D.H. and Kimura,S.J.
  TITLE     Angiotensin-converting enzyme in sarcoid uveitis
  JOURNAL   Invest Ophthalmol Vis Sci 18 (12), 1285-1287 (1979)
   PUBMED   229083
REFERENCE   7  (residues 1 to 1313)
  AUTHORS   Sedov,V.A.
  TITLE     [To sanitize liv stock raising of helminthiases]
  JOURNAL   Veterinariia (12), 10-12 (1978)
   PUBMED   734899
REFERENCE   8  (residues 1 to 1313)
  AUTHORS   Zderkiewicz,E.
  TITLE     [Autoregulation of cerebral blood flow]
  JOURNAL   Pol Tyg Lek 33 (29), 1157-1159 (1978)
   PUBMED   704419
REFERENCE   9  (residues 1 to 1313)
  AUTHORS   Sancho,J., Re,R., Burton,J., Barger,A.C. and Haber,E.
  TITLE     The role of the renin-angiotensin-aldosterone system in
            cardiovascular homeostasis in normal human subjects
  JOURNAL   Circulation 53 (3), 400-405 (1976)
   PUBMED   174834
REFERENCE   10 (residues 1 to 1313)
  AUTHORS   Silverstein,E., Friedland,J., Lyons,H.A. and Gourin,A.
  TITLE     Elevation of angiotensin-converting enzyme in granulomatous lymph
            nodes and serum in sarcoidosis: clinical and possible pathogenic
            significance
  JOURNAL   Ann N Y Acad Sci 278, 498-513 (1976)
   PUBMED   183595
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U03734.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U03734.1, BC085760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1313
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..1313
                     /product="angiotensin-converting enzyme precursor"
                     /EC_number="3.4.15.1"
                     /note="kininase II; angiotensin-converting enzyme;
                     dipeptidyl carboxypeptidase I; angiotensin 1 converting
                     enzyme 1; Dipeptidyl carboxypeptidase 1 (Angiotensin
                     I-converting enzyme); angiotensin I-converting enzyme
                     (Dipeptidyl carboxypeptidase 1); angiotensin I converting
                     enzyme 1; angiotensin I converting enzyme
                     (peptidyl-dipeptidase A) 1; angiotensin-converting
                     enzyme-like"
                     /calculated_mol_wt=147263
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3635
     mat_peptide     36..1313
                     /product="Angiotensin-converting enzyme.
                     /id=PRO_0000028557"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
                     /calculated_mol_wt=147263
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Region          46..629
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:460196"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Region          650..1227
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:460196"
     Site            683
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            701
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Site            1197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     Region          1221..1262
                     /region_name="Juxtamembrane stalk.
                     /evidence=ECO:0000250|UniProtKB:P12821"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
     Site            1266..1282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
     Site            1306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P47820.1)"
     CDS             1..1313
                     /gene="Ace"
                     /gene_synonym="CD143; Dcp1; StsRR92"
                     /coded_by="NM_012544.1:24..3965"
                     /db_xref="GeneID:24310"
                     /db_xref="RGD:2493"
ORIGIN      
        1 mgaasgqrgr wplsppllml slllllllpp spapaldpgl qpgnfsadea gaqlfadsyn
       61 ssaevvmfqs taaswahdtn iteenarlqe eaalinqefa evwgkkakel yesiwqnftd
      121 qklrriigsv qtlgpanlpl tqrlqynsll snmsriystg kvcfpnktat cwsldpeltn
      181 ilassrnyak vlfawegwhd avgiplkply qdftalsnea yrqdgfsdtg aywrswyesp
      241 sfeeslehly hqveplylnl hafvrralhr rygdkyinlr gpipahllgd mwaqsweniy
      301 dmvvpfpdkp nldvtstmvq kgwnathmfr vaeefftslg lspmppefwa esmlekpadg
      361 revvchasaw dfynrkdfri kqctrvtmdq lstvhhemgh vqyylqykdl hvslrrganp
      421 gfheaigdvl alsvstpahl hkiglldrva ndiesdinyl lkmalekiaf lpfgylvdqw
      481 rwgvfsgrtp psrynydwwy lrtkyqgicp pvarnethfd agakfhipsv tpyiryfvsf
      541 vlqfqfhqal ckeaghqgpl hqcdiyqstk agaklqqvlq agcsrpwqev lkdlvgsdal
      601 dasalmeyfq pvsqwlqeqn qrngevlgwp eyqwrpplpd nypegidlet deakanrfve
      661 eydrtakvlw neyaeanwhy ntnitiegsk illqknkevs nhtlkygtwa ktfdvsnfqn
      721 stikriikkv qnvdravlpp neleeynqil ldmettysva nvcytngtcl slepdltnim
      781 atsrkyeell wvwkswrdkv grailpffpk yvdfsnkiak lngysdagds wrssyesddl
      841 eqdleklyqe lqplylnlha yvrrslhrhy gseyinldgp ipahllgnmw aqtwsniydl
      901 vapfpsapsi dateamikqg wtprrifkea dnfftslgll pvppefwnks mlekptdgre
      961 vvchasawdf yngkdfrikq ctsvnmeelv iahhemghiq yfmqykdlpv tfreganpgf
     1021 heaigdvlal svstpkhlhs lnllssegsg yehdinflmk maldkiafip fsylidqwrw
     1081 rvfdgsitke nynqewwslr lkyqglcppv prsqgdfdpg skfhvpanvp yiryfisfii
     1141 qfqfhealcr aaghtgplyk cdiyqskeag klladamklg yskqwpeamk iitgqpnmsa
     1201 saimnyfkpl tewlvtenrr hgetlgwpey twtpntarae gslpessrvn flgmylepqq
     1261 arvgqwvllf lgvallvatv glahrlynih nhhslrrphr gpqfgsevel rhs
//
LOCUS       NP_112396                492 aa            linear   ROD 27-APR-2025
DEFINITION  c-erbAalpha2 isoform TRalpha2 [Rattus norvegicus].
ACCESSION   NP_112396
VERSION     NP_112396.2
DBSOURCE    REFSEQ: accession NM_031134.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Fernandez,M., Pannella,M., Baldassarro,V.A., Flagelli,A.,
            Alastra,G., Giardino,L. and Calza,L.
  TITLE     Thyroid Hormone Signaling in Embryonic Stem Cells: Crosstalk with
            the Retinoic Acid Pathway
  JOURNAL   Int J Mol Sci 21 (23), 8945 (2020)
   PUBMED   33255695
  REMARK    GeneRIF: Thyroid Hormone Signaling in Embryonic Stem Cells:
            Crosstalk with the Retinoic Acid Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Benedetti,V., Lavecchia,A.M., Locatelli,M., Brizi,V., Corna,D.,
            Todeschini,M., Novelli,R., Benigni,A., Zoja,C., Remuzzi,G. and
            Xinaris,C.
  TITLE     Alteration of thyroid hormone signaling triggers the
            diabetes-induced pathological growth, remodeling, and
            dedifferentiation of podocytes
  JOURNAL   JCI Insight 4 (18), 130249 (2019)
   PUBMED   31534055
  REMARK    GeneRIF: Alteration of thyroid hormone signaling triggers the
            diabetes-induced pathological growth, remodeling, and
            dedifferentiation of podocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 492)
  AUTHORS   da Conceicao,R.R., Laureano-Melo,R., Oliveira,K.C., de Carvalho
            Melo,M.C., Kasamatsu,T.S., de Barros Maciel,R.M., de Souza,J.S. and
            Giannocco,G.
  TITLE     Antidepressant behavior in thyroidectomized Wistar rats is induced
            by hippocampal hypothyroidism
  JOURNAL   Physiol Behav 157, 158-164 (2016)
   PUBMED   26861177
  REMARK    GeneRIF: This study demonstrated that reduction of the thyroid
            hormone receptor alfa (Tralpha1)mRNA expression in hippocampus of
            thyroidectomized Wistar rats.
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Zheng,K., Sulieman,F.J., Li,J., Wei,Q., Xu,M. and Shi,F.
  TITLE     Nitric oxide and thyroid hormone receptor alpha 1 contribute to
            ovarian follicular development in immature hyper- and hypo-thyroid
            rats
  JOURNAL   Reprod Biol 15 (1), 27-33 (2015)
   PUBMED   25726374
  REMARK    GeneRIF: The roles of nitric oxide synthase and TRalph1 in
            hyperthyroid and hypothyroid rats are reported.
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Frau,C., Loi,R., Petrelli,A., Perra,A., Menegon,S., Kowalik,M.A.,
            Pinna,S., Leoni,V.P., Fornari,F., Gramantieri,L.,
            Ledda-Columbano,G.M., Giordano,S. and Columbano,A.
  TITLE     Local hypothyroidism favors the progression of preneoplastic
            lesions to hepatocellular carcinoma in rats
  JOURNAL   Hepatology 61 (1), 249-259 (2015)
   PUBMED   25156012
  REMARK    GeneRIF: down-regulated in hepatocellular carcinoma
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Koenig,R.J., Lazar,M.A., Hodin,R.A., Brent,G.A., Larsen,P.R.,
            Chin,W.W. and Moore,D.D.
  TITLE     Inhibition of thyroid hormone action by a non-hormone binding
            c-erbA protein generated by alternative mRNA splicing
  JOURNAL   Nature 337 (6208), 659-661 (1989)
   PUBMED   2537467
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Lazar,M.A., Hodin,R.A., Darling,D.S. and Chin,W.W.
  TITLE     Identification of a rat c-erbA alpha-related protein which binds
            deoxyribonucleic acid but does not bind thyroid hormone
  JOURNAL   Mol Endocrinol 2 (10), 893-901 (1988)
   PUBMED   2903438
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Izumo,S. and Mahdavi,V.
  TITLE     Thyroid hormone receptor alpha isoforms generated by alternative
            splicing differentially activate myosin HC gene transcription
  JOURNAL   Nature 334 (6182), 539-542 (1988)
   PUBMED   2841611
  REMARK    Erratum:[Nature 1988 Oct 20;335(6192):744]
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Lazar,M.A. and Chin,W.W.
  TITLE     Regulation of two c-erbA messenger ribonucleic acids in rat GH3
            cells by thyroid hormone
  JOURNAL   Mol Endocrinol 2 (6), 479-484 (1988)
   PUBMED   2901667
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Weinberger,C., Thompson,C.C., Ong,E.S., Lebo,R., Gruol,D.J. and
            Evans,R.M.
  TITLE     The c-erb-A gene encodes a thyroid hormone receptor
  JOURNAL   Nature 324 (6098), 641-646 (1986)
   PUBMED   2879243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M31174.1, CB580585.1 and AI764185.1.
            
            On May 6, 2005 this sequence version replaced NP_112396.1.
            
            Transcript Variant: This variant (TRalpha2) contains an alternate
            3' terminal exon compared to variant TRalpha1. The resulting
            protein (c-erbAalpha2, also known as TRalpha 2) has a distinct
            C-terminus compared to isoform TRalpha1, and fails to bind thyroid
            hormones or to trans-activate thyroid hormone responsive genes.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: M31174.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..492
                     /product="c-erbAalpha2 isoform TRalpha2"
                     /note="c-erbA-alpha2; c-erb-A thyroid hormone receptor;
                     thyroid hormone receptor alpha 1 (avian erythroblastic
                     leukemia viral (v-erb-a) oncogene homolog 1 formerly
                     ERBA1); c-erbAalpha2; C-erbA-alpha; nuclear receptor
                     subfamily 1 group A member 1"
                     /calculated_mol_wt=54897
     Region          1..52
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (P63059.1)"
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63059.1)"
     Region          52..138
                     /region_name="NR_DBD_TR"
                     /note="DNA-binding domain of thyroid hormone receptors
                     (TRs) is composed of two C4-type zinc fingers; cd06961"
                     /db_xref="CDD:143519"
     Site            order(53,56,70,73,91,97,107,110)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143519"
     Site            order(63..65,71..72,74,76,78..79,82,104..105,108,111,
                     124..126,131,134..135,137..138)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143519"
     Site            order(63,66,121,123..124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:143519"
     Region          162..370
                     /region_name="NR_LBD_TR"
                     /note="The ligand binding domain of thyroid hormone
                     receptor, a members of a superfamily of nuclear receptors;
                     cd06935"
                     /db_xref="CDD:132733"
     Site            order(215,218..219,221..222,225,228,256,259,263,275..277,
                     287,290,292,299)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132733"
     Region          457..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63059.1)"
     CDS             1..492
                     /gene="Thra"
                     /gene_synonym="c-erbA-1; ERBA1; Thra1"
                     /coded_by="NM_031134.2:303..1781"
                     /note="isoform TRalpha2 is encoded by transcript variant
                     TRalpha2"
                     /db_xref="GeneID:81812"
                     /db_xref="RGD:3857"
ORIGIN      
        1 meqkpskvec gsdpeensar spdgkrkrkn gqcplkssms gyipsyldkd eqcvvcgdka
       61 tgyhyrcitc egckgffrrt iqknlhptys ckydsccvid kitrnqcqlc rfkkciavgm
      121 amdlvlddsk rvakrklieq nrerrrkeem irslqqrpep tpeewdlihv ateahrstna
      181 qgshwkqrrk flpddigqsp ivsmpdgdkv dleafseftk iitpaitrvv dfakklpmfs
      241 elpcedqiil lkgccmeims lraavrydpe sdtltlsgem avkreqlkng glgvvsdaif
      301 elgkslsafn lddtevallq avllmstdrs gllcvdkiek sqeayllafe hyvnhrkhni
      361 phfwpkllmk erevqssily kgaaaegrpg gslgvhpegq qllgmhvvqg pqvrqleqqf
      421 geagslrgpv lqhqspkspq qrllellhrs gilhsravcg eddsseassl sssssdedte
      481 vcedlagkaa sp
//
LOCUS       NP_001030095             640 aa            linear   ROD 27-APR-2025
DEFINITION  tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like [Rattus
            norvegicus].
ACCESSION   NP_001030095 XP_217318
VERSION     NP_001030095.1
DBSOURCE    REFSEQ: accession NM_001034923.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105780.1.
            
            On Oct 21, 2005 this sequence version replaced XP_217318.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..640
                     /product="tRNA-dihydrouridine(47) synthase
                     [NAD(P)(+)]-like"
                     /EC_number="1.3.1.89"
                     /note="mRNA-dihydrouridine synthase DUS3L"
                     /calculated_mol_wt=71409
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRC5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96G46; propagated from
                     UniProtKB/Swiss-Prot (Q3KRC5.1)"
     Region          47..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRC5.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91XI1; propagated from
                     UniProtKB/Swiss-Prot (Q3KRC5.1)"
     Region          296..528
                     /region_name="DUS_like_FMN"
                     /note="Dihydrouridine synthase-like (DUS-like) FMN-binding
                     domain. Members of this family catalyze the reduction of
                     the 5,6-double bond of a uridine residue on tRNA.
                     Dihydrouridine modification of tRNA is widely observed in
                     prokaryotes and eukaryotes, and also...; cd02801"
                     /db_xref="CDD:239200"
     Site            order(300..302,326,355,383,425,455,487,489,510..511)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239200"
     Site            order(355,386..387,425,427,454..455,457..458,488..489,511)
                     /site_type="active"
                     /db_xref="CDD:239200"
     Site            order(386,427,455,457)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239200"
     Site            order(387,425,454,458,488..489)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239200"
     CDS             1..640
                     /gene="Dus3l"
                     /coded_by="NM_001034923.1:48..1970"
                     /db_xref="GeneID:301122"
                     /db_xref="RGD:1563228"
ORIGIN      
        1 maevaevaae sggggdsgvg acergvapik aqyrttkerf heyldadkqe gacqetpteg
       61 paepeakrir ledgqengkt evavesherq vpkrargqnk srphmkpahy dkerlcpsll
      121 qesatpcafg drcrflhdvg ryletkpadl gphcvlfntf grcpysmtcr fagahlgpeg
      181 qnlvqeevva rcaqlpsvrn gldralqqql rkrqvcfera eqalshltqg pmptiapest
      241 vatltpkhss chvqldnvgg dgarqgspvp tcgpltdedv vrlrpcekkr ldisgklyla
      301 plttcgnlpf rrickrfgad vtcgemamct nllqgqmsew allkrhpced ifgvqlegaf
      361 pdtmtkcael lnrtidvdfv dinvgcpidl vykkgggcal mnrsakfqqi vrgmnevldv
      421 pltvkmrtgv qervslahrl lpelrnwgva lvtlhgrsre qrytrladwp yieqcakvas
      481 pmplfgngdi lsfedancam qtgvagimva rgallkpwlf teikeqrhwd issserldil
      541 rdfthygleh wgsdtqgver trrfllewls flcryvpvgl lerlpqrine rppyylgrdy
      601 letlmasqqa adwiriseml lgpvppgfvf lpkhkanayk
//
LOCUS       NP_001002851             171 aa            linear   ROD 27-APR-2025
DEFINITION  neudesin precursor [Rattus norvegicus].
ACCESSION   NP_001002851 XP_213975
VERSION     NP_001002851.1
DBSOURCE    REFSEQ: accession NM_001002851.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Moutaoufik,M.T., Malty,R., Amin,S., Zhang,Q., Phanse,S.,
            Gagarinova,A., Zilocchi,M., Hoell,L., Minic,Z., Gagarinova,M.,
            Aoki,H., Stockwell,J., Jessulat,M., Goebels,F., Broderick,K.,
            Scott,N.E., Vlasblom,J., Musso,G., Prasad,B., Lamantea,E.,
            Garavaglia,B., Rajput,A., Murayama,K., Okazaki,Y., Foster,L.J.,
            Bader,G.D., Cayabyab,F.S. and Babu,M.
  TITLE     Rewiring of the Human Mitochondrial Interactome during Neuronal
            Reprogramming Reveals Regulators of the Respirasome and
            Neurogenesis
  JOURNAL   iScience 19, 1114-1132 (2019)
   PUBMED   31536960
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Byerly,M.S., Swanson,R.D., Semsarzadeh,N.N., McCulloh,P.S.,
            Kwon,K., Aja,S., Moran,T.H., Wong,G.W. and Blackshaw,S.
  TITLE     Identification of hypothalamic neuron-derived neurotrophic factor
            as a novel factor modulating appetite
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 304 (12), R1085-R1095 (2013)
   PUBMED   23576617
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Kimura,I., Yoshioka,M., Konishi,M., Miyake,A. and Itoh,N.
  TITLE     Neudesin, a novel secreted protein with a unique primary structure
            and neurotrophic activity
  JOURNAL   J Neurosci Res 79 (3), 287-294 (2005)
   PUBMED   15605373
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY623793.1.
            
            On Aug 30, 2004 this sequence version replaced XP_213975.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY623793.1, FM060032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..171
                     /product="neudesin precursor"
                     /note="neuron-derived neurotrophic factor; spinal cord
                     injury-related protein 10; secreted protein of unknown
                     function; Spinal cord injury related protein 10;
                     SCIRP10-related protein"
                     /calculated_mol_wt=15685
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3325
     mat_peptide     31..171
                     /product="Neudesin. /id=PRO_0000042834"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IUR5.1)"
                     /calculated_mol_wt=15685
     Region          47..109
                     /region_name="Cyt-b5"
                     /note="Cytochrome b5-like Heme/Steroid binding domain;
                     pfam00173"
                     /db_xref="CDD:459698"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMX5; propagated from
                     UniProtKB/Swiss-Prot (Q6IUR5.1)"
     Region          151..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IUR5.1)"
     CDS             1..171
                     /gene="Nenf"
                     /gene_synonym="SCIRP10; Spuf"
                     /coded_by="NM_001002851.1:20..535"
                     /db_xref="GeneID:289380"
                     /db_xref="RGD:1303289"
ORIGIN      
        1 marpapwwwl rplaalalal alvrvpsara gqmprpaerg ppvrlfteee larysgeeed
       61 qpiylavkgv vfdvtsgkef ygrgapynal agkdssrgva kmsldpadlt hdisgltake
      121 lealddifsk vykakypivg ytarrilned gspnldfkpe dqphfdikde f
//
LOCUS       NP_001007722             172 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial membrane protein 2 [Rattus norvegicus].
ACCESSION   NP_001007722 XP_340745
VERSION     NP_001007722.1
DBSOURCE    REFSEQ: accession NM_001007721.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Pan,J., Luo,X., Zhao,S., Li,J. and Jiang,Z.
  TITLE     miR-340-5p mediates the therapeutic effect of mesenchymal stem
            cells on corneal neovascularization
  JOURNAL   Graefes Arch Clin Exp Ophthalmol 260 (2), 497-507 (2022)
   PUBMED   34495369
  REMARK    GeneRIF: miR-340-5p mediates the therapeutic effect of mesenchymal
            stem cells on corneal neovascularization.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Gee,H.Y., Ashraf,S., Wan,X., Vega-Warner,V., Esteve-Rudd,J.,
            Lovric,S., Fang,H., Hurd,T.W., Sadowski,C.E., Allen,S.J.,
            Otto,E.A., Korkmaz,E., Washburn,J., Levy,S., Williams,D.S.,
            Bakkaloglu,S.A., Zolotnitskaya,A., Ozaltin,F., Zhou,W. and
            Hildebrandt,F.
  TITLE     Mutations in EMP2 cause childhood-onset nephrotic syndrome
  JOURNAL   Am J Hum Genet 94 (6), 884-890 (2014)
   PUBMED   24814193
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Gordon,L.K., Kiyohara,M., Fu,M., Braun,J., Dhawan,P., Chan,A.,
            Goodglick,L. and Wadehra,M.
  TITLE     EMP2 regulates angiogenesis in endometrial cancer cells through
            induction of VEGF
  JOURNAL   Oncogene 32 (46), 5369-5376 (2013)
   PUBMED   23334331
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Morales,S.A., Telander,D.G., Leon,D., Forward,K., Braun,J.,
            Wadehra,M. and Gordon,L.K.
  TITLE     Epithelial membrane protein 2 controls VEGF expression in ARPE-19
            cells
  JOURNAL   Invest Ophthalmol Vis Sci 54 (3), 2367-2372 (2013)
   PUBMED   23439602
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Morales,S.A., Telander,D.G., Mareninov,S., Nagy,A., Wadehra,M.,
            Braun,J. and Gordon,L.K.
  TITLE     Anti-EMP2 diabody blocks epithelial membrane protein 2 (EMP2) and
            FAK mediated collagen gel contraction in ARPE-19 cells
  JOURNAL   Exp Eye Res 102, 10-16 (2012)
   PUBMED   22728127
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Wadehra,M., Forbes,A., Pushkarna,N., Goodglick,L., Gordon,L.K.,
            Williams,C.J. and Braun,J.
  TITLE     Epithelial membrane protein-2 regulates surface expression of
            alphavbeta3 integrin in the endometrium
  JOURNAL   Dev Biol 287 (2), 336-345 (2005)
   PUBMED   16216233
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Wadehra,M., Goodglick,L. and Braun,J.
  TITLE     The tetraspan protein EMP2 modulates the surface expression of
            caveolins and glycosylphosphatidyl inositol-linked proteins
  JOURNAL   Mol Biol Cell 15 (5), 2073-2083 (2004)
   PUBMED   14978215
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Wadehra,M., Su,H., Gordon,L.K., Goodglick,L. and Braun,J.
  TITLE     The tetraspan protein EMP2 increases surface expression of class I
            major histocompatibility complex proteins and susceptibility to
            CTL-mediated cell death
  JOURNAL   Clin Immunol 107 (2), 129-136 (2003)
   PUBMED   12763482
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Wadehra,M., Iyer,R., Goodglick,L. and Braun,J.
  TITLE     The tetraspan protein epithelial membrane protein-2 interacts with
            beta1 integrins and regulates adhesion
  JOURNAL   J Biol Chem 277 (43), 41094-41100 (2002)
   PUBMED   12189152
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Wilson,H.L., Wilson,S.A., Surprenant,A. and North,R.A.
  TITLE     Epithelial membrane proteins induce membrane blebbing and interact
            with the P2X7 receptor C terminus
  JOURNAL   J Biol Chem 277 (37), 34017-34023 (2002)
   PUBMED   12107182
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081865.1.
            
            On Nov 29, 2004 this sequence version replaced XP_340745.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081865.1, CK478294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..172
                     /product="epithelial membrane protein 2"
                     /calculated_mol_wt=19518
     Region          1..165
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; pfam00822"
                     /db_xref="CDD:395662"
     Site            1..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HH2.1)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HH2.1)"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HH2.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HH2.1)"
     CDS             1..172
                     /gene="Emp2"
                     /gene_synonym="EMP-2"
                     /coded_by="NM_001007721.1:162..680"
                     /db_xref="GeneID:360468"
                     /db_xref="RGD:1359629"
ORIGIN      
        1 mlvilafiiv fhivstallf istidnawwv gdgfsadiwr vctnstncte indlssteef
       61 sgysvmqavq atmilstils cisflifllq lfrlkqgerf vltaiiqlms clcvmigasv
      121 ytdrrqdlhh qnsqlyyllq egsygysfil awvafaftfi sglmymilrk rk
//
LOCUS       NP_001013973             165 aa            linear   ROD 27-APR-2025
DEFINITION  UDP-N-acetylglucosamine transferase subunit ALG13 [Rattus
            norvegicus].
ACCESSION   NP_001013973 XP_217068
VERSION     NP_001013973.1
DBSOURCE    REFSEQ: accession NM_001013951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088233.1.
            
            On Apr 1, 2005 this sequence version replaced XP_217068.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088233.1, FQ229089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq34"
     Protein         1..165
                     /product="UDP-N-acetylglucosamine transferase subunit
                     ALG13"
                     /EC_number="2.4.1.141"
                     /note="UDP-N-acetylglucosamine transferase subunit ALG13
                     homolog; glycosyltransferase 28 domain-containing protein
                     1; asparagine-linked glycosylation 13 homolog"
                     /calculated_mol_wt=18198
     Region          5..153
                     /region_name="PssE"
                     /note="PssE/Cps14G family polysaccharide biosynthesis
                     glycosyltransferase; NF041548"
                     /db_xref="CDD:469433"
     CDS             1..165
                     /gene="Alg13l1"
                     /coded_by="NM_001013951.1:13..510"
                     /db_xref="GeneID:300284"
                     /db_xref="RGD:1359416"
ORIGIN      
        1 mkrafvtvgt tsfddlvarv vandtvqilk slgynhlvlq igrgtvvpep fstepftldv
       61 yrykeslked lqqadlvish agagsclesl ekgkplvvvv neklmnnhqf elakqlhkeg
      121 hlfyctcsml pgllqsmdls tlkcyppgqp ekfsafldkv vglqk
//
LOCUS       NP_037201                216 aa            linear   ROD 27-APR-2025
DEFINITION  H-2 class II histocompatibility antigen gamma chain [Rattus
            norvegicus].
ACCESSION   NP_037201
VERSION     NP_037201.1
DBSOURCE    REFSEQ: accession NM_013069.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Song,H., Zhu,Z., Zhou,Y., Du,N., Song,T., Liang,H., Chen,X.,
            Wang,Y., Wang,Y. and Hu,Y.
  TITLE     MIF/CD74 axis participates in inflammatory activation of Schwann
            cells following sciatic nerve injury
  JOURNAL   J Mol Histol 50 (4), 355-367 (2019)
   PUBMED   31197516
  REMARK    GeneRIF: macrophage migration inhibitory factor (MIF) was
            identified as a core regulator of inflammatory response following
            sciatic nerve injury through interaction with CD74 membrane
            receptor.
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Su,Y., Wang,Y., Zhou,Y., Zhu,Z., Zhang,Q., Zhang,X., Wang,W.,
            Gu,X., Guo,A. and Wang,Y.
  TITLE     Macrophage migration inhibitory factor activates inflammatory
            responses of astrocytes through interaction with CD74 receptor
  JOURNAL   Oncotarget 8 (2), 2719-2730 (2017)
   PUBMED   27926507
  REMARK    GeneRIF: cytokine MIF was able to elicit inflammatory response of
            astrocytes through interaction with CD74 receptor, and activation
            of ERK was necessary for the intracellular signal transduction.
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Wang,J., Lin,J., Schlotterer,A., Wu,L., Fleming,T., Busch,S.,
            Dietrich,N. and Hammes,H.P.
  TITLE     CD74 indicates microglial activation in experimental diabetic
            retinopathy and exogenous methylglyoxal mimics the response in
            normoglycemic retina
  JOURNAL   Acta Diabetol 51 (5), 813-821 (2014)
   PUBMED   24974304
  REMARK    GeneRIF: Methylglyoxal induced gene expression of CD74 in the in
            the diabetic retina.
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zhen,A., Krutzik,S.R., Levin,B.R., Kasparian,S., Zack,J.A. and
            Kitchen,S.G.
  TITLE     CD4 ligation on human blood monocytes triggers macrophage
            differentiation and enhances HIV infection
  JOURNAL   J Virol 88 (17), 9934-9946 (2014)
   PUBMED   24942581
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Xiong,C., Huang,B., Cun,Y., Aghdasi,B.G. and Zhou,Y.
  TITLE     Migration inhibitory factor enhances inflammation via CD74 in
            cartilage end plates with Modic type 1 changes on MRI
  JOURNAL   Clin Orthop Relat Res 472 (6), 1943-1954 (2014)
   PUBMED   24569872
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Ghosh,P., Amaya,M., Mellins,E. and Wiley,D.C.
  TITLE     The structure of an intermediate in class II MHC maturation: CLIP
            bound to HLA-DR3
  JOURNAL   Nature 378 (6556), 457-462 (1995)
   PUBMED   7477400
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Riberdy,J.M., Newcomb,J.R., Surman,M.J., Barbosa,J.A. and
            Cresswell,P.
  TITLE     HLA-DR molecules from an antigen-processing mutant cell line are
            associated with invariant chain peptides
  JOURNAL   Nature 360 (6403), 474-477 (1992)
   PUBMED   1448172
REFERENCE   8  (residues 1 to 216)
  AUTHORS   McKnight,A.J., Mason,D.W. and Barclay,A.N.
  TITLE     Sequence of a rat MHC class II-associated invariant chain cDNA
            clone containing a 64 amino acid thyroglobulin-like domain
  JOURNAL   Nucleic Acids Res 17 (10), 3983-3984 (1989)
   PUBMED   2499873
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Henkes,W., Syha,J. and Reske,K.
  TITLE     Nucleotide sequence of rat invariant gamma chain cDNA clone pLR
            gamma 34.3
  JOURNAL   Nucleic Acids Res 16 (24), 11822 (1988)
   PUBMED   3264906
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Sant,A.J., Cullen,S.E., Giacoletto,K.S. and Schwartz,B.D.
  TITLE     Invariant chain is the core protein of the Ia-associated
            chondroitin sulfate proteoglycan
  JOURNAL   J Exp Med 162 (6), 1916-1934 (1985)
   PUBMED   3864916
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB696567.1, BC059152.1 and CB611598.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ231756.1, FQ232412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..216
                     /product="H-2 class II histocompatibility antigen gamma
                     chain"
                     /note="ii; ia antigen-associated invariant chain; MHC
                     class II-associated invariant chain; Cd74 molecule, major
                     histocompatibility complex, class II invariant chain"
                     /calculated_mol_wt=24372
     Region          1..113
                     /region_name="MHC2-interact"
                     /note="CLIP, MHC2 interacting; pfam09307"
                     /db_xref="CDD:462750"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10247.2)"
     Site            31..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P10247.2)"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10247.2)"
     Region          120..185
                     /region_name="MHCassoc_trimer"
                     /note="Class II MHC-associated invariant chain
                     trimerization domain; pfam08831"
                     /db_xref="CDD:462614"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10247.2)"
     CDS             1..216
                     /gene="Cd74"
                     /gene_synonym="INVG34"
                     /coded_by="NM_013069.2:97..747"
                     /db_xref="GeneID:25599"
                     /db_xref="RGD:2313"
ORIGIN      
        1 mddqrdlisn heqlpilgqr arapesncnr gvlytsvsvl valllagqat tayflyqqqg
       61 rldkltvtsq nlqlenlrmk lpksakpvsp mrmatpllmr plsmdnmlqa pvknvtkygn
      121 mtqdhvmhll tksgpvnypq lkgsfpenlk hlknsmngld wkvfeswmkq wllfemskns
      181 leekqptqtp pkepldmedp ssglgvtkqd mgqmfl
//
LOCUS       NP_695210                342 aa            linear   ROD 27-APR-2025
DEFINITION  sideroflexin-5 [Rattus norvegicus].
ACCESSION   NP_695210
VERSION     NP_695210.1
DBSOURCE    REFSEQ: accession NM_153298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Kory,N., Wyant,G.A., Prakash,G., Uit de Bos,J., Bottanelli,F.,
            Pacold,M.E., Chan,S.H., Lewis,C.A., Wang,T., Keys,H.R., Guo,Y.E.
            and Sabatini,D.M.
  TITLE     SFXN1 is a mitochondrial serine transporter required for one-carbon
            metabolism
  JOURNAL   Science 362 (6416) (2018)
   PUBMED   30442778
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Miyake,S., Yamashita,T., Taniguchi,M., Tamatani,M., Sato,K. and
            Tohyama,M.
  TITLE     Identification and characterization of a novel mitochondrial
            tricarboxylate carrier
  JOURNAL   Biochem Biophys Res Commun 295 (2), 463-468 (2002)
   PUBMED   12150972
  REMARK    GeneRIF: identification and functional characterization and
            possible role in biosynthesis and bioenergetics in the brain
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB056724.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            17 bp suspected to be vector contamination from the 5' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB056724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..342
                     /product="sideroflexin-5"
                     /note="tricarboxylate carrier BBG-TCC; solute carrier
                     family 64 member 5"
                     /calculated_mol_wt=37173
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD0.1)"
     Region          28..342
                     /region_name="SFXNs"
                     /note="Sideroflexins; pfam03820"
                     /db_xref="CDD:461063"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD0.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD0.1)"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD0.1)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD0.1)"
     CDS             1..342
                     /gene="Sfxn5"
                     /gene_synonym="BBG-TCC; SLC64A5"
                     /coded_by="NM_153298.1:38..1066"
                     /db_xref="GeneID:261737"
                     /db_xref="RGD:628706"
ORIGIN      
        1 madtattasa asaaasasna ssdappfqlg kprfqqtsfy grfrhfldii dprtlfvtek
       61 rlreavqlle dykhgtlrpg vtneqlwsaq kikqailhpd tnekifmpfr msgyipfgtp
      121 ivvglllpnq tlastvfwqw lnqshnacvn yanrnatkps paskfiqgyl gavisavsia
      181 vglnvlvqka nkftpatrll vqrfvpfpav asanicnvvl mrygeleegi dvldadgnlv
      241 gsskiaarha lletaltrvv lpmpilvlpp ivmsmlekta llqarprlll pvhslvclaa
      301 fglalplais lfpqmseiet sqlepeiara tssrtvvynk gl
//
LOCUS       NP_001020318             336 aa            linear   ROD 27-APR-2025
DEFINITION  probable G-protein coupled receptor 160 [Rattus norvegicus].
ACCESSION   NP_001020318 XP_574913
VERSION     NP_001020318.1
DBSOURCE    REFSEQ: accession NM_001025147.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Samson,W.K., Salvemini,D. and Yosten,G.L.C.
  TITLE     Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise
  JOURNAL   Endocrinology 162 (8) (2021)
   PUBMED   34043767
  REMARK    GeneRIF: Overcoming Stress, Hunger, and Pain: Cocaine- and
            Amphetamine-Regulated Transcript Peptide's Promise.
            Review article
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082060.1.
            
            On Jul 1, 2005 this sequence version replaced XP_574913.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082060.1, CV120480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..336
                     /product="probable G-protein coupled receptor 160"
                     /calculated_mol_wt=38652
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     Site            273..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H29.1)"
     CDS             1..336
                     /gene="Gpr160"
                     /coded_by="NM_001025147.1:219..1229"
                     /db_xref="GeneID:499588"
                     /db_xref="RGD:1560200"
ORIGIN      
        1 mtalpskncs fqyqshqapr sldatcllll iilgkvllnv lilrvkrkdt swsfmeyfcf
       61 slalvdllll vnisvltyfr dfvvlgirft nyhiclltqi vsfaygflhy pvcslacidy
      121 wcnlsratkp ssrwqkllyl ltviltwisv layvlgdpai saslkthkts vnqcpsyvst
      181 qshwlslsml milsvaflis wqevvaliqa iriasyknka vlyfpfppht sytvspravl
      241 lprlivcflg twfpfvalqv lilslrvqip ayiemnvpwl yfvnsfliaa vywfnchkly
      301 wrdgmfpvdp finwkccfvp vhrlkqverp msiiic
//
LOCUS       NP_113698                414 aa            linear   ROD 27-APR-2025
DEFINITION  isocitrate dehydrogenase [NADP] cytoplasmic [Rattus norvegicus].
ACCESSION   NP_113698
VERSION     NP_113698.1
DBSOURCE    REFSEQ: accession NM_031510.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Sei,H., Hirade,N., Kamiya,K., Nakashima,F., Yoshitake,J., Kano,K.,
            Mishiro-Sato,E., Kikuchi,R., Uchida,K. and Shibata,T.
  TITLE     Isocitrate dehydrogenase 1 upregulation in urinary extracellular
            vesicles from proximal tubules of type 2 diabetic rats
  JOURNAL   FASEB J 38 (10), e23688 (2024)
   PUBMED   38780519
  REMARK    GeneRIF: Isocitrate dehydrogenase 1 upregulation in urinary
            extracellular vesicles from proximal tubules of type 2 diabetic
            rats.
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Clement,A., Doyen,M., Fauvelle,F., Hossu,G., Chen,B.,
            Barberi-Heyob,M., Hirtz,A., Stupar,V., Lamiral,Z., Pouget,C.,
            Gauchotte,G., Karcher,G., Beaumont,M., Verger,A. and Lemasson,B.
  TITLE     In vivo characterization of physiological and metabolic changes
            related to isocitrate dehydrogenase 1 mutation expcression by
            multiparametric MRI and MRS in a rat model with orthotopically
            grafted human-derived glioblastoma cell lines
  JOURNAL   NMR Biomed 34 (6), e4490 (2021)
   PUBMED   33599048
  REMARK    GeneRIF: In vivo characterization of physiological and metabolic
            changes related to isocitrate dehydrogenase 1 mutation expcression
            by multiparametric MRI and MRS in a rat model with orthotopically
            grafted human-derived glioblastoma cell lines.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Wang,T., Drill,E., Vakiani,E., Pak,L.M., Boerner,T., Askan,G.,
            Schvartzman,J.M., Simpson,A.L., Jarnagin,W.R. and Sigel,C.S.
  TITLE     Distinct histomorphological features are associated with IDH1
            mutation in intrahepatic cholangiocarcinoma
  JOURNAL   Hum Pathol 91, 19-25 (2019)
   PUBMED   31121195
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Al-Amodi,H.S.A.B., Nabih,E.S., Kamel,H.F.M., El Sayed,M.A. and
            Dwedar,I.A.M.
  TITLE     Wild-Type Isocitrate Dehydrogenase 1 Over-Expression is Related to
            Cancer Stem Cells Survival in Lung Adenocarcinoma
  JOURNAL   Cancer Invest 36 (3), 185-189 (2018)
   PUBMED   29537891
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Lee,J.H., Shin,D.H., Park,W.Y., Shin,N., Kim,A., Lee,H.J.,
            Kim,Y.K., Choi,K.U., Kim,J.Y., Yang,Y.I., Lee,C.H. and Sol,M.Y.
  TITLE     IDH1 R132C mutation is detected in clear cell hepatocellular
            carcinoma by pyrosequencing
  JOURNAL   World J Surg Oncol 15 (1), 82 (2017)
   PUBMED   28403884
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Jennings,G.T., Sechi,S., Stevenson,P.M., Tuckey,R.C., Parmelee,D.
            and McAlister-Henn,L.
  TITLE     Cytosolic NADP(+)-dependent isocitrate dehydrogenase. Isolation of
            rat cDNA and study of tissue-specific and developmental expression
            of mRNA
  JOURNAL   J Biol Chem 269 (37), 23128-23134 (1994)
   PUBMED   8083215
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Sechi,S., Parmelee,D., Roller,P.P. and Jennings,G.T.
  TITLE     Structural characterization of cytosolic NADP(+)-dependent
            isocitrate dehydrogenase from rat ovary
  JOURNAL   Enzyme Protein 48 (1), 27-36 (1994)
   PUBMED   7787968
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Bobyleva,V., Kneer,N., Bellei,M., Battelli,D. and Lardy,H.A.
  TITLE     Concerning the mechanism of increased thermogenesis in rats treated
            with dehydroepiandrosterone
  JOURNAL   J Bioenerg Biomembr 25 (3), 313-321 (1993)
   PUBMED   8349575
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Yasue,M., Serikawa,T. and Yamada,J.
  TITLE     Chromosomal assignments of 23 biochemical loci of the rat by using
            rat x mouse somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 57 (2-3), 142-148 (1991)
   PUBMED   1914521
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Nichols,E.A. and Ruddle,F.H.
  TITLE     Polymorphism and linkage of glutathione reductase in Mus musculus
  JOURNAL   Biochem Genet 13 (5-6), 323-329 (1975)
   PUBMED   1180875
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L35317.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L35317.1, FQ214242.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..414
                     /product="isocitrate dehydrogenase [NADP] cytoplasmic"
                     /EC_number="1.1.1.42"
                     /note="IDH; IDP; NADP(+)-specific ICDH; oxalosuccinate
                     decarboxylase; cytosolic NADP-isocitrate dehydrogenase;
                     Isocitrate dehydrogenase 1, soluble; isocitrate
                     dehydrogenase 1 (NADP+), soluble; isocitrate dehydrogenase
                     (NADP(+)) 1, cytosolic"
                     /calculated_mol_wt=46603
     Region          1..411
                     /region_name="PTZ00435"
                     /note="isocitrate dehydrogenase; Provisional"
                     /db_xref="CDD:240417"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O75874; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75874; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O88844; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            139
                     /site_type="other"
                     /note="Critical for catalysis. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P41562.1)"
     Site            212
                     /site_type="other"
                     /note="Critical for catalysis. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P41562.1)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O88844; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O88844; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            243
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O88844; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75874; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88844; propagated from
                     UniProtKB/Swiss-Prot (P41562.1)"
     CDS             1..414
                     /gene="Idh1"
                     /gene_synonym="IDPc"
                     /coded_by="NM_031510.1:30..1274"
                     /db_xref="GeneID:24479"
                     /db_xref="RGD:2862"
ORIGIN      
        1 msrkihggsv vemqgdemtr iiwelikekl ilpyveldlh sydlgienrd atndqvtkda
       61 aeaikkynvg vkcatitpde krveefklkq mwkspngtir nilggtvfre aiickniprl
      121 vtgwvkpiii grhaygdqyr atdfvvpgpg kveitytpkd gsqkvtylvh dfeegggvam
      181 gmynqdksie dfahssfqma lskgwplyls tkntilkkyd grfkdifqei ydkqykskfe
      241 aqkiwyehrl iddmvaqamk seggfiwack nydgdvqsds vaqgygslgm mtsvlicpdg
      301 ktveaeaahg tvtrhyrmyq kgqetstnpi asifawsrgl ahrakldnnt elsffanale
      361 evcietieag fmtkdlaaci kglpnvqrsd ylntfefmdk lgenlkakla qakl
//
LOCUS       NP_446214                424 aa            linear   ROD 27-APR-2025
DEFINITION  zona pellucida sperm-binding protein 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_446214 XP_346430
VERSION     NP_446214.1
DBSOURCE    REFSEQ: accession NM_053762.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Lv,C., Huang,H.L., Yi,D.J., Peng,T.L., Tan,H.J., Quan,R.P.,
            Deng,H.W. and Xiao,H.M.
  TITLE     Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the zona
            pellucida, resulting in zona absence and female infertility in
            ratsdagger
  JOURNAL   Biol Reprod 104 (6), 1262-1270 (2021)
   PUBMED   33624742
  REMARK    GeneRIF: Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the
            zona pellucida, resulting in zona absence and female infertility in
            ratsdagger.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Dai,C., Hu,L., Gong,F., Tan,Y., Cai,S., Zhang,S., Dai,J., Lu,C.,
            Chen,J., Chen,Y., Lu,G., Du,J. and Lin,G.
  TITLE     ZP2 pathogenic variants cause in vitro fertilization failure and
            female infertility
  JOURNAL   Genet Med 21 (2), 431-440 (2019)
   PUBMED   29895852
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Chen,T., Bian,Y., Liu,X., Zhao,S., Wu,K., Yan,L., Li,M., Yang,Z.,
            Liu,H., Zhao,H. and Chen,Z.J.
  TITLE     A Recurrent Missense Mutation in ZP3 Causes Empty Follicle Syndrome
            and Female Infertility
  JOURNAL   Am J Hum Genet 101 (3), 459-465 (2017)
   PUBMED   28886344
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Louros,N.N., Chrysina,E.D., Baltatzis,G.E., Patsouris,E.S.,
            Hamodrakas,S.J. and Iconomidou,V.A.
  TITLE     A common 'aggregation-prone' interface possibly participates in the
            self-assembly of human zona pellucida proteins
  JOURNAL   FEBS Lett 590 (5), 619-630 (2016)
   PUBMED   26879157
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Jose,O., Hernandez-Hernandez,O., Chirinos,M.,
            Gonzalez-Gonzalez,M.E., Larrea,F., Almanza,A., Felix,R., Darszon,A.
            and Trevino,C.L.
  TITLE     Recombinant human ZP3-induced sperm acrosome reaction: evidence for
            the involvement of T- and L-type voltage-gated calcium channels
  JOURNAL   Biochem Biophys Res Commun 395 (4), 530-534 (2010)
   PUBMED   20394732
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Cohen,N. and Wassarman,P.M.
  TITLE     Association of egg zona pellucida glycoprotein mZP3 with sperm
            protein sp56 during fertilization in mice
  JOURNAL   Int J Dev Biol 45 (3), 569-576 (2001)
   PUBMED   11417900
REFERENCE   7  (residues 1 to 424)
  AUTHORS   O'Toole,C.M., Arnoult,C., Darszon,A., Steinhardt,R.A. and
            Florman,H.M.
  TITLE     Ca(2+) entry through store-operated channels in mouse sperm is
            initiated by egg ZP3 and drives the acrosome reaction
  JOURNAL   Mol Biol Cell 11 (5), 1571-1584 (2000)
   PUBMED   10793136
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Akatsuka,K., Yoshida-Komiya,H., Tulsiani,D.R., Orgebin-Crist,M.C.,
            Hiroi,M. and Araki,Y.
  TITLE     Rat zona pellucida glycoproteins: molecular cloning and
            characterization of the three major components
  JOURNAL   Mol Reprod Dev 51 (4), 454-467 (1998)
   PUBMED   9820205
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Rankin,T.L., Tong,Z.B., Castle,P.E., Lee,E., Gore-Langton,R.,
            Nelson,L.M. and Dean,J.
  TITLE     Human ZP3 restores fertility in Zp3 null mice without affecting
            order-specific sperm binding
  JOURNAL   Development 125 (13), 2415-2424 (1998)
   PUBMED   9609824
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Lu,Q. and Shur,B.D.
  TITLE     Sperm from beta 1,4-galactosyltransferase-null mice are refractory
            to ZP3-induced acrosome reactions and penetrate the zona pellucida
            poorly
  JOURNAL   Development 124 (20), 4121-4131 (1997)
   PUBMED   9374408
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D78482.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346430.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D78482.1, BC127488.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132271,
                                           SAMD00132281 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..424
                     /product="zona pellucida sperm-binding protein 3
                     precursor"
                     /note="zona pellucida sperm-binding protein 3; zona
                     pellucida protein C; zona pellucida glycoprotein 3 (sperm
                     receptor); zona pellucida glycoprotein ZP3"
                     /calculated_mol_wt=43524
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2343
     mat_peptide     23..351
                     /product="Zona pellucida sperm-binding protein 3.
                     /id=PRO_0000041721"
                     /note="propagated from UniProtKB/Swiss-Prot (P97708.2)"
                     /calculated_mol_wt=35915
     Site            23
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            32
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            39
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P97708.2)"
     Region          45..304
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            155
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            162
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            304
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16342937; propagated from
                     UniProtKB/Swiss-Prot (P97708.2)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97708.2)"
     CDS             1..424
                     /gene="Zp3"
                     /gene_synonym="Zp-3"
                     /coded_by="NM_053762.1:30..1304"
                     /db_xref="GeneID:114639"
                     /db_xref="RGD:620606"
ORIGIN      
        1 mgpscllflc lllcggpelc ypqtqwllpg gtptpagsss pveveckeae lvvtarrdlf
       61 gtgklvqpgd ltlgsegcqp lvavdtdvvr lnaqlhecss gvqvtedalv ystfllhdpr
      121 pvnglsilrt nrvevpiecr yprqgnvssh piqptwvpfs atvsseekla fslrlmeedw
      181 ntekssptfh lgevahlqae vqtgshlplq lfvdhcvatp splpgqnssp hhfivdshgc
      241 lvdglsesfs afqvprprpe tlqftvdvfh fanssrntvy itchlkvapa nqipdklnka
      301 csfnktsqsw lpvegdadic dccsngncsn ssssefethe paqwstlvsr nrrhvtdead
      361 vtvgpliflg kandqavegw tssaqtsval glglatvafl tlaaivlgvt rmchtssylv
      421 slpq
//
LOCUS       NP_001034083             102 aa            linear   ROD 27-APR-2025
DEFINITION  small vasohibin-binding protein isoform a [Rattus norvegicus].
ACCESSION   NP_001034083 XP_342898
VERSION     NP_001034083.1
DBSOURCE    REFSEQ: accession NM_001038994.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Iqbal,Z., Tawamie,H., Ba,W., Reis,A., Halak,B.A., Sticht,H.,
            Uebe,S., Kasri,N.N., Riazuddin,S., van Bokhoven,H. and Abou
            Jamra,R.
  TITLE     Loss of function of SVBP leads to autosomal recessive intellectual
            disability, microcephaly, ataxia, and hypotonia
  JOURNAL   Genet Med 21 (8), 1790-1796 (2019)
   PUBMED   30607023
  REMARK    GeneRIF: Knocking down Svbp in rat primary hippocampal neurons led
            to a significant decrease in the number of excitatory synapses.
            SVBP is not only involved in angiogenesis, but also has vital
            functions in the central nervous system. Biallelic loss-of-function
            variants in SVBP lead to intellectual disability.
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Zhou,C., Yan,L., Zhang,W.H. and Liu,Z.
  TITLE     Structural basis of tubulin detyrosination by VASH2/SVBP
            heterodimer
  JOURNAL   Nat Commun 10 (1), 3212 (2019)
   PUBMED   31324789
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Adamopoulos,A., Landskron,L., Heidebrecht,T., Tsakou,F.,
            Bleijerveld,O.B., Altelaar,M., Nieuwenhuis,J., Celie,P.H.N.,
            Brummelkamp,T.R. and Perrakis,A.
  TITLE     Crystal structure of the tubulin tyrosine carboxypeptidase complex
            VASH1-SVBP
  JOURNAL   Nat Struct Mol Biol 26 (7), 567-570 (2019)
   PUBMED   31270470
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Wang,N., Bosc,C., Ryul Choi,S., Boulan,B., Peris,L., Olieric,N.,
            Bao,H., Krichen,F., Chen,L., Andrieux,A., Olieric,V., Moutin,M.J.,
            Steinmetz,M.O. and Huang,H.
  TITLE     Structural basis of tubulin detyrosination by the vasohibin-SVBP
            enzyme complex
  JOURNAL   Nat Struct Mol Biol 26 (7), 571-582 (2019)
   PUBMED   31235911
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Li,F., Hu,Y., Qi,S., Luo,X. and Yu,H.
  TITLE     Structural basis of tubulin detyrosination by vasohibins
  JOURNAL   Nat Struct Mol Biol 26 (7), 583-591 (2019)
   PUBMED   31235910
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Liao,S., Rajendraprasad,G., Wang,N., Eibes,S., Gao,J., Yu,H.,
            Wu,G., Tu,X., Huang,H., Barisic,M. and Xu,C.
  TITLE     Molecular basis of vasohibins-mediated detyrosination and its
            impact on spindle function and mitosis
  JOURNAL   Cell Res 29 (7), 533-547 (2019)
   PUBMED   31171830
  REMARK    Erratum:[Cell Res. 2019 Sep;29(9):778. doi:
            10.1038/s41422-019-0215-y. PMID: 31395957]
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Nieuwenhuis,J., Adamopoulos,A., Bleijerveld,O.B., Mazouzi,A.,
            Stickel,E., Celie,P., Altelaar,M., Knipscheer,P., Perrakis,A.,
            Blomen,V.A. and Brummelkamp,T.R.
  TITLE     Vasohibins encode tubulin detyrosinating activity
  JOURNAL   Science 358 (6369), 1453-1456 (2017)
   PUBMED   29146869
REFERENCE   8  (residues 1 to 102)
  AUTHORS   Aillaud,C., Bosc,C., Peris,L., Bosson,A., Heemeryck,P., Van
            Dijk,J., Le Friec,J., Boulan,B., Vossier,F., Sanman,L.E., Syed,S.,
            Amara,N., Coute,Y., Lafanechere,L., Denarier,E., Delphin,C.,
            Pelletier,L., Humbert,S., Bogyo,M., Andrieux,A., Rogowski,K. and
            Moutin,M.J.
  TITLE     Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate
            neuron differentiation
  JOURNAL   Science 358 (6369), 1448-1453 (2017)
   PUBMED   29146868
REFERENCE   9  (residues 1 to 102)
  AUTHORS   Suzuki,Y., Kobayashi,M., Miyashita,H., Ohta,H., Sonoda,H. and
            Sato,Y.
  TITLE     Isolation of a small vasohibin-binding protein (SVBP) and its role
            in vasohibin secretion
  JOURNAL   J Cell Sci 123 (Pt 18), 3094-3101 (2010)
   PUBMED   20736312
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BF559487.1 and
            BC099226.1.
            
            On Jan 12, 2006 this sequence version replaced XP_342898.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132297,
                              SAMD00155312 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..102
                     /product="small vasohibin-binding protein isoform a"
                     /note="coiled-coil domain-containing protein 23;
                     coiled-coil domain containing 23"
                     /calculated_mol_wt=11757
     Region          42..98
                     /region_name="CCDC23"
                     /note="Coiled-coil domain-containing protein 23;
                     pfam15674"
                     /db_xref="CDD:434848"
     CDS             1..102
                     /gene="Svbp"
                     /gene_synonym="Ccdc23; RGD1311232"
                     /coded_by="NM_001038994.2:124..432"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:362578"
                     /db_xref="RGD:1311232"
ORIGIN      
        1 mtavplcrkl rlrseetrlg phskvradqe afgsqtmdpp arkekskvke pafrvekakq
       61 ksaqqelkqr qraeiyalnr vmteleqqqf defckqmqpp ge
//
LOCUS       NP_446134                715 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent zinc metalloprotease YME1L1 [Rattus norvegicus].
ACCESSION   NP_446134
VERSION     NP_446134.2
DBSOURCE    REFSEQ: accession NM_053682.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Shi,H., Rampello,A.J. and Glynn,S.E.
  TITLE     Engineered AAA+ proteases reveal principles of proteolysis at the
            mitochondrial inner membrane
  JOURNAL   Nat Commun 7, 13301 (2016)
   PUBMED   27786171
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Hartmann,B., Wai,T., Hu,H., MacVicar,T., Musante,L.,
            Fischer-Zirnsak,B., Stenzel,W., Graf,R., van den Heuvel,L.,
            Ropers,H.H., Wienker,T.F., Hubner,C., Langer,T. and Kaindl,A.M.
  TITLE     Homozygous YME1L1 mutation causes mitochondriopathy with optic
            atrophy and mitochondrial network fragmentation
  JOURNAL   Elife 5, e16078 (2016)
   PUBMED   27495975
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Stiburek,L., Cesnekova,J., Kostkova,O., Fornuskova,D., Vinsova,K.,
            Wenchich,L., Houstek,J. and Zeman,J.
  TITLE     YME1L controls the accumulation of respiratory chain subunits and
            is required for apoptotic resistance, cristae morphogenesis, and
            cell proliferation
  JOURNAL   Mol Biol Cell 23 (6), 1010-1023 (2012)
   PUBMED   22262461
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Coppola,M., Pizzigoni,A., Banfi,S., Bassi,M.T., Casari,G. and
            Incerti,B.
  TITLE     Identification and characterization of YME1L1, a novel
            paraplegin-related gene
  JOURNAL   Genomics 66 (1), 48-54 (2000)
   PUBMED   10843804
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081751.1.
            
            On Sep 16, 2004 this sequence version replaced NP_446134.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081751.1, AF151784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..715
                     /product="ATP-dependent zinc metalloprotease YME1L1"
                     /note="ATP-dependent metalloprotease YME1L1; meg-4;
                     YME1-like protein 1; ATP-dependent metalloprotease FtsH1
                     homolog"
                     /calculated_mol_wt=79681
     Region          31..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925S8.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925S8.1)"
     Region          <274..709
                     /region_name="HflB"
                     /note="ATP-dependent Zn proteases [Posttranslational
                     modification, protein turnover, chaperones]; COG0465"
                     /db_xref="CDD:440233"
     CDS             1..715
                     /gene="Yme1l1"
                     /gene_synonym="FtsH1"
                     /coded_by="NM_053682.2:167..2314"
                     /db_xref="GeneID:114217"
                     /db_xref="RGD:620764"
ORIGIN      
        1 mfslsstvqp qvtvplshli nafhspknis vsvntsaspk qhrdtvaehe apssepvlnl
       61 rdlglselki gqtdklvenl lpgfykdkrv sscwhtshis aqsffenkyg hldmfstlrs
      121 sslyrqhpkt lqsicsdlqn fpvfiqsrgf ktlksrtrrl qstserlaea qniapsfvkg
      181 fllrdrgtdl esldklmktk nipevhqdaf ktgfaegflk aqaltqktnd slrrtrlilf
      241 vlllfgiygl lknpflsvrf rtttgldsav dpvqmknvtf ehvkgveeak qelqevvefl
      301 knpqkftvlg gklpkgillv gppgtgktll aravageadv pfyyasgsef demfvgvgas
      361 rirnlfreak anapcvifid eldsvggkri espmhpysrq tinqllaemd gfkpnegvii
      421 igatnfpeal dnalirpgrf dmqvtvprpd vkgrteilkw ylnkikfdks vdpeiiargt
      481 vgfsgaelen lvnqaalkaa vdgkemvtmk elefskdkil mgperrsvei dnknktitay
      541 hesghaiiay ytkdampink atimprgptl ghvsllpend rwnetraqll aqmdvsmggr
      601 vaeelifgtd hittgassdf dnatkiakrm vtkfgmsekl gvmtysdtgk lspetqsaie
      661 qeirillres yerakhilkt hakehknlae alltyetlda keiqivlegk klevr
//
LOCUS       NP_620188                746 aa            linear   ROD 27-APR-2025
DEFINITION  SNF-related serine/threonine-protein kinase [Rattus norvegicus].
ACCESSION   NP_620188 XP_237743
VERSION     NP_620188.1
DBSOURCE    REFSEQ: accession NM_138833.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Wang,Z.Y., Liu,X.X. and Deng,Y.F.
  TITLE     Negative feedback of SNRK to circ-SNRK regulates cardiac function
            post-myocardial infarction
  JOURNAL   Cell Death Differ 29 (4), 709-721 (2022)
   PUBMED   34621049
  REMARK    GeneRIF: Negative feedback of SNRK to circ-SNRK regulates cardiac
            function post-myocardial infarction.
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Kertesz,N., Samson,J., Debacker,C., Wu,H. and Labastie,M.C.
  TITLE     Cloning and characterization of human and mouse SNRK sucrose
            non-fermenting protein (SNF-1)-related kinases
  JOURNAL   Gene 294 (1-2), 13-24 (2002)
   PUBMED   12234663
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Lefebvre,D.L., Bai,Y., Shahmolky,N., Sharma,M., Poon,R.,
            Drucker,D.J. and Rosen,C.F.
  TITLE     Identification and characterization of a novel
            sucrose-non-fermenting protein kinase/AMP-activated protein
            kinase-related protein kinase, SNARK
  JOURNAL   Biochem J 355 (Pt 2), 297-305 (2001)
   PUBMED   11284715
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Yoshida,K., Yamada,M., Nishio,C., Konishi,A. and Hatanaka,H.
  TITLE     SNRK, a member of the SNF1 family, is related to low K(+)-induced
            apoptosis of cultured rat cerebellar granule neurons
  JOURNAL   Brain Res 873 (2), 274-282 (2000)
   PUBMED   10930554
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Becker,W., Heukelbach,J., Kentrup,H. and Joost,H.G.
  TITLE     Molecular cloning and characterization of a novel mammalian protein
            kinase harboring a homology domain that defines a subfamily of
            serine/threonine kinases
  JOURNAL   Eur J Biochem 235 (3), 736-743 (1996)
   PUBMED   8654423
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X89383.1.
            
            On Dec 17, 2003 this sequence version replaced XP_237743.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X89383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..746
                     /product="SNF-related serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /note="SNF1-related kinase"
                     /calculated_mol_wt=81497
     Region          12..269
                     /region_name="STKc_SNRK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     SNF1-related kinase; cd14074"
                     /db_xref="CDD:270976"
     Site            order(22..26,30,43,45,76,92..95,99,101..102,104,138..139,
                     141,143..144,146,157..158,161,175..179,181,211..214)
                     /site_type="active"
                     /db_xref="CDD:270976"
     Site            order(22..25,30,43,45,76,92..95,99,143..144,146,157..158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270976"
     Site            order(99,101..102,104,139,141,143,161,175..179,181,
                     211..214)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270976"
     Site            157..179
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270976"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1.
                     /evidence=ECO:0000250|UniProtKB:Q9NRH2; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Region          288..335
                     /region_name="UBA_SNRK"
                     /note="UBA domain of SNF-related serine/threonine-protein
                     kinase (SNRK) and similar proteins mainly found in
                     metazoa; cd14339"
                     /db_xref="CDD:270524"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Region          383..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63553.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRH2; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Region          494..638
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63553.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     Site            534
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDU5; propagated from
                     UniProtKB/Swiss-Prot (Q63553.1)"
     CDS             1..746
                     /gene="Snrk"
                     /coded_by="NM_138833.1:150..2390"
                     /db_xref="GeneID:170837"
                     /db_xref="RGD:69653"
ORIGIN      
        1 magfkrgydg kiaglydldk tlgrghfavv klarhvftge kvavkvidkt kldtlatghl
       61 fqevrcmklv qhpnivrlye vidtqtklyl ilelgdggdm fdyimkheeg lnedlakkyf
      121 aqivhaisyc hklhvvhrdl kpenvvffek qglvkltdfg fsnkfqpgkk lttscgslay
      181 sapeillgde ydapavdiws lgvilfmlvc gqppfqeand setltmimdc kytvpprvsa
      241 gcrdlitrml qrdpkrrasl eeieshpwlq gvdpspatky niplvsyknl seeehnsiiq
      301 rmvlgdiadr daivealetn rynhitatyf llaerilrek qekeiqtrsa spsnikaqfr
      361 qswptkidvp qdleddltat plshatvpqs paragdsvln ghrskglcdp akkdelpela
      421 gpalstvppa slkpaasgrk clfrveedee edeedkkpvs lstqvvlrrk psvtnrltsr
      481 ksapvlnqif eegesddefd mdenlppkls rlkmniaspg tvhkryhrrk sqgrgsscss
      541 setsdddses rrrldkdsgl ayswhrrdss egppgsegdg ggqskpsggg gvdkaspgeq
      601 gtggsgqggs ggtpsgtags srrcagpdss ssspasaapr gaelvqslkl vslclgsqlh
      661 gakyildpqk allssvkvqe rstwkmcisa pgpgpsadld pvrtkklrnn vlqlplcekt
      721 isvniqrsrk egllcasspa scchvi
//
LOCUS       NP_001006957             488 aa            linear   ROD 27-APR-2025
DEFINITION  katanin p60 ATPase-containing subunit A-like 1 [Rattus norvegicus].
ACCESSION   NP_001006957 XP_213698
VERSION     NP_001006957.1
DBSOURCE    REFSEQ: accession NM_001006956.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Cheung,K., Senese,S., Kuang,J., Bui,N., Ongpipattanakul,C.,
            Gholkar,A., Cohn,W., Capri,J., Whitelegge,J.P. and Torres,J.Z.
  TITLE     Proteomic Analysis of the Mammalian Katanin Family of
            Microtubule-severing Enzymes Defines Katanin p80 subunit B-like 1
            (KATNBL1) as a Regulator of Mammalian Katanin Microtubule-severing
  JOURNAL   Mol Cell Proteomics 15 (5), 1658-1669 (2016)
   PUBMED   26929214
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Smith,L.B., Milne,L., Nelson,N., Eddie,S., Brown,P., Atanassova,N.,
            O'Bryan,M.K., O'Donnell,L., Rhodes,D., Wells,S., Napper,D.,
            Nolan,P., Lalanne,Z., Cheeseman,M. and Peters,J.
  TITLE     KATNAL1 regulation of sertoli cell microtubule dynamics is
            essential for spermiogenesis and male fertility
  JOURNAL   PLoS Genet 8 (5), e1002697 (2012)
   PUBMED   22654668
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083673.1.
            
            On Nov 22, 2004 this sequence version replaced XP_213698.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083673.1, SRR8487231.74245.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMD00132277
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..488
                     /product="katanin p60 ATPase-containing subunit A-like 1"
                     /EC_number="5.6.1.1"
                     /note="p60 katanin-like 1; katanin p60 subunit A-like 1;
                     katanin p60 ATPase-containing subunit A-like 1-like"
                     /calculated_mol_wt=55070
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW62; propagated from
                     UniProtKB/Swiss-Prot (Q5XIK7.1)"
     Region          4..72
                     /region_name="Kp60-NTD"
                     /note="N-terminal domain (NTD) found in katanin p60 (Kp60)
                     ATPase-containing subunit A1, and similar proteins;
                     cd21748"
                     /db_xref="CDD:439297"
     Site            order(7,14,17..20,22,29,51,55,58..59,61..62,65..66,68..69,
                     72)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439297"
     Region          52..452
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          128..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIK7.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIK7.1)"
     Region          207..376
                     /region_name="RecA-like_KTNA1"
                     /note="Katanin p60 ATPase-containing subunit A1; cd19522"
                     /db_xref="CDD:410930"
     Site            order(208..211,248..254)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:410930"
     Region          <448..486
                     /region_name="Vps4_C"
                     /note="Vps4 C terminal oligomerization domain; pfam09336"
                     /db_xref="CDD:462762"
     CDS             1..488
                     /gene="Katnal1"
                     /coded_by="NM_001006956.1:81..1547"
                     /db_xref="GeneID:288449"
                     /db_xref="RGD:1359252"
ORIGIN      
        1 mnlaeicena kkgreyallg nydssmvyyq gviqqiqrhc qslrdpatka kwqqvrqell
       61 eeyeqvksiv stlesfkmdk ppdfpvscrd epfrdpavwp ppvpaehrap pqirrpnrev
      121 rplrkdmgag arglvgrahq isksdkaasr dkdyrargrd dkarknmqdg asdgeipkfd
      181 gagydkdlve alerdivsrn psihwddiad leeakkllre avvlpmwmpd ffkgirrpwk
      241 gvlmvgppgt gktmlakava tecgttffnv ssstltskyr geseklvrll femarfyapt
      301 tifideidsi csrrgtsdeh easrrvksel liqmdgvgga lenddpskmv mvlaatnfpw
      361 didealrrrl ekriyiplpt akgraellki slreveldpd ihlediaekt egysgaditn
      421 icrdaslmam rrringlspe eiralskeel qmpvtrgdle lalkkiaksv saadlekyek
      481 wmvefgsa
//
LOCUS       NP_037006               2338 aa            linear   ROD 27-APR-2025
DEFINITION  proto-oncogene tyrosine-protein kinase ROS precursor [Rattus
            norvegicus].
ACCESSION   NP_037006
VERSION     NP_037006.1
DBSOURCE    REFSEQ: accession NM_012874.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2338)
  AUTHORS   Oguz,N., Kirca,M., Cetin,A. and Yesilkaya,A.
  TITLE     Effect of uric acid on inflammatory COX-2 and ROS pathways in
            vascular smooth muscle cells
  JOURNAL   J Recept Signal Transduct Res 37 (5), 500-505 (2017)
   PUBMED   28770648
  REMARK    GeneRIF: Uric acid plays an important role in CVD pathogenesis by
            inducing inflammatory COX-2 and ROS pathways. This is the first
            study demonstrating losartan's ability to reduce uric-acid-induced
            COX-2 elevation.
REFERENCE   2  (residues 1 to 2338)
  AUTHORS   Yovchev,M.I., Grozdanov,P.N., Joseph,B., Gupta,S. and Dabeva,M.D.
  TITLE     Novel hepatic progenitor cell surface markers in the adult rat
            liver
  JOURNAL   Hepatology 45 (1), 139-149 (2007)
   PUBMED   17187413
  REMARK    GeneRIF: We identified novel cell surface markers specific for
            hepatic progenitor/oval cells. Six are unique for the adult
            progenitors (CD133, claudin-7, cadherin 22, mucin-1, ros-1, Gabrp).
REFERENCE   3  (residues 1 to 2338)
  AUTHORS   Charest,A., Wilker,E.W., McLaughlin,M.E., Lane,K., Gowda,R.,
            Coven,S., McMahon,K., Kovach,S., Feng,Y., Yaffe,M.B., Jacks,T. and
            Housman,D.
  TITLE     ROS fusion tyrosine kinase activates a SH2 domain-containing
            phosphatase-2/phosphatidylinositol 3-kinase/mammalian target of
            rapamycin signaling axis to form glioblastoma in mice
  JOURNAL   Cancer Res 66 (15), 7473-7481 (2006)
   PUBMED   16885344
REFERENCE   4  (residues 1 to 2338)
  AUTHORS   Xu,Y., Yeung,C.H., Setiawan,I., Avram,C., Biber,J., Wagenfeld,A.,
            Lang,F. and Cooper,T.G.
  TITLE     Sodium-inorganic phosphate cotransporter NaPi-IIb in the epididymis
            and its potential role in male fertility studied in a transgenic
            mouse model
  JOURNAL   Biol Reprod 69 (4), 1135-1141 (2003)
   PUBMED   12773415
REFERENCE   5  (residues 1 to 2338)
  AUTHORS   Keilhack,H., Muller,M., Bohmer,S.A., Frank,C., Weidner,K.M.,
            Birchmeier,W., Ligensa,T., Berndt,A., Kosmehl,H., Gunther,B.,
            Muller,T., Birchmeier,C. and Bohmer,F.D.
  TITLE     Negative regulation of Ros receptor tyrosine kinase signaling. An
            epithelial function of the SH2 domain protein tyrosine phosphatase
            SHP-1
  JOURNAL   J Cell Biol 152 (2), 325-334 (2001)
   PUBMED   11266449
REFERENCE   6  (residues 1 to 2338)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 2338)
  AUTHORS   Sonnenberg-Riethmacher,E., Walter,B., Riethmacher,D., Godecke,S.
            and Birchmeier,C.
  TITLE     The c-ros tyrosine kinase receptor controls regionalization and
            differentiation of epithelial cells in the epididymis
  JOURNAL   Genes Dev 10 (10), 1184-1193 (1996)
   PUBMED   8675006
REFERENCE   8  (residues 1 to 2338)
  AUTHORS   Riethmacher,D., Langholz,O., Godecke,S., Sachs,M. and Birchmeier,C.
  TITLE     Biochemical and functional characterization of the murine ros
            protooncogene
  JOURNAL   Oncogene 9 (12), 3617-3626 (1994)
   PUBMED   7970722
REFERENCE   9  (residues 1 to 2338)
  AUTHORS   Chen,F., Cooney,A.J., Wang,Y., Law,S.W. and O'Malley,B.W.
  TITLE     Cloning of a novel orphan receptor (GCNF) expressed during germ
            cell development
  JOURNAL   Mol Endocrinol 8 (10), 1434-1444 (1994)
   PUBMED   7854358
REFERENCE   10 (residues 1 to 2338)
  AUTHORS   Matsushime,H. and Shibuya,M.
  TITLE     Tissue-specific expression of rat c-ros-1 gene and partial
            structural similarity of its predicted products with sev protein of
            Drosophila melanogaster
  JOURNAL   J Virol 64 (5), 2117-2125 (1990)
   PUBMED   2139140
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M35106.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M35106.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132281,
                                           SAMD00132297 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2338
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..2338
                     /product="proto-oncogene tyrosine-protein kinase ROS
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="proto-oncogene tyrosine-protein kinase ROS;
                     proto-oncogene tyrosine-protein kinase ROS-like; c-ros-1;
                     proto-oncogene c-Ros-1; v-ros UR2 sarcoma virus oncogene
                     homolog 1; heart - derived c - ros - 1 proto - oncogene;
                     Ros1 proto-oncogene; c-Ros receptor tyrosine kinase;
                     receptor tyrosine kinase c-ros oncogene 1; c-ros oncogene
                     1, receptor tyrosine kinase"
                     /calculated_mol_wt=258617
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
                     /calculated_mol_wt=3058
     mat_peptide     28..2338
                     /product="Proto-oncogene tyrosine-protein kinase ROS.
                     /id=PRO_0000278116"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63132.1)"
                     /calculated_mol_wt=258617
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Region          <99..>296
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Region          567..663
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(567,636,651)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            623
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            order(652..653,655..656)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            934
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            1010
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Region          1036..1142
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1036,1115,1130)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1131..1132,1134..1135)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Region          1448..1526
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          1550..1629
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Region          1649..1740
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Site            order(1729..1730,1732..1733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1745..1838
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1830..1831,1833..1834)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1854..1874
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63132.1)"
     Region          1947..2208
                     /region_name="PTKc_c-ros"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     C-ros; cd05044"
                     /db_xref="CDD:270640"
     Site            order(1947,1951,1970,1972,2018..2021,2024..2025,2071,
                     2075..2076,2078,2094,2112..2116,2125,2159)
                     /site_type="active"
                     /db_xref="CDD:270640"
     Site            order(1947,1951,1970,1972,2018..2021,2024..2025,
                     2075..2076,2078,2094)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270640"
     Site            order(2071,2075,2112..2116,2125,2159)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270640"
     Site            2093..2118
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270640"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P08922; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     Region          2277..2314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63132.1)"
     Site            2325
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P08922; propagated from
                     UniProtKB/Swiss-Prot (Q63132.1)"
     CDS             1..2338
                     /gene="Ros1"
                     /gene_synonym="ROS1C"
                     /coded_by="NM_012874.1:402..7418"
                     /db_xref="GeneID:25346"
                     /db_xref="RGD:3591"
ORIGIN      
        1 mkrirwltpk patfvvlgcv wisvaqgtil sscltscvtn lgrqldsgtr ynlseaciqg
       61 cqfwnsidqe kcalkcndty vticeresce vgcsnaegsy eeevldntel ptapfassig
      121 sngvtlrwnp anisgvkyii qwkyaqlpgs waytetvskl symveplhpf teyifrvvwi
      181 ftaqlhlysp pspsyrthpy gvpetapfit niessspdtv evswappyfp ggpilgynlr
      241 lisktqklds gtqrtsfqfy stlpnttyrf siaavnevge gpeaesmitt pspavqeeeq
      301 wlflsrktsl rkrslkylvd eahclwsdai rhnitgisvn tqqevvyfse gtiiwmkgaa
      361 nmsdvsdlri fyrgsalvss isvdwlyqrm yfimdnrvhv cdlkhcsnle eitpfsivap
      421 qkvvvdsyng yvfyllrdgi yrvhlplpsv rdtkavrive sgtlkdfavk pqskriiyfn
      481 gtmqvfmstf ldgsafhrvl pwvpladvks facenndfli tdgkaifqqd slsfnefivg
      541 cdlshieefg fgnlvifgss vqsyplpghp qevsvlfgsr ealiqwkppi laigaspsaw
      601 qnwtyevkvs sqdilettqv flnisrtvln vpklqsstky mvsvrasspk gpgpwsepsv
      661 gttlvpatep pfimavkedg lwskplssfg pgeflssdvg nvsdmdwynn slyysdtkgn
      721 vyvrplngmd isenyhissi agacalafew lghflywagk tyviqrqsvl tghtdivthv
      781 kllvndmavd pvggylywtt lysvestrln gesslvlqaq pwlsgkkvia ltldlsdgll
      841 ywlvqdnqci hlytavlrgw sgadatitef aawstseisq nalmyysgrl fwingfriit
      901 aqeigqrtsv svsepgkfnq ftiiqtslkp lpgnfsstpt vipdsvqess frieghtssf
      961 rilwneppav dwgivfysve fsahskflai eqqslpvftv eglepyalfn lsvtpytywg
     1021 kgqktslsfr apesvpsape nprifilslg rytrknevvv efrwnkpkhe ngvltkseif
     1081 yhiskqsgtn kstedwvsvs vtppvmsfql eamspgyivs fqvrvftskg pgpfsdivms
     1141 ktseikpcpy lisllgnkie fldmdqnqvv wtfslegavs tvgytaddem gyfaqgdalf
     1201 llnlhnhsss klfqdvlasd iaviavdwia rhlyfalkas qdgtqifdvd lehkvkspre
     1261 vkickshtai isfsmyplls rlywtevsdl gyqmfycnis shtlhhvlqp kasnqhgrrq
     1321 cscnvtesel sgamtvdtsd pdrpwiyftk qqeiwamdle gcqcwkvimv patpgkriis
     1381 ltvdgefiyw ittmkddtei yqakkgsgai lsqvkaprsk hilayssalq pfpdkaylsv
     1441 asnmveasil natntslilk lppvktnltw hgittptsty lvyymeanra nssdrkhnml
     1501 esqenvarie glqpfstyvi qiavknyysd plehlslgke iqgktksgvp gavchinatv
     1561 lsdtsllvfw teshkpngpk elvryqlvms ylapipetpl rqdefpsarl sllvtklsgg
     1621 qqyvlkilac hseemwctes hpvsvnmfdt pekpsalvpe ntsllldwka psnanltrfw
     1681 felqkwkyse fyhvkascsq gpvyvcnian lqpytpynir vvvvyttgen sssipesfkt
     1741 kagvpskpgi pkllegskns iqwekaedng nrlmyytlev rksisndsrd qslrwtavfn
     1801 gscssictwr sknlkgtfqf ravasnaigf geyseisedi tlvedgfwit etsfiltiiv
     1861 giflvatvpl tfvwhrslkn hkatkeglsv lndndqelae lrglaagvgl anacyavhtl
     1921 ptqeeieslp afpreklslr lllgsgafge vyegtavdil grgsgeikva vktlkkgstd
     1981 qekieflkea hlmskfnhpn ilkqlgvcll sepqyiilel meggdllsyl rkargttlsg
     2041 plltladlve lcvdiskgcv yleqmhfihr dlaarnclvs vkdytsprvv kigdfglare
     2101 iykhdyyrkr gegllpvrwm apenlmdgif tsqsdvwsfg ilvweiltlg hqpypahsnl
     2161 dvlnyvqagg rlepprncpd dlwnlmfrcw aqepdqrptf yniqdqlqlf rnvslnnvsh
     2221 cgqaapaggv inkgfegedn ematlnsddt mpvalmetrn qeglnymvla tkcsqsedry
     2281 egplgskesg lhdlkkderq padkdfcqqp qvaygspghs eglnyaclah sghgdvse
//
LOCUS       NP_001012127             384 aa            linear   ROD 27-APR-2025
DEFINITION  MAP kinase-activated protein kinase 3 [Rattus norvegicus].
ACCESSION   NP_001012127 XP_236618
VERSION     NP_001012127.1
DBSOURCE    REFSEQ: accession NM_001012127.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Zaru,R., Ronkina,N., Gaestel,M., Arthur,J.S. and Watts,C.
  TITLE     The MAPK-activated kinase Rsk controls an acute Toll-like receptor
            signaling response in dendritic cells and is activated through two
            distinct pathways
  JOURNAL   Nat Immunol 8 (11), 1227-1235 (2007)
   PUBMED   17906627
  REMARK    Erratum:[Nat Immunol. 2008 Jan;9(1):105]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Gaestel,M.
  TITLE     MAPKAP kinases - MKs - two's company, three's a crowd
  JOURNAL   Nat Rev Mol Cell Biol 7 (2), 120-130 (2006)
   PUBMED   16421520
  REMARK    Review article
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Eyers,C.E., McNeill,H., Knebel,A., Morrice,N., Arthur,S.J.,
            Cuenda,A. and Cohen,P.
  TITLE     The phosphorylation of CapZ-interacting protein (CapZIP) by
            stress-activated protein kinases triggers its dissociation from
            CapZ
  JOURNAL   Biochem J 389 (Pt 1), 127-135 (2005)
   PUBMED   15850461
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Clifton,A.D., Young,P.R. and Cohen,P.
  TITLE     A comparison of the substrate specificity of MAPKAP kinase-2 and
            MAPKAP kinase-3 and their activation by cytokines and cellular
            stress
  JOURNAL   FEBS Lett 392 (3), 209-214 (1996)
   PUBMED   8774846
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081974.1.
            
            On Feb 11, 2005 this sequence version replaced XP_236618.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081974.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132264,
                                           SAMD00132274 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..384
                     /product="MAP kinase-activated protein kinase 3"
                     /EC_number="2.7.11.1"
                     /note="MAPKAPK-3; MAPKAP kinase 3; mitogen-activated
                     protein kinase-activated protein kinase 3"
                     /calculated_mol_wt=43091
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q16644; propagated from
                     UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          41..306
                     /region_name="STKc_MAPKAPK3"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     3; cd14172"
                     /db_xref="CDD:271074"
     Site            order(52..57,60,73,75,100,120..123,127,129,167..168,170,
                     172..173,175,188..189,192,205..209,211)
                     /site_type="active"
                     /db_xref="CDD:271074"
     Site            order(52..57,60,73,75,100,120..123,173,175,188..189)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271074"
     Site            order(54..57,59,208..212,216,218,221,242,244..247,
                     261..262,264..265,289..290)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271074"
     Site            order(56,127,129,167..168,170,172,192,205..209,211)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271074"
     Site            order(188..197,199..209)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271074"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q3UMW7; propagated from
                     UniProtKB/Swiss-Prot (Q66H84.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          309..345
                     /region_name="Autoinhibitory helix. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q66H84.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          337..346
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          347..371
                     /region_name="p38 MAPK-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          352..355
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          359..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     Region          366..370
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H84.1)"
     CDS             1..384
                     /gene="Mapkapk3"
                     /gene_synonym="MAPKAP-K3; MK-3"
                     /coded_by="NM_001012127.1:284..1438"
                     /db_xref="GeneID:315994"
                     /db_xref="RGD:1304980"
ORIGIN      
        1 mdgetagekg slvpqpgalg apalggapap gvrrepkkya vtddyqlskq vlglgvngkv
       61 lecyhrrsgq kcalkllyds pkarqevdhh wqasggphiv rildvyenmh hgkrcllivm
      121 ecmeggelfs riqergdqaf tereaaeimr digtaiqflh sqniahrdvk penllytske
      181 kdavlkltdf gfakettqna lqtpcytpyy vapevlgpek ydkscdmwsl gvimyillcg
      241 fppfysntgq aispgmkrri rlgqygfpkp ewadvsedak qlirlllktd pterltimqf
      301 mnhpwinqsm evpqtplhta rvleedkdhw ddvkeemtsa latmrvdydq vkikdlktsn
      361 nrllnkrrkk qggsssaspg cnnq
//
LOCUS       NP_001102390             436 aa            linear   ROD 27-APR-2025
DEFINITION  T-box transcription factor TBX6 [Rattus norvegicus].
ACCESSION   NP_001102390 XP_001080027 XP_344964
VERSION     NP_001102390.1
DBSOURCE    REFSEQ: accession NM_001108920.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Chen,M., Maloney,J.A., Kallop,D.Y., Atwal,J.K., Tam,S.J., Baer,K.,
            Kissel,H., Kaminker,J.S., Lewcock,J.W., Weimer,R.M. and Watts,R.J.
  TITLE     Spatially coordinated kinase signaling regulates local axon
            degeneration
  JOURNAL   J Neurosci 32 (39), 13439-13453 (2012)
   PUBMED   23015435
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Chalamalasetty,R.B., Dunty,W.C. Jr., Biris,K.K., Ajima,R.,
            Iacovino,M., Beisaw,A., Feigenbaum,L., Chapman,D.L., Yoon,J.K.,
            Kyba,M. and Yamaguchi,T.P.
  TITLE     The Wnt3a/beta-catenin target gene Mesogenin1 controls the
            segmentation clock by activating a Notch signalling program
  JOURNAL   Nat Commun 2, 390 (2011)
   PUBMED   21750544
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Pereira,L.A., Wong,M.S., Lim,S.M., Sides,A., Stanley,E.G. and
            Elefanty,A.G.
  TITLE     Brachyury and related Tbx proteins interact with the Mixl1
            homeodomain protein and negatively regulate Mixl1 transcriptional
            activity
  JOURNAL   PLoS One 6 (12), e28394 (2011)
   PUBMED   22164283
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Takahashi,J., Ohbayashi,A., Oginuma,M., Saito,D., Mochizuki,A.,
            Saga,Y. and Takada,S.
  TITLE     Analysis of Ripply1/2-deficient mouse embryos reveals a mechanism
            underlying the rostro-caudal patterning within a somite
  JOURNAL   Dev Biol 342 (2), 134-145 (2010)
   PUBMED   20346937
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Lee,D., Park,C., Lee,H., Lugus,J.J., Kim,S.H., Arentson,E.,
            Chung,Y.S., Gomez,G., Kyba,M., Lin,S., Janknecht,R., Lim,D.S. and
            Choi,K.
  TITLE     ER71 acts downstream of BMP, Notch, and Wnt signaling in blood and
            vessel progenitor specification
  JOURNAL   Cell Stem Cell 2 (5), 497-507 (2008)
   PUBMED   18462699
REFERENCE   6  (residues 1 to 436)
  AUTHORS   White,P.H. and Chapman,D.L.
  TITLE     Dll1 is a downstream target of Tbx6 in the paraxial mesoderm
  JOURNAL   Genesis 42 (3), 193-202 (2005)
   PUBMED   15986483
REFERENCE   7  (residues 1 to 436)
  AUTHORS   White,P.H., Farkas,D.R. and Chapman,D.L.
  TITLE     Regulation of Tbx6 expression by Notch signaling
  JOURNAL   Genesis 42 (2), 61-70 (2005)
   PUBMED   15864811
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Garcia-Garcia,M.J., Eggenschwiler,J.T., Caspary,T., Alcorn,H.L.,
            Wyler,M.R., Huangfu,D., Rakeman,A.S., Lee,J.D., Feinberg,E.H.,
            Timmer,J.R. and Anderson,K.V.
  TITLE     Analysis of mouse embryonic patterning and morphogenesis by forward
            genetics
  JOURNAL   Proc Natl Acad Sci U S A 102 (17), 5913-5919 (2005)
   PUBMED   15755804
REFERENCE   9  (residues 1 to 436)
  AUTHORS   White,P.H., Farkas,D.R., McFadden,E.E. and Chapman,D.L.
  TITLE     Defective somite patterning in mouse embryos with reduced levels of
            Tbx6
  JOURNAL   Development 130 (8), 1681-1690 (2003)
   PUBMED   12620991
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Chapman,D.L. and Papaioannou,V.E.
  TITLE     Three neural tubes in mouse embryos with mutations in the T-box
            gene Tbx6
  JOURNAL   Nature 391 (6668), 695-697 (1998)
   PUBMED   9490412
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473956.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_344964.1, XP_001080027.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680412,
                              SAMN06680422 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..436
                     /product="T-box transcription factor TBX6"
                     /note="T-box protein 6; T-box 6"
                     /calculated_mol_wt=47085
     Region          67..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJK7.1)"
     Region          91..273
                     /region_name="T-box_TBX6"
                     /note="DNA-binding domain of T-box transcription factor 6,
                     and related T-box proteins; cd20196"
                     /db_xref="CDD:410322"
     Site            order(118..119,152,196,199,212..213,250..253,258,261..262,
                     265..271)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410322"
     Region          275..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJK7.1)"
     Region          <324..424
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          360..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZJK7.1)"
     CDS             1..436
                     /gene="Tbx6"
                     /coded_by="NM_001108920.1:25..1335"
                     /db_xref="GeneID:365371"
                     /db_xref="RGD:1307716"
ORIGIN      
        1 myhprelyps lgtgyrlghp qpgadstfpp altegyrypd ldtskldcfl sgieaaphtl
       61 aappplpllp salgpetapp ppealhslpg vslslenqel wkefsavgte miitkagrrm
      121 fpacrvsvtg ldpearylfl ldvvpvdgar yrwqgqhwep sgkaeprlpd rvyihpdspa
      181 tgahwmrqpv sfhrvkltns tldphghlil hsmhkyqpri hlvratqlcs qhwggvasfr
      241 fpettfisvt ayqnpritql kiaanpfakg frengrnckr erdarvkrkl rgpepvatea
      301 cgsgdtpggp cdstlggdir dsdpepaptp qeaasasapp cggpsaeayl lhpaafhgap
      361 shlpartpsf peapdpgrpa pysaaflelq pgpgssayqt tpsvtpfaph fiqgapfplp
      421 ypgpggyldm gskqmy
//
LOCUS       NP_001014226             341 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 22 [Rattus norvegicus].
ACCESSION   NP_001014226 XP_343330
VERSION     NP_001014226.1
DBSOURCE    REFSEQ: accession NM_001014204.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086949.1.
            
            On Apr 20, 2005 this sequence version replaced XP_343330.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086949.1, SRR8487226.183246.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..341
                     /product="dnaJ homolog subfamily C member 22"
                     /note="DnaJ (Hsp40) homolog, subfamily C, member 22"
                     /calculated_mol_wt=38112
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PR00.1)"
     Region          278..335
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(305..307,317,320..321,324..325)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     CDS             1..341
                     /gene="Dnajc22"
                     /gene_synonym="RGD1311098"
                     /coded_by="NM_001014204.1:167..1192"
                     /db_xref="GeneID:362998"
                     /db_xref="RGD:1311098"
ORIGIN      
        1 makgllmtya lwafggpvgl hhlylgrdsh allwmltlgg gglgwlwefw klpsfvaqan
       61 gvqswkqrpe eerpplsllr fasqmvvgvy fglvalisls stanfyivgl plavglgvll
      121 vaavgnqtsd fkntlgaafl tspvfygrpi ailpislaas itaqkhrryk vsavsetlsv
      181 rlyrvglayl aftgplayst lyntaatiny aaetlgsfls wfnffpllgr lvesvlllpc
      241 riwwllvgap gfnssqfqew eklyefvdsf qdekrqlahq vlgipegatn eeihrsyrdl
      301 vkvwhpdhnr hqteeaqrhf leiqaayevl sqpkkprasw r
//
LOCUS       NP_001011903             370 aa            linear   ROD 27-APR-2025
DEFINITION  protein-tyrosine sulfotransferase 1 [Rattus norvegicus].
ACCESSION   NP_001011903 XP_213761
VERSION     NP_001011903.2
DBSOURCE    REFSEQ: accession NM_001011903.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Tanaka,S., Nishiyori,T., Kojo,H., Otsubo,R., Tsuruta,M., Kurogi,K.,
            Liu,M.C., Suiko,M., Sakakibara,Y. and Kakuta,Y.
  TITLE     Structural basis for the broad substrate specificity of the human
            tyrosylprotein sulfotransferase-1
  JOURNAL   Sci Rep 7 (1), 8776 (2017)
   PUBMED   28821720
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Kang,B.W., Jeon,H.S., Chae,Y.S., Lee,S.J., Park,J.S., Choi,G.S. and
            Kim,J.G.
  TITLE     Impact of Genetic Variation in MicroRNA-binding Site on
            Susceptibility to Colorectal Cancer
  JOURNAL   Anticancer Res 36 (7), 3353-3361 (2016)
   PUBMED   27354594
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Hoffhines,A.J., Damoc,E., Bridges,K.G., Leary,J.A. and Moore,K.L.
  TITLE     Detection and purification of tyrosine-sulfated proteins using a
            novel anti-sulfotyrosine monoclonal antibody
  JOURNAL   J Biol Chem 281 (49), 37877-37887 (2006)
   PUBMED   17046811
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Goettsch,S., Badea,R.A., Mueller,J.W., Wotzlaw,C., Schoelermann,B.,
            Schulz,L., Rabiller,M., Bayer,P. and Hartmann-Fatu,C.
  TITLE     Human TPST1 transmembrane domain triggers enzyme dimerisation and
            localisation to the Golgi compartment
  JOURNAL   J Mol Biol 361 (3), 436-449 (2006)
   PUBMED   16859706
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Ouyang,Yb., Lane,W.S. and Moore,K.L.
  TITLE     Tyrosylprotein sulfotransferase: purification and molecular cloning
            of an enzyme that catalyzes tyrosine O-sulfation, a common
            posttranslational modification of eukaryotic proteins
  JOURNAL   Proc Natl Acad Sci U S A 95 (6), 2896-2901 (1998)
   PUBMED   9501187
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105826.1.
            
            On Dec 7, 2007 this sequence version replaced NP_001011903.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105826.1, SRR8487231.11168.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..370
                     /product="protein-tyrosine sulfotransferase 1"
                     /EC_number="2.8.2.20"
                     /note="TPST-1"
                     /calculated_mol_wt=42004
     Site            9..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR92.1)"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3KR92.1)"
     Region          72..261
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
     Region          102..106
                     /region_name="Interaction with peptide substrate.
                     /evidence=ECO:0000250|UniProtKB:O60507"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR92.1)"
     Site            159
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:O60704; propagated from
                     UniProtKB/Swiss-Prot (Q3KR92.1)"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3KR92.1)"
     Site            286
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:O60704; propagated from
                     UniProtKB/Swiss-Prot (Q3KR92.1)"
     CDS             1..370
                     /gene="Tpst1"
                     /coded_by="NM_001011903.2:256..1368"
                     /db_xref="GeneID:288617"
                     /db_xref="RGD:1308473"
ORIGIN      
        1 mvgklkqnll laclvissvt vfylgqhame chhrieersq parlenpkat vrtgldikan
       61 ktftyhknmp lifiggvprs gttlmramld ahpdircgee trviprilal kqmwsrsske
      121 kirldeagvt devldsamqa fllevivkhg epapylcnkd pfalksltyl arlfpnakfl
      181 lmvrdgrasv hsmisrkvti agfdlnsyrd cltkwnraie tmynqcmevg ykkcmlvhye
      241 qlvlhperwm rtllkflhip wnhsvlhhee migkaggvsl skverstdqv ikpvnvgals
      301 kwvgkippdv lqdmaviapm laklgydpya nppnygkpdp kilentrrvh kgefqlpdfl
      361 kekpqteqve
//
LOCUS       NP_001020797             365 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001020797 XP_213410
VERSION     NP_001020797.1
DBSOURCE    REFSEQ: accession NM_001025626.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Minczuk,M., He,J., Duch,A.M., Ettema,T.J., Chlebowski,A.,
            Dzionek,K., Nijtmans,L.G., Huynen,M.A. and Holt,I.J.
  TITLE     TEFM (c17orf42) is necessary for transcription of human mtDNA
  JOURNAL   Nucleic Acids Res 39 (10), 4284-4299 (2011)
   PUBMED   21278163
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC098792.1.
            
            On Jul 22, 2005 this sequence version replaced XP_213410.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098792.1, FM108449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132298, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q25"
     Protein         1..365
                     /product="transcription elongation factor, mitochondrial"
                     /calculated_mol_wt=36924
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q4KM51.1)"
                     /calculated_mol_wt=4633
     mat_peptide     41..365
                     /product="Transcription elongation factor, mitochondrial.
                     /id=PRO_0000406331"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM51.1)"
                     /calculated_mol_wt=36924
     Region          81..129
                     /region_name="HHH_3"
                     /note="Helix-hairpin-helix motif; pfam12836"
                     /db_xref="CDD:463723"
     Region          172..354
                     /region_name="RuvC-like"
                     /note="Crossover junction endodeoxyribonuclease RuvC and
                     similar proteins; cl21482"
                     /db_xref="CDD:473878"
     Site            order(253,255,257..259,261..262)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438561"
     CDS             1..365
                     /gene="Tefm"
                     /gene_synonym="RGD1306595"
                     /coded_by="NM_001025626.1:24..1121"
                     /db_xref="GeneID:287554"
                     /db_xref="RGD:1306595"
ORIGIN      
        1 mawranlacl ikaggrtrwf plpeylsmsp vlhntcsrrk stapeklaas vaacdtngke
       61 pgtalgrlys peqqasilhv lntasdkele afrllrgrks vnivehrkkf gpfqslesli
      121 gvpliqykta vevcnsilcp enrrrkksqe kwvlrkfikp gvekerlkav nsivsivfgt
      181 rriawahldr kptvldwqqa ecwkltnkty pssfyleeis svvskipkad lyileksgls
      241 iqntslfpil lhfliteaml yallnktfak dgqhrvlsin rnavgkhfdl migdtrtsgr
      301 elvkqflses vlkeqprvff prelavqyrq kivksshrie elydsllqav afyelvfgsg
      361 selkc
//
LOCUS       NP_001094456            1211 aa            linear   ROD 27-APR-2025
DEFINITION  homeodomain-interacting protein kinase 1 [Rattus norvegicus].
ACCESSION   NP_001094456 XP_001064683 XP_345268
VERSION     NP_001094456.1
DBSOURCE    REFSEQ: accession NM_001100986.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Kulkarni,P., Jolly,M.K., Jia,D., Mooney,S.M., Bhargava,A.,
            Kagohara,L.T., Chen,Y., Hao,P., He,Y., Veltri,R.W., Grishaev,A.,
            Weninger,K., Levine,H. and Orban,J.
  TITLE     Phosphorylation-induced conformational dynamics in an intrinsically
            disordered protein and potential role in phenotypic heterogeneity
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), E2644-E2653 (2017)
   PUBMED   28289210
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Mooney,S.M., Qiu,R., Kim,J.J., Sacho,E.J., Rajagopalan,K.,
            Johng,D., Shiraishi,T., Kulkarni,P. and Weninger,K.R.
  TITLE     Cancer/testis antigen PAGE4, a regulator of c-Jun transactivation,
            is phosphorylated by homeodomain-interacting protein kinase 1, a
            component of the stress-response pathway
  JOURNAL   Biochemistry 53 (10), 1670-1679 (2014)
   PUBMED   24559171
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Shang,Y., Doan,C.N., Arnold,T.D., Lee,S., Tang,A.A., Reichardt,L.F.
            and Huang,E.J.
  TITLE     Transcriptional corepressors HIPK1 and HIPK2 control angiogenesis
            via TGF-beta-TAK1-dependent mechanism
  JOURNAL   PLoS Biol 11 (4), e1001527 (2013)
   PUBMED   23565059
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Inoue,T., Kagawa,T., Inoue-Mochita,M., Isono,K., Ohtsu,N.,
            Nobuhisa,I., Fukushima,M., Tanihara,H. and Taga,T.
  TITLE     Involvement of the Hipk family in regulation of eyeball size, lens
            formation and retinal morphogenesis
  JOURNAL   FEBS Lett 584 (14), 3233-3238 (2010)
   PUBMED   20579985
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Isono,K., Nemoto,K., Li,Y., Takada,Y., Suzuki,R., Katsuki,M.,
            Nakagawara,A. and Koseki,H.
  TITLE     Overlapping roles for homeodomain-interacting protein kinases hipk1
            and hipk2 in the mediation of cell growth in response to
            morphogenetic and genotoxic signals
  JOURNAL   Mol Cell Biol 26 (7), 2758-2771 (2006)
   PUBMED   16537918
  REMARK    Erratum:[Mol Cell Biol. 2014 Jul;34(14):2772]
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Li,X., Zhang,R., Luo,D., Park,S.J., Wang,Q., Kim,Y. and Min,W.
  TITLE     Tumor necrosis factor alpha-induced desumoylation and cytoplasmic
            translocation of homeodomain-interacting protein kinase 1 are
            critical for apoptosis signal-regulating kinase 1-JNK/p38
            activation
  JOURNAL   J Biol Chem 280 (15), 15061-15070 (2005)
   PUBMED   15701637
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Kondo,S., Lu,Y., Debbas,M., Lin,A.W., Sarosi,I., Itie,A.,
            Wakeham,A., Tuan,J., Saris,C., Elliott,G., Ma,W., Benchimol,S.,
            Lowe,S.W., Mak,T.W. and Thukral,S.K.
  TITLE     Characterization of cells and gene-targeted mice deficient for the
            p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)
  JOURNAL   Proc Natl Acad Sci U S A 100 (9), 5431-5436 (2003)
   PUBMED   12702766
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Ecsedy,J.A., Michaelson,J.S. and Leder,P.
  TITLE     Homeodomain-interacting protein kinase 1 modulates Daxx
            localization, phosphorylation, and transcriptional activity
  JOURNAL   Mol Cell Biol 23 (3), 950-960 (2003)
   PUBMED   12529400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Oct 20, 2007 this sequence version replaced
            XP_001064683.1, XP_345268.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF460311.1, SRR22582416.290191.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1211
                     /product="homeodomain-interacting protein kinase 1"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=130655
     Region          174..528
                     /region_name="STKc_HIPK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Homeodomain-Interacting Protein Kinase 1; cd14228"
                     /db_xref="CDD:271130"
     Site            order(196..200,204,217,219,233,252,268..271,274,276..277,
                     315,317,319..320,322,337,340,350,352..355,357,394)
                     /site_type="active"
                     /db_xref="CDD:271130"
     Site            order(196..200,204,217,219,252,268..271,274,315,317,
                     319..320,322,337)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271130"
     Site            order(233,276,315,317,340,350,352..355,357,394)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271130"
     Site            336..357
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271130"
     Region          <618..925
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          835..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          844..847
                     /region_name="Nuclear localization signal 1 (NLS1).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86Z02; propagated from
                     UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          885..1094
                     /region_name="Interaction with TP53.
                     /evidence=ECO:0000250|UniProtKB:O88904"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          891..998
                     /region_name="Required for localization to nuclear
                     speckles. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          902..926
                     /region_name="SUMO interaction motifs (SIM), required for
                     nuclear localization and kinase activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          1002..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          1047..1070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Region          1085..1105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P5.1)"
     Site            1201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86Z02; propagated from
                     UniProtKB/Swiss-Prot (A4L9P5.1)"
     CDS             1..1211
                     /gene="Hipk1"
                     /coded_by="NM_001100986.1:188..3823"
                     /db_xref="GeneID:365895"
                     /db_xref="RGD:1304941"
ORIGIN      
        1 masqlqvfsp psvsssafcs akklkiepsg wdvsgqssnd kyythsktlp atqgqasssh
       61 qvanfnipay dqglllqapa vehivvtaad ssgsaatatf qssqtlthrs nvsllepyqk
      121 cglkrkseev dsngsvqiie ehpplmlqnr tvvgaaattt tvttksssss gegdyqlvqh
      181 eilcsmtnsy evleflgrgt fgqvakcwkr stkeivaiki lknhpsyarq gqievsilsr
      241 lssenadeyn fvrsyecfqh knhtclvfem leqnlydflk qnkfsplplk yirpilqqva
      301 talmklkslg lihadlkpen imlvdpvrqp yrvkvidfgs ashvskavcs tylqsryyra
      361 peiilglpfc eaidmwslgc viaelflgwp lypgaseydq iryisqtqgl paeyllsagt
      421 kttrffnrdp nlgyplwrlk tpeeheletg ikskearkyi fnclddmaqv nmstdlegtd
      481 mlaekadrre yidllkkmlt idadkrvtpl ktlnhqfvtm thlldfphsn hvkscfqnme
      541 ickrrvhmyd tvsqikspft thvapststn ltmsfsnqls tvhnqasvla ssstaaaatl
      601 slansdvsll nyqsalypps aapvpgvaqq gvslqpgttq ictqtdpfqq tfivcppafq
      661 tglqattkhs gfpvrmdnav plvpqapaaq plqiqsgvlt qgsctplmva tlhpqvatit
      721 pqyavpftls caagrpalve qtaavlqawp ggtqqillps awqqlpgval hnsvqptavi
      781 peamgssqql adwrnahshg nqystimqqp slltnhvtla taqplnvgva hvvrqqqsss
      841 lpsrknkqsa pvsstsslev lpsqvyslvg ssplrttssy nslvpvqdqh qpiiipdtps
      901 ppvsvitirs dtdeeednkf kpsssslkar snvisyvtvn dspdsdssls spyptdtlsa
      961 lrgnsgtlle gpgrtaadgi gtrtiivppl ktqlgdctga tqasgllsss ktkpvasvsg
     1021 qssgccitpt gyraqrggas avqplnlsqn qqsssastsq erssnpaprr qqafvaplsq
     1081 apyafqhgsp lhstghphla papahlpsqp hlytyaapts aaalgstssi ahlfspqgss
     1141 rhaaaytthp stlvhqvpvs vgpslltsas vapaqyqhqf atqsyigssr gstiytgypl
     1201 sptkisqysy l
//
LOCUS       NP_001128474             104 aa            linear   ROD 27-APR-2025
DEFINITION  colipase-like protein 2 precursor [Rattus norvegicus].
ACCESSION   NP_001128474 XP_001070754 XP_001078433
VERSION     NP_001128474.1
DBSOURCE    REFSEQ: accession NM_001135002.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On or before Sep 17, 2008 this sequence version replaced
            XP_001070754.1, XP_001078433.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16676784,
                              SAMN16676788 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..104
                     /product="colipase-like protein 2 precursor"
                     /note="colipase-like protein 2"
                     /calculated_mol_wt=9520
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1992
     mat_peptide     20..104
                     /product="Colipase-like protein 2. /id=PRO_0000416691"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVN1.1)"
                     /calculated_mol_wt=9520
     Region          34..>90
                     /region_name="COLIPASE"
                     /note="Colipase; a stoichiometric cofactor for pancreatic
                     lipase, allowing the enzyme to anchor itself to the
                     water-lipid interface and stabilizing the active enzyme
                     conformation; cl29842"
                     /db_xref="CDD:475263"
     Site            order(36..37,59,66,85..87)
                     /site_type="other"
                     /note="lipase interaction site [polypeptide binding]"
                     /db_xref="CDD:119409"
     CDS             1..104
                     /gene="Clpsl2"
                     /coded_by="NM_001135002.1:30..344"
                     /db_xref="GeneID:689425"
                     /db_xref="RGD:1592336"
ORIGIN      
        1 maftqalvtv laflvgtlph kfdfsensdl kkangdkcvh hsqcfsdccl idlersgafc
       61 tskshvgmac lpqtkrslni lcpcriglsc hskdpmcprr cqmi
//
LOCUS       NP_001014203             267 aa            linear   ROD 27-APR-2025
DEFINITION  diphthine--ammonia ligase [Rattus norvegicus].
ACCESSION   NP_001014203 XP_342493
VERSION     NP_001014203.1
DBSOURCE    REFSEQ: accession NM_001014181.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Su,X., Lin,Z., Chen,W., Jiang,H., Zhang,S. and Lin,H.
  TITLE     Chemogenomic approach identified yeast YLR143W as diphthamide
            synthetase
  JOURNAL   Proc Natl Acad Sci U S A 109 (49), 19983-19987 (2012)
   PUBMED   23169644
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087148.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342493.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087148.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..267
                     /product="diphthine--ammonia ligase"
                     /EC_number="6.3.1.14"
                     /note="ATP-binding domain-containing protein 4;
                     diphthamide synthase; diphthamide synthetase; ATP binding
                     domain 4; protein DPH6 homolog"
                     /calculated_mol_wt=29853
     Region          2..219
                     /region_name="AANH_PF0828-like"
                     /note="putative ATP pyrophosphatase PF0828 and similar
                     proteins; cd01994"
                     /db_xref="CDD:467498"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ28; propagated from
                     UniProtKB/Swiss-Prot (Q5M9F5.1)"
     CDS             1..267
                     /gene="Dph6"
                     /gene_synonym="Atpbd4; RGD1310006"
                     /coded_by="NM_001014181.1:48..851"
                     /db_xref="GeneID:362191"
                     /db_xref="RGD:1310006"
ORIGIN      
        1 mrvaalisgg kdscynmmrc iaeghqival anlrpddnqv esdeldsymy qtvghhaidl
       61 yaeamalply rrtirgrsle tgrvytrceg devedlyell klvkekeeie gvsvgailsd
      121 yqrvrvenvc krlnlqplay lwqrnqedll remiasniea iiikvaalgl dpdkhlgktl
      181 gemepyllel skkygvhvcg eggeyetftl dcplfkkkiv vdtseavihs adafapvayl
      241 rlsglhleek vssvpgddet tsyihns
//
LOCUS       NP_001007735             299 aa            linear   ROD 27-APR-2025
DEFINITION  ethylmalonyl-CoA decarboxylase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001007735 XP_341745
VERSION     NP_001007735.1
DBSOURCE    REFSEQ: accession NM_001007734.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079052.1.
            
            On Nov 29, 2004 this sequence version replaced XP_341745.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079052.1, CK470945.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..299
                     /product="ethylmalonyl-CoA decarboxylase isoform 1"
                     /EC_number="4.1.1.94"
                     /note="enoyl-CoA hydratase domain-containing protein 1;
                     enoyl Coenzyme A hydratase domain containing 1;
                     methylmalonyl-CoA decarboxylase; enoyl CoA hydratase
                     domain containing 1"
                     /calculated_mol_wt=32500
     Region          52..292
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
     Site            209
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9D9V3; propagated from
                     UniProtKB/Swiss-Prot (Q6AYG5.1)"
     CDS             1..299
                     /gene="Echdc1"
                     /gene_synonym="MMCD"
                     /coded_by="NM_001007734.1:141..1040"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361465"
                     /db_xref="RGD:1359654"
ORIGIN      
        1 maksllassl svrtkilqtg vslyntthgf heeevkkile qfpggsidlq kkqngigilt
       61 lnnsnkmnaf sgammlqlle rvielenwte gkglivhgak ntfcsgsdln avkalstpen
      121 gvalsmfmqn tltrfmrlpl isvalvqgwa mgggaeltta cdfrlmtees virfvhkemg
      181 ivpswggasr lveiigsrqa lkvlsgtfkl dskealrigl adevlqpsde ataleqaqew
      241 leqfvsgpaq virglkksvc sgrelyleea lqnerdvlet lwggpanlea iakkgkhtk
//
LOCUS       NP_113815                445 aa            linear   ROD 27-APR-2025
DEFINITION  oxysterols receptor LXR-alpha [Rattus norvegicus].
ACCESSION   NP_113815
VERSION     NP_113815.2
DBSOURCE    REFSEQ: accession NM_031627.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Yu,X., Ding,X., Feng,H., Bi,Y., Li,Y., Shan,J. and Bian,H.
  TITLE     Excessive exogenous cholesterol activating intestinal
            LXRalpha-ABCA1/G5/G8 signaling pathway can not reverse
            atherosclerosis in ApoE-/- mice
  JOURNAL   Lipids Health Dis 22 (1), 51 (2023)
   PUBMED   37061692
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Ali,U., Wabitsch,M., Tews,D. and Colitti,M.
  TITLE     Effects of allicin on human Simpson-Golabi-Behmel syndrome cells in
            mediating browning phenotype
  JOURNAL   Front Endocrinol (Lausanne) 14, 1141303 (2023)
   PUBMED   36936145
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Huang,Q., Su,J., Xu,J., Yu,H., Jin,X., Wang,Y., Yan,M., Yu,J.,
            Chen,S., Wang,Y. and Lv,G.
  TITLE     Beneficial effects of Panax notoginseng (Burkill) F. H. Chen flower
            saponins in rats with metabolic hypertension by inhibiting the
            activation of the renin-angiotensin-aldosterone system through
            complement 3
  JOURNAL   BMC Complement Med Ther 23 (1), 13 (2023)
   PUBMED   36653797
  REMARK    Erratum:[BMC Complement Med Ther. 2023 Mar 8;23(1):76. doi:
            10.1186/s12906-023-03893-1. PMID: 36890530]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Harchegani,A.B., Rostami,S., Mohsenifar,Z., Dafchahi,A.B.,
            Moghadam,F.M., Jaafarzadeh,M., Saraabestan,S.S. and Ranji,N.
  TITLE     Anti-apoptotic properties of N-Acetyl cysteine and its effects on
            of Liver X receptor and Sirtuin 1 expression in the liver of rats
            exposed to Lead
  JOURNAL   J Trace Elem Med Biol 74, 127070 (2022)
   PUBMED   36155419
  REMARK    GeneRIF: Anti-apoptotic properties of N-Acetyl cysteine and its
            effects on of Liver X receptor and Sirtuin 1 expression in the
            liver of rats exposed to Lead.
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Grbic,E., Gorkic,N., Pleskovic,A., Ljuca,F., Gasparini,M., Mrda,B.,
            Cilensek,I., Fras,Z. and Petrovic,D.
  TITLE     Association between the rs2279238 of the Liver X receptor alpha
            gene polymorphism and advanced carotid atherosclerosis in the
            Slovenian cohort
  JOURNAL   Gene 840, 146764 (2022)
   PUBMED   35907563
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Whitney,K.D., Watson,M.A., Goodwin,B., Galardi,C.M., Maglich,J.M.,
            Wilson,J.G., Willson,T.M., Collins,J.L. and Kliewer,S.A.
  TITLE     Liver X receptor (LXR) regulation of the LXRalpha gene in human
            macrophages
  JOURNAL   J Biol Chem 276 (47), 43509-43515 (2001)
   PUBMED   11546778
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Chiang,J.Y., Kimmel,R. and Stroup,D.
  TITLE     Regulation of cholesterol 7alpha-hydroxylase gene (CYP7A1)
            transcription by the liver orphan receptor (LXRalpha)
  JOURNAL   Gene 262 (1-2), 257-265 (2001)
   PUBMED   11179691
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Repa,J.J., Liang,G., Ou,J., Bashmakov,Y., Lobaccaro,J.M.,
            Shimomura,I., Shan,B., Brown,M.S., Goldstein,J.L. and
            Mangelsdorf,D.J.
  TITLE     Regulation of mouse sterol regulatory element-binding protein-1c
            gene (SREBP-1c) by oxysterol receptors, LXRalpha and LXRbeta
  JOURNAL   Genes Dev 14 (22), 2819-2830 (2000)
   PUBMED   11090130
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Lehmann,J.M., Kliewer,S.A., Moore,L.B., Smith-Oliver,T.A.,
            Oliver,B.B., Su,J.L., Sundseth,S.S., Winegar,D.A., Blanchard,D.E.,
            Spencer,T.A. and Willson,T.M.
  TITLE     Activation of the nuclear receptor LXR by oxysterols defines a new
            hormone response pathway
  JOURNAL   J Biol Chem 272 (6), 3137-3140 (1997)
   PUBMED   9013544
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Apfel,R., Benbrook,D., Lernhardt,E., Ortiz,M.A., Salbert,G. and
            Pfahl,M.
  TITLE     A novel orphan receptor specific for a subset of thyroid
            hormone-responsive elements and its interaction with the
            retinoid/thyroid hormone receptor subfamily
  JOURNAL   Mol Cell Biol 14 (10), 7025-7035 (1994)
   PUBMED   7935418
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088750.1.
            
            On Apr 14, 2007 this sequence version replaced NP_113815.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088750.1, U11685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..445
                     /product="oxysterols receptor LXR-alpha"
                     /EC_number="3.4.13.9"
                     /note="RLD-1; liver X receptor alpha; nuclear orphan
                     receptor LXR-alpha"
                     /calculated_mol_wt=50401
     Region          1..94
                     /region_name="Transactivation AF-1, required for
                     ligand-independent transactivation function.
                     /evidence=ECO:0000250|UniProtKB:Q13133"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62685.1)"
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62685.1)"
     Region          62..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62685.1)"
     Region          76..176
                     /region_name="NR_DBD_LXR"
                     /note="DNA-binding domain of Liver X receptors (LXRs)
                     family is composed of two C4-type zinc fingers; cd07160"
                     /db_xref="CDD:143534"
     Site            order(96,99,113,116,132,138,148,151)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143534"
     Site            order(101..102,142..143,146)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143534"
     Site            order(105..108,114..115,117,119,122,145..147,149,152,163,
                     166)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143534"
     Region          178..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62685.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62685.1)"
     Region          203..445
                     /region_name="Transactivation AF-2, required for
                     ligand-dependent transactivation function, mediates
                     interaction with CCAR2.
                     /evidence=ECO:0000250|UniProtKB:Q13133"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62685.1)"
     Region          208..443
                     /region_name="NR_LBD_LXR"
                     /note="The ligand binding domain of Liver X receptors, a
                     family of nuclear receptors of ligand-activated
                     transcription factors; cd06954"
                     /db_xref="CDD:132752"
     Site            order(252,255..256,258..259,293,296..297,300,311,333,337,
                     419,422..423,426,433,437,441)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132752"
     Site            order(264,267,271,281..282,284..285,289,435..436,439)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132752"
     Site            order(366,377,381,385,388,392,400,402..404,406..407,
                     409..411,413..414,417)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132752"
     CDS             1..445
                     /gene="Nr1h3"
                     /gene_synonym="LXRalpha"
                     /coded_by="NM_031627.2:18..1355"
                     /db_xref="GeneID:58852"
                     /db_xref="RGD:61909"
ORIGIN      
        1 mslwleaavp dvspdsatel wktepqdagd qggntcilre earmpqstgg alriglesse
       61 ptallpraet lpeptelrpq krkkgpapkm lgnelcsvcg dkasgfhynv lscegckgff
      121 rrsvikgary ichsgghcpm dtymrrkcqe crlrkcrqag mreecvlsee qirlkklkrq
      181 eeeqaqatsv sprvssppqv lpqlspeqlg mieklvaaqq qcnrrsfsdr lrvtpwpiap
      241 dpqsrearqq rfahftelai vsvqeivdfa kqlpgflqls redqiallkt saievmllet
      301 srrynpgses itflkdfsyn redfakaglq vefinpifef srsmnelqln daefalliai
      361 sifsadrpnv qdqlqverlq htyvealhay vsinhphdrl mfprmlmklv slrtlssvhs
      421 eqvfalrlqd kklppllsei wdvhe
//
LOCUS       NP_001007712             508 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription factor IIF subunit 1 [Rattus norvegicus].
ACCESSION   NP_001007712 XP_236789
VERSION     NP_001007712.1
DBSOURCE    REFSEQ: accession NM_001007711.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   He,Y., Yan,C., Fang,J., Inouye,C., Tjian,R., Ivanov,I. and
            Nogales,E.
  TITLE     Near-atomic resolution visualization of human transcription
            promoter opening
  JOURNAL   Nature 533 (7603), 359-365 (2016)
   PUBMED   27193682
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Gelev,V., Zabolotny,J.M., Lange,M., Hiromura,M., Yoo,S.W.,
            Orlando,J.S., Kushnir,A., Horikoshi,N., Paquet,E., Bachvarov,D.,
            Schaffer,P.A. and Usheva,A.
  TITLE     A new paradigm for transcription factor TFIIB functionality
  JOURNAL   Sci Rep 4, 3664 (2014)
   PUBMED   24441171
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Grunberg,S. and Hahn,S.
  TITLE     Structural insights into transcription initiation by RNA polymerase
            II
  JOURNAL   Trends Biochem Sci 38 (12), 603-611 (2013)
   PUBMED   24120742
  REMARK    Review article
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Kwak,H. and Lis,J.T.
  TITLE     Control of transcriptional elongation
  JOURNAL   Annu Rev Genet 47, 483-508 (2013)
   PUBMED   24050178
  REMARK    Review article
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Newberry,E.P., Latifi,T., Battaile,J.T. and Towler,D.A.
  TITLE     Structure-function analysis of Msx2-mediated transcriptional
            suppression
  JOURNAL   Biochemistry 36 (34), 10451-10462 (1997)
   PUBMED   9265625
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Fang,S.M. and Burton,Z.F.
  TITLE     RNA polymerase II-associated protein (RAP) 74 binds transcription
            factor (TF) IIB and blocks TFIIB-RAP30 binding
  JOURNAL   J Biol Chem 271 (20), 11703-11709 (1996)
   PUBMED   8662660
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Dikstein,R., Ruppert,S. and Tjian,R.
  TITLE     TAFII250 is a bipartite protein kinase that phosphorylates the base
            transcription factor RAP74
  JOURNAL   Cell 84 (5), 781-790 (1996)
   PUBMED   8625415
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Garrett,K.P., Serizawa,H., Hanley,J.P., Bradsher,J.N., Tsuboi,A.,
            Arai,N., Yokota,T., Arai,K., Conaway,R.C. and Conaway,J.W.
  TITLE     The carboxyl terminus of RAP30 is similar in sequence to region 4
            of bacterial sigma factors and is required for function
  JOURNAL   J Biol Chem 267 (33), 23942-23949 (1992)
   PUBMED   1429731
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Finkelstein,A., Kostrub,C.F., Li,J., Chavez,D.P., Wang,B.Q.,
            Fang,S.M., Greenblatt,J. and Burton,Z.F.
  TITLE     A cDNA encoding RAP74, a general initiation factor for
            transcription by RNA polymerase II
  JOURNAL   Nature 355 (6359), 464-467 (1992)
   PUBMED   1734284
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079136.1.
            
            On Nov 29, 2004 this sequence version replaced XP_236789.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079136.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06680448
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..508
                     /product="general transcription factor IIF subunit 1"
                     /note="TFIIF-alpha; transcription initiation factor IIF
                     subunit alpha; general transcription factor IIF,
                     polypeptide 1, 74kDa"
                     /calculated_mol_wt=57050
     Region          2..508
                     /region_name="TFIIF_alpha"
                     /note="Transcription initiation factor IIF, alpha subunit
                     (TFIIF-alpha); pfam05793"
                     /db_xref="CDD:310411"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Region          177..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            407
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35269; propagated from
                     UniProtKB/Swiss-Prot (Q6AY96.1)"
     CDS             1..508
                     /gene="Gtf2f1"
                     /coded_by="NM_001007711.1:127..1653"
                     /db_xref="GeneID:316123"
                     /db_xref="RGD:1359646"
ORIGIN      
        1 maalgsssqn vteyvvrvpk ntakrynima fnaadkvnfa twnqarlerd lsnkkiyqee
       61 empesgagse fnrklreear rkkygivlke frpedqpwll rvngksgrkf kgikkggvte
      121 ntayyiftqc adgafeafpv qnwynftpla rhrtltaeea eeewerrnkv lnhfsimqqr
      181 rlkdqdqded eeekekrsrk kpselrihdl eddlemssda sdasgeegsr askakkkapv
      241 tkagrkkkkk kgsddeafed sddgdfegqe vdymsdgsss spdeaegkpk vpqqedgpkg
      301 vdeqsessee seeekppeed keeeeekkap tpqekkrrkd ssddsdssee sdidsetssa
      361 lfmakkktpp krerkpsggs skgtsrpgtp saeaastsst lraaaskleq gkrtsetpaa
      421 krlrmdtgpq slsgkstpss gdvqvtedav rryltrkpmt tkdllkkfqt kktglsseqt
      481 vnvlaqilkr lnperkmigd kmhfslke
//
LOCUS       NP_001030174             361 aa            linear   ROD 27-APR-2025
DEFINITION  outer mitochondrial transmembrane helix translocase [Rattus
            norvegicus].
ACCESSION   NP_001030174 XP_220076
VERSION     NP_001030174.1
DBSOURCE    REFSEQ: accession NM_001035002.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Zhang,J., Wang,Y., Chi,Z., Keuss,M.J., Pai,Y.M., Kang,H.C.,
            Shin,J.H., Bugayenko,A., Wang,H., Xiong,Y., Pletnikov,M.V.,
            Mattson,M.P., Dawson,T.M. and Dawson,V.L.
  TITLE     The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic
            plasticity and behavior
  JOURNAL   Cell 145 (2), 284-299 (2011)
   PUBMED   21496646
  REMARK    GeneRIF: This study identifies an AAA+ ATPase that plays a critical
            role in regulating the surface expression of AMPAR and thereby
            regulates synaptic plasticity and learning and memory.
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Dai,C., Liang,D., Li,H., Sasaki,M., Dawson,T.M. and Dawson,V.L.
  TITLE     Functional identification of neuroprotective molecules
  JOURNAL   PLoS One 5 (11), e15008 (2010)
   PUBMED   21124846
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC094514.1.
            
            On Oct 26, 2005 this sequence version replaced XP_220076.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094514.1, SRR8487231.65694.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..361
                     /product="outer mitochondrial transmembrane helix
                     translocase"
                     /EC_number="3.6.1.3"
                     /note="ATPase family AAA domain-containing protein 1;
                     neuroprotective protein 6; thorase"
                     /calculated_mol_wt=40586
     Region          4..344
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Site            16..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J9.1)"
     Region          92..257
                     /region_name="RecA-like_ATAD1"
                     /note="ATPase domain of ATPase family AAA
                     domain-containing protein 1 and similar ATPase domains;
                     cd19520"
                     /db_xref="CDD:410928"
     Site            order(93..96,135..141)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:410928"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D5T0; propagated from
                     UniProtKB/Swiss-Prot (Q505J9.1)"
     CDS             1..361
                     /gene="Atad1"
                     /gene_synonym="Ab2-088"
                     /coded_by="NM_001035002.1:42..1127"
                     /db_xref="GeneID:309532"
                     /db_xref="RGD:1308570"
ORIGIN      
        1 mvhaeafsrp lsrnevvgli frltifgavt yftikwmvda idptrkqkve aqkqaeklmk
       61 qigvknvkls eyemsiaahl vdplnmhvtw sdiaglddvi tdlkdtvilp ikkkhlfens
      121 rllqppkgvl lygppgcgkt liakatakea gcrfinlqps tltdkwyges qklaaavfsl
      181 aiklqpsiif ideidsflrn rsssdheata mmkaqfmslw dgldtdhscq vivmgatnrp
      241 qdldsaimrr mptrfhinqp alkqreailk lilknenvdr hvdllevaqe tdgfsgsdlk
      301 emcrdaallc vreyvnstse eshdedeirp vqqqdlhrai ekmkkskdaa fqsvlthvcl
      361 d
//
LOCUS       NP_036745               1057 aa            linear   ROD 27-APR-2025
DEFINITION  atrial natriuretic peptide receptor 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_036745
VERSION     NP_036745.1
DBSOURCE    REFSEQ: accession NM_012613.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nagaraj,G. and Vellaichamy,E.
  TITLE     Triiodo-L-thyronine (T3) downregulates Npr1 gene (coding for
            natriuretic peptide receptor-A) transcription in H9c2 cells:
            involvement of beta-AR-ROS signaling
  JOURNAL   Endocrine 85 (3), 1075-1090 (2024)
   PUBMED   38713329
  REMARK    GeneRIF: Triiodo-L-thyronine (T3) downregulates Npr1 gene (coding
            for natriuretic peptide receptor-A) transcription in H9c2 cells:
            involvement of beta-AR-ROS signaling.
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tokudome,T., Otani,K., Mao,Y., Jensen,L.J., Arai,Y., Miyazaki,T.,
            Sonobe,T., Pearson,J.T., Osaki,T., Minamino,N., Ishida,J.,
            Fukamizu,A., Kawakami,H., Onozuka,D., Nishimura,K., Miyazato,M. and
            Nishimura,H.
  TITLE     Endothelial Natriuretic Peptide Receptor 1 Play Crucial Role for
            Acute and Chronic Blood Pressure Regulation by Atrial Natriuretic
            Peptide
  JOURNAL   Hypertension 79 (7), 1409-1422 (2022)
   PUBMED   35534926
  REMARK    GeneRIF: Endothelial Natriuretic Peptide Receptor 1 Play Crucial
            Role for Acute and Chronic Blood Pressure Regulation by Atrial
            Natriuretic Peptide.
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Manivasagam,S. and Vellaichamy,E.
  TITLE     Suppression of Npr1, not Npr2 gene function induces hypertrophic
            growth in H9c2 cells in vitro
  JOURNAL   Biochem Biophys Res Commun 491 (2), 250-256 (2017)
   PUBMED   28743500
  REMARK    GeneRIF: Suppression of Npr1, not Npr2 gene function induces
            hypertrophic growth in cardiomyocytes in vitro.
REFERENCE   4  (residues 1 to 1057)
  AUTHORS   Manivasagam,S., Subramanian,V., Tumala,A. and Vellaichamy,E.
  TITLE     Differential expression and regulation of anti-hypertrophic genes
            Npr1 and Npr2 during beta-adrenergic receptor activation-induced
            hypertrophic growth in rats
  JOURNAL   Mol Cell Endocrinol 433, 117-129 (2016)
   PUBMED   27283501
  REMARK    GeneRIF: Atenolol treatment normalized the altered expression of
            Npr1 and Npr2 genes.
REFERENCE   5  (residues 1 to 1057)
  AUTHORS   Sen,A., Kumar,P., Garg,R., Lindsey,S.H., Katakam,P.V.,
            Bloodworth,M. and Pandey,K.N.
  TITLE     Transforming growth factor beta1 antagonizes the transcription,
            expression and vascular signaling of guanylyl cyclase/natriuretic
            peptide receptor A - role of deltaEF1
  JOURNAL   FEBS J 283 (9), 1767-1781 (2016)
   PUBMED   26934489
  REMARK    GeneRIF: The results suggest that an antagonistic cascade exists
            between the TGF-beta1/Smad/deltaEF1 pathways and Npr1 expression
            and receptor signaling that is relevant to renal and vascular
            remodeling, and may be critical in the regulation of blood pressure
            and cardiovascular homeostasis.
REFERENCE   6  (residues 1 to 1057)
  AUTHORS   Deng,Y. and Rapp,J.P.
  TITLE     Cosegregation of blood pressure with angiotensin converting enzyme
            and atrial natriuretic peptide receptor genes using Dahl
            salt-sensitive rats
  JOURNAL   Nat Genet 1 (4), 267-272 (1992)
   PUBMED   1363813
REFERENCE   7  (residues 1 to 1057)
  AUTHORS   Bennett,B.D., Bennett,G.L., Vitangcol,R.V., Jewett,J.R.,
            Burnier,J., Henzel,W. and Lowe,D.G.
  TITLE     Extracellular domain-IgG fusion proteins for three human
            natriuretic peptide receptors. Hormone pharmacology and application
            to solid phase screening of synthetic peptide antisera
  JOURNAL   J Biol Chem 266 (34), 23060-23067 (1991)
   PUBMED   1660465
REFERENCE   8  (residues 1 to 1057)
  AUTHORS   Duda,T., Goraczniak,R.M. and Sharma,R.K.
  TITLE     Site-directed mutational analysis of a membrane guanylate cyclase
            cDNA reveals the atrial natriuretic factor signaling site
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7882-7886 (1991)
   PUBMED   1679239
REFERENCE   9  (residues 1 to 1057)
  AUTHORS   Koller,K.J., Lowe,D.G., Bennett,G.L., Minamino,N., Kangawa,K.,
            Matsuo,H. and Goeddel,D.V.
  TITLE     Selective activation of the B natriuretic peptide receptor by
            C-type natriuretic peptide (CNP)
  JOURNAL   Science 252 (5002), 120-123 (1991)
   PUBMED   1672777
REFERENCE   10 (residues 1 to 1057)
  AUTHORS   Yamaguchi,M., Rutledge,L.J. and Garbers,D.L.
  TITLE     The primary structure of the rat guanylyl cyclase A/atrial
            natriuretic peptide receptor gene
  JOURNAL   J Biol Chem 265 (33), 20414-20420 (1990)
   PUBMED   1978722
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J05677.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128742.1, X14773.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1057
                     /product="atrial natriuretic peptide receptor 1 precursor"
                     /EC_number="4.6.1.2"
                     /note="atrial natriuretic peptide receptor A; atrial
                     natriuretic peptide receptor 1; GC-A; ANP-A; atrial
                     natriuretic peptide A-type receptor; ANPR-A; guanylate
                     cyclase A; atrial natriuretic peptide receptor type A;
                     natriuretic peptide receptor A/guanylate cyclase A
                     (atrionatriuretic peptide receptor A)"
                     /calculated_mol_wt=115840
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3130
     mat_peptide     29..1057
                     /product="Atrial natriuretic peptide receptor 1.
                     /id=PRO_0000012362"
                     /note="propagated from UniProtKB/Swiss-Prot (P18910.1)"
                     /calculated_mol_wt=115840
     Region          32..439
                     /region_name="PBP1_NPR_A"
                     /note="Ligand-binding domain of type A natriuretic peptide
                     receptor; cd06385"
                     /db_xref="CDD:380608"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            order(81,113..114)
                     /site_type="other"
                     /note="Cl binding site [ion binding]"
                     /db_xref="CDD:380608"
     Site            order(95,99,115..116,119,123,127..128,193..194,197,200)
                     /site_type="other"
                     /note="dimer interface (closed form) [polypeptide
                     binding]"
                     /db_xref="CDD:380608"
     Site            order(115..116,119,123,141..142,186,193..194,197,200..201,
                     213)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380608"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:10894551,
                     ECO:0000269|PubMed:15117952; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            order(228..229,249,256)
                     /site_type="other"
                     /note="dimer interface (open form) [polypeptide binding]"
                     /db_xref="CDD:380608"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            423
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            470..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18910.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20977274; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Region          530..803
                     /region_name="PK_GC-A_B"
                     /note="Pseudokinase domain of the membrane Guanylate
                     Cyclase receptors, GC-A and GC-B; cd14042"
                     /db_xref="CDD:270944"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20977274,
                     ECO:0000269|PubMed:9528788; propagated from
                     UniProtKB/Swiss-Prot (P18910.1)"
     Region          <809..857
                     /region_name="HNOBA"
                     /note="Heme NO binding associated; pfam07701"
                     /db_xref="CDD:462234"
     Region          836..1025
                     /region_name="CYCc"
                     /note="Adenylyl- / guanylyl cyclase, catalytic domain;
                     smart00044"
                     /db_xref="CDD:214485"
     Site            order(875,877..882,917,919..921,924,989..991,995..996,
                     999..1000,1037)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(877,921)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(882,894,897..898,901,905,917..918,977,980,990..993,
                     996,1037)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..1057
                     /gene="Npr1"
                     /gene_synonym="Anpra; Gca; NPR-A; Npra"
                     /coded_by="NM_012613.1:371..3544"
                     /db_xref="GeneID:24603"
                     /db_xref="RGD:3195"
ORIGIN      
        1 mpgsrrvrpr lrallllppl lllrgghasd ltvavvlplt ntsypwswar vgpavelala
       61 rvkarpdllp gwtvrmvlgs senaagvcsd taaplaavdl kwehspavfl gpgcvysaap
      121 vgrftahwrv plltagapal gigvkdeyal ttrtgpshvk lgdfvtalhr rlgwehqalv
      181 lyadrlgddr pcffivegly mrvrerlnit vnhqefvegd pdhypkllra vrrkgrviyi
      241 csspdafrnl mllalnaglt gedyvffhld vfgqslksaq glvpqkpwer gdgqdrsarq
      301 afqaakiity kepdnpeyle flkqlkllad kkfnftvedg lkniipasfh dglllyvqav
      361 tetlaqggtv tdgenitqrm wnrsfqgvtg ylkidrngdr dtdfslwdmd petgafrvvl
      421 nyngtsqelm avsehklywp lgypppdvpk cgfdnedpac nqdhfstlev lalvgslsli
      481 sflivsffiy rkmqlekelv selwrvrwed lqpsslerhl rsagsrltls grgsnygsll
      541 ttegqfqvfa ktayykgnlv avkrvnrkri eltrkvlfel khmrdvqneh ltrfvgactd
      601 ppniciltey cprgslqdil enesitldwm frysltndiv kgmlflhnga icshgnlkss
      661 ncvvdgrfvl kitdyglesf rdpepeqght lfakklwtap ellrmasppa rgsqagdvys
      721 fgiilqeial rsgvfyvegl dlspkeiier vtrgeqppfr psmdlqshle elgqlmqrcw
      781 aedpqerppf qqirlalrkf nkenssnild nllsrmeqya nnleelveer tqayleekrk
      841 aeallyqilp hsvaeqlkrg etvqaeafds vtiyfsdivg ftalsaestp mqvvtllndl
      901 ytcfdavidn fdvykvetig daymvvsglp vrngqlhare varmalalld avrsfrirhr
      961 pqeqlrlrig ihtgpvcagv vglkmprycl fgdtvntasr mesngealki hlssetkavl
     1021 eefdgfelel rgdvemkgkg kvrtywllge rgcstrg
//
LOCUS       NP_037181                271 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 4 precursor
            [Rattus norvegicus].
ACCESSION   NP_037181
VERSION     NP_037181.1
DBSOURCE    REFSEQ: accession NM_013049.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Zhao,M., Li,Y., Wei,X., Zhang,Q., Jia,H., Quan,S., Cao,D., Wang,L.,
            Yang,T., Zhao,J., Pei,M., Tian,S., Yu,Y., Guo,Y. and Yang,X.
  TITLE     Negative immune factors might predominate local tumor immune status
            and promote carcinogenesis in cervical carcinoma
  JOURNAL   Virol J 14 (1), 5 (2017)
   PUBMED   28086903
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zhang,N., Li,G., Xiao,B., Liu,Y., Cai,Y., Sun,X. and Liang,J.
  TITLE     [Dynamic change OX40/OX40L mRNA in experimental allergic neuritis]
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 35 (9), 964-968 (2010)
   PUBMED   20871162
  REMARK    GeneRIF: OX40 and OX40L may play a role in the pathogenesis of
            experimental allegic neuritis.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Abe,J., Ueha,S., Suzuki,J., Tokano,Y., Matsushima,K. and
            Ishikawa,S.
  TITLE     Increased Foxp3(+) CD4(+) regulatory T cells with intact
            suppressive activity but altered cellular localization in murine
            lupus
  JOURNAL   Am J Pathol 173 (6), 1682-1692 (2008)
   PUBMED   19008373
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Chen,Z., Herman,A.E., Matos,M., Mathis,D. and Benoist,C.
  TITLE     Where CD4+CD25+ T reg cells impinge on autoimmune diabetes
  JOURNAL   J Exp Med 202 (10), 1387-1397 (2005)
   PUBMED   16301745
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Song,J., Salek-Ardakani,S., Rogers,P.R., Cheng,M., Van Parijs,L.
            and Croft,M.
  TITLE     The costimulation-regulated duration of PKB activation controls T
            cell longevity
  JOURNAL   Nat Immunol 5 (2), 150-158 (2004)
   PUBMED   14730361
  REMARK    Erratum:[Nat Immunol. 2004 Nov;5(11):1190]
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Pippig,S.D., Pena-Rossi,C., Long,J., Godfrey,W.R., Fowell,D.J.,
            Reiner,S.L., Birkeland,M.L., Locksley,R.M., Barclay,A.N. and
            Killeen,N.
  TITLE     Robust B cell immunity but impaired T cell proliferation in the
            absence of CD134 (OX40)
  JOURNAL   J Immunol 163 (12), 6520-6529 (1999)
   PUBMED   10586044
REFERENCE   7  (residues 1 to 271)
  AUTHORS   al-Shamkhani,A., Birkeland,M.L., Puklavec,M., Brown,M.H., James,W.
            and Barclay,A.N.
  TITLE     OX40 is differentially expressed on activated rat and mouse T cells
            and is the sole receptor for the OX40 ligand
  JOURNAL   Eur J Immunol 26 (8), 1695-1699 (1996)
   PUBMED   8765008
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Stuber,E., Neurath,M., Calderhead,D., Fell,H.P. and Strober,W.
  TITLE     Cross-linking of OX40 ligand, a member of the TNF/NGF cytokine
            family, induces proliferation and differentiation in murine splenic
            B cells
  JOURNAL   Immunity 2 (5), 507-521 (1995)
   PUBMED   7749983
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Mallett,S., Fossum,S. and Barclay,A.N.
  TITLE     Characterization of the MRC OX40 antigen of activated CD4 positive
            T lymphocytes--a molecule related to nerve growth factor receptor
  JOURNAL   EMBO J 9 (4), 1063-1068 (1990)
   PUBMED   2157591
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Paterson,D.J., Jefferies,W.A., Green,J.R., Brandon,M.R.,
            Corthesy,P., Puklavec,M. and Williams,A.F.
  TITLE     Antigens of activated rat T lymphocytes including a molecule of
            50,000 Mr detected only on CD4 positive T blasts
  JOURNAL   Mol Immunol 24 (12), 1281-1290 (1987)
   PUBMED   2828930
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X17037.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X17037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /strain="PVG/DA"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..271
                     /product="tumor necrosis factor receptor superfamily
                     member 4 precursor"
                     /note="tumor necrosis factor superfamily, member 4;
                     Tax-transcriptionally activated glycoprotein 1; MRC OX40;
                     OX40 antigen; OX40L receptor; tumor necrosis factor
                     (ligand) superfamily member 4; tumor necrosis factor
                     receptor superfamily, member 4"
                     /calculated_mol_wt=27777
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2137
     mat_peptide     20..271
                     /product="tumor necrosis factor receptor superfamily
                     member 4"
                     /calculated_mol_wt=27777
     Region          24..167
                     /region_name="TNFRSF4"
                     /note="Tumor necrosis factor receptor superfamily member 4
                     (TNFRSF4), also known as CD134 or OXO40; cd13406"
                     /db_xref="CDD:276911"
     Region          25..60
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P15725.1)"
     Region          26..59
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276911"
     Site            order(28..32,40,50,73..74,77)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276911"
     Region          61..102
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P15725.1)"
     Region          62..102
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276911"
     Region          103..123
                     /region_name="TNFR-Cys 3, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P15725.1)"
     Region          104..163
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276911"
     Region          124..164
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P15725.1)"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15725.1)"
     Site            211..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P15725.1)"
     CDS             1..271
                     /gene="Tnfrsf4"
                     /gene_synonym="Ox40; Txgp1"
                     /coded_by="NM_013049.1:15..830"
                     /db_xref="GeneID:25572"
                     /db_xref="RGD:3920"
ORIGIN      
        1 myvwvqqpta flllglslgv tvklncvkdt ypsghkccre cqpghgmvsr cdhtrdtvch
       61 pcepgfynea vnydtckqct qcnhrsgsel kqnctptedt vcqcrpgtqp rqdsshklgv
      121 dcvpcppghf spgsnqackp wtnctlsgkq irhpasnsld tvcedrslla tllwetqrtt
      181 frpttvpstt vwprtsqlps tptlvapegp afavilglgl gllapltvll alyllrkawr
      241 spntpkpcwg nsfrtpiqee qtdthftlak i
//
LOCUS       NP_001020798             703 aa            linear   ROD 27-APR-2025
DEFINITION  prolyl 3-hydroxylase 2 precursor [Rattus norvegicus].
ACCESSION   NP_001020798 XP_213603
VERSION     NP_001020798.1
DBSOURCE    REFSEQ: accession NM_001025627.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Fernandes,R.J., Farnand,A.W., Traeger,G.R., Weis,M.A. and Eyre,D.R.
  TITLE     A role for prolyl 3-hydroxylase 2 in post-translational
            modification of fibril-forming collagens
  JOURNAL   J Biol Chem 286 (35), 30662-30669 (2011)
   PUBMED   21757687
  REMARK    GeneRIF: P3H2 has preferred substrate sequences among the classes
            of 3Hyp sites in clade A collagen chains
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Shah,R., Smith,P., Purdie,C., Quinlan,P., Baker,L., Aman,P.,
            Thompson,A.M. and Crook,T.
  TITLE     The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for
            epigenetic silencing in breast cancer
  JOURNAL   Br J Cancer 100 (10), 1687-1696 (2009)
   PUBMED   19436308
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Tiainen,P., Pasanen,A., Sormunen,R. and Myllyharju,J.
  TITLE     Characterization of recombinant human prolyl 3-hydroxylase
            isoenzyme 2, an enzyme modifying the basement membrane collagen IV
  JOURNAL   J Biol Chem 283 (28), 19432-19439 (2008)
   PUBMED   18487197
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Jarnum,S., Kjellman,C., Darabi,A., Nilsson,I., Edvardsen,K. and
            Aman,P.
  TITLE     LEPREL1, a novel ER and Golgi resident member of the Leprecan
            family
  JOURNAL   Biochem Biophys Res Commun 317 (2), 342-351 (2004)
   PUBMED   15063763
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099107.1.
            
            On Jul 22, 2005 this sequence version replaced XP_213603.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..703
                     /product="prolyl 3-hydroxylase 2 precursor"
                     /EC_number="1.14.11.7"
                     /note="leprecan-like protein 1; leprecan-like 1"
                     /calculated_mol_wt=77457
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2394
     Region          18..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     mat_peptide     22..703
                     /product="Prolyl 3-hydroxylase 2. /id=PRO_0000240358"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
                     /calculated_mol_wt=77457
     Region          42..75
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Region          <137..370
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          144..177
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Region          205..238
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Region          301..334
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Site            444
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Site            455
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Region          467..665
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            544
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q4KLM6.1)"
     Region          700..703
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU10138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM6.1)"
     CDS             1..703
                     /gene="P3h2"
                     /gene_synonym="Leprel1"
                     /coded_by="NM_001025627.1:154..2265"
                     /db_xref="GeneID:288016"
                     /db_xref="RGD:1304568"
ORIGIN      
        1 mrestwvsll lllllpapqr ggpqdgrgsp epepergplq pfdllyasgv aayysgdyeg
       61 avrdleaalr shrrlrdirt rcarhcaarr plappgagpg aelpffravl erarcsrscq
      121 sqrlggpasr hrvsedvrsd fqrrvpynyl qrayiklnql dkameaahtf fmanpehmem
      181 qqniedykat arveaplvdr eakphlesyn agvkhyeadd feaaikyfeq alreyfnedm
      241 vcralcegpq rfeeyeylgs kgslyeaiad hymqvlvcqh ecvrelatrp grlspienfl
      301 plhydylqfa yyrvgeyvka lecakaylmf hpddqdvldn vdfyeslldd stdpasiear
      361 edltafvkrh kleaeliksa aeglgfsyse pnywisyggr qdenrvpsgv nmdgaevhgl
      421 smgkksppki grdlreggpl lyenitfvyn seqlngtqrv lldnvlseeq crelhsvasg
      481 imlvgdgyrg ktsphtpnek fegatvlkal kfgyegrvpl ksarlfydis ekarkivesy
      541 fmlnstlyfs ythmvcrtal sgqqdrrndl shpihadncl ldpeanecwk eppaytfrdy
      601 sallymnddf eggefiftem daktvtasik pkcgrmisfs sggenphgvk avtrgqrcav
      661 alwftldply releriqade viaildqeqh gkhglninpk del
//
LOCUS       NP_001019946             822 aa            linear   ROD 27-APR-2025
DEFINITION  neurotrophin receptor-interacting factor 1 [Rattus norvegicus].
ACCESSION   NP_001019946 XP_218292
VERSION     NP_001019946.1
DBSOURCE    REFSEQ: accession NM_001024775.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Valle-Garcia,D., Qadeer,Z.A., McHugh,D.S., Ghiraldini,F.G.,
            Chowdhury,A.H., Hasson,D., Dyer,M.A., Recillas-Targa,F. and
            Bernstein,E.
  TITLE     ATRX binds to atypical chromatin domains at the 3' exons of zinc
            finger genes to preserve H3K9me3 enrichment
  JOURNAL   Epigenetics 11 (6), 398-414 (2016)
   PUBMED   27029610
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Frietze,S., O'Geen,H., Blahnik,K.R., Jin,V.X. and Farnham,P.J.
  TITLE     ZNF274 recruits the histone methyltransferase SETDB1 to the 3' ends
            of ZNF genes
  JOURNAL   PLoS One 5 (12), e15082 (2010)
   PUBMED   21170338
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Geetha,T., Kenchappa,R.S., Wooten,M.W. and Carter,B.D.
  TITLE     TRAF6-mediated ubiquitination regulates nuclear translocation of
            NRIF, the p75 receptor interactor
  JOURNAL   EMBO J 24 (22), 3859-3868 (2005)
   PUBMED   16252010
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Linggi,M.S., Burke,T.L., Williams,B.B., Harrington,A., Kraemer,R.,
            Hempstead,B.L., Yoon,S.O. and Carter,B.D.
  TITLE     Neurotrophin receptor interacting factor (NRIF) is an essential
            mediator of apoptotic signaling by the p75 neurotrophin receptor
  JOURNAL   J Biol Chem 280 (14), 13801-13808 (2005)
   PUBMED   15668238
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Benzel,I., Barde,Y.A. and Casademunt,E.
  TITLE     Strain-specific complementation between NRIF1 and NRIF2, two zinc
            finger proteins sharing structural and biochemical properties
  JOURNAL   Gene 281 (1-2), 19-30 (2001)
   PUBMED   11750124
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Casademunt,E., Carter,B.D., Benzel,I., Frade,J.M., Dechant,G. and
            Barde,Y.A.
  TITLE     The zinc finger protein NRIF interacts with the neurotrophin
            receptor p75(NTR) and participates in programmed cell death
  JOURNAL   EMBO J 18 (21), 6050-6061 (1999)
   PUBMED   10545116
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097420.1.
            
            On Jun 10, 2005 this sequence version replaced XP_218292.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..822
                     /product="neurotrophin receptor-interacting factor 1"
                     /note="zinc finger protein 274"
                     /calculated_mol_wt=93497
     Region          14..73
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          157..239
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          277..318
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          376..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8E9.1)"
     Region          499..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8E9.1)"
     Region          653..672
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          680..700
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          696..717
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          708..728
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          720..744
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          734..756
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          736..756
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(741,743,745,747..748,751..752,755,769,771,775..776,
                     779..780,783,797,799,801,803..804,807..808,811)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          762..784
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          764..784
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          776..801
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          792..812
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..822
                     /gene="Zfp110"
                     /gene_synonym="Nrif1"
                     /coded_by="NM_001024775.1:197..2665"
                     /db_xref="GeneID:308362"
                     /db_xref="RGD:1306339"
ORIGIN      
        1 mastlpttwp hesvkfedvs ltftkeewaq ldlqqkclyr eimmenynnm isvehhfskp
       61 nvisqleeae dcwpmereir qdilpecsgp sldpgmnsfp aesplmkikv vevltlnkdv
      121 agprnaliqs lypesrenln pgnlkpakps krltdtealr qkfrhfqyee sagpqkavsr
      181 lrklchqwlq pnirskkqii ellvfeqfls alpekfrvwl esqhpedcra avallenmts
      241 vtkddaqlvc sseatdqlke krkdvatlpv tvppeepvtf qdvavgfsqe ewrllgpvqr
      301 teyhdvmlet lgnlvsvgwe ptlenraisp dspipvvkpi hdpnpkdlsr ngiqstvfei
      361 isqdrvqeih tiesnqagll qekshpqkkl sessksqegt nlhksqgsld evpprkhvkv
      421 kqkgtrkgkd rkntismtrg lrirnqqkds vewqgrgdsn pmthgysikn qrgseqgtag
      481 arrdpitltv saqfyqkatg seegrfrdns naivpdtptk ihqkspewhk vgrsnnsmss
      541 vqndqmgsga grgrdntilt halpvkihqk gyeegkvqgn rnslrhvkah qkgskgervr
      601 elstsekhvp yiknhlktse rekgrennds ikygpyiktc yrgsevrklr rannctkais
      661 rhaqqiffik ihkgsqvcrc secgkmfrns ryfsvhkkih tgerpymcma cgkafvqsss
      721 ltqhlrihsg erpfecsecg rtfndrsais qhlrthtgak pyhcqhcgka frqsshltrh
      781 erthtgerpy vcsncgkaft qsshlighqk thrikfkkqp kl
//
LOCUS       NP_001005872             513 aa            linear   ROD 27-APR-2025
DEFINITION  histone acetyltransferase KAT5 [Rattus norvegicus].
ACCESSION   NP_001005872 XP_341996
VERSION     NP_001005872.1
DBSOURCE    REFSEQ: accession NM_001005872.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Cheng,X., Ma,X., Zhu,Q., Song,D., Ding,X., Li,L., Jiang,X.,
            Wang,X., Tian,R., Su,H., Shen,Z., Chen,S., Liu,T., Gong,W., Liu,W.
            and Sun,Q.
  TITLE     Pacer Is a Mediator of mTORC1 and GSK3-TIP60 Signaling in
            Regulation of Autophagosome Maturation and Lipid Metabolism
  JOURNAL   Mol Cell 73 (4), 788-802 (2019)
   PUBMED   30704899
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Xu,S., Panikker,P., Iqbal,S. and Elefant,F.
  TITLE     Tip60 HAT Action Mediates Environmental Enrichment Induced
            Cognitive Restoration
  JOURNAL   PLoS One 11 (7), e0159623 (2016)
   PUBMED   27454757
  REMARK    GeneRIF: Our results implicate Tip60 as a critical mediator of
            EE-induced benefits, and provide broad insights into synergistic
            behavioral and epigenetic based therapeutic approaches for
            treatment of cognitive disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Obri,A., Ouararhni,K., Papin,C., Diebold,M.L., Padmanabhan,K.,
            Marek,M., Stoll,I., Roy,L., Reilly,P.T., Mak,T.W., Dimitrov,S.,
            Romier,C. and Hamiche,A.
  TITLE     ANP32E is a histone chaperone that removes H2A.Z from chromatin
  JOURNAL   Nature 505 (7485), 648-653 (2014)
   PUBMED   24463511
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Mahajan,M.A. and Stanley,F.M.
  TITLE     Insulin-activated Elk-1 recruits the TIP60/NuA4 complex to increase
            prolactin gene transcription
  JOURNAL   Mol Cell Endocrinol 382 (1), 159-169 (2014)
   PUBMED   24075908
  REMARK    GeneRIF: insulin activates prolactin gene transcription by
            activating Elk-1 that recruits the NuA4 complex to the promoter.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Xiao,J., Liu,C., Li,G., Peng,S., Hu,J., Qu,L., Lv,P., Zhang,Y.,
            Ma,D. and Chen,Y.
  TITLE     PDCD5 negatively regulates autoimmunity by upregulating FOXP3(+)
            regulatory T cells and suppressing Th17 and Th1 responses
  JOURNAL   J Autoimmun 47, 34-44 (2013)
   PUBMED   24012345
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Kioussi,C., Briata,P., Baek,S.H., Rose,D.W., Hamblet,N.S.,
            Herman,T., Ohgi,K.A., Lin,C., Gleiberman,A., Wang,J., Brault,V.,
            Ruiz-Lozano,P., Nguyen,H.D., Kemler,R., Glass,C.K.,
            Wynshaw-Boris,A. and Rosenfeld,M.G.
  TITLE     Identification of a Wnt/Dvl/beta-Catenin --> Pitx2 pathway
            mediating cell-type-specific proliferation during development
  JOURNAL   Cell 111 (5), 673-685 (2002)
   PUBMED   12464179
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Prendergast,M.A., Rogers,D.T., Mulholland,P.J., Littleton,J.M.,
            Wilkins,L.H. Jr., Self,R.L. and Nath,A.
  TITLE     Neurotoxic effects of the human immunodeficiency virus type-1
            transcription factor Tat require function of a polyamine
            sensitive-site on the N-methyl-D-aspartate receptor
  JOURNAL   Brain Res 954 (2), 300-307 (2002)
   PUBMED   12414113
  REMARK    GeneRIF: The neurotoxic effects of HIV-1 Tat are mediated, in part,
            by direct interactions with a polyamine-sensitive site on the NMDA
            receptor.
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Cao,X. and Sudhof,T.C.
  TITLE     A transcriptionally [correction of transcriptively] active complex
            of APP with Fe65 and histone acetyltransferase Tip60
  JOURNAL   Science 293 (5527), 115-120 (2001)
   PUBMED   11441186
  REMARK    Erratum:[Science 2001 Aug 24;293(5534):1436]
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Sheridan,A.M., Force,T., Yoon,H.J., O'Leary,E., Choukroun,G.,
            Taheri,M.R. and Bonventre,J.V.
  TITLE     PLIP, a novel splice variant of Tip60, interacts with group IV
            cytosolic phospholipase A(2), induces apoptosis, and potentiates
            prostaglandin production
  JOURNAL   Mol Cell Biol 21 (14), 4470-4481 (2001)
   PUBMED   11416127
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Ikura,T., Ogryzko,V.V., Grigoriev,M., Groisman,R., Wang,J.,
            Horikoshi,M., Scully,R., Qin,J. and Nakatani,Y.
  TITLE     Involvement of the TIP60 histone acetylase complex in DNA repair
            and apoptosis
  JOURNAL   Cell 102 (4), 463-473 (2000)
   PUBMED   10966108
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083879.1.
            
            On Oct 25, 2004 this sequence version replaced XP_341996.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083879.1, SRR8487227.338122.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..513
                     /product="histone acetyltransferase KAT5"
                     /EC_number="2.3.1.48"
                     /note="60 kDa Tat-interactive protein; histone
                     acetyltransferase HTATIP; protein lactyltransferase KAT5;
                     HIV-1 tat interactive protein, homolog; HIV-1 Tat
                     interactive protein, 60 kD; K(lysine) acetyltransferase 5;
                     protein acetyltransferase KAT5; protein
                     crotonyltransferase KAT5; protein
                     2-hydroxyisobutyryltransferase KAT5"
                     /calculated_mol_wt=58467
     Region          7..65
                     /region_name="Tudor-knot"
                     /note="RNA binding activity-knot of a chromodomain;
                     pfam11717"
                     /db_xref="CDD:432022"
     Site            order(22,28..30,45,47..50,54,56..59,61..62,69,72..73)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350845"
     Site            order(22,47,50,54)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350845"
     Region          43..504
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            order(44,46..51,53..57)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     Site            order(44,47,51,53,57)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Region          69..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Region          122..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            148
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            150
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            187
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Site            327
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q92993; propagated from
                     UniProtKB/Swiss-Prot (Q99MK2.2)"
     Region          368..513
                     /region_name="Interaction with ATF2.
                     /evidence=ECO:0000250|UniProtKB:Q92993"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MK2.2)"
     CDS             1..513
                     /gene="Kat5"
                     /gene_synonym="Htatip; Htatip1; Tip60"
                     /coded_by="NM_001005872.1:6..1547"
                     /db_xref="GeneID:192218"
                     /db_xref="RGD:621061"
ORIGIN      
        1 maevgeiieg crlpvlrrnq dnedewplae ilsvkdisgr klfyvhyidf nkrldewvth
       61 erldlkkiqf pkkeaktptk nglpgsrpgs perevpasaq asgktlpipv qitlrfnlpk
      121 ereaipggep dqplsssscl qpnhrstkrk vevvspatpv psetapasvf pqngsarrav
      181 aaqpgrkrks nclgtdedsq dssdgipsap rmtgslvsdr shddivtrmk niecielgrh
      241 rlkpwyfspy pqelttlpvl ylcefclkyg rslkclqrhl tkcdlrhppg neiyrkgtis
      301 ffeidgrknk sysqnlclla kcfldhktly ydtdpflfyv mteydckgfh ivgyfskeke
      361 stedynvaci ltlppyqrrg ygklliefsy elskvegktg tpekplsdlg llsyrsywsq
      421 tileilmglk sesgerpqit ineiseitsi kkedvistlq ylnlinyykg qyiltlsedi
      481 vdgheramlk rllridskcl hftpkdwskr gkw
//
LOCUS       NP_114027                494 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2C23 [Rattus norvegicus].
ACCESSION   NP_114027 XP_346586
VERSION     NP_114027.2
DBSOURCE    REFSEQ: accession NM_031839.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Munoz,M., Lopez-Oliva,M.E., Pinilla,E., Martinez,M.P., Sanchez,A.,
            Rodriguez,C., Garcia-Sacristan,A., Hernandez,M., Rivera,L. and
            Prieto,D.
  TITLE     CYP epoxygenase-derived H2O2 is involved in the endothelium-derived
            hyperpolarization (EDH) and relaxation of intrarenal arteries
  JOURNAL   Free Radic Biol Med 106, 168-183 (2017)
   PUBMED   28212823
  REMARK    GeneRIF: CYP2C11 and CYP2C23 epoxygenases were highly expressed in
            interlobar renal arteries and renal cortex, respectively, and were
            co-localized with eNOS in renal endothelial cells. These results
            demonstrate that H2O2 is involved in the EDH-type relaxant
            responses of renal arteries and that CYP 2C epoxygenases are
            physiologically relevant endothelial sources of vasodilator H2O2 in
            the kidney.
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Sarkar,P., Narayanan,J. and Harder,D.R.
  TITLE     Differential effect of amyloid beta on the cytochrome P450
            epoxygenase activity in rat brain
  JOURNAL   Neuroscience 194, 241-249 (2011)
   PUBMED   21843605
  REMARK    GeneRIF: Epoxygenase activity of cultured astrocytes and neurons
            shows reduction in total epoxyeicosatrienoic acids and DiHETE
            production (to 80% and approximately 70% of vehicle respectively)
            in presence of amyloid beta.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Wang,R.X., Chai,Q., Lu,T. and Lee,H.C.
  TITLE     Activation of vascular BK channels by docosahexaenoic acid is
            dependent on cytochrome P450 epoxygenase activity
  JOURNAL   Cardiovasc Res 90 (2), 344-352 (2011)
   PUBMED   21187320
  REMARK    GeneRIF: docosahexaenoic acid-mediated vasodilatation is mediated
            through CYP epoxygenase metabolites by activation of vascular BK
            channels
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Sun,P., Lin,D.H., Yue,P., Jiang,H., Gotlinger,K.H.,
            Schwartzman,M.L., Falck,J.R., Goli,M. and Wang,W.H.
  TITLE     High potassium intake enhances the inhibitory effect of 11,12-EET
            on ENaC
  JOURNAL   J Am Soc Nephrol 21 (10), 1667-1677 (2010)
   PUBMED   20595684
  REMARK    GeneRIF: High dietary potassium enhances the inhibitory effect of
            arachidonic acid and 11,12-epoxyeicosatrienoic acid on ENaC by
            increasing cytochrome P450 epoxygenase activity and decreasing
            soluble epoxide hydrolase activity, respectively.
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Singh,H. and Schwartzman,M.L.
  TITLE     Renal vascular cytochrome P450-derived eicosanoids in
            androgen-induced hypertension
  JOURNAL   Pharmacol Rep 60 (1), 29-37 (2008)
   PUBMED   18276983
  REMARK    GeneRIF: Increased vascular tone brought about by downregulation of
            CYP2C23 and decreased levels of vasodilatory EETs may constitute
            important factors in androgen-induced hypertension.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Muller,D.N., Theuer,J., Shagdarsuren,E., Kaergel,E., Honeck,H.,
            Park,J.K., Markovic,M., Barbosa-Sicard,E., Dechend,R., Wellner,M.,
            Kirsch,T., Fiebeler,A., Rothe,M., Haller,H., Luft,F.C. and
            Schunck,W.H.
  TITLE     A peroxisome proliferator-activated receptor-alpha activator
            induces renal CYP2C23 activity and protects from angiotensin
            II-induced renal injury
  JOURNAL   Am J Pathol 164 (2), 521-532 (2004)
   PUBMED   14742258
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Holla,V.R., Makita,K., Zaphiropoulos,P.G. and Capdevila,J.H.
  TITLE     The kidney cytochrome P-450 2C23 arachidonic acid epoxygenase is
            upregulated during dietary salt loading
  JOURNAL   J Clin Invest 104 (6), 751-760 (1999)
   PUBMED   10491410
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Imaoka,S., Wedlund,P.J., Ogawa,H., Kimura,S., Gonzalez,F.J. and
            Kim,H.Y.
  TITLE     Identification of CYP2C23 expressed in rat kidney as an arachidonic
            acid epoxygenase
  JOURNAL   J Pharmacol Exp Ther 267 (2), 1012-1016 (1993)
   PUBMED   8246128
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Karara,A., Makita,K., Jacobson,H.R., Falck,J.R., Guengerich,F.P.,
            DuBois,R.N. and Capdevila,J.H.
  TITLE     Molecular cloning, expression, and enzymatic characterization of
            the rat kidney cytochrome P-450 arachidonic acid epoxygenase
  JOURNAL   J Biol Chem 268 (18), 13565-13570 (1993)
   PUBMED   8514789
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Cook,E.A., Groenewegen,W.A., Gloger,I.S., Piggott,J.R.,
            Suckling,K.E. and Wolf,C.R.
  TITLE     cDNA and deduced amino acid sequence of a novel cytochrome P-450
            from female rat liver mRNA with high homology to P-450 IIC family
  JOURNAL   Nucleic Acids Res 18 (23), 7156 (1990)
   PUBMED   2263487
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078707.1.
            
            On Apr 5, 2007 this sequence version replaced NP_114027.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078707.1, U04733.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..494
                     /product="cytochrome P450 2C23"
                     /EC_number="1.14.14.1"
                     /note="CYPIIC23; arachidonic acid epoxygenase"
                     /calculated_mol_wt=56301
     Region          65..489
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(101,116..117,124,128,298,301..302,305..306,309,360,
                     365..366,369..370,372,431..433,437,439..441,445,448)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(112,117..118,208..209,212,218,237,241,244,296..297,
                     300..301,304..305,366,370,480..481)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00176; propagated from
                     UniProtKB/Swiss-Prot (P24470.2)"
     Site            253
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q64458; propagated from
                     UniProtKB/Swiss-Prot (P24470.2)"
     Site            379
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q64458; propagated from
                     UniProtKB/Swiss-Prot (P24470.2)"
     CDS             1..494
                     /gene="Cyp2c23"
                     /coded_by="NM_031839.3:25..1509"
                     /db_xref="GeneID:83790"
                     /db_xref="RGD:620370"
ORIGIN      
        1 mellgfttla lvvsvtclsl lsvwtklrtr grlppgptpl piignllqln lkdipaslsk
       61 lakeygpvyt lyfgtsptvv lhgydvvkea llqqgdeflg rgplpiiedt hkgyglifsn
      121 gerwkvmrrf slmtlrnfgm gkrsleervq eearclveel qktkaqpfdp tfilacapcn
      181 vicsilfndr fqynnktfln lmdllnknfq qvnsvwcqmy nlwptiikyl pgkhiefakr
      241 iddvknfile kvkehqksld panprdyidc flskieeekd nlksefhlen lavcgsnlft
      301 agtettsttl rfgllllmky pevqakvhee ldrvigrhqp psmkdkmklp ytdavlheiq
      361 ryitllpssl phavvqdtkf rdyvipkgtt vlpmlssvml dqkefanpek fdpghfldkn
      421 gcfkktdyfv pfslgkracv geslarmelf lffttllqkf slktlvepkd ldikpittgi
      481 inlpppyklc lvpr
//
LOCUS       NP_001013877             349 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell immunoglobulin and mucin domain-containing protein 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001013877 XP_220341
VERSION     NP_001013877.1
DBSOURCE    REFSEQ: accession NM_001013855.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Han,J., Seaman,W.E., Di,X., Wang,W., Willingham,M., Torti,F.M. and
            Torti,S.V.
  TITLE     Iron uptake mediated by binding of H-ferritin to the TIM-2 receptor
            in mouse cells
  JOURNAL   PLoS One 6 (8), e23800 (2011)
   PUBMED   21886823
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089832.1.
            
            On Apr 1, 2005 this sequence version replaced XP_220341.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..349
                     /product="T-cell immunoglobulin and mucin
                     domain-containing protein 2 precursor"
                     /note="T-cell immunoglobulin and mucin domain-containing
                     protein 2; TIM-2; TIMD-2; T-cell membrane protein 2;
                     T-cell immunoglobulin mucin receptor 2"
                     /calculated_mol_wt=36480
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2083
     Region          20..126
                     /region_name="IgV_TIM-3_like"
                     /note="Immunoglobulin Variable (IgV) domain of T cell
                     Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and
                     similar domains; cd20982"
                     /db_xref="CDD:409574"
     Region          20..35
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409574"
     Region          20..24
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409574"
     mat_peptide     21..349
                     /product="T-cell immunoglobulin and mucin
                     domain-containing protein 2. /id=PRO_0000042100"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVR0.1)"
                     /calculated_mol_wt=36480
     Region          27..35
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409574"
     Region          36..44
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409574"
     Region          45..51
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409574"
     Region          46..59
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409574"
     Region          61..76
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409574"
     Region          62..67
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409574"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409574"
     Region          78..109
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409574"
     Region          78..82
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409574"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVR0.1)"
     Region          89..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409574"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVR0.1)"
     Region          100..110
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409574"
     Region          110..117
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409574"
     Region          117..126
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409574"
     Region          118..126
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409574"
     Region          128..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVR0.1)"
     Site            276..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVR0.1)"
     CDS             1..349
                     /gene="Timd2"
                     /gene_synonym="Tim2"
                     /coded_by="NM_001013855.1:55..1104"
                     /db_xref="GeneID:287222"
                     /db_xref="RGD:1359571"
ORIGIN      
        1 mvqlqvfisg lllllpgava sytvvqghsv tlpciystty rdemvptcwg rgecrssyct
       61 rsliwtngyk vtyqrsnryq lkgnisegnv sltientvvs dsgpycciae ipgafyfvdy
      121 llevkaelpt spptrptntg rptttrptnt grptttrptn tgrpttterp tttgrpttte
      181 rptttgrptt istrsthvpt strvststpp tpeqtqthrs eattyypdqt taevteapsh
      241 tptdwnntat ssddswnsdt eaippqklqr nptkgfyvgm sfaallllll astvaitrym
      301 vmrknsgslr fvafpvskig asqnkvveqa riedevyiie dspyfeees
//
LOCUS       NP_001032364             415 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein F [Rattus norvegicus].
ACCESSION   NP_001032364
VERSION     NP_001032364.1
DBSOURCE    REFSEQ: accession NM_001037287.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Lo,C.S., Shi,Y., Chenier,I., Ghosh,A., Wu,C.H., Cailhier,J.F.,
            Ethier,J., Lattouf,J.B., Filep,J.G., Ingelfinger,J.R., Zhang,S.L.
            and Chan,J.S.D.
  TITLE     Heterogeneous Nuclear Ribonucleoprotein F Stimulates Sirtuin-1 Gene
            Expression and Attenuates Nephropathy Progression in Diabetic Mice
  JOURNAL   Diabetes 66 (7), 1964-1978 (2017)
   PUBMED   28424160
  REMARK    GeneRIF: hnRNP F protects kidneys against oxidative stress and
            nephropathy via stimulation of Sirtuin-1 expression and signaling
            in diabetes.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dominguez,C., Fisette,J.F., Chabot,B. and Allain,F.H.
  TITLE     Structural basis of G-tract recognition and encaging by hnRNP F
            quasi-RRMs
  JOURNAL   Nat Struct Mol Biol 17 (7), 853-861 (2010)
   PUBMED   20526337
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Wei,C.C., Zhang,S.L., Chen,Y.W., Guo,D.F., Ingelfinger,J.R.,
            Bomsztyk,K. and Chan,J.S.
  TITLE     Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen
            gene expression in kidney cells
  JOURNAL   J Biol Chem 281 (35), 25344-25355 (2006)
   PUBMED   16837467
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Wei,C.C., Guo,D.F., Zhang,S.L., Ingelfinger,J.R. and Chan,J.S.
  TITLE     Heterogenous nuclear ribonucleoprotein F modulates angiotensinogen
            gene expression in rat kidney proximal tubular cells
  JOURNAL   J Am Soc Nephrol 16 (3), 616-628 (2005)
   PUBMED   15659559
  REMARK    GeneRIF: hnRNP F binds to rANG-IRE and modulates renal ANG gene
            expression, implicating that dysregulation of hnRNP F might affect
            renin-angiotensin system activation and, subsequently, kidney
            injury in diabetes
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Yoshida,T., Makino,Y. and Tamura,T.
  TITLE     Association of the rat heterogeneous nuclear RNA-ribonucleoprotein
            F with TATA-binding protein
  JOURNAL   FEBS Lett 457 (2), 251-254 (1999)
   PUBMED   10471789
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Gamberi,C., Izaurralde,E., Beisel,C. and Mattaj,I.W.
  TITLE     Interaction between the human nuclear cap-binding protein complex
            and hnRNP F
  JOURNAL   Mol Cell Biol 17 (5), 2587-2597 (1997)
   PUBMED   9111328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK366752.1 and BC103634.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EV772154.1, EV765436.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..415
                     /product="heterogeneous nuclear ribonucleoprotein F"
                     /note="hnRNP F; ribonucleoprotein F"
                     /calculated_mol_wt=45599
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein F, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            16
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            20
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            52
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            75
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          81..86
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            116
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            120
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            150
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            173
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          179..184
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X1; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          255..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          289..363
                     /region_name="RRM3_hnRNPH_CRSF1_like"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H protein
                     family, G-rich sequence factor 1 (GRSF-1) and similar
                     proteins; cd12506"
                     /db_xref="CDD:409929"
     Site            294
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            298
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            326
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            349
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          355..360
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     CDS             1..415
                     /gene="Hnrnpf"
                     /gene_synonym="Hnrpf"
                     /coded_by="NM_001037287.1:280..1527"
                     /db_xref="GeneID:64200"
                     /db_xref="RGD:620366"
ORIGIN      
        1 mmlgpeggeg yvvklrglpw scsiedvqnf lsdctihdgv agvhfiytre grqsgeafve
       61 leseddvkla lkkdresmgh ryievfkshr temdwvlkhs gpnsadsand gfvrlrglpf
      121 gctkeeivqf fsgleivpng itlpvdpegk itgeafvqfa sqelaekalg khkerighry
      181 ievfkssqee vrsysdpplk fmsvqrpgpy drpgtarryi givkqagldr mrsgaysagy
      241 ggyeeysgls dgygfttdlf grdlsyclsg mydhrygdse ftvqsttghc vhmrglpyka
      301 tendiynffs plnpvrvhie igpdgrvtge advefathee avaamskdra nmqhryielf
      361 lnsttgasng ayssqvmqgm gvsaaqatys glesqsvsgc ygagysgqns mggyd
//
LOCUS       NP_001020931             562 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 1 [Rattus
            norvegicus].
ACCESSION   NP_001020931 XP_573373
VERSION     NP_001020931.1
DBSOURCE    REFSEQ: accession NM_001025760.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099191.1.
            
            On Jul 22, 2005 this sequence version replaced XP_573373.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099191.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..562
                     /product="zinc finger protein with KRAB and SCAN domains
                     1"
                     /note="zinc finger protein 36 (KOX 18)"
                     /calculated_mol_wt=63234
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI1.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KLI1.1)"
     Region          31..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI1.1)"
     Region          52..162
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          164..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI1.1)"
     Region          226..265
                     /region_name="KRAB_A-box"
                     /note="KRAB (Kruppel-associated box) domain -A box;
                     cd07765"
                     /db_xref="CDD:143639"
     Region          261..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI1.1)"
     Region          353..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <355..536
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          378..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(411,413,415,417..418,421..422,425,439,441,445..446,
                     449..450,453,467,469,471,473..474,477..478,481)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          434..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          490..510
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          518..538
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..562
                     /gene="Zkscan1"
                     /coded_by="NM_001025760.1:186..1874"
                     /db_xref="GeneID:498160"
                     /db_xref="RGD:1560616"
ORIGIN      
        1 mmtaesreat glspqaaqek dgivivkvee edeedhmwgq daslqetppp dpevfrqrfr
       61 rfcyqntfgp realnrlkel chqwlrpevn tkeqilellv leqflsilpk elqvwlqeyr
      121 pdsgeeavtl ledleldlsg qqvpgqvhgp emlargvvpl dpvqesssfd hheaaqshfk
      181 hssrkprlls pralpathvp apqhegnprd qamasallta dsqamvkied mavslileew
      241 gcqnlarrnl nrdsrqmnlg tvfsqgsenr ngsestskae vkgdstshge iagrfqkefg
      301 ekreqqgrvi erqqknpeek tgkekkapgp ptakekkptt gergprekgk glgrsfslsa
      361 nfnntpeeip sgakthrcde cgkcftrsss lirhkiihtg ekpyecnecg kafslnsnlv
      421 lhqrihtgek phecnecgka fshssnlilh qrihsgekpy ecnecgkafs qssdltkhqr
      481 ihtgekpyec secgkafnrn sylilhrrih trekpykctk cgkaftrsst ltlhhrihar
      541 eraseyspas ldtfgaflks cv
//
LOCUS       NP_942052                333 aa            linear   ROD 27-APR-2025
DEFINITION  serine racemase [Rattus norvegicus].
ACCESSION   NP_942052 XP_220701
VERSION     NP_942052.1
DBSOURCE    REFSEQ: accession NM_198757.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Bean,L., Bose,P.K., Rani,A. and Kumar,A.
  TITLE     Serine racemase expression profile in the prefrontal cortex and
            hippocampal subregions during aging in male and female rats
  JOURNAL   Aging (Albany NY) 16 (10), 8402-8416 (2024)
   PUBMED   38761177
  REMARK    GeneRIF: Serine racemase expression profile in the prefrontal
            cortex and hippocampal subregions during aging in male and female
            rats.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Watanabe,A., Sasaki,T., Yukami,T., Kanki,H., Sakaguchi,M.,
            Takemori,H., Kitagawa,K. and Mochizuki,H.
  TITLE     Serine racemase inhibition induces nitric oxide-mediated
            neurovascular protection during cerebral ischemia
  JOURNAL   Neuroscience 339, 139-149 (2016)
   PUBMED   27693471
  REMARK    GeneRIF: Study to demonstrate that serine racemase inhibitor
            alleviates neuronal ischemic injury. Serine racemase inhibition
            acts on the neurovascular unit as a neuroprotectant and ameliorant
            of reductions in regional cerebral blood flow.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Ito,T., Hayashida,M., Kobayashi,S., Muto,N., Hayashi,A.,
            Yoshimura,T. and Mori,H.
  TITLE     Serine racemase is involved in d-aspartate biosynthesis
  JOURNAL   J Biochem 160 (6), 345-353 (2016)
   PUBMED   27387750
  REMARK    GeneRIF: results indicate that SRR indeed acts as a d-Asp
            biosynthetic enzyme in some organs and/or tissues, and also provide
            evidences that there should be some additional enzyme for d-Asp
            synthesis in mammals.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Kolodney,G., Dumin,E., Safory,H., Rosenberg,D., Mori,H.,
            Radzishevsky,I. and Wolosker,H.
  TITLE     Nuclear Compartmentalization of Serine Racemase Regulates D-Serine
            Production: IMPLICATIONS FOR N-METHYL-D-ASPARTATE (NMDA) RECEPTOR
            ACTIVATION
  JOURNAL   J Biol Chem 290 (52), 31037-31050 (2015)
   PUBMED   26553873
  REMARK    GeneRIF: that nuclear translocation of SR provides a fail-safe
            mechanism to prevent or limit secondary NMDAR-mediated toxicity in
            nearby synapses.
            Erratum:[J Biol Chem. 2016 Feb 5;291(6):2630. doi:
            10.1074/jbc.A115.699496. Radzishevisky, Inna [corrected to
            Radzishevsky, Inna]. PMID: 26851299]
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Zhang,H., Kuang,X.L., Chang,Y., Lu,J., Jiang,H. and Wu,S.
  TITLE     Reduced serine racemase expression in aging rat cerebellum is
            associated with oxidative DNA stress and hypermethylation in the
            promoter
  JOURNAL   Brain Res 1629, 221-230 (2015)
   PUBMED   26505919
  REMARK    GeneRIF: In aging cerebellum, oxidative DNA stress was associated
            with reduced serine racemase expression.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Konno,R.
  TITLE     Rat cerebral serine racemase: amino acid deletion and truncation at
            carboxy terminus
  JOURNAL   Neurosci Lett 349 (2), 111-114 (2003)
   PUBMED   12946565
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Cook,S.P., Galve-Roperh,I., Martinez del Pozo,A. and
            Rodriguez-Crespo,I.
  TITLE     Direct calcium binding results in activation of brain serine
            racemase
  JOURNAL   J Biol Chem 277 (31), 27782-27792 (2002)
   PUBMED   12021263
REFERENCE   8  (residues 1 to 333)
  AUTHORS   De Miranda,J., Santoro,A., Engelender,S. and Wolosker,H.
  TITLE     Human serine racemase: moleular cloning, genomic organization and
            functional analysis
  JOURNAL   Gene 256 (1-2), 183-188 (2000)
   PUBMED   11054547
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Wolosker,H., Blackshaw,S. and Snyder,S.H.
  TITLE     Serine racemase: a glial enzyme synthesizing D-serine to regulate
            glutamate-N-methyl-D-aspartate neurotransmission
  JOURNAL   Proc Natl Acad Sci U S A 96 (23), 13409-13414 (1999)
   PUBMED   10557334
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Wolosker,H., Sheth,K.N., Takahashi,M., Mothet,J.P., Brady,R.O. Jr.,
            Ferris,C.D. and Snyder,S.H.
  TITLE     Purification of serine racemase: biosynthesis of the neuromodulator
            D-serine
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 721-725 (1999)
   PUBMED   9892700
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082014.1.
            
            On Dec 17, 2003 this sequence version replaced XP_220701.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082014.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..333
                     /product="serine racemase"
                     /EC_number="4.3.1.17"
                     /EC_number="5.1.1.18"
                     /EC_number="4.3.1.18"
                     /note="D-serine dehydratase; L-serine dehydratase;
                     D-serine ammonia-lyase; L-serine ammonia-lyase"
                     /calculated_mol_wt=35562
     Region          5..322
                     /region_name="Trp-synth-beta_II"
                     /note="Tryptophan synthase beta superfamily (fold type
                     II); this family of pyridoxal phosphate (PLP)-dependent
                     enzymes catalyzes beta-replacement and beta-elimination
                     reactions. This CD corresponds to
                     aminocyclopropane-1-carboxylate deaminase (ACCD),
                     tryptophan...; cl00342"
                     /db_xref="CDD:444852"
     Site            order(9..10,13,16..17,48..49,198..199,268,271..272,275,
                     279..281,315..318)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:107205"
     Site            order(56,86,185..189,313)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107205"
     Site            56
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107205"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZX7; propagated from
                     UniProtKB/Swiss-Prot (Q76EQ0.1)"
     CDS             1..333
                     /gene="Srr"
                     /coded_by="NM_198757.2:330..1331"
                     /db_xref="GeneID:303306"
                     /db_xref="RGD:735094"
ORIGIN      
        1 mcaqycisfa dvekahlniq dsvhltpvlt ssilnqiagr nlffkcelfq ktgsfkirga
       61 lnairglipd tlegkpkavv thssgnhgqa ltyaaklegi payivvpqta pnckklaiqa
      121 ygasivysep sdesrenvaq riiqetegil vhpnqepavi agqgtialev lnqvplvdal
      181 vvpvggggmv agiaitiktl kpsvkvyaae psnaddcyqs klkgeltpnl hppetiadgv
      241 kssiglntwp iirdlvddvf tvtedeikya tqlvwermkl lieptagvgl aavlsqhfqt
      301 vspevknici vlsggnvdlt slswvkqaer pap
//
LOCUS       NP_001011957             387 aa            linear   ROD 27-APR-2025
DEFINITION  RNA polymerase II elongation factor ELL3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001011957 XP_230508 XP_347327
VERSION     NP_001011957.1
DBSOURCE    REFSEQ: accession NM_001011957.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Lin,C., Garruss,A.S., Luo,Z., Guo,F. and Shilatifard,A.
  TITLE     The RNA Pol II elongation factor Ell3 marks enhancers in ES cells
            and primes future gene activation
  JOURNAL   Cell 152 (1-2), 144-156 (2013)
   PUBMED   23273992
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Luo,Z., Lin,C. and Shilatifard,A.
  TITLE     The super elongation complex (SEC) family in transcriptional
            control
  JOURNAL   Nat Rev Mol Cell Biol 13 (9), 543-547 (2012)
   PUBMED   22895430
  REMARK    Review article
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Ahn,H.J., Cha,Y., Moon,S.H., Jung,J.E. and Park,K.S.
  TITLE     Ell3 enhances differentiation of mouse embryonic stem cells by
            regulating epithelial-mesenchymal transition and apoptosis
  JOURNAL   PLoS One 7 (6), e40293 (2012)
   PUBMED   22768269
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Miller,T., Williams,K., Johnstone,R.W. and Shilatifard,A.
  TITLE     Identification, cloning, expression, and biochemical
            characterization of the testis-specific RNA polymerase II
            elongation factor ELL3
  JOURNAL   J Biol Chem 275 (41), 32052-32056 (2000)
   PUBMED   10882741
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC084693.1.
            
            On or before Feb 11, 2005 this sequence version replaced
            XP_230508.2, XP_347327.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084693.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132269,
                                           SAMD00132279 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..387
                     /product="RNA polymerase II elongation factor ELL3 isoform
                     1"
                     /note="RNA polymerase II elongation factor ELL3;
                     elongation factor RNA polymerase II-like 3"
                     /calculated_mol_wt=43672
     Region          23..>115
                     /region_name="ELL"
                     /note="RNA polymerase II elongation factor ELL; pfam10390"
                     /db_xref="CDD:463068"
     Region          127..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XFX8.1)"
     Region          186..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XFX8.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX8.1)"
     Region          281..381
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..387
                     /gene="Ell3"
                     /coded_by="NM_001011957.1:53..1216"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:296102"
                     /db_xref="RGD:1309917"
ORIGIN      
        1 megtqealsg kmrllftpaa rtsllmlrln eaalralqec qqqqvrpvia fqgqrgylrl
       61 pgpgwsclfs fivsqcgqeg ggldlvyqrl grsgpnclhc lgslrerlti waamdtipap
      121 llaqehlteg treseswqds edepeghpqm alqevsdpla snheqslpgs ssepmaqwev
      181 rnhtylsnre pdqplpssas qkrldkkrsa pitteepeek rpralplass plqglsnqds
      241 peeqdwgqda dgdsrleqsl svqsasesps peevpdyllq ystihsaeqq qayeqdfetd
      301 yaeyrilhar vgaasqrfte lgaeikrlqr gtpehkvled kivqeykkfr krypsyseek
      361 rrceylhekl shikglilef eeknrgs
//
LOCUS       NP_001104526             687 aa            linear   ROD 27-APR-2025
DEFINITION  double-stranded RNA-specific editase 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001104526
VERSION     NP_001104526.1
DBSOURCE    REFSEQ: accession NM_001111056.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Gurung,S., Evans,A.J., Wilkinson,K.A. and Henley,J.M.
  TITLE     ADAR2-mediated Q/R editing of GluK2 regulates kainate receptor
            upscaling in response to suppression of synaptic activity
  JOURNAL   J Cell Sci 131 (24) (2018)
   PUBMED   30559217
  REMARK    GeneRIF: that activity-dependent regulation of ADAR2 proteostasis
            and GluK2 Q/R editing are key determinants of kainate receptors
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Behm,M., Wahlstedt,H., Widmark,A., Eriksson,M. and Ohman,M.
  TITLE     Accumulation of nuclear ADAR2 regulates adenosine-to-inosine RNA
            editing during neuronal development
  JOURNAL   J Cell Sci 130 (4), 745-753 (2017)
   PUBMED   28082424
  REMARK    GeneRIF: lower levels of ADAR2 in the nucleus of immature neurons
            than in mature neurons.
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Tariq,A., Garncarz,W., Handl,C., Balik,A., Pusch,O. and
            Jantsch,M.F.
  TITLE     RNA-interacting proteins act as site-specific repressors of
            ADAR2-mediated RNA editing and fluctuate upon neuronal stimulation
  JOURNAL   Nucleic Acids Res 41 (4), 2581-2593 (2013)
   PUBMED   23275536
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Yang,L., Huang,P., Li,F., Zhao,L., Zhang,Y., Li,S., Gan,Z., Lin,A.,
            Li,W. and Liu,Y.
  TITLE     c-Jun amino-terminal kinase-1 mediates glucose-responsive
            upregulation of the RNA editing enzyme ADAR2 in pancreatic
            beta-cells
  JOURNAL   PLoS One 7 (11), e48611 (2012)
   PUBMED   23139803
  REMARK    GeneRIF: The JNK1 pathway may be functionally linked to the
            nutrient-sensing actions of ADAR2-mediated RNA editing in
            professional secretory cells.
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Rueter,S.M., Dawson,T.R. and Emeson,R.B.
  TITLE     Regulation of alternative splicing by RNA editing
  JOURNAL   Nature 399 (6731), 75-80 (1999)
   PUBMED   10331393
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Belcher,S.M. and Howe,J.R.
  TITLE     Characterization of RNA editing of the glutamate-receptor subunits
            GluR5 and GluR6 in granule cells during cerebellar development
  JOURNAL   Brain Res Mol Brain Res 52 (1), 130-138 (1997)
   PUBMED   9450685
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Gerber,A., O'Connell,M.A. and Keller,W.
  TITLE     Two forms of human double-stranded RNA-specific editase 1 (hRED1)
            generated by the insertion of an Alu cassette
  JOURNAL   RNA 3 (5), 453-463 (1997)
   PUBMED   9149227
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Lai,F., Chen,C.X., Carter,K.C. and Nishikura,K.
  TITLE     Editing of glutamate receptor B subunit ion channel RNAs by four
            alternatively spliced DRADA2 double-stranded RNA adenosine
            deaminases
  JOURNAL   Mol Cell Biol 17 (5), 2413-2424 (1997)
   PUBMED   9111310
REFERENCE   9  (residues 1 to 687)
  AUTHORS   O'Connell,M.A., Gerber,A. and Keller,W.
  TITLE     Purification of human double-stranded RNA-specific editase 1
            (hRED1) involved in editing of brain glutamate receptor B pre-mRNA
  JOURNAL   J Biol Chem 272 (1), 473-478 (1997)
   PUBMED   8995285
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Melcher,T., Maas,S., Herb,A., Sprengel,R., Seeburg,P.H. and
            Higuchi,M.
  TITLE     A mammalian RNA editing enzyme
  JOURNAL   Nature 379 (6564), 460-464 (1996)
   PUBMED   8559253
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB576423.1, JAXUCZ010000020.1,
            U43534.1, CB801553.1, BF388249.1 and CK840559.1.
            
            Summary: This gene encodes a double-stranded-RNA-specific adenosine
            deaminase that is involved in editing pre-mRNAs by site-specific
            conversion of adenosine (A) to inosine (I). Substrates for this
            enzyme include ionotropic glutamate receptors (GluR2-6) and
            serotonin receptor (5HT2C). Studies in rodents have shown that this
            protein can modify its own pre-mRNA by A->I editing to create a
            novel acceptor splice site, alternative splicing to which results
            in down regulation of its protein expression. Additional splicing
            events result in transcript variants encoding different isoforms.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3, also referred to as 2f)
            results from an auto RNA editing event (AA->AI) in the intronic
            sequence that creates a novel acceptor splice site, splicing to
            which inserts 47 nt into the coding region causing a frame-shift,
            compared to transcript variant 1. Translation initiation from the
            upstream AUG will result in a very short protein of 82 aa. However,
            studies reported in PMID:10331393 show that leaky translation
            initiation from an in-frame, downstream AUG allows some protein
            expression, and that this isoform (3) exhibits RNA editing
            activity. Isoform 3 is 24 aa shorter at the N-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of the transcript and
            the encoded protein are supported by transcript alignment and
            PMID:10331393.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26360176.928481.1, SRR26360194.1736135.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 10331393
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..687
                     /product="double-stranded RNA-specific editase 1 isoform
                     3"
                     /EC_number="3.5.4.37"
                     /note="RNA-editing enzyme 1; double-stranded RNA-specific
                     editase 1; dsRNA adenosine deaminase; RNA-editing
                     deaminase 1; RNA editing deaminase of glutamate receptors;
                     double stranded RNA specific deaminase RED1"
                     /calculated_mol_wt=75027
     Region          51..122
                     /region_name="DSRM_RED1_rpt1"
                     /note="first double-stranded RNA binding motif of
                     RNA-editing deaminase 1 (RED1) and similar proteins;
                     cd19895"
                     /db_xref="CDD:380724"
     Site            order(56,59..60,63..64,66,80..81,83,85,102..104,107)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380724"
     Region          208..277
                     /region_name="DSRM_RED1_rpt2"
                     /note="second double-stranded RNA binding motif of
                     RNA-editing deaminase 1 (RED1) and similar proteins;
                     cd19898"
                     /db_xref="CDD:380727"
     Site            order(211,213..214,217..218,233..235,237,239,255..258,261)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380727"
     Region          298..684
                     /region_name="ADEAMc"
                     /note="tRNA-specific and double-stranded RNA adenosine
                     deaminase (RNA-specific editase); smart00552"
                     /db_xref="CDD:214718"
     CDS             1..687
                     /gene="Adarb1"
                     /gene_synonym="Adar2; Red1"
                     /coded_by="NM_001111056.1:492..2555"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25367"
                     /db_xref="RGD:2033"
ORIGIN      
        1 mppkdsstpg pgegiplsng gggstsrkrp leegsnghsk yrlkkrrktp gpvlpknalm
       61 qlneikpglq ymllsqtgpv haplfvmsve vngqvfegsg ptkkkaklha aekalrsfvq
      121 fpnaseahla mgrtlsvntd ftsdqadfpd tlfngfetpd kseppfyvgs ngddsfsssg
      181 dvslsaspvp asltqpplpi pppfpppsgk npvmilnelr pglkydflse sgeshaksfv
      241 msvvvdgqff egsgrnkkla karaaqsala tvfnlhldqt psrqpvlseg lqlhlpqvla
      301 davsrlvlgk fsdltdnfss pharrkvlsg vvmttgtdvk dakvisvstg tkcingeyms
      361 drglalndch aeiisrrsll rflyaqlely lnnkedqkks ifqkserggf rlkdtvqfhl
      421 yistspcgda rifsphepvl egmapdshql tepadrhpnr kargqlrtki esgegtipvr
      481 snasiqtwdg vlqgerlltm scsdkiarwn vvgiqgalls ifvepiyfss iilgslyhgd
      541 hlsramyqri sniedlpply tlnkpllsgi snaearqpgk apnfsvnwtv gdtaievina
      601 ttgkdelgrp srlckhalyc rwmrvhgkvp phllrtkitk pttyheskla akeyqaakar
      661 lftafikagl gawvekpteq dqfsftp
//
LOCUS       NP_001007653             145 aa            linear   ROD 27-APR-2025
DEFINITION  DNA polymerase epsilon subunit 3 [Rattus norvegicus].
ACCESSION   NP_001007653 XP_216420
VERSION     NP_001007653.1
DBSOURCE    REFSEQ: accession NM_001007652.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Hargreaves,D.C. and Crabtree,G.R.
  TITLE     ATP-dependent chromatin remodeling: genetics, genomics and
            mechanisms
  JOURNAL   Cell Res 21 (3), 396-420 (2011)
   PUBMED   21358755
  REMARK    Review article
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Pospiech,H. and Syvaoja,J.E.
  TITLE     DNA polymerase epsilon - more than a polymerase
  JOURNAL   ScientificWorldJournal 3, 87-104 (2003)
   PUBMED   12806123
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Li,Y., Pursell,Z.F. and Linn,S.
  TITLE     Identification and cloning of two histone fold motif-containing
            subunits of HeLa DNA polymerase epsilon
  JOURNAL   J Biol Chem 275 (30), 23247-23252 (2000)
   PUBMED   10801849
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083800.1.
            
            On Nov 29, 2004 this sequence version replaced XP_216420.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083800.1, EV768825.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..145
                     /product="DNA polymerase epsilon subunit 3"
                     /EC_number="2.7.7.7"
                     /note="DNA-directed DNA polymerase epsilon 3; DNA
                     polymerase II subunit 3; DNA polymerase epsilon subunit
                     p17; polymerase (DNA directed), epsilon 3 (p17 subunit);
                     polymerase (DNA directed), epsilon 3, accessory subunit;
                     polymerase (DNA) epsilon 3, accessory subunit"
                     /calculated_mol_wt=16543
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRF9; propagated from
                     UniProtKB/Swiss-Prot (Q642A5.1)"
     Region          6..92
                     /region_name="HFD_POLE3_DPB4"
                     /note="histone-fold domain found in DNA polymerase epsilon
                     subunit 3 (POLE3) and similar proteins; cd22928"
                     /db_xref="CDD:467053"
     Site            order(6..7,39,43,46..47,50..51,66..67,75,80,86..87,90)
                     /site_type="other"
                     /note="catalytic subunit binding site [polypeptide
                     binding]"
                     /db_xref="CDD:467053"
     Site            order(14,18..19,21,29..30,32..33,36..37,39..41,43..49,
                     62..66,69,76..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467053"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRF9; propagated from
                     UniProtKB/Swiss-Prot (Q642A5.1)"
     Region          93..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642A5.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q642A5.1)"
     CDS             1..145
                     /gene="Pole3"
                     /coded_by="NM_001007652.2:14..451"
                     /db_xref="GeneID:298098"
                     /db_xref="RGD:1359475"
ORIGIN      
        1 maerpedlnl pnavitriik ealpdgvnis kearsaisra asvfvlyats cannfamkgk
       61 rktlnasdvl sameemefqr fvtplkeale ayrreqkgkk easeqkkkdk dkkdceeqdk
      121 sreeededee rldeeeqnee eevdn
//
LOCUS       NP_476460                288 aa            linear   ROD 27-APR-2025
DEFINITION  transformer-2 protein homolog beta [Rattus norvegicus].
ACCESSION   NP_476460
VERSION     NP_476460.1
DBSOURCE    REFSEQ: accession NM_057119.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.Y., Li,H.L., Su,J.B., Ding,F.H., Zhao,J.J., Chai,F., Li,Y.X.,
            Cui,S.C., Sun,F.Y., Wu,Z.Y., Xu,P. and Chen,X.H.
  TITLE     Regulation of RAGE splicing by hnRNP A1 and Tra2beta-1 and its
            potential role in AD pathogenesis
  JOURNAL   J Neurochem 133 (2), 187-198 (2015)
   PUBMED   25689357
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Storbeck,M., Hupperich,K., Gaspar,J.A., Meganathan,K., Martinez
            Carrera,L., Wirth,R., Sachinidis,A. and Wirth,B.
  TITLE     Neuronal-specific deficiency of the splicing factor Tra2b causes
            apoptosis in neurogenic areas of the developing mouse brain
  JOURNAL   PLoS One 9 (2), e89020 (2014)
   PUBMED   24586484
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Karunakaran,D.K., Congdon,S., Guerrette,T., Banday,A.R.,
            Lemoine,C., Chhaya,N. and Kanadia,R.
  TITLE     The expression analysis of Sfrs10 and Celf4 during mouse retinal
            development
  JOURNAL   Gene Expr Patterns 13 (8), 425-436 (2013)
   PUBMED   23932931
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Karunakaran,D.K., Banday,A.R., Wu,Q. and Kanadia,R.
  TITLE     Expression analysis of an evolutionarily conserved alternative
            splicing factor, Sfrs10, in age-related macular degeneration
  JOURNAL   PLoS One 8 (9), e75964 (2013)
   PUBMED   24098751
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Li,S.J., Li,Y., Cui,S.C., Qi,Y., Zhao,J.J., Liu,X.Y., Xu,P. and
            Chen,X.H.
  TITLE     Splicing factor transformer-2beta (Tra2beta) regulates the
            expression of regulator of G protein signaling 4 (RGS4) gene and is
            induced by morphine
  JOURNAL   PLoS One 8 (8), e72220 (2013)
   PUBMED   23977258
  REMARK    GeneRIF: Tra2beta regulates the expression of RGS4 gene and is
            induced by morphine.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Hofmann,Y. and Wirth,B.
  TITLE     hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN)
            via direct interaction with Htra2-beta1
  JOURNAL   Hum Mol Genet 11 (17), 2037-2049 (2002)
   PUBMED   12165565
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Venables,J.P., Elliott,D.J., Makarova,O.V., Makarov,E.M.,
            Cooke,H.J. and Eperon,I.C.
  TITLE     RBMY, a probable human spermatogenesis factor, and other hnRNP G
            proteins interact with Tra2beta and affect splicing
  JOURNAL   Hum Mol Genet 9 (5), 685-694 (2000)
   PUBMED   10749975
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Nayler,O., Stratling,W., Bourquin,J.P., Stagljar,I., Lindemann,L.,
            Jasper,H., Hartmann,A.M., Fackelmayer,F.O., Ullrich,A. and Stamm,S.
  TITLE     SAF-B protein couples transcription and pre-mRNA splicing to
            SAR/MAR elements
  JOURNAL   Nucleic Acids Res 26 (15), 3542-3549 (1998)
   PUBMED   9671816
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Tacke,R., Tohyama,M., Ogawa,S. and Manley,J.L.
  TITLE     Human Tra2 proteins are sequence-specific activators of pre-mRNA
            splicing
  JOURNAL   Cell 93 (1), 139-148 (1998)
   PUBMED   9546399
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Matsuo,N., Ogawa,S., Imai,Y., Takagi,T., Tohyama,M., Stern,D. and
            Wanaka,A.
  TITLE     Cloning of a novel RNA binding polypeptide (RA301) induced by
            hypoxia/reoxygenation
  JOURNAL   J Biol Chem 270 (47), 28216-28222 (1995)
   PUBMED   7499316
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D49708.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D49708.1, FQ212414.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..288
                     /product="transformer-2 protein homolog beta"
                     /note="RA301; TRA2-beta; TRA-2 beta; transformer-2 protein
                     homolog B; splicing factor, arginine/serine-rich 10
                     (transformer 2 homolog, Drosophila); serine/arginine-rich
                     splicing factor 10; transformer 2 beta homolog"
                     /calculated_mol_wt=33535
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62997.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Region          117..196
                     /region_name="RRM_TRA2"
                     /note="RNA recognition motif (RRM) found in transformer-2
                     protein homolog TRA2-alpha, TRA2-beta and similar
                     proteins; cd12363"
                     /db_xref="CDD:409798"
     Site            order(119,123..124,148,150,159,161,163,165,187..190,
                     193..196)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409798"
     Region          193..230
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P62997.1)"
     Region          196..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62997.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Site            241
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62995; Dimethylated
                     arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62995;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62995; propagated from
                     UniProtKB/Swiss-Prot (P62997.1)"
     Region          242..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62997.1)"
     CDS             1..288
                     /gene="Tra2b"
                     /gene_synonym="Sfrs10; Srsf10"
                     /coded_by="NM_057119.1:136..1002"
                     /db_xref="GeneID:117259"
                     /db_xref="RGD:619886"
ORIGIN      
        1 msdsgeqnyg eresrsasrs gsahgsgksa rhtparsrsk edsrrsrsks rsrsesrsrs
       61 rrssrrhytr srsrsrshrr srsrsysrdy rrrhshshsp mstrrrhvgn ranpdpnccl
      121 gvfglslytt erdlrevfsk ygpiadvsiv ydqqsrrsrg fafvyfenvd dakeakeran
      181 gmeldgrrir vdfsitkrph tptpgiymgr ptygssrrrd yydrgydrgy ddrdyysrsy
      241 rggggggggw raaqdrdqiy rrrspspyys rggyrsrsrs rsysprry
//
LOCUS       NP_001012478             366 aa            linear   ROD 27-APR-2025
DEFINITION  septin-1 [Rattus norvegicus].
ACCESSION   NP_001012478 XP_215071
VERSION     NP_001012478.1
DBSOURCE    REFSEQ: accession NM_001012460.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Zhu,J., Qi,S.T., Wang,Y.P., Wang,Z.B., Ouyang,Y.C., Hou,Y.,
            Schatten,H. and Sun,Q.Y.
  TITLE     Septin1 is required for spindle assembly and chromosome congression
            in mouse oocytes
  JOURNAL   Dev Dyn 240 (10), 2281-2289 (2011)
   PUBMED   21932310
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Chen,T.C., Lee,S.A., Hong,T.M., Shih,J.Y., Lai,J.M., Chiou,H.Y.,
            Yang,S.C., Chan,C.H., Kao,C.Y., Yang,P.C. and Huang,C.Y.
  TITLE     From midbody protein-protein interaction network construction to
            novel regulators in cytokinesis
  JOURNAL   J Proteome Res 8 (11), 4943-4953 (2009)
   PUBMED   19799413
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089897.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215071.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089897.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132274,
                                           SAMD00132279 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..366
                     /product="septin-1"
                     /EC_number="3.1.5.1"
                     /calculated_mol_wt=41927
     Region          23..295
                     /region_name="Septin"
                     /note="pfam00735"
                     /db_xref="CDD:395596"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(34..40,89,92,170..171,173,229..230)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            64..72
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            66
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          89..92
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            89..92
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(91..126,127..136)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          170..173
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            170..173
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            229..231
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000250|UniProtKB:Q8WYJ6; propagated from
                     UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P42209; propagated from
                     UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000250|UniProtKB:Q8WYJ6; propagated from
                     UniProtKB/Swiss-Prot (Q5EB96.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000250|UniProtKB:Q8WYJ6; propagated from
                     UniProtKB/Swiss-Prot (Q5EB96.1)"
     Region          347..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB96.1)"
     CDS             1..366
                     /gene="Septin1"
                     /gene_synonym="Sept1"
                     /coded_by="NM_001012460.1:44..1144"
                     /db_xref="GeneID:293507"
                     /db_xref="RGD:1307216"
ORIGIN      
        1 mdkeyvgfaa lpnqlhrksv kkgfdftlmv agesglgkst linslfltnl yedrqvpdas
       61 arttqtltie rrgveieegg ikvkltlvdt pgfgdsvdcs dcwlpvvrfi eeqfeqylrd
      121 esglnrkniq dsrvhcclyf ispfgrglrp ldvaflravh ekvniipvig kadallpret
      181 qvlkqkirdq lkeeeiniyq fpecdsdede efkkqneemk enipfavvgs sevvregtrp
      241 vrgrryswgt vevenphhcd flnlrrmlvq thlqdlkevt hdllyegyra rclqslarpg
      301 ardrasrskl srqsateipl pmlpladtek lirekdeelr rmqemlekmq aqmqqsqaqg
      361 eqsdvl
//
LOCUS       NP_001008294             397 aa            linear   ROD 27-APR-2025
DEFINITION  dimethyladenosine transferase 2, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001008294 XP_213965
VERSION     NP_001008294.1
DBSOURCE    REFSEQ: accession NM_001008293.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Hillen,H.S., Morozov,Y.I., Sarfallah,A., Temiakov,D. and Cramer,P.
  TITLE     Structural Basis of Mitochondrial Transcription Initiation
  JOURNAL   Cell 171 (5), 1072-1081 (2017)
   PUBMED   29149603
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Watanabe,A., Arai,M., Koitabashi,N., Niwano,K., Ohyama,Y.,
            Yamada,Y., Kato,N. and Kurabayashi,M.
  TITLE     Mitochondrial transcription factors TFAM and TFB2M regulate Serca2
            gene transcription
  JOURNAL   Cardiovasc Res 90 (1), 57-67 (2011)
   PUBMED   21113058
  REMARK    GeneRIF: Mitochondrial transcription factors TFAM and TFB2M
            regulate Serca2 gene transcription in cardiac myocytes.
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Litonin,D., Sologub,M., Shi,Y., Savkina,M., Anikin,M.,
            Falkenberg,M., Gustafsson,C.M. and Temiakov,D.
  TITLE     Human mitochondrial transcription revisited: only TFAM and TFB2M
            are required for transcription of the mitochondrial genes in vitro
  JOURNAL   J Biol Chem 285 (24), 18129-18133 (2010)
   PUBMED   20410300
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Bogenhagen,D.F., Rousseau,D. and Burke,S.
  TITLE     The layered structure of human mitochondrial DNA nucleoids
  JOURNAL   J Biol Chem 283 (6), 3665-3675 (2008)
   PUBMED   18063578
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085870.1.
            
            On Dec 16, 2004 this sequence version replaced XP_213965.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085870.1, SRR8487227.24141.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..397
                     /product="dimethyladenosine transferase 2, mitochondrial"
                     /note="mtTFB2; dimethyladenosine transferase 2,
                     mitochondrial-like; mitochondrial 12S rRNA dimethylase 2;
                     mitochondrial transcription factor B2;
                     S-adenosylmethionine-6-N', N'-adenosyl(rRNA)
                     dimethyltransferase 2"
                     /calculated_mol_wt=41186
     transit_peptide 1..44
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5U2T7.1)"
                     /calculated_mol_wt=4854
     mat_peptide     45..397
                     /product="Dimethyladenosine transferase 2, mitochondrial.
                     /id=PRO_0000273181"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T7.1)"
                     /calculated_mol_wt=41186
     Region          82..380
                     /region_name="RsmA"
                     /note="16S rRNA A1518 and A1519 N6-dimethyltransferase
                     RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase
                     activity) [Translation, ribosomal structure and
                     biogenesis]; COG0030"
                     /db_xref="CDD:439801"
     Region          329..330
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9H5Q4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T7.1)"
     CDS             1..397
                     /gene="Tfb2m"
                     /coded_by="NM_001008293.1:91..1284"
                     /db_xref="GeneID:289307"
                     /db_xref="RGD:1307091"
ORIGIN      
        1 mrglamrlpp rlalsvlagr gpscilgsga atrkdwqern rrsfsdlytq plpdcdfees
       61 sswthksrse ptrhiackks arnlvrdlle hqnpshqlil ecnpgpgilt gallkagarv
      121 vafesekmfi phleslrkna dgelqvvhcd ffkidpryqe lvrpdvnsht ifqnlgikav
      181 pwsagvpikv fgilpnkher rllwkilfdl yscesiyryg rvelnmfise kefrkliatp
      241 krpdlyqvlg vlwqvaceik flhmepwssf svhaenghle kskhseslnl lkqnlylvrm
      301 tprrtlften lsplnydmff hlvkhcfgkr napiihhlrs lstvdpinil rqirkrpgdt
      361 aakmyphdfk rlfetierse dsvfkwiydy csddsel
//
LOCUS       NP_852097                809 aa            linear   ROD 27-APR-2025
DEFINITION  BLOC-2 complex member HPS6 [Rattus norvegicus].
ACCESSION   NP_852097
VERSION     NP_852097.1
DBSOURCE    REFSEQ: accession NM_181432.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Li,K., Yang,L., Zhang,C., Niu,Y., Li,W. and Liu,J.J.
  TITLE     HPS6 interacts with dynactin p150Glued to mediate retrograde
            trafficking and maturation of lysosomes
  JOURNAL   J Cell Sci 127 (Pt 21), 4574-4588 (2014)
   PUBMED   25189619
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Bultema,J.J., Ambrosio,A.L., Burek,C.L. and Di Pietro,S.M.
  TITLE     BLOC-2, AP-3, and AP-1 proteins function in concert with Rab38 and
            Rab32 proteins to mediate protein trafficking to lysosome-related
            organelles
  JOURNAL   J Biol Chem 287 (23), 19550-19563 (2012)
   PUBMED   22511774
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Huizing,M., Pederson,B., Hess,R.A., Griffin,A., Helip-Wooley,A.,
            Westbroek,W., Dorward,H., O'Brien,K.J., Golas,G., Tsilou,E.,
            White,J.G. and Gahl,W.A.
  TITLE     Clinical and cellular characterisation of Hermansky-Pudlak syndrome
            type 6
  JOURNAL   J Med Genet 46 (12), 803-810 (2009)
   PUBMED   19843503
REFERENCE   5  (residues 1 to 809)
  AUTHORS   Di Pietro,S.M., Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Characterization of BLOC-2, a complex containing the
            Hermansky-Pudlak syndrome proteins HPS3, HPS5 and HPS6
  JOURNAL   Traffic 5 (4), 276-283 (2004)
   PUBMED   15030569
REFERENCE   6  (residues 1 to 809)
  AUTHORS   Zhang,Q., Zhao,B., Li,W., Oiso,N., Novak,E.K., Rusiniak,M.E.,
            Gautam,R., Chintala,S., O'Brien,E.P., Zhang,Y., Roe,B.A.,
            Elliott,R.W., Eicher,E.M., Liang,P., Kratz,C., Legius,E.,
            Spritz,R.A., O'Sullivan,T.N., Copeland,N.G., Jenkins,N.A. and
            Swank,R.T.
  TITLE     Ru2 and Ru encode mouse orthologs of the genes mutated in human
            Hermansky-Pudlak syndrome types 5 and 6
  JOURNAL   Nat Genet 33 (2), 145-153 (2003)
   PUBMED   12548288
REFERENCE   7  (residues 1 to 809)
  AUTHORS   Mayerhofer,A., Russell,L.D., Grothe,C., Rudolf,M. and Gratzl,M.
  TITLE     Presence and localization of a 30-kDa basic fibroblast growth
            factor-like protein in rodent testes
  JOURNAL   Endocrinology 129 (2), 921-924 (1991)
   PUBMED   1855483
REFERENCE   8  (residues 1 to 809)
  AUTHORS   Moore,K.J., Swing,D.A., Copeland,N.G. and Jenkins,N.A.
  TITLE     Interaction of the murine dilute suppressor gene (dsu) with
            fourteen coat color mutations
  JOURNAL   Genetics 125 (2), 421-430 (1990)
   PUBMED   2379821
  REMARK    Erratum:[Genetics 1990 Sep;126(1):285]
REFERENCE   9  (residues 1 to 809)
  AUTHORS   Novak,E.K., Hui,S.W. and Swank,R.T.
  TITLE     Platelet storage pool deficiency in mouse pigment mutations
            associated with seven distinct genetic loci
  JOURNAL   Blood 63 (3), 536-544 (1984)
   PUBMED   6696991
REFERENCE   10 (residues 1 to 809)
  AUTHORS   Markert,C.L. and Silvers,W.K.
  TITLE     The Effects of Genotype and Cell Environment on Melanoblast
            Differentiation in the House Mouse
  JOURNAL   Genetics 41 (3), 429-450 (1956)
   PUBMED   17247639
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086975.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC086975.1, SRR8487227.207505.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..809
                     /product="BLOC-2 complex member HPS6"
                     /note="ruby-eye-like protein; hermansky-Pudlak syndrome 6
                     protein homolog; ruby-eye protein homolog"
                     /calculated_mol_wt=87332
     Region          2..386
                     /region_name="HPS6"
                     /note="Hermansky-Pudlak syndrome 6 protein N-terminal
                     domain; pfam15702"
                     /db_xref="CDD:464811"
     Region          401..766
                     /region_name="HPS6_C"
                     /note="Hermansky-Pudlak syndrome 6 protein C-terminal
                     domain; pfam20468"
                     /db_xref="CDD:466617"
     Region          747..809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M733.1)"
     CDS             1..809
                     /gene="Hps6"
                     /gene_synonym="Hsp6"
                     /coded_by="NM_181432.2:69..2498"
                     /db_xref="GeneID:309446"
                     /db_xref="RGD:631341"
ORIGIN      
        1 mkragtlrll sdlsnftgaa rlrellagdp ailvrcspdg rhllllrppg spapqllvav
       61 rgpglplera wsegdpspld vffvpwlarp alilvwesgl tevwgvgmep gwkllqstel
      121 cpdggarvma vaatrgrlvw ceerqpgved qpgqlsmafn hcvcvktldt sgeagtklgc
      181 thillhhcps fgliasrkel flvptsttwp gvahvlliws pskgkvivaa pslglshsks
      241 lnpkqgdtwd frtllrglpg flspreplav htwapssqgl llldlkgkvs lvqchggtrt
      301 vgllqeapvg lqgsaalgtf hgtlacvlgs tlelldmssg rllerkvlst drvhlleppa
      361 pgvkneedle trgalrllsa lglfcvcwea pqglevpsdk dlvfeeacgy yqrrslrgtq
      421 ltpeelrhns mfrapqalas ilqghlppsa llttlraelr dyrsieqlka qlvagddeet
      481 gwtelaehev arllrthltg dqlaqfntif qalptaawsa tlqalqlqpd rsgrlrsqap
      541 pdvwkkvlra ptagkehpng ilppfellcq clgqlepqwl ppfvelaqqq ggpgwgaegp
      601 slplyrrals vlgeegkrpe alelelllgs grpkavlqav rqlikkeqwe raleagltld
      661 ssspllrsei fnlllaefaq hrrldthlpl lcrlcppeva pdelllllrt hlpddagatp
      721 fpepgaepga eppltvglvr alleqtgaqg rssgpvqstf edilwdsgtp pptpprgpmt
      781 tlqasdhpgq eawgpsgqgl gaadvgvhs
//
LOCUS       NP_001019496             160 aa            linear   ROD 27-APR-2025
DEFINITION  cell cycle regulator of non-homologous end joining [Rattus
            norvegicus].
ACCESSION   NP_001019496 XP_575427
VERSION     NP_001019496.1
DBSOURCE    REFSEQ: accession NM_001024325.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Arnoult,N., Correia,A., Ma,J., Merlo,A., Garcia-Gomez,S., Maric,M.,
            Tognetti,M., Benner,C.W., Boulton,S.J., Saghatelian,A. and
            Karlseder,J.
  TITLE     Regulation of DNA repair pathway choice in S and G2 phases by the
            NHEJ inhibitor CYREN
  JOURNAL   Nature 549 (7673), 548-552 (2017)
   PUBMED   28959974
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Slavoff,S.A., Heo,J., Budnik,B.A., Hanakahi,L.A. and Saghatelian,A.
  TITLE     A human short open reading frame (sORF)-encoded polypeptide that
            stimulates DNA end joining
  JOURNAL   J Biol Chem 289 (16), 10950-10957 (2014)
   PUBMED   24610814
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Agarwal,S., Harada,J., Schreifels,J., Lech,P., Nikolai,B.,
            Yamaguchi,T., Chanda,S.K. and Somia,N.V.
  TITLE     Isolation, characterization, and genetic complementation of a
            cellular mutant resistant to retroviral infection
  JOURNAL   Proc Natl Acad Sci U S A 103 (43), 15933-15938 (2006)
   PUBMED   17043244
  REMARK    GeneRIF: Characterizes the hamster ortholog and suggests that it
            may modulate the ability of the proteasome to degrade retroviral
            cores upon cellular infection.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079043.1.
            
            On May 27, 2005 this sequence version replaced XP_575427.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079043.1, CK470463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06680432
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..160
                     /product="cell cycle regulator of non-homologous end
                     joining"
                     /note="modulator of retrovirus infection homolog"
                     /calculated_mol_wt=17356
     Region          1..21
                     /region_name="KBM. /evidence=ECO:0000250|UniProtKB:Q9BWK5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH4.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BWK5; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH4.1)"
     Region          57..160
                     /region_name="MRI"
                     /note="Modulator of retrovirus infection; pfam15325"
                     /db_xref="CDD:434635"
     Region          78..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH4.1)"
     Region          150..160
                     /region_name="XLM. /evidence=ECO:0000250|UniProtKB:Q9BWK5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH4.1)"
     CDS             1..160
                     /gene="Cyren"
                     /gene_synonym="Mri"
                     /coded_by="NM_001024325.1:416..898"
                     /db_xref="GeneID:500077"
                     /db_xref="RGD:1563238"
ORIGIN      
        1 metlksdnkk rvlpswmtap gnerkvvsvk takrkqtaai rvgaatrapa ketvycmnea
       61 emvdvalgil iegrkqekpw eqpslvapdk lqlsppcses phtsspgsss eeedsrtdsp
      121 alglspargp easnspcsrs peegkeeede lkyvreiffs
//
LOCUS       NP_955424                515 aa            linear   ROD 27-APR-2025
DEFINITION  TOX high mobility group box family member 2 [Rattus norvegicus].
ACCESSION   NP_955424 XP_230852
VERSION     NP_955424.2
DBSOURCE    REFSEQ: accession NM_199392.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Vong,Q.P., Leung,W.H., Houston,J., Li,Y., Rooney,B., Holladay,M.,
            Oostendorp,R.A. and Leung,W.
  TITLE     TOX2 regulates human natural killer cell development by controlling
            T-BET expression
  JOURNAL   Blood 124 (26), 3905-3913 (2014)
   PUBMED   25352127
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Kajitani,T., Mizutani,T., Yamada,K., Yazawa,T., Sekiguchi,T.,
            Yoshino,M., Kawata,H. and Miyamoto,K.
  TITLE     Cloning and characterization of granulosa cell high-mobility group
            (HMG)-box protein-1, a novel HMG-box transcriptional regulator
            strongly expressed in rat ovarian granulosa cells
  JOURNAL   Endocrinology 145 (5), 2307-2318 (2004)
   PUBMED   14764631
  REMARK    GeneRIF: data strongly suggest that granulosa cell HMG-box
            protein-1(GCX-1) is a novel transcriptional activator that is
            expressed in reproductive tissues involving the
            hypothalamo-pituitary-gonadal axis, and functions as a regulator of
            follicular development
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB096685.1.
            
            On Jun 22, 2007 this sequence version replaced NP_955424.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB096685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..515
                     /product="TOX high mobility group box family member 2"
                     /note="granulosa cell HMG box protein 1"
                     /calculated_mol_wt=54123
     Region          247..316
                     /region_name="HMG-box_TOX-like"
                     /note="high mobility group (HMG)-box found in the TOX high
                     mobility group box family; cd21995"
                     /db_xref="CDD:438811"
     Site            order(247..248,250..254,257..258,265,277..278,281,
                     284..285,292,296,299,303,306)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438811"
     CDS             1..515
                     /gene="Tox2"
                     /gene_synonym="GCX-1; Gcx1"
                     /coded_by="NM_199392.2:34..1581"
                     /db_xref="GeneID:311615"
                     /db_xref="RGD:735184"
ORIGIN      
        1 mdvrlypsap avgarpgaep aglahldyyh cgkfdgdsay vgmsdgnpel lstsqtynsq
       61 gesnedyeip pitppnlpep sllhlgdhea gyhslchgla pngllpaysy qamdlpaimv
      121 snmlaqdghl lsgqlptiqe mvhsevaayd sgrpgpllgr pamlashmsa lsqsqlisqm
      181 glrsgiahss psppgsksat pspssstqee esdahfkisg ekrpstdpgk kaknpkkkkk
      241 kdpnepqkpv sayalffrdt qaaikgqnps atfgdvskiv asmwdslgee qkqaykrkte
      301 aakkeylkal aayraslvsk sppdqgeakn aqanppakml ppkqpmyamp glasfltpsd
      361 lqafrsaasp aslartlgsk allpglstsp pppsfplsps lhqqlplpph aqgtllsppl
      421 smspapqppv lpapmalqvq lamspsppgp qdfphisdfp sgsgsrspgp snpsssgdwd
      481 gsypsgergl gtcrlcrssp ppttspknlq epsar
//
LOCUS       NP_001012016             569 aa            linear   ROD 27-APR-2025
DEFINITION  TBCC domain-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001012016 XP_221321
VERSION     NP_001012016.1
DBSOURCE    REFSEQ: accession NM_001012016.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Goncalves,J., Nolasco,S., Nascimento,R., Lopez Fanarraga,M.,
            Zabala,J.C. and Soares,H.
  TITLE     TBCCD1, a new centrosomal protein, is required for centrosome and
            Golgi apparatus positioning
  JOURNAL   EMBO Rep 11 (3), 194-200 (2010)
   PUBMED   20168327
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089823.1.
            
            On Feb 11, 2005 this sequence version replaced XP_221321.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089823.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..569
                     /product="TBCC domain-containing protein 1"
                     /note="crystallin, gamma S"
                     /calculated_mol_wt=64562
     Region          329..444
                     /region_name="TBCC"
                     /note="Tubulin binding cofactor C; pfam07986"
                     /db_xref="CDD:462331"
     CDS             1..569
                     /gene="Tbccd1"
                     /gene_synonym="Crygs"
                     /coded_by="NM_001012016.1:282..1991"
                     /db_xref="GeneID:303830"
                     /db_xref="RGD:1309604"
ORIGIN      
        1 mdqsgvllwv kaepfivgal qepppsklsl hylkkvaayv rtraterayp rlywptwrhi
       61 acgklqlakd lawlyfeifd nlsertpeer lewseilsnc ttkdevekqr nqlsvdtlqf
      121 llflyiqqln kislrtsfig eewpsprnrp kspspaerss chnknwndyn hqafvcdhls
      181 ellellldpe qltesfhstq ssllsreavt alsfliegtv srtkkvyplh elalwqplha
      241 angfskiskt fslykleawl raclttnpfg lsaclqsgkk lawahkvega tkrakiacna
      301 hmaprshriv vmsqvcnqtl akssetlvga hvrahrcnes fiyllsplrs mtiekcrnst
      361 fvlgpvetal hlhgcenlkv iavchrlsvs stigctfhim tpsrplilsg nqtvtfapfh
      421 thypmledhm artglatvpn ywddpmvlgg egtdtrvfql lppsefyvfv tpfemegdta
      481 eipgglppay qkalahreqr ihnwqktvke arltkeqrkq fqvlvenkfy ewlvstghrq
      541 qldslvpppa asnqvakkdl twshgalet
//
LOCUS       NP_064467                147 aa            linear   ROD 27-APR-2025
DEFINITION  ribonuclease 4 precursor [Rattus norvegicus].
ACCESSION   NP_064467
VERSION     NP_064467.1
DBSOURCE    REFSEQ: accession NM_020082.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Premzl,M.
  TITLE     Comparative genomic analysis of eutherian ribonuclease A genes
  JOURNAL   Mol Genet Genomics 289 (2), 161-167 (2014)
   PUBMED   24337645
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Boj,S.F., van Es,J.H., Huch,M., Li,V.S., Jose,A., Hatzis,P.,
            Mokry,M., Haegebarth,A., van den Born,M., Chambon,P., Voshol,P.,
            Dor,Y., Cuppen,E., Fillat,C. and Clevers,H.
  TITLE     Diabetes risk gene and Wnt effector Tcf7l2/TCF4 controls hepatic
            response to perinatal and adult metabolic demand
  JOURNAL   Cell 151 (7), 1595-1607 (2012)
   PUBMED   23260145
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Zhao,W., Kote-Jarai,Z., van Santen,Y., Hofsteenge,J. and
            Beintema,J.J.
  TITLE     Ribonucleases from rat and bovine liver: purification, specificity
            and structural characterization
  JOURNAL   Biochim Biophys Acta 1384 (1), 55-65 (1998)
   PUBMED   9602056
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Shapiro,R., Fett,J.W., Strydom,D.J. and Vallee,B.L.
  TITLE     Isolation and characterization of a human colon carcinoma-secreted
            enzyme with pancreatic ribonuclease-like activity
  JOURNAL   Biochemistry 25 (23), 7255-7264 (1986)
   PUBMED   3467790
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070953.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070953.1, FQ214834.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..147
                     /product="ribonuclease 4 precursor"
                     /note="RL3; RNase 4; ribonuclease 4; ribonuclease A b1;
                     ribonuclease, RNase A family 4"
                     /calculated_mol_wt=13852
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3070
     mat_peptide     29..147
                     /product="Ribonuclease 4. /id=PRO_0000030887"
                     /note="propagated from UniProtKB/Swiss-Prot (O55004.1)"
                     /calculated_mol_wt=13852
     Region          29..147
                     /region_name="RNAse_Pc"
                     /note="Pancreatic ribonuclease; smart00092"
                     /db_xref="CDD:128403"
     Site            29
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P15467; propagated from
                     UniProtKB/Swiss-Prot (O55004.1)"
     Site            order(36..45,52,56,58..60,68,71..76,107,126,142)
                     /site_type="active"
                     /note="dimerization with domain swap [active]"
                     /db_xref="CDD:119387"
     Site            order(40,68,72,98,108,144..145)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:119387"
     Site            order(69,101,110,125,127,129..130,132)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119387"
     CDS             1..147
                     /gene="Rnase4"
                     /gene_synonym="Rab1"
                     /coded_by="NM_020082.2:66..509"
                     /db_xref="GeneID:56759"
                     /db_xref="RGD:61823"
ORIGIN      
        1 mdiqrtqsll llllltllgl glvqpsygqd rmyqrflrqh vdpegtggsd nycnvmmqrr
       61 rmtstqckrf ntfihediwn irsicdtani pckngnmnch egivrvtdcr etgssvphnc
      121 ryrarastrr vviacegtpe vpvhfdr
//
LOCUS       NP_445890                683 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF103 [Rattus norvegicus].
ACCESSION   NP_445890 XP_346700
VERSION     NP_445890.2
DBSOURCE    REFSEQ: accession NM_053438.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Maruyama,Y., Yamada,M., Takahashi,K. and Yamada,M.
  TITLE     Ubiquitin ligase Kf-1 is involved in the endoplasmic
            reticulum-associated degradation pathway
  JOURNAL   Biochem Biophys Res Commun 374 (4), 737-741 (2008)
   PUBMED   18675248
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Yamada,M., Yamada,M., Yamazaki,S., Takahashi,K., Nishioka,G.,
            Kudo,K., Ozawa,H., Yamada,S., Kiuchi,Y., Kamijima,K., Higuchi,T.
            and Momose,K.
  TITLE     Identification of a novel gene with RING-H2 finger motif induced
            after chronic antidepressant treatment in rat brain
  JOURNAL   Biochem Biophys Res Commun 278 (1), 150-157 (2000)
   PUBMED   11071867
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Lorick,K.L., Jensen,J.P., Fang,S., Ong,A.M., Hatakeyama,S. and
            Weissman,A.M.
  TITLE     RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
            ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11364-11369 (1999)
   PUBMED   10500182
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100629.1.
            
            On Dec 5, 2007 this sequence version replaced NP_445890.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100629.1, AF306394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..683
                     /product="E3 ubiquitin-protein ligase RNF103"
                     /EC_number="2.3.2.27"
                     /note="zfp-103; zinc finger protein 103; RING-type E3
                     ubiquitin transferase RNF103"
                     /calculated_mol_wt=79049
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPZ8.1)"
     Site            326..346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPZ8.1)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPZ8.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPZ8.1)"
     Region          525..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPZ8.1)"
     Region          613..667
                     /region_name="RING-H2_RNF103"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 103 (RNF103) and similar proteins; cd16473"
                     /db_xref="CDD:438136"
     CDS             1..683
                     /gene="Rnf103"
                     /gene_synonym="Adrg34; Kf1; Zfp103"
                     /coded_by="NM_053438.2:30..2081"
                     /db_xref="GeneID:84508"
                     /db_xref="RGD:620586"
ORIGIN      
        1 mwlklfflll yflilfvlar ffeaivwyet gifatqlvdp valsfkklkt ilecrglgys
       61 glpekkdvre lveksgdlme gelysalkee easesvsstn fsgemhfyel vedtkdgiwl
      121 vqviandrsp lvgkihwekm vkkvsrfgir tgtfncssdp rycrrrgwvr stlimsvpqt
      181 stskgkvmlk eysgrkieve hifkwitaha asriktiynv ehlkeewnks dqywvkiylf
      241 anldqppaff salsikftgr vefifvnven wnnksymtdi giynmpsyil rtpegiyryg
      301 nhtgefislq amdsflrslq pevndlfvls lvlvnlmawm dlfitqgati krfvvlistl
      361 gtynslliis wlpvlgflql pyldsfyeys lrllrysntt tlaswvradw mfysshpalf
      421 lstylghgll idyfekkrrr snndevnann lewlsslwdw ytsylfhpia sfqnfpvdsd
      481 wdedpdlfle rlafpdlwlh pliptdyikn lpmwrfkclg aqseeemses sqdtendsds
      541 dntdtfsssk dvfedkqnvh sspgrtsrcd teacscankc cqtspcerkr rsygshntke
      601 dmepdwltwp agtlhctecv vclenfengc llmglpcghv fhqncivmwl aggrhccpvc
      661 rwpsykkkqp yaqqqplsnd aps
//
LOCUS       NP_001014004             304 aa            linear   ROD 27-APR-2025
DEFINITION  calcium release-activated calcium channel protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001014004 XP_222178
VERSION     NP_001014004.1
DBSOURCE    REFSEQ: accession NM_001013982.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Falcon,D., Calderon-Sanchez,E.M., Mayoral-Gonzalez,I.,
            Martin-Bornez,M., Dominguez-Rodriguez,A., Gutierrez-Carretero,E.,
            Ordonez-Fernandez,A., Rosado,J.A. and Smani,T.
  TITLE     Inhibition of adenylyl cyclase 8 prevents the upregulation of Orai1
            channel, which improves cardiac function after myocardial
            infarction
  JOURNAL   Mol Ther 32 (3), 646-662 (2024)
   PUBMED   38291755
  REMARK    GeneRIF: Inhibition of adenylyl cyclase 8 prevents the upregulation
            of Orai1 channel, which improves cardiac function after myocardial
            infarction.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Zhang,S. and Zang,W.
  TITLE     The Role and Mechanism of STIM1/Orai1-Regulated Ca2+ Influx in
            Myocardial Hypertrophy in Type 2 Diabetes Mellitus
  JOURNAL   Ann Clin Lab Sci 54 (1), 17-25 (2024)
   PUBMED   38514055
  REMARK    GeneRIF: The Role and Mechanism of STIM1/Orai1-Regulated Ca[2+]
            Influx in Myocardial Hypertrophy in Type 2 Diabetes Mellitus.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Sukkar,B., Oktay,L., Sahaboglu,A., Moayedi,A., Zenouri,S.,
            Al-Maghout,T., Canto,A., Miranda,M., Durdagi,S. and Hosseinzadeh,Z.
  TITLE     Inhibition of altered Orai1 channels in Muller cells protects
            photoreceptors in retinal degeneration
  JOURNAL   Glia 71 (11), 2511-2526 (2023)
   PUBMED   37533369
  REMARK    GeneRIF: Inhibition of altered Orai1 channels in Muller cells
            protects photoreceptors in retinal degeneration.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Angulo,J., Fernandez,A., Sevilleja-Ortiz,A., Sanchez-Ferrer,A.,
            Rodriguez-Manas,L. and El Assar,M.
  TITLE     Upregulation of Orai Channels Contributes to Aging-Related Vascular
            Alterations in Rat Coronary Arteries
  JOURNAL   Int J Mol Sci 24 (17), 13402 (2023)
   PUBMED   37686206
  REMARK    GeneRIF: Upregulation of Orai Channels Contributes to Aging-Related
            Vascular Alterations in Rat Coronary Arteries.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Zhu,M., Lv,B., Ge,W., Cui,Z., Zhao,K., Feng,Y. and Yang,X.
  TITLE     Suppression of store-operated Ca2+ entry regulated by silencing
            Orai1 inhibits C6 glioma cell motility via decreasing Pyk2 activity
            and promoting focal adhesion
  JOURNAL   Cell Cycle 19 (24), 3468-3479 (2020)
   PUBMED   33269647
  REMARK    GeneRIF: Suppression of store-operated Ca(2+) entry regulated by
            silencing Orai1 inhibits C6 glioma cell motility via decreasing
            Pyk2 activity and promoting focal adhesion.
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Prakriya,M., Feske,S., Gwack,Y., Srikanth,S., Rao,A. and Hogan,P.G.
  TITLE     Orai1 is an essential pore subunit of the CRAC channel
  JOURNAL   Nature 443 (7108), 230-233 (2006)
   PUBMED   16921383
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Mercer,J.C., Dehaven,W.I., Smyth,J.T., Wedel,B., Boyles,R.R.,
            Bird,G.S. and Putney,J.W. Jr.
  TITLE     Large store-operated calcium selective currents due to
            co-expression of Orai1 or Orai2 with the intracellular calcium
            sensor, Stim1
  JOURNAL   J Biol Chem 281 (34), 24979-24990 (2006)
   PUBMED   16807233
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Soboloff,J., Spassova,M.A., Tang,X.D., Hewavitharana,T., Xu,W. and
            Gill,D.L.
  TITLE     Orai1 and STIM reconstitute store-operated calcium channel function
  JOURNAL   J Biol Chem 281 (30), 20661-20665 (2006)
   PUBMED   16766533
  REMARK    GeneRIF: suppression of store-operated channels function by Orai1
            overexpression likely reflects a required stoichiometry between
            STIM1 and Orai1 [Orai1]
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Peinelt,C., Vig,M., Koomoa,D.L., Beck,A., Nadler,M.J.,
            Koblan-Huberson,M., Lis,A., Fleig,A., Penner,R. and Kinet,J.P.
  TITLE     Amplification of CRAC current by STIM1 and CRACM1 (Orai1)
  JOURNAL   Nat Cell Biol 8 (7), 771-773 (2006)
   PUBMED   16733527
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Vig,M., Peinelt,C., Beck,A., Koomoa,D.L., Rabah,D.,
            Koblan-Huberson,M., Kraft,S., Turner,H., Fleig,A., Penner,R. and
            Kinet,J.P.
  TITLE     CRACM1 is a plasma membrane protein essential for store-operated
            Ca2+ entry
  JOURNAL   Science 312 (5777), 1220-1223 (2006)
   PUBMED   16645049
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088225.1.
            
            On Apr 20, 2005 this sequence version replaced XP_222178.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088225.1, EU644749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..304
                     /product="calcium release-activated calcium channel
                     protein 1"
                     /note="calcium release-activated calcium modulator 1;
                     protein orai-1; transmembrane protein 142A"
                     /calculated_mol_wt=32909
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Region          3..49
                     /region_name="Required for generation of inwardly
                     rectifying CRAC currents.
                     /evidence=ECO:0000250|UniProtKB:Q96D31"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Region          39..60
                     /region_name="AKAP5 association region.
                     /evidence=ECO:0000250|UniProtKB:Q96D31"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Region          71..91
                     /region_name="Interaction with STIM1.
                     /evidence=ECO:0000250|UniProtKB:Q96D31"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Region          74..270
                     /region_name="Orai-1"
                     /note="Mediator of CRAC channel activity; pfam07856"
                     /db_xref="CDD:462291"
     Site            89..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            107
                     /site_type="other"
                     /note="Confers selective permeability to Ca(2+) ions.
                     /evidence=ECO:0000250|UniProtKB:Q96D31; propagated from
                     UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            225
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Region          275..295
                     /region_name="Interaction with STIM1.
                     /evidence=ECO:0000250|UniProtKB:Q96D31"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M848.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96D31; propagated from
                     UniProtKB/Swiss-Prot (Q5M848.1)"
     CDS             1..304
                     /gene="Orai1"
                     /gene_synonym="RGD1311873"
                     /coded_by="NM_001013982.1:86..1000"
                     /db_xref="GeneID:304496"
                     /db_xref="RGD:1311873"
ORIGIN      
        1 mhpepapppn nsnpelplsg gsstsgsrrs rrrsgdgept gapplppppa vsypdwigqs
       61 ysevmslneh smqalswrkl ylsraklkas srtsallsgf amvamvevql dtdhdyppgl
      121 livfsacttv lvavhlfalm istcilpnie avsnvhnlns vkesphermh rhielawafs
      181 tvigtllfla evvllcwvkf lplkrqagqp sptkpptepa vvvanssnng gitpgeaaai
      241 astaimvpcg lvfivfavhf yrslvshktd rqfqelnela efarlqdqld hrgdhsltpg
      301 thya
//
LOCUS       NP_445977                598 aa            linear   ROD 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX52 [Rattus norvegicus].
ACCESSION   NP_445977
VERSION     NP_445977.1
DBSOURCE    REFSEQ: accession NM_053525.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Saad,Y., Garrett,M.R., Manickavasagam,E., Yerga-Woolwine,S.,
            Farms,P., Radecki,T. and Joe,B.
  TITLE     Fine-mapping and comprehensive transcript analysis reveals
            nonsynonymous variants within a novel 1.17 Mb blood pressure QTL
            region on rat chromosome 10
  JOURNAL   Genomics 89 (3), 343-353 (2007)
   PUBMED   17218081
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Venema,J., Bousquet-Antonelli,C., Gelugne,J.P.,
            Caizergues-Ferrer,M. and Tollervey,D.
  TITLE     Rok1p is a putative RNA helicase required for rRNA processing
  JOURNAL   Mol Cell Biol 17 (6), 3398-3407 (1997)
   PUBMED   9154839
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Murakami,M., Kudo,I., Fujimori,Y., Suga,H. and Inoue,K.
  TITLE     Group II phospholipase A2 inhibitors suppressed
            lysophosphatidylserine-dependent degranulation of rat peritoneal
            mast cells
  JOURNAL   Biochem Biophys Res Commun 181 (2), 714-721 (1991)
   PUBMED   1721808
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB055628.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB055628.1, BC089107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132271, SAMD00132274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..598
                     /product="probable ATP-dependent RNA helicase DDX52"
                     /EC_number="3.6.4.13"
                     /note="DEAD (Asp-Glu-Ala-Asp) box polypeptide 52; DEAD box
                     protein 52; rROK1L; ATP-dependent, RNA helicase; DEAD-box
                     helicase 52"
                     /calculated_mol_wt=67109
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2R4; propagated from
                     UniProtKB/Swiss-Prot (Q99PT0.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2R4; propagated from
                     UniProtKB/Swiss-Prot (Q99PT0.1)"
     Region          59..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PT0.1)"
     Region          163..534
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          166..194
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PT0.1)"
     Region          319..322
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PT0.1)"
     Region          578..598
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PT0.1)"
     CDS             1..598
                     /gene="Ddx52"
                     /gene_synonym="Rok1"
                     /coded_by="NM_053525.1:7..1803"
                     /db_xref="GeneID:85432"
                     /db_xref="RGD:621743"
ORIGIN      
        1 mdsydlfrrl gagakfdvkr fsadatrfqv gkrkfgsdss etvkgldffg nkksvsdecg
       61 glqtqqelqn eettegglle rskepkkkkr kkmtadvpaq edldgtiqwt ssveaklqdk
      121 kangekklts eklehlrkek inffrnkhki hvqgtdlpdp iatfqqldqe ykisprllqn
      181 ildagfqvpt piqmqaipvm lhgrellasa ptgsgktlaf sipilmqlkq ptnkgfralv
      241 isptrelasq ihrelikise gtgfrihmih kaaiaakkfg pksskkfdil vttpnrliyl
      301 lkqeppgidl tsvewlvvde sdklfedgkt gfrdqlasif lactspkvrr amfsatfayd
      361 veqwcklnld nivsvsigar nsavetveqe llfvgsetgk llamrelvkk gfnppvlvfv
      421 qsierakelf heliyeginv dvihaertqq qrdntvhsfr agkiwvlict allargidfk
      481 gvnlvinydf ptssveyihr igrtgragnr gkavtffted dkpllrsvan viqqagcpvp
      541 eyikgfqkll skqkkkmikk pleresistt pkyfleqakq kkvagqnskk ketlkgks
//
LOCUS       NP_058716                462 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-6 receptor subunit alpha precursor [Rattus norvegicus].
ACCESSION   NP_058716
VERSION     NP_058716.2
DBSOURCE    REFSEQ: accession NM_017020.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   He,Q., Lin,Y., Liao,B., Zhou,L., Ai,J., Jin,X., Li,H. and Wang,K.
  TITLE     The role of interleukin-6/interleukin-6 receptor signaling in the
            mechanical stress-induced extracellular matrix remodeling of
            bladder smooth muscle
  JOURNAL   Arch Biochem Biophys 702, 108674 (2021)
   PUBMED   33189652
  REMARK    GeneRIF: The role of interleukin-6/interleukin-6 receptor signaling
            in the mechanical stress-induced extracellular matrix remodeling of
            bladder smooth muscle.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Leo,A., Nesci,V., Tallarico,M., Amodio,N., Gallo Cantafio,E.M., De
            Sarro,G., Constanti,A., Russo,E. and Citraro,R.
  TITLE     IL-6 Receptor Blockade by Tocilizumab Has Anti-absence and
            Anti-epileptogenic Effects in the WAG/Rij Rat Model of Absence
            Epilepsy
  JOURNAL   Neurotherapeutics 17 (4), 2004-2014 (2020)
   PUBMED   32681356
  REMARK    GeneRIF: IL-6 Receptor Blockade by Tocilizumab Has Anti-absence and
            Anti-epileptogenic Effects in the WAG/Rij Rat Model of Absence
            Epilepsy.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Zhang,D., Mou,J.Y., Wang,F., Liu,J. and Hu,X.
  TITLE     CRNDE enhances neuropathic pain via modulating miR-136/IL6R axis in
            CCI rat models
  JOURNAL   J Cell Physiol 234 (12), 22234-22241 (2019)
   PUBMED   31131445
  REMARK    GeneRIF: CRNDE could induce interleukin 6 receptor (IL6R)
            expression positively.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Li,N.C., Wei,X.X., Hu,Y.L., Hou,X. and Xu,H.
  TITLE     Aerobic exercise blocks interleukin-6 levels and germ cell
            apoptosis in obese rats
  JOURNAL   Andrologia 50 (2) (2018)
   PUBMED   28776758
  REMARK    GeneRIF: Aerobic exercise improves the lipid metabolism disorder
            and interferes with germ cell apoptosis by reducing interleukin-6
            and interleukin-6 receptor expression in nutritional obesity rat
            model.
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Zhang,J.Z., Liu,C.M., Peng,H.P. and Zhang,Y.
  TITLE     Association of genetic variations in IL-6/IL-6R pathway genes with
            gastric cancer risk in a Chinese population
  JOURNAL   Gene 623, 1-4 (2017)
   PUBMED   28442395
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Watanabe,D., Yoshimura,R., Khalil,M., Yoshida,K., Kishimoto,T.,
            Taga,T. and Kiyama,H.
  TITLE     Characteristic localization of gp130 (the signal-transducing
            receptor component used in common for IL-6/IL-11/CNTF/LIF/OSM) in
            the rat brain
  JOURNAL   Eur J Neurosci 8 (8), 1630-1640 (1996)
   PUBMED   8921254
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Hoffmann,R., Henninger,H.P., Schulze-Specking,A. and Decker,K.
  TITLE     Regulation of interleukin-6 receptor expression in rat Kupffer
            cells: modulation by cytokines, dexamethasone and prostaglandin E2
  JOURNAL   J Hepatol 21 (4), 543-550 (1994)
   PUBMED   7814800
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Fiorillo,M.T., Toniatti,C., Van Snick,J. and Ciliberto,G.
  TITLE     Expression of the murine interleukin 6 receptor in hepatoma cells:
            the intracytoplasmic domain is not required for interleukin 6
            signal transduction
  JOURNAL   Eur J Immunol 22 (3), 799-804 (1992)
   PUBMED   1312474
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Hibi,M., Murakami,M., Saito,M., Hirano,T., Taga,T. and Kishimoto,T.
  TITLE     Molecular cloning and expression of an IL-6 signal transducer,
            gp130
  JOURNAL   Cell 63 (6), 1149-1157 (1990)
   PUBMED   2261637
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Baumann,M., Baumann,H. and Fey,G.H.
  TITLE     Molecular cloning, characterization and functional expression of
            the rat liver interleukin 6 receptor
  JOURNAL   J Biol Chem 265 (32), 19853-19862 (1990)
   PUBMED   2174054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jan 1, 2008 this sequence version replaced NP_058716.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M58587.1, SRR22582416.948486.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..462
                     /product="interleukin-6 receptor subunit alpha precursor"
                     /note="interleukin-6 receptor subunit alpha; IL-6R 1;
                     IL-6R-alpha; IL-6RA; IL-6R subunit alpha; IL-6 receptor
                     subunit alpha; interleukin 6 receptor, alpha"
                     /calculated_mol_wt=48657
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1797
     mat_peptide     20..462
                     /product="Interleukin-6 receptor subunit alpha.
                     /id=PRO_0000010898"
                     /note="propagated from UniProtKB/Swiss-Prot (P22273.2)"
                     /calculated_mol_wt=48657
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Region          34..106
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          43..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P08887; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Region          57..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          75..79
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Region          89..94
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          99..102
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          114..210
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Site            order(213,281,296)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          213..290
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P08887; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Site            order(297..298,300..301)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          300..304
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P22273.2)"
     Site            354..355
                     /site_type="cleavage"
                     /note="Cleavage, by ADAM10 and ADAM17.
                     /evidence=ECO:0000250|UniProtKB:P08887; propagated from
                     UniProtKB/Swiss-Prot (P22273.2)"
     Site            365..385
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22273.2)"
     Region          423..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22273.2)"
     CDS             1..462
                     /gene="Il6r"
                     /gene_synonym="IL6R1; Il6ra"
                     /coded_by="NM_017020.3:20..1408"
                     /db_xref="GeneID:24499"
                     /db_xref="RGD:2902"
ORIGIN      
        1 mlavgctllv allaapaval vlgscralev angtvtslpg atvtlicpgk eaagnatihw
       61 vysgsqsrew tttgntlvlr avqvndtghy lcflddhlvg tvpllvdvpp eepklscfrk
      121 nplvnafcew hpsstpsptt kavmfakkin ttngksdfqv pcqysqqlks fsceveileg
      181 dkvyhivslc vansvgsrss hnvvfqslkm vqpdppanlv vsaipgrprw lkvswqdpes
      241 wdpsyyllqf elryrpvwsk tftvwplqva qhqcvihdal rgvkhvvqvr gkeefdigqw
      301 skwspevtgt pwlaeprttp agipgnptqv svedydnhed qygssteats vlapvqgssp
      361 iplptflvag gslafglllc vfiilrlkkk wksqaekesk ttspppyplg plkptfllvp
      421 lltpsgshns sgtdntgshs clgvrdpqcp ndnsnrdylf pr
//
LOCUS       NP_445937                 89 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A6 [Rattus norvegicus].
ACCESSION   NP_445937
VERSION     NP_445937.1
DBSOURCE    REFSEQ: accession NM_053485.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Zhang,X.F., Ma,J.X., Wang,Y.L. and Ma,X.L.
  TITLE     Calcyclin (S100A6) Attenuates Inflammatory Response and Mediates
            Apoptosis of Chondrocytes in Osteoarthritis via the PI3K/AKT
            Pathway
  JOURNAL   Orthop Surg 13 (3), 1094-1101 (2021)
   PUBMED   33942537
  REMARK    GeneRIF: Calcyclin (S100A6) Attenuates Inflammatory Response and
            Mediates Apoptosis of Chondrocytes in Osteoarthritis via the
            PI3K/AKT Pathway.
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Haldar,B., Hamilton,C.L., Solodushko,V., Abney,K.A., Alexeyev,M.,
            Honkanen,R.E., Scammell,J.G. and Cioffi,D.L.
  TITLE     S100A6 is a positive regulator of PPP5C-FKBP51-dependent regulation
            of endothelial calcium signaling
  JOURNAL   FASEB J 34 (2), 3179-3196 (2020)
   PUBMED   31916625
  REMARK    GeneRIF: S100A6 is a positive regulator of PPP5C-FKBP51-dependent
            regulation of endothelial calcium signaling.
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Mofid,A., Newman,N.S., Lee,P.J., Abbasi,C., Matkar,P.N.,
            Rudenko,D., Kuliszewski,M.A., Chen,H.H., Afrasiabi,K.,
            Tsoporis,J.N., Gramolini,A.O., Connelly,K.A., Parker,T.G. and
            Leong-Poi,H.
  TITLE     Cardiac Overexpression of S100A6 Attenuates Cardiomyocyte Apoptosis
            and Reduces Infarct Size After Myocardial Ischemia-Reperfusion
  JOURNAL   J Am Heart Assoc 6 (2), e004738 (2017)
   PUBMED   28174168
  REMARK    GeneRIF: S100A6 overexpression by ultrasound-targeted microbubble
            destruction helps ameliorate myocardial ischemia-reperfusion,
            resulting in lower mortality and improved left ventricular systolic
            function post-ischemia-reperfusion via attenuation of apoptosis,
            reduction in cardiac hypertrophy, and reduced infarct size
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Zhou,X., Wang,P., Michal,J.J., Wang,Y., Zhao,J., Jiang,Z. and
            Liu,B.
  TITLE     Molecular characterization of the porcine S100A6 gene and analysis
            of its expression in pigs infected with highly pathogenic porcine
            reproductive and respiratory syndrome virus (HP-PRRSV)
  JOURNAL   J Appl Genet 56 (3), 355-363 (2015)
   PUBMED   25480733
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Deloulme,J.C., Assard,N., Mbele,G.O., Mangin,C., Kuwano,R. and
            Baudier,J.
  TITLE     S100A6 and S100A11 are specific targets of the calcium- and
            zinc-binding S100B protein in vivo
  JOURNAL   J Biol Chem 275 (45), 35302-35310 (2000)
   PUBMED   10913138
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Konrad,L. and Aumuller,G.
  TITLE     Calcyclin is differentially expressed in rat testicular cells
  JOURNAL   Biochim Biophys Acta 1489 (2-3), 440-444 (1999)
   PUBMED   10673048
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Young,L.H., Yang,X. and Voigt,J.M.
  TITLE     Alteration of gene expression in rat mammary tumors induced by
            N-methyl-N-nitrosourea
  JOURNAL   Mol Carcinog 15 (4), 251-260 (1996)
   PUBMED   8634083
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Filipek,A., Heizmann,C.W. and Kuznicki,J.
  TITLE     Calcyclin is a calcium and zinc binding protein
  JOURNAL   FEBS Lett 264 (2), 263-266 (1990)
   PUBMED   2358072
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Murphy,L.C., Murphy,L.J., Tsuyuki,D., Duckworth,M.L. and Shiu,R.P.
  TITLE     Cloning and characterization of a cDNA encoding a highly conserved,
            putative calcium binding protein, identified by an anti-prolactin
            receptor antiserum
  JOURNAL   J Biol Chem 263 (5), 2397-2401 (1988)
   PUBMED   2448309
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF140232.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF140232.1, BC166598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..89
                     /product="protein S100-A6"
                     /note="calcyclin; prolactin receptor-associated protein;
                     calcium binding protein A6 (calcyclin)"
                     /calculated_mol_wt=9903
     Region          1..88
                     /region_name="S-100A6"
                     /note="S-100A6 domain found in proteins similar to S100A6.
                     S100A6 is a member of the S100 domain family within
                     EF-hand Ca2+-binding proteins superfamily. Note that the
                     S-100 hierarchy, to which this S-100A6 group belongs,
                     contains only S-100 EF-hand domains; cd05029"
                     /db_xref="CDD:240155"
     Site            order(1,4..5,8..9,11..13,16,27..28,69..71,74..75,78..79,
                     81..82,85,87..88)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240155"
     Site            order(20,23,25,28,33,61,63,65,67,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240155"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06703; propagated from
                     UniProtKB/Swiss-Prot (P05964.3)"
     Site            47
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P14069; propagated from
                     UniProtKB/Swiss-Prot (P05964.3)"
     CDS             1..89
                     /gene="S100a6"
                     /coded_by="NM_053485.2:40..309"
                     /db_xref="GeneID:85247"
                     /db_xref="RGD:620264"
ORIGIN      
        1 macpldqaig llvaifhkys gkegdkhtls kkelkeliqk eltigaklqd aeiarlmddl
       61 drnkdqevnf qeyvaflgal aliynealk
//
LOCUS       NP_001020220             316 aa            linear   ROD 27-APR-2025
DEFINITION  acrosin-binding protein isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001020220 XP_575666
VERSION     NP_001020220.1
DBSOURCE    REFSEQ: accession NM_001025049.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Kanemori,Y., Koga,Y., Sudo,M., Kang,W., Kashiwabara,S., Ikawa,M.,
            Hasuwa,H., Nagashima,K., Ishikawa,Y., Ogonuki,N., Ogura,A. and
            Baba,T.
  TITLE     Biogenesis of sperm acrosome is regulated by pre-mRNA alternative
            splicing of Acrbp in the mouse
  JOURNAL   Proc Natl Acad Sci U S A 113 (26), E3696-E3705 (2016)
   PUBMED   27303034
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kanemori,Y., Ryu,J.H., Sudo,M., Niida-Araida,Y., Kodaira,K.,
            Takenaka,M., Kohno,N., Sugiura,S., Kashiwabara,S. and Baba,T.
  TITLE     Two functional forms of ACRBP/sp32 are produced by pre-mRNA
            alternative splicing in the mouse
  JOURNAL   Biol Reprod 88 (4), 105 (2013)
   PUBMED   23426433
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Tardif,S., Guyonnet,B., Cormier,N. and Cornwall,G.A.
  TITLE     Alteration in the processing of the ACRBP/sp32 protein and sperm
            head/acrosome malformations in proprotein convertase 4 (PCSK4) null
            mice
  JOURNAL   Mol Hum Reprod 18 (6), 298-307 (2012)
   PUBMED   22357636
REFERENCE   4  (residues 1 to 316)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Dube,C., Leclerc,P., Baba,T., Reyes-Moreno,C. and Bailey,J.L.
  TITLE     The proacrosin binding protein, sp32, is tyrosine phosphorylated
            during capacitation of pig sperm
  JOURNAL   J Androl 26 (4), 519-528 (2005)
   PUBMED   15955892
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Baba,T., Niida,Y., Michikawa,Y., Kashiwabara,S., Kodaira,K.,
            Takenaka,M., Kohno,N., Gerton,G.L. and Arai,Y.
  TITLE     An acrosomal protein, sp32, in mammalian sperm is a binding protein
            specific for two proacrosins and an acrosin intermediate
  JOURNAL   J Biol Chem 269 (13), 10133-10140 (1994)
   PUBMED   8144514
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079212.1.
            
            On Jun 25, 2005 this sequence version replaced XP_575666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079212.1, CK604050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..316
                     /product="acrosin-binding protein isoform 1 precursor"
                     /note="proacrosin-binding protein sp32; proacrosin binding
                     protein; acrosin-binding protein, 60 kDa form"
                     /calculated_mol_wt=33320
     Region          1..239
                     /region_name="PBP_sp32"
                     /note="Proacrosin binding protein sp32; pfam07222"
                     /db_xref="CDD:429354"
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2614
     Region          25..104
                     /region_name="Pro-ACR binding.
                     /evidence=ECO:0000250|UniProtKB:Q3V140"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY33.2)"
     Region          181..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY33.2)"
     CDS             1..316
                     /gene="Acrbp"
                     /coded_by="NM_001025049.1:96..1046"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:500316"
                     /db_xref="RGD:1564880"
ORIGIN      
        1 mklaasfllm llevlllpet plsaeealas tpgsplsste yerffalltp twkaettcrl
       61 rathgcrnpt lvqldqyenh glvpdgavcs dlpyaswfes fcqfaqyrcs nhvyyakrvr
      121 csqpvsilsp ntlkevessa evpltsvttp ivsratateh qafqpwperl nnnveellqs
      181 slslggkeqq ssrklgleqq hkqeqiqehk leeaqeqeeq eeeeeeeeak qeegqgteeg
      241 ldsvsrlqsd sepkfqsksl ssnpsfftpr vrevesaplm meniqelirs aqemdemnel
      301 yddswrsqst gryrkl
//
LOCUS       NP_958738               1839 aa            linear   ROD 27-APR-2025
DEFINITION  SH3 and multiple ankyrin repeat domains protein 2 isoform a [Rattus
            norvegicus].
ACCESSION   NP_958738
VERSION     NP_958738.1
DBSOURCE    REFSEQ: accession NM_201350.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1839)
  AUTHORS   Li,N., Ren,C., Li,S., Yu,W., Jin,K. and Ji,X.
  TITLE     Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway
  JOURNAL   Prog Neurobiol 230, 102514 (2023)
   PUBMED   37574039
  REMARK    GeneRIF: Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway.
REFERENCE   2  (residues 1 to 1839)
  AUTHORS   Fu,Y., Liu,D., Guo,J., Long,H., Xiao,W., Xiao,W., Feng,L., Luo,Z.
            and Xiao,B.
  TITLE     Dynamic Change of Shanks Gene mRNA Expression and DNA Methylation
            in Epileptic Rat Model and Human Patients
  JOURNAL   Mol Neurobiol 57 (9), 3712-3726 (2020)
   PUBMED   32564287
  REMARK    GeneRIF: Dynamic Change of Shanks Gene mRNA Expression and DNA
            Methylation in Epileptic Rat Model and Human Patients.
REFERENCE   3  (residues 1 to 1839)
  AUTHORS   Ishida,H., Skorobogatov,A., Yamniuk,A.P. and Vogel,H.J.
  TITLE     Solution structures of the SH3 domains from Shank scaffold proteins
            and their interactions with Cav1.3 calcium channels
  JOURNAL   FEBS Lett 592 (16), 2786-2797 (2018)
   PUBMED   30058071
REFERENCE   4  (residues 1 to 1839)
  AUTHORS   Modi,M.E., Brooks,J.M., Guilmette,E.R., Beyna,M., Graf,R., Reim,D.,
            Schmeisser,M.J., Boeckers,T.M., O'Donnell,P. and Buhl,D.L.
  TITLE     Hyperactivity and Hypermotivation Associated With Increased
            Striatal mGluR1 Signaling in a Shank2 Rat Model of Autism
  JOURNAL   Front Mol Neurosci 11, 107 (2018)
   PUBMED   29970986
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1839)
  AUTHORS   Shi,R., Redman,P., Ghose,D., Hwang,H., Liu,Y., Ren,X., Ding,L.J.,
            Liu,M., Jones,K.J. and Xu,W.
  TITLE     Shank Proteins Differentially Regulate Synaptic Transmission
  JOURNAL   eNeuro 4 (6) (2017)
   PUBMED   29250591
  REMARK    GeneRIF: Loss of scaffold proteins via knockdown of Shank1 or
            Shank2, but not Shank3, led to a reduction of the number but not
            the unitary response of AMPAR-containing synapses. Only when both
            Shank1 and Shank2 were knocked down, were both the number and the
            unitary response of active synapses reduced. This reduction was
            accompanied by a decrease in NMDAR-mediated synaptic response.
            Erratum:[eNeuro. 2018 Mar 19;5(1):ENEURO.0073-18.2018. doi:
            10.1523/ENEURO.0073-18.2018. PMID: 29569864]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1839)
  AUTHORS   Boeckers,T.M., Winter,C., Smalla,K.H., Kreutz,M.R., Bockmann,J.,
            Seidenbecher,C., Garner,C.C. and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated proteins ProSAP1 and ProSAP2
            interact with synaptic proteins of the SAPAP/GKAP family
  JOURNAL   Biochem Biophys Res Commun 264 (1), 247-252 (1999)
   PUBMED   10527873
REFERENCE   7  (residues 1 to 1839)
  AUTHORS   Lim,S., Naisbitt,S., Yoon,J., Hwang,J.I., Suh,P.G., Sheng,M. and
            Kim,E.
  TITLE     Characterization of the Shank family of synaptic proteins. Multiple
            genes, alternative splicing, and differential expression in brain
            and development
  JOURNAL   J Biol Chem 274 (41), 29510-29518 (1999)
   PUBMED   10506216
REFERENCE   8  (residues 1 to 1839)
  AUTHORS   Boeckers,T.M., Kreutz,M.R., Winter,C., Zuschratter,W., Smalla,K.H.,
            Sanmarti-Vila,L., Wex,H., Langnaese,K., Bockmann,J., Garner,C.C.
            and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated protein-1/cortactin binding protein
            1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the
            postsynaptic density
  JOURNAL   J Neurosci 19 (15), 6506-6518 (1999)
   PUBMED   10414979
REFERENCE   9  (residues 1 to 1839)
  AUTHORS   Zitzer,H., Richter,D. and Kreienkamp,H.J.
  TITLE     Agonist-dependent interaction of the rat somatostatin receptor
            subtype 2 with cortactin-binding protein 1
  JOURNAL   J Biol Chem 274 (26), 18153-18156 (1999)
   PUBMED   10373412
REFERENCE   10 (residues 1 to 1839)
  AUTHORS   Du,Y., Weed,S.A., Xiong,W.C., Marshall,T.D. and Parsons,J.T.
  TITLE     Identification of a novel cortactin SH3 domain-binding protein and
            its localization to growth cones of cultured neurons
  JOURNAL   Mol Cell Biol 18 (10), 5838-5851 (1998)
   PUBMED   9742101
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY298755.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY298755.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1839
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..1839
                     /product="SH3 and multiple ankyrin repeat domains protein
                     2 isoform a"
                     /note="SH3 and multiple ankyrin repeat domains protein 2;
                     GKAP/SAPAP-interacting protein; proline-rich
                     synapse-associated protein 1; cortactin-binding protein 1;
                     SH3 and multiple ankyrin repeat domains protein 2-like;
                     SH3/ankyrin domain gene 2"
                     /calculated_mol_wt=199725
     Region          55..142
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          149..388
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          197..228
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(230,232,236..237,240..242,244..245,249,252,261,263,
                     265,303..304,307..309,311..312,316,319,328,330,332,
                     336..337,340..342,344..345,349,352,361)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          230..261
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          263..328
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          330..361
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          530..581
                     /region_name="SH3_Shank2"
                     /note="Src homology 3 domain of SH3 and multiple ankyrin
                     repeat domains protein 2; cd11983"
                     /db_xref="CDD:212916"
     Site            order(536,538,541,545,563..564,577,579..580)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212916"
     Region          620..721
                     /region_name="PDZ_SHANK1_3-like"
                     /note="PDZ domain of SH3 and multiple ankyrin repeat
                     domains protein 1 (SHANK1), SHANK2, SHANK3, and related
                     domains; cd06746"
                     /db_xref="CDD:467228"
     Site            order(620..625,655..658,693,695,718)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467228"
     Site            order(637..643,667,670,699,703,706..707)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467228"
     Region          <1058..1467
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1772..1837
                     /region_name="SAM_Shank1,2,3"
                     /note="SAM domain of Shank1,2,3 family proteins; cd09506"
                     /db_xref="CDD:188905"
     Site            order(1775..1777,1779,1793..1794,1807)
                     /site_type="other"
                     /note="polymer interface (interfiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     Site            order(1792..1793,1825)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188905"
     Site            order(1816,1818,1823)
                     /site_type="other"
                     /note="polymer interface (intrafiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     CDS             1..1839
                     /gene="Shank2"
                     /gene_synonym="CortBP1; ProSAP1; Shank2E; Spank-3"
                     /coded_by="NM_201350.1:104..5623"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:171093"
                     /db_xref="RGD:628772"
ORIGIN      
        1 mprsptssed emaqsfsdys vgsesdsske etiydtirat tekpggvkme dlqgntlvir
       61 vviqdlqqtk cirfnpdatv wvakqrilct lnqglkdvln yglfqpasng rdgkfldeer
      121 llreypqpmg qgvpslefry kkrvykqsnl dekqlarlht ktnlkkfmdh tqhrsveklv
      181 klldrgldpn fhdletgetp ltlaaqldgs mevikalrng gahldfrsrd gmtalhkaar
      241 mrnqvalktl lelgaspdyk dsygltplyh taivggdpyc celllhehas vcckdengwh
      301 eihqacrygh vqhlehllfy gadmsaqnas gntalhical ynqdscarvl lfrggdkelk
      361 nynsqtpfqv aiiagnfela eyiknhketd ivpfreapay snrrrrppnt laaprvllrs
      421 nsdnnlnaga pewavcsaat shrslspqll qqtpskpdga tkslgsyapg prsrspslnr
      481 lggagedgkr pqpphwhvgs pftpgankds lstfeypgpr rklysavpgr lfvaikpyqp
      541 qvdgeiplhr gdrvkvlsig eggfwegsar ghigwfpaec veevqckprd sqaetradrs
      601 kklfrhytvg sydsfdaasd ciiedktvvl qkkdnegfgf vlrgakadtp ieeftptpaf
      661 palqylesvd eggvawqagl rtgdflievn nenvvkvghr qvvnmirqgg nhlvlkvvtv
      721 trnldpddta rkkappppkr apttaltlrs ksmtaeleel dkpeeivpas kpsrtaenva
      781 iesrvatikq rptsrcfpaa sdvnsvyerq giavmtptvp gspkgpflgl prgtmrrqks
      841 idsriflsgi teeerqflap pmlkftrsls mpdtsedipp ppqsvppspp ppspttyncp
      901 rsptprvygt ikpafnqnpv akvppatrsd tvatmmrekg mfyrreldrf sldsedvysr
      961 spapqaafrt krgqmpenpy sevgkiaska vyvpakparr kgmlvkqsnv edspektcsi
     1021 piptiivkep stsssgkssq gssmeidpqa tepgqlrpdd sltvsspfaa aiagavrdre
     1081 krlearrnsp aflstdlgde dvglgppapr mqpskfpeeg gfgdedeteq pllptpgaap
     1141 relenhflgg geagaqgeag gplsstskak gpesgpaaal kssspaspen yvhpltgrll
     1201 dpssplalal sardramqes qqghkgeapk adlnkplyid tkmrpsvesg fppvtrqntr
     1261 gplrrqeten kyetdlskdr raddkknmli nivdtaqqks agllmvhtvd ipvagpplee
     1321 eedredgdtk pdhspstvpe gvpktegalq isaapepaaa pgrtivaags veeavilpfr
     1381 ipppplasvd ldedflftep lppplefans fdipddraas vpaladlvkq kksdtpqpps
     1441 lnssqpanst dskkpagisn clpssflppp esfdavtdsg ieevdsrsss dhhlettsti
     1501 stvssistls seggesmdtc tvyadgqafv vdkppvppkp kmkpivhksn alyqdtlpee
     1561 dtdgfvippp apppppgsaq agvakviqpr tsklwgdvte vkspilsgpk anviselnsi
     1621 lqqmnrgksv kpgeglelpv gaksanlapr spevmstvsg trsttvtftv rpgtsqpitl
     1681 qsrppdyesr tsgprrapsp vvsptelske ilptppsaaa aspsptlsdv fslpsqspag
     1741 dlfglnpagr srspspsilq qpisnkpftt kpvhlwtkpd vadwleslnl gehketfmdn
     1801 eidgshlpnl qkedlidlgv trvghrmnie ralkqlldr
//
LOCUS       NP_001008326             115 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 218 [Rattus norvegicus].
ACCESSION   NP_001008326 XP_217107
VERSION     NP_001008326.1
DBSOURCE    REFSEQ: accession NM_001008325.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085342.1.
            
            On Dec 16, 2004 this sequence version replaced XP_217107.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085342.1, CO389659.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..115
                     /product="transmembrane protein 218"
                     /calculated_mol_wt=12348
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Y9.1)"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Y9.1)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Y9.1)"
     CDS             1..115
                     /gene="Tmem218"
                     /gene_synonym="RGD1311364"
                     /coded_by="NM_001008325.1:49..396"
                     /db_xref="GeneID:300516"
                     /db_xref="RGD:1311364"
ORIGIN      
        1 magmvlgvga gvfllallwv lvlllcvllc rasgiarfsi ifvflgalii ttvlllfpra
       61 sefpapqgem kivdaffigr yvllaflsav flgglflllt hhvlepiyak plrsc
//
LOCUS       NP_114054                 87 aa            linear   ROD 27-APR-2025
DEFINITION  acyl-CoA-binding protein [Rattus norvegicus].
ACCESSION   NP_114054 XP_001055495
VERSION     NP_114054.1
DBSOURCE    REFSEQ: accession NM_031853.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Bourzam,A., Hamdi,Y., Bahdoudi,S., Duraisamy,K., El Mehdi,M.,
            Basille-Dugay,M., Dlimi,O., Kharrat,M., Vejux,A., Lizard,G.,
            Ghrairi,T., Lefranc,B., Vaudry,D., Boutin,J.A., Leprince,J. and
            Masmoudi-Kouki,O.
  TITLE     Octadecaneuropeptide, ODN, Promotes Cell Survival against
            6-OHDA-Induced Oxidative Stress and Apoptosis by Modulating the
            Expression of miR-34b, miR-29a, and miR-21in Cultured Astrocytes
  JOURNAL   Cells 13 (14), 1188 (2024)
   PUBMED   39056770
  REMARK    GeneRIF: Octadecaneuropeptide, ODN, Promotes Cell Survival against
            6-OHDA-Induced Oxidative Stress and Apoptosis by Modulating the
            Expression of miR-34b, miR-29a, and miR-21in Cultured Astrocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Ghouili,I., Bahdoudi,S., Morin,F., Amri,F., Hamdi,Y., Coly,P.M.,
            Walet-Balieu,M.L., Leprince,J., Zekri,S., Vaudry,H., Vaudry,D.,
            Castel,H., Amri,M., Tonon,M.C. and Masmoudi-Kouki,O.
  TITLE     Endogenous Expression of ODN-Related Peptides in Astrocytes
            Contributes to Cell Protection Against Oxidative Stress:
            Astrocyte-Neuron Crosstalk Relevance for Neuronal Survival
  JOURNAL   Mol Neurobiol 55 (6), 4596-4611 (2018)
   PUBMED   28698967
  REMARK    GeneRIF: astrocytes produce authentic ODN, notably in a moderate
            oxidative stress situation, and this glio- and neuro-protective
            agent may form part of the brain defense mechanisms against
            oxidative stress injury.
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Yoshihara,E., Iwahashi,K., Waga,C., Murayama,O., Ohtani,N.,
            Narita,S., Nagahori,K., Numajiri,M. and Onozawa,Y.
  TITLE     Relationship between alcohol dependence and the DBI rs2276596 (C/A)
            polymorphism in Japanese
  JOURNAL   Nihon Arukoru Yakubutsu Igakkai Zasshi 49 (1), 39-44 (2014)
   PUBMED   24818357
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Lanfray,D., Arthaud,S., Ouellet,J., Compere,V., Do Rego,J.L.,
            Leprince,J., Lefranc,B., Castel,H., Bouchard,C.,
            Monge-Roffarello,B., Richard,D., Pelletier,G., Vaudry,H.,
            Tonon,M.C. and Morin,F.
  TITLE     Gliotransmission and brain glucose sensing: critical role of
            endozepines
  JOURNAL   Diabetes 62 (3), 801-810 (2013)
   PUBMED   23160530
  REMARK    GeneRIF: Data suggest that neuroglia play important role in glucose
            sensing in hypothalamus and may regulate energy balance/appetite
            control through production/secretion of endozepines (diazepam
            binding inhibitor and processing product, octadecaneuropeptide).
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Ludewig,A.H., Nitz,I., Klapper,M. and Doring,F.
  TITLE     Identification of a novel human Acyl-CoA binding protein isoform
            with a unique C-terminal domain
  JOURNAL   IUBMB Life 63 (7), 547-552 (2011)
   PUBMED   21698759
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Mandrup,S., Hummel,R., Ravn,S., Jensen,G., Andreasen,P.H.,
            Gregersen,N., Knudsen,J. and Kristiansen,K.
  TITLE     Acyl-CoA-binding protein/diazepam-binding inhibitor gene and
            pseudogenes. A typical housekeeping gene family
  JOURNAL   J Mol Biol 228 (3), 1011-1022 (1992)
   PUBMED   1469708
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Slobodyansky,E., Guidotti,A., Wambebe,C., Berkovich,A. and Costa,E.
  TITLE     Isolation and characterization of a rat brain
            triakontatetraneuropeptide, a posttranslational product of diazepam
            binding inhibitor: specific action at the Ro 5-4864 recognition
            site
  JOURNAL   J Neurochem 53 (4), 1276-1284 (1989)
   PUBMED   2769267
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Knudsen,J., Hojrup,P., Hansen,H.O., Hansen,H.F. and Roepstorff,P.
  TITLE     Acyl-CoA-binding protein in the rat. Purification, binding
            characteristics, tissue concentrations and amino acid sequence
  JOURNAL   Biochem J 262 (2), 513-519 (1989)
   PUBMED   2803267
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Gray,P.W.
  TITLE     Molecular biology of diazepam binding inhibitor
  JOURNAL   Neuropharmacology 26 (7B), 863-865 (1987)
   PUBMED   2821429
REFERENCE   10 (residues 1 to 87)
  AUTHORS   Ferrero,P., Santi,M.R., Conti-Tronconi,B., Costa,E. and Guidotti,A.
  TITLE     Study of an octadecaneuropeptide derived from diazepam binding
            inhibitor (DBI): biological activity and presence in rat brain
  JOURNAL   Proc Natl Acad Sci U S A 83 (3), 827-831 (1986)
   PUBMED   3456171
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1986 Apr;83(8):2776. doi:
            10.1073/pnas.83.8.2776. PMID: 3458238]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M14201.1 and BC084717.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001055495.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M14201.1, CF977190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132294, SAMD00132297
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q11"
     Protein         1..87
                     /product="acyl-CoA-binding protein"
                     /EC_number="3.4.17.3"
                     /note="GABA receptor modulator; diazepam binding
                     inhibitor-like; octadecaneuropeptide; endozepine;
                     triakontatetraneuropeptide; LRRGT00046; diazepam binding
                     inhibitor (GABA receptor modulator, acyl-CoA binding
                     protein); diazepam binding inhibitor (GABA receptor
                     modulator, acyl-Coenzyme A binding protein); Diazepam
                     binding inhibitor (GABA receptor modulator, acyl-Coenxyme
                     A binding protein); diazepam binding inhibitor, acyl-CoA
                     binding protein"
                     /calculated_mol_wt=9896
     Region          2..86
                     /region_name="ACBP"
                     /note="Acyl CoA binding protein (ACBP) binds thiol esters
                     of long fatty acids and coenzyme A in a one-to-one binding
                     mode with high specificity and affinity. Acyl-CoAs are
                     important intermediates in fatty lipid synthesis and fatty
                     acid degradation and play a...; cd00435"
                     /db_xref="CDD:238248"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:2803267; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07108; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     Site            order(10,13..14,16,19..20,22,25..26,28..29,32..33,50..51,
                     54..55,74)
                     /site_type="other"
                     /note="acyl-CoA binding pocket [chemical binding]"
                     /db_xref="CDD:238248"
     Site            order(14,29,32..33,55,74)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:238248"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P07108; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P31786; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07108; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07108; propagated from
                     UniProtKB/Swiss-Prot (P11030.3)"
     CDS             1..87
                     /gene="Dbi"
                     /gene_synonym="Acbp; Acoabp3; Ep; Odn; RNACOABP3; Ttn"
                     /coded_by="NM_031853.4:118..381"
                     /db_xref="GeneID:25045"
                     /db_xref="RGD:2490"
ORIGIN      
        1 msqadfdkaa eevkrlktqp tdeemlfiys hfkqatvgdv ntdrpglldl kgkakwdswn
       61 klkgtskena mktyvekvee lkkkygi
//
LOCUS       NP_067727                692 aa            linear   ROD 27-APR-2025
DEFINITION  synaptopodin [Rattus norvegicus].
ACCESSION   NP_067727
VERSION     NP_067727.2
DBSOURCE    REFSEQ: accession NM_021695.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Ribeiro,P.C., Lojudice,F.H., Fernandes-Charpiot,I.M.M.,
            Baptista,M.A.S.F., de Almeida Araujo,S., Mendes,G.E.F.,
            Sogayar,M.C., Abbud-Filho,M. and Caldas,H.C.
  TITLE     Therapeutic potential of human induced pluripotent stem cells and
            renal progenitor cells in experimental chronic kidney disease
  JOURNAL   Stem Cell Res Ther 11 (1), 530 (2020)
   PUBMED   33298161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Konietzny,A., Gonzalez-Gallego,J., Bar,J., Perez-Alvarez,A.,
            Drakew,A., Demmers,J.A.A., Dekkers,D.H.W., Hammer,J.A. 3rd,
            Frotscher,M., Oertner,T.G., Wagner,W., Kneussel,M. and
            Mikhaylova,M.
  TITLE     Myosin V regulates synaptopodin clustering and localization in the
            dendrites of hippocampal neurons
  JOURNAL   J Cell Sci 132 (16) (2019)
   PUBMED   31371487
  REMARK    GeneRIF: Myosin V regulates synaptopodin clustering and
            localization in the dendrites of hippocampal neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Ji,C., Tang,M., Zeidler,C., Hohfeld,J. and Johnson,G.V.
  TITLE     BAG3 and SYNPO (synaptopodin) facilitate phospho-MAPT/Tau
            degradation via autophagy in neuronal processes
  JOURNAL   Autophagy 15 (7), 1199-1213 (2019)
   PUBMED   30744518
  REMARK    GeneRIF: The study provides evidence of a novel role for the
            co-chaperone BAG3 in synapses. In cooperation with SYNPO, it
            functions as part of a surveillance complex that facilitates the
            autophagic clearance of MAPT p-Ser262, and possibly other MAPT
            species at the post-synapse.
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Dorval,G., Kuzmuk,V., Gribouval,O., Welsh,G.I., Bierzynska,A.,
            Schmitt,A., Miserey-Lenkei,S., Koziell,A., Haq,S., Benmerah,A.,
            Mollet,G., Boyer,O., Saleem,M.A. and Antignac,C.
  TITLE     TBC1D8B Loss-of-Function Mutations Lead to X-Linked Nephrotic
            Syndrome via Defective Trafficking Pathways
  JOURNAL   Am J Hum Genet 104 (2), 348-355 (2019)
   PUBMED   30661770
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Wang,L., Dumoulin,A., Renner,M., Triller,A. and Specht,C.G.
  TITLE     The Role of Synaptopodin in Membrane Protein Diffusion in the
            Dendritic Spine Neck
  JOURNAL   PLoS One 11 (2), e0148310 (2016)
   PUBMED   26840625
  REMARK    GeneRIF: Using single particle tracking we have identified a
            specific effect of synaptopodin on the diffusion of metabotropic
            mGluR5 receptors in the spine neck.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Asanuma,K., Kim,K., Oh,J., Giardino,L., Chabanis,S., Faul,C.,
            Reiser,J. and Mundel,P.
  TITLE     Synaptopodin regulates the actin-bundling activity of alpha-actinin
            in an isoform-specific manner
  JOURNAL   J Clin Invest 115 (5), 1188-1198 (2005)
   PUBMED   15841212
  REMARK    Erratum:[J Clin Invest. 2012 Feb 1;122(2):781]
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Deller,T., Korte,M., Chabanis,S., Drakew,A., Schwegler,H.,
            Stefani,G.G., Zuniga,A., Schwarz,K., Bonhoeffer,T., Zeller,R.,
            Frotscher,M. and Mundel,P.
  TITLE     Synaptopodin-deficient mice lack a spine apparatus and show
            deficits in synaptic plasticity
  JOURNAL   Proc Natl Acad Sci U S A 100 (18), 10494-10499 (2003)
   PUBMED   12928494
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Yamazaki,M., Matsuo,R., Fukazawa,Y., Ozawa,F. and Inokuchi,K.
  TITLE     Regulated expression of an actin-associated protein, synaptopodin,
            during long-term potentiation
  JOURNAL   J Neurochem 79 (1), 192-199 (2001)
   PUBMED   11595771
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Deller,T., Merten,T., Roth,S.U., Mundel,P. and Frotscher,M.
  TITLE     Actin-associated protein synaptopodin in the rat hippocampal
            formation: localization in the spine neck and close association
            with the spine apparatus of principal neurons
  JOURNAL   J Comp Neurol 418 (2), 164-181 (2000)
   PUBMED   10701442
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Mundel,P., Heid,H.W., Mundel,T.M., Kruger,M., Reiser,J. and Kriz,W.
  TITLE     Synaptopodin: an actin-associated protein in telencephalic
            dendrites and renal podocytes
  JOURNAL   J Cell Biol 139 (1), 193-204 (1997)
   PUBMED   9314539
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB769636.1, CB794090.1, AB013130.1, DY313339.1 and EV779156.1.
            
            On Oct 16, 2007 this sequence version replaced NP_067727.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06621351,
                              SAMN12840113 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..692
                     /product="synaptopodin"
                     /calculated_mol_wt=74206
     Region          <15..>125
                     /region_name="PRK13914"
                     /note="invasion associated endopeptidase"
                     /db_xref="CDD:237555"
     Region          <50..361
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <496..689
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..692
                     /gene="Synpo"
                     /coded_by="NM_021695.2:531..2609"
                     /db_xref="GeneID:60324"
                     /db_xref="RGD:620668"
ORIGIN      
        1 megyseeasl lrhlekvase eeevplvvyl kenaalltan glhlsqnret qqsspnppet
       61 eevpspaadi nqnpsspnat lttaasnshh nqptadvnqn ppatitpvqq nssetqcspn
      121 gtldskpntp saddgqrpvp aeevrssill idkvsappsa aspfsreatp lsssgppaad
      181 lmssslligm qpstlvasae qevsghaavt tptkvysevh ltlakpasvv nrtarpfgmq
      241 spgttsqieq spmmgrrhfg ekawappass madrspqpqr himarspmve rrlvgqrspv
      301 verrplgnft ppptyaetls tapvasqvrs ppsystlyps sdpkpphlkg qvvpanktgi
      361 leesmarrgs rksmftfvek pkvtpnpdll dlvqtadekr rqrdqgevgm edepfalgae
      421 asnfqqepia rdrsgpaaae etvpewascl kspriqakpk pkpnqnlsea sgkgaelyar
      481 rqsrmekyvi essghaelar cpsptmslps swkyttnapg gfrvaslspa rtppaslyhg
      541 ylpengvlrp eptkqqphqm rpslyalspv kepakissra tssrassrtv spraaspakp
      601 ssldlvpnlp raglppspal prpsrsspgl ynapvqdslq ptavsptyss dispvspsra
      661 wsprakqapr psfstrnagi eaqvwkpsfc fk
//
LOCUS       NP_001017489             570 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2D [Rattus norvegicus].
ACCESSION   NP_001017489 XP_573446
VERSION     NP_001017489.1
DBSOURCE    REFSEQ: accession NM_001017489.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Dmitriev,S.E., Terenin,I.M., Andreev,D.E., Ivanov,P.A.,
            Dunaevsky,J.E., Merrick,W.C. and Shatsky,I.N.
  TITLE     GTP-independent tRNA delivery to the ribosomal P-site by a novel
            eukaryotic translation factor
  JOURNAL   J Biol Chem 285 (35), 26779-26787 (2010)
   PUBMED   20566627
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Skabkin,M.A., Skabkina,O.V., Dhote,V., Komar,A.A., Hellen,C.U. and
            Pestova,T.V.
  TITLE     Activities of Ligatin and MCT-1/DENR in eukaryotic translation
            initiation and ribosomal recycling
  JOURNAL   Genes Dev 24 (16), 1787-1801 (2010)
   PUBMED   20713520
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087701.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573446.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087701.1, SRR8487231.127654.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..570
                     /product="eukaryotic translation initiation factor 2D"
                     /note="ligatin"
                     /calculated_mol_wt=62538
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P41214; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Region          6..81
                     /region_name="eIF2D_N"
                     /note="N-terminal domain of eIF2D and related proteins;
                     cd11610"
                     /db_xref="CDD:211423"
     Site            order(29..30,73,75,78..81)
                     /site_type="other"
                     /note="PUA domain interface [polypeptide binding]"
                     /db_xref="CDD:211423"
     Region          92..173
                     /region_name="PUA_eIF2d-like"
                     /note="PUA RNA-binding domain of eukaryotic translation
                     initiation factor 2D and similar proteins; cd21156"
                     /db_xref="CDD:409298"
     Site            order(101..102,105,110..111,113)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409298"
     Region          178..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Region          215..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61211; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61211; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41214; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG7.1)"
     Region          477..561
                     /region_name="eIF2D_C"
                     /note="C-terminal domain of eIF2D and related proteins;
                     cd11608"
                     /db_xref="CDD:211321"
     Site            order(485,488..489,491,509,512..514,516..518,520,536,539)
                     /site_type="other"
                     /note="putative rRNA binding site [nucleotide binding]"
                     /db_xref="CDD:211321"
     CDS             1..570
                     /gene="Eif2d"
                     /gene_synonym="Lgtn"
                     /coded_by="NM_001017489.1:199..1911"
                     /db_xref="GeneID:498225"
                     /db_xref="RGD:1561765"
ORIGIN      
        1 mfakafrvks ntaikgsdrr klradvtvaf ptlgtdqvse lipgkeelnv vklyahkgda
       61 vtvytsggnp ilfeleknly ptvytlwshp dllpafitwp lvleklvgga dlmlpgvvvp
      121 ptglpqvqqg dlcaialvgn rapvavgvaa mstaqmlasg lkgkgisvlh tyqdhlwrsg
      181 dkssppaiap ldptdsceek adlglhgnlr slslegeeen gqvpnpeasd dpnsralsqd
      241 svdgkplqeq mdelleqcfl halksrvkka dlplltstll gshmfsccpe gqqldikkss
      301 ykklskflqh mqqeqivqvk elskgvesiv avdwrhprit sfivpepsla sqtvqegsre
      361 kpylppdiks lycvpanmtq lflesghkkg stlegsevrr iitdyakrnn lvdadnrnlv
      421 kldpilcdci lekneqhlvm klpwdslltr clknlqpayq vtfpgqepii kkgklcpidi
      481 tlvlktynkk vtvvrnlety gldpcsvaai lqqrcqasti vspapgakds lqvqvqgnqi
      541 hhlgqlllee yrlpgkyiqg lekapkpgkk
//
LOCUS       NP_598287                123 aa            linear   ROD 27-APR-2025
DEFINITION  potassium voltage-gated channel subfamily E member 2 [Rattus
            norvegicus].
ACCESSION   NP_598287
VERSION     NP_598287.1
DBSOURCE    REFSEQ: accession NM_133603.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Liu,W.J., Deng,J.X., Wang,G., Gao,K.P., Lin,Z.X., Liu,S.Y.,
            Wang,Y.H. and Liu,J.
  TITLE     Manipulation of KCNE2 expression modulates action potential
            duration and Ito and IK in rat and mouse ventricular myocytes
  JOURNAL   Am J Physiol Heart Circ Physiol 309 (8), H1288-H1302 (2015)
   PUBMED   26297229
  REMARK    GeneRIF: Endogenous KCNE2 in cardiomyocytes is important in
            maintaining cardiac electrical stability mainly by regulating Ito
            and action potential duration.
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Liu,W., Deng,J., Wang,G., Zhang,C., Luo,X., Yan,D., Su,Q. and
            Liu,J.
  TITLE     KCNE2 modulates cardiac L-type Ca(2+) channel
  JOURNAL   J Mol Cell Cardiol 72, 208-218 (2014)
   PUBMED   24681347
  REMARK    GeneRIF: The KCNE2 mutation R27C may induce familial atrial
            fibrillation partially through enhancing the suppression of Cav1.2
            calcium channel.
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Sachse,C.C., Kim,Y.H., Agsten,M., Huth,T., Alzheimer,C.,
            Kovacs,D.M. and Kim,D.Y.
  TITLE     BACE1 and presenilin/gamma-secretase regulate proteolytic
            processing of KCNE1 and 2, auxiliary subunits of voltage-gated
            potassium channels
  JOURNAL   FASEB J 27 (6), 2458-2467 (2013)
   PUBMED   23504710
  REMARK    GeneRIF: KCNE1 and KCNE2, auxiliary subunits of voltage-gated
            potassium channels, undergo sequential cleavage mediated by either
            alpha-secretase and presenilin(PS)/gamma-secretase or BACE1 and
            PS/gamma-secretase in cells.
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Zhang,M., Wang,Y., Jiang,M., Zankov,D.P., Chowdhury,S.,
            Kasirajan,V. and Tseng,G.N.
  TITLE     KCNE2 protein is more abundant in ventricles than in atria and can
            accelerate hERG protein degradation in a phosphorylation-dependent
            manner
  JOURNAL   Am J Physiol Heart Circ Physiol 302 (4), H910-H922 (2012)
   PUBMED   22180649
  REMARK    GeneRIF: KCNE2 can modulate its partner channel function not only
            by altering channel conductance and/or gating kinetics, but also by
            affecting protein stability.
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Kanda,V.A., Lewis,A., Xu,X. and Abbott,G.W.
  TITLE     KCNE1 and KCNE2 provide a checkpoint governing voltage-gated
            potassium channel alpha-subunit composition
  JOURNAL   Biophys J 101 (6), 1364-1375 (2011)
   PUBMED   21943417
  REMARK    GeneRIF: KCNE1 and KCNE2 suppress currents generated by homomeric
            Kv1.4, Kv3.3, and Kv3.4 channels
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Jiang,M., Zhang,M., Tang,D.G., Clemo,H.F., Liu,J., Holwitt,D.,
            Kasirajan,V., Pond,A.L., Wettwer,E. and Tseng,G.N.
  TITLE     KCNE2 protein is expressed in ventricles of different species, and
            changes in its expression contribute to electrical remodeling in
            diseased hearts
  JOURNAL   Circulation 109 (14), 1783-1788 (2004)
   PUBMED   15066947
  REMARK    GeneRIF: In aging rat ventricle, KCNE2 may associate with HCN2 and
            enhance its current amplitude. KCNE2 protein is expressed in
            ventricles, and it can play diverse roles in ventricular electrical
            activity under (patho)physiological conditions.
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Lewis,A., McCrossan,Z.A. and Abbott,G.W.
  TITLE     MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
            gating
  JOURNAL   J Biol Chem 279 (9), 7884-7892 (2004)
   PUBMED   14679187
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Ohya,S., Asakura,K., Muraki,K., Watanabe,M. and Imaizumi,Y.
  TITLE     Molecular and functional characterization of ERG, KCNQ, and KCNE
            subtypes in rat stomach smooth muscle
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 282 (2), G277-G287 (2002)
   PUBMED   11804849
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Yu,H., Wu,J., Potapova,I., Wymore,R.T., Holmes,B., Zuckerman,J.,
            Pan,Z., Wang,H., Shi,W., Robinson,R.B., El-Maghrabi,M.R.,
            Benjamin,W., Dixon,J., McKinnon,D., Cohen,I.S. and Wymore,R.
  TITLE     MinK-related peptide 1: A beta subunit for the HCN ion channel
            subunit family enhances expression and speeds activation
  JOURNAL   Circ Res 88 (12), E84-E87 (2001)
   PUBMED   11420311
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Abbott,G.W., Sesti,F., Splawski,I., Buck,M.E., Lehmann,M.H.,
            Timothy,K.W., Keating,M.T. and Goldstein,S.A.
  TITLE     MiRP1 forms IKr potassium channels with HERG and is associated with
            cardiac arrhythmia
  JOURNAL   Cell 97 (2), 175-187 (1999)
   PUBMED   10219239
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089778.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089778.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132278, SAMD00132302
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..123
                     /product="potassium voltage-gated channel subfamily E
                     member 2"
                     /note="potassium channel, voltage-gated Isk-related
                     subfamily E regulatory beta subunit 2; potassium channel
                     subunit beta MiRP1; potassium channel, voltage gated
                     subfamily E regulatory beta subunit 2; minimum potassium
                     ion channel-related peptide 1; potassium voltage-gated
                     channel, Isk-related subfamily, gene 2; minK-related
                     peptide 1; potassium voltage-gated channel, Isk-related
                     family, member 2"
                     /calculated_mol_wt=14225
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63161.1)"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63161.1)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P63161.1)"
     Region          <50..108
                     /region_name="ISK_Channel"
                     /note="Slow voltage-gated potassium channel; pfam02060"
                     /db_xref="CDD:460432"
     CDS             1..123
                     /gene="Kcne2"
                     /gene_synonym="Mirp1"
                     /coded_by="NM_133603.2:194..565"
                     /db_xref="GeneID:171138"
                     /db_xref="RGD:621383"
ORIGIN      
        1 mttlanltqt ledafkkvfi tymdswrrnt taeqqalqar vdaenfyyvi lylmvmigmf
       61 afivvailvs tvkskrrehs qdpyhqyive dwqqkyrsqi lhledskati henlgatgft
      121 vsp
//
LOCUS       NP_001101905             394 aa            linear   ROD 27-APR-2025
DEFINITION  metallophosphoesterase 1 [Rattus norvegicus].
ACCESSION   NP_001101905 XP_001066434 XP_341628
VERSION     NP_001101905.1
DBSOURCE    REFSEQ: accession NM_001108435.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Hirata,T., Mishra,S.K., Nakamura,S., Saito,K., Motooka,D.,
            Takada,Y., Kanzawa,N., Murakami,Y., Maeda,Y., Fujita,M.,
            Yamaguchi,Y. and Kinoshita,T.
  TITLE     Identification of a Golgi GPI-N-acetylgalactosamine transferase
            with tandem transmembrane regions in the catalytic domain
  JOURNAL   Nat Commun 9 (1), 405 (2018)
   PUBMED   29374258
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC162043.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001066434.1, XP_341628.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC162043.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..394
                     /product="metallophosphoesterase 1"
                     /EC_number="3.1.-.-"
                     /note="post-GPI attachment to proteins factor 5"
                     /calculated_mol_wt=45523
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC86.1)"
     Region          70..327
                     /region_name="MPP_MPPE1"
                     /note="human MPPE1 and related proteins,
                     metallophosphatase domain; cd08165"
                     /db_xref="CDD:277372"
     Site            order(74,76,116,154..155,247,301,303)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277372"
     Site            order(74,76,116,154,247,301,303)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277372"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC86.1)"
     CDS             1..394
                     /gene="Mppe1"
                     /coded_by="NM_001108435.2:454..1638"
                     /db_xref="GeneID:361344"
                     /db_xref="RGD:1309184"
ORIGIN      
        1 malvrwglrr qnfhllrrrr vlllkltvvv isvllfceyf iyylvlfrch wpevkmparg
       61 grqepvlkam fladthllge irghwldklr rewqmerafq talwllqpev vfilgdvfde
      121 gkwssaqawa ddlhrfqrmf rhgshvqlkv vignhdigfh yqmskyrinr fekvfgserl
      181 fslkgvnfvm vnsvamegdg cticseaeae lreisrklnc sqeqvqgssq cdheprlpls
      241 apvllqhypl yrasdancsg edaappeers vpfeekydvl sreasqkllw wlrprlilsg
      301 hthsacevlh pggapevsvp sfswrnrnnp sfimgsltsr dyalskcylp cedtvlttyc
      361 aaaafllvli lahferlpss flfgwklcrs hlrr
//
LOCUS       NP_001093990             530 aa            linear   ROD 27-APR-2025
DEFINITION  chaperone Ric-8A [Rattus norvegicus].
ACCESSION   NP_001093990 XP_001058411 XP_215118
VERSION     NP_001093990.1
DBSOURCE    REFSEQ: accession NM_001100520.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Seven,A.B., Hilger,D., Papasergi-Scott,M.M., Zhang,L., Qu,Q.,
            Kobilka,B.K., Tall,G.G. and Skiniotis,G.
  TITLE     Structures of Galpha Proteins in Complex with Their Chaperone
            Reveal Quality Control Mechanisms
  JOURNAL   Cell Rep 30 (11), 3699-3709 (2020)
   PUBMED   32126208
REFERENCE   2  (residues 1 to 530)
  AUTHORS   McClelland,L.J., Zhang,K., Mou,T.C., Johnston,J., Yates-Hansen,C.,
            Li,S., Thomas,C.J., Doukov,T.I., Triest,S., Wohlkonig,A.,
            Tall,G.G., Steyaert,J., Chiu,W. and Sprang,S.R.
  TITLE     Structure of the G protein chaperone and guanine nucleotide
            exchange factor Ric-8A bound to Galphai1
  JOURNAL   Nat Commun 11 (1), 1077 (2020)
   PUBMED   32103024
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Zeng,B., Mou,T.C., Doukov,T.I., Steiner,A., Yu,W.,
            Papasergi-Scott,M., Tall,G.G., Hagn,F. and Sprang,S.R.
  TITLE     Structure, Function, and Dynamics of the Galpha Binding Domain of
            Ric-8A
  JOURNAL   Structure 27 (7), 1137-1147 (2019)
   PUBMED   31155309
  REMARK    GeneRIF: Structure, function, and dynamics of the Galpha binding
            domain of Ric-8A have been reported.
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Kant,R., Zeng,B., Thomas,C.J., Bothner,B. and Sprang,S.R.
  TITLE     Ric-8A, a G protein chaperone with nucleotide exchange activity
            induces long-range secondary structure changes in Galpha
  JOURNAL   Elife 5, e19238 (2016)
   PUBMED   28008853
  REMARK    GeneRIF: In contrast to G protein-coupled receptors, Ric-8A
            interacts with Switches I and II of Galpha and possibly at the
            Galpha domain interface.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Black,L.A., Thomas,C.J., Nix,G.N., Terwilliger,M.C., Sprang,S.R.
            and Ross,J.B.A.
  TITLE     Nanosecond Dynamics of Galphai1 Bound to Nucleotides or Ric-8A, a
            Galpha Chaperone with GEF Activity
  JOURNAL   Biophys J 111 (4), 722-731 (2016)
   PUBMED   27558716
  REMARK    GeneRIF: Induction of Galphai1 structural heterogeneity by Ric-8A
            provides a mechanism for nucleotide release
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Thomas,C.J., Tall,G.G., Adhikari,A. and Sprang,S.R.
  TITLE     Ric-8A catalyzes guanine nucleotide exchange on G alphai1 bound to
            the GPR/GoLoco exchange inhibitor AGS3
  JOURNAL   J Biol Chem 283 (34), 23150-23160 (2008)
   PUBMED   18541531
  REMARK    GeneRIF: Ric-8A has a role in catalyzing guanine nucleotide
            exchange on G alphai1 bound to the GPR/GoLoco exchange inhibitor
            AGS3
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Wang,S.C., Lai,H.L., Chiu,Y.T., Ou,R., Huang,C.L. and Chern,Y.
  TITLE     Regulation of type V adenylate cyclase by Ric8a, a guanine
            nucleotide exchange factor
  JOURNAL   Biochem J 406 (3), 383-388 (2007)
   PUBMED   17593019
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Tonissoo,T., Koks,S., Meier,R., Raud,S., Plaas,M., Vasar,E. and
            Karis,A.
  TITLE     Heterozygous mice with Ric-8 mutation exhibit impaired spatial
            memory and decreased anxiety
  JOURNAL   Behav Brain Res 167 (1), 42-48 (2006)
   PUBMED   16221497
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Tall,G.G. and Gilman,A.G.
  TITLE     Resistance to inhibitors of cholinesterase 8A catalyzes release of
            Galphai-GTP and nuclear mitotic apparatus protein (NuMA) from
            NuMA/LGN/Galphai-GDP complexes
  JOURNAL   Proc Natl Acad Sci U S A 102 (46), 16584-16589 (2005)
   PUBMED   16275912
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Tall,G.G., Krumins,A.M. and Gilman,A.G.
  TITLE     Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein
            guanine nucleotide exchange factor
  JOURNAL   J Biol Chem 278 (10), 8356-8362 (2003)
   PUBMED   12509430
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC160852.1.
            
            On or before Sep 7, 2008 this sequence version replaced
            XP_001058411.1, XP_215118.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160852.1, AY177754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..530
                     /product="chaperone Ric-8A"
                     /note="synembryn-A; resistance to inhibitors of
                     cholinesterase 8A; heterotrimeric G protein guanine
                     nucleotide exchange factor Ric-8A; resistance to
                     inhibitors of cholinesterase 8A-like protein; resistance
                     to inhibitors of cholinesterase 8 homolog"
                     /calculated_mol_wt=59696
     Region          67..491
                     /region_name="Ric8"
                     /note="Guanine nucleotide exchange factor synembryn;
                     pfam10165"
                     /db_xref="CDD:462973"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29844055,
                     ECO:0000269|PubMed:32103024, ECO:0000269|PubMed:32126208;
                     propagated from UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK2.
                     /evidence=ECO:0000269|PubMed:29844055,
                     ECO:0000269|PubMed:32103024, ECO:0000269|PubMed:32126208;
                     propagated from UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TIR3; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPQ8; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32126208; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29844055,
                     ECO:0000269|PubMed:32126208; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG1.3)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29844055,
                     ECO:0000269|PubMed:32126208; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG1.3)"
     CDS             1..530
                     /gene="Ric8a"
                     /gene_synonym="Ric-8A; Ric8"
                     /coded_by="NM_001100520.1:232..1824"
                     /db_xref="GeneID:293614"
                     /db_xref="RGD:727957"
ORIGIN      
        1 mepravadal etgeedavte alrsfnrehs qsftfddaqq edrkrlakll vsvleqglsp
       61 khrvtwlqti rilsrdrscl dsfasrqslh alacyadiai seepipqppd mdvlleslkc
      121 lcnlvlsspt aqmlaaearl vvrlaervgl yrkrsyphev qffdlrllfl ltalrtdvrq
      181 qlfqelhgvr lltdaleltl gvapkenplv ilpaqetera meilkvlfni tydsvkrevd
      241 eedaalyryl gtllrhcvma daagdrteef hghtvnllgn lplkcldvll alelhegsle
      301 fmgvnmdvin allaflekrl hqthrlkecv apvlsvltec armhrparkf lkaqvlpplr
      361 dvrtrpevgd llrnklvrlm thldtdvkrv aaeflfvlcs esvprfikyt gygnaaglla
      421 arglmaggrp egqysededt dteeyreaka sinpvtgrve ekppnpmegm teeqkeheam
      481 klvnmfdkls rhrliqpmgm sprghltslq damcetmegq lssdpdsdpd
//
LOCUS       NP_001009665             213 aa            linear   ROD 27-APR-2025
DEFINITION  receptor-binding cancer antigen expressed on SiSo cells [Rattus
            norvegicus].
ACCESSION   NP_001009665 XP_216915
VERSION     NP_001009665.1
DBSOURCE    REFSEQ: accession NM_001009665.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Wicherek,L., Basta,P., Sikora,J., Galazka,K., Rytlewski,K.,
            Grabiec,M., Lazar,A. and Kalinka,J.
  TITLE     RCAS1 decidual immunoreactivity in severe pre-eclampsia: immune
            cell presence and activity
  JOURNAL   Am J Reprod Immunol 58 (4), 358-366 (2007)
   PUBMED   17845206
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Popiela,T.J., Rudnicka-Sosin,L., Dutsch-Wicherek,M., Klimek,M.,
            Basta,P., Galazka,K. and Wicherek,L.
  TITLE     The metallothionein and RCAS1 expression analysis in breast cancer
            and adjacent tissue regarding the immune cells presence and their
            activity
  JOURNAL   Neuro Endocrinol Lett 27 (6), 786-794 (2006)
   PUBMED   17187007
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Sonoda,K., Miyamoto,S., Hirakawa,T., Yagi,H., Yotsumoto,F.,
            Nakashima,M., Watanabe,T. and Nakano,H.
  TITLE     Clinical significance of RCAS1 as a biomarker of uterine cancer
  JOURNAL   Gynecol Oncol 103 (3), 924-931 (2006)
   PUBMED   16842844
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Wicherek,L., Popiela,T.J., Galazka,K., Dutsch-Wicherek,M.,
            Oplawski,M., Basta,A. and Klimek,M.
  TITLE     Metallothionein and RCAS1 expression in comparison to immunological
            cells activity in endometriosis, endometrial adenocarcinoma and
            endometrium according to menstrual cycle changes
  JOURNAL   Gynecol Oncol 99 (3), 622-630 (2005)
   PUBMED   16112719
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Akahira,J.I., Aoki,M., Suzuki,T., Moriya,T., Niikura,H., Ito,K.,
            Inoue,S., Okamura,K., Sasano,H. and Yaegashi,N.
  TITLE     Expression of EBAG9/RCAS1 is associated with advanced disease in
            human epithelial ovarian cancer
  JOURNAL   Br J Cancer 90 (11), 2197-2202 (2004)
   PUBMED   15164121
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Takahashi,S., Urano,T., Tsuchiya,F., Fujimura,T., Kitamura,T.,
            Ouchi,Y., Muramatsu,M. and Inoue,S.
  TITLE     EBAG9/RCAS1 expression and its prognostic significance in prostatic
            cancer
  JOURNAL   Int J Cancer 106 (3), 310-315 (2003)
   PUBMED   12845666
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Tsuneizumi,M., Nagai,H., Harada,H., Kazui,T. and Emi,M.
  TITLE     A highly polymorphic CA repeat marker at the EBAG9/RCAS1 locus on
            8q23 that detected frequent multiplication in breast cancer
  JOURNAL   Ann Hum Biol 29 (4), 457-460 (2002)
   PUBMED   12160478
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Rousseau,J., Tetu,B., Caron,D., Malenfant,P., Cattaruzzi,P.,
            Audette,M., Doillon,C., Tremblay,J.P. and Guerette,B.
  TITLE     RCAS1 is associated with ductal breast cancer progression
  JOURNAL   Biochem Biophys Res Commun 293 (5), 1544-1549 (2002)
   PUBMED   12054692
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Suzuki,T., Inoue,S., Kawabata,W., Akahira,J., Moriya,T.,
            Tsuchiya,F., Ogawa,S., Muramatsu,M. and Sasano,H.
  TITLE     EBAG9/RCAS1 in human breast carcinoma: a possible factor in
            endocrine-immune interactions
  JOURNAL   Br J Cancer 85 (11), 1731-1737 (2001)
   PUBMED   11742495
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087093.1.
            
            On Jan 13, 2005 this sequence version replaced XP_216915.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087093.1, SRR8487231.85055.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..213
                     /product="receptor-binding cancer antigen expressed on
                     SiSo cells"
                     /note="estrogen receptor-binding fragment-associated gene
                     9 protein"
                     /calculated_mol_wt=24056
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP2.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP2.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O00559; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O00559; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP2.1)"
     Region          <160..203
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     Region          179..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP2.1)"
     CDS             1..213
                     /gene="Ebag9"
                     /coded_by="NM_001009665.1:211..852"
                     /db_xref="GeneID:299864"
                     /db_xref="RGD:1307293"
ORIGIN      
        1 maitqfrlfk vctclatvls flkrlicrsg rgrklsgdqi tlpttvdyss vpkqtdveew
       61 tswdedapts vkieggtgna aaqqnsleql epdyfkdmtp tirktqkivi kkreplsfgv
      121 pdgstgfssr laatqdmpfi hqsselgdld twqensnawe eeedaawqae evlrqqkiad
      181 rekraaeqqr kkmekeaqrl lkkeqnkmgv kls
//
LOCUS       NP_036738                200 aa            linear   ROD 27-APR-2025
DEFINITION  myosin light chain 3 [Rattus norvegicus].
ACCESSION   NP_036738
VERSION     NP_036738.1
DBSOURCE    REFSEQ: accession NM_012606.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Dogra,A., Kour,D., Gour,A., Bhardwaj,M., Bag,S., Dhiman,S.K.,
            Kumar,A., Singh,G. and Nandi,U.
  TITLE     Ameliorating effect of rutin against diclofenac-induced cardiac
            injury in rats with underlying function of FABP3, MYL3, and ANP
  JOURNAL   Drug Chem Toxicol 46 (3), 597-608 (2023)
   PUBMED   35509154
  REMARK    GeneRIF: Ameliorating effect of rutin against diclofenac-induced
            cardiac injury in rats with underlying function of FABP3, MYL3, and
            ANP.
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Zhong,S. and Thompson,L.V.
  TITLE     The roles of myosin ATPase activity and myosin light chain relative
            content in the slowing of type IIB fibers with hindlimb unweighting
            in rats
  JOURNAL   Am J Physiol Cell Physiol 293 (2), C723-C728 (2007)
   PUBMED   17494635
  REMARK    GeneRIF: Slowing of shortening velocity in type IIb fibers with
            hindlimb unloading involves a decrease in the relative amount of
            Myl3.
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Morita,H., Larson,M.G., Barr,S.C., Vasan,R.S., O'Donnell,C.J.,
            Hirschhorn,J.N., Levy,D., Corey,D., Seidman,C.E., Seidman,J.G. and
            Benjamin,E.J.
  TITLE     Single-gene mutations and increased left ventricular wall thickness
            in the community: the Framingham Heart Study
  JOURNAL   Circulation 113 (23), 2697-2705 (2006)
   PUBMED   16754800
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Haase,H., Dobbernack,G., Tunnemann,G., Karczewski,P., Cardoso,C.,
            Petzhold,D., Schlegel,W.P., Lutter,S., Pierschalek,P., Behlke,J.
            and Morano,I.
  TITLE     Minigenes encoding N-terminal domains of human cardiac myosin light
            chain-1 improve heart function of transgenic rats
  JOURNAL   FASEB J 20 (7), 865-873 (2006)
   PUBMED   16675844
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Yamashita,H., Sugiura,S., Fujita,H., Yasuda,Si., Nagai,R.,
            Saeki,Y., Sunagawa,K. and Sugi,H.
  TITLE     Myosin light chain isoforms modify force-generating ability of
            cardiac myosin by changing the kinetics of actin-myosin interaction
  JOURNAL   Cardiovasc Res 60 (3), 580-588 (2003)
   PUBMED   14659803
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Harada,A., Furuta,B., Takeuchi,K., Itakura,M., Takahashi,M. and
            Umeda,M.
  TITLE     Nadrin, a novel neuron-specific GTPase-activating protein involved
            in regulated exocytosis
  JOURNAL   J Biol Chem 275 (47), 36885-36891 (2000)
   PUBMED   10967100
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Poetter,K., Jiang,H., Hassanzadeh,S., Master,S.R., Chang,A.,
            Dalakas,M.C., Rayment,I., Sellers,J.R., Fananapazir,L. and
            Epstein,N.D.
  TITLE     Mutations in either the essential or regulatory light chains of
            myosin are associated with a rare myopathy in human heart and
            skeletal muscle
  JOURNAL   Nat Genet 13 (1), 63-69 (1996)
   PUBMED   8673105
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Brand,T., Milting,H., Zippel,M. and Jockusch,H.
  TITLE     Differential synthesis by cultured atrial and ventricular rat
            cardiac myocytes of myosin light chain isoforms
  JOURNAL   FEBS Lett 283 (2), 289-290 (1991)
   PUBMED   2044768
  REMARK    Erratum:[FEBS Lett 1991 Sep 2;289(1):127]
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Periasamy,M., Wadgaonkar,R., Kumar,C., Martin,B.J. and
            Siddiqui,M.A.
  TITLE     Characterization of a rat myosin alkali light chain gene expressed
            in ventricular and slow twitch skeletal muscles
  JOURNAL   Nucleic Acids Res 17 (19), 7723-7734 (1989)
   PUBMED   2798124
REFERENCE   10 (residues 1 to 200)
  AUTHORS   McNally,E.M., Buttrick,P.M. and Leinwand,L.A.
  TITLE     Ventricular myosin light chain 1 is developmentally regulated and
            does not change in hypertension
  JOURNAL   Nucleic Acids Res 17 (7), 2753-2767 (1989)
   PUBMED   2717409
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081832.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081832.1, FQ216255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132287, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..200
                     /product="myosin light chain 3"
                     /note="MLC1SB; ventricular/slow twitch myosin alkali light
                     chain; Myosin light chain 3, alkali, cardiac ventricles;
                     ventricular, skeletal, slow; myosin, light polypeptide 3;
                     ventricular myosin light chain 1; myosin alkali light
                     chain 1, ventricular; myosin, light chain 3, alkali;
                     ventricular, skeletal, slow"
                     /calculated_mol_wt=22025
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16409.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine.
                     /evidence=ECO:0000250|UniProtKB:P09542; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     Region          49..199
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P09542; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P16409.2)"
     CDS             1..200
                     /gene="Myl3"
                     /gene_synonym="MLClV; Mylc1v; rVMLC1"
                     /coded_by="NM_012606.2:53..655"
                     /db_xref="GeneID:24585"
                     /db_xref="RGD:3142"
ORIGIN      
        1 mapkkpepkk ddaktaapka apapaaapaa apeperpkea efdaskikie ftpeqieefk
       61 eafqlfdrtp kgemkitygq cgdvlralgq nptqaevlrv lgkpkqeeln skmmdfetfl
      121 pmlqhisknk dtgtyedfve glrvfdkegn gtvmgaelrh vlatlgerlt edeveklmag
      181 qedsngciny eafvkhimas
//
LOCUS       NP_001094012             472 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 3, X-linked
            [Rattus norvegicus].
ACCESSION   NP_001094012 XP_001056580 XP_001056649 XP_216704
VERSION     NP_001094012.1
DBSOURCE    REFSEQ: accession NM_001100542.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Young-Baird,S.K., Lourenco,M.B., Elder,M.K., Klann,E., Liebau,S.
            and Dever,T.E.
  TITLE     Suppression of MEHMO Syndrome Mutation in eIF2 by Small Molecule
            ISRIB
  JOURNAL   Mol Cell 77 (4), 875-886 (2020)
   PUBMED   31836389
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Borck,G., Shin,B.S., Stiller,B., Mimouni-Bloch,A., Thiele,H.,
            Kim,J.R., Thakur,M., Skinner,C., Aschenbach,L., Smirin-Yosef,P.,
            Har-Zahav,A., Nurnberg,G., Altmuller,J., Frommolt,P., Hofmann,K.,
            Konen,O., Nurnberg,P., Munnich,A., Schwartz,C.E., Gothelf,D.,
            Colleaux,L., Dever,T.E., Kubisch,C. and Basel-Vanagaite,L.
  TITLE     eIF2gamma mutation that disrupts eIF2 complex integrity links
            intellectual disability to impaired translation initiation
  JOURNAL   Mol Cell 48 (4), 641-646 (2012)
   PUBMED   23063529
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Mikami,S., Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     An efficient mammalian cell-free translation system supplemented
            with translation factors
  JOURNAL   Protein Expr Purif 46 (2), 348-357 (2006)
   PUBMED   16289705
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Bohnsack,M.T., Regener,K., Schwappach,B., Saffrich,R.,
            Paraskeva,E., Hartmann,E. and Gorlich,D.
  TITLE     Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
            transport pathways to confine translation to the cytoplasm
  JOURNAL   EMBO J 21 (22), 6205-6215 (2002)
   PUBMED   12426392
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Kruger,M., Beger,C., Li,Q.X., Welch,P.J., Tritz,R., Leavitt,M.,
            Barber,J.R. and Wong-Staal,F.
  TITLE     Identification of eIF2Bgamma and eIF2gamma as cofactors of
            hepatitis C virus internal ribosome entry site-mediated translation
            using a functional genomics approach
  JOURNAL   Proc Natl Acad Sci U S A 97 (15), 8566-8571 (2000)
   PUBMED   10900014
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Gil,C., Plana,M., Riera,M. and Itarte,E.
  TITLE     Rat liver pp49, a protein that forms complexes with protein kinase
            CK2, is composed of the beta and the gamma subunits of translation
            initiation factor eIF-2
  JOURNAL   Biochem Biophys Res Commun 225 (3), 1052-1057 (1996)
   PUBMED   8780732
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Bommer,U.A., Lutsch,G., Behlke,J., Stahl,J., Nesytova,N., Henske,A.
            and Bielka,H.
  TITLE     Shape and location of eukaryotic initiation factor eIF-2 on the 40S
            ribosomal subunit of rat liver. Immunoelectron-microscopic and
            hydrodynamic investigations
  JOURNAL   Eur J Biochem 172 (3), 653-662 (1988)
   PUBMED   2450747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI029347.1, BC166783.1, BC091286.1, EV772689.1 and BM392036.1.
            
            On or before Jun 1, 2008 this sequence version replaced
            XP_216704.2, XP_001056649.1, XP_001056580.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166783.1, SRR8487230.106833.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..472
                     /product="eukaryotic translation initiation factor 2
                     subunit 3, X-linked"
                     /EC_number="3.6.5.3"
                     /note="eIF-2-gamma X; eukaryotic translation initiation
                     factor 2 subunit gamma, X-linked; eIF2-gamma; eIF2-gamma
                     X; eukaryotic translation initiation factor 2, subunit 3,
                     structural gene X-linked; eukaryotic translation
                     initiation factor 2, subunit 3 gamma"
                     /calculated_mol_wt=50949
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P41091; propagated from
                     UniProtKB/Swiss-Prot (P81795.2)"
     Region          13..466
                     /region_name="PTZ00327"
                     /note="eukaryotic translation initiation factor 2 gamma
                     subunit; Provisional"
                     /db_xref="CDD:240362"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0N1; propagated from
                     UniProtKB/Swiss-Prot (P81795.2)"
     Region          48..55
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     Region          76..80
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     Region          134..137
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     Region          190..193
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     Region          225..227
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     Region          457..469
                     /region_name="Interacts with Cdc123.
                     /evidence=ECO:0000250|UniProtKB:P41091"
                     /note="propagated from UniProtKB/Swiss-Prot (P81795.2)"
     CDS             1..472
                     /gene="Eif2s3"
                     /gene_synonym="Eif2g; Eif2s3x; PP42"
                     /coded_by="NM_001100542.1:24..1442"
                     /db_xref="GeneID:299027"
                     /db_xref="RGD:1561279"
ORIGIN      
        1 maggeagvtl gqphlsrqdl atldvtkltp lshevisrqa tinigtighv ahgkstvvka
       61 isgvhtvrfk nelernitik lgyanakiyk lddpscprpe cyrscgsstp defptdipgt
      121 kgnfklvrhv sfvdcpghdi lmatmlngaa vmdaalllia gnescpqpqt sehlaaieim
      181 klkhililqn kidlvkesqa keqyeqilaf vqgtvaegap iipisaqlky nievvceyiv
      241 kkipvpprdf tseprlivir sfdvnkpgce vddlkggvag gsilkgvlkv gqeievrpgi
      301 vskdsegklm ckpifskivs lfaehndlqy aapggligvg tkidptlcra drmvgqvlga
      361 vgalpeifte leisyfllrr llgvrtegdk kaakvqklsk nevlmvnigs lstggrvsav
      421 kadlgkivlt npvctevgek ialsrrvekh wrligwgqir rgvtikptvd dd
//
LOCUS       NP_001020052             718 aa            linear   ROD 27-APR-2025
DEFINITION  tensin-4 precursor [Rattus norvegicus].
ACCESSION   NP_001020052 XP_239343
VERSION     NP_001020052.1
DBSOURCE    REFSEQ: accession NM_001024881.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Liao,Y.C., Si,L., deVere White,R.W. and Lo,S.H.
  TITLE     The phosphotyrosine-independent interaction of DLC-1 and the SH2
            domain of cten regulates focal adhesion localization and growth
            suppression activity of DLC-1
  JOURNAL   J Cell Biol 176 (1), 43-49 (2007)
   PUBMED   17190795
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097378.1.
            
            On Jun 17, 2005 this sequence version replaced XP_239343.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097378.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..718
                     /product="tensin-4 precursor"
                     /note="C-terminal tensin-like"
                     /calculated_mol_wt=75876
     sig_peptide     1..14
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q4V8I3.2)"
                     /calculated_mol_wt=1388
     mat_peptide     15..718
                     /product="Tensin-4. /id=PRO_0000248215"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8I3.2)"
                     /calculated_mol_wt=75876
     Region          188..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8I3.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZW8; propagated from
                     UniProtKB/Swiss-Prot (Q4V8I3.2)"
     Region          272..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8I3.2)"
     Region          447..560
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(458,476,512,514)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(513,542)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     Region          583..712
                     /region_name="PTB_tensin"
                     /note="Tensin Phosphotyrosine-binding (PTB) domain;
                     cd01213"
                     /db_xref="CDD:269924"
     Site            order(588,672,693)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269924"
     Site            order(652..657,679,702,706)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269924"
     CDS             1..718
                     /gene="Tns4"
                     /gene_synonym="RGD1310402"
                     /coded_by="NM_001024881.1:117..2273"
                     /db_xref="GeneID:303517"
                     /db_xref="RGD:1310402"
ORIGIN      
        1 mssslltggh vvsltphees rmalhptpsh dlpalcpyyt teswgtqplm dptlckgssn
       61 rlqqaqqaea raqcllqcpg eqasgasqdl dscidfslea lnkmileldp tfqllpsgia
      121 gpqaeptnsv asrtkkeepd aldikyievt strsrcldsp qrcsspcvtp pfgsprsggl
      181 flsrdipret rsssneslif sgnqgrgssp htpsslsnsi pcresrasgs platppgwek
      241 glrapqwgsr vstlsaspvs disyvfgsnq slphsslssy ppssrslgsp assssslhsl
      301 drgsqcvrss daqvpsnpiv gmgqpqavps tpvakeqass cppsvtnsma dipivlingn
      361 pepqsppaqq tpryqdsvqs ratspshlcq atkshsktlp dvpltspshl cqatkshskt
      421 lpdvpltasp espakdmqpt mkfvmdtsky wlkpsitreq ainllrtekp gtfvirdsss
      481 yrgsfglalk vqetpasapn rpgedstdfi rhflvessak gvhlkgadee pyfgslsafv
      541 cqhsimalal pckltipqke lggaepasds pthgqtsclk isagchtlyl tsvsvetlsg
      601 alavqkaisv mlerdvlptp tvvhfkvteq gitltdvqrk vffrrhypli alrfcgmdpe
      661 qrkwqkyckp srifgfvaks qtepqenach lfaeydaaqp asqvislvta llkdterv
//
LOCUS       NP_001119843             343 aa            linear   ROD 27-APR-2025
DEFINITION  arginine-hydroxylase NDUFAF5, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_001119843 XP_001080214 XP_215857
VERSION     NP_001119843.1
DBSOURCE    REFSEQ: accession NM_001126371.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Rhein,V.F., Carroll,J., Ding,S., Fearnley,I.M. and Walker,J.E.
  TITLE     NDUFAF5 Hydroxylates NDUFS7 at an Early Stage in the Assembly of
            Human Complex I
  JOURNAL   J Biol Chem 291 (28), 14851-14860 (2016)
   PUBMED   27226634
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Sugiana,C., Pagliarini,D.J., McKenzie,M., Kirby,D.M., Salemi,R.,
            Abu-Amero,K.K., Dahl,H.H., Hutchison,W.M., Vascotto,K.A.,
            Smith,S.M., Newbold,R.F., Christodoulou,J., Calvo,S., Mootha,V.K.,
            Ryan,M.T. and Thorburn,D.R.
  TITLE     Mutation of C20orf7 disrupts complex I assembly and causes lethal
            neonatal mitochondrial disease
  JOURNAL   Am J Hum Genet 83 (4), 468-478 (2008)
   PUBMED   18940309
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166551.1.
            
            On or before May 8, 2008 this sequence version replaced
            XP_001080214.1, XP_215857.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166551.1, FQ213977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..343
                     /product="arginine-hydroxylase NDUFAF5, mitochondrial
                     precursor"
                     /note="probable methyltransferase C20orf7 homolog,
                     mitochondrial; NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex assembly factor 5; NADH dehydrogenase
                     (ubiquinone) complex I, assembly factor 5; putative
                     methyltransferase NDUFAF5; arginine-hydroxylase NDUFAF5,
                     mitochondrial"
                     /calculated_mol_wt=35166
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (B2GV71.1)"
                     /calculated_mol_wt=3082
     Region          18..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV71.1)"
     mat_peptide     30..343
                     /product="Arginine-hydroxylase NDUFAF5, mitochondrial.
                     /id=PRO_0000358879"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV71.1)"
                     /calculated_mol_wt=35166
     Region          74..310
                     /region_name="BioC"
                     /note="malonyl-acyl carrier protein O-methyltransferase
                     BioC; TIGR02072"
                     /db_xref="CDD:273953"
     CDS             1..343
                     /gene="Ndufaf5"
                     /gene_synonym="RGD1309829"
                     /coded_by="NM_001126371.1:36..1067"
                     /db_xref="GeneID:296190"
                     /db_xref="RGD:1309829"
ORIGIN      
        1 mlrrvvlsrl yarlggpavs agrggrrgva ssvppsgsts pralnifdre lkrkqknwaa
       61 rqpepmkfdy lkeeigsria drvydiardf plaldigcgr gyiaqhlnke tvgkifqtdi
      121 aehalknsie tdiptvnila deeflpfpen tfdlvvssls lhwvndlpra leqihyvlkp
      181 dgvfvgamfg gdtlyelrcs lqlaetereg gfsphispft avndlghllg ragfntltvd
      241 tdeiqvnypg mfelmedlkg mgesncswnr kallhrdtml aaaavyremy snedgsipat
      301 yqiyhmigwk yhdsqarpae rgsatvsfgd larlndtmsq gkk
//
LOCUS       NP_001020916             257 aa            linear   ROD 27-APR-2025
DEFINITION  AN1-type zinc finger protein 2B [Rattus norvegicus].
ACCESSION   NP_001020916 XP_343594
VERSION     NP_001020916.1
DBSOURCE    REFSEQ: accession NM_001025745.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Rahighi,S., Braunstein,I., Ternette,N., Kessler,B., Kawasaki,M.,
            Kato,R., Matsui,T., Weiss,T.M., Stanhill,A. and Wakatsuki,S.
  TITLE     Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked
            Tri-Ubiquitin Chains
  JOURNAL   Structure 24 (3), 412-422 (2016)
   PUBMED   26876100
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Osorio,F.G., Soria-Valles,C., Santiago-Fernandez,O., Bernal,T.,
            Mittelbrunn,M., Colado,E., Rodriguez,F., Bonzon-Kulichenko,E.,
            Vazquez,J., Porta-de-la-Riva,M., Ceron,J., Fueyo,A., Li,J.,
            Green,A.R., Freije,J.M. and Lopez-Otin,C.
  TITLE     Loss of the proteostasis factor AIRAPL causes myeloid
            transformation by deregulating IGF-1 signaling
  JOURNAL   Nat Med 22 (1), 91-96 (2016)
   PUBMED   26692333
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Glinka,T., Alter,J., Braunstein,I., Tzach,L., Wei Sheng,C.,
            Geifman,S., Edelmann,M.J., Kessler,B.M. and Stanhill,A.
  TITLE     Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
            complex
  JOURNAL   Biochem J 457 (2), 253-261 (2014)
   PUBMED   24160817
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Yun,C., Stanhill,A., Yang,Y., Zhang,Y., Haynes,C.M., Xu,C.F.,
            Neubert,T.A., Mor,A., Philips,M.R. and Ron,D.
  TITLE     Proteasomal adaptation to environmental stress links resistance to
            proteotoxicity with longevity in Caenorhabditis elegans
  JOURNAL   Proc Natl Acad Sci U S A 105 (19), 7094-7099 (2008)
   PUBMED   18467495
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099215.1.
            
            On Jul 22, 2005 this sequence version replaced XP_343594.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099215.1, SRR8487227.120884.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..257
                     /product="AN1-type zinc finger protein 2B"
                     /note="AIRAP-like protein; arsenite-inducible
                     RNA-associated protein-like protein; zinc finger, AN1 type
                     domain 2B"
                     /calculated_mol_wt=27794
     mat_peptide     1..254
                     /product="AN1-type zinc finger protein 2B.
                     /evidence=ECO:0000250|UniProtKB:Q91X58.
                     /id=PRO_0000232878"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLG9.1)"
                     /calculated_mol_wt=27622
     Region          10..46
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          100..136
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          141..151
                     /region_name="VCP/p97-interacting motif (VIM).
                     /evidence=ECO:0000250|UniProtKB:Q8WV99"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Region          153..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91X58; propagated from
                     UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91X58; propagated from
                     UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Region          197..213
                     /region_name="UIM"
                     /note="Ubiquitin interaction motif; pfam02809"
                     /db_xref="CDD:460703"
     Region          254..257
                     /region_name="CAAX motif.
                     /evidence=ECO:0000250|UniProtKB:Q91X58"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLG9.1)"
     Site            254
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:Q91X58; propagated from
                     UniProtKB/Swiss-Prot (Q4KLG9.1)"
     CDS             1..257
                     /gene="Zfand2b"
                     /gene_synonym="RGD1306260"
                     /coded_by="NM_001025745.1:199..972"
                     /db_xref="GeneID:363253"
                     /db_xref="RGD:1306260"
ORIGIN      
        1 mefpdlgahc sepscqrldf lplkcdacsg ifcadhvaya hhhcgsayqk diqvpvcplc
       61 nvpvpvarge ppdravgehi drdcrsdpaq qkrkiftnkc ersgcrqrem mkltcdrcgr
      121 nfcikhrhpl dhdcsgeghp tsraglaais raqglastst vpspsrtlps ssspsratpq
      181 lpprttspvi alqnglsede alqralelsl aeakpqipss qeeedlalaq alsaseaeyq
      241 qqqaqsrslk psncslc
//
LOCUS       NP_001006965             334 aa            linear   ROD 27-APR-2025
DEFINITION  BRISC and BRCA1-A complex member 1 [Rattus norvegicus].
ACCESSION   NP_001006965 XP_214301
VERSION     NP_001006965.1
DBSOURCE    REFSEQ: accession NM_001006964.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Rozenova,K., Jiang,J., Donaghy,R., Aressy,B., Greenberg,R.A. and
            Tong,W.
  TITLE     MERIT40 deficiency expands hematopoietic stem cell pools by
            regulating thrombopoietin receptor signaling
  JOURNAL   Blood 125 (11), 1730-1738 (2015)
   PUBMED   25636339
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Zheng,H., Gupta,V., Patterson-Fortin,J., Bhattacharya,S.,
            Katlinski,K., Wu,J., Varghese,B., Carbone,C.J., Aressy,B.,
            Fuchs,S.Y. and Greenberg,R.A.
  TITLE     A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates
            interferon responses
  JOURNAL   Cell Rep 5 (1), 180-193 (2013)
   PUBMED   24075985
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Cooper,E.M., Cutcliffe,C., Kristiansen,T.Z., Pandey,A.,
            Pickart,C.M. and Cohen,R.E.
  TITLE     K63-specific deubiquitination by two JAMM/MPN+ complexes:
            BRISC-associated Brcc36 and proteasomal Poh1
  JOURNAL   EMBO J 28 (6), 621-631 (2009)
   PUBMED   19214193
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Wang,B., Hurov,K., Hofmann,K. and Elledge,S.J.
  TITLE     NBA1, a new player in the Brca1 A complex, is required for DNA
            damage resistance and checkpoint control
  JOURNAL   Genes Dev 23 (6), 729-739 (2009)
   PUBMED   19261749
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Feng,L., Huang,J. and Chen,J.
  TITLE     MERIT40 facilitates BRCA1 localization and DNA damage repair
  JOURNAL   Genes Dev 23 (6), 719-728 (2009)
   PUBMED   19261748
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Shao,G., Patterson-Fortin,J., Messick,T.E., Feng,D., Shanbhag,N.,
            Wang,Y. and Greenberg,R.A.
  TITLE     MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to
            DNA double-strand breaks
  JOURNAL   Genes Dev 23 (6), 740-754 (2009)
   PUBMED   19261746
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083685.1.
            
            On Nov 22, 2004 this sequence version replaced XP_214301.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083685.1, FQ233705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..334
                     /product="BRISC and BRCA1-A complex member 1"
                     /note="BRCA1-A complex subunit MERIT40; new component of
                     the BRCA1-A complex; mediator of RAP80 interactions and
                     targeting subunit of 40 kDa"
                     /calculated_mol_wt=36747
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWV8; propagated from
                     UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Region          <24..>93
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NWV8; propagated from
                     UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Region          96..316
                     /region_name="vWA_BABAM1"
                     /note="Von-Willebrand factor A (vWA) domain found in BRISC
                     and BRCA1-A complex member 1; cd21502"
                     /db_xref="CDD:411071"
     Region          100..303
                     /region_name="VWFA-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIJ6.1)"
     Site            order(131,134..135,138..139,142..144,297..298,301,
                     304..305,309..311,315..316)
                     /site_type="other"
                     /note="BRCA1-A/BRISC complex interface [polypeptide
                     binding]"
                     /db_xref="CDD:411071"
     CDS             1..334
                     /gene="Babam1"
                     /gene_synonym="Merit40"
                     /coded_by="NM_001006964.1:183..1187"
                     /db_xref="GeneID:290631"
                     /db_xref="RGD:1359516"
ORIGIN      
        1 mevaeanspt eeeeeeeeee geepiseprp htrsnpegae draigaqanv gsrsegegea
       61 ataddgaasv pgavpkpwqv papasevqir tprvncpekv iicldlseem svpklesfng
      121 srtnalnvsq kmvemfvrtk hkidkshefa lvvvnddsaw lsgltsdpre lcsclydlet
      181 ascstfnleg lfsliqqkte lpvtenvqti pppyvvrtil vysrppcqpq fsltepmkkm
      241 fqcpyfffdi iyihsgpeek eddmswkdmf afmgsldtkg tsykyavala gpalelhncv
      301 akllahplqr pcqshasysl leedeeageg eatv
//
LOCUS       NP_001013897             385 aa            linear   ROD 27-APR-2025
DEFINITION  rhomboid domain-containing protein 3 [Rattus norvegicus].
ACCESSION   NP_001013897 XP_214071
VERSION     NP_001013897.1
DBSOURCE    REFSEQ: accession NM_001013875.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Liu,J., Liu,S., Xia,M., Xu,S., Wang,C., Bao,Y., Jiang,M., Wu,Y.,
            Xu,T. and Cao,X.
  TITLE     Rhomboid domain-containing protein 3 is a negative regulator of
            TLR3-triggered natural killer cell activation
  JOURNAL   Proc Natl Acad Sci U S A 110 (19), 7814-7819 (2013)
   PUBMED   23610400
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081912.1.
            
            On Apr 20, 2005 this sequence version replaced XP_214071.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081912.1, SRR8487230.142987.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..385
                     /product="rhomboid domain-containing protein 3"
                     /calculated_mol_wt=40967
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B3.1)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B3.1)"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B3.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B3.1)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B3.1)"
     Region          326..369
                     /region_name="UBA_like_SF"
                     /note="UBA domain-like superfamily; cl21463"
                     /db_xref="CDD:473871"
     CDS             1..385
                     /gene="Rhbdd3"
                     /gene_synonym="RGD1311827"
                     /coded_by="NM_001013875.1:546..1703"
                     /db_xref="GeneID:289753"
                     /db_xref="RGD:1311827"
ORIGIN      
        1 mhawdppasl sralplassv lmlllsclwl lgagpslrla pelltepwqv hrllthalgh
       61 talpglllsl lllptlgwwq echlgtlrfl hnsavlalat gllavllagl glssaaggcg
      121 ympvhlamla gqsyypgwpq rtlppwllpw lllaltllls seppflqllc gllaglayaa
      181 gafrwlelse rrlqvlqegv lcrtlagcwp lkllptpgsl gelpvtypag vrpatprppy
      241 lasssswpht dgfaqlppgl gpgqltwkns erdldwagps fasatpmwaa ldeqmlqegi
      301 qaslldvsvq gsqntlwspk psvsslrlqq lqhmgfpteq aavalaatgr vegavsllve
      361 glvdtealvt eersgpahck dtgvs
//
LOCUS       NP_001019968            2256 aa            linear   ROD 27-APR-2025
DEFINITION  GON-4-like protein [Rattus norvegicus].
ACCESSION   NP_001019968 XP_342279 XP_574976
VERSION     NP_001019968.1
DBSOURCE    REFSEQ: accession NM_001024797.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2256)
  AUTHORS   Lu,P., Hankel,I.L., Hostager,B.S., Swartzendruber,J.A.,
            Friedman,A.D., Brenton,J.L., Rothman,P.B. and Colgan,J.D.
  TITLE     The developmental regulator protein Gon4l associates with protein
            YY1, co-repressor Sin3a, and histone deacetylase 1 and mediates
            transcriptional repression
  JOURNAL   J Biol Chem 286 (20), 18311-18319 (2011)
   PUBMED   21454521
REFERENCE   2  (residues 1 to 2256)
  AUTHORS   Lu,P., Hankel,I.L., Knisz,J., Marquardt,A., Chiang,M.Y., Grosse,J.,
            Constien,R., Meyer,T., Schroeder,A., Zeitlmann,L., Al-Alem,U.,
            Friedman,A.D., Elliott,E.I., Meyerholz,D.K., Waldschmidt,T.J.,
            Rothman,P.B. and Colgan,J.D.
  TITLE     The Justy mutation identifies Gon4-like as a gene that is essential
            for B lymphopoiesis
  JOURNAL   J Exp Med 207 (7), 1359-1367 (2010)
   PUBMED   20530203
REFERENCE   3  (residues 1 to 2256)
  AUTHORS   Ohtomo,T., Horii,T., Nomizu,M., Suga,T. and Yamada,J.
  TITLE     Cloning and expression analysis of YY1AP-related protein in the rat
            brain
  JOURNAL   Amino Acids 34 (1), 155-161 (2008)
   PUBMED   17285227
  REMARK    GeneRIF: suggest that YARP functions at a late stage of
            neurogenesis during perinatal development of the rat brain, as well
            as in mature neurons.
REFERENCE   4  (residues 1 to 2256)
  AUTHORS   Kuryshev,V.Y., Vorobyov,E., Zink,D., Schmitz,J.,
            Rozhdestvensky,T.S., Munstermann,E., Ernst,U., Wellenreuther,R.,
            Moosmayer,P., Bechtel,S., Schupp,I., Horst,J., Korn,B., Poustka,A.
            and Wiemann,S.
  TITLE     An anthropoid-specific segmental duplication on human chromosome
            1q22
  JOURNAL   Genomics 88 (2), 143-151 (2006)
   PUBMED   16545939
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY724781.1.
            
            On or before Jul 26, 2005 this sequence version replaced
            XP_574976.1, XP_342279.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY724781.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132278
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2256
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2256
                     /product="GON-4-like protein"
                     /note="YY1AP-related protein1; GON-4 homolog"
                     /calculated_mol_wt=247773
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          105..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          227..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          366..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          441..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          545..573
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          609..1363
                     /region_name="Required for interaction with YY1, SIN3A and
                     HDAC1, and transcriptional repression activity.
                     /evidence=ECO:0000250|UniProtKB:Q9DB00"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DB00; propagated from
                     UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          947..969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          <991..1291
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1078..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          1241..1288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          1360..1620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Site            1445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3T8J9; propagated from
                     UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          1668..1713
                     /region_name="PAH"
                     /note="Paired amphipathic helix repeat; pfam02671"
                     /db_xref="CDD:460645"
     Region          <1768..1794
                     /region_name="PAH"
                     /note="Paired amphipathic helix repeat; pfam02671"
                     /db_xref="CDD:460645"
     Region          1831..1886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          1909..1966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Site            1921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3T8J9; propagated from
                     UniProtKB/Swiss-Prot (Q535K8.1)"
     Site            1994
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3T8J9; propagated from
                     UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          2050..2078
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          2110..2148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     Region          2158..2223
                     /region_name="CASP8AP2"
                     /note="Caspase 8-associated protein 2 myb-like domain;
                     cd12202"
                     /db_xref="CDD:213401"
     Region          2223..2256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q535K8.1)"
     CDS             1..2256
                     /gene="Gon4l"
                     /gene_synonym="Dingo; Yarp"
                     /coded_by="NM_001024797.1:266..7036"
                     /db_xref="GeneID:499653"
                     /db_xref="RGD:1564691"
ORIGIN      
        1 mlpckkrsgv tesaqqqddq egedlhleaa vkpdtdqlpd ctseslswgq shdsagcpev
       61 hsmqdvgsql svegtplssk mltqrvnlav seavdvpvsq eipvpsless hslpvhmgkg
      121 rlqstasrkg kkiafmpgqv tredggdhtv peeppsgeha eevkaeggel emhsegdlps
      181 lssgsqsakp raqprksfqp dgsafpqeks lgplvrqaee dmedgglfip teeqdgeesd
      241 krkktkkgtk rkrdgrgqeq gtmtydpkvd dmldrtledg akqhnltavn vrnilhevit
      301 nehvvammka aisetedmpl fepkmtrskl kevvekgvvi ptwnispikk asetkqppqf
      361 vdihleddds sdeeyqpdee eedetaeesl lesdvesaas sprgvkrsrl rlsseaaead
      421 eesgvlseve kvatpalrhi saevvpmgpp pppkpkqtrd stfmeklnav deelaaspvc
      481 mdsfqpmeds liafrtrskm plkdvplgql eaelqapdit pdmydpntad dedwklwlgg
      541 llnddvened eadddddpey nfledldepd tedfrtdrav ritkkevngl meelfetvqs
      601 vvpskfqdem gfsnmeddgp eeeervtesr psfntpqalr feeplanlln erhrtvkell
      661 eqlkmkkssv rqqpeveklk pqtekvhqtl vldpaqrsrl qqqmqqhvql ltqiylltts
      721 npnlsseast trvflkelgt faenstalhq qfnprfqtlf qpcnwvgamq liedfthisi
      781 dcsphktvkk tasefpclpk qvawilatnk vfmypellpi cslkannprd ktiftkaedn
      841 llalglkhfe gtefpkplis kylvtcktah qltvriknln lnrapnnvik fykktkqlpv
      901 lvrcceeiqp hqwkppieke ehrlpfwlka slqsiqeelr nlaggatagg svtaatetst
      961 dqhlqktspv vggdtqypll lpkgvvlklk pgskrfsrka wrqkrplvqk plliqpspsv
     1021 qpvfnpgkma twptqsevpp sntvvqiphl iqpaavlqtl pgfpsvgvcg edsfespaal
     1081 pampsgsear tsfpwsesqs appsssapkl mlpslgpskf rkpyvrrkpt rrkgakaspc
     1141 vkpapiihpt pviftvpatt vkvvslgggc nmiqpvtaav apspqtipit tllvnptsfp
     1201 cslnqplvas sispllvssn plalpvtslp eekahvsldi aegknapqnp epkikpqept
     1261 pqcatvfske eprswhpsad tgnqeavses sacswaavkt egqegsseks vcgwtvvkte
     1321 dgghavqplp qdpqdslnsp skdllnmvkl eaedcmeeis sdfpkqdige evkeeccmel
     1381 drdspqekas svsemskqta tpreetqaak sptvsqdapd airdaskglp qstlssmdqg
     1441 tvlnsppgkp edsanadgqs vgtpagtdtg aekdgaeeee eedfddltqd eedelssase
     1501 esvlsvpelq etmekltwla serrmsqege seeensqeen sepeeeeeee aegmetlqke
     1561 deatdeaggg aaekppstla sphtapevet sitpagesik aagkgrsshr arsrrgsrar
     1621 askdasklll lydedildrd plreqkdlaf aqayltrvre alqhipgkye dflqiiyefe
     1681 snaqmhsavd lfkslqtllh dwpqllkdfa afllpeqals cglfeeqqaf eksrkflrql
     1741 eicfaenpsh hqkiikvlqg cadclpqdit elktqmwqll rghdhlqdef siffdhlrpa
     1801 anrmgdfeei nwteekeyef dgfeevilpe veeeeepakv staskskrrk eigvqhqdke
     1861 sewpeaakdg scpcheggpe sklkkskrrn chcsskvcds ksykskeple lvgsgplqea
     1921 stvpgtkeag qgkdmseeet megqenvevs qnktgrttrk geapipgstv rtallcsaev
     1981 tpielslegp tccspetprl ppqtgavvcs vrrnqagpev vsclgtssip pkegedqkav
     2041 ansetiaplp etseterlpg tvelpaplps pvslstrdtg rrhiygkagt qswlldnrae
     2101 akaahmvapi rgtssgasas eaaptasreg laedsetqgk gpeavlpkas eatvcannsk
     2161 vsstgekvvl wtreadrvil tmcqeqgaqp htfsvisqql gnktpvevsh rfrelmqlfh
     2221 taceassede ddatstsnad qlsdhgdlls eeelde
//
LOCUS       NP_908937                264 aa            linear   ROD 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 9 [Rattus
            norvegicus].
ACCESSION   NP_908937
VERSION     NP_908937.2
DBSOURCE    REFSEQ: accession NM_184048.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Malkowska,M., Kokoszynska,K., Rychlewski,L. and Wyrwicz,L.
  TITLE     Structural bioinformatics of the general transcription factor TFIID
  JOURNAL   Biochimie 95 (4), 680-691 (2013)
   PUBMED   23146842
  REMARK    Review article
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Sengupta,T., Cohet,N., Morle,F. and Bieker,J.J.
  TITLE     Distinct modes of gene regulation by a cell-specific
            transcriptional activator
  JOURNAL   Proc Natl Acad Sci U S A 106 (11), 4213-4218 (2009)
   PUBMED   19251649
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Tatarakis,A., Margaritis,T., Martinez-Jimenez,C.P., Kouskouti,A.,
            Mohan,W.S. 2nd, Haroniti,A., Kafetzopoulos,D., Tora,L. and
            Talianidis,I.
  TITLE     Dominant and redundant functions of TFIID involved in the
            regulation of hepatic genes
  JOURNAL   Mol Cell 31 (4), 531-543 (2008)
   PUBMED   18722179
REFERENCE   5  (residues 1 to 264)
  AUTHORS   McKeegan,K.S., Debieux,C.M., Boulon,S., Bertrand,E. and
            Watkins,N.J.
  TITLE     A dynamic scaffold of pre-snoRNP factors facilitates human box C/D
            snoRNP assembly
  JOURNAL   Mol Cell Biol 27 (19), 6782-6793 (2007)
   PUBMED   17636026
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Buschmann,T., Lin,Y., Aithmitti,N., Fuchs,S.Y., Lu,H.,
            Resnick-Silverman,L., Manfredi,J.J., Ronai,Z. and Wu,X.
  TITLE     Stabilization and activation of p53 by the coactivator protein
            TAFII31
  JOURNAL   J Biol Chem 276 (17), 13852-13857 (2001)
   PUBMED   11278372
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Fontes,J.D., Jiang,B. and Peterlin,B.M.
  TITLE     The class II trans-activator CIITA interacts with the
            TBP-associated factor TAFII32
  JOURNAL   Nucleic Acids Res 25 (12), 2522-2528 (1997)
   PUBMED   9171108
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Aoki,T., Koike,T., Nakano,T., Shibahara,K., Nishimura,H.,
            Kikuchi,H. and Honjo,T.
  TITLE     Rat TAFII31 gene is induced upon programmed cell death in
            differentiated PC12 cells deprived of NGF
  JOURNAL   Biochem Biophys Res Commun 234 (1), 230-234 (1997)
   PUBMED   9168994
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB743840.1 and BC091109.1.
            
            On Jun 29, 2005 this sequence version replaced NP_908937.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 3. Both variants 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213120.1, FQ215462.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..264
                     /product="transcription initiation factor TFIID subunit 9"
                     /EC_number="2.7.4.3"
                     /note="TAF9 RNA polymerase II, TATA box binding
                     protein-associated factor; RNA polymerase II
                     TBP-associated factor subunit G; transcription initiation
                     factor TFIID 31 kDa subunit; transcription initiation
                     factor TFIID 32 kDa subunit; TAF9 RNA polymerase II, TATA
                     box binding protein (TBP)-associated factor"
                     /calculated_mol_wt=28863
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          9..130
                     /region_name="TFIID-31kDa"
                     /note="Transcription initiation factor IID, 31kD subunit;
                     pfam02291"
                     /db_xref="CDD:460525"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          150..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          233..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKE0.1)"
     CDS             1..264
                     /gene="Taf9"
                     /gene_synonym="CINAP; TAFII31; TAFII32"
                     /coded_by="NM_184048.2:190..984"
                     /db_xref="GeneID:373541"
                     /db_xref="RGD:727861"
ORIGIN      
        1 mesgkmaspk smpkdaqmma qilkdmgite yeprvinqml efafryvtti lddakiyssh
       61 akkptvdadd vrlaiqcrad qsftsppprd flldiarqrn qtplplikpy sgprlppdry
      121 cltapnyrlk slqkkaptpa gritvprlsv gsvssrpstp tlgtptpqam svstkvgtpm
      181 sltgqrftvq mpasqspavk asipatpavq nvlinpslig sknilittnm vsqntanesa
      241 nalkrkreee dddddddddd ydnl
//
LOCUS       NP_077048                168 aa            linear   ROD 27-APR-2025
DEFINITION  DNA damage-inducible transcript 3 protein [Rattus norvegicus].
ACCESSION   NP_077048
VERSION     NP_077048.2
DBSOURCE    REFSEQ: accession NM_024134.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Mou,L., Sun,D., Qu,J., Tan,X., Wang,S., Zeng,Q. and Liu,C.
  TITLE     GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline
  JOURNAL   J Hazard Mater 476, 135101 (2024)
   PUBMED   39002476
  REMARK    GeneRIF: GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline.
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Ishteyaque,S., Yadav,K.S., Verma,S., Washimkar,K.R. and Mugale,M.N.
  TITLE     CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit apoptosis
            and promotes progression of hepatocellular carcinoma
  JOURNAL   Arch Biochem Biophys 745, 109701 (2023)
   PUBMED   37499993
  REMARK    GeneRIF: CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit
            apoptosis and promotes progression of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Wang,S., Duan,J., Liao,J., Wang,Y., Xiao,X., Li,L., Liu,Y., Gu,H.,
            Yang,P., Fu,D., Du,J., Li,X. and Shao,M.
  TITLE     LncRNA H19 inhibits ER stress induced apoptosis and improves
            diabetic cardiomyopathy by regulating PI3K/AKT/mTOR axis
  JOURNAL   Aging (Albany NY) 14 (16), 6809-6828 (2022)
   PUBMED   36044268
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Yuan,Z., Xiao-Wei,L., Juan,W., Xiu-Juan,L., Nian-Yun,Z. and Lei,S.
  TITLE     HIIT and MICT attenuate high-fat diet-induced hepatic lipid
            accumulation and ER stress via the PERK-ATF4-CHOP signaling pathway
  JOURNAL   J Physiol Biochem 78 (3), 641-652 (2022)
   PUBMED   35315506
  REMARK    GeneRIF: HIIT and MICT attenuate high-fat diet-induced hepatic
            lipid accumulation and ER stress via the PERK-ATF4-CHOP signaling
            pathway.
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Zhan,W., Chen,L., Liu,H., Long,C., Liu,J., Ding,S., Wu,Q. and
            Chen,S.
  TITLE     Pcsk6 Deficiency Promotes Cardiomyocyte Senescence by Modulating
            Ddit3-Mediated ER Stress
  JOURNAL   Genes (Basel) 13 (4), 711 (2022)
   PUBMED   35456517
  REMARK    GeneRIF: Pcsk6 Deficiency Promotes Cardiomyocyte Senescence by
            Modulating Ddit3-Mediated ER Stress.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Jousse,C., Bruhat,A., Carraro,V., Urano,F., Ferrara,M., Ron,D. and
            Fafournoux,P.
  TITLE     Inhibition of CHOP translation by a peptide encoded by an open
            reading frame localized in the chop 5'UTR
  JOURNAL   Nucleic Acids Res 29 (21), 4341-4351 (2001)
   PUBMED   11691921
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Sylvester,S.L., ap Rhys,C.M., Luethy-Martindale,J.D. and
            Holbrook,N.J.
  TITLE     Induction of GADD153, a CCAAT/enhancer-binding protein
            (C/EBP)-related gene, during the acute phase response in rats.
            Evidence for the involvement of C/EBPs in regulating its expression
  JOURNAL   J Biol Chem 269 (31), 20119-20125 (1994)
   PUBMED   8051100
  REMARK    Erratum:[J Biol Chem. 1995 Jun 16;270(24):14842. PMID: 7782352]
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Aman,P., Ron,D., Mandahl,N., Fioretos,T., Heim,S., Arheden,K.,
            Willen,H., Rydholm,A. and Mitelman,F.
  TITLE     Rearrangement of the transcription factor gene CHOP in myxoid
            liposarcomas with t(12;16)(q13;p11)
  JOURNAL   Genes Chromosomes Cancer 5 (4), 278-285 (1992)
   PUBMED   1283316
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Ron,D. and Habener,J.F.
  TITLE     CHOP, a novel developmentally regulated nuclear protein that
            dimerizes with transcription factors C/EBP and LAP and functions as
            a dominant-negative inhibitor of gene transcription
  JOURNAL   Genes Dev 6 (3), 439-453 (1992)
   PUBMED   1547942
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Kesterton,D.B.
  TITLE     A projectionist speaks
  JOURNAL   Med Biol Illus 27 (1), 15-19 (1977)
   PUBMED   70575
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CF977695.1, AW916370.1, U30186.1 and BF282473.1.
            
            On Oct 19, 2007 this sequence version replaced NP_077048.1.
            
            Transcript Variant: This variant (2) lacks a segment in the 5' UTR,
            compared to variant 2. Variants 1 and 2 both encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF977695.1, U30186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..168
                     /product="DNA damage-inducible transcript 3 protein"
                     /note="C/EBP homologous protein; DDIT-3; growth arrest and
                     DNA-damage-inducible protein GADD153; c/EBP-homologous
                     protein 10; C/EBP zeta; CCAAT/enhancer-binding protein
                     homologous protein"
                     /calculated_mol_wt=18897
     Region          10..26
                     /region_name="N-terminal. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Region          10..18
                     /region_name="Interaction with TRIB3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Region          34..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:P35639; propagated from
                     UniProtKB/Swiss-Prot (Q62857.1)"
     Region          100..160
                     /region_name="BRLZ"
                     /note="basic region leucin zipper; smart00338"
                     /db_xref="CDD:197664"
     Region          100..129
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     Region          101..152
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269861"
     Site            order(104..105,107..109,111..116,118..120)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269861"
     Site            order(119,122..123,126..127,129..130,133..134,136..137,
                     140..141,143..144,147..148,150..151)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269861"
     Region          133..147
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62857.1)"
     CDS             1..168
                     /gene="Ddit3"
                     /gene_synonym="CHOP; CHOP-10; Chop10; Gadd153; RM4"
                     /coded_by="NM_024134.2:119..625"
                     /db_xref="GeneID:29467"
                     /db_xref="RGD:62391"
ORIGIN      
        1 maaeslpfaf etvsswelea wyedlqevls sdeiggtyis spgneeeesk tfttldpasl
       61 awlteepgpa evtstsqspr spdssqssma qeeeeedqgr trkrkqsgqc aaragkqrmk
      121 ekeqenerkv aqlaeenerl kqeierltre vettrralid rmvslhqa
//
LOCUS       NP_065413                398 aa            linear   ROD 27-APR-2025
DEFINITION  arylacetamide deacetylase [Rattus norvegicus].
ACCESSION   NP_065413
VERSION     NP_065413.1
DBSOURCE    REFSEQ: accession NM_020538.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Lo,V., Erickson,B., Thomason-Hughes,M., Ko,K.W., Dolinsky,V.W.,
            Nelson,R. and Lehner,R.
  TITLE     Arylacetamide deacetylase attenuates fatty-acid-induced
            triacylglycerol accumulation in rat hepatoma cells
  JOURNAL   J Lipid Res 51 (2), 368-377 (2010)
   PUBMED   19654421
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Watanabe,A., Fukami,T., Nakajima,M., Takamiya,M., Aoki,Y. and
            Yokoi,T.
  TITLE     Human arylacetamide deacetylase is a principal enzyme in flutamide
            hydrolysis
  JOURNAL   Drug Metab Dispos 37 (7), 1513-1520 (2009)
   PUBMED   19339378
  REMARK    Erratum:[Drug Metab Dispos. 2014 Jun;42(6):1066]
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Ross,M.K. and Crow,J.A.
  TITLE     Human carboxylesterases and their role in xenobiotic and endobiotic
            metabolism
  JOURNAL   J Biochem Mol Toxicol 21 (4), 187-196 (2007)
   PUBMED   17936933
  REMARK    Review article
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Frick,C., Atanasov,A.G., Arnold,P., Ozols,J. and Odermatt,A.
  TITLE     Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1
            in the endoplasmic reticulum lumen is dependent on its N-terminal
            region sharing similar topological determinants with 50-kDa
            esterase
  JOURNAL   J Biol Chem 279 (30), 31131-31138 (2004)
   PUBMED   15152005
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Trickett,J.I., Patel,D.D., Knight,B.L., Saggerson,E.D.,
            Gibbons,G.F. and Pease,R.J.
  TITLE     Characterization of the rodent genes for arylacetamide deacetylase,
            a putative microsomal lipase, and evidence for transcriptional
            regulation
  JOURNAL   J Biol Chem 276 (43), 39522-39532 (2001)
   PUBMED   11481320
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Mziaut,H., Korza,G., Hand,A.R., Gerard,C. and Ozols,J.
  TITLE     Targeting proteins to the lumen of endoplasmic reticulum using
            N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the
            50-kDa esterase
  JOURNAL   J Biol Chem 274 (20), 14122-14129 (1999)
   PUBMED   10318829
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Ozols,J.
  TITLE     Determination of lumenal orientation of microsomal 50-kDa
            esterase/N-deacetylase
  JOURNAL   Biochemistry 37 (28), 10336-10344 (1998)
   PUBMED   9665742
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF182426.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF182426.1, BC088143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..398
                     /product="arylacetamide deacetylase"
                     /EC_number="3.1.1.3"
                     /note="arylacetamide deacetylase (esterase)"
                     /calculated_mol_wt=45562
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZH8.3)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZH8.3)"
     Region          106..373
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
     Region          110..112
                     /region_name="Involved in the stabilization of the
                     negatively charged intermediate by the formation of the
                     oxyanion hole. /evidence=ECO:0000250|UniProtKB:Q5NUF3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZH8.3)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZH8.3)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZH8.3)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZH8.3)"
     CDS             1..398
                     /gene="Aadac"
                     /gene_synonym="Aada"
                     /coded_by="NM_020538.1:26..1222"
                     /db_xref="GeneID:57300"
                     /db_xref="RGD:631440"
ORIGIN      
        1 mgrtifllis vvlvayyiyi plpddieepw kiilgntllk lggdlasfge llglnhfmdt
       61 vqlfmrfqvv pptsdenvtv metdfnsvpv riyipkrkst tlrrglffih gggwclgsaa
      121 yfmydtlsrr tahrldavvv stdyglapky hfpkqfedvy hslrwflqed ilekygvdpr
      181 rvgvsgdsag gnltaavtqq ilqdpdvkik lkvqaliypa lqaldmnvps qqensqypll
      241 trsllirfws eyfttdrdle kamllnqhvp vefshllqfv nwssllpqry kkgyfyktpt
      301 pgslelaqky pgftdvkacp llandsilhh lpmtyiitcq ydvlrddglm yvkrlqntgv
      361 hvthhhiedg fhgaltlpgl kityrmqnqy lnwlhknl
//
LOCUS       NP_037100                570 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-1 receptor accessory protein precursor [Rattus
            norvegicus].
ACCESSION   NP_037100
VERSION     NP_037100.1
DBSOURCE    REFSEQ: accession NM_012968.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Ishiguro,T., Takeda,J., Fang,X., Bronson,H. and Olson,D.M.
  TITLE     Interleukin (IL)-1 in rat parturition: IL-1 receptors 1 and 2 and
            accessory proteins abundance in pregnant rat uterus at term -
            regulation by progesterone
  JOURNAL   Physiol Rep 4 (14) (2016)
   PUBMED   27440742
  REMARK    GeneRIF: Activity of Il-1 in parturition is regulated by
            progesterone via Il1R1/Il1R2/Il-1RAcp pathway.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Yamagata,A., Yoshida,T., Sato,Y., Goto-Ito,S., Uemura,T., Maeda,A.,
            Shiroshima,T., Iwasawa-Okamoto,S., Mori,H., Mishina,M. and Fukai,S.
  TITLE     Mechanisms of splicing-dependent trans-synaptic adhesion by
            PTPdelta-IL1RAPL1/IL-1RAcP for synaptic differentiation
  JOURNAL   Nat Commun 6, 6926 (2015)
   PUBMED   25908590
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Yoshida,T., Shiroshima,T., Lee,S.J., Yasumura,M., Uemura,T.,
            Chen,X., Iwakura,Y. and Mishina,M.
  TITLE     Interleukin-1 receptor accessory protein organizes neuronal
            synaptogenesis as a cell adhesion molecule
  JOURNAL   J Neurosci 32 (8), 2588-2600 (2012)
   PUBMED   22357843
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Gardoni,F., Boraso,M., Zianni,E., Corsini,E., Galli,C.L.,
            Cattabeni,F., Marinovich,M., Di Luca,M. and Viviani,B.
  TITLE     Distribution of interleukin-1 receptor complex at the synaptic
            membrane driven by interleukin-1beta and NMDA stimulation
  JOURNAL   J Neuroinflammation 8 (1), 14 (2011)
   PUBMED   21314939
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Ali,S., Huber,M., Kollewe,C., Bischoff,S.C., Falk,W. and
            Martin,M.U.
  TITLE     IL-1 receptor accessory protein is essential for IL-33-induced
            activation of T lymphocytes and mast cells
  JOURNAL   Proc Natl Acad Sci U S A 104 (47), 18660-18665 (2007)
   PUBMED   18003919
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Chackerian,A.A., Oldham,E.R., Murphy,E.E., Schmitz,J., Pflanz,S.
            and Kastelein,R.A.
  TITLE     IL-1 receptor accessory protein and ST2 comprise the IL-33 receptor
            complex
  JOURNAL   J Immunol 179 (4), 2551-2555 (2007)
   PUBMED   17675517
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Teshima,S., Nakanishi,H., Nishizawa,M., Kitagawa,K., Kaibori,M.,
            Yamada,M., Habara,K., Kwon,A.H., Kamiyama,Y., Ito,S. and Okumura,T.
  TITLE     Up-regulation of IL-1 receptor through PI3K/Akt is essential for
            the induction of iNOS gene expression in hepatocytes
  JOURNAL   J Hepatol 40 (4), 616-623 (2004)
   PUBMED   15030977
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Radons,J., Gabler,S., Wesche,H., Korherr,C., Hofmeister,R. and
            Falk,W.
  TITLE     Identification of essential regions in the cytoplasmic tail of
            interleukin-1 receptor accessory protein critical for interleukin-1
            signaling
  JOURNAL   J Biol Chem 277 (19), 16456-16463 (2002)
   PUBMED   11880380
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Liu,C., Chalmers,D., Maki,R. and De Souza,E.B.
  TITLE     Rat homolog of mouse interleukin-1 receptor accessory protein:
            cloning, localization and modulation studies
  JOURNAL   J Neuroimmunol 66 (1-2), 41-48 (1996)
   PUBMED   8964912
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U48592.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U48592.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132303,
                                           SAMD00132307 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..570
                     /product="interleukin-1 receptor accessory protein
                     precursor"
                     /EC_number="3.2.2.6"
                     /note="IL-1 receptor accessory protein"
                     /calculated_mol_wt=63362
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2255
     mat_peptide     21..570
                     /product="Interleukin-1 receptor accessory protein.
                     /id=PRO_0000015453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63621.1)"
                     /calculated_mol_wt=63362
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63621.1)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          174..178
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          195..199
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     Region          226..229
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63621.1)"
     Region          405..552
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          550..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63621.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPH3; propagated from
                     UniProtKB/Swiss-Prot (Q63621.1)"
     CDS             1..570
                     /gene="Il1rap"
                     /gene_synonym="IL-1RAcp; Il1racpb"
                     /coded_by="NM_012968.1:103..1815"
                     /db_xref="GeneID:25466"
                     /db_xref="RGD:2893"
ORIGIN      
        1 mglpwclmsl ffcgilqsha sercddwgld tmrqiqvfed eparikcplf ehflkynyst
       61 ahssgltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmrlpvhrly ieqgihnitc pnvdgyfpss vkpsvtwykg
      181 cteivnfhnv qpkgmnlsff iplvsnngny tcvvtyleng rlfhltrtmt vkvvgspkda
      241 vpphiyspnd rvvyekepge elvipckvyf sfimdshnei wwtidgkkpd dvpvditiie
      301 svsysstede trtqilsikk vtpedlkrny vcharnaege aeqaakvkqk vipprytvel
      361 acgfgatvfl vvvlivvyhv ywlemvlfyr ahfgtdetil dgkeydiyvs yarnaeeeef
      421 vlltlrgvle nefgyklcif drdsfpggiv tdetlsfiqk srrllvvlsp nyvlqgtqal
      481 lelkaglenm asrgninvil vqykavkdlk vkelkraksv ltvikwkgek skypqgrfwk
      541 qlqvampvkk sprwsssdkq glsysslknv
//
LOCUS       NP_058809                602 aa            linear   ROD 27-APR-2025
DEFINITION  progranulin isoform a precursor [Rattus norvegicus].
ACCESSION   NP_058809
VERSION     NP_058809.2
DBSOURCE    REFSEQ: accession NM_017113.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Liao,A., Zheng,W., Wang,S., Wang,N., Li,Y., Chen,D. and Wang,Y.
  TITLE     Sortilin is associated with progranulin deficiency and autism-like
            behaviors in valproic acid-induced autism rats
  JOURNAL   CNS Neurosci Ther 30 (9), e70015 (2024)
   PUBMED   39218796
  REMARK    GeneRIF: Sortilin is associated with progranulin deficiency and
            autism-like behaviors in valproic acid-induced autism rats.
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Horinokita,I., Hayashi,H., Oteki,R., Mizumura,R., Yamaguchi,T.,
            Usui,A., Yuan,B. and Takagi,N.
  TITLE     Involvement of Progranulin and Granulin Expression in Inflammatory
            Responses after Cerebral Ischemia
  JOURNAL   Int J Mol Sci 20 (20), 5210 (2019)
   PUBMED   31640144
  REMARK    GeneRIF: Study demonstrated that the level of PGRN protein in the
            cerebral cortex was significantly increased after
            microsphere-induced cerebral embolism (ME). Furthermore, PGRN was
            expressed in the microglia of the ipsilateral hemisphere after ME.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Wang,S., Wei,J., Fan,Y., Ding,H., Tian,H., Zhou,X. and Cheng,L.
  TITLE     Progranulin Is Positively Associated with Intervertebral Disc
            Degeneration by Interaction with IL-10 and IL-17 Through TNF
            Pathways
  JOURNAL   Inflammation 41 (5), 1852-1863 (2018)
   PUBMED   29992506
  REMARK    GeneRIF: PGRN is associated with intervertebral disc degeneration
            through interfering with IL-10 and IL-17
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Chen,L., Li,Q., Wang,J., Jin,S., Zheng,H., Lin,J., He,F., Zhang,H.,
            Ma,S., Mei,J. and Yu,J.
  TITLE     MiR-29b-3p promotes chondrocyte apoptosis and facilitates the
            occurrence and development of osteoarthritis by targeting PGRN
  JOURNAL   J Cell Mol Med 21 (12), 3347-3359 (2017)
   PUBMED   28609022
  REMARK    GeneRIF: MiR-29b-3p promotes chondrocyte apoptosis and facilitates
            the occurrence and development of osteoarthritis by targeting PGRN.
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Lee,C.W., Stankowski,J.N., Chew,J., Cook,C.N., Lam,Y.W.,
            Almeida,S., Carlomagno,Y., Lau,K.F., Prudencio,M., Gao,F.B.,
            Bogyo,M., Dickson,D.W. and Petrucelli,L.
  TITLE     The lysosomal protein cathepsin L is a progranulin protease
  JOURNAL   Mol Neurodegener 12 (1), 55 (2017)
   PUBMED   28743268
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Suzuki,M., Bannai,M., Matsumuro,M., Furuhata,Y., Ikemura,R.,
            Kuranaga,E., Kaneda,Y., Nishihara,M. and Takahashi,M.
  TITLE     Suppression of copulatory behavior by intracerebroventricular
            infusion of antisense oligodeoxynucleotide of granulin in neonatal
            male rats
  JOURNAL   Physiol Behav 68 (5), 707-713 (2000)
   PUBMED   10764901
REFERENCE   7  (residues 1 to 602)
  AUTHORS   Bhandari,V., Giaid,A. and Bateman,A.
  TITLE     The complementary deoxyribonucleic acid sequence, tissue
            distribution, and cellular localization of the rat granulin
            precursor
  JOURNAL   Endocrinology 133 (6), 2682-2689 (1993)
   PUBMED   8243292
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Plowman,G.D., Green,J.M., Neubauer,M.G., Buckley,S.D.,
            McDonald,V.L., Todaro,G.J. and Shoyab,M.
  TITLE     The epithelin precursor encodes two proteins with opposing
            activities on epithelial cell growth
  JOURNAL   J Biol Chem 267 (18), 13073-13078 (1992)
   PUBMED   1618805
REFERENCE   9  (residues 1 to 602)
  AUTHORS   Bateman,A., Belcourt,D., Bennett,H., Lazure,C. and Solomon,S.
  TITLE     Granulins, a novel class of peptide from leukocytes
  JOURNAL   Biochem Biophys Res Commun 173 (3), 1161-1168 (1990)
   PUBMED   2268320
REFERENCE   10 (residues 1 to 602)
  AUTHORS   Shoyab,M., McDonald,V.L., Byles,C., Todaro,G.J. and Plowman,G.D.
  TITLE     Epithelins 1 and 2: isolation and characterization of two
            cysteine-rich growth-modulating proteins
  JOURNAL   Proc Natl Acad Sci U S A 87 (20), 7912-7916 (1990)
   PUBMED   2236009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB731349.1, X62322.1, CK365572.1 and BC072469.1.
            
            On Mar 13, 2009 this sequence version replaced NP_058809.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X62322.1, SRR8487226.222781.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..602
                     /product="progranulin isoform a precursor"
                     /note="granulins; acrogranin; progranulin; proepithelin;
                     prostate cancer cell-derived growth factor; epithelin"
                     /calculated_mol_wt=61657
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3517
     Region          79..125
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          140..190
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          222..272
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          296..346
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          388..>421
                     /region_name="Granulin"
                     /note="pfam00396"
                     /db_xref="CDD:459799"
     Region          456..506
                     /region_name="GRAN"
                     /note="Granulin; smart00277"
                     /db_xref="CDD:197621"
     Region          541..582
                     /region_name="Granulin"
                     /note="pfam00396"
                     /db_xref="CDD:459799"
     CDS             1..602
                     /gene="Grn"
                     /gene_synonym="PEPI; PGRN"
                     /coded_by="NM_017113.2:18..1826"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29143"
                     /db_xref="RGD:61983"
ORIGIN      
        1 mpprergprr rqtmwilvsw lalvarlvag tqcpdgqfcp vaccldqgga nysccnplld
       61 twpiitsrrl dgscqirdhc pdgysclltv sgtssccpfs egvscddgqh ccprgfhcsv
      121 dgkscsqisd sllgavqcpg sqfecpdsat ccimidgswg ccpmpqascc edrvhccphg
      181 ascdlvhtrc isptgthpll kkfpaqrtnr avafpfsvvc pdaktqcpdd stccelptgk
      241 ygccpmpnai ccsdhlhccp qdtvcdliqs kciskdyttd lmtklpgypv nevkcdlevs
      301 cpdgytccrl ntgawgccpf tkavccedhi hccpagfqch tetgtcelgv lqvpwmkkvt
      361 aslslpdpqi lkndvpcddf sscpsnntcc rlssgdwgcc pipeavccld hqhccpqgfk
      421 cmdegycqkg drmvaglekm pvrqttllqh gdigcdqhts cpvgqtccps lkgswaccql
      481 phavccedrq hccpagytcn vkartcekda gsvqpsmdlt fgskvgnvec gaghfchdnq
      541 scckdsqggw accpyvkgvc crdgrhccpi gfhcsakgtk clrkktprwd illrdpaprp
      601 ll
//
LOCUS       NP_114000                195 aa            linear   ROD 27-APR-2025
DEFINITION  sialomucin core protein 24 precursor [Rattus norvegicus].
ACCESSION   NP_114000
VERSION     NP_114000.1
DBSOURCE    REFSEQ: accession NM_031812.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Chen,W.L., Huang,A.F., Huang,S.M., Ho,C.L., Chang,Y.L. and
            Chan,J.Y.
  TITLE     CD164 promotes lung tumor-initiating cells with stem cell activity
            and determines tumor growth and drug resistance via Akt/mTOR
            signaling
  JOURNAL   Oncotarget 8 (33), 54115-54135 (2016)
   PUBMED   28903328
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nyegaard,M., Rendtorff,N.D., Nielsen,M.S., Corydon,T.J.,
            Demontis,D., Starnawska,A., Hedemand,A., Buniello,A., Niola,F.,
            Overgaard,M.T., Leal,S.M., Ahmad,W., Wikman,F.P., Petersen,K.B.,
            Cruger,D.G., Oostrik,J., Kremer,H., Tommerup,N., Frodin,M.,
            Steel,K.P., Tranebjaerg,L. and Borglum,A.D.
  TITLE     A Novel Locus Harbouring a Functional CD164 Nonsense Mutation
            Identified in a Large Danish Family with Nonsyndromic Hearing
            Impairment
  JOURNAL   PLoS Genet 11 (7), e1005386 (2015)
   PUBMED   26197441
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Mo,D., Costa,S.A., Ihrke,G., Youker,R.T., Pastor-Soler,N.,
            Hughey,R.P. and Weisz,O.A.
  TITLE     Sialylation of N-linked glycans mediates apical delivery of endolyn
            in MDCK cells via a galectin-9-dependent mechanism
  JOURNAL   Mol Biol Cell 23 (18), 3636-3646 (2012)
   PUBMED   22855528
  REMARK    GeneRIF: Data indicate that galectin-9 plays a role in apical
            sorting of endolyn.
            Erratum:[Mol Biol Cell. 2012 Oct;23(20):4142]
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Potter,B.A., Ihrke,G., Bruns,J.R., Weixel,K.M. and Weisz,O.A.
  TITLE     Specific N-glycans direct apical delivery of transmembrane, but not
            soluble or glycosylphosphatidylinositol-anchored forms of endolyn
            in Madin-Darby canine kidney cells
  JOURNAL   Mol Biol Cell 15 (3), 1407-1416 (2004)
   PUBMED   14699065
  REMARK    GeneRIF: Specific N-glycans are only essential for the apical
            sorting of transmembrane endolyn, suggesting fundamental
            differences in the mechanisms by which soluble,
            glycosylphosphatidylinositol-anchored, and transmembrane proteins
            are sorted.
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Chan,J.Y., Lee-Prudhoe,J.E., Jorgensen,B., Ihrke,G., Doyonnas,R.,
            Zannettino,A.C., Buckle,V.J., Ward,C.J., Simmons,P.J. and Watt,S.M.
  TITLE     Relationship between novel isoforms, functionally important
            domains, and subcellular distribution of CD164/endolyn
  JOURNAL   J Biol Chem 276 (3), 2139-2152 (2001)
   PUBMED   11027692
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Ihrke,G., Gray,S.R. and Luzio,J.P.
  TITLE     Endolyn is a mucin-like type I membrane protein targeted to
            lysosomes by its cytoplasmic tail
  JOURNAL   Biochem J 345 Pt 2 (Pt 2), 287-296 (2000)
   PUBMED   10620506
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Kurosawa,N., Kanemitsu,Y., Matsui,T., Shimada,K., Ishihama,H. and
            Muramatsu,T.
  TITLE     Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164
  JOURNAL   Eur J Biochem 265 (1), 466-472 (1999)
   PUBMED   10491205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ238574.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ238574.1, BC062064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..195
                     /product="sialomucin core protein 24 precursor"
                     /note="CD164 antigen; endolyn; sialomucin core protein 24;
                     MGC-24; MUC-24; multi-glycosylated core protein 24; CD164
                     molecule, sialomucin"
                     /calculated_mol_wt=18223
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2272
     mat_peptide     24..195
                     /product="Sialomucin core protein 24. /id=PRO_5000065184"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX82.1)"
                     /calculated_mol_wt=18223
     Site            26
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Region          27..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Region          57..195
                     /region_name="MGC-24"
                     /note="Multi-glycosylated core protein 24 (MGC-24),
                     sialomucin; pfam05283"
                     /db_xref="CDD:461610"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Region          114..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QX82.1)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX82.1)"
     Region          189..195
                     /region_name="Required for endosomal and lysosomal
                     localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX82.1)"
     CDS             1..195
                     /gene="Cd164"
                     /gene_synonym="MGC-24v"
                     /coded_by="NM_031812.1:15..602"
                     /db_xref="GeneID:83689"
                     /db_xref="RGD:70942"
ORIGIN      
        1 msgasrglfw aatclaalcl saaqsnssas pnvtdppttt skvvpttltt tkppetcesf
       61 nscvscvnat ltnnitcvwl dcheanktyc sselvsnctq ktstdscsvi pttpvptnst
      121 akpttrpssp tptpsvvtsa gatnttvtpt sqperkstfd aasfiggivl vlgvqaviff
      181 lykfcksker nyhtl
//
LOCUS       NP_037142                330 aa            linear   ROD 27-APR-2025
DEFINITION  5'-AMP-activated protein kinase subunit gamma-1 [Rattus
            norvegicus].
ACCESSION   NP_037142
VERSION     NP_037142.1
DBSOURCE    REFSEQ: accession NM_013010.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Bai,W., Guo,T., Wang,H., Li,B., Sun,Q., Wu,W., Zhang,J., Zhou,J.,
            Luo,J., Zhu,M., Lu,J., Li,P., Dong,B., Han,S., Pang,X., Zhang,G.,
            Bai,Y. and Wang,S.
  TITLE     S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming
  JOURNAL   EMBO Rep 25 (1), 128-143 (2024)
   PUBMED   38177907
  REMARK    GeneRIF: S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Jeon,Y.H., He,M., Austin,J., Shin,H., Pfleger,J. and Abdellatif,M.
  TITLE     Adiponectin enhances the bioenergetics of cardiac myocytes via an
            AMPK- and succinate dehydrogenase-dependent mechanism
  JOURNAL   Cell Signal 78, 109866 (2021)
   PUBMED   33271223
  REMARK    GeneRIF: Adiponectin enhances the bioenergetics of cardiac myocytes
            via an AMPK- and succinate dehydrogenase-dependent mechanism.
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Dopie,J., Rajakyla,E.K., Joensuu,M.S., Huet,G., Ferrantelli,E.,
            Xie,T., Jaalinoja,H., Jokitalo,E. and Vartiainen,M.K.
  TITLE     Genome-wide RNAi screen for nuclear actin reveals a network of
            cofilin regulators
  JOURNAL   J Cell Sci 128 (13), 2388-2400 (2015)
   PUBMED   26021350
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Xiao,B., Sanders,M.J., Underwood,E., Heath,R., Mayer,F.V.,
            Carmena,D., Jing,C., Walker,P.A., Eccleston,J.F., Haire,L.F.,
            Saiu,P., Howell,S.A., Aasland,R., Martin,S.R., Carling,D. and
            Gamblin,S.J.
  TITLE     Structure of mammalian AMPK and its regulation by ADP
  JOURNAL   Nature 472 (7342), 230-233 (2011)
   PUBMED   21399626
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Zhu,L., Chen,L., Zhou,X.M., Zhang,Y.Y., Zhang,Y.J., Zhao,J.,
            Ji,S.R., Wu,J.W. and Wu,Y.
  TITLE     Structural insights into the architecture and allostery of
            full-length AMP-activated protein kinase
  JOURNAL   Structure 19 (4), 515-522 (2011)
   PUBMED   21481774
  REMARK    GeneRIF: Studies determine the three-dimensional reconstruction and
            subunit organization of the full-length rat AMPK
            (alpha1beta1gamma1) through single-particle electron
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Cheung,P.C., Salt,I.P., Davies,S.P., Hardie,D.G. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase gamma-subunit
            isoforms and their role in AMP binding
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 659-669 (2000)
   PUBMED   10698692
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Turnley,A.M., Stapleton,D., Mann,R.J., Witters,L.A., Kemp,B.E. and
            Bartlett,P.F.
  TITLE     Cellular distribution and developmental expression of AMP-activated
            protein kinase isoforms in mouse central nervous system
  JOURNAL   J Neurochem 72 (4), 1707-1716 (1999)
   PUBMED   10098881
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Gao,G., Fernandez,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
            Dyck,J.R., Kemp,B.E. and Witters,L.A.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J Biol Chem 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Stapleton,D., Gao,G., Michell,B.J., Widmer,J., Mitchelhill,K.,
            Teh,T., House,C.M., Witters,L.A. and Kemp,B.E.
  TITLE     Mammalian 5'-AMP-activated protein kinase non-catalytic subunits
            are homologs of proteins that interact with yeast Snf1 protein
            kinase
  JOURNAL   J Biol Chem 269 (47), 29343-29346 (1994)
   PUBMED   7961907
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097940.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097940.1, X95578.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..330
                     /product="5'-AMP-activated protein kinase subunit gamma-1"
                     /note="AMP-activated protein kinase, noncatalytic gamma-1
                     subunit; protein kinase, AMP-activated, gamma 1
                     non-catalytic subunit; AMPKg; AMPK gamma-1 chain; AMPK
                     gamma1; AMPK subunit gamma-1; Protein kinase AMP-activated
                     gamma"
                     /calculated_mol_wt=37255
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P80385.3)"
     Region          37..173
                     /region_name="CBS_euAMPK_gamma-like_repeat1"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains found in AMP-activated
                     protein kinase gamma-like proteins, repeat 1; cd04618"
                     /db_xref="CDD:341388"
     Site            order(44,46..48,70..72,151,165,167,169..170,173)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341388"
     Region          44..117
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Site            order(70,84,88..89,92,129,151..153,169)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341388"
     Region          129..173
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Region          137..158
                     /region_name="AMPK pseudosubstrate"
                     /note="propagated from UniProtKB/Swiss-Prot (P80385.3)"
     Region          199..322
                     /region_name="CBS_euAMPK_gamma-like_repeat2"
                     /note="CBS pair domain found in 5'-AMP (adenosine
                     monophosphate)-activated protein kinase; cd04641"
                     /db_xref="CDD:341399"
     Site            order(200,202..204,226..228,298,311,313,315..316,319)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341399"
     Region          200..265
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     Site            order(226,239,243..244,247,276,298..300,315)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341399"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000305|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ULK1.
                     /evidence=ECO:0000305|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:21460634; propagated from
                     UniProtKB/Swiss-Prot (P80385.3)"
     Region          276..319
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     CDS             1..330
                     /gene="Prkag1"
                     /gene_synonym="Prkaac; Prkga1"
                     /coded_by="NM_013010.2:17..1009"
                     /db_xref="GeneID:25520"
                     /db_xref="RGD:3388"
ORIGIN      
        1 mesvaaesap apenehsqet pesnssvytt fmkshrcydl iptssklvvf dtslqvkkaf
       61 falvtngvra aplwdskkqs fvgmltitdf inilhryyks alvqiyelee hkietwrevy
      121 lqdsfkplvc ispnaslfda vsslirnkih rlpvidpesg ntlyilthkr ilkflklfit
      181 efpkpefmsk sleelqigty aniamvrttt pvyvalgifv qhrvsalpvv dekgrvvdiy
      241 skfdvinlaa ektynnldvs vtkalqhrsh yfegvlkcyl hetleaiinr lveaevhrlv
      301 vvdehdvvkg ivslsdilqa lvltggekkp
//
LOCUS       NP_001099182             879 aa            linear   ROD 27-APR-2025
DEFINITION  metabotropic glutamate receptor 3 precursor [Rattus norvegicus].
ACCESSION   NP_001099182 XP_001062001 XP_001069653
VERSION     NP_001099182.1
DBSOURCE    REFSEQ: accession NM_001105712.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Joffe,M.E., Santiago,C.I., Oliver,K.H., Maksymetz,J., Harris,N.A.,
            Engers,J.L., Lindsley,C.W., Winder,D.G. and Conn,P.J.
  TITLE     mGlu2 and mGlu3 Negative Allosteric Modulators Divergently Enhance
            Thalamocortical Transmission and Exert Rapid Antidepressant-like
            Effects
  JOURNAL   Neuron 105 (1), 46-59 (2020)
   PUBMED   31735403
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Alese,O.O. and Mabandla,M.V.
  TITLE     Transgenerational deep sequencing revealed hypermethylation of
            hippocampal mGluR1 gene with altered mRNA expression of mGluR5 and
            mGluR3 associated with behavioral changes in Sprague Dawley rats
            with history of prolonged febrile seizure
  JOURNAL   PLoS One 14 (11), e0225034 (2019)
   PUBMED   31710636
  REMARK    GeneRIF: significant decrease in mGluR5 mRNA expression with a
            resultant increased expression of mGluR3 mRNA expression and
            hypermethylation of mGluR1 gene across both generations of rats, is
            reported.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Wong,A.M., Scott,A.K., Johnson,C.S., Mohr,M.A., Mittelman-Smith,M.
            and Micevych,P.E.
  TITLE     ERalphaDelta4, an ERalpha splice variant missing exon4, interacts
            with caveolin-3 and mGluR2/3
  JOURNAL   J Neuroendocrinol 31 (6), e12725 (2019)
   PUBMED   31050077
  REMARK    GeneRIF: ERalphaDelta4, an ERalpha splice variant missing exon4,
            interacts with caveolin-3 and mGluR2/3.
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Wood,C.M., Wafford,K.A., McCarthy,A.P., Hewes,N., Shanks,E.,
            Lodge,D. and Robinson,E.S.J.
  TITLE     Investigating the role of mGluR2 versus mGluR3 in
            antipsychotic-like effects, sleep-wake architecture and network
            oscillatory activity using novel Han Wistar rats lacking mGluR2
            expression
  JOURNAL   Neuropharmacology 140, 246-259 (2018)
   PUBMED   30005976
  REMARK    GeneRIF: studies illustrate the significant contribution of mGluR2
            to the antipsychotic-like, sleep and EEG effects of drugs acting on
            group II mGluRs; however, we also provide evidence of a role for
            mGluR3 activity in the control of sleep and wake cortical theta and
            gamma oscillations
REFERENCE   5  (residues 1 to 879)
  AUTHORS   Nasca,C., Bigio,B., Zelli,D., de Angelis,P., Lau,T., Okamoto,M.,
            Soya,H., Ni,J., Brichta,L., Greengard,P., Neve,R.L., Lee,F.S. and
            McEwen,B.S.
  TITLE     Role of the Astroglial Glutamate Exchanger xCT in Ventral
            Hippocampus in Resilience to Stress
  JOURNAL   Neuron 96 (2), 402-413 (2017)
   PUBMED   29024663
REFERENCE   6  (residues 1 to 879)
  AUTHORS   Tamaru,Y., Nomura,S., Mizuno,N. and Shigemoto,R.
  TITLE     Distribution of metabotropic glutamate receptor mGluR3 in the mouse
            CNS: differential location relative to pre- and postsynaptic sites
  JOURNAL   Neuroscience 106 (3), 481-503 (2001)
   PUBMED   11591452
REFERENCE   7  (residues 1 to 879)
  AUTHORS   Chavis,P., Shinozaki,H., Bockaert,J. and Fagni,L.
  TITLE     The metabotropic glutamate receptor types 2/3 inhibit L-type
            calcium channels via a pertussis toxin-sensitive G-protein in
            cultured cerebellar granule cells
  JOURNAL   J Neurosci 14 (11 Pt 2), 7067-7076 (1994)
   PUBMED   7965099
REFERENCE   8  (residues 1 to 879)
  AUTHORS   Guidi,B., Ronchi,S., Ori,E., Varni,P.F., Cassinadri,T., Tripodi,A.,
            Borghi,A., Mattei,F., Demaria,F., Galavotti,E. et al.
  TITLE     [Lead concentrations in breast milk of women living in urban areas
            compared with women living in rural areas]
  JOURNAL   Pediatr Med Chir 14 (6), 611-616 (1992)
   PUBMED   1298935
REFERENCE   9  (residues 1 to 879)
  AUTHORS   Tanabe,Y., Masu,M., Ishii,T., Shigemoto,R. and Nakanishi,S.
  TITLE     A family of metabotropic glutamate receptors
  JOURNAL   Neuron 8 (1), 169-179 (1992)
   PUBMED   1309649
REFERENCE   10 (residues 1 to 879)
  AUTHORS   Lipovskii,S.M.
  TITLE     [Levels of histamine in the tissues of the stomach and liver of
            non-pregnant and pregnant guinea pigs, their fetuses, in the blood
            of pregnant females and in fetal fluids]
  JOURNAL   Fiziol Zh SSSR Im I M Sechenova 61 (1), 90-95 (1975)
   PUBMED   1109982
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474013.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001062001.1, XP_001069653.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: M92076.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760393, SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..879
                     /product="metabotropic glutamate receptor 3 precursor"
                     /note="metabotropic glutamate receptor 3; glutamate
                     receptor, metabotropic 3"
                     /calculated_mol_wt=96424
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2555
     mat_peptide     23..879
                     /product="Metabotropic glutamate receptor 3.
                     /id=PRO_0000012929"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
                     /calculated_mol_wt=96424
     Region          33..494
                     /region_name="PBP1_mGluR_groupII"
                     /note="ligand binding domain of the group II metabotropic
                     glutamate receptor; cd06375"
                     /db_xref="CDD:380598"
     Site            order(64,68,150..151,172..174,222,301,389)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380598"
     Site            order(103,106,156,159,182,246)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380598"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17360426; propagated from
                     UniProtKB/Swiss-Prot (P31422.1)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31422.1)"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31422.1)"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P31422.1)"
     Region          505..555
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          575..828
                     /region_name="7tmC_mGluR3"
                     /note="metabotropic glutamate receptor 3 in group 2,
                     member of the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15448"
                     /db_xref="CDD:320564"
     Region          575..600
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320564"
     Site            577..599
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Site            order(578,581..582,585..586,588..589,623,627,630..631,639,
                     643)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320564"
     Region          612..633
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320564"
     Site            614..634
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Site            order(632,644..645,648..649,652,732,737,740..741,744,778,
                     781..782,785,789,799..800,803,806,810)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320564"
     Region          642..666
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320564"
     Site            646..664
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Region          688..708
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320564"
     Site            689..709
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Region          733..759
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320564"
     Site            735..756
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Region          767..790
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320564"
     Site            770..792
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     Region          797..822
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320564"
     Site            803..828
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31422.1)"
     CDS             1..879
                     /gene="Grm3"
                     /gene_synonym="mGluR3"
                     /coded_by="NM_001105712.1:224..2863"
                     /db_xref="GeneID:24416"
                     /db_xref="RGD:2744"
ORIGIN      
        1 mkmltrlqil mlalfskgfl lslgdhnfmr reikiegdlv lgglfpinek gtgteecgri
       61 nedrgiqrle amlfaidein kdnyllpgvk lgvhildtcs rdtyaleqsl efvrasltkv
      121 deaeymcpdg syaiqenipl liagviggsy ssvsiqvanl lrlfqipqis yastsaklsd
      181 ksrydyfart vppdfyqaka maeilrffnw tyvstvaseg dygetgieaf eqearlrnic
      241 iataekvgrs nirksydsvi rellqkpnar vvvlfmrsdd sreliaaanr vnasftwvas
      301 dgwgaqesiv kgsehvayga itlelashpv rqfdryfqsl npynnhrnpw frdfweqkfq
      361 cslqnkrnhr qvcdkhlaid ssnyeqeski mfvvnavyam ahalhkmqrt lcpnttklcd
      421 amkildgkkl ykeyllkinf tapfnpnkga dsivkfdtfg dgmgrynvfn lqqtggkysy
      481 lkvghwaetl sldvdsihws rnsvptsqcs dpcapnemkn mqpgdvccwi cipcepyeyl
      541 vdeftcmdcg pgqwptadls gcynlpedyi kwedawaigp vtiaclgflc tcivitvfik
      601 hnntplvkas grelcyillf gvslsycmtf ffiakpspvi calrrlglgt sfaicysall
      661 tktnciarif dgvkngaqrp kfispssqvf iclglilvqi vmvsvwlile tpgtrrytlp
      721 ekretvilkc nvkdssmlis ltydvvlvil ctvyafktrk cpenfneakf igftmyttci
      781 iwlaflpify vtssdyrvqt ttmcisvsls gfvvlgclfa pkvhivlfqp qknvvthrlh
      841 lnrfsvsgta ttysqssast yvptvcngre vldsttssl
//
LOCUS       NP_446368                835 aa            linear   ROD 27-APR-2025
DEFINITION  transcription intermediary factor 1-beta [Rattus norvegicus].
ACCESSION   NP_446368 XP_001062234 XP_344862
VERSION     NP_446368.1
DBSOURCE    REFSEQ: accession NM_053916.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Wang,W., Yan,T., Guo,X., Cai,H., Liang,C., Huang,L., Wang,Y., Ma,P.
            and Qi,S.
  TITLE     KAP1 phosphorylation promotes the survival of neural stem cells
            after ischemia/reperfusion by maintaining the stability of PCNA
  JOURNAL   Stem Cell Res Ther 13 (1), 290 (2022)
   PUBMED   35799276
  REMARK    GeneRIF: KAP1 phosphorylation promotes the survival of neural stem
            cells after ischemia/reperfusion by maintaining the stability of
            PCNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Valle-Garcia,D., Qadeer,Z.A., McHugh,D.S., Ghiraldini,F.G.,
            Chowdhury,A.H., Hasson,D., Dyer,M.A., Recillas-Targa,F. and
            Bernstein,E.
  TITLE     ATRX binds to atypical chromatin domains at the 3' exons of zinc
            finger genes to preserve H3K9me3 enrichment
  JOURNAL   Epigenetics 11 (6), 398-414 (2016)
   PUBMED   27029610
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Serra,R.W., Fang,M., Park,S.M., Hutchinson,L. and Green,M.R.
  TITLE     A KRAS-directed transcriptional silencing pathway that mediates the
            CpG island methylator phenotype
  JOURNAL   Elife 3, e02313 (2014)
   PUBMED   24623306
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Wang,W., Cai,J., Wu,Y., Hu,L., Chen,Z., Hu,J., Chen,Z., Li,W.,
            Guo,M. and Huang,Z.
  TITLE     Novel activity of KRAB domain that functions to reinforce nuclear
            localization of KRAB-containing zinc finger proteins by interacting
            with KAP1
  JOURNAL   Cell Mol Life Sci 70 (20), 3947-3958 (2013)
   PUBMED   23665872
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Krebs,C.J., Schultz,D.C. and Robins,D.M.
  TITLE     The KRAB zinc finger protein RSL1 regulates sex- and
            tissue-specific promoter methylation and dynamic hormone-responsive
            chromatin configuration
  JOURNAL   Mol Cell Biol 32 (18), 3732-3742 (2012)
   PUBMED   22801370
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Nielsen,A.L., Ortiz,J.A., You,J., Oulad-Abdelghani,M.,
            Khechumian,R., Gansmuller,A., Chambon,P. and Losson,R.
  TITLE     Interaction with members of the heterochromatin protein 1 (HP1)
            family and histone deacetylation are differentially involved in
            transcriptional silencing by members of the TIF1 family
  JOURNAL   EMBO J 18 (22), 6385-6395 (1999)
   PUBMED   10562550
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Huang,Z., Philippin,B., O'Leary,E., Bonventre,J.V., Kriz,W. and
            Witzgall,R.
  TITLE     Expression of the transcriptional repressor protein Kid-1 leads to
            the disintegration of the nucleolus
  JOURNAL   J Biol Chem 274 (12), 7640-7648 (1999)
   PUBMED   10075651
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Kim,S.S., Chen,Y.M., O'Leary,E., Witzgall,R., Vidal,M. and
            Bonventre,J.V.
  TITLE     A novel member of the RING finger family, KRIP-1, associates with
            the KRAB-A transcriptional repressor domain of zinc finger proteins
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15299-15304 (1996)
   PUBMED   8986806
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Moosmann,P., Georgiev,O., Le Douarin,B., Bourquin,J.P. and
            Schaffner,W.
  TITLE     Transcriptional repression by RING finger protein TIF1 beta that
            interacts with the KRAB repressor domain of KOX1
  JOURNAL   Nucleic Acids Res 24 (24), 4859-4867 (1996)
   PUBMED   9016654
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Friedman,J.R., Fredericks,W.J., Jensen,D.E., Speicher,D.W.,
            Huang,X.P., Neilson,E.G. and Rauscher,F.J. 3rd.
  TITLE     KAP-1, a novel corepressor for the highly conserved KRAB repression
            domain
  JOURNAL   Genes Dev 10 (16), 2067-2078 (1996)
   PUBMED   8769649
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC166843.1.
            
            On or before Oct 23, 2008 this sequence version replaced
            XP_344862.3, XP_001062234.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..835
                     /product="transcription intermediary factor 1-beta"
                     /EC_number="2.3.2.27"
                     /note="TIF1-beta; KRAB-associated protein 1; nuclear
                     corepressor KAP-1; tripartite motif-containing protein 28;
                     E3 SUMO-protein ligase TRIM28; tripartite motif protein
                     28; RING-type E3 ubiquitin transferase TIF1-beta"
                     /calculated_mol_wt=88825
     Region          14..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          64..126
                     /region_name="RING-HC_TIF1beta"
                     /note="RING finger, HC subclass, found in transcription
                     inknown asiary factor 1-beta (TIF1-beta); cd16765"
                     /db_xref="CDD:438421"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          150..201
                     /region_name="Bbox1_TIF1b_C-VI"
                     /note="B-box-type 1 zinc finger found in transcription
                     intermediary factor 1-beta (TIF1-beta); cd19846"
                     /db_xref="CDD:380904"
     Region          208..251
                     /region_name="Bbox2_TIF1b_C-VI"
                     /note="B-box-type 2 zinc finger found in transcription
                     intermediary factor 1-beta (TIF1-beta); cd19829"
                     /db_xref="CDD:380887"
     Region          248..378
                     /region_name="Leucine zipper alpha helical coiled-coil
                     region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Region          249..378
                     /region_name="Interaction with MAGEC2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Region          254..380
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Site            268
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q62318; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            306
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            342
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          368..372
                     /region_name="Involved in binding PPP1CA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Site            379
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          413..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62318; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          477..514
                     /region_name="HP1 box"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          482..495
                     /region_name="PxVxL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O08629.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          628..670
                     /region_name="PHD_TIF1beta"
                     /note="PHD finger found in transcription intermediary
                     factor 1-beta (TIF1-beta); cd15623"
                     /db_xref="CDD:277093"
     Site            order(628,633..634,637..642,649,662..663)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277093"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Region          697..803
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            order(725,728,731,773,777,783)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99934"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62318; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            771
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            775
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q62318; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR and dsDNA kinase.
                     /evidence=ECO:0000250|UniProtKB:Q13263; propagated from
                     UniProtKB/Swiss-Prot (O08629.2)"
     CDS             1..835
                     /gene="Trim28"
                     /gene_synonym="Kap1; Krip1; Tif1b"
                     /coded_by="NM_053916.1:284..2791"
                     /db_xref="GeneID:116698"
                     /db_xref="RGD:620289"
ORIGIN      
        1 maasaaaata aasaataasa asgspgsgeg saggekrpaa ssaaaasasa sspaggggea
       61 qellehcgvc rerlrperdp rllpclhsac saclgpatpa aannsgdggs agdgamvdcp
      121 vckqqcyskd ivenyfmrds gskassdsqd anqcctsced napatsycve cseplcetcv
      181 eahqrvkytk dhtvrstgpa ktrdgertvy cnvhkheplv lfcescdtlt crdcqlnahk
      241 dhqyqfleda vrnqrkllas lvkrlgdkha tlqkntkevr ssirqvsdvq krvqvdvkma
      301 ilqimkelnk rgrvlvndaq kvtegqqerl erqhwtmtki qkhqehilrf aswalesdnn
      361 talllskkli yfqlhralkm ivdpvephge mkfqwdlnaw tksaeafgki vaerpgtnst
      421 gpgpmappra pgplskqgsg ssqpmevqeg ygfgtddpys saephvsgmk rsrsgegevs
      481 glmrkvprvs lerldldlts dsqppvfkvf pgsttedynl iviergaaaa aagqagtvpp
      541 gapgapplpg maivkeeete aaigappaap egpetkpvlm altegpgaeg prlaspsgst
      601 ssglevvape vtsapvsgpg ilddsaticr vcqkpgdlvm cnqcefcfhl dchlpslqdv
      661 pgeewscslc hvlpdlkeed gslsldgads tgvvaklspa nqrkcervll alfchepcrp
      721 lhqlatdstf smeqpggtld ltlirarlqe klsppysspq efaqdvgrmf kqfnkltedk
      781 advqsiiglq rffetrmnda fgdtkfsavl veppplnlps aglssqelsg pgdgp
//
LOCUS       NP_001013983             376 aa            linear   ROD 27-APR-2025
DEFINITION  actin-related protein T1 [Rattus norvegicus].
ACCESSION   NP_001013983 XP_229114
VERSION     NP_001013983.1
DBSOURCE    REFSEQ: accession NM_001013961.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Bal,E., Park,H.S., Belaid-Choucair,Z., Kayserili,H., Naville,M.,
            Madrange,M., Chiticariu,E., Hadj-Rabia,S., Cagnard,N., Kuonen,F.,
            Bachmann,D., Huber,M., Le Gall,C., Cote,F., Hanein,S., Rosti,R.O.,
            Aslanger,A.D., Waisfisz,Q., Bodemer,C., Hermine,O.,
            Morice-Picard,F., Labeille,B., Caux,F., Mazereeuw-Hautier,J.,
            Philip,N., Levy,N., Taieb,A., Avril,M.F., Headon,D.J., Gyapay,G.,
            Magnaldo,T., Fraitag,S., Crollius,H.R., Vabres,P., Hohl,D.,
            Munnich,A. and Smahi,A.
  TITLE     Mutations in ACTRT1 and its enhancer RNA elements lead to aberrant
            activation of Hedgehog signaling in inherited and sporadic basal
            cell carcinomas
  JOURNAL   Nat Med 23 (10), 1226-1233 (2017)
   PUBMED   28869610
  REMARK    Erratum:[Nat Med. 2025 Apr;31(4):1364. doi:
            10.1038/s41591-025-03531-y. PMID: 39915680]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083679.1.
            
            On Apr 20, 2005 this sequence version replaced XP_229114.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC083679.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq35"
     Protein         1..376
                     /product="actin-related protein T1"
                     /calculated_mol_wt=42064
     Region          10..367
                     /region_name="ASKHA_NBD_actin_Arp-T1-3"
                     /note="nucleotide-binding domain (NBD) of actin,
                     actin-related proteins T1-T3 (Arp-T1-3), and similar
                     proteins; cd13397"
                     /db_xref="CDD:466848"
     CDS             1..376
                     /gene="Actrt1"
                     /coded_by="NM_001013961.1:118..1248"
                     /db_xref="GeneID:302796"
                     /db_xref="RGD:1359559"
ORIGIN      
        1 mlntarldnp avifdngsgl ckvgisgeiv prhvinsvvg hpkfnipsar snrkryfvge
       61 eaqcmydgly lhypierglv trwddmeklw kdlfewelgv kpneqpvfmt epslnpretr
      121 ektteimfek fnvpalylcn havgalcasa citglvldsg dgvtctvpiy egyslprait
      181 klyvagrdit ehltrlllak gytfpcilnk avvddikekl ctvswgskds ekcyqrslse
      241 yklpdgntiq msdhlcqvpe vlftpehlgi hdlgiskmvc nsimkcdtdi qenlfaeivl
      301 sggttlfpgl qdrllkelev lafegtpiki taspdrcysa wiggsvmtsl ttfkqmwvta
      361 edfkeygafv vqrkcf
//
LOCUS       NP_001017461            1023 aa            linear   ROD 27-APR-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001017461 XP_573650
VERSION     NP_001017461.1
DBSOURCE    REFSEQ: accession NM_001017461.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Artiukhov,A.V., Grabarska,A., Gumbarewicz,E., Aleshin,V.A.,
            Kahne,T., Obata,T., Kazantsev,A.V., Lukashev,N.V., Stepulak,A.,
            Fernie,A.R. and Bunik,V.I.
  TITLE     Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues
  JOURNAL   Sci Rep 10 (1), 1886 (2020)
   PUBMED   32024885
  REMARK    GeneRIF: Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Wang,Y., Guo,Y.R., Liu,K., Yin,Z., Liu,R., Xia,Y., Tan,L., Yang,P.,
            Lee,J.H., Li,X.J., Hawke,D., Zheng,Y., Qian,X., Lyu,J., He,J.,
            Xing,D., Tao,Y.J. and Lu,Z.
  TITLE     KAT2A coupled with the alpha-KGDH complex acts as a histone H3
            succinyltransferase
  JOURNAL   Nature 552 (7684), 273-277 (2017)
   PUBMED   29211711
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Tsepkova,P.M., Artiukhov,A.V., Boyko,A.I., Aleshin,V.A.,
            Mkrtchyan,G.V., Zvyagintseva,M.A., Ryabov,S.I., Ksenofontov,A.L.,
            Baratova,L.A., Graf,A.V. and Bunik,V.I.
  TITLE     Thiamine Induces Long-Term Changes in Amino Acid Profiles and
            Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in Rat
            Brain
  JOURNAL   Biochemistry (Mosc) 82 (6), 723-736 (2017)
   PUBMED   28601082
  REMARK    GeneRIF: Thiamine Induces Long-Term Changes in Amino Acid Profiles
            and Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in
            Rat Brain
REFERENCE   4  (residues 1 to 1023)
  AUTHORS   Denton,R.M., Pullen,T.J., Armstrong,C.T., Heesom,K.J. and
            Rutter,G.A.
  TITLE     Calcium-insensitive splice variants of mammalian E1 subunit of
            2-oxoglutarate dehydrogenase complex with tissue-specific patterns
            of expression
  JOURNAL   Biochem J 473 (9), 1165-1178 (2016)
   PUBMED   26936970
  REMARK    GeneRIF: Tissue-specific expression of OGDH splice variants may
            thus provide a mechanism that tunes the control of the enzyme to
            the specialized metabolic and signalling needs of individual cell
            types
REFERENCE   5  (residues 1 to 1023)
  AUTHORS   Quinlan,C.L., Goncalves,R.L., Hey-Mogensen,M., Yadava,N.,
            Bunik,V.I. and Brand,M.D.
  TITLE     The 2-oxoacid dehydrogenase complexes in mitochondria can produce
            superoxide/hydrogen peroxide at much higher rates than complex I
  JOURNAL   J Biol Chem 289 (12), 8312-8325 (2014)
   PUBMED   24515115
  REMARK    GeneRIF: H2O2 production from Ogdh can be considerable but may
            previously have been misattributed to complex I.
REFERENCE   6  (residues 1 to 1023)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 1023)
  AUTHORS   Sheu,K.F. and Blass,J.P.
  TITLE     The alpha-ketoglutarate dehydrogenase complex
  JOURNAL   Ann N Y Acad Sci 893, 61-78 (1999)
   PUBMED   10672230
  REMARK    Review article
REFERENCE   8  (residues 1 to 1023)
  AUTHORS   Bruschi,S.A., Lindsay,J.G. and Crabb,J.W.
  TITLE     Mitochondrial stress protein recognition of inactivated
            dehydrogenases during mammalian cell death
  JOURNAL   Proc Natl Acad Sci U S A 95 (23), 13413-13418 (1998)
   PUBMED   9811814
REFERENCE   9  (residues 1 to 1023)
  AUTHORS   Andersson,U., Leighton,B., Young,M.E., Blomstrand,E. and
            Newsholme,E.A.
  TITLE     Inactivation of aconitase and oxoglutarate dehydrogenase in
            skeletal muscle in vitro by superoxide anions and/or nitric oxide
  JOURNAL   Biochem Biophys Res Commun 249 (2), 512-516 (1998)
   PUBMED   9712727
REFERENCE   10 (residues 1 to 1023)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083811.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573650.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083811.1, FQ222842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 precursor"
                     /EC_number="1.2.4.2"
                     /note="2-oxoglutarate dehydrogenase E1 component,
                     mitochondrial; 2-oxoglutarate dehydrogenase,
                     mitochondrial; alpha-ketoglutarate dehydrogenase; OGDC-E1;
                     2-oxoglutarate dehydrogenase complex component E1;
                     2-oxoglutarate dehydrogenase, mitochondrial-like;
                     oxoglutarate dehydrogenase (lipoamide); oxoglutarate
                     (alpha-ketoglutarate) dehydrogenase (lipoamide);
                     alpha-KGDH-E1; thiamine diphosphate (ThDP)-dependent
                     2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=111687
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5XI78.1)"
                     /calculated_mol_wt=4627
     mat_peptide     41..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1. /id=PRO_0000271367"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI78.1)"
                     /calculated_mol_wt=111687
     Region          49..1016
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     Site            970
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02218; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     CDS             1..1023
                     /gene="Ogdh"
                     /gene_synonym="E1o; OGDH-E1"
                     /coded_by="NM_001017461.1:79..3150"
                     /db_xref="GeneID:360975"
                     /db_xref="RGD:1561359"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnkpaa irtfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplsls rsslatmaha qslveaqpnv
      121 dklvedhlav qslirayqir ghhvaqldpl gildadldss vpadiisstd klgfyglhes
      181 dldkvfhlpt ttfiggqepa lplreiirrl emaycqhigv efmfindleq cqwirqkfet
      241 pgimqftnee krtllarlvr strfeeflqr kwssekrfgl egcevlipal ktiidmssan
      301 gvdyvimgmp hrgrlnvlan virkeleqif cqfdskleaa degsgdmkyh lgmyhrrinr
      361 vtdrnitlsl vanpshleaa dpvvmgktka eqfycgdteg kkvmsillhg daafagqgiv
      421 yetfhlsdlp sytthgtvhv vvnnqigftt dprmarsspy ptdvarvvna pifhvnsddp
      481 eavmyvckva aewrntfhkd vvvdlvcyrr nghnemdepm ftqplmykqi rkqkpvlqky
      541 aellvsqgvv nqpeyeeeis kydkiceeaf trskdekilh ikhwldspwp gfftldgqpr
      601 smtcpstgle edilthignv assvpvenft ihgglsrilk trrelvtnrt vdwalaeyma
      661 fgsllkegih vrlsgqdver gtfshrhhvl hdqnvdkrtc ipmnhlwpnq apytvcnssl
      721 seygvlgfel gfamaspnal vlweaqfgdf nnmaqciidq ficpgqakwv rqngivlllp
      781 hgmegmgpeh ssarperflq mcnddpdvlp nlqeenfdis qlydcnwivv ncstpgnffh
      841 vlrrqillpf rkplivftpk sllrhpeart sfdemlpgth fqrvipedgp aaqnpdkvkr
      901 llfctgkvyy dltrerkard maeevaitri eqlspfpfdl llkeaqkypn aelawcqeeh
      961 knqgyydyvk prlrttidra kpvwyagrdp aaapatgnkk thltelqrfl dtafdldafk
     1021 kfs
//
LOCUS       NP_001095151             824 aa            linear   ROD 27-APR-2025
DEFINITION  AMP deaminase 2 [Rattus norvegicus].
ACCESSION   NP_001095151 XP_001069998 XP_342314
VERSION     NP_001095151.1
DBSOURCE    REFSEQ: accession NM_001101681.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Helmering,J., Juan,T., Li,C.M., Chhoa,M., Baron,W., Gyuris,T.,
            Richards,W.G., Turk,J.R., Lawrence,J., Cosgrove,P.A., Busby,J.,
            Kim,K.W., Kaufman,S.A., Cummings,C., Carlson,G., Veniant,M.M. and
            Lloyd,D.J.
  TITLE     A mutation in Ampd2 is associated with nephrotic syndrome and
            hypercholesterolemia in mice
  JOURNAL   Lipids Health Dis 13, 167 (2014)
   PUBMED   25361754
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Akizu,N., Cantagrel,V., Schroth,J., Cai,N., Vaux,K., McCloskey,D.,
            Naviaux,R.K., Van Vleet,J., Fenstermaker,A.G., Silhavy,J.L.,
            Scheliga,J.S., Toyama,K., Morisaki,H., Sonmez,F.M., Celep,F.,
            Oraby,A., Zaki,M.S., Al-Baradie,R., Faqeih,E.A., Saleh,M.A.,
            Spencer,E., Rosti,R.O., Scott,E., Nickerson,E., Gabriel,S.,
            Morisaki,T., Holmes,E.W. and Gleeson,J.G.
  TITLE     AMPD2 regulates GTP synthesis and is mutated in a potentially
            treatable neurodegenerative brainstem disorder
  JOURNAL   Cell 154 (3), 505-517 (2013)
   PUBMED   23911318
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Toyama,K., Morisaki,H., Cheng,J., Kawachi,H., Shimizu,F., Ikawa,M.,
            Okabe,M. and Morisaki,T.
  TITLE     Proteinuria in AMPD2-deficient mice
  JOURNAL   Genes Cells 17 (1), 28-38 (2012)
   PUBMED   22212473
  REMARK    Erratum:[Genes Cells. 2014 Jun;19(6):540]
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Juan,T., Veniant,M.M., Helmering,J., Babij,P., Baker,D.M.,
            Damore,M.A., Bass,M.B., Gyuris,T., Chhoa,M., Li,C.M., Ebeling,C.,
            Amato,J., Carlson,G.A. and Lloyd,D.J.
  TITLE     Identification of three loci affecting HDL-cholesterol levels in a
            screen for chemically induced recessive mutations in mice
  JOURNAL   J Lipid Res 50 (3), 534-545 (2009)
   PUBMED   18974039
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Mahnke-Zizelman,D.K., Tullson,P.C. and Sabina,R.L.
  TITLE     Novel aspects of tetramer assembly and N-terminal domain structure
            and function are revealed by recombinant expression of human AMP
            deaminase isoforms
  JOURNAL   J Biol Chem 273 (52), 35118-35125 (1998)
   PUBMED   9857047
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Mahnke-Zizelman,D.K., D'cunha,J., Wojnar,J.M., Brogley,M.A. and
            Sabina,R.L.
  TITLE     Regulation of rat AMP deaminase 3 (isoform C) by development and
            skeletal muscle fibre type
  JOURNAL   Biochem J 326 (Pt 2) (Pt 2), 521-529 (1997)
   PUBMED   9291127
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Morisaki,T., Sabina,R.L. and Holmes,E.W.
  TITLE     Adenylate deaminase. A multigene family in humans and rats
  JOURNAL   J Biol Chem 265 (20), 11482-11486 (1990)
   PUBMED   2365682
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166402.1.
            
            On or before Aug 19, 2007 this sequence version replaced
            XP_342314.2, XP_001069998.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166402.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..824
                     /product="AMP deaminase 2"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L)"
                     /calculated_mol_wt=94656
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02356.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            44
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01433; propagated from
                     UniProtKB/Swiss-Prot (Q02356.2)"
     Region          163..806
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..824
                     /gene="Ampd2"
                     /gene_synonym="Ampd"
                     /coded_by="NM_001101681.2:49..2523"
                     /db_xref="GeneID:362015"
                     /db_xref="RGD:2110"
ORIGIN      
        1 masypgpgks kakypfkkra slqasaaape arsglgaspl qsarslpgta pclkhfpldl
       61 rtsmdgkcke iaeelfsrsl aeselrsapy efpeespieq leerrqrler qisqdvklep
      121 dillrakqdf lktdsdsdlq lykeqgegqg drglwerdvv lerefqrvii sgeekcgvpf
      181 tdlldaaksv vralfireky malslqsfcp ttrrylqqla ekpletrtye qspdtpvsad
      241 apvhppaleq hpyehcepst mpgdlglglr mvrgvvhvyt rrdpdehcpe velpypdlqe
      301 fvadvnvlma liingpiksf cyrrlqylss kfqmhvllne mkelaaqkkv phrdfynirk
      361 vdthihassc mnqkhllrfi kramkrhlee ivhveqgreq tlrevfesmn ltaydlsvdt
      421 ldvhadrntf hrfdkfnaky npigesvlre ifiktdnkis gkyfahiike vmsdleesky
      481 qnaelrlsiy grsrdewdkl arwavnhrvh spnvrwlvqv prlfdvyrtk gqlanfqeml
      541 eniflplfea tvhpashpel hlflehvdgf dsvddeskpe nhvfnlespl peawveednp
      601 pyayylyytf anmamlnhlr rqrgfhtfvl rphcgeagpi hhlvsafmla enishglllr
      661 kapvlqylyy laqigiamsp lsnnslflsy hrnplpeyls rglmvslstd dplqfhftke
      721 plmeeysiat qvwklsscdm celarnsvlm sgfshkvksh wlgpnytkeg pegndirrtn
      781 vpdirvgyry etlcqelali tqavqsemle tipeevgivm spgp
//
LOCUS       NP_058890                494 aa            linear   ROD 27-APR-2025
DEFINITION  acetylcholine receptor subunit epsilon precursor [Rattus
            norvegicus].
ACCESSION   NP_058890
VERSION     NP_058890.1
DBSOURCE    REFSEQ: accession NM_017194.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Witzemann,V., Chevessier,F., Pacifici,P.G. and Yampolsky,P.
  TITLE     The neuromuscular junction: selective remodeling of synaptic
            regulators at the nerve/muscle interface
  JOURNAL   Mech Dev 130 (6-8), 402-411 (2013)
   PUBMED   23032192
  REMARK    Review article
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Rasoulpour,R.J., Ellis-Hutchings,R.G., Terry,C., Millar,N.S.,
            Zablotny,C.L., Gibb,A., Marshall,V., Collins,T., Carney,E.W. and
            Billington,R.
  TITLE     A novel mode-of-action mediated by the fetal muscle nicotinic
            acetylcholine receptor resulting in developmental toxicity in rats
  JOURNAL   Toxicol Sci 127 (2), 522-534 (2012)
   PUBMED   22461452
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Albuquerque,E.X., Pereira,E.F., Alkondon,M. and Rogers,S.W.
  TITLE     Mammalian nicotinic acetylcholine receptors: from structure to
            function
  JOURNAL   Physiol Rev 89 (1), 73-120 (2009)
   PUBMED   19126755
  REMARK    Review article
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Yumoto,N., Wakatsuki,S. and Sehara-Fujisawa,A.
  TITLE     The acetylcholine receptor gamma-to-epsilon switch occurs in
            individual endplates
  JOURNAL   Biochem Biophys Res Commun 331 (4), 1522-1527 (2005)
   PUBMED   15883046
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Wang,Z.Z., Washabaugh,C.H., Yao,Y., Wang,J.M., Zhang,L.,
            Ontell,M.P., Watkins,S.C., Rudnicki,M.A. and Ontell,M.
  TITLE     Aberrant development of motor axons and neuromuscular synapses in
            MyoD-null mice
  JOURNAL   J Neurosci 23 (12), 5161-5169 (2003)
   PUBMED   12832540
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Witzemann,V., Stein,E., Barg,B., Konno,T., Koenen,M., Kues,W.,
            Criado,M., Hofmann,M. and Sakmann,B.
  TITLE     Primary structure and functional expression of the alpha-, beta-,
            gamma-, delta- and epsilon-subunits of the acetylcholine receptor
            from rat muscle
  JOURNAL   Eur J Biochem 194 (2), 437-448 (1990)
   PUBMED   1702709
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Gu,Y., Franco,A. Jr., Gardner,P.D., Lansman,J.B., Forsayeth,J.R.
            and Hall,Z.W.
  TITLE     Properties of embryonic and adult muscle acetylcholine receptors
            transiently expressed in COS cells
  JOURNAL   Neuron 5 (2), 147-157 (1990)
   PUBMED   2383398
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Criado,M., Witzemann,V., Koenen,M. and Sakmann,B.
  TITLE     Nucleotide sequence of the rat muscle acetylcholine receptor
            epsilon-subunit
  JOURNAL   Nucleic Acids Res 16 (22), 10920 (1988)
   PUBMED   3205730
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Witzemann,V., Barg,B., Nishikawa,Y., Sakmann,B. and Numa,S.
  TITLE     Differential regulation of muscle acetylcholine receptor gamma- and
            epsilon-subunit mRNAs
  JOURNAL   FEBS Lett 223 (1), 104-112 (1987)
   PUBMED   3666131
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Porter,C.W., Barnard,E.A. and Chiu,T.H.
  TITLE     The ultrastructural localization and quantitation of cholinergic
            receptors at the mouse motor endplate
  JOURNAL   J Membr Biol 14 (4), 383-402 (1973)
   PUBMED   4781450
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X74836.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X74836.1, X13252.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132268 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..494
                     /product="acetylcholine receptor subunit epsilon
                     precursor"
                     /note="acetylcholine receptor subunit epsilon; cholinergic
                     receptor, nicotinic, epsilon (muscle); cholinergic
                     receptor, nicotinic epsilon; acetylcholine receptor
                     epsilon; cholinergic receptor, nicotinic, epsilon
                     polypeptide; epsilon-subunit; gene for acetylcholine
                     receptor epsilon subunit"
                     /calculated_mol_wt=52860
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2107
     mat_peptide     21..494
                     /product="acetylcholine receptor subunit epsilon"
                     /calculated_mol_wt=52860
     Region          49..239
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(59,61,67..68,75,97,99,108..109,111,113..114,
                     125..127,129,139,141,143,147,169,239)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P09660.2)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P09660.2)"
     Site            240..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09660.2)"
     Region          247..475
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            273..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09660.2)"
     Site            307..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09660.2)"
     Site            458..481
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09660.2)"
     CDS             1..494
                     /gene="Chrne"
                     /gene_synonym="nAChR"
                     /coded_by="NM_017194.1:42..1526"
                     /db_xref="GeneID:29422"
                     /db_xref="RGD:2353"
ORIGIN      
        1 mtmallgtll llalfgrsqg kneelslyhh lfdnydpecr pvrrpedtvt itlkvtltnl
       61 islnekeetl ttsvwigiew qdyrlnfskd dfagveilrv psehvwlpei vlennidgqf
      121 gvaydcnvlv yeggsvswlp paiyrstcav evtyfpfdwq ncslifrsqt ynaeevelif
      181 avdddgnain kididtaaft engewaidyc pgmirhyegg stedpgetdv iytliirrkp
      241 lfyviniivp cvlisglvll ayflpaqagg qkctvsinvl laqtvflfli aqkipetsls
      301 vpllgrylif vmvvatlivm ncvivlnvsl rtptthatsp rlrqillell prllglsppp
      361 edpgaaspar rassvgillr aeelilkkpr selvfegqrh rhgtwtaaal cqnlgaaape
      421 vrccvdavnf vaestrdqea tgeelsdwvr mgkaldnvcf waalvlfsvg stliflggyf
      481 nqvpdlpypp ciqp
//
LOCUS       NP_001007017            5141 aa            linear   ROD 27-APR-2025
DEFINITION  SCO-spondin precursor [Rattus norvegicus].
ACCESSION   NP_001007017
VERSION     NP_001007017.1
DBSOURCE    REFSEQ: accession NM_001007016.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 5141)
  AUTHORS   Meiniel,O., Meiniel,R., Lalloue,F., Didier,R., Jauberteau,M.O.,
            Meiniel,A. and Petit,D.
  TITLE     The lengthening of a giant protein: when, how, and why?
  JOURNAL   J Mol Evol 66 (1), 1-10 (2008)
   PUBMED   18046595
REFERENCE   2  (residues 1 to 5141)
  AUTHORS   Phosri,C., Martin,M.P., Sihanonth,P., Whalley,A.J. and Watling,R.
  TITLE     Molecular study of the genus Astraeus
  JOURNAL   Mycol Res 111 (Pt 3), 275-286 (2007)
   PUBMED   17360168
REFERENCE   3  (residues 1 to 5141)
  AUTHORS   Meiniel,O. and Meiniel,A.
  TITLE     The complex multidomain organization of SCO-spondin protein is
            highly conserved in mammals
  JOURNAL   Brain Res Rev 53 (2), 321-327 (2007)
   PUBMED   17126404
  REMARK    Review article
REFERENCE   4  (residues 1 to 5141)
  AUTHORS   Richter,H.G., Tome,M.M., Yulis,C.R., Vio,K.J., Jimenez,A.J.,
            Perez-Figares,J.M. and Rodriguez,E.M.
  TITLE     Transcription of SCO-spondin in the subcommissural organ: evidence
            for down-regulation mediated by serotonin
  JOURNAL   Brain Res Mol Brain Res 129 (1-2), 151-162 (2004)
   PUBMED   15469891
  REMARK    GeneRIF: Results indicate that 5HT down-regulates SCO-spondin
            biosynthesis but apparently not its release, and suggest that 5HT
            may exert the effect on the SCO via the cerebrospinal fluid.
REFERENCE   5  (residues 1 to 5141)
  AUTHORS   Bamdad,M., Volle,D., Dastugue,B. and Meiniel,A.
  TITLE     Alpha1beta1-integrin is an essential signal for neurite outgrowth
            induced by thrombospondin type 1 repeats of SCO-spondin
  JOURNAL   Cell Tissue Res 315 (1), 15-25 (2004)
   PUBMED   14564503
REFERENCE   6  (residues 1 to 5141)
  AUTHORS   Goncalves-Mendes,N., Simon-Chazottes,D., Creveaux,I., Meiniel,A.,
            Guenet,J.L. and Meiniel,R.
  TITLE     Mouse SCO-spondin, a gene of the thrombospondin type 1 repeat (TSR)
            superfamily expressed in the brain
  JOURNAL   Gene 312, 263-270 (2003)
   PUBMED   12909363
REFERENCE   7  (residues 1 to 5141)
  AUTHORS   El-Bitar,F., Bamdad,M., Dastugue,B. and Meiniel,A.
  TITLE     Effects of SCO-spondin thrombospondin type 1 repeats (TSR) in
            comparison to Reissner's fiber material on the differentiation of
            the B104 neuroblastoma cell line
  JOURNAL   Cell Tissue Res 304 (3), 361-369 (2001)
   PUBMED   11456412
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ629845.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ629845.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMD00132263,
                                           SAMD00132264 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..5141
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..5141
                     /product="SCO-spondin precursor"
                     /function="putative role in neuronal development"
                     /note="subcommissural organ spondin"
                     /calculated_mol_wt=548856
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1815
     mat_peptide     18..5141
                     /product="SCO-spondin. /id=PRO_0000245044"
                     /note="propagated from UniProtKB/Swiss-Prot (Q700K0.1)"
                     /calculated_mol_wt=548856
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          192..341
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          396..468
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          472..527
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(481,485,500,504)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          556..716
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Site            657
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          <770..826
                     /region_name="C8"
                     /note="This domain contains 8 conserved cysteine residues;
                     smart00832"
                     /db_xref="CDD:214843"
     Site            822
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          830..883
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(839,843,853,859)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            895
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            991
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1008..1167
                     /region_name="VWD"
                     /note="von Willebrand factor (vWF) type D domain;
                     smart00216"
                     /db_xref="CDD:214566"
     Region          1209..1276
                     /region_name="C8"
                     /note="C8 domain; pfam08742"
                     /db_xref="CDD:462584"
     Region          1280..1336
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(1289,1293,1308,1313)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            1357
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1381..1416
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1386,1395,1406..1407)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1399,1402,1406,1412..1413)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1409..1413
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1421..1455
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1426,1434,1445..1446)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1438,1441,1445,1451..1452)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1448..1452
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1457..1491
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1462,1470,1481..1482)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1474,1477,1481,1487..1488)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1484..1488
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1497..1528
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(1502,1510,1521..1522)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1514,1517,1521,1527..1528)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1524..1528
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1533..1567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1568..1604
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(1575,1583,1594..1595)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1587,1590,1594,1600..1601)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1597..1601
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1655
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            1668
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1702..1753
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            1725
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1759..1812
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Site            1814
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          1817..1873
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(1826,1829,1842,1848)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Region          1917..1970
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            2035
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          2087..2109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          <2111..2225
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cl25480"
                     /db_xref="CDD:330301"
     Site            order(2111,2139,2144)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            2130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            2148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          2236..2270
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2241,2249,2260..2261)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2253,2256,2260,2266..2267)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Region          2262..2335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            2263..2267
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2392..2426
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2397,2405,2416..2417)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2409,2412,2416,2422..2423)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2419..2423
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2449..2483
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(2454,2462,2473..2474)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(2466,2469,2473,2479..2480)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            2476..2480
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          2486..2537
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Region          2543..2595
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          2618..2660
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            2630
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            2679
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          2703..2752
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          2760..2813
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          2819..2867
                     /region_name="TSP_1"
                     /note="Thrombospondin type 1 domain; pfam00090"
                     /db_xref="CDD:459668"
     Region          2871..2930
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(2883,2890,2903,2907)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            2921
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          2932..2979
                     /region_name="VWC_out"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00215"
                     /db_xref="CDD:214565"
     Site            2951
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          2972..3023
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          3029..3067
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Site            3046
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3075..3127
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            3101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            3148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            3158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3240..3292
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            3295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3300..3350
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(3307,3311,3321,3325)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            3384
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3390..>3435
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Region          3460..3504
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            3506
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3514..3570
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(3523,3527,3540,3547)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            3584
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            3611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3633..3677
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            3787
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3810..3862
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          3879..3927
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            3910
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          3945..3998
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4003..4055
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4058..4113
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(4067,4071,4084,4090)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            4135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4158..4208
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4252..4303
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            4345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4367..4418
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            4416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4422..4477
                     /region_name="TIL"
                     /note="trypsin inhibitor-like cysteine rich domain;
                     cd19941"
                     /db_xref="CDD:410995"
     Site            order(4431,4435,4448,4454)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            4557
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4611..4659
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          4673..4719
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(4674,4678,4691,4696)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            4727
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            4744
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            4749
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4761..4811
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; cl46269"
                     /db_xref="CDD:480609"
     Region          4814..4868
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            order(4823,4827,4840,4845)
                     /site_type="other"
                     /note="reactive site [polypeptide binding]"
                     /db_xref="CDD:410995"
     Site            4899
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4920..4978
                     /region_name="TIL"
                     /note="Trypsin Inhibitor like cysteine rich domain;
                     pfam01826"
                     /db_xref="CDD:460351"
     Site            4942
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Site            4949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     Region          4980..5035
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Site            5055
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q700K0.1)"
     CDS             1..5141
                     /gene="Sspo"
                     /gene_synonym="Scospondin"
                     /coded_by="NM_001007016.1:1..15426"
                     /db_xref="GeneID:474348"
                     /db_xref="RGD:1549716"
ORIGIN      
        1 mllpallfgm lwapanghwc eqietvhvee evtprredlv pctslyhysr lgwkldlswg
       61 ghvgltrppa lglcaiykpp etrpatwnrt vraccpgwgg ihctealaea spkghcfvtw
      121 hcqplagsan ssagsleecc aqpwghswwn sssqmclscs gqhrpgnass egllqplaga
      181 vgqlwsqrqr psatcatwsg fhyqtfdgqh yhflgqctyl lagamdstwa vhlrpsvhcp
      241 qprqcwlvqv imgpeevliq dgevsvkgqp vpvgesqllh gmslqwqgdw lvlsgglgvv
      301 vrldrsssii isvdhefwgr tqglcglyng rpeddfvepg gglamlaatf gnswrlpgye
      361 pgcldtveva rgcegllegt ltgleagklq aqaqdlchql ledpfsqchg qvppdeyhet
      421 clfaycvgat agsgpeeqvk avcatfanya qacarqhiyv hwrkpgfcer lcpggqlysd
      481 cisscppscs avaqgeegsc gkecvsgcec ptglfwdgal cvpaahcpcy yrrqryapgd
      541 tvkqqcnpcv cqdgrwhcaq apcpaecavg gdghyctfdg rsfsfrgnpg cqyslvqdsv
      601 kgqllvvleh gacetgsclh alsaflgkth iqlrysgavl vdgqdvdlpw igaegfnvsh
      661 asstflllrw pgawvlwgva dpavyitldp rhayqvqglc gtftwkqqdd fltpagdiet
      721 svtafaskfq vsgdgrcplv dntplsscst ysqrlafaea acaalhghaf qechglvere
      781 pfrlrclesm cscapgrdcl csvlsayahh caqegvllqw rnetlcsvpc pggqvyqeca
      841 pacghycgep edckelgscv agcncppgll wdlegqcvpp smcpcqlggh ryafnttttl
      901 kdcshcicqe rglwnciahh cprqwalcpq eliyapgacl ltcdslganh sclagstdgc
      961 vcpsgtvlld khcvspdlcp crhngqwypp natiqedcni cvcqnqrwhc tgqrcsgwcq
     1021 asgaphyvtf dglvftfpga ceyllvreag grfsvsiqnl pcgasgltct kalavrldst
     1081 vvhmlrgqav tvngvsiklp kvytgpglsl hhaglflllt trlgltllwd ggtrvlvqls
     1141 phfhgrvtgl cgnfdgdvsn dlrsrqgvle ptaeltahsw rlnplcpepg dlphpcsvna
     1201 hrvnwarahc evilqpifap chtevppqqy yewcvydacg cdtggdcecl csaiatyade
     1261 carhrhhvrw rsqelcplqc eggqvyepcg stcpptchdh hpelrwhcqa itcvegcfcp
     1321 egtllhggtc veltdcpcew qgsffppgav lqkdcgnctc qesqwhcnps gapceemepg
     1381 caegealcre sghcvplewl cdnqddcgdg sdeegcdtsv cgegqmscqs grclplslic
     1441 dgqddcgdgt deqgclcpqg flacadgrcl ppallcdghp dcldaadees clgwvsctsg
     1501 evscvdgpci rtiqlcdgvw dcpdgadegp vhcsspslpt ppagigqnps tsspdtspsp
     1561 vgsaspaspc slsefqcnsg ectprgwrcd reedctdgsd eldcggpckl yqmpcahgph
     1621 clspgqlcdg vaqcpdgsde dpdvceersa sggpngtavp cpefscpngt cidfllvcdg
     1681 spdceladet epsldeqgcg twgswgpwep csqtcgpgiq srnrncsiss lhvlqncpgl
     1741 qhqsqscfte acpvdgewss wslwspcsep cggtmtrhrq crppqnggqd callpgsths
     1801 thqtspcpqe gclnvtcfge lvfrpcapcp ltcddisgea vcspdrpcss pgcwcpegkv
     1861 lgtegrcvrp rqcpclvdgi rywpgqrikm dcqlcfcqdg qphrcrpnpe cavdcgwssw
     1921 spwaeclgpc ssqslqwsfr spnnprlsgh grqcrgihrk arrcqtepce gceqwgltyh
     1981 vgerwrggpc tvceclhrsi trcspycpig scpqswvlve gmgescchca lpgknqtmip
     2041 vttpapvptp spqigaslvt yvlppmsdac ysplglaglp twapsqpleh straapveap
     2101 tagpgpreda yaewhtqply lqldllwprn ltgimvqrag ssaayisnls lqfssdglqw
     2161 hsvlnslsst lpppkpspes snhmvpevwt fdqmvqaryi rvwphgshlr dnnqqdiflw
     2221 vellgckpvp plaplcpgtr hrcangdcal kggpcdgavd cedgsdeegc gplrastasr
     2281 vhstartpal sptqpgkfpf hpregladme hqqpkqespm psagvspsas egllpvsgqs
     2341 mqtltttstf ppglkslhpg maavtvhsph svmpgtpvgq svsprpfplm rcgpgqvpcd
     2401 vlgcveqeql cdgredcldg sdeqhcaspe pftvpttalp glpasralcs psqlscgsge
     2461 clplehrcdl qvncqdgsde ddcvdcvlap wsgwsdcsrs cglglifqhr ellrpplpgg
     2521 sclldqlrsq pcfvqacpva gawakwgpwe pcsvscgggh qsrqrscvdp ppknggapcp
     2581 gpshekvlcn lqlcpgdtdc epgrvhvnae lcqkgllppc ppscldpean rscsghcveg
     2641 crcppglflq dshclplsec pclvgqklmq pglaflldnc sqcicesgil lckpaacsqs
     2701 cgwsawspwt acdhscgsgv rarfrsptnp paafggspce gdrqelqacy tdcgtdipgw
     2761 tpwtswsscs qsclvpggdp grrqrsrlcp ssrdtfcpge atqeepcsps lcpvpsawgl
     2821 waswsacsas cnggiqtrgr scsgsapgnp vclgphtqtr dcnvhpctaq cpgnmvfrsa
     2881 ekcleeggpc pqlclaqdpg vectgscapg cscppglflh nasclprsqc pcqlhgqlya
     2941 pgavarldcn nctcssgemv ctsercpvac gwspwtpwsp csqscnvgir rrfragtapp
     3001 aafggaecrg pnldaefctl rpcqgpgaaw sswtpcsvpc gggyrnrtqg sgrhspvefs
     3061 tcslqpcagp vpgvcpkdqq wldcaqgpas cahlstprea nqtchpgcyc lsgmlllnnv
     3121 cvpaqdcpca hrgrlhspgs avilpcencs cvsglitncs swpceegqpa wsswtpwsvc
     3181 sascsparrh rrrfcvrpst tapfsldlpt tvaaptmlcp gpeaeeepcl lpgcnqagvw
     3241 gpwspwsgcs rscggglrsr tracdkpppq glgdfcegpq aqgeacqaqp cpvancstie
     3301 gaeyspcgpp cprscddlvh cmwhcqpgcy cppgkvlsad gaicvqphhc scldlltgkr
     3361 hhpgsqlmrp dgcnhctcme grlnctdlpc qvsgdwcpws ewtacsqpcr gqtrtrsrac
     3421 vcpapqhgga pcpeeagetg vqhqmeacpn ptacpvdgaw spwgswspcd aclgqsyrsr
     3481 mcshpppsdg gtpclgghqq srpcrnsstp ctdcgggqdl lpcgqpcphs cqdlslgstc
     3541 qpgssgcqsg cgcppgqlsq dglcvfpadc hchfqpkamg ipenqsrsvg salsswesle
     3601 pgevvtgpcd nctcvagvlq chevpscpgp giwsswgpwe kcsvpcggge qlrsrqcarp
     3661 pcpglaqqsr tchihvcret gcpagrlyre cqpsegcpfs cahvtgqvac fsesceegch
     3721 cpegtfqhhs acvqecpcvl tvsllqelgv astalrsypv llgdegqplg pgdeldpgqm
     3781 lqtvcgncsc vhgklscsme ecsrvrgyfg pwgmwslcsh scgglgtrtr trqcvlptla
     3841 paglscrgpl qdleycfspe cpgtagstve pvtglaggwg pwspwspcsh sctdlthpaw
     3901 rsrtrlclan ctvgdssqer pcnlpscttl plcpgpgcgs encfwtswap wepcsrscgv
     3961 gqqrrlrayh ppgpgghwcp diltayqerr fcnlracpvp ggwshwspws wcdrscgggr
     4021 slrsrscssp ppknggascv gerhhvrscn pmpcekdcpa gmemvscanr cpyscsdlqe
     4081 avmcqedqac qlgcrcsegf leqdggcvpv ghcectdaqg rswapgsqhq dacnncscqa
     4141 gqlsctaqpc pppahcawsh wsawsacshs cgphgqqsrf rsstsgswal ecqkeqsqsq
     4201 pcpedpcppl clheahlhvl gdnwlhgecq qcsctpegvi ckdtdcavpg gwtlwsswsy
     4261 csvscgggsq vrtrscmvsa pqhgspscqg pdtqtqhcgq qlclqlleic swgpwgpcsr
     4321 scgtglasrs gscpclltke dsecndtfsg ldtqacypgp cqedcmwsdw sswtrcscki
     4381 lvqqryrhqv papgqagegt lctgldghfr pcaigncsed sclppfefqs cgspcaglca
     4441 thlshqlcqd lppcqpgcyc pmglleqdgg cilpeqcncw htsgegarvt lapghrlqlg
     4501 ckecvcqsge lqcssqgceg llpltgwsew spcgpclpqs alapdsrtal evhwplntsv
     4561 tllaseqyrh rlcldpetgr pwagdpalct vplsqqrlcs dpgachdtcq wgpwgpwspc
     4621 qvpcsggfkl rwreasdnsv gecrgpwaqt escnmgscpg escetrdtvf tldcanqcpr
     4681 scadlwegvq clqgpcspgc rcppgqlvqd ghcvpisscr cglpsanasw elaptqvvql
     4741 dchnctcing tlmcpypecp vlgpwspwse csavcgggtm vryrsceehp dsapcqaldm
     4801 eqrvecnlqt cpecppgqvl stcatlcpsf cshlwpgtic vrepcqlgcg cpggqllhsg
     4861 tcippeacpc trlslpwglt lpleeqaqel psgtvltwnc thctcqggvf tcshtdcqec
     4921 ppgeilqlge lrpcektcle mnktqawsnc teaqvpgcvc qlghfrshtg lcvpedhcec
     4981 whhgsphlpg sewqeacesc rclhgksvct qhcpelscaq gevvvqepgs ccpicqqdtl
     5041 eeepvscrhl telrnltkgp chldqvevsy csghcrsstn vmteepylqs qcdccsyrld
     5101 pdspvrilnl lcpdgrtepv llpvihnchc sacqggefsk h
//
LOCUS       NP_579838               1157 aa            linear   ROD 27-APR-2025
DEFINITION  hephaestin precursor [Rattus norvegicus].
ACCESSION   NP_579838
VERSION     NP_579838.1
DBSOURCE    REFSEQ: accession NM_133304.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   Wang,J., Qu,D., An,J., Yuan,G. and Liu,Y.
  TITLE     Integrated microarray analysis provided novel insights to the
            pathogenesis of glaucoma
  JOURNAL   Mol Med Rep 16 (6), 8735-8746 (2017)
   PUBMED   28990066
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Drakesmith,H., Nemeth,E. and Ganz,T.
  TITLE     Ironing out Ferroportin
  JOURNAL   Cell Metab 22 (5), 777-787 (2015)
   PUBMED   26437604
  REMARK    Review article
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   Kong,W.N., Wu,Q., Shen,D., Zhao,S.E., Guo,P., Duan,X.L. and
            Chang,Y.Z.
  TITLE     Age-dependent expression of duodenal cytochrome b, divalent metal
            transporter 1, ferroportin 1, and hephaestin in the duodenum of
            rats
  JOURNAL   J Gastroenterol Hepatol 30 (3), 513-520 (2015)
   PUBMED   25318588
  REMARK    GeneRIF: Hepcidin or enterocyte iron levels may be involved in the
            regulation of the age-dependent expression in the duodenum.
REFERENCE   4  (residues 1 to 1157)
  AUTHORS   Vashchenko,G. and Macgillivray,R.T.
  TITLE     Functional role of the putative iron ligands in the ferroxidase
            activity of recombinant human hephaestin
  JOURNAL   J Biol Inorg Chem 17 (8), 1187-1195 (2012)
   PUBMED   22961397
REFERENCE   5  (residues 1 to 1157)
  AUTHORS   Ranganathan,P.N., Lu,Y., Fuqua,B.K. and Collins,J.F.
  TITLE     Immunoreactive hephaestin and ferroxidase activity are present in
            the cytosolic fraction of rat enterocytes
  JOURNAL   Biometals 25 (4), 687-695 (2012)
   PUBMED   22350470
  REMARK    GeneRIF: Cytosolic Heph increased upon iron-deprivation but more
            important, decreased significantly upon copper-deprivation,
            mimicking the response of membrane-bound Heph.
REFERENCE   6  (residues 1 to 1157)
  AUTHORS   Qian,Z.M., Chang,Y.Z., Zhu,L., Yang,L., Du,J.R., Ho,K.P., Wang,Q.,
            Li,L.Z., Wang,C.Y., Ge,X., Jing,N.L., Li,L. and Ke,Y.
  TITLE     Development and iron-dependent expression of hephaestin in
            different brain regions of rats
  JOURNAL   J Cell Biochem 102 (5), 1225-1233 (2007)
   PUBMED   17516501
  REMARK    GeneRIF: Development and iron-dependent expression of Heph in
            different brain regions is reported.
REFERENCE   7  (residues 1 to 1157)
  AUTHORS   Wang,J., Jiang,H. and Xie,J.X.
  TITLE     Ferroportin1 and hephaestin are involved in the nigral iron
            accumulation of 6-OHDA-lesioned rats
  JOURNAL   Eur J Neurosci 25 (9), 2766-2772 (2007)
   PUBMED   17561842
  REMARK    GeneRIF: These results show for the first time that FP1 and HP
            co-localize in the rat brain, and suggest that decreased expression
            of these transporters in the SN can account for the increased iron
            levels.
REFERENCE   8  (residues 1 to 1157)
  AUTHORS   Qian,Z.M., Chang,Y.Z., Leung,G., Du,J.R., Zhu,L., Wang,Q., Niu,L.,
            Xu,Y.J., Yang,L., Ho,K.P. and Ke,Y.
  TITLE     Expression of ferroportin1, hephaestin and ceruloplasmin in rat
            heart
  JOURNAL   Biochim Biophys Acta 1772 (5), 527-532 (2007)
   PUBMED   17383861
  REMARK    GeneRIF: Hephaestin might have a role in heart iron homeostasis.
REFERENCE   9  (residues 1 to 1157)
  AUTHORS   Simovich,M.J., Conrad,M.E., Umbreit,J.N., Moore,E.G.,
            Hainsworth,L.N. and Smith,H.K.
  TITLE     Cellular location of proteins related to iron absorption and
            transport
  JOURNAL   Am J Hematol 69 (3), 164-170 (2002)
   PUBMED   11891802
  REMARK    GeneRIF: cellular locations identified by immunofluorescence
REFERENCE   10 (residues 1 to 1157)
  AUTHORS   Frazer,D.M., Vulpe,C.D., McKie,A.T., Wilkins,S.J., Trinder,D.,
            Cleghorn,G.J. and Anderson,G.J.
  TITLE     Cloning and gastrointestinal expression of rat hephaestin:
            relationship to other iron transport proteins
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 281 (4), G931-G939 (2001)
   PUBMED   11557513
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF246120.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF246120.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..1157
                     /product="hephaestin precursor"
                     /EC_number="1.16.3.1"
                     /calculated_mol_wt=127104
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2508
     mat_peptide     24..1157
                     /product="Hephaestin. /id=PRO_0000002917"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920H8.1)"
                     /calculated_mol_wt=127104
     Region          26..208
                     /region_name="CuRO_1_ceruloplasmin"
                     /note="The first cupredoxin domain of Ceruloplasmin;
                     cd04222"
                     /db_xref="CDD:259884"
     Site            order(26,28,34,36..37,39..40,53..54,57..58,60..62,64..69,
                     72..76,94..99,104,121,123,176,179..184,193..197,200,202)
                     /site_type="other"
                     /note="Domain 2 interface [polypeptide binding]"
                     /db_xref="CDD:259884"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            order(126,128..129,132,134,137,141,143,170..172,174,177,
                     183,186,188,190,192)
                     /site_type="other"
                     /note="Domain 6 interface [polypeptide binding]"
                     /db_xref="CDD:259884"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Region          223..363
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Region          377..571
                     /region_name="CuRO_3_ceruloplasmin"
                     /note="The third cupredoxin domain of Ceruloplasmin;
                     cd04224"
                     /db_xref="CDD:259886"
     Site            order(390..391,393..394,396,398..399,416..417,419..424,
                     427..431,451..456,459,478,485,533..535,537,539,545..550,
                     553,555,557,569..571)
                     /site_type="other"
                     /note="Domain 4 interface [polypeptide binding]"
                     /db_xref="CDD:259886"
     Site            order(483,485..486,488..489,491,522..525,527,530,534,536,
                     539,544..545,549)
                     /site_type="other"
                     /note="Domain 2 interface [polypeptide binding]"
                     /db_xref="CDD:259886"
     Region          574..717
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Site            587
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            713
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Region          732..903
                     /region_name="CuRO_5_ceruloplasmin"
                     /note="The fifth cupredoxin domain of Ceruloplasmin;
                     cd04225"
                     /db_xref="CDD:259887"
     Site            order(740,742..748,751..752,766..769,771,773..783,
                     804..809,812,814,829,831,833,838,872..874,876,878,880,886,
                     889..893,896..898,900)
                     /site_type="other"
                     /note="Domain 6 interface [polypeptide binding]"
                     /db_xref="CDD:259887"
     Site            757
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            order(838..839,841..842,865..873,879,882,887..888,892)
                     /site_type="other"
                     /note="Domain 4 interface [polypeptide binding]"
                     /db_xref="CDD:259887"
     Region          919..1062
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Site            930
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            1110..1130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            1144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            1149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     Site            1154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0Z4; propagated from
                     UniProtKB/Swiss-Prot (Q920H8.1)"
     CDS             1..1157
                     /gene="Heph"
                     /coded_by="NM_133304.1:82..3555"
                     /db_xref="GeneID:117240"
                     /db_xref="RGD:71060"
ORIGIN      
        1 mkaghllwal llmhslcslp tdgairnyyl giqdiqwnya pkgrnvitnq tlnndtvass
       61 flksgknrig gtykktvyke ysdgtytnei akpawlgflg pllkaemgdv ilihlknfas
      121 rpytihphgv fyekdsegsl ypdgssgylk addsvppggs hvynwsipeg hapteadpac
      181 ltwiyhshvd aprdiatgli gplitckrgt ldgnsppqrk dvdhnffllf svidenlswh
      241 lddniatycs dpasvdkedg pfqdsnrmha ingfvfgnlp elsmcaqkhv awhlfgmgne
      301 idvhtaffhg qtlsirghrt dvahifpatf vtaemvpqks gtwliscvvn shlksgmqaf
      361 ykvdscsmdp pveqltgkvr qyfiqaheiq wdygpighdg rtgkslrepg sgpdkyfqks
      421 ssriggtywk vryeafqdet fqerlhqeee thlgilgpvi raevgdtiqv vfynrasqpf
      481 siqphgvfye kssegtvynd gtsypkvaks fekvtyywtv pphagptaed pacltwmyfs
      541 aadptrdtns glvgpllvck agalgedgkq kgvdkeffll ftifdenesw ynnanqaagm
      601 ldsrllsedv egfedsnrmh aingflfsnl prldickgdt vawhllglgt endvhgvmfe
      661 gntlqlqgmr ksaamlfpht fvtaimqpdn pgifeiycqa gshreagmqa iynvsqcssh
      721 qdsprqhyqa srvyyimaee iewdycpdrs welewyntse kdsyghvfls nkdgllgsky
      781 kkavfreytd gtfripqprs gpeehlgilg plirgevgdi ltvvfknkas rpysihahgv
      841 lesstgwpqa aepgevltyq wnipersgpg psdsacvswi yysavdpikd mysglvgplv
      901 icrngilepn ggrndmdref allflifden qswylkenia tygpqetshv nlqdatfles
      961 nkmhaingkl yanlrgltvy qgervawyml amgqdtdiht vhfhaesfly qnghsyradv
     1021 vdlfpgtfev vemvasnpga wlmhchvtdh vhagmetift vlsheehfst mttitkeigk
     1081 avilqnigeg nvkmlgmnip vknveilssa liaicvvlll ialalggvvw yqhrqrklrr
     1141 nrrsilddsf kllslkq
//
LOCUS       NP_112266                377 aa            linear   ROD 27-APR-2025
DEFINITION  actin, aortic smooth muscle [Rattus norvegicus].
ACCESSION   NP_112266 XP_001079913
VERSION     NP_112266.1
DBSOURCE    REFSEQ: accession NM_031004.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Ali,E.M.T., El-Sayed,S.M. and Elbastawisy,Y.M.
  TITLE     Ultrastructural aberrations, histological disruption and
            upregulation of the VEGF, CD34 and ASMA immunoexpression in the
            myocardium of anemic albino rats
  JOURNAL   Acta Histochem 123 (5), 151731 (2021)
   PUBMED   34052675
  REMARK    GeneRIF: Ultrastructural aberrations, histological disruption and
            upregulation of the VEGF, CD34 and ASMA immunoexpression in the
            myocardium of anemic albino rats.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Ren,M., Wang,T., Wei,X., Wang,Y., Ouyang,C., Xie,Y., Ye,X. and
            Han,Z.
  TITLE     LncRNA H19 regulates smooth muscle cell functions and participates
            in the development of aortic dissection through sponging
            miR-193b-3p
  JOURNAL   Biosci Rep 41 (1) (2021)
   PUBMED   33403385
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Xian,S., Chen,A., Wu,X., Lu,C., Wu,Y., Huang,F. and Zeng,Z.
  TITLE     Activation of activin/Smad2 and 3 signaling pathway and
            the&nbsp;potential involvement of endothelial-mesenchymal
            transition in the valvular damage due to rheumatic heart disease
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33179113
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Spade,D.J., Hall,S.J., Wortzel,J.D., Reyes,G. and Boekelheide,K.
  TITLE     All-trans Retinoic Acid Disrupts Development in Ex Vivo Cultured
            Fetal Rat Testes. II: Modulation of Mono-(2-ethylhexyl) Phthalate
            Toxicity
  JOURNAL   Toxicol Sci 168 (1), 149-159 (2019)
   PUBMED   30476341
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Minocha,E., Chaturvedi,C.P. and Nityanand,S.
  TITLE     Renogenic characterization and in vitro differentiation of rat
            amniotic fluid stem cells into renal proximal tubular- and
            juxtaglomerular-like cells
  JOURNAL   In Vitro Cell Dev Biol Anim 55 (2), 138-147 (2019)
   PUBMED   30645697
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Shah,N.M., Groves,A.K. and Anderson,D.J.
  TITLE     Alternative neural crest cell fates are instructively promoted by
            TGFbeta superfamily members
  JOURNAL   Cell 85 (3), 331-343 (1996)
   PUBMED   8616889
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Hsu,C.Y. and Frankel,F.R.
  TITLE     Conserved and unique sequences in the 3'-untranslated region of rat
            smooth-muscle alpha-actin mRNA
  JOURNAL   Gene 69 (2), 345-348 (1988)
   PUBMED   3234770
REFERENCE   8  (residues 1 to 377)
  AUTHORS   McHugh,K.M. and Lessard,J.L.
  TITLE     The nucleotide sequence of a rat vascular smooth muscle alpha-actin
            cDNA
  JOURNAL   Nucleic Acids Res 16 (9), 4167 (1988)
   PUBMED   3375082
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Hsu,C.Y. and Frankel,F.R.
  TITLE     Effect of estrogen on the expression of mRNAs of different actin
            isoforms in immature rat uterus. Cloning of alpha-smooth muscle
            actin message
  JOURNAL   J Biol Chem 262 (20), 9594-9600 (1987)
   PUBMED   3597426
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Mayer,Y., Czosnek,H., Zeelon,P.E., Yaffe,D. and Nudel,U.
  TITLE     Expression of the genes coding for the skeletal muscle and cardiac
            actions in the heart
  JOURNAL   Nucleic Acids Res 12 (2), 1087-1100 (1984)
   PUBMED   6546444
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN934985.1, CB608976.1, BI287899.1 and BI282383.1.
            
            On Jul 24, 2006 this sequence version replaced XP_001079913.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158550.1, SRR8487226.75077.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..377
                     /product="actin, aortic smooth muscle"
                     /note="alpha-actin-2; smooth muscle alpha-actin; actin,
                     alpha 2, smooth muscle, aorta"
                     /calculated_mol_wt=41878
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine, in intermediate form.
                     /evidence=ECO:0000250|UniProtKB:P62737; propagated from
                     UniProtKB/Swiss-Prot (P62738.1)"
     mat_peptide     3..377
                     /product="Actin, aortic smooth muscle.
                     /evidence=ECO:0000250|UniProtKB:P62737.
                     /id=PRO_0000442610"
                     /note="propagated from UniProtKB/Swiss-Prot (P62738.1)"
                     /calculated_mol_wt=41775
     Region          8..372
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     Site            75
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000250|UniProtKB:P62739; propagated from
                     UniProtKB/Swiss-Prot (P62738.1)"
     Site            86
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68032; propagated from
                     UniProtKB/Swiss-Prot (P62738.1)"
     CDS             1..377
                     /gene="Acta2"
                     /coded_by="NM_031004.2:58..1191"
                     /db_xref="GeneID:81633"
                     /db_xref="RGD:621676"
ORIGIN      
        1 mceeedstal vcdngsglck agfagddapr avfpsivgrp rhqgvmvgmg qkdsyvgdea
       61 qskrgiltlk ypiehgiitn wddmekiwhh sfynelrvap eehptlltea plnpkanrek
      121 mtqimfetfn vpamyvaiqa vlslyasgrt tgivldsgdg vthnvpiyeg yalphaimrl
      181 dlagrdltdy lmkiltergy sfvttaerei vrdikeklcy valdfenema taasssslek
      241 syelpdgqvi tignerfrcp etlfqpsfig mesagihett ynsimkcdid irkdlyannv
      301 lsggttmypg iadrmqkeit alapstmkik iiapperkys vwiggsilas lstfqqmwis
      361 kqeydeagps ivhrkcf
//
LOCUS       NP_786939               1320 aa            linear   ROD 27-APR-2025
DEFINITION  immunoglobulin superfamily member 1 precursor [Rattus norvegicus].
ACCESSION   NP_786939
VERSION     NP_786939.1
DBSOURCE    REFSEQ: accession NM_175763.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1320)
  AUTHORS   Wang,Y., Brule,E., Silander,T., Bak,B., Joustra,S.D. and
            Bernard,D.J.
  TITLE     The short mRNA isoform of the immunoglobulin superfamily, member 1
            gene encodes an intracellular glycoprotein
  JOURNAL   PLoS One 12 (7), e0180731 (2017)
   PUBMED   28686733
  REMARK    GeneRIF: Contrary to earlier predictions, neither the murine nor
            rat IGSF1-2 is secreted from heterologous or homologous cells. In
            addition, neither protein associates with the plasma membrane.
            Rather, IGSF1-2 appears to be retained in the endoplasmic
            reticulum.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1320)
  AUTHORS   Joustra,S.D., Meijer,O.C., Heinen,C.A., Mol,I.M., Laghmani el,H.,
            Sengers,R.M., Carreno,G., van Trotsenburg,A.S., Biermasz,N.R.,
            Bernard,D.J., Wit,J.M., Oostdijk,W., van Pelt,A.M., Hamer,G. and
            Wagenaar,G.T.
  TITLE     Spatial and temporal expression of immunoglobulin superfamily
            member 1 in the rat
  JOURNAL   J Endocrinol 226 (3), 181-191 (2015)
   PUBMED   26163525
  REMARK    GeneRIF: High levels of Igsf1 in brain, pituitary and fetal liver.
            Also expressed in pancreas, heart, skeletal muscle, adrenal gland
            and testis.
REFERENCE   3  (residues 1 to 1320)
  AUTHORS   Chapman,S.C. and Woodruff,T.K.
  TITLE     Modulation of activin signal transduction by inhibin B and
            inhibin-binding protein (INhBP)
  JOURNAL   Mol Endocrinol 15 (4), 668-679 (2001)
   PUBMED   11266516
REFERENCE   4  (residues 1 to 1320)
  AUTHORS   Bernard,D.J. and Woodruff,T.K.
  TITLE     Inhibin binding protein in rats: alternative transcripts and
            regulation in the pituitary across the estrous cycle
  JOURNAL   Mol Endocrinol 15 (4), 654-667 (2001)
   PUBMED   11266515
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF322216.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF322216.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1320
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..1320
                     /product="immunoglobulin superfamily member 1 precursor"
                     /note="inhibin-binding protein"
                     /calculated_mol_wt=145117
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
                     /calculated_mol_wt=2195
     mat_peptide     19..1320
                     /product="Immunoglobulin superfamily member 1.
                     /id=PRO_0000318514"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
                     /calculated_mol_wt=145117
     Region          28..114
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          45..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          57..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          80..84
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          94..99
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..112
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          122..212
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          139..143
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..155
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          173..177
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          187..192
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          205..208
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..307
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          235..239
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          247..251
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          270..274
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          284..289
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          300..303
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..405
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          330..334
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..346
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          366..370
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          380..385
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          395..401
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          407..488
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          419..423
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          431..435
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          449..453
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          463..468
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          481..484
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            505..525
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
     Site            535..555
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          575..663
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          592..596
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          605..609
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          627..631
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          641..646
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          656..659
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          669..756
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          683..687
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          695..699
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          717..721
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          731..736
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            731
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          749..752
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          762..852
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          779..783
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          791..795
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          816..820
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          830..835
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            830
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          845..848
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          858..944
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            874
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          875..879
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          887..891
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          909..913
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          923..928
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            923
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          941..944
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          954..1044
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            970
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          971..975
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          983..987
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1005..1009
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            1011
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1019..1024
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1037..1040
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1050..1140
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1066
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1067..1071
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          1079..1083
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          1101..1105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          1115..1120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Site            1131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1133..1136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          1146..1232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1163..1167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1175..1179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1193..1197
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1207..1212
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1225..1228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1320
                     /gene="Igsf1"
                     /gene_synonym="Inhbp"
                     /coded_by="NM_175763.2:172..4134"
                     /db_xref="GeneID:302822"
                     /db_xref="RGD:631402"
ORIGIN      
        1 mmlrtftlll lciwlnrgmt smaavesqpe lwiesnypqa pwenitlwck spsrvsskfl
       61 llkdntqmtw ihppyktfqv sffigaltes ntglyrccyw nekgwskpsk ileleapgql
      121 pkpifwiqae tppfpgcnvn ilchgwlqdl vfmlfkegyt epidyqvptg tmaifsidnl
      181 apenegiyic rthiqmlptl wsepsnplkl vvaglypkpt ltahpgpila pgeslslrcq
      241 gpiygmtfal mrledlkkpy yykkpiknea yfyfqalktq dtghylcfyy dgsyrgslls
      301 dilkiwvtdt fpktwllvqp spviqmgqnv slrcgglmdg vglalhkkge ekplqfldat
      361 sntgnnsffl knvtyrdagi yschyyltwk tsikmatynt velivvawps svfkvgktit
      421 lqcrvshpvl efsleweett tfqkfsvdgd fiitniegqg tgtyscsyri eshaniwshr
      481 seplklvgpa vtgflpwnsi lneairvslt vqflsllllv lwlqwkcrrl rlreawllgt
      541 aqgvamlvil iallccglcn galteeieii mptpkpelwa etnfpqapwk nvtlwcrsps
      601 gstkefvllk dgtgwiatrp aseqvraafp lgaltqshtg syhchsweem avsepseale
      661 lvgtdilpkp visaslpirg qelqirckgw leglgfalyk mgeqepvqql gavgreafft
      721 iqrmedkeeg nyscrthtek qpfkwsepsa plelvikely pkpffktwas pvvtpgsrvt
      781 fncstsrehm sfilykdgne iassdpvwgn pgtstahfli isvgigdggn yscryydfsi
      841 wsepsdpvel ivtefypkpt llaqpgpvvl pgknvtlrcq gifqgmrfal lqegahaplq
      901 fqsasgtsvd fllhtvgaed fgnyscvyye ttmsnrgsyl stplmiwvtd tfprpwlsae
      961 pssvvtmgqn vtlwcqgpvh gvgyilhkeg eatsmqlwds tsnegafpii nisgasigry
     1021 sccyhpdwms pikiqpsntl elivtgllpk psllvqpgpm vvpgenmtfq cqgelpdstf
     1081 vllkegtqqp ieqqrpsgyr adfwmpvvrd qdsgvyscvy yldsaplvas nhsnsleiwv
     1141 tdkppkpsls awpstvfklg kditlqcrgp lpgvefvleh dgeeapqqfs edgdfvignm
     1201 egkgignysc syrlqaypdi wsepsdslel vgaagpvaqe ctvgnivrst livvvvvalg
     1261 ivlaiewkkw prlrtrgset dgrdqtivle ecnqdgepgt atnspssalq gvsveqtvpi
//
LOCUS       NP_001041645             670 aa            linear   ROD 27-APR-2025
DEFINITION  SH2B adapter protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001041645
VERSION     NP_001041645.1
DBSOURCE    REFSEQ: accession NM_001048180.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Liu,B.L., Cheng,M., Hu,S., Wang,S., Wang,L., Tu,X., Huang,C.X.,
            Jiang,H. and Wu,G.
  TITLE     Overexpression of miR-142-3p improves mitochondrial function in
            cardiac hypertrophy
  JOURNAL   Biomed Pharmacother 108, 1347-1356 (2018)
   PUBMED   30372837
  REMARK    GeneRIF: miR-14 2-3 p not only mitigate cardiac hypertrophy by
            directly inhibit the expression of gene SH2B1, but also can protect
            mitochondrial function in cardiac hypertrophy of vitro and vivo.
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Yuan,J., Zeng,L., Sun,Y., Wang,N., Sun,Q., Cheng,Z. and Wang,Y.
  TITLE     SH2B1 protects against OGD/R-induced apoptosis in PC12 cells via
            activation of the JAK2/STAT3 signaling pathway
  JOURNAL   Mol Med Rep 18 (3), 2613-2620 (2018)
   PUBMED   30015896
  REMARK    GeneRIF: SH2B1 overexpression resulted in increased viability,
            reduced lactate dehydrogenase release and a reduction in the
            expression levels of proteins associated with the apoptotic cascade
            in PC12 cells under the oxygenglucose deprivation condition.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Franquinho,F., Nogueira-Rodrigues,J., Duarte,J.M., Esteves,S.S.,
            Carter-Su,C., Monaco,A.P., Molnar,Z., Velayos-Baeza,A., Brites,P.
            and Sousa,M.M.
  TITLE     The Dyslexia-susceptibility Protein KIAA0319 Inhibits Axon Growth
            Through Smad2 Signaling
  JOURNAL   Cereb Cortex 27 (3), 1732-1747 (2017)
   PUBMED   28334068
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Chen,C.J., Shih,C.H., Chang,Y.J., Hong,S.J., Li,T.N., Wang,L.H. and
            Chen,L.
  TITLE     SH2B1 and IRSp53 proteins promote the formation of dendrites and
            dendritic branches
  JOURNAL   J Biol Chem 290 (10), 6010-6021 (2015)
   PUBMED   25586189
  REMARK    GeneRIF: These findings suggest that SH2B1-IRSp53 complexes promote
            the formation of filopodia, neurite initiation, and neuronal
            branching.
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Shih,C.H., Chen,C.J. and Chen,L.
  TITLE     New function of the adaptor protein SH2B1 in brain-derived
            neurotrophic factor-induced neurite outgrowth
  JOURNAL   PLoS One 8 (11), e79619 (2013)
   PUBMED   24260264
  REMARK    GeneRIF: findings demonstrate that SH2B1beta promotes BDNF-induced
            neurite outgrowth through enhancing pathways involved MEK-ERK1/2
            and PI3K-AKT.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Diakonova,M., Gunter,D.R., Herrington,J. and Carter-Su,C.
  TITLE     SH2-Bbeta is a Rac-binding protein that regulates cell motility
  JOURNAL   J Biol Chem 277 (12), 10669-10677 (2002)
   PUBMED   11786545
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Riedel,H., Yousaf,N., Zhao,Y., Dai,H., Deng,Y. and Wang,J.
  TITLE     PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated
            mitogenesis
  JOURNAL   Oncogene 19 (1), 39-50 (2000)
   PUBMED   10644978
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Kasus-Jacobi,A., Perdereau,D., Auzan,C., Clauser,E., Van
            Obberghen,E., Mauvais-Jarvis,F., Girard,J. and Burnol,A.F.
  TITLE     Identification of the rat adapter Grb14 as an inhibitor of insulin
            actions
  JOURNAL   J Biol Chem 273 (40), 26026-26035 (1998)
   PUBMED   9748281
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Rui,L., Mathews,L.S., Hotta,K., Gustafson,T.A. and Carter-Su,C.
  TITLE     Identification of SH2-Bbeta as a substrate of the tyrosine kinase
            JAK2 involved in growth hormone signaling
  JOURNAL   Mol Cell Biol 17 (11), 6633-6644 (1997)
   PUBMED   9343427
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Osborne,M.A., Dalton,S. and Kochan,J.P.
  TITLE     The yeast tribrid system--genetic detection of trans-phosphorylated
            ITAM-SH2-interactions
  JOURNAL   Biotechnology (N Y) 13 (13), 1474-1478 (1995)
   PUBMED   9636306
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF047577.1, U57391.1, AAHX01008496.1, BM389529.1 and AI029537.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF047577.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..670
                     /product="SH2B adapter protein 1 isoform 2"
                     /note="SH2B adapter protein 1; SH2 domain-containing
                     protein 1B; fceRI gamma-chain-interacting protein SH2-B;
                     SH2-B PH domain-containing signaling mediator 1"
                     /calculated_mol_wt=70732
     Region          1..555
                     /region_name="Interaction with JAK2 (low-affinity binding,
                     independent of JAK2 phosphorylation)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          24..85
                     /region_name="Required for self-association.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          26..81
                     /region_name="Phe_ZIP"
                     /note="Phenylalanine zipper; pfam08916"
                     /db_xref="CDD:462631"
     Region          85..196
                     /region_name="Interaction with RAC1.
                     /evidence=ECO:0000269|PubMed:11786545"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1 or MAPK3, in vitro.
                     /evidence=ECO:0000269|PubMed:10473609; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          100..243
                     /region_name="Required for NGF signaling"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          124..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          175..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          224..233
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          247..378
                     /region_name="PH_SH2B_family"
                     /note="SH2B adapter protein 1, 2, and 3 Pleckstrin
                     homology (PH) domain; cd01231"
                     /db_xref="CDD:269938"
     Region          262..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRF2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          418..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2 and PDGFR.
                     /evidence=ECO:0000269|PubMed:12551917; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          468..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2.
                     /evidence=ECO:0000269|PubMed:12551917; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          518..614
                     /region_name="SH2_SH2B_family"
                     /note="Src homology 2 (SH2) domain found in SH2B adapter
                     protein family; cd10346"
                     /db_xref="CDD:198209"
     Site            order(534,555,576,578)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198209"
     Site            order(577,604)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198209"
     CDS             1..670
                     /gene="Sh2b1"
                     /gene_synonym="Sh2-b; Sh2b; Sh2bpsm1"
                     /coded_by="NM_001048180.1:1..2013"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:89817"
                     /db_xref="RGD:620132"
ORIGIN      
        1 mngapspedg vfpsppalpp ppppswqefc esharaaald larrfrlyla shpqyaepga
       61 eaafsgrfae lflqhfeaev arasgslspp vlaplspgve ippshdlsle scrvggplav
      121 lgpsrssedl agplpssvss sttsskpklk krfslrsvgr svrgsvrgil qwrgavesps
      181 qagplettsg ppvlggnsns nssggagtvg ralandgtsp gerwthrfer lrlsrgggtl
      241 rdgagviqre ellsfmgaee aapdpagvgr gggaagltsg gggqpqwqkc rlllrsegeg
      301 gggsrleffv ppkasrprls ipcstitdvr tatalempdr entfvvkveg pseyilettd
      361 alhvkawvsd iqeclspgpc paisprpmtl plapgtsflt kdnteslelp clnhseslps
      421 qdlllgpses ndrlsqgayg glsdrpsasf spssasiaas hfdsmellpp elppripiee
      481 gppagtvhpl stpyppldtp eaatgsflfq geaeggegdq plsgypwfhg mlsrlkaaql
      541 vleggtsshg vflvrqsetr rgeyvltfnf qgkakhlrls lneegqcrvq hlwfqsifdm
      601 lehfrvhpip lesggssdvv lvsyvpsqrq qgreqagsha gvcegdrcyp dasstllpfg
      661 asdcvtehlp
//
LOCUS       NP_001025192             115 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein P2 [Rattus norvegicus].
ACCESSION   NP_001025192 XP_215116
VERSION     NP_001025192.1
DBSOURCE    REFSEQ: accession NM_001030021.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Mikula,M., Dzwonek,A., Karczmarski,J., Rubel,T., Dadlez,M.,
            Wyrwicz,L.S., Bomsztyk,K. and Ostrowski,J.
  TITLE     Landscape of the hnRNP K protein-protein interactome
  JOURNAL   Proteomics 6 (8), 2395-2406 (2006)
   PUBMED   16518874
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Furukawa,T., Uchiumi,T., Tokunaga,R. and Taketani,S.
  TITLE     Ribosomal protein P2, a novel iron-binding protein
  JOURNAL   Arch Biochem Biophys 298 (1), 182-186 (1992)
   PUBMED   1524426
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Chan,Y.L. and Wool,I.G.
  TITLE     The structure of a gene containing introns and encoding rat
            ribosomal protein P2
  JOURNAL   Nucleic Acids Res 19 (18), 4895-4900 (1991)
   PUBMED   1923757
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Wool,I.G., Chan,Y.L., Gluck,A. and Suzuki,K.
  TITLE     The primary structure of rat ribosomal proteins P0, P1, and P2 and
            a proposal for a uniform nomenclature for mammalian and yeast
            ribosomal proteins
  JOURNAL   Biochimie 73 (7-8), 861-870 (1991)
   PUBMED   1742361
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Ikeda,M., Saito,T., Endo,T., Tsurugi,K. and Onaya,T.
  TITLE     Thyrotropin stimulates the expression of an acidic ribosomal
            protein, P0, messenger ribonucleic acid in cultured rat thyroid
            (FRTL) cells
  JOURNAL   Endocrinology 128 (5), 2540-2547 (1991)
   PUBMED   1850354
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099697.1.
            
            On Aug 5, 2005 this sequence version replaced XP_215116.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099697.1, FQ217658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..115
                     /product="large ribosomal subunit protein P2"
                     /note="60S acidic ribosomal protein P2; ribosomal protein,
                     large P2; 60S acidic ribosomal protein P2-like"
                     /calculated_mol_wt=11561
     Region          1..>66
                     /region_name="Ribosomal_P2"
                     /note="Ribosomal protein P2. This subfamily represents the
                     eukaryotic large ribosomal protein P2. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P2 is located in
                     the L12 stalk, with proteins...; cd05833"
                     /db_xref="CDD:100111"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Region          76..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02401.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05387; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02401.2)"
     CDS             1..115
                     /gene="Rplp2"
                     /gene_synonym="RP2"
                     /coded_by="NM_001030021.1:45..392"
                     /db_xref="GeneID:140662"
                     /db_xref="RGD:621775"
ORIGIN      
        1 mryvasylla alggnsnpsa kdikkildsv gieadderln kviselngkn iedviaqgvg
       61 klasvpagga vavsaapgsa apaagsapaa aeekkdekke eseesdddmg fglfd
//
LOCUS       NP_001008319             436 aa            linear   ROD 27-APR-2025
DEFINITION  protein arginine methyltransferase NDUFAF7, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_001008319 XP_216627
VERSION     NP_001008319.1
DBSOURCE    REFSEQ: accession NM_001008318.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Zurita Rendon,O., Silva Neiva,L., Sasarman,F. and Shoubridge,E.A.
  TITLE     The arginine methyltransferase NDUFAF7 is essential for complex I
            assembly and early vertebrate embryogenesis
  JOURNAL   Hum Mol Genet 23 (19), 5159-5170 (2014)
   PUBMED   24838397
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Rhein,V.F., Carroll,J., Ding,S., Fearnley,I.M. and Walker,J.E.
  TITLE     NDUFAF7 methylates arginine 85 in the NDUFS2 subunit of human
            complex I
  JOURNAL   J Biol Chem 288 (46), 33016-33026 (2013)
   PUBMED   24089531
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Carilla-Latorre,S., Gallardo,M.E., Annesley,S.J., Calvo-Garrido,J.,
            Grana,O., Accari,S.L., Smith,P.K., Valencia,A., Garesse,R.,
            Fisher,P.R. and Escalante,R.
  TITLE     MidA is a putative methyltransferase that is required for
            mitochondrial complex I function
  JOURNAL   J Cell Sci 123 (Pt 10), 1674-1683 (2010)
   PUBMED   20406883
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083810.1.
            
            On Dec 16, 2004 this sequence version replaced XP_216627.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083810.1, SRR8487226.103227.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..436
                     /product="protein arginine methyltransferase NDUFAF7,
                     mitochondrial precursor"
                     /EC_number="2.1.1.320"
                     /note="protein midA homolog, mitochondrial; NADH
                     dehydrogenase [ubiquinone] complex I, assembly factor 7;
                     NADH dehydrogenase (ubiquinone) complex I, assembly factor
                     7; protein arginine methyltransferase NDUFAF7,
                     mitochondrial"
                     /calculated_mol_wt=44055
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5XI79.1)"
                     /calculated_mol_wt=4679
     Region          34..402
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
     mat_peptide     42..436
                     /product="Protein arginine methyltransferase NDUFAF7,
                     mitochondrial. /id=PRO_0000315674"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI79.1)"
                     /calculated_mol_wt=44055
     Region          413..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI79.1)"
     CDS             1..436
                     /gene="Ndufaf7"
                     /gene_synonym="RGD1311578"
                     /coded_by="NM_001008318.1:19..1329"
                     /db_xref="GeneID:298748"
                     /db_xref="RGD:1311578"
ORIGIN      
        1 mnalvrrcva rtgipsiwrr kcfssgnepa esnhvtpmlr hlmykikstg pitvaeymke
       61 vltnpakgyy vhhdmlgekg dfitspeisq ifgellgvwf vsewmasgks tafqlvelgp
      121 grgtltadil rvfsqlgsvl ktcdisihlv evsqklseiq altlteetvp lerdaeslvy
      181 mkgvtksgip iswyrdlkdv ptgysfylah effdvlpvhk fqktphgwre vfvdidpqsp
      241 dklrfvlapc atpaeafiqr derrehvevc pdagvviqel sqriastgga aliadyghdg
      301 tktdtlrgfy ehqlhdvlta pgtadltadv dfsylrrmaq grvaslgpve qrtflknmgi
      361 dvrlkvlldk agdpslqqql lrgydmlmnp qkmgerfhff allphqrlhv gsqggkacqs
      421 eapstsvpgf delvwh
//
LOCUS       NP_036740                750 aa            linear   ROD 27-APR-2025
DEFINITION  neprilysin [Rattus norvegicus].
ACCESSION   NP_036740
VERSION     NP_036740.1
DBSOURCE    REFSEQ: accession NM_012608.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Vasilev,D., Dubrovskaya,N.M. and Nalivaeva,N.N.
  TITLE     Caspase Inhibition Restores NEP Expression and Rescues Olfactory
            Deficit in Rats Caused by Prenatal Hypoxia
  JOURNAL   J Mol Neurosci 72 (7), 1516-1526 (2022)
   PUBMED   35344141
  REMARK    GeneRIF: Caspase Inhibition Restores NEP Expression and Rescues
            Olfactory Deficit in Rats Caused by Prenatal Hypoxia.
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Vasilev,D.S., Dubrovskaya,N.M., Zhuravin,I.A. and Nalivaeva,N.N.
  TITLE     Developmental Profile of Brain Neprilysin Expression Correlates
            with Olfactory Behaviour of Rats
  JOURNAL   J Mol Neurosci 71 (9), 1772-1785 (2021)
   PUBMED   33433852
  REMARK    GeneRIF: Developmental Profile of Brain Neprilysin Expression
            Correlates with Olfactory Behaviour of Rats.
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Dominguez-Vias,G., Aretxaga-Maza,G., Prieto,I., Segarra,A.B.,
            Luna,J.D., Gasparo,M. and Ramirez-Sanchez,M.
  TITLE     Light-dark influence on enkephalinase activity in hypothalamus and
            pituitary
  JOURNAL   Neuro Endocrinol Lett 39 (4), 277-280 (2018)
   PUBMED   30531704
  REMARK    GeneRIF: In standard light/dark conditions, the results
            demonstrated an opposite daily rhythm in hypothalamus and
            pituitary. While the highest levels of AlaAP or enkephalinase
            activities were measured in hypothalamus during the dark period,
            they were the highest in the pituitary during the light one.
REFERENCE   4  (residues 1 to 750)
  AUTHORS   de Oliveira,R.W., Julian,G.S., Perry,J.C., Tufik,S. and Chagas,J.R.
  TITLE     Chronic intermittent hypoxia induces changes on the expression and
            activity of neprilysin (EC 3.4.24.11) in the brain of rats
  JOURNAL   Neurosci Lett 678, 43-47 (2018)
   PUBMED   29702204
  REMARK    GeneRIF: Study shows that chronic intermittent hypoxia (CIH)
            induces changes on the expression and activity of neprilysin (NEP)
            in the brain of rats. Data show that CIH protocol increases the
            expression and activity of NEP selectively in the temporal cortex.
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Liu,C.X., Tan,L., Sun,F.R., Zhang,W., Miao,D., Tan,M.S., Wan,Y.,
            Tan,C.C., Yu,J.T. and Tan,L.
  TITLE     The Association of MME microRNA Binding Site Polymorphism with the
            Risk of Late Onset Alzheimer's Disease in Northern Han Chinese
  JOURNAL   Curr Neurovasc Res 14 (2), 90-95 (2017)
   PUBMED   28294061
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Dutriez,I., Sales,N., Fournie-Zaluski,M.C. and Roques,B.P.
  TITLE     Pre- and post-natal ontogeny of neutral endopeptidase 24-11
            ('enkephalinase') studied by in vitro autoradiography in the rat
  JOURNAL   Experientia 48 (3), 290-300 (1992)
   PUBMED   1547865
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Yandle,T.G., Brennan,S.O., Espiner,E.A., Nicholls,M.G. and
            Richards,A.M.
  TITLE     Endopeptidase-24.11 in human plasma degrades atrial natriuretic
            factor (ANF) to ANF(99-105/106-126)
  JOURNAL   Peptides 10 (4), 891-894 (1989)
   PUBMED   2531377
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Bateman,R.C. Jr., Jackson,D., Slaughter,C.A., Unnithan,S.,
            Chai,Y.G., Moomaw,C. and Hersh,L.B.
  TITLE     Identification of the active-site arginine in rat neutral
            endopeptidase 24.11 (enkephalinase) as arginine 102 and analysis of
            a glutamine 102 mutant
  JOURNAL   J Biol Chem 264 (11), 6151-6157 (1989)
   PUBMED   2703483
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Shipp,M.A., Vijayaraghavan,J., Schmidt,E.V., Masteller,E.L.,
            D'Adamio,L., Hersh,L.B. and Reinherz,E.L.
  TITLE     Common acute lymphoblastic leukemia antigen (CALLA) is active
            neutral endopeptidase 24.11 ('enkephalinase'): direct evidence by
            cDNA transfection analysis
  JOURNAL   Proc Natl Acad Sci U S A 86 (1), 297-301 (1989)
   PUBMED   2521388
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Marcais-Collado,H., Uchida,G., Costentin,J., Schwartz,J.C. and
            Lecomte,J.M.
  TITLE     Naloxone-reversible antidiarrheal effects of enkephalinase
            inhibitors
  JOURNAL   Eur J Pharmacol 144 (2), 125-132 (1987)
   PUBMED   3481337
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085753.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085753.1, SRR8487227.322012.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..750
                     /product="neprilysin"
                     /EC_number="3.4.24.11"
                     /note="membrane metallo-endopeptidase (neutral
                     endopeptidase/enkephalinase); atriopeptidase; neutral
                     endopeptidase 24.11; skin fibroblast elastase"
                     /calculated_mol_wt=85664
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08473; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Region          16..23
                     /region_name="Stop-transfer sequence.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07861.2)"
     Site            29..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07861.2)"
     Region          79..748
                     /region_name="M13"
                     /note="Peptidase family M13 includes neprilysin and
                     endothelin-converting enzyme I; cd08662"
                     /db_xref="CDD:341056"
     Site            order(107,537,542..545,564,580..581,584..585,588,647,690,
                     693..694,711..712,718)
                     /site_type="active"
                     /db_xref="CDD:341056"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P08473; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:3555489; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P08473; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P08473; propagated from
                     UniProtKB/Swiss-Prot (P07861.2)"
     CDS             1..750
                     /gene="Mme"
                     /gene_synonym="CD10; Nep; SFE"
                     /coded_by="NM_012608.2:129..2381"
                     /db_xref="GeneID:24590"
                     /db_xref="RGD:3098"
ORIGIN      
        1 mgrsesqmdi tdinapkpkk kqrwtpleis lsvlvlllti iavtmialya tyddgickss
       61 dciksaarli qnmdasaepc tdffkyacgg wlkrnvipet ssrysnfdil rdelevilkd
      121 vlqepktedi vavqkaktly rscinesaid srggqplltl lpdiygwpva sqnweqtygt
      181 swtaeksiaq lnskygkkvl inffvgtddk nstqhiihfd qprlglpsrd yyectgiyke
      241 actayvdfmi svarlirqeq rlpidenqls lemnkvmele keianattkp edrndpmlly
      301 nkmtlaklqn nfsleingkp fswsnftnei mstvniniqn eeevvvyape yltklkpilt
      361 kysprdlqnl mswrfimdlv sslsrnykes rnafrkalyg ttsetatwrr canyvngnme
      421 navgrlyvea afageskhvv edliaqirev fiqtlddltw mdaetkkkae ekalaikeri
      481 gypddiisne nklnneylel nykeeeyfen iiqnlkfsqs kqlkklrekv dkdewisgaa
      541 vvnafyssgr nqivfpagil qppffsarqs nslnyggigm vigheithgf ddngrnfnkd
      601 gdlvdwwtqq sannfkdqsq cmvyqygnft wdlaggqhln gintlgenia dnggigqayr
      661 ayqnyvkkng eekllpgldl nhkqlfflnf aqvwcgtyrp eyavnsiktd vhspgnfrii
      721 gtlqnsaefa dafhcrknsy mnperkcrvw
//
LOCUS       NP_113929                502 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 5
            [Rattus norvegicus].
ACCESSION   NP_113929 XP_001075869
VERSION     NP_113929.1
DBSOURCE    REFSEQ: accession NM_031741.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Minocha,E., Chaturvedi,C.P. and Nityanand,S.
  TITLE     Renogenic characterization and in vitro differentiation of rat
            amniotic fluid stem cells into renal proximal tubular- and
            juxtaglomerular-like cells
  JOURNAL   In Vitro Cell Dev Biol Anim 55 (2), 138-147 (2019)
   PUBMED   30645697
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Ebert,K., Ludwig,M., Geillinger,K.E., Schoberth,G.C.,
            Essenwanger,J., Stolz,J., Daniel,H. and Witt,H.
  TITLE     Reassessment of GLUT7 and GLUT9 as Putative Fructose and Glucose
            Transporters
  JOURNAL   J Membr Biol 250 (2), 171-182 (2017)
   PUBMED   28083649
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Nomura,N., Verdon,G., Kang,H.J., Shimamura,T., Nomura,Y.,
            Sonoda,Y., Hussien,S.A., Qureshi,A.A., Coincon,M., Sato,Y., Abe,H.,
            Nakada-Nakura,Y., Hino,T., Arakawa,T., Kusano-Arai,O., Iwanari,H.,
            Murata,T., Kobayashi,T., Hamakubo,T., Kasahara,M., Iwata,S. and
            Drew,D.
  TITLE     Structure and mechanism of the mammalian fructose transporter GLUT5
  JOURNAL   Nature 526 (7573), 397-401 (2015)
   PUBMED   26416735
  REMARK    GeneRIF: crystal structures of GLUT5 from Rattus norvegicus and Bos
            taurus in open outward- and open inward-facing conformations,
            respectively
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Patel,C., Douard,V., Yu,S., Gao,N. and Ferraris,R.P.
  TITLE     Transport, metabolism, and endosomal trafficking-dependent
            regulation of intestinal fructose absorption
  JOURNAL   FASEB J 29 (9), 4046-4058 (2015)
   PUBMED   26071406
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Suzuki,T., Douard,V., Mochizuki,K., Goda,T. and Ferraris,R.P.
  TITLE     Diet-induced epigenetic regulation in vivo of the intestinal
            fructose transporter Glut5 during development of rat small
            intestine
  JOURNAL   Biochem J 435 (1), 43-53 (2011)
   PUBMED   21222652
  REMARK    GeneRIF: investigation of influence of dietary carbohydrates on
            expression of Glut5 in small intestine: Glut5 mRNA increased with
            fructose perfusion and age, a pattern that matched that of Pol II
            binding and histone H3 acetylation at Glut5 promoter
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Hajduch,E., Litherland,G.J., Turban,S., Brot-Laroche,E. and
            Hundal,H.S.
  TITLE     Insulin regulates the expression of the GLUT5 transporter in L6
            skeletal muscle cells
  JOURNAL   FEBS Lett 549 (1-3), 77-82 (2003)
   PUBMED   12914929
  REMARK    GeneRIF: insulin is capable of increasing the abundance and
            functional activity of GLUT5 in skeletal muscle cells, most likely
            mediated via activation of the GLUT5 promoter
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Jiang,L., David,E.S., Espina,N. and Ferraris,R.P.
  TITLE     GLUT-5 expression in neonatal rats: crypt-villus location and
            age-dependent regulation
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 281 (3), G666-G674 (2001)
   PUBMED   11518678
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Darakhshan,F., Hajduch,E., Kristiansen,S., Richter,E.A. and
            Hundal,H.S.
  TITLE     Biochemical and functional characterization of the GLUT5 fructose
            transporter in rat skeletal muscle
  JOURNAL   Biochem J 336 (Pt 2) (Pt 2), 361-366 (1998)
   PUBMED   9820812
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Inukai,K., Asano,T., Katagiri,H., Ishihara,H., Anai,M.,
            Fukushima,Y., Tsukuda,K., Kikuchi,M., Yazaki,Y. and Oka,Y.
  TITLE     Cloning and increased expression with fructose feeding of rat
            jejunal GLUT5
  JOURNAL   Endocrinology 133 (5), 2009-2014 (1993)
   PUBMED   8404647
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Rand,E.B., Depaoli,A.M., Davidson,N.O., Bell,G.I. and Burant,C.F.
  TITLE     Sequence, tissue distribution, and functional characterization of
            the rat fructose transporter GLUT5
  JOURNAL   Am J Physiol 264 (6 Pt 1), G1169-G1176 (1993)
   PUBMED   8333543
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D13871.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001075869.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D13871.1, L05195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..502
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 5"
                     /note="solute carrier family 2 (facilitated glucose
                     transporter), member 5; GLUT-5; fructose transporter;
                     glucose transporter type 5, small intestine; solute
                     carrier family 2 (facilitated glucose/fructose
                     transporter), member 5"
                     /calculated_mol_wt=55428
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P22732; propagated from
                     UniProtKB/Swiss-Prot (P43427.1)"
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Region          19..470
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(31,35,166,169..170,173,287..288,292..293,296..297,
                     324,386..387,390..391,395,418..419,422)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43427.1)"
     Site            68..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            126..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            161..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            342..362
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            371..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            412..432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     Site            439..459
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43427.1)"
     CDS             1..502
                     /gene="Slc2a5"
                     /coded_by="NM_031741.1:43..1551"
                     /db_xref="GeneID:65197"
                     /db_xref="RGD:68328"
ORIGIN      
        1 mekedqektg kltlvlalat flaafgssfq ygynvaavns psefmqqfyn dtyydrnken
       61 iesftltllw sltvsmfpfg gfigslmvgf lvnnlgrkga llfnnifsil pailmgcski
      121 aksfeiiias rllvgicagi ssnvvpmylg elapknlrga lgvvpqlfit vgilvaqlfg
      181 lrsvlaseeg wpillgltgv paglqllllp ffpespryll iqkknesaae kalqtlrgwk
      241 dvdmemeeir kedeaekaag fisvwklfrm qslrwqlist ivlmtgqqls gvnaiyyyad
      301 qiylsagvks ndvqyvtagt gavnvfmtmv tvfvvelwgr rnllligfst cltacivltv
      361 alalqntisw mpyvsivcvi vyvighavgp spipalfite iflqssrpsa ymiggsvhwl
      421 snfivglifp fiqvglgpys fiifaiicll tsiyifmvvp etkgrtfvei nqifakknkv
      481 sdvypekeek elndlppatr eq
//
LOCUS       NP_077357                524 aa            linear   ROD 27-APR-2025
DEFINITION  glycerol kinase [Rattus norvegicus].
ACCESSION   NP_077357 XP_346875
VERSION     NP_077357.2
DBSOURCE    REFSEQ: accession NM_024381.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Parr,L.S., Sriram,G., Nazarian,R., Rahib,L. and Dipple,K.M.
  TITLE     The ATP-stimulated translocation promoter (ASTP) activity of
            glycerol kinase plays central role in adipogenesis
  JOURNAL   Mol Genet Metab 124 (4), 254-265 (2018)
   PUBMED   29960856
  REMARK    GeneRIF: To further elucidate the contributions of the enzymatic
            (phosphorylation) and alternative (ASTP) functions of GK in
            adipogenesis, we performed experiments on mammalian GK and E. coli
            GK. We determined that the ASTP function of GK (which is absent in
            E. coli GK) plays a greater role than the enzymatic activity in
            these processes.
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Kosuga,M., Henderson-MacLennan,N.K., Zhang,Y.H., Huang,B.L.,
            Dipple,K.M. and McCabe,E.R.
  TITLE     Glycerol homeostasis and metabolism in glycerol kinase carrier mice
  JOURNAL   Mol Genet Metab 103 (3), 297-299 (2011)
   PUBMED   21536471
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Sriram,G., Parr,L.S., Rahib,L., Liao,J.C. and Dipple,K.M.
  TITLE     Moonlighting function of glycerol kinase causes systems-level
            changes in rat hepatoma cells
  JOURNAL   Metab Eng 12 (4), 332-340 (2010)
   PUBMED   20399282
  REMARK    GeneRIF: This systems biology approach further emphasizes glucose
            kinase's essential role in central and lipid metabolism and
            experimentally verifies lucose kinase's alternative function of
            affecting glucocorticoid receptor transcription factor activity.
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Okamoto,K., Hirano,H. and Isohashi,F.
  TITLE     Molecular cloning of rat liver glucocorticoid-receptor
            translocation promoter
  JOURNAL   Biochem Biophys Res Commun 193 (3), 848-854 (1993)
   PUBMED   8323560
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Walker,A.P., Muscatelli,F. and Monaco,A.P.
  TITLE     Isolation of the human Xp21 glycerol kinase gene by positional
            cloning
  JOURNAL   Hum Mol Genet 2 (2), 107-114 (1993)
   PUBMED   8499898
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Okamoto,K., Isohashi,F., Ueda,K. and Sakamoto,Y.
  TITLE     Properties of an adenosine triphosphate-stimulated factor that
            enhances the nuclear binding of activated glucocorticoid-receptor
            complex: binding to histone-agarose
  JOURNAL   Endocrinology 124 (2), 675-680 (1989)
   PUBMED   2912694
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Seltzer,W.K. and McCabe,E.R.
  TITLE     Human and rat adrenal glycerol kinase: subcellular distribution and
            bisubstrate kinetics
  JOURNAL   Mol Cell Biochem 62 (1), 43-50 (1984)
   PUBMED   6330523
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Jenkins,B.T. and Hajra,A.K.
  TITLE     Glycerol kinase and dihydroxyacetone kinase in rat brain
  JOURNAL   J Neurochem 26 (2), 377-385 (1976)
   PUBMED   3631
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16102.1, CO564445.1, CO557097.1 and JAXUCZ010000021.1.
            
            On Oct 12, 2007 this sequence version replaced NP_077357.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.21438.1,
                                           SRR26643429.59037.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..524
                     /product="glycerol kinase"
                     /EC_number="2.7.1.30"
                     /note="glycerokinase; ATP:glycerol 3-phosphotransferase;
                     ATP-stimulated glucocorticoid-receptor translocation
                     promoter; ATP-stimulated glucocorticoid-receptor
                     translocaton promoter"
                     /calculated_mol_wt=57332
     Region          11..510
                     /region_name="ASKHA_NBD_FGGY_GK1-3-like"
                     /note="nucleotide-binding domain (NBD) of metazoan
                     glycerol kinase 1-3 (GK1-3) and similar proteins; cd07792"
                     /db_xref="CDD:466802"
     CDS             1..524
                     /gene="Gk"
                     /gene_synonym="ASTP; Gyk"
                     /coded_by="NM_024381.2:97..1671"
                     /db_xref="GeneID:79223"
                     /db_xref="RGD:70893"
ORIGIN      
        1 maaakkavlg plvgavdqgt sstrflvfns ktaellshhq veikqefpre gwveqdpkei
       61 lqsvyeciek tceklgqlni disnikaigv snqrettvvw dkltgeplyn avvwldlrtq
      121 stveklskri pgnnnfvksk tglplstyfs avklrwlldn vkkvqeavee nralfgtids
      181 wliwsltggi nggvhctdvt nasrtmlfni hslewdkelc effgipmeil pnvrssseiy
      241 glmkagaleg vpisgclgdq saalvgqmcf qdgqakntyg tgcfllcntg hkcvfsehgl
      301 lttvayklgr dkpvyyaleg svaiagavir wlrdnlgiik sseeieklak evgtsygcyf
      361 vpafsglyap ywepsargii cgltqftnkc hiafaaleav cfqtreilda mnrdcgipls
      421 hlqvdggmts nkilmqlqad ilyipvvkps mpettalgaa maagaaegvg vwslepedls
      481 avtmerfepq inaeeseiry stwkkavmks igwvttqspe sgip
//
LOCUS       NP_001071143             477 aa            linear   ROD 27-APR-2025
DEFINITION  tripartite motif-containing protein 72 [Rattus norvegicus].
ACCESSION   NP_001071143 XP_001080388 XP_344968
VERSION     NP_001071143.1
DBSOURCE    REFSEQ: accession NM_001077675.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Zhu,X.Z., Wang,J.Q. and Wu,Y.H.
  TITLE     MG53 ameliorates nerve injury induced neuropathic pain through the
            regulation of Nrf2/HO-1 signaling in rats
  JOURNAL   Behav Brain Res 449, 114489 (2023)
   PUBMED   37169128
  REMARK    GeneRIF: MG53 ameliorates nerve injury induced neuropathic pain
            through the regulation of Nrf2/HO-1 signaling in rats.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Huang,L.T., Chou,H.C. and Chen,C.M.
  TITLE     TRIM72 mediates lung epithelial cell death upon hyperoxia exposure
  JOURNAL   J Chin Med Assoc 84 (1), 79-86 (2021)
   PUBMED   32796321
  REMARK    GeneRIF: TRIM72 mediates lung epithelial cell death upon hyperoxia
            exposure.
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Liu,W., Wang,G., Zhang,C., Ding,W., Cheng,W., Luo,Y., Wei,C. and
            Liu,J.
  TITLE     MG53, A Novel Regulator of KChIP2 and Ito,f, Plays a Critical Role
            in Electrophysiological Remodeling in Cardiac Hypertrophy
  JOURNAL   Circulation 139 (18), 2142-2156 (2019)
   PUBMED   30760025
  REMARK    GeneRIF: These findings establish MG53 as a novel regulator of
            KChIP2 and Ito,f by modulating NF-kappaB activity and reveal its
            critical role in electrophysiological remodeling in cardiac
            hypertrophy.
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Guo,J., Jia,F., Jiang,Y., Li,Q., Yang,Y., Xiao,M. and Xiao,H.
  TITLE     Potential role of MG53 in the regulation of
            transforming-growth-factor-beta1-induced atrial fibrosis and
            vulnerability to atrial fibrillation
  JOURNAL   Exp Cell Res 362 (2), 436-443 (2018)
   PUBMED   29233682
  REMARK    GeneRIF: This suggests that MG53 is a potential regulator of atrial
            fibrosis induced by the TGF-beta1/Smad pathway in patients with
            atrial fibrillation .
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Qi,J., Yang,B., Ren,C., Fu,J. and Zhang,J.
  TITLE     Swimming Exercise Alleviated Insulin Resistance by Regulating
            Tripartite Motif Family Protein 72 Expression and AKT Signal
            Pathway in Sprague-Dawley Rats Fed with High-Fat Diet
  JOURNAL   J Diabetes Res 2016, 1564386 (2016)
   PUBMED   27843952
  REMARK    GeneRIF: These results suggest that an 8-week swimming exercise
            improves HFD-induced insulin resistance maybe through a reduction
            of TRIM72 in skeletal muscle and enhancement of AKT signal
            transduction.
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Yi,J.S., Park,J.S., Ham,Y.M., Nguyen,N., Lee,N.R., Hong,J.,
            Kim,B.W., Lee,H., Lee,C.S., Jeong,B.C., Song,H.K., Cho,H.,
            Kim,Y.K., Lee,J.S., Park,K.S., Shin,H., Choi,I., Lee,S.H.,
            Park,W.J., Park,S.Y., Choi,C.S., Lin,P., Karunasiri,M., Tan,T.,
            Duann,P., Zhu,H., Ma,J. and Ko,Y.G.
  TITLE     MG53-induced IRS-1 ubiquitination negatively regulates skeletal
            myogenesis and insulin signalling
  JOURNAL   Nat Commun 4, 2354 (2013)
   PUBMED   23965929
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Cao,C.M., Zhang,Y., Weisleder,N., Ferrante,C., Wang,X., Lv,F.,
            Zhang,Y., Song,R., Hwang,M., Jin,L., Guo,J., Peng,W., Li,G.,
            Nishi,M., Takeshima,H., Ma,J. and Xiao,R.P.
  TITLE     MG53 constitutes a primary determinant of cardiac ischemic
            preconditioning
  JOURNAL   Circulation 121 (23), 2565-2574 (2010)
   PUBMED   20516375
  REMARK    GeneRIF: MG53, a member of the muscle-specific transmembrane
            adaptor molecule (TRIM) protein family, is a crucial component of
            the cardiac ischemic preconditioning response.
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Cai,C., Weisleder,N., Ko,J.K., Komazaki,S., Sunada,Y., Nishi,M.,
            Takeshima,H. and Ma,J.
  TITLE     Membrane repair defects in muscular dystrophy are linked to altered
            interaction between MG53, caveolin-3, and dysferlin
  JOURNAL   J Biol Chem 284 (23), 15894-15902 (2009)
   PUBMED   19380584
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Cai,C., Masumiya,H., Weisleder,N., Pan,Z., Nishi,M., Komazaki,S.,
            Takeshima,H. and Ma,J.
  TITLE     MG53 regulates membrane budding and exocytosis in muscle cells
  JOURNAL   J Biol Chem 284 (5), 3314-3322 (2009)
   PUBMED   19029292
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Cai,C., Masumiya,H., Weisleder,N., Matsuda,N., Nishi,M., Hwang,M.,
            Ko,J.K., Lin,P., Thornton,A., Zhao,X., Pan,Z., Komazaki,S.,
            Brotto,M., Takeshima,H. and Ma,J.
  TITLE     MG53 nucleates assembly of cell membrane repair machinery
  JOURNAL   Nat Cell Biol 11 (1), 56-64 (2009)
   PUBMED   19043407
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127539.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_344968.2, XP_001080388.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127539.1, FQ224850.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..477
                     /product="tripartite motif-containing protein 72"
                     /EC_number="2.3.2.27"
                     /note="mg53; mitsugumin-53; tripartite motif containing
                     72, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=52701
     Region          8..68
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(14,17,29,31,34,37,53,56)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          84..125
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <136..>253
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0JPQ4.1)"
     Region          278..470
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..477
                     /gene="Trim72"
                     /gene_synonym="RGD1562778"
                     /coded_by="NM_001077675.1:89..1522"
                     /db_xref="GeneID:365377"
                     /db_xref="RGD:1562778"
ORIGIN      
        1 mstapgllrq elscplclql fdapvtaecg hsfcraclir vagepaddgt vacpccqast
       61 rpqalstnlq larlveglaq vpqghceehl dplsiyceqd rtlvcgvcas lgshrghrll
      121 paaeaharlk tqlpqqkaql qeacmrkeks vavlehqlve veetvrqfrg avgeqlgkmr
      181 mflaalessl dreaervrge agvalrrels slnsyleqlr qmekvleeva dkpqteflmk
      241 fclvtsrlqk ilsespppar ldiqlpvisd dfkfqvwkkm fralmpelee ltfdpssahp
      301 slvvsasgrr vecseqkapp agedtcqfdk tvavvakqll sqgehyweve vgdkprwalg
      361 vmaadasrrg rlhavpsqgl wllglrdgki leahveakep ralrtperpp ariglylsfa
      421 dgvltfydas ntdaltplfs fherlpgpvy pmfdvcwhdk gknsqplllv gpdseqa
//
LOCUS       NP_511178                290 aa            linear   ROD 27-APR-2025
DEFINITION  enoyl-CoA hydratase, mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_511178
VERSION     NP_511178.1
DBSOURCE    REFSEQ: accession NM_078623.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Yamada,K., Aiba,K., Kitaura,Y., Kondo,Y., Nomura,N., Nakamura,Y.,
            Fukushi,D., Murayama,K., Shimomura,Y., Pitt,J., Yamaguchi,S.,
            Yokochi,K. and Wakamatsu,N.
  TITLE     Clinical, biochemical and metabolic characterisation of a mild form
            of human short-chain enoyl-CoA hydratase deficiency: significance
            of increased N-acetyl-S-(2-carboxypropyl)cysteine excretion
  JOURNAL   J Med Genet 52 (10), 691-698 (2015)
   PUBMED   26251176
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Zhang,X., Yang,J., Guo,Y., Ye,H., Yu,C., Xu,C., Xu,L., Wu,S.,
            Sun,W., Wei,H., Gao,X., Zhu,Y., Qian,X., Jiang,Y., Li,Y. and He,F.
  TITLE     Functional proteomic analysis of nonalcoholic fatty liver disease
            in rat models: enoyl-coenzyme a hydratase down-regulation
            exacerbates hepatic steatosis
  JOURNAL   Hepatology 51 (4), 1190-1199 (2010)
   PUBMED   20162621
  REMARK    GeneRIF: enoyl-coenzyme a hydratase down-regulation exacerbates
            hepatic steatosis.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Feng,Y., Hofstein,H.A., Zwahlen,J. and Tonge,P.J.
  TITLE     Effect of mutagenesis on the stereochemistry of enoyl-CoA hydratase
  JOURNAL   Biochemistry 41 (42), 12883-12890 (2002)
   PUBMED   12379132
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Engel,C.K., Kiema,T.R., Hiltunen,J.K. and Wierenga,R.K.
  TITLE     The crystal structure of enoyl-CoA hydratase complexed with
            octanoyl-CoA reveals the structural adaptations required for
            binding of a long chain fatty acid-CoA molecule
  JOURNAL   J Mol Biol 275 (5), 847-859 (1998)
   PUBMED   9480773
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Engel,C.K., Mathieu,M., Zeelen,J.P., Hiltunen,J.K. and
            Wierenga,R.K.
  TITLE     Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5
            angstroms resolution: a spiral fold defines the CoA-binding pocket
  JOURNAL   EMBO J 15 (19), 5135-5145 (1996)
   PUBMED   8895557
REFERENCE   7  (residues 1 to 290)
  AUTHORS   D'Ordine,R.L., Bahnson,B.J., Tonge,P.J. and Anderson,V.E.
  TITLE     Enoyl-coenzyme A hydratase-catalyzed exchange of the alpha-protons
            of coenzyme A thiol esters: a model for an enolized intermediate in
            the enzyme-catalyzed elimination?
  JOURNAL   Biochemistry 33 (49), 14733-14742 (1994)
   PUBMED   7993901
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Minami-Ishii,N., Taketani,S., Osumi,T. and Hashimoto,T.
  TITLE     Molecular cloning and sequence analysis of the cDNA for rat
            mitochondrial enoyl-CoA hydratase. Structural and evolutionary
            relationships linked to the bifunctional enzyme of the peroxisomal
            beta-oxidation system
  JOURNAL   Eur J Biochem 185 (1), 73-78 (1989)
   PUBMED   2806264
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC064655.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064655.1, X15958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..290
                     /product="enoyl-CoA hydratase, mitochondrial precursor"
                     /EC_number="5.3.3.8"
                     /EC_number="4.2.1.17"
                     /note="mitochondrial short-chain enoyl-coenzyme A
                     hydratase 1; enoyl-CoA hydratase, mitochondrial; SCEH;
                     enoyl-CoA hydratase 1; short-chain enoyl-CoA hydratase;
                     enoyl Coenzyme A hydratase, short chain 1; enoyl-CoA
                     hydratase, mitochondrial-like; Enoyl-CoA hydratase, short
                     chain 1, mitochondrial; enoyl Coenzyme A hydratase, short
                     chain, 1, mitochondrial; enoyl CoA hydratase, short chain,
                     1, mitochondrial"
                     /calculated_mol_wt=28288
     transit_peptide 1..29
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:2806264; propagated from
                     UniProtKB/Swiss-Prot (P14604.1)"
                     /calculated_mol_wt=3247
     mat_peptide     30..290
                     /product="Enoyl-CoA hydratase, mitochondrial.
                     /id=PRO_0000007414"
                     /note="propagated from UniProtKB/Swiss-Prot (P14604.1)"
                     /calculated_mol_wt=28288
     Region          32..288
                     /region_name="crotonase-like"
                     /note="Crotonase/Enoyl-Coenzyme A (CoA) hydratase
                     superfamily. This superfamily contains a diverse set of
                     enzymes including enoyl-CoA hydratase, napthoate synthase,
                     methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA
                     dehydratase, and dienoyl-CoA isomerase; cl23717"
                     /db_xref="CDD:474030"
     Site            order(58,60,92,96..100,137,139..141,163..164,167)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119339"
     Site            order(98,141)
                     /site_type="active"
                     /note="oxyanion hole (OAH) forming residues [active]"
                     /db_xref="CDD:119339"
     Site            101
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BH95; propagated from
                     UniProtKB/Swiss-Prot (P14604.1)"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BH95; propagated from
                     UniProtKB/Swiss-Prot (P14604.1)"
     Site            order(121,129,150..153,165..168,174,176..178,180..181,
                     186..187,189..190,192..193,196,207,210,225,228..229)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:119339"
     Site            164
                     /site_type="other"
                     /note="Important for catalytic activity; propagated from
                     UniProtKB/Swiss-Prot (P14604.1)"
     Site            211
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BH95; propagated from
                     UniProtKB/Swiss-Prot (P14604.1)"
     CDS             1..290
                     /gene="Echs1"
                     /gene_synonym="mECH; mECH1"
                     /coded_by="NM_078623.2:18..890"
                     /db_xref="GeneID:140547"
                     /db_xref="RGD:69330"
ORIGIN      
        1 maalrallpr acnsllspvr cpefrrfasg anfqyiitek kgknssvgli qlnrpkalna
       61 lcnglieeln qaletfeedp avgaivltgg ekafaagadi kemqnrtfqd cysgkflshw
      121 dhitrikkpv iaavngyalg ggcelammcd iiyagekaqf gqpeillgti pgaggtqrlt
      181 ravgkslame mvltgdrisa qdakqaglvs kifpvetlve eaiqcaekia nnskiivama
      241 kesvnaafem tltegnklek klfystfatd drregmsafv ekrkanfkdh
//
LOCUS       NP_001034297             528 aa            linear   ROD 27-APR-2025
DEFINITION  protein spinster homolog 1 [Rattus norvegicus].
ACCESSION   NP_001034297 XP_341928
VERSION     NP_001034297.2
DBSOURCE    REFSEQ: accession NM_001039208.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK604160.1, CA339235.1, BU671623.1 and BC087072.1.
            
            On Apr 18, 2009 this sequence version replaced NP_001034297.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..528
                     /product="protein spinster homolog 1"
                     /note="spinster homolog 1; SPNS sphingolipid transporter
                     1; RSpin1"
                     /calculated_mol_wt=56665
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2V7; propagated from
                     UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Region          62..479
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(72..73,76..77,80,112,164..165,167..169,172,192,
                     195..196,199,280,283..284,287..289,292,333,337,390..391,
                     395,399,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            465..485
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2YDU8.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2V7; propagated from
                     UniProtKB/Swiss-Prot (Q2YDU8.2)"
     CDS             1..528
                     /gene="Spns1"
                     /gene_synonym="RGD1305613"
                     /coded_by="NM_001039208.2:347..1933"
                     /db_xref="GeneID:361648"
                     /db_xref="RGD:1305613"
ORIGIN      
        1 magsdtapfl sqaddpddgp apghpglpgp mgnpksgele vpdceglqri tglsrghstl
       61 ivvvlcyinl lnymdrftva gvltdieqff nigdgstgli qtvfissymv lapvfgylgd
      121 rynrkylmcg giafwslvtl gssfiprehf wlllltrglv gvgeasysti aptliadlfv
      181 adqrsrmlsi fyfaipvgsg lgyiagskvk dlagdwhwal rvtpglgvla vlllflvvqe
      241 pprgaverhs gspplsptsw wadlkalarn psfvlsslgf tavafvtgsl alwapafllr
      301 srvvlgetpp clpgdscsss dslifglitc ltgvlgvglg veisrrlrrf npradplvca
      361 agllgsspfl flslacargs ivatyififi getllsmnwa ivadillyvv iptrrstaea
      421 fqivlshllg dagspyligl isdrlrrswp psflsefral qfslmlcafv galggaaflg
      481 tamfiendrr raqlhvqgll hetepsddqi vvpqrgrstr vpvssvli
//
LOCUS       NP_001014214             492 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 39B [Rattus norvegicus].
ACCESSION   NP_001014214 XP_342928
VERSION     NP_001014214.1
DBSOURCE    REFSEQ: accession NM_001014192.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082025.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342928.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..492
                     /product="transmembrane protein 39B"
                     /calculated_mol_wt=56244
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H44.1)"
     Region          48..478
                     /region_name="Tmp39"
                     /note="Putative transmembrane protein; pfam10271"
                     /db_xref="CDD:463038"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            153..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            322..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     Site            447..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H44.1)"
     CDS             1..492
                     /gene="Tmem39b"
                     /coded_by="NM_001014192.1:103..1581"
                     /db_xref="GeneID:362608"
                     /db_xref="RGD:1359450"
ORIGIN      
        1 mggrrgpnrt syyrnplcep gssgasgggh sssasvssvr srsrttsgtg lsspplaaqt
       61 vvplqhckip elpvqasilf elqlffcqli alfvhyiniy ktvwwyppsh ppshtslnfh
      121 lidfnllmvt tivlgrrfig sivkeasqrg kvslfrsill fltrftvlta tgwslcrsli
      181 hlfrtysfln llflcypfgm yipflqlnyd lrktnlfshv asmgpreavs glarsrdyfl
      241 tlretwkqht rqlygpeamp thacclspsl irneveflkm dfnwrmkevl vssmlsayyv
      301 afvpvwfvkn thyydkrwsc elfllvsist svilmqhllp asycdllhka aahlgcwqkv
      361 dpalcsnvlq hpwteecmwp qgvlvkhskn vykalghynv aipsdvshfr fhfffsnplr
      421 ilnilllleg avivyqlysl mssekwhqti slalilfsny yaffkllrdr lvlgkaysys
      481 aspqrdldhr fs
//
LOCUS       NP_068532                508 aa            linear   ROD 27-APR-2025
DEFINITION  ranBP-type and C3HC4-type zinc finger-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_068532
VERSION     NP_068532.2
DBSOURCE    REFSEQ: accession NM_021764.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Van Quickelberghe,E., De Sutter,D., van Loo,G., Eyckerman,S. and
            Gevaert,K.
  TITLE     A protein-protein interaction map of the TNF-induced NF-kappaB
            signal transduction pathway
  JOURNAL   Sci Data 5, 180289 (2018)
   PUBMED   30561431
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Damgaard,R.B., Walker,J.A., Marco-Casanova,P., Morgan,N.V.,
            Titheradge,H.L., Elliott,P.R., McHale,D., Maher,E.R.,
            McKenzie,A.N.J. and Komander,D.
  TITLE     The Deubiquitinase OTULIN Is an Essential Negative Regulator of
            Inflammation and Autoimmunity
  JOURNAL   Cell 166 (5), 1215-1230 (2016)
   PUBMED   27523608
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Elliott,P.R., Nielsen,S.V., Marco-Casanova,P., Fiil,B.K.,
            Keusekotten,K., Mailand,N., Freund,S.M., Gyrd-Hansen,M. and
            Komander,D.
  TITLE     Molecular basis and regulation of OTULIN-LUBAC interaction
  JOURNAL   Mol Cell 54 (3), 335-348 (2014)
   PUBMED   24726323
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Muller-Rischart,A.K., Pilsl,A., Beaudette,P., Patra,M., Hadian,K.,
            Funke,M., Peis,R., Deinlein,A., Schweimer,C., Kuhn,P.H.,
            Lichtenthaler,S.F., Motori,E., Hrelia,S., Wurst,W., Trumbach,D.,
            Langer,T., Krappmann,D., Dittmar,G., Tatzelt,J. and Winklhofer,K.F.
  TITLE     The E3 ligase parkin maintains mitochondrial integrity by
            increasing linear ubiquitination of NEMO
  JOURNAL   Mol Cell 49 (5), 908-921 (2013)
   PUBMED   23453807
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Chu,W.M.
  TITLE     Tumor necrosis factor
  JOURNAL   Cancer Lett 328 (2), 222-225 (2013)
   PUBMED   23085193
  REMARK    Review article
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Kirisako,T., Kamei,K., Murata,S., Kato,M., Fukumoto,H., Kanie,M.,
            Sano,S., Tokunaga,F., Tanaka,K. and Iwai,K.
  TITLE     A ubiquitin ligase complex assembles linear polyubiquitin chains
  JOURNAL   EMBO J 25 (20), 4877-4887 (2006)
   PUBMED   17006537
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Tatematsu,K., Yoshimoto,N., Koyanagi,T., Tokunaga,C., Tachibana,T.,
            Yoneda,Y., Yoshida,M., Okajima,T., Tanizawa,K. and Kuroda,S.
  TITLE     Nuclear-cytoplasmic shuttling of a RING-IBR protein RBCK1 and its
            functional interaction with nuclear body proteins
  JOURNAL   J Biol Chem 280 (24), 22937-22944 (2005)
   PUBMED   15833741
  REMARK    GeneRIF: RBCK1 (human C20orf18 and rat Pkcbpb15) is involved in
            transcriptional machinery in the nuclear bodies, and its
            transcriptional activity is regulated by nucleocytoplasmic
            shuttling.
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Yamanaka,K., Ishikawa,H., Megumi,Y., Tokunaga,F., Kanie,M.,
            Rouault,T.A., Morishima,I., Minato,N., Ishimori,K. and Iwai,K.
  TITLE     Identification of the ubiquitin-protein ligase that recognizes
            oxidized IRP2
  JOURNAL   Nat Cell Biol 5 (4), 336-340 (2003)
   PUBMED   12629548
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Tokunaga,C., Tatematsu,K., Kuroda,S., Nakagawa,N. and Kikkawa,U.
  TITLE     Molecular cloning and characterization of RBCK2, a splicing variant
            of a RBCC family protein, RBCK1
  JOURNAL   FEBS Lett 435 (1), 11-15 (1998)
   PUBMED   9755849
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Tokunaga,C., Kuroda,S., Tatematsu,K., Nakagawa,N., Ono,Y. and
            Kikkawa,U.
  TITLE     Molecular cloning and characterization of a novel protein kinase
            C-interacting protein with structural motifs related to RBCC family
            proteins
  JOURNAL   Biochem Biophys Res Commun 244 (2), 353-359 (1998)
   PUBMED   9514928
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U48248.1.
            
            On Apr 12, 2007 this sequence version replaced NP_068532.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U48248.1, BC061723.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676811 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..508
                     /product="ranBP-type and C3HC4-type zinc finger-containing
                     protein 1"
                     /EC_number="2.3.2.31"
                     /note="protein kinase C-binding protein beta-15;
                     ubiquitin-conjugating enzyme 7-interacting protein 3;
                     heme-oxidized IRP2 ubiquitin ligase 1 homolog; RBCC
                     protein interacting with PKC 1; protein kinase C-binding
                     protein Beta15; RanBP-type and C3HC4-type zinc finger
                     containing 1; RING-type E3 ubiquitin transferase HOIL-1"
                     /calculated_mol_wt=57554
     Region          1..268
                     /region_name="Interaction with TAB2.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62921.3)"
     Region          1..218
                     /region_name="Interaction with IRF3.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62921.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8; propagated from
                     UniProtKB/Swiss-Prot (Q62921.3)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8; propagated from
                     UniProtKB/Swiss-Prot (Q62921.3)"
     Region          53..133
                     /region_name="Ubl_HOIL1"
                     /note="ubiquitin-like (Ubl) domain found in heme-oxidized
                     IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins;
                     cd01799"
                     /db_xref="CDD:340497"
     Site            order(56,61..63,65..67,69..72,91..92,94..95,131..133)
                     /site_type="other"
                     /note="UBA interaction site [polypeptide binding]"
                     /db_xref="CDD:340497"
     Region          69..131
                     /region_name="Interaction with RNF31.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62921.3)"
     Region          161..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62921.3)"
     Region          195..215
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          195..214
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Region          271..326
                     /region_name="mRING-HC-C3HC3D_RBR_HOIL1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1)
                     and similar proteins; cd16633"
                     /db_xref="CDD:438295"
     Region          276..504
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62921.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9BYM8; propagated from
                     UniProtKB/Swiss-Prot (Q62921.3)"
     Region          359..423
                     /region_name="BRcat_RBR_HOIL1"
                     /note="BRcat domain found in heme-oxidized IRP2 ubiquitin
                     ligase 1 (HOIL-1) and similar proteins; cd20345"
                     /db_xref="CDD:439006"
     Region          436..508
                     /region_name="Rcat_RBR_HOIL1"
                     /note="Rcat domain found in heme-oxidized IRP2 ubiquitin
                     ligase 1 (HOIL-1) and similar proteins; cd20358"
                     /db_xref="CDD:439019"
     CDS             1..508
                     /gene="Rbck1"
                     /gene_synonym="HOIL-1; Pkcbpb15"
                     /coded_by="NM_021764.1:296..1822"
                     /db_xref="GeneID:60383"
                     /db_xref="RGD:708404"
ORIGIN      
        1 mdektkkaee malslaravt ggdeqaaiky atwlaeqkvp lrvqvkpevs ptqdirlcvs
       61 vedaymhtvt iwltvrpdmt vaslkdmvfl dygfppslqq wvvgqrlard qetlhshgir
      121 rngdsaylyl lsarntslnp qelqrqrqlr mledlgfkdl tlqprgplep vlpkprthqe
      181 tgqpdaapes ppvgwqcpgc tfinkptrpg cemccrarpe ayqipasyqp deeerarlag
      241 eeealrqyeq rkqqqqegny lqhvqleqrs lvlntepaec pvcysvlapg eavvlreclh
      301 tfcreclqgt irnsqeaevs cpfidntysc pgkllereir allspedyqr fldlgvsiae
      361 nrstlsyhck tpdcrgwcff eddvneftcp vctrvncllc kaihermncr eyqddlahra
      421 rndvaaqqtt emlrvmlqqg eamycpqcri vvqkkdgcdw irctvchtei cwvtkgprwg
      481 pggpgdtsgg crcrvngipc hpscqnch
//
LOCUS       NP_001097998             984 aa            linear   ROD 27-APR-2025
DEFINITION  ephrin type-B receptor 1 precursor [Rattus norvegicus].
ACCESSION   NP_001097998 XP_001059882 XP_001081949 XP_217250
VERSION     NP_001097998.1
DBSOURCE    REFSEQ: accession NM_001104528.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Omoumi,S., Rashidy-Pour,A., Seyedinia,S.A., Tarahomi,P.,
            Vafaei,A.A. and Raise-Abdullahi,P.
  TITLE     Corticosterone injection into the infralimbic prefrontal cortex
            enhances fear memory extinction: Involvement of GABA receptors and
            the extracellular signal-regulated kinase
  JOURNAL   Physiol Behav 265, 114156 (2023)
   PUBMED   36918107
  REMARK    GeneRIF: Corticosterone injection into the infralimbic prefrontal
            cortex enhances fear memory extinction: Involvement of GABA
            receptors and the extracellular signal-regulated kinase.
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Li,X., Chen,S., Feng,D., Fu,Y., Wu,H., Lu,J. and Bao,J.
  TITLE     Calcium-sensing receptor promotes calcium oxalate crystal adhesion
            and renal injury in Wistar rats by promoting ROS production and
            subsequent regulation of PS ectropion, OPN, KIM-1, and ERK
            expression
  JOURNAL   Ren Fail 43 (1), 465-476 (2021)
   PUBMED   33678127
  REMARK    GeneRIF: Calcium-sensing receptor promotes calcium oxalate crystal
            adhesion and renal injury in Wistar rats by promoting ROS
            production and subsequent regulation of PS ectropion, OPN, KIM-1,
            and ERK expression.
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Jin,F., Zhao,L., Hu,Q. and Qi,F.
  TITLE     Peripheral EphrinB1/EphB1 signalling attenuates muscle hyperalgesia
            in MPS patients and a rat model of taut band-associated persistent
            muscle pain
  JOURNAL   Mol Pain 16, 1744806920984079 (2020)
   PUBMED   33356837
  REMARK    GeneRIF: Peripheral EphrinB1/EphB1 signalling attenuates muscle
            hyperalgesia in MPS patients and a rat model of taut
            band-associated persistent muscle pain.
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Zhang,M. and Wang,Z.
  TITLE     Downregulation of miR143/145 gene cluster expression promotes the
            aortic media degeneration process via the TGF-beta1 signaling
            pathway
  JOURNAL   Am J Transl Res 11 (1), 370-378 (2019)
   PUBMED   30787994
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 984)
  AUTHORS   Lim,S.H.
  TITLE     Larch Arabinogalactan Attenuates Myocardial Injury by Inhibiting
            Apoptotic Cascades in a Rat Model of Ischemia-Reperfusion
  JOURNAL   J Med Food 20 (7), 691-699 (2017)
   PUBMED   28622474
REFERENCE   6  (residues 1 to 984)
  AUTHORS   Stein,E., Lane,A.A., Cerretti,D.P., Schoecklmann,H.O.,
            Schroff,A.D., Van Etten,R.L. and Daniel,T.O.
  TITLE     Eph receptors discriminate specific ligand oligomers to determine
            alternative signaling complexes, attachment, and assembly responses
  JOURNAL   Genes Dev 12 (5), 667-678 (1998)
   PUBMED   9499402
REFERENCE   7  (residues 1 to 984)
  AUTHORS   Stein,E., Huynh-Do,U., Lane,A.A., Cerretti,D.P. and Daniel,T.O.
  TITLE     Nck recruitment to Eph receptor, EphB1/ELK, couples ligand
            activation to c-Jun kinase
  JOURNAL   J Biol Chem 273 (3), 1303-1308 (1998)
   PUBMED   9430661
REFERENCE   8  (residues 1 to 984)
  AUTHORS   Cerretti,D.P., Vanden Bos,T., Nelson,N., Kozlosky,C.J., Reddy,P.,
            Maraskovsky,E., Park,L.S., Lyman,S.D., Copeland,N.G., Gilbert,D.J.
            et al.
  TITLE     Isolation of LERK-5: a ligand of the eph-related receptor tyrosine
            kinases
  JOURNAL   Mol Immunol 32 (16), 1197-1205 (1995)
   PUBMED   8559144
REFERENCE   9  (residues 1 to 984)
  AUTHORS   Lhotak,V., Greer,P., Letwin,K. and Pawson,T.
  TITLE     Characterization of elk, a brain-specific receptor tyrosine kinase
  JOURNAL   Mol Cell Biol 11 (5), 2496-2502 (1991)
   PUBMED   2017163
REFERENCE   10 (residues 1 to 984)
  AUTHORS   Letwin,K., Yee,S.P. and Pawson,T.
  TITLE     Novel protein-tyrosine kinase cDNAs related to fps/fes and eph
            cloned using anti-phosphotyrosine antibody
  JOURNAL   Oncogene 3 (6), 621-627 (1988)
   PUBMED   2485255
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473954.2.
            
            On or before Sep 14, 2007 this sequence version replaced
            XP_217250.1, XP_001059882.1, XP_001081949.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760384
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..984
                     /product="ephrin type-B receptor 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-B receptor 1; tyrosine-protein kinase
                     receptor EPH-2; Eph receptor B2 (ELK-related protein
                     tyrosine kinase)"
                     /calculated_mol_wt=108167
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1735
     mat_peptide     18..984
                     /product="Ephrin type-B receptor 1. /id=PRO_0000016825"
                     /note="propagated from UniProtKB/Swiss-Prot (P09759.2)"
                     /calculated_mol_wt=108167
     Region          20..195
                     /region_name="EphR_LBD_B1"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 1;
                     cd10476"
                     /db_xref="CDD:198444"
     Site            order(27..29,31,43..46,48,52,54,56,59,92..94,98,100,146,
                     148,154..155,157..158,183,185,187)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198444"
     Site            order(323,398,411)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          326..412
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P09759.2)"
     Site            order(412..413,415..416)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(417,498,513)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P09759.2)"
     Region          435..518
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P09759.2)"
     Site            order(514..515,517..518)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            541..563
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09759.2)"
     Region          542..616
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P54753; propagated from
                     UniProtKB/Swiss-Prot (P09759.2)"
     Region          614..882
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(625..629,633,649,651,697..698,700,704,744,748..749,
                     751,762,783..787,796,830)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(625..627,629,633,649,651,697..698,700,704,749,751,
                     762)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(744,748,783..787,796,830)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            761..789
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          908..975
                     /region_name="SAM_EPH-B1"
                     /note="SAM domain of EPH-B1 subfamily of tyrosine kinase
                     receptors; cd09551"
                     /db_xref="CDD:188950"
     Site            order(928,961)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188950"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P09759.2)"
     Region          982..984
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P09759.2)"
     CDS             1..984
                     /gene="Ephb1"
                     /gene_synonym="elk; Ephb2; Erk"
                     /coded_by="NM_001104528.1:269..3223"
                     /db_xref="GeneID:24338"
                     /db_xref="RGD:2556"
ORIGIN      
        1 maldclllfl lasavaamee tlmdtrtata elgwtanpas gweevsgyde nlntirtyqv
       61 cnvfepnqnn wllttfinrr gahriytemr ftvrdcsslp nvpgscketf nlyyyetdsv
      121 iatkksafws eapylkvdti aadesfsqvd fggrlmkvnt evrsfgpltr ngfylafqdy
      181 gacmsllsvr vffkkcpsiv qnfavfpetm tgaestslvi argtcipnae evdvpiklyc
      241 ngdgewmvpi grctckagye pensvackac pagtfkasqe aegcshcpsn srspseaspi
      301 ctcrtgyyra dfdppevact svpsgprnvi sivnetsiil ewhppretgg rddvtyniic
      361 kkcradrrsc srcddnvefv prqlgltecr vsisslwaht pytfdiqain gvsskspfpp
      421 qhvsvnittn qaapstvpim hqvsatmrsi tlswpqpeqp ngiildyeir yyekehnefn
      481 ssmarsqtnt aridglrpgm vyvvqvrart vagygkfsgk mcfqtltddd ykselreqlp
      541 liagsaaagv vfvvslvais ivcsrkrays keavysdklq hystgrgspg mkiyidpfty
      601 edpneavref akeidvsfvk ieevigagef gevykgrlkl pgkreiyvai ktlkagysek
      661 qrrdflseas imgqfdhpni irlegvvtks rpvmiitefm engaldsflr qndgqftviq
      721 lvgmlrgiaa gmkylsemny vhrdlaarni lvnsnlvckv sdfglsrylq ddtsdptyts
      781 slggkipvrw tapeaiayrk ftsasdvwsy givmwevmsf gerpywdmsn qdvinaieqd
      841 yrlpppmdcp aalhqlmldc wqkdrnsrpr faeivntldk mirnpaslkt vatitavpsq
      901 plldrsipdf tafttvddwl saikmvqyrd sfltagftsl qlvtqmtsed llrigvtlag
      961 hqkkilssih smrvqmnqsp svma
//
LOCUS       NP_114189                531 aa            linear   ROD 27-APR-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily D member 2 [Rattus norvegicus].
ACCESSION   NP_114189
VERSION     NP_114189.1
DBSOURCE    REFSEQ: accession NM_031983.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Singh,A.P. and Archer,T.K.
  TITLE     Analysis of the SWI/SNF chromatin-remodeling complex during early
            heart development and BAF250a repression cardiac gene transcription
            during P19 cell differentiation
  JOURNAL   Nucleic Acids Res 42 (5), 2958-2975 (2014)
   PUBMED   24335282
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Shain,A.H. and Pollack,J.R.
  TITLE     The spectrum of SWI/SNF mutations, ubiquitous in human cancers
  JOURNAL   PLoS One 8 (1), e55119 (2013)
   PUBMED   23355908
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Hargreaves,D.C. and Crabtree,G.R.
  TITLE     ATP-dependent chromatin remodeling: genetics, genomics and
            mechanisms
  JOURNAL   Cell Res 21 (3), 396-420 (2011)
   PUBMED   21358755
  REMARK    Review article
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Mahajan,M.C., Narlikar,G.J., Boyapaty,G., Kingston,R.E. and
            Weissman,S.M.
  TITLE     Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF
            form a chromatin remodeling complex at the beta-globin locus
            control region
  JOURNAL   Proc Natl Acad Sci U S A 102 (42), 15012-15017 (2005)
   PUBMED   16217013
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Olave,I., Wang,W., Xue,Y., Kuo,A. and Crabtree,G.R.
  TITLE     Identification of a polymorphic, neuron-specific chromatin
            remodeling complex
  JOURNAL   Genes Dev 16 (19), 2509-2517 (2002)
   PUBMED   12368262
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Otsuki,T., Furukawa,Y., Ikeda,K., Endo,H., Yamashita,T.,
            Shinohara,A., Iwamatsu,A., Ozawa,K. and Liu,J.M.
  TITLE     Fanconi anemia protein, FANCA, associates with BRG1, a component of
            the human SWI/SNF complex
  JOURNAL   Hum Mol Genet 10 (23), 2651-2660 (2001)
   PUBMED   11726552
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Nomoto,K., Nakazato,S., Kazahari,K. and Ono,M.
  TITLE     Gene structure of rat BAF60b, a component of mammalian SW1/SNF
            complexes, and its physical linkage to the growth hormone gene and
            transcription factor SUG/proteasome p45 gene
  JOURNAL   Gene 202 (1-2), 157-165 (1997)
   PUBMED   9427560
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062063.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062063.1, AB003504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..531
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily D member
                     2"
                     /note="BRG1-associated factor 60B; 60 kDa
                     BRG-1/Brm-associated factor subunit B; SWI/SNF related,
                     matrix associated, actin dependent regulator of chromatin,
                     subfamily d, member 2"
                     /calculated_mol_wt=58997
     Region          20..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54772.3)"
     Region          <43..148
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Site            81
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (O54772.3)"
     Site            104
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (O54772.3)"
     Region          202..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54772.3)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (O54772.3)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q92925; propagated from
                     UniProtKB/Swiss-Prot (O54772.3)"
     Region          307..386
                     /region_name="SWIB_BAF60B"
                     /note="SWIB domain found in BRG1-associated factor 60B
                     (BAF60B) and similar proteins; cd17675"
                     /db_xref="CDD:349494"
     Site            order(329,332..333,335..336,339..340,345,350..351,353,370,
                     373..374)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349494"
     CDS             1..531
                     /gene="Smarcd2"
                     /gene_synonym="BAF60b"
                     /coded_by="NM_031983.2:86..1681"
                     /db_xref="GeneID:83833"
                     /db_xref="RGD:69289"
ORIGIN      
        1 msgrgaggfp lpplspggga vaaalgappp pagpgmlpnp alrgpgpsgg mgvpgaaafr
       61 pmgpagpaaq yqrpgmspgs rmpmaglqvg ppagspfgta aplrpgmppt mmdpfrkrll
      121 vpqaqppmpa qrrglkrrkm adkvlpqrir elvpesqaym dllaferkld qtiarkrmei
      181 qeaikkpltq krklriyisn tfspskadgd nsgtagtpgg tpaadkvasw elrvegklld
      241 dpskqkrkfs sffkslviel dkelygpdnh lvewhrmptt qetdgfqvkr pgdlnvkctl
      301 llmldhqppq ykldprlarl lgvhtqtraa imqalwlyik hnqlqdgher eyincnryfr
      361 qifscgrlrf seipmklagl lqhpdpivin hvisvdpndq kktacydidv evddplkaqm
      421 snflasttnq qeiasldvki hetiesinql ktqrdfmlsf stepqdfiqe wlrsqrrdlk
      481 iitdvignpe eerraafyhq pwaqeavgrh ifakvqqrrq eleqvlgirl t
//
LOCUS       NP_062056                377 aa            linear   ROD 27-APR-2025
DEFINITION  actin, alpha cardiac muscle 1 [Rattus norvegicus].
ACCESSION   NP_062056 XP_215801
VERSION     NP_062056.1
DBSOURCE    REFSEQ: accession NM_019183.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Biesemann,C., Gronborg,M., Luquet,E., Wichert,S.P., Bernard,V.,
            Bungers,S.R., Cooper,B., Varoqueaux,F., Li,L., Byrne,J.A.,
            Urlaub,H., Jahn,O., Brose,N. and Herzog,E.
  TITLE     Proteomic screening of glutamatergic mouse brain synaptosomes
            isolated by fluorescence activated sorting
  JOURNAL   EMBO J 33 (2), 157-170 (2014)
   PUBMED   24413018
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Galic,M., Jeong,S., Tsai,F.C., Joubert,L.M., Wu,Y.I., Hahn,K.M.,
            Cui,Y. and Meyer,T.
  TITLE     External push and internal pull forces recruit curvature-sensing
            N-BAR domain proteins to the plasma membrane
  JOURNAL   Nat Cell Biol 14 (8), 874-881 (2012)
   PUBMED   22750946
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Olson,T.M., Michels,V.V., Thibodeau,S.N., Tai,Y.S. and Keating,M.T.
  TITLE     Actin mutations in dilated cardiomyopathy, a heritable form of
            heart failure
  JOURNAL   Science 280 (5364), 750-752 (1998)
   PUBMED   9563954
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Kumar,A., Crawford,K., Close,L., Madison,M., Lorenz,J.,
            Doetschman,T., Pawlowski,S., Duffy,J., Neumann,J., Robbins,J.,
            Boivin,G.P., O'Toole,B.A. and Lessard,J.L.
  TITLE     Rescue of cardiac alpha-actin-deficient mice by enteric smooth
            muscle gamma-actin
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4406-4411 (1997)
   PUBMED   9114002
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Mayer,Y., Czosnek,H., Zeelon,P.E., Yaffe,D. and Nudel,U.
  TITLE     Expression of the genes coding for the skeletal muscle and cardiac
            actions in the heart
  JOURNAL   Nucleic Acids Res 12 (2), 1087-1100 (1984)
   PUBMED   6546444
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Howie,L.J. and Drury,T.F.
  TITLE     Current estimates from the Health Interview Survey: United
            States--1977
  JOURNAL   Vital Health Stat 10 (126), 1-98 (1978)
   PUBMED   734919
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Falicki,Z., Pilasiewicz,B. and Pawlowicz,B.
  TITLE     [Analysis of written enunciations of a patient as the basis for
            diagnosing schizophrenia]
  JOURNAL   Pol Tyg Lek 33 (32), 1259-1260 (1978)
   PUBMED   704424
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK356511.1, CF109672.1, AI706373.1 and AI603593.1.
            
            On Oct 23, 2005 this sequence version replaced XP_215801.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..377
                     /product="actin, alpha cardiac muscle 1"
                     /note="alpha-actin cardiac; alpha-cardiac actin; actin,
                     alpha, cardiac 1"
                     /calculated_mol_wt=41888
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine, in intermediate form.
                     /evidence=ECO:0000250|UniProtKB:P62737; propagated from
                     UniProtKB/Swiss-Prot (P68035.1)"
     mat_peptide     3..377
                     /product="Actin, alpha cardiac muscle 1.
                     /evidence=ECO:0000250|UniProtKB:P68135.
                     /id=PRO_0000000817"
                     /note="propagated from UniProtKB/Swiss-Prot (P68035.1)"
                     /calculated_mol_wt=41785
     Region          8..372
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     Site            75
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000250|UniProtKB:P62739; propagated from
                     UniProtKB/Swiss-Prot (P68035.1)"
     Site            86
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68032; propagated from
                     UniProtKB/Swiss-Prot (P68035.1)"
     CDS             1..377
                     /gene="Actc1"
                     /coded_by="NM_019183.1:193..1326"
                     /db_xref="GeneID:29275"
                     /db_xref="RGD:2026"
ORIGIN      
        1 mcddeettal vcdngsglvk agfagddapr avfpsivgrp rhqgvmvgmg qkdsyvgdea
       61 qskrgiltlk ypiehgiitn wddmekiwhh tfynelrvap eehptlltea plnpkanrek
      121 mtqimfetfn vpamyvaiqa vlslyasgrt tgivldsgdg vthnvpiyeg yalphaimrl
      181 dlagrdltdy lmkiltergy sfvttaerei vrdikeklcy valdfenema taasssslek
      241 syelpdgqvi tignerfrcp etlfqpsfig mesagihett ynsimkcdid irkdlyannv
      301 lsggttmypg iadrmqkeit alapstmkik iiapperkys vwiggsilas lstfqqmwis
      361 kqeydeagps ivhrkcf
//
LOCUS       NP_001008349             466 aa            linear   ROD 27-APR-2025
DEFINITION  FERM domain-containing protein 8 [Rattus norvegicus].
ACCESSION   NP_001008349 XP_219520
VERSION     NP_001008349.1
DBSOURCE    REFSEQ: accession NM_001008348.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Kunzel,U., Grieve,A.G., Meng,Y., Sieber,B., Cowley,S.A. and
            Freeman,M.
  TITLE     FRMD8 promotes inflammatory and growth factor signalling by
            stabilising the iRhom/ADAM17 sheddase complex
  JOURNAL   Elife 7, e35012 (2018)
   PUBMED   29897336
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Oikonomidi,I., Burbridge,E., Cavadas,M., Sullivan,G., Collis,B.,
            Naegele,H., Clancy,D., Brezinova,J., Hu,T., Bileck,A., Gerner,C.,
            Bolado,A., von Kriegsheim,A., Martin,S.J., Steinberg,F.,
            Strisovsky,K. and Adrain,C.
  TITLE     iTAP, a novel iRhom interactor, controls TNF secretion by policing
            the stability of iRhom/TACE
  JOURNAL   Elife 7, e35032 (2018)
   PUBMED   29897333
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085896.1.
            
            On Dec 16, 2004 this sequence version replaced XP_219520.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085896.1, FQ211651.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..466
                     /product="FERM domain-containing protein 8"
                     /note="FKSG44 protein"
                     /calculated_mol_wt=51651
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZ67; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Region          136..273
                     /region_name="FERM_M"
                     /note="FERM central domain; pfam00373"
                     /db_xref="CDD:459788"
     Region          379..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZ67; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZ67; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UFK8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Region          442..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2R3.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZ67; propagated from
                     UniProtKB/Swiss-Prot (Q5U2R3.1)"
     CDS             1..466
                     /gene="Frmd8"
                     /gene_synonym="RGD1310323"
                     /coded_by="NM_001008348.1:158..1558"
                     /db_xref="GeneID:309172"
                     /db_xref="RGD:1310323"
ORIGIN      
        1 megaegnagq pgpaershrs svssvgaraa dvlvyladdt vvplavenls sisahelhra
       61 vrevlqlpdm aleafalwlv spllevqlkp khqpyklgrq wpelllrftd asdddiamde
      121 pslqfrrnvf fpkrrelqvh deevlrllye eakgnvltar ypcdledcev lgglvcrvql
      181 gpyqpgqpaa ctvrekldsf lpahlckrgh glfaafrgrg aktgpceqgl lnayrqvkem
      241 aggdserett lgshyrayll kchelpfygc affhgevdkp tqgflhrggr kpvtvaisle
      301 gvhvidnrek hvllglrfqe lswdhtspee eepvlwlefd gdsegtpvnk llriyskqae
      361 lmsvlieyci elsqaaepal pqesasgpqe apspssaptq rpklrrqgsv vcsriqhlst
      421 idyvedgsgi krvkpkrtts ffsrqlsssh gsytvvqpnd nspeqg
//
LOCUS       NP_001003957             689 aa            linear   ROD 27-APR-2025
DEFINITION  DNA (cytosine-5)-methyltransferase 3A isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001003957
VERSION     NP_001003957.1
DBSOURCE    REFSEQ: accession NM_001003957.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Cheng,P., Wei,H.Z., Chen,H.W., Wang,Z.Q., Mao,P. and Zhang,H.H.
  TITLE     DNMT3a-mediated methylation of PPARgamma promote intervertebral
            disc degeneration by regulating the NF-kappaB pathway
  JOURNAL   J Cell Mol Med 28 (2), e18048 (2024)
   PUBMED   37986543
  REMARK    GeneRIF: DNMT3a-mediated methylation of PPARgamma promote
            intervertebral disc degeneration by regulating the NF-kappaB
            pathway.
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Gu,Y.H., Wang,J., Lu,W.C., Cheng,Y., Tao,R., Zhang,S.J., Xu,T.,
            Zhai,K.W., Luo,S.X. and Xin,W.J.
  TITLE     POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment
  JOURNAL   Neurochem Res 48 (12), 3652-3664 (2023)
   PUBMED   37592110
  REMARK    GeneRIF: POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment.
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Kuang,J., Xu,M., Xu,C., Wang,Y., Ni,C., Wei,S., Liu,Z., Kong,M.,
            Zhou,Q., Yao,M. and Ni,H.
  TITLE     miR-199a-3p mediates bone cancer pain through upregulation of
            dnmt3a expression in spinal dorsal horn neurons
  JOURNAL   Biochem Biophys Res Commun 682, 97-103 (2023)
   PUBMED   37804593
  REMARK    GeneRIF: miR-199a-3p mediates bone cancer pain through upregulation
            of dnmt3a expression in spinal dorsal horn neurons.
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Frances,R., Mata-Garrido,J., de la Fuente,R., Carcelen,M.,
            Lafarga,M., Berciano,M.T., Garcia,R., Hurle,M.A. and Tramullas,M.
  TITLE     Identification of Epigenetic Interactions between MicroRNA-30c-5p
            and DNA Methyltransferases in Neuropathic Pain
  JOURNAL   Int J Mol Sci 23 (22), 13994 (2022)
   PUBMED   36430472
  REMARK    GeneRIF: Identification of Epigenetic Interactions between
            MicroRNA-30c-5p and DNA Methyltransferases in Neuropathic Pain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 689)
  AUTHORS   Wei,J., Cheng,J., Waddell,N.J., Wang,Z.J., Pang,X., Cao,Q., Liu,A.,
            Chitaman,J.M., Abreu,K., Jasrotia,R.S., Duffney,L.J., Zhang,J.,
            Dietz,D.M., Feng,J. and Yan,Z.
  TITLE     DNA Methyltransferase 3A Is Involved in the Sustained Effects of
            Chronic Stress on Synaptic Functions and Behaviors
  JOURNAL   Cereb Cortex 31 (4), 1998-2012 (2021)
   PUBMED   33230530
  REMARK    GeneRIF: DNA Methyltransferase 3A Is Involved in the Sustained
            Effects of Chronic Stress on Synaptic Functions and Behaviors.
REFERENCE   6  (residues 1 to 689)
  AUTHORS   Hata,K., Okano,M., Lei,H. and Li,E.
  TITLE     Dnmt3L cooperates with the Dnmt3 family of de novo DNA
            methyltransferases to establish maternal imprints in mice
  JOURNAL   Development 129 (8), 1983-1993 (2002)
   PUBMED   11934864
REFERENCE   7  (residues 1 to 689)
  AUTHORS   Gowher,H. and Jeltsch,A.
  TITLE     Enzymatic properties of recombinant Dnmt3a DNA methyltransferase
            from mouse: the enzyme modifies DNA in a non-processive manner and
            also methylates non-CpG [correction of non-CpA] sites
  JOURNAL   J Mol Biol 309 (5), 1201-1208 (2001)
   PUBMED   11399089
  REMARK    Erratum:[J Mol Biol 2001 Jul 20;310(4):951]
REFERENCE   8  (residues 1 to 689)
  AUTHORS   Mizuno,S., Chijiwa,T., Okamura,T., Akashi,K., Fukumaki,Y., Niho,Y.
            and Sasaki,H.
  TITLE     Expression of DNA methyltransferases DNMT1, 3A, and 3B in normal
            hematopoiesis and in acute and chronic myelogenous leukemia
  JOURNAL   Blood 97 (5), 1172-1179 (2001)
   PUBMED   11222358
REFERENCE   9  (residues 1 to 689)
  AUTHORS   Okano,M., Bell,D.W., Haber,D.A. and Li,E.
  TITLE     DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
            methylation and mammalian development
  JOURNAL   Cell 99 (3), 247-257 (1999)
   PUBMED   10555141
REFERENCE   10 (residues 1 to 689)
  AUTHORS   Okano,M., Xie,S. and Li,E.
  TITLE     Cloning and characterization of a family of novel mammalian DNA
            (cytosine-5) methyltransferases
  JOURNAL   Nat Genet 19 (3), 219-220 (1998)
   PUBMED   9662389
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BN000396.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BN000396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..689
                     /product="DNA (cytosine-5)-methyltransferase 3A isoform 2"
                     /EC_number="2.1.1.37"
                     /note="DNA methyltransferase 3A; DNA
                     (cytosine-5)-methyltransferase 3A; DNA
                     (cytosine-5-)-methyltransferase 3 alpha; cysteine
                     methyltransferase DNMT3A"
                     /calculated_mol_wt=77694
     Region          62..195
                     /region_name="PWWP_DNMT3A"
                     /note="PWWP domain found in DNA
                     (cytosine-5)-methyltransferase 3A (DNMT3A); cd20154"
                     /db_xref="CDD:438982"
     Site            order(78,80,83,95,107,110,112..114)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438982"
     Site            81..84
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438982"
     Region          264..391
                     /region_name="ADDz_Dnmt3a"
                     /note="ADDz domain found in DNA (cytosine-5)
                     methyltransferases (C5-MTases) 3a (Dnmt3a); cd11729"
                     /db_xref="CDD:277255"
     Site            order(306,308,310..313,318..325,352..353,355,358)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:277255"
     Region          408..686
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     CDS             1..689
                     /gene="Dnmt3a"
                     /coded_by="NM_001003957.1:147..2216"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:444984"
                     /db_xref="RGD:1303336"
ORIGIN      
        1 mnaveesqas gesqkveeas ppavqqptdp asptvattpe pvgadagdkn atkaaddepe
       61 yedgrgfgig elvwgklrgf swwpgrivsw wmtgrsraae gtrwvmwfgd gkfsvvcvek
      121 lmplssfcsa fhqatynkqp myrkaiyevl qvassragkl fpachdsdes dtgkavevqn
      181 kqmiewalgg fqpsgpkgle ppeeeknpyk evytdmwvep eaaayapppp akkprkstte
      241 kpkvkeiide rtrerlvyev rqkcrniedi ciscgslnvt lehplfiggm cqnckncfle
      301 cayqydddgy qsycticcgg revlmcgnnn ccrcfcvecv dllvgpgaaq aaikedpwnc
      361 ymcghkgtyg llrrredwps rlqmffannh dqefdppkvy ppvpaekrkp irvlslfdgi
      421 atgllvlkdl giqvdryias evcedsitvg mvrhqgkimy vgdvrsvtqk hiqewgpfdl
      481 viggspcndl sivnparkgl yegtgrlffe fyrllhdarp kegddrpffw lfenvvamgv
      541 sdkrdisrfl esnpvmidak evsaahrary fwgnlpgmnr plastvndkl elqeclehgr
      601 iakfskvrti ttrsnsikqg kdqhfpvfmn ekedilwcte mervfgfpvh ytdvsnmsrl
      661 arqrllgrsw svpvirhlfa plkeyfacv
//
LOCUS       NP_001102318             326 aa            linear   ROD 27-APR-2025
DEFINITION  ELAV-like protein 1 [Rattus norvegicus].
ACCESSION   NP_001102318 XP_001065476 XP_344064
VERSION     NP_001102318.1
DBSOURCE    REFSEQ: accession NM_001108848.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Han,W., Gu,D., Chen,H., Tao,X. and Chen,L.
  TITLE     HPF1 regulates tendon stem/progenitor cell senescence and tendon
            repair via PARP1-mediated poly-ADP ribosylation of HuR
  JOURNAL   Genes Genomics 46 (1), 27-36 (2024)
   PUBMED   37713069
  REMARK    GeneRIF: HPF1 regulates tendon stem/progenitor cell senescence and
            tendon repair via PARP1-mediated poly-ADP ribosylation of HuR.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Wang,C., Zhang,X., Zhu,X., Chen,R. and Lian,N.
  TITLE     The RNA Binding Protein HuR Promotes Neuronal Apoptosis in Rats
            with Spinal Cord Injury via the HDAC1/RAD21 Axis
  JOURNAL   Neuroscience 522, 109-120 (2023)
   PUBMED   37164303
  REMARK    GeneRIF: The RNA Binding Protein HuR Promotes Neuronal Apoptosis in
            Rats with Spinal Cord Injury via the HDAC1/RAD21 Axis.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Du,Y., Zhang,R., Zhang,G., Wu,H., Zhan,S. and Bu,N.
  TITLE     Downregulation of ELAVL1 attenuates ferroptosis-induced neuronal
            impairment in rats with cerebral ischemia/reperfusion via reducing
            DNMT3B-dependent PINK1 methylation
  JOURNAL   Metab Brain Dis 37 (8), 2763-2775 (2022)
   PUBMED   36173508
  REMARK    GeneRIF: Downregulation of ELAVL1 attenuates ferroptosis-induced
            neuronal impairment in rats with cerebral ischemia/reperfusion via
            reducing DNMT3B-dependent PINK1 methylation.
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Lai,Y., Tang,H., Zhang,X., Zhou,Z., Zhou,M., Hu,Z., Zhu,F.,
            Zhang,L. and Nie,J.
  TITLE     Trimethylamine-N-Oxide Aggravates Kidney Injury via Activation of
            p38/MAPK Signaling and Upregulation of HuR
  JOURNAL   Kidney Blood Press Res 47 (1), 61-71 (2022)
   PUBMED   34788763
  REMARK    GeneRIF: Trimethylamine-N-Oxide Aggravates Kidney Injury via
            Activation of p38/MAPK Signaling and Upregulation of HuR.
REFERENCE   6  (residues 1 to 326)
  AUTHORS   McMullen,M.R., Cocuzzi,E., Hatzoglou,M. and Nagy,L.E.
  TITLE     Chronic ethanol exposure increases the binding of HuR to the
            TNFalpha 3'-untranslated region in macrophages
  JOURNAL   J Biol Chem 278 (40), 38333-38341 (2003)
   PUBMED   12876290
  REMARK    GeneRIF: increased binding of HuR to the TNFalpha 3'-UTR
            contributes to increased LPS-stimulated TNFalpha expression in
            macrophages after chronic ethanol exposure
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Tran,H., Maurer,F. and Nagamine,Y.
  TITLE     Stabilization of urokinase and urokinase receptor mRNAs by HuR is
            linked to its cytoplasmic accumulation induced by activated
            mitogen-activated protein kinase-activated protein kinase 2
  JOURNAL   Mol Cell Biol 23 (20), 7177-7188 (2003)
   PUBMED   14517288
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Akool,el.-S., Kleinert,H., Hamada,F.M., Abdelwahab,M.H.,
            Forstermann,U., Pfeilschifter,J. and Eberhardt,W.
  TITLE     Nitric oxide increases the decay of matrix metalloproteinase 9 mRNA
            by inhibiting the expression of mRNA-stabilizing factor HuR
  JOURNAL   Mol Cell Biol 23 (14), 4901-4916 (2003)
   PUBMED   12832476
  REMARK    GeneRIF: These results demonstrate that NO acts in a cGMP-dependent
            mechanism to inhibit the expression level of HuR, thereby reducing
            the stability of MMP-9 mRNA
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Tang,K., Breen,E.C. and Wagner,P.D.
  TITLE     Hu protein R-mediated posttranscriptional regulation of VEGF
            expression in rat gastrocnemius muscle
  JOURNAL   Am J Physiol Heart Circ Physiol 283 (4), H1497-H1504 (2002)
   PUBMED   12234802
  REMARK    GeneRIF: Hu protein R-mediated posttranscriptional regulation of
            VEGF expression in rat gastrocnemius muscle.
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Ma,W.J., Cheng,S., Campbell,C., Wright,A. and Furneaux,H.
  TITLE     Cloning and characterization of HuR, a ubiquitously expressed
            Elav-like protein
  JOURNAL   J Biol Chem 271 (14), 8144-8151 (1996)
   PUBMED   8626503
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474084.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_344064.3, XP_001065476.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168972.1, EV766896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..326
                     /product="ELAV-like protein 1"
                     /note="ELAV like 1; ELAV (embryonic lethal, abnormal
                     vision, Drosophila)-like 1 (Hu antigen R);
                     mRNA-stabilizing factor HuR; hu-antigen R"
                     /calculated_mol_wt=36038
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Region          19..326
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            206
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P70372; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            217
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by CARM1, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q15717;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15717; propagated from
                     UniProtKB/Swiss-Prot (B5DF91.1)"
     CDS             1..326
                     /gene="Elavl1"
                     /gene_synonym="Hua; HuR"
                     /coded_by="NM_001108848.1:153..1133"
                     /db_xref="GeneID:363854"
                     /db_xref="RGD:1308649"
ORIGIN      
        1 msngyedhma edcrddigrt nlivnylpqn mtqeelrslf ssigevesak lirdkvaghs
       61 lgygfvnyvt akdaeraist lnglrlqskt ikvsyarpss evikdanlyi sglprtmtqk
      121 dvedmfsrfg riinsrvlvd qttglsrgva firfdkrsea eeaitsfngh kppgssepit
      181 vkfaanpnqn knmallsqly hsparrfggp vhhqaqrfrf spmgvdhmsg isgvnvpgna
      241 ssgwcifiyn lgqdadegil wqmfgpfgav tnvkvirdfn tnkckgfgfv tmtnyeeaam
      301 aiaslngyrl gdkilqvsfk tnkshk
//
LOCUS       NP_001014190             573 aa            linear   ROD 27-APR-2025
DEFINITION  DNA polymerase lambda [Rattus norvegicus].
ACCESSION   NP_001014190 XP_342059
VERSION     NP_001014190.1
DBSOURCE    REFSEQ: accession NM_001014168.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Capp,J.P., Boudsocq,F., Bergoglio,V., Trouche,D., Cazaux,C.,
            Blanco,L., Hoffmann,J.S. and Canitrot,Y.
  TITLE     The R438W polymorphism of human DNA polymerase lambda triggers
            cellular sensitivity to camptothecin by compromising the homologous
            recombination repair pathway
  JOURNAL   Carcinogenesis 31 (10), 1742-1747 (2010)
   PUBMED   20693240
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Lieber,M.R.
  TITLE     The mechanism of double-strand DNA break repair by the
            nonhomologous DNA end-joining pathway
  JOURNAL   Annu Rev Biochem 79, 181-211 (2010)
   PUBMED   20192759
  REMARK    Review article
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Terrados,G., Capp,J.P., Canitrot,Y., Garcia-Diaz,M., Bebenek,K.,
            Kirchhoff,T., Villanueva,A., Boudsocq,F., Bergoglio,V., Cazaux,C.,
            Kunkel,T.A., Hoffmann,J.S. and Blanco,L.
  TITLE     Characterization of a natural mutator variant of human DNA
            polymerase lambda which promotes chromosomal instability by
            compromising NHEJ
  JOURNAL   PLoS One 4 (10), e7290 (2009)
   PUBMED   19806195
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Aoufouchi,S., Flatter,E., Dahan,A., Faili,A., Bertocci,B.,
            Storck,S., Delbos,F., Cocea,L., Gupta,N., Weill,J.C. and
            Reynaud,C.A.
  TITLE     Two novel human and mouse DNA polymerases of the polX family
  JOURNAL   Nucleic Acids Res 28 (18), 3684-3693 (2000)
   PUBMED   10982892
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Garcia-Diaz,M., Dominguez,O., Lopez-Fernandez,L.A., de Lera,L.T.,
            Saniger,M.L., Ruiz,J.F., Parraga,M., Garcia-Ortiz,M.J.,
            Kirchhoff,T., del Mazo,J., Bernad,A. and Blanco,L.
  TITLE     DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA
            polymerase with a potential role in meiosis
  JOURNAL   J Mol Biol 301 (4), 851-867 (2000)
   PUBMED   10966791
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085841.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342059.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085841.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..573
                     /product="DNA polymerase lambda"
                     /EC_number="2.7.7.7"
                     /note="DNA-directed DNA polymerase lambda; pol Lambda;
                     polymerase (DNA directed), lambda; polymerase (DNA)
                     lambda"
                     /calculated_mol_wt=62270
     Region          40..123
                     /region_name="BRCT_polymerase_lambda"
                     /note="BRCT domain of DNA polymerase lambda and similar
                     proteins; cd17715"
                     /db_xref="CDD:349347"
     Region          126..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI3.1)"
     Region          253..571
                     /region_name="NT_POLXc"
                     /note="Nucleotidyltransferase (NT) domain of family X DNA
                     Polymerases; cd00141"
                     /db_xref="CDD:143386"
     Region          263..277
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UGP5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI3.1)"
     Site            order(337,339,341..346,349,370,384,414..415,418,420,
                     422..425,427,470,472,486,488,503..508,511,527)
                     /site_type="active"
                     /db_xref="CDD:143386"
     Site            order(337,339,341..346,349,370,414,418,424..425,427,470,
                     472,486,488,503..508,511)
                     /site_type="other"
                     /note="primer binding site [nucleotide binding]"
                     /db_xref="CDD:143386"
     Region          343..346
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UGP5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI3.1)"
     Site            order(384,414..415,418,420,422..425,427,470,488,503..506,
                     508,511,527)
                     /site_type="other"
                     /note="NTP binding site [chemical binding]"
                     /db_xref="CDD:143386"
     Region          418..427
                     /region_name="Involved in primer binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI3.1)"
     Site            order(425,427,488)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143386"
     Region          464..503
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UGP5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI3.1)"
     CDS             1..573
                     /gene="Poll"
                     /coded_by="NM_001014168.1:46..1767"
                     /db_xref="GeneID:361767"
                     /db_xref="RGD:1308053"
ORIGIN      
        1 mdpqgilkaf pkrkkihadp ssnalakipk reagdargwl sslrahimpt gigraraelf
       61 ekqiiqhggq vcsaqapgvt hivvdegmdy eralrllrlp qlppgaqlvk sawlslclqe
      121 kkltdtdgfs lsspkrslne pqpsksgqda sapgtqgvlp rttlslsppc travspppka
      181 ekppktqtql ssedeasdge gpqvssadlq alisghyptp pgedggpdpa pealgkwvca
      241 qpssqkatny nlhiteklev lakaynvqgd kwralgyaka inalksfhkp vssyqeacsi
      301 pgvgrrmaek vmeilesghl rkldhisdsv pvlelfsniw gagtktaqmw yhqgfrsled
      361 irglasltaq qaiglkhydd fldrmpreea aeieqmvrvs aqafnpgllc vacgsfrrgk
      421 vtcgdvdvli thpdgrshqg ifsplldslr qqgfltddlv sqeengqqqk ylgvcrlpga
      481 gqrhrrldii vvpysefaca llyftgsahf nrsmralakt kgmslsehal saavvrnsqg
      541 vkvgagqvlp tptekdvfkl lglpyrepae rdw
//
LOCUS       NP_073193               1235 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase TAO2 [Rattus norvegicus].
ACCESSION   NP_073193
VERSION     NP_073193.1
DBSOURCE    REFSEQ: accession NM_022702.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Yadav,S., Oses-Prieto,J.A., Peters,C.J., Zhou,J., Pleasure,S.J.,
            Burlingame,A.L., Jan,L.Y. and Jan,Y.N.
  TITLE     TAOK2 Kinase Mediates PSD95 Stability and Dendritic Spine
            Maturation through Septin7 Phosphorylation
  JOURNAL   Neuron 93 (2), 379-393 (2017)
   PUBMED   28065648
  REMARK    GeneRIF: TAOK2 directly phosphorylates the cytoskeletal GTPase
            Septin7, at an evolutionary conserved residue. This phosphorylation
            induces translocation of Septin7 to the spine, where it associates
            with and stabilizes the scaffolding protein PSD95, promoting
            dendritic spine maturation.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   de Anda,F.C., Rosario,A.L., Durak,O., Tran,T., Graff,J.,
            Meletis,K., Rei,D., Soda,T., Madabhushi,R., Ginty,D.D.,
            Kolodkin,A.L. and Tsai,L.H.
  TITLE     Autism spectrum disorder susceptibility gene TAOK2 affects basal
            dendrite formation in the neocortex
  JOURNAL   Nat Neurosci 15 (7), 1022-1031 (2012)
   PUBMED   22683681
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Cuadrado,A. and Nebreda,A.R.
  TITLE     Mechanisms and functions of p38 MAPK signalling
  JOURNAL   Biochem J 429 (3), 403-417 (2010)
   PUBMED   20626350
  REMARK    Review article
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Yasuda,S., Tanaka,H., Sugiura,H., Okamura,K., Sakaguchi,T.,
            Tran,U., Takemiya,T., Mizoguchi,A., Yagita,Y., Sakurai,T., De
            Robertis,E.M. and Yamagata,K.
  TITLE     Activity-induced protocadherin arcadlin regulates dendritic spine
            number by triggering N-cadherin endocytosis via TAO2beta and p38
            MAP kinases
  JOURNAL   Neuron 56 (3), 456-471 (2007)
   PUBMED   17988630
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Zhou,T.J., Sun,L.G., Gao,Y. and Goldsmith,E.J.
  TITLE     Crystal structure of the MAP3K TAO2 kinase domain bound by an
            inhibitor staurosporine
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 38 (6), 385-392 (2006)
   PUBMED   16761096
  REMARK    GeneRIF: this analysis of atomic details for TAO2-staurosporine
            interactions explains the relatively low potency of staurosporine
            against TAO2
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Zhou,T., Raman,M., Gao,Y., Earnest,S., Chen,Z., Machius,M.,
            Cobb,M.H. and Goldsmith,E.J.
  TITLE     Crystal structure of the TAO2 kinase domain: activation and
            specificity of a Ste20p MAP3K
  JOURNAL   Structure 12 (10), 1891-1900 (2004)
   PUBMED   15458637
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Chen,Z. and Cobb,M.H.
  TITLE     Regulation of stress-responsive mitogen-activated protein (MAP)
            kinase pathways by TAO2
  JOURNAL   J Biol Chem 276 (19), 16070-16075 (2001)
   PUBMED   11279118
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Chen,Z., Hutchison,M. and Cobb,M.H.
  TITLE     Isolation of the protein kinase TAO2 and identification of its
            mitogen-activated protein kinase/extracellular signal-regulated
            kinase kinase binding domain
  JOURNAL   J Biol Chem 274 (40), 28803-28807 (1999)
   PUBMED   10497253
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF140556.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF140556.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..1235
                     /product="serine/threonine-protein kinase TAO2"
                     /EC_number="2.7.11.1"
                     /note="serine-threonine kinase; thousand and one amino
                     acid protein 2"
                     /calculated_mol_wt=138620
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL54; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Region          12..319
                     /region_name="STKc_TAO2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Thousand-and-One Amino acids 2; cd06634"
                     /db_xref="CDD:270804"
     Site            order(34..38,42,55,57,89,105..108,110..111,114,155..156,
                     158,169,314)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270804"
     Site            order(34..38,42,55,57,89,105..108,110..111,114,151,
                     153..156,158,168..169,172,182..185,187,217,226)
                     /site_type="active"
                     /db_xref="CDD:270804"
     Site            order(37..38,151,153..155,172,182..185,187,217,226)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270804"
     Site            168..187
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270804"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15458637; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Region          318..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL54; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Region          <469..>749
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQ29; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL54; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL54; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UL54; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Region          892..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            967..987
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            989..1009
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            1014..1034
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            1038
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17988630; propagated from
                     UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            1040..1060
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Site            1170..1190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     Region          1210..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLS3.1)"
     CDS             1..1235
                     /gene="Taok2"
                     /gene_synonym="Tao2"
                     /coded_by="NM_022702.1:193..3900"
                     /db_xref="GeneID:64666"
                     /db_xref="RGD:621590"
ORIGIN      
        1 mpaggragsl kdpdvaelff kddpeklfsd lreighgsfg avyfardvrn sevvaikkms
       61 ysgkqsnekw qdiikevrfl qklrhpntiq yrgcylreht awlvmeyclg sasdllevhk
      121 kplqeveiaa vthgalqgla ylhshnmihr dvkagnills epglvklgdf gsasimapan
      181 sfvgtpywma pevilamdeg qydgkvdvws lgitcielae rkpplfnmna msalyhiaqn
      241 espalqsghw seyfrnfvds clqkipqdrp tsevllkhrf vlrerpptvi mdliqrtkda
      301 vreldnlqyr kmkkilfqea pngpgaeape eeeeaepymh ragtltsles shsvpsmsis
      361 assqsssvns ladasdneee eeeeeeeeee eeeegpesre mammqegeht vtshssiihr
      421 lpgsdnlydd pyqpemtpgp lqppaappts tssssarrra ycrnrdhfat irtaslvsrq
      481 iqeheqdsal reqlsgykrm rrqhqkqlla lesrlrgere ehsgrlqrel eaqragfgte
      541 aeklarrhqa igekearaaq aeerkfqqhi lgqqkkelaa lleaqkrtyk lrkeqlkeel
      601 qenpstpkre kaewllrqke qlqqcqaeee agllrrqrqy felqcrqykr kmllarhsld
      661 qdllredlnk kqtqkdleca lllrqheatr elelrqlqav qrtraeltrl qhqtelgnql
      721 eynkrreqel rqkhaaqvrq qpkslkvrag qlpmglpatg algplstgtl seeqpcssgq
      781 eailgqrmlg eeeeavperm ilgkegttle peeqrilgee mgtfssspqk hrslvneedw
      841 diskemkesr vpslasqern iigqeeagaw nlwekehgnl vdmefklgwv qgpvltpvpe
      901 eeeeeeeegg apigtprdpg dgcpspdipp epppshlrqy pasqlpgfls hglltglsfa
      961 vgsssgllpl llllllplla aqgggglqaa llalevglvg lgasylflct alhlppslfl
     1021 llaqgtalga vlslswrrgl mgvplglgaa wllawpslal plaamaaggk wvrqqgpqmr
     1081 rgisrlwlrv llrlspmvfr alqgcaavgd rglfalypkt nkngfrsrlp vpwprqgnpr
     1141 ttqhplalla rvwalckgwn wrlarashrl asclppwavh ilaswgllkg erpsriprll
     1201 prsqrrlgls asrqlppgtv agrrsqtrra lppwr
//
LOCUS       NP_001015028             885 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 6 [Rattus
            norvegicus].
ACCESSION   NP_001015028 XP_342834
VERSION     NP_001015028.2
DBSOURCE    REFSEQ: accession NM_001015028.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Nakajima,Y., Kiyonari,H., Mukumoto,Y. and Yokoyama,T.
  TITLE     The Inv compartment of renal cilia is an intraciliary
            signal-activating center to phosphorylate ANKS6
  JOURNAL   Kidney Int 93 (5), 1108-1117 (2018)
   PUBMED   29395339
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 885)
  AUTHORS   Delestre,L., Bakey,Z., Prado,C., Hoffmann,S., Bihoreau,M.T.,
            Lelongt,B. and Gauguier,D.
  TITLE     ANKS3 Co-Localises with ANKS6 in Mouse Renal Cilia and Is
            Associated with Vasopressin Signaling and Apoptosis In Vivo in Mice
  JOURNAL   PLoS One 10 (9), e0136781 (2015)
   PUBMED   26327442
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Ramachandran,H., Engel,C., Muller,B., Dengjel,J., Walz,G. and
            Yakulov,T.A.
  TITLE     Anks3 alters the sub-cellular localization of the Nek7 kinase
  JOURNAL   Biochem Biophys Res Commun 464 (3), 901-907 (2015)
   PUBMED   26188091
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Li,Y., Klena,N.T., Gabriel,G.C., Liu,X., Kim,A.J., Lemke,K.,
            Chen,Y., Chatterjee,B., Devine,W., Damerla,R.R., Chang,C., Yagi,H.,
            San Agustin,J.T., Thahir,M., Anderton,S., Lawhead,C., Vescovi,A.,
            Pratt,H., Morgan,J., Haynes,L., Smith,C.L., Eppig,J.T.,
            Reinholdt,L., Francis,R., Leatherbury,L., Ganapathiraju,M.K.,
            Tobita,K., Pazour,G.J. and Lo,C.W.
  TITLE     Global genetic analysis in mice unveils central role for cilia in
            congenital heart disease
  JOURNAL   Nature 521 (7553), 520-524 (2015)
   PUBMED   25807483
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Stagner,E.E., Bouvrette,D.J., Cheng,J. and Bryda,E.C.
  TITLE     The polycystic kidney disease-related proteins Bicc1 and SamCystin
            interact
  JOURNAL   Biochem Biophys Res Commun 383 (1), 16-21 (2009)
   PUBMED   19324013
  REMARK    GeneRIF: Bicc1 and SamCystin interact at the protein level
            suggesting that they function in a common molecular pathway that
            when perturbed, is involved in cystogenesis.
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Kaisaki,P.J., Bergmann,C., Brown,J.H., Outeda,P., Lens,X.M.,
            Peters,D.J., Gretz,N., Gauguier,D. and Bihoreau,M.T.
  TITLE     Genomic organization and mutation screening of the human ortholog
            of Pkdr1 associated with polycystic kidney disease in the rat
  JOURNAL   Eur J Med Genet 51 (4), 325-331 (2008)
   PUBMED   18434273
  REMARK    GeneRIF: Susceptibility to renal cyst formation in the (cy/+) rat
            is caused by a missense mutation in Pkdr1 encoding the novel
            protein SamCystin.
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Brown,J.H., Bihoreau,M.T., Hoffmann,S., Kranzlin,B.,
            Tychinskaya,I., Obermuller,N., Podlich,D., Boehn,S.N.,
            Kaisaki,P.J., Megel,N., Danoy,P., Copley,R.R., Broxholme,J.,
            Witzgall,R., Lathrop,M., Gretz,N. and Gauguier,D.
  TITLE     Missense mutation in sterile alpha motif of novel protein SamCystin
            is associated with polycystic kidney disease in (cy/+) rat
  JOURNAL   J Am Soc Nephrol 16 (12), 3517-3526 (2005)
   PUBMED   16207829
REFERENCE   9  (residues 1 to 885)
  AUTHORS   Bihoreau,M.T., Ceccherini,I., Browne,J., Kranzlin,B., Romeo,G.,
            Lathrop,G.M., James,M.R. and Gretz,N.
  TITLE     Location of the first genetic locus, PKDr1, controlling autosomal
            dominant polycystic kidney disease in Han:SPRD cy/+ rat
  JOURNAL   Hum Mol Genet 6 (4), 609-613 (1997)
   PUBMED   9097967
REFERENCE   10 (residues 1 to 885)
  AUTHORS   Schafer,K., Gretz,N., Bader,M., Oberbaumer,I., Eckardt,K.U.,
            Kriz,W. and Bachmann,S.
  TITLE     Characterization of the Han:SPRD rat model for hereditary
            polycystic kidney disease
  JOURNAL   Kidney Int 46 (1), 134-152 (1994)
   PUBMED   7933831
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY661303.1.
            
            On or before Dec 3, 2005 this sequence version replaced
            XP_342834.2, NP_001015028.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY661303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..885
                     /product="ankyrin repeat and SAM domain-containing protein
                     6"
                     /note="samcystin; polycystic kidney disease protein 1;
                     sterile alpha motif domain-containing protein 6; SAM
                     domain-containing protein 6"
                     /calculated_mol_wt=93662
     Region          8..37
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          9..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <43..268
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          68..97
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          69..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(70,74..75,78..80,82..83,87,90,99,101,103,107..108,
                     111..113,115..116,120,123,132,134,136,140..141,144..146,
                     148..149,153,156,165)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          101..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          101..130
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Site            129
                     /site_type="hydroxylation"
                     /note="3-hydroxyasparagine.
                     /evidence=ECO:0000269|PubMed:23793029; propagated from
                     UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          134..165
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          134..163
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          167..210
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          181..210
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          214..244
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          215..244
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          282..312
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          287..380
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(292..294,296..297,301,304,314,316,318,322..323,
                     326..328,330..331,335,338,347,350,352,356..357,360..362,
                     364..365,369,372)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          316..347
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          316..345
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          350..380
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          350..379
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          355..>420
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          383..414
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          383..411
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          415..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          491..522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          563..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68DC2; propagated from
                     UniProtKB/Swiss-Prot (P0C0T2.2)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68DC2; propagated from
                     UniProtKB/Swiss-Prot (P0C0T2.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68DC2; propagated from
                     UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          771..835
                     /region_name="SAM_ANKS6"
                     /note="SAM domain of ANKS6 (or SamCystin) subfamily;
                     cd09518"
                     /db_xref="CDD:188917"
     Site            823
                     /site_type="other"
                     /note="Essential for ANKS3 interaction.
                     /evidence=ECO:0000269|PubMed:26327442; propagated from
                     UniProtKB/Swiss-Prot (P0C0T2.2)"
     Region          855..885
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0T2.2)"
     CDS             1..885
                     /gene="Anks6"
                     /gene_synonym="Pkdr1; Samd6"
                     /coded_by="NM_001015028.2:152..2809"
                     /db_xref="GeneID:362515"
                     /db_xref="RGD:3334"
ORIGIN      
        1 mgegalapgl qlllraceqg dtdtarrlle pggepvagse agaepagpea araveagtpv
       61 pvdcsdeagn salqlaaagg heplvrfllr rgasvnsrnh ygwsalmqaa rcghasvahl
      121 lldhgadvna qnrlgasvlt vasrgghlgv vkllleagat vdhrnpsges tasggsrdel
      181 lgitalmaav qhgheavvrl lmewgadpnh tartvgwspl mlaallgkls vvqqlvekga
      241 npdhlgvlek tafevaldrk hrdladyldp lttvrpktde ekrrpdifha lkmgnfqlvk
      301 eiadedpnhv nlvngdgatp lmlaavtgql plvqllvekh admnkqdsvh gwtalmqaty
      361 hgnkeivkyl lnqgadvtlr akngytafdl vmllndpdte lvrllasvcm qvnkdrggrp
      421 shrpplphsk arqpwsipml pddkgglksw wsrmsnrfrk lklmqtlprg laanqplpfs
      481 depelaldst mrappqdrtn hlgppeaaha akdsgpgnpr rekddvlltt mlrngapfpr
      541 lpsdklkavi ppflppssfe lwssdrsrtc pngkadpmkt vlpprasrah pvgcvgtdga
      601 agrpvkfpsi srsptspass gnfnhsphss ggasgvgsms rlggelhnrs ggsvdsvlsq
      661 iaaqrkkaag lceqkppcqq sspvgpatgs sppelpasll gsgsgssnvt ssskkldpgk
      721 rppsgtsats kstsptltps pspkghtaes svssssshrq skssggsssg titdedeltg
      781 ilkklsleky qpifeeqevd meafltltdg dlqelgiktd gsrqqilaai selnagkgre
      841 rqilqetihn fhssfessas ntrapgnsps magwvrpeet vssrr
//
LOCUS       NP_001120921             375 aa            linear   ROD 27-APR-2025
DEFINITION  actin, cytoplasmic 2 [Rattus norvegicus].
ACCESSION   NP_001120921 XP_001058533 XP_001076100
VERSION     NP_001120921.1
DBSOURCE    REFSEQ: accession NM_001127449.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Mahuzier,A., Shihavuddin,A., Fournier,C., Lansade,P., Faucourt,M.,
            Menezes,N., Meunier,A., Garfa-Traore,M., Carlier,M.F.,
            Voituriez,R., Genovesio,A., Spassky,N. and Delgehyr,N.
  TITLE     Ependymal cilia beating induces an actin network to protect
            centrioles against shear stress
  JOURNAL   Nat Commun 9 (1), 2279 (2018)
   PUBMED   29891944
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Rainger,J., Williamson,K.A., Soares,D.C., Truch,J., Kurian,D.,
            Gillessen-Kaesbach,G., Seawright,A., Prendergast,J., Halachev,M.,
            Wheeler,A., McTeir,L., Gill,A.C., van Heyningen,V., Davey,M.G. and
            FitzPatrick,D.R.
  CONSRTM   UK10K
  TITLE     A recurrent de novo mutation in ACTG1 causes isolated ocular
            coloboma
  JOURNAL   Hum Mutat 38 (8), 942-946 (2017)
   PUBMED   28493397
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Wu,X.S., Lee,S.H., Sheng,J., Zhang,Z., Zhao,W.D., Wang,D., Jin,Y.,
            Charnay,P., Ervasti,J.M. and Wu,L.G.
  TITLE     Actin Is Crucial for All Kinetically Distinguishable Forms of
            Endocytosis at Synapses
  JOURNAL   Neuron 92 (5), 1020-1035 (2016)
   PUBMED   27840001
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Pasquier,E., Tuset,M.P., Sinnappan,S., Carnell,M., Macmillan,A. and
            Kavallaris,M.
  TITLE     gamma-Actin plays a key role in endothelial cell motility and
            neovessel maintenance
  JOURNAL   Vasc Cell 7, 2 (2015)
   PUBMED   25705373
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Micheva,K.D., Vallee,A., Beaulieu,C., Herman,I.M. and Leclerc,N.
  TITLE     beta-Actin is confined to structures having high capacity of
            remodelling in developing and adult rat cerebellum
  JOURNAL   Eur J Neurosci 10 (12), 3785-3798 (1998)
   PUBMED   9875357
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Mandai,K., Nakanishi,H., Satoh,A., Obaishi,H., Wada,M.,
            Nishioka,H., Itoh,M., Mizoguchi,A., Aoki,T., Fujimoto,T.,
            Matsuda,Y., Tsukita,S. and Takai,Y.
  TITLE     Afadin: A novel actin filament-binding protein with one PDZ domain
            localized at cadherin-based cell-to-cell adherens junction
  JOURNAL   J Cell Biol 139 (2), 517-528 (1997)
   PUBMED   9334353
  REMARK    Erratum:[J Cell Biol 1997 Nov 17;139(4):1060]
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Weinstock,R.S., Saville,C.M. and Messina,J.L.
  TITLE     Role of cytosolic calcium in regulation of cytoskeletal gene
            expression by insulin
  JOURNAL   Am J Physiol 264 (4 Pt 1), E519-E525 (1993)
   PUBMED   8476030
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Brown,C.W., McHugh,K.M. and Lessard,J.L.
  TITLE     A cDNA sequence encoding cytoskeletal gamma-actin from rat
  JOURNAL   Nucleic Acids Res 18 (17), 5312 (1990)
   PUBMED   2402472
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Akamizu,T., Saji,M. and Kohn,L.D.
  TITLE     A microsequencing approach to identify proteins which appear to
            interact with thyrotropin in rat FRTL-5 thyroid cells
  JOURNAL   Biochem Biophys Res Commun 170 (1), 351-358 (1990)
   PUBMED   2372296
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK595239.1, CK364554.1 and CF110974.1.
            
            On or before May 21, 2008 this sequence version replaced
            XP_001076100.1, XP_001058533.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00155330,
                              SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..375
                     /product="actin, cytoplasmic 2"
                     /note="gamma-actin; actin, gamma, cytoplasmic 1"
                     /calculated_mol_wt=41662
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P63261; propagated from
                     UniProtKB/Swiss-Prot (P63259.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglutamate, in Actin, cytoplasmic 2,
                     N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P63261; propagated from
                     UniProtKB/Swiss-Prot (P63259.1)"
     Region          6..370
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     Site            73
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000250|UniProtKB:P63258; propagated from
                     UniProtKB/Swiss-Prot (P63259.1)"
     Site            84
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63261; propagated from
                     UniProtKB/Swiss-Prot (P63259.1)"
     CDS             1..375
                     /gene="Actg1"
                     /gene_synonym="Actg"
                     /coded_by="NM_001127449.1:75..1202"
                     /db_xref="GeneID:287876"
                     /db_xref="RGD:1304556"
ORIGIN      
        1 meeeiaalvi dngsgmckag fagddaprav fpsivgrprh qgvmvgmgqk dsyvgdeaqs
       61 krgiltlkyp iehgivtnwd dmekiwhhtf ynelrvapee hpvllteapl npkanrekmt
      121 qimfetfntp amyvaiqavl slyasgrttg ivmdsgdgvt htvpiyegya lphailrldl
      181 agrdltdylm kiltergysf tttaereivr dikeklcyva ldfeqemata assssleksy
      241 elpdgqviti gnerfrcpea lfqpsflgme scgihettfn simkcdvdir kdlyantvls
      301 ggttmypgia drmqkeital apstmkikii apperkysvw iggsilasls tfqqmwiskq
      361 eydesgpsiv hrkcf
//
LOCUS       NP_001094055             329 aa            linear   ROD 27-APR-2025
DEFINITION  CAAX prenyl protease 2 [Rattus norvegicus].
ACCESSION   NP_001094055 XP_001071802 XP_219685
VERSION     NP_001094055.1
DBSOURCE    REFSEQ: accession NM_001100585.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Burrows,J.F., Kelvin,A.A., McFarlane,C., Burden,R.E.,
            McGrattan,M.J., De la Vega,M., Govender,U., Quinn,D.J., Dib,K.,
            Gadina,M., Scott,C.J. and Johnston,J.A.
  TITLE     USP17 regulates Ras activation and cell proliferation by blocking
            RCE1 activity
  JOURNAL   J Biol Chem 284 (14), 9587-9595 (2009)
   PUBMED   19188362
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC158593.1 and BC087629.1.
            
            On or before May 31, 2008 this sequence version replaced
            XP_001071802.1, XP_219685.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087629.1, CK596437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..329
                     /product="CAAX prenyl protease 2"
                     /EC_number="3.4.26.1"
                     /note="FACE-2; prenyl protein-specific endoprotease 2;
                     farnesylated proteins-converting enzyme 2; RCE1 homolog,
                     prenyl protein peptidase; RCE1 homolog, prenyl protein
                     protease"
                     /calculated_mol_wt=35919
     Region          164..267
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
     CDS             1..329
                     /gene="Rce1"
                     /coded_by="NM_001100585.1:12..1001"
                     /db_xref="GeneID:309153"
                     /db_xref="RGD:1309261"
ORIGIN      
        1 maalggdglr llsvsrperq pesaalsspg pglccwvsvf scfslacsyv gslyvwksel
       61 prdhpavikr rftsvlvvss lsplcvllwr eltgiqpgts lltlmgfrle gifpaallpl
      121 lltmilflgp lmqlcmdcpc dltdglkvvl aprswarrlt dmrwlrnqvi aplteelvfr
      181 acmlpmlapc tglgpavftc plffgvahfh hiieqlrfrq ssvgsiflsa afqfsytavf
      241 gaytaflfir tghligpvlc hsfcnymgfp avcaalehpq kwpllagyal gvglfllllq
      301 pltdpklygs lplcmllert gasetllcs
//
LOCUS       NP_001013922             244 aa            linear   ROD 27-APR-2025
DEFINITION  INO80 complex subunit E [Rattus norvegicus].
ACCESSION   NP_001013922 XP_215078
VERSION     NP_001013922.1
DBSOURCE    REFSEQ: accession NM_001013900.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079045.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215078.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079045.1, FQ223207.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..244
                     /product="INO80 complex subunit E"
                     /note="coiled-coil domain-containing protein 95;
                     coiled-coil domain containing 95"
                     /calculated_mol_wt=26227
     Region          59..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH2.1)"
     CDS             1..244
                     /gene="Ino80e"
                     /gene_synonym="Ccdc95"
                     /coded_by="NM_001013900.1:122..856"
                     /db_xref="GeneID:293494"
                     /db_xref="RGD:1359572"
ORIGIN      
        1 mngpadgevd ykkkyrnlkr klkfliyehe cfqeelrkaq rkllkvsrdk sflldrllqy
       61 envdedssds datassdnse tegtpklsdt papkrkrspp mggapspssl slppssgfpl
      121 qtsgapspyl sslasppypp fpsdylalql pepsplrpkl ekrprlprkl kmavgppdcp
      181 vggplafpar gsgasvgaal tplpppkmpp htilstvpqq mfsdagsgdd aldgdddlvi
      241 dipe
//
LOCUS       NP_001034543             432 aa            linear   ROD 27-APR-2025
DEFINITION  PC-esterase domain-containing protein 1B [Rattus norvegicus].
ACCESSION   NP_001034543 XP_235668
VERSION     NP_001034543.1
DBSOURCE    REFSEQ: accession NM_001039454.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC112322.1.
            
            On Feb 7, 2006 this sequence version replaced XP_235668.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112322.1, DN935280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..432
                     /product="PC-esterase domain-containing protein 1B"
                     /note="protein FAM113B; family with sequence similarity
                     113, member B; translation initiation factor IF-2-like"
                     /calculated_mol_wt=49844
     Region          17..253
                     /region_name="SGNH_hydrolase"
                     /note="or GDSL_hydrolase, is a diverse family of lipases
                     and esterases. The tertiary fold of the enzyme is
                     substantially different from that of the alpha/beta
                     hydrolase family and unique among all known hydrolases;
                     its active site closely resembles the typical...; cl01053"
                     /db_xref="CDD:470049"
     Site            order(24,64,126,232,235)
                     /site_type="active"
                     /db_xref="CDD:238141"
     Site            order(24,232,235)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238141"
     Site            order(24,64,126)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238141"
     Region          273..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1K5.1)"
     Region          407..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1K5.1)"
     CDS             1..432
                     /gene="Pced1b"
                     /gene_synonym="Fam113b; RGD1561028"
                     /coded_by="NM_001039454.1:409..1707"
                     /db_xref="GeneID:315283"
                     /db_xref="RGD:1561028"
ORIGIN      
        1 mvrllasevq qllhnkfvvv lgdsvhravy kdlvlllqkd clltnkqlrt kgelsfekdq
       61 lmmggeldtl hnrtdyrevr efcsdhhlvr fyfltrvyse ymesvlkelq sgnhapdvii
      121 mnsclwdvsr ygrnslssyr qnlenlfgrm devlpkscll vwntamplgd kikaaflpqk
      181 ckgqyprisv atlkkkvtqa nfyshaeatk hyfdvldlnf hfrqarkhlq gdgvhwneha
      241 hrklsyllla hmadawgvel phrdpwepgf eawessgqve erqpqdnigp qfaqsppypf
      301 prpppllpsp glpirpppll gcplpppqpm pplplypqvs yfssdpvfqs defyihsdsp
      361 ssnhtgyafe gdfsfypqpp mpnfrppchq rqapvvhrgf prhfprgpym pwrerprrpq
      421 khapaclesr pq
//
LOCUS       NP_001008309             577 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger-containing ubiquitin peptidase 1 [Rattus norvegicus].
ACCESSION   NP_001008309 XP_215390
VERSION     NP_001008309.1
DBSOURCE    REFSEQ: accession NM_001008308.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085885.1.
            
            On Dec 16, 2004 this sequence version replaced XP_215390.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..577
                     /product="zinc finger-containing ubiquitin peptidase 1"
                     /EC_number="3.4.19.12"
                     /note="zinc finger with UFM1-specific peptidase domain
                     protein; lys-63-specific deubiquitinase ZUFSP; ubiquitin
                     carboxyl-terminal hydrolase ZUFSP"
                     /calculated_mol_wt=65591
     Region          225..247
                     /region_name="MIU. /evidence=ECO:0000250|UniProtKB:Q96AP4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S3.1)"
     Region          231..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S3.1)"
     Region          248..273
                     /region_name="zUBD/ZHA.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S3.1)"
     Site            261
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S3.1)"
     Region          335..550
                     /region_name="Peptidase_C78"
                     /note="Peptidase family C78; pfam07910"
                     /db_xref="CDD:400318"
     Site            486
                     /site_type="other"
                     /note="Involved in the stabilization of negative charge on
                     the oxyanion by the formation of the oxyanion hole.
                     /evidence=ECO:0000250|UniProtKB:Q96AP4; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S3.1)"
     CDS             1..577
                     /gene="Zup1"
                     /gene_synonym="DUB; RGD1307672; Zufsp"
                     /coded_by="NM_001008308.1:89..1822"
                     /db_xref="GeneID:294390"
                     /db_xref="RGD:1307672"
ORIGIN      
        1 mlscdicget vtsepdrkah livhmeneii cpfcklsgin ynemcfhiet ahfeqttpek
       61 sfetlaavqy ensdlgntkl hstvevtsgi hsacasnfpk esseslskdr tlkqeafyte
      121 svaesrkyqk srekqsglse aqgsiyetty sppecpfcgr ierysqdmei hvktkhasll
      181 espledchqp lydcpmcglv ctnyhilqeh vdlhleessf qqgmdrvqcs sdrelahqlq
      241 qeeerkrkse esrqereefq klqrqygldn sggykqqqlr hmelevtrgr mhpsefhsrk
      301 admlesiavg iddgktktsg iiealhryyq niatdvrcvw lstvvdhfhs sfgdkgwgcg
      361 yrnfqmllss llqnevysdc lkgmsvpcip kiqsmiedaw negfdpqgas qlnnklqgtk
      421 awigaceiyt lltslkvkcr iidfhkstgp sgthprlfew ilnyyssete gapkvvctsk
      481 ppvylqhqgh srtvvgieer knrtlcllif dpgcpsremq kllkqdmeag slrqlrkcvg
      541 nlkhkqyqiv avegilspee raarkqasqv ftaekip
//
LOCUS       NP_062153                356 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction alpha-5 protein [Rattus norvegicus].
ACCESSION   NP_062153 XP_001063632
VERSION     NP_062153.1
DBSOURCE    REFSEQ: accession NM_019280.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Ma,J., Ma,S., Yin,C. and Wu,H.
  TITLE     Shengmai San-derived herbal prevents the development of a
            vulnerable substrate for atrial fibrillation in a rat model of
            ischemic heart failure
  JOURNAL   Biomed Pharmacother 100, 156-167 (2018)
   PUBMED   29428663
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Zhou,H.S., Li,M., Sui,B.D., Wei,L., Hou,R., Chen,W.S., Li,Q.,
            Bi,S.H., Zhang,J.Z. and Yi,D.H.
  TITLE     Lipopolysaccharide impairs permeability of pulmonary microvascular
            endothelial cells via Connexin40
  JOURNAL   Microvasc Res 115, 58-67 (2018)
   PUBMED   28870649
  REMARK    GeneRIF: Lipopolysaccharide impairs permeability of pulmonary
            microvascular endothelial cells via Connexin40/protein kinase
            C/nfkappaB pathway.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Kanthan,A., Fahmy,P., Rao,R., Pouliopoulos,J., Alexander,I.E.,
            Thomas,S.P. and Kizana,E.
  TITLE     Human Connexin40 Mutations Slow Conduction and Increase Propensity
            for Atrial Fibrillation
  JOURNAL   Heart Lung Circ 27 (1), 114-121 (2018)
   PUBMED   28457700
  REMARK    GeneRIF: The A96S, G38D, and P88S Cx40 mutations slow conduction
            and increased the propensity for inducible AF.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Chen,W., Guo,Y., Yang,W., Zheng,P., Zeng,J. and Tong,W.
  TITLE     Connexin40 correlates with oxidative stress in brains of traumatic
            brain injury rats
  JOURNAL   Restor Neurol Neurosci 35 (2), 217-224 (2017)
   PUBMED   28157110
  REMARK    GeneRIF: This study demonstrated the Cx40 was upregulated after
            traumatic brain injury in a linear correlated manner with increased
            oxidative stress.
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Xu,Q., Lin,X., Matiukas,A., Zhang,X. and Veenstra,R.D.
  TITLE     Specificity of the connexin W3/4 locus for functional gap junction
            formation
  JOURNAL   Channels (Austin) 10 (6), 453-465 (2016)
   PUBMED   27304225
  REMARK    GeneRIF: data are consistent with contributions of G2 and D3
            residues to Cx40 channel pore structure, but not with postulated
            hydrophobic W4 intermolecular interactions; results indicate an
            absolute requirement for an amphipathic W3/4 residue; alternatively
            hypothesize that the connexin D2/3-W3/4 locus interacts with the
            highly conserved FIFR M1 motif to stabilize the NT domain within
            the pore
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Beblo,D.A., Wang,H.Z., Beyer,E.C., Westphale,E.M. and Veenstra,R.D.
  TITLE     Unique conductance, gating, and selective permeability properties
            of gap junction channels formed by connexin40
  JOURNAL   Circ Res 77 (4), 813-822 (1995)
   PUBMED   7554128
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Davis,L.M., Kanter,H.L., Beyer,E.C. and Saffitz,J.E.
  TITLE     Distinct gap junction protein phenotypes in cardiac tissues with
            disparate conduction properties
  JOURNAL   J Am Coll Cardiol 24 (4), 1124-1132 (1994)
   PUBMED   7930207
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Beyer,E.C., Reed,K.E., Westphale,E.M., Kanter,H.L. and Larson,D.M.
  TITLE     Molecular cloning and expression of rat connexin40, a gap junction
            protein expressed in vascular smooth muscle
  JOURNAL   J Membr Biol 127 (1), 69-76 (1992)
   PUBMED   1328644
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Kanter,H.L., Saffitz,J.E. and Beyer,E.C.
  TITLE     Cardiac myocytes express multiple gap junction proteins
  JOURNAL   Circ Res 70 (2), 438-444 (1992)
   PUBMED   1310450
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Haefliger,J.A., Bruzzone,R., Jenkins,N.A., Gilbert,D.J.,
            Copeland,N.G. and Paul,D.L.
  TITLE     Four novel members of the connexin family of gap junction proteins.
            Molecular cloning, expression, and chromosome mapping
  JOURNAL   J Biol Chem 267 (3), 2057-2064 (1992)
   PUBMED   1370487
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF021806.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001063632.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF021806.1, CK365277.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..356
                     /product="gap junction alpha-5 protein"
                     /note="connexin 40; connexin i; gap junction membrane
                     channel protein alpha 5"
                     /calculated_mol_wt=40102
     Region          3..230
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Region          241..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Region          255..356
                     /region_name="Connexin40_C"
                     /note="Connexin 40 C-terminal domain; pfam16791"
                     /db_xref="CDD:465272"
     Region          279..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28234.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P28234.2)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P28234.2)"
     CDS             1..356
                     /gene="Gja5"
                     /gene_synonym="Cx40; Cxni"
                     /coded_by="NM_019280.1:91..1161"
                     /db_xref="GeneID:50563"
                     /db_xref="RGD:2692"
ORIGIN      
        1 mgdwsflgef leevhkhstv igkvwltvlf ifrmlvlgta aesswgdeqa dfrcdtiqpg
       61 cqnvcydqaf pishirywvl qiifvstpsl vymghamhtv rmqekqklre aekakeaggt
      121 gtyeylaeka elscwkevng kivlqgtlln tyvctilirt amevafmvgq yllygifldt
      181 lhvcrrspcp hpvncyvsrp teknvfivfm mavaglslfl slaelyhlgw kkirqrlaks
      241 rqgdkhqllg pstslvqglt pppdfnqclk nspdekffsd fsnnmgsrkn pdplateevp
      301 nqeqipeegf ihtqygqkpe qpsgasaghr fpqgyhsdkr rlskasskar sddlsv
//
LOCUS       NP_113735                478 aa            linear   ROD 27-APR-2025
DEFINITION  muscarinic acetylcholine receptor M4 [Rattus norvegicus].
ACCESSION   NP_113735 XP_001078223 XP_345404
VERSION     NP_113735.1
DBSOURCE    REFSEQ: accession NM_031547.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Brugnoli,A., Pisano,C.A. and Morari,M.
  TITLE     Striatal and nigral muscarinic type 1 and type 4 receptors modulate
            levodopa-induced dyskinesia and striato-nigral pathway activation
            in 6-hydroxydopamine hemilesioned rats
  JOURNAL   Neurobiol Dis 144, 105044 (2020)
   PUBMED   32798726
  REMARK    GeneRIF: Striatal and nigral muscarinic type 1 and type 4 receptors
            modulate levodopa-induced dyskinesia and striato-nigral pathway
            activation in 6-hydroxydopamine hemilesioned rats.
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Lima,J.D., Sobrinho,C.R., Santos,L.K., Takakura,A.C. and
            Moreira,T.S.
  TITLE     M4-muscarinic acetylcholine receptor into the pedunculopontine
            tegmental nucleus mediates respiratory modulation of conscious rats
  JOURNAL   Respir Physiol Neurobiol 269, 103254 (2019)
   PUBMED   31325565
  REMARK    GeneRIF: Our data suggest that the changes in respiratory frequency
            and tidal volume produced by muscarinic cholinergic stimulation of
            the pedunculopontine tegmental nucleus is presumably mediated
            through a Gi-coupled M4 muscarinic receptors.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   He,N., Mao,L.M., Sturich,A.W., Jin,D.Z. and Wang,J.Q.
  TITLE     Inhibition of basal and amphetamine-stimulated extracellular
            signal-regulated kinase (ERK) phosphorylation in the rat forebrain
            by muscarinic acetylcholine M4 receptors
  JOURNAL   Brain Res 1688, 103-112 (2018)
   PUBMED   29577888
  REMARK    GeneRIF: Study showed that the muscarinic M4 receptor-preferring
            antagonist tropicamide consistently increased ERK phosphorylation
            in the striatum and medial prefrontal cortex.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Thiele,A.
  TITLE     Muscarinic signaling in the brain
  JOURNAL   Annu Rev Neurosci 36, 271-294 (2013)
   PUBMED   23841840
  REMARK    Review article
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Kovalenko,N.Y., Matsievskii,D.D. and Reshetnyak,V.K.
  TITLE     Role of various subtypes of muscarinic cholinergic receptors in the
            development of posthemorrhagic abnormalities in systemic and portal
            circulation in rats
  JOURNAL   Bull Exp Biol Med 152 (3), 293-297 (2012)
   PUBMED   22803069
  REMARK    GeneRIF: M1 and M4 muscarinic receptors are involved in
            shock-limiting and shock-activating processes, respectively, on the
            course of posthemorrhagic abnormalities in systemic and hepatic
            portal circulation.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Szpirer,C., Szpirer,J., Van Vooren,P., Tissir,F., Simon,J.S.,
            Koike,G., Jacob,H.J., Lander,E.S., Helou,K., Klinga-Levan,K. and
            Levan,G.
  TITLE     Gene-based anchoring of the rat genetic linkage and cytogenetic
            maps: new regional localizations, orientation of the linkage
            groups, and insights into mammalian chromosome evolution
  JOURNAL   Mamm Genome 9 (9), 721-734 (1998)
   PUBMED   9716657
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Mieda,M., Haga,T. and Saffen,D.W.
  TITLE     Promoter region of the rat m4 muscarinic acetylcholine receptor
            gene contains a cell type-specific silencer element
  JOURNAL   J Biol Chem 271 (9), 5177-5182 (1996)
   PUBMED   8617799
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hersch,S.M., Gutekunst,C.A., Rees,H.D., Heilman,C.J. and Levey,A.I.
  TITLE     Distribution of m1-m4 muscarinic receptor proteins in the rat
            striatum: light and electron microscopic immunocytochemistry using
            subtype-specific antibodies
  JOURNAL   J Neurosci 14 (5 Pt 2), 3351-3363 (1994)
   PUBMED   8182478
REFERENCE   9  (residues 1 to 478)
  AUTHORS   van Koppen,C.J., Lenz,W. and Nathanson,N.M.
  TITLE     Isolation, sequence and functional expression of the mouse m4
            muscarinic acetylcholine receptor gene
  JOURNAL   Biochim Biophys Acta 1173 (3), 342-344 (1993)
   PUBMED   7916637
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bonner,T.I., Buckley,N.J., Young,A.C. and Brann,M.R.
  TITLE     Identification of a family of muscarinic acetylcholine receptor
            genes
  JOURNAL   Science 237 (4814), 527-532 (1987)
   PUBMED   3037705
  REMARK    Erratum:[Science 1987 Sep 25;237(4822):237]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV213670.1, M16409.1 and CR472483.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_345404.3, XP_001078223.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV213670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..478
                     /product="muscarinic acetylcholine receptor M4"
                     /note="cholinergic receptor, muscarin 4"
                     /calculated_mol_wt=52764
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08485.1)"
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08485.1)"
     Site            31..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          32..463
                     /region_name="7tmA_mAChR_M4"
                     /note="muscarinic acetylcholine receptor subtype M4,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15298"
                     /db_xref="CDD:341344"
     Region          33..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341344"
     Region          66..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341344"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          104..134
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341344"
     Site            106..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Site            order(111..112,115..116,163,195,198..199,202..203,412,
                     415..416,438,441..442)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:341344"
     Region          146..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341344"
     Site            148..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          191..220
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341344"
     Site            193..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          271..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          392..422
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341344"
     Site            401..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Region          431..456
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341344"
     Site            436..455
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08485.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P08485.1)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P08485.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P08485.1)"
     CDS             1..478
                     /gene="Chrm4"
                     /gene_synonym="M4"
                     /coded_by="NM_031547.1:175..1611"
                     /db_xref="GeneID:25111"
                     /db_xref="RGD:2344"
ORIGIN      
        1 manftpvngs sanqsvrlvt aahnhletve mvfiatvtgs lslvtvvgni lvmlsikvnr
       61 qlqtvnnyfl fslacadlii gafsmnlytl yiikgywplg avvcdlwlal dyvvsnasvm
      121 nlliisfdry fcvtkpltyp arrttkmagl miaaawvlsf vlwapailfw qfvvgkrtvp
      181 dnqcfiqfls npavtfgtai aafylpvvim tvlyihisla srsrvhkhrp egpkekkakt
      241 laflksplmk psikkpppgg asreelrngk leeapppalp ppprpvpdkd tsnesssgsa
      301 tqntkerppt elstaeattp alpaptlqpr tlnpaskwsk iqivtkqtgn ecvtaieivp
      361 atpagmrpaa nvarkfasia rnqvrkkrqm aarerkvtrt ifaillafil twtpynvmvl
      421 vntfcqscip ervwsigywl cyvnstinpa cyalcnatfk ktfrhlllcq yrnigtar
//
LOCUS       NP_062233                 76 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c oxidase subunit 6C-2 [Rattus norvegicus].
ACCESSION   NP_062233
VERSION     NP_062233.2
DBSOURCE    REFSEQ: accession NM_019360.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Zong,S., Wu,M., Gu,J., Liu,T., Guo,R. and Yang,M.
  TITLE     Structure of the intact 14-subunit human cytochrome c oxidase
  JOURNAL   Cell Res 28 (10), 1026-1034 (2018)
   PUBMED   30030519
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Lau,N.C., Seto,A.G., Kim,J., Kuramochi-Miyagawa,S., Nakano,T.,
            Bartel,D.P. and Kingston,R.E.
  TITLE     Characterization of the piRNA complex from rat testes
  JOURNAL   Science 313 (5785), 363-367 (2006)
   PUBMED   16778019
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Farkas,R.H., Qian,J., Goldberg,J.L., Quigley,H.A. and Zack,D.J.
  TITLE     Gene expression profiling of purified rat retinal ganglion cells
  JOURNAL   Invest Ophthalmol Vis Sci 45 (8), 2503-2513 (2004)
   PUBMED   15277470
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Sheehan,T.E., Kumar,P.A. and Hood,D.A.
  TITLE     Tissue-specific regulation of cytochrome c oxidase subunit
            expression by thyroid hormone
  JOURNAL   Am J Physiol Endocrinol Metab 286 (6), E968-E974 (2004)
   PUBMED   14970006
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Crosignani,P.
  TITLE     [Malignant breast tumors in the population of the province of
            Varese from 01/01/76 to 12/31/87]
  JOURNAL   Pathologica 84 (1094), 1-9 (1992)
   PUBMED   1300526
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Suske,G., Enders,C., Schlerf,A. and Kadenbach,B.
  TITLE     Organization and nucleotide sequence of two chromosomal genes for
            rat cytochrome c oxidase subunit VIc: a structural and a processed
            gene
  JOURNAL   DNA 7 (3), 163-171 (1988)
   PUBMED   2836143
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Cao,X.N., Hengst,L., Schlerf,A., Droste,M., Mengel,T. and
            Kadenbach,B.
  TITLE     Complexity of nucleus-encoded genes of mammalian cytochrome c
            oxidase
  JOURNAL   Ann N Y Acad Sci 550, 337-347 (1988)
   PUBMED   2854406
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Suske,G., Mengel,T., Cordingley,M. and Kadenbach,B.
  TITLE     Molecular cloning and further characterization of cDNAs for rat
            nuclear-encoded cytochrome c oxidase subunits VIc and VIII
  JOURNAL   Eur J Biochem 168 (1), 233-237 (1987)
   PUBMED   2822403
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Parimoo,S., Seelan,R.S., Desai,S., Buso,G. and Padmanaban,G.
  TITLE     Construction of a cDNA clone for a nuclear-coded subunit of
            cytochrome c oxidase from rat liver
  JOURNAL   Biochem Biophys Res Commun 118 (3), 902-909 (1984)
   PUBMED   6200111
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CF976717.1, BC058480.1 and AI716762.1.
            
            On Nov 15, 2007 this sequence version replaced NP_062233.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF976718.1, FQ217805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..76
                     /product="cytochrome c oxidase subunit 6C-2"
                     /note="cytochrome c oxidase polypeptide VIc-2; cytochrome
                     oxidase subunit VIc; cytochrome c oxidase, subunit VIc"
                     /calculated_mol_wt=8324
     Region          7..75
                     /region_name="COX6C"
                     /note="Cytochrome c oxidase subunit VIc; pfam02937"
                     /db_xref="CDD:460756"
     Site            15..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11951.3)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11951.3)"
     CDS             1..76
                     /gene="Cox6c"
                     /gene_synonym="COVIc; COX-VIc; Cox6c2"
                     /coded_by="NM_019360.2:85..315"
                     /db_xref="GeneID:54322"
                     /db_xref="RGD:620616"
ORIGIN      
        1 mssgallpkp qmrgllakrl rvhivgafvv algvaaaykf gvaeprkkay adfyrnydsm
       61 kdfeemrqag vfqsak
//
LOCUS       NP_001017498             454 aa            linear   ROD 27-APR-2025
DEFINITION  sperm microtubule associated protein 2-like [Rattus norvegicus].
ACCESSION   NP_001017498 XP_573583
VERSION     NP_001017498.1
DBSOURCE    REFSEQ: accession NM_001017498.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087065.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573583.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..454
                     /product="sperm microtubule associated protein 2-like"
                     /note="testicular haploid expressed gene protein-like;
                     theg spermatid protein-like; theg spermatid-like protein"
                     /calculated_mol_wt=51107
     Region          1..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          167..185
                     /region_name="THEG 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          168..224
                     /region_name="THEG"
                     /note="Testicular haploid expressed repeat; pfam14912"
                     /db_xref="CDD:464368"
     Region          203..270
                     /region_name="THEG"
                     /note="Testicular haploid expressed repeat; pfam14912"
                     /db_xref="CDD:464368"
     Region          207..226
                     /region_name="THEG 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          253..272
                     /region_name="THEG 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          284..339
                     /region_name="THEG"
                     /note="Testicular haploid expressed repeat; pfam14912"
                     /db_xref="CDD:464368"
     Region          286..305
                     /region_name="THEG 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          322..341
                     /region_name="THEG 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          358..414
                     /region_name="THEG"
                     /note="Testicular haploid expressed repeat; pfam14912"
                     /db_xref="CDD:464368"
     Region          362..381
                     /region_name="THEG 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          393..452
                     /region_name="THEG"
                     /note="Testicular haploid expressed repeat; pfam14912"
                     /db_xref="CDD:464368"
     Region          398..417
                     /region_name="THEG 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     Region          435..454
                     /region_name="THEG 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQR6.1)"
     CDS             1..454
                     /gene="Spmap2l"
                     /gene_synonym="Thegl"
                     /coded_by="NM_001017498.1:144..1508"
                     /db_xref="GeneID:498350"
                     /db_xref="RGD:1562571"
ORIGIN      
        1 meegdfsgse psevtdgqnt nttmttetht ttehqpkplv vrllevhncd edeedeeeeq
       61 eedheapkth ksheasvsfk svnssdspka sdlplsckas dflgsskasd psesfkalqs
      121 sesqedvkdd lfsnavirts pslmtgyppq lqltslrahp atrdlvkkcf ysrkrvqdls
      181 rpkkqwgtpd rrlfwgnqep irpvseaalk apsskriedl aqprlvsrhy vpnrvqyyys
      241 cgrdsviwei pppalitqps kriqklakpn rfktqslinr enlpgtlrys dpsprilrls
      301 iakgtdpnyi ppktiqtkis fstlsavasp rivdlahpri kieglcyere rselpirpva
      361 paallanpse rtiflakskr vhedylpvrd arwpisyaat hpqvseriqe lanphtrspt
      421 hvvyydpdvf kvkpsalkah csnrvkelae pivr
//
LOCUS       NP_001009639             176 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin polymerization-promoting protein family member 3 [Rattus
            norvegicus].
ACCESSION   NP_001009639 XP_214677
VERSION     NP_001009639.1
DBSOURCE    REFSEQ: accession NM_001009639.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Shukla,V., Kaushal,J.B., Sankhwar,P., Manohar,M. and Dwivedi,A.
  TITLE     Inhibition of TPPP3 attenuates beta-catenin/NF-kappaB/COX-2
            signaling in endometrial stromal cells and impairs decidualization
  JOURNAL   J Endocrinol 240 (3), 417-429 (2019)
   PUBMED   30667362
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Shukla,V., Popli,P., Kaushal,J.B., Gupta,K. and Dwivedi,A.
  TITLE     Uterine TPPP3 plays important role in embryo implantation via
            modulation of beta-catenin
  JOURNAL   Biol Reprod 99 (5), 982-999 (2018)
   PUBMED   29901777
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Vincze,O., Tokesi,N., Olah,J., Hlavanda,E., Zotter,A., Horvath,I.,
            Lehotzky,A., Tirian,L., Medzihradszky,K.F., Kovacs,J., Orosz,F. and
            Ovadi,J.
  TITLE     Tubulin polymerization promoting proteins (TPPPs): members of a new
            family with distinct structures and functions
  JOURNAL   Biochemistry 45 (46), 13818-13826 (2006)
   PUBMED   17105200
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087585.1.
            
            On Jan 13, 2005 this sequence version replaced XP_214677.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087585.1, FQ214701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..176
                     /product="tubulin polymerization-promoting protein family
                     member 3"
                     /calculated_mol_wt=18848
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW30; propagated from
                     UniProtKB/Swiss-Prot (Q5PPN5.1)"
     Region          11..166
                     /region_name="p25-alpha"
                     /note="pfam05517"
                     /db_xref="CDD:461670"
     CDS             1..176
                     /gene="Tppp3"
                     /gene_synonym="CGI-38; RGD1305061"
                     /coded_by="NM_001009639.1:106..636"
                     /db_xref="GeneID:291966"
                     /db_xref="RGD:1305061"
ORIGIN      
        1 maastdiagl eesfrkfaih gdpkasgqem ngknwaklck dckvadgkav tgtdvdivfs
       61 kvkaksarvi nyeefkkale elatkrfkgk tkeeafdaic qliagkepan igvtkaktgg
      121 avdrltdtsk ytgshkerfd esgkgkgiag rqdilddsgy vsayknagty dakvkk
//
LOCUS       NP_570837                678 aa            linear   ROD 27-APR-2025
DEFINITION  RAS guanyl-releasing protein 4 [Rattus norvegicus].
ACCESSION   NP_570837
VERSION     NP_570837.2
DBSOURCE    REFSEQ: accession NM_130824.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Kono,M., Yasuda,S., Stevens,R.L., Koide,H., Kurita,T., Shimizu,Y.,
            Kanetsuka,Y., Oku,K., Bohgaki,T., Amengual,O., Horita,T.,
            Shimizu,T., Majima,T., Koike,T. and Atsumi,T.
  TITLE     Ras guanine nucleotide-releasing protein 4 is aberrantly expressed
            in the fibroblast-like synoviocytes of patients with rheumatoid
            arthritis and controls their proliferation
  JOURNAL   Arthritis Rheumatol 67 (2), 396-407 (2015)
   PUBMED   25330932
  REMARK    GeneRIF: RasGRP-4 is aberrantly expressed in fibroblast-like
            synoviocytes and helps regulate their growth.
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Li,L., Yang,Y. and Stevens,R.L.
  TITLE     RasGRP4 regulates the expression of prostaglandin D2 in human and
            rat mast cell lines
  JOURNAL   J Biol Chem 278 (7), 4725-4729 (2003)
   PUBMED   12493770
  REMARK    GeneRIF: RasGRP4 regulates the expression of prostaglandin D2 in
            mast cell
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Li,L., Yang,Y. and Stevens,R.L.
  TITLE     Cloning of rat Ras guanine nucleotide releasing protein 4, and
            evaluation of its expression in rat mast cells and their bone
            marrow progenitors
  JOURNAL   Mol Immunol 38 (16-18), 1283-1288 (2002)
   PUBMED   12217396
  REMARK    GeneRIF: Cloning of Ras guanine nucleotide releasing protein 4, and
            evaluation of its expression in mast cells and their bone marrow
            progenitors.
            Review article
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Reuther,G.W., Lambert,Q.T., Rebhun,J.F., Caligiuri,M.A.,
            Quilliam,L.A. and Der,C.J.
  TITLE     RasGRP4 is a novel Ras activator isolated from acute myeloid
            leukemia
  JOURNAL   J Biol Chem 277 (34), 30508-30514 (2002)
   PUBMED   11880369
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF465263.1.
            
            On Mar 15, 2007 this sequence version replaced NP_570837.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF465263.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..678
                     /product="RAS guanyl-releasing protein 4"
                     /calculated_mol_wt=75274
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I4.1)"
     Region          57..172
                     /region_name="REM"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     GTPases; N-terminal domain (RasGef_N), also called REM
                     domain (Ras exchanger motif). This domain is common in
                     nucleotide exchange factors for Ras-like small GTPases and
                     is typically found immediately...; cd06224"
                     /db_xref="CDD:100121"
     Site            order(68,115,119..120,123,126..127,162..163,166)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:100121"
     Region          165..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I4.1)"
     Region          197..432
                     /region_name="RasGEF"
                     /note="Guanine nucleotide exchange factor for Ras-like
                     small GTPases; smart00147"
                     /db_xref="CDD:214539"
     Site            order(230..232,240..241,243..245,247..248,251..252,255,
                     288,291..292,294..296,298..301,303..304,324,327,332..334,
                     337,350..352,355..357,359..361,363..366,381,385,420,
                     423..424)
                     /site_type="other"
                     /note="Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:238087"
     Region          538..599
                     /region_name="C1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     superfamily; cl00040"
                     /db_xref="CDD:412127"
     Region          598..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I4.1)"
     Region          651..678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I4.1)"
     CDS             1..678
                     /gene="Rasgrp4"
                     /coded_by="NM_130824.2:1..2037"
                     /db_xref="GeneID:170668"
                     /db_xref="RGD:620476"
ORIGIN      
        1 mnrkdikrks hqecsgkagg hgrprqarrh ktcptpreis kvmaslnlgv lsesscsvde
       61 lleecircfd sagslhrgdh ilkmvltmhs wvlpssdlaa rlltsyqkaa kdarelrqlq
      121 icylvrywlt hhpevvhqep qleaiinrfw ttvaqegnma qrslgdasnl lspggpgppp
      181 lmsspglgkk rkvsllfdhl eteelaqhlt ylefrsfqai tpqdlrgyvl qgsvrgcpal
      241 egsvglsnsv srwvqvmvls rpgpaqraqv ldkfirvaqr lrqmqnfntl mavtgglchs
      301 aisrlkdshv hlspdstkal leltellssh nnyayyrrtw asctdfrlpv lgvhlkdlvs
      361 lyeahpdrlp dgrlhlpkln slylrlqela alqrqhppcs anedllhllt lsldlfyted
      421 eiyelsyare prcpkslpls pfkapvvvew ahgvtpkpds atlgqhveql vesvfknydp
      481 eghgsisled feklsanfpf achglhpppr hgsgsfsree ltkyllhasa icsklglafl
      541 hafqevtfrk ptfchscngf vstgplwgvt krgyrcqdcg lcchrhcrdq vrveckkrpe
      601 tkgdpgppga pgpatplppt gcgseeglsy tlsphlesgc hlhhawtqte sshsswepem
      661 vpcpapvlps kasskssv
//
LOCUS       NP_997689                351 aa            linear   ROD 27-APR-2025
DEFINITION  1-acylglycerol-3-phosphate O-acyltransferase ABHD5 [Rattus
            norvegicus].
ACCESSION   NP_997689 XP_236775
VERSION     NP_997689.1
DBSOURCE    REFSEQ: accession NM_212524.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Ou,J., Peng,Y., Yang,W., Zhang,Y., Hao,J., Li,F., Chen,Y., Zhao,Y.,
            Xie,X., Wu,S., Zha,L., Luo,X., Xie,G., Wang,L., Sun,W., Zhou,Q.,
            Li,J. and Liang,H.
  TITLE     ABHD5 blunts the sensitivity of colorectal cancer to fluorouracil
            via promoting autophagic uracil yield
  JOURNAL   Nat Commun 10 (1), 1078 (2019)
   PUBMED   30842415
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Dettlaff-Pokora,A., Sledzinski,T. and Swierczynski,J.
  TITLE     Upregulation of Pnpla2 and Abhd5 and downregulation of G0s2 gene
            expression in mesenteric white adipose tissue as a potential reason
            for elevated concentration of circulating NEFA after removal of
            retroperitoneal, epididymal, and inguinal adipose tissue
  JOURNAL   Mol Cell Biochem 422 (1-2), 21-29 (2016)
   PUBMED   27590244
  REMARK    GeneRIF: upregulation of Pnpla2 expression and activation of ATGL
            (due to an increase in ABHD5 and decrease in G0S2 levels), as well
            as a coordinated interplay of these genes with Lipe in mesenteric
            WAT, contribute, at least in part, to an increase in the
            concentration of circulating NEFA in rats with reduced fat mass.
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Chamoun,Z., Vacca,F., Parton,R.G. and Gruenberg,J.
  TITLE     PNPLA3/adiponutrin functions in lipid droplet formation
  JOURNAL   Biol Cell 105 (5), 219-233 (2013)
   PUBMED   23398201
REFERENCE   4  (residues 1 to 351)
  AUTHORS   MacPherson,R.E., Ramos,S.V., Vandenboom,R., Roy,B.D. and
            Peters,S.J.
  TITLE     Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at
            rest and following stimulated contraction
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 304 (8), R644-R650 (2013)
   PUBMED   23408028
  REMARK    GeneRIF: in skeletal muscle, during contraction-induced muscle
            lipolysis, ATGL and CGI-58 strongly associate and that the PLIN
            proteins work together to regulate lipolysis
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Badin,P.M., Loubiere,C., Coonen,M., Louche,K., Tavernier,G.,
            Bourlier,V., Mairal,A., Rustan,A.C., Smith,S.R., Langin,D. and
            Moro,C.
  TITLE     Regulation of skeletal muscle lipolysis and oxidative metabolism by
            the co-lipase CGI-58
  JOURNAL   J Lipid Res 53 (5), 839-848 (2012)
   PUBMED   22383684
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Yamaguchi,T., Omatsu,N., Morimoto,E., Nakashima,H., Ueno,K.,
            Tanaka,T., Satouchi,K., Hirose,F. and Osumi,T.
  TITLE     CGI-58 facilitates lipolysis on lipid droplets but is not involved
            in the vesiculation of lipid droplets caused by hormonal
            stimulation
  JOURNAL   J Lipid Res 48 (5), 1078-1089 (2007)
   PUBMED   17308334
  REMARK    GeneRIF: CGI-58 facilitates lipolysis in cooperation with perilipin
            and other factors, including lipases
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Schweiger,M., Schreiber,R., Haemmerle,G., Lass,A., Fledelius,C.,
            Jacobsen,P., Tornqvist,H., Zechner,R. and Zimmermann,R.
  TITLE     Adipose triglyceride lipase and hormone-sensitive lipase are the
            major enzymes in adipose tissue triacylglycerol catabolism
  JOURNAL   J Biol Chem 281 (52), 40236-40241 (2006)
   PUBMED   17074755
REFERENCE   8  (residues 1 to 351)
  AUTHORS   Lass,A., Zimmermann,R., Haemmerle,G., Riederer,M., Schoiswohl,G.,
            Schweiger,M., Kienesberger,P., Strauss,J.G., Gorkiewicz,G. and
            Zechner,R.
  TITLE     Adipose triglyceride lipase-mediated lipolysis of cellular fat
            stores is activated by CGI-58 and defective in Chanarin-Dorfman
            Syndrome
  JOURNAL   Cell Metab 3 (5), 309-319 (2006)
   PUBMED   16679289
REFERENCE   9  (residues 1 to 351)
  AUTHORS   Yamaguchi,T., Omatsu,N., Matsushita,S. and Osumi,T.
  TITLE     CGI-58 interacts with perilipin and is localized to lipid droplets.
            Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman
            syndrome
  JOURNAL   J Biol Chem 279 (29), 30490-30497 (2004)
   PUBMED   15136565
  REMARK    GeneRIF: CGI-58 interacts with perilipin and is localized to lipid
            droplets
REFERENCE   10 (residues 1 to 351)
  AUTHORS   Lefevre,C., Jobard,F., Caux,F., Bouadjar,B., Karaduman,A.,
            Heilig,R., Lakhdar,H., Wollenberg,A., Verret,J.L., Weissenbach,J.,
            Ozguc,M., Lathrop,M., Prud'homme,J.F. and Fischer,J.
  TITLE     Mutations in CGI-58, the gene encoding a new protein of the
            esterase/lipase/thioesterase subfamily, in Chanarin-Dorfman
            syndrome
  JOURNAL   Am J Hum Genet 69 (5), 1002-1012 (2001)
   PUBMED   11590543
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY550934.1.
            
            On Aug 30, 2004 this sequence version replaced XP_236775.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY550934.1, BC127470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Rattus norvegicus"
                     /strain="ZDF"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..351
                     /product="1-acylglycerol-3-phosphate O-acyltransferase
                     ABHD5"
                     /EC_number="2.3.1.51"
                     /note="lipid droplet-binding protein CGI-58; abhydrolase
                     domain-containing protein 5"
                     /calculated_mol_wt=38973
     Region          3..347
                     /region_name="PLN02894"
                     /note="hydrolase, alpha/beta fold family protein"
                     /db_xref="CDD:215484"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6QA69.1)"
     Region          329..334
                     /region_name="HXXXXD motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QA69.1)"
     CDS             1..351
                     /gene="Abhd5"
                     /gene_synonym="CGI-58"
                     /coded_by="NM_212524.1:41..1096"
                     /db_xref="GeneID:316122"
                     /db_xref="RGD:1303237"
ORIGIN      
        1 mkamaaeeev dsadagggsg wltgwlptwc ptstshlkea eekmlkcvpc tykkepvris
       61 ngnsiwtlmf shnmssktpl vllhgfgggl glwalnfedl stdrpvyafd llgfgrssrp
      121 rfdsdaeeve nqfvesieew rcalrldkmi llghnlggfl aaayslkyps rvshlilvep
      181 wgfperpdla dqerpipvwi ralgaaltpf nplaglriag pfglslvqrl rpdfkrkyss
      241 mfeddtvtey iyhcnvqtps getafknmti pygwakrpml qrigglhpdi pvsvifgars
      301 cidgnsgtsi qslrpksyvk tiailgaghy vyadqpeefn qkvkeichtv d
//
LOCUS       NP_001103466              88 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein C-I precursor [Rattus norvegicus].
ACCESSION   NP_001103466
VERSION     NP_001103466.1
DBSOURCE    REFSEQ: accession NM_001109996.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Wang,X., Gong,Y., Deng,T., Zhang,L., Liao,X., Han,C., Yang,C.,
            Huang,J., Wang,Q., Song,X., Zhang,T., Yu,T., Zhu,G., Ye,X. and
            Peng,T.
  TITLE     Diagnostic and prognostic significance of mRNA expressions of
            apolipoprotein A and C family genes in hepatitis B virus-related
            hepatocellular carcinoma
  JOURNAL   J Cell Biochem 120 (10), 18246-18265 (2019)
   PUBMED   31211449
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Cohen,M., Yossef,R., Erez,T., Kugel,A., Welt,M., Karpasas,M.M.,
            Bones,J., Rudd,P.M., Taieb,J., Boissin,H., Harats,D., Noy,K.,
            Tekoah,Y., Lichtenstein,R.G., Rubin,E. and Porgador,A.
  TITLE     Serum apolipoproteins C-I and C-III are reduced in stomach cancer
            patients: results from MALDI-based peptidome and immuno-based
            clinical assays
  JOURNAL   PLoS One 6 (1), e14540 (2011)
   PUBMED   21267442
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Westerterp,M., Berbee,J.F., Delsing,D.J., Jong,M.C., Gijbels,M.J.,
            Dahlmans,V.E., Offerman,E.H., Romijn,J.A., Havekes,L.M. and
            Rensen,P.C.
  TITLE     Apolipoprotein C-I binds free fatty acids and reduces their
            intracellular esterification
  JOURNAL   J Lipid Res 48 (6), 1353-1361 (2007)
   PUBMED   17339654
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Masson,D., Pais de Barros,J.P., Zak,Z., Gautier,T., Le Guern,N.,
            Assem,M., Chisholm,J.W., Paterniti,J.R. Jr. and Lagrost,L.
  TITLE     Human apoA-I expression in CETP transgenic rats leads to lower
            levels of apoC-I in HDL and to magnification of CETP-mediated
            lipoprotein changes
  JOURNAL   J Lipid Res 47 (2), 356-365 (2006)
   PUBMED   16282639
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Ricci,F., Kern,S.E., Hruban,R.H. and Iacobuzio-Donahue,C.A.
  TITLE     Stromal responses to carcinomas of the pancreas: juxtatumoral gene
            expression conforms to the infiltrating pattern and not the
            biologic subtype
  JOURNAL   Cancer Biol Ther 4 (3), 302-307 (2005)
   PUBMED   15876873
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Shen,P. and Howlett,G.J.
  TITLE     Two coding regions closely linked to the rat apolipoprotein E gene:
            nucleotide sequences of rat apolipoprotein C-I and ECL cDNA
  JOURNAL   Arch Biochem Biophys 297 (2), 345-353 (1992)
   PUBMED   1379790
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Sehayek,E. and Eisenberg,S.
  TITLE     Mechanisms of inhibition by apolipoprotein C of apolipoprotein
            E-dependent cellular metabolism of human triglyceride-rich
            lipoproteins through the low density lipoprotein receptor pathway
  JOURNAL   J Biol Chem 266 (27), 18259-18267 (1991)
   PUBMED   1917954
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Poensgen,J.
  TITLE     Apolipoprotein C-1 inhibits the hydrolysis by phospholipase A2 of
            phospholipids in liposomes and cell membranes
  JOURNAL   Biochim Biophys Acta 1042 (2), 188-192 (1990)
   PUBMED   2302419
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Shen,P.Y. and Howlett,G.J.
  TITLE     Nucleotide sequence of cDNA for rat apolipoprotein C-I
  JOURNAL   Nucleic Acids Res 17 (15), 6405 (1989)
   PUBMED   2771655
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Kinnunen,P.K. and Ehnolm,C.
  TITLE     Effect of serum and C-apoproteins from very low density
            lipoproteins on human postheparin plasma hepatic lipase
  JOURNAL   FEBS Lett 65 (3), 354-357 (1976)
   PUBMED   182536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY327505.1 and BC098670.1.
            
            Transcript Variant: This variant (2) contains an additional 5'
            non-coding exon, therefore, has a different 5' UTR compared to
            transcript variant 1. Transcript variants 1 and 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212377.1, FQ210440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..88
                     /product="apolipoprotein C-I precursor"
                     /note="apo-CI; apoC-I; liver regeneration-related protein
                     LRRG04; apolipoprotein C-I"
                     /calculated_mol_wt=7187
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2691
     mat_peptide     27..88
                     /product="apolipoprotein C-I"
                     /calculated_mol_wt=7187
     Region          27..87
                     /region_name="ApoC-I"
                     /note="Apolipoprotein C-I (ApoC-1); pfam04691"
                     /db_xref="CDD:428068"
     CDS             1..88
                     /gene="Apoc1"
                     /gene_synonym="ALPCI; Apo-CIB; ApoC-IB; LRRG04"
                     /coded_by="NM_001109996.1:49..315"
                     /db_xref="GeneID:25292"
                     /db_xref="RGD:2134"
ORIGIN      
        1 mrlfialpvl ivvvamaleg papaqaapdf ssameslpdk lkefgntled karaaiehik
       61 qkeimiktrn wfsetlnkmk eklkttfa
//
LOCUS       NP_446426                217 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 4E [Rattus norvegicus].
ACCESSION   NP_446426
VERSION     NP_446426.1
DBSOURCE    REFSEQ: accession NM_053974.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dong,R., Li,X., Flores,A.D. and Lai,K.O.
  TITLE     The translation initiating factor eIF4E and arginine methylation
            underlie G3BP1 function in dendritic spine development of neurons
  JOURNAL   J Biol Chem 299 (8), 105029 (2023)
   PUBMED   37442236
  REMARK    GeneRIF: The translation initiating factor eIF4E and arginine
            methylation underlie G3BP1 function in dendritic spine development
            of neurons.
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Martinez-Alonso,E., Escobar-Peso,A., Guerra-Perez,N., Roca,M.,
            Masjuan,J. and Alcazar,A.
  TITLE     Dihydropyrimidinase-Related Protein 2 Is a New Partner in the
            Binding between 4E-BP2 and eIF4E Related to Neuronal Death after
            Cerebral Ischemia
  JOURNAL   Int J Mol Sci 24 (9), 8246 (2023)
   PUBMED   37175950
  REMARK    GeneRIF: Dihydropyrimidinase-Related Protein 2 Is a New Partner in
            the Binding between 4E-BP2 and eIF4E Related to Neuronal Death
            after Cerebral Ischemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Martinez-Alonso,E., Guerra-Perez,N., Escobar-Peso,A., Regidor,I.,
            Masjuan,J. and Alcazar,A.
  TITLE     Differential Association of 4E-BP2-Interacting Proteins Is Related
            to Selective Delayed Neuronal Death after Ischemia
  JOURNAL   Int J Mol Sci 22 (19), 10327 (2021)
   PUBMED   34638676
  REMARK    GeneRIF: Differential Association of 4E-BP2-Interacting Proteins Is
            Related to Selective Delayed Neuronal Death after Ischemia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Gindina,S., Botsford,B., Cowansage,K., LeDoux,J., Klann,E.,
            Hoeffer,C. and Ostroff,L.
  TITLE     Upregulation of eIF4E, but not other translation initiation
            factors, in dendritic spines during memory formation
  JOURNAL   J Comp Neurol 529 (11), 3112-3126 (2021)
   PUBMED   33864263
  REMARK    GeneRIF: Upregulation of eIF4E, but not other translation
            initiation factors, in dendritic spines during memory formation.
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Li,B., Huang,Z., Meng,J., Yu,W. and Yang,H.
  TITLE     MiR-202-5p attenuates neurological deficits and neuronal injury in
            MCAO model rats and OGD-induced injury in Neuro-2a cells by
            targeting eIF4E-mediated induction of autophagy and inhibition of
            Akt/GSK-3beta pathway
  JOURNAL   Mol Cell Probes 51, 101497 (2020)
   PUBMED   31877332
  REMARK    GeneRIF: MiR-202-5p attenuates neurological deficits and neuronal
            injury in MCAO model rats and OGD-induced injury in Neuro-2a cells
            by targeting eIF4E-mediated induction of autophagy and inhibition
            of Akt/GSK-3beta pathway.
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Potter,M.W., Shah,S.A., Elbirt,K.K. and Callery,M.P.
  TITLE     Endotoxin (LPS) stimulates 4E-BP1/PHAS-I phosphorylation in
            macrophages
  JOURNAL   J Surg Res 97 (1), 54-59 (2001)
   PUBMED   11319880
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Makhlouf,A.A., Namboodiri,A.M. and McDermott,P.J.
  TITLE     Transcriptional regulation of the rat eIF4E gene in cardiac muscle
            cells: the role of specific elements in the promoter region
  JOURNAL   Gene 267 (1), 1-12 (2001)
   PUBMED   11311550
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Tinton,S.A. and Buc-Calderon,P.M.
  TITLE     Hypoxia increases the association of 4E-binding protein 1 with the
            initiation factor 4E in isolated rat hepatocytes
  JOURNAL   FEBS Lett 446 (1), 55-59 (1999)
   PUBMED   10100614
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Miyagi,Y., Kerr,S., Sugiyama,A., Asai,A., Shibuya,M., Fujimoto,H.
            and Kuchino,Y.
  TITLE     Abundant expression of translation initiation factor EIF-4E in
            post-meiotic germ cells of the rat testis
  JOURNAL   Lab Invest 73 (6), 890-898 (1995)
   PUBMED   8558852
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Lin,T.A., Kong,X., Haystead,T.A., Pause,A., Belsham,G.,
            Sonenberg,N. and Lawrence,J.C. Jr.
  TITLE     PHAS-I as a link between mitogen-activated protein kinase and
            translation initiation
  JOURNAL   Science 266 (5185), 653-656 (1994)
   PUBMED   7939721
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087001.1, X83399.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..217
                     /product="eukaryotic translation initiation factor 4E"
                     /note="eIF-4E; eIF-4F 25 kDa subunit; mRNA cap-binding
                     protein; eukaryotic initiation factor 4E"
                     /calculated_mol_wt=24922
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63074.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P06730; propagated from
                     UniProtKB/Swiss-Prot (P63074.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P06730; propagated from
                     UniProtKB/Swiss-Prot (P63074.1)"
     Region          37..40
                     /region_name="EIF4EBP1/2/3 binding.
                     /evidence=ECO:0000250|UniProtKB:P06730"
                     /note="propagated from UniProtKB/Swiss-Prot (P63074.1)"
     Region          38..197
                     /region_name="IF4E"
                     /note="Eukaryotic initiation factor 4E; pfam01652"
                     /db_xref="CDD:460281"
     Region          73..77
                     /region_name="EIF4EBP1/2/3 binding.
                     /evidence=ECO:0000250|UniProtKB:P06730"
                     /note="propagated from UniProtKB/Swiss-Prot (P63074.1)"
     Region          132..139
                     /region_name="EIF4EBP1/2/3 binding.
                     /evidence=ECO:0000250|UniProtKB:P06730"
                     /note="propagated from UniProtKB/Swiss-Prot (P63074.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC and MKNK2.
                     /evidence=ECO:0000250|UniProtKB:P06730; propagated from
                     UniProtKB/Swiss-Prot (P63074.1)"
     CDS             1..217
                     /gene="Eif4e"
                     /coded_by="NM_053974.2:14..667"
                     /db_xref="GeneID:117045"
                     /db_xref="RGD:69647"
ORIGIN      
        1 matvepettp ttnpppaeee ktesnqevan pehyikhplq nrwalwffkn dksktwqanl
       61 rliskfdtve dfwalynhiq lssnlmpgcd yslfkdgiep mwedeknkrg grwlitlnkq
      121 qrrsdldrfw letllclige sfddysddvc gavvnvrakg dkiaiwttec enrdavthig
      181 rvykerlglp pkivigyqsh adtatksgst tknrfvv
//
LOCUS       NP_998727                488 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM39 [Rattus norvegicus].
ACCESSION   NP_998727 XP_227954
VERSION     NP_998727.1
DBSOURCE    REFSEQ: accession NM_213562.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Suzuki,M., Watanabe,M., Nakamaru,Y., Takagi,D., Takahashi,H.,
            Fukuda,S. and Hatakeyama,S.
  TITLE     TRIM39 negatively regulates the NFkappaB-mediated signaling pathway
            through stabilization of Cactin
  JOURNAL   Cell Mol Life Sci 73 (5), 1085-1101 (2016)
   PUBMED   26363554
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhang,L., Mei,Y., Fu,N.Y., Guan,L., Xie,W., Liu,H.H., Yu,C.D.,
            Yin,Z., Yu,V.C. and You,H.
  TITLE     TRIM39 regulates cell cycle progression and DNA damage responses
            via stabilizing p21
  JOURNAL   Proc Natl Acad Sci U S A 109 (51), 20937-20942 (2012)
   PUBMED   23213251
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):4148]
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Lee,S.S., Fu,N.Y., Sukumaran,S.K., Wan,K.F., Wan,Q. and Yu,V.C.
  TITLE     TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through
            inhibition of its poly-ubiquitination process
  JOURNAL   Exp Cell Res 315 (7), 1313-1325 (2009)
   PUBMED   19100260
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883050.1.
            
            On Aug 30, 2004 this sequence version replaced XP_227954.2.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..488
                     /product="E3 ubiquitin-protein ligase TRIM39"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 39; tripartite
                     motif-containing protein 39; RING finger protein 23;
                     RING-type E3 ubiquitin transferase TRIM39"
                     /calculated_mol_wt=56264
     Region          22..82
                     /region_name="RING-HC_TRIM7-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins, TRIM7, TRIM11 and TRIM27, and
                     similar proteins; cd16594"
                     /db_xref="CDD:438256"
     Region          103..146
                     /region_name="Bbox2_TRIM39-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM39, TRIM58 and similar
                     proteins; cd19780"
                     /db_xref="CDD:380838"
     Region          <144..>271
                     /region_name="PRK02224"
                     /note="DNA double-strand break repair Rad50 ATPase"
                     /db_xref="CDD:179385"
     Region          268..307
                     /region_name="Interaction with CDKN1A.
                     /evidence=ECO:0000250|UniProtKB:Q9HCM9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFZ5.1)"
     Region          305..483
                     /region_name="SPRY_PRY_TRIM39"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     39 (TRIM39) and TRIM39-like; cd13745"
                     /db_xref="CDD:293979"
     Region          359..488
                     /region_name="Interaction with CDKN1A.
                     /evidence=ECO:0000250|UniProtKB:Q9HCM9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFZ5.1)"
     CDS             1..488
                     /gene="Trim39"
                     /gene_synonym="Rnf23"
                     /coded_by="NM_213562.1:118..1584"
                     /db_xref="GeneID:309591"
                     /db_xref="RGD:1303115"
ORIGIN      
        1 maetslleag asaastaaal enlqveascs vcleylkepv iiecghnfck acitrwwedl
       61 erdfpcpvcr ktsryrslrp nrqlgsmvei akqlqtvkrk irdeslcsqh heplslfcye
      121 dqeavclica ishthrahtv vpmddatqey keklqkclep leqklqeitc ckaseerkpg
      181 elkrlvesrr qqilkefeel hrrldeeqqt llsrleeeeq dilqrlrena ahlgdrrrdl
      241 ahlaaevegk clqsgfemlk dvkstlekce kvktmevtsv sieleknfsh fprqyfalrk
      301 ilkqliadvt ldpetahpnl vlsedrksvk fvetrlrdlp dtpqrftfyp cvlategfts
      361 grhywevevg dkthwavgvc rdsvsrkgel tplpetgywr vrlwngdkya atttpftplh
      421 ikvkpkrvgi fldyeagtls fynvtdrshi ytftdtftek lwplfypgir agrknaaplt
      481 irpptdwe
//
LOCUS       NP_695215                333 aa            linear   ROD 27-APR-2025
DEFINITION  torsin-1A precursor [Rattus norvegicus].
ACCESSION   NP_695215
VERSION     NP_695215.2
DBSOURCE    REFSEQ: accession NM_153303.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Beauvais,G., Rodriguez-Losada,N., Ying,L., Zakirova,Z.,
            Watson,J.L., Readhead,B., Gadue,P., French,D.L., Ehrlich,M.E. and
            Gonzalez-Alegre,P.
  TITLE     Exploring the Interaction Between eIF2alpha Dysregulation, Acute
            Endoplasmic Reticulum Stress and DYT1 Dystonia in the Mammalian
            Brain
  JOURNAL   Neuroscience 371, 455-468 (2018)
   PUBMED   29289717
  REMARK    GeneRIF: TorsinA was post-transcriptionally upregulated upon acute
            ER stress, suggesting a role in this response. Increased basal
            phosphorylation of eIF2alpha in DYT1 transgenic rats was associated
            with abnormal response to acute ER stress. Unbiased RNA-Seq-based
            transcriptomic analysis of embryonic brain tissue in heterozygous
            and homozygous DYT1 knockin mice confirmed presence of eIF2alpha
            dysregulation in the DYT1 brain.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Zhao,C., Brown,R.S., Chase,A.R., Eisele,M.R. and Schlieker,C.
  TITLE     Regulation of Torsin ATPases by LAP1 and LULL1
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), E1545-E1554 (2013)
   PUBMED   23569223
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Grundmann,K., Glockle,N., Martella,G., Sciamanna,G., Hauser,T.K.,
            Yu,L., Castaneda,S., Pichler,B., Fehrenbacher,B., Schaller,M.,
            Nuscher,B., Haass,C., Hettich,J., Yue,Z., Nguyen,H.P., Pisani,A.,
            Riess,O. and Ott,T.
  TITLE     Generation of a novel rodent model for DYT1 dystonia
  JOURNAL   Neurobiol Dis 47 (1), 61-74 (2012)
   PUBMED   22472189
  REMARK    GeneRIF: developed transgenic rat models for DYT1 dystonia
            harboring the full length human mutant and wildtype Tor1A gene.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Granata,A., Koo,S.J., Haucke,V., Schiavo,G. and Warner,T.T.
  TITLE     CSN complex controls the stability of selected synaptic proteins
            via a torsinA-dependent process
  JOURNAL   EMBO J 30 (1), 181-193 (2011)
   PUBMED   21102408
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Kim,C.E., Perez,A., Perkins,G., Ellisman,M.H. and Dauer,W.T.
  TITLE     A molecular mechanism underlying the neural-specific defect in
            torsinA mutant mice
  JOURNAL   Proc Natl Acad Sci U S A 107 (21), 9861-9866 (2010)
   PUBMED   20457914
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Goodchild,R.E. and Dauer,W.T.
  TITLE     The AAA+ protein torsinA interacts with a conserved domain present
            in LAP1 and a novel ER protein
  JOURNAL   J Cell Biol 168 (6), 855-862 (2005)
   PUBMED   15767459
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Torres,G.E., Sweeney,A.L., Beaulieu,J.M., Shashidharan,P. and
            Caron,M.G.
  TITLE     Effect of torsinA on membrane proteins reveals a loss of function
            and a dominant-negative phenotype of the dystonia-associated
            DeltaE-torsinA mutant
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15650-15655 (2004)
   PUBMED   15505207
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Kamm,C., Boston,H., Hewett,J., Wilbur,J., Corey,D.P., Hanson,P.I.,
            Ramesh,V. and Breakefield,X.O.
  TITLE     The early onset dystonia protein torsinA interacts with kinesin
            light chain 1
  JOURNAL   J Biol Chem 279 (19), 19882-19892 (2004)
   PUBMED   14970196
  REMARK    GeneRIF: wild-type torsinA undergoes anterograde transport along
            microtubules mediated by kinesin and may act as a molecular
            chaperone regulating kinesin activity and/or cargo binding
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Hewett,J., Ziefer,P., Bergeron,D., Naismith,T., Boston,H.,
            Slater,D., Wilbur,J., Schuback,D., Kamm,C., Smith,N., Camp,S.,
            Ozelius,L.J., Ramesh,V., Hanson,P.I. and Breakefield,X.O.
  TITLE     TorsinA in PC12 cells: localization in the endoplasmic reticulum
            and response to stress
  JOURNAL   J Neurosci Res 72 (2), 158-168 (2003)
   PUBMED   12671990
  REMARK    GeneRIF: Mutant torsinA may interfere with and/or compromise ER
            functions, especially in dopaminergic neurons, which have high
            levels of torsinA and are intrinsically vulnerable to oxidative
            stress.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Konakova,M. and Pulst,S.M.
  TITLE     Immunocytochemical characterization of torsin proteins in mouse
            brain
  JOURNAL   Brain Res 922 (1), 1-8 (2001)
   PUBMED   11730696
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078714.1.
            
            On Aug 23, 2004 this sequence version replaced NP_695215.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078714.1, AY054303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMN16676787
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..333
                     /product="torsin-1A precursor"
                     /note="torsin A; dystonia 1, torsion (autosomal dominant;
                     torsin A); torsin-1A; torsin ATPase 1; dystonia 1 protein"
                     /calculated_mol_wt=35829
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2138
     mat_peptide     21..333
                     /product="Torsin-1A. /id=PRO_0000429276"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68G38.1)"
                     /calculated_mol_wt=35829
     Region          56..170
                     /region_name="Torsin"
                     /note="pfam06309"
                     /db_xref="CDD:399367"
     Region          92..252
                     /region_name="Interaction with SNAPIN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68G38.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (Q68G38.1)"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (Q68G38.1)"
     Region          252..333
                     /region_name="Interaction with KLC1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68G38.1)"
     Region          313..333
                     /region_name="Interaction with SYNE3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68G38.1)"
     CDS             1..333
                     /gene="Tor1a"
                     /gene_synonym="Dyt1"
                     /coded_by="NM_153303.2:39..1040"
                     /db_xref="GeneID:266606"
                     /db_xref="RGD:628863"
ORIGIN      
        1 mklgratlal lllvpcvvra vepislglal agvltgyisy prlyclfaec cgqkrslsre
       61 alqkdldnkl fgqhlakrvi lnavsgflsn pkpkkpltls lhgwtgtgkn faskiiaeni
      121 yegglnsdyv hlfvatlhfp hasnitlykd qlqmwirgnv sacarsifif demdkmhagl
      181 idaikpfldy ydvvdevsyq kaififlsna gaeritdval dfwrsgkqre eiklrdmeha
      241 lavsvfnnkn sgfwhsslid rnlidyfvpf lpleykhlkm cirvemqsrg yeedediink
      301 vaeemtffpk eekvfsdkgc ktvftkldyy ldd
//
LOCUS       NP_058799                773 aa            linear   ROD 27-APR-2025
DEFINITION  elongin-A [Rattus norvegicus].
ACCESSION   NP_058799
VERSION     NP_058799.2
DBSOURCE    REFSEQ: accession NM_017103.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Weems,J.C., Slaughter,B.D., Unruh,J.R., Boeing,S., Hall,S.M.,
            McLaird,M.B., Yasukawa,T., Aso,T., Svejstrup,J.Q., Conaway,J.W. and
            Conaway,R.C.
  TITLE     Cockayne syndrome B protein regulates recruitment of the Elongin A
            ubiquitin ligase to sites of DNA damage
  JOURNAL   J Biol Chem 292 (16), 6431-6437 (2017)
   PUBMED   28292928
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Kawauchi,J., Inoue,M., Fukuda,M., Uchida,Y., Yasukawa,T.,
            Conaway,R.C., Conaway,J.W., Aso,T. and Kitajima,S.
  TITLE     Transcriptional properties of mammalian elongin A and its role in
            stress response
  JOURNAL   J Biol Chem 288 (34), 24302-24315 (2013)
   PUBMED   23828199
  REMARK    GeneRIF: Elongin A transcription elongation activity, but not its
            ubiquitination activity, is most important for its function in
            induction of transcription of ATF3 and p21.
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Kamura,T., Burian,D., Yan,Q., Schmidt,S.L., Lane,W.S., Querido,E.,
            Branton,P.E., Shilatifard,A., Conaway,R.C. and Conaway,J.W.
  TITLE     Muf1, a novel Elongin BC-interacting leucine-rich repeat protein
            that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin
            ligase
  JOURNAL   J Biol Chem 276 (32), 29748-29753 (2001)
   PUBMED   11384984
REFERENCE   5  (residues 1 to 773)
  AUTHORS   Aso,T., Haque,D., Barstead,R.J., Conaway,R.C. and Conaway,J.W.
  TITLE     The inducible elongin A elongation activation domain: structure,
            function and interaction with the elongin BC complex
  JOURNAL   EMBO J 15 (20), 5557-5566 (1996)
   PUBMED   8896449
REFERENCE   6  (residues 1 to 773)
  AUTHORS   Aso,T., Lane,W.S., Conaway,J.W. and Conaway,R.C.
  TITLE     Elongin (SIII): a multisubunit regulator of elongation by RNA
            polymerase II
  JOURNAL   Science 269 (5229), 1439-1443 (1995)
   PUBMED   7660129
REFERENCE   7  (residues 1 to 773)
  AUTHORS   Bradsher,J.N., Jackson,K.W., Conaway,R.C. and Conaway,J.W.
  TITLE     RNA polymerase II transcription factor SIII. I. Identification,
            purification, and properties
  JOURNAL   J Biol Chem 268 (34), 25587-25593 (1993)
   PUBMED   8244996
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081815.1.
            
            On Jun 10, 2007 this sequence version replaced NP_058799.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081815.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..773
                     /product="elongin-A"
                     /note="transcription elongation factor B polypeptide 3;
                     SIII p110; elongin 110 kDa subunit; RNA polymerase II
                     transcription factor SIII subunit A; RNA polymerase II
                     transcription factor SIII subunit A1; transcription
                     elongation factor B subunit 3; transcription elongation
                     factor B (SIII), polypeptide 3; RNA polymerase II
                     transcription factor elongin subunit A (110 kDa)"
                     /calculated_mol_wt=87101
     Region          <37..76
                     /region_name="TFIIS_I"
                     /note="N-terminal domain (domain I) of transcription
                     elongation factor S-II (TFIIS); similar to a domain found
                     in elongin A and CRSP70; likely to be involved in
                     transcription; domain I from TFIIS interacts with RNA
                     polymerase II holoenzyme; cd00183"
                     /db_xref="CDD:238107"
     Region          79..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63187.1)"
     Region          162..>399
                     /region_name="PTZ00112"
                     /note="origin recognition complex 1 protein; Provisional"
                     /db_xref="CDD:240274"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CB77; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14241; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14241; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Site            430
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CB77; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14241; propagated from
                     UniProtKB/Swiss-Prot (Q63187.1)"
     Region          521..680
                     /region_name="Activation domain.
                     /evidence=ECO:0000269|PubMed:8896449"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63187.1)"
     Region          549..558
                     /region_name="BC-box.
                     /evidence=ECO:0000269|PubMed:8896449"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63187.1)"
     Region          565..663
                     /region_name="Elongin_A"
                     /note="RNA polymerase II transcription factor SIII
                     (Elongin) subunit A; pfam06881"
                     /db_xref="CDD:462026"
     Region          671..747
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63187.1)"
     CDS             1..773
                     /gene="Eloa"
                     /gene_synonym="El; Tceb3"
                     /coded_by="NM_017103.2:67..2388"
                     /db_xref="GeneID:25562"
                     /db_xref="RGD:3827"
ORIGIN      
        1 maaesalqvv eklqarlaan pdpkkllkyl kklsvlpitv dilvetgvgk tvnsfrkheq
       61 vgnfardlva qwkklvpver nneaedqdfe ksnsrkrprd vpqqeeeaeg nyqeswqasg
      121 sqpyspehrq kkhrklpele rphkvahghe rrderkrchk vsppyssdpe ssdyghvqsp
      181 ppssphqmyt dlsrspemdq epivshpkpg kvhsntfqdr lgvshlgehq gkgavsqnkp
      241 hksshkekrp vdargdekss vmgrekshka sskeesrrll sedsakeklp ssvvkkekdr
      301 egnslkkkls paldvasdnh fkkpkhkdse kiksdknkqs vdsvdsgrgt gdplprakdk
      361 vpnnlkaqeg kvrtnsdrks pgslpkveem dmddefeqpt msfesylsyd qprkkkkkvv
      421 ktsgtalgek glkkkdskst sknlnsaqkl pkvnenksdk lqpagaeptr prkvptdvlp
      481 alpdiplpai qtnyrplpsl elissfqpkr kafsspqeee eagftgrrmn skmqvysgsk
      541 caylpkmmtl hqqcirvlkn nidsifevgg vpysvlepvl erctpdqlyr ieecnhvlie
      601 etdqlwkvhc hrdfkeerpe eyeswremyl rlqdareqrl rlltnnirsa hankpkgrqa
      661 kmafvnsvak pprdvrrrqe kfgtggaavp ekvrikpapy ttgsshvpas nssssfhssp
      721 eelayegpst ssahlapvas ssvsydprkp avkkiapmma ktikafknrf srr
//
LOCUS       NP_073180                210 aa            linear   ROD 27-APR-2025
DEFINITION  synaptosomal-associated protein 23 isoform 1 [Rattus norvegicus].
ACCESSION   NP_073180
VERSION     NP_073180.1
DBSOURCE    REFSEQ: accession NM_022689.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Dolai,S., Takahashi,T., Qin,T., Liang,T., Xie,L., Kang,F.,
            Miao,Y.F., Xie,H., Kang,Y., Manuel,J., Winter,E., Roche,P.A.,
            Cattral,M.S. and Gaisano,H.Y.
  TITLE     Pancreas-specific SNAP23 depletion prevents pancreatitis by
            attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes
  JOURNAL   Autophagy 17 (10), 3068-3081 (2021)
   PUBMED   33213278
  REMARK    GeneRIF: Pancreas-specific SNAP23 depletion prevents pancreatitis
            by attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes.
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Serrano-Lopez,E.M., Lopez-Martinez,D., Gomez-Fernandez,J.C.,
            Egea-Jimenez,A.L. and Corbalan-Garcia,S.
  TITLE     PKCepsilon controls the fusion of secretory vesicles in mast cells
            in a phosphatidic acid-dependent mode
  JOURNAL   Int J Biol Macromol 185, 377-389 (2021)
   PUBMED   34147527
  REMARK    GeneRIF: PKCepsilon controls the fusion of secretory vesicles in
            mast cells in a phosphatidic acid-dependent mode.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Naskar,P., Naqvi,N. and Puri,N.
  TITLE     Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23
            leads to massive inhibition in exocytosis from mast cells
  JOURNAL   J Biosci 43 (1), 127-138 (2018)
   PUBMED   29485121
  REMARK    GeneRIF: Blocking dephosphorylation at serine 120 residue in
            SNAP-23 leads to massive inhibition in exocytosis from mast cells.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Weber,P., Batoulis,H., Rink,K.M., Dahlhoff,S., Pinkwart,K.,
            Sollner,T.H. and Lang,T.
  TITLE     Electrostatic anchoring precedes stable membrane attachment of
            SNAP25/SNAP23 to the plasma membrane
  JOURNAL   Elife 6, e19394 (2017)
   PUBMED   28240595
  REMARK    GeneRIF: Electrostatic anchoring precedes stable membrane
            attachment of SNAP25 and SNAP23 to the plasma membrane.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Rao,S.K., Huynh,C., Proux-Gillardeaux,V., Galli,T. and Andrews,N.W.
  TITLE     Identification of SNAREs involved in synaptotagmin VII-regulated
            lysosomal exocytosis
  JOURNAL   J Biol Chem 279 (19), 20471-20479 (2004)
   PUBMED   14993220
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Abonyo,B.O., Gou,D., Wang,P., Narasaraju,T., Wang,Z. and Liu,L.
  TITLE     Syntaxin 2 and SNAP-23 are required for regulated surfactant
            secretion
  JOURNAL   Biochemistry 43 (12), 3499-3506 (2004)
   PUBMED   15035620
  REMARK    GeneRIF: SNAP-23 is expressed in alveolar type II cells of the
            lung; evidence supports its functional role in exocytosis of lung
            surfactant by alveolar type II cells.
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Banerjee,A., Li,G., Alexander,E.A. and Schwartz,J.H.
  TITLE     Role of SNAP-23 in trafficking of H+-ATPase in cultured inner
            medullary collecting duct cells
  JOURNAL   Am J Physiol Cell Physiol 280 (4), C775-C781 (2001)
   PUBMED   11245593
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Okamoto,M., Schoch,S. and Sudhof,T.C.
  TITLE     EHSH1/intersectin, a protein that contains EH and SH3 domains and
            binds to dynamin and SNAP-25. A protein connection between
            exocytosis and endocytosis?
  JOURNAL   J Biol Chem 274 (26), 18446-18454 (1999)
   PUBMED   10373452
REFERENCE   10 (residues 1 to 210)
  AUTHORS   St-Denis,J.F., Cabaniols,J.P., Cushman,S.W. and Roche,P.A.
  TITLE     SNAP-23 participates in SNARE complex assembly in rat adipose cells
  JOURNAL   Biochem J 338 (Pt 3) (Pt 3), 709-715 (1999)
   PUBMED   10051443
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127494.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127494.1, DY319893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..210
                     /product="synaptosomal-associated protein 23 isoform 1"
                     /note="SNAP-23; vesicle-membrane fusion protein SNAP-23;
                     synaptosomal-associated protein, 23 kD;
                     synaptosomal-associated protein 23"
                     /calculated_mol_wt=23104
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09044; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          86..147
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          104..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70377.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          148..206
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(148,150..151,154..159,161..162,165..166,168..170,
                     172..173,176..177,179..180,182..187,189..190,193,196,200,
                     203,206)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            179
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..210
                     /gene="Snap23"
                     /coded_by="NM_022689.2:149..781"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64630"
                     /db_xref="RGD:620221"
ORIGIN      
        1 mddlspeeiq lrahqvtdes lestrrilgl aiesqdagik titmldeqge qlnrieegmd
       61 qinkdmreae ktltelnkcc glcvcpcnrt knfesgknyk atwgdggdss psnvvskqps
      121 ritngqpqqt tgaasggyik ritndarede meenltqvgs ilgnlknmal dmgneidaqn
      181 qqiqkiteka dtnknridia ntrakklids
//
LOCUS       NP_542421               1430 aa            linear   ROD 27-APR-2025
DEFINITION  caskin-1 [Rattus norvegicus].
ACCESSION   NP_542421
VERSION     NP_542421.2
DBSOURCE    REFSEQ: accession NM_080690.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1430)
  AUTHORS   Stafford,R.L., Hinde,E., Knight,M.J., Pennella,M.A., Ear,J.,
            Digman,M.A., Gratton,E. and Bowie,J.U.
  TITLE     Tandem SAM domain structure of human Caskin1: a presynaptic,
            self-assembling scaffold for CASK
  JOURNAL   Structure 19 (12), 1826-1836 (2011)
   PUBMED   22153505
REFERENCE   2  (residues 1 to 1430)
  AUTHORS   Stafford,R.L., Ear,J., Knight,M.J. and Bowie,J.U.
  TITLE     The molecular basis of the Caskin1 and Mint1 interaction with CASK
  JOURNAL   J Mol Biol 412 (1), 3-13 (2011)
   PUBMED   21763699
REFERENCE   3  (residues 1 to 1430)
  AUTHORS   Balazs,A., Csizmok,V., Buday,L., Rakacs,M., Kiss,R., Bokor,M.,
            Udupa,R., Tompa,K. and Tompa,P.
  TITLE     High levels of structural disorder in scaffold proteins as
            exemplified by a novel neuronal protein, CASK-interactive protein1
  JOURNAL   FEBS J 276 (14), 3744-3756 (2009)
   PUBMED   19523119
  REMARK    GeneRIF: proline-rich region of Caskin1 is biochemically
            functional, as it interacts with the adaptor protein
            Abl-interactor-2.
REFERENCE   4  (residues 1 to 1430)
  AUTHORS   Tabuchi,K., Biederer,T., Butz,S. and Sudhof,T.C.
  TITLE     CASK participates in alternative tripartite complexes in which Mint
            1 competes for binding with caskin 1, a novel CASK-binding protein
  JOURNAL   J Neurosci 22 (11), 4264-4273 (2002)
   PUBMED   12040031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF451975.1, AA819372.1, CB800449.1, CB738051.1, CB733612.1 and
            JAXUCZ010000010.1.
            
            On Oct 11, 2007 this sequence version replaced NP_542421.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.59203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1430
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..1430
                     /product="caskin-1"
                     /note="cask-interacting protein 1"
                     /calculated_mol_wt=150136
     Region          7..46
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          30..291
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          48..79
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          48..77
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          81..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          81..110
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            order(114,116,120..121,124..126,128..129,133,136,145,147,
                     149,153..154,157..159,161..162,166,169,186,188,190,
                     194..195,198..200,202..203,207,210)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          114..145
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          114..143
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          147..186
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          147..176
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          188..218
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          188..217
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          220..249
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          221..251
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          253..287
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          284..345
                     /region_name="SH3_Caskin1"
                     /note="Src Homology 3 domain of CASK interacting protein
                     1; cd12062"
                     /db_xref="CDD:212995"
     Site            order(290,292,295,300,318..319,338,340..341)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212995"
     Region          348..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          373..421
                     /region_name="Caskin1-CID"
                     /note="Caskin1 CASK-interaction domain; pfam16600"
                     /db_xref="CDD:465190"
     Region          375..471
                     /region_name="CASK-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            398
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8WXD9; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          421..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          473..538
                     /region_name="SAM_caskin1,2_repeat1"
                     /note="SAM domain of caskin protein repeat 1; cd09497"
                     /db_xref="CDD:188896"
     Region          540..609
                     /region_name="SAM_caskin1,2_repeat2"
                     /note="SAM domain of caskin protein repeat 2; cd09498"
                     /db_xref="CDD:188897"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          667..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          <700..>828
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          877..948
                     /region_name="Caskin-Pro-rich"
                     /note="Proline rich region of Caskin proteins; pfam16907"
                     /db_xref="CDD:465308"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          1015..1040
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          1055..1371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            1066
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          <1217..>1406
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Site            1362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P9K8; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK2.1)"
     Region          1368..1430
                     /region_name="Caskin-tail"
                     /note="C-terminal region of Caskin; pfam16632"
                     /db_xref="CDD:465209"
     Region          1388..1407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK2.1)"
     CDS             1..1430
                     /gene="Caskin1"
                     /coded_by="NM_080690.2:171..4463"
                     /db_xref="GeneID:140722"
                     /db_xref="RGD:620191"
ORIGIN      
        1 mgkeqelvqa vkaedvgtaq rllqrprpgk akllgstkki nvnfqdpdgf salhhaalng
       61 ntelisllle aqaavdikdn kgmrplhyaa wqgrkepmkl vlkagsavnv psdeghiplh
      121 laaqhghydv semllqhqsn pcmvdnsgkt pldlacefgr vgvvqlllss nmcaallepr
      181 pgdttdpngt splhlaakng hidiirlllq agidinrqtk sgtalheaal cgktevvrll
      241 ldsginaqvr ntysqtaldi vhqfttsqas keikqllrea saalqvratk dycnnydlts
      301 lnvkagdiit vleqhpdgrw kgcihdnrtg ndrvgyfpss lgeaivkrag srtgsepspp
      361 qgggslgpsa ppeeiwvlrk pfaggdrsgs lsnvaggrst gghalhagae gvkllatvls
      421 qksvsesspg dspvkppegs sgaarsqppa ahagqvygeq ppkklesssa segksaeavs
      481 qwlatfqlql yapnftsagy dlptisrmtp edltaigvtk pghrkkitae isglnipdcl
      541 pehkpanlav wlsmiglaqy ykvlvdngye nidfitditw edlqeigitk lghqkklmla
      601 vrklaelqka eyskyeggpl rrkapqslem maiespppse paaaecqspk mttfqdsels
      661 gelqaalsgp aeagaaaaek ssnhlpatpr ttsrqessls grarhmsssq ellgdgpqgp
      721 gspmsrsqey lldegpapgt ppkevrssrh ghsvkrasvp pvpgkprqvl psgvshftpp
      781 qtptkaqpgs pqalggphgp atakvkptpq llpptdrpms prslpqspth rgfayvlpqp
      841 vegeagppap gpvpppvpaa vptlclppea dvepgrpkkr ahslnryaas dseperdell
      901 vpaaagpyat vqrrvgrshs vrapagtdkn vnrsqsfavr prkkgppppp pkrsssamas
      961 anladepspd vetedgrlgv raqrrrasdl agsvdtgsag svksiaamle lssiggggra
     1021 irrppeghpt prpaspdpgr vatvlasvkh keaigpdgev vnrrrtlsgp vtgllatarr
     1081 gpgepaeqsh fmedgtarqr lrgpakgeag vegpplarve asatlkrrir akqsqqenvk
     1141 filtesdtvk rrpkakepdi gpepppplsv yqngtatirr rpaseqagpp elppppppae
     1201 ppptdlmplp plplpdgsar kpvkppvspk pilaqpvski qgsptpaskk vplpgpgspe
     1261 vkrahgtppp vspkpppppt apkpakalag lqsssatpsp vpsparqppa alikpasspp
     1321 sqsaspakpp spgapalqvp tkppraaasv vsgppvasdc aspgdsarqk leetsaclaa
     1381 alqaveekir qedgqgprps sieekstgsi ledigsmfdd ladqldamle
//
LOCUS       NP_112415                381 aa            linear   ROD 27-APR-2025
DEFINITION  sharpin [Rattus norvegicus].
ACCESSION   NP_112415
VERSION     NP_112415.1
DBSOURCE    REFSEQ: accession NM_031153.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Damgaard,R.B., Walker,J.A., Marco-Casanova,P., Morgan,N.V.,
            Titheradge,H.L., Elliott,P.R., McHale,D., Maher,E.R.,
            McKenzie,A.N.J. and Komander,D.
  TITLE     The Deubiquitinase OTULIN Is an Essential Negative Regulator of
            Inflammation and Autoimmunity
  JOURNAL   Cell 166 (5), 1215-1230 (2016)
   PUBMED   27523608
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Elliott,P.R., Nielsen,S.V., Marco-Casanova,P., Fiil,B.K.,
            Keusekotten,K., Mailand,N., Freund,S.M., Gyrd-Hansen,M. and
            Komander,D.
  TITLE     Molecular basis and regulation of OTULIN-LUBAC interaction
  JOURNAL   Mol Cell 54 (3), 335-348 (2014)
   PUBMED   24726323
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Calderwood,D.A., Campbell,I.D. and Critchley,D.R.
  TITLE     Talins and kindlins: partners in integrin-mediated adhesion
  JOURNAL   Nat Rev Mol Cell Biol 14 (8), 503-517 (2013)
   PUBMED   23860236
  REMARK    Review article
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Bouvard,D., Pouwels,J., De Franceschi,N. and Ivaska,J.
  TITLE     Integrin inactivators: balancing cellular functions in vitro and in
            vivo
  JOURNAL   Nat Rev Mol Cell Biol 14 (7), 430-442 (2013)
   PUBMED   23719537
  REMARK    Review article
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Chu,W.M.
  TITLE     Tumor necrosis factor
  JOURNAL   Cancer Lett 328 (2), 222-225 (2013)
   PUBMED   23085193
  REMARK    Review article
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Gerlach,B., Cordier,S.M., Schmukle,A.C., Emmerich,C.H., Rieser,E.,
            Haas,T.L., Webb,A.I., Rickard,J.A., Anderton,H., Wong,W.W.,
            Nachbur,U., Gangoda,L., Warnken,U., Purcell,A.W., Silke,J. and
            Walczak,H.
  TITLE     Linear ubiquitination prevents inflammation and regulates immune
            signalling
  JOURNAL   Nature 471 (7340), 591-596 (2011)
   PUBMED   21455173
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Jung,J., Kim,J.M., Park,B., Cheon,Y., Lee,B., Choo,S.H., Koh,S.S.
            and Lee,S.
  TITLE     Newly identified tumor-associated role of human Sharpin
  JOURNAL   Mol Cell Biochem 340 (1-2), 161-167 (2010)
   PUBMED   20179993
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Daigo,Y., Takayama,I., Ward,S.M., Sanders,K.M. and Fujino,M.A.
  TITLE     Novel human and mouse genes encoding a shank-interacting protein
            and its upregulation in gastric fundus of W/WV mouse
  JOURNAL   J Gastroenterol Hepatol 18 (6), 712-718 (2003)
   PUBMED   12753155
  REMARK    GeneRIF: The upregulation of Shank-interacting protein-like 1
            (SIPL1) in the fundus of W/WV mice, and expression in the upper
            gastrointestinal tract suggest that the SIPL1 gene could be
            associated with interstitial cells of Cajal (ICC) function in mice
            and humans.
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Lim,S., Sala,C., Yoon,J., Park,S., Kuroda,S., Sheng,M. and Kim,E.
  TITLE     Sharpin, a novel postsynaptic density protein that directly
            interacts with the shank family of proteins
  JOURNAL   Mol Cell Neurosci 17 (2), 385-397 (2001)
   PUBMED   11178875
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Gijbels,M.J., HogenEsch,H., Blauw,B., Roholl,P. and Zurcher,C.
  TITLE     Ultrastructure of epidermis of mice with chronic proliferative
            dermatitis
  JOURNAL   Ultrastruct Pathol 19 (2), 107-111 (1995)
   PUBMED   7792947
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083553.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083553.1, AF203906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..381
                     /product="sharpin"
                     /note="shank-associated RH domain-interacting protein;
                     shank-interacting protein; SHANK-associated RH domain
                     interacting protein"
                     /calculated_mol_wt=40156
     Region          1..177
                     /region_name="Self-association.
                     /evidence=ECO:0000269|PubMed:11178875"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQL9.1)"
     Region          18..125
                     /region_name="Sharpin_PH"
                     /note="Sharpin PH domain; pfam16764"
                     /db_xref="CDD:465263"
     Region          121..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQL9.1)"
     Region          172..305
                     /region_name="Interaction with SHANK1.
                     /evidence=ECO:0000269|PubMed:11178875"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQL9.1)"
     Region          215..299
                     /region_name="Ubl_HOIL1"
                     /note="ubiquitin-like (Ubl) domain found in heme-oxidized
                     IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins;
                     cd01799"
                     /db_xref="CDD:340497"
     Site            order(217,222..224,226..228,230..233,257..258,260..261,
                     297..299)
                     /site_type="other"
                     /note="UBA interaction site [polypeptide binding]"
                     /db_xref="CDD:340497"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H0F6; propagated from
                     UniProtKB/Swiss-Prot (Q9EQL9.1)"
     Region          346..370
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          346..365
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     CDS             1..381
                     /gene="Sharpin"
                     /gene_synonym="Conneck1"
                     /coded_by="NM_031153.2:346..1491"
                     /db_xref="GeneID:81859"
                     /db_xref="RGD:631353"
ORIGIN      
        1 msppaggaaa aadpaspvvl lavqaavrll gaghedeaql rklqlkadpe rpgrfrlgll
       61 giepgavsle wplesicyti rgpnqhelqp ppggpgtfsv hflnseeaqq waalvrdata
      121 egqngndsta pvptpamcpt sppcssvtpt pkatqpemdl pqgsgnlkke elathlaqai
      181 aggdekaaaq vaailaqhhv alnvqlleaw fprgpirlqv tvedatsvls ssssahvslq
      241 ihphcsiaal qeqvfsefgf ppavqrwvig rclcmpersl asygvsqdgd paflyllsap
      301 revsghspqh skmdrklgcl fpqslelphn lqasssslps ppqpgwscps ctfinasnrp
      361 gcemcstqrp cawdpltats t
//
LOCUS       NP_001007742             369 aa            linear   ROD 27-APR-2025
DEFINITION  interferon-stimulated 20 kDa exonuclease-like 2 [Rattus
            norvegicus].
ACCESSION   NP_001007742 XP_342274
VERSION     NP_001007742.1
DBSOURCE    REFSEQ: accession NM_001007741.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Coute,Y., Kindbeiter,K., Belin,S., Dieckmann,R., Duret,L.,
            Bezin,L., Sanchez,J.C. and Diaz,J.J.
  TITLE     ISG20L2, a novel vertebrate nucleolar exoribonuclease involved in
            ribosome biogenesis
  JOURNAL   Mol Cell Proteomics 7 (3), 546-559 (2008)
   PUBMED   18065403
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079314.1.
            
            On Nov 29, 2004 this sequence version replaced XP_342274.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079314.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..369
                     /product="interferon-stimulated 20 kDa exonuclease-like 2"
                     /calculated_mol_wt=41180
     Region          36..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU3.1)"
     Region          80..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU3.1)"
     Region          125..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXU3.1)"
     Region          196..352
                     /region_name="ISG20"
                     /note="DEDDh 3'-5' exonuclease domain of Interferon
                     Stimulated Gene product of 20 kDa, and similar proteins;
                     cd06149"
                     /db_xref="CDD:99852"
     Site            order(199..202,204,242,246,278..279,281..283,338,343)
                     /site_type="active"
                     /db_xref="CDD:99852"
     Site            order(199..202,204,242,246,278..279,281..282,338,343)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99852"
     Site            order(199,201,283,338,343)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99852"
     CDS             1..369
                     /gene="Isg20l2"
                     /coded_by="NM_001007741.1:397..1506"
                     /db_xref="GeneID:361977"
                     /db_xref="RGD:1359413"
ORIGIN      
        1 mstillnldf gepskkafgg nakhqrfvkk rrfleqkgfl skknqppskv sklnseppkk
       61 getsrvdsis kilsclkkkk eaaaskrdse qskdkkasls wltpapskkt dsvvakidll
      121 gefqsalpkp krrtqkkgsk kplkkkiate nstqtqskdk gsnkkplkkn avqnstqaqp
      181 edkcpkvpqs lprkmvaidc emvgtgpkgr vsslarcsiv nyngdvlyde yirppcyivd
      241 yrtrwsgirk chmvnatpfk tarsqilkil sgkvvvghai hndykalqyf hpksltrdts
      301 qipllnrkad cpenvtlslk hltkkllsrd iqtglsghss vedaqatlel yklveveweq
      361 hlaqnppen
//
LOCUS       NP_579851                366 aa            linear   ROD 27-APR-2025
DEFINITION  protein Tob1 [Rattus norvegicus].
ACCESSION   NP_579851
VERSION     NP_579851.2
DBSOURCE    REFSEQ: accession NM_133317.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Perez,R.C., Yang,X., Familari,M., Martinez,G., Lovicu,F.J.,
            Hime,G.R. and de Iongh,R.U.
  TITLE     TOB1 and TOB2 mark distinct RNA processing granules in
            differentiating lens fiber cells
  JOURNAL   J Mol Histol 55 (1), 121-138 (2024)
   PUBMED   38165569
  REMARK    GeneRIF: TOB1 and TOB2 mark distinct RNA processing granules in
            differentiating lens fiber cells.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Doidge,R., Mittal,S., Aslam,A. and Winkler,G.S.
  TITLE     The anti-proliferative activity of BTG/TOB proteins is mediated via
            the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the
            Ccr4-not complex
  JOURNAL   PLoS One 7 (12), e51331 (2012)
   PUBMED   23236473
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Hosoda,N., Funakoshi,Y., Hirasawa,M., Yamagishi,R., Asano,Y.,
            Miyagawa,R., Ogami,K., Tsujimoto,M. and Hoshino,S.
  TITLE     Anti-proliferative protein Tob negatively regulates CPEB3 target by
            recruiting Caf1 deadenylase
  JOURNAL   EMBO J 30 (7), 1311-1323 (2011)
   PUBMED   21336257
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Horiuchi,M., Takeuchi,K., Noda,N., Muroya,N., Suzuki,T.,
            Nakamura,T., Kawamura-Tsuzuku,J., Takahasi,K., Yamamoto,T. and
            Inagaki,F.
  TITLE     Structural basis for the antiproliferative activity of the
            Tob-hCaf1 complex
  JOURNAL   J Biol Chem 284 (19), 13244-13255 (2009)
   PUBMED   19276069
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Miyasaka,T., Morita,M., Ito,K., Suzuki,T., Fukuda,H., Takeda,S.,
            Inoue,J., Semba,K. and Yamamoto,T.
  TITLE     Interaction of antiproliferative protein Tob with the CCR4-NOT
            deadenylase complex
  JOURNAL   Cancer Sci 99 (4), 755-761 (2008)
   PUBMED   18377426
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Jin,M., Wang,X.M., Tu,Y., Zhang,X.H., Gao,X., Guo,N., Xie,Z.,
            Zhao,G., Jing,N., Li,B.M. and Yu,L.
  TITLE     The negative cell cycle regulator, Tob (transducer of ErbB-2), is a
            multifunctional protein involved in hippocampus-dependent learning
            and memory
  JOURNAL   Neuroscience 131 (3), 647-659 (2005)
   PUBMED   15730870
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Maekawa,M., Nishida,E. and Tanoue,T.
  TITLE     Identification of the Anti-proliferative protein Tob as a MAPK
            substrate
  JOURNAL   J Biol Chem 277 (40), 37783-37787 (2002)
   PUBMED   12151396
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Yoshida,Y., Tanaka,S., Umemori,H., Minowa,O., Usui,M., Ikematsu,N.,
            Hosoda,E., Imamura,T., Kuno,J., Yamashita,T., Miyazono,K., Noda,M.,
            Noda,T. and Yamamoto,T.
  TITLE     Negative regulation of BMP/Smad signaling by Tob in osteoblasts
  JOURNAL   Cell 103 (7), 1085-1097 (2000)
   PUBMED   11163184
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Matsuda,S., Kawamura-Tsuzuku,J., Ohsugi,M., Yoshida,M., Emi,M.,
            Nakamura,Y., Onda,M., Yoshida,Y., Nishiyama,A. and Yamamoto,T.
  TITLE     Tob, a novel protein that interacts with p185erbB2, is associated
            with anti-proliferative activity
  JOURNAL   Oncogene 12 (4), 705-713 (1996)
   PUBMED   8632892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Nov 23, 2005 this sequence version replaced NP_579851.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF349723.1, SRR26643291.28998.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..366
                     /product="protein Tob1"
                     /note="transducer of ERBB2, 1"
                     /calculated_mol_wt=40450
     Region          1..106
                     /region_name="btg1"
                     /note="tob/btg1 family; smart00099"
                     /db_xref="CDD:128410"
     Region          22..39
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5K6.1)"
     Region          82..92
                     /region_name="Important for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5K6.1)"
     Region          144..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5K6.1)"
     Region          161..220
                     /region_name="Required for interaction with CPEB3.
                     /evidence=ECO:0000250|UniProtKB:P50616"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5K6.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P50616; propagated from
                     UniProtKB/Swiss-Prot (Q8R5K6.1)"
     Region          228..236
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5K6.1)"
     CDS             1..366
                     /gene="Tob1"
                     /coded_by="NM_133317.2:151..1251"
                     /db_xref="GeneID:170842"
                     /db_xref="RGD:621126"
ORIGIN      
        1 mqleiqvaln fiisylynkl prrrvnifge elerllkqky eghwypekpy kgsgfrcihv
       61 gekvdpvieq askesgldid dvrgnlpqdl svwidpfevs yqigekgpvk vlyvddsnen
      121 gceldkeikn sfnpeaqvfm pisdpassvs sspsppfghs aavsptfmpr stqpltftta
      181 tfaatkfgst kmknsgrssk vartspislg lnvnvndllk qkaisssmhs lyglglgsqq
      241 qpqpqpqqpp sqpppppppp qqqqqqqqqq qqqqqqqqqq pqqqtsalsp nakefifpnm
      301 qgqgsstngm fpgdsplnls plqysnafdv faaygglnek sfvdglnfsl nniqysnqqf
      361 qpvman
//
LOCUS       NP_852038                910 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor ionotropic, kainate 3 isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_852038 XP_579717
VERSION     NP_852038.2
DBSOURCE    REFSEQ: accession NM_181373.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Kumari,J., Vinnakota,R. and Kumar,J.
  TITLE     Structural and Functional Insights into GluK3-kainate Receptor
            Desensitization and Recovery
  JOURNAL   Sci Rep 9 (1), 10254 (2019)
   PUBMED   31311973
  REMARK    GeneRIF: Structural and Functional Insights into GluK3-kainate
            Receptor Desensitization and Recovery.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Fujikawa,T., Petralia,R.S., Fitzgerald,T.S., Wang,Y.X., Millis,B.,
            Morgado-Diaz,J.A., Kitamura,K. and Kachar,B.
  TITLE     Localization of kainate receptors in inner and outer hair cell
            synapses
  JOURNAL   Hear Res 314, 20-32 (2014)
   PUBMED   24858010
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Zhou,W., Zhou,L.Q., Zhang,S.L., Liu,B., Leng,Y.M., Zhou,R.H. and
            Kong,W.J.
  TITLE     The changes in mGluR2 and mGluR7 expression in rat medial
            vestibular nucleus and flocculus following unilateral
            labyrinthectomy
  JOURNAL   Int J Mol Sci 14 (11), 22857-22875 (2013)
   PUBMED   24264036
  REMARK    GeneRIF: Our results suggest that mGluR2 and mGluR7 may contribute
            to the early rebalancing of spontaneous resting activity in the MVN
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Veran,J., Kumar,J., Pinheiro,P.S., Athane,A., Mayer,M.L.,
            Perrais,D. and Mulle,C.
  TITLE     Zinc potentiates GluK3 glutamate receptor function by stabilizing
            the ligand binding domain dimer interface
  JOURNAL   Neuron 76 (3), 565-578 (2012)
   PUBMED   23141068
  REMARK    GeneRIF: Zinc binding stabilizes the labile GluK3 dimer interface,
            slows desensitization and potentiates currents.
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Schiffer,H.H., Swanson,G.T. and Heinemann,S.F.
  TITLE     Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are
            functional kainate receptor subunits with a low sensitivity to
            glutamate
  JOURNAL   Neuron 19 (5), 1141-1146 (1997)
   PUBMED   9390526
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Flor,P.J., Van Der Putten,H., Ruegg,D., Lukic,S., Leonhardt,T.,
            Bence,M., Sansig,G., Knopfel,T. and Kuhn,R.
  TITLE     A novel splice variant of a metabotropic glutamate receptor, human
            mGluR7b
  JOURNAL   Neuropharmacology 36 (2), 153-159 (1997)
   PUBMED   9144652
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Nutt,S.L., Hoo,K.H., Rampersad,V., Deverill,R.M., Elliott,C.E.,
            Fletcher,E.J., Adams,S.L., Korczak,B., Foldes,R.L. and Kamboj,R.K.
  TITLE     Molecular characterization of the human EAA5 (GluR7) receptor: a
            high-affinity kainate receptor with novel potential RNA editing
            sites
  JOURNAL   Recept Channels 2 (4), 315-326 (1994)
   PUBMED   7719709
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Lomeli,H., Wisden,W., Kohler,M., Keinanen,K., Sommer,B. and
            Seeburg,P.H.
  TITLE     High-affinity kainate and domoate receptors in rat brain
  JOURNAL   FEBS Lett 307 (2), 139-143 (1992)
   PUBMED   1322826
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Bettler,B., Egebjerg,J., Sharma,G., Pecht,G., Hermans-Borgmeyer,I.,
            Moll,C., Stevens,C.F. and Heinemann,S.
  TITLE     Cloning of a putative glutamate receptor: a low affinity
            kainate-binding subunit
  JOURNAL   Neuron 8 (2), 257-265 (1992)
   PUBMED   1371217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF027331.1, JAXUCZ010000005.1
            and M83552.1.
            
            On Dec 20, 2007 this sequence version replaced NP_852038.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. Compared to other kainate or AMPA receptors, this subunit
            exhibits a lower sensitivity to glutamate, and thus may play a
            unique role in neurotransmission in the brain. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2, also known as GluR7b) uses a
            different donor splice site at the penultimate exon compared to
            transcript variant 1. This results in a frame-shift and a shorter
            isoform (2) with a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF027331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840106, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..910
                     /product="glutamate receptor ionotropic, kainate 3 isoform
                     2 precursor"
                     /note="glutamate receptor subunit kainate subtype;
                     glutamate receptor 7; glutamate receptor, ionotropic,
                     kainate 3"
                     /calculated_mol_wt=99367
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3771
     Region          37..417
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            order(90..92,96,127,179,182,186,189,192..193,203..206)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142,
                     ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20951142; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Region          433..801
                     /region_name="PBP2_iGluR_Kainate_GluR7"
                     /note="GluR7 subtype of kainate receptor, type 2
                     periplasmic-binding fold superfamily; cd13723"
                     /db_xref="CDD:270441"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            order(491,518..520,525)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270441"
     Site            order(521..523,526..527,531..534,537,695,761..762,
                     776..777,780..782,784..785,787..790)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270441"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     Site            637..657
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     Site            752
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42264.1)"
     Site            821..841
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42264.1)"
     CDS             1..910
                     /gene="Grik3"
                     /gene_synonym="GluK3; gluR-7; GluR7"
                     /coded_by="NM_181373.3:132..2864"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:298521"
                     /db_xref="RGD:71027"
ORIGIN      
        1 mtapwrrlrs lvweywagfl vcafwipdsr gmphvirigg ifeyadgpna qvmnaeehaf
       61 rfsaniinrn rtllpnttlt ydiqrihfhd sfeatkkacd qlalgvvaif gpsqgsctna
      121 vqsicnalev phiqlrwkhh pldnkdtfyv nlypdyasls haildlvqsl kwrsatvvyd
      181 dstglirlqe limapsryni rlkirqlpid sddsrpllke mkrgrefrii fdcshtmaaq
      241 ilkqamamgm mteyyhfift tldlyaldle pyrysgvnlt gfrilnvdnp hvsaivekws
      301 merlqaapra esglldgvmm tdaallydav hivsvcyqra pqmtvnslqc hrhkawrfgg
      361 rfmnfikeaq wegltgrivf nktsglrtdf dldiislked glekvgvwsp adglniteva
      421 kgrgpnvtds ltnrslivtt lleepfvmfr ksdrtlygnd rfegycidll kelahilgfs
      481 yeirlvedgk ygaqddkgqw ngmvkelidh kadlavaplt ithvrekaid fskpfmtlgv
      541 silyrkpngt npsvfsflnp lspdiwmyvl laylgvscvl fviarfspye wydahpcnpg
      601 sevvennftl lnsfwfgmgs lmqqgselmp kalstriigg iwwfftliii ssytanlaaf
      661 ltvermespi dsaddlakqt kieygavkdg atmtffkksk istfekmwaf msskpsalvk
      721 nneegiqrtl tadyallmes ttieyitqrn cnltqiggli dskgygigtp mgspyrdkit
      781 iailqlqeed klhimkekww rgsgcpeeen keasalgiqk iggifivlaa glvlsvlvav
      841 gefiyklrkt aereqvrpwr rlrwtgkeal flqhsgrrdp llphlpaasq aqatasydgq
      901 drcgyqhahl
//
LOCUS       NP_445747                713 aa            linear   ROD 27-APR-2025
DEFINITION  calpastatin isoform a [Rattus norvegicus].
ACCESSION   NP_445747 XP_346608 XP_347364
VERSION     NP_445747.2
DBSOURCE    REFSEQ: accession NM_053295.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Gritsyna,Y.V., Salmov,N.N., Bobylev,A.G., Ulanova,A.D.,
            Kukushkin,N.I., Podlubnaya,Z.A. and Vikhlyantsev,I.M.
  TITLE     Increased Autolysis of mu-Calpain in Skeletal Muscles of Chronic
            Alcohol-Fed Rats
  JOURNAL   Alcohol Clin Exp Res 41 (10), 1686-1694 (2017)
   PUBMED   28800153
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Manfredi,L.H., Lustrino,D., Machado,J., Silveira,W.A., Zanon,N.M.,
            Navegantes,L.C. and Kettelhut,I.C.
  TITLE     Adrenodemedullation activates the Ca2+-dependent proteolysis in
            soleus muscles from rats exposed to cold
  JOURNAL   J Appl Physiol (1985) 122 (2), 317-326 (2017)
   PUBMED   27765842
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Mochida,S., Hida,Y., Tanifuji,S., Hagiwara,A., Hamada,S., Abe,M.,
            Ma,H., Yasumura,M., Kitajima,I., Sakimura,K. and Ohtsuka,T.
  TITLE     SAD-B Phosphorylation of CAST Controls Active Zone Vesicle
            Recycling for Synaptic Depression
  JOURNAL   Cell Rep 16 (11), 2901-2913 (2016)
   PUBMED   27626661
REFERENCE   4  (residues 1 to 713)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 713)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 713)
  AUTHORS   Yasuoka,H., Sugano,Y., Oka,T., Watanabe,C., Kaneko,Y., Nojima,T.,
            Matsumura,M., Fujii,T. and Mimori,T.
  TITLE     [Antigenic epitopes recognized by autoantibodies to calpastatin in
            patients with rheumatoid arthritis and their clinical significance]
  JOURNAL   Ryumachi 37 (3), 458-466 (1997)
   PUBMED   9256029
REFERENCE   7  (residues 1 to 713)
  AUTHORS   Despres,N., Talbot,G., Plouffe,B., Boire,G. and Menard,H.A.
  TITLE     Detection and expression of a cDNA clone that encodes a polypeptide
            containing two inhibitory domains of human calpastatin and its
            recognition by rheumatoid arthritis sera
  JOURNAL   J Clin Invest 95 (4), 1891-1896 (1995)
   PUBMED   7706496
REFERENCE   8  (residues 1 to 713)
  AUTHORS   Lee,W.J., Hatanaka,M. and Maki,M.
  TITLE     Multiple forms of rat calpastatin cDNA in the coding region of
            functionally unknown amino-terminal domain
  JOURNAL   Biochim Biophys Acta 1129 (2), 251-253 (1992)
   PUBMED   1730065
REFERENCE   9  (residues 1 to 713)
  AUTHORS   Ishida,S., Emori,Y. and Suzuki,K.
  TITLE     Rat calpastatin has diverged primary sequence from other mammalian
            calpastatins but retains functionally important sequences
  JOURNAL   Biochim Biophys Acta 1088 (3), 436-438 (1991)
   PUBMED   2015306
REFERENCE   10 (residues 1 to 713)
  AUTHORS   Uemori,T., Shimojo,T., Asada,K., Asano,T., Kimizuka,F., Kato,I.,
            Maki,M., Hatanaka,M., Murachi,T., Hanzawa,H. et al.
  TITLE     Characterization of a functional domain of human calpastatin
  JOURNAL   Biochem Biophys Res Commun 166 (3), 1485-1493 (1990)
   PUBMED   2407243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091239.1 and Y13588.1.
            
            On Sep 23, 2005 this sequence version replaced NP_445747.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ186624.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q11"
     Protein         1..713
                     /product="calpastatin isoform a"
                     /note="calpain inhibitor"
                     /calculated_mol_wt=77166
     Region          1..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27321.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            86
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51125; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          128..258
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          208..260
                     /region_name="Inhibitory domain 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P27321.3)"
     Region          253..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27321.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          269..391
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          405..501
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          442..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27321.3)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          516..638
                     /region_name="Calpain_inhib"
                     /note="Calpain inhibitor; pfam00748"
                     /db_xref="CDD:459923"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20810; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Region          544..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27321.3)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P27321.3)"
     CDS             1..713
                     /gene="Cast"
                     /coded_by="NM_053295.2:148..2289"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:25403"
                     /db_xref="RGD:2278"
ORIGIN      
        1 msrpgpkpaa ssrprrgaaa shtqehvnek nigssskpae kkgsdevtas saatgtsprm
       61 sttgakavki eseksqssep pvihekkpkg kpkegsepqt lpkhasdtgs khahkekals
      121 rsneqivsek ssesktkfqd apsadgesva ggvtvatasd kvvvkkkekk sltptlpmes
      181 tlnklsdksg vnaalddlid tlgecedtnk ddppytgpvv ldpmdstyle algikegtip
      241 peyrkllekn eaitgplpds pkpmgidhai dalssdftcs sptgkqteke kstgesskaq
      301 sagvtrsavp pqekkrkvee evmndqalqa lsdslgtrqp dpqshlrqak qvkeakakee
      361 rqekcgeded tvpaeyrlkp akdkdgkpll pepeetskcl seseligels adfvqptyqe
      421 kpsmpaakik kgvvpddave tlarslgtrk edpedekslv dkvkekakee dheklgekee
      481 tippdyrlei vkdkdgkpll pkeaeeqlpp lsddflldal sqdfsspani lslgfedakl
      541 saavsetvsq vpapsnhtaa pppgterrdk elddaldels dslgqrqpdp denkplddkv
      601 kekikaehse klgerddtip peyrhlldnd gkdkpekplt kntekpgqdq dpidalsedl
      661 dscppttets qnttkekgkk tssskaskne ektkdsskkt eevpkpkvde dat
//
LOCUS       NP_113920                304 aa            linear   ROD 27-APR-2025
DEFINITION  sulfotransferase 1C1 [Rattus norvegicus].
ACCESSION   NP_113920
VERSION     NP_113920.2
DBSOURCE    REFSEQ: accession NM_031732.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Runge-Morris,M. and Kocarek,T.A.
  TITLE     Expression of the sulfotransferase 1C family: implications for
            xenobiotic toxicity
  JOURNAL   Drug Metab Rev 45 (4), 450-459 (2013)
   PUBMED   24028175
  REMARK    Review article
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Meinl,W., Donath,C., Schneider,H., Sommer,Y. and Glatt,H.
  TITLE     SULT1C3, an orphan sequence of the human genome, encodes an enzyme
            activating various promutagens
  JOURNAL   Food Chem Toxicol 46 (4), 1249-1256 (2008)
   PUBMED   17936463
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Matsui,M., Tamura,H., Nagai,F., Homma,H., Miyawaki,A. and
            Mikoshiba,K.
  TITLE     On the nature of rat hepatic and mouse olfactory sulfotransferases
  JOURNAL   Chem Biol Interact 109 (1-3), 69-80 (1998)
   PUBMED   9566734
  REMARK    Review article
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Yamazoe,Y., Nagata,K., Ozawa,S. and Kato,R.
  TITLE     Structural similarity and diversity of sulfotransferases
  JOURNAL   Chem Biol Interact 92 (1-3), 107-117 (1994)
   PUBMED   8033246
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Nagata,K., Ozawa,S., Miyata,M., Shimada,M., Gong,D.W., Yamazoe,Y.
            and Kato,R.
  TITLE     Isolation and expression of a cDNA encoding a male-specific rat
            sulfotransferase that catalyzes activation of
            N-hydroxy-2-acetylaminofluorene
  JOURNAL   J Biol Chem 268 (33), 24720-24725 (1993)
   PUBMED   8227031
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088125.1.
            
            On Jun 10, 2007 this sequence version replaced NP_113920.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088125.1, FQ219411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..304
                     /product="sulfotransferase 1C1"
                     /EC_number="2.8.2.-"
                     /note="sulfotransferase, phenol preferring 2;
                     sulfotransferase family 1A, member 2; sulfotransferase
                     family 1A, phenol-preferring, member 2; Phenol
                     sulfotransferase 1c1; N-hydroxyarylamine sulfotransferase;
                     sulfotransferase family, cytosolic, 1C, member 1;
                     sulphotransferase family cytosolic 1A phenol-preferring
                     member 2; N-hydroxylarylamine sulfotransferase;
                     sulfotransferase 1C1-like; sulfotransferase family,
                     cytosolic, 1C, member 3"
                     /calculated_mol_wt=35643
     Region          46..296
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     CDS             1..304
                     /gene="Sult1c3"
                     /gene_synonym="HAST-I; St1c1; Stp2; Sult1a2; Sult1c1"
                     /coded_by="NM_031732.2:115..1029"
                     /db_xref="GeneID:65185"
                     /db_xref="RGD:3768"
ORIGIN      
        1 mslekmkdlh lgeqdlqpet revngilmsk lmsdnwdkiw nfqakpddll iatyakagtt
       61 wtqeivdmiq ndgdvqkcqr antydrhpfi ewtlppplns gldlankmps prtlkthlpv
      121 hmlppsfwke nskiiyvarn akdclvsyyy fsrmnkmlpd pgtlgeyieq fkagkvlwgs
      181 wydhvkgwwd vkdqhrilyl fyedmkedpk reikkiakfl ekdiseevln kiiyhtsfdv
      241 mkenpmanyt tlpssimdhs ispfmrkgmp gdwknyftva qsedfdedyr rkmagsnitf
      301 rtei
//
LOCUS       NP_001014067             276 aa            linear   ROD 27-APR-2025
DEFINITION  ARL14 effector protein [Rattus norvegicus].
ACCESSION   NP_001014067 XP_230362
VERSION     NP_001014067.1
DBSOURCE    REFSEQ: accession NM_001014045.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089920.1.
            
            On Apr 20, 2005 this sequence version replaced XP_230362.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089920.1, SRR8487231.49843.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q33"
     Protein         1..276
                     /product="ARL14 effector protein"
                     /note="ARF7 effector protein; ADP-ribosylation factor-like
                     14 effector protein; uncharacterized protein C11orf46
                     homolog; ADP-ribosylation factor like GTPase 14 effector
                     protein"
                     /calculated_mol_wt=30981
     Region          145..248
                     /region_name="ARF7EP_C"
                     /note="ARF7 effector protein C-terminus; pfam14949"
                     /db_xref="CDD:464395"
     Region          159..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVK8.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N8R7; propagated from
                     UniProtKB/Swiss-Prot (Q5FVK8.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVK8.1)"
     CDS             1..276
                     /gene="Arl14ep"
                     /gene_synonym="ARF7EP; RGD1311463"
                     /coded_by="NM_001014045.1:100..930"
                     /db_xref="GeneID:311279"
                     /db_xref="RGD:1311463"
ORIGIN      
        1 mdpcsvgvql rtthdchktf ytrhtgfktl kelssndmll lqlrtgmtls gnnticlhhv
       61 kiyierfeel qksccdpfni hkklakknlh vidlddatfl sakfgrqlvp gwklcpkctq
      121 iingsvdvds ddrqrrkpes dgrtakalrs lqftnpgkqt efapesgkre krkltknasa
      181 ssdrqiipak skvydsqgll ifsgmdlcdc ldedclgcfy acptcgstkc gaecrcdrkw
      241 lyeqieiegg eiihnkhagk aygllspchp ydilqk
//
LOCUS       NP_071989                 63 aa            linear   ROD 27-APR-2025
DEFINITION  beta-defensin 4 precursor [Rattus norvegicus].
ACCESSION   NP_071989
VERSION     NP_071989.1
DBSOURCE    REFSEQ: accession NM_022544.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Kolar,S.S., Baidouri,H., Hanlon,S. and McDermott,A.M.
  TITLE     Protective role of murine beta-defensins 3 and 4 and
            cathelin-related antimicrobial peptide in Fusarium solani keratitis
  JOURNAL   Infect Immun 81 (8), 2669-2677 (2013)
   PUBMED   23670560
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Deng,L.X., Wu,G.X., Cao,Y., Fan,B., Gao,X., Luo,L. and Huang,N.
  TITLE     The chromosomal protein HMGN2 mediates lipopolysaccharide-induced
            expression of beta-defensins in A549 cells
  JOURNAL   FEBS J 278 (12), 2152-2166 (2011)
   PUBMED   21518253
  REMARK    GeneRIF: HMGN2 acts as a positive modulator of nuclear factor
            kappaB signalling to promote lipopolysaccharide-induced
            beta-defensin-2 expression.
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Augustin,D.K., Heimer,S.R., Tam,C., Li,W.Y., Le Due,J.M.,
            Evans,D.J. and Fleiszig,S.M.
  TITLE     Role of defensins in corneal epithelial barrier function against
            Pseudomonas aeruginosa traversal
  JOURNAL   Infect Immun 79 (2), 595-605 (2011)
   PUBMED   21115716
REFERENCE   4  (residues 1 to 63)
  AUTHORS   Chen,L., Sun,B.B., Wang,T., Wang,X., Li,J.Q., Wang,H.X.,
            Zhang,S.F., Liu,D.S., Liu,L., Xu,D., Ou,X.M., Chen,Y.J., Yang,T.,
            Zhou,H. and Wen,F.Q.
  TITLE     Cigarette smoke enhances {beta}-defensin 2 expression in rat
            airways via nuclear factor-{kappa}B activation
  JOURNAL   Eur Respir J 36 (3), 638-645 (2010)
   PUBMED   20150208
  REMARK    GeneRIF: Cigarette smoke enhances {beta}-defensin 2 expression in
            rat airways via nuclear factor-{kappa}B activation
REFERENCE   5  (residues 1 to 63)
  AUTHORS   Rohrl,J., Yang,D., Oppenheim,J.J. and Hehlgans,T.
  TITLE     Specific binding and chemotactic activity of mBD4 and its
            functional orthologue hBD2 to CCR6-expressing cells
  JOURNAL   J Biol Chem 285 (10), 7028-7034 (2010)
   PUBMED   20068036
REFERENCE   6  (residues 1 to 63)
  AUTHORS   Ashitani,J., Kumamoto,K., Hiratsuka,T., Mukae,H., Nakazato,M. and
            Matsukura,S.
  TITLE     [Beta-defensins in plasma and bronchoalveolar lavage fluid in
            patients with non-tuberculous mycobacterium infection]
  JOURNAL   Nihon Kokyuki Gakkai Zasshi 39 (1), 12-16 (2001)
   PUBMED   11296379
REFERENCE   7  (residues 1 to 63)
  AUTHORS   Jia,H.P., Mills,J.N., Barahmand-Pour,F., Nishimura,D.,
            Mallampali,R.K., Wang,G., Wiles,K., Tack,B.F., Bevins,C.L. and
            McCray,P.B. Jr.
  TITLE     Molecular cloning and characterization of rat genes encoding
            homologues of human beta-defensins
  JOURNAL   Infect Immun 67 (9), 4827-4833 (1999)
   PUBMED   10456937
REFERENCE   8  (residues 1 to 63)
  AUTHORS   Hiratsuka,T., Nakazato,M., Ashitani,J. and Matsukura,S.
  TITLE     [A study of human beta-defensin-1 and human beta-defensin-2 in
            airway mucosal defense]
  JOURNAL   Kansenshogaku Zasshi 73 (2), 156-162 (1999)
   PUBMED   10213993
REFERENCE   9  (residues 1 to 63)
  AUTHORS   Singh,P.K., Jia,H.P., Wiles,K., Hesselberth,J., Liu,L.,
            Conway,B.A., Greenberg,E.P., Valore,E.V., Welsh,M.J., Ganz,T.,
            Tack,B.F. and McCray,P.B. Jr.
  TITLE     Production of beta-defensins by human airway epithelia
  JOURNAL   Proc Natl Acad Sci U S A 95 (25), 14961-14966 (1998)
   PUBMED   9843998
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1999 Mar 2;96(5):2569]
REFERENCE   10 (residues 1 to 63)
  AUTHORS   Bals,R., Wang,X., Wu,Z., Freeman,T., Bafna,V., Zasloff,M. and
            Wilson,J.M.
  TITLE     Human beta-defensin 2 is a salt-sensitive peptide antibiotic
            expressed in human lung
  JOURNAL   J Clin Invest 102 (5), 874-880 (1998)
   PUBMED   9727055
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY621374.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY621374.1, AF068861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..63
                     /product="beta-defensin 4 precursor"
                     /note="beta-defensin 4; BD-2; BD-4; RBD-2; RBD-4; beta
                     defensin-2; defensin beta 3; beta-defensin 3"
                     /calculated_mol_wt=4382
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2582
     mat_peptide     23..63
                     /product="Beta-defensin 4. /id=PRO_0000006962"
                     /note="propagated from UniProtKB/Swiss-Prot (O88514.1)"
                     /calculated_mol_wt=4382
     Site            23
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P46162; propagated from
                     UniProtKB/Swiss-Prot (O88514.1)"
     Region          27..61
                     /region_name="Defensin_beta"
                     /note="Beta defensin; pfam00711"
                     /db_xref="CDD:459914"
     CDS             1..63
                     /gene="Defb4"
                     /gene_synonym="Defb2; Defb3"
                     /coded_by="NM_022544.2:139..330"
                     /db_xref="GeneID:64389"
                     /db_xref="RGD:619944"
ORIGIN      
        1 mrihyllfsf llvllsplsa ftqsinnpit cltkggvcwg pctggfrqig tcglprvrcc
       61 kkk
//
LOCUS       NP_001009654             226 aa            linear   ROD 27-APR-2025
DEFINITION  kinetochore protein Spc25 [Rattus norvegicus].
ACCESSION   NP_001009654 XP_215747
VERSION     NP_001009654.1
DBSOURCE    REFSEQ: accession NM_001009654.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Bharadwaj,R., Qi,W. and Yu,H.
  TITLE     Identification of two novel components of the human NDC80
            kinetochore complex
  JOURNAL   J Biol Chem 279 (13), 13076-13085 (2004)
   PUBMED   14699129
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088213.1.
            
            On Jan 13, 2005 this sequence version replaced XP_215747.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088213.1, EV776670.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..226
                     /product="kinetochore protein Spc25"
                     /note="spindle pole body component 25 homolog; SPC25,
                     NDC80 kinetochore complex component, homolog"
                     /calculated_mol_wt=26058
     Region          1..146
                     /region_name="Interaction with the N-terminus of SPBC24.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M856.1)"
     Region          1..58
                     /region_name="Interaction with the NDC80-NUF2 subcomplex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M856.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HBM1; propagated from
                     UniProtKB/Swiss-Prot (Q5M856.1)"
     Region          69..>165
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          130..217
                     /region_name="RWD_Spc25"
                     /note="RWD domain of kinetochore protein Spc25 and related
                     proteins; cd23784"
                     /db_xref="CDD:467646"
     Site            order(132..133,135..137,140..141,143,145,147..148,150,156,
                     162,199,202..203,208..215,217)
                     /site_type="other"
                     /note="Spc24 interface [polypeptide binding]"
                     /db_xref="CDD:467646"
     Region          147..226
                     /region_name="Interaction with the C-terminus of SPBC24.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M856.1)"
     Site            order(149..151,154,156..157,159,161,171,173,178,184,190,
                     209)
                     /site_type="other"
                     /note="CENP-T binding site [polypeptide binding]"
                     /db_xref="CDD:467646"
     CDS             1..226
                     /gene="Spc25"
                     /gene_synonym="RGD1307811; Spbc25"
                     /coded_by="NM_001009654.1:69..749"
                     /db_xref="GeneID:295661"
                     /db_xref="RGD:1307811"
ORIGIN      
        1 mgedelaafe ksinefgdkf ryrlsdnrsq vlglkdafkd siralsekls lklkeeerma
       61 emileyknql ckqnkliqek kdnvlkmiae vkgkgqevev ltaniqdlke eyarkketis
      121 tankaneerl krlqksadly rdrlgleirk ipgdklqfif tsidpknpes pfmfslsine
      181 akeyevsdcs phleclaefq ekvrktnnfs aflanvrkaf iakvhn
//
LOCUS       NP_071586                403 aa            linear   ROD 27-APR-2025
DEFINITION  queuine tRNA-ribosyltransferase catalytic subunit 1 [Rattus
            norvegicus].
ACCESSION   NP_071586
VERSION     NP_071586.2
DBSOURCE    REFSEQ: accession NM_022250.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chen,Y.C., Kelly,V.P., Stachura,S.V. and Garcia,G.A.
  TITLE     Characterization of the human tRNA-guanine transglycosylase:
            confirmation of the heterodimeric subunit structure
  JOURNAL   RNA 16 (5), 958-968 (2010)
   PUBMED   20354154
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Boland,C., Hayes,P., Santa-Maria,I., Nishimura,S. and Kelly,V.P.
  TITLE     Queuosine formation in eukaryotic tRNA occurs via a
            mitochondria-localized heteromeric transglycosylase
  JOURNAL   J Biol Chem 284 (27), 18218-18227 (2009)
   PUBMED   19414587
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Shindo-Okada,N., Okada,N., Ohgi,T., Goto,T. and Nishimura,S.
  TITLE     Transfer ribonucleic acid guanine transglycosylase isolated from
            rat liver
  JOURNAL   Biochemistry 19 (2), 395-400 (1980)
   PUBMED   6986171
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097321.1.
            
            On Oct 12, 2007 this sequence version replaced NP_071586.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097321.1, SRR8487230.58597.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..403
                     /product="queuine tRNA-ribosyltransferase catalytic
                     subunit 1"
                     /EC_number="2.4.2.64"
                     /note="guanine insertion enzyme; tRNA-guanine
                     transglycosylase; queuine tRNA-ribosyltransferase 1"
                     /calculated_mol_wt=44056
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BXR0; propagated from
                     UniProtKB/Swiss-Prot (Q4QR99.1)"
     Region          26..381
                     /region_name="TGT"
                     /note="Queuine tRNA-ribosyltransferase; pfam01702"
                     /db_xref="CDD:460299"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BXR0; propagated from
                     UniProtKB/Swiss-Prot (Q4QR99.1)"
     Region          260..266
                     /region_name="RNA binding.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03218"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR99.1)"
     Region          284..288
                     /region_name="RNA binding, important for wobble base 34
                     recognition. /evidence=ECO:0000255|HAMAP-Rule:MF_03218"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR99.1)"
     CDS             1..403
                     /gene="Qtrt1"
                     /gene_synonym="Tgt; Tgut"
                     /coded_by="NM_022250.2:13..1224"
                     /db_xref="GeneID:64016"
                     /db_xref="RGD:620996"
ORIGIN      
        1 maavgspgsl esaprimrlv aecsrsrara gelrlphgtv atpvfmpvgt qatmkgitae
       61 qldslgcric lgntyhlglr pgpeliqkah glhgfmnwph nlltdsggfq mvslislsev
      121 teegvrfrsp ydgeetllsp ersveiqnal gsdiimqldd vvsstvtgpr veeamhrsvr
      181 wldrciaahk rqdkqnlfai iqgglnadlr ttclkemtkr dvpgfaiggl sggeskeqfw
      241 kmvalstsml pkdkprylmg vgyatdlvvc valgcdmfdc vyptrtarfg salvptgnlq
      301 lkkqqyakdf spinpecpca tcqthsrafl htllhsdnta alhhltvhni ayqlqllsaa
      361 rssileqrfp dfvrnfmrtm ygdhslcpaw aiealasvgi tlt
//
LOCUS       NP_001032278             782 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar RNA helicase 2 [Rattus norvegicus].
ACCESSION   NP_001032278 XP_228810
VERSION     NP_001032278.1
DBSOURCE    REFSEQ: accession NM_001037201.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Song,C., Hotz-Wagenblatt,A., Voit,R. and Grummt,I.
  TITLE     SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic
            R loops and safeguard genome stability
  JOURNAL   Genes Dev 31 (13), 1370-1381 (2017)
   PUBMED   28790157
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Calo,E., Flynn,R.A., Martin,L., Spitale,R.C., Chang,H.Y. and
            Wysocka,J.
  TITLE     RNA helicase DDX21 coordinates transcription and ribosomal RNA
            processing
  JOURNAL   Nature 518 (7538), 249-253 (2015)
   PUBMED   25470060
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Zhang,Z., Kim,T., Bao,M., Facchinetti,V., Jung,S.Y., Ghaffari,A.A.,
            Qin,J., Cheng,G. and Liu,Y.J.
  TITLE     DDX1, DDX21, and DHX36 helicases form a complex with the adaptor
            molecule TRIF to sense dsRNA in dendritic cells
  JOURNAL   Immunity 34 (6), 866-878 (2011)
   PUBMED   21703541
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Valdez,B.C., Henning,D., Perumal,K. and Busch,H.
  TITLE     RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two
            activities in separate domains of the same protein
  JOURNAL   Eur J Biochem 250 (3), 800-807 (1997)
   PUBMED   9461305
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Sykes,D.E. and Weiser,M.M.
  TITLE     The identification of genes specifically expressed in epithelial
            cells of the rat intestinal crypts
  JOURNAL   Differentiation 50 (1), 41-46 (1992)
   PUBMED   1639225
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105878.1.
            
            On Nov 18, 2005 this sequence version replaced XP_228810.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105878.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..782
                     /product="nucleolar RNA helicase 2"
                     /EC_number="3.6.4.13"
                     /note="RH II/Gu; gu-alpha; DEAD box protein 21; nucleolar
                     RNA helicase Gu; nucleolar RNA helicase II; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 21; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 21a; DEAD-box helicase
                     21; DEAD (Asp-Glu-Ala-Asp) box polypeptide 21b; DEAD
                     (Asp-Glu-Ala-Asp) box helicase 21"
                     /calculated_mol_wt=85835
     Region          1..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            39
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          182..210
                     /region_name="Q motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00552"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          184..570
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          335..338
                     /region_name="DEAD box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            596
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          613..705
                     /region_name="GUCT_RHII_Gualpha_beta"
                     /note="RNA-binding GUCT domain found in vertebrate RNA
                     helicase II/Gualpha (RH-II/Gualpha), RNA helicase
                     II/Gubeta (RH-II/Gubeta) and similar proteins; cd12936"
                     /db_xref="CDD:240593"
     Region          704..782
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          716..>765
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          720..747
                     /region_name="3 X 5 AA repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            778
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     CDS             1..782
                     /gene="Ddx21"
                     /gene_synonym="Ddx21a; Ddx21b"
                     /coded_by="NM_001037201.1:45..2393"
                     /db_xref="GeneID:317399"
                     /db_xref="RGD:1307306"
ORIGIN      
        1 mpgklrsask sesegteesm etlqkpsekk trkekpkskt deategveea asskvkavkk
       61 kgpseddvgp pkskkakkqe eepqddpask sktskkkkep lekkapsakt kemkaeepse
      121 eeadapkpkk tkkgkeangd vgekspglkn glshpkpdss stqapgeese tekeipveqk
      181 egafsnfpis eetvkllkar gvnflfpiqa ktfhhvysgk dliaqartgt gktfsfaipl
      241 ieklqgglqe rkrgrapqvl vlaptrelan qvskdfsdit kklsvacfyg gtpyggqier
      301 mrsgidilvg tpgrikdhlq ngkldltklk hvvldevdqm ldmgfadqve eilcvaykkd
      361 sednpqtllf satcphwvfn vakkymksty eqvdligkkt qkaaitvehl aikchwtera
      421 avigdvirvy sghqgrtiif cetkkdaqel sqntcikqda qslhgdipqk qreitlkgfr
      481 ngnfgvlvat nvaargldip evdlvvqscp pkdvesyihr sgrtgragrt gvcicfyqhk
      541 eeyqlaqveq kagikfkrig vpsateiika sskdairlld svpptaighf kqsaekliee
      601 kgavealaaa lahisgatsv dqrslinsqa gfvtmilrcs vempnisyaw kelkeqlges
      661 idakvkgmvf lkgklgvcfd vrteavteik ekwhdsrrwq ltvateqpel egppegyrgg
      721 rgqrdgsrgs frgqrggsrn frgqgqrggs rnfrgqrpgg gnksnrspnk gqkrsfskaf
      781 gq
//
LOCUS       NP_112297                355 aa            linear   ROD 27-APR-2025
DEFINITION  guanine nucleotide-binding protein G(i) subunit alpha-2 [Rattus
            norvegicus].
ACCESSION   NP_112297
VERSION     NP_112297.1
DBSOURCE    REFSEQ: accession NM_031035.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Sarkar,O., Li,Y. and Anand-Srivastava,M.B.
  TITLE     Nitric oxide attenuates overexpression of Gialpha proteins in
            vascular smooth muscle cells from SHR: Role of ROS and ROS-mediated
            signaling
  JOURNAL   PLoS One 12 (7), e0179301 (2017)
   PUBMED   28692698
  REMARK    GeneRIF: Nitric oxide decreased the enhanced expression of
            Gialpha-2/3 proteins and hyperproliferation of Vascular smooth
            muscle cells from spontaneously hypertensive rats by
            cGMP-independent mechanism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Ali El-Basyuni,Y., Li,Y. and Anand-Srivastava,M.B.
  TITLE     Knockdown of Inhibitory Guanine Nucleotide Binding Protein
            Gialpha-2 by Antisense Oligodeoxynucleotides Attenuates the
            Development of Hypertension and Tachycardia in Spontaneously
            Hypertensive Rats
  JOURNAL   J Am Heart Assoc 5 (11), e004594 (2016)
   PUBMED   27912212
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Wang,X.Y., Fan,X.S., Cai,L., Liu,S., Cong,X.F. and Chen,X.
  TITLE     Lysophosphatidic acid rescues bone mesenchymal stem cells from
            hydrogen peroxide-induced apoptosis
  JOURNAL   Apoptosis 20 (3), 273-284 (2015)
   PUBMED   25633408
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Moller,D., Kling,R.C., Skultety,M., Leuner,K., Hubner,H. and
            Gmeiner,P.
  TITLE     Functionally selective dopamine D, D receptor partial agonists
  JOURNAL   J Med Chem 57 (11), 4861-4875 (2014)
   PUBMED   24831693
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Lerman,B.B., Dong,B., Stein,K.M., Markowitz,S.M., Linden,J. and
            Catanzaro,D.F.
  TITLE     Right ventricular outflow tract tachycardia due to a somatic cell
            mutation in G protein subunitalphai2
  JOURNAL   J Clin Invest 101 (12), 2862-2868 (1998)
   PUBMED   9637720
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Rudolph,U., Spicher,K. and Birnbaumer,L.
  TITLE     Adenylyl cyclase inhibition and altered G protein subunit
            expression and ADP-ribosylation patterns in tissues and cells from
            Gi2 alpha-/-mice
  JOURNAL   Proc Natl Acad Sci U S A 93 (8), 3209-3214 (1996)
   PUBMED   8622915
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Linder,M.E., Ewald,D.A., Miller,R.J. and Gilman,A.G.
  TITLE     Purification and characterization of Go alpha and three types of Gi
            alpha after expression in Escherichia coli
  JOURNAL   J Biol Chem 265 (14), 8243-8251 (1990)
   PUBMED   2159473
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Molecular cloning of five GTP-binding protein cDNA species from rat
            olfactory neuroepithelium
  JOURNAL   J Biol Chem 262 (29), 14241-14249 (1987)
   PUBMED   2820999
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Itoh,H., Kozasa,T., Nagata,S., Nakamura,S., Katada,T., Ui,M.,
            Iwai,S., Ohtsuka,E., Kawasaki,H., Suzuki,K. et al.
  TITLE     Molecular cloning and sequence determination of cDNAs for alpha
            subunits of the guanine nucleotide-binding proteins Gs, Gi, and Go
            from rat brain
  JOURNAL   Proc Natl Acad Sci U S A 83 (11), 3776-3780 (1986)
   PUBMED   3086867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO394955.1, BC078806.1 and CR465951.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078806.1, M17528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..355
                     /product="guanine nucleotide-binding protein G(i) subunit
                     alpha-2"
                     /note="guanine nucleotide-binding protein G(i), alpha-2
                     subunit; G alpha inhibitory type 2 (a); G alpha inhibitory
                     type 2 (b); adenylate cyclase-inhibiting G alpha protein;
                     GTP-binding protein (G-alpha-i2); guanine nucleotide
                     binding protein, alpha inhibiting 2; guanine nucleotide
                     binding protein (G protein), alpha inhibiting 2; guanine
                     nucleotide binding protein (G protein), alpha inhibiting
                     activity polypeptide 2; heterotrimeric guanine
                     nucleotide-binding protein 1c"
                     /calculated_mol_wt=40368
     Region          34..349
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          35..48
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04897.3)"
     Site            order(40,45..47,182,201,204,270..271,273,326..327)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            40..47
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(41..43,71,75,79,82,85..86,104,107,150,179,204,212,
                     216)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          174..182
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04897.3)"
     Site            177..185
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            182
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(183,185,187,198,200,204..206,208,211..212,214..217)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(185,210,213..214,217)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          197..206
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04897.3)"
     Site            201..204
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            202..218
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          266..273
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04897.3)"
     Site            270..273
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(318..329,331..334)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          325..330
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P04897.3)"
     Site            326..328
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..355
                     /gene="Gnai2"
                     /gene_synonym="Galphai2; Hg1c"
                     /coded_by="NM_031035.3:153..1220"
                     /db_xref="GeneID:81664"
                     /db_xref="RGD:620243"
ORIGIN      
        1 mgctvsaedk aaaerskmid knlredgeka arevkllllg agesgkstiv kqmkiihedg
       61 yseeecrqyr avvysntiqs imaivkamgn lqidfadpqr addarqlfal scaaeeqgml
      121 pedlsgvirr lwadhgvqac fgrsreyqln dsaayylndl eriaqsdyip tqqdvlrtrv
      181 kttgivethf tfkdlhfkmf dvggqrserk kwihcfegvt aiifcvalsa ydlvlaedee
      241 mnrmhesmkl fdsicnnkwf tdtsiilfln kkdlfeekit qsplticfpe ytgankydea
      301 asyiqskfed lnkrkdtkei ythftcatdt knvqfvfdav tdviiknnlk dcglf
//
LOCUS       NP_001020196             415 aa            linear   ROD 27-APR-2025
DEFINITION  dynein assembly factor with WD repeat domains 1 [Rattus
            norvegicus].
ACCESSION   NP_001020196 XP_343610
VERSION     NP_001020196.1
DBSOURCE    REFSEQ: accession NM_001025025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Solomon,G.M., Francis,R., Chu,K.K., Birket,S.E., Gabriel,G.,
            Trombley,J.E., Lemke,K.L., Klena,N., Turner,B., Tearney,G.J.,
            Lo,C.W. and Rowe,S.M.
  TITLE     Assessment of ciliary phenotype in primary ciliary dyskinesia by
            micro-optical coherence tomography
  JOURNAL   JCI Insight 2 (5), e91702 (2017)
   PUBMED   28289722
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Li,Y., Klena,N.T., Gabriel,G.C., Liu,X., Kim,A.J., Lemke,K.,
            Chen,Y., Chatterjee,B., Devine,W., Damerla,R.R., Chang,C., Yagi,H.,
            San Agustin,J.T., Thahir,M., Anderton,S., Lawhead,C., Vescovi,A.,
            Pratt,H., Morgan,J., Haynes,L., Smith,C.L., Eppig,J.T.,
            Reinholdt,L., Francis,R., Leatherbury,L., Ganapathiraju,M.K.,
            Tobita,K., Pazour,G.J. and Lo,C.W.
  TITLE     Global genetic analysis in mice unveils central role for cilia in
            congenital heart disease
  JOURNAL   Nature 521 (7553), 520-524 (2015)
   PUBMED   25807483
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091226.1.
            
            On Jun 25, 2005 this sequence version replaced XP_343610.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091226.1, BC079402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..415
                     /product="dynein assembly factor with WD repeat domains 1"
                     /note="WD repeat-containing protein 69; outer row dynein
                     assembly protein 16 homolog; dynein assembly factor with
                     WDR repeat domains 1"
                     /calculated_mol_wt=45728
     Region          87..415
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          90..129
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          96..132
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..174
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          137..175
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          175..214
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          181..217
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          217..256
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          222..258
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          259..298
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          265..300
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          301..340
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          306..342
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          343..384
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          348..384
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          386..415
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK30.1)"
     Region          390..414
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..415
                     /gene="Daw1"
                     /gene_synonym="Wdr69"
                     /coded_by="NM_001025025.1:36..1283"
                     /db_xref="GeneID:363267"
                     /db_xref="RGD:1561436"
ORIGIN      
        1 mklkslllry yppgimleye kggelktksi dllelspstd vntlvgeiqk veplitasrt
       61 kqvrllvqrl qeklrqhcdh nfylfkvlra hilpltnval nkagscfitg sydrtckvwd
      121 tasgeelhtl eghrnvvyai afnnpygdki atgsfdktck lwsaetgkcy htfrghtaei
      181 vclsfnpqst vvatgsmdtt aklwdiqsge evvtltghla eiislsfdts gdriitgsfd
      241 htvvvwdast grkvhtligh caeissalfs wdcsliltgs mdktcmlwda tsgkcvatlt
      301 ghddeildsc fdytgkliat asadgtarvy nattrkcitk leghegeisk isfnpqgnrl
      361 ltgssdktar iwdvqtgqcl qvleghtdei fscafnykgn ivitgskdns criwr
//
LOCUS       NP_071634                451 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin alpha-1A chain [Rattus norvegicus].
ACCESSION   NP_071634 XP_217040
VERSION     NP_071634.1
DBSOURCE    REFSEQ: accession NM_022298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Renguet,E., De Loof,M., Fourny,N., Ginion,A., Bouzin,C., Pous,C.,
            Horman,S., Beauloye,C., Bultot,L. and Bertrand,L.
  TITLE     alpha-Tubulin acetylation on lysine 40 controls cardiac glucose
            uptake
  JOURNAL   Am J Physiol Heart Circ Physiol 322 (6), H1032-H1043 (2022)
   PUBMED   35486479
  REMARK    GeneRIF: alpha-Tubulin acetylation on lysine 40 controls cardiac
            glucose uptake.
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Yang,L., Zhao,L., Cui,L., Huang,Y., Ye,J., Zhang,Q., Jiang,X.,
            Zhang,D. and Huang,Y.
  TITLE     Decreased alpha-tubulin acetylation induced by an acidic
            environment impairs autophagosome formation and leads to rat
            cardiomyocyte injury
  JOURNAL   J Mol Cell Cardiol 127, 143-153 (2019)
   PUBMED   30582931
  REMARK    GeneRIF: HDAC6-mediated alpha-tubulin acetylation is an important
            mechanism of acidic pH-dependent autophagy in cardiomyocytes.
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Shin,S., Lim,S., Jeong,H., Kwan,L.T. and Kim,Y.K.
  TITLE     Visualization of TauTubulin Interaction in a Living Cell Using
            Bifluorescence Complementation Technique
  JOURNAL   Int J Mol Sci 19 (10), 2978 (2018)
   PUBMED   30274285
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Nakakura,T., Nemoto,T., Suzuki,T., Asano-Hoshino,A., Tanaka,H.,
            Arisawa,K., Nishijima,Y., Kiuchi,Y. and Hagiwara,H.
  TITLE     Adrenalectomy facilitates ATAT1 expression and alpha-tubulin
            acetylation in ACTH-producing corticotrophs
  JOURNAL   Cell Tissue Res 366 (2), 363-370 (2016)
   PUBMED   27314403
  REMARK    GeneRIF: These results agree with the hypothesis that the
            acetylation of alpha-tubulin by ATAT1 regulates the intracellular
            transport of secretory granules in corticotrophs.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Best,A., Ahmed,S., Kozma,R. and Lim,L.
  TITLE     The Ras-related GTPase Rac1 binds tubulin
  JOURNAL   J Biol Chem 271 (7), 3756-3762 (1996)
   PUBMED   8631991
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Ginzburg,I., Teichman,A., Griffin,W.S. and Littauer,U.Z.
  TITLE     Differential expression of alpha-tubulin mRNA in rat cerebellum as
            revealed by in situ hybridization
  JOURNAL   FEBS Lett 194 (1), 161-164 (1986)
   PUBMED   3753592
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Lemischka,I. and Sharp,P.A.
  TITLE     The sequences of an expressed rat alpha-tubulin gene and a
            pseudogene with an inserted repetitive element
  JOURNAL   Nature 300 (5890), 330-335 (1982)
   PUBMED   6927856
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Lemischka,I.R., Farmer,S., Racaniello,V.R. and Sharp,P.A.
  TITLE     Nucleotide sequence and evolution of a mammalian alpha-tubulin
            messenger RNA
  JOURNAL   J Mol Biol 151 (1), 101-120 (1981)
   PUBMED   7328649
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Ginzburg,I., Behar,L., Givol,D. and Littauer,U.Z.
  TITLE     The nucleotide sequence of rat alpha-tubulin: 3'-end
            characteristics, and evolutionary conservation
  JOURNAL   Nucleic Acids Res 9 (12), 2691-2697 (1981)
   PUBMED   6269058
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from V01227.1.
            
            On Jan 12, 2005 this sequence version replaced XP_217040.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: V01227.1, BC078830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132299, SAMD00132300
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..451
                     /product="tubulin alpha-1A chain"
                     /note="alpha-tubulin 1; tubulin alpha-1 chain; tubulin,
                     alpha 1"
                     /calculated_mol_wt=50005
     Region          1..440
                     /region_name="PTZ00335"
                     /note="tubulin alpha chain; Provisional"
                     /db_xref="CDD:185562"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q71U36; propagated from
                     UniProtKB/Swiss-Prot (P68370.1)"
     Region          432..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P68370.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68373; propagated from
                     UniProtKB/Swiss-Prot (P68370.1)"
     Site            451
                     /site_type="other"
                     /note="Involved in polymerization; propagated from
                     UniProtKB/Swiss-Prot (P68370.1)"
     CDS             1..451
                     /gene="Tuba1a"
                     /gene_synonym="Tuba1"
                     /coded_by="NM_022298.1:67..1422"
                     /db_xref="GeneID:64158"
                     /db_xref="RGD:619717"
ORIGIN      
        1 mrecisihvg qagvqignac welyclehgi qpdgqmpsdk tigggddsfn tffsetgagk
       61 hvpravfvdl eptvidevrt gtyrqlfhpe qlitgkedaa nnyarghyti gkeiidlvld
      121 rirkladqct glqgflvfhs fgggtgsgft sllmerlsvd ygkksklefs iypapqvsta
      181 vvepynsilt thttlehsdc afmvdneaiy dicrrnldie rptytnlnrl igqivssita
      241 slrfdgalnv dltefqtnlv pyprihfpla tyapvisaek ayheqlsvae itnacfepan
      301 qmvkcdprhg kymaccllyr gdvvpkdvna aiatiktkrt iqfvdwcptg fkvginyqpp
      361 tvvpggdlak vqravcmlsn ttaiaeawar ldhkfdlmya krafvhwyvg egmeegefse
      421 aredmaalek dyeevgvdsv egegeeegee y
//
LOCUS       NP_569097                358 aa            linear   ROD 27-APR-2025
DEFINITION  src kinase-associated phosphoprotein 2 [Rattus norvegicus].
ACCESSION   NP_569097
VERSION     NP_569097.1
DBSOURCE    REFSEQ: accession NM_130413.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Kirchgessner,H., Dietrich,J., Scherer,J., Isomaki,P., Korinek,V.,
            Hilgert,I., Bruyns,E., Leo,A., Cope,A.P. and Schraven,B.
  TITLE     The transmembrane adaptor protein TRIM regulates T cell receptor
            (TCR) expression and TCR-mediated signaling via an association with
            the TCR zeta chain
  JOURNAL   J Exp Med 193 (11), 1269-1284 (2001)
   PUBMED   11390434
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Curtis,D.J., Jane,S.M., Hilton,D.J., Dougherty,L., Bodine,D.M. and
            Begley,C.G.
  TITLE     Adaptor protein SKAP55R is associated with myeloid differentiation
            and growth arrest
  JOURNAL   Exp Hematol 28 (11), 1250-1259 (2000)
   PUBMED   11063873
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF302132.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF302132.1, BC070949.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..358
                     /product="src kinase-associated phosphoprotein 2"
                     /note="Src kinase-associated phosphoprotein;
                     Fyn-associated protein; adaptor protein; SKAP-HOM;
                     SKAP-55HOM; SKAP55-HOM; SKAP55 homolog; src
                     family-associated phosphoprotein 2; src kinase-associated
                     phosphoprotein 55-related protein"
                     /calculated_mol_wt=40586
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Region          60..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75563; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Region          117..222
                     /region_name="PH_Skap-hom_Skap2"
                     /note="Src kinase-associated phosphoprotein homolog and
                     Skap 2 Pleckstrin homology (PH) domain; cd13381"
                     /db_xref="CDD:270181"
     Site            order(125,127,131,138,140,151,195,197)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270181"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3UND0; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75563; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Region          227..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3UND0; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G0.1)"
     Region          300..352
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(305,307,310,314,334..335,348,350..351)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     CDS             1..358
                     /gene="Skap2"
                     /gene_synonym="Scap2; Scap55r"
                     /coded_by="NM_130413.1:133..1209"
                     /db_xref="GeneID:155183"
                     /db_xref="RGD:620159"
ORIGIN      
        1 mpnpgstssp gsipeeirnl ladvetfvad tlkgenlskk akekrdslik kikdvksvyp
       61 qefqdkgdae egdeyddpfa gppdtislas erydkdddgp sdgnqfppia aqdlsfvika
      121 gylekrrkdh sflgfewqkr wcalsktvfy yygsdkdkqq kgefaiegyd vrmnntlrkd
      181 akkdccfeic apdkriyqft aaspkdaeew vqqlkfilqd mgsdvipede dekgdlyddv
      241 dhpvpvsspq rsqpiddeiy eelpeeeedt asvkmdeqgk gsrdsvqhps gdkstdyanf
      301 yqglwdctgs lsdelsfkrg dviyilskey nrygwwvgem qgaiglvpka ylmemydi
//
LOCUS       NP_001013203             649 aa            linear   ROD 27-APR-2025
DEFINITION  atypical kinase COQ8A, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001013203 XP_341163
VERSION     NP_001013203.1
DBSOURCE    REFSEQ: accession NM_001013185.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Stefely,J.A., Licitra,F., Laredj,L., Reidenbach,A.G.,
            Kemmerer,Z.A., Grangeray,A., Jaeg-Ehret,T., Minogue,C.E.,
            Ulbrich,A., Hutchins,P.D., Wilkerson,E.M., Ruan,Z., Aydin,D.,
            Hebert,A.S., Guo,X., Freiberger,E.C., Reutenauer,L., Jochem,A.,
            Chergova,M., Johnson,I.E., Lohman,D.C., Rush,M.J.P., Kwiecien,N.W.,
            Singh,P.K., Schlagowski,A.I., Floyd,B.J., Forsman,U.,
            Sindelar,P.J., Westphall,M.S., Pierrel,F., Zoll,J., Dal Peraro,M.,
            Kannan,N., Bingman,C.A., Coon,J.J., Isope,P., Puccio,H. and
            Pagliarini,D.J.
  TITLE     Cerebellar Ataxia and Coenzyme Q Deficiency through Loss of
            Unorthodox Kinase Activity
  JOURNAL   Mol Cell 63 (4), 608-620 (2016)
   PUBMED   27499294
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Stefely,J.A., Reidenbach,A.G., Ulbrich,A., Oruganty,K., Floyd,B.J.,
            Jochem,A., Saunders,J.M., Johnson,I.E., Minogue,C.E., Wrobel,R.L.,
            Barber,G.E., Lee,D., Li,S., Kannan,N., Coon,J.J., Bingman,C.A. and
            Pagliarini,D.J.
  TITLE     Mitochondrial ADCK3 employs an atypical protein kinase-like fold to
            enable coenzyme Q biosynthesis
  JOURNAL   Mol Cell 57 (1), 83-94 (2015)
   PUBMED   25498144
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Gerards,M., van den Bosch,B., Calis,C., Schoonderwoerd,K., van
            Engelen,K., Tijssen,M., de Coo,R., van der Kooi,A. and Smeets,H.
  TITLE     Nonsense mutations in CABC1/ADCK3 cause progressive cerebellar
            ataxia and atrophy
  JOURNAL   Mitochondrion 10 (5), 510-515 (2010)
   PUBMED   20580948
  REMARK    GeneRIF: These results indicate that CABC1 is an important
            candidate for mutation analysis in progressive cerebellar ataxia
            and atrophy on MRI to identify those patients who may benefit from
            CoQ10 treatment.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091388.1.
            
            On Apr 20, 2005 this sequence version replaced XP_341163.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..649
                     /product="atypical kinase COQ8A, mitochondrial"
                     /note="chaperone activity of bc1 complex-like,
                     mitochondrial; aarF domain-containing protein kinase 3;
                     chaperone, ABC1 activity of bc1 complex like; atypical
                     kinase ADCK3, mitochondrial; aarF domain containing kinase
                     3; coenzyme Q protein 8A"
                     /calculated_mol_wt=55037
     transit_peptide 1..163
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q8NI60; propagated from
                     UniProtKB/Swiss-Prot (Q5BJQ0.1)"
                     /calculated_mol_wt=17207
     Region          84..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
     mat_peptide     164..649
                     /product="Atypical kinase COQ8A, mitochondrial.
                     /id=PRO_0000271795"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
                     /calculated_mol_wt=55037
     Region          183..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
     Site            215..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
     Region          277..280
                     /region_name="KxGQ motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NI60"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
     Region          296..546
                     /region_name="ABC1_ADCK3"
                     /note="Activator of bc1 complex (ABC1) kinases, also
                     called aarF domain containing kinase 3; cd13970"
                     /db_xref="CDD:270872"
     Region          338..341
                     /region_name="AAAS motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NI60"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJQ0.1)"
     Site            order(350..354,356,366,368,427,446..449,489,493..494,496,
                     507..508)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
     CDS             1..649
                     /gene="Coq8a"
                     /gene_synonym="Adck3; Cabc1"
                     /coded_by="NM_001013185.1:37..1986"
                     /db_xref="GeneID:360887"
                     /db_xref="RGD:1308245"
ORIGIN      
        1 maamlgdaim vakglakltq aavethlqnl glggelilaa ralqstaveq ismvfgkvqg
       61 qdkhedsyat enfedleaev qfstpqaags spdfstassl dqplssslgh ahregpapay
      121 vssgpfreag lsgqatsplg rvngrlfvdc rdlflansiq rrffhqdqap vggltaedie
      181 karqakarpe skphkqmlse rarerkvpvt rigrlanfgg lavglgfgal aevakkslrs
      241 enstgkkavl dsspflsean aerivstlck vrgaalklgq mlsiqddafi nphlakifer
      301 vrqsadfmpl kqmtktlnnd lgphwrdkle yfeerpfaaa sigqvhlarl kggrevamki
      361 qypgvaqsin sdvnnlmavl nmsnmlpegl fpehlidvlr reltlecdyq reaayakkfr
      421 ellkdhpffy vpeivdelcs phvlttelit gfpldqaegl sqevrneicy nilvlclrel
      481 fefhvmqtdp nwsnffydpq qhkvalldfg atreydrsft dlyiqviraa adqdreavlk
      541 ksiemkfltg yevkamedah ldaililgea faseepfdfg tqsttekihn lipimlkhrl
      601 ipppeetysl hrkmggsfli csklkacfpc kamfeeaysn ycrmksglq
//
LOCUS       NP_001032857             343 aa            linear   ROD 27-APR-2025
DEFINITION  N-acetyl-D-glucosamine kinase [Rattus norvegicus].
ACCESSION   NP_001032857 XP_216188
VERSION     NP_001032857.1
DBSOURCE    REFSEQ: accession NM_001037768.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Islam,M.A., Sharif,S.R., Lee,H. and Moon,I.S.
  TITLE     N-Acetyl-D-Glucosamine Kinase Promotes the Axonal Growth of
            Developing Neurons
  JOURNAL   Mol Cells 38 (10), 876-885 (2015)
   PUBMED   26467288
  REMARK    GeneRIF: this work studied the role played by NAGK in axonal
            development.
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Islam,M.A., Sharif,S.R., Lee,H., Seog,D.H. and Moon,I.S.
  TITLE     N-acetyl-D-glucosamine kinase interacts with dynein light-chain
            roadblock type 1 at Golgi outposts in neuronal dendritic branch
            points
  JOURNAL   Exp Mol Med 47 (8), e177 (2015)
   PUBMED   26272270
  REMARK    GeneRIF: The interaction between NAGK and Dynlrb1 frequently occurs
            at dendritic branch points.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Sharif,S.R., Lee,H., Islam,M.A., Seog,D.H. and Moon,I.S.
  TITLE     N-acetyl-D-glucosamine kinase is a component of nuclear speckles
            and paraspeckles
  JOURNAL   Mol Cells 38 (5), 402-408 (2015)
   PUBMED   25921606
  REMARK    GeneRIF: Data shows associations between NAGK, speckle, paraspeckle
            and general transcription factor suggesting its regulatory roles in
            gene expression.
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Lee,H., Cho,S.J. and Moon,I.S.
  TITLE     The non-canonical effect of N-acetyl-D-glucosamine kinase on the
            formation of neuronal dendrites
  JOURNAL   Mol Cells 37 (3), 248-256 (2014)
   PUBMED   24625575
  REMARK    GeneRIF: Upregulation of dendritic complexity is a non-canonical
            function of NAGK.
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Bergfeld,A.K., Pearce,O.M., Diaz,S.L., Pham,T. and Varki,A.
  TITLE     Metabolism of vertebrate amino sugars with N-glycolyl groups:
            elucidating the intracellular fate of the non-human sialic acid
            N-glycolylneuraminic acid
  JOURNAL   J Biol Chem 287 (34), 28865-28881 (2012)
   PUBMED   22692205
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Ghaderi,D., Strauss,H.M., Reinke,S., Cirak,S., Reutter,W., Lucka,L.
            and Hinderlich,S.
  TITLE     Evidence for dynamic interplay of different oligomeric states of
            UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase by
            biophysical methods
  JOURNAL   J Mol Biol 369 (3), 746-758 (2007)
   PUBMED   17448495
  REMARK    GeneRIF: analysis of oligomeric states of UDP-N-acetylglucosamine
            2-epimerase/N-acetylmannosamine kinase by biophysical methods
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Hinderlich,S., Berger,M., Schwarzkopf,M., Effertz,K. and Reutter,W.
  TITLE     Molecular cloning and characterization of murine and human
            N-acetylglucosamine kinase
  JOURNAL   Eur J Biochem 267 (11), 3301-3308 (2000)
   PUBMED   10824116
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Hinderlich,S., Nohring,S., Weise,C., Franke,P., Stasche,R. and
            Reutter,W.
  TITLE     Purification and characterization of N-acetylglucosamine kinase
            from rat liver--comparison with UDP-N-acetylglucosamine
            2-epimerase/N-acetylmannosamine kinase
  JOURNAL   Eur J Biochem 252 (1), 133-139 (1998)
   PUBMED   9523722
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107647.1.
            
            On Dec 16, 2005 this sequence version replaced XP_216188.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107647.1, SRR8487231.87796.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..343
                     /product="N-acetyl-D-glucosamine kinase"
                     /EC_number="2.7.1.60"
                     /EC_number="2.7.1.59"
                     /note="glcNAc kinase; muramyl dipeptide kinase;
                     N-acetyl-D-mannosamine kinase"
                     /calculated_mol_wt=37065
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:9523722; propagated from
                     UniProtKB/Swiss-Prot (P81799.4)"
     Region          4..322
                     /region_name="ASKHA_NBD_NAGK_meta"
                     /note="nucleotide-binding domain (NBD) of
                     N-acetyl-D-glucosamine kinase (NAGK) and similar proteins;
                     cd24078"
                     /db_xref="CDD:466928"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P81799.4)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UJ70; propagated from
                     UniProtKB/Swiss-Prot (P81799.4)"
     CDS             1..343
                     /gene="Nagk"
                     /coded_by="NM_001037768.1:38..1069"
                     /db_xref="GeneID:297393"
                     /db_xref="RGD:1305057"
ORIGIN      
        1 maalyggveg ggtrskvlll sedgqilaea dglstnhwli gtgtcverin emvdrakrka
       61 gvdplvplrs lglslsggeq edavrllmee lrdrfpylse syfittdaag siatatpdgg
      121 ivlisgtgsn crlinpdgse sgcggwghmm gdegsaywia hqavkivfds idnleaaphd
      181 ighvkqamfn yfqvpdrlgi lthlyrdfdk skfagfcqki aegaqqgdpl srfifrkage
      241 mlgrhvvavl peidpvlfqg elglpilcvg svwkswellk egfllaltqg reqqaqnsfs
      301 sftlmklrhs salggaslga rhighhlpmd ysvnaiafys ytf
//
LOCUS       NP_446401               1163 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated inwardly rectifying potassium channel KCNH2 [Rattus
            norvegicus].
ACCESSION   NP_446401
VERSION     NP_446401.1
DBSOURCE    REFSEQ: accession NM_053949.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Hu,S., Li,Z., Liu,H., Cao,W., Meng,Y., Liu,C., He,S., Lin,Q.,
            Shang,M., Lin,F., Yi,N., Wang,H., Sachinidis,A., Ying,Q., Li,L. and
            Peng,L.
  TITLE     Kcnh2 deletion is associated with rat embryonic development defects
            via destruction of KCNH2-integrin beta1 complex
  JOURNAL   Int J Mol Med 53 (2) (2024)
   PUBMED   38063256
  REMARK    GeneRIF: Kcnh2 deletion is associated with rat embryonic
            development defects via destruction of KCNH2-integrin beta1
            complex.
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Xu,W., Dahlke,S.P., Sung,M., Samal,B., Emery,A.C., Elkahloun,A. and
            Eiden,L.E.
  TITLE     ERK-dependent induction of the immediate-early gene Egr1 and the
            late gene Gpr50 contribute to two distinct phases of PACAP Gs-GPCR
            signaling for neuritogenesis
  JOURNAL   J Neuroendocrinol 34 (9), e13182 (2022)
   PUBMED   35841324
  REMARK    GeneRIF: ERK-dependent induction of the immediate-early gene Egr1
            and the late gene Gpr50 contribute to two distinct phases of PACAP
            Gs-GPCR signaling for neuritogenesis.
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Wang,D., Liu,C., Liu,H., Meng,Y., Lin,F., Gu,Y., Wang,H., Shang,M.,
            Tong,C., Sachinidis,A., Ying,Q., Li,L. and Peng,L.
  TITLE     ERG1 plays an essential role in rat cardiomyocyte fate decision by
            mediating AKT signaling
  JOURNAL   Stem Cells 39 (4), 443-457 (2021)
   PUBMED   33426760
  REMARK    GeneRIF: ERG1 plays an essential role in rat cardiomyocyte fate
            decision by mediating AKT signaling.
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Li,Z., Meng,Y., Liu,C., Liu,H., Cao,W., Tong,C., Lu,M., Li,L. and
            Peng,L.
  TITLE     Kcnh2 mediates FAK/AKT-FOXO3A pathway to attenuate sepsis-induced
            cardiac dysfunction
  JOURNAL   Cell Prolif 54 (2), e12962 (2021)
   PUBMED   33263944
  REMARK    GeneRIF: Kcnh2 mediates FAK/AKT-FOXO3A pathway to attenuate
            sepsis-induced cardiac dysfunction.
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Hajimirzaei,N., Khalili,N.P., Boroumand,B., Safari,F.,
            Pourhosseini,A., Judi-Chelan,R. and Tavakoli,F.
  TITLE     Comparative Study of the Effect of Macrolide Antibiotics
            Erythromycin, Clarithromycin, and Azithromycin on the ERG1 Gene
            Expression in H9c2 Cardiomyoblast Cells
  JOURNAL   Drug Res (Stuttg) 70 (8), 341-347 (2020)
   PUBMED   32559772
  REMARK    GeneRIF: Comparative Study of the Effect of Macrolide Antibiotics
            Erythromycin, Clarithromycin, and Azithromycin on the ERG1 Gene
            Expression in H9c2 Cardiomyoblast Cells.
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   Li,X., Xu,J. and Li,M.
  TITLE     The human delta1261 mutation of the HERG potassium channel results
            in a truncated protein that contains a subunit interaction domain
            and decreases the channel expression
  JOURNAL   J Biol Chem 272 (2), 705-708 (1997)
   PUBMED   8995352
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   Smith,P.L., Baukrowitz,T. and Yellen,G.
  TITLE     The inward rectification mechanism of the HERG cardiac potassium
            channel
  JOURNAL   Nature 379 (6568), 833-836 (1996)
   PUBMED   8587608
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Trudeau,M.C., Warmke,J.W., Ganetzky,B. and Robertson,G.A.
  TITLE     HERG, a human inward rectifier in the voltage-gated potassium
            channel family
  JOURNAL   Science 269 (5220), 92-95 (1995)
   PUBMED   7604285
  REMARK    Erratum:[Science. 1996 May 24;272(5265):1087. PMID: 8638148]
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   Sanguinetti,M.C., Jiang,C., Curran,M.E. and Keating,M.T.
  TITLE     A mechanistic link between an inherited and an acquired cardiac
            arrhythmia: HERG encodes the IKr potassium channel
  JOURNAL   Cell 81 (2), 299-307 (1995)
   PUBMED   7736582
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Curran,M.E., Splawski,I., Timothy,K.W., Vincent,G.M., Green,E.D.
            and Keating,M.T.
  TITLE     A molecular basis for cardiac arrhythmia: HERG mutations cause long
            QT syndrome
  JOURNAL   Cell 80 (5), 795-803 (1995)
   PUBMED   7889573
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Z96106.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z96106.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..1163
                     /product="voltage-gated inwardly rectifying potassium
                     channel KCNH2"
                     /note="RERG; r-ERG; eag-related protein 1;
                     ether-a-go-go-related protein 1; ether-a-go-go-related
                     gene potassium channel 1; voltage-gated potassium channel
                     subunit Kv11.1; potassium channel, voltage gated eag
                     related subfamily H, member 2; ERG-1; potassium
                     voltage-gated channel, subfamily H (eag-related), member
                     2"
                     /calculated_mol_wt=126821
     Region          38..130
                     /region_name="PAS_9"
                     /note="PAS domain; pfam13426"
                     /db_xref="CDD:463873"
     Region          235..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12809; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35219; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12809; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            406..426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Region          411..670
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            453..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            498..518
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            523..543
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            550..570
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Region          626..631
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:Q63472"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            641..661
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Region          744..855
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Region          744..844
                     /region_name="cNMP-binding domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00060"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            order(808..809,820..822)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(842..844,848..850)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          873..992
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            873
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12809; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35219; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Region          1015..1043
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            1018
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35219; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     Region          1126..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08962.1)"
     Site            1141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12809; propagated from
                     UniProtKB/Swiss-Prot (O08962.1)"
     CDS             1..1163
                     /gene="Kcnh2"
                     /gene_synonym="ERG1"
                     /coded_by="NM_053949.1:1..3492"
                     /db_xref="GeneID:117018"
                     /db_xref="RGD:621414"
ORIGIN      
        1 mpvrrghvap qntfldtiir kfegqsrkfi ianarvenca viycndgfce lcgysraevm
       61 qrpctcdflh gprtqrraaa qiaqallgae erkveiafyr kdgscflclv dvvpvknedg
      121 avimfilnfe vvmekdmvgs pahdtnhrgp stswlasgra ktfrlklpal laltarespm
      181 rtgstgspga pgavvvdvdl tpaapssesl aldevsamdn hvaglgpaee rralvgpasa
      241 spvasipgph pspraqslnp dasgsscsla rtrsrescas vrrassaddi eamragalpl
      301 pprhastgam hplrsgllns tsdsdlvryr tiskipqitl nfvdlkgdpf lasptsdrei
      361 iapkikerth nvtekvtqvl slgadvlpey klqaprihrw tilhyspfka vwdwlilllv
      421 iytavftpys aafllketed gsqapdcgya cqplavvdll vdimfivdil infrttyvna
      481 neevvshpgr iavhyfkgwf lidmvaaipf dllifgsgse eligllktar llrlvrvark
      541 ldryseygaa vlfllmctfa liahwlaciw yaignmeqph mdshigwlhn lgdqigkpyn
      601 ssglggpsik dkyvtalyft fssltsvgfg nvspntnsek ifsicvmlig slmyasifgn
      661 vsaiiqrlys gtaryhtqml rvrefirfhq ipnplrqrle eyfqhawsyt ngidmnavlk
      721 gfpeclqadi clhlnrsllq hckpfrgatk gclralamkf ktthappgdt lvhagdllta
      781 lyfisrgsie ilrgdvvvai lgkndifgep lnlyarpgks ngdvraltyc dlhkihrddl
      841 levldmypef sdhfwsslei tfnlrdtnmi pgspssaele sgfnrqrkrk lsfrrrtdkd
      901 teqpgevsal gqgparvgpg pscrgqpggp wgespssgps spessedegp grsssplrlv
      961 pfssprppgd spggeplted gekssdtcnp lsgafsgvsn ifsfwgdsrg rqyqelprcp
     1021 apapsllnip lsspgrrsrg dvesrldalq rqlnrletrl sadmatvlql lqrqmtlvpp
     1081 aysavttpgp gptstspllp vgpvptltld slsqvsqfva feelpagape lpqdgptrrl
     1141 slpgqlgalt sqplhrhgsd pgs
//
LOCUS       NP_001014061             184 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor alpha-induced protein 8-like protein 2
            [Rattus norvegicus].
ACCESSION   NP_001014061 XP_227431
VERSION     NP_001014061.1
DBSOURCE    REFSEQ: accession NM_001014039.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   DU,Y., Liu,X., Xiao,C., Li,J., Sheng,Z., Wang,Y., Wang,R. and Yu,X.
  TITLE     TIPE2 regulates periodontal inflammation by inhibiting NF-kappaB
            p65 phosphorylation
  JOURNAL   J Appl Oral Sci 31, e20230162 (2023)
   PUBMED   37493703
  REMARK    GeneRIF: TIPE2 regulates periodontal inflammation by inhibiting
            NF-kappaB p65 phosphorylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Sun,X., Li,X., Zhou,Y., Wang,Y. and Liu,X.
  TITLE     Exogenous TIPE2 Inhibit TAK1 to Improve Inflammation and
            Neuropathic Pain Induced by Sciatic Nerve Injury Through
            Inactivating NF-kappaB and JNK
  JOURNAL   Neurochem Res 47 (10), 3167-3177 (2022)
   PUBMED   35842555
  REMARK    GeneRIF: Exogenous TIPE2 Inhibit TAK1 to Improve Inflammation and
            Neuropathic Pain Induced by Sciatic Nerve Injury Through
            Inactivating NF-kappaB and JNK.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kong,Q., Yuan,M., Ming,T., Fang,Q., Wu,X. and Song,X.
  TITLE     Expression and regulation of tumor necrosis factor-alpha-induced
            protein-8-like 2 is associated with acute lung injury induced by
            myocardial ischemia reperfusion in diabetic rats
  JOURNAL   Microvasc Res 130, 104009 (2020)
   PUBMED   32333940
  REMARK    GeneRIF: Expression and regulation of tumor necrosis
            factor-alpha-induced protein-8-like 2 is associated with acute lung
            injury induced by myocardial ischemia reperfusion in diabetic rats.
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Shi,C., Wang,Y., Zhuang,G., Qi,Z., Li,Y. and Yin,P.
  TITLE     Tumor necrosis factor-alpha-induced protein-8 like 2 regulates
            lipopolysaccharide-induced rat rheumatoid arthritis immune
            responses and is associated with Rac activation and interferon
            regulatory factor 3 phosphorylation
  JOURNAL   Mol Med Rep 16 (5), 6346-6353 (2017)
   PUBMED   28849230
  REMARK    GeneRIF: TIPE2 regulates lipopolysaccharide-induced rat rheumatoid
            arthritis immune responses and is associated with Rac1 activation
            and IRF3 phosphorylation.
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Liu,M.W., Liu,R., Wu,H.Y., Zhang,W., Xia,J., Dong,M.N., Yu,W.,
            Wang,Q., Xie,F.M., Wang,R., Huang,Y.Q. and Qian,C.Y.
  TITLE     Protective effect of Xuebijing injection on D-galactosamine- and
            lipopolysaccharide-induced acute liver injury in rats through the
            regulation of p38 MAPK, MMP-9 and HO-1 expression by increasing
            TIPE2 expression
  JOURNAL   Int J Mol Med 38 (5), 1419-1432 (2016)
   PUBMED   27666960
  REMARK    GeneRIF: Expression of tumor necrosis factor (TNF)alphainduced
            protein 8-like 2 (TIPE2), matrix metalloproteinase-9 (MMP-9) and
            heme oxygenase-1 (HO-1) and mitogen-activated protein kinase (MAPK)
            signaling was modulated by Xuebijing injection (XBJ).
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Luan,Y.Y., Yao,Y.M., Zhang,L., Dong,N., Zhang,Q.H., Yu,Y. and
            Sheng,Z.Y.
  TITLE     Expression of tumor necrosis factor-alpha induced protein 8 like-2
            contributes to the immunosuppressive property of CD4(+)CD25(+)
            regulatory T cells in mice
  JOURNAL   Mol Immunol 49 (1-2), 219-226 (2011)
   PUBMED   21963221
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Xi,W., Hu,Y., Liu,Y., Zhang,J., Wang,L., Lou,Y., Qu,Z., Cui,J.,
            Zhang,G., Liang,X., Ma,C., Gao,C., Chen,Y. and Liu,S.
  TITLE     Roles of TIPE2 in hepatitis B virus-induced hepatic inflammation in
            humans and mice
  JOURNAL   Mol Immunol 48 (9-10), 1203-1208 (2011)
   PUBMED   21466895
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Zhang,G., Hao,C., Lou,Y., Xi,W., Wang,X., Wang,Y., Qu,Z., Guo,C.,
            Chen,Y., Zhang,Y. and Liu,S.
  TITLE     Tissue-specific expression of TIPE2 provides insights into its
            function
  JOURNAL   Mol Immunol 47 (15), 2435-2442 (2010)
   PUBMED   20663561
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079019.1.
            
            On Apr 20, 2005 this sequence version replaced XP_227431.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079019.1, CK470001.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..184
                     /product="tumor necrosis factor alpha-induced protein
                     8-like protein 2"
                     /note="tumor necrosis factor, alpha-induced protein 8-like
                     protein 2; TIPE2; TNFAIP8-like protein 2; TNF
                     alpha-induced protein 8-like protein 2; tumor necrosis
                     factor, alpha-induced protein 8-like 2"
                     /calculated_mol_wt=20620
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P589; propagated from
                     UniProtKB/Swiss-Prot (Q6AYJ8.1)"
     Region          25..182
                     /region_name="DUF758"
                     /note="Domain of unknown function (DUF758); pfam05527"
                     /db_xref="CDD:461672"
     CDS             1..184
                     /gene="Tnfaip8l2"
                     /gene_synonym="RGD1310519"
                     /coded_by="NM_001014039.1:359..913"
                     /db_xref="GeneID:310663"
                     /db_xref="RGD:1310519"
ORIGIN      
        1 mesfssksla lqaekkllsk magrsvahlf idetssevld elyrvskeyt hsrskaqrvi
       61 kdlikvavkv avlhrsgcfs pgelalatrf rqklrqgamt alsfgevdft feaavlagll
      121 iecreillel vehhltpksh drirhvfdhy sdpdlltaly gpdftqhldk icdglrklld
      181 egkl
//
LOCUS       NP_001100128             542 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC domain-containing protein 7 [Rattus norvegicus].
ACCESSION   NP_001100128 XP_216407
VERSION     NP_001100128.1
DBSOURCE    REFSEQ: accession NM_001106658.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161967.1.
            
            On Oct 4, 2007 this sequence version replaced XP_216407.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..542
                     /product="zinc finger CCHC domain-containing protein 7"
                     /note="TRAMP-like complex RNA-binding factor ZCCHC7; zinc
                     finger, CCHC domain containing 7"
                     /calculated_mol_wt=63195
     Region          110..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC15.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B1WC15.1)"
     Region          <235..364
                     /region_name="AIR1"
                     /note="Arginine methyltransferase-interacting protein,
                     contains RING Zn-finger [Posttranslational modification,
                     protein turnover, chaperones / Intracellular trafficking
                     and secretion]; COG5082"
                     /db_xref="CDD:227414"
     Region          396..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC15.1)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3Z6; propagated from
                     UniProtKB/Swiss-Prot (B1WC15.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3Z6; propagated from
                     UniProtKB/Swiss-Prot (B1WC15.1)"
     CDS             1..542
                     /gene="Zcchc7"
                     /coded_by="NM_001106658.2:43..1671"
                     /db_xref="GeneID:298086"
                     /db_xref="RGD:1310467"
ORIGIN      
        1 mfggfetiea feddlyrdds sselsvdsev efqlysqvhy sqnihnanee egyeeknces
       61 setvsiqpdq knlivlsdse viqlsdtsev itlsdedsiy rckrknievq aqektqspat
      121 prsnkvankc krsnkkpepe espstirevm iievssdeee estisenenv eswmllgcee
      181 ddkdndilln lvgckdagae gendvnwfis dkdieakidn nrssgrwnnr yysvnknvtc
      241 rncdkrghls kncplpqkvr pcclcsergh lqygcparyc ldcslpmsst hrcfersswr
      301 krcdrcdmig hyadacpeiw rqyhlttkpg ppkkpktpsg qsalvycync aqkghyghec
      361 terrmfnqaf ptspfiycyd dkydiqqrdr rikrklkdik kngdfprqfk rphgeetdry
      421 hhdrrksrfs gkrsrwpres ketqkektrg regekhrrdr qprdededfp rglkpnssss
      481 snsqkpsksl hqashyhrlr eeklrresmr skpkkrkfve dgshddlfli kqrkkkpkss
      541 gf
//
LOCUS       NP_001107873            1649 aa            linear   ROD 27-APR-2025
DEFINITION  cortactin-binding protein 2 [Rattus norvegicus].
ACCESSION   NP_001107873 XP_001058537 XP_347231
VERSION     NP_001107873.1
DBSOURCE    REFSEQ: accession NM_001114401.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1649)
  AUTHORS   Shih,P.Y., Hsieh,B.Y., Tsai,C.Y., Lo,C.A., Chen,B.E. and Hsueh,Y.P.
  TITLE     Autism-linked mutations of CTTNBP2 reduce social interaction and
            impair dendritic spine formation via diverse mechanisms
  JOURNAL   Acta Neuropathol Commun 8 (1), 185 (2020)
   PUBMED   33168105
  REMARK    GeneRIF: Autism-linked mutations of CTTNBP2 reduce social
            interaction and impair dendritic spine formation via diverse
            mechanisms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1649)
  AUTHORS   Shih,P.Y., Lee,S.P., Chen,Y.K. and Hsueh,Y.P.
  TITLE     Cortactin-binding protein 2 increases microtubule stability and
            regulates dendritic arborization
  JOURNAL   J Cell Sci 127 (Pt 16), 3521-3534 (2014)
   PUBMED   24928895
  REMARK    GeneRIF: Cttnbp2 increases microtubule stability and regulates
            dendritic arborization.
REFERENCE   3  (residues 1 to 1649)
  AUTHORS   Chen,Y.K. and Hsueh,Y.P.
  TITLE     Cortactin-binding protein 2 modulates the mobility of cortactin and
            regulates dendritic spine formation and maintenance
  JOURNAL   J Neurosci 32 (3), 1043-1055 (2012)
   PUBMED   22262902
  REMARK    GeneRIF: This sst=udy demonistrated that Cortactin-binding protein
            2 modulates the mobility of cortactin and regulates dendritic spine
            formation and maintenance.
REFERENCE   4  (residues 1 to 1649)
  AUTHORS   Thomas,J.W., Touchman,J.W., Blakesley,R.W., Bouffard,G.G.,
            Beckstrom-Sternberg,S.M., Margulies,E.H., Blanchette,M.,
            Siepel,A.C., Thomas,P.J., McDowell,J.C., Maskeri,B., Hansen,N.F.,
            Schwartz,M.S., Weber,R.J., Kent,W.J., Karolchik,D., Bruen,T.C.,
            Bevan,R., Cutler,D.J., Schwartz,S., Elnitski,L., Idol,J.R.,
            Prasad,A.B., Lee-Lin,S.Q., Maduro,V.V., Summers,T.J., Portnoy,M.E.,
            Dietrich,N.L., Akhter,N., Ayele,K., Benjamin,B., Cariaga,K.,
            Brinkley,C.P., Brooks,S.Y., Granite,S., Guan,X., Gupta,J.,
            Haghighi,P., Ho,S.L., Huang,M.C., Karlins,E., Laric,P.L.,
            Legaspi,R., Lim,M.J., Maduro,Q.L., Masiello,C.A., Mastrian,S.D.,
            McCloskey,J.C., Pearson,R., Stantripop,S., Tiongson,E.E.,
            Tran,J.T., Tsurgeon,C., Vogt,J.L., Walker,M.A., Wetherby,K.D.,
            Wiggins,L.S., Young,A.C., Zhang,L.H., Osoegawa,K., Zhu,B., Zhao,B.,
            Shu,C.L., De Jong,P.J., Lawrence,C.E., Smit,A.F., Chakravarti,A.,
            Haussler,D., Green,P., Miller,W. and Green,E.D.
  TITLE     Comparative analyses of multi-species sequences from targeted
            genomic regions
  JOURNAL   Nature 424 (6950), 788-793 (2003)
   PUBMED   12917688
REFERENCE   5  (residues 1 to 1649)
  AUTHORS   Ohoka,Y. and Takai,Y.
  TITLE     Isolation and characterization of cortactin isoforms and a novel
            cortactin-binding protein, CBP90
  JOURNAL   Genes Cells 3 (9), 603-612 (1998)
   PUBMED   9813110
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DP000027.1.
            
            On or before Feb 10, 2008 this sequence version replaced
            XP_347231.3, XP_001058537.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132268
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1649
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..1649
                     /product="cortactin-binding protein 2"
                     /note="brain specific cortactin-binding protein CBP90"
                     /calculated_mol_wt=178637
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          36..179
                     /region_name="CortBP2"
                     /note="Cortactin-binding protein-2; pfam09727"
                     /db_xref="CDD:462860"
     Region          <134..476
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Region          296..>701
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          322..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          451..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          492..604
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Site            495
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:B9EJA2; propagated from
                     UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          688..959
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          699..729
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          702..731
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          733..764
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          733..762
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Site            order(766,768,772..773,776..778,780..781,785,788,797,799,
                     801,805..806,809..811,813..814,818,821,830,832,834,
                     838..839,842..844,846..847,851,854)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          766..797
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          766..795
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          799..830
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          799..828
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          832..861
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          901..931
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          901..925
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <1077..1357
                     /region_name="PRK11331"
                     /note="5-methylcytosine-specific restriction enzyme
                     subunit McrB; Provisional"
                     /db_xref="CDD:183088"
     Region          1438..1471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2IBD4.1)"
     Region          1527..1649
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2IBD4.1)"
     CDS             1..1649
                     /gene="Cttnbp2"
                     /gene_synonym="Cbp90; Cortbp2"
                     /coded_by="NM_001114401.1:91..5040"
                     /db_xref="GeneID:282587"
                     /db_xref="RGD:628691"
ORIGIN      
        1 matdsascep dlsrapgdae gataeaakke fdvdtlskse lrmllsvmeg eleardlvie
       61 alrarrkevf iqerygrfnl ndpflalqrd yeagagdkek pvctnplsil eavmahcrkm
      121 qermsaqlaa aesrqkklem eklqlqaleq ehkklaahle eergknkhvv lmlvkeckql
      181 sgkvveeaqk leevmvklee ekkktseled qlsaekqrsa gmeaqlekql fefdtereql
      241 rakltreeah ttdlkeeidk mkkmmeqmkk gndgkpglsl prktkdkrla sisvategpv
      301 trsvacqtdv vtestdpvkk lplsvpikps tgsplvstnt kgnvgpsall irpgidrqas
      361 hsdlgpsppt alpssasrie engpsagnap dlsnstpstp sgtapaaaqt lgaapqnhsq
      421 appvhslhsp canthpglnp riqaarfrfq gnandpdqng nntqsppsrd vsptsrdnlv
      481 akqlarntvt qalsrftspq agassrlgas pggdagtcpp vgrtglktpg aarvdrgnpp
      541 pippkkpgls qtpspphpql rasnagakvd nkivasppst lpqgtkvvne envpkssspq
      601 lppkpsidlt vasagcpvsa latsqvgawp aetpglnqpa ctdsslvipt tvafrssinp
      661 vsassrspga sdsllvtasg wspsltpllm sggpaplagr ptllqqaaaq gnvtllsmll
      721 neegldinyc cedshsalys aaknghtdcv rlllnaearv daadkngftp lcvaaaqghf
      781 ecielltayn aninhsaagg qtplylackt gnkeciklll eagtdrsikt rdgwtpihaa
      841 vdtgnvdslk llmyhrvpap gnslsaeepk sglfslngge sppgsskpvv padlinhadk
      901 egwtaahiaa skgfknclei lcrhgglepe rrdkcnrtvh dvatddckhl lenlnalkip
      961 lrisvgeiqp sndgsddfec ehtictlnir kqtswedfsk avsqaltnhf qaissdgcwg
     1021 ledgtlnntt dsciglgtss iqsimlgsip wstgqsfsqs pwdfmkkkkv eqvtvllsgp
     1081 qegclssvty tsmiplqmlq nylrlveqyh nvifhgpegs lqdyianqla lcmkhrqmaa
     1141 gfpceivrae vdsgfskeql vdvfisnacl ipvkqfpvkk kiivilenle ksslsellgd
     1201 flaplenrst espctfqkgn gtsecyyfhe ncfllgtlak aclqgsdllv qqhfrwvqlr
     1261 wdcepsqgll qrflrrkavs kfrgqlpapc dpvckivdwv isvwrqlnsc larlgtpeal
     1321 lgpkyflscp vvpghaqatv kwmsklwnai iaprvqeail sraamnkqpg arqtaskkhp
     1381 sqgqqavvra alsillnkai lhgcplprte ldqqiadfkg gsfplsivss yskkkgesaa
     1441 wrkvntsprk kpghfsspmw nkpdlkhegm rnksvphlni nrssslskqq slendlsmtl
     1501 tldhrlslgs ddeadlvkel qsmcsskses diskiadsre dlrtfdssrt npvtsapvnl
     1561 rmpvpqkeas plsshqttec snsksktelg vsrvksflpv prskvaqcsq ntkrssssss
     1621 ntrqleinnn skeenwnvdk hehvekrnk
//
LOCUS       NP_063970                339 aa            linear   ROD 27-APR-2025
DEFINITION  annexin A2 [Rattus norvegicus].
ACCESSION   NP_063970
VERSION     NP_063970.1
DBSOURCE    REFSEQ: accession NM_019905.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Liu,B., Xing,Z., Song,F., Li,D., Zhao,B., Xu,C., Xia,W. and Ji,H.
  TITLE     METTL3-mediated ANXA2 inhibition confers neuroprotection in
            ischemic stroke: Evidence from in vivo and in vitro studies
  JOURNAL   FASEB J 37 (7), e22974 (2023)
   PUBMED   37249328
  REMARK    GeneRIF: METTL3-mediated ANXA2 inhibition confers neuroprotection
            in ischemic stroke: Evidence from in vivo and in vitro studies.
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Li,D.W., Qi,X.D., Zhang,C.H. and Sun,W.P.
  TITLE     Annexin A2 degradation contributes to dopaminergic cell apoptosis
            via regulating p53 in neurodegenerative conditions
  JOURNAL   Neuroreport 32 (15), 1263-1268 (2021)
   PUBMED   34494994
  REMARK    GeneRIF: Annexin A2 degradation contributes to dopaminergic cell
            apoptosis via regulating p53 in neurodegenerative conditions.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Wang,Y., Xu,W., Zu,M. and Xu,H.
  TITLE     Circular RNA circ_0021093 regulates miR-432/Annexin A2 pathway to
            promote hepatocellular carcinoma progression
  JOURNAL   Anticancer Drugs 32 (5), 484-495 (2021)
   PUBMED   33675609
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Fahling,M., Paliege,A., Jonsson,S., Becirovic-Agic,M.,
            Melville,J.M., Skogstrand,T. and Hultstrom,M.
  TITLE     NFAT5 regulates renal gene expression in response to angiotensin II
            through Annexin-A2-mediated posttranscriptional regulation in
            hypertensive rats
  JOURNAL   Am J Physiol Renal Physiol 316 (1), F101-F112 (2019)
   PUBMED   30332317
  REMARK    GeneRIF: ANGII increases Annexin-A2 nucleic acid-binding activity
            and elevates protein levels of the NFAT5 transcription factor in
            kidneys of hypertensive rats.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Liao,L., Zheng,B., Yi,B., Liu,C., Chen,L., Zeng,Z. and Gao,J.
  TITLE     Annexin A2-modulated proliferation of pulmonary arterial smooth
            muscle cells depends on caveolae and caveolin-1 in hepatopulmonary
            syndrome
  JOURNAL   Exp Cell Res 359 (1), 266-274 (2017)
   PUBMED   28729092
  REMARK    GeneRIF: Cav-1 participates upstream of ANXA2 in the activation of
            ERK1/2 and NF-kappaB.
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Takahashi,S., Reddy,S.V., Chirgwin,J.M., Devlin,R., Haipek,C.,
            Anderson,J. and Roodman,G.D.
  TITLE     Cloning and identification of annexin II as an autocrine/paracrine
            factor that increases osteoclast formation and bone resorption
  JOURNAL   J Biol Chem 269 (46), 28696-28701 (1994)
   PUBMED   7961821
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Upton,A.L. and Moss,S.E.
  TITLE     Molecular cloning of a novel N-terminal variant of annexin II from
            rat basophilic leukaemia cells
  JOURNAL   Biochem J 302 (Pt 2) (Pt 2), 425-428 (1994)
   PUBMED   8092993
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Mizutani,A., Usuda,N., Tokumitsu,H., Minami,H., Yasui,K.,
            Kobayashi,R. and Hidaka,H.
  TITLE     CAP-50, a newly identified annexin, localizes in nuclei of cultured
            fibroblast 3Y1 cells
  JOURNAL   J Biol Chem 267 (19), 13498-13504 (1992)
   PUBMED   1618851
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Blackwood,R.A. and Ernst,J.D.
  TITLE     Characterization of Ca2(+)-dependent phospholipid binding, vesicle
            aggregation and membrane fusion by annexins
  JOURNAL   Biochem J 266 (1), 195-200 (1990)
   PUBMED   2138016
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Huang,K.S., Wallner,B.P., Mattaliano,R.J., Tizard,R., Burne,C.,
            Frey,A., Hession,C., McGray,P., Sinclair,L.K., Chow,E.P. et al.
  TITLE     Two human 35 kd inhibitors of phospholipase A2 are related to
            substrates of pp60v-src and of the epidermal growth factor
            receptor/kinase
  JOURNAL   Cell 46 (2), 191-199 (1986)
   PUBMED   3013422
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X66871.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X66871.1, BC059136.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..339
                     /product="annexin A2"
                     /note="p36; PAP-IV; annexin-2; protein I; lipocortin II;
                     chromobindin-8; placental anticoagulant protein IV;
                     calpactin-1 heavy chain; calpactin I heavy chain"
                     /calculated_mol_wt=38547
     Region          2..24
                     /region_name="S100A10-binding site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.5;
                     propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P07355; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P07355; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Region          33..104
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Region          37..102
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            49
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07356; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Region          105..176
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Region          109..174
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            152
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07356; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07355; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Region          189..261
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Region          193..259
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P07356; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Site            227
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07356; propagated from
                     UniProtKB/Swiss-Prot (Q07936.2)"
     Region          265..336
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07936.2)"
     Region          269..334
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     CDS             1..339
                     /gene="Anxa2"
                     /gene_synonym="ANX2"
                     /coded_by="NM_019905.1:43..1062"
                     /db_xref="GeneID:56611"
                     /db_xref="RGD:621170"
ORIGIN      
        1 mstvheilck lslegdhstp psaygsvkpy tnfdaerdal nietaiktkg vdevtivnil
       61 tnrsnaqrqd iafayqrrtk kelpsamksa lsghletvml gllktpaqyd aselkasmkg
      121 lgtdedslie iicsrtnqel qeinrvykem yktdlekdii sdtsgefrkl lvalakgkra
      181 edgsvidyel idqdarelyd agvkrkgtdv pkwisimter svchlqkvfe ryksyspydm
      241 lesirkevkg dlenaflnlv qciqnkplyf adrlydsmkg kgtrdkvlir imvsrsevdm
      301 lkirsefkrk ygkslyyfiq qdtkgdyqka llylcggdd
//
LOCUS       NP_071614                107 aa            linear   ROD 27-APR-2025
DEFINITION  glutaredoxin-1 [Rattus norvegicus].
ACCESSION   NP_071614
VERSION     NP_071614.1
DBSOURCE    REFSEQ: accession NM_022278.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Gao,X.H., Qanungo,S., Pai,H.V., Starke,D.W., Steller,K.M.,
            Fujioka,H., Lesnefsky,E.J., Kerner,J., Rosca,M.G., Hoppel,C.L. and
            Mieyal,J.J.
  TITLE     Aging-dependent changes in rat heart mitochondrial
            glutaredoxins--Implications for redox regulation
  JOURNAL   Redox Biol 1 (1), 586-598 (2013)
   PUBMED   25126518
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Picklo,M.J. Sr., Idso,J.P. and Jackson,M.I.
  TITLE     S-Glutathionylation of hepatic and visceral adipose proteins
            decreases in obese rats
  JOURNAL   Obesity (Silver Spring) 21 (2), 297-305 (2013)
   PUBMED   23404913
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Aon-Bertolino,M.L., Romero,J.I., Galeano,P., Holubiec,M.,
            Badorrey,M.S., Saraceno,G.E., Hanschmann,E.M., Lillig,C.H. and
            Capani,F.
  TITLE     Thioredoxin and glutaredoxin system proteins-immunolocalization in
            the rat central nervous system
  JOURNAL   Biochim Biophys Acta 1810 (1), 93-110 (2011)
   PUBMED   20620191
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Gallogly,M.M., Shelton,M.D., Qanungo,S., Pai,H.V., Starke,D.W.,
            Hoppel,C.L., Lesnefsky,E.J. and Mieyal,J.J.
  TITLE     Glutaredoxin regulates apoptosis in cardiomyocytes via NFkappaB
            targets Bcl-2 and Bcl-xL: implications for cardiac aging
  JOURNAL   Antioxid Redox Signal 12 (12), 1339-1353 (2010)
   PUBMED   19938943
  REMARK    GeneRIF: Grx1 decreases by ~40% in 2-yr-old Fischer 344 rat hearts
            vs 6-mo-old controls. Grx1 knockdown in H9c2 cardiomyocytes
            increases apoptosis, & decreases NFkappaB transcription,&
            production of Bcl-2 & Bcl-xL.
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Terada,T., Okamoto,K., Nishikawa,J., Miura,T., Nishinaka,T. and
            Nishihara,T.
  TITLE     Site-directed mutagenesis of rat thioltransferase: effects of
            essential cysteine residues for the protection against oxidative
            stress
  JOURNAL   J Biochem Mol Toxicol 24 (1), 60-65 (2010)
   PUBMED   20175144
  REMARK    GeneRIF: study reports Cys23 of thioltransferase is an essential
            residue for catalytic activity & the other Cys26 is also important
            but Cys79 & Cys83 were not essential; for protection of cells from
            oxidative stress active thioltransferase is essential
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Ehrhart,J., Gluck,M., Mieyal,J. and Zeevalk,G.D.
  TITLE     Functional glutaredoxin (thioltransferase) activity in rat brain
            and liver mitochondria
  JOURNAL   Parkinsonism Relat Disord 8 (6), 395-400 (2002)
   PUBMED   12217626
  REMARK    GeneRIF: The presence of enzyme activity in subcellular organelles
            in brain and liver and in mitochondria demonstrates functional
            glutaredoxin activity.
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Porras,P., Pedrajas,J.R., Martinez-Galisteo,E., Padilla,C.A.,
            Johansson,C., Holmgren,A. and Barcena,J.A.
  TITLE     Glutaredoxins catalyze the reduction of glutathione by
            dihydrolipoamide with high efficiency
  JOURNAL   Biochem Biophys Res Commun 295 (5), 1046-1051 (2002)
   PUBMED   12135599
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Kobayashi,M., Nakamura,H., Yodoi,J. and Shiota,K.
  TITLE     Immunohistochemical localization of thioredoxin and glutaredoxin in
            mouse embryos and fetuses
  JOURNAL   Antioxid Redox Signal 2 (4), 653-663 (2000)
   PUBMED   11213470
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Takagi,Y., Nakamura,T., Nishiyama,A., Nozaki,K., Tanaka,T.,
            Hashimoto,N. and Yodoi,J.
  TITLE     Localization of glutaredoxin (thioltransferase) in the rat brain
            and possible functional implications during focal ischemia
  JOURNAL   Biochem Biophys Res Commun 258 (2), 390-394 (1999)
   PUBMED   10329397
REFERENCE   10 (residues 1 to 107)
  AUTHORS   Padilla,C.A., Martinez-Galisteo,E., Barcena,J.A., Spyrou,G. and
            Holmgren,A.
  TITLE     Purification from placenta, amino acid sequence, structure
            comparisons and cDNA cloning of human glutaredoxin
  JOURNAL   Eur J Biochem 227 (1-2), 27-34 (1995)
   PUBMED   7851394
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF167981.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF167981.3, BC061555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q11"
     Protein         1..107
                     /product="glutaredoxin-1"
                     /EC_number="1.8.4.1"
                     /note="glutaredoxin 1 (thioltransferase); TTase-1;
                     thioltransferase-1; glutaredoxin (thioltransferase)"
                     /calculated_mol_wt=11748
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P10575; propagated from
                     UniProtKB/Swiss-Prot (Q9ESH6.3)"
     Region          15..99
                     /region_name="GRX_euk"
                     /note="Glutaredoxin; TIGR02180"
                     /db_xref="CDD:274016"
     Site            order(20,23,25,68..71,82..85)
                     /site_type="other"
                     /note="GSH binding site [chemical binding]"
                     /db_xref="CDD:239511"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239511"
     CDS             1..107
                     /gene="Glrx"
                     /gene_synonym="Glrx1; Grx"
                     /coded_by="NM_022278.1:32..355"
                     /db_xref="GeneID:64045"
                     /db_xref="RGD:70951"
ORIGIN      
        1 maqefvncki qsgkvvvfik ptcpycrktq eilsqlpfkr gllefvdita tnntnaiqdy
       61 lqqltgartv prvfigkdci ggcsdllsmq qngeltarlk qigalql
//
LOCUS       NP_001014101             525 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger C2HC domain-containing protein 1C [Rattus norvegicus].
ACCESSION   NP_001014101 XP_234421
VERSION     NP_001014101.1
DBSOURCE    REFSEQ: accession NM_001014079.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078967.1.
            
            On Apr 20, 2005 this sequence version replaced XP_234421.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132267
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..525
                     /product="zinc finger C2HC domain-containing protein 1C"
                     /note="protein FAM164C; family with sequence similarity
                     164, member C"
                     /calculated_mol_wt=59319
     Region          23..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          85..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          145..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          188..>293
                     /region_name="HlpA"
                     /note="Periplasmic chaperone for outer membrane proteins,
                     Skp family [Cell wall/membrane/envelope biogenesis,
                     Posttranslational modification, protein turnover,
                     chaperones]; COG2825"
                     /db_xref="CDD:442073"
     Region          292..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          330..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          356..379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYP4.1)"
     Region          378..401
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          489..511
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     CDS             1..525
                     /gene="Zc2hc1c"
                     /gene_synonym="Fam164c; RGD1307122"
                     /coded_by="NM_001014079.1:104..1681"
                     /db_xref="GeneID:314321"
                     /db_xref="RGD:1307122"
ORIGIN      
        1 maglqlaphl pvgvmfphnk teahglhsak hdpyeqsdsp qrssmghlrt sfqqklwsnt
       61 eleqedvist hpkrnictka rrhscphsag isqqgsgnna qgqgkglfyl ssptprypka
      121 ndqdfipfrk krvgvdrayp lkpmvhrksh stsetgidgd qngyprlpds sefsdssfgl
      181 rswvnpslla spqaekvmaq lhrtewtqiq rleaageslq keirrkeill reklkkteeg
      241 lrriqrekkq aifqedrelq rmvlprrrvr dgdldtthns clspelrsev fsrnrgedqt
      301 ceqaqenssp lqlsdyeiqr lkrerlmvsn nkirdrdsgp sagtfsqpae dlgdelqass
      361 lsgtpgssgs sssteeqelg kcshcgrsfl slrlqrhstv cgkmqgskrk vfdssrarak
      421 gteleqylnw rgpatdkaep pprkstwrqk hesfirtlrh arqvqqviar ggnpsdlpsi
      481 lpaenpdyvq cphcsrhfap kvaerhipkc ktiknrpppp rrhds
//
LOCUS       NP_001019471             602 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate-rich protein 6 [Rattus norvegicus].
ACCESSION   NP_001019471 XP_574950
VERSION     NP_001019471.1
DBSOURCE    REFSEQ: accession NM_001024300.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083834.1.
            
            On May 27, 2005 this sequence version replaced XP_574950.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083834.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..602
                     /product="glutamate-rich protein 6"
                     /note="protein FAM194A; family with sequence similarity
                     194, member A"
                     /calculated_mol_wt=67834
     Region          22..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI56.1)"
     Region          362..564
                     /region_name="FAM194"
                     /note="FAM194 protein; pfam14977"
                     /db_xref="CDD:464417"
     CDS             1..602
                     /gene="Erich6"
                     /gene_synonym="Fam194a"
                     /coded_by="NM_001024300.1:154..1962"
                     /db_xref="GeneID:499626"
                     /db_xref="RGD:1559451"
ORIGIN      
        1 meddiwkavd lsgvfdedsv elrprltsvs spslsstppp splsspswse eelpaprsdg
       61 spassisahk sypkifqtfk kdlsevtvdr lmypsfyerv qisiqtedqs wlqrisarkr
      121 ikripsieit eapqenlask lrenwvinpe epklsilcem efnedfvnff etslrtlpsi
      181 gpptilsyrk eyscmdvilk deqelgatce fcgsdlqslf fnmdtsldda gtkgkshrsc
      241 clqfqnlldy iteerlttks pemelisisp haahgsdadr lkakekamqr kqerqmarhf
      301 tiipeqspvg teedtkhlkt isyqlsgdyl qnvrteevdl qitnisitcc dswkicgkvm
      361 gnellekdyk hgskfltsfp dgtiqifyps gnlaiirvpn ktdgficiiq edtatspail
      421 alfdssgrss cyhpngnvwv yinilggqys dqagnrirtw nwsstkptpa fvsfkpvlla
      481 lnryigiril eqdkvsihfl amgqqaticl gtkvvlqdpe evptlrflsg ddllllasli
      541 kirrlfskme gcvnfpvska werlkqpsyl sslslkllal cqnsgiqqni metitelike
      601 ne
//
LOCUS       NP_071792                415 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein F [Rattus norvegicus].
ACCESSION   NP_071792
VERSION     NP_071792.1
DBSOURCE    REFSEQ: accession NM_022397.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Lo,C.S., Shi,Y., Chenier,I., Ghosh,A., Wu,C.H., Cailhier,J.F.,
            Ethier,J., Lattouf,J.B., Filep,J.G., Ingelfinger,J.R., Zhang,S.L.
            and Chan,J.S.D.
  TITLE     Heterogeneous Nuclear Ribonucleoprotein F Stimulates Sirtuin-1 Gene
            Expression and Attenuates Nephropathy Progression in Diabetic Mice
  JOURNAL   Diabetes 66 (7), 1964-1978 (2017)
   PUBMED   28424160
  REMARK    GeneRIF: hnRNP F protects kidneys against oxidative stress and
            nephropathy via stimulation of Sirtuin-1 expression and signaling
            in diabetes.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dominguez,C., Fisette,J.F., Chabot,B. and Allain,F.H.
  TITLE     Structural basis of G-tract recognition and encaging by hnRNP F
            quasi-RRMs
  JOURNAL   Nat Struct Mol Biol 17 (7), 853-861 (2010)
   PUBMED   20526337
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Wei,C.C., Zhang,S.L., Chen,Y.W., Guo,D.F., Ingelfinger,J.R.,
            Bomsztyk,K. and Chan,J.S.
  TITLE     Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen
            gene expression in kidney cells
  JOURNAL   J Biol Chem 281 (35), 25344-25355 (2006)
   PUBMED   16837467
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Wei,C.C., Guo,D.F., Zhang,S.L., Ingelfinger,J.R. and Chan,J.S.
  TITLE     Heterogenous nuclear ribonucleoprotein F modulates angiotensinogen
            gene expression in rat kidney proximal tubular cells
  JOURNAL   J Am Soc Nephrol 16 (3), 616-628 (2005)
   PUBMED   15659559
  REMARK    GeneRIF: hnRNP F binds to rANG-IRE and modulates renal ANG gene
            expression, implicating that dysregulation of hnRNP F might affect
            renin-angiotensin system activation and, subsequently, kidney
            injury in diabetes
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Yoshida,T., Makino,Y. and Tamura,T.
  TITLE     Association of the rat heterogeneous nuclear RNA-ribonucleoprotein
            F with TATA-binding protein
  JOURNAL   FEBS Lett 457 (2), 251-254 (1999)
   PUBMED   10471789
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Gamberi,C., Izaurralde,E., Beisel,C. and Mattaj,I.W.
  TITLE     Interaction between the human nuclear cap-binding protein complex
            and hnRNP F
  JOURNAL   Mol Cell Biol 17 (5), 2587-2597 (1997)
   PUBMED   9111328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK473366.1 and BC103634.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103634.1, BC097275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..415
                     /product="heterogeneous nuclear ribonucleoprotein F"
                     /note="hnRNP F; ribonucleoprotein F"
                     /calculated_mol_wt=45599
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein F, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            16
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            20
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            52
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            75
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          81..86
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            116
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            120
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            150
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            173
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          179..184
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X1; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          255..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          289..363
                     /region_name="RRM3_hnRNPH_CRSF1_like"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H protein
                     family, G-rich sequence factor 1 (GRSF-1) and similar
                     proteins; cd12506"
                     /db_xref="CDD:409929"
     Site            294
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            298
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            326
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            349
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          355..360
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     CDS             1..415
                     /gene="Hnrnpf"
                     /gene_synonym="Hnrpf"
                     /coded_by="NM_022397.3:294..1541"
                     /db_xref="GeneID:64200"
                     /db_xref="RGD:620366"
ORIGIN      
        1 mmlgpeggeg yvvklrglpw scsiedvqnf lsdctihdgv agvhfiytre grqsgeafve
       61 leseddvkla lkkdresmgh ryievfkshr temdwvlkhs gpnsadsand gfvrlrglpf
      121 gctkeeivqf fsgleivpng itlpvdpegk itgeafvqfa sqelaekalg khkerighry
      181 ievfkssqee vrsysdpplk fmsvqrpgpy drpgtarryi givkqagldr mrsgaysagy
      241 ggyeeysgls dgygfttdlf grdlsyclsg mydhrygdse ftvqsttghc vhmrglpyka
      301 tendiynffs plnpvrvhie igpdgrvtge advefathee avaamskdra nmqhryielf
      361 lnsttgasng ayssqvmqgm gvsaaqatys glesqsvsgc ygagysgqns mggyd
//
LOCUS       NP_001071139             596 aa            linear   ROD 27-APR-2025
DEFINITION  endoribonuclease ZC3H12A [Rattus norvegicus].
ACCESSION   NP_001071139 XP_001057109 XP_233517
VERSION     NP_001071139.1
DBSOURCE    REFSEQ: accession NM_001077671.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Li,M., Yang,J., Zhao,Y., Song,Y., Yin,S., Guo,J., Zhang,H.,
            Wang,K., Wei,L., Li,S. and Xu,W.
  TITLE     MCPIP1 inhibits Hepatitis B virus replication by destabilizing
            viral RNA and negatively regulates the virus-induced innate
            inflammatory responses
  JOURNAL   Antiviral Res 174, 104705 (2020)
   PUBMED   31926181
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Zhang,Y., Huang,T., Jiang,L., Gao,J., Yu,D., Ge,Y. and Lin,S.
  TITLE     MCP-induced protein 1 attenuates sepsis-induced acute lung injury
            by modulating macrophage polarization via the JNK/c-Myc pathway
  JOURNAL   Int Immunopharmacol 75, 105741 (2019)
   PUBMED   31323531
  REMARK    GeneRIF: With the help of a cecal ligation puncture-induced model
            of acute lung injury (ALI) in rats, we demonstrated that MCPIP1
            overexpression induced by MG132 can alleviate sepsis-induced
            pathologic changes, increase in water content and protein leakage
            in the lungs, and induction of systemic inflammatory mediators, and
            thereby improve the 7-day mortality rate in sepsis-induced ALI.
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Tyka,K., Jorns,A., Turatsinze,J.V., Eizirik,D.L., Lenzen,S. and
            Gurgul-Convey,E.
  TITLE     MCPIP1 regulates the sensitivity of pancreatic beta-cells to
            cytokine toxicity
  JOURNAL   Cell Death Dis 10 (1), 29 (2019)
   PUBMED   30631045
  REMARK    GeneRIF: Since MCPIP1 expression undergoes fluctuations in islets
            during type 1 diabetes development in the IDDM rat and regulates
            the beta-cell fate upon exposure to proinflammatory cytokines,
            manipulations of its expression and activity might open new
            perspectives for type 1 diabetes treatment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Nakatsuka,Y., Vandenbon,A., Mino,T., Yoshinaga,M., Uehata,T.,
            Cui,X., Sato,A., Tsujimura,T., Suzuki,Y., Sato,A., Handa,T.,
            Chin,K., Sawa,T., Hirai,T. and Takeuchi,O.
  TITLE     Pulmonary Regnase-1 orchestrates the interplay of epithelium and
            adaptive immune systems to protect against pneumonia
  JOURNAL   Mucosal Immunol 11 (4), 1203-1218 (2018)
   PUBMED   29695841
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Li,M., Yan,K., Wei,L., Yang,Y., Qian,Q. and Xu,W.
  TITLE     MCPIP1 inhibits coxsackievirus B3 replication by targeting viral
            RNA and negatively regulates virus-induced inflammation
  JOURNAL   Med Microbiol Immunol 207 (1), 27-38 (2018)
   PUBMED   29043433
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Younce,C.W., Azfer,A. and Kolattukudy,P.E.
  TITLE     MCP-1 (monocyte chemotactic protein-1)-induced protein, a recently
            identified zinc finger protein, induces adipogenesis in 3T3-L1
            pre-adipocytes without peroxisome proliferator-activated receptor
            gamma
  JOURNAL   J Biol Chem 284 (40), 27620-27628 (2009)
   PUBMED   19666473
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Matsushita,K., Takeuchi,O., Standley,D.M., Kumagai,Y., Kawagoe,T.,
            Miyake,T., Satoh,T., Kato,H., Tsujimura,T., Nakamura,H. and
            Akira,S.
  TITLE     Zc3h12a is an RNase essential for controlling immune responses by
            regulating mRNA decay
  JOURNAL   Nature 458 (7242), 1185-1190 (2009)
   PUBMED   19322177
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Niu,J., Azfer,A., Zhelyabovska,O., Fatma,S. and Kolattukudy,P.E.
  TITLE     Monocyte chemotactic protein (MCP)-1 promotes angiogenesis via a
            novel transcription factor, MCP-1-induced protein (MCPIP)
  JOURNAL   J Biol Chem 283 (21), 14542-14551 (2008)
   PUBMED   18364357
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Liang,J., Wang,J., Azfer,A., Song,W., Tromp,G., Kolattukudy,P.E.
            and Fu,M.
  TITLE     A novel CCCH-zinc finger protein family regulates proinflammatory
            activation of macrophages
  JOURNAL   J Biol Chem 283 (10), 6337-6346 (2008)
   PUBMED   18178554
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Zhou,L., Azfer,A., Niu,J., Graham,S., Choudhury,M., Adamski,F.M.,
            Younce,C., Binkley,P.F. and Kolattukudy,P.E.
  TITLE     Monocyte chemoattractant protein-1 induces a novel transcription
            factor that causes cardiac myocyte apoptosis and ventricular
            dysfunction
  JOURNAL   Circ Res 98 (9), 1177-1185 (2006)
   PUBMED   16574901
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127516.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_233517.3, XP_001057109.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127516.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..596
                     /product="endoribonuclease ZC3H12A"
                     /EC_number="3.4.19.12"
                     /note="ribonuclease ZC3H12A; Zinc finger CCCH
                     domain-containing protein 12A; bifunctional
                     endoribonuclease and deubiquitinase ZC3H12A; regnase-1;
                     MCP-induced protein 1; monocyte chemotactic
                     protein-induced protein 1"
                     /calculated_mol_wt=65797
     Region          24..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          42..87
                     /region_name="Ubiquitin association domain.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E7"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          49..89
                     /region_name="UBA_6"
                     /note="UBA-like domain; pfam18039"
                     /db_xref="CDD:407876"
     Region          81..150
                     /region_name="Necessary for interaction with TANK.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          92..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8; propagated from
                     UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          112..281
                     /region_name="RNase.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          138..268
                     /region_name="PIN_Zc3h12-like"
                     /note="PRORP-like PIN domain of ribonuclease Zc3h12a and
                     related proteins; cd18729"
                     /db_xref="CDD:350296"
     Region          214..220
                     /region_name="RNA binding.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          278..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          301..454
                     /region_name="Necessary for interaction with ZC3H12D.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          305..323
                     /region_name="zf-CCCH_2"
                     /note="RNA-binding, Nab2-type zinc finger; pfam14608"
                     /db_xref="CDD:464217"
     Region          <323..584
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          339..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E8; propagated from
                     UniProtKB/Swiss-Prot (A0JPN4.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E7; propagated from
                     UniProtKB/Swiss-Prot (A0JPN4.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5D1E7; propagated from
                     UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          447..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          517..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPN4.1)"
     Region          547..590
                     /region_name="Regnase_1_C"
                     /note="Endoribonuclease Regnase 1/ ZC3H12 C-terminal
                     domain; pfam18561"
                     /db_xref="CDD:465803"
     CDS             1..596
                     /gene="Zc3h12a"
                     /gene_synonym="MCPIP-1; Reg1; RGD1306776"
                     /coded_by="NM_001077671.1:96..1886"
                     /db_xref="GeneID:313587"
                     /db_xref="RGD:1306776"
ORIGIN      
        1 msdpcgkklv qeisptmslw gledrhscqg qpqpdqdpva keasaselqm kvdffrklgy
       61 ssseihsalq klgvqadtnt vlgelvkhgs aterecqast dpcpqpplvp rggstpkpst
      121 vepslpeedk essdlrpvvi dgsnvamshg nkevfscrgi llavnwfler ghtditvfvp
      181 swrkeqprpd vpitdqhilr elekkkilvf tpsrrvggkr vvcyddrfiv klayesdgvv
      241 vsndtyrdlq gerqewkrfi eerllmysfv ndkfmppddp lgrhgpsldn flrkkplpse
      301 hrkqpcpygr kctygikcrf fhperpsrpq rsvadelran allspprtpv kdkssqrpsp
      361 asqpnsmsle aepgspdgkk lgtrsspgph qegstqtcap agrslpvsgg sfgptewlph
      421 tldslpytsq ecldsgigsl esqmselwgl rggspgesgp trgpytgyqt ygsklpaapa
      481 fspfrqaigt ghfsvptdyv pppptypare ywsepyplpp ptpvlqepqr prprasgdpw
      541 grvsdlaker agvytklcgv fpphlveavm grfpqlldpq qlaaeilsyk sqhlse
//
LOCUS       NP_001009246             337 aa            linear   ROD 27-APR-2025
DEFINITION  manganese-dependent ADP-ribose/CDP-alcohol diphosphatase [Rattus
            norvegicus].
ACCESSION   NP_001009246 XP_213355
VERSION     NP_001009246.1
DBSOURCE    REFSEQ: accession NM_001009246.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Canales,J., Fernandez,A., Rodrigues,J.R., Ferreira,R.,
            Ribeiro,J.M., Cabezas,A., Costas,M.J. and Cameselle,J.C.
  TITLE     Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by
            the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase
  JOURNAL   FEBS Lett 583 (10), 1593-1598 (2009)
   PUBMED   19379742
  REMARK    GeneRIF: The phosphoanhydride bond of cyclic ADP-ribose or cADPR is
            hydrolyzed by the Mn(2+)-dependent ADP-ribose/CDP-alcohol
            pyrophosphatase.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Canales,J., Fernandez,A., Ribeiro,J.M., Cabezas,A., Rodrigues,J.R.,
            Cameselle,J.C. and Costas,M.J.
  TITLE     Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel
            metallophosphoesterase family preferentially expressed in rodent
            immune cells
  JOURNAL   Biochem J 413 (1), 103-113 (2008)
   PUBMED   18352857
  REMARK    GeneRIF: The structure and function of Mn2+-dependent
            ADP-ribose/CDP-alcohol pyrophosphatase in immune tissues are
            reported.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088174.1.
            
            On Jan 7, 2005 this sequence version replaced XP_213355.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06680448
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..337
                     /product="manganese-dependent ADP-ribose/CDP-alcohol
                     diphosphatase"
                     /EC_number="3.6.1.13"
                     /EC_number="3.6.1.16"
                     /EC_number="3.6.1.53"
                     /note="liver manganese (II)-dependent
                     ADP-ribose/CDP-alcohol pyrophosphatase; CDP-choline
                     phosphohydrolase"
                     /calculated_mol_wt=38581
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q3LIE5; propagated from
                     UniProtKB/Swiss-Prot (Q5M886.1)"
     Region          18..322
                     /region_name="MPP_Nbla03831"
                     /note="Homo sapiens Nbla03831 and related proteins,
                     metallophosphatase domain; cd07396"
                     /db_xref="CDD:277341"
     Site            order(25,27,42,74,110..111,241,278,280)
                     /site_type="active"
                     /db_xref="CDD:277341"
     Site            order(25,27,74,110,241,278,280)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277341"
     CDS             1..337
                     /gene="Adprm"
                     /gene_synonym="ADPRibase-Mn; MDS006; RGD1309906"
                     /coded_by="NM_001009246.1:154..1167"
                     /db_xref="GeneID:287406"
                     /db_xref="RGD:1309906"
ORIGIN      
        1 madkpdpssp adgpeplfsf gviadiqyad ledgynfqrs rrryyrhslv hlqgaiedwn
       61 kessmpccvl qlgdiidgyn aqykvseksl elvmntfqml kvpvhhtwgn hefynfsrdy
      121 lansklnskf ledqipqhpe ttpsenyyay hfvpfpkfrf illdsydlsv lgidqfspky
      181 eqcmkilreh npnvelnspq glsepqyvqf nggfsqeqln wlnevltfsd anqekvvivs
      241 hlpiypeasd svclawnyvd alsiiwshqc vvcflaghth dggysedpfg vhhvnlegvi
      301 etapdsqafg tvhvypdkml lkgrgrvpdr imnykre
//
LOCUS       NP_116008                586 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein L isoform b [Rattus
            norvegicus].
ACCESSION   NP_116008 XP_214878
VERSION     NP_116008.2
DBSOURCE    REFSEQ: accession NM_032619.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Atianand,M.K., Hu,W., Satpathy,A.T., Shen,Y., Ricci,E.P.,
            Alvarez-Dominguez,J.R., Bhatta,A., Schattgen,S.A., McGowan,J.D.,
            Blin,J., Braun,J.E., Gandhi,P., Moore,M.J., Chang,H.Y.,
            Lodish,H.F., Caffrey,D.R. and Fitzgerald,K.A.
  TITLE     A Long Noncoding RNA lincRNA-EPS Acts as a Transcriptional Brake to
            Restrain Inflammation
  JOURNAL   Cell 165 (7), 1672-1685 (2016)
   PUBMED   27315481
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Loh,T.J., Cho,S., Moon,H., Jang,H.N., Williams,D.R., Jung,D.W.,
            Kim,I.C., Ghigna,C., Biamonti,G., Zheng,X. and Shen,H.
  TITLE     hnRNP L inhibits CD44 V10 exon splicing through interacting with
            its upstream intron
  JOURNAL   Biochim Biophys Acta 1849 (6), 743-750 (2015)
   PUBMED   25623890
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Yau,W.Y., Shih,H.C., Tsai,M.H., Sheu,J.C., Chen,C.H. and Chow,L.P.
  TITLE     Autoantibody recognition of an N-terminal epitope of hnRNP L marks
            the risk for developing HBV-related hepatocellular carcinoma
  JOURNAL   J Proteomics 94, 346-358 (2013)
   PUBMED   24125732
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Costain,W.J. and Mishra,R.K.
  TITLE     PLG regulates hnRNP-L expression in the rat striatum and
            pre-frontal cortex: identification by ddPCR
  JOURNAL   Peptides 24 (1), 137-146 (2003)
   PUBMED   12576095
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Kuninger,D.T., Izumi,T., Papaconstantinou,J. and Mitra,S.
  TITLE     Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like
            repressor element in the AP-endonuclease 1 promoter
  JOURNAL   Nucleic Acids Res 30 (3), 823-829 (2002)
   PUBMED   11809897
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Hamilton,B.J., Nichols,R.C., Tsukamoto,H., Boado,R.J.,
            Pardridge,W.M. and Rigby,W.F.
  TITLE     hnRNP A2 and hnRNP L bind the 3'UTR of glucose transporter 1 mRNA
            and exist as a complex in vivo
  JOURNAL   Biochem Biophys Res Commun 261 (3), 646-651 (1999)
   PUBMED   10441480
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Pinol-Roma,S., Swanson,M.S., Gall,J.G. and Dreyfuss,G.
  TITLE     A novel heterogeneous nuclear RNP protein with a unique
            distribution on nascent transcripts
  JOURNAL   J Cell Biol 109 (6 Pt 1), 2575-2587 (1989)
   PUBMED   2687284
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 4, 2008 this sequence version replaced NP_116008.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169048.1, SRR26643429.1451.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..586
                     /product="heterogeneous nuclear ribonucleoprotein L
                     isoform b"
                     /note="heterogenous nuclear ribonucleoprotein L"
                     /calculated_mol_wt=63833
     Region          97..584
                     /region_name="hnRNP-L_PTB"
                     /note="hnRNP-L/PTB/hephaestus splicing factor family;
                     TIGR01649"
                     /db_xref="CDD:273733"
     CDS             1..586
                     /gene="Hnrnpl"
                     /gene_synonym="hnrnp-L; Hnrpl"
                     /coded_by="NM_032619.2:1..1761"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:80846"
                     /db_xref="RGD:71059"
ORIGIN      
        1 msrrllprae krrrrleqrq qpdeqlrrag amvkmaaagg gggggryygg gneggrapkr
       61 lktenagdqh gggggggsga agggggenyd dphktpaspv vhirglidgv veadlvealq
      121 efgpisyvvv mpkkrqalve fedvlgacna vnyaadnqiy iaghpafvny stsqkisrpg
      181 dsddsrsvns vllftilnpi ysittdvlyt icnpcgpvqr ivifrkngvq amvefdsvqs
      241 aqrakaslng adiysgcctl kieyakptrl nvfkndqdtw dytnpnlsgq gdpgsnpnkr
      301 qrqppllgdh paeyggphgg yhshyhdegy gpppphyegr rmgppvgghr rgpsrygpqy
      361 ghpppppppp dygphadspv lmvygldqsk mncdrvfnvf clygnvekvk fmkskpgaam
      421 vemadgyavd raithlnnnf mfgqkmnvcv skqpaimpgq sygledgscs ykdfsesrnn
      481 rfstpeqaak nriqhpsnvl hffnaplevt eenffeicde lgvkrptsvk vfsgkserss
      541 sgllewdsks daletlgfln hyqmknpngp ypytlklcfs taqhas
//
LOCUS       NP_112262                325 aa            linear   ROD 27-APR-2025
DEFINITION  aldo-keto reductase family 1 member A1 [Rattus norvegicus].
ACCESSION   NP_112262
VERSION     NP_112262.1
DBSOURCE    REFSEQ: accession NM_031000.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Zhou,H.L., Zhang,R., Anand,P., Stomberski,C.T., Qian,Z.,
            Hausladen,A., Wang,L., Rhee,E.P., Parikh,S.M., Karumanchi,S.A. and
            Stamler,J.S.
  TITLE     Author Correction: Metabolic reprogramming by the S-nitroso-CoA
            reductase system protects against kidney injury
  JOURNAL   Nature 570 (7759), E23 (2019)
   PUBMED   31089212
  REMARK    Correction to:[Nature. 2019 Jan;565(7737):96-100. doi:
            10.1038/s41586-018-0749-z. PMID: 30487609]
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Liu,C., Li,Y., Wei,M., Zhao,L., Yu,Y. and Li,G.
  TITLE     Identification of a novel glycolysis-related gene signature that
            can predict the survival of patients with lung adenocarcinoma
  JOURNAL   Cell Cycle 18 (5), 568-579 (2019)
   PUBMED   30727821
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Homma,T., Shirato,T., Akihara,R., Kobayashi,S., Lee,J.,
            Yamada,K.I., Miyata,S., Takahashi,M. and Fujii,J.
  TITLE     Mice deficient in aldo-keto reductase 1a (Akr1a) are resistant to
            thioacetamide-induced liver injury
  JOURNAL   Toxicol Lett 294, 37-43 (2018)
   PUBMED   29763686
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hlavac,V., Brynychova,V., Vaclavikova,R., Ehrlichova,M., Vrana,D.,
            Pecha,V., Trnkova,M., Kodet,R., Mrhalova,M., Kubackova,K.,
            Gatek,J., Vazan,P. and Soucek,P.
  TITLE     The role of cytochromes p450 and aldo-keto reductases in prognosis
            of breast carcinoma patients
  JOURNAL   Medicine (Baltimore) 93 (28), e255 (2014)
   PUBMED   25526449
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Kurahashi,T., Kwon,M., Homma,T., Saito,Y., Lee,J., Takahashi,M.,
            Yamada,K., Miyata,S. and Fujii,J.
  TITLE     Reductive detoxification of acrolein as a potential role for
            aldehyde reductase (AKR1A) in mammals
  JOURNAL   Biochem Biophys Res Commun 452 (1), 136-141 (2014)
   PUBMED   25152401
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Crosas,B., Hyndman,D.J., Gallego,O., Martras,S., Pares,X.,
            Flynn,T.G. and Farres,J.
  TITLE     Human aldose reductase and human small intestine aldose reductase
            are efficient retinal reductases: consequences for retinoid
            metabolism
  JOURNAL   Biochem J 373 (Pt 3), 973-979 (2003)
   PUBMED   12732097
REFERENCE   7  (residues 1 to 325)
  AUTHORS   O'connor,T., Ireland,L.S., Harrison,D.J. and Hayes,J.D.
  TITLE     Major differences exist in the function and tissue-specific
            expression of human aflatoxin B1 aldehyde reductase and the
            principal human aldo-keto reductase AKR1 family members
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 487-504 (1999)
   PUBMED   10510318
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Suzuki,K., Koh,Y.H., Mizuno,H., Hamaoka,R. and Taniguchi,N.
  TITLE     Overexpression of aldehyde reductase protects PC12 cells from the
            cytotoxicity of methylglyoxal or 3-deoxyglucosone
  JOURNAL   J Biochem 123 (2), 353-357 (1998)
   PUBMED   9538214
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Barski,O.A., Gabbay,K.H., Grimshaw,C.E. and Bohren,K.M.
  TITLE     Mechanism of human aldehyde reductase: characterization of the
            active site pocket
  JOURNAL   Biochemistry 34 (35), 11264-11275 (1995)
   PUBMED   7669785
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Takahashi,M., Fujii,J., Teshima,T., Suzuki,K., Shiba,T. and
            Taniguchi,N.
  TITLE     Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde
            reductase in rat liver established by amino acid sequencing and
            cDNA expression
  JOURNAL   Gene 127 (2), 249-253 (1993)
   PUBMED   8500767
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D10854.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D10854.1, BC059133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132275, SAMD00132305
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Rattus norvegicus"
                     /strain="DONRYU"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..325
                     /product="aldo-keto reductase family 1 member A1"
                     /EC_number="1.1.1.2"
                     /EC_number="1.1.1.54"
                     /EC_number="1.1.1.19"
                     /EC_number="1.1.1.20"
                     /EC_number="1.1.1.372"
                     /note="alcohol dehydrogenase; aldehyde reductase;
                     3-DG-reducing enzyme; glucuronate reductase;
                     glucuronolactone reductase; scorR; S-nitroso-CoA
                     reductase"
                     /calculated_mol_wt=36375
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Region          8..312
                     /region_name="AKR_AKR1A1-4"
                     /note="AKR1A family of aldo-keto reductase (AKR); cd19106"
                     /db_xref="CDD:381332"
     Site            13
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            order(20..22,45,50,80,82,113..114,162..163,184,210..217,
                     246,261..266,269,273,301)
                     /site_type="active"
                     /db_xref="CDD:381332"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            30
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            34
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14550; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            order(45,50,80,113)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381332"
     Site            61
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            80
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250|UniProtKB:P14550; Not glycated.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            97
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JII6; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            127
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            134
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            145
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (Glc) (glycation) lysine.
                     /evidence=ECO:0000269|PubMed:7827091; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            157
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14550; propagated from
                     UniProtKB/Swiss-Prot (P51635.2)"
     Site            240
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            257
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            263
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            287
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            294
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     Site            308
                     /site_type="other"
                     /note="Not glycated. /evidence=ECO:0000269|PubMed:7827091;
                     propagated from UniProtKB/Swiss-Prot (P51635.2)"
     CDS             1..325
                     /gene="Akr1a1"
                     /gene_synonym="Akr1a4"
                     /coded_by="NM_031000.3:54..1031"
                     /db_xref="GeneID:78959"
                     /db_xref="RGD:68346"
ORIGIN      
        1 mtassvllht gqkmpliglg twksepgqvk aaikyalsvg yrhidcasvy gneteigeal
       61 kesvgagkav preelfvtsk lwntkhhped vepavrktla dlqleyldly lmhwpyafer
      121 gdnpfpknad gtvkydsthy ketwkaleal vakglvkalg lsnfssrqid dvlsvasvrp
      181 avlqvechpy laqneliahc qarglevtay splgssdraw rhpdepvlle epvvlalaek
      241 hgrspaqill rwqvqrkvic ipksitpsri lqniqvfdft fspeemkqld alnknwryiv
      301 pmitvdgkrv prdaghplyp fndpy
//
LOCUS       NP_001104527             677 aa            linear   ROD 27-APR-2025
DEFINITION  double-stranded RNA-specific editase 1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001104527
VERSION     NP_001104527.1
DBSOURCE    REFSEQ: accession NM_001111057.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Gurung,S., Evans,A.J., Wilkinson,K.A. and Henley,J.M.
  TITLE     ADAR2-mediated Q/R editing of GluK2 regulates kainate receptor
            upscaling in response to suppression of synaptic activity
  JOURNAL   J Cell Sci 131 (24) (2018)
   PUBMED   30559217
  REMARK    GeneRIF: that activity-dependent regulation of ADAR2 proteostasis
            and GluK2 Q/R editing are key determinants of kainate receptors
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Behm,M., Wahlstedt,H., Widmark,A., Eriksson,M. and Ohman,M.
  TITLE     Accumulation of nuclear ADAR2 regulates adenosine-to-inosine RNA
            editing during neuronal development
  JOURNAL   J Cell Sci 130 (4), 745-753 (2017)
   PUBMED   28082424
  REMARK    GeneRIF: lower levels of ADAR2 in the nucleus of immature neurons
            than in mature neurons.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Tariq,A., Garncarz,W., Handl,C., Balik,A., Pusch,O. and
            Jantsch,M.F.
  TITLE     RNA-interacting proteins act as site-specific repressors of
            ADAR2-mediated RNA editing and fluctuate upon neuronal stimulation
  JOURNAL   Nucleic Acids Res 41 (4), 2581-2593 (2013)
   PUBMED   23275536
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Yang,L., Huang,P., Li,F., Zhao,L., Zhang,Y., Li,S., Gan,Z., Lin,A.,
            Li,W. and Liu,Y.
  TITLE     c-Jun amino-terminal kinase-1 mediates glucose-responsive
            upregulation of the RNA editing enzyme ADAR2 in pancreatic
            beta-cells
  JOURNAL   PLoS One 7 (11), e48611 (2012)
   PUBMED   23139803
  REMARK    GeneRIF: The JNK1 pathway may be functionally linked to the
            nutrient-sensing actions of ADAR2-mediated RNA editing in
            professional secretory cells.
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Rueter,S.M., Dawson,T.R. and Emeson,R.B.
  TITLE     Regulation of alternative splicing by RNA editing
  JOURNAL   Nature 399 (6731), 75-80 (1999)
   PUBMED   10331393
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Belcher,S.M. and Howe,J.R.
  TITLE     Characterization of RNA editing of the glutamate-receptor subunits
            GluR5 and GluR6 in granule cells during cerebellar development
  JOURNAL   Brain Res Mol Brain Res 52 (1), 130-138 (1997)
   PUBMED   9450685
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Gerber,A., O'Connell,M.A. and Keller,W.
  TITLE     Two forms of human double-stranded RNA-specific editase 1 (hRED1)
            generated by the insertion of an Alu cassette
  JOURNAL   RNA 3 (5), 453-463 (1997)
   PUBMED   9149227
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Lai,F., Chen,C.X., Carter,K.C. and Nishikura,K.
  TITLE     Editing of glutamate receptor B subunit ion channel RNAs by four
            alternatively spliced DRADA2 double-stranded RNA adenosine
            deaminases
  JOURNAL   Mol Cell Biol 17 (5), 2413-2424 (1997)
   PUBMED   9111310
REFERENCE   9  (residues 1 to 677)
  AUTHORS   O'Connell,M.A., Gerber,A. and Keller,W.
  TITLE     Purification of human double-stranded RNA-specific editase 1
            (hRED1) involved in editing of brain glutamate receptor B pre-mRNA
  JOURNAL   J Biol Chem 272 (1), 473-478 (1997)
   PUBMED   8995285
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Melcher,T., Maas,S., Herb,A., Sprengel,R., Seeburg,P.H. and
            Higuchi,M.
  TITLE     A mammalian RNA editing enzyme
  JOURNAL   Nature 379 (6564), 460-464 (1996)
   PUBMED   8559253
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB576423.1, JAXUCZ010000020.1,
            U43534.1, CB556744.1, CB801553.1, BF388249.1 and CK840559.1.
            
            Summary: This gene encodes a double-stranded-RNA-specific adenosine
            deaminase that is involved in editing pre-mRNAs by site-specific
            conversion of adenosine (A) to inosine (I). Substrates for this
            enzyme include ionotropic glutamate receptors (GluR2-6) and
            serotonin receptor (5HT2C). Studies in rodents have shown that this
            protein can modify its own pre-mRNA by A->I editing to create a
            novel acceptor splice site, alternative splicing to which results
            in down regulation of its protein expression. Additional splicing
            events result in transcript variants encoding different isoforms.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4, also referred to as 2e)
            results from an auto RNA editing event (AA->AI) in the intronic
            sequence that creates a novel acceptor splice site, splicing to
            which inserts 47 nt into the coding region causing a frame-shift,
            compared to transcript variant 2. Translation initiation from the
            upstream AUG will result in a very short protein of 82 aa. However,
            studies reported in PMID:10331393 show that leaky translation
            initiation from an in-frame, downstream AUG allows some protein
            expression, and that this isoform (3) exhibits RNA editing
            activity. Isoform 4 is 24 aa shorter at the N-terminus compared to
            isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of the transcript and
            the encoded protein are supported by transcript alignment and
            PMID:10331393.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR26643299.66281.1, SRR26360186.1728957.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 10331393
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..677
                     /product="double-stranded RNA-specific editase 1 isoform
                     4"
                     /EC_number="3.5.4.37"
                     /note="RNA-editing enzyme 1; double-stranded RNA-specific
                     editase 1; dsRNA adenosine deaminase; RNA-editing
                     deaminase 1; RNA editing deaminase of glutamate receptors;
                     double stranded RNA specific deaminase RED1"
                     /calculated_mol_wt=73989
     Region          51..122
                     /region_name="DSRM_RED1_rpt1"
                     /note="first double-stranded RNA binding motif of
                     RNA-editing deaminase 1 (RED1) and similar proteins;
                     cd19895"
                     /db_xref="CDD:380724"
     Site            order(56,59..60,63..64,66,80..81,83,85,102..104,107)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380724"
     Region          208..277
                     /region_name="DSRM_RED1_rpt2"
                     /note="second double-stranded RNA binding motif of
                     RNA-editing deaminase 1 (RED1) and similar proteins;
                     cd19898"
                     /db_xref="CDD:380727"
     Site            order(211,213..214,217..218,233..235,237,239,255..258,261)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380727"
     Region          298..674
                     /region_name="ADEAMc"
                     /note="tRNA-specific and double-stranded RNA adenosine
                     deaminase (RNA-specific editase); smart00552"
                     /db_xref="CDD:214718"
     CDS             1..677
                     /gene="Adarb1"
                     /gene_synonym="Adar2; Red1"
                     /coded_by="NM_001111057.1:492..2525"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:25367"
                     /db_xref="RGD:2033"
ORIGIN      
        1 mppkdsstpg pgegiplsng gggstsrkrp leegsnghsk yrlkkrrktp gpvlpknalm
       61 qlneikpglq ymllsqtgpv haplfvmsve vngqvfegsg ptkkkaklha aekalrsfvq
      121 fpnaseahla mgrtlsvntd ftsdqadfpd tlfngfetpd kseppfyvgs ngddsfsssg
      181 dvslsaspvp asltqpplpi pppfpppsgk npvmilnelr pglkydflse sgeshaksfv
      241 msvvvdgqff egsgrnkkla karaaqsala tvfnlhldqt psrqpvlseg lqlhlpqvla
      301 davsrlvlgk fsdltdnfss pharrkvlsg vvmttgtdvk dakvisvstg tkcingeyms
      361 drglalndch aeiisrrsll rflyaqlely lnnkedqkks ifqkserggf rlkdtvqfhl
      421 yistspcgda rifsphepvl eepadrhpnr kargqlrtki esgegtipvr snasiqtwdg
      481 vlqgerlltm scsdkiarwn vvgiqgalls ifvepiyfss iilgslyhgd hlsramyqri
      541 sniedlpply tlnkpllsgi snaearqpgk apnfsvnwtv gdtaievina ttgkdelgrp
      601 srlckhalyc rwmrvhgkvp phllrtkitk pttyheskla akeyqaakar lftafikagl
      661 gawvekpteq dqfsftp
//
LOCUS       NP_001032362             415 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein F [Rattus norvegicus].
ACCESSION   NP_001032362
VERSION     NP_001032362.1
DBSOURCE    REFSEQ: accession NM_001037285.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Lo,C.S., Shi,Y., Chenier,I., Ghosh,A., Wu,C.H., Cailhier,J.F.,
            Ethier,J., Lattouf,J.B., Filep,J.G., Ingelfinger,J.R., Zhang,S.L.
            and Chan,J.S.D.
  TITLE     Heterogeneous Nuclear Ribonucleoprotein F Stimulates Sirtuin-1 Gene
            Expression and Attenuates Nephropathy Progression in Diabetic Mice
  JOURNAL   Diabetes 66 (7), 1964-1978 (2017)
   PUBMED   28424160
  REMARK    GeneRIF: hnRNP F protects kidneys against oxidative stress and
            nephropathy via stimulation of Sirtuin-1 expression and signaling
            in diabetes.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Dominguez,C., Fisette,J.F., Chabot,B. and Allain,F.H.
  TITLE     Structural basis of G-tract recognition and encaging by hnRNP F
            quasi-RRMs
  JOURNAL   Nat Struct Mol Biol 17 (7), 853-861 (2010)
   PUBMED   20526337
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Wei,C.C., Zhang,S.L., Chen,Y.W., Guo,D.F., Ingelfinger,J.R.,
            Bomsztyk,K. and Chan,J.S.
  TITLE     Heterogeneous nuclear ribonucleoprotein K modulates angiotensinogen
            gene expression in kidney cells
  JOURNAL   J Biol Chem 281 (35), 25344-25355 (2006)
   PUBMED   16837467
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Wei,C.C., Guo,D.F., Zhang,S.L., Ingelfinger,J.R. and Chan,J.S.
  TITLE     Heterogenous nuclear ribonucleoprotein F modulates angiotensinogen
            gene expression in rat kidney proximal tubular cells
  JOURNAL   J Am Soc Nephrol 16 (3), 616-628 (2005)
   PUBMED   15659559
  REMARK    GeneRIF: hnRNP F binds to rANG-IRE and modulates renal ANG gene
            expression, implicating that dysregulation of hnRNP F might affect
            renin-angiotensin system activation and, subsequently, kidney
            injury in diabetes
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Yoshida,T., Makino,Y. and Tamura,T.
  TITLE     Association of the rat heterogeneous nuclear RNA-ribonucleoprotein
            F with TATA-binding protein
  JOURNAL   FEBS Lett 457 (2), 251-254 (1999)
   PUBMED   10471789
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Gamberi,C., Izaurralde,E., Beisel,C. and Mattaj,I.W.
  TITLE     Interaction between the human nuclear cap-binding protein complex
            and hnRNP F
  JOURNAL   Mol Cell Biol 17 (5), 2587-2597 (1997)
   PUBMED   9111328
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK473366.1 and BC103634.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF553584.1, CK473366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..415
                     /product="heterogeneous nuclear ribonucleoprotein F"
                     /note="hnRNP F; ribonucleoprotein F"
                     /calculated_mol_wt=45599
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Heterogeneous nuclear
                     ribonucleoprotein F, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          10..88
                     /region_name="RRM1_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12729"
                     /db_xref="CDD:410128"
     Site            16
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            20
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            52
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            75
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          81..86
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          103..192
                     /region_name="RRM2_hnRNPH_hnRNPH2_hnRNPF"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H, hnRNP H2,
                     hnRNP F and similar proteins; cd12731"
                     /db_xref="CDD:410130"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            116
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            120
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            150
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            173
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          179..184
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X1; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          255..290
                     /region_name="zf-RNPHF"
                     /note="RNPHF zinc finger; pfam08080"
                     /db_xref="CDD:429823"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52597; propagated from
                     UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          289..363
                     /region_name="RRM3_hnRNPH_CRSF1_like"
                     /note="RNA recognition motif 3 (RRM3) found in
                     heterogeneous nuclear ribonucleoprotein hnRNP H protein
                     family, G-rich sequence factor 1 (GRSF-1) and similar
                     proteins; cd12506"
                     /db_xref="CDD:409929"
     Site            294
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            298
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            326
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Site            349
                     /site_type="other"
                     /note="Interaction with RNA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     Region          355..360
                     /region_name="Interaction with RNA. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q794E4.3)"
     CDS             1..415
                     /gene="Hnrnpf"
                     /gene_synonym="Hnrpf"
                     /coded_by="NM_001037285.1:323..1570"
                     /db_xref="GeneID:64200"
                     /db_xref="RGD:620366"
ORIGIN      
        1 mmlgpeggeg yvvklrglpw scsiedvqnf lsdctihdgv agvhfiytre grqsgeafve
       61 leseddvkla lkkdresmgh ryievfkshr temdwvlkhs gpnsadsand gfvrlrglpf
      121 gctkeeivqf fsgleivpng itlpvdpegk itgeafvqfa sqelaekalg khkerighry
      181 ievfkssqee vrsysdpplk fmsvqrpgpy drpgtarryi givkqagldr mrsgaysagy
      241 ggyeeysgls dgygfttdlf grdlsyclsg mydhrygdse ftvqsttghc vhmrglpyka
      301 tendiynffs plnpvrvhie igpdgrvtge advefathee avaamskdra nmqhryielf
      361 lnsttgasng ayssqvmqgm gvsaaqatys glesqsvsgc ygagysgqns mggyd
//
LOCUS       NP_062185                934 aa            linear   ROD 27-APR-2025
DEFINITION  inositol-trisphosphate 3-kinase B [Rattus norvegicus].
ACCESSION   NP_062185
VERSION     NP_062185.2
DBSOURCE    REFSEQ: accession NM_019312.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Jia,Y., Loison,F., Hattori,H., Li,Y., Erneux,C., Park,S.Y., Gao,C.,
            Chai,L., Silberstein,L.E., Schurmans,S. and Luo,H.R.
  TITLE     Inositol trisphosphate 3-kinase B (InsP3KB) as a physiological
            modulator of myelopoiesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (12), 4739-4744 (2008)
   PUBMED   18339802
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Yu,J.C., Lloyd-Burton,S.M., Irvine,R.F. and Schell,M.J.
  TITLE     Regulation of the localization and activity of inositol
            1,4,5-trisphosphate 3-kinase B in intact cells by proteolysis
  JOURNAL   Biochem J 392 (Pt 3), 435-441 (2005)
   PUBMED   16173920
  REMARK    GeneRIF: The localization and activity of inositol
            1,4,5-trisphosphate 3-kinase B(IP3KB) and its modulation by
            proteolysis are reported.
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Hascakova-Bartova,R., Pouillon,V., Dewaste,V., Moreau,C.,
            Jacques,C., Banting,G., Schurmans,S. and Erneux,C.
  TITLE     Identification and subcellular distribution of endogenous
            Ins(1,4,5)P(3) 3-kinase B in mouse tissues
  JOURNAL   Biochem Biophys Res Commun 323 (3), 920-925 (2004)
   PUBMED   15381088
REFERENCE   4  (residues 1 to 934)
  AUTHORS   Wen,B.G., Pletcher,M.T., Warashina,M., Choe,S.H., Ziaee,N.,
            Wiltshire,T., Sauer,K. and Cooke,M.P.
  TITLE     Inositol (1,4,5) trisphosphate 3 kinase B controls positive
            selection of T cells and modulates Erk activity
  JOURNAL   Proc Natl Acad Sci U S A 101 (15), 5604-5609 (2004)
   PUBMED   15064401
REFERENCE   5  (residues 1 to 934)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   6  (residues 1 to 934)
  AUTHORS   Pouillon,V., Hascakova-Bartova,R., Pajak,B., Adam,E., Bex,F.,
            Dewaste,V., Van Lint,C., Leo,O., Erneux,C. and Schurmans,S.
  TITLE     Inositol 1,3,4,5-tetrakisphosphate is essential for T lymphocyte
            development
  JOURNAL   Nat Immunol 4 (11), 1136-1143 (2003)
   PUBMED   14517551
REFERENCE   7  (residues 1 to 934)
  AUTHORS   Zou,Y., Millette,C.F. and Sperry,A.O.
  TITLE     KRP3A and KRP3B: candidate motors in spermatid maturation in the
            seminiferous epithelium
  JOURNAL   Biol Reprod 66 (3), 843-855 (2002)
   PUBMED   11870094
REFERENCE   8  (residues 1 to 934)
  AUTHORS   Thomas,S., Brake,B., Luzio,J.P., Stanley,K. and Banting,G.
  TITLE     Isolation and sequence of a full length cDNA encoding a novel rat
            inositol 1,4,5-trisphosphate 3-kinase
  JOURNAL   Biochim Biophys Acta 1220 (2), 219-222 (1994)
   PUBMED   8312366
REFERENCE   9  (residues 1 to 934)
  AUTHORS   Takazawa,K., Perret,J., Dumont,J.E. and Erneux,C.
  TITLE     Molecular cloning and expression of a new putative inositol
            1,4,5-trisphosphate 3-kinase isoenzyme
  JOURNAL   Biochem J 278 (Pt 3) (Pt 3), 883-886 (1991)
   PUBMED   1654894
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AA859368.1, BF418570.1, AJ242781.1 and BE113255.1.
            
            On Jan 10, 2008 this sequence version replaced NP_062185.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AJ242781.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5756307, SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..934
                     /product="inositol-trisphosphate 3-kinase B"
                     /EC_number="2.7.1.127"
                     /note="IP3K-B; IP3 3-kinase B; insP 3-kinase B; inositol
                     1,4,5-trisphosphate 3-kinase B"
                     /calculated_mol_wt=101689
     Region          20..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P42335.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P42335.3)"
     Region          58..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27987; propagated from
                     UniProtKB/Swiss-Prot (P42335.3)"
     Region          <161..307
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          161..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P42335.3)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P42335.3)"
     Region          364..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Region          522..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Region          568..626
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     Region          714..925
                     /region_name="IPK"
                     /note="Inositol polyphosphate kinase; pfam03770"
                     /db_xref="CDD:397715"
     Region          756..764
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42335.3)"
     CDS             1..934
                     /gene="Itpkb"
                     /gene_synonym="IP3K B"
                     /coded_by="NM_019312.2:495..3299"
                     /db_xref="GeneID:54260"
                     /db_xref="RGD:2932"
ORIGIN      
        1 mavycyalns lvimnstnel ksgsplpsgs etpqpsgraa lspgsvfspg rgasflfppa
       61 eslsleepgs aggwrsgrrr lnsssgsggg ssssnsssss gvgspswagr lrgdaqqvva
      121 trilsppgpe eaqrklrilq relqnvqvnq kvgmfeaqiq aqtsaiqapr sprlgrarsp
      181 spcpfrsssq ppervlapcs pseerrtksw geqctetpda nsrrrsrlst hpskdkegva
      241 pllgpasptr lgtqspstsv rmergspasp rcgsptpmei dkrtapsleh fgtsltlatk
      301 vaasaasagp hpghdsvlme adcelgamrp weahlerrgq flgretgsap epirthirep
      361 pgrvervhsv ggqgswtpev ikrpeegtvd aqsselsenp rwsrlpgdpg svgpekggsr
      421 ipgirgpqqt ldsmregssa lgllggsqaa qpgsmdvetg iscgrmlepl ppgevttnlk
      481 epqclpgdrm gmqpessivw psaveeapli wtcdtgiqlk gtwrsqdgda hpscqekspd
      541 qkdkacspsn ipaipaviit dmgaqedggl eeiqgsprgp lplrklssss asstgfsssy
      601 edseedissd pertldpnsa flhtldqqkp rvskswrkik nmvqwspfvm sfkkkypwiq
      661 laghagsfka aangrilkkh ceseqrcldr lmadvlrpfv payhgdvvkd gerynqmddl
      721 ladfdspcvm dckmgirtyl eeeltkarkk pslrkdmyqk mvevdpeapt eeekaqravt
      781 kprymqwret isstatlgfr iegikkedgs vnrdfkktkt reqvteafre ftkgnqnili
      841 ayrdrlkair etlevspffk chevigssll fihdkkeqak vwmidfgktt plpegqtlqh
      901 dvpwqegnre dgylsglnnl idiltemsqg splt
//
LOCUS       NP_597684               1259 aa            linear   ROD 27-APR-2025
DEFINITION  SH3 and multiple ankyrin repeat domains protein 2 isoform c [Rattus
            norvegicus].
ACCESSION   NP_597684 XP_219506
VERSION     NP_597684.1
DBSOURCE    REFSEQ: accession NM_133440.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1259)
  AUTHORS   Li,N., Ren,C., Li,S., Yu,W., Jin,K. and Ji,X.
  TITLE     Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway
  JOURNAL   Prog Neurobiol 230, 102514 (2023)
   PUBMED   37574039
  REMARK    GeneRIF: Remote ischemic conditioning alleviates chronic cerebral
            hypoperfusion-induced cognitive decline and synaptic dysfunction
            via the miR-218a-5p/SHANK2 pathway.
REFERENCE   2  (residues 1 to 1259)
  AUTHORS   Fu,Y., Liu,D., Guo,J., Long,H., Xiao,W., Xiao,W., Feng,L., Luo,Z.
            and Xiao,B.
  TITLE     Dynamic Change of Shanks Gene mRNA Expression and DNA Methylation
            in Epileptic Rat Model and Human Patients
  JOURNAL   Mol Neurobiol 57 (9), 3712-3726 (2020)
   PUBMED   32564287
  REMARK    GeneRIF: Dynamic Change of Shanks Gene mRNA Expression and DNA
            Methylation in Epileptic Rat Model and Human Patients.
REFERENCE   3  (residues 1 to 1259)
  AUTHORS   Ishida,H., Skorobogatov,A., Yamniuk,A.P. and Vogel,H.J.
  TITLE     Solution structures of the SH3 domains from Shank scaffold proteins
            and their interactions with Cav1.3 calcium channels
  JOURNAL   FEBS Lett 592 (16), 2786-2797 (2018)
   PUBMED   30058071
REFERENCE   4  (residues 1 to 1259)
  AUTHORS   Modi,M.E., Brooks,J.M., Guilmette,E.R., Beyna,M., Graf,R., Reim,D.,
            Schmeisser,M.J., Boeckers,T.M., O'Donnell,P. and Buhl,D.L.
  TITLE     Hyperactivity and Hypermotivation Associated With Increased
            Striatal mGluR1 Signaling in a Shank2 Rat Model of Autism
  JOURNAL   Front Mol Neurosci 11, 107 (2018)
   PUBMED   29970986
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1259)
  AUTHORS   Shi,R., Redman,P., Ghose,D., Hwang,H., Liu,Y., Ren,X., Ding,L.J.,
            Liu,M., Jones,K.J. and Xu,W.
  TITLE     Shank Proteins Differentially Regulate Synaptic Transmission
  JOURNAL   eNeuro 4 (6) (2017)
   PUBMED   29250591
  REMARK    GeneRIF: Loss of scaffold proteins via knockdown of Shank1 or
            Shank2, but not Shank3, led to a reduction of the number but not
            the unitary response of AMPAR-containing synapses. Only when both
            Shank1 and Shank2 were knocked down, were both the number and the
            unitary response of active synapses reduced. This reduction was
            accompanied by a decrease in NMDAR-mediated synaptic response.
            Erratum:[eNeuro. 2018 Mar 19;5(1):ENEURO.0073-18.2018. doi:
            10.1523/ENEURO.0073-18.2018. PMID: 29569864]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1259)
  AUTHORS   Boeckers,T.M., Winter,C., Smalla,K.H., Kreutz,M.R., Bockmann,J.,
            Seidenbecher,C., Garner,C.C. and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated proteins ProSAP1 and ProSAP2
            interact with synaptic proteins of the SAPAP/GKAP family
  JOURNAL   Biochem Biophys Res Commun 264 (1), 247-252 (1999)
   PUBMED   10527873
REFERENCE   7  (residues 1 to 1259)
  AUTHORS   Lim,S., Naisbitt,S., Yoon,J., Hwang,J.I., Suh,P.G., Sheng,M. and
            Kim,E.
  TITLE     Characterization of the Shank family of synaptic proteins. Multiple
            genes, alternative splicing, and differential expression in brain
            and development
  JOURNAL   J Biol Chem 274 (41), 29510-29518 (1999)
   PUBMED   10506216
REFERENCE   8  (residues 1 to 1259)
  AUTHORS   Boeckers,T.M., Kreutz,M.R., Winter,C., Zuschratter,W., Smalla,K.H.,
            Sanmarti-Vila,L., Wex,H., Langnaese,K., Bockmann,J., Garner,C.C.
            and Gundelfinger,E.D.
  TITLE     Proline-rich synapse-associated protein-1/cortactin binding protein
            1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the
            postsynaptic density
  JOURNAL   J Neurosci 19 (15), 6506-6518 (1999)
   PUBMED   10414979
REFERENCE   9  (residues 1 to 1259)
  AUTHORS   Zitzer,H., Richter,D. and Kreienkamp,H.J.
  TITLE     Agonist-dependent interaction of the rat somatostatin receptor
            subtype 2 with cortactin-binding protein 1
  JOURNAL   J Biol Chem 274 (26), 18153-18156 (1999)
   PUBMED   10373412
REFERENCE   10 (residues 1 to 1259)
  AUTHORS   Du,Y., Weed,S.A., Xiong,W.C., Marshall,T.D. and Parsons,J.T.
  TITLE     Identification of a novel cortactin SH3 domain-binding protein and
            its localization to growth cones of cultured neurons
  JOURNAL   Mol Cell Biol 18 (10), 5838-5851 (1998)
   PUBMED   9742101
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ131899.1.
            
            On Jan 25, 2004 this sequence version replaced XP_219506.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ131899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155310, SAMD00155311
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1259
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..1259
                     /product="SH3 and multiple ankyrin repeat domains protein
                     2 isoform c"
                     /note="SH3 and multiple ankyrin repeat domains protein 2;
                     GKAP/SAPAP-interacting protein; proline-rich
                     synapse-associated protein 1; cortactin-binding protein 1;
                     SH3 and multiple ankyrin repeat domains protein 2-like;
                     SH3/ankyrin domain gene 2"
                     /calculated_mol_wt=134963
     mat_peptide     1..1259
                     /product="SH3 and multiple ankyrin repeat domains protein
                     2 isoform c"
                     /note="alternative names: CortBP1 gene for cortactin
                     binding protein 1"
                     /calculated_mol_wt=135094
     Region          30..131
                     /region_name="PDZ_SHANK1_3-like"
                     /note="PDZ domain of SH3 and multiple ankyrin repeat
                     domains protein 1 (SHANK1), SHANK2, SHANK3, and related
                     domains; cd06746"
                     /db_xref="CDD:467228"
     Site            order(30..35,65..68,103,105,128)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467228"
     Site            order(47..53,77,80,109,113,116..117)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467228"
     Region          <478..887
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1192..1257
                     /region_name="SAM_Shank1,2,3"
                     /note="SAM domain of Shank1,2,3 family proteins; cd09506"
                     /db_xref="CDD:188905"
     Site            order(1195..1197,1199,1213..1214,1227)
                     /site_type="other"
                     /note="polymer interface (interfiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     Site            order(1212..1213,1245)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188905"
     Site            order(1236,1238,1243)
                     /site_type="other"
                     /note="polymer interface (intrafiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     CDS             1..1259
                     /gene="Shank2"
                     /gene_synonym="CortBP1; ProSAP1; Shank2E; Spank-3"
                     /coded_by="NM_133440.1:531..4310"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:171093"
                     /db_xref="RGD:628772"
ORIGIN      
        1 mmsvpgggaa tvmmtgynng ryprnslysd ciiedktvvl qkkdnegfgf vlrgakadtp
       61 ieeftptpaf palqylesvd eggvawqagl rtgdflievn nenvvkvghr qvvnmirqgg
      121 nhlvlkvvtv trnldpddta rkkappppkr apttaltlrs ksmtaeleel vdkasvrkkk
      181 dkpeeivpas kpsrtaenva iesrvatikq rptsrcfpaa sdvnsvyerq giavmtptvp
      241 gspkgpflgl prgtmrrqks idsriflsgi teeerqflap pmlkftrsls mpdtsedipp
      301 ppqsvppspp ppspttyncp rsptprvygt ikpafnqnpv akvppatrsd tvatmmrekg
      361 mfyrreldrf sldsedvysr spapqaafrt krgqmpenpy sevgkiaska vyvpakparr
      421 kgmlvkqsnv edspektcsi piptiivkep stsssgkssq gssmeidpqa tepgqlrpdd
      481 sltvsspfaa aiagavrdre krlearrnsp aflstdlgde dvglgppapr mqpskfpeeg
      541 gfgdedeteq pllptpgaap relenhflgg geagaqgeag gplsstskak gpesgpaaal
      601 kssspaspen yvhpltgrll dpssplalal sardramqes qqghkgeapk adlnkplyid
      661 tkmrpsvesg fppvtrqntr gplrrqeten kyetdlskdr raddkknmli nivdtaqqks
      721 agllmvhtvd ipvagpplee eedredgdtk pdhspstvpe gvpktegalq isaapepaaa
      781 pgrtivaags veeavilpfr ipppplasvd ldedflftep lppplefans fdipddraas
      841 vpaladlvkq kksdtpqpps lnssqpanst dskkpagisn clpssflppp esfdavtdsg
      901 ieevdsrsss dhhlettsti stvssistls seggesmdtc tvyadgqafv vdkppvppkp
      961 kmkpivhksn alyqdtlpee dtdgfvippp apppppgsaq agvakviqpr tsklwgdvte
     1021 vkspilsgpk anviselnsi lqqmnrgksv kpgeglelpv gaksanlapr spevmstvsg
     1081 trsttvtftv rpgtsqpitl qsrppdyesr tsgprrapsp vvsptelske ilptppsaaa
     1141 aspsptlsdv fslpsqspag dlfglnpagr srspspsilq qpisnkpftt kpvhlwtkpd
     1201 vadwleslnl gehketfmdn eidgshlpnl qkedlidlgv trvghrmnie ralkqlldr
//
LOCUS       NP_073635                477 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM17 [Rattus norvegicus].
ACCESSION   NP_073635
VERSION     NP_073635.1
DBSOURCE    REFSEQ: accession NM_022798.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Mandell,M.A., Jain,A., Arko-Mensah,J., Chauhan,S., Kimura,T.,
            Dinkins,C., Silvestri,G., Munch,J., Kirchhoff,F., Simonsen,A.,
            Wei,Y., Levine,B., Johansen,T. and Deretic,V.
  TITLE     TRIM proteins regulate autophagy and can target autophagic
            substrates by direct recognition
  JOURNAL   Dev Cell 30 (4), 394-409 (2014)
   PUBMED   25127057
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Urano,T., Usui,T., Takeda,S., Ikeda,K., Okada,A., Ishida,Y.,
            Iwayanagi,T., Otomo,J., Ouchi,Y. and Inoue,S.
  TITLE     TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3
            ligase
  JOURNAL   Biochem Biophys Res Commun 383 (2), 263-268 (2009)
   PUBMED   19358823
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Ogawa,S., Goto,W., Orimo,A., Hosoi,T., Ouchi,Y., Muramatsu,M. and
            Inoue,S.
  TITLE     Molecular cloning of a novel RING finger-B box-coiled coil (RBCC)
            protein, terf, expressed in the testis
  JOURNAL   Biochem Biophys Res Commun 251 (2), 515-519 (1998)
   PUBMED   9792805
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078819.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078819.1, AF156272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..477
                     /product="E3 ubiquitin-protein ligase TRIM17"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 17; testis RING finger
                     protein; tripartite motif-containing protein 17; RING
                     finger protein terf; ring finger protein 16; RING-type E3
                     ubiquitin transferase TRIM17"
                     /calculated_mol_wt=54823
     Region          9..78
                     /region_name="RING-HC_TRIM17_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein TRIM17 and similar proteins;
                     cd16595"
                     /db_xref="CDD:438257"
     Region          <64..262
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          98..139
                     /region_name="Bbox2_TRIM7-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM7, TRIM27 and similar
                     proteins; cd19762"
                     /db_xref="CDD:380820"
     Region          296..472
                     /region_name="SPRY_PRY_TRIM17"
                     /note="PRY/SPRY domain of tripartite motif-binding protein
                     17 (TRIM17), also known as testis RING finger protein
                     (terf); cd15812"
                     /db_xref="CDD:293984"
     CDS             1..477
                     /gene="Trim17"
                     /gene_synonym="Rnf16"
                     /coded_by="NM_022798.2:58..1491"
                     /db_xref="GeneID:64702"
                     /db_xref="RGD:69290"
ORIGIN      
        1 mdavelarrl qeeatcsicl dyftdpvmta cghnfcreci qmswekgkgk kgkkkqkgsf
       61 pcpecremsp qrnlrpnrll tkvaemarqh pglhkrdlcq ihqeplklfc qddqtpicvv
      121 creaqehrmh rvlpldeaar eyklrleedi kylreemmkt etlqakeeqt ltewqervke
      181 rrerileefq kvvlflveee rrllqilkke eddtlgklqd skasldhqsr sldlillqle
      241 eqtqqeplqm lqdvkdtltr keslsmqype vvlpvaiktv crvpgqievl ksfqedvvpd
      301 pstaypylll yesrqrryls pppegsapys kdrflaypca vgqksfssgr hywevgmnlt
      361 gdalwalgvc rdnvsrkdrv lkspengfwv vqlskgkkhl pllpnsipvt lteppshmgi
      421 fldfqagevs fysvndgshl hsfsqvafpg pllpffclgs pksgqmvist vtmwvkg
//
LOCUS       NP_071886                504 aa            linear   ROD 27-APR-2025
DEFINITION  activin receptor type-1-like precursor [Rattus norvegicus].
ACCESSION   NP_071886
VERSION     NP_071886.1
DBSOURCE    REFSEQ: accession NM_022441.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Li,Q., Zhou,X. and Zhou,X.
  TITLE     Downregulation of miR-98 contributes to hypoxic pulmonary
            hypertension by targeting ALK1
  JOURNAL   Mol Med Rep 20 (3), 2167-2176 (2019)
   PUBMED   31322216
  REMARK    GeneRIF: These results provided clear evidence that miR98 was a
            direct regulator of ALK1, and that the downregulation of miR98
            contributed to the pathogenesis of hypoxic pulmonary hypertension.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Abdullahi,W., Brzica,H., Hirsch,N.A., Reilly,B.G. and
            Ronaldson,P.T.
  TITLE     Functional Expression of Organic Anion Transporting Polypeptide 1a4
            Is Regulated by Transforming Growth Factor-beta/Activin
            Receptor-like Kinase 1 Signaling at the Blood-Brain Barrier
  JOURNAL   Mol Pharmacol 94 (6), 1321-1333 (2018)
   PUBMED   30262595
  REMARK    GeneRIF: Oatp1a4 transport activity at the BBB is directly
            regulated by TGF-beta/ALK1 signaling.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Hofmann,A.D., Zimmer,J., Takahashi,T., Gosemann,J.H. and Puri,P.
  TITLE     The Role of Activin Receptor-Like Kinase 1 Signaling in the
            Pulmonary Vasculature of Experimental Diaphragmatic Hernia
  JOURNAL   Eur J Pediatr Surg 26 (1), 106-111 (2016)
   PUBMED   26540443
  REMARK    GeneRIF: Increased expression of ALK-1 in the pulmonary vasculature
            of congenital diaphragmatic hernia (CDH) suggest that ALK-1 may
            play a crucial role in the molecular pathogenesis of vascular
            remodeling in CDH.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Alaa El Din,F., Patri,S., Thoreau,V., Rodriguez-Ballesteros,M.,
            Hamade,E., Bailly,S., Gilbert-Dussardier,B., Abou Merhi,R. and
            Kitzis,A.
  TITLE     Functional and splicing defect analysis of 23 ACVRL1 mutations in a
            cohort of patients affected by Hereditary Hemorrhagic
            Telangiectasia
  JOURNAL   PLoS One 10 (7), e0132111 (2015)
   PUBMED   26176610
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Sanz-Ramos,P., Dotor,J. and Izal-Azcarate,I.
  TITLE     The role of Alk-1 and Alk-5 in the mechanosensing of chondrocytes
  JOURNAL   Cell Mol Biol Lett 19 (4), 659-674 (2014)
   PUBMED   25424912
  REMARK    GeneRIF: Overexpression of Alk-5 and silencing of Alk-1 led to a
            loss of the chondrocyte phenotype, proving that they are key
            regulators of chondrocyte mechanosensing.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Pangas,S.A. and Woodruff,T.K.
  TITLE     Activin signal transduction pathways
  JOURNAL   Trends Endocrinol Metab 11 (8), 309-314 (2000)
   PUBMED   10996525
  REMARK    Review article
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Oh,S.P., Seki,T., Goss,K.A., Imamura,T., Yi,Y., Donahoe,P.K.,
            Li,L., Miyazono,K., ten Dijke,P., Kim,S. and Li,E.
  TITLE     Activin receptor-like kinase 1 modulates transforming growth
            factor-beta 1 signaling in the regulation of angiogenesis
  JOURNAL   Proc Natl Acad Sci U S A 97 (6), 2626-2631 (2000)
   PUBMED   10716993
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Panchenko,M.P., Williams,M.C., Brody,J.S. and Yu,Q.
  TITLE     Type I receptor serine-threonine kinase preferentially expressed in
            pulmonary blood vessels
  JOURNAL   Am J Physiol 270 (4 Pt 1), L547-L558 (1996)
   PUBMED   8928814
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Attisano,L., Carcamo,J., Ventura,F., Weis,F.M., Massague,J. and
            Wrana,J.L.
  TITLE     Identification of human activin and TGF beta type I receptors that
            form heteromeric kinase complexes with type II receptors
  JOURNAL   Cell 75 (4), 671-680 (1993)
   PUBMED   8242742
REFERENCE   10 (residues 1 to 504)
  AUTHORS   He,W.W., Gustafson,M.L., Hirobe,S. and Donahoe,P.K.
  TITLE     Developmental expression of four novel serine/threonine kinase
            receptors homologous to the activin/transforming growth factor-beta
            type II receptor family
  JOURNAL   Dev Dyn 196 (2), 133-142 (1993)
   PUBMED   8395914
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083173.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083173.1, L36088.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..504
                     /product="activin receptor type-1-like precursor"
                     /EC_number="2.7.11.30"
                     /note="serine/threonine-protein kinase receptor R3; SKR3;
                     TSR-I; TGF-B superfamily receptor type I; Activin receptor
                     like kinase 1; activin A receptor type II-like 1; activin
                     A receptor type IL; activin receptor type-1-like"
                     /calculated_mol_wt=54483
     sig_peptide     1..20
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
                     /calculated_mol_wt=2239
     mat_peptide     21..504
                     /product="Activin receptor type-1-like.
                     /id=PRO_0000024422"
                     /note="propagated from UniProtKB/Swiss-Prot (P80203.2)"
                     /calculated_mol_wt=54483
     Region          30..99
                     /region_name="TFP_LU_ECD_ALK1"
                     /note="extracellular domain (ECD) found in activin
                     receptor-like kinase 1 (ALK-1) and similar proteins;
                     cd23534"
                     /db_xref="CDD:467064"
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
     Region          74..77
                     /region_name="Mediates specificity for BMP ligand.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P80203.2)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P80203.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P80203.2)"
     Region          175..201
                     /region_name="TGF_beta_GS"
                     /note="Transforming growth factor beta type I GS-motif;
                     pfam08515"
                     /db_xref="CDD:462503"
     Region          197..494
                     /region_name="STKc_ACVR1_ALK1"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Activin Type I Receptor and Activin receptor-Like Kinase
                     1; cd14142"
                     /db_xref="CDD:271044"
     Site            order(197..198,201..202,240..241,244..245,248..249,263,
                     265)
                     /site_type="other"
                     /note="FKBP12 binding site [polypeptide binding]"
                     /db_xref="CDD:271044"
     Site            order(209..213,217,228,230,258,278..281,285,287,331,333,
                     335..336,338,349,352,372..375)
                     /site_type="active"
                     /db_xref="CDD:271044"
     Site            order(209..215,217,228,230,278..279,281,285,335..336,338,
                     349)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271044"
     Site            order(213,285,287,331,333,335,352,372..375)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271044"
     Site            348..375
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271044"
     CDS             1..504
                     /gene="Acvrl1"
                     /gene_synonym="Alk1; R-3; R3; SETHKIR"
                     /coded_by="NM_022441.2:142..1656"
                     /db_xref="GeneID:25237"
                     /db_xref="RGD:2029"
ORIGIN      
        1 mtlgifrrvf lmlsvalglt kgdlvkpsrg qlvnctcenp hckrpicqga wctvvlvreq
       61 grhpqvyrgc gslnqelclg rptefvnhhc cyrsfcnhnv slmleatqtp seepevdahl
      121 plilgpvlal lvlvalgtlg lwrvrrrqek qrglhsdlge sslilkaseq gdsmlgdflv
      181 sdcttgsgsg lpflvqrtva rqvalvecvg kgrygevwrg swhgesvavk ifssrdeqsw
      241 freteiyntv llrhdnilgf iasdmtsrns stqlwlithy hehgslydfl qrqtlepqla
      301 lrlavsaacg lahlhveifg tqgkpaiahr dlksrnvlvk snlqcciadl glavmhsqss
      361 dyldignnpr vgtkrymape vldeqirtdc fesykwtdiw afglvlweia rrtiingive
      421 dyrppfydmv pndpsfedmk kvvcvdqqtp tipnrlaadp vlsglaqmmr ecwypnpsar
      481 ltalrikktl qklsqnpekp kvih
//
LOCUS       NP_001007664             515 aa            linear   ROD 27-APR-2025
DEFINITION  integrator complex subunit 14 [Rattus norvegicus].
ACCESSION   NP_001007664 XP_217173
VERSION     NP_001007664.1
DBSOURCE    REFSEQ: accession NM_001007663.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082006.1.
            
            On Nov 29, 2004 this sequence version replaced XP_217173.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082006.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..515
                     /product="integrator complex subunit 14"
                     /note="UPF0464 protein C15orf44 homolog; von Willebrand
                     factor A domain-containing protein 9; von Willebrand
                     factor A domain containing 9"
                     /calculated_mol_wt=57013
     Region          3..114
                     /region_name="VWA_2"
                     /note="von Willebrand factor type A domain; pfam13519"
                     /db_xref="CDD:463909"
     Region          209..356
                     /region_name="IntS14_b-barrel"
                     /note="Integrator complex subunit 14, beta-barrel domain;
                     pfam19435"
                     /db_xref="CDD:466081"
     Region          405..509
                     /region_name="IntS14_C"
                     /note="Integrator complex subunit 14, alpha-helical
                     domain; pfam20504"
                     /db_xref="CDD:466653"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96SY0; propagated from
                     UniProtKB/Swiss-Prot (Q66H58.1)"
     CDS             1..515
                     /gene="Ints14"
                     /gene_synonym="RGD1359616; Vwa9"
                     /coded_by="NM_001007663.1:364..1911"
                     /db_xref="GeneID:300782"
                     /db_xref="RGD:1359616"
ORIGIN      
        1 mptvvvmdvs lsmtrpvsve gseeyqrkhl aahgltmlfe hmatnyklef talvvfsslw
       61 elmvpftrdy ntlqealsnm ddydktcles alvgvcnivq qewggaipcq vvlvtdgclg
      121 igrgslrhsl atqnqrsess rfplpfpfps klyvmcmanl eelqstdsle clerlidlnn
      181 gegqiftidg plclknvqsm fgklidlayt pfhaalkcgh ltadvqvfpr pepfvideei
      241 dpipkvintd leivgfidia dissppvlsr hlvlpialnk egdevgagit ddnedensan
      301 qiagkipnfc vllhgslkve gmvalvqlgp ewhgmlysqa dskkksnlmm slfepgpepl
      361 pwlgkmaqlg pisdakenpy geddnkspfp lqpknkrsya qnvtvwikps glqtdvqkil
      421 rnarklpekt qtfykelnrl rkaalafgfl dllkgvadml erectllpdt ahpdaafqlt
      481 haaqqlklas teyavydlni tplhtdfsgs sterm
//
LOCUS       NP_001032753             352 aa            linear   ROD 27-APR-2025
DEFINITION  dysbindin [Rattus norvegicus].
ACCESSION   NP_001032753
VERSION     NP_001032753.1
DBSOURCE    REFSEQ: accession NM_001037664.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Gokhale,A., Hartwig,C., Freeman,A.H., Das,R., Zlatic,S.A.,
            Vistein,R., Burch,A., Carrot,G., Lewis,A.F., Nelms,S.,
            Dickman,D.K., Puthenveedu,M.A., Cox,D.N. and Faundez,V.
  TITLE     The Proteome of BLOC-1 Genetic Defects Identifies the Arp2/3 Actin
            Polymerization Complex to Function Downstream of the Schizophrenia
            Susceptibility Factor Dysbindin at the Synapse
  JOURNAL   J Neurosci 36 (49), 12393-12411 (2016)
   PUBMED   27927957
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Jia,J.M., Hu,Z., Nordman,J. and Li,Z.
  TITLE     The schizophrenia susceptibility gene dysbindin regulates dendritic
            spine dynamics
  JOURNAL   J Neurosci 34 (41), 13725-13736 (2014)
   PUBMED   25297099
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Rangrez,A.Y., Bernt,A., Poyanmehr,R., Harazin,V., Boomgaarden,I.,
            Kuhn,C., Rohrbeck,A., Frank,D. and Frey,N.
  TITLE     Dysbindin is a potent inducer of RhoA-SRF-mediated cardiomyocyte
            hypertrophy
  JOURNAL   J Cell Biol 203 (4), 643-656 (2013)
   PUBMED   24385487
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Matteucci,A., Gaddini,L., Macchia,G., Varano,M., Petrucci,T.C.,
            Macioce,P., Malchiodi-Albedi,F. and Ceccarini,M.
  TITLE     Developmental expression of dysbindin in Muller cells of rat retina
  JOURNAL   Exp Eye Res 116, 1-8 (2013)
   PUBMED   23954924
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Zhang,Y., Xu,Y., Zhu,Q., Zhao,F., Luo,J., Zhang,X. and Wang,X.
  TITLE     Upregulation of dysbindin in temporal lobe epileptic foci of human
            and experimental animals
  JOURNAL   Synapse 66 (7), 622-629 (2012)
   PUBMED   22337344
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Benson,M.A., Tinsley,C.L. and Blake,D.J.
  TITLE     Myospryn is a novel binding partner for dysbindin in muscle
  JOURNAL   J Biol Chem 279 (11), 10450-10458 (2004)
   PUBMED   14688250
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Li,W., Zhang,Q., Oiso,N., Novak,E.K., Gautam,R., O'Brien,E.P.,
            Tinsley,C.L., Blake,D.J., Spritz,R.A., Copeland,N.G., Jenkins,N.A.,
            Amato,D., Roe,B.A., Starcevic,M., Dell'Angelica,E.C., Elliott,R.W.,
            Mishra,V., Kingsmore,S.F., Paylor,R.E. and Swank,R.T.
  TITLE     Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
            dysbindin, a member of the biogenesis of lysosome-related
            organelles complex 1 (BLOC-1)
  JOURNAL   Nat Genet 35 (1), 84-89 (2003)
   PUBMED   12923531
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Schwab,S.G., Knapp,M., Mondabon,S., Hallmayer,J.,
            Borrmann-Hassenbach,M., Albus,M., Lerer,B., Rietschel,M.,
            Trixler,M., Maier,W. and Wildenauer,D.B.
  TITLE     Support for association of schizophrenia with genetic variation in
            the 6p22.3 gene, dysbindin, in sib-pair families with linkage and
            in an additional sample of triad families
  JOURNAL   Am J Hum Genet 72 (1), 185-190 (2003)
   PUBMED   12474144
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Benson,M.A., Newey,S.E., Martin-Rendon,E., Hawkes,R. and Blake,D.J.
  TITLE     Dysbindin, a novel coiled-coil-containing protein that interacts
            with the dystrobrevins in muscle and brain
  JOURNAL   J Biol Chem 276 (26), 24232-24241 (2001)
   PUBMED   11316798
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Swank,R.T., Sweet,H.O., Davisson,M.T., Reddington,M. and Novak,E.K.
  TITLE     Sandy: a new mouse model for platelet storage pool deficiency
  JOURNAL   Genet Res 58 (1), 51-62 (1991)
   PUBMED   1936982
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088267.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088267.1, SRR8487230.73011.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..352
                     /product="dysbindin"
                     /note="dysbindin-1; BLOC-1 subunit 8; biogenesis of
                     lysosome-related organelles complex 1 subunit 8;
                     distrobrevin binding protein 1"
                     /calculated_mol_wt=39611
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EV8; propagated from
                     UniProtKB/Swiss-Prot (Q5M834.1)"
     Region          175..315
                     /region_name="Dysbindin"
                     /note="Dysbindin (Dystrobrevin binding protein 1);
                     pfam04440"
                     /db_xref="CDD:461312"
     Region          243..256
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M834.1)"
     Region          267..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M834.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WZ8; propagated from
                     UniProtKB/Swiss-Prot (Q5M834.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91WZ8; propagated from
                     UniProtKB/Swiss-Prot (Q5M834.1)"
     CDS             1..352
                     /gene="Dtnbp1"
                     /coded_by="NM_001037664.1:111..1169"
                     /db_xref="GeneID:641528"
                     /db_xref="RGD:1590759"
ORIGIN      
        1 mletlrerll svqqdftsgl ktlsdkskea kvksrprtap ylpkysagld llsryedtwa
       61 alhrrakeca dagelvdsev vmlsahwekk rtslaelqeq lqqlpallqd veslmaslah
      121 letsfeeven hllhledlcg qcelerhkqa harhledykk skrkeleafk aeldtehaqk
      181 ilemehtqql klkerqkffe eafqqdmeqy lstghlqiae rrepmgsmss mevnvdvleq
      241 mdlmdlsdqe aldvflnsgg edntvispgl emesnpsqne mnlqipnpse sasqppasps
      301 actdldtada pliqadeeev qvdtalvtln tdrkstpgvs ddsdqcdstq di
//
LOCUS       NP_062109                157 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor HES-2 [Rattus norvegicus].
ACCESSION   NP_062109
VERSION     NP_062109.1
DBSOURCE    REFSEQ: accession NM_019236.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Kobayashi,T., Terada,Y., Kuwana,H., Tanaka,H., Okado,T.,
            Kuwahara,M., Tohda,S., Sakano,S. and Sasaki,S.
  TITLE     Expression and function of the Delta-1/Notch-2/Hes-1 pathway during
            experimental acute kidney injury
  JOURNAL   Kidney Int 73 (11), 1240-1250 (2008)
   PUBMED   18418349
  REMARK    GeneRIF: Delta-1/Notch-2/Hes-1 signaling pathway may regulate the
            regeneration and proliferation of renal tubules during acute kidney
            injury.
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Ishibashi,M., Sasai,Y., Nakanishi,S. and Kageyama,R.
  TITLE     Molecular characterization of HES-2, a mammalian helix-loop-helix
            factor structurally related to Drosophila hairy and Enhancer of
            split
  JOURNAL   Eur J Biochem 215 (3), 645-652 (1993)
   PUBMED   8354270
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D14029.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D14029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..157
                     /product="transcription factor HES-2"
                     /note="hairy and enhancer of split 2"
                     /calculated_mol_wt=16897
     Region          10..73
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     Site            order(22..23,25,30,55..56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381392"
     Site            order(28..29,32..33,35..36,40,56..57,60..61,64,66..67,
                     70..71)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381392"
     Region          84..128
                     /region_name="ORANGE"
                     /note="Orange domain; smart00511"
                     /db_xref="CDD:128787"
     Region          124..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35429.1)"
     Region          154..157
                     /region_name="WRPW motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P35429.1)"
     CDS             1..157
                     /gene="Hes2"
                     /coded_by="NM_019236.1:120..593"
                     /db_xref="GeneID:29567"
                     /db_xref="RGD:62082"
ORIGIN      
        1 mrlprgvgda aelrkslkpl lekrrrarin eslsqlkglv lpllgaetsr ysklekadil
       61 emtvrflreq pasvcsteap gsldsylegy raclarlarv lpacsvlepa vsarllehlr
      121 qrtvsggpps ltpasasapa psppvpppss lglwrpw
//
LOCUS       NP_001102914             380 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF13 precursor [Rattus norvegicus].
ACCESSION   NP_001102914 XP_001057588 XP_001057631 XP_001057755 XP_001057819
            XP_001057871 XP_006232453
VERSION     NP_001102914.1
DBSOURCE    REFSEQ: accession NM_001109444.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Arshad,M., Ye,Z., Gu,X., Wong,C.K., Liu,Y., Li,D., Zhou,L.,
            Zhang,Y., Bay,W.P., Yu,V.C. and Li,P.
  TITLE     RNF13, a RING finger protein, mediates endoplasmic reticulum
            stress-induced apoptosis through the inositol-requiring enzyme
            (IRE1alpha)/c-Jun NH2-terminal kinase pathway
  JOURNAL   J Biol Chem 288 (12), 8726-8736 (2013)
   PUBMED   23378536
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Bocock,J.P., Carmicle,S., Chhotani,S., Ruffolo,M.R., Chu,H. and
            Erickson,A.H.
  TITLE     The PA-TM-RING protein RING finger protein 13 is an endosomal
            integral membrane E3 ubiquitin ligase whose RING finger domain is
            released to the cytoplasm by proteolysis
  JOURNAL   FEBS J 276 (7), 1860-1877 (2009)
   PUBMED   19292867
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081881.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006232453.1, XP_001057819.1, XP_001057871.1, XP_001057631.1,
            XP_001057755.1, XP_001057588.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081881.1, SRR8487230.147215.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..380
                     /product="E3 ubiquitin-protein ligase RNF13 precursor"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF13; RING-type E3
                     ubiquitin transferase RNF13"
                     /calculated_mol_wt=38848
     sig_peptide     1..34
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66HG0.1)"
                     /calculated_mol_wt=3756
     Region          23..180
                     /region_name="PA_C_RZF_like"
                     /note="PA_C-RZF_ like: Protease-associated (PA) domain
                     C_RZF-like. This group includes various PA
                     domain-containing proteins similar to C-RZF (chicken
                     embryo RING zinc finger) protein. These proteins contain a
                     C3H2C3 RING finger. C-RZF is expressed in embryo...;
                     cd02123"
                     /db_xref="CDD:239038"
     mat_peptide     35..380
                     /product="E3 ubiquitin-protein ligase RNF13.
                     /id=PRO_0000307369"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG0.1)"
                     /calculated_mol_wt=38848
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66HG0.1)"
     Site            130..132
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239038"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG0.1)"
     Region          230..288
                     /region_name="RING-H2_RNF13"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 13 (RNF13) and similar proteins; cd16796"
                     /db_xref="CDD:438450"
     Site            order(240,243,258,260,263,266,278,281)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438450"
     Region          285..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG0.1)"
     CDS             1..380
                     /gene="Rnf13"
                     /coded_by="NM_001109444.2:85..1227"
                     /db_xref="GeneID:681578"
                     /db_xref="RGD:1594062"
ORIGIN      
        1 mllsigmlml satqvytilt vqlfaflnll pveadilayn fenasqtfed lparfgyrlp
       61 aeglkgflin skpenacepi vppplkdnss gtfivlirrl dcnfdikvln aqragykaai
      121 vhnvdsddli smgsndidil kkidipsvfi gessanslkd eftyekgghv ilvpelslpl
      181 eyylipflii vgiclilivi fmitkfvqdr hrnrrnrlrk dqlkklpvhk fkkgdeydvc
      241 aicleeyedg dklrilpcsh ayhckcvdpw ltktkktcpv ckqkvvpsqg dsdsdtdssq
      301 eenqvsehtp llppsasart qsfgslsesh shhmtessdy edddneetds sdadneitdh
      361 svvvqlqpng epdyniantv
//
LOCUS       NP_071620                106 aa            linear   ROD 27-APR-2025
DEFINITION  guanylate cyclase activator 2B precursor [Rattus norvegicus].
ACCESSION   NP_071620 XP_346751
VERSION     NP_071620.1
DBSOURCE    REFSEQ: accession NM_022284.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Brenna,O., Furnes,M.W., Munkvold,B., Kidd,M., Sandvik,A.K. and
            Gustafsson,B.I.
  TITLE     Cellular localization of guanylin and uroguanylin mRNAs in human
            and rat duodenal and colonic mucosa
  JOURNAL   Cell Tissue Res 365 (2), 331-341 (2016)
   PUBMED   27044258
  REMARK    GeneRIF: The specific cellular distribution of both GN and UGN
            differs between duodenum and colon and between human and rat
            intestines.
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Lessa,L.M., Carraro-Lacroix,L.R., Crajoinas,R.O., Bezerra,C.N.,
            Dariolli,R., Girardi,A.C., Fonteles,M.C. and Malnic,G.
  TITLE     Mechanisms underlying the inhibitory effects of uroguanylin on NHE3
            transport activity in renal proximal tubule
  JOURNAL   Am J Physiol Renal Physiol 303 (10), F1399-F1408 (2012)
   PUBMED   22952280
  REMARK    GeneRIF: our data suggest that the inhibitory effect of UGN on NHE3
            transport activity in proximal tubule is mediated by activation of
            both cGMP/PKG and cAMP/PKA signaling pathways
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Hagstrom,S.A., Watson,R.F., Pauer,G.J. and Grossman,G.H.
  TITLE     Tulp1 is involved in specific photoreceptor protein transport
            pathways
  JOURNAL   Adv Exp Med Biol 723, 783-789 (2012)
   PUBMED   22183407
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Qian,X., Moss,N.G., Fellner,R.C., Taylor-Blake,B. and Goy,M.F.
  TITLE     The rat kidney contains high levels of prouroguanylin (the
            uroguanylin precursor) but does not express GC-C (the enteric
            uroguanylin receptor)
  JOURNAL   Am J Physiol Renal Physiol 300 (2), F561-F573 (2011)
   PUBMED   21106860
  REMARK    GeneRIF: these studies provide a comprehensive description of Ugn
            and GC-C expression in the kidney of the Sprague-Dawley rat.
REFERENCE   5  (residues 1 to 106)
  AUTHORS   McCue,H.V., Haynes,L.P. and Burgoyne,R.D.
  TITLE     The diversity of calcium sensor proteins in the regulation of
            neuronal function
  JOURNAL   Cold Spring Harb Perspect Biol 2 (8), a004085 (2010)
   PUBMED   20668007
  REMARK    Review article
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Santos-Neto,M.S., Carvalho,A.F., Monteiro,H.S., Forte,L.R. and
            Fonteles,M.C.
  TITLE     Interaction of atrial natriuretic peptide, urodilatin, guanylin and
            uroguanylin in the isolated perfused rat kidney
  JOURNAL   Regul Pept 136 (1-3), 14-22 (2006)
   PUBMED   16814407
  REMARK    GeneRIF: atrial natriuretic peptide, urodilatin, guanylin and
            uroguanylin interact in rat kidney
REFERENCE   7  (residues 1 to 106)
  AUTHORS   Lorenz,J.N., Nieman,M., Sabo,J., Sanford,L.P., Hawkins,J.A.,
            Elitsur,N., Gawenis,L.R., Clarke,L.L. and Cohen,M.B.
  TITLE     Uroguanylin knockout mice have increased blood pressure and
            impaired natriuretic response to enteral NaCl load
  JOURNAL   J Clin Invest 112 (8), 1244-1254 (2003)
   PUBMED   14561709
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Blanchard,R.K. and Cousins,R.J.
  TITLE     Upregulation of rat intestinal uroguanylin mRNA by dietary zinc
            restriction
  JOURNAL   Am J Physiol 272 (5 Pt 1), G972-G978 (1997)
   PUBMED   9176203
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Li,Z., Perkins,A.G., Peters,M.F., Campa,M.J. and Goy,M.F.
  TITLE     Purification, cDNA sequence, and tissue distribution of rat
            uroguanylin
  JOURNAL   Regul Pept 68 (1), 45-56 (1997)
   PUBMED   9094754
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Miyazato,M., Nakazato,M., Matsukura,S., Kangawa,K. and Matsuo,H.
  TITLE     Uroguanylin gene expression in the alimentary tract and
            extra-gastrointestinal tissues
  JOURNAL   FEBS Lett 398 (2-3), 170-174 (1996)
   PUBMED   8977100
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U41322.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346751.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U41322.1, CB809177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..106
                     /product="guanylate cyclase activator 2B precursor"
                     /note="guanylate cyclase activator 2b (retina);
                     uroguanylin"
                     /calculated_mol_wt=9406
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2186
     Region          22..106
                     /region_name="Guanylin"
                     /note="Guanylin precursor; pfam02058"
                     /db_xref="CDD:460430"
     CDS             1..106
                     /gene="Guca2b"
                     /coded_by="NM_022284.2:37..357"
                     /db_xref="GeneID:64055"
                     /db_xref="RGD:620044"
ORIGIN      
        1 msgsqlwaav llllvlqsaq gvyikyhgfq vqlesvkkln eleekqmsdp qqqksgllpd
       61 vcynpalpld lqpvcasqea astfkalrti atdecelcin vactgc
//
LOCUS       NP_001019936             983 aa            linear   ROD 27-APR-2025
DEFINITION  next to BRCA1 gene 1 protein [Rattus norvegicus].
ACCESSION   NP_001019936 XP_220926
VERSION     NP_001019936.1
DBSOURCE    REFSEQ: accession NM_001024765.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Chan,N.C., Salazar,A.M., Pham,A.H., Sweredoski,M.J., Kolawa,N.J.,
            Graham,R.L., Hess,S. and Chan,D.C.
  TITLE     Broad activation of the ubiquitin-proteasome system by Parkin is
            critical for mitophagy
  JOURNAL   Hum Mol Genet 20 (9), 1726-1737 (2011)
   PUBMED   21296869
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Itakura,E. and Mizushima,N.
  TITLE     p62 Targeting to the autophagosome formation site requires
            self-oligomerization but not LC3 binding
  JOURNAL   J Cell Biol 192 (1), 17-27 (2011)
   PUBMED   21220506
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Whitehouse,C.A., Waters,S., Marchbank,K., Horner,A., McGowan,N.W.,
            Jovanovic,J.V., Xavier,G.M., Kashima,T.G., Cobourne,M.T.,
            Richards,G.O., Sharpe,P.T., Skerry,T.M., Grigoriadis,A.E. and
            Solomon,E.
  TITLE     Neighbor of Brca1 gene (Nbr1) functions as a negative regulator of
            postnatal osteoblastic bone formation and p38 MAPK activity
  JOURNAL   Proc Natl Acad Sci U S A 107 (29), 12913-12918 (2010)
   PUBMED   20616007
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2013 Mar 12;110(11):4428]
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Waters,S., Marchbank,K., Solomon,E., Whitehouse,C. and Gautel,M.
  TITLE     Interactions with LC3 and polyubiquitin chains link nbr1 to
            autophagic protein turnover
  JOURNAL   FEBS Lett 583 (12), 1846-1852 (2009)
   PUBMED   19427866
REFERENCE   6  (residues 1 to 983)
  AUTHORS   Kirkin,V., Lamark,T., Sou,Y.S., Bjorkoy,G., Nunn,J.L., Bruun,J.A.,
            Shvets,E., McEwan,D.G., Clausen,T.H., Wild,P., Bilusic,I.,
            Theurillat,J.P., Overvatn,A., Ishii,T., Elazar,Z., Komatsu,M.,
            Dikic,I. and Johansen,T.
  TITLE     A role for NBR1 in autophagosomal degradation of ubiquitinated
            substrates
  JOURNAL   Mol Cell 33 (4), 505-516 (2009)
   PUBMED   19250911
REFERENCE   7  (residues 1 to 983)
  AUTHORS   Lange,S., Xiang,F., Yakovenko,A., Vihola,A., Hackman,P.,
            Rostkova,E., Kristensen,J., Brandmeier,B., Franzen,G., Hedberg,B.,
            Gunnarsson,L.G., Hughes,S.M., Marchand,S., Sejersen,T., Richard,I.,
            Edstrom,L., Ehler,E., Udd,B. and Gautel,M.
  TITLE     The kinase domain of titin controls muscle gene expression and
            protein turnover
  JOURNAL   Science 308 (5728), 1599-1603 (2005)
   PUBMED   15802564
REFERENCE   8  (residues 1 to 983)
  AUTHORS   Dimitrov,S., Brennerova,M. and Forejt,J.
  TITLE     Expression profiles and intergenic structure of head-to-head
            oriented Brca1 and Nbr1 genes
  JOURNAL   Gene 262 (1-2), 89-98 (2001)
   PUBMED   11179671
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC095903.1.
            
            On Jun 10, 2005 this sequence version replaced XP_220926.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC095903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..983
                     /product="next to BRCA1 gene 1 protein"
                     /note="neighbor of BRCA1 gene 1 protein; next to the
                     Brca1; ovarian carcinoma antigen CA125"
                     /calculated_mol_wt=109698
     Region          5..86
                     /region_name="PB1_NBR1"
                     /note="The PB1 domain is an essential part of NBR1
                     protein, next to BRCA1, a scaffold protein mediating
                     specific protein-protein interaction with both titin
                     protein kinase and with another scaffold protein p62. A
                     canonical PB1-PB1 interaction, which involves...; cd06396"
                     /db_xref="CDD:99718"
     Site            order(50,52,54,63)
                     /site_type="other"
                     /note="PB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:99718"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14596; propagated from
                     UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          126..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          217..261
                     /region_name="ZZ_NBR1_like"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     Drosophila ref(2)P, NBR1, Human sequestosome 1 and related
                     proteins. The ZZ motif coordinates two zinc ions and most
                     likely participates in ligand binding or molecular
                     scaffolding. Drosophila ref(2)P appears...; cd02340"
                     /db_xref="CDD:239080"
     Site            order(219,222,233,236,242,245,252,256)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239080"
     Site            order(219,222,242,245)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239080"
     Site            order(220,230,232,238,240)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239080"
     Site            order(231,258,261)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239080"
     Site            order(233,236,252,256)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239080"
     Region          371..481
                     /region_name="NBR1_like"
                     /note="Functionally uncharacterized domain in neighbor of
                     Brca1 Gene 1 and related proteins; cd14947"
                     /db_xref="CDD:271343"
     Region          544..638
                     /region_name="ATG8 family proteins-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14596; propagated from
                     UniProtKB/Swiss-Prot (Q501R9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q501R9.1)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          611..645
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          745..756
                     /region_name="ATG8 family proteins-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          768..813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          867..894
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q501R9.1)"
     Region          933..971
                     /region_name="UBA_NBR1"
                     /note="UBA domain of next to BRCA1 gene 1 protein (NBR1)
                     and similar proteins; cd14319"
                     /db_xref="CDD:270504"
     CDS             1..983
                     /gene="Nbr1"
                     /gene_synonym="Ca125; RGD1311421"
                     /coded_by="NM_001024765.1:175..3126"
                     /db_xref="GeneID:303554"
                     /db_xref="RGD:69195"
ORIGIN      
        1 mepqvtlnvt fknetqsflv sdpenttwad veamvkvsfd lntiqikyld eeneeisins
       61 qgeyeealkm anikqgnqlq mqvhegchvv devlpqtvve kqatartgkk plahysslvr
      121 vlgsdmktte eptaearspv pcdtdkpqdk ppdwftsyle mfreqvvket vekleqrlqe
      181 klvlqkppfs sspsevsmpi seeetlflpe nqfswhiacs hcqkrivgvr yqcslcpsyn
      241 icedceagpy shdtnhillk frrpvvisse pffyskyptp rlpaaleqvr lqkqvdknfv
      301 kaekqrlrae kkqrkaevke lkkqlklhrk ihlwnsihgl qspksplgrp esllqsntlm
      361 lplqpcapvm ptlsaafvde nlpdgthlqp gtkfikhwrm kntgnvkwsa dtklkfmwgn
      421 ltlastekkd vlvpclkagh igvvsvefia ptlegtytlh wrlshkgqqf gprvwcsiiv
      481 dpfpssespv nlerdgisss kaddftceqe eafllaeeei plgevtkqte gtgssapqkt
      541 qhaaserely ipsvdlltaq dllsfelldi nivqelervp hntpvdvtpr msplphdspl
      601 iekpglgriq eesegaglka spdstvltkr kaetpasvee teedlsgtqf vcetvirslt
      661 ldaapdhnpp crqrspqrel qlysteeqqp lmlpgfcrkd sslkfalpee gphgdereei
      721 vhiaeeeaie eedvqdeevq sqssassedy iiilpecfdt srplgdsmys salsqpgler
      781 gaegepgies gqepaearer lperesqpke qsisdiltts qhldtvplvp evaglpaals
      841 rsapcgqyea prvdspvtiq evlpvpdhvr geprgstgla nsrqkscdhs rhhngssiag
      901 glvkgalsva asaykalfsg ppvtaqpvis edqtaalmah lfemgfcdrq lnlrllrkhn
      961 hnilqvvtel lqvnnndwys hry
//
LOCUS       NP_058952                853 aa            linear   ROD 27-APR-2025
DEFINITION  transforming growth factor beta receptor type 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_058952
VERSION     NP_058952.1
DBSOURCE    REFSEQ: accession NM_017256.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Henen,M.A., Mahlawat,P., Zwieb,C., Kodali,R.B., Hinck,C.S.,
            Hanna,R.D., Krzysiak,T.C., Ilangovan,U., Cano,K.E., Hinck,G.,
            Vonberg,M., McCabe,M. and Hinck,A.P.
  TITLE     TGF-beta2 uses the concave surface of its extended finger region to
            bind betaglycan's ZP domain via three residues specific to TGF-beta
            and inhibin-alpha
  JOURNAL   J Biol Chem 294 (9), 3065-3080 (2019)
   PUBMED   30598510
  REMARK    GeneRIF: identify the BGZP-C-binding site on TGF-beta2 and shed
            light on the specificity of BG for select TGF-beta-type GFs and the
            mechanisms by which BG influences their signaling
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Hill,C.R., Jacobs,B.H., Brown,C.B., Barnett,J.V. and Goudy,S.L.
  TITLE     Type III transforming growth factor beta receptor regulates
            vascular and osteoblast development during palatogenesis
  JOURNAL   Dev Dyn 244 (2), 122-133 (2015)
   PUBMED   25382630
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Orostica,M.L., Lopez,J., Zuniga,L.M., Utz,D., Diaz,P., Reuquen,P.,
            Parada-Bustamante,A., Cardenas,H. and Orihuela,P.A.
  TITLE     Mating decreases plasma levels of TGFbeta1 and regulates myosalpinx
            expression of TGFbeta1/TGFBR3 in the rat
  JOURNAL   Mol Reprod Dev 81 (11), 1053-1061 (2014)
   PUBMED   25359088
  REMARK    GeneRIF: Mating decreases plasma levels of TGFbeta1 and regulates
            myosalpinx expression of TGFbeta1/TGFBR3 in the rat.
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Liang,H., Zhang,C., Ban,T., Liu,Y., Mei,L., Piao,X., Zhao,D.,
            Lu,Y., Chu,W. and Yang,B.
  TITLE     A novel reciprocal loop between microRNA-21 and TGFbetaRIII is
            involved in cardiac fibrosis
  JOURNAL   Int J Biochem Cell Biol 44 (12), 2152-2160 (2012)
   PUBMED   22960625
REFERENCE   5  (residues 1 to 853)
  AUTHORS   Lin,S.J., Hu,Y., Zhu,J., Woodruff,T.K. and Jardetzky,T.S.
  TITLE     Structure of betaglycan zona pellucida (ZP)-C domain provides
            insights into ZP-mediated protein polymerization and TGF-beta
            binding
  JOURNAL   Proc Natl Acad Sci U S A 108 (13), 5232-5236 (2011)
   PUBMED   21402931
  REMARK    GeneRIF: Data present the 2.0-A resolution crystal structure of the
            betaglycan ZP-C region in combination with a downstream region
            known as the external hydrophobic patch.
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Moren,A., Ichijo,H. and Miyazono,K.
  TITLE     Molecular cloning and characterization of the human and porcine
            transforming growth factor-beta type III receptors
  JOURNAL   Biochem Biophys Res Commun 189 (1), 356-362 (1992)
   PUBMED   1333192
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Andres,J.L., DeFalcis,D., Noda,M. and Massague,J.
  TITLE     Binding of two growth factor families to separate domains of the
            proteoglycan betaglycan
  JOURNAL   J Biol Chem 267 (9), 5927-5930 (1992)
   PUBMED   1556106
REFERENCE   8  (residues 1 to 853)
  AUTHORS   Andres,J.L., Ronnstrand,L., Cheifetz,S. and Massague,J.
  TITLE     Purification of the transforming growth factor-beta (TGF-beta)
            binding proteoglycan betaglycan
  JOURNAL   J Biol Chem 266 (34), 23282-23287 (1991)
   PUBMED   1744125
REFERENCE   9  (residues 1 to 853)
  AUTHORS   Wang,X.F., Lin,H.Y., Ng-Eaton,E., Downward,J., Lodish,H.F. and
            Weinberg,R.A.
  TITLE     Expression cloning and characterization of the TGF-beta type III
            receptor
  JOURNAL   Cell 67 (4), 797-805 (1991)
   PUBMED   1657407
REFERENCE   10 (residues 1 to 853)
  AUTHORS   Lopez-Casillas,F., Cheifetz,S., Doody,J., Andres,J.L., Lane,W.S.
            and Massague,J.
  TITLE     Structure and expression of the membrane proteoglycan betaglycan, a
            component of the TGF-beta receptor system
  JOURNAL   Cell 67 (4), 785-795 (1991)
   PUBMED   1657406
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M77809.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M77809.1, M80784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..853
                     /product="transforming growth factor beta receptor type 3
                     precursor"
                     /note="TGF-beta receptor type III; transforming growth
                     factor beta receptor type 3; TGFR-3; TGF-beta receptor
                     type 3; transforming growth factor, beta receptor III"
                     /calculated_mol_wt=91707
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2414
     mat_peptide     24..853
                     /product="Transforming growth factor beta receptor type 3.
                     /id=PRO_0000041666"
                     /note="propagated from UniProtKB/Swiss-Prot (P26342.1)"
                     /calculated_mol_wt=91707
     Site            37
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Region          456..733
                     /region_name="ZP"
                     /note="Zona pellucida (ZP) domain; smart00241"
                     /db_xref="CDD:214579"
     Site            493
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Region          530..559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26342.1)"
     Site            535
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Site            546
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Site            572
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21402931; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Site            698
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21402931; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     Region          737..751
                     /region_name="Interaction with TGF-beta ligand.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P26342.1)"
     Site            790..811
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26342.1)"
     Region          820..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26342.1)"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03167; propagated from
                     UniProtKB/Swiss-Prot (P26342.1)"
     CDS             1..853
                     /gene="Tgfbr3"
                     /gene_synonym="betaglycan"
                     /coded_by="NM_017256.1:335..2896"
                     /db_xref="GeneID:29610"
                     /db_xref="RGD:61821"
ORIGIN      
        1 mavtshhmip vmvvlmsacl atagpepstr celspinash pvqalmesft vlsgcasrgt
       61 tglprevhvl nlrstdqgpg qrqrevtlhl npiasvhthh kpivfllnsp qplvwhlkte
      121 rlaagvprlf lvsegsvvqf psgnfsltae teernfpqen ehllrwaqke ygavtsftel
      181 kiarniyikv gedqvfpptc nigknflsln ylaeylqpka aegcvlpsqp hekevhiiel
      241 itpssnpysa fqvdiivdir paqedpevvk nlvlilkckk svnwviksfd vkgnlkviap
      301 nsigfgkese rsmtmtklvr ddipstqenl mkwaldngyr pvtsytmapv anrfhlrlen
      361 neemrdeevh tippelrill dpdhppaldn plfpgegspn gglpfpfpdi prrgwkeged
      421 riprpkqpiv psvqllpdhr epeevqggvd ialsvkcdhe kmvvavdkds fqtngysgme
      481 ltlldpscka kmngthfvle splngcgtrh rrstpdgvvy ynsivvqaps pgdssgwpdg
      541 yedlesgdng fpgdgdeget aplsragvvv fncslrqlrn psgfqgqldg natfnmelyn
      601 tdlflvpspg vfsvaenehv yvevsvtkad qdlgfaiqtc flspysnpdr msdytiieni
      661 cpkddsvkfy sskrvhfpip haevdkkrfs flfksvfnts llflhceltl csrkkgslkl
      721 prcvtpddac tsldatmiwt mmqnkktftk plavvlqvdy kenvpstkds spipppppqi
      781 fhgldtltvm giafaafvig alltgalwyi yshtgetarr qqvptsppas enssaahsig
      841 stqstpcsss sta
//
LOCUS       NP_001029181             606 aa            linear   ROD 27-APR-2025
DEFINITION  cell surface glycoprotein MUC18 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001029181
VERSION     NP_001029181.1
DBSOURCE    REFSEQ: accession NM_001034009.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Yamchi,N.N., Rahbarghazi,R., Bedate,A.M., Mahdipour,M., Nouri,M.
            and Khanbabaee,R.
  TITLE     Menstrual blood CD146+ mesenchymal stem cells reduced fibrosis rate
            in the rat model of premature ovarian failure
  JOURNAL   Cell Biochem Funct 39 (8), 998-1008 (2021)
   PUBMED   34477225
  REMARK    GeneRIF: Menstrual blood CD146(+) mesenchymal stem cells reduced
            fibrosis rate in the rat model of premature ovarian failure.
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Marr,N., Meeson,R., Kelly,E.F., Fang,Y., Peffers,M.J.,
            Pitsillides,A.A., Dudhia,J. and Thorpe,C.T.
  TITLE     CD146 Delineates an Interfascicular Cell Sub-Population in Tendon
            That Is Recruited during Injury through Its Ligand Laminin-alpha4
  JOURNAL   Int J Mol Sci 22 (18), 9729 (2021)
   PUBMED   34575887
  REMARK    GeneRIF: CD146 Delineates an Interfascicular Cell Sub-Population in
            Tendon That Is Recruited during Injury through Its Ligand
            Laminin-alpha4.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Obara,M., Sato,S., Takahashi,K., Kondo,Y., Hirose,M., Nata,K. and
            Taira,E.
  TITLE     Expression of cell adhesion molecule, Gicerin/CD146 during the
            formation of heart and in the cardiac hypertrophy
  JOURNAL   Mol Cell Biochem 476 (5), 2021-2028 (2021)
   PUBMED   33515199
  REMARK    GeneRIF: Expression of cell adhesion molecule, Gicerin/CD146 during
            the formation of heart and in the cardiac hypertrophy.
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Liu,G., Sun,X., Bian,J., Wu,R., Guan,X., Ouyang,B., Huang,Y.,
            Xiao,H., Luo,D., Atala,A., Zhang,Y. and Deng,C.
  TITLE     Correction of diabetic erectile dysfunction with adipose derived
            stem cells modified with the vascular endothelial growth factor
            gene in a rodent diabetic model
  JOURNAL   PLoS One 8 (8), e72790 (2013)
   PUBMED   24023647
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Taira,E., Kohama,K., Tsukamoto,Y., Okumura,S. and Miki,N.
  TITLE     Gicerin/CD146 is involved in neurite extension of NGF-treated PC12
            cells
  JOURNAL   J Cell Physiol 204 (2), 632-637 (2005)
   PUBMED   15880440
  REMARK    GeneRIF: Increase of gicerin expression by NGF promotes the
            gicerin-gicerin homophilic interaction resulting in the neurite
            extension.
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Taira,E., Kohama,K., Tsukamoto,Y., Okumura,S. and Miki,N.
  TITLE     Characterization of Gicerin/MUC18/CD146 in the rat nervous system
  JOURNAL   J Cell Physiol 198 (3), 377-387 (2004)
   PUBMED   14755543
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Okumura,S., Kohama,K., Kim,S., Iwao,H., Miki,N. and Taira,E.
  TITLE     Induction of gicerin/CD146 in the rat carotid artery after balloon
            injury
  JOURNAL   Biochem Biophys Res Commun 313 (4), 902-906 (2004)
   PUBMED   14706627
  REMARK    GeneRIF: expression of gicerin was increased in the rat carotid
            arteries after balloon injury. Gicerin might be involved in the
            arteriosclerotic neointima formation in the artery.
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Tsukamoto,Y., Egawa,M., Hiroi,S., Furuya,M., Tsuchiya,S.,
            Sasaki,F., Miki,N. and Taira,E.
  TITLE     Gicerin, an Ig-superfamily cell adhesion molecule, promotes the
            invasive and metastatic activities of a mouse fibroblast cell line
  JOURNAL   J Cell Physiol 197 (1), 103-109 (2003)
   PUBMED   12942546
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Li,B.S., Su,Q.N., Kiyama,H., Miki,N., Robinow,D.R. and Zhang,L.
  TITLE     Expression of gicerin, a novel cell adhesion molecule, is
            upregulated in the astrocytes after hypoglossal nerve injury in
            rats
  JOURNAL   Neurosci Lett 260 (3), 149-152 (1999)
   PUBMED   10076889
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070916.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070916.1, AB035507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..606
                     /product="cell surface glycoprotein MUC18 isoform 2
                     precursor"
                     /note="cell surface glycoprotein MUC18; gicerin;
                     melanoma-associated antigen MUC18; l-gicerin"
                     /calculated_mol_wt=64307
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2394
     Region          43..120
                     /region_name="CD19_double_Ig"
                     /note="CD19 (Cluster of Differentiation 19), a unique
                     double immunoglobulin (Ig)-fold domain; cl49627"
                     /db_xref="CDD:483967"
     Region          43..50
                     /region_name="strand B"
                     /note="strand B [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(45,47,49,81,102,104,106,111)
                     /site_type="other"
                     /note="CD81 binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          51..60
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:467824"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          60..67
                     /region_name="strand C"
                     /note="strand C [structural motif]"
                     /db_xref="CDD:467824"
     Site            order(67,117)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:467824"
     Region          76..80
                     /region_name="strand C'"
                     /note="strand C' [structural motif]"
                     /db_xref="CDD:467824"
     Region          81..90
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:467824"
     Region          90..120
                     /region_name="protodomain 2+4"
                     /note="protodomain 2+4 [structural motif]"
                     /db_xref="CDD:467824"
     Region          90..94
                     /region_name="strand D"
                     /note="strand D [structural motif]"
                     /db_xref="CDD:467824"
     Region          101..106
                     /region_name="strand E"
                     /note="strand E [structural motif]"
                     /db_xref="CDD:467824"
     Region          112..120
                     /region_name="strand F"
                     /note="strand F [structural motif]"
                     /db_xref="CDD:467824"
     Region          141..236
                     /region_name="C2-set_2"
                     /note="CD80-like C2-set immunoglobulin domain; pfam08205"
                     /db_xref="CDD:400489"
     Region          173..177
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          264..323
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          282..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          348..412
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          <452..508
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          463..467
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          487..491
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          499..503
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Region          527..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     Site            561..581
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPF2.2)"
     CDS             1..606
                     /gene="Mcam"
                     /gene_synonym="CD146; Muc18"
                     /coded_by="NM_001034009.1:19..1839"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:78967"
                     /db_xref="RGD:620463"
ORIGIN      
        1 mglprlvcaf lfaaccccrs atgvpgeekq ptptpdpvev evgntallkc gpahpsgnfs
       61 qvewflihke rqipifrvhq gkgqsepgey ehrlslhgpg atlalsqvtp hddrmflcks
      121 kqprpqdhyv qlqvykapee ptiqanvlgi hvdiqelkev atcvgrngyp ipqviwykng
      181 rplqeeenrv hiqssqtves sglytlksvl sarlvkedkd aqfycelsyr lpsgnrmkes
      241 kevtvpvlyp aekvwvevep vgllkegdhv kircltdgnp qphftinkkn psteemeees
      301 tdengllsle paqkhhsgvy qcqsldlett vmlssdplel lvnyvsdvqv dptapevqeg
      361 dsltltckae snqdlefewl rdktgqllgk gpilqlnnvk reaggrylcv asvpsvpgln
      421 rtrrvsvgif gspwmaaker kvwaqenaml nlsceasghp qptiswning satewnpdpq
      481 tvvstlnvlv tpelletgae ctasnslgsn ttviilklvt lttltpdssq ttglstptvs
      541 phsranstst ekklpqqesk gvvivavivc tlvlavlgat lyyfykkgkl pcgrsgkqem
      601 erntsi
//
LOCUS       NP_001034081              66 aa            linear   ROD 27-APR-2025
DEFINITION  small vasohibin-binding protein isoform b [Rattus norvegicus].
ACCESSION   NP_001034081
VERSION     NP_001034081.1
DBSOURCE    REFSEQ: accession NM_001038992.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Iqbal,Z., Tawamie,H., Ba,W., Reis,A., Halak,B.A., Sticht,H.,
            Uebe,S., Kasri,N.N., Riazuddin,S., van Bokhoven,H. and Abou
            Jamra,R.
  TITLE     Loss of function of SVBP leads to autosomal recessive intellectual
            disability, microcephaly, ataxia, and hypotonia
  JOURNAL   Genet Med 21 (8), 1790-1796 (2019)
   PUBMED   30607023
  REMARK    GeneRIF: Knocking down Svbp in rat primary hippocampal neurons led
            to a significant decrease in the number of excitatory synapses.
            SVBP is not only involved in angiogenesis, but also has vital
            functions in the central nervous system. Biallelic loss-of-function
            variants in SVBP lead to intellectual disability.
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Zhou,C., Yan,L., Zhang,W.H. and Liu,Z.
  TITLE     Structural basis of tubulin detyrosination by VASH2/SVBP
            heterodimer
  JOURNAL   Nat Commun 10 (1), 3212 (2019)
   PUBMED   31324789
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Adamopoulos,A., Landskron,L., Heidebrecht,T., Tsakou,F.,
            Bleijerveld,O.B., Altelaar,M., Nieuwenhuis,J., Celie,P.H.N.,
            Brummelkamp,T.R. and Perrakis,A.
  TITLE     Crystal structure of the tubulin tyrosine carboxypeptidase complex
            VASH1-SVBP
  JOURNAL   Nat Struct Mol Biol 26 (7), 567-570 (2019)
   PUBMED   31270470
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Wang,N., Bosc,C., Ryul Choi,S., Boulan,B., Peris,L., Olieric,N.,
            Bao,H., Krichen,F., Chen,L., Andrieux,A., Olieric,V., Moutin,M.J.,
            Steinmetz,M.O. and Huang,H.
  TITLE     Structural basis of tubulin detyrosination by the vasohibin-SVBP
            enzyme complex
  JOURNAL   Nat Struct Mol Biol 26 (7), 571-582 (2019)
   PUBMED   31235911
REFERENCE   5  (residues 1 to 66)
  AUTHORS   Li,F., Hu,Y., Qi,S., Luo,X. and Yu,H.
  TITLE     Structural basis of tubulin detyrosination by vasohibins
  JOURNAL   Nat Struct Mol Biol 26 (7), 583-591 (2019)
   PUBMED   31235910
REFERENCE   6  (residues 1 to 66)
  AUTHORS   Liao,S., Rajendraprasad,G., Wang,N., Eibes,S., Gao,J., Yu,H.,
            Wu,G., Tu,X., Huang,H., Barisic,M. and Xu,C.
  TITLE     Molecular basis of vasohibins-mediated detyrosination and its
            impact on spindle function and mitosis
  JOURNAL   Cell Res 29 (7), 533-547 (2019)
   PUBMED   31171830
  REMARK    Erratum:[Cell Res. 2019 Sep;29(9):778. doi:
            10.1038/s41422-019-0215-y. PMID: 31395957]
REFERENCE   7  (residues 1 to 66)
  AUTHORS   Nieuwenhuis,J., Adamopoulos,A., Bleijerveld,O.B., Mazouzi,A.,
            Stickel,E., Celie,P., Altelaar,M., Knipscheer,P., Perrakis,A.,
            Blomen,V.A. and Brummelkamp,T.R.
  TITLE     Vasohibins encode tubulin detyrosinating activity
  JOURNAL   Science 358 (6369), 1453-1456 (2017)
   PUBMED   29146869
REFERENCE   8  (residues 1 to 66)
  AUTHORS   Aillaud,C., Bosc,C., Peris,L., Bosson,A., Heemeryck,P., Van
            Dijk,J., Le Friec,J., Boulan,B., Vossier,F., Sanman,L.E., Syed,S.,
            Amara,N., Coute,Y., Lafanechere,L., Denarier,E., Delphin,C.,
            Pelletier,L., Humbert,S., Bogyo,M., Andrieux,A., Rogowski,K. and
            Moutin,M.J.
  TITLE     Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate
            neuron differentiation
  JOURNAL   Science 358 (6369), 1448-1453 (2017)
   PUBMED   29146868
REFERENCE   9  (residues 1 to 66)
  AUTHORS   Suzuki,Y., Kobayashi,M., Miyashita,H., Ohta,H., Sonoda,H. and
            Sato,Y.
  TITLE     Isolation of a small vasohibin-binding protein (SVBP) and its role
            in vasohibin secretion
  JOURNAL   J Cell Sci 123 (Pt 18), 3094-3101 (2010)
   PUBMED   20736312
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099226.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099226.1, CV078848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..66
                     /product="small vasohibin-binding protein isoform b"
                     /note="coiled-coil domain-containing protein 23;
                     coiled-coil domain containing 23"
                     /calculated_mol_wt=7705
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLG3.1)"
     Region          6..62
                     /region_name="CCDC23"
                     /note="Coiled-coil domain-containing protein 23;
                     pfam15674"
                     /db_xref="CDD:434848"
     CDS             1..66
                     /gene="Svbp"
                     /gene_synonym="Ccdc23; RGD1311232"
                     /coded_by="NM_001038992.1:132..332"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:362578"
                     /db_xref="RGD:1311232"
ORIGIN      
        1 mdpparkeks kvkepafrve kakqksaqqe lkqrqraeiy alnrvmtele qqqfdefckq
       61 mqppge
//
LOCUS       NP_001101806             329 aa            linear   ROD 27-APR-2025
DEFINITION  serine dehydratase-like [Rattus norvegicus].
ACCESSION   NP_001101806 XP_001079897 XP_341090
VERSION     NP_001101806.1
DBSOURCE    REFSEQ: accession NM_001108336.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Katane,M., Nakasako,K., Yako,K., Saitoh,Y., Sekine,M. and Homma,H.
  TITLE     Identification of an l-serine/l-threonine dehydratase with
            glutamate racemase activity in mammals
  JOURNAL   Biochem J 477 (21), 4221-4241 (2020)
   PUBMED   33079132
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473973.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001079897.1, XP_341090.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132308,
                              SAMEA5756307 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..329
                     /product="serine dehydratase-like"
                     /EC_number="4.3.1.17"
                     /EC_number="4.3.1.19"
                     /EC_number="5.1.1.3"
                     /note="L-serine dehydratase-like; L-serine deaminase;
                     glutamate racemase; L-threonine dehydratase; L-serine
                     dehydratase/L-threonine deaminase"
                     /calculated_mol_wt=34822
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96GA7; propagated from
                     UniProtKB/Swiss-Prot (A0A6N3IN21.1)"
     Region          17..326
                     /region_name="L-Ser-dehyd"
                     /note="Serine dehydratase is a pyridoxal phosphate
                     (PLP)-dependent enzyme which catalyzes the conversion of
                     L-, D-serine, or L-threonine to pyruvate/ketobutyrate and
                     ammonia; cd06448"
                     /db_xref="CDD:107209"
     Site            order(48,74,174..178)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107209"
     Site            48
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107209"
     CDS             1..329
                     /gene="Sdsl"
                     /gene_synonym="Sdhl; TDH"
                     /coded_by="NM_001108336.1:262..1251"
                     /db_xref="GeneID:360816"
                     /db_xref="RGD:1309192"
ORIGIN      
        1 megasaecvr aepfhrvtpl leswalsqva gmpvflkyen vqiagsfkir gighfcqqma
       61 krgcrhlvcs sggnagiaaa ysaqklgipv tivlpestsk qvvrrlegeg aevqltgkvw
      121 deanvraqel atrdgwvnvs pfdhpliweg naslvrelke slrtppgavv lavgggglla
      181 gvvagllevg wqhvpivame trgahsfnaa llagrlvtlp ditsvarslg aktvaartle
      241 cakecevlse vvedreavra vqrfldderm lvepacgaal aavysgilgr lqtegrlspa
      301 ldsvvvivcg gnnissqqlq elktqlncs
//
LOCUS       NP_446212                581 aa            linear   ROD 27-APR-2025
DEFINITION  TRAF-type zinc finger domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_446212 XP_001076427 XP_341087
VERSION     NP_446212.2
DBSOURCE    REFSEQ: accession NM_053760.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Sanada,T., Takaesu,G., Mashima,R., Yoshida,R., Kobayashi,T. and
            Yoshimura,A.
  TITLE     FLN29 deficiency reveals its negative regulatory role in the
            Toll-like receptor (TLR) and retinoic acid-inducible gene I
            (RIG-I)-like helicase signaling pathway
  JOURNAL   J Biol Chem 283 (49), 33858-33864 (2008)
   PUBMED   18849341
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Cattaruzza,M., Schafer,K. and Hecker,M.
  TITLE     Cytokine-induced down-regulation of zfm1/splicing factor-1 promotes
            smooth muscle cell proliferation
  JOURNAL   J Biol Chem 277 (8), 6582-6589 (2002)
   PUBMED   11748220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Oct 23, 2008 this sequence version replaced
            XP_341087.2, XP_001076427.1, NP_446212.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.776944.1,
                                           SRR26360194.988585.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..581
                     /product="TRAF-type zinc finger domain-containing protein
                     1"
                     /note="FLN29 gene product"
                     /calculated_mol_wt=64234
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Region          <12..131
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Region          402..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14545; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     Region          465..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MM4.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99MM4.2)"
     CDS             1..581
                     /gene="Trafd1"
                     /gene_synonym="Fln29"
                     /coded_by="NM_053760.2:100..1845"
                     /db_xref="GeneID:114635"
                     /db_xref="RGD:620171"
ORIGIN      
        1 maefpddqaa rlcdnckkei pvfnftihei hcqrnigvcp vckepfpksd mdihvatehc
       61 qvtckcnkkl ekrqlkqhve tecplrlavc qhcdlelsvv klkehedycg artelcgscg
      121 rnvlvkelqt hpavcgrvee ekrseaavpp eaydepwsqd riwiasqllr qiealdppmr
      181 lpgrplrafe adpfysrtas qrgvtahfpi qnnlfeeqer qernrshqsp kdsaensahl
      241 dfmlalslqn egqassmveq gfwesvpead paragptslg dikgaadetl lpcefceely
      301 peellidhqt scnpshalrs lntgsssirg vedpgaifqn flqqatsnql dtlmglsssa
      361 avedsiiipc efcgvqleee vlfhhqdqcd qrpatanhra megiptqdsq pedrspelsr
      421 rrvkhqgdls sgymddvkqe svkgstysls pnrtmnnvst cnrllnssgp rsdcqrsppg
      481 vlklnnsgsq dirgrirgsq ngpiasahap vihsirnlyp enlapsfphg spgrfgasgr
      541 segsrssrvt ptaasyhsra akakppkqqg agdaeeeeee e
//
LOCUS       NP_001014177             842 aa            linear   ROD 27-APR-2025
DEFINITION  TATA box-binding protein-associated factor, RNA polymerase I,
            subunit C [Rattus norvegicus].
ACCESSION   NP_001014177 XP_341699
VERSION     NP_001014177.1
DBSOURCE    REFSEQ: accession NM_001014155.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     TFIIB-related factors in RNA polymerase I transcription
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 265-273 (2013)
   PUBMED   22960599
  REMARK    Review article
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Zhai,N., Zhao,Z.L., Cheng,M.B., Di,Y.W., Yan,H.X., Cao,C.Y.,
            Dai,H., Zhang,Y. and Shen,Y.F.
  TITLE     Human PIH1 associates with histone H4 to mediate the
            glucose-dependent enhancement of pre-rRNA synthesis
  JOURNAL   J Mol Cell Biol 4 (4), 231-241 (2012)
   PUBMED   22368283
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Schneider,D.A.
  TITLE     RNA polymerase I activity is regulated at multiple steps in the
            transcription cycle: recent insights into factors that influence
            transcription elongation
  JOURNAL   Gene 493 (2), 176-184 (2012)
   PUBMED   21893173
  REMARK    Review article
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Lin,C.Y., Tuan,J., Scalia,P., Bui,T. and Comai,L.
  TITLE     The cell cycle regulatory factor TAF1 stimulates ribosomal DNA
            transcription by binding to the activator UBF
  JOURNAL   Curr Biol 12 (24), 2142-2146 (2002)
   PUBMED   12498690
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061804.1.
            
            On Apr 20, 2005 this sequence version replaced XP_341699.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061804.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..842
                     /product="TATA box-binding protein-associated factor, RNA
                     polymerase I, subunit C"
                     /note="TBP-associated factor 1C; TATA box-binding
                     protein-associated factor 1C; transcription initiation
                     factor SL1/TIF-IB subunit C; TATA box binding protein
                     (Tbp)-associated factor, RNA polymerase I, C"
                     /calculated_mol_wt=92241
     Region          574..605
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P773.1)"
     Region          667..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P773.1)"
     Region          702..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P773.1)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15572; propagated from
                     UniProtKB/Swiss-Prot (Q6P773.1)"
     CDS             1..842
                     /gene="Taf1c"
                     /coded_by="NM_001014155.1:65..2593"
                     /db_xref="GeneID:361420"
                     /db_xref="RGD:1305658"
ORIGIN      
        1 mdfpstlrps lfmagplgmt dgpdlsfmcs wrdaltlpga qpqncrdqts sfaknllwep
       61 stpgplplvp pgpdpwdpgl aaqdflfrgg hyyqyqsrvv ldvteqlsrf lwdhgdiafa
      121 plgklmlenf rlegnrgysk kvtivsvkrl lqdlgghqpw gcpwaslsrr lrrfsilggp
      181 vlsrsvsllm grllheelat rweqllmdea ftggalawlp grtaragqlv ypsggaldkl
      241 yfqevsvnsg gnprvledpg hiqlrgpvrq vvtstvqget llavrsdyhc avwkidkqep
      301 paplqvlqve kgatgislsp hlsgelaics rsgtvclwtp qdglqtiykd petlafrdps
      361 pwrwadftah prvltvgdrt gvkmvdiqgp pgcglllfca gaeaacqkge rvllaqylgq
      421 pgpastslhl ictqfsiylm derlplvpml kwdhglpsap llarllppas pgyprplllg
      481 gqggqvqllh iagegtsipq lagppqslps itdslsafpl lepkrqqqlq erleapvigl
      541 aaappcasap glllfqlsaa gdvfyqhlri qqtsslrepd hpaperpasr aaappvdqgs
      601 tpswtsrasa rcsrwlealm elsptnpvwa aptfshrrfl ghmerqksqe tlaqklqaam
      661 akgqllrpgd lgtlpkaepp papqcsqqde lterltkawe gqaaawwkrh qdqtsgsqrq
      721 skrpkrrtql sstfssftsy mdspdassap hsqdlsnsea cpqpprtpps qeltqelwaq
      781 gvqherrqtl rdymaklplq dnpgpvatpp sqtssrqtrs frqqtpvlsg shpprkkprm
      841 gf
//
LOCUS       NP_001017380             953 aa            linear   ROD 27-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase CYLD [Rattus norvegicus].
ACCESSION   NP_001017380 XP_232641
VERSION     NP_001017380.1
DBSOURCE    REFSEQ: accession NM_001017380.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Wang,H., Wu,B., Wang,H., Jiang,C. and Liu,Z.
  TITLE     LncRNA growth arrest specific transcript 5 inhibits the growth of
            pituitary neuroendocrine tumors via miR-27a-5p/cylindromatosis axis
  JOURNAL   Bioengineered 13 (4), 10274-10286 (2022)
   PUBMED   35435104
  REMARK    GeneRIF: LncRNA growth arrest specific transcript 5 inhibits the
            growth of pituitary neuroendocrine tumors via
            miR-27a-5p/cylindromatosis axis.
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Chen,Q., Lei,Y.Q., Liu,J.F., Wang,Z.C. and Cao,H.
  TITLE     Beneficial effects of chlorogenic acid treatment on
            neuroinflammation after deep hypothermic circulatory arrest may be
            mediated through CYLD/NF-kappaB signaling
  JOURNAL   Brain Res 1767, 147572 (2021)
   PUBMED   34216581
  REMARK    GeneRIF: Beneficial effects of chlorogenic acid treatment on
            neuroinflammation after deep hypothermic circulatory arrest may be
            mediated through CYLD/NF-kappaB signaling.
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Ji,Y.X., Huang,Z., Yang,X., Wang,X., Zhao,L.P., Wang,P.X.,
            Zhang,X.J., Alves-Bezerra,M., Cai,L., Zhang,P., Lu,Y.X., Bai,L.,
            Gao,M.M., Zhao,H., Tian,S., Wang,Y., Huang,Z.X., Zhu,X.Y.,
            Zhang,Y., Gong,J., She,Z.G., Li,F., Cohen,D.E. and Li,H.
  TITLE     The deubiquitinating enzyme cylindromatosis mitigates nonalcoholic
            steatohepatitis
  JOURNAL   Nat Med 24 (2), 213-223 (2018)
   PUBMED   29291351
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Ma,Q., Ruan,H., Peng,L., Zhang,M., Gack,M.U. and Yao,W.D.
  TITLE     Proteasome-independent polyubiquitin linkage regulates synapse
            scaffolding, efficacy, and plasticity
  JOURNAL   Proc Natl Acad Sci U S A 114 (41), E8760-E8769 (2017)
   PUBMED   28973854
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Yu,B., Liu,Z., Fu,Y., Wang,Y., Zhang,L., Cai,Z., Yu,F., Wang,X.,
            Zhou,J. and Kong,W.
  TITLE     CYLD Deubiquitinates Nicotinamide Adenine Dinucleotide Phosphate
            Oxidase 4 Contributing to Adventitial Remodeling
  JOURNAL   Arterioscler Thromb Vasc Biol 37 (9), 1698-1709 (2017)
   PUBMED   28751569
  REMARK    GeneRIF: CYLD contributes to the transdifferentiation of
            adventitial fibroblasts via deubiquitinating Nox4 and may play a
            role in vascular remodeling.
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Wooten,M.W., Geetha,T., Babu,J.R., Seibenhener,M.L., Peng,J.,
            Cox,N., Diaz-Meco,M.T. and Moscat,J.
  TITLE     Essential role of sequestosome 1/p62 in regulating accumulation of
            Lys63-ubiquitinated proteins
  JOURNAL   J Biol Chem 283 (11), 6783-6789 (2008)
   PUBMED   18174161
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Stegmeier,F., Sowa,M.E., Nalepa,G., Gygi,S.P., Harper,J.W. and
            Elledge,S.J.
  TITLE     The tumor suppressor CYLD regulates entry into mitosis
  JOURNAL   Proc Natl Acad Sci U S A 104 (21), 8869-8874 (2007)
   PUBMED   17495026
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Reiley,W.W., Zhang,M., Jin,W., Losiewicz,M., Donohue,K.B.,
            Norbury,C.C. and Sun,S.C.
  TITLE     Regulation of T cell development by the deubiquitinating enzyme
            CYLD
  JOURNAL   Nat Immunol 7 (4), 411-417 (2006)
   PUBMED   16501569
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Saito,K., Kigawa,T., Koshiba,S., Sato,K., Matsuo,Y., Sakamoto,A.,
            Takagi,T., Shirouzu,M., Yabuki,T., Nunokawa,E., Seki,E.,
            Matsuda,T., Aoki,M., Miyata,Y., Hirakawa,N., Inoue,M., Terada,T.,
            Nagase,T., Kikuno,R., Nakayama,M., Ohara,O., Tanaka,A. and
            Yokoyama,S.
  TITLE     The CAP-Gly domain of CYLD associates with the proline-rich
            sequence in NEMO/IKKgamma
  JOURNAL   Structure 12 (9), 1719-1728 (2004)
   PUBMED   15341735
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Bignell,G.R., Warren,W., Seal,S., Takahashi,M., Rapley,E.,
            Barfoot,R., Green,H., Brown,C., Biggs,P.J., Lakhani,S.R., Jones,C.,
            Hansen,J., Blair,E., Hofmann,B., Siebert,R., Turner,G., Evans,D.G.,
            Schrander-Stumpel,C., Beemer,F.A., van Den Ouweland,A., Halley,D.,
            Delpech,B., Cleveland,M.G., Leigh,I., Leisti,J. and Rasmussen,S.
  TITLE     Identification of the familial cylindromatosis tumour-suppressor
            gene
  JOURNAL   Nat Genet 25 (2), 160-165 (2000)
   PUBMED   10835629
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082001.1.
            
            On Apr 22, 2005 this sequence version replaced XP_232641.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082001.1, SRR8487231.48683.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..953
                     /product="ubiquitin carboxyl-terminal hydrolase CYLD"
                     /EC_number="3.4.19.12"
                     /note="probable ubiquitin carboxyl-terminal hydrolase
                     CYLD; ubiquitin thioesterase CYLD; deubiquitinating enzyme
                     CYLD; ubiquitin-specific-processing protease CYLD;
                     ubiquitin thiolesterase CYLD; retinitis pigmentosa 1
                     homolog; cylindromatosis (turban tumor syndrome); probable
                     ubiquitin carboxyl-terminal hydrolase CYLD-like; 40S
                     ribosomal protein S3a-like"
                     /calculated_mol_wt=106582
     Region          106..590
                     /region_name="Interaction with TRIP.
                     /evidence=ECO:0000250|UniProtKB:Q9NQC7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     Region          127..203
                     /region_name="CAP_GLY"
                     /note="Cytoskeleton-associated proteins (CAPs) are
                     involved in the organisation of microtubules and
                     transportation of vesicles and organelles along the
                     cytoskeletal network; smart01052"
                     /db_xref="CDD:214997"
     Region          232..>286
                     /region_name="CAP_GLY"
                     /note="Cytoskeleton-associated proteins (CAPs) are
                     involved in the organisation of microtubules and
                     transportation of vesicles and organelles along the
                     cytoskeletal network; smart01052"
                     /db_xref="CDD:214997"
     Region          304..460
                     /region_name="CYLD_phos_site"
                     /note="Phosphorylation region of CYLD, unstructured;
                     pfam16607"
                     /db_xref="CDD:465194"
     Region          318..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NQC7; propagated from
                     UniProtKB/Swiss-Prot (Q66H62.1)"
     Region          387..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     Region          391..466
                     /region_name="Interaction with TRAF2.
                     /evidence=ECO:0000250|UniProtKB:Q9NQC7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H62.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66H62.1)"
     Region          467..681
                     /region_name="Interaction with IKBKG/NEMO.
                     /evidence=ECO:0000250|UniProtKB:Q9NQC7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     Region          469..537
                     /region_name="CAP_GLY"
                     /note="Cytoskeleton-associated proteins (CAPs) are
                     involved in the organisation of microtubules and
                     transportation of vesicles and organelles along the
                     cytoskeletal network; smart01052"
                     /db_xref="CDD:214997"
     Region          590..945
                     /region_name="Peptidase_C19N"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02670"
                     /db_xref="CDD:239135"
     Site            order(593,598,868,887)
                     /site_type="active"
                     /db_xref="CDD:239135"
     Region          778..830
                     /region_name="B-box.
                     /evidence=ECO:0000250|UniProtKB:Q9NQC7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H62.1)"
     CDS             1..953
                     /gene="Cyld"
                     /gene_synonym="LRRGT00003; Rp1; Rp1h"
                     /coded_by="NM_001017380.1:196..3057"
                     /db_xref="GeneID:312937"
                     /db_xref="RGD:1308346"
ORIGIN      
        1 mssglwnqek vtspyweerl fylllqecsv tdkqtqkllr vpkgsigqyi qdrsvghsrv
       61 psakgkknqi glkileqpha vlfvdekdvv einekftell laitnceerl slfrnrirls
      121 kglqvdvgsp vrvqlrsgee kfpgvvrfrg pllaertvsg iffgvellee grgqgftdgv
      181 yqgkqlfqcd edcgvfvald kleliedddn glesdfagpg dtvqvepppl einsrvslkv
      241 gestesgtvi fcdvlpgkes lgyfvgvdmd npignwdgrf dgvqlcsfas vestvllhin
      301 diipdsvtqe rrppklafms rgvgdkgsss hnkpkvtgst sdpgsrnrse lfytlngssv
      361 dsqqqskskn pwyidevaed paksltemss dfghsspppq ppsmnslsse nrfhslpfsl
      421 tkmpntngsm ahsplslsvq svmgelnstp vqesppmpss sgnahglevg slaevkenpp
      481 fygvirwigq ppglsdvlag leledecagc tdgtfrgtry ftcalkkalf vklkscrpds
      541 rfaslqpvsn qiercnslaf ggylsevvee ntppkmekeg leimigkkkg iqghynscyl
      601 dstlfclfaf ssaldtvllr pkekndveyy setqellrte ivnplriygy vcatkimklr
      661 kilekveaas gftseekdpe eflnilfhdi lrvepllkir sagqkvqdcn fyqifmekne
      721 kvgvptiqql lewsfinsnl kfaeapscli iqmprfgkdf klfkkifpsl elnitdlled
      781 tprqcricgg lamyecrecy ddpdisagki kqfcktcstq vhlhprrlnh tyhpvslpkd
      841 lpdwdwrhgc ipcqkmelfa vlcietshyv afvkygkdds awlffdsmad rdggqngfni
      901 pqvtpcpevg eylkmsledl hsldsrriqg carrllcday mcmyqsptms lyk
//
LOCUS       NP_942077               1050 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase iota [Rattus norvegicus].
ACCESSION   NP_942077 XP_342660
VERSION     NP_942077.2
DBSOURCE    REFSEQ: accession NM_198782.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Yang,J., Seo,J., Nair,R., Han,S., Jang,S., Kim,K., Han,K.,
            Paik,S.K., Choi,J., Lee,S., Bae,Y.C., Topham,M.K., Prescott,S.M.,
            Rhee,J.S., Choi,S.Y. and Kim,E.
  TITLE     DGKiota regulates presynaptic release during mGluR-dependent LTD
  JOURNAL   EMBO J 30 (1), 165-180 (2011)
   PUBMED   21119615
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Regier,D.S., Higbee,J., Lund,K.M., Sakane,F., Prescott,S.M. and
            Topham,M.K.
  TITLE     Diacylglycerol kinase iota regulates Ras guanyl-releasing protein 3
            and inhibits Rap1 signaling
  JOURNAL   Proc Natl Acad Sci U S A 102 (21), 7595-7600 (2005)
   PUBMED   15894621
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Ito,T., Hozumi,Y., Sakane,F., Saino-Saito,S., Kanoh,H., Aoyagi,M.,
            Kondo,H. and Goto,K.
  TITLE     Cloning and characterization of diacylglycerol kinase iota splice
            variants in rat brain
  JOURNAL   J Biol Chem 279 (22), 23317-23326 (2004)
   PUBMED   15024004
  REMARK    GeneRIF: novel splice variants, which contain either insertion 1
            (71 bp) or insertion 2 (19 bp) or both in the carboxyl-terminal
            portion
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Sommer,W., Arlinde,C., Caberlotto,L., Thorsell,A., Hyytia,P. and
            Heilig,M.
  TITLE     Differential expression of diacylglycerol kinase iota and L18A
            mRNAs in the brains of alcohol-preferring AA and alcohol-avoiding
            ANA rats
  JOURNAL   Mol Psychiatry 6 (1), 103-8 (2001)
   PUBMED   11244494
  REMARK    GeneRIF: Diacylglycerol kinase iota is exclusively found in the
            brain and is expressed in a distinct regional pattern. Differential
            expression of splice variants in the cortex of alcohol accepting
            (AA) and alcohol non-accepting (ANA) rat lines.
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Ding,L., Traer,E., McIntyre,T.M., Zimmerman,G.A. and Prescott,S.M.
  TITLE     The cloning and characterization of a novel human diacylglycerol
            kinase, DGKiota
  JOURNAL   J Biol Chem 273 (49), 32746-32752 (1998)
   PUBMED   9830018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1, AB058962.1, AW526027.1 and CN544764.1.
            
            On Oct 19, 2007 this sequence version replaced NP_942077.1.
            
            Sequence Note: The RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB058962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..1050
                     /product="diacylglycerol kinase iota"
                     /EC_number="2.7.1.107"
                     /note="diglyceride kinase iota; DGK-iota; DAG kinase iota;
                     diacylglycerol kinase iota-3"
                     /calculated_mol_wt=115763
     Region          52..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAB7.1)"
     Region          163..235
                     /region_name="C1_DGKiota_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase iota (DAG kinase
                     iota) and similar proteins; cd20850"
                     /db_xref="CDD:410400"
     Region          244..318
                     /region_name="C1_DGKiota_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase iota (DAG kinase
                     iota) and similar proteins; cd20896"
                     /db_xref="CDD:410446"
     Region          325..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAB7.1)"
     Region          373..494
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          521..678
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          910..941
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <932..1049
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          943..972
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAB7.1)"
     Site            order(945,949..950,953..955,957..958,962,965,976,978,981,
                     985..986,989..991,993..994,998,1001,1010,1012,1014,
                     1018..1019,1022..1024,1026..1027,1031)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          945..976
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          978..1010
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          979..1008
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAB7.1)"
     Region          1048..1050
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:21119615"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAB7.1)"
     CDS             1..1050
                     /gene="Dgki"
                     /gene_synonym="rDGKi-3"
                     /coded_by="NM_198782.2:241..3393"
                     /db_xref="GeneID:688705"
                     /db_xref="RGD:735049"
ORIGIN      
        1 mdaagrgchl lplpaargpa rapaassals paglcsgtas assaaagava mnpsssagee
       61 rgatggssss gsgagscclg aeggvdprga gaaaaaalee paaagqkeke ealeeklrdl
      121 tfrkqvsyrk aisrtglqhl apahplglpv angpakepra tldwsenavn gehlwletnv
      181 sgdlcylgee ncqvrfaksa lrrkcavcki vvhtacieql ekinfrckpt freggsrspr
      241 enfvrhhwvh rrrqegkckq cgkgfqqkfs fhskeivais cswckqafhn kvtcfmlhhi
      301 eepcslgaha avivpptwii kvkkpqnslk asnrkkkrts fkrkaskrgt eqenkgrpfv
      361 ikpissplmk pllvfvnpks ggnqgtkvlq mfmwylnprq vfdlsqegpk dalelyrkvp
      421 nlrilacggd gtvgwilsil delqlspqpp vgvlplgtgn dlartlnwgg gytdepvski
      481 lcqvedgtiv qldrwnlhve rnpdlppeel edgvcklpln vfnnyfslgf dahvtlefhe
      541 sreanpekfn srfrnkmfya gaafsdflqr ssrdlskhvk vvcdgtdltp kiqdlkfqci
      601 vflnipryca gtmpwgnpgd hhdfepqrhd dgyievigft maslaalqvg ghgerlhqcr
      661 evmlltyksi pmqvdgepcr lapamirisl rnqanmvqks krrtsmplln dpqsvpdrlr
      721 irvnkislqd yeglhydkek lreasiplgi lvvrgdcdle tcrmyidrlq edlqsvssgs
      781 qrvhyqdqet sfpraisaqr lsprwcflda tsadrfyrid rsqehlhfvm eishdeifil
      841 dpdmvvsqqa gtppgmpdlv veqasglsdw wnpalrkrml sdsgmitphy edsdlkdfsh
      901 srvlqspvss edhailqavi tgdlmklmes yknggslliq gpghcsllhy aaktgngeiv
      961 kyildhgpae lldmadsetg etalhkaacq rnravcqllv dagaslrqtd skgktpqera
     1021 qqagdpdlaa ylesrqnyki ighedletav
//
LOCUS       NP_001004083             415 aa            linear   ROD 27-APR-2025
DEFINITION  prolyl hydroxylase EGLN2 [Rattus norvegicus].
ACCESSION   NP_001004083
VERSION     NP_001004083.1
DBSOURCE    REFSEQ: accession NM_001004083.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Li,S., Fu,J., Wang,Y., Hu,C. and Xu,F.
  TITLE     LncRNA MIAT enhances cerebral ischaemia/reperfusion injury in rat
            model via interacting with EGLN2 and reduces its ubiquitin-mediated
            degradation
  JOURNAL   J Cell Mol Med 25 (21), 10140-10151 (2021)
   PUBMED   34687132
  REMARK    GeneRIF: LncRNA MIAT enhances cerebral ischaemia/reperfusion injury
            in rat model via interacting with EGLN2 and reduces its
            ubiquitin-mediated degradation.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Chen,Y.F., Pandey,S., Day,C.H., Chen,Y.F., Jiang,A.Z., Ho,T.J.,
            Chen,R.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     Synergistic effect of HIF-1alpha and FoxO3a trigger cardiomyocyte
            apoptosis under hyperglycemic ischemia condition
  JOURNAL   J Cell Physiol 233 (4), 3660-3671 (2018)
   PUBMED   29030976
  REMARK    GeneRIF: that combined function of HIF-1alpha and FoxO3a under high
            glucose plus hypoxia condition lead to enhanced expression of BNIP3
            inducing cardiomyocyte death
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Ahmed,S., Ayscough,A., Barker,G.R., Canning,H.E., Davenport,R.,
            Downham,R., Harrison,D., Jenkins,K., Kinsella,N., Livermore,D.G.,
            Wright,S., Ivetac,A.D., Skene,R., Wilkens,S.J., Webster,N.A. and
            Hendrick,A.G.
  TITLE     1,2,4-Triazolo-[1,5-a]pyridine HIF Prolylhydroxylase Domain-1
            (PHD-1) Inhibitors With a Novel Monodentate Binding Interaction
  JOURNAL   J Med Chem 60 (13), 5663-5672 (2017)
   PUBMED   28594552
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Laitala,A., Aro,E., Walkinshaw,G., Maki,J.M., Rossi,M.,
            Heikkila,M., Savolainen,E.R., Arend,M., Kivirikko,K.I., Koivunen,P.
            and Myllyharju,J.
  TITLE     Transmembrane prolyl 4-hydroxylase is a fourth prolyl 4-hydroxylase
            regulating EPO production and erythropoiesis
  JOURNAL   Blood 120 (16), 3336-3344 (2012)
   PUBMED   22955912
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Hsieh,Y.L., Chou,L.W., Chang,P.L., Yang,C.C., Kao,M.J. and
            Hong,C.Z.
  TITLE     Low-level laser therapy alleviates neuropathic pain and promotes
            function recovery in rats with chronic constriction injury:
            possible involvements in hypoxia-inducible factor 1alpha
            (HIF-1alpha)
  JOURNAL   J Comp Neurol 520 (13), 2903-2916 (2012)
   PUBMED   22351621
  REMARK    GeneRIF: In conclusion, a low-level laser could modulate HIF-1alpha
            activity in nerve entrapment neuropathy
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Metzen,E., Berchner-Pfannschmidt,U., Stengel,P., Marxsen,J.H.,
            Stolze,I., Klinger,M., Huang,W.Q., Wotzlaw,C., Hellwig-Burgel,T.,
            Jelkmann,W., Acker,H. and Fandrey,J.
  TITLE     Intracellular localisation of human HIF-1 alpha hydroxylases:
            implications for oxygen sensing
  JOURNAL   J Cell Sci 116 (Pt 7), 1319-1326 (2003)
   PUBMED   12615973
REFERENCE   7  (residues 1 to 415)
  AUTHORS   McNeill,L.A., Hewitson,K.S., Gleadle,J.M., Horsfall,L.E.,
            Oldham,N.J., Maxwell,P.H., Pugh,C.W., Ratcliffe,P.J. and
            Schofield,C.J.
  TITLE     The use of dioxygen by HIF prolyl hydroxylase (PHD1)
  JOURNAL   Bioorg Med Chem Lett 12 (12), 1547-1550 (2002)
   PUBMED   12039559
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Seth,P., Krop,I., Porter,D. and Polyak,K.
  TITLE     Novel estrogen and tamoxifen induced genes identified by SAGE
            (Serial Analysis of Gene Expression)
  JOURNAL   Oncogene 21 (5), 836-843 (2002)
   PUBMED   11850811
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Bruick,R.K. and McKnight,S.L.
  TITLE     A conserved family of prolyl-4-hydroxylases that modify HIF
  JOURNAL   Science 294 (5545), 1337-1340 (2001)
   PUBMED   11598268
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Epstein,A.C., Gleadle,J.M., McNeill,L.A., Hewitson,K.S.,
            O'Rourke,J., Mole,D.R., Mukherji,M., Metzen,E., Wilson,M.I.,
            Dhanda,A., Tian,Y.M., Masson,N., Hamilton,D.L., Jaakkola,P.,
            Barstead,R., Hodgkin,J., Maxwell,P.H., Pugh,C.W., Schofield,C.J.
            and Ratcliffe,P.J.
  TITLE     C. elegans EGL-9 and mammalian homologs define a family of
            dioxygenases that regulate HIF by prolyl hydroxylation
  JOURNAL   Cell 107 (1), 43-54 (2001)
   PUBMED   11595184
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078907.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..415
                     /product="prolyl hydroxylase EGLN2"
                     /EC_number="1.14.11.29"
                     /note="HIF-1alpha prolyl-4-hydroxylase-1; HIF-prolyl
                     hydroxylase 1; hypoxia-inducible factor prolyl hydroxylase
                     1; prolyl hydroxylase domain-containing protein 1"
                     /calculated_mol_wt=44550
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU4.1)"
     Region          43..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU4.1)"
     Region          89..134
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q96KS0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU4.1)"
     Region          108..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU4.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96KS0; propagated from
                     UniProtKB/Swiss-Prot (Q6AYU4.1)"
     Region          213..383
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Region          233..243
                     /region_name="Beta(2)beta(3) 'finger-like' loop.
                     /evidence=ECO:0000250|UniProtKB:Q9GZT9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU4.1)"
     CDS             1..415
                     /gene="Egln2"
                     /gene_synonym="HIF-PH1; HPH-1; HPH-3; PHD-1; PHD1"
                     /coded_by="NM_001004083.1:271..1518"
                     /db_xref="GeneID:308457"
                     /db_xref="RGD:631376"
ORIGIN      
        1 mdspcqpqal nqalpqlpgs vseslepsra rmgvesylpc pllpsyhrsg asgeasagng
       61 tprttatatt ttasplregf ggqdggelwp lqsegaaalv tkecqrlaaq garpeapkrk
      121 wakdggdaps pskrpwarqe nqeakgesgv gcdsgggssn stthssgeas srlreeaqps
      181 aperlaldyi vpcmryygic vkdnflgavl ggrvlaevea lkwggrlrdg qlvsqraipp
      241 rsirgdqiaw veghepgcrs igalmahvda virhcagrlg nyvingrtka mvacypgngl
      301 gyvrhvdnph gdgrcitciy ylnqnwdvkv hggllqifpe grpvvaniep lfdrllifws
      361 drrnphevkp ayatryaitv wyfdakeraa ardkyqlasg qkgvqvpvsq patpt
//
LOCUS       NP_062004                251 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.11br [Rattus norvegicus].
ACCESSION   NP_062004
VERSION     NP_062004.1
DBSOURCE    REFSEQ: accession NM_019131.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO562261.1, BC078780.1,
            M34134.1 and AA899493.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.11, also known as variant 6)
            has a different 5' UTR and 5' coding region compared to variant 1.
            The resulting protein (isoform Tpm1.11br, also referred to as
            TMBr-2) has a distinct N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M34134.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..251
                     /product="tropomyosin alpha-1 chain isoform Tpm1.11br"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=28573
     Region          12..223
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..251
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_019131.2:152..907"
                     /note="isoform Tpm1.11br is encoded by transcript variant
                     Tpm1.11"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeerags lqreldqerk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedkyeeeik vlsdklkeae traefaersv tkleksiddl edkflcfspp ktpsssrmsh
      241 lselciclls s
//
LOCUS       NP_001007696             566 aa            linear   ROD 27-APR-2025
DEFINITION  T-complex protein 11 homolog [Rattus norvegicus].
ACCESSION   NP_001007696 XP_228029
VERSION     NP_001007696.1
DBSOURCE    REFSEQ: accession NM_001007695.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Stanger,S.J., Law,E.A., Jamsai,D., O'Bryan,M.K., Nixon,B.,
            McLaughlin,E.A., Aitken,R.J. and Roman,S.D.
  TITLE     A novel germ cell protein, SPIF (sperm PKA interacting factor), is
            essential for the formation of a PKA/TCP11 complex that undergoes
            conformational and phosphorylation changes upon capacitation
  JOURNAL   FASEB J 30 (8), 2777-2791 (2016)
   PUBMED   27105888
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Liu,Y., Jiang,M., Li,C., Yang,P., Sun,H., Tao,D., Zhang,S. and
            Ma,Y.
  TITLE     Human t-complex protein 11 (TCP11), a testis-specific gene product,
            is a potential determinant of the sperm morphology
  JOURNAL   Tohoku J Exp Med 224 (2), 111-117 (2011)
   PUBMED   21597245
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Adeoya-Osiguwa,S.A., Dudley,R.K., Hosseini,R. and Fraser,L.R.
  TITLE     FPP modulates mammalian sperm function via TCP-11 and the adenylyl
            cyclase/cAMP pathway
  JOURNAL   Mol Reprod Dev 51 (4), 468-476 (1998)
   PUBMED   9820206
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Fraser,L.R., Hosseini,R., Hanyalogou,A., Talmor,A. and Dudley,R.K.
  TITLE     TCP-11, the product of a mouse t-complex gene, plays a role in
            stimulation of capacitation and inhibition of the spontaneous
            acrosome reaction
  JOURNAL   Mol Reprod Dev 48 (3), 375-382 (1997)
   PUBMED   9322250
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083899.1.
            
            On Nov 29, 2004 this sequence version replaced XP_228029.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..566
                     /product="T-complex protein 11 homolog"
                     /calculated_mol_wt=62481
     Region          1..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI00.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI00.1)"
     Region          132..550
                     /region_name="Tcp11"
                     /note="T-complex protein 11; pfam05794"
                     /db_xref="CDD:461743"
     Region          328..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI00.1)"
     Site            393..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI00.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI00.1)"
     CDS             1..566
                     /gene="Tcp11"
                     /coded_by="NM_001007695.1:59..1759"
                     /db_xref="GeneID:309641"
                     /db_xref="RGD:1359387"
ORIGIN      
        1 mpdlkeraar kepgaaesas resrggntre sassaqghrs rrfnrrssta altpgsaqgr
       61 gvqtaprapv ghgglrtglt srcpqpsara klpsvtrgap lppspgkghf gatpishrlg
      121 ltervhdask ldchledrks asslesrgke vmpsdfwdhl keqlsavppd fscalellke
      181 ikeillslll prqsrlrnei eealdmeflh qqadrgdlnv sylskyilnm mvllcapvrd
      241 eavqrlenis dpvrllrgif qvlgqmkmdm vnytiqslqp qlqehsiqfe raqfqerlnk
      301 dpsllnhttk wltqaatqli apsgscydiq dpssssgpsp sdiaipepls pamvlsqgfl
      361 nlltwdpene efpetlladr srlqelesqq nqltilasvl lvassfsgsv lfgspqfvdr
      421 lkritkslve dfnsrpeevm qtvsdqvtee ihqslknmgl splssentds ligqlqniak
      481 kencvrsvid qrihlflkcc fvlgvqrsll dlpgglslie aelaelgqkf vslthhnqqv
      541 fapyyteilk tlinpvqtlt tkvgsl
//
LOCUS       NP_001007721             454 aa            linear   ROD 27-APR-2025
DEFINITION  Golgi reassembly-stacking protein 2 [Rattus norvegicus].
ACCESSION   NP_001007721 NP_620184 XP_346654 XP_579651
VERSION     NP_001007721.1
DBSOURCE    REFSEQ: accession NM_001007720.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Piao,H., Kim,J., Noh,S.H., Kweon,H.S., Kim,J.Y. and Lee,M.G.
  TITLE     Sec16A is critical for both conventional and unconventional
            secretion of CFTR
  JOURNAL   Sci Rep 7, 39887 (2017)
   PUBMED   28067262
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Kim,J., Noh,S.H., Piao,H., Kim,D.H., Kim,K., Cha,J.S., Chung,W.Y.,
            Cho,H.S., Kim,J.Y. and Lee,M.G.
  TITLE     Monomerization and ER Relocalization of GRASP Is a Requisite for
            Unconventional Secretion of CFTR
  JOURNAL   Traffic 17 (7), 733-753 (2016)
   PUBMED   27062250
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Feng,Y., Yu,W., Li,X., Lin,S., Zhou,Y., Hu,J. and Liu,X.
  TITLE     Structural insight into Golgi membrane stacking by GRASP65 and
            GRASP55 proteins
  JOURNAL   J Biol Chem 288 (39), 28418-28427 (2013)
   PUBMED   23940043
  REMARK    GeneRIF: GRASP65 and GRASP55 proteins have roles in Golgi membrane
            stacking
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Truschel,S.T., Zhang,M., Bachert,C., Macbeth,M.R. and Linstedt,A.D.
  TITLE     Allosteric regulation of GRASP protein-dependent Golgi membrane
            tethering by mitotic phosphorylation
  JOURNAL   J Biol Chem 287 (24), 19870-19875 (2012)
   PUBMED   22523075
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Gee,H.Y., Noh,S.H., Tang,B.L., Kim,K.H. and Lee,M.G.
  TITLE     Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent
            unconventional secretion pathway
  JOURNAL   Cell 146 (5), 746-760 (2011)
   PUBMED   21884936
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Duran,J.M., Kinseth,M., Bossard,C., Rose,D.W., Polishchuk,R.,
            Wu,C.C., Yates,J., Zimmerman,T. and Malhotra,V.
  TITLE     The role of GRASP55 in Golgi fragmentation and entry of cells into
            mitosis
  JOURNAL   Mol Biol Cell 19 (6), 2579-2587 (2008)
   PUBMED   18385516
  REMARK    GeneRIF: GRASP55 has no role in the organization of Golgi membranes
            per se, but it controls their fragmentation by regulating the
            release of a partner, which requires a G2-specific phosphorylation
            at T225/T249.
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Wu,C.C., MacCoss,M.J., Mardones,G., Finnigan,C., Mogelsvang,S.,
            Yates,J.R. 3rd and Howell,K.E.
  TITLE     Organellar proteomics reveals Golgi arginine dimethylation
  JOURNAL   Mol Biol Cell 15 (6), 2907-2919 (2004)
   PUBMED   15047867
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Barr,F.A., Preisinger,C., Kopajtich,R. and Korner,R.
  TITLE     Golgi matrix proteins interact with p24 cargo receptors and aid
            their efficient retention in the Golgi apparatus
  JOURNAL   J Cell Biol 155 (6), 885-891 (2001)
   PUBMED   11739402
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Short,B., Preisinger,C., Korner,R., Kopajtich,R., Byron,O. and
            Barr,F.A.
  TITLE     A GRASP55-rab2 effector complex linking Golgi structure to membrane
            traffic
  JOURNAL   J Cell Biol 155 (6), 877-883 (2001)
   PUBMED   11739401
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Shorter,J., Watson,R., Giannakou,M.E., Clarke,M., Warren,G. and
            Barr,F.A.
  TITLE     GRASP55, a second mammalian GRASP protein involved in the stacking
            of Golgi cisternae in a cell-free system
  JOURNAL   EMBO J 18 (18), 4949-4960 (1999)
   PUBMED   10487747
  REMARK    GeneRIF: Identification of GRASP55, and demonstration that it
            functions in the stacking of Golgi cisternae in a similar manner to
            the related protein GRASP65.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078731.1.
            
            On or before Oct 20, 2005 this sequence version replaced
            NP_620184.1, XP_346654.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078731.1, AF110267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q22"
     Protein         1..454
                     /product="Golgi reassembly-stacking protein 2"
                     /note="golgi reassembly-stacking protein of 55 kDa; Golgi
                     reassembly-stacking protein 2-like"
                     /calculated_mol_wt=47179
     Region          <14..100
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          15..215
                     /region_name="GRASP.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            30
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000269|PubMed:15047867; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            47
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000269|PubMed:15047867; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Region          69..204
                     /region_name="GRASP55_65"
                     /note="GRASP55/65 PDZ-like domain; pfam04495"
                     /db_xref="CDD:427981"
     Region          194..199
                     /region_name="Important for membrane binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Region          <217..422
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Region          377..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JX3; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JX3; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8Y8; propagated from
                     UniProtKB/Swiss-Prot (Q9R064.3)"
     CDS             1..454
                     /gene="Gorasp2"
                     /gene_synonym="GRASP55; Grs2"
                     /coded_by="NM_001007720.1:29..1393"
                     /db_xref="GeneID:113961"
                     /db_xref="RGD:619911"
ORIGIN      
        1 mgssqsveip gggtegyhvl rvqenspghr aglepffdfi vsingsrlnk dndtlkdllk
       61 anvekpvkml iyssktlelr easvtpsnlw ggqgllgvsi rfcsfdgane nvwhvleves
      121 nspaalaglr phsdyiigad tvmnesedlf slietheakp lklyvyntdt dncreviitp
      181 nsawggegsl gcgigygylh riptrpfeeg kkislpgqmt gtpmtppkdg ftevqlssvs
      241 ppslsppgta gveqslsgls issappavsn vlstgvptvp llppqvnqsl asvppmnpaa
      301 tlpslmplsa glpslpnlps lsnfnlpaph impgvglpel gkpglpplps lpprnlpgia
      361 plpmpsdflp sfplvpegss aasageplss lpamgppsdp vmttakadts sltvdvmspa
      421 skvpttvedr vsdctpamek pvsavtdana seas
//
LOCUS       NP_001008367             340 aa            linear   ROD 27-APR-2025
DEFINITION  centromere protein N [Rattus norvegicus].
ACCESSION   NP_001008367 XP_341696
VERSION     NP_001008367.1
DBSOURCE    REFSEQ: accession NM_001008366.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085839.1.
            
            On Dec 16, 2004 this sequence version replaced XP_341696.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085839.1, SRR8487231.114351.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..340
                     /product="centromere protein N"
                     /note="CENP-N"
                     /calculated_mol_wt=39328
     Region          4..340
                     /region_name="CENP-N"
                     /note="Kinetochore protein CHL4 like; pfam05238"
                     /db_xref="CDD:398764"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96H22; propagated from
                     UniProtKB/Swiss-Prot (Q5U2W4.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96H22; propagated from
                     UniProtKB/Swiss-Prot (Q5U2W4.1)"
     CDS             1..340
                     /gene="Cenpn"
                     /gene_synonym="Da2-27; Da2-4; RGD1310953"
                     /coded_by="NM_001008366.1:216..1238"
                     /db_xref="GeneID:361416"
                     /db_xref="RGD:1310953"
ORIGIN      
        1 mdenvaeflr riilkiplce mktileawdf lsedqlqsin lkqrkeflaq evillcedkc
       61 aslddmalld lmytqfhrhq klwnvfqmsk epggndvdlf dmeqfqssfk rilqralknv
      121 tvsfrvyekn svwirvawgt qysqpnqykp tfvvyypqtp yvfisscylk stvpllhqal
      181 kvaskhhqma qldlrsrhld sltaivfney dqtfenynst aswregslgl ktdldskiih
      241 enteekvrih ratqeafgay pqpqlefaqy kletkfksdv gggiladrke plrclvkfss
      301 phllealksl apagiadtpl splltcipsk kmnyfkirdk
//
LOCUS       NP_001102589             445 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin beta-2A chain [Rattus norvegicus].
ACCESSION   NP_001102589 XP_001060757 XP_574013
VERSION     NP_001102589.1
DBSOURCE    REFSEQ: accession NM_001109119.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   2  (residues 1 to 445)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Ginzburg,I., Teichman,A., Dodemont,H.J., Behar,L. and Littauer,U.Z.
  TITLE     Regulation of three beta-tubulin mRNAs during rat brain development
  JOURNAL   EMBO J 4 (13B), 3667-3673 (1985)
   PUBMED   2868892
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473977.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_574013.2, XP_001060757.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..445
                     /product="tubulin beta-2A chain"
                     /note="Tubulin beta-2B chain; T beta-15; tubulin beta-2A
                     chain pseudogene"
                     /calculated_mol_wt=49776
     Region          1..430
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (P85108.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P99024; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q13885; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Site            318
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P07437; propagated from
                     UniProtKB/Swiss-Prot (P85108.1)"
     Region          422..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P85108.1)"
     CDS             1..445
                     /gene="Tubb2a"
                     /gene_synonym="Tubb2b"
                     /coded_by="NM_001109119.1:78..1415"
                     /db_xref="GeneID:498736"
                     /db_xref="RGD:1588452"
ORIGIN      
        1 mreivhiqag qcgnqigakf wevisdehgi dptgsyhgds dlqlerinvy yneaagnkyv
       61 prailvdlep gtmdsvrsgp fgqifrpdnf vfgqsgagnn wakghytega elvdsvldvv
      121 rkesescdcl qgfqlthslg ggtgsgmgtl liskireeyp drimntfsvm pspkvsdtvv
      181 epynatlsvh qlventdety sidnealydi cfrtlklttp tygdlnhlvs atmsgvttcl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltsrgsqq yraltvpelt qqmfdsknmm
      301 aacdprhgry ltvaaifrgr msmkevdeqm lnvqnknssy fvewipnnvk tavcdipprg
      361 lkmsatfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata deqgefeeee gedea
//
LOCUS       NP_058883                210 aa            linear   ROD 27-APR-2025
DEFINITION  high mobility group protein B2 [Rattus norvegicus].
ACCESSION   NP_058883 XP_001054623 XP_573903
VERSION     NP_058883.1
DBSOURCE    REFSEQ: accession NM_017187.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kong,D., Liu,J., Lu,J., Zeng,C., Chen,H., Duan,Z., Yu,K., Zheng,X.,
            Zou,P., Zhou,L., Lv,Y., Zeng,Q., Lu,L., Li,J. and He,Y.
  TITLE     HMGB2 Release Promotes Pulmonary Hypertension and Predicts Severity
            and Mortality of Patients With Pulmonary Arterial Hypertension
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (6), e172-e195 (2024)
   PUBMED   38572649
  REMARK    GeneRIF: HMGB2 Release Promotes Pulmonary Hypertension and Predicts
            Severity and Mortality of Patients With Pulmonary Arterial
            Hypertension.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Yang,P., He,J., Wang,C., Yang,C. and Jian,F.
  TITLE     Downregulation of High mobility group box 2 relieves spinal cord
            injury by inhibiting microglia-mediated neuroinflammation
  JOURNAL   Exp Anim 72 (2), 199-208 (2023)
   PUBMED   36503880
  REMARK    GeneRIF: Downregulation of High mobility group box 2 relieves
            spinal cord injury by inhibiting microglia-mediated
            neuroinflammation.
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Lee,D., Taniguchi,N., Sato,K., Choijookhuu,N., Hishikawa,Y.,
            Kataoka,H., Morinaga,H., Lotz,M. and Chosa,E.
  TITLE     HMGB2 is a novel adipogenic factor that regulates ectopic fat
            infiltration in skeletal muscles
  JOURNAL   Sci Rep 8 (1), 9601 (2018)
   PUBMED   29942000
  REMARK    GeneRIF: the enhance expression of HMGB2 induces the adipogenesis
            of MSCs and the fat infiltration into skeletal muscles through the
            cascade of HMGB2-PDGFRA
            Erratum:[Sci Rep. 2020 Mar 10;10(1):4647. doi:
            10.1038/s41598-020-61550-w. PMID: 32157195]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Lee,S., Nam,Y., Koo,J.Y., Lim,D., Park,J., Ock,J., Kim,J., Suk,K.
            and Park,S.B.
  TITLE     A small molecule binding HMGB1 and HMGB2 inhibits
            microglia-mediated neuroinflammation
  JOURNAL   Nat Chem Biol 10 (12), 1055-1060 (2014)
   PUBMED   25306442
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Abraham,A.B., Bronstein,R., Reddy,A.S., Maletic-Savatic,M.,
            Aguirre,A. and Tsirka,S.E.
  TITLE     Aberrant neural stem cell proliferation and increased adult
            neurogenesis in mice lacking chromatin protein HMGB2
  JOURNAL   PLoS One 8 (12), e84838 (2013)
   PUBMED   24391977
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Beliavtseva,L.M., Kozlov,S.V., Kulikova,O.G., Surkova,E.A. and
            Fedorova,N.A.
  TITLE     [Effect of HMG proteins and their phosphorylated forms on the
            process of transcription in neuronal nuclei of the rat brain (data
            from an immunochemical analysis)]
  JOURNAL   Biokhimiia 57 (2), 214-219 (1992)
   PUBMED   1525238
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Mosevitsky,M.I., Novitskaya,V.A., Iogannsen,M.G. and
            Zabezhinsky,M.A.
  TITLE     Tissue specificity of nucleo-cytoplasmic distribution of HMG1 and
            HMG2 proteins and their probable functions
  JOURNAL   Eur J Biochem 185 (2), 303-310 (1989)
   PUBMED   2583185
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Waga,S., Mizuno,S. and Yoshida,M.
  TITLE     Nonhistone proteins HMG1 and HMG2 suppress the nucleosome assembly
            at physiological ionic strength
  JOURNAL   Biochim Biophys Acta 1007 (2), 209-214 (1989)
   PUBMED   2465778
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Kuehl,L.
  TITLE     Synthesis of high mobility group proteins in regenerating rat liver
  JOURNAL   J Biol Chem 254 (15), 7276-7281 (1979)
   PUBMED   457681
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Chiou,W.L. and Niazi,S.
  TITLE     Pharmaceutical applications of solid dispersion systems:
            dissolution of griseofulvin-succinic acid eutectic mixture
  JOURNAL   J Pharm Sci 65 (8), 1212-1214 (1976)
   PUBMED   978439
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089854.1.
            
            On or before Oct 27, 2007 this sequence version replaced
            XP_573903.2, XP_001054623.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089854.1, FQ225084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132300, SAMD00132302
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p11"
     Protein         1..210
                     /product="high mobility group protein B2"
                     /note="HMG-2; high mobility group protein 2"
                     /calculated_mol_wt=24028
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63159; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P26583; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26583; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Region          51..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52925.2)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Region          93..163
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156,159,162..163)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09429; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P30681; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P52925.2)"
     Region          162..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52925.2)"
     Region          165..180
                     /region_name="Required for chemotactic activity.
                     /evidence=ECO:0000250|UniProtKB:P26583"
                     /note="propagated from UniProtKB/Swiss-Prot (P52925.2)"
     CDS             1..210
                     /gene="Hmgb2"
                     /gene_synonym="Hmg2"
                     /coded_by="NM_017187.2:153..785"
                     /db_xref="GeneID:29395"
                     /db_xref="RGD:69291"
ORIGIN      
        1 mgkgdpnkpr gkmssyaffv qtcreehkkk hpdssvnfae fskkcserwk tmsakekskf
       61 edlaksdkar ydremknyvp pkgdkkgkkk dpnapkrpps afflfcsehr pkiksehpgl
      121 sigdtakklg emwseqsakd kqpyeqkaak lkekyekdia ayrakgksev gkkgpgrptg
      181 skkknepede eeeeeeedde deeeededee
//
LOCUS       NP_001099603             669 aa            linear   ROD 27-APR-2025
DEFINITION  dymeclin [Rattus norvegicus].
ACCESSION   NP_001099603 XP_001054727 XP_214529
VERSION     NP_001099603.2
DBSOURCE    REFSEQ: accession NM_001106133.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Denais,C., Dent,C.L., Southgate,L., Hoyle,J., Dafou,D.,
            Trembath,R.C. and Machado,R.D.
  TITLE     Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome,
            encodes a protein integral to extracellular matrix and golgi
            organization and is associated with protein secretion pathways
            critical in bone development
  JOURNAL   Hum Mutat 32 (2), 231-239 (2011)
   PUBMED   21280149
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Cohn,D.H., Ehtesham,N., Krakow,D., Unger,S., Shanske,A.,
            Reinker,K., Powell,B.R. and Rimoin,D.L.
  TITLE     Mental retardation and abnormal skeletal development
            (Dyggve-Melchior-Clausen dysplasia) due to mutations in a novel,
            evolutionarily conserved gene
  JOURNAL   Am J Hum Genet 72 (2), 419-428 (2003)
   PUBMED   12491225
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB712341.1, BC098944.1, EV765460.1, JAXUCZ010000018.1, DV722630.1
            and CO558582.1.
            
            On Oct 12, 2007 this sequence version replaced NP_001099603.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..669
                     /product="dymeclin"
                     /calculated_mol_wt=75917
     Region          1..646
                     /region_name="Dymeclin"
                     /note="Dyggve-Melchior-Clausen syndrome protein;
                     pfam09742"
                     /db_xref="CDD:462873"
     CDS             1..669
                     /gene="Dym"
                     /gene_synonym="RGD1309111"
                     /coded_by="NM_001106133.2:265..2274"
                     /db_xref="GeneID:291433"
                     /db_xref="RGD:1309111"
ORIGIN      
        1 mgsnsskisd lpkneylkrl sgpeaisend pfwnqlfsfs fsaptsstel klleeatisv
       61 ckslvennpr tgnlaaltkv flartrelrl saecqnhifi wqthnalfii ccllkvfice
      121 mseeelqlhf tyeeklpgty ssdsedllee llcsliqlit dtpllditye isveaisami
      181 vflscqlfhk evlrqsishk ylmqgpclpy tsklvktlly nfirqekppp pgthvfpqqs
      241 dgggllygla sgvatglwtv ftlggvgska aspeltspla nqslllllvl vnltdapdip
      301 npyrqavtsf kntqdsspfp ssvphtfqin fnslyttlce qqtsdqatll lytllhqnan
      361 vrtymlartd menlvlpile ilyhveerns hhvymaliil lilteddgfn rsihevilkn
      421 itwyservlt eislgsllil vvirtiqynm trtrdkylht nclaalanms aqfrslhqya
      481 aqriislfsl lskkhnkvle qatqqadsvt fvrlsdlqsp vaqdlsviee virmmleiin
      541 scltnslhhn pnlvyallyk rdlfeqfrth psfqdimqni dlvisffssr llqsgaelsv
      601 ervleiikqg vvalpkdrlk kfpelkfkyv eeeqpeeffi pyvwslvyns avglywnpqd
      661 iqlfamdsd
//
LOCUS       NP_001076010             285 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein D0 isoform d [Rattus
            norvegicus].
ACCESSION   NP_001076010
VERSION     NP_001076010.1
DBSOURCE    REFSEQ: accession NM_001082541.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Yan,J., Du,F., Li,S.D., Yuan,Y., Jiang,J.Y., Li,S., Li,X.Y. and
            Du,Z.X.
  TITLE     AUF1 modulates TGF-beta signal in renal tubular epithelial cells
            via post-transcriptional regulation of Nedd4L expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (1), 48-56 (2018)
   PUBMED   28986222
  REMARK    GeneRIF: AUF1 might be a potential player in renal
            tubulointerstitial fibrosis through modulation of TGF-beta signal
            transduction via posttranscriptional regulation of Nedd4L.
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Castellanos-Rubio,A., Fernandez-Jimenez,N., Kratchmarov,R., Luo,X.,
            Bhagat,G., Green,P.H., Schneider,R., Kiledjian,M., Bilbao,J.R. and
            Ghosh,S.
  TITLE     A long noncoding RNA associated with susceptibility to celiac
            disease
  JOURNAL   Science 352 (6281), 91-95 (2016)
   PUBMED   27034373
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Lee,K.H., Kim,S.H., Kim,H.J., Kim,W., Lee,H.R., Jung,Y., Choi,J.H.,
            Hong,K.Y., Jang,S.K. and Kim,K.T.
  TITLE     AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
            translation
  JOURNAL   Nucleic Acids Res 42 (6), 3590-3606 (2014)
   PUBMED   24423872
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Raineri,I., Wegmueller,D., Gross,B., Certa,U. and Moroni,C.
  TITLE     Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover
            studied by RNA interference
  JOURNAL   Nucleic Acids Res 32 (4), 1279-1288 (2004)
   PUBMED   14976220
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Arao,Y., Kikuchi,A., Ikeda,K., Nomoto,S., Horiguchi,H. and
            Kayama,F.
  TITLE     A+U-rich-element RNA-binding factor 1/heterogeneous nuclear
            ribonucleoprotein D gene expression is regulated by oestrogen in
            the rat uterus
  JOURNAL   Biochem J 361 (Pt 1), 125-132 (2002)
   PUBMED   11742537
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Ehrenman,K., Long,L., Wagner,B.J. and Brewer,G.
  TITLE     Characterization of cDNAs encoding the murine A+U-rich RNA-binding
            protein AUF1
  JOURNAL   Gene 149 (2), 315-319 (1994)
   PUBMED   7959009
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Ishikawa,F., Matunis,M.J., Dreyfuss,G. and Cech,T.R.
  TITLE     Nuclear proteins that bind the pre-mRNA 3' splice site sequence
            r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
  JOURNAL   Mol Cell Biol 13 (7), 4301-4310 (1993)
   PUBMED   8321232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO560068.1, AB046618.1 and CB798484.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB046618.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..285
                     /product="heterogeneous nuclear ribonucleoprotein D0
                     isoform d"
                     /note="heterogeneous nuclear ribonucleoprotein D0; hnRNP
                     D0; AU-rich element RNA-binding protein 1; AU-rich element
                     RNA-binding factor 1; RNA binding protein p45AUF1"
                     /calculated_mol_wt=30365
     Region          <55..76
                     /region_name="CBFNT"
                     /note="CBFNT (NUC161) domain; pfam08143"
                     /db_xref="CDD:311868"
     Region          78..151
                     /region_name="RRM1_hnRNPD"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12756"
                     /db_xref="CDD:410150"
     Region          162..236
                     /region_name="RRM2_hnRNPD"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12583"
                     /db_xref="CDD:241027"
     Site            order(162,164,166..167,191..194,196..197,200..202,204,206,
                     223,230..232,234..236)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:241027"
     CDS             1..285
                     /gene="Hnrnpd"
                     /gene_synonym="Auf1; Hnrpd"
                     /coded_by="NM_001082541.1:286..1143"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:79256"
                     /db_xref="RGD:620365"
ORIGIN      
        1 mseeqfggdg aaaaataavg gsageqegam vaaaqgaaaa agsgsgggsa pggteggste
       61 aegakidask needegkmfi gglswdttkk dlkdyfskfg dvvdctlkld pitgrsrgfg
      121 fvlfkesesv dkvmdqkehk lngkvidpkr akamktkepv kkifvgglsp dtpeekirey
      181 fggfgevesi elpmdnktnk rrgfcfitfk eeepvkkime kkyhnvglsk ceikvamske
      241 qyqqqqqwgs rggfagrarg rggdqqsgyg kvsrrgghqn sykpy
//
LOCUS       NP_001012184             403 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding motif, single-stranded-interacting protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001012184 XP_342439
VERSION     NP_001012184.1
DBSOURCE    REFSEQ: accession NM_001012184.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087094.1.
            
            On Feb 11, 2005 this sequence version replaced XP_342439.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087094.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..403
                     /product="RNA-binding motif, single-stranded-interacting
                     protein 1"
                     /calculated_mol_wt=43937
     Region          30..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP1.1)"
     Region          55..140
                     /region_name="RRM1_MSSP1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     single-stranded DNA-binding protein MSSP-1; cd12470"
                     /db_xref="CDD:409900"
     Region          141..225
                     /region_name="RRM2_MSSP1"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     single-stranded DNA-binding protein MSSP-1; cd12473"
                     /db_xref="CDD:409903"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P29558; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP1.1)"
     CDS             1..403
                     /gene="Rbms1"
                     /coded_by="NM_001012184.1:440..1651"
                     /db_xref="GeneID:362138"
                     /db_xref="RGD:1307777"
ORIGIN      
        1 mgkvwkqqmy pqyatyyypq ylqakqslvp ahpmappsps ttssnnnsss ssnsgwdqls
       61 ktnlyirglp pnttdqdlvk lcqpygkivs tkaildkatn kckgygfvdf dspaaaqkav
      121 salkasgvqa qmakqqeqdp tnlyisnlpl smdeqelenm lkpfgqvist rvlrdssgts
      181 rgvgfarmes tekceavigh fngkfiktpp gvsaptepll ckfadggqkk rqnpnkyipn
      241 grpwpregea gmtltydptt aalhngfyps pysiatnrmi tqtsltpyia spvsayqvqs
      301 pswmqpqpyi lqhpgavltp smehtmslqp asmisplaqq mshlslgstg tympatsamq
      361 gaylpqythm qtatvpveea sgqqqvtvet sndhspytfp pnk
//
LOCUS       NP_001004262             657 aa            linear   ROD 27-APR-2025
DEFINITION  conserved oligomeric Golgi complex subunit 6 [Rattus norvegicus].
ACCESSION   NP_001004262 XP_227136
VERSION     NP_001004262.1
DBSOURCE    REFSEQ: accession NM_001004262.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Lubbehusen,J., Thiel,C., Rind,N., Ungar,D., Prinsen,B.H., de
            Koning,T.J., van Hasselt,P.M. and Korner,C.
  TITLE     Fatal outcome due to deficiency of subunit 6 of the conserved
            oligomeric Golgi complex leading to a new type of congenital
            disorders of glycosylation
  JOURNAL   Hum Mol Genet 19 (18), 3623-3633 (2010)
   PUBMED   20605848
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079442.1.
            
            On Sep 10, 2004 this sequence version replaced XP_227136.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..657
                     /product="conserved oligomeric Golgi complex subunit 6"
                     /note="COG complex subunit 6"
                     /calculated_mol_wt=72826
     Region          14..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FP9.1)"
     Region          56..652
                     /region_name="COG6"
                     /note="Conserved oligomeric complex COG6; pfam06419"
                     /db_xref="CDD:461904"
     CDS             1..657
                     /gene="Cog6"
                     /coded_by="NM_001004262.1:3..1976"
                     /db_xref="GeneID:310411"
                     /db_xref="RGD:1303283"
ORIGIN      
        1 madtsgevaa vpasgaangl sngagatpaq pnnplsrklh kiletrlend kemlealkal
       61 saffvenslr trrnlrgdie rrslaineef vsifkdvkee lesinedvqa mssccqdmts
      121 rlqaakeqtq dlivkttklq aenqrleira qvadaflskf qltsdemtll rgtrggpvte
      181 dffkalgrvk qihndvkvll rtnqqtagle imeqmallqe tayerlyrwa qsecraltqe
      241 scdvsavltq amealqdrpv lykytldefg tarrstvvrg fidaltrggp ggtprpiemh
      301 shdplryvgd mlawlhqata sekehleall khvtaqgvke niqevvghit egvcrplkvr
      361 ieqvilaepg avllykisnl lkfyhhtisg ivgnsaatll ttieemhlls kkiffsslsl
      421 hanklmdkie lpppdlgpss alsqtltllr dvlashdssv vpldarqadf vqvlscvldp
      481 llqmctvsas nlgtadmatf mvnslymmkt tlalfeftdr rlemlqfqie ahldtlineq
      541 asyvltrvgl syiyntiqqh rpdqgslasm pnldsvalka amaqfdryls apdhllmpql
      601 nsllsatvke qiikqstelv craygevhaa vmnpvnaykd pesilhrspe qvktlls
//
LOCUS       NP_059029                442 aa            linear   ROD 27-APR-2025
DEFINITION  endothelin receptor type B precursor [Rattus norvegicus].
ACCESSION   NP_059029 XP_344452
VERSION     NP_059029.1
DBSOURCE    REFSEQ: accession NM_017333.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Yang,P., Wu,Y., Li,F., Tang,J., Zheng,Z. and Tian,Q.
  TITLE     Activation of ETAR and ETBR in myocardial tissue characterizes
            heart failure induced by experimental autoimmune myocarditis
  JOURNAL   BMC Cardiovasc Disord 24 (1), 11 (2024)
   PUBMED   38166688
  REMARK    GeneRIF: Activation of ETAR and ETBR in myocardial tissue
            characterizes heart failure induced by experimental autoimmune
            myocarditis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yang,P., Li,F., Tang,J., Tian,Q. and Zheng,Z.
  TITLE     ET-1 receptor type B (ETBR) overexpression associated with ICAM-1
            downregulation leads to inflammatory attenuation in experimental
            autoimmune myocarditis
  JOURNAL   PeerJ 11, e16320 (2023)
   PUBMED   37901475
  REMARK    GeneRIF: ET-1 receptor type B (ETBR) overexpression associated with
            ICAM-1 downregulation leads to inflammatory attenuation in
            experimental autoimmune myocarditis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Becker,B.K., Grady,C.M., Markl,A.E., Torres Rodriguez,A.A. and
            Pollock,D.M.
  TITLE     Elevated renal afferent nerve activity in a rat model of endothelin
            B receptor deficiency
  JOURNAL   Am J Physiol Renal Physiol 325 (2), F235-F247 (2023)
   PUBMED   37348026
  REMARK    GeneRIF: Elevated renal afferent nerve activity in a rat model of
            endothelin B receptor deficiency.
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Cassinotti,L., Guil,M., Bianciotti,L. and Vatta,M.
  TITLE     Role of Brain Endothelin Receptor Type B (ETB) in the Regulation of
            Tyrosine Hydroxylase in the Olfactory Bulb of DOCA-Salt
            Hypertensive Rats
  JOURNAL   Curr Vasc Pharmacol 21 (4), 246-256 (2023)
   PUBMED   37349999
  REMARK    GeneRIF: Role of Brain Endothelin Receptor Type B (ETB) in the
            Regulation of Tyrosine Hydroxylase in the Olfactory Bulb of
            DOCA-Salt Hypertensive Rats.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Chen,K.C., Chen,K.C., Song,Z.M. and Croaker,G.D.
  TITLE     Structural heart defects associated with ETB mutation, a cause of
            Hirschsprung disease
  JOURNAL   BMC Cardiovasc Disord 21 (1), 475 (2021)
   PUBMED   34600481
  REMARK    GeneRIF: Structural heart defects associated with ETB mutation, a
            cause of Hirschsprung disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Puffenberger,E.G., Hosoda,K., Washington,S.S., Nakao,K., deWit,D.,
            Yanagisawa,M. and Chakravart,A.
  TITLE     A missense mutation of the endothelin-B receptor gene in multigenic
            Hirschsprung's disease
  JOURNAL   Cell 79 (7), 1257-1266 (1994)
   PUBMED   8001158
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Hori,S., Komatsu,Y., Shigemoto,R., Mizuno,N. and Nakanishi,S.
  TITLE     Distinct tissue distribution and cellular localization of two
            messenger ribonucleic acids encoding different subtypes of rat
            endothelin receptors
  JOURNAL   Endocrinology 130 (4), 1885-1895 (1992)
   PUBMED   1312429
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Sakamoto,A., Yanagisawa,M., Sakurai,T., Takuwa,Y., Yanagisawa,H.
            and Masaki,T.
  TITLE     Cloning and functional expression of human cDNA for the ETB
            endothelin receptor
  JOURNAL   Biochem Biophys Res Commun 178 (2), 656-663 (1991)
   PUBMED   1713452
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Sakurai,T., Yanagisawa,M., Takuwa,Y., Miyazaki,H., Kimura,S.,
            Goto,K. and Masaki,T.
  TITLE     Cloning of a cDNA encoding a non-isopeptide-selective subtype of
            the endothelin receptor
  JOURNAL   Nature 348 (6303), 732-735 (1990)
   PUBMED   2175397
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Moore,K.J., Swing,D.A., Copeland,N.G. and Jenkins,N.A.
  TITLE     Interaction of the murine dilute suppressor gene (dsu) with
            fourteen coat color mutations
  JOURNAL   Genetics 125 (2), 421-430 (1990)
   PUBMED   2379821
  REMARK    Erratum:[Genetics 1990 Sep;126(1):285]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from S65355.1.
            
            On Dec 17, 2003 this sequence version replaced XP_344452.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: X57764.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5756307,
                                    SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q22"
     Protein         1..442
                     /product="endothelin receptor type B precursor"
                     /note="endothelin B receptor; ET-B; endothelin receptor
                     non-selective type; ET-BR"
                     /calculated_mol_wt=46840
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2633
     mat_peptide     27..442
                     /product="Endothelin receptor type B. /id=PRO_0000012733"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
                     /calculated_mol_wt=46840
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Region          102..397
                     /region_name="7tmA_ET-BR"
                     /note="endothelin B receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd15976"
                     /db_xref="CDD:320642"
     Site            102..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Region          103..129
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320642"
     Region          136..162
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320642"
     Site            138..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Site            order(158,161..162,174..179,181..182,185,230,232..236,270,
                     273..275,277..279,281..282,336,339..340,342..343,346,
                     364..365,367..369,372,375..376)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320642"
     Region          174..204
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320642"
     Site            176..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Region          216..236
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320642"
     Site            219..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Region          270..295
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320642"
     Site            272..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Region          316..346
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320642"
     Site            325..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Site            363..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21451.2)"
     Region          365..390
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320642"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28088; propagated from
                     UniProtKB/Swiss-Prot (P21451.2)"
     CDS             1..442
                     /gene="Ednrb"
                     /gene_synonym="Ednra; Etb"
                     /coded_by="NM_017333.1:252..1580"
                     /db_xref="GeneID:50672"
                     /db_xref="RGD:2536"
ORIGIN      
        1 mqssasrcgr alvalllacg llgvwgekrg fppaqatpsl lgtkevmtpp tktswtrgsn
       61 sslmrssapa evtkggrvag vpprsfpppc qrkieinktf kyintivscl vfvlgiigns
      121 tllriiyknk cmrngpnili aslalgdllh iiidipinay kllagdwpfg aemcklvpfi
      181 qkasvgitvl slcalsidry ravaswsrik gigvpkwtav eivliwvvsv vlavpeaigf
      241 dvitsdykgk plrvcmlnpf qktafmqfyk takdwwlfsf yfclplaita ifytlmtcem
      301 lrkksgmqia lndhlkqrre vaktvfclvl vfalcwlplh lsrilkltly dqsnpqrcel
      361 lsfllvldyi ginmaslnsc inpialylvs krfkncfksc lccwcqtfee kqsleekqsc
      421 lkfkandhgy dnfrssnkys ss
//
LOCUS       NP_001029066             626 aa            linear   ROD 27-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 1 isoform 5
            [Rattus norvegicus].
ACCESSION   NP_001029066 XP_223515
VERSION     NP_001029066.1
DBSOURCE    REFSEQ: accession NM_001033894.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Berg,J.M., Lee,C., Chen,L., Galvan,L., Cepeda,C., Chen,J.Y.,
            Penagarikano,O., Stein,J.L., Li,A., Oguro-Ando,A., Miller,J.A.,
            Vashisht,A.A., Starks,M.E., Kite,E.P., Tam,E., Gdalyahu,A.,
            Al-Sharif,N.B., Burkett,Z.D., White,S.A., Fears,S.C., Levine,M.S.,
            Wohlschlegel,J.A. and Geschwind,D.H.
  TITLE     JAKMIP1, a Novel Regulator of Neuronal Translation, Modulates
            Synaptic Function and Autistic-like Behaviors in Mouse
  JOURNAL   Neuron 88 (6), 1173-1191 (2015)
   PUBMED   26627310
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Vidal,R.L., Fuentes,P., Valenzuela,J.I., Alvarado-Diaz,C.P.,
            Ramirez,O.A., Kukuljan,M. and Couve,A.
  TITLE     RNA interference of Marlin-1/Jakmip1 results in abnormal
            morphogenesis and migration of cortical pyramidal neurons
  JOURNAL   Mol Cell Neurosci 51 (1-2), 1-11 (2012)
   PUBMED   22828129
  REMARK    GeneRIF: RNA interference of Marlin-1 in vivo results in abnormal
            migration and abnormal morphology of newborn pyramidal neurons
            during the formation of the cortex.
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Vidal,R.L., Valenzuela,J.I., Lujan,R. and Couve,A.
  TITLE     Cellular and subcellular localization of Marlin-1 in the brain
  JOURNAL   BMC Neurosci 10, 37 (2009)
   PUBMED   19386132
  REMARK    GeneRIF: Marlin-1 is enriched in restricted areas of the brain
            including olfactory bulb, cerebral cortex, hippocampus and
            cerebellum; it is abundant in dendrites and axons of hippocampal
            neurons, associated with microtubules at the ultrastructural level.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Vidal,R.L., Ramirez,A., Castro,M., Concha,I.I. and Couve,A.
  TITLE     Marlin-1 is expressed in testis and associates to the cytoskeleton
            and GABAB receptors
  JOURNAL   J Cell Biochem 103 (3), 886-895 (2008)
   PUBMED   17668444
  REMARK    GeneRIF: Our findings demonstrate that Marlin-1 associates with a
            microtubule fraction and with GABA(B) receptors in testis
            suggesting that the set of protein interactions of Marlin-1 are
            conserved in different tissues.
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Nishimura,Y., Martin,C.L., Vazquez-Lopez,A., Spence,S.J.,
            Alvarez-Retuerto,A.I., Sigman,M., Steindler,C., Pellegrini,S.,
            Schanen,N.C., Warren,S.T. and Geschwind,D.H.
  TITLE     Genome-wide expression profiling of lymphoblastoid cell lines
            distinguishes different forms of autism and reveals shared pathways
  JOURNAL   Hum Mol Genet 16 (14), 1682-1698 (2007)
   PUBMED   17519220
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Vidal,R.L., Ramirez,O.A., Sandoval,L., Koenig-Robert,R., Hartel,S.
            and Couve,A.
  TITLE     Marlin-1 and conventional kinesin link GABAB receptors to the
            cytoskeleton and regulate receptor transport
  JOURNAL   Mol Cell Neurosci 35 (3), 501-512 (2007)
   PUBMED   17532644
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Couve,A., Restituito,S., Brandon,J.M., Charles,K.J., Bawagan,H.,
            Freeman,K.B., Pangalos,M.N., Calver,A.R. and Moss,S.J.
  TITLE     Marlin-1, a novel RNA-binding protein associates with GABA
            receptors
  JOURNAL   J Biol Chem 279 (14), 13934-13943 (2004)
   PUBMED   14718537
  REMARK    GeneRIF: Marlin-1 functions to regulate the cellular levels of
            GABA(B) R2 subunits, which may have significant effects on the
            production of functional GABA(B) receptor heterodimers.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC104677.1.
            
            On Sep 30, 2005 this sequence version replaced XP_223515.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC104677.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..626
                     /product="janus kinase and microtubule-interacting protein
                     1 isoform 5"
                     /note="multiple alpha helices and RNA-linker protein 1;
                     multiple coiled-coil GABABR1-binding protein"
                     /calculated_mol_wt=72976
     Region          1..365
                     /region_name="Mediates association with microtubules.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          <24..>607
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          365..626
                     /region_name="Mediates interaction with TYK2 and GABBR1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          415..605
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          452..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     CDS             1..626
                     /gene="Jakmip1"
                     /gene_synonym="Marlin-1; Marlin1"
                     /coded_by="NM_001033894.1:204..2084"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:305434"
                     /db_xref="RGD:1562401"
ORIGIN      
        1 mskkgrskge kpetetdsvq maneelrakl tniqiefqqe kskvgklrer lqeaklereq
       61 eqrrhtayis elkaklheek tkelqalrea lirqheqeaa rtakikegel qrlqatlnvl
      121 rdgaadkvkt alladareea rrtfdgerqr lqqeilelka arkqaeeals ncmqadkaka
      181 adlraayqah qdevhrikre cerdirrlmd eikgkervil alekelgvqa gqtqrlllqk
      241 ealdeqlvqv keaerhhssp krelppgigd maelmggqdq hmderdvrrf qlkiaelnsv
      301 irkledrntl ladernellk rsretevqlk plveknkrmn kknedllhsi qrmeeklksl
      361 trenvemkek lsaqaslkrh tslndlsltr deqeieflrl qvleqqhvid dlslererll
      421 rskrhrgksl kppkkhvvet ffgfdeesvd setlsetsyn tdrtdrtpat peedldettt
      481 reeadlrfcq ltreyqalqr ayallqeqvg gtldaerear treqlqadll rcqakiedle
      541 kllvekgqda awveekqvlm rtnqdlleki yrlemeenql ksemqdakdq nellefrvle
      601 levrdsicck lsngadilfe pklkfv
//
LOCUS       NP_001129348             417 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial tRNA-specific 2-thiouridylase 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001129348 XP_343307
VERSION     NP_001129348.1
DBSOURCE    REFSEQ: accession NM_001135876.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Gaignard,P., Gonzales,E., Ackermann,O., Labrune,P., Correia,I.,
            Therond,P., Jacquemin,E. and Slama,A.
  TITLE     Mitochondrial Infantile Liver Disease due to TRMU Gene Mutations:
            Three New Cases
  JOURNAL   JIMD Rep 11, 117-123 (2013)
   PUBMED   23625533
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Zeharia,A., Shaag,A., Pappo,O., Mager-Heckel,A.M., Saada,A.,
            Beinat,M., Karicheva,O., Mandel,H., Ofek,N., Segel,R., Marom,D.,
            Rotig,A., Tarassov,I. and Elpeleg,O.
  TITLE     Acute infantile liver failure due to mutations in the TRMU gene
  JOURNAL   Am J Hum Genet 85 (3), 401-407 (2009)
   PUBMED   19732863
  REMARK    Erratum:[Am J Hum Genet. 2010 Feb;86(2):295]
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Yan,Q. and Guan,M.X.
  TITLE     Identification and characterization of mouse TRMU gene encoding the
            mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase
  JOURNAL   Biochim Biophys Acta 1676 (2), 119-126 (2004)
   PUBMED   14746906
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Oct 16, 2008 this sequence version replaced XP_343307.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.1246463.1,
                                           SRR26360176.993407.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..417
                     /product="mitochondrial tRNA-specific 2-thiouridylase 1
                     isoform 1"
                     /EC_number="2.8.1.14"
                     /note="mitochondrial tRNA-specific 2-thiouridylase 1; tRNA
                     (5-methylaminomethyl-2-thiouridylate)-methyltransferase 1;
                     tRNA 5-methylaminomethyl-2-thiouridylate
                     methyltransferase"
                     /calculated_mol_wt=47167
     Region          6..383
                     /region_name="MnmA_TRMU-like"
                     /note="MnmA/TRMU family 2-thiouridylases and similar
                     proteins; cd01998"
                     /db_xref="CDD:467502"
     CDS             1..417
                     /gene="Trmu"
                     /gene_synonym="Mtu1"
                     /coded_by="NM_001135876.1:70..1323"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362976"
                     /db_xref="RGD:1311229"
ORIGIN      
        1 msalrhvvca lsggvdsava alllrrrgyq vtgvfmknwd sldeqgicaa dkdcedaykv
       61 cqildipfhq vsyvkeywnd vfsdflneye kgrtpnpdis cnkhikfscf hhyavdnlga
      121 davatghyar tsledeevfe qkhtkrpdgl frnrfevrnp vkllqaadsf kdqtfflsqv
      181 sqdalrrtif plgeltkdfv kkiaaenrlh hvlqkkesmg icfigkrnle hfllqylqpr
      241 pgkfisiedn rvlgthkgwf lytlgqraki sglsepwyvv ekdgtkgdvl vaprvdhpal
      301 yrdllrtnrv hwiaeeppaa lvrdkmmech frfrhqmalv pcvltlnqdg tvwvtavkav
      361 rglalgqfav fykgeeclgs gkilrlgpsa ytlqkgknrt rvapevssds pglhpts
//
LOCUS       NP_001032733             385 aa            linear   ROD 27-APR-2025
DEFINITION  probable splicing factor YJU2B [Rattus norvegicus].
ACCESSION   NP_001032733 XP_222461
VERSION     NP_001032733.1
DBSOURCE    REFSEQ: accession NM_001037644.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Lammers,R., Gross,G., Mayr,U. and Collins,J.
  TITLE     Alternative mechanisms for gene activation induced by
            poly(rI).poly(rC) and Newcastle disease virus
  JOURNAL   Eur J Biochem 178 (1), 93-99 (1988)
   PUBMED   3203696
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107912.1.
            
            On Dec 9, 2005 this sequence version replaced XP_222461.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107912.1, SRR8487226.58039.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..385
                     /product="probable splicing factor YJU2B"
                     /note="coiled-coil domain-containing protein 130;
                     coiled-coil domain containing 130"
                     /calculated_mol_wt=43669
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32PZ9.1)"
     Region          9..384
                     /region_name="Saf4_Yju2"
                     /note="Saf4/Yju2 protein; pfam04502"
                     /db_xref="CDD:461333"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13994; propagated from
                     UniProtKB/Swiss-Prot (Q32PZ9.1)"
     Region          256..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32PZ9.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13994; propagated from
                     UniProtKB/Swiss-Prot (Q32PZ9.1)"
     CDS             1..385
                     /gene="Yju2b"
                     /gene_synonym="Ccdc130; RGD1307598"
                     /coded_by="NM_001037644.1:216..1373"
                     /db_xref="GeneID:304656"
                     /db_xref="RGD:1307598"
ORIGIN      
        1 mgerkgqnky yppdfnpekh gslnryhnsh plrerarkls qgiliirfem pyniwcdgck
       61 nhigmgvryn aekkkvgnyy ttpiyrfrmk chlcvnyiem qtdpancdyv ivsgasrkee
      121 rwdmedneqv lttehekkek letdamfrle hgeadrstlk kalptlshiq eaqnawkddf
      181 alnsmlrrhf rekkkamqee eekdqalqak anlaiplvpe seddrrlaal lrlhtldsye
      241 dkqrmkrtei ihrswfpsaq gpstssskas tvlkklcrgr rpptgsagap gdlgivrrks
      301 reapespqct adnslseepr gppgttpdsk tlqgtaeapr tsktleskrn csdqalplgs
      361 sqedllhpnt pnaslvadys dsese
//
LOCUS       NP_001009652             470 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic 60S subunit biogenesis factor ZNF622 [Rattus
            norvegicus].
ACCESSION   NP_001009652 XP_215512
VERSION     NP_001009652.1
DBSOURCE    REFSEQ: accession NM_001009652.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Seong,H.A., Jung,H., Manoharan,R. and Ha,H.
  TITLE     Positive regulation of apoptosis signal-regulating kinase 1
            signaling by ZPR9 protein, a zinc finger protein
  JOURNAL   J Biol Chem 286 (36), 31123-31135 (2011)
   PUBMED   21771788
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Seong,H.A., Kim,K.T. and Ha,H.
  TITLE     Enhancement of B-MYB transcriptional activity by ZPR9, a novel zinc
            finger protein
  JOURNAL   J Biol Chem 278 (11), 9655-9662 (2003)
   PUBMED   12645566
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088214.1.
            
            On Jan 13, 2005 this sequence version replaced XP_215512.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088214.1, SRR8487226.184223.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q22"
     Protein         1..470
                     /product="cytoplasmic 60S subunit biogenesis factor
                     ZNF622"
                     /note="liver regeneration-related protein LRRG121"
                     /calculated_mol_wt=53508
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q969S3; propagated from
                     UniProtKB/Swiss-Prot (Q7TM96.2)"
     Region          <6..49
                     /region_name="PTZ00448"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:185627"
     Region          6..28
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(13..15,17..18,22,27,74,77..81,83..84)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          68..91
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          69..91
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          135..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TM96.2)"
     Region          247..346
                     /region_name="zf-C2H2_2"
                     /note="C2H2 type zinc-finger (2 copies); pfam12756"
                     /db_xref="CDD:463690"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q969S3; propagated from
                     UniProtKB/Swiss-Prot (Q7TM96.2)"
     CDS             1..470
                     /gene="Zfp622"
                     /gene_synonym="Znf622"
                     /coded_by="NM_001009652.1:103..1515"
                     /db_xref="GeneID:294846"
                     /db_xref="RGD:1309146"
ORIGIN      
        1 matytcitcr vafrdaemqr ahyktdwhry nlrrkvanma pvtaegfqer vraqravaee
       61 eskgtatyct vcskkfatfn ayenhlksrr hvelekkavq avsrqvemmn eknlekglgv
      121 dsvnkdamna aiqqaikaqp stspkkapfm ptdesrrvag avrrgtperd ptekpprlqw
      181 feqqakklak qqweeseeeg eeddedwedi dsddglecen pgveeedaed aeaeespplg
      241 aipitdclfc shhssslvkn vahmtkvhsf fipdieylsd lkglikylge kvgvgkiclw
      301 cnekgksfys teavqahmnd kshcklftdg daalefadfy dfrssypdyk egqdpaeied
      361 lssekilecd detmelilps garvghrslm ryykqrfglp ravtvarnqk avgrvlqqyr
      421 algwtgstga almrerdmqy vqrmkskwml ktgmknnatk qmhfraqvrf
//
LOCUS       NP_112327                217 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL1 [Rattus norvegicus].
ACCESSION   NP_112327
VERSION     NP_112327.1
DBSOURCE    REFSEQ: accession NM_031065.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 217)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L10a
  JOURNAL   Biochem Biophys Res Commun 220 (3), 954-957 (1996)
   PUBMED   8607874
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Haviryaji,K.S., Srinivas,R., Suryanarayana,T. and Vemuri,M.C.
  TITLE     Effect of ethanol on hepatic ribosomal proteins and mRNA
  JOURNAL   Mol Cell Biochem 115 (2), 143-147 (1992)
   PUBMED   1448059
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Lavergne,J.P., Marzouki,A., Reboud,J.P. and Reboud,A.M.
  TITLE     Reconstitution of the active rat liver 60 S ribosomal subunit from
            different preparations of core particles and split proteins
  JOURNAL   FEBS Lett 236 (2), 345-351 (1988)
   PUBMED   3044828
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X93352.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X93352.1, FQ221725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..217
                     /product="large ribosomal subunit protein uL1"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10a"
                     /calculated_mol_wt=24700
     Region          2..217
                     /region_name="Ribosomal_L1"
                     /note="Ribosomal protein L1. The L1 protein, located near
                     the E-site of the ribosome, forms part of the L1 stalk
                     along with 23S rRNA. In bacteria and archaea, L1 functions
                     both as a ribosomal protein that binds rRNA, and as a
                     translation repressor that binds...; cl00322"
                     /db_xref="CDD:469720"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62906; propagated from
                     UniProtKB/Swiss-Prot (P62907.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P53026; propagated from
                     UniProtKB/Swiss-Prot (P62907.2)"
     Site            order(26..28,31,33,35,37,162,164,166,210..211,213)
                     /site_type="other"
                     /note="mRNA/rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238235"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53026; propagated from
                     UniProtKB/Swiss-Prot (P62907.2)"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62906; propagated from
                     UniProtKB/Swiss-Prot (P62907.2)"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62906; propagated from
                     UniProtKB/Swiss-Prot (P62907.2)"
     CDS             1..217
                     /gene="Rpl10a"
                     /coded_by="NM_031065.1:27..680"
                     /db_xref="GeneID:81729"
                     /db_xref="RGD:620497"
ORIGIN      
        1 msskvsrdtl yeavrevlhg nqrkrrkfle tvelqislkn ydpqkdkrfs gtvrlkstpr
       61 pkfsvcvlgd qqhcdeakav diphmdieal kklnknkklv kklakkydaf laseslikqi
      121 prilgpglnk agkfpsllth nenmvakvde vkstikfqmk kvlclavavg hvkmtddelv
      181 ynihlavnfl vsllkknwqn vralyikstm gkpqrly
//
LOCUS       NP_001020898             487 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF8 [Rattus norvegicus].
ACCESSION   NP_001020898 XP_342109
VERSION     NP_001020898.1
DBSOURCE    REFSEQ: accession NM_001025727.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Valnegri,P., Huang,J., Yamada,T., Yang,Y., Mejia,L.A., Cho,H.Y.,
            Oldenborg,A. and Bonni,A.
  TITLE     RNF8/UBC13 ubiquitin signaling suppresses synapse formation in the
            mammalian brain
  JOURNAL   Nat Commun 8 (1), 1271 (2017)
   PUBMED   29097665
  REMARK    GeneRIF: Knockdown or conditional knockout of RNF8 or UBC13 in
            rodent cerebellar granule neurons robustly increases the number of
            parallel fiber presynaptic boutons and functional parallel
            fiber/Purkinje cell synapses. In contrast to the role of nuclear
            RNF8 in proliferating cells, RNF8 operates in the cytoplasm in
            neurons to suppress synapse differentiation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Gou,L.T., Kang,J.Y., Dai,P., Wang,X., Li,F., Zhao,S., Zhang,M.,
            Hua,M.M., Lu,Y., Zhu,Y., Li,Z., Chen,H., Wu,L.G., Li,D., Fu,X.D.,
            Li,J., Shi,H.J. and Liu,M.F.
  TITLE     Ubiquitination-Deficient Mutations in Human Piwi Cause Male
            Infertility by Impairing Histone-to-Protamine Exchange during
            Spermiogenesis
  JOURNAL   Cell 169 (6), 1090-1104 (2017)
   PUBMED   28552346
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Panier,S. and Boulton,S.J.
  TITLE     Double-strand break repair: 53BP1 comes into focus
  JOURNAL   Nat Rev Mol Cell Biol 15 (1), 7-18 (2014)
   PUBMED   24326623
  REMARK    Review article
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Mattiroli,F., Vissers,J.H., van Dijk,W.J., Ikpa,P., Citterio,E.,
            Vermeulen,W., Marteijn,J.A. and Sixma,T.K.
  TITLE     RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage
            signaling
  JOURNAL   Cell 150 (6), 1182-1195 (2012)
   PUBMED   22980979
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Mallette,F.A., Mattiroli,F., Cui,G., Young,L.C., Hendzel,M.J.,
            Mer,G., Sixma,T.K. and Richard,S.
  TITLE     RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers
            53BP1 recruitment to DNA damage sites
  JOURNAL   EMBO J 31 (8), 1865-1878 (2012)
   PUBMED   22373579
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Ramachandran,S., Chahwan,R., Nepal,R.M., Frieder,D., Panier,S.,
            Roa,S., Zaheen,A., Durocher,D., Scharff,M.D. and Martin,A.
  TITLE     The RNF8/RNF168 ubiquitin ligase cascade facilitates class switch
            recombination
  JOURNAL   Proc Natl Acad Sci U S A 107 (2), 809-814 (2010)
   PUBMED   20080757
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Wu,J., Huen,M.S., Lu,L.Y., Ye,L., Dou,Y., Ljungman,M., Chen,J. and
            Yu,X.
  TITLE     Histone ubiquitination associates with BRCA1-dependent DNA damage
            response
  JOURNAL   Mol Cell Biol 29 (3), 849-860 (2009)
   PUBMED   19015238
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Zhang,S., Chea,J., Meng,X., Zhou,Y., Lee,E.Y. and Lee,M.Y.
  TITLE     PCNA is ubiquitinated by RNF8
  JOURNAL   Cell Cycle 7 (21), 3399-3404 (2008)
   PUBMED   18948756
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Huen,M.S., Grant,R., Manke,I., Minn,K., Yu,X., Yaffe,M.B. and
            Chen,J.
  TITLE     RNF8 transduces the DNA-damage signal via histone ubiquitylation
            and checkpoint protein assembly
  JOURNAL   Cell 131 (5), 901-914 (2007)
   PUBMED   18001825
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Mailand,N., Bekker-Jensen,S., Faustrup,H., Melander,F., Bartek,J.,
            Lukas,C. and Lukas,J.
  TITLE     RNF8 ubiquitylates histones at DNA double-strand breaks and
            promotes assembly of repair proteins
  JOURNAL   Cell 131 (5), 887-900 (2007)
   PUBMED   18001824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC099079.1.
            
            On Jul 22, 2005 this sequence version replaced XP_342109.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099079.1, SRR8487230.81971.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132265, SAMD00132269
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..487
                     /product="E3 ubiquitin-protein ligase RNF8"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 8, E3 ubiquitin protein ligase;
                     RING-type E3 ubiquitin transferase RNF8"
                     /calculated_mol_wt=55484
     Region          18..126
                     /region_name="FHA_RNF8"
                     /note="forkhead associated (FHA) domain found in RING
                     finger protein 8 (RNF8) and similar proteins; cd22663"
                     /db_xref="CDD:438715"
     Site            order(42,55,57..61,82..83,110)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438715"
     Region          68..72
                     /region_name="Required for interaction with PIWIL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03067"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN8.1)"
     Region          135..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLN8.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O76064; propagated from
                     UniProtKB/Swiss-Prot (Q4KLN8.1)"
     Region          276..>407
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          402..464
                     /region_name="RING-HC_RNF8"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 8 (RNF8) and similar proteins; cd16535"
                     /db_xref="CDD:438197"
     Site            order(402..403,417..418,421..423,450..455,457..458,
                     461..462)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438197"
     Site            order(404,406..410,431..432,435..436,440,443)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438197"
     CDS             1..487
                     /gene="Rnf8"
                     /coded_by="NM_001025727.1:85..1548"
                     /db_xref="GeneID:361815"
                     /db_xref="RGD:1308035"
ORIGIN      
        1 mgepdplvsg qlaarrswcl rrlgmdrewl qleagsevti grgfsvtyql iskvcplmis
       61 rnhcvlkqnp egqwtimdnk slngvwlnre rlaplqgyci rkgdhiqlgv pleskehaey
      121 eyevieedre slapclapkn dhttekhkgl rtkrkfssdg veslpaegps dlrcplakgs
      181 skpaepeklh gkgeaasqpl gclcptlasl easertagph acstlpkvle lypkkqkacs
      241 psasqsslel fkmtmsrmlk lktqmqekqi avlnvkrqar kgsskkvvrm ekelrdlqsq
      301 lyaeqaqqqa rveqlektfq eeeqhlqgle keqgecdlkq qllqalqehr almeeldrsk
      361 kdfekiiqak nkelertkee kdkvqaqkee vlshmndvle nelqciicse yfieavtlnc
      421 ahsfcsfcis ewmkrkvecp icrkdiesrt nslvldncis kmverlssdv kerrsvlire
      481 rrakrll
//
LOCUS       NP_062131                142 aa            linear   ROD 27-APR-2025
DEFINITION  cystatin-8 precursor [Rattus norvegicus].
ACCESSION   NP_062131
VERSION     NP_062131.1
DBSOURCE    REFSEQ: accession NM_019258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Cornwall,G.A., Hsia,N. and Sutton,H.G.
  TITLE     Structure, alternative splicing and chromosomal localization of the
            cystatin-related epididymal spermatogenic gene
  JOURNAL   Biochem J 340 (Pt 1) (Pt 1), 85-93 (1999)
   PUBMED   10229662
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Cornwall,G.A. and Hann,S.R.
  TITLE     Transient appearance of CRES protein during spermatogenesis and
            caput epididymal sperm maturation
  JOURNAL   Mol Reprod Dev 41 (1), 37-46 (1995)
   PUBMED   7619504
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Cornwall,G.A., Orgebin-Crist,M.C. and Hann,S.R.
  TITLE     The CRES gene: a unique testis-regulated gene related to the
            cystatin family is highly restricted in its expression to the
            proximal region of the mouse epididymis
  JOURNAL   Mol Endocrinol 6 (10), 1653-1664 (1992)
   PUBMED   1280328
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF090692.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF090692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..142
                     /product="cystatin-8 precursor"
                     /note="cystatin-related epididymal spermatogenic protein;
                     cystatin 8 (cystatin-related epididymal spermatogenic);
                     cystatin 8 (cystatin-related epididymal specific)"
                     /calculated_mol_wt=14191
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2073
     mat_peptide     20..142
                     /product="Cystatin-8. /id=PRO_0000006655"
                     /note="propagated from UniProtKB/Swiss-Prot (O88969.1)"
                     /calculated_mol_wt=14191
     Region          38..140
                     /region_name="CY"
                     /note="Cystatin-like domain; smart00043"
                     /db_xref="CDD:214484"
     Region          77..81
                     /region_name="Secondary area of contact.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O88969.1)"
     Site            order(77..79,81)
                     /site_type="active"
                     /note="putative proteinase inhibition site [active]"
                     /db_xref="CDD:238002"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88969.1)"
     CDS             1..142
                     /gene="Cst8"
                     /coded_by="NM_019258.1:195..623"
                     /db_xref="GeneID:29679"
                     /db_xref="RGD:2434"
ORIGIN      
        1 mtkplllsli ffiipaalav dvdqsknevk aqryfgsisi snanvkqcvw famkeynkgs
       61 edkylflldk tlhatlqitd rmeyhidvqi srsncrkpln ntencipqkn pklekklscs
      121 flvgalpwng efdllskeck dv
//
LOCUS       NP_001019532             222 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione S-transferase A6 [Rattus norvegicus].
ACCESSION   NP_001019532 XP_576528
VERSION     NP_001019532.1
DBSOURCE    REFSEQ: accession NM_001024361.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Buhrke,T., Lengler,I. and Lampen,A.
  TITLE     Analysis of proteomic changes induced upon cellular differentiation
            of the human intestinal cell line Caco-2
  JOURNAL   Dev Growth Differ 53 (3), 411-426 (2011)
   PUBMED   21492153
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Baur,J.A., Pearson,K.J., Price,N.L., Jamieson,H.A., Lerin,C.,
            Kalra,A., Prabhu,V.V., Allard,J.S., Lopez-Lluch,G., Lewis,K.,
            Pistell,P.J., Poosala,S., Becker,K.G., Boss,O., Gwinn,D., Wang,M.,
            Ramaswamy,S., Fishbein,K.W., Spencer,R.G., Lakatta,E.G., Le
            Couteur,D., Shaw,R.J., Navas,P., Puigserver,P., Ingram,D.K., de
            Cabo,R. and Sinclair,D.A.
  TITLE     Resveratrol improves health and survival of mice on a high-calorie
            diet
  JOURNAL   Nature 444 (7117), 337-342 (2006)
   PUBMED   17086191
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079271.1.
            
            On May 27, 2005 this sequence version replaced XP_576528.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079271.1, CO563436.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..222
                     /product="glutathione S-transferase A6"
                     /EC_number="2.5.1.18"
                     /note="GST class-alpha member 6"
                     /calculated_mol_wt=25677
     Region          4..82
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Region          86..220
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(86..87,89,93..95,97..98,101,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(97,104,107,110..111,131..132,135,152..155,158,
                     161..162,165..166,169,193..194,196..201)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(101,107,111,131,208,216,220)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     CDS             1..222
                     /gene="Gsta6"
                     /coded_by="NM_001024361.1:130..798"
                     /db_xref="GeneID:501110"
                     /db_xref="RGD:1565402"
ORIGIN      
        1 maekplfhyd eargrmesvr wllaaagvey eekfihtned leklrsdgvl mfqqvpmvev
       61 dgmklvqtra imnyfsskyn lygkdmkera lidmysegla dlnemfilyp fdppgvkean
      121 ialmkekatn ryfpafekvf eshgqdylvg nklskadvhl vemiynmeel dtnilanfpl
      181 lqalktrisd mptikkflqp gsqrqppvde ksiqktrkif kf
//
LOCUS       NP_001013189             304 aa            linear   ROD 27-APR-2025
DEFINITION  PTB domain-containing engulfment adapter protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001013189 XP_234765
VERSION     NP_001013189.1
DBSOURCE    REFSEQ: accession NM_001013171.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Martins-Silva,C., Ferreira,L.T., Cyr,M., Koenen,J., Fernandes,D.R.,
            Carvalho,N.R., Ribeiro,C.B., Marion,S., Chavez-Olortegui,C.,
            Prado,M.A. and Prado,V.F.
  TITLE     A rat homologue of CED-6 is expressed in neurons and interacts with
            clathrin
  JOURNAL   Brain Res 1119 (1), 1-12 (2006)
   PUBMED   17007823
  REMARK    GeneRIF: The present findings suggest that CED-6 may have a role in
            endocytic trafficking or signaling in neurons.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Su,H.P., Nakada-Tsukui,K., Tosello-Trampont,A.C., Li,Y., Bu,G.,
            Henson,P.M. and Ravichandran,K.S.
  TITLE     Interaction of CED-6/GULP, an adapter protein involved in
            engulfment of apoptotic cells with CED-1 and CD91/low density
            lipoprotein receptor-related protein (LRP)
  JOURNAL   J Biol Chem 277 (14), 11772-11779 (2002)
   PUBMED   11729193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087053.1, CB738009.1 and BM390519.1.
            
            On Apr 20, 2005 this sequence version replaced XP_234765.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087053.1, SRR8487227.350737.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..304
                     /product="PTB domain-containing engulfment adapter protein
                     1"
                     /note="cell death protein 6 homolog; PTB domain adapter
                     protein CED-6; GULP, engulfment adaptor PTB domain
                     containing 1"
                     /calculated_mol_wt=34154
     Region          14..157
                     /region_name="PTB_CED-6"
                     /note="Cell death protein 6 homolog (CED-6/GULP1)
                     Phosphotyrosine-binding (PTB) domain; cd01273"
                     /db_xref="CDD:269971"
     Site            order(30,109,129)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269971"
     Site            order(98..103,116,138,142)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269971"
     Region          150..191
                     /region_name="ZIP_TSC22D-like"
                     /note="leucine zipper found in the TSC22 domain leucine
                     zipper transcription factors, c-Myc-binding protein, and
                     similar proteins; cl40461"
                     /db_xref="CDD:424092"
     Site            order(160..161,163..167,169..170,172..173,176..177,
                     179..180,183..184,186..187,190..191)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409275"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBP9; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS4.1)"
     CDS             1..304
                     /gene="Gulp1"
                     /gene_synonym="CED-6"
                     /coded_by="NM_001013171.2:106..1020"
                     /db_xref="GeneID:314543"
                     /db_xref="RGD:1306380"
ORIGIN      
        1 mnrafsrkkd ktwmhmpeal skhyvpynak flgsteveqp kgtevvrdav rklkfarhik
       61 ksegqkipkv elqisiygvk ilepktkevq hncqlhrisf caddktdkri ftfickdses
      121 nkhlcfvfds ekcaeeitlt igqafdlayr kflesggkdv etrkqiagmq kriqdleten
      181 melknkvqdl enrlrttqvs stpaggvtvt spstdifdmi pfspishpsp tsagngtqlp
      241 pipsrsseik rdlfgaepfd pfncgagdfp pdiqskldem qegfkmgltl egtvfcldpl
      301 dsrc
//
LOCUS       NP_001014199             444 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_001014199 XP_342359
VERSION     NP_001014199.1
DBSOURCE    REFSEQ: accession NM_001014177.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079224.1.
            
            On Apr 1, 2005 this sequence version replaced XP_342359.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079224.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132263,
                                           SAMD00132265 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..444
                     /product="spermatogenesis-associated protein 1"
                     /calculated_mol_wt=50968
     Region          145..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY22.1)"
     Region          279..428
                     /region_name="SPATA1_C"
                     /note="Spermatogenesis-associated C-terminus; pfam15743"
                     /db_xref="CDD:464839"
     CDS             1..444
                     /gene="Spata1"
                     /coded_by="NM_001014177.1:203..1537"
                     /db_xref="GeneID:362056"
                     /db_xref="RGD:1359500"
ORIGIN      
        1 mslnpsrpss selvelhvfy vpegswnykl ntisievinn fisagfirvs pqltlqalre
       61 rlgeflgvda vaekflflkc ignnlavvke kqeselklks fappyalqpe lyllpvidhl
      121 gnvysastvn ldeqqsvddt meidgtihrp dslslskdep gdpsllentw rdfpnheeae
      181 esqptqqhfg nprlpgslee sddclgnvks pflwknnded egeeddkati nrrqaklvcd
      241 kehsalpdli dfpsfpsqrv ssrlvdtsll kierekiieq mkqvkeerky lenireelik
      301 kveklfeqsk skryhacdsw kkkyfdtkkv tasleevltk lredlelyyk kllmqleare
      361 ikmrprnlan isdsknylii qitevqhaid qlkrkldtdk mklilevkmr kqaasdlqtl
      421 radltqkkmg tpfrspifsg svpt
//
LOCUS       NP_001011951             424 aa            linear   ROD 27-APR-2025
DEFINITION  splicing factor 3B subunit 4 [Rattus norvegicus].
ACCESSION   NP_001011951 XP_238245
VERSION     NP_001011951.1
DBSOURCE    REFSEQ: accession NM_001011951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Li,Y., Diao,Y., Wang,Z., Wang,S., Peng,J. and Kong,B.
  TITLE     The splicing factor SF3B4 drives proliferation and invasion in
            cervical cancer by regulating SPAG5
  JOURNAL   Cell Death Discov 8 (1), 326 (2022)
   PUBMED   35853859
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Liu,Z., Li,W., Pang,Y., Zhou,Z., Liu,S., Cheng,K., Qin,Q., Jia,Y.
            and Liu,S.
  TITLE     SF3B4 is regulated by microRNA-133b and promotes cell proliferation
            and metastasis in hepatocellular carcinoma
  JOURNAL   EBioMedicine 38, 57-68 (2018)
   PUBMED   30391496
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Shen,Q., Eun,J.W., Lee,K., Kim,H.S., Yang,H.D., Kim,S.Y., Lee,E.K.,
            Kim,T., Kang,K., Kim,S., Min,D.H., Oh,S.N., Lee,Y.J., Moon,H.,
            Ro,S.W., Park,W.S., Lee,J.Y. and Nam,S.W.
  TITLE     Barrier to autointegration factor 1, procollagen-lysine,
            2-oxoglutarate 5-dioxygenase 3, and splicing factor 3b subunit 4 as
            early-stage cancer decision markers and drivers of hepatocellular
            carcinoma
  JOURNAL   Hepatology 67 (4), 1360-1377 (2018)
   PUBMED   29059470
  REMARK    Erratum:[Hepatology. 2018 Jul;68(1):391. doi: 10.1002/hep.30114.
            PMID: 29975814]
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Teng,T., Tsai,J.H., Puyang,X., Seiler,M., Peng,S., Prajapati,S.,
            Aird,D., Buonamici,S., Caleb,B., Chan,B., Corson,L., Feala,J.,
            Fekkes,P., Gerard,B., Karr,C., Korpal,M., Liu,X., T Lowe,J.,
            Mizui,Y., Palacino,J., Park,E., Smith,P.G., Subramanian,V.,
            Wu,Z.J., Zou,J., Yu,L., Chicas,A., Warmuth,M., Larsen,N. and Zhu,P.
  TITLE     Splicing modulators act at the branch point adenosine binding
            pocket defined by the PHF5A-SF3b complex
  JOURNAL   Nat Commun 8, 15522 (2017)
   PUBMED   28541300
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Bernier,F.P., Caluseriu,O., Ng,S., Schwartzentruber,J.,
            Buckingham,K.J., Innes,A.M., Jabs,E.W., Innis,J.W., Schuette,J.L.,
            Gorski,J.L., Byers,P.H., Andelfinger,G., Siu,V., Lauzon,J.,
            Fernandez,B.A., McMillin,M., Scott,R.H., Racher,H., Majewski,J.,
            Nickerson,D.A., Shendure,J., Bamshad,M.J. and Parboosingh,J.S.
  CONSRTM   FORGE Canada Consortium
  TITLE     Haploinsufficiency of SF3B4, a component of the pre-mRNA
            spliceosomal complex, causes Nager syndrome
  JOURNAL   Am J Hum Genet 90 (5), 925-933 (2012)
   PUBMED   22541558
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078997.1.
            
            On Feb 11, 2005 this sequence version replaced XP_238245.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078997.1, SRR8487231.138883.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..424
                     /product="splicing factor 3B subunit 4"
                     /calculated_mol_wt=44225
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q15427; propagated from
                     UniProtKB/Swiss-Prot (Q6AYL5.1)"
     Region          15..88
                     /region_name="RRM1_SF3B4"
                     /note="RNA recognition motif 1 (RRM1) found in splicing
                     factor 3B subunit 4 (SF3B4) and similar proteins; cd12334"
                     /db_xref="CDD:409771"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q15427; propagated from
                     UniProtKB/Swiss-Prot (Q6AYL5.1)"
     Region          99..181
                     /region_name="RRM2_SF3B4"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     factor 3B subunit 4 (SF3B4) and similar proteins; cd12335"
                     /db_xref="CDD:409772"
     Region          207..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYL5.1)"
     CDS             1..424
                     /gene="Sf3b4"
                     /coded_by="NM_001011951.1:238..1512"
                     /db_xref="GeneID:295270"
                     /db_xref="RGD:1309667"
ORIGIN      
        1 maagpisern qdatvyvggl dekvsepllw elflqagpvv nthmpkdrvt gqhqgygfve
       61 flseedadya ikimnmikly gkpirvnkas ahnknldvga nifignldpe idekllydtf
      121 safgvilqtp kimrdpdtgn skgyafinfa sfdasdaaie amngqylcnr pitvsyafkk
      181 dskgerhgsa aerllaaqnp lsqadrphql fadappppsa pnpvvsslgs glpppgmppp
      241 gsfpppvppp galppgippa mppppmppga gghgppaagt pgaghpghgh shphpfppgg
      301 mphpgmsqmq lahhgphglg hphagppgsg gqppprpppg mphpgpppmg mpprgppfgs
      361 pmghpgpmpp hgmrgppplm pphgytgppr pppygyqrgp lppprptprp pvpprgplrg
      421 plpq
//
LOCUS       NP_001008364             171 aa            linear   ROD 27-APR-2025
DEFINITION  AN1-type zinc finger protein 2A [Rattus norvegicus].
ACCESSION   NP_001008364 XP_341041
VERSION     NP_001008364.1
DBSOURCE    REFSEQ: accession NM_001008363.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Stanhill,A., Haynes,C.M., Zhang,Y., Min,G., Steele,M.C.,
            Kalinina,J., Martinez,E., Pickart,C.M., Kong,X.P. and Ron,D.
  TITLE     An arsenite-inducible 19S regulatory particle-associated protein
            adapts proteasomes to proteotoxicity
  JOURNAL   Mol Cell 23 (6), 875-885 (2006)
   PUBMED   16973439
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085928.1.
            
            On Dec 16, 2004 this sequence version replaced XP_341041.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085928.1, FQ096930.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..171
                     /product="AN1-type zinc finger protein 2A"
                     /note="zinc finger, AN1-type domain 2A"
                     /calculated_mol_wt=19136
     Region          10..46
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          100..134
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          135..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2P3.1)"
     CDS             1..171
                     /gene="Zfand2a"
                     /gene_synonym="RGD1310991"
                     /coded_by="NM_001008363.1:251..766"
                     /db_xref="GeneID:360772"
                     /db_xref="RGD:1310991"
ORIGIN      
        1 mefpdlgkhc septckqldf lpitcdackq dfckdhfsys ghkcpfafkk dvqvpvcplc
       61 napipvrrgd ipdvvvgehm drdctfhpgr nrnkvfthrc skegcrkkem lqlacaqchg
      121 nfciqhrhpl dhncqagsss vsrgrssasr aaeqkpsgvs wlaqrlrrtv k
//
LOCUS       NP_001103085             738 aa            linear   ROD 27-APR-2025
DEFINITION  glycogen [starch] synthase, muscle [Rattus norvegicus].
ACCESSION   NP_001103085 XP_001076910 XP_001076928 XP_001076950 XP_001076978
            XP_001077000
VERSION     NP_001103085.1
DBSOURCE    REFSEQ: accession NM_001109615.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Tagliabracci,V.S., Heiss,C., Karthik,C., Contreras,C.J.,
            Glushka,J., Ishihara,M., Azadi,P., Hurley,T.D., DePaoli-Roach,A.A.
            and Roach,P.J.
  TITLE     Phosphate incorporation during glycogen synthesis and Lafora
            disease
  JOURNAL   Cell Metab 13 (3), 274-282 (2011)
   PUBMED   21356517
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Lai,Y.C., Stuenaes,J.T., Kuo,C.H. and Jensen,J.
  TITLE     Insulin-stimulated glycogen synthesis and glycogen synthase
            activation after electrical stimulation of epitrochlearis muscles
            with different initial glycogen contents
  JOURNAL   Arch Physiol Biochem 116 (3), 116-127 (2010)
   PUBMED   20597590
  REMARK    GeneRIF: After contraction insulin-stimulated glycogen synthesis
            was increased by rather similar magnitude at all glycogen contents
            in concert with increased glycogen synthase activation.
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Cameron,J.M., Levandovskiy,V., MacKay,N., Utgikar,R., Ackerley,C.,
            Chiasson,D., Halliday,W., Raiman,J. and Robinson,B.H.
  TITLE     Identification of a novel mutation in GYS1 (muscle-specific
            glycogen synthase) resulting in sudden cardiac death, that is
            diagnosable from skin fibroblasts
  JOURNAL   Mol Genet Metab 98 (4), 378-382 (2009)
   PUBMED   19699667
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Lai,Y.C., Lin,F.C. and Jensen,J.
  TITLE     Glycogen content regulates insulin- but not contraction-mediated
            glycogen synthase activation in the rat slow-twitch soleus muscles
  JOURNAL   Acta Physiol (Oxf) 197 (2), 139-150 (2009)
   PUBMED   19432592
  REMARK    GeneRIF: After contraction, glycogen synthase (GS) was increased to
            similar levels in muscles with low, normal and high glycogen
            content; rate of glycogen synthesis after contraction was also
            similar; insulin increased GS activation at all glycogen contents.
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Grekinis,D., Reimann,E.M. and Schlender,K.K.
  TITLE     Phosphorylation and inactivation of rat heart glycogen synthase by
            cAMP-dependent and cAMP-independent protein kinases
  JOURNAL   Int J Biochem Cell Biol 27 (6), 565-573 (1995)
   PUBMED   7671134
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Lomako,J., Lomako,W.M., Whelan,W.J., Dombro,R.S., Neary,J.T. and
            Norenberg,M.D.
  TITLE     Glycogen synthesis in the astrocyte: from glycogenin to proglycogen
            to glycogen
  JOURNAL   FASEB J 7 (14), 1386-1393 (1993)
   PUBMED   8224611
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Jaspers,S.R., Rulfs,J., Johnson,G.L., Mole,J.E. and Miller,T.B. Jr.
  TITLE     Amino-terminal sequence analysis of rat heart and muscle glycogen
            synthase: homology to the rabbit enzyme and the implications for
            hormonal control
  JOURNAL   Arch Biochem Biophys 268 (2), 630-636 (1989)
   PUBMED   2492421
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Satoh,K. and Sato,K.
  TITLE     Glycogen-binding protein components of rat tissues
  JOURNAL   Biochem Biophys Res Commun 96 (1), 28-33 (1980)
   PUBMED   6449198
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Dietz,M.R., Chiasson,J.L., Soderling,T.R. and Exton,J.H.
  TITLE     Epinephrine regulation of skeletal muscle glycogen metabolism.
            Studies utilizing the perfused rat hindlimb preparation
  JOURNAL   J Biol Chem 255 (6), 2301-2307 (1980)
   PUBMED   6244274
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001077000.1, XP_001076928.1, XP_001076978.1, XP_001076950.1,
            XP_001076910.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC131849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..738
                     /product="glycogen [starch] synthase, muscle"
                     /EC_number="2.4.1.11"
                     /note="glycogen synthase 1, muscle"
                     /calculated_mol_wt=83941
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK and PKA.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1E4; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Region          31..663
                     /region_name="Glycogen_syn"
                     /note="Glycogen synthase; pfam05693"
                     /db_xref="CDD:399009"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Region          632..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1E4; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            711
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13807; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13807; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13807; propagated from
                     UniProtKB/Swiss-Prot (A2RRU1.1)"
     CDS             1..738
                     /gene="Gys1"
                     /coded_by="NM_001109615.1:216..2432"
                     /db_xref="GeneID:690987"
                     /db_xref="RGD:1589798"
ORIGIN      
        1 mplsrslsms slpgledwed efdpenavlf evawevankv ggiytvlqtk akvtgdewgd
       61 nyylvgpyte qgvrtqvell epptpelkrt ldsmnskgck vyfgrwlieg gplvvlldvg
      121 asawalerwk gelwdtcnig vpwydreand avlfgflttw flgeflaqne ekpyvvahfh
      181 ewlagvglcl crarrlpvat iftthatllg rylcagavdf ynnlenfnvd keagerqiyh
      241 rycmeraaah cahvfttvsq itaieaqhll krkpdivtpn glnvkkfsam hefqnlhaqs
      301 kariqefvrg hfyghldfnl dktlyffiag ryefsnkgad iflealarln yllrvngseq
      361 tvvaffimpa rtnnfnvetl kgqavrkqlw dtantvkekf grklyesllv gslpdmnkml
      421 dkedftmmkr aifatqrqsf ppvcthnmld dssdpiltti rriglfnssa drvkvifhpe
      481 flsstspllp vdyeefvrgc hlgvfpsyye pwgytpaect vmgipsistn lsgfgcfmee
      541 hiadpsaygi yildrrfrsl ddscsqltsf lysfcqqsrr qriiqrnrte rlsdlldwky
      601 lgryymsarh malakafpdh ftyephevda tqgyryprpa svppspslsr hssphqsede
      661 eeprdgplre dserydeeee aakdrrnira pewprrascs sstggskrsn svdtgpsssl
      721 stpteplspt sslgeern
//
LOCUS       NP_596871                801 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-4 receptor subunit alpha precursor [Rattus norvegicus].
ACCESSION   NP_596871
VERSION     NP_596871.2
DBSOURCE    REFSEQ: accession NM_133380.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Nakamaru,Y., Takagi,D., Homma,A., Hatakeyama,S. and Fukuda,S.
  TITLE     Oxidative stress regulates IL-4 gene expression in mast cells
            through the reduction of histone deacetylase
  JOURNAL   Otolaryngol Head Neck Surg 152 (1), 48-52 (2015)
   PUBMED   25411311
  REMARK    GeneRIF: Our results suggest that oxidative stress may up-regulate
            IL-4 gene expression in mast cells via a decrease in HDAC activity.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Qiu,Y., Nguyen,K.D., Odegaard,J.I., Cui,X., Tian,X., Locksley,R.M.,
            Palmiter,R.D. and Chawla,A.
  TITLE     Eosinophils and type 2 cytokine signaling in macrophages
            orchestrate development of functional beige fat
  JOURNAL   Cell 157 (6), 1292-1308 (2014)
   PUBMED   24906148
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Leipe,J., Schramm,M.A., Prots,I., Schulze-Koops,H. and Skapenko,A.
  TITLE     Increased Th17 cell frequency and poor clinical outcome in
            rheumatoid arthritis are associated with a genetic variant in the
            IL4R gene, rs1805010
  JOURNAL   Arthritis Rheumatol 66 (5), 1165-1175 (2014)
   PUBMED   24782180
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Garcia-Berrocoso,T., Giralt,D., Bustamante,A., Llombart,V.,
            Rubiera,M., Penalba,A., Boada,C., Espadaler,M., Molina,C. and
            Montaner,J.
  TITLE     Role of beta-defensin 2 and interleukin-4 receptor as stroke
            outcome biomarkers
  JOURNAL   J Neurochem 129 (3), 463-472 (2014)
   PUBMED   24386991
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Chen,G., Nagasawa,R., Imasawa,T., Eto,Y., Kikuchi,K. and
            Maruyama,N.
  TITLE     Identification of soluble interleukin-4 receptor in rat glomerular
            epithelial cells(1)
  JOURNAL   Biochim Biophys Acta 1452 (1), 79-88 (1999)
   PUBMED   10525162
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Grimbacher,B., Holland,S.M. and Puck,J.M.
  TITLE     The interleukin-4 receptor variant Q576R in hyper-IgE syndrome
  JOURNAL   N Engl J Med 338 (15), 1073-1074 (1998)
   PUBMED   9537881
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Hershey,G.K., Friedrich,M.F., Esswein,L.A., Thomas,M.L. and
            Chatila,T.A.
  TITLE     The association of atopy with a gain-of-function mutation in the
            alpha subunit of the interleukin-4 receptor
  JOURNAL   N Engl J Med 337 (24), 1720-1725 (1997)
   PUBMED   9392697
REFERENCE   9  (residues 1 to 801)
  AUTHORS   Richter,G., Hein,G., Blankenstein,T. and Diamantstein,T.
  TITLE     The rat interleukin 4 receptor: coevolution of ligand and receptor
  JOURNAL   Cytokine 7 (3), 237-241 (1995)
   PUBMED   7640343
REFERENCE   10 (residues 1 to 801)
  AUTHORS   Gessner,A., Schroppel,K., Will,A., Enssle,K.H., Lauffer,L. and
            Rollinghoff,M.
  TITLE     Recombinant soluble interleukin-4 (IL-4) receptor acts as an
            antagonist of IL-4 in murine cutaneous Leishmaniasis
  JOURNAL   Infect Immun 62 (10), 4112-4117 (1994)
   PUBMED   7927664
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB015747.1, BQ204155.1 and AW527353.1.
            
            On Oct 23, 2007 this sequence version replaced NP_596871.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB015747.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..801
                     /product="interleukin-4 receptor subunit alpha precursor"
                     /note="interleukin-4 receptor alpha chain; interleukin-4
                     receptor subunit alpha; IL-4R-alpha; IL-4RA; IL-4R subunit
                     alpha; IL-4 receptor subunit alpha; interleukin 4
                     receptor, alpha"
                     /calculated_mol_wt=84078
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2659
     mat_peptide     26..801
                     /product="Interleukin-4 receptor subunit alpha.
                     /id=PRO_0000010892"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
                     /calculated_mol_wt=84078
     Region          28..121
                     /region_name="IL4Ra_N"
                     /note="Interleukin-4 receptor alpha chain, N-terminal;
                     pfam09238"
                     /db_xref="CDD:462720"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Region          123..220
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(123,193,208)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16382; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            order(209..210,212..213)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          212..216
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Site            233..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Region          262..270
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Region          424..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Region          439..549
                     /region_name="Required for IRS1 activation and IL4-induced
                     cell growth. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P24394; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Region          493..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Region          549..644
                     /region_name="Required for IL4-induced gene expression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P24394; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P24394; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P24394; propagated from
                     UniProtKB/Swiss-Prot (Q63257.2)"
     Region          698..703
                     /region_name="ITIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     Region          767..801
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63257.2)"
     CDS             1..801
                     /gene="Il4r"
                     /gene_synonym="Il4ra"
                     /coded_by="NM_133380.2:172..2577"
                     /db_xref="GeneID:25084"
                     /db_xref="RGD:2899"
ORIGIN      
        1 mgwlctkfls svsclillwv tgsggikvlg dptcfsdyir tstcewqlds tvdcssqlll
       61 dyrllfefse nltctpknsa dtvcvcqmai eepiqadtyw lelwsergql wqgsfkpsdn
      121 vkppapdnlt lhtnvsnall lmwsnpypsn nflhkglicm vnisrednpa efkvynvtyt
      181 epklsfpvnt ltsgvryrar vrvlsqsfpg iwsewspsit wynhfqlpll qrlplgvsis
      241 cicillfclt cyfsiikikk iwwdqiptpa rsplaaiiiq dtkvslwekq trsqestksr
      301 hwktcltkll pcllehrvkk erespkaakt kplqspekag wypaevsrtv lwpenvhvsv
      361 vrcmelfeap vqnveeeede mvkgdlsmsp ensgggfqes qadimarlte nlfsdllgae
      421 nggvgqssma esssllpses gqastswacf ptgpsettcq vtgqqpphpd peratgtact
      481 qvplvisdnp ayrsfsdfss papnpgelas eqkqaghlee gdllspvdph ssgppmqqae
      541 sweqilhmsv lqhgtagstp aptsgyqefv qavkqgasqd agvpgvgpsg dtgykafssl
      601 lsssgvctdt aaagtdsgcg gykpfqnpvp nqspnsmplf tfgldmelpp splnsappns
      661 tpeclglelg lkggtwlkap ppseqvpkpf gddlglgivy ssltchlcgh lkqhhsqeed
      721 gqihvvaspg cgccydeksp slgnlsgtle scpgemsqea nltlaprtps nlsgvgkgpg
      781 hspvpsqtte vpvgtlgvtv s
//
LOCUS       NP_036832                288 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-1B [Rattus norvegicus].
ACCESSION   NP_036832 XP_346562
VERSION     NP_036832.1
DBSOURCE    REFSEQ: accession NM_012700.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Vardar,G., Chang,S., Arancillo,M., Wu,Y.J., Trimbuch,T. and
            Rosenmund,C.
  TITLE     Distinct Functions of Syntaxin-1 in Neuronal Maintenance, Synaptic
            Vesicle Docking, and Fusion in Mouse Neurons
  JOURNAL   J Neurosci 36 (30), 7911-7924 (2016)
   PUBMED   27466336
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Gu,Y., Chiu,S.L., Liu,B., Wu,P.H., Delannoy,M., Lin,D.T., Wirtz,D.
            and Huganir,R.L.
  TITLE     Differential vesicular sorting of AMPA and GABAA receptors
  JOURNAL   Proc Natl Acad Sci U S A 113 (7), E922-E931 (2016)
   PUBMED   26839408
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Murphy,S., Zweyer,M., Henry,M., Meleady,P., Mundegar,R.R.,
            Swandulla,D. and Ohlendieck,K.
  TITLE     Label-free mass spectrometric analysis reveals complex changes in
            the brain proteome from the mdx-4cv mouse model of Duchenne
            muscular dystrophy
  JOURNAL   Clin Proteomics 12, 27 (2015)
   PUBMED   26604869
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Mishima,T., Fujiwara,T., Sanada,M., Kofuji,T., Kanai-Azuma,M. and
            Akagawa,K.
  TITLE     Syntaxin 1B, but not syntaxin 1A, is necessary for the regulation
            of synaptic vesicle exocytosis and of the readily releasable pool
            at central synapses
  JOURNAL   PLoS One 9 (2), e90004 (2014)
   PUBMED   24587181
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Arancillo,M., Min,S.W., Gerber,S., Munster-Wandowski,A., Wu,Y.J.,
            Herman,M., Trimbuch,T., Rah,J.C., Ahnert-Hilger,G., Riedel,D.,
            Sudhof,T.C. and Rosenmund,C.
  TITLE     Titration of Syntaxin1 in mammalian synapses reveals multiple roles
            in vesicle docking, priming, and release probability
  JOURNAL   J Neurosci 33 (42), 16698-16714 (2013)
   PUBMED   24133272
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Li,C., Ullrich,B., Zhang,J.Z., Anderson,R.G., Brose,N. and
            Sudhof,T.C.
  TITLE     Ca(2+)-dependent and -independent activities of neural and
            non-neural synaptotagmins
  JOURNAL   Nature 375 (6532), 594-599 (1995)
   PUBMED   7791877
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Pevsner,J., Hsu,S.C. and Scheller,R.H.
  TITLE     n-Sec1: a neural-specific syntaxin-binding protein
  JOURNAL   Proc Natl Acad Sci U S A 91 (4), 1445-1449 (1994)
   PUBMED   8108429
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Bennett,M.K., Garcia-Arraras,J.E., Elferink,L.A., Peterson,K.,
            Fleming,A.M., Hazuka,C.D. and Scheller,R.H.
  TITLE     The syntaxin family of vesicular transport receptors
  JOURNAL   Cell 74 (5), 863-873 (1993)
   PUBMED   7690687
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bennett,M.K., Calakos,N. and Scheller,R.H.
  TITLE     Syntaxin: a synaptic protein implicated in docking of synaptic
            vesicles at presynaptic active zones
  JOURNAL   Science 257 (5067), 255-259 (1992)
   PUBMED   1321498
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and M95735.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346562.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.5488.1, M95735.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..288
                     /product="syntaxin-1B"
                     /note="syntaxin 1B2; P35B; Syntaxin 2"
                     /calculated_mol_wt=33114
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61265.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61264; propagated from
                     UniProtKB/Swiss-Prot (P61265.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12692561,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P61265.1)"
     Region          29..180
                     /region_name="SynN"
                     /note="Syntaxin N-terminus domain; syntaxins are nervous
                     system-specific proteins implicated in the docking of
                     synaptic vesicles with the presynaptic plasma membrane;
                     they are a family of receptors for intracellular transport
                     vesicles; each target membrane may...; cd00179"
                     /db_xref="CDD:238105"
     Site            order(29,33,40,113..114,117..118,121,124..125,131,134,165)
                     /site_type="active"
                     /note="nSec1 interaction sites [active]"
                     /db_xref="CDD:238105"
     Site            order(60,71,74..75,82,86,89,96,119,124,127,133,140..141,
                     144..145,147..148,151,177)
                     /site_type="active"
                     /note="interdomain interaction site [active]"
                     /db_xref="CDD:238105"
     Site            order(157..167,176..180)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238105"
     Region          190..258
                     /region_name="SNARE_syntaxin1"
                     /note="SNARE motif of syntaxin 1; cd15880"
                     /db_xref="CDD:277233"
     Site            order(195,197..198,200..205,207..209,211..212,214..216,
                     218..219,221..223,225..226,228..233,235..240,242..247,
                     249..251)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277233"
     Site            order(212,215..216,219..220,222..224,227..233,235..237,
                     239..244)
                     /site_type="other"
                     /note="Munc18 interface [polypeptide binding]"
                     /db_xref="CDD:277233"
     Site            225
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277233"
     Site            252..253
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type C (BoNT/C).
                     /evidence=ECO:0000269|PubMed:7737992; propagated from
                     UniProtKB/Swiss-Prot (P61265.1)"
     Site            265..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P61265.1)"
     CDS             1..288
                     /gene="Stx1b"
                     /gene_synonym="Stx1b2; Stx2"
                     /coded_by="NM_012700.2:52..918"
                     /db_xref="GeneID:24923"
                     /db_xref="RGD:3784"
ORIGIN      
        1 mkdrtqelrs akdsddeeev vhvdrdhfmd effeqveeir gcieklsedv eqvkkqhsai
       61 laapnpdekt kqeledltad ikktankvrs klkaieqsie qeeglnrssa dlrirktqhs
      121 tlsrkfvevm teynatqsky rdrckdriqr qleitgrttt neeledmles gklaiftddi
      181 kmdsqmtkqa lneietrhne iikletsire lhdmfvdmam lvesqgemid rieynvehsv
      241 dyveravsdt kkavkyqska rrkkimiiic cvvlgvvlas siggtlgl
//
LOCUS       NP_036971                105 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c, somatic [Rattus norvegicus].
ACCESSION   NP_036971
VERSION     NP_036971.1
DBSOURCE    REFSEQ: accession NM_012839.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Serrya,M.S., Nader,M.A. and Abdelmageed,M.E.
  TITLE     Hepatoprotective effect of the tyrosine kinase inhibitor nilotinib
            against cyclosporine-A induced liver injury in rats through
            blocking the Bax/Cytochrome C/caspase-3 apoptotic signaling pathway
  JOURNAL   J Biochem Mol Toxicol 35 (6), 1-13 (2021)
   PUBMED   33710703
  REMARK    GeneRIF: Hepatoprotective effect of the tyrosine kinase inhibitor
            nilotinib against cyclosporine-A induced liver injury in rats
            through blocking the Bax/Cytochrome C/caspase-3 apoptotic signaling
            pathway.
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Ye,L. and Yang,S.
  TITLE     [Sirtuin 3 inhibits cardiomyocyte apoptosis by reducing cytochrome
            C release in myocardiac H9c2 cells with calcium overload]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 31 (8), 1031-1035 (2015)
   PUBMED   26271974
  REMARK    GeneRIF: Data show that sirtuin 3 could inhibit cell apoptosis by
            reducing cytochrome C (CytC) release and inhibiting caspase-3
            activation in cardiomyocyte models with calcium overload.
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gao,G., Yu,Z., Yan,J., Li,J., Shen,S., Jia,B., Guan,K., Gao,X. and
            Kan,Q.
  TITLE     Poly (ADP-ribose) polymerase- and cytochrome c-mediated apoptosis
            induces hepatocyte injury in a rat model of hyperammonia-induced
            hepatic failure
  JOURNAL   Mol Med Rep 11 (6), 4211-4219 (2015)
   PUBMED   25634059
  REMARK    GeneRIF: results suggested that hepatocyte injury and liver
            dysfunction may be caused by inducing apoptosis via the PARP and
            Cyt C pathways.
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Pu,H., Wang,X., Su,L., Ma,C., Zhang,Y., Zhang,L., Chen,X., Li,X.,
            Wang,H., Liu,X. and Zhang,J.
  TITLE     Heroin activates ATF3 and CytC via c-Jun N-terminal kinase pathways
            to mediate neuronal apoptosis
  JOURNAL   Med Sci Monit Basic Res 21, 53-62 (2015)
   PUBMED   25848832
  REMARK    GeneRIF: Heroin activates ATF3 and CytC via c-Jun N-terminal kinase
            pathways to mediate neuronal apoptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Ogneva,I.V., Birjukov,N.S., Veselova,O.M. and Larina,I.M.
  TITLE     [Cytochrome C content and mitochondrial activity in rat's cardiac
            and skeletal muscle cells in the course of 3-day gravitational
            unloading]
  JOURNAL   Aviakosm Ekolog Med 48 (6), 23-29 (2014)
   PUBMED   25928980
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Virbasius,J.V. and Scarpulla,R.C.
  TITLE     Structure and expression of rodent genes encoding the
            testis-specific cytochrome c. Differences in gene structure and
            evolution between somatic and testicular variants
  JOURNAL   J Biol Chem 263 (14), 6791-6796 (1988)
   PUBMED   2834389
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Penney,D.G., Zak,R. and Aschenbrenner,V.
  TITLE     Carbon monoxide inhalation: effect on heart cytochrome c in the
            neonatal and adult rat
  JOURNAL   J Toxicol Environ Health 12 (2-3), 395-406 (1983)
   PUBMED   6317876
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Scarpulla,R.C. and Wu,R.
  TITLE     Nonallelic members of the cytochrome c multigene family of the rat
            may arise through different messenger RNAs
  JOURNAL   Cell 32 (2), 473-482 (1983)
   PUBMED   6130852
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Scarpulla,R.C., Agne,K.M. and Wu,R.
  TITLE     Isolation and structure of a rat cytochrome c gene
  JOURNAL   J Biol Chem 256 (12), 6480-6486 (1981)
   PUBMED   6263917
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Carlson,S.S., Mross,G.A., Wilson,A.C., Mead,R.T., Wolin,L.D.,
            Bowers,S.F., Foley,N.T., Muijsers,A.O. and Margoliash,E.
  TITLE     Primary structure of mouse, rat, and guinea pig cytochrome c
  JOURNAL   Biochemistry 16 (7), 1437-1442 (1977)
   PUBMED   191069
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081849.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081849.1, FQ219963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132293, SAMD00132294
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..105
                     /product="cytochrome c, somatic"
                     /note="Cytochrome C, expressed in somatic tissues"
                     /calculated_mol_wt=11474
     Region          2..100
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000269|PubMed:191069; propagated from
                     UniProtKB/Swiss-Prot (P62898.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62894; propagated from
                     UniProtKB/Swiss-Prot (P62898.2)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62897; propagated from
                     UniProtKB/Swiss-Prot (P62898.2)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62894; propagated from
                     UniProtKB/Swiss-Prot (P62898.2)"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62897; propagated from
                     UniProtKB/Swiss-Prot (P62898.2)"
     CDS             1..105
                     /gene="Cycs"
                     /gene_synonym="CYCSA"
                     /coded_by="NM_012839.2:76..393"
                     /db_xref="GeneID:25309"
                     /db_xref="RGD:2451"
ORIGIN      
        1 mgdvekgkki fvqkcaqcht vekggkhktg pnlhglfgrk tgqaagfsyt danknkgitw
       61 gedtlmeyle npkkyipgtk mifagikkkg eradliaylk katne
//
LOCUS       NP_620233                 81 aa            linear   ROD 27-APR-2025
DEFINITION  ubiquitin-like protein NEDD8 [Rattus norvegicus].
ACCESSION   NP_620233
VERSION     NP_620233.1
DBSOURCE    REFSEQ: accession NM_138878.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Bayraktar,G., Yuanxiang,P., Confettura,A.D., Gomes,G.M., Raza,S.A.,
            Stork,O., Tajima,S., Suetake,I., Karpova,A., Yildirim,F. and
            Kreutz,M.R.
  TITLE     Synaptic control of DNA methylation involves activity-dependent
            degradation of DNMT3A1 in the nucleus
  JOURNAL   Neuropsychopharmacology 45 (12), 2120-2130 (2020)
   PUBMED   32726795
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Zhang,Q.G., Han,D., Wang,R.M., Dong,Y., Yang,F., Vadlamudi,R.K. and
            Brann,D.W.
  TITLE     C terminus of Hsc70-interacting protein (CHIP)-mediated degradation
            of hippocampal estrogen receptor-alpha and the critical period
            hypothesis of estrogen neuroprotection
  JOURNAL   Proc Natl Acad Sci U S A 108 (35), E617-E624 (2011)
   PUBMED   21808025
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Buchwalter,A., Van Dort,C., Schultz,S., Smith,R., Le,I.P.,
            Abbott,J.L., Oosterhouse,E., Johnson,A.E., Hansen-Smith,F. and
            Burnatowska-Hledin,M.
  TITLE     Expression of VACM-1/cul5 mutant in endothelial cells induces MAPK
            phosphorylation and maspin degradation and converts cells to the
            angiogenic phenotype
  JOURNAL   Microvasc Res 75 (2), 155-168 (2008)
   PUBMED   17950367
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Huang,D.T., Paydar,A., Zhuang,M., Waddell,M.B., Holton,J.M. and
            Schulman,B.A.
  TITLE     Structural basis for recruitment of Ubc12 by an E2 binding domain
            in NEDD8's E1
  JOURNAL   Mol Cell 17 (3), 341-350 (2005)
   PUBMED   15694336
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Dil Kuazi,A., Kito,K., Abe,Y., Shin,R.W., Kamitani,T. and Ueda,N.
  TITLE     NEDD8 protein is involved in ubiquitinated inclusion bodies
  JOURNAL   J Pathol 199 (2), 259-266 (2003)
   PUBMED   12533840
REFERENCE   7  (residues 1 to 81)
  AUTHORS   Antenos,M., Casper,R.F. and Brown,T.J.
  TITLE     Interaction with Nedd8, a ubiquitin-like protein, enhances the
            transcriptional activity of the aryl hydrocarbon receptor
  JOURNAL   J Biol Chem 277 (46), 44028-44034 (2002)
   PUBMED   12215427
REFERENCE   8  (residues 1 to 81)
  AUTHORS   Singer,J.D., Gurian-West,M., Clurman,B. and Roberts,J.M.
  TITLE     Cullin-3 targets cyclin E for ubiquitination and controls S phase
            in mammalian cells
  JOURNAL   Genes Dev 13 (18), 2375-2387 (1999)
   PUBMED   10500095
REFERENCE   9  (residues 1 to 81)
  AUTHORS   Page,R., Morris,C., Williams,J., von Ruhland,C. and Malik,A.N.
  TITLE     Isolation of diabetes-associated kidney genes using differential
            display
  JOURNAL   Biochem Biophys Res Commun 232 (1), 49-53 (1997)
   PUBMED   9125149
REFERENCE   10 (residues 1 to 81)
  AUTHORS   Lee,N.H., Weinstock,K.G., Kirkness,E.F., Earle-Hughes,J.A.,
            Fuldner,R.A., Marmaros,S., Glodek,A., Gocayne,J.D., Adams,M.D.,
            Kerlavage,A.R. et al.
  TITLE     Comparative expressed-sequence-tag analysis of differential gene
            expression profiles in PC-12 cells before and after nerve growth
            factor treatment
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8303-8307 (1995)
   PUBMED   7667285
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB581170.1 and BC084728.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084728.1, CB576942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMD00132295
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..81
                     /product="ubiquitin-like protein NEDD8"
                     /note="neural precursor cell expressed, developmentally
                     down-regulated gene 8; neddylin; neural precursor cell
                     expressed, developmentally down-regulated 8"
                     /calculated_mol_wt=8841
     mat_peptide     1..76
                     /product="Ubiquitin-like protein NEDD8.
                     /id=PRO_0000042773"
                     /note="propagated from UniProtKB/Swiss-Prot (Q71UE8.1)"
                     /calculated_mol_wt=8560
     Region          3..76
                     /region_name="Ubl_NEDD8"
                     /note="ubiquitin-like (Ubl) domain found in neural
                     precursor cell expressed developmentally down-regulated
                     protein 8 (NEDD8) and similar proteins; cd01806"
                     /db_xref="CDD:340504"
     Site            order(6..10,28..29,31..32,34..37,40,42,44,47..49,68,
                     70..76)
                     /site_type="other"
                     /note="E1/E2/E3 interaction site [polypeptide binding]"
                     /db_xref="CDD:340504"
     Site            order(6,8..9,40,42,44..54,59,68,70..76)
                     /site_type="other"
                     /note="NEDP1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340504"
     Site            order(6..11,31..37,39..40,47,68,70..74)
                     /site_type="other"
                     /note="bacterial deamidase effectors interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:340504"
     Site            order(6,11,27,29,48)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340504"
     Site            8
                     /site_type="other"
                     /note="Interaction with UBE1C.
                     /evidence=ECO:0000250|UniProtKB:Q15843; propagated from
                     UniProtKB/Swiss-Prot (Q71UE8.1)"
     Site            44
                     /site_type="other"
                     /note="Interaction with UBE1C.
                     /evidence=ECO:0000250|UniProtKB:Q15843; propagated from
                     UniProtKB/Swiss-Prot (Q71UE8.1)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P29595; propagated from
                     UniProtKB/Swiss-Prot (Q71UE8.1)"
     Region          70..72
                     /region_name="Interaction with UBE1C.
                     /evidence=ECO:0000250|UniProtKB:Q15843"
                     /note="propagated from UniProtKB/Swiss-Prot (Q71UE8.1)"
     CDS             1..81
                     /gene="Nedd8"
                     /gene_synonym="CDK8"
                     /coded_by="NM_138878.2:260..505"
                     /db_xref="GeneID:25490"
                     /db_xref="RGD:3158"
ORIGIN      
        1 mlikvktltg keieidiept dkverikerv eekegippqq qrliysgkqm ndektaadyk
       61 ilggsvlhlv lalrgggglg q
//
LOCUS       NP_476478                230 aa            linear   ROD 27-APR-2025
DEFINITION  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase [Rattus
            norvegicus].
ACCESSION   NP_476478
VERSION     NP_476478.1
DBSOURCE    REFSEQ: accession NM_057137.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Herman,G.E.
  TITLE     Disorders of cholesterol biosynthesis: prototypic metabolic
            malformation syndromes
  JOURNAL   Hum Mol Genet 12 Spec No 1, R75-R88 (2003)
   PUBMED   12668600
  REMARK    Review article
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Bae,S., Seong,J. and Paik,Y.
  TITLE     Cholesterol biosynthesis from lanosterol: molecular cloning,
            chromosomal localization, functional expression and liver-specific
            gene regulation of rat sterol delta8-isomerase, a cholesterogenic
            enzyme with multiple functions
  JOURNAL   Biochem J 353 (Pt 3), 689-699 (2001)
   PUBMED   11171067
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Seo,K.W., Kon,Y. and Watanabe,T.
  TITLE     Embryonic hematopoiesis defect in the tattered-Hokkaido (Tdho)
            mouse
  JOURNAL   Comp Med 50 (1), 27-31 (2000)
   PUBMED   10987663
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Dussossoy,D., Carayon,P., Belugou,S., Feraut,D., Bord,A.,
            Goubet,C., Roque,C., Vidal,H., Combes,T., Loison,G. and Casellas,P.
  TITLE     Colocalization of sterol isomerase and sigma(1) receptor at
            endoplasmic reticulum and nuclear envelope level
  JOURNAL   Eur J Biochem 263 (2), 377-386 (1999)
   PUBMED   10406945
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Braverman,N., Lin,P., Moebius,F.F., Obie,C., Moser,A.,
            Glossmann,H., Wilcox,W.R., Rimoin,D.L., Smith,M., Kratz,L.,
            Kelley,R.I. and Valle,D.
  TITLE     Mutations in the gene encoding 3 beta-hydroxysteroid-delta 8, delta
            7-isomerase cause X-linked dominant Conradi-Hunermann syndrome
  JOURNAL   Nat Genet 22 (3), 291-294 (1999)
   PUBMED   10391219
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Derry,J.M., Gormally,E., Means,G.D., Zhao,W., Meindl,A.,
            Kelley,R.I., Boyd,Y. and Herman,G.E.
  TITLE     Mutations in a delta 8-delta 7 sterol isomerase in the tattered
            mouse and X-linked dominant chondrodysplasia punctata.
            jderry@immunex.com
  JOURNAL   Nat Genet 22 (3), 286-290 (1999)
   PUBMED   10391218
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Moebius,F.F., Soellner,K.E., Fiechtner,B., Huck,C.W., Bonn,G. and
            Glossmann,H.
  TITLE     Histidine77, glutamic acid81, glutamic acid123, threonine126,
            asparagine194, and tryptophan197 of the human emopamil binding
            protein are required for in vivo sterol delta 8-delta 7
            isomerization
  JOURNAL   Biochemistry 38 (3), 1119-1127 (1999)
   PUBMED   9894009
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Silve,S., Dupuy,P.H., Labit-Lebouteiller,C., Kaghad,M., Chalon,P.,
            Rahier,A., Taton,M., Lupker,J., Shire,D. and Loison,G.
  TITLE     Emopamil-binding protein, a mammalian protein that binds a series
            of structurally diverse neuroprotective agents, exhibits
            delta8-delta7 sterol isomerase activity in yeast
  JOURNAL   J Biol Chem 271 (37), 22434-22440 (1996)
   PUBMED   8798407
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF071501.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF071501.1, FQ112249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..230
                     /product="3-beta-hydroxysteroid-Delta(8),
                     Delta(7)-isomerase"
                     /EC_number="5.3.3.5"
                     /EC_number="3.3.2.11"
                     /note="sterol 8-isomerase; D8-D7 sterol isomerase;
                     emopamil-binding protein; emopamil binding protein (sterol
                     isomerase); cholestenol Delta-isomerase; delta(8)-Delta(7)
                     sterol isomerase; phenylalkylamine Ca2+ antagonist
                     (emopamil) binding protein; cholesterol-5,6-epoxide
                     hydrolase subunit EBP"
                     /calculated_mol_wt=26606
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15125; propagated from
                     UniProtKB/Swiss-Prot (Q9JJ46.3)"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ46.3)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ46.3)"
     Region          96..207
                     /region_name="EBP"
                     /note="EXPERA (EXPanded EBP superfamily); pfam05241"
                     /db_xref="CDD:461600"
     Site            121..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ46.3)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ46.3)"
     CDS             1..230
                     /gene="Ebp"
                     /coded_by="NM_057137.1:103..795"
                     /db_xref="GeneID:117278"
                     /db_xref="RGD:620957"
ORIGIN      
        1 mttnmlplhp ywprhlrldn fvpndlptwh ilvglfsfsg vlivitwlls srvsvvplgt
       61 grrlalcwfa vctfihlvie gwfsfyheil ledqaflsql wkeyskgdsr yilsdgfivc
      121 mesvtaclwg plslwvviaf lrhqpfrfvl qlvvsvgqiy gdvlyfltel rdgfqhgelg
      181 hplyfwfyfv imnaiwlvip gilvfdaikh ltnaqsmldn kvmkikskhn
//
LOCUS       NP_001128489             172 aa            linear   ROD 27-APR-2025
DEFINITION  myosin regulatory light chain RLC-A [Rattus norvegicus].
ACCESSION   NP_001128489
VERSION     NP_001128489.1
DBSOURCE    REFSEQ: accession NM_001135017.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Toepfer,C.N., Sikkel,M.B., Caorsi,V., Vydyanath,A., Torre,I.,
            Copeland,O., Lyon,A.R., Marston,S.B., Luther,P.K., Macleod,K.T.,
            West,T.G. and Ferenczi,M.A.
  TITLE     A post-MI power struggle: adaptations in cardiac power occur at the
            sarcomere level alongside MyBP-C and RLC phosphorylation
  JOURNAL   Am J Physiol Heart Circ Physiol 311 (2), H465-H475 (2016)
   PUBMED   27233767
  REMARK    GeneRIF: Phosphorylation of myosin regulatory light chain (RLC)
            increased and remained elevated post-MI, while phosphorylation of
            myosin binding protein-C (MyBP-C) was initially depressed but then
            increased as the hearts became decompensated.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Kiyomitsu,T. and Cheeseman,I.M.
  TITLE     Cortical dynein and asymmetric membrane elongation coordinately
            position the spindle in anaphase
  JOURNAL   Cell 154 (2), 391-402 (2013)
   PUBMED   23870127
  REMARK    Erratum:[Cell. 2013 Sep 12;154(6):1401]
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Frobel,J., Cadeddu,R.P., Hartwig,S., Bruns,I., Wilk,C.M.,
            Kundgen,A., Fischer,J.C., Schroeder,T., Steidl,U.G., Germing,U.,
            Lehr,S., Haas,R. and Czibere,A.
  TITLE     Platelet proteome analysis reveals integrin-dependent aggregation
            defects in patients with myelodysplastic syndromes
  JOURNAL   Mol Cell Proteomics 12 (5), 1272-1280 (2013)
   PUBMED   23382103
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Park,I., Han,C., Jin,S., Lee,B., Choi,H., Kwon,J.T., Kim,D.,
            Kim,J., Lifirsu,E., Park,W.J., Park,Z.Y., Kim,D.H. and Cho,C.
  TITLE     Myosin regulatory light chains are required to maintain the
            stability of myosin II and cellular integrity
  JOURNAL   Biochem J 434 (1), 171-180 (2011)
   PUBMED   21126233
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Noda,Y., Horikawa,S., Katayama,Y. and Sasaki,S.
  TITLE     Identification of a multiprotein 'motor' complex binding to water
            channel aquaporin-2
  JOURNAL   Biochem Biophys Res Commun 330 (4), 1041-1047 (2005)
   PUBMED   15823548
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Wang,Y. and Chantler,P.D.
  TITLE     Functional analysis of individual brain myosin II isoforms through
            hybrid formation
  JOURNAL   FEBS Lett 348 (3), 244-248 (1994)
   PUBMED   8034049
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Feinstein,D.L., Durand,M. and Milner,R.J.
  TITLE     Expression of myosin regulatory light chains in rat brain:
            characterization of a novel isoform
  JOURNAL   Brain Res Mol Brain Res 10 (2), 97-105 (1991)
   PUBMED   1649372
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Grant,J.W., Taubman,M.B., Church,S.L., Johnson,R.L. and
            Nadal-Ginard,B.
  TITLE     Mammalian nonsarcomeric myosin regulatory light chains are encoded
            by two differentially regulated and linked genes
  JOURNAL   J Cell Biol 111 (3), 1127-1135 (1990)
   PUBMED   2391362
  REMARK    Erratum:[J Cell Biol 1990 Nov;111(5 Pt 1):2207]
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Taubman,M.B., Grant,J.W. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of mammalian myosin regulatory light
            chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric,
            and nonmuscle tissues
  JOURNAL   J Cell Biol 104 (6), 1505-1513 (1987)
   PUBMED   3584239
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV767772.1, X05566.1 and BQ207032.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217399.1, FQ229140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..172
                     /product="myosin regulatory light chain RLC-A"
                     /note="myosin RLC-A; myosin, light chain 12A, regulatory,
                     non-sarcomeric"
                     /calculated_mol_wt=19764
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13832.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MLCK. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P13832.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MLCK. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P13832.2)"
     Region          25..163
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..172
                     /gene="Myl12a"
                     /gene_synonym="RGD1309537; Rlc-a"
                     /coded_by="NM_001135017.1:128..646"
                     /db_xref="GeneID:501203"
                     /db_xref="RGD:1309537"
ORIGIN      
        1 msskraktkt tkkrpqrats nvfamfdqsq iqefkeafnm idqnrdgfid kedlhdmlas
       61 mgknptdeyl dammneapgp inftmfltmf geklngtdpe dvirnafacf deeaigtiqe
      121 dylrellttm gdrftdeevd elyreapidk kgnfnyieft rilkhgakdk dd
//
LOCUS       NP_852046                657 aa            linear   ROD 27-APR-2025
DEFINITION  broad substrate specificity ATP-binding cassette transporter ABCG2
            [Rattus norvegicus].
ACCESSION   NP_852046
VERSION     NP_852046.1
DBSOURCE    REFSEQ: accession NM_181381.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Chen,F., Wang,L., Zhai,X., Wang,N., Qin,Y., Zhu,C., Wu,S. and Lu,Y.
  TITLE     Effect of capsaicin on breast cancer resistance protein
            (BCRP/Abcg2) and pharmacokinetics of probe substrates in rats
  JOURNAL   Xenobiotica 52 (2), 209-217 (2022)
   PUBMED   35345975
  REMARK    GeneRIF: Effect of capsaicin on breast cancer resistance protein
            (BCRP/Abcg2) and pharmacokinetics of probe substrates in rats.
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Wu,T., Sheng,Y., Qin,Y.Y., Kong,W.M., Jin,M.M., Yang,H.Y.,
            Zheng,X.K., Dai,C., Liu,M., Liu,X.D. and Liu,L.
  TITLE     Bile duct ligation causes opposite impacts on the expression and
            function of BCRP and P-gp in rat brain partly via affecting
            membrane expression of ezrin/radixin/moesin proteins
  JOURNAL   Acta Pharmacol Sin 42 (11), 1942-1950 (2021)
   PUBMED   33558655
  REMARK    GeneRIF: Bile duct ligation causes opposite impacts on the
            expression and function of BCRP and P-gp in rat brain partly via
            affecting membrane expression of ezrin/radixin/moesin proteins.
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Ganguly,S., Finkelstein,D., Shaw,T.I., Michalek,R.D., Zorn,K.M.,
            Ekins,S., Yasuda,K., Fukuda,Y., Schuetz,J.D., Mukherjee,K. and
            Schuetz,E.G.
  TITLE     Metabolomic and transcriptomic analysis reveals endogenous
            substrates and metabolic adaptation in rats lacking Abcg2 and
            Abcb1a transporters
  JOURNAL   PLoS One 16 (7), e0253852 (2021)
   PUBMED   34255797
  REMARK    GeneRIF: Metabolomic and transcriptomic analysis reveals endogenous
            substrates and metabolic adaptation in rats lacking Abcg2 and
            Abcb1a transporters.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Taniguchi,T., Omura,K., Motoki,K., Sakai,M., Chikamatsu,N.,
            Ashizawa,N., Takada,T. and Iwanaga,T.
  TITLE     Hypouricemic agents reduce indoxyl sulfate excretion by inhibiting
            the renal transporters OAT1/3 and ABCG2
  JOURNAL   Sci Rep 11 (1), 7232 (2021)
   PUBMED   33790363
  REMARK    GeneRIF: Hypouricemic agents reduce indoxyl sulfate excretion by
            inhibiting the renal transporters OAT1/3 and ABCG2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Morimoto,C., Tamura,Y., Asakawa,S., Kuribayashi-Okuma,E.,
            Nemoto,Y., Li,J., Murase,T., Nakamura,T., Hosoyamada,M., Uchida,S.
            and Shibata,S.
  TITLE     ABCG2 expression and uric acid metabolism of the intestine in
            hyperuricemia model rat
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 39 (5), 744-759 (2020)
   PUBMED   31983315
  REMARK    GeneRIF: ABCG2 expression and uric acid metabolism of the intestine
            in hyperuricemia model rat.
            Erratum:[Nucleosides Nucleotides Nucleic Acids.
            2020;39(10-12):1474. doi: 10.1080/15257770.2020.1834331. PMID:
            33231139]
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Jonker,J.W., Buitelaar,M., Wagenaar,E., Van Der Valk,M.A.,
            Scheffer,G.L., Scheper,R.J., Plosch,T., Kuipers,F., Elferink,R.P.,
            Rosing,H., Beijnen,J.H. and Schinkel,A.H.
  TITLE     The breast cancer resistance protein protects against a major
            chlorophyll-derived dietary phototoxin and protoporphyria
  JOURNAL   Proc Natl Acad Sci U S A 99 (24), 15649-15654 (2002)
   PUBMED   12429862
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Steinbach,D., Sell,W., Voigt,A., Hermann,J., Zintl,F. and
            Sauerbrey,A.
  TITLE     BCRP gene expression is associated with a poor response to
            remission induction therapy in childhood acute myeloid leukemia
  JOURNAL   Leukemia 16 (8), 1443-1447 (2002)
   PUBMED   12145683
REFERENCE   8  (residues 1 to 657)
  AUTHORS   Sauerbrey,A., Sell,W., Steinbach,D., Voigt,A. and Zintl,F.
  TITLE     Expression of the BCRP gene (ABCG2/MXR/ABCP) in childhood acute
            lymphoblastic leukaemia
  JOURNAL   Br J Haematol 118 (1), 147-150 (2002)
   PUBMED   12100141
REFERENCE   9  (residues 1 to 657)
  AUTHORS   Faneyte,I.F., Kristel,P.M., Maliepaard,M., Scheffer,G.L.,
            Scheper,R.J., Schellens,J.H. and van de Vijver,M.J.
  TITLE     Expression of the breast cancer resistance protein in breast cancer
  JOURNAL   Clin Cancer Res 8 (4), 1068-1074 (2002)
   PUBMED   11948115
REFERENCE   10 (residues 1 to 657)
  AUTHORS   Doyle,L.A., Yang,W., Abruzzo,L.V., Krogmann,T., Gao,Y., Rishi,A.K.
            and Ross,D.D.
  TITLE     A multidrug resistance transporter from human MCF-7 breast cancer
            cells
  JOURNAL   Proc Natl Acad Sci U S A 95 (26), 15665-15670 (1998)
   PUBMED   9861027
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1999 Mar 2;96(5):2569]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY089997.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY089997.1, AB105817.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..657
                     /product="broad substrate specificity ATP-binding cassette
                     transporter ABCG2"
                     /EC_number="7.6.2.2"
                     /note="ATP-binding cassette sub-family G member 2; breast
                     cancer resistance protein 1 homolog; ATP-binding cassette,
                     sub-family G (WHITE), member 2; ATP-binding cassette
                     protein G2; urate exporter; ATP binding cassette subfamily
                     G member 2 (Junior blood group); ATP-binding cassette,
                     subfamily G (WHITE), member 2"
                     /calculated_mol_wt=72830
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Region          46..651
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            429..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            507..527
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            596
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80W57.1)"
     Site            633..653
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W57.1)"
     CDS             1..657
                     /gene="Abcg2"
                     /gene_synonym="Bcrp; BCRP1"
                     /coded_by="NM_181381.2:82..2055"
                     /db_xref="GeneID:312382"
                     /db_xref="RGD:631345"
ORIGIN      
        1 msssndhvlv pmsqrnkngl pgmssrgart laegdvlsfh hityrvkvks gflvrktaek
       61 eilsdingim kpglnailgp tgggksslld vlaarkdprg lsgdvlinga pqpanfkcss
      121 gyvvqddvvm gtltvrenlq fsaalrlpka mkthekneri ntiikelgld kvadskvgtq
      181 ftrgisgger krtsigmeli tdpsilflde pttgldssta navllllkrm skqgrtiifs
      241 ihqprysifk lfdsltllas gklmfhgpaq kaleyfasag yhcepynnpa dffldvingd
      301 ssavmlnrge qdheanktee pskrekpiie nlaefyinst iygetkaeld qlpvaqkkkg
      361 ssafrepvyv tsfchqlrwi arrsfknllg npqasvaqli vtvilgliig alyfglkndp
      421 tgmqnragvf fflttnqcft svsavelfvv ekklfiheyi sgyyrvssyf fgklvsdllp
      481 mrflpsviyt cllyfmlglk rtveaffimm ftlimvayta ssmalaiaag qsvvsvatll
      541 mtisfvfmml fsgllvnlrt igpwlswlqy fsiprygfta lqhneflgqe fcpglnvtmn
      601 stcvnsytic tgndylinqg idlspwglwr nhvalacmii ifltiaylkl lflkkys
//
LOCUS       NP_112365                196 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL19 [Rattus norvegicus].
ACCESSION   NP_112365
VERSION     NP_112365.1
DBSOURCE    REFSEQ: accession NM_031103.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Sugihara,Y., Sadohara,E., Yonezawa,K., Kugo,M., Oshima,K.,
            Matsuda,T. and Nadano,D.
  TITLE     Identification and expression of an autosomal paralogue of
            ribosomal protein S4, X-linked, in mice: potential involvement of
            testis-specific ribosomal proteins in translation and
            spermatogenesis
  JOURNAL   Gene 521 (1), 91-99 (2013)
   PUBMED   23500592
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Davies,B., Feo,S., Heard,E. and Fried,M.
  TITLE     A strategy to detect and isolate an intron-containing gene in the
            presence of multiple processed pseudogenes
  JOURNAL   Proc Natl Acad Sci U S A 86 (17), 6691-6695 (1989)
   PUBMED   2771953
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Chan,Y.L., Lin,A., McNally,J., Peleg,D., Meyuhas,O. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L19. A determination
            from the sequence of nucleotides in a cDNA and from the sequence of
            amino acids in the protein
  JOURNAL   J Biol Chem 262 (3), 1111-1115 (1987)
   PUBMED   3542997
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Buisson,M. and Reboud,A.M.
  TITLE     Carbodiimide-induced protein--RNA crosslinking in mammalian
            ribosomal subunits
  JOURNAL   FEBS Lett 148 (2), 247-250 (1982)
   PUBMED   6759166
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Faliks,D. and Meyuhas,O.
  TITLE     Coordinate regulation of ribosomal protein mRNA level in
            regenerating rat liver. Study with the corresponding mouse cloned
            cDNAs
  JOURNAL   Nucleic Acids Res 10 (3), 789-801 (1982)
   PUBMED   6121318
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Ulbrich,N., Lin,A. and Wool,I.G.
  TITLE     Identification by affinity chromatography of the eukaryotic
            ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid
  JOURNAL   J Biol Chem 254 (17), 8641-8645 (1979)
   PUBMED   468846
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X82202.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF110514.1, FQ222282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..196
                     /product="large ribosomal subunit protein eL19"
                     /EC_number="6.3.5.5"
                     /note="60S ribosomal protein L19; 60S ribosomal protein
                     L19-like"
                     /calculated_mol_wt=23335
     Region          4..167
                     /region_name="Ribosomal_L19e_E"
                     /note="Ribosomal protein L19e, eukaryotic. L19e is found
                     in the large ribosomal subunit of eukaryotes and archaea.
                     L19e is distinct from the ribosomal subunit L19, which is
                     found in prokaryotes. It consists of two small globular
                     domains connected by an...; cd01417"
                     /db_xref="CDD:238705"
     Site            order(4,8..9,18..24,26,29,38,42,53,55..60,62,64,66..67,
                     69..70,72,74..79,81..89,92,95..97,100..101,103,110,
                     117..118,120..121,124..126,129,131,134..135)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238705"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P84098; propagated from
                     UniProtKB/Swiss-Prot (P84100.1)"
     Site            28..47
                     /site_type="active"
                     /note="putative translocon docking site [active]"
                     /db_xref="CDD:238705"
     Site            order(112..113,115..119,139..149)
                     /site_type="active"
                     /note="putative intersubunit bridge [active]"
                     /db_xref="CDD:238705"
     Region          157..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84100.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P84098; propagated from
                     UniProtKB/Swiss-Prot (P84100.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P84098; propagated from
                     UniProtKB/Swiss-Prot (P84100.1)"
     CDS             1..196
                     /gene="Rpl19"
                     /coded_by="NM_031103.1:29..619"
                     /db_xref="GeneID:81767"
                     /db_xref="RGD:621183"
ORIGIN      
        1 msmlrlqkrl assvlrcgkk kvwldpnetn eianansrqq irklikdgli irkpvtvhsr
       61 arcrkntlar rkgrhmgigk rkgtanarmp ekvtwmrrmr ilrrllrryr eskkidrhmy
      121 hslylkvkgn vfknkrilme hihklkadka rkklladqae arrsktkear krreerlqak
      181 keeiiktlsk eeetkk
//
LOCUS       NP_001008387             447 aa            linear   ROD 27-APR-2025
DEFINITION  D-ribitol-5-phosphate cytidylyltransferase [Rattus norvegicus].
ACCESSION   NP_001008387
VERSION     NP_001008387.1
DBSOURCE    REFSEQ: accession NM_001008386.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Riemersma,M., Froese,D.S., van Tol,W., Engelke,U.F., Kopec,J., van
            Scherpenzeel,M., Ashikov,A., Krojer,T., von Delft,F., Tessari,M.,
            Buczkowska,A., Swiezewska,E., Jae,L.T., Brummelkamp,T.R., Manya,H.,
            Endo,T., van Bokhoven,H., Yue,W.W. and Lefeber,D.J.
  TITLE     Human ISPD Is a Cytidyltransferase Required for Dystroglycan
            O-Mannosylation
  JOURNAL   Chem Biol 22 (12), 1643-1652 (2015)
   PUBMED   26687144
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wright,K.M., Lyon,K.A., Leung,H., Leahy,D.J., Ma,L. and Ginty,D.D.
  TITLE     Dystroglycan organizes axon guidance cue localization and axonal
            pathfinding
  JOURNAL   Neuron 76 (5), 931-944 (2012)
   PUBMED   23217742
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Roscioli,T., Kamsteeg,E.J., Buysse,K., Maystadt,I., van
            Reeuwijk,J., van den Elzen,C., van Beusekom,E., Riemersma,M.,
            Pfundt,R., Vissers,L.E., Schraders,M., Altunoglu,U., Buckley,M.F.,
            Brunner,H.G., Grisart,B., Zhou,H., Veltman,J.A., Gilissen,C.,
            Mancini,G.M., Delree,P., Willemsen,M.A., Ramadza,D.P., Chitayat,D.,
            Bennett,C., Sheridan,E., Peeters,E.A., Tan-Sindhunata,G.M., de
            Die-Smulders,C.E., Devriendt,K., Kayserili,H., El-Hashash,O.A.,
            Stemple,D.L., Lefeber,D.J., Lin,Y.Y. and van Bokhoven,H.
  TITLE     Mutations in ISPD cause Walker-Warburg syndrome and defective
            glycosylation of alpha-dystroglycan
  JOURNAL   Nat Genet 44 (5), 581-585 (2012)
   PUBMED   22522421
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Willer,T., Lee,H., Lommel,M., Yoshida-Moriguchi,T., de
            Bernabe,D.B., Venzke,D., Cirak,S., Schachter,H., Vajsar,J.,
            Voit,T., Muntoni,F., Loder,A.S., Dobyns,W.B., Winder,T.L.,
            Strahl,S., Mathews,K.D., Nelson,S.F., Moore,S.A. and Campbell,K.P.
  TITLE     ISPD loss-of-function mutations disrupt dystroglycan
            O-mannosylation and cause Walker-Warburg syndrome
  JOURNAL   Nat Genet 44 (5), 575-580 (2012)
   PUBMED   22522420
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY769992.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY769992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132301
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16-q21"
     Protein         1..447
                     /product="D-ribitol-5-phosphate cytidylyltransferase"
                     /EC_number="2.7.7.40"
                     /note="2-C-methyl-D-erythritol 4-phosphate
                     cytidylyltransferase-like protein; isoprenoid synthase
                     domain-containing protein; notch1-induced protein;
                     isoprenoid synthase domain containing"
                     /calculated_mol_wt=49061
     Region          45..271
                     /region_name="CDP-ME_synthetase"
                     /note="CDP-ME synthetase is involved in
                     mevalonate-independent isoprenoid production; cd02516"
                     /db_xref="CDD:133009"
     Site            order(50,52..57,64,121..124,127,154..156,261)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133009"
     Site            57
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (Q5S6T3.1)"
     Site            64
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (Q5S6T3.1)"
     Site            order(157,176,184,186,204..209,236..237,239..240,243,
                     249..252,256..257)
                     /site_type="active"
                     /note="dimer interface [active]"
                     /db_xref="CDD:133009"
     Site            203
                     /site_type="other"
                     /note="Positions substrate for the nucleophilic attack.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (Q5S6T3.1)"
     Site            261
                     /site_type="other"
                     /note="Positions substrate for the nucleophilic attack.
                     /evidence=ECO:0000250|UniProtKB:Q46893; propagated from
                     UniProtKB/Swiss-Prot (Q5S6T3.1)"
     Region          281..447
                     /region_name="ISPD_C"
                     /note="D-ribitol-5-phosphate cytidylyltransferase
                     C-terminal domain; pfam18706"
                     /db_xref="CDD:465843"
     CDS             1..447
                     /gene="Crppa"
                     /gene_synonym="Ispd; Nip"
                     /coded_by="NM_001008386.1:93..1436"
                     /db_xref="GeneID:493574"
                     /db_xref="RGD:1359368"
ORIGIN      
        1 mesgpcsrpa eprhcvsgra gaglafpafp lsaagaepgs rigtvaavlp aggcgermgv
       61 rtpkqfcrvl erplisytlq amervcwikd ivvtvtgenm eamrsiiqry ghkrislaea
      121 gatrhrsifn glkalaedqp gceltrpevv iihdavrpfv eedillrvvl aakehgaaga
      181 irplvstvvs psadghldhs ldrakhrase mpqafhfdvi yeayqkcsdf dlefgteclq
      241 lalkychrka klvegtpdlw kvtykqdlca aeamikekis qeicvvvntk deesvghlle
      301 evlrnelnci kvtstvldrt sgdienfidq cysficvnvv ssesretrkl lsileesslp
      361 llypvvvvlv hcfdftvvpl aqkmenlvwi relakeakgr nvllsgvlln hsqdeqklqe
      421 slvqsaaiia alvkernsal vgqllva
//
LOCUS       NP_001019538             461 aa            linear   ROD 27-APR-2025
DEFINITION  armadillo repeat-containing X-linked protein 1 [Rattus norvegicus].
ACCESSION   NP_001019538 XP_577018
VERSION     NP_001019538.1
DBSOURCE    REFSEQ: accession NM_001024367.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085780.1.
            
            On May 27, 2005 this sequence version replaced XP_577018.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085780.1, CK480596.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..461
                     /product="armadillo repeat-containing X-linked protein 1"
                     /calculated_mol_wt=50918
     Region          1..6
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          26..36
                     /region_name="Mitochondrion outer membrane (MOM)-targeting
                     sequence. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          34..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          148..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          203..243
                     /region_name="ARM 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          210..430
                     /region_name="Arm_2"
                     /note="Armadillo-like; pfam04826"
                     /db_xref="CDD:461447"
     Region          245..284
                     /region_name="ARM 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          366..406
                     /region_name="ARM 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     Region          423..461
                     /region_name="ARM 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U310.1)"
     CDS             1..461
                     /gene="Armcx1"
                     /coded_by="NM_001024367.1:351..1736"
                     /db_xref="GeneID:501619"
                     /db_xref="RGD:1561629"
ORIGIN      
        1 mgrtreagcv aagmvigaga cycvyrltwg kdeneklwdd edeeeeeeee scsgkpeigg
       61 ktvkerkthv gvgagakpqd dskskaeanv gpengpdvkk evypeshseg gleakakalf
      121 kslkeqasak agrgirfpni srirtltssl pcpggrgggc hpgrtgsrar nrtsgkvkrk
      181 nrsksnkapa tawpvrrgkf sfpykiddil sapdlqkvln ilertndpft qevalvtlgn
      241 naaysfnqna irelggvpii akliktrdpi irektynaln nlsvnsenqg kiktyisqvc
      301 ddtmvcrlds avqmaglrll tnmtvtnhyq hllsysfpdf fallflgnhf tkiqtmklii
      361 nftenpamtr elvsckvpse lislfnkewd reillniltl fenindniks eglassrkef
      421 srsslfflfk esgvcvkkik alashkdlvv kvkvlkvltk l
//
LOCUS       NP_001012235             317 aa            linear   ROD 27-APR-2025
DEFINITION  protein IMPACT [Rattus norvegicus].
ACCESSION   NP_001012235
VERSION     NP_001012235.1
DBSOURCE    REFSEQ: accession NM_001012235.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cambiaghi,T.D., Pereira,C.M., Shanmugam,R., Bolech,M., Wek,R.C.,
            Sattlegger,E. and Castilho,B.A.
  TITLE     Evolutionarily conserved IMPACT impairs various stress responses
            that require GCN1 for activating the eIF2 kinase GCN2
  JOURNAL   Biochem Biophys Res Commun 443 (2), 592-597 (2014)
   PUBMED   24333428
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Roffe,M., Hajj,G.N., Azevedo,H.F., Alves,V.S. and Castilho,B.A.
  TITLE     IMPACT is a developmentally regulated protein in neurons that
            opposes the eukaryotic initiation factor 2alpha kinase GCN2 in the
            modulation of neurite outgrowth
  JOURNAL   J Biol Chem 288 (15), 10860-10869 (2013)
   PUBMED   23447528
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Waller,T., Lee,S.J. and Sattlegger,E.
  TITLE     Evidence that Yih1 resides in a complex with ribosomes
  JOURNAL   FEBS J 279 (10), 1761-1776 (2012)
   PUBMED   22404850
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Pereira,C.M., Sattlegger,E., Jiang,H.Y., Longo,B.M., Jaqueta,C.B.,
            Hinnebusch,A.G., Wek,R.C., Mello,L.E. and Castilho,B.A.
  TITLE     IMPACT, a protein preferentially expressed in the mouse brain,
            binds GCN1 and inhibits GCN2 activation
  JOURNAL   J Biol Chem 280 (31), 28316-28323 (2005)
   PUBMED   15937339
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Okamura,K., Sakaki,Y. and Ito,T.
  TITLE     Comparative genomics approach toward critical determinants for the
            imprinting of an evolutionarily conserved gene Impact
  JOURNAL   Biochem Biophys Res Commun 329 (3), 824-830 (2005)
   PUBMED   15752730
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY574213.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY574213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..317
                     /product="protein IMPACT"
                     /note="imprinted and ancient gene protein homolog"
                     /calculated_mol_wt=35864
     Region          13..113
                     /region_name="RWD_IMPACT"
                     /note="RWD domain of protein IMPACT and related proteins;
                     cd23821"
                     /db_xref="CDD:467657"
     Region          117..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GFD9.1)"
     Region          180..287
                     /region_name="UPF0029"
                     /note="Uncharacterized protein family UPF0029; pfam01205"
                     /db_xref="CDD:460111"
     Region          295..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GFD9.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5GFD9.1)"
     CDS             1..317
                     /gene="Impact"
                     /coded_by="NM_001012235.1:87..1040"
                     /db_xref="GeneID:497198"
                     /db_xref="RGD:1591977"
ORIGIN      
        1 maevesgsnq rqneeieama aiygeewcvi devakifcir itddmddpkw tlclqvmlps
       61 eypgtappvy qlnapwlkgq eraelaksle eiymkniges ilyqwvekir daliqksqit
      121 epgpdekkkt eeeevegedd pilehppenp vktwdlkise sapeaeelpp iahgapitdr
      181 rstfqahlap vvcidqvkkv laklyenkki asathniyay riycedkqtf lqdseddget
      241 aaggrllhlm eilnvknvmv vvsrwyggil lgpdrfkhin ncarnilvek nftnspeesa
      301 ksfgkkkvkk dkkkgdh
//
LOCUS       NP_001101129            1074 aa            linear   ROD 27-APR-2025
DEFINITION  semaphorin-5A precursor [Rattus norvegicus].
ACCESSION   NP_001101129 XP_001066339 XP_241275
VERSION     NP_001101129.1
DBSOURCE    REFSEQ: accession NM_001107659.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Matsuoka,R.L., Chivatakarn,O., Badea,T.C., Samuels,I.S., Cahill,H.,
            Katayama,K., Kumar,S.R., Suto,F., Chedotal,A., Peachey,N.S.,
            Nathans,J., Yoshida,Y., Giger,R.J. and Kolodkin,A.L.
  TITLE     Class 5 transmembrane semaphorins control selective Mammalian
            retinal lamination and function
  JOURNAL   Neuron 71 (3), 460-473 (2011)
   PUBMED   21835343
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Sadanandam,A., Rosenbaugh,E.G., Singh,S., Varney,M. and Singh,R.K.
  TITLE     Semaphorin 5A promotes angiogenesis by increasing endothelial cell
            proliferation, migration, and decreasing apoptosis
  JOURNAL   Microvasc Res 79 (1), 1-9 (2010)
   PUBMED   19850054
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Pineda,D., Garcia,B., Olmos,J.L., Davila,J.C., Real,M.A. and
            Guirado,S.
  TITLE     Semaphorin5A expression in the developing chick telencephalon
  JOURNAL   Brain Res Bull 66 (4-6), 436-440 (2005)
   PUBMED   16144627
  REMARK    GeneRIF: Semaphorin5A expression in the developing chick
            telencephalon.
REFERENCE   4  (residues 1 to 1074)
  AUTHORS   Fiore,R., Rahim,B., Christoffels,V.M., Moorman,A.F. and
            Puschel,A.W.
  TITLE     Inactivation of the Sema5a gene results in embryonic lethality and
            defective remodeling of the cranial vascular system
  JOURNAL   Mol Cell Biol 25 (6), 2310-2319 (2005)
   PUBMED   15743826
  REMARK    Erratum:[Mol Cell Biol. 2020 Sep 28;40(20):e00409-20. doi:
            10.1128/MCB.00409-20. PMID: 32989048]
REFERENCE   5  (residues 1 to 1074)
  AUTHORS   Kantor,D.B., Chivatakarn,O., Peer,K.L., Oster,S.F., Inatani,M.,
            Hansen,M.J., Flanagan,J.G., Yamaguchi,Y., Sretavan,D.W., Giger,R.J.
            and Kolodkin,A.L.
  TITLE     Semaphorin 5A is a bifunctional axon guidance cue regulated by
            heparan and chondroitin sulfate proteoglycans
  JOURNAL   Neuron 44 (6), 961-975 (2004)
   PUBMED   15603739
REFERENCE   6  (residues 1 to 1074)
  AUTHORS   Artigiani,S., Conrotto,P., Fazzari,P., Gilestro,G.F., Barberis,D.,
            Giordano,S., Comoglio,P.M. and Tamagnone,L.
  TITLE     Plexin-B3 is a functional receptor for semaphorin 5A
  JOURNAL   EMBO Rep 5 (7), 710-714 (2004)
   PUBMED   15218527
REFERENCE   7  (residues 1 to 1074)
  AUTHORS   Oster,S.F., Bodeker,M.O., He,F. and Sretavan,D.W.
  TITLE     Invariant Sema5A inhibition serves an ensheathing function during
            optic nerve development
  JOURNAL   Development 130 (4), 775-784 (2003)
   PUBMED   12506007
REFERENCE   8  (residues 1 to 1074)
  AUTHORS   Simmons,A.D., Puschel,A.W., McPherson,J.D., Overhauser,J. and
            Lovett,M.
  TITLE     Molecular cloning and mapping of human semaphorin F from the
            Cri-du-chat candidate interval
  JOURNAL   Biochem Biophys Res Commun 242 (3), 685-691 (1998)
   PUBMED   9464278
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001066339.1, XP_241275.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.7448.1,
                                           SRR26360190.1357902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..1074
                     /product="semaphorin-5A precursor"
                     /note="sema F; semaphorin-F; sema domain, seven
                     thrombospondin repeats (type 1 and type 1-like),
                     transmembrane domain (TM) and short cytoplasmic domain,
                     (semaphorin) 5A"
                     /calculated_mol_wt=117921
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2476
     mat_peptide     23..1074
                     /product="Semaphorin-5A. /evidence=ECO:0000255.
                     /id=PRO_0000420236"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTD8.1)"
                     /calculated_mol_wt=117921
     Region          50..485
                     /region_name="Sema_5A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 5A (Sema5A); cd11263"
                     /db_xref="CDD:200524"
     Site            order(105..108,158..159,163,185,187..188,195,205,208..209,
                     211,216,238,261..265,267,370,374,377)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200524"
     Site            147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            order(239..241,244..246,280,284..286,288,290,309..311,
                     315..316,383,398)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200524"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Region          486..533
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            536
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Region          544..595
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Region          598..651
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          656..702
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            717
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Region          787..839
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Region          853..896
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            898
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Region          899..940
                     /region_name="TSP1"
                     /note="Thrombospondin type 1 repeats; smart00209"
                     /db_xref="CDD:214559"
     Site            933
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            969..989
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTD8.1)"
     Site            1015
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTD8.1)"
     CDS             1..1074
                     /gene="Sema5a"
                     /coded_by="NM_001107659.2:667..3891"
                     /db_xref="GeneID:310207"
                     /db_xref="RGD:1308650"
ORIGIN      
        1 mkgacilawl fsslgvwrla rpetqdpakc qraehpvvsy keigpwlref raenavdfsr
       61 ltfdpgqkel vvgarnylfr lqledlsliq avqwecdeat kkacyskgks keecqnyirv
      121 llvggdrlft cgtnaftpvc tirslsnlte ihdqisgmar cpyspqhnst alltasgely
      181 aatamdfpgr dpaiyrslgt lpplrtaqyn skwlnepnfv ssydignfty fffrenaveh
      241 dcgktvfsra arvckndigg rflledtwtt fmkarlncsr pgevpfyyne lqstfflpel
      301 dliygifttn vnsiaasavc vfnlsaisqa fngpfkyqen srsawlpypn pnpnfqcgtm
      361 dqglyvnlte rnlqdaqkfi lmhevvqpvt tvpsfmedns rfshvavdvv qgrdtlvhii
      421 ylatdygtik kvraplsqss gsclleeiel fperksepir slkilhsqsv lfvglqehvv
      481 kiplkrchfh qtrgacigaq dpycgwdavm kkctsleesl smtqwdqsvp tcptrnltvd
      541 gsfgpwspwt pcthtdgtav gsclcrsrsc dspapqcggw qcegprmeit ncsrnggwtp
      601 wtswspcstt cgigfqvrqr scsnptprhg grvcvgqnre erycnehllc pphvfwtgwg
      661 pwerctaqcg ggiqarrrtc engpdcagcn veyqpcntna cpelkkttpw tpwtpvnisd
      721 ngghyeqrfr ytckarlpdp nllevgrqri emrycssdgt sgcstdglsg dflragrysa
      781 htvngawsaw tswsqcsrdc srgirnrkrv cnnpepkygg mpclgpslef qecnilpcpv
      841 dgvwscwssw skcsatcggg hymrtrsctn papayggdic lglhteealc ntqtcpenws
      901 ewsewsvcda sgtqvrtrqc illfpvgsqc sgnttesrpc vfdsnfipev svarsssvee
      961 krcgefnmfh mmavglsssi lgclltllvy tycqryqqqs hdatvihpvs paalnssitn
     1021 hinkldkyds veaikafnkn nlileernky fnphltgkty snayftdlnn ydey
//
LOCUS       NP_620816                431 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-11 receptor subunit alpha precursor [Rattus
            norvegicus].
ACCESSION   NP_620816
VERSION     NP_620816.1
DBSOURCE    REFSEQ: accession NM_139116.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Zuo,D., Zheng,Q., Xiao,M., Wang,X., Chen,H., Xu,J., Zhang,Q.,
            Xiong,Y., Ye,L. and Feng,Z.
  TITLE     Anti-apoptosis effect of recombinant human interleukin-11 in
            neonatal hypoxic-ischemic rats through activating the
            IL-11Ralpha/STAT3 signaling pathway
  JOURNAL   J Stroke Cerebrovasc Dis 32 (2), 106923 (2023)
   PUBMED   36521373
  REMARK    GeneRIF: Anti-apoptosis effect of recombinant human interleukin-11
            in neonatal hypoxic-ischemic rats through activating the
            IL-11Ralpha/STAT3 signaling pathway.
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Nieminen,P., Morgan,N.V., Fenwick,A.L., Parmanen,S., Veistinen,L.,
            Mikkola,M.L., van der Spek,P.J., Giraud,A., Judd,L., Arte,S.,
            Brueton,L.A., Wall,S.A., Mathijssen,I.M., Maher,E.R., Wilkie,A.O.,
            Kreiborg,S. and Thesleff,I.
  TITLE     Inactivation of IL11 signaling causes craniosynostosis, delayed
            tooth eruption, and supernumerary teeth
  JOURNAL   Am J Hum Genet 89 (1), 67-81 (2011)
   PUBMED   21741611
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Ain,R., Trinh,M.L. and Soares,M.J.
  TITLE     Interleukin-11 signaling is required for the differentiation of
            natural killer cells at the maternal-fetal interface
  JOURNAL   Dev Dyn 231 (4), 700-708 (2004)
   PUBMED   15499555
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Kiessling,S., Muller-Newen,G., Leeb,S.N., Hausmann,M., Rath,H.C.,
            Strater,J., Spottl,T., Schlottmann,K., Grossmann,J.,
            Montero-Julian,F.A., Scholmerich,J., Andus,T., Buschauer,A.,
            Heinrich,P.C. and Rogler,G.
  TITLE     Functional expression of the interleukin-11 receptor alpha-chain
            and evidence of antiapoptotic effects in human colonic epithelial
            cells
  JOURNAL   J Biol Chem 279 (11), 10304-10315 (2004)
   PUBMED   14701802
  REMARK    GeneRIF: IL11RA has a role in apoptosis
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Li,R., Hartley,L. and Robb,L.
  TITLE     Cloning of rat interleukin 11 and interleukin 11 receptor alpha
            chain and analysis of their expression in rat uterus in the
            peri-implantation period
  JOURNAL   Reproduction 122 (4), 593-600 (2001)
   PUBMED   11570967
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Bilinski,P., Roopenian,D. and Gossler,A.
  TITLE     Maternal IL-11Ralpha function is required for normal decidua and
            fetoplacental development in mice
  JOURNAL   Genes Dev 12 (14), 2234-2243 (1998)
   PUBMED   9679067
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Robb,L., Li,R., Hartley,L., Nandurkar,H.H., Koentgen,F. and
            Begley,C.G.
  TITLE     Infertility in female mice lacking the receptor for interleukin 11
            is due to a defective uterine response to implantation
  JOURNAL   Nat Med 4 (3), 303-308 (1998)
   PUBMED   9500603
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Hilton,D.J., Hilton,A.A., Raicevic,A., Rakar,S., Harrison-Smith,M.,
            Gough,N.M., Begley,C.G., Metcalf,D., Nicola,N.A. and Willson,T.A.
  TITLE     Cloning of a murine IL-11 receptor alpha-chain; requirement for
            gp130 for high affinity binding and signal transduction
  JOURNAL   EMBO J 13 (20), 4765-4775 (1994)
   PUBMED   7957045
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF347936.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF347936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..431
                     /product="interleukin-11 receptor subunit alpha precursor"
                     /note="interleukin-11 receptor alpha chain; interleukin 11
                     receptor, alpha chain 1; interleukin-11 receptor subunit
                     alpha; IL-11RA; IL-11R-alpha; IL-11R subunit alpha; IL-11
                     receptor subunit alpha"
                     /calculated_mol_wt=44523
     sig_peptide     1..23
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q99MF4.1)"
                     /calculated_mol_wt=2280
     mat_peptide     24..431
                     /product="Interleukin-11 receptor subunit alpha.
                     /id=PRO_0000010916"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
                     /calculated_mol_wt=44523
     Region          33..95
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          44..48
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          56..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          77..81
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..97
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          102..105
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          111..202
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MF4.1)"
     Region          151..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MF4.1)"
     Region          218..310
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(218,285,303)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          304..308
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
     Site            order(304..305,307..308)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          310..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
     Site            372..392
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
     Region          402..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MF4.1)"
     CDS             1..431
                     /gene="Il11ra1"
                     /coded_by="NM_139116.1:57..1352"
                     /db_xref="GeneID:245983"
                     /db_xref="RGD:621332"
ORIGIN      
        1 msssrsgltr vlvavatalv ssstpcpqaw gppgvqygqp grpvmlccpg vnagtpvswf
       61 rdgdsrllqg pdsglghrlv laqvdsrdeg tyvcrtldgv fggmvtlklg spparpevsc
      121 qavdyenfsc twspgrvsgl ptryltsyrk ktlpgaesqr espstgpwpc pqdpleasrc
      181 vvhgaefwse yrinvtevnp lgastclldv rlqrilrpdp pqglrvesvp gyprrlhasw
      241 typaswrrqp hfllkfrlqy rpaqhpawst vepigleeli tdavaglpha vrvsardfld
      301 agtwsawspe awgtpstgpl rdevpdgsrg heqkleaaaq edspappsps lqpdprpldh
      361 rdpleqvavl aslgifsflg lavgalalgl wlrlrrsgkd gpqkpgflap mipgdklpgi
      421 pnlqrtpenf s
//
LOCUS       NP_001100894             515 aa            linear   ROD 27-APR-2025
DEFINITION  Y+L amino acid transporter 2 [Rattus norvegicus].
ACCESSION   NP_001100894 XP_001074601 XP_226422
VERSION     NP_001100894.1
DBSOURCE    REFSEQ: accession NM_001107424.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zielinska,M., Milewski,K., Skowronska,M., Gajos,A., Zieminska,E.,
            Beresewicz,A. and Albrecht,J.
  TITLE     Induction of inducible nitric oxide synthase expression in
            ammonia-exposed cultured astrocytes is coupled to increased
            arginine transport by upregulated y(+)LAT2 transporter
  JOURNAL   J Neurochem 135 (6), 1272-1281 (2015)
   PUBMED   26448619
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Zielinska,M., Skowronska,M., Fresko,I. and Albrecht,J.
  TITLE     Upregulation of the heteromeric yLAT2 transporter contributes to
            ammonia-induced increase of arginine uptake in rat cerebral
            cortical astrocytes
  JOURNAL   Neurochem Int 61 (4), 531-535 (2012)
   PUBMED   22401943
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kaneko,S., Ando,A., Okuda-Ashitaka,E., Maeda,M., Furuta,K.,
            Suzuki,M., Matsumura,M. and Ito,S.
  TITLE     Ornithine transport via cationic amino acid transporter-1 is
            involved in ornithine cytotoxicity in retinal pigment epithelial
            cells
  JOURNAL   Invest Ophthalmol Vis Sci 48 (1), 464-471 (2007)
   PUBMED   17197568
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001074601.1, XP_226422.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132263 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..515
                     /product="Y+L amino acid transporter 2"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 6; solute carrier family 7
                     (amino acid transporter light chain, y+L system), member
                     6; y(+)L-type amino acid transporter 2"
                     /calculated_mol_wt=56684
     Region          17..501
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            267..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            312..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            425..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     Site            452..472
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZMM8.1)"
     CDS             1..515
                     /gene="Slc7a6"
                     /gene_synonym="y+LAT-2; Y+LAT2"
                     /coded_by="NM_001107424.1:37..1584"
                     /db_xref="GeneID:307811"
                     /db_xref="RGD:1309193"
ORIGIN      
        1 mearelgspt ptyhllpkan qhtvkedass psqgspetmq lkkeisllng vslvvgnmig
       61 sgifvspkgv lkytasygls lvvwaigglf svvgalcyae lgttitksga syayileafg
      121 gfiafirlwv slliveptsq aiiaitfany iikpsfptcd ppyvacrlla aacvclltfv
      181 ncayvkwgtr vqdtftyakv laliaiiimg lvklcqghte hfqdafkgss wnvgdlslal
      241 ysalfsysgw dtlnfvteei knpernlpla igismpivtl iyiltnvayy tvlniqdvhk
      301 sdavavtfad qtfgmfswti piavalscfg glnasifass rlffvgsreg hlpnllsmih
      361 ierftpvpal lfnctmtliy lvvkdvflli nyfsfsywff vglsvvgqly lrwkepdwpr
      421 plklslffpi vfcicslflv avplfsdtin sligigials gvpvyfmgvy lpearrplfi
      481 rkvlatvtrv tqklcfcvlt eldvaeeknv erktd
//
LOCUS       NP_071570                539 aa            linear   ROD 27-APR-2025
DEFINITION  acid-sensing ion channel 4 [Rattus norvegicus].
ACCESSION   NP_071570
VERSION     NP_071570.2
DBSOURCE    REFSEQ: accession NM_022234.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Lin,S.H., Chien,Y.C., Chiang,W.W., Liu,Y.Z., Lien,C.C. and
            Chen,C.C.
  TITLE     Genetic mapping of ASIC4 and contrasting phenotype to ASIC1a in
            modulating innate fear and anxiety
  JOURNAL   Eur J Neurosci 41 (12), 1553-1568 (2015)
   PUBMED   25828470
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Andrey,F., Tsintsadze,T., Volkova,T., Lozovaya,N. and Krishtal,O.
  TITLE     Acid sensing ionic channels: modulation by redox reagents
  JOURNAL   Biochim Biophys Acta 1745 (1), 1-6 (2005)
   PUBMED   16085050
  REMARK    GeneRIF: Acid-sensing ion channel currents are susceptible to
            regulation by redox agents. (Acid-sensing ion channels)
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Akopian,A.N., Chen,C.C., Ding,Y., Cesare,P. and Wood,J.N.
  TITLE     A new member of the acid-sensing ion channel family
  JOURNAL   Neuroreport 11 (10), 2217-2222 (2000)
   PUBMED   10923674
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Grunder,S., Geissler,H.S., Bassler,E.L. and Ruppersberg,J.P.
  TITLE     A new member of acid-sensing ion channels from pituitary gland
  JOURNAL   Neuroreport 11 (8), 1607-1611 (2000)
   PUBMED   10852210
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB703338.1, AJ271642.1 and AJ242554.1.
            
            On Dec 19, 2006 this sequence version replaced NP_071570.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ271642.1, AJ242554.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..539
                     /product="acid-sensing ion channel 4"
                     /note="spinal chord ASIC; putative acid-sensing ion
                     channel; amiloride-sensitive cation channel 4, pituitary;
                     acid-sensing (proton-gated) ion channel family member 4;
                     acid sensing ion channel 4; spinal cord ASIC"
                     /calculated_mol_wt=59195
     Region          40..488
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Site            243
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Site            439..459
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Region          452..454
                     /region_name="GAS motif, ion selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P78348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS6.1)"
     Region          501..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHS6.1)"
     CDS             1..539
                     /gene="Asic4"
                     /gene_synonym="Accn4; Spasic"
                     /coded_by="NM_022234.2:312..1931"
                     /db_xref="GeneID:63882"
                     /db_xref="RGD:621068"
ORIGIN      
        1 mpieivckik faeedakpke keagdeqsll gaaqgpaapr dlatfastst lhglgracgp
       61 gphglrrtlw vlalltslaa flyqaaslar gyltrphlva mdpaapapva gfpavtlcni
      121 nrfrhsalsd adifhlanlt glppkdrdgh raaglrypep dmvdilnrtg hqladmlksc
      181 nfsghhcsas nfsvvytryg kcytfnadpq sslpsraggm gsgleimldi qqeeylpiwr
      241 etnetsfeag irvqihsqee ppyihqlgfg vspgfqtfvs cqeqrltylp qpwgncraes
      301 klrepelqgy saysvsacrl rcekeavlqr chcrmvhmpg neticppniy iecadhtlds
      361 lgggsegpcf cptpcnltry gkeismvkip nrgsarylar kynrnetyir enflvldvff
      421 ealtseameq raayglsall gdlggqmglf igasiltlle ildyiyevsw drlkrvwrrp
      481 ktplrtstgg istlglqelk eqspcpnrgr aegggasnll pnhhhphgpp gslfedfac
//
LOCUS       NP_001014071             688 aa            linear   ROD 27-APR-2025
DEFINITION  protein sel-1 homolog 2 precursor [Rattus norvegicus].
ACCESSION   NP_001014071 XP_230648
VERSION     NP_001014071.1
DBSOURCE    REFSEQ: accession NM_001014049.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083893.1.
            
            On Apr 20, 2005 this sequence version replaced XP_230648.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083893.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..688
                     /product="protein sel-1 homolog 2 precursor"
                     /note="protein sel-1 homolog 2; sel-1L2; suppressor of
                     lin-12-like protein 2; sel-1 suppressor of lin-12-like 2;
                     SEL1L2 ERAD E3 ligase adaptor subunit; SEL1L2 adaptor
                     subunit of ERAD E3 ligase; SEL1L2 adaptor subunit of ERAD
                     E3 ubiquitin ligase"
                     /calculated_mol_wt=75854
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI05.1)"
                     /calculated_mol_wt=1996
     mat_peptide     19..688
                     /product="Protein sel-1 homolog 2. /id=PRO_0000305161"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
                     /calculated_mol_wt=75854
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          88..119
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          107..142
                     /region_name="Sel1-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          <124..331
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          126..155
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          143..178
                     /region_name="Sel1-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          162..191
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          179..214
                     /region_name="Sel1-like 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          198..227
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          215..250
                     /region_name="Sel1-like 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          282..476
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          297..333
                     /region_name="Sel1-like 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          317..346
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          334..370
                     /region_name="Sel1-like 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          354..383
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          371..406
                     /region_name="Sel1-like 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          390..419
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          407..442
                     /region_name="Sel1-like 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          443..478
                     /region_name="Sel1-like 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          494..523
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          531..>620
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          534..563
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          551..586
                     /region_name="Sel1-like 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          570..600
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          588..623
                     /region_name="Sel1-like 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     Region          588..620
                     /region_name="SEL1"
                     /note="Sel1-like repeats; smart00671"
                     /db_xref="CDD:214772"
     Site            663..683
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI05.1)"
     CDS             1..688
                     /gene="Sel1l2"
                     /gene_synonym="RGD1311278"
                     /coded_by="NM_001014049.1:73..2139"
                     /db_xref="GeneID:311470"
                     /db_xref="RGD:1311278"
ORIGIN      
        1 mnplallvei liiievttkn seaerynrkq kevnvttqvs vskvkqflsh lleqgkanki
       61 ankrenplek kkhqhklkik giqnknllkr nqnyfkkpak ksitdkgdel fkmgnkilqe
      121 sksqkqktea ytfftraadm gnlkamekma dallfgsfgm qnitaaiqly eslakegsyk
      181 aqnalgflss ygigmeydqa kaliyytfgs aggsmmsqmi lgyrylsgin vlqncevaln
      241 hykkvadyia dkleksegip vekvrlterp enlssnseil dwdiyqyykf laergdvqiq
      301 vslgqlhlig rkgldqdysk alyyflkaak agsanamafi gkmylegnaa apqnnatafk
      361 yfsmaaskgn aiglhglgll yfhgkgvpvn ygealkyfqk aaekgwpnaq fhlgfmyysg
      421 sgvwkdykla fkyfylasqs gqplaiyyla emyatgtgvl rscrtavepy kgvcelghwa
      481 ekfltayfay kdgdvdssli qyallaemgy evaqsnsafi leskkakilg kekmypmall
      541 lwnraaiqgn afarvkigdy hyygygtkkd yetaathysi aadkhhsaqa mfnlaymyeh
      601 glgiaqdihl arrlydmaaq tspdahipvf falmkletmh flqdilffnf ttkwkwlkld
      661 stigpywdll viglivvvli fllrnhhr
//
LOCUS       NP_113988                318 aa            linear   ROD 27-APR-2025
DEFINITION  death effector domain-containing protein [Rattus norvegicus].
ACCESSION   NP_113988
VERSION     NP_113988.1
DBSOURCE    REFSEQ: accession NM_031800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Mori,M., Kitazume,M., Ose,R., Kurokawa,J., Koga,K., Osuga,Y.,
            Arai,S. and Miyazaki,T.
  TITLE     Death effector domain-containing protein (DEDD) is required for
            uterine decidualization during early pregnancy in mice
  JOURNAL   J Clin Invest 121 (1), 318-327 (2011)
   PUBMED   21135503
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Leo,C.P., Hsu,S.Y., McGee,E.A., Salanova,M. and Hsueh,A.J.
  TITLE     DEFT, a novel death effector domain-containing molecule
            predominantly expressed in testicular germ cells
  JOURNAL   Endocrinology 139 (12), 4839-4848 (1998)
   PUBMED   9832420
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Stegh,A.H., Schickling,O., Ehret,A., Scaffidi,C., Peterhansel,C.,
            Hofmann,T.G., Grummt,I., Krammer,P.H. and Peter,M.E.
  TITLE     DEDD, a novel death effector domain-containing protein, targeted to
            the nucleolus
  JOURNAL   EMBO J 17 (20), 5974-5986 (1998)
   PUBMED   9774341
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF053362.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF053362.1, CO398364.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..318
                     /product="death effector domain-containing protein"
                     /note="death effector domain-containing testicular
                     molecule"
                     /calculated_mol_wt=36716
     Region          22..118
                     /region_name="DED_DEDD"
                     /note="Death Effector Domain of DEDD; cd08790"
                     /db_xref="CDD:260058"
     Region          128..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2K0.1)"
     CDS             1..318
                     /gene="Dedd"
                     /gene_synonym="Deft"
                     /coded_by="NM_031800.1:51..1007"
                     /db_xref="GeneID:83631"
                     /db_xref="RGD:620050"
ORIGIN      
        1 maglkrrasq vwpeerveqe hglyslhrmf divgthlthr dvrvlsflfv dviddhergl
       61 irngrdflla lerqgrcdes nfrqvlqllr iitrhdllpy vtlkkrravc pdlvdkylee
      121 tsiryvtpra lsdpeprppq psktvpphyp vvccptsgsq mcskrpargr ttlgsqrkrr
      181 ksvtpdpkek qtcdirlrvr aeycqhetal qgnvfsnkqd plerqferfn qantilksrd
      241 lgsiicdikf seltyldafw rdyingslle alkgvfitds lkqavgheai kllvnvdeed
      301 yelgrqkllr nlmlqalp
//
LOCUS       NP_955750                927 aa            linear   ROD 27-APR-2025
DEFINITION  dual serine/threonine and tyrosine protein kinase [Rattus
            norvegicus].
ACCESSION   NP_955750 XP_222647
VERSION     NP_955750.1
DBSOURCE    REFSEQ: accession NM_199463.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Lee,J.Y.W., Hsu,C.K., Michael,M., Nanda,A., Liu,L., McMillan,J.R.,
            Pourreyron,C., Takeichi,T., Tolar,J., Reid,E., Hayday,T.,
            Blumen,S.C., Abu-Mouch,S., Straussberg,R., Basel-Vanagaite,L.,
            Barhum,Y., Zouabi,Y., Al-Ajmi,H., Huang,H.Y., Lin,T.C., Akiyama,M.,
            Lee,J.Y.Y., McLean,W.H.I., Simpson,M.A., Parsons,M. and
            McGrath,J.A.
  TITLE     Large Intragenic Deletion in DSTYK Underlies Autosomal-Recessive
            Complicated Spastic Paraparesis, SPG23
  JOURNAL   Am J Hum Genet 100 (2), 364-370 (2017)
   PUBMED   28157540
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Sanna-Cherchi,S., Sampogna,R.V., Papeta,N., Burgess,K.E.,
            Nees,S.N., Perry,B.J., Choi,M., Bodria,M., Liu,Y., Weng,P.L.,
            Lozanovski,V.J., Verbitsky,M., Lugani,F., Sterken,R., Paragas,N.,
            Caridi,G., Carrea,A., Dagnino,M., Materna-Kiryluk,A.,
            Santamaria,G., Murtas,C., Ristoska-Bojkovska,N., Izzi,C., Kacak,N.,
            Bianco,B., Giberti,S., Gigante,M., Piaggio,G., Gesualdo,L.,
            Vukic,D.K., Vukojevic,K., Saraga-Babic,M., Saraga,M., Gucev,Z.,
            Allegri,L., Latos-Bielenska,A., Casu,D., State,M., Scolari,F.,
            Ravazzolo,R., Kiryluk,K., Al-Awqati,Q., D'Agati,V.D.,
            Drummond,I.A., Tasic,V., Lifton,R.P., Ghiggeri,G.M. and
            Gharavi,A.G.
  TITLE     Mutations in DSTYK and dominant urinary tract malformations
  JOURNAL   N Engl J Med 369 (7), 621-629 (2013)
   PUBMED   23862974
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Peng,J., Dong,W., Chen,Y., Mo,R., Cheng,J.F., Hui,C.C., Mohandas,N.
            and Huang,C.H.
  TITLE     Dusty protein kinases: primary structure, gene evolution, tissue
            specific expression and unique features of the catalytic domain
  JOURNAL   Biochim Biophys Acta 1759 (11-12), 562-572 (2006)
   PUBMED   17123648
REFERENCE   4  (residues 1 to 927)
  AUTHORS   Zha,J., Zhou,Q., Xu,L.G., Chen,D., Li,L., Zhai,Z. and Shu,H.B.
  TITLE     RIP5 is a RIP-homologous inducer of cell death
  JOURNAL   Biochem Biophys Res Commun 319 (2), 298-303 (2004)
   PUBMED   15178406
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY429675.1.
            
            On Jan 21, 2004 this sequence version replaced XP_222647.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY429675.1, AY208851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..927
                     /product="dual serine/threonine and tyrosine protein
                     kinase"
                     /EC_number="2.7.12.1"
                     /note="dusty PK; receptor-interacting
                     serine/threonine-protein kinase 5; receptor interacting
                     protein kinase 5; dusty protein kinase"
                     /calculated_mol_wt=104767
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XUX2.1)"
     Region          649..910
                     /region_name="PKc_Dusty"
                     /note="Catalytic domain of the Dual-specificity Protein
                     Kinase, Dusty; cd13975"
                     /db_xref="CDD:270877"
     Site            order(656..660,664,677,679,709,732..735,738,740,775,777,
                     779..780,782,793,796,809..812)
                     /site_type="active"
                     /db_xref="CDD:270877"
     Site            order(656..660,664,677,679,709,732..735,738,775,777,
                     779..780,782,793)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270877"
     Site            order(660,738,740,775,777,779,796,809..812)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270877"
     Site            792..812
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270877"
     CDS             1..927
                     /gene="Dstyk"
                     /gene_synonym="DustyPK; Ripk5"
                     /coded_by="NM_199463.2:70..2853"
                     /db_xref="GeneID:304791"
                     /db_xref="RGD:735051"
ORIGIN      
        1 meadgqswsg esvsgpgpgg ggmirelcrg fgryrrylgr lrqnlretqk ffrdikcshs
       61 hscpsspagg gaaelgpagd vaaaplpagq lscisfppme ekylqqivdh lpcililgqd
      121 cnakcqllnl llavrvlptl kldsdesckl rrlrftygtr tqvslalpgq yelvhtlash
      181 qdnwetipee dlevqedsed tarvladlev tmhhallqev divvapchsh rpavdvlsdl
      241 andflpvity alhkdelser deqelqeirk yfsfpvfffk vptleiirss sgradsersp
      301 lsgqlmdlgy lssshrncma sdqdcraqsm lveqseklrq lstfshqllq trlvdaakal
      361 navhshcldi finqafdmqr dlqitpkrle ytrkkenely eslmnianrk qeemkdmive
      421 tlntmkeell ddaanmefkd vivpengetv gtreikscir qiqeliisrl nqavanklis
      481 svdylresfv gtlerclqsl eksqdvsvhi tsnylkqiln aayhvevtfh sgssvtrmlw
      541 eqikqiiqri twvnpptitl ewkrkvaqea idslsaskla ksicsqfrtr lnssheafaa
      601 slrqleaghs grlektedlw lkvrkdhapr larlslesrs lqdvllhrkp klgqelgrgq
      661 ygvvylcdnw gghfpcalks vvppdekhwn dlalefhymr slpkherlvd lhgsvidyny
      721 gggssvavll imerlhrdly tglkaglsle trlqialdvv egirflhsqg lvhrdiklkn
      781 vlldkqnrak itdlgfckpe ammsgsivgt pihmapelft gkydnsvdvy afgilfwyic
      841 sgsiklpeaf ercaskdhlw nnvrrgtrpe rlpvfdeecw qlmeacwdgd pskrpllgiv
      901 qpilrsimdr lckcdserps rglddst
//
LOCUS       NP_001008362             349 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF167 precursor [Rattus norvegicus].
ACCESSION   NP_001008362 XP_340834
VERSION     NP_001008362.1
DBSOURCE    REFSEQ: accession NM_001008361.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Yamada,H.Y. and Gorbsky,G.J.
  TITLE     Tumor suppressor candidate TSSC5 is regulated by UbcH6 and a novel
            ubiquitin ligase RING105
  JOURNAL   Oncogene 25 (9), 1330-1339 (2006)
   PUBMED   16314844
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083670.1.
            
            On Dec 16, 2004 this sequence version replaced XP_340834.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083670.1, SRR8487227.279624.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..349
                     /product="E3 ubiquitin-protein ligase RNF167 precursor"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RNF167; RING-type E3
                     ubiquitin transferase RNF167"
                     /calculated_mol_wt=36090
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XIL0.1)"
                     /calculated_mol_wt=2145
     Region          20..170
                     /region_name="PA_C_RZF_like"
                     /note="PA_C-RZF_ like: Protease-associated (PA) domain
                     C_RZF-like. This group includes various PA
                     domain-containing proteins similar to C-RZF (chicken
                     embryo RING zinc finger) protein. These proteins contain a
                     C3H2C3 RING finger. C-RZF is expressed in embryo...;
                     cd02123"
                     /db_xref="CDD:239038"
     mat_peptide     22..349
                     /product="E3 ubiquitin-protein ligase RNF167.
                     /id=PRO_0000245595"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL0.1)"
                     /calculated_mol_wt=36090
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XIL0.1)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XIL0.1)"
     Site            120..122
                     /site_type="other"
                     /note="PA/protease or protease-like domain interface
                     [polypeptide binding]"
                     /db_xref="CDD:239038"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL0.1)"
     Region          221..277
                     /region_name="RING-H2_RNF13"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 13 (RNF13) and similar proteins; cd16796"
                     /db_xref="CDD:438450"
     Site            order(230,233,248,250,253,256,268,271)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438450"
     Region          271..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIL0.1)"
     CDS             1..349
                     /gene="Rnf167"
                     /gene_synonym="RGD1305972"
                     /coded_by="NM_001008361.1:613..1662"
                     /db_xref="GeneID:360554"
                     /db_xref="RGD:1305972"
ORIGIN      
        1 mhpaafplpv vvatvlwgaa pirglirats ehnasmdfad lpalfgatls deglqgflve
       61 ahpenacspi apppsapvng svfiallrrf dcnfdlkvln aqkagygaav vhnvnsnell
      121 nmvwnseeiq qqiwipsvfi gersaeylra lfvyekgarv llvpdnsfpl gyylipftgi
      181 vgllvlamgt vlivrciqhr krlqrnrltk eqlkqipthd yqkgdeydvc aicldeyedg
      241 dklrilpcah ayhsrcvdpw ltqtrktcpi ckqpvhrgpg deeqeeetqg qeeegdegep
      301 rdqpasewtp llgssptlpt sfgslapapl vfpgpstdps pspssaala
//
LOCUS       NP_997710                433 aa            linear   ROD 27-APR-2025
DEFINITION  keratin, type I cytoskeletal 17 [Rattus norvegicus].
ACCESSION   NP_997710 XP_213478
VERSION     NP_997710.1
DBSOURCE    REFSEQ: accession NM_212545.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Saunders,S.P., Goh,C.S., Brown,S.J., Palmer,C.N., Porter,R.M.,
            Cole,C., Campbell,L.E., Gierlinski,M., Barton,G.J., Schneider,G.,
            Balmain,A., Prescott,A.R., Weidinger,S., Baurecht,H., Kabesch,M.,
            Gieger,C., Lee,Y.A., Tavendale,R., Mukhopadhyay,S., Turner,S.W.,
            Madhok,V.B., Sullivan,F.M., Relton,C., Burn,J., Meggitt,S.,
            Smith,C.H., Allen,M.A., Barker,J.N., Reynolds,N.J., Cordell,H.J.,
            Irvine,A.D., McLean,W.H., Sandilands,A. and Fallon,P.G.
  TITLE     Tmem79/Matt is the matted mouse gene and is a predisposing gene for
            atopic dermatitis in human subjects
  JOURNAL   J Allergy Clin Immunol 132 (5), 1121-1129 (2013)
   PUBMED   24084074
  REMARK    Erratum:[J Allergy Clin Immunol. 2015 Dec;136(6):1710. doi:
            10.1016/j.jaci.2015.10.002. PMID: 28843836]
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Andl,T., Murchison,E.P., Liu,F., Zhang,Y., Yunta-Gonzalez,M.,
            Tobias,J.W., Andl,C.D., Seykora,J.T., Hannon,G.J. and Millar,S.E.
  TITLE     The miRNA-processing enzyme dicer is essential for the
            morphogenesis and maintenance of hair follicles
  JOURNAL   Curr Biol 16 (10), 1041-1049 (2006)
   PUBMED   16682203
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Kim,S., Wong,P. and Coulombe,P.A.
  TITLE     A keratin cytoskeletal protein regulates protein synthesis and
            epithelial cell growth
  JOURNAL   Nature 441 (7091), 362-365 (2006)
   PUBMED   16710422
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Tong,X. and Coulombe,P.A.
  TITLE     Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
            fashion
  JOURNAL   Genes Dev 20 (10), 1353-1364 (2006)
   PUBMED   16702408
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Shen,Z., Wang,G., Fan,J.Y., Li,W. and Liu,Y.F.
  TITLE     HLA DR B1*04, *07-restricted epitopes on Keratin 17 for
            autoreactive T cells in psoriasis
  JOURNAL   J Dermatol Sci 38 (1), 25-39 (2005)
   PUBMED   15795121
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Wong,P., Domergue,R. and Coulombe,P.A.
  TITLE     Overcoming functional redundancy to elicit pachyonychia
            congenita-like nail lesions in transgenic mice
  JOURNAL   Mol Cell Biol 25 (1), 197-205 (2005)
   PUBMED   15601842
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Hesse,M., Zimek,A., Weber,K. and Magin,T.M.
  TITLE     Comprehensive analysis of keratin gene clusters in humans and
            rodents
  JOURNAL   Eur J Cell Biol 83 (1), 19-26 (2004)
   PUBMED   15085952
REFERENCE   9  (residues 1 to 433)
  AUTHORS   McGowan,K.M., Tong,X., Colucci-Guyon,E., Langa,F., Babinet,C. and
            Coulombe,P.A.
  TITLE     Keratin 17 null mice exhibit age- and strain-dependent alopecia
  JOURNAL   Genes Dev 16 (11), 1412-1422 (2002)
   PUBMED   12050118
REFERENCE   10 (residues 1 to 433)
  AUTHORS   McLean,W.H., Rugg,E.L., Lunny,D.P., Morley,S.M., Lane,E.B.,
            Swensson,O., Dopping-Hepenstal,P.J., Griffiths,W.A., Eady,R.A.,
            Higgins,C. et al.
  TITLE     Keratin 16 and keratin 17 mutations cause pachyonychia congenita
  JOURNAL   Nat Genet 9 (3), 273-278 (1995)
   PUBMED   7539673
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100058.1.
            
            On Aug 30, 2004 this sequence version replaced XP_213478.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100058.1, BK004050.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132280,
                                           SAMD00132281 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..433
                     /product="keratin, type I cytoskeletal 17"
                     /note="K17; CK-17; cytokeratin-17; type I keratin KA17;
                     keratin 17, type I"
                     /calculated_mol_wt=47992
     Region          1..83
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61414; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          84..394
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          84..120
                     /region_name="Coil 1A. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          121..138
                     /region_name="Linker 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          139..230
                     /region_name="Coil 1B. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          231..250
                     /region_name="Linker 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          251..392
                     /region_name="Coil 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6IFV3; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04695; propagated from
                     UniProtKB/Swiss-Prot (Q6IFU8.1)"
     Region          393..433
                     /region_name="Tail. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IFU8.1)"
     CDS             1..433
                     /gene="Krt17"
                     /gene_synonym="Ka17"
                     /coded_by="NM_212545.2:54..1355"
                     /db_xref="GeneID:287702"
                     /db_xref="RGD:1303181"
ORIGIN      
        1 mtttirqfts sssikgssgl gggssrtscr lsgslgagsc rlgsasglgs alggnsyssc
       61 ysfgtgsgyg gnfggvdgll aggekatmqn lndrlasyld kvraleeant elevkirdwy
      121 qkqapgpard ysayyqtied lknkilvatv dnasillqid narlaaddfr tkfeteqalr
      181 msveadingl rrvldeltla radlemqien lkeelaylkk nheeemnalr gqvggeinve
      241 mdaapgvdls rilsemrdqy ekmaeknrkd aedwffskte elnrevatns elvqsgksei
      301 selrrtmqal eielqsqlsm kaslegslae tenrycvqls qiqgligsve eqlaqlrcem
      361 eqqnqeykil ldvktrleqe iatyrrlleg edahltqykp kepvttrqvr tiveevqdgk
      421 vissreqvhq ttr
//
LOCUS       NP_114023                512 aa            linear   ROD 27-APR-2025
DEFINITION  alanine--glyoxylate aminotransferase 2, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_114023
VERSION     NP_114023.1
DBSOURCE    REFSEQ: accession NM_031835.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Granot-Hershkovitz,E., Spitzer,B., Yang,Y., Tarraf,W., Yu,B.,
            Boerwinkle,E., Fornage,M., Mosley,T.H., DeCarli,C., Kristal,B.S.,
            Gonzalez,H.M. and Sofer,T.
  TITLE     Genetic loci of beta-aminoisobutyric acid are associated with
            aging-related mild cognitive impairment
  JOURNAL   Transl Psychiatry 13 (1), 140 (2023)
   PUBMED   37120436
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Wei,J., Zhang,J., Wei,J., Hu,M., Chen,X., Qin,X., Chen,J., Lei,F.
            and Qin,Y.
  TITLE     Identification of AGXT2, SHMT1, and ACO2 as important biomarkers of
            acute kidney injury by WGCNA
  JOURNAL   PLoS One 18 (2), e0281439 (2023)
   PUBMED   36735737
  REMARK    GeneRIF: Identification of AGXT2, SHMT1, and ACO2 as important
            biomarkers of acute kidney injury by WGCNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yoshino,Y., Kumon,H., Mori,T., Yoshida,T., Tachibana,A.,
            Shimizu,H., Iga,J.I. and Ueno,S.I.
  TITLE     Effects of AGXT2 variants on blood pressure and blood sugar among
            750 older Japanese subjects recruited by the complete enumeration
            survey method
  JOURNAL   BMC Genomics 22 (1), 287 (2021)
   PUBMED   33879046
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Amir,M., Hassanein,S.I., Abdel Rahman,M.F. and Gad,M.Z.
  TITLE     AGXT2 and DDAH-1 genetic variants are highly correlated with serum
            ADMA and SDMA levels and with incidence of coronary artery disease
            in Egyptians
  JOURNAL   Mol Biol Rep 45 (6), 2411-2419 (2018)
   PUBMED   30284143
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Hu,X.L., Zhou,J.P., Kuang,D.B., Qi,H., Peng,L.M., Yang,T.L., Li,X.,
            Zhang,W., Zhou,H.H. and Chen,X.P.
  TITLE     Considerable impacts of AGXT2 V140I polymorphism on chronic heart
            failure in the Chinese population
  JOURNAL   Atherosclerosis 251, 255-262 (2016)
   PUBMED   27423328
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Lee,I.S., Muragaki,Y., Ideguchi,T., Hase,T., Tsuji,M., Ooshima,A.,
            Okuno,E. and Kido,R.
  TITLE     Molecular cloning and sequencing of a cDNA encoding
            alanine-glyoxylate aminotransferase 2 from rat kidney
  JOURNAL   J Biochem 117 (4), 856-862 (1995)
   PUBMED   7592550
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Ogawa,T., Kimoto,M. and Sasaoka,K.
  TITLE     Dimethylarginine:pyruvate aminotransferase in rats. Purification,
            properties, and identity with alanine:glyoxylate aminotransferase 2
  JOURNAL   J Biol Chem 265 (34), 20938-20945 (1990)
   PUBMED   2123486
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Ueno,S., Sano,A., Hineno,T., Kondoh,K., Mizuno,T., Morino,H. and
            Kakimoto,Y.
  TITLE     Further studies on D-3-aminoisobutyrate-pyruvate aminotransferase
  JOURNAL   Biochim Biophys Acta 1035 (2), 128-131 (1990)
   PUBMED   2393662
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Tamaki,N., Kaneko,M., Mizota,C., Kikugawa,M. and Fujimoto,S.
  TITLE     Purification, characterization and inhibition of
            D-3-aminoisobutyrate aminotransferase from the rat liver
  JOURNAL   Eur J Biochem 189 (1), 39-45 (1990)
   PUBMED   2158891
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Okuno,E., Minatogawa,Y. and Kido,R.
  TITLE     Co-purification of alanine-glyoxylate aminotransferase with
            2-aminobutyrate aminotransferase in rat kidney
  JOURNAL   Biochim Biophys Acta 715 (1), 97-104 (1982)
   PUBMED   6803844
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081765.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081765.1, AB002584.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..512
                     /product="alanine--glyoxylate aminotransferase 2,
                     mitochondrial"
                     /EC_number="2.6.1.44"
                     /EC_number="2.6.1.40"
                     /EC_number="2.6.1.18"
                     /note="AGT 2; D-AIBAT; beta-ALAAT II;
                     (R)-3-amino-2-methylpropionate--pyruvate transaminase;
                     beta-alanine-pyruvate aminotransferase;
                     D-3-aminoisobutyrate-pyruvate aminotransferase;
                     D-beta-aminoisobutyrate-pyruvate aminotransferase"
                     /calculated_mol_wt=52646
     transit_peptide 1..39
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:10989446; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
                     /calculated_mol_wt=4574
     mat_peptide     40..512
                     /product="Alanine--glyoxylate aminotransferase 2,
                     mitochondrial. /id=PRO_0000001270"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64565.2)"
                     /calculated_mol_wt=52646
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Region          64..505
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
     Site            69
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Site            415
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     Site            452
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3UEG6; propagated from
                     UniProtKB/Swiss-Prot (Q64565.2)"
     CDS             1..512
                     /gene="Agxt2"
                     /gene_synonym="AGT2"
                     /coded_by="NM_031835.2:38..1576"
                     /db_xref="GeneID:83784"
                     /db_xref="RGD:621767"
ORIGIN      
        1 mslawrtlqk afyletslri lqmrpslsca sriyvpkltl htkhnmppcd fspekyqsla
       61 ynhvleihkq hlspvntayf qkplllhqgh mewlfdsegn ryldffsgiv tvgvghchpk
      121 vtavakkqmd rlwhtssvff hspmheyaer lsallpeplk viflvnsgse andlamvmar
      181 aysnhtdiis frgayhgcsp ytlgltnvgi ykmkvpstia cqstmcpdvf rgpwggshcr
      241 dspvqtvrkc scapdgcqak eryieqfkdt lntsvatsia gffaepiqgv ngvvqypkef
      301 lkeafalvre rggvciadev qtgfgrlgsh fwgfqthdtm pdivtmakgi gngfpmaavv
      361 ttpeiassla khlhhfstfg gsplacaigs avlevieeen lqrnsqevgt ymllkfaklr
      421 defdivgdvr gkglmvgiem vqdkisrqpl pktevnqihe dckdmgllvg rggnfsqtfr
      481 iappmrvtkl evdfafevfr saltqhmerr ak
//
LOCUS       NP_954517                410 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein NOB1 [Rattus norvegicus].
ACCESSION   NP_954517 XP_214674
VERSION     NP_954517.1
DBSOURCE    REFSEQ: accession NM_199086.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Henras,A.K., Plisson-Chastang,C., O'Donohue,M.F., Chakraborty,A.
            and Gleizes,P.E.
  TITLE     An overview of pre-ribosomal RNA processing in eukaryotes
  JOURNAL   Wiley Interdiscip Rev RNA 6 (2), 225-242 (2015)
   PUBMED   25346433
  REMARK    Review article
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zemp,I., Wandrey,F., Rao,S., Ashiono,C., Wyler,E., Montellese,C.
            and Kutay,U.
  TITLE     CK1delta and CK1epsilon are components of human 40S subunit
            precursors required for cytoplasmic 40S maturation
  JOURNAL   J Cell Sci 127 (Pt 6), 1242-1253 (2014)
   PUBMED   24424021
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Preti,M., O'Donohue,M.F., Montel-Lehry,N., Bortolin-Cavaille,M.L.,
            Choesmel,V. and Gleizes,P.E.
  TITLE     Gradual processing of the ITS1 from the nucleolus to the cytoplasm
            during synthesis of the human 18S rRNA
  JOURNAL   Nucleic Acids Res 41 (8), 4709-4723 (2013)
   PUBMED   23482395
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Sloan,K.E., Mattijssen,S., Lebaron,S., Tollervey,D., Pruijn,G.J.
            and Watkins,N.J.
  TITLE     Both endonucleolytic and exonucleolytic cleavage mediate ITS1
            removal during human ribosomal RNA processing
  JOURNAL   J Cell Biol 200 (5), 577-588 (2013)
   PUBMED   23439679
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Lei,B.
  TITLE     Rod-driven OFF pathway responses in the distal retina: dark-adapted
            flicker electroretinogram in mouse
  JOURNAL   PLoS One 7 (8), e43856 (2012)
   PUBMED   22937111
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Han,Y., Hong,L., Chen,Y., Zhong,C., Wang,Y., Zhao,D., Xue,T.,
            Qiao,L. and Qiu,J.
  TITLE     Up-regulation of Nob1 in the rat auditory system with noise-induced
            hearing loss
  JOURNAL   Neurosci Lett 491 (1), 79-82 (2011)
   PUBMED   21219967
  REMARK    GeneRIF: Nob1 may play an important role in auditory function
            following acoustic trauma.
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Fatica,A., Oeffinger,M., Dlakic,M. and Tollervey,D.
  TITLE     Nob1p is required for cleavage of the 3' end of 18S rRNA
  JOURNAL   Mol Cell Biol 23 (5), 1798-1807 (2003)
   PUBMED   12588997
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY341886.1.
            
            On Jan 1, 2004 this sequence version replaced XP_214674.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY341886.1, BC126076.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..410
                     /product="RNA-binding protein NOB1"
                     /note="nin one binding protein; NIN1/PSMD8 binding protein
                     1 homolog"
                     /calculated_mol_wt=46294
     Region          7..93
                     /region_name="PIN_6"
                     /note="PIN domain of ribonuclease; pfam17146"
                     /db_xref="CDD:465362"
     Region          153..210
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     Region          180..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6VEU1.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ULX3; propagated from
                     UniProtKB/Swiss-Prot (Q6VEU1.1)"
     Region          258..330
                     /region_name="NOB1_Zn_bind"
                     /note="Nin one binding (NOB1) Zn-ribbon like; pfam08772"
                     /db_xref="CDD:462597"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ULX3; propagated from
                     UniProtKB/Swiss-Prot (Q6VEU1.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ULX3; propagated from
                     UniProtKB/Swiss-Prot (Q6VEU1.1)"
     CDS             1..410
                     /gene="Nob1"
                     /gene_synonym="Nob1p"
                     /coded_by="NM_199086.1:9..1241"
                     /db_xref="GeneID:291996"
                     /db_xref="RGD:735222"
ORIGIN      
        1 mapvehvvad agaflrdapl qdigkniyti revvreirdk atrrrlavlp yelrfkepfp
       61 eyvrlvtefs kktgdypsls atdiqvlalt yqleaefvgv shlkkepekv kvsssiqhpe
      121 tplhisgfhl pskskalqet vdhgppadgs enlefssfmf wrnplpnidh elqqllidgr
      181 eeeeeeeeee eeedeledsd ddgggwitps nikqiqhese qcdipkdvqv gcvttdfamq
      241 nvllqmglhv lavngmlvre arsyilrchg cfkttsdmnr vfcghcgnkt lkkvsvtind
      301 dgtlhmhfsr npkvlnprgl ryslptpkgg kyavnphlte dqrfpqlrls hkarqktnvf
      361 apdyiagvsp faendissrs ailqvrdsml gagrrrlnpn asrkkfvkkr
//
LOCUS       NP_001077280             883 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor 2 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001077280
VERSION     NP_001077280.1
DBSOURCE    REFSEQ: accession NM_001083811.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Zhang,J., Liu,Z., Liu,X., Wang,X. and Yu,L.
  TITLE     Intravenous Injection of GluR2-3Y Inhibits Repeated Morphine-Primed
            Reinstatement of Drug Seeking in Rats
  JOURNAL   Brain Sci 13 (4), 590 (2023)
   PUBMED   37190555
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Han,J.X., Wen,C.X., Sun,R., Tang,M.Y., Li,X.M. and Lian,H.
  TITLE     The dorsal hippocampal CA3 regulates spatial reference memory
            through the CtBP2/GluR2 pathway
  JOURNAL   FASEB J 36 (9), e22456 (2022)
   PUBMED   35969153
  REMARK    GeneRIF: The dorsal hippocampal CA3 regulates spatial reference
            memory through the CtBP2/GluR2 pathway.
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Herguedas,B., Kohegyi,B.K., Dohrke,J.N., Watson,J.F., Zhang,D.,
            Ho,H., Shaikh,S.A., Lape,R., Krieger,J.M. and Greger,I.H.
  TITLE     Mechanisms underlying TARP modulation of the GluA1/2-gamma8 AMPA
            receptor
  JOURNAL   Nat Commun 13 (1), 734 (2022)
   PUBMED   35136046
  REMARK    GeneRIF: Mechanisms underlying TARP modulation of the
            GluA1/2-gamma8 AMPA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Schwarz,A.P., Kovalenko,A.A., Zakharova,M.V. and Zaitsev,A.V.
  TITLE     The application of the self-probing primer PCR for quantitative
            expression analysis of R607Q (un)edited GluA2 AMPA receptor mRNA
  JOURNAL   Biochem Biophys Res Commun 569, 174-178 (2021)
   PUBMED   34252589
  REMARK    GeneRIF: The application of the self-probing primer PCR for
            quantitative expression analysis of R607Q (un)edited GluA2 AMPA
            receptor mRNA.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Pereyra,M., de Landeta,A.B., Dalto,J.F., Katche,C. and Medina,J.H.
  TITLE     AMPA Receptor Expression Requirement During Long-Term Memory
            Retrieval and Its Association with mTORC1 Signaling
  JOURNAL   Mol Neurobiol 58 (4), 1711-1722 (2021)
   PUBMED   33244735
  REMARK    GeneRIF: AMPA Receptor Expression Requirement During Long-Term
            Memory Retrieval and Its Association with mTORC1 Signaling.
REFERENCE   6  (residues 1 to 883)
  AUTHORS   Hume,R.I., Dingledine,R. and Heinemann,S.F.
  TITLE     Identification of a site in glutamate receptor subunits that
            controls calcium permeability
  JOURNAL   Science 253 (5023), 1028-1031 (1991)
   PUBMED   1653450
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Nakanishi,N., Shneider,N.A. and Axel,R.
  TITLE     A family of glutamate receptor genes: evidence for the formation of
            heteromultimeric receptors with distinct channel properties
  JOURNAL   Neuron 5 (5), 569-581 (1990)
   PUBMED   1699567
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Sommer,B., Keinanen,K., Verdoorn,T.A., Wisden,W., Burnashev,N.,
            Herb,A., Kohler,M., Takagi,T., Sakmann,B. and Seeburg,P.H.
  TITLE     Flip and flop: a cell-specific functional switch in
            glutamate-operated channels of the CNS
  JOURNAL   Science 249 (4976), 1580-1585 (1990)
   PUBMED   1699275
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Boulter,J., Hollmann,M., O'Shea-Greenfield,A., Hartley,M.,
            Deneris,E., Maron,C. and Heinemann,S.
  TITLE     Molecular cloning and functional expression of glutamate receptor
            subunit genes
  JOURNAL   Science 249 (4972), 1033-1037 (1990)
   PUBMED   2168579
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Keinanen,K., Wisden,W., Sommer,B., Werner,P., Herb,A.,
            Verdoorn,T.A., Sakmann,B. and Seeburg,P.H.
  TITLE     A family of AMPA-selective glutamate receptors
  JOURNAL   Science 249 (4968), 556-560 (1990)
   PUBMED   2166337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M38061.1, AF164344.1,
            CO400088.1, M85035.1 and JAXUCZ010000002.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to a family of glutamate receptors that are
            sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate
            (AMPA), and function as ligand-activated cation channels. These
            channels are assembled from 4 related subunits, Gria1-4. The
            subunit encoded by this gene (Gria2) is subject to RNA editing (Q/R
            and R/G), which is thought to render the channels impermeable to
            Ca(2+), and to affect the kinetic aspects of these channels in rat
            brain. Alternative splicing, resulting in transcript variants
            encoding different isoforms (flip and flop), has been noted for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate exon in the
            3' coding region compared to transcript variant 1, and encodes an
            isoform (2, also known as the flop isoform) that is the same length
            as isoform 1, but with few amino acid differences. RNA editing
            changes Gln607Arg (CAG->CGG) and Arg764Gly (AGA->GGA).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M85035.1, SRR26360194.1157002.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 7992055, 12045112
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q33"
     Protein         1..883
                     /product="glutamate receptor 2 isoform 2 precursor"
                     /note="glutamate receptor B; AMPA-selective glutamate
                     receptor 2; glutamate receptor, ionotropic, AMPA 2"
                     /calculated_mol_wt=96078
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     Region          28..398
                     /region_name="PBP1_iGluR_AMPA_GluR2"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the GluR2 subunit of the
                     AMPA receptor; cd06389"
                     /db_xref="CDD:380612"
     Site            order(69..71,74..75,78,98..99,102..103,106,152,162,
                     165..166,169..170,177,179,198,329..331,333,335)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380612"
     Site            order(69..71,74..75,78,98..99,102..103,106,152,162,
                     165..166,169..170,177,179,198,329..331,333,335)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380612"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21317873; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            370
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19946266,
                     ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Region          413..794
                     /region_name="PBP2_iGluR_AMPA"
                     /note="The ligand-binding domain of the AMPA
                     (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic
                     acid) subtypes of ionotropic glutamate receptors, a member
                     of the type 2 periplasmic binding fold protein
                     superfamily; cd13715"
                     /db_xref="CDD:270433"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            order(452,456,503..504,507,512..515,750,768..769,772..777,
                     779,782)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            order(471,499..501,506,671,674..676,725..726,729,753)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            474
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            order(514..518,772,775,780..781,784)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270433"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            617..637
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            654
                     /site_type="other"
                     /note="Crucial to convey clamshell closure to channel
                     opening. /evidence=ECO:0000269|PubMed:25103405; propagated
                     from UniProtKB/Swiss-Prot (P19491.2)"
     Site            681
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:8848293; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG.
                     /evidence=ECO:0000269|PubMed:8848293; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            773
                     /site_type="other"
                     /note="Interaction with the cone snail toxin
                     Con-ikot-ikot. /evidence=ECO:0000269|PubMed:25103405;
                     propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            813..833
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            863
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Region          867..877
                     /region_name="Required for interaction with IQSEC1.
                     /evidence=ECO:0000269|PubMed:20547133"
                     /note="propagated from UniProtKB/Swiss-Prot (P19491.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:15240807,
                     ECO:0000269|PubMed:20547133; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23819; propagated from
                     UniProtKB/Swiss-Prot (P19491.2)"
     CDS             1..883
                     /gene="Gria2"
                     /gene_synonym="GluA2; gluR-B; GluR-K2; GluR2"
                     /coded_by="NM_001083811.1:431..3082"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29627"
                     /db_xref="RGD:61862"
ORIGIN      
        1 mqkimhisvl lspvlwglif gvssnsiqig glfprgadqe ysafrvgmvq fstsefrltp
       61 hidnlevans favtnafcsq fsrgvyaifg fydkksvnti tsfcgtlhvs fitpsfptdg
      121 thpfviqmrp dlkgallsli eyyqwdkfay lydsdrglst lqavldsaae kkwqvtainv
      181 gninndkkde tyrslfqdle lkkerrvild cerdkvndiv dqvitigkhv kgyhyiianl
      241 gftdgdllki qfgganvsgf qivdyddslv skfierwstl eekeypgaht atikytsalt
      301 ydavqvmtea frnlrkqrie isrrgnagdc lanpavpwgq gveieralkq vqveglsgni
      361 kfdqngkrin ytinimelkt ngprkigyws evdkmvvtlt elpsgndtsg lenktvvvtt
      421 ilespyvmmk knhemlegne ryegycvdla aeiakhcgfk ykltivgdgk ygardadtki
      481 wngmvgelvy gkadiaiapl titlvreevi dfskpfmslg isimikkpqk skpgvfsfld
      541 playeiwmci vfayigvsvv lflvsrfspy ewhteefedg retqssestn efgifnslwf
      601 slgafmrqgc disprslsgr ivggvwwfft liiissytan laafltverm vspiesaedl
      661 skqteiaygt ldsgstkeff rrskiavfdk mwtymrsaep svfvrttaeg varvrkskgk
      721 yayllestmn eyieqrkpcd tmkvggnlds kgygiatpkg sslgnavnla vlklneqgll
      781 dklknkwwyd kgecgsgggd skektsalsl snvagvfyil vgglglamlv aliefcyksr
      841 aeakrmkvak npqninpsss qnsqnfatyk egynvygies vki
//
LOCUS       NP_001012003             576 aa            linear   ROD 27-APR-2025
DEFINITION  origin recognition complex subunit 2 [Rattus norvegicus].
ACCESSION   NP_001012003 XP_217403
VERSION     NP_001012003.1
DBSOURCE    REFSEQ: accession NM_001012003.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Bronze-da-Rocha,E., Lin,C.M., Shimura,T. and Aladjem,M.I.
  TITLE     Interactions of MCP1 with components of the replication machinery
            in mammalian cells
  JOURNAL   Int J Biol Sci 7 (2), 193-208 (2011)
   PUBMED   21383955
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Shen,Z., Sathyan,K.M., Geng,Y., Zheng,R., Chakraborty,A.,
            Freeman,B., Wang,F., Prasanth,K.V. and Prasanth,S.G.
  TITLE     A WD-repeat protein stabilizes ORC binding to chromatin
  JOURNAL   Mol Cell 40 (1), 99-111 (2010)
   PUBMED   20932478
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Ishii,H., Inageta,T., Mimori,K., Saito,T., Sasaki,H., Isobe,M.,
            Mori,M., Croce,C.M., Huebner,K., Ozawa,K. and Furukawa,Y.
  TITLE     Frag1, a homolog of alternative replication factor C subunits,
            links replication stress surveillance with apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 102 (27), 9655-9660 (2005)
   PUBMED   15983387
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Dannenberg,J.H., David,G., Zhong,S., van der Torre,J., Wong,W.H.
            and Depinho,R.A.
  TITLE     mSin3A corepressor regulates diverse transcriptional networks
            governing normal and neoplastic growth and survival
  JOURNAL   Genes Dev 19 (13), 1581-1595 (2005)
   PUBMED   15998811
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Prasanth,S.G., Prasanth,K.V., Siddiqui,K., Spector,D.L. and
            Stillman,B.
  TITLE     Human Orc2 localizes to centrosomes, centromeres and
            heterochromatin during chromosome inheritance
  JOURNAL   EMBO J 23 (13), 2651-2663 (2004)
   PUBMED   15215892
  REMARK    Erratum:[EMBO J. 2005 Mar 9;24(5):1092-4]
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Craig,J.M., Earle,E., Canham,P., Wong,L.H., Anderson,M. and
            Choo,K.H.
  TITLE     Analysis of mammalian proteins involved in chromatin modification
            reveals new metaphase centromeric proteins and distinct chromosomal
            distribution patterns
  JOURNAL   Hum Mol Genet 12 (23), 3109-3121 (2003)
   PUBMED   14519686
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Geng,Y., Yu,Q., Sicinska,E., Das,M., Schneider,J.E.,
            Bhattacharya,S., Rideout,W.M., Bronson,R.T., Gardner,H. and
            Sicinski,P.
  TITLE     Cyclin E ablation in the mouse
  JOURNAL   Cell 114 (4), 431-443 (2003)
   PUBMED   12941272
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB164704.1.
            
            On Feb 11, 2005 this sequence version replaced XP_217403.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB164704.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..576
                     /product="origin recognition complex subunit 2"
                     /calculated_mol_wt=65719
     Region          1..100
                     /region_name="Involved in LRWD1-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75PQ8.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13416; propagated from
                     UniProtKB/Swiss-Prot (Q75PQ8.1)"
     Region          119..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q75PQ8.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13416; propagated from
                     UniProtKB/Swiss-Prot (Q75PQ8.1)"
     Region          254..560
                     /region_name="ORC2"
                     /note="Origin recognition complex subunit 2; pfam04084"
                     /db_xref="CDD:461163"
     CDS             1..576
                     /gene="Orc2"
                     /gene_synonym="Orc2l"
                     /coded_by="NM_001012003.1:62..1792"
                     /db_xref="GeneID:301430"
                     /db_xref="RGD:1311844"
ORIGIN      
        1 mstlrlkeak vpsvqfvgdd dvlshildre ggtklkkekv qllvnpqkvi kkaeceleks
       61 dlevledqny vevlgrniqe slgngsavdg rnkvysfqhr khpeemtkla lelaktsgki
      121 dplasndpki tkniarkskg hssekaplen nnknefpsiq phnvrkrlia srshcdsese
      181 ysasssedde evakddeedt nvvrcskksq gqnrllpapv skeilpkkrk rdkagdlvee
      241 yfeahssskv ltsdrtlqkl rrarvdqktl rnllskfvps fsteigqlnq qherlfdkwi
      301 lqlrlgfniv lyglgskrdl lekfrttmlq dsihvvingf fpgisvksil nsitedvlsh
      361 mgtfqsvldq rdwimnrfke dsslelflli hnldsqmlrg dnsqqilgql sslrnvylia
      421 sidhlnaplm wdhakqslyn wlwyetttys pyteetsyen sllvkqsgsl plsslihvlr
      481 sltpnargif rllmkyqldn qdcpsyigls fqdfyqqcre aflvnsdltl raqltefrdh
      541 klirtkkgtd gveyllipvd sgtladflek eeeees
//
LOCUS       NP_997682                141 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11
            [Rattus norvegicus].
ACCESSION   NP_997682 XP_217316
VERSION     NP_997682.1
DBSOURCE    REFSEQ: accession NM_212517.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Liu,Y., Qu,H.Q., Chang,X., Qu,J., Mentch,F.D., Nguyen,K., Tian,L.,
            Glessner,J., Sleiman,P.M.A. and Hakonarson,H.
  TITLE     Mutation burden analysis of six common mental disorders in African
            Americans by whole genome sequencing
  JOURNAL   Hum Mol Genet 31 (22), 3769-3776 (2022)
   PUBMED   35642741
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Stroud,D.A., Surgenor,E.E., Formosa,L.E., Reljic,B., Frazier,A.E.,
            Dibley,M.G., Osellame,L.D., Stait,T., Beilharz,T.H., Thorburn,D.R.,
            Salim,A. and Ryan,M.T.
  TITLE     Accessory subunits are integral for assembly and function of human
            mitochondrial complex I
  JOURNAL   Nature 538 (7623), 123-126 (2016)
   PUBMED   27626371
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY272059.1.
            
            On Aug 30, 2004 this sequence version replaced XP_217316.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY272059.1, DV716312.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..141
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 11"
                     /EC_number="7.1.1.2"
                     /note="NADH-ubiquinone oxidoreductase subunit B14.7;
                     CI-B14.7; complex I-B14.7; NADH dehydrogenase (ubiquinone)
                     1 alpha subcomplex 11"
                     /calculated_mol_wt=14723
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8HXG6; propagated from
                     UniProtKB/Swiss-Prot (Q80W89.1)"
     Region          18..119
                     /region_name="Tim17"
                     /note="Tim17/Tim22/Tim23/Pmp24 family; pfam02466"
                     /db_xref="CDD:460567"
     Site            21..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W89.1)"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W89.1)"
     CDS             1..141
                     /gene="Ndufa11"
                     /coded_by="NM_212517.1:49..474"
                     /db_xref="GeneID:301123"
                     /db_xref="RGD:1303292"
ORIGIN      
        1 makrffeayn etpdgtqchr kayittalgg lcglissays ithnpadspl eavarvgrft
       61 ftaaaigamf glttcvsaqv rekpddplny figgcagglt lgarthsygt aaigcvymgt
      121 aaalfkmgkl egwelfatpk v
//
LOCUS       NP_001029186             512 aa            linear   ROD 27-APR-2025
DEFINITION  acid-sensing ion channel 2 isoform MDEG1 [Rattus norvegicus].
ACCESSION   NP_001029186
VERSION     NP_001029186.1
DBSOURCE    REFSEQ: accession NM_001034014.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Shibata,Y., Kumamoto,N., Sakuma,E., Ishida,Y., Ueda,T., Shimada,S.
            and Ugawa,S.
  TITLE     A gain-of-function mutation in the acid-sensing ion channel 2a
            induces marked cerebellar maldevelopment in rats
  JOURNAL   Biochem Biophys Res Commun 610, 77-84 (2022)
   PUBMED   35447498
  REMARK    GeneRIF: A gain-of-function mutation in the acid-sensing ion
            channel 2a induces marked cerebellar maldevelopment in rats.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Yan,X., Zhang,S., Zhao,H., Liu,P., Huang,H., Niu,W., Wang,W. and
            Zhang,C.
  TITLE     ASIC2 Synergizes with TRPV1 in the Mechano-Electrical Transduction
            of Arterial Baroreceptors
  JOURNAL   Neurosci Bull 37 (10), 1381-1396 (2021)
   PUBMED   34215968
  REMARK    GeneRIF: ASIC2 Synergizes with TRPV1 in the Mechano-Electrical
            Transduction of Arterial Baroreceptors.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Liu,Y., Hagan,R. and Schoellerman,J.
  TITLE     Dual actions of Psalmotoxin at ASIC1a and ASIC2a heteromeric
            channels (ASIC1a/2a)
  JOURNAL   Sci Rep 8 (1), 7179 (2018)
   PUBMED   29739981
  REMARK    GeneRIF: Our findings identify PcTx1 as a valuable tool for
            studying ASIC1a/2a function and contribute significantly to the
            understanding of the diverse and complex pharmacology of PcTx1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Zhang,H., Gao,G., Zhang,Y., Sun,Y., Li,H., Dong,S., Ma,W., Liu,B.,
            Wang,W., Wu,H. and Zhang,H.
  TITLE     Glucose Deficiency Elevates Acid-Sensing Ion Channel 2a Expression
            and Increases Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Sci Rep 7 (1), 5870 (2017)
   PUBMED   28725010
  REMARK    GeneRIF: hippocampal glucose hypometabolism elevates ASIC2a
            expression by suppressing TFCP2 expression, which further enhances
            the intrinsic excitability of CA1 pyramidal neurons and increases
            seizure susceptibility in patients with temporal lobe epilepsy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Wu,H., Wang,C., Liu,B., Li,H., Zhang,Y., Dong,S., Gao,G. and
            Zhang,H.
  TITLE     Altered Expression Pattern of Acid-Sensing Ion Channel Isoforms in
            Piriform Cortex After Seizures
  JOURNAL   Mol Neurobiol 53 (3), 1782-1793 (2016)
   PUBMED   25744567
  REMARK    GeneRIF: ASICs may enhance susceptibility to epileptogenesis in the
            piriform cortex.
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Bassilana,F., Champigny,G., Waldmann,R., de Weille,J.R.,
            Heurteaux,C. and Lazdunski,M.
  TITLE     The acid-sensitive ionic channel subunit ASIC and the mammalian
            degenerin MDEG form a heteromultimeric H+-gated Na+ channel with
            novel properties
  JOURNAL   J Biol Chem 272 (46), 28819-28822 (1997)
   PUBMED   9360943
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Waldmann,R., Champigny,G., Voilley,N., Lauritzen,I. and
            Lazdunski,M.
  TITLE     The mammalian degenerin MDEG, an amiloride-sensitive cation channel
            activated by mutations causing neurodegeneration in Caenorhabditis
            elegans
  JOURNAL   J Biol Chem 271 (18), 10433-10436 (1996)
   PUBMED   8631835
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Sokolov,Iu.N., Kaigorodtseva,R.N. and Rudykh,V.F.
  TITLE     [Various roentgenomorphological parallels in ulcers of the
            pyloro-duodenal area]
  JOURNAL   Vestn Rentgenol Radiol (6), 3-11 (1978)
   PUBMED   734884
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Carson,A.
  TITLE     Writing good abstracts: it's a tought job
  JOURNAL   Phys Ther 58 (2), 175-177 (1978)
   PUBMED   625485
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Tanaka,S., Tamura,K. and Mizuno,Y.
  TITLE     [Clinical consideration with special reference to autopsy cases of
            malignant tumor in the oral cavity, treated with Bleomycin
            (author's transl)]
  JOURNAL   Hiroshima Daigaku Shigaku Zasshi 8 (2), 168-175 (1975)
   PUBMED   69641
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U53211.1.
            
            Transcript Variant: This variant (MDEG1) uses an alternate 5'
            terminal exon compared to variant MDEG2. The resulting protein
            (isoform MDGEG1) is shorter and has a distinct N-terminus compared
            to isoform MDEG2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U53211.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..512
                     /product="acid-sensing ion channel 2 isoform MDEG1"
                     /note="degenerin; brain sodium channel 1; acid-sensing ion
                     channel 2; amiloride-sensitive brain sodium channel 2;
                     BNC1; acid-sensing proton-gated ion channel 2 short
                     variant MDEG2; acid-sensing (proton-gated) ion channel 2;
                     amiloride-sensitive cation channel 1, neuronal"
                     /calculated_mol_wt=57608
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62962.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62962.1)"
     Region          18..506
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62962.1)"
     Site            365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15504740; propagated from
                     UniProtKB/Swiss-Prot (Q62962.1)"
     Site            392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15504740; propagated from
                     UniProtKB/Swiss-Prot (Q62962.1)"
     Site            428..448
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62962.1)"
     Region          441..443
                     /region_name="GAS motif, ion selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P78348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62962.1)"
     CDS             1..512
                     /gene="Asic2"
                     /gene_synonym="Accn1; BNaC1; BNC1k; MDEG; MDEG1; MDEG2"
                     /coded_by="NM_001034014.1:154..1692"
                     /note="isoform MDEG1 is encoded by transcript variant
                     MDEG1"
                     /db_xref="GeneID:25364"
                     /db_xref="RGD:2017"
ORIGIN      
        1 mdlkespseg slqpssiqif antstlhgir hifvygplti rrvlwavafv gslglllves
       61 servsyyfsy qhvtkvdevv aqslvfpavt lcnlngfrfs rlttndlyha gellalldvn
      121 lqipdphlad ptvlealrqk anfkhykpkq fsmleflhrv ghdlkdmmly ckfkgqecgh
      181 qdfttvftky gkcymfnsge dgkpllttvk ggtgngleim ldiqqdeylp iwgeteettf
      241 eagvkvqihs qseppfiqel gfgvapgfqt fvatqeqrlt ylpppwgecr ssemgldffp
      301 vysitacrid cetryivenc ncrmvhmpgd apfctpeqhk ecaepalgll aekdsnyclc
      361 rtpcnltryn kelsmvkips ktsakylekk fnksekyise nilvldiffe alnyetieqk
      421 kayevaallg diggqmglfi gaslltilel fdyiyelike klldllgkee eegshdenms
      481 tcdtmpnhse tishtvnvpl qtalgtleei ac
//
LOCUS       NP_899158                232 aa            linear   ROD 27-APR-2025
DEFINITION  steroid receptor RNA activator 1 [Rattus norvegicus].
ACCESSION   NP_899158 XP_341598
VERSION     NP_899158.3
DBSOURCE    REFSEQ: accession NM_183329.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Jiang,B., Wang,H. and Xu,H.
  TITLE     Steroid receptor RNA activator affects the development of
            poststroke depression by regulating the peroxisome
            proliferator-activated receptor gamma signaling pathway
  JOURNAL   Neuroreport 31 (1), 48-56 (2020)
   PUBMED   31714481
  REMARK    GeneRIF: Steroid receptor RNA activator affects the development of
            poststroke depression by regulating the peroxisome
            proliferator-activated receptor gamma signaling pathway.
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Greco,S., Zaccagnini,G., Perfetti,A., Fuschi,P., Valaperta,R.,
            Voellenkle,C., Castelvecchio,S., Gaetano,C., Finato,N.,
            Beltrami,A.P., Menicanti,L. and Martelli,F.
  TITLE     Long noncoding RNA dysregulation in ischemic heart failure
  JOURNAL   J Transl Med 14 (1), 183 (2016)
   PUBMED   27317124
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Kotan,L.D., Cooper,C., Darcan,S., Carr,I.M., Ozen,S., Yan,Y.,
            Hamedani,M.K., Gurbuz,F., Mengen,E., Turan,I., Ulubay,A., Akkus,G.,
            Yuksel,B., Topaloglu,A.K. and Leygue,E.
  TITLE     Idiopathic Hypogonadotropic Hypogonadism Caused by Inactivating
            Mutations in SRA1
  JOURNAL   J Clin Res Pediatr Endocrinol 8 (2), 125-134 (2016)
   PUBMED   27086651
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Bilinovich,S.M., Davis,C.M., Morris,D.L., Ray,L.A., Prokop,J.W.,
            Buchan,G.J. and Leeper,T.C.
  TITLE     The C-terminal domain of SRA1p has a fold more similar to PRP18
            than to an RRM and does not directly bind to the SRA1 RNA STR7
            region
  JOURNAL   J Mol Biol 426 (8), 1753-1765 (2014)
   PUBMED   24486611
REFERENCE   5  (residues 1 to 232)
  AUTHORS   McKay,D.B., Xi,L., Barthel,K.K.B. and Cech,T.R.
  TITLE     Structure and function of steroid receptor RNA activator protein,
            the proposed partner of SRA noncoding RNA
  JOURNAL   J Mol Biol 426 (8), 1766-1785 (2014)
   PUBMED   24486609
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Lanz,R.B., Chua,S.S., Barron,N., Soder,B.M., DeMayo,F. and
            O'Malley,B.W.
  TITLE     Steroid receptor RNA activator stimulates proliferation as well as
            apoptosis in vivo
  JOURNAL   Mol Cell Biol 23 (20), 7163-7176 (2003)
   PUBMED   14517287
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Emberley,E., Huang,G.J., Hamedani,M.K., Czosnek,A., Ali,D.,
            Grolla,A., Lu,B., Watson,P.H., Murphy,L.C. and Leygue,E.
  TITLE     Identification of new human coding steroid receptor RNA activator
            isoforms
  JOURNAL   Biochem Biophys Res Commun 301 (2), 509-515 (2003)
   PUBMED   12565891
  REMARK    Erratum:[Biochem Biophys Res Commun. 2003 Aug 1;307(3):757]
REFERENCE   8  (residues 1 to 232)
  AUTHORS   Kawashima,H., Takano,H., Sugita,S., Takahara,Y., Sugimura,K. and
            Nakatani,T.
  TITLE     A novel steroid receptor co-activator protein (SRAP) as an
            alternative form of steroid receptor RNA-activator gene: expression
            in prostate cancer cells and enhancement of androgen receptor
            activity
  JOURNAL   Biochem J 369 (Pt 1), 163-171 (2003)
   PUBMED   12350225
REFERENCE   9  (residues 1 to 232)
  AUTHORS   Wolf,G., Jocks,T., Zahner,G., Panzer,U. and Stahl,R.A.
  TITLE     Existence of a regulatory loop between MCP-1 and TGF-beta in
            glomerular immune injury
  JOURNAL   Am J Physiol Renal Physiol 283 (5), F1075-F1084 (2002)
   PUBMED   12372783
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Lanz,R.B., McKenna,N.J., Onate,S.A., Albrecht,U., Wong,J.,
            Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     A steroid receptor coactivator, SRA, functions as an RNA and is
            present in an SRC-1 complex
  JOURNAL   Cell 97 (1), 17-27 (1999)
   PUBMED   10199399
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY542868.1 and
            CB322787.1.
            
            On Oct 28, 2005 this sequence version replaced NP_899158.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF110391.1, CB567439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..232
                     /product="steroid receptor RNA activator 1"
                     /note="SRAP; steroid receptor RNA activator protein"
                     /calculated_mol_wt=25234
     Region          78..210
                     /region_name="SRA1"
                     /note="Steroid receptor RNA activator (SRA1); pfam07304"
                     /db_xref="CDD:429397"
     CDS             1..232
                     /gene="Sra1"
                     /coded_by="NM_183329.3:21..719"
                     /db_xref="GeneID:252891"
                     /db_xref="RGD:621148"
ORIGIN      
        1 mtccpaggae vemaelyvkp gnkergwndp pqfsyglqtq tggtkrtplt krvaapqdgs
       61 prapetsgpp pvdhpppssk asrpppmgsc pasgvdppss pviesetlie dvlrpleqal
      121 edcrghtkkq vcddisrrla llheqwdggk lsvpvkkrma llvqellhhq wdtaddihrs
      181 lmvdhvtevs qwmvgvkrli aekrslssee nkeetstvap enqtipgfqp ss
//
LOCUS       NP_001100728             492 aa            linear   ROD 27-APR-2025
DEFINITION  beclin 1-associated autophagy-related key regulator [Rattus
            norvegicus].
ACCESSION   NP_001100728 XP_001073554 XP_223939
VERSION     NP_001100728.1
DBSOURCE    REFSEQ: accession NM_001107258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Li,S., Gao,L., Zhang,W., Yu,Y., Zheng,J., Liang,X., Xin,S., Ren,W.
            and Zhi,K.
  TITLE     MiR-152-5p suppresses osteogenic differentiation of mandible
            mesenchymal stem cells by regulating ATG14-mediated autophagy
  JOURNAL   Stem Cell Res Ther 13 (1), 359 (2022)
   PUBMED   35883156
  REMARK    GeneRIF: MiR-152-5p suppresses osteogenic differentiation of
            mandible mesenchymal stem cells by regulating ATG14-mediated
            autophagy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Chauhan,S., Mandell,M.A. and Deretic,V.
  TITLE     IRGM governs the core autophagy machinery to conduct antimicrobial
            defense
  JOURNAL   Mol Cell 58 (3), 507-521 (2015)
   PUBMED   25891078
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Diao,J., Liu,R., Rong,Y., Zhao,M., Zhang,J., Lai,Y., Zhou,Q.,
            Wilz,L.M., Li,J., Vivona,S., Pfuetzner,R.A., Brunger,A.T. and
            Zhong,Q.
  TITLE     ATG14 promotes membrane tethering and fusion of autophagosomes to
            endolysosomes
  JOURNAL   Nature 520 (7548), 563-566 (2015)
   PUBMED   25686604
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Pampliega,O., Orhon,I., Patel,B., Sridhar,S., Diaz-Carretero,A.,
            Beau,I., Codogno,P., Satir,B.H., Satir,P. and Cuervo,A.M.
  TITLE     Functional interaction between autophagy and ciliogenesis
  JOURNAL   Nature 502 (7470), 194-200 (2013)
   PUBMED   24089209
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Fogel,A.I., Dlouhy,B.J., Wang,C., Ryu,S.W., Neutzner,A.,
            Hasson,S.A., Sideris,D.P., Abeliovich,H. and Youle,R.J.
  TITLE     Role of membrane association and Atg14-dependent phosphorylation in
            beclin-1-mediated autophagy
  JOURNAL   Mol Cell Biol 33 (18), 3675-3688 (2013)
   PUBMED   23878393
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Fan,W., Nassiri,A. and Zhong,Q.
  TITLE     Autophagosome targeting and membrane curvature sensing by
            Barkor/Atg14(L)
  JOURNAL   Proc Natl Acad Sci U S A 108 (19), 7769-7774 (2011)
   PUBMED   21518905
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Sun,Q., Zhang,J., Fan,W., Wong,K.N., Ding,X., Chen,S. and Zhong,Q.
  TITLE     The RUN domain of rubicon is important for hVps34 binding, lipid
            kinase inhibition, and autophagy suppression
  JOURNAL   J Biol Chem 286 (1), 185-191 (2011)
   PUBMED   21062745
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Yang,Z. and Klionsky,D.J.
  TITLE     Mammalian autophagy: core molecular machinery and signaling
            regulation
  JOURNAL   Curr Opin Cell Biol 22 (2), 124-131 (2010)
   PUBMED   20034776
  REMARK    Review article
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Matsunaga,K., Saitoh,T., Tabata,K., Omori,H., Satoh,T.,
            Kurotori,N., Maejima,I., Shirahama-Noda,K., Ichimura,T., Isobe,T.,
            Akira,S., Noda,T. and Yoshimori,T.
  TITLE     Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally
            regulate autophagy at different stages
  JOURNAL   Nat Cell Biol 11 (4), 385-396 (2009)
   PUBMED   19270696
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Zhong,Y., Wang,Q.J., Li,X., Yan,Y., Backer,J.M., Chait,B.T.,
            Heintz,N. and Yue,Z.
  TITLE     Distinct regulation of autophagic activity by Atg14L and Rubicon
            associated with Beclin 1-phosphatidylinositol-3-kinase complex
  JOURNAL   Nat Cell Biol 11 (4), 468-476 (2009)
   PUBMED   19270693
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474040.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001073554.1, XP_223939.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223033.1, SRR8487226.173115.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..492
                     /product="beclin 1-associated autophagy-related key
                     regulator"
                     /note="barkor; autophagy-related protein 14-like protein;
                     beclin 1-associated autophagy-related key regulator-like;
                     ATG14 autophagy related 14 homolog"
                     /calculated_mol_wt=55214
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZNE5; propagated from
                     UniProtKB/Swiss-Prot (D4A4K3.1)"
     Region          43..383
                     /region_name="ATG14"
                     /note="Vacuolar sorting 38 and autophagy-related subunit
                     14; pfam10186"
                     /db_xref="CDD:462986"
     Region          213..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A4K3.1)"
     Region          411..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A4K3.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZNE5; propagated from
                     UniProtKB/Swiss-Prot (D4A4K3.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZNE5; propagated from
                     UniProtKB/Swiss-Prot (D4A4K3.1)"
     CDS             1..492
                     /gene="Atg14"
                     /gene_synonym="Atg14L; RGD1304610"
                     /coded_by="NM_001107258.1:36..1514"
                     /db_xref="GeneID:305831"
                     /db_xref="RGD:1304610"
ORIGIN      
        1 maspsgkgsw tpeapgfgpr alapdlvdsv ddaeglyvav ercplcnttr rrltcakcvq
       61 sgdfvyfdgr drerfidkke rlsqlknkqe efqkevlkam egkrltdqlr wkimsckmri
      121 eqlkqtickg neemkknseg llknkeknqk lysraqrhqe kkekiqrhnr klgdlvekkt
      181 sdlrehydrl aclrrlhile ltsvifpmde vktsgrdpad vssetdsamt ssmvsklaea
      241 rrttylsgrw vcddhngdts isitgpwisl pnngdysayy nwveekkttq gpdmehnnpa
      301 ytisaalgya tqlvnivshi ldinlpkklc nsefcgenls kqrltravrk lnanilylcs
      361 sqhvnldqlq plhtlrnlmh lvsphsehlg rsgpfevrad leesmefvdp gvagesdvsg
      421 dervsdeetd lgtdwenlps prfcdipsqp vevsqsqstq asppiasssa ggmissaaas
      481 vtswfkaytg hr
//
LOCUS       NP_001007750             200 aa            linear   ROD 27-APR-2025
DEFINITION  ATP synthase subunit s, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_001007750 XP_343075
VERSION     NP_001007750.1
DBSOURCE    REFSEQ: accession NM_001007749.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Sanadi,D.R., Pringle,M., Kantham,L., Hughes,J.B. and Srivastava,A.
  TITLE     Evidence for the involvement of coupling factor B in the H+ channel
            of the mitochondrial H+-ATPase
  JOURNAL   Proc Natl Acad Sci U S A 81 (5), 1371-1374 (1984)
   PUBMED   6143319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083655.1.
            
            On Nov 29, 2004 this sequence version replaced XP_343075.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132297
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..200
                     /product="ATP synthase subunit s, mitochondrial precursor"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase subunit s, mitochondrial; ATP
                     synthase-coupling factor B; Factor B; ATP synthase, H+
                     transporting, mitochondrial F0 complex, subunit s (factor
                     B); mitochondrial ATP synthase regulatory component factor
                     B; distal membrane arm assembly complex 2 like; ATP
                     synthase, H+ transporting, mitochondrial Fo complex,
                     subunit s (factor B); distal membrane arm assembly complex
                     2-like protein"
                     /calculated_mol_wt=20289
     Region          1..61
                     /region_name="N-terminal domain.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
     transit_peptide 1..25
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:P22027; propagated from
                     UniProtKB/Swiss-Prot (Q5XIM4.1)"
                     /calculated_mol_wt=3054
     mat_peptide     26..200
                     /product="ATP synthase subunit s, mitochondrial.
                     /id=PRO_0000002541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
                     /calculated_mol_wt=20289
     Region          62..87
                     /region_name="LRR 1.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
     Region          88..116
                     /region_name="LRR 2.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
     Region          97..>166
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          111..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          117..141
                     /region_name="LRR 3.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
     Region          140..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          142..173
                     /region_name="LRR 4.
                     /evidence=ECO:0000250|UniProtKB:P22027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIM4.1)"
     CDS             1..200
                     /gene="Dmac2l"
                     /gene_synonym="Atp5s"
                     /coded_by="NM_001007749.1:316..918"
                     /db_xref="GeneID:362749"
                     /db_xref="RGD:1359208"
ORIGIN      
        1 mmmfgkisrq lfslkkipws cdsryfwewl ntvfnkvdye rikdvgpdra asewllrcga
       61 kvrycghqkw lqdynklpgg svdrykiqai datdscimdi gfdhlvgleh veritlcrch
      121 yiednclqrl sqlenlrksl leleiiacgn vtdngvialr hfknlkylfl sdlpgikdke
      181 ylaevftkal pslelklnlk
//
LOCUS       NP_001013086             277 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein mL46 [Rattus norvegicus].
ACCESSION   NP_001013086 XP_214972
VERSION     NP_001013086.1
DBSOURCE    REFSEQ: accession NM_001013068.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086407.1.
            
            On Apr 20, 2005 this sequence version replaced XP_214972.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086407.1, EV768008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132296
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..277
                     /product="large ribosomal subunit protein mL46"
                     /note="39S ribosomal protein L46, mitochondrial; L46mt;
                     MRP-L46"
                     /calculated_mol_wt=31542
     Region          43..139
                     /region_name="MRP-L46"
                     /note="39S mitochondrial ribosomal protein L46; pfam11788"
                     /db_xref="CDD:432074"
     Region          134..273
                     /region_name="NUDIX_MRP_L46"
                     /note="Mitochondrial ribosomal protein L46; cd04661"
                     /db_xref="CDD:467546"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2W6; propagated from
                     UniProtKB/Swiss-Prot (Q5RK00.1)"
     CDS             1..277
                     /gene="Mrpl46"
                     /coded_by="NM_001013068.1:28..861"
                     /db_xref="GeneID:293054"
                     /db_xref="RGD:1309123"
ORIGIN      
        1 maapigrtll gvakgwrqld rlwagssrgl sleaapsssr spwrlsgalc lqrpplitkp
       61 ltplqeemag llqqvevers lysdhelral deaqrlakkk adlydeeqdq dvtlaqdled
      121 mweqeflqfr pgareteadk kndrtslhrk ldrnlillvr eklgdqdlwm lpqvewqpge
      181 tlrgtaeril atlsennmea kflgnapcgh ykfkfpkair tesdlgvkvf ffkallltgd
      241 fvqtgkkgrh vwaskeelgd ylqpkylaqv rrflldl
//
LOCUS       NP_001020572             656 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear pore complex protein Nup85 [Rattus norvegicus].
ACCESSION   NP_001020572 XP_213516
VERSION     NP_001020572.1
DBSOURCE    REFSEQ: accession NM_001025401.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Braun,D.A., Lovric,S., Schapiro,D., Schneider,R., Marquez,J.,
            Asif,M., Hussain,M.S., Daga,A., Widmeier,E., Rao,J., Ashraf,S.,
            Tan,W., Lusk,C.P., Kolb,A., Jobst-Schwan,T., Schmidt,J.M.,
            Hoogstraten,C.A., Eddy,K., Kitzler,T.M., Shril,S., Moawia,A.,
            Schrage,K., Khayyat,A.I.A., Lawson,J.A., Gee,H.Y., Warejko,J.K.,
            Hermle,T., Majmundar,A.J., Hugo,H., Budde,B., Motameny,S.,
            Altmuller,J., Noegel,A.A., Fathy,H.M., Gale,D.P., Waseem,S.S.,
            Khan,A., Kerecuk,L., Hashmi,S., Mohebbi,N., Ettenger,R.,
            Serdaroglu,E., Alhasan,K.A., Hashem,M., Goncalves,S., Ariceta,G.,
            Ubetagoyena,M., Antonin,W., Baig,S.M., Alkuraya,F.S., Shen,Q.,
            Xu,H., Antignac,C., Lifton,R.P., Mane,S., Nurnberg,P., Khokha,M.K.
            and Hildebrandt,F.
  TITLE     Mutations in multiple components of the nuclear pore complex cause
            nephrotic syndrome
  JOURNAL   J Clin Invest 128 (10), 4313-4328 (2018)
   PUBMED   30179222
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Bonnet,A. and Palancade,B.
  TITLE     Regulation of mRNA trafficking by nuclear pore complexes
  JOURNAL   Genes (Basel) 5 (3), 767-791 (2014)
   PUBMED   25184662
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Glavy,J.S., Krutchinsky,A.N., Cristea,I.M., Berke,I.C., Boehmer,T.,
            Blobel,G. and Chait,B.T.
  TITLE     Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
            subcomplex
  JOURNAL   Proc Natl Acad Sci U S A 104 (10), 3811-3816 (2007)
   PUBMED   17360435
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Terashima,Y., Onai,N., Murai,M., Enomoto,M., Poonpiriya,V.,
            Hamada,T., Motomura,K., Suwa,M., Ezaki,T., Haga,T., Kanegasaki,S.
            and Matsushima,K.
  TITLE     Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated
            monocyte chemotaxis
  JOURNAL   Nat Immunol 6 (8), 827-835 (2005)
   PUBMED   15995708
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Loiodice,I., Alves,A., Rabut,G., Van Overbeek,M., Ellenberg,J.,
            Sibarita,J.B. and Doye,V.
  TITLE     The entire Nup107-160 complex, including three new members, is
            targeted as one entity to kinetochores in mitosis
  JOURNAL   Mol Biol Cell 15 (7), 3333-3344 (2004)
   PUBMED   15146057
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Harel,A., Orjalo,A.V., Vincent,T., Lachish-Zalait,A., Vasu,S.,
            Shah,S., Zimmerman,E., Elbaum,M. and Forbes,D.J.
  TITLE     Removal of a single pore subcomplex results in vertebrate nuclei
            devoid of nuclear pores
  JOURNAL   Mol Cell 11 (4), 853-864 (2003)
   PUBMED   12718872
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098031.1.
            
            On Jul 15, 2005 this sequence version replaced XP_213516.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098031.1, SRR8487230.25280.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..656
                     /product="nuclear pore complex protein Nup85"
                     /note="nucleoporin NUP85; pericentrin-1; 85 kDa
                     nucleoporin; nucleoporin 85kDa"
                     /calculated_mol_wt=74751
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW27; propagated from
                     UniProtKB/Swiss-Prot (Q4QQS8.1)"
     Region          53..606
                     /region_name="Nucleopor_Nup85"
                     /note="Nup85 Nucleoporin; pfam07575"
                     /db_xref="CDD:400113"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R480; propagated from
                     UniProtKB/Swiss-Prot (Q4QQS8.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW27; propagated from
                     UniProtKB/Swiss-Prot (Q4QQS8.1)"
     CDS             1..656
                     /gene="Nup85"
                     /gene_synonym="Pcnt1"
                     /coded_by="NM_001025401.1:24..1994"
                     /db_xref="GeneID:287830"
                     /db_xref="RGD:1311942"
ORIGIN      
        1 meeldcepav twipgvnskk kqmcfdwgpg emllcetsfn ktdksekvps cpfiyiirkd
       61 vdvysqilrk lfneshgifv glqrleeels gksrkaqlvr vsknyrsvir acmeemhqva
      121 iaakdpasgr qfssqvsils ameliwnlce ilfievapag plllhlldwv rlhvcevdsl
      181 sadvlgsdhp skhesfwnlv tvlvlqgrld earqmlskea daspssagmc rvlgdlmrtm
      241 pilspgntqt ltelelkwqh wreecerhlq dntfaanphl eslckimlgd eatlleqkel
      301 msnwyhflvt rllysnptvk ptdlhlyaqs sldmflgges spepldnilm aafefdihqv
      361 ikecsialsn wwfvahltdl ldhcrllqsh nlyfgsnmre fllleyasgl fahhslwqlg
      421 vdyfdycpel grvslelhie riplnteqka lkvlriceqr qmteqvgsic kilamkavrn
      481 nrlgsalsws irakdaafat lvsdrflrdy cergcfsdld lidnlgpamm lsdrltflgk
      541 yrefhrlyge krfgdaasll lslmtsqiap rsfwmtlltd alplleqkqv ifsaeqtyel
      601 mrcledlasr rpecgepdaq rlqdddiett kvemlrlala rnlaraiire gslegs
//
LOCUS       NP_001029204             198 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily C member 12 [Rattus norvegicus].
ACCESSION   NP_001029204
VERSION     NP_001029204.1
DBSOURCE    REFSEQ: accession NM_001034032.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Choi,J., Djebbar,S., Fournier,A. and Labrie,C.
  TITLE     The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by
            endoplasmic reticulum stress
  JOURNAL   Cell Stress Chaperones 19 (3), 439-446 (2014)
   PUBMED   24122553
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Lee,J., Hahn,Y., Yun,J.H., Mita,K. and Chung,J.H.
  TITLE     Characterization of JDP genes, an evolutionarily conserved J
            domain-only protein family, from human and moths
  JOURNAL   Biochim Biophys Acta 1491 (1-3), 355-363 (2000)
   PUBMED   10760603
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100072.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100072.1, CF977760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p11"
     Protein         1..198
                     /product="dnaJ homolog subfamily C member 12"
                     /note="J domain protein 1; j domain-containing protein 1;
                     DnaJ (Hsp40) homolog, subfamily C, member 12"
                     /calculated_mol_wt=22847
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKB3; propagated from
                     UniProtKB/Swiss-Prot (Q925T0.1)"
     Region          14..76
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(42..44,53,56..57,60..61)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          121..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925T0.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKB3; propagated from
                     UniProtKB/Swiss-Prot (Q925T0.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R022; propagated from
                     UniProtKB/Swiss-Prot (Q925T0.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R022; propagated from
                     UniProtKB/Swiss-Prot (Q925T0.1)"
     CDS             1..198
                     /gene="Dnajc12"
                     /gene_synonym="Jdp1"
                     /coded_by="NM_001034032.1:36..632"
                     /db_xref="GeneID:619393"
                     /db_xref="RGD:1591898"
ORIGIN      
        1 mdailnyrpe gsedyytllg cdelssveqi laefkvrale chpdkhpens kavetfqklq
       61 kakeilsnae srarydhwrr sqmsmsfeqw ealadsvkts mhwavrskkd lmlegseqty
      121 tntaqnkers eqretkqgdp dstpekmmqk esespekgis pqnpdspgls dwncghlhfr
      181 wsgdtpsell rkfrnyei
//
LOCUS       NP_001073178             331 aa            linear   ROD 27-APR-2025
DEFINITION  N-arachidonyl glycine receptor [Rattus norvegicus].
ACCESSION   NP_001073178 XP_001053946
VERSION     NP_001073178.1
DBSOURCE    REFSEQ: accession NM_001079710.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Narasimhan,M., Mahimainathan,L., Reddy,P.H. and Benamar,K.
  TITLE     GPR18-NAGly system in periaqueductal gray and chronic neuropathic
            pain
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (12), 165974 (2020)
   PUBMED   32949767
  REMARK    GeneRIF: GPR18-NAGly system in periaqueductal gray and chronic
            neuropathic pain.
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Wrobel,A., Szopa,A., Serefko,A. and Poleszak,E.
  TITLE     A Novel Alternative in the Treatment of Detrusor Overactivity? In
            Vivo Activity of O-1602, the Newly Synthesized Agonist of GPR55 and
            GPR18 Cannabinoid Receptors
  JOURNAL   Molecules 25 (6), 1384 (2020)
   PUBMED   32197469
  REMARK    GeneRIF: A Novel Alternative in the Treatment of Detrusor
            Overactivity? In Vivo Activity of O-1602, the Newly Synthesized
            Agonist of GPR55 and GPR18 Cannabinoid Receptors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Wang,X., Sumida,H. and Cyster,J.G.
  TITLE     GPR18 is required for a normal CD8alphaalpha intestinal
            intraepithelial lymphocyte compartment
  JOURNAL   J Exp Med 211 (12), 2351-2359 (2014)
   PUBMED   25348153
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Penumarti,A. and Abdel-Rahman,A.A.
  TITLE     The novel endocannabinoid receptor GPR18 is expressed in the
            rostral ventrolateral medulla and exerts tonic restraining
            influence on blood pressure
  JOURNAL   J Pharmacol Exp Ther 349 (1), 29-38 (2014)
   PUBMED   24431468
  REMARK    GeneRIF: The role of a novel cannabinoid receptor GPR18, espressed
            in the rostral ventrolateral medulla, in central blood pressure
            control.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128782.1.
            
            On Dec 11, 2006 this sequence version replaced XP_001053946.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128782.1, CO570572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q25"
     Protein         1..331
                     /product="N-arachidonyl glycine receptor"
                     /note="NAGly receptor"
                     /calculated_mol_wt=37425
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          23..297
                     /region_name="7tmA_NAGly_R_GPR18"
                     /note="N-arachidonyl glycine receptor, GPR18, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15166"
                     /db_xref="CDD:320294"
     Region          23..50
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320294"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          57..82
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320294"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Site            order(78,81..82,94..99,101..102,105,150,152..156,184,
                     187..189,191..193,195..196,245,248..249,251..252,255,
                     264..265,267..269,272,275..276)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320294"
     Region          94..124
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320294"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          136..158
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320294"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          184..213
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320294"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A1A5S3.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          225..255
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320294"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Region          265..290
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320294"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5S3.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1Z6; propagated from
                     UniProtKB/Swiss-Prot (A1A5S3.1)"
     CDS             1..331
                     /gene="Gpr18"
                     /coded_by="NM_001079710.1:222..1217"
                     /db_xref="GeneID:679957"
                     /db_xref="RGD:1304889"
ORIGIN      
        1 maipsnrdql alsngshpee ykiaalvfys cifligllvn vtalwvfsct tkkrttvtiy
       61 mmnvalldlv filslpfrmf yyakgewpfg dyfchilgal vvfypslalw llalisadry
      121 maivqpkyak elkntgkavl acvgvwimtl tttvplllld edpdkasspa tclkisdiih
      181 lkavnvlnft rliffflipl fimigcyvvi ihsllrgqts klkpkvkeks iriivtlllq
      241 vlacfvpfhi cfallmlqge ensyspwgaf ttflmnlstc ldvvlyyivs kqfqarvisv
      301 mlyrnylrsv rrksvrsgsl rslsnmnsem l
//
LOCUS       NP_001012763             237 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 22 [Rattus norvegicus].
ACCESSION   NP_001012763 NP_598263 XP_346722
VERSION     NP_001012763.1
DBSOURCE    REFSEQ: accession NM_001012745.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Lee,S.K., Kim,Y.S., Lee,S.S., Lee,Y.J., Song,I.S., Park,S.C.,
            Kozak,C. and Yamada,Y.
  TITLE     Molecular cloning, chromosomal mapping, and characteristic
            expression in tooth organ of rat and mouse Krox-25
  JOURNAL   Genomics 83 (2), 243-253 (2004)
   PUBMED   14706453
  REMARK    GeneRIF: analysis revealed an intense expression of Krox-25 mRNA in
            rat and mouse teeth; results suggest that Krox-25 plays an
            important role as a transcription factor for the
            cytodifferentiation and amelogenesis of enamel epithelium.
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Teo,W., Chen,H., Poon,T. and Ganss,B.
  TITLE     Developmental expression pattern and DNA-binding properties of the
            zinc finger transcription factor Krox-26
  JOURNAL   Connect Tissue Res 44 Suppl 1, 161-166 (2003)
   PUBMED   12952191
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090354.1.
            
            On or before Sep 27, 2007 this sequence version replaced
            NP_598263.1, XP_346722.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090354.1, CA511320.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..237
                     /product="zinc finger protein 22"
                     /note="krueppel-type zinc finger protein Krox-25; zinc
                     finger protein 22 (KOX 15)"
                     /calculated_mol_wt=27155
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERU2.2)"
     Site            18
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERU3; propagated from
                     UniProtKB/Swiss-Prot (Q9ERU2.2)"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERU3; propagated from
                     UniProtKB/Swiss-Prot (Q9ERU2.2)"
     Region          <53..192
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          57..77
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          85..105
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          113..133
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(118,120,122,124..125,128..129,132,146,148,152..153,
                     156..157,160,174,176,178,180..181,184..185,188)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          141..161
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          169..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          188..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERU2.2)"
     CDS             1..237
                     /gene="Zfp422"
                     /gene_synonym="Kox15; Krox-25; Znf22"
                     /coded_by="NM_001012745.1:300..1013"
                     /db_xref="GeneID:360389"
                     /db_xref="RGD:620229"
ORIGIN      
        1 mrlgkpkggi srsasqgkty eskrktarqr qkwgvairfd sglsrrrrnv dekpykctkc
       61 sksfsqsstl fqhkkihtgk kshkcadcgk sffqssnliq hrrihtgekp ykcdecgerf
      121 kqssnliqhq rihtgekpyc cdecgrcfsq sshliqhqrt htgekpyqce ecdkcfsqss
      181 hlrqhmkvhk ekkshkrgkn arakthpvsw krgkgrkava glrqvkgaas glfkkkk
//
LOCUS       NP_001005537             557 aa            linear   ROD 27-APR-2025
DEFINITION  protein Red [Rattus norvegicus].
ACCESSION   NP_001005537 XP_214579
VERSION     NP_001005537.1
DBSOURCE    REFSEQ: accession NM_001005537.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Hu,L., Yang,F., Liu,X., Xu,D. and Dai,W.
  TITLE     Nuclear protein IK undergoes dynamic subcellular translocation and
            forms unique nuclear bodies during the cell cycle
  JOURNAL   Biomark Res 1 (1), 11 (2013)
   PUBMED   24252166
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Yeh,P.C., Yeh,C.C., Chen,Y.C. and Juang,Y.L.
  TITLE     RED, a spindle pole-associated protein, is required for kinetochore
            localization of MAD1, mitotic progression, and activation of the
            spindle assembly checkpoint
  JOURNAL   J Biol Chem 287 (15), 11704-11716 (2012)
   PUBMED   22351768
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Krief,P., Augery-Bourget,Y., Plaisance,S., Merck,M.F., Assier,E.,
            Tanchou,V., Billard,M., Boucheix,C., Jasmin,C. and Azzarone,B.
  TITLE     A new cytokine (IK) down-regulating HLA class II: monoclonal
            antibodies, cloning and chromosome localization
  JOURNAL   Oncogene 9 (12), 3449-3456 (1994)
   PUBMED   7970704
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081870.1.
            
            On Oct 8, 2004 this sequence version replaced XP_214579.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081870.1, FQ212525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..557
                     /product="protein Red"
                     /note="Ik factor; chondrosarcoma-associated protein 2;
                     cytokine IK; IK cytokine, down-regulator of HLA II"
                     /calculated_mol_wt=65457
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG8.1)"
     Region          84..295
                     /region_name="RED_N"
                     /note="RED-like protein N-terminal region; pfam07808"
                     /db_xref="CDD:462273"
     Site            98
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1M8; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Region          181..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG8.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Region          294..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG8.1)"
     Region          342..375
                     /region_name="17 X 2 AA tandem repeats of R-[ED]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG8.1)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Region          445..549
                     /region_name="RED_C"
                     /note="RED-like protein C-terminal region; pfam07807"
                     /db_xref="CDD:462272"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13123; propagated from
                     UniProtKB/Swiss-Prot (Q66HG8.1)"
     CDS             1..557
                     /gene="Ik"
                     /gene_synonym="CSA2; RED"
                     /coded_by="NM_001005537.1:123..1796"
                     /db_xref="GeneID:291659"
                     /db_xref="RGD:1359352"
ORIGIN      
        1 mperdsepfs nplapdghdv ddphsfhqsk ltnedfrkll mtpraaptsa ppsksrhhem
       61 preynededp aarrrkkksy yaklrqqeie rerelaekyr drakerrdgv nkdyeeteli
      121 sttanyravg ptaeadksaa ekrrqliqes kflggdmeht hlvkgldfal lqkvraeias
      181 kekeeeelme kpqketkkde dpenkiefkt rlgrnvyrml fksksyerne lflpgrmayv
      241 vdlddeyadt dipttlirsk adcptmeaqt tlttndivis kltqilsylr qgtrnkklkk
      301 kdkgkleekk ppeadmnife digdyvpstt ktprdkerer yrererdrer drdrerdrer
      361 drerererdr erereeekkr hsyfekpkvd depmdvdkgp gsakeliksi nekfagsagw
      421 egteslkkpe dkkqlgdffg msnsyaecyp atmddmavds deevdyskmd qgnkkgplgr
      481 wdfdtqeeys eymnnkealp kaafqygikm segrktrrfk etndkaeldr qwkkisaiie
      541 krkkmeadgv evkrpky
//
LOCUS       NP_001014138             271 aa            linear   ROD 27-APR-2025
DEFINITION  jmjC domain-containing protein 8 precursor [Rattus norvegicus].
ACCESSION   NP_001014138 XP_340773
VERSION     NP_001014138.1
DBSOURCE    REFSEQ: accession NM_001014116.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Yeo,K.S., Tan,M.C., Lim,Y.Y. and Ea,C.K.
  TITLE     JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
  JOURNAL   Sci Rep 7 (1), 15407 (2017)
   PUBMED   29133832
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Yeo,K.S., Tan,M.C., Wong,W.Y., Loh,S.W., Lam,Y.L., Tan,C.L.,
            Lim,Y.Y. and Ea,C.K.
  TITLE     JMJD8 is a positive regulator of TNF-induced NF-kappaB signaling
  JOURNAL   Sci Rep 6, 34125 (2016)
   PUBMED   27671354
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Boeckel,J.N., Derlet,A., Glaser,S.F., Luczak,A., Lucas,T.,
            Heumuller,A.W., Kruger,M., Zehendner,C.M., Kaluza,D.,
            Doddaballapur,A., Ohtani,K., Treguer,K. and Dimmeler,S.
  TITLE     JMJD8 Regulates Angiogenic Sprouting and Cellular Metabolism by
            Interacting With Pyruvate Kinase M2 in Endothelial Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 36 (7), 1425-1433 (2016)
   PUBMED   27199445
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079205.1.
            
            On Apr 20, 2005 this sequence version replaced XP_340773.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079205.1, FQ110973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..271
                     /product="jmjC domain-containing protein 8 precursor"
                     /note="jmjC domain-containing protein 8; jumonji
                     domain-containing protein 8"
                     /calculated_mol_wt=27724
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3045
     Region          61..255
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     CDS             1..271
                     /gene="Jmjd8"
                     /gene_synonym="RGD1307381"
                     /coded_by="NM_001014116.1:222..1037"
                     /db_xref="GeneID:360498"
                     /db_xref="RGD:1307381"
ORIGIN      
        1 mlmaaagrfg llllivlwtm vtvvlpasge ggwkqsrlgt eaavmeeerc tverrahlty
       61 sefmqhyafl kpvilqgltd nskfralcsr enllasfgdn vvrlstanty syqkvdlpfq
      121 eyveqllhpq dpeslgndtl yffgdnnfte waplfqhyrp ppfrllgttp aysfgiagag
      181 sgvpfhwhgp gfseviygrk rwflyppekt pefhpnkttl awlleiypsl apsarplect
      241 iqagealyfp drwwhatlnl dtsvfistfl g
//
LOCUS       NP_001100895            1548 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear factor of activated T-cells 5 [Rattus norvegicus].
ACCESSION   NP_001100895 XP_001076581 XP_003751918 XP_226436
VERSION     NP_001100895.1
DBSOURCE    REFSEQ: accession NM_001107425.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1548)
  AUTHORS   Wang,M., Zhao,M., Xu,S., Zheng,Z., Zhang,J., Pan,W., Yin,Z.,
            Liu,J., Wei,C., Wan,J. and Xu,Y.
  TITLE     TRPA1 deficiency attenuates cardiac fibrosis via regulating
            GRK5/NFAT signaling in diabetic rats
  JOURNAL   Biochem Pharmacol 214, 115671 (2023)
   PUBMED   37380112
  REMARK    GeneRIF: TRPA1 deficiency attenuates cardiac fibrosis via
            regulating GRK5/NFAT signaling in diabetic rats.
REFERENCE   2  (residues 1 to 1548)
  AUTHORS   Xia,X., Niu,H., Ma,Y., Qu,B., He,M., Yu,K., Wang,E., Zhang,L.,
            Gu,J. and Liu,G.
  TITLE     LncRNA CCAT1 Protects Astrocytes Against OGD/R-Induced Damage by
            Targeting the miR-218/NFAT5-Signaling Axis
  JOURNAL   Cell Mol Neurobiol 40 (8), 1383-1393 (2020)
   PUBMED   32239388
  REMARK    GeneRIF: LncRNA CCAT1 Protects Astrocytes Against OGD/R-Induced
            Damage by Targeting the miR-218/NFAT5-Signaling Axis.
REFERENCE   3  (residues 1 to 1548)
  AUTHORS   Lin,X.C., Pan,M., Zhu,L.P., Sun,Q., Zhou,Z.S., Li,C.C. and
            Zhang,G.G.
  TITLE     NFAT5 promotes arteriogenesis via MCP-1-dependent monocyte
            recruitment
  JOURNAL   J Cell Mol Med 24 (2), 2052-2063 (2020)
   PUBMED   31883300
  REMARK    GeneRIF: NFAT5 promotes arteriogenesis via MCP-1-dependent monocyte
            recruitment.
REFERENCE   4  (residues 1 to 1548)
  AUTHORS   Ma,R., Xu,Y., Zhou,H., Zhang,D., Yao,D., Song,L. and Liu,Y.
  TITLE     Participation of the AngII/TRPC6/NFAT axis in the pathogenesis of
            podocyte injury in rats with type 2 diabetes
  JOURNAL   Mol Med Rep 19 (3), 2421-2430 (2019)
   PUBMED   30664212
  REMARK    GeneRIF: the present results suggested that the AngII/TRPC6/NFAT
            axis may be a crucial signaling pathway in podocytes that is
            necessary for maintaining the integrity of the glomerular
            filtration barrier
REFERENCE   5  (residues 1 to 1548)
  AUTHORS   Fahling,M., Paliege,A., Jonsson,S., Becirovic-Agic,M.,
            Melville,J.M., Skogstrand,T. and Hultstrom,M.
  TITLE     NFAT5 regulates renal gene expression in response to angiotensin II
            through Annexin-A2-mediated posttranscriptional regulation in
            hypertensive rats
  JOURNAL   Am J Physiol Renal Physiol 316 (1), F101-F112 (2019)
   PUBMED   30332317
  REMARK    GeneRIF: ANGII increases Annexin-A2 nucleic acid-binding activity
            and elevates protein levels of the NFAT5 transcription factor in
            kidneys of hypertensive rats.
REFERENCE   6  (residues 1 to 1548)
  AUTHORS   Wilkins,B.J., De Windt,L.J., Bueno,O.F., Braz,J.C., Glascock,B.J.,
            Kimball,T.F. and Molkentin,J.D.
  TITLE     Targeted disruption of NFATc3, but not NFATc4, reveals an intrinsic
            defect in calcineurin-mediated cardiac hypertrophic growth
  JOURNAL   Mol Cell Biol 22 (21), 7603-7613 (2002)
   PUBMED   12370307
REFERENCE   7  (residues 1 to 1548)
  AUTHORS   Maouyo,D., Kim,J.Y., Lee,S.D., Wu,Y., Woo,S.K. and Kwon,H.M.
  TITLE     Mouse TonEBP-NFAT5: expression in early development and alternative
            splicing
  JOURNAL   Am J Physiol Renal Physiol 282 (5), F802-F809 (2002)
   PUBMED   11934689
REFERENCE   8  (residues 1 to 1548)
  AUTHORS   Stroud,J.C., Lopez-Rodriguez,C., Rao,A. and Chen,L.
  TITLE     Structure of a TonEBP-DNA complex reveals DNA encircled by a
            transcription factor
  JOURNAL   Nat Struct Biol 9 (2), 90-94 (2002)
   PUBMED   11780147
REFERENCE   9  (residues 1 to 1548)
  AUTHORS   Lopez-Rodriguez,C., Aramburu,J., Jin,L., Rakeman,A.S., Michino,M.
            and Rao,A.
  TITLE     Bridging the NFAT and NF-kappaB families: NFAT5 dimerization
            regulates cytokine gene transcription in response to osmotic stress
  JOURNAL   Immunity 15 (1), 47-58 (2001)
   PUBMED   11485737
REFERENCE   10 (residues 1 to 1548)
  AUTHORS   Pan,S., Tsuruta,R., Masuda,E.S., Imamura,R., Bazan,F., Arai,K.,
            Arai,N. and Miyatake,S.
  TITLE     NFATz: a novel rel similarity domain containing protein
  JOURNAL   Biochem Biophys Res Commun 272 (3), 765-776 (2000)
   PUBMED   10860829
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_003751918.2, XP_001076581.1, XP_226436.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1548
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..1548
                     /product="nuclear factor of activated T-cells 5"
                     /note="T-cell transcription factor NFAT5; nuclear factor
                     of activated T-cells 5, tonicity-responsive"
                     /calculated_mol_wt=167077
     Region          54..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94916; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV30; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          141..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94916; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:O94916; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94916; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          192..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          258..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          297..457
                     /region_name="RHD-n_TonEBP"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of tonicity-responsive enhancer binding protein
                     (TonEBP); cd07882"
                     /db_xref="CDD:143642"
     Site            order(310,313,315..320,406,408..409,424,426,457)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143642"
     Region          461..560
                     /region_name="IPT_NFAT"
                     /note="IPT domain of the NFAT family of transcription
                     factors. NFAT transcription complexes are a target of
                     calcineurin, a calcium dependent phosphatase, and activate
                     genes mainly involved in cell-cell-interaction; cd01178"
                     /db_xref="CDD:238583"
     Site            order(485,548)
                     /site_type="DNA binding"
                     /note="DNA binding sites [nucleotide binding]"
                     /db_xref="CDD:238583"
     Site            577
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94916; propagated from
                     UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          659..682
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          750..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          851..892
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          970..1010
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          1097..1127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     Region          1257..1388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGB1.1)"
     CDS             1..1548
                     /gene="Nfat5"
                     /gene_synonym="NF-AT5; Nfat; TonEBP"
                     /coded_by="NM_001107425.1:807..5453"
                     /db_xref="GeneID:307820"
                     /db_xref="RGD:1309142"
ORIGIN      
        1 mpsdfislls adldlespks lysrdslklh psqnfhragl leesvydllp kelqlpppre
       61 tsaasmsqts ggeagspppa vvaadassap sssmggacss fttsssptiy stsvtdskam
      121 qvescssavg vsnrgvsekq ltgntvqqhp stpkrhtvly ispppedlld nsrmscqdeg
      181 cgleseqscs mwmedspsnf snmstssynd ntevprksrk rnpkqrpgvk rrdceesnmd
      241 ifdadsakap hyvlsqlttd nkgnskagng tldsqkgtgv kkspmlcgqy pvksegkelk
      301 ivvqpetqhr aryltegsrg svkdrtqqgf ptvkleghne pvvlqvfvgn dsgrvkphgf
      361 yqacrvtgrn ttpckevdie gttvievgld pssnmtlavd cvgilklrna dvearigiag
      421 skkkstrarl vfrvnitrkd gstltlqtps spilctqpag vpeilkkslh scsvkgeeev
      481 fligknflkg tkvifqenvs denswkseae idmelfhqnh livkvppyhd qhitlpvsvg
      541 iyvvtnagrs hdvqpftytp dpaagalsvn vkkeisspar pcsfeealka mkttgcnvdk
      601 vtilpnalit plisssmikt edvtpmevts ekrsspifqt tktvgstqqt letisniagn
      661 asfsspsssh lspenenqqq lqpkaynpet lttiqtqdis qpgtfpavsa ssqlpssdal
      721 lqqaaqfqtr daqsrdtmqs dsvvnlsqlt eapqqqqspl qeqaqipsni fpspnsvsql
      781 qstiqqlqag sftgstasgs ngsvdlvqqv leaqqqlssv lfstpdgnen vqeqlnadif
      841 qvsqiqnsvs pgmfsstesa vhtrpdnllp gradsvhqqt entlssqqqq qqqqqqqqqq
      901 qviessaamv memqqsicqa aaqiqselfp saasangslq qspvyqqpsh mmsalptsed
      961 mqmqcelfss ppavsgnets ttttpqvatp gstmfqppns gdgeetgaqa kqiqssvfqt
     1021 mvqmqhsgds qpqvnlfsst knimsvqsng tqqqgnslfq qgsemlslqs gsflqqsshs
     1081 qaqlfhpqnp iadaqslsqe tqgpmfhsan pivhsqtsta sseqlqpsmf hsqstiavlq
     1141 gssvpqdqqs pniylsqssi snlqtntvaq eeqisffsaq nsisplqsts nteqqaafqq
     1201 qppishiqtp llsqeqaqps qqglfqpqva lgslpanpmp qnqqgpifqt qrpivgmqsn
     1261 spsqeqqqqq qqqqqqqqqq qqqsilfsnq namatmasqk qpppnmifsp nqnpmasqeq
     1321 qnqsifhqqs nmapmnqeqq pmqfqnqptv sslqnpgptp sespqtslfh sspqiqlvqg
     1381 spssqeqqvt lflspasmsa lqtsinqpdm qqsplyspqn nipgiqgsts spqpqaalfh
     1441 nttggtinql qnspgssqqt sgmflfgiqn ncsqlltsgp atlpeqlmai nqpgqpqneg
     1501 qssvttllsq qmpesaplas svnnsqnmek idllvslqsq gnnltgsf
//
LOCUS       NP_001030007             877 aa            linear   ROD 27-APR-2025
DEFINITION  KAT8 regulatory NSL complex subunit 3 [Rattus norvegicus].
ACCESSION   NP_001030007 XP_237086
VERSION     NP_001030007.1
DBSOURCE    REFSEQ: accession NM_001034835.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105865.1.
            
            On Oct 18, 2005 this sequence version replaced XP_237086.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105865.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..877
                     /product="KAT8 regulatory NSL complex subunit 3"
                     /note="NSL complex protein NSL3; non-specific lethal 3
                     homolog"
                     /calculated_mol_wt=92904
     Region          <323..472
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
     Region          478..561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR73.1)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2N6; propagated from
                     UniProtKB/Swiss-Prot (Q3KR73.1)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2RSY1; propagated from
                     UniProtKB/Swiss-Prot (Q3KR73.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2N6; propagated from
                     UniProtKB/Swiss-Prot (Q3KR73.1)"
     Region          599..618
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR73.1)"
     Region          670..691
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR73.1)"
     Region          735..757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR73.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2N6; propagated from
                     UniProtKB/Swiss-Prot (Q3KR73.1)"
     Region          843..877
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KR73.1)"
     CDS             1..877
                     /gene="Kansl3"
                     /gene_synonym="RGD1309220"
                     /coded_by="NM_001034835.1:70..2703"
                     /db_xref="GeneID:316328"
                     /db_xref="RGD:1309220"
ORIGIN      
        1 mahrggerdf qtsarrmgts llfqlsvher eldlvfldhs yakpwsahpd assarptrml
       61 fvtprrqqen tiesdvpidv etvtatpapl ydnqkarsvm necerhvifa rtdadapppp
      121 edweehvnrt gwtvaqnklf nkilkalqsd rlarlanega cnepvlrrva vdkcarrvrq
      181 alasvswdtk liqwlhttlv etlslpmlaa yldalqtlkg kiptlidrml vssntktgaa
      241 gaealslllk rpwdpavgvl shnkpsklpg spliliassg psssvfpasr rhrfwqsqls
      301 clgkvipvat hllnngsgvg vlqclehmtg avrskvleih shfphkpiil igwstgalva
      361 chvsvmeyvt avvclgfpll tvdgprgdvd dplldmktpv lfvigqnslq chpeamedfr
      421 ekiraenslv vvggaddnlr iskakkkseg ltqsmvdrci qdeivdfltg vltraeghvg
      481 seprdqdaek kkkprdvarr dlafeiperg srpaspaarl ptspsgsedl ssvsssptss
      541 pktkgttvts aqkssqigts qllrrhvqrt davlthrqaq vpissepvee vekeelrvql
      601 krhhpssplp gakpskrpki kvslisqgdt vggpctlsqg gtpeaaggkp itmtlgasag
      661 akeltglltt aksssseggv tasaapsvas snatpnaiht lqsrlvatsp gsslpgaasa
      721 ssllqglsfs lqdisskttg lpgspspgpa pqatsvklpt pmqslgaitt gtstivrtip
      781 vattlsslaa tpggkptaih qlltngglak lasslpglaq isnqasglkv pttitltlrg
      841 qpsrittlsp mgsgaaasee pnsqmlpsss qrlppap
//
LOCUS       NP_001017514             383 aa            linear   ROD 27-APR-2025
DEFINITION  izumo sperm-egg fusion protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001017514 XP_574449
VERSION     NP_001017514.1
DBSOURCE    REFSEQ: accession NM_001017514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Lai,X., Liu,R., Li,M., Fan,Y., Li,H., Han,G., Guo,R., Ma,H., Su,H.
            and Xing,W.
  TITLE     Participation of WD repeat-containing protein 54 (WDR54) in rat
            sperm-oocyte fusion through interaction with both IZUMO1 and JUNO
  JOURNAL   Theriogenology 214, 286-297 (2024)
   PUBMED   37951137
  REMARK    GeneRIF: Participation of WD repeat-containing protein 54 (WDR54)
            in rat sperm-oocyte fusion through interaction with both IZUMO1 and
            JUNO.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Matsumura,T., Noda,T., Satouh,Y., Morohoshi,A., Yuri,S., Ogawa,M.,
            Lu,Y., Isotani,A. and Ikawa,M.
  TITLE     Sperm IZUMO1 Is Required for Binding Preceding Fusion With Oolemma
            in Mice and Rats
  JOURNAL   Front Cell Dev Biol 9, 810118 (2022)
   PUBMED   35096839
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Young,S.A., Miyata,H., Satouh,Y., Muto,M., Larsen,M.R.,
            Aitken,R.J., Baker,M.A. and Ikawa,M.
  TITLE     CRISPR/Cas9-mediated mutation revealed cytoplasmic tail is
            dispensable for IZUMO1 function and male fertility
  JOURNAL   Reproduction 152 (6), 665-672 (2016)
   PUBMED   27624483
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Ohto,U., Ishida,H., Krayukhina,E., Uchiyama,S., Inoue,N. and
            Shimizu,T.
  TITLE     Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during
            mammalian fertilization
  JOURNAL   Nature 534 (7608), 566-569 (2016)
   PUBMED   27309808
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Bianchi,E., Doe,B., Goulding,D. and Wright,G.J.
  TITLE     Juno is the egg Izumo receptor and is essential for mammalian
            fertilization
  JOURNAL   Nature 508 (7497), 483-487 (2014)
   PUBMED   24739963
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Fujihara,Y., Murakami,M., Inoue,N., Satouh,Y., Kaseda,K., Ikawa,M.
            and Okabe,M.
  TITLE     Sperm equatorial segment protein 1, SPESP1, is required for fully
            fertile sperm in mouse
  JOURNAL   J Cell Sci 123 (Pt 9), 1531-1536 (2010)
   PUBMED   20375058
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Inoue,N., Kasahara,T., Ikawa,M. and Okabe,M.
  TITLE     Identification and disruption of sperm-specific angiotensin
            converting enzyme-3 (ACE3) in mouse
  JOURNAL   PLoS One 5 (4), e10301 (2010)
   PUBMED   20421979
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Ellerman,D.A., Pei,J., Gupta,S., Snell,W.J., Myles,D. and
            Primakoff,P.
  TITLE     Izumo is part of a multiprotein family whose members form large
            complexes on mammalian sperm
  JOURNAL   Mol Reprod Dev 76 (12), 1188-1199 (2009)
   PUBMED   19658160
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Miranda,P.V., Allaire,A., Sosnik,J. and Visconti,P.E.
  TITLE     Localization of low-density detergent-resistant membrane proteins
            in intact and acrosome-reacted mouse sperm
  JOURNAL   Biol Reprod 80 (5), 897-904 (2009)
   PUBMED   19144954
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Inoue,N., Ikawa,M., Isotani,A. and Okabe,M.
  TITLE     The immunoglobulin superfamily protein Izumo is required for sperm
            to fuse with eggs
  JOURNAL   Nature 434 (7030), 234-238 (2005)
   PUBMED   15759005
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079244.1.
            
            On Apr 29, 2005 this sequence version replaced XP_574449.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079244.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..383
                     /product="izumo sperm-egg fusion protein 1 precursor"
                     /note="izumo sperm-egg fusion protein 1; OBF; oocyte
                     binding/fusion factor; sperm-specific protein izumo; izumo
                     sperm-egg fusion 1"
                     /calculated_mol_wt=41355
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
                     /calculated_mol_wt=2242
     mat_peptide     22..383
                     /product="Izumo sperm-egg fusion protein 1.
                     /id=PRO_0000045484"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY06.1)"
                     /calculated_mol_wt=41355
     Region          22..165
                     /region_name="IZUMO"
                     /note="Izumo sperm-egg fusion, Ig domain-associated;
                     pfam15005"
                     /db_xref="CDD:464437"
     Region          148..160
                     /region_name="Important for interaction with IZUMO1R.
                     /evidence=ECO:0000250|UniProtKB:Q8IYV9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY06.1)"
     Region          168..255
                     /region_name="Izumo-Ig"
                     /note="Izumo-like Immunoglobulin domain; pfam16706"
                     /db_xref="CDD:465242"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
     Site            307..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY06.1)"
     Region          335..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY06.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY06.1)"
     CDS             1..383
                     /gene="Izumo1"
                     /coded_by="NM_001017514.1:301..1452"
                     /db_xref="GeneID:499152"
                     /db_xref="RGD:1565454"
ORIGIN      
        1 mglhftllla alanclcpar lciicdpfvv aaiktleqny lpthlapehh edvmkrveqe
       61 vrnfadlpln qntflgvvde dtleqaswsf lkdlkritds dvkgelfvke lfwmlrlqkd
      121 ifatlvarfq kevycpnqcg tmsqtliwcn kcekqmhfcr ksmdcgerqi evhrledmvl
      181 dcqlswhhas egltdysfyr vwgnssetlm skgkepyltk tmvgpedagn yrceldtvna
      241 gpatiiyyhv tvlpprsvee kpppnivtqe eeetpvqviv ptlepepepe piptvthrpe
      301 kklksrllil lilgfvvlva sviasvlhfr ktrvksknsn venktsaaef kseaespqkm
      361 gsrklsqaef htdssdkvee adn
//
LOCUS       NP_001073174             754 aa            linear   ROD 27-APR-2025
DEFINITION  RNA exonuclease 5 [Rattus norvegicus].
ACCESSION   NP_001073174 XP_001075588 XP_001075607 XP_219390
VERSION     NP_001073174.1
DBSOURCE    REFSEQ: accession NM_001079706.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128775.1.
            
            On or before Dec 11, 2006 this sequence version replaced
            XP_219390.4, XP_001075607.1, XP_001075588.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128775.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132303, SAMD00132304
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..754
                     /product="RNA exonuclease 5"
                     /note="putative RNA exonuclease NEF-sp"
                     /calculated_mol_wt=85922
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R7.1)"
     Region          223..371
                     /region_name="REX1_like"
                     /note="DEDDh 3'-5' exonuclease domain of RNA exonuclease
                     1, -3 and similar eukaryotic proteins; cd06145"
                     /db_xref="CDD:99848"
     Site            order(226..229,231,304..305,307..309,357,362)
                     /site_type="active"
                     /db_xref="CDD:99848"
     Site            order(226..229,231,304..305,307..308,357,362)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99848"
     Site            order(226,228,309,357,362)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99848"
     Region          489..559
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          585..655
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..754
                     /gene="Rexo5"
                     /gene_synonym="2610020h08rik; Exnef; RGD1305412"
                     /coded_by="NM_001079706.1:82..2346"
                     /db_xref="GeneID:309036"
                     /db_xref="RGD:1305412"
ORIGIN      
        1 meleeeenpr krketpnsal tteldrpswd vqdpepqakk arlstilftd ncevthrqlc
       61 ellkyailgk stlpkpswcq llhqkqlnnv vvfilkgmsq lhfyrfylef rflrktfrhk
      121 fslppptssf lfdiiglqkk ksargcprtv egplisatlk ssidlqndpi iqkygyknvs
      181 ltrclltkee mktfhfplqg spncenfill kysgfitdss plfgldcevc ltsmgkeltr
      241 islvaeggyc lmdelvkpdf kildyltsfs gitkeilnpv ttklkdvqkl lrellppdav
      301 lvghcldldl rvlkiihpyv idtsllyigk qgrrfkltfl akvilgkdiq cpnklghdgi
      361 edartalelv qyflkygpkk iaefnleala anqeqgnkeg athmrsvlec ldsmgqkllf
      421 ltqdidelss yrncqtvkcs snkevleqar vevplfpfni vqfsfrpfpp lfaeemknnm
      481 ktrwtemsti yagpfskdcn vgslkkvfss lgpvqsitlv letyrpyfsi qyelleaaql
      541 aietmngtil egscirvhrl lteltlecdt lvreleqdse nqgtiyvagi getfkehlle
      601 qsnlfpdlea vilpkelksr kqknycflkf ktfnsaqval evlkgkdwkl kgrnaltsrh
      661 lqawlknihp epsmpmglri vppllerhif rtlkanhpki vawrwsrrie klyhslspgt
      721 fclillpgtk ntfgshpglg lmkikeeegg dtll
//
LOCUS       NP_001011914             176 aa            linear   ROD 27-APR-2025
DEFINITION  protein Dr1 [Rattus norvegicus].
ACCESSION   NP_001011914 XP_214124
VERSION     NP_001011914.1
DBSOURCE    REFSEQ: accession NM_001011914.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Li,H., Wei,Y., Xi,Y., Jiao,L., Wen,X., Wu,R., Chang,G., Sun,F. and
            Hao,J.
  TITLE     DR1-CSE/H2S pathway upregulates autophagy and inhibits H9C2 cells
            damage induced by high glucose
  JOURNAL   Acta Cardiol 78 (5), 594-606 (2023)
   PUBMED   36197015
  REMARK    GeneRIF: DR1-CSE/H2S pathway upregulates autophagy and inhibits
            H9C2 cells damage induced by high glucose.
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Krebs,A.R., Demmers,J., Karmodiya,K., Chang,N.C., Chang,A.C. and
            Tora,L.
  TITLE     ATAC and Mediator coactivators form a stable complex and regulate a
            set of non-coding RNA genes
  JOURNAL   EMBO Rep 11 (7), 541-547 (2010)
   PUBMED   20508642
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083822.1.
            
            On Feb 11, 2005 this sequence version replaced XP_214124.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083822.1, EV768811.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN16676784
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..176
                     /product="protein Dr1"
                     /note="NC2-beta; negative cofactor 2-beta; TATA-binding
                     protein-associated phosphoprotein; down-regulator of
                     transcription 1, TBP-binding (negative cofactor 2);
                     protein Dr1-like"
                     /calculated_mol_wt=19299
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q01658; propagated from
                     UniProtKB/Swiss-Prot (Q5XI68.1)"
     Region          8..130
                     /region_name="HFD_Dr1"
                     /note="histone-fold domain found in protein Dr1 and
                     similar proteins; cd22905"
                     /db_xref="CDD:467030"
     Site            order(9,11..14,17,21..22,24..26,30..32,35,38..39,42..43,
                     45..48,51..52,55,65..68,71,83,86,90,94)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467030"
     Site            order(12,14..16,63..65,95,101..102)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467030"
     Region          100..103
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI68.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01658; propagated from
                     UniProtKB/Swiss-Prot (Q5XI68.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01658; propagated from
                     UniProtKB/Swiss-Prot (Q5XI68.1)"
     Site            order(115,118..119,121..122,125..126,129..130)
                     /site_type="other"
                     /note="TBP binding site [polypeptide binding]"
                     /db_xref="CDD:467030"
     Region          152..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI68.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01658; propagated from
                     UniProtKB/Swiss-Prot (Q5XI68.1)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01658; propagated from
                     UniProtKB/Swiss-Prot (Q5XI68.1)"
     CDS             1..176
                     /gene="Dr1"
                     /coded_by="NM_001011914.1:622..1152"
                     /db_xref="GeneID:289881"
                     /db_xref="RGD:1305201"
ORIGIN      
        1 masssgnddd ltipraaink miketlpnvr vandarelvv ncctefihli sseaneicnk
       61 sekktispeh viqaleslgf gsyisevkev lqecktvalk rrkassrlen lgipeeellr
      121 qqqelfakar qqqaelaqqe wlqmqqaaqq aqlaaasasa snqagssqde dddddi
//
LOCUS       NP_001014280             302 aa            linear   ROD 27-APR-2025
DEFINITION  cardiolipin synthase (CMP-forming) [Rattus norvegicus].
ACCESSION   NP_001014280 XP_345439
VERSION     NP_001014280.1
DBSOURCE    REFSEQ: accession NM_001014258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Ohlig,T., Le,D.V., Gardemann,A., Wolke,C., Gurtler,S., Peter,D.,
            Schild,L. and Lendeckel,U.
  TITLE     Effects of siRNA-dependent knock-down of cardiolipin synthase and
            tafazzin on mitochondria and proliferation of glioma cells
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 379-387 (2018)
   PUBMED   29325722
  REMARK    GeneRIF: Knock-down of cardiolipin synthase affected the cellular
            CL content in the presence of linoleic acid (LA) in the culture
            medium.
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Ren,M., Phoon,C.K. and Schlame,M.
  TITLE     Metabolism and function of mitochondrial cardiolipin
  JOURNAL   Prog Lipid Res 55, 1-16 (2014)
   PUBMED   24769127
  REMARK    Review article
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Cheng,H., Mancuso,D.J., Jiang,X., Guan,S., Yang,J., Yang,K.,
            Sun,G., Gross,R.W. and Han,X.
  TITLE     Shotgun lipidomics reveals the temporally dependent, highly
            diversified cardiolipin profile in the mammalian brain: temporally
            coordinated postnatal diversification of cardiolipin molecular
            species with neuronal remodeling
  JOURNAL   Biochemistry 47 (21), 5869-5880 (2008)
   PUBMED   18454555
  REMARK    GeneRIF: CL has roles in in neuronal signaling, mitochondrial
            bioenergetics, and apoptosis
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Schlame,M. and Hostetler,K.Y.
  TITLE     Solubilization, purification, and characterization of cardiolipin
            synthase from rat liver mitochondria. Demonstration of its
            phospholipid requirement
  JOURNAL   J Biol Chem 266 (33), 22398-22403 (1991)
   PUBMED   1657995
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Hostetler,K.Y.
  TITLE     Effect of thyroxine on the activity of mitochondrial cardiolipin
            synthase in rat liver
  JOURNAL   Biochim Biophys Acta 1086 (1), 139-140 (1991)
   PUBMED   1659453
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085849.1.
            
            On Apr 20, 2005 this sequence version replaced XP_345439.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085849.1, SRR8487227.254384.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..302
                     /product="cardiolipin synthase (CMP-forming)"
                     /EC_number="2.7.8.41"
                     /note="cardiolipin synthetase; CLS"
                     /calculated_mol_wt=32497
     Region          65..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     Region          <92..288
                     /region_name="PLN02794"
                     /note="cardiolipin synthase"
                     /db_xref="CDD:178391"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     Site            190..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     Site            250..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     Site            271..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2V5.1)"
     CDS             1..302
                     /gene="Crls1"
                     /gene_synonym="RGD1311037"
                     /coded_by="NM_001014258.1:133..1041"
                     /db_xref="GeneID:366196"
                     /db_xref="RGD:1311037"
ORIGIN      
        1 mlawrvarga wgslrvavrp pgarlgrggs rrallppaac clgclaerwr lrpaafalrl
       61 pgtsprthcs gagkaapepa aggdaaaqap sarwvrasat ssyenpwtip nllsmtrigl
      121 apvlgylile edfnvalgvf alagltdlld gfiarnwanq ksalgsaldp ladkvlisil
      181 yisltyadli pvpltymiis rdvmliaavf yvryrtlptp rtlakyfnpc yatarlkptf
      241 iskvntavql ilvaaslaap vfnyadsiyl qilwcctaft taasaysyyh ygrktvqvik
      301 gk
//
LOCUS       NP_446133                101 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A3 [Rattus norvegicus].
ACCESSION   NP_446133
VERSION     NP_446133.1
DBSOURCE    REFSEQ: accession NM_053681.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Kizawa,K. and Ito,M.
  TITLE     Characterization of epithelial cells in the hair follicle with S100
            proteins
  JOURNAL   Methods Mol Biol 289, 209-222 (2005)
   PUBMED   15502186
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Fritz,G., Heizmann,C.W. and Kroneck,P.M.
  TITLE     Probing the structure of the human Ca2+- and Zn2+-binding protein
            S100A3: spectroscopic investigations of its transition metal ion
            complexes, and three-dimensional structural model
  JOURNAL   Biochim Biophys Acta 1448 (2), 264-276 (1998)
   PUBMED   9920417
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF140231.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF140231.1, SRR8487226.203205.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132266, SAMD00132283
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..101
                     /product="protein S100-A3"
                     /calculated_mol_wt=11616
     Region          4..90
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(4..20,26..28,37..38,40..42,70..73,75..76,78..81,
                     83..90)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(20,25,28,33..34,63,65,67,69,71,74)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     CDS             1..101
                     /gene="S100a3"
                     /coded_by="NM_053681.1:47..352"
                     /db_xref="GeneID:114216"
                     /db_xref="RGD:620260"
ORIGIN      
        1 mtrpleqava aivctfqeya grcgdkykic qselkellqk elptwtpsef recdynkfms
       61 vldtnkdcev dfgeyvrsla slclycheyf kecppeppcp q
//
LOCUS       NP_058942                438 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 5 isoform
            b [Rattus norvegicus].
ACCESSION   NP_058942 XP_346829
VERSION     NP_058942.1
DBSOURCE    REFSEQ: accession NM_017246.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Stankiewicz,T.R., Ramaswami,S.A., Bouchard,R.J., Aktories,K. and
            Linseman,D.A.
  TITLE     Neuronal apoptosis induced by selective inhibition of Rac GTPase
            versus global suppression of Rho family GTPases is mediated by
            alterations in distinct mitogen-activated protein kinase signaling
            cascades
  JOURNAL   J Biol Chem 290 (15), 9363-9376 (2015)
   PUBMED   25666619
  REMARK    GeneRIF: Data indicate that NSC23766-mediated Rac inhibition
            induces cerebellar granule neurons (CGNs) apoptosis through
            deactivation of prosurvival MAP Kinase Kinase 5 MEK5/ERK5 kinase
            signaling.
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Woo,C.H., Le,N.T., Shishido,T., Chang,E., Lee,H., Heo,K.S.,
            Mickelsen,D.M., Lu,Y., McClain,C., Spangenberg,T., Yan,C.,
            Molina,C.A., Yang,J., Patterson,C. and Abe,J.
  TITLE     Novel role of C terminus of Hsc70-interacting protein (CHIP)
            ubiquitin ligase on inhibiting cardiac apoptosis and dysfunction
            via regulating ERK5-mediated degradation of inducible cAMP early
            repressor
  JOURNAL   FASEB J 24 (12), 4917-4928 (2010)
   PUBMED   20724525
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Ohnesorge,N., Viemann,D., Schmidt,N., Czymai,T., Spiering,D.,
            Schmolke,M., Ludwig,S., Roth,J., Goebeler,M. and Schmidt,M.
  TITLE     Erk5 activation elicits a vasoprotective endothelial phenotype via
            induction of Kruppel-like factor 4 (KLF4)
  JOURNAL   J Biol Chem 285 (34), 26199-26210 (2010)
   PUBMED   20551324
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Haines,J.D., Fang,J., Mushynski,W.E. and Almazan,G.
  TITLE     Mitogen-activated protein kinase activated protein kinase 2 (MK2)
            participates in p38 MAPK regulated control of oligodendrocyte
            differentiation
  JOURNAL   Glia 58 (11), 1384-1393 (2010)
   PUBMED   20607863
  REMARK    GeneRIF: The p38-mitogen-activated protein kinase activated protein
            kinase 2 (MK2) pathway is a component of the signaling cascade
            regulating oligodendrocyte differentiation.
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Gerits,N., Shiryaev,A., Kostenko,S., Klenow,H., Shiryaeva,O.,
            Johannessen,M. and Moens,U.
  TITLE     The transcriptional regulation and cell-specific expression of the
            MAPK-activated protein kinase MK5
  JOURNAL   Cell Mol Biol Lett 14 (4), 548-574 (2009)
   PUBMED   19484198
  REMARK    GeneRIF: Several binding motifs for heat shock factor are dispersed
            in the mouse and rat promoter, and temperature shock transiently
            enhanced the MAP-kinase-activated kinase 5 transcript levels.
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Thomas,J.A., Haudek,S.B., Koroglu,T., Tsen,M.F., Bryant,D.D.,
            White,D.J., Kusewitt,D.F., Horton,J.W. and Giroir,B.P.
  TITLE     IRAK1 deletion disrupts cardiac Toll/IL-1 signaling and protects
            against contractile dysfunction
  JOURNAL   Am J Physiol Heart Circ Physiol 285 (2), H597-H606 (2003)
   PUBMED   12860565
  REMARK    Erratum:[Am J Physiol Heart Circ Physiol. 2004 Jan;286(1):H477]
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Mehta,P.B., Jenkins,B.L., McCarthy,L., Thilak,L., Robson,C.N.,
            Neal,D.E. and Leung,H.Y.
  TITLE     MEK5 overexpression is associated with metastatic prostate cancer,
            and stimulates proliferation, MMP-9 expression and invasion
  JOURNAL   Oncogene 22 (9), 1381-1389 (2003)
   PUBMED   12618764
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Watson,F.L., Heerssen,H.M., Bhattacharyya,A., Klesse,L., Lin,M.Z.
            and Segal,R.A.
  TITLE     Neurotrophins use the Erk5 pathway to mediate a retrograde survival
            response
  JOURNAL   Nat Neurosci 4 (10), 981-988 (2001)
   PUBMED   11544482
  REMARK    Erratum:[Nat Neurosci 2002 Oct;5(10):1017]
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Nicol,R.L., Frey,N., Pearson,G., Cobb,M., Richardson,J. and
            Olson,E.N.
  TITLE     Activated MEK5 induces serial assembly of sarcomeres and eccentric
            cardiac hypertrophy
  JOURNAL   EMBO J 20 (11), 2757-2767 (2001)
   PUBMED   11387209
REFERENCE   10 (residues 1 to 438)
  AUTHORS   English,J.M., Vanderbilt,C.A., Xu,S., Marcus,S. and Cobb,M.H.
  TITLE     Isolation of MEK5 and differential expression of alternatively
            spliced forms
  JOURNAL   J Biol Chem 270 (48), 28897-28902 (1995)
   PUBMED   7499418
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078860.1 and U37464.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346829.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            coding region compared to variant 1. The resulting protein (isoform
            b) is shorter but has the same N- and C-termini compared to isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U37464.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..438
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 5 isoform b"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 5; MAPKK 5; MAPK/ERK kinase 5; MAP kinase kinase 5;
                     MEK 5"
                     /calculated_mol_wt=48924
     Region          17..107
                     /region_name="PB1_Map2k5"
                     /note="PB1 domain is essential part of the
                     mitogen-activated protein kinase kinase 5 (Map2k5, alias
                     MEK5) one of the key member of the signaling kinases
                     cascade which involved in angiogenesis and early
                     cardiovascular development. The PB1 domain of Map2k5...;
                     cd06395"
                     /db_xref="CDD:99717"
     Site            order(64,66,68,77)
                     /site_type="other"
                     /note="PB1 interaction surface [polypeptide binding]"
                     /db_xref="CDD:99717"
     Region          164..432
                     /region_name="PKc_MKK5"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-activated protein Kinase Kinase 5;
                     cd06619"
                     /db_xref="CDD:132950"
     Site            order(172..176,180,193,195,225,241..244,247..248,251,283,
                     285..288,290,300..301,304,316..319,321,348)
                     /site_type="active"
                     /db_xref="CDD:132950"
     Site            order(172..176,178,180,193,195,225,241..244,247..248,
                     250..251,285,287..288,290,301)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132950"
     Site            order(175..176,283,285..287,304,316..319,321,348)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:132950"
     Site            300..321
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:132950"
     CDS             1..438
                     /gene="Map2k5"
                     /gene_synonym="Mek5"
                     /coded_by="NM_017246.2:600..1916"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:29568"
                     /db_xref="RGD:61890"
ORIGIN      
        1 mlwlalgpfr amenqvlvir ikipnsgavd wtvhsgpqll frdvldvigq vlpeatttaf
       61 eyededgdri tvrsdeemka mlsyyystvm eqqvngqlie plqifprack ppgernihgl
      121 kvntragpsq htspvvsdsl psnslkkssa elrkilangq mneqdiryrd tlghgnggtv
      181 ykayhvpsgk ilavkvilld itlelqkqim seleilykcd ssyiigfyga ffvenrisic
      241 tefmdggsld vyrkipehvl griavavvkg ltylwslkil hrdvkpsnml vntsgqvklc
      301 dfgvstqlvn siaktyvgtn aymaperisg eqygihsdvw slgisfmeiq knqgslmplq
      361 llqcivdeds pvlplgefse pfvhfitqcm rkqpkerpap eelmghpfiv qfndgnatvv
      421 smwvcralee rrsqqgpp
//
LOCUS       NP_001014282             207 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor A N-terminal and central
            domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001014282 XP_345559
VERSION     NP_001014282.1
DBSOURCE    REFSEQ: accession NM_001014260.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY316983.1, BC083757.1 and AI043997.1.
            
            On Apr 1, 2005 this sequence version replaced XP_345559.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY316983.1, BC083757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..207
                     /product="transcription elongation factor A N-terminal and
                     central domain-containing protein 2"
                     /note="transcription elongation factor A (SII) N-terminal
                     and central domain containing 2"
                     /calculated_mol_wt=24168
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96MN5; propagated from
                     UniProtKB/Swiss-Prot (Q5XIC7.1)"
     Region          38..111
                     /region_name="TFIIS_I"
                     /note="N-terminal domain (domain I) of transcription
                     elongation factor S-II (TFIIS); similar to a domain found
                     in elongin A and CRSP70; likely to be involved in
                     transcription; domain I from TFIIS interacts with RNA
                     polymerase II holoenzyme; cd00183"
                     /db_xref="CDD:238107"
     Site            order(46..47,50,88..89)
                     /site_type="other"
                     /note="putative RNA polymerase binding site [polypeptide
                     binding]"
                     /db_xref="CDD:238107"
     Region          126..>202
                     /region_name="TFIIS_M"
                     /note="Transcription factor S-II (TFIIS), central domain;
                     pfam07500"
                     /db_xref="CDD:462184"
     CDS             1..207
                     /gene="Tceanc2"
                     /coded_by="NM_001014260.2:147..770"
                     /db_xref="GeneID:366431"
                     /db_xref="RGD:1359481"
ORIGIN      
        1 mdkfvirtpr iqnspkkklk ekvykqatie slkrvvvied ikrwktvlel peqtkenlva
       61 alqelkkkip srevlrstri ghavnkvrrh sdpevaglak evytewktfi enhldrpsie
      121 vhsdpktesf rknaqkllse alelkmdhll venieretfh lcsrlinrpy rrtvralvft
      181 lkhraeireq vksgtlpvgt fvqthkk
//
LOCUS       NP_808793                390 aa            linear   ROD 27-APR-2025
DEFINITION  platelet-activating factor acetylhydrolase 2, cytoplasmic [Rattus
            norvegicus].
ACCESSION   NP_808793
VERSION     NP_808793.1
DBSOURCE    REFSEQ: accession NM_177932.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Bonin,F., Ryan,S.D., Migahed,L., Mo,F., Lallier,J., Franks,D.J.,
            Arai,H. and Bennett,S.A.
  TITLE     Anti-apoptotic actions of the platelet-activating factor
            acetylhydrolase I alpha2 catalytic subunit
  JOURNAL   J Biol Chem 279 (50), 52425-52436 (2004)
   PUBMED   15456758
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Karasawa,K., Qiu,X. and Lee,T.
  TITLE     Purification and characterization from rat kidney membranes of a
            novel platelet-activating factor (PAF)-dependent transacetylase
            that catalyzes the hydrolysis of PAF, formation of PAF analogs, and
            C2-ceramide
  JOURNAL   J Biol Chem 274 (13), 8655-8661 (1999)
   PUBMED   10085103
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY225592.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY225592.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..390
                     /product="platelet-activating factor acetylhydrolase 2,
                     cytoplasmic"
                     /EC_number="3.1.1.47"
                     /EC_number="2.3.1.149"
                     /note="serine-dependent phospholipase A2; SD-PLA2;
                     platelet-activating factor acetylhydrolase 2, 40kDa;
                     PAF:sphingosine transacetylase; PAF:lysophospholipid
                     transacetylase; platelet-activating factor
                     acetyltransferase PAFAH2"
                     /calculated_mol_wt=43361
     Region          1..379
                     /region_name="PAF-AH_p_II"
                     /note="Platelet-activating factor acetylhydrolase, isoform
                     II; pfam03403"
                     /db_xref="CDD:397462"
     CDS             1..390
                     /gene="Pafah2"
                     /coded_by="NM_177932.2:15..1187"
                     /db_xref="GeneID:313611"
                     /db_xref="RGD:631399"
ORIGIN      
        1 mgagqsicfp pisgphhigc tdvmeghsle gslfrlfypc easetceqpl wipryeycvg
       61 ladylqynkr wvgllfnvgi gscrlpvswn gpfktkesgy pliilshglg gfrvsysafc
      121 melasrgfvv aaiehrdqsa aatyfckqts qessptesle eewipfrrik egekefhvrn
      181 pqvhqrakec vrvlqilqda sagkpvinvf pggldlmtlk gsidmsrvav mghsfggata
      241 ilaltqeaqf rcaialdawm fplehdfypk argpvffinv ekfqtvesvn lmkkicaqhe
      301 qsrivtvlga vhrsqtdfaf vtgnmigklf ssgtrgtldp yegqevmvra mlaflqkhld
      361 lkedydqwns fiegigpsli qgaphylssl
//
LOCUS       NP_001004277             413 aa            linear   ROD 27-APR-2025
DEFINITION  lysosomal phospholipase A and acyltransferase precursor [Rattus
            norvegicus].
ACCESSION   NP_001004277 XP_341682
VERSION     NP_001004277.1
DBSOURCE    REFSEQ: accession NM_001004277.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Danyukova,T., Ariunbat,K., Thelen,M., Brocke-Ahmadinejad,N.,
            Mole,S.E. and Storch,S.
  TITLE     Loss of CLN7 results in depletion of soluble lysosomal proteins and
            impaired mTOR reactivation
  JOURNAL   Hum Mol Genet 27 (10), 1711-1722 (2018)
   PUBMED   29514215
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Abe,A., Kelly,R. and Shayman,J.A.
  TITLE     The measurement of lysosomal phospholipase A2 activity in plasma
  JOURNAL   J Lipid Res 51 (8), 2464-2470 (2010)
   PUBMED   20410020
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Abe,A., Hiraoka,M. and Shayman,J.A.
  TITLE     The acylation of lipophilic alcohols by lysosomal phospholipase A2
  JOURNAL   J Lipid Res 48 (10), 2255-2263 (2007)
   PUBMED   17626977
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Abe,A., Hiraoka,M. and Shayman,J.A.
  TITLE     Positional specificity of lysosomal phospholipase A2
  JOURNAL   J Lipid Res 47 (10), 2268-2279 (2006)
   PUBMED   16837646
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Hiraoka,M., Abe,A., Lu,Y., Yang,K., Han,X., Gross,R.W. and
            Shayman,J.A.
  TITLE     Lysosomal phospholipase A2 and phospholipidosis
  JOURNAL   Mol Cell Biol 26 (16), 6139-6148 (2006)
   PUBMED   16880524
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Taniyama,Y., Fuse,H., Satomi,T., Tozawa,R., Yasuhara,Y.,
            Shimakawa,K., Shibata,S., Hattori,M., Nakata,M. and Taketomi,S.
  TITLE     Loss of lysophospholipase 3 increases atherosclerosis in
            apolipoprotein E-deficient mice
  JOURNAL   Biochem Biophys Res Commun 330 (1), 104-110 (2005)
   PUBMED   15781238
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Abe,A., Hiraoka,M., Wild,S., Wilcoxen,S.E., Paine,R. 3rd and
            Shayman,J.A.
  TITLE     Lysosomal phospholipase A2 is selectively expressed in alveolar
            macrophages
  JOURNAL   J Biol Chem 279 (41), 42605-42611 (2004)
   PUBMED   15294901
  REMARK    GeneRIF: LPLA2 may be a major enzyme of pulmonary surfactant
            phospholipid degradation by alveolar macrophages
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Hiraoka,M., Abe,A. and Shayman,J.A.
  TITLE     Cloning and characterization of a lysosomal phospholipase A2,
            1-O-acylceramide synthase
  JOURNAL   J Biol Chem 277 (12), 10090-10099 (2002)
   PUBMED   11790796
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Fisher,A.B. and Dodia,C.
  TITLE     Lysosomal-type PLA2 and turnover of alveolar DPPC
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 280 (4), L748-L754 (2001)
   PUBMED   11238016
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098894.1.
            
            On Sep 10, 2004 this sequence version replaced XP_341682.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098894.1, AY490816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..413
                     /product="lysosomal phospholipase A and acyltransferase
                     precursor"
                     /EC_number="3.1.1.4"
                     /EC_number="3.1.1.32"
                     /note="lysophospholipase 3; lysosomal phospholipase A and
                     acyltransferase; 1-O-acylceramide synthase; lysosomal
                     phospholipase A2; LCAT-like lysophospholipase; group XV
                     phospholipase A2"
                     /calculated_mol_wt=43566
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3844
     mat_peptide     34..413
                     /product="Lysosomal phospholipase A and acyltransferase.
                     /evidence=ECO:0000255. /id=PRO_0000413420"
                     /note="propagated from UniProtKB/Swiss-Prot (Q675A5.1)"
                     /calculated_mol_wt=43566
     Region          84..396
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675A5.1)"
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675A5.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675A5.1)"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q675A5.1)"
     CDS             1..413
                     /gene="Pla2g15"
                     /gene_synonym="1-O-acylceramidesynthase; ACS; LLPL; LPLA2;
                     Lypla3"
                     /coded_by="NM_001004277.2:29..1270"
                     /db_xref="GeneID:361401"
                     /db_xref="RGD:1302982"
ORIGIN      
        1 mdrhlcicre iqlrsgllfp flllmmladl alpaqrhppv vlvpgdlgnq leakldkpkv
       61 vhylcskrtd syftlwlnle lllpviidcw idnirlvynr tsrttqfpdg vdvrvpgfge
      121 tfslefldps krnvgsyfyt mveslvgwgy trgedvrgap ydwrrapnen gpyflalqem
      181 ieemyqmygg pvvlvahsmg nmymlyflqr qpqawkdkyi qafvslgapw ggvaktlrvl
      241 asgdnnripv igplkireqq rsavstswll pynhtwshek vfvytptany tlrdyhrffq
      301 digfedgwfm rqdtqglvea lvppgvelhc lygtgvptpn sfyyenfpdr dpkicfgdgd
      361 gtvnlesvlq cqawqsrqeh kvslqelpgs ehiemlanat tlaylkrvll eep
//
LOCUS       NP_612542                330 aa            linear   ROD 27-APR-2025
DEFINITION  spondin-2 precursor [Rattus norvegicus].
ACCESSION   NP_612542 XP_346467
VERSION     NP_612542.1
DBSOURCE    REFSEQ: accession NM_138533.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Zhu,L.H., Huang,L., Zhang,X., Zhang,P., Zhang,S.M., Guan,H.,
            Zhang,Y., Zhu,X.Y., Tian,S., Deng,K. and Li,H.
  TITLE     Mindin regulates vascular smooth muscle cell phenotype and prevents
            neointima formation
  JOURNAL   Clin Sci (Lond) 129 (2), 129-145 (2015)
   PUBMED   25751394
  REMARK    GeneRIF: Mindin protects against vascular hyperplasia by
            suppression of abnormal VSMC proliferation, migration and
            phenotypic switching in an AKT-dependent manner.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Cheng,Y.C., Chen,T.A., Chen,C.Y., Liang,C.M. and Liang,S.M.
  TITLE     3'poly-G-tailed ODNs inhibit F-spondin to induce cell death and
            neurite retraction in rat embryonic neurons
  JOURNAL   Mol Neurobiol 45 (3), 536-549 (2012)
   PUBMED   22592270
  REMARK    GeneRIF: 3'G-oligodeoxyribonucleotides enhance nucleus YB-1 to
            inhibit F-spondin leading to cell death and neurite retraction of
            embryonic neuron cells.
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Liao,C.H., Yeh,S.C., Huang,Y.H., Chen,R.N., Tsai,M.M., Chen,W.J.,
            Chi,H.C., Tai,P.J., Liao,C.J., Wu,S.M., Cheng,W.L., Pai,L.M. and
            Lin,K.H.
  TITLE     Positive regulation of spondin 2 by thyroid hormone is associated
            with cell migration and invasion
  JOURNAL   Endocr Relat Cancer 17 (1), 99-111 (2010)
   PUBMED   19903741
  REMARK    GeneRIF: Spon2 protein was 9.2-fold & mRNA 16.5-fold higher in the
            T3-treated thyroidectomized (Tx)rats compared with the Tx group.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Fevre-Montange,M., Champier,J., Durand,A., Wierinckx,A.,
            Honnorat,J., Guyotat,J. and Jouvet,A.
  TITLE     Microarray gene expression profiling in meningiomas: differential
            expression according to grade or histopathological subtype
  JOURNAL   Int J Oncol 35 (6), 1395-1407 (2009)
   PUBMED   19885562
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Attur,M.G., Palmer,G.D., Al-Mussawir,H.E., Dave,M., Teixeira,C.C.,
            Rifkin,D.B., Appleton,C.T., Beier,F. and Abramson,S.B.
  TITLE     F-spondin, a neuroregulatory protein, is up-regulated in
            osteoarthritis and regulates cartilage metabolism via TGF-beta
            activation
  JOURNAL   FASEB J 23 (1), 79-89 (2009)
   PUBMED   18780763
  REMARK    GeneRIF: These studies identify F-spondin as a novel protein in
            osteoarthritis cartilage, where it may act in situ at lesional
            areas to activate latent TGF-beta and induce cartilage degradation.
            Erratum:[FASEB J. 2009 Aug;23(8):2790]
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Paakkonen,K., Tossavainen,H., Permi,P., Rakkolainen,H., Rauvala,H.,
            Raulo,E., Kilpelainen,I. and Guntert,P.
  TITLE     Solution structures of the first and fourth TSR domains of
            F-spondin
  JOURNAL   Proteins 64 (3), 665-672 (2006)
   PUBMED   16736493
  REMARK    GeneRIF: NMR solution structures of TSR domains of F-spondin showed
            that they have an unusual fold that is characterized by a long,
            nonglobular shape, consisting of two beta-strands and one irregular
            extended strand.
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Schubert,D., Klar,A., Park,M., Dargusch,R. and Fischer,W.H.
  TITLE     F-spondin promotes nerve precursor differentiation
  JOURNAL   J Neurochem 96 (2), 444-453 (2006)
   PUBMED   16300627
  REMARK    GeneRIF: F-spondin can alter cell differentiation in multiple ways,
            depending upon its concentration and distribution between
            substrate-attached and soluble forms.
REFERENCE   9  (residues 1 to 330)
  AUTHORS   He,Y.W., Li,H., Zhang,J., Hsu,C.L., Lin,E., Zhang,N., Guo,J.,
            Forbush,K.A. and Bevan,M.J.
  TITLE     The extracellular matrix protein mindin is a pattern-recognition
            molecule for microbial pathogens
  JOURNAL   Nat Immunol 5 (1), 88-97 (2004)
   PUBMED   14691481
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Feinstein,Y., Borrell,V., Garcia,C., Burstyn-Cohen,T., Tzarfaty,V.,
            Frumkin,A., Nose,A., Okamoto,H., Higashijima,S., Soriano,E. and
            Klar,A.
  TITLE     F-spondin and mindin: two structurally and functionally related
            genes expressed in the hippocampus that promote outgrowth of
            embryonic hippocampal neurons
  JOURNAL   Development 126 (16), 3637-3648 (1999)
   PUBMED   10409509
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078734.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346467.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078734.1, SRR8487231.139517.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..330
                     /product="spondin-2 precursor"
                     /note="F-spondin; mindin; spondin 2, extracellular matrix
                     protein; spondin-2-like"
                     /calculated_mol_wt=33274
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2759
     mat_peptide     26..330
                     /product="Spondin-2. /id=PRO_0000035872"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV75.1)"
                     /calculated_mol_wt=33274
     Region          40..234
                     /region_name="Spond_N"
                     /note="Spondin_N; pfam06468"
                     /db_xref="CDD:461924"
     Site            140
                     /site_type="other"
                     /note="Important for metal ion-dependent interaction with
                     integrin. /evidence=ECO:0000250|UniProtKB:Q9BUD6;
                     propagated from UniProtKB/Swiss-Prot (Q9WV75.1)"
     Region          277..329
                     /region_name="TSP1_spondin"
                     /note="Spondin-like TSP1 domain; pfam19028"
                     /db_xref="CDD:465948"
     Site            282
                     /site_type="glycosylation"
                     /note="C-linked (Man) tryptophan.
                     /evidence=ECO:0000250|UniProtKB:Q9BUD6; propagated from
                     UniProtKB/Swiss-Prot (Q9WV75.1)"
     CDS             1..330
                     /gene="Spon2"
                     /coded_by="NM_138533.3:203..1195"
                     /db_xref="GeneID:171569"
                     /db_xref="RGD:708584"
ORIGIN      
        1 menvsfsldr tlwvfllaml gstagqplgg esvctarpla rysitftgkw sqtafpkqyp
       61 lfrppaqwss llgaahssdy smwrkneyvs nglrdfaerg eawalmkeie aageklqsvh
      121 avfsapavps gtgqtsaele vhprhslvsf vvrivpspdw fvgidsldlc eggrwkeqvv
      181 ldlyphdagt dsgftfsspn fatipqdtvt eitasspshp ansfyyprlk slppiakvtf
      241 vrlrqspraf appsldlasr gneivdslsv petpldcevs lwsswglcgg pcgklgaksr
      301 tryvrvqpan ngtpcpelee eaecapdncv
//
LOCUS       NP_114008                695 aa            linear   ROD 27-APR-2025
DEFINITION  segment polarity protein dishevelled homolog DVL-1 [Rattus
            norvegicus].
ACCESSION   NP_114008
VERSION     NP_114008.1
DBSOURCE    REFSEQ: accession NM_031820.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Zhu,Y., Li,Y., Jin,W., Li,Z., Zhang,L., Fang,Y. and Zhang,Y.
  TITLE     Hyperoxia exposure upregulates Dvl-1 and activates Wnt/beta-catenin
            signaling pathway in newborn rat lung
  JOURNAL   BMC Mol Cell Biol 24 (1), 4 (2023)
   PUBMED   36726071
  REMARK    GeneRIF: Hyperoxia exposure upregulates Dvl-1 and activates
            Wnt/beta-catenin signaling pathway in newborn rat lung.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Zhang,X., Zhang,X., Li,X., Ma,J., Xie,D. and Jiang,N.
  TITLE     Dishevelled-1 regulated apoptosis through NF-kappaB in cerebral
            ischemia/reperfusion injury in rats
  JOURNAL   Neurosci Lett 722, 134862 (2020)
   PUBMED   32105766
  REMARK    GeneRIF: Dishevelled-1 regulated apoptosis through NF-kappaB in
            cerebral ischemia/reperfusion injury in rats.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Wei,X., Gong,J., Ma,J., Zhang,T., Li,Y., Lan,T., Guo,P. and Qi,S.
  TITLE     Targeting the Dvl-1/beta-arrestin2/JNK3 interaction disrupts
            Wnt5a-JNK3 signaling and protects hippocampal CA1 neurons during
            cerebral ischemia reperfusion
  JOURNAL   Neuropharmacology 135, 11-21 (2018)
   PUBMED   29510185
  REMARK    GeneRIF: results indicate that Wnt5a-mediated JNK3 activation
            participates in Ischemia/Reperfusion brain injury by targeting the
            Dvl-1-beta-arrestin2/JNK3 interaction
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Zhang,X., Yu,X., Jiang,G., Miao,Y., Wang,L., Zhang,Y., Liu,Y.,
            Fan,C., Lin,X., Dong,Q., Han,Q., Zhao,H., Han,Y., Han,X., Rong,X.,
            Ding,S., Wang,E. and Wang,E.
  TITLE     Cytosolic TMEM88 promotes invasion and metastasis in lung cancer
            cells by binding DVLS
  JOURNAL   Cancer Res 75 (21), 4527-4537 (2015)
   PUBMED   26359454
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Ciani,L., Marzo,A., Boyle,K., Stamatakou,E., Lopes,D.M., Anane,D.,
            McLeod,F., Rosso,S.B., Gibb,A. and Salinas,P.C.
  TITLE     Wnt signalling tunes neurotransmitter release by directly targeting
            Synaptotagmin-1
  JOURNAL   Nat Commun 6, 8302 (2015)
   PUBMED   26400647
  REMARK    GeneRIF: The interaction of Dvl1 with Syt-1, which is regulated by
            Wnts, modulates neurotransmitter release.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Lijam,N., Paylor,R., McDonald,M.P., Crawley,J.N., Deng,C.X.,
            Herrup,K., Stevens,K.E., Maccaferri,G., McBain,C.J., Sussman,D.J.
            and Wynshaw-Boris,A.
  TITLE     Social interaction and sensorimotor gating abnormalities in mice
            lacking Dvl1
  JOURNAL   Cell 90 (5), 895-905 (1997)
   PUBMED   9298901
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Wagner,U., Brownlees,J., Irving,N.G., Lucas,F.R., Salinas,P.C. and
            Miller,C.C.
  TITLE     Overexpression of the mouse dishevelled-1 protein inhibits
            GSK-3beta-mediated phosphorylation of tau in transfected mammalian
            cells
  JOURNAL   FEBS Lett 411 (2-3), 369-372 (1997)
   PUBMED   9271238
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Steitz,S.A., Tsang,M. and Sussman,D.J.
  TITLE     Wnt-mediated relocalization of dishevelled proteins
  JOURNAL   In Vitro Cell Dev Biol Anim 32 (7), 441-445 (1996)
   PUBMED   8856345
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Pizzuti,A., Amati,F., Calabrese,G., Mari,A., Colosimo,A.,
            Silani,V., Giardino,L., Ratti,A., Penso,D., Calza,L., Palka,G.,
            Scarlato,G., Novelli,G. and Dallapiccola,B.
  TITLE     cDNA characterization and chromosomal mapping of two human
            homologues of the Drosophila dishevelled polarity gene
  JOURNAL   Hum Mol Genet 5 (7), 953-958 (1996)
   PUBMED   8817329
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Pizzuti,A., Novelli,G., Mari,A., Ratti,A., Colosimo,A., Amati,F.,
            Penso,D., Sangiuolo,F., Calabrese,G., Palka,G., Silani,V.,
            Gennarelli,M., Mingarelli,R., Scarlato,G., Scambler,P. and
            Dallapiccola,B.
  TITLE     Human homologue sequences to the Drosophila dishevelled
            segment-polarity gene are deleted in the DiGeorge syndrome
  JOURNAL   Am J Hum Genet 58 (4), 722-729 (1996)
   PUBMED   8644734
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF143546.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF143545.2, AF143546.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Rattus norvegicus"
                     /strain="SHRSP"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..695
                     /product="segment polarity protein dishevelled homolog
                     DVL-1"
                     /note="DSH homolog 1; dishevelled-1; dishevelled, dsh
                     homolog 1"
                     /calculated_mol_wt=75316
     Region          1..85
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     Region          89..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVB9.3)"
     Region          90..247
                     /region_name="Dishevelled"
                     /note="Dishevelled specific domain; pfam02377"
                     /db_xref="CDD:460544"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WVB9.3)"
     Region          251..337
                     /region_name="PDZ_Dishevelled-like"
                     /note="PDZ domain of segment polarity protein dishevelled
                     homolog DVL1, DVL2, DVL3, and related domains; cd06717"
                     /db_xref="CDD:467201"
     Site            order(261..267,281,284,314,318,321..322)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467201"
     Region          417..499
                     /region_name="DEP_dishevelled"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in dishevelled-like proteins. Dishevelled-like
                     proteins play a key role in the transduction of the Wnt
                     signal from the cell surface to the nucleus, which in turn
                     is an important regulatory pathway...; cd04438"
                     /db_xref="CDD:239885"
     Region          503..685
                     /region_name="Dsh_C"
                     /note="Segment polarity protein dishevelled (Dsh) C
                     terminal; pfam12316"
                     /db_xref="CDD:463531"
     Region          551..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVB9.3)"
     CDS             1..695
                     /gene="Dvl1"
                     /gene_synonym="dvl-1"
                     /coded_by="NM_031820.1:2..2089"
                     /db_xref="GeneID:83721"
                     /db_xref="RGD:620632"
ORIGIN      
        1 maetkiiyhm deeetpylvk lpvapervtl adfknvlsnr pvhaykfffk smdqdfgvvk
       61 eeifddnakl pcfngrvvsw lvlaegahsd agsqgtdsht dlppplertg gigdsrppsf
      121 hpnvassrdg mdnetgtesm vshrrerarr rnrdeaartn ghprgdrrre lglppdsast
      181 vlsselesss fidsdeednt srlsssteqs tssrlirkhk crrrkqrlrq tdrassfssi
      241 tdstmslnii tvtlnmerhh flgisivgqs ndrgdggiyi gsimkggava adgriepgdm
      301 llqvndvnfe nmsnddavrv lreivsqtgp isltvakcwd ptprsyftip radpvrpidp
      361 aawlshtaal tgalprygts pcssaitrts sssltssvpg apqleeaplt vksdmsaivr
      421 vmqlpdsgle irdrmwlkit ianavigadv vdwlythveg fkerrearky assmlkhgfl
      481 rhtvnkitfs eqcyyvfgdl csnlaslnln sgssgasdqd tlaplphpsv pwplgqgypy
      541 qypgpppcfp payqdpgfsy gsgsagsqqs egskssgstr sshrtpgree rratgaggsg
      601 sesdhtvpsg sgstgwwerp vsqlsrgssp rsqasavapg lpplhpltka yavvggppgg
      661 ppvrelaavp peltgsrqsf qkamgnpcef fvdim
//
LOCUS       NP_001020914             305 aa            linear   ROD 27-APR-2025
DEFINITION  superkiller complex protein 8 [Rattus norvegicus].
ACCESSION   NP_001020914 XP_343393
VERSION     NP_001020914.1
DBSOURCE    REFSEQ: accession NM_001025743.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Strikoudis,A., Lazaris,C., Trimarchi,T., Galvao Neto,A.L., Yang,Y.,
            Ntziachristos,P., Rothbart,S., Buckley,S., Dolgalev,I.,
            Stadtfeld,M., Strahl,B.D., Dynlacht,B.D., Tsirigos,A. and
            Aifantis,I.
  TITLE     Regulation of transcriptional elongation in pluripotency and cell
            differentiation by the PHD-finger protein Phf5a
  JOURNAL   Nat Cell Biol 18 (11), 1127-1138 (2016)
   PUBMED   27749823
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Muntean,A.G., Tan,J., Sitwala,K., Huang,Y., Bronstein,J.,
            Connelly,J.A., Basrur,V., Elenitoba-Johnson,K.S. and Hess,J.L.
  TITLE     The PAF complex synergizes with MLL fusion proteins at HOX loci to
            promote leukemogenesis
  JOURNAL   Cancer Cell 17 (6), 609-621 (2010)
   PUBMED   20541477
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Jaehning,J.A.
  TITLE     The Paf1 complex: platform or player in RNA polymerase II
            transcription?
  JOURNAL   Biochim Biophys Acta 1799 (5-6), 379-388 (2010)
   PUBMED   20060942
  REMARK    Review article
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Kim,J., Guermah,M. and Roeder,R.G.
  TITLE     The human PAF1 complex acts in chromatin transcription elongation
            both independently and cooperatively with SII/TFIIS
  JOURNAL   Cell 140 (4), 491-503 (2010)
   PUBMED   20178742
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Zhu,B., Mandal,S.S., Pham,A.D., Zheng,Y., Erdjument-Bromage,H.,
            Batra,S.K., Tempst,P. and Reinberg,D.
  TITLE     The human PAF complex coordinates transcription with events
            downstream of RNA synthesis
  JOURNAL   Genes Dev 19 (14), 1668-1673 (2005)
   PUBMED   16024656
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098059.1.
            
            On Jul 22, 2005 this sequence version replaced XP_343393.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098059.1, SRR8487230.9852.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..305
                     /product="superkiller complex protein 8"
                     /note="WD repeat-containing protein 61; WD repeat domain
                     61; SKI8 subunit of superkiller complex protein"
                     /calculated_mol_wt=33616
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZS3; propagated from
                     UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in WD repeat-containing protein
                     61, N-terminally processed. /evidence=ECO:0000269|Ref.2;
                     propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          <13..302
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          14..57
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          19..62
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          62..101
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          68..105
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          104..143
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          110..146
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          146..187
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          152..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          188..227
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          193..229
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..269
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     Region          236..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          272..305
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A0.1)"
     CDS             1..305
                     /gene="Skic8"
                     /gene_synonym="RGD1308228; Ski8; Wdr61"
                     /coded_by="NM_001025743.1:106..1023"
                     /db_xref="GeneID:363064"
                     /db_xref="RGD:1308228"
ORIGIN      
        1 mtnqysilfk qeqahddaiw svawetnkke nietvvtgsl ddlvkvwkwr derlelqwsl
       61 eghqlgvvsv dishtlpiaa sssldahirl wdlengkqmk sidagpvdaw tlafspdsqh
      121 latgthmgkv nifgvesgkk eysldtrgkf ilsiayspdg kylasgaidg iinifdiatg
      181 kllhtlegha mpirsltfsp dsqllvtasd dgyikiydvq hanlagtlsg haswvlnvaf
      241 cpddthfvss ssdksvkvwd vgtrtcihtf fdhqdqvwgv kyngngskiv svgddqeihv
      301 ydcpi
//
LOCUS       NP_062222               1203 aa            linear   ROD 27-APR-2025
DEFINITION  STE20-like serine/threonine-protein kinase [Rattus norvegicus].
ACCESSION   NP_062222 XP_579435
VERSION     NP_062222.2
DBSOURCE    REFSEQ: accession NM_019349.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1203)
  AUTHORS   Li,D., Ni,H., Rui,Q., Gao,R. and Chen,G.
  TITLE     Deletion of Mst1 attenuates neuronal loss and improves neurological
            impairment in a rat model of traumatic brain injury
  JOURNAL   Brain Res 1688, 15-21 (2018)
   PUBMED   29054447
  REMARK    GeneRIF: Study found that the phosphorylation level of Mammalian
            STE20-like kinase-1 (Mst1) in injured area was significantly
            increased after traumatic brain injury (TBI) in rat model of TBI.
REFERENCE   2  (residues 1 to 1203)
  AUTHORS   Fokin,A.I., Klementeva,T.S., Nadezhdina,E.S. and Burakov,A.V.
  TITLE     SLK/LOSK kinase regulates cell motility independently of
            microtubule organization and Golgi polarization
  JOURNAL   Cytoskeleton (Hoboken) 73 (2), 83-92 (2016)
   PUBMED   26818812
REFERENCE   3  (residues 1 to 1203)
  AUTHORS   Jaberi,A., Hooker,E., Guillemette,J., Papillon,J., Kristof,A.S. and
            Cybulsky,A.V.
  TITLE     Identification of Tpr and alpha-actinin-4 as two novel
            SLK-interacting proteins
  JOURNAL   Biochim Biophys Acta 1853 (10 Pt A), 2539-2552 (2015)
   PUBMED   26094769
REFERENCE   4  (residues 1 to 1203)
  AUTHORS   Baron,K.D., Al-Zahrani,K., Conway,J., Labreche,C., Storbeck,C.J.,
            Visvader,J.E. and Sabourin,L.A.
  TITLE     Recruitment and activation of SLK at the leading edge of migrating
            cells requires Src family kinase activity and the LIM-only protein
            4
  JOURNAL   Biochim Biophys Acta 1853 (7), 1683-1692 (2015)
   PUBMED   25882817
  REMARK    Erratum:[Biochim Biophys Acta. 2015 Oct;1853(10 Pt A):2754]
REFERENCE   5  (residues 1 to 1203)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1203)
  AUTHORS   Pike,A.C., Rellos,P., Niesen,F.H., Turnbull,A., Oliver,A.W.,
            Parker,S.A., Turk,B.E., Pearl,L.H. and Knapp,S.
  TITLE     Activation segment dimerization: a mechanism for kinase
            autophosphorylation of non-consensus sites
  JOURNAL   EMBO J 27 (4), 704-714 (2008)
   PUBMED   18239682
REFERENCE   7  (residues 1 to 1203)
  AUTHORS   Hao,W., Takano,T., Guillemette,J., Papillon,J., Ren,G. and
            Cybulsky,A.V.
  TITLE     Induction of apoptosis by the Ste20-like kinase SLK, a germinal
            center kinase that activates apoptosis signal-regulating kinase and
            p38
  JOURNAL   J Biol Chem 281 (6), 3075-3084 (2006)
   PUBMED   16316999
  REMARK    GeneRIF: SLK is an anoxia/recovery-dependent kinase that is
            activated via homodimerization and that signals via ASK1 and p38 to
            promote apoptosis
REFERENCE   8  (residues 1 to 1203)
  AUTHORS   Vitt,U., Gietzen,D., Stevens,K., Wingrove,J., Becha,S., Bulloch,S.,
            Burrill,J., Chawla,N., Chien,J., Crawford,M., Ison,C., Kearney,L.,
            Kwong,M., Park,J., Policky,J., Weiler,M., White,R., Xu,Y.,
            Daniels,S., Jacob,H., Jensen-Seaman,M.I., Lazar,J., Stuve,L. and
            Schmidt,J.
  TITLE     Identification of candidate disease genes by EST alignments,
            synteny, and expression and verification of Ensembl genes on rat
            chromosome 1q43-54
  JOURNAL   Genome Res 14 (4), 640-650 (2004)
   PUBMED   15060005
REFERENCE   9  (residues 1 to 1203)
  AUTHORS   Cybulsky,A.V., Takano,T., Papillon,J., Khadir,A., Bijian,K.,
            Chien,C.C., Alpers,C.E. and Rabb,H.
  TITLE     Renal expression and activity of the germinal center kinase SK2
  JOURNAL   Am J Physiol Renal Physiol 286 (1), F16-F25 (2004)
   PUBMED   12965890
  REMARK    GeneRIF: Stk2 is a renal epithelial protein kinase whose expression
            and activity are increased during development and recovery from
            acute renal failure (germinal center kinase SK2)
REFERENCE   10 (residues 1 to 1203)
  AUTHORS   Yue,C.C.
  TITLE     Novel putative protein kinase clones from a rat large granular
            lymphocyte tumor cell line
  JOURNAL   Mol Immunol 28 (4-5), 399-408 (1991)
   PUBMED   2062320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI136919.1, AB003357.1 and CK227996.1.
            
            On Mar 15, 2007 this sequence version replaced NP_062222.1.
            
            Sequence Note: The sequence AB003357.1 is chimeric. Only the Slk
            sequence region was propagated into this RefSeq record.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1203
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1203
                     /product="STE20-like serine/threonine-protein kinase"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 2; STE20-related kinase;
                     STE20-related serine/threonine-protein kinase"
                     /calculated_mol_wt=137579
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          28..309
                     /region_name="STKc_SLK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Ste20-Like Kinase; cd06643"
                     /db_xref="CDD:270811"
     Site            order(40..44,48,61,63,92,108..111,114..115,118,155,
                     157..160,162,172..173,176,190..193,195,227,236)
                     /site_type="active"
                     /db_xref="CDD:270811"
     Site            order(40..44,48,61,63,79,92,106,108..111,114..115,118,
                     159..160,162,172..173)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270811"
     Site            order(43..44,155,157..159,176,190..193,195,227,236)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270811"
     Site            172..195
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270811"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O54988; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          308..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08815.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54988; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          364..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08815.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            438..439
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O08815.1)"
     Region          515..761
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08815.1)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54988; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54988; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          773..792
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08815.1)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          851..958
                     /region_name="PKK"
                     /note="Polo kinase kinase; pfam12474"
                     /db_xref="CDD:463600"
     Region          988..1128
                     /region_name="PKK"
                     /note="Polo kinase kinase; pfam12474"
                     /db_xref="CDD:463600"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2G2; propagated from
                     UniProtKB/Swiss-Prot (O08815.1)"
     Region          1079..1100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08815.1)"
     CDS             1..1203
                     /gene="Slk"
                     /gene_synonym="SK2; Stk2"
                     /coded_by="NM_019349.2:169..3780"
                     /db_xref="GeneID:54308"
                     /db_xref="RGD:3780"
ORIGIN      
        1 msffnfrkif klgsekkkkq yehvkrdlnp eefweiigel gdgafgkvyk aqnketnvla
       61 aakvidtkse eeledymvei dilascdhpn ivklldafyy ennlwilief caggavdavm
      121 lelerpltes qiqvvckqtl ealnylhdnk iihrdlkagn ilftldgdik ladfgvsakn
      181 trtiqrrdsf igtpywmape vvmcetskdr pydykadvws lgitliemae iepphhelnp
      241 mrvllkiaks epptlaqpsr wssnfkdflk kcleknvdar wttsqllqhp fvtvdsnkpv
      301 reliaeakae vteevedgke eddddetesa lpipankras sdlsiassee dklsqnacil
      361 esvsertehn tsgdkfsnkv lsekptpegp ektvdvdgpa ndvnletvae pndqavgfhe
      421 ngrekkrpql esqpdtedqq tvdvnlvgeg ndsnivilet ntdclkpeed rneenqeiie
      481 nkltqseeik dihiqtmdlv sqetgekead fqaidnevgf tkeetqeklg kddkthkvvi
      541 sditsevgtd eppgdtqksa eqsqdaegga geeapepaqt ltekategpe ahgaeeeprs
      601 gervedkqle qqsavcegeg qvtstsestr atteepetde vdqvsesnsi eelerlgvtg
      661 aeeqalgskg eaateldler eenaqelpvk aepqapaasq asepppvlip sinihsente
      721 nkgemgalpk petilppepe ngkgndtdsg tgstvensss dlnlsissfl sktkdsgsvs
      781 lqetrrqkkt lkktrkfivd gvevsvttsk ivtdsdskte elrflrrqel relrllqkee
      841 qkaqqqlngk lqqqreqifr rfeqemlskk rqydqeienl ekqqkqtier leqehtnrlr
      901 deakrikgeq ekelskfqnm lrnrkkeeqe fvqkqqqeld galkkiiqqq kaelaniere
      961 clnnkqqllr areaaiwele erhlqekhql lkqqlkdqyf iqrhqllkrh eketeqmqry
     1021 nqrlieelkn rqtqerarlp kiqrseaktr mamfkkslri nstatpdqdr ekikqfaaqe
     1081 ekrqknerma qhqkhesqmr dlqlqceanv relhqlqnek chllvehetq klkeldeehs
     1141 qelkewrekl rprkktleee farklqeqev ffkmtgesec lnpsaqsris kfypiptlhs
     1201 tgs
//
LOCUS       NP_075591               1487 aa            linear   ROD 27-APR-2025
DEFINITION  murinoglobulin-1 precursor [Rattus norvegicus].
ACCESSION   NP_075591 XP_346725
VERSION     NP_075591.1
DBSOURCE    REFSEQ: accession NM_023103.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1487)
  AUTHORS   Ganaie,I.A., Malik,M.Z., Naqvi,S.H., Jain,S.K. and Wajid,S.
  TITLE     Differential levels of Alpha-1-inhibitor III, Immunoglobulin heavy
            chain variable region, and Hypertrophied skeletal muscle protein
            GTF3 in rat mammary tumorigenesis
  JOURNAL   Biochimie 174, 57-68 (2020)
   PUBMED   32325114
  REMARK    GeneRIF: Differential levels of Alpha-1-inhibitor III,
            Immunoglobulin heavy chain variable region, and Hypertrophied
            skeletal muscle protein GTF3 in rat mammary tumorigenesis.
REFERENCE   2  (residues 1 to 1487)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 1487)
  AUTHORS   Stamer,W.D., Hoffman,E.A., Luther,J.M., Hachey,D.L. and Schey,K.L.
  TITLE     Protein profile of exosomes from trabecular meshwork cells
  JOURNAL   J Proteomics 74 (6), 796-804 (2011)
   PUBMED   21362503
REFERENCE   4  (residues 1 to 1487)
  AUTHORS   Esadeg,S., He,H., Pijnenborg,R., Van Leuven,F. and Croy,B.A.
  TITLE     Alpha-2 macroglobulin controls trophoblast positioning in mouse
            implantation sites
  JOURNAL   Placenta 24 (10), 912-921 (2003)
   PUBMED   14580373
REFERENCE   5  (residues 1 to 1487)
  AUTHORS   Regler,R., Sickinger,S. and Schweizer,M.
  TITLE     Differential regulation of the two mRNA species of the rodent
            negative acute phase protein alpha 1-inhibitor 3
  JOURNAL   FEBS Lett 282 (2), 368-372 (1991)
   PUBMED   1709877
REFERENCE   6  (residues 1 to 1487)
  AUTHORS   Sugiyama,K., Izumi,S., Tomino,S. and Nagase,S.
  TITLE     Tumor-associated expression of a serum protein, termed aX protein
            (alpha 1-inhibitor III), and its mRNA in rat liver
  JOURNAL   Jpn J Cancer Res 80 (8), 759-764 (1989)
   PUBMED   2511184
REFERENCE   7  (residues 1 to 1487)
  AUTHORS   Braciak,T.A., Northemann,W., Hudson,G.O., Shiels,B.R., Gehring,M.R.
            and Fey,G.H.
  TITLE     Sequence and acute phase regulation of rat alpha 1-inhibitor III
            messenger RNA
  JOURNAL   J Biol Chem 263 (8), 3999-4012 (1988)
   PUBMED   2831216
REFERENCE   8  (residues 1 to 1487)
  AUTHORS   Schweizer,M., Takabayashi,K., Geiger,T., Laux,T., Biermann,G.,
            Buhler,J.M., Gauthier,F., Roberts,L.M. and Heinrich,P.C.
  TITLE     Identification and sequencing of cDNA clones for the rodent
            negative acute-phase protein alpha 1-inhibitor 3
  JOURNAL   Eur J Biochem 164 (2), 375-381 (1987)
   PUBMED   2436907
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X52984.1.
            
            On Jan 9, 2004 this sequence version replaced XP_346725.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X52984.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1487
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1487
                     /product="murinoglobulin-1 precursor"
                     /note="plasma proteinase inhibitor alpha-1-inhibitor III;
                     murinoglobulin-1-like; alpha-X protein; alpha x protein;
                     Murinoglobulin 1 homolog"
                     /calculated_mol_wt=162633
     sig_peptide     1..24
                     /note="alpha(10-inhibitor 3"
                     /calculated_mol_wt=2712
     mat_peptide     25..1487
                     /product="murinoglobulin-1"
                     /calculated_mol_wt=162633
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Region          <129..1359
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            393
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Region          686..745
                     /region_name="Bait region.
                     /evidence=ECO:0000250|UniProtKB:P28665"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03626.1)"
     Region          751..841
                     /region_name="A2M"
                     /note="Alpha-2-macroglobulin family; pfam00207"
                     /db_xref="CDD:459711"
     Site            760
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            787
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Region          971..1277
                     /region_name="A2M_2"
                     /note="Proteins similar to alpha2-macroglobulin (alpha
                     (2)-M). This group also contains the pregnancy zone
                     protein (PZP). Alpha(2)-M and PZP are broadly specific
                     proteinase inhibitors. Alpha (2)-M is a major carrier
                     protein in serum. The structural thioester...; cd02897"
                     /db_xref="CDD:239227"
     Site            order(985,987..988,991,1031,1041,1044,1098,1100..1101,
                     1261)
                     /site_type="other"
                     /note="surface patch"
                     /db_xref="CDD:239227"
     Site            985..988
                     /site_type="active"
                     /note="thioester region [active]"
                     /db_xref="CDD:239227"
     Site            1004
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            order(1087,1091,1093,1101)
                     /site_type="other"
                     /note="specificity defining residues"
                     /db_xref="CDD:239227"
     Site            1153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Site            1324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     Region          1387..1477
                     /region_name="A2M_recep"
                     /note="A-macroglobulin receptor binding domain; pfam07677"
                     /db_xref="CDD:462226"
     Site            1437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03626.1)"
     CDS             1..1487
                     /gene="Mug1"
                     /gene_synonym="A1i3"
                     /coded_by="NM_023103.1:52..4515"
                     /db_xref="GeneID:497794"
                     /db_xref="RGD:621366"
ORIGIN      
        1 mkknreaqlc lfsallaflp fasllngnsk ymvlvpsqly tetpekiclh lyhlnetvtv
       61 taslisqrgt rklfdelvvd kdlfhclsft iprlpsseee esldiniega khkfserrvv
      121 lvknkesvvf vqtdkpvykp gqsvkfrvvs mdknlhplne lfplayiedp kmnrimqwqd
      181 iktenglkql sfslsaepiq gpykivilkq sgvkeehsft vmefvlprfg vdvkvpnais
      241 vydeiinvta caiytygkpv pghvkislch gnpsfssetk sackeedsel dnngcstqev
      301 nitefqlken ylkmhqafhv natvteegtg sefsgsgrie vertrnkflf lkadshfrhg
      361 ipffvkirlv dikgdpipne qvfikaqeag ytnatttdqh glakfsidts sisgyslnik
      421 vyhkeessci hssctaerha eehhtayavy slsksyiyld teagvlpcnq ihtvqahfil
      481 kgqvlgvlpq ivfhylvmaq gsilqtgnht hqvepgvsqv qgnfaleipv efsmvpvakm
      541 liytilpdge viadsvtfqv ekclrnkvhl sfspsqslpa sqthmrvtas pqslcglrav
      601 dqsvlllkpe aelspsliyd lpgmqdsnfi pssyhpfede ydclmyqprd teeltysvpy
      661 grekdvyryv rdmgltaftn lkikhptycy emnmvvlsap aveselsprg gefemmplgv
      721 nksplpkepp rkdpppkdpv ietirnyfpe twiwdlvtvn ssgvtevemt vpdtitewka
      781 galclsndtg lglssvatlq afqpffvelt mpysvirgea fmlkatvmny lptslpmavq
      841 leaspdftav pvgndqdsyc lgangrhtss wlvtpkslgn vnfsvsveaq qspelcgsqv
      901 atvpetgrkd tvvkvlivep egikkehtfs sllcasdael setlslllpp tvvkdsarah
      961 fsvmgdilss aikntqnliq mpygcgeqnm vlfapniyvl kylnetqqlt ekikskalgy
     1021 lragyqreln ykhkdgsysa fgdhngqgqg ntwltafvlk sfaqarafif ideshitdaf
     1081 twlskqqkds gcfrssgslf nnamkggvdd eitlsayitm allesslpdt dpvvskalgc
     1141 leaswetieq grngsfvytk tlmayafala gnqekrneil ksldkeaire dnsihwerpq
     1201 kptksegyly tpqassaeve msayvvlarl taqpapsped lalsmgtikw ltkqqnshgg
     1261 fsstqdtvva ldalskygaa tfsksqktpl vtiqssgsfs qkfqvdnsnr lllqqvslpd
     1321 ipgnytvsvs gegcvyaqtt lrynmplekq qpafalkvqt vpltcnnpkg qnsfqislei
     1381 sytgsrpasn mviadvkmls gfiplkptvk klerlehvsr tevttnnvll yldqvtnqtl
     1441 sfsfiiqqdi pvknlqpaiv kvydyyetde vafaeysspc ssdkqnv
//
LOCUS       NP_001008358             723 aa            linear   ROD 27-APR-2025
DEFINITION  host cell factor 2 [Rattus norvegicus].
ACCESSION   NP_001008358 XP_235011
VERSION     NP_001008358.1
DBSOURCE    REFSEQ: accession NM_001008357.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   2  (residues 1 to 723)
  AUTHORS   Rizki,G., Iwata,T.N., Li,J., Riedel,C.G., Picard,C.L., Jan,M.,
            Murphy,C.T. and Lee,S.S.
  TITLE     The evolutionarily conserved longevity determinants HCF-1 and
            SIR-2.1/SIRT1 collaborate to regulate DAF-16/FOXO
  JOURNAL   PLoS Genet 7 (9), e1002235 (2011)
   PUBMED   21909281
REFERENCE   3  (residues 1 to 723)
  AUTHORS   Johnson,K.M., Mahajan,S.S. and Wilson,A.C.
  TITLE     Herpes simplex virus transactivator VP16 discriminates between
            HCF-1 and a novel family member, HCF-2
  JOURNAL   J Virol 73 (5), 3930-3940 (1999)
   PUBMED   10196288
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085951.1.
            
            On Dec 16, 2004 this sequence version replaced XP_235011.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085951.1, SRR8487231.21566.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..723
                     /product="host cell factor 2"
                     /note="HCF-2; C2 factor"
                     /calculated_mol_wt=79018
     Region          14..332
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          23..69
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          34..79
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG2.1)"
     Region          83..130
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG2.1)"
     Region          127..186
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          190..241
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          207..255
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG2.1)"
     Region          245..312
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          257..305
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG2.1)"
     Region          312..355
                     /region_name="Kelch_5"
                     /note="Kelch motif; pfam13854"
                     /db_xref="CDD:433528"
     Region          398..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG2.1)"
     Region          <549..603
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(592..593,595..596)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          609..709
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(609,682,703)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(704..705,707..708)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..723
                     /gene="Hcfc2"
                     /coded_by="NM_001008357.1:7..2178"
                     /db_xref="GeneID:314704"
                     /db_xref="RGD:1307385"
ORIGIN      
        1 maapsllnwr rvssftgpvp rarhghrava irelmiifgg gnegiadelh vyntvtnqwf
       61 lpavrgdipp gcaahgfvcd gtrilvfggm veygrysnel yelqasrwlw kkvkpqppps
      121 glppcprlgh sfslygnkcy lfaglanese dsnnnvpryl ndfyelelqh gsgvvgwsvp
      181 atkgtvpspr eshtaviyck rdsgspkmyv fggmcgarld dlwqldletm swskpetkgt
      241 vplprslhta svignkmyif ggwvphkgen tensphdcew rctssfsyln ldtaewttlv
      301 sdsqedkkns rprpraghca vaigtrlyfw sgrdgykkal nsqvcckdlw yldtekppap
      361 sqvqlikatt nsfhvkwdev ptvegyllql ntdlthqaas pdasaapntl ggrtdphrqg
      421 snsilhnsvs dpanctkpeh tavaargmsl kskpdsraad ssvalhspla pntsnnnscm
      481 admlwksevd eicalpatki srveahaaat pfsketpsnp vailkaeqwc dvgifknnta
      541 lvsqfyllpk gkqsmskvgn advpdysllk kqdlvpgtvy kfrvaaingc gigpfsklse
      601 fktcipgfpg apstvriskn vegihlswep ptspsgnile ysaylairta qvqdnpsqlv
      661 fmriycglkt scivtagqla nahidytsrp aivfrisakn ekgygpatqv rwlqgnskka
      721 pls
//
LOCUS       NP_445739                399 aa            linear   ROD 27-APR-2025
DEFINITION  beta-1,4-galactosyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_445739 XP_001058948 XP_342821
VERSION     NP_445739.1
DBSOURCE    REFSEQ: accession NM_053287.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Zhao,J., Gao,Y., Cheng,C., Yan,M. and Wang,J.
  TITLE     Upregulation of beta-1,4-galactosyltransferase I in rat spinal cord
            with experimental autoimmune encephalomyelitis
  JOURNAL   J Mol Neurosci 49 (3), 437-445 (2013)
   PUBMED   22706684
  REMARK    GeneRIF: beta-1,4-GalT-I may be an inflammatory mediator regulating
            adhesion & migration of inflammatory cells in EAE by modifying
            galactosylated carbohydrate chains to modulate selectin-ligand
            biosynthesis & interaction with E-selectin.
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Liu,X., Cheng,C., Shao,B., Wu,X., Ji,Y., Lu,X. and Shen,A.
  TITLE     The functional interaction between CDK11p58 and
            beta-1,4-galactosyltransferase I involved in astrocyte activation
            caused by lipopolysaccharide
  JOURNAL   Inflammation 35 (4), 1365-1377 (2012)
   PUBMED   22527143
  REMARK    GeneRIF: These findings indicated that the functional interaction
            between CDK11(p58) and beta-1,4-GalT-I may play an important role
            during astrocyte activation after LPS administration.
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Yuan,Q., Yang,H., Cheng,C., Li,C., Wu,X., Huan,W., Sun,H., Zhou,Z.,
            Wang,Y., Zhao,Y., Lu,X. and Shen,A.
  TITLE     beta-1,4-Galactosyltransferase I involved in Schwann cells
            proliferation and apoptosis induced by tumor necrosis factor-alpha
            via the activation of MAP kinases signal pathways
  JOURNAL   Mol Cell Biochem 365 (1-2), 149-158 (2012)
   PUBMED   22359038
  REMARK    GeneRIF: B4galt1 may play an important role in Schwann cell
            proliferation and apoptosis induced by tumor necrosis factor-alpha
            via different signal pathways and tumor necrosis factor receptors.
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Sato,T. and Furukawa,K.
  TITLE     [Regulation of human beta-1,4-galactosyltransferase V gene
            expression in cancer cells]
  JOURNAL   Yakugaku Zasshi 132 (6), 691-697 (2012)
   PUBMED   22687727
  REMARK    GeneRIF: The expression of the beta-1,4-GalT V gene has been shown
            to be regulated by transcription factors Sp1 and Ets-1 in cancer
            cells.(review)
            Review article
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Yamada,K.A. and Rothman,S.M.
  TITLE     Diazoxide blocks glutamate desensitization and prolongs excitatory
            postsynaptic currents in rat hippocampal neurons
  JOURNAL   J Physiol 458, 409-423 (1992)
   PUBMED   1302270
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Aoki,D., Appert,H.E., Johnson,D., Wong,S.S. and Fukuda,M.N.
  TITLE     Analysis of the substrate binding sites of human
            galactosyltransferase by protein engineering
  JOURNAL   EMBO J 9 (10), 3171-3178 (1990)
   PUBMED   2120039
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Lopez,L.C., Maillet,C.M., Oleszkowicz,K. and Shur,B.D.
  TITLE     Cell surface and Golgi pools of beta-1,4-galactosyltransferase are
            differentially regulated during embryonal carcinoma cell
            differentiation
  JOURNAL   Mol Cell Biol 9 (6), 2370-2377 (1989)
   PUBMED   2503706
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Roth,J., Lentze,M.J. and Berger,E.G.
  TITLE     Immunocytochemical demonstration of ecto-galactosyltransferase in
            absorptive intestinal cells
  JOURNAL   J Cell Biol 100 (1), 118-125 (1985)
   PUBMED   3917437
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Gerber,A.C., Kozdrowski,I., Wyss,S.R. and Berger,E.G.
  TITLE     The charge heterogeneity of soluble human galactosyltransferases
            isolated from milk, amniotic fluid and malignant ascites
  JOURNAL   Eur J Biochem 93 (3), 453-460 (1979)
   PUBMED   33805
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AA818683.1, AA956551.1, AI709691.1, CB741712.1, CB736416.1 and
            CK364907.1.
            
            On or before Oct 11, 2007 this sequence version replaced
            XP_342821.1, XP_001058948.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16676811
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..399
                     /product="beta-1,4-galactosyltransferase 1"
                     /EC_number="2.4.1.22"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /EC_number="2.4.1.275"
                     /note="b4Gal-T1; beta4Gal-T1; beta-1,4-GalTase 1;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 1;
                     Glycoprotein-4-beta-galactosyltransferase 2;
                     UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,
                     polypeptide 1; nal synthase; lactose synthase A protein;
                     N-acetyllactosamine synthase;
                     beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase; neolactotriaosylceramide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=44353
     Region          176..394
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(184,186,188,223,249..251)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(249,251,344)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..399
                     /gene="B4galt1"
                     /gene_synonym="Ggtb2"
                     /coded_by="NM_053287.1:219..1418"
                     /db_xref="GeneID:24390"
                     /db_xref="RGD:620900"
ORIGIN      
        1 mrfrepflgg saampgatlq racrllvavc alhlgvtlvy ylsgrdlsrl pqlvgvsssl
       61 qggtngaaas kqpsgelrpr garpppplgv spkprpgsds spdaasgpgl ksnltsvpmp
      121 tstglltlpa cpeespllvg pmvidfnipv dlellakknp eikmggryfp kdcisphkva
      181 iiipfrnrqe hlkywlyylh pvlqrqqldy giyvinqagd tmfnraklln vgfqealkdy
      241 dyncfvfsdv dlipmddhna yrcfsqprhi svamdkfgfs lpyvqyfggv salskqqflt
      301 ingfpnnywg wggedddifn rlvhkgmsis rpnavvgrcr mirhsrdkkn epnpqrfdri
      361 ahtketmrld glnsltyqvl diqryplytk itvdigtpr
//
LOCUS       NP_001037691             258 aa            linear   ROD 27-APR-2025
DEFINITION  RBPJ-interacting and tubulin-associated protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001037691 XP_001079864 XP_213787
VERSION     NP_001037691.1
DBSOURCE    REFSEQ: accession NM_001044226.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wacker,S.A., Alvarado,C., von Wichert,G., Knippschild,U.,
            Wiedenmann,J., Clauss,K., Nienhaus,G.U., Hameister,H., Baumann,B.,
            Borggrefe,T., Knochel,W. and Oswald,F.
  TITLE     RITA, a novel modulator of Notch signalling, acts via nuclear
            export of RBP-J
  JOURNAL   EMBO J 30 (1), 43-56 (2011)
   PUBMED   21102556
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC112384.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_213787.2, XP_001079864.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..258
                     /product="RBPJ-interacting and tubulin-associated protein
                     1"
                     /calculated_mol_wt=28017
     Region          1..258
                     /region_name="RITA"
                     /note="RBPJ-interacting and tubulin associated protein;
                     pfam17066"
                     /db_xref="CDD:465342"
     Region          28..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     Region          81..97
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     Region          117..145
                     /region_name="Interaction with RBPJ/RBPSUH.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     Region          132..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     Region          145..258
                     /region_name="Interaction with tubulin.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     Region          195..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ10.1)"
     CDS             1..258
                     /gene="Rita1"
                     /gene_synonym="RGD1306772; Rita"
                     /coded_by="NM_001044226.1:442..1218"
                     /db_xref="GeneID:288683"
                     /db_xref="RGD:1306772"
ORIGIN      
        1 mqalhlqhrn prsyrvkara syvdetlfgs ptgtrptlpd fdppwvqncn rsrgvspgpp
       61 kvslakrdce spssrgstpn ltprkknkyr lightpsycd eslfgsrpqg tskersrtav
      121 edaaklrtlf wtppatprgs hsprpretpl raihptgppr teprvatgsq mvsrdgldap
      181 rslgqrrsys lthlavpstg hpastapqtn gpwsprpyts gatvqsplvt rkvcsgsvsg
      241 pttpqrgacp qkpkppwk
//
LOCUS       NP_001012086             359 aa            linear   ROD 27-APR-2025
DEFINITION  cytohesin-interacting protein [Rattus norvegicus].
ACCESSION   NP_001012086 XP_229936
VERSION     NP_001012086.1
DBSOURCE    REFSEQ: accession NM_001012086.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Boehm,T., Hofer,S., Winklehner,P., Kellersch,B., Geiger,C.,
            Trockenbacher,A., Neyer,S., Fiegl,H., Ebner,S., Ivarsson,L.,
            Schneider,R., Kremmer,E., Heufler,C. and Kolanus,W.
  TITLE     Attenuation of cell adhesion in lymphocytes is regulated by CYTIP,
            a protein which mediates signal complex sequestration
  JOURNAL   EMBO J 22 (5), 1014-1024 (2003)
   PUBMED   12606567
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088207.1.
            
            On Feb 11, 2005 this sequence version replaced XP_229936.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088207.1, CO559105.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..359
                     /product="cytohesin-interacting protein"
                     /note="pleckstrin homology Sec7 and coiled-coil
                     domain-binding protein; pleckstrin homology, Sec7 and
                     coiled-coil domains, binding protein"
                     /calculated_mol_wt=39826
     Region          73..163
                     /region_name="PDZ_tamalin_CYTIP-like"
                     /note="PDZ domain of tamalin, cytohesin-1-interacting
                     protein (CYTIP), and related domains; cd06713"
                     /db_xref="CDD:467197"
     Site            order(87..93,112,115,144,148,151..152)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467197"
     Region          166..188
                     /region_name="Interaction with CYTH1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0L6.1)"
     CDS             1..359
                     /gene="Cytip"
                     /gene_synonym="Pscdbp"
                     /coded_by="NM_001012086.1:48..1127"
                     /db_xref="GeneID:311047"
                     /db_xref="RGD:1307990"
ORIGIN      
        1 mslqrllqqq ssngnleyca dsayssyptl tgpltvednr riqmladtva tlprgrkqla
       61 larssslgdf scsqrkvvtv ekqdngtfgf eiqtyrlqnq nicssevctm ickvqedspa
      121 hcaglqvgdi fanvngvste gfthkqvvdl irssgnllti etlngtmihr raeleaklqt
      181 lkqtlkkkwv elrslhlqeq rllhgdaans pnlenmnlde sslfgnllgp spafldrprl
      241 ssessckswl ssltvdsedd ygtsvsedsi rgafsrqtst ddecfhskdg deilrnassr
      301 rnrsisitss gsfsplwesn yssvfgtlpr ksrrgsvrkq ilkfipglhr aveeeesrf
//
LOCUS       NP_113818                483 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX25 [Rattus norvegicus].
ACCESSION   NP_113818
VERSION     NP_113818.2
DBSOURCE    REFSEQ: accession NM_031630.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Onohara,Y. and Yokota,S.
  TITLE     Expression of DDX25 in nuage components of mammalian spermatogenic
            cells: immunofluorescence and immunoelectron microscopic study
  JOURNAL   Histochem Cell Biol 137 (1), 37-51 (2012)
   PUBMED   22038044
  REMARK    GeneRIF: The results suggest that DDX25 functions in meiotic
            cells,intermitochondrial cement,loose aggregates of
            particles,chromatoid bodies,late chromatoid bodies,satellite
            bodies,granulated bodies,mitochondria-associated granules and
            reticulated bodies.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Dufau,M.L., Sato,H., Gutti,R. and Tsai-Morris,C.H.
  TITLE     Gonadotropin-regulated testicular helicase (GRTH/DDX25): a master
            post-transcriptional regulator of spermatogenesis
  JOURNAL   Adv Exp Med Biol 707, 23-29 (2011)
   PUBMED   21691948
  REMARK    GeneRIF: studies on GRTH [proide insights into the intrinsic
            requirements of spermatogenesis and open new avenues for studies on
            regulating spermatogenesis, infertility and male contraception
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Sheng,Y., Tsai-Morris,C.H., Gutti,R., Maeda,Y. and Dufau,M.L.
  TITLE     Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is a
            transport protein involved in gene-specific mRNA export and protein
            translation during spermatogenesis
  JOURNAL   J Biol Chem 281 (46), 35048-35056 (2006)
   PUBMED   16968703
  REMARK    GeneRIF: The results of this study indicate that the mammalian
            GRTH/Ddx25 gene is a multifunctional RNA helicase that is an
            essential regulator of sperm maturation.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Tsai-Morris,C.H., Sheng,Y., Lee,E., Lei,K.J. and Dufau,M.L.
  TITLE     Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is
            essential for spermatid development and completion of
            spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 101 (17), 6373-6378 (2004)
   PUBMED   15096601
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Sheng,Y., Tsai-Morris,C.H. and Dufau,M.L.
  TITLE     Cell-specific and hormone-regulated expression of
            gonadotropin-regulated testicular RNA helicase gene (GRTH/Ddx25)
            resulting from alternative utilization of translation initiation
            codons in the rat testis
  JOURNAL   J Biol Chem 278 (30), 27796-27803 (2003)
   PUBMED   12734186
  REMARK    GeneRIF: expression is regulated by gonadotropin/androgen at the
            translational level
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Tang,P.Z., Tsai-Morris,C.H. and Dufau,M.L.
  TITLE     A novel gonadotropin-regulated testicular RNA helicase. A new
            member of the dead-box family
  JOURNAL   J Biol Chem 274 (53), 37932-37940 (1999)
   PUBMED   10608860
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF142629.2.
            
            On Jul 24, 2003 this sequence version replaced NP_113818.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF142629.2, BC078791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..483
                     /product="ATP-dependent RNA helicase DDX25"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 25; gonadotropin-regulated
                     testicular RNA helicase; DEAD
                     (aspartate-glutamate-alanine-aspartate) box polypeptide
                     25; DEAD (Asp-Glu-Ala-Asp) box polypeptide 25; DEAD
                     (Asp-Glu-Ala-Asp) box helicase 25"
                     /calculated_mol_wt=54660
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QY15; propagated from
                     UniProtKB/Swiss-Prot (Q9QY16.2)"
     Region          61..74
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY16.2)"
     Region          80..308
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          97..125
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY16.2)"
     Region          100..114
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:16968703"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY16.2)"
     Site            order(145..151,247)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          247..250
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QY16.2)"
     Region          312..448
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(401,403,434,437..438)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..483
                     /gene="Ddx25"
                     /gene_synonym="GRTH"
                     /coded_by="NM_031630.2:26..1477"
                     /db_xref="GeneID:58856"
                     /db_xref="RGD:68381"
ORIGIN      
        1 masllwggda gaaeserlns hfsnlvhprk nlrgirsttv pnidgslnte edddeddvvd
       61 laansllnkl irqslvessh rvevlqkdps splysvktfe elrlkeellk giyamgfnrp
      121 skiqemalpm mlahppqnli aqsqsgtgkt aafvlamlnr vnalelfpqc lclaptyela
      181 lqtgrvverm gkfcvdvevm yairgnripr gtdvtkqivi gtpgtvldwc fkrklidltk
      241 irvfvldead vmidtqgfsd qsiriqralp secqmllfsa tfedsvwqfa eriipdpnvi
      301 klrkeeltln nirqyyvlce nrkdkyqalc niyggitigq aiifcqtrrn akwltvemmq
      361 dghqvsllsg eltveqrasi iqrfrdgkek vlittnvcar gidvkqvtiv vnfdlpvnqs
      421 eepdyetylh rigrtgrfgk kglafnmiev dklpllmkiq dhfnssikql dpedmdeiek
      481 iey
//
LOCUS       NP_001099760             148 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL15 [Rattus norvegicus].
ACCESSION   NP_001099760 XP_001077420 XP_215041
VERSION     NP_001099760.1
DBSOURCE    REFSEQ: accession NM_001106290.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Wool,I.G., Chan,Y.L., Paz,V. and Olvera,J.
  TITLE     The primary structure of rat ribosomal proteins: the amino acid
            sequences of L27a and L28 and corrections in the sequences of S4
            and S12
  JOURNAL   Biochim Biophys Acta 1050 (1-3), 69-73 (1990)
   PUBMED   2207170
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Fleming,G., Belhumeur,P., Skup,D. and Fried,H.M.
  TITLE     Functional substitution of mouse ribosomal protein L27' for yeast
            ribosomal protein L29 in yeast ribosomes
  JOURNAL   Proc Natl Acad Sci U S A 86 (1), 217-221 (1989)
   PUBMED   2643099
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Tsurugi,K., Collatz,E., Todokoro,K. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of 60 S ribosomal subunit proteins L3, L6, L7',
            L8, L10, L15, L17, L18, L19, L23', L25, L27', L28, L29, L31, L32,
            L34, L35, L36, L36', and L37'
  JOURNAL   J Biol Chem 252 (11), 3961-3969 (1977)
   PUBMED   863909
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473956.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_215041.4, XP_001077420.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB313343.1, FQ144030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..148
                     /product="large ribosomal subunit protein uL15"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L27a"
                     /calculated_mol_wt=16487
     Region          1..148
                     /region_name="PTZ00160"
                     /note="60S ribosomal protein L27a; Provisional"
                     /db_xref="CDD:185489"
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18445.3)"
     Site            39
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyhistidine.
                     /evidence=ECO:0000250|UniProtKB:P46776; propagated from
                     UniProtKB/Swiss-Prot (P18445.3)"
     Site            47
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P46776; propagated from
                     UniProtKB/Swiss-Prot (P18445.3)"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P46776; propagated from
                     UniProtKB/Swiss-Prot (P18445.3)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46776; propagated from
                     UniProtKB/Swiss-Prot (P18445.3)"
     Site            110
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P46776; propagated from
                     UniProtKB/Swiss-Prot (P18445.3)"
     CDS             1..148
                     /gene="Rpl27a"
                     /coded_by="NM_001106290.1:29..475"
                     /db_xref="GeneID:293418"
                     /db_xref="RGD:1309771"
ORIGIN      
        1 mpsrlrktrk lrghvshghg rigkhrkhpg grgnaggmhh hrinfdkyhp gyfgkvgmrh
       61 yhlkrnqsfc ptvnldklwt lvseqtrvna aknkngvapi idvvrsgyyk vlgkgklpkq
      121 pvivkakffs rraeekikgv ggacvlva
//
LOCUS       NP_001009603             319 aa            linear   ROD 27-APR-2025
DEFINITION  N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
            [Rattus norvegicus].
ACCESSION   NP_001009603 XP_215159
VERSION     NP_001009603.1
DBSOURCE    REFSEQ: accession NM_001009603.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Tsirulnikov,K., Abuladze,N., Vahi,R., Hasnain,H., Phillips,M.,
            Ryan,C.M., Atanasov,I., Faull,K.F., Kurtz,I. and Pushkin,A.
  TITLE     Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis
            C virus core protein
  JOURNAL   FEBS Lett 586 (21), 3799-3804 (2012)
   PUBMED   23010594
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Tsirulnikov,K., Abuladze,N., Bragin,A., Faull,K., Cascio,D.,
            Damoiseaux,R., Schibler,M.J. and Pushkin,A.
  TITLE     Inhibition of aminoacylase 3 protects rat brain cortex neuronal
            cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and
            4-hydroxy-2-nonenal
  JOURNAL   Toxicol Appl Pharmacol 263 (3), 303-314 (2012)
   PUBMED   22819785
  REMARK    GeneRIF: we report a new potential mechanism for neuronal damage in
            Alzheimer disease that involves AA3; This previously unrecognized
            mechanism may also function in Parkinson disease
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Hsieh,J.M., Tsirulnikov,K., Sawaya,M.R., Magilnick,N., Abuladze,N.,
            Kurtz,I., Abramson,J. and Pushkin,A.
  TITLE     Structures of aminoacylase 3 in complex with acetylated substrates
  JOURNAL   Proc Natl Acad Sci U S A 107 (42), 17962-17967 (2010)
   PUBMED   20921362
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Ryazantsev,S., Abuladze,N., Newman,D., Bondar,G., Kurtz,I. and
            Pushkin,A.
  TITLE     Structural characterization of dimeric murine aminoacylase III
  JOURNAL   FEBS Lett 581 (9), 1898-1902 (2007)
   PUBMED   17434493
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Pushkin,A., Carpenito,G., Abuladze,N., Newman,D., Tsuprun,V.,
            Ryazantsev,S., Motemoturu,S., Sassani,P., Solovieva,N.,
            Dukkipati,R. and Kurtz,I.
  TITLE     Structural characterization, tissue distribution, and functional
            expression of murine aminoacylase III
  JOURNAL   Am J Physiol Cell Physiol 286 (4), C848-C856 (2004)
   PUBMED   14656720
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088190.1.
            
            On Jan 13, 2005 this sequence version replaced XP_215159.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..319
                     /product="N-acyl-aromatic-L-amino acid amidohydrolase
                     (carboxylate-forming)"
                     /EC_number="3.5.1.114"
                     /note="aspartoacylase 3; aspartoacylase-2; ACY-3;
                     aspartoacylase (aminoacylase) 3; aspartoacylase
                     (aminocyclase) 3"
                     /calculated_mol_wt=35288
     Region          1..210
                     /region_name="Hydrolytic domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M876.1)"
     Region          13..303
                     /region_name="Peptidase_M14_like"
                     /note="M14 family of metallocarboxypeptidases and related
                     proteins; cl11393"
                     /db_xref="CDD:472171"
     Site            order(21,24,63,70..71,116..117,127,164,168,178)
                     /site_type="active"
                     /db_xref="CDD:349480"
     Region          211..318
                     /region_name="Shielding domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M876.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M876.1)"
     CDS             1..319
                     /gene="Acy3"
                     /gene_synonym="RGD1305394"
                     /coded_by="NM_001009603.1:195..1154"
                     /db_xref="GeneID:293653"
                     /db_xref="RGD:1305394"
ORIGIN      
        1 mcslpgsrkp llrvavtggt hgnemcgvyl arywlqnpge lqrpsfsamp vlanpaataa
       61 crryidrdln rtftltflgs tatpddpyev kraqelnqll gpkgtcqafd fildlhntta
      121 ntgaclisev sqnpfnlhlc hylqlqnpgl pcrlfqfepp gtesysmdsv skngislelg
      181 pqpqgvlrae lfsqmramva sildfielfn qgmefpafem evyknlgsvd fprttdghlt
      241 gtvhsrlqdh dfeplrpgep ifklfsgedv lyegdsvvyp lfvneaayye krvaflksek
      301 irisvpalpg ltpsstqtp
//
LOCUS       NP_001013145             199 aa            linear   ROD 27-APR-2025
DEFINITION  transgelin-2 [Rattus norvegicus].
ACCESSION   NP_001013145 XP_222906
VERSION     NP_001013145.1
DBSOURCE    REFSEQ: accession NM_001013127.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Buhrke,T., Lengler,I. and Lampen,A.
  TITLE     Analysis of proteomic changes induced upon cellular differentiation
            of the human intestinal cell line Caco-2
  JOURNAL   Dev Growth Differ 53 (3), 411-426 (2011)
   PUBMED   21492153
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC084703.1.
            
            On Apr 20, 2005 this sequence version replaced XP_222906.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084703.1, FQ223112.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..199
                     /product="transgelin-2"
                     /calculated_mol_wt=22262
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Region          18..154
                     /region_name="CH_TAGLN2"
                     /note="calponin homology (CH) domain found in
                     transgelin-2; cd21280"
                     /db_xref="CDD:409129"
     Site            20
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Site            order(26,30,88,90..91,94..95,97,107..115,121,123..124,
                     126..127,130..131,134)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409129"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Region          174..199
                     /region_name="Calponin-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Region          174..198
                     /region_name="Calponin"
                     /note="Calponin family repeat; pfam00402"
                     /db_xref="CDD:459803"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Site            182
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     Site            196
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P37802; propagated from
                     UniProtKB/Swiss-Prot (Q5XFX0.1)"
     CDS             1..199
                     /gene="Tagln2"
                     /coded_by="NM_001013127.1:55..654"
                     /db_xref="GeneID:304983"
                     /db_xref="RGD:1310840"
ORIGIN      
        1 manrgpsygl srevqqkiek qydpdleqil iqwittqcrk gvsqpqpgre nfqnwlkdgt
       61 vlcelinsly pegqapvkki qastmafkqm eqisqflqaa eryginttdi fqtvdlwegk
      121 nmacvqrtlm nlgglavard dglfsgdpnw fpkkskenpr nfsdnqlqeg knviglqmgt
      181 nrgasqagmt gygmprqil
//
LOCUS       NP_001032273             414 aa            linear   ROD 27-APR-2025
DEFINITION  bifunctional peptidase and arginyl-hydroxylase JMJD5 [Rattus
            norvegicus].
ACCESSION   NP_001032273 XP_219312
VERSION     NP_001032273.1
DBSOURCE    REFSEQ: accession NM_001037196.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Saran,A.R., Kalinowska,D., Oh,S., Janknecht,R. and DiTacchio,L.
  TITLE     JMJD5 links CRY1 function and proteasomal degradation
  JOURNAL   PLoS Biol 16 (11), e2006145 (2018)
   PUBMED   30500822
  REMARK    Erratum:[PLoS Biol. 2019 Aug 21;17(8):e3000454. doi:
            10.1371/journal.pbio.3000454. PMID: 31433800]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Liu,H., Wang,C., Lee,S., Deng,Y., Wither,M., Oh,S., Ning,F.,
            Dege,C., Zhang,Q., Liu,X., Johnson,A.M., Zang,J., Chen,Z.,
            Janknecht,R., Hansen,K., Marrack,P., Li,C.Y., Kappler,J.W.,
            Hagman,J. and Zhang,G.
  TITLE     Clipping of arginine-methylated histone tails by JMJD5 and JMJD7
  JOURNAL   Proc Natl Acad Sci U S A 114 (37), E7717-E7726 (2017)
   PUBMED   28847961
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Black,J.C., Van Rechem,C. and Whetstine,J.R.
  TITLE     Histone lysine methylation dynamics: establishment, regulation, and
            biological impact
  JOURNAL   Mol Cell 48 (4), 491-507 (2012)
   PUBMED   23200123
  REMARK    Review article
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Wang,Z., Wang,C., Huang,X., Shen,Y., Shen,J. and Ying,K.
  TITLE     Differential proteome profiling of pleural effusions from lung
            cancer and benign inflammatory disease patients
  JOURNAL   Biochim Biophys Acta 1824 (4), 692-700 (2012)
   PUBMED   22326748
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Hsia,D.A., Tepper,C.G., Pochampalli,M.R., Hsia,E.Y., Izumiya,C.,
            Huerta,S.B., Wright,M.E., Chen,H.W., Kung,H.J. and Izumiya,Y.
  TITLE     KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1
            coding region to regulate cancer cell proliferation
  JOURNAL   Proc Natl Acad Sci U S A 107 (21), 9671-9676 (2010)
   PUBMED   20457893
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100627.1.
            
            On Nov 18, 2005 this sequence version replaced XP_219312.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100627.1, SRR8487227.244427.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..414
                     /product="bifunctional peptidase and arginyl-hydroxylase
                     JMJD5"
                     /EC_number="1.14.11.73"
                     /note="jmjC domain-containing protein 5; lysine
                     (K)-specific demethylase 8; lysine-specific demethylase 8;
                     jumonji domain-containing protein 5; jumonji domain
                     containing 5; arginyl C3-hydroxylase KDM8; jumonji C
                     domain-containing protein 5; L-arginine (3R)-hydroxylase
                     KDM8"
                     /calculated_mol_wt=47116
     Region          1..107
                     /region_name="Interaction with RCCD1.
                     /evidence=ECO:0000250|UniProtKB:Q8N371"
                     /note="propagated from UniProtKB/Swiss-Prot (Q497B8.1)"
     Region          152..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q497B8.1)"
     Region          189..414
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     CDS             1..414
                     /gene="Kdm8"
                     /gene_synonym="Jmjd5; RGD1304823"
                     /coded_by="NM_001037196.1:274..1518"
                     /db_xref="GeneID:308976"
                     /db_xref="RGD:1304823"
ORIGIN      
        1 msedtteplv gpstlwkdlr allpdteeel kldlsekvdr smatllrqal glfyegrwqk
       61 clqaseavld ysweklntgp wrdvdkewrr vysfgcllkt lclcqapqka tavaealrvc
      121 dmgllmgaai lgdillkvat vlqthllprk qpacgphqdq patkkakhda sstpdvvldr
      181 evprlrcppl qhfkkhflvp grpvilegva dhwpcmkkws lqyiqeiagc rtvpvevgsr
      241 ytdedwsqtl mtvnefihky ilseakdvgy laqhqlfdqi pelkqdisip dycclgngee
      301 eeitinawfg pqgtisplhq dpqqnflvqv lgrkyirlys pqeseavyph ethilhntsq
      361 vdvenpdlek fpkfteapfl scilspgdtl fipakywhyv rsldlsfsvs fwws
//
LOCUS       NP_076464                265 aa            linear   ROD 27-APR-2025
DEFINITION  synaptoporin precursor [Rattus norvegicus].
ACCESSION   NP_076464
VERSION     NP_076464.1
DBSOURCE    REFSEQ: accession NM_023974.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Lee,K.J., Queenan,B.N., Rozeboom,A.M., Bellmore,R., Lim,S.T.,
            Vicini,S. and Pak,D.T.
  TITLE     Mossy fiber-CA3 synapses mediate homeostatic plasticity in mature
            hippocampal neurons
  JOURNAL   Neuron 77 (1), 99-114 (2013)
   PUBMED   23312519
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Dai,J., Ji,C., Gu,S., Wu,Q., Wang,L., Xu,J., Zeng,L., Ye,X.,
            Yin,G., Xie,Y. and Mao,Y.
  TITLE     Cloning and sequence analysis of the human cDNA encoding the
            synaptoporin (delta), a highly conservative synaptic vesicle
            protein
  JOURNAL   Mol Biol Rep 30 (3), 185-191 (2003)
   PUBMED   12974474
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Knaus,P., Marqueze-Pouey,B., Scherer,H. and Betz,H.
  TITLE     Synaptoporin, a novel putative channel protein of synaptic vesicles
  JOURNAL   Neuron 5 (4), 453-462 (1990)
   PUBMED   2206533
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF306459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF306459.1, FQ101854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN14984024
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16-p15"
     Protein         1..265
                     /product="synaptoporin precursor"
                     /note="synaptorin"
                     /calculated_mol_wt=27015
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2111
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22831.2)"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22831.2)"
     Region          69..196
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22831.2)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     Region          210..242
                     /region_name="5 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22831.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P22831.2)"
     Region          221..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22831.2)"
     CDS             1..265
                     /gene="Synpr"
                     /coded_by="NM_023974.1:263..1060"
                     /db_xref="GeneID:66030"
                     /db_xref="RGD:708366"
ORIGIN      
        1 mcmvifaplf aifafatcgg ysgglrlsvd cvnktesnls idiafaypfr lhqvtfevpt
       61 cegkerqkla lvgdssssae ffvtvavfaf lyslaatvvy iffqnkyren nrgplidfiv
      121 tvvfsflwlv gssawakgls dvkvatdpke vlllmsackq psnkcmavhs pvmsslntsv
      181 vfgflnfilw agniwfvfke tgwhssgqry lsdpmekhss synqggynqd sygssggysq
      241 qaslgptsde fgqqpsgpts fnnqi
//
LOCUS       NP_446307                687 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 8 [Rattus norvegicus].
ACCESSION   NP_446307 XP_001074708 XP_343177
VERSION     NP_446307.1
DBSOURCE    REFSEQ: accession NM_053855.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Asirvatham,A.L., Schworer,C.M., Stahl,R., Heitzman,D. and
            Carey,D.J.
  TITLE     Role of A-kinase anchoring proteins in cyclic-AMP-mediated Schwann
            cell proliferation
  JOURNAL   Cell Signal 83, 109977 (2021)
   PUBMED   33716104
  REMARK    GeneRIF: Role of A-kinase anchoring proteins in cyclic-AMP-mediated
            Schwann cell proliferation.
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Marstad,A., Landsverk,O.J., Stromme,O., Otterlei,M., Collas,P.,
            Sundan,A. and Brede,G.
  TITLE     A-kinase anchoring protein AKAP95 is a novel regulator of ribosomal
            RNA synthesis
  JOURNAL   FEBS J 283 (4), 757-770 (2016)
   PUBMED   26683827
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Gao,X., Chaturvedi,D. and Patel,T.B.
  TITLE     Localization and retention of p90 ribosomal S6 kinase 1 in the
            nucleus: implications for its function
  JOURNAL   Mol Biol Cell 23 (3), 503-515 (2012)
   PUBMED   22130794
  REMARK    GeneRIF: new insights into how AKAP95 orchestrates cell cycle
            progression.
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Jungmann,R.A. and Kiryukhina,O.
  TITLE     Cyclic AMP and AKAP-mediated targeting of protein kinase A
            regulates lactate dehydrogenase subunit A mRNA stability
  JOURNAL   J Biol Chem 280 (26), 25170-25177 (2005)
   PUBMED   15878851
  REMARK    GeneRIF: lactate dehydrogenase subunit A mRNA stability is
            regulated by Cyclic AMP and AKAP-mediated targeting of protein
            kinase A
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Tasken,K. and Aandahl,E.M.
  TITLE     Localized effects of cAMP mediated by distinct routes of protein
            kinase A
  JOURNAL   Physiol Rev 84 (1), 137-167 (2004)
   PUBMED   14715913
  REMARK    Review article
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Bomar,J., Moreira,P., Balise,J.J. and Collas,P.
  TITLE     Differential regulation of maternal and paternal chromosome
            condensation in mitotic zygotes
  JOURNAL   J Cell Sci 115 (Pt 14), 2931-2940 (2002)
   PUBMED   12082153
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Akileswaran,L., Taraska,J.W., Sayer,J.A., Gettemy,J.M. and
            Coghlan,V.M.
  TITLE     A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix
            and associates with p68 RNA helicase
  JOURNAL   J Biol Chem 276 (20), 17448-17454 (2001)
   PUBMED   11279182
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Coghlan,V.M., Langeberg,L.K., Fernandez,A., Lamb,N.J. and
            Scott,J.D.
  TITLE     Cloning and characterization of AKAP 95, a nuclear protein that
            associates with the regulatory subunit of type II cAMP-dependent
            protein kinase
  JOURNAL   J Biol Chem 269 (10), 7658-7665 (1994)
   PUBMED   8125992
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166580.1.
            
            On or before Sep 7, 2008 this sequence version replaced
            XP_343177.1, XP_001074708.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166580.1, U01914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..687
                     /product="A-kinase anchor protein 8"
                     /note="A kinase (PRKA) anchor protein 8; AKAP 95; A-kinase
                     anchor protein 95 kDa; AKAP-8"
                     /calculated_mol_wt=76031
     Region          1..210
                     /region_name="Interaction with DPY30.
                     /evidence=ECO:0000250|UniProtKB:O43823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          1..195
                     /region_name="Interaction with MCM2.
                     /evidence=ECO:0000250|UniProtKB:O43823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Region          104..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          109..201
                     /region_name="Interaction with DDX5.
                     /evidence=ECO:0000269|PubMed:11279182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            109
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Region          127..152
                     /region_name="Nuclear matrix targeting site.
                     /evidence=ECO:0000305|PubMed:11279182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          189..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43823; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Site            233
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Site            277
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O43823; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Region          278..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          287..304
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O43823,
                     ECO:0000269|PubMed:11279182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Region          385..448
                     /region_name="Involved in chromatin-binding.
                     /evidence=ECO:0000250|UniProtKB:O43823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          413..544
                     /region_name="AKAP95"
                     /note="A-kinase anchoring protein 95 (AKAP95); pfam04988"
                     /db_xref="CDD:461509"
     Region          523..565
                     /region_name="Involved in condensin complex recruitment.
                     /evidence=ECO:0000250|UniProtKB:O43823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     Region          568..585
                     /region_name="RII-binding.
                     /evidence=ECO:0000305|PubMed:8125992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          572..589
                     /region_name="Required for interaction with MYCBP.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Region          606..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63014.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63014.1)"
     CDS             1..687
                     /gene="Akap8"
                     /gene_synonym="Akap95"
                     /coded_by="NM_053855.1:26..2089"
                     /db_xref="GeneID:116633"
                     /db_xref="RGD:620832"
ORIGIN      
        1 meqsyggyga wsagpantqg tygsgvaswq gyenysyyna qntsvptgtp ysygpaswea
       61 tkasdgglaa gssamhvasf apepctdnsd sliakinqrl dmlskeggrg gissggegmq
      121 drdssfrfqp yesydsrpcm pehtpyrpsy sydydfdlgt drngsfggtf ndcrdptper
      181 galdgflrgr gqgrfqdrsn sstfirsdpf mppsassepl sttwselnym ggrglggpst
      241 nrpppslfsq smapdysmmg mqgvggfggt mpygcgrsqt rirdwprrrg ferfgpdnmg
      301 rkrkpfplye epdaklarad segdlsendd gagdlrsgde efrgeddlcd srkqrgeked
      361 ededvkkrre kqrrrdrmrd raadriqfac svckfrsfed eeiqkhlqsk fhketlrfis
      421 tklpdktvef lqeyiinrnk kiekrrqell ekespkpkpd pfkgigqehf fkrieaahcl
      481 acdmlipaqh qllqrhlhsv dhnhnrrlaa eqfkktslhv aksvlnnkhi vkmlekylkg
      541 edpfvnetad letegdenlg eeketpeeva aevlaevita avkavegdge paaehsdvla
      601 evegpvdtae agsdshtgkl leeqtcetas etrnmedmar geaaearnea avpaaaagsp
      661 vpviaipgil edeleqtdae akdtpte
//
LOCUS       NP_653360                432 aa            linear   ROD 27-APR-2025
DEFINITION  acetylserotonin O-methyltransferase [Rattus norvegicus].
ACCESSION   NP_653360
VERSION     NP_653360.2
DBSOURCE    REFSEQ: accession NM_144759.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Paiva,R.V.N., Mondes,P.H.L., Brandao,B.J., Sant'Anna,J.N., Freire
            Dos Santos,M.E., Fighera,Y.M., Santos,L.C., Markus,R.P.,
            Fernandes,P.A.C.M., Silva,J.F. and Tamura,E.K.
  TITLE     Effects of acute hypothyroidism on plasma melatonin and Aanat and
            Asmt expression in the pineal gland and gonads of rats
  JOURNAL   Front Endocrinol (Lausanne) 15, 1322867 (2024)
   PUBMED   39149125
  REMARK    GeneRIF: Effects of acute hypothyroidism on plasma melatonin and
            Aanat and Asmt expression in the pineal gland and gonads of rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Coelho,L.A., Andrade-Silva,J., Motta-Teixeira,L.C., Amaral,F.G.,
            Reiter,R.J. and Cipolla-Neto,J.
  TITLE     The Absence of Pineal Melatonin Abolishes the Daily Rhythm of Tph1
            (Tryptophan Hydroxylase 1), Asmt (Acetylserotonin
            O-Methyltransferase), and Aanat (Aralkylamine N-Acetyltransferase)
            mRNA Expressions in Rat Testes
  JOURNAL   Mol Neurobiol 56 (11), 7800-7809 (2019)
   PUBMED   31124080
  REMARK    GeneRIF: The testes of control animals express the Tph1, Aanat, and
            Asmt and Per2 genes with 24-h rhythms in mRNA, reaching the maximal
            values during the dark phase.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Rath,M.F., Coon,S.L., Amaral,F.G., Weller,J.L., Moller,M. and
            Klein,D.C.
  TITLE     Melatonin Synthesis: Acetylserotonin O-Methyltransferase (ASMT) Is
            Strongly Expressed in a Subpopulation of Pinealocytes in the Male
            Rat Pineal Gland
  JOURNAL   Endocrinology 157 (5), 2028-2040 (2016)
   PUBMED   26950199
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Botros,H.G., Legrand,P., Pagan,C., Bondet,V., Weber,P.,
            Ben-Abdallah,M., Lemiere,N., Huguet,G., Bellalou,J., Maronde,E.,
            Beguin,P., Haouz,A., Shepard,W. and Bourgeron,T.
  TITLE     Crystal structure and functional mapping of human ASMT, the last
            enzyme of the melatonin synthesis pathway
  JOURNAL   J Pineal Res 54 (1), 46-57 (2013)
   PUBMED   22775292
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Shimozuma,M., Tokuyama,R., Tatehara,S., Umeki,H., Ide,S.,
            Mishima,K., Saito,I. and Satomura,K.
  TITLE     Expression and cellular localizaion of melatonin-synthesizing
            enzymes in rat and human salivary glands
  JOURNAL   Histochem Cell Biol 135 (4), 389-396 (2011)
   PUBMED   21437622
  REMARK    GeneRIF: The expression of HIOMT in epithelial cells of striated
            ducts in rat submandibular glands.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Kasahara,T., Abe,K., Mekada,K., Yoshiki,A. and Kato,T.
  TITLE     Genetic variation of melatonin productivity in laboratory mice
            under domestication
  JOURNAL   Proc Natl Acad Sci U S A 107 (14), 6412-6417 (2010)
   PUBMED   20308563
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Hosaka,T., Mimuro,T., Hamada,N., Itoh,M.T. and Ishizuka,B.
  TITLE     Stimulatory effects of LH on release of melatonin and activities of
            its synthesizing enzymes NAT and HIOMT in organ-cultured pineal
            glands of female rats
  JOURNAL   Horm Metab Res 34 (8), 441-445 (2002)
   PUBMED   12198599
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Gauer,F. and Craft,C.M.
  TITLE     Circadian regulation of hydroxyindole-O-methyltransferase mRNA
            levels in rat pineal and retina
  JOURNAL   Brain Res 737 (1-2), 99-109 (1996)
   PUBMED   8930356
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Ebihara,S., Marks,T., Hudson,D.J. and Menaker,M.
  TITLE     Genetic control of melatonin synthesis in the pineal gland of the
            mouse
  JOURNAL   Science 231 (4737), 491-493 (1986)
   PUBMED   3941912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB765131.1, EU741665.1 and L78306.1.
            
            On Jun 10, 2008 this sequence version replaced NP_653360.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU741665.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..432
                     /product="acetylserotonin O-methyltransferase"
                     /EC_number="2.1.1.4"
                     /note="hydroxyindole O-methyltransferase"
                     /calculated_mol_wt=45457
     Region          16..99
                     /region_name="dimerization2"
                     /note="dimerization domain; pfam16864"
                     /db_xref="CDD:465287"
     Region          116..327
                     /region_name="Methyltransf_2"
                     /note="O-methyltransferase domain; pfam00891"
                     /db_xref="CDD:395719"
     Site            order(185..191,209..210,235..237,251)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     Region          373..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B3GSH5.1)"
     CDS             1..432
                     /gene="Asmt"
                     /coded_by="NM_144759.2:21..1319"
                     /db_xref="GeneID:246281"
                     /db_xref="RGD:708472"
ORIGIN      
        1 mapgregeld rdfrvlmsla hgfmvsqvlf aaldlgifdl aaqgpvaaea vaqtggwspr
       61 gtqllmdact rlgllrgagd gsytnsalss tflvsgspqs qrcmllylag ttygcwahla
      121 agvregrnqy sravgisaed pfsaiyrsep erllfmrglq etwslcggrv ltafdlsrfr
      181 vicdlgggsg alaqeaarly pgssvcvfdl pdviaaarth flspgarpsv rfvagdffrs
      241 rlpradlfil arvlhdwadg acvellgrlh racrpggall lveavlakgg agplrsllls
      301 lnmmlqaegw erqasdyrnl atragfprlq lrrpggpyha mlarrgprpg iitgvgsntt
      361 gtgsfvtgir rdvpgarsda agtgsgtgnt gsgimlqget lesevsapqa gsdvggagne
      421 prsgtlkqgd wk
//
LOCUS       NP_705893                840 aa            linear   ROD 27-APR-2025
DEFINITION  heat shock 70 kDa protein 4 [Rattus norvegicus].
ACCESSION   NP_705893
VERSION     NP_705893.1
DBSOURCE    REFSEQ: accession NM_153629.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Tu,Z., Jin,P., Wang,Q., Feng,Y., Chu,X., Fu,L., Hou,S. and Li,W.
  TITLE     Dynamically changed HSP70 after reperfusion following cerebral
            infarction in human and rats: correlation with p38 MAPK
  JOURNAL   Neuroreport 35 (7), 439-446 (2024)
   PUBMED   38597327
  REMARK    GeneRIF: Dynamically changed HSP70 after reperfusion following
            cerebral infarction in human and rats: correlation with p38 MAPK.
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Lee,C.H., Su,T.C., Lee,M.S., Hsu,C.S., Yang,R.C. and Kao,J.K.
  TITLE     Heat shock protein 70 protects the lungs from hyperoxic injury in a
            neonatal rat model of bronchopulmonary dysplasia
  JOURNAL   PLoS One 18 (5), e0285944 (2023)
   PUBMED   37200358
  REMARK    GeneRIF: Heat shock protein 70 protects the lungs from hyperoxic
            injury in a neonatal rat model of bronchopulmonary dysplasia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Qu,B., Zhao,Q., Ma,Q., Yang,T., Li,X., Chen,Y., Yang,J. and
            Zhang,Y.
  TITLE     Overexpression of miR-144-3p alleviates polycystic ovaries syndrome
            through targeting expression of HSP-70
  JOURNAL   Gene Ther 29 (5), 217-226 (2022)
   PUBMED   32917949
  REMARK    GeneRIF: Overexpression of miR-144-3p alleviates polycystic ovaries
            syndrome through targeting expression of HSP-70.
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Belity,T., Horowitz,M., Hoffman,J.R., Epstein,Y., Bruchim,Y.,
            Todder,D. and Cohen,H.
  TITLE     Heat-Stress Preconditioning Attenuates Behavioral Responses to
            Psychological Stress: The Role of HSP-70 in Modulating Stress
            Responses
  JOURNAL   Int J Mol Sci 23 (8), 4129 (2022)
   PUBMED   35456946
  REMARK    GeneRIF: Heat-Stress Preconditioning Attenuates Behavioral
            Responses to Psychological Stress: The Role of HSP-70 in Modulating
            Stress Responses.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Porto,R.R., Dutra,F.D., Crestani,A.P., Holsinger,R.M.D.,
            Quillfeldt,J.A., Homem de Bittencourt,P.I. Jr. and de Oliveira
            Alvares,L.
  TITLE     HSP70 Facilitates Memory Consolidation of Fear Conditioning through
            MAPK Pathway in the Hippocampus
  JOURNAL   Neuroscience 375, 108-118 (2018)
   PUBMED   29374537
  REMARK    GeneRIF: Male rats were trained in contextual fear conditioning
            task and HSP70 content was analyzed by western blot in the
            hippocampus at different time points. We observed rapid and
            transient elevations in HSP70 60min following training. Double
            immunofluorescence with GFAP and HSP72 revealed that astrocytes
            were not the site for HSP72 induction by CFC training.
REFERENCE   6  (residues 1 to 840)
  AUTHORS   Luo,D.L., Zhou,J.H., Liu,B.H., Huang,X.K., Chen,J.P., Qiu,J.,
            Xiong,R.P. and Wang,Z.G.
  TITLE     [Study on the relationship of heat shock protein 70 with secondary
            liver damage in early stage after severe multiple injury]
  JOURNAL   Zhongguo Wei Zhong Bing Ji Jiu Yi Xue 15 (4), 204-206 (2003)
   PUBMED   12857439
  REMARK    GeneRIF: Excessive expression of HSP70 may cause injury to liver
            after severe multiple injury.
REFERENCE   7  (residues 1 to 840)
  AUTHORS   Weiss,Y.G., Maloyan,A., Tazelaar,J., Raj,N. and Deutschman,C.S.
  TITLE     Adenoviral transfer of HSP-70 into pulmonary epithelium ameliorates
            experimental acute respiratory distress syndrome
  JOURNAL   J Clin Invest 110 (6), 801-806 (2002)
   PUBMED   12235111
REFERENCE   8  (residues 1 to 840)
  AUTHORS   Thomas,G., Souil,E., Richard,M.J., Saunier,B., Polla,B.S. and
            Bachelet,M.
  TITLE     Hyperthermia assists survival of astrocytes from oxidative-mediated
            necrotic cell death
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 48 (2), 191-198 (2002)
   PUBMED   11990455
  REMARK    GeneRIF: As Hsp70 may transfer from glial to neuronal cells, its
            synthesis by astrocytes may represent an important survival
            mechanism by which astrocytes protect neurons against
            oxidative-mediated cell death
REFERENCE   9  (residues 1 to 840)
  AUTHORS   Harano,T., Nose,S., Uezu,R., Shimizu,N. and Fujiki,Y.
  TITLE     Hsp70 regulates the interaction between the peroxisome targeting
            signal type 1 (PTS1)-receptor Pex5p and PTS1
  JOURNAL   Biochem J 357 (Pt 1), 157-165 (2001)
   PUBMED   11415446
REFERENCE   10 (residues 1 to 840)
  AUTHORS   Yagita,Y., Kitagawa,K., Taguchi,A., Ohtsuki,T., Kuwabara,K.,
            Mabuchi,T., Matsumoto,M., Yanagihara,T. and Hori,M.
  TITLE     Molecular cloning of a novel member of the HSP110 family of genes,
            ischemia-responsive protein 94 kDa (irp94), expressed in rat brain
            after transient forebrain ischemia
  JOURNAL   J Neurochem 72 (4), 1544-1551 (1999)
   PUBMED   10098860
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF077354.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF077354.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..840
                     /product="heat shock 70 kDa protein 4"
                     /note="expressed in rat brain after transient forebrain
                     ischemia; ischemia responsive 94 kDa protein; heat shock
                     protein 4; heat shock protein family A member 4"
                     /calculated_mol_wt=93926
     Region          2..382
                     /region_name="ASKHA_NBD_HSP70_HSPA4"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 4 (HSPA4) and similar proteins; cd11737"
                     /db_xref="CDD:466843"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61316; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61316; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            430
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Region          <499..743
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          500..575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88600.1)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61316; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Site            773
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P34932; propagated from
                     UniProtKB/Swiss-Prot (O88600.1)"
     Region          781..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88600.1)"
     CDS             1..840
                     /gene="Hspa4"
                     /gene_synonym="Hsp110; Hsp70; irp94"
                     /coded_by="NM_153629.1:226..2748"
                     /db_xref="GeneID:266759"
                     /db_xref="RGD:628878"
ORIGIN      
        1 msvvgidlgf qscyvavara ggietianey sdrctpacvs fgpknrsvga aaksqvisna
       61 kntvqgfkrf hgrafsdpfv eaeksnlayd ivqlptgltg ikvtymeeer nftteqvtam
      121 llsklketae svlkkpvvdc vvsvpsfytd aerrsvmdat qiaglnclrl mnettavala
      181 ygiykqdlpa leekprnvvf vdmghsayqv svcafnrgkl kvlatafdtt lggrkfdevl
      241 vnhfceefgk kykldikskv rallrlsqec eklkklmsan asdlplsiec fmndidvsgt
      301 mnrgkflemc ddllarvepp lrsildqskl kkediyavei vggatripav kekiskffgk
      361 elsttlnade avtrgcalqc ailspafkvr efsitdvvpy pislrwnspa eegssdcevf
      421 pknhaapfsk vltfyrkepf tleayysspq dlpypdpaia qfsvqkvtpq sdgssskvkv
      481 kvrvnvhgif svssaalvev hkseeseepm etdqnakeee kmqvdqeeph teeqqpqtpa
      541 enkaeseeme tsqagskdkk mdqppqakka kvktstvdlp iesqllwqld remlglyten
      601 egkmimqdkl ekerndakna veeyvyemrd klsgeyekfv seddrnnftl kledtenwly
      661 edgedqpkqv yvdklaelrt lgqpiktrfq eseerpklfe elgkqiqqym kvissfknke
      721 dqyehldaad mtkvekstne amewmnskln lqnkqsltad pvvktkeiea kikeltnics
      781 piiskpkpkv eppkeepkha eqngpvdgqg dnpgtqaaeh gadtavpsdg dkklpemdid
//
LOCUS       NP_001020847             420 aa            linear   ROD 27-APR-2025
DEFINITION  pre-mRNA-splicing factor RBM22 [Rattus norvegicus].
ACCESSION   NP_001020847
VERSION     NP_001020847.1
DBSOURCE    REFSEQ: accession NM_001025676.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Chanarat,S. and Strasser,K.
  TITLE     Splicing and beyond: the many faces of the Prp19 complex
  JOURNAL   Biochim Biophys Acta 1833 (10), 2126-2134 (2013)
   PUBMED   23742842
  REMARK    Review article
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Rasche,N., Dybkov,O., Schmitzova,J., Akyildiz,B., Fabrizio,P. and
            Luhrmann,R.
  TITLE     Cwc2 and its human homologue RBM22 promote an active conformation
            of the spliceosome catalytic centre
  JOURNAL   EMBO J 31 (6), 1591-1604 (2012)
   PUBMED   22246180
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Janowicz,A., Michalak,M. and Krebs,J.
  TITLE     Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7
  JOURNAL   Biochim Biophys Acta 1813 (5), 1045-1049 (2011)
   PUBMED   21122810
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Montaville,P., Dai,Y., Cheung,C.Y., Giller,K., Becker,S.,
            Michalak,M., Webb,S.E., Miller,A.L. and Krebs,J.
  TITLE     Nuclear translocation of the calcium-binding protein ALG-2 induced
            by the RNA-binding protein RBM22
  JOURNAL   Biochim Biophys Acta 1763 (11), 1335-1343 (2006)
   PUBMED   17045351
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Kitaura,Y., Matsumoto,S., Satoh,H., Hitomi,K. and Maki,M.
  TITLE     Peflin and ALG-2, members of the penta-EF-hand protein family, form
            a heterodimer that dissociates in a Ca2+-dependent manner
  JOURNAL   J Biol Chem 276 (17), 14053-14058 (2001)
   PUBMED   11278427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097991.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097991.1, SRR8487227.197734.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155325, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..420
                     /product="pre-mRNA-splicing factor RBM22"
                     /calculated_mol_wt=46733
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NW64; propagated from
                     UniProtKB/Swiss-Prot (Q4V7D7.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NW64; propagated from
                     UniProtKB/Swiss-Prot (Q4V7D7.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NW64; propagated from
                     UniProtKB/Swiss-Prot (Q4V7D7.1)"
     Region          159..185
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NW64; propagated from
                     UniProtKB/Swiss-Prot (Q4V7D7.1)"
     Region          231..304
                     /region_name="RRM_RBM22"
                     /note="RNA recognition motif (RRM) found in
                     Pre-mRNA-splicing factor RBM22 and similar proteins;
                     cd12224"
                     /db_xref="CDD:409671"
     Region          303..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7D7.1)"
     Region          371..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7D7.1)"
     CDS             1..420
                     /gene="Rbm22"
                     /coded_by="NM_001025676.1:54..1316"
                     /db_xref="GeneID:307410"
                     /db_xref="RGD:1305770"
ORIGIN      
        1 matslgsnty nrqnwedadf pilcqtclge npyirmtkek ygkeckicar pftvfrwcpg
       61 vrmrfkktev cqtcsklknv cqtclldley glpiqvrdag lsfkddmpks dvnkeyytqn
      121 mereisnsdg trpvgmlgka tstsdmllkl arttpyykrn rphicsfwvk geckrgeecp
      181 yrhekptdpd dpladqnikd ryygindpva dkllkrastm prldppedkt ittlyvgglg
      241 dtitetdlrn hfyqfgeirt vtvvqrqqca fiqfatrqaa evaaeksfnk livngrrlnv
      301 kwgrsqaarg kekekdgttd sgiklepvpg lpgalppppa aeeeasanyf nlppsgppav
      361 vnialppppg iapppppgfg phlfhpmgpp ppfmrapgpi hypsqdpqrm gahagkhssp
//
LOCUS       NP_445943                812 aa            linear   ROD 27-APR-2025
DEFINITION  plasminogen precursor [Rattus norvegicus].
ACCESSION   NP_445943 XP_001068594 XP_574314
VERSION     NP_445943.1
DBSOURCE    REFSEQ: accession NM_053491.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Cramer,D.A.T., Yin,V., Caval,T., Franc,V., Yu,D., Wu,G., Lloyd,G.,
            Langendorf,C., Whisstock,J.C., Law,R.H.P. and Heck,A.J.R.
  TITLE     Proteoform-Resolved Profiling of Plasminogen Activation Reveals
            Novel Abundant Phosphorylation Site and Primary N-Terminal Cleavage
            Site
  JOURNAL   Mol Cell Proteomics 23 (1), 100696 (2024)
   PUBMED   38101751
  REMARK    GeneRIF: Proteoform-Resolved Profiling of Plasminogen Activation
            Reveals Novel Abundant Phosphorylation Site and Primary N-Terminal
            Cleavage Site.
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Wu,Y., Wang,T., Guo,C., Zhang,D., Ge,X., Huang,Z., Zhou,X., Li,Y.,
            Peng,Q. and Li,J.
  TITLE     Plasminogen improves lung lesions and hypoxemia in patients with
            COVID-19
  JOURNAL   QJM 113 (8), 539-545 (2020)
   PUBMED   32275753
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Liu,C.M., Chen,J., Yang,S., Mao,L.G., Jiang,T.T., Tu,H.H.,
            Chen,Z.L., Hu,Y.T., Gan,L., Li,Z.J. and Li,J.C.
  TITLE     The Chinese herbal formula Zhibai Dihuang Granule treat
            Yin-deficiency-heat syndrome rats by regulating the immune
            responses
  JOURNAL   J Ethnopharmacol 225, 271-278 (2018)
   PUBMED   29729385
REFERENCE   4  (residues 1 to 812)
  AUTHORS   Zachar,R., Al-Mashhadi,A., Dimke,H., Svenningsen,P., Jensen,B.L.
            and Carlstrom,M.
  TITLE     Hydronephrosis is associated with elevated plasmin in urine in
            pediatric patients and rats and changes in NCC and gamma-ENaC
            abundance in rat kidney
  JOURNAL   Am J Physiol Renal Physiol 315 (3), F547-F557 (2018)
   PUBMED   29767556
  REMARK    GeneRIF: The presence of active plasmin in urine in hydronephrosis
            could cause abnormal proteolytic activation of ENaC-gamma and
            impaired ability to excrete Na via NCC.
REFERENCE   5  (residues 1 to 812)
  AUTHORS   Grundel,A., Pfeiffer,M., Jacobs,E. and Dumke,R.
  TITLE     Network of Surface-Displayed Glycolytic Enzymes in Mycoplasma
            pneumoniae and Their Interactions with Human Plasminogen
  JOURNAL   Infect Immun 84 (3), 666-676 (2015)
   PUBMED   26667841
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 812)
  AUTHORS   Kanalas,J.J. and Makker,S.P.
  TITLE     Identification of the rat Heymann nephritis autoantigen (GP330) as
            a receptor site for plasminogen
  JOURNAL   J Biol Chem 266 (17), 10825-10829 (1991)
   PUBMED   1645711
REFERENCE   7  (residues 1 to 812)
  AUTHORS   Ichinose,A., Espling,E.S., Takamatsu,J., Saito,H., Shinmyozu,K.,
            Maruyama,I., Petersen,T.E. and Davie,E.W.
  TITLE     Two types of abnormal genes for plasminogen in families with a
            predisposition for thrombosis
  JOURNAL   Proc Natl Acad Sci U S A 88 (1), 115-119 (1991)
   PUBMED   1986355
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Apr 1;88(7):2967]
REFERENCE   8  (residues 1 to 812)
  AUTHORS   Silverstein,R.L., Leung,L.L., Harpel,P.C. and Nachman,R.L.
  TITLE     Complex formation of platelet thrombospondin with plasminogen.
            Modulation of activation by tissue activator
  JOURNAL   J Clin Invest 74 (5), 1625-1633 (1984)
   PUBMED   6438154
REFERENCE   9  (residues 1 to 812)
  AUTHORS   Miyata,T., Iwanaga,S., Sakata,Y. and Aoki,N.
  TITLE     Plasminogen Tochigi: inactive plasmin resulting from replacement of
            alanine-600 by threonine in the active site
  JOURNAL   Proc Natl Acad Sci U S A 79 (20), 6132-6136 (1982)
   PUBMED   6216475
REFERENCE   10 (residues 1 to 812)
  AUTHORS   Brower,M.S. and Harpel,P.C.
  TITLE     Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor
            and C1 inactivator by human polymorphonuclear leukocyte elastase
  JOURNAL   J Biol Chem 257 (16), 9849-9854 (1982)
   PUBMED   6980881
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091135.1.
            
            On or before Feb 14, 2007 this sequence version replaced
            XP_574314.1, XP_001068594.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091135.1, FQ210878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q11"
     Protein         1..812
                     /product="plasminogen precursor"
                     /EC_number="3.4.21.7"
                     /calculated_mol_wt=88342
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2213
     mat_peptide     20..812
                     /product="Plasminogen. /id=PRO_0000028079"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01177.2)"
                     /calculated_mol_wt=88342
     Region          33..97
                     /region_name="PAN_AP_HGF"
                     /note="Subfamily of PAN/APPLE-like domains; present in
                     N-terminal (N) domains of plasminogen/hepatocyte growth
                     factor proteins, and various proteins found in Bilateria,
                     such as leech anti-platelet proteins. PAN/APPLE domains
                     fulfill diverse biological functions...; cd01099"
                     /db_xref="CDD:238532"
     Site            order(38,40,52)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238532"
     Region          101..183
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            112
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(127,137,163,165,173)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          183..262
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            194
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(209,219,244,246,254)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          273..354
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            284
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(299,309,334,336,344)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          374..456
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            385
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(400,410,436,438,446)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          480..562
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            490
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(505,516,542,544,552)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          582..807
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            582
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00747; propagated from
                     UniProtKB/Swiss-Prot (Q01177.2)"
     Site            order(624,667,762)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00747; propagated from
                     UniProtKB/Swiss-Prot (Q01177.2)"
     Site            order(756,781,783)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..812
                     /gene="Plg"
                     /gene_synonym="Ab1-346"
                     /coded_by="NM_053491.2:38..2476"
                     /db_xref="GeneID:85253"
                     /db_xref="RGD:619893"
ORIGIN      
        1 mdhkeiillf llflkpgqgd sldgyvstqg aslhsltkkq laagsiadcl akcegetdfi
       61 crsfqyhske qqcvimaens ktssiirmrd vilfekrvyl secktgigkg yrgtmsktkt
      121 gvtcqkwsdt sphvpkysps thpsegleen ycrnpdndeq gpwcyttdpd qryeycnipe
      181 ceeecmycsg ekyegkiskt msgldcqswd sqsphahgyi pakfpsknlk mnycrnpdge
      241 prpwcfttdp nkrweycdip rcttpppppg ptyqclkgrg enyrgtvsvt asgktcqrws
      301 eqtphrhnrt penfpcknle enycrnpdge tapwcyttds qlrweyceip scgssvspdq
      361 sdssvlpeqt pvvqecyqgn gksyrgtsst tntgkkcqsw vsmtphshsk tpanfpdagl
      421 emnycrnpdn dqrgpwcftt dpsvrweycn lkrcsetggg vaesaivpqv psapgtsetd
      481 cmygngkeyr gktavtaagt pcqewaaqep hshriftpqt npraglekny crnpdgdvng
      541 pwcytmnprk lydycniplc aslssfecgk pqvepkkcpg rvvggcvanp hswpwqislr
      601 trfsgqhfcg gtlispewvl taahclekss rpefykvilg aheerilgsd vqqiavtklv
      661 lepndadial lklsrpatit dnvipaclps pnyvvadrtl cyitgwgetk gtpgagrlke
      721 aqlpvienkv cnraeylnnr vkstelcagh laggidscqg dsggplvcfe kdkyilqgvt
      781 swglgcarpn kpgvyvrvsr yvnwieremr nd
//
LOCUS       NP_001103350             725 aa            linear   ROD 27-APR-2025
DEFINITION  beta-adducin isoform a [Rattus norvegicus].
ACCESSION   NP_001103350
VERSION     NP_001103350.1
DBSOURCE    REFSEQ: accession NM_001109880.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Engmann,O., Giralt,A., Gervasi,N., Marion-Poll,L., Gasmi,L.,
            Filhol,O., Picciotto,M.R., Gilligan,D., Greengard,P., Nairn,A.C.,
            Herve,D. and Girault,J.A.
  TITLE     DARPP-32 interaction with adducin may mediate rapid environmental
            effects on striatal neurons
  JOURNAL   Nat Commun 6, 10099 (2015)
   PUBMED   26639316
  REMARK    GeneRIF: Darpp32 interaction with beta-adducin may be the molecular
            pathway by which environmental changes may rapidly alter
            responsiveness of striatal neurons involved in the reward system.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Xu,T., Liu,W., Yang,C., Ba,X., Wang,X., Jiang,Y. and Zeng,X.
  TITLE     Lipid raft-associated beta-adducin is required for PSGL-1-mediated
            neutrophil rolling on P-selectin
  JOURNAL   J Leukoc Biol 97 (2), 297-306 (2015)
   PUBMED   25425738
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Valencia,D.M., Naranjo,C.A., Parra,M.V., Caro,M.A., Valencia,A.V.,
            Jaramillo,C.J. and Bedoya,G.
  TITLE     [Association and interaction of AGT, AGTR1, ACE, ADRB2, DRD1, ADD1,
            ADD2, ATP2B1, TBXA2R and PTGS2 genes on the risk of hypertension in
            Antioquian population]
  JOURNAL   Biomedica 33 (4), 598-614 (2013)
   PUBMED   24652215
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Bednarek,E. and Caroni,P.
  TITLE     beta-Adducin is required for stable assembly of new synapses and
            improved memory upon environmental enrichment
  JOURNAL   Neuron 69 (6), 1132-1146 (2011)
   PUBMED   21435558
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Sonoyama,K., Greenstein,A.S., Micheletti,R., Ferrari,P.,
            Schiavone,A., Aghamohammadzadeh,R., Withers,S.B., Tripodi,G.,
            Ferrandi,M. and Heagerty,A.M.
  TITLE     Mutation in the beta adducin subunit causes tissue-specific damage
            to myogenic tone
  JOURNAL   J Hypertens 29 (3), 466-474 (2011)
   PUBMED   21150638
  REMARK    GeneRIF: Mutations in the beta subunit of the adducin protein
            result in damage to renal artery myogenic tone and this is
            associated with renal damage as manifest by proteinuria.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Kuhlman,P.A., Hughes,C.A., Bennett,V. and Fowler,V.M.
  TITLE     A new function for adducin. Calcium/calmodulin-regulated capping of
            the barbed ends of actin filaments
  JOURNAL   J Biol Chem 271 (14), 7986-7991 (1996)
   PUBMED   8626479
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Tripodi,G., Piscone,A., Borsani,G., Tisminetzky,S., Salardi,S.,
            Sidoli,A., James,P., Pongor,S., Bianchi,G. and Baralle,F.E.
  TITLE     Molecular cloning of an adducin-like protein: evidence of a
            polymorphism in the normotensive and hypertensive rats of the Milan
            strain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 939-947 (1991)
   PUBMED   2059221
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M63894.1, AF130338.1 and DY315967.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680412,
                              SAMN06680413 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..725
                     /product="beta-adducin isoform a"
                     /note="adducin-63; erythrocyte adducin subunit beta;
                     adducin beta; adducin 2 (beta); beta-adducin"
                     /calculated_mol_wt=80446
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Region          130..379
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(139,143,155,176,178..179,229,231..232,237..239,247,
                     249..250,261,289,300,307,311,318,336)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(160,173..174,199..201,227,229,290)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(227,229,290)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Region          <388..692
                     /region_name="DUF612"
                     /note="Protein of unknown function, DUF612; pfam04747"
                     /db_xref="CDD:282585"
     Region          425..444
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Region          <514..656
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Region          525..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Region          703..720
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     CDS             1..725
                     /gene="Add2"
                     /gene_synonym="beta-ADD"
                     /coded_by="NM_001109880.1:188..2365"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24171"
                     /db_xref="RGD:2042"
ORIGIN      
        1 msedtvpeaa spppsqgqhy fdrfseddpe ylrlrnraad lrqdfnlmeq kkrvtmilqs
       61 psfreelegl iqeqmkkgnn ssniwalrqi adfmastsha vfpassmnfs mmtpindlht
      121 adslnlakge rlmrckissv yrlldlygwa qlsdtyvtlr vskeqdhfli spkgvscsev
      181 tasslikvni lgevvekgss cfpvdttgfs lhsaiyaarp dvrcaihlht pataavsamk
      241 cgllpvshna llvgdmayyd fngemeqead rinlqkclgp tckilvlrnh gmvalgdtve
      301 eafykvfhlq aacevqvsal ssaggtenli lleqekhrph evgsvqwags tfgpmqksrl
      361 gehefealmr mldnlgyrtg ytyrhpfvqe ktkhksevei patvtafvfe edgvpvpalr
      421 qhaqkqqkek trwlntpnty lrvnvadevq rnmgsprpkt twmkadevek sssgmpirie
      481 npnqfvplyt dpqevldmrn kireqnrqdi ksagpqsqll asviaeksrs pstesqlask
      541 gdadtkdele etvpnpfsql tdqeleeykk everkkleqe qegekdaate epgspvkstp
      601 aspvqsptra gtkspavsps kasedakkte vseantepep ekpegvvvng keeepsveev
      661 lskgpgqmtt nadtdgdsyk dktesvtsgp lspegspsks pskkkkkfrt psflkkskkk
      721 ekves
//
LOCUS       NP_001073355             267 aa            linear   ROD 27-APR-2025
DEFINITION  CUE domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001073355 XP_001067247 XP_215274
VERSION     NP_001073355.1
DBSOURCE    REFSEQ: accession NM_001079886.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Huang,Y., Xiao,X., Xiao,H., Hu,Z. and Tan,F.
  TITLE     CUEDC2 ablation enhances the efficacy of mesenchymal stem cells in
            ameliorating cerebral ischemia/reperfusion insult
  JOURNAL   Aging (Albany NY) 13 (3), 4335-4356 (2021)
   PUBMED   33494071
  REMARK    GeneRIF: CUEDC2 ablation enhances the efficacy of mesenchymal stem
            cells in ameliorating cerebral ischemia/reperfusion insult.
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Chen,Y., Wang,S.X., Mu,R., Luo,X., Liu,Z.S., Liang,B., Zhuo,H.L.,
            Hao,X.P., Wang,Q., Fang,D.F., Bai,Z.F., Wang,Q.Y., Wang,H.M.,
            Jin,B.F., Gong,W.L., Zhou,T., Zhang,X.M., Xia,Q. and Li,T.
  TITLE     Dysregulation of the miR-324-5p-CUEDC2 axis leads to macrophage
            dysfunction and is associated with colon cancer
  JOURNAL   Cell Rep 7 (6), 1982-1993 (2014)
   PUBMED   24882011
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127518.1.
            
            On or before Jan 5, 2007 this sequence version replaced
            XP_215274.3, XP_001067247.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127518.1, SRR8487230.80015.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..267
                     /product="CUE domain-containing protein 2"
                     /calculated_mol_wt=30151
     Region          90..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L131.1)"
     Region          126..166
                     /region_name="CUE_CUED2"
                     /note="CUE domain found in CUE domain-containing protein 2
                     (CUED2) and similar proteins; cd14367"
                     /db_xref="CDD:270550"
     CDS             1..267
                     /gene="Cuedc2"
                     /coded_by="NM_001079886.1:556..1359"
                     /db_xref="GeneID:294009"
                     /db_xref="RGD:1308096"
ORIGIN      
        1 melerivssa lfafvqthlp eadlsgldev ifsyvlgvle dlgpsgpsee nfdmeafiem
       61 meayvpgfah ihrgiiedmv qtlsvqlssa rnketlrrpe klkeesrppa atgntqdeaa
      121 aaeeeqpgvd vllevfptcs meqaqwvlak argnleeavq mliegkeegp pgwggpnqdl
      181 prrlrgprke elksfilqky mmvdraedqk thrpmapkea pkkliryidn qvvstkgerf
      241 kdvrnpetee mkatyinlkp arkyrfh
//
LOCUS       NP_001013895             194 aa            linear   ROD 27-APR-2025
DEFINITION  deubiquitinase DESI2 [Rattus norvegicus].
ACCESSION   NP_001013895 XP_213951
VERSION     NP_001013895.1
DBSOURCE    REFSEQ: accession NM_001013873.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Li,S.Y., Wang,C.Y., Zhao,J.J., Long,C.Y., Xiao,Y.X., Tang,X.B.,
            Yuan,Z.W. and Bai,Y.Z.
  TITLE     Upregulation of PPPDE1 contributes to anorectal malformations via
            the mitochondrial apoptosis pathway during hindgut development in
            rats
  JOURNAL   Exp Cell Res 402 (2), 112574 (2021)
   PUBMED   33794264
  REMARK    GeneRIF: Upregulation of PPPDE1 contributes to anorectal
            malformations via the mitochondrial apoptosis pathway during
            hindgut development in rats.
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Xie,X., Wang,X., Jiang,D., Wang,J., Fei,R., Cong,X., Wei,L.,
            Wang,Y. and Chen,H.
  TITLE     PPPDE1 is a novel deubiquitinase belonging to a cysteine
            isopeptidase family
  JOURNAL   Biochem Biophys Res Commun 488 (2), 291-296 (2017)
   PUBMED   28483520
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Shin,E.J., Shin,H.M., Nam,E., Kim,W.S., Kim,J.H., Oh,B.H. and
            Yun,Y.
  TITLE     DeSUMOylating isopeptidase: a second class of SUMO protease
  JOURNAL   EMBO Rep 13 (4), 339-346 (2012)
   PUBMED   22370726
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Cai,P., Xia,X., Li,F., Cui,Y., Yang,Q. and Chen,M.
  TITLE     PNAS4 knockout does not induce obviously neurocytes apoptosis and
            abnormal development in mice brain
  JOURNAL   Mol Biol Rep 39 (1), 621-628 (2012)
   PUBMED   21553223
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083584.1.
            
            On Apr 20, 2005 this sequence version replaced XP_213951.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083584.1, FQ226068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q25"
     Protein         1..194
                     /product="deubiquitinase DESI2"
                     /EC_number="3.1.2.22"
                     /EC_number="3.4.19.12"
                     /note="PPPDE peptidase domain-containing protein 1; family
                     with sequence similarity 152, member A; PPPDE peptidase
                     domain containing 1; S-depalmitoylase DESI2; palmitoyl
                     protein thioesterase DESI2"
                     /calculated_mol_wt=21287
     Region          7..149
                     /region_name="Peptidase_C97"
                     /note="PPPDE putative peptidase domain; pfam05903"
                     /db_xref="CDD:461775"
     Region          166..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIT6.1)"
     CDS             1..194
                     /gene="Desi2"
                     /gene_synonym="CGI-146; DeSI-2; Fam152a; PNAS-4; Pppde1"
                     /coded_by="NM_001013873.1:403..987"
                     /db_xref="GeneID:289277"
                     /db_xref="RGD:1359392"
ORIGIN      
        1 mganqlvvln vydmywmney tssigigvfh sgievygref aygghpypfs gifeispgna
       61 aelgetfkfk eavvlgstdf leddiekive elgkeykgna yhlmhkncnh fssalseilc
      121 gkeiprwinr layfsscipf lqsclpkewl tpaalqssvs qelqdeleea edaaastama
      181 saaaggrtgr htkl
//
LOCUS       NP_604451                756 aa            linear   ROD 27-APR-2025
DEFINITION  SH2B adapter protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_604451
VERSION     NP_604451.2
DBSOURCE    REFSEQ: accession NM_134456.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Liu,B.L., Cheng,M., Hu,S., Wang,S., Wang,L., Tu,X., Huang,C.X.,
            Jiang,H. and Wu,G.
  TITLE     Overexpression of miR-142-3p improves mitochondrial function in
            cardiac hypertrophy
  JOURNAL   Biomed Pharmacother 108, 1347-1356 (2018)
   PUBMED   30372837
  REMARK    GeneRIF: miR-14 2-3 p not only mitigate cardiac hypertrophy by
            directly inhibit the expression of gene SH2B1, but also can protect
            mitochondrial function in cardiac hypertrophy of vitro and vivo.
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Yuan,J., Zeng,L., Sun,Y., Wang,N., Sun,Q., Cheng,Z. and Wang,Y.
  TITLE     SH2B1 protects against OGD/R-induced apoptosis in PC12 cells via
            activation of the JAK2/STAT3 signaling pathway
  JOURNAL   Mol Med Rep 18 (3), 2613-2620 (2018)
   PUBMED   30015896
  REMARK    GeneRIF: SH2B1 overexpression resulted in increased viability,
            reduced lactate dehydrogenase release and a reduction in the
            expression levels of proteins associated with the apoptotic cascade
            in PC12 cells under the oxygenglucose deprivation condition.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Franquinho,F., Nogueira-Rodrigues,J., Duarte,J.M., Esteves,S.S.,
            Carter-Su,C., Monaco,A.P., Molnar,Z., Velayos-Baeza,A., Brites,P.
            and Sousa,M.M.
  TITLE     The Dyslexia-susceptibility Protein KIAA0319 Inhibits Axon Growth
            Through Smad2 Signaling
  JOURNAL   Cereb Cortex 27 (3), 1732-1747 (2017)
   PUBMED   28334068
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Chen,C.J., Shih,C.H., Chang,Y.J., Hong,S.J., Li,T.N., Wang,L.H. and
            Chen,L.
  TITLE     SH2B1 and IRSp53 proteins promote the formation of dendrites and
            dendritic branches
  JOURNAL   J Biol Chem 290 (10), 6010-6021 (2015)
   PUBMED   25586189
  REMARK    GeneRIF: These findings suggest that SH2B1-IRSp53 complexes promote
            the formation of filopodia, neurite initiation, and neuronal
            branching.
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Shih,C.H., Chen,C.J. and Chen,L.
  TITLE     New function of the adaptor protein SH2B1 in brain-derived
            neurotrophic factor-induced neurite outgrowth
  JOURNAL   PLoS One 8 (11), e79619 (2013)
   PUBMED   24260264
  REMARK    GeneRIF: findings demonstrate that SH2B1beta promotes BDNF-induced
            neurite outgrowth through enhancing pathways involved MEK-ERK1/2
            and PI3K-AKT.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Diakonova,M., Gunter,D.R., Herrington,J. and Carter-Su,C.
  TITLE     SH2-Bbeta is a Rac-binding protein that regulates cell motility
  JOURNAL   J Biol Chem 277 (12), 10669-10677 (2002)
   PUBMED   11786545
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Riedel,H., Yousaf,N., Zhao,Y., Dai,H., Deng,Y. and Wang,J.
  TITLE     PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated
            mitogenesis
  JOURNAL   Oncogene 19 (1), 39-50 (2000)
   PUBMED   10644978
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Kasus-Jacobi,A., Perdereau,D., Auzan,C., Clauser,E., Van
            Obberghen,E., Mauvais-Jarvis,F., Girard,J. and Burnol,A.F.
  TITLE     Identification of the rat adapter Grb14 as an inhibitor of insulin
            actions
  JOURNAL   J Biol Chem 273 (40), 26026-26035 (1998)
   PUBMED   9748281
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Rui,L., Mathews,L.S., Hotta,K., Gustafson,T.A. and Carter-Su,C.
  TITLE     Identification of SH2-Bbeta as a substrate of the tyrosine kinase
            JAK2 involved in growth hormone signaling
  JOURNAL   Mol Cell Biol 17 (11), 6633-6644 (1997)
   PUBMED   9343427
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Osborne,M.A., Dalton,S. and Kochan,J.P.
  TITLE     The yeast tribrid system--genetic detection of trans-phosphorylated
            ITAM-SH2-interactions
  JOURNAL   Biotechnology (N Y) 13 (13), 1474-1478 (1995)
   PUBMED   9636306
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB742512.1, U57391.1, AF047577.1, BM389529.1 and AI029537.1.
            
            On Oct 8, 2005 this sequence version replaced NP_604451.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: U57391.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..756
                     /product="SH2B adapter protein 1 isoform 1"
                     /note="SH2B adapter protein 1; SH2 domain-containing
                     protein 1B; fceRI gamma-chain-interacting protein SH2-B;
                     SH2-B PH domain-containing signaling mediator 1"
                     /calculated_mol_wt=79506
     Region          1..555
                     /region_name="Interaction with JAK2 (low-affinity binding,
                     independent of JAK2 phosphorylation)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          24..85
                     /region_name="Required for self-association.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          26..81
                     /region_name="Phe_ZIP"
                     /note="Phenylalanine zipper; pfam08916"
                     /db_xref="CDD:462631"
     Region          85..196
                     /region_name="Interaction with RAC1.
                     /evidence=ECO:0000269|PubMed:11786545"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1 or MAPK3, in vitro.
                     /evidence=ECO:0000269|PubMed:10473609; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          100..243
                     /region_name="Required for NGF signaling"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          124..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          175..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          224..233
                     /region_name="Required for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          247..378
                     /region_name="PH_SH2B_family"
                     /note="SH2B adapter protein 1, 2, and 3 Pleckstrin
                     homology (PH) domain; cd01231"
                     /db_xref="CDD:269938"
     Region          262..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRF2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          418..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91ZM2; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2 and PDGFR.
                     /evidence=ECO:0000269|PubMed:12551917; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          468..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2.
                     /evidence=ECO:0000269|PubMed:12551917; propagated from
                     UniProtKB/Swiss-Prot (Q62985.1)"
     Region          518..614
                     /region_name="SH2_SH2B_family"
                     /note="Src homology 2 (SH2) domain found in SH2B adapter
                     protein family; cd10346"
                     /db_xref="CDD:198209"
     Site            order(534,555,576,578)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198209"
     Site            order(577,604)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198209"
     Region          626..691
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     Region          736..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62985.1)"
     CDS             1..756
                     /gene="Sh2b1"
                     /gene_synonym="Sh2-b; Sh2b; Sh2bpsm1"
                     /coded_by="NM_134456.3:301..2571"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:89817"
                     /db_xref="RGD:620132"
ORIGIN      
        1 mngapspedg vfpsppalpp ppppswqefc esharaaald larrfrlyla shpqyaepga
       61 eaafsgrfae lflqhfeaev arasgslspp vlaplspgve ippshdlsle scrvggplav
      121 lgpsrssedl agplpssvss sttsskpklk krfslrsvgr svrgsvrgil qwrgavesps
      181 qagplettsg ppvlggnsns nssggagtvg ralandgtsp gerwthrfer lrlsrgggtl
      241 rdgagviqre ellsfmgaee aapdpagvgr gggaagltsg gggqpqwqkc rlllrsegeg
      301 gggsrleffv ppkasrprls ipcstitdvr tatalempdr entfvvkveg pseyilettd
      361 alhvkawvsd iqeclspgpc paisprpmtl plapgtsflt kdnteslelp clnhseslps
      421 qdlllgpses ndrlsqgayg glsdrpsasf spssasiaas hfdsmellpp elppripiee
      481 gppagtvhpl stpyppldtp eaatgsflfq geaeggegdq plsgypwfhg mlsrlkaaql
      541 vleggtsshg vflvrqsetr rgeyvltfnf qgkakhlrls lneegqcrvq hlwfqsifdm
      601 lehfrvhpip lesggssdvv lvsyvpsqrq qerstsrdpt qpsepppwtd pphpgaeeas
      661 gapevaaata aaakerqeke kaggggvqee lvpmaelvpm aeleeaiapg teaqggagss
      721 gdlevslmvq lqqlplggng eegghprain nqysfv
//
LOCUS       NP_001029240             287 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform a [Rattus norvegicus].
ACCESSION   NP_001029240
VERSION     NP_001029240.1
DBSOURCE    REFSEQ: accession NM_001034068.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB787774.1, M60667.1,
            AF372217.1 and AA899493.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF372217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..287
                     /product="tropomyosin alpha-1 chain isoform a"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32725
     Region          48..259
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..287
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034068.1:107..970"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledkf lcfsppktps ssrmshlsel cicllss
//
LOCUS       NP_112330                418 aa            linear   ROD 27-APR-2025
DEFINITION  actin-related protein 3 [Rattus norvegicus].
ACCESSION   NP_112330 XP_341113
VERSION     NP_112330.1
DBSOURCE    REFSEQ: accession NM_031068.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Su,L., Wang,Z., Xie,S., Hu,D., Cheng,Y.C., Mruk,D.D. and Guan,Y.
  TITLE     Testin regulates the blood-testis barrier via disturbing
            occludin/ZO-1 association and actin organization
  JOURNAL   J Cell Physiol 235 (9), 6127-6138 (2020)
   PUBMED   31975378
  REMARK    GeneRIF: Testin regulates the blood-testis barrier via disturbing
            occludin/ZO-1 association and actin organization.
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Rao,J., Ashraf,S., Tan,W., van der Ven,A.T., Gee,H.Y., Braun,D.A.,
            Feher,K., George,S.P., Esmaeilniakooshkghazi,A., Choi,W.I.,
            Jobst-Schwan,T., Schneider,R., Schmidt,J.M., Widmeier,E.,
            Warejko,J.K., Hermle,T., Schapiro,D., Lovric,S., Shril,S., Daga,A.,
            Nayir,A., Shenoy,M., Tse,Y., Bald,M., Helmchen,U., Mir,S.,
            Berdeli,A., Kari,J.A., El Desoky,S., Soliman,N.A., Bagga,A.,
            Mane,S., Jairajpuri,M.A., Lifton,R.P., Khurana,S., Martins,J.C. and
            Hildebrandt,F.
  TITLE     Advillin acts upstream of phospholipase C 1 in steroid-resistant
            nephrotic syndrome
  JOURNAL   J Clin Invest 127 (12), 4257-4269 (2017)
   PUBMED   29058690
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Detsika,M.G., Lygirou,V., Frantzis,V., Zoidakis,J., Atsaves,V.,
            Poulaki,E., Gakiopoulou,H., Vlahou,A. and Lianos,E.A.
  TITLE     Effect of Heme Oxygenase-1 Deficiency on Glomerular Proteomics
  JOURNAL   Am J Nephrol 43 (6), 441-450 (2016)
   PUBMED   27251563
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Rucksaken,R., Haonon,O., Pinlaor,P., Pairojkul,C., Roytrakul,S.,
            Yongvanit,P., Selmi,C. and Pinlaor,S.
  TITLE     Plasma IgG autoantibody against actin-related protein 3 in liver
            fluke Opisthorchis viverrini infection
  JOURNAL   Parasite Immunol 37 (7), 340-348 (2015)
   PUBMED   25809205
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Lee,H.K., Finniss,S., Cazacu,S., Xiang,C., Poisson,L.M.,
            Blumberg,P.M. and Brodie,C.
  TITLE     RasGRP3 regulates the migration of glioma cells via interaction
            with Arp3
  JOURNAL   Oncotarget 6 (3), 1850-1864 (2015)
   PUBMED   25682201
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Gavard,J., Lambert,M., Grosheva,I., Marthiens,V., Irinopoulou,T.,
            Riou,J.F., Bershadsky,A. and Mege,R.M.
  TITLE     Lamellipodium extension and cadherin adhesion: two cell responses
            to cadherin activation relying on distinct signalling pathways
  JOURNAL   J Cell Sci 117 (Pt 2), 257-270 (2004)
   PUBMED   14657280
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Rombouts,K., Knittel,T., Machesky,L., Braet,F., Wielant,A.,
            Hellemans,K., De Bleser,P., Gelman,I., Ramadori,G. and Geerts,A.
  TITLE     Actin filament formation, reorganization and migration are impaired
            in hepatic stellate cells under influence of trichostatin A, a
            histone deacetylase inhibitor
  JOURNAL   J Hepatol 37 (6), 788-796 (2002)
   PUBMED   12445420
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Gournier,H., Goley,E.D., Niederstrasser,H., Trinh,T. and Welch,M.D.
  TITLE     Reconstitution of human Arp2/3 complex reveals critical roles of
            individual subunits in complex structure and activity
  JOURNAL   Mol Cell 8 (5), 1041-1052 (2001)
   PUBMED   11741539
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Bailly,M., Macaluso,F., Cammer,M., Chan,A., Segall,J.E. and
            Condeelis,J.S.
  TITLE     Relationship between Arp2/3 complex and the barbed ends of actin
            filaments at the leading edge of carcinoma cells after epidermal
            growth factor stimulation
  JOURNAL   J Cell Biol 145 (2), 331-345 (1999)
   PUBMED   10209028
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098014.1.
            
            On Jul 18, 2005 this sequence version replaced XP_341113.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098014.1, FQ212256.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676806, SAMN16676807
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q12"
     Protein         1..418
                     /product="actin-related protein 3"
                     /note="actin-like protein 3; actin-related protein 3
                     homolog (yest); ARP3 actin related protein 3 homolog"
                     /calculated_mol_wt=47226
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P61158; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C7.1)"
     Region          7..410
                     /region_name="ASKHA_NBD_Arp3-like"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein3 (Arp3) and similar proteins; cd10221"
                     /db_xref="CDD:466822"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61158; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C7.1)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61158; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C7.1)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61158; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C7.1)"
     Site            254
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61158; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C7.1)"
     CDS             1..418
                     /gene="Actr3"
                     /gene_synonym="Arp3"
                     /coded_by="NM_031068.1:86..1342"
                     /db_xref="GeneID:81732"
                     /db_xref="RGD:71024"
ORIGIN      
        1 magrlpacvv dcgtgytklg yagntepqfi ipsciaikes akvgdqaqrr vmkgvddldf
       61 figdeaiekp tyatkwpirh givedwdlme rfmeqvifky lraepedhyf lltepplntp
      121 enreytaeim fesfnvpgly iavqavlala aswtsrqvge rtltgtvids gdgvthvipv
      181 aegyvigsci khipiagrdi tyfiqqllrd revgippeqs letakavker ysyvcpdlvk
      241 efnkydtdgs kwikqytgvn aiskkefsid vgyerflgpe iffhpefanp dftqpisevv
      301 deviqncpid vrrplykniv lsggstmfrd fgrrlqrdlk rtvdarlkls eelsggrlkp
      361 kpidvqvith hmqryavwfg gsmlastpef yqvchtkkdy eeigpsicrh npvfgvms
//
LOCUS       NP_001019542             193 aa            linear   ROD 27-APR-2025
DEFINITION  neurocalcin-delta [Rattus norvegicus].
ACCESSION   NP_001019542 XP_580130
VERSION     NP_001019542.1
DBSOURCE    REFSEQ: accession NM_001024371.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Duda,T., Pertzev,A. and Sharma,R.K.
  TITLE     Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked
            with blood pressure regulation
  JOURNAL   Biochemistry 51 (46), 9394-9405 (2012)
   PUBMED   23088492
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Duda,T. and Sharma,R.K.
  TITLE     ONE-GC membrane guanylate cyclase, a trimodal odorant signal
            transducer
  JOURNAL   Biochem Biophys Res Commun 367 (2), 440-445 (2008)
   PUBMED   18178149
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Ivings,L., Pennington,S.R., Jenkins,R., Weiss,J.L. and
            Burgoyne,R.D.
  TITLE     Identification of Ca2+-dependent binding partners for the neuronal
            calcium sensor protein neurocalcin delta: interaction with actin,
            clathrin and tubulin
  JOURNAL   Biochem J 363 (Pt 3), 599-608 (2002)
   PUBMED   11964161
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087105.1.
            
            On May 27, 2005 this sequence version replaced XP_580130.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087105.1, CK603233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="Ncald"
                     /coded_by="NM_001024371.1:165..746"
                     /db_xref="GeneID:553106"
                     /db_xref="RGD:1560287"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_001020862             174 aa            linear   ROD 27-APR-2025
DEFINITION  adipose-secreted signaling protein [Rattus norvegicus].
ACCESSION   NP_001020862 XP_230611
VERSION     NP_001020862.1
DBSOURCE    REFSEQ: accession NM_001025691.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098814.1.
            
            On Jul 22, 2005 this sequence version replaced XP_230611.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098814.1, EV766681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..174
                     /product="adipose-secreted signaling protein"
                     /note="UPF0687 protein C20orf27 homolog"
                     /calculated_mol_wt=19325
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZN8; propagated from
                     UniProtKB/Swiss-Prot (Q4KM45.1)"
     Region          28..173
                     /region_name="DUF4517"
                     /note="Domain of unknown function (DUF4517); pfam15006"
                     /db_xref="CDD:464438"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1K7; propagated from
                     UniProtKB/Swiss-Prot (Q4KM45.1)"
     CDS             1..174
                     /gene="Adissp"
                     /gene_synonym="RGD1311739"
                     /coded_by="NM_001025691.1:197..721"
                     /db_xref="GeneID:311428"
                     /db_xref="RGD:1311739"
ORIGIN      
        1 maaanrgskp rvrsirfaag hdaegsqshv hfdeklhdsv vmvtqesdns flvkvgflki
       61 lhryeitftl pavrrlskdi reapvhslhl kllsvtpipe gysikceysa hkegvlkeem
      121 llacegdigt cvhvtvqarv mdrhhgtpml ldgvkcvgae leydsehsdw hgfd
//
LOCUS       NP_072127                536 aa            linear   ROD 27-APR-2025
DEFINITION  heparanase precursor [Rattus norvegicus].
ACCESSION   NP_072127
VERSION     NP_072127.1
DBSOURCE    REFSEQ: accession NM_022605.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Whitehead,M.J., McGonigal,R., Willison,H.J. and Barnett,S.C.
  TITLE     Heparanase attenuates axon degeneration following sciatic nerve
            transection
  JOURNAL   Sci Rep 8 (1), 5219 (2018)
   PUBMED   29581478
  REMARK    GeneRIF: We identified Hpse as a previously unexplored candidate,
            being up-regulated following injury. We confirmed these results and
            demonstrated inhibition of Hpse led to an acceleration of axonal
            degeneration, accompanied by an increase in b-catenin
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Changyaleket,B., Chong,Z.Z., Dull,R.O., Nanegrungsunk,D. and Xu,H.
  TITLE     Heparanase promotes neuroinflammatory response during subarachnoid
            hemorrhage in rats
  JOURNAL   J Neuroinflammation 14 (1), 137 (2017)
   PUBMED   28720149
  REMARK    GeneRIF: Heparanase plays an important role in mediating the
            neuroinflammatory response after subarachnoid hemorrhage.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Wang,F., Jia,J., Lal,N., Zhang,D., Chiu,A.P., Wan,A., Vlodavsky,I.,
            Hussein,B. and Rodrigues,B.
  TITLE     High glucose facilitated endothelial heparanase transfer to the
            cardiomyocyte modifies its cell death signature
  JOURNAL   Cardiovasc Res 112 (3), 656-668 (2016)
   PUBMED   27979811
  REMARK    GeneRIF: Endothelial cell-to-cardiomyocyte transfer of heparanase
            to modulates the cardiomyocyte cell death signature. This mechanism
            was observed in the acutely diabetic heart, and its interruption
            following chronic diabetes may contribute towards the development
            of diabetic cardiomyopathy.
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Ishiguro-Oonuma,T., Suemoto,M., Okada,M., Yoshioka,K., Hara,Y.,
            Hashizume,K. and Kizaki,K.
  TITLE     Aberrant gene expression of heparanase in ventricular hypertrophy
            induced by monocrotaline in rats
  JOURNAL   J Vet Med Sci 78 (3), 499-503 (2016)
   PUBMED   26638897
  REMARK    GeneRIF: the expression of the gene for heparanase was increased in
            the right and left ventricles after treatment with monocrotaline
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Wang,Y., Chiu,A.P., Neumaier,K., Wang,F., Zhang,D., Hussein,B.,
            Lal,N., Wan,A., Liu,G., Vlodavsky,I. and Rodrigues,B.
  TITLE     Endothelial cell heparanase taken up by cardiomyocytes regulates
            lipoprotein lipase transfer to the coronary lumen after diabetes
  JOURNAL   Diabetes 63 (8), 2643-2655 (2014)
   PUBMED   24608441
  REMARK    GeneRIF: Inhibiting heparanase function could offer a new strategy
            for managing cardiomyopathy observed after diabetes.
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Goldshmidt,O., Zcharia,E., Cohen,M., Aingorn,H., Cohen,I.,
            Nadav,L., Katz,B.Z., Geiger,B. and Vlodavsky,I.
  TITLE     Heparanase mediates cell adhesion independent of its enzymatic
            activity
  JOURNAL   FASEB J 17 (9), 1015-1025 (2003)
   PUBMED   12773484
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Okada,Y., Yamada,S., Toyoshima,M., Dong,J., Nakajima,M. and
            Sugahara,K.
  TITLE     Structural recognition by recombinant human heparanase that plays
            critical roles in tumor metastasis. Hierarchical sulfate groups
            with different effects and the essential target disulfated
            trisaccharide sequence
  JOURNAL   J Biol Chem 277 (45), 42488-42495 (2002)
   PUBMED   12213822
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Podyma-Inoue,K.A., Yokote,H., Sakaguchi,K., Ikuta,M. and
            Yanagishita,M.
  TITLE     Characterization of heparanase from a rat parathyroid cell line
  JOURNAL   J Biol Chem 277 (36), 32459-32465 (2002)
   PUBMED   12077130
  REMARK    GeneRIF: characterization of rat heparanase activity in a
            parathyroid cell line
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Bame,K.J., Venkatesan,I., Dehdashti,J., McFarlane,J. and
            Burfeind,R.
  TITLE     Characterization of a novel intracellular heparanase that has a
            FERM domain
  JOURNAL   Biochem J 364 (Pt 1), 265-274 (2002)
   PUBMED   11988100
  REMARK    GeneRIF: Characterization of a novel intracellular heparanase that
            has a FERM domain.
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Hulett,M.D., Freeman,C., Hamdorf,B.J., Baker,R.T., Harris,M.J. and
            Parish,C.R.
  TITLE     Cloning of mammalian heparanase, an important enzyme in tumor
            invasion and metastasis
  JOURNAL   Nat Med 5 (7), 803-809 (1999)
   PUBMED   10395326
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF184967.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF184967.1, AF359508.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..536
                     /product="heparanase precursor"
                     /EC_number="3.2.1.166"
                     /note="endo-glucoronidase"
                     /calculated_mol_wt=58180
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2407
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251; propagated from
                     UniProtKB/Swiss-Prot (Q71RP1.1)"
     Region          <177..363
                     /region_name="Glyco_hydro_79n"
                     /note="Glycosyl hydrolase family 79, N-terminal domain;
                     pfam03662"
                     /db_xref="CDD:461010"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251; propagated from
                     UniProtKB/Swiss-Prot (Q71RP1.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251; propagated from
                     UniProtKB/Swiss-Prot (Q71RP1.1)"
     Region          281..410
                     /region_name="Required for heterodimerization with the
                     heparanase 8 kDa subunit.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q71RP1.1)"
     Site            452
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251; propagated from
                     UniProtKB/Swiss-Prot (Q71RP1.1)"
     Region          520..536
                     /region_name="Required for transferring proheparanase to
                     the Golgi apparatus, secretion and subsequent enzyme
                     activity and for enhancement of PKB/AKT1 phosphorylation.
                     /evidence=ECO:0000250|UniProtKB:Q9Y251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q71RP1.1)"
     CDS             1..536
                     /gene="Hpse"
                     /gene_synonym="Hep; Hpa"
                     /coded_by="NM_022605.1:66..1676"
                     /db_xref="GeneID:64537"
                     /db_xref="RGD:61969"
ORIGIN      
        1 mlrpllllwl wgrlraltqg tpagtaptkd vvdlefytkr lfqsvspsfl sitidaslat
       61 dprfltflgs prlralargl spaylrfggt ktdflifdpn keptseersy wqsqdnndic
      121 gservsadvl rklqmewpfq ellllreqyq refknstysr ssvdmlysfa kcsrldlifg
      181 lnallrtpdl rwnssnaqll lnycsskgyn iswelgnepn sfwkkaqisi dglqlgedfv
      241 elhkllqksa fqnaklygpd igqprgktvk llrsflkagg evidsltwhh yylngrvatk
      301 edflssdvld tfilsvqkil kvtkemtpgk kvwlgetssa ygggapllsn tfaagfmwld
      361 klglsaqlgi evvmrqvffg agnyhlvden feplpdywls llfkklvgpk vlmsrvkgpd
      421 rsklrvylhc tnvyhpryre gdltlyvlnl hnvtkhlklp ppmfsrpvdk yllkpfgsdg
      481 llsksvqlng qtlkmvdeqt lpaltekplp agsslsvpaf sygffvirna kiaaci
//
LOCUS       NP_001005564             569 aa            linear   ROD 27-APR-2025
DEFINITION  peroxynitrite isomerase THAP4 [Rattus norvegicus].
ACCESSION   NP_001005564 XP_343634
VERSION     NP_001005564.1
DBSOURCE    REFSEQ: accession NM_001005564.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Katayama,K., Ito,J., Murakami,R., Yamashita,A., Sasajima,H.,
            Narahashi,S., Chiba,J., Yamamoto,I., Fujii,W., Tochigi,Y. and
            Suzuki,H.
  TITLE     Mutation of the Thap4 gene causes dwarfism and testicular anomalies
            in rats and mice
  JOURNAL   Mamm Genome 35 (2), 149-159 (2024)
   PUBMED   38658415
  REMARK    GeneRIF: Mutation of the Thap4 gene causes dwarfism and testicular
            anomalies in rats and mice.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   De Simone,G., di Masi,A., Polticelli,F. and Ascenzi,P.
  TITLE     Human nitrobindin: the first example of an all-beta-barrel ferric
            heme-protein that catalyzes peroxynitrite detoxification
  JOURNAL   FEBS Open Bio 8 (12), 2002-2010 (2018)
   PUBMED   30524950
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Bianchetti,C.M., Bingman,C.A. and Phillips,G.N. Jr.
  TITLE     Structure of the C-terminal heme-binding domain of THAP domain
            containing protein 4 from Homo sapiens
  JOURNAL   Proteins 79 (4), 1337-1341 (2011)
   PUBMED   21387410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081882.1.
            
            On Oct 8, 2004 this sequence version replaced XP_343634.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081882.1, SRR8487230.82825.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..569
                     /product="peroxynitrite isomerase THAP4"
                     /note="THAP domain-containing protein 4; ferric
                     nitrobindin"
                     /calculated_mol_wt=62276
     Region          5..85
                     /region_name="THAP"
                     /note="THAP domain; pfam05485"
                     /db_xref="CDD:461662"
     Region          83..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B6.1)"
     Region          <138..>322
                     /region_name="PHA03377"
                     /note="EBNA-3C; Provisional"
                     /db_xref="CDD:177614"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WY91; propagated from
                     UniProtKB/Swiss-Prot (Q642B6.1)"
     Region          230..233
                     /region_name="HCFC1-binding motif (HBM).
                     /evidence=ECO:0000250|UniProtKB:Q8WTV1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B6.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WY91; propagated from
                     UniProtKB/Swiss-Prot (Q642B6.1)"
     Region          235..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B6.1)"
     Region          <342..389
                     /region_name="HrpB7"
                     /note="Bacterial type III secretion protein (HrpB7);
                     pfam09486"
                     /db_xref="CDD:370523"
     Region          407..569
                     /region_name="Nitrobindin.
                     /evidence=ECO:0000250|UniProtKB:Q8WY91"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B6.1)"
     Region          414..567
                     /region_name="lipocalin_heme-bd-THAP4-like"
                     /note="heme-binding beta-barrel domain of human THAP4,
                     Arabidopsis thaliana nitrobindin, and similar proteins;
                     cd07828"
                     /db_xref="CDD:381185"
     Site            order(420,424,436,440,442,446,448,456,458,460,462,
                     471..472,474,476,478,493,497,512,514,528,531,533,535,543,
                     545,547,549,551,559..560,562,564)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381185"
     Site            order(436,440,442,460,462,471..472,493,497,528,531,533,
                     547,549,551,559..560)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381185"
     CDS             1..569
                     /gene="Thap4"
                     /gene_synonym="Nb(III)"
                     /coded_by="NM_001005564.1:40..1749"
                     /db_xref="GeneID:363291"
                     /db_xref="RGD:1359473"
ORIGIN      
        1 mviccaavnc snrqgkgekr avsfhrfplk dskrliqwlk avqrdnwtpt kysflcsehf
       61 tkdsfskrle dqhrllkpta vpsifhlsek krgagghgpa rrkttgamrg htsaatgkgt
      121 igsslsssdn lmakpesrkl kraspqddta pkatpgavsq epgqslertp gdqaaplarg
      181 qeeaqvsate adhqkasssa adaggadksg ismddftppg sgackfigsl hsysfsskht
      241 rerpsvprep mdrkrlkrdi eprcsgnsva qsppssslta tpqkasqsps apptdvtpkp
      301 aaeavqsehs danpmsinev ilsasgackl idslhsycfs arqnksqvcc lreqvekkng
      361 elkslrqrvs rsdsqvrklr ekldelrras lpylpylsgl lppsheppkl npvveplswm
      421 lgtwlseppg vgtfptlqpf qyleevhish vgqpmlnfsf nsfhpethkp mhrecgfirl
      481 kpdtnkvafv saqntgvvev eegevngqel cvsshsisri sfakephvqq itrkfrlnse
      541 gkleqtvsma tttqpmtqhl hitykkvtp
//
LOCUS       NP_001009686             549 aa            linear   ROD 27-APR-2025
DEFINITION  DDB1- and CUL4-associated factor 11 [Rattus norvegicus].
ACCESSION   NP_001009686 XP_240183
VERSION     NP_001009686.1
DBSOURCE    REFSEQ: accession NM_001009686.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091364.1.
            
            On Jan 13, 2005 this sequence version replaced XP_240183.2.
            
            Transcript Variant: This variant (1) is the protein-coding variant.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091364.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..549
                     /product="DDB1- and CUL4-associated factor 11"
                     /note="WD repeat-containing protein 23; WD repeat domain
                     23"
                     /calculated_mol_wt=61746
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91VU6; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91VU6; propagated from
                     UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          80..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          170..210
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          <180..511
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          180..214
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          216..258
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          221..263
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          269..305
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          305..345
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          310..352
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          353..392
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          359..394
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          435..480
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          444..470
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          481..520
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M9G8.1)"
     Region          486..510
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..549
                     /gene="Dcaf11"
                     /gene_synonym="Wdr23"
                     /coded_by="NM_001009686.2:261..1910"
                     /db_xref="GeneID:305895"
                     /db_xref="RGD:1311288"
ORIGIN      
        1 mgsrnsssag sgslepsegl srrgaglrrs eeeeeededv dlaqvlayll rrgqvrlvqg
       61 ggaanlqliq alsdseeehd sawdgrlgdr ynppvdatpd treleyneik trvelatgrl
      121 glgrtaqehs fprmlhqrer glchrgsfsl geqsrvmshf lpndlsftdt ysqkafcgiy
      181 skdgqifmsa cqdqtirlyd crygrfhkfk sikardvgws vldvaftpdg nhflysswsd
      241 yihicsiyge gdthtaldlr pderrfavfs iavssdgrev lggandgcly vfdreqnrrt
      301 lqiesheddv navafadiss qilfsggdda ickvwdrrtm reddpkpvga laghqdgitf
      361 idskgdaryl isnskdqtik lwdirrfssr egmeasrlaa tqqnwdyrwq qvpkkawkkl
      421 klpgdsslmt yrghgvlhtl ircrfspahs tgqqfiysgc stgkvvvydl lsghivkklt
      481 nhkacvrdvs whpfeekivs sswdgslrlw qyrqaeyfqd dmtesdrnrv cssgpapvpc
      541 psvafsspq
//
LOCUS       NP_036950                205 aa            linear   ROD 27-APR-2025
DEFINITION  serotonin N-acetyltransferase [Rattus norvegicus].
ACCESSION   NP_036950
VERSION     NP_036950.1
DBSOURCE    REFSEQ: accession NM_012818.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Paiva,R.V.N., Mondes,P.H.L., Brandao,B.J., Sant'Anna,J.N., Freire
            Dos Santos,M.E., Fighera,Y.M., Santos,L.C., Markus,R.P.,
            Fernandes,P.A.C.M., Silva,J.F. and Tamura,E.K.
  TITLE     Effects of acute hypothyroidism on plasma melatonin and Aanat and
            Asmt expression in the pineal gland and gonads of rats
  JOURNAL   Front Endocrinol (Lausanne) 15, 1322867 (2024)
   PUBMED   39149125
  REMARK    GeneRIF: Effects of acute hypothyroidism on plasma melatonin and
            Aanat and Asmt expression in the pineal gland and gonads of rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Mohammadi,S., Zahmatkesh,M., Asgari,Y., Aminyavari,S. and
            Hassanzadeh,G.
  TITLE     Evaluation of hippocampal arylalkylamine N-acetyltransferase
            activity in amyloid-beta neurotoxicity
  JOURNAL   J Mol Endocrinol 71 (2), e220161 (2023)
   PUBMED   37256589
  REMARK    GeneRIF: Evaluation of hippocampal arylalkylamine
            N-acetyltransferase activity in amyloid-beta neurotoxicity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Coelho,L.A., Andrade-Silva,J., Motta-Teixeira,L.C., Amaral,F.G.,
            Reiter,R.J. and Cipolla-Neto,J.
  TITLE     The Absence of Pineal Melatonin Abolishes the Daily Rhythm of Tph1
            (Tryptophan Hydroxylase 1), Asmt (Acetylserotonin
            O-Methyltransferase), and Aanat (Aralkylamine N-Acetyltransferase)
            mRNA Expressions in Rat Testes
  JOURNAL   Mol Neurobiol 56 (11), 7800-7809 (2019)
   PUBMED   31124080
  REMARK    GeneRIF: The testes of control animals express the Tph1, Aanat, and
            Asmt and Per2 genes with 24-h rhythms in mRNA, reaching the maximal
            values during the dark phase.
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Chen,L., Zhou,T., Wu,N., O'Brien,A., Venter,J., Ceci,L.,
            Kyritsi,K., Onori,P., Gaudio,E., Sybenga,A., Xie,L., Wu,C.,
            Fabris,L., Invernizzi,P., Zawieja,D., Liangpunsakul,S., Meng,F.,
            Francis,H., Alpini,G., Huang,Q. and Glaser,S.
  TITLE     Pinealectomy or light exposure exacerbates biliary damage and liver
            fibrosis in cholestatic rats through decreased melatonin synthesis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1865 (6), 1525-1539 (2019)
   PUBMED   30890428
  REMARK    GeneRIF: Melatonin decreases biliary hyperplasia and liver fibrosis
            during cholestasis-induced biliary injury via melatonin-dependent
            autocrine signaling through increased biliary AANAT expression and
            melatonin secretion, downregulation of miR-200b and specific
            circadian clock genes.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Yang,Y., Sun,B., Huang,J., Xu,L., Pan,J., Fang,C., Li,M., Li,G.,
            Tao,Y., Yang,X., Wu,Y., Miao,P., Wang,Y., Li,H., Ren,J., Zhan,M.,
            Fang,Y., Feng,X. and Ding,X.
  TITLE     Up-regulation of miR-325-3p suppresses pineal aralkylamine
            N-acetyltransferase (Aanat) after neonatal hypoxia-ischemia brain
            injury in rats
  JOURNAL   Brain Res 1668, 28-35 (2017)
   PUBMED   28502584
  REMARK    GeneRIF: identified one microRNA, miR-325-3p, as a potential
            candidate responsible for the down regulation of Aanat after
            survivors of hypoxic-ischemic brain damage
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Borjigin,J., Wang,M.M. and Snyder,S.H.
  TITLE     Diurnal variation in mRNA encoding serotonin N-acetyltransferase in
            pineal gland
  JOURNAL   Nature 378 (6559), 783-785 (1995)
   PUBMED   8524412
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Coon,S.L., Roseboom,P.H., Baler,R., Weller,J.L., Namboodiri,M.A.,
            Koonin,E.V. and Klein,D.C.
  TITLE     Pineal serotonin N-acetyltransferase: expression cloning and
            molecular analysis
  JOURNAL   Science 270 (5242), 1681-1683 (1995)
   PUBMED   7502081
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Baler,R. and Klein,D.C.
  TITLE     Circadian expression of transcription factor Fra-2 in the rat
            pineal gland
  JOURNAL   J Biol Chem 270 (45), 27319-27325 (1995)
   PUBMED   7592994
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Kelly,S.L. and Sim,E.
  TITLE     Arylamine N-acetyltransferase in Balb/c mice: identification of a
            novel mouse isoenzyme by cloning and expression in vitro
  JOURNAL   Biochem J 302 (Pt 2) (Pt 2), 347-353 (1994)
   PUBMED   7545952
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Ritta,M.N. and Cardinali,D.P.
  TITLE     Prostaglandin E2 increases adenosine 3',5'-monophosphate
            concentration and binding-site occupancy, and stimulates
            serotonin-N-acetyltransferase activity in rat pineal glands in
            vitro
  JOURNAL   Mol Cell Endocrinol 23 (2), 151-159 (1981)
   PUBMED   6268470
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U38306.1.
            
            Summary: The protein encoded by this gene belongs to the
            acetyltransferase superfamily. It is the penultimate enzyme in
            melatonin synthesis and controls the night/day rhythm in melatonin
            production in the vertebrate pineal gland. Melatonin is essential
            for the function of the circadian clock that influences activity
            and sleep. This enzyme is regulated by cAMP-dependent
            phosphorylation that promotes its interaction with 14-3-3 proteins
            and thus protects the enzyme against proteasomal degradation. This
            gene may contribute to numerous genetic diseases such as delayed
            sleep phase syndrome. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U38306.1, DQ075321.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.2"
     Protein         1..205
                     /product="serotonin N-acetyltransferase"
                     /EC_number="2.3.1.87"
                     /note="arylakylamine N-acetyltransferase; serotonin
                     acetylase; Seretonin N-acetyltransferase; Arylalkylamine N
                     - acetyltransferase (Serotonin N - acetyltransferase);
                     arylalkylamine N-acetyltransferase"
                     /calculated_mol_wt=23011
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:O97756; propagated from
                     UniProtKB/Swiss-Prot (Q64666.1)"
     Region          35..182
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Site            118
                     /site_type="other"
                     /note="Important for the catalytic mechanism, involved in
                     substrate deprotonation.
                     /evidence=ECO:0000250|UniProtKB:Q29495; propagated from
                     UniProtKB/Swiss-Prot (Q64666.1)"
     Site            120
                     /site_type="other"
                     /note="Important for the catalytic mechanism, involved in
                     substrate deprotonation.
                     /evidence=ECO:0000250|UniProtKB:Q29495; propagated from
                     UniProtKB/Swiss-Prot (Q64666.1)"
     Site            122
                     /site_type="other"
                     /note="Important for the catalytic mechanism, involved in
                     substrate deprotonation. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q64666.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29495; propagated from
                     UniProtKB/Swiss-Prot (Q64666.1)"
     CDS             1..205
                     /gene="Aanat"
                     /gene_synonym="AA-NAT; Nat4"
                     /coded_by="NM_012818.2:116..733"
                     /db_xref="GeneID:25120"
                     /db_xref="RGD:2006"
ORIGIN      
        1 mlsihplkpe alhlplgtse flgcqrrhtl pasefrcltp edatsafeie reafisvsgt
       61 cplhldeirh fltlcpelsl gwfeegclva fiigslwdke rltqesltlh rpggrtahlh
      121 vlavhrtfrq qgkgsvllwr ylhhlgsqpa vrravlmcen alvpfyekfg fqamgpcait
      181 mgsltftelq cslrchtflr rnsgc
//
LOCUS       NP_058891                226 aa            linear   ROD 27-APR-2025
DEFINITION  neuromodulin [Rattus norvegicus].
ACCESSION   NP_058891
VERSION     NP_058891.1
DBSOURCE    REFSEQ: accession NM_017195.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Hu,Y., Sun,Y.F., Yuan,H., Liu,J., Chen,L., Liu,D.H., Xu,Y.,
            Zhou,X.F., Ding,L., Zhang,Z.T., Xiong,L.L., Xue,L.L. and Wang,T.H.
  TITLE     Vof16-miR-185-5p-GAP43 network improves the outcomes following
            spinal cord injury via enhancing self-repair and promoting axonal
            growth
  JOURNAL   CNS Neurosci Ther 30 (4), e14535 (2024)
   PUBMED   38168094
  REMARK    GeneRIF: Vof16-miR-185-5p-GAP43 network improves the outcomes
            following spinal cord injury via enhancing self-repair and
            promoting axonal growth.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Li,T., Jia,Y., Fu,J., Fu,Z., Qiao,Z., Liu,X., Lv,T., Tang,R. and
            Yang,G.
  TITLE     P53-induced GAP-43 Upregulation in Primary Cortical Neurons of Rats
  JOURNAL   Protein Pept Lett 31 (3), 229-235 (2024)
   PUBMED   38288820
  REMARK    GeneRIF: P53-induced GAP-43 Upregulation in Primary Cortical
            Neurons of Rats.
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Jyothi,A.K., Thotakura,B., Priyadarshini,S.C., Patil,S.,
            Poojari,M.S. and Subramanian,M.
  TITLE     Paternal stress alters synaptic density and expression of GAP-43,
            GRIN1, M1 and SYP genes in the hippocampus and cortex of offspring
            of stress-induced male rats
  JOURNAL   Morphologie 107 (356), 67-79 (2023)
   PUBMED   35715368
  REMARK    GeneRIF: Paternal stress alters synaptic density and expression of
            GAP-43, GRIN1, M1 and SYP genes in the hippocampus and cortex of
            offspring of stress-induced male rats.
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Zhao,H., Liu,Z.D., Zhang,Y.B., Gao,X.Y., Wang,C., Liu,Y. and
            Wang,X.F.
  TITLE     NEP1-40 promotes myelin regeneration via upregulation of GAP-43 and
            MAP-2 expression after focal cerebral ischemia in rats
  JOURNAL   Mol Med Rep 24 (6) (2021)
   PUBMED   34643252
  REMARK    GeneRIF: NEP140 promotes myelin regeneration via upregulation of
            GAP43 and MAP2 expression after focal cerebral ischemia in rats.
            Erratum:[Mol Med Rep. 2023 Mar;27(3):58. doi:
            10.3892/mmr.2023.12945. PMID: 36695184]
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Rahmati,M. and Taherabadi,S.J.
  TITLE     The effects of exercise training on Kinesin and GAP-43 expression
            in skeletal muscle fibers of STZ-induced diabetic rats
  JOURNAL   Sci Rep 11 (1), 9535 (2021)
   PUBMED   33953268
  REMARK    GeneRIF: The effects of exercise training on Kinesin and GAP-43
            expression in skeletal muscle fibers of STZ-induced diabetic rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Spencer,S.A., Schuh,S.M., Liu,W.S. and Willard,M.B.
  TITLE     GAP-43, a protein associated with axon growth, is phosphorylated at
            three sites in cultured neurons and rat brain
  JOURNAL   J Biol Chem 267 (13), 9059-9064 (1992)
   PUBMED   1533624
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Nedivi,E., Basi,G.S., Akey,I.V. and Skene,J.H.
  TITLE     A neural-specific GAP-43 core promoter located between unusual DNA
            elements that interact to regulate its activity
  JOURNAL   J Neurosci 12 (3), 691-704 (1992)
   PUBMED   1532026
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Houbre,D., Duportail,G., Deloulme,J.C. and Baudier,J.
  TITLE     The interactions of the brain-specific calmodulin-binding protein
            kinase C substrate, neuromodulin (GAP 43), with membrane
            phospholipids
  JOURNAL   J Biol Chem 266 (11), 7121-7131 (1991)
   PUBMED   1826685
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Rosenthal,A., Chan,S.Y., Henzel,W., Haskell,C., Kuang,W.J.,
            Chen,E., Wilcox,J.N., Ullrich,A., Goeddel,D.V. and Routtenberg,A.
  TITLE     Primary structure and mRNA localization of protein F1, a
            growth-related protein kinase C substrate associated with synaptic
            plasticity
  JOURNAL   EMBO J 6 (12), 3641-3646 (1987)
   PUBMED   3428269
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Karns,L.R., Ng,S.C., Freeman,J.A. and Fishman,M.C.
  TITLE     Cloning of complementary DNA for GAP-43, a neuronal growth-related
            protein
  JOURNAL   Science 236 (4801), 597-600 (1987)
   PUBMED   2437653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X06338.1, BF560544.1 and BI304179.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X06338.1, BC127502.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..226
                     /product="neuromodulin"
                     /note="brain abundant, membrane attached signal protein 2;
                     protein F1; axonal membrane protein GAP-43; growth
                     accentuating protein 43"
                     /calculated_mol_wt=23472
     Region          1..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07936.1)"
     Region          2..31
                     /region_name="Neuromodulin_N"
                     /note="Gap junction protein N-terminal region; pfam10580"
                     /db_xref="CDD:431370"
     Region          30..52
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PHK and PKC.
                     /evidence=ECO:0000269|PubMed:1533624,
                     ECO:0000269|PubMed:8454596; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Region          73..226
                     /region_name="Neuromodulin"
                     /note="pfam06614"
                     /db_xref="CDD:461961"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:1533624,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06837; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06837; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06837; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:1533624, ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07936.1)"
     CDS             1..226
                     /gene="Gap43"
                     /gene_synonym="Basp2"
                     /coded_by="NM_017195.3:217..897"
                     /db_xref="GeneID:29423"
                     /db_xref="RGD:62071"
ORIGIN      
        1 mlccmrrtkq vekndedqki eqdgvkpedk ahkaatkiqa sfrghitrkk lkdekkgdap
       61 aaeaeakekd dapvadgvek kegdgsattd aapatspkae epskagdaps eekkgegdaa
      121 pseekagsae tesaakattd nspsskaedg pakeepkqad vpaavtdaaa ttpaaedaak
      181 aaqpptetae ssqaeeekea vdeakpkesa rqdegkedpe adqeha
//
LOCUS       NP_001030112             217 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC-type and RNA-binding motif-containing protein 1
            [Rattus norvegicus].
ACCESSION   NP_001030112 XP_343321
VERSION     NP_001030112.1
DBSOURCE    REFSEQ: accession NM_001034940.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099747.1.
            
            On Oct 21, 2005 this sequence version replaced XP_343321.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099747.1, SRR8487227.64010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..217
                     /product="zinc finger CCHC-type and RNA-binding
                     motif-containing protein 1"
                     /note="U11/U12 snRNP 31 kDa protein; U11/U12 small nuclear
                     ribonucleoprotein 31 kDa protein; zinc finger CCHC-type
                     and RNA binding motif 1"
                     /calculated_mol_wt=24414
     Region          9..84
                     /region_name="RRM_ZCRB1"
                     /note="RNA recognition motif (RRM) found in Zinc finger
                     CCHC-type and RNA-binding motif-containing protein 1
                     (ZCRB1) and similar proteins; cd12393"
                     /db_xref="CDD:409827"
     Region          <97..123
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          120..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V6.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBF4; propagated from
                     UniProtKB/Swiss-Prot (Q499V6.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBF4; propagated from
                     UniProtKB/Swiss-Prot (Q499V6.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBF4; propagated from
                     UniProtKB/Swiss-Prot (Q499V6.1)"
     CDS             1..217
                     /gene="Zcrb1"
                     /gene_synonym="RGD1309851"
                     /coded_by="NM_001034940.1:140..793"
                     /db_xref="GeneID:362990"
                     /db_xref="RGD:1309851"
ORIGIN      
        1 msgglapsks tvyvsnlpfs ltnndlyrif skygkvvkvt imkdkdtrks kgvafilfld
       61 kdsalnctra innkqlfgrv ikasiaidng raaefirrrn yfdkskcyec gesghlsyac
      121 pknmlgerep pkkkekkkkk kvpepeeeie evevseeege dpaldslsqa iafqqakiee
      181 eqnkwrpstg gpstsddsrr prikksayfs deeelsd
//
LOCUS       NP_110494                359 aa            linear   ROD 27-APR-2025
DEFINITION  NF-kappa-B inhibitor beta [Rattus norvegicus].
ACCESSION   NP_110494
VERSION     NP_110494.2
DBSOURCE    REFSEQ: accession NM_030867.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Zhao,H. and Gong,N.
  TITLE     miR-20a regulates inflammatory in osteoarthritis by targeting the
            IkappaBbeta and regulates NK-kappaB signaling pathway activation
  JOURNAL   Biochem Biophys Res Commun 518 (4), 632-637 (2019)
   PUBMED   31451219
  REMARK    GeneRIF: Results indicate an increase in articular cavity
            inflammation in rats with osteoarthritis (OA) in the presence of
            miR-20a by targeting on NFKB inhibitor beta (IkappaBbeta) and
            activating the NF-kappa B (NF-kappaB) signaling pathway.
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Gu,H., Cui,M., Bai,Y., Chen,F., Ma,K., Zhou,C. and Guo,L.
  TITLE     Angiopoietin-1/Tie2 signaling pathway inhibits
            lipopolysaccharide-induced activation of RAW264.7 macrophage cells
  JOURNAL   Biochem Biophys Res Commun 392 (2), 178-182 (2010)
   PUBMED   20060382
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Hayden,M.S. and Ghosh,S.
  TITLE     Shared principles in NF-kappaB signaling
  JOURNAL   Cell 132 (3), 344-362 (2008)
   PUBMED   18267068
  REMARK    Review article
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Xu,S., Bayat,H., Hou,X. and Jiang,B.
  TITLE     Ribosomal S6 kinase-1 modulates interleukin-1beta-induced
            persistent activation of NF-kappaB through phosphorylation of
            IkappaBbeta
  JOURNAL   Am J Physiol Cell Physiol 291 (6), C1336-C1345 (2006)
   PUBMED   16822942
  REMARK    GeneRIF: Data suggest that RSK1 directly phosphorylates IkappaBbeta
            and contributes to the persistent activation of NF-kappaB by
            IL-1beta.
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Nakajima,K., Matsushita,Y., Tohyama,Y., Kohsaka,S. and Kurihara,T.
  TITLE     Differential suppression of endotoxin-inducible inflammatory
            cytokines by nuclear factor kappa B (NFkappaB) inhibitor in rat
            microglia
  JOURNAL   Neurosci Lett 401 (3), 199-202 (2006)
   PUBMED   16580131
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Stasiolek,M., Gavrilyuk,V., Sharp,A., Horvath,P., Selmaj,K. and
            Feinstein,D.L.
  TITLE     Inhibitory and stimulatory effects of lactacystin on expression of
            nitric oxide synthase type 2 in brain glial cells. The role of
            Ikappa B-beta
  JOURNAL   J Biol Chem 275 (32), 24847-24856 (2000)
   PUBMED   10827092
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Jaffray,C., Mendez,C., Denham,W., Carter,G. and Norman,J.
  TITLE     Specific pancreatic enzymes activate macrophages to produce tumor
            necrosis factor-alpha: role of nuclear factor kappa B and
            inhibitory kappa B proteins
  JOURNAL   J Gastrointest Surg 4 (4), 370-7 (2000)
   PUBMED   11058855
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Cheshire,J.L. and Baldwin,A.S. Jr.
  TITLE     Synergistic activation of NF-kappaB by tumor necrosis factor alpha
            and gamma interferon via enhanced I kappaB alpha degradation and de
            novo I kappaBbeta degradation
  JOURNAL   Mol Cell Biol 17 (11), 6746-6754 (1997)
   PUBMED   9343439
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085729.1.
            
            On Nov 15, 2004 this sequence version replaced NP_110494.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085729.1, FQ235103.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..359
                     /product="NF-kappa-B inhibitor beta"
                     /note="ikB-B; ikB-beta; ikappaBbeta; NF-kappa-BIB; nuclear
                     factor of kappa light chain gene enhancer in B-cells
                     inhibitor, beta; I-kappa-B-beta; nuclear factor of kappa
                     light polypeptide gene enhancer in B-cells inhibitor,
                     beta"
                     /calculated_mol_wt=37951
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:16822942; propagated from
                     UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:16822942; propagated from
                     UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          56..310
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(57,59,63..64,67..69,71..72,76,79,91,93,95,99..100,
                     103..105,107..108,112,115,124,126,128,132..133,136..138,
                     140..141,145,148)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          57..91
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          57..86
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          93..124
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          93..122
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          126..155
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          153..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Site            order(206,208,212..213,216..218,220..221,225,228,237,239,
                     242,246..247,250..252,254..255,259,262,271,273,275,
                     279..280,283..285,287..288,292,295)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          206..237
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..235
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          239..271
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          240..269
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          273..302
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Region          273..298
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          298..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIA3.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15653; propagated from
                     UniProtKB/Swiss-Prot (Q9JIA3.1)"
     CDS             1..359
                     /gene="Nfkbib"
                     /coded_by="NM_030867.2:260..1339"
                     /db_xref="GeneID:81525"
                     /db_xref="RGD:621887"
ORIGIN      
        1 magvaclgkt adadewcdsg lgslgpdaaa pggpglvael spelswaplv fgyvtedgdt
       61 alhlavihqh epfldfllgf sagteyldlq ndlgqtalhl aailgeastv eklyaagagv
      121 lvtergghta lhlacrvrah tcayvllqpr pshprdasdt yltqsqdhtp dtshapvatd
      181 pqpnpgneee lrdedwrlql eaenydghtp lhvavihkda emvqllrdag adlnkpeptc
      241 grtplhlave gqaagvlall lkagadptar myggrtplgs allrpnpvla rllrahgape
      301 pededdklsp csnsssdsds dnrdegdeyd divvhsrrsq nqpppspaak plpddpnpa
//
LOCUS       NP_001103137             271 aa            linear   ROD 27-APR-2025
DEFINITION  TIP41-like protein [Rattus norvegicus].
ACCESSION   NP_001103137 XP_341146
VERSION     NP_001103137.1
DBSOURCE    REFSEQ: accession NM_001109667.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   McConnell,J.L., Gomez,R.J., McCorvey,L.R., Law,B.K. and
            Wadzinski,B.E.
  TITLE     Identification of a PP2A-interacting protein that functions as a
            negative regulator of phosphatase activity in the ATM/ATR signaling
            pathway
  JOURNAL   Oncogene 26 (41), 6021-6030 (2007)
   PUBMED   17384681
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128780.1.
            
            On Sep 7, 2008 this sequence version replaced XP_341146.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128780.1, CK367135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..271
                     /product="TIP41-like protein"
                     /note="TIP41, TOR signaling pathway regulator-like;
                     CG9578-like; TIP41, TOR signalling pathway regulator-like"
                     /calculated_mol_wt=31094
     Region          50..218
                     /region_name="TIP41"
                     /note="TIP41-like family; pfam04176"
                     /db_xref="CDD:461208"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75663; propagated from
                     UniProtKB/Swiss-Prot (A2VCX1.1)"
     Region          173..271
                     /region_name="Interaction with PPP2CA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VCX1.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75663; propagated from
                     UniProtKB/Swiss-Prot (A2VCX1.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2VCX1.1)"
     CDS             1..271
                     /gene="Tiprl"
                     /gene_synonym="RGD1310442"
                     /coded_by="NM_001109667.1:46..861"
                     /db_xref="GeneID:360869"
                     /db_xref="RGD:1310442"
ORIGIN      
        1 mmihgfqssh qdfsfgpwkl taskthimks advekladel hmpslpemmf gdnvlriqhg
       61 sgfgiefnat dalrcvnnyq gmlkvacaee wqesrtegeh skevikpydw tyttdykgtl
      121 lgeslklkvv pttdhidtek lkareqikff eevllfedel hdhgvsslsv kirvmpssff
      181 lllrfflrid gvlirmndtr lyheadktym lreytsresk ianlmhvpps lftepneisq
      241 ylpikeavce klvfperidp npvdsesaps e
//
LOCUS       NP_001012220             584 aa            linear   ROD 27-APR-2025
DEFINITION  cation channel sperm-associated protein 2 [Rattus norvegicus].
ACCESSION   NP_001012220 XP_345426 XP_347328
VERSION     NP_001012220.1
DBSOURCE    REFSEQ: accession NM_001012220.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Ameli,M., Moghimian,M., Saeb,F., Bashtani,E., Shokoohi,M.,
            Salimnejad,R. and Abtahi,H.
  TITLE     The effect of clomiphene citrate and human chorionic gonadotropin
            on the expression of CatSper1, CatSper2, LHCGR, and SF1 genes, as
            well as the structural changes in testicular tissue of adult rats
  JOURNAL   Mol Reprod Dev 86 (6), 738-748 (2019)
   PUBMED   31041823
  REMARK    GeneRIF: The effect of clomiphene citrate and human chorionic
            gonadotropin on the expression of CatSper1, CatSper2, LHCGR, and
            SF1 genes, as well as the structural changes in testicular tissue
            of adult rats.
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Zhang,Z., Wang,G.L., Li,H.X., Li,L., Cui,Q.W., Wei,C.B. and Zhou,F.
  TITLE     Regulation of fertilization in male rats by CatSper2 knockdown
  JOURNAL   Asian J Androl 14 (2), 301-309 (2012)
   PUBMED   22002435
  REMARK    GeneRIF: It is feasible to achieve male contraception by silencing
            the expression of CatSper2, the key protein involved in sperm
            hyperactivation.
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Chung,J.J., Navarro,B., Krapivinsky,G., Krapivinsky,L. and
            Clapham,D.E.
  TITLE     A novel gene required for male fertility and functional CATSPER
            channel formation in spermatozoa
  JOURNAL   Nat Commun 2, 153 (2011)
   PUBMED   21224844
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Marquez,B., Ignotz,G. and Suarez,S.S.
  TITLE     Contributions of extracellular and intracellular Ca2+ to regulation
            of sperm motility: Release of intracellular stores can
            hyperactivate CatSper1 and CatSper2 null sperm
  JOURNAL   Dev Biol 303 (1), 214-221 (2007)
   PUBMED   17174296
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Qi,H., Moran,M.M., Navarro,B., Chong,J.A., Krapivinsky,G.,
            Krapivinsky,L., Kirichok,Y., Ramsey,I.S., Quill,T.A. and
            Clapham,D.E.
  TITLE     All four CatSper ion channel proteins are required for male
            fertility and sperm cell hyperactivated motility
  JOURNAL   Proc Natl Acad Sci U S A 104 (4), 1219-1223 (2007)
   PUBMED   17227845
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Quill,T.A., Sugden,S.A., Rossi,K.L., Doolittle,L.K., Hammer,R.E.
            and Garbers,D.L.
  TITLE     Hyperactivated sperm motility driven by CatSper2 is required for
            fertilization
  JOURNAL   Proc Natl Acad Sci U S A 100 (25), 14869-14874 (2003)
   PUBMED   14657366
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Quill,T.A., Ren,D., Clapham,D.E. and Garbers,D.L.
  TITLE     A voltage-gated ion channel expressed specifically in spermatozoa
  JOURNAL   Proc Natl Acad Sci U S A 98 (22), 12527-12531 (2001)
   PUBMED   11675491
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079422.1.
            
            On or before Feb 11, 2005 this sequence version replaced
            XP_345426.1, XP_347328.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..584
                     /product="cation channel sperm-associated protein 2"
                     /calculated_mol_wt=68135
     Region          105..348
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            107..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Site            139..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Site            174..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Site            202..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Site            238..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Site            313..339
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Region          <351..>494
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          376..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     Region          <422..456
                     /region_name="ANAPC15"
                     /note="Anaphase-promoting complex subunit 15; pfam15243"
                     /db_xref="CDD:464583"
     Region          480..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP6.1)"
     CDS             1..584
                     /gene="Catsper2"
                     /coded_by="NM_001012220.1:353..2107"
                     /db_xref="GeneID:366174"
                     /db_xref="RGD:1307620"
ORIGIN      
        1 maherghlql pradairskl idtfsliehl qglsqavprh tlreildpac qkklmlgdqe
       61 qlvrfsirar rmghithaqr llsrlrvrcg grpplslwag wvldssifsn fiisliflnt
      121 fvlmveielm nstntslwpl klalevtdwf illsfiveil lmwlasfflf wknawsvfdf
      181 vvtmlsllpe fvvligvsad svwlqllrvs rvlrslklfa rfpqikvill alvralksmt
      241 fllmllliff yvfavagvyf fkeysrstie nleynmffsd llnslvtvfi lftldhwyav
      301 lqdvwkvpea srvfssiyvi lwlllgsiif rniivammvt nfqnirnelh eemthlevqy
      361 kadifkrrii qrrqqseslr gtsqgkvsed itetseatde ekseaeesee ekseeeksdv
      421 eksdeeknde eksdeeende eksdveksde ekndeekgyt ekvysgrtfv ersyaersfa
      481 gkaenekvqk elkekaypgs ppnssshdea faaddtylen ldwetlvhen lpglmdmdqd
      541 drvvwprdsl fryfellesl qynleerkrl qefavqalmn fedk
//
LOCUS       NP_077067                494 aa            linear   ROD 27-APR-2025
DEFINITION  NADPH:adrenodoxin oxidoreductase, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_077067
VERSION     NP_077067.1
DBSOURCE    REFSEQ: accession NM_024153.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Bubenek,S., Nastase,A., Niculescu,A.M., Baila,S., Herlea,V.,
            Lazar,V., Paslaru,L., Botezatu,A., Tomescu,D., Popescu,I. and
            Dima,S.
  TITLE     Assessment of gene expression profiles in peripheral occlusive
            arterial disease
  JOURNAL   Can J Cardiol 28 (6), 712-720 (2012)
   PUBMED   22721676
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Miller,W.L.
  TITLE     Androgen synthesis in adrenarche
  JOURNAL   Rev Endocr Metab Disord 10 (1), 3-17 (2009)
   PUBMED   18821018
  REMARK    Review article
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Sagara,Y., Watanabe,Y., Kodama,H. and Aramaki,H.
  TITLE     cDNA cloning, overproduction and characterization of rat
            adrenodoxin reductase
  JOURNAL   Biochim Biophys Acta 1434 (2), 284-295 (1999)
   PUBMED   10525147
REFERENCE   7  (residues 1 to 494)
  AUTHORS   McLean,M.P., Nelson,S.E., Billheimer,J.T. and Gibori,G.
  TITLE     Differential capacity for cholesterol transport and processing in
            large and small rat luteal cells
  JOURNAL   Endocrinology 131 (5), 2203-2212 (1992)
   PUBMED   1425418
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Hanukoglu,I., Suh,B.S., Himmelhoch,S. and Amsterdam,A.
  TITLE     Induction and mitochondrial localization of cytochrome P450scc
            system enzymes in normal and transformed ovarian granulosa cells
  JOURNAL   J Cell Biol 111 (4), 1373-1381 (1990)
   PUBMED   2170421
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D63761.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D63761.1, BC088844.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..494
                     /product="NADPH:adrenodoxin oxidoreductase, mitochondrial
                     precursor"
                     /EC_number="1.18.1.6"
                     /note="NADPH:adrenodoxin oxidoreductase, mitochondrial;
                     ferredoxin--NADP(+) reductase; adrenodoxin reductase"
                     /calculated_mol_wt=50317
     transit_peptide 1..34
                     /calculated_mol_wt=4064
     Region          20..489
                     /region_name="PLN02852"
                     /note="ferredoxin-NADP+ reductase; cl30539"
                     /db_xref="CDD:357415"
     mat_peptide     35..494
                     /product="NADPH:adrenodoxin oxidoreductase, mitochondrial"
                     /calculated_mol_wt=50317
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22570; propagated from
                     UniProtKB/Swiss-Prot (P56522.1)"
     CDS             1..494
                     /gene="Fdxr"
                     /gene_synonym="AR"
                     /coded_by="NM_024153.1:23..1507"
                     /db_xref="GeneID:79122"
                     /db_xref="RGD:621648"
ORIGIN      
        1 maprcwrwws wsawpgvrpl psrstptpgf ckkfstqett pqicvvgsgp agfytaqhll
       61 khhtrahvdi yekqlvpfgl vrfgvapdhp evknvintft qtarsdrcaf rgnvvvgrdv
      121 svpelreayh avvlsygaed hqpleipgee lpgvvsaraf vgwynglpen qklapdlscd
      181 tavilgqgnv aldvarillt ppehlektdi tevalgvlrq srvktvwivg rrgplqvaft
      241 ikelremiql pgtqpildps dflglqdrik dvprprkrlt elllrtatek pgveeaarra
      301 lasrawglrf frspqqvlpt pdgrrvagir lavtrlegvg estravptgd vedlpcglll
      361 ssvgyksrpi dpsvpfdpkl giipntegrv vnapglycsg wvkrgptgvi tttmtdsflt
      421 sqvllkdlka gllpsgprpg ytaiqallsd rgvrpvsfsd wekldaeeva rgqgtgkpre
      481 klvdrremlq llgh
//
LOCUS       NP_001020918             236 aa            linear   ROD 27-APR-2025
DEFINITION  protein YIPF6 [Rattus norvegicus].
ACCESSION   NP_001020918 XP_343796
VERSION     NP_001020918.1
DBSOURCE    REFSEQ: accession NM_001025747.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Soonthornsit,J., Sakai,N., Sasaki,Y., Watanabe,R., Osako,S. and
            Nakamura,N.
  TITLE     YIPF1, YIPF2, and YIPF6 are medial-/trans-Golgi and trans-Golgi
            network-localized Yip domain family proteins, which play a role in
            the Golgi reassembly and glycan synthesis
  JOURNAL   Exp Cell Res 353 (2), 100-108 (2017)
   PUBMED   28286305
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Brandl,K., Tomisato,W., Li,X., Neppl,C., Pirie,E., Falk,W., Xia,Y.,
            Moresco,E.M., Baccala,R., Theofilopoulos,A.N., Schnabl,B. and
            Beutler,B.
  TITLE     Yip1 domain family, member 6 (Yipf6) mutation induces spontaneous
            intestinal inflammation in mice
  JOURNAL   Proc Natl Acad Sci U S A 109 (31), 12650-12655 (2012)
   PUBMED   22802641
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097987.1.
            
            On Jul 22, 2005 this sequence version replaced XP_343796.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097987.1, FQ103556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..236
                     /product="protein YIPF6"
                     /note="YIP1 family member 6"
                     /calculated_mol_wt=25976
     Region          2..232
                     /region_name="YIP1"
                     /note="Rab GTPase interacting factor, Golgi membrane
                     protein [Intracellular trafficking and secretion];
                     cl46908"
                     /db_xref="CDD:481248"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96EC8; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU5.1)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU5.1)"
     CDS             1..236
                     /gene="Yipf6"
                     /coded_by="NM_001025747.1:6..716"
                     /db_xref="GeneID:363476"
                     /db_xref="RGD:1566154"
ORIGIN      
        1 maeaedspge qeatsskplf aglsdvsisq dipiegeiti psgtraqecd sstlnesirr
       61 timrdlkavg rkfmhvlypr ksntllrdwd lwgplilcvs lalmlqkssv egkrdggspe
      121 faevfviiwf gavtitlnsk llggnisffq slcvlgycvl plniamlicr llllagqgpi
      181 nfmirlfvvl vmfawsvias tafladcqpp nrkalavypv flfyfvvswm iltftp
//
LOCUS       NP_001101931             218 aa            linear   ROD 27-APR-2025
DEFINITION  tubulin polymerization-promoting protein [Rattus norvegicus].
ACCESSION   NP_001101931 XP_001060230 XP_341747
VERSION     NP_001101931.1
DBSOURCE    REFSEQ: accession NM_001108461.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Fu,M.M., McAlear,T.S., Nguyen,H., Oses-Prieto,J.A., Valenzuela,A.,
            Shi,R.D., Perrino,J.J., Huang,T.T., Burlingame,A.L., Bechstedt,S.
            and Barres,B.A.
  TITLE     The Golgi Outpost Protein TPPP Nucleates Microtubules and Is
            Critical for Myelination
  JOURNAL   Cell 179 (1), 132-146 (2019)
   PUBMED   31522887
  REMARK    GeneRIF: These results demonstrate that TPPP on Golgi outposts are
            important for local microtubule nucleation and myelin sheath
            elongation.
REFERENCE   2  (residues 1 to 218)
  AUTHORS   DeBonis,S., Neumann,E. and Skoufias,D.A.
  TITLE     Self protein-protein interactions are involved in TPPP/p25 mediated
            microtubule bundling
  JOURNAL   Sci Rep 5, 13242 (2015)
   PUBMED   26289831
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Ejlerskov,P., Rasmussen,I., Nielsen,T.T., Bergstrom,A.L.,
            Tohyama,Y., Jensen,P.H. and Vilhardt,F.
  TITLE     Tubulin polymerization-promoting protein (TPPP/p25alpha) promotes
            unconventional secretion of alpha-synuclein through exophagy by
            impairing autophagosome-lysosome fusion
  JOURNAL   J Biol Chem 288 (24), 17313-17335 (2013)
   PUBMED   23629650
  REMARK    GeneRIF: Exophagy, with or without expression of TPPP, may be an
            important physiological mechanism for unconventional secretion of
            alpha-synuclein from dopaminergic neurons.
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Schofield,A.V., Steel,R. and Bernard,O.
  TITLE     Rho-associated coiled-coil kinase (ROCK) protein controls
            microtubule dynamics in a novel signaling pathway that regulates
            cell migration
  JOURNAL   J Biol Chem 287 (52), 43620-43629 (2012)
   PUBMED   23093407
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Heng,Y.W., Lim,H.H., Mina,T., Utomo,P., Zhong,S., Lim,C.T. and
            Koh,C.G.
  TITLE     TPPP acts downstream of RhoA-ROCK-LIMK2 to regulate astral
            microtubule organization and spindle orientation
  JOURNAL   J Cell Sci 125 (Pt 6), 1579-1590 (2012)
   PUBMED   22328514
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Goldbaum,O., Jensen,P.H. and Richter-Landsberg,C.
  TITLE     The expression of tubulin polymerization promoting protein
            TPPP/p25alpha is developmentally regulated in cultured rat brain
            oligodendrocytes and affected by proteolytic stress
  JOURNAL   Glia 56 (16), 1736-1746 (2008)
   PUBMED   18563798
  REMARK    GeneRIF: Malfunction of the proteasomal system, leading to the
            accumulation of aggregation prone proteins and the pro-aggregatory
            protein TPPP/p25alpha, is causally related to the protein
            aggregation process in a variety of neurodegenerative diseases.
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Acevedo,K., Li,R., Soo,P., Suryadinata,R., Sarcevic,B.,
            Valova,V.A., Graham,M.E., Robinson,P.J. and Bernard,O.
  TITLE     The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its
            ability to assemble microtubules
  JOURNAL   Exp Cell Res 313 (20), 4091-4106 (2007)
   PUBMED   18028908
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Vincze,O., Tokesi,N., Olah,J., Hlavanda,E., Zotter,A., Horvath,I.,
            Lehotzky,A., Tirian,L., Medzihradszky,K.F., Kovacs,J., Orosz,F. and
            Ovadi,J.
  TITLE     Tubulin polymerization promoting proteins (TPPPs): members of a new
            family with distinct structures and functions
  JOURNAL   Biochemistry 45 (46), 13818-13826 (2006)
   PUBMED   17105200
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Lindersson,E., Lundvig,D., Petersen,C., Madsen,P., Nyengaard,J.R.,
            Hojrup,P., Moos,T., Otzen,D., Gai,W.P., Blumbergs,P.C. and
            Jensen,P.H.
  TITLE     p25alpha Stimulates alpha-synuclein aggregation and is co-localized
            with aggregated alpha-synuclein in alpha-synucleinopathies
  JOURNAL   J Biol Chem 280 (7), 5703-5715 (2005)
   PUBMED   15590652
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474002.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_341747.2, XP_001060230.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK600925.1, CK357749.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00155336,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..218
                     /product="tubulin polymerization-promoting protein"
                     /note="p25-alpha; 25 kDa brain-specific protein"
                     /calculated_mol_wt=23415
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Region          2..115
                     /region_name="Mediates interaction with LIMK1.
                     /evidence=ECO:0000250|UniProtKB:O94811"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Region          51..206
                     /region_name="p25-alpha"
                     /note="pfam05517"
                     /db_xref="CDD:461670"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQD2; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94811; propagated from
                     UniProtKB/Swiss-Prot (D3ZQL7.1)"
     Region          165..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZQL7.1)"
     CDS             1..218
                     /gene="Tppp"
                     /gene_synonym="RGD1310121; TPPP/p25"
                     /coded_by="NM_001108461.1:81..737"
                     /db_xref="GeneID:361466"
                     /db_xref="RGD:1310121"
ORIGIN      
        1 madskakptk aanktppksp gdpakaakrl sleseganeg aaaapelsal eeafrrfavh
       61 gdtratgkem hgknwsklck dchvidgknv tvtdvdivfs kikgkscrti tfeqfqeale
      121 elakkrfkdk sseeavrevh rliegrapvi sgvtkavssp tvsrltdtsk ftgshkerfd
      181 qsgkgkgkag rvdlvdesgy vpgykhagty dqkvqggk
//
LOCUS       NP_001005539             445 aa            linear   ROD 27-APR-2025
DEFINITION  cyclic GMP-AMP phosphodiesterase SMPDL3A precursor [Rattus
            norvegicus].
ACCESSION   NP_001005539 XP_215397
VERSION     NP_001005539.1
DBSOURCE    REFSEQ: accession NM_001005539.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Lim,S.M., Yeung,K., Tresaugues,L., Ling,T.H. and Nordlund,P.
  TITLE     The structure and catalytic mechanism of human sphingomyelin
            phosphodiesterase like 3a--an acid sphingomyelinase homologue with
            a novel nucleotide hydrolase activity
  JOURNAL   FEBS J 283 (6), 1107-1123 (2016)
   PUBMED   26783088
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Heinz,L.X., Baumann,C.L., Koberlin,M.S., Snijder,B., Gawish,R.,
            Shui,G., Sharif,O., Aspalter,I.M., Muller,A.C., Kandasamy,R.K.,
            Breitwieser,F.P., Pichlmair,A., Bruckner,M., Rebsamen,M., Bluml,S.,
            Karonitsch,T., Fauster,A., Colinge,J., Bennett,K.L., Knapp,S.,
            Wenk,M.R. and Superti-Furga,G.
  TITLE     The Lipid-Modifying Enzyme SMPDL3B Negatively Regulates Innate
            Immunity
  JOURNAL   Cell Rep 11 (12), 1919-1928 (2015)
   PUBMED   26095358
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Traini,M., Quinn,C.M., Sandoval,C., Johansson,E., Schroder,K.,
            Kockx,M., Meikle,P.J., Jessup,W. and Kritharides,L.
  TITLE     Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel
            nucleotide phosphodiesterase regulated by cholesterol in human
            macrophages
  JOURNAL   J Biol Chem 289 (47), 32895-32913 (2014)
   PUBMED   25288789
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Yang,Y., Yin,J., Baumgartner,W., Samapati,R., Solymosi,E.A.,
            Reppien,E., Kuebler,W.M. and Uhlig,S.
  TITLE     Platelet-activating factor reduces endothelial nitric oxide
            production: role of acid sphingomyelinase
  JOURNAL   Eur Respir J 36 (2), 417-427 (2010)
   PUBMED   19926744
  REMARK    GeneRIF: Platelet-activating factor reduces endothelial nitric
            oxide production: role of acid sphingomyelinase
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Wright,K.O., Messing,E.M. and Reeder,J.E.
  TITLE     Increased expression of the acid sphingomyelinase-like protein
            ASML3a in bladder tumors
  JOURNAL   J Urol 168 (6), 2645-2649 (2002)
   PUBMED   12442002
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082029.1.
            
            On Oct 8, 2004 this sequence version replaced XP_215397.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..445
                     /product="cyclic GMP-AMP phosphodiesterase SMPDL3A
                     precursor"
                     /EC_number="3.6.1.15"
                     /note="ASM-like phosphodiesterase 3a; acid
                     sphingomyelinase-like phosphodiesterase 3A; 2',3'-cGAMP
                     phosphodiesterase SMPDL3A; cyclic GMP-AMP
                     phosphodiesterase SMPDL3A"
                     /calculated_mol_wt=47607
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2307
     mat_peptide     23..445
                     /product="Cyclic GMP-AMP phosphodiesterase SMPDL3A.
                     /id=PRO_0000002330"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z7.1)"
                     /calculated_mol_wt=47607
     Region          37..333
                     /region_name="MPP_ASMase"
                     /note="acid sphingomyelinase and related proteins,
                     metallophosphatase domain; cd00842"
                     /db_xref="CDD:277321"
     Site            order(42,44,107,148..149,249,290,292)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277321"
     Site            order(42,44,107,148,249,290,292)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277321"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     Region          305..444
                     /region_name="ASMase_C"
                     /note="Acid sphingomyelin phosphodiesterase C-terminal
                     region; pfam19272"
                     /db_xref="CDD:466022"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q641Z7.1)"
     CDS             1..445
                     /gene="Smpdl3a"
                     /coded_by="NM_001005539.1:15..1352"
                     /db_xref="GeneID:294422"
                     /db_xref="RGD:1359277"
ORIGIN      
        1 malpgnflcc llvawlcdpg lgvplapayg apavgqfwhv tdlhldptyh itddhtkvca
       61 sskganvsnp gpfgdvlcds pyqlilsafd fiknsgqeas fmiwtgdspp hvpvrelstg
      121 svievitnmt vtvqnlfpnl qvfpalgnhd ywpqdqlpia tskvysavsd lwkpwldeea
      181 istlrkggfy sqkvasnpdl riislntnly ygpnimtlnk tdpanqfewl entlnsslrn
      241 kekvyviahv pvgylpyatk tpamrqyyne klvdifrrys sviagqfygh thrdslmvls
      301 dkngnpinsv fvapavtpvk gvleketnnp gvrlfqykpg dytlldmlqy ylnlteanlk
      361 gesnwtleyt ltqaygvadl qpkslhglaq qlatidskqf lkyyhyffvs ydssapcdqr
      421 cktlqicaim nldlvsyedc lkrhl
//
LOCUS       NP_445932                600 aa            linear   ROD 27-APR-2025
DEFINITION  DNA polymerase alpha subunit B [Rattus norvegicus].
ACCESSION   NP_445932
VERSION     NP_445932.2
DBSOURCE    REFSEQ: accession NM_053480.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Baranovskiy,A.G., Lada,A.G., Siebler,H.M., Zhang,Y., Pavlov,Y.I.
            and Tahirov,T.H.
  TITLE     DNA polymerase delta and zeta switch by sharing accessory subunits
            of DNA polymerase delta
  JOURNAL   J Biol Chem 287 (21), 17281-17287 (2012)
   PUBMED   22465957
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Popanda,O., Flohr,C., Dai,J.C., Hunzicker,A. and Thielmann,H.W.
  TITLE     A mutation in subunit B of the DNA polymerase alpha-primase complex
            from Novikoff hepatoma cells concomitant with a conformational
            change and abnormal catalytic properties of the DNA polymerase
            alpha-primase complex
  JOURNAL   Mol Carcinog 31 (4), 171-183 (2001)
   PUBMED   11536367
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Mizuno,T., Ito,N., Yokoi,M., Kobayashi,A., Tamai,K., Miyazawa,H.
            and Hanaoka,F.
  TITLE     The second-largest subunit of the mouse DNA polymerase
            alpha-primase complex facilitates both production and nuclear
            translocation of the catalytic subunit of DNA polymerase alpha
  JOURNAL   Mol Cell Biol 18 (6), 3552-3562 (1998)
   PUBMED   9584195
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Lopez-Girona,A., Bachs,O. and Agell,N.
  TITLE     Calmodulin is involved in the induction of DNA polymerases alpha
            and delta activities in normal rat kidney cells activated to
            proliferate
  JOURNAL   Biochem Biophys Res Commun 217 (2), 566-574 (1995)
   PUBMED   7503737
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097300.1.
            
            On Jun 12, 2005 this sequence version replaced NP_445932.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097300.1, AJ245648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..600
                     /product="DNA polymerase alpha subunit B"
                     /EC_number="2.7.7.7"
                     /note="DNA-directed DNA polymerase alpha 2; DNA polymerase
                     subunit II; polymerase (DNA directed), alpha 2, accessory
                     subunit; DNA polymerase alpha 70 kDa subunit; DNA
                     polymerase alpha subunit II; polymerase (DNA) alpha 2,
                     accessory subunit"
                     /calculated_mol_wt=66554
     Region          21..238
                     /region_name="Pol_alpha_B_N"
                     /note="DNA polymerase alpha subunit B N-terminal;
                     pfam08418"
                     /db_xref="CDD:462470"
     Region          112..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89043.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14181; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14181; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14181; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14181; propagated from
                     UniProtKB/Swiss-Prot (O89043.2)"
     Region          <206..587
                     /region_name="POL12"
                     /note="DNA polymerase alpha-primase complex,
                     polymerase-associated subunit B [DNA replication,
                     recombination, and repair]; COG5214"
                     /db_xref="CDD:227539"
     CDS             1..600
                     /gene="Pola2"
                     /coded_by="NM_053480.2:132..1934"
                     /db_xref="GeneID:85242"
                     /db_xref="RGD:621817"
ORIGIN      
        1 mavstqqlae elqifgldce dslleklael ctlyrqteer mvseliafct sagkscltge
       61 ilssfehevl nkklskachs askdnrhaga rdivsiqeli eaeeeeetll sayttpskgp
      121 hkrvsstpet pltkrsistr sphqllspss fspsatpsqk yssrtnrgev vttfgsaqgv
      181 swsgrggsgs islkvmgype pltssyktmf qqlpdirevl tckieelgse lkehykieaf
      241 tpllvpaqep villgqigcd sngrlnsksv ilegdrehss gaqipvdmse lkdyslfpgq
      301 vvimegfntt grrltatkly egvplpfyqp teeegdfeqt mvlvacgpyt tsdsitydpl
      361 ldlistinhd rldvcilfgp fldakheqve nckltspfed ifkqclrtvi egtrssgshl
      421 vfvpslrdvh hepvypqppf tfselpredk krvqfvsepc nlsingvmfg ltstdllfhi
      481 gaeeicsssg tsdrfsrilk hiltqrsyyp lypphedmai dyenfytyaq lpvtpdvfiv
      541 pselryfvkd ifgcvcmnpg rltkgqvggt fgrlylrrqp kgtdsegrqg lsvaaqvvri
//
LOCUS       NP_598293                452 aa            linear   ROD 27-APR-2025
DEFINITION  translation initiation factor eIF2B subunit gamma [Rattus
            norvegicus].
ACCESSION   NP_598293
VERSION     NP_598293.2
DBSOURCE    REFSEQ: accession NM_133609.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Kashiwagi,K., Shigeta,T., Imataka,H., Ito,T. and Yokoyama,S.
  TITLE     Expression, purification, and crystallization of
            Schizosaccharomyces pombe eIF2B
  JOURNAL   J Struct Funct Genomics 17 (1), 33-38 (2016)
   PUBMED   27023709
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Hinnebusch,A.G. and Lorsch,J.R.
  TITLE     The mechanism of eukaryotic translation initiation: new insights
            and challenges
  JOURNAL   Cold Spring Harb Perspect Biol 4 (10), a011544 (2012)
   PUBMED   22815232
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Mikami,S., Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     An efficient mammalian cell-free translation system supplemented
            with translation factors
  JOURNAL   Protein Expr Purif 46 (2), 348-357 (2006)
   PUBMED   16289705
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Van Haren,K., van der Voorn,J.P., Peterson,D.R., van der Knaap,M.S.
            and Powers,J.M.
  TITLE     The life and death of oligodendrocytes in vanishing white matter
            disease
  JOURNAL   J Neuropathol Exp Neurol 63 (6), 618-630 (2004)
   PUBMED   15217090
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Li,W., Wang,X., Van Der Knaap,M.S. and Proud,C.G.
  TITLE     Mutations linked to leukoencephalopathy with vanishing white matter
            impair the function of the eukaryotic initiation factor 2B complex
            in diverse ways
  JOURNAL   Mol Cell Biol 24 (8), 3295-3306 (2004)
   PUBMED   15060152
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Fabian,J.R., Kimball,S.R., Heinzinger,N.K. and Jefferson,L.S.
  TITLE     Subunit assembly and guanine nucleotide exchange activity of
            eukaryotic initiation factor-2B expressed in Sf9 cells
  JOURNAL   J Biol Chem 272 (19), 12359-12365 (1997)
   PUBMED   9139680
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Price,N.T., Kimball,S.R., Jefferson,L.S. and Proud,C.G.
  TITLE     Cloning of cDNA for the gamma-subunit of mammalian translation
            initiation factor 2B, the guanine nucleotide-exchange factor for
            eukaryotic initiation factor 2
  JOURNAL   Biochem J 318 (Pt 2) (Pt 2), 631-636 (1996)
   PUBMED   8809057
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Gilligan,M., Welsh,G.I., Flynn,A., Bujalska,I., Diggle,T.A.,
            Denton,R.M., Proud,C.G. and Docherty,K.
  TITLE     Glucose stimulates the activity of the guanine nucleotide-exchange
            factor eIF-2B in isolated rat islets of Langerhans
  JOURNAL   J Biol Chem 271 (4), 2121-2125 (1996)
   PUBMED   8567668
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Karinch,A.M., Kimball,S.R., Vary,T.C. and Jefferson,L.S.
  TITLE     Regulation of eukaryotic initiation factor-2B activity in muscle of
            diabetic rats
  JOURNAL   Am J Physiol 264 (1 Pt 1), E101-E108 (1993)
   PUBMED   8430778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072507.1.
            
            On Jun 13, 2004 this sequence version replaced NP_598293.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072507.1, U38253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..452
                     /product="translation initiation factor eIF2B subunit
                     gamma"
                     /note="translation initiation factor eIF-2B subunit gamma;
                     eIF2B GDP-GTP exchange factor subunit gamma; eIF-2B
                     GDP-GTP exchange factor subunit gamma; eukaryotic
                     translation initiation factor 2B, subunit 3 (gamma, 58kD);
                     eukaryotic translation initiation factor 2B, subunit 3
                     gamma"
                     /calculated_mol_wt=50305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR50; propagated from
                     UniProtKB/Swiss-Prot (P70541.2)"
     Region          3..212
                     /region_name="eIF-2B_gamma_N"
                     /note="The N-terminal domain of gamma subunit of the
                     eIF-2B is a subfamily of glycosyltransferase 2; cd04198"
                     /db_xref="CDD:133041"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR50; propagated from
                     UniProtKB/Swiss-Prot (P70541.2)"
     Region          357..437
                     /region_name="LbH_eIF2B_gamma_C"
                     /note="eIF-2B gamma subunit, C-terminal Left-handed
                     parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic
                     translation initiator, a guanine nucleotide exchange
                     factor (GEF) composed of five different subunits (alpha,
                     beta, gamma, delta and epsilon). eIF2B is...; cd04652"
                     /db_xref="CDD:100057"
     CDS             1..452
                     /gene="Eif2b3"
                     /coded_by="NM_133609.2:109..1467"
                     /db_xref="GeneID:171145"
                     /db_xref="RGD:620821"
ORIGIN      
        1 mefqavvmav gggsrmtdlt ssipkpllpv gnkpliwypl nllervgfee vivvttkdvq
       61 kalcaefkmk lkpdivcipd eadmgtadsl rhiypklktd vlvlgcdlit dvalhevvdl
      121 fraydaslam lmrkgqeste pvpgqkgkkk tveqrdfigv dstgkrllfm aneadldeel
      181 vikgsilqkh prihfqtglv dahlyclkky vvdflmenks itsirselip ylvrkqfssa
      241 ssqqrqedke edlkkkepks ldiysfikkd ntltlapyda cwnafrrdkw edlsrsqvrc
      301 yvhimkeglc srvstlglym eanrqvpkll svlcpeesmi hpsaqiankh ligadsligs
      361 dtqvgekssi krsvigsscv irdrvtvtnc llmnsvtvee gssihgsvic nnavveagae
      421 irdcligsgq rieakakrmn evivgndqlm ei
//
LOCUS       NP_001104280             786 aa            linear   ROD 27-APR-2025
DEFINITION  myosin light chain kinase 3 [Rattus norvegicus].
ACCESSION   NP_001104280 XP_001064628 XP_214645
VERSION     NP_001104280.1
DBSOURCE    REFSEQ: accession NM_001110810.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Avila-Rodriguez,D., Solano Agama,C., Gonzalez-Pozos,S., Vicente
            Mendez-Mendez,J., Ortiz Plata,A., Arreola-Mendoza,L. and
            Mendoza-Garrido,M.E.
  TITLE     The shift in GH3 cell shape and cell motility is dependent on MLCK
            and ROCK
  JOURNAL   Exp Cell Res 354 (1), 1-17 (2017)
   PUBMED   28300565
  REMARK    GeneRIF: We found that a rounded shape with high cortical tension
            depends on MLCK and ROCK, whereas in cells with an elongated shape,
            MLCK is the primary protein responsible for cell spreading.
            Further, in cells with a slow and directionally persistent
            motility, MLCK predominates, while rapid and erratic movement is
            ROCK-dependent
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Eikemo,H., Moltzau,L.R., Hussain,R.I., Nguyen,C.H., Qvigstad,E.,
            Levy,F.O., Skomedal,T. and Osnes,J.B.
  TITLE     CaMKII in addition to MLCK contributes to phosphorylation of
            regulatory light chain in cardiomyocytes
  JOURNAL   Biochem Biophys Res Commun 471 (1), 219-225 (2016)
   PUBMED   26809094
  REMARK    GeneRIF: In conclusion, in addition to MLCK, CaMKII phosphorylates
            RLC in cardiomyocytes.
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Gao,L., Zheng,Y.J., Gu,S.S., Tan,J.L., Paul,C., Wang,Y.G. and
            Yang,H.T.
  TITLE     Degradation of cardiac myosin light chain kinase by matrix
            metalloproteinase-2 contributes to myocardial contractile
            dysfunction during ischemia/reperfusion
  JOURNAL   J Mol Cell Cardiol 77, 102-112 (2014)
   PUBMED   25451385
  REMARK    GeneRIF: Ischemia/reperfusion-activated MMP-2 leads to the
            degradation of cardiac MLCK.
REFERENCE   4  (residues 1 to 786)
  AUTHORS   Al-Sadi,R., Ye,D., Dokladny,K. and Ma,T.Y.
  TITLE     Mechanism of IL-1beta-induced increase in intestinal epithelial
            tight junction permeability
  JOURNAL   J Immunol 180 (8), 5653-5661 (2008)
   PUBMED   18390750
REFERENCE   5  (residues 1 to 786)
  AUTHORS   Chan,J.Y., Takeda,M., Briggs,L.E., Graham,M.L., Lu,J.T.,
            Horikoshi,N., Weinberg,E.O., Aoki,H., Sato,N., Chien,K.R. and
            Kasahara,H.
  TITLE     Identification of cardiac-specific myosin light chain kinase
  JOURNAL   Circ Res 102 (5), 571-580 (2008)
   PUBMED   18202317
REFERENCE   6  (residues 1 to 786)
  AUTHORS   Seguchi,O., Takashima,S., Yamazaki,S., Asakura,M., Asano,Y.,
            Shintani,Y., Wakeno,M., Minamino,T., Kondo,H., Furukawa,H.,
            Nakamaru,K., Naito,A., Takahashi,T., Ohtsuka,T., Kawakami,K.,
            Isomura,T., Kitamura,S., Tomoike,H., Mochizuki,N. and Kitakaze,M.
  TITLE     A cardiac myosin light chain kinase regulates sarcomere assembly in
            the vertebrate heart
  JOURNAL   J Clin Invest 117 (10), 2812-2824 (2007)
   PUBMED   17885681
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EU236721.1.
            
            On or before Nov 24, 2007 this sequence version replaced
            XP_001064628.1, XP_214645.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU236721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..786
                     /product="myosin light chain kinase 3"
                     /EC_number="2.7.11.18"
                     /function="phosphorylates MLC-2v"
                     /note="cardiac-MLCK; cardiac-MyBP-C-associated Ca/CaM
                     kinase; putative myosin light chain kinase 3"
                     /calculated_mol_wt=85380
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          233..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          279..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          333..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          477..737
                     /region_name="STKc_MLCK3"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Myosin Light Chain Kinase 3; cd14192"
                     /db_xref="CDD:271094"
     Site            order(488..492,494,496,509,511,540,556..557,559,563,565,
                     603,605,607..608,610,622..623,626,641..644)
                     /site_type="active"
                     /db_xref="CDD:271094"
     Site            order(488..492,494,496,509,511,540,556..557,559,563,
                     607..608,610,622..623)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271094"
     Site            order(492,563,565,603,605,607,626,641..644)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271094"
     Site            622..644
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271094"
     CDS             1..786
                     /gene="Mylk3"
                     /gene_synonym="MLCK; RGD1305801"
                     /coded_by="NM_001110810.1:238..2598"
                     /db_xref="GeneID:291926"
                     /db_xref="RGD:1305801"
ORIGIN      
        1 msgvseedpe glgpqglpal ggaclvtvdk klnvltekvd rllhfqedvt eklqcvcqgm
       61 dhleqglhrl easqelglag pgstspaaaq aawpevlelv ravrqegaqh garlealfkm
      121 vvavdraitl vgstiqnskv ddfilqgtvp wrkgsladgp eenkeqaeva gvkpkhvlnt
      181 gsvqaatsra lweesqkqdt pvgtveglpl iidtslkgad ltqagaslrq gvealdpgqe
      241 pppaeaesrl palasedtgt tlelsvaidr isevltslrm sqsagegtss skpdcsepgp
      301 qplgplttds dihsdeglpr isvrmremtt peelfetqgg spigsaeapg pgtvledqip
      361 kgarpfpplp krscnnggas aeeatgpgae pirgpslvtr dwrdepvgtt dlqqgrdpga
      421 vspepgkdha aqgpgrteag rrvssaaeaa ivvlddsaap papfehrvvs ikdtlistsy
      481 tvsqhevlgg grfgqvhrct erstglalaa kiikvknikd redvkneini mnqlshvnli
      541 qlydafeskn sftlimeyvd ggelfdritd ekyhlteldv vlftrqiceg vhylhqhyil
      601 hldlkpenil cvsqtghqik iidfglarry kpreklkvnf gtpeflapev vnyefvsfpt
      661 dmwsvgvity mllsglspfl getdaetmnf ivncswdfda dtfkglseea kdfvsrllvk
      721 ekscrmsatq clkhewlnhl iakasgsnvr lrsqlllqky maqrkwkkhf hvvtavnrlr
      781 kfptcp
//
LOCUS       NP_036848                494 aa            linear   ROD 27-APR-2025
DEFINITION  monocarboxylate transporter 1 [Rattus norvegicus].
ACCESSION   NP_036848
VERSION     NP_036848.1
DBSOURCE    REFSEQ: accession NM_012716.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Xu,L., Yang,M., Wei,A., Wei,Z., Qin,Y., Wang,K., Li,B., Chen,K.,
            Liu,C., Li,C. and Wang,T.
  TITLE     Aerobic exercise-induced HIF-1alpha upregulation in heart failure:
            exploring potential impacts on MCT1 and MPC1 regulation
  JOURNAL   Mol Med 30 (1), 83 (2024)
   PUBMED   38867145
  REMARK    GeneRIF: Aerobic exercise-induced HIF-1alpha upregulation in heart
            failure: exploring potential impacts on MCT1 and MPC1 regulation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Wu,X., Wang,Z., Li,H., Xie,X., Wu,J., Shen,H., Li,X., Wang,Z. and
            Chen,G.
  TITLE     Loss of monocarboxylate transporter 1 aggravates white matter
            injury after experimental subarachnoid hemorrhage in rats
  JOURNAL   Front Med 15 (6), 887-902 (2021)
   PUBMED   34874512
  REMARK    GeneRIF: Loss of monocarboxylate transporter 1 aggravates white
            matter injury after experimental subarachnoid hemorrhage in rats.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Kopnick,A.L., Geistlinger,K. and Beitz,E.
  TITLE     Cysteine 159 delineates a hinge region of the alternating access
            monocarboxylate transporter 1 and is targeted by cysteine-modifying
            inhibitors
  JOURNAL   FEBS J 288 (20), 6052-6062 (2021)
   PUBMED   33999492
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Ahmadi,A., Sheikholeslami-Vatani,D., Ghaeeni,S. and Baazm,M.
  TITLE     The effects of different training modalities on monocarboxylate
            transporters MCT1 and MCT4, hypoxia inducible factor-1alpha
            (HIF-1alpha), and PGC-1alpha gene expression in rat skeletal
            muscles
  JOURNAL   Mol Biol Rep 48 (3), 2153-2161 (2021)
   PUBMED   33625690
  REMARK    GeneRIF: The effects of different training modalities on
            monocarboxylate transporters MCT1 and MCT4, hypoxia inducible
            factor-1alpha (HIF-1alpha), and PGC-1alpha gene expression in rat
            skeletal muscles.
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Elizondo-Vega,R., Oyarce,K., Salgado,M., Barahona,M.J., Recabal,A.,
            Ordenes,P., Lopez,S., Pincheira,R., Luz-Crawford,P. and
            Garcia-Robles,M.A.
  TITLE     Inhibition of Hypothalamic MCT4 and MCT1-MCT4 Expressions Affects
            Food Intake and Alters Orexigenic and Anorexigenic Neuropeptide
            Expressions
  JOURNAL   Mol Neurobiol 57 (2), 896-909 (2020)
   PUBMED   31578706
  REMARK    GeneRIF: Inhibition of Hypothalamic MCT4 and MCT1-MCT4 Expressions
            Affects Food Intake and Alters Orexigenic and Anorexigenic
            Neuropeptide Expressions.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Orsenigo,M.N., Tosco,M., Bazzini,C., Laforenza,U. and Faelli,A.
  TITLE     A monocarboxylate transporter MCT1 is located at the basolateral
            pole of rat jejunum
  JOURNAL   Exp Physiol 84 (6), 1033-1042 (1999)
   PUBMED   10564700
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Broer,S., Schneider,H.P., Broer,A., Rahman,B., Hamprecht,B. and
            Deitmer,J.W.
  TITLE     Characterization of the monocarboxylate transporter 1 expressed in
            Xenopus laevis oocytes by changes in cytosolic pH
  JOURNAL   Biochem J 333 (Pt 1) (Pt 1), 167-174 (1998)
   PUBMED   9639576
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Broer,S., Rahman,B., Pellegri,G., Pellerin,L., Martin,J.L.,
            Verleysdonk,S., Hamprecht,B. and Magistretti,P.J.
  TITLE     Comparison of lactate transport in astroglial cells and
            monocarboxylate transporter 1 (MCT 1) expressing Xenopus laevis
            oocytes. Expression of two different monocarboxylate transporters
            in astroglial cells and neurons
  JOURNAL   J Biol Chem 272 (48), 30096-30102 (1997)
   PUBMED   9374487
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Takanaga,H., Tamai,I., Inaba,S., Sai,Y., Higashida,H., Yamamoto,H.
            and Tsuji,A.
  TITLE     cDNA cloning and functional characterization of rat intestinal
            monocarboxylate transporter
  JOURNAL   Biochem Biophys Res Commun 217 (1), 370-377 (1995)
   PUBMED   8526936
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Jackson,V.N., Price,N.T. and Halestrap,A.P.
  TITLE     cDNA cloning of MCT1, a monocarboxylate transporter from rat
            skeletal muscle
  JOURNAL   Biochim Biophys Acta 1238 (2), 193-196 (1995)
   PUBMED   7548134
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078877.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078877.1, D63834.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..494
                     /product="monocarboxylate transporter 1"
                     /note="solute carrier 16 (monocarboxylic acid
                     transporter), member 1; MCT 1; solute carrier family 16,
                     member 1 (monocarboxylic acid transporter 1); solute
                     carrier family 16 (monocarboxylic acid transporters),
                     member 1; solute carrier family 16 (monocarboxylate
                     transporter), member 1"
                     /calculated_mol_wt=53107
     Region          1..462
                     /region_name="2A0113"
                     /note="monocarboxylate transporter 1; TIGR00892"
                     /db_xref="CDD:273325"
     Site            23..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            56..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            110..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            147..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            175..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16396499,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            255..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            289..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            322..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            347..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            415..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Region          446..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53987.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P53985; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53985; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P53987.1)"
     CDS             1..494
                     /gene="Slc16a1"
                     /gene_synonym="MCT1; RATMCT1; RNMCT1"
                     /coded_by="NM_012716.2:192..1676"
                     /db_xref="GeneID:25027"
                     /db_xref="RGD:3690"
ORIGIN      
        1 mppaiggpvg ytppdggwgw avvvgafisi gfsyafpksi tvffkeieii fsattsevsw
       61 issimlavmy aggpissilv nkygsrpvmi aggclsgcgl iaasfcntvq elyfcigvig
      121 glglafnlnp altmigkyfy kkrplangla magspvflst laplnqaffg ifgwrgsfli
      181 lgglllnccv agslmrpigp qqgkveklks keslqeagks dantdliggs pkgeklsvfq
      241 tvnkfldlsl fthrgfllyl sgnvvmffgl ftplvflsny gkskhfssek safllsilaf
      301 vdmvarpsmg laantrwirp rvqyffaasv vangvchlla plsttyvgfc iyagvfgfaf
      361 gwlssvlfet lmdlvgpqrf ssavglvtiv eccpvllgpp llgrlndmyg dykytywacg
      421 viliiaglyl figmginyrl vakeqkaeek krdgkedets tdvdekpkkt mketqspapl
      481 qnssgdpaee espv
//
LOCUS       NP_001001800             230 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 141 [Rattus norvegicus].
ACCESSION   NP_001001800 XP_219002
VERSION     NP_001001800.1
DBSOURCE    REFSEQ: accession NM_001001800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Miyamoto,K., Uechi,A. and Saito,K.
  TITLE     The zinc finger domain of RING finger protein 141 reveals a unique
            RING fold
  JOURNAL   Protein Sci 26 (8), 1681-1686 (2017)
   PUBMED   28547869
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Lee,Y.I., Giovinazzo,D., Kang,H.C., Lee,Y., Jeong,J.S.,
            Doulias,P.T., Xie,Z., Hu,J., Ghasemi,M., Ischiropoulos,H., Qian,J.,
            Zhu,H., Blackshaw,S., Dawson,V.L. and Dawson,T.M.
  TITLE     Protein microarray characterization of the S-nitrosoproteome
  JOURNAL   Mol Cell Proteomics 13 (1), 63-72 (2014)
   PUBMED   24105792
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Qiu,W., Zhang,S., Xiao,C., Xu,W., Ma,Y., Liu,Y. and Wu,Q.
  TITLE     Molecular cloning and characterization of a mouse
            spermatogenesis-related ring finger gene znf230
  JOURNAL   Biochem Biophys Res Commun 306 (2), 347-353 (2003)
   PUBMED   12804569
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY621087.1.
            
            On Aug 30, 2004 this sequence version replaced XP_219002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY621087.1, FQ089272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..230
                     /product="RING finger protein 141"
                     /calculated_mol_wt=25340
     Region          153..192
                     /region_name="RING-HC_RNF141"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 141 (RNF141) and similar proteins; cd16545"
                     /db_xref="CDD:438207"
     CDS             1..230
                     /gene="Rnf141"
                     /coded_by="NM_001001800.1:114..806"
                     /db_xref="GeneID:308900"
                     /db_xref="RGD:1303154"
ORIGIN      
        1 mgqqisdqtq lvinklpekv akhvtlvres gsltyeeflg rvaelndvta kiaagqekhl
       61 lfevqpgsds safwkvvvrv vctkinkssg iveasrimnl yqfiqlykdi tsqaagvlaq
      121 sstseepdgn pssvtscqas lwmgrvkqlt deeeccicmd gradlilpca hsfcqkcidk
      181 wsdrhrncpi crlqmtgane swvvsdapte ddmanyilnm adeagqphrp
//
LOCUS       NP_835195                678 aa            linear   ROD 27-APR-2025
DEFINITION  inositol-trisphosphate 3-kinase C [Rattus norvegicus].
ACCESSION   NP_835195
VERSION     NP_835195.1
DBSOURCE    REFSEQ: accession NM_178094.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Zhu,L., Zheng,Y., Wu,T., He,J., Fang,X., Zhou,S., Wang,K. and
            Wang,N.
  TITLE     Immune-related genes STIM1, ITPKC and PELI1 polymorphisms are
            associated with risk of colorectal cancer
  JOURNAL   Eur J Cancer Prev 30 (5), 357-363 (2021)
   PUBMED   33470690
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Pouillon,V., Hascakova-Bartova,R., Pajak,B., Adam,E., Bex,F.,
            Dewaste,V., Van Lint,C., Leo,O., Erneux,C. and Schurmans,S.
  TITLE     Inositol 1,3,4,5-tetrakisphosphate is essential for T lymphocyte
            development
  JOURNAL   Nat Immunol 4 (11), 1136-1143 (2003)
   PUBMED   14517551
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Nalaskowski,M.M., Bertsch,U., Fanick,W., Stockebrand,M.C.,
            Schmale,H. and Mayr,G.W.
  TITLE     Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically
            specialized for basal cellular inositol trisphosphate
            phosphorylation and shuttles actively between nucleus and cytoplasm
  JOURNAL   J Biol Chem 278 (22), 19765-19776 (2003)
   PUBMED   12649294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ440782.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ440782.1, AY160770.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..678
                     /product="inositol-trisphosphate 3-kinase C"
                     /EC_number="2.7.1.127"
                     /function="involved in inositol phosphate metabolism"
                     /note="IP3K C; IP3 3-kinase C; insP 3-kinase C; inositol
                     1,4,5-trisphosphate 3-kinase C"
                     /calculated_mol_wt=74332
     Region          25..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TS72; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Region          201..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Region          318..326
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Region          329..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96DU7; propagated from
                     UniProtKB/Swiss-Prot (Q80ZG2.1)"
     Region          462..673
                     /region_name="IPK"
                     /note="Inositol polyphosphate kinase; pfam03770"
                     /db_xref="CDD:397715"
     Region          504..512
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80ZG2.1)"
     CDS             1..678
                     /gene="Itpkc"
                     /gene_synonym="IP3K-C"
                     /coded_by="NM_178094.3:109..2145"
                     /db_xref="GeneID:308451"
                     /db_xref="RGD:631336"
ORIGIN      
        1 mrrcpcrgsl seaeagalpa earmglealr ggrrrqpglq rpgpgaggpt grpegggpra
       61 wiegfslhse aertdfgpap cpdgpqaepc gdeheeceaa glgvasekps qnkeldgsnl
      121 qthpklsspl aememagswt dgfrtdlhrp dlqarpkras lctqpgfdes wteldrselw
      181 qtlperdkpw vdhlrthqdm srlqnhpacp spepsagtsc kelsadgsrt phdtdgfwie
      241 sqtdgsligp stqtacrqpa ndgfsaqdtd gtliqpgtdd gpwvdsvlek sngddplmep
      301 eprdlvtnlc shlecsslcp vprliitses pepgaqplgp qarieggtgg fssassfdes
      361 eddlvagggg tsdpedrsgs kpwkklktvl kyspfvvsfh khyypwvqls ghagnfqage
      421 dgrilkrfcq ceqrslellm gdplrpfvpt yygmvqrdgq afnqmedlla dfegpsimdc
      481 kmgsrtylee elvkarerpk prkdmyekmv avdpgaptpe ehaqgavtkp rymqwretls
      541 ststlgfrie gikkadgtcn tnfkktqale qvtkvledfv ngdvgilrky varledlrdt
      601 lenspffkth evvgssllfv hdhtglakvw midfgktval pdhqmlshrl pwaegnredg
      661 ylwgldnlic llqglaqs
//
LOCUS       NP_001037720             374 aa            linear   ROD 27-APR-2025
DEFINITION  4-hydroxybenzoate polyprenyltransferase, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_001037720 XP_001061021 XP_573556
VERSION     NP_001037720.1
DBSOURCE    REFSEQ: accession NM_001044255.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Desbats,M.A., Morbidoni,V., Silic-Benussi,M., Doimo,M.,
            Ciminale,V., Cassina,M., Sacconi,S., Hirano,M., Basso,G.,
            Pierrel,F., Navas,P., Salviati,L. and Trevisson,E.
  TITLE     The COQ2 genotype predicts the severity of coenzyme Q10 deficiency
  JOURNAL   Hum Mol Genet 25 (19), 4256-4265 (2016)
   PUBMED   27493029
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Sasaki,D., Kotoh,J., Watadani,R. and Matsumoto,K.
  TITLE     New animal models reveal that coenzyme Q2 (Coq2) and
            placenta-specific 8 (Plac8) are candidate genes for the onset of
            type 2 diabetes associated with obesity in rats
  JOURNAL   Mamm Genome 26 (11-12), 619-629 (2015)
   PUBMED   26296322
  REMARK    GeneRIF: coenzyme Q2 (Coq2) and placenta-specific 8 (Plac8) are
            differentially expressed in obese rats, suggesting that these two
            genes are candidates for the onset of type 2 diabetes associated
            with obesity in rats.
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Lopez-Martin,J.M., Salviati,L., Trevisson,E., Montini,G.,
            DiMauro,S., Quinzii,C., Hirano,M., Rodriguez-Hernandez,A.,
            Cordero,M.D., Sanchez-Alcazar,J.A., Santos-Ocana,C. and Navas,P.
  TITLE     Missense mutation of the COQ2 gene causes defects of bioenergetics
            and de novo pyrimidine synthesis
  JOURNAL   Hum Mol Genet 16 (9), 1091-1097 (2007)
   PUBMED   17374725
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Quinzii,C., Naini,A., Salviati,L., Trevisson,E., Navas,P.,
            Dimauro,S. and Hirano,M.
  TITLE     A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2)
            causes primary coenzyme Q10 deficiency
  JOURNAL   Am J Hum Genet 78 (2), 345-349 (2006)
   PUBMED   16400613
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Forsgren,M., Attersand,A., Lake,S., Grunler,J., Swiezewska,E.,
            Dallner,G. and Climent,I.
  TITLE     Isolation and functional expression of human COQ2, a gene encoding
            a polyprenyl transferase involved in the synthesis of CoQ
  JOURNAL   Biochem J 382 (Pt 2), 519-526 (2004)
   PUBMED   15153069
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099827.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_573556.2, XP_001061021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..374
                     /product="4-hydroxybenzoate polyprenyltransferase,
                     mitochondrial precursor"
                     /EC_number="2.5.1.39"
                     /note="para-hydroxybenzoate--polyprenyltransferase,
                     mitochondrial; 4-hydroxybenzoate polyprenyltransferase,
                     mitochondrial; coenzyme Q2 4-hydroxybenzoate
                     polyprenyltransferase; coenzyme Q2 homolog,
                     prenyltransferase; 4-HB polyprenyltransferase;
                     PHB:polyprenyltransferase"
                     /calculated_mol_wt=34118
     transit_peptide 1..63
                     /note="Mitochondrion.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03189; propagated from
                     UniProtKB/Swiss-Prot (Q499N4.1)"
                     /calculated_mol_wt=6306
     mat_peptide     64..374
                     /product="4-hydroxybenzoate polyprenyltransferase,
                     mitochondrial. /evidence=ECO:0000255|HAMAP-Rule:MF_03189.
                     /id=PRO_0000228625"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
                     /calculated_mol_wt=34118
     Region          68..353
                     /region_name="PT_UbiA"
                     /note="UbiA family of prenyltransferases (PTases);
                     cl00337"
                     /db_xref="CDD:469727"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            301..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     Site            333..353
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499N4.1)"
     CDS             1..374
                     /gene="Coq2"
                     /gene_synonym="PHB:PPT; RGD1306722"
                     /coded_by="NM_001044255.1:5..1129"
                     /db_xref="GeneID:498332"
                     /db_xref="RGD:1306722"
ORIGIN      
        1 mlrlggaglv rglrvvspaw lrgpgglpla larttgtsga rdrrapasgt qrgralslsa
       61 aavvnsaprp lqpylrlmrl dkpigtwlly lpctwsigla adpgcfpdwy mlslfgtgai
      121 lmrgagctin dmwdrdfdkk vertanrpia agdisafqsf vflgaqltla lgvllhlnyy
      181 siamgaasll lvvtyplmkr vtfwpqlalg ltfnwgallg wsavkgscdp avclplyfsg
      241 vmwtliydti yahqdkkdda liglkstall frentkqwls gfgvamvgal slvgassgqt
      301 lpyyaavaav gahlahqiyt vdihraedcw ekftsnrtvg lllflgivlg nlykdkpdet
      361 kgvdavgees erts
//
LOCUS       NP_001012008             556 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 18 [Rattus norvegicus].
ACCESSION   NP_001012008 XP_220609
VERSION     NP_001012008.1
DBSOURCE    REFSEQ: accession NM_001012008.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081874.1.
            
            On Feb 11, 2005 this sequence version replaced XP_220609.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081874.1, SRR8487231.75872.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..556
                     /product="zinc finger protein 18"
                     /note="zinc finger protein 535; zinc finger with KRAB and
                     SCAN domains 6"
                     /calculated_mol_wt=62816
     Region          37..144
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          169..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q642B9.1)"
     Region          229..278
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <428..521
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          473..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(478,480,482,484..485,488..489,492,506,508,512..513,
                     516..517,520,534,536,538,540..541,544..545,548)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          501..521
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          513..537
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          527..549
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..556
                     /gene="Zfp18"
                     /gene_synonym="Zfp535; Zkscan6; Znf18"
                     /coded_by="NM_001012008.1:29..1699"
                     /db_xref="GeneID:303226"
                     /db_xref="RGD:1305130"
ORIGIN      
        1 mpvnlgqalg llpflakaed atfsgsdviq qrelanpeta rqlfrqfryq vmsgpqetlr
       61 qlrklcfqwl rpevhtkeqi leilmleqfl tilpgeiqmw vrkqcpgsge eavtlveslk
      121 gdpqklwqwi siqvlgqeip fekensarcr gdkvepalea eptvevvpqd lplqntssap
      181 gellshgvke esdlepelal aasqlparpe erptrdqevg tallpslqee qwrhldstqk
      241 eqywdlmlet ygkmvsgvag isnskpdltn maeygeelvg lhlhsaekma rapckedrqe
      301 ndkenlnlen hrdqgcldvf dqapgeappq talsdffges ephhfggesv pealenlqge
      361 gtgahlfphe rgsgkqlgqh iqssssgels alwleekrea sqkgqarapm aqklptcrec
      421 gktfyrnsql vfhqrthtge tyfhcrickk aflrssdfvk hqrthtgekp ckcdycgkgf
      481 sdfsglrhhe kihtgekpyk cpiceksfiq rsnfnrhqrv htgekpykct hcgkrfswss
      541 sldkhqrshl gkkpcp
//
LOCUS       NP_446186                389 aa            linear   ROD 27-APR-2025
DEFINITION  neutrophil cytosolic factor 1 [Rattus norvegicus].
ACCESSION   NP_446186
VERSION     NP_446186.2
DBSOURCE    REFSEQ: accession NM_053734.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Cao,M., Mao,Z., Peng,M., Zhao,Q., Sun,X., Yan,J. and Yuan,W.
  TITLE     Extracellular cyclophilin A induces cardiac hypertrophy via the
            ERK/p47phox pathway
  JOURNAL   Mol Cell Endocrinol 518, 110990 (2020)
   PUBMED   32805334
  REMARK    GeneRIF: Extracellular cyclophilin A induces cardiac hypertrophy
            via the ERK/p47phox pathway.
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Li,Y.J., Zhao,W., Yu,X.J., Li,F.X., Liu,Z.T., Li,L. and Xu,S.Y.
  TITLE     Activation of p47phox as a Mechanism of Bupivacaine-Induced Burst
            Production of Reactive Oxygen Species and Neural Toxicity
  JOURNAL   Oxid Med Cell Longev 2017, 8539026 (2017)
   PUBMED   28751934
  REMARK    GeneRIF: enhancing p47phox membrane translocation is a major
            mechanism whereby bupivacaine induced neurotoxicity and that
            pretreatment with VAS2870 or local p47phox gene knockdown
            attenuated bupivacaine-induced neuronal cell injury.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Winiarska,K., Dzik,J.M., Labudda,M., Focht,D., Sierakowski,B.,
            Owczarek,A., Komorowski,L. and Bielecki,W.
  TITLE     Melatonin nephroprotective action in Zucker diabetic fatty rats
            involves its inhibitory effect on NADPH oxidase
  JOURNAL   J Pineal Res 60 (1), 109-117 (2016)
   PUBMED   26514550
  REMARK    GeneRIF: it is concluded that: (i) melatonin beneficial action
            against diabetic nephropathy involves attenuation of the excessive
            activity of Nox; and (ii) the mechanism of melatonin inhibitory
            effect on Nox is based on the mitigation of expression and membrane
            translocation of its regulatory subunits.
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Sharma,N.M., Rabeler,B., Zheng,H., Raichlin,E. and Patel,K.P.
  TITLE     Exercise Training Attenuates Upregulation of p47(phox) and
            p67(phox) in Hearts of Diabetic Rats
  JOURNAL   Oxid Med Cell Longev 2016, 5868913 (2016)
   PUBMED   26989452
  REMARK    GeneRIF: Exercise Training attenuates the increased expression of
            p47(phox) and p67(phox) in the hearts of diabetic rats which could
            be an underlying mechanism for improving intracardiac matrix and
            thus cardiac function and prevent cardiac remodeling in diabetic
            cardiomyopathy.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Lian,S., Xia,Y., Khoi,P.N., Ung,T.T., Yoon,H.J., Kim,N.H., Kim,K.K.
            and Jung,Y.D.
  TITLE     Cadmium induces matrix metalloproteinase-9 expression via
            ROS-dependent EGFR, NF-small ka, CyrillicB, and AP-1 pathways in
            human endothelial cells
  JOURNAL   Toxicology 338, 104-116 (2015)
   PUBMED   26514923
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Jackson,S.H., Gallin,J.I. and Holland,S.M.
  TITLE     The p47phox mouse knock-out model of chronic granulomatous disease
  JOURNAL   J Exp Med 182 (3), 751-758 (1995)
   PUBMED   7650482
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Volpp,B.D. and Lin,Y.
  TITLE     In vitro molecular reconstitution of the respiratory burst in B
            lymphoblasts from p47-phox-deficient chronic granulomatous disease
  JOURNAL   J Clin Invest 91 (1), 201-207 (1993)
   PUBMED   7678602
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Francke,U., Hsieh,C.L., Foellmer,B.E., Lomax,K.J., Malech,H.L. and
            Leto,T.L.
  TITLE     Genes for two autosomal recessive forms of chronic granulomatous
            disease assigned to 1q25 (NCF2) and 7q11.23 (NCF1)
  JOURNAL   Am J Hum Genet 47 (3), 483-492 (1990)
   PUBMED   2393022
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Volpp,B.D., Nauseef,W.M., Donelson,J.E., Moser,D.R. and Clark,R.A.
  TITLE     Cloning of the cDNA and functional expression of the 47-kilodalton
            cytosolic component of human neutrophil respiratory burst oxidase
  JOURNAL   Proc Natl Acad Sci U S A 86 (18), 7195-7199 (1989)
   PUBMED   2550933
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Dec;86(23):9563]
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Lomax,K.J., Leto,T.L., Nunoi,H., Gallin,J.I. and Malech,H.L.
  TITLE     Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in
            chronic granulomatous disease
  JOURNAL   Science 245 (4916), 409-412 (1989)
   PUBMED   2547247
  REMARK    Erratum:[Science 1989 Nov 24;246(4933):987]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061810.1.
            
            On Dec 20, 2003 this sequence version replaced NP_446186.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061810.1, AF547392.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..389
                     /product="neutrophil cytosolic factor 1"
                     /note="phagocyte oxidase 47 kDa; neutrophil cytosol factor
                     1; neutrophil cytosol factor 1-like"
                     /calculated_mol_wt=44549
     Region          6..123
                     /region_name="PX_p47phox"
                     /note="The phosphoinositide binding Phox Homology domain
                     of the p47phox subunit of NADPH oxidase; cd06887"
                     /db_xref="CDD:132797"
     Site            order(43..45,77..78,90)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132797"
     Site            order(51,55,70,74..75)
                     /site_type="other"
                     /note="anionic phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:132797"
     Region          160..212
                     /region_name="SH3_p47phox_1"
                     /note="First or N-terminal Src homology 3 domain of the
                     p47phox subunit of NADPH oxidase, also called Neutrophil
                     Cytosolic Factor 1; cd12021"
                     /db_xref="CDD:212954"
     Site            order(165,167,173..174,191..193,204,206,208..209)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212954"
     Region          230..282
                     /region_name="SH3_p47phox_2"
                     /note="Second or C-terminal Src homology 3 domain of the
                     p47phox subunit of NADPH oxidase, also called Neutrophil
                     Cytosolic Factor 1; cd12022"
                     /db_xref="CDD:212955"
     Site            order(241,243..244,261..263,274,276,278..279)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212955"
     Region          282..331
                     /region_name="NECFESHC"
                     /note="SH3 terminal domain of 2nd SH3 on Neutrophil
                     cytosol factor 1; pfam16621"
                     /db_xref="CDD:465204"
     Region          292..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M707.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14598; propagated from
                     UniProtKB/Swiss-Prot (F1M707.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1M707.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14598; propagated from
                     UniProtKB/Swiss-Prot (F1M707.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14598; propagated from
                     UniProtKB/Swiss-Prot (F1M707.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14598; propagated from
                     UniProtKB/Swiss-Prot (F1M707.2)"
     Region          358..389
                     /region_name="p47_phox_C"
                     /note="NADPH oxidase subunit p47Phox, C terminal domain;
                     pfam08944"
                     /db_xref="CDD:430336"
     CDS             1..389
                     /gene="Ncf1"
                     /gene_synonym="Ncf-1; p47phox"
                     /coded_by="NM_053734.2:15..1184"
                     /db_xref="GeneID:114553"
                     /db_xref="RGD:61307"
ORIGIN      
        1 mgdtfirhia llgfekrfvp sqhyvymflv kwqdlsekvv yrkfteiyef hkmlkemfpi
       61 eageihtenr viphlpaprw ydgqraaesr qgtlteyfns lmglpvkisr cphllnffkv
      121 rpddlklpnd sqvkkpetyl takdgknnva ditgpiilqt yraiadyekg sktemtvatg
      181 dvvdvvekse sgwwfcqmkt krgwvpasyl epldspdeae dpdpnyagep yvtikayaav
      241 eedevslseg eaievihkll dgwwvvrkgd itgyfpsmyl qkageeitqa qrqirsrgap
      301 prrstirnaq sihqrsrkrl sqdtyrrnsv rflqqrrrpa rpgpqspdsk dnpstprakp
      361 qpavpprpss dlilhrctes tkrkltsav
//
LOCUS       NP_542144                608 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear protein localization protein 4 homolog [Rattus norvegicus].
ACCESSION   NP_542144
VERSION     NP_542144.1
DBSOURCE    REFSEQ: accession NM_080577.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Hao,Q., Jiao,S., Shi,Z., Li,C., Meng,X., Zhang,Z., Wang,Y.,
            Song,X., Wang,W., Zhang,R., Zhao,Y., Wong,C.C. and Zhou,Z.
  TITLE     A non-canonical role of the p97 complex in RIG-I antiviral
            signaling
  JOURNAL   EMBO J 34 (23), 2903-2920 (2015)
   PUBMED   26471729
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Zhong,Y., Shen,H., Wang,Y., Yang,Y., Yang,P. and Fang,S.
  TITLE     Identification of ERAD components essential for dislocation of the
            null Hong Kong variant of alpha-1-antitrypsin (NHK)
  JOURNAL   Biochem Biophys Res Commun 458 (2), 424-428 (2015)
   PUBMED   25660456
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Bebeacua,C., Forster,A., McKeown,C., Meyer,H.H., Zhang,X. and
            Freemont,P.S.
  TITLE     Distinct conformations of the protein complex p97-Ufd1-Npl4
            revealed by electron cryomicroscopy
  JOURNAL   Proc Natl Acad Sci U S A 109 (4), 1098-1103 (2012)
   PUBMED   22232657
REFERENCE   4  (residues 1 to 608)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Alexandru,G., Graumann,J., Smith,G.T., Kolawa,N.J., Fang,R. and
            Deshaies,R.J.
  TITLE     UBXD7 binds multiple ubiquitin ligases and implicates p97 in
            HIF1alpha turnover
  JOURNAL   Cell 134 (5), 804-816 (2008)
   PUBMED   18775313
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Meyer,H.H., Wang,Y. and Warren,G.
  TITLE     Direct binding of ubiquitin conjugates by the mammalian p97 adaptor
            complexes, p47 and Ufd1-Npl4
  JOURNAL   EMBO J 21 (21), 5645-5652 (2002)
   PUBMED   12411482
REFERENCE   7  (residues 1 to 608)
  AUTHORS   Ye,Y., Meyer,H.H. and Rapoport,T.A.
  TITLE     The AAA ATPase Cdc48/p97 and its partners transport proteins from
            the ER into the cytosol
  JOURNAL   Nature 414 (6864), 652-656 (2001)
   PUBMED   11740563
REFERENCE   8  (residues 1 to 608)
  AUTHORS   Hetzer,M., Meyer,H.H., Walther,T.C., Bilbao-Cortes,D., Warren,G.
            and Mattaj,I.W.
  TITLE     Distinct AAA-ATPase p97 complexes function in discrete steps of
            nuclear assembly
  JOURNAL   Nat Cell Biol 3 (12), 1086-1091 (2001)
   PUBMED   11781570
REFERENCE   9  (residues 1 to 608)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   10 (residues 1 to 608)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC101887.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101887.1, AF234600.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..608
                     /product="nuclear protein localization protein 4 homolog"
                     /note="homolog of yeast nuclear protein localization 4;
                     nuclear protein localization 4 homolog"
                     /calculated_mol_wt=67925
     Region          1..80
                     /region_name="UN_NPL4"
                     /note="Nuclear pore localization protein NPL4; pfam11543"
                     /db_xref="CDD:431926"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8TAT6; propagated from
                     UniProtKB/Swiss-Prot (Q9ES54.3)"
     Region          105..245
                     /region_name="zf-NPL4"
                     /note="NPL4 family, putative zinc binding region;
                     pfam05020"
                     /db_xref="CDD:461523"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60670; propagated from
                     UniProtKB/Swiss-Prot (Q9ES54.3)"
     Region          249..555
                     /region_name="NPL4"
                     /note="NPL4 family; pfam05021"
                     /db_xref="CDD:461524"
     Region          584..606
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          584..603
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     CDS             1..608
                     /gene="Nploc4"
                     /gene_synonym="Npl4"
                     /coded_by="NM_080577.2:154..1980"
                     /db_xref="GeneID:140639"
                     /db_xref="RGD:620794"
ORIGIN      
        1 maesiiirvq spdgvkrita tkretaatfl kkvakefgfq nngfsvyinr nktgeitass
       61 skslhllkik hgdllflfps slagpsseme tstsvglkaf gaphvvedei dqylskqdgk
      121 iyrsrdpqlc rhgplgkcvh cvplepfded ylnhleppvk hmsfhayirk ltggadkgkf
      181 valeniscki ksgceghlpw pngictkcqp saitlnrqky rhvdnimfen htvadrfldf
      241 wrktgnqhfg ylygrytehk diplgiraev aaiyeppqig tqnslelled pkaevvdeia
      301 sklglrkvgw iftdlvsedt rkgtvrysrn kdtyflssee citagdfqnk hpnicrlspd
      361 ghfgskfvta vatggpdnqv hfegyqvsnq cmalvrdecl lpckdapelg yakessseqy
      421 vpdvfykdid kfgneitqla rplpveylii ditttfpkdp vytfsisqnp fpienrdvlg
      481 etqdfhslat ylsqntssvf ldtisdfhll lflvtnevmp lqdsisllle avrtrneela
      541 qtwkkseqwa tieqlcstvg vqlpglhefg avggsaraat samwacqhct fmnqpgtghc
      601 emcslprt
//
LOCUS       NP_001004222             341 aa            linear   ROD 27-APR-2025
DEFINITION  arfaptin-2 [Rattus norvegicus].
ACCESSION   NP_001004222 XP_215031
VERSION     NP_001004222.1
DBSOURCE    REFSEQ: accession NM_001004222.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Herlo,R., Lund,V.K., Lycas,M.D., Jansen,A.M., Khelashvili,G.,
            Andersen,R.C., Bhatia,V., Pedersen,T.S., Albornoz,P.B.C.,
            Johner,N., Ammendrup-Johnsen,I., Christensen,N.R., Erlendsson,S.,
            Stoklund,M., Larsen,J.B., Weinstein,H., Kjaerulff,O., Stamou,D.,
            Gether,U. and Madsen,K.L.
  TITLE     An Amphipathic Helix Directs Cellular Membrane Curvature Sensing
            and Function of the BAR Domain Protein PICK1
  JOURNAL   Cell Rep 23 (7), 2056-2069 (2018)
   PUBMED   29768204
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Cruz-Garcia,D., Ortega-Bellido,M., Scarpa,M., Villeneuve,J.,
            Jovic,M., Porzner,M., Balla,T., Seufferlein,T. and Malhotra,V.
  TITLE     Recruitment of arfaptins to the trans-Golgi network by PI(4)P and
            their involvement in cargo export
  JOURNAL   EMBO J 32 (12), 1717-1729 (2013)
   PUBMED   23695357
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Rangone,H., Pardo,R., Colin,E., Girault,J.A., Saudou,F. and
            Humbert,S.
  TITLE     Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits
            PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment
  JOURNAL   J Biol Chem 280 (23), 22021-22028 (2005)
   PUBMED   15809304
  REMARK    GeneRIF: arfaptin 2 phosphorylation at Ser260 by Akt inhibits
            PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Peters,P.J., Ning,K., Palacios,F., Boshans,R.L., Kazantsev,A.,
            Thompson,L.M., Woodman,B., Bates,G.P. and D'Souza-Schorey,C.
  TITLE     Arfaptin 2 regulates the aggregation of mutant huntingtin protein
  JOURNAL   Nat Cell Biol 4 (3), 240-245 (2002)
   PUBMED   11854752
REFERENCE   7  (residues 1 to 341)
  AUTHORS   D'Souza-Schorey,C., Boshans,R.L., McDonough,M., Stahl,P.D. and Van
            Aelst,L.
  TITLE     A role for POR1, a Rac1-interacting protein, in ARF6-mediated
            cytoskeletal rearrangements
  JOURNAL   EMBO J 16 (17), 5445-5454 (1997)
   PUBMED   9312003
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Van Aelst,L., Joneson,T. and Bar-Sagi,D.
  TITLE     Identification of a novel Rac1-interacting protein involved in
            membrane ruffling
  JOURNAL   EMBO J 15 (15), 3778-3786 (1996)
   PUBMED   8670882
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079174.1.
            
            On Sep 10, 2004 this sequence version replaced XP_215031.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079174.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..341
                     /product="arfaptin-2"
                     /note="ADP-ribosylation factor interacting protein 2
                     (arfaptin 2); partner of Rac1; ADP-ribosylation
                     factor-interacting protein 2"
                     /calculated_mol_wt=37642
     Region          46..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY65.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53365; propagated from
                     UniProtKB/Swiss-Prot (Q6AY65.1)"
     Region          136..323
                     /region_name="BAR_Arfaptin"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin;
                     cd07660"
                     /db_xref="CDD:153344"
     Site            order(139..140,146,150,153,156..157,160,163..164,168,
                     170..171,174,177..178,181..182,184..185,188,192,290,
                     294..295,298..299,301..302,309..310,312..313)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153344"
     Site            order(145,148,151..152,155..156,158..160,162..163,197,200,
                     204,207..208)
                     /site_type="other"
                     /note="Rac binding site [polypeptide binding]"
                     /db_xref="CDD:153344"
     CDS             1..341
                     /gene="Arfip2"
                     /gene_synonym="POR"
                     /coded_by="NM_001004222.1:139..1164"
                     /db_xref="GeneID:293344"
                     /db_xref="RGD:1303204"
ORIGIN      
        1 mtdgilgkaa tmeipihgng eagqlpeddg leqdlqqvmv sgpnlnetsi vsggyggsgd
       61 gliptgsgrh pshstspsgp gdevargiag ekfdivkkwg intykctkql lserfgrgsr
      121 tvdlelelqi ellretkrky esvlqlgral tahlysllqt qhalgdafad lsqkspelqe
      181 efgynaetqk llckngetll gavnffvssi ntlvtktmed tlmtvkqyea arleydayrt
      241 dleelslgpr dagtrgrles aqatfqthrd kyeklrgdva iklkfleenk ikvmhkqlll
      301 fhnavsayfa gnqkqleqtl qqfniklrpp gaekpswlee q
//
LOCUS       NP_001014187             398 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis associated 6-like protein [Rattus norvegicus].
ACCESSION   NP_001014187 XP_342042
VERSION     NP_001014187.1
DBSOURCE    REFSEQ: accession NM_001014165.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079024.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342042.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..398
                     /product="spermatogenesis associated 6-like protein"
                     /note="uncharacterized protein C9orf68 homolog"
                     /calculated_mol_wt=45977
     Region          7..145
                     /region_name="SPATA6"
                     /note="Spermatogenesis-assoc protein 6; pfam14909"
                     /db_xref="CDD:464365"
     Region          170..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYJ3.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYJ3.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYJ3.1)"
     CDS             1..398
                     /gene="Spata6l"
                     /gene_synonym="RGD1310039"
                     /coded_by="NM_001014165.1:123..1319"
                     /db_xref="GeneID:361747"
                     /db_xref="RGD:1310039"
ORIGIN      
        1 mplevvvelq iraiscpgvf lpdkevvylg vyllnqylet dcfpsvfpiv iqqsmrfekv
       61 feeamdpgav aellesfltr felvqlvspa weelayyekn trdflfpepk ltsshlgmqr
      121 evlmktaiwf pgiapklefs trtailecvf pcknrflwee rcklqqsfsk lngpannrkk
      181 kpkeknsdql skgtpfwgps pqrlhlhrpt qrnpgksfrf lgerkppfvv rhvdsgnpfg
      241 ennlehhsqk srrkpkfinf dlakkrafsl dsleanikvv repderivlr sqsppplnsg
      301 hfrkpllnhq gdvdfhpett vttsqlsspp spldhsllqe rfqpcsasmw qkiqeracsl
      361 ltpnrahpke dsisetnsih erpsyllrkh llrehryf
//
LOCUS       NP_446359                310 aa            linear   ROD 27-APR-2025
DEFINITION  deoxyribonuclease gamma precursor [Rattus norvegicus].
ACCESSION   NP_446359 XP_003751494
VERSION     NP_446359.1
DBSOURCE    REFSEQ: accession NM_053907.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Jimenez-Alcazar,M., Rangaswamy,C., Panda,R., Bitterling,J.,
            Simsek,Y.J., Long,A.T., Bilyy,R., Krenn,V., Renne,C., Renne,T.,
            Kluge,S., Panzer,U., Mizuta,R., Mannherz,H.G., Kitamura,D.,
            Herrmann,M., Napirei,M. and Fuchs,T.A.
  TITLE     Host DNases prevent vascular occlusion by neutrophil extracellular
            traps
  JOURNAL   Science 358 (6367), 1202-1206 (2017)
   PUBMED   29191910
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Errami,Y., Naura,A.S., Kim,H., Ju,J., Suzuki,Y., El-Bahrawy,A.H.,
            Ghonim,M.A., Hemeida,R.A., Mansy,M.S., Zhang,J., Xu,M.,
            Smulson,M.E., Brim,H. and Boulares,A.H.
  TITLE     Apoptotic DNA fragmentation may be a cooperative activity between
            caspase-activated deoxyribonuclease and the poly(ADP-ribose)
            polymerase-regulated DNAS1L3, an endoplasmic reticulum-localized
            endonuclease that translocates to the nucleus during apoptosis
  JOURNAL   J Biol Chem 288 (5), 3460-3468 (2013)
   PUBMED   23229555
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Shiokawa,D. and Tanuma,S.
  TITLE     Differential DNases are selectively used in neuronal apoptosis
            depending on the differentiation state
  JOURNAL   Cell Death Differ 11 (10), 1112-1120 (2004)
   PUBMED   15167901
  REMARK    GeneRIF: DNase gamma is suggested to be involved in naturally
            occurring apoptosis in developing nervous systems
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Higami,Y., Tsuchiya,T., To,K., Chiba,T., Yamaza,H., Shiokawa,D.,
            Tanuma,S. and Shimokawa,I.
  TITLE     Expression of DNase gamma during Fas-independent apoptotic DNA
            fragmentation in rodent hepatocytes
  JOURNAL   Cell Tissue Res 316 (3), 403-407 (2004)
   PUBMED   15118903
  REMARK    GeneRIF: DNase gamma plays an important role in Fas-independent
            apoptotic DNA fragmentation in hepatocytes.
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Shiokawa,D., Kobayashi,T. and Tanuma,S.
  TITLE     Involvement of DNase gamma in apoptosis associated with myogenic
            differentiation of C2C12 cells
  JOURNAL   J Biol Chem 277 (34), 31031-31037 (2002)
   PUBMED   12050166
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Liu,Q.Y., Pandey,S., Singh,R.K., Lin,W., Ribecco,M.,
            Borowy-Borowski,H., Smith,B., LeBlanc,J., Walker,P.R. and
            Sikorska,M.
  TITLE     DNaseY: a rat DNaseI-like gene coding for a constitutively
            expressed chromatin-bound endonuclease
  JOURNAL   Biochemistry 37 (28), 10134-10143 (1998)
   PUBMED   9665719
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Shiokawa,D. and Tanuma,S.
  TITLE     Molecular cloning and expression of a cDNA encoding an apoptotic
            endonuclease DNase gamma
  JOURNAL   Biochem J 332 (Pt 3) (Pt 3), 713-720 (1998)
   PUBMED   9620874
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Shiokawa,D., Iwamatsu,A. and Tanuma,S.
  TITLE     Purification, characterization, and amino acid sequencing of DNase
            gamma from rat spleen
  JOURNAL   Arch Biochem Biophys 346 (1), 15-20 (1997)
   PUBMED   9328279
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Shiokawa,D., Ohyama,H., Yamada,T. and Tanuma,S.
  TITLE     Purification and properties of DNase gamma from apoptotic rat
            thymocytes
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 675-681 (1997)
   PUBMED   9307016
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Shiokawa,D., Ohyama,H., Yamada,T., Takahashi,K. and Tanuma,S.
  TITLE     Identification of an endonuclease responsible for apoptosis in rat
            thymocytes
  JOURNAL   Eur J Biochem 226 (1), 23-30 (1994)
   PUBMED   7957253
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U75689.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003751494.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ231976.1, FQ230990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..310
                     /product="deoxyribonuclease gamma precursor"
                     /function="apoptosis"
                     /note="deoxyribonuclease gamma; DNaseY; DNase I-like 3;
                     DNase gamma; deoxyribonuclease I-like 3; deoxyribonuclease
                     gamma-like; deoxyribonuclease 1-like 3"
                     /calculated_mol_wt=33064
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2662
     Region          9..287
                     /region_name="DNaseIc"
                     /note="deoxyribonuclease I; smart00476"
                     /db_xref="CDD:128752"
     mat_peptide     26..310
                     /product="Deoxyribonuclease gamma. /id=PRO_0000007290"
                     /note="propagated from UniProtKB/Swiss-Prot (O89107.1)"
                     /calculated_mol_wt=33064
     Site            order(32..33,35,39,64,66..68,102..103,105,137,160,163,194,
                     196,201,234,238..239,278..279)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197337"
     Site            order(32,64,105,160,194,196,239,278..279)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197337"
     Site            order(32,64,278)
                     /site_type="other"
                     /note="putative Mg binding site IVb [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(34,160,194,196,279)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197337"
     Site            34
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:197337"
     Site            order(35,39,66..68,102..103,105,137,160,163,194,196,201,
                     238,279)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197337"
     Region          40..56
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O89107.1)"
     Site            order(126,138)
                     /site_type="other"
                     /note="Ca binding site II [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(194,239,279)
                     /site_type="other"
                     /note="putative Mg binding site IVa [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(198,224)
                     /site_type="metal-binding"
                     /note="metal binding site III [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(227,229)
                     /site_type="other"
                     /note="Ca binding site I [ion binding]"
                     /db_xref="CDD:197337"
     Region          289..310
                     /region_name="Not required for free DNA-nuclease activity
                     but required for activity towards liposome-coated DNA.
                     /evidence=ECO:0000250|UniProtKB:O55070"
                     /note="propagated from UniProtKB/Swiss-Prot (O89107.1)"
     Region          301..307
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O89107.1)"
     CDS             1..310
                     /gene="Dnase1l3"
                     /coded_by="NM_053907.1:203..1135"
                     /db_xref="GeneID:116687"
                     /db_xref="RGD:620669"
ORIGIN      
        1 mslypaspyl aslllfilal hgalslrlcs fnvrsfgesk kenhnamdii vkiikrcdli
       61 llmeikdsnn nicpmlmekl ngnsrrstty nyvissrlgr ntykeqyafl ykeklvsvka
      121 kylyhdyqdg dtdvfsrepf vvwfqapfta akdfvivplh ttpetsvkei deladvytdv
      181 rrrwkaenfi fmgdfnagcs yvpkkawkni rlrtdpnfvw ligdqedttv kkstscaydr
      241 ivlrgqeivn svvprssgvf dfqkayelse eealdvsdhf pvefklqssr aftnsrksvs
      301 lkkkkkgsrs
//
LOCUS       NP_001009672             101 aa            linear   ROD 27-APR-2025
DEFINITION  small ubiquitin-related modifier 1 [Rattus norvegicus].
ACCESSION   NP_001009672 XP_217413
VERSION     NP_001009672.1
DBSOURCE    REFSEQ: accession NM_001009672.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Wang,L., Wang,P., Xu,S., Li,Z., Duan,D.D., Ye,J., Li,J., Ding,Y.,
            Zhang,W., Lu,J. and Liu,P.
  TITLE     The cross-talk between PARylation and SUMOylation in C/EBPbeta at
            K134 site participates in pathological cardiac hypertrophy
  JOURNAL   Int J Biol Sci 18 (2), 783-799 (2022)
   PUBMED   35002525
  REMARK    GeneRIF: The cross-talk between PARylation and SUMOylation in
            C/EBPbeta at K134 site participates in pathological cardiac
            hypertrophy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Du,C.P., Wang,M., Geng,C., Hu,B., Meng,L., Xu,Y., Cheng,B.,
            Wang,N., Zhu,Q.J. and Hou,X.Y.
  TITLE     Activity-Induced SUMOylation of Neuronal Nitric Oxide Synthase Is
            Associated with Plasticity of Synaptic Transmission and
            Extracellular Signal-Regulated Kinase 1/2 Signaling
  JOURNAL   Antioxid Redox Signal 32 (1), 18-34 (2020)
   PUBMED   31642335
  REMARK    GeneRIF: Activity-Induced SUMOylation of Neuronal Nitric Oxide
            Synthase Is Associated with Plasticity of Synaptic Transmission and
            Extracellular Signal-Regulated Kinase 1/2 Signaling.
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Chen,Y.D., Liu,J.Y., Lu,Y.M., Zhu,H.T., Tang,W., Wang,Q.X. and
            Lu,H.Y.
  TITLE     Functional roles of C/EBPalpha and SUMO-modification in lung
            development
  JOURNAL   Int J Mol Med 40 (4), 1037-1046 (2017)
   PUBMED   28902364
  REMARK    GeneRIF: C/EBPalpha played a role in lung development and provided
            the insight into the mechanism underlying SUMO-modification.
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Cuomo,O., Pignataro,G., Sirabella,R., Molinaro,P., Anzilotti,S.,
            Scorziello,A., Sisalli,M.J., Di Renzo,G. and Annunziato,L.
  TITLE     Sumoylation of LYS590 of NCX3 f-Loop by SUMO1 Participates in Brain
            Neuroprotection Induced by Ischemic Preconditioning
  JOURNAL   Stroke 47 (4), 1085-1093 (2016)
   PUBMED   26979866
  REMARK    GeneRIF: SUMO1 knockdown worsened ischemic damage and reduced the
            protective effect of preconditioning. NCX3 sumoylation participates
            in SUMO1 protective role during ischemic preconditioning.
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Jiang,Y., Wang,J., Tian,H., Li,G., Zhu,H., Liu,L., Hu,R. and Dai,A.
  TITLE     Increased SUMO-1 expression in response to hypoxia: Interaction
            with HIF-1alpha in hypoxic pulmonary hypertension
  JOURNAL   Int J Mol Med 36 (1), 271-281 (2015)
   PUBMED   25976847
  REMARK    GeneRIF: SUMO1 may participate in the modulation of HIF1alpha
            through sumoylation in hypoxic pulmonary hypertension.
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Eloranta,J.J. and Hurst,H.C.
  TITLE     Transcription factor AP-2 interacts with the SUMO-conjugating
            enzyme UBC9 and is sumolated in vivo
  JOURNAL   J Biol Chem 277 (34), 30798-30804 (2002)
   PUBMED   12072434
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Hardeland,U., Steinacher,R., Jiricny,J. and Schar,P.
  TITLE     Modification of the human thymine-DNA glycosylase by ubiquitin-like
            proteins facilitates enzymatic turnover
  JOURNAL   EMBO J 21 (6), 1456-1464 (2002)
   PUBMED   11889051
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Hong,Y., Rogers,R., Matunis,M.J., Mayhew,C.N., Goodson,M.L.,
            Park-Sarge,O.K. and Sarge,K.D.
  TITLE     Regulation of heat shock transcription factor 1 by stress-induced
            SUMO-1 modification
  JOURNAL   J Biol Chem 276 (43), 40263-40267 (2001)
   PUBMED   11514557
  REMARK    Erratum:[J Biol Chem 2002 Jul 19;277(29):26708. Goodson M
            [corrected to Goodson ML]]
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Duprez,E., Saurin,A.J., Desterro,J.M., Lallemand-Breitenbach,V.,
            Howe,K., Boddy,M.N., Solomon,E., de The,H., Hay,R.T. and
            Freemont,P.S.
  TITLE     SUMO-1 modification of the acute promyelocytic leukaemia protein
            PML: implications for nuclear localisation
  JOURNAL   J Cell Sci 112 (Pt 3), 381-393 (1999)
   PUBMED   9885291
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Sternsdorf,T., Jensen,K. and Will,H.
  TITLE     Evidence for covalent modification of the nuclear dot-associated
            proteins PML and Sp100 by PIC1/SUMO-1
  JOURNAL   J Cell Biol 139 (7), 1621-1634 (1997)
   PUBMED   9412458
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088322.1.
            
            On Jan 13, 2005 this sequence version replaced XP_217413.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088322.1, FQ215643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMD00132302
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..101
                     /product="small ubiquitin-related modifier 1"
                     /note="SUMO-1; ubiquitin-like 1 (sentrin); SMT3 suppressor
                     of mif two 3 homolog 1"
                     /calculated_mol_wt=11426
     mat_peptide     2..97
                     /product="Small ubiquitin-related modifier 1.
                     /id=PRO_0000267610"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0H3.1)"
                     /calculated_mol_wt=11001
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P63165; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H3.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H3.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63165; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H3.1)"
     Region          21..96
                     /region_name="Ubl_SUMO1"
                     /note="ubiquitin-like (Ubl) domain found in small
                     ubiquitin-related modifier 1 (SUMO-1) and similar
                     proteins; cd16114"
                     /db_xref="CDD:340531"
     Site            order(21,23,27,29,31,33,35..39,41..43,46..47,50,54,60..61,
                     63,65,68,70,89,91..96)
                     /site_type="other"
                     /note="SUMO1-SAE2-SAE1 complex [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(21,23,32..38,42..43,46..47,50,54..55)
                     /site_type="other"
                     /note="peptide binding site 1 [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(21,26,32,34..39,41..43,46..47,50..51,53..55)
                     /site_type="other"
                     /note="peptide binding site 2 [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(21,23,33..37,42,46..47,50,54)
                     /site_type="other"
                     /note="SUMO1-Ysmb-9 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340531"
     Site            order(25,27..29,66..67,81..83,85..87,89..91)
                     /site_type="other"
                     /note="SUMO1-UBC9 interaction site [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(29..39,42,46,50,54,61,63,92,94..96)
                     /site_type="other"
                     /note="SUMO1-E2I-RanBP2 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340531"
     Site            order(29..31,58,60..61,63,67..70,89,91..96)
                     /site_type="other"
                     /note="SUMO1-SAE2-SAE1-ATP-Mg complex [polypeptide
                     binding]"
                     /db_xref="CDD:340531"
     Site            order(29,60,63,65,67..68,70,75,79,89,91..96)
                     /site_type="other"
                     /note="SUMO1-SENP1-Rangap complex [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63165; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H3.1)"
     Site            36
                     /site_type="other"
                     /note="Interaction with PIAS2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q5I0H3.1)"
     Site            order(48,54)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340531"
     Site            order(58,92..96)
                     /site_type="other"
                     /note="SUMO1-UBE2K interaction site [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(60,63,65,67..70,72,75,89,91..96)
                     /site_type="other"
                     /note="SUMO1-SENP2 interaction site [polypeptide binding]"
                     /db_xref="CDD:340531"
     Site            order(60,63,65,67..68,70,72,74..75,79..80,89,91..96)
                     /site_type="other"
                     /note="SUMO1-SENP1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340531"
     CDS             1..101
                     /gene="Sumo1"
                     /coded_by="NM_001009672.1:42..347"
                     /db_xref="GeneID:301442"
                     /db_xref="RGD:1306919"
ORIGIN      
        1 msdqeakpst edlgdkkege yiklkvigqd sseihfkvkm tthlkklkes ycqrqgvpmn
       61 slrflfegqr iadnhtpkel gmeeedviev yqeqtgghst v
//
LOCUS       NP_001026818             239 aa            linear   ROD 27-APR-2025
DEFINITION  EF-hand domain-containing protein D2 [Rattus norvegicus].
ACCESSION   NP_001026818 XP_216579
VERSION     NP_001026818.1
DBSOURCE    REFSEQ: accession NM_001031648.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Giricz,Z., Makkos,A., Schreckenberg,R., Poling,J., Lorchner,H.,
            Kiss,K., Bencsik,P., Braun,T., Schulz,R., Ferdinandy,P. and
            Schluter,K.D.
  TITLE     Swiprosin-1/EFhD-2 Expression in Cardiac Remodeling and
            Post-Infarct Repair: Effect of Ischemic Conditioning
  JOURNAL   Int J Mol Sci 21 (9), 3359 (2020)
   PUBMED   32397496
  REMARK    GeneRIF: Swiprosin-1/EFhD-2 Expression in Cardiac Remodeling and
            Post-Infarct Repair: Effect of Ischemic Conditioning.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Nippert,F., Schreckenberg,R., Hess,A., Weber,M. and Schluter,K.D.
  TITLE     The Effects of Swiprosin-1 on the Formation of Pseudopodia-Like
            Structures and beta-Adrenoceptor Coupling in Cultured Adult Rat
            Ventricular Cardiomyocytes
  JOURNAL   PLoS One 11 (12), e0167655 (2016)
   PUBMED   27992454
  REMARK    GeneRIF: Study reports that adult rat ventricular cardiomyocytes
            (ARVC) constitutively express swiprosin-1 on mRNA and protein level
            and that swiprosin-1 is required to initiate the formation of
            pseudopodia-like structures (spreading), a process necessary to
            adapt to culture conditions. Also, the expression level of
            swiprosin-1 is associated to that of GRK2 and thereby to
            beta-adrenoceptor responsiveness.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Vega,I.E., Traverso,E.E., Ferrer-Acosta,Y., Matos,E., Colon,M.,
            Gonzalez,J., Dickson,D., Hutton,M., Lewis,J. and Yen,S.H.
  TITLE     A novel calcium-binding protein is associated with tau proteins in
            tauopathy
  JOURNAL   J Neurochem 106 (1), 96-106 (2008)
   PUBMED   18346207
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098936.1.
            
            On Aug 12, 2005 this sequence version replaced XP_216579.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098936.1, DN932671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..239
                     /product="EF-hand domain-containing protein D2"
                     /note="swiprosin-1; EF hand domain containing 2"
                     /calculated_mol_wt=26628
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96C19; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C19; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C19; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D8Y0; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     Region          95..153
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(104,106,108,115,140,142,144,151)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96C19; propagated from
                     UniProtKB/Swiss-Prot (Q4FZY0.1)"
     CDS             1..239
                     /gene="Efhd2"
                     /coded_by="NM_001031648.1:28..747"
                     /db_xref="GeneID:298609"
                     /db_xref="RGD:1307585"
ORIGIN      
        1 matdelaskl srrlqmedeg geateqpgln gaaaaaaeap detaqalgsa ddelsakllr
       61 radlnqgige pqspsrrvfn pytefkefsr kqikdmekmf kqydagkdgf idlmelklmm
      121 eklgapqthl glksmiqevd edfdsklsfr efllifrkaa agelqedsgl hvlarlseid
      181 vstegvkgak nffeakvqai nvssrfeeei kaeqeerkkq aeevkqrkaa fkelqstfk
//
LOCUS       NP_001153128             256 aa            linear   ROD 27-APR-2025
DEFINITION  SCG6 (secretogranin VI) isoform SCG6 precursor [Rattus norvegicus].
ACCESSION   NP_001153128
VERSION     NP_001153128.1
DBSOURCE    REFSEQ: accession NM_001159656.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Taneera,J., Dhaiban,S., Mohammed,A.K., Mukhopadhyay,D.,
            Aljaibeji,H., Sulaiman,N., Fadista,J. and Salehi,A.
  TITLE     GNAS gene is an important regulator of insulin secretory capacity
            in pancreatic beta-cells
  JOURNAL   Gene 715, 144028 (2019)
   PUBMED   31374326
  REMARK    GeneRIF: GNAS is a crucial gene for the beta-cell insulin secretory
            capacity.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Masyuk,T.V., Masyuk,A.I., Lorenzo Pisarello,M., Howard,B.N.,
            Huang,B.Q., Lee,P.Y., Fung,X., Sergienko,E., Ardecky,R.J.,
            Chung,T.D.Y., Pinkerton,A.B. and LaRusso,N.F.
  TITLE     TGR5 contributes to hepatic cystogenesis in rodents with polycystic
            liver diseases through cyclic adenosine monophosphate/Galphas
            signaling
  JOURNAL   Hepatology 66 (4), 1197-1218 (2017)
   PUBMED   28543567
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Xue,N., Wei,C., Zhang,L., Liu,H., Wang,X. and Wang,L.
  TITLE     The Characteristics of Hepatic Gsalpha-cAMP Axis in HSHF Diet-Fed
            Obese Insulin Resistance Rats and Genetic Diabetic Mice
  JOURNAL   Biol Pharm Bull 40 (6), 774-781 (2017)
   PUBMED   28260721
  REMARK    GeneRIF: Our data revealed a positive correlation between hepatic
            Gsalpha-cAMP signal axis and fasting blood glucose (FBG) in slight
            insulin resistance stage of HIgh Sugar High Fat-diet rats and
            diabetic db/db mice. The current finding thus suggested hepatic
            Gsalpha-cAMP signal axis plays a central role in regulating of FBG
            during the developing and development of T2DM.
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Erb,S.J., Schappi,J.M. and Rasenick,M.M.
  TITLE     Antidepressants Accumulate in Lipid Rafts Independent of Monoamine
            Transporters to Modulate Redistribution of the G Protein, Galphas
  JOURNAL   J Biol Chem 291 (38), 19725-19733 (2016)
   PUBMED   27432886
  REMARK    GeneRIF: Translocation of Galphas, which shows delayed onset after
            chronic antidepressant treatment of rats or of C6 glioma cells,
            tracks with the delayed onset of therapeutic action of
            antidepressants
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Sarma,T., Koutsouris,A., Yu,J.Z., Krbanjevic,A., Hope,T.J. and
            Rasenick,M.M.
  TITLE     Activation of microtubule dynamics increases neuronal growth via
            the nerve growth factor (NGF)- and Galphas-mediated signaling
            pathways
  JOURNAL   J Biol Chem 290 (16), 10045-10056 (2015)
   PUBMED   25691569
  REMARK    GeneRIF: Activated Galpha s translocates from the plasma membrane
            and, through interaction with tubulin/microtubules in the cytosol,
            is important for neurite formation, development, and outgrowth.
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Eaton,S.A., Hough,T., Fischer-Colbrie,R. and Peters,J.
  TITLE     Maternal inheritance of the Gnas cluster mutation Ex1A-T affects
            size, implicating NESP55 in growth
  JOURNAL   Mamm Genome 24 (7-8), 276-285 (2013)
   PUBMED   23839232
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Swaroop,A., Agarwal,N., Gruen,J.R., Bick,D. and Weissman,S.M.
  TITLE     Differential expression of novel Gs alpha signal transduction
            protein cDNA species
  JOURNAL   Nucleic Acids Res 19 (17), 4725-4729 (1991)
   PUBMED   1716359
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Weinstein,L.S., Gejman,P.V., Friedman,E., Kadowaki,T.,
            Collins,R.M., Gershon,E.S. and Spiegel,A.M.
  TITLE     Mutations of the Gs alpha-subunit gene in Albright hereditary
            osteodystrophy detected by denaturing gradient gel electrophoresis
  JOURNAL   Proc Natl Acad Sci U S A 87 (21), 8287-8290 (1990)
   PUBMED   2122458
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Golf: an olfactory neuron specific-G protein involved in odorant
            signal transduction
  JOURNAL   Science 244 (4906), 790-795 (1989)
   PUBMED   2499043
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Votan-Bonamour,B., Plauchu,H. and Guibaud,P.
  TITLE     [Ectopic crystalline lens linked to its cause (homocyst inuria) by
            a simple geneological enquiry]
  JOURNAL   J Genet Hum 24 Suppl, 103-106 (1976)
   PUBMED   799727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB770483.1, AF105254.1,
            BC168156.1, AF107845.1 and BF394587.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            In addition, one of the transcripts contains a second overlapping
            ORF, which encodes a structurally unrelated protein - Alex.
            Alternative splicing of downstream exons is also observed, which
            results in different forms of the stimulatory G-protein alpha
            subunit, a key element of the classical signal transduction pathway
            linking receptor-ligand interactions with the activation of
            adenylyl cyclase and a variety of cellular reponses. Multiple
            transcript variants have been found for this gene. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (5) is maternally expressed. It
            lacks several 3' exons and has alternate 5' and 3' exons, as
            compared to variant 3. Variants 4 and 5 both encode neuroendocrine
            secretory protein 55 (NESP55), which localizes to large secretory
            vesicles of endocrine cells and neurons. The coding regions of
            variants 4 and 5 do not overlap the coding regions used by other
            transcripts; thus NESP55 has no similarity to isoforms of the
            G-protein alpha subunit.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF107845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 23839232
            NMD candidate  :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..256
                     /product="SCG6 (secretogranin VI) isoform SCG6 precursor"
                     /note="GNAS complex locus XLas-like; guanine
                     nucleotide-binding protein G-s, alpha subunit; guanine
                     nucleotide binding protein alpha s; adenylate
                     cyclase-stimulating G alpha protein; GNAS (guanine
                     nucleotide binding protein, alpha stimulating) complex
                     locus; SCG6 (secretogranin VI)"
                     /calculated_mol_wt=23835
     Region          1..256
                     /region_name="NESP55"
                     /note="Neuroendocrine-specific golgi protein P55 (NESP55);
                     pfam06390"
                     /db_xref="CDD:115071"
     sig_peptide     1..46
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=5358
     mat_peptide     47..256
                     /product="Neuroendocrine secretory protein 55.
                     /id=PRO_0000253973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=23835
     Region          61..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
     mat_peptide     170..173
                     /product="LHAL tetrapeptide. /evidence=ECO:0000255,
                     ECO:0000303|PubMed:10729789. /id=PRO_0000253974"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=453
     mat_peptide     249..256
                     /product="GPIPIRRH peptide. /evidence=ECO:0000255,
                     ECO:0000303|PubMed:10729789. /id=PRO_0000253975"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=945
     CDS             1..256
                     /gene="Gnas"
                     /gene_synonym="ALEX; G-alpha-8; Gnas1; Gnpas; Nesp55;
                     SCG6"
                     /coded_by="NM_001159656.1:249..1019"
                     /note="isoform SCG6 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:24896"
                     /db_xref="RGD:2716"
ORIGIN      
        1 mdrrsrahqw rrarhnyndl cppigrraat allwlscsia llralassna raqqraaqrr
       61 sflnahhrsa aaaaaaqvlp essesesdhe heeaepelar pecleydqdd yetetdsete
      121 pesdiqsete fetepetepe tapttepete pedergprga tfnqsltqrl halklqsada
      181 sprraqpttq epesasegee pqrepldedp rdpeeseelr eanrqprrck trrparrrdq
      241 spespprkgp ipirrh
//
LOCUS       NP_001091710             176 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial inner membrane protein Mpv17 [Rattus norvegicus].
ACCESSION   NP_001091710 XP_001075775 XP_340740
VERSION     NP_001091710.1
DBSOURCE    REFSEQ: accession NM_001098240.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Dalla Rosa,I., Camara,Y., Durigon,R., Moss,C.F., Vidoni,S.,
            Akman,G., Hunt,L., Johnson,M.A., Grocott,S., Wang,L.,
            Thorburn,D.R., Hirano,M., Poulton,J., Taylor,R.W., Elgar,G.,
            Marti,R., Voshol,P., Holt,I.J. and Spinazzola,A.
  TITLE     MPV17 Loss Causes Deoxynucleotide Insufficiency and Slow DNA
            Replication in Mitochondria
  JOURNAL   PLoS Genet 12 (1), e1005779 (2016)
   PUBMED   26760297
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Li,A., Li,L., Sun,X., Ni,Y., Chen,X., Guo,A. and Chen,X.
  TITLE     Increased Expression of Mitochondrial Inner-Membrane Protein Mpv17
            After Intracerebral Hemorrhage in Adult Rats
  JOURNAL   Neurochem Res 40 (8), 1620-1630 (2015)
   PUBMED   26123482
  REMARK    GeneRIF: Mpv17 expression was increased after intracerebral
            hemorrhage.
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Antonenkov,V.D., Isomursu,A., Mennerich,D., Vapola,M.H., Weiher,H.,
            Kietzmann,T. and Hiltunen,J.K.
  TITLE     The Human Mitochondrial DNA Depletion Syndrome Gene MPV17 Encodes a
            Non-selective Channel That Modulates Membrane Potential
  JOURNAL   J Biol Chem 290 (22), 13840-13861 (2015)
   PUBMED   25861990
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Spinazzola,A., Viscomi,C., Fernandez-Vizarra,E., Carrara,F.,
            D'Adamo,P., Calvo,S., Marsano,R.M., Donnini,C., Weiher,H.,
            Strisciuglio,P., Parini,R., Sarzi,E., Chan,A., DiMauro,S.,
            Rotig,A., Gasparini,P., Ferrero,I., Mootha,V.K., Tiranti,V. and
            Zeviani,M.
  TITLE     MPV17 encodes an inner mitochondrial membrane protein and is
            mutated in infantile hepatic mitochondrial DNA depletion
  JOURNAL   Nat Genet 38 (5), 570-575 (2006)
   PUBMED   16582910
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Meyer zum Gottesberge,A.M. and Felix,H.
  TITLE     Abnormal basement membrane in the inner ear and the kidney of the
            Mpv17-/- mouse strain: ultrastructural and immunohistochemical
            investigations
  JOURNAL   Histochem Cell Biol 124 (6), 507-516 (2005)
   PUBMED   16041630
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Zwacka,R.M., Reuter,A., Pfaff,E., Moll,J., Gorgas,K., Karasawa,M.
            and Weiher,H.
  TITLE     The glomerulosclerosis gene Mpv17 encodes a peroxisomal protein
            producing reactive oxygen species
  JOURNAL   EMBO J 13 (21), 5129-5134 (1994)
   PUBMED   7957077
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091193.1.
            
            On or before May 25, 2007 this sequence version replaced
            XP_340740.1, XP_001075775.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091193.1, DN948643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..176
                     /product="mitochondrial inner membrane protein Mpv17"
                     /note="protein Mpv17; Mpv17 transgene, kidney disease
                     mutant-like; MPV17 mitochondrial membrane protein-like;
                     MpV17 mitochondrial inner membrane protein"
                     /calculated_mol_wt=19496
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK62.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK62.1)"
     Site            92
                     /site_type="other"
                     /note="Determines ion selectivity.
                     /evidence=ECO:0000250|UniProtKB:P39210; propagated from
                     UniProtKB/Swiss-Prot (Q5BK62.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK62.1)"
     Region          109..170
                     /region_name="Mpv17_PMP22"
                     /note="Mpv17 / PMP22 family; pfam04117"
                     /db_xref="CDD:461182"
     Site            131..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK62.1)"
     CDS             1..176
                     /gene="Mpv17"
                     /gene_synonym="Mpv17l"
                     /coded_by="NM_001098240.1:252..782"
                     /db_xref="GeneID:360463"
                     /db_xref="RGD:1310512"
ORIGIN      
        1 malwrayqra laahpwkvqv ltagslmglg diisqqlver rglqqhqtgr tltmaslgcg
       61 fvgpvvggwy rvldhlipgt tkvnalkkml ldqggfapcf lgcflplvgv lngmsaqdnw
      121 aklkrdypda litnyylwpa vqlanfylvp lhyrlavvqc vavvwnsyls wkahql
//
LOCUS       NP_001020212             409 aa            linear   ROD 27-APR-2025
DEFINITION  immediate early response gene 5-like protein [Rattus norvegicus].
ACCESSION   NP_001020212 XP_575108
VERSION     NP_001020212.1
DBSOURCE    REFSEQ: accession NM_001025041.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087095.1.
            
            On Jun 25, 2005 this sequence version replaced XP_575108.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC087095.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..409
                     /product="immediate early response gene 5-like protein"
                     /calculated_mol_wt=42742
     Region          1..409
                     /region_name="IER"
                     /note="Immediate early response protein (IER); pfam05760"
                     /db_xref="CDD:461732"
     Region          168..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP0.1)"
     Region          312..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP0.1)"
     CDS             1..409
                     /gene="Ier5l"
                     /coded_by="NM_001025041.1:197..1426"
                     /db_xref="GeneID:499772"
                     /db_xref="RGD:1561058"
ORIGIN      
        1 mecaldaqsl isislrkihs srtqrggikl hknllvsyvl rnarqlylse ryaelyrrqq
       61 qqqqqqqqpp hhqhqhlaya apgmpasaad fgplqlgggg daearepvar hqlhqlhqlh
      121 qlhlqqqlhq hqhpaprgct aaapvavaga pagcagalse lpgcaalqpp hgaphrgqhl
      181 eplqpgpapl pppapaalcp rdprvpaacs apsappgaap ptvaassppa spapssspgf
      241 yrgaypapsd fgvhcssqtt vldldthvvt tvengylhqd ccasahcpcc gqgapgpgla
      301 saagckrkyy pgqeeeddee edagdlgaep pggtpfapck rarfedfcpd sspdasnisn
      361 lisifgsgfs glvsrqpdss eqppplngql cakqalaslg awtraivaf
//
LOCUS       NP_853658                278 aa            linear   ROD 27-APR-2025
DEFINITION  HCLS1-associated protein X-1 [Rattus norvegicus].
ACCESSION   NP_853658
VERSION     NP_853658.1
DBSOURCE    REFSEQ: accession NM_181627.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Choi,H.Y., Park,N., Lee,B., Choe,Y.I., Woo,D.K., Park,J.Y. and
            Yoo,J.C.
  TITLE     CPNE1-mediated neuronal differentiation can be inhibited by HAX1
            expression in HiB5 cells
  JOURNAL   Biochem Biophys Res Commun 533 (3), 319-324 (2020)
   PUBMED   32958249
  REMARK    GeneRIF: CPNE1-mediated neuronal differentiation can be inhibited
            by HAX1 expression in HiB5 cells.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Lu,X., Xue,P., Fu,L., Zhang,J., Jiang,J., Guo,X., Bao,G., Xu,G.,
            Sun,Y., Chen,J. and Cui,Z.
  TITLE     HAX1 is associated with neuronal apoptosis and astrocyte
            proliferation after spinal cord injury
  JOURNAL   Tissue Cell 54, 1-9 (2018)
   PUBMED   30309497
  REMARK    GeneRIF: our data indicated that HAX1 might play significant roles
            in pathological process of neuronal apoptosis and astrocyte
            proliferation during spinal cord injury
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Cui,L., He,W.J., Xu,F., Jiang,L., Lv,M.L., Huang,H., Xu,J.P.,
            Wu,Y., Zhong,H.B., Zhang,S.Y., Chen,L.F., Shen,C.L., Yao,G., Li,L.,
            Li,M. and Zeng,S.M.
  TITLE     Alterations in the expression of Hs1-associated protein X-1 in the
            rat retina after optic nerve crush
  JOURNAL   Mol Med Rep 14 (5), 4761-4766 (2016)
   PUBMED   27748880
  REMARK    GeneRIF: these results suggested that Hax1 may participate in
            regulating RGC apoptosis via interacting with caspase3 and HtrA2
            following ONC.
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Abdelwahid,E., Li,H., Wu,J., Irioda,A.C., de Carvalho,K.A. and
            Luo,X.
  TITLE     Endoplasmic reticulum (ER) stress triggers Hax1-dependent
            mitochondrial apoptotic events in cardiac cells
  JOURNAL   Apoptosis 21 (11), 1227-1239 (2016)
   PUBMED   27654581
  REMARK    GeneRIF: Hax1 is significantly downregulated in cardiac cells upon
            endoplasmic reticulum stress induction.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Koontz,J. and Kontrogianni-Konstantopoulos,A.
  TITLE     Competition through dimerization between antiapoptotic and
            proapoptotic HS-1-associated protein X-1 (Hax-1)
  JOURNAL   J Biol Chem 289 (6), 3468-3477 (2014)
   PUBMED   24347163
  REMARK    GeneRIF: Hax-1 is a family of anti- and proapoptotic regulators
            that may modulate cell survival and death through homo- or
            heterodimerization.
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Ortiz,D.F., Moseley,J., Calderon,G., Swift,A.L., Li,S. and
            Arias,I.M.
  TITLE     Identification of HAX-1 as a protein that binds bile salt export
            protein and regulates its abundance in the apical membrane of
            Madin-Darby canine kidney cells
  JOURNAL   J Biol Chem 279 (31), 32761-32770 (2004)
   PUBMED   15159385
  REMARK    GeneRIF: HAX-1 binds bile salt export protein (BSEP), cortactin,
            MDR1, and MDR2. HAX-1 and cortactin regulate BSEP abundance in the
            apical membrane of cells.
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Yin,H., Morioka,H., Towle,C.A., Vidal,M., Watanabe,T. and
            Weissbach,L.
  TITLE     Evidence that HAX-1 is an interleukin-1 alpha N-terminal binding
            protein
  JOURNAL   Cytokine 15 (3), 122-137 (2001)
   PUBMED   11554782
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Gallagher,A.R., Cedzich,A., Gretz,N., Somlo,S. and Witzgall,R.
  TITLE     The polycystic kidney disease protein PKD2 interacts with Hax-1, a
            protein associated with the actin cytoskeleton
  JOURNAL   Proc Natl Acad Sci U S A 97 (8), 4017-4022 (2000)
   PUBMED   10760273
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Suzuki,Y., Demoliere,C., Kitamura,D., Takeshita,H., Deuschle,U. and
            Watanabe,T.
  TITLE     HAX-1, a novel intracellular protein, localized on mitochondria,
            directly associates with HS1, a substrate of Src family tyrosine
            kinases
  JOURNAL   J Immunol 158 (6), 2736-2744 (1997)
   PUBMED   9058808
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY291062.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY291062.1, FQ213378.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132291,
                                           SAMD00132292 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..278
                     /product="HCLS1-associated protein X-1"
                     /note="HS1-binding protein 1; HS1-associating protein X-1;
                     HSP1BP-1; HS1 binding protein"
                     /calculated_mol_wt=31317
     Region          2..43
                     /region_name="Required for localization in mitochondria"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O00165; propagated from
                     UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          15..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          99..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          113..278
                     /region_name="Involved in HCLS1 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Site            126..127
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          174..205
                     /region_name="Involved in CASP9 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          175..246
                     /region_name="Involved in GNA13 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          182..278
                     /region_name="Required for localization in sarcoplasmic
                     reticulum"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          183..278
                     /region_name="Involved in PKD2 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00165; propagated from
                     UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00165; propagated from
                     UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          202..244
                     /region_name="Involved in ATP2A2 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          202..224
                     /region_name="Involved in PLN binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          209..278
                     /region_name="Mediates interaction with UCP3.
                     /evidence=ECO:0000250|UniProtKB:O35387"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     Region          269..278
                     /region_name="Required for ITGB6 binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TSE9.1)"
     CDS             1..278
                     /gene="Hax1"
                     /gene_synonym="HAX-1; Hs1bp1"
                     /coded_by="NM_181627.2:67..903"
                     /db_xref="GeneID:291202"
                     /db_xref="RGD:727960"
ORIGIN      
        1 msvfdlfrgf fgfpgprshr dpffggmtrd ddddeddeee edsgawgres yafdgfhpte
       61 efgfsfsprg gmrfhgnfgf ddlvrdfnsi fsemgawtlp shspelpgpe setpgvrlre
      121 gqtlrdsmlk ypdshqprif egvleshakp esskpapdwg sqgpfhrldd twpvsphsra
      181 redkdldsqv sqeglgpllq pqpksyfksi svtkitkpdg tveehrtvvd segrrettvt
      241 hqeahdssrs dpdpprssal ddpfsildll lgrwfrsr
//
LOCUS       NP_062146                191 aa            linear   ROD 27-APR-2025
DEFINITION  calcium-activated potassium channel subunit beta-1 [Rattus
            norvegicus].
ACCESSION   NP_062146
VERSION     NP_062146.1
DBSOURCE    REFSEQ: accession NM_019273.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Mysiewicz,S., North,K.C., Moreira,L. Jr., Odum,S.J., Bukiya,A.N.
            and Dopico,A.M.
  TITLE     Interspecies and regional variability of alcohol action on large
            cerebral arteries: regulation by KCNMB1 proteins
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 324 (4), R480-R496 (2023)
   PUBMED   36717168
  REMARK    GeneRIF: Interspecies and regional variability of alcohol action on
            large cerebral arteries: regulation by KCNMB1 proteins.
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bukiya,A.N., Leo,M.D., Jaggar,J.H. and Dopico,A.M.
  TITLE     Cholesterol activates BK channels by increasing KCNMB1 protein
            levels in the plasmalemma
  JOURNAL   J Biol Chem 296, 100381 (2021)
   PUBMED   33556372
  REMARK    GeneRIF: Cholesterol activates BK channels by increasing KCNMB1
            protein levels in the plasmalemma.
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Xu,T., Zhao,M., Li,H., Zhou,X., Liu,B., Sun,M., Xu,Z. and Gao,Q.
  TITLE     Antenatal Dexamethasone Exposure Impairs the High-Conductance
            Ca2+-Activated K+ Channels via Epigenetic Alteration at Gene
            Promoter in Male Offspring
  JOURNAL   Arterioscler Thromb Vasc Biol 40 (11), e284-e295 (2020)
   PUBMED   32967457
  REMARK    GeneRIF: Antenatal Dexamethasone Exposure Impairs the
            High-Conductance Ca(2+)-Activated K(+) Channels via Epigenetic
            Alteration at Gene Promoter in Male Offspring.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Reed,J.T., Pareek,T., Sriramula,S. and Pabbidi,M.R.
  TITLE     Aging influences cerebrovascular myogenic reactivity and BK channel
            function in a sex-specific manner
  JOURNAL   Cardiovasc Res 116 (7), 1372-1385 (2020)
   PUBMED   31738403
  REMARK    GeneRIF: Aging influences cerebrovascular myogenic reactivity and
            BK channel function in a sex-specific manner.
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Leo,M.D., Zhai,X., Yin,W. and Jaggar,J.H.
  TITLE     Impaired Trafficking of beta1 Subunits Inhibits BK Channels in
            Cerebral Arteries of Hypertensive Rats
  JOURNAL   Hypertension 72 (3), 765-775 (2018)
   PUBMED   30012867
  REMARK    GeneRIF: Data show that potassium channel subfamily M regulatory
            beta subunit 1 (beta1 Subunit) surface trafficking is Impaired in
            cerebral arteries of stroke-prone spontaneously hypertensive rats
            (SP-SHRs).
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Amberg,G.C. and Santana,L.F.
  TITLE     Downregulation of the BK channel beta1 subunit in genetic
            hypertension
  JOURNAL   Circ Res 93 (10), 965-971 (2003)
   PUBMED   14551242
  REMARK    GeneRIF: lower expression of the beta1 subunit during genetic
            borderline and severe hypertension reduced BK channel activity by
            decreasing the sensitivity of these channels to physiological
            changes in Ca2+
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Nehrke,K., Quinn,C.C. and Begenisich,T.
  TITLE     Molecular identification of Ca2+-activated K+ channels in parotid
            acinar cells
  JOURNAL   Am J Physiol Cell Physiol 284 (2), C535-C546 (2003)
   PUBMED   12388098
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Falk,T., Kilani,R.K., Strazdas,L.A., Borders,R.S., Steidl,J.V.,
            Yool,A.J. and Sherman,S.J.
  TITLE     Developmental regulation of the A-type potassium-channel current in
            hippocampal neurons: role of the Kvbeta 1.1 subunit
  JOURNAL   Neuroscience 120 (2), 387-404 (2003)
   PUBMED   12890510
  REMARK    GeneRIF: Kvbeta 1.1 contributes to the developmental control of the
            A-typepotassium channel current in hippocampal neurons.
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Jiang,Z., Wallner,M., Meera,P. and Toro,L.
  TITLE     Human and rodent MaxiK channel beta-subunit genes: cloning and
            characterization
  JOURNAL   Genomics 55 (1), 57-67 (1999)
   PUBMED   9888999
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Chang,C.P., Dworetzky,S.I., Wang,J. and Goldstein,M.E.
  TITLE     Differential expression of the alpha and beta subunits of the
            large-conductance calcium-activated potassium channel: implication
            for channel diversity
  JOURNAL   Brain Res Mol Brain Res 45 (1), 33-40 (1997)
   PUBMED   9105668
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF020712.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF020712.1, FM030431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..191
                     /product="calcium-activated potassium channel subunit
                     beta-1"
                     /note="slowpoke-beta; BK channel subunit beta-1; maxi K
                     channel subunit beta-1; potassium channel subfamily M
                     regulatory beta subunit 1; charybdotoxin receptor subunit
                     beta-1; potassium large conductance calcium-activated
                     channel, subfamily M, beta member 1; calcium-activated
                     potassium channel subunit beta; calcium-activated
                     potassium channel, subfamily M subunit beta-1;
                     calcium-activated potassium channel beta subunit"
                     /calculated_mol_wt=21777
     Region          7..190
                     /region_name="CaKB"
                     /note="Calcium-activated potassium channel, beta subunit;
                     pfam03185"
                     /db_xref="CDD:460838"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97678.4)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97678.4)"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97678.4)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97678.4)"
     CDS             1..191
                     /gene="Kcnmb1"
                     /gene_synonym="BKbeta; BKbeta1; k(VCA)beta-1; slo-beta;
                     slo-beta-1"
                     /coded_by="NM_019273.1:314..889"
                     /db_xref="GeneID:29747"
                     /db_xref="RGD:2961"
ORIGIN      
        1 mgkklvmaqk rgetralclg vamvvcaait yyilgttvlp lyqksvwtqe stchlvetni
       61 kdqeelegrk vpqypclwvn vsavgrwaml yhtedtrdqn qqcsyiprnl dnyqtalvdv
      121 kkvranfykh hnfycfsapq vnetsvvyqr lygpqillfs ffwptflltg glliiamvkl
      181 nrslsvlaaq k
//
LOCUS       NP_569095                461 aa            linear   ROD 27-APR-2025
DEFINITION  coronin-1A [Rattus norvegicus].
ACCESSION   NP_569095
VERSION     NP_569095.1
DBSOURCE    REFSEQ: accession NM_130411.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Alvarez Julia,A., Frasch,A.C. and Fuchsova,B.
  TITLE     Neuronal filopodium formation induced by the membrane glycoprotein
            M6a (Gpm6a) is facilitated by coronin-1a, Rac1, and p21-activated
            kinase 1 (Pak1)
  JOURNAL   J Neurochem 137 (1), 46-61 (2016)
   PUBMED   26809475
  REMARK    GeneRIF: Formation of filopodia by membrane glycoprotein M6a
            (Gpm6a) requires actin regulator coronin-1a (Coro1a), known to
            regulate plasma membrane localization and activation of Rac1 and
            its downstream effector Pak1.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Lelli,A., Michel,V., Boutet de Monvel,J., Cortese,M.,
            Bosch-Grau,M., Aghaie,A., Perfettini,I., Dupont,T., Avan,P.,
            El-Amraoui,A. and Petit,C.
  TITLE     Class III myosins shape the auditory hair bundles by limiting
            microvilli and stereocilia growth
  JOURNAL   J Cell Biol 212 (2), 231-244 (2016)
   PUBMED   26754646
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Terzi,Y.K., Kocaefe,Y.C. and Ayter,S.
  TITLE     Coronin 1A inhibits neurite outgrowth in PC12 cells
  JOURNAL   Neurosci Lett 582, 38-42 (2014)
   PUBMED   25179994
  REMARK    GeneRIF: Coronin 1A has an inhibitory effect on neurite outgrowth
            in vitro.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Mace,E.M. and Orange,J.S.
  TITLE     Lytic immune synapse function requires filamentous actin
            deconstruction by Coronin 1A
  JOURNAL   Proc Natl Acad Sci U S A 111 (18), 6708-6713 (2014)
   PUBMED   24760828
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Jayachandran,R., Liu,X., Bosedasgupta,S., Muller,P., Zhang,C.L.,
            Moshous,D., Studer,V., Schneider,J., Genoud,C., Fossoud,C.,
            Gambino,F., Khelfaoui,M., Muller,C., Bartholdi,D., Rossez,H.,
            Stiess,M., Houbaert,X., Jaussi,R., Frey,D., Kammerer,R.A.,
            Deupi,X., de Villartay,J.P., Luthi,A., Humeau,Y. and Pieters,J.
  TITLE     Coronin 1 regulates cognition and behavior through modulation of
            cAMP/protein kinase A signaling
  JOURNAL   PLoS Biol 12 (3), e1001820 (2014)
   PUBMED   24667537
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Didichenko,S.A., Segal,A.W. and Thelen,M.
  TITLE     Evidence for a pool of coronin in mammalian cells that is sensitive
            to PI 3-kinase
  JOURNAL   FEBS Lett 485 (2-3), 147-152 (2000)
   PUBMED   11094157
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Reeves,E.P., Dekker,L.V., Forbes,L.V., Wientjes,F.B., Grogan,A.,
            Pappin,D.J. and Segal,A.W.
  TITLE     Direct interaction between p47phox and protein kinase C: evidence
            for targeting of protein kinase C by p47phox in neutrophils
  JOURNAL   Biochem J 344 Pt 3 (Pt 3), 859-866 (1999)
   PUBMED   10585874
  REMARK    Erratum:[Biochem J 2000 Feb 1;345 Pt 3:767]
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Chu,C.C. and Paul,W.E.
  TITLE     Expressed genes in interleukin-4 treated B cells identified by cDNA
            representational difference analysis
  JOURNAL   Mol Immunol 35 (8), 487-502 (1998)
   PUBMED   9798653
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Grogan,A., Reeves,E., Keep,N., Wientjes,F., Totty,N.F.,
            Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Cytosolic phox proteins interact with and regulate the assembly of
            coronin in neutrophils
  JOURNAL   J Cell Sci 110 (Pt 24), 3071-3081 (1997)
   PUBMED   9365277
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Suzuki,K., Nishihata,J., Arai,Y., Honma,N., Yamamoto,K., Irimura,T.
            and Toyoshima,S.
  TITLE     Molecular cloning of a novel actin-binding protein, p57, with a WD
            repeat and a leucine zipper motif
  JOURNAL   FEBS Lett 364 (3), 283-288 (1995)
   PUBMED   7758584
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF495469.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF495469.1, FQ230931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680416, SAMN06680422
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..461
                     /product="coronin-1A"
                     /note="TACO; coronin-like protein A; tryptophan
                     aspartate-containing coat protein; clipin-A; coronin,
                     actin binding protein 1A"
                     /calculated_mol_wt=50934
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P31146; propagated from
                     UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P31146; propagated from
                     UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          9..461
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..63
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          73..110
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          123..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          164..204
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          180..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          207..251
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          223..263
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          258..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          270..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          302..349
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Region          407..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:O89053; propagated from
                     UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q91ZN1.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O89053; propagated from
                     UniProtKB/Swiss-Prot (Q91ZN1.3)"
     CDS             1..461
                     /gene="Coro1a"
                     /coded_by="NM_130411.2:105..1490"
                     /db_xref="GeneID:155151"
                     /db_xref="RGD:620009"
ORIGIN      
        1 msrqvvrssk frhvfgqpak adqcyedvrv sqttwdsgfc avnpkfmali ceasgggafl
       61 vlplgktgrv dknvplvcgh tapvldiawc phndnviasg sedctvmvwe ipdgglvlpl
      121 repvvtlegh tkrvgivawh ptaqnvllsa gcdnvilvwd vgtgaavltl gpdvhpdtiy
      181 svdwsrdgal ictscrdkrv rvieprkgtv vaekerpheg trpvhavfvs egkilttgfs
      241 rmserqvalw dtkhleepls lqeldtssgv llpffdpdtn ivylcgkgds siryfeitse
      301 apflhylsmf sskesqrgmg ympkrglevn kceiarfykl herkcepiam tvprksdlfq
      361 edlypptagp dpaltaeewl sgrdagplli slkdgyvppk srelrvnrgl dsarrratpe
      421 psstlssdtv srleedvrnl naivqklqer ldrleetvqa k
//
LOCUS       NP_001019521             162 aa            linear   ROD 27-APR-2025
DEFINITION  EF-hand calcium-binding domain-containing protein 11 [Rattus
            norvegicus].
ACCESSION   NP_001019521 XP_576087
VERSION     NP_001019521.1
DBSOURCE    REFSEQ: accession NM_001024350.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Herlan,L., Schulz,A., Schulte,L., Schulz,H., Hubner,N. and
            Kreutz,R.
  TITLE     Novel candidate genes for impaired nephron development in a rat
            model with inherited nephron deficit and albuminuria
  JOURNAL   Clin Exp Pharmacol Physiol 42 (10), 1051-1058 (2015)
   PUBMED   26192016
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079408.1.
            
            On May 27, 2005 this sequence version replaced XP_576087.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079408.1, CK469542.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418988 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..162
                     /product="EF-hand calcium-binding domain-containing
                     protein 11"
                     /note="EF-hand domain-containing protein C14orf143
                     homolog"
                     /calculated_mol_wt=18363
     Region          20..156
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..162
                     /gene="Efcab11"
                     /coded_by="NM_001024350.1:66..554"
                     /db_xref="GeneID:500705"
                     /db_xref="RGD:1565006"
ORIGIN      
        1 mflseagarp rageisaser rkwvevfkac dednkgylsr edfkvaivml fgykpskiea
       61 davmssanpd tsgvslegfl nvvqrkkeaq lyrneirhif tafdvhyrgf ltledfkraf
      121 sqvapklpsr tvlevfread qdsdghvsfr dfeyamnhgk ak
//
LOCUS       NP_113833                148 aa            linear   ROD 27-APR-2025
DEFINITION  receptor activity-modifying protein 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_113833
VERSION     NP_113833.1
DBSOURCE    REFSEQ: accession NM_031645.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Meng,Q., Shi,D., Feng,J., Su,Y., Long,Y., He,S., Wang,S., Wang,Y.,
            Zhang,X. and Chen,X.
  TITLE     Hypercholesterolemia Up-Regulates the Expression of Intermedin and
            Its Receptor Components in the Aorta of Rats via Inducing the
            Oxidative Stress
  JOURNAL   Ann Clin Lab Sci 46 (1), 5-17 (2016)
   PUBMED   26927337
  REMARK    GeneRIF: Increased expression of IMD and all its receptor
            components (CRLR, RAMP1, RAMP2, and RAMP3) were displayed within
            the aorta of rats with Hypercholesterolemia.
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Fu,W., Ruangkittisakul,A., MacTavish,D., Shi,J.Y., Ballanyi,K. and
            Jhamandas,J.H.
  TITLE     Amyloid beta (Abeta) peptide directly activates amylin-3 receptor
            subtype by triggering multiple intracellular signaling pathways
  JOURNAL   J Biol Chem 287 (22), 18820-18830 (2012)
   PUBMED   22500019
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Nagayama,T., Seiryu,M., Deguchi,T., Kano,M., Suzuki,T.,
            Takano-Yamamoto,T. and Ichikawa,H.
  TITLE     Increase of CGRP-containing nerve fibers in the rat periodontal
            ligament after luxation
  JOURNAL   Cell Mol Neurobiol 32 (3), 391-397 (2012)
   PUBMED   22038237
  REMARK    GeneRIF: After traumatic injury to periodontal ligament, CGRP nerve
            fibers appear in close vicinity of small and large receptor
            activity modifying protein (RAMP)1 cells at 5-7 days.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Csati,A., Tajti,J., Tuka,B., Edvinsson,L. and Warfvinge,K.
  TITLE     Calcitonin gene-related peptide and its receptor components in the
            human sphenopalatine ganglion -- interaction with the sensory
            system
  JOURNAL   Brain Res 1435, 29-39 (2012)
   PUBMED   22208649
  REMARK    GeneRIF: The present finding demonstrated that RAMP1
            immunoreactivity was localized in many neurons and phenopalatine
            ganglion.
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Edvinsson,L., Eftekhari,S., Salvatore,C.A. and Warfvinge,K.
  TITLE     Cerebellar distribution of calcitonin gene-related peptide (CGRP)
            and its receptor components calcitonin receptor-like receptor (CLR)
            and receptor activity modifying protein 1 (RAMP1) in rat
  JOURNAL   Mol Cell Neurosci 46 (1), 333-339 (2011)
   PUBMED   21040789
  REMARK    GeneRIF: Data demonstrate that there is a rich expression of
            calcitonin gene-related peptide (CGRP) and its receptor elements
            CLR and RAMP1 in the cerebellum which points towards a functional
            role of CGRP in cerebellar Purkinje cells.
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Husmann,K., Sexton,P.M., Fischer,J.A. and Born,W.
  TITLE     Mouse receptor-activity-modifying proteins 1, -2 and -3: amino acid
            sequence, expression and function
  JOURNAL   Mol Cell Endocrinol 162 (1-2), 35-43 (2000)
   PUBMED   10854696
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Nagae,T., Mukoyama,M., Sugawara,A., Mori,K., Yahata,K.,
            Kasahara,M., Suganami,T., Makino,H., Fujinaga,Y., Yoshioka,T.,
            Tanaka,I. and Nakao,K.
  TITLE     Rat receptor-activity-modifying proteins (RAMPs) for
            adrenomedullin/CGRP receptor: cloning and upregulation in
            obstructive nephropathy
  JOURNAL   Biochem Biophys Res Commun 270 (1), 89-93 (2000)
   PUBMED   10733909
REFERENCE   8  (residues 1 to 148)
  AUTHORS   McLatchie,L.M., Fraser,N.J., Main,M.J., Wise,A., Brown,J.,
            Thompson,N., Solari,R., Lee,M.G. and Foord,S.M.
  TITLE     RAMPs regulate the transport and ligand specificity of the
            calcitonin-receptor-like receptor
  JOURNAL   Nature 393 (6683), 333-339 (1998)
   PUBMED   9620797
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Palmberg,I. and Reuter,M.
  TITLE     Sensory receptors in the head of Stenostomum leucops. I.
            Presumptive photoreceptors
  JOURNAL   Acta Biol Hung 43 (1-4), 259-267 (1992)
   PUBMED   1299115
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Lengvari,I., Csoknya,M., Merchenthaler,I. and Hamori,J.
  TITLE     Immunohistochemical study of the nervous system in earthworm
            (Lumbricus terrestris L.)
  JOURNAL   Acta Biol Hung 43 (1-4), 253-258 (1992)
   PUBMED   1299114
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB042887.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB042887.1, DV720488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..148
                     /product="receptor activity-modifying protein 1 precursor"
                     /note="receptor (calcitonin) activity modifying protein 1;
                     receptor (G protein-coupled) activity modifying protein 1"
                     /calculated_mol_wt=13905
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2928
     mat_peptide     27..148
                     /product="Receptor activity-modifying protein 1.
                     /id=PRO_0000030170"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ74.1)"
                     /calculated_mol_wt=13905
     Region          37..145
                     /region_name="RAMP"
                     /note="Receptor activity modifying family; pfam04901"
                     /db_xref="CDD:461471"
     Site            119..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JJ74.1)"
     CDS             1..148
                     /gene="Ramp1"
                     /coded_by="NM_031645.1:40..486"
                     /db_xref="GeneID:58965"
                     /db_xref="RGD:61870"
ORIGIN      
        1 mapglrglpr rglwlllahh lfmvtacrdp dygtliqelc lsrfkedmet igktlwcdwg
       61 ktigsygelt hctklvanki gcfwpnpevd kffiavhhry fskcpvsgra lrdppnsilc
      121 pfivlpitvt llmtalvvwr skrtegiv
//
LOCUS       NP_852042                445 aa            linear   ROD 27-APR-2025
DEFINITION  reticulon-4 receptor-like 1 precursor [Rattus norvegicus].
ACCESSION   NP_852042
VERSION     NP_852042.1
DBSOURCE    REFSEQ: accession NM_181377.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Yoo,S.W., Motari,M.G. and Schnaar,R.L.
  TITLE     Agenesis of the corpus callosum in Nogo receptor deficient mice
  JOURNAL   J Comp Neurol 525 (2), 291-301 (2017)
   PUBMED   27339102
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Dickendesher,T.L., Baldwin,K.T., Mironova,Y.A., Koriyama,Y.,
            Raiker,S.J., Askew,K.L., Wood,A., Geoffroy,C.G., Zheng,B.,
            Liepmann,C.D., Katagiri,Y., Benowitz,L.I., Geller,H.M. and
            Giger,R.J.
  TITLE     NgR1 and NgR3 are receptors for chondroitin sulfate proteoglycans
  JOURNAL   Nat Neurosci 15 (5), 703-712 (2012)
   PUBMED   22406547
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Thomas,R., Favell,K., Morante-Redolat,J., Pool,M., Kent,C.,
            Wright,M., Daignault,K., Ferraro,G.B., Montcalm,S., Durocher,Y.,
            Fournier,A., Perez-Tur,J. and Barker,P.A.
  TITLE     LGI1 is a Nogo receptor 1 ligand that antagonizes myelin-based
            growth inhibition
  JOURNAL   J Neurosci 30 (19), 6607-6612 (2010)
   PUBMED   20463223
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Richard,M., Sacquet,J., Jourdan,F. and Pellier-Monnin,V.
  TITLE     Spatio-temporal expression pattern of receptors for
            myelin-associated inhibitors in the developing rat olfactory system
  JOURNAL   Brain Res 1252, 52-65 (2009)
   PUBMED   19063867
  REMARK    GeneRIF: spatio-temporal expression pattern of NgR1, NgR2 & NgR3
            mRNAs & corresponding proteins in developing olfactory system; data
            suggest, in non-pathological conditions, NgR1 & homologs may play a
            role in axon outgrowth in the olfactory system.
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Venkatesh,K., Chivatakarn,O., Lee,H., Joshi,P.S., Kantor,D.B.,
            Newman,B.A., Mage,R., Rader,C. and Giger,R.J.
  TITLE     The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent
            receptor selective for myelin-associated glycoprotein
  JOURNAL   J Neurosci 25 (4), 808-822 (2005)
   PUBMED   15673660
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Pignot,V., Hein,A.E., Barske,C., Wiessner,C., Walmsley,A.R.,
            Kaupmann,K., Mayeur,H., Sommer,B., Mir,A.K. and Frentzel,S.
  TITLE     Characterization of two novel proteins, NgRH1 and NgRH2,
            structurally and biochemically homologous to the Nogo-66 receptor
  JOURNAL   J Neurochem 85 (3), 717-728 (2003)
   PUBMED   12694398
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC129084.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129084.1, AF532861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..445
                     /product="reticulon-4 receptor-like 1 precursor"
                     /note="ngR3; nogo receptor-like 2; nogo-66
                     receptor-related protein 3; Nogo-66 receptor homolog 2"
                     /calculated_mol_wt=47294
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2499
     mat_peptide     25..424
                     /product="Reticulon-4 receptor-like 1. /id=PRO_0000046046"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
                     /calculated_mol_wt=45187
     Region          37..58
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          55..76
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          77..98
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <80..>255
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          101..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          102..126
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          126..147
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          127..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..219
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          199..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          222..243
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          223..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          304..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Region          401..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     Site            424..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WD0.1)"
     CDS             1..445
                     /gene="Rtn4rl1"
                     /gene_synonym="Ngrh2"
                     /coded_by="NM_181377.3:309..1646"
                     /db_xref="GeneID:303311"
                     /db_xref="RGD:727812"
ORIGIN      
        1 mlrkgccvel lllllagelp lsggcprdcv cypspmtvsc qahnfaaipe gipedserif
       61 lqnnhitflq qghfspamvt lwiysnnitf iapntfegfv hleeldlgdn rqlrtlapet
      121 fqglvklhal ylykcglssl pagifgglhs lqylylqdnh ieylqddifv dlvnlshlfl
      181 hgnklwslgq gifrglvnld rlllhenqlq wvhhkafhdl hrlttlflfn nsltelqgdc
      241 laplvalefl rlngnawdcg crarslwewl rrfrgsssvv pcatpelrqg qdlkslrved
      301 frnctgpasp hqikshtlst sdraarkehh pshgasrdkg hphghlpgsr sgskkpgknc
      361 tshrnrnqis kgsagkelpe lqdyapdyqh kfsfdimpta rpkrkgkcar rtpirapsgv
      421 qqassgtalg vsllawilgl vvslr
//
LOCUS       NP_001025090             277 aa            linear   ROD 27-APR-2025
DEFINITION  adaptin ear-binding coat-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_001025090
VERSION     NP_001025090.1
DBSOURCE    REFSEQ: accession NM_001029919.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Ritter,B., Murphy,S., Dokainish,H., Girard,M., Gudheti,M.V.,
            Kozlov,G., Halin,M., Philie,J., Jorgensen,E.M., Gehring,K. and
            McPherson,P.S.
  TITLE     NECAP 1 regulates AP-2 interactions to control vesicle size,
            number, and cargo during clathrin-mediated endocytosis
  JOURNAL   PLoS Biol 11 (10), e1001670 (2013)
   PUBMED   24130457
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Ritter,B., Denisov,A.Y., Philie,J., Allaire,P.D.,
            Legendre-Guillemin,V., Zylbergold,P., Gehring,K. and McPherson,P.S.
  TITLE     The NECAP PHear domain increases clathrin accessory protein binding
            potential
  JOURNAL   EMBO J 26 (18), 4066-4077 (2007)
   PUBMED   17762867
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Murshid,A., Srivastava,A., Kumar,R. and Presley,J.F.
  TITLE     Characterization of the localization and function of NECAP 1 in
            neurons
  JOURNAL   J Neurochem 98 (6), 1746-1762 (2006)
   PUBMED   16879712
  REMARK    GeneRIF: NECAP 1 plays a role in clathrin-mediated neuronal
            endocytosis, including a role in presynaptic endocytosis. (NECAP 1)
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Mishra,S.K., Hawryluk,M.J., Brett,T.J., Keyel,P.A., Dupin,A.L.,
            Jha,A., Heuser,J.E., Fremont,D.H. and Traub,L.M.
  TITLE     Dual engagement regulation of protein interactions with the AP-2
            adaptor alpha appendage
  JOURNAL   J Biol Chem 279 (44), 46191-46203 (2004)
   PUBMED   15292237
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Ritter,B., Philie,J., Girard,M., Tung,E.C., Blondeau,F. and
            McPherson,P.S.
  TITLE     Identification of a family of endocytic proteins that define a new
            alpha-adaptin ear-binding motif
  JOURNAL   EMBO Rep 4 (11), 1089-1095 (2003)
   PUBMED   14555962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097496.1 and CO402572.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..277
                     /product="adaptin ear-binding coat-associated protein 1"
                     /note="adaptin ear-binding clathrin-associated protein;
                     NECAP-1; NECAP endocytosis-associated protein 1"
                     /calculated_mol_wt=29661
     Region          7..164
                     /region_name="DUF1681"
                     /note="Protein of unknown function (DUF1681); pfam07933"
                     /db_xref="CDD:462320"
     Region          164..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P69682.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NC96; propagated from
                     UniProtKB/Swiss-Prot (P69682.1)"
     Region          254..257
                     /region_name="WXXF motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P69682.1)"
     Region          274..277
                     /region_name="WXXF motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P69682.1)"
     CDS             1..277
                     /gene="Necap1"
                     /gene_synonym="RGD1306053"
                     /coded_by="NM_001029919.2:20..853"
                     /db_xref="GeneID:312694"
                     /db_xref="RGD:1306053"
ORIGIN      
        1 maaeleyesv lcvkpdvsvy ripprasnrg yrasdwkldq pdwtgrlrit skgkiayikl
       61 edkvsgelfa qapveqypgi avetvadssr yfviriqdgt grsafigigf tdrgdafdfn
      121 vslqdhfkwv kqeteiskes qemdsrpkld lgfkegqtik lsignitakk ggtskprasg
      181 tgglsllppp pggkvtippp sssvaisnhv tpppipksnh gsndsdilld ldspapvpts
      241 apapapasts ndlwgdfsta sssvpnqapq psnwvqf
//
LOCUS       NP_001007725             240 aa            linear   ROD 27-APR-2025
DEFINITION  dephospho-CoA kinase domain-containing protein [Rattus norvegicus].
ACCESSION   NP_001007725 XP_340918
VERSION     NP_001007725.1
DBSOURCE    REFSEQ: accession NM_001007724.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079186.1.
            
            On Nov 29, 2004 this sequence version replaced XP_340918.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079186.1, EV778343.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..240
                     /product="dephospho-CoA kinase domain-containing protein"
                     /calculated_mol_wt=27221
     Region          1..196
                     /region_name="CoaE"
                     /note="Dephospho-CoA kinase [Coenzyme transport and
                     metabolism]; COG0237"
                     /db_xref="CDD:440007"
     CDS             1..240
                     /gene="Dcakd"
                     /coded_by="NM_001007724.1:168..890"
                     /db_xref="GeneID:360639"
                     /db_xref="RGD:1359211"
ORIGIN      
        1 mflvgltggi asgkssviqv fqqlgcavid vdviarhivq pgcpahrriv eafgtevlle
       61 ngdinrkvlg dlifnqpdrr qllnsithpe irkemmketf kyflrgyryv ildipllfet
      121 kkllkymkht vvvycdrdtq larlmkrnnl nredaearin sqlplkdkar manhvldnsg
      181 ewsltrrqvi llhaklersm eylplrlgfl tglagiasll ylltryllps pqlgnpgskp
//
LOCUS       NP_001011984             634 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat and SOCS box protein 2 [Rattus norvegicus].
ACCESSION   NP_001011984 XP_216768
VERSION     NP_001011984.1
DBSOURCE    REFSEQ: accession NM_001011984.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Rajan,S., Chu Pham Dang,H., Djambazian,H., Zuzan,H., Fedyshyn,Y.,
            Ketela,T., Moffat,J., Hudson,T.J. and Sladek,R.
  TITLE     Analysis of early C2C12 myogenesis identifies stably and
            differentially expressed transcriptional regulators whose
            knock-down inhibits myoblast differentiation
  JOURNAL   Physiol Genomics 44 (2), 183-197 (2012)
   PUBMED   22147266
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Bello,N.F., Lamsoul,I., Heuze,M.L., Metais,A., Moreaux,G.,
            Calderwood,D.A., Duprez,D., Moog-Lutz,C. and Lutz,P.G.
  TITLE     The E3 ubiquitin ligase specificity subunit ASB2beta is a novel
            regulator of muscle differentiation that targets filamin B to
            proteasomal degradation
  JOURNAL   Cell Death Differ 16 (6), 921-932 (2009)
   PUBMED   19300455
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Kohroki,J., Nishiyama,T., Nakamura,T. and Masuho,Y.
  TITLE     ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin
            ligase complexes
  JOURNAL   FEBS Lett 579 (30), 6796-6802 (2005)
   PUBMED   16325183
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085882.1.
            
            On Feb 11, 2005 this sequence version replaced XP_216768.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..634
                     /product="ankyrin repeat and SOCS box protein 2"
                     /note="ASB-2; ankyrin repeat and SOCS box-containing
                     protein 2; ankyrin repeat and SOCS box protein 2-like"
                     /calculated_mol_wt=70074
     Region          35..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          104..133
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          119..400
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          137..169
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          137..167
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          171..200
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          173..202
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          204..235
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          204..233
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Site            order(237,239,243..244,247..249,251..252,256,259,268,270,
                     272,276..277,280..282,284..285,289,292,301,303,305,
                     309..310,313..315,317..318,322,325,334)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          237..268
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          237..266
                     /region_name="ANK 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          270..301
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          270..299
                     /region_name="ANK 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          303..334
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          303..332
                     /region_name="ANK 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          336..365
                     /region_name="ANK 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          368..397
                     /region_name="ANK 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          368..396
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96Q27; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          373..469
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          401..440
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          410..439
                     /region_name="ANK 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          440..469
                     /region_name="ANK 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          442..469
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          473..501
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          476..504
                     /region_name="ANK 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S6.1)"
     Region          590..634
                     /region_name="SOCS_ASB2"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB2-like proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. ASB2
                     targets specific proteins to destruction by the proteasome
                     in leukemia cells that have been...; cd03721"
                     /db_xref="CDD:239691"
     Site            order(591..596,602,612,618,623)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239691"
     CDS             1..634
                     /gene="Asb2"
                     /coded_by="NM_001011984.1:179..2083"
                     /db_xref="GeneID:299266"
                     /db_xref="RGD:1306414"
ORIGIN      
        1 msteistrgr qraigheeys lysslseeel vqmaieqsla dktrgptpae tsvssqtnhq
       61 pghihpwtrs ssppesppar aplglfqgvm qkyssnlfkt sqmaamdpvl kaikegdeea
      121 lkamiqdgkn laepnkegwl plheaayygk lgclkvlqra ypgtidqrtl qeetalylat
      181 crehldclls llqagaepdi snksretply kacerknaea vrilvqynad anhrcnrgwt
      241 alhesvsrnd levmeilvsg gakveaknvy sitplfvaaq sgqlealrfl akhgadintq
      301 asdsasalye acknehedvv efllsqgada nkankdgllp lhvaskkgny rivqmllpvt
      361 srtrvrrsgi splhlaaern hdavlealla arfdvntpla perarlyedr rtsalyfavv
      421 nnnvyatell llagadpnrd vispllvair hgclrtmqll ldhganiday iathptafpa
      481 timfamkcls llkflmdlgc dgepcfscly gngphppapr sgrfndapvd dkapsvvqfc
      541 eflsapevsr wagpiidvll dyvgnvqlcs rlkehidsfe dwavikekae pprplahlcr
      601 lrvrkaigky riklldtlpl pgrlirylky entq
//
LOCUS       NP_001071060              70 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL38 [Rattus norvegicus].
ACCESSION   NP_001071060 XP_001071627 XP_001071665
VERSION     NP_001071060.1
DBSOURCE    REFSEQ: accession NM_001077592.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Kondrashov,N., Pusic,A., Stumpf,C.R., Shimizu,K., Hsieh,A.C.,
            Ishijima,J., Shiroishi,T. and Barna,M.
  TITLE     Ribosome-mediated specificity in Hox mRNA translation and
            vertebrate tissue patterning
  JOURNAL   Cell 145 (3), 383-397 (2011)
   PUBMED   21529712
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Noben-Trauth,K. and Latoche,J.R.
  TITLE     Ectopic mineralization in the middle ear and chronic otitis media
            with effusion caused by RPL38 deficiency in the Tail-short (Ts)
            mouse
  JOURNAL   J Biol Chem 286 (4), 3079-3093 (2011)
   PUBMED   21062742
REFERENCE   5  (residues 1 to 70)
  AUTHORS   Bayes,A., van de Lagemaat,L.N., Collins,M.O., Croning,M.D.,
            Whittle,I.R., Choudhary,J.S. and Grant,S.G.
  TITLE     Characterization of the proteome, diseases and evolution of the
            human postsynaptic density
  JOURNAL   Nat Neurosci 14 (1), 19-21 (2011)
   PUBMED   21170055
REFERENCE   6  (residues 1 to 70)
  AUTHORS   Trinidad,J.C., Specht,C.G., Thalhammer,A., Schoepfer,R. and
            Burlingame,A.L.
  TITLE     Comprehensive identification of phosphorylation sites in
            postsynaptic density preparations
  JOURNAL   Mol Cell Proteomics 5 (5), 914-922 (2006)
   PUBMED   16452087
REFERENCE   7  (residues 1 to 70)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 70)
  AUTHORS   Kuwano,Y., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L38
  JOURNAL   Biochem Biophys Res Commun 175 (2), 551-555 (1991)
   PUBMED   1840484
REFERENCE   9  (residues 1 to 70)
  AUTHORS   Tsurugi,K., Collatz,E., Todokoro,K., Ulbrich,N., Lightfoot,H.N. and
            Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 60 S ribosomal subunit proteins La, Lb, Lf,
            P1, P2, L13', L14, L18', L20, and L38
  JOURNAL   J Biol Chem 253 (3), 946-955 (1978)
   PUBMED   621213
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC101933.1.
            
            On or before Nov 9, 2006 this sequence version replaced
            XP_001071627.1, XP_001071665.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101933.1, CB567125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..70
                     /product="large ribosomal subunit protein eL38"
                     /note="60S ribosomal protein L38"
                     /calculated_mol_wt=8087
     Region          2..68
                     /region_name="Ribosomal_L38e"
                     /note="Ribosomal L38e protein family; pfam01781"
                     /db_xref="CDD:460326"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (P63174.2)"
     Site            67
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63173; propagated from
                     UniProtKB/Swiss-Prot (P63174.2)"
     CDS             1..70
                     /gene="Rpl38"
                     /coded_by="NM_001077592.1:52..264"
                     /db_xref="GeneID:689284"
                     /db_xref="RGD:1305573"
ORIGIN      
        1 mprkieeikd flltarrkda ksvkikknkd nvkfkvrcsr ylytlvitdk ekaeklkqsl
       61 ppglavkelk
//
LOCUS       NP_112275               1502 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family C member 6 [Rattus norvegicus].
ACCESSION   NP_112275
VERSION     NP_112275.1
DBSOURCE    REFSEQ: accession NM_031013.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1502)
  AUTHORS   Szeri,F., Niaziorimi,F., Donnelly,S., Orndorff,J. and van de
            Wetering,K.
  TITLE     Generation of fully functional fluorescent fusion proteins to gain
            insights into ABCC6 biology
  JOURNAL   FEBS Lett 595 (6), 799-810 (2021)
   PUBMED   33058196
REFERENCE   2  (residues 1 to 1502)
  AUTHORS   Li,Q., Kingman,J., van de Wetering,K., Tannouri,S., Sundberg,J.P.
            and Uitto,J.
  TITLE     Abcc6 Knockout Rat Model Highlights the Role of Liver in PPi
            Homeostasis in Pseudoxanthoma Elasticum
  JOURNAL   J Invest Dermatol 137 (5), 1025-1032 (2017)
   PUBMED   28111129
  REMARK    GeneRIF: This study suggests a critical role of hepatic ABCC6 in
            contributing to plasma inorganic pyrophosphate levels, identifying
            liver as a target of molecular correction to counteract ectopic
            mineralization in pseudoxanthoma elasticum
REFERENCE   3  (residues 1 to 1502)
  AUTHORS   Jansen,R.S., Duijst,S., Mahakena,S., Sommer,D., Szeri,F.,
            Varadi,A., Plomp,A., Bergen,A.A., Oude Elferink,R.P., Borst,P. and
            van de Wetering,K.
  TITLE     ABCC6-mediated ATP secretion by the liver is the main source of the
            mineralization inhibitor inorganic pyrophosphate in the systemic
            circulation-brief report
  JOURNAL   Arterioscler Thromb Vasc Biol 34 (9), 1985-1989 (2014)
   PUBMED   24969777
  REMARK    GeneRIF: In the absence of transfected rat ABCC6, HeLa and HEK293
            cells released almost no ATP, but on induction of rat ABCC6, they
            released substantial amounts of ATP into the cell culture medium.
REFERENCE   4  (residues 1 to 1502)
  AUTHORS   Lau,W.L., Liu,S. and Vaziri,N.D.
  TITLE     Chronic kidney disease results in deficiency of ABCC6, the novel
            inhibitor of vascular calcification
  JOURNAL   Am J Nephrol 40 (1), 51-55 (2014)
   PUBMED   24994603
  REMARK    GeneRIF: In a rat model of CKD, ABCC6 protein expression was
            decreased in liver and kidney, however mRNA levels were unchanged.
REFERENCE   5  (residues 1 to 1502)
  AUTHORS   Hanafy,S., El-Kadi,A.O. and Jamali,F.
  TITLE     Effect of inflammation on molecular targets and drug transporters
  JOURNAL   J Pharm Pharm Sci 15 (3), 361-375 (2012)
   PUBMED   22974786
REFERENCE   6  (residues 1 to 1502)
  AUTHORS   Cai,L., Lumsden,A., Guenther,U.P., Neldner,S.A., Zach,S.,
            Knoblauch,H., Ramesar,R., Hohl,D., Callen,D.F., Neldner,K.H.,
            Lindpaintner,K., Richards,R.I. and Struk,B.
  TITLE     A novel Q378X mutation exists in the transmembrane transporter
            protein ABCC6 and its pseudogene: implications for mutation
            analysis in pseudoxanthoma elasticum
  JOURNAL   J Mol Med (Berl) 79 (9), 536-546 (2001)
   PUBMED   11692167
REFERENCE   7  (residues 1 to 1502)
  AUTHORS   Ringpfeil,F., Pulkkinen,L. and Uitto,J.
  TITLE     Molecular genetics of pseudoxanthoma elasticum
  JOURNAL   Exp Dermatol 10 (4), 221-228 (2001)
   PUBMED   11493310
  REMARK    Review article
REFERENCE   8  (residues 1 to 1502)
  AUTHORS   Bergen,A.A., Plomp,A.S., Schuurman,E.J., Terry,S., Breuning,M.,
            Dauwerse,H., Swart,J., Kool,M., van Soest,S., Baas,F., ten
            Brink,J.B. and de Jong,P.T.
  TITLE     Mutations in ABCC6 cause pseudoxanthoma elasticum
  JOURNAL   Nat Genet 25 (2), 228-231 (2000)
   PUBMED   10835643
REFERENCE   9  (residues 1 to 1502)
  AUTHORS   Madon,J., Hagenbuch,B., Landmann,L., Meier,P.J. and Stieger,B.
  TITLE     Transport function and hepatocellular localization of mrp6 in rat
            liver
  JOURNAL   Mol Pharmacol 57 (3), 634-641 (2000)
   PUBMED   10692506
REFERENCE   10 (residues 1 to 1502)
  AUTHORS   Hirohashi,T., Suzuki,H., Ito,K., Ogawa,K., Kume,K., Shimizu,T. and
            Sugiyama,Y.
  TITLE     Hepatic expression of multidrug resistance-associated protein-like
            proteins maintained in eisai hyperbilirubinemic rats
  JOURNAL   Mol Pharmacol 53 (6), 1068-1075 (1998)
   PUBMED   9614210
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U73038.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U73038.1, AB010466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1502
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1502
                     /product="ATP-binding cassette sub-family C member 6"
                     /EC_number="7.6.2.3"
                     /note="multidrug resistance-associated protein 6; MLP-1;
                     MRP-like protein 1; ATP-binding cassette, sub-family C
                     (CFTR/MRP), member 6; liver multidrug
                     resistance-associated protein 6; ATP-binding cassette,
                     subfamily C (CFTR/MRP), member 6"
                     /calculated_mol_wt=164865
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88269.1)"
     Region          36..1501
                     /region_name="MRP_assoc_pro"
                     /note="multi drug resistance-associated protein (MRP);
                     TIGR00957"
                     /db_xref="CDD:188098"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            138..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            301..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            348..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            425..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            449..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            532..552
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            575..595
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Region          854..909
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88269.1)"
     Site            939..959
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            997..1017
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            1061..1081
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            1083..1103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            1175..1195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            1198..1218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88269.1)"
     Site            1285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95255; propagated from
                     UniProtKB/Swiss-Prot (O88269.1)"
     CDS             1..1502
                     /gene="Abcc6"
                     /gene_synonym="Mrp6"
                     /coded_by="NM_031013.1:72..4580"
                     /db_xref="GeneID:81642"
                     /db_xref="RGD:620268"
ORIGIN      
        1 mngehsmatp gescaglrvw nqteqepvay hllnlcflra agswvppmyl wvlgpiylly
       61 ihrhgccylr msrlfkikmv lgfalillyt fnaavplwri hrgmpqapel lihptvwltt
      121 msfatflihm erkkgvrasg llfgywllcc lvpaidtvqq asagsfrqep lhhlatylcl
      181 slvvaelvls clvdqppffs edskplnpcp eaeasfpska mfwwasgllw kgyrkllgpk
      241 dlwslerens seelvsqler ewrrnfselp ghkghsgmgt peteaflqpe rsqrgpllra
      301 iwrvfrstfl lgtlslvisd afrfavpkll slflefmgdl essawtgwll avlmflsacl
      361 qtlfeqqymy rvkvlqmrlr taitglvyrk vlvlssgsrk ssaagdvvnl vsvdvqrlve
      421 silhlnglwl lflwiivcfv ylwqllgpsa ltavavflsl lplnffitkk rsfhqeeqmr
      481 qkasrarlts smlrtvrtik shgwecafle rllhirgqel galktsaflf svslvsfqvs
      541 tflvalvvfa vhtlvaedna mdaekafvtl tvlsilnkaq aflpfsvhcl vqarvsfdrl
      601 aaflcleevd pngmvlspsr csskdrisih ngtfawsqes ppclhginlt vpqgcllavv
      661 gpvgagkssl lsallgellk vegsvsiegs vayvpqeawv qntsvvenvc frqeldlpwl
      721 qevleacalg sdvasfpagv htpvgeqgmn lsggqkqrls laravyrraa vylmddplaa
      781 ldahvsqevf kqvigpsgll qgttrilvth tlhvlpqadq ilvlangtia emgsyqdllh
      841 rngalvglld garqpagege geahaaatsd dlggfsgggt ptrrperprp sdaapvkgst
      901 seaqmepsld dvevtgltag edsvqygrvk satylsylra vgtplctytl flflcqqvas
      961 fcqgywlslw addpvvdgkq mhsalrgsif gllgclqaig lfasmaavfl ggarascllf
     1021 rsllwdvars pigffertpv gnllnrfske tdivdvdipd kmrtlltyaf gllevglavs
     1081 matplaivai lplmllyagf qslyvatccq lrrlesasys svcshlaetf qgsqvvrafq
     1141 aqgpftaqhd almdenqris fprlvadrwl aanlellgng lvfvaatcav lskahlsagl
     1201 agfsvsaalq vtqtlqwvvr swtdlensmv avervqdyvh tpkeapwrlp ssaaqplwpc
     1261 ggqiefrdfg lrhrpelpma vqgvslkiha gekvgivgrt gagkssltwg llrlqeateg
     1321 giwidgvpit dmglhtlrsr itiipqdpvl fpgslrmnld llqentdegi waaletvqlk
     1381 afvtslpgql qyecsgqgdd lsvgqkqllc larallrktq ilildeatas vdpgteiqmq
     1441 aalerwfaqc tvlliahrlr svmncarvlv mdegqvaesg spaqllaqkg lfyrlaqesg
     1501 la
//
LOCUS       NP_036623                562 aa            linear   ROD 27-APR-2025
DEFINITION  beta-adducin isoform b [Rattus norvegicus].
ACCESSION   NP_036623 XP_342716
VERSION     NP_036623.1
DBSOURCE    REFSEQ: accession NM_012491.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Engmann,O., Giralt,A., Gervasi,N., Marion-Poll,L., Gasmi,L.,
            Filhol,O., Picciotto,M.R., Gilligan,D., Greengard,P., Nairn,A.C.,
            Herve,D. and Girault,J.A.
  TITLE     DARPP-32 interaction with adducin may mediate rapid environmental
            effects on striatal neurons
  JOURNAL   Nat Commun 6, 10099 (2015)
   PUBMED   26639316
  REMARK    GeneRIF: Darpp32 interaction with beta-adducin may be the molecular
            pathway by which environmental changes may rapidly alter
            responsiveness of striatal neurons involved in the reward system.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Xu,T., Liu,W., Yang,C., Ba,X., Wang,X., Jiang,Y. and Zeng,X.
  TITLE     Lipid raft-associated beta-adducin is required for PSGL-1-mediated
            neutrophil rolling on P-selectin
  JOURNAL   J Leukoc Biol 97 (2), 297-306 (2015)
   PUBMED   25425738
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Valencia,D.M., Naranjo,C.A., Parra,M.V., Caro,M.A., Valencia,A.V.,
            Jaramillo,C.J. and Bedoya,G.
  TITLE     [Association and interaction of AGT, AGTR1, ACE, ADRB2, DRD1, ADD1,
            ADD2, ATP2B1, TBXA2R and PTGS2 genes on the risk of hypertension in
            Antioquian population]
  JOURNAL   Biomedica 33 (4), 598-614 (2013)
   PUBMED   24652215
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Bednarek,E. and Caroni,P.
  TITLE     beta-Adducin is required for stable assembly of new synapses and
            improved memory upon environmental enrichment
  JOURNAL   Neuron 69 (6), 1132-1146 (2011)
   PUBMED   21435558
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Sonoyama,K., Greenstein,A.S., Micheletti,R., Ferrari,P.,
            Schiavone,A., Aghamohammadzadeh,R., Withers,S.B., Tripodi,G.,
            Ferrandi,M. and Heagerty,A.M.
  TITLE     Mutation in the beta adducin subunit causes tissue-specific damage
            to myogenic tone
  JOURNAL   J Hypertens 29 (3), 466-474 (2011)
   PUBMED   21150638
  REMARK    GeneRIF: Mutations in the beta subunit of the adducin protein
            result in damage to renal artery myogenic tone and this is
            associated with renal damage as manifest by proteinuria.
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Kuhlman,P.A., Hughes,C.A., Bennett,V. and Fowler,V.M.
  TITLE     A new function for adducin. Calcium/calmodulin-regulated capping of
            the barbed ends of actin filaments
  JOURNAL   J Biol Chem 271 (14), 7986-7991 (1996)
   PUBMED   8626479
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Tripodi,G., Piscone,A., Borsani,G., Tisminetzky,S., Salardi,S.,
            Sidoli,A., James,P., Pongor,S., Bianchi,G. and Baralle,F.E.
  TITLE     Molecular cloning of an adducin-like protein: evidence of a
            polymorphism in the normotensive and hypertensive rats of the Milan
            strain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 939-947 (1991)
   PUBMED   2059221
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M63894.1, EV762188.1 and BE121149.1.
            
            On Jan 11, 2004 this sequence version replaced XP_342716.1.
            
            Transcript Variant: This variant (2) contains a distinct 3' UTR and
            lacks a portion of the 3' coding region, compared to variant 1. The
            resulting isoform (b) has a shorter, unique C-terminus when
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: M63894.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN06680412, SAMN06680413 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..562
                     /product="beta-adducin isoform b"
                     /note="adducin-63; erythrocyte adducin subunit beta;
                     adducin beta; adducin 2 (beta); beta-adducin"
                     /calculated_mol_wt=62657
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35612; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Region          130..379
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(139,143,155,176,178..179,229,231..232,237..239,247,
                     249..250,261,289,300,307,311,318,336)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(160,173..174,199..201,227,229,290)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(227,229,290)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Region          425..444
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05764.4)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (Q05764.4)"
     CDS             1..562
                     /gene="Add2"
                     /gene_synonym="beta-ADD"
                     /coded_by="NM_012491.2:188..1876"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:24171"
                     /db_xref="RGD:2042"
ORIGIN      
        1 msedtvpeaa spppsqgqhy fdrfseddpe ylrlrnraad lrqdfnlmeq kkrvtmilqs
       61 psfreelegl iqeqmkkgnn ssniwalrqi adfmastsha vfpassmnfs mmtpindlht
      121 adslnlakge rlmrckissv yrlldlygwa qlsdtyvtlr vskeqdhfli spkgvscsev
      181 tasslikvni lgevvekgss cfpvdttgfs lhsaiyaarp dvrcaihlht pataavsamk
      241 cgllpvshna llvgdmayyd fngemeqead rinlqkclgp tckilvlrnh gmvalgdtve
      301 eafykvfhlq aacevqvsal ssaggtenli lleqekhrph evgsvqwags tfgpmqksrl
      361 gehefealmr mldnlgyrtg ytyrhpfvqe ktkhksevei patvtafvfe edgvpvpalr
      421 qhaqkqqkek trwlntpnty lrvnvadevq rnmgsprpkt twmkadevek sssgmpirie
      481 npnqfvplyt dpqevldmrn kireqnrqdi ksagpqsqll asviaeksrs pvqqrlppte
      541 geayqtpgag qgtpessgpl tp
//
LOCUS       NP_001014063             391 aa            linear   ROD 27-APR-2025
DEFINITION  terminal nucleotidyltransferase 5C [Rattus norvegicus].
ACCESSION   NP_001014063 XP_227541
VERSION     NP_001014063.1
DBSOURCE    REFSEQ: accession NM_001014041.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Mroczek,S., Chlebowska,J., Kulinski,T.M., Gewartowska,O.,
            Gruchota,J., Cysewski,D., Liudkovska,V., Borsuk,E., Nowis,D. and
            Dziembowski,A.
  TITLE     The non-canonical poly(A) polymerase FAM46C acts as an
            onco-suppressor in multiple myeloma
  JOURNAL   Nat Commun 8 (1), 619 (2017)
   PUBMED   28931820
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083570.1.
            
            On Apr 20, 2005 this sequence version replaced XP_227541.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083570.1, FQ182982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..391
                     /product="terminal nucleotidyltransferase 5C"
                     /EC_number="2.7.7.19"
                     /note="protein FAM46C; putative nucleotidyltransferase
                     FAM46C; family with sequence similarity 46, member C"
                     /calculated_mol_wt=44668
     Region          17..334
                     /region_name="NTP_transf_7"
                     /note="Nucleotidyltransferase; pfam07984"
                     /db_xref="CDD:462329"
     CDS             1..391
                     /gene="Tent5c"
                     /gene_synonym="Fam46c"
                     /coded_by="NM_001014041.1:260..1435"
                     /db_xref="GeneID:310721"
                     /db_xref="RGD:1359446"
ORIGIN      
        1 madegsstkd sesfsvlnwd qvsrlhevlt evvpihgrgn fptleitlkd ivqtvrsrle
       61 eagikvqdvr lngsaaghvl vkdnglgckd ldlifhvalp teaefqlvrd vvlcsllnfl
      121 pegvnklkis pvtlkeayvq klvkvctdtd rwslislsnk ngrnvelkfv dsirrqfefs
      181 vdsfqiilds llffydcssn pvsehfhptv vgesmygdfe eafdhlqnrl iatknpeeir
      241 gggllkysnl lvrdfrpadq eeiktlerym csrffidfpd ileqqrklet ylqnhfadee
      301 rskydylmil rrvvnestvc lmgherrqtl nlisllalrv laeqniipsa tnvtcyyqpa
      361 pyvsdgnfnn yyiahppvty sqpyptwlpc n
//
LOCUS       NP_114012                737 aa            linear   ROD 27-APR-2025
DEFINITION  transcriptional repressor CTCF [Rattus norvegicus].
ACCESSION   NP_114012
VERSION     NP_114012.1
DBSOURCE    REFSEQ: accession NM_031824.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Shen,J., Han,Q., Li,W., Chen,X., Lu,J., Zheng,J. and Xue,S.
  TITLE     miR-383-5p Regulated by the Transcription Factor CTCF Affects
            Neuronal Impairment in Cerebral Ischemia by Mediating Deacetylase
            HDAC9 Activity
  JOURNAL   Mol Neurobiol 59 (10), 6307-6320 (2022)
   PUBMED   35927544
  REMARK    GeneRIF: miR-383-5p Regulated by the Transcription Factor CTCF
            Affects Neuronal Impairment in Cerebral Ischemia by Mediating
            Deacetylase HDAC9 Activity.
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Wang,D., Lin,B., Zhang,W. and Wang,X.
  TITLE     Up-regulation of SNHG16 induced by CTCF accelerates cardiac
            hypertrophy by targeting miR-182-5p/IGF1 axis
  JOURNAL   Cell Biol Int 44 (7), 1426-1435 (2020)
   PUBMED   32125046
  REMARK    GeneRIF: Up-regulation of SNHG16 induced by CTCF accelerates
            cardiac hypertrophy by targeting miR-182-5p/IGF1 axis.
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Akhtar,M.S., Akhter,N., Najm,M.Z., Deo,S.V.S., Shukla,N.K.,
            Almalki,S.S.R., Alharbi,R.A., Sindi,A.A.A., Alruwetei,A., Ahmad,A.
            and Husain,S.A.
  TITLE     Association of mutation and low expression of the CTCF gene with
            breast cancer progression
  JOURNAL   Saudi Pharm J 28 (5), 607-614 (2020)
   PUBMED   32435142
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Lupey-Green,L.N., Caruso,L.B., Madzo,J., Martin,K.A., Tan,Y.,
            Hulse,M. and Tempera,I.
  TITLE     PARP1 Stabilizes CTCF Binding and Chromatin Structure To Maintain
            Epstein-Barr Virus Latency Type
  JOURNAL   J Virol 92 (18), e00755-18 (2018)
   PUBMED   29976663
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Chao,W., Huynh,K.D., Spencer,R.J., Davidow,L.S. and Lee,J.T.
  TITLE     CTCF, a candidate trans-acting factor for X-inactivation choice
  JOURNAL   Science 295 (5553), 345-347 (2002)
   PUBMED   11743158
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Yang,Y., Quitschke,W.W., Vostrov,A.A. and Brewer,G.J.
  TITLE     CTCF is essential for up-regulating expression from the amyloid
            precursor protein promoter during differentiation of primary
            hippocampal neurons
  JOURNAL   J Neurochem 73 (6), 2286-2298 (1999)
   PUBMED   10582586
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Filippova,G.N., Lindblom,A., Meincke,L.J., Klenova,E.M.,
            Neiman,P.E., Collins,S.J., Doggett,N.A. and Lobanenkov,V.V.
  TITLE     A widely expressed transcription factor with multiple DNA sequence
            specificity, CTCF, is localized at chromosome segment 16q22.1
            within one of the smallest regions of overlap for common deletions
            in breast and prostate cancers
  JOURNAL   Genes Chromosomes Cancer 22 (1), 26-36 (1998)
   PUBMED   9591631
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Vostrov,A.A. and Quitschke,W.W.
  TITLE     The zinc finger protein CTCF binds to the APBbeta domain of the
            amyloid beta-protein precursor promoter. Evidence for a role in
            transcriptional activation
  JOURNAL   J Biol Chem 272 (52), 33353-33359 (1997)
   PUBMED   9407128
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Filippova,G.N., Fagerlie,S., Klenova,E.M., Myers,C., Dehner,Y.,
            Goodwin,G., Neiman,P.E., Collins,S.J. and Lobanenkov,V.V.
  TITLE     An exceptionally conserved transcriptional repressor, CTCF, employs
            different combinations of zinc fingers to bind diverged promoter
            sequences of avian and mammalian c-myc oncogenes
  JOURNAL   Mol Cell Biol 16 (6), 2802-2813 (1996)
   PUBMED   8649389
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF133731.2.
            
            Sequence Note: This sequence has been modified as follows: removed
            36 bp suspected to be vector contamination from the 5' end.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF133731.2 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Rattus norvegicus"
                     /strain="Copenhagen"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..737
                     /product="transcriptional repressor CTCF"
                     /note="CTCFL paralog; 11-zinc finger protein;
                     CCCTC-binding factor (zinc finger protein)"
                     /calculated_mol_wt=83749
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          180..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          266..289
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(273,275,277,279..280,283..284,287,301,303,307..308,
                     311..312,315,329,331,333,335..336,339..340,346)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          280..305
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..333
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          324..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..375
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <366..500
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          409..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,488,502,504,508..509,
                     512..513,516,530,532,534,536..537,540..541,545)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          509..534
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          525..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          573..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49711; propagated from
                     UniProtKB/Swiss-Prot (Q9R1D1.1)"
     Region          699..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1D1.1)"
     CDS             1..737
                     /gene="Ctcf"
                     /coded_by="NM_031824.1:169..2382"
                     /db_xref="GeneID:83726"
                     /db_xref="RGD:621344"
ORIGIN      
        1 megeaveaiv eesetfikgk erktyqrrre ggqeedachl pqnqtdggev vqdvnssvqm
       61 vmmeqldptl lqmktevmeg tvapeaeaav ddtqiitlqv vnmeeqpini gelqlvqvpv
      121 pvtvpvatts veelqgayen evskeglaes epmichtlpl pegfqvvkvg angevetleq
      181 gelppqedps wqkdpdyqpp akktkktkks klryteegkd vdvsvydfee eqqegllsev
      241 naekvvgnmk ppkptkikkk gvkktfqcel csytcprrsn ldrhmkshtd erphkchlcg
      301 rafrtvtllr nhlnthtgtr phkcpdcdma fvtsgelvrh rrykhthekp fkcsmcdyas
      361 vevsklkrhi rshtgerpfq cslcsyasrd tyklkrhmrt hsgekpyecy icharftqsg
      421 tmkmhilqkh tenvakfhcp hcdtviarks dlgvhlrkqh syieqgkkcr ycdavfhery
      481 aliqhqkshk nekrfkcdqc dyacrqerhm imhkrthtge kpyacshcdk tfrqkqlldm
      541 hfkryhdpnf vpaafvcskc gktftrrntm arhadncagp dgvegengge tkkskrgrkr
      601 kmrskkedss dsenaepdld dneeeeepav eiepepepqp qpqpqpqpqp vapapppakk
      661 rrgrppgrtn qpkqnqptai iqvedqntga ieniivevkk epdaepaege eeeaqaapad
      721 apngdltpem ilsmmdr
//
LOCUS       NP_942045                588 aa            linear   ROD 27-APR-2025
DEFINITION  cryptochrome-1 [Rattus norvegicus].
ACCESSION   NP_942045 XP_216868
VERSION     NP_942045.2
DBSOURCE    REFSEQ: accession NM_198750.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Peng,J., Zhao,J., Tang,Q., Wang,J., Song,W., Lu,X., Huang,X.,
            Chen,G., Zheng,W., Zhang,L., Han,Y., Yan,C., Wan,Q. and Chen,L.
  TITLE     Low intensity near-infrared light promotes bone regeneration via
            circadian clock protein cryptochrome 1
  JOURNAL   Int J Oral Sci 14 (1), 53 (2022)
   PUBMED   36376275
  REMARK    GeneRIF: Low intensity near-infrared light promotes bone
            regeneration via circadian clock protein cryptochrome 1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Toledo,M., Batista-Gonzalez,A., Merheb,E., Aoun,M.L., Tarabra,E.,
            Feng,D., Sarparanta,J., Merlo,P., Botre,F., Schwartz,G.J.,
            Pessin,J.E. and Singh,R.
  TITLE     Autophagy Regulates the Liver Clock and Glucose Metabolism by
            Degrading CRY1
  JOURNAL   Cell Metab 28 (2), 268-281 (2018)
   PUBMED   29937374
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Wong,J.C.Y., Smyllie,N.J., Banks,G.T., Pothecary,C.A.,
            Barnard,A.R., Maywood,E.S., Jagannath,A., Hughes,S., van der
            Horst,G.T.J., MacLaren,R.E., Hankins,M.W., Hastings,M.H.,
            Nolan,P.M., Foster,R.G. and Peirson,S.N.
  TITLE     Differential roles for cryptochromes in the mammalian retinal clock
  JOURNAL   FASEB J 32 (8), 4302-4314 (2018)
   PUBMED   29561690
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Mavroudis,P.D., DuBois,D.C., Almon,R.R. and Jusko,W.J.
  TITLE     Modeling circadian variability of core-clock and clock-controlled
            genes in four tissues of the rat
  JOURNAL   PLoS One 13 (6), e0197534 (2018)
   PUBMED   29894471
  REMARK    GeneRIF: The model efficiently described the synchronous
            rhythmicity of core-clock genes and further predicted that their
            phases are mainly regulated by Per2 and Cry1 transcriptional delays
            and Rev-Erba and Cry1 degradation rates.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Tong,X., Zhang,D., Charney,N., Jin,E., VanDommelen,K., Stamper,K.,
            Gupta,N., Saldate,J. and Yin,L.
  TITLE     DDB1-Mediated CRY1 Degradation Promotes FOXO1-Driven
            Gluconeogenesis in Liver
  JOURNAL   Diabetes 66 (10), 2571-2582 (2017)
   PUBMED   28790135
  REMARK    Erratum:[Diabetes. 2017 Dec;66(12):3144. doi: 10.2337/db17-er12e.
            PMID: 28993340]
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Kume,K., Zylka,M.J., Sriram,S., Shearman,L.P., Weaver,D.R., Jin,X.,
            Maywood,E.S., Hastings,M.H. and Reppert,S.M.
  TITLE     mCRY1 and mCRY2 are essential components of the negative limb of
            the circadian clock feedback loop
  JOURNAL   Cell 98 (2), 193-205 (1999)
   PUBMED   10428031
REFERENCE   7  (residues 1 to 588)
  AUTHORS   van der Horst,G.T., Muijtjens,M., Kobayashi,K., Takano,R.,
            Kanno,S., Takao,M., de Wit,J., Verkerk,A., Eker,A.P., van
            Leenen,D., Buijs,R., Bootsma,D., Hoeijmakers,J.H. and Yasui,A.
  TITLE     Mammalian Cry1 and Cry2 are essential for maintenance of circadian
            rhythms
  JOURNAL   Nature 398 (6728), 627-630 (1999)
   PUBMED   10217146
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Kobayashi,K., Kanno,S., Smit,B., van der Horst,G.T., Takao,M. and
            Yasui,A.
  TITLE     Characterization of photolyase/blue-light receptor homologs in
            mouse and human cells
  JOURNAL   Nucleic Acids Res 26 (22), 5086-5092 (1998)
   PUBMED   9801304
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Zhao,S. and Sancar,A.
  TITLE     Human blue-light photoreceptor hCRY2 specifically interacts with
            protein serine/threonine phosphatase 5 and modulates its activity
  JOURNAL   Photochem Photobiol 66 (5), 727-731 (1997)
   PUBMED   9383998
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Hsu,D.S., Zhao,X., Zhao,S., Kazantsev,A., Wang,R.P., Todo,T.,
            Wei,Y.F. and Sancar,A.
  TITLE     Putative human blue-light photoreceptors hCRY1 and hCRY2 are
            flavoproteins
  JOURNAL   Biochemistry 35 (44), 13871-13877 (1996)
   PUBMED   8909283
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107677.1.
            
            On Nov 6, 2005 this sequence version replaced NP_942045.1.
            
            Summary: This gene encodes a flavin adenine dinucleotide-binding
            protein that is a key component of the circadian core oscillator
            complex, which regulates the circadian clock. This gene is
            upregulated by Clock/Arntl heterodimers but then represses this
            upregulation in a feedback loop using Per/Cry heterodimers to
            interact with Clock/Arntl. Polymorphisms in this gene have been
            associated with altered sleep patterns. The encoded protein is
            widely conserved across plants and animals. Loss of the related
            gene in mouse results in a shortened circadian cycle in complete
            darkness. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107677.1, AF545855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..588
                     /product="cryptochrome-1"
                     /note="cryptochrome 1 (photolyase-like); cryptochrome
                     circadian clock 1"
                     /calculated_mol_wt=66100
     Region          5..487
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
     Region          50..54
                     /region_name="LIR 1.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          82..87
                     /region_name="LIR 2.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          151..156
                     /region_name="LIR 3.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          255..260
                     /region_name="LIR 4.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          271..276
                     /region_name="LIR 5.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          285..290
                     /region_name="LIR 6.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          335..339
                     /region_name="LIR 7.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          371..470
                     /region_name="Required for inhibition of
                     CLOCK-BMAL1-mediated transcription.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          379..384
                     /region_name="LIR 8.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          395..400
                     /region_name="LIR 9.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          411..416
                     /region_name="LIR 10.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          430..435
                     /region_name="LIR 11.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          471..493
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          486..491
                     /region_name="LIR 12.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          492..497
                     /region_name="LIR 13.
                     /evidence=ECO:0000250|UniProtKB:P97784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Region          511..588
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32Q86.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q32Q86.1)"
     CDS             1..588
                     /gene="Cry1"
                     /coded_by="NM_198750.2:537..2303"
                     /db_xref="GeneID:299691"
                     /db_xref="RGD:735083"
ORIGIN      
        1 mgvnavhwfr kglrlhdnpa lkeciqgadt ircvyildpw fagssnvgin rwrfllqcle
       61 dldanlrkln srlfvirgqp advfprlfke wnitklsiey dsepfgkerd aaikklatea
      121 gvevivrish tlydldkiie lnggqpplty krfqtlvskm eplempadti tsdvigkctt
      181 plsddhdeky gvpsleelgf dtdglssavw pggetealtr lerhlerkaw vanferprmn
      241 ansllasptg lspylrfgcl scrlfyfklt dlykkvkkns spplslygql lwreffytaa
      301 tnnprfdkme gnpicvqipw dknpealakw aegrtgfpwi daimtqlrqe gwihhlarha
      361 vacfltrgdl wisweegmkv feellldadw sinagswmwl scssffqqff hcycpvgfgr
      421 rtdpngdyir rylpvlrgfp akyiydpwna pegiqkvakc ligvnypkpm vnhaeasrln
      481 iermkqiyqq lsryrglgll asvpsnpngn gglmgyapge nvpsggsggg ncsqgsgilh
      541 yahgdsqqtn plkqgrssmg tglssgkrps qeedaqsvgp kvqrqssn
//
LOCUS       NP_001032865             311 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 177 [Rattus norvegicus].
ACCESSION   NP_001032865 XP_222563
VERSION     NP_001032865.1
DBSOURCE    REFSEQ: accession NM_001037776.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lorenzi,I., Oeljeklaus,S., Aich,A., Ronsor,C., Callegari,S.,
            Dudek,J., Warscheid,B., Dennerlein,S. and Rehling,P.
  TITLE     The mitochondrial TMEM177 associates with COX20 during COX2
            biogenesis
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (2), 323-333 (2018)
   PUBMED   29154948
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098688.1.
            
            On Dec 16, 2005 this sequence version replaced XP_222563.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098688.1, EX491701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q11"
     Protein         1..311
                     /product="transmembrane protein 177"
                     /calculated_mol_wt=33870
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM93.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM93.1)"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM93.1)"
     CDS             1..311
                     /gene="Tmem177"
                     /gene_synonym="RGD1310320"
                     /coded_by="NM_001037776.1:236..1171"
                     /db_xref="GeneID:304735"
                     /db_xref="RGD:1310320"
ORIGIN      
        1 magplwraav fiqrhrtsll vgscvglfgv qisfhlfpdp ivqwlyqywp qgqpaplspq
       61 lrslfqevlk digvpsghcy kpftaftfqp vsagfpqlpa gavvgipaif lgglvtnidh
      121 tvvihgqkvd wqspagtrlr daltlshdaq kfalakevvy lesgmaalqt lpapvclagt
      181 waisvgakha lglyggpmsl raafnlvaiv vgyvayafsk dsltvalegw ldhrtaslsa
      241 ayvrggvefy ekilsgnlal rsllgrqgek lytpsgnivp rhwfrinhlp yttrrdsllq
      301 mwrakvspgh f
//
LOCUS       NP_001014117             776 aa            linear   ROD 27-APR-2025
DEFINITION  cilium assembly protein DZIP1L [Rattus norvegicus].
ACCESSION   NP_001014117 XP_236602
VERSION     NP_001014117.1
DBSOURCE    REFSEQ: accession NM_001014095.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Wang,C., Li,J., Takemaru,K.I., Jiang,X., Xu,G. and Wang,B.
  TITLE     Centrosomal protein Dzip1l binds Cby, promotes ciliary bud
            formation, and acts redundantly with Bromi to regulate ciliogenesis
            in the mouse
  JOURNAL   Development 145 (6) (2018)
   PUBMED   29487109
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Lu,H., Galeano,M.C.R., Ott,E., Kaeslin,G., Kausalya,P.J.,
            Kramer,C., Ortiz-Bruchle,N., Hilger,N., Metzis,V., Hiersche,M.,
            Tay,S.Y., Tunningley,R., Vij,S., Courtney,A.D., Whittle,B.,
            Wuhl,E., Vester,U., Hartleben,B., Neuber,S., Frank,V., Little,M.H.,
            Epting,D., Papathanasiou,P., Perkins,A.C., Wright,G.D.,
            Hunziker,W., Gee,H.Y., Otto,E.A., Zerres,K., Hildebrandt,F.,
            Roy,S., Wicking,C. and Bergmann,C.
  TITLE     Mutations in DZIP1L, which encodes a ciliary-transition-zone
            protein, cause autosomal recessive polycystic kidney disease
  JOURNAL   Nat Genet 49 (7), 1025-1034 (2017)
   PUBMED   28530676
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Glazer,A.M., Wilkinson,A.W., Backer,C.B., Lapan,S.W., Gutzman,J.H.,
            Cheeseman,I.M. and Reddien,P.W.
  TITLE     The Zn finger protein Iguana impacts Hedgehog signaling by
            promoting ciliogenesis
  JOURNAL   Dev Biol 337 (1), 148-156 (2010)
   PUBMED   19852954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083786.1.
            
            On Apr 20, 2005 this sequence version replaced XP_236602.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083786.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676785
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..776
                     /product="cilium assembly protein DZIP1L"
                     /note="zinc finger protein DZIP1L; DAZ-interacting protein
                     1-like protein; DAZ interacting protein 1-like"
                     /calculated_mol_wt=87894
     Region          24..144
                     /region_name="Dzip-like_N"
                     /note="Iguana/Dzip1-like DAZ-interacting protein
                     N-terminal; pfam13815"
                     /db_xref="CDD:433498"
     Region          <110..>392
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q499E4; propagated from
                     UniProtKB/Swiss-Prot (Q5XIA0.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q499E4; propagated from
                     UniProtKB/Swiss-Prot (Q5XIA0.1)"
     Region          <511..>666
                     /region_name="PTZ00249"
                     /note="variable surface protein Vir28; Provisional"
                     /db_xref="CDD:140276"
     Region          520..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIA0.1)"
     CDS             1..776
                     /gene="Dzip1l"
                     /gene_synonym="RGD1311430"
                     /coded_by="NM_001014095.1:110..2440"
                     /db_xref="GeneID:315952"
                     /db_xref="RGD:1311430"
ORIGIN      
        1 mqysvatadg lsgppsgayt lptfkfqprr esidwrrisa vdvdrvarel dvatlqenia
       61 gvtfcnldre vcnhcrqpvd pvllkvlrla qliieyllhc qdclsasvaq learlqaslg
      121 qqqrgqqelg rqadelkgvr eesrrrrkmi stlqqlllqt gahsyhtchl cdktfmnatf
      181 lrghiqrrha gmaevgkqkq eqqlgevlee lraklkwtqg eleaqreaer qrqaqelemi
      241 rqreieakkk fdewkekers klygeidklk qlfwdefktv anqnstleek lkvlqsysmt
      301 eshlgslrde eseerlkhaq elqalrekmd iqktewkrkm kalheeraae rrqlqeener
      361 lhvtlsqdqk kaaaqsqrhi nalraqlqeq arliesqeet iqtlsfrrme evqevpkavv
      421 teedsseeel easleeqqeq rkvlaalrnn pawlkqfrpi ledtleekle gmgikrgtkg
      481 isaqtvrrle pllrtqreqt arsfreflsl reklnqevss rakkrwegta vvpqpdgqpp
      541 vksqrttlat revrpktrtl tvalpskpae pststprghs shgpgltqvs tpiprprvhg
      601 psstpvspgp glstppfsse eepegdvvqr vslqppkvlp rsapqpednw gwsdsetsee
      661 saqspgkgsd glassatlvq smvknlekql etpakkpsgg vnmflrpnta lqrsstpark
      721 tqlsedesdl eissledlsh dlgpkgkptp lshsklpekf daspwssgsr pripgw
//
LOCUS       NP_001128232             623 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein L isoform a [Rattus
            norvegicus].
ACCESSION   NP_001128232 XP_001068144 XP_001068191 XP_001074287 XP_001074316
VERSION     NP_001128232.1
DBSOURCE    REFSEQ: accession NM_001134760.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Atianand,M.K., Hu,W., Satpathy,A.T., Shen,Y., Ricci,E.P.,
            Alvarez-Dominguez,J.R., Bhatta,A., Schattgen,S.A., McGowan,J.D.,
            Blin,J., Braun,J.E., Gandhi,P., Moore,M.J., Chang,H.Y.,
            Lodish,H.F., Caffrey,D.R. and Fitzgerald,K.A.
  TITLE     A Long Noncoding RNA lincRNA-EPS Acts as a Transcriptional Brake to
            Restrain Inflammation
  JOURNAL   Cell 165 (7), 1672-1685 (2016)
   PUBMED   27315481
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Loh,T.J., Cho,S., Moon,H., Jang,H.N., Williams,D.R., Jung,D.W.,
            Kim,I.C., Ghigna,C., Biamonti,G., Zheng,X. and Shen,H.
  TITLE     hnRNP L inhibits CD44 V10 exon splicing through interacting with
            its upstream intron
  JOURNAL   Biochim Biophys Acta 1849 (6), 743-750 (2015)
   PUBMED   25623890
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Yau,W.Y., Shih,H.C., Tsai,M.H., Sheu,J.C., Chen,C.H. and Chow,L.P.
  TITLE     Autoantibody recognition of an N-terminal epitope of hnRNP L marks
            the risk for developing HBV-related hepatocellular carcinoma
  JOURNAL   J Proteomics 94, 346-358 (2013)
   PUBMED   24125732
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Costain,W.J. and Mishra,R.K.
  TITLE     PLG regulates hnRNP-L expression in the rat striatum and
            pre-frontal cortex: identification by ddPCR
  JOURNAL   Peptides 24 (1), 137-146 (2003)
   PUBMED   12576095
REFERENCE   7  (residues 1 to 623)
  AUTHORS   Kuninger,D.T., Izumi,T., Papaconstantinou,J. and Mitra,S.
  TITLE     Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like
            repressor element in the AP-endonuclease 1 promoter
  JOURNAL   Nucleic Acids Res 30 (3), 823-829 (2002)
   PUBMED   11809897
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Hamilton,B.J., Nichols,R.C., Tsukamoto,H., Boado,R.J.,
            Pardridge,W.M. and Rigby,W.F.
  TITLE     hnRNP A2 and hnRNP L bind the 3'UTR of glucose transporter 1 mRNA
            and exist as a complex in vivo
  JOURNAL   Biochem Biophys Res Commun 261 (3), 646-651 (1999)
   PUBMED   10441480
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Pinol-Roma,S., Swanson,M.S., Gall,J.G. and Dreyfuss,G.
  TITLE     A novel heterogeneous nuclear RNP protein with a unique
            distribution on nascent transcripts
  JOURNAL   J Cell Biol 109 (6 Pt 1), 2575-2587 (1989)
   PUBMED   2687284
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Sep 5, 2008 this sequence version replaced
            XP_001068191.1, XP_001068144.1, XP_001074316.1, XP_001074287.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.1453.1,
                                           SRR26643299.1857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..623
                     /product="heterogeneous nuclear ribonucleoprotein L
                     isoform a"
                     /note="heterogenous nuclear ribonucleoprotein L"
                     /calculated_mol_wt=67772
     Region          97..621
                     /region_name="hnRNP-L_PTB"
                     /note="hnRNP-L/PTB/hephaestus splicing factor family;
                     TIGR01649"
                     /db_xref="CDD:273733"
     CDS             1..623
                     /gene="Hnrnpl"
                     /gene_synonym="hnrnp-L; Hnrpl"
                     /coded_by="NM_001134760.1:1..1872"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:80846"
                     /db_xref="RGD:71059"
ORIGIN      
        1 msrrllprae krrrrleqrq qpdeqlrrag amvkmaaagg gggggryygg gneggrapkr
       61 lktenagdqh gggggggsga agggggenyd dphktpaspv vhirglidgv veadlvealq
      121 efgpisyvvv mpkkrqalve fedvlgacna vnyaadnqiy iaghpafvny stsqkisrpg
      181 dsddsrsvns vllftilnpi ysittdvlyt icnpcgpvqr ivifrkngvq amvefdsvqs
      241 aqrakaslng adiysgcctl kieyakptrl nvfkndqdtw dytnpnlsgq gdpgsnpnkr
      301 qrqppllgdh paeygegrgf psvdsrgsca parrpprkfs pvlplfpshp pggphggyhs
      361 hyhdegygpp pphyegrrmg ppvgghrrgp srygpqyghp pppppppdyg phadspvlmv
      421 ygldqskmnc drvfnvfcly gnvekvkfmk skpgaamvem adgyavdrai thlnnnfmfg
      481 qkmnvcvskq paimpgqsyg ledgscsykd fsesrnnrfs tpeqaaknri qhpsnvlhff
      541 naplevteen ffeicdelgv krptsvkvfs gksersssgl lewdsksdal etlgflnhyq
      601 mknpngpypy tlklcfstaq has
//
LOCUS       NP_001128212             995 aa            linear   ROD 27-APR-2025
DEFINITION  tudor domain-containing protein 5 [Rattus norvegicus].
ACCESSION   NP_001128212
VERSION     NP_001128212.1
DBSOURCE    REFSEQ: accession NM_001134740.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Pek,J.W., Anand,A. and Kai,T.
  TITLE     Tudor domain proteins in development
  JOURNAL   Development 139 (13), 2255-2266 (2012)
   PUBMED   22669818
  REMARK    Review article
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Yabuta,Y., Ohta,H., Abe,T., Kurimoto,K., Chuma,S. and Saitou,M.
  TITLE     TDRD5 is required for retrotransposon silencing, chromatoid body
            assembly, and spermiogenesis in mice
  JOURNAL   J Cell Biol 192 (5), 781-795 (2011)
   PUBMED   21383078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC168218.1.
            
            Summary: This gene encodes a member of the tudor domain-containing
            protein family. Tudor domain-containing proteins regulate a variety
            of processes including RNA metabolism, histone modification, and
            the DNA damage response. The tudor domain commonly functions to
            link methylated arginine or lysine marks to downstream effector
            proteins. In mouse, this gene is expressed in the primordial germ
            cells and in male germ cells during embryogenesis. In addition, it
            is expressed in adult testis cells where the protein is a component
            of the intermitochondrial cement and chromatoid bodies.
            Loss-of-function mutations in mouse result in arrest of
            spermatogenesis. [provided by RefSeq, Mar 2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168218.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..995
                     /product="tudor domain-containing protein 5"
                     /calculated_mol_wt=111197
     Region          4..98
                     /region_name="LOTUS_1_TDRD5"
                     /note="The first LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09985"
                     /db_xref="CDD:193599"
     Region          127..196
                     /region_name="LOTUS_2_TDRD5"
                     /note="The second LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09975"
                     /db_xref="CDD:193589"
     Region          292..365
                     /region_name="LOTUS_3_TDRD5"
                     /note="The third LOTUS domain on Tudor-containing protein
                     5 (TDRD5); cd09976"
                     /db_xref="CDD:193590"
     Region          484..601
                     /region_name="Tudor_TDRD5"
                     /note="Tudor domain found in Tudor domain-containing
                     protein 5 (TDRD5) and similar proteins; cd20419"
                     /db_xref="CDD:410490"
     Site            order(544,551,568,571,573)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410490"
     Region          747..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C4.1)"
     Region          857..892
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C4.1)"
     Region          911..960
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C4.1)"
     Site            946
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5VCS6; propagated from
                     UniProtKB/Swiss-Prot (B4F7C4.1)"
     CDS             1..995
                     /gene="Tdrd5"
                     /coded_by="NM_001134740.1:3..2990"
                     /db_xref="GeneID:289129"
                     /db_xref="RGD:1307078"
ORIGIN      
        1 mseqeriqdc lrkeirslli stkdgltpqq lekeyllmvg nhlplrilgy rstmelvldm
       61 pdvvsvcpcg dgtvilkaip destkgiasl vakqrrshkv rnsmqkgrss vcsgrvpyrg
      121 rvppilpavv kselkdllal spvllsdfek afarrfgrsf qymqygflsm fevlsaasdv
      181 icveqtrags lltlkksase ekqrewpagk iftqpfrmkq qgsystgfpv tktrfsqpis
      241 nmeppkqvls mekipmfntv easrlshtek lnqlestfks viaqigpggt vdpdlkhkik
      301 fvvskfpqgl fiskllgefe lvfkeqlspk qlgflnvtel vgalsdilrv efseekqdll
      361 vfdadlrpll pagplssvrn sclvqpdkri eanawassps rnslstvavk kttwdcplkn
      421 hkeaeqkayk kpnlvvkplq lqvetnksql slsmanhdip pdavrakklc rlppldtstl
      481 vgvfveyiis psqfyvriys rdsselledm miemrrcysn qlvsdryvmp eyfiqpghlc
      541 cvrisedkww yrviihrilg kkevevfypd fgnigtvqks slrflkccyt klpaqaipcs
      601 lawvrpaeeh wtskailhfq klcglkplvg vvdeyidgil niflcdtssn edvyfhhvlr
      661 teghaivcre napskgfrdf nppalytnss aapgdmvlte lghpaqqhyl nedgeilqqp
      721 qqdindeksi shlksvseel lkdsklgplk tresceeepq wsilkpkdpk eenedevptg
      781 mpclesvtig ddiwdenwlp lqakmgkagg pashlftssl vgkkqyqtrg ettrkdwcfs
      841 tskdiwddsw qplglandvk grthtpegpi aqeknigttr irkqpdlqyp ldsstlpkle
      901 efyisliksq qsaegsqsep asiqtplkpg qasstapsst paagdspenh sgsapdfsea
      961 lhsskyshgc lgsscavshv qeppalvpqc errea
//
LOCUS       NP_001093980             335 aa            linear   ROD 27-APR-2025
DEFINITION  tRNA N6-adenosine threonylcarbamoyltransferase [Rattus norvegicus].
ACCESSION   NP_001093980 XP_001064067 XP_214163
VERSION     NP_001093980.1
DBSOURCE    REFSEQ: accession NM_001100510.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Braun,D.A., Rao,J., Mollet,G., Schapiro,D., Daugeron,M.C., Tan,W.,
            Gribouval,O., Boyer,O., Revy,P., Jobst-Schwan,T., Schmidt,J.M.,
            Lawson,J.A., Schanze,D., Ashraf,S., Ullmann,J.F.P.,
            Hoogstraten,C.A., Boddaert,N., Collinet,B., Martin,G., Liger,D.,
            Lovric,S., Furlano,M., Guerrera,I.C., Sanchez-Ferras,O., Hu,J.F.,
            Boschat,A.C., Sanquer,S., Menten,B., Vergult,S., De Rocker,N.,
            Airik,M., Hermle,T., Shril,S., Widmeier,E., Gee,H.Y., Choi,W.I.,
            Sadowski,C.E., Pabst,W.L., Warejko,J.K., Daga,A., Basta,T.,
            Matejas,V., Scharmann,K., Kienast,S.D., Behnam,B., Beeson,B.,
            Begtrup,A., Bruce,M., Ch'ng,G.S., Lin,S.P., Chang,J.H., Chen,C.H.,
            Cho,M.T., Gaffney,P.M., Gipson,P.E., Hsu,C.H., Kari,J.A., Ke,Y.Y.,
            Kiraly-Borri,C., Lai,W.M., Lemyre,E., Littlejohn,R.O., Masri,A.,
            Moghtaderi,M., Nakamura,K., Ozaltin,F., Praet,M., Prasad,C.,
            Prytula,A., Roeder,E.R., Rump,P., Schnur,R.E., Shiihara,T.,
            Sinha,M.D., Soliman,N.A., Soulami,K., Sweetser,D.A., Tsai,W.H.,
            Tsai,J.D., Topaloglu,R., Vester,U., Viskochil,D.H.,
            Vatanavicharn,N., Waxler,J.L., Wierenga,K.J., Wolf,M.T.F.,
            Wong,S.N., Leidel,S.A., Truglio,G., Dedon,P.C., Poduri,A., Mane,S.,
            Lifton,R.P., Bouchard,M., Kannu,P., Chitayat,D., Magen,D.,
            Callewaert,B., van Tilbeurgh,H., Zenker,M., Antignac,C. and
            Hildebrandt,F.
  TITLE     Mutations in KEOPS-complex genes cause nephrotic syndrome with
            primary microcephaly
  JOURNAL   Nat Genet 49 (10), 1529-1538 (2017)
   PUBMED   28805828
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Wan,L.C., Maisonneuve,P., Szilard,R.K., Lambert,J.P., Ng,T.F.,
            Manczyk,N., Huang,H., Laister,R., Caudy,A.A., Gingras,A.C.,
            Durocher,D. and Sicheri,F.
  TITLE     Proteomic analysis of the human KEOPS complex identifies C14ORF142
            as a core subunit homologous to yeast Gon7
  JOURNAL   Nucleic Acids Res 45 (2), 805-817 (2017)
   PUBMED   27903914
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Yao,M., Akiyama,K., Tan,Y., Sarker,A.H., Ikeda,S., Alam,S.S.,
            Tsutsui,K., Yoshida,M.C. and Seki,S.
  TITLE     Genomic structure of the rat major AP endonuclease gene (Apex) with
            an adjacent putative O-sialoglycoprotease gene (Prsmg1/Gcpl1) and a
            processed Apex pseudogene (Apexp1)
  JOURNAL   Acta Med Okayama 53 (6), 245-252 (1999)
   PUBMED   10631378
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Akiyama,K., Seki,S., Oshida,T. and Yoshida,M.C.
  TITLE     Structure, promoter analysis and chromosomal assignment of the
            human APEX gene
  JOURNAL   Biochim Biophys Acta 1219 (1), 15-25 (1994)
   PUBMED   8086453
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158592.1.
            
            On or before Jun 4, 2008 this sequence version replaced
            XP_001064067.1, XP_214163.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158592.1, SRR8487226.118690.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676808 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..335
                     /product="tRNA N6-adenosine threonylcarbamoyltransferase"
                     /EC_number="2.3.1.234"
                     /note="probable O-sialoglycoprotein endopeptidase;
                     probable tRNA threonylcarbamoyladenosine biosynthesis
                     protein Osgep; Prsmg1/Gcpl1; O-sialoglycoprotease;
                     pasteurella haemolytica metalloprotease homolog with
                     glycoprotein substrates/gpc-like protein 1; t(6)A
                     synthase; N6-L-threonylcarbamoyladenine synthase; t(6)A37
                     threonylcarbamoyladenosine biosynthesis protein Osgep;
                     probable tRNA N6-adenosine threonylcarbamoyltransferase"
                     /calculated_mol_wt=36226
     Region          4..310
                     /region_name="ASKHA_NBD_OSGEP_like_euk"
                     /note="nucleotide-binding domain (NBD) of
                     O-sialoglycoprotein endopeptidase (OSGEP) and similar
                     proteins mainly from eukaryotes; cd24132"
                     /db_xref="CDD:466982"
     CDS             1..335
                     /gene="Osgep"
                     /coded_by="NM_001100510.1:90..1097"
                     /db_xref="GeneID:290028"
                     /db_xref="RGD:1308578"
ORIGIN      
        1 mpavlgfegs ankigvgvvr dgtvlanprr tyvtapgtgf lpgdtarhhr avildllqea
       61 lteagltpkd idciaytkgp gmgaplasva vvartvaqlw nkpllgvnhc ighiemgrli
      121 tgavnptvly vsggntqvis ysehryrifg etidiavgnc ldrfarvlki sndpspgyni
      181 eqmakrgkkl velpytvkgm dvsfsgilsf iedaaqrmla tgectpedlc fslqetvfam
      241 lveiterama hcgskealiv ggvgcnvrlq emmatmcqer gaqlfatder fcidngamia
      301 qagwemfqag hrtplqdsgi tqryrtdeve vtwrd
//
LOCUS       NP_076492                846 aa            linear   ROD 27-APR-2025
DEFINITION  selenocysteine insertion sequence-binding protein 2 [Rattus
            norvegicus].
ACCESSION   NP_076492
VERSION     NP_076492.1
DBSOURCE    REFSEQ: accession NM_024002.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Seeher,S., Atassi,T., Mahdi,Y., Carlson,B.A., Braun,D., Wirth,E.K.,
            Klein,M.O., Reix,N., Miniard,A.C., Schomburg,L., Hatfield,D.L.,
            Driscoll,D.M. and Schweizer,U.
  TITLE     Secisbp2 is essential for embryonic development and enhances
            selenoprotein expression
  JOURNAL   Antioxid Redox Signal 21 (6), 835-849 (2014)
   PUBMED   24274065
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Seeher,S., Carlson,B.A., Miniard,A.C., Wirth,E.K., Mahdi,Y.,
            Hatfield,D.L., Driscoll,D.M. and Schweizer,U.
  TITLE     Impaired selenoprotein expression in brain triggers striatal
            neuronal loss leading to co-ordination defects in mice
  JOURNAL   Biochem J 462 (1), 67-75 (2014)
   PUBMED   24844465
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Bubenik,J.L., Miniard,A.C. and Driscoll,D.M.
  TITLE     Characterization of the UGA-recoding and SECIS-binding activities
            of SECIS-binding protein 2
  JOURNAL   RNA Biol 11 (11), 1402-1413 (2014)
   PUBMED   25692238
  REMARK    GeneRIF: Data show that a purified recombinant protein encompassing
            amino acids 517-777 of SECIS-binding protein 2 (SBP2) binds to
            SECIS elements with high affinity and selectivity.
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Bifano,A.L., Atassi,T., Ferrara,T. and Driscoll,D.M.
  TITLE     Identification of nucleotides and amino acids that mediate the
            interaction between ribosomal protein L30 and the SECIS element
  JOURNAL   BMC Mol Biol 14, 12 (2013)
   PUBMED   23777426
  REMARK    GeneRIF: L30 and SBP2 bind to overlapping but non-identical sites
            on the SECIS.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 846)
  AUTHORS   Gonzalez-Flores,J.N., Gupta,N., DeMong,L.W. and Copeland,P.R.
  TITLE     The selenocysteine-specific elongation factor contains a novel and
            multi-functional domain
  JOURNAL   J Biol Chem 287 (46), 38936-38945 (2012)
   PUBMED   22992746
  REMARK    GeneRIF: SBP2/SECIS complex activates eEFSec by directing
            functional interactions between Domain IV and the ribosome to
            promote Sec-tRNA(Sec) binding and accommodation into the ribosomal
            A-site
REFERENCE   6  (residues 1 to 846)
  AUTHORS   Lu,C., Qiu,F., Zhou,H., Peng,Y., Hao,W., Xu,J., Yuan,J., Wang,S.,
            Qiang,B., Xu,C. and Peng,X.
  TITLE     Identification and characterization of selenoprotein K: an
            antioxidant in cardiomyocytes
  JOURNAL   FEBS Lett 580 (22), 5189-5197 (2006)
   PUBMED   16962588
REFERENCE   7  (residues 1 to 846)
  AUTHORS   Chavatte,L., Brown,B.A. and Driscoll,D.M.
  TITLE     Ribosomal protein L30 is a component of the UGA-selenocysteine
            recoding machinery in eukaryotes
  JOURNAL   Nat Struct Mol Biol 12 (5), 408-416 (2005)
   PUBMED   15821744
REFERENCE   8  (residues 1 to 846)
  AUTHORS   Copeland,P.R., Stepanik,V.A. and Driscoll,D.M.
  TITLE     Insight into mammalian selenocysteine insertion: domain structure
            and ribosome binding properties of Sec insertion sequence binding
            protein 2
  JOURNAL   Mol Cell Biol 21 (5), 1491-1498 (2001)
   PUBMED   11238886
REFERENCE   9  (residues 1 to 846)
  AUTHORS   Copeland,P.R., Fletcher,J.E., Carlson,B.A., Hatfield,D.L. and
            Driscoll,D.M.
  TITLE     A novel RNA binding protein, SBP2, is required for the translation
            of mammalian selenoprotein mRNAs
  JOURNAL   EMBO J 19 (2), 306-314 (2000)
   PUBMED   10637234
REFERENCE   10 (residues 1 to 846)
  AUTHORS   Copeland,P.R. and Driscoll,D.M.
  TITLE     Purification, redox sensitivity, and RNA binding properties of
            SECIS-binding protein 2, a protein involved in selenoprotein
            biosynthesis
  JOURNAL   J Biol Chem 274 (36), 25447-25454 (1999)
   PUBMED   10464275
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ251245.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ251245.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..846
                     /product="selenocysteine insertion sequence-binding
                     protein 2"
                     /function="essential for selenocysteine incorporation"
                     /calculated_mol_wt=93169
     Region          151..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          266..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          321..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          370..380
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:10637234"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          448..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          475..613
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          650..750
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     Region          666..687
                     /region_name="RNA-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     Region          774..804
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX72.1)"
     CDS             1..846
                     /gene="Secisbp2"
                     /gene_synonym="Sbp2"
                     /coded_by="NM_024002.1:44..2584"
                     /db_xref="GeneID:79049"
                     /db_xref="RGD:620991"
ORIGIN      
        1 maserprepe gedsiklsad vkpfvpkfag lnvawsesse acvfpgcaat yypfvqespa
       61 aeqkmypedm afgapafpaq yvsseialhp fayptyales tqsvcsvptl qydysqaqch
      121 pgfrpakprn ehacppqeak cvfkkkssde rraweeqkss nrradgavpc earpargsch
      181 lksdgyhkrp drksriltks astskpefef srldfpelqs pknsnlpetq kqprwgplgp
      241 aasnmsllge agkpvadmve gkmvktdhtd gavtnnaats spsctrelsw tpmgyivrqt
      301 vssdsaaate tvnsiinlkk ttssadaknv svtsealssd psfsrekrvh pgpkakasqg
      361 seleqnessk knkkkkeksk ssyevlpvqe ppriedaeef pnlsvaserr hrgespklqs
      421 kqqaqndfkt ggkksqvpvq ldlggmlaal ekqqhaphak pssrpvvfsv gavpvlskda
      481 ssgergrrss qvktphnpld ssaplmkkgk qreipkakkp tslkkiilke rqermqqrlq
      541 esavsptvas ddsqdvesgv tnqipspdnp tgpekteepm sstpvveges eepagtefqr
      601 dpeacqpapd satfpkihsr rfrdycsqml skevdacvtg llkelvrfqd rmyqkdpvka
      661 ktkrrlvlgl revlkhlklr klkciiispn cektqskggl ddtlhtiidc aceqnipfvf
      721 alnrkalgrs lnkavpvsiv gifsydgaqd qfhkmveltm aarqayktml etmrqeqage
      781 pgpqtppspp mqdpiqstde gtlastgeep hyieiwrkhl eaysqhalel edsleastsq
      841 mmnlnl
//
LOCUS       NP_001011907             463 aa            linear   ROD 27-APR-2025
DEFINITION  NADH dehydrogenase [ubiquinone] iron-sulfur protein 2,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_001011907 XP_213940
VERSION     NP_001011907.1
DBSOURCE    REFSEQ: accession NM_001011907.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Dunham-Snary,K.J., Wu,D., Potus,F., Sykes,E.A., Mewburn,J.D.,
            Charles,R.L., Eaton,P., Sultanian,R.A. and Archer,S.L.
  TITLE     Ndufs2, a Core Subunit of Mitochondrial Complex I, Is Essential for
            Acute Oxygen-Sensing and Hypoxic Pulmonary Vasoconstriction
  JOURNAL   Circ Res 124 (12), 1727-1746 (2019)
   PUBMED   30922174
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Wang,Z., Fan,M., Candas,D., Zhang,T.Q., Qin,L., Eldridge,A.,
            Wachsmann-Hogiu,S., Ahmed,K.M., Chromy,B.A., Nantajit,D., Duru,N.,
            He,F., Chen,M., Finkel,T., Weinstein,L.S. and Li,J.J.
  TITLE     Cyclin B1/Cdk1 coordinates mitochondrial respiration for cell-cycle
            G2/M progression
  JOURNAL   Dev Cell 29 (2), 217-232 (2014)
   PUBMED   24746669
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Akude,E., Zherebitskaya,E., Chowdhury,S.K., Smith,D.R.,
            Dobrowsky,R.T. and Fernyhough,P.
  TITLE     Diminished superoxide generation is associated with respiratory
            chain dysfunction and changes in the mitochondrial proteome of
            sensory neurons from diabetic rats
  JOURNAL   Diabetes 60 (1), 288-297 (2011)
   PUBMED   20876714
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Tuppen,H.A., Hogan,V.E., He,L., Blakely,E.L., Worgan,L.,
            Al-Dosary,M., Saretzki,G., Alston,C.L., Morris,A.A., Clarke,M.,
            Jones,S., Devlin,A.M., Mansour,S., Chrzanowska-Lightowlers,Z.M.,
            Thorburn,D.R., McFarland,R. and Taylor,R.W.
  TITLE     The p.M292T NDUFS2 mutation causes complex I-deficient Leigh
            syndrome in multiple families
  JOURNAL   Brain 133 (10), 2952-2963 (2010)
   PUBMED   20819849
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Davison,E.J., Pennington,K., Hung,C.C., Peng,J., Rafiq,R.,
            Ostareck-Lederer,A., Ostareck,D.H., Ardley,H.C., Banks,R.E. and
            Robinson,P.A.
  TITLE     Proteomic analysis of increased Parkin expression and its
            interactants provides evidence for a role in modulation of
            mitochondrial function
  JOURNAL   Proteomics 9 (18), 4284-4297 (2009)
   PUBMED   19725078
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Murray,J., Taylor,S.W., Zhang,B., Ghosh,S.S. and Capaldi,R.A.
  TITLE     Oxidative damage to mitochondrial complex I due to peroxynitrite:
            identification of reactive tyrosines by mass spectrometry
  JOURNAL   J Biol Chem 278 (39), 37223-37230 (2003)
   PUBMED   12857734
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Loeffen,J., Elpeleg,O., Smeitink,J., Smeets,R.,
            Stockler-Ipsiroglu,S., Mandel,H., Sengers,R., Trijbels,F. and van
            den Heuvel,L.
  TITLE     Mutations in the complex I NDUFS2 gene of patients with
            cardiomyopathy and encephalomyopathy
  JOURNAL   Ann Neurol 49 (2), 195-201 (2001)
   PUBMED   11220739
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Procaccio,V., de Sury,R., Martinez,P., Depetris,D., Rabilloud,T.,
            Soularue,P., Lunardi,J. and Issartel,J.
  TITLE     Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa
            subunit of the mitochondrial respiratory Complex I and
            immunodetection of the mature protein in mitochondria
  JOURNAL   Mamm Genome 9 (6), 482-484 (1998)
   PUBMED   9585441
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082067.1.
            
            On Feb 11, 2005 this sequence version replaced XP_213940.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082067.1, FQ215922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..463
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 2, mitochondrial precursor"
                     /EC_number="7.1.1.2"
                     /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
                     2, mitochondrial; CI-49kD; complex I-49kD; NADH-ubiquinone
                     oxidoreductase 49 kDa subunit; NADH dehydrogenase
                     (ubiquinone) Fe-S protein 2; NADH dehydrogenase
                     [ubiquinone] iron-sulfur protein 2, mitochondrial-like"
                     /calculated_mol_wt=49244
     transit_peptide 1..33
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:P17694; propagated from
                     UniProtKB/Swiss-Prot (Q641Y2.1)"
                     /calculated_mol_wt=3336
     mat_peptide     34..463
                     /product="NADH dehydrogenase [ubiquinone] iron-sulfur
                     protein 2, mitochondrial. /id=PRO_0000342702"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y2.1)"
                     /calculated_mol_wt=49244
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91WD5; propagated from
                     UniProtKB/Swiss-Prot (Q641Y2.1)"
     Region          77..463
                     /region_name="PRK06075"
                     /note="NADH-quinone oxidoreductase subunit D"
                     /db_xref="CDD:180385"
     Site            118
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P17694; propagated from
                     UniProtKB/Swiss-Prot (Q641Y2.1)"
     CDS             1..463
                     /gene="Ndufs2"
                     /coded_by="NM_001011907.1:7..1398"
                     /db_xref="GeneID:289218"
                     /db_xref="RGD:1307109"
ORIGIN      
        1 maalravcsl rgvgaqvlra gsgirlpsqp srgarrwqpd iewaeqfsga vmypsketah
       61 wkpppwndvd vlkekvvtnv tlnfgpqhpa ahgvlrlvle lsgemvrkcd phigllhrgt
      121 eklieyktyl qalpyfdrld yvsmmcneqa yslaveklln iqpppraqwi rvlfgeitri
      181 lnhimavtth aldigamtpf fwmfeerekm fefyervsga rmhaayirpg gvhqdlplgl
      241 mddiyefskn fslridevee mltnnriwrn rtvdigvvsa edalnygfsg vmlrgsgiqw
      301 dlrktqpydv ydqvefdvpi gsrgdcydry lcrveemrqs lriieqclnk mppgeikvdd
      361 akvsppkrae mktsmeslih hfklytegyq vppgatytai eapkgefgvy lvsdgssrpy
      421 rckikapgfa hlagldkmsk ghmladvvai igtqdivfge idr
//
LOCUS       NP_073206                861 aa            linear   ROD 27-APR-2025
DEFINITION  major vault protein [Rattus norvegicus].
ACCESSION   NP_073206
VERSION     NP_073206.2
DBSOURCE    REFSEQ: accession NM_022715.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Yu,K., Yau,Y.H., Sinha,A., Tan,T., Kickhoefer,V.A., Rome,L.H.,
            Lee,H., Shochat,S.G. and Lim,S.
  TITLE     Modulation of the Vault Protein-Protein Interaction for Tuning of
            Molecular Release
  JOURNAL   Sci Rep 7 (1), 14816 (2017)
   PUBMED   29093465
  REMARK    GeneRIF: The predicted docking shows that the vault-interacting
            domain of vault poly(ADP-ribose)-polymerase (INT) interaction sites
            are located between MVP domains 3 and 5.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Stamer,W.D., Hoffman,E.A., Luther,J.M., Hachey,D.L. and Schey,K.L.
  TITLE     Protein profile of exosomes from trabecular meshwork cells
  JOURNAL   J Proteomics 74 (6), 796-804 (2011)
   PUBMED   21362503
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Kim,E., Lee,S., Mian,M.F., Yun,S.U., Song,M., Yi,K.S., Ryu,S.H. and
            Suh,P.G.
  TITLE     Crosstalk between Src and major vault protein in epidermal growth
            factor-dependent cell signalling
  JOURNAL   FEBS J 273 (4), 793-804 (2006)
   PUBMED   16441665
  REMARK    GeneRIF: Data show that the interaction between Src and major vault
            protein (MVP) is critically dependent on Src activity and protein
            (MVP) tyrosyl phosphorylation, which are induced by epidermal
            growth factor stimulation.
            Erratum:[FEBS J. 2006 Jun;273(11):2577]
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Kolli,S., Zito,C.I., Mossink,M.H., Wiemer,E.A. and Bennett,A.M.
  TITLE     The major vault protein is a novel substrate for the tyrosine
            phosphatase SHP-2 and scaffold protein in epidermal growth factor
            signaling
  JOURNAL   J Biol Chem 279 (28), 29374-29385 (2004)
   PUBMED   15133037
REFERENCE   8  (residues 1 to 861)
  AUTHORS   Ehrnsperger,C. and Volknandt,W.
  TITLE     Major vault protein is a substrate of endogenous protein kinases in
            CHO and PC12 cells
  JOURNAL   Biol Chem 382 (10), 1463-1471 (2001)
   PUBMED   11727830
  REMARK    GeneRIF: casein kinase II enhances the phosphorylation of MVP in
            PC12 cells.Our results suggest that cell-specific phosphorylation
            of MVP may play a critical role in vault function.
REFERENCE   9  (residues 1 to 861)
  AUTHORS   Kickhoefer,V.A., Stephen,A.G., Harrington,L., Robinson,M.O. and
            Rome,L.H.
  TITLE     Vaults and telomerase share a common subunit, TEP1
  JOURNAL   J Biol Chem 274 (46), 32712-32717 (1999)
   PUBMED   10551828
REFERENCE   10 (residues 1 to 861)
  AUTHORS   Kickhoefer,V.A. and Rome,L.H.
  TITLE     The sequence of a cDNA encoding the major vault protein from Rattus
            norvegicus
  JOURNAL   Gene 151 (1-2), 257-260 (1994)
   PUBMED   7828886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U09870.2.
            
            On Jan 21, 2004 this sequence version replaced NP_073206.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09870.2, BC071174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..861
                     /product="major vault protein"
                     /calculated_mol_wt=95667
     Region          2..56
                     /region_name="MVP 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q14764; propagated from
                     UniProtKB/Swiss-Prot (Q62667.4)"
     Region          4..850
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     Region          57..111
                     /region_name="MVP 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          112..164
                     /region_name="MVP 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          165..217
                     /region_name="MVP 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          218..272
                     /region_name="MVP 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          273..323
                     /region_name="MVP 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          324..379
                     /region_name="MVP 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          380..457
                     /region_name="MVP 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62667.4)"
     Region          435..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     Region          458..520
                     /region_name="MVP 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00571,
                     ECO:0000269|PubMed:19150846"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62667.4)"
     CDS             1..861
                     /gene="Mvp"
                     /coded_by="NM_022715.2:62..2647"
                     /db_xref="GeneID:64681"
                     /db_xref="RGD:70932"
ORIGIN      
        1 mateeaiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapvrm vtvpprhyci
       61 vanpvsrdtq ssvlfditgq vrlrhadqei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkngdkvmag dewlfegpgt yipqkevevv eiiqatvikq nqalrlrark
      181 ecfdregkgr vtgeewlvrs vgaylpavfe evldlvdavi ltektalhlr alqnfrdlrg
      241 vlhrtgeewl vtvqdteahv pdvyeevlgv vpittlgprh ycvildpmgp dgknqlgqkr
      301 vvkgeksffl qpgerlergi qdvyvlseqq glllkalqpl eegeseekvs hqagdcwlir
      361 gpleyvpsak vevveerqai pldqnegiyv qdvktgkvra vigstymltq devlwekelp
      421 sgveellnlg hdpladrgqk gtakplqpsa prnktrvvsy rvphnaavqv ydyrakrarv
      481 vfgpelvtld peeqftvlsl sagrpkrpha rralclllgp dfftdvitie tadharlqlq
      541 laynwhfelk nrndpaeaak lfsvpdfvgd ackaiasrvr gavasvtfdd fhknsariir
      601 mavfgfemse dtgpdgtllp kardqavfpq nglvvssvdv qsvepvdqrt rdalqrsvql
      661 aieittnsqe aaakheaqrl eqeargrler qkildqseae karkellele amsmavestg
      721 nakaeaesra eaariegegs vlqaklkaqa laieteaele rvkkvremel iyaraqlele
      781 vskaqqlanv eakkfkemte algpgtirdl avagpemqvk llqslglkst litdgsspin
      841 lfstafgllg lgsdgqppaq k
//
LOCUS       NP_001030314             646 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor E2-alpha isoform b [Rattus norvegicus].
ACCESSION   NP_001030314 XP_001076440
VERSION     NP_001030314.1
DBSOURCE    REFSEQ: accession NM_001035237.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Guo,Q., Liu,Y., Sun,R., Yang,F., Qiao,P., Zhang,R., Song,L., E,L.
            and Liu,H.
  TITLE     Mechanical stimulation induced osteogenic differentiation of BMSCs
            through TWIST/E2A/p21 axis
  JOURNAL   Biosci Rep 40 (5) (2020)
   PUBMED   32309849
  REMARK    GeneRIF: Mechanical stimulation induced osteogenic differentiation
            of BMSCs through TWIST/E2A/p21 axis.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Siu,M.K., Chen,W.Y., Tsai,H.Y., Chen,H.Y., Yin,J.J., Chen,C.L.,
            Tsai,Y.C. and Liu,Y.N.
  TITLE     TCF7 is suppressed by the androgen receptor via microRNA-1-mediated
            downregulation and is involved in the development of resistance to
            androgen deprivation in prostate cancer
  JOURNAL   Prostate Cancer Prostatic Dis 20 (2), 172-178 (2017)
   PUBMED   28220803
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Wang,Z., Kim,J., Teng,Y., Ding,H.F., Zhang,J., Hai,T., Cowell,J.K.
            and Yan,C.
  TITLE     Loss of ATF3 promotes hormone-induced prostate carcinogenesis and
            the emergence of CK5(+)CK8(+) epithelial cells
  JOURNAL   Oncogene 35 (27), 3555-3564 (2016)
   PUBMED   26522727
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Udayakumar,T.S., Stoyanova,R., Shareef,M.M., Mu,Z., Philip,S.,
            Burnstein,K.L. and Pollack,A.
  TITLE     Edelfosine Promotes Apoptosis in Androgen-Deprived Prostate Tumors
            by Increasing ATF3 and Inhibiting Androgen Receptor Activity
  JOURNAL   Mol Cancer Ther 15 (6), 1353-1363 (2016)
   PUBMED   26944919
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Zhu,G., Li,X., Guo,B., Ke,Q., Dong,M. and Li,F.
  TITLE     PAK5-mediated E47 phosphorylation promotes epithelial-mesenchymal
            transition and metastasis of colon cancer
  JOURNAL   Oncogene 35 (15), 1943-1954 (2016)
   PUBMED   26212009
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Metz,R. and Ziff,E.
  TITLE     The helix-loop-helix protein rE12 and the C/EBP-related factor
            rNFIL-6 bind to neighboring sites within the c-fos serum response
            element
  JOURNAL   Oncogene 6 (12), 2165-2178 (1991)
   PUBMED   1766666
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Nelson,C., Shen,L.P., Meister,A., Fodor,E. and Rutter,W.J.
  TITLE     Pan: a transcriptional regulator that binds chymotrypsin, insulin,
            and AP-4 enhancer motifs
  JOURNAL   Genes Dev 4 (6), 1035-1043 (1990)
   PUBMED   2200736
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Murre,C., McCaw,P.S., Vaessin,H., Caudy,M., Jan,L.Y., Jan,Y.N.,
            Cabrera,C.V., Buskin,J.N., Hauschka,S.D., Lassar,A.B. et al.
  TITLE     Interactions between heterologous helix-loop-helix proteins
            generate complexes that bind specifically to a common DNA sequence
  JOURNAL   Cell 58 (3), 537-544 (1989)
   PUBMED   2503252
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X54549.1, BC078750.1 and BQ192196.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001076440.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078750.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..646
                     /product="transcription factor E2-alpha isoform b"
                     /note="transcription factor E2-alpha; TCF-3; transcription
                     regulator Pan; pancreas specific transcription factor 1c;
                     immunoglobulin enhancer-binding factor E12/E47;
                     transcription factor E2a; transcription factor E2a-like"
                     /calculated_mol_wt=67154
     Region          533..606
                     /region_name="bHLH_E-protein_E47-like"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor E47 and similar proteins; cd18943"
                     /db_xref="CDD:381513"
     Site            order(543,547,549..551,553,558,579..580)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381513"
     Site            order(556..557,560..561,563..564,567,571,581,584,588,
                     590..592,594..595,597..599,601)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     Site            order(556..557,560..561,563..564,567,571,581,584,588,591,
                     594..599)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     CDS             1..646
                     /gene="Tcf3"
                     /gene_synonym="Pan2; Tcfe2a"
                     /coded_by="NM_001035237.1:74..2014"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:171046"
                     /db_xref="RGD:620914"
ORIGIN      
        1 mmnqsqrmap vgsdkelsdl ldfsmmfplp vangkgrpas lagtqfagsg ledrpssgsw
       61 gnseqnsssf dpsraysega hfsdshsslp pstflgaglg gkgsernaya tfgrdtsvgt
      121 lsqagflpge lglsspgpls psgvksssqy ytsfpsnprr raadggldtq pkkvrkvppg
      181 lpssvypsss gdnysrdata ypsaktpssa ypspfyvadg slhpsaelws ppgqvgfgpm
      241 lgdgsaplpl apgsssvssg afgglqqqdr mgyqlhgsev ngtlpavssf saapgtysgt
      301 sghtppvsga dsllgtrgtt asssgdalgk alasiyspdh ssnnfspsps tpvgspqglp
      361 gtsqwpraga psalspnyda glhglskmed rldeaihvlr shavgtasel hgllpghstl
      421 ttsfagpmsl ggrhaglvsg shpedgltsg asllhnhasl psqpsslpdl sqrppdsfsg
      481 lgragvtaga seikreeked eevtsvadae edkkdlkvpr trtsstdevl sleekdlrdr
      541 errmannare rvrvrdinea frelgrmcql hlksdkaqtk llilqqavqv ilgleqqvre
      601 rnlnpkaacl krreeekvsg vvgdpqlals aahpglgeah npaghl
//
LOCUS       NP_653346                673 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein-signaling modulator 1 isoform a [Rattus norvegicus].
ACCESSION   NP_653346
VERSION     NP_653346.2
DBSOURCE    REFSEQ: accession NM_144745.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Conley,J.M. and Watts,V.J.
  TITLE     Differential effects of AGS3 expression on D(2L) dopamine
            receptor-mediated adenylyl cyclase signaling
  JOURNAL   Cell Mol Neurobiol 33 (4), 551-558 (2013)
   PUBMED   23504261
  REMARK    GeneRIF: AGS3 reduced D(2L)DR-mediated sensitization of AC1 and
            AC2.
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Wang,W., Li,Q., Zou,F., Yu,Z., Wang,Y., Lu,T., Hu,T. and Cui,G.
  TITLE     Increased expression of AGS3 in rat brain cortex after traumatic
            brain injury
  JOURNAL   J Neurosci Res 91 (5), 726-736 (2013)
   PUBMED   23404409
  REMARK    GeneRIF: This study demonistrated that the ags3 expression
            increassing in rat brain cortex after traumatic brain injury.
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Regner,K.R., Nozu,K., Lanier,S.M., Blumer,J.B., Avner,E.D.,
            Sweeney,W.E. Jr. and Park,F.
  TITLE     Loss of activator of G-protein signaling 3 impairs renal tubular
            regeneration following acute kidney injury in rodents
  JOURNAL   FASEB J 25 (6), 1844-1855 (2011)
   PUBMED   21343176
  REMARK    GeneRIF: These data suggest that Gpsm1 acts through a novel
            receptor-independent mechanism to facilitate renal tubular
            epithelial cell proliferation and renal tubular regeneration.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Xu,Z., Xia,B., Gong,Q., Bailey,J., Groves,B., Radeke,M., Wood,S.A.,
            Szumlinski,K.K. and Ma,D.
  TITLE     Identification of a deubiquitinating enzyme as a novel
            AGS3-interacting protein
  JOURNAL   PLoS One 5 (3), e9725 (2010)
   PUBMED   20305814
  REMARK    GeneRIF: levels of AGS3 and USP9x are co-regulated in the
            prefrontal cortex of rats withdrawn from repeated cocaine treatment
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Bernard,M.L., Peterson,Y.K., Chung,P., Jourdan,J. and Lanier,S.M.
  TITLE     Selective interaction of AGS3 with G-proteins and the influence of
            AGS3 on the activation state of G-proteins
  JOURNAL   J Biol Chem 276 (2), 1585-1593 (2001)
   PUBMED   11042168
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Natochin,M., Lester,B., Peterson,Y.K., Bernard,M.L., Lanier,S.M.
            and Artemyev,N.O.
  TITLE     AGS3 inhibits GDP dissociation from galpha subunits of the Gi
            family and rhodopsin-dependent activation of transducin
  JOURNAL   J Biol Chem 275 (52), 40981-40985 (2000)
   PUBMED   11024022
REFERENCE   8  (residues 1 to 673)
  AUTHORS   De Vries,L., Fischer,T., Tronchere,H., Brothers,G.M.,
            Strockbine,B., Siderovski,D.P. and Farquhar,M.G.
  TITLE     Activator of G protein signaling 3 is a guanine dissociation
            inhibitor for Galpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14364-14369 (2000)
   PUBMED   11121039
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Peterson,Y.K., Bernard,M.L., Ma,H., Hazard,S. 3rd, Graber,S.G. and
            Lanier,S.M.
  TITLE     Stabilization of the GDP-bound conformation of Gialpha by a peptide
            derived from the G-protein regulatory motif of AGS3
  JOURNAL   J Biol Chem 275 (43), 33193-33196 (2000)
   PUBMED   10969064
  REMARK    GeneRIF: The GPR motif in this protein and other proteins is
            actually associated with activity as a GDI - guanine nucleotide
            dissociation inhibitor and not GTPase activator as initially
            suggested.
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Takesono,A., Cismowski,M.J., Ribas,C., Bernard,M., Chung,P.,
            Hazard,S. 3rd, Duzic,E. and Lanier,S.M.
  TITLE     Receptor-independent activators of heterotrimeric G-protein
            signaling pathways
  JOURNAL   J Biol Chem 274 (47), 33202-33205 (1999)
   PUBMED   10559191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB743977.1, AF107723.1, CB615566.1, BC105302.1 and BF408282.1.
            
            On Feb 28, 2009 this sequence version replaced NP_653346.1.
            
            Transcript Variant: This variant (1, also known as AGS3-LONG)
            represents the longer transcript and encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132263 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..673
                     /product="G-protein-signaling modulator 1 isoform a"
                     /note="activator of G-protein signaling 3; G-protein
                     signalling modulator 1 (AGS3-like, C. elegans); G-protein
                     signaling modulator 1 (AGS3-like, C. elegans)"
                     /calculated_mol_wt=74309
     Region          1..507
                     /region_name="Mediates association with membranes"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          31..56
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          68..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          69..322
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(70..71,74..75,77,107,110..111,114..115,117..118,147,
                     150..151,154..155,158)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          105..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(207,210..211,214..215,217,247,250..251,254..255,
                     257..258,287,290..291,294..295,298)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          207..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          239..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          286..313
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..358
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          320..354
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          361..485
                     /region_name="Interaction with STK11/LKB1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            418
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6IR34; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          420..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          494..515
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          510..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          547..567
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          595..615
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          609..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          629..650
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          645..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     CDS             1..673
                     /gene="Gpsm1"
                     /gene_synonym="Ags3"
                     /coded_by="NM_144745.2:119..2140"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:246254"
                     /db_xref="RGD:628682"
ORIGIN      
        1 maspappaae elpgpaarrl ysrmeascle lalegerlck agdfkagvaf feaavqvgte
       61 dlktlsaiys qlgnayfylk eyaralqfhk hdlllartig drmgeakasg nlgntlkvlg
      121 rfdeaivccq rhldiaqeqg dkvgearaly nignvyhakg kqlswnaaqd pghlppdvre
      181 tlhrasefye rnlslvkelg draaqgrayg nlgnthyllg nfteattfhk erlaiakefg
      241 dkaaerrays nlgnahiflg rfdvaaehyk ktlqlsrqlr dqaveaqacy slgntytllq
      301 dyeraaeyhl rhlviaqela drvgegracw slgnayvsmg spaqaltfak khlqisqeig
      361 drngeltarm niahlqlalg rltspaaaek pdlagyeaqg arpkrtqrls aetwdllrlp
      421 ldreqngeth htgdwrgpsr dslplpmrsr kyqegpdaie rrpregshsp ldsadvrvqv
      481 prtgipraps sdeecffdll skfqssrmdd qrcpleegqa gaaeataapt leeraaqpsv
      541 taspqteeff dliassqsrr lddqrasvgs lpglritlnn vghlrgdgdp qepgdeffnm
      601 likyqssrid dqrcpppdvl prgptmpded ffsliqrvqa krmdeqrvdl agspdqeasg
      661 lpdprqqcpp gas
//
LOCUS       NP_037217                432 aa            linear   ROD 27-APR-2025
DEFINITION  urokinase-type plasminogen activator precursor [Rattus norvegicus].
ACCESSION   NP_037217 XP_346473
VERSION     NP_037217.3
DBSOURCE    REFSEQ: accession NM_013085.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Liu,Y., Zhao,K., Xiong,Z., Yi,Y., Xiong,C., Huang,D. and Zhao,H.
  TITLE     Transcriptional activation and regulation of urokinase plasminogen
            activator inducted by LPS through MyD88 independent pathway in rat
            Sertoli cells
  JOURNAL   Folia Histochem Cytobiol 59 (4), 236-244 (2021)
   PUBMED   34852179
  REMARK    GeneRIF: Transcriptional activation and regulation of urokinase
            plasminogen activator inducted by LPS through MyD88 independent
            pathway in rat Sertoli cells.
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Shi,Y., Zhang,Z., Cai,D., Kuang,J., Jin,S., Zhu,C., Shen,Y.,
            Feng,W., Ying,S. and Wang,L.
  TITLE     Urokinase Attenuates Pulmonary Thromboembolism in an Animal Model
            by Inhibition of Inflammatory Response
  JOURNAL   J Immunol Res 2018, 6941368 (2018)
   PUBMED   30671487
  REMARK    GeneRIF: that study shows that urokinase attenuates pulmonary
            thromboembolism in an animal model by inhibition of inflammatory
            response
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Li,W.D., Hu,N., Lei,F.R., Wei,S., Rong,J.J., Zhuang,H. and Li,X.Q.
  TITLE     Autophagy inhibits endothelial progenitor cells migration via the
            regulation of MMP2, MMP9 and uPA under normoxia condition
  JOURNAL   Biochem Biophys Res Commun 466 (3), 376-380 (2015)
   PUBMED   26363453
  REMARK    GeneRIF: autophagy could regulate the EPCs migration through
            mTOR-P70 S6K pathway, and MMP2, MMP9 and uPA may also involve in
            the regulation mechanism
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Longstaff,C. and Kolev,K.
  TITLE     Basic mechanisms and regulation of fibrinolysis
  JOURNAL   J Thromb Haemost 13 Suppl 1, S98-S105 (2015)
   PUBMED   26149056
  REMARK    Review article
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Grundel,A., Friedrich,K., Pfeiffer,M., Jacobs,E. and Dumke,R.
  TITLE     Subunits of the Pyruvate Dehydrogenase Cluster of Mycoplasma
            pneumoniae Are Surface-Displayed Proteins that Bind and Activate
            Human Plasminogen
  JOURNAL   PLoS One 10 (5), e0126600 (2015)
   PUBMED   25978044
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Ragno,P., Cassano,S., Degen,J., Kessler,C., Blasi,F. and Rossi,G.
  TITLE     The receptor for the plasminogen activator of urokinase type is
            up-regulated in transformed rat thyroid cells
  JOURNAL   FEBS Lett 306 (2-3), 193-198 (1992)
   PUBMED   1321734
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Henderson,B.R., Tansey,W.P., Phillips,S.M., Ramshaw,I.A. and
            Kefford,R.F.
  TITLE     Transcriptional and posttranscriptional activation of urokinase
            plasminogen activator gene expression in metastatic tumor cells
  JOURNAL   Cancer Res 52 (9), 2489-2496 (1992)
   PUBMED   1568219
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Oka,T., Ishida,T., Nishino,T. and Sugimachi,K.
  TITLE     Immunohistochemical evidence of urokinase-type plasminogen
            activator in primary and metastatic tumors of pulmonary
            adenocarcinoma
  JOURNAL   Cancer Res 51 (13), 3522-3525 (1991)
   PUBMED   2054790
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Nakagawa,M., Fukuyama,K., Epstein,W.L., Hara,A. and Sawada,H.
  TITLE     Partial purification and characterization of epidermal plasminogen
            activator and their inhibitor
  JOURNAL   Chem Pharm Bull (Tokyo) 37 (7), 1859-1863 (1989)
   PUBMED   2509088
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Kohga,S., Harvey,S.R., Weaver,R.M. and Markus,G.
  TITLE     Localization of plasminogen activators in human colon cancer by
            immunoperoxidase staining
  JOURNAL   Cancer Res 45 (4), 1787-1796 (1985)
   PUBMED   3884145
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105859.1.
            
            On Apr 13, 2007 this sequence version replaced NP_037217.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105859.1, X63434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..432
                     /product="urokinase-type plasminogen activator precursor"
                     /EC_number="3.4.21.73"
                     /note="urokinase-type plasminogen activator; uPA;
                     U-plasminogen activator; Urinary plasminogen activator,
                     urokinase; urokinase plasminogen activator"
                     /calculated_mol_wt=45823
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2104
     mat_peptide     20..432
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028333"
                     /note="propagated from UniProtKB/Swiss-Prot (P29598.1)"
                     /calculated_mol_wt=45823
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor"
                     /note="propagated from UniProtKB/Swiss-Prot (P29598.1)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,142)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..178
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P29598.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00749; propagated from
                     UniProtKB/Swiss-Prot (P29598.1)"
     Region          179..423
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(225,276,377)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(371,396,398)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..432
                     /gene="Plau"
                     /gene_synonym="UPAM"
                     /coded_by="NM_013085.3:63..1361"
                     /db_xref="GeneID:25619"
                     /db_xref="RGD:3343"
ORIGIN      
        1 mrvwlaslfl calvahsegg selgasdesn cgcqnggvcv sykyfssirr cscpkkfkge
       61 hceidtsktc yhgngqsyrg kantdtkgrp clawnspavl qqtynahrsd alslglgkhn
      121 ycrnpdnqrr pwcyvqiglk qfvqecmvqd cslskkpsst vdqqgfqcgq kalrprfkiv
      181 ggeftvvenq pwfaaiylkn kggsppsfkc ggslispcwv asathcfvnq pkkeeyvvyl
      241 gqskrnsynp gemkfeveql ilhedfsdet lafhndiall kirtstgqca qpsrtiqtic
      301 lpprfgdapf gsdceitgfg qesatdyfyp kdlkmsvvki isheqckqph yygseinykm
      361 lcaadpewkt dscsgdsggp licnidgrpt lsgivswgsg caeknkpgvy trvsyflnwi
      421 qshigeengl af
//
LOCUS       NP_001013230             407 aa            linear   ROD 27-APR-2025
DEFINITION  snRNA-activating protein complex subunit 3 [Rattus norvegicus].
ACCESSION   NP_001013230 XP_342856
VERSION     NP_001013230.1
DBSOURCE    REFSEQ: accession NM_001013212.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Vannini,A.
  TITLE     A structural perspective on RNA polymerase I and RNA polymerase III
            transcription machineries
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 258-264 (2013)
   PUBMED   23031840
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091186.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342856.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091186.1, SRR8487231.154063.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..407
                     /product="snRNA-activating protein complex subunit 3"
                     /note="SNAPc subunit 3"
                     /calculated_mol_wt=46099
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK68.1)"
     Region          198..401
                     /region_name="SNAPC3"
                     /note="snRNA-activating protein complex (SNAPc), subunit
                     3; pfam12251"
                     /db_xref="CDD:463506"
     CDS             1..407
                     /gene="Snapc3"
                     /coded_by="NM_001013212.1:17..1240"
                     /db_xref="GeneID:362537"
                     /db_xref="RGD:1305172"
ORIGIN      
        1 maedpqggga ggpqhpvpsg shssfpeyel pelhtrvfhv gafgelwrgr lgaqdlslne
       61 pqaaaqptdg easnngfeda avaedlgcsl eaaaelrvvc gldklrclge dedpevipen
      121 tdlvtlcvrk glldyreeni tidracrqet fayemeshal gkkpenpadm ieegesilsv
      181 nilypvifnk hrehkpyqtv lvlgsqklte lrdsiccvsd lqiggefsna pdqapehisk
      241 dlyksaffyf egtfyndkry pecrdlsrti iewseshdrg ygkfqtarme dftfndlnik
      301 lgfpylychq gdcehvvvit dirlvhhddc ldrtlypllt kkhwlwtrkc fvckmytarw
      361 vtnndtfape dpcffcdvcf rmlhydsegn klgeflaypy vdpgtfn
//
LOCUS       NP_001099721             382 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic tRNA 2-thiolation protein 1 [Rattus norvegicus].
ACCESSION   NP_001099721 XP_001080387 XP_218640
VERSION     NP_001099721.1
DBSOURCE    REFSEQ: accession NM_001106251.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001080387.1, XP_218640.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161898.1, DY311478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..382
                     /product="cytoplasmic tRNA 2-thiolation protein 1"
                     /note="ATP binding domain 3; cytosolic thiouridylase
                     subunit 1 homolog; cytoplasmic tRNA adenylyltransferase 1;
                     ATP-binding domain-containing protein 3"
                     /calculated_mol_wt=40111
     Region          34..243
                     /region_name="CTU1-like"
                     /note="cytoplasmic tRNA 2-thiolation protein 1 and similar
                     proteins; cd01713"
                     /db_xref="CDD:467486"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z7A3; propagated from
                     UniProtKB/Swiss-Prot (B1WBV0.1)"
     Region          207..308
                     /region_name="TIGR00269"
                     /note="TIGR00269 family protein"
                     /db_xref="CDD:129370"
     Region          350..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBV0.1)"
     CDS             1..382
                     /gene="Ctu1"
                     /gene_synonym="Atpbd3; RGD1308740"
                     /coded_by="NM_001106251.1:95..1243"
                     /db_xref="GeneID:292847"
                     /db_xref="RGD:1308740"
ORIGIN      
        1 mpaptcfsch karaalrrpr sgqalcgpcf caafeaevlr tvlaghllpq gavvavgasg
       61 gkdstvlahv lrelaprlgi tlhlvavdeg iggyrdaale avrsqaarwe lpltivayed
      121 lfggwtmdav arstagsgrs rscctfcgvl rrraleegar lvgathivtg hnaddmaetv
      181 lmnflrgdag rlarggvlgs tgegcalprc rplqfasqke vvlyahfrhl ryfseecvya
      241 peafrghard llklleaarp savldlvhsa erlalapaak ppppgtcsrc galasnklcq
      301 acalldglnr glprlaigkg rrvlqveppp lgnpsrvtsd pvalpepctc kqskdesnpc
      361 gnggdragat cvsksdlspv ae
//
LOCUS       NP_067695                420 aa            linear   ROD 27-APR-2025
DEFINITION  nucleobindin-2 precursor [Rattus norvegicus].
ACCESSION   NP_067695
VERSION     NP_067695.1
DBSOURCE    REFSEQ: accession NM_021663.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Yu,H., Liu,Q., Xie,M., Fan,J., Luo,J., Huang,J. and Chen,L.
  TITLE     Nesfatin-1 inhibits cerebral aneurysms by activating Nrf2 and
            inhibiting NF-kappaB signaling
  JOURNAL   CNS Neurosci Ther 30 (8), e14864 (2024)
   PUBMED   39097921
  REMARK    GeneRIF: Nesfatin-1 inhibits cerebral aneurysms by activating Nrf2
            and inhibiting NF-kappaB signaling.
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Zhang,L., Zhuo,Z., Chen,L., Liu,J., Huang,J., Deng,J., Lu,W. and
            Jiang,X.
  TITLE     Nesfatin-1 alleviates hyperoxia-induced bronchopulmonary dysplasia
            (BPD) via the nuclear factor-kappaB (NF-kappaB) p65 signaling
            pathway
  JOURNAL   J Biochem Mol Toxicol 38 (4), e23680 (2024)
   PUBMED   38511245
  REMARK    GeneRIF: Nesfatin-1 alleviates hyperoxia-induced bronchopulmonary
            dysplasia (BPD) via the nuclear factor-kappaB (NF-kappaB) p65
            signaling pathway.
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Dang,Q., Zhu,Y., Zhang,Y., Hu,Z., Wei,Y., Chen,Z., Jiang,X., Cai,X.
            and Yu,H.
  TITLE     Nuclear Binding Protein 2/Nesfatin-1 Affects Trophoblast Cell
            Fusion during Placental Development via the EGFR-PLCG1-CAMK4
            Pathway
  JOURNAL   Int J Mol Sci 25 (3), 1925 (2024)
   PUBMED   38339201
  REMARK    GeneRIF: Nuclear Binding Protein 2/Nesfatin-1 Affects Trophoblast
            Cell Fusion during Placental Development via the EGFR-PLCG1-CAMK4
            Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Lahane,G.P. and Dhar,A.
  TITLE     Nesfatin-1 peptide protects rat renal epithelial cells against high
            glucose and H2O2 induced injury via inhibition of oxidative stress,
            apoptosis, and fibrosis
  JOURNAL   Peptides 165, 171013 (2023)
   PUBMED   37105355
  REMARK    GeneRIF: Nesfatin-1 peptide protects rat renal epithelial cells
            against high glucose and H2O2 induced injury via inhibition of
            oxidative stress, apoptosis, and fibrosis.
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Li,Q., Wang,Y., Wei,R., An,Z., Dong,Z., Guan,Y. and Zhu,X.
  TITLE     A research on the expression of Nucb2/ cAMP / PKA in the
            hippocampus of alcohol-dependent rats
  JOURNAL   Biochem Biophys Res Commun 658, 148-152 (2023)
   PUBMED   37031608
  REMARK    GeneRIF: A research on the expression of Nucb2/ cAMP / PKA in the
            hippocampus of alcohol-dependent rats.
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Oh-I,S., Shimizu,H., Satoh,T., Okada,S., Adachi,S., Inoue,K.,
            Eguchi,H., Yamamoto,M., Imaki,T., Hashimoto,K., Tsuchiya,T.,
            Monden,T., Horiguchi,K., Yamada,M. and Mori,M.
  TITLE     Identification of nesfatin-1 as a satiety molecule in the
            hypothalamus
  JOURNAL   Nature 443 (7112), 709-712 (2006)
   PUBMED   17036007
  REMARK    GeneRIF: nesfatin, corresponding to NEFA/nucleobindin2 (NUCB2), a
            secreted protein of unknown function, is expressed in the
            appetite-control hypothalamic nuclei in rats
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Morel-Huaux,V.M., Pypaert,M., Wouters,S., Tartakoff,A.M.,
            Jurgan,U., Gevaert,K. and Courtoy,P.J.
  TITLE     The calcium-binding protein p54/NEFA is a novel luminal resident of
            medial Golgi cisternae that traffics independently of mannosidase
            II
  JOURNAL   Eur J Cell Biol 81 (2), 87-100 (2002)
   PUBMED   11893086
  REMARK    GeneRIF: Since NEFA is a peripheral luminal membrane constituent,
            its distinct trafficking from the transmembrane marker mannosidase
            II suggests a novel Golgi retention mechanism.
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Taniguchi,N., Taniura,H., Niinobe,M., Takayama,C.,
            Tominaga-Yoshino,K., Ogura,A. and Yoshikawa,K.
  TITLE     The postmitotic growth suppressor necdin interacts with a
            calcium-binding protein (NEFA) in neuronal cytoplasm
  JOURNAL   J Biol Chem 275 (41), 31674-31681 (2000)
   PUBMED   10915798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061778.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061778.1, SRR8487230.112013.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..420
                     /product="nucleobindin-2 precursor"
                     /note="DNA-binding protein NEFA; nesfatin-1;
                     prepronefastin; prepronesfatin"
                     /calculated_mol_wt=47254
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2855
     mat_peptide     25..420
                     /product="Nucleobindin-2. /id=PRO_0000004167"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI85.1)"
                     /calculated_mol_wt=47254
     Region          194..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI85.1)"
     Region          213..420
                     /region_name="Binds to necdin. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI85.1)"
     Region          247..322
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          304..334
                     /region_name="GBA. /evidence=ECO:0000250|UniProtKB:P80303"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI85.1)"
     Region          <307..>400
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JI85.1)"
     Region          366..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JI85.1)"
     CDS             1..420
                     /gene="Nucb2"
                     /gene_synonym="Nefa; p54"
                     /coded_by="NM_021663.2:214..1476"
                     /db_xref="GeneID:59295"
                     /db_xref="RGD:620888"
ORIGIN      
        1 mrwrtiqary cfllvpcvlt aleavpidvd ktkvhnvepv esarieppdt glyydeylkq
       61 vievletdph freklqkadi eeirsgrlsq eldlvshkvr trldelkrqe vgrlrmlika
      121 kldalqdtgm nhhlllkqfe hlnhqnpdtf eskdldmlik aatadleqyd rtrheefkky
      181 emmkeherre ylktlseekr keeeakfaem krkhedhpkv nhpgskdqlk evweetdgld
      241 pndfdpktff klhdvnndgf ldeqelealf tkeldkvynp qnaeddmiem eeerlrmreh
      301 vmneidnnkd rlvtleeflr atekkeflep dswetldqqq lfteeelkey esiiaiqese
      361 lkkkadelqk qkeelqrqhd hleaqkqeyq qavqqleqkk fqqgiapsgp agelkfepht
//
LOCUS       NP_001020158             229 aa            linear   ROD 27-APR-2025
DEFINITION  spliceosome-associated protein CWC15 homolog [Rattus norvegicus].
ACCESSION   NP_001020158 XP_217080
VERSION     NP_001020158.1
DBSOURCE    REFSEQ: accession NM_001024987.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Chanarat,S. and Strasser,K.
  TITLE     Splicing and beyond: the many faces of the Prp19 complex
  JOURNAL   Biochim Biophys Acta 1833 (10), 2126-2134 (2013)
   PUBMED   23742842
  REMARK    Review article
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Grote,M., Wolf,E., Will,C.L., Lemm,I., Agafonov,D.E., Schomburg,A.,
            Fischle,W., Urlaub,H. and Luhrmann,R.
  TITLE     Molecular architecture of the human Prp19/CDC5L complex
  JOURNAL   Mol Cell Biol 30 (9), 2105-2119 (2010)
   PUBMED   20176811
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091396.1.
            
            On Jun 25, 2005 this sequence version replaced XP_217080.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091396.1, FM074559.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..229
                     /product="spliceosome-associated protein CWC15 homolog"
                     /note="protein CWC15 homolog; CWC15 spliceosome-associated
                     protein homolog"
                     /calculated_mol_wt=26507
     Region          1..228
                     /region_name="Cwf_Cwc_15"
                     /note="Cwf15/Cwc15 cell cycle control protein; pfam04889"
                     /db_xref="CDD:428176"
     Region          1..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJP2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P013; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP2.1)"
     Site            18
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHS9; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP2.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P013; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP2.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP2.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5BJP2.1)"
     CDS             1..229
                     /gene="Cwc15"
                     /gene_synonym="RGD1310669"
                     /coded_by="NM_001024987.1:126..815"
                     /db_xref="GeneID:300361"
                     /db_xref="RGD:1310669"
ORIGIN      
        1 mttaarptfe parggrgkge gdlsqlskqy ssrdlpshtk ikyrqttqda peevrnrdfr
       61 releereraa areknrdrpt rehttsssvs kkprldqipa anldaddplt deededfeee
      121 sddddtaall aelekikker aeeqarkeqe qkaeeerirm enilsgnpll nltgpsqpqa
      181 nfkvkrrwdd dvvfkncakg iddqkkdkrf vndtlrsefh kkfmekyik
//
LOCUS       NP_062059                200 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 4A [Rattus norvegicus].
ACCESSION   NP_062059
VERSION     NP_062059.1
DBSOURCE    REFSEQ: accession NM_019186.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Wu,Y. and Smas,C.M.
  TITLE     Wdnm1-like, a new adipokine with a role in MMP-2 activation
  JOURNAL   Am J Physiol Endocrinol Metab 295 (1), E205-E215 (2008)
   PUBMED   18492766
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Hofmann,I., Thompson,A., Sanderson,C.M. and Munro,S.
  TITLE     The Arl4 family of small G proteins can recruit the cytohesin Arf6
            exchange factors to the plasma membrane
  JOURNAL   Curr Biol 17 (8), 711-716 (2007)
   PUBMED   17398095
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Schurmann,A., Koling,S., Jacobs,S., Saftig,P., Krauss,S.,
            Wennemuth,G., Kluge,R. and Joost,H.G.
  TITLE     Reduced sperm count and normal fertility in male mice with targeted
            disruption of the ADP-ribosylation factor-like 4 (Arl4) gene
  JOURNAL   Mol Cell Biol 22 (8), 2761-2768 (2002)
   PUBMED   11909968
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Lin,C.Y., Huang,P.H., Liao,W.L., Cheng,H.J., Huang,C.F., Kuo,J.C.,
            Patton,W.A., Massenburg,D., Moss,J. and Lee,F.J.
  TITLE     ARL4, an ARF-like protein that is developmentally regulated and
            localized to nuclei and nucleoli
  JOURNAL   J Biol Chem 275 (48), 37815-37823 (2000)
   PUBMED   10980193
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Schurmann,A., Breiner,M., Becker,W., Huppertz,C., Kainulainen,H.,
            Kentrup,H. and Joost,H.G.
  TITLE     Cloning of two novel ADP-ribosylation factor-like proteins and
            characterization of their differential expression in 3T3-L1 cells
  JOURNAL   J Biol Chem 269 (22), 15683-15688 (1994)
   PUBMED   8195219
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X77235.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X77235.1, BC088148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..200
                     /product="ADP-ribosylation factor-like protein 4A"
                     /note="ADP-ribosylation factor-like 4;
                     ADP-ribosylation-like 4; ADP-ribosylation factor-like 4A;
                     ADP-ribosylation factor like GTPase 4A"
                     /calculated_mol_wt=22457
     Region          18..200
                     /region_name="Arl4_Arl7"
                     /note="Arf-like 4 (Arl4) and 7 (Arl7) GTPases; cd04152"
                     /db_xref="CDD:206719"
     Site            27..34
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206719"
     Site            order(29..35,50..51,78,134..135,137,168..170)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206719"
     Site            order(29..30,34,38,50..57,84,89)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206719"
     Site            39..54
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206719"
     Site            order(51..55,60,75,79,85,87..89)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206719"
     Site            51
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206719"
     Site            order(52..59,74,85,88..89)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206719"
     Site            order(55..67,69..74)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206719"
     Site            75..92
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206719"
     Site            75..78
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206719"
     Site            134..137
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206719"
     Site            168..170
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206719"
     Site            order(188..191,197..200)
                     /site_type="active"
                     /note="putative nuclear localization signal [active]"
                     /db_xref="CDD:206719"
     CDS             1..200
                     /gene="Arl4a"
                     /gene_synonym="Arl4"
                     /coded_by="NM_019186.1:111..713"
                     /db_xref="GeneID:29308"
                     /db_xref="RGD:2152"
ORIGIN      
        1 mgnglsdqts ilsslpsfqs fhivilgldc agkttvlyrl qfnefvntvp tkgfntekik
       61 vtlgnsktvt fhfwdvggqe klrplwksyt rctdgivfvv dsvdvermee aktelhkitr
      121 isenqgvpvl ivankqdlrn slslseiekl lamgelssst pwhlqptcai igdglkegle
      181 klhdmiikrr kmlrqqkkkr
//
LOCUS       NP_001007759             486 aa            linear   ROD 27-APR-2025
DEFINITION  FMR1-interacting protein NUFIP1 [Rattus norvegicus].
ACCESSION   NP_001007759 XP_344439
VERSION     NP_001007759.1
DBSOURCE    REFSEQ: accession NM_001007758.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   McKeegan,K.S., Debieux,C.M., Boulon,S., Bertrand,E. and
            Watkins,N.J.
  TITLE     A dynamic scaffold of pre-snoRNP factors facilitates human box C/D
            snoRNP assembly
  JOURNAL   Mol Cell Biol 27 (19), 6782-6793 (2007)
   PUBMED   17636026
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Cabart,P., Chew,H.K. and Murphy,S.
  TITLE     BRCA1 cooperates with NUFIP and P-TEFb to activate transcription by
            RNA polymerase II
  JOURNAL   Oncogene 23 (31), 5316-5329 (2004)
   PUBMED   15107825
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Bardoni,B., Willemsen,R., Weiler,I.J., Schenck,A., Severijnen,L.A.,
            Hindelang,C., Lalli,E. and Mandel,J.L.
  TITLE     NUFIP1 (nuclear FMRP interacting protein 1) is a nucleocytoplasmic
            shuttling protein associated with active synaptoneurosomes
  JOURNAL   Exp Cell Res 289 (1), 95-107 (2003)
   PUBMED   12941608
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Bardoni,B., Schenck,A. and Mandel,J.L.
  TITLE     A novel RNA-binding nuclear protein that interacts with the fragile
            X mental retardation (FMR1) protein
  JOURNAL   Hum Mol Genet 8 (13), 2557-2566 (1999)
   PUBMED   10556305
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082111.1.
            
            On Nov 29, 2004 this sequence version replaced XP_344439.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082111.1, SRR8487227.239465.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..486
                     /product="FMR1-interacting protein NUFIP1"
                     /note="nuclear FMRP-interacting protein 1; NUFIP1, FMR1
                     interacting protein 1"
                     /calculated_mol_wt=54959
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W3.1)"
     Region          <4..140
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          166..190
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          209..261
                     /region_name="NUFIP1"
                     /note="Nuclear fragile X mental retardation-interacting
                     protein 1 (NUFIP1); pfam10453"
                     /db_xref="CDD:463096"
     Region          236..252
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W3.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHK0; propagated from
                     UniProtKB/Swiss-Prot (Q641W3.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHK0; propagated from
                     UniProtKB/Swiss-Prot (Q641W3.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHK0; propagated from
                     UniProtKB/Swiss-Prot (Q641W3.1)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHK0; propagated from
                     UniProtKB/Swiss-Prot (Q641W3.1)"
     CDS             1..486
                     /gene="Nufip1"
                     /coded_by="NM_001007758.1:4..1464"
                     /db_xref="GeneID:364430"
                     /db_xref="RGD:1359440"
ORIGIN      
        1 maeptpagwp sapeltpapg tpseaappqd nwvywamlpp pppplsspva gtepcqkeqp
       61 hvepqptsga fppfdaqilp aaqppfdaqa ppdgqsqfnd qqawnfqast pwywglspng
      121 fptyntsfhs pathsyfpqs yanyndfnlp qnrkqkkkkr kepvfhffcd tcdrgfknqe
      181 kydihmsehk kcpevdcsfs ahekivqfhw rnmhapgmkk ikldtpedia rwreerrkny
      241 ptlanierkk llqlekekrg evltttqygk mkgmsrhsqm akirspgkhy kwksggarqr
      301 avlglgnrar dlkpeiptkv nvdplgvlih sdsesdkdek sqraivpkev tpalcslmss
      361 ygnvsgsese peeapiktea evlaenrvlp ssppksprhn vrttartvlr akwkaqrsgl
      421 rkitlkqkks pchplfeprt rhphllemll apdirhernv ilqcvryiik kdffgltags
      481 vktedv
//
LOCUS       NP_671739                503 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 3A9 [Rattus norvegicus].
ACCESSION   NP_671739
VERSION     NP_671739.2
DBSOURCE    REFSEQ: accession NM_147206.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Li,X., Jin,X., Zhou,X., Wang,X., Shi,D., Xiao,Y. and Bi,D.
  TITLE     Pregnane X receptor is required for IFN-alpha-mediated CYP3A29
            expression in pigs
  JOURNAL   Biochem Biophys Res Commun 445 (2), 469-474 (2014)
   PUBMED   24525126
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Bedewy,A.M. and El-Maghraby,S.M.
  TITLE     Do SLCO1B3 (T334G) and CYP3A5*3 polymorphisms affect response in
            Egyptian chronic myeloid leukemia patients receiving imatinib
            therapy?
  JOURNAL   Hematology 18 (4), 211-216 (2013)
   PUBMED   23394475
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Xie,H., Liu,J. and Ling,T.Y.
  TITLE     [Expression of cytochrome P450 related genes in oral submucous
            fibrosis tissue]
  JOURNAL   Zhonghua Kou Qiang Yi Xue Za Zhi 47 (12), 743-747 (2012)
   PUBMED   23328101
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Silveira,V.S., Canalle,R., Scrideli,C.A., Queiroz,R.G., Lopes,L.F.
            and Tone,L.G.
  TITLE     CYP3A5 and NAT2 gene polymorphisms: role in childhood acute
            lymphoblastic leukemia risk and treatment outcome
  JOURNAL   Mol Cell Biochem 364 (1-2), 217-223 (2012)
   PUBMED   22215203
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Green,H., Khan,M.S., Jakobsen-Falk,I., Avall-Lundqvist,E. and
            Peterson,C.
  TITLE     Impact of CYP3A5*3 and CYP2C8-HapC on
            paclitaxel/carboplatin-induced myelosuppression in patients with
            ovarian cancer
  JOURNAL   J Pharm Sci 100 (10), 4205-4209 (2011)
   PUBMED   21702053
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Rowlands,J.C., Wang,H., Hakkak,R., Ronis,M.J., Strobel,H.W. and
            Badger,T.M.
  TITLE     Chronic intragastric infusion of ethanol-containing diets induces
            CYP3A9 while decreasing CYP3A2 in male rats
  JOURNAL   J Pharmacol Exp Ther 295 (2), 747-752 (2000)
   PUBMED   11046114
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Jager,W., Correia,M.A., Bornheim,L.M., Mahnke,A., Hanstein,W.G.,
            Xue,L. and Benet,L.Z.
  TITLE     Ethynylestradiol-mediated induction of hepatic CYP3A9 in female
            rats: implication for cyclosporine metabolism
  JOURNAL   Drug Metab Dispos 27 (12), 1505-1511 (1999)
   PUBMED   10570034
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Wang,H. and Strobel,H.W.
  TITLE     Regulation of CYP3A9 gene expression by estrogen and catalytic
            studies using cytochrome P450 3A9 expressed in Escherichia coli
  JOURNAL   Arch Biochem Biophys 344 (2), 365-372 (1997)
   PUBMED   9264551
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Mahnke,A., Strotkamp,D., Roos,P.H., Hanstein,W.G., Chabot,G.G. and
            Nef,P.
  TITLE     Expression and inducibility of cytochrome P450 3A9 (CYP3A9) and
            other members of the CYP3A subfamily in rat liver
  JOURNAL   Arch Biochem Biophys 337 (1), 62-68 (1997)
   PUBMED   8990268
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Wang,H., Kawashima,H. and Strobel,H.W.
  TITLE     cDNA cloning of a novel CYP3A from rat brain
  JOURNAL   Biochem Biophys Res Commun 221 (1), 157-162 (1996)
   PUBMED   8660328
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086985.1.
            
            On Apr 4, 2007 this sequence version replaced NP_671739.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086985.1, U60085.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..503
                     /product="cytochrome P450 3A9"
                     /EC_number="1.14.14.1"
                     /note="olfactory cytochrome P450olf3; 3AH15; CYPIIIA9;
                     P450-OLF3; olfactive; cytochrome P450-OLF3; cytochrome
                     P450 olfactive 3; cytochrome P450, family 3, subfamily a,
                     polypeptide 13"
                     /calculated_mol_wt=57647
     Region          67..492
                     /region_name="CYP3A"
                     /note="cytochrome P450 family 3, subfamily A; cd20650"
                     /db_xref="CDD:410743"
     Site            order(76,105..108,119..120,210,212..213,215,220,241,301,
                     304..305,309,370..372,374,481..482)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410743"
     Site            order(105,118..119,126,130,137,302,305..306,309,370,373,
                     375,434..437,440..444,448)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410743"
     CDS             1..503
                     /gene="Cyp3a9"
                     /gene_synonym="Cyp3a13; P450olf3"
                     /coded_by="NM_147206.2:93..1604"
                     /db_xref="GeneID:171352"
                     /db_xref="RGD:708392"
ORIGIN      
        1 mdlipnfsme twlllvislv llylygthsh gifkklgipg pkplpflgti layrkgfwef
       61 dkychkkygk lwglydgrqp vlaitdpdii ktvlvkecys tftnrrnfgp vgilkkaisi
      121 sedeewkrir allsptftsg klkemfpiin qytdmlvrnm rqgseegkpt smkdifgays
      181 mdvitatsfg vnvdslnnpq dpfvekikkl lkfdifdplf lsvtlfpflt plfealnvsm
      241 fprdvidffk tsvermkenr mkekekqrmd flqlminsqn skvkdshkal sdveivaqsv
      301 ififagyett ssalsfvlyl laihpdiqkk lqdeidaalp nkahatydtl lqmeyldmvv
      361 netlrlypia grlervcktd veingvfipk gtvvmiptfa lhkdphywpe peefrperfs
      421 kknqdninpy mylpfgngpr ncigmrfalm nmkvalvrvl qnfsfqpcke tqiplklskq
      481 gllqpekpll lkvvsrdetv nga
//
LOCUS       NP_001073676             608 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 652 [Rattus norvegicus].
ACCESSION   NP_001073676 XP_001081321 XP_573180
VERSION     NP_001073676.1
DBSOURCE    REFSEQ: accession NM_001080207.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC129097.1.
            
            On or before Jan 15, 2007 this sequence version replaced
            XP_573180.2, XP_001081321.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            40 bp suspected to be vector contamination from the 3' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129097.1, EV765444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..608
                     /product="zinc finger protein 652"
                     /calculated_mol_wt=69427
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1L1J6.1)"
     Region          60..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1J6.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1L1J6.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1L1J6.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D9; propagated from
                     UniProtKB/Swiss-Prot (A1L1J6.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D9; propagated from
                     UniProtKB/Swiss-Prot (A1L1J6.1)"
     Region          246..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          330..350
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          358..378
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <380..463
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          386..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(391,393,395,397..398,401..402,405,419,421,425..426,
                     429..430,433,447,449,451,453..454,457..458,461)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          414..434
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..>487
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          442..462
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..477
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          470..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..608
                     /region_name="Mediates interaction with CBFA2T3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1J6.1)"
     Region          540..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1L1J6.1)"
     CDS             1..608
                     /gene="Zfp652"
                     /gene_synonym="RGD1566329; Znf652"
                     /coded_by="NM_001080207.1:144..1970"
                     /db_xref="GeneID:497984"
                     /db_xref="RGD:1566329"
ORIGIN      
        1 msytaspcqe lvepcavhae gmaqeeshrs qapptfyhga sqeldlstkv ykresgspys
       61 vladskmskp hlheteeqpy frepravsdv htvkedrens ddteeeeevs ykreqiivev
      121 nlnnqtlnvs kgekgvssqs ketpvlktss eeeeeeteed atdnssdyge ngrqkkkekq
      181 vekvrvtqrr trraasvaaa ttsptprttr grrksaelpk rkkraakepk apvqkakcde
      241 ketltcekcp rvfntrwyle khmnvthrrm qicdkcgkkf vleselslhq qtdcekniqc
      301 vscnksfkkl wslhehikiv hgyaekkfac eicekkfytm ahvrkhmvah tkdmpftcet
      361 cgksfkrsms lkvhslqhsg ekpfrcencd erfqykyqlr shmsihighk qfmcqwcgkd
      421 fnmkqyfdeh mkthtgekpf iceicgksft srpnmkrhrr thtgekpypc dvcgqrfrfs
      481 nmlkahkekc frvtspvnvp pavqiplasa paapapavan tptspapavs mnpvgsalps
      541 rpvphpfshl hihthphhsh hlpippvphl ppppalfkse plnhrsqsed tflrhlaekn
      601 spaqaqhh
//
LOCUS       NP_476544                522 aa            linear   ROD 27-APR-2025
DEFINITION  BAR/IMD domain-containing adapter protein 2 [Rattus norvegicus].
ACCESSION   NP_476544
VERSION     NP_476544.1
DBSOURCE    REFSEQ: accession NM_057196.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Liu,F., Chen,Y., Zhao,S., Li,M., Luo,F. and Tang,C.E.
  TITLE     Insulin Receptor Substrate p53 Ameliorates High-Glucose-Induced
            Activation of NF-kappaB and Impaired Mobility of HUVECs
  JOURNAL   Biomed Res Int 2021, 3210586 (2021)
   PUBMED   33506012
  REMARK    GeneRIF: Insulin Receptor Substrate p53 Ameliorates
            High-Glucose-Induced Activation of NF-kappaB and Impaired Mobility
            of HUVECs.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Dosemeci,A., Burch,A., Loo,H., Toy,D. and Tao-Cheng,J.H.
  TITLE     IRSp53 accumulates at the postsynaptic density under excitatory
            conditions
  JOURNAL   PLoS One 12 (12), e0190250 (2017)
   PUBMED   29284046
  REMARK    GeneRIF: IRSp53 molecules may have a structural role organizing the
            Shank scaffold and/or linking the PSD to the actin cytoskeleton
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Chuang,H.C., Huang,T.N. and Hsueh,Y.P.
  TITLE     T-Brain-1--A Potential Master Regulator in Autism Spectrum
            Disorders
  JOURNAL   Autism Res 8 (4), 412-426 (2015)
   PUBMED   25600067
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Chen,C.J., Shih,C.H., Chang,Y.J., Hong,S.J., Li,T.N., Wang,L.H. and
            Chen,L.
  TITLE     SH2B1 and IRSp53 proteins promote the formation of dendrites and
            dendritic branches
  JOURNAL   J Biol Chem 290 (10), 6010-6021 (2015)
   PUBMED   25586189
  REMARK    GeneRIF: These findings suggest that SH2B1-IRSp53 complexes promote
            the formation of filopodia, neurite initiation, and neuronal
            branching.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Bockmann,J., Kreutz,M.R., Gundelfinger,E.D. and Bockers,T.M.
  TITLE     ProSAP/Shank postsynaptic density proteins interact with insulin
            receptor tyrosine kinase substrate IRSp53
  JOURNAL   J Neurochem 83 (4), 1013-1017 (2002)
   PUBMED   12421375
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Okamura-Oho,Y., Miyashita,T. and Yamada,M.
  TITLE     Distinctive tissue distribution and phosphorylation of IRSp53
            isoforms
  JOURNAL   Biochem Biophys Res Commun 289 (5), 957-960 (2001)
   PUBMED   11741283
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Krugmann,S., Jordens,I., Gevaert,K., Driessens,M.,
            Vandekerckhove,J. and Hall,A.
  TITLE     Cdc42 induces filopodia by promoting the formation of an
            IRSp53:Mena complex
  JOURNAL   Curr Biol 11 (21), 1645-1655 (2001)
   PUBMED   11696321
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Thomas,E.A., Foye,P.E., Alvarez,C.E., Usui,H. and Sutcliffe,J.G.
  TITLE     Insulin receptor substrate protein p53 localization in rats
            suggests mechanism for specific polyglutamine neurodegeneration
  JOURNAL   Neurosci Lett 309 (3), 145-148 (2001)
   PUBMED   11514062
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Okamura-Oho,Y., Miyashita,T., Ohmi,K. and Yamada,M.
  TITLE     Dentatorubral-pallidoluysian atrophy protein interacts through a
            proline-rich region near polyglutamine with the SH3 domain of an
            insulin receptor tyrosine kinase substrate
  JOURNAL   Hum Mol Genet 8 (6), 947-957 (1999)
   PUBMED   10332026
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY037934.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY037934.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..522
                     /product="BAR/IMD domain-containing adapter protein 2"
                     /note="insulin receptor substrate 53; BAI-associated
                     protein 2; insulin receptor substrate p53; insulin
                     receptor substrate protein of 53 kDa; insulin receptor
                     tyrosine kinase substrate protein p53; brain-specific
                     angiogenesis inhibitor 1-associated protein 2;
                     BAI1-associated protein 2; brain-specific angiogenesis
                     inhibitor 1-associated protein 2-like"
                     /calculated_mol_wt=57411
     Region          5..236
                     /region_name="I-BAR_IMD_IRSp53"
                     /note="Inverse (I)-BAR, also known as the IRSp53/MIM
                     homology Domain (IMD), of Insulin Receptor tyrosine kinase
                     Substrate p53; cd07646"
                     /db_xref="CDD:153330"
     Site            order(5,9,12,15..16,23..24,27..28,31,34..35,37..38,41..42,
                     44..45,48..49,51..52,55..56,58..59,62..63,66..69,71..72,
                     75..76,79,86,97,101,176,180,183..184,187..188,190..192,
                     194..195,197..199,201..202,205..206,208..209,211..213,216,
                     219,223,226..227,229..230,232..233,235..236)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153330"
     Site            order(11,23,143)
                     /site_type="other"
                     /note="putative Rac binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:153330"
     Site            order(108,130,147,171)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153330"
     Site            order(142,145,147)
                     /site_type="other"
                     /note="putative actin binding residues [polypeptide
                     binding]"
                     /db_xref="CDD:153330"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Region          308..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Region          378..436
                     /region_name="SH3_Irsp53"
                     /note="Src Homology 3 domain of Insulin Receptor tyrosine
                     kinase Substrate p53; cd11915"
                     /db_xref="CDD:212848"
     Site            order(383..384,386,393..394,406..407,412..414,416,
                     426..427,429..432)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212848"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQB8; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKX1; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Region          445..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6GMN2.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6GMN2.1)"
     CDS             1..522
                     /gene="Baiap2"
                     /gene_synonym="Irsp53"
                     /coded_by="NM_057196.1:62..1630"
                     /db_xref="GeneID:117542"
                     /db_xref="RGD:619814"
ORIGIN      
        1 mslsrseemh rltenvykti meqfnpslrn fiamgknyek alagvtfaak gyfdalvkmg
       61 elasesqgsk elgdvlfqma evhrqiqnql eemlkafhne lltqleqkve ldsrylsaal
      121 kkyqteqrsk gdaldkcqae lkklrkksqg sknpqkysdk elqyidaisn kqgelenyvs
      181 dgyktaltee rrrfcflvek qcavaknsaa yhskgkella qklplwqqac adpnkipdra
      241 aqlmqqmans ngsilpsals asksnlvisd pipgakplpv ppelapfvgr msaqenvpvm
      301 ngvagadsed ynpwadrkaa qpkslsppqs qsklsdsysn tlpvrksvtp knsyattenk
      361 tlprsssmaa glerngrmrv kaifshaagd nstllsfkeg dlitllvpea rdgwhygese
      421 ktkmrgwfpf sytrvldsdg sdrlhmslqq gkssstgnll dkddlalppp dygtssrafp
      481 sqtagtfkqr pysvavpafs qglddygars vssgsgtlvs tv
//
LOCUS       NP_116003                337 aa            linear   ROD 27-APR-2025
DEFINITION  glutaredoxin-3 [Rattus norvegicus].
ACCESSION   NP_116003
VERSION     NP_116003.2
DBSOURCE    REFSEQ: accession NM_032614.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Frey,A.G., Palenchar,D.J., Wildemann,J.D. and Philpott,C.C.
  TITLE     A Glutaredoxin.BolA Complex Serves as an Iron-Sulfur Cluster
            Chaperone for the Cytosolic Cluster Assembly Machinery
  JOURNAL   J Biol Chem 291 (43), 22344-22356 (2016)
   PUBMED   27519415
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Banci,L., Ciofi-Baffoni,S., Gajda,K., Muzzioli,R., Peruzzini,R. and
            Winkelmann,J.
  TITLE     N-terminal domains mediate [2Fe-2S] cluster transfer from
            glutaredoxin-3 to anamorsin
  JOURNAL   Nat Chem Biol 11 (10), 772-778 (2015)
   PUBMED   26302480
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Aon-Bertolino,M.L., Romero,J.I., Galeano,P., Holubiec,M.,
            Badorrey,M.S., Saraceno,G.E., Hanschmann,E.M., Lillig,C.H. and
            Capani,F.
  TITLE     Thioredoxin and glutaredoxin system proteins-immunolocalization in
            the rat central nervous system
  JOURNAL   Biochim Biophys Acta 1810 (1), 93-110 (2011)
   PUBMED   20620191
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Jeong,D., Kim,J.M., Cha,H., Oh,J.G., Park,J., Yun,S.H., Ju,E.S.,
            Jeon,E.S., Hajjar,R.J. and Park,W.J.
  TITLE     PICOT attenuates cardiac hypertrophy by disrupting calcineurin-NFAT
            signaling
  JOURNAL   Circ Res 102 (6), 711-719 (2008)
   PUBMED   18258855
  REMARK    GeneRIF: Data suggest that PICOT inhibits cardiac hypertrophy
            largely by negatively regulating calcineurin-NFAT signaling via
            disruption of the MLP-calcineurin interaction.
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Witte,S., Villalba,M., Bi,K., Liu,Y., Isakov,N. and Altman,A.
  TITLE     Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB
            pathways by PICOT, a novel protein kinase C-interacting protein
            with a thioredoxin homology domain
  JOURNAL   J Biol Chem 275 (3), 1902-1909 (2000)
   PUBMED   10636891
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086381.1.
            
            On Oct 27, 2005 this sequence version replaced NP_116003.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086381.1, CF110478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..337
                     /product="glutaredoxin-3"
                     /note="thioredoxin-like 2; PKCq-interacting protein;
                     thioredoxin-like protein 2; PKC-theta-interacting protein;
                     PKC-interacting cousin of thioredoxin"
                     /calculated_mol_wt=37718
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (Q9JLZ1.2)"
     Region          20..115
                     /region_name="TRX_PICOT"
                     /note="TRX domain, PICOT (for PKC-interacting cousin of
                     TRX) subfamily; PICOT is a protein that interacts with
                     protein kinase C (PKC) theta, a calcium independent PKC
                     isoform selectively expressed in skeletal muscle and T
                     lymphocytes. PICOT contains an...; cd02984"
                     /db_xref="CDD:239282"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O76003; propagated from
                     UniProtKB/Swiss-Prot (Q9JLZ1.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O76003; propagated from
                     UniProtKB/Swiss-Prot (Q9JLZ1.2)"
     Region          139..227
                     /region_name="GRX_PICOT_like"
                     /note="Glutaredoxin (GRX) family, PKC-interacting cousin
                     of TRX (PICOT)-like subfamily; composed of PICOT and
                     GRX-PICOT-like proteins. The non-PICOT members of this
                     family contain only the GRX-like domain, whereas PICOT
                     contains an N-terminal TRX-like domain...; cd03028"
                     /db_xref="CDD:239326"
     Site            order(153,161..163,201..202)
                     /site_type="other"
                     /note="putative GSH binding site [chemical binding]"
                     /db_xref="CDD:239326"
     Site            order(161,164)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239326"
     Region          241..329
                     /region_name="GRX_PICOT_like"
                     /note="Glutaredoxin (GRX) family, PKC-interacting cousin
                     of TRX (PICOT)-like subfamily; composed of PICOT and
                     GRX-PICOT-like proteins. The non-PICOT members of this
                     family contain only the GRX-like domain, whereas PICOT
                     contains an N-terminal TRX-like domain...; cd03028"
                     /db_xref="CDD:239326"
     Site            order(255,263..265,303..304)
                     /site_type="other"
                     /note="putative GSH binding site [chemical binding]"
                     /db_xref="CDD:239326"
     Site            order(263,266)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239326"
     CDS             1..337
                     /gene="Glrx3"
                     /gene_synonym="PICOT; Txnl2"
                     /coded_by="NM_032614.2:7..1020"
                     /db_xref="GeneID:58815"
                     /db_xref="RGD:69414"
ORIGIN      
        1 maagaaeaae aavavvevgs arqfeellrl ktksllvvhf wapwapqcvq mndvmaelak
       61 ehphvsfvkl eaeavpevse kyeissvptf lffknsqkvd rldgahapel tkkvqrhvss
      121 gsfppstneh vkedlnlrlk klthaapcml fmkgtpqepr cgfskqmvei lhkhniqfss
      181 fdifsdeevr qglktysnwp typqlyvsge liggldiike leaseeldti cpkapkleer
      241 lkvltnkasv mlfmkgnkqe akcgfskqil eilnstgvey etfdiledee vrqglktfsn
      301 wptypqlyvr gdlvggldiv kelkdngell pilkgen
//
LOCUS       NP_543181                282 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase SIAH1 [Rattus norvegicus].
ACCESSION   NP_543181
VERSION     NP_543181.2
DBSOURCE    REFSEQ: accession NM_080905.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Tian,X., Gong,L., Jin,A., Wang,Y., Zhou,X. and Tan,Y.
  TITLE     E3 ubiquitin ligase siah-1 nuclear accumulation is critical for
            homocysteine-induced impairment of C6 astroglioma cells
  JOURNAL   Mol Med Rep 20 (3), 2227-2235 (2019)
   PUBMED   31322210
  REMARK    GeneRIF: These findings suggest that siah1 is involved in
            homocysteineinduced cell damage by promoting the nuclear
            translocation of glyceraldehyde 3phosphate dehydrogenase .
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Huo,J., Ma,R., Chai,X., Liang,H.J., Jiang,P., Zhu,X.L., Chen,X. and
            Su,B.X.
  TITLE     Inhibiting a spinal cord signaling pathway protects against
            ischemia injury in rats
  JOURNAL   J Thorac Cardiovasc Surg 157 (2), 494-503 (2019)
   PUBMED   30195603
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Huo,J., Zhu,X.L., Ma,R., Dong,H.L. and Su,B.X.
  TITLE     GAPDH/Siah1 cascade is involved in traumatic spinal cord injury and
            could be attenuated by sivelestat sodium
  JOURNAL   Neuroscience 330, 171-180 (2016)
   PUBMED   27256506
  REMARK    GeneRIF: Study reveals GAPDH/Siah1 as a novel signaling pathway in
            apoptosis and function recovery after traumatic spinal cord injury.
            This signaling pathway in the spinal cord can be blocked by
            sivelestat sodium.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Kilanczyk,E., Filipek,A. and Hetman,M.
  TITLE     Calcyclin-binding protein/Siah-1-interacting protein as a regulator
            of transcriptional responses in brain cells
  JOURNAL   J Neurosci Res 93 (1), 75-81 (2015)
   PUBMED   25163685
  REMARK    GeneRIF: The results of this study indicated that CacyBP/SIP is a
            novel regulator of CRE- and NFAT-driven transcription.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Waites,C.L., Leal-Ortiz,S.A., Okerlund,N., Dalke,H., Fejtova,A.,
            Altrock,W.D., Gundelfinger,E.D. and Garner,C.C.
  TITLE     Bassoon and Piccolo maintain synapse integrity by regulating
            protein ubiquitination and degradation
  JOURNAL   EMBO J 32 (7), 954-969 (2013)
   PUBMED   23403927
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Wheeler,T.C., Chin,L.S., Li,Y., Roudabush,F.L. and Li,L.
  TITLE     Regulation of synaptophysin degradation by mammalian homologues of
            seven in absentia
  JOURNAL   J Biol Chem 277 (12), 10273-10282 (2002)
   PUBMED   11786535
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Liu,J., Stevens,J., Rote,C.A., Yost,H.J., Hu,Y., Neufeld,K.L.,
            White,R.L. and Matsunami,N.
  TITLE     Siah-1 mediates a novel beta-catenin degradation pathway linking
            p53 to the adenomatous polyposis coli protein
  JOURNAL   Mol Cell 7 (5), 927-936 (2001)
   PUBMED   11389840
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Kammermeier,P.J. and Ikeda,S.R.
  TITLE     A role for Seven in Absentia Homolog (Siah1a) in metabotropic
            glutamate receptor signaling
  JOURNAL   BMC Neurosci 2, 15 (2001)
   PUBMED   11686852
  REMARK    GeneRIF: Binds group I metabotropic glutamate receptors and
            calmodulin; calmodulin binding may play a role in the regulation of
            group I mGluR function
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Ishikawa,K., Nash,S.R., Nishimune,A., Neki,A., Kaneko,S. and
            Nakanishi,S.
  TITLE     Competitive interaction of seven in absentia homolog-1A and
            Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic
            glutamate receptors
  JOURNAL   Genes Cells 4 (7), 381-390 (1999)
   PUBMED   10469171
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Wicker,C. and Puigserver,A.
  TITLE     Rat pancreatic colipase mRNA: nucleotide sequence of a cDNA clone
            and nutritional regulation by a lipidic diet
  JOURNAL   Biochem Biophys Res Commun 167 (1), 130-136 (1990)
   PUBMED   2129524
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV213782.1, AF389476.1 and BQ780107.1.
            
            On Dec 1, 2005 this sequence version replaced NP_543181.1.
            
            Sequence Note: This RefSeq record was created using sequences from
            two different strains, W and Sprague-Dawley, because no single
            transcript from the same strain was available for the full length
            of the gene.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV213782.1, CB746687.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..282
                     /product="E3 ubiquitin-protein ligase SIAH1"
                     /EC_number="2.3.2.27"
                     /note="siah-1; siah-1a; seven in absentia homolog 1; seven
                     in absentia 1A; RING-type E3 ubiquitin transferase SIAH1"
                     /calculated_mol_wt=31006
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920M9.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000250|UniProtKB:Q8IUQ4; propagated from
                     UniProtKB/Swiss-Prot (Q920M9.2)"
     Region          36..86
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(41,44,55,59,62,65,72,75)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     Region          82..278
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          90..282
                     /region_name="SBD. /evidence=ECO:0000250|UniProtKB:P61092"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920M9.2)"
     CDS             1..282
                     /gene="Siah1"
                     /gene_synonym="SIAH; Siah1a"
                     /coded_by="NM_080905.2:181..1029"
                     /db_xref="GeneID:140941"
                     /db_xref="RGD:620449"
ORIGIN      
        1 msrqtatalp tgtskcppsq rvpaltgtta snndlaslfe cpvcfdyvlp pilqcqsghl
       61 vcsncrpklt ccptcrgplg sirnlamekv ansvlfpcky assgceitlp htekaeheel
      121 cefrpyscpc pgasckwqgs ldavmphlmh qhksittlqg edivflatdi nlpgavdwvm
      181 mqscfgfhfm lvlekqekyd ghqqffaivq ligtrkqaen fayrlelngh rrrltweatp
      241 rsihegiata imnsdclvfd tsiaqlfaen gnlginvtis mc
//
LOCUS       NP_001013227             357 aa            linear   ROD 27-APR-2025
DEFINITION  dnaJ homolog subfamily B member 6 [Rattus norvegicus].
ACCESSION   NP_001013227 XP_342608
VERSION     NP_001013227.1
DBSOURCE    REFSEQ: accession NM_001013209.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Smith,C. and D'Mello,S.R.
  TITLE     Cell and Context-Dependent Effects of the Heat Shock Protein DNAJB6
            on Neuronal Survival
  JOURNAL   Mol Neurobiol 53 (8), 5628-5639 (2016)
   PUBMED   26476842
  REMARK    GeneRIF: These results conclude that neurotoxicity resulting from
            elevated DNAJB6 is cell cycle dependent.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Sarparanta,J., Jonson,P.H., Golzio,C., Sandell,S., Luque,H.,
            Screen,M., McDonald,K., Stajich,J.M., Mahjneh,I., Vihola,A.,
            Raheem,O., Penttila,S., Lehtinen,S., Huovinen,S., Palmio,J.,
            Tasca,G., Ricci,E., Hackman,P., Hauser,M., Katsanis,N. and Udd,B.
  TITLE     Mutations affecting the cytoplasmic functions of the co-chaperone
            DNAJB6 cause limb-girdle muscular dystrophy
  JOURNAL   Nat Genet 44 (4), 450-455,S1-S2 (2012)
   PUBMED   22366786
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Watson,E.D., Hughes,M., Simmons,D.G., Natale,D.R., Sutherland,A.E.
            and Cross,J.C.
  TITLE     Cell-cell adhesion defects in Mrj mutant trophoblast cells are
            associated with failure to pattern the chorion during early
            placental development
  JOURNAL   Dev Dyn 240 (11), 2505-2519 (2011)
   PUBMED   21972064
REFERENCE   4  (residues 1 to 357)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Hageman,J., van Waarde,M.A., Zylicz,A., Walerych,D. and
            Kampinga,H.H.
  TITLE     The diverse members of the mammalian HSP70 machine show distinct
            chaperone-like activities
  JOURNAL   Biochem J 435 (1), 127-142 (2011)
   PUBMED   21231916
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Zhang,Y., Yang,Z., Cao,Y., Zhang,S., Li,H., Huang,Y., Ding,Y.Q. and
            Liu,X.
  TITLE     The Hsp40 family chaperone protein DnaJB6 enhances Schlafen1
            nuclear localization which is critical for promotion of cell-cycle
            arrest in T-cells
  JOURNAL   Biochem J 413 (2), 239-250 (2008)
   PUBMED   18373498
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Dai,Y.S., Xu,J. and Molkentin,J.D.
  TITLE     The DnaJ-related factor Mrj interacts with nuclear factor of
            activated T cells c3 and mediates transcriptional repression
            through class II histone deacetylase recruitment
  JOURNAL   Mol Cell Biol 25 (22), 9936-9948 (2005)
   PUBMED   16260608
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Chuang,J.Z., Zhou,H., Zhu,M., Li,S.H., Li,X.J. and Sung,C.H.
  TITLE     Characterization of a brain-enriched chaperone, MRJ, that inhibits
            Huntingtin aggregation and toxicity independently
  JOURNAL   J Biol Chem 277 (22), 19831-19838 (2002)
   PUBMED   11896048
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Izawa,I., Nishizawa,M., Ohtakara,K., Ohtsuka,K., Inada,H. and
            Inagaki,M.
  TITLE     Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin
            8/18 filament regulatory protein
  JOURNAL   J Biol Chem 275 (44), 34521-34527 (2000)
   PUBMED   10954706
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Hunter,P.J., Swanson,B.J., Haendel,M.A., Lyons,G.E. and Cross,J.C.
  TITLE     Mrj encodes a DnaJ-related co-chaperone that is essential for
            murine placental development
  JOURNAL   Development 126 (6), 1247-1258 (1999)
   PUBMED   10021343
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078908.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342608.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078908.1, SRR8487231.173067.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..357
                     /product="dnaJ homolog subfamily B member 6"
                     /note="MRJ; HSJ-2; MSJ-1; hsp40 homolog; heat shock
                     protein J2; DnaJ (Hsp40) homolog, subfamily B, member 6"
                     /calculated_mol_wt=38791
     Region          2..147
                     /region_name="Interaction with HSP70.
                     /evidence=ECO:0000250|UniProtKB:O75190"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU3.1)"
     Region          3..>108
                     /region_name="PRK10767"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:236757"
     Region          120..243
                     /region_name="Interaction with KRT18.
                     /evidence=ECO:0000250|UniProtKB:O75190"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU3.1)"
     Site            136
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54946; propagated from
                     UniProtKB/Swiss-Prot (Q6AYU3.1)"
     Region          243..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYU3.1)"
     CDS             1..357
                     /gene="Dnajb6"
                     /coded_by="NM_001013209.1:118..1191"
                     /db_xref="GeneID:362293"
                     /db_xref="RGD:1308207"
ORIGIN      
        1 mvdyyevlgv qrhaspedik kayrkqalkw hpdknpenke eaerkfkqva eayevlsdak
       61 krdiydkygk eglngggggg gshfdspfef gftfrnpddv freffggrdp fsfdffedpf
      121 ddffgnrrgp rgsrsrgags ffsafsgfps fgsgfpafdt gftpfgslgh ggltsfssas
      181 fggsgmgnfk siststkivn gkkittkriv engqerveve edgqlkslti ngvadenala
      241 eecrrrgqpt palapgpapa parvpsqarp ptpaptpapa qtpapsvstr pqkpprpapt
      301 aklvsksnwe deeqdrqrvp gncdapmtsa glkeggkrkk qkqkedskkk kstkgnh
//
LOCUS       NP_001020905             432 aa            linear   ROD 27-APR-2025
DEFINITION  transcriptional adapter 3 [Rattus norvegicus].
ACCESSION   NP_001020905 XP_575640
VERSION     NP_001020905.1
DBSOURCE    REFSEQ: accession NM_001025734.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Li,C.W., Ai,N., Dinh,G.K., Welsh,W.J. and Chen,J.D.
  TITLE     Human ADA3 regulates RARalpha transcriptional activity through
            direct contact between LxxLL motifs and the receptor coactivator
            pocket
  JOURNAL   Nucleic Acids Res 38 (16), 5291-5303 (2010)
   PUBMED   20413580
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Krebs,A.R., Demmers,J., Karmodiya,K., Chang,N.C., Chang,A.C. and
            Tora,L.
  TITLE     ATAC and Mediator coactivators form a stable complex and regulate a
            set of non-coding RNA genes
  JOURNAL   EMBO Rep 11 (7), 541-547 (2010)
   PUBMED   20508642
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Kurabe,N., Katagiri,K., Komiya,Y., Ito,R., Sugiyama,A., Kawasaki,Y.
            and Tashiro,F.
  TITLE     Deregulated expression of a novel component of TFTC/STAGA histone
            acetyltransferase complexes, rat SGF29, in hepatocellular
            carcinoma: possible implication for the oncogenic potential of
            c-Myc
  JOURNAL   Oncogene 26 (38), 5626-5634 (2007)
   PUBMED   17334388
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Benecke,A., Gaudon,C., Garnier,J.M., vom Baur,E., Chambon,P. and
            Losson,R.
  TITLE     ADA3-containing complexes associate with estrogen receptor alpha
  JOURNAL   Nucleic Acids Res 30 (11), 2508-2514 (2002)
   PUBMED   12034840
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Brand,M., Yamamoto,K., Staub,A. and Tora,L.
  TITLE     Identification of TATA-binding protein-free TAFII-containing
            complex subunits suggests a role in nucleosome acetylation and
            signal transduction
  JOURNAL   J Biol Chem 274 (26), 18285-18289 (1999)
   PUBMED   10373431
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097414.1.
            
            On Jul 22, 2005 this sequence version replaced XP_575640.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097414.1, SRR8487227.54958.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..432
                     /product="transcriptional adapter 3"
                     /note="ADA3 homolog; ADA3-like protein"
                     /calculated_mol_wt=48767
     Region          87..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8F5.1)"
     Region          272..319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8F5.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75528; propagated from
                     UniProtKB/Swiss-Prot (Q4V8F5.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75528; propagated from
                     UniProtKB/Swiss-Prot (Q4V8F5.1)"
     Region          309..422
                     /region_name="Ada3"
                     /note="Histone acetyltransferases subunit 3; pfam10198"
                     /db_xref="CDD:462993"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75528; propagated from
                     UniProtKB/Swiss-Prot (Q4V8F5.1)"
     CDS             1..432
                     /gene="Tada3"
                     /gene_synonym="Tada3l"
                     /coded_by="NM_001025734.1:307..1605"
                     /db_xref="GeneID:362414"
                     /db_xref="RGD:1564009"
ORIGIN      
        1 mselkdcplq fhdfksvdhm kvcprytavl arseddgigi eeldtlqlel etllssasrr
       61 lrvleaetqi ltdwqdkkgd rrilklardh elgappkhgk pkkqklegkt ghgpgpgpgr
      121 pksknvqpki qeyeftddpi dvpripknda pnrfwasvep ycaditseev rtleellkpp
      181 edeaehykip plgkhysqrw aqedlleeqk dgaraaavad kkkgligplt eldtkdvdal
      241 lkkseaqheq pedgcpfgal tqrllqalve eniispmeds pipdmsgkes gadgastspr
      301 nqnkpfsvph tkslesrike eliaqglles edrpaedsed evlaelrkrq aelkalsahn
      361 rtkkhdllrl akeevsrqel rqrvrmadne vmdafrkima arqkkrtptk kekdqawktl
      421 keresilkll dg
//
LOCUS       NP_001007670             468 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 672 [Rattus norvegicus].
ACCESSION   NP_001007670 XP_220456
VERSION     NP_001007670.1
DBSOURCE    REFSEQ: accession NM_001007669.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081919.1.
            
            On Nov 29, 2004 this sequence version replaced XP_220456.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081919.1, CA510973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..468
                     /product="zinc finger protein 672"
                     /calculated_mol_wt=52033
     Region          13..416
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          17..37
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(22,24,26,28..29,32..33,36,50,52,56..57,60..61,64,78,
                     80,82,84..85,88..89,92)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          45..65
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          73..93
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          102..123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          169..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          204..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(209,211,213,215..216,219..220,223,237,239,243..244,
                     247..248,251,265,267,269,271..272,275..276,279)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          232..252
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(293,295,297,299..300,303..304,307,321,323,327..328,
                     331..332,335,349,351,353,355..356,359..360,363)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..468
                     /gene="Zfp672"
                     /gene_synonym="Znf672"
                     /coded_by="NM_001007669.1:510..1916"
                     /db_xref="GeneID:303165"
                     /db_xref="RGD:1359094"
ORIGIN      
        1 mftapgvaat rerpyscsvc gksfqysavl lrherahggd krfrclecge rcarasdlrv
       61 hrwthagqtl yicsecgqsf shsslldlhl gthrrrsstc pcrlcgrrfp hvsalllhrv
      121 rqhppekphr cplcarsfrq salpfhlara hppettiata papstlyhct qcprafhssa
      181 glrnhsrihv vpslsdpgae ahrcgvcgks fsksstltrh lqrhsgekpf kcpecgkgfl
      241 esatlvrhqr thtgekpyac ndcgrcfses stllrhqrsh qgerphicat cgkgfgqryd
      301 lvvhqrshtg erpfpcpecg rgftdrsdlt khlrthtgek pyhcelcgkr ftcisnlnvh
      361 lrnhaghkph kcpecgksfs vasklalhrk thlgertaec tecgkffshg rslsqhqrsh
      421 rraraaamaa tttttvvtem tigpsltltg pteqeksgll vstfqetc
//
LOCUS       NP_001009693             951 aa            linear   ROD 27-APR-2025
DEFINITION  thyroid hormone receptor-associated protein 3 [Rattus norvegicus].
ACCESSION   NP_001009693 XP_233523
VERSION     NP_001009693.1
DBSOURCE    REFSEQ: accession NM_001009693.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Horiuchi,K., Kawamura,T., Iwanari,H., Ohashi,R., Naito,M.,
            Kodama,T. and Hamakubo,T.
  TITLE     Identification of Wilms' tumor 1-associating protein complex and
            its role in alternative splicing and the cell cycle
  JOURNAL   J Biol Chem 288 (46), 33292-33302 (2013)
   PUBMED   24100041
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Lande-Diner,L., Boyault,C., Kim,J.Y. and Weitz,C.J.
  TITLE     A positive feedback loop links circadian clock factor CLOCK-BMAL1
            to the basic transcriptional machinery
  JOURNAL   Proc Natl Acad Sci U S A 110 (40), 16021-16026 (2013)
   PUBMED   24043798
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Heyd,F. and Lynch,K.W.
  TITLE     Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
            alternative splicing
  JOURNAL   Mol Cell 40 (1), 126-137 (2010)
   PUBMED   20932480
REFERENCE   6  (residues 1 to 951)
  AUTHORS   Ito,M., Okano,H.J., Darnell,R.B. and Roeder,R.G.
  TITLE     The TRAP100 component of the TRAP/Mediator complex is essential in
            broad transcriptional events and development
  JOURNAL   EMBO J 21 (13), 3464-3475 (2002)
   PUBMED   12093747
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Ge,K., Guermah,M., Yuan,C.X., Ito,M., Wallberg,A.E.,
            Spiegelman,B.M. and Roeder,R.G.
  TITLE     Transcription coactivator TRAP220 is required for PPAR gamma
            2-stimulated adipogenesis
  JOURNAL   Nature 417 (6888), 563-567 (2002)
   PUBMED   12037571
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Kang,Y.K., Guermah,M., Yuan,C.X. and Roeder,R.G.
  TITLE     The TRAP/Mediator coactivator complex interacts directly with
            estrogen receptors alpha and beta through the TRAP220 subunit and
            directly enhances estrogen receptor function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2642-2647 (2002)
   PUBMED   11867769
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 951)
  AUTHORS   Ito,M., Yuan,C.X., Malik,S., Gu,W., Fondell,J.D., Yamamura,S.,
            Fu,Z.Y., Zhang,X., Qin,J. and Roeder,R.G.
  TITLE     Identity between TRAP and SMCC complexes indicates novel pathways
            for the function of nuclear receptors and diverse mammalian
            activators
  JOURNAL   Mol Cell 3 (3), 361-370 (1999)
   PUBMED   10198638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088415.1.
            
            On Jan 13, 2005 this sequence version replaced XP_233523.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088415.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..951
                     /product="thyroid hormone receptor-associated protein 3"
                     /note="trap150; thyroid hormone receptor-associated
                     protein complex 150 kDa component"
                     /calculated_mol_wt=108122
     Region          1..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          2..190
                     /region_name="Required for mRNA splicing activation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            17
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            66
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            101
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            108
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          117..558
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          248..766
                     /region_name="THRAP3_BCLAF1"
                     /note="THRAP3/BCLAF1 family; pfam15440"
                     /db_xref="CDD:464718"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            252
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            346
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          359..951
                     /region_name="Required for mRNA decay activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            452
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            468
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            476
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            516
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            555
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          659..951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            808
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            841
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q569Z6; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Region          <857..>923
                     /region_name="Btz"
                     /note="CASC3/Barentsz eIF4AIII binding; cl09653"
                     /db_xref="CDD:447763"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W1; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5M7V8.1)"
     CDS             1..951
                     /gene="Thrap3"
                     /coded_by="NM_001009693.1:159..3014"
                     /db_xref="GeneID:313591"
                     /db_xref="RGD:1306129"
ORIGIN      
        1 msktnksksg srssrsrsas rsrsrsfsks rsrsrsvsrs rkrrlssrsr srsyspahnr
       61 ernhprvyqn rdfrghnrgy rrpyyfrgrn rgfypwgqyn rggygnyrsn wqnyrqaysp
      121 rrgrsrsrsp krrspsprsr shsrnsdkss sdrsrrssss rsssnhsrve sskrkstkek
      181 kssskdsrps qaagdnqgde akeqtfsggt sqdikgsess kpwpdattyg tgsasrasvs
      241 dlsprerspa lksplqsvvv rrrsprpspv pkpspplsna sqmgssmsgg agyqsgahqg
      301 pfdhgsgsls pskkspvgks ppatgsaygs sqkeesaasg gaaytkryle eqktengkdk
      361 eqkqtntdke klkekggfsd advkmksdpf apktdtekpf rgsqspkryk lrddfekkma
      421 dfhkeemdeq dkdkckgrke pefddepkfi skviagaskn qeeeksgkwe slhagkekqr
      481 kaeeleeepf tersrkeerg gskrsesghr gfvpeknfrv taykavqeks ssppprktse
      541 srdklgnkgd fssgkssfsi treaqvnvrm dsfdedlarp sgllaqerkl crdlvhsnkk
      601 eqefrsifqh iqsaqsqrsp selfaqhivt ivhhvkehhf gssgmtlher ftkylkrgne
      661 qeaaktkksp eihrridisp stfrkhglth eelksprepg ykaegkykdd pvdlrldier
      721 rkkhkerdlk rgksresvds rdsshsrers tektekthkg skkqkkhrra rdrsrsssss
      781 sqsshsykae eypeeaedre esttgfdksr lgtkdfvgpn erggrargtf qfrargrgwg
      841 rgnysgnnnn nsnndfqkrs reeewdpeyt pkskkyylhd dregegsdkw msrgrgrgaf
      901 prgrgrfmfr ksstspkwah dkfsgeegei eddesgtenr eekdslqpsa e
//
LOCUS       NP_077327                646 aa            linear   ROD 27-APR-2025
DEFINITION  heat shock cognate 71 kDa protein [Rattus norvegicus].
ACCESSION   NP_077327 XP_001053026
VERSION     NP_077327.1
DBSOURCE    REFSEQ: accession NM_024351.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Xu,S., Liu,S., Yang,J., Li,R., Mao,M., Feng,S. and Wang,X.
  TITLE     miR-3120/Hsc70 participates in forced swim stress-induced
            mechanical hyperalgesia in rats in an inflammatory state
  JOURNAL   Mol Med Rep 29 (1) (2024)
   PUBMED   37947174
  REMARK    GeneRIF: miR-3120/Hsc70 participates in forced swim stress-induced
            mechanical hyperalgesia in rats in an inflammatory state.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Mi,J., Yang,Y., Yao,H., Huan,Z., Xu,C., Ren,Z., Li,W., Tang,Y.,
            Fu,R. and Ge,X.
  TITLE     Inhibition of heat shock protein family A member 8 attenuates
            spinal cord ischemia-reperfusion injury via astrocyte
            NF-kappaB/NLRP3 inflammasome pathway : HSPA8 inhibition protects
            spinal ischemia-reperfusion injury
  JOURNAL   J Neuroinflammation 18 (1), 170 (2021)
   PUBMED   34362408
  REMARK    GeneRIF: Inhibition of heat shock protein family A member 8
            attenuates spinal cord ischemia-reperfusion injury via astrocyte
            NF-kappaB/NLRP3 inflammasome pathway : HSPA8 inhibition protects
            spinal ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Dong,F. and Zhang,J.
  TITLE     Carboxyl terminus of Hsc70-interacting protein (CHIP) promotes
            pulmonary artery smooth muscle cell (PASMC) proliferation via
            enhancement of intracellular Ca2+ concentration ([Ca2+]i)
  JOURNAL   Exp Lung Res 46 (9), 332-340 (2020)
   PUBMED   32873086
  REMARK    GeneRIF: Carboxyl terminus of Hsc70-interacting protein (CHIP)
            promotes pulmonary artery smooth muscle cell (PASMC) proliferation
            via enhancement of intracellular Ca(2+) concentration ([Ca(2+)]i).
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Sahni,S., Krisp,C., Molloy,M.P., Nahm,C., Maloney,S., Gillson,J.,
            Gill,A.J., Samra,J. and Mittal,A.
  TITLE     PSMD11, PTPRM and PTPRB as novel biomarkers of pancreatic cancer
            progression
  JOURNAL   Biochim Biophys Acta Gen Subj 1864 (11), 129682 (2020)
   PUBMED   32663515
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Ikezaki,M., Nishioka,N., Nishikawa,T., Higashimoto,N. and Ihara,Y.
  TITLE     Hsc70 is required for E-cadherin expression in epithelial-like
            NRK-52E cells
  JOURNAL   Biochem Biophys Res Commun 527 (2), 481-488 (2020)
   PUBMED   32336545
  REMARK    GeneRIF: Hsc70 is required for E-cadherin expression in
            epithelial-like NRK-52E cells.
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Morita,K., Wakui,H., Komatsuda,A., Ohtani,H., Miura,A.B., Itoh,H.
            and Tashima,Y.
  TITLE     Induction of heat-shock proteins HSP73 and HSP90 in rat kidneys
            after ischemia
  JOURNAL   Ren Fail 17 (4), 405-419 (1995)
   PUBMED   7569112
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Lee,Y.C. and Lai,Y.K.
  TITLE     Integrity of intermediate filaments is associated with the
            development of acquired thermotolerance in 9L rat brain tumor cells
  JOURNAL   J Cell Biochem 57 (1), 150-162 (1995)
   PUBMED   7721954
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Green,L.A. and Liem,R.K.
  TITLE     Beta-internexin is a microtubule-associated protein identical to
            the 70-kDa heat-shock cognate protein and the clathrin uncoating
            ATPase
  JOURNAL   J Biol Chem 264 (26), 15210-15215 (1989)
   PUBMED   2527848
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Sorger,P.K. and Pelham,H.R.
  TITLE     Cloning and expression of a gene encoding hsc73, the major
            hsp70-like protein in unstressed rat cells
  JOURNAL   EMBO J 6 (4), 993-998 (1987)
   PUBMED   3595567
REFERENCE   10 (residues 1 to 646)
  AUTHORS   O'Malley,K., Mauron,A., Barchas,J.D. and Kedes,L.
  TITLE     Constitutively expressed rat mRNA encoding a 70-kilodalton
            heat-shock-like protein
  JOURNAL   Mol Cell Biol 5 (12), 3476-3483 (1985)
   PUBMED   3939319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC061547.1 and BC098914.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001053026.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098914.1, M11942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..646
                     /product="heat shock cognate 71 kDa protein"
                     /EC_number="3.6.4.10"
                     /note="heat shock 70kD protein 8; Heat shock cognate
                     protein 70; heat shock protein A8; heat shock protein 8;
                     heat shock 70kDa protein 8"
                     /calculated_mol_wt=70740
     Region          1..613
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          2..386
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P63018.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Region          186..377
                     /region_name="Interaction with BAG1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P63018.1)"
     Site            246
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            328
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Region          394..509
                     /region_name="Substrate-binding domain (SBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P63018.1)"
     Site            469
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            512
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            561
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11142;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            589
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            597
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Site            601
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11142; propagated from
                     UniProtKB/Swiss-Prot (P63018.1)"
     Region          614..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63018.1)"
     CDS             1..646
                     /gene="Hspa8"
                     /gene_synonym="Hsc70"
                     /coded_by="NM_024351.2:81..2021"
                     /db_xref="GeneID:24468"
                     /db_xref="RGD:621725"
ORIGIN      
        1 mskgpavgid lgttyscvgv fqhgkveiia ndqgnrttps yvaftdterl igdaaknqva
       61 mnptntvfda krligrrfdd avvqsdmkhw pfmvvndagr pkvqveykge tksfypeevs
      121 smvltkmkei aeaylgktvt navvtvpayf ndsqrqatkd agtiaglnvl riineptaaa
      181 iaygldkkvg aernvlifdl gggtfdvsil tiedgifevk stagdthlgg edfdnrmvnh
      241 fiaefkrkhk kdisenkrav rrlrtacera krtlssstqa sieidslyeg idfytsitra
      301 rfeelnadlf rgtldpveka lrdakldksq ihdivlvggs tripkiqkll qdffngkeln
      361 ksinpdeava ygaavqaail sgdksenvqd lllldvtpls lgietaggvm tvlikrntti
      421 ptkqtqtftt ysdnqpgvli qvyegeramt kdnnllgkfe ltgippaprg vpqievtfdi
      481 dangilnvsa vdkstgkenk ititndkgrl skediermvq eaekykaede kqrdkvsskn
      541 slesyafnmk atvedeklqg kindedkqki ldkcneiisw ldknqtaeke efehqqkele
      601 kvcnpiitkl yqsaggmpgg mpggfpggga ppsggassgp tieevd
//
LOCUS       NP_058993                419 aa            linear   ROD 27-APR-2025
DEFINITION  G protein-activated inward rectifier potassium channel 4 [Rattus
            norvegicus].
ACCESSION   NP_058993 XP_346828
VERSION     NP_058993.1
DBSOURCE    REFSEQ: accession NM_017297.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   He,F., Zhao,J., Li,L. and Guo,R.
  TITLE     Effect of small interference RNA on the acetylcholine-sensitive
            potassium channel in H9c2 cells
  JOURNAL   Ann Clin Lab Sci 45 (1), 58-63 (2015)
   PUBMED   25696012
  REMARK    GeneRIF: The KCNJ5 gene and Kir3.4 protein were measured, and
            acetylcholine-sensitive potassium channel currents were recorded by
            patch-clamp.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bingen,B.O., Askar,S.F., Neshati,Z., Feola,I., Panfilov,A.V., de
            Vries,A.A. and Pijnappels,D.A.
  TITLE     Constitutively Active Acetylcholine-Dependent Potassium Current
            Increases Atrial Defibrillation Threshold by Favoring Post-Shock
            Re-Initiation
  JOURNAL   Sci Rep 5, 15187 (2015)
   PUBMED   26487066
  REMARK    GeneRIF: Blocking IK,ACh-c by tertiapin significantly decreased
            DFT, which correlated with a significant increase in wavelength
            during reentry. Genetic knockdown experiments with Kcnj5-specific
            shRNA to modulate IK,ACh-c, yielded similar results
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Liang,B., Nissen,J.D., Laursen,M., Wang,X., Skibsbye,L.,
            Hearing,M.C., Andersen,M.N., Rasmussen,H.B., Wickman,K.,
            Grunnet,M., Olesen,S.P. and Jespersen,T.
  TITLE     G-protein-coupled inward rectifier potassium current contributes to
            ventricular repolarization
  JOURNAL   Cardiovasc Res 101 (1), 175-184 (2014)
   PUBMED   24148898
  REMARK    GeneRIF: localized in intercalated discs in rat ventricle, whereas
            it was expressed in intercalated discs and outer sarcolemmas in rat
            atrium
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Kloukina,V., Herzer,S., Karlsson,N., Perez,M., Daraio,T. and
            Meister,B.
  TITLE     G-protein-gated inwardly rectifying K+ channel 4 (GIRK4)
            immunoreactivity in chemically defined neurons of the hypothalamic
            arcuate nucleus that control body weight
  JOURNAL   J Chem Neuroanat 44 (1), 14-23 (2012)
   PUBMED   22465809
  REMARK    GeneRIF: the GIRK4 channel protein plays a role in regulating
            membrane excitability in chemically defined neurons of the arcuate
            nucleus that control body weight
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Christensen,H.R., Zeng,Q., Murawsky,M.K. and Gregerson,K.A.
  TITLE     Estrogen regulation of the dopamine-activated GIRK channel in
            pituitary lactotrophs: implications for regulation of prolactin
            release during the estrous cycle
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 301 (3), R746-R756 (2011)
   PUBMED   21653876
  REMARK    GeneRIF: Estradiol regulates dopamine-activataed GIRK channel
            activity in pituitary lactotrophs, regulating prolactin release
            during the estrous cycle.
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Dobrzynski,H., Marples,D.D., Musa,H., Yamanushi,T.T., Henderson,Z.,
            Takagishi,Y., Honjo,H., Kodama,I. and Boyett,M.R.
  TITLE     Distribution of the muscarinic K+ channel proteins Kir3.1 and
            Kir3.4 in the ventricle, atrium, and sinoatrial node of heart
  JOURNAL   J Histochem Cytochem 49 (10), 1221-1234 (2001)
   PUBMED   11561006
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Huang,C.L., Feng,S. and Hilgemann,D.W.
  TITLE     Direct activation of inward rectifier potassium channels by PIP2
            and its stabilization by Gbetagamma
  JOURNAL   Nature 391 (6669), 803-806 (1998)
   PUBMED   9486652
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Ferrer,J., Nichols,C.G., Makhina,E.N., Salkoff,L., Bernstein,J.,
            Gerhard,D., Wasson,J., Ramanadham,S. and Permutt,A.
  TITLE     Pancreatic islet cells express a family of inwardly rectifying K+
            channel subunits which interact to form G-protein-activated
            channels
  JOURNAL   J Biol Chem 270 (44), 26086-26091 (1995)
   PUBMED   7592809
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Krapivinsky,G., Gordon,E.A., Wickman,K., Velimirovic,B.,
            Krapivinsky,L. and Clapham,D.E.
  TITLE     The G-protein-gated atrial K+ channel IKACh is a heteromultimer of
            two inwardly rectifying K(+)-channel proteins
  JOURNAL   Nature 374 (6518), 135-141 (1995)
   PUBMED   7877685
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Iizuka,M., Kubo,Y., Tsunenari,I., Pan,C.X., Akiba,I. and Kono,T.
  TITLE     Functional characterization and localization of a cardiac-type
            inwardly rectifying K+ channel
  JOURNAL   Recept Channels 3 (4), 299-315 (1995)
   PUBMED   8834003
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087022.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346828.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087022.1, D50135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663600, SAMN13663601
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..419
                     /product="G protein-activated inward rectifier potassium
                     channel 4"
                     /note="CIR; GIRK4; KATP-1; heart KATP channel; cardiac
                     inward rectifier; inward rectifier K(+) channel Kir3.4;
                     potassium voltage-gated channel subfamily J member 5;
                     potassium channel, inwardly rectifying subfamily J member
                     5; GIRK-4"
                     /calculated_mol_wt=47652
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48542; propagated from
                     UniProtKB/Swiss-Prot (P48548.2)"
     Region          54..193
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48548.2)"
     Region          149..154
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P48548.2)"
     Site            164..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48548.2)"
     Site            179
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P48548.2)"
     Region          200..371
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Region          380..419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48548.2)"
     CDS             1..419
                     /gene="Kcnj5"
                     /coded_by="NM_017297.2:177..1436"
                     /db_xref="GeneID:29713"
                     /db_xref="RGD:61971"
ORIGIN      
        1 magdsrnamn qdmeigvtsq dhkkipkqar dyipiatdrt rllpegkkpr qrymektgkc
       61 nvhhgnvqet yrylsdlftt lvdlkwrfnl lvftmvytit wlffgfiwwl iayvrgdldh
      121 vgdqewipcv enlsgfvsaf lfsietetti gygfrvitek cpegiilllv qailgsivna
      181 fmvgcmfvki sqpkkraetl mfsnnavism rdeklclmfr vgdlrnshiv easiraklik
      241 srqtkegefi plnqtdinvg fdtgddrlfl vspliishei nekspfwems raqleqeefe
      301 vvvilegmve atgmtcqars symdtevlwg hrftpvltle kgfyevdynt fhdtyetntp
      361 sccakelaem krngqllqsl psppllggca eaekeaeaeh deeeepngls vsratrgsm
//
LOCUS       NP_001007621             359 aa            linear   ROD 27-APR-2025
DEFINITION  pyruvate dehydrogenase E1 component subunit beta, mitochondrial
            precursor [Rattus norvegicus].
ACCESSION   NP_001007621 XP_214142
VERSION     NP_001007621.1
DBSOURCE    REFSEQ: accession NM_001007620.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Mitra,A., Basak,T., Ahmad,S., Datta,K., Datta,R., Sengupta,S. and
            Sarkar,S.
  TITLE     Comparative Proteome Profiling during Cardiac Hypertrophy and
            Myocardial Infarction Reveals Altered Glucose Oxidation by
            Differential Activation of Pyruvate Dehydrogenase E1 Component
            Subunit beta
  JOURNAL   J Mol Biol 427 (11), 2104-2120 (2015)
   PUBMED   25451023
  REMARK    GeneRIF: Phosphorylation of the pyruvate dehydrogenase E1-beta
            leads to a decrease in ventricular ATP level during myocardial
            infarction.
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Wallwiener,M., Wallwiener,C.W., Molinas,R., Rajab,T.K.,
            Brucker,S.Y., Kraemer,B. and Hartkopf,A.D.
  TITLE     Intraabdominal adhesion formation is associated with differential
            mRNA expression of metabolic genes PDHb and SDHa
  JOURNAL   Arch Gynecol Obstet 286 (3), 683-686 (2012)
   PUBMED   22569713
  REMARK    GeneRIF: up-regulated by 23 % in peritoneal adhesions
REFERENCE   3  (residues 1 to 359)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Kato,M., Wynn,R.M., Chuang,J.L., Tso,S.C., Machius,M., Li,J. and
            Chuang,D.T.
  TITLE     Structural basis for inactivation of the human pyruvate
            dehydrogenase complex by phosphorylation: role of disordered
            phosphorylation loops
  JOURNAL   Structure 16 (12), 1849-1859 (2008)
   PUBMED   19081061
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Okajima,K., Korotchkina,L.G., Prasad,C., Rupar,T., Phillips,J.A.
            3rd, Ficicioglu,C., Hertecant,J., Patel,M.S. and Kerr,D.S.
  TITLE     Mutations of the E1beta subunit gene (PDHB) in four families with
            pyruvate dehydrogenase deficiency
  JOURNAL   Mol Genet Metab 93 (4), 371-380 (2008)
   PUBMED   18164639
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Patel,M.S. and Korotchkina,L.G.
  TITLE     Regulation of mammalian pyruvate dehydrogenase complex by
            phosphorylation: complexity of multiple phosphorylation sites and
            kinases
  JOURNAL   Exp Mol Med 33 (4), 191-197 (2001)
   PUBMED   11795479
  REMARK    Review article
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Maury,J., Kerbey,A.L., Priestman,D.A., Patel,M.S., Girard,J. and
            Ferre,P.
  TITLE     Pretranslational regulation of pyruvate dehydrogenase complex
            subunits in white adipose tissue during the suckling-weaning
            transition in the rat
  JOURNAL   Biochem J 311 (Pt 2) (Pt 2), 531-535 (1995)
   PUBMED   7487891
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Matuda,S., Nakano,K., Ohta,S., Saheki,T., Kawanishi,Y. and
            Miyata,T.
  TITLE     The alpha-ketoacid dehydrogenase complexes. Sequence similarity of
            rat pyruvate dehydrogenase with Escherichia coli and Azotobacter
            vinelandii alpha-ketoglutarate dehydrogenase
  JOURNAL   Biochim Biophys Acta 1089 (1), 1-7 (1991)
   PUBMED   2025639
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Huh,T.L., Casazza,J.P., Huh,J.W., Chi,Y.T. and Song,B.J.
  TITLE     Characterization of two cDNA clones for pyruvate dehydrogenase E1
            beta subunit and its regulation in tricarboxylic acid
            cycle-deficient fibroblast
  JOURNAL   J Biol Chem 265 (22), 13320-13326 (1990)
   PUBMED   2376596
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079137.1.
            
            On Nov 29, 2004 this sequence version replaced XP_214142.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079137.1, FQ215211.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..359
                     /product="pyruvate dehydrogenase E1 component subunit
                     beta, mitochondrial precursor"
                     /EC_number="1.2.4.1"
                     /note="pyruvate dehydrogenase E1 component subunit beta,
                     mitochondrial; PDHE1-B; pyruvate dehydrogenase (lipoamide)
                     beta; pyruvate dehydrogenase E1 beta subunit"
                     /calculated_mol_wt=35842
     transit_peptide 1..30
                     /note="Mitochondrion. /evidence=ECO:0000269|Ref.3;
                     propagated from UniProtKB/Swiss-Prot (P49432.2)"
                     /calculated_mol_wt=3159
     mat_peptide     31..359
                     /product="Pyruvate dehydrogenase E1 component subunit
                     beta, mitochondrial. /id=PRO_0000020459"
                     /note="propagated from UniProtKB/Swiss-Prot (P49432.2)"
                     /calculated_mol_wt=35842
     Region          <31..355
                     /region_name="PRK11892"
                     /note="pyruvate dehydrogenase subunit beta; Provisional"
                     /db_xref="CDD:237011"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D051; propagated from
                     UniProtKB/Swiss-Prot (P49432.2)"
     Site            319
                     /site_type="other"
                     /note="Important for interaction with DLAT.
                     /evidence=ECO:0000250|UniProtKB:P11177; propagated from
                     UniProtKB/Swiss-Prot (P49432.2)"
     Site            354
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D051; propagated from
                     UniProtKB/Swiss-Prot (P49432.2)"
     CDS             1..359
                     /gene="Pdhb"
                     /coded_by="NM_001007620.1:328..1407"
                     /db_xref="GeneID:289950"
                     /db_xref="RGD:1359146"
ORIGIN      
        1 maavaglvrg plrqasgllk rrfhrsapaa vqltvreain qgmdeelerd ekvfllgeev
       61 aqydgaykvs rglwkkygdk riidtpisem gfagiavgaa maglrpicef mtfnfsmqai
      121 dqvinsaakt yymsaglqpv pivfrgpnga sagvaaqhsq cfaawyghcp glkvvspwns
      181 edakgliksa irddnpvvml enelmygvaf elpteaqskd flipigkaki erqgthitvv
      241 ahsrpvghcl eaaavlskeg iecevinlrt irpmdieaie asvmktnhlv tveggwpqfg
      301 vgaeicarim egpafnflda pavrvtgadv pmpyakiled nsipqvkdii faikktlni
//
LOCUS       NP_001007732             137 aa            linear   ROD 27-APR-2025
DEFINITION  golgin subfamily A member 7 [Rattus norvegicus].
ACCESSION   NP_001007732 XP_341458
VERSION     NP_001007732.1
DBSOURCE    REFSEQ: accession NM_001007731.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Swarthout,J.T., Lobo,S., Farh,L., Croke,M.R., Greentree,W.K.,
            Deschenes,R.J. and Linder,M.E.
  TITLE     DHHC9 and GCP16 constitute a human protein fatty acyltransferase
            with specificity for H- and N-Ras
  JOURNAL   J Biol Chem 280 (35), 31141-31148 (2005)
   PUBMED   16000296
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Ohta,E., Misumi,Y., Sohda,M., Fujiwara,T., Yano,A. and Ikehara,Y.
  TITLE     Identification and characterization of GCP16, a novel acylated
            Golgi protein that interacts with GCP170
  JOURNAL   J Biol Chem 278 (51), 51957-51967 (2003)
   PUBMED   14522980
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078959.1.
            
            On Nov 29, 2004 this sequence version replaced XP_341458.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078959.1, EV777441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..137
                     /product="golgin subfamily A member 7"
                     /note="golgi autoantigen, golgin subfamily a, 7"
                     /calculated_mol_wt=15647
     Region          11..124
                     /region_name="Erf4"
                     /note="Golgin subfamily A member 7/ERF4 family; pfam10256"
                     /db_xref="CDD:463029"
     CDS             1..137
                     /gene="Golga7"
                     /coded_by="NM_001007731.1:218..631"
                     /db_xref="GeneID:361171"
                     /db_xref="RGD:1359725"
ORIGIN      
        1 mrpqqapvsg kvfiqrdyss gtrcqfqtkf paelenrvdr qqfeetvrtl nnlyaeaekl
       61 ggqsylegcl acltaytifl cmethyekvl kkvskyiqeq nekiyapqgl lltdpiergl
      121 rvieitiyed rgvssgr
//
LOCUS       NP_001029243             284 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.3sm [Rattus norvegicus].
ACCESSION   NP_001029243
VERSION     NP_001029243.1
DBSOURCE    REFSEQ: accession NM_001034071.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU670983.1, AF372216.1,
            M60667.1 and BC078780.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.3, also known as variant 4)
            has multiple differences in the coding region, compared to variant
            1, resulting in a shorter protein (isoform Tpm1.3sm). Isoform
            Tpm1.3sm is the same length as isoforms Tpm1.6cy and Tpm1.7cy but
            is the product of alternate splicing and contains short regions of
            sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF372216.1, SRR8487231.158269.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093047, SAMN16676787
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.3sm"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32662
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034071.1:107..961"
                     /note="isoform Tpm1.3sm is encoded by transcript variant
                     Tpm1.3"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle edisakekll rasederdrv
       61 leelhkaeds llaadetaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddleekv ahakeenlsm hqmldqtlle lnnm
//
LOCUS       NP_001102419             392 aa            linear   ROD 27-APR-2025
DEFINITION  HORMA domain-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001102419 XP_001060782 XP_345249
VERSION     NP_001102419.1
DBSOURCE    REFSEQ: accession NM_001108949.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Jordan,P.W., Karppinen,J. and Handel,M.A.
  TITLE     Polo-like kinase is required for synaptonemal complex disassembly
            and phosphorylation in mouse spermatocytes
  JOURNAL   J Cell Sci 125 (Pt 21), 5061-5072 (2012)
   PUBMED   22854038
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Kogo,H., Tsutsumi,M., Ohye,T., Inagaki,H., Abe,T. and Kurahashi,H.
  TITLE     HORMAD1-dependent checkpoint/surveillance mechanism eliminates
            asynaptic oocytes
  JOURNAL   Genes Cells 17 (6), 439-454 (2012)
   PUBMED   22530760
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Wojtasz,L., Cloutier,J.M., Baumann,M., Daniel,K., Varga,J., Fu,J.,
            Anastassiadis,K., Stewart,A.F., Remenyi,A., Turner,J.M. and Toth,A.
  TITLE     Meiotic DNA double-strand breaks and chromosome asynapsis in mice
            are monitored by distinct HORMAD2-independent and -dependent
            mechanisms
  JOURNAL   Genes Dev 26 (9), 958-973 (2012)
   PUBMED   22549958
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Daniel,K., Lange,J., Hached,K., Fu,J., Anastassiadis,K., Roig,I.,
            Cooke,H.J., Stewart,A.F., Wassmann,K., Jasin,M., Keeney,S. and
            Toth,A.
  TITLE     Meiotic homologue alignment and its quality surveillance are
            controlled by mouse HORMAD1
  JOURNAL   Nat Cell Biol 13 (5), 599-610 (2011)
   PUBMED   21478856
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Shin,Y.H., Choi,Y., Erdin,S.U., Yatsenko,S.A., Kloc,M., Yang,F.,
            Wang,P.J., Meistrich,M.L. and Rajkovic,A.
  TITLE     Hormad1 mutation disrupts synaptonemal complex formation,
            recombination, and chromosome segregation in mammalian meiosis
  JOURNAL   PLoS Genet 6 (11), e1001190 (2010)
   PUBMED   21079677
  REMARK    Erratum:[PLoS Genet. 2011;7(2). doi:
            10.1371/annotation/8aa656b6-55f7-4795-a441-cf243ea62175]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Fukuda,T., Daniel,K., Wojtasz,L., Toth,A. and Hoog,C.
  TITLE     A novel mammalian HORMA domain-containing protein, HORMAD1,
            preferentially associates with unsynapsed meiotic chromosomes
  JOURNAL   Exp Cell Res 316 (2), 158-171 (2010)
   PUBMED   19686734
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Wojtasz,L., Daniel,K., Roig,I., Bolcun-Filas,E., Xu,H.,
            Boonsanay,V., Eckmann,C.R., Cooke,H.J., Jasin,M., Keeney,S.,
            McKay,M.J. and Toth,A.
  TITLE     Mouse HORMAD1 and HORMAD2, two conserved meiotic chromosomal
            proteins, are depleted from synapsed chromosome axes with the help
            of TRIP13 AAA-ATPase
  JOURNAL   PLoS Genet 5 (10), e1000702 (2009)
   PUBMED   19851446
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474015.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_345249.3, XP_001060782.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..392
                     /product="HORMA domain-containing protein 1"
                     /calculated_mol_wt=44754
     Region          27..221
                     /region_name="HORMA"
                     /note="HORMA domain; pfam02301"
                     /db_xref="CDD:460526"
     Region          271..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZWE7.1)"
     Region          371..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZWE7.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D5T7; propagated from
                     UniProtKB/Swiss-Prot (D3ZWE7.1)"
     Region          381..384
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZWE7.1)"
     CDS             1..392
                     /gene="Hormad1"
                     /gene_synonym="RGD1564960"
                     /coded_by="NM_001108949.1:77..1255"
                     /db_xref="GeneID:365868"
                     /db_xref="RGD:1564960"
ORIGIN      
        1 matmqlrrta smsalvfpnk isteqqslmf vkrllavsvs citylrgifp eraygtryld
       61 dlcvkilked kncpgssqlv kwmlgcydal qkkylrmiil avytnpedpq tisecyqfkf
      121 kytkngpimd fisknqnnks sttsadtkka sillirkiyv lmqnlgplpn dvcltmklfy
      181 ydevtppdyq ppgfkdgdce gvifdgdpty lnvgevptpf htfrlkvtte kermenidsa
      241 iltpkdskip fqkilmdkdd vedenhnnfd iktkmneqne nsgtseikep nldckeeeim
      301 qfkknqsssi sqcqveqlis ktseldvses ktrsgkifqc kmvngnqqgq iskenrkrsl
      361 rqsgktvlhi lesssqesvl krrrvsepne ht
//
LOCUS       NP_001020801             231 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 6-interacting protein 4
            [Rattus norvegicus].
ACCESSION   NP_001020801
VERSION     NP_001020801.1
DBSOURCE    REFSEQ: accession NM_001025630.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097374.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097374.1, EV774925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..231
                     /product="ADP-ribosylation factor-like protein
                     6-interacting protein 4"
                     /note="aip-4; ARL-6-interacting protein 4; splicing factor
                     SRrp37; ADP-ribosylation-like factor 6 interacting protein
                     4; ADP-ribosylation factor-like 6 interacting protein 4;
                     ADP-ribosylation factor like GTPase 6 interacting protein
                     4"
                     /calculated_mol_wt=25638
     Region          1..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8I5.1)"
     Region          36..229
                     /region_name="SR-25"
                     /note="Nuclear RNA-splicing-associated protein; pfam10500"
                     /db_xref="CDD:463119"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8I5.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66PJ3; propagated from
                     UniProtKB/Swiss-Prot (Q4V8I5.1)"
     CDS             1..231
                     /gene="Arl6ip4"
                     /coded_by="NM_001025630.1:334..1029"
                     /db_xref="GeneID:288656"
                     /db_xref="RGD:1307657"
ORIGIN      
        1 mahvssrkrs rsrsrsrgrr gsekrskrss kdssrncsts ksqghkasst sgveerskhk
       61 aqrtsrssss ssssssssss sstssssssd grkkrgkhkd kkkrkkkkkr kkkmkrkgke
      121 kavvvhqaea lpgpsldqwh rsagedndgp vltdeqksri qamkpmtkee wdarqsvirk
      181 vvdpetgrtr likgdgevle eivtkerhre inkqatrgdg lafqmragll p
//
LOCUS       NP_001102889             124 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein C-IV precursor [Rattus norvegicus].
ACCESSION   NP_001102889 XP_001057696
VERSION     NP_001102889.1
DBSOURCE    REFSEQ: accession NM_001109419.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Wang,X., Gong,Y., Deng,T., Zhang,L., Liao,X., Han,C., Yang,C.,
            Huang,J., Wang,Q., Song,X., Zhang,T., Yu,T., Zhu,G., Ye,X. and
            Peng,T.
  TITLE     Diagnostic and prognostic significance of mRNA expressions of
            apolipoprotein A and C family genes in hepatitis B virus-related
            hepatocellular carcinoma
  JOURNAL   J Cell Biochem 120 (10), 18246-18265 (2019)
   PUBMED   31211449
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Kim,E., Li,K., Lieu,C., Tong,S., Kawai,S., Fukutomi,T., Zhou,Y.,
            Wands,J. and Li,J.
  TITLE     Expression of apolipoprotein C-IV is regulated by Ku
            antigen/peroxisome proliferator-activated receptor gamma complex
            and correlates with liver steatosis
  JOURNAL   J Hepatol 49 (5), 787-798 (2008)
   PUBMED   18809223
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Mancone,C., Amicone,L., Fimia,G.M., Bravo,E., Piacentini,M.,
            Tripodi,M. and Alonzi,T.
  TITLE     Proteomic analysis of human very low-density lipoprotein by
            two-dimensional gel electrophoresis and MALDI-TOF/TOF
  JOURNAL   Proteomics 7 (1), 143-154 (2007)
   PUBMED   17154273
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Kotite,L., Zhang,L.H., Yu,Z., Burlingame,A.L. and Havel,R.J.
  TITLE     Human apoC-IV: isolation, characterization, and immunochemical
            quantification in plasma and plasma lipoproteins
  JOURNAL   J Lipid Res 44 (7), 1387-1394 (2003)
   PUBMED   12700345
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Allan,C.M. and Taylor,J.M.
  TITLE     Expression of a novel human apolipoprotein (apoC-IV) causes
            hypertriglyceridemia in transgenic mice
  JOURNAL   J Lipid Res 37 (7), 1510-1518 (1996)
   PUBMED   8827523
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Shen,P. and Howlett,G.J.
  TITLE     Two coding regions closely linked to the rat apolipoprotein E gene:
            nucleotide sequences of rat apolipoprotein C-I and ECL cDNA
  JOURNAL   Arch Biochem Biophys 297 (2), 345-353 (1992)
   PUBMED   1379790
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On Oct 4, 2007 this sequence version replaced XP_001057696.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ218092.1, FQ218144.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..124
                     /product="apolipoprotein C-IV precursor"
                     /note="ECL; apo-CIV; apoC-IV; apolipoprotein E-linked;
                     apolipoprotein C-IV; apolipoprotein C2 linked;
                     apolipoprotein CIV"
                     /calculated_mol_wt=11549
     sig_peptide     1..27
                     /note="/evidence=ECO:0000250|UniProtKB:P55057; propagated
                     from UniProtKB/Swiss-Prot (P55797.2)"
                     /calculated_mol_wt=3001
     mat_peptide     28..124
                     /product="Apolipoprotein C-IV. /id=PRO_0000002039"
                     /note="propagated from UniProtKB/Swiss-Prot (P55797.2)"
                     /calculated_mol_wt=11549
     Region          28..120
                     /region_name="APOC4"
                     /note="Apolipoprotein C4; pfam15119"
                     /db_xref="CDD:434474"
     CDS             1..124
                     /gene="Apoc4"
                     /gene_synonym="Acl"
                     /coded_by="NM_001109419.1:41..415"
                     /db_xref="GeneID:680551"
                     /db_xref="RGD:70959"
ORIGIN      
        1 msllrcrqqt lpslclsvlf lacfvasmpt esltptpgpe nsrwslvrar vmemveplvt
       61 rtrdrwrwfw gpraiqgfvq tyyedhlkdl gprtqawlqs srdhllnkth slcprllcrd
      121 wtqg
//
LOCUS       NP_001012065             528 aa            linear   ROD 27-APR-2025
DEFINITION  atypical kinase COQ8B, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001012065 XP_218358
VERSION     NP_001012065.1
DBSOURCE    REFSEQ: accession NM_001012065.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Stefely,J.A., Licitra,F., Laredj,L., Reidenbach,A.G.,
            Kemmerer,Z.A., Grangeray,A., Jaeg-Ehret,T., Minogue,C.E.,
            Ulbrich,A., Hutchins,P.D., Wilkerson,E.M., Ruan,Z., Aydin,D.,
            Hebert,A.S., Guo,X., Freiberger,E.C., Reutenauer,L., Jochem,A.,
            Chergova,M., Johnson,I.E., Lohman,D.C., Rush,M.J.P., Kwiecien,N.W.,
            Singh,P.K., Schlagowski,A.I., Floyd,B.J., Forsman,U.,
            Sindelar,P.J., Westphall,M.S., Pierrel,F., Zoll,J., Dal Peraro,M.,
            Kannan,N., Bingman,C.A., Coon,J.J., Isope,P., Puccio,H. and
            Pagliarini,D.J.
  TITLE     Cerebellar Ataxia and Coenzyme Q Deficiency through Loss of
            Unorthodox Kinase Activity
  JOURNAL   Mol Cell 63 (4), 608-620 (2016)
   PUBMED   27499294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079227.1.
            
            On Feb 11, 2005 this sequence version replaced XP_218358.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079227.1, SRR8487227.182781.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..528
                     /product="atypical kinase COQ8B, mitochondrial"
                     /note="aarF domain-containing protein kinase 4; aarF
                     domain containing kinase 4; coenzyme Q protein 8B"
                     /calculated_mol_wt=58774
     Site            93..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY19.1)"
     Region          151..154
                     /region_name="KxGQ motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NI60"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY19.1)"
     Region          171..420
                     /region_name="ABC1_ADCK3"
                     /note="Activator of bc1 complex (ABC1) kinases, also
                     called aarF domain containing kinase 3; cd13970"
                     /db_xref="CDD:270872"
     Region          212..215
                     /region_name="AAAS motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NI60"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY19.1)"
     Site            order(224..228,230,240,242,301,320..323,363,367..368,370,
                     381..382)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:270872"
     CDS             1..528
                     /gene="Coq8b"
                     /gene_synonym="Adck4"
                     /coded_by="NM_001012065.1:77..1663"
                     /db_xref="GeneID:308453"
                     /db_xref="RGD:1311356"
ORIGIN      
        1 mwlelgamlr ttcgplgrav rlpcagalrl rphwwgpcrd claqrvhqdq pgrgltedei
       61 rrarearlrk aprpqlsdrs rerkvpasri srlasfggla vglglgalae vtkkslpggs
      121 lqhegsspfl teanaerivq tlctvrgaal kigqmlsiqd nslispqlqr vfervrqsad
      181 fmprwqmmkv leeelgkdwq dkvasleevp faaasigqvh qgvlkdgtev avkiqypgva
      241 esiqsdvqnl lallkmsvgl peglfaeqsl qtlqqelawe cdyrreaaca qtfkklladd
      301 pffrvpavve elcttrvlgm elaggipldq cqglsqdirn qicfqllrlc lrelfefrfm
      361 qtdpnwanfl ydasshkvtl ldfgasrafg teftdhyiev vkaaadgdrd rvlqksqdlk
      421 fltgfetkaf sdahveavmi lgepfaasgs ydfgagetar riqglipvll rhrlrpppee
      481 tyalhrklag aflacarlha hiacrdlfqd tyhrywasrq tlplpaas
//
LOCUS       NP_001019935             477 aa            linear   ROD 27-APR-2025
DEFINITION  proton-coupled amino acid transporter 3 [Rattus norvegicus].
ACCESSION   NP_001019935 XP_220441
VERSION     NP_001019935.1
DBSOURCE    REFSEQ: accession NM_001024764.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097463.1.
            
            On Jun 10, 2005 this sequence version replaced XP_220441.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..477
                     /product="proton-coupled amino acid transporter 3"
                     /note="tramdorin-2; proton/amino acid transporter 3;
                     solute carrier family 36 (proton/amino acid symporter),
                     member 3"
                     /calculated_mol_wt=52720
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Region          52..458
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            292..312
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            345..365
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            400..420
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     Site            440..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8B1.1)"
     CDS             1..477
                     /gene="Slc36a3"
                     /coded_by="NM_001024764.1:211..1644"
                     /db_xref="GeneID:303148"
                     /db_xref="RGD:1309092"
ORIGIN      
        1 mgktpllred grcqrntfgg skasskgsss sssnntvssk kkprrkadal mfiqifihll
       61 ksnigtgflg lplavknagl lvgpvsllai galtvhcmdi llncachlts rlqrsfvnye
      121 ettmysletc pspwlrthsv wgryvvsfll ivtqlgfcsv yfmfmadnlq qiveeahfts
      181 nvcqprqslv mtsildtrfy mltilpflil lvlvqnpqvl sifstlatit tlsslalife
      241 yliqiphhsh lplvaswktf llffgtaift fegvgmvlpl ksqmkspqqf pavlylgmsf
      301 viflyiclgt lgymkfgadt qasitlnlpn cwlyqsvklm ysvgifftya lqfhvpaeii
      361 vpyvvsrase nwalfidltv raalvcltcf savliprldl vislvgsvss salaliippl
      421 leiatfysen iscttiakdi misilgllgc vlgtyqalye mtqqsrfpml nstnvht
//
LOCUS       NP_446263                337 aa            linear   ROD 27-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF2 [Rattus
            norvegicus].
ACCESSION   NP_446263
VERSION     NP_446263.2
DBSOURCE    REFSEQ: accession NM_053811.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lu,X., He,L., Zhou,Q., Wang,M., Shen,W.J., Azhar,S., Pan,F., Guo,Z.
            and Hu,Z.
  TITLE     NHERF1 and NHERF2 regulation of SR-B1 stability via ubiquitination
            and proteasome degradation
  JOURNAL   Biochem Biophys Res Commun 490 (4), 1168-1175 (2017)
   PUBMED   28669731
  REMARK    GeneRIF: The results suggest that NHERF1 and NHERF2 down-regulated
            SR-B1 at least in part via the ubiquitin/proteasome pathway.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Briffa,J.F., Grinfeld,E., Jenkin,K.A., Mathai,M.L., Poronnik,P.,
            McAinch,A.J. and Hryciw,D.H.
  TITLE     Diet induced obesity in rats reduces NHE3 and Na(+) /K(+) -ATPase
            expression in the kidney
  JOURNAL   Clin Exp Pharmacol Physiol 42 (10), 1118-1126 (2015)
   PUBMED   26173747
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Kamiya,K., Michel,V., Giraudet,F., Riederer,B., Foucher,I.,
            Papal,S., Perfettini,I., Le Gal,S., Verpy,E., Xia,W., Seidler,U.,
            Georgescu,M.M., Avan,P., El-Amraoui,A. and Petit,C.
  TITLE     An unusually powerful mode of low-frequency sound interference due
            to defective hair bundles of the auditory outer hair cells
  JOURNAL   Proc Natl Acad Sci U S A 111 (25), 9307-9312 (2014)
   PUBMED   24920589
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Yang,J., Singh,V., Cha,B., Chen,T.E., Sarker,R., Murtazina,R.,
            Jin,S., Zachos,N.C., Patterson,G.H., Tse,C.M., Kovbasnjuk,O., Li,X.
            and Donowitz,M.
  TITLE     NHERF2 protein mobility rate is determined by a unique C-terminal
            domain that is also necessary for its regulation of NHE3 protein in
            OK cells
  JOURNAL   J Biol Chem 288 (23), 16960-16974 (2013)
   PUBMED   23612977
  REMARK    GeneRIF: NHERF2 domain was functionally significant in NHE3
            regulation, being necessary for stimulation by lysophosphatidic
            acid of activity and increased mobility of NHE3
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Shenolikar,S., Voltz,J.W., Minkoff,C.M., Wade,J.B. and Weinman,E.J.
  TITLE     Targeted disruption of the mouse NHERF-1 gene promotes
            internalization of proximal tubule sodium-phosphate cotransporter
            type IIa and renal phosphate wasting
  JOURNAL   Proc Natl Acad Sci U S A 99 (17), 11470-11475 (2002)
   PUBMED   12169661
REFERENCE   7  (residues 1 to 337)
  AUTHORS   DeMarco,S.J., Chicka,M.C. and Strehler,E.E.
  TITLE     Plasma membrane Ca2+ ATPase isoform 2b interacts preferentially
            with Na+/H+ exchanger regulatory factor 2 in apical plasma
            membranes
  JOURNAL   J Biol Chem 277 (12), 10506-10511 (2002)
   PUBMED   11786550
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Takeda,T., McQuistan,T., Orlando,R.A. and Farquhar,M.G.
  TITLE     Loss of glomerular foot processes is associated with uncoupling of
            podocalyxin from the actin cytoskeleton
  JOURNAL   J Clin Invest 108 (2), 289-301 (2001)
   PUBMED   11457882
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Fouassier,L., Duan,C.Y., Feranchak,A.P., Yun,C.H., Sutherland,E.,
            Simon,F., Fitz,J.G. and Doctor,R.B.
  TITLE     Ezrin-radixin-moesin-binding phosphoprotein 50 is expressed at the
            apical membrane of rat liver epithelia
  JOURNAL   Hepatology 33 (1), 166-176 (2001)
   PUBMED   11124833
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Zhang,J., Coward,P., Xian,M. and Lau,Y.F.
  TITLE     In vitro binding and expression studies demonstrate a role for the
            mouse Sry Q-rich domain in sex determination
  JOURNAL   Int J Dev Biol 43 (3), 219-227 (1999)
   PUBMED   10410901
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF294257.1, CK840521.1 and JAXUCZ010000010.1.
            
            On Oct 11, 2007 this sequence version replaced NP_446263.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF294257.1, AF259898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..337
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF2"
                     /note="solute carrier family 9, subfamily A (NHE3, cation
                     proton antiporter 3), member 3 regulator 2; SIP-1; TKA-1;
                     NHERF-2; SRY-interacting protein 1; tyrosine kinase
                     activator protein 1; NHE3 kinase A regulatory protein
                     E3KARP; sodium-hydrogen exchanger regulatory factor 2;
                     SLC9A3 regulator 2; solute carrier family 9
                     (sodium/hydrogen exchanger), member 3 regulator 2"
                     /calculated_mol_wt=37220
     Region          10..89
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(20..26,37,40,69,73,76..77)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          127..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Region          150..229
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(160..166,177,180,209,213,216..217)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15599; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Region          232..337
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     Region          246..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15599; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15599; propagated from
                     UniProtKB/Swiss-Prot (Q920G2.1)"
     CDS             1..337
                     /gene="Nherf2"
                     /gene_synonym="E3karp; Slc9a3r2"
                     /coded_by="NM_053811.3:76..1089"
                     /db_xref="GeneID:116501"
                     /db_xref="RGD:620380"
ORIGIN      
        1 maapeslrpr lcrlvrgeqg ygfhlhgekg rrgqfirrve pgspaeaaal ragdrlvevn
       61 gvnvegethh qvvqrikave gqtqllvvdk etdeelcrrq ltcteemahr glppahnpwe
      121 pkpdwacsgs lgsdtgqkdv ngpprelrpr lchlrrgpqg ygfnlhsdks rpgqyirsvd
      181 pgspaslsgl raqdrlievn gqnveglrha evvarikaqe dearllvvdp etdehfkrlr
      241 vvptedhveg plpspvtngt slaqlnggsv cssrsdlpgs ekdnedgsaw krdpfqesgl
      301 hlsptaaeak ekaratrvnk rapqmdwnrk reifsnf
//
LOCUS       NP_110457               1073 aa            linear   ROD 27-APR-2025
DEFINITION  leucine zipper protein 1 [Rattus norvegicus].
ACCESSION   NP_110457
VERSION     NP_110457.2
DBSOURCE    REFSEQ: accession NM_030830.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1073)
  AUTHORS   Fan,D., Jiang,W.L., Jin,Z.L., Cao,J.L., Li,Y., He,T., Zhang,W.,
            Peng,L., Liu,H.X., Wu,X.Y., Chen,M., Fan,Y.Z., He,B., Yu,W.X.,
            Wang,H.R., Hu,X.R. and Lu,Z.B.
  TITLE     Leucine zipper protein 1 attenuates pressure overload-induced
            cardiac hypertrophy through inhibiting Stat3 signaling
  JOURNAL   J Adv Res 63, 117-128 (2024)
   PUBMED   37806546
  REMARK    GeneRIF: Leucine zipper protein 1 attenuates pressure
            overload-induced cardiac hypertrophy through inhibiting Stat3
            signaling.
REFERENCE   2  (residues 1 to 1073)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 1073)
  AUTHORS   Hsu,C.Y., Chang,N.C., Lee,M.W., Lee,K.H., Sun,D.S., Lai,C. and
            Chang,A.C.
  TITLE     LUZP deficiency affects neural tube closure during brain
            development
  JOURNAL   Biochem Biophys Res Commun 376 (3), 466-471 (2008)
   PUBMED   18801334
REFERENCE   4  (residues 1 to 1073)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   5  (residues 1 to 1073)
  AUTHORS   Lee,M.W., Chang,A.C., Sun,D.S., Hsu,C.Y. and Chang,N.C.
  TITLE     Restricted expression of LUZP in neural lineage cells: a study in
            embryonic stem cells
  JOURNAL   J Biomed Sci 8 (6), 504-511 (2001)
   PUBMED   11702014
REFERENCE   6  (residues 1 to 1073)
  AUTHORS   Sun,D.S., Chang,A.C., Jenkins,N.A., Gilbert,D.J., Copeland,N.G. and
            Chang,N.C.
  TITLE     Identification, molecular characterization, and chromosomal
            localization of the cDNA encoding a novel leucine zipper
            motif-containing protein
  JOURNAL   Genomics 36 (1), 54-62 (1996)
   PUBMED   8812416
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473968.1.
            
            On Feb 1, 2008 this sequence version replaced NP_110457.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132264 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1073
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1073
                     /product="leucine zipper protein 1"
                     /note="leucine zipper motif-containing protein; fimbacin;
                     filamin mechanobinding actin cross-linking protein"
                     /calculated_mol_wt=119681
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          <7..>406
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          247..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          374..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          432..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          569..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          675..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          789..837
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          834..884
                     /region_name="Required for interaction with FLNA.
                     /evidence=ECO:0000250|UniProtKB:Q86V48"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Region          929..1000
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            957
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86V48; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV1.1)"
     CDS             1..1073
                     /gene="Luzp1"
                     /gene_synonym="Luzp"
                     /coded_by="NM_030830.2:371..3592"
                     /db_xref="GeneID:79428"
                     /db_xref="RGD:61839"
ORIGIN      
        1 madianykda asnrhlrfkl qslsrrldel eeatknlqka edelldlqdk viqaegsnss
       61 mlaeievlrq rvlkiegkde eikraedlch tmkekleeee nltrelksei drlqkrmadl
      121 ekleealsrs knecsqlcls lneernltkk isselemlrv kvkelessed rlekteqslv
      181 seleklkslt lsfvnerkyl nekekenekl ikeltqkleq nkkinrdhmr nastflernd
      241 lriedgisst lpskesrrkg sldylkqven etrdksenek nrnqednkvk dlnqeieklk
      301 tqikhfesle eelkkmrakn ndlqdnylte lnknrslasq leevklqvkk qkelgngdie
      361 gedafllgrg rhertklkgh ggevsvskht sreqspqhkr erlrnrgfal ndehcslsnk
      421 qvsspaftnk raakasnmgv gpdsgtqetk rtedrlapgs sqsegkkgre qpsvlsrypp
      481 aaqdhtkvwr gnpkpgtesg lkgkvekttr tfsdsahgsv pndvvgkgdk tsdfsseahc
      541 gkrgqvpgha sqvtqvaesg cskaigalas sqrassegls kgkkaangle tdanfphska
      601 pilskypyss rsqenilqgf svpnkegvdh svavvmedss qhealrcrvi kssgrekpds
      661 dddldieslv taklvnttit pepepklqpn srekvksrgg trtalfendk naavendsak
      721 smrsssnave fpdancagvk nqrpfsprea lrsraiikpv iidkdvkkim ggsgtevvle
      781 kqkstpksvt skvtssitiy psdssgprav pteaprerht stsniqvgpp eltsvsnhis
      841 splelsihkh ditlqlteae rvgdgspknr aetvvsrssi likpsdsver nshafpaeti
      901 rwkshstsse vassdtrhit vrnawkskrd lkcsedpptr igrnveatna ytqrsstdfl
      961 eleqprshpp eqgtrkvgns gdapelssrr tqssltasev ltrrnrigda vtaaswnhss
     1021 nveegedstf vssrrvhnpl ehseppgkqg lpeservwte erlhparpya eed
//
LOCUS       NP_445945                581 aa            linear   ROD 27-APR-2025
DEFINITION  2-hydroxyacyl-CoA lyase 1 [Rattus norvegicus].
ACCESSION   NP_445945
VERSION     NP_445945.1
DBSOURCE    REFSEQ: accession NM_053493.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Mezzar,S., De Schryver,E., Asselberghs,S., Meyhi,E., Morvay,P.L.,
            Baes,M. and Van Veldhoven,P.P.
  TITLE     Phytol-induced pathology in 2-hydroxyacyl-CoA lyase (HACL1)
            deficient mice. Evidence for a second non-HACL1-related lyase
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1862 (9), 972-990 (2017)
   PUBMED   28629946
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Kitamura,T., Seki,N. and Kihara,A.
  TITLE     Phytosphingosine degradation pathway includes fatty acid
            alpha-oxidation reactions in the endoplasmic reticulum
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), E2616-E2623 (2017)
   PUBMED   28289220
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Fraccascia,P., Casteels,M., De Schryver,E. and Van Veldhoven,P.P.
  TITLE     Role of thiamine pyrophosphate in oligomerisation, functioning and
            import of peroxisomal 2-hydroxyacyl-CoA lyase
  JOURNAL   Biochim Biophys Acta 1814 (10), 1226-1233 (2011)
   PUBMED   21708296
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Foulon,V., Sniekers,M., Huysmans,E., Asselberghs,S., Mahieu,V.,
            Mannaerts,G.P., Van Veldhoven,P.P. and Casteels,M.
  TITLE     Breakdown of 2-hydroxylated straight chain fatty acids via
            peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the
            alpha-oxidation of straight chain fatty acids
  JOURNAL   J Biol Chem 280 (11), 9802-9812 (2005)
   PUBMED   15644336
  REMARK    GeneRIF: 2-hydroxyphytanoyl-CoA lyase has a role in the breakdown
            of long chain 2-hydroxyfatty acids
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Huyghe,S., Casteels,M., Janssen,A., Meulders,L., Mannaerts,G.P.,
            Declercq,P.E., Van Veldhoven,P.P. and Baes,M.
  TITLE     Prenatal and postnatal development of peroxisomal
            lipid-metabolizing pathways in the mouse
  JOURNAL   Biochem J 353 (Pt 3), 673-680 (2001)
   PUBMED   11171065
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Foulon,V., Antonenkov,V.D., Croes,K., Waelkens,E., Mannaerts,G.P.,
            Van Veldhoven,P.P. and Casteels,M.
  TITLE     Purification, molecular cloning, and expression of
            2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine
            pyrophosphate-dependent enzyme that catalyzes the carbon-carbon
            bond cleavage during alpha-oxidation of 3-methyl-branched fatty
            acids
  JOURNAL   Proc Natl Acad Sci U S A 96 (18), 10039-10044 (1999)
   PUBMED   10468558
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ517469.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ517469.1, BC078697.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..581
                     /product="2-hydroxyacyl-CoA lyase 1"
                     /EC_number="4.1.2.63"
                     /note="2-HPCL; phytanoyl-Coenzyme A 2-hydroxylase 2;
                     phytanoyl-CoA 2-hydroxylase 2; 2-hydroxyphytanoyl-CoA
                     lyase; 2-hydroxyphytanoyl-Coenzyme A lyase"
                     /calculated_mol_wt=63485
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8CHM7.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8CHM7.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8CHM7.1)"
     Region          19..564
                     /region_name="PRK09259"
                     /note="putative oxalyl-CoA decarboxylase; Validated"
                     /db_xref="CDD:236433"
     Region          404..489
                     /region_name="Thiamine pyrophosphate binding.
                     /evidence=ECO:0000250|UniProtKB:P40149"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM7.1)"
     Region          579..581
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000250|UniProtKB:Q9UJ83"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM7.1)"
     CDS             1..581
                     /gene="Hacl1"
                     /gene_synonym="Hpcl2; Phyh2"
                     /coded_by="NM_053493.1:99..1844"
                     /db_xref="GeneID:85255"
                     /db_xref="RGD:619849"
ORIGIN      
        1 msesnsaegs drseeqvsga kviaqalktq dveymfgvvg ipvteialaa qelgikyigm
       61 rneqaacyaa savgyltgrp gvclvvsgpg lihalggman anmncwpliv iggssernqe
      121 amgafqefpq veacrlyskf sarpssiqhi pfviekavrs siygrpgacy idvpadlvtl
      181 qesttsikyk eccmppplsl aetsavraaa svlrsakqpl liigkgaays haedsirklv
      241 elcnlpflpt pmgkgvvpdn hpncvgaars ralqfadviv lfgarlnwil hfglppryqa
      301 dvkfiqidic aeelgnnvrp svtllgdvna vskqlleqfv knpwqyptds kwwetlrekr
      361 knneavskel askkslpmny ytvfyhvqeq lprncfivse gantmdigrt vlqnylprhr
      421 ldagsfgtmg vglgfaiaaa vvakerspgq rvicvegdsa fgfsgmevet icrynlpiii
      481 lvvnnngiyq gfdadtwgki lnfqgtatti ppmcllpnsh yeqvmtafgg kgyfvqtpee
      541 lqdslrqalk dtskpclini miepqstrka qdfhwltrsn i
//
LOCUS       NP_068612                130 aa            linear   ROD 27-APR-2025
DEFINITION  histone H2A type 3 [Rattus norvegicus].
ACCESSION   NP_068612 XP_579450
VERSION     NP_068612.2
DBSOURCE    REFSEQ: accession NM_021840.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Park,J.H., Kim,C.K., Lee,S.B., Lee,K.H., Cho,S.W. and Ahn,J.Y.
  TITLE     Akt attenuates apoptotic death through phosphorylation of H2A under
            hydrogen peroxide-induced oxidative stress in PC12 cells and
            hippocampal neurons
  JOURNAL   Sci Rep 6, 21857 (2016)
   PUBMED   26899247
  REMARK    GeneRIF: Akt-mediated H2A phosphorylation has an anti-apoptotic
            function in conditions of H2O2-induced oxidative stress in neurons
            and PC12 cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Lan,L., Nakajima,S., Kapetanaki,M.G., Hsieh,C.L., Fagerburg,M.,
            Thickman,K., Rodriguez-Collazo,P., Leuba,S.H., Levine,A.S. and
            Rapic-Otrin,V.
  TITLE     Monoubiquitinated histone H2A destabilizes photolesion-containing
            nucleosomes with concomitant release of UV-damaged DNA-binding
            protein E3 ligase
  JOURNAL   J Biol Chem 287 (15), 12036-12049 (2012)
   PUBMED   22334663
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Kido,T. and Lau,Y.F.
  TITLE     The rat Tspy is preferentially expressed in elongated spermatids
            and interacts with the core histones
  JOURNAL   Biochem Biophys Res Commun 350 (1), 56-67 (2006)
   PUBMED   16996029
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Benedetti,A., Fulceri,R., Allan,B.B., Houston,P., Sukhodub,A.L.,
            Marcolongo,P., Ethell,B., Burchell,B. and Burchell,A.
  TITLE     Histone 2A stimulates glucose-6-phosphatase activity by
            permeabilization of liver microsomes
  JOURNAL   Biochem J 367 (Pt 2), 505-510 (2002)
   PUBMED   12097138
  REMARK    GeneRIF: the results demonstrate that histone 2A stimulates
            glucose-6-phosphatase activity by permeabilizing the microsomal
            membrane.
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Huh,N.E., Hwang,I.W., Lim,K., You,K.H. and Chae,C.B.
  TITLE     Presence of a bi-directional S phase-specific transcription
            regulatory element in the promoter shared by testis-specific TH2A
            and TH2B histone genes
  JOURNAL   Nucleic Acids Res 19 (1), 93-98 (1991)
   PUBMED   2011515
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099140.1.
            
            On Sep 18, 2005 this sequence version replaced NP_068612.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC099140.1, CV113368.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..130
                     /product="histone H2A type 3"
                     /note="histone cluster 3, H2a; histone 3, H2a; histone 2a"
                     /calculated_mol_wt=13990
     Region          1..130
                     /region_name="PTZ00017"
                     /note="histone H2A; Provisional"
                     /db_xref="CDD:185399"
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZT6.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L7L0; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT6.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA5.
                     /evidence=ECO:0000250|UniProtKB:Q7L7L0; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT6.3)"
     Site            4
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BFU2; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT6.3)"
     Site            105
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000250|UniProtKB:P0C0S8; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT6.3)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DCAF1.
                     /evidence=ECO:0000250|UniProtKB:Q7L7L0; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT6.3)"
     CDS             1..130
                     /gene="H2ac25"
                     /gene_synonym="H2a; Hist3h2a"
                     /coded_by="NM_021840.2:6..398"
                     /db_xref="GeneID:64646"
                     /db_xref="RGD:621437"
ORIGIN      
        1 msgrgkqggk arakaksrss raglqfpvgr vhrllrkgny servgagapv ylaavleylt
       61 aeilelagna ardnkktrii prhlqlairn deelnkllgr vtiaqggvlp niqavllpkk
      121 teshhkakgk
//
LOCUS       NP_067720                336 aa            linear   ROD 27-APR-2025
DEFINITION  potassium channel subfamily K member 1 [Rattus norvegicus].
ACCESSION   NP_067720
VERSION     NP_067720.1
DBSOURCE    REFSEQ: accession NM_021688.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Jia,S., Wei,G., Bono,J., Pan,Z., Zheng,B., Wang,B., Adaralegbe,A.,
            Tenorio,C., Bekker,A. and Tao,Y.X.
  TITLE     TET1 overexpression attenuates paclitaxel-induced neuropathic pain
            through rescuing K2p1.1 expression in primary sensory neurons of
            male rats
  JOURNAL   Life Sci 297, 120486 (2022)
   PUBMED   35304127
  REMARK    GeneRIF: TET1 overexpression attenuates paclitaxel-induced
            neuropathic pain through rescuing K2p1.1 expression in primary
            sensory neurons of male rats.
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Rhodin,K., Divaris,K., North,K.E., Barros,S.P., Moss,K., Beck,J.D.
            and Offenbacher,S.
  TITLE     Chronic periodontitis genome-wide association studies: gene-centric
            and gene set enrichment analyses
  JOURNAL   J Dent Res 93 (9), 882-890 (2014)
   PUBMED   25056994
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Ma,L., Zhang,X., Zhou,M. and Chen,H.
  TITLE     Acid-sensitive TWIK and TASK two-pore domain potassium channels
            change ion selectivity and become permeable to sodium in
            extracellular acidification
  JOURNAL   J Biol Chem 287 (44), 37145-37153 (2012)
   PUBMED   22948150
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Miller,A.N. and Long,S.B.
  TITLE     Crystal structure of the human two-pore domain potassium channel
            K2P1
  JOURNAL   Science 335 (6067), 432-436 (2012)
   PUBMED   22282804
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Ma,L., Zhang,X. and Chen,H.
  TITLE     TWIK-1 two-pore domain potassium channels change ion selectivity
            and conduct inward leak sodium currents in hypokalemia
  JOURNAL   Sci Signal 4 (176), ra37 (2011)
   PUBMED   21653227
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Washburn,C.P., Bayliss,D.A. and Guyenet,P.G.
  TITLE     Cardiorespiratory neurons of the rat ventrolateral medulla contain
            TASK-1 and TASK-3 channel mRNA
  JOURNAL   Respir Physiol Neurobiol 138 (1), 19-35 (2003)
   PUBMED   14519375
  REMARK    GeneRIF: TASK-1 mRNA is present in ventrolateral medulla neurons
            that regulate respiration or circulation (C1 adrenergic neurons).
            TASK channels are expressed by respiratory cells with putative
            rhythmogenic function and by premotor and motor neurons.
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Nicolas,M.T., Barhanin,J., Reyes,R. and Dememes,D.
  TITLE     Cellular localization of TWIK-1, a two-pore-domain potassium
            channel in the rodent inner ear
  JOURNAL   Hear Res 181 (1-2), 20-26 (2003)
   PUBMED   12855359
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Konu,O., Kane,J.K., Barrett,T., Vawter,M.P., Chang,R., Ma,J.Z.,
            Donovan,D.M., Sharp,B., Becker,K.G. and Li,M.D.
  TITLE     Region-specific transcriptional response to chronic nicotine in rat
            brain
  JOURNAL   Brain Res 909 (1-2), 194-203 (2001)
   PUBMED   11478936
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Cluzeaud,F., Reyes,R., Escoubet,B., Fay,M., Lazdunski,M.,
            Bonvalet,J.P., Lesage,F. and Farman,N.
  TITLE     Expression of TWIK-1, a novel weakly inward rectifying potassium
            channel in rat kidney
  JOURNAL   Am J Physiol 275 (6), C1602-C1609 (1998)
   PUBMED   9843722
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Lesage,F., Lauritzen,I., Duprat,F., Reyes,R., Fink,M., Heurteaux,C.
            and Lazdunski,M.
  TITLE     The structure, function and distribution of the mouse TWIK-1 K+
            channel
  JOURNAL   FEBS Lett 402 (1), 28-32 (1997)
   PUBMED   9013852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC061807.1 and JAXUCZ010000019.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.59977.1,
                                           SRR26643297.52114.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..336
                     /product="potassium channel subfamily K member 1"
                     /note="rTWIK; inward rectifying potassium channel protein
                     TWIK-1; putative potassium channel TWIK; potassium
                     channel, subfamily K, member 1; potassium channel K2P1;
                     potassium channel, two pore domain subfamily K, member 1"
                     /calculated_mol_wt=38097
     Site            21..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Region          <98..157
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          117..122
                     /region_name="Selectivity filter 1.
                     /evidence=ECO:0000250|UniProtKB:O00180"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            118
                     /site_type="other"
                     /note="Important for increased permeability to Na(+) when
                     K(+) levels are subphysiological.
                     /evidence=ECO:0000250|UniProtKB:O00180; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            133..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            146
                     /site_type="other"
                     /note="Part of a hydrophobic barrier that is
                     stochastically dewetted and limits ion permeability.
                     /evidence=ECO:0000250|UniProtKB:O00180; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            182..202
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Region          191..267
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          225..230
                     /region_name="Selectivity filter 2.
                     /evidence=ECO:0000250|UniProtKB:O00180"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            244..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            261
                     /site_type="other"
                     /note="Part of a hydrophobic barrier that is
                     stochastically dewetted and limits ion permeability.
                     /evidence=ECO:0000250|UniProtKB:O00180; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Region          293..299
                     /region_name="Important for intracellular retention in
                     recycling endosomes.
                     /evidence=ECO:0000250|UniProtKB:O00180"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Region          310..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2T2.1)"
     CDS             1..336
                     /gene="Kcnk1"
                     /gene_synonym="Twik"
                     /coded_by="NM_021688.3:24..1034"
                     /db_xref="GeneID:59324"
                     /db_xref="RGD:621447"
ORIGIN      
        1 mlqslagssc vrlverhrsa wcfgflvlgy llylvfgavv fssvelpyed llrqelrklk
       61 rrfleehecl sepqleqflg rvleasnygv svlsnasgnw nwdftsalff astvlsttgy
      121 ghtvplsdgg kafciiysvi gipftllflt avvqrvtvhv trrpvlyfhi rwgfskqvva
      181 ivhavllgfv tvscfffipa avfsvleddw nflesfyfcf islstiglgd yvpgegynqk
      241 frelykigit cylllgliam lvvletfcel helkkfrkmf yvkkdkdedq vhimehdqls
      301 fssiteqaag lkeeqkqnep fvasqsppye dgsanh
//
LOCUS       NP_620807                271 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 150A precursor [Rattus norvegicus].
ACCESSION   NP_620807
VERSION     NP_620807.1
DBSOURCE    REFSEQ: accession NM_139107.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Chung,J., Nakatsu,F., Baskin,J.M. and De Camilli,P.
  TITLE     Plasticity of PI4KIIIalpha interactions at the plasma membrane
  JOURNAL   EMBO Rep 16 (3), 312-320 (2015)
   PUBMED   25608530
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zhang,J., D'Ercole,A.J. and Underwood,L.E.
  TITLE     Identification of a new gene (rat TM6P1) encoding a
            fasting-inducible, integral membrane protein with six transmembrane
            domains
  JOURNAL   Biochim Biophys Acta 1492 (1), 280-284 (2000)
   PUBMED   10858565
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF186469.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF186469.1, EV771873.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..271
                     /product="transmembrane protein 150A precursor"
                     /note="fasting-inducible; membrane integrated protein
                     containing 6 transmembrane domains; fasting-inducible
                     integral membrane protein TM6P1; transmembrane protein
                     150"
                     /calculated_mol_wt=26427
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2641
     Region          3..229
                     /region_name="Frag1"
                     /note="Frag1/DRAM/Sfk1 family; pfam10277"
                     /db_xref="CDD:431193"
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Region          5..25
                     /region_name="transmembrane domain 1"
     Site            37
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Region          80..96
                     /region_name="transmembrane domain 2"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Region          111..128
                     /region_name="transmembrane domain 3"
     Region          141..162
                     /region_name="transmembrane domain 4"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     Region          179..197
                     /region_name="transmembrane domain 5"
     Region          209..227
                     /region_name="transmembrane domain 6"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZE9.1)"
     CDS             1..271
                     /gene="Tmem150a"
                     /gene_synonym="Tm6p1; Tmem150"
                     /coded_by="NM_139107.1:128..943"
                     /db_xref="GeneID:245966"
                     /db_xref="RGD:619998"
ORIGIN      
        1 mtawillpvs lsafsitgiw tvyamavmnr hvcpvenwsy ndscspdpae qggpktcctl
       61 ddvpliskcg typpesclfs lignmgafmv alicllrygq lleqnrhswi nttalitgct
      121 naaglvvvgn fqvdhakslh yigagvafpa gllfvclhcv lfyhgattpl dmamaylrsv
      181 laviafvtlv lsgvfflhes selqhgaalc ewvfvldili fygtfsyefg avssdtlvaa
      241 lqpapgrack ssgssststh lncapesiam i
//
LOCUS       NP_113897                132 aa            linear   ROD 27-APR-2025
DEFINITION  small ribosomal subunit protein eS12 [Rattus norvegicus].
ACCESSION   NP_113897
VERSION     NP_113897.2
DBSOURCE    REFSEQ: accession NM_031709.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Lan,X., Li,D., Zhong,B., Ren,J., Wang,X., Sun,Q., Li,Y., Liu,L.,
            Liu,L. and Lu,S.
  TITLE     Identification of differentially expressed genes related to
            metabolic syndrome induced with high-fat diet in E3 rats
  JOURNAL   Exp Biol Med (Maywood) 240 (2), 235-241 (2015)
   PUBMED   25294893
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Won,K.J., Lee,P., Jung,S.H., Jiang,X., Lee,C.K., Lin,H.Y., Kang,H.,
            Lee,H.M., Kim,J., Toyokuni,S. and Kim,B.
  TITLE     3-morpholinosydnonimine participates in the attenuation of
            neointima formation via inhibition of annexin A2-mediated vascular
            smooth muscle cell migration
  JOURNAL   Proteomics 11 (2), 193-201 (2011)
   PUBMED   21204247
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Wool,I.G., Chan,Y.L., Paz,V. and Olvera,J.
  TITLE     The primary structure of rat ribosomal proteins: the amino acid
            sequences of L27a and L28 and corrections in the sequences of S4
            and S12
  JOURNAL   Biochim Biophys Acta 1050 (1-3), 69-73 (1990)
   PUBMED   2207170
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Lavergne,J.P., Marzouki,A., Reboud,J.P. and Reboud,A.M.
  TITLE     Topography and stoichiometry of acidic phosphoproteins in rat liver
            60 S ribosomal subunit
  JOURNAL   FEBS Lett 232 (1), 29-34 (1988)
   PUBMED   3366245
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Lin,A., Chan,Y.L., Jones,R. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein S12. The
            relationship of rat S12 to other ribosomal proteins and a
            correlation of the amino acid sequences of rat and yeast ribosomal
            proteins
  JOURNAL   J Biol Chem 262 (29), 14343-14351 (1987)
   PUBMED   3308890
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Collatz,E., Ulbrich,N., Tsurugi,K., Lightfoot,H.N., MacKinlay,W.,
            Lin,A. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 40 S ribosomal subunit proteins Sa, Sc,
            S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18,
            S19, S20, S21, S26, S27', and S29
  JOURNAL   J Biol Chem 252 (24), 9071-9080 (1977)
   PUBMED   925037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC058460.1.
            
            On Oct 26, 2005 this sequence version replaced NP_113897.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058460.1, FQ217474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..132
                     /product="small ribosomal subunit protein eS12"
                     /note="40S ribosomal protein S12"
                     /calculated_mol_wt=14384
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:3308890, ECO:0000269|Ref.3;
                     propagated from UniProtKB/Swiss-Prot (P63324.2)"
     Region          16..111
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..132
                     /gene="Rps12"
                     /coded_by="NM_031709.3:119..517"
                     /db_xref="GeneID:65139"
                     /db_xref="RGD:62024"
ORIGIN      
        1 maeegiaagg vmdvntalqe vlktalihdg largireaak aldkrqahlc vlasncdepm
       61 yvklvealca ehqinlikvd dnkklgewvg lckidregkp rkvvgcscvv vkdygkesqa
      121 kdvieeyfkc kk
//
LOCUS       NP_001020203             603 aa            linear   ROD 27-APR-2025
DEFINITION  T-cell surface protein tactile precursor [Rattus norvegicus].
ACCESSION   NP_001020203 XP_573281
VERSION     NP_001020203.1
DBSOURCE    REFSEQ: accession NM_001025032.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Chan,C.J., Martinet,L., Gilfillan,S., Souza-Fonseca-Guimaraes,F.,
            Chow,M.T., Town,L., Ritchie,D.S., Colonna,M., Andrews,D.M. and
            Smyth,M.J.
  TITLE     The receptors CD96 and CD226 oppose each other in the regulation of
            natural killer cell functions
  JOURNAL   Nat Immunol 15 (5), 431-438 (2014)
   PUBMED   24658051
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Kaname,T., Yanagi,K., Chinen,Y., Makita,Y., Okamoto,N., Maehara,H.,
            Owan,I., Kanaya,F., Kubota,Y., Oike,Y., Yamamoto,T., Kurosawa,K.,
            Fukushima,Y., Bohring,A., Opitz,J.M., Yoshiura,K., Niikawa,N. and
            Naritomi,K.
  TITLE     Mutations in CD96, a member of the immunoglobulin superfamily,
            cause a form of the C (Opitz trigonocephaly) syndrome
  JOURNAL   Am J Hum Genet 81 (4), 835-841 (2007)
   PUBMED   17847009
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091206.1.
            
            On Jun 25, 2005 this sequence version replaced XP_573281.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091206.1, FQ228851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..603
                     /product="T-cell surface protein tactile precursor"
                     /note="T-cell surface protein tactile; cell surface
                     antigen CD96; t cell-activated increased late expression
                     protein; CD96 antigen"
                     /calculated_mol_wt=64667
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2580
     mat_peptide     22..603
                     /product="T-cell surface protein tactile.
                     /id=PRO_0000313892"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK49.1)"
                     /calculated_mol_wt=64667
     Region          33..137
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          42..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409383"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Region          56..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409383"
     Region          99..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409383"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Region          116..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409383"
     Region          130..133
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409383"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Region          267..343
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Region          <350..493
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          359..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Region          403..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            416
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK49.1)"
     Site            538..558
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK49.1)"
     CDS             1..603
                     /gene="Cd96"
                     /coded_by="NM_001025032.1:33..1844"
                     /db_xref="GeneID:498079"
                     /db_xref="RGD:1565249"
ORIGIN      
        1 mgrkwtycvv yaiiqiqffr gaweelfnag dnnvyalpgs dvnltcqtme kdlmvqmqws
       61 kvtdeidmiv vyhpqygfhy mqgvacesrv aavetlkdat kwtlnlrnis sslsgkyecs
      121 ftmyptgtkt ivynlivepy tqdehnrtie ietnrtleip cfqntsseis prftfswlve
      181 kdgvedvlft ydyhvsnsta fkgrvglgad yglrlspvqi qddgrtfscf lrisplkvwk
      241 tsttvkvfak peilmtvent tmdvlgervf tcllknvfpk asitwlidgr lfqgneegiy
      301 itneeknsss gfwelksvlt rmhnrtsqsn nmtvwcmals pgpgnkmwnt ssqpitfsld
      361 sgtaptkrlp nvtgstlgaq tfpdaevspt rylatssmti vdenvltpdp tpqtsnssmt
      421 tkdvnysqps sgtdaknssr aasssdggsr pfpstsppkw lslphtstgp qepdsavswi
      481 ptdaytsgss dasltshdvi irttkefpdv lttangttki khghvtgitv nkprdgmswp
      541 vavatllffc illfglgvrk wcqyqkeime rpppfkpppp pikymciqep tgrgmpchem
      601 evl
//
LOCUS       NP_036739               1064 aa            linear   ROD 27-APR-2025
DEFINITION  neurofilament heavy polypeptide [Rattus norvegicus].
ACCESSION   NP_036739
VERSION     NP_036739.2
DBSOURCE    REFSEQ: accession NM_012607.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Liu,X., Xu,W., Zhang,Z., Liu,H., Lv,L., Han,D., Liu,L., Yao,A. and
            Xu,T.
  TITLE     Vascular Endothelial Growth Factor-Transfected Bone Marrow
            Mesenchymal Stem Cells Improve the Recovery of Motor and Sensory
            Functions of Rats With Spinal Cord Injury
  JOURNAL   Spine (Phila Pa 1976) 45 (7), E364-E372 (2020)
   PUBMED   32168135
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Li,J., Gu,Y., An,H., Zhou,Z., Zheng,D., Wang,Z., Wen,Z., Shen,H.Y.,
            Wang,Q. and Wang,H.
  TITLE     Cerebrospinal fluid light and heavy neurofilament level increased
            in anti-N-methyl-d-aspartate receptor encephalitis
  JOURNAL   Brain Behav 9 (8), e01354 (2019)
   PUBMED   31313506
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Ehler,J., Petzold,A., Wittstock,M., Kolbaske,S., Gloger,M.,
            Henschel,J., Heslegrave,A., Zetterberg,H., Lunn,M.P., Rommer,P.S.,
            Grossmann,A., Sharshar,T., Richter,G., Noldge-Schomburg,G. and
            Sauer,M.
  TITLE     The prognostic value of neurofilament levels in patients with
            sepsis-associated encephalopathy - A prospective, pilot
            observational study
  JOURNAL   PLoS One 14 (1), e0211184 (2019)
   PUBMED   30677080
  REMARK    Erratum:[PLoS One. 2019 Feb 20;14(2):e0212830. doi:
            10.1371/journal.pone.0212830. PMID: 30785958]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Mages,B., Aleithe,S., Altmann,S., Blietz,A., Nitzsche,B.,
            Barthel,H., Horn,A.K.E., Hobusch,C., Hartig,W., Krueger,M. and
            Michalski,D.
  TITLE     Impaired Neurofilament Integrity and Neuronal Morphology in
            Different Models of Focal Cerebral Ischemia and Human Stroke Tissue
  JOURNAL   Front Cell Neurosci 12, 161 (2018)
   PUBMED   29967576
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Zhang,X., Li,Z., Zhang,Q., Chen,L., Huang,X., Zhang,Y., Liu,X.,
            Liu,W. and Li,W.
  TITLE     Mechanisms Underlying H2O2-Evoked Carbonyl Modification of
            Cytoskeletal Protein and Axon Injury in PC-12 Cells
  JOURNAL   Cell Physiol Biochem 48 (3), 1088-1098 (2018)
   PUBMED   30041238
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Klosen,P. and van den Bosch de Aguilar,P.
  TITLE     Spontaneous perikaryal neurofilament phosphorylation in the
            septofimbrial nucleus of the rat
  JOURNAL   Neurosci Lett 139 (1), 108-113 (1992)
   PUBMED   1407676
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Pennypacker,K., Fischer,I. and Levitt,P.
  TITLE     Early in vitro genesis and differentiation of axons and dendrites
            by hippocampal neurons analyzed quantitatively with neurofilament-H
            and microtubule-associated protein 2 antibodies
  JOURNAL   Exp Neurol 111 (1), 25-35 (1991)
   PUBMED   1898595
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Chin,S.S. and Liem,R.K.
  TITLE     Transfected rat high-molecular-weight neurofilament (NF-H)
            coassembles with vimentin in a predominantly nonphosphorylated form
  JOURNAL   J Neurosci 10 (11), 3714-3726 (1990)
   PUBMED   2230956
REFERENCE   9  (residues 1 to 1064)
  AUTHORS   Schlaepfer,W.W. and Bruce,J.
  TITLE     Simultaneous up-regulation of neurofilament proteins during the
            postnatal development of the rat nervous system
  JOURNAL   J Neurosci Res 25 (1), 39-49 (1990)
   PUBMED   2108255
REFERENCE   10 (residues 1 to 1064)
  AUTHORS   Dautigny,A., Pham-Dinh,D., Roussel,C., Felix,J.M., Nussbaum,J.L.
            and Jolles,P.
  TITLE     The large neurofilament subunit (NF-H) of the rat: cDNA cloning and
            in situ detection
  JOURNAL   Biochem Biophys Res Commun 154 (3), 1099-1106 (1988)
   PUBMED   2457365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1, CB585094.1 and CB582861.1.
            
            On Oct 17, 2007 this sequence version replaced NP_036739.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M37227.1, M21964.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840122,
                                           SAMN14984016 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1064
                     /product="neurofilament heavy polypeptide"
                     /note="NF-H; 200 kDa neurofilament protein; neurofilament
                     triplet H protein; neurofilament, heavy polypeptide"
                     /calculated_mol_wt=114281
     Region          96..412
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          <495..1064
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     CDS             1..1064
                     /gene="Nefh"
                     /gene_synonym="Nfh"
                     /coded_by="NM_012607.2:53..3247"
                     /db_xref="GeneID:24587"
                     /db_xref="RGD:3159"
ORIGIN      
        1 mmsfggadal lgapfaplhg ggslhyalsr kagaggtrsa agsssgfhsw artsvssvsa
       61 spsrfrgaga asstdsldtl sngpegcvva avaarsekeq lqalndrfag yidkvrqlea
      121 hnrslegeaa alrqqqagra amgelyerev remrgavlrl gaargqlrle qehllediah
      181 vrqrldeear qreeaeaaar alarfaqeae aarvelqkka qalqeecgyl rrhhqeevge
      241 llgqiqgcga aqaqaqaear dalkcdvtsa lreiraqleg htvqstlqse ewfrvrldrl
      301 seaakvntda mrsaqeeite yrrqlqartt elealkstke slerqrsele drhqvdmasy
      361 qdaiqqldne lrntkwemaa qlreyqdlln vkmaldieia ayrkllegee crigfgpspf
      421 slteglpkip smsthikvks eekikvveks eketviveeq teeiqvteev teeedkeaqg
      481 eeeeeaeegg eeaattsppa eeaaspeket kspvkeeaks paeakspaea kspaeakspa
      541 evkspavaks paevkspaev kspaeakspa eakspaevks patvkspgea kspaeakspa
      601 evkspveaks paeakspasv kspgeakspa eakspaevks patvkspvea kspaevkspv
      661 tvkspaeaks pvevkspasv kspseakspa gakspaeaks pvvakspaea kspaeakppa
      721 eakspaeaks paeakspaea kspaeakspv evkspekaks pvkegaksla eakspekaks
      781 pvkeeikppa evkspekaks pmkeeakspe kaktldvksp eaktpakeea krpadirspe
      841 qvkspakeea kspekeetrt ekvapkkeev kspveevkak eppkkveeek tpatpktevk
      901 eskkdeapke aqkpkaeeke pltekpkdsp geakkeeake kkaaapeeet paklgvkeea
      961 kpkekaedak akepskpsek ekpkkeevpa apekkdtkee ktteskkpee kpkmeakake
     1021 edkglpqeps kpktekaeks sstdqkdsqp sekapedkaa kgdk
//
LOCUS       NP_001102592             379 aa            linear   ROD 27-APR-2025
DEFINITION  stimulator of interferon genes protein [Rattus norvegicus].
ACCESSION   NP_001102592 XP_001062602 XP_574124
VERSION     NP_001102592.1
DBSOURCE    REFSEQ: accession NM_001109122.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Mou,L., Sun,D., Qu,J., Tan,X., Wang,S., Zeng,Q. and Liu,C.
  TITLE     GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline
  JOURNAL   J Hazard Mater 476, 135101 (2024)
   PUBMED   39002476
  REMARK    GeneRIF: GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline.
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Fan,C., Du,J., Yu,Z., Wang,J., Yao,L., Ji,Z., He,W., Deng,Y.,
            Geng,D., Wu,X. and Mao,H.
  TITLE     Inhibition of MAGL attenuates Intervertebral Disc Degeneration by
            Delaying nucleus pulposus senescence through STING
  JOURNAL   Int Immunopharmacol 131, 111904 (2024)
   PUBMED   38518595
  REMARK    GeneRIF: Inhibition of MAGL attenuates Intervertebral Disc
            Degeneration by Delaying nucleus pulposus senescence through STING.
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Chen,Z., Chen,C., Yang,X., Zhou,Y., Cao,X., Han,C., Zhou,T.,
            Zhao,J. and Qin,A.
  TITLE     Dysfunction of STING Autophagy Degradation in Senescent Nucleus
            Pulposus Cells Accelerates Intervertebral Disc Degeneration
  JOURNAL   Int J Biol Sci 20 (7), 2370-2387 (2024)
   PUBMED   38725841
  REMARK    GeneRIF: Dysfunction of STING Autophagy Degradation in Senescent
            Nucleus Pulposus Cells Accelerates Intervertebral Disc
            Degeneration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Zhu,S., Chen,Q., Sun,J., Du,W., Chen,Z., Yu,M., Tao,J., Zhou,Y.,
            Zhao,Y. and Zhang,Q.
  TITLE     The cGAS-STING pathway promotes endometriosis by up-regulating
            autophagy
  JOURNAL   Int Immunopharmacol 117, 109644 (2023)
   PUBMED   36878046
  REMARK    GeneRIF: The cGAS-STING pathway promotes endometriosis by
            up-regulating autophagy.
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Wu,W., Zhang,X., Wang,S., Li,T., Hao,Q., Li,S., Yao,W. and Sun,R.
  TITLE     Pharmacological inhibition of the cGAS-STING signaling pathway
            suppresses microglial M1-polarization in the spinal cord and
            attenuates neuropathic pain
  JOURNAL   Neuropharmacology 217, 109206 (2022)
   PUBMED   35926582
  REMARK    GeneRIF: Pharmacological inhibition of the cGAS-STING signaling
            pathway suppresses microglial M1-polarization in the spinal cord
            and attenuates neuropathic pain.
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Tsuchida,T., Zou,J., Saitoh,T., Kumar,H., Abe,T., Matsuura,Y.,
            Kawai,T. and Akira,S.
  TITLE     The ubiquitin ligase TRIM56 regulates innate immune responses to
            intracellular double-stranded DNA
  JOURNAL   Immunity 33 (5), 765-776 (2010)
   PUBMED   21074459
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Saitoh,T., Fujita,N., Hayashi,T., Takahara,K., Satoh,T., Lee,H.,
            Matsunaga,K., Kageyama,S., Omori,H., Noda,T., Yamamoto,N.,
            Kawai,T., Ishii,K., Takeuchi,O., Yoshimori,T. and Akira,S.
  TITLE     Atg9a controls dsDNA-driven dynamic translocation of STING and the
            innate immune response
  JOURNAL   Proc Natl Acad Sci U S A 106 (49), 20842-20846 (2009)
   PUBMED   19926846
REFERENCE   8  (residues 1 to 379)
  AUTHORS   Ishikawa,H., Ma,Z. and Barber,G.N.
  TITLE     STING regulates intracellular DNA-mediated, type I
            interferon-dependent innate immunity
  JOURNAL   Nature 461 (7265), 788-792 (2009)
   PUBMED   19776740
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Sun,W., Li,Y., Chen,L., Chen,H., You,F., Zhou,X., Zhou,Y., Zhai,Z.,
            Chen,D. and Jiang,Z.
  TITLE     ERIS, an endoplasmic reticulum IFN stimulator, activates innate
            immune signaling through dimerization
  JOURNAL   Proc Natl Acad Sci U S A 106 (21), 8653-8658 (2009)
   PUBMED   19433799
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Zhong,B., Yang,Y., Li,S., Wang,Y.Y., Li,Y., Diao,F., Lei,C., He,X.,
            Zhang,L., Tien,P. and Shu,H.B.
  TITLE     The adaptor protein MITA links virus-sensing receptors to IRF3
            transcription factor activation
  JOURNAL   Immunity 29 (4), 538-550 (2008)
   PUBMED   18818105
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473974.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001062602.1, XP_574124.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: JN587497.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..379
                     /product="stimulator of interferon genes protein"
                     /note="mitochondrial transmembrane protein 173"
                     /calculated_mol_wt=42524
     Region          1..190
                     /region_name="Mediates interaction with ZDHHC1 and
                     ZDHHC11. /evidence=ECO:0000250|UniProtKB:Q86WV6"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            18..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Region          44..337
                     /region_name="TMEM173"
                     /note="Transmembrane protein 173; pfam15009"
                     /db_xref="CDD:464441"
     Site            45..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            92..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            117..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Region          153..340
                     /region_name="Cyclic dinucleotide-binding domain (CBD).
                     /evidence=ECO:0000269|PubMed:26669264"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86WV6; propagated from
                     UniProtKB/Swiss-Prot (F1M391.2)"
     Region          340..379
                     /region_name="C-terminal tail (CTT).
                     /evidence=ECO:0000250|UniProtKB:Q86WV6"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86WV6; propagated from
                     UniProtKB/Swiss-Prot (F1M391.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000250|UniProtKB:Q86WV6; propagated from
                     UniProtKB/Swiss-Prot (F1M391.2)"
     Region          363..366
                     /region_name="pLxIS motif.
                     /evidence=ECO:0000250|UniProtKB:Q86WV6"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M391.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000250|UniProtKB:Q86WV6; propagated from
                     UniProtKB/Swiss-Prot (F1M391.2)"
     CDS             1..379
                     /gene="Sting1"
                     /gene_synonym="RGD1562552; rSTING; Tmem173"
                     /coded_by="NM_001109122.1:357..1496"
                     /db_xref="GeneID:498840"
                     /db_xref="RGD:1562552"
ORIGIN      
        1 mpysnlhpsi prprsyrfkl aafvllvgsl mslwmtgepp shtlhylalh vasqqlglll
       61 kklcclaeel chvqsryqgs ywkavracvg spicfmalil lsfyfycsle ntsdlrlawh
      121 lgilvlsksl smtldlqsla paevsavcee knfnvahgla wsyyigylkl ilpglqarir
      181 mfnqlhnnml sgagsrrlyi lfpldcgvpd dlsvadpnir frdmlpqqnt dragvknray
      241 snsvyellen gqpagacile yatplqtlfa msqdgkagfs redrleqakl fcrtleeila
      301 dvpesrnhcr livyqeseeg nsfslsqevl rhirqeekee vtmsgpptsv aprpsllsqe
      361 prllisgmeq plplrtdli
//
LOCUS       NP_542149                836 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family B member 6 [Rattus norvegicus].
ACCESSION   NP_542149
VERSION     NP_542149.1
DBSOURCE    REFSEQ: accession NM_080582.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Zhang,C., Li,D., Zhang,J., Chen,X., Huang,M., Archacki,S., Tian,Y.,
            Ren,W., Mei,A., Zhang,Q., Fang,M., Su,Z., Yin,Y., Liu,D., Chen,Y.,
            Cui,X., Li,C., Yang,H., Wang,Q., Wang,J., Liu,M. and Deng,Y.
  TITLE     Mutations in ABCB6 cause dyschromatosis universalis hereditaria
  JOURNAL   J Invest Dermatol 133 (9), 2221-2228 (2013)
   PUBMED   23519333
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Wang,L., He,F., Bu,J., Zhen,Y., Liu,X., Du,W., Dong,J.,
            Cooney,J.D., Dubey,S.K., Shi,Y., Gong,B., Li,J., McBride,P.F.,
            Jia,Y., Lu,F., Soltis,K.A., Lin,Y., Namburi,P., Liang,C.,
            Sundaresan,P., Paw,B.H., Li,W., Li,D.Y., Phillips,J.D. and Yang,Z.
  TITLE     ABCB6 mutations cause ocular coloboma
  JOURNAL   Am J Hum Genet 90 (1), 40-48 (2012)
   PUBMED   22226084
  REMARK    Erratum:[Am J Hum Genet. 2012 Aug 10;91(2):397. Zhen, Yuanli
            [added]; Li, Wei [added]; Wang, Lejing [corrected to Wang, Lejin];
            Liu, Xiaqi [corrected to Liu, Xiaoqui]]
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Aldahmesh,M.A., Mohamed,J.Y., Alkuraya,H.S., Verma,I.C., Puri,R.D.,
            Alaiya,A.A., Rizzo,W.B. and Alkuraya,F.S.
  TITLE     Recessive mutations in ELOVL4 cause ichthyosis, intellectual
            disability, and spastic quadriplegia
  JOURNAL   Am J Hum Genet 89 (6), 745-750 (2011)
   PUBMED   22100072
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Tsuchida,M., Emi,Y., Kida,Y. and Sakaguchi,M.
  TITLE     Human ABC transporter isoform B6 (ABCB6) localizes primarily in the
            Golgi apparatus
  JOURNAL   Biochem Biophys Res Commun 369 (2), 369-375 (2008)
   PUBMED   18279659
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Krishnamurthy,P.C., Du,G., Fukuda,Y., Sun,D., Sampath,J.,
            Mercer,K.E., Wang,J., Sosa-Pineda,B., Murti,K.G. and Schuetz,J.D.
  TITLE     Identification of a mammalian mitochondrial porphyrin transporter
  JOURNAL   Nature 443 (7111), 586-589 (2006)
   PUBMED   17006453
REFERENCE   7  (residues 1 to 836)
  AUTHORS   Melaine,N., Satie,A.P., Lassurguere,J., Desmots,S., Jegou,B. and
            Samson,M.
  TITLE     Molecular cloning of several rat ABC transporters including a new
            ABC transporter, Abcb8, and their expression in rat testis
  JOURNAL   Int J Androl 29 (3), 392-399 (2006)
   PUBMED   16390497
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Mitsuhashi,N., Miki,T., Senbongi,H., Yokoi,N., Yano,H.,
            Miyazaki,M., Nakajima,N., Iwanaga,T., Yokoyama,Y., Shibata,T. and
            Seino,S.
  TITLE     MTABC3, a novel mitochondrial ATP-binding cassette protein involved
            in iron homeostasis
  JOURNAL   J Biol Chem 275 (23), 17536-17540 (2000)
   PUBMED   10837493
REFERENCE   9  (residues 1 to 836)
  AUTHORS   Hirsch-Ernst,K.I., Gaini-Rahimi,S., Ernst,B.P., Schmitz-Salue,C.,
            Blume,S. and Kahl,G.F.
  TITLE     Molecular cDNA cloning and tissue distribution of mRNA encoding a
            novel ATP-binding cassette (ABC) half-transporter
  JOURNAL   Biochem Biophys Res Commun 249 (1), 151-155 (1998)
   PUBMED   9705847
REFERENCE   10 (residues 1 to 836)
  AUTHORS   Furuya,K.N., Bradley,G., Sun,D., Schuetz,E.G. and Schuetz,J.D.
  TITLE     Identification of a new P-glycoprotein-like ATP-binding cassette
            transporter gene that is overexpressed during hepatocarcinogenesis
  JOURNAL   Cancer Res 57 (17), 3708-3716 (1997)
   PUBMED   9288777
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ003004.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ003004.1, BC085712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..836
                     /product="ATP-binding cassette sub-family B member 6"
                     /EC_number="7.6.2.5"
                     /note="ATP-binding cassette, sub-family B (MDR/TAP),
                     member 6; ATP-binding cassette sub-family B member 6,
                     mitochondrial; ABC-type heme transporter ABCB6;
                     ubiquitously-expressed mammalian ABC half transporter;
                     mammalian mitochondrial ABC protein 3; ATP-binding
                     cassette, subfamily B (MDR/TAP), member 6"
                     /calculated_mol_wt=93174
     Region          1..236
                     /region_name="Required for ATPase activity.
                     /evidence=ECO:0000250|UniProtKB:Q9NP58"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Region          1..205
                     /region_name="Required for the lysosomal targeting.
                     /evidence=ECO:0000250|UniProtKB:Q9NP58"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Region          6..255
                     /region_name="MTABC_N"
                     /note="Mitochondrial ABC-transporter N-terminal five TM
                     region; pfam16185"
                     /db_xref="CDD:465049"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Region          232..830
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            376..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            398..418
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            500..520
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     Site            530..550
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70595.1)"
     CDS             1..836
                     /gene="Abcb6"
                     /gene_synonym="MTABC3"
                     /coded_by="NM_080582.1:155..2665"
                     /db_xref="GeneID:140669"
                     /db_xref="RGD:71077"
ORIGIN      
        1 mvtvgnycea egpagpawtq nglspcffyt lvpstlmtlg vlalvlvlpc rrrevpagte
       61 elswaagprv apyalqlsla ilqmalplas lagrvgtarg vrlpgyllla svleslasac
      121 glwllvvers qarqslamgv wmkfrhslgl lllwtvtfaa enlvlvswns pqwwwsradl
      181 gqqvqfglwv lrymtsgglf ilglwapglr pqsytlhvne edqdggrnqg rstdprstwr
      241 dlgrklrlls gylwprgsps lqltvllcmg lmgldralnv lvpifyrdiv nlltskapws
      301 slawtvttyv flkflqgggt gstgfvsnlr tflwirvqqf tsrgvelrlf shlhelslrw
      361 hlgrrtgevl rivdrgtssv tgllsylvfn iiptladiii giiyfsmffn awfglivflc
      421 mslyliltim vtewrakfrr dmntqenatr aravdsllnf etvkyynaeg yeleryreai
      481 lkfqglewks taslvllnqt qnmvigfgll agsllcayfv serrlqvgdf vlfgtyitql
      541 ymplnwfgty yrmiqtnfid menmfdllke etevkdvpga gplrfhkgrv efenvhfsya
      601 dgretlqdvs ftvmpgqtva lvgpsgagks tilrllfrfy dissgcirid gqdisqvtqi
      661 slrshigvvp qdtvlfndti annirygrvt agdseiqaaa qaagihdail sfpegyetqv
      721 gerglklsgg ekqrvaiart ilkapdiill deatsaldts neraiqasla kvctnrttiv
      781 vahrlstvvn adqilvikdg ciiergrhea llsrggvyae mwqlqqqgqe tvpeds
//
LOCUS       NP_445866                740 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX1 [Rattus norvegicus].
ACCESSION   NP_445866 XP_343038
VERSION     NP_445866.1
DBSOURCE    REFSEQ: accession NM_053414.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Li,Z., Zhou,M., Cai,Z., Liu,H., Zhong,W., Hao,Q., Cheng,D., Hu,X.,
            Hou,J., Xu,P., Xue,Y., Zhou,Y. and Xu,T.
  TITLE     RNA-binding protein DDX1 is responsible for fatty acid-mediated
            repression of insulin translation
  JOURNAL   Nucleic Acids Res 46 (22), 12052-12066 (2018)
   PUBMED   30295850
  REMARK    GeneRIF: DDX1-mediated repression of insulin translation worsens
            the situation of insulin resistance and contributes to the
            elevation of blood glucose levels in obese animals
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Jefferson,M., Donaszi-Ivanov,A., Pollen,S., Dalmay,T., Saalbach,G.
            and Powell,P.P.
  TITLE     Host factors that interact with the pestivirus N-terminal protease,
            Npro, are components of the ribonucleoprotein complex
  JOURNAL   J Virol 88 (18), 10340-10353 (2014)
   PUBMED   24965446
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Popow,J., Jurkin,J., Schleiffer,A. and Martinez,J.
  TITLE     Analysis of orthologous groups reveals archease and DDX1 as tRNA
            splicing factors
  JOURNAL   Nature 511 (7507), 104-107 (2014)
   PUBMED   24870230
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Perez-Gonzalez,A., Pazo,A., Navajas,R., Ciordia,S.,
            Rodriguez-Frandsen,A. and Nieto,A.
  TITLE     hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel
            transcription-dependent shuttling RNA-transporting complex
  JOURNAL   PLoS One 9 (3), e90957 (2014)
   PUBMED   24608264
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Onishi,H., Kino,Y., Morita,T., Futai,E., Sasagawa,N. and Ishiura,S.
  TITLE     MBNL1 associates with YB-1 in cytoplasmic stress granules
  JOURNAL   J Neurosci Res 86 (9), 1994-2002 (2008)
   PUBMED   18335541
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Chen,H.C., Lin,W.C., Tsay,Y.G., Lee,S.C. and Chang,C.J.
  TITLE     An RNA helicase, DDX1, interacting with poly(A) RNA and
            heterogeneous nuclear ribonucleoprotein K
  JOURNAL   J Biol Chem 277 (43), 40403-40409 (2002)
   PUBMED   12183465
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Bleoo,S., Sun,X., Hendzel,M.J., Rowe,J.M., Packer,M. and Godbout,R.
  TITLE     Association of human DEAD box protein DDX1 with a cleavage
            stimulation factor involved in 3'-end processing of pre-MRNA
  JOURNAL   Mol Biol Cell 12 (10), 3046-3059 (2001)
   PUBMED   11598190
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Karlsson,A., Helou,K., Walentinsson,A., Hedrich,H.J., Szpirer,C.
            and Levan,G.
  TITLE     Amplification of Mycn, Ddx1, Rrm2, and Odc1 in rat uterine
            endometrial carcinomas
  JOURNAL   Genes Chromosomes Cancer 31 (4), 345-356 (2001)
   PUBMED   11433525
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Godbout,R. and Squire,J.
  TITLE     Amplification of a DEAD box protein gene in retinoblastoma cell
            lines
  JOURNAL   Proc Natl Acad Sci U S A 90 (16), 7578-7582 (1993)
   PUBMED   7689221
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082049.1.
            
            On Apr 19, 2005 this sequence version replaced XP_343038.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..740
                     /product="ATP-dependent RNA helicase DDX1"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 1; DEAD/H-box helicase 1; DEAD/H
                     (Asp-Glu-Ala-Asp/His) box polypeptide 1; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 1; DEAD
                     (Asp-Glu-Ala-Asp) box helicase 1"
                     /calculated_mol_wt=82366
     Region          1..525
                     /region_name="Necessary for interaction with RELA.
                     /evidence=ECO:0000250|UniProtKB:Q92499"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y8.1)"
     Region          1..448
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000250|UniProtKB:Q91VR5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y8.1)"
     Region          1..295
                     /region_name="Necessary for interaction with HNRNPK.
                     /evidence=ECO:0000250|UniProtKB:Q92499"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y8.1)"
     Region          4..>62
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            48..54
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          93..245
                     /region_name="SPRY_DDX1"
                     /note="SPRY domain associated with DEAD box gene DDX1;
                     cd12873"
                     /db_xref="CDD:293933"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92499; propagated from
                     UniProtKB/Swiss-Prot (Q641Y8.1)"
     Site            268
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92499; propagated from
                     UniProtKB/Swiss-Prot (Q641Y8.1)"
     Site            281
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q92499; propagated from
                     UniProtKB/Swiss-Prot (Q641Y8.1)"
     Region          284..625
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          370..373
                     /region_name="DEAD box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y8.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q641Y8.1)"
     Region          525..740
                     /region_name="Necessary for interaction with HNRNPK.
                     /evidence=ECO:0000250|UniProtKB:Q92499"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Y8.1)"
     CDS             1..740
                     /gene="Ddx1"
                     /coded_by="NM_053414.1:47..2269"
                     /db_xref="GeneID:84474"
                     /db_xref="RGD:619903"
ORIGIN      
        1 maafsemgvm peiaqaveem dwllptdiqa esiplilggg dvlmaaetgs gktgafsipv
       61 iqivyetlkd qqegkkgkat iktgasvlnk wqmnpydrgs afaigsdglc cqsrevkewh
      121 gcratrgllr gkhyyevsch dqglcrvgws tmqasldlgt dkfgfgfggt gkkshnkqfd
      181 nygeeftmhd tigcyldidk ghvkfskngk dlglafeipa hiknqalfpa cvlknaelkf
      241 nfgeeefkfp pkdgfvalsk apdsyvvksq htgnaqvsqt kflpnapkal ivepsrelae
      301 qtlnnvkqfk kyidnpklre lliiggvaar dqlsvldngv divvgtpgrl ddlvstgkln
      361 lsqvrflvld eadgllsqgy sdfinrmhnq ipqitsdgkr lqvivcsatl hsfdvkklse
      421 kimhfptwvd lkgedsvpdt vhhvvvpvnp ktdrlwerlg knhirtddvh akdntrpgan
      481 spemwseaik ilkgeyavra ikehkmdqai ifcrtkidcd nleqyfmqqg ggpdkkghqf
      541 scvclhgdrk pherkqnler fkkgdvrfli ctdvaargid ihgvpyvinv tlpdekqnyv
      601 hrigrvgrae rmglaislva tekekvwyhv csnrgkgcyn trlkedggct iwynemqlls
      661 eieehlncti sqvepdikvp vdefdgkvty gqkraagggn ykghvdilap tvqelaalek
      721 eaqtsflhlg ylpnqlfrtf
//
LOCUS       NP_059004                960 aa            linear   ROD 27-APR-2025
DEFINITION  semaphorin-6C precursor [Rattus norvegicus].
ACCESSION   NP_059004
VERSION     NP_059004.1
DBSOURCE    REFSEQ: accession NM_017308.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Yoshida,Y., Han,B., Mendelsohn,M. and Jessell,T.M.
  TITLE     PlexinA1 signaling directs the segregation of proprioceptive
            sensory axons in the developing spinal cord
  JOURNAL   Neuron 52 (5), 775-788 (2006)
   PUBMED   17145500
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Qu,X., Wei,H., Zhai,Y., Que,H., Chen,Q., Tang,F., Wu,Y., Xing,G.,
            Zhu,Y., Liu,S., Fan,M. and He,F.
  TITLE     Identification, characterization, and functional study of the two
            novel human members of the semaphorin gene family
  JOURNAL   J Biol Chem 277 (38), 35574-35585 (2002)
   PUBMED   12110693
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Kikuchi,K., Chedotal,A., Hanafusa,H., Ujimasa,Y., de Castro,F.,
            Goodman,C.S. and Kimura,T.
  TITLE     Cloning and characterization of a novel class VI semaphorin,
            semaphorin Y
  JOURNAL   Mol Cell Neurosci 13 (1), 9-23 (1999)
   PUBMED   10049528
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB000817.2.
            
            Sequence Note: This sequence has been modified as follows: removed
            16 bp suspected to be vector contamination from the 5' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000817.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..960
                     /product="semaphorin-6C precursor"
                     /note="semaphorin-Y; Sema Y; sema domain, transmembrane
                     domain (TM), and cytoplasmic domain, (semaphorin) 6C"
                     /calculated_mol_wt=100088
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2541
     mat_peptide     24..960
                     /product="Semaphorin-6C. /id=PRO_0000032346"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
                     /calculated_mol_wt=100088
     Region          52..516
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Site            436
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Region          517..>538
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          555..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Site            636..656
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Region          685..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Region          730..>956
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          745..792
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
     Region          806..960
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTL3.1)"
     CDS             1..960
                     /gene="Sema6c"
                     /coded_by="NM_017308.1:35..2917"
                     /db_xref="GeneID:29744"
                     /db_xref="RGD:3659"
ORIGIN      
        1 mpraphsmpl llllllslpq aqtafpqdpi plltsdlqgt spsswfrgle ddavaaelgl
       61 dfqrfltlnr tllvaardhv fsfdlqaqee geglvpnkfl twrsqdmenc avrgkltdec
      121 ynyirvlvpw dsqtllacgt nsfspvcrsy gitslqqege elsgqarcpf datqstvais
      181 aegslysata adfqasdavv yrslgpqppl rsakydskwl rephfvyale hgdhvyfffr
      241 evsvedarlg rvqfsrvarv ckrdmggspr aldrhwtsfl klrlncsvpg dstfyfdvlq
      301 sltgpvnlhg rsalfgvftt qtnsipgsav cafylddier gfegkfkeqr sldgawtpvs
      361 edkvpsprpg scagvgaaal fsssqdlpdd vllfikahpl ldpavppath qplltltsra
      421 lltqvavdgm agphrnttvl flgsndgtvl kvlppggqsl gpepiileei daysharcsg
      481 krspraarri igleldtegh rlfvafpgci vylslsrcar hgacqrscla sldpycgwhr
      541 frgcvnirgp ggtdvdltgn qesmehgdcq dgatgsqsgp gdsayvllgp gpspetpssp
      601 sdahpgpqss tlgahtqgvr rdlspasasr sipiplllac vaaafalgas vsgllvscac
      661 rranrrrskd ietpglprpl slrslarlhg ggpepppppk dgdaaqtpql yttflpppeg
      721 gsppelaclp tpettpelpv khlrasggpw ewnqngnnas egpgrprgcs aaggpaprvl
      781 vrppppgcpg qevevttlee llrylhgpqp prkgseplas apftsrppas epgaalfvds
      841 spmprdcvpp lrldvppdgk raapsgrpal sapaprlgvs gsrrlpfpth rappglltrv
      901 psggpsrysg gpgrhllylg rpdghrgrsl krvdvkspls pkpplatppq paphgshfnf
//
LOCUS       NP_001013137             377 aa            linear   ROD 27-APR-2025
DEFINITION  guanine nucleotide-binding protein subunit alpha-13 [Rattus
            norvegicus].
ACCESSION   NP_001013137 XP_221066
VERSION     NP_001013137.1
DBSOURCE    REFSEQ: accession NM_001013119.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wang,Y., Chen,D., Zhang,Y., Wang,P., Zheng,C., Zhang,S., Yu,B.,
            Zhang,L., Zhao,G., Ma,B., Cai,Z., Xie,N., Huang,S., Liu,Z., Mo,X.,
            Guan,Y., Wang,X., Fu,Y., Ma,D., Wang,Y. and Kong,W.
  TITLE     Novel Adipokine, FAM19A5, Inhibits Neointima Formation After Injury
            Through Sphingosine-1-Phosphate Receptor 2
  JOURNAL   Circulation 138 (1), 48-63 (2018)
   PUBMED   29453251
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Jiang,L.I., Wang,J.E. and Sternweis,P.C.
  TITLE     Regions on adenylyl cyclase VII required for selective regulation
            by the G13 pathway
  JOURNAL   Mol Pharmacol 83 (3), 587-593 (2013)
   PUBMED   23229509
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Zhang,Y., Fu,C., Asico,L.D., Villar,V.A., Ren,H., He,D., Wang,Z.,
            Yang,J., Jose,P.A. and Zeng,C.
  TITLE     Role of Galpha(12)- and Galpha(13)-protein subunit linkage of D(3)
            dopamine receptors in the natriuretic effect of D(3) dopamine
            receptor in kidney
  JOURNAL   Hypertens Res 34 (9), 1011-1016 (2011)
   PUBMED   21633357
  REMARK    GeneRIF: It was concluded that a D3 receptor interaction with
            Galpha12/Galpha13 that increases sodium excretion may have a role
            in the regulation of blood pressure.
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Gu,J.L., Muller,S., Mancino,V., Offermanns,S. and Simon,M.I.
  TITLE     Interaction of G alpha(12) with G alpha(13) and G alpha(q)
            signaling pathways
  JOURNAL   Proc Natl Acad Sci U S A 99 (14), 9352-9357 (2002)
   PUBMED   12077299
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Klages,B., Brandt,U., Simon,M.I., Schultz,G. and Offermanns,S.
  TITLE     Activation of G12/G13 results in shape change and
            Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse
            platelets
  JOURNAL   J Cell Biol 144 (4), 745-754 (1999)
   PUBMED   10037795
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Jho,E.H. and Malbon,C.C.
  TITLE     Galpha12 and Galpha13 mediate differentiation of P19 mouse
            embryonal carcinoma cells in response to retinoic acid
  JOURNAL   J Biol Chem 272 (39), 24461-24467 (1997)
   PUBMED   9305907
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Macrez-Lepretre,N., Kalkbrenner,F., Morel,J.L., Schultz,G. and
            Mironneau,J.
  TITLE     G protein heterotrimer Galpha13beta1gamma3 couples the angiotensin
            AT1A receptor to increases in cytoplasmic Ca2+ in rat portal vein
            myocytes
  JOURNAL   J Biol Chem 272 (15), 10095-10102 (1997)
   PUBMED   9092554
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Offermanns,S., Mancino,V., Revel,J.P. and Simon,M.I.
  TITLE     Vascular system defects and impaired cell chemokinesis as a result
            of Galpha13 deficiency
  JOURNAL   Science 275 (5299), 533-536 (1997)
   PUBMED   8999798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY553632.1.
            
            On Apr 20, 2005 this sequence version replaced XP_221066.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY553631.1, AY553632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="SHR"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..377
                     /product="guanine nucleotide-binding protein subunit
                     alpha-13"
                     /note="guanine nucleotide binding protein, alpha 13; G
                     alpha-13; guanine nucleotide binding protein (G protein),
                     alpha 13"
                     /calculated_mol_wt=43881
     Region          29..375
                     /region_name="G_alpha"
                     /note="G protein alpha subunit; smart00275"
                     /db_xref="CDD:214595"
     Region          50..63
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     Region          195..203
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q14344; propagated from
                     UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     Region          218..227
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     Region          287..294
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     Region          347..352
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q7Y5.1)"
     CDS             1..377
                     /gene="Gna13"
                     /gene_synonym="Galpha13"
                     /coded_by="NM_001013119.1:1..1134"
                     /db_xref="GeneID:303634"
                     /db_xref="RGD:1310221"
ORIGIN      
        1 madflpsrsv lsvcfpgcvl tngeaeqqrk skeidkclsr ektyvkrlvk illlgagesg
       61 kstflkqmri ihgqdfdqra reefrptiys nvikgmrvlv dareklhipw gdnknqvhgd
      121 klmafdtrap maaqgmvetr vflqylpair alwddsgiqn aydrrrefql gesvkyfldn
      181 ldklgvpdyi psqqdillar rptkgiheyd feiknvpfkm vdvggqrser krwfecfdsv
      241 tsilflvsss efdqvlmedr ltnrltesln ifetivnnrv fsnvsiilfl nktdlleekv
      301 qvvsikdyfl efegdphclr dvqkflvecf rgkrrdqqqr plyhhfttai ntenirlvfr
      361 dvkdtilhdn lkqlmlq
//
LOCUS       NP_001102871              98 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor A protein-like 7 [Rattus
            norvegicus].
ACCESSION   NP_001102871 XP_001056630
VERSION     NP_001102871.1
DBSOURCE    REFSEQ: accession NM_001109401.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Rattan,R., Narita,K., Chien,J., Maguire,J.L., Shridhar,R., Giri,S.
            and Shridhar,V.
  TITLE     TCEAL7, a putative tumor suppressor gene, negatively regulates
            NF-kappaB pathway
  JOURNAL   Oncogene 29 (9), 1362-1373 (2010)
   PUBMED   19966855
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Chien,J., Narita,K., Rattan,R., Giri,S., Shridhar,R., Staub,J.,
            Beleford,D., Lai,J., Roberts,L.R., Molina,J., Kaufmann,S.H.,
            Prendergast,G.C. and Shridhar,V.
  TITLE     A role for candidate tumor-suppressor gene TCEAL7 in the regulation
            of c-Myc activity, cyclin D1 levels and cellular transformation
  JOURNAL   Oncogene 27 (58), 7223-7234 (2008)
   PUBMED   18806825
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474117.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001056630.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: FQ215415.1, FQ214942.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760384, SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..98
                     /product="transcription elongation factor A protein-like
                     7"
                     /note="TCEA-like protein 7; transcription elongation
                     factor S-II protein-like 7; transcription elongation
                     factor A (SII)-like 7"
                     /calculated_mol_wt=11802
     Region          1..98
                     /region_name="BEX"
                     /note="Brain expressed X-linked like family; pfam04538"
                     /db_xref="CDD:461346"
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZT37.1)"
     CDS             1..98
                     /gene="Tceal7"
                     /coded_by="NM_001109401.1:134..430"
                     /db_xref="GeneID:680319"
                     /db_xref="RGD:1593009"
ORIGIN      
        1 mqrscnekeg kpkcsepkre eehpygafeg qrlegnfrqr llqsleefke didyrhfkge
       61 emtgeeeeme rcleeirslr kkfralhsnr thsrdrpf
//
LOCUS       NP_570091               1505 aa            linear   ROD 27-APR-2025
DEFINITION  synaptonemal complex protein 2 [Rattus norvegicus].
ACCESSION   NP_570091 XP_346681
VERSION     NP_570091.1
DBSOURCE    REFSEQ: accession NM_130735.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1505)
  AUTHORS   Zhou,J., Stein,P., Leu,N.A., Chmatal,L., Xue,J., Ma,J., Huang,X.,
            Lampson,M.A., Schultz,R.M. and Wang,P.J.
  TITLE     Accelerated reproductive aging in females lacking a novel
            centromere protein SYCP2L
  JOURNAL   Hum Mol Genet 24 (22), 6505-6514 (2015)
   PUBMED   26362258
REFERENCE   2  (residues 1 to 1505)
  AUTHORS   Llano,E., Herran,Y., Garcia-Tunon,I., Gutierrez-Caballero,C., de
            Alava,E., Barbero,J.L., Schimenti,J., de Rooij,D.G.,
            Sanchez-Martin,M. and Pendas,A.M.
  TITLE     Meiotic cohesin complexes are essential for the formation of the
            axial element in mice
  JOURNAL   J Cell Biol 197 (7), 877-885 (2012)
   PUBMED   22711701
REFERENCE   3  (residues 1 to 1505)
  AUTHORS   La Salle,S., Palmer,K., O'Brien,M., Schimenti,J.C., Eppig,J. and
            Handel,M.A.
  TITLE     Spata22, a novel vertebrate-specific gene, is required for meiotic
            progress in mouse germ cells
  JOURNAL   Biol Reprod 86 (2), 45 (2012)
   PUBMED   22011390
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1505)
  AUTHORS   Berkowitz,K.M., Sowash,A.R., Koenig,L.R., Urcuyo,D., Khan,F.,
            Yang,F., Wang,P.J., Jongens,T.A. and Kaestner,K.H.
  TITLE     Disruption of CHTF18 causes defective meiotic recombination in male
            mice
  JOURNAL   PLoS Genet 8 (11), e1002996 (2012)
   PUBMED   23133398
REFERENCE   5  (residues 1 to 1505)
  AUTHORS   Kouznetsova,A., Benavente,R., Pastink,A. and Hoog,C.
  TITLE     Meiosis in mice without a synaptonemal complex
  JOURNAL   PLoS One 6 (12), e28255 (2011)
   PUBMED   22164254
REFERENCE   6  (residues 1 to 1505)
  AUTHORS   Shakib,K., Norman,J.T., Fine,L.G., Brown,L.R. and
            Godovac-Zimmermann,J.
  TITLE     Proteomics profiling of nuclear proteins for kidney fibroblasts
            suggests hypoxia, meiosis, and cancer may meet in the nucleus
  JOURNAL   Proteomics 5 (11), 2819-2838 (2005)
   PUBMED   15942958
REFERENCE   7  (residues 1 to 1505)
  AUTHORS   Eijpe,M., Heyting,C., Gross,B. and Jessberger,R.
  TITLE     Association of mammalian SMC1 and SMC3 proteins with meiotic
            chromosomes and synaptonemal complexes
  JOURNAL   J Cell Sci 113 (Pt 4), 673-682 (2000)
   PUBMED   10652260
REFERENCE   8  (residues 1 to 1505)
  AUTHORS   Schalk,J.A., Offenberg,H.H., Peters,E., Groot,N.P., Hoovers,J.M.
            and Heyting,C.
  TITLE     Isolation and characterization of the human SCP2 cDNA and
            chromosomal localization of the gene
  JOURNAL   Mamm Genome 10 (6), 642-644 (1999)
   PUBMED   10341103
REFERENCE   9  (residues 1 to 1505)
  AUTHORS   Schalk,J.A., Dietrich,A.J., Vink,A.C., Offenberg,H.H., van
            Aalderen,M. and Heyting,C.
  TITLE     Localization of SCP2 and SCP3 protein molecules within synaptonemal
            complexes of the rat
  JOURNAL   Chromosoma 107 (8), 540-548 (1998)
   PUBMED   9933407
REFERENCE   10 (residues 1 to 1505)
  AUTHORS   Offenberg,H.H., Schalk,J.A., Meuwissen,R.L., van Aalderen,M.,
            Kester,H.A., Dietrich,A.J. and Heyting,C.
  TITLE     SCP2: a major protein component of the axial elements of
            synaptonemal complexes of the rat
  JOURNAL   Nucleic Acids Res 26 (11), 2572-2579 (1998)
   PUBMED   9592139
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Y08981.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346681.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y08981.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132264,
                                           SAMD00132266 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1505
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..1505
                     /product="synaptonemal complex protein 2"
                     /function="DNA binding protein"
                     /note="SCP-2; rnSCP2; synaptonemal complex lateral element
                     protein"
                     /calculated_mol_wt=172463
     Region          9..187
                     /region_name="SYCP2_ARLD"
                     /note="Synaptonemal complex 2 armadillo-repeat-like
                     domain; pfam18581"
                     /db_xref="CDD:465809"
     Region          278..389
                     /region_name="SYCP2_SLD"
                     /note="Synaptonemal complex 2 Spt16M-like domain;
                     pfam18584"
                     /db_xref="CDD:465811"
     Region          439..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Region          536..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Region          745..764
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Region          949..974
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Region          1035..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Region          1199..1239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70608.1)"
     Site            1218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (O70608.1)"
     CDS             1..1505
                     /gene="Sycp2"
                     /coded_by="NM_130735.1:154..4671"
                     /db_xref="GeneID:83820"
                     /db_xref="RGD:69429"
ORIGIN      
        1 mpvrpdpqql ekciddalrk ndfkplvtll qidicedvki kcskqflrkl ddlicrelhk
       61 kdiqtisnil isigrcskni filgqtglqt mikqglvqkm vswfenskei ilsqrqskde
      121 avmnmiedlf dllmvvydvn degknqvles fiphicalvi dsrvnfciqq ealkkmnlml
      181 dripqdanki lcnqeiltlm snmgerildv gdyelqvgiv ealcrmttek rrqelayewf
      241 smdfianafk kikdcefetd criflnlvng mlgdrrrvft fpclsaflgk yelqipsdek
      301 leefwidfnl gshtlsfyia gddddhqwea vtvpeekvdm ynievreskk lltltlkniv
      361 kiskkegkel llyfdaalei tnvtkklfgg nkykeftrkq disvaktsih vlfdasgsqi
      421 lvpesqpspv kenlihlkek snlqkkltnp lepdnsssqr drknsqdeit tpsrkkmsea
      481 smivpdtdry tvrspillin tstprrsrap lqaihsaeka vsktsesgvd yavslksrqs
      541 dgrnrgnnra nhnktatvqn kghehhespd qtfneieetl sdayavekvd kpvlpgvldi
      601 sknkahsrwa cwtpvttikl cnnqrscalp gdtftqdtgv nkkctkqksv sdddseetqr
      661 vkyskdvikc nkseeaevce rniqeqnhpk ysqkkntana kkndwhiese ttyksvllnk
      721 tteesliykk tcvlskdvnt ticdkspsrk smrshtksrk elmsevtsce ldeipvrens
      781 kgkrftgtae slinlinkry nssddmistr klkeprdgsg fskkpelqfn kvqrksyrkl
      841 ktvvnvtsec plndvynfsl ngadepvikl giqefqattr easmdnsikl vdvrnrderd
      901 lslktkderi lsherktlfs dtetecgwdd sktdiswlrk pkskrlmdys rnkntkkcks
      961 iksrsstekg qprstvvlsk niakndyevi vdgrtrlprr atktkknykd lstsgseses
     1021 ekeisylfkd klptkeetvh ssaqtkklpk kqqkvfntea lkgqpseeqk nsstlrngre
     1081 dslylssasv sgssssvevm rctekiterd ftqdydyitk slspypkaas peflnrsnrv
     1141 vghgkspris etsavcvrks cspasglpfs prhttknnsv mnikntnsvi nnqrtqhcns
     1201 ysdvssnsse klymepespd scenhvqskr eenhaaspfs lssekiekiw fdmpndnthv
     1261 sgpsqrgskr rmyleedels npseaevqea eerehlvskk lcqrehfdqh tsetslstpe
     1321 fsvpkdwqqe lqgagmfydn insdykrktd tqhkimddft tktlkltqqh llamacqarg
     1381 hrdenidkfq vtlldelekv ekdsqtlrdl ekefvdieek ivhkmrafhq sererfralk
     1441 tsldksllvy nsvyeenvlt semclmkanm kmlqdkllke mheeellnir rgleslfkdh
     1501 egnna
//
LOCUS       NP_001103611            1216 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 5B [Rattus norvegicus].
ACCESSION   NP_001103611 XP_001055509 XP_001057591 XP_001057637 XP_218162
VERSION     NP_001103611.1
DBSOURCE    REFSEQ: accession NM_001110141.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Hinnebusch,A.G.
  TITLE     The scanning mechanism of eukaryotic translation initiation
  JOURNAL   Annu Rev Biochem 83, 779-812 (2014)
   PUBMED   24499181
  REMARK    Review article
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Bohnsack,M.T., Regener,K., Schwappach,B., Saffrich,R.,
            Paraskeva,E., Hartmann,E. and Gorlich,D.
  TITLE     Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
            transport pathways to confine translation to the cytoplasm
  JOURNAL   EMBO J 21 (22), 6205-6215 (2002)
   PUBMED   12426392
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Wilson,S.A., Sieiro-Vazquez,C., Edwards,N.J., Iourin,O.,
            Byles,E.D., Kotsopoulou,E., Adamson,C.S., Kingsman,S.M.,
            Kingsman,A.J. and Martin-Rendon,E.
  TITLE     Cloning and characterization of hIF2, a human homologue of
            bacterial translation initiation factor 2, and its interaction with
            HIV-1 matrix
  JOURNAL   Biochem J 342 (Pt 1) (Pt 1), 97-103 (1999)
   PUBMED   10432305
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Ohsawa,K., Imai,Y., Ito,D. and Kohsaka,S.
  TITLE     Molecular cloning and characterization of annexin V-binding
            proteins with highly hydrophilic peptide structure
  JOURNAL   J Neurochem 67 (1), 89-97 (1996)
   PUBMED   8667030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Oct 26, 2007 this sequence version replaced
            XP_001057637.1, XP_001057591.1, XP_218162.4, XP_001055509.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166424.1, SRR26643295.35005.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..1216
                     /product="eukaryotic translation initiation factor 5B"
                     /EC_number="3.6.5.3"
                     /note="eIF-5B; translation initiation factor IF-2; annexin
                     V-binding protein ABP-7"
                     /calculated_mol_wt=137556
     Region          1..604
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q05D44; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05D44; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     Region          623..1198
                     /region_name="PRK04004"
                     /note="translation initiation factor IF-2; Validated;
                     cl44330"
                     /db_xref="CDD:457675"
     Region          634..641
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Region          659..663
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Region          698..701
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Region          752..755
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Region          820..822
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GUV7.1)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60841; propagated from
                     UniProtKB/Swiss-Prot (B2GUV7.1)"
     CDS             1..1216
                     /gene="Eif5b"
                     /coded_by="NM_001110141.1:149..3799"
                     /db_xref="GeneID:308306"
                     /db_xref="RGD:735017"
ORIGIN      
        1 mgkkqknkse dstkddtdlg alaaeiegag aakeqepqkg kgkkkkekkk qdfdendilr
       61 eleelsleaq gigadrdaat vkptenneee saskqdkkkk gqkgkktsfd endseeledk
      121 dskskkparp nsevllsgse daddpnklsk kgkkaqkstk krdgseeded nskrskersr
      181 vnssgesgge sdeflqsrkg qkknqknksv ptidsgnedd dssfkiktva qkkaekkere
      241 rkkreeekak lrkvkekeel ekgrkeqskq repqkrpdee vlvlrgtpda gaaseekgdi
      301 aatleddneg dkkkkdkkkk ktekddkeke kkkgpskstv kaiqealakl reeeerqkre
      361 eeerikrlee leakrkeeer leqekrerkk qkekerkerl kkegklltks qreararaev
      421 tlrhlqaqgv evpskdslpk krpvyedkkk kktpqqlesk ealetvevsa pvevvdqgvp
      481 ekeetppsvd aeedeeteda glddweamas deerekegnm ihieveenpe eeeeeeeded
      541 eedsedeede gdsegsdgde edyklsdekd lgkagdtkpn kdassdseyd sdddrtkeer
      601 aydkakrrie krrlehgknv nteklrapii cvlghvdtgk tkildklrht hvqdgeaggi
      661 tqqigatnvp leaineqtkm iknfdrenvr ipgmliidtp ghesfsnlrn rgsslcdiai
      721 lvvdimhgle pqtiesinil kskkcpfiva lnkidrlydw kkspdsdvav tlkkqkkntk
      781 defeerakai ivefaqqgln aalfyenkdp rtfvslvpts ahtgdgmgsl iyllveltqt
      841 mlskrlahce elraqvmevk alpgmgttid vilingrlke gdtiivpgve gpivtqirgl
      901 llpppmkelr vknqyekhke veaaqgvkil gkdlektlag lpllvaykdd eipvlkdeli
      961 helkqtlnai kleekgvyvq astlgsleal leflktsevp yaginigpvh kkdvmkasvm
     1021 lehdpqyavi lafdvrierd aqemadslgv rifsaeiiyh lfdaftkyrq dykkqkqeef
     1081 khiavfpckm kilpqyifns rdpivigvtv eagqvkqgtp mcvpsknfvd igivtsiein
     1141 hkqvdvakkg qevcvkiepi pgespkmfgr hfeatdilvs kisrqsidal kdwfrdemqk
     1201 sdwqlivelk kvfeii
//
LOCUS       NP_001032387             264 aa            linear   ROD 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 9 [Rattus
            norvegicus].
ACCESSION   NP_001032387
VERSION     NP_001032387.1
DBSOURCE    REFSEQ: accession NM_001037310.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Malkowska,M., Kokoszynska,K., Rychlewski,L. and Wyrwicz,L.
  TITLE     Structural bioinformatics of the general transcription factor TFIID
  JOURNAL   Biochimie 95 (4), 680-691 (2013)
   PUBMED   23146842
  REMARK    Review article
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Spedale,G., Timmers,H.T. and Pijnappel,W.W.
  TITLE     ATAC-king the complexity of SAGA during evolution
  JOURNAL   Genes Dev 26 (6), 527-541 (2012)
   PUBMED   22426530
  REMARK    Review article
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Sengupta,T., Cohet,N., Morle,F. and Bieker,J.J.
  TITLE     Distinct modes of gene regulation by a cell-specific
            transcriptional activator
  JOURNAL   Proc Natl Acad Sci U S A 106 (11), 4213-4218 (2009)
   PUBMED   19251649
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Tatarakis,A., Margaritis,T., Martinez-Jimenez,C.P., Kouskouti,A.,
            Mohan,W.S. 2nd, Haroniti,A., Kafetzopoulos,D., Tora,L. and
            Talianidis,I.
  TITLE     Dominant and redundant functions of TFIID involved in the
            regulation of hepatic genes
  JOURNAL   Mol Cell 31 (4), 531-543 (2008)
   PUBMED   18722179
REFERENCE   5  (residues 1 to 264)
  AUTHORS   McKeegan,K.S., Debieux,C.M., Boulon,S., Bertrand,E. and
            Watkins,N.J.
  TITLE     A dynamic scaffold of pre-snoRNP factors facilitates human box C/D
            snoRNP assembly
  JOURNAL   Mol Cell Biol 27 (19), 6782-6793 (2007)
   PUBMED   17636026
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Buschmann,T., Lin,Y., Aithmitti,N., Fuchs,S.Y., Lu,H.,
            Resnick-Silverman,L., Manfredi,J.J., Ronai,Z. and Wu,X.
  TITLE     Stabilization and activation of p53 by the coactivator protein
            TAFII31
  JOURNAL   J Biol Chem 276 (17), 13852-13857 (2001)
   PUBMED   11278372
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Fontes,J.D., Jiang,B. and Peterlin,B.M.
  TITLE     The class II trans-activator CIITA interacts with the
            TBP-associated factor TAFII32
  JOURNAL   Nucleic Acids Res 25 (12), 2522-2528 (1997)
   PUBMED   9171108
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Aoki,T., Koike,T., Nakano,T., Shibahara,K., Nishimura,H.,
            Kikuchi,H. and Honjo,T.
  TITLE     Rat TAFII31 gene is induced upon programmed cell death in
            differentiated PC12 cells deprived of NGF
  JOURNAL   Biochem Biophys Res Commun 234 (1), 230-234 (1997)
   PUBMED   9168994
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV127122.1, CB724309.1 and BC091109.1.
            
            Transcript Variant: This variant (3) represents the longer
            transcript. Both variants 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CV127122.1, CK596546.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..264
                     /product="transcription initiation factor TFIID subunit 9"
                     /EC_number="2.7.4.3"
                     /note="TAF9 RNA polymerase II, TATA box binding
                     protein-associated factor; RNA polymerase II
                     TBP-associated factor subunit G; transcription initiation
                     factor TFIID 31 kDa subunit; transcription initiation
                     factor TFIID 32 kDa subunit; TAF9 RNA polymerase II, TATA
                     box binding protein (TBP)-associated factor"
                     /calculated_mol_wt=28863
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          9..130
                     /region_name="TFIID-31kDa"
                     /note="Transcription initiation factor IID, 31kD subunit;
                     pfam02291"
                     /db_xref="CDD:460525"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          150..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16594; propagated from
                     UniProtKB/Swiss-Prot (Q5BKE0.1)"
     Region          233..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BKE0.1)"
     CDS             1..264
                     /gene="Taf9"
                     /gene_synonym="CINAP; TAFII31; TAFII32"
                     /coded_by="NM_001037310.1:669..1463"
                     /db_xref="GeneID:373541"
                     /db_xref="RGD:727861"
ORIGIN      
        1 mesgkmaspk smpkdaqmma qilkdmgite yeprvinqml efafryvtti lddakiyssh
       61 akkptvdadd vrlaiqcrad qsftsppprd flldiarqrn qtplplikpy sgprlppdry
      121 cltapnyrlk slqkkaptpa gritvprlsv gsvssrpstp tlgtptpqam svstkvgtpm
      181 sltgqrftvq mpasqspavk asipatpavq nvlinpslig sknilittnm vsqntanesa
      241 nalkrkreee dddddddddd ydnl
//
LOCUS       NP_068510                560 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 5 group A member 2 [Rattus norvegicus].
ACCESSION   NP_068510
VERSION     NP_068510.1
DBSOURCE    REFSEQ: accession NM_021742.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Ma,B., Qiao,H., Guo,Y., Wei,J., Yang,Q., Feng,X. and Li,Z.
  TITLE     TGF-beta1 induced activations of Smad2 and miRNAs inhibit SF-1- and
            LRH-1-dependent CYP19 expression in rat Leydig cellsdagger
  JOURNAL   Biol Reprod 108 (5), 778-790 (2023)
   PUBMED   36857632
  REMARK    GeneRIF: TGF-beta1 induced activations of Smad2 and miRNAs inhibit
            SF-1- and LRH-1-dependent CYP19 expression in rat Leydig
            cellsdagger.
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Zhang,T., Yu,F., Guo,L., Chen,M., Yuan,X. and Wu,B.
  TITLE     Small Heterodimer Partner Regulates Circadian Cytochromes p450 and
            Drug-Induced Hepatotoxicity
  JOURNAL   Theranostics 8 (19), 5246-5258 (2018)
   PUBMED   30555544
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Schwaderer,J., Gaiser,A.K., Phan,T.S., Delgado,M.E. and Brunner,T.
  TITLE     Liver receptor homolog-1 (NR5a2) regulates CD95/Fas ligand
            transcription and associated T-cell effector functions
  JOURNAL   Cell Death Dis 8 (4), e2745 (2017)
   PUBMED   28406481
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Lai,W.A., Yeh,Y.T., Fang,W.L., Wu,L.S., Harada,N., Wang,P.H.,
            Ke,F.C., Lee,W.L. and Hwang,J.J.
  TITLE     Calcineurin and CRTC2 mediate FSH and TGFbeta1 upregulation of
            Cyp19a1 and Nr5a in ovary granulosa cells
  JOURNAL   J Mol Endocrinol 53 (2), 259-270 (2014)
   PUBMED   25057110
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Hale,M.A., Swift,G.H., Hoang,C.Q., Deering,T.G., Masui,T.,
            Lee,Y.K., Xue,J. and MacDonald,R.J.
  TITLE     The nuclear hormone receptor family member NR5A2 controls aspects
            of multipotent progenitor cell formation and acinar differentiation
            during pancreatic organogenesis
  JOURNAL   Development 141 (16), 3123-3133 (2014)
   PUBMED   25063451
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Pezzi,V., Sirianni,R., Chimento,A., Maggiolini,M., Bourguiba,S.,
            Delalande,C., Carreau,S., Ando,S., Simpson,E.R. and Clyne,C.D.
  TITLE     Differential expression of steroidogenic factor-1/adrenal 4 binding
            protein and liver receptor homolog-1 (LRH-1)/fetoprotein
            transcription factor in the rat testis: LRH-1 as a potential
            regulator of testicular aromatase expression
  JOURNAL   Endocrinology 145 (5), 2186-2196 (2004)
   PUBMED   14736734
  REMARK    GeneRIF: evidence provided that LRH-1 plays an important role in
            the regulation of aromatase expression in Leydig cells
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Falender,A.E., Lanz,R., Malenfant,D., Belanger,L. and Richards,J.S.
  TITLE     Differential expression of steroidogenic factor-1 and FTF/LRH-1 in
            the rodent ovary
  JOURNAL   Endocrinology 144 (8), 3598-3610 (2003)
   PUBMED   12865342
  REMARK    GeneRIF: data indicate that granulosa cells of small and
            preovulatory follicles express both SF-1 and FTF/LRH-1 and that
            each orphan receptor may regulate target gene expression in these
            cells
REFERENCE   8  (residues 1 to 560)
  AUTHORS   Liu,D.L., Liu,W.Z., Li,Q.L., Wang,H.M., Qian,D., Treuter,E. and
            Zhu,C.
  TITLE     Expression and functional analysis of liver receptor homologue 1 as
            a potential steroidogenic factor in rat ovary
  JOURNAL   Biol Reprod 69 (2), 508-517 (2003)
   PUBMED   12672674
  REMARK    GeneRIF: Liver receptor homologue 1 (LRH-1) is a member of the
            nuclear receptor superfamily originally found in liver cells. LRH-1
            participates in regulation of cholesterol metabolism and bile acid
            synthesis. Recent studies have shown that LRH-1 is even more highl
REFERENCE   9  (residues 1 to 560)
  AUTHORS   Chen,F., Ma,L., Dawson,P.A., Sinal,C.J., Sehayek,E., Gonzalez,F.J.,
            Breslow,J., Ananthanarayanan,M. and Shneider,B.L.
  TITLE     Liver receptor homologue-1 mediates species- and cell line-specific
            bile acid-dependent negative feedback regulation of the apical
            sodium-dependent bile acid transporter
  JOURNAL   J Biol Chem 278 (22), 19909-19916 (2003)
   PUBMED   12456679
REFERENCE   10 (residues 1 to 560)
  AUTHORS   Galarneau,L., Pare,J.F., Allard,D., Hamel,D., Levesque,L.,
            Tugwood,J.D., Green,S. and Belanger,L.
  TITLE     The alpha1-fetoprotein locus is activated by a nuclear receptor of
            the Drosophila FTZ-F1 family
  JOURNAL   Mol Cell Biol 16 (7), 3853-3865 (1996)
   PUBMED   8668203
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB012960.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB012960.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..560
                     /product="nuclear receptor subfamily 5 group A member 2"
                     /note="liver receptor homolog 1; FTZ-F1 beta2 protein;
                     fetoprotein transcription factor"
                     /calculated_mol_wt=63773
     Region          17..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWM1.1)"
     Region          107..199
                     /region_name="NR_DBD_Lrh-1_like"
                     /note="The DNA-binding domain of Lrh-1 like nuclear
                     receptor family like is composed of two C4-type zinc
                     fingers; cd07167"
                     /db_xref="CDD:143541"
     Site            order(107,110,124,127,143,149,159,162)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143541"
     Site            order(117..119,125..126,128,130,132..133,136,156..157,163,
                     176..178,181..187,193)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143541"
     Region          173..188
                     /region_name="C-terminal extension (CTE).
                     /evidence=ECO:0000250|UniProtKB:O00482"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWM1.1)"
     Region          189..208
                     /region_name="FTZ-F1 box.
                     /evidence=ECO:0000250|UniProtKB:O00482"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWM1.1)"
     Region          320..560
                     /region_name="NR_LBD_Lrh-1"
                     /note="The ligand binding domain of the liver receptor
                     homolog-1, a member of nuclear receptor superfamily;
                     cd07069"
                     /db_xref="CDD:132754"
     Site            order(352..357,359..361,438,539..541,543..545,547..548)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:132754"
     Site            order(361,364..365,401..402,405,409,424,435,438..440,443,
                     446..447,532,535..536,539)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132754"
     Site            order(373,376,380,390,393..394,397..398,549..550,553..554)
                     /site_type="active"
                     /note="corepressor recognition site [active]"
                     /db_xref="CDD:132754"
     Region          547..558
                     /region_name="AF-2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01189"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWM1.1)"
     CDS             1..560
                     /gene="Nr5a2"
                     /gene_synonym="Ftf; Lrh-1"
                     /coded_by="NM_021742.1:91..1773"
                     /db_xref="GeneID:60349"
                     /db_xref="RGD:68353"
ORIGIN      
        1 msassitgdf qdflkhglpa iapapgsetp hspkleekhr ekraglpdrh rrpiparsrl
       61 vmlpkvetea sglvrshgeq gqmpenmqvs qfkmvnysyd edleelcpvc gdkvsgyhyg
      121 lltcesckgf fkrtvqnqkr ytcienqncq idktqrkrcp ycrfkkcidv gmkleavrad
      181 rmrggrnkfg pmykrdralk qqkkaliran glkleamsqv iqampsdlts aiqnihsask
      241 glplshvalp ptdydrspfv tspismtmpp hgslhgyqpy ghfpnraiks eypdpysssp
      301 esmmgysymd gyqtsspasi phlilellkc epdepqvqak imaylqqeqn nrnrqeklsa
      361 fgllckmadq tlfsivewar ssiffrelkv ddqmkllqnc wsellildhi yrqvahgkeg
      421 tiflvtgehv dyssiisnte vafnnllsla qelvvrlrsl qfdqrefvcl kflvlfssdv
      481 knlenfqlve gvqeqvnaal ldytlcnypq qtekfgqlll rlpeiraisk qaedylyykh
      541 vngdvpynnl liemlhakra
//
LOCUS       NP_001002023             437 aa            linear   ROD 27-APR-2025
DEFINITION  epsilon-sarcoglycan [Rattus norvegicus].
ACCESSION   NP_001002023
VERSION     NP_001002023.1
DBSOURCE    REFSEQ: accession NM_001002023.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Hou,J.Y., Wang,Y.G., Ma,S.J., Yang,B.Y. and Li,Q.P.
  TITLE     Identification of a prognostic 5-Gene expression signature for
            gastric cancer
  JOURNAL   J Cancer Res Clin Oncol 143 (4), 619-629 (2017)
   PUBMED   28035468
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Vermiglio,G., Runci,M., Scibilia,A., Biasini,F. and Cutroneo,G.
  TITLE     Preliminary study on sarcoglycan sub-complex in rat cerebral and
            cerebellar cortex
  JOURNAL   Ital J Anat Embryol 117 (1), 54-64 (2012)
   PUBMED   22894000
  REMARK    GeneRIF: In cerebellar neurons and glial cells alpha-, beta-,
            gamma-, delta-, and epsilon-sarcoglycans are all expressed.
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Sharma,P., Tran,T., Stelmack,G.L., McNeill,K., Gosens,R.,
            Mutawe,M.M., Unruh,H., Gerthoffer,W.T. and Halayko,A.J.
  TITLE     Expression of the dystrophin-glycoprotein complex is a marker for
            human airway smooth muscle phenotype maturation
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 294 (1), L57-L68 (2008)
   PUBMED   17993586
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Esapa,C.T., Waite,A., Locke,M., Benson,M.A., Kraus,M.,
            McIlhinney,R.A., Sillitoe,R.V., Beesley,P.W. and Blake,D.J.
  TITLE     SGCE missense mutations that cause myoclonus-dystonia syndrome
            impair epsilon-sarcoglycan trafficking to the plasma membrane:
            modulation by ubiquitination and torsinA
  JOURNAL   Hum Mol Genet 16 (3), 327-342 (2007)
   PUBMED   17200151
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Xiao,J. and LeDoux,M.S.
  TITLE     Cloning, developmental regulation and neural localization of rat
            epsilon-sarcoglycan
  JOURNAL   Brain Res Mol Brain Res 119 (2), 132-143 (2003)
   PUBMED   14625080
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Coral-Vazquez,R., Cohn,R.D., Moore,S.A., Hill,J.A., Weiss,R.M.,
            Davisson,R.L., Straub,V., Barresi,R., Bansal,D., Hrstka,R.F.,
            Williamson,R. and Campbell,K.P.
  TITLE     Disruption of the sarcoglycan-sarcospan complex in vascular smooth
            muscle: a novel mechanism for cardiomyopathy and muscular dystrophy
  JOURNAL   Cell 98 (4), 465-474 (1999)
   PUBMED   10481911
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089947.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089947.1, AY164274.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132267,
                                           SAMD00132277 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q21"
     Protein         1..437
                     /product="epsilon-sarcoglycan"
                     /note="epsilon-SG"
                     /calculated_mol_wt=49709
     Region          32..419
                     /region_name="Sarcoglycan_2"
                     /note="Sarcoglycan alpha/epsilon; pfam05510"
                     /db_xref="CDD:461668"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6YAT4.1)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YAT4.1)"
     CDS             1..437
                     /gene="Sgce"
                     /coded_by="NM_001002023.2:43..1356"
                     /db_xref="GeneID:432360"
                     /db_xref="RGD:1303201"
ORIGIN      
        1 mllfwwwelg dpcawtgkgr gtlkmspatt gtflltvytl fskvhsdrnv ypsagvlfvh
       61 vlereyfkge fppypkpgev sndpitfntn lmgypdrpgw lryiqrtpys dgvlygspta
      121 envgkptiie itaynrrtfe tarhnliini msaeefplpy qaeffiknmn veemlasevl
      181 gdflgavknv wqperlnain itsaldrggr vplpikdmke gvyvmvgadv afssclreve
      241 npqnqlrcsq emepvitcdk kfrtqfyidw ckislvdktk qvstyqevvr gegilpdgge
      301 ykppsdslks rdyytdflvt lavpsavalv lflilayimc crregvekrn mqtpdiqlvh
      361 hssiqkstke lrdmsknrei awplstlpvf hpvtgeiipp mhtdnydstn mplmqtqpnl
      421 phqtqipqqq ttgkwyp
//
LOCUS       NP_599180                636 aa            linear   ROD 27-APR-2025
DEFINITION  polyadenylate-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_599180
VERSION     NP_599180.1
DBSOURCE    REFSEQ: accession NM_134353.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Tan,J., Xie,Y., Yao,A., Qin,Y., Li,L., Shen,L., Zhang,X., Xu,C.,
            Jiang,X., Wang,A. and Yan,Z.
  TITLE     Long noncoding RNA-dependent regulation of vascular smooth muscle
            cell proliferation and migration in hypertension
  JOURNAL   Int J Biochem Cell Biol 118, 105653 (2020)
   PUBMED   31743794
  REMARK    GeneRIF: Long noncoding RNA-dependent regulation of vascular smooth
            muscle cell proliferation and migration in hypertension.
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Copsey,A.C., Cooper,S., Parker,R., Lineham,E., Lapworth,C.,
            Jallad,D., Sweet,S. and Morley,S.J.
  TITLE     The helicase, DDX3X, interacts with poly(A)-binding protein 1
            (PABP1) and caprin-1 at the leading edge of migrating fibroblasts
            and is required for efficient cell spreading
  JOURNAL   Biochem J 474 (18), 3109-3120 (2017)
   PUBMED   28733330
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Bayes,A., Collins,M.O., Reig-Viader,R., Gou,G., Goulding,D.,
            Izquierdo,A., Choudhary,J.S., Emes,R.D. and Grant,S.G.
  TITLE     Evolution of complexity in the zebrafish synapse proteome
  JOURNAL   Nat Commun 8, 14613 (2017)
   PUBMED   28252024
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Suzuki,Y., Chin,W.X., Han,Q., Ichiyama,K., Lee,C.H., Eyo,Z.W.,
            Ebina,H., Takahashi,H., Takahashi,C., Tan,B.H., Hishiki,T.,
            Ohba,K., Matsuyama,T., Koyanagi,Y., Tan,Y.J., Sawasaki,T.,
            Chu,J.J., Vasudevan,S.G., Sano,K. and Yamamoto,N.
  TITLE     Characterization of RyDEN (C19orf66) as an Interferon-Stimulated
            Cellular Inhibitor against Dengue Virus Replication
  JOURNAL   PLoS Pathog 12 (1), e1005357 (2016)
   PUBMED   26735137
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Berg,J.M., Lee,C., Chen,L., Galvan,L., Cepeda,C., Chen,J.Y.,
            Penagarikano,O., Stein,J.L., Li,A., Oguro-Ando,A., Miller,J.A.,
            Vashisht,A.A., Starks,M.E., Kite,E.P., Tam,E., Gdalyahu,A.,
            Al-Sharif,N.B., Burkett,Z.D., White,S.A., Fears,S.C., Levine,M.S.,
            Wohlschlegel,J.A. and Geschwind,D.H.
  TITLE     JAKMIP1, a Novel Regulator of Neuronal Translation, Modulates
            Synaptic Function and Autistic-like Behaviors in Mouse
  JOURNAL   Neuron 88 (6), 1173-1191 (2015)
   PUBMED   26627310
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Linker,K., Pautz,A., Fechir,M., Hubrich,T., Greeve,J. and
            Kleinert,H.
  TITLE     Involvement of KSRP in the post-transcriptional regulation of human
            iNOS expression-complex interplay of KSRP with TTP and HuR
  JOURNAL   Nucleic Acids Res 33 (15), 4813-4827 (2005)
   PUBMED   16126846
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Ralser,M., Albrecht,M., Nonhoff,U., Lengauer,T., Lehrach,H. and
            Krobitsch,S.
  TITLE     An integrative approach to gain insights into the cellular function
            of human ataxin-2
  JOURNAL   J Mol Biol 346 (1), 203-214 (2005)
   PUBMED   15663938
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Villace,P., Marion,R.M. and Ortin,J.
  TITLE     The composition of Staufen-containing RNA granules from human cells
            indicates their role in the regulated transport and translation of
            messenger RNAs
  JOURNAL   Nucleic Acids Res 32 (8), 2411-2420 (2004)
   PUBMED   15121898
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Mohr,E., Prakash,N., Vieluf,K., Fuhrmann,C., Buck,F. and Richter,D.
  TITLE     Vasopressin mRNA localization in nerve cells: characterization of
            cis-acting elements and trans-acting factors
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7072-7079 (2001)
   PUBMED   11416190
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ298278.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ298278.1, BC083176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..636
                     /product="polyadenylate-binding protein 1"
                     /note="poly(A)-binding protein 1; PABP-1"
                     /calculated_mol_wt=70570
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Region          11..615
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          166..289
                     /region_name="UNR-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            299
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            385
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            419
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            432
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            436
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            455
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by CARM1.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            460
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by CARM1.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            475
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P29341; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            481
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            493
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940; Dimethylated
                     arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            506
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            512
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     Site            518
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P11940; propagated from
                     UniProtKB/Swiss-Prot (Q9EPH8.1)"
     CDS             1..636
                     /gene="Pabpc1"
                     /gene_synonym="Pabp; PABP 1; Pabp1"
                     /coded_by="NM_134353.3:200..2110"
                     /db_xref="GeneID:171350"
                     /db_xref="RGD:619838"
ORIGIN      
        1 mnpsapsypm aslyvgdlhp dvteamlyek fspagpilsi rvcrdmitrr slgyayvnfq
       61 qpadaerald tmnfdvikgk pvrimwsqrd pslrksgvgn ifiknldksi dnkalydtfs
      121 afgnilsckv vcdengskgy gfvhfetqea aeraiekmng mllndrkvfv grfksrkere
      181 aelgarakef tnvyiknfge dmdderlkel fgkfgpalsv kvmtdesgks kgfgfvsfer
      241 hedaqkavde mngkelngkq iyvgraqkkv erqtelkrkf eqmkqdritr yqgvnlyvkn
      301 lddgidderl rkefspfgti tsakvmmegg rskgfgfvcf sspeeatkav temngrivat
      361 kplyvalaqr keerqahltn qymqrmasvr avpnpvinpy qpappsgyfm aaipqtqnra
      421 ayyppsqiaq lrpsprwtaq garphpfqnm pgairpaapr ppfstmrpas sqvprvmstq
      481 rvantstqtm gprpaaaata atpavrtvpq ykyaagvrnp qqhlnaqpqv tmqqpavhvq
      541 gqepltasml asappqeqkq mlgerlfpli qamhpslagk itgmlleidn sellhmlesp
      601 eslrskvdea vavlqahqak eaaqkavnsa tgvptv
//
LOCUS       NP_058753                114 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear transition protein 2 [Rattus norvegicus].
ACCESSION   NP_058753
VERSION     NP_058753.2
DBSOURCE    REFSEQ: accession NM_017057.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Barral,S., Morozumi,Y., Tanaka,H., Montellier,E., Govin,J., de
            Dieuleveult,M., Charbonnier,G., Coute,Y., Puthier,D., Buchou,T.,
            Boussouar,F., Urahama,T., Fenaille,F., Curtet,S., Hery,P.,
            Fernandez-Nunez,N., Shiota,H., Gerard,M., Rousseaux,S.,
            Kurumizaka,H. and Khochbin,S.
  TITLE     Histone Variant H2A.L.2 Guides Transition Protein-Dependent
            Protamine Assembly in Male Germ Cells
  JOURNAL   Mol Cell 66 (1), 89-101 (2017)
   PUBMED   28366643
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Pradeepa,M.M., Nikhil,G., Hari Kishore,A., Bharath,G.N., Kundu,T.K.
            and Rao,M.R.
  TITLE     Acetylation of transition protein 2 (TP2) by KAT3B (p300) alters
            its DNA condensation property and interaction with putative histone
            chaperone NPM3
  JOURNAL   J Biol Chem 284 (43), 29956-29967 (2009)
   PUBMED   19710011
  REMARK    GeneRIF: Acetylation of transition protein 2 (TP2) by KAT3B (p300)
            alters its DNA condensation property and interaction with putative
            histone chaperone NPM3.
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Kolthur-Seetharam,U., Pradeepa,M.M., Gupta,N., Narayanaswamy,R. and
            Rao,M.R.
  TITLE     Spatiotemporal organization of AT- and GC-rich DNA and their
            association with transition proteins TP1 and TP2 in rat condensing
            spermatids
  JOURNAL   J Histochem Cytochem 57 (10), 951-962 (2009)
   PUBMED   19506090
  REMARK    GeneRIF: TP1 and TP2 may have concerted functional roles during
            chromatin remodeling in mammalian spermiogenesis.
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Kleene,K.C. and Bagarova,J.
  TITLE     Comparative genomics reveals gene-specific and shared regulatory
            sequences in the spermatid-expressed mammalian Odf1, Prm1, Prm2,
            Tnp1, and Tnp2 genes
  JOURNAL   Genomics 92 (2), 101-106 (2008)
   PUBMED   18562159
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Pradeepa,M.M., Manjunatha,S., Sathish,V., Agrawal,S. and Rao,M.R.
  TITLE     Involvement of importin-4 in the transport of transition protein 2
            into the spermatid nucleus
  JOURNAL   Mol Cell Biol 28 (13), 4331-4341 (2008)
   PUBMED   17682055
  REMARK    GeneRIF: A detailed analysis to characterize the molecular
            components underlying the nuclear translocation of TP2, was carried
            out.
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Kundu,T.K. and Rao,M.R.
  TITLE     Characterization of the zinc-metalloprotein nature of rat
            spermatidal protein TP2
  JOURNAL   FEBS Lett 351 (1), 6-10 (1994)
   PUBMED   8076694
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Keime,S., Heitland,K., Kumm,S., Schlosser,M., Hroch,N., Holtz,W.
            and Engel,W.
  TITLE     Characterization of four genes encoding basic proteins of the
            porcine spermatid nucleus and close linkage of three of them
  JOURNAL   Biol Chem Hoppe Seyler 373 (5), 261-270 (1992)
   PUBMED   1627265
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Baskaran,R. and Rao,M.R.
  TITLE     Mammalian spermatid specific protein, TP2, is a zinc metalloprotein
            with two finger motifs
  JOURNAL   Biochem Biophys Res Commun 179 (3), 1491-1499 (1991)
   PUBMED   1930189
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Luerssen,H., Maier,W.M., Hoyer-Fender,S. and Engel,W.
  TITLE     The nucleotide sequence of rat transition protein 2 (TP2) cDNA
  JOURNAL   Nucleic Acids Res 17 (9), 3585 (1989)
   PUBMED   2726489
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Cole,K.D. and Kistler,W.S.
  TITLE     Nuclear transition protein 2 (TP2) of mammalian spermatids has a
            very basic carboxyl terminal domain
  JOURNAL   Biochem Biophys Res Commun 147 (1), 437-442 (1987)
   PUBMED   3307778
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078849.1.
            
            On Aug 8, 2004 this sequence version replaced NP_058753.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078849.1, X14776.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..114
                     /product="nuclear transition protein 2"
                     /note="haploid expressed, male germcell specific,
                     chromatin binding; TP2; TP-2"
                     /calculated_mol_wt=12707
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11101.2)"
     Region          1..110
                     /region_name="TP2"
                     /note="Nuclear transition protein 2; pfam01254"
                     /db_xref="CDD:426159"
     Region          87..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:10961985,
                     ECO:0000269|PubMed:17682055"
                     /note="propagated from UniProtKB/Swiss-Prot (P11101.2)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:11772016; propagated from
                     UniProtKB/Swiss-Prot (P11101.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:11772016; propagated from
                     UniProtKB/Swiss-Prot (P11101.2)"
     CDS             1..114
                     /gene="Tnp2"
                     /coded_by="NM_017057.2:55..399"
                     /db_xref="GeneID:24840"
                     /db_xref="RGD:3885"
ORIGIN      
        1 mdtkmqslpt thphphsssr pqshtnnqca cshhcrscsq aghpsssssp ssgpptkhpk
       61 tpmhsrysps rpshrgscpk nrktlegkvs krkavrrrkr thrakrrssg rryk
//
LOCUS       NP_062061                113 aa            linear   ROD 27-APR-2025
DEFINITION  beta-microseminoprotein precursor [Rattus norvegicus].
ACCESSION   NP_062061
VERSION     NP_062061.1
DBSOURCE    REFSEQ: accession NM_019188.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Bergstrom,S.H., Jaremo,H., Nilsson,M., Adamo,H.H. and Bergh,A.
  TITLE     Prostate tumors downregulate microseminoprotein-beta (MSMB) in the
            surrounding benign prostate epithelium and this response is
            associated with tumor aggressiveness
  JOURNAL   Prostate 78 (4), 257-265 (2018)
   PUBMED   29250809
  REMARK    GeneRIF: Aggressive prostate tumors suppress MSMB synthesis in the
            benign prostate and this could explain why serum levels of MSMB are
            decreased in prostate cancer patients.
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Imasato,Y., Onita,T., Moussa,M., Sakai,H., Chan,F.L.,
            Koropatnick,J., Chin,J.L. and Xuan,J.W.
  TITLE     Rodent PSP94 gene expression is more specific to the dorsolateral
            prostate and less sensitive to androgen ablation than probasin
  JOURNAL   Endocrinology 142 (5), 2138-2146 (2001)
   PUBMED   11316782
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Fernlund,P., Granberg,L.B. and Larsson,I.
  TITLE     Cloning of beta-microseminoprotein of the rat: a rapidly evolving
            mucosal surface protein
  JOURNAL   Arch Biochem Biophys 334 (1), 73-82 (1996)
   PUBMED   8837741
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U65486.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U65486.1, CB779813.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..113
                     /product="beta-microseminoprotein precursor"
                     /note="beta-microseminoprotein; PSP-94; prostate secretory
                     protein PSP94; prostate secreted seminal plasma protein;
                     prostate secretory protein of 94 amino acids"
                     /calculated_mol_wt=10738
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2029
     mat_peptide     21..113
                     /product="beta-microseminoprotein"
                     /calculated_mol_wt=10738
     Region          21..113
                     /region_name="PSP94"
                     /note="Beta-microseminoprotein (PSP-94); pfam05825"
                     /db_xref="CDD:283482"
     CDS             1..113
                     /gene="Msmb"
                     /gene_synonym="PSP94"
                     /coded_by="NM_019188.1:30..371"
                     /db_xref="GeneID:29311"
                     /db_xref="RGD:3113"
ORIGIN      
        1 mkarlgsllv latlvtasna acsiqrlkrl pneksdectd vdggkhvlnt ywqkncewcf
       61 cektaitcct ktlipvsydk krcqrqfhse nctysvvert npgktcpvng wti
//
LOCUS       NP_113784                806 aa            linear   ROD 27-APR-2025
DEFINITION  U4/U6.U5 tri-snRNP-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_113784
VERSION     NP_113784.1
DBSOURCE    REFSEQ: accession NM_031596.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Lemm,I., Girard,C., Kuhn,A.N., Watkins,N.J., Schneider,M.,
            Bordonne,R. and Luhrmann,R.
  TITLE     Ongoing U snRNP biogenesis is required for the integrity of Cajal
            bodies
  JOURNAL   Mol Biol Cell 17 (7), 3221-3231 (2006)
   PUBMED   16687569
REFERENCE   5  (residues 1 to 806)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   6  (residues 1 to 806)
  AUTHORS   Kikuchi,M., Nakao,M., Inoue,Y., Matsunaga,K., Shichijo,S.,
            Yamana,H. and Itoh,K.
  TITLE     Identification of a SART-1-derived peptide capable of inducing
            HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes
  JOURNAL   Int J Cancer 81 (3), 459-466 (1999)
   PUBMED   10209962
REFERENCE   7  (residues 1 to 806)
  AUTHORS   Gotoh,M., Shichijo,S., Hoshino,T., Imai,Y., Imaizumi,T., Inoue,Y.,
            Takasu,H., Yamaoka,T. and Itoh,K.
  TITLE     Sequence analysis of genes encoding rodent homologues of the human
            tumor-rejection antigen SART-1
  JOURNAL   Jpn J Cancer Res 89 (8), 849-854 (1998)
   PUBMED   9765622
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB014722.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB014722.1, BC083551.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..806
                     /product="U4/U6.U5 tri-snRNP-associated protein 1"
                     /note="SART-1; rSART-1; squamous cell carcinoma antigen
                     recognized by T cells 1; SART1, U4/U6.U5
                     tri-snRNP-associated protein 1"
                     /calculated_mol_wt=90908
     Region          1..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Region          118..137
                     /region_name="HIND"
                     /note="HIND motif; pfam19252"
                     /db_xref="CDD:466011"
     Region          165..759
                     /region_name="SART-1"
                     /note="SART-1 family; pfam03343"
                     /db_xref="CDD:460888"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z315; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Region          418..505
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Region          578..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43290; propagated from
                     UniProtKB/Swiss-Prot (Q5XIW8.1)"
     CDS             1..806
                     /gene="Sart1"
                     /coded_by="NM_031596.1:59..2479"
                     /db_xref="GeneID:29678"
                     /db_xref="RGD:61930"
ORIGIN      
        1 mgsskkhrge keaagttaaa gtggtteqpp rhrehkkhkh rssgggssgg errkrsrerg
       61 aergsgrrga eaearsgahg rersqaepse rrvkrekrde gyeaaasska ssgdasslsi
      121 eetnklrakl glkplevnav kkeagtkeep vaadvinpma lrqreelrek laaakekrll
      181 nqklgkiktl geddpwlddt aawiersrql qkekdlaekr aklleemdqe fgvstlveee
      241 feqrrqdlys ardlqgltve haidsfrege tvvltlkdkg vlqegedvlv nvnmvdkera
      301 dknvelrkkk pdylpyvede svddlaqqkp rsilakydee legerphsfr leqggmadgl
      361 rereleeirt klrlqaqsln tvgprlasey lspeemvtfk ktkrrvkkir kkekevimra
      421 ddllplgedq tqdgdfgsrl rgrgrrrvpe veeealedee kdpvaqppps ddtrvenmdi
      481 sdeedggalp sgppeleede aelelqkqle kgrrlrqlqq lqqlrdsgek vleivkkles
      541 rqrgweeeed perkgtivfn atsefcrtlg eiptyglagn reeqeelmdf erdeersang
      601 gsesdgeeni gwstvnldee kqhqdfsass ttildeepiv nrglaaalll cqnkgllett
      661 vqkvarvkap nkslpsavyc iedkmaiddk ysrreeyrgf tqdfkekdgy kpdvkieyvd
      721 etgrkltpke afrqlshrfh gkgsgkmkte rrmkkldeea llkkmsssdt plgtvallqe
      781 kqkaqktpyi vlsgsgksmn antitk
//
LOCUS       NP_036956                 88 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein C-I precursor [Rattus norvegicus].
ACCESSION   NP_036956
VERSION     NP_036956.1
DBSOURCE    REFSEQ: accession NM_012824.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Wang,X., Gong,Y., Deng,T., Zhang,L., Liao,X., Han,C., Yang,C.,
            Huang,J., Wang,Q., Song,X., Zhang,T., Yu,T., Zhu,G., Ye,X. and
            Peng,T.
  TITLE     Diagnostic and prognostic significance of mRNA expressions of
            apolipoprotein A and C family genes in hepatitis B virus-related
            hepatocellular carcinoma
  JOURNAL   J Cell Biochem 120 (10), 18246-18265 (2019)
   PUBMED   31211449
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Cohen,M., Yossef,R., Erez,T., Kugel,A., Welt,M., Karpasas,M.M.,
            Bones,J., Rudd,P.M., Taieb,J., Boissin,H., Harats,D., Noy,K.,
            Tekoah,Y., Lichtenstein,R.G., Rubin,E. and Porgador,A.
  TITLE     Serum apolipoproteins C-I and C-III are reduced in stomach cancer
            patients: results from MALDI-based peptidome and immuno-based
            clinical assays
  JOURNAL   PLoS One 6 (1), e14540 (2011)
   PUBMED   21267442
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Westerterp,M., Berbee,J.F., Delsing,D.J., Jong,M.C., Gijbels,M.J.,
            Dahlmans,V.E., Offerman,E.H., Romijn,J.A., Havekes,L.M. and
            Rensen,P.C.
  TITLE     Apolipoprotein C-I binds free fatty acids and reduces their
            intracellular esterification
  JOURNAL   J Lipid Res 48 (6), 1353-1361 (2007)
   PUBMED   17339654
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Masson,D., Pais de Barros,J.P., Zak,Z., Gautier,T., Le Guern,N.,
            Assem,M., Chisholm,J.W., Paterniti,J.R. Jr. and Lagrost,L.
  TITLE     Human apoA-I expression in CETP transgenic rats leads to lower
            levels of apoC-I in HDL and to magnification of CETP-mediated
            lipoprotein changes
  JOURNAL   J Lipid Res 47 (2), 356-365 (2006)
   PUBMED   16282639
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Ricci,F., Kern,S.E., Hruban,R.H. and Iacobuzio-Donahue,C.A.
  TITLE     Stromal responses to carcinomas of the pancreas: juxtatumoral gene
            expression conforms to the infiltrating pattern and not the
            biologic subtype
  JOURNAL   Cancer Biol Ther 4 (3), 302-307 (2005)
   PUBMED   15876873
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Shen,P. and Howlett,G.J.
  TITLE     Two coding regions closely linked to the rat apolipoprotein E gene:
            nucleotide sequences of rat apolipoprotein C-I and ECL cDNA
  JOURNAL   Arch Biochem Biophys 297 (2), 345-353 (1992)
   PUBMED   1379790
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Sehayek,E. and Eisenberg,S.
  TITLE     Mechanisms of inhibition by apolipoprotein C of apolipoprotein
            E-dependent cellular metabolism of human triglyceride-rich
            lipoproteins through the low density lipoprotein receptor pathway
  JOURNAL   J Biol Chem 266 (27), 18259-18267 (1991)
   PUBMED   1917954
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Poensgen,J.
  TITLE     Apolipoprotein C-1 inhibits the hydrolysis by phospholipase A2 of
            phospholipids in liposomes and cell membranes
  JOURNAL   Biochim Biophys Acta 1042 (2), 188-192 (1990)
   PUBMED   2302419
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Shen,P.Y. and Howlett,G.J.
  TITLE     Nucleotide sequence of cDNA for rat apolipoprotein C-I
  JOURNAL   Nucleic Acids Res 17 (15), 6405 (1989)
   PUBMED   2771655
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Kinnunen,P.K. and Ehnolm,C.
  TITLE     Effect of serum and C-apoproteins from very low density
            lipoproteins on human postheparin plasma hepatic lipase
  JOURNAL   FEBS Lett 65 (3), 354-357 (1976)
   PUBMED   182536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X15512.1 and BC098670.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Transcript variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X15512.1, CO806913.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..88
                     /product="apolipoprotein C-I precursor"
                     /note="apo-CI; apoC-I; liver regeneration-related protein
                     LRRG04; apolipoprotein C-I"
                     /calculated_mol_wt=7187
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2691
     mat_peptide     27..88
                     /product="apolipoprotein C-I"
                     /calculated_mol_wt=7187
     Region          27..87
                     /region_name="ApoC-I"
                     /note="Apolipoprotein C-I (ApoC-1); pfam04691"
                     /db_xref="CDD:428068"
     CDS             1..88
                     /gene="Apoc1"
                     /gene_synonym="ALPCI; Apo-CIB; ApoC-IB; LRRG04"
                     /coded_by="NM_012824.2:84..350"
                     /db_xref="GeneID:25292"
                     /db_xref="RGD:2134"
ORIGIN      
        1 mrlfialpvl ivvvamaleg papaqaapdf ssameslpdk lkefgntled karaaiehik
       61 qkeimiktrn wfsetlnkmk eklkttfa
//
LOCUS       NP_001019442             192 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF185 [Rattus norvegicus].
ACCESSION   NP_001019442 XP_573638
VERSION     NP_001019442.1
DBSOURCE    REFSEQ: accession NM_001024271.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Kaneko,M., Iwase,I., Yamasaki,Y., Takai,T., Wu,Y., Kanemoto,S.,
            Matsuhisa,K., Asada,R., Okuma,Y., Watanabe,T., Imaizumi,K. and
            Nomura,Y.
  TITLE     Genome-wide identification and gene expression profiling of
            ubiquitin ligases for endoplasmic reticulum protein degradation
  JOURNAL   Sci Rep 6, 30955 (2016)
   PUBMED   27485036
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   El Khouri,E., Le Pavec,G., Toledano,M.B. and Delaunay-Moisan,A.
  TITLE     RNF185 is a novel E3 ligase of endoplasmic reticulum-associated
            degradation (ERAD) that targets cystic fibrosis transmembrane
            conductance regulator (CFTR)
  JOURNAL   J Biol Chem 288 (43), 31177-31191 (2013)
   PUBMED   24019521
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC092655.1.
            
            On May 27, 2005 this sequence version replaced XP_573638.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092655.1, FN801244.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840111 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..192
                     /product="E3 ubiquitin-protein ligase RNF185"
                     /EC_number="2.3.2.27"
                     /note="RING-type E3 ubiquitin transferase RNF185"
                     /calculated_mol_wt=20362
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Y3.1)"
     Region          29..80
                     /region_name="Required for ubiquitin ligase activity and
                     protection against ER stress-induced cell death.
                     /evidence=ECO:0000250|UniProtKB:Q96GF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Y3.1)"
     Region          37..93
                     /region_name="RING-HC_RNF185"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 185 (RNF185) and similar proteins; cd16744"
                     /db_xref="CDD:438402"
     Region          90..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Y3.1)"
     Site            131..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Y3.1)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Y3.1)"
     CDS             1..192
                     /gene="Rnf185"
                     /coded_by="NM_001024271.1:153..731"
                     /db_xref="GeneID:360967"
                     /db_xref="RGD:1564777"
ORIGIN      
        1 maskgpsasa stenssaggp sgssngtges ggqdstfecn icldtakdav islcghlfcw
       61 pclhqwletr pnrqvcpvck agisrdkvip lygrgstgqq dprektpprp qgqrpepenr
      121 ggfqgfgfgd ggfqmsfgig afpfgifata fnindgrppp avpgtpqyvd eqflsrlflf
      181 valvimfwll ia
//
LOCUS       NP_598303                130 aa            linear   ROD 27-APR-2025
DEFINITION  glycoprotein hormone alpha-2 precursor [Rattus norvegicus].
ACCESSION   NP_598303
VERSION     NP_598303.1
DBSOURCE    REFSEQ: accession NM_133619.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Sun,S.C., Hsu,P.J., Wu,F.J., Li,S.H., Lu,C.H. and Luo,C.W.
  TITLE     Thyrostimulin, but not thyroid-stimulating hormone (TSH), acts as a
            paracrine regulator to activate the TSH receptor in mammalian ovary
  JOURNAL   J Biol Chem 285 (6), 3758-3765 (2010)
   PUBMED   19955180
  REMARK    GeneRIF: Data indicate that the presence of thyrostimulin in the
            ovary suggests that it may have a primitive function in
            reproduction when it activates ovarian TSHR.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Nagasaki,H., Wang,Z., Jackson,V.R., Lin,S., Nothacker,H.P. and
            Civelli,O.
  TITLE     Differential expression of the thyrostimulin subunits, glycoprotein
            alpha2 and beta5 in the rat pituitary
  JOURNAL   J Mol Endocrinol 37 (1), 39-50 (2006)
   PUBMED   16901922
  REMARK    GeneRIF: Results describe the differential expression of the
            thyrostimulin subunits, glycoprotein alpha2 and beta5 in the rat
            pituitary, and suggest that the thyrostimulin system is
            functionally different from the thyroid-stimulating hormone system.
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Li,C., Hirooka,Y., Habu,S., Takagi,J., Gotoh,M. and Nogimori,T.
  TITLE     Distribution of thyrostimulin in the rat: an immunohistochemical
            study
  JOURNAL   Endocr Regul 38 (4), 131-142 (2004)
   PUBMED   15841792
  REMARK    GeneRIF: Thyrostimulin immunoreactivity was visualized in the
            anterior pituitary, central nervous system, adrenal gland, stomach,
            duodenum, pancreas and testis; findings suggest that thyrostimulin
            is widely distributed [thyrostimulin]
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Hsu,S.Y., Nakabayashi,K. and Bhalla,A.
  TITLE     Evolution of glycoprotein hormone subunit genes in bilateral
            metazoa: identification of two novel human glycoprotein hormone
            subunit family genes, GPA2 and GPB5
  JOURNAL   Mol Endocrinol 16 (7), 1538-1551 (2002)
   PUBMED   12089349
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Nakabayashi,K., Matsumi,H., Bhalla,A., Bae,J., Mosselman,S.,
            Hsu,S.Y. and Hsueh,A.J.
  TITLE     Thyrostimulin, a heterodimer of two new human glycoprotein hormone
            subunits, activates the thyroid-stimulating hormone receptor
  JOURNAL   J Clin Invest 109 (11), 1445-1452 (2002)
   PUBMED   12045258
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF260741.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF260741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132308 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..130
                     /product="glycoprotein hormone alpha-2 precursor"
                     /note="glycoprotein-alpha 2; thyrostimulin subunit alpha;
                     glycoprotein hormone alpha 2; putative secreted protein
                     ZSIG51; cysteine knot protein"
                     /calculated_mol_wt=11892
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925Q4.1)"
                     /calculated_mol_wt=2326
     mat_peptide     23..130
                     /product="Glycoprotein hormone alpha-2.
                     /id=PRO_0000011674"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925Q4.1)"
                     /calculated_mol_wt=11892
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925Q4.1)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925Q4.1)"
     CDS             1..130
                     /gene="Gpha2"
                     /gene_synonym="Gpa2; Zsig51"
                     /coded_by="NM_133619.2:203..595"
                     /db_xref="GeneID:171158"
                     /db_xref="RGD:621748"
ORIGIN      
        1 mpmaprvllf cllglavteg hgleaavpip gchlhpfnvt vrsdrhgtcq gshvaqacvg
       61 hcessafpsr ysvlvasgyr hnitsvsqcc tisslkkvrv wlhcvgnqrg eleiftarac
      121 qcdmcrlsry
//
LOCUS       NP_071548               1300 aa            linear   ROD 27-APR-2025
DEFINITION  insulin receptor-related protein precursor [Rattus norvegicus].
ACCESSION   NP_071548 XP_001068054 XP_574972
VERSION     NP_071548.2
DBSOURCE    REFSEQ: accession NM_022212.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1300)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   2  (residues 1 to 1300)
  AUTHORS   Deyev,I.E., Sohet,F., Vassilenko,K.P., Serova,O.V., Popova,N.V.,
            Zozulya,S.A., Burova,E.B., Houillier,P., Rzhevsky,D.I.,
            Berchatova,A.A., Murashev,A.N., Chugunov,A.O., Efremov,R.G.,
            Nikol'sky,N.N., Bertelli,E., Eladari,D. and Petrenko,A.G.
  TITLE     Insulin receptor-related receptor as an extracellular alkali sensor
  JOURNAL   Cell Metab 13 (6), 679-689 (2011)
   PUBMED   21641549
REFERENCE   3  (residues 1 to 1300)
  AUTHORS   Vogel,R., Garten,A., Klammt,J., Barnikol-Oettler,A. and Kiess,W.
  TITLE     Activation of Erk1/2 phosphorylation but not of Akt/Pkb through an
            inducible CSF1R/IRR-receptor construct in INS-1E beta-cells
  JOURNAL   Arch Physiol Biochem 116 (3), 128-136 (2010)
   PUBMED   20536329
  REMARK    GeneRIF: the influence of a stimulatable IRR-tyrosine kinase on
            major IR/IGF1R signaling pathways and on proliferation and
            apoptosis of INS-1E beta-cells
REFERENCE   4  (residues 1 to 1300)
  AUTHORS   Nef,S., Verma-Kurvari,S., Merenmies,J., Vassalli,J.D.,
            Efstratiadis,A., Accili,D. and Parada,L.F.
  TITLE     Testis determination requires insulin receptor family function in
            mice
  JOURNAL   Nature 426 (6964), 291-295 (2003)
   PUBMED   14628051
REFERENCE   5  (residues 1 to 1300)
  AUTHORS   Itoh,N., Jobo,K., Tsujimoto,K., Ohta,M. and Kawasaki,T.
  TITLE     Two truncated forms of rat insulin receptor-related receptor
  JOURNAL   J Biol Chem 268 (24), 17983-17986 (1993)
   PUBMED   7688734
REFERENCE   6  (residues 1 to 1300)
  AUTHORS   Kurachi,H., Jobo,K., Ohta,M., Kawasaki,T. and Itoh,N.
  TITLE     A new member of the insulin receptor family, insulin
            receptor-related receptor, is expressed preferentially in the
            kidney
  JOURNAL   Biochem Biophys Res Commun 187 (2), 934-939 (1992)
   PUBMED   1530648
REFERENCE   7  (residues 1 to 1300)
  AUTHORS   Shier,P. and Watt,V.M.
  TITLE     Tissue-specific expression of the rat insulin receptor-related
            receptor gene
  JOURNAL   Mol Endocrinol 6 (5), 723-729 (1992)
   PUBMED   1603082
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473976.2.
            
            On or before Oct 23, 2008 this sequence version replaced
            XP_574972.1, XP_001068054.1, NP_071548.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1300
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1300
                     /product="insulin receptor-related protein precursor"
                     /EC_number="2.7.10.1"
                     /note="insulin receptor-related protein; IRR; IR-related
                     receptor"
                     /calculated_mol_wt=142357
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2508
     mat_peptide     24..1300
                     /product="Insulin receptor-related protein.
                     /id=PRO_0000016707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64716.3)"
                     /calculated_mol_wt=142357
     Region          47..158
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Region          173..326
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Region          346..461
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            492
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Region          494..600
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            order(589..590,592..593)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          605..>649
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            616
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            634
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            756
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Region          819..908
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            885
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            order(898..899,901..902)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            898
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            922..942
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64716.3)"
     Region          972..1248
                     /region_name="PTKc_InsR_like"
                     /note="Catalytic domain of Insulin Receptor-like Protein
                     Tyrosine Kinases; cd05032"
                     /db_xref="CDD:173625"
     Site            order(985,987..989,993,1011,1013,1060,1062,1066,1115,
                     1119..1120,1122,1133,1150..1152,1154..1155,1164,1166,1198)
                     /site_type="active"
                     /db_xref="CDD:173625"
     Site            order(985,987..989,993,1011,1013,1060,1062,1066,1120,1122,
                     1133)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173625"
     Site            order(1115,1119,1150..1152,1154..1155,1164,1166,1198)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173625"
     Site            1132..1157
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173625"
     Site            1145
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q64716.3)"
     Region          1270..1300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64716.3)"
     CDS             1..1300
                     /gene="Insrr"
                     /gene_synonym="Sirr"
                     /coded_by="NM_022212.2:399..4301"
                     /db_xref="GeneID:60663"
                     /db_xref="RGD:67399"
ORIGIN      
        1 mavpalwpwg vyllmsllsl gscldtlevc psldirsevt elrrlencsv veghlqillm
       61 faatgedfrg lsfprltqvt dylllfrvyg leslrdlfpn lavirgarlf lgyaliifem
      121 phlrdiglps lgavlrgavr veknqelchl stidwgllqp apganhivgn klgeecadvc
      181 pgvlgaagep cvrttfgght dyrcwtsshc qrvcpcprgl actvggecch seclggcsqp
      241 edpracvacr hlyfqgvclp tcppgtyqye swrcvtaelc ghlrevpgha tafgiyegsc
      301 laqcppgftr ngssifchkc eglcpkeckv gtktidsvqa tqdlvgcthv egslilnlrq
      361 gynlepelqr nlglvetitg flkikhsfal vtlgffknlk lirgdsmvdg nytlyvldnq
      421 nlqqlgswva agltipvgki yfafnprlcl ehiyqleevt gtrgrqskae inprtngdra
      481 acqtrtlrfv fnlteedril lrweryeple ardllsfivy ykespfqnat ehvgpdacgt
      541 qswnlldvel plsrtqepgv tlaplkpwtq yavfvraitl ttaedsphqg aqspivylrt
      601 lpaaptvpqd vistsnsssh llvrwkppvq rngnityylv lwqrlaedgd lyindychrg
      661 lrlptsshdt rfdredpale aepeqgccpc qhsppgqalp aleaqevtfq kkfenflhha
      721 itipkapwkv tsinknpqrd serhrretgl lrlgknnsdf eihedkvpre ravlsglrhf
      781 teyridihac nhaahtvgcs aatfvfartm phreadgipg kvvwkavgks svilhwlepp
      841 dpnglilkye ikyrrlgeea tvlcvsrlry akvggvhlal lppgnysakv ratslagngs
      901 wtdgvafyit gpeeedtggl rilltvtpvg fmllvmlaal gffyskkrns tlytsvnpey
      961 fsashmyvpd ewevpreqia iirelgqgsf gmvyeglarg leageestpv alktvnelas
     1021 arerveflke asvmkafkch hvvrllgvvs qgqptlvime lmtrgdlksh lrslrpeaen
     1081 npglpqpals dmiqmageia dgmaylaakk fvhrdlaarn cmvsqdftvk igdfgmtrdv
     1141 yetdyyrkgg kgllpvrwma peslkdgift thsdvwsfgv vlweivtlae qpyqglsneq
     1201 vlkfvmdggv leeqedcpiq lqelmrrcwq htprlrptfv hildriqdel rpsfrlcsfy
     1261 yspecqrgqa sllpteaepd spptlngasd ygppngdpgh
//
LOCUS       NP_036714                347 aa            linear   ROD 27-APR-2025
DEFINITION  haptoglobin precursor [Rattus norvegicus].
ACCESSION   NP_036714
VERSION     NP_036714.2
DBSOURCE    REFSEQ: accession NM_012582.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Ding,F., Sun,K., Sun,N., Jiang,Q., Cao,M. and Wu,Z.
  TITLE     iTRAQ-based proteomics reveals SOD2 as a potential salivary
            biomarker in liver cancer
  JOURNAL   Int J Biol Markers 34 (3), 221-231 (2019)
   PUBMED   31041878
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Yang,Y., Kimura-Ohba,S., Thompson,J.F., Salayandia,V.M., Cosse,M.,
            Raz,L., Jalal,F.Y. and Rosenberg,G.A.
  TITLE     Vascular tight junction disruption and angiogenesis in
            spontaneously hypertensive rat with neuroinflammatory white matter
            injury
  JOURNAL   Neurobiol Dis 114, 95-110 (2018)
   PUBMED   29486300
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Heawchaiyaphum,C., Pientong,C., Phusingha,P., Vatanasapt,P.,
            Promthet,S., Daduang,J., Teeramatwanich,W., Kongyingyoes,B.,
            Chuerduangphui,J. and Ekalaksananan,T.
  TITLE     Peroxiredoxin-2 and zinc-alpha-2-glycoprotein as potentially
            combined novel salivary biomarkers for early detection of oral
            squamous cell carcinoma using proteomic approaches
  JOURNAL   J Proteomics 173, 52-61 (2018)
   PUBMED   29199150
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Irwin,D.C., Baek,J.H., Hassell,K., Nuss,R., Eigenberger,P.,
            Lisk,C., Loomis,Z., Maltzahn,J., Stenmark,K.R., Nozik-Grayck,E. and
            Buehler,P.W.
  TITLE     Hemoglobin-induced lung vascular oxidation, inflammation, and
            remodeling contribute to the progression of hypoxic pulmonary
            hypertension and is attenuated in rats with repeated-dose
            haptoglobin administration
  JOURNAL   Free Radic Biol Med 82, 50-62 (2015)
   PUBMED   25656991
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Jubelirer,S.J.
  TITLE     Primary pulmonary hypertension. Its association with
            microangiopathic hemolytic anemia and thrombocytopenia
  JOURNAL   Arch Intern Med 151 (6), 1221-1223 (1991)
   PUBMED   2043024
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Marinkovic,S. and Baumann,H.
  TITLE     Structure, hormonal regulation, and identification of the
            interleukin-6- and dexamethasone-responsive element of the rat
            haptoglobin gene
  JOURNAL   Mol Cell Biol 10 (4), 1573-1583 (1990)
   PUBMED   2320005
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Frohlander,N. and Johnson,O.
  TITLE     Haptoglobin groups in acute myocardial infarction
  JOURNAL   Hum Hered 39 (6), 345-350 (1989)
   PUBMED   2613263
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Dash,S. and Das,K.C.
  TITLE     Serum haptoglobin concentrations in 'pure' iron-deficiency anemia
  JOURNAL   Clin Chem 24 (5), 839-840 (1978)
   PUBMED   647925
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Snyder,S., Coodley,E.L., Durham,B.C. and Pennock,R.S.
  TITLE     Serum glycoproteins in coronary artery disease
  JOURNAL   Circulation 56 (3), 359-362 (1977)
   PUBMED   884791
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089816.1.
            
            On Feb 20, 2005 this sequence version replaced NP_036714.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089816.1, AF476963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..347
                     /product="haptoglobin precursor"
                     /note="liver regeneration-related protein LRRG173;
                     zonulin"
                     /calculated_mol_wt=36622
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1959
     mat_peptide     19..347
                     /product="Haptoglobin. /id=PRO_0000028483"
                     /note="propagated from UniProtKB/Swiss-Prot (P06866.3)"
                     /calculated_mol_wt=36622
     Region          33..87
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(43,53)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          103..343
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            103
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(143,187,296)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06866.3)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06866.3)"
     Region          259..264
                     /region_name="Interaction with CD163.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P06866.3)"
     Site            order(290,317,319)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..347
                     /gene="Hp"
                     /gene_synonym="Ba1-647"
                     /coded_by="NM_012582.2:14..1057"
                     /db_xref="GeneID:24464"
                     /db_xref="RGD:2825"
ORIGIN      
        1 mralgavvtl llwgqlfave lgndatdied dscpkppeia ngyvehlvry rcrqfyklqt
       61 egdgiytlns ekqwvnpaag dklpkceavc gkpkhpvdqv qriiggsmda kgsfpwqakm
      121 isrhglttga tlisdqwllt taqnlflnhs enatakdiap tltlyvgknq lveiekvvlh
      181 persvvdigl iklkqkvlvt ekvmpiclps kdyvapgrmg yvsgwgrnvn frfterlkyv
      241 mlpvadqekc elhyekstvp ekkgavspvg vqpilnkhtf cagltkyeed tcygdagsaf
      301 avhdteedtw yaagilsfdk scavaeygvy vratdlkdwv qetmakn
//
LOCUS       NP_695218                476 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 45 [Rattus norvegicus].
ACCESSION   NP_695218
VERSION     NP_695218.1
DBSOURCE    REFSEQ: accession NM_153306.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Tamada,H., Sakashita,E., Shimazaki,K., Ueno,E., Hamamoto,T.,
            Kagawa,Y. and Endo,H.
  TITLE     cDNA cloning and characterization of Drb1, a new member of RRM-type
            neural RNA-binding protein
  JOURNAL   Biochem Biophys Res Commun 297 (1), 96-104 (2002)
   PUBMED   12220514
  REMARK    GeneRIF: a new member of RRM-type neural RNA-binding protein
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB036990.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB036990.1, SRR8487231.120643.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..476
                     /product="RNA-binding protein 45"
                     /note="developmentally-regulated RNA-binding protein 1"
                     /calculated_mol_wt=53300
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFD1.1)"
     Region          23..104
                     /region_name="RRM1_RBM45"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12366"
                     /db_xref="CDD:409801"
     Region          120..193
                     /region_name="RRM2_RBM45"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12367"
                     /db_xref="CDD:409802"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8CFD1.1)"
     Region          248..320
                     /region_name="RRM3_RBM45"
                     /note="RNA recognition motif 3 (RRM3) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12368"
                     /db_xref="CDD:409803"
     Region          393..460
                     /region_name="RRM4_RBM45"
                     /note="RNA recognition motif 4 (RRM4) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12369"
                     /db_xref="CDD:409804"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IUH3; propagated from
                     UniProtKB/Swiss-Prot (Q8CFD1.1)"
     CDS             1..476
                     /gene="Rbm45"
                     /gene_synonym="Drb1"
                     /coded_by="NM_153306.1:51..1481"
                     /db_xref="GeneID:266631"
                     /db_xref="RGD:628862"
ORIGIN      
        1 mddagssggs ggfrpgvdsl deppnsrifl viskytsesv lrehfspfgd iqdiwvvrdk
       61 htkeskgiaf vkfarssqac rameemhgqc lgpndtkpik vfiaqsrssg shrdvedeel
      121 trifvmipks yteedlrekf kvygdieycs viknkvtges kglgyvrylk psqaaqaien
      181 cdrsfralla epknkvlesp eqdyyssvrq etlgheprgn lfpfvgeqqs efstfdknds
      241 rgqeaiskrl svasrvpfte eqlfsifdiv pgleycevhr dpylnyghgv vqyfnvasav
      301 yaqyklhgfq yppgnriavs flddgsnsad lirkmatqmv aaqlastvws npshqqflqf
      361 ggsagsqvpq iqtdvvlpsc rkkappetpv kerlfivfnp hplpldvled ifcrfgnlie
      421 vylvsgknvg yvkyadrmsa ndaittlhgk ilngvrlkvm ladsprevsk krqrty
//
LOCUS       NP_001094046             323 aa            linear   ROD 27-APR-2025
DEFINITION  aldo-keto reductase family 1, member C19 [Rattus norvegicus].
ACCESSION   NP_001094046 XP_001062695 XP_225544
VERSION     NP_001094046.1
DBSOURCE    REFSEQ: accession NM_001100576.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Satoshi,Endo., Matsunaga,T. and Hara,A.
  TITLE     Characterization of aldo-keto reductase 1C subfamily members
            encoded in two rat genes (akr1c19 and RGD1564865). Relationship to
            9-hydroxyprostaglandin dehydrogenase
  JOURNAL   Arch Biochem Biophys 700, 108755 (2021)
   PUBMED   33482148
  REMARK    GeneRIF: Characterization of aldo-keto reductase 1C subfamily
            members encoded in two rat genes (akr1c19 and RGD1564865).
            Relationship to 9-hydroxyprostaglandin dehydrogenase.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Pawlowski,J., Huizinga,M. and Penning,T.M.
  TITLE     Isolation and partial characterization of a full-length cDNA clone
            for 3 alpha-hydroxysteroid dehydrogenase: a potential target enzyme
            for nonsteroidal anti-inflammatory drugs
  JOURNAL   Agents Actions 34 (1-2), 289-293 (1991)
   PUBMED   1793046
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On or before Aug 4, 2007 this sequence version replaced
            XP_225544.3, XP_001062695.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.61348.1,
                                           SRR26360172.423556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.2"
     Protein         1..323
                     /product="aldo-keto reductase family 1, member C19"
                     /note="NAD-preferring dehydrogenase for
                     17beta-hydroxysteroids and 9-hydroxyprostaglandins"
                     /calculated_mol_wt=36816
     Region          6..308
                     /region_name="AKR_AKR1C1-35"
                     /note="AKR1C family of aldo-keto reductase (AKR); cd19108"
                     /db_xref="CDD:381334"
     Site            order(22..24,50,54..55,84,86,117..118,120,128..129,
                     166..167,190,216..222,224,227,236,253,268..273,276,
                     279..280,306,308)
                     /site_type="active"
                     /db_xref="CDD:381334"
     Site            order(50,55,84,117)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381334"
     CDS             1..323
                     /gene="Akr1c19"
                     /gene_synonym="RAKi; RGD1562954"
                     /coded_by="NM_001100576.1:151..1122"
                     /db_xref="GeneID:307096"
                     /db_xref="RGD:1562954"
ORIGIN      
        1 msskqqlvkl ndghfipalg fgtykpeevp enkpleaihl aveagfrhid tayvyqtenh
       61 vgqaikskia agivkredif ittklwctfh rpemvlssle kslknlqldy vdlyiihypm
      121 qmksgedmfp edengktlfd tvdlcatwea mekckdagla ksigvsnfnr rqlekilnkp
      181 glkykpvcnq vechlylnqs kllnycksrd ivlvaycalg sqrpkrwvdp sspvllndpv
      241 lcdvakkhqr ssaqialryq lqrgnvvlaq sykeneiken iqvfefelps edmkildsld
      301 rnlryapapf gqghpeypfs def
//
LOCUS       NP_001121537             106 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL42 [Rattus norvegicus].
ACCESSION   NP_001121537 XP_001068688 XP_214958
VERSION     NP_001121537.1
DBSOURCE    REFSEQ: accession NM_001128065.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Gallagher,M.J., Chan,Y.L., Lin,A. and Wool,I.G.
  TITLE     Primary structure of rat ribosomal protein L36a
  JOURNAL   DNA 7 (4), 269-273 (1988)
   PUBMED   3396452
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Tsurugi,K., Collatz,E., Todokoro,K. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of 60 S ribosomal subunit proteins L3, L6, L7',
            L8, L10, L15, L17, L18, L19, L23', L25, L27', L28, L29, L31, L32,
            L34, L35, L36, L36', and L37'
  JOURNAL   J Biol Chem 252 (11), 3961-3969 (1977)
   PUBMED   863909
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473969.2.
            
            On or before Jun 3, 2008 this sequence version replaced
            XP_001068688.1, XP_214958.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF287837.1, FQ211253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..106
                     /product="large ribosomal subunit protein eL42"
                     /note="60S ribosomal protein L36a; 60S ribosomal protein
                     L44"
                     /calculated_mol_wt=12310
     Region          1..86
                     /region_name="PTZ00157"
                     /note="60S ribosomal protein L36a; Provisional"
                     /db_xref="CDD:240296"
     Region          34..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P83883.2)"
     CDS             1..106
                     /gene="Rpl36a"
                     /coded_by="NM_001128065.1:51..371"
                     /db_xref="GeneID:292964"
                     /db_xref="RGD:1306640"
ORIGIN      
        1 mvnvpktrrt fckkcgkhqp hkvtqykkgk dslyaqgkrr ydrkqsgygg qtkpifrkka
       61 kttkkivlrl ecvepncrsk rmlaikrckh felggdkkrk gqviqf
//
LOCUS       NP_037040                278 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor ligand superfamily member 6 [Rattus
            norvegicus].
ACCESSION   NP_037040
VERSION     NP_037040.1
DBSOURCE    REFSEQ: accession NM_012908.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Yang,S., Gao,J., Chen,M., Sun,Y., Qiao,X., Mao,H., Guo,L., Yu,Y.
            and Yang,D.
  TITLE     Let-7a promotes periodontal bone regeneration of bone marrow
            mesenchymal stem cell aggregates via the Fas/FasL-autophagy pathway
  JOURNAL   J Cell Mol Med 27 (24), 4056-4068 (2023)
   PUBMED   37855249
  REMARK    GeneRIF: Let-7a promotes periodontal bone regeneration of bone
            marrow mesenchymal stem cell aggregates via the Fas/FasL-autophagy
            pathway.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Liu,R., Peng,Z., Zhang,Y., Li,R. and Wang,Y.
  TITLE     Upregulation of miR-128 inhibits neuronal cell apoptosis following
            spinal cord injury via FasL downregulation by repressing ULK1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34296305
  REMARK    GeneRIF: Upregulation of miR128 inhibits neuronal cell apoptosis
            following spinal cord injury via FasL downregulation by repressing
            ULK1.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Tang,H., Zhang,S., Huang,C., Li,K., Zhao,Q. and Li,X.
  TITLE     MiR-448-5p/VEGFA Axis Protects Cardiomyocytes from Hypoxia Through
            Regulating the FAS/FAS-L Signaling Pathway
  JOURNAL   Int Heart J 62 (3), 647-657 (2021)
   PUBMED   33994507
  REMARK    GeneRIF: MiR-448-5p/VEGFA Axis Protects Cardiomyocytes from Hypoxia
            Through Regulating the FAS/FAS-L Signaling Pathway.
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Tang,M., Pan,H., Zheng,Z., Guo,Y., Peng,J., Yang,J., Luo,Y., He,J.,
            Yan,S., Wang,P., Zhang,Y. and Zhou,Y.
  TITLE     Prostaglandin E1 protects cardiomyocytes against
            hypoxia-reperfusion induced injury via the miR-21-5p/FASLG axis
  JOURNAL   Biosci Rep 39 (12) (2019)
   PUBMED   31782491
  REMARK    GeneRIF: Prostaglandin E1 protects cardiomyocytes against
            hypoxia-reperfusion induced injury via the miR-21-5p/FASLG axis.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Du,X., Hong,L., Sun,L., Sang,H., Qian,A., Li,W., Zhuang,H.,
            Liang,H., Song,D., Li,C., Wang,W. and Li,X.
  TITLE     miR-21 induces endothelial progenitor cells proliferation and
            angiogenesis via targeting FASLG and is a potential prognostic
            marker in deep venous thrombosis
  JOURNAL   J Transl Med 17 (1), 270 (2019)
   PUBMED   31416448
  REMARK    GeneRIF: FASLG was a target of miR-21 and revealed that FASLG
            knockdown inhibited function of endothelial progenitor cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Gratas,C., Tohma,Y., Barnas,C., Taniere,P., Hainaut,P. and
            Ohgaki,H.
  TITLE     Up-regulation of Fas (APO-1/CD95) ligand and down-regulation of Fas
            expression in human esophageal cancer
  JOURNAL   Cancer Res 58 (10), 2057-2062 (1998)
   PUBMED   9605741
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Kitagawa,M., Yamaguchi,S., Takahashi,M., Tanizawa,T., Hirokawa,K.
            and Kamiyama,R.
  TITLE     Localization of Fas and Fas ligand in bone marrow cells
            demonstrating myelodysplasia
  JOURNAL   Leukemia 12 (4), 486-492 (1998)
   PUBMED   9557605
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Lee,S., Chong,S.Y., Lee,J.W., Kim,S.C., Min,Y.H., Hahn,J.S. and
            Ko,Y.W.
  TITLE     Difference in the expression of Fas/Fas-ligand and the lymphocyte
            subset reconstitution according to the occurrence of acute GVHD
  JOURNAL   Bone Marrow Transplant 20 (10), 883-888 (1997)
   PUBMED   9404931
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Takahashi,T., Tanaka,M., Brannan,C.I., Jenkins,N.A., Copeland,N.G.,
            Suda,T. and Nagata,S.
  TITLE     Generalized lymphoproliferative disease in mice, caused by a point
            mutation in the Fas ligand
  JOURNAL   Cell 76 (6), 969-976 (1994)
   PUBMED   7511063
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Suda,T., Takahashi,T., Golstein,P. and Nagata,S.
  TITLE     Molecular cloning and expression of the Fas ligand, a novel member
            of the tumor necrosis factor family
  JOURNAL   Cell 75 (6), 1169-1178 (1993)
   PUBMED   7505205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U03470.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U03470.1, LN874405.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984043 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..278
                     /product="tumor necrosis factor ligand superfamily member
                     6"
                     /note="CD95L protein; CD95 ligand; Tumor necrosis factor
                     (ligand) superfamily, member 6 (apoptosis (APO-1) antigen
                     ligand 1) (Fas antigen ligand); Apoptosis (APO-1) antigen
                     ligand 1 (Fas antigen ligand); tumor necrosis factor
                     ligand 1a; Fas ligand (TNF superfamily, member 6)"
                     /calculated_mol_wt=31009
     Region          26..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36940.1)"
     Site            78..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36940.1)"
     Site            78..79
                     /site_type="cleavage"
                     /note="Cleavage, by SPPL2A. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P36940.1)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P36940.1)"
     Region          125..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36940.1)"
     Site            126..127
                     /site_type="cleavage"
                     /note="Cleavage, by ADAM10. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P36940.1)"
     Site            order(145,187,189,241,246,272,276)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Region          157..278
                     /region_name="TNF"
                     /note="TNF(Tumour Necrosis Factor) family; pfam00229"
                     /db_xref="CDD:425540"
     Site            order(160..161,166,205,212,217)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P36940.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P36940.1)"
     CDS             1..278
                     /gene="Faslg"
                     /gene_synonym="Apt1Lg1; CD95-L; Fasl; Tnfsf6; Tnlg1a"
                     /coded_by="NM_012908.1:74..910"
                     /db_xref="GeneID:25385"
                     /db_xref="RGD:3880"
ORIGIN      
        1 mqqpvnypcp qiywvdssat spwappgsvf scpssgprgp gqrrpppppp ppsplpppsq
       61 ppplpplspl kkkdnielwl pviffmvlva lvgmglgmyq lfhlqkelae lreftnhslr
      121 vssfekqian pstpsetkkp rsvahltgnp rsrsiplewe dtygtalisg vkykkgglvi
      181 neaglyfvys kvyfrgqscn sqplshkvym rnfkypgdlv lmeekklnyc ttgqiwahss
      241 ylgavfnltv adhlyvnisq lslinfeesk tffglykl
//
LOCUS       NP_037013                317 aa            linear   ROD 27-APR-2025
DEFINITION  osteopontin precursor [Rattus norvegicus].
ACCESSION   NP_037013
VERSION     NP_037013.2
DBSOURCE    REFSEQ: accession NM_012881.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Xie,H., Lu,F., Li,X., Wang,E., Mo,J. and Liang,W.
  TITLE     Silencing of secreted phosphoprotein 1 attenuates sciatic nerve
            injury-induced neuropathic pain: Regulating extracellular
            signal-regulated kinase and neuroinflammatory signaling pathways
  JOURNAL   Immun Inflamm Dis 12 (2), e1132 (2024)
   PUBMED   38415922
  REMARK    GeneRIF: Silencing of secreted phosphoprotein 1 attenuates sciatic
            nerve injury-induced neuropathic pain: Regulating extracellular
            signal-regulated kinase and neuroinflammatory signaling pathways.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Yu,G., Wang,X., Luo,J., Su,X., Tao,H., Wen,Z. and Guan,H.
  TITLE     [Role of SPP1 in acute kidney injury induced by renal
            ischemia-reperfusion in rats]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 43 (11), 1947-1954 (2023)
   PUBMED   38081614
  REMARK    GeneRIF: [Role of SPP1 in acute kidney injury induced by renal
            ischemia-reperfusion in rats].
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Ji,W., Sun,Z., Yang,Y., Hu,M., Zhang,Q., Fu,J., Chen,J., Huang,Y.
            and Cheng,Y.
  TITLE     Downregulation of RUNX1-Activated Osteopontin Facilitates Burn
            Wound Healing by Activating the MAPK Pathways
  JOURNAL   J Burn Care Res 44 (6), 1371-1381 (2023)
   PUBMED   36913234
  REMARK    GeneRIF: Downregulation of RUNX1-Activated Osteopontin Facilitates
            Burn Wound Healing by Activating the MAPK Pathways.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Chang,C.J., Lai,Y.J., Tung,Y.C., Wu,L.S., Hsu,L.A., Tseng,C.N.,
            Chang,G.J., Yang,K.C. and Yeh,Y.H.
  TITLE     Osteopontin mediation of disturbed flow-induced endothelial
            mesenchymal transition through CD44 is a novel mechanism of
            neointimal hyperplasia in arteriovenous fistulae for hemodialysis
            access
  JOURNAL   Kidney Int 103 (4), 702-718 (2023)
   PUBMED   36646166
  REMARK    GeneRIF: Osteopontin mediation of disturbed flow-induced
            endothelial mesenchymal transition through CD44 is a novel
            mechanism of neointimal hyperplasia in arteriovenous fistulae for
            hemodialysis access.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Zhang,R., Wang,M., Lu,H., Wang,J., Han,X., Liu,Z., Li,L., Li,M.,
            Tian,X., Chen,S., Zhang,G., Xiong,Y. and Li,J.
  TITLE     A miR-340/SPP1 axis inhibits the activation and proliferation of
            hepatic stellate cells by inhibiting the TGF-beta1/Smads pathway
  JOURNAL   Adv Clin Exp Med 32 (4), 469-479 (2023)
   PUBMED   36413180
  REMARK    GeneRIF: A miR-340/SPP1 axis inhibits the activation and
            proliferation of hepatic stellate cells by inhibiting the
            TGF-beta1/Smads pathway.
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Singh,K., Mukherjee,A.B., De Vouge,M.W. and Mukherjee,B.B.
  TITLE     Differential processing of osteopontin transcripts in rat kidney-
            and osteoblast-derived cell lines
  JOURNAL   J Biol Chem 267 (33), 23847-23851 (1992)
   PUBMED   1429723
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Senger,D.R., Perruzzi,C.A., Papadopoulos,A. and Tenen,D.G.
  TITLE     Purification of a human milk protein closely similar to
            tumor-secreted phosphoproteins and osteopontin
  JOURNAL   Biochim Biophys Acta 996 (1-2), 43-48 (1989)
   PUBMED   2736258
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Senger,D.R., Perruzzi,C.A., Gracey,C.F., Papadopoulos,A. and
            Tenen,D.G.
  TITLE     Secreted phosphoproteins associated with neoplastic transformation:
            close homology with plasma proteins cleaved during blood
            coagulation
  JOURNAL   Cancer Res 48 (20), 5770-5774 (1988)
   PUBMED   3167835
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Prince,C.W., Oosawa,T., Butler,W.T., Tomana,M., Bhown,A.S.,
            Bhown,M. and Schrohenloher,R.E.
  TITLE     Isolation, characterization, and biosynthesis of a phosphorylated
            glycoprotein from rat bone
  JOURNAL   J Biol Chem 262 (6), 2900-2907 (1987)
   PUBMED   3469201
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Oldberg,A., Franzen,A. and Heinegard,D.
  TITLE     Cloning and sequence analysis of rat bone sialoprotein
            (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence
  JOURNAL   Proc Natl Acad Sci U S A 83 (23), 8819-8823 (1986)
   PUBMED   3024151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV102664.1, BC078874.1 and BU759036.1.
            
            On Apr 12, 2007 this sequence version replaced NP_037013.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078874.1, FQ222192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16093045
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..317
                     /product="osteopontin precursor"
                     /note="osteopontin; SPP-1; bone sialoprotein 1;
                     Sialoprotein (osteopontin); osteopontin-like"
                     /calculated_mol_wt=33248
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1733
     mat_peptide     17..317
                     /product="Osteopontin. /id=PRO_0000020325"
                     /note="propagated from UniProtKB/Swiss-Prot (P08721.2)"
                     /calculated_mol_wt=33248
     Region          22..317
                     /region_name="Osteopontin"
                     /note="pfam00865"
                     /db_xref="CDD:459969"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Region          43..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08721.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            123
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            132
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            137
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Region          144..146
                     /region_name="Cell attachment site"
                     /note="propagated from UniProtKB/Swiss-Prot (P08721.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P31096; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            219
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            311
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10451; propagated from
                     UniProtKB/Swiss-Prot (P08721.2)"
     CDS             1..317
                     /gene="Spp1"
                     /gene_synonym="OSP"
                     /coded_by="NM_012881.2:107..1060"
                     /db_xref="GeneID:25353"
                     /db_xref="RGD:3752"
ORIGIN      
        1 mrlavvcfcl fglasclpvk vaefgsseek ahyskhsdav atwlkpdpsq kqnllapqns
       61 vsseetddfk qetlpsnsne shdhmddddd ddddgdhaes edsvnsdesd eshhsdesde
      121 sftastqadv ltpiaptvdv pdgrgdslay glrsksrsfp vsdeqypdat dedltsrmks
      181 qesdeaikvi pvaqrlsvps dqdsngktsh essqldepsv ethsleqske ykqrashest
      241 eqsdaidsae kpdaidsaer sdaidsqass kaslehqshe fhshedklvl dpkskeddry
      301 lkfrishele ssssevn
//
LOCUS       NP_476555                683 aa            linear   ROD 27-APR-2025
DEFINITION  synaptic vesicle glycoprotein 2B [Rattus norvegicus].
ACCESSION   NP_476555
VERSION     NP_476555.1
DBSOURCE    REFSEQ: accession NM_057207.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Fronczak,K.M., Li,Y., Henchir,J., Dixon,C.E. and Carlson,S.W.
  TITLE     Reductions in Synaptic Vesicle Glycoprotein 2 Isoforms in the
            Cortex and Hippocampus in a Rat Model of Traumatic Brain Injury
  JOURNAL   Mol Neurobiol 58 (11), 6006-6019 (2021)
   PUBMED   34435329
  REMARK    GeneRIF: Reductions in Synaptic Vesicle Glycoprotein 2 Isoforms in
            the Cortex and Hippocampus in a Rat Model of Traumatic Brain
            Injury.
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Tejero,R., Lopez-Manzaneda,M., Arumugam,S. and Tabares,L.
  TITLE     Synaptotagmin-2, and -1, linked to neurotransmission impairment and
            vulnerability in Spinal Muscular Atrophy
  JOURNAL   Hum Mol Genet 25 (21), 4703-4716 (2016)
   PUBMED   28173138
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Wilhelm,B.G., Mandad,S., Truckenbrodt,S., Krohnert,K., Schafer,C.,
            Rammner,B., Koo,S.J., Classen,G.A., Krauss,M., Haucke,V., Urlaub,H.
            and Rizzoli,S.O.
  TITLE     Composition of isolated synaptic boutons reveals the amounts of
            vesicle trafficking proteins
  JOURNAL   Science 344 (6187), 1023-1028 (2014)
   PUBMED   24876496
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Boyken,J., Gronborg,M., Riedel,D., Urlaub,H., Jahn,R. and Chua,J.J.
  TITLE     Molecular profiling of synaptic vesicle docking sites reveals novel
            proteins but few differences between glutamatergic and GABAergic
            synapses
  JOURNAL   Neuron 78 (2), 285-297 (2013)
   PUBMED   23622064
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Yang,S.Y., Jeon,S.K., Kang,J.H., Yoo,H.I., Kim,Y.S., Moon,J.S.,
            Kim,M.S., Koh,J.T., Oh,W.M. and Kim,S.H.
  TITLE     Synaptic vesicle protein 2b is expressed temporospatially in
            (pre)odontoblasts in developing molars
  JOURNAL   Eur J Oral Sci 120 (6), 505-512 (2012)
   PUBMED   23167466
  REMARK    GeneRIF: For the first time, synaptic vesicle protein (SV) 2b, an
            important transmembrane transporter of Ca2+-stimulated vesicle
            exocytosis, was identified as a differentially expressed molecule
            localized in fully differentiated odontoblasts and
            pre-odontoblasts.
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Pyle,R.A., Schivell,A.E., Hidaka,H. and Bajjalieh,S.M.
  TITLE     Phosphorylation of synaptic vesicle protein 2 modulates binding to
            synaptotagmin
  JOURNAL   J Biol Chem 275 (22), 17195-17200 (2000)
   PUBMED   10747945
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Janz,R. and Sudhof,T.C.
  TITLE     SV2C is a synaptic vesicle protein with an unusually restricted
            localization: anatomy of a synaptic vesicle protein family
  JOURNAL   Neuroscience 94 (4), 1279-1290 (1999)
   PUBMED   10625067
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Janz,R., Hofmann,K. and Sudhof,T.C.
  TITLE     SVOP, an evolutionarily conserved synaptic vesicle protein,
            suggests novel transport functions of synaptic vesicles
  JOURNAL   J Neurosci 18 (22), 9269-9281 (1998)
   PUBMED   9801366
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Hayashi,M., Yamamoto,A., Yatsushiro,S., Yamada,H., Futai,M.,
            Yamaguchi,A. and Moriyama,Y.
  TITLE     Synaptic vesicle protein SV2B, but not SV2A, is predominantly
            expressed and associated with microvesicles in rat pinealocytes
  JOURNAL   J Neurochem 71 (1), 356-365 (1998)
   PUBMED   9648885
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Bajjalieh,S.M., Peterson,K., Linial,M. and Scheller,R.H.
  TITLE     Brain contains two forms of synaptic vesicle protein 2
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2150-2154 (1993)
   PUBMED   7681585
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L10362.1, CB609053.1, CO402345.1, DV721065.1, BG671769.1,
            BF285601.1 and AI716529.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L10362.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..683
                     /product="synaptic vesicle glycoprotein 2B"
                     /note="synaptic vesicle protein 2B"
                     /calculated_mol_wt=77372
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Region          8..683
                     /region_name="synapt_SV2"
                     /note="synaptic vesicle protein SV2; TIGR01299"
                     /db_xref="CDD:130366"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            206..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG39; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            441
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            516
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63564.1)"
     Site            536..556
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            566..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            593..613
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            627..649
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     Site            654..672
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63564.1)"
     CDS             1..683
                     /gene="Sv2b"
                     /coded_by="NM_057207.3:440..2491"
                     /db_xref="GeneID:117556"
                     /db_xref="RGD:619716"
ORIGIN      
        1 mddyryrdny egyapndgyy rgneqnpeed aqsdvteghd eedeiyegey qgiphpddvk
       61 skqtkmapsr adglrgqadl maermedeeq lahqyetiid ecghgrfqwt lffvlvlalm
      121 adgvevfvvs falpsaekdm clssskkgml glivylgmma gafilgglad klgrkkvlsm
      181 slainasfas lssfvqgyga flfcrlisgi giggslpivf ayfseflsre krgehlswlg
      241 ifwmtggiya samawsiiph ygwgfsmgtn yhfhswrvfv ivcalpatvs mvalkfmpes
      301 prfllemgkh deawmilkqv hdtnmrakgt pekvftvshi ktpkqmdefi eiqsstgtwy
      361 qrwlvrfmti fkqvwdnaly cvmgpyrmnt lilavvwftm alsyygltvw fpdmiryfqd
      421 eeykskmkvf fgehvhgati nftmenqihq hgklvndkfi kmyfkhvlfe dtffdkcyfe
      481 dvtstdtyfk nctiesttfy ntdlykhkfi dcrfinstfl eqkegchmdf eedndfliyl
      541 vsflgslsvl pgniisallm drigrlkmig gsmlisavcc fflffgnses amigwqclfc
      601 gtsiaawnal dvitvelypt nqratafgil nglcklgail gntifasfvg itkvvpilla
      661 aaslvggglv alrlpetreq vlm
//
LOCUS       NP_001099181             872 aa            linear   ROD 27-APR-2025
DEFINITION  metabotropic glutamate receptor 2 precursor [Rattus norvegicus].
ACCESSION   NP_001099181 XP_001073809 XP_343471
VERSION     NP_001099181.1
DBSOURCE    REFSEQ: accession NM_001105711.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   De Gasperi,R., Gama Sosa,M.A., Perez Garcia,G., Perez,G.M.,
            Pryor,D., Morrison,C.L., Lind,R., Abutarboush,R., Kawoos,U.,
            Statz,J.K., Patterson,J., Hof,P.R., Zhu,C.W., Ahlers,S.T.,
            Cook,D.G. and Elder,G.A.
  TITLE     Metabotropic Glutamate Receptor 2 Expression Is Chronically
            Elevated in Male Rats With Post-Traumatic Stress Disorder Related
            Behavioral Traits Following Repetitive Low-Level Blast Exposure
  JOURNAL   J Neurotrauma 41 (5-6), 714-733 (2024)
   PUBMED   37917117
  REMARK    GeneRIF: Metabotropic Glutamate Receptor 2 Expression Is
            Chronically Elevated in Male Rats With Post-Traumatic Stress
            Disorder Related Behavioral Traits Following Repetitive Low-Level
            Blast Exposure.
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Bodzeta,A., Berger,F. and MacGillavry,H.D.
  TITLE     Subsynaptic mobility of presynaptic mGluR types is differentially
            regulated by intra- and extracellular interactions
  JOURNAL   Mol Biol Cell 33 (8), ar66 (2022)
   PUBMED   35511883
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Khodagholi,F., Maleki,A., Motamedi,F., Mousavi,M.A., Rafiei,S. and
            Moslemi,M.
  TITLE     Oxytocin Prevents the Development of 3-NP-Induced Anxiety and
            Depression in Male and Female Rats: Possible Interaction of OXTR
            and mGluR2
  JOURNAL   Cell Mol Neurobiol 42 (4), 1105-1123 (2022)
   PUBMED   33201416
  REMARK    GeneRIF: Oxytocin Prevents the Development of 3-NP-Induced Anxiety
            and Depression in Male and Female Rats: Possible Interaction of
            OXTR and mGluR2.
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Elhussiny,M.E.A., Carini,G., Mingardi,J., Tornese,P., Sala,N.,
            Bono,F., Fiorentini,C., La Via,L., Popoli,M., Musazzi,L. and
            Barbon,A.
  TITLE     Modulation by chronic stress and ketamine of ionotropic AMPA/NMDA
            and metabotropic glutamate receptors in the rat hippocampus
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 104, 110033 (2021)
   PUBMED   32640261
  REMARK    GeneRIF: Modulation by chronic stress and ketamine of ionotropic
            AMPA/NMDA and metabotropic glutamate receptors in the rat
            hippocampus.
REFERENCE   5  (residues 1 to 872)
  AUTHORS   Sweeten,B.L.W., Adkins,A.M., Wellman,L.L. and Sanford,L.D.
  TITLE     Group II metabotropic glutamate receptor activation in the
            basolateral amygdala mediates individual differences in
            stress-induced changes in rapid eye movement sleep
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 104, 110014 (2021)
   PUBMED   32534177
  REMARK    GeneRIF: Group II metabotropic glutamate receptor activation in the
            basolateral amygdala mediates individual differences in
            stress-induced changes in rapid eye movement sleep.
REFERENCE   6  (residues 1 to 872)
  AUTHORS   Lujan,R., Roberts,J.D., Shigemoto,R., Ohishi,H. and Somogyi,P.
  TITLE     Differential plasma membrane distribution of metabotropic glutamate
            receptors mGluR1 alpha, mGluR2 and mGluR5, relative to
            neurotransmitter release sites
  JOURNAL   J Chem Neuroanat 13 (4), 219-241 (1997)
   PUBMED   9412905
REFERENCE   7  (residues 1 to 872)
  AUTHORS   Yokoi,M., Kobayashi,K., Manabe,T., Takahashi,T., Sakaguchi,I.,
            Katsuura,G., Shigemoto,R., Ohishi,H., Nomura,S., Nakamura,K.,
            Nakao,K., Katsuki,M. and Nakanishi,S.
  TITLE     Impairment of hippocampal mossy fiber LTD in mice lacking mGluR2
  JOURNAL   Science 273 (5275), 645-647 (1996)
   PUBMED   8662555
REFERENCE   8  (residues 1 to 872)
  AUTHORS   Chavis,P., Shinozaki,H., Bockaert,J. and Fagni,L.
  TITLE     The metabotropic glutamate receptor types 2/3 inhibit L-type
            calcium channels via a pertussis toxin-sensitive G-protein in
            cultured cerebellar granule cells
  JOURNAL   J Neurosci 14 (11 Pt 2), 7067-7076 (1994)
   PUBMED   7965099
REFERENCE   9  (residues 1 to 872)
  AUTHORS   Guariso,G., Fait,P., Rini,A. and Zancan,L.
  TITLE     [Liver transplant in childhood: our experience]
  JOURNAL   Pediatr Med Chir 14 (6), 603-607 (1992)
   PUBMED   1298933
REFERENCE   10 (residues 1 to 872)
  AUTHORS   Tanabe,Y., Masu,M., Ishii,T., Shigemoto,R. and Nakanishi,S.
  TITLE     A family of metabotropic glutamate receptors
  JOURNAL   Neuron 8 (1), 169-179 (1992)
   PUBMED   1309649
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473954.2.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001073809.1, XP_343471.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M92075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..872
                     /product="metabotropic glutamate receptor 2 precursor"
                     /note="metabotropic glutamate receptor 2; mGluR2;
                     glutamate receptor, metabotropic 2"
                     /calculated_mol_wt=93875
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1917
     mat_peptide     19..872
                     /product="Metabotropic glutamate receptor 2.
                     /id=PRO_0000012926"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
                     /calculated_mol_wt=93875
     Region          26..480
                     /region_name="PBP1_mGluR_groupII"
                     /note="ligand binding domain of the group II metabotropic
                     glutamate receptor; cd06375"
                     /db_xref="CDD:380598"
     Site            order(57,61,144..145,166..168,216,295,377)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380598"
     Site            order(96,99,150,153,176,240)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380598"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q14416; propagated from
                     UniProtKB/Swiss-Prot (P31421.1)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q14416; propagated from
                     UniProtKB/Swiss-Prot (P31421.1)"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31421.1)"
     Site            402
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31421.1)"
     Region          496..546
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Site            547
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31421.1)"
     Region          566..819
                     /region_name="7tmC_mGluR2"
                     /note="metabotropic glutamate receptor 2 in group 2,
                     member of the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15447"
                     /db_xref="CDD:320563"
     Region          566..591
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320563"
     Site            568..590
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Site            order(569,572..573,576..577,579..580,614,618,621..622,630,
                     634)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320563"
     Region          603..624
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320563"
     Site            605..625
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Site            order(623,635..636,639..640,643,723,728,731..732,735,769,
                     772..773,776,780,790..791,794,797,801)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320563"
     Region          633..657
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320563"
     Site            637..655
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Region          677..685
                     /region_name="Important for interaction with HTR2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Region          679..699
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320563"
     Site            680..700
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Region          724..750
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320563"
     Site            726..747
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Region          758..781
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320563"
     Site            761..783
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     Region          788..813
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320563"
     Site            794..819
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31421.1)"
     CDS             1..872
                     /gene="Grm2"
                     /gene_synonym="mGlu2"
                     /coded_by="NM_001105711.1:199..2817"
                     /db_xref="GeneID:24415"
                     /db_xref="RGD:2743"
ORIGIN      
        1 mesllgflal lllwgavaeg pakkvltleg dlvlgglfpv hqkggpaeec gpvnehrgiq
       61 rleamlfald rinrdphllp gvrlgahild scskdthale qaldfvrasl srgadgsrhi
      121 cpdgsyaths daptavtgvi ggsysdvsiq vanllrlfqi pqisyastsa klsdksrydy
      181 fartvppdff qakamaeilr ffnwtyvstv asegdygetg ieafeleara rnicvatsek
      241 vgramsraaf egvvrallqk psarvavlft rsedarella atqrlnasft wvasdgwgal
      301 esvvagsera aegaitiela sypisdfasy fqsldpwnns rnpwfrefwe erfhcsfrqr
      361 dcaahslrav pfeqeskimf vvnavyamah alhnmhralc pntthlcdam rpvngrrlyk
      421 dfvlnvkfda pfrpadtdde vrfdrfgdgi gryniftylr agsgryryqk vgywaegltl
      481 dtsfipwasp sagplpasrc sepclqnevk svqpgevccw lcipcqpyey rldeftcadc
      541 glgywpnasl tgcfelpqey irwgdawavg pvtiaclgal atlfvlgvfv rhnatpvvka
      601 sgrelcyill ggvflcycmt fvfiakpsta vctlrrlglg tafsvcysal ltktnriari
      661 fggaregaqr prfispasqv aiclalisgq llivaawlvv eapgtgketa perrevvtlr
      721 cnhrdasmlg slaynvllia lctlyafktr kcpenfneak figftmyttc iiwlaflpif
      781 yvtssdyrvq tttmcvsvsl sgsvvlgclf apklhiilfq pqknvvshra ptsrfgsaap
      841 rasanlgqgs gsqfvptvcn grevvdstts sl
//
LOCUS       NP_001094463             563 aa            linear   ROD 27-APR-2025
DEFINITION  sperm-tail PG-rich repeat-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001094463 XP_001060952
VERSION     NP_001094463.1
DBSOURCE    REFSEQ: accession NM_001100993.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128777.1.
            
            On Aug 13, 2007 this sequence version replaced XP_001060952.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..563
                     /product="sperm-tail PG-rich repeat-containing protein 2"
                     /note="uncharacterized protein C4orf37 homolog"
                     /calculated_mol_wt=63293
     Region          21..34
                     /region_name="STPGR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          63..73
                     /region_name="STPGR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          97..107
                     /region_name="STPGR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          131..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          200..219
                     /region_name="STPGR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          250..263
                     /region_name="STPGR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          292..321
                     /region_name="STPGR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          334..353
                     /region_name="STPGR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          423..438
                     /region_name="STPGR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          473..483
                     /region_name="STPGR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     Region          507..518
                     /region_name="STPGR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5R9.1)"
     CDS             1..563
                     /gene="Stpg2"
                     /coded_by="NM_001100993.1:209..1900"
                     /db_xref="GeneID:499719"
                     /db_xref="RGD:1591946"
ORIGIN      
        1 mydraprwld lanrgsteeh vgpgtyqvpf pkqqatgcya pflslsskkd ayvvssdpgk
       61 avpgpahynv sqaqykikgg rtlqnrekrf kklisdgpgp asydcpylgt lcirirqkic
      121 rkpavsrsld ipsipssgks hgyhlneddt imrrtppssd ktmgpayynp qfdypkaslk
      181 ykgvnfgiat grqellkysg pgpghydiiq krklryenin ikrdqehycy syvprlyeei
      241 alqeekkgvp gpgkyniksq fdhiksmsti vdassllffp eterfepiks stpapgtyne
      301 trtafkvpkk rsglfspfgq raarftedyk ahelpgpgfy distnivkaq vkkphlkkkm
      361 ktgfgssvpr alfavqekaf agpgpsdyqv vrgihdelpn lmnkyaafls reerttpvqe
      421 mslpapgcyd vqksydmsqv qhnympprss vakqrhssfl saaprclgki sdgpgpatyn
      481 pilmksgaii sfvkaprrfe efqdkfspgp ttyelspffr hsllkrtynv tlpcsaslnr
      541 ehaghavqkt rqkyqrerfk hpn
//
LOCUS       NP_001004200             423 aa            linear   ROD 27-APR-2025
DEFINITION  COP9 signalosome complex subunit 3 [Rattus norvegicus].
ACCESSION   NP_001004200 XP_213326
VERSION     NP_001004200.1
DBSOURCE    REFSEQ: accession NM_001004200.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Sharon,M., Mao,H., Boeri Erba,E., Stephens,E., Zheng,N. and
            Robinson,C.V.
  TITLE     Symmetrical modularity of the COP9 signalosome complex suggests its
            multifunctionality
  JOURNAL   Structure 17 (1), 31-40 (2009)
   PUBMED   19141280
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,J., Walz,K., Nakamura,H., Carattini-Rivera,S., Zhao,Q.,
            Vogel,H., Wei,N., Justice,M.J., Bradley,A. and Lupski,J.R.
  TITLE     COP9 signalosome subunit 3 is essential for maintenance of cell
            proliferation in the mouse embryonic epiblast
  JOURNAL   Mol Cell Biol 23 (19), 6798-6808 (2003)
   PUBMED   12972600
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079143.1.
            
            On Sep 10, 2004 this sequence version replaced XP_213326.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079143.1, FQ228882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..423
                     /product="COP9 signalosome complex subunit 3"
                     /note="SGN3; signalosome subunit 3; COP9 (constitutive
                     photomorphogenic) homolog, subunit 3"
                     /calculated_mol_wt=47728
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9UNS2; propagated from
                     UniProtKB/Swiss-Prot (Q68FW9.1)"
     Region          259..362
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Region          402..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FW9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FW9.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FW9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UNS2; propagated from
                     UniProtKB/Swiss-Prot (Q68FW9.1)"
     CDS             1..423
                     /gene="Cops3"
                     /coded_by="NM_001004200.1:45..1316"
                     /db_xref="GeneID:287367"
                     /db_xref="RGD:1303002"
ORIGIN      
        1 masaleqfvn svrqlsaqgq mtqlcelink sgellaknls hldtvlgald vqehslgvla
       61 vlfvkfsmps vpdfetlfsq vqlfistcng ehiryatdtf aglchqltna lverkqplrg
      121 igilkqaidk mqmntnqlts vhadlcqlcl lakcfkpalp yldvdmmdic kengaydakh
      181 flcyyyyggm iytglknfer alyfyeqait tpamavshim lesykkyilv slillgkvqq
      241 lpkytsqivg rfikplsnay helaqvystn npselrnlvn khsetftrdn nmglvkqcls
      301 slykkniqrl tktfltlslq dmasrvqlsg pqeaekyvlh miedgeifas inqkdgmvsf
      361 hdnpekynnp amlhnidqem lkcielderl kamdqeitvn pqfvqksmgs qeddsgnkps
      421 sys
//
LOCUS       NP_001028878             802 aa            linear   ROD 27-APR-2025
DEFINITION  aldehyde dehydrogenase family 16 member A1 [Rattus norvegicus].
ACCESSION   NP_001028878 XP_341855
VERSION     NP_001028878.1
DBSOURCE    REFSEQ: accession NM_001033706.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC101860.1.
            
            On Sep 25, 2005 this sequence version replaced XP_341855.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..802
                     /product="aldehyde dehydrogenase family 16 member A1"
                     /note="aldehyde dehydrogenase 16A1"
                     /calculated_mol_wt=85284
     Region          19..491
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(172..176,184,199,201..202,248..251,254,257..258,
                     272..274,305,398,400,426,464)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143395"
     Site            order(176,272,302,305)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143395"
     Region          513..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T1L0.1)"
     Region          525..>765
                     /region_name="AdhE"
                     /note="Acyl-CoA reductase or other NAD-dependent aldehyde
                     dehydrogenase [Lipid transport and metabolism]; COG1012"
                     /db_xref="CDD:440636"
     CDS             1..802
                     /gene="Aldh16a1"
                     /coded_by="NM_001033706.1:58..2466"
                     /db_xref="GeneID:361571"
                     /db_xref="RGD:1566295"
ORIGIN      
        1 maatriqpst reifttleyg pvpeshacal awldthnrll ghyvngmwlk pehrnpapcq
       61 dpitgenlas clqaeaedis aaveaaritf ktwsqlpgta rgqhltrlak viqkhqrllw
      121 tleslvtgra vrevrdgdip laqqllhyha lqahaqdsal adweplgvig lilptsfsfl
      181 dmmwrvcpal amgctvvalv ppsfptplll aqlagelgsf pgilnvvcgp vslgpvlasq
      241 pgvqkvafcg aveegralrq tlagrgatlg lalgteslll ltdsadvdsa vegvvdavws
      301 drslgglrll iqesvwdeam krlqarmaqi rsgkgldgav dmgargaaar dlaqsfvdea
      361 qsqggqvfqa gdmpsnspff sptlvsglpp aapcaqaevp wpvvmaspfr tvkealalan
      421 gtprggsasv wserlgqale lgyglqvgtv winahglrdp avptggckes gsswhggpdg
      481 lyeylqllgt pyresflces lnydtfglav ssslpsgpet gpspappygl fvrgrfqspg
      541 tqssrpikds sgkvssyvae ggakdirgav eaahqaapgw gaqspraras llwalaaale
      601 rrkqvlaaql erhgaaptva etevelsvrr lqtwatrvqd qgqtlqvtgl rgpvlrlrep
      661 lgvlavvcpd ewpmlafvsl lapalahgna vvlvpsgscp llaleacqdi aalfpaglvn
      721 vvtgdrdhlt rclalhqdvq amwyfgsaqg sqfvewasag nlkpvwvnrd fprawdvevq
      781 gseqelslha artkalwlpm gd
//
LOCUS       NP_446431                179 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylation factor-like protein 5A [Rattus norvegicus].
ACCESSION   NP_446431
VERSION     NP_446431.1
DBSOURCE    REFSEQ: accession NM_053979.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Rosa-Ferreira,C., Christis,C., Torres,I.L. and Munro,S.
  TITLE     The small G protein Arl5 contributes to endosome-to-Golgi traffic
            by aiding the recruitment of the GARP complex to the Golgi
  JOURNAL   Biol Open 4 (4), 474-481 (2015)
   PUBMED   25795912
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Breiner,M., Schurmann,A., Becker,W. and Joost,H.G.
  TITLE     Cloning of a novel member (ARL5) of the ARF-family of Ras-related
            GTPases
  JOURNAL   Biochim Biophys Acta 1308 (1), 1-6 (1996)
   PUBMED   8765741
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097294.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097294.1, X78604.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..179
                     /product="ADP-ribosylation factor-like protein 5A"
                     /note="ADP-ribosylation factor-like 5; ADP-ribosylation
                     factor-like 5A; ADP-ribosylation factor like GTPase 5A"
                     /calculated_mol_wt=20583
     Region          3..175
                     /region_name="Arl5_Arl8"
                     /note="Arf-like 5 (Arl5) and 8 (Arl8) GTPases; cd04153"
                     /db_xref="CDD:133353"
     Site            23..30
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133353"
     Site            order(25..31,125..126,128,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133353"
     Site            order(25..26,30,34,46..53,75,80)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133353"
     Site            35..50
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133353"
     Site            order(47..51,56,66,70,76,78..80)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133353"
     Site            47
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133353"
     Site            order(48..55,65,76,79..80)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133353"
     Site            order(51..57,60..65)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:133353"
     Site            66..83
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133353"
     Site            66..69
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133353"
     Site            125..128
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133353"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133353"
     CDS             1..179
                     /gene="Arl5a"
                     /gene_synonym="Arl5"
                     /coded_by="NM_053979.2:192..731"
                     /db_xref="GeneID:117050"
                     /db_xref="RGD:621327"
ORIGIN      
        1 mgilftriwr lfnhqehkvi ivgldnagkt tilyqfsmne vvhtsptigs nveeivvnnt
       61 rflmwdiggq eslrsswnty ytntefvivv vdstdreris vtreelykml ahedlrkagl
      121 lifankqdvk ecmtvaeisq flkltsikdh qwhiqaccal tgeglcqgle wmmsrlkir
//
LOCUS       NP_113863                911 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-actinin-4 [Rattus norvegicus].
ACCESSION   NP_113863 XP_346542
VERSION     NP_113863.2
DBSOURCE    REFSEQ: accession NM_031675.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Ge,H., Yu,A., Chen,J., Yuan,J., Yin,Y., Duanmu,W., Tan,L., Yang,Y.,
            Lan,C., Chen,W., Feng,H. and Hu,R.
  TITLE     Poly-L-ornithine enhances migration of neural stem/progenitor cells
            via promoting alpha-Actinin 4 binding to actin filaments
  JOURNAL   Sci Rep 6, 37681 (2016)
   PUBMED   27874083
  REMARK    GeneRIF: Polyornithine activates alpha-Actinins 4 (ACTN4), which is
            firstly certified to be expessed in neural stem/progenitor cells,
            to promote filopodia formation and therefore enhances NSPCs
            migration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Sun,Y., Jaldin-Fincati,J., Liu,Z., Bilan,P.J. and Klip,A.
  TITLE     A complex of Rab13 with MICAL-L2 and alpha-actinin-4 is essential
            for insulin-dependent GLUT4 exocytosis
  JOURNAL   Mol Biol Cell 27 (1), 75-89 (2016)
   PUBMED   26538022
  REMARK    GeneRIF: Findings suggest that MICAL-L2 is an effector of
            insulin-activated Rab13, which links to GLUT4 through ACTN4,
            localizing GLUT4 vesicles at the muscle cell periphery to enable
            their fusion with the membrane.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Kalinowska,M., Chavez,A.E., Lutzu,S., Castillo,P.E., Bukauskas,F.F.
            and Francesconi,A.
  TITLE     Actinin-4 Governs Dendritic Spine Dynamics and Promotes Their
            Remodeling by Metabotropic Glutamate Receptors
  JOURNAL   J Biol Chem 290 (26), 15909-15920 (2015)
   PUBMED   25944910
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Ehrlicher,A.J., Krishnan,R., Guo,M., Bidan,C.M., Weitz,D.A. and
            Pollak,M.R.
  TITLE     Alpha-actinin binding kinetics modulate cellular dynamics and force
            generation
  JOURNAL   Proc Natl Acad Sci U S A 112 (21), 6619-6624 (2015)
   PUBMED   25918384
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Zhao,X., Hsu,K.S., Lim,J.H., Bruggeman,L.A. and Kao,H.Y.
  TITLE     alpha-Actinin 4 potentiates nuclear factor
            kappa-light-chain-enhancer of activated B-cell (NF-kappaB) activity
            in podocytes independent of its cytoplasmic actin binding function
  JOURNAL   J Biol Chem 290 (1), 338-349 (2015)
   PUBMED   25411248
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Honda,K., Yamada,T., Endo,R., Ino,Y., Gotoh,M., Tsuda,H.,
            Yamada,Y., Chiba,H. and Hirohashi,S.
  TITLE     Actinin-4, a novel actin-bundling protein associated with cell
            motility and cancer invasion
  JOURNAL   J Cell Biol 140 (6), 1383-1393 (1998)
   PUBMED   9508771
  REMARK    Erratum:[J Cell Biol 1998 Oct 5;143(1):following 276]
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Geisert,E.E. Jr., Yang,L. and Irwin,M.H.
  TITLE     Astrocyte growth, reactivity, and the target of the
            antiproliferative antibody, TAPA
  JOURNAL   J Neurosci 16 (17), 5478-5487 (1996)
   PUBMED   8757260
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Irwin,M.H. and Geisert,E.E. Jr.
  TITLE     The upregulation of a glial cell surface antigen at the astrocytic
            scar in the rat
  JOURNAL   Neurosci Lett 154 (1-2), 57-60 (1993)
   PUBMED   8361649
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Geisert,E.E. Jr., Murphy,T.P., Irwin,M.H. and Larjava,H.
  TITLE     A novel cell adhesion molecule, G-CAM, found on cultured rat glia
  JOURNAL   Neurosci Lett 133 (2), 262-266 (1991)
   PUBMED   1816505
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Poliakov,L.E., Malinskii,D.M. and Kubakin,V.I.
  TITLE     [Complex evaluation of the health status indicators of military
            personnel]
  JOURNAL   Voen Med Zh (11), 15-20 (1978)
   PUBMED   734924
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB805703.1, BC061788.1, BQ206143.1 and AI070095.1.
            
            On Oct 12, 2005 this sequence version replaced NP_113863.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061788.1, AY724534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..911
                     /product="alpha-actinin-4"
                     /note="non-muscle alpha-actinin 4; F-actin cross-linking
                     protein"
                     /calculated_mol_wt=104784
     Region          1..269
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          12..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          12..26
                     /region_name="Interaction with VCL.
                     /evidence=ECO:0000250|UniProtKB:O43707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P12814; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          40..61
                     /region_name="Interaction with VCL.
                     /evidence=ECO:0000250|UniProtKB:O43707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          47..151
                     /region_name="CH_ACTN_rpt1"
                     /note="first calponin homology (CH) domain found in the
                     alpha-actinin family; cd21214"
                     /db_xref="CDD:409063"
     Site            order(52,56,100,104..106,109..110,125..133,141,143..144,
                     147..148,150..151)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409063"
     Site            order(67,69,93..95)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409063"
     Region          84..88
                     /region_name="LXXLL motif.
                     /evidence=ECO:0000250|UniProtKB:O43707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          108..126
                     /region_name="Interaction with VCL.
                     /evidence=ECO:0000250|UniProtKB:O43707"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43707; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          155..269
                     /region_name="CH_ACTN_rpt2"
                     /note="second calponin homology (CH) domain found in the
                     alpha-actinin family; cd21216"
                     /db_xref="CDD:409065"
     Site            order(165,169,216..218,221..222,237..245,256,258..259,
                     262..263,265..266)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409065"
     Region          177..192
                     /region_name="Polyphosphoinositide (PIP2)-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            214
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P12814; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O43707; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          293..403
                     /region_name="Spectrin 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          296..517
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            404..409
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          413..518
                     /region_name="Spectrin 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          414..640
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            519..524
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          528..639
                     /region_name="Spectrin 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          532..754
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            592
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43707; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            625
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43707; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            640..645
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          649..752
                     /region_name="Spectrin 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12814; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          736..911
                     /region_name="Mediates interaction with MICALL2.
                     /evidence=ECO:0000250|UniProtKB:P57780"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          759..>868
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            779
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P57780; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Region          841..907
                     /region_name="EFhand_Ca_insen"
                     /note="Ca2+ insensitive EF hand; pfam08726"
                     /db_xref="CDD:430177"
     Site            859
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P57780; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1P2; propagated from
                     UniProtKB/Swiss-Prot (Q9QXQ0.2)"
     CDS             1..911
                     /gene="Actn4"
                     /coded_by="NM_031675.2:109..2844"
                     /db_xref="GeneID:63836"
                     /db_xref="RGD:61816"
ORIGIN      
        1 mvdyhaanqa yqygpssggn gtgggggmgd ymaqeddwdr dllldpawek qqrktftawc
       61 nshlrkagtq ienidedfrd glklmlllev isgerlpkpe rgkmrvhkin nvnkaldfia
      121 skgvklvsig aeeivdgnak mtlgmiwtii lrfaiqdisv eetsakegll lwcqrktapy
      181 knvnvqnfhi swkdglafna lihrhrpeli eydklrkddp vtnlnnafev aekyldipkm
      241 ldaedivnta rpdekaimty vssfyhafsg aqkaetaanr ickvlavnqe nehlmedyer
      301 lasdllewir rtipwledrv pqktiqemqq kledfrdyrr vhkppkvqek cqleinfntl
      361 qtklrlsnrp afmpsegrmv sdinngwqhl eqaekgyeew llneirrler ldhlaekfrq
      421 kasiheawtd gkeamlkhrd yetatlsdik alirkheafe sdlaahqdrv eqiaaiaqel
      481 neldyydshn vntrcqkicd qwdnlgslth srrealekte kqletidqlh leyakraapf
      541 nnwmesamed lqdmfivhti eeieglisah dqfkstlpda drereailai hkeaqriaes
      601 nhiklsgsnp ytsvtpqiin skwekvqqlv pkrdhallee qskqqsnehl rrqfasqanm
      661 vgpwiqtkme eigrisiemn gtledqlshl kqyersivdy kpnldlleqq hqliqealif
      721 dnkhtnytme hlrvgweqll ttiartinev enqiltrdak gisqeqmqef rasfnhfdkd
      781 hggalgpeef kaclislgyd vendrqgdae fnrimsvvdp nhsglvtfqa fidfmsrett
      841 dtdtadqvia sfkvlagdkn fitaeelrre lppdqaeyci armapyqgpd aapgaldyks
      901 fstalygesd l
//
LOCUS       NP_542944                189 aa            linear   ROD 27-APR-2025
DEFINITION  GTPase NRas [Rattus norvegicus].
ACCESSION   NP_542944 XP_346632
VERSION     NP_542944.1
DBSOURCE    REFSEQ: accession NM_080766.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Nakagawa,R., Muroyama,R., Saeki,C., Oikawa,T., Kaise,Y., Koike,K.,
            Arai,J., Nakano,M., Matsubara,Y., Takano,K., Hirata,Y., Saruta,M.,
            Zeniya,M. and Kato,N.
  TITLE     CD4+ T cells from patients with primary biliary cholangitis show T
            cell activation and differentially expressed T-cell receptor
            repertoires
  JOURNAL   Hepatol Res 49 (6), 653-662 (2019)
   PUBMED   30690835
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dietrich,P., Gaza,A., Wormser,L., Fritz,V., Hellerbrand,C. and
            Bosserhoff,A.K.
  TITLE     Neuroblastoma RAS Viral Oncogene Homolog (NRAS) Is a Novel
            Prognostic Marker and Contributes to Sorafenib Resistance in
            Hepatocellular Carcinoma
  JOURNAL   Neoplasia 21 (3), 257-268 (2019)
   PUBMED   30685691
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Yin,C., Zhu,B., Zhang,T., Liu,T., Chen,S., Liu,Y., Li,X., Miao,X.,
            Li,S., Mi,X., Zhang,J., Li,L., Wei,G., Xu,Z.X., Gao,X., Huang,C.,
            Wei,Z., Goding,C.R., Wang,P., Deng,X. and Cui,R.
  TITLE     Pharmacological Targeting of STK19 Inhibits Oncogenic NRAS-Driven
            Melanomagenesis
  JOURNAL   Cell 176 (5), 1113-1127 (2019)
   PUBMED   30712867
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Adler,N.R., Wolfe,R., Kelly,J.W., Haydon,A., McArthur,G.A.,
            McLean,C.A. and Mar,V.J.
  TITLE     Tumour mutation status and sites of metastasis in patients with
            cutaneous melanoma
  JOURNAL   Br J Cancer 117 (7), 1026-1035 (2017)
   PUBMED   28787433
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Fujiyoshi,K., Yamamoto,G., Takenoya,T., Takahashi,A., Arai,Y.,
            Yamada,M., Kakuta,M., Yamaguchi,K., Akagi,Y., Nishimura,Y.,
            Sakamoto,H. and Akagi,K.
  TITLE     Metastatic Pattern of Stage IV Colorectal Cancer with
            High-Frequency Microsatellite Instability as a Prognostic Factor
  JOURNAL   Anticancer Res 37 (1), 239-247 (2017)
   PUBMED   28011498
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Masui,T., Mann,A.M., Borgeson,C.D., Garland,E.M., Okamura,T.,
            Fujii,H., Pelling,J.C. and Cohen,S.M.
  TITLE     Sequencing analysis of Ha-, Ki-, and N-ras genes in rat urinary
            bladder tumors induced by
            N-[4-(5-nitro-2-furyl)-2-thiazolyl]formamide (FANFT) and sodium
            saccharin
  JOURNAL   Teratog Carcinog Mutagen 13 (5), 225-233 (1993)
   PUBMED   7905676
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Fujimoto,Y., Ishizaka,Y., Tahira,T., Sone,H., Takahashi,H.,
            Enomoto,K., Mori,M., Sugimura,T. and Nagao,M.
  TITLE     Possible involvement of c-myc but not ras genes in hepatocellular
            carcinomas developing after spontaneous hepatitis in LEC rats
  JOURNAL   Mol Carcinog 4 (4), 269-274 (1991)
   PUBMED   1714740
REFERENCE   8  (residues 1 to 189)
  AUTHORS   McMahon,G., Davis,E.F., Huber,L.J., Kim,Y. and Wogan,G.N.
  TITLE     Characterization of c-Ki-ras and N-ras oncogenes in aflatoxin
            B1-induced rat liver tumors
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 1104-1108 (1990)
   PUBMED   2105496
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Leibovitch,S.A., Leibovitch,M.P., Guillier,M., Hillion,J. and
            Harel,J.
  TITLE     Differential expression of protooncogenes related to transformation
            and cancer progression in rat myoblasts
  JOURNAL   Cancer Res 46 (8), 4097-4103 (1986)
   PUBMED   2425941
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Hu,L.F., Wang,L.P., Ju,L.W., Huang,L.H., Li,X.L., Li,X.Z. and
            Gu,J.R.
  TITLE     Expression of N-ras gene in human primary hepatocarcinoma
  JOURNAL   Sci Sin B 29 (2), 181-186 (1986)
   PUBMED   3018923
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098659.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346632.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098659.1, SRR8487231.30993.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..189
                     /product="GTPase NRas"
                     /EC_number="3.6.5.2"
                     /note="transforming protein N-Ras; neuroblastoma ras
                     oncogene; neuroblastoma RAS viral (v-ras) oncogene
                     homolog; neuroblastoma RAS viral oncogene homolog"
                     /calculated_mol_wt=21112
     mat_peptide     1..186
                     /product="GTPase NRas. /id=PRO_0000043014"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04970.1)"
                     /calculated_mol_wt=20914
     Region          3..164
                     /region_name="H_N_K_Ras_like"
                     /note="Ras GTPase family containing H-Ras,N-Ras and
                     K-Ras4A/4B; cd04138"
                     /db_xref="CDD:133338"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133338"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133338"
     Site            order(12..18,28..30,32,35,60,116..117,119..120,145..146)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133338"
     Site            order(17..18,30..32,34,37,40..41,54..55,57,59..61,63..65,
                     67,69..71,73,102..103,147)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:133338"
     Site            order(25,37..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133338"
     Region          32..40
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04970.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133338"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133338"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133338"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133338"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01111; propagated from
                     UniProtKB/Swiss-Prot (Q04970.1)"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133338"
     Site            145..147
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133338"
     Region          166..185
                     /region_name="Hypervariable region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04970.1)"
     CDS             1..189
                     /gene="Nras"
                     /coded_by="NM_080766.2:103..672"
                     /db_xref="GeneID:24605"
                     /db_xref="RGD:3205"
ORIGIN      
        1 mteyklvvvg aggvgksalt iqliqnhfvd eydptiedsy rkqvvidget clldildtag
       61 qeeysamrdq ymrtgegflc vfainnsksf adinlyreqi krvkdsddvp mvlvgnkcdl
      121 ptrtvdtkqa helaksygip fietsaktrq gvedafytlv reirqyrmkk lnssedgtqg
      181 cmglpcvvm
//
LOCUS       NP_001102495             180 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF5 [Rattus norvegicus].
ACCESSION   NP_001102495
VERSION     NP_001102495.1
DBSOURCE    REFSEQ: accession NM_001109025.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   El Khouri,E., Le Pavec,G., Toledano,M.B. and Delaunay-Moisan,A.
  TITLE     RNF185 is a novel E3 ligase of endoplasmic reticulum-associated
            degradation (ERAD) that targets cystic fibrosis transmembrane
            conductance regulator (CFTR)
  JOURNAL   J Biol Chem 288 (43), 31177-31191 (2013)
   PUBMED   24019521
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Kuang,E., Okumura,C.Y., Sheffy-Levin,S., Varsano,T., Shu,V.C.,
            Qi,J., Niesman,I.R., Yang,H.J., Lopez-Otin,C., Yang,W.Y.,
            Reed,J.C., Broday,L., Nizet,V. and Ronai,Z.A.
  TITLE     Regulation of ATG4B stability by RNF5 limits basal levels of
            autophagy and influences susceptibility to bacterial infection
  JOURNAL   PLoS Genet 8 (10), e1003007 (2012)
   PUBMED   23093945
  REMARK    Erratum:[PLoS Genet. 2020 May 11;16(5):e1008795. doi:
            10.1371/journal.pgen.1008795. PMID: 32392217]
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Tcherpakov,M., Delaunay,A., Toth,J., Kadoya,T., Petroski,M.D. and
            Ronai,Z.A.
  TITLE     Regulation of endoplasmic reticulum-associated degradation by
            RNF5-dependent ubiquitination of JNK-associated membrane protein
            (JAMP)
  JOURNAL   J Biol Chem 284 (18), 12099-12109 (2009)
   PUBMED   19269966
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Zhong,B., Zhang,L., Lei,C., Li,Y., Mao,A.P., Yang,Y., Wang,Y.Y.,
            Zhang,X.L. and Shu,H.B.
  TITLE     The ubiquitin ligase RNF5 regulates antiviral responses by
            mediating degradation of the adaptor protein MITA
  JOURNAL   Immunity 30 (3), 397-407 (2009)
   PUBMED   19285439
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY573537.1 and BC088341.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088341.1, DV721801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..180
                     /product="E3 ubiquitin-protein ligase RNF5"
                     /EC_number="2.3.2.27"
                     /note="ing finger protein 5 pseudogene; ring finger
                     protein 5, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase RNF5"
                     /calculated_mol_wt=19706
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q99942; propagated from
                     UniProtKB/Swiss-Prot (Q5M807.1)"
     Region          25..81
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(27,30,42,44,47,50,64,67)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438402"
     Region          79..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M807.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99942; propagated from
                     UniProtKB/Swiss-Prot (Q5M807.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99942; propagated from
                     UniProtKB/Swiss-Prot (Q5M807.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99942; propagated from
                     UniProtKB/Swiss-Prot (Q5M807.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M807.1)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M807.1)"
     CDS             1..180
                     /gene="Rnf5"
                     /coded_by="NM_001109025.2:99..641"
                     /db_xref="GeneID:407784"
                     /db_xref="RGD:1588458"
ORIGIN      
        1 maaaeeedgg pegpnrergg asatfecnic letareavvs vcghlycwpc lhqwletrpd
       61 rqecpvckag isrekvvply grgsqkpqdp rlktpprpqg qrpapesrgg fqpfgdaggf
      121 hfsfgvgafp fgffttvfna hepfrrgagv dlgqghpass wqdslflfla iffffwllsi
//
LOCUS       NP_001029129             422 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNG3 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001029129
VERSION     NP_001029129.1
DBSOURCE    REFSEQ: accession NM_001033957.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Mederos Y Schnitzler,M., Rinne,S., Skrobek,L., Renigunta,V.,
            Schlichthorl,G., Derst,C., Gudermann,T., Daut,J. and
            Preisig-Muller,R.
  TITLE     Mutation of histidine 105 in the T1 domain of the potassium channel
            Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4
  JOURNAL   J Biol Chem 284 (7), 4695-4704 (2009)
   PUBMED   19074135
  REMARK    GeneRIF: Mutation of histidine 105 in the T1 domain of the
            potassium channel Kv2.1 disrupts heteromerization with Kv6.3 and
            Kv6.4.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Vega-Saenz de Miera,E.C.
  TITLE     Modification of Kv2.1 K+ currents by the silent Kv10 subunits
  JOURNAL   Brain Res Mol Brain Res 123 (1-2), 91-103 (2004)
   PUBMED   15046870
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Ottschytsch,N., Raes,A., Van Hoorick,D. and Snyders,D.J.
  TITLE     Obligatory heterotetramerization of three previously
            uncharacterized Kv channel alpha-subunits identified in the human
            genome
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 7986-7991 (2002)
   PUBMED   12060745
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Sano,Y., Mochizuki,S., Miyake,A., Kitada,C., Inamura,K., Yokoi,H.,
            Nozawa,K., Matsushime,H. and Furuichi,K.
  TITLE     Molecular cloning and characterization of Kv6.3, a novel modulatory
            subunit for voltage-gated K(+) channel Kv2.1
  JOURNAL   FEBS Lett 512 (1-3), 230-234 (2002)
   PUBMED   11852086
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF454549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF454549.1, AI043703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..422
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNG3 isoform 2"
                     /note="potassium voltage-gated channel, subfamily G,
                     memeber 3; potassium voltage-gated channel, subfamily G,
                     member 3; voltage-gated potassium channel subunit Kv6.3;
                     voltage-gated potassium channel subunit Kv10.1; potassium
                     channel, voltage gated modifier subfamily G, member 3;
                     voltage-gated potassium channel 6.3; voltage-gated
                     potassium channel regulatory subunit KCNG3"
                     /calculated_mol_wt=48071
     Region          11..122
                     /region_name="BTB_POZ_KCNG3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily G member 3 (KCNG3);
                     cd18422"
                     /db_xref="CDD:349729"
     Site            order(14,16..23,26,62,64..65,68,71,75,78,82,84,92..93,96)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349729"
     Region          199..406
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     CDS             1..422
                     /gene="Kcng3"
                     /gene_synonym="Kv10.1; Kv6.3"
                     /coded_by="NM_001033957.1:43..1311"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171011"
                     /db_xref="RGD:628832"
ORIGIN      
        1 mtfgrggaas vvlnvggary slsrellkdf plrrvsrlhg crserdvlev cddydrerne
       61 yffdrhseaf gfillyvrgh gklrfaprmc elsfynemiy wglegahley ccqrrlddrm
      121 sdthtfhaae elgreqprpt gpeaapsrrw lermrrtfee ptsslaaqil asvsvvfviv
      181 smvvlcastl pdwraaaadn rslddrsrii eaicigwfta ecivrfivsk nkcefvkrpl
      241 niidllaitp yyisvlmtvf tgensqlqra gvtlrvlrmm rifwviklar hfiglqtlgl
      301 tlkrcyremv mllvficvam aifsalsqll ehgldletsn kdfasipaac wwviismttv
      361 gygdmypitv pgrilggvcv vsgivllalp itfiyhsfvq cyhelkfrsa rysrslsaef
      421 ln
//
LOCUS       NP_001011964             522 aa            linear   ROD 27-APR-2025
DEFINITION  target of rapamycin complex 2 subunit MAPKAP1 [Rattus norvegicus].
ACCESSION   NP_001011964 XP_216040
VERSION     NP_001011964.1
DBSOURCE    REFSEQ: accession NM_001011964.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Laplante,M. and Sabatini,D.M.
  TITLE     mTOR signaling in growth control and disease
  JOURNAL   Cell 149 (2), 274-293 (2012)
   PUBMED   22500797
  REMARK    Review article
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Murata,H., Sakaguchi,M., Jin,Y., Sakaguchi,Y., Futami,J.,
            Yamada,H., Kataoka,K. and Huh,N.H.
  TITLE     A new cytosolic pathway from a Parkinson disease-associated kinase,
            BRPK/PINK1: activation of AKT via mTORC2
  JOURNAL   J Biol Chem 286 (9), 7182-7189 (2011)
   PUBMED   21177249
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Ma,X.M. and Blenis,J.
  TITLE     Molecular mechanisms of mTOR-mediated translational control
  JOURNAL   Nat Rev Mol Cell Biol 10 (5), 307-318 (2009)
   PUBMED   19339977
  REMARK    Review article
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Schroder,W.A., Buck,M., Cloonan,N., Hancock,J.F., Suhrbier,A.,
            Sculley,T. and Bushell,G.
  TITLE     Human Sin1 contains Ras-binding and pleckstrin homology domains and
            suppresses Ras signalling
  JOURNAL   Cell Signal 19 (6), 1279-1289 (2007)
   PUBMED   17303383
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Jacinto,E., Facchinetti,V., Liu,D., Soto,N., Wei,S., Jung,S.Y.,
            Huang,Q., Qin,J. and Su,B.
  TITLE     SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
            phosphorylation and substrate specificity
  JOURNAL   Cell 127 (1), 125-137 (2006)
   PUBMED   16962653
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079073.1.
            
            On Feb 11, 2005 this sequence version replaced XP_216040.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079073.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132272
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..522
                     /product="target of rapamycin complex 2 subunit MAPKAP1"
                     /note="TORC2 subunit MAPKAP1; SAPK-interacting protein 1;
                     stress-activated map kinase-interacting protein 1;
                     mitogen-activated protein kinase 2-associated protein 1;
                     mitogen-activated protein kinase associated protein 1;
                     target of rapamycin complex 2 subunit MAPKAP1-like"
                     /calculated_mol_wt=58912
     Region          2..267
                     /region_name="Interaction with NBN.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          2..184
                     /region_name="Interaction with MAP3K2.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          18..129
                     /region_name="SIN1"
                     /note="Stress-activated map kinase interacting protein 1
                     (SIN1); pfam05422"
                     /db_xref="CDD:461648"
     Region          38..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          140..266
                     /region_name="CRIM"
                     /note="SAPK-interacting protein 1 (Sin1), middle CRIM
                     domain; pfam16978"
                     /db_xref="CDD:465326"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          279..353
                     /region_name="SIN1-type RBD. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          383..490
                     /region_name="PH_Avo1"
                     /note="Avo1 Pleckstrin homology (PH) domain; cd13331"
                     /db_xref="CDD:270139"
     Site            order(385..388,399..403,430,452,466..469,474,477..478,481)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270139"
     Site            order(390,392..393,398,400,427..428,430,464,466)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270139"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKH7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Region          468..522
                     /region_name="Interaction with ATF2.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYF1.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BPZ7; propagated from
                     UniProtKB/Swiss-Prot (Q6AYF1.1)"
     CDS             1..522
                     /gene="Mapkap1"
                     /coded_by="NM_001011964.1:443..2011"
                     /db_xref="GeneID:296648"
                     /db_xref="RGD:1305363"
ORIGIN      
        1 mafldnptii lahirqshvt sddtgmcemv lidhdvdlek thppsvpgds gsevqgssge
       61 tqgyiyaqsv ditsswdfgi rrrsntaqrl erlrkerqnq ikckniqwke rnskqsaqel
      121 kslfekkslk ekppssgkqs ilsvrleqcp lqlnnpfney skfdgkghvg ttatkkidvy
      181 lplhssqdrl lpmtvvtmas arvqdligli cwqytsegre pklndnvsay clhiaeddge
      241 vdtdfpplds nepihkfgfs tlalvekyss pgltskeslf vrinaahgfs liqvdntkvt
      301 mkeillkalk rrkgsqkisg pqyrlekqse pnigvdlest lesqnawefc lvrenssrad
      361 gvfeedsqid iatvqdmlss hhyksfkvsm ihrlrfttdv qlgisgdkve idpvtnqkas
      421 tkfwikqkpi sidcdllcac dlaeekspsh avfkltylss hdykhlyfes daatvseivl
      481 kvnyilesra staradyfaq kqrklnrrts fsfqkekksg qq
//
LOCUS       NP_001020150             407 aa            linear   ROD 27-APR-2025
DEFINITION  G patch domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_001020150 XP_215614
VERSION     NP_001020150.1
DBSOURCE    REFSEQ: accession NM_001024979.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC093381.1.
            
            On Jun 25, 2005 this sequence version replaced XP_215614.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093381.1, CV078035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..407
                     /product="G patch domain-containing protein 4"
                     /calculated_mol_wt=45942
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q5T3I0; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5T3I0; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     Region          8..55
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          116..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q566R3.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5T3I0; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T3I0; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T3I0; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     Region          187..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q566R3.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TFK5; propagated from
                     UniProtKB/Swiss-Prot (Q566R3.1)"
     CDS             1..407
                     /gene="Gpatch4"
                     /gene_synonym="RGD1311086"
                     /coded_by="NM_001024979.1:120..1343"
                     /db_xref="GeneID:295228"
                     /db_xref="RGD:1311086"
ORIGIN      
        1 msvtpevksr gmkfaeeqll khgwtqgkgl grkengitqa lkvtlkqdth gvghdpakef
       61 tdhwwsdlfn ktaanlvvds gkdgvqirrl skettqrshs kpsllyqkfv ktatltsgee
      121 kpdrdlescs dvdnrepipp kiltdemllk acegrtahka arigitmkak larleaqeqa
      181 flarlkgskd vgtsqpltds epsqkkkkrr kqkeeeeaat tekslgeell ehtdksfrks
      241 kkkkkkkkde regtaigsee eeaagvcgpa elsteqsdqs srkkkkrrrr hheeeeemgv
      301 cdeggrdvtg gpkavnsgad tdpwrsskkr qtceedldtq deedkddltk kerkvrkkdk
      361 kkrqqyceev ldvsnkddgr tweaedgger sqphpkarak kkkrktd
//
LOCUS       NP_037175                143 aa            linear   ROD 27-APR-2025
DEFINITION  TSC22 domain family protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_037175
VERSION     NP_037175.1
DBSOURCE    REFSEQ: accession NM_013043.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Yan,X., Zhang,J., Pan,L., Wang,P., Xue,H., Zhang,L., Gao,X.,
            Zhao,X., Ning,Y. and Chen,Y.G.
  TITLE     TSC-22 promotes transforming growth factor beta-mediated cardiac
            myofibroblast differentiation by antagonizing Smad7 activity
  JOURNAL   Mol Cell Biol 31 (18), 3700-3709 (2011)
   PUBMED   21791611
  REMARK    GeneRIF: TSC-22 can promote the differentiation of cardiac
            myofibroblasts by increasing expression of the fibrotic genes for
            alpha-smooth muscle actin, PAI-1, fibronectin, and collagen I.
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Huser,C.A., Pringle,M.A., Heath,V.J., Bell,A.K., Kendrick,H.,
            Smalley,M.J., Crighton,D., Ryan,K.M., Gusterson,B.A. and Stein,T.
  TITLE     TSC-22D1 isoforms have opposing roles in mammary epithelial cell
            survival
  JOURNAL   Cell Death Differ 17 (2), 304-315 (2010)
   PUBMED   19745830
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Ohta,S., Shimekake,Y. and Nagata,K.
  TITLE     Molecular cloning and characterization of a transcription factor
            for the C-type natriuretic peptide gene promoter
  JOURNAL   Eur J Biochem 242 (3), 460-466 (1996)
   PUBMED   9022669
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Hamil,K.G. and Hall,S.H.
  TITLE     Cloning of rat Sertoli cell follicle-stimulating hormone primary
            response complementary deoxyribonucleic acid: regulation of TSC-22
            gene expression
  JOURNAL   Endocrinology 134 (3), 1205-1212 (1994)
   PUBMED   8161377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB771530.1, L25785.1 and BG372788.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB771530.1, BC127547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..143
                     /product="TSC22 domain family protein 1 isoform 2"
                     /note="TSC22 domain family protein 1; regulatory protein
                     TSC-22; TGFB-stimulated clone 22 homolog; transforming
                     growth factor beta-1-induced transcript 4 protein;
                     Transforming growth factor beta stimulated clone 22;
                     transforming growth factor beta 1 induced transcript 4"
                     /calculated_mol_wt=15451
     Region          53..131
                     /region_name="ZIP_TSC22D1"
                     /note="leucine zipper domain found in TSC22 domain family
                     protein 1; cd21938"
                     /db_xref="CDD:409278"
     Site            order(71..73,76,79..80,83..84,86..87,90..91,93..94,97..98,
                     101,105)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409278"
     CDS             1..143
                     /gene="Tsc22d1"
                     /gene_synonym="Tgfb1i4; TS22A; TSC-22"
                     /coded_by="NM_013043.2:187..618"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:498545"
                     /db_xref="RGD:3850"
ORIGIN      
        1 mksqwcrpva mdlgvyqlrh fsisflssll gtenasvrld nssgasvvai dnkieqamdl
       61 vkshlmyavr eevevlkeqi kelieknsql eqennllktl aspeqlaqfq aqlqtgsppa
      121 ttqpqgttqp paqpasqgsg sta
//
LOCUS       NP_579844                284 aa            linear   ROD 27-APR-2025
DEFINITION  protein-S-isoprenylcysteine O-methyltransferase [Rattus
            norvegicus].
ACCESSION   NP_579844 XP_342989
VERSION     NP_579844.2
DBSOURCE    REFSEQ: accession NM_133310.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ibrahim,M.X., Sayin,V.I., Akula,M.K., Liu,M., Fong,L.G., Young,S.G.
            and Bergo,M.O.
  TITLE     Targeting isoprenylcysteine methylation ameliorates disease in a
            mouse model of progeria
  JOURNAL   Science 340 (6138), 1330-1333 (2013)
   PUBMED   23686339
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Jayaram,B., Syed,I., Singh,A., Subasinghe,W., Kyathanahalli,C.N.
            and Kowluru,A.
  TITLE     Isoprenylcysteine carboxyl methyltransferase facilitates
            glucose-induced Rac1 activation, ROS generation and insulin
            secretion in INS 832/13 beta-cells
  JOURNAL   Islets 3 (2), 48-57 (2011)
   PUBMED   21346419
  REMARK    GeneRIF: data suggest that ICMT regulates glucose-induced Rac1
            activation, generation of reactive oxygen species and insulin
            secretion in pancreatic beta-cells
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Baron,R.A. and Casey,P.J.
  TITLE     Analysis of the kinetic mechanism of recombinant human
            isoprenylcysteine carboxylmethyltransferase (Icmt)
  JOURNAL   BMC Biochem 5, 19 (2004)
   PUBMED   15625008
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Bergo,M.O., Gavino,B.J., Hong,C., Beigneux,A.P., McMahon,M.,
            Casey,P.J. and Young,S.G.
  TITLE     Inactivation of Icmt inhibits transformation by oncogenic K-Ras and
            B-Raf
  JOURNAL   J Clin Invest 113 (4), 539-550 (2004)
   PUBMED   14966563
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kramer,K., Harrington,E.O., Lu,Q., Bellas,R., Newton,J.,
            Sheahan,K.L. and Rounds,S.
  TITLE     Isoprenylcysteine carboxyl methyltransferase activity modulates
            endothelial cell apoptosis
  JOURNAL   Mol Biol Cell 14 (3), 848-857 (2003)
   PUBMED   12631708
  REMARK    GeneRIF: findings suggest that inhibition of
            isoprenylcysteine-O-carboxyl methyltransferase (ICMT) causes
            endothelial cell apoptosis by attenuation of Ras GTPase methylation
            and activation and its downstream antiapoptotic signaling pathway.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Bergo,M.O., Leung,G.K., Ambroziak,P., Otto,J.C., Casey,P.J.,
            Gomes,A.Q., Seabra,M.C. and Young,S.G.
  TITLE     Isoprenylcysteine carboxyl methyltransferase deficiency in mice
  JOURNAL   J Biol Chem 276 (8), 5841-5845 (2001)
   PUBMED   11121396
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Bergo,M.O., Leung,G.K., Ambroziak,P., Otto,J.C., Casey,P.J. and
            Young,S.G.
  TITLE     Targeted inactivation of the isoprenylcysteine carboxyl
            methyltransferase gene causes mislocalization of K-Ras in mammalian
            cells
  JOURNAL   J Biol Chem 275 (23), 17605-17610 (2000)
   PUBMED   10747846
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Desrosiers,R.R., Nguyen,Q.T. and Beliveau,R.
  TITLE     The carboxyl methyltransferase modifying G proteins is a
            metalloenzyme
  JOURNAL   Biochem Biophys Res Commun 261 (3), 790-797 (1999)
   PUBMED   10441503
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Dai,Q., Choy,E., Chiu,V., Romano,J., Slivka,S.R., Steitz,S.A.,
            Michaelis,S. and Philips,M.R.
  TITLE     Mammalian prenylcysteine carboxyl methyltransferase is in the
            endoplasmic reticulum
  JOURNAL   J Biol Chem 273 (24), 15030-15034 (1998)
   PUBMED   9614111
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Boivin,D., Lin,W. and Beliveau,R.
  TITLE     Essential arginine residues in isoprenylcysteine protein carboxyl
            methyltransferase
  JOURNAL   Biochem Cell Biol 75 (1), 63-69 (1997)
   PUBMED   9192075
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB616023.1 and BC083923.1.
            
            On Oct 11, 2007 this sequence version replaced NP_579844.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF075595.1, EV765737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..284
                     /product="protein-S-isoprenylcysteine O-methyltransferase"
                     /EC_number="2.1.1.100"
                     /note="farnesyl cysteine carboxyl methyltransferase; PPMT;
                     pcCMT; prenylcysteine carboxyl methyltransferase;
                     prenylated protein carboxyl methyltransferase;
                     prenylcysteine carboxyl methlytransferase"
                     /calculated_mol_wt=31681
     Site            17..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            42..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            70..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            93..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            132..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            155..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Region          163..257
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; pfam04140"
                     /db_xref="CDD:427740"
     Site            213..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     Site            230..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVM4.2)"
     CDS             1..284
                     /gene="Icmt"
                     /gene_synonym="fcmt"
                     /coded_by="NM_133310.2:58..912"
                     /db_xref="GeneID:170818"
                     /db_xref="RGD:621618"
ORIGIN      
        1 magcaarvpp gsearlslat fllgasvlal plltraglqg rtglalyvag lnalllllyr
       61 ppryqiaira cflgfvfgcg vllsfsqssw nhfgwyvcsl slfhyseylv tavnnpksls
      121 ldsfllnhsl eytvaalssw ieftlenifw pelkqitwls aagllmvifg eclrkvamft
      181 agsnfnhvvq seksdthtlv tsgvyawcrh psyvgwfyws igtqvmlcnp icgvvyaltv
      241 wrffrdrtee eeislihffg eeyldykkrv ptglpfikgv kvgl
//
LOCUS       NP_001094470             326 aa            linear   ROD 27-APR-2025
DEFINITION  microtubule-associated protein RP/EB family member 2 [Rattus
            norvegicus].
ACCESSION   NP_001094470 XP_001054908 XP_001054963 XP_001055029
VERSION     NP_001094470.1
DBSOURCE    REFSEQ: accession NM_001101000.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Yue,J., Xie,M., Gou,X., Lee,P., Schneider,M.D. and Wu,X.
  TITLE     Microtubules regulate focal adhesion dynamics through MAP4K4
  JOURNAL   Dev Cell 31 (5), 572-585 (2014)
   PUBMED   25490267
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Sigal,A., Milo,R., Cohen,A., Geva-Zatorsky,N., Klein,Y., Alaluf,I.,
            Swerdlin,N., Perzov,N., Danon,T., Liron,Y., Raveh,T.,
            Carpenter,A.E., Lahav,G. and Alon,U.
  TITLE     Dynamic proteomics in individual human cells uncovers widespread
            cell-cycle dependence of nuclear proteins
  JOURNAL   Nat Methods 3 (7), 525-531 (2006)
   PUBMED   16791210
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Komarova,Y., Lansbergen,G., Galjart,N., Grosveld,F., Borisy,G.G.
            and Akhmanova,A.
  TITLE     EB1 and EB3 control CLIP dissociation from the ends of growing
            microtubules
  JOURNAL   Mol Biol Cell 16 (11), 5334-5345 (2005)
   PUBMED   16148041
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105879.1.
            
            On or before Aug 13, 2007 this sequence version replaced
            XP_001054963.1, XP_001055029.1, XP_001054908.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105879.1, SRR8487230.33330.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..326
                     /product="microtubule-associated protein RP/EB family
                     member 2"
                     /note="microtubule-associated protein RP/EB family member
                     2-like"
                     /calculated_mol_wt=36857
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Region          58..315
                     /region_name="BIM1"
                     /note="Microtubule-binding protein involved in cell cycle
                     control [Cell division and chromosome partitioning /
                     Cytoskeleton]; COG5217"
                     /db_xref="CDD:227542"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q15555; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Region          170..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Region          186..326
                     /region_name="DCTN1-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15555; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15555; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Region          258..301
                     /region_name="APC-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     Region          297..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q0.1)"
     CDS             1..326
                     /gene="Mapre2"
                     /coded_by="NM_001101000.1:32..1012"
                     /db_xref="GeneID:679221"
                     /db_xref="RGD:1590736"
ORIGIN      
        1 mpgptqtlsp ngennndiiq dngtiipfrk htvrgersys wgmavnvyst sitqetmsrh
       61 diiawvndiv slnytkveql csgaaycqfm dmlfpgcisl kkvkfqakle heyihnfkll
      121 qasfkrmnvd kvipveklvk grfqdnldfi qwfkkfydan ydgkeydpve arqgqdaipp
      181 pdpgeqifnl pkkshhansp tagaaksspa akpgstpsrp ssakrasssg sasrsdkdle
      241 tqviqlneqv hslklalegv ekerdfyfgk lreiellcqe hgqenddlvq rlmevlyasd
      301 eqegqteepe veeqthdqqp qqqeey
//
LOCUS       NP_001019945             451 aa            linear   ROD 27-APR-2025
DEFINITION  differentially expressed in FDCP 8 homolog [Rattus norvegicus].
ACCESSION   NP_001019945 XP_226601
VERSION     NP_001019945.1
DBSOURCE    REFSEQ: accession NM_001024774.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Fujiwara,T., Ye,S., Castro-Gomes,T., Winchell,C.G., Andrews,N.W.,
            Voth,D.E., Varughese,K.I., Mackintosh,S.G., Feng,Y., Pavlos,N.,
            Nakamura,T., Manolagas,S.C. and Zhao,H.
  TITLE     PLEKHM1/DEF8/RAB7 complex regulates lysosome positioning and bone
            homeostasis
  JOURNAL   JCI Insight 1 (17), e86330 (2016)
   PUBMED   27777970
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097376.1.
            
            On Jun 10, 2005 this sequence version replaced XP_226601.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..451
                     /product="differentially expressed in FDCP 8 homolog"
                     /note="DEF-8"
                     /calculated_mol_wt=52567
     Region          18..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8I4.1)"
     Region          134..194
                     /region_name="C1_DEF8"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in differentially expressed in FDCP 8 (DEF-8) and
                     similar proteins; cd20819"
                     /db_xref="CDD:410369"
     Region          234..434
                     /region_name="zf-RING_9"
                     /note="Putative zinc-RING and/or ribbon; pfam13901"
                     /db_xref="CDD:464030"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V8I4.1)"
     CDS             1..451
                     /gene="Def8"
                     /coded_by="NM_001024774.1:80..1435"
                     /db_xref="GeneID:307973"
                     /db_xref="RGD:1309008"
ORIGIN      
        1 meydeklvrf rqahlnpfnk hlgprhheqe pnekaqevts edtlpelpag epefcyserm
       61 mdlglsedhf srpvglflas dvqqlrqaie eckqvilelp eqsekqkdav vrlihlrlkl
      121 qelkdpneee pnirvllehr fykeksksvk qtcdkcntii wgliqtwytc tgcyyrchsk
      181 clnlisrpcv sskvshqaey elnicpetgl dsqdyrcaec rapislrgvp searqcdytg
      241 qyycshchwn dlaviparvv hnwdfeprkv srcsmrylal mvsrpvlrlr einpllfnyv
      301 eelveirklr qdillmkpyf itckeamear lllqlqdrqh fvendemysi qdllevhmgr
      361 lscslteiht ifakhikldc ercqakgfvc elckegdvlf pfdshtsvcn dcsavfhrdc
      421 yydnsttcpk carltlrkqs lfqepgldvd a
//
LOCUS       NP_612535                428 aa            linear   ROD 27-APR-2025
DEFINITION  nocturnin [Rattus norvegicus].
ACCESSION   NP_612535 XP_001055998 XP_227134
VERSION     NP_612535.1
DBSOURCE    REFSEQ: accession NM_138526.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Estrella,M.A., Du,J., Chen,L., Rath,S., Prangley,E., Chitrakar,A.,
            Aoki,T., Schedl,P., Rabinowitz,J. and Korennykh,A.
  TITLE     The metabolites NADP+ and NADPH are the targets of the circadian
            protein Nocturnin (Curled)
  JOURNAL   Nat Commun 10 (1), 2367 (2019)
   PUBMED   31147539
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Nishikawa,S., Hatanaka,Y., Tokoro,M., Shin,S.W., Shimizu,N.,
            Nishihara,T., Kato,R., Takemoto,A., Amano,T., Anzai,M.,
            Kishigami,S., Hosoi,Y. and Matsumoto,K.
  TITLE     Functional analysis of nocturnin, a circadian deadenylase, at
            maternal-to-zygotic transition in mice
  JOURNAL   J Reprod Dev 59 (3), 258-265 (2013)
   PUBMED   23449310
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Niu,S., Shingle,D.L., Garbarino-Pico,E., Kojima,S., Gilbert,M. and
            Green,C.B.
  TITLE     The circadian deadenylase Nocturnin is necessary for stabilization
            of the iNOS mRNA in mice
  JOURNAL   PLoS One 6 (11), e26954 (2011)
   PUBMED   22073225
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Kawai,M., Delany,A.M., Green,C.B., Adamo,M.L. and Rosen,C.J.
  TITLE     Nocturnin suppresses igf1 expression in bone by targeting the 3'
            untranslated region of igf1 mRNA
  JOURNAL   Endocrinology 151 (10), 4861-4870 (2010)
   PUBMED   20685873
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Kawai,M., Green,C.B., Lecka-Czernik,B., Douris,N., Gilbert,M.R.,
            Kojima,S., Ackert-Bicknell,C., Garg,N., Horowitz,M.C., Adamo,M.L.,
            Clemmons,D.R. and Rosen,C.J.
  TITLE     A circadian-regulated gene, Nocturnin, promotes adipogenesis by
            stimulating PPAR-gamma nuclear translocation
  JOURNAL   Proc Natl Acad Sci U S A 107 (23), 10508-10513 (2010)
   PUBMED   20498072
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Zheng,D., Ezzeddine,N., Chen,C.Y., Zhu,W., He,X. and Shyu,A.B.
  TITLE     Deadenylation is prerequisite for P-body formation and mRNA decay
            in mammalian cells
  JOURNAL   J Cell Biol 182 (1), 89-101 (2008)
   PUBMED   18625844
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Garbarino-Pico,E., Niu,S., Rollag,M.D., Strayer,C.A., Besharse,J.C.
            and Green,C.B.
  TITLE     Immediate early response of the circadian polyA ribonuclease
            nocturnin to two extracellular stimuli
  JOURNAL   RNA 13 (5), 745-755 (2007)
   PUBMED   17400819
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Volkman,B.F., Prehoda,K.E., Scott,J.A., Peterson,F.C. and Lim,W.A.
  TITLE     Structure of the N-WASP EVH1 domain-WIP complex: insight into the
            molecular basis of Wiskott-Aldrich Syndrome
  JOURNAL   Cell 111 (4), 565-576 (2002)
   PUBMED   12437929
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Wang,Y., Osterbur,D.L., Megaw,P.L., Tosini,G., Fukuhara,C.,
            Green,C.B. and Besharse,J.C.
  TITLE     Rhythmic expression of Nocturnin mRNA in multiple tissues of the
            mouse
  JOURNAL   BMC Dev Biol 1, 9 (2001)
   PUBMED   11394964
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Mar 22, 2008 this sequence version replaced
            XP_227134.4, XP_001055998.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.9345.1,
                                           SRR26643289.6181.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..428
                     /product="nocturnin"
                     /EC_number="3.1.3.108"
                     /note="nocturin; CCR4 protein homolog; carbon catabolite
                     epression 4 homolog; CCR4 carbon catabolite repression
                     4-like B; circadian deadenylase NOC; carbon catabolite
                     repression 4-like protein"
                     /calculated_mol_wt=40459
     transit_peptide 1..72
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9ET55.2)"
                     /calculated_mol_wt=7681
     Region          21..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ET55.2)"
     mat_peptide     73..428
                     /product="Nocturnin. /evidence=ECO:0000255.
                     /id=PRO_0000424685"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ET55.2)"
                     /calculated_mol_wt=40459
     Region          141..420
                     /region_name="Deadenylase_nocturnin"
                     /note="C-terminal deadenylase domain of nocturnin and
                     related domains; cd09096"
                     /db_xref="CDD:197330"
     Site            order(146,192,283,286,288,294,321,323,325,364,369,
                     373..374,411)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197330"
     Site            order(146,192,283,286,288,294,321,323,325,364,369,373,411)
                     /site_type="other"
                     /note="putative poly(A) RNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:197330"
     Site            order(146,192,283,321,323,374,410..411)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197330"
     Site            order(146,192,410)
                     /site_type="other"
                     /note="putative Mg binding site A [ion binding]"
                     /db_xref="CDD:197330"
     Site            order(283,323,411)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197330"
     Site            order(321,323,411)
                     /site_type="other"
                     /note="putative Mg binding site B [ion binding]"
                     /db_xref="CDD:197330"
     Region          340..350
                     /region_name="Interaction with PPARG.
                     /evidence=ECO:0000250|UniProtKB:O35710"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ET55.2)"
     CDS             1..428
                     /gene="Noct"
                     /gene_synonym="Ccr4; Ccrn4l; Ccrn4lb"
                     /coded_by="NM_138526.1:226..1512"
                     /db_xref="GeneID:310395"
                     /db_xref="RGD:1587344"
ORIGIN      
        1 myqsprrlcs alllrdapgl rrtlvpgprr tlappvlgsr paspqlqaaa sgaarsrprt
       61 vspmgngtsr lysalaktin ssaaaqhpey lvsadpehle pidpkellee cravlhtrpp
      121 ryqrdfvdlr tdcssshppi rvmqwnilaq algegkdnfv qcpvealkwe erkclileei
      181 layqpdilcl qevdhyfdtf qpllsrlgyq gtffpkpwsp cldvehnngp dgcalfflqs
      241 rfklinstni rltamtlktn qvaiaqtlec kesgrqfcia vthlkartgw erfrsaqgcd
      301 llqnlqnite gakiplivcg dfnaepteev ykhfasssln lnsaykllsp dgqseppytt
      361 wkirtsgecr htldyiwysr halsvtsald llteeqigpn rlpsfhypsd hlslvcdfsf
      421 neepdell
//
LOCUS       NP_602308                477 aa            linear   ROD 27-APR-2025
DEFINITION  angiotensinogen precursor [Rattus norvegicus].
ACCESSION   NP_602308
VERSION     NP_602308.1
DBSOURCE    REFSEQ: accession NM_134432.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Toth,D.D., Souder,C.L. 2nd, Patuel,S., English,C.D., Konig,I.,
            Ivantsova,E., Malphurs,W., Watkins,J., Anne Costa,K., Bowden,J.A.,
            Zubcevic,J. and Martyniuk,C.J.
  TITLE     Angiotensin II Alters Mitochondrial Membrane Potential and Lipid
            Metabolism in Rat Colonic Epithelial Cells
  JOURNAL   Biomolecules 14 (8), 974 (2024)
   PUBMED   39199363
  REMARK    GeneRIF: Angiotensin II Alters Mitochondrial Membrane Potential and
            Lipid Metabolism in Rat Colonic Epithelial Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,W., Cai,S., Wu,F., Luo,Y., Xiao,H., Yu,D., Zhong,X., Tao,P.
            and Huang,S.
  TITLE     Combining experiments and bioinformatics to identify transforming
            growth factor-beta1 as a key regulator in angiotensin II-induced
            trophoblast senescence
  JOURNAL   Placenta 152, 31-38 (2024)
   PUBMED   38781757
  REMARK    GeneRIF: Combining experiments and bioinformatics to identify
            transforming growth factor-beta1 as a key regulator in angiotensin
            II-induced trophoblast senescence.
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Marunouchi,T., Onda,S., Kurasawa,M. and Tanonaka,K.
  TITLE     Angiotensin II Is Involved in MLKL Activation During the
            Development of Heart Failure Following Myocardial Infarction in
            Rats
  JOURNAL   Biol Pharm Bull 47 (4), 809-817 (2024)
   PUBMED   38583954
  REMARK    GeneRIF: Angiotensin II Is Involved in MLKL Activation During the
            Development of Heart Failure Following Myocardial Infarction in
            Rats.
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Paes-Leme,B., Monteiro,L.D.R.N., Gholami,K., Hoe,S.Z.,
            Ferguson,A.V., Murphy,D., Antunes-Rodrigues,J., Rorato,R.,
            Reis,L.C. and Mecawi,A.S.
  TITLE     Fasting increases circulating angiotensin levels and brain Agtr1a
            expression in male rats
  JOURNAL   J Neuroendocrinol 35 (11), e13334 (2023)
   PUBMED   37667574
  REMARK    GeneRIF: Fasting increases circulating angiotensin levels and brain
            Agtr1a expression in male rats.
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Sykora,M., Kratky,V., Kopkan,L., Tribulova,N. and Szeiffova
            Bacova,B.
  TITLE     Anti-Fibrotic Potential of Angiotensin (1-7) in Hemodynamically
            Overloaded Rat Heart
  JOURNAL   Int J Mol Sci 24 (4), 3490 (2023)
   PUBMED   36834901
  REMARK    GeneRIF: Anti-Fibrotic Potential of Angiotensin (1-7) in
            Hemodynamically Overloaded Rat Heart.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Jeunemaitre,X., Soubrier,F., Kotelevtsev,Y.V., Lifton,R.P.,
            Williams,C.S., Charru,A., Hunt,S.C., Hopkins,P.N., Williams,R.R.,
            Lalouel,J.M. et al.
  TITLE     Molecular basis of human hypertension: role of angiotensinogen
  JOURNAL   Cell 71 (1), 169-180 (1992)
   PUBMED   1394429
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Hermann,K., Rittweger,R. and Ring,J.
  TITLE     Urinary excretion of angiotensin I, II, arginine vasopressin and
            oxytocin in patients with anaphylactoid reactions
  JOURNAL   Clin Exp Allergy 22 (9), 845-853 (1992)
   PUBMED   1422942
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Mauzy,C.A., Hwang,O., Egloff,A.M., Wu,L.H. and Chung,F.Z.
  TITLE     Cloning, expression, and characterization of a gene encoding the
            human angiotensin II type 1A receptor
  JOURNAL   Biochem Biophys Res Commun 186 (1), 277-284 (1992)
   PUBMED   1378723
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Tucker,B.J., Mundy,C.A., Maciejewski,A.R., Printz,M.P.,
            Ziegler,M.G., Pelayo,J.C. and Blantz,R.C.
  TITLE     Changes in glomerular hemodynamic response to angiotensin II after
            subacute renal denervation in rats
  JOURNAL   J Clin Invest 78 (3), 680-688 (1986)
   PUBMED   3745432
REFERENCE   10 (residues 1 to 477)
  AUTHORS   Ohkubo,H., Nakayama,K., Tanaka,T. and Nakanishi,S.
  TITLE     Tissue distribution of rat angiotensinogen mRNA and structural
            analysis of its heterogeneity
  JOURNAL   J Biol Chem 261 (1), 319-323 (1986)
   PUBMED   3753601
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078741.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..477
                     /product="angiotensinogen precursor"
                     /note="angiotensin II; serpin A8; angiotensinogen (serpin
                     peptidase inhibitor, clade A, member 8)"
                     /calculated_mol_wt=49547
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2453
     mat_peptide     25..477
                     /product="Angiotensinogen. /id=PRO_0000032468"
                     /note="propagated from UniProtKB/Swiss-Prot (P01015.1)"
                     /calculated_mol_wt=49547
     Region          28..475
                     /region_name="serpinA8_AGT"
                     /note="serpin family A member 8, angiotensinogen; cd02054"
                     /db_xref="CDD:381010"
     Site            order(28..41,92..93,96,100,103,106..107,147,150..151,
                     154..155,158..159,355,362,390..391)
                     /site_type="other"
                     /note="renin binding site [polypeptide binding]"
                     /db_xref="CDD:381010"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01015.1)"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01015.1)"
     Site            order(426..437,446..451)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381010"
     CDS             1..477
                     /gene="Agt"
                     /gene_synonym="Ang; AngII; ANRT; PAT"
                     /coded_by="NM_134432.2:201..1634"
                     /db_xref="GeneID:24179"
                     /db_xref="RGD:2069"
ORIGIN      
        1 mtptgaglka tifciltwvs ltagdrvyih pfhllyysks tcaqlenpsv etlpeptfep
       61 vpiqaktspv dektlrdklv latekleaed rqraaqvami anfmgfrmyk mlseargvas
      121 gavlsppalf gtlvsfylgs ldptasqlqv llgvpvkegd ctsrldghkv ltalqavqgl
      181 lvtqggsssq tpllqstvvg lftapglrlk qpfveslgpf tpaifprsld lstdpvlaaq
      241 kinrfvqavt gwkmnlpleg vstdstlffn tyvhfqgkmr gfsqltglhe fwvdnstsvs
      301 vpmlsgtgnf qhwsdaqnnf svtrvplges vtllliqpqc asdldrvevl vfqhdfltwi
      361 knppprairl tlpqleirgs ynlqdllaqa klstllgaea nlgkmgdtnp rvgevlnsil
      421 lelqageeeq ptesaqqpgs pevldvtlss pflfaiyerd sgalhflgrv dnpqnvv
//
LOCUS       NP_445955                548 aa            linear   ROD 27-APR-2025
DEFINITION  LIM domain-containing protein ajuba [Rattus norvegicus].
ACCESSION   NP_445955 XP_341314
VERSION     NP_445955.1
DBSOURCE    REFSEQ: accession NM_053503.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Foxler,D.E., Bridge,K.S., James,V., Webb,T.M., Mee,M., Wong,S.C.,
            Feng,Y., Constantin-Teodosiu,D., Petursdottir,T.E., Bjornsson,J.,
            Ingvarsson,S., Ratcliffe,P.J., Longmore,G.D. and Sharp,T.V.
  TITLE     The LIMD1 protein bridges an association between the prolyl
            hydroxylases and VHL to repress HIF-1 activity
  JOURNAL   Nat Cell Biol 14 (2), 201-208 (2012)
   PUBMED   22286099
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 548)
  AUTHORS   James,V., Zhang,Y., Foxler,D.E., de Moor,C.H., Kong,Y.W.,
            Webb,T.M., Self,T.J., Feng,Y., Lagos,D., Chu,C.Y., Rana,T.M.,
            Morley,S.J., Longmore,G.D., Bushell,M. and Sharp,T.V.
  TITLE     LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for
            microRNA-mediated gene silencing
  JOURNAL   Proc Natl Acad Sci U S A 107 (28), 12499-12504 (2010)
   PUBMED   20616046
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Das Thakur,M., Feng,Y., Jagannathan,R., Seppa,M.J., Skeath,J.B. and
            Longmore,G.D.
  TITLE     Ajuba LIM proteins are negative regulators of the Hippo signaling
            pathway
  JOURNAL   Curr Biol 20 (7), 657-662 (2010)
   PUBMED   20303269
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Zheng,P. and Dean,J.
  TITLE     Role of Filia, a maternal effect gene, in maintaining euploidy
            during cleavage-stage mouse embryogenesis
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7473-7478 (2009)
   PUBMED   19376971
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Montoya-Durango,D.E., Velu,C.S., Kazanjian,A., Rojas,M.E.,
            Jay,C.M., Longmore,G.D. and Grimes,H.L.
  TITLE     Ajuba functions as a histone deacetylase-dependent co-repressor for
            autoregulation of the growth factor-independent-1 transcription
            factor
  JOURNAL   J Biol Chem 283 (46), 32056-32065 (2008)
   PUBMED   18805794
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Kisseleva,M., Feng,Y., Ward,M., Song,C., Anderson,R.A. and
            Longmore,G.D.
  TITLE     The LIM protein Ajuba regulates phosphatidylinositol
            4,5-bisphosphate levels in migrating cells through an interaction
            with and activation of PIPKI alpha
  JOURNAL   Mol Cell Biol 25 (10), 3956-3966 (2005)
   PUBMED   15870270
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Pratt,S.J., Epple,H., Ward,M., Feng,Y., Braga,V.M. and
            Longmore,G.D.
  TITLE     The LIM protein Ajuba influences p130Cas localization and Rac1
            activity during cell migration
  JOURNAL   J Cell Biol 168 (5), 813-824 (2005)
   PUBMED   15728191
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Marie,H., Pratt,S.J., Betson,M., Epple,H., Kittler,J.T., Meek,L.,
            Moss,S.J., Troyanovsky,S., Attwell,D., Longmore,G.D. and Braga,V.M.
  TITLE     The LIM protein Ajuba is recruited to cadherin-dependent cell
            junctions through an association with alpha-catenin
  JOURNAL   J Biol Chem 278 (2), 1220-1228 (2003)
   PUBMED   12417594
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Marie,H., Billups,D., Bedford,F.K., Dumoulin,A., Goyal,R.K.,
            Longmore,G.D., Moss,S.J. and Attwell,D.
  TITLE     The amino terminus of the glial glutamate transporter GLT-1
            interacts with the LIM protein Ajuba
  JOURNAL   Mol Cell Neurosci 19 (2), 152-164 (2002)
   PUBMED   11860269
  REMARK    GeneRIF: We propose that Ajuba is a scaffolding protein allowing
            GLT-1 to regulate intracellular signaling or interact with the
            cytoskeleton.
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Goyal,R.K., Lin,P., Kanungo,J., Payne,A.S., Muslin,A.J. and
            Longmore,G.D.
  TITLE     Ajuba, a novel LIM protein, interacts with Grb2, augments
            mitogen-activated protein kinase activity in fibroblasts, and
            promotes meiotic maturation of Xenopus oocytes in a Grb2- and
            Ras-dependent manner
  JOURNAL   Mol Cell Biol 19 (6), 4379-4389 (1999)
   PUBMED   10330178
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085802.1.
            
            On Nov 22, 2004 this sequence version replaced XP_341314.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085802.1, AJ306292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676787 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..548
                     /product="LIM domain-containing protein ajuba"
                     /note="protein ajuba; ajuba homolog; jub, ajuba homolog"
                     /calculated_mol_wt=57950
     Region          1..345
                     /region_name="PreLIM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Region          1..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IF1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IF1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IF1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IF1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96IF1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Region          290..298
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Region          307..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Z2.1)"
     Region          348..401
                     /region_name="LIM1_Ajuba_like"
                     /note="The first LIM domain of Ajuba-like proteins;
                     cd09352"
                     /db_xref="CDD:188738"
     Site            order(348,351,370,373,376,379,397,400)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188738"
     Region          413..465
                     /region_name="LIM2_Ajuba_like"
                     /note="The second LIM domain of Ajuba-like proteins;
                     cd09355"
                     /db_xref="CDD:188741"
     Site            order(413,416,433,436,439,442,461,464)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188741"
     Region          473..534
                     /region_name="LIM3_Ajuba_like"
                     /note="The third LIM domain of Ajuba-like proteins;
                     cd09438"
                     /db_xref="CDD:188822"
     Site            order(473,476,500,503,506,509,530,533)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188822"
     CDS             1..548
                     /gene="Ajuba"
                     /gene_synonym="Jub"
                     /coded_by="NM_053503.1:323..1969"
                     /db_xref="GeneID:85265"
                     /db_xref="RGD:620407"
ORIGIN      
        1 merlgekasr lleklrlsds gsakfgrrkg easrsgsdgt pgagkgrlsg lggprksghr
       61 ganggpgdea lepareqgpl daernargsf eaqrfegsfp ggppptralp lplssppdfr
      121 lettapalsp rssfasssas daskpssprg sllldgagas gaggsrpcsn rtsgismgyd
      181 qrhgsplpag pclfglpltt apsgyssggv psaypelhaa ldrlcahrpv gfgcqesrhs
      241 yppalgspga ltgavvgtag plerrgtqpg rhsvtgygdc aagaryqdel tallrltvat
      301 ggreagarge plgiepsgle espgsfvpea srsrirepea redyfgtcik cnkgiygqsn
      361 acqaldslyh tqcfvccscg rtlrckafys vngsvyceed ylfsgfqeaa ekccvcghli
      421 lekilqamgk syhpgcfrci vcnkcldgvp ftvdfsnqvy cvtdyhknya pkcaacgqpi
      481 lpsegcediv rvismdrdyh fecyhcedcr mqlsdeegcc cfpldghllc hgchmqrlsa
      541 rqpptnyi
//
LOCUS       NP_036975                160 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial membrane protein 1 [Rattus norvegicus].
ACCESSION   NP_036975
VERSION     NP_036975.1
DBSOURCE    REFSEQ: accession NM_012843.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Lee,H.S., Sherley,J.L., Chen,J.J., Chiu,C.C., Chiou,L.L.,
            Liang,J.D., Yang,P.C., Huang,G.T. and Sheu,J.C.
  TITLE     EMP-1 is a junctional protein in a liver stem cell line and in the
            liver
  JOURNAL   Biochem Biophys Res Commun 334 (4), 996-1003 (2005)
   PUBMED   16036215
  REMARK    GeneRIF: This report is the first to indicate EMP-1 to be a
            junctional protein in the liver.
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Wilson,H.L., Wilson,S.A., Surprenant,A. and North,R.A.
  TITLE     Epithelial membrane proteins induce membrane blebbing and interact
            with the P2X7 receptor C terminus
  JOURNAL   J Biol Chem 277 (37), 34017-34023 (2002)
   PUBMED   12107182
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Chen,Y., Medvedev,A., Ruzanov,P., Marvin,K.W. and Jetten,A.M.
  TITLE     cDNA cloning, genomic structure, and chromosome mapping of the
            human epithelial membrane protein CL-20 gene (EMP1), a member of
            the PMP22 family
  JOURNAL   Genomics 41 (1), 40-48 (1997)
   PUBMED   9126480
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Taylor,V., Welcher,A.A., Program,A.E. and Suter,U.
  TITLE     Epithelial membrane protein-1, peripheral myelin protein 22, and
            lens membrane protein 20 define a novel gene family
  JOURNAL   J Biol Chem 270 (48), 28824-28833 (1995)
   PUBMED   7499407
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087031.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087031.1, DY320853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q43"
     Protein         1..160
                     /product="epithelial membrane protein 1"
                     /note="tumor-associated membrane protein"
                     /calculated_mol_wt=17695
     Region          1..154
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; pfam00822"
                     /db_xref="CDD:395662"
     Site            1..21
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54848.1)"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54848.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54848.1)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54848.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54848.1)"
     CDS             1..160
                     /gene="Emp1"
                     /gene_synonym="CL-20; EMP-1; ENP1MR; TMP"
                     /coded_by="NM_012843.2:146..628"
                     /db_xref="GeneID:25314"
                     /db_xref="RGD:2552"
ORIGIN      
        1 mlvllaglfv vhiataimlf vstianvwmv adgidssigl wknctsgscd gslsygndda
       61 ikavqafmil siifsiislv vfvfqlftme kgnrfflsgs tmlvcwlcil igvsiythhy
      121 ahsegnffps shqgycfilt wicfcfsfii gilymvlrkk
//
LOCUS       NP_001094488             243 aa            linear   ROD 27-APR-2025
DEFINITION  ornithine decarboxylase antizyme 3 [Rattus norvegicus].
ACCESSION   NP_001094488
VERSION     NP_001094488.1
DBSOURCE    REFSEQ: accession NM_001101018.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Ramos-Molina,B., Lambertos,A., Lopez-Contreras,A.J., Kasprzak,J.M.,
            Czerwoniec,A., Bujnicki,J.M., Cremades,A. and Penafiel,R.
  TITLE     Structural and degradative aspects of ornithine decarboxylase
            antizyme inhibitor 2
  JOURNAL   FEBS Open Bio 4, 510-521 (2014)
   PUBMED   24967154
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Olsen,R.R. and Zetter,B.R.
  TITLE     Evidence of a role for antizyme and antizyme inhibitor as
            regulators of human cancer
  JOURNAL   Mol Cancer Res 9 (10), 1285-1293 (2011)
   PUBMED   21849468
  REMARK    Review article
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ruan,Y., Cheng,M., Ou,Y., Oko,R. and van der Hoorn,F.A.
  TITLE     Ornithine decarboxylase antizyme Oaz3 modulates protein phosphatase
            activity
  JOURNAL   J Biol Chem 286 (33), 29417-29427 (2011)
   PUBMED   21712390
  REMARK    GeneRIF: Ornithine decarboxylase antizyme Oaz3 modulates protein
            phosphatase activity.
REFERENCE   5  (residues 1 to 243)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Kanerva,K., Makitie,L.T., Pelander,A., Heiskala,M. and
            Andersson,L.C.
  TITLE     Human ornithine decarboxylase paralogue (ODCp) is an antizyme
            inhibitor but not an arginine decarboxylase
  JOURNAL   Biochem J 409 (1), 187-192 (2008)
   PUBMED   17900240
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Fitzgerald,C., Sikora,C., Lawson,V., Dong,K., Cheng,M., Oko,R. and
            van der Hoorn,F.A.
  TITLE     Mammalian transcription in support of hybrid mRNA and protein
            synthesis in testis and lung
  JOURNAL   J Biol Chem 281 (50), 38172-38180 (2006)
   PUBMED   17040916
  REMARK    GeneRIF: N-terminal protein sequencing suggests translation
            initiation from a non-AUG (CUG) start site.
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Lopez-Contreras,A.J., Lopez-Garcia,C., Jimenez-Cervantes,C.,
            Cremades,A. and Penafiel,R.
  TITLE     Mouse ornithine decarboxylase-like gene encodes an antizyme
            inhibitor devoid of ornithine and arginine decarboxylating activity
  JOURNAL   J Biol Chem 281 (41), 30896-30906 (2006)
   PUBMED   16916800
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Zhang,J., Wang,Y., Zhou,Y., Cao,Z., Huang,P. and Lu,B.
  TITLE     Yeast two-hybrid screens imply that GGNBP1, GGNBP2 and OAZ3 are
            potential interaction partners of testicular germ cell-specific
            protein GGN1
  JOURNAL   FEBS Lett 579 (2), 559-566 (2005)
   PUBMED   15642376
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Ivanov,I.P., Rohrwasser,A., Terreros,D.A., Gesteland,R.F. and
            Atkins,J.F.
  TITLE     Discovery of a spermatogenesis stage-specific ornithine
            decarboxylase antizyme: antizyme 3
  JOURNAL   Proc Natl Acad Sci U S A 97 (9), 4808-4813 (2000)
   PUBMED   10781085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DQ431008.1 and AW529628.1.
            
            Summary: The protein encoded by this gene belongs to the ornithine
            decarboxylase antizyme family, which plays a role in cell growth
            and proliferation by regulating intracellular polyamine levels.
            Expression of antizymes requires +1 ribosomal frameshifting, which
            is enhanced by high levels of polyamines. Antizymes in turn bind to
            and inhibit ornithine decarboxylase (ODC), the key enzyme in
            polyamine biosynthesis; thus, completing the auto-regulatory
            circuit. This gene encodes antizyme 3, the third member of the
            antizyme family. Like antizymes 1 and 2, antizyme 3 inhibits ODC
            activity and polyamine uptake; however, it does not stimulate ODC
            degradation. Also, while antizymes 1 and 2 have broad tissue
            distribution, expression of antizyme 3 is restricted to haploid
            germ cells in testis, suggesting a distinct role for this antizyme
            in spermiogenesis. Antizyme 3 gene knockout studies showed that
            homozygous mutant male mice were infertile, and indicated the
            likely role of this antizyme in the formation of a rigid connection
            between the sperm head and tail during spermatogenesis. This
            transcript initiates translation from a non-AUG (CUG) codon that is
            highly conserved among the antizyme 3 orthologs. [provided by
            RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ431008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 17040916
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ribosomal slippage       :: inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..243
                     /product="ornithine decarboxylase antizyme 3"
                     /note="antizyme 3"
                     /calculated_mol_wt=28054
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1BPI0.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1BPI0.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1BPI0.1)"
     Region          49
                     /region_name="alternative AUG translation initiation site"
     Region          151..234
                     /region_name="ODC_AZ"
                     /note="Ornithine decarboxylase antizyme; pfam02100"
                     /db_xref="CDD:460445"
     CDS             1..243
                     /gene="Oaz3"
                     /gene_synonym="Az3; Oaz-t; ODC-Az 3"
                     /coded_by="join(NM_001101018.1:12..269,
                     NM_001101018.1:271..744)"
                     /ribosomal_slippage
                     /note="protein translation is dependent on
                     polyamine-induced +1 ribosomal frameshift; non-AUG (CUG)
                     translation initiation codon"
                     /db_xref="GeneID:689588"
                     /db_xref="RGD:1599278"
ORIGIN      
        1 mpctrsrpsl yslsyikrgk trnclypfws pyayylycyk yritlrekml pccyrsityk
       61 eqedltlrph cclpcsclpy sclpcsesle glqvgrstaq ekdhsqlkel ysagnltvls
      121 adpllhqdpv qldfhfrltp hssahwhgll cdhqlfldip fqaleqgnre sltatleyve
      181 ektnvdsvfv nfqsnhkdrg allrafsymg fevvrpdhpa lppwdnvifm vyplerdlgq
      241 pgq
//
LOCUS       NP_001020943             341 aa            linear   ROD 27-APR-2025
DEFINITION  O(6)-methylguanine-induced apoptosis 2 [Rattus norvegicus].
ACCESSION   NP_001020943 XP_575933
VERSION     NP_001020943.1
DBSOURCE    REFSEQ: accession NM_001025772.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Fujikane,R., Sanada,M., Sekiguchi,M. and Hidaka,M.
  TITLE     The identification of a novel gene, MAPO2, that is involved in the
            induction of apoptosis triggered by O-methylguanine
  JOURNAL   PLoS One 7 (9), e44817 (2012)
   PUBMED   23028632
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098937.1.
            
            On Jul 22, 2005 this sequence version replaced XP_575933.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..341
                     /product="O(6)-methylguanine-induced apoptosis 2"
                     /note="UPF0490 protein C1orf201 homolog; sperm-tail
                     PG-rich repeat-containing protein 1;
                     O6-methylguanine-induced apoptosis 2"
                     /calculated_mol_wt=37403
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          73..80
                     /region_name="STPGR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5TH74; propagated from
                     UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          115..123
                     /region_name="STPGR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          154..160
                     /region_name="STPGR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          194..213
                     /region_name="STPGR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          232..254
                     /region_name="STPGR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          273..284
                     /region_name="STPGR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     Region          313..323
                     /region_name="STPGR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLY8.1)"
     CDS             1..341
                     /gene="Stpg1"
                     /gene_synonym="Mapo2"
                     /coded_by="NM_001025772.1:161..1186"
                     /db_xref="GeneID:500566"
                     /db_xref="RGD:1560169"
ORIGIN      
        1 msqkfantgs fieredlgkp nkgvdrvqkg ftaayptqss ipyrhrrsvi pesekrgfns
       61 qarrfyskkd dipgpgfynv ihqslvfnsv slskrgtctf pstcarlgpi iskypaanay
      121 tirselaskk dfsnscssmf qlptfikvvk setpapnhyn asisickqrn nvcaragfls
      181 ktprgfvpss epggpapghy dvneslvres pkvlvscfks ktgrglkpts tgpgpgyynp
      241 ndqtkilrks hlpkttllnf saqplplpek pplpgpgqye ivnyqgppkh fistasfvsn
      301 tsrwpvkssk ptlpgpasyk peipgkqsfl ynednkwipa v
//
LOCUS       NP_113742                512 aa            linear   ROD 27-APR-2025
DEFINITION  activin receptor type-2B precursor [Rattus norvegicus].
ACCESSION   NP_113742 XP_217297
VERSION     NP_113742.1
DBSOURCE    REFSEQ: accession NM_031554.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Feng,B., Meng,L., Luan,L., Fang,Z., Zhao,P. and Zhao,G.
  TITLE     Upregulation of Extracellular Vesicles-Encapsulated miR-132
            Released From Mesenchymal Stem Cells Attenuates Ischemic Neuronal
            Injury by Inhibiting Smad2/c-jun Pathway via Acvr2b Suppression
  JOURNAL   Front Cell Dev Biol 8, 568304 (2021)
   PUBMED   33763412
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Szabo,Z., Vainio,L., Lin,R., Swan,J., Hulmi,J.J., Rahtu-Korpela,L.,
            Serpi,R., Laitinen,M., Pasternack,A., Ritvos,O., Kerkela,R. and
            Magga,J.
  TITLE     Systemic blockade of ACVR2B ligands attenuates muscle wasting in
            ischemic heart failure without compromising cardiac function
  JOURNAL   FASEB J 34 (8), 9911-9924 (2020)
   PUBMED   32427381
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Tauer,J.T. and Rauch,F.
  TITLE     Novel ActRIIB ligand trap increases muscle mass and improves bone
            geometry in a mouse model of severe osteogenesis imperfecta
  JOURNAL   Bone 128, 115036 (2019)
   PUBMED   31419601
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Goebel,E.J., Corpina,R.A., Hinck,C.S., Czepnik,M., Castonguay,R.,
            Grenha,R., Boisvert,A., Miklossy,G., Fullerton,P.T., Matzuk,M.M.,
            Idone,V.J., Economides,A.N., Kumar,R., Hinck,A.P. and Thompson,T.B.
  TITLE     Structural characterization of an activin class ternary receptor
            complex reveals a third paradigm for receptor specificity
  JOURNAL   Proc Natl Acad Sci U S A 116 (31), 15505-15513 (2019)
   PUBMED   31315975
  REMARK    GeneRIF: the structure of an activin class member, GDF11, in
            complex with the type II receptor ActRIIB and the type I receptor
            Alk5, is reported.
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Magga,J., Vainio,L., Kilpio,T., Hulmi,J.J., Taponen,S., Lin,R.,
            Rasanen,M., Szabo,Z., Gao,E., Rahtu-Korpela,L., Alakoski,T.,
            Ulvila,J., Laitinen,M., Pasternack,A., Koch,W.J., Alitalo,K.,
            Kivela,R., Ritvos,O. and Kerkela,R.
  TITLE     Systemic Blockade of ACVR2B Ligands Protects Myocardium from Acute
            Ischemia-Reperfusion Injury
  JOURNAL   Mol Ther 27 (3), 600-610 (2019)
   PUBMED   30765322
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Feng,Z.M., Madigan,M.B. and Chen,C.L.
  TITLE     Expression of type II activin receptor genes in the male and female
            reproductive tissues of the rat
  JOURNAL   Endocrinology 132 (6), 2593-2600 (1993)
   PUBMED   7916681
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Nakamura,T., Sugino,K., Kurosawa,N., Sawai,M., Takio,K., Eto,Y.,
            Iwashita,S., Muramatsu,M., Titani,K. and Sugino,H.
  TITLE     Isolation and characterization of activin receptor from mouse
            embryonal carcinoma cells. Identification of its
            serine/threonine/tyrosine protein kinase activity
  JOURNAL   J Biol Chem 267 (26), 18924-18928 (1992)
   PUBMED   1326537
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Legerski,R., Zhou,X., Dresback,J., Eberspaecher,H., McKinney,S.,
            Segarini,P. and de Crombrugghe,B.
  TITLE     Molecular cloning and characterization of a novel rat activin
            receptor
  JOURNAL   Biochem Biophys Res Commun 183 (2), 672-679 (1992)
   PUBMED   1312838
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Attisano,L., Wrana,J.L., Cheifetz,S. and Massague,J.
  TITLE     Novel activin receptors: distinct genes and alternative mRNA
            splicing generate a repertoire of serine/threonine kinase receptors
  JOURNAL   Cell 68 (1), 97-108 (1992)
   PUBMED   1310075
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Pukach,L.P.
  TITLE     [Value of electrocardiography in the selection of persons for work
            under high altitude conditions]
  JOURNAL   Voen Med Zh (11), 49-51 (1978)
   PUBMED   734934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097358.1.
            
            On Jun 13, 2005 this sequence version replaced XP_217297.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097358.1, M87067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132301, SAMEA5756307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..512
                     /product="activin receptor type-2B precursor"
                     /EC_number="2.7.11.30"
                     /note="activin receptor type-2B; ACTR-IIB; activin
                     receptor type IIB; Activine receptor 2b (transmembrane
                     serine kinase); ActRIIB type II activin receptor B;
                     activin receptor IIB; activin A receptor, type IIB"
                     /calculated_mol_wt=55583
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2190
     Region          26..116
                     /region_name="TFP_LU_ECD_ACVR2B"
                     /note="extracellular domain (ECD) found in activin
                     receptor type-2B (ACTR-IIB) and similar proteins; cd23632"
                     /db_xref="CDD:467152"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38445.3)"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P38445.3)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P38445.3)"
     Region          194..484
                     /region_name="STKc_ACVR2b"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Activin Type IIB Receptor; cd14140"
                     /db_xref="CDD:271042"
     Site            order(196..200,204,215,217,245,265..268,272,274,321,323,
                     325..326,328,339,342,360..363)
                     /site_type="active"
                     /db_xref="CDD:271042"
     Site            order(196..202,204,215,217,265..266,268,272,325..326,328,
                     339)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271042"
     Site            order(200,272,274,321,323,325,342,360..363)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271042"
     Site            338..363
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271042"
     Region          491..512
                     /region_name="Interaction with DYNLT1.
                     /evidence=ECO:0000250|UniProtKB:P27040"
                     /note="propagated from UniProtKB/Swiss-Prot (P38445.3)"
     CDS             1..512
                     /gene="Acvr2b"
                     /coded_by="NM_031554.1:215..1753"
                     /db_xref="GeneID:25366"
                     /db_xref="RGD:2028"
ORIGIN      
        1 mtapwaalal lwgslcagsg rgeaetreci yynanweler tnqsglerce geqdkrlhcy
       61 aswrnssgti elvkkgcwld dfncydrqec vateenpqvy fcccegnfcn erfthlpepg
      121 gpevtyeppp taptlltvla ysllpiggls livllafwmy rhrkppyghv dihedpgppp
      181 psplvglkpl qlleikargr fgcvwkaqlm ndfvavkifp lqdkqswqse reifstpgmk
      241 henllqfiaa ekrgsnleve lwlitafhdk gsltdylkgn iitwnelchv aetmsrglsy
      301 lhedvpwcrg eghkpsiahr dfksknvllk sdltavladf glavrfepgk ppgdthgqvg
      361 trrymapevl egainfqrda flridmyamg lvlwelvsrc kaadgpvdey mlpfeeeigq
      421 hpsleelqev vvhkkmrpti kdhwlkhpgl aqlcvtieec wdhdaearls agcveervsl
      481 irrsvnssts dclvslvtsv tnvdllpkes si
//
LOCUS       NP_570826                318 aa            linear   ROD 27-APR-2025
DEFINITION  potassium channel subfamily K member 15 precursor [Rattus
            norvegicus].
ACCESSION   NP_570826 XP_342573
VERSION     NP_570826.1
DBSOURCE    REFSEQ: accession NM_130813.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Karschin,C., Wischmeyer,E., Preisig-Muller,R., Rajan,S., Derst,C.,
            Grzeschik,K.H., Daut,J. and Karschin,A.
  TITLE     Expression pattern in brain of TASK-1, TASK-3, and a tandem pore
            domain K(+) channel subunit, TASK-5, associated with the central
            auditory nervous system
  JOURNAL   Mol Cell Neurosci 18 (6), 632-648 (2001)
   PUBMED   11749039
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF467250.1.
            
            On Jan 1, 2004 this sequence version replaced XP_342573.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF467250.1, AF294353.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680414, SAMN06680427
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /strain="LE"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..318
                     /product="potassium channel subfamily K member 15
                     precursor"
                     /note="rTASK-5; TWIK-related acid-sensitive K(+) channel
                     5; acid-sensitive potassium channel protein TASK-5;
                     potassium channel, two pore domain subfamily K, member 15;
                     potassium channel, subfamily K, member 15 (TASK-5);
                     potassium channel subfamily K member 15"
                     /calculated_mol_wt=33178
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2492
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I0.1)"
     Region          <73..132
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I0.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I0.1)"
     Region          <184..243
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I0.1)"
     Region          296..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R5I0.1)"
     CDS             1..318
                     /gene="Kcnk15"
                     /coded_by="NM_130813.1:81..1037"
                     /db_xref="GeneID:156873"
                     /db_xref="RGD:619733"
ORIGIN      
        1 mrkqsartaa lilcilsyll vgaavfdale seaersrqrl larkrgefrr kyrfsaddyr
       61 elerlalqae phragrqwrf agsfyfaitv ittigyghaa pgtdsgkvfc mfyallgipl
      121 tlvtfqslge rlnalvrcll laakrclglr rphvsaenmv vaglllcaat lalgaaafah
      181 fegwtffhay yycfitltti gfgdfvalqr dealqkkppy vafsflyill gltvigafln
      241 lvvlrflasa eaperaalrr asvfrrgape srvripypfh pletwardnp afspplspea
      301 vhdchsspdr lrarrksi
//
LOCUS       NP_955419                409 aa            linear   ROD 27-APR-2025
DEFINITION  transcription termination factor 3, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_955419 XP_216818
VERSION     NP_955419.1
DBSOURCE    REFSEQ: accession NM_199387.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Park,C.B., Asin-Cayuela,J., Camara,Y., Shi,Y., Pellegrini,M.,
            Gaspari,M., Wibom,R., Hultenby,K., Erdjument-Bromage,H., Tempst,P.,
            Falkenberg,M., Gustafsson,C.M. and Larsson,N.G.
  TITLE     MTERF3 is a negative regulator of mammalian mtDNA transcription
  JOURNAL   Cell 130 (2), 273-285 (2007)
   PUBMED   17662942
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062080.1.
            
            On Jan 12, 2004 this sequence version replaced XP_216818.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062080.1, SRR8487226.129116.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..409
                     /product="transcription termination factor 3,
                     mitochondrial precursor"
                     /note="mTERF domain-containing protein 1, mitochondrial;
                     transcription termination factor 3, mitochondrial; MTERF
                     domain containing 1"
                     /calculated_mol_wt=39637
     transit_peptide 1..64
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q96E29; propagated from
                     UniProtKB/Swiss-Prot (Q6P6Q6.1)"
                     /calculated_mol_wt=7047
     mat_peptide     65..409
                     /product="Transcription termination factor 3,
                     mitochondrial. /id=PRO_0000255459"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6Q6.1)"
                     /calculated_mol_wt=39637
     Region          74..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6Q6.1)"
     Region          <145..390
                     /region_name="mTERF"
                     /note="pfam02536"
                     /db_xref="CDD:460581"
     CDS             1..409
                     /gene="Mterf3"
                     /gene_synonym="Cgi12; Mterfd1"
                     /coded_by="NM_199387.1:130..1359"
                     /db_xref="GeneID:299514"
                     /db_xref="RGD:735158"
ORIGIN      
        1 mallaqqlsr wfnsvklssf ikatqvtkhs aglgknasaq allssdtcfl qwgiktdral
       61 fswssfqsan ttrrksstns tllpsvseqp ekiprlesel pleelddlpp lsplqpvsee
      121 eaiqiaaysp lplssstlad yvdhsetlqk lvqlgvdlsk iekhpdvanl llrlnfekdi
      181 kqillflkdl glednqlgpf ltknyaifse dlenlktrva ylqsknfskt diacmvknap
      241 fllsfsverl dnrlgffqke lelsvkktrd lvvrlprllt gslepvkenm kvyrlelgfk
      301 hneiqhmvtk ipkmltankr kltetfdyvh nvmniphhii vkfpqvfntr vfkikerhlf
      361 laylgkaqyd pakpnyvsld kfvsfpdevf ckeiakasvn dfekflktl
//
LOCUS       NP_001007681             337 aa            linear   ROD 27-APR-2025
DEFINITION  monoacylglycerol lipase ABHD6 [Rattus norvegicus].
ACCESSION   NP_001007681 XP_223871
VERSION     NP_001007681.1
DBSOURCE    REFSEQ: accession NM_001007680.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Noguchi,K., Kadekawa,K., Nishijima,S., Sakanashi,M.,
            Okitsu-Sakurayama,S., Higa-Nakamine,S., Yamamoto,H. and Sugaya,K.
  TITLE     Phenotypic Characterization of the Endocannabinoid-Degrading Enzyme
            Alpha/Beta-Hydrolase Domain 6 Knockout Rat
  JOURNAL   Cannabis Cannabinoid Res 7 (2), 179-187 (2022)
   PUBMED   34468198
  REMARK    GeneRIF: Phenotypic Characterization of the
            Endocannabinoid-Degrading Enzyme Alpha/Beta-Hydrolase Domain 6
            Knockout Rat.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Zhao,S., Mugabo,Y., Ballentine,G., Attane,C., Iglesias,J.,
            Poursharifi,P., Zhang,D., Nguyen,T.A., Erb,H., Prentki,R.,
            Peyot,M.L., Joly,E., Tobin,S., Fulton,S., Brown,J.M., Madiraju,S.R.
            and Prentki,M.
  TITLE     alpha/beta-Hydrolase Domain 6 Deletion Induces Adipose Browning and
            Prevents Obesity and Type 2 Diabetes
  JOURNAL   Cell Rep 14 (12), 2872-2888 (2016)
   PUBMED   26997277
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Pribasnig,M.A., Mrak,I., Grabner,G.F., Taschler,U.,
            Knittelfelder,O., Scherz,B., Eichmann,T.O., Heier,C., Grumet,L.,
            Kowaliuk,J., Romauch,M., Holler,S., Anderl,F., Wolinski,H.,
            Lass,A., Breinbauer,R., Marsche,G., Brown,J.M. and Zimmermann,R.
  TITLE     alpha/beta Hydrolase Domain-containing 6 (ABHD6) Degrades the Late
            Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate
  JOURNAL   J Biol Chem 290 (50), 29869-29881 (2015)
   PUBMED   26491015
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Thomas,G., Betters,J.L., Lord,C.C., Brown,A.L., Marshall,S.,
            Ferguson,D., Sawyer,J., Davis,M.A., Melchior,J.T., Blume,L.C.,
            Howlett,A.C., Ivanova,P.T., Milne,S.B., Myers,D.S., Mrak,I.,
            Leber,V., Heier,C., Taschler,U., Blankman,J.L., Cravatt,B.F.,
            Lee,R.G., Crooke,R.M., Graham,M.J., Zimmermann,R., Brown,H.A. and
            Brown,J.M.
  TITLE     The serine hydrolase ABHD6 Is a critical regulator of the metabolic
            syndrome
  JOURNAL   Cell Rep 5 (2), 508-520 (2013)
   PUBMED   24095738
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Navia-Paldanius,D., Savinainen,J.R. and Laitinen,J.T.
  TITLE     Biochemical and pharmacological characterization of human
            alpha/beta-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12)
  JOURNAL   J Lipid Res 53 (11), 2413-2424 (2012)
   PUBMED   22969151
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Schwenk,J., Harmel,N., Brechet,A., Zolles,G., Berkefeld,H.,
            Muller,C.S., Bildl,W., Baehrens,D., Huber,B., Kulik,A., Klocker,N.,
            Schulte,U. and Fakler,B.
  TITLE     High-resolution proteomics unravel architecture and molecular
            diversity of native AMPA receptor complexes
  JOURNAL   Neuron 74 (4), 621-633 (2012)
   PUBMED   22632720
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Marrs,W.R., Blankman,J.L., Horne,E.A., Thomazeau,A., Lin,Y.H.,
            Coy,J., Bodor,A.L., Muccioli,G.G., Hu,S.S., Woodruff,G., Fung,S.,
            Lafourcade,M., Alexander,J.P., Long,J.Z., Li,W., Xu,C., Moller,T.,
            Mackie,K., Manzoni,O.J., Cravatt,B.F. and Stella,N.
  TITLE     The serine hydrolase ABHD6 controls the accumulation and efficacy
            of 2-AG at cannabinoid receptors
  JOURNAL   Nat Neurosci 13 (8), 951-957 (2010)
   PUBMED   20657592
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Blankman,J.L., Simon,G.M. and Cravatt,B.F.
  TITLE     A comprehensive profile of brain enzymes that hydrolyze the
            endocannabinoid 2-arachidonoylglycerol
  JOURNAL   Chem Biol 14 (12), 1347-1356 (2007)
   PUBMED   18096503
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083826.1.
            
            On Nov 29, 2004 this sequence version replaced XP_223871.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083826.1, SRR8487231.11565.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..337
                     /product="monoacylglycerol lipase ABHD6"
                     /EC_number="3.1.1.23"
                     /note="2-arachidonoylglycerol hydrolase; abhydrolase
                     domain-containing protein 6"
                     /calculated_mol_wt=38181
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI64.1)"
     Region          51..327
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     CDS             1..337
                     /gene="Abhd6"
                     /coded_by="NM_001007680.1:72..1085"
                     /db_xref="GeneID:305795"
                     /db_xref="RGD:1359323"
ORIGIN      
        1 mdldvvnmfv iaggtlaipi lafvasfllw psaliriyyw ywrrtlgmqv ryvhhedyqf
       61 cysfrgrpgh kpsvlmlhgf sahkdmwlsv vkflpknlhl vcvdmpgheg ttrsslddls
      121 ivgqvkrihq fveclklnkk pfhligtsmg gnvagvyaay ypsdvcslsl vcpaglqyst
      181 dnrfvqrlke ledsaatqki plipstpeem semlqlcsyv rfkvpqqilq glvdvriphn
      241 sfyrklflei vseksryslh enmdkikvpt qiiwgkqdqv ldvsgadila ksitnsqvev
      301 lencghsvvm erprktaklv vdflasvhnp dnnkkln
//
LOCUS       NP_113798                501 aa            linear   ROD 27-APR-2025
DEFINITION  G protein-activated inward rectifier potassium channel 1 [Rattus
            norvegicus].
ACCESSION   NP_113798
VERSION     NP_113798.1
DBSOURCE    REFSEQ: accession NM_031610.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Baculis,B.C., Weiss,A.C., Pang,W., Jeong,H.G., Lee,J.H., Liu,D.C.,
            Tsai,N.P. and Chung,H.J.
  TITLE     Prolonged seizure activity causes caspase dependent cleavage and
            dysfunction of G-protein activated inwardly rectifying potassium
            channels
  JOURNAL   Sci Rep 7 (1), 12313 (2017)
   PUBMED   28951616
  REMARK    GeneRIF: Study is first to show direct cleavage of GIRK1 and GIRK2
            subunits by caspase-3, with cleavage sites in GIRK1 (387ECLD390)
            and GIRK2 (349YEVD352) and suggests the possible role of caspase-3
            mediated down-regulation of GIRK channel function and expression in
            hippocampal neuronal injury during prolonged epileptic seizures.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Li,Y., Fu,X., Zhang,Z. and Yu,B.
  TITLE     Knockdown of cardiac Kir3.1 gene with siRNA can improve bradycardia
            in an experimental sinus bradycardia rat model
  JOURNAL   Mol Cell Biochem 429 (1-2), 103-111 (2017)
   PUBMED   28205094
  REMARK    GeneRIF: Study provides evidence that Kir3.1 is involved in the
            pathogenesis of sinus bradycardia since its ihibition with siRNA
            can reverse the sinus bradycardia.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Kramer,P.F. and Williams,J.T.
  TITLE     Calcium Release from Stores Inhibits GIRK
  JOURNAL   Cell Rep 17 (12), 3246-3255 (2016)
   PUBMED   28009293
  REMARK    GeneRIF: Transient activation of mGluRs decreased the GIRK current
            evoked by GABAB and D2 receptors, although less efficaciously for
            D2.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Montalbano,A., Corradetti,R. and Mlinar,B.
  TITLE     Pharmacological Characterization of 5-HT1A Autoreceptor-Coupled
            GIRK Channels in Rat Dorsal Raphe 5-HT Neurons
  JOURNAL   PLoS One 10 (10), e0140369 (2015)
   PUBMED   26460748
  REMARK    GeneRIF: inwardly rectifying K+ channels coupled to 5-HT1A
            autoreceptors display pharmacological properties generally expected
            for neuronal GIRK channels, but different from GIRK1-GIRK2
            heteromers
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Lyu,C., Mulder,J., Barde,S., Sahlholm,K., Zeberg,H., Nilsson,J.,
            Arhem,P., Hokfelt,T., Fried,K. and Shi,T.J.
  TITLE     G protein-gated inwardly rectifying potassium channel subunits 1
            and 2 are down-regulated in rat dorsal root ganglion neurons and
            spinal cord after peripheral axotomy
  JOURNAL   Mol Pain 11, 44 (2015)
   PUBMED   26199148
  REMARK    GeneRIF: Fourteen days after axotomy, GIRK1 and GIRK2 were
            down-regulated in DRG neurons at the mRNA and protein levels.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Karschin,C., Dissmann,E., Stuhmer,W. and Karschin,A.
  TITLE     IRK(1-3) and GIRK(1-4) inwardly rectifying K+ channel mRNAs are
            differentially expressed in the adult rat brain
  JOURNAL   J Neurosci 16 (11), 3559-3570 (1996)
   PUBMED   8642402
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Slesinger,P.A., Reuveny,E., Jan,Y.N. and Jan,L.Y.
  TITLE     Identification of structural elements involved in G protein gating
            of the GIRK1 potassium channel
  JOURNAL   Neuron 15 (5), 1145-1156 (1995)
   PUBMED   7576657
REFERENCE   8  (residues 1 to 501)
  AUTHORS   DePaoli,A.M., Bell,G.I. and Stoffel,M.
  TITLE     G protein-activated inwardly rectifying potassium channel
            (GIRK1/KGA) mRNA in adult rat heart and brain by in situ
            hybridization histochemistry
  JOURNAL   Mol Cell Neurosci 5 (6), 515-522 (1994)
   PUBMED   7704424
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Dascal,N., Schreibmayer,W., Lim,N.F., Wang,W., Chavkin,C.,
            DiMagno,L., Labarca,C., Kieffer,B.L., Gaveriaux-Ruff,C.,
            Trollinger,D. et al.
  TITLE     Atrial G protein-activated K+ channel: expression cloning and
            molecular properties
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10235-10239 (1993)
   PUBMED   8234283
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Kubo,Y., Reuveny,E., Slesinger,P.A., Jan,Y.N. and Jan,L.Y.
  TITLE     Primary structure and functional expression of a rat
            G-protein-coupled muscarinic potassium channel
  JOURNAL   Nature 364 (6440), 802-806 (1993)
   PUBMED   8355805
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L25264.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L25264.1, U09243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..501
                     /product="G protein-activated inward rectifier potassium
                     channel 1"
                     /note="KGA; KGB1; GIRK1; inward rectifier K(+) channel
                     Kir3.1; potassium channel, inwardly rectifying subfamily J
                     member 3; GIRK-1; potassium channel inwarding rectifying
                     channel subfamily J member 3; potassium channel subunit
                     Kir3.1 type 3 delta; potassium voltage-gated channel
                     subfamily J member 3"
                     /calculated_mol_wt=56442
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     Region          47..187
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            81..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P63251.1)"
     Region          143..148
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     Site            173
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P63251.1)"
     Region          182..209
                     /region_name="Polyphosphoinositide (PIP2)-binding.
                     /evidence=ECO:0000269|PubMed:9486652"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     Region          194..364
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63250; propagated from
                     UniProtKB/Swiss-Prot (P63251.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63250; propagated from
                     UniProtKB/Swiss-Prot (P63251.1)"
     Region          456..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63251.1)"
     CDS             1..501
                     /gene="Kcnj3"
                     /coded_by="NM_031610.3:59..1564"
                     /db_xref="GeneID:50599"
                     /db_xref="RGD:2958"
ORIGIN      
        1 msalrrkfgd dyqvvttsss gsglqpqgpg qgpqqqlvpk kkrqrfvdkn grcnvqhgnl
       61 gsetsrylsd lfttlvdlkw rwnlfifilt ytvawlfmas mwwviaytrg dlnkahvgny
      121 tpcvanvynf psaflffiet eatigygyry itdkcpegii lflfqsilgs ivdafligcm
      181 fikmsqpkkr aetlmfseha vismrdgklt lmfrvgnlrn shmvsaqirc kllksrqtpe
      241 geflpldqle ldvgfstgad qlflvsplti chvidakspf ydlsqrsmqt eqfevvvile
      301 givettgmtc qartsytede vlwghrffpv isleegffkv dysqfhatfe vptppysvke
      361 qeemllmssp liapaitnsk erhnsvecld glddistklp sklqkitgre dfpkkllrms
      421 sttsekaysl gdlpmklqri ssvpgnseek lvskttkmls dpmsqsvadl ppklqkmagg
      481 ptrmegnlpa klrkmnsdrf t
//
LOCUS       NP_001076009             304 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein D0 isoform c [Rattus
            norvegicus].
ACCESSION   NP_001076009
VERSION     NP_001076009.1
DBSOURCE    REFSEQ: accession NM_001082540.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Yan,J., Du,F., Li,S.D., Yuan,Y., Jiang,J.Y., Li,S., Li,X.Y. and
            Du,Z.X.
  TITLE     AUF1 modulates TGF-beta signal in renal tubular epithelial cells
            via post-transcriptional regulation of Nedd4L expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (1), 48-56 (2018)
   PUBMED   28986222
  REMARK    GeneRIF: AUF1 might be a potential player in renal
            tubulointerstitial fibrosis through modulation of TGF-beta signal
            transduction via posttranscriptional regulation of Nedd4L.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Castellanos-Rubio,A., Fernandez-Jimenez,N., Kratchmarov,R., Luo,X.,
            Bhagat,G., Green,P.H., Schneider,R., Kiledjian,M., Bilbao,J.R. and
            Ghosh,S.
  TITLE     A long noncoding RNA associated with susceptibility to celiac
            disease
  JOURNAL   Science 352 (6281), 91-95 (2016)
   PUBMED   27034373
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Lee,K.H., Kim,S.H., Kim,H.J., Kim,W., Lee,H.R., Jung,Y., Choi,J.H.,
            Hong,K.Y., Jang,S.K. and Kim,K.T.
  TITLE     AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
            translation
  JOURNAL   Nucleic Acids Res 42 (6), 3590-3606 (2014)
   PUBMED   24423872
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Raineri,I., Wegmueller,D., Gross,B., Certa,U. and Moroni,C.
  TITLE     Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover
            studied by RNA interference
  JOURNAL   Nucleic Acids Res 32 (4), 1279-1288 (2004)
   PUBMED   14976220
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Arao,Y., Kikuchi,A., Ikeda,K., Nomoto,S., Horiguchi,H. and
            Kayama,F.
  TITLE     A+U-rich-element RNA-binding factor 1/heterogeneous nuclear
            ribonucleoprotein D gene expression is regulated by oestrogen in
            the rat uterus
  JOURNAL   Biochem J 361 (Pt 1), 125-132 (2002)
   PUBMED   11742537
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Ehrenman,K., Long,L., Wagner,B.J. and Brewer,G.
  TITLE     Characterization of cDNAs encoding the murine A+U-rich RNA-binding
            protein AUF1
  JOURNAL   Gene 149 (2), 315-319 (1994)
   PUBMED   7959009
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Ishikawa,F., Matunis,M.J., Dreyfuss,G. and Cech,T.R.
  TITLE     Nuclear proteins that bind the pre-mRNA 3' splice site sequence
            r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
  JOURNAL   Mol Cell Biol 13 (7), 4301-4310 (1993)
   PUBMED   8321232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO567918.1, AB046617.1 and CB798484.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB046617.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..304
                     /product="heterogeneous nuclear ribonucleoprotein D0
                     isoform c"
                     /note="heterogeneous nuclear ribonucleoprotein D0; hnRNP
                     D0; AU-rich element RNA-binding protein 1; AU-rich element
                     RNA-binding factor 1; RNA binding protein p45AUF1"
                     /calculated_mol_wt=32541
     Region          <55..76
                     /region_name="CBFNT"
                     /note="CBFNT (NUC161) domain; pfam08143"
                     /db_xref="CDD:311868"
     Region          97..170
                     /region_name="RRM1_hnRNPD"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12756"
                     /db_xref="CDD:410150"
     Region          181..255
                     /region_name="RRM2_hnRNPD"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12583"
                     /db_xref="CDD:241027"
     Site            order(181,183,185..186,210..213,215..216,219..221,223,225,
                     242,249..251,253..255)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:241027"
     CDS             1..304
                     /gene="Hnrnpd"
                     /gene_synonym="Auf1; Hnrpd"
                     /coded_by="NM_001082540.1:286..1200"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:79256"
                     /db_xref="RGD:620365"
ORIGIN      
        1 mseeqfggdg aaaaataavg gsageqegam vaaaqgaaaa agsgsgggsa pggteggste
       61 aegakidask needeghsns sprhteaata qreewkmfig glswdttkkd lkdyfskfgd
      121 vvdctlkldp itgrsrgfgf vlfkesesvd kvmdqkehkl ngkvidpkra kamktkepvk
      181 kifvgglspd tpeekireyf ggfgevesie lpmdnktnkr rgfcfitfke eepvkkimek
      241 kyhnvglskc eikvamskeq yqqqqqwgsr ggfagrargr ggdqqsgygk vsrrgghqns
      301 ykpy
//
LOCUS       NP_001017490             262 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 81 precursor [Rattus norvegicus].
ACCESSION   NP_001017490 XP_573449
VERSION     NP_001017490.1
DBSOURCE    REFSEQ: accession NM_001017490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079284.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573449.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079284.1, CK469549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..262
                     /product="transmembrane protein 81 precursor"
                     /calculated_mol_wt=25754
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW8.1)"
                     /calculated_mol_wt=3150
     mat_peptide     31..262
                     /product="Transmembrane protein 81. /id=PRO_0000287878"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW8.1)"
                     /calculated_mol_wt=25754
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW8.1)"
     Region          100..163
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          100..104
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          118..122
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          143..147
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..162
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW8.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW8.1)"
     CDS             1..262
                     /gene="Tmem81"
                     /coded_by="NM_001017490.1:422..1210"
                     /db_xref="GeneID:498229"
                     /db_xref="RGD:1561544"
ORIGIN      
        1 mkavatvfic gslvlitylp lvvtspqtla ipeklrqavg rvvvnatacs vtcglgykee
       61 tscevgpdgv rrdcrsqrle cltnwicgml hftiiqrqqf elnclssdil tkgqeafrft
      121 wklargiist ndelfkpfra nspflrfkpa yesdsgtyrc dvqqlknlkl vkrlyfglrv
      181 lppklvnlnf qqsltedqkl aeegwevhld nqsqphlpgw rkkvslalgv giaagvvggv
      241 lvnvalcrvl ggtggngnls sl
//
LOCUS       NP_113765                104 aa            linear   ROD 27-APR-2025
DEFINITION  somatoliberin precursor [Rattus norvegicus].
ACCESSION   NP_113765
VERSION     NP_113765.1
DBSOURCE    REFSEQ: accession NM_031577.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Sapkota,S., Haider Ali,M., Alshamrani,A.A., Napit,P.R., Roy,S.C.,
            Pasula,M.B. and Briski,K.P.
  TITLE     GHRH Neurons from the Ventromedial Hypothalamic Nucleus Provide
            Dynamic and Sex-Specific Input to the Brain Glucose-Regulatory
            Network
  JOURNAL   Neuroscience 529, 73-87 (2023)
   PUBMED   37572878
  REMARK    GeneRIF: GHRH Neurons from the Ventromedial Hypothalamic Nucleus
            Provide Dynamic and Sex-Specific Input to the Brain
            Glucose-Regulatory Network.
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Kiscsatari,L., Varga,Z., Schally,A.V., Gaspar,R., Nagy,C.T.,
            Giricz,Z., Ferdinandy,P., Fabian,G., Kahan,Z. and Gorbe,A.
  TITLE     Protection of neonatal rat cardiac myocytes against
            radiation-induced damage with agonists of growth hormone-releasing
            hormone
  JOURNAL   Pharmacol Res 111, 859-866 (2016)
   PUBMED   27480202
  REMARK    GeneRIF: GHRH agonistic analogs, JI-34 and MR-356 alleviated
            radiation-induced damage of cardiac myocytes.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Romero,M.J., Lucas,R., Dou,H., Sridhar,S., Czikora,I.,
            Mosieri,E.M., Rick,F.G., Block,N.L., Sridhar,S., Fulton,D.,
            Weintraub,N.L., Bagi,Z. and Schally,A.V.
  TITLE     Role of growth hormone-releasing hormone in dyslipidemia associated
            with experimental type 1 diabetes
  JOURNAL   Proc Natl Acad Sci U S A 113 (7), 1895-1900 (2016)
   PUBMED   26831066
  REMARK    GeneRIF: findings support the hypothesis that antagonizing the
            signaling of GHRH in T1D may improve GLP-1 function in the small
            intestine, which, in turn, diminishes TRL and reduces renal and
            vascular complications
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Cai,R., Schally,A.V., Cui,T., Szalontay,L., Halmos,G., Sha,W.,
            Kovacs,M., Jaszberenyi,M., He,J., Rick,F.G., Popovics,P.,
            Kanashiro-Takeuchi,R., Hare,J.M., Block,N.L. and Zarandi,M.
  TITLE     Synthesis of new potent agonistic analogs of growth
            hormone-releasing hormone (GHRH) and evaluation of their endocrine
            and cardiac activities
  JOURNAL   Peptides 52, 104-112 (2014)
   PUBMED   24373935
  REMARK    GeneRIF: JI-38 had shown promising results in multiple fields
            including cardiology, diabetes and wound healing, our new, more
            potent, GHRH agonists should manifest additional efficacy for
            possible medical applications.
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Leggett,J., Harper,E., Waite,E., Marks,P., Martinez,A. and
            Lightman,S.
  TITLE     GHRH receptor-targeted botulinum neurotoxin selectively inhibits
            pulsatile GH secretion in male rats
  JOURNAL   Endocrinology 154 (9), 3305-3318 (2013)
   PUBMED   23825127
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Lin,C., Lin,S.C., Chang,C.P. and Rosenfeld,M.G.
  TITLE     Pit-1-dependent expression of the receptor for growth hormone
            releasing factor mediates pituitary cell growth
  JOURNAL   Nature 360 (6406), 765-768 (1992)
   PUBMED   1334535
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Asa,S.L., Kovacs,K., Stefaneanu,L., Horvath,E., Billestrup,N.,
            Gonzalez-Manchon,C. and Vale,W.
  TITLE     Pituitary adenomas in mice transgenic for growth hormone-releasing
            hormone
  JOURNAL   Endocrinology 131 (5), 2083-2089 (1992)
   PUBMED   1425411
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Mayo,K.E.
  TITLE     Molecular cloning and expression of a pituitary-specific receptor
            for growth hormone-releasing hormone
  JOURNAL   Mol Endocrinol 6 (10), 1734-1744 (1992)
   PUBMED   1333056
REFERENCE   9  (residues 1 to 104)
  AUTHORS   Bagnato,A., Moretti,C., Ohnishi,J., Frajese,G. and Catt,K.J.
  TITLE     Expression of the growth hormone-releasing hormone gene and its
            peptide product in the rat ovary
  JOURNAL   Endocrinology 130 (3), 1097-1102 (1992)
   PUBMED   1537276
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Gonzalez-Crespo,S. and Boronat,A.
  TITLE     Expression of the rat growth hormone-releasing hormone gene in
            placenta is directed by an alternative promoter
  JOURNAL   Proc Natl Acad Sci U S A 88 (19), 8749-8753 (1991)
   PUBMED   1924334
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M73486.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M73486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..104
                     /product="somatoliberin precursor"
                     /note="somatoliberin; GRF; growth hormone-releasing
                     factor"
                     /calculated_mol_wt=10233
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2052
     mat_peptide     31..73
                     /product="Somatoliberin. /id=PRO_0000011448"
                     /note="propagated from UniProtKB/Swiss-Prot (P09916.2)"
                     /calculated_mol_wt=5233
     Region          31..58
                     /region_name="Hormone_2"
                     /note="Peptide hormone; pfam00123"
                     /db_xref="CDD:459681"
     CDS             1..104
                     /gene="Ghrh"
                     /gene_synonym="GHRF"
                     /coded_by="NM_031577.1:196..510"
                     /db_xref="GeneID:29446"
                     /db_xref="RGD:61883"
ORIGIN      
        1 mplwvffvll tltsgshcsl ppsppfrvrr hadaiftssy rrilgqlyar kllheimnrq
       61 qgernqeqrs rfnrhldrvw aedkqmales ilqgfprmkl saea
//
LOCUS       NP_001100218             125 aa            linear   ROD 27-APR-2025
DEFINITION  basic leucine zipper transcriptional factor ATF-like [Rattus
            norvegicus].
ACCESSION   NP_001100218 XP_001057854 XP_216745
VERSION     NP_001100218.1
DBSOURCE    REFSEQ: accession NM_001106748.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Chen,L.Y., Fan,X.P., Fan,Y.C., Zhao,J., Gao,S., Li,F., Qi,Z.X. and
            Wang,K.
  TITLE     BATF Interference Blocks Th17 Cell Differentiation and Inflammatory
            Response in Hepatitis B Virus Transgenic Mice
  JOURNAL   Dig Dis Sci 64 (3), 773-780 (2019)
   PUBMED   30498928
  REMARK    GeneRIF: Hepatitis B virus markedly upregulated hepatic BATF
            expression and promoted Th17 cell activation.
REFERENCE   2  (residues 1 to 125)
  AUTHORS   He,L., Peng,X., Chen,Y., Liu,G., Liu,Z., Zhu,J., Liu,Y., Liu,H.,
            Liang,Y., Liu,F., Sun,L. and Peng,Y.
  TITLE     Regulation of IgA Class Switch Recombination in Immunoglobulin A
            Nephropathy: Retinoic Acid Signaling and BATF
  JOURNAL   Am J Nephrol 43 (3), 179-194 (2016)
   PUBMED   27073891
  REMARK    GeneRIF: upregulated in blood, spleen, and bone marrow in IgA
            nephropathy
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Glasmacher,E., Agrawal,S., Chang,A.B., Murphy,T.L., Zeng,W., Vander
            Lugt,B., Khan,A.A., Ciofani,M., Spooner,C.J., Rutz,S., Hackney,J.,
            Nurieva,R., Escalante,C.R., Ouyang,W., Littman,D.R., Murphy,K.M.
            and Singh,H.
  TITLE     A genomic regulatory element that directs assembly and function of
            immune-specific AP-1-IRF complexes
  JOURNAL   Science 338 (6109), 975-980 (2012)
   PUBMED   22983707
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Tussiwand,R., Lee,W.L., Murphy,T.L., Mashayekhi,M., KC,W.,
            Albring,J.C., Satpathy,A.T., Rotondo,J.A., Edelson,B.T.,
            Kretzer,N.M., Wu,X., Weiss,L.A., Glasmacher,E., Li,P., Liao,W.,
            Behnke,M., Lam,S.S., Aurthur,C.T., Leonard,W.J., Singh,H.,
            Stallings,C.L., Sibley,L.D., Schreiber,R.D. and Murphy,K.M.
  TITLE     Compensatory dendritic cell development mediated by BATF-IRF
            interactions
  JOURNAL   Nature 490 (7421), 502-507 (2012)
   PUBMED   22992524
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Li,P., Spolski,R., Liao,W., Wang,L., Murphy,T.L., Murphy,K.M. and
            Leonard,W.J.
  TITLE     BATF-JUN is critical for IRF4-mediated transcription in T cells
  JOURNAL   Nature 490 (7421), 543-546 (2012)
   PUBMED   22992523
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Wang,J., Sun,Q., Morita,Y., Jiang,H., Gross,A., Lechel,A.,
            Hildner,K., Guachalla,L.M., Gompf,A., Hartmann,D., Schambach,A.,
            Wuestefeld,T., Dauch,D., Schrezenmeier,H., Hofmann,W.K.,
            Nakauchi,H., Ju,Z., Kestler,H.A., Zender,L. and Rudolph,K.L.
  TITLE     A differentiation checkpoint limits hematopoietic stem cell
            self-renewal in response to DNA damage
  JOURNAL   Cell 148 (5), 1001-1014 (2012)
   PUBMED   22385964
  REMARK    Erratum:[Cell. 2014 Sep 11;158(6):1444]
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Ise,W., Kohyama,M., Schraml,B.U., Zhang,T., Schwer,B., Basu,U.,
            Alt,F.W., Tang,J., Oltz,E.M., Murphy,T.L. and Murphy,K.M.
  TITLE     The transcription factor BATF controls the global regulators of
            class-switch recombination in both B cells and T cells
  JOURNAL   Nat Immunol 12 (6), 536-543 (2011)
   PUBMED   21572431
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Betz,B.C., Jordan-Williams,K.L., Wang,C., Kang,S.G., Liao,J.,
            Logan,M.R., Kim,C.H. and Taparowsky,E.J.
  TITLE     Batf coordinates multiple aspects of B and T cell function required
            for normal antibody responses
  JOURNAL   J Exp Med 207 (5), 933-942 (2010)
   PUBMED   20421391
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Schraml,B.U., Hildner,K., Ise,W., Lee,W.L., Smith,W.A., Solomon,B.,
            Sahota,G., Sim,J., Mukasa,R., Cemerski,S., Hatton,R.D.,
            Stormo,G.D., Weaver,C.T., Russell,J.H., Murphy,T.L. and Murphy,K.M.
  TITLE     The AP-1 transcription factor Batf controls T(H)17 differentiation
  JOURNAL   Nature 460 (7253), 405-409 (2009)
   PUBMED   19578362
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Kuwamura,M., Maeda,M., Kuramoto,T., Kitada,K., Kanehara,T.,
            Moriyama,M., Nakane,Y., Yamate,J., Ushijima,T., Kotani,T. and
            Serikawa,T.
  TITLE     The myelin vacuolation (mv) rat with a null mutation in the
            attractin gene
  JOURNAL   Lab Invest 82 (10), 1279-1286 (2002)
   PUBMED   12379762
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473982.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001057854.1, XP_216745.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760396,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..125
                     /product="basic leucine zipper transcriptional factor
                     ATF-like"
                     /note="B-cell-activating transcription factor; basic
                     leucine zipper transcription factor, ATF-like"
                     /calculated_mol_wt=13933
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7E1.1)"
     Region          26..83
                     /region_name="bZIP_BATF"
                     /note="Basic leucine zipper (bZIP) domain of BATF
                     proteins: a DNA-binding and dimerization domain; cd14701"
                     /db_xref="CDD:269849"
     Region          28..82
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269849"
     Region          28..50
                     /region_name="Basic motif"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7E1.1)"
     Site            order(32..33,35..37,39..44,46..48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269849"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35284; propagated from
                     UniProtKB/Swiss-Prot (D4A7E1.1)"
     Site            order(47,50..51,54..55,57..58,61..62,64..65,68..69,71..72,
                     75..76,78..79)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269849"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O35284; propagated from
                     UniProtKB/Swiss-Prot (D4A7E1.1)"
     Region          54..75
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A7E1.1)"
     CDS             1..125
                     /gene="Batf"
                     /gene_synonym="B-ATF"
                     /coded_by="NM_001106748.1:236..613"
                     /db_xref="GeneID:299206"
                     /db_xref="RGD:1304923"
ORIGIN      
        1 mphssdssds sfsrspppgk qdssddvrkv qrreknriaa qksrqrqtqk adtlhlesed
       61 lekqnaalrk eikqlteelk yftsvlsshe plcsvlasgt psppevvysa hafhqphiss
      121 prfqp
//
LOCUS       NP_604453                217 aa            linear   ROD 27-APR-2025
DEFINITION  homologous-pairing protein 2 homolog [Rattus norvegicus].
ACCESSION   NP_604453
VERSION     NP_604453.2
DBSOURCE    REFSEQ: accession NM_134458.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Zangen,D., Kaufman,Y., Zeligson,S., Perlberg,S., Fridman,H.,
            Kanaan,M., Abdulhadi-Atwan,M., Abu Libdeh,A., Gussow,A.,
            Kisslov,I., Carmel,L., Renbaum,P. and Levy-Lahad,E.
  TITLE     XX ovarian dysgenesis is caused by a PSMC3IP/HOP2 mutation that
            abolishes coactivation of estrogen-driven transcription
  JOURNAL   Am J Hum Genet 89 (4), 572-579 (2011)
   PUBMED   21963259
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Ko,L., Cardona,G.R., Henrion-Caude,A. and Chin,W.W.
  TITLE     Identification and characterization of a tissue-specific
            coactivator, GT198, that interacts with the DNA-binding domains of
            nuclear receptors
  JOURNAL   Mol Cell Biol 22 (1), 357-369 (2002)
   PUBMED   11739747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF352812.1 and CK840952.1.
            
            On Oct 13, 2005 this sequence version replaced NP_604453.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF352812.1, SRR8487227.291632.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..217
                     /product="homologous-pairing protein 2 homolog"
                     /note="proteasome 26S ATPase subunit 3-interacting
                     protein; proteasome (prosome, macropain) 26S subunit,
                     ATPase 3, interacting protein; nuclear receptor
                     coactivator GT198"
                     /calculated_mol_wt=24638
     Region          11..74
                     /region_name="TBPIP"
                     /note="TBPIP/Hop2 winged helix domain; pfam07106"
                     /db_xref="CDD:429296"
     Region          89..117
                     /region_name="Interaction with NR3C1, homodimerization and
                     transcriptional activation almost abolished when missing.
                     /evidence=ECO:0000269|PubMed:11739747"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZY6.1)"
     Region          118..182
                     /region_name="DNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZY6.1)"
     Region          118..182
                     /region_name="Interaction with NR3C1 decreased when
                     missing"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZY6.1)"
     Region          154..210
                     /region_name="LZ3wCH"
                     /note="Leucine zipper with capping helix domain;
                     pfam18517"
                     /db_xref="CDD:465789"
     CDS             1..217
                     /gene="Psmc3ip"
                     /gene_synonym="Gt198; Tbpip"
                     /coded_by="NM_134458.2:23..676"
                     /db_xref="GeneID:140938"
                     /db_xref="RGD:621885"
ORIGIN      
        1 msksraeaaa gapgivlryl qeqnrpysaq dvfgnlqkeh glgkaavvka ldqlaqqgki
       61 kektygkqki yfadqdqfdt vsdadlhsld asimaltakv qglqqscrhm eaelkeltsa
      121 lttpemqtei qelkkecary terlknikaa tnhvtpeeke kvyrerqkyc kewrkrkrmt
      181 telcdaileg ypkskkqffe evgietdedh nvtlpdp
//
LOCUS       NP_001104587             949 aa            linear   ROD 27-APR-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001104587
VERSION     NP_001104587.1
DBSOURCE    REFSEQ: accession NM_001111117.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Jack,A., Hamad,M.I.K., Gonda,S., Gralla,S., Pahl,S., Hollmann,M.
            and Wahle,P.
  TITLE     Development of Cortical Pyramidal Cell and Interneuronal Dendrites:
            a Role for Kainate Receptor Subunits and NETO1
  JOURNAL   Mol Neurobiol 56 (7), 4960-4979 (2019)
   PUBMED   30421168
  REMARK    GeneRIF: Gluk1 and NETO1 specifically promote dendrite growth of
            interneurons in the visual cortex.
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Duan,G.F., Ye,Y., Xu,S., Tao,W., Zhao,S., Jin,T., Nicoll,R.A.,
            Shi,Y.S. and Sheng,N.
  TITLE     Signal peptide represses GluK1 surface and synaptic trafficking
            through binding to amino-terminal domain
  JOURNAL   Nat Commun 9 (1), 4879 (2018)
   PUBMED   30451858
  REMARK    GeneRIF: Signal peptide represses GluK1 surface and synaptic
            trafficking through binding to amino-terminal domain.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 949)
  AUTHORS   Sheng,N., Shi,Y.S. and Nicoll,R.A.
  TITLE     Amino-terminal domains of kainate receptors determine the
            differential dependence on Neto auxiliary subunits for trafficking
  JOURNAL   Proc Natl Acad Sci U S A 114 (5), 1159-1164 (2017)
   PUBMED   28100490
  REMARK    GeneRIF: In the CA1 hippocampal pyramidal cell, GluK1 had no effect
            on synaptic transmission. GluK1 which requires the auxiliary
            subunits Neto1 and Neto2 for surface and synaptic trafficking. It
            is the amino-terminal domains of GluK1 and GluK2 that control their
            strikingly different trafficking properties.
REFERENCE   5  (residues 1 to 949)
  AUTHORS   Fisher,M.T. and Fisher,J.L.
  TITLE     Contributions of different kainate receptor subunits to the
            properties of recombinant homomeric and heteromeric receptors
  JOURNAL   Neuroscience 278, 70-80 (2014)
   PUBMED   25139762
REFERENCE   6  (residues 1 to 949)
  AUTHORS   Sailer,A., Swanson,G.T., Perez-Otano,I., O'Leary,L., Malkmus,S.A.,
            Dyck,R.H., Dickinson-Anson,H., Schiffer,H.H., Maron,C., Yaksh,T.L.,
            Gage,F.H., O'Gorman,S. and Heinemann,S.F.
  TITLE     Generation and analysis of GluR5(Q636R) kainate receptor mutant
            mice
  JOURNAL   J Neurosci 19 (20), 8757-8764 (1999)
   PUBMED   10516295
REFERENCE   7  (residues 1 to 949)
  AUTHORS   Brakeman,P.R., Lanahan,A.A., O'Brien,R., Roche,K., Barnes,C.A.,
            Huganir,R.L. and Worley,P.F.
  TITLE     Homer: a protein that selectively binds metabotropic glutamate
            receptors
  JOURNAL   Nature 386 (6622), 284-288 (1997)
   PUBMED   9069287
REFERENCE   8  (residues 1 to 949)
  AUTHORS   Lomeli,H., Wisden,W., Kohler,M., Keinanen,K., Sommer,B. and
            Seeburg,P.H.
  TITLE     High-affinity kainate and domoate receptors in rat brain
  JOURNAL   FEBS Lett 307 (2), 139-143 (1992)
   PUBMED   1322826
REFERENCE   9  (residues 1 to 949)
  AUTHORS   Sommer,B., Burnashev,N., Verdoorn,T.A., Keinanen,K., Sakmann,B. and
            Seeburg,P.H.
  TITLE     A glutamate receptor channel with high affinity for domoate and
            kainate
  JOURNAL   EMBO J 11 (4), 1651-1656 (1992)
   PUBMED   1373382
REFERENCE   10 (residues 1 to 949)
  AUTHORS   Bettler,B., Boulter,J., Hermans-Borgmeyer,I., O'Shea-Greenfield,A.,
            Deneris,E.S., Moll,C., Borgmeyer,U., Hollmann,M. and Heinemann,S.
  TITLE     Cloning of a novel glutamate receptor subunit, GluR5: expression in
            the nervous system during development
  JOURNAL   Neuron 5 (5), 583-595 (1990)
   PUBMED   1977421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M83560.1, Z11714.1,
            JAXUCZ010000011.1 and AI145540.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). RNA editing (CAG->CGG) changes Gln636Arg.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z11714.1, SRR26360176.2329989.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 10516295
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..949
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     1 precursor"
                     /note="glutamate receptor 5; glutamate receptor
                     ionotropic, kainate 1"
                     /calculated_mol_wt=104381
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
                     /calculated_mol_wt=3617
     mat_peptide     31..949
                     /product="Glutamate receptor ionotropic, kainate 1.
                     /id=PRO_0000011543"
                     /note="propagated from UniProtKB/Swiss-Prot (P22756.3)"
                     /calculated_mol_wt=104381
     Region          38..431
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Region          446..815
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            446
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            561
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            577..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22756.3)"
     Site            654..674
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22756.3)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P22756.3)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P22756.3)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22756.3)"
     Site            835..855
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22756.3)"
     CDS             1..949
                     /gene="Grik1"
                     /gene_synonym="GluK1; GluR5"
                     /coded_by="NM_001111117.1:186..3035"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29559"
                     /db_xref="RGD:2732"
ORIGIN      
        1 merstvliqp glwtrdtswt llyflcyilp qtspqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dsrdlfyinl ypdyaaisra vldlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlppank dakpllkemk kskefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltgritfnk tdglrkdfdl diislkeegt ekasgevskh lykvwkkigi
      421 wnsnsglnmt dgnrdrsnni tdslanrtli vttileepyv myrksdkply gndrfegycl
      481 dllkelsnil gflydvklvp dgkygaqndk gewngmvkel idhradlava pltityvrek
      541 vidfskpfmt lgisilyrkp ngtnpgvfsf lnplspdiwm yvllaclgvs cvlfviarft
      601 pyewynphpc npdsdvvenn ftllnsfwfg vgalmqqgse lmpkalstri vggiwwfftl
      661 iiissytanl aafltverme spidsaddla kqtkieygav rdgstmtffk kskistyekm
      721 wafmssrqqs alvknsdegi qrvlttdyal lmestsieyv tqrncnltqi gglidskgyg
      781 vgtpigspyr dkitiailql qeegklhmmk ekwwrgngcp eedskeasal gveniggifi
      841 vlaaglvlsv fvaigeflyk srknndveqk gkssrlrfyf rnkvrfhgsk keslgvekcl
      901 sfnaimeelg islknqkklk kksrtkgkss ftsiltchqr rtqrketva
//
LOCUS       NP_001012221             520 aa            linear   ROD 27-APR-2025
DEFINITION  succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial
            precursor [Rattus norvegicus].
ACCESSION   NP_001012221 XP_345578
VERSION     NP_001012221.1
DBSOURCE    REFSEQ: accession NM_001012221.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Bregere,C., Rebrin,I., Gallaher,T.K. and Sohal,R.S.
  TITLE     Effects of age and calorie restriction on tryptophan nitration,
            protein content, and activity of succinyl-CoA:3-ketoacid CoA
            transferase in rat kidney mitochondria
  JOURNAL   Free Radic Biol Med 48 (4), 609-618 (2010)
   PUBMED   20025965
  REMARK    GeneRIF: succinyl-CoA:3-ketoacid CoA transferase in rat kidney
            mitochondria is affected by age and caloric restriction
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Tanaka,H., Kohroki,J., Iguchi,N., Onishi,M. and Nishimune,Y.
  TITLE     Cloning and characterization of a human orthologue of
            testis-specific succinyl CoA: 3-oxo acid CoA transferase (Scot-t)
            cDNA
  JOURNAL   Mol Hum Reprod 8 (1), 16-23 (2002)
   PUBMED   11756565
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Koga,M., Tanaka,H., Yomogida,K., Nozaki,M., Tsuchida,J., Ohta,H.,
            Nakamura,Y., Masai,K., Yoshimura,Y., Yamanaka,M., Iguchi,N.,
            Nojima,H., Matsumiya,K., Okuyama,A. and Nishimune,Y.
  TITLE     Isolation and characterization of a haploid germ cell-specific
            novel complementary deoxyribonucleic acid; testis-specific
            homologue of succinyl CoA:3-Oxo acid CoA transferase
  JOURNAL   Biol Reprod 63 (6), 1601-1609 (2000)
   PUBMED   11090426
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083681.1.
            
            On Feb 11, 2005 this sequence version replaced XP_345578.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC083681.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..520
                     /product="succinyl-CoA:3-ketoacid coenzyme A transferase
                     2A, mitochondrial precursor"
                     /EC_number="2.8.3.5"
                     /note="3-oxoacid CoA-transferase 2A; testis-specific
                     succinyl-CoA:3-oxoacid CoA-transferase 1;
                     succinyl-CoA:3-ketoacid coenzyme A transferase 2A,
                     mitochondrial; rCG31267-like"
                     /calculated_mol_wt=52371
     transit_peptide 1..39
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q5XIJ9.1)"
                     /calculated_mol_wt=4547
     mat_peptide     40..520
                     /product="Succinyl-CoA:3-ketoacid coenzyme A transferase
                     2A, mitochondrial. /id=PRO_0000366210"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIJ9.1)"
                     /calculated_mol_wt=52371
     Region          41..279
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
     Region          280..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIJ9.1)"
     Region          300..506
                     /region_name="SugarP_isomerase"
                     /note="Sugar Phosphate Isomerase family; includes type A
                     ribose 5-phosphate isomerase (RPI_A),
                     glucosamine-6-phosphate (GlcN6P) deaminase, and
                     6-phosphogluconolactonase (6PGL). RPI catalyzes the
                     reversible conversion of ribose-5-phosphate to
                     ribulose...; cl00339"
                     /db_xref="CDD:469729"
     CDS             1..520
                     /gene="Oxct2b"
                     /gene_synonym="Oxct2a; SCOT-t1"
                     /coded_by="NM_001012221.1:39..1601"
                     /db_xref="GeneID:366463"
                     /db_xref="RGD:1306953"
ORIGIN      
        1 maalrllawa fsrrvsahrp qptlphhlir hypttrcgkv kfytdpvkav egikdgasvm
       61 lggfglcgip enligalktk gvkdlkiiss nvgvddfglg illaskqvrr vvcsylgenk
      121 lceqlylagk lelemtpqgt laeriraggt gvpafytptg ygtqvqeggv piryspeghl
      181 itlsqprevr efegqhhlle rairadfali kgwkadrsgn vifrgsarnf nvpmckaadi
      241 svveveeivd vgtfapedih ipniyvkrvi kgprfekrie rlttrdsppa pgskdqdpkr
      301 triikraale fkdgmyanlg igipvlasny ispkmtvylh sengilglgp fplkkevdpd
      361 iinagkqtvt vipggcffas ddsfamirgg hiqltmlgam qvskygdlan wmvpgkkvkg
      421 mggamdlvss kktkvvvtme hctktkqpki lekctmpltg kscvdliite kavfevdrsk
      481 glklvelweg ssldevkatt gcsfkvcpnl kpmqqiksda
//
LOCUS       NP_113909                480 aa            linear   ROD 27-APR-2025
DEFINITION  serine protease HTRA1 precursor [Rattus norvegicus].
ACCESSION   NP_113909
VERSION     NP_113909.1
DBSOURCE    REFSEQ: accession NM_031721.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Tavarna,T., Wolfe,B., Wu,X.J. and Reyes,L.
  TITLE     Porphyromonas gingivalis-mediated disruption in spiral artery
            remodeling is associated with altered uterine NK cell populations
            and dysregulated IL-18 and Htra1
  JOURNAL   Sci Rep 12 (1), 14799 (2022)
   PUBMED   36042379
  REMARK    GeneRIF: Porphyromonas gingivalis-mediated disruption in spiral
            artery remodeling is associated with altered uterine NK cell
            populations and dysregulated IL-18 and Htra1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Wang,W., Zhao,M., Cui,L., Ren,Y., Zhang,J., Chen,J., Jia,L.,
            Zhang,J., Yang,J., Chen,G., Ashby,C.R. Jr., Wu,C., Chen,Z.S. and
            Wang,L.
  TITLE     Characterization of a novel HDAC/RXR/HtrA1 signaling axis as a
            novel target to overcome cisplatin resistance in human non-small
            cell lung cancer
  JOURNAL   Mol Cancer 19 (1), 134 (2020)
   PUBMED   32878625
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Zurawa-Janicka,D., Kobiela,J., Slebioda,T., Peksa,R.,
            Stanislawowski,M., Wierzbicki,P.M., Wenta,T., Lipinska,B.,
            Kmiec,Z., Biernat,W., Lachinski,A.J. and Sledzinski,Z.
  TITLE     Expression of HTRA Genes and Its Association with Microsatellite
            Instability and Survival of Patients with Colorectal Cancer
  JOURNAL   Int J Mol Sci 21 (11), 3947 (2020)
   PUBMED   32486357
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Yao,Y. and Li,N.
  TITLE     Effect of HtrA1 Polymorphism on Sensitivity to Chemotherapy in
            Patients with Colon Cancer
  JOURNAL   Med Sci Monit 26, e921933 (2020)
   PUBMED   32218415
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Xiong,Z., Fu,Z., Shi,J., Jiang,X. and Wan,H.
  TITLE     HtrA1 Down-regulation Induces Cisplatin Resistance in Colon Cancer
            by Increasing XIAP and Activating PI3K/Akt Pathway
  JOURNAL   Ann Clin Lab Sci 47 (3), 264-270 (2017)
   PUBMED   28667026
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Cameron,D.J., Yang,Z., Gibbs,D., Chen,H., Kaminoh,Y., Jorgensen,A.,
            Zeng,J., Luo,L., Brinton,E., Brinton,G., Brand,J.M.,
            Bernstein,P.S., Zabriskie,N.A., Tang,S., Constantine,R., Tong,Z.
            and Zhang,K.
  TITLE     HTRA1 variant confers similar risks to geographic atrophy and
            neovascular age-related macular degeneration
  JOURNAL   Cell Cycle 6 (9), 1122-1125 (2007)
   PUBMED   17426452
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Sheng,J., Organ,E.L., Hao,C., Wells,K.S., Ruley,H.E. and Rubin,D.H.
  TITLE     Mutations in the IGF-II pathway that confer resistance to lytic
            reovirus infection
  JOURNAL   BMC Cell Biol 5, 32 (2004)
   PUBMED   15333144
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Tocharus,J., Tsuchiya,A., Kajikawa,M., Ueta,Y., Oka,C. and
            Kawaichi,M.
  TITLE     Developmentally regulated expression of mouse HtrA3 and its role as
            an inhibitor of TGF-beta signaling
  JOURNAL   Dev Growth Differ 46 (3), 257-274 (2004)
   PUBMED   15206957
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Oka,C., Tsujimoto,R., Kajikawa,M., Koshiba-Takeuchi,K., Ina,J.,
            Yano,M., Tsuchiya,A., Ueta,Y., Soma,A., Kanda,H., Matsumoto,M. and
            Kawaichi,M.
  TITLE     HtrA1 serine protease inhibits signaling mediated by Tgfbeta family
            proteins
  JOURNAL   Development 131 (5), 1041-1053 (2004)
   PUBMED   14973287
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Hu,S.I., Carozza,M., Klein,M., Nantermet,P., Luk,D. and Crowl,R.M.
  TITLE     Human HtrA, an evolutionarily conserved serine protease identified
            as a differentially expressed gene product in osteoarthritic
            cartilage
  JOURNAL   J Biol Chem 273 (51), 34406-34412 (1998)
   PUBMED   9852107
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF179370.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF179370.1, BC081767.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..480
                     /product="serine protease HTRA1 precursor"
                     /EC_number="3.4.21.-"
                     /note="protease, serine, 11 (Igf binding); protease serine
                     11; serine protease HTRA1; serine protease 11;
                     high-temperature requirement A serine peptidase 1"
                     /calculated_mol_wt=48979
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2369
     mat_peptide     23..480
                     /product="Serine protease HTRA1. /id=PRO_0000416251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZK5.1)"
                     /calculated_mol_wt=48979
     Region          37..89
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     pfam00219"
                     /db_xref="CDD:459717"
     Region          115..155
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            169
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q92743; propagated from
                     UniProtKB/Swiss-Prot (Q9QZK5.1)"
     Site            171
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q92743; propagated from
                     UniProtKB/Swiss-Prot (Q9QZK5.1)"
     Region          202..477
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
     Region          204..364
                     /region_name="Serine protease. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZK5.1)"
     Site            278
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q92743; propagated from
                     UniProtKB/Swiss-Prot (Q9QZK5.1)"
     CDS             1..480
                     /gene="Htra1"
                     /gene_synonym="Prss11"
                     /coded_by="NM_031721.1:41..1483"
                     /db_xref="GeneID:65164"
                     /db_xref="RGD:69235"
ORIGIN      
        1 mqflrtalls llllllaaps lalpsgisrs apaatvcpeh cdptrcappp tdceggrvrd
       61 acgccevcga legavcglqe gpcgeglqcv vpfgvpasat vrrraqaglc vcassepvcg
      121 sdaktytnlc qlraasrrse klrqppvivl qrgacgqgqe dpnslrhkyn fiadvvekia
      181 pavvhielyr klpfskrevp vasgsgfivs edglivtnah vvtnknrvkv elkngatyea
      241 kikdvdekad ialikidhqg klpvlllgrs selrpgefvv aigspfslqn tvttgivstt
      301 qrggkelglr nsdmdyiqtd aiinygnsgg plvnldgevi gintlkvtag isfaipsdki
      361 kkflteshdr qakgktvtkk kyigirmmsl tsskakelkd rhrdfpdvis gayiievipd
      421 tpaeagglke ndviisingq svvtandvsd vikkentlnm vvrrgnediv itvvpeeidp
//
LOCUS       NP_071588                550 aa            linear   ROD 27-APR-2025
DEFINITION  acetyl-coenzyme A transporter 1 [Rattus norvegicus].
ACCESSION   NP_071588
VERSION     NP_071588.2
DBSOURCE    REFSEQ: accession NM_022252.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Mao,F., Li,Z., Zhao,B., Lin,P., Liu,P., Zhai,M., Liu,Q., Shao,C.,
            Sun,W. and Gong,Y.
  TITLE     Identification and functional analysis of a SLC33A1: c.339T>G
            (p.Ser113Arg) variant in the original SPG42 family
  JOURNAL   Hum Mutat 36 (2), 240-249 (2015)
   PUBMED   25402622
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Bora,R.S., Ichikawa,S., Kanamori,A. and Hirabayashi,Y.
  TITLE     cDNA cloning of putative rat acetyl-CoA transporter and its
            expression pattern in brain
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 204-208 (2000)
   PUBMED   10965123
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Bora,R.S., Kanamori,A. and Hirabayashi,Y.
  TITLE     Cloning and characterization of a putative mouse acetyl-CoA
            transporter cDNA
  JOURNAL   Gene 238 (2), 455-462 (1999)
   PUBMED   10570973
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078832.1.
            
            On Aug 8, 2004 this sequence version replaced NP_071588.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078832.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..550
                     /product="acetyl-coenzyme A transporter 1"
                     /note="AT-1; acetyl-CoA transporter 1; solute carrier
                     family 33 (acetyl-CoA transporter), member 1;
                     acetyl-coenzyme A transporter 1-like"
                     /calculated_mol_wt=60971
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99J27; propagated from
                     UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            75..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Region          86..459
                     /region_name="2A0125"
                     /note="AmpG-like permease; TIGR00901"
                     /db_xref="CDD:273329"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            301..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            345..365
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            376..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            406..426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     Site            510..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYY8.1)"
     CDS             1..550
                     /gene="Slc33a1"
                     /gene_synonym="Acatn"
                     /coded_by="NM_022252.2:175..1827"
                     /db_xref="GeneID:64018"
                     /db_xref="RGD:620653"
ORIGIN      
        1 msptishkdn srqrrsgmfg haldmksgpl ppggwddnhq dsvggegdre vllgdvgpgd
       61 fpkakrsyra elssillllf lyvlqgiplg lagsiplilq sknvsytdqa ffsfvfwpfs
      121 lkllwaplvd avyfknfgrr kswlvptqyi lgifmiylst qvdrllgnid grtpdvvalt
      181 vtfflfefla atqdiavdgw altmlsrenv gyastcnsvg qtagyflgnv lflalesadf
      241 cnkylrfqpq prgivtlsdf lffwgtvfli tttlvallkk etreasvvke etqgitdtyk
      301 llfsiikmpa vlafcllilt skigfsaada vtglklveeg vpkehlalla vpmvplqiil
      361 plliskytag pqplnifyka mpyrlllgle yallvwwtpk vehqggfpiy yyiivllsya
      421 lhqvtlysmy vsimafnakv sdpliggtym tllntvsnlg gnwpstvalw lvdpltvkec
      481 vgasnqncrt peaielckkl ggscvtaldg yyvesivcvl igfgwwfflg pkfkklqdeg
      541 psswkckrtn
//
LOCUS       NP_446273                206 aa            linear   ROD 27-APR-2025
DEFINITION  ras-related protein Ral-B [Rattus norvegicus].
ACCESSION   NP_446273
VERSION     NP_446273.1
DBSOURCE    REFSEQ: accession NM_053821.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Simicek,M., Lievens,S., Laga,M., Guzenko,D., Aushev,V.N., Kalev,P.,
            Baietti,M.F., Strelkov,S.V., Gevaert,K., Tavernier,J. and
            Sablina,A.A.
  TITLE     The deubiquitylase USP33 discriminates between RALB functions in
            autophagy and innate immune response
  JOURNAL   Nat Cell Biol 15 (10), 1220-1230 (2013)
   PUBMED   24056301
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Martin,T.D., Mitin,N., Cox,A.D., Yeh,J.J. and Der,C.J.
  TITLE     Phosphorylation by protein kinase Calpha regulates RalB small
            GTPase protein activation, subcellular localization, and effector
            utilization
  JOURNAL   J Biol Chem 287 (18), 14827-14836 (2012)
   PUBMED   22393054
  REMARK    GeneRIF: phosphorylation by PKCalpha is critical for RalB-mediated
            vesicle trafficking and exocytosis.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Fenwick,R.B., Prasannan,S., Campbell,L.J., Nietlispach,D.,
            Evetts,K.A., Camonis,J., Mott,H.R. and Owen,D.
  TITLE     Solution structure and dynamics of the small GTPase RalB in its
            active conformation: significance for effector protein binding
  JOURNAL   Biochemistry 48 (10), 2192-2206 (2009)
   PUBMED   19166349
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Cascone,I., Selimoglu,R., Ozdemir,C., Del Nery,E., Yeaman,C.,
            White,M. and Camonis,J.
  TITLE     Distinct roles of RalA and RalB in the progression of cytokinesis
            are supported by distinct RalGEFs
  JOURNAL   EMBO J 27 (18), 2375-2387 (2008)
   PUBMED   18756269
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Falsetti,S.C., Wang,D.A., Peng,H., Carrico,D., Cox,A.D., Der,C.J.,
            Hamilton,A.D. and Sebti,S.M.
  TITLE     Geranylgeranyltransferase I inhibitors target RalB to inhibit
            anchorage-dependent growth and induce apoptosis and RalA to inhibit
            anchorage-independent growth
  JOURNAL   Mol Cell Biol 27 (22), 8003-8014 (2007)
   PUBMED   17875936
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Li,G., Han,L., Chou,T.C., Fujita,Y., Arunachalam,L., Xu,A.,
            Wong,A., Chiew,S.K., Wan,Q., Wang,L. and Sugita,S.
  TITLE     RalA and RalB function as the critical GTP sensors for
            GTP-dependent exocytosis
  JOURNAL   J Neurosci 27 (1), 190-202 (2007)
   PUBMED   17202486
  REMARK    GeneRIF: Our results indicate that endogenous RalA and RalB
            function specifically as GTP sensors for the GTP-dependent
            exocytosis of dense core vesicles.
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Lim,K.H., O'Hayer,K., Adam,S.J., Kendall,S.D., Campbell,P.M.,
            Der,C.J. and Counter,C.M.
  TITLE     Divergent roles for RalA and RalB in malignant growth of human
            pancreatic carcinoma cells
  JOURNAL   Curr Biol 16 (24), 2385-2394 (2006)
   PUBMED   17174914
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Rosse,C., Hatzoglou,A., Parrini,M.C., White,M.A., Chavrier,P. and
            Camonis,J.
  TITLE     RalB mobilizes the exocyst to drive cell migration
  JOURNAL   Mol Cell Biol 26 (2), 727-734 (2006)
   PUBMED   16382162
  REMARK    GeneRIF: RalB regulation of exocyst function is required for the
            coordinated delivery of secretory vesicles to the sites of dynamic
            plasma membrane expansion that specify directional movement.
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Lalli,G. and Hall,A.
  TITLE     Ral GTPases regulate neurite branching through GAP-43 and the
            exocyst complex
  JOURNAL   J Cell Biol 171 (5), 857-869 (2005)
   PUBMED   16330713
  REMARK    GeneRIF: The two Ral isoforms, RalA and -B, promote branching
            through distinct pathways, involving the exocyst complex and
            phospholipase D, respectively.
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Wildey,G.M., Viggeswarapu,M., Rim,S. and Denker,J.K.
  TITLE     Isolation of cDNA clones and tissue expression of rat ral A and ral
            B GTP-binding proteins
  JOURNAL   Biochem Biophys Res Commun 194 (1), 552-559 (1993)
   PUBMED   7687439
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072505.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072505.1, CK366097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN16093049
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q11"
     Protein         1..206
                     /product="ras-related protein Ral-B"
                     /EC_number="3.6.5.2"
                     /note="v-ral simian leukemia viral oncogene homolog B (ras
                     related); v-ral simian leukemia viral oncogene homolog B
                     (ras related; GTP binding protein); RALB Ras like
                     proto-oncogene B"
                     /calculated_mol_wt=23186
     mat_peptide     1..203
                     /product="Ras-related protein Ral-B. /id=PRO_0000082700"
                     /note="propagated from UniProtKB/Swiss-Prot (P36860.1)"
                     /calculated_mol_wt=22988
     Region          15..178
                     /region_name="RalA_RalB"
                     /note="Ral (Ras-like) family containing highly homologous
                     RalA and RalB; cd04139"
                     /db_xref="CDD:206710"
     Site            21..28
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206710"
     Site            order(22..23,70..72,74..75,79,82,97,99,102..103,106..107,
                     110)
                     /site_type="active"
                     /note="GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            order(23..29,39..40,46,71,128..129,131,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206710"
     Site            order(28..29,43,45,51..52,65..66,68,70..71,160)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206710"
     Site            order(36,38,47..52,56,60..61,161..164,166)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206710"
     Region          43..51
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36860.1)"
     Site            44..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206710"
     Site            46
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206710"
     Site            68..71
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206710"
     Site            70..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206710"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206710"
     Site            order(140..141,144,148,156)
                     /site_type="active"
                     /note="alternate GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206710"
     Region          181..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36860.1)"
     Site            203
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P36860.1)"
     CDS             1..206
                     /gene="Ralb"
                     /gene_synonym="dRalb"
                     /coded_by="NM_053821.2:217..837"
                     /db_xref="GeneID:116546"
                     /db_xref="RGD:619852"
ORIGIN      
        1 maankgksqg slvlhkvimv gsggvgksal tlqfmydefv edyeptkads yrkkvvldge
       61 evqidildta gqedyaaird nyfrsgegfl lvfsitehes ftataefreq ilrvkaeedk
      121 ipllvvgnks dleerrqvpv eeargkaeew gvqyvetsak tranvdkvff dlmreirakk
      181 msenkdkngr ksgkskksfk erccll
//
LOCUS       NP_001003974             158 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein-signaling modulator 3 [Rattus norvegicus].
ACCESSION   NP_001003974
VERSION     NP_001003974.1
DBSOURCE    REFSEQ: accession NM_001003974.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Giguere,P.M., Billard,M.J., Laroche,G., Buckley,B.K.,
            Timoshchenko,R.G., McGinnis,M.W., Esserman,D., Foreman,O., Liu,P.,
            Siderovski,D.P. and Tarrant,T.K.
  TITLE     G-protein signaling modulator-3, a gene linked to autoimmune
            diseases, regulates monocyte function and its deficiency protects
            from inflammatory arthritis
  JOURNAL   Mol Immunol 54 (2), 193-198 (2013)
   PUBMED   23280397
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Cao,X., Cismowski,M.J., Sato,M., Blumer,J.B. and Lanier,S.M.
  TITLE     Identification and characterization of AGS4: a protein containing
            three G-protein regulatory motifs that regulate the activation
            state of Gialpha
  JOURNAL   J Biol Chem 279 (26), 27567-27574 (2004)
   PUBMED   15096500
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC088220.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088220.1, CO570164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680432, SAMN06680437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..158
                     /product="G-protein-signaling modulator 3"
                     /note="G-protein signalling modulator 3 (AGS3-like, C.
                     elegans); activator of G-protein signalling 4; G-protein
                     signaling modulator 3 (AGS3-like, C. elegans)"
                     /calculated_mol_wt=17361
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG88.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4H4; propagated from
                     UniProtKB/Swiss-Prot (Q6MG88.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4H4; propagated from
                     UniProtKB/Swiss-Prot (Q6MG88.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U1Z5; propagated from
                     UniProtKB/Swiss-Prot (Q6MG88.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4H4; propagated from
                     UniProtKB/Swiss-Prot (Q6MG88.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4H4; propagated from
                     UniProtKB/Swiss-Prot (Q6MG88.1)"
     Region          78..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG88.1)"
     CDS             1..158
                     /gene="Gpsm3"
                     /gene_synonym="AGS4; G18; Ng1"
                     /coded_by="NM_001003974.2:311..787"
                     /db_xref="GeneID:406163"
                     /db_xref="RGD:1303014"
ORIGIN      
        1 meaerpqedg eqslpqddqg wppvnstarp wrsappsppp pgtrhtalgp rsgsllslqt
       61 ellldlvaea qsrrleeqra afhtpkvpps laptpprlle dkeqlystil shqcqrieaq
      121 rsdpplppgg qellelllrv qgggrmedqr srppthtc
//
LOCUS       NP_001004282             297 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 178A precursor [Rattus norvegicus].
ACCESSION   NP_001004282 XP_343008
VERSION     NP_001004282.1
DBSOURCE    REFSEQ: accession NM_001004282.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Decker,C.E., Yang,Z., Rimer,R., Park-Min,K.H., Macaubas,C.,
            Mellins,E.D., Novack,D.V. and Faccio,R.
  TITLE     Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
            regulate bone mass
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15654-15659 (2015)
   PUBMED   26644563
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079338.1.
            
            On Sep 10, 2004 this sequence version replaced XP_343008.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            30 bp suspected to be vector contamination from the 5' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079338.1, CK366007.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..297
                     /product="transmembrane protein 178A precursor"
                     /note="transmembrane protein 178"
                     /calculated_mol_wt=30569
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68FV0.1)"
                     /calculated_mol_wt=2529
     mat_peptide     26..297
                     /product="Transmembrane protein 178A. /id=PRO_0000287282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV0.1)"
                     /calculated_mol_wt=30569
     Region          41..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV0.1)"
     Region          106..274
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68FV0.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV0.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV0.1)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FV0.1)"
     CDS             1..297
                     /gene="Tmem178a"
                     /gene_synonym="Tmem178"
                     /coded_by="NM_001004282.1:9..902"
                     /db_xref="GeneID:362691"
                     /db_xref="RGD:1303057"
ORIGIN      
        1 mepralvtal slglslcslg llvtaiftdh wyetdprrhk escersraga dppdqknrlm
       61 plshlplrds pplgrrllpg gpgrsdpesw rsllglggld aecgrplfat ysglwrkcyf
      121 lgidrdidtl ilkgiaqrct avkyhfsqpi rlrnipfnlt kiiqqdewhl lhlrritagf
      181 lgmavavllc gcivatvsff weesltqhva gllflmtgif ctislctyaa svsydlnrvp
      241 kliyslphdv ehgyswsifc awcslgfiva agglciaypf isrtkiahlk sgrdstv
//
LOCUS       NP_659560                583 aa            linear   ROD 27-APR-2025
DEFINITION  torsin-1A-interacting protein 1 [Rattus norvegicus].
ACCESSION   NP_659560
VERSION     NP_659560.2
DBSOURCE    REFSEQ: accession NM_145092.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Rose,A.E., Zhao,C., Turner,E.M., Steyer,A.M. and Schlieker,C.
  TITLE     Arresting a Torsin ATPase reshapes the endoplasmic reticulum
  JOURNAL   J Biol Chem 289 (1), 552-564 (2014)
   PUBMED   24275647
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Santos,M., Rebelo,S., Van Kleeff,P.J., Kim,C.E., Dauer,W.T.,
            Fardilha,M., da Cruz E Silva,O.A. and da Cruz E Silva,E.F.
  TITLE     The nuclear envelope protein, LAP1B, is a novel protein phosphatase
            1 substrate
  JOURNAL   PLoS One 8 (10), e76788 (2013)
   PUBMED   24116158
  REMARK    GeneRIF: Data indicate that the protein phosphatase 1 (PP1) and
            nuclear membrane protein lamina associated polypeptide 1B (LAP1B)
            LAP1B:PP1 complex can be immunoprecipitated from cerebral cortex.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Zhao,C., Brown,R.S., Chase,A.R., Eisele,M.R. and Schlieker,C.
  TITLE     Regulation of Torsin ATPases by LAP1 and LULL1
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), E1545-E1554 (2013)
   PUBMED   23569223
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Kim,C.E., Perez,A., Perkins,G., Ellisman,M.H. and Dauer,W.T.
  TITLE     A molecular mechanism underlying the neural-specific defect in
            torsinA mutant mice
  JOURNAL   Proc Natl Acad Sci U S A 107 (21), 9861-9866 (2010)
   PUBMED   20457914
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Pestov,N.B., Ahmad,N., Korneenko,T.V., Zhao,H., Radkov,R.,
            Schaer,D., Roy,S., Bibert,S., Geering,K. and Modyanov,N.N.
  TITLE     Evolution of Na,K-ATPase beta m-subunit into a coregulator of
            transcription in placental mammals
  JOURNAL   Proc Natl Acad Sci U S A 104 (27), 11215-11220 (2007)
   PUBMED   17592128
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Hewett,J.W., Zeng,J., Niland,B.P., Bragg,D.C. and Breakefield,X.O.
  TITLE     Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
            extension through interference with cytoskeletal dynamics
  JOURNAL   Neurobiol Dis 22 (1), 98-111 (2006)
   PUBMED   16361107
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Segawa,M., Niino,K., Mineki,R., Kaga,N., Murayama,K., Sugimoto,K.,
            Watanabe,Y., Furukawa,K. and Horigome,T.
  TITLE     Proteome analysis of a rat liver nuclear insoluble protein fraction
            and localization of a novel protein, ISP36, to compartments in the
            interchromatin space
  JOURNAL   FEBS J 272 (17), 4327-4338 (2005)
   PUBMED   16128803
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Goodchild,R.E. and Dauer,W.T.
  TITLE     The AAA+ protein torsinA interacts with a conserved domain present
            in LAP1 and a novel ER protein
  JOURNAL   J Cell Biol 168 (6), 855-862 (2005)
   PUBMED   15767459
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Martin,L., Crimaudo,C. and Gerace,L.
  TITLE     cDNA cloning and characterization of lamina-associated polypeptide
            1C (LAP1C), an integral protein of the inner nuclear membrane
  JOURNAL   J Biol Chem 270 (15), 8822-8828 (1995)
   PUBMED   7721789
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086987.1.
            
            On Oct 12, 2005 this sequence version replaced NP_659560.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086987.1, U20286.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..583
                     /product="torsin-1A-interacting protein 1"
                     /note="lamina-associated polypeptide 1C; lamina-associated
                     polypeptide 1B; torsin A interacting protein 1"
                     /calculated_mol_wt=65518
     Region          23..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Region          145..350
                     /region_name="LAP1_N"
                     /note="Lamina-associated polypeptide 1, N-terminal;
                     pfam20443"
                     /db_xref="CDD:466592"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5JTV8; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Region          353..583
                     /region_name="LAP1_C"
                     /note="Lamina-associated polypeptide 1, AAA+ activator
                     domain; pfam05609"
                     /db_xref="CDD:461691"
     Region          356..583
                     /region_name="Interaction with TOR1A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQX1.1)"
     Site            399
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5PQX1.1)"
     CDS             1..583
                     /gene="Tor1aip1"
                     /gene_synonym="Lap1b; Lap1c"
                     /coded_by="NM_145092.2:189..1940"
                     /db_xref="GeneID:246314"
                     /db_xref="RGD:628851"
ORIGIN      
        1 magerwraeg lgegwaiyvt prapiregrr rlatqngdgs dapayethps rhgrrevrfs
       61 eeppevygdf epraakersp gerrtppekf rsdsakeevr esaynlrsrq rrqrgpqeae
      121 emktrrstrl eqhsqqaqqq lspatsgrgl rdaqslsedr gedepssqpv tsqtvskktv
      181 rtpetsvmse dpisnlcrpp lrsprpdasi vqhinpfeeg eteddlessy sdvtirirsr
      241 dsvesrdeaa vaaghhpdsl wglphsrgdf tahenqpsll ptgcqknpqe wveqavrmrt
      301 rmaynniqks dfgnqspsts rqqaavqppd essvkikwwl lilvaalamg iywffhtpvv
      361 ettavqefqn qmkqlqskyq sqdeklwkrg ttflekhlns slprpqpail lltaaqdaae
      421 vlkclseqia dayssfrsvr airidgagka aqdsdlvkhe vdqeltdgfr ngqnaavvhr
      481 feslpagstl ifykycdhen aafkdvalvl tvlleeqtle aslglkeiee kvrdflkvkf
      541 tssdtansyn hmdpdklngl wsrishlvlp vqpenalkag scl
//
LOCUS       NP_112300                327 aa            linear   ROD 27-APR-2025
DEFINITION  gonadotropin-releasing hormone receptor [Rattus norvegicus].
ACCESSION   NP_112300
VERSION     NP_112300.2
DBSOURCE    REFSEQ: accession NM_031038.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Li,H., Guo,Y., Zhang,G., Deng,J., Fischer,H., Craig,L.B., Yu,X. and
            Kem,D.C.
  TITLE     Gonadotrophin-releasing hormone receptor autoantibodies induce
            polycystic ovary syndrome-like features in a rat model
  JOURNAL   Exp Physiol 106 (4), 902-912 (2021)
   PUBMED   33576068
  REMARK    GeneRIF: Gonadotrophin-releasing hormone receptor autoantibodies
            induce polycystic ovary syndrome-like features in a rat model.
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Kyritsi,K., Meng,F., Zhou,T., Wu,N., Venter,J., Francis,H.,
            Kennedy,L., Onori,P., Franchitto,A., Bernuzzi,F., Invernizzi,P.,
            McDaniel,K., Mancinelli,R., Alvaro,D., Gaudio,E., Alpini,G. and
            Glaser,S.
  TITLE     Knockdown of Hepatic Gonadotropin-Releasing Hormone by
            Vivo-Morpholino Decreases Liver Fibrosis in Multidrug Resistance
            Gene 2 Knockout Mice by Down-Regulation of miR-200b
  JOURNAL   Am J Pathol 187 (7), 1551-1565 (2017)
   PUBMED   28502477
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Nelson,B.S., Black,K.L. and Daniel,J.M.
  TITLE     Circulating Estradiol Regulates Brain-Derived Estradiol via Actions
            at GnRH Receptors to Impact Memory in Ovariectomized Rats
  JOURNAL   eNeuro 3 (6) (2016)
   PUBMED   28032117
  REMARK    GeneRIF: Prevention of estradiol synthesis blocked the ability of
            peripheral estradiol administration in ovariectomized rats to
            enhance hippocampus-dependent memory in a radial-maze task.
            Hippocampal GnRH receptor antagonism blocked the ability of
            peripheral estradiol administration in ovariectomized rats to
            enhance hippocampus-dependent memory.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Bjelobaba,I., Janjic,M.M., Tavcar,J.S., Kucka,M., Tomic,M. and
            Stojilkovic,S.S.
  TITLE     The relationship between basal and regulated Gnrhr expression in
            rodent pituitary gonadotrophs
  JOURNAL   Mol Cell Endocrinol 437, 302-311 (2016)
   PUBMED   27569529
  REMARK    GeneRIF: the age-dependent basal and regulated Gnrhr transcription
            could account for the initial blockade and subsequent activation of
            the reproductive system during development.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Terashima,R., Laoharatchatathanin,T., Kurusu,S. and Kawaminami,M.
  TITLE     Augmentation of gonadotropin-releasing hormone receptor expression
            in the post-lactational mammary tissues of rats
  JOURNAL   J Reprod Dev 62 (5), 495-499 (2016)
   PUBMED   27349532
  REMARK    GeneRIF: GnRH-R is expressed in the mammary tissues after weaning;
            GnRH is involved in the involution and tissue remodeling of
            post-lactating rat mammary tissues
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Kudo,A., Park,M.K. and Kawashima,S.
  TITLE     Isolation of rat GnRH receptor cDNA having different 5'-noncoding
            sequence
  JOURNAL   Zoolog Sci 10 (5), 863-867 (1993)
   PUBMED   7764374
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Perrin,M.H., Bilezikjian,L.M., Hoeger,C., Donaldson,C.J.,
            Rivier,J., Haas,Y. and Vale,W.W.
  TITLE     Molecular and functional characterization of GnRH receptors cloned
            from rat pituitary and a mouse pituitary tumor cell line
  JOURNAL   Biochem Biophys Res Commun 191 (3), 1139-1144 (1993)
   PUBMED   7916600
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Kaiser,U.B., Zhao,D., Cardona,G.R. and Chin,W.W.
  TITLE     Isolation and characterization of cDNAs encoding the rat pituitary
            gonadotropin-releasing hormone receptor
  JOURNAL   Biochem Biophys Res Commun 189 (3), 1645-1652 (1992)
   PUBMED   1339279
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Eidne,K.A., Sellar,R.E., Couper,G., Anderson,L. and Taylor,P.L.
  TITLE     Molecular cloning and characterisation of the rat pituitary
            gonadotropin-releasing hormone (GnRH) receptor
  JOURNAL   Mol Cell Endocrinol 90 (1), R5-R9 (1992)
   PUBMED   1338727
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Marian,J. and Conn,P.M.
  TITLE     Subcellular localization of the receptor for gonadotropin-releasing
            hormone in pituitary and ovarian tissue
  JOURNAL   Endocrinology 112 (1), 104-112 (1983)
   PUBMED   6291912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB775870.1, X68980.1, L07646.1 and JAXUCZ010000014.1.
            
            On Oct 18, 2005 this sequence version replaced NP_112300.1.
            
            Sequence Note: This RefSeq record was created using sequences from
            two different strains, Sprague-Dawley and BN/SsNHsdMCW, because no
            single transcript from the same strain was available for the full
            length of the gene.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X68980.1, X76635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..327
                     /product="gonadotropin-releasing hormone receptor"
                     /note="growth hormone; gnRH-R; gnRH receptor"
                     /calculated_mol_wt=37631
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30969.2)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30969.2)"
     Region          36..327
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          38..67
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320505"
     Site            39..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Region          77..100
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320505"
     Site            78..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30969.2)"
     Region          115..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320505"
     Site            116..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Region          158..174
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320505"
     Site            165..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Region          208..231
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320505"
     Site            212..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Region          265..287
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320505"
     Site            281..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     Region          301..326
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320505"
     Site            306..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30969.2)"
     CDS             1..327
                     /gene="Gnrhr"
                     /gene_synonym="GH1; Lhrhr"
                     /coded_by="NM_031038.3:88..1071"
                     /db_xref="GeneID:81668"
                     /db_xref="RGD:70513"
ORIGIN      
        1 mannasleqd qnhcsainns ipltqgklpt ltlsgkirvt vtfflfllst afnasflvkl
       61 qrwtqkrkkg kklsrmkvll khltlanlle tlivmpldgm wnitvqwyag eflckvlsyl
      121 klfsmyapaf mmvvisldrs lavtqplavq sksklersmt slawilsivf agpqlyifrm
      181 iyladgsgpa vfsqcvthcs fpqwwheafy nfftfsclfi ipllimlicn akiifaltrv
      241 lhqdprklql nqsknnipra rlrtlkmtva fatsfvicwt pyyvlgiwyw fdpemlnrvs
      301 epvnhffflf aflnpcfdpl iygyfsl
//
LOCUS       NP_036780                638 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial sodium channel subunit beta [Rattus norvegicus].
ACCESSION   NP_036780
VERSION     NP_036780.1
DBSOURCE    REFSEQ: accession NM_012648.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Rauh,R., Hoerner,C. and Korbmacher,C.
  TITLE     deltabetagamma-ENaC is inhibited by CFTR but stimulated by cAMP in
            Xenopus laevis oocytes
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 312 (2), L277-L287 (2017)
   PUBMED   27941075
  REMARK    GeneRIF: deltabetagamma-ENaC is inhibited by CFTR but activated by
            cyclic AMP.
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Li,Y.L., Zhang,D., Tu,H. and Muelleman,R.L.
  TITLE     Altered ENaC is Associated With Aortic Baroreceptor Dysfunction in
            Chronic Heart Failure
  JOURNAL   Am J Hypertens 29 (5), 582-589 (2016)
   PUBMED   26297031
  REMARK    GeneRIF: Decreased expression of Scnn1b/g and activation of ENaC
            could be involved in attenuation of the aortic baroreceptor
            sensitivity in congestive heart failure.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Abramova,T.O., Smolenskaya,S.E., Antonov,E.V., Redina,O.E. and
            Markel,A.L.
  TITLE     [Expression of Catechol-O-Methyltransferase (Comt),
            Mineralocorticoid Receptor (Mlr), and Epithelial Sodium Channel
            (ENaC) Genes in Kidneys of Hypertensive ISIAH Rats at Rest and
            during Response to Stress]
  JOURNAL   Genetika 52 (2), 206-214 (2016)
   PUBMED   27215035
  REMARK    GeneRIF: The discovered changes in the expression level of
            catechol-o-methyltransferase , mineralocorticoid receptor , and
            b-subunit of epithelial sodium channel confirm their involvement in
            increased sympathetic stimulation of the of hypertensive rats
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Warrington,J.P., Coleman,K., Skaggs,C., Hosick,P.A., George,E.M.,
            Stec,D.E., Ryan,M.J., Granger,J.P. and Drummond,H.A.
  TITLE     Heme oxygenase-1 promotes migration and beta-epithelial Na+ channel
            expression in cytotrophoblasts and ischemic placentas
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 306 (9), R641-R646 (2014)
   PUBMED   24553299
  REMARK    GeneRIF: Suggest that beta-ENaC mediates cytotrophoblast migration
            and increasing beta-ENaC expression by HO-1 induction enhances
            migration.
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Warnock,D.G., Kusche-Vihrog,K., Tarjus,A., Sheng,S.,
            Oberleithner,H., Kleyman,T.R. and Jaisser,F.
  TITLE     Blood pressure and amiloride-sensitive sodium channels in vascular
            and renal cells
  JOURNAL   Nat Rev Nephrol 10 (3), 146-157 (2014)
   PUBMED   24419567
  REMARK    Review article
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Kreutz,R., Struk,B., Rubattu,S., Hubner,N., Szpirer,J., Szpirer,C.,
            Ganten,D. and Lindpaintner,K.
  TITLE     Role of the alpha-, beta-, and gamma-subunits of epithelial sodium
            channel in a model of polygenic hypertension
  JOURNAL   Hypertension 29 (1 Pt 1), 131-136 (1997)
   PUBMED   9039092
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Staub,O., Dho,S., Henry,P., Correa,J., Ishikawa,T., McGlade,J. and
            Rotin,D.
  TITLE     WW domains of Nedd4 bind to the proline-rich PY motifs in the
            epithelial Na+ channel deleted in Liddle's syndrome
  JOURNAL   EMBO J 15 (10), 2371-2380 (1996)
   PUBMED   8665844
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Chang,S.S., Grunder,S., Hanukoglu,A., Rosler,A., Mathew,P.M.,
            Hanukoglu,I., Schild,L., Lu,Y., Shimkets,R.A., Nelson-Williams,C.,
            Rossier,B.C. and Lifton,R.P.
  TITLE     Mutations in subunits of the epithelial sodium channel cause salt
            wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1
  JOURNAL   Nat Genet 12 (3), 248-253 (1996)
   PUBMED   8589714
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Shimkets,R.A., Warnock,D.G., Bositis,C.M., Nelson-Williams,C.,
            Hansson,J.H., Schambelan,M., Gill,J.R. Jr., Ulick,S., Milora,R.V.,
            Findling,J.W. et al.
  TITLE     Liddle's syndrome: heritable human hypertension caused by mutations
            in the beta subunit of the epithelial sodium channel
  JOURNAL   Cell 79 (3), 407-414 (1994)
   PUBMED   7954808
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Canessa,C.M., Schild,L., Buell,G., Thorens,B., Gautschi,I.,
            Horisberger,J.D. and Rossier,B.C.
  TITLE     Amiloride-sensitive epithelial Na+ channel is made of three
            homologous subunits
  JOURNAL   Nature 367 (6462), 463-467 (1994)
   PUBMED   8107805
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X77932.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            17 bp suspected to be vector contamination from the 5' end.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X77932.1, U35174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..638
                     /product="epithelial sodium channel subunit beta"
                     /note="amiloride-sensitive sodium channel subunit beta;
                     sodium channel, non-voltage-gated 1, beta subunit; SCNEB;
                     beta-ENaC; sodium channel epithelial 1 beta subunit;
                     beta-NaCH; epithelial Na(+) channel subunit beta;
                     nonvoltage-gated sodium channel 1 subunit beta; sodium
                     channel, nonvoltage-gated, type I, beta"
                     /calculated_mol_wt=71947
     Region          21..621
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37090.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37090.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37090.2)"
     Site            531..551
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37090.2)"
     Region          598..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P37090.2)"
     Region          614..618
                     /region_name="PY motif, recruits WW domain-containing
                     proteins and is thereby required for ubiquitination and
                     inhibition of the channel by NEDD4 and NEDD4L.
                     /evidence=ECO:0000269|PubMed:12654927,
                     ECO:0000269|PubMed:8665844"
                     /note="propagated from UniProtKB/Swiss-Prot (P37090.2)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU38; propagated from
                     UniProtKB/Swiss-Prot (P37090.2)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU38; propagated from
                     UniProtKB/Swiss-Prot (P37090.2)"
     CDS             1..638
                     /gene="Scnn1b"
                     /gene_synonym="RNENACB"
                     /coded_by="NM_012648.1:56..1972"
                     /db_xref="GeneID:24767"
                     /db_xref="RGD:3640"
ORIGIN      
        1 mpvkkyllkc lhrlqkgpgy tykellvwyc nntnthgpkr iicegpkkka mwflltllfa
       61 clvcwqwgvf iqtylswevs vslsmgfktm nfpavtvcns spfqyskvkh llkdlyklme
      121 avldkilapk sshtnttstl nftiwnhtpl vlidernpdh pvvlnlfgds hnssnpapgs
      181 tcnaqgckva mrlcsangtv ctfrnftsat qavtewyilq atnifsqvlp qdlvgmgyap
      241 driilaclfg tepcshrnft pifypdygnc yifnwgmtek alpsanpgte fglklildig
      301 qedyvpflas tagarlmlhe qrtypfiree giyamagtet sigvlldklq gkgepyspct
      361 mngsdvaiqn lysdynttys iqaclhscfq dhmihncscg hylyplpage kycnnrdfpd
      421 waycylslqm svvqretcls mckescndtq ykmtismadw pseasedwil hvlsqerdqs
      481 snitlsrkgi vklniyfqef nyrtieespa nnivwllsnl ggqfgfwmgg svlcliefge
      541 iiidfiwitv iklvasckgl rrrrpqrpyt gppptvaelv eahtncvfqp dttscrpnae
      601 vypdqqtlpi pgtpppnyds lrlqpldtme sdseveai
//
LOCUS       NP_001009399             362 aa            linear   ROD 27-APR-2025
DEFINITION  sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating [Rattus
            norvegicus].
ACCESSION   NP_001009399 XP_219730
VERSION     NP_001009399.1
DBSOURCE    REFSEQ: accession NM_001009399.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Moessinger,C., Kuerschner,L., Spandl,J., Shevchenko,A. and
            Thiele,C.
  TITLE     Human lysophosphatidylcholine acyltransferases 1 and 2 are located
            in lipid droplets where they catalyze the formation of
            phosphatidylcholine
  JOURNAL   J Biol Chem 286 (24), 21330-21339 (2011)
   PUBMED   21498505
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Jiang,F. and Herman,G.E.
  TITLE     Analysis of Nsdhl-deficient embryos reveals a role for Hedgehog
            signaling in early placental development
  JOURNAL   Hum Mol Genet 15 (22), 3293-3305 (2006)
   PUBMED   17028112
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Caldas,H., Cunningham,D., Wang,X., Jiang,F., Humphries,L.,
            Kelley,R.I. and Herman,G.E.
  TITLE     Placental defects are associated with male lethality in bare
            patches and striated embryos deficient in the NAD(P)H Steroid
            Dehydrogenase-like (NSDHL) Enzyme
  JOURNAL   Mol Genet Metab 84 (1), 48-60 (2005)
   PUBMED   15639195
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Fujimoto,Y., Itabe,H., Sakai,J., Makita,M., Noda,J., Mori,M.,
            Higashi,Y., Kojima,S. and Takano,T.
  TITLE     Identification of major proteins in the lipid droplet-enriched
            fraction isolated from the human hepatocyte cell line HuH7
  JOURNAL   Biochim Biophys Acta 1644 (1), 47-59 (2004)
   PUBMED   14741744
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Herman,G.E.
  TITLE     Disorders of cholesterol biosynthesis: prototypic metabolic
            malformation syndromes
  JOURNAL   Hum Mol Genet 12 Spec No 1, R75-R88 (2003)
   PUBMED   12668600
  REMARK    Review article
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Liu,X.Y., Dangel,A.W., Kelley,R.I., Zhao,W., Denny,P.,
            Botcherby,M., Cattanach,B., Peters,J., Hunsicker,P.R., Mallon,A.M.,
            Strivens,M.A., Bate,R., Miller,W., Rhodes,M., Brown,S.D. and
            Herman,G.E.
  TITLE     The gene mutated in bare patches and striated mice encodes a novel
            3beta-hydroxysteroid dehydrogenase
  JOURNAL   Nat Genet 22 (2), 182-187 (1999)
   PUBMED   10369263
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Phillips,R.J. and Kaufman,M.H.
  TITLE     Bare-patches, a new sex-linked gene in the mouse, associated with a
            high production of XO females. II. Investigations into the nature
            and mechanism of the XO production
  JOURNAL   Genet Res 24 (1), 27-41 (1974)
   PUBMED   4435359
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087626.1.
            
            On Jan 7, 2005 this sequence version replaced XP_219730.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087626.1, SRR8487226.4265.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..362
                     /product="sterol-4-alpha-carboxylate 3-dehydrogenase,
                     decarboxylating"
                     /EC_number="1.1.1.170"
                     /note="NAD(P) dependent steroid dehydrogenase-like"
                     /calculated_mol_wt=40281
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q15738; propagated from
                     UniProtKB/Swiss-Prot (Q5PPL3.1)"
     Region          29..355
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(33,35..36,38,57..59,93..95,132..134,161,165,
                     189..192)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(110,134,161,165)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPL3.1)"
     Region          359..362
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000250|UniProtKB:Q9R1J0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPL3.1)"
     CDS             1..362
                     /gene="Nsdhl"
                     /coded_by="NM_001009399.1:117..1205"
                     /db_xref="GeneID:309262"
                     /db_xref="RGD:1359337"
ORIGIN      
        1 meqavrsesk kgqvtgtdli nevskakkct viggsgflgq hmveqllsrg yavnvfdvrq
       61 gfdnprvqff igdlcnqqdl ypalkgvstv fhcasppsns nnkelfyrvn stgtktviet
      121 ckeagvqkli ltssasvvfe gvdikngted lpyamkpidy ytetkilqer avldandpkk
      181 nfltaairph gifgprdpql vpvlidaark gkmkfmigng knlvdftfve nvvhghilaa
      241 ehlsrdaglg gkafhitnde pipfwtflsr iltglnyeap kyhipyrvay ylafllsllv
      301 mvlspliqiq ttftpfrval agtfhyysce kakkligyrp lvtmddaver tvqsfhhlrk
      361 dk
//
LOCUS       NP_001012192             386 aa            linear   ROD 27-APR-2025
DEFINITION  EARP and GARP complex-interacting protein 1 [Rattus norvegicus].
ACCESSION   NP_001012192 XP_343043
VERSION     NP_001012192.1
DBSOURCE    REFSEQ: accession NM_001012192.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Gershlick,D.C., Schindler,C., Chen,Y. and Bonifacino,J.S.
  TITLE     TSSC1 is novel component of the endosomal retrieval machinery
  JOURNAL   Mol Biol Cell 27 (18), 2867-2878 (2016)
   PUBMED   27440922
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Topalidou,I., Cattin-Ortola,J., Pappas,A.L., Cooper,K.,
            Merrihew,G.E., MacCoss,M.J. and Ailion,M.
  TITLE     The EARP Complex and Its Interactor EIPR-1 Are Required for Cargo
            Sorting to Dense-Core Vesicles
  JOURNAL   PLoS Genet 12 (5), e1006074 (2016)
   PUBMED   27191843
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Canestri,F.
  TITLE     A proposed clinical application of a model of CO2 laser radiation
            induced damage craters
  JOURNAL   J Med Eng Technol 12 (3), 112-117 (1988)
   PUBMED   3172165
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087633.1.
            
            On Feb 11, 2005 this sequence version replaced XP_343043.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087633.1, SRR8487226.26863.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..386
                     /product="EARP and GARP complex-interacting protein 1"
                     /note="protein TSSC1; EARP-interacting protein;
                     endosome-associated recycling protein-interacting protein;
                     tumor suppressing subtransferable candidate 1;
                     tumor-suppressing STF cDNA 1 protein; Golgi-associated
                     retrograde protein-interacting protein; tumor-suppressing
                     subchromosomal transferable fragment candidate gene 1
                     protein"
                     /calculated_mol_wt=43026
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q53HC9; propagated from
                     UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          <39..299
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          68..130
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..172
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          137..174
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..222
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          188..224
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          226..266
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          227..>373
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          231..269
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          270..310
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          275..343
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          312..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53HC9; propagated from
                     UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          344..384
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPK9.1)"
     Region          349..373
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..386
                     /gene="Eipr1"
                     /gene_synonym="Tssc1"
                     /coded_by="NM_001012192.1:72..1232"
                     /db_xref="GeneID:362721"
                     /db_xref="RGD:1305817"
ORIGIN      
        1 meddapviyg lefqaraltp qtaetdairf lvgtqslkyd nqihiidfdd enniinknvl
       61 lhqageiwhi saspadkgvl atcynktsds rvqacaavwr mpkelesgsh espedpasta
      121 qtlellchld ngaqgnvacv vwepmgdgkk visladshil lwdlqpsssq avlassaale
      181 grgqlkftsg rwsphhnctq vatasdttlr gwdtrsmsqi ycienahgql vrdldfnpnk
      241 qyylascgdd ckvkfwdtrn vtepvktlee hshwvwsvry nhshdqlvlt gssdsrvils
      301 nmvsissepf ghlvddddvs dpeehhteks keplqdnvia tyeehedsvy avdwasadpw
      361 lfaslsydgr lvinrvpral kyhill
//
LOCUS       NP_001000942             312 aa            linear   ROD 27-APR-2025
DEFINITION  olfactory receptor 1500 [Rattus norvegicus].
ACCESSION   NP_001000942
VERSION     NP_001000942.1
DBSOURCE    REFSEQ: accession NM_001000942.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Buck,L. and Axel,R.
  TITLE     A novel multigene family may encode odorant receptors: a molecular
            basis for odor recognition
  JOURNAL   Cell 65 (1), 175-187 (1991)
   PUBMED   1840504
COMMENT     REVIEWED REFSEQ: This record has been curated by Janet Young and
            Barbara Trask (FHCRC). The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M64391.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..312
                     /product="olfactory receptor 1500"
                     /note="olfactory receptor-like protein I14"
                     /calculated_mol_wt=35508
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23273.1)"
     Region          26..294
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            26..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Region          27..51
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320584"
     Site            58..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Region          60..82
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320584"
     Region          98..120
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320584"
     Site            101..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Site            140..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Region          143..159
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320584"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320584"
     Site            197..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     Region          238..260
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320584"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320584"
     Site            273..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23273.1)"
     CDS             1..312
                     /gene="Olr1500"
                     /coded_by="NM_001000942.1:1..939"
                     /db_xref="GeneID:405281"
                     /db_xref="RGD:1334013"
ORIGIN      
        1 mtgnnqtlil eflllglpip seyhllfyal flamyltiil gnlliivlvr ldshlhmpmy
       61 lflsnlsfsd lcfssvtmpk llqnmqsqvp sisyagcltq lyffmvfgdm esfllvvmay
      121 dryvaicfpl hyttimstkf caslvlllwm lttthallht lliarlsfce knvilhffcd
      181 isallklscs diyvnelmiy ilggliiiip fllivmsyvr iffsilkfps iqdiykvfst
      241 cgshlsvvtl fygtifgiyl cpsgnnstvk eiamammytv vtpmlnpfiy slrnrdmkra
      301 lirvictkki sl
//
LOCUS       NP_001011986             471 aa            linear   ROD 27-APR-2025
DEFINITION  splicing factor 3A subunit 2 [Rattus norvegicus].
ACCESSION   NP_001011986 XP_216844
VERSION     NP_001011986.1
DBSOURCE    REFSEQ: accession NM_001011986.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Tanackovic,G. and Kramer,A.
  TITLE     Human splicing factor SF3a, but not SF1, is essential for pre-mRNA
            splicing in vivo
  JOURNAL   Mol Biol Cell 16 (3), 1366-1377 (2005)
   PUBMED   15647371
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Gringel,S., van Bergeijk,J., Haastert,K., Grothe,C. and Claus,P.
  TITLE     Nuclear fibroblast growth factor-2 interacts specifically with
            splicing factor SF3a66
  JOURNAL   Biol Chem 385 (12), 1203-1208 (2004)
   PUBMED   15653435
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Nesic,D. and Kramer,A.
  TITLE     Domains in human splicing factors SF3a60 and SF3a66 required for
            binding to SF3a120, assembly of the 17S U2 snRNP, and
            prespliceosome formation
  JOURNAL   Mol Cell Biol 21 (19), 6406-6417 (2001)
   PUBMED   11533230
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Hong,W., Bennett,M., Xiao,Y., Feld Kramer,R., Wang,C. and Reed,R.
  TITLE     Association of U2 snRNP with the spliceosomal complex E
  JOURNAL   Nucleic Acids Res 25 (2), 354-361 (1997)
   PUBMED   9016565
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079320.1.
            
            On Feb 11, 2005 this sequence version replaced XP_216844.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079320.1, DN948235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..471
                     /product="splicing factor 3A subunit 2"
                     /note="splicing factor 3a, subunit 2, 66kDa"
                     /calculated_mol_wt=49759
     Region          1..217
                     /region_name="PRP11"
                     /note="Splicing factor 3a, subunit 2 [RNA processing and
                     modification]; COG5246"
                     /db_xref="CDD:227571"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q15428; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT8.1)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q62203; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT8.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15428; propagated from
                     UniProtKB/Swiss-Prot (Q6AXT8.1)"
     Region          217..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXT8.1)"
     Region          <324..>442
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..471
                     /gene="Sf3a2"
                     /coded_by="NM_001011986.1:82..1497"
                     /db_xref="GeneID:299620"
                     /db_xref="RGD:1308627"
ORIGIN      
        1 mdfqhrpggk tgsggvasss esnrdrrerl rqlaletidi nkdpyfmknh lgsyecklcl
       61 tlhnnegsyl ahtqgkkhqt nlarraakea keapaqpape kvkvevkkfv kigrpgykvt
      121 kqrdtemgqq sllfqidype iaegvmprhr fmsayeqrie ppdrrwqyll maaepyetia
      181 fkvpsreidk aegkfwthwn retkqfflqf hfkmekppap pslpagppgv krpppplmng
      241 lpprpplpda lpppppgglp lppmpptgpa psgppgppqm pppapgvhpp apvvhpptsg
      301 vhppapgvhp papvvhppts gvhppapgvh ppapgvhppa pgvhppapgv hppapgvhpp
      361 apgvhppapg vhppapgvhp ppsagvhpqa pgvhppapav hpqapgvhpp apgihpqapg
      421 vhpqpppgvh paapgvhpqp pgvhptpmpp mlrpplpsdg pgnmpppppg n
//
LOCUS       NP_001119740             642 aa            linear   ROD 27-APR-2025
DEFINITION  tigger transposable element derived 5 [Rattus norvegicus].
ACCESSION   NP_001119740 XP_001074511 XP_235436
VERSION     NP_001119740.1
DBSOURCE    REFSEQ: accession NM_001126268.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161993.1.
            
            On or before May 7, 2008 this sequence version replaced
            XP_001074511.1, XP_235436.4.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC161993.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..642
                     /product="tigger transposable element derived 5"
                     /note="tigger transposable element-derived protein 5;
                     tigger transposable element derived 5 homolog"
                     /calculated_mol_wt=70137
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC39.1)"
     Region          62..111
                     /region_name="CENP-B_N"
                     /note="CENP-B N-terminal DNA-binding domain; pfam04218"
                     /db_xref="CDD:461229"
     Region          131..191
                     /region_name="HTH_Tnp_Tc5"
                     /note="Tc5 transposase DNA-binding domain; pfam03221"
                     /db_xref="CDD:460850"
     Region          198..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC39.1)"
     Region          279..485
                     /region_name="DDE_3"
                     /note="DDE superfamily endonuclease; cl46863"
                     /db_xref="CDD:481203"
     Region          543..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC39.1)"
     CDS             1..642
                     /gene="Tigd5"
                     /coded_by="NM_001126268.2:142..2070"
                     /db_xref="GeneID:300034"
                     /db_xref="RGD:1311576"
ORIGIN      
        1 mypaspsagp alhpvphrar lprprclaep prspapgpgs tarppppapg prprvavkmt
       61 frkaysikdk lqaiervkgg erqasvcrdf gvpggtlrgw lkdepklrwf ldqlggevgt
      121 qrkkmrlane eeidravysw fltlrqhgvp lsgpviqaqa eafarqiygp ectfkashgw
      181 fwrwqkrhgi ssqriygeae ppvagpapvk eepaqpssag llldgtpatl phseggygde
      241 qiynanvtgl ywrllpeqna tpgtgdsrep gecsrrwcsd rvtvllaanl tgshklkplv
      301 igqlpdppsl rhhnqdkfpa syryspdawl srpllrgwff eefvpgvkry lrrsclqqka
      361 vllvahppcp swttsmpave esegtprqcq pellgspeel qtpdgavrvl flsrgnsrah
      421 ipaplehgvv aafkhlykre llrlavscas gspldfmrsf mlkdmlylag lswdlvqags
      481 iercwllglr aafepgqqpa hqveeaaehs rmlsdlthla alaykrlape evaewlhldd
      541 dgglpegcge evapaappsp aslpssigag eeeeeeateq ggvlvptage avwgletalr
      601 wlesqdprev gplrlvqlrs litmarrlgg igpsaaasdd gv
//
LOCUS       NP_001102291             737 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family D member 1 [Rattus norvegicus].
ACCESSION   NP_001102291 XP_001059399 XP_343841
VERSION     NP_001102291.1
DBSOURCE    REFSEQ: accession NM_001108821.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Geillon,F., Gondcaille,C., Raas,Q., Dias,A.M.M., Pecqueur,D.,
            Truntzer,C., Lucchi,G., Ducoroy,P., Falson,P., Savary,S. and
            Trompier,D.
  TITLE     Peroxisomal ATP-binding cassette transporters form mainly tetramers
  JOURNAL   J Biol Chem 292 (17), 6965-6977 (2017)
   PUBMED   28258215
  REMARK    GeneRIF: ABCD1 and its homolog ABCD2 exist mainly as homotetramers
            in the peroxisomal membrane
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Morita,M., Kawamichi,M., Shimura,Y., Kawaguchi,K., Watanabe,S. and
            Imanaka,T.
  TITLE     Brain microsomal fatty acid elongation is increased in
            abcd1-deficient mouse during active myelination phase
  JOURNAL   Metab Brain Dis 30 (6), 1359-1367 (2015)
   PUBMED   26108493
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Kruska,N., Schonfeld,P., Pujol,A. and Reiser,G.
  TITLE     Astrocytes and mitochondria from adrenoleukodystrophy protein
            (ABCD1)-deficient mice reveal that the
            adrenoleukodystrophy-associated very long-chain fatty acids target
            several cellular energy-dependent functions
  JOURNAL   Biochim Biophys Acta 1852 (5), 925-936 (2015)
   PUBMED   25583114
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Muneer,Z., Wiesinger,C., Voigtlander,T., Werner,H.B., Berger,J. and
            Forss-Petter,S.
  TITLE     Abcd2 is a strong modifier of the metabolic impairments in
            peritoneal macrophages of ABCD1-deficient mice
  JOURNAL   PLoS One 9 (9), e108655 (2014)
   PUBMED   25255441
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Geillon,F., Gondcaille,C., Charbonnier,S., Van Roermund,C.W.,
            Lopez,T.E., Dias,A.M., Pais de Barros,J.P., Arnould,C.,
            Wanders,R.J., Trompier,D. and Savary,S.
  TITLE     Structure-function analysis of peroxisomal ATP-binding cassette
            transporters using chimeric dimers
  JOURNAL   J Biol Chem 289 (35), 24511-24520 (2014)
   PUBMED   25043761
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Forss-Petter,S., Werner,H., Berger,J., Lassmann,H., Molzer,B.,
            Schwab,M.H., Bernheimer,H., Zimmermann,F. and Nave,K.A.
  TITLE     Targeted inactivation of the X-linked adrenoleukodystrophy gene in
            mice
  JOURNAL   J Neurosci Res 50 (5), 829-843 (1997)
   PUBMED   9418970
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Lu,J.F., Lawler,A.M., Watkins,P.A., Powers,J.M., Moser,A.B.,
            Moser,H.W. and Smith,K.D.
  TITLE     A mouse model for X-linked adrenoleukodystrophy
  JOURNAL   Proc Natl Acad Sci U S A 94 (17), 9366-9371 (1997)
   PUBMED   9256488
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Kobayashi,T., Shinnoh,N., Kondo,A. and Yamada,T.
  TITLE     Adrenoleukodystrophy protein-deficient mice represent abnormality
            of very long chain fatty acid metabolism
  JOURNAL   Biochem Biophys Res Commun 232 (3), 631-636 (1997)
   PUBMED   9126326
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Contreras,M., Sengupta,T.K., Sheikh,F., Aubourg,P. and Singh,I.
  TITLE     Topology of ATP-binding domain of adrenoleukodystrophy gene product
            in peroxisomes
  JOURNAL   Arch Biochem Biophys 334 (2), 369-379 (1996)
   PUBMED   8900413
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Kemp,S., Ligtenberg,M.J., van Geel,B.M., Barth,P.G.,
            Wolterman,R.A., Schoute,F., Sarde,C.O., Mandel,J.L., van Oost,B.A.
            and Bolhuis,P.A.
  TITLE     Identification of a two base pair deletion in five unrelated
            families with adrenoleukodystrophy: a possible hot spot for
            mutations
  JOURNAL   Biochem Biophys Res Commun 202 (2), 647-653 (1994)
   PUBMED   8048932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474099.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001059399.1, XP_343841.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132266,
                              SAMD00132270 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..737
                     /product="ATP-binding cassette sub-family D member 1"
                     /EC_number="7.6.2.4"
                     /note="ATP-binding cassette, sub-family D (ALD), member 1;
                     ATP-binding cassette, subfamily D (ALD), member 1;
                     adrenoleukodystrophy protein"
                     /calculated_mol_wt=81807
     Region          1..682
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Region          68..187
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000250|UniProtKB:P33897"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Region          68..85
                     /region_name="PEX19 binding site and required for
                     peroxisomal targeting.
                     /evidence=ECO:0000250|UniProtKB:P33897"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            132..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Site            474..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     Region          659..737
                     /region_name="Required for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:P33897"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZHR2.1)"
     CDS             1..737
                     /gene="Abcd1"
                     /gene_synonym="ALDP; RGD1562128"
                     /coded_by="NM_001108821.1:435..2648"
                     /db_xref="GeneID:363516"
                     /db_xref="RGD:1562128"
ORIGIN      
        1 mpvlstpsrp srvttlkrta vvlaltaygv hkiyplvrqc ltpargpqvp agestqeasg
       61 attakagmnr vflqrllvll rllfpgvlcr etgllalhsa alvsrtflsv yvarldgrla
      121 rcivrkdpra fswqllqwll ialpatfins airylegqla lsfrsrlvah ayglyfsqqt
      181 yyrvsnmdgr lrnpdqslte dmvafaasva hlysnltkpl ldvavtsytl lraarsrgag
      241 tawpsaiagl vvfltanvlr afspkfgelv aeearrkgel rymhsrvvan seeiafyggh
      301 evelallqhs yqdlasqinl illerlwyvm leqflmkyvw sasgllmvav piitatgyae
      361 sdseamkkaa lemkeeelvs erteaftiar nlltaaadat erimssykev telagytarv
      421 yemfqvfedv qhcrfkrtgd leeaqagpgs mvhsgvhieg plkiqgqvvd veqgiiceni
      481 piitptgevv vaslnirvee gmhllitgpn gcgksslfri lgglwptysg vlykpppqrm
      541 fyipqrpyms vgslrdqviy pdsaedmrrk gcseqqleai lgivhlrhil qreggweavc
      601 dwkdvlsgge kqrigmarmf yhrpkyalld ectsavsidv egkifqaakd agisllsith
      661 rpslwkyhth llqfdgeggw kfekldsaar lslteekqrl eqqlagipkm qgrlqelrqi
      721 lgeaaapvqp lvpgipt
//
LOCUS       NP_001013915             411 aa            linear   ROD 27-APR-2025
DEFINITION  actin-like protein 9 [Rattus norvegicus].
ACCESSION   NP_001013915 XP_218157
VERSION     NP_001013915.1
DBSOURCE    REFSEQ: accession NM_001013893.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079230.1.
            
            On Apr 20, 2005 this sequence version replaced XP_218157.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC079230.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..411
                     /product="actin-like protein 9"
                     /calculated_mol_wt=45971
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY16.1)"
     Region          47..410
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     CDS             1..411
                     /gene="Actl9b"
                     /gene_synonym="Actl9"
                     /coded_by="NM_001013893.1:56..1291"
                     /db_xref="GeneID:292516"
                     /db_xref="RGD:1359476"
ORIGIN      
        1 mdvngpkrwe phrsldlnpr stpvyksplq epcgvfgnkg ttkmsgvvid mgtgickmgf
       61 agqtrptyiv rnivgcqpkr rttmeqpkme mfigeaahar peltlmhpvr ngivvdweaa
      121 efiwrhilen dlrldtqdhp llftdppfnp asnreklvev afeslhspai yvasqsvlsv
      181 yangrvnglv vdtghgvsyt vpvfqgynlp sgiqrmdlag hyltkflaek ilrssfavkk
      241 edmdtmenik qqycyvaldf qkeqgrpdek frrclklpdg qmitvgkelf qcpellfhpp
      301 dtsgpsslgl psmvehslst vpqelradme qnvllcggss lftgfegrfk tellrrlgpe
      361 ahvvvvaqan rnlsvwiggs ilaslcafqt rwvlreqyee hgpdivlrkc s
//
LOCUS       NP_113702               1132 aa            linear   ROD 27-APR-2025
DEFINITION  tyrosine-protein kinase JAK2 [Rattus norvegicus].
ACCESSION   NP_113702
VERSION     NP_113702.1
DBSOURCE    REFSEQ: accession NM_031514.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Zhang,Z., Shang,G., Lu,Z., Hu,J., Liu,H., Lu,T. and Lu,X.
  TITLE     Daucosterol regulates JAK2-STAT3 signaling pathway to promote
            megakaryocyte differentiation
  JOURNAL   Blood Cells Mol Dis 107, 102858 (2024)
   PUBMED   38796983
  REMARK    GeneRIF: Daucosterol regulates JAK2-STAT3 signaling pathway to
            promote megakaryocyte differentiation.
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Xiong,C., Li,B., Song,R., Ma,Z., Huber,S.A. and Liu,W.
  TITLE     IFITM3 mediates inflammation induced myocardial injury through
            JAK2/STAT3 signaling pathway
  JOURNAL   Mol Immunol 167, 1-15 (2024)
   PUBMED   38306778
  REMARK    GeneRIF: IFITM3 mediates inflammation induced myocardial injury
            through JAK2/STAT3 signaling pathway.
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Yang,Z., Liang,Z., Rao,J., Xie,H., Zhou,M., Xu,X., Lin,Y., Lin,F.,
            Wang,C. and Chen,C.
  TITLE     Hypoxic-preconditioned mesenchymal stem cell-derived small
            extracellular vesicles promote the recovery of spinal cord injury
            by affecting the phenotype of astrocytes through the
            miR-21/JAK2/STAT3 pathway
  JOURNAL   CNS Neurosci Ther 30 (3), e14428 (2024)
   PUBMED   37641874
  REMARK    GeneRIF: Hypoxic-preconditioned mesenchymal stem cell-derived small
            extracellular vesicles promote the recovery of spinal cord injury
            by affecting the phenotype of astrocytes through the
            miR-21/JAK2/STAT3 pathway.
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Bao,H., Wang,X., Zhou,H., Zhou,W., Liao,F., Wei,F., Yang,S., Luo,Z.
            and Li,W.
  TITLE     PCSK9 regulates myofibroblast transformation through the JAK2/STAT3
            pathway to regulate fibrosis after myocardial infarction
  JOURNAL   Biochem Pharmacol 220, 115996 (2024)
   PUBMED   38154546
  REMARK    GeneRIF: PCSK9 regulates myofibroblast transformation through the
            JAK2/STAT3 pathway to regulate fibrosis after myocardial
            infarction.
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Alnajem,A. and Al-Maghrebi,M.
  TITLE     The Regulatory Effects of JAK2/STAT3 on Spermatogenesis and the
            Redox Keap1/Nrf2 Axis in an Animal Model of Testicular Ischemia
            Reperfusion Injury
  JOURNAL   Cells 12 (18), 2292 (2023)
   PUBMED   37759514
  REMARK    GeneRIF: The Regulatory Effects of JAK2/STAT3 on Spermatogenesis
            and the Redox Keap1/Nrf2 Axis in an Animal Model of Testicular
            Ischemia Reperfusion Injury.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Argetsinger,L.S., Hsu,G.W., Myers,M.G. Jr., Billestrup,N.,
            White,M.F. and Carter-Su,C.
  TITLE     Growth hormone, interferon-gamma, and leukemia inhibitory factor
            promoted tyrosyl phosphorylation of insulin receptor substrate-1
  JOURNAL   J Biol Chem 270 (24), 14685-14692 (1995)
   PUBMED   7782332
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Duhe,R.J., Rui,H., Greenwood,J.D., Garvey,K. and Farrar,W.L.
  TITLE     Cloning of the gene encoding rat JAK2, a protein tyrosine kinase
  JOURNAL   Gene 158 (2), 281-285 (1995)
   PUBMED   7607555
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   He,T.C., Jiang,N., Zhuang,H. and Wojchowski,D.M.
  TITLE     Erythropoietin-induced recruitment of Shc via a receptor
            phosphotyrosine-independent, Jak2-associated pathway
  JOURNAL   J Biol Chem 270 (19), 11055-11061 (1995)
   PUBMED   7538110
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Miura,O., Miura,Y., Nakamura,N., Quelle,F.W., Witthuhn,B.A.,
            Ihle,J.N. and Aoki,N.
  TITLE     Induction of tyrosine phosphorylation of Vav and expression of
            Pim-1 correlates with Jak2-mediated growth signaling from the
            erythropoietin receptor
  JOURNAL   Blood 84 (12), 4135-4141 (1994)
   PUBMED   7527668
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U13396.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U13396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..1132
                     /product="tyrosine-protein kinase JAK2"
                     /EC_number="2.7.10.2"
                     /note="JAK-2; Janus kinase 2 (a protein tyrosine kinase)"
                     /calculated_mol_wt=130455
     Region          1..239
                     /region_name="Interaction with cytokine/interferon/growth
                     hormone receptors. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62689.1)"
     Region          39..134
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Region          143..261
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          266..386
                     /region_name="FERM_C_JAK2"
                     /note="FERM domain C-lobe of Janus kinase (JAK) 2;
                     cd13333"
                     /db_xref="CDD:270141"
     Site            order(274,295,297,316)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270141"
     Site            order(320,325..328,366,370,373..374)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270141"
     Site            366..377
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270141"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Region          386..482
                     /region_name="SH2_Jak2"
                     /note="Src homology 2 (SH2) domain in the Janus kinase 2
                     (Jak2) proteins; cd10379"
                     /db_xref="CDD:198242"
     Site            order(406,426,451,453)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198242"
     Site            order(452,481)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198242"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Region          545..806
                     /region_name="PTK_Jak2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Janus kinase 2; cd05078"
                     /db_xref="CDD:270663"
     Site            order(551,554..555,557,559,579,581,626..629,633,673,
                     677..678,680,699,711..715,724,759)
                     /site_type="active"
                     /db_xref="CDD:270663"
     Site            order(551,554..555,557,559,579,581,626..629,633,673,
                     677..678,680)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270663"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O60674; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            617
                     /site_type="other"
                     /note="V617F mutation site"
                     /db_xref="CDD:270663"
     Site            order(673,677,711..715,724,759)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270663"
     Site            698..717
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270663"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Region          844..1127
                     /region_name="PTKc_Jak2_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Janus kinase 2; cd14205"
                     /db_xref="CDD:271107"
     Site            order(855..857,863,880,911,929..933,935,976,980..981,983,
                     993..994,1013..1017,1026,1075)
                     /site_type="active"
                     /db_xref="CDD:271107"
     Site            order(855..857,863,880,911,929..933,935,980..981,983,
                     993..994)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271107"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            order(976,980,1013..1017,1026,1075)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271107"
     Site            993..1019
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271107"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O60674; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:O60674; propagated from
                     UniProtKB/Swiss-Prot (Q62689.1)"
     CDS             1..1132
                     /gene="Jak2"
                     /coded_by="NM_031514.1:157..3555"
                     /db_xref="GeneID:24514"
                     /db_xref="RGD:2939"
ORIGIN      
        1 mgmacltmte megtstspah qngdipgnan svkqtepvlq vylyhslgqa egdylkfpng
       61 eyvaeeicva askacgitpv yhnmfalmse teriwyppnh vfhidestrh nilyrirfyf
      121 phwycsgsnr tyrygvsrga eapllddfvm sylfaqwrhd fvhgwikvpv thetqeeclg
      181 mavldmmria kekdqtplav ynsisyktfl pkcvrakiqd yhiltrkrir yrfrrfiqqf
      241 sqckatarnl klkylinlet lqsafyteqf evkesargps geeifatiii tgnggiqwsr
      301 gkhkesetlt eqdlqlycdf pdiidvsikq anqecstesr vvtvhkqdgk vleielsslk
      361 ealsfvslid gyyrltadah hylckevapp avlenihsnc hgpismdfai sklkkagnqt
      421 glyvlrcspk dfnkyfltfa verenvieyk hclitkneng eynlsgtkrn fsslkdllnc
      481 yqmetvrsds iifqftkccp pkpkdksnll vfrtngvsdv qlsptlqrhn nvnqmvfhki
      541 rnedlifnes lgqgtftkif kgvrrevgdy gqlhetevll kvldkahrny sesffeaasm
      601 msqlshkhlv lnygvcvcge enilvqefvk fgsldtylkk nknsinilwk lgvakqlawa
      661 mhfleeksli hgnvcaknil lireedrktg nppfiklsdp gisitvlpkd ilqeripwvp
      721 pecienpknl tlatdkwsfg ttlweicsgg dkplsaldsq rklqfyedkh qlpapkwtel
      781 anlintcmdy epdfrpafra virdlnslft pdyelltend mlpnmrigal gfsgafedrd
      841 ptqfeerhlk flqqlgkgnf gsvemcrydp lqdntgevva vkklqhstee hlrdfereie
      901 ilkslqhdni vkykgvcysa grrnlrlime ylpygslrdy lqkhkeridh kkllqytsqi
      961 ckgmeylgtk ryihrdlatr nilvenenrv kigdfgltkv lpqdkeyykv kepgespifw
     1021 yapesltesk fsvasdvwsf gvvlyelfty ieksksppve fmrmigndkq gqmivfhlie
     1081 llknngrlpr pegcpdeiyv imtecwnnnv nqrpsfrdls lrvdqirdsm aa
//
LOCUS       NP_001007734             219 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-sugar pyrophosphatase [Rattus norvegicus].
ACCESSION   NP_001007734 XP_341560
VERSION     NP_001007734.1
DBSOURCE    REFSEQ: accession NM_001007733.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Wright,R.H., Lioutas,A., Le Dily,F., Soronellas,D., Pohl,A.,
            Bonet,J., Nacht,A.S., Samino,S., Font-Mateu,J., Vicent,G.P.,
            Wierer,M., Trabado,M.A., Schelhorn,C., Carolis,C., Macias,M.J.,
            Yanes,O., Oliva,B. and Beato,M.
  TITLE     ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
            chromatin remodeling
  JOURNAL   Science 352 (6290), 1221-1225 (2016)
   PUBMED   27257257
REFERENCE   2  (residues 1 to 219)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Ito,R., Sekiguchi,M., Setoyama,D., Nakatsu,Y., Yamagata,Y. and
            Hayakawa,H.
  TITLE     Cleavage of oxidized guanine nucleotide and ADP sugar by human
            NUDT5 protein
  JOURNAL   J Biochem 149 (6), 731-738 (2011)
   PUBMED   21389046
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Kamiya,H., Hori,M., Arimori,T., Sekiguchi,M., Yamagata,Y. and
            Harashima,H.
  TITLE     NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with
            broad substrate specificity
  JOURNAL   DNA Repair (Amst) 8 (10), 1250-1254 (2009)
   PUBMED   19699693
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Zha,M., Guo,Q., Zhang,Y., Yu,B., Ou,Y., Zhong,C. and Ding,J.
  TITLE     Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from
            structural and kinetic studies
  JOURNAL   J Mol Biol 379 (3), 568-578 (2008)
   PUBMED   18462755
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Zha,M., Zhong,C., Peng,Y., Hu,H. and Ding,J.
  TITLE     Crystal structures of human NUDT5 reveal insights into the
            structural basis of the substrate specificity
  JOURNAL   J Mol Biol 364 (5), 1021-1033 (2006)
   PUBMED   17052728
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Yang,H., Slupska,M.M., Wei,Y.F., Tai,J.H., Luther,W.M., Xia,Y.R.,
            Shih,D.M., Chiang,J.H., Baikalov,C., Fitz-Gibbon,S., Phan,I.T.,
            Conrad,A. and Miller,J.H.
  TITLE     Cloning and characterization of a new member of the Nudix
            hydrolases from human and mouse
  JOURNAL   J Biol Chem 275 (12), 8844-8853 (2000)
   PUBMED   10722730
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Gasmi,L., Cartwright,J.L. and McLennan,A.G.
  TITLE     Cloning, expression and characterization of YSA1H, a human
            adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif
  JOURNAL   Biochem J 344 Pt 2 (Pt 2), 331-337 (1999)
   PUBMED   10567213
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079176.1.
            
            On Nov 29, 2004 this sequence version replaced XP_341560.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079176.1, CK474906.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..219
                     /product="ADP-sugar pyrophosphatase"
                     /EC_number="3.6.1.13"
                     /EC_number="3.6.1.58"
                     /EC_number="2.7.7.96"
                     /note="nudix motif 5; nucleoside diphosphate-linked moiety
                     X motif 5; nudix-type motif 5; 8-oxo-dGDP phosphatase;
                     nudix (nucleoside diphosphate linked moiety X)-type motif
                     5; nuclear ATP-synthesis protein NUDIX5"
                     /calculated_mol_wt=23986
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKK9; propagated from
                     UniProtKB/Swiss-Prot (Q6AY63.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKK9; propagated from
                     UniProtKB/Swiss-Prot (Q6AY63.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKK9; propagated from
                     UniProtKB/Swiss-Prot (Q6AY63.1)"
     Region          59..205
                     /region_name="NUDIX_ADPRase_Nudt5"
                     /note="ADP-ribose pyrophosphatase; cd18888"
                     /db_xref="CDD:467598"
     Region          97..118
                     /region_name="Nudix box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY63.1)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKK9; propagated from
                     UniProtKB/Swiss-Prot (Q6AY63.1)"
     Site            218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKK9; propagated from
                     UniProtKB/Swiss-Prot (Q6AY63.1)"
     CDS             1..219
                     /gene="Nudt5"
                     /coded_by="NM_001007733.1:150..809"
                     /db_xref="GeneID:361274"
                     /db_xref="RGD:1359284"
ORIGIN      
        1 metqepkdss ppteqrilse elisegkwvk fekttymdpt gktrtwetvk lttrkgksad
       61 avsvipvlqr tlhhecivlv kqfrppmggy clefpaglie dgespeaaal releeetgyk
      121 gdiaecspav cmdpglsnct thvvtvting ddagnvrpkp kpgdgefvev islpkndllt
      181 rldalgaedr ltvdarvyay alalkhanak pfevpflkf
//
LOCUS       NP_001032854             207 aa            linear   ROD 27-APR-2025
DEFINITION  SPRY domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_001032854 XP_222316
VERSION     NP_001032854.1
DBSOURCE    REFSEQ: accession NM_001037765.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Zhong,Z., Zhang,H., Bai,M., Ni,J., Wan,B., Chen,X. and Yu,L.
  TITLE     Cloning and characterization of a novel human SPRYD4 gene encoding
            a putative SPRY domain-containing protein
  JOURNAL   DNA Seq 19 (1), 68-72 (2008)
   PUBMED   17852359
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099138.1.
            
            On Dec 16, 2005 this sequence version replaced XP_222316.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099138.1, CK599461.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..207
                     /product="SPRY domain-containing protein 4"
                     /calculated_mol_wt=23119
     Region          32..200
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91WK1; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT8.1)"
     Site            130
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8WW59; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT8.1)"
     CDS             1..207
                     /gene="Spryd4"
                     /gene_synonym="RGD1306649"
                     /coded_by="NM_001037765.1:7..630"
                     /db_xref="GeneID:288772"
                     /db_xref="RGD:1306649"
ORIGIN      
        1 malpfarcwn lyrwgtkrwg vtagesrrgi sfkleektah sslalfrgdt gvkyglvgle
       61 ptkvalnler frdwavvlad ttvtsgrhyw evtvkrsqqf rigvadvdms rdscvgaddr
      121 swvfsyaqrk whsmlaneka pikgigqpek vgllldyeak klslvdvnri svihtlqtdf
      181 rgpvapafal wdgellthsg levpkgl
//
LOCUS       NP_001008336             407 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic initiation factor 4A-II [Rattus norvegicus].
ACCESSION   NP_001008336 XP_221325
VERSION     NP_001008336.1
DBSOURCE    REFSEQ: accession NM_001008335.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Lu,W.T., Wilczynska,A., Smith,E. and Bushell,M.
  TITLE     The diverse roles of the eIF4A family: you are the company you keep
  JOURNAL   Biochem Soc Trans 42 (1), 166-172 (2014)
   PUBMED   24450646
  REMARK    Review article
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Parsyan,A., Svitkin,Y., Shahbazian,D., Gkogkas,C., Lasko,P.,
            Merrick,W.C. and Sonenberg,N.
  TITLE     mRNA helicases: the tacticians of translational control
  JOURNAL   Nat Rev Mol Cell Biol 12 (4), 235-245 (2011)
   PUBMED   21427765
  REMARK    Review article
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Kyono,K., Miyashiro,M. and Taguchi,I.
  TITLE     Human eukaryotic initiation factor 4AII associates with hepatitis C
            virus NS5B protein in vitro
  JOURNAL   Biochem Biophys Res Commun 292 (3), 659-666 (2002)
   PUBMED   11922617
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Selvamurugan,N., Joost,O.H., Haas,E.S., Brown,J.W., Galvin,N.J. and
            Eliceiri,G.L.
  TITLE     Intracellular localization and unique conserved sequences of three
            small nucleolar RNAs
  JOURNAL   Nucleic Acids Res 25 (8), 1591-1596 (1997)
   PUBMED   9092667
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085859.1.
            
            On Dec 16, 2004 this sequence version replaced XP_221325.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085859.1, SRR8487230.144060.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..407
                     /product="eukaryotic initiation factor 4A-II"
                     /EC_number="3.6.4.13"
                     /note="protein synthesis initiation factor 4AII; eIF4A-II;
                     eIF-4A-II; ATP-dependent RNA helicase eIF4A-2; eukaryotic
                     translation initiation factor 4A"
                     /calculated_mol_wt=46271
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI1.1)"
     Region          21..407
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          33..61
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI1.1)"
     Site            order(35,53,55,60,79..85)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350804"
     Site            order(36,46,49,54)
                     /site_type="other"
                     /note="eIF4G interface [polypeptide binding]"
                     /db_xref="CDD:350804"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14240; propagated from
                     UniProtKB/Swiss-Prot (Q5RKI1.1)"
     Region          183..186
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKI1.1)"
     CDS             1..407
                     /gene="Eif4a2"
                     /coded_by="NM_001008335.1:22..1245"
                     /db_xref="GeneID:303831"
                     /db_xref="RGD:1309225"
ORIGIN      
        1 msggsadynr ehggpegmdp dgviesnwne ivdnfddmnl kesllrgiya ygfekpsaiq
       61 qraiipcikg ydviaqaqsg tgktatfais ilqqleiefk etqalvlapt relaqqiqkv
      121 ilalgdymga tchaciggtn vrnemqklqa eaphivvgtp grvfdmlnrr ylspkwikmf
      181 vldeademls rgfkdqiyei fqklntsiqv vllsatmptd vlevtkkfmr dpirilvkke
      241 eltlegikqf yinvereewk ldtlcdlyet ltitqavifl ntrrkvdwlt ekmhardftv
      301 salhgdmdqk erdvimrefr sgssrvlitt dllargidvq qvslvinydl ptnrenyihr
      361 igrggrfgrk gvainfvtee dkrilrdiet fynttveemp mnvadli
//
LOCUS       NP_037229                284 aa            linear   ROD 27-APR-2025
DEFINITION  deoxyribonuclease-1 precursor [Rattus norvegicus].
ACCESSION   NP_037229
VERSION     NP_037229.1
DBSOURCE    REFSEQ: accession NM_013097.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Fahmi,T., Wang,X., Zhdanov,D.D., Islam,I., Apostolov,E.O.,
            Savenka,A.V. and Basnakian,A.G.
  TITLE     DNase I Induces Other Endonucleases in Kidney Tubular Epithelial
            Cells by Its DNA-Degrading Activity
  JOURNAL   Int J Mol Sci 21 (22), 8665 (2020)
   PUBMED   33212932
  REMARK    GeneRIF: DNase I Induces Other Endonucleases in Kidney Tubular
            Epithelial Cells by Its DNA-Degrading Activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Jimenez-Alcazar,M., Rangaswamy,C., Panda,R., Bitterling,J.,
            Simsek,Y.J., Long,A.T., Bilyy,R., Krenn,V., Renne,C., Renne,T.,
            Kluge,S., Panzer,U., Mizuta,R., Mannherz,H.G., Kitamura,D.,
            Herrmann,M., Napirei,M. and Fuchs,T.A.
  TITLE     Host DNases prevent vascular occlusion by neutrophil extracellular
            traps
  JOURNAL   Science 358 (6367), 1202-1206 (2017)
   PUBMED   29191910
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Gatselis,N.K., Vakrakou,A.G., Zachou,K., Androutsakos,T.,
            Azariadis,K., Hatzis,G., Manoussakis,M.N. and Dalekos,G.N.
  TITLE     Decreased serum DNase1-activity in patients with autoimmune liver
            diseases
  JOURNAL   Autoimmunity 50 (2), 125-132 (2017)
   PUBMED   28263100
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Udayanga,K.G., Miyata,H., Yokoo,Y., Qi,W.M., Takahara,E.,
            Mantani,Y., Yokoyama,T., Hoshi,N. and Kitagawa,H.
  TITLE     Immunohistochemical study of the apoptosis process in epidermal
            epithelial cells of rats under a physiological condition
  JOURNAL   Histol Histopathol 26 (7), 811-820 (2011)
   PUBMED   21630211
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Napirei,M., Wulf,S., Eulitz,D., Mannherz,H.G. and Kloeckl,T.
  TITLE     Comparative characterization of rat deoxyribonuclease 1 (Dnase1)
            and murine deoxyribonuclease 1-like 3 (Dnase1l3)
  JOURNAL   Biochem J 389 (Pt 2), 355-364 (2005)
   PUBMED   15796714
  REMARK    GeneRIF: A comparison of the expression and transport of DNAse1
            from rats and DNAse1L3 from mice is reported.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Basnakian,A.G., Singh,A.B. and Shah,S.V.
  TITLE     Identification and expression of deoxyribonuclease (DNase) I
            alternative transcripts in the rat
  JOURNAL   Gene 289 (1-2), 87-96 (2002)
   PUBMED   12036587
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Tsutsumi,S., Kaneko,Y., Asao,T., Kuwano,H., Kudo,S., Takeshita,H.,
            Yasuda,T. and Kishi,K.
  TITLE     DNase I is present in the chief cells of human and rat stomachs
  JOURNAL   Histochem J 33 (9-10), 531-535 (2001)
   PUBMED   12005024
  REMARK    GeneRIF: results show that the chief cells of the stomach produce
            DNase I
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Liu,Q.Y., Ribecco,M., Hou,Y., Walker,P.R. and Sikorska,M.
  TITLE     DNase I primary transcript is alternatively spliced in both normal
            and apoptotic cells: no evidence of up-regulation in apoptosis
  JOURNAL   DNA Cell Biol 16 (8), 911-918 (1997)
   PUBMED   9303433
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Peitsch,M.C., Polzar,B., Stephan,H., Crompton,T., MacDonald,H.R.,
            Mannherz,H.G. and Tschopp,J.
  TITLE     Characterization of the endogenous deoxyribonuclease involved in
            nuclear DNA degradation during apoptosis (programmed cell death)
  JOURNAL   EMBO J 12 (1), 371-377 (1993)
   PUBMED   8428592
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Polzar,B. and Mannherz,H.G.
  TITLE     Nucleotide sequence of a full length cDNA clone encoding the
            deoxyribonuclease I from the rat parotid gland
  JOURNAL   Nucleic Acids Res 18 (23), 7151 (1990)
   PUBMED   2263485
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF397150.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089764.1, AF397150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..284
                     /product="deoxyribonuclease-1 precursor"
                     /EC_number="3.1.21.1"
                     /note="alternatively spliced; DNase I; deoxyribonuclease
                     I"
                     /calculated_mol_wt=29677
     sig_peptide     1..22
                     /note="/evidence=ECO:0000250|UniProtKB:P00639; propagated
                     from UniProtKB/Swiss-Prot (P21704.1)"
                     /calculated_mol_wt=2406
     Region          20..282
                     /region_name="DNaseIc"
                     /note="deoxyribonuclease I; smart00476"
                     /db_xref="CDD:128752"
     mat_peptide     23..284
                     /product="Deoxyribonuclease-1. /id=PRO_0000007281"
                     /note="propagated from UniProtKB/Swiss-Prot (P21704.1)"
                     /calculated_mol_wt=29677
     Site            order(29..30,32,36,61,63..65,97..98,100,133,156,159,190,
                     192,197,229,233..234,273..274)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197337"
     Site            order(29,61,100,156,190,192,234,273..274)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197337"
     Site            order(29,61,273)
                     /site_type="other"
                     /note="putative Mg binding site IVb [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(31,156,190,192,274)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197337"
     Site            31
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:197337"
     Site            order(32,36,63..65,97..98,100,133,156,159,190,192,197,233,
                     274)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:197337"
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21704.1)"
     Site            87
                     /site_type="other"
                     /note="Nitration by tetranitromethane destroys a Ca(2+)
                     binding site and inactivates enzyme.
                     /evidence=ECO:0000250|UniProtKB:P00639; propagated from
                     UniProtKB/Swiss-Prot (P21704.1)"
     Site            order(121,134)
                     /site_type="other"
                     /note="Ca binding site II [ion binding]"
                     /db_xref="CDD:197337"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21704.1)"
     Site            order(190,234,274)
                     /site_type="other"
                     /note="putative Mg binding site IVa [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(194,220)
                     /site_type="metal-binding"
                     /note="metal binding site III [ion binding]"
                     /db_xref="CDD:197337"
     Site            order(223,225)
                     /site_type="other"
                     /note="Ca binding site I [ion binding]"
                     /db_xref="CDD:197337"
     CDS             1..284
                     /gene="Dnase1"
                     /coded_by="NM_013097.2:279..1133"
                     /db_xref="GeneID:25633"
                     /db_xref="RGD:2510"
ORIGIN      
        1 mrytglmgil ltlvnllqla atlriaafni rtfgdtkmsn atlssyivki lsrydiavvq
       61 evrdthlvav gklldelnrd ipdnyryiis eplgrksyke qylfvyrpsq vsvldsyhyd
      121 dgcepcgndt fsrepaivkf fspytevref aivplhsapt eavseidaly dvyldvrqkw
      181 gledimfmgd fnagcsyvts sqwssirlrt spifqwlipd sadttatsth caydrivvag
      241 allqaavvps savpfdfqae yrltnqmaea isdhypvevt lrkt
//
LOCUS       NP_599193                192 aa            linear   ROD 27-APR-2025
DEFINITION  ras-related C3 botulinum toxin substrate 1 [Rattus norvegicus].
ACCESSION   NP_599193 XP_344080
VERSION     NP_599193.1
DBSOURCE    REFSEQ: accession NM_134366.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Wan,Y., Zhou,J., Zhang,P., Lin,X. and Li,H.
  TITLE     Inhibition of spinal Rac1 attenuates chronic inflammatory pain by
            regulating the activation of astrocytes
  JOURNAL   Cell Signal 114, 110972 (2024)
   PUBMED   37984604
  REMARK    GeneRIF: Inhibition of spinal Rac1 attenuates chronic inflammatory
            pain by regulating the activation of astrocytes.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Fu,H., Zhang,P., Zhao,X.D. and Zhong,X.Y.
  TITLE     Interfering with Rac1-activation during neonatal
            monocyte-macrophage differentiation influences the inflammatory
            responses of M1 macrophages
  JOURNAL   Cell Death Dis 14 (9), 619 (2023)
   PUBMED   37735499
  REMARK    GeneRIF: Interfering with Rac1-activation during neonatal
            monocyte-macrophage differentiation influences the inflammatory
            responses of M1 macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Dalto,J.F. and Medina,J.H.
  TITLE     Time-dependent inhibition of Rac1 in the VTA enhances long-term
            aversive memory: implications in active forgetting mechanisms
  JOURNAL   Sci Rep 13 (1), 13507 (2023)
   PUBMED   37598223
  REMARK    GeneRIF: Time-dependent inhibition of Rac1 in the VTA enhances
            long-term aversive memory: implications in active forgetting
            mechanisms.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Li,C., Li,Y., Li,Y., Wang,Y., Teng,Y. and Hao,Y.
  TITLE     MicroRNA-194-5p attenuates hypoxia/reoxygenation-induced apoptosis
            in H9C2 cardiomyocytes by inhibiting the over-activation of RAC1
            protein
  JOURNAL   Mol Med Rep 27 (2) (2023)
   PUBMED   36562344
  REMARK    GeneRIF: MicroRNA1945p attenuates hypoxia/reoxygenationinduced
            apoptosis in H9C2 cardiomyocytes by inhibiting the overactivation
            of RAC1 protein.
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Xu,L., Yang,L., Wu,Y., Wan,X., Tang,X., Xu,Y., Chen,Q., Liu,Y. and
            Liu,S.
  TITLE     Rac1/PAK1 signaling contributes to bone cancer pain by Regulation
            dendritic spine remodeling in rats
  JOURNAL   Mol Pain 19, 17448069231161031 (2023)
   PUBMED   36938611
  REMARK    GeneRIF: Rac1/PAK1 signaling contributes to bone cancer pain by
            Regulation dendritic spine remodeling in rats.
            Erratum:[Mol Pain. 2023 Jan-Dec;19:17448069231182501. doi:
            10.1177/17448069231182501. PMID: 37608691]
REFERENCE   6  (residues 1 to 192)
  AUTHORS   D'Souza-Schorey,C., Boshans,R.L., McDonough,M., Stahl,P.D. and Van
            Aelst,L.
  TITLE     A role for POR1, a Rac1-interacting protein, in ARF6-mediated
            cytoskeletal rearrangements
  JOURNAL   EMBO J 16 (17), 5445-5454 (1997)
   PUBMED   9312003
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Fanger,G.R., Johnson,N.L. and Johnson,G.L.
  TITLE     MEK kinases are regulated by EGF and selectively interact with
            Rac/Cdc42
  JOURNAL   EMBO J 16 (16), 4961-4972 (1997)
   PUBMED   9305638
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Teramoto,H., Coso,O.A., Miyata,H., Igishi,T., Miki,T. and
            Gutkind,J.S.
  TITLE     Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the
            c-Jun N-terminal kinase/stress-activated protein kinase pathway. A
            role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel
            member of the mixed lineage kinase family
  JOURNAL   J Biol Chem 271 (44), 27225-27228 (1996)
   PUBMED   8910292
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Symons,M., Derry,J.M., Karlak,B., Jiang,S., Lemahieu,V.,
            Mccormick,F., Francke,U. and Abo,A.
  TITLE     Wiskott-Aldrich syndrome protein, a novel effector for the GTPase
            CDC42Hs, is implicated in actin polymerization
  JOURNAL   Cell 84 (5), 723-734 (1996)
   PUBMED   8625410
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Best,A., Ahmed,S., Kozma,R. and Lim,L.
  TITLE     The Ras-related GTPase Rac1 binds tubulin
  JOURNAL   J Biol Chem 271 (7), 3756-3762 (1996)
   PUBMED   8631991
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY491395.1.
            
            On Oct 25, 2004 this sequence version replaced XP_344080.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY491395.1, EV778673.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..192
                     /product="ras-related C3 botulinum toxin substrate 1"
                     /EC_number="3.6.5.2"
                     /note="rho family, small GTP binding protein Rac1;
                     p21-Rac1; ras-related C3 botulinum toxin substrate 1 (rho
                     family small GTP binding protein Rac1)"
                     /calculated_mol_wt=21319
     mat_peptide     1..189
                     /product="Ras-related C3 botulinum toxin substrate 1.
                     /id=PRO_0000042040"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RUV5.1)"
                     /calculated_mol_wt=21111
     Region          3..176
                     /region_name="Rac1_like"
                     /note="Ras-related C3 botulinum toxin substrate 1 (rho
                     family, small GTP binding protein Rac1)-like consists of
                     Rac1, Rac2 and Rac3; cd01871"
                     /db_xref="CDD:206663"
     Site            order(3,5,31..32,35..36,38..39,41,43,52,56..61,64..67,
                     70..71,73..74)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206663"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206663"
     Site            order(13,15..18,116,118..119,159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206663"
     Site            order(22,25..26,28,30..31,160,162)
                     /site_type="active"
                     /note="p67PhoxTPR effector interaction site [active]"
                     /db_xref="CDD:206663"
     Site            25..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206663"
     Site            order(32,34,36..38,61..64,67,70)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206663"
     Region          32..40
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RUV5.1)"
     Site            order(35..36,59,64,66..67,69..70,73,103..104,106)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206663"
     Site            order(35..37,39,56..58,64,67,70..71,73..74)
                     /site_type="other"
                     /note="Arfaptin/Por effector interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206663"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206663"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206663"
     Site            60..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206663"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63000; propagated from
                     UniProtKB/Swiss-Prot (Q6RUV5.1)"
     Site            115..118
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206663"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206663"
     Region          179..188
                     /region_name="Polybasic region, required for nuclear
                     import. /evidence=ECO:0000250|UniProtKB:P63000"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6RUV5.1)"
     Site            189
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P63000; propagated from
                     UniProtKB/Swiss-Prot (Q6RUV5.1)"
     CDS             1..192
                     /gene="Rac1"
                     /coded_by="NM_134366.1:1..579"
                     /db_xref="GeneID:363875"
                     /db_xref="RGD:619755"
ORIGIN      
        1 mqaikcvvvg dgavgktcll isyttnafpg eyiptvfdny sanvmvdgkp vnlglwdtag
       61 qedydrlrpl sypqtdvfli cfslvspasf envrakwype vrhhcpntpi ilvgtkldlr
      121 ddkdtieklk ekkltpityp qglamakeig avkylecsal tqrglktvfd eairavlcpp
      181 pvkkrkrkcl ll
//
LOCUS       NP_001008351             211 aa            linear   ROD 27-APR-2025
DEFINITION  transcription initiation factor TFIID subunit 11 [Rattus
            norvegicus].
ACCESSION   NP_001008351 XP_228026
VERSION     NP_001008351.1
DBSOURCE    REFSEQ: accession NM_001008350.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Malkowska,M., Kokoszynska,K., Rychlewski,L. and Wyrwicz,L.
  TITLE     Structural bioinformatics of the general transcription factor TFIID
  JOURNAL   Biochimie 95 (4), 680-691 (2013)
   PUBMED   23146842
  REMARK    Review article
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Tatarakis,A., Margaritis,T., Martinez-Jimenez,C.P., Kouskouti,A.,
            Mohan,W.S. 2nd, Haroniti,A., Kafetzopoulos,D., Tora,L. and
            Talianidis,I.
  TITLE     Dominant and redundant functions of TFIID involved in the
            regulation of hepatic genes
  JOURNAL   Mol Cell 31 (4), 531-543 (2008)
   PUBMED   18722179
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Mengus,G., Gangloff,Y.G., Carre,L., Lavigne,A.C. and Davidson,I.
  TITLE     The human transcription factor IID subunit human TATA-binding
            protein-associated factor 28 interacts in a ligand-reversible
            manner with the vitamin D(3) and thyroid hormone receptors
  JOURNAL   J Biol Chem 275 (14), 10064-10071 (2000)
   PUBMED   10744685
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Caron,C., Mengus,G., Dubrowskaya,V., Roisin,A., Davidson,I. and
            Jalinot,P.
  TITLE     Human TAF(II)28 interacts with the human T cell leukemia virus type
            I Tax transactivator and promotes its transcriptional activity
  JOURNAL   Proc Natl Acad Sci U S A 94 (8), 3662-3667 (1997)
   PUBMED   9108034
REFERENCE   6  (residues 1 to 211)
  AUTHORS   May,M., Mengus,G., Lavigne,A.C., Chambon,P. and Davidson,I.
  TITLE     Human TAF(II28) promotes transcriptional stimulation by activation
            function 2 of the retinoid X receptors
  JOURNAL   EMBO J 15 (12), 3093-3104 (1996)
   PUBMED   8670810
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Mengus,G., May,M., Jacq,X., Staub,A., Tora,L., Chambon,P. and
            Davidson,I.
  TITLE     Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28:
            three subunits of the human transcription factor TFIID
  JOURNAL   EMBO J 14 (7), 1520-1531 (1995)
   PUBMED   7729427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086421.1.
            
            On Dec 16, 2004 this sequence version replaced XP_228026.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086421.1, CO382774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132291,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..211
                     /product="transcription initiation factor TFIID subunit
                     11"
                     /note="TATA box binding protein (TBP)-associated factor
                     11; TAFII28; TAFII-28; TAF(II)28; TFIID subunit p30-beta;
                     transcription initiation factor TFIID 28 kDa subunit;
                     TAF11 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor"
                     /calculated_mol_wt=23175
     Region          1..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U1X0.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q15544; propagated from
                     UniProtKB/Swiss-Prot (Q5U1X0.1)"
     Region          108..193
                     /region_name="TAFII28"
                     /note="hTAFII28-like protein conserved region; pfam04719"
                     /db_xref="CDD:428086"
     Site            order(113,115,118..119,121..123,125..126,131,148,152,161,
                     172,175..176,183..185,188..189,191..193,195..197)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467028"
     Site            order(116,119..120,123..124,127..130,133..134,137..138,
                     141..142,157..159,161..163,166,170,181..184,187..188,191)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467028"
     CDS             1..211
                     /gene="Taf11"
                     /coded_by="NM_001008350.1:80..715"
                     /db_xref="GeneID:309638"
                     /db_xref="RGD:1305626"
ORIGIN      
        1 mdnlgesptd kagepgesee tratpgapvs adtegipeet dqvgdadske aaaeeselks
       61 qdvsdvtaae redpslltpa akklkldtkd kkekkqkvde deiqkmqilv ssfseeqlnr
      121 yemyrrsafp kaaikrliqs itgtsvsqnv viamsgiskv fvgevveeal dvcekwgemp
      181 plqpkhmrea vrrlkskgqi pnskhkkitf f
//
LOCUS       NP_077070                673 aa            linear   ROD 27-APR-2025
DEFINITION  annexin A6 [Rattus norvegicus].
ACCESSION   NP_077070 XP_346393
VERSION     NP_077070.2
DBSOURCE    REFSEQ: accession NM_024156.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Cui,L., Rashdan,N.A., Zhu,D., Milne,E.M., Ajuh,P., Milne,G.,
            Helfrich,M.H., Lim,K., Prasad,S., Lerman,D.A., Vesey,A.T.,
            Dweck,M.R., Jenkins,W.S., Newby,D.E., Farquharson,C. and
            Macrae,V.E.
  TITLE     End stage renal disease-induced hypercalcemia may promote aortic
            valve calcification via Annexin VI enrichment of valve interstitial
            cell derived-matrix vesicles
  JOURNAL   J Cell Physiol 232 (11), 2985-2995 (2017)
   PUBMED   28369848
  REMARK    GeneRIF: Annexin VI is enriched in calcifying valve interstitial
            cell derived-matrix vesicles from patients with end stage renal
            disease-induced hypercalcemia and aortic valve calcification.
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Banerjee,P. and Bandyopadhyay,A.
  TITLE     Cytosolic dynamics of annexin A6 trigger feedback regulation of
            hypertrophy via atrial natriuretic peptide in cardiomyocytes
  JOURNAL   J Biol Chem 289 (9), 5371-5385 (2014)
   PUBMED   24403064
  REMARK    GeneRIF: the present study delivers a cooperative mechanism where
            Anxa6 potentiates ANP-dependent counterhypertrophic responses in
            cardiomyocytes by facilitating regulated traffic of pro-ANP.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Alvares,K., Stern,P.H. and Veis,A.
  TITLE     Dentin phosphoprotein binds annexin 2 and is involved in calcium
            transport in rat kidney ureteric bud cells
  JOURNAL   J Biol Chem 288 (18), 13036-13045 (2013)
   PUBMED   23525114
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Domon,M.M., Besson,F., Tylki-Szymanska,A., Bandorowicz-Pikula,J.
            and Pikula,S.
  TITLE     Interaction of AnxA6 with isolated and artificial lipid
            microdomains; importance of lipid composition and calcium content
  JOURNAL   Mol Biosyst 9 (4), 668-676 (2013)
   PUBMED   23360953
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Chow,A., Davis,A.J. and Gawler,D.J.
  TITLE     Identification of a novel protein complex containing annexin VI,
            Fyn, Pyk2, and the p120(GAP) C2 domain
  JOURNAL   FEBS Lett 469 (1), 88-92 (2000)
   PUBMED   10708762
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Fan,H., Josic,D., Lim,Y.P. and Reutter,W.
  TITLE     cDNA cloning and tissue-specific regulation of expression of rat
            calcium-binding protein 65/67. Identification as a homologue of
            annexin VI
  JOURNAL   Eur J Biochem 230 (2), 741-751 (1995)
   PUBMED   7607247
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Doubell,A.F., Lazure,C., Charbonneau,C. and Thibault,G.
  TITLE     Identification and immunolocalisation of annexins V and VI, the
            major cardiac annexins, in rat heart
  JOURNAL   Cardiovasc Res 27 (7), 1359-1367 (1993)
   PUBMED   8252600
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Mizutani,A., Usuda,N., Tokumitsu,H., Minami,H., Yasui,K.,
            Kobayashi,R. and Hidaka,H.
  TITLE     CAP-50, a newly identified annexin, localizes in nuclei of cultured
            fibroblast 3Y1 cells
  JOURNAL   J Biol Chem 267 (19), 13498-13504 (1992)
   PUBMED   1618851
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Blackwood,R.A. and Ernst,J.D.
  TITLE     Characterization of Ca2(+)-dependent phospholipid binding, vesicle
            aggregation and membrane fusion by annexins
  JOURNAL   Biochem J 266 (1), 195-200 (1990)
   PUBMED   2138016
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB585592.1 and BC072523.1.
            
            On Mar 14, 2007 this sequence version replaced NP_077070.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072523.1, SRR8487227.28378.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..673
                     /product="annexin A6"
                     /note="lipocortin VI; chromobindin-20; 67 kDa calelectrin;
                     calphobindin-II; calcium-binding protein CATA 65/67; CBP
                     65/67; annexin-6; calcium-binding protein 65/67; annexin
                     VI"
                     /calculated_mol_wt=75625
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          20..91
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          24..89
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          92..163
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          97..161
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          175..247
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          179..245
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14824; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          251..322
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          255..320
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            306
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          363..434
                     /region_name="Annexin 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          368..432
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            370
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            418
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          435..506
                     /region_name="Annexin 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          439..504
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            483
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          521..595
                     /region_name="Annexin 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          527..593
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     Region          599..670
                     /region_name="Annexin 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P48037.2)"
     Region          603..668
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            620
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08133; propagated from
                     UniProtKB/Swiss-Prot (P48037.2)"
     CDS             1..673
                     /gene="Anxa6"
                     /gene_synonym="Anx6; CPB-II"
                     /coded_by="NM_024156.2:107..2128"
                     /db_xref="GeneID:79125"
                     /db_xref="RGD:621172"
ORIGIN      
        1 makiaqgamy rgsvhdfadf danqdaealy tamkgfgsdk esilelitsr snkqrqeicq
       61 sykslygkdl iadlkyeltg kferlivnlm rplaycdake ikdaisgigt dekclieila
      121 srtneqihql vaaykdayer dlesdiigdt sghfqkmlvv llqgtrendd vvsedlvqqd
      181 vqdlyeagel kwgtdeaqfi yilgnrskqh lrlvfdeylk ttgkpieasi rgelsgdfek
      241 lmlavvkcir stpeyfaerl fkamkglgtr dntlirimvs rseldmldir eifrtkyeks
      301 lysmikndts geykkallkl cggdddaagq ffpeaaqvay qmwelsavsr velkgtvraa
      361 ndfnpdadak alrkamkgig tdeatiidii tqrsnaqrqq irqtfkshfg rdlmadlkse
      421 isgdlarlil glmmppahyd akqlkkameg agtdekalie ilatrtnaei raineayked
      481 yhksledals sdtsghfkri lislatgnre eggenrdqaq edaqvaaeil eiadtpsgdk
      541 tsletrfmtv lctrsyphlr rvfqefikkt nydiehvikk emsgdvkdaf vaivqsvknk
      601 plffadklyk smkgagtdek tltrvmvsrs eidllnirre fiekydkslh qaiegdtsgd
      661 fmkallalcg ged
//
LOCUS       NP_001029241             284 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.6cy [Rattus norvegicus].
ACCESSION   NP_001029241
VERSION     NP_001029241.1
DBSOURCE    REFSEQ: accession NM_001034069.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU670983.1, M60666.1 and
            BC078780.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.6, also known as variant 2)
            contains a different 3' exon compared to variant 1. The resulting
            protein (isoform Tpm1.6cy, also referred to as TM-2) is shorter and
            has a distinct C-terminus compared to isoform a. Isoform Tpm1.6cy
            is the same length as isoforms Tpm1.7cy and Tpm1.3sm but is the
            product of alternate splicing and contains short regions of
            sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M60666.1, EV764384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.6cy"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32578
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034069.1:107..961"
                     /note="isoform Tpm1.6cy is encoded by transcript variant
                     Tpm1.6"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddleekv ahakeenlsm hqmldqtlle lnnm
//
LOCUS       NP_001011926             292 aa            linear   ROD 27-APR-2025
DEFINITION  AKT-interacting protein [Rattus norvegicus].
ACCESSION   NP_001011926 XP_214647
VERSION     NP_001011926.1
DBSOURCE    REFSEQ: accession NM_001011926.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Xu,L., Sowa,M.E., Chen,J., Li,X., Gygi,S.P. and Harper,J.W.
  TITLE     An FTS/Hook/p107(FHIP) complex interacts with and promotes
            endosomal clustering by the homotypic vacuolar protein sorting
            complex
  JOURNAL   Mol Biol Cell 19 (12), 5059-5071 (2008)
   PUBMED   18799622
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Remy,I. and Michnick,S.W.
  TITLE     Regulation of apoptosis by the Ft1 protein, a new modulator of
            protein kinase B/Akt
  JOURNAL   Mol Cell Biol 24 (4), 1493-1504 (2004)
   PUBMED   14749367
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089985.1.
            
            On Feb 11, 2005 this sequence version replaced XP_214647.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089985.1, FQ213781.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p11"
     Protein         1..292
                     /product="AKT-interacting protein"
                     /note="fused toes protein homolog"
                     /calculated_mol_wt=32861
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH4.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H8T0; propagated from
                     UniProtKB/Swiss-Prot (Q5FVH4.1)"
     Region          77..189
                     /region_name="UEV_AKTIP"
                     /note="ubiquitin E2 variant (UEV) domain of
                     AKT-interacting protein and related proteins; cd23814"
                     /db_xref="CDD:467434"
     CDS             1..292
                     /gene="Aktip"
                     /gene_synonym="Fts"
                     /coded_by="NM_001011926.1:160..1038"
                     /db_xref="GeneID:291906"
                     /db_xref="RGD:1311170"
ORIGIN      
        1 mnplwsmssg svrkraegee ktlagdvkts pprsapkkql psipknalpi skptspapaa
       61 qstngthasy gpfyleysll aeftmvvkqk lpgvyvqpsy rsalvwfgvi firhglyqdg
      121 vfkftvyipd nypdgdcprl lfdipvfhpl vdptsgeldv krafakwrrn hnhiwqvlmy
      181 arrvfykidt tsplnpeaav lyekdiqlfk skvvdsvkvc tarlfdqpki edpyaisfsp
      241 wnpsvhdear ekmltqkkpd eqhnksvhva glswvkpgsv qpfskeektv at
//
LOCUS       NP_001128162              37 aa            linear   ROD 27-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit 4 [Rattus norvegicus].
ACCESSION   NP_001128162
VERSION     NP_001128162.1
DBSOURCE    REFSEQ: accession NM_001134690.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 37)
  AUTHORS   Dumax-Vorzet,A., Roboti,P. and High,S.
  TITLE     OST4 is a subunit of the mammalian oligosaccharyltransferase
            required for efficient N-glycosylation
  JOURNAL   J Cell Sci 126 (Pt 12), 2595-2606 (2013)
   PUBMED   23606741
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ194673.1, BC157814.1 and BI277067.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ142883.1, BC157814.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..37
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..37
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 4"
                     /note="oligosaccharyltransferase 4 homolog"
                     /calculated_mol_wt=4062
     Region          1..34
                     /region_name="Ost4"
                     /note="Oligosaccaryltransferase; pfam10215"
                     /db_xref="CDD:431142"
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BLS0.1)"
     CDS             1..37
                     /gene="Ost4"
                     /coded_by="NM_001134690.1:171..284"
                     /db_xref="GeneID:100188932"
                     /db_xref="RGD:2300150"
ORIGIN      
        1 mitdvqlaif anmlgvslfl lvvlyhyvav nnpkkqe
//
LOCUS       NP_878262                476 aa            linear   ROD 27-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type 1G isoform 1
            [Rattus norvegicus].
ACCESSION   NP_878262 XP_341178
VERSION     NP_878262.1
DBSOURCE    REFSEQ: accession NM_182842.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Davare,M.A., Fortin,D.A., Saneyoshi,T., Nygaard,S., Kaech,S.,
            Banker,G., Soderling,T.R. and Wayman,G.A.
  TITLE     Transient receptor potential canonical 5 channels activate
            Ca2+/calmodulin kinase Igamma to promote axon formation in
            hippocampal neurons
  JOURNAL   J Neurosci 29 (31), 9794-9808 (2009)
   PUBMED   19657032
  REMARK    GeneRIF: These results are consistent with a model in which highly
            localized calcium influx through the TRPC5 channels activates CaMKK
            and CaMKI, which subsequently promote axon formation.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Nishimura,H., Sakagami,H., Uezu,A., Fukunaga,K., Watanabe,M. and
            Kondo,H.
  TITLE     Cloning, characterization and expression of two alternatively
            splicing isoforms of Ca2+/calmodulin-dependent protein kinase I
            gamma in the rat brain
  JOURNAL   J Neurochem 85 (5), 1216-1227 (2003)
   PUBMED   12753081
  REMARK    GeneRIF: findings suggest that both alternatively splicing isoforms
            of CaMKI gamma may be involved in Ca2+ signal transduction in the
            cytoplasmic compartment of certain neuronal population
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Takemoto-Kimura,S., Terai,H., Takamoto,M., Ohmae,S., Kikumura,S.,
            Segi,E., Arakawa,Y., Furuyashiki,T., Narumiya,S. and Bito,H.
  TITLE     Molecular cloning and characterization of CLICK-III/CaMKIgamma, a
            novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein
            kinase (CaMK)
  JOURNAL   J Biol Chem 278 (20), 18597-18605 (2003)
   PUBMED   12637513
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Yokokura,H., Terada,O., Naito,Y. and Hidaka,H.
  TITLE     Isolation and comparison of rat cDNAs encoding
            Ca2+/calmodulin-dependent protein kinase I isoforms
  JOURNAL   Biochim Biophys Acta 1338 (1), 8-12 (1997)
   PUBMED   9074610
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB101231.1.
            
            On Dec 17, 2003 this sequence version replaced XP_341178.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            25 bp suspected to be vector contamination from the 3' end.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB101231.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132268 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..476
                     /product="calcium/calmodulin-dependent protein kinase type
                     1G isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase type
                     1G; caMKIG; CLICK III; caM-KI gamma; caM kinase IG; caMKI
                     gamma; caM kinase I gamma; caMK-like CREB kinase III;
                     calcium/calmodulin-dependent protein kinase I gamma"
                     /calculated_mol_wt=53048
     Region          19..303
                     /region_name="STKc_CaMKI_gamma"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type I gamma;
                     cd14166"
                     /db_xref="CDD:271068"
     Site            order(29..33,37,50,52,81,97..100,104,106,142..143,145,
                     147..148,150,163..164,167,180..184,186)
                     /site_type="active"
                     /db_xref="CDD:271068"
     Site            order(29..32,37,50,52,81,97..100,104,147..148,150,
                     163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271068"
     Site            order(33,104,106,142..143,145,147,167,180..184,186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271068"
     Site            163..184
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271068"
     Region          277..317
                     /region_name="Autoinhibitory domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ7.1)"
     Region          297..318
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ7.1)"
     Region          326..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNJ7.1)"
     CDS             1..476
                     /gene="Camk1g"
                     /coded_by="NM_182842.1:81..1511"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171358"
                     /db_xref="RGD:621800"
ORIGIN      
        1 mgrkeeedcs swkkqttnir ktfifmevlg sgafsevflv kqrvtgklfa lkcikkspaf
       61 rdssleneia vlkrikheni vtlediyest thyylvmqlv sggelfdril ergvytekda
      121 slviqqvlsa vkylhengiv hrdlkpenll yltpeenski mitdfglskm eqngvmstac
      181 gtpgyvapev laqkpyskav dcwsigvity illcgyppfy eetesklfek ikegyyefes
      241 pfwddisesa kdfichllek dpnerytcek alrhpwidgn talhrdiyps vslqiqknfa
      301 kskwrqafna aavvhhmrkl hmnlhspsvr qevenrppvs papevsrpgs hdssiteapi
      361 ldpstplpal trlpcshssr psapggrsln clvngslris sslvpmqqgp latgpcgccs
      421 sclnignkgk ssycseptlf rkankkqnfk sevmvpvkag gsthcragqt gvclim
//
LOCUS       NP_001020200             147 aa            linear   ROD 27-APR-2025
DEFINITION  TRAF-interacting protein with FHA domain-containing protein B
            [Rattus norvegicus].
ACCESSION   NP_001020200 XP_344569
VERSION     NP_001020200.1
DBSOURCE    REFSEQ: accession NM_001025029.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schroder,J.C., Lassig,A.K., Galetzka,D., Peters,A., Castle,J.C.,
            Diederich,S., Zechner,U., Muller-Forell,W., Keilmann,A. and
            Bartsch,O.
  TITLE     A boy with homozygous microdeletion of NEUROG1 presents with a
            congenital cranial dysinnervation disorder [Moebius syndrome
            variant]
  JOURNAL   Behav Brain Funct 9, 7 (2013)
   PUBMED   23419067
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091188.1.
            
            On Jun 25, 2005 this sequence version replaced XP_344569.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091188.1, CO567269.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..147
                     /product="TRAF-interacting protein with FHA
                     domain-containing protein B"
                     /note="TIFA-like protein; TIFA inhibitor B;
                     TRAF-interacting protein with forkhead-associated domain,
                     family member B"
                     /calculated_mol_wt=16535
     Region          5..133
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(39..40,54..55,57,82..83)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     CDS             1..147
                     /gene="Tifab"
                     /gene_synonym="RGD1311681"
                     /coded_by="NM_001025029.1:292..735"
                     /db_xref="GeneID:364674"
                     /db_xref="RGD:1311681"
ORIGIN      
        1 merpltvlqv slyhptqgpv afakvplqlq hdasrllvgr gqdthlqlql pqlsrhhlcl
       61 epylekgsnl lafclkvltr qscvwvnglp lryleqvplh svnrisfsgi qmlirkegga
      121 sleafvcyfh lspspliyrp kaqetde
//
LOCUS       NP_001005765             184 aa            linear   ROD 27-APR-2025
DEFINITION  ras-related protein Rap-1A [Rattus norvegicus].
ACCESSION   NP_001005765 XP_215669
VERSION     NP_001005765.1
DBSOURCE    REFSEQ: accession NM_001005765.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Keyes,J., Ganesan,A., Molinar-Inglis,O., Hamidzadeh,A., Zhang,J.,
            Ling,M., Trejo,J., Levchenko,A. and Zhang,J.
  TITLE     Signaling diversity enabled by Rap1-regulated plasma membrane ERK
            with distinct temporal dynamics
  JOURNAL   Elife 9, e57410 (2020)
   PUBMED   32452765
  REMARK    GeneRIF: Signaling diversity enabled by Rap1-regulated plasma
            membrane ERK with distinct temporal dynamics.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Moon,M.Y., Kim,H.J., Kim,M.J., Uhm,S., Park,J.W., Suk,K.T.,
            Park,J.B., Kim,D.J. and Kim,S.E.
  TITLE     Rap1 regulates hepatic stellate cell migration through the
            modulation of RhoA activity in response to TGF-beta1
  JOURNAL   Int J Mol Med 44 (2), 491-502 (2019)
   PUBMED   31173168
  REMARK    GeneRIF: These findings suggest that TGFbeta1 regulates Rap1,
            resulting in the suppression of RhoA, activation of and formation
            of Factin during the migration of hepatic stellate cells.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Fang,B., Wei,L., Dong,K., Niu,X., Sui,X. and Zhang,H.
  TITLE     miR-202 modulates the progression of neuropathic pain through
            targeting RAP1A
  JOURNAL   J Cell Biochem 120 (3), 2973-2982 (2019)
   PUBMED   30520098
  REMARK    GeneRIF: that RAP1A was a direct target gene of miR-202 in the PC12
            cell. RAP1A expression was upregulated in the spinal dorsal horn of
            bilateral sciatic nerve chronic constriction injury (bCCI)rat.
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Yang,Y., Yang,F., Wu,X., Lv,X. and Li,J.
  TITLE     EPAC activation inhibits acetaldehyde-induced activation and
            proliferation of hepatic stellate cell via Rap1
  JOURNAL   Can J Physiol Pharmacol 94 (5), 498-507 (2016)
   PUBMED   26854595
  REMARK    GeneRIF: Data suggest activation of EPAC1/2 (exchange proteins
            activated by cAMP) and Rap1 (RAS-related GTP-binding protein 1) in
            hepatic stellate cells down-regulates proliferation and synthesis
            of a-smooth muscle actin/collagen I/collagen II in an in vitro
            model of alcoholic cirrhosis (AC); in AC, expression of EPAC1 is
            down-regulated but expression of EPAC2 is up-regulated; EPAC1
            activation increases GTP-bound (activated) Rap1.
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Walkup,W.G. 4th, Washburn,L., Sweredoski,M.J., Carlisle,H.J.,
            Graham,R.L., Hess,S. and Kennedy,M.B.
  TITLE     Phosphorylation of synaptic GTPase-activating protein (synGAP) by
            Ca2+/calmodulin-dependent protein kinase II (CaMKII) and
            cyclin-dependent kinase 5 (CDK5) alters the ratio of its GAP
            activity toward Ras and Rap GTPases
  JOURNAL   J Biol Chem 290 (8), 4908-4927 (2015)
   PUBMED   25533468
  REMARK    GeneRIF: Phosphorylation of synaptic GTPase-activating protein
            (synGAP) by Ca2+/calmodulin-dependent protein kinase II (CaMKII)
            and cyclin-dependent kinase 5 (CDK5) alters the ratio of its GAP
            activity toward Ras and Rap GTPases.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Berruti,G.
  TITLE     A novel rap1/B-Raf/14-3-3 theta protein complex is formed in vivo
            during the morphogenetic differentiation of postmeiotic male germ
            cells
  JOURNAL   Exp Cell Res 257 (1), 172-179 (2000)
   PUBMED   10854065
REFERENCE   7  (residues 1 to 184)
  AUTHORS   York,R.D., Yao,H., Dillon,T., Ellig,C.L., Eckert,S.P.,
            McCleskey,E.W. and Stork,P.J.
  TITLE     Rap1 mediates sustained MAP kinase activation induced by nerve
            growth factor
  JOURNAL   Nature 392 (6676), 622-626 (1998)
   PUBMED   9560161
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Urayama,O., Murakoshi,T., Kubota,M., Hara,Y., Chihara,J. and
            Ikawa,Y.
  TITLE     Coincident induction of K rev-1/rap 1A, rap 1B and H-ras mRNAs in
            the rat spinal cord by noxious stimulation
  JOURNAL   Brain Res Mol Brain Res 45 (2), 331-334 (1997)
   PUBMED   9149109
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Cruise,J.L., Rafferty,M.P. and Riehle,M.M.
  TITLE     Cell-cycle regulated expression of Rap1 in regenerating liver
  JOURNAL   Biochem Biophys Res Commun 230 (3), 578-581 (1997)
   PUBMED   9015365
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Kitayama,H., Sugimoto,Y., Matsuzaki,T., Ikawa,Y. and Noda,M.
  TITLE     A ras-related gene with transformation suppressor activity
  JOURNAL   Cell 56 (1), 77-84 (1989)
   PUBMED   2642744
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083813.1.
            
            On Oct 15, 2004 this sequence version replaced XP_215669.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083813.1, FQ233812.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..184
                     /product="ras-related protein Rap-1A"
                     /EC_number="3.6.5.2"
                     /note="ras-related protein Krev-1; RAS-related protein 1a"
                     /calculated_mol_wt=20856
     mat_peptide     1..181
                     /product="Ras-related protein Rap-1A. /id=PRO_0000030203"
                     /note="propagated from UniProtKB/Swiss-Prot (P62836.1)"
                     /calculated_mol_wt=20648
     Region          3..167
                     /region_name="Rap1"
                     /note="Rap1 family GTPase consists of Rap1a and Rap1b
                     isoforms; cd04175"
                     /db_xref="CDD:133375"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133375"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133375"
     Site            order(12..18,28..30,32,34..35,60,116..117,119,147..149)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133375"
     Site            order(17..18,32,34,40..41,54..55,57,59..60,149)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133375"
     Site            order(25,31,33,36..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133375"
     Region          32..40
                     /region_name="Effector region. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P62836.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133375"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133375"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133375"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133375"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133375"
     Site            147..149
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133375"
     Site            181
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P62834; propagated from
                     UniProtKB/Swiss-Prot (P62836.1)"
     CDS             1..184
                     /gene="Rap1a"
                     /gene_synonym="rap 1A; RAP-1A"
                     /coded_by="NM_001005765.1:117..671"
                     /db_xref="GeneID:295347"
                     /db_xref="RGD:1359694"
ORIGIN      
        1 mreyklvvlg sggvgksalt vqfvqgifve kydptiedsy rkqvevdcqq cmleildtag
       61 teqftamrdl ymkngqgfal vysitaqstf ndlqdlreqi lrvkdtedvp milvgnkcdl
      121 edervvgkeq gqnlarqwcn caflessaks kinvneifyd lvrqinrktp vekkkpkkks
      181 clll
//
LOCUS       NP_446316                806 aa            linear   ROD 27-APR-2025
DEFINITION  transitional endoplasmic reticulum ATPase [Rattus norvegicus].
ACCESSION   NP_446316
VERSION     NP_446316.1
DBSOURCE    REFSEQ: accession NM_053864.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Kartal,B., Alimogullari,E. and Cayli,S.
  TITLE     The immunoexpression of valosin-containing protein and small
            VCP-interacting protein in rat ovaries
  JOURNAL   Anat Histol Embryol 52 (4), 546-551 (2023)
   PUBMED   36843060
  REMARK    GeneRIF: The immunoexpression of valosin-containing protein and
            small VCP-interacting protein in rat ovaries.
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Turakhiya,A., Meyer,S.R., Marincola,G., Bohm,S., Vanselow,J.T.,
            Schlosser,A., Hofmann,K. and Buchberger,A.
  TITLE     ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance
            of Arsenite-Induced Stress Granules
  JOURNAL   Mol Cell 70 (5), 906-919 (2018)
   PUBMED   29804830
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Zhou,N., Ma,B., Stoll,S., Hays,T.T. and Qiu,H.
  TITLE     The valosin-containing protein is a novel repressor of
            cardiomyocyte hypertrophy induced by pressure overload
  JOURNAL   Aging Cell 16 (5), 1168-1179 (2017)
   PUBMED   28799247
  REMARK    GeneRIF: Valosin-containing protein is a novel repressor of
            cardiomyocyte hypertrophy induced by pressure overload.
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Flack,J.E., Mieszczanek,J., Novcic,N. and Bienz,M.
  TITLE     Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the
            HECT E3 Ubiquitin Ligase Hyd/UBR5
  JOURNAL   Mol Cell 67 (2), 181-193 (2017)
   PUBMED   28689657
REFERENCE   5  (residues 1 to 806)
  AUTHORS   Papadopoulos,C., Kirchner,P., Bug,M., Grum,D., Koerver,L.,
            Schulze,N., Poehler,R., Dressler,A., Fengler,S., Arhzaouy,K.,
            Lux,V., Ehrmann,M., Weihl,C.C. and Meyer,H.
  TITLE     VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of
            ruptured lysosomes by autophagy
  JOURNAL   EMBO J 36 (2), 135-150 (2017)
   PUBMED   27753622
REFERENCE   6  (residues 1 to 806)
  AUTHORS   Zhang,S.H., Liu,J., Kobayashi,R. and Tonks,N.K.
  TITLE     Identification of the cell cycle regulator VCP (p97/CDC48) as a
            substrate of the band 4.1-related protein-tyrosine phosphatase
            PTPH1
  JOURNAL   J Biol Chem 274 (25), 17806-17812 (1999)
   PUBMED   10364224
REFERENCE   7  (residues 1 to 806)
  AUTHORS   Rabouille,C., Kondo,H., Newman,R., Hui,N., Freemont,P. and
            Warren,G.
  TITLE     Syntaxin 5 is a common component of the NSF- and p97-mediated
            reassembly pathways of Golgi cisternae from mitotic Golgi fragments
            in vitro
  JOURNAL   Cell 92 (5), 603-610 (1998)
   PUBMED   9506515
REFERENCE   8  (residues 1 to 806)
  AUTHORS   Dai,R.M., Chen,E., Longo,D.L., Gorbea,C.M. and Li,C.C.
  TITLE     Involvement of valosin-containing protein, an ATPase Co-purified
            with IkappaBalpha and 26 S proteasome, in
            ubiquitin-proteasome-mediated degradation of IkappaBalpha
  JOURNAL   J Biol Chem 273 (6), 3562-3573 (1998)
   PUBMED   9452483
REFERENCE   9  (residues 1 to 806)
  AUTHORS   Kondo,H., Rabouille,C., Newman,R., Levine,T.P., Pappin,D.,
            Freemont,P. and Warren,G.
  TITLE     p47 is a cofactor for p97-mediated membrane fusion
  JOURNAL   Nature 388 (6637), 75-78 (1997)
   PUBMED   9214505
REFERENCE   10 (residues 1 to 806)
  AUTHORS   Zhang,L., Ashendel,C.L., Becker,G.W. and Morre,D.J.
  TITLE     Isolation and characterization of the principal ATPase associated
            with transitional endoplasmic reticulum of rat liver
  JOURNAL   J Cell Biol 127 (6 Pt 2), 1871-1883 (1994)
   PUBMED   7806566
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC060518.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060518.1, U11760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q22"
     Protein         1..806
                     /product="transitional endoplasmic reticulum ATPase"
                     /EC_number="3.6.4.6"
                     /note="TER ATPase; 15S Mg(2+)-ATPase p97 subunit"
                     /calculated_mol_wt=89218
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Region          25..764
                     /region_name="CDC48"
                     /note="AAA family ATPase, CDC48 subfamily; TIGR01243"
                     /db_xref="CDD:273521"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            315
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by VCPKMT.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            502
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01853; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            505
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01853; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            668
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01853; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Region          708..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46462.3)"
     Site            754
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01853; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Region          768..806
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46462.3)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55072; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     Region          797..806
                     /region_name="Interaction with UBXN6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46462.3)"
     Region          802..806
                     /region_name="PIM motif.
                     /evidence=ECO:0000250|UniProtKB:P55072"
                     /note="propagated from UniProtKB/Swiss-Prot (P46462.3)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01853; propagated from
                     UniProtKB/Swiss-Prot (P46462.3)"
     CDS             1..806
                     /gene="Vcp"
                     /coded_by="NM_053864.2:212..2632"
                     /db_xref="GeneID:116643"
                     /db_xref="RGD:621595"
ORIGIN      
        1 masgadskgd dlstailkqk nrpnrlivde ainednsvvs lsqpkmdelq lfrgdtvllk
       61 gkkrreavci vlsddtcsde kirmnrvvrn nlrvrlgdvi siqpcpdvky gkrihvlpid
      121 dtvegitgnl fevylkpyfl eayrpirkgd iflvrggmra vefkvvetdp spycivapdt
      181 vihcegepik redeeeslne vgyddiggcr kqlaqikemv elplrhpalf kaigvkpprg
      241 illygppgtg ktliaravan etgaffflin gpeimsklag esesnlrkaf eeaeknapai
      301 ifideldaia pkrekthgev errivsqllt lmdglkqrah vivmaatnrp nsidpalrrf
      361 grfdrevdig ipdatgrlei lqihtknmkl addvdleqva nethghvgad laalcseaal
      421 qairkkmdli dledetidae vmnslavtmd dfrwalsqsn psalretvve vpqvtwedig
      481 gledvkrelq elvqypvehp dkflkfgmtp skgvlfygpp gcgktllaka ianecqanfi
      541 sikgpelltm wfgeseanvr eifdkarqaa pcvlffdeld siakarggni gdgggaadrv
      601 inqiltemdg mstkknvfii gatnrpdiid pailrpgrld qliyiplpde ksrvailkan
      661 lrkspvakdv dleflakmtn gfsgadltei cqracklair esieseirre rerqtnpsam
      721 eveeddpvpe irrdhfeeam rfarrsvsdn dirkyemfaq tlqqsrgfgs frfpsgnqgg
      781 agpsqgsggg tggnvytedn dddlyg
//
LOCUS       NP_074051                533 aa            linear   ROD 27-APR-2025
DEFINITION  beta-1,4 N-acetylgalactosaminyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_074051
VERSION     NP_074051.1
DBSOURCE    REFSEQ: accession NM_022860.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Rabionet,M., van der Spoel,A.C., Chuang,C.C., von
            Tumpling-Radosta,B., Litjens,M., Bouwmeester,D., Hellbusch,C.C.,
            Korner,C., Wiegandt,H., Gorgas,K., Platt,F.M., Grone,H.J. and
            Sandhoff,R.
  TITLE     Male germ cells require polyenoic sphingolipids with complex
            glycosylation for completion of meiosis: a link to ceramide
            synthase-3
  JOURNAL   J Biol Chem 283 (19), 13357-13369 (2008)
   PUBMED   18308723
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Liu,Y., Wada,R., Kawai,H., Sango,K., Deng,C., Tai,T.,
            McDonald,M.P., Araujo,K., Crawley,J.N., Bierfreund,U., Sandhoff,K.,
            Suzuki,K. and Proia,R.L.
  TITLE     A genetic model of substrate deprivation therapy for a
            glycosphingolipid storage disorder
  JOURNAL   J Clin Invest 103 (4), 497-505 (1999)
   PUBMED   10021458
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Takamiya,K., Yamamoto,A., Furukawa,K., Yamashiro,S., Shin,M.,
            Okada,M., Fukumoto,S., Haraguchi,M., Takeda,N., Fujimura,K.,
            Sakae,M., Kishikawa,M., Shiku,H., Furukawa,K. and Aizawa,S.
  TITLE     Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides
            but exhibit only subtle defects in their nervous system
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10662-10667 (1996)
   PUBMED   8855236
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Ruan,S., Raj,B.K., Furukawa,K. and Lloyd,K.O.
  TITLE     Analysis of melanoma cells stably transfected with beta 1,4GalNAc
            transferase (GM2/GD2 synthase) cDNA: relative glycosyltransferase
            levels play a dominant role in determining ganglioside expression
  JOURNAL   Arch Biochem Biophys 323 (1), 11-18 (1995)
   PUBMED   7487055
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Yamashiro,S., Haraguchi,M., Furukawa,K., Takamiya,K., Yamamoto,A.,
            Nagata,Y., Lloyd,K.O., Shiku,H. and Furukawa,K.
  TITLE     Substrate specificity of beta 1,4-N-acetylgalactosaminyltransferase
            in vitro and in cDNA-transfected cells. GM2/GD2 synthase
            efficiently generates asialo-GM2 in certain cells
  JOURNAL   J Biol Chem 270 (11), 6149-6155 (1995)
   PUBMED   7890749
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Hidari,J.K., Ichikawa,S., Furukawa,K., Yamasaki,M. and
            Hirabayashi,Y.
  TITLE     beta 1-4N-acetylgalactosaminyltransferase can synthesize both
            asialoglycosphingolipid GM2 and glycosphingolipid GM2 in vitro and
            in vivo: isolation and characterization of a beta
            1-4N-acetylgalactosaminyltransferase cDNA clone from rat ascites
            hepatoma cell line AH7974F
  JOURNAL   Biochem J 303 (Pt 3) (Pt 3), 957-965 (1994)
   PUBMED   7980468
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Nagata,Y., Yamashiro,S., Yodoi,J., Lloyd,K.O., Shiku,H. and
            Furukawa,K.
  TITLE     Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase
            cDNAs that determine the expression of GM2 and GD2 gangliosides
  JOURNAL   J Biol Chem 267 (17), 12082-12089 (1992)
   PUBMED   1601877
  REMARK    Erratum:[J Biol Chem. 1994 Mar 4;269(9):7045. PMID: 8120069]
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Iber,H., Zacharias,C. and Sandhoff,K.
  TITLE     The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver
            Golgi by the same set of glycosyltransferases that catalyse the
            biosynthesis of asialo-, a- and b-series gangliosides
  JOURNAL   Glycobiology 2 (2), 137-142 (1992)
   PUBMED   1606358
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Pohlentz,G., Klein,D., Schwarzmann,G., Schmitz,D. and Sandhoff,K.
  TITLE     Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases
            are single enzymes in Golgi vesicles from rat liver
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7044-7048 (1988)
   PUBMED   3140234
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081799.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081799.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..533
                     /product="beta-1,4 N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.92"
                     /note="GM2/GD2 synthase;
                     (N-acetylneuraminyl)-galactosylglucosylceramide;
                     beta-4N-acetylgalactosaminyltransferase;
                     UDP-N-acetyl-alpha-D-galactosamine:(N-acetylneuraminyl)-
                     galactosylglucosylceramide-beta-1,
                     4-N-acetylgalactosaminyltransferase; GA2 synthase; GM2
                     synthase"
                     /calculated_mol_wt=59148
     Site            8..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10468.1)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q10468.1)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q10468.1)"
     Region          280..426
                     /region_name="Glycos_transf_2"
                     /note="Glycosyl transferase family 2; pfam00535"
                     /db_xref="CDD:425738"
     CDS             1..533
                     /gene="B4galnt1"
                     /gene_synonym="Galgt1; GalNAc-T"
                     /coded_by="NM_022860.2:142..1743"
                     /db_xref="GeneID:64828"
                     /db_xref="RGD:620490"
ORIGIN      
        1 mrldrralya lvlllacasl gllyastrda pglpnplalw sppqgpprld lldlatepry
       61 ahipvrikeq vvgllaqnnc scessggrfa lpflrqvrai dftkafdaee lravsisreq
      121 eyqaflarsr sladqlliap ansplqyplq gvevqplrsi lvpglslqea svqeiyqvnl
      181 iaslgtwdva gevtgvtltg egqsdltlas pildklnrql qlvtyssrsy qantadtvrf
      241 stkghevaft ilirhppnpr lyppsslpqg aqynisalvt vatktflryd rlraliasir
      301 rfyptvtivi addsdkperi sdphvehyfm pfgkgwfagr nlavsqvttk yvlwvdddfv
      361 ftartrlekl vdvlertpld lvggavreis gyattyrqll svepgapgfg nclrqkqgfh
      421 helagfpncv vtdgvvnffl artdkvrqvg fdprlnrvah leffldglgs lrvgscsdvv
      481 vdhaskvklp wtskdpgael yaryrypgsl dqsqvakhrl lffkhrlqcm tae
//
LOCUS       NP_001102738             562 aa            linear   ROD 27-APR-2025
DEFINITION  glucocorticoid modulatory element-binding protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001102738 XP_001064903 XP_575922
VERSION     NP_001102738.1
DBSOURCE    REFSEQ: accession NM_001109268.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Jimenez-Lara,A.M., Heine,M.J. and Gronemeyer,H.
  TITLE     Cloning of a mouse glucocorticoid modulatory element binding
            protein, a new member of the KDWK family
  JOURNAL   FEBS Lett 468 (2-3), 203-210 (2000)
   PUBMED   10692587
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Oshima,H., Szapary,D. and Simons,S.S. Jr.
  TITLE     The factor binding to the glucocorticoid modulatory element of the
            tyrosine aminotransferase gene is a novel and ubiquitous
            heteromeric complex
  JOURNAL   J Biol Chem 270 (37), 21893-21901 (1995)
   PUBMED   7665613
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158640.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064903.1, XP_575922.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158640.1, SRR8487226.64242.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..562
                     /product="glucocorticoid modulatory element-binding
                     protein 1"
                     /note="GMEB-1"
                     /calculated_mol_wt=61063
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y692; propagated from
                     UniProtKB/Swiss-Prot (Q9QUZ8.3)"
     Region          80..155
                     /region_name="SAND"
                     /note="SAND domain; pfam01342"
                     /db_xref="CDD:460167"
     Region          360..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QUZ8.3)"
     CDS             1..562
                     /gene="Gmeb1"
                     /gene_synonym="RGD1563208"
                     /coded_by="NM_001109268.2:74..1762"
                     /db_xref="GeneID:500558"
                     /db_xref="RGD:1563208"
ORIGIN      
        1 manaevsvpv gdvvvvpteg negenpedtk tqvilqlqpv qqgiyeagse nsaavvavet
       61 htihkieegi dassieaned meiaypitcg eskavllwkk fvcpginvkc vkfndqlisp
      121 khfvhlagks tlkdwkrair lggimlrkmm dsgqidfyqh dkvcsntcrs tkfdllissa
      181 rapvpgqqts vvqtptsadg nitqiaisee smeeaglewn saltaavtma teegikkese
      241 eisedtlmfw kgiadvglme evvcniqkei eellrgvqqr lihapfqvtd aavlnnvant
      301 fglmdtvkrv ldnrrkqveh geeqflytla dlerqleeqk kqaqdprlks qtvqnvvlmp
      361 vstpkppkrp rlqrpasttv lspspvqqpq ftvispitit pvgqsfsmgn ipvatlsqgt
      421 spvtvhtlps gpqlfryatv vssaksnspd tvtihpsssl allsstsmqd gstlgnmatm
      481 vspvelvame sgltsaiqav estsedgqti ieidpapdpe addpegkavi letelrteek
      541 vvanmeerqh qvhnveivvl ed
//
LOCUS       NP_037039                229 aa            linear   ROD 27-APR-2025
DEFINITION  C->U-editing enzyme APOBEC-1 [Rattus norvegicus].
ACCESSION   NP_037039
VERSION     NP_037039.1
DBSOURCE    REFSEQ: accession NM_012907.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Li,X., Wang,Y., Liu,Y., Yang,B., Wang,X., Wei,J., Lu,Z., Zhang,Y.,
            Wu,J., Huang,X., Yang,L. and Chen,J.
  TITLE     Base editing with a Cpf1-cytidine deaminase fusion
  JOURNAL   Nat Biotechnol 36 (4), 324-327 (2018)
   PUBMED   29553573
  REMARK    GeneRIF: To overcome this limitation, we developed a
            CRISPR-Cpf1-based BE by fusing the rat cytosine deaminase APOBEC1
            to a catalytically inactive version of Lachnospiraceae bacterium
            Cpf1.
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Fossat,N., Tourle,K., Radziewic,T., Barratt,K., Liebhold,D.,
            Studdert,J.B., Power,M., Jones,V., Loebel,D.A. and Tam,P.P.
  TITLE     C to U RNA editing mediated by APOBEC1 requires RNA-binding protein
            RBM47
  JOURNAL   EMBO Rep 15 (8), 903-910 (2014)
   PUBMED   24916387
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Saraconi,G., Severi,F., Sala,C., Mattiuz,G. and Conticello,S.G.
  TITLE     The RNA editing enzyme APOBEC1 induces somatic mutations and a
            compatible mutational signature is present in esophageal
            adenocarcinomas
  JOURNAL   Genome Biol 15 (7), 417 (2014)
   PUBMED   25085003
  REMARK    GeneRIF: Results show that expression of APOBEC1 induces a mutator
            phenotype in 2 different cellular models.
            Erratum:[Genome Biol. 2014;15(11):497]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Li,W., Cheng,X., Chen,H.S. and He,Z.Y.
  TITLE     Apobec-1 increases cyclooxygenase-2 and aggravates injury in
            oxygen-deprived neurogenic cells and middle cerebral artery
            occlusion rats
  JOURNAL   Neurochem Res 38 (7), 1434-1445 (2013)
   PUBMED   23609497
  REMARK    GeneRIF: Apobec-1 increased COX-2 expression and COX-2 mRNA
            stabilization in neurogenic cells, and failed to catalyze C-to-U
            editing of COX-2 mRNA
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Sun,H., Samarghandi,A., Zhang,N., Yao,Z., Xiong,M. and Teng,B.B.
  TITLE     Proprotein convertase subtilisin/kexin type 9 interacts with
            apolipoprotein B and prevents its intracellular degradation,
            irrespective of the low-density lipoprotein receptor
  JOURNAL   Arterioscler Thromb Vasc Biol 32 (7), 1585-1595 (2012)
   PUBMED   22580899
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Osuga,J., Yagyu,H., Ohashi,K., Harada,K., Yazaki,Y., Yamada,N. and
            Ishibashi,S.
  TITLE     Effects of apo E deficiency on plasma lipid levels in mice lacking
            APOBEC-1
  JOURNAL   Biochem Biophys Res Commun 236 (2), 375-378 (1997)
   PUBMED   9240444
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Phung,T.L., Sowden,M.P., Sparks,J.D., Sparks,C.E. and Smith,H.C.
  TITLE     Regulation of hepatic apolipoprotein B RNA editing in the
            genetically obese Zucker rat
  JOURNAL   Metabolism 45 (9), 1056-1058 (1996)
   PUBMED   8781289
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Morrison,J.R., Paszty,C., Stevens,M.E., Hughes,S.D., Forte,T.,
            Scott,J. and Rubin,E.M.
  TITLE     Apolipoprotein B RNA editing enzyme-deficient mice are viable
            despite alterations in lipoprotein metabolism
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7154-7159 (1996)
   PUBMED   8692961
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Hirano,K., Young,S.G., Farese,R.V. Jr., Ng,J., Sande,E.,
            Warburton,C., Powell-Braxton,L.M. and Davidson,N.O.
  TITLE     Targeted disruption of the mouse apobec-1 gene abolishes
            apolipoprotein B mRNA editing and eliminates apolipoprotein B48
  JOURNAL   J Biol Chem 271 (17), 9887-9890 (1996)
   PUBMED   8626621
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Teng,B., Burant,C.F. and Davidson,N.O.
  TITLE     Molecular cloning of an apolipoprotein B messenger RNA editing
            protein
  JOURNAL   Science 260 (5115), 1816-1819 (1993)
   PUBMED   8511591
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085335.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085335.1, L07114.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09767679, SAMN09767680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..229
                     /product="C->U-editing enzyme APOBEC-1"
                     /EC_number="3.5.4.36"
                     /note="apolipoprotein B mRNA-editing enzyme 1;
                     apolipoprotein B mRNA editing enzyme, catalytic
                     polypeptide 1; Apolipoprotein B editing protein;
                     apolipoprotein B editing complex 1; mRNA(cytosine(6666))
                     deaminase 1; apo B messenger RNA-editing protein"
                     /calculated_mol_wt=27143
     Region          16..186
                     /region_name="NAD1"
                     /note="Novel AID APOBEC clade 1; pfam18778"
                     /db_xref="CDD:465865"
     CDS             1..229
                     /gene="Apobec1"
                     /gene_synonym="apobec-1; REPR"
                     /coded_by="NM_012907.2:495..1184"
                     /db_xref="GeneID:25383"
                     /db_xref="RGD:2133"
ORIGIN      
        1 mssetgpvav dptlrrriep hefevffdpr elrketclly einwggrhsi wrhtsqntnk
       61 hvevnfiekf tteryfcpnt rcsitwflsw spcgecsrai teflsryphv tlfiyiarly
      121 hhadprnrqg lrdlissgvt iqimteqesg ycwrnfvnys psneahwpry phlwvrlyvl
      181 elyciilglp pclnilrrkq pqltfftial qschyqrlpp hilwatglk
//
LOCUS       NP_077372               2434 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family A member 2 [Rattus norvegicus].
ACCESSION   NP_077372
VERSION     NP_077372.1
DBSOURCE    REFSEQ: accession NM_024396.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-Binding Cassette Transporter-2 (ABCA2) Overexpression
            Modulates Sphingosine Levels and Transcription of the Amyloid
            Precursor Protein (APP) Gene
  JOURNAL   Curr Alzheimer Res 12 (9), 847-859 (2015)
   PUBMED   26510981
REFERENCE   2  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-binding cassette transporter-2 (ABCA2) regulates
            esterification of plasma membrane cholesterol by modulation of
            sphingolipid metabolism
  JOURNAL   Biochim Biophys Acta 1841 (1), 168-179 (2014)
   PUBMED   24201375
  REMARK    GeneRIF: control of ABCA2 expression level may be a key locus of
            regulation for esterification of plasma membrane-derived
            cholesterol through modulation of sphingolipid metabolism.
REFERENCE   3  (residues 1 to 2434)
  AUTHORS   Michaki,V., Guix,F.X., Vennekens,K., Munck,S., Dingwall,C.,
            Davis,J.B., Townsend,D.M., Tew,K.D., Feiguin,F., De Strooper,B.,
            Dotti,C.G. and Wahle,T.
  TITLE     Down-regulation of the ATP-binding cassette transporter 2 (Abca2)
            reduces amyloid-beta production by altering Nicastrin maturation
            and intracellular localization
  JOURNAL   J Biol Chem 287 (2), 1100-1111 (2012)
   PUBMED   22086926
  REMARK    GeneRIF: Down-regulation of the ATP-binding cassette transporter 2
            (Abca2) reduces amyloid-beta production by altering Nicastrin
            maturation and intracellular localization.
REFERENCE   4  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-binding cassette transporter-2 (ABCA2) regulates
            cholesterol homeostasis and low-density lipoprotein receptor
            metabolism in N2a neuroblastoma cells
  JOURNAL   Biochim Biophys Acta 1811 (12), 1152-1164 (2011)
   PUBMED   21810484
REFERENCE   5  (residues 1 to 2434)
  AUTHORS   Davis,W. Jr.
  TITLE     The ATP-binding cassette transporter-2 (ABCA2) increases endogenous
            amyloid precursor protein expression and Abeta fragment generation
  JOURNAL   Curr Alzheimer Res 7 (7), 566-577 (2010)
   PUBMED   20704561
REFERENCE   6  (residues 1 to 2434)
  AUTHORS   Zhou,C.J., Inagaki,N., Pleasure,S.J., Zhao,L.X., Kikuyama,S. and
            Shioda,S.
  TITLE     ATP-binding cassette transporter ABCA2 (ABC2) expression in the
            developing spinal cord and PNS during myelination
  JOURNAL   J Comp Neurol 451 (4), 334-345 (2002)
   PUBMED   12210128
  REMARK    GeneRIF: ATP-binding cassette transporter ABCA2 (ABC2) expression
            in the developing spinal cord and PNS during myelination.
REFERENCE   7  (residues 1 to 2434)
  AUTHORS   Vulevic,B., Chen,Z., Boyd,J.T., Davis,W. Jr., Walsh,E.S.,
            Belinsky,M.G. and Tew,K.D.
  TITLE     Cloning and characterization of human adenosine
            5'-triphosphate-binding cassette, sub-family A, transporter 2
            (ABCA2)
  JOURNAL   Cancer Res 61 (8), 3339-3347 (2001)
   PUBMED   11309290
REFERENCE   8  (residues 1 to 2434)
  AUTHORS   Kaminski,W.E., Piehler,A., Pullmann,K., Porsch-Ozcurumez,M.,
            Duong,C., Bared,G.M., Buchler,C. and Schmitz,G.
  TITLE     Complete coding sequence, promoter region, and genomic structure of
            the human ABCA2 gene and evidence for sterol-dependent regulation
            in macrophages
  JOURNAL   Biochem Biophys Res Commun 281 (1), 249-258 (2001)
   PUBMED   11178988
REFERENCE   9  (residues 1 to 2434)
  AUTHORS   Zhou,C., Zhao,L., Inagaki,N., Guan,J., Nakajo,S., Hirabayashi,T.,
            Kikuyama,S. and Shioda,S.
  TITLE     Atp-binding cassette transporter ABC2/ABCA2 in the rat brain: a
            novel mammalian lysosome-associated membrane protein and a specific
            marker for oligodendrocytes but not for myelin sheaths
  JOURNAL   J Neurosci 21 (3), 849-857 (2001)
   PUBMED   11157071
REFERENCE   10 (residues 1 to 2434)
  AUTHORS   Zhao,L.X., Zhou,C.J., Tanaka,A., Nakata,M., Hirabayashi,T.,
            Amachi,T., Shioda,S., Ueda,K. and Inagaki,N.
  TITLE     Cloning, characterization and tissue distribution of the rat
            ATP-binding cassette (ABC) transporter ABC2/ABCA2
  JOURNAL   Biochem J 350 Pt 3 (Pt 3), 865-872 (2000)
   PUBMED   10970803
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB037937.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB037937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2434
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..2434
                     /product="ATP-binding cassette sub-family A member 2"
                     /note="ATP-binding cassette 2; ATP-binding cassette
                     transporter 2; ATP-binding cassette, sub-family A (ABC1),
                     member 2; ATP-binding cassette, subfamily A (ABC1), member
                     2"
                     /calculated_mol_wt=270798
     Region          1..2368
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            271
                     /site_type="methylation"
                     /note="N5-methylglutamine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZC7; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Region          354..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            420
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            476
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            484
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            530
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            549
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            590
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            699..719
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            750..770
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            782..802
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            813..833
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            857..877
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            893..913
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Region          1225..1246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZC7; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1461..1481
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1549
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1557
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Region          1587..1606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1776
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1793..1813
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1842..1862
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1873..1893
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1906..1926
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            1992..2012
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            2055
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     Site            2411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESR9.1)"
     CDS             1..2434
                     /gene="Abca2"
                     /gene_synonym="Abc2"
                     /coded_by="NM_024396.1:68..7372"
                     /db_xref="GeneID:79248"
                     /db_xref="RGD:620238"
ORIGIN      
        1 mgflhqlqll lwknvtlkrr spwvlafeif iplvlffill glrqkkptis vkeafytaap
       61 ltsagilpvm qslcpdgqrd efgflqyans tvtqllerln rvveesnlfd perpslgsel
      121 ealhqrleal ssgpgtwesh sarpavssfs ldsvardkre lwrflmqnls lpnstaqall
      181 aarvdpsevy rllfgplpdl dgklgflrkq epwshlgsnp lfqmeellla palleqltca
      241 pgsgelgril tmpeghqvdl qgyrdavcsg qataraqhfs dlatelrnql diakiaqqlg
      301 fnvpngsdpq pqapspqslq allgdlldvq kvlqdvdvls alalllpqga cagrapapqa
      361 gspsgpanst gvgantgpnt tveegtqspv tpaspdtlqg qcsafvqlwa glqpilcgnn
      421 rtiepealrr gnmsslgfts keqrnlgllv hlmtsnpkil yapagseadh vilkanetfa
      481 fvgnvthyaq vwlnisaeir sfleqgrlqq hlhwlqqyva dlrlhpeamn lsldelppal
      541 rldyfslpng tallqqldti dnaacgwiqf mskvsvdifk gfpdeesivn ytlnqayqdn
      601 vtvfasvifq trkdgslpph vhykirqnss ftektneirr aywrpgpntg grfyflygfv
      661 wiqdmierai intfvghdvv epgnyvqmfp ypcytrddfl fviehmmplc mviswvysva
      721 mtiqhivaek ehrlkevmkt mglnnavhwv awfitgfvql sisvtaltai lkygqvlmhs
      781 hvliiwlfla vyavatimfc flvsvlyska klasacggii yflsyvpymy vaireevahd
      841 kitafekcia slmsttafgl gskyfalyev agvgiqwhtf sqspvegddf nlllavtmlm
      901 vdtvvygvlt wyieavhpgm yglprpwyfp lqksywlgsg rtetwewswp wahaprlsvm
      961 eedqacames rhfeetrgme eepthlplvv cvdkltkvyk ndkklalnkl slnlyenqvv
     1021 sflghngagk tttmsiltgl fpptsgsati yghdirtemd eirknlgmcp qhnvlfdqlt
     1081 veehlwfysr lksmaqeeir kemdkmiedl elsnkrhslv qtlsggmkrk lsvaiafvgg
     1141 sraiildept agvdpyarra iwdlilkykp grtillsthh mdeadllgdr iaiishgklk
     1201 ccgsplflkg aygdgyrltl vkrpaepgts qepgmassps grpqlsncse mqvsqfirkh
     1261 vassllvsdt stelsyilps eavkkgafer lfqqlehsld alhlssfglm dttleevflk
     1321 vseedqslen seadvkesrk dalpgaeglt avesqagnla rcselaqsqa slqsassvgs
     1381 argdegagyt dgygdyrplf dnlqdpdsvs lqeaemeala rvgqgsrkle gwwlkmrqfh
     1441 gllvkrfhca rrnskalcsq illpaffvcv amtvalsvpe igdlpplvls psqyhnytqp
     1501 rgnfipyane erreyrlrls pdaspqqlvs tfrlpsgvga tcvlkspang slgpmlnlss
     1561 gesrllaarf fdsmclesft qglplsnfvp pppspapsds plspdedsll awntslppta
     1621 gpetwtwaps lprlvhepvr ctcsaqgtgf scpssvgghp pqmrvvtgdi ltditghnvs
     1681 eyllftsdrf rlhrygaitf gniqksipap igtrtplmvr kiavrrvaqv lynnkgyhsm
     1741 ptylnslnna ilranlpksk gnpaaygitv tnhpmnktsa slsldyllqg tdvviaifii
     1801 vamsfvpasf vvflvaekst kakhlqfvsg cnpviywlan yvwdmlnylv patcciiilf
     1861 vfdlpaytsp tnfpavlslf llygwsitpi mypasfwfev pssayvfliv inlfigitat
     1921 vatfllqlfe hdkdlkvvns ylkscflifp nynlghglme iayneyiney yakigqfdkm
     1981 kspfewdivt rglvamtveg fvgffltimc qynflrqpqr lpvstkpved dvdvaserqr
     2041 vlrgdadndm vkienltkvy ksrkigrila vdrlclgvrp gecfgllgvn gagktstfkm
     2101 ltgdesttgg eafvnghsvl kdllqvqqsl gycpqfdalf deltarehlq lytrlrgipw
     2161 kdeaqvvrwa lekleltkca dkpagsysgg nkrklstaia ligypafifl depttgmdpk
     2221 arrflwnlil dliktgrsvv ltshsmeece avctrlaimv ngrlrclgsi qhlknrfgdg
     2281 ymitvrtkss qnvkdvvrff nrnfpeamlk erhhtkvqyq lksehislaq vfskmehvvg
     2341 vlgiedysvs qttldnvfvn fakkqsdnve qqeaepstlp splgllsllr prpaptelra
     2401 lvadepedld tedeglisfe eeraqlsfnt dtlc
//
LOCUS       NP_037265                449 aa            linear   ROD 27-APR-2025
DEFINITION  glycine receptor subunit alpha-1 precursor [Rattus norvegicus].
ACCESSION   NP_037265
VERSION     NP_037265.1
DBSOURCE    REFSEQ: accession NM_013133.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Velazquez-Flores,M.A., Sanchez-Chavez,G., Morales-Lazaro,S.L., Ruiz
            Esparza-Garrido,R., Canizales-Ontiveros,A. and Salceda,R.
  TITLE     Streptozotocin-Induced Diabetic Rats Showed a Differential Glycine
            Receptor Expression in the Spinal Cord: A GlyR Role in Diabetic
            Neuropathy
  JOURNAL   Neurochem Res 49 (3), 684-691 (2024)
   PUBMED   38017313
  REMARK    GeneRIF: Streptozotocin-Induced Diabetic Rats Showed a Differential
            Glycine Receptor Expression in the Spinal Cord: A GlyR Role in
            Diabetic Neuropathy.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Ivica,J., Lape,R. and Sivilotti,L.G.
  TITLE     Acidic pH reduces agonist efficacy and responses to synaptic-like
            glycine applications in zebrafish alpha1 and rat alpha1beta
            recombinant glycine receptors
  JOURNAL   J Physiol 600 (2), 333-347 (2022)
   PUBMED   34802146
  REMARK    GeneRIF: Acidic pH reduces agonist efficacy and responses to
            synaptic-like glycine applications in zebrafish alpha1 and rat
            alpha1beta recombinant glycine receptors.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Schaefer,N., Berger,A., van Brederode,J., Zheng,F., Zhang,Y.,
            Leacock,S., Littau,L., Jablonka,S., Malhotra,S., Topf,M.,
            Winter,F., Davydova,D., Lynch,J.W., Paige,C.J., Alzheimer,C.,
            Harvey,R.J. and Villmann,C.
  TITLE     Disruption of a Structurally Important Extracellular Element in the
            Glycine Receptor Leads to Decreased Synaptic Integration and
            Signaling Resulting in Severe Startle Disease
  JOURNAL   J Neurosci 37 (33), 7948-7961 (2017)
   PUBMED   28724750
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Zhou,W., Zhou,L.Q., Shi,H., Leng,Y.M., Liu,B., Zhang,S.L. and
            Kong,W.J.
  TITLE     Expression of glycine receptors and gephyrin in rat medial
            vestibular nuclei and flocculi following unilateral labyrinthectomy
  JOURNAL   Int J Mol Med 38 (5), 1481-1489 (2016)
   PUBMED   28026001
  REMARK    GeneRIF: the role of gephyrin and glycine receptor (GlyR) in
            vestibular compensation, was investigated.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Zhang,Y., Bode,A., Nguyen,B., Keramidas,A. and Lynch,J.W.
  TITLE     Investigating the Mechanism by Which Gain-of-function Mutations to
            the alpha1 Glycine Receptor Cause Hyperekplexia
  JOURNAL   J Biol Chem 291 (29), 15332-15341 (2016)
   PUBMED   27226610
  REMARK    GeneRIF: gain-of-function GLRA1 mutations also cause hyperekplexia,
            although the mechanism is unknown. Here we identify two new
            gain-of-function mutations (I43F and W170S) and characterize these
            along with known gain-of-function mutations (Q226E, V280M, and
            R414H) to identify how they cause hyperekplexia.
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Becker,C.M., Schmieden,V., Tarroni,P., Strasser,U. and Betz,H.
  TITLE     Isoform-selective deficit of glycine receptors in the mouse mutant
            spastic
  JOURNAL   Neuron 8 (2), 283-289 (1992)
   PUBMED   1371219
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Akagi,H., Hirai,K. and Hishinuma,F.
  TITLE     Functional properties of strychnine-sensitive glycine receptors
            expressed in Xenopus oocytes injected with a single mRNA
  JOURNAL   Neurosci Res 11 (1), 28-40 (1991)
   PUBMED   1716350
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Malosio,M.L., Grenningloh,G., Kuhse,J., Schmieden,V., Schmitt,B.,
            Prior,P. and Betz,H.
  TITLE     Alternative splicing generates two variants of the alpha 1 subunit
            of the inhibitory glycine receptor
  JOURNAL   J Biol Chem 266 (4), 2048-2053 (1991)
   PUBMED   1703526
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Ruiz-Gomez,A., Morato,E., Garcia-Calvo,M., Valdivieso,F. and
            Mayor,F. Jr.
  TITLE     Localization of the strychnine binding site on the 48-kilodalton
            subunit of the glycine receptor
  JOURNAL   Biochemistry 29 (30), 7033-7040 (1990)
   PUBMED   2171639
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Grenningloh,G., Schmieden,V., Schofield,P.R., Seeburg,P.H.,
            Siddique,T., Mohandas,T.K., Becker,C.M. and Betz,H.
  TITLE     Alpha subunit variants of the human glycine receptor: primary
            structures, functional expression and chromosomal localization of
            the corresponding genes
  JOURNAL   EMBO J 9 (3), 771-776 (1990)
   PUBMED   2155780
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D00833.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D00833.1, AJ310834.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..449
                     /product="glycine receptor subunit alpha-1 precursor"
                     /note="glycine receptor, alpha 1 subunit; glycine receptor
                     subunit alpha-1; glycine receptor 48 kDa subunit; glycine
                     receptor strychnine-binding subunit"
                     /calculated_mol_wt=48382
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3322
     Region          7..438
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     mat_peptide     29..449
                     /product="glycine receptor subunit alpha-1"
                     /calculated_mol_wt=48382
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P07727.4)"
     Site            251..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07727.4)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07727.4)"
     Site            289
                     /site_type="other"
                     /note="Important for obstruction of the ion pore in the
                     closed conformation.
                     /evidence=ECO:0000250|UniProtKB:O93430; propagated from
                     UniProtKB/Swiss-Prot (P07727.4)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07727.4)"
     Site            418..438
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07727.4)"
     CDS             1..449
                     /gene="Glra1"
                     /gene_synonym="GLYRA1"
                     /coded_by="NM_013133.1:185..1534"
                     /db_xref="GeneID:25674"
                     /db_xref="RGD:2704"
ORIGIN      
        1 mysfntlrfy lwetivffsl aaskeadaar sapkpmspsd fldklmgrts gydarirpnf
       61 kgppvnvscn ifinsfgsia ettmdyrvni flrqqwndpr layneypdds ldldpsmlds
      121 iwkpdlffan ekgahfheit tdnkllrisr ngnvlysiri tltlacpmdl knfpmdvqtc
      181 imqlesfgyt mndlifewqe qgavqvadgl tlpqfilkee kdlryctkhy ntgkftciea
      241 rfhlerqmgy yliqmyipsl livilswisf winmdaapar vglgittvlt mttqssgsra
      301 slpkvsyvka idiwmavcll fvfsalleya avnfvsrqhk ellrfrrkrr hhkddeggeg
      361 rfnfsaygmg paclqakdgi svkgannnnt tnpapapsks peemrklfiq rakkidkisr
      421 igfpmaflif nmfywiiyki vrredvhnk
//
LOCUS       NP_113969                569 aa            linear   ROD 27-APR-2025
DEFINITION  amyloid-beta A4 precursor protein-binding family A member 3 [Rattus
            norvegicus].
ACCESSION   NP_113969
VERSION     NP_113969.1
DBSOURCE    REFSEQ: accession NM_031781.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Hirose,Y., Johnson,Z.I., Schoepflin,Z.R., Markova,D.Z., Chiba,K.,
            Toyama,Y., Shapiro,I.M. and Risbud,M.V.
  TITLE     FIH-1-Mint3 axis does not control HIF-1 transcriptional activity in
            nucleus pulposus cells
  JOURNAL   J Biol Chem 289 (30), 20594-20605 (2014)
   PUBMED   24867948
  REMARK    GeneRIF: FIH-1-Mint3 axis does not control HIF-1 transcriptional
            activity in nucleus pulposus cells.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Sakamoto,T. and Seiki,M.
  TITLE     Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1)
            in macrophages by suppressing the activity of factor inhibiting
            HIF-1
  JOURNAL   J Biol Chem 284 (44), 30350-30359 (2009)
   PUBMED   19726677
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Ho,A., Morishita,W., Atasoy,D., Liu,X., Tabuchi,K., Hammer,R.E.,
            Malenka,R.C. and Sudhof,T.C.
  TITLE     Genetic analysis of Mint/X11 proteins: essential presynaptic
            functions of a neuronal adaptor protein family
  JOURNAL   J Neurosci 26 (50), 13089-13101 (2006)
   PUBMED   17167098
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Biederer,T., Cao,X., Sudhof,T.C. and Liu,X.
  TITLE     Regulation of APP-dependent transcription complexes by Mint/X11s:
            differential functions of Mint isoforms
  JOURNAL   J Neurosci 22 (17), 7340-7351 (2002)
   PUBMED   12196555
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Okamoto,M. and Sudhof,T.C.
  TITLE     Mint 3: a ubiquitous mint isoform that does not bind to munc18-1 or
            -2
  JOURNAL   Eur J Cell Biol 77 (3), 161-165 (1998)
   PUBMED   9860131
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Gynther,B.D., Vickery,R.M. and Rowe,M.J.
  TITLE     Responses of slowly adapting type II afferent fibres in cat hairy
            skin to vibrotactile stimuli
  JOURNAL   J Physiol 458, 151-169 (1992)
   PUBMED   1302262
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF029109.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF029109.1, BC161842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..569
                     /product="amyloid-beta A4 precursor protein-binding family
                     A member 3"
                     /note="mint-3; adapter protein X11gamma; neuron-specific
                     X11L2 protein; neuronal Munc18-1-interacting protein 3;
                     amyloid beta (A4) precursor protein-binding, family A,
                     member 3 (X11-like 2)"
                     /calculated_mol_wt=60509
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70248.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O96018; propagated from
                     UniProtKB/Swiss-Prot (O70248.2)"
     Region          124..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70248.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O70248.2)"
     Region          208..359
                     /region_name="PTB_X11"
                     /note="X11-like Phosphotyrosine-binding (PTB) domain;
                     cd01208"
                     /db_xref="CDD:269919"
     Site            order(219,297,329)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269919"
     Site            order(237,286,289..294,337,348,351)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269919"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O96018; propagated from
                     UniProtKB/Swiss-Prot (O70248.2)"
     Region          388..473
                     /region_name="PDZ1_APBA1_3-like"
                     /note="PDZ domain 1 of amyloid-beta A4 precursor
                     protein-binding family A member 1 (APBA1), APBA2, APBA3,
                     and related domains; cd06720"
                     /db_xref="CDD:467203"
     Site            order(399..405,419,422,452,456,459..460)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467203"
     Region          477..553
                     /region_name="PDZ2_APBA1_3-like"
                     /note="PDZ domain 2 of amyloid-beta A4 precursor
                     protein-binding family A member 1 (APBA1), APBA2, APBA3,
                     and related domains; cd06793"
                     /db_xref="CDD:467255"
     Site            order(491..497,502,505,534,538,541..542)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467255"
     CDS             1..569
                     /gene="Apba3"
                     /gene_synonym="Mint3"
                     /coded_by="NM_031781.1:85..1794"
                     /db_xref="GeneID:83611"
                     /db_xref="RGD:620846"
ORIGIN      
        1 meflpepqhp pgpptmdlee pkgpevpsed hpsntqgalg prgpdtlsem eldtssvral
       61 vqqlealpsd lggqfpdgap cplhiatgqg latqenldag gllsaeaggd nllgllrcea
      121 slpaqsvppd paqaaprllq ppedpggdpg wmegtepadn rssssspelw letaplvthr
      181 dppvgtqsqe tlascpavse vpgpcgqeel mdgvlfgaky lgstqllser npppstrmgq
      241 aqeamdrvka pegesqpmte vdifistkrv kvlaadsqda lmdhalqtis yiadigpvlv
      301 lmarrrlakr ttsqdrqrql ykmlchvfhs edaqliaqai gqafsiaysq flqengidps
      361 qvgmqpsasa shphngdldh fcnsqncrev ciqkrpgegl gvalvesgwg sllptavian
      421 llhggpaerc galsigdrvt aingtslvgl slaacqaavr evrrhssvtl siihcppvtt
      481 avihrphvre qlgfcvengi icsllrgsaa erggvrvghr iievngqsvv amphariiql
      541 ltetreihik tmpaatyrll tgqeqpvyl
//
LOCUS       NP_001101504             675 aa            linear   ROD 27-APR-2025
DEFINITION  protein PALS1 [Rattus norvegicus].
ACCESSION   NP_001101504 XP_001080868 XP_234328
VERSION     NP_001101504.1
DBSOURCE    REFSEQ: accession NM_001108034.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Kim,J.Y., Song,J.Y., Karnam,S., Park,J.Y., Lee,J.J., Kim,S. and
            Cho,S.H.
  TITLE     Common and distinctive localization patterns of Crumbs polarity
            complex proteins in the mammalian eye
  JOURNAL   Gene Expr Patterns 17 (1), 31-37 (2015)
   PUBMED   25636444
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Monastyrskaya,K., Sanchez-Freire,V., Hashemi Gheinani,A.,
            Klumpp,D.J., Babiychuk,E.B., Draeger,A. and Burkhard,F.C.
  TITLE     miR-199a-5p regulates urothelial permeability and may play a role
            in bladder pain syndrome
  JOURNAL   Am J Pathol 182 (2), 431-448 (2013)
   PUBMED   23201090
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Ozcelik,M., Cotter,L., Jacob,C., Pereira,J.A., Relvas,J.B.,
            Suter,U. and Tricaud,N.
  TITLE     Pals1 is a major regulator of the epithelial-like polarization and
            the extension of the myelin sheath in peripheral nerves
  JOURNAL   J Neurosci 30 (11), 4120-4131 (2010)
   PUBMED   20237282
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Ishiuchi,T., Misaki,K., Yonemura,S., Takeichi,M. and Tanoue,T.
  TITLE     Mammalian Fat and Dachsous cadherins regulate apical membrane
            organization in the embryonic cerebral cortex
  JOURNAL   J Cell Biol 185 (6), 959-967 (2009)
   PUBMED   19506035
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Wong,E.W., Mruk,D.D., Lee,W.M. and Cheng,C.Y.
  TITLE     Par3/Par6 polarity complex coordinates apical ectoplasmic
            specialization and blood-testis barrier restructuring during
            spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (28), 9657-9662 (2008)
   PUBMED   18621709
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Stucke,V.M., Timmerman,E., Vandekerckhove,J., Gevaert,K. and
            Hall,A.
  TITLE     The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
            facilitates epithelial tight junction formation
  JOURNAL   Mol Biol Cell 18 (5), 1744-1755 (2007)
   PUBMED   17332497
REFERENCE   8  (residues 1 to 675)
  AUTHORS   van Rossum,A.G., Aartsen,W.M., Meuleman,J., Klooster,J.,
            Malysheva,A., Versteeg,I., Arsanto,J.P., Le Bivic,A. and
            Wijnholds,J.
  TITLE     Pals1/Mpp5 is required for correct localization of Crb1 at the
            subapical region in polarized Muller glia cells
  JOURNAL   Hum Mol Genet 15 (18), 2659-2672 (2006)
   PUBMED   16885194
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Kantardzhieva,A., Gosens,I., Alexeeva,S., Punte,I.M., Versteeg,I.,
            Krieger,E., Neefjes-Mol,C.A., den Hollander,A.I., Letteboer,S.J.,
            Klooster,J., Cremers,F.P., Roepman,R. and Wijnholds,J.
  TITLE     MPP5 recruits MPP4 to the CRB1 complex in photoreceptors
  JOURNAL   Invest Ophthalmol Vis Sci 46 (6), 2192-2201 (2005)
   PUBMED   15914641
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Kamberov,E., Makarova,O., Roh,M., Liu,A., Karnak,D., Straight,S.
            and Margolis,B.
  TITLE     Molecular cloning and characterization of Pals, proteins associated
            with mLin-7
  JOURNAL   J Biol Chem 275 (15), 11425-11431 (2000)
   PUBMED   10753959
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473947.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234328.1, XP_001080868.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC168247.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..675
                     /product="protein PALS1"
                     /note="MAGUK p55 subfamily member 5; membrane protein,
                     palmitoylated 5 (MAGUK p55 subfamily member 5); membrane
                     palmitoylated protein 5; protein associated with Lin-7 1;
                     protein associated with LIN7 1, MAGUK family member"
                     /calculated_mol_wt=77022
     Region          1..345
                     /region_name="Required for the correct localization of
                     PALS1 and PATJ at cell-cell contacts and the normal
                     formation of tight junctions and adherens junctions.
                     /evidence=ECO:0000250|UniProtKB:Q9JLB2"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E7.1)"
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3R9; propagated from
                     UniProtKB/Swiss-Prot (B4F7E7.1)"
     Region          21..140
                     /region_name="Interaction with PARD6B.
                     /evidence=ECO:0000250|UniProtKB:Q9JLB2"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E7.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLB2; propagated from
                     UniProtKB/Swiss-Prot (B4F7E7.1)"
     Region          52..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E7.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3R9; propagated from
                     UniProtKB/Swiss-Prot (B4F7E7.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N3R9; propagated from
                     UniProtKB/Swiss-Prot (B4F7E7.1)"
     Region          123..170
                     /region_name="L27_N"
                     /note="pfam09060"
                     /db_xref="CDD:462666"
     Region          181..243
                     /region_name="Interaction with LIN7C.
                     /evidence=ECO:0000250|UniProtKB:Q9JLB2"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7E7.1)"
     Region          189..237
                     /region_name="L27"
                     /note="domain in receptor targeting proteins Lin-2 and
                     Lin-7; smart00569"
                     /db_xref="CDD:197794"
     Region          255..334
                     /region_name="PDZ_MPP5-like"
                     /note="PDZ domain of membrane palmitoylated protein 5
                     (MPP5), Drosophila Stardust, and related domains; cd06798"
                     /db_xref="CDD:467259"
     Site            order(266..272,281,284,314,318,321..322)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467259"
     Region          349..411
                     /region_name="SH3_MPP5"
                     /note="Src Homology 3 domain of Membrane Protein,
                     Palmitoylated 5 (or MAGUK p55 subfamily member 5);
                     cd12036"
                     /db_xref="CDD:212969"
     Site            order(351,375..376)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212969"
     Site            order(354,356,359,370,388..389,408,410..411)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212969"
     Site            order(486,492,509,516,519,528,551,556)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:238026"
     Site            order(486,492)
                     /site_type="other"
                     /note="G-X2-G-X-G-K"
                     /db_xref="CDD:238026"
     Region          491..661
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..675
                     /gene="Pals1"
                     /gene_synonym="Mpp5"
                     /coded_by="NM_001108034.1:252..2279"
                     /db_xref="GeneID:314259"
                     /db_xref="RGD:1308071"
ORIGIN      
        1 mttsymnghv teesdsgikn lglaspeehp khremavdcp gdlgtrlmpv rrsaqlerir
       61 qqqedmrrrr eeegkkqeld lnssmrlkkl aqippktgid npifdteegi vlesphyavk
      121 ilevedlfss lkhiqhtlvd sqsqedisll lqlvqnrdfq nafkihnavt vhmnkasppf
      181 plianvqdlv qevqtvlkpv hqkegqelta llnaphiqal llahdkvaeq emqlepitde
      241 rvyesighyg getvkivrie kardiplgat vrnemdsvii srivkggaae ksgllhegde
      301 vleingieir gkdvnevfdl lsdmhgtltf vlipsqqikp ppaketvihv kahfdydpsd
      361 dpyvpcrelg lsfqkgdilh visqedpnww qayregdedn qplaglvpgk sfqqqreamk
      421 qtieedkepe ksgklwcakk nkkkrkkvly nanknddydn eeiltyeems lyhqpanrkr
      481 piiligpqnc gqnelrqrlm nkekdrfasa vphttrnrrd hevagrdyhf vsrqafeadi
      541 aagkfiehge feknlygtsi dsvrqvinsg kicllslraq slktlrnsdl kpyiifiapp
      601 sqerlralla kegknpkpee lreiiektre meqnnghyfd taivnsdldk ayqellrlin
      661 kldtepqwvp stwlr
//
LOCUS       NP_659554                392 aa            linear   ROD 27-APR-2025
DEFINITION  SERPINE1 mRNA-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_659554 XP_342706
VERSION     NP_659554.1
DBSOURCE    REFSEQ: accession NM_145086.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Saito,A., Souza,E.E., Costa,F.C., Meirelles,G.V., Goncalves,K.A.,
            Santos,M.T., Bressan,G.C., McComb,M.E., Costello,C.E., Whelan,S.A.
            and Kobarg,J.
  TITLE     Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and
            Affects PML Nuclear Body Formation
  JOURNAL   J Proteome Res 16 (9), 3147-3157 (2017)
   PUBMED   28695742
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Peluso,J.J., Yuan,A., Liu,X. and Lodde,V.
  TITLE     Plasminogen activator inhibitor 1 RNA-binding protein interacts
            with progesterone receptor membrane component 1 to regulate
            progesterone's ability to maintain the viability of spontaneously
            immortalized granulosa cells and rat granulosa cells
  JOURNAL   Biol Reprod 88 (1), 20 (2013)
   PUBMED   23242527
  REMARK    GeneRIF: These studies support the concept that the interaction
            between PAIRBP1-PGRMC1 is an essential component of the mechanism
            through which progesterone inhibits apoptosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Peluso,J.J., Pappalardo,A., Losel,R. and Wehling,M.
  TITLE     Expression and function of PAIRBP1 within gonadotropin-primed
            immature rat ovaries: PAIRBP1 regulation of granulosa and luteal
            cell viability
  JOURNAL   Biol Reprod 73 (2), 261-270 (2005)
   PUBMED   15814896
  REMARK    GeneRIF: PAIRBP1 plays an important role in mediating the
            antiapoptotic action of progesterone in ovarian granulosa and
            luteal cells.
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Peluso,J.J., Pappalardo,A., Fernandez,G. and Wu,C.A.
  TITLE     Involvement of an unnamed protein, RDA288, in the mechanism through
            which progesterone mediates its antiapoptotic action in
            spontaneously immortalized granulosa cells
  JOURNAL   Endocrinology 145 (6), 3014-3022 (2004)
   PUBMED   14988380
  REMARK    GeneRIF: RDA288 in cytoplasm and plasma membrane components of
            granulosa cells of antral follicles. Present on extracellular
            surface of plasma membrane. RDA288 plays significant role in
            mediating progesterone's antiapoptotic action in granulosa cells.
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Blasi,F., Ciarrocchi,A., Luddi,A., Strazza,M., Riccio,M., Santi,S.,
            Arcone,R., Pietropaolo,C., D'Angelo,R., Costantino-Ceccarini,E. and
            Melli,M.
  TITLE     Stage-specific gene expression in early differentiating
            oligodendrocytes
  JOURNAL   Glia 39 (2), 114-123 (2002)
   PUBMED   12112363
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Heaton,J.H., Dlakic,W.M., Dlakic,M. and Gelehrter,T.D.
  TITLE     Identification and cDNA cloning of a novel RNA-binding protein that
            interacts with the cyclic nucleotide-responsive sequence in the
            Type-1 plasminogen activator inhibitor mRNA
  JOURNAL   J Biol Chem 276 (5), 3341-3347 (2001)
   PUBMED   11001948
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Sykes,D.E. and Weiser,M.M.
  TITLE     The identification of genes specifically expressed in epithelial
            cells of the rat intestinal crypts
  JOURNAL   Differentiation 50 (1), 41-46 (1992)
   PUBMED   1639225
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079337.1.
            
            On Jan 21, 2005 this sequence version replaced XP_342706.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079337.1, FQ228026.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q31"
     Protein         1..392
                     /product="SERPINE1 mRNA-binding protein 1"
                     /note="plasminogen activator inhibitor 1 RNA-binding
                     protein; RNA binding protein RDA288; PAI1 RNA-binding
                     protein 1; PAI-1 mRNA-binding protein; hypothetical RNA
                     binding protein RDA288"
                     /calculated_mol_wt=42853
     Region          5..151
                     /region_name="IHABP4_N"
                     /note="Intracellular hyaluronan-binding protein 4
                     N-terminal; pfam16174"
                     /db_xref="CDD:465041"
     Region          189..297
                     /region_name="HABP4_PAI-RBP1"
                     /note="Hyaluronan / mRNA binding family; pfam04774"
                     /db_xref="CDD:461421"
     CDS             1..392
                     /gene="Serbp1"
                     /gene_synonym="Pai-Rbp1; Pairbp1; Rda288"
                     /coded_by="NM_145086.1:66..1244"
                     /db_xref="GeneID:246303"
                     /db_xref="RGD:619907"
ORIGIN      
        1 mpghlqegfg cvvtnrfdql fddesdpfev lkaaenkkke aggggvggpg aksaaqaaaq
       61 tnsnaagkql rkesqkdrkn plppsvgvad kkeetqppva lkkegirrvg rrpdqqlqgd
      121 gkiidrrper rpprerrfek pleekgegge fsvdrpiier pirgrgglgr grggrgrgmg
      181 rgdgfdsrgk refdrhsgsd rssfshysgl khedkrggsg shnwgtvkde ltdleqsnvt
      241 eetpegeehp vadtenkene veevkeegpk emtldewkai qnkdrakvef nirkpnegad
      301 gqwkkgfvlh kskseeahae dsvmdhhfrk panditsqle infgdlgrpg rggrggrggr
      361 grggrpnrgs rtdkssasap dvddpeafpa la
//
LOCUS       NP_001094414             654 aa            linear   ROD 27-APR-2025
DEFINITION  sperm motility kinase [Rattus norvegicus].
ACCESSION   NP_001094414 XP_001070118
VERSION     NP_001094414.1
DBSOURCE    REFSEQ: accession NM_001100944.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128761.1.
            
            On Aug 12, 2007 this sequence version replaced XP_001070118.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128761.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: translation inferred
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..654
                     /product="sperm motility kinase"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=73716
     Region          23..270
                     /region_name="STKc_AMPK-like"
                     /note="Catalytic domain of AMP-activated protein
                     kinase-like Serine/Threonine Kinases; cd14003"
                     /db_xref="CDD:270905"
     Site            order(30..34,38,51,53,80,96..99,103,105..106,108,141..142,
                     144,146..147,149,159..160,163,177..181,183,213..216)
                     /site_type="active"
                     /db_xref="CDD:270905"
     Site            order(30..33,38,51,53,80,96..99,103,146..147,149,159..160)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270905"
     Site            order(103,105..106,108,142,144,146,163,177..181,183,
                     213..216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270905"
     Site            order(159..170,174..181)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270905"
     Region          290..329
                     /region_name="UBA_MARK_Par1"
                     /note="UBA domain found in microtubule-associated protein
                     (MAP)/microtubule affinity-regulating kinase (MARK)/
                     partitioning-defective 1 (Par-1) and similar proteins;
                     cd14337"
                     /db_xref="CDD:270522"
     Region          336..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5Q6.1)"
     Region          563..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5Q6.1)"
     CDS             1..654
                     /gene="Smok"
                     /gene_synonym="RGD1562638; RGD1564276"
                     /coded_by="NM_001100944.1:361..2325"
                     /db_xref="GeneID:290818"
                     /db_xref="RGD:1562638"
ORIGIN      
        1 mkrwqvcqdl rsspfqedal tdhyrilasl gqggfgevkl ashlltqtkv aikvlpksnk
       61 nlllkseiei mksldhphii kllhiidtne nifivlehav ggelltried fgylpeeecn
      121 rlfrqmvlal qychqrgiih rdikpenill dhkgnvklsd fglstkivmg qklttlcgtl
      181 pycapelfnl ngydgqaidv wslgvvlyym atgclpfqgf tyqaikqkil sgrysvnfrl
      241 spdlwdviak lltvnprerp rvheilrfnw lknenevsps slggntdshp dptilvmmgd
      301 mgyeqgqire slrerkfdqv matylmlrek acsedksikt phptqcaqtl kstgsttekq
      361 ttlrrgsslp tlttfylpsk leslnkekrt tmrhtmppnl ncfnksesln kgrrtivsht
      421 isptlncfnk seslnkgkrt ivrhtmppkk tspvrricpr lhksfgmgsa sedsskrnss
      481 dpsltifssq sfmsafkygs tyskrkaflq cilhyhasqe edqykttiip sgklnttvpp
      541 nslqedqptg hlhnvltaga vdnrnlqeks ppfsttatkg egpaikeres ipssprapre
      601 qfrgrsqtpp rapfrrrvwk tlksgflkgl gslccclpiq kkvhpasnrv ppmk
//
LOCUS       NP_001099580             475 aa            linear   ROD 27-APR-2025
DEFINITION  doublecortin domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001099580 XP_001070222 XP_225316
VERSION     NP_001099580.2
DBSOURCE    REFSEQ: accession NM_001106110.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Mascheretti,S., Trezzi,V., Giorda,R., Boivin,M., Plourde,V.,
            Vitaro,F., Brendgen,M., Dionne,G. and Marino,C.
  TITLE     Complex effects of dyslexia risk factors account for ADHD traits:
            evidence from two independent samples
  JOURNAL   J Child Psychol Psychiatry 58 (1), 75-82 (2017)
   PUBMED   27501527
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Girard,M., Bizet,A.A., Lachaux,A., Gonzales,E., Filhol,E.,
            Collardeau-Frachon,S., Jeanpierre,C., Henry,C., Fabre,M.,
            Viremouneix,L., Galmiche,L., Debray,D., Bole-Feysot,C.,
            Nitschke,P., Pariente,D., Guettier,C., Lyonnet,S., Heidet,L.,
            Bertholet,A., Jacquemin,E., Henrion-Caude,A. and Saunier,S.
  TITLE     DCDC2 Mutations Cause Neonatal Sclerosing Cholangitis
  JOURNAL   Hum Mutat 37 (10), 1025-1029 (2016)
   PUBMED   27319779
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Che,A., Truong,D.T., Fitch,R.H. and LoTurco,J.J.
  TITLE     Mutation of the Dyslexia-Associated Gene Dcdc2 Enhances
            Glutamatergic Synaptic Transmission Between Layer 4 Neurons in
            Mouse Neocortex
  JOURNAL   Cereb Cortex 26 (9), 3705-3718 (2016)
   PUBMED   26250775
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Zhang,Y., Li,J., Song,S., Tardif,T., Burmeister,M.,
            Villafuerte,S.M., Su,M., McBride,C. and Shu,H.
  TITLE     Association of DCDC2 Polymorphisms with Normal Variations in
            Reading Abilities in a Chinese Population
  JOURNAL   PLoS One 11 (4), e0153603 (2016)
   PUBMED   27100778
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Grati,M., Chakchouk,I., Ma,Q., Bensaid,M., Desmidt,A., Turki,N.,
            Yan,D., Baanannou,A., Mittal,R., Driss,N., Blanton,S., Farooq,A.,
            Lu,Z., Liu,X.Z. and Masmoudi,S.
  TITLE     A missense mutation in DCDC2 causes human recessive deafness
            DFNB66, likely by interfering with sensory hair cell and supporting
            cell cilia length regulation
  JOURNAL   Hum Mol Genet 24 (9), 2482-2491 (2015)
   PUBMED   25601850
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Wilcke,A., Weissfuss,J., Kirsten,H., Wolfram,G., Boltze,J. and
            Ahnert,P.
  TITLE     The role of gene DCDC2 in German dyslexics
  JOURNAL   Ann Dyslexia 59 (1), 1-11 (2009)
   PUBMED   19238550
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Burbridge,T.J., Wang,Y., Volz,A.J., Peschansky,V.J., Lisann,L.,
            Galaburda,A.M., Lo Turco,J.J. and Rosen,G.D.
  TITLE     Postnatal analysis of the effect of embryonic knockdown and
            overexpression of candidate dyslexia susceptibility gene homolog
            Dcdc2 in the rat
  JOURNAL   Neuroscience 152 (3), 723-733 (2008)
   PUBMED   18313856
  REMARK    GeneRIF: These results support the claim that knockdown of Dcdc2
            expression results in neuronal migration disorders similar to those
            seen in the brains of dyslexics.
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Wang,Y., Paramasivam,M., Thomas,A., Bai,J., Kaminen-Ahola,N.,
            Kere,J., Voskuil,J., Rosen,G.D., Galaburda,A.M. and Loturco,J.J.
  TITLE     DYX1C1 functions in neuronal migration in developing neocortex
  JOURNAL   Neuroscience 143 (2), 515-522 (2006)
   PUBMED   16989952
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Meng,H., Smith,S.D., Hager,K., Held,M., Liu,J., Olson,R.K.,
            Pennington,B.F., DeFries,J.C., Gelernter,J., O'Reilly-Pol,T.,
            Somlo,S., Skudlarski,P., Shaywitz,S.E., Shaywitz,B.A.,
            Marchione,K., Wang,Y., Paramasivam,M., LoTurco,J.J., Page,G.P. and
            Gruen,J.R.
  TITLE     DCDC2 is associated with reading disability and modulates neuronal
            development in the brain
  JOURNAL   Proc Natl Acad Sci U S A 102 (47), 17053-17058 (2005)
   PUBMED   16278297
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2005 Dec 20;102(51):18763]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000017.1.
            
            On Feb 14, 2008 this sequence version replaced NP_001099580.1.
            
            Summary: This gene encodes a member of the doublecortin family. The
            protein encoded by this gene contains two doublecortin domains. The
            doublecortin domain has been demonstrated to bind tubulin and
            enhance microtubule polymerization. Knockdown of this gene
            expression results in neuronal migration disorders similar to those
            seen in the brains of dyslexics. [provided by RefSeq, Sep 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.71894.1,
                                           SRR26643287.33768.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..475
                     /product="doublecortin domain-containing protein 2"
                     /calculated_mol_wt=51902
     Region          17..96
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          138..217
                     /region_name="DCX2_DCDC2"
                     /note="Doublecortin-like domain 2 found in doublecortin
                     domain-containing protein 2 (DCDC2); cd17152"
                     /db_xref="CDD:340672"
     Region          234..475
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZR10.1)"
     Region          <250..>445
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZR10.1)"
     CDS             1..475
                     /gene="Dcdc2"
                     /coded_by="NM_001106110.2:41..1468"
                     /db_xref="GeneID:291130"
                     /db_xref="RGD:1310227"
ORIGIN      
        1 mngpsprssh lsqpvvksvl vyrngdpffa grrvvihekk vssfdiflke vtggvqapfg
       61 avrniytprt ghrirkldqi esggnyvagg qeafkklnyl digeikkrpm eavntevkpv
      121 ihskinvsar frkalhepct ifliangdli spasrllipr kalnqwdhvl qmvtekitlr
      181 sgavhrlytl egklvesgae lengqfyvav grdkfkrlpy sellfdksam rrpygqkass
      241 lppmvgsrks kgsgnyrqsk stigssdnss pqplkrkgkk dsnsekptkv kqsvksknsh
      301 qaipdndegi fkagaerset rgaaevqede dtqvevpvdq rpaeivdeee dgektskdan
      361 qkddfsamng eaedragskv adapeeeegi pdqgekkasp srvnggtdee ngeeldqvte
      421 elqptvdekg kaegdnsaqd eagldaqrpp rpevtvtspq enegnesnka ssava
//
LOCUS       NP_001076008             334 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein D0 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001076008
VERSION     NP_001076008.1
DBSOURCE    REFSEQ: accession NM_001082539.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Yan,J., Du,F., Li,S.D., Yuan,Y., Jiang,J.Y., Li,S., Li,X.Y. and
            Du,Z.X.
  TITLE     AUF1 modulates TGF-beta signal in renal tubular epithelial cells
            via post-transcriptional regulation of Nedd4L expression
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (1), 48-56 (2018)
   PUBMED   28986222
  REMARK    GeneRIF: AUF1 might be a potential player in renal
            tubulointerstitial fibrosis through modulation of TGF-beta signal
            transduction via posttranscriptional regulation of Nedd4L.
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Castellanos-Rubio,A., Fernandez-Jimenez,N., Kratchmarov,R., Luo,X.,
            Bhagat,G., Green,P.H., Schneider,R., Kiledjian,M., Bilbao,J.R. and
            Ghosh,S.
  TITLE     A long noncoding RNA associated with susceptibility to celiac
            disease
  JOURNAL   Science 352 (6281), 91-95 (2016)
   PUBMED   27034373
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Lee,K.H., Kim,S.H., Kim,H.J., Kim,W., Lee,H.R., Jung,Y., Choi,J.H.,
            Hong,K.Y., Jang,S.K. and Kim,K.T.
  TITLE     AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic
            translation
  JOURNAL   Nucleic Acids Res 42 (6), 3590-3606 (2014)
   PUBMED   24423872
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Raineri,I., Wegmueller,D., Gross,B., Certa,U. and Moroni,C.
  TITLE     Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover
            studied by RNA interference
  JOURNAL   Nucleic Acids Res 32 (4), 1279-1288 (2004)
   PUBMED   14976220
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Arao,Y., Kikuchi,A., Ikeda,K., Nomoto,S., Horiguchi,H. and
            Kayama,F.
  TITLE     A+U-rich-element RNA-binding factor 1/heterogeneous nuclear
            ribonucleoprotein D gene expression is regulated by oestrogen in
            the rat uterus
  JOURNAL   Biochem J 361 (Pt 1), 125-132 (2002)
   PUBMED   11742537
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Ehrenman,K., Long,L., Wagner,B.J. and Brewer,G.
  TITLE     Characterization of cDNAs encoding the murine A+U-rich RNA-binding
            protein AUF1
  JOURNAL   Gene 149 (2), 315-319 (1994)
   PUBMED   7959009
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Ishikawa,F., Matunis,M.J., Dreyfuss,G. and Cech,T.R.
  TITLE     Nuclear proteins that bind the pre-mRNA 3' splice site sequence
            r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
  JOURNAL   Mol Cell Biol 13 (7), 4301-4310 (1993)
   PUBMED   8321232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO560068.1, AB046616.1 and CB798484.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF110094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..334
                     /product="heterogeneous nuclear ribonucleoprotein D0
                     isoform b"
                     /note="heterogeneous nuclear ribonucleoprotein D0; hnRNP
                     D0; AU-rich element RNA-binding protein 1; AU-rich element
                     RNA-binding factor 1; RNA binding protein p45AUF1"
                     /calculated_mol_wt=35911
     Region          <55..76
                     /region_name="CBFNT"
                     /note="CBFNT (NUC161) domain; pfam08143"
                     /db_xref="CDD:311868"
     Region          78..151
                     /region_name="RRM1_hnRNPD"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12756"
                     /db_xref="CDD:410150"
     Region          162..236
                     /region_name="RRM2_hnRNPD"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein D0 (hnRNP D0) and
                     similar proteins; cd12583"
                     /db_xref="CDD:241027"
     Site            order(162,164,166..167,191..194,196..197,200..202,204,206,
                     223,230..232,234..236)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:241027"
     CDS             1..334
                     /gene="Hnrnpd"
                     /gene_synonym="Auf1; Hnrpd"
                     /coded_by="NM_001082539.1:286..1290"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:79256"
                     /db_xref="RGD:620365"
ORIGIN      
        1 mseeqfggdg aaaaataavg gsageqegam vaaaqgaaaa agsgsgggsa pggteggste
       61 aegakidask needegkmfi gglswdttkk dlkdyfskfg dvvdctlkld pitgrsrgfg
      121 fvlfkesesv dkvmdqkehk lngkvidpkr akamktkepv kkifvgglsp dtpeekirey
      181 fggfgevesi elpmdnktnk rrgfcfitfk eeepvkkime kkyhnvglsk ceikvamske
      241 qyqqqqqwgs rggfagrarg rgggpsqnwn qgysnywnqg ygsygynsqg yggyggydyt
      301 gynsyygygd ysnqqsgygk vsrrgghqns ykpy
//
LOCUS       NP_113771               1217 aa            linear   ROD 27-APR-2025
DEFINITION  structural maintenance of chromosomes protein 3 [Rattus
            norvegicus].
ACCESSION   NP_113771
VERSION     NP_113771.2
DBSOURCE    REFSEQ: accession NM_031583.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Dong,X., Chen,G., Cai,Z., Li,Z., Qiu,L., Xu,H., Yuan,Y., Liu,X.L.
            and Liu,J.
  TITLE     CDK13 RNA Over-Editing Mediated by ADAR1 Associates with Poor
            Prognosis of Hepatocellular Carcinoma Patients
  JOURNAL   Cell Physiol Biochem 47 (6), 2602-2612 (2018)
   PUBMED   29996118
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Gil-Rodriguez,M.C., Deardorff,M.A., Ansari,M., Tan,C.A.,
            Parenti,I., Baquero-Montoya,C., Ousager,L.B., Puisac,B.,
            Hernandez-Marcos,M., Teresa-Rodrigo,M.E., Marcos-Alcalde,I.,
            Wesselink,J.J., Lusa-Bernal,S., Bijlsma,E.K., Braunholz,D.,
            Bueno-Martinez,I., Clark,D., Cooper,N.S., Curry,C.J., Fisher,R.,
            Fryer,A., Ganesh,J., Gervasini,C., Gillessen-Kaesbach,G., Guo,Y.,
            Hakonarson,H., Hopkin,R.J., Kaur,M., Keating,B.J., Kibaek,M.,
            Kinning,E., Kleefstra,T., Kline,A.D., Kuchinskaya,E., Larizza,L.,
            Li,Y.R., Liu,X., Mariani,M., Picker,J.D., Pie,A., Pozojevic,J.,
            Queralt,E., Richer,J., Roeder,E., Sinha,A., Scott,R.H., So,J.,
            Wusik,K.A., Wilson,L., Zhang,J., Gomez-Puertas,P., Casale,C.H.,
            Strom,L., Selicorni,A., Ramos,F.J., Jackson,L.G., Krantz,I.D.,
            Das,S., Hennekam,R.C., Kaiser,F.J., FitzPatrick,D.R. and Pie,J.
  TITLE     De novo heterozygous mutations in SMC3 cause a range of Cornelia de
            Lange syndrome-overlapping phenotypes
  JOURNAL   Hum Mutat 36 (4), 454-462 (2015)
   PUBMED   25655089
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Liu,H., Rankin,S. and Yu,H.
  TITLE     Phosphorylation-enabled binding of SGO1-PP2A to cohesin protects
            sororin and centromeric cohesion during mitosis
  JOURNAL   Nat Cell Biol 15 (1), 40-49 (2013)
   PUBMED   23242214
  REMARK    Erratum:[Nat Cell Biol. 2013 Feb;15(2):229]
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Llano,E., Herran,Y., Garcia-Tunon,I., Gutierrez-Caballero,C., de
            Alava,E., Barbero,J.L., Schimenti,J., de Rooij,D.G.,
            Sanchez-Martin,M. and Pendas,A.M.
  TITLE     Meiotic cohesin complexes are essential for the formation of the
            axial element in mice
  JOURNAL   J Cell Biol 197 (7), 877-885 (2012)
   PUBMED   22711701
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Bermudez,V.P., Farina,A., Higashi,T.L., Du,F., Tappin,I.,
            Takahashi,T.S. and Hurwitz,J.
  TITLE     In vitro loading of human cohesin on DNA by the human Scc2-Scc4
            loader complex
  JOURNAL   Proc Natl Acad Sci U S A 109 (24), 9366-9371 (2012)
   PUBMED   22628566
REFERENCE   6  (residues 1 to 1217)
  AUTHORS   Eijpe,M., Heyting,C., Gross,B. and Jessberger,R.
  TITLE     Association of mammalian SMC1 and SMC3 proteins with meiotic
            chromosomes and synaptonemal complexes
  JOURNAL   J Cell Sci 113 (Pt 4), 673-682 (2000)
   PUBMED   10652260
REFERENCE   7  (residues 1 to 1217)
  AUTHORS   Darwiche,N., Freeman,L.A. and Strunnikov,A.
  TITLE     Characterization of the components of the putative mammalian sister
            chromatid cohesion complex
  JOURNAL   Gene 233 (1-2), 39-47 (1999)
   PUBMED   10375619
REFERENCE   8  (residues 1 to 1217)
  AUTHORS   Schmiesing,J.A., Ball,A.R. Jr., Gregson,H.C., Alderton,J.M.,
            Zhou,S. and Yokomori,K.
  TITLE     Identification of two distinct human SMC protein complexes involved
            in mitotic chromosome dynamics
  JOURNAL   Proc Natl Acad Sci U S A 95 (22), 12906-12911 (1998)
   PUBMED   9789013
REFERENCE   9  (residues 1 to 1217)
  AUTHORS   Wu,R.R. and Couchman,J.R.
  TITLE     cDNA cloning of the basement membrane chondroitin sulfate
            proteoglycan core protein, bamacan: a five domain structure
            including coiled-coil motifs
  JOURNAL   J Cell Biol 136 (2), 433-444 (1997)
   PUBMED   9015313
REFERENCE   10 (residues 1 to 1217)
  AUTHORS   Couchman,J.R., Kapoor,R., Sthanam,M. and Wu,R.R.
  TITLE     Perlecan and basement membrane-chondroitin sulfate proteoglycan
            (bamacan) are two basement membrane chondroitin/dermatan sulfate
            proteoglycans in the Engelbreth-Holm-Swarm tumor matrix
  JOURNAL   J Biol Chem 271 (16), 9595-9602 (1996)
   PUBMED   8621634
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BE109731.1, EV773232.1, BF396983.1, EV776219.1, CA511001.1,
            BP486487.1, BP499171.1, CO395251.1 and CA509998.1.
            
            On Oct 20, 2007 this sequence version replaced NP_113771.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1217
                     /product="structural maintenance of chromosomes protein 3"
                     /note="chondroitin sulfate proteoglycan 6; chromosome
                     segregation protein SmcD; basement membrane-associated
                     chondroitin proteoglycan; SMC protein 3; basement membrane
                     chondroitin sulfate proteoglycan; structural maintenace of
                     chromosomes 3"
                     /calculated_mol_wt=141411
     Region          2..1197
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; pfam02463"
                     /db_xref="CDD:426784"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Region          242..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97690.1)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            1013
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CW03; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Region          1059..1090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97690.1)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            1074
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     Site            1083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQE7; propagated from
                     UniProtKB/Swiss-Prot (P97690.1)"
     CDS             1..1217
                     /gene="Smc3"
                     /gene_synonym="bamacan; Cspg6; SMC-3"
                     /coded_by="NM_031583.2:123..3776"
                     /db_xref="GeneID:29486"
                     /db_xref="RGD:62006"
ORIGIN      
        1 myikqviiqg frsyrdqtiv dpfsskhnvi vgrngsgksn ffyaiqfvls defshlrpeq
       61 rlallhegtg prvisafvei ifdnsdnrlp idkeevslrr vigakkdqyf ldkkmvtknd
      121 vmnllesagf srsnpyyivk qgkinqmata pdsqrlkllr evagtrvyde rkeesislmk
      181 etegkrekin ellkyieerl htleeekeel aqyqkwdkmr raleytiynq elnetrakld
      241 elsakretsg eksrqlrdaq qdardkmedi erqvrelktk isamkeekeq lsaerqeqik
      301 qrtklelkak dlqdelagns eqrkrllker qkllekieek qkelaetepk fnsvkekeer
      361 giarlaqatq ertdlyakqg rgsqftskee rdkwikkelk sldqaindkk rqiaaihkdl
      421 edteankekn leqynkldqd lnevkarvee ldrkyyevkn kkdelqsern ylwreenaeq
      481 qalaakredl ekkqqllraa tgkailngid sinkvldhfr rkginqhvqn gyhgivmnnf
      541 ecepafytcv evtagnrlfy hivdsdevst kilmefnkmn lpgevtflpl nkldvrdtay
      601 petndaipmi sklrynprfd kafkhvfgkt licrsmevst qlaraftmdc itlegdqvsh
      661 rgaltggyyd trksrlelqk dvrkaeeelg eleaklnenl rrnierinne idqlmnqmqq
      721 ietqqrkfka srdsilsemk mlkekrqqse ktfmpkqrsl qsleaslham estreslkae
      781 lgtdllsqls ledqkrvdal ndeirqlqqe nrqllnerik legiitrvet ylnenlrkrl
      841 dqveqelnel reteggtvlt attseleain krvkdtmars edldnsidkt eagikelqks
      901 merwknmeke hmdainhdtk elekmtnrqg mllkkkeecm kkirelgslp qeafekyqtl
      961 slkqlfrkle qcntelkkys hvnkkaldqf vnfseqkekl ikrqeeldrg yksimelmnv
     1021 lelrkyeaiq ltfkqvsknf sevfqklvpg gkatlvmkkg dvegsqsqde gegsgeserg
     1081 sgsqssvpsv dqftgvgirv sftgkqgemr emqqlsggqk slvalalifa iqkcdpapfy
     1141 lfdeidqald aqhrkavsdm imelavhaqf itttfrpell esadkfygvk frnkvshidv
     1201 itaemakdfv eddtthg
//
LOCUS       NP_001099558             339 aa            linear   ROD 27-APR-2025
DEFINITION  erlin-2 [Rattus norvegicus].
ACCESSION   NP_001099558 XP_001061817 XP_214372
VERSION     NP_001099558.1
DBSOURCE    REFSEQ: accession NM_001106088.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Fork,C., Hitzel,J., Nichols,B.J., Tikkanen,R. and Brandes,R.P.
  TITLE     Flotillin-1 facilitates toll-like receptor 3 signaling in human
            endothelial cells
  JOURNAL   Basic Res Cardiol 109 (6), 439 (2014)
   PUBMED   25204797
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Huber,M.D., Vesely,P.W., Datta,K. and Gerace,L.
  TITLE     Erlins restrict SREBP activation in the ER and regulate cellular
            cholesterol homeostasis
  JOURNAL   J Cell Biol 203 (3), 427-436 (2013)
   PUBMED   24217618
REFERENCE   3  (residues 1 to 339)
  AUTHORS   El Khouri,E., Le Pavec,G., Toledano,M.B. and Delaunay-Moisan,A.
  TITLE     RNF185 is a novel E3 ligase of endoplasmic reticulum-associated
            degradation (ERAD) that targets cystic fibrosis transmembrane
            conductance regulator (CFTR)
  JOURNAL   J Biol Chem 288 (43), 31177-31191 (2013)
   PUBMED   24019521
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Teranishi,Y., Hur,J.Y., Gu,G.J., Kihara,T., Ishikawa,T.,
            Nishimura,T., Winblad,B., Behbahani,H., Kamali-Moghaddam,M.,
            Frykman,S. and Tjernberg,L.O.
  TITLE     Erlin-2 is associated with active gamma-secretase in brain and
            affects amyloid beta-peptide production
  JOURNAL   Biochem Biophys Res Commun 424 (3), 476-481 (2012)
   PUBMED   22771797
  REMARK    GeneRIF: a novel brain gamma-secretase associated protein ,
            erlin-2, that resides in detergent resistant membranes and affects
            amyloid beta-peptide production.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Pearce,M.M., Wormer,D.B., Wilkens,S. and Wojcikiewicz,R.J.
  TITLE     An endoplasmic reticulum (ER) membrane complex composed of SPFH1
            and SPFH2 mediates the ER-associated degradation of inositol
            1,4,5-trisphosphate receptors
  JOURNAL   J Biol Chem 284 (16), 10433-10445 (2009)
   PUBMED   19240031
  REMARK    GeneRIF: Results suggest that this novel SPFH1/2 complex is a
            recognition factor that targets IP(3)Rs and perhaps other
            substrates for ERAD.
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Lyssand,J.S., DeFino,M.C., Tang,X.B., Hertz,A.L., Feller,D.B.,
            Wacker,J.L., Adams,M.E. and Hague,C.
  TITLE     Blood pressure is regulated by an alpha1D-adrenergic
            receptor/dystrophin signalosome
  JOURNAL   J Biol Chem 283 (27), 18792-18800 (2008)
   PUBMED   18468998
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Browman,D.T., Resek,M.E., Zajchowski,L.D. and Robbins,S.M.
  TITLE     Erlin-1 and erlin-2 are novel members of the prohibitin family of
            proteins that define lipid-raft-like domains of the ER
  JOURNAL   J Cell Sci 119 (Pt 15), 3149-3160 (2006)
   PUBMED   16835267
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168668.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001061817.1, XP_214372.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..339
                     /product="erlin-2"
                     /note="SPFH domain family, member 2; SPFH
                     domain-containing protein 2; endoplasmic reticulum lipid
                     raft-associated protein 2;
                     stomatin-prohibitin-flotillin-HflC/K domain-containing
                     protein 2"
                     /calculated_mol_wt=37579
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DEH2.1)"
     Region          16..308
                     /region_name="SPFH_like_u3"
                     /note="Uncharacterized family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03406"
                     /db_xref="CDD:259804"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B5DEH2.1)"
     Region          177..309
                     /region_name="Interaction with ERLIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DEH2.1)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75477; propagated from
                     UniProtKB/Swiss-Prot (B5DEH2.1)"
     CDS             1..339
                     /gene="Erlin2"
                     /gene_synonym="RGD1309010; Spfh2"
                     /coded_by="NM_001106088.2:50..1069"
                     /db_xref="GeneID:290823"
                     /db_xref="RGD:1309010"
ORIGIN      
        1 maqlgavvav assffcaslf savhkieegh igvyyrggal ltstsgpgfh lmlpfitsyk
       61 svqttlqtde vknvpcgtsg gvmiyfdrie vvnflvphav ydivknytad ydkalifnki
      121 hhelnqfcsv htlqevyiel fdqidenlkl alqqdltsma pglviqavrv tkpnipeair
      181 rnyelmesek tklliaaqkq kvvekeaete rkkalieaek vaqvaeityg qkvmeketek
      241 kiseiedaaf larekakada ecytalkiae anklkltpey lqlmkykaia snskiyfgkd
      301 ipnmfmdsag glgkqsegls dklgfglede pletatkdn
//
LOCUS       NP_001005873             779 aa            linear   ROD 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DHX40 [Rattus norvegicus].
ACCESSION   NP_001005873 XP_213429
VERSION     NP_001005873.1
DBSOURCE    REFSEQ: accession NM_001005873.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Xu,J., Wu,H., Zhang,C., Cao,Y., Wang,L., Zeng,L., Ye,X., Wu,Q.,
            Dai,J., Xie,Y. and Mao,Y.
  TITLE     Identification of a novel human DDX40gene, a new member of the
            DEAH-box protein family
  JOURNAL   J Hum Genet 47 (12), 681-683 (2002)
   PUBMED   12522690
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083821.1.
            
            On Oct 23, 2004 this sequence version replaced XP_213429.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..779
                     /product="probable ATP-dependent RNA helicase DHX40"
                     /EC_number="3.6.4.13"
                     /note="DEAH box protein 40; DEAH (Asp-Glu-Ala-His) box
                     polypeptide 40"
                     /calculated_mol_wt=88383
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI69.1)"
     Region          51..>699
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          173..176
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI69.1)"
     CDS             1..779
                     /gene="Dhx40"
                     /coded_by="NM_001005873.1:93..2432"
                     /db_xref="GeneID:287595"
                     /db_xref="RGD:1359618"
ORIGIN      
        1 msrfpavagr aprrqeeger pvelqeerps avriadreek gctsqeggtt ptfpiqkqrk
       61 kliqavrdns flivtgntgs gkttqlpkyl yeagfsqhgm igvtqprkva aisvaqrvae
      121 emkctlgskv gyqvrfddcs sketaikymt dgcllkhilg dpnlnkfsvi ildeahertl
      181 ttdilfgllk klfqdkspnr kehlkvvvms atmelaklsa ffgncpifdi pgrlypvrek
      241 fcnligprdr entayiqaiv kvtmdihlne magdilvflt gqfeieksce llfqmaesvd
      301 ydydvqdttl dgllilpcyg smttdqqrri flppppgirk cvistnisat sltidgiryv
      361 vdggfvkqln hnprlgldil evvpisksea lqrsgragrt asgkcfriys kdfwnqcmpd
      421 hvipeikrts ltsvvltlkc laihdvirfp yldppnerli lealkqlyqc daidrsghvt
      481 rlglsmvefp lpphltcavi raasldcedl llpiaamlsv envfirpvdp eyqkeaeqkh
      541 relaakaggf ndfatlavif eqckssgapa swcqkhwihw rclfsafrve aqlrelirkl
      601 kqqsdfpret fegpkhevlr rclcagyfkn varrsvgrtf ctmdgrgspv hihpssalhe
      661 qetklewiif hevlvttkvy arivcpirye wvrdllpklh elnahdlssv arremrddar
      721 rkwtnkenvk qlkdgiskev lkkmqrrndd ksisdararf lerkqqriqd hsdtlketg
//
LOCUS       NP_478116                626 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 37 [Rattus norvegicus].
ACCESSION   NP_478116 XP_232947
VERSION     NP_478116.2
DBSOURCE    REFSEQ: accession NM_058209.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Vanden Heuvel,J.P., Holden,P., Tugwood,J., Ingle,C., Yen,W.,
            Galjart,N. and Greenlee,W.F.
  TITLE     Identification of a novel peroxisome proliferator responsive cDNA
            isolated from rat hepatocytes as the zinc-finger protein ZFP-37
  JOURNAL   Toxicol Appl Pharmacol 152 (1), 107-118 (1998)
   PUBMED   9772206
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB727538.1 and BC166844.1.
            
            On May 29, 2008 this sequence version replaced NP_478116.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760389
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..626
                     /product="zinc finger protein 37"
                     /note="zfp-37"
                     /calculated_mol_wt=70743
     Region          41..89
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          243..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..>598
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(434,436,438,440..441,444..445,448,462,464,468..469,
                     472..473,476,490,492,494,496..497,500..501,504)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          485..505
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          513..533
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          541..561
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(546,548,550,552..553,556..557,560,574,576,580..581,
                     584..585,588,602,604,606,608..609,612..613,616)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          569..589
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          595..617
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          597..617
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..626
                     /gene="Zfp37"
                     /coded_by="NM_058209.2:1..1881"
                     /db_xref="GeneID:115768"
                     /db_xref="RGD:620723"
ORIGIN      
        1 msasdsnkdl tkpeavgrrs tdkarrpkem atpepaesda keweqlepgq rnvykdtkle
       61 tcsnpasmgn qdpkqglvsk ldgeeerwss vranknssss lhrlkktgts akvqqdgaqt
      121 egkqkfqrkl tsevtfrkks snskkssect llekknvhsk hdpsekrlhk snlygknlnq
      181 nldlpsqiki sakkkpdtan eyrkslshsa sdvnrdeist rkkcdkspnn klfgkgdknq
      241 tgkkcekvcr hsashtkedk ihtgekrksp crspsksdka pgsgkpyecn qcgkvlshkq
      301 glldhqrtht gekpyecnec giafsqkshl vvhqrthtge kpyecvqcgk ahghkhaltd
      361 hlrihtgekp ykcnecgktf rhssnlmqhi rshtgekpye ckecgksfry nssltehvrt
      421 htgeipyecn ecgkafkygs sltkhmriht gekpfectec gktfskkshl vihqrthtke
      481 kpykckecgk afghssslty hlrthtgdcp fecnqcgkaf kqiegltqhq rvhtgekpye
      541 cvecgkafsq kshlivhqrt htgekpfecy ecgkafnaks qlvihqrsht gekpyecvec
      601 gkafkqnasl trhmkihsee qsqeed
//
LOCUS       NP_899154                362 aa            linear   ROD 27-APR-2025
DEFINITION  ADP-ribosylhydrolase ARH1 [Rattus norvegicus].
ACCESSION   NP_899154 XP_340990
VERSION     NP_899154.2
DBSOURCE    REFSEQ: accession NM_183325.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Rack,J.G.M., Ariza,A., Drown,B.S., Henfrey,C., Bartlett,E.,
            Shirai,T., Hergenrother,P.J. and Ahel,I.
  TITLE     (ADP-ribosyl)hydrolases: Structural Basis for Differential
            Substrate Recognition and Inhibition
  JOURNAL   Cell Chem Biol 25 (12), 1533-1546 (2018)
   PUBMED   30472116
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Kato,J., Zhu,J., Liu,C., Stylianou,M., Hoffmann,V., Lizak,M.J.,
            Glasgow,C.G. and Moss,J.
  TITLE     ADP-ribosylarginine hydrolase regulates cell proliferation and
            tumorigenesis
  JOURNAL   Cancer Res 71 (15), 5327-5335 (2011)
   PUBMED   21697277
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Kernstock,S., Koch-Nolte,F., Mueller-Dieckmann,J., Weiss,M.S. and
            Mueller-Dieckmann,C.
  TITLE     Cloning, expression, purification and crystallization as well as
            X-ray fluorescence and preliminary X-ray diffraction analyses of
            human ADP-ribosylhydrolase 1
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 65 (Pt 5), 529-532
            (2009)
   PUBMED   19407395
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Miyaoka,T., Tsuchiya,M., Yamada,K., Badruzzaman,M., Yamamori,C.,
            Ishino,H. and Shimoyama,M.
  TITLE     Immunohistochemical localization of ADP-ribosylarginine hydrolase
            in rodent CNS
  JOURNAL   Brain Res 746 (1-2), 1-9 (1997)
   PUBMED   9037477
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Takada,T., Iida,K. and Moss,J.
  TITLE     Cloning and site-directed mutagenesis of human ADP-ribosylarginine
            hydrolase
  JOURNAL   J Biol Chem 268 (24), 17837-17843 (1993)
   PUBMED   8349667
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Moss,J., Stanley,S.J., Nightingale,M.S., Murtagh,J.J. Jr.,
            Monaco,L., Mishima,K., Chen,H.C., Williamson,K.C. and Tsai,S.C.
  TITLE     Molecular and immunological characterization of ADP-ribosylarginine
            hydrolases
  JOURNAL   J Biol Chem 267 (15), 10481-10488 (1992)
   PUBMED   1375222
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082065.1.
            
            On Sep 16, 2004 this sequence version replaced NP_899154.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082065.1, EV769937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..362
                     /product="ADP-ribosylhydrolase ARH1"
                     /EC_number="3.2.2.19"
                     /note="[Protein ADP-ribosylarginine] hydrolase;
                     ADP-ribose-L-arginine cleaving enzyme"
                     /calculated_mol_wt=39830
     Region          11..328
                     /region_name="ADP_ribosyl_GH"
                     /note="ADP-ribosylglycohydrolase; pfam03747"
                     /db_xref="CDD:461037"
     Region          106..108
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:P54922"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02589.2)"
     Region          168..170
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:P54922"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02589.2)"
     Region          268..270
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:P54922"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02589.2)"
     Region          274..275
                     /region_name="Substrate.
                     /evidence=ECO:0000250|UniProtKB:P54922"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02589.2)"
     CDS             1..362
                     /gene="Adprh"
                     /gene_synonym="ADPRHA"
                     /coded_by="NM_183325.2:146..1234"
                     /db_xref="GeneID:25371"
                     /db_xref="RGD:2052"
ORIGIN      
        1 mggglieryv aamvlsaagd tlgyfngkwe flrdgekihr qlaqmgdlea idvaqwrvsd
       61 dtimhlatae almeagsspd lpqlysllak hyrdcmgdmd grapggacmq namqldpdra
      121 dgwripfnsh eggcgaamra mciglrfphp sqldtliqvs iesgrmthhh ptgylgslas
      181 alftayavng ksprqwgkgl mevlpeakay vtqsgyfvke nlqhwsyfek ewekylelrg
      241 ildgksapvf pkpfgvkerd qfyievsysg wggssghdap miaydallaa gdswkelahr
      301 affhggdsds tatiagcwwg vmhgfkgvnp snyekleyrq rleeagraly slgskedtil
      361 gp
//
LOCUS       NP_062082                367 aa            linear   ROD 27-APR-2025
DEFINITION  uroporphyrinogen decarboxylase [Rattus norvegicus].
ACCESSION   NP_062082 XP_001067008 XP_342888
VERSION     NP_062082.1
DBSOURCE    REFSEQ: accession NM_019209.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Barupala,D.P., Dzul,S.P., Riggs-Gelasco,P.J. and Stemmler,T.L.
  TITLE     Synthesis, delivery and regulation of eukaryotic heme and Fe-S
            cluster cofactors
  JOURNAL   Arch Biochem Biophys 592, 60-75 (2016)
   PUBMED   26785297
  REMARK    Review article
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Sopena,Y.E., Ferramola de Sancovich,A.M. and Sancovich,H.A.
  TITLE     Hexachlorobenzene treatment on hepatic mitochondrial function
            parameters and intracellular coproporphyrinogen oxidase location
  JOURNAL   Int J Toxicol 27 (6), 455-465 (2008)
   PUBMED   19482825
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Cunha,L., Kuti,M., Bishop,D.F., Mezei,M., Zeng,L., Zhou,M.M. and
            Desnick,R.J.
  TITLE     Human uroporphyrinogen III synthase: NMR-based mapping of the
            active site
  JOURNAL   Proteins 71 (2), 855-873 (2008)
   PUBMED   18004775
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Phillips,J.D., Bergonia,H.A., Reilly,C.A., Franklin,M.R. and
            Kushner,J.P.
  TITLE     A porphomethene inhibitor of uroporphyrinogen decarboxylase causes
            porphyria cutanea tarda
  JOURNAL   Proc Natl Acad Sci U S A 104 (12), 5079-5084 (2007)
   PUBMED   17360334
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Ajioka,R.S., Phillips,J.D. and Kushner,J.P.
  TITLE     Biosynthesis of heme in mammals
  JOURNAL   Biochim Biophys Acta 1763 (7), 723-736 (2006)
   PUBMED   16839620
  REMARK    Review article
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Navone,N.M., Polo,C.F., Frisardi,A.L., Andrade,N.E. and Battle,A.M.
  TITLE     Heme biosynthesis in human breast cancer--mimetic 'in vitro'
            studies and some heme enzymic activity levels
  JOURNAL   Int J Biochem 22 (12), 1407-1411 (1990)
   PUBMED   2276414
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Garey,J.R., Hansen,J.L., Harrison,L.M., Kennedy,J.B. and
            Kushner,J.P.
  TITLE     A point mutation in the coding region of uroporphyrinogen
            decarboxylase associated with familial porphyria cutanea tarda
  JOURNAL   Blood 73 (4), 892-895 (1989)
   PUBMED   2920211
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Blekkenhorst,G.H., Eales,L. and Pimstone,N.R.
  TITLE     Activation of uroporphyrinogen decarboxylase by ferrous iron in
            porphyria cutanea tarda
  JOURNAL   S Afr Med J 56 (22), 918-920 (1979)
   PUBMED   515872
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Elder,G.H., Lee,G.B. and Tovey,J.A.
  TITLE     Decreased activity of hepatic uroporphyrinogen decarboxylase in
            sporadic porphyria cutanea tarda
  JOURNAL   N Engl J Med 299 (6), 274-278 (1978)
   PUBMED   661926
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Louw,M., Neethling,A.C., Percy,V.A., Carstens,M. and Shanley,B.C.
  TITLE     Effects of hexachlorobenzene feeding and iron overload on enzymes
            of haem biosynthesis and cytochrome P 450 in rat liver
  JOURNAL   Clin Sci Mol Med 53 (2), 111-115 (1977)
   PUBMED   891100
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY314066.1, EV767503.1, BI282626.1 and BF414694.1.
            
            On or before Oct 28, 2007 this sequence version replaced
            XP_342888.2, XP_001067008.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158690.1, FQ234620.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..367
                     /product="uroporphyrinogen decarboxylase"
                     /EC_number="4.1.1.37"
                     /note="UPD; URO-D; uroporphyrinogen III decarboxylase;
                     porphyrinogen carboxylase"
                     /calculated_mol_wt=40452
     Region          20..359
                     /region_name="URO-D"
                     /note="Uroporphyrinogen decarboxylase (URO-D) is a dimeric
                     cytosolic enzyme that decarboxylates the four acetate side
                     chains of uroporphyrinogen III (uro-III) to create
                     coproporphyrinogen III, without requiring any prosthetic
                     groups or cofactors. This reaction...; cd00717"
                     /db_xref="CDD:238368"
     Site            order(36..41,46,50,55,82..88,100,105,154,164,170,217,
                     219..220,261,339)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238368"
     Site            order(37,41,86,164,219,339)
                     /site_type="active"
                     /db_xref="CDD:238368"
     CDS             1..367
                     /gene="Urod"
                     /gene_synonym="porphyrinogen carboxy-lyase"
                     /coded_by="NM_019209.1:38..1141"
                     /db_xref="GeneID:29421"
                     /db_xref="RGD:3946"
ORIGIN      
        1 meanglglqn fpelkndtfl raawgeetdy tpvwcmrqag rylpefretr aaqdffstcr
       61 speacceltl qplrrfplda aiifsdilvv pqalgmevtm vpgkgpsfpe plreerdler
      121 lrdpaavase lgyvfqaitl trqqlagrvp ligfagapwt lmtymveggs sstmaqakrw
      181 lyqkplashk llgiltdalv pyligqvaag aqalqlfesh aghlgselfs kfalpyirdv
      241 akrvkaglqk aglapvpmii fakdghfale elaqagyevv gldwtvapkk arervgktvt
      301 lqgnldpcal yaseeeigrl vqqmlndfgp qryianlghg lypdmdpehv gafvdavhkh
      361 srllrqn
//
LOCUS       NP_001100139             504 aa            linear   ROD 27-APR-2025
DEFINITION  metalloendopeptidase OMA1, mitochondrial [Rattus norvegicus].
ACCESSION   NP_001100139 XP_001063646 XP_216446
VERSION     NP_001100139.1
DBSOURCE    REFSEQ: accession NM_001106669.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Garcia,I., Calderon,F., la Torre,P., Vallier,S.S., Rodriguez,C.,
            Agarwala,D., Keniry,M., Innis-Whitehouse,W. and Gilkerson,R.
  TITLE     Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts
  JOURNAL   Mitochondrion 57, 88-96 (2021)
   PUBMED   33383158
  REMARK    GeneRIF: Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Murata,D., Yamada,T., Tokuyama,T., Arai,K., Quiros,P.M.,
            Lopez-Otin,C., Iijima,M. and Sesaki,H.
  TITLE     Mitochondrial Safeguard: a stress response that offsets extreme
            fusion and protects respiratory function via flickering-induced
            Oma1 activation
  JOURNAL   EMBO J 39 (24), e105074 (2020)
   PUBMED   33200421
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Desmurs,M., Foti,M., Raemy,E., Vaz,F.M., Martinou,J.C., Bairoch,A.
            and Lane,L.
  TITLE     C11orf83, a mitochondrial cardiolipin-binding protein involved in
            bc1 complex assembly and supercomplex stabilization
  JOURNAL   Mol Cell Biol 35 (7), 1139-1156 (2015)
   PUBMED   25605331
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Quiros,P.M., Ramsay,A.J., Sala,D., Fernandez-Vizarra,E.,
            Rodriguez,F., Peinado,J.R., Fernandez-Garcia,M.S., Vega,J.A.,
            Enriquez,J.A., Zorzano,A. and Lopez-Otin,C.
  TITLE     Loss of mitochondrial protease OMA1 alters processing of the GTPase
            OPA1 and causes obesity and defective thermogenesis in mice
  JOURNAL   EMBO J 31 (9), 2117-2133 (2012)
   PUBMED   22433842
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Ehses,S., Raschke,I., Mancuso,G., Bernacchia,A., Geimer,S.,
            Tondera,D., Martinou,J.C., Westermann,B., Rugarli,E.I. and
            Langer,T.
  TITLE     Regulation of OPA1 processing and mitochondrial fusion by m-AAA
            protease isoenzymes and OMA1
  JOURNAL   J Cell Biol 187 (7), 1023-1036 (2009)
   PUBMED   20038678
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Head,B., Griparic,L., Amiri,M., Gandre-Babbe,S. and van der
            Bliek,A.M.
  TITLE     Inducible proteolytic inactivation of OPA1 mediated by the OMA1
            protease in mammalian cells
  JOURNAL   J Cell Biol 187 (7), 959-966 (2009)
   PUBMED   20038677
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473998.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_216446.3, XP_001063646.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760384,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..504
                     /product="metalloendopeptidase OMA1, mitochondrial"
                     /note="overlapping with the m-AAA protease 1 homolog; OMA1
                     homolog, zinc metallopeptidase; zinc metallopeptidase
                     homolog"
                     /calculated_mol_wt=52600
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (D3ZS74.1)"
                     /calculated_mol_wt=4563
     Region          127..146
                     /region_name="Cardiolipin-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9D8H7"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZS74.1)"
     Region          144..174
                     /region_name="Stress-sensor region.
                     /evidence=ECO:0000250|UniProtKB:Q9D8H7"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZS74.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZS74.1)"
     Region          242..435
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(306..307,310,371,375,418)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(306,310,371,418)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
     CDS             1..504
                     /gene="Oma1"
                     /gene_synonym="RGD1304821"
                     /coded_by="NM_001106669.1:79..1593"
                     /db_xref="GeneID:298282"
                     /db_xref="RGD:1304821"
ORIGIN      
        1 mnflyglqsa trnqflsgvn tlarrrtwtp pagcplasrl pavnanwgls tvshcysvil
       61 lprnlhfcrt lknkrsrcls saqskemgvl tynwtvwgda scspnyaair evrsfhtsap
      121 rqaapvpllm lilkpvqkll aiivgrgirk wwqalppdkk alfkdsvkrn kwrlllglsa
      181 fgllfvvfyf thlevspvtg rsklllvgke hfrllsdley evwmeefknd llpeedpryl
      241 tvkkvvyhlt qcnqdvpgvs einwvvhvvh spkvnafvlp ngqvfvftgl lnsvtdmhql
      301 sfllgheiah avlghaaeka slvhlldflg mifltmiwai cprdslavlg qwiqsklqey
      361 mfdrpysrtl eaeadkiglq laakacvdvr assvfwqqme fseslhgypk lpewlsthps
      421 hgnraeyldr lipqalklre vcncpplsgp dprllfrltv khlledseke dlnitvkkqk
      481 pdalpiqkqe qipltyalgk rtag
//
LOCUS       NP_001019498             594 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 467 [Rattus norvegicus].
ACCESSION   NP_001019498 XP_575461
VERSION     NP_001019498.1
DBSOURCE    REFSEQ: accession NM_001024327.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Nakayama,K., Kim,K.W. and Miyajima,A.
  TITLE     A novel nuclear zinc finger protein EZI enhances nuclear retention
            and transactivation of STAT3
  JOURNAL   EMBO J 21 (22), 6174-6184 (2002)
   PUBMED   12426389
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086534.1.
            
            On May 27, 2005 this sequence version replaced XP_575461.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086534.1, CK364973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..594
                     /product="zinc finger protein 467"
                     /calculated_mol_wt=65622
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RJR4.1)"
     Region          162..182
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          190..564
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          190..210
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          218..238
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(223,225,227,229..230,233..234,237,251,253,257..258,
                     261..262,265,279,281,283,285..286,289..290,293)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          246..266
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          274..294
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          302..322
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          313..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RJR4.1)"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          432..452
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          460..480
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          488..508
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(493,495,497,499..500,503..504,507,521,523,527..528,
                     531..532,535,549,551,553,555..556,559..560,563)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          516..536
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          544..564
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..594
                     /gene="Zfp467"
                     /gene_synonym="Znf467"
                     /coded_by="NM_001024327.1:84..1868"
                     /db_xref="GeneID:500110"
                     /db_xref="RGD:1561603"
ORIGIN      
        1 mretlealns lgfsvgqpem apqseprdgf snpqekmssr destlhscsg petpgqkegi
       61 hteqaeapcm gsqacipqka epassvpgee wmirkvkved edqeaeeeve wpqhlsflps
      121 pfptpdlgql avayklepgt pgtlggials gwapipekpy gceecerrfr dqltlrlhqr
      181 lhrgegpcac pdcgrsftqr ahmllhqrsh rgerpfpcse cdkrfskkah ltrhlrthtg
      241 erpypcaecg krfsqkihlg shqkthtger pfpctecekr frkkthlirh qrihtgerpy
      301 qctqctrsft hkqhlvrhqr vhdaasrtrs spdipatphp ptaslapspt gpkpfacshc
      361 gqsfgwkknl athqslhlte grpfgcdeca lgtnvdpaae psactphapd cgpgsgpvap
      421 qrttssersf fcpdcgrgfa hgqhlarhrr vhtgerpfac aqcgrrfgsr pnlvahsrah
      481 sgarpfacaq cgrrfsrksh lgrhqavhtg srphacavca rcfssktnlv rhqaihtgsr
      541 pfscpqcaks fsrkthlvrh qrihgeaalp asasnlsapa wsnpsevvpp piff
//
LOCUS       NP_714946                199 aa            linear   ROD 27-APR-2025
DEFINITION  calcipressin-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_714946
VERSION     NP_714946.2
DBSOURCE    REFSEQ: accession NM_153724.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Gong,M., Tao,L. and Li,X.
  TITLE     MicroRNA-21-3p/Rcan1 signaling axis affects apoptosis of
            cardiomyocytes of sepsis rats
  JOURNAL   Gen Physiol Biophys 42 (3), 217-227 (2023)
   PUBMED   37098739
  REMARK    GeneRIF: MicroRNA-21-3p/Rcan1 signaling axis affects apoptosis of
            cardiomyocytes of sepsis rats.
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Huang,B., He,Y., Li,S., Wei,X., Liu,J., Shan,Z., Huang,Y., Chen,J.
            and Zhao,F.
  TITLE     The RCAN1.4-calcineurin/NFAT signaling pathway is essential for
            hypoxic adaption of intervertebral discs
  JOURNAL   Exp Mol Med 52 (5), 865-875 (2020)
   PUBMED   32467610
  REMARK    GeneRIF: The RCAN1.4-calcineurin/NFAT signaling pathway is
            essential for hypoxic adaption of intervertebral discs.
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Wang,G., Zhao,Y., Liu,S., Jia,J. and Lu,T.
  TITLE     Critical role of regulator of calcineurin 1 in spinal cord injury
  JOURNAL   J Physiol Biochem 72 (4), 605-613 (2016)
   PUBMED   27339639
  REMARK    GeneRIF: RCAN1 plays a critical role in spinal cord injury.
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Redina,O.E., Smolenskaya,S.E., Fedoseeva,L.A. and Markel,A.L.
  TITLE     [Differentially expressed genes in the locus associated with
            relative kidney weight and resting blood pressure in hypertensive
            rats of the ISIAH strain]
  JOURNAL   Mol Biol (Mosk) 50 (6), 944-952 (2016)
   PUBMED   28064310
  REMARK    GeneRIF: Six differentially expressed genes (Kcne1, Rcan1, Mx1,
            Mx2, Tmprss2, and RGD1559516) were identified in the renal cortex,
            and three genes (Rcan1, Mx2, and Tmprss2) were identified in the
            renal medulla.
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Emrani,R., Rebillard,A., Lefeuvre,L., Gratas-Delamarche,A.,
            Davies,K.J. and Cillard,J.
  TITLE     The calcineurin antagonist RCAN1-4 is induced by exhaustive
            exercise in rat skeletal muscle
  JOURNAL   Free Radic Biol Med 87, 290-299 (2015)
   PUBMED   26122706
  REMARK    GeneRIF: We propose that increased RCAN1-4 expression and the
            signal transduction pathways it regulates represent important
            components of the physiological adaptation to exercise-induced
            oxidative stress.
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Bush,E., Fielitz,J., Melvin,L., Martinez-Arnold,M., McKinsey,T.A.,
            Plichta,R. and Olson,E.N.
  TITLE     A small molecular activator of cardiac hypertrophy uncovered in a
            chemical screen for modifiers of the calcineurin signaling pathway
  JOURNAL   Proc Natl Acad Sci U S A 101 (9), 2870-2875 (2004)
   PUBMED   14976250
  REMARK    GeneRIF: In the heart MCIP1 gene is activated by calcineurin and
            has been proposed to fulfill a negative feedback loop that
            restrains potentially pathological calcineurin signaling
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Genesca,L., Aubareda,A., Fuentes,J.J., Estivill,X., De La Luna,S.
            and Perez-Riba,M.
  TITLE     Phosphorylation of calcipressin 1 increases its ability to inhibit
            calcineurin and decreases calcipressin half-life
  JOURNAL   Biochem J 374 (Pt 2), 567-575 (2003)
   PUBMED   12809556
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Wang,Y., De Keulenaer,G.W., Weinberg,E.O., Muangman,S.,
            Gualberto,A., Landschulz,K.T., Turi,T.G., Thompson,J.F. and
            Lee,R.T.
  TITLE     Direct biomechanical induction of endogenous calcineurin inhibitor
            Down Syndrome Critical Region-1 in cardiac myocytes
  JOURNAL   Am J Physiol Heart Circ Physiol 283 (2), H533-H539 (2002)
   PUBMED   12124198
REFERENCE   9  (residues 1 to 199)
  AUTHORS   Ermak,G., Morgan,T.E. and Davies,K.J.
  TITLE     Chronic overexpression of the calcineurin inhibitory gene DSCR1
            (Adapt78) is associated with Alzheimer's disease
  JOURNAL   J Biol Chem 276 (42), 38787-38794 (2001)
   PUBMED   11483593
REFERENCE   10 (residues 1 to 199)
  AUTHORS   Rothermel,B., Vega,R.B., Yang,J., Wu,H., Bassel-Duby,R. and
            Williams,R.S.
  TITLE     A protein encoded within the Down syndrome critical region is
            enriched in striated muscles and inhibits calcineurin signaling
  JOURNAL   J Biol Chem 275 (12), 8719-8725 (2000)
   PUBMED   10722714
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072478.1.
            
            On Jun 13, 2004 this sequence version replaced NP_714946.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072478.1, EX488565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMEA5756307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..199
                     /product="calcipressin-1 isoform 2"
                     /note="calcipressin-1; down syndrome critical region
                     protein 1 homolog; myocyte-enriched
                     calcineurin-interacting protein 1; Down syndrome critical
                     region homolog 1; Down syndrome critical region gene 1"
                     /calculated_mol_wt=22817
     Region          22..192
                     /region_name="Calcipressin"
                     /note="pfam04847"
                     /db_xref="CDD:282674"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53805; propagated from
                     UniProtKB/Swiss-Prot (Q6IN33.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53805; propagated from
                     UniProtKB/Swiss-Prot (Q6IN33.1)"
     Region          162..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN33.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHG6; propagated from
                     UniProtKB/Swiss-Prot (Q6IN33.1)"
     CDS             1..199
                     /gene="Rcan1"
                     /gene_synonym="Dscr1; Mcip1"
                     /coded_by="NM_153724.2:63..662"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:266766"
                     /db_xref="RGD:631338"
ORIGIN      
        1 mhfrdfnynf ssliacvang dvfsesetra kfeslfrtyd kditfqyfks fkrvrinfsn
       61 plsaadarlq lhkteflgke mklyfaqtlh igsshlappn pdkqflispp asppvgwkqv
      121 edatpvinyd llyaisklgp gekyelhaat dttpsvvvhv cesdqeeeee eeeemermkr
      181 pkpkiiqtrr peytpihls
//
LOCUS       NP_001020046             348 aa            linear   ROD 27-APR-2025
DEFINITION  GPALPP motifs-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001020046 XP_216616
VERSION     NP_001020046.1
DBSOURCE    REFSEQ: accession NM_001024875.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097485.1.
            
            On Jun 17, 2005 this sequence version replaced XP_216616.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097485.1, SRR8487227.2322.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..348
                     /product="GPALPP motifs-containing protein 1"
                     /calculated_mol_wt=39043
     Region          1..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8IXQ4; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          7..12
                     /region_name="GPALPP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IXQ4; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          32..37
                     /region_name="GPALPP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          93..98
                     /region_name="GPALPP motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          113..118
                     /region_name="GPALPP motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          177..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V893.1)"
     Region          204..340
                     /region_name="DUF3752"
                     /note="Protein of unknown function (DUF3752); pfam12572"
                     /db_xref="CDD:463632"
     CDS             1..348
                     /gene="Gpalpp1"
                     /gene_synonym="RGD1307254"
                     /coded_by="NM_001024875.1:84..1130"
                     /db_xref="GeneID:298712"
                     /db_xref="RGD:1307254"
ORIGIN      
        1 mardligpal ppgfkeratv edqerdpspv agpalppnyr ssssdssdsn edssslseeg
       61 nqeseeddag ptakkqrrnq drdddddddg ffgpalppgf kkqddspprp iigpalppgf
      121 ikspqkndkg renpgqvspf fnseeaesge dedivgpmpa kgpvdysvta efekraqrmk
      181 ekltkgddds pkpvtreswm telppemkdf glgprtfkrr addksgdrsv wtdtpadrer
      241 kakeiqeark slskkdeenm lsgrdkrlae qvssyneskr seslmdihhk rlktkaaedk
      301 nrhqertpfd rdkdlkvnrf deaqkkalik ksrelntrfs hgkgnmfl
//
LOCUS       NP_001101510             597 aa            linear   ROD 27-APR-2025
DEFINITION  ribosomal oxygenase 1 [Rattus norvegicus].
ACCESSION   NP_001101510 XP_001057487 XP_234396
VERSION     NP_001101510.1
DBSOURCE    REFSEQ: accession NM_001108040.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Sinha,K.M., Yasuda,H., Coombes,M.M., Dent,S.Y. and de
            Crombrugghe,B.
  TITLE     Regulation of the osteoblast-specific transcription factor Osterix
            by NO66, a Jumonji family histone demethylase
  JOURNAL   EMBO J 29 (1), 68-79 (2010)
   PUBMED   19927124
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Eilbracht,J., Reichenzeller,M., Hergt,M., Schnolzer,M., Heid,H.,
            Stohr,M., Franke,W.W. and Schmidt-Zachmann,M.S.
  TITLE     NO66, a highly conserved dual location protein in the nucleolus and
            in a special type of synchronously replicating chromatin
  JOURNAL   Mol Biol Cell 15 (4), 1816-1832 (2004)
   PUBMED   14742713
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473982.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234396.1, XP_001057487.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..597
                     /product="ribosomal oxygenase 1"
                     /EC_number="1.14.11.27"
                     /EC_number="1.14.11.79"
                     /note="nucleolar protein 66; myc-associated protein with
                     JmjC domain; lysine-specific demethylase NO66; histone
                     lysine demethylase NO66; bifunctional lysine-specific
                     demethylase and histidyl-hydroxylase NO66"
                     /calculated_mol_wt=67324
     Region          1..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU57.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6W3; propagated from
                     UniProtKB/Swiss-Prot (D3ZU57.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZU57.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZU57.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6W3; propagated from
                     UniProtKB/Swiss-Prot (D3ZU57.1)"
     Region          253..380
                     /region_name="JmjC_2"
                     /note="JmjC domain; pfam08007"
                     /db_xref="CDD:462340"
     CDS             1..597
                     /gene="Riox1"
                     /gene_synonym="No66; RGD1307704"
                     /coded_by="NM_001108040.1:431..2224"
                     /db_xref="GeneID:314300"
                     /db_xref="RGD:1307704"
ORIGIN      
        1 mdelpngnga aplkrgrgrr rrqpqprgas vlalplrprk vrrhrksaas rvaalraral
       61 lsedsdsnve svrgkrerpa elpeasrsae prpvpvrprp asatlprrve graalsrnlg
      121 kpaplpgshv ddperpwdsp lqqvlaelng ipssrrraar lfewllaplp pdhfyrrlwe
      181 reavlvrrqd hsyyeglfst sdldwmlrye dvhfgqhlda aryidgrret lnppgralpa
      241 aawslyqagc slrllcpqaf sptvwqflav lqeqfgsmag snvyltppns qgfaphyddi
      301 eafvlqlegr klwrvyrprd pseelaltss pnfsqedlge pvlqtvlepg dllyfprgfi
      361 hqaecqdgvh slhltlstyq rntwgdflea vlplamqaai eenvefrrgl prdfmdymga
      421 qhsdskdprr tafmekvrvl varlghfapv davadqrakd fihdslppvl tdreralsvh
      481 glpirweage pvnvgaqltt etqvhmlqdg iarlvgeggr lflyytvens rvyhleepkc
      541 leiypqqada melllrsype fvrvgdlpcd svedqlslat mlydkglllt ktplvls
//
LOCUS       NP_062011                507 aa            linear   ROD 27-APR-2025
DEFINITION  25-hydroxycholesterol 7-alpha-hydroxylase [Rattus norvegicus].
ACCESSION   NP_062011 XP_001060253 XP_342219
VERSION     NP_062011.1
DBSOURCE    REFSEQ: accession NM_019138.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Wicher,G. and Norlin,M.
  TITLE     Estrogen-mediated regulation of steroid metabolism in rat glial
            cells; effects on neurosteroid levels via regulation of
            CYP7B1-mediated catalysis
  JOURNAL   J Steroid Biochem Mol Biol 145, 21-27 (2015)
   PUBMED   25263657
  REMARK    GeneRIF: estrogen suppresses CYP7B1-catalyzed 7alpha-hydroxylation
            of DEHA
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Yi,T., Wang,X., Kelly,L.M., An,J., Xu,Y., Sailer,A.W.,
            Gustafsson,J.A., Russell,D.W. and Cyster,J.G.
  TITLE     Oxysterol gradient generation by lymphoid stromal cells guides
            activated B cell movement during humoral responses
  JOURNAL   Immunity 37 (3), 535-548 (2012)
   PUBMED   22999953
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Noreau,A., Dion,P.A., Szuto,A., Levert,A., Thibodeau,P., Brais,B.,
            Dupre,N., Rioux,M.F. and Rouleau,G.A.
  TITLE     CYP7B1 mutations in French-Canadian hereditary spastic paraplegia
            subjects
  JOURNAL   Can J Neurol Sci 39 (1), 91-94 (2012)
   PUBMED   22384504
  REMARK    GeneRIF: This study deminitrated that CYP7B1 mutations in patients
            with hereditary spastic paraplegia in French-Canadian.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Shi,Q.Y., Lin,Y.G., Zhou,X., Lin,Y.Q. and Yan,S.
  TITLE     [Interaction among peroxisome proliferators-activated receptor
            alpha, cytochrome P450 oxysterol 7alpha-hydroxylase and estrogen
            receptor and its association with intrahepatic cholestasis in
            pregnant rats]
  JOURNAL   Zhonghua Fu Chan Ke Za Zhi 45 (6), 440-444 (2010)
   PUBMED   21029595
  REMARK    GeneRIF: Abnormal expression of PPARalpha, CYP7B1 and ER may play a
            role in the pathogenesis of estrogen-induced intrahepatic
            cholestasis.
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Galman,C., Bonde,Y., Matasconi,M., Angelin,B. and Rudling,M.
  TITLE     Dramatically increased intestinal absorption of cholesterol
            following hypophysectomy is normalized by thyroid hormone
  JOURNAL   Gastroenterology 134 (4), 1127-1136 (2008)
   PUBMED   18395092
  REMARK    GeneRIF: Hepatic secretion of cholesterol and ABCG5/G8 expression
            are strongly stimulated in hypophysectomized rats during treatment
            with thyroid hormone.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Weihua,Z., Lathe,R., Warner,M. and Gustafsson,J.A.
  TITLE     An endocrine pathway in the prostate, ERbeta, AR,
            5alpha-androstane-3beta,17beta-diol, and CYP7B1, regulates prostate
            growth
  JOURNAL   Proc Natl Acad Sci U S A 99 (21), 13589-13594 (2002)
   PUBMED   12370428
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2006 May 23;103(21):8298]
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Pandak,W.M., Hylemon,P.B., Ren,S., Marques,D., Gil,G., Redford,K.,
            Mallonee,D. and Vlahcevic,Z.R.
  TITLE     Regulation of oxysterol 7alpha-hydroxylase (CYP7B1) in primary
            cultures of rat hepatocytes
  JOURNAL   Hepatology 35 (6), 1400-1408 (2002)
   PUBMED   12029625
  REMARK    GeneRIF: CYP7B1 specific activity is highly regulated but does not
            seem to be rate limiting for bile acid synthesis.
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Laes,J.F., Ravoet,M., Quan,X., Van Vooren,P., Szpirer,J. and
            Szpirer,C.
  TITLE     Improved radiation hybrid map of rat chromosome 2: colocalization
            of the genes encoding corticotropin-releasing hormone and
            IL6-receptor with quantitative trait loci regulating the
            inflammatory response
  JOURNAL   Cytogenet Cell Genet 92 (1-2), 130-133 (2001)
   PUBMED   11306811
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Li-Hawkins,J., Lund,E.G., Bronson,A.D. and Russell,D.W.
  TITLE     Expression cloning of an oxysterol 7alpha-hydroxylase selective for
            24-hydroxycholesterol
  JOURNAL   J Biol Chem 275 (22), 16543-16549 (2000)
   PUBMED   10748047
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Stapleton,G., Steel,M., Richardson,M., Mason,J.O., Rose,K.A.,
            Morris,R.G. and Lathe,R.
  TITLE     A novel cytochrome P450 expressed primarily in brain
  JOURNAL   J Biol Chem 270 (50), 29739-29745 (1995)
   PUBMED   8530364
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB800565.1, CB760136.1, U36992.1, BF283070.1 and CB749347.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_001060253.1, XP_342219.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5756307,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /strain="LE"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..507
                     /product="25-hydroxycholesterol 7-alpha-hydroxylase"
                     /EC_number="1.14.14.29"
                     /note="HCT-1; cytochrome P450 7B1; oxysterol
                     7-alpha-hydroxylase; hippocampal transcript 1 protein;
                     cytochrome P450, subfamily 7B, polypeptide 1; cytochrome
                     P450, family 7, subfamily b, polypeptide 1"
                     /calculated_mol_wt=58441
     Region          67..500
                     /region_name="cytochrome_P450"
                     /note="cytochrome P450 (CYP) superfamily; cl41757"
                     /db_xref="CDD:477761"
     Site            order(132,136,143,190,286..287,290..291,294..295,298,358,
                     366,368,395,439..441,445..449,452..453)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410651"
     Site            order(217..218,286,289..290,294,364..367)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410651"
     CDS             1..507
                     /gene="Cyp7b1"
                     /coded_by="NM_019138.1:119..1642"
                     /db_xref="GeneID:25429"
                     /db_xref="RGD:2483"
ORIGIN      
        1 megattpdaa spgplsllgl lfavtlllpv lflltrrtrr pcepplikgw ipylgmalkf
       61 wkdplaflqt lqrqcgdtft vllggkyitf vlnpfqyqyv mknpkqlsfe kfsrrlsaka
      121 fsvkklltnd dlsndihrgy lllqgksldg lletmiqevk eifesrllkl tdwntarvfd
      181 fcsslvfeit fttiygkila ankkqiisel rddflkfddh fpylvsdipi qllrnaefmq
      241 kkiikcltpe kvaqmqrrse ivqerqemlk kyygheefei gahhlgllwa slantipamf
      301 wamyyllqhp eamevlrdei dsflqstgqk kgpgisvhft reqldslvcl esailevlrl
      361 csyssiirev qedmdfsses rsyrlrkgdf vavfppmihn dpevfdapkd frfdrfvedg
      421 kkkttffkgg kklksyiipf glgtskcpgr yfainemkll viilltyfdl evidtkpigl
      481 nhsrmflgiq hpdsdisfry kakswrs
//
LOCUS       NP_445847                 85 aa            linear   ROD 27-APR-2025
DEFINITION  small muscular protein [Rattus norvegicus].
ACCESSION   NP_445847
VERSION     NP_445847.1
DBSOURCE    REFSEQ: accession NM_053395.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Palmer,S., Groves,N., Schindeler,A., Yeoh,T., Biben,C., Wang,C.C.,
            Sparrow,D.B., Barnett,L., Jenkins,N.A., Copeland,N.G., Koentgen,F.,
            Mohun,T. and Harvey,R.P.
  TITLE     The small muscle-specific protein Csl modifies cell shape and
            promotes myocyte fusion in an insulin-like growth factor
            1-dependent manner
  JOURNAL   J Cell Biol 153 (5), 985-998 (2001)
   PUBMED   11381084
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Kemp,T.J., Sadusky,T.J., Simon,M., Brown,R., Eastwood,M.,
            Sassoon,D.A. and Coulton,G.R.
  TITLE     Identification of a novel stretch-responsive skeletal muscle gene
            (Smpx)
  JOURNAL   Genomics 72 (3), 260-271 (2001)
   PUBMED   11401441
  REMARK    Erratum:[Genomics 2001 Jun 1;74(2):251]
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Patzak,D., Zhuchenko,O., Lee,C.C. and Wehnert,M.
  TITLE     Identification, mapping, and genomic structure of a novel
            X-chromosomal human gene (SMPX) encoding a small muscular protein
  JOURNAL   Hum Genet 105 (5), 506-512 (1999)
   PUBMED   10598820
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF364071.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF364071.1, CK358795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..85
                     /product="small muscular protein"
                     /note="stretch-responsive skeletal muscle protein"
                     /calculated_mol_wt=8989
     Region          1..84
                     /region_name="Chisel"
                     /note="Stretch-responsive small skeletal muscle X protein,
                     Chisel; pfam15355"
                     /db_xref="CDD:405939"
     Region          19..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925F0.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925F0.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925F0.1)"
     CDS             1..85
                     /gene="Smpx"
                     /coded_by="NM_053395.1:190..447"
                     /db_xref="GeneID:84416"
                     /db_xref="RGD:69233"
ORIGIN      
        1 mskqpisnvr siqaninipm gafrpgagqp prrkestpgt aegapatpee kkpvpgmkkf
       61 pgpvvnlsei qnvkselkyv pkgeq
//
LOCUS       NP_037081                434 aa            linear   ROD 27-APR-2025
DEFINITION  beta-enolase [Rattus norvegicus].
ACCESSION   NP_037081
VERSION     NP_037081.2
DBSOURCE    REFSEQ: accession NM_012949.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Obermajer,N., Doljak,B., Jamnik,P., Fonovic,U.P. and Kos,J.
  TITLE     Cathepsin X cleaves the C-terminal dipeptide of alpha- and
            gamma-enolase and impairs survival and neuritogenesis of neuronal
            cells
  JOURNAL   Int J Biochem Cell Biol 41 (8-9), 1685-1696 (2009)
   PUBMED   19433310
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Seweryn,E., Bednarz-Misa,I.S., Danielewicz,R., Saczko,J.,
            Kulbacka,J., Dawiskiba,T. and Pietkiewicz,J.
  TITLE     Distribution of beta-enolase in normal and tumor rat cells
  JOURNAL   Folia Histochem Cytobiol 46 (4), 519-524 (2008)
   PUBMED   19141407
  REMARK    GeneRIF: The cellular localization of the muscle-specific isoform
            of the enolase in normal rat cardiomyocytes (H9c2, an embryonic rat
            heart-derived cell line) and a rat sarcoma (R1) cell line is
            reported here.
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Sun,H., Liu,J., Ding,F., Wang,X., Liu,M. and Gu,X.
  TITLE     Investigation of differentially expressed proteins in rat
            gastrocnemius muscle during denervation-reinnervation
  JOURNAL   J Muscle Res Cell Motil 27 (3-4), 241-250 (2006)
   PUBMED   16752196
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Keller,A., Rouzeau,J.D., Farhadian,F., Wisnewsky,C., Marotte,F.,
            Lamande,N., Samuel,J.L., Schwartz,K., Lazar,M. and Lucas,M.
  TITLE     Differential expression of alpha- and beta-enolase genes during rat
            heart development and hypertrophy
  JOURNAL   Am J Physiol 269 (6 Pt 2), H1843-H1851 (1995)
   PUBMED   8594891
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Sakimura,K., Kushiya,E., Ohshima-Ichimura,Y., Mitsui,H. and
            Takahashi,Y.
  TITLE     Structure and expression of rat muscle-specific enolase gene
  JOURNAL   FEBS Lett 277 (1-2), 78-82 (1990)
   PUBMED   2269373
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Ohshima,Y., Mitsui,H., Takayama,Y., Kushiya,E., Sakimura,K. and
            Takahashi,Y.
  TITLE     cDNA cloning and nucleotide sequence of rat muscle-specific enolase
            (beta beta enolase)
  JOURNAL   FEBS Lett 242 (2), 425-430 (1989)
   PUBMED   2914621
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Kato,K., Shimizu,A., Semba,R. and Satoh,T.
  TITLE     Tissue distribution, developmental profiles and effect of
            denervation of enolase isozymes in rat muscles
  JOURNAL   Biochim Biophys Acta 841 (1), 50-58 (1985)
   PUBMED   3893549
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY321069.1 and BC083566.1.
            
            On Mar 8, 2007 this sequence version replaced NP_037081.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215526.1, Y00979.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..434
                     /product="beta-enolase"
                     /EC_number="4.2.1.11"
                     /note="muscle-specific enolase; skeletal muscle enolase;
                     2-phospho-D-glycerate hydro-lyase; Muscle specific enolase
                     (beta beta enolose) (two splicing products); enolase 3,
                     beta, muscle"
                     /calculated_mol_wt=46883
     Region          2..431
                     /region_name="PLN00191"
                     /note="enolase"
                     /db_xref="CDD:215095"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P13929; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13929; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15429.3)"
     CDS             1..434
                     /gene="Eno3"
                     /gene_synonym="BBE; MSE"
                     /coded_by="NM_012949.2:52..1356"
                     /db_xref="GeneID:25438"
                     /db_xref="RGD:2555"
ORIGIN      
        1 mamqkifare ildsrgnptv evdlhtakgr fraavpsgas tgiyealelr dgdksrylgk
       61 gvlkavehin ktlgpallek klsvvdqekv dkfmieldgt enkskfgana ilgvslavck
      121 agaaekgvpl yrhiadlagn pdlvlpvpaf nvinggshag nklamqefmi lpvgassfke
      181 amrigaevyh hlkgvikaky gkdatnvgde ggfapnilen nealellkta iqaagypdkv
      241 vigmdvaase fyrngkydld fkspddparh isgeklgely ksfiknypvv siedpfdqdd
      301 watwtsflsg vdiqivgddl tvtnpkriaq avekkacncl llkvnqigsv tesiqackla
      361 qsngwgvmvs hrsgetedtf iadlvvglct gqiktgapcr serlakynql mrieealgdk
      421 avfagrkfrn pkak
//
LOCUS       NP_001009255             221 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 9 [Rattus norvegicus].
ACCESSION   NP_001009255 XP_213798
VERSION     NP_001009255.1
DBSOURCE    REFSEQ: accession NM_001009255.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Tariq,A., Garncarz,W., Handl,C., Balik,A., Pusch,O. and
            Jantsch,M.F.
  TITLE     RNA-interacting proteins act as site-specific repressors of
            ADAR2-mediated RNA editing and fluctuate upon neuronal stimulation
  JOURNAL   Nucleic Acids Res 41 (4), 2581-2593 (2013)
   PUBMED   23275536
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Yoshino,H., Enokida,H., Chiyomaru,T., Tatarano,S., Hidaka,H.,
            Yamasaki,T., Gotannda,T., Tachiwada,T., Nohata,N., Yamane,T.,
            Seki,N. and Nakagawa,M.
  TITLE     Tumor suppressive microRNA-1 mediated novel apoptosis pathways
            through direct inhibition of splicing factor serine/arginine-rich 9
            (SRSF9/SRp30c) in bladder cancer
  JOURNAL   Biochem Biophys Res Commun 417 (1), 588-593 (2012)
   PUBMED   22178073
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Wei,Z.S., Hong,M.F., Su,Q.X., Wang,X.H., Yu,Q.Y., Peng,Z.X.,
            Zhang,M.X., Jie,A., Wang,R. and Huang,Y.Q.
  TITLE     Super-high-dose methylprednisolone does not improve efficacy or
            induce glucocorticoid resistance in experimental allergic
            encephalomyelitis
  JOURNAL   Neuroimmunomodulation 18 (1), 28-36 (2011)
   PUBMED   20616573
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Wang,J., Gao,Q.S., Wang,Y., Lafyatis,R., Stamm,S. and Andreadis,A.
  TITLE     Tau exon 10, whose missplicing causes frontotemporal dementia, is
            regulated by an intricate interplay of cis elements and trans
            factors
  JOURNAL   J Neurochem 88 (5), 1078-1090 (2004)
   PUBMED   15009664
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Venables,J.P., Elliott,D.J., Makarova,O.V., Makarov,E.M.,
            Cooke,H.J. and Eperon,I.C.
  TITLE     RBMY, a probable human spermatogenesis factor, and other hnRNP G
            proteins interact with Tra2beta and affect splicing
  JOURNAL   Hum Mol Genet 9 (5), 685-694 (2000)
   PUBMED   10749975
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Nayler,O., Stratling,W., Bourquin,J.P., Stagljar,I., Lindemann,L.,
            Jasper,H., Hartmann,A.M., Fackelmayer,F.O., Ullrich,A. and Stamm,S.
  TITLE     SAF-B protein couples transcription and pre-mRNA splicing to
            SAR/MAR elements
  JOURNAL   Nucleic Acids Res 26 (15), 3542-3549 (1998)
   PUBMED   9671816
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087684.1.
            
            On Jan 7, 2005 this sequence version replaced XP_213798.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087684.1, CO395358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..221
                     /product="serine/arginine-rich splicing factor 9"
                     /note="splicing factor, arginine/serine-rich 9"
                     /calculated_mol_wt=25367
     Region          15..86
                     /region_name="RRM1_SRSF9"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     serine/arginine-rich splicing factor 9 (SRSF9); cd12598"
                     /db_xref="CDD:241042"
     Region          103..186
                     /region_name="RRM2_SRSF9"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     serine/arginine-rich splicing factor 9 (SRSF9); cd12768"
                     /db_xref="CDD:410161"
     Region          187..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Region          188..200
                     /region_name="Interaction with SAFB1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13242; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13242; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13242; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13242; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13242; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PPI1.1)"
     CDS             1..221
                     /gene="Srsf9"
                     /gene_synonym="Sfrs9"
                     /coded_by="NM_001009255.1:64..729"
                     /db_xref="GeneID:288701"
                     /db_xref="RGD:1309495"
ORIGIN      
        1 msgwadergg egdgriyvgn lptdvrekdl edlfykygri reielknrhg lvpfafvrfe
       61 dprdaedaiy grngydygqc rlrvefpray ggrggwpras rngpptrrsd frvlvsglpp
      121 sgswqdlkdh mreagdvcya dvqkdgmgmv eylrkedmey alrklddtkf rshegetsyi
      181 rvypergtsy gcsrsrsgsr grdspyqsrg sphyfspfrp y
//
LOCUS       NP_001020589             601 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A
            beta isoform [Rattus norvegicus].
ACCESSION   NP_001020589 XP_236227
VERSION     NP_001020589.1
DBSOURCE    REFSEQ: accession NM_001025418.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Biesemann,C., Gronborg,M., Luquet,E., Wichert,S.P., Bernard,V.,
            Bungers,S.R., Cooper,B., Varoqueaux,F., Li,L., Byrne,J.A.,
            Urlaub,H., Jahn,O., Brose,N. and Herzog,E.
  TITLE     Proteomic screening of glutamatergic mouse brain synaptosomes
            isolated by fluorescence activated sorting
  JOURNAL   EMBO J 33 (2), 157-170 (2014)
   PUBMED   24413018
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Seshacharyulu,P., Pandey,P., Datta,K. and Batra,S.K.
  TITLE     Phosphatase: PP2A structural importance, regulation and its
            aberrant expression in cancer
  JOURNAL   Cancer Lett 335 (1), 9-18 (2013)
   PUBMED   23454242
  REMARK    Review article
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Guenebeaud,C., Goldschneider,D., Castets,M., Guix,C., Chazot,G.,
            Delloye-Bourgeois,C., Eisenberg-Lerner,A., Shohat,G., Zhang,M.,
            Laudet,V., Kimchi,A., Bernet,A. and Mehlen,P.
  TITLE     The dependence receptor UNC5H2/B triggers apoptosis via
            PP2A-mediated dephosphorylation of DAP kinase
  JOURNAL   Mol Cell 40 (6), 863-876 (2010)
   PUBMED   21172653
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098007.1.
            
            On Jul 15, 2005 this sequence version replaced XP_236227.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098007.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..601
                     /product="serine/threonine-protein phosphatase 2A 65 kDa
                     regulatory subunit A beta isoform"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit A, beta"
                     /calculated_mol_wt=65876
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P30154; propagated from
                     UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          20..58
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          25..49
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          59..96
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          63..90
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          97..135
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          100..130
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          102..239
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          136..173
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          143..165
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          174..212
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          178..206
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          193..364
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          213..251
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          216..246
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          252..290
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          257..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(273..274,277,280..281,312..313,316,319..320,323,
                     355..356,359,362..363,366,394..395,398,401..402,433..434,
                     437,440..441)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          291..333
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          295..323
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          <297..478
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          334..372
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          337..367
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          373..411
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          376..402
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          412..450
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          413..442
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          451..489
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          454..480
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          490..528
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          491..520
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          529..567
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          530..556
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          568..601
                     /region_name="HEAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQT4.1)"
     Region          571..597
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..601
                     /gene="Ppp2r1b"
                     /coded_by="NM_001025418.1:3..1808"
                     /db_xref="GeneID:315648"
                     /db_xref="RGD:1304764"
ORIGIN      
        1 magaagpgtv pgaaggdgdd slypiavlid elrnedvqlr lnsikklsti alalgvertr
       61 tellpfltdt iydedevlla laeqlgnftg lvggpdfahc llppleslat veetvvrdka
      121 veslrqisqe htpvaleahf vplvkrlasg dwftsrtsac glfsvcypra snavkaeirq
      181 hfrslcsddt pmvrraaask lgefakvlel dsvkteivpl ftnlasdeqd svrllaveac
      241 vsiaqllsqd dlealvmptl rqaaedkswr vrymvadkfs elqkavgpki alsdlipafq
      301 sllrdceaev raaaahkvre lcenlptegr etvimnqilp yikelvsdtn qhvksalasv
      361 imglstvlgk entiehllpl flaqlkdecp evrlniisnl dcvnevigir qlsqsllpai
      421 velaedakwr vrlaiieymp llagqlgvef fdeklnslcm awlvdhvyai reaatnnlmk
      481 lvqkfgtewa qntivpkvlv mandpnylhr mttlfcinal seacgkeitt kqmlpivlkm
      541 agdqvanvrf nvakslqkig pildtnalqg evkpvlqklg qdedmdvkyf aqeaisvlal
      601 a
//
LOCUS       NP_775143                190 aa            linear   ROD 27-APR-2025
DEFINITION  selenoprotein S [Rattus norvegicus].
ACCESSION   NP_775143
VERSION     NP_775143.2
DBSOURCE    REFSEQ: accession NM_173120.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Hughes,D.J., Kunicka,T., Schomburg,L., Liska,V., Swan,N. and
            Soucek,P.
  TITLE     Expression of Selenoprotein Genes and Association with Selenium
            Status in Colorectal Adenoma and Colorectal Cancer
  JOURNAL   Nutrients 10 (11), 1812 (2018)
   PUBMED   30469315
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Gladyshev,V.N., Arner,E.S., Berry,M.J., Brigelius-Flohe,R.,
            Bruford,E.A., Burk,R.F., Carlson,B.A., Castellano,S., Chavatte,L.,
            Conrad,M., Copeland,P.R., Diamond,A.M., Driscoll,D.M., Ferreiro,A.,
            Flohe,L., Green,F.R., Guigo,R., Handy,D.E., Hatfield,D.L.,
            Hesketh,J., Hoffmann,P.R., Holmgren,A., Hondal,R.J., Howard,M.T.,
            Huang,K., Kim,H.Y., Kim,I.Y., Kohrle,J., Krol,A., Kryukov,G.V.,
            Lee,B.J., Lee,B.C., Lei,X.G., Liu,Q., Lescure,A., Lobanov,A.V.,
            Loscalzo,J., Maiorino,M., Mariotti,M., Sandeep Prabhu,K.,
            Rayman,M.P., Rozovsky,S., Salinas,G., Schmidt,E.E., Schomburg,L.,
            Schweizer,U., Simonovic,M., Sunde,R.A., Tsuji,P.A., Tweedie,S.,
            Ursini,F., Whanger,P.D. and Zhang,Y.
  TITLE     Selenoprotein Gene Nomenclature
  JOURNAL   J Biol Chem 291 (46), 24036-24040 (2016)
   PUBMED   27645994
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Ye,Y., Fu,F., Li,X., Yang,J. and Liu,H.
  TITLE     Selenoprotein S Is Highly Expressed in the Blood Vessels and
            Prevents Vascular Smooth Muscle Cells From Apoptosis
  JOURNAL   J Cell Biochem 117 (1), 106-117 (2016)
   PUBMED   26058460
  REMARK    GeneRIF: Selenoprotein S Is Highly Expressed in the Blood Vessels
            and Prevents Vascular Smooth Muscle Cells From Apoptosis
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Liu,Y., Soetandyo,N., Lee,J.G., Liu,L., Xu,Y., Clemons,W.M. Jr. and
            Ye,Y.
  TITLE     USP13 antagonizes gp78 to maintain functionality of a chaperone in
            ER-associated degradation
  JOURNAL   Elife 3, e01369 (2014)
   PUBMED   24424410
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Bubenik,J.L., Miniard,A.C. and Driscoll,D.M.
  TITLE     Alternative transcripts and 3'UTR elements govern the incorporation
            of selenocysteine into selenoprotein S
  JOURNAL   PLoS One 8 (4), e62102 (2013)
   PUBMED   23614019
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Curran,J.E., Jowett,J.B., Elliott,K.S., Gao,Y., Gluschenko,K.,
            Wang,J., Abel Azim,D.M., Cai,G., Mahaney,M.C., Comuzzie,A.G.,
            Dyer,T.D., Walder,K.R., Zimmet,P., MacCluer,J.W., Collier,G.R.,
            Kissebah,A.H. and Blangero,J.
  TITLE     Genetic variation in selenoprotein S influences inflammatory
            response
  JOURNAL   Nat Genet 37 (11), 1234-1241 (2005)
   PUBMED   16227999
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Ye,Y., Shibata,Y., Yun,C., Ron,D. and Rapoport,T.A.
  TITLE     A membrane protein complex mediates retro-translocation from the ER
            lumen into the cytosol
  JOURNAL   Nature 429 (6994), 841-847 (2004)
   PUBMED   15215856
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Gao,Y., Feng,H.C., Walder,K., Bolton,K., Sunderland,T., Bishara,N.,
            Quick,M., Kantham,L. and Collier,G.R.
  TITLE     Regulation of the selenoprotein SelS by glucose deprivation and
            endoplasmic reticulum stress - SelS is a novel glucose-regulated
            protein
  JOURNAL   FEBS Lett 563 (1-3), 185-190 (2004)
   PUBMED   15063746
REFERENCE   9  (residues 1 to 190)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
REFERENCE   10 (residues 1 to 190)
  AUTHORS   Walder,K., Kantham,L., McMillan,J.S., Trevaskis,J., Kerr,L., De
            Silva,A., Sunderland,T., Godde,N., Gao,Y., Bishara,N., Windmill,K.,
            Tenne-Brown,J., Augert,G., Zimmet,P.Z. and Collier,G.R.
  TITLE     Tanis: a link between type 2 diabetes and inflammation?
  JOURNAL   Diabetes 51 (6), 1859-1866 (2002)
   PUBMED   12031974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC059111.1 and AF367467.1.
            
            On Aug 2, 2006 this sequence version replaced NP_775143.1.
            
            Summary: This gene encodes a transmembrane protein that is
            localized in the endoplasmic reticulum (ER). It is involved in the
            degradation process of misfolded proteins in the ER, and may also
            have a role in inflammation control. This protein is a
            selenoprotein, containing the rare amino acid selenocysteine (Sec).
            Sec is encoded by the UGA codon, which normally signals translation
            termination. The 3' UTRs of selenoprotein mRNAs contain a conserved
            stem-loop structure, designated the Sec insertion sequence (SECIS)
            element, that is necessary for the recognition of UGA as a Sec
            codon, rather than as a stop signal. Two additional
            phylogenetically conserved stem-loop structures (Stem-loop 1 and
            Stem-loop 2) in the 3' UTR of this mRNA have been shown to function
            as modulators of Sec insertion (PMID:23614019). [provided by
            RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF367467.1, FQ218853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: inferred from conservation
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..190
                     /product="selenoprotein S"
                     /note="Tanis; VCP-interacting membrane protein;
                     VCP-interacting membrane selenoprotein"
                     /calculated_mol_wt=21221
     Region          1..188
                     /region_name="Selenoprotein_S"
                     /note="Selenoprotein S (SelS); pfam06936"
                     /db_xref="CDD:462043"
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHV8.3)"
     Region          78..90
                     /region_name="VCP/p97-interacting motif (VIM).
                     /evidence=ECO:0000250|UniProtKB:Q9BQE4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHV8.3)"
     Region          96..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHV8.3)"
     Site            189
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..190
                     /gene="Selenos"
                     /gene_synonym="Sels; sg2; Vimp"
                     /coded_by="NM_173120.2:29..601"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:286900"
                     /db_xref="RGD:628897"
ORIGIN      
        1 mdrgeeplsa rpaleteslr flhvtvgsll asygwyilfs cvllyiviqk lslrlralrq
       61 rqldqaeavl epdvvvkrqe alaaarlrmq edlnaqvekh keklrqleee krrqkiemwd
      121 smqegrsykr nsgrpqeedg pgpstssvip kgksdkkplr gggynpltge gggtcswrpg
      181 rrgpssggus
//
LOCUS       NP_001037748             162 aa            linear   ROD 27-APR-2025
DEFINITION  sorting nexin-3 [Rattus norvegicus].
ACCESSION   NP_001037748 XP_001068918
VERSION     NP_001037748.1
DBSOURCE    REFSEQ: accession NM_001044283.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Gallon,M. and Cullen,P.J.
  TITLE     Retromer and sorting nexins in endosomal sorting
  JOURNAL   Biochem Soc Trans 43 (1), 33-47 (2015)
   PUBMED   25619244
  REMARK    Review article
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Harrison,M.S., Hung,C.S., Liu,T.T., Christiano,R., Walther,T.C. and
            Burd,C.G.
  TITLE     A mechanism for retromer endosomal coat complex assembly with cargo
  JOURNAL   Proc Natl Acad Sci U S A 111 (1), 267-272 (2014)
   PUBMED   24344282
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Chua,R.Y. and Wong,S.H.
  TITLE     SNX3 recruits to phagosomes and negatively regulates phagocytosis
            in dendritic cells
  JOURNAL   Immunology 139 (1), 30-47 (2013)
   PUBMED   23237080
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Chen,C., Garcia-Santos,D., Ishikawa,Y., Seguin,A., Li,L.,
            Fegan,K.H., Hildick-Smith,G.J., Shah,D.I., Cooney,J.D., Chen,W.,
            King,M.J., Yien,Y.Y., Schultz,I.J., Anderson,H., Dalton,A.J.,
            Freedman,M.L., Kingsley,P.D., Palis,J., Hattangadi,S.M.,
            Lodish,H.F., Ward,D.M., Kaplan,J., Maeda,T., Ponka,P. and Paw,B.H.
  TITLE     Snx3 regulates recycling of the transferrin receptor and iron
            assimilation
  JOURNAL   Cell Metab 17 (3), 343-352 (2013)
   PUBMED   23416069
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Pons,V., Ustunel,C., Rolland,C., Torti,E., Parton,R.G. and
            Gruenberg,J.
  TITLE     SNX12 role in endosome membrane transport
  JOURNAL   PLoS One 7 (6), e38949 (2012)
   PUBMED   22719997
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Dong,H., Yuan,H., Jin,W., Shen,Y., Xu,X. and Wang,H.
  TITLE     Involvement of beta3A subunit of adaptor protein-3 in intracellular
            trafficking of receptor-like protein tyrosine phosphatase PCP-2
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 39 (7), 540-546 (2007)
   PUBMED   17622474
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Zhong,Q., Watson,M.J., Lazar,C.S., Hounslow,A.M., Waltho,J.P. and
            Gill,G.N.
  TITLE     Determinants of the endosomal localization of sorting nexin 1
  JOURNAL   Mol Biol Cell 16 (4), 2049-2057 (2005)
   PUBMED   15673616
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Xu,Y., Hortsman,H., Seet,L., Wong,S.H. and Hong,W.
  TITLE     SNX3 regulates endosomal function through its PX-domain-mediated
            interaction with PtdIns(3)P
  JOURNAL   Nat Cell Biol 3 (7), 658-666 (2001)
   PUBMED   11433298
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Parks,W.T., Frank,D.B., Huff,C., Renfrew Haft,C., Martin,J.,
            Meng,X., de Caestecker,M.P., McNally,J.G., Reddi,A., Taylor,S.I.,
            Roberts,A.B., Wang,T. and Lechleider,R.J.
  TITLE     Sorting nexin 6, a novel SNX, interacts with the transforming
            growth factor-beta family of receptor serine-threonine kinases
  JOURNAL   J Biol Chem 276 (22), 19332-19339 (2001)
   PUBMED   11279102
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Barr,V.A., Haft,D.H. and
            Taylor,S.I.
  TITLE     Identification of a family of sorting nexin molecules and
            characterization of their association with receptors
  JOURNAL   Mol Cell Biol 18 (12), 7278-7287 (1998)
   PUBMED   9819414
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107918.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001068918.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107918.1, FQ234595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q13"
     Protein         1..162
                     /product="sorting nexin-3"
                     /calculated_mol_wt=18631
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O60493; propagated from
                     UniProtKB/Swiss-Prot (Q5U211.1)"
     Region          28..150
                     /region_name="PX_SNX3"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 3; cd07293"
                     /db_xref="CDD:132826"
     Site            43
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O60493; propagated from
                     UniProtKB/Swiss-Prot (Q5U211.1)"
     Site            order(70,72,75,95..96,109,118)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132826"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U211.1)"
     Region          147..162
                     /region_name="Binds predominantly to PtdIns(P5) and weaker
                     to PtdIns(P3) abd PtdIns(P4), involved in neurite
                     outgrowth regulation.
                     /evidence=ECO:0000250|UniProtKB:O70492"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U211.1)"
     CDS             1..162
                     /gene="Snx3"
                     /coded_by="NM_001044283.1:327..815"
                     /db_xref="GeneID:684097"
                     /db_xref="RGD:1595151"
ORIGIN      
        1 maetvadtrr litkpqnlnd aygppsnfle idvsnpqtvg vgrgrfttye irvktnlpif
       61 klkestvrrr ysdfewlrse lereskvvvp plpgkaflrq lpfrgddgif ddnfieerkq
      121 gleqfinkva ghplaqnerc lhmflqdeii dksytpskir ha
//
LOCUS       NP_059055                200 aa            linear   ROD 27-APR-2025
DEFINITION  ras-related protein Rab-10 [Rattus norvegicus].
ACCESSION   NP_059055 XP_346788
VERSION     NP_059055.2
DBSOURCE    REFSEQ: accession NM_017359.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Shi,G., Zhang,Z., Ma,S., Li,Y., Du,S., Chu,Y., Li,Y., Tang,X.,
            Yang,Y., Chen,Z., Wang,Z. and Wu,H.
  TITLE     Hepatic interferon regulatory factor 8 expression mediates liver
            ischemia/reperfusion injury in mice
  JOURNAL   Biochem Pharmacol 192, 114728 (2021)
   PUBMED   34400126
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Bruno,J., Brumfield,A., Chaudhary,N., Iaea,D. and McGraw,T.E.
  TITLE     SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
            trafficking in adipocytes
  JOURNAL   J Cell Biol 214 (1), 61-76 (2016)
   PUBMED   27354378
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Gerondopoulos,A., Bastos,R.N., Yoshimura,S., Anderson,R.,
            Carpanini,S., Aligianis,I., Handley,M.T. and Barr,F.A.
  TITLE     Rab18 and a Rab18 GEF complex are required for normal ER structure
  JOURNAL   J Cell Biol 205 (5), 707-720 (2014)
   PUBMED   24891604
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Xu,X.H., Deng,C.Y., Liu,Y., He,M., Peng,J., Wang,T., Yuan,L.,
            Zheng,Z.S., Blackshear,P.J. and Luo,Z.G.
  TITLE     MARCKS regulates membrane targeting of Rab10 vesicles to promote
            axon development
  JOURNAL   Cell Res 24 (5), 576-594 (2014)
   PUBMED   24662485
  REMARK    GeneRIF: Either genetic silencing of MARCKS or disruption of its
            interaction with Rab10 inhibited axon growth of cortical neurons.
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Babbey,C.M., Ahktar,N., Wang,E., Chen,C.C., Grant,B.D. and
            Dunn,K.W.
  TITLE     Rab10 regulates membrane transport through early endosomes of
            polarized Madin-Darby canine kidney cells
  JOURNAL   Mol Biol Cell 17 (7), 3156-3175 (2006)
   PUBMED   16641372
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Bell,A.W., Ward,M.A., Blackstock,W.P., Freeman,H.N.,
            Choudhary,J.S., Lewis,A.P., Chotai,D., Fazel,A., Gushue,J.N.,
            Paiement,J., Palcy,S., Chevet,E., Lafreniere-Roula,M., Solari,R.,
            Thomas,D.Y., Rowley,A. and Bergeron,J.J.
  TITLE     Proteomics characterization of abundant Golgi membrane proteins
  JOURNAL   J Biol Chem 276 (7), 5152-5165 (2001)
   PUBMED   11042173
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Chen,Y.T., Holcomb,C. and Moore,H.P.
  TITLE     Expression and localization of two low molecular weight GTP-binding
            proteins, Rab8 and Rab10, by epitope tag
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6508-6512 (1993)
   PUBMED   7688123
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Elferink,L.A., Anzai,K. and Scheller,R.H.
  TITLE     rab15, a novel low molecular weight GTP-binding protein
            specifically expressed in rat brain
  JOURNAL   J Biol Chem 267 (9), 5768-5775 (1992)
   PUBMED   1313420
  REMARK    Erratum:[J Biol Chem. 1992 Nov 5;267(31):22693. PMID: 1429617]
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085744.1.
            
            On Mar 27, 2005 this sequence version replaced NP_059055.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085744.1, BC070518.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..200
                     /product="ras-related protein Rab-10"
                     /EC_number="3.6.5.2"
                     /note="ras-related protein rab10"
                     /calculated_mol_wt=22410
     Region          7..173
                     /region_name="Rab8_Rab10_Rab13_like"
                     /note="Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13);
                     cd01867"
                     /db_xref="CDD:206659"
     Site            7..11
                     /site_type="other"
                     /note="Rab subfamily motif 1 (RabSF1)"
                     /db_xref="CDD:206659"
     Site            16..23
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206659"
     Site            order(18..24,34..37,40..41,67,122..123,125..126,153..154)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206659"
     Site            order(24..36,38..40)
                     /site_type="other"
                     /note="Rab subfamily motif 2 (RabSF2)"
                     /db_xref="CDD:206659"
     Site            order(34,39..47)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206659"
     Site            order(37,39,43..50,57,59)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:206659"
     Site            41
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206659"
     Site            order(42,44..46,61,63,70..71,74,78,80..83,170)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206659"
     Site            order(42..43,45,63..64,71,73,75..77)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206659"
     Site            42..46
                     /site_type="other"
                     /note="Rab family motif 1 (RabF1)"
                     /db_xref="CDD:206659"
     Site            59..63
                     /site_type="other"
                     /note="Rab family motif 2 (RabF2)"
                     /db_xref="CDD:206659"
     Site            64..67
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206659"
     Site            order(67,69..79)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206659"
     Site            70..75
                     /site_type="other"
                     /note="Rab family motif 3 (RabF3)"
                     /db_xref="CDD:206659"
     Site            78..82
                     /site_type="other"
                     /note="Rab family motif 4 (RabF4)"
                     /db_xref="CDD:206659"
     Site            87..92
                     /site_type="other"
                     /note="Rab family motif 5 (RabF5)"
                     /db_xref="CDD:206659"
     Site            110..119
                     /site_type="other"
                     /note="Rab subfamily motif 3 (RabSF3)"
                     /db_xref="CDD:206659"
     Site            122..125
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206659"
     Site            152..154
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206659"
     Site            168..173
                     /site_type="other"
                     /note="Rab subfamily motif 4 (RabSF4)"
                     /db_xref="CDD:206659"
     CDS             1..200
                     /gene="Rab10"
                     /gene_synonym="Ac1075"
                     /coded_by="NM_017359.2:49..651"
                     /db_xref="GeneID:50993"
                     /db_xref="RGD:620879"
ORIGIN      
        1 makktydllf kllligdsgv gktcvlfrfs ddafnttfis tigidfkikt velqgkkikl
       61 qiwdtagqer fhtittsyyr gamgimlvyd itngksfeni skwlrnideh anedvermll
      121 gnkcdmddkr vvpkgkgeqi arehgirffe tsakaninie kafltlaedi lrktpvkepn
      181 senvdissgg gvtgwkskcc
//
LOCUS       NP_001107042             363 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor IIIA [Rattus norvegicus].
ACCESSION   NP_001107042 XP_001069721
VERSION     NP_001107042.1
DBSOURCE    REFSEQ: accession NM_001113570.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Sloan,K.E., Bohnsack,M.T. and Watkins,N.J.
  TITLE     The 5S RNP couples p53 homeostasis to ribosome biogenesis and
            nucleolar stress
  JOURNAL   Cell Rep 5 (1), 237-247 (2013)
   PUBMED   24120868
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Vannini,A.
  TITLE     A structural perspective on RNA polymerase I and RNA polymerase III
            transcription machineries
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 258-264 (2013)
   PUBMED   23031840
  REMARK    Review article
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Hanas,J.S., Hocker,J.R., Cheng,Y.G., Lerner,M.R., Brackett,D.J.,
            Lightfoot,S.A., Hanas,R.J., Madhusudhan,K.T. and Moreland,R.J.
  TITLE     cDNA cloning, DNA binding, and evolution of mammalian transcription
            factor IIIA
  JOURNAL   Gene 282 (1-2), 43-52 (2002)
   PUBMED   11814676
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Moreland,R.J., Dresser,M.E., Rodgers,J.S., Roe,B.A., Conaway,J.W.,
            Conaway,R.C. and Hanas,J.S.
  TITLE     Identification of a transcription factor IIIA-interacting protein
  JOURNAL   Nucleic Acids Res 28 (9), 1986-1993 (2000)
   PUBMED   10756201
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB616240.1, AF391798.1,
            CB578423.1 and CK842762.1.
            
            On Jan 25, 2008 this sequence version replaced XP_001069721.1.
            
            Summary: The product of this gene is a zinc finger protein with
            nine Cis[2]-His[2] zinc finger domains. It functions as an RNA
            polymerase III transcription factor to induce transcription of the
            5S rRNA genes. The protein binds to a 50 bp internal promoter in
            the 5S genes called the internal control region (ICR), and
            nucleates formation of a stable preinitiation complex. This complex
            recruits the TFIIIC and TFIIIB transcription factors and RNA
            polymerase III to form the complete transcription complex. The
            protein is thought to be translated using a non-AUG translation
            initiation site in mammals based on sequence analysis, protein
            homology, and the size of the purified protein. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF391798.1, SRR8487227.204770.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: inferred from conservation
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..363
                     /product="transcription factor IIIA"
                     /note="TFIIIA; factor A"
                     /calculated_mol_wt=41256
     Region          40..62
                     /region_name="zinc finger"
     Region          43..62
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(47,49,51,53..54,57..58,61,77,79,83..84,87..88,91,
                     107,109,111,113..114,117..118,122)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <62..185
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          70..92
                     /region_name="zinc finger"
     Region          70..92
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          100..123
                     /region_name="zinc finger"
     Region          100..123
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          132..154
                     /region_name="zinc finger"
     Region          135..154
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(139,141,143,145..146,149..150,153,169,171,175..176,
                     179..180,183,222,224,226,228..229,232..233,236)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          162..184
                     /region_name="zinc finger"
     Region          162..184
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          189..211
                     /region_name="zinc finger"
     Region          216..237
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          217..237
                     /region_name="zinc finger"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <243..295
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          246..269
                     /region_name="zinc finger"
     Region          246..269
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..299
                     /region_name="zinc finger"
     Region          277..299
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHT8.2)"
     CDS             1..363
                     /gene="Gtf3a"
                     /coded_by="NM_001113570.1:159..1250"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:246299"
                     /db_xref="RGD:619746"
ORIGIN      
        1 meprvsvaea vssltiadaf vracvgpapp rpalpsrfic sfpdcsasyn kawkldahlc
       61 khtgerpfvc dyegcgkafi rdyhlsrhil ihtgekpfvc adngcnqkfs tksnlkkhie
      121 rkhenpqkqy vcnfegckka fkkhqqlrth qcqhtneplf rcthegcgkh faspsrlkrh
      181 gkvhegylcq kgcsfvgktw tellkhtrea hkeevtctvc qkmfkrkdhl kqhmkthape
      241 rdvyrcpreg cartyttvfn lqshilsfhe ekrpfvceha gcgktfamkq slmrhsvvhd
      301 pdkkrmklkv rpprerrsla srlsgyvppk gkqepdcslp nstesssspe atmlapaall
      361 tvh
//
LOCUS       NP_446043                410 aa            linear   ROD 27-APR-2025
DEFINITION  dipeptidase 1 precursor [Rattus norvegicus].
ACCESSION   NP_446043
VERSION     NP_446043.1
DBSOURCE    REFSEQ: accession NM_053591.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Cui,X., Liu,X., Han,Q., Zhu,J., Li,J., Ren,Z., Liu,L., Luo,Y.,
            Wang,Z., Zhang,D., Fan,Y., Zhang,D. and Dong,G.
  TITLE     DPEP1 is a direct target of miR-193a-5p and promotes hepatoblastoma
            progression by PI3K/Akt/mTOR pathway
  JOURNAL   Cell Death Dis 10 (10), 701 (2019)
   PUBMED   31541079
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Choudhury,S.R., Babes,L., Rahn,J.J., Ahn,B.Y., Goring,K.R.,
            King,J.C., Lau,A., Petri,B., Hao,X., Chojnacki,A.K.,
            Thanabalasuriar,A., McAvoy,E.F., Tabaries,S., Schraeder,C.,
            Patel,K.D., Siegel,P.M., Kopciuk,K.A., Schriemer,D.C., Muruve,D.A.,
            Kelly,M.M., Yipp,B.G., Kubes,P., Robbins,S.M. and Senger,D.L.
  TITLE     Dipeptidase-1 Is an Adhesion Receptor for Neutrophil Recruitment in
            Lungs and Liver
  JOURNAL   Cell 178 (5), 1205-1221 (2019)
   PUBMED   31442408
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Toiyama,Y., Inoue,Y., Yasuda,H., Saigusa,S., Yokoe,T., Okugawa,Y.,
            Tanaka,K., Miki,C. and Kusunoki,M.
  TITLE     DPEP1, expressed in the early stages of colon carcinogenesis,
            affects cancer cell invasiveness
  JOURNAL   J Gastroenterol 46 (2), 153-163 (2011)
   PUBMED   20824289
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Camano,S., Lazaro,A., Moreno-Gordaliza,E., Torres,A.M., de
            Lucas,C., Humanes,B., Lazaro,J.A., Milagros Gomez-Gomez,M.,
            Bosca,L. and Tejedor,A.
  TITLE     Cilastatin attenuates cisplatin-induced proximal tubular cell
            damage
  JOURNAL   J Pharmacol Exp Ther 334 (2), 419-429 (2010)
   PUBMED   20435919
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Pare,G., Chasman,D.I., Parker,A.N., Zee,R.R., Malarstig,A.,
            Seedorf,U., Collins,R., Watkins,H., Hamsten,A., Miletich,J.P. and
            Ridker,P.M.
  TITLE     Novel associations of CPS1, MUT, NOX4, and DPEP1 with plasma
            homocysteine in a healthy population: a genome-wide evaluation of
            13 974 participants in the Women's Genome Health Study
  JOURNAL   Circ Cardiovasc Genet 2 (2), 142-150 (2009)
   PUBMED   20031578
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Keynan,S., Habgood,N.T., Hooper,N.M. and Turner,A.J.
  TITLE     Site-directed mutagenesis of conserved cysteine residues in porcine
            membrane dipeptidase. Cys 361 alone is involved in disulfide-linked
            dimerization
  JOURNAL   Biochemistry 35 (38), 12511-12517 (1996)
   PUBMED   8823187
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Mori,M., Hikida,M., Nishihara,T., Nasu,T. and Mitsuhashi,S.
  TITLE     Comparative stability of carbapenem and penem antibiotics to human
            recombinant dehydropeptidase-I
  JOURNAL   J Antimicrob Chemother 37 (5), 1034-1036 (1996)
   PUBMED   8737157
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Keynan,S., Hooper,N.M. and Turner,A.J.
  TITLE     Directed mutagenesis of pig renal membrane dipeptidase. His219 is
            critical but the DHXXH motif is not essential for zinc binding or
            catalytic activity
  JOURNAL   FEBS Lett 349 (1), 50-54 (1994)
   PUBMED   8045301
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Adachi,H., Ishida,N. and Tsujimoto,M.
  TITLE     Primary structure of rat renal dipeptidase and expression of its
            mRNA in rat tissues and COS-1 cells
  JOURNAL   Biochim Biophys Acta 1132 (3), 311-314 (1992)
   PUBMED   1420313
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Campbell,B.J., Forrester,L.J., Zahler,W.L. and Burks,M.
  TITLE     Beta-lactamase activity of purified and partially characterized
            human renal dipeptidase
  JOURNAL   J Biol Chem 259 (23), 14586-14590 (1984)
   PUBMED   6334084
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072476.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072476.1, L07315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..410
                     /product="dipeptidase 1 precursor"
                     /EC_number="3.4.13.19"
                     /EC_number="3.5.2.6"
                     /note="renal dipeptidase; microsomal dipeptidase;
                     dipeptidase 1 (renal); beta-lactamase"
                     /calculated_mol_wt=43587
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1953
     mat_peptide     17..384
                     /product="Dipeptidase 1. /id=PRO_0000018660"
                     /note="propagated from UniProtKB/Swiss-Prot (P31430.2)"
                     /calculated_mol_wt=40864
     Region          26..352
                     /region_name="Peptidase_M19"
                     /note="Membrane dipeptidase (Peptidase family M19);
                     pfam01244"
                     /db_xref="CDD:395996"
     Site            order(36,38,84,141,214,235,246,304,307)
                     /site_type="active"
                     /db_xref="CDD:238626"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31430.2)"
     Site            order(86,95..97,99..100,103,107,151..152,154..155,
                     158..159)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238626"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31430.2)"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31430.2)"
     CDS             1..410
                     /gene="Dpep1"
                     /coded_by="NM_053591.2:152..1384"
                     /db_xref="GeneID:94199"
                     /db_xref="RGD:620324"
ORIGIN      
        1 mliiwwfwsl laicasdsfr nqaenimrtt pvidghndlp wqmltlfnnq lrkseanlsa
       61 laethtnipk lragfvggqf wsaympcdtq nkdavkrile qidvihrmcq lypetfecvt
      121 nssdilqafr rgkvasligv egghlidssl gvlrtlyhlg mryltlthnc ntpwadnwlv
      181 dkgddeaesq glspfgklvl nemnrlgvmi dlshvsvatm kdalqlskap vifshssays
      241 vcphrrnvpd dvlqlvkstn slvmvnfynq fvscsdsatl sqvadhldhi kkvagagavg
      301 lggdydgvtn lpvgledvsk ypdliaellr rnwtetevrg llaenllrvf savelvsnim
      361 qvpeeetipv ekldgscrtf yghsrapsih lqigallasl aslvfslhll
//
LOCUS       NP_001020891             920 aa            linear   ROD 27-APR-2025
DEFINITION  2-oxoadipate dehydrogenase complex component E1 [Rattus
            norvegicus].
ACCESSION   NP_001020891 XP_341558
VERSION     NP_001020891.1
DBSOURCE    REFSEQ: accession NM_001025720.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Artiukhov,A.V., Grabarska,A., Gumbarewicz,E., Aleshin,V.A.,
            Kahne,T., Obata,T., Kazantsev,A.V., Lukashev,N.V., Stepulak,A.,
            Fernie,A.R. and Bunik,V.I.
  TITLE     Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues
  JOURNAL   Sci Rep 10 (1), 1886 (2020)
   PUBMED   32024885
  REMARK    GeneRIF: Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Tsepkova,P.M., Artiukhov,A.V., Boyko,A.I., Aleshin,V.A.,
            Mkrtchyan,G.V., Zvyagintseva,M.A., Ryabov,S.I., Ksenofontov,A.L.,
            Baratova,L.A., Graf,A.V. and Bunik,V.I.
  TITLE     Thiamine Induces Long-Term Changes in Amino Acid Profiles and
            Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in Rat
            Brain
  JOURNAL   Biochemistry (Mosc) 82 (6), 723-736 (2017)
   PUBMED   28601082
  REMARK    GeneRIF: Thiamine Induces Long-Term Changes in Amino Acid Profiles
            and Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in
            Rat Brain
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Nagamachi,A., Matsui,H., Asou,H., Ozaki,Y., Aki,D., Kanai,A.,
            Takubo,K., Suda,T., Nakamura,T., Wolff,L., Honda,H. and Inaba,T.
  TITLE     Haploinsufficiency of SAMD9L, an endosome fusion facilitator,
            causes myeloid malignancies in mice mimicking human diseases with
            monosomy 7
  JOURNAL   Cancer Cell 24 (3), 305-317 (2013)
   PUBMED   24029230
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Xu,W.Y., Gu,M.M., Sun,L.H., Guo,W.T., Zhu,H.B., Ma,J.F., Yuan,W.T.,
            Kuang,Y., Ji,B.J., Wu,X.L., Chen,Y., Zhang,H.X., Sun,F.T.,
            Huang,W., Huang,L., Chen,S.D. and Wang,Z.G.
  TITLE     A nonsense mutation in DHTKD1 causes Charcot-Marie-Tooth disease
            type 2 in a large Chinese pedigree
  JOURNAL   Am J Hum Genet 91 (6), 1088-1094 (2012)
   PUBMED   23141294
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099075.1.
            
            On Jul 22, 2005 this sequence version replaced XP_341558.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..920
                     /product="2-oxoadipate dehydrogenase complex component E1"
                     /EC_number="1.2.4.2"
                     /note="probable 2-oxoglutarate dehydrogenase E1 component
                     DHKTD1, mitochondrial; dehydrogenase E1 and transketolase
                     domain-containing protein 1; probable 2-oxoglutarate
                     dehydrogenase E1 component DHKTD1, mitochondrial-like;
                     alpha-KADH-E1; alpha-ketoadipate dehydrogenase;
                     2-oxoadipate dehydrogenase, mitochondrial"
                     /calculated_mol_wt=102511
     Region          58..914
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
     Region          299..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLP0.1)"
     CDS             1..920
                     /gene="Dhtkd1"
                     /gene_synonym="E1a; OADC-E1; OADH-E1"
                     /coded_by="NM_001025720.1:70..2832"
                     /db_xref="GeneID:361272"
                     /db_xref="RGD:1308092"
ORIGIN      
        1 masatvaaag ralrravpll rrsyqtergv ygyrprkags geprgdrarp svdhglarlv
       61 tvycehghka aqinplfpgq alldtvpeiq alvqtlqgpf tttgllnmgk eeasleevla
      121 ylnhiycgpi sietaqlqsq eekdwfarrf eelkketftt eerkhlskll lesqefdhfl
      181 atkfatvkry ggegaesmmg ffhellklsa yggitdiiig mphrgrlnll tgllqlppel
      241 mfrkmrglse fpenvaaigd vlshltssvd ldfgahrplh vtmlpnpshl eainpvavgk
      301 trgrqqsqed gdyspngsaq pgdkviclqv hgdasfcgqg ivletftlsn lphfriggsi
      361 hlivnnqlgy ttpaergrss lyssdigklv gcaiihvngd speevvratr lafeyqrqfr
      421 kdviidllcy rqwghnelde pfftnpvmyk iirarksipd tyaehliasg lmtqeevsdi
      481 kasyyaklng hlanvahysp paphlqarwq glvqpaacvt twdtgvplel lrfvgvksve
      541 vpeelqlhsh llkmyvqsrm ekvkngtnld wataetlalg sllaqgfnvr lsgqdvgrgt
      601 fsqrhamvvc qntddvyipl nhmdpnqkgf levsnsplse eavlgfeygm siespkllpl
      661 weaqfgdffn gaqiifdtfi sggeakwllq sglvillphg ydgagpdhss crierflqmc
      721 dsaeegvdsd tvnmfvvhpt tpaqyfhllr rqmmrnfrkp livaspkmll rypvavstle
      781 emapgtafkp vigdssvdpk nvktlifcsg khfyallkqr eslgakkrdf aiirleelcp
      841 fpldslqqem gkykhvqdii wsqeepqnmg pwsfvyprfe kqlacklrlv srpplpapav
      901 gigtvhqqqh eailfktfts
//
LOCUS       NP_062144                471 aa            linear   ROD 27-APR-2025
DEFINITION  heat shock 70 kDa protein 13 precursor [Rattus norvegicus].
ACCESSION   NP_062144
VERSION     NP_062144.2
DBSOURCE    REFSEQ: accession NM_019271.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Otterson,G.A. and Kaye,F.J.
  TITLE     A 'core ATPase', Hsp70-like structure is conserved in human, rat,
            and C. elegans STCH proteins
  JOURNAL   Gene 199 (1-2), 287-292 (1997)
   PUBMED   9358068
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Otterson,G.A., Flynn,G.C., Kratzke,R.A., Coxon,A., Johnston,P.G.
            and Kaye,F.J.
  TITLE     Stch encodes the 'ATPase core' of a microsomal stress 70 protein
  JOURNAL   EMBO J 13 (5), 1216-1225 (1994)
   PUBMED   8131751
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070954.1.
            
            On Jun 10, 2007 this sequence version replaced NP_062144.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070954.1, AF006617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11p11"
     Protein         1..471
                     /product="heat shock 70 kDa protein 13 precursor"
                     /note="stress 70 protein chaperone, microsome-associated,
                     60kD human homolog; heat shock 70 kDa protein 13; heat
                     shock protein 70 family, member 13; microsomal stress-70
                     protein ATPase core; stress-70 protein chaperone
                     microsome-associated 60 kDa protein; heat shock protein
                     70kDa family, member 13; stress 70 protein chaperone,
                     microsome-associated, human homolog; heat shock protein
                     13"
                     /calculated_mol_wt=49605
     sig_peptide     1..22
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35162.2)"
                     /calculated_mol_wt=2209
     Region          10..452
                     /region_name="ASKHA_NBD_HSP70_HSPA13"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 13 (HSPA13) and similar proteins; cd10237"
                     /db_xref="CDD:466835"
     mat_peptide     23..471
                     /product="Heat shock 70 kDa protein 13.
                     /id=PRO_0000013561"
                     /note="propagated from UniProtKB/Swiss-Prot (O35162.2)"
                     /calculated_mol_wt=49605
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (O35162.2)"
     Region          316..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35162.2)"
     CDS             1..471
                     /gene="Hspa13"
                     /gene_synonym="Stch"
                     /coded_by="NM_019271.2:4..1419"
                     /db_xref="GeneID:29734"
                     /db_xref="RGD:3775"
ORIGIN      
        1 magemtilgs avltlllagy laqqylplpt pkvigidlgt tycsvgvffp gtgkvkvipd
       61 enghisipsm vsftdgdvyv gyeslelads npqntiydak rfigkiftpe eleaeigryp
      121 fkvlhkngma efsvtsneti ivspeyvgsr lllklkemae kylgmpvana visvpaefdl
      181 qqrnstiqaa nlaglkilrv ineptaaama yglhkvdvfy vlvidlgggt ldvsllnkqg
      241 gmfltramsg nnklggqdfn qrllqylyke iyqtygflps rkeeihrlrq avemvklnlt
      301 lhqsaqvsvl ltveendsqk pqnadsklpe dqltpgdghh vnrvfrpgls dstsgksqvl
      361 fetevsrklf ntlnedlfqk ilvpiqqvlk eglldkteid evvlvggstr iprirqviqe
      421 ffgkdpntsv dpdlavvtgv aiqagidggs wplqvsalei pnkhlqktnf n
//
LOCUS       NP_001121052             520 aa            linear   ROD 27-APR-2025
DEFINITION  succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
            precursor [Rattus norvegicus].
ACCESSION   NP_001121052 XP_001053611 XP_001053666 XP_001073299 XP_001073523
VERSION     NP_001121052.1
DBSOURCE    REFSEQ: accession NM_001127580.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Cotter,D.G., d'Avignon,D.A., Wentz,A.E., Weber,M.L. and
            Crawford,P.A.
  TITLE     Obligate role for ketone body oxidation in neonatal metabolic
            homeostasis
  JOURNAL   J Biol Chem 286 (9), 6902-6910 (2011)
   PUBMED   21209089
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Fraser,M.E., Hayakawa,K. and Brown,W.D.
  TITLE     Catalytic role of the conformational change in
            succinyl-CoA:3-oxoacid CoA transferase on binding CoA
  JOURNAL   Biochemistry 49 (48), 10319-10328 (2010)
   PUBMED   20977214
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Coker,S.F., Lloyd,A.J., Mitchell,E., Lewis,G.R., Coker,A.R. and
            Shoolingin-Jordan,P.M.
  TITLE     The high-resolution structure of pig heart succinyl-CoA:3-oxoacid
            coenzyme A transferase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 66 (Pt 7), 797-805 (2010)
   PUBMED   20606260
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Hasan,N.M., Longacre,M.J., Seed Ahmed,M., Kendrick,M.A., Gu,H.,
            Ostenson,C.G., Fukao,T. and MacDonald,M.J.
  TITLE     Lower succinyl-CoA:3-ketoacid-CoA transferase (SCOT) and ATP
            citrate lyase in pancreatic islets of a rat model of type 2
            diabetes: knockdown of SCOT inhibits insulin release in rat
            insulinoma cells
  JOURNAL   Arch Biochem Biophys 499 (1-2), 62-68 (2010)
   PUBMED   20460097
  REMARK    GeneRIF: mRNAs of SCOT and ATP citrate lyase were decreased 55% and
            58% and enzyme activities were decreased >70% in pancreatic islets
            of the GK rat, a model of type 2 diabetes.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Bregere,C., Rebrin,I., Gallaher,T.K. and Sohal,R.S.
  TITLE     Effects of age and calorie restriction on tryptophan nitration,
            protein content, and activity of succinyl-CoA:3-ketoacid CoA
            transferase in rat kidney mitochondria
  JOURNAL   Free Radic Biol Med 48 (4), 609-618 (2010)
   PUBMED   20025965
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Grinblat,L., Pacheco Bolanos,L.F. and Stoppani,A.O.
  TITLE     Decreased rate of ketone-body oxidation and decreased activity of
            D-3-hydroxybutyrate dehydrogenase and succinyl-CoA:3-oxo-acid
            CoA-transferase in heart mitochondria of diabetic rats
  JOURNAL   Biochem J 240 (1), 49-56 (1986)
   PUBMED   3548709
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Williamson,D.H. and Ilic,V.
  TITLE     Activities of enzymes of acetoacetate metabolism in rat brown
            adipose tissue during development
  JOURNAL   Biochem J 231 (3), 773-775 (1985)
   PUBMED   2866764
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Escriva,F., Rodriguez,C. and Pascual-Leone,A.M.
  TITLE     Glycemia, ketonemia, and brain enzymes of ketone body utilization
            in suckling and adult rats undernourished from intrauterine life
  JOURNAL   J Neurochem 44 (5), 1358-1362 (1985)
   PUBMED   2985752
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Pacanis,A. and Rogulski,J.
  TITLE     Substrate specificity of succinyl-CoA transferase from rat kidney
            mitochondria
  JOURNAL   Acta Biochim Pol 24 (1), 3-11 (1977)
   PUBMED   868435
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Askew,E.W., Dohm,G.L. and Huston,R.L.
  TITLE     Fatty acid and ketone body metabolism in the rat: response to diet
            and exercise
  JOURNAL   J Nutr 105 (11), 1422-1432 (1975)
   PUBMED   475
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166478.1.
            
            On or before May 31, 2008 this sequence version replaced
            XP_001073299.1, XP_001073523.1, XP_001053666.1, XP_001053611.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166478.1, AY724483.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..520
                     /product="succinyl-CoA:3-ketoacid coenzyme A transferase
                     1, mitochondrial precursor"
                     /EC_number="2.8.3.5"
                     /note="scot-S; somatic-type succinyl-CoA:3-oxoacid
                     CoA-transferase; succinyl-CoA:3-ketoacid CoA transferase;
                     succinyl-CoA:3-ketoacid coenzyme A transferase 1,
                     mitochondrial; succinyl-CoA:3-ketoacid-coenzyme A
                     transferase 1, mitochondrial-like; succinyl-CoA:3-oxoacid
                     CoA transferase"
                     /calculated_mol_wt=52047
     transit_peptide 1..39
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:P55809; propagated from
                     UniProtKB/Swiss-Prot (B2GV06.1)"
                     /calculated_mol_wt=4175
     mat_peptide     40..520
                     /product="Succinyl-CoA:3-ketoacid coenzyme A transferase
                     1, mitochondrial. /id=PRO_0000349127"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV06.1)"
                     /calculated_mol_wt=52047
     Region          41..279
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55809; propagated from
                     UniProtKB/Swiss-Prot (B2GV06.1)"
     Region          300..508
                     /region_name="SugarP_isomerase"
                     /note="Sugar Phosphate Isomerase family; includes type A
                     ribose 5-phosphate isomerase (RPI_A),
                     glucosamine-6-phosphate (GlcN6P) deaminase, and
                     6-phosphogluconolactonase (6PGL). RPI catalyzes the
                     reversible conversion of ribose-5-phosphate to
                     ribulose...; cl00339"
                     /db_xref="CDD:469729"
     CDS             1..520
                     /gene="Oxct1"
                     /gene_synonym="SCOT"
                     /coded_by="NM_001127580.1:99..1661"
                     /db_xref="GeneID:690163"
                     /db_xref="RGD:1584008"
ORIGIN      
        1 maalkllssg lrlcasarns rgalhkgcac yfsvstrhht kfytdpveav kdipngatll
       61 vggfglcgip enligallkt gvkdltavsn nagvdnfglg lllrskqikr missyvgena
      121 eferqflsge leveltpqgt laeriragga gvpafytstg ygtlvqeggs pikynkdgsv
      181 aiaskprevr efrgqhfile eaitgdfalv kawkadragn vifrksarnf nlpmckaagt
      241 tvveveeivd igsfapedih ipkiyvhrli kgekyekrie rlslrkegeg kaksgkpged
      301 vreriikraa lefedgmyan lgigipllas nfispnmtvh lqsengvlgl gpyplkdead
      361 adlinagket vtvlpgasff ssdesfamir gghvnltmlg amqvskygdl anwmipgkmv
      421 kgmggamdlv sssktkvvvt mehsakgnah kimekctlpl tgkqcvnrii tekgvfdvdk
      481 kngltlielw egltvddirk stgcdfavsp nlmpmqqist
//
LOCUS       NP_598244                913 aa            linear   ROD 27-APR-2025
DEFINITION  trafficking kinesin-binding protein 2 [Rattus norvegicus].
ACCESSION   NP_598244
VERSION     NP_598244.2
DBSOURCE    REFSEQ: accession NM_133560.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Loss,O. and Stephenson,F.A.
  TITLE     Localization of the kinesin adaptor proteins trafficking kinesin
            proteins 1 and 2 in primary cultures of hippocampal pyramidal and
            cortical neurons
  JOURNAL   J Neurosci Res 93 (7), 1056-1066 (2015)
   PUBMED   25653102
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Lin,M.Y. and Sheng,Z.H.
  TITLE     Regulation of mitochondrial transport in neurons
  JOURNAL   Exp Cell Res 334 (1), 35-44 (2015)
   PUBMED   25612908
  REMARK    Review article
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Randall,T.S., Moores,C. and Stephenson,F.A.
  TITLE     Delineation of the TRAK binding regions of the kinesin-1 motor
            proteins
  JOURNAL   FEBS Lett 587 (23), 3763-3769 (2013)
   PUBMED   24161670
REFERENCE   4  (residues 1 to 913)
  AUTHORS   van Spronsen,M., Mikhaylova,M., Lipka,J., Schlager,M.A., van den
            Heuvel,D.J., Kuijpers,M., Wulf,P.S., Keijzer,N., Demmers,J.,
            Kapitein,L.C., Jaarsma,D., Gerritsen,H.C., Akhmanova,A. and
            Hoogenraad,C.C.
  TITLE     TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking
            to axons and dendrites
  JOURNAL   Neuron 77 (3), 485-502 (2013)
   PUBMED   23395375
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Li,Y., Lim,S., Hoffman,D., Aspenstrom,P., Federoff,H.J. and
            Rempe,D.A.
  TITLE     HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters
            mitochondrial distribution and transport
  JOURNAL   J Cell Biol 185 (6), 1065-1081 (2009)
   PUBMED   19528298
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Kirk,E., Chin,L.S. and Li,L.
  TITLE     GRIF1 binds Hrs and is a new regulator of endosomal trafficking
  JOURNAL   J Cell Sci 119 (Pt 22), 4689-4701 (2006)
   PUBMED   17062640
  REMARK    GeneRIF: GRIF1 may participate in microtubule-based transport of
            early endosomes by acting as an adaptor linking Hrs-containing
            endosomes to kinesin.
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Fransson,S., Ruusala,A. and Aspenstrom,P.
  TITLE     The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in
            mitochondrial trafficking
  JOURNAL   Biochem Biophys Res Commun 344 (2), 500-510 (2006)
   PUBMED   16630562
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Beck,M., Brickley,K., Wilkinson,H.L., Sharma,S., Smith,M.,
            Chazot,P.L., Pollard,S. and Stephenson,F.A.
  TITLE     Identification, molecular cloning, and characterization of a novel
            GABAA receptor-associated protein, GRIF-1
  JOURNAL   J Biol Chem 277 (33), 30079-30090 (2002)
   PUBMED   12034717
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AJ288898.2 and BC088393.1.
            
            On Sep 20, 2005 this sequence version replaced NP_598244.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088393.1, AJ288898.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..913
                     /product="trafficking kinesin-binding protein 2"
                     /note="GABA-A receptor interacting factor-1; O-GlcNAc
                     transferase-interacting protein of 98 kDa; amyotrophic
                     lateral sclerosis 2 chromosomal region candidate gene 3
                     protein homolog; amyotrophic lateral sclerosis 2
                     (juvenile) chromosome region, candidate 3 homolog;
                     amyotrophic lateral sclerosis 2 (juvenile) chromosome
                     region candidate 3; trafficking protein, kinesin binding
                     2"
                     /calculated_mol_wt=101509
     Region          11..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H7.2)"
     Region          48..353
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          359..507
                     /region_name="Interaction with HGS.
                     /evidence=ECO:0000269|PubMed:17062640"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H7.2)"
     Region          414..565
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     Region          442..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H7.2)"
     Region          688..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H7.2)"
     Region          769..790
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H7.2)"
     CDS             1..913
                     /gene="Trak2"
                     /gene_synonym="Als2cr3; GRIF-1"
                     /coded_by="NM_133560.2:371..3112"
                     /db_xref="GeneID:171086"
                     /db_xref="RGD:620915"
ORIGIN      
        1 mslsqnaifk sqtgeenlms snhrdsesit dvcsnedlpe velvnlleeq lpqyklrvds
       61 lflyenqdws qsshqqqdas etlspvlaee tfrymilgtd rveqmtktyn didmvthlla
      121 erdrdlelaa rigqallkrn hvlseqnesl eeqlgqafdq vnqlqhelsk keellrivsi
      181 aseesetdss cstplrfnes fslsqgllql dmmheklkel eeenmalrsk achiktetft
      241 yeekeqklin dcvnelretn aqmsrmteel sgksdellry qeeissllsq ivdlqhklke
      301 hviekeelrl hlqaskdaqr qltmelhelq drnmeclgml hesqeeikel rnkagpsahl
      361 cfsqaygvfa geslaaeieg tmrkklslde esvfkqkaqq krvfdtvkva ndtrgrsvtf
      421 pvllpipgsn rssvimtakp fesgvqqted ktlpnqgsst evpgnshprd ppglpedsdl
      481 atalhrlslr rqnylsekqf faeewerklq ilaeqeeevs scealtenla sfctdqsett
      541 elgsagclrg fmpeklqivk plegsqtlhh wqqlaqpnlg tildprpgvi tkgftqmpkd
      601 avyhisdlee deevgitfqv qqplqleqkp appppvtgif lppmtsaggp vsvatsnpgk
      661 clsftnstft fttcrilhps ditqvtpssg fpslscgssa gsasntavns paasyrlsig
      721 esitnrrdst itfsstrsla kllqergisa kvyhspasen pllqlrpkal atpstppnsp
      781 sqspcsspvp feprvhvsen flasrpaetf lqemyglrps rappdvgqlk mnlvdrlkrl
      841 giarvvktpv prengksrea emglqkpdsa vylnsggsll gglrrnqslp vmmgsfgapv
      901 cttspkmgil ked
//
LOCUS       NP_036643               1452 aa            linear   ROD 27-APR-2025
DEFINITION  copper-transporting ATPase 2 [Rattus norvegicus].
ACCESSION   NP_036643
VERSION     NP_036643.2
DBSOURCE    REFSEQ: accession NM_012511.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1452)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 1452)
  AUTHORS   Sanchez-Monteagudo,A., Alvarez-Sauco,M., Sastre,I.,
            Martinez-Torres,I., Lupo,V., Berenguer,M. and Espinos,C.
  TITLE     Genetics of Wilson disease and Wilson-like phenotype in a clinical
            series from eastern Spain
  JOURNAL   Clin Genet 97 (5), 758-763 (2020)
   PUBMED   32043565
REFERENCE   3  (residues 1 to 1452)
  AUTHORS   Fujiyoshi,J., Yamaza,H., Sonoda,S., Yuniartha,R., Ihara,K.,
            Nonaka,K., Taguchi,T., Ohga,S. and Yamaza,T.
  TITLE     Therapeutic potential of hepatocyte-like-cells converted from stem
            cells from human exfoliated deciduous teeth in fulminant Wilson's
            disease
  JOURNAL   Sci Rep 9 (1), 1535 (2019)
   PUBMED   30733544
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1452)
  AUTHORS   Platonova,N.A., Orlov,I.A., Klotchenko,S.A., Babich,V.S.,
            Ilyechova,E.Y., Babich,P.S., Garmai,Y.P., Vasin,A.V.,
            Tsymbalenko,N.V. and Puchkova,L.V.
  TITLE     Ceruloplasmin gene expression profile changes in the rat mammary
            gland during pregnancy, lactation and involution
  JOURNAL   J Trace Elem Med Biol 43, 126-134 (2017)
   PUBMED   28089327
REFERENCE   5  (residues 1 to 1452)
  AUTHORS   Papur,O.S., Terzioglu,O. and Koc,A.
  TITLE     Functional characterization of new mutations in Wilson disease gene
            (ATP7B) using the yeast model
  JOURNAL   J Trace Elem Med Biol 31, 33-36 (2015)
   PUBMED   26004889
REFERENCE   6  (residues 1 to 1452)
  AUTHORS   Mercer,J.F., Grimes,A. and Rauch,H.
  TITLE     Hepatic metallothionein gene expression in toxic milk mice
  JOURNAL   J Nutr 122 (6), 1254-1259 (1992)
   PUBMED   1588441
REFERENCE   7  (residues 1 to 1452)
  AUTHORS   Okayasu,T., Tochimaru,H., Hyuga,T., Takahashi,T., Takekoshi,Y.,
            Li,Y., Togashi,Y., Takeichi,N., Kasai,N. and Arashima,S.
  TITLE     Inherited copper toxicity in Long-Evans cinnamon rats exhibiting
            spontaneous hepatitis: a model of Wilson's disease
  JOURNAL   Pediatr Res 31 (3), 253-257 (1992)
   PUBMED   1561010
REFERENCE   8  (residues 1 to 1452)
  AUTHORS   Li,Y., Togashi,Y., Sato,S., Emoto,T., Kang,J.H., Takeichi,N.,
            Kobayashi,H., Kojima,Y., Une,Y. and Uchino,J.
  TITLE     Spontaneous hepatic copper accumulation in Long-Evans Cinnamon rats
            with hereditary hepatitis. A model of Wilson's disease
  JOURNAL   J Clin Invest 87 (5), 1858-1861 (1991)
   PUBMED   2022751
REFERENCE   9  (residues 1 to 1452)
  AUTHORS   Biempica,L., Rauch,H., Quintana,N. and Sternlieb,I.
  TITLE     Morphologic and chemical studies on a murine mutation (toxic milk
            mice) resulting in hepatic copper toxicosis
  JOURNAL   Lab Invest 59 (4), 500-508 (1988)
   PUBMED   2845190
REFERENCE   10 (residues 1 to 1452)
  AUTHORS   Masuda,R., Yoshida,M.C., Sasaki,M., Dempo,K. and Mori,M.
  TITLE     Hereditary hepatitis of LEC rats is controlled by a single
            autosomal recessive gene
  JOURNAL   Lab Anim 22 (2), 166-169 (1988)
   PUBMED   3392951
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB017792.1 and JAXUCZ010000016.1.
            
            On Oct 11, 2007 this sequence version replaced NP_036643.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB017792.1, AB017791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1452
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..1452
                     /product="copper-transporting ATPase 2"
                     /EC_number="7.2.2.8"
                     /note="copper pump 2; pineal night-specific ATPase; wilson
                     disease-associated protein homolog; ATPase, Cu++
                     transporting, beta polypeptide (same as Wilson disease);
                     PINA gene, promoter"
                     /calculated_mol_wt=155900
     Region          59..122
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(65..67,70)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          144..207
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(150..152,155)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          259..320
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(264..266,269)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          327..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Region          354..424
                     /region_name="UxxU_metal_bind"
                     /note="metal-binding (seleno)protein; NF041115"
                     /db_xref="CDD:469038"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64535.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64535.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64535.1)"
     Region          484..546
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(489..491,494)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          559..622
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(565..567,570)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          644..1341
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            646..667
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            690..709
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            717..737
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            757..777
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            912..934
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            965..986
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            order(975,977,1318)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(1019..1021,1089,1135..1137,1167,1207..1209,1229,
                     1232,1235,1254,1257)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            1310..1327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64535.1)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64535.1)"
     Site            1444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64535.1)"
     CDS             1..1452
                     /gene="Atp7b"
                     /gene_synonym="Hts; PINA; Wd"
                     /coded_by="NM_012511.2:5..4363"
                     /db_xref="GeneID:24218"
                     /db_xref="RGD:2180"
ORIGIN      
        1 mpeqerkvta keasrkilsk lalptrpwgq smkqsfafdn vgyeggldst cssstttgvv
       61 silgmtchsc vksiedriss lkgivsikvs leqgsatvky vpsvlnlqqi clqiedmgfe
      121 asaaegkaas wpsrsspaqe avvklrvegm tcqscvssie gkirklqgvv rvkvslsnqe
      181 avityqpyli qpedlrdhic dmgfeaaikn rtaplrlgpi dinklestnl kraavppiqn
      241 snhletpghq qnhlatlplr idgmhckscv lniegnigql pgvqnihvsl enktaqvqyd
      301 sscitplflq taiealppgy fkvslpdgle kesgsssvps lgssqrqqep gpcrtavlti
      361 tgiprdssvq pmedmlsqmk gvqqidisla egtgavlydp svvssdelrt avedmgfevs
      421 vnpenittnr vssgnsvpqa vgdspgsvqn masdtrgllt hqgpgylsds ppspggtasq
      481 kcfvqikgmt cascvsnier slqrhagils vlvalmsgka evkydpeviq spriaqlied
      541 lgfeaaimed ntvsegdiel iitgmtcasc vhnieskltr tngityasva latskahvkf
      601 dpeiigprdi ikvieeigfh aslahrnpna hhldhkteik qwkksflcsl vfgipvmglm
      661 iymlipsskp hetmvldhni ipglsvlnli ffilctfvqf lggwyfyvqa ykslrhksan
      721 mdvlivlatt iayayslvil vvaiaekaek spvtffdtpp mlfvfialgr wlehvakskt
      781 sealaklmsl qateatvvtl gednlilree qvpmelvqrg diikvvpggk fpvdgkvleg
      841 ntmadeslit geampvtkkp gsiviagsin ahgsvlikat hvgndttlaq ivklveeaqm
      901 skapiqqlad rfsgyfvpfi iiistltlvv wiiigfvdfg ivqkyfpsps khisqtevii
      961 rfafqtsitv lciacpcslg latptavmvg tgvaaqngvl ikggkplema hkiktvmfdk
     1021 tgtithgvpr vmrflllvdv atlslrkvla vvgtaeasse hplgvavtky ckeelgtetl
     1081 gystdfqavp gcgisckvsn vesilahrgp tahpigvgnp pigegtgpqt fsvlignrew
     1141 mrrngltiss disdamtdhe mkgqtailva idgvlcgmia iadavkpeaa laiytlksmg
     1201 vdvalitgdn rktaraiatq vginkvfaev lpshkvakvq elqnkgkkva mvgdgvndsp
     1261 alaqadvgia igtgtdvaie aadvvlirnd lldvvasihl skrtvrrirv nlvlaliynm
     1321 vgipiaagvf mpigivlqpw mgsaamaass vsvvlsslql kcyrkpdler yeaqahgrmk
     1381 plsasqvsvh vgmddrrrds pratpwdqvs yvsqvslssl tsdrlsrhgg maedggdkws
     1441 lllsdrdeeq ci
//
LOCUS       NP_001019441            1130 aa            linear   ROD 27-APR-2025
DEFINITION  proline-, glutamic acid- and leucine-rich protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001019441 XP_340832
VERSION     NP_001019441.2
DBSOURCE    REFSEQ: accession NM_001024270.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Raman,N., Weir,E. and Muller,S.
  TITLE     The AAA ATPase MDN1 Acts as a SUMO-Targeted Regulator in Mammalian
            Pre-ribosome Remodeling
  JOURNAL   Mol Cell 64 (3), 607-615 (2016)
   PUBMED   27814492
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Wang,J., Qiang,Z., Song,S., Shi,L., Ma,C., Tan,X., Yin,D. and
            Niu,Z.
  TITLE     Temporal expression of Pelp1 during proliferation and osteogenic
            differentiation of rat bone marrow mesenchymal stem cells
  JOURNAL   PLoS One 8 (10), e75477 (2013)
   PUBMED   24146754
  REMARK    GeneRIF: Pelp1 may be a key regulator of proliferation and
            osteogenic differentiation of bone marrow mesenchymal stem cells.
            Erratum:[PLoS One. 2013;8(12).
            doi:10.1371/annotation/5fa9cfb4-9964-4586-845d-d8205f318d68]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Wang,J., Zhu,Q., Song,S., Dong,J., Shi,L., Tao,R., Ding,Y. and
            Hong,B.
  TITLE     Increased PELP1 expression in rat periodontal ligament tissue in
            response to estrogens treatment
  JOURNAL   J Mol Histol 44 (3), 347-356 (2013)
   PUBMED   23436000
  REMARK    GeneRIF: Estradiol treatment of PDLFCs induced PELP1 protein level
            compared to untreated cells.
REFERENCE   4  (residues 1 to 1130)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 1130)
  AUTHORS   Gururaj,A.E., Peng,S., Vadlamudi,R.K. and Kumar,R.
  TITLE     Estrogen induces expression of BCAS3, a novel estrogen
            receptor-alpha coactivator, through proline-, glutamic acid-, and
            leucine-rich protein-1 (PELP1)
  JOURNAL   Mol Endocrinol 21 (8), 1847-1860 (2007)
   PUBMED   17505058
  REMARK    Erratum:[Mol Endocrinol. 2013 May;27(5):862]
REFERENCE   6  (residues 1 to 1130)
  AUTHORS   Khan,M.M., Hadman,M., Wakade,C., De Sevilla,L.M., Dhandapani,K.M.,
            Mahesh,V.B., Vadlamudi,R.K. and Brann,D.W.
  TITLE     Cloning, expression, and localization of MNAR/PELP1 in rodent
            brain: colocalization in estrogen receptor-alpha- but not in
            gonadotropin-releasing hormone-positive neurons
  JOURNAL   Endocrinology 146 (12), 5215-5227 (2005)
   PUBMED   16141397
  REMARK    GeneRIF: MNAR/PELP1 is expressed in key neural tissues of the rat
            brain that are known targets of steroid action; its expression is
            primarily neuronal; and MNAR/PELP1-ir is strongly colocalized in
            ER-alpha, but not GnRH neurons in rodent brain.
REFERENCE   7  (residues 1 to 1130)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC101890.1.
            
            On Sep 25, 2005 this sequence version replaced NP_001019441.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101890.1, AY970831.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1130
                     /product="proline-, glutamic acid- and leucine-rich
                     protein 1"
                     /note="proline-, glutamic acid-, leucine-rich protein 1;
                     modulator of non-genomic activity of estrogen receptor;
                     modulator of nongenomic activity of estrogen receptor;
                     proline, glutamic acid and leucine rich protein 1"
                     /calculated_mol_wt=119026
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          2..80
                     /region_name="Required for modulation of ESR1
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBD5; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          33..37
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          65..227
                     /region_name="RIX1"
                     /note="rRNA processing/ribosome biogenesis; pfam08167"
                     /db_xref="CDD:429855"
     Region          69..73
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          111..115
                     /region_name="LXXLL motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          121..189
                     /region_name="Required for modulation of ESR1
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          155..159
                     /region_name="LXXLL motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          177..181
                     /region_name="LXXLL motif 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          264..268
                     /region_name="LXXLL motif 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          271..275
                     /region_name="LXXLL motif 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          365..369
                     /region_name="LXXLL motif 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          424..475
                     /region_name="NUC202"
                     /note="NUC202 domain; pfam08166"
                     /db_xref="CDD:149302"
     Region          460..464
                     /region_name="LXXLL motif 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          580..584
                     /region_name="LXXLL motif 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          585..589
                     /region_name="LXXLL motif 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          <609..>638
                     /region_name="NUC202"
                     /note="NUC202 domain; pfam08166"
                     /db_xref="CDD:149302"
     Region          639..773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          <669..775
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBD5; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          785..1130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q56B11.2)"
     Region          <994..1122
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IZL8; propagated from
                     UniProtKB/Swiss-Prot (Q56B11.2)"
     CDS             1..1130
                     /gene="Pelp1"
                     /gene_synonym="RGD1306320"
                     /coded_by="NM_001024270.2:3..3395"
                     /db_xref="GeneID:360552"
                     /db_xref="RGD:1306320"
ORIGIN      
        1 maaavlsgpt tgspagapgg pgglsaagsg prlrlllles vsgllqprtg shvapvhppi
       61 qwapylpglm cllrlhgtag gaqnlsalga lvnlsnahls siktrfeglc llsllvgesp
      121 telfqqhcvs wlrsiqqvlq sqdspptmel availrdllr yasqlptlfr distnhlpgl
      181 ltsllglrpe ceqsalegmk acvtyfprac gflkgklasf flsrldslnp qlqqlacecy
      241 srlpslgagf sqglkhtenw eqelhsllts lhsllgslfe etetapvqse gpgvemllsp
      301 seddnthvll qlwqrfsgla rclglmlsse fgapvsvpvq eildlicril gisskninll
      361 gdgplrllll pslhlealdl lsalilacgg rllrfgalis rllpqvlntw stgrdalapg
      421 qerpystirt kvyailelwv qvcgasagml qggasgeall thllsdispp adalklcstr
      481 gssdgglqsg kpsapkklkl dmgealapps qrkgdrnans dvcaaalrgl srtilmcgpl
      541 vkeethrrlh dlvlplvmsv qqgevlgssp ynssccrlel yrlllallla psprcpppls
      601 calkafslgq wedslevssf csealvtcsa lthprvpplq ssgpacptpa pvpppeapss
      661 frapafhtpg pmpsigalps pgpvpsagpi ptvgsmssag svpstgpvps rpgppatanh
      721 lglavpglvs vpprllpgse nhragsgedp vlapsgtppp sippdetfgg rvprpafvhy
      781 dkeeasdvei slesdsddsv vivpeglpsl ppppsgtppp vaptgpptas ppvpakedse
      841 elpatpgplp ppppppppvs gpvtlpppql vpegtpgggg ptameedltv ininssdeee
      901 eeeeeeeeed edeeeedfee eeedeeeyfe eeeeeeefee efeeeegele eeeeeeeeel
      961 eevedvefgs ageveeggpp pptlppalpp tdspkvqpea epepglllev eepgaedgpg
     1021 peiaptlape vlpsqeever egesptagpp qelveeessa pptlleegte gggdkvpppp
     1081 etpaqeemet eteasapqgk eqddtaamla dfidcppdde kpppatepds
//
LOCUS       NP_001007753             498 aa            linear   ROD 27-APR-2025
DEFINITION  meiosis-specific nuclear structural protein 1 [Rattus norvegicus].
ACCESSION   NP_001007753 XP_343426
VERSION     NP_001007753.1
DBSOURCE    REFSEQ: accession NM_001007752.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Zhou,J., Yang,F., Leu,N.A. and Wang,P.J.
  TITLE     MNS1 is essential for spermiogenesis and motile ciliary functions
            in mice
  JOURNAL   PLoS Genet 8 (3), e1002516 (2012)
   PUBMED   22396656
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Furukawa,K., Inagaki,H., Naruge,T., Tabata,S., Tomida,T.,
            Yamaguchi,A., Yoshikuni,M., Nagahama,Y. and Hotta,Y.
  TITLE     cDNA cloning and functional characterization of a meiosis-specific
            protein (MNS1) with apparent nuclear association
  JOURNAL   Chromosome Res 2 (2), 99-113 (1994)
   PUBMED   8032679
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079390.1.
            
            On Nov 29, 2004 this sequence version replaced XP_343426.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079390.1, SRR8487227.87753.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132266, SAMD00132280
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..498
                     /product="meiosis-specific nuclear structural protein 1"
                     /calculated_mol_wt=61109
     Region          1..314
                     /region_name="Interaction with BBOF1.
                     /evidence=ECO:0000250|UniProtKB:Q61884"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXQ8.1)"
     Region          114..454
                     /region_name="TPH"
                     /note="Trichohyalin-plectin-homology domain; pfam13868"
                     /db_xref="CDD:464007"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61884; propagated from
                     UniProtKB/Swiss-Prot (Q6AXQ8.1)"
     CDS             1..498
                     /gene="Mns1"
                     /coded_by="NM_001007752.1:132..1628"
                     /db_xref="GeneID:363093"
                     /db_xref="RGD:1549718"
ORIGIN      
        1 mankkramsf sekhqqlvde nfrkslhvqv lnklerqakn qvvqnender verqrflrvl
       61 qneqfeldme eavqkaeenk rmrdrqleqe erlanelarl kheslkdekm rqqvrensie
      121 lreleqklka aymnkeraaq ivekdvikye qmkrdaeier immeehkrll keenvkqekr
      181 dkeraqyyvd lekqledqer rkqeayeqll keklmideiv rkiyeedqle rqqklekrna
      241 iqkyikefqr aqdlwrqkkr eemeeenrki lefakiqeqr egermarvqe seekrvqrqn
      301 lliqkleetl rqrddlervr qelyleeyae fiklkmkeev eqrlrkqrdr kqdfkdqmal
      361 revllqaake eeeafkkaml akfaeddrie lmnaqkqrmk qlehkravek lieerrnqfl
      421 adkqreleel qlqqrrqgci neiieeerlr llkehaskll gylpkgvfkk eddvdmlgee
      481 frkayqkkse vceekgss
//
LOCUS       NP_001009631             188 aa            linear   ROD 27-APR-2025
DEFINITION  calcium load-activated calcium channel [Rattus norvegicus].
ACCESSION   NP_001009631 XP_003751315 XP_008767944 XP_237903
VERSION     NP_001009631.1
DBSOURCE    REFSEQ: accession NM_001009631.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Wang,Q.C., Zheng,Q., Tan,H., Zhang,B., Li,X., Yang,Y., Yu,J.,
            Liu,Y., Chai,H., Wang,X., Sun,Z., Wang,J.Q., Zhu,S., Wang,F.,
            Yang,M., Guo,C., Wang,H., Zheng,Q., Li,Y., Chen,Q., Zhou,A. and
            Tang,T.S.
  TITLE     TMCO1 Is an ER Ca(2+) Load-Activated Ca(2+) Channel
  JOURNAL   Cell 165 (6), 1454-1466 (2016)
   PUBMED   27212239
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088319.1.
            
            On or before Aug 24, 2014 this sequence version replaced
            XP_008767944.1, XP_003751315.1, XP_237903.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088319.1, FQ117851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..188
                     /product="calcium load-activated calcium channel"
                     /note="transmembrane and coiled-coil domains protein 1;
                     meg-2-like protein; putative membrane protein; CLAC
                     channel; transmembrane and coiled-coil domain-containing
                     protein 1; GEL complex subunit TMCO1"
                     /calculated_mol_wt=21044
     Site            5..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0H4.1)"
     Region          8..165
                     /region_name="EMC3_TMCO1"
                     /note="Integral membrane protein EMC3/TMCO1-like;
                     pfam01956"
                     /db_xref="CDD:396507"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UM00; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H4.1)"
     Site            87..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0H4.1)"
     Site            141..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0H4.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UM00; propagated from
                     UniProtKB/Swiss-Prot (Q5I0H4.1)"
     CDS             1..188
                     /gene="Tmco1"
                     /coded_by="NM_001009631.1:50..616"
                     /db_xref="GeneID:289196"
                     /db_xref="RGD:1359178"
ORIGIN      
        1 mstmfadtll ivfisvctal laegitwvlv yrtdkykrlk aevekqskkl ekkketites
       61 agrqqkkkie rqeeklknnn rdlsmvrmks mfaigfcfta lmgmfnsifd grvvaklpft
      121 plsyiqglsh rnllgddttd csfiflyilc tmsirqniqk ilglapsraa tkqaggflgp
      181 pppsgkfs
//
LOCUS       NP_835194                440 aa            linear   ROD 27-APR-2025
DEFINITION  microtubule-associated tumor suppressor 1 homolog isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_835194 XP_001064538 XP_573915
VERSION     NP_835194.2
DBSOURCE    REFSEQ: accession NM_178093.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Sim,J., Kim,Y., Kim,H., Bang,S., Jee,S., Park,S., Shin,S.J. and
            Jang,K.
  TITLE     Loss of MTUS1 Expression Is Associated With Poor Prognosis in
            Patients With Gallbladder Carcinoma
  JOURNAL   In Vivo 34 (1), 125-132 (2020)
   PUBMED   31882471
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhao,T., Ding,X., Chang,B., Zhou,X. and Wang,A.
  TITLE     MTUS1/ATIP3a down-regulation is associated with enhanced migration,
            invasion and poor prognosis in salivary adenoid cystic carcinoma
  JOURNAL   BMC Cancer 15, 203 (2015)
   PUBMED   25885343
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Varghayee,N., Krezel,M.A., Rezmann,L., Chow,L., Frauman,A.G.,
            Louis,W.J. and Louis,S.N.
  TITLE     Function and expression of ATIP and its variants in cardiomyoblast
            cell line H9c2
  JOURNAL   J Renin Angiotensin Aldosterone Syst 16 (1), 79-91 (2015)
   PUBMED   23559668
  REMARK    GeneRIF: This is the first report to identify that ATIP may have a
            similar role in other disease states characterised by excessive
            growth
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Jing,F., Mogi,M., Min,L.J., Ohshima,K., Nakaoka,H., Tsukuda,K.,
            Wang,X., Iwanami,J. and Horiuchi,M.
  TITLE     Effect of angiotensin II type 2 receptor-interacting protein on
            adipose tissue function via modulation of macrophage polarization
  JOURNAL   PLoS One 8 (4), e60067 (2013)
   PUBMED   23565185
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Rodrigues-Ferreira,S., Di Tommaso,A., Dimitrov,A., Cazaubon,S.,
            Gruel,N., Colasson,H., Nicolas,A., Chaverot,N., Molinie,V.,
            Reyal,F., Sigal-Zafrani,B., Terris,B., Delattre,O., Radvanyi,F.,
            Perez,F., Vincent-Salomon,A. and Nahmias,C.
  TITLE     8p22 MTUS1 gene product ATIP3 is a novel anti-mitotic protein
            underexpressed in invasive breast carcinoma of poor prognosis
  JOURNAL   PLoS One 4 (10), e7239 (2009)
   PUBMED   19794912
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Li,J.M., Mogi,M., Tsukuda,K., Tomochika,H., Iwanami,J., Min,L.J.,
            Nahmias,C., Iwai,M. and Horiuchi,M.
  TITLE     Angiotensin II-induced neural differentiation via angiotensin II
            type 2 (AT2) receptor-MMS2 cascade involving interaction between
            AT2 receptor-interacting protein and Src homology 2
            domain-containing protein-tyrosine phosphatase 1
  JOURNAL   Mol Endocrinol 21 (2), 499-511 (2007)
   PUBMED   17068200
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Pils,D., Horak,P., Gleiss,A., Sax,C., Fabjani,G., Moebus,V.J.,
            Zielinski,C., Reinthaller,A., Zeillinger,R. and Krainer,M.
  TITLE     Five genes from chromosomal band 8p22 are significantly
            down-regulated in ovarian carcinoma: N33 and EFA6R have a potential
            impact on overall survival
  JOURNAL   Cancer 104 (11), 2417-2429 (2005)
   PUBMED   16270321
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Wruck,C.J., Funke-Kaiser,H., Pufe,T., Kusserow,H., Menk,M.,
            Schefe,J.H., Kruse,M.L., Stoll,M. and Unger,T.
  TITLE     Regulation of transport of the angiotensin AT2 receptor by a novel
            membrane-associated Golgi protein
  JOURNAL   Arterioscler Thromb Vasc Biol 25 (1), 57-64 (2005)
   PUBMED   15539617
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Seibold,S., Rudroff,C., Weber,M., Galle,J., Wanner,C. and Marx,M.
  TITLE     Identification of a new tumor suppressor gene located at chromosome
            8p21.3-22
  JOURNAL   FASEB J 17 (9), 1180-1182 (2003)
   PUBMED   12692079
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072537.1.
            
            On or before Feb 12, 2007 this sequence version replaced
            XP_573915.2, XP_001064538.1, NP_835194.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072537.1, BC166591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..440
                     /product="microtubule-associated tumor suppressor 1
                     homolog isoform 2"
                     /note="microtubule-associated tumor suppressor 1 homolog;
                     growth factor inhibitor; angiotensin-II type 2
                     receptor-interacting protein; transcription factor MTSG1;
                     microtubule associated tumor suppressor 1; mitochondrial
                     tumor suppressor 1"
                     /calculated_mol_wt=50614
     Region          <66..385
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Region          407..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ULD2; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5HZI1; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5HZI1; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6IMY1.1)"
     CDS             1..440
                     /gene="Mtus1"
                     /gene_synonym="Atip3b; ATIP4; Mtsg1"
                     /coded_by="NM_178093.2:233..1555"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:306487"
                     /db_xref="RGD:631381"
ORIGIN      
        1 mllspkfsls tihvrltakg llrnlrlpsg lrkntvifht vekgrqknpr slciqtqtap
       61 dvlstertle ladyktkcen qsgfilhlkq llscgntkfe altvviqhll sereealkqh
      121 ktlsqelvsl rgelvaasst ceklekarnd lqtayegfvq klnqqhqtdq telenrlkef
      181 ytaeceklqs iyieeaekyk tqlqeqfdnl naahettkle ieashsekve llkktyetsl
      241 seikksheme kkllenllne kqeslekqin dlksendaln erlkseeqkq lsrekanskn
      301 pqvmyleqel eslkavleik neklhqqdlk lmkmeklvdn nttlvdkltr fqqeneelka
      361 rmdrhmaisr qlsteqaalq eslekeskvn krlsmeneel lwklhngdlc spkrsptssa
      421 ipfqsprnsg sfsspsispr
//
LOCUS       NP_001005545             381 aa            linear   ROD 27-APR-2025
DEFINITION  MYG1 exonuclease precursor [Rattus norvegicus].
ACCESSION   NP_001005545 XP_217056
VERSION     NP_001005545.1
DBSOURCE    REFSEQ: accession NM_001005545.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Philips,M.A., Kingo,K., Karelson,M., Ratsep,R., Aunin,E.,
            Reimann,E., Reemann,P., Porosaar,O., Vikesa,J., Nielsen,F.C.,
            Vasar,E., Silm,H. and Koks,S.
  TITLE     Promoter polymorphism -119C/G in MYG1 (C12orf10) gene is related to
            vitiligo susceptibility and Arg4Gln affects mitochondrial entrance
            of Myg1
  JOURNAL   BMC Med Genet 11, 56 (2010)
   PUBMED   20377893
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Philips,M.A., Abramov,U., Lillevali,K., Luuk,H., Kurrikoff,K.,
            Raud,S., Plaas,M., Innos,J., Puussaar,T., Koks,S. and Vasar,E.
  TITLE     Myg1-deficient mice display alterations in stress-induced responses
            and reduction of sex-dependent behavioural differences
  JOURNAL   Behav Brain Res 207 (1), 182-195 (2010)
   PUBMED   19818808
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Philips,M.A., Vikesa,J., Luuk,H., Jonson,L., Lillevali,K.,
            Rehfeld,J.F., Vasar,E., Koks,S. and Nielsen,F.C.
  TITLE     Characterization of MYG1 gene and protein: subcellular distribution
            and function
  JOURNAL   Biol Cell 101 (6), 361-373 (2009)
   PUBMED   19014353
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082112.1.
            
            On Oct 8, 2004 this sequence version replaced XP_217056.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082112.1, FQ230067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..381
                     /product="MYG1 exonuclease precursor"
                     /note="UPF0160 protein MYG1, mitochondrial; melanocyte
                     proliferating gene 1"
                     /calculated_mol_wt=37589
     transit_peptide 1..47
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q641W2.1)"
                     /calculated_mol_wt=5318
     Region          46..366
                     /region_name="UPF0160"
                     /note="Uncharacterized protein family (UPF0160);
                     pfam03690"
                     /db_xref="CDD:461014"
     mat_peptide     48..381
                     /product="MYG1 exonuclease. /id=PRO_0000371227"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641W2.1)"
                     /calculated_mol_wt=37589
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9HB07; propagated from
                     UniProtKB/Swiss-Prot (Q641W2.1)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JK81; propagated from
                     UniProtKB/Swiss-Prot (Q641W2.1)"
     CDS             1..381
                     /gene="Myg1"
                     /gene_synonym="C12orf10"
                     /coded_by="NM_001005545.1:2..1147"
                     /db_xref="GeneID:300258"
                     /db_xref="RGD:1359237"
ORIGIN      
        1 mgrgflrgvl tllplrsvlq vqhcmlvsep dlppkrprnn lmapprigth ngtfhcdeal
       61 acallrllpe yrnaeivrtr dpeklalcdi vvdvggeynp qrhrydhhqr tftetmsslc
      121 pgkpwqtkls saglvylhfg hkllaqllgt seedsvvdti ydkmyenfve evdavdngis
      181 qwaegeprya ltttlsarvs rlnptwnqpd qdteagfrra mdlvqeeflq rlnfyqhswl
      241 paralveeal aqrfkvdssg eivelakggc pwkehlyhle selsptvait fviytdqagq
      301 wrvqcvpkep hsfqsrlplp epwrglrdea ldqvsgipgc ifvhasgfig ghhtregaln
      361 maratlaqrt apvplanavv q
//
LOCUS       NP_001103080             129 aa            linear   ROD 27-APR-2025
DEFINITION  histone H2A.J [Rattus norvegicus].
ACCESSION   NP_001103080 XP_001075643
VERSION     NP_001103080.1
DBSOURCE    REFSEQ: accession NM_001109610.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC157816.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001075643.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: EV762958.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q43"
     Protein         1..129
                     /product="histone H2A.J"
                     /note="histone H2A.J-like; H2A histone family, member J"
                     /calculated_mol_wt=13914
     Region          1..129
                     /region_name="PTZ00017"
                     /note="histone H2A; Provisional"
                     /db_xref="CDD:185399"
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A9UMV8.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1M2; propagated from
                     UniProtKB/Swiss-Prot (A9UMV8.1)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1M2; propagated from
                     UniProtKB/Swiss-Prot (A9UMV8.1)"
     Site            105
                     /site_type="methylation"
                     /note="N5-methylglutamine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (A9UMV8.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DCAF1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (A9UMV8.1)"
     CDS             1..129
                     /gene="H2aj"
                     /gene_synonym="H2a/j; H2afj"
                     /coded_by="NM_001109610.2:35..424"
                     /db_xref="GeneID:690795"
                     /db_xref="RGD:1592176"
ORIGIN      
        1 msgrgkqggk vrakaksrss raglqfpvgr vhrllrkgny aervgagapv ylaavleylt
       61 aeilelagna ardnkktrii prhlqlairn deelnkllgr vtiaqggvlp niqavllpkk
      121 tesqkvksk
//
LOCUS       NP_001014266             276 aa            linear   ROD 27-APR-2025
DEFINITION  NADH-cytochrome b5 reductase 2 [Rattus norvegicus].
ACCESSION   NP_001014266 XP_344946
VERSION     NP_001014266.1
DBSOURCE    REFSEQ: accession NM_001014244.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chen,J., Sun,Y., Chen,L. and Zhou,Y.
  TITLE     NADH-Cytochrome B5 reductase 2 suppresses retinal vascular
            dysfunction through regulation of vascular endothelial growth
            factor A in diabetic retinopathy
  JOURNAL   Exp Eye Res 222, 109186 (2022)
   PUBMED   35820466
  REMARK    GeneRIF: NADH-Cytochrome B5 reductase 2 suppresses retinal vascular
            dysfunction through regulation of vascular endothelial growth
            factor A in diabetic retinopathy.
REFERENCE   2  (residues 1 to 276)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Marohnic,C.C., Crowley,L.J., Davis,C.A., Smith,E.T. and Barber,M.J.
  TITLE     Cytochrome b5 reductase: role of the si-face residues, proline 92
            and tyrosine 93, in structure and catalysis
  JOURNAL   Biochemistry 44 (7), 2449-2461 (2005)
   PUBMED   15709757
  REMARK    GeneRIF: Changes in the nature of the side-chain constituents in
            the conserved residues, such as proline-92 and tyrosine-93, exert
            considerable influence on the flavin prosthetic group and
            significantly impact cytochrome B5 reductase turnover.
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Zhu,H., Qiu,H., Yoon,H.W., Huang,S. and Bunn,H.F.
  TITLE     Identification of a cytochrome b-type NAD(P)H oxidoreductase
            ubiquitously expressed in human cells
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 14742-14747 (1999)
   PUBMED   10611283
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079235.1.
            
            On Apr 20, 2005 this sequence version replaced XP_344946.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..276
                     /product="NADH-cytochrome b5 reductase 2"
                     /EC_number="1.6.2.2"
                     /note="b5R.2"
                     /calculated_mol_wt=31108
     Region          <13..276
                     /region_name="PLN02252"
                     /note="nitrate reductase [NADPH]"
                     /db_xref="CDD:215141"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (Q6AY12.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00387; propagated from
                     UniProtKB/Swiss-Prot (Q6AY12.1)"
     CDS             1..276
                     /gene="Cyb5r2"
                     /gene_synonym="RGD1308421"
                     /coded_by="NM_001014244.1:244..1074"
                     /db_xref="GeneID:365345"
                     /db_xref="RGD:1308421"
ORIGIN      
        1 msvkkkdlit lqdpeakypl pliekeqinh ntrrfrfglp spdhvlglpv gnyvhllaqi
       61 nnelvirayt pvssdddqgf vdliikiyfk nvhpkypegg kmtqylenmk igdtilfrgp
      121 tgrlfynepg tlliktdkts epekklvhhl gmiaggtgit pmlqlirhit kdtsdgtrms
      181 llfanqteed illrkeleev atthqnqfsl wytldrppsg weyssgfita dmikehlppp
      241 geatlilvcg pppliqeaah psleqlgytk dmifty
//
LOCUS       NP_001019429             898 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 574 [Rattus norvegicus].
ACCESSION   NP_001019429 XP_218459
VERSION     NP_001019429.1
DBSOURCE    REFSEQ: accession NM_001024258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC094953.1.
            
            On May 27, 2005 this sequence version replaced XP_218459.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094953.1, FQ170749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..898
                     /product="zinc finger protein 574"
                     /calculated_mol_wt=99224
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN55; propagated from
                     UniProtKB/Swiss-Prot (Q504L7.1)"
     Region          243..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q504L7.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN55; propagated from
                     UniProtKB/Swiss-Prot (Q504L7.1)"
     Region          312..332
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          339..359
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(344,346,348,350..351,354..355,358,372,374,378..379,
                     382..383,386,399,401,403,405..406,409..410,413)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          367..387
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          395..414
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          417..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q504L7.1)"
     Region          458..>492
                     /region_name="lambda-1"
                     /note="inner capsid protein lambda-1 or VP3; cd11674"
                     /db_xref="CDD:212564"
     Region          469..490
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(469,472,485,490)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:212564"
     Region          496..850
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          498..518
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(503,505,507,509..510,513..514,517,531,533,537..538,
                     541..542,545,559,561,563,565..566,569..570,573)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          526..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          554..574
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          582..602
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          610..631
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          639..656
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          691..735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q504L7.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN55; propagated from
                     UniProtKB/Swiss-Prot (Q504L7.1)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN55; propagated from
                     UniProtKB/Swiss-Prot (Q504L7.1)"
     Region          742..762
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(747,749,751,753..754,757..758,761,775,777,781..782,
                     785..786,789,803,805,807,809..810,813..814,817)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          770..790
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          798..818
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          826..846
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            834
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZN55; propagated from
                     UniProtKB/Swiss-Prot (Q504L7.1)"
     CDS             1..898
                     /gene="Zfp574"
                     /gene_synonym="Znf574"
                     /coded_by="NM_001024258.1:123..2819"
                     /db_xref="GeneID:308434"
                     /db_xref="RGD:1311420"
ORIGIN      
        1 mteeseetvl yiehryvcse cnqlygslee vlvhqnshvp qqhfelvgva dpgvtvatea
       61 tsgtglyqtl iqesqyqcle cgqlllspsq llehqelhlk mmapqeavpa epppkvppls
      121 sstihyecvd ckalfasqem wlshrqthlr atpnkapapv vlgspvvlgp pvgqarvave
      181 hsyrkaeegg egaavpsvaa atemvtevel llykcsecsq lfqmpadfle hqathfpapv
      241 peaeepatqq etlvpsptea avsqpdplpa sdhsyelrne lrngeamgrd rrgrkprrss
      301 sgesgatqel fcsacdqifl sphqlqqhlr shregvfkcp lcsrvfpsps sldqhlgdhs
      361 seshflcvdc glafgteall lahrrahtpn plhscpcgkt fvnltkflyh rrthgaggvp
      421 lpttpvppee paisfpepap aetgeleape lpvseessae paapgtyrcl lcsrefskal
      481 qltrhqrfvh rlerrhkcsi cgkmfkkksh vrnhlrthtg erpfpcpdcs kpfnspanla
      541 rhrlthtger pyrcgdcgka ftqsstlrqh rlvhaqhfpy rcqecgvrfh rpyrllmhry
      601 hhtgeypykc recprsfllr rllevhqlvv hagrqphrcp scgaafpssl rlrehrcaaa
      661 aaqaprrfec gtcgkkvgsa arlqaheaah aaagpgevla keppapraar atrtpvapsp
      721 talggttsaa paaparrrgl ecseckklfs tetslqvhrr ihtgerpypc pdcgkafrqs
      781 thlkdhrrlh tgerpfacev cgkafaismr laehrrihtg erpyscpdcg ksyrsfsnlw
      841 khrkthqqqh qaavrqqlae aeaavglavm etavealplv eaieiyplae adgvqisg
//
LOCUS       NP_001019540             127 aa            linear   ROD 27-APR-2025
DEFINITION  protein yippee-like 4 [Rattus norvegicus].
ACCESSION   NP_001019540 XP_578138
VERSION     NP_001019540.1
DBSOURCE    REFSEQ: accession NM_001024369.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083749.1.
            
            On May 27, 2005 this sequence version replaced XP_578138.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083749.1, CO402835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..127
                     /product="protein yippee-like 4"
                     /calculated_mol_wt=14184
     Region          28..118
                     /region_name="RLR_C_like"
                     /note="C-terminal domain of Retinoic acid-inducible gene
                     (RIG)-I-like Receptors, Cereblon (CRBN), and similar
                     protein domains; cl13152"
                     /db_xref="CDD:472430"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5XID5.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5XID5.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5XID5.1)"
     CDS             1..127
                     /gene="Ypel4"
                     /coded_by="NM_001024369.1:360..743"
                     /db_xref="GeneID:502643"
                     /db_xref="RGD:1560142"
ORIGIN      
        1 mpscdpgpap aclptktfrs ylprchrtys cvhcrahlak hdelisksfq gshgraylfn
       61 svvnvgcgpa eqrllltglh svadifcesc kttlgwkyeq afetsqkyke gkyiiemshm
      121 vkdngwd
//
LOCUS       NP_077358                479 aa            linear   ROD 27-APR-2025
DEFINITION  heparin cofactor 2 precursor [Rattus norvegicus].
ACCESSION   NP_077358
VERSION     NP_077358.1
DBSOURCE    REFSEQ: accession NM_024382.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Noda,A., Wada,H., Kusiya,F., Sakakura,M., Onishi,K., Nakatani,K.,
            Gabazza,E.C., Asahara,N., Tsukada,M., Nobori,T. and Shiku,H.
  TITLE     Plasma levels of heparin cofactor II (HCII) and thrombin-HCII
            complex in patients with disseminated intravascular coagulation
  JOURNAL   Clin Appl Thromb Hemost 8 (3), 265-271 (2002)
   PUBMED   12361205
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Lind,B. and Thorsen,S.
  TITLE     A novel missense mutation in the human plasmin inhibitor
            (alpha2-antiplasmin) gene associated with a bleeding tendency
  JOURNAL   Br J Haematol 107 (2), 317-322 (1999)
   PUBMED   10583218
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Robbie,L.A., Booth,N.A., Brown,A.J. and Bennett,B.
  TITLE     Inhibitors of fibrinolysis are elevated in atherosclerotic plaque
  JOURNAL   Arterioscler Thromb Vasc Biol 16 (4), 539-545 (1996)
   PUBMED   8624776
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Kondo,S., Tokunaga,F., Kario,K., Matsuo,T. and Koide,T.
  TITLE     Molecular and cellular basis for type I heparin cofactor II
            deficiency (heparin cofactor II Awaji)
  JOURNAL   Blood 87 (3), 1006-1012 (1996)
   PUBMED   8562924
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Westrup,D. and Ragg,H.
  TITLE     Secondary thrombin-binding site, glycosaminoglycan binding domain
            and reactive center region of leuserpin-2 are strongly conserved in
            mammalian species
  JOURNAL   Biochim Biophys Acta 1217 (1), 90-92 (1994)
   PUBMED   8286422
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X74549.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X74549.1, BC091145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..479
                     /product="heparin cofactor 2 precursor"
                     /note="heparin cofactor 2; HC-II; heparin cofactor II;
                     protease inhibitor leuserpin-2; serpin D1; serine (or
                     cysteine) peptidase inhibitor, clade D, member 1; serine
                     (or cysteine) proteinase inhibitor, clade D, member 1;
                     leuserpin 2; serpin peptidase inhibitor, clade D (heparin
                     cofactor), member 1"
                     /calculated_mol_wt=52546
     sig_peptide     1..18
                     /calculated_mol_wt=2024
     mat_peptide     19..479
                     /product="heparin cofactor 2"
                     /calculated_mol_wt=52546
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64268.1)"
     Region          33..479
                     /region_name="serpinD1_HCF2"
                     /note="serpin family D member 1, Heparin cofactor II;
                     cd02047"
                     /db_xref="CDD:381004"
     Region          55..79
                     /region_name="2 X 11 AA approximate repeats, Asp/Glu-rich
                     (acidic) (hirudin-like)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64268.1)"
     Site            order(57..62,64,67..68,71,285..289,307,341..342,368,
                     438..446,448,453)
                     /site_type="other"
                     /note="thrombin binding site [polypeptide binding]"
                     /db_xref="CDD:381004"
     Site            61
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q64268.1)"
     Site            74
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q64268.1)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64268.1)"
     Region          172..192
                     /region_name="Glycosaminoglycan-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64268.1)"
     Site            367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64268.1)"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64268.1)"
     Site            429..454
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381004"
     Site            443..444
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q64268.1)"
     CDS             1..479
                     /gene="Serpind1"
                     /gene_synonym="rls2var1"
                     /coded_by="NM_024382.1:120..1559"
                     /db_xref="GeneID:79224"
                     /db_xref="RGD:619854"
ORIGIN      
        1 mkhpaytlll slimsmcags kglaeqltke nltvsllppn fhkentvtnd wipegeeddd
       61 yldlekllse dddyiyvvda vsptdsessa gnilqlfqgk sriqrlniln akfafnlyrv
      121 lkdqatssdn ifiapvgist amgmislglr getheevhsv lhfkdfvnas skyevttihn
      181 lfrklthrlf rrnfgytlqs vndlyiqkqf piredfkaam refyfaeaqe adfsdpafis
      241 kanshilklt kglikealen tdsatqmmil nciyfkgawm nkfpvemthn hnfrlnerev
      301 vkvsmmqtkg nflaandqel dcdilqleyv ggismlivip rklsgmktle aqltpqvver
      361 wqksmtnrtr evllpkfkle knynlvevlk smgitklfnk ngnmsgisdq riiidlfkhq
      421 stitvneegt qaaavttvgf mplstqvrft vdrpflflvy ehrtscllfm grvanpaks
//
LOCUS       NP_446015                427 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-dependent RNA helicase DDX39A [Rattus norvegicus].
ACCESSION   NP_446015
VERSION     NP_446015.2
DBSOURCE    REFSEQ: accession NM_053563.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Wisskirchen,C., Ludersdorfer,T.H., Muller,D.A., Moritz,E. and
            Pavlovic,J.
  TITLE     Interferon-induced antiviral protein MxA interacts with the
            cellular RNA helicases UAP56 and URH49
  JOURNAL   J Biol Chem 286 (40), 34743-34751 (2011)
   PUBMED   21859714
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Kim,D., Kim,S.H., Cho,S.H., Shin,K. and Kim,S.
  TITLE     SOCS3 suppresses the expression of IL-4 cytokine by inhibiting the
            phosphorylation of c-Jun through the ERK signaling pathway in rat
            mast cell line RBL-2H3
  JOURNAL   Mol Immunol 48 (5), 776-781 (2011)
   PUBMED   21168220
  REMARK    GeneRIF: Overexpression of SOCS3 was found to reduce the level of
            calcium ionophore-induced phosphorylation of ERK1/2 and c-Jun
            transcription factor
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Dufu,K., Livingstone,M.J., Seebacher,J., Gygi,S.P., Wilson,S.A. and
            Reed,R.
  TITLE     ATP is required for interactions between UAP56 and two conserved
            mRNA export proteins, Aly and CIP29, to assemble the TREX complex
  JOURNAL   Genes Dev 24 (18), 2043-2053 (2010)
   PUBMED   20844015
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Allcock,R., Dolecki,K.J., Boodhoo,A., Abdul Khalil,A., Wong,A.M.
            and Price,P.
  TITLE     Genomic sequence and expression profile of murine Bat1a and Nfkbil1
  JOURNAL   DNA Seq 17 (4), 292-299 (2006)
   PUBMED   17312949
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Pryor,A., Tung,L., Yang,Z., Kapadia,F., Chang,T.H. and Johnson,L.F.
  TITLE     Growth-regulated expression and G0-specific turnover of the mRNA
            that encodes URH49, a mammalian DExH/D box protein that is highly
            related to the mRNA export protein UAP56
  JOURNAL   Nucleic Acids Res 32 (6), 1857-1865 (2004)
   PUBMED   15047853
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Peelman,L.J., Chardon,P., Nunes,M., Renard,C., Geffrotin,C.,
            Vaiman,M., Van Zeveren,A., Coppieters,W., van de Weghe,A.,
            Bouquet,Y. et al.
  TITLE     The BAT1 gene in the MHC encodes an evolutionarily conserved
            putative nuclear RNA helicase of the DEAD family
  JOURNAL   Genomics 26 (2), 210-218 (1995)
   PUBMED   7601445
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086328.1.
            
            On Nov 22, 2004 this sequence version replaced NP_446015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..427
                     /product="ATP-dependent RNA helicase DDX39A"
                     /EC_number="3.6.4.13"
                     /note="ATP-dependent RNA helicase DDX39; DEAD box protein
                     39; nuclear RNA helicase, DECD variant of DEAD box family;
                     DEAD (Asp-Glu-Ala-Asp) box polypeptide 39; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 39A; DEAD-box helicase
                     39A"
                     /calculated_mol_wt=48979
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U216.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q5U216.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q5U216.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q5U216.1)"
     Region          43..250
                     /region_name="DEADc_DDX39"
                     /note="DEAD-box helicase domain of DEAD box protein 39;
                     cd17950"
                     /db_xref="CDD:350708"
     Region          44..72
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U216.1)"
     Site            order(46,64,66..68,71,90..96,195..196)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350708"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q5U216.1)"
     Region          195..198
                     /region_name="DECD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U216.1)"
     Region          261..390
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(349,351,376,379..380)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00148; propagated from
                     UniProtKB/Swiss-Prot (Q5U216.1)"
     CDS             1..427
                     /gene="Ddx39a"
                     /gene_synonym="Ddx39; Ddxl"
                     /coded_by="NM_053563.2:304..1587"
                     /db_xref="GeneID:89827"
                     /db_xref="RGD:619920"
ORIGIN      
        1 maeqdvenel ldydedeepq vpqestpapp kkdvkgsyvs ihssgfrdfl lkpellraiv
       61 dcgfehpsev qhecipqail gmdvlcqaks gmgktavfvl atlqqiepin gqvsvlvmch
      121 trelafqisk eyerfskymp svkvsvffgg lsikkdedvl kkncphvvvg tpgrilalvr
      181 srslnlrnvk hfvldecdkm leqldmrrdv qeifrltphe kqcmmfsatl skeirpvcrk
      241 fmqdpmevfv ddetkltlhg lqqyyvklkd seknrklfdl ldvlefnqvv ifvksvqrcm
      301 alaqllveqn fpaiaihrgm aqeerlsryq qfkdfqrril vatnlfgrgm diervnivfn
      361 ydmpedsdty lhrvaragrf gtkglavtfv sdendakiln dvqdrfevnv aelpeeidis
      421 tyieqsr
//
LOCUS       NP_001012347             257 aa            linear   ROD 27-APR-2025
DEFINITION  regulator of G-protein signaling 7-binding protein [Rattus
            norvegicus].
ACCESSION   NP_001012347 XP_215473
VERSION     NP_001012347.1
DBSOURCE    REFSEQ: accession NM_001012347.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aguado,C., Orlandi,C., Fajardo-Serrano,A., Gil-Minguez,M.,
            Martemyanov,K.A. and Lujan,R.
  TITLE     Cellular and Subcellular Localization of the RGS7/Gbeta5/R7BP
            Complex in the Cerebellar Cortex
  JOURNAL   Front Neuroanat 10, 114 (2016)
   PUBMED   27965545
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Ostrovskaya,O., Xie,K., Masuho,I., Fajardo-Serrano,A., Lujan,R.,
            Wickman,K. and Martemyanov,K.A.
  TITLE     RGS7/Gbeta5/R7BP complex regulates synaptic plasticity and memory
            by modulating hippocampal GABABR-GIRK signaling
  JOURNAL   Elife 3, e02053 (2014)
   PUBMED   24755289
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Jia,L., Linder,M.E. and Blumer,K.J.
  TITLE     Gi/o signaling and the palmitoyltransferase DHHC2 regulate
            palmitate cycling and shuttling of RGS7 family-binding protein
  JOURNAL   J Biol Chem 286 (15), 13695-13703 (2011)
   PUBMED   21343290
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Beaulieu,J.M. and Gainetdinov,R.R.
  TITLE     The physiology, signaling, and pharmacology of dopamine receptors
  JOURNAL   Pharmacol Rev 63 (1), 182-217 (2011)
   PUBMED   21303898
  REMARK    Review article
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Grabowska,D., Jayaraman,M., Kaltenbronn,K.M., Sandiford,S.L.,
            Wang,Q., Jenkins,S., Slepak,V.Z., Smith,Y. and Blumer,K.J.
  TITLE     Postnatal induction and localization of R7BP, a membrane-anchoring
            protein for regulator of G protein signaling 7 family-Gbeta5
            complexes in brain
  JOURNAL   Neuroscience 151 (4), 969-982 (2008)
   PUBMED   18248908
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Anderson,G.R., Lujan,R., Semenov,A., Pravetoni,M., Posokhova,E.N.,
            Song,J.H., Uversky,V., Chen,C.K., Wickman,K. and Martemyanov,K.A.
  TITLE     Expression and localization of RGS9-2/G 5/R7BP complex in vivo is
            set by dynamic control of its constitutive degradation by cellular
            cysteine proteases
  JOURNAL   J Neurosci 27 (51), 14117-14127 (2007)
   PUBMED   18094251
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Drenan,R.M., Doupnik,C.A., Boyle,M.P., Muglia,L.J., Huettner,J.E.,
            Linder,M.E. and Blumer,K.J.
  TITLE     Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP,
            a novel membrane anchor for the RGS7 family
  JOURNAL   J Cell Biol 169 (4), 623-633 (2005)
   PUBMED   15897264
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089977.1.
            
            On Feb 18, 2005 this sequence version replaced XP_215473.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089977.1, SRR8487226.71706.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..257
                     /product="regulator of G-protein signaling 7-binding
                     protein"
                     /note="R7 binding protein; R7 family-binding protein"
                     /calculated_mol_wt=28835
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH8.1)"
     Region          172..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH8.1)"
     Region          242..247
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH8.1)"
     CDS             1..257
                     /gene="Rgs7bp"
                     /gene_synonym="R7bp; RGD1309360"
                     /coded_by="NM_001012347.1:374..1147"
                     /db_xref="GeneID:294715"
                     /db_xref="RGD:1309360"
ORIGIN      
        1 mssapngrkk rpsrstrssi fqiskpplqs gdwerrgsgs esahktqral ddckmlvqef
       61 ntqvalyrel visigdvsvs cpslraemhk trtkgcemar qahqklaais gpedgeihpe
      121 icrlyiqlqc clemytteml ksicllgslq fhrkgkeasg gaksldskie enaetpaled
      181 slsspldsqq qswqvatdie nterdmremk nllsklretm plplknqdds sllnltpypm
      241 vrrrkrrffg lcclvss
//
LOCUS       NP_001094477             552 aa            linear   ROD 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 6A [Rattus norvegicus].
ACCESSION   NP_001094477 XP_001065121 XP_001065178
VERSION     NP_001094477.1
DBSOURCE    REFSEQ: accession NM_001101007.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Paine,M.L., Gibbins,J.R., Chew,K.E., Demetriou,A. and Kefford,R.F.
  TITLE     Loss of keratin expression in anaplastic carcinoma cells due to
            posttranscriptional down-regulation acting in trans
  JOURNAL   Cancer Res 52 (23), 6603-6611 (1992)
   PUBMED   1384967
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099121.1.
            
            On or before Aug 13, 2007 this sequence version replaced
            XP_001065178.1, XP_001065121.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099121.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132281,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..552
                     /product="keratin, type II cytoskeletal 6A"
                     /note="keratin K6; K6a keratin; cytokeratin-6A; type-II
                     keratin Kb6; keratin, type II cytoskeletal 5; keratin,
                     type II cytoskeletal 5-like"
                     /calculated_mol_wt=59118
     Region          1..151
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          15..148
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          151..464
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          152..187
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          188..206
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          207..298
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          299..322
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          323..461
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Site            403
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q4FZU2.1)"
     Region          462..552
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     Region          524..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU2.1)"
     CDS             1..552
                     /gene="Krt6c"
                     /gene_synonym="CK-6A; Krt6a"
                     /coded_by="NM_001101007.1:34..1692"
                     /db_xref="GeneID:683313"
                     /db_xref="RGD:1588056"
ORIGIN      
        1 mstktvirsq tshrgfsags arlpglnrsg fssvsvcrsr gsggsravcg gagfgsrslc
       61 gvgssqrisi gggscgiggg yggrfggsfg ygggaggslg fgagagfggg yggagfpvcp
      121 pggiqevtin qslltpmnlq idptiqrvrt eereqiktln nkfasfidkv rfleqqnkvl
      181 dtkwallqeq gtktvrqgle tlfeqyindl rkeldnilgq rgrldselrn mqgtvedyks
      241 kyedeinrrt aaenefvtlk kdvdaaymnk velqakadsl tdeinflral yeaelsqmqt
      301 hisdtsvvls mdnnrsldld siiaevkaqy eeiakrsrae aeswyqtkye elqitagrhg
      361 ddlrntkqei seinrmiqrl rseidhvkkq ianlqaaiae aeqrgemalk dargklegle
      421 dalqkakqdm arllkeyqdl mnvklaldve iatyrtlleg eecrlngegv gpvnisvvqs
      481 tvsssygsag gasssiglgg sssfsyggsh sigggfsags grgissglss sggssstiky
      541 tttsstrksy rp
//
LOCUS       NP_446148                156 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 3 [Rattus norvegicus].
ACCESSION   NP_446148 XP_001063211 XP_343774
VERSION     NP_446148.1
DBSOURCE    REFSEQ: accession NM_053696.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Lin,P., Lin,C. and Diao,L.
  TITLE     RBM3 Ameliorates Acute Brain Injury-induced Inflammation and
            Oxidative Stress by Stabilizing GAS6 mRNA Through Nrf2 Signaling
            Pathway
  JOURNAL   Neuroscience 547, 74-87 (2024)
   PUBMED   38555015
  REMARK    GeneRIF: RBM3 Ameliorates Acute Brain Injury-induced Inflammation
            and Oxidative Stress by Stabilizing GAS6 mRNA Through Nrf2
            Signaling Pathway.
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Sertel,S.M., von Elling-Tammen,M.S. and Rizzoli,S.O.
  TITLE     The mRNA-Binding Protein RBM3 Regulates Activity Patterns and Local
            Synaptic Translation in Cultured Hippocampal Neurons
  JOURNAL   J Neurosci 41 (6), 1157-1173 (2021)
   PUBMED   33310754
  REMARK    GeneRIF: The mRNA-Binding Protein RBM3 Regulates Activity Patterns
            and Local Synaptic Translation in Cultured Hippocampal Neurons.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Van Pelt,D.W., Confides,A.L., Judge,A.R., Vanderklish,P.W. and
            Dupont-Versteegden,E.E.
  TITLE     Cold shock protein RBM3 attenuates atrophy and induces hypertrophy
            in skeletal muscle
  JOURNAL   J Muscle Res Cell Motil 39 (1-2), 35-40 (2018)
   PUBMED   30051360
  REMARK    GeneRIF: Overexpression of RBM3 also attenuated muscle atrophy in
            rat soleus muscle undergoing disuse atrophy. These findings provide
            direct evidence for a novel role of RBM3 in inducing hypertrophy as
            well as attenuating atrophy.
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Jackson,T.C., Manole,M.D., Kotermanski,S.E., Jackson,E.K.,
            Clark,R.S. and Kochanek,P.M.
  TITLE     Cold stress protein RBM3 responds to temperature change in an
            ultra-sensitive manner in young neurons
  JOURNAL   Neuroscience 305, 268-278 (2015)
   PUBMED   26265550
  REMARK    GeneRIF: This study showed that a 1 degrees C reduction in
            temperature can induce pleiotropic biochemical changes by
            upregulating global protein synthesis in neurons.
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Cui,Z., Zhang,J., Bao,G., Xu,G., Sun,Y., Wang,L., Chen,J., Jin,H.,
            Liu,J., Yang,L., Feng,G. and Li,W.
  TITLE     Spatiotemporal profile and essential role of RBM3 expression after
            spinal cord injury in adult rats
  JOURNAL   J Mol Neurosci 54 (2), 252-263 (2014)
   PUBMED   24668366
  REMARK    GeneRIF: RBM3 expression was increased in astrocytes after spinal
            cord injury. RBM3 regulated proliferation of astrocytes in vitro.
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Pilotte,J., Cunningham,B.A., Edelman,G.M. and Vanderklish,P.W.
  TITLE     Developmentally regulated expression of the cold-inducible
            RNA-binding motif protein 3 in euthermic rat brain
  JOURNAL   Brain Res 1258, 12-24 (2009)
   PUBMED   19150436
  REMARK    GeneRIF: These results indicate that expression of RBM3 is
            dynamically regulated in the developing brain and suggest that it
            contributes to translation-dependent processes underlying
            proliferation, differentiation, and plasticity.
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Dupont-Versteegden,E.E., Nagarajan,R., Beggs,M.L., Bearden,E.D.,
            Simpson,P.M. and Peterson,C.A.
  TITLE     Identification of cold-shock protein RBM3 as a possible regulator
            of skeletal muscle size through expression profiling
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 295 (4), R1263-R1273 (2008)
   PUBMED   18753264
  REMARK    GeneRIF: Aa cold-shock response may be part of a compensatory
            mechanism in muscles undergoing atrophy to preserve remaining
            muscle mass. RBM3, which was induced most highly in atrophic muscle
            from old rats, may be a therapeutic target to prevent muscle loss.
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Smart,F., Aschrafi,A., Atkins,A., Owens,G.C., Pilotte,J.,
            Cunningham,B.A. and Vanderklish,P.W.
  TITLE     Two isoforms of the cold-inducible mRNA-binding protein RBM3
            localize to dendrites and promote translation
  JOURNAL   J Neurochem 101 (5), 1367-1379 (2007)
   PUBMED   17403028
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Dresios,J., Aschrafi,A., Owens,G.C., Vanderklish,P.W., Edelman,G.M.
            and Mauro,V.P.
  TITLE     Cold stress-induced protein Rbm3 binds 60S ribosomal subunits,
            alters microRNA levels, and enhances global protein synthesis
  JOURNAL   Proc Natl Acad Sci U S A 102 (6), 1865-1870 (2005)
   PUBMED   15684048
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY319481.1, AF355190.1, DN933310.1 and CA340698.1.
            
            On or before Jun 5, 2008 this sequence version replaced
            XP_343774.2, XP_001063211.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ235187.1, FQ232482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..156
                     /product="RNA-binding protein 3"
                     /note="putative RNA-binding protein 3; RNA binding motif
                     (RNP1, RRM) protein 3"
                     /calculated_mol_wt=16852
     Region          6..85
                     /region_name="RRM_CIRBP_RBM3"
                     /note="RNA recognition motif (RRM) found in cold inducible
                     RNA binding protein (CIRBP), RNA binding motif protein 3
                     (RBM3) and similar proteins; cd12449"
                     /db_xref="CDD:409883"
     Site            47
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            105
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O89086; Dimethylated
                     arginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P98179;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            120
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            130
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O89086; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P98179; propagated from
                     UniProtKB/Swiss-Prot (Q925G0.2)"
     CDS             1..156
                     /gene="Rbm3"
                     /coded_by="NM_053696.1:101..571"
                     /db_xref="GeneID:114488"
                     /db_xref="RGD:620145"
ORIGIN      
        1 msseegklfv gglnfntdeq aledhfssfg pisevvvvkd retqrsrgfg fitftnpeha
       61 sdamramnge sldgrqirvd hagksargtr ggafgahgrg rsysrgggdq gygsgrydsr
      121 pggygygygr srdysgrsqg gydrysggny rdnydn
//
LOCUS       NP_001034097             243 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 176A [Rattus norvegicus].
ACCESSION   NP_001034097 XP_216137
VERSION     NP_001034097.1
DBSOURCE    REFSEQ: accession NM_001039008.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Condamine,T., Le Texier,L., Howie,D., Lavault,A., Hill,M.,
            Halary,F., Cobbold,S., Waldmann,H., Cuturi,M.C. and Chiffoleau,E.
  TITLE     Tmem176B and Tmem176A are associated with the immature state of
            dendritic cells
  JOURNAL   J Leukoc Biol 88 (3), 507-515 (2010)
   PUBMED   20501748
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098714.1.
            
            On Jan 12, 2006 this sequence version replaced XP_216137.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098714.1, FQ209561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..243
                     /product="transmembrane protein 176A"
                     /note="hepatocellular carcinoma-associated antigen 112"
                     /calculated_mol_wt=26482
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCS1; propagated from
                     UniProtKB/Swiss-Prot (Q4G068.1)"
     Region          63..223
                     /region_name="CD20"
                     /note="CD20-like family; pfam04103"
                     /db_xref="CDD:461174"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G068.1)"
     Site            92..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G068.1)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G068.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G068.1)"
     CDS             1..243
                     /gene="Tmem176a"
                     /gene_synonym="0610011i04rik; RGD1310725"
                     /coded_by="NM_001039008.1:13..744"
                     /db_xref="GeneID:297077"
                     /db_xref="RGD:1310725"
ORIGIN      
        1 mstdmgtadv gevdpeapqp tnievhihqe svlaklllag csflrvpasa stqsqgssrv
       61 lvaswvvqiv lgilsvvlgg ilyichylam ntqgapfwtg ivamlagava flqkkrggtc
      121 walmrillvl asfctavaai vigsrefnny wyylrddvck sdtsyrwstm psitpvpeea
      181 nriglckyyt smlktllisl qamllgvwvl lllaslipvc vylwkrfftk aetekkllga
      241 avi
//
LOCUS       NP_599216                721 aa            linear   ROD 27-APR-2025
DEFINITION  long-chain-fatty-acid--CoA ligase ACSBG1 [Rattus norvegicus].
ACCESSION   NP_599216
VERSION     NP_599216.1
DBSOURCE    REFSEQ: accession NM_134389.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Oishi,T., Iino,K., Okawa,Y., Kakizawa,K., Matsunari,S.,
            Yamashita,M., Taniguchi,T., Maekawa,M., Suda,T. and Oki,Y.
  TITLE     DNA methylation analysis in malignant pheochromocytoma and
            paraganglioma
  JOURNAL   J Clin Transl Endocrinol 7, 12-20 (2016)
   PUBMED   29067245
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Ohkuni,A., Ohno,Y. and Kihara,A.
  TITLE     Identification of acyl-CoA synthetases involved in the mammalian
            sphingosine 1-phosphate metabolic pathway
  JOURNAL   Biochem Biophys Res Commun 442 (3-4), 195-201 (2013)
   PUBMED   24269233
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Sheng,Y., Tsai-Morris,C.H., Li,J. and Dufau,M.L.
  TITLE     Lessons from the gonadotropin-regulated long chain acyl-CoA
            synthetase (GR-LACS) null mouse model: a role in steroidogenesis,
            but not result in X-ALD phenotype
  JOURNAL   J Steroid Biochem Mol Biol 114 (1-2), 44-56 (2009)
   PUBMED   19167491
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Song,S.Y., Kato,C., Adachi,E., Moriya-Sato,A., Inagawa-Ogashiwa,M.,
            Umeda,R. and Hashimoto,N.
  TITLE     Expression of an acyl-CoA synthetase, lipidosin, in astrocytes of
            the murine brain and its up-regulation during remyelination
            following cuprizone-induced demyelination
  JOURNAL   J Neurosci Res 85 (16), 3586-3597 (2007)
   PUBMED   17722065
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Li,J., Sheng,Y., Tang,P.Z., Tsai-Morris,C.H. and Dufau,M.L.
  TITLE     Tissue-cell- and species-specific expression of
            gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in
            gonads, adrenal and brain. Identification of novel forms in the
            brain
  JOURNAL   J Steroid Biochem Mol Biol 98 (4-5), 207-217 (2006)
   PUBMED   16469493
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Asheuer,M., Bieche,I., Laurendeau,I., Moser,A., Hainque,B.,
            Vidaud,M. and Aubourg,P.
  TITLE     Decreased expression of ABCD4 and BG1 genes early in the
            pathogenesis of X-linked adrenoleukodystrophy
  JOURNAL   Hum Mol Genet 14 (10), 1293-1303 (2005)
   PUBMED   15800013
REFERENCE   7  (residues 1 to 721)
  AUTHORS   Fraisl,P., Forss-Petter,S., Zigman,M. and Berger,J.
  TITLE     Murine bubblegum orthologue is a microsomal very long-chain
            acyl-CoA synthetase
  JOURNAL   Biochem J 377 (Pt 1), 85-93 (2004)
   PUBMED   14516277
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Tang,P.Z., Tsai-Morris,C.H. and Dufau,M.L.
  TITLE     Cloning and characterization of a hormonally regulated rat long
            chain acyl-CoA synthetase
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6581-6586 (2001)
   PUBMED   11381125
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Steinberg,S.J., Morgenthaler,J., Heinzer,A.K., Smith,K.D. and
            Watkins,P.A.
  TITLE     Very long-chain acyl-CoA synthetases. Human 'bubblegum' represents
            a new family of proteins capable of activating very long-chain
            fatty acids
  JOURNAL   J Biol Chem 275 (45), 35162-35169 (2000)
   PUBMED   10954726
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF208125.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF208125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..721
                     /product="long-chain-fatty-acid--CoA ligase ACSBG1"
                     /EC_number="6.2.1.3"
                     /note="gonadotropin-regulated long chain acyl CoA
                     synthetase; lipidosin"
                     /calculated_mol_wt=80388
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924N5.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q924N5.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q924N5.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q924N5.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q924N5.1)"
     Region          122..716
                     /region_name="ACSBG_like"
                     /note="Bubblegum-like very long-chain fatty acid CoA
                     synthetase (VL-FACS); cd05933"
                     /db_xref="CDD:341256"
     Site            order(276,279..284,286..287)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341256"
     Site            order(279,401..402,469..474,547,559,562,574,696)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341256"
     Site            order(279,323..324,372,374..375,378,401..402,469..474,547,
                     559,562,571..574,673)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341256"
     Site            order(323,374..375,378,401,571..573,667,673)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341256"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99PU5; propagated from
                     UniProtKB/Swiss-Prot (Q924N5.1)"
     CDS             1..721
                     /gene="Acsbg1"
                     /gene_synonym="Grlacs; Lpd"
                     /coded_by="NM_134389.1:29..2194"
                     /db_xref="GeneID:171410"
                     /db_xref="RGD:708557"
ORIGIN      
        1 mprsseagyc clsrdsnmpd srddqqqgas mgtspdnsqt sslidgrtls kespshglel
       61 sapekaraas ldaseealwt tradgrvrlr lepfctqlpy tvhqmfyeal dkygnlsalg
      121 fkrkdkweri syyqyyliar kvakgflklg lerahsvail gfnspewffs avgtvfaggi
      181 vtgiyttssp eacqyiahdc ranvivvdtq kqlekilkiw kdlphlkavv iyqepppkkm
      241 anvytmeeli elgqevpeea ldaiidtqqp nqccvlvyts gttgnpkgvm lsqdnitwta
      301 rygsqagdiq paevqqevvv sylplshiaa qiydlwtgiq wgaqvcfadp dalkgtlvnt
      361 lreveptshm gvprvwekim eriqevaaqs gfirrkmllw amsvtleqnl tcpsndlkpf
      421 tsrladylvl arvrqalgfa kcqknfygaa pmtaetqrff lglnirlyag yglsestgph
      481 fmsspynyrl yssgrvvpgc rvklvnqdad gigeiclwgr tifmgylnme dktheaidse
      541 gwlhtgdmgr ldddgflyit grlkeliita ggenvppvpi eeavkmelpi issamligdq
      601 rkflsmlltl kctlnpetse ptdnlteqav efcqrvgska stvseivgqk deavyqaihe
      661 giqrvnanaa arpyhiqkwa ilerdfsisg gelgptmklk rltvlekykd iidsfyqeqk
      721 q
//
LOCUS       NP_071530                178 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-1 receptor antagonist protein precursor [Rattus
            norvegicus].
ACCESSION   NP_071530 XP_001071294 XP_001071330
VERSION     NP_071530.1
DBSOURCE    REFSEQ: accession NM_022194.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Bai,N., Zhang,Q., Zhang,W., Liu,B., Yang,F., Brann,D. and Wang,R.
  TITLE     G-protein-coupled estrogen receptor activation upregulates
            interleukin-1 receptor antagonist in the hippocampus after global
            cerebral ischemia: implications for neuronal self-defense
  JOURNAL   J Neuroinflammation 17 (1), 45 (2020)
   PUBMED   32007102
  REMARK    GeneRIF: G-protein-coupled estrogen receptor activation upregulates
            interleukin-1 receptor antagonist in the hippocampus after global
            cerebral ischemia: implications for neuronal self-defense.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Yamato,M., Tamura,Y., Eguchi,A., Kume,S., Miyashige,Y., Nakano,M.,
            Watanabe,Y. and Kataoka,Y.
  TITLE     Brain interleukin-1beta and the intrinsic receptor antagonist
            control peripheral Toll-like receptor 3-mediated suppression of
            spontaneous activity in rats
  JOURNAL   PLoS One 9 (3), e90950 (2014)
   PUBMED   24621600
  REMARK    GeneRIF: IL-1beta is the key trigger of neuroinflammation and that
            IL-1ra prevents the neuroinflammation entering the chronic state
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Teng,Y. and Gao,Y.
  TITLE     Tobacco smoking associated with the increases of the
            bronchoalveolar levels of interleukin-5 and interleukin-1 receptor
            antagonist in acute eosinophilic pneumonia
  JOURNAL   Eur Rev Med Pharmacol Sci 18 (6), 887-893 (2014)
   PUBMED   24706315
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Prins,M., Eriksson,C., Wierinckx,A., Bol,J.G., Binnekade,R.,
            Tilders,F.J. and Van Dam,A.M.
  TITLE     Interleukin-1beta and interleukin-1 receptor antagonist appear in
            grey matter additionally to white matter lesions during
            experimental multiple sclerosis
  JOURNAL   PLoS One 8 (12), e83835 (2013)
   PUBMED   24376764
  REMARK    GeneRIF: Interleukin-1beta and interleukin-1 receptor antagonist
            appear in grey matter additionally to white matter during
            experimental multiple sclerosis
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Vijmasi,T., Chen,F.Y., Chen,Y.T., Gallup,M. and McNamara,N.
  TITLE     Topical administration of interleukin-1 receptor antagonist as a
            therapy for aqueous-deficient dry eye in autoimmune disease
  JOURNAL   Mol Vis 19, 1957-1965 (2013)
   PUBMED   24068863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Ulich,T.R., Guo,K., Yin,S., del Castillo,J., Yi,E.S., Thompson,R.C.
            and Eisenberg,S.P.
  TITLE     Endotoxin-induced cytokine gene expression in vivo. IV. Expression
            of interleukin-1 alpha/beta and interleukin-1 receptor antagonist
            mRNA during endotoxemia and during endotoxin-initiated local acute
            inflammation
  JOURNAL   Am J Pathol 141 (1), 61-68 (1992)
   PUBMED   1385928
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Dripps,D.J., Verderber,E., Ng,R.K., Thompson,R.C. and
            Eisenberg,S.P.
  TITLE     Interleukin-1 receptor antagonist binds to the type II
            interleukin-1 receptor on B cells and neutrophils
  JOURNAL   J Biol Chem 266 (30), 20311-20315 (1991)
   PUBMED   1834644
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Granowitz,E.V., Clark,B.D., Mancilla,J. and Dinarello,C.A.
  TITLE     Interleukin-1 receptor antagonist competitively inhibits the
            binding of interleukin-1 to the type II interleukin-1 receptor
  JOURNAL   J Biol Chem 266 (22), 14147-14150 (1991)
   PUBMED   1830582
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Eisenberg,S.P., Brewer,M.T., Verderber,E., Heimdal,P.,
            Brandhuber,B.J. and Thompson,R.C.
  TITLE     Interleukin 1 receptor antagonist is a member of the interleukin 1
            gene family: evolution of a cytokine control mechanism
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5232-5236 (1991)
   PUBMED   1828896
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Dripps,D.J., Brandhuber,B.J., Thompson,R.C. and Eisenberg,S.P.
  TITLE     Interleukin-1 (IL-1) receptor antagonist binds to the 80-kDa IL-1
            receptor but does not initiate IL-1 signal transduction
  JOURNAL   J Biol Chem 266 (16), 10331-10336 (1991)
   PUBMED   1828071
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CK364274.1 and
            BC070930.1.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001071294.1, XP_001071330.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070930.1, CK364274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..178
                     /product="interleukin-1 receptor antagonist protein
                     precursor"
                     /note="interleukin-1 receptor antagonist protein; IRAP;
                     IL-1RN; IL1 inhibitor"
                     /calculated_mol_wt=17381
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2920
     mat_peptide     27..178
                     /product="Interleukin-1 receptor antagonist protein.
                     /id=PRO_0000015333"
                     /note="propagated from UniProtKB/Swiss-Prot (P25086.1)"
                     /calculated_mol_wt=17381
     Region          34..177
                     /region_name="beta-trefoil_IL1"
                     /note="beta-trefoil domain found in the interleukin-1
                     (IL-1) family of cytokines; cl00094"
                     /db_xref="CDD:469612"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25086.1)"
     CDS             1..178
                     /gene="Il1rn"
                     /gene_synonym="IL-1ra; Il1ra"
                     /coded_by="NM_022194.2:5..541"
                     /db_xref="GeneID:60582"
                     /db_xref="RGD:621159"
ORIGIN      
        1 meicrgpysh lislllillf rsesaghpag krpckmqafr iwdtnqktfy lrnnqliagy
       61 lqgpntklee kidmvpidfr nvflgihggk lclscvksgd dtklqleevn itdlnknkee
      121 dkrftfirse tgpttsfesl acpgwflctt leadhpvslt ntpkepctvt kfyfqedq
//
LOCUS       NP_001009292             271 aa            linear   ROD 27-APR-2025
DEFINITION  structure-specific endonuclease subunit SLX1 [Rattus norvegicus].
ACCESSION   NP_001009292 XP_215073
VERSION     NP_001009292.1
DBSOURCE    REFSEQ: accession NM_001009292.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wan,B., Yin,J., Horvath,K., Sarkar,J., Chen,Y., Wu,J., Wan,K.,
            Lu,J., Gu,P., Yu,E.Y., Lue,N.F., Chang,S., Liu,Y. and Lei,M.
  TITLE     SLX4 assembles a telomere maintenance toolkit by bridging multiple
            endonucleases with telomeres
  JOURNAL   Cell Rep 4 (5), 861-869 (2013)
   PUBMED   24012755
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Vannier,J.B., Pavicic-Kaltenbrunner,V., Petalcorin,M.I., Ding,H.
            and Boulton,S.J.
  TITLE     RTEL1 dismantles T loops and counteracts telomeric G4-DNA to
            maintain telomere integrity
  JOURNAL   Cell 149 (4), 795-806 (2012)
   PUBMED   22579284
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Fekairi,S., Scaglione,S., Chahwan,C., Taylor,E.R., Tissier,A.,
            Coulon,S., Dong,M.Q., Ruse,C., Yates,J.R. 3rd, Russell,P.,
            Fuchs,R.P., McGowan,C.H. and Gaillard,P.H.L.
  TITLE     Human SLX4 is a Holliday junction resolvase subunit that binds
            multiple DNA repair/recombination endonucleases
  JOURNAL   Cell 138 (1), 78-89 (2009)
   PUBMED   19596236
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Andersen,S.L., Bergstralh,D.T., Kohl,K.P., LaRocque,J.R.,
            Moore,C.B. and Sekelsky,J.
  TITLE     Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with
            DNA structure-specific endonucleases in DNA repair and
            recombination
  JOURNAL   Mol Cell 35 (1), 128-135 (2009)
   PUBMED   19595722
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Munoz,I.M., Hain,K., Declais,A.C., Gardiner,M., Toh,G.W.,
            Sanchez-Pulido,L., Heuckmann,J.M., Toth,R., Macartney,T.,
            Eppink,B., Kanaar,R., Ponting,C.P., Lilley,D.M. and Rouse,J.
  TITLE     Coordination of structure-specific nucleases by human SLX4/BTBD12
            is required for DNA repair
  JOURNAL   Mol Cell 35 (1), 116-127 (2009)
   PUBMED   19595721
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087090.1.
            
            On Jan 7, 2005 this sequence version replaced XP_215073.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087090.1, SRR8487231.21191.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..271
                     /product="structure-specific endonuclease subunit SLX1"
                     /note="GIY-YIG domain containing 2; GIY-YIG
                     domain-containing protein 1"
                     /calculated_mol_wt=30615
     Region          10..85
                     /region_name="GIY-YIG_SLX1"
                     /note="Catalytic GIY-YIG domain of yeast
                     structure-specific endonuclease subunit SLX1 and its
                     eukaryotic homologs; cd10455"
                     /db_xref="CDD:198402"
     Site            order(12..14,28..30)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198402"
     Site            order(14,28,30,38,42,79)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198402"
     Site            79
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198402"
     CDS             1..271
                     /gene="Slx1b"
                     /gene_synonym="Giyd1; Giyd2; LRRGT00058; RGD1311568"
                     /coded_by="NM_001009292.1:136..951"
                     /db_xref="GeneID:293489"
                     /db_xref="RGD:1311568"
ORIGIN      
        1 mghaarpgrf fgvyllycqn prhrgrvyvg ftvnparrvr qhnagrkkgg awrtsgrgpw
       61 dmvlilhgfp savaalrfew awqhpqasrr lthvgprlrs easftfhlrv lahmlrvppw
      121 vrlpltvrwl rpdfrhelcp appphmpiaf gppppqplvp krpaaseads errldlgaka
      181 sctlcarmlq deegplccph pgcplrahii claeeflqee pgqllplegh cpsckksllw
      241 gnlvgqched teeeevdlel eeehwtdlle t
//
LOCUS       NP_001009675             165 aa            linear   ROD 27-APR-2025
DEFINITION  transcription elongation factor A protein-like 1 [Rattus
            norvegicus].
ACCESSION   NP_001009675 XP_217602
VERSION     NP_001009675.1
DBSOURCE    REFSEQ: accession NM_001009675.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087575.1.
            
            On Jan 13, 2005 this sequence version replaced XP_217602.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087575.1, FQ214955.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq32"
     Protein         1..165
                     /product="transcription elongation factor A protein-like
                     1"
                     /note="TCEA-like protein 1; transcription elongation
                     factor S-II protein-like 1; transcription elongation
                     factor A (SII)-like 1"
                     /calculated_mol_wt=19131
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPP3.1)"
     Region          89..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPP3.1)"
     Region          <93..165
                     /region_name="BEX"
                     /note="Brain expressed X-linked like family; pfam04538"
                     /db_xref="CDD:461346"
     CDS             1..165
                     /gene="Tceal1"
                     /coded_by="NM_001009675.1:128..625"
                     /db_xref="GeneID:302593"
                     /db_xref="RGD:1549724"
ORIGIN      
        1 menshnesee qpqstpkvee eqpaveqspe nqcseddqss edlsseeqss deeffpeell
       61 pellpemllc edrppqeclp qknafedrip meqppcgigk hkleegsfke rlarsrpqfr
      121 gdihgrnlsn eemiraadel eemkrvrnkl mimhwkakrs rpypi
//
LOCUS       NP_001100543             402 aa            linear   ROD 27-APR-2025
DEFINITION  NAD-dependent protein deacetylase sirtuin-7 [Rattus norvegicus].
ACCESSION   NP_001100543 XP_001081828 XP_221204
VERSION     NP_001100543.1
DBSOURCE    REFSEQ: accession NM_001107073.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Wang,Y., Wu,X.Q., Cai,J.R., Ji,H.X. and Xu,T.
  TITLE     SIRT7 silencing by miR-152-3p confers cell apoptosis and renal
            functional impairment induced by renal ischaemia/reperfusion injury
  JOURNAL   Int Urol Nephrol 55 (2), 367-376 (2023)
   PUBMED   35941302
  REMARK    GeneRIF: SIRT7 silencing by miR-152-3p confers cell apoptosis and
            renal functional impairment induced by renal ischaemia/reperfusion
            injury.
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Song,C.Y., Guo,Y., Chen,F.Y. and Liu,W.G.
  TITLE     Resveratrol Promotes Osteogenic Differentiation of Bone
            Marrow-Derived Mesenchymal Stem Cells Through miR-193a/SIRT7 Axis
  JOURNAL   Calcif Tissue Int 110 (1), 117-130 (2022)
   PUBMED   34477918
  REMARK    GeneRIF: Resveratrol Promotes Osteogenic Differentiation of Bone
            Marrow-Derived Mesenchymal Stem Cells Through miR-193a/SIRT7 Axis.
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Xu,S., Tao,H., Cao,W., Cao,L., Lin,Y., Zhao,S.M., Xu,W., Cao,J. and
            Zhao,J.Y.
  TITLE     Ketogenic diets inhibit mitochondrial biogenesis and induce cardiac
            fibrosis
  JOURNAL   Signal Transduct Target Ther 6 (1), 54 (2021)
   PUBMED   33558457
  REMARK    GeneRIF: Ketogenic diets inhibit mitochondrial biogenesis and
            induce cardiac fibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Chen,Q., Liu,Y., Ding,X., Li,Q., Qiu,F., Wang,M., Shen,Z., Zheng,H.
            and Fu,G.
  TITLE     Bone marrow mesenchymal stem cell-secreted exosomes carrying
            microRNA-125b protect against myocardial ischemia reperfusion
            injury via targeting SIRT7
  JOURNAL   Mol Cell Biochem 465 (1-2), 103-114 (2020)
   PUBMED   31858380
  REMARK    GeneRIF: the injection of BMSC-Exo-125b alleviated the pathological
            damages and down-regulated SIRT7 in myocardium tissues of I/R rats.
            BMSC-derived exosomes carrying miR-125b protected against
            myocardial I/R by targeting SIRT7.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Bao,X., Liu,Z., Zhang,W., Gladysz,K., Fung,Y.M.E., Tian,G.,
            Xiong,Y., Wong,J.W.H., Yuen,K.W.Y. and Li,X.D.
  TITLE     Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics
  JOURNAL   Mol Cell 76 (4), 660-675 (2019)
   PUBMED   31542297
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Grummt,I.
  TITLE     The nucleolus-guardian of cellular homeostasis and genome integrity
  JOURNAL   Chromosoma 122 (6), 487-497 (2013)
   PUBMED   24022641
  REMARK    Review article
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Barber,M.F., Michishita-Kioi,E., Xi,Y., Tasselli,L., Kioi,M.,
            Moqtaderi,Z., Tennen,R.I., Paredes,S., Young,N.L., Chen,K.,
            Struhl,K., Garcia,B.A., Gozani,O., Li,W. and Chua,K.F.
  TITLE     SIRT7 links H3K18 deacetylation to maintenance of oncogenic
            transformation
  JOURNAL   Nature 487 (7405), 114-118 (2012)
   PUBMED   22722849
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Peserico,A. and Simone,C.
  TITLE     Physical and functional HAT/HDAC interplay regulates protein
            acetylation balance
  JOURNAL   J Biomed Biotechnol 2011, 371832 (2011)
   PUBMED   21151613
  REMARK    Review article
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Grob,A., Roussel,P., Wright,J.E., McStay,B., Hernandez-Verdun,D.
            and Sirri,V.
  TITLE     Involvement of SIRT7 in resumption of rDNA transcription at the
            exit from mitosis
  JOURNAL   J Cell Sci 122 (Pt 4), 489-498 (2009)
   PUBMED   19174463
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Michishita,E., Park,J.Y., Burneskis,J.M., Barrett,J.C. and
            Horikawa,I.
  TITLE     Evolutionarily conserved and nonconserved cellular localizations
            and functions of human SIRT proteins
  JOURNAL   Mol Biol Cell 16 (10), 4623-4635 (2005)
   PUBMED   16079181
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_221204.4, XP_001081828.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC167031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..402
                     /product="NAD-dependent protein deacetylase sirtuin-7"
                     /EC_number="2.3.1.286"
                     /note="NAD-dependent deacetylase sirtuin-7; SIR2-like
                     protein 7; regulatory protein SIR2 homolog 7;
                     NAD-dependent protein deacylase sirtuin-7"
                     /calculated_mol_wt=44982
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RZ55.1)"
     Region          <11..>91
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          59..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RZ55.1)"
     Region          102..315
                     /region_name="SIRT7"
                     /note="Eukaryotic and prokaryotic group (class4) which
                     includes human sirtuin SIRT6, SIRT7, and several bacterial
                     homologs; and are members of the SIR2 family of proteins,
                     silent information regulator 2 (Sir2) enzymes which
                     catalyze NAD+-dependent protein...; cd01410"
                     /db_xref="CDD:238701"
     Site            order(110,112..113,120..121,150,168..169,171,188,269,274,
                     299..300,315)
                     /site_type="other"
                     /note="NAD+ binding site [chemical binding]"
                     /db_xref="CDD:238701"
     Site            order(170,188,238,240..244,273..274,278)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238701"
     Site            order(196,199,226,229)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:238701"
     Region          355..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RZ55.1)"
     Site            390
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9NRC8;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9NRC8; propagated from
                     UniProtKB/Swiss-Prot (B2RZ55.1)"
     CDS             1..402
                     /gene="Sirt7"
                     /coded_by="NM_001107073.1:21..1229"
                     /db_xref="GeneID:303745"
                     /db_xref="RGD:1305876"
ORIGIN      
        1 maaggglsrs erkaaervrr lreeqqrerl rqvsrilrka aaersaeegr llaesedlvt
       61 elqgrsrrre glkrrqeevc ddpeelrrkv relagavrsa rhlvvytgag istaasipdy
      121 rgpngvwtll qkgrpvsaad lseaeptlth msitqlhkhk lvqhvvsqnc dglhlrsglp
      181 rtaiselhgn myievctsci pnreyvrvfd vtertalhrh ltgrtchkcg tqlrdtivhf
      241 gergtlgqpl nweaateaas kadtilclgs slkvlkkypr lwcmtkppsr rpklyivnlq
      301 wtpkddwaal klhgkcddvm rllmdelgle ipvynrwqdp ifslatplra geegshsrks
      361 lcrsreeppp gdqsaplasa tpilggwfgr gcakrakrkk aa
//
LOCUS       NP_001004214             231 aa            linear   ROD 27-APR-2025
DEFINITION  ribosyldihydronicotinamide dehydrogenase [quinone] [Rattus
            norvegicus].
ACCESSION   NP_001004214 XP_214470
VERSION     NP_001004214.1
DBSOURCE    REFSEQ: accession NM_001004214.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Ran,L.Y., Xiang,J., Zeng,X.X., He,W.W., Dong,Y.T., Yu,W.F.,
            Qi,X.L., Xiao,Y., Cao,K., Zou,J. and Guan,Z.Z.
  TITLE     The influence of NQO2 on the dysfunctional autophagy and oxidative
            stress induced in the hippocampus of rats and in SH-SY5Y cells by
            fluoride
  JOURNAL   CNS Neurosci Ther 29 (4), 1129-1141 (2023)
   PUBMED   36650666
  REMARK    GeneRIF: The influence of NQO2 on the dysfunctional autophagy and
            oxidative stress induced in the hippocampus of rats and in SH-SY5Y
            cells by fluoride.
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Zhang,X., Wang,Y., Yang,W., Hou,X., Zou,J. and Cao,K.
  TITLE     Resveratrol inhibits angiotensin II-induced ERK1/2 activation by
            downregulating quinone reductase 2 in rat vascular smooth muscle
            cells
  JOURNAL   J Biomed Res 26 (2), 103-109 (2012)
   PUBMED   23554738
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Hubackova,M., Vaclavikova,R., Ehrlichova,M., Mrhalova,M., Kodet,R.,
            Kubackova,K., Vrana,D., Gut,I. and Soucek,P.
  TITLE     Association of superoxide dismutases and NAD(P)H quinone
            oxidoreductases with prognosis of patients with breast carcinomas
  JOURNAL   Int J Cancer 130 (2), 338-348 (2012)
   PUBMED   21351093
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Zhang,X.W., Wang,Y., Cai,J.B., Hou,X.F., Wang,H.G., Zou,J.G. and
            Cao,K.J.
  TITLE     Downregulation of quinone reductase 2 attenuates vascular smooth
            muscle cells proliferation and neointimal formation in balloon
            injured rat carotid artery
  JOURNAL   Cell Physiol Biochem 29 (3-4), 453-462 (2012)
   PUBMED   22508052
  REMARK    GeneRIF: Downregulation of NQO2 significantly suppresses vascular
            smooth muscle cell proliferation and progression of neointimal
            formation after vascular injury.
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Benoit,C.E., Bastianetto,S., Brouillette,J., Tse,Y., Boutin,J.A.,
            Delagrange,P., Wong,T., Sarret,P. and Quirion,R.
  TITLE     Loss of quinone reductase 2 function selectively facilitates
            learning behaviors
  JOURNAL   J Neurosci 30 (38), 12690-12700 (2010)
   PUBMED   20861374
  REMARK    GeneRIF: these data suggest a role for QR2 in cognitive behaviors
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Brouillette,J. and Quirion,R.
  TITLE     Transthyretin: a key gene involved in the maintenance of memory
            capacities during aging
  JOURNAL   Neurobiol Aging 29 (11), 1721-1732 (2008)
   PUBMED   17512093
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Das,A., Kole,L., Wang,L., Barrios,R., Moorthy,B. and Jaiswal,A.K.
  TITLE     BALT development and augmentation of hyperoxic lung injury in mice
            deficient in NQO1 and NQO2
  JOURNAL   Free Radic Biol Med 40 (10), 1843-1856 (2006)
   PUBMED   16678022
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Ostrousky,O., Meged,S., Loewenthal,R., Valevski,A., Weizman,A.,
            Carp,H. and Gazit,E.
  TITLE     NQO2 gene is associated with clozapine-induced agranulocytosis
  JOURNAL   Tissue Antigens 62 (6), 483-491 (2003)
   PUBMED   14617031
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Long,D.J. 2nd, Iskander,K., Gaikwad,A., Arin,M., Roop,D.R.,
            Knox,R., Barrios,R. and Jaiswal,A.K.
  TITLE     Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2
            (NQO2) leads to myeloid hyperplasia of bone marrow and decreased
            sensitivity to menadione toxicity
  JOURNAL   J Biol Chem 277 (48), 46131-46139 (2002)
   PUBMED   12351651
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Knox,R.J., Jenkins,T.C., Hobbs,S.M., Chen,S., Melton,R.G. and
            Burke,P.J.
  TITLE     Bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954)
            by human NAD(P)H quinone oxidoreductase 2: a novel
            co-substrate-mediated antitumor prodrug therapy
  JOURNAL   Cancer Res 60 (15), 4179-4186 (2000)
   PUBMED   10945627
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079157.1.
            
            On Sep 10, 2004 this sequence version replaced XP_214470.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079157.1, CV106092.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132263,
                                           SAMD00132264 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..231
                     /product="ribosyldihydronicotinamide dehydrogenase
                     [quinone]"
                     /EC_number="1.10.5.1"
                     /note="ribosyldihydronicotinamide dehydrogenase;
                     N-ribosyldihydronicotinamide:quinone reductase 2; QR2;
                     NRH:quinone oxidoreductase 2; NRH dehydrogenase [quinone]
                     2; NAD(P)H dehydrogenase, quinone 2; NAD(P)H quinone
                     dehydrogenase 2"
                     /calculated_mol_wt=26144
     Region          5..216
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16083; propagated from
                     UniProtKB/Swiss-Prot (Q6AY80.3)"
     CDS             1..231
                     /gene="Nqo2"
                     /coded_by="NM_001004214.1:104..799"
                     /db_xref="GeneID:291084"
                     /db_xref="RGD:1303320"
ORIGIN      
        1 magkkvllvy ahqepksfng smkqvaveel skqgctvtvs dlytmnfepr atrndvtgal
       61 snpevfkygi eayeaykkka ltsdileeqr kvqeadlvif qfplywfsvp ailkgwmdrv
      121 lcqgfafdvp gfydsgflkd klallsfttg gtaemytkag vngdfryflw plqhgtlhfc
      181 gfkvlapqis fgpevsseeq rkvmlaswvq rlksiwkeep ihctpswyfq g
//
LOCUS       NP_001008526             447 aa            linear   ROD 27-APR-2025
DEFINITION  BAG family molecular chaperone regulator 5 [Rattus norvegicus].
ACCESSION   NP_001008526 XP_345727
VERSION     NP_001008526.1
DBSOURCE    REFSEQ: accession NM_001008526.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Xi,J., Li,Q.Q., Li,B.Q. and Li,N.
  TITLE     miR-155 inhibition represents a potential valuable regulator in
            mitigating myocardial hypoxia/reoxygenation injury through
            targeting BAG5 and MAPK/JNK signaling
  JOURNAL   Mol Med Rep 21 (3), 1011-1020 (2020)
   PUBMED   31922242
  REMARK    GeneRIF: miR155 inhibition represents a potential valuable
            regulator in mitigating myocardial hypoxia/reoxygenation injury
            through targeting BAG5 and MAPK/JNK signaling.
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Gupta,M.K., Tahrir,F.G., Knezevic,T., White,M.K., Gordon,J.,
            Cheung,J.Y., Khalili,K. and Feldman,A.M.
  TITLE     GRP78 Interacting Partner Bag5 Responds to ER Stress and Protects
            Cardiomyocytes From ER Stress-Induced Apoptosis
  JOURNAL   J Cell Biochem 117 (8), 1813-1821 (2016)
   PUBMED   26729625
  REMARK    GeneRIF: Bag5 protein expression is significantly increased in the
            ER during ER stress and that this in turn modulates GRP78 protein
            stability and reduces ER stress.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Che,X.Q., Tang,B.S., Wang,H.F., Yan,X.X., Jiang,H., Shen,L., Xu,Q.,
            Wang,G.H., Zhang,H.N., Wang,C.Y. and Guo,J.F.
  TITLE     The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic
            ataxin3-80Q
  JOURNAL   Int J Neurosci 125 (5), 390-394 (2015)
   PUBMED   25006867
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Beilina,A., Rudenko,I.N., Kaganovich,A., Civiero,L., Chau,H.,
            Kalia,S.K., Kalia,L.V., Lobbestael,E., Chia,R., Ndukwe,K., Ding,J.,
            Nalls,M.A., Olszewski,M., Hauser,D.N., Kumaran,R., Lozano,A.M.,
            Baekelandt,V., Greene,L.E., Taymans,J.M., Greggio,E. and
            Cookson,M.R.
  CONSRTM   International Parkinson's Disease Genomics Consortium; North
            American Brain Expression Consortium
  TITLE     Unbiased screen for interactors of leucine-rich repeat kinase 2
            supports a common pathway for sporadic and familial Parkinson
            disease
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2626-2631 (2014)
   PUBMED   24510904
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Wang,X., Guo,J., Fei,E., Mu,Y., He,S., Che,X., Tan,J., Xia,K.,
            Zhang,Z., Wang,G. and Tang,B.
  TITLE     BAG5 protects against mitochondrial oxidative damage through
            regulating PINK1 degradation
  JOURNAL   PLoS One 9 (1), e86276 (2014)
   PUBMED   24475098
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Ma,M., Wang,X., Ding,X., Jing,J., Ma,Y. and Teng,J.
  TITLE     Protective effect of BAG5 on MPP+-induced apoptosis in PC12 cells
  JOURNAL   Neurol Res 34 (10), 977-983 (2012)
   PUBMED   23146300
  REMARK    GeneRIF: BAG5 induction inhibits MPP(+)-induced apoptosis through
            both endogenous and mitochondria-mediated pathways of apoptosis.
REFERENCE   7  (residues 1 to 447)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Kalia,L.V., Kalia,S.K., Chau,H., Lozano,A.M., Hyman,B.T. and
            McLean,P.J.
  TITLE     Ubiquitinylation of alpha-synuclein by carboxyl terminus
            Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated
            athanogene 5 (BAG5)
  JOURNAL   PLoS One 6 (2), e14695 (2011)
   PUBMED   21358815
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Kalia,S.K., Lee,S., Smith,P.D., Liu,L., Crocker,S.J.,
            Thorarinsdottir,T.E., Glover,J.R., Fon,E.A., Park,D.S. and
            Lozano,A.M.
  TITLE     BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
  JOURNAL   Neuron 44 (6), 931-945 (2004)
   PUBMED   15603737
  REMARK    GeneRIF: BAG5 enhances dopamine neuron death in a rat model of
            Parkinson's disease, whereas a mutant that inhibits BAG5 activity
            attenuates dopaminergic neurodegeneration.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088418.1.
            
            On Dec 16, 2004 this sequence version replaced XP_345727.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088418.1, AY366364.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..447
                     /product="BAG family molecular chaperone regulator 5"
                     /note="BAG-5; bcl-2-associated athanogene 5;
                     BCL2-associated athanogene 5; BCL2-associated athanogene
                     5-like 1"
                     /calculated_mol_wt=50900
     Region          9..86
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     Region          182..260
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     Region          275..350
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     Region          366..442
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     CDS             1..447
                     /gene="Bag5"
                     /gene_synonym="Bag5l1"
                     /coded_by="NM_001008526.2:138..1481"
                     /db_xref="GeneID:366734"
                     /db_xref="RGD:1310847"
ORIGIN      
        1 mdmgnqhpsi srlqeiqrev ksieqqvvgf sglsddknyk rleriltkql feidsvdteg
       61 kgdiqqarkr aaqdterllk eleqnanhph rieiknifqe aqalvkektv pfysgsncvt
      121 sefeeaiqdi ilrlthvktg gkislrkary htltkicavq eiiedcvrkq pslplsedvh
      181 psvakinsvm cevnkargtl iallmgvdss etcrhlscvl sglmadldal dvcgrteirn
      241 yrrevvedin kllkyldlee eadnthafdl gqnhsiikie nvlkrmremk nellqaqspp
      301 elylrsktel qgligqldev sleknpcire arrravievq tlityldlke alekrklfpc
      361 eetpphkavw nvlgnlseiq gevlsfggnr tdknyirlee lltkqlltld avdplgeekc
      421 kaarkqavkl aqnilsyldm ksdewey
//
LOCUS       NP_037024                563 aa            linear   ROD 27-APR-2025
DEFINITION  acid-sensing ion channel 2 isoform MDEG2 [Rattus norvegicus].
ACCESSION   NP_037024
VERSION     NP_037024.2
DBSOURCE    REFSEQ: accession NM_012892.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Shibata,Y., Kumamoto,N., Sakuma,E., Ishida,Y., Ueda,T., Shimada,S.
            and Ugawa,S.
  TITLE     A gain-of-function mutation in the acid-sensing ion channel 2a
            induces marked cerebellar maldevelopment in rats
  JOURNAL   Biochem Biophys Res Commun 610, 77-84 (2022)
   PUBMED   35447498
  REMARK    GeneRIF: A gain-of-function mutation in the acid-sensing ion
            channel 2a induces marked cerebellar maldevelopment in rats.
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Yan,X., Zhang,S., Zhao,H., Liu,P., Huang,H., Niu,W., Wang,W. and
            Zhang,C.
  TITLE     ASIC2 Synergizes with TRPV1 in the Mechano-Electrical Transduction
            of Arterial Baroreceptors
  JOURNAL   Neurosci Bull 37 (10), 1381-1396 (2021)
   PUBMED   34215968
  REMARK    GeneRIF: ASIC2 Synergizes with TRPV1 in the Mechano-Electrical
            Transduction of Arterial Baroreceptors.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Liu,Y., Hagan,R. and Schoellerman,J.
  TITLE     Dual actions of Psalmotoxin at ASIC1a and ASIC2a heteromeric
            channels (ASIC1a/2a)
  JOURNAL   Sci Rep 8 (1), 7179 (2018)
   PUBMED   29739981
  REMARK    GeneRIF: Our findings identify PcTx1 as a valuable tool for
            studying ASIC1a/2a function and contribute significantly to the
            understanding of the diverse and complex pharmacology of PcTx1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Zhang,H., Gao,G., Zhang,Y., Sun,Y., Li,H., Dong,S., Ma,W., Liu,B.,
            Wang,W., Wu,H. and Zhang,H.
  TITLE     Glucose Deficiency Elevates Acid-Sensing Ion Channel 2a Expression
            and Increases Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Sci Rep 7 (1), 5870 (2017)
   PUBMED   28725010
  REMARK    GeneRIF: hippocampal glucose hypometabolism elevates ASIC2a
            expression by suppressing TFCP2 expression, which further enhances
            the intrinsic excitability of CA1 pyramidal neurons and increases
            seizure susceptibility in patients with temporal lobe epilepsy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Wu,H., Wang,C., Liu,B., Li,H., Zhang,Y., Dong,S., Gao,G. and
            Zhang,H.
  TITLE     Altered Expression Pattern of Acid-Sensing Ion Channel Isoforms in
            Piriform Cortex After Seizures
  JOURNAL   Mol Neurobiol 53 (3), 1782-1793 (2016)
   PUBMED   25744567
  REMARK    GeneRIF: ASICs may enhance susceptibility to epileptogenesis in the
            piriform cortex.
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Bassilana,F., Champigny,G., Waldmann,R., de Weille,J.R.,
            Heurteaux,C. and Lazdunski,M.
  TITLE     The acid-sensitive ionic channel subunit ASIC and the mammalian
            degenerin MDEG form a heteromultimeric H+-gated Na+ channel with
            novel properties
  JOURNAL   J Biol Chem 272 (46), 28819-28822 (1997)
   PUBMED   9360943
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Waldmann,R., Champigny,G., Voilley,N., Lauritzen,I. and
            Lazdunski,M.
  TITLE     The mammalian degenerin MDEG, an amiloride-sensitive cation channel
            activated by mutations causing neurodegeneration in Caenorhabditis
            elegans
  JOURNAL   J Biol Chem 271 (18), 10433-10436 (1996)
   PUBMED   8631835
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Sokolov,Iu.N., Kaigorodtseva,R.N. and Rudykh,V.F.
  TITLE     [Various roentgenomorphological parallels in ulcers of the
            pyloro-duodenal area]
  JOURNAL   Vestn Rentgenol Radiol (6), 3-11 (1978)
   PUBMED   734884
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Carson,A.
  TITLE     Writing good abstracts: it's a tought job
  JOURNAL   Phys Ther 58 (2), 175-177 (1978)
   PUBMED   625485
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Tanaka,S., Tamura,K. and Mizuno,Y.
  TITLE     [Clinical consideration with special reference to autopsy cases of
            malignant tumor in the oral cavity, treated with Bleomycin
            (author's transl)]
  JOURNAL   Hiroshima Daigaku Shigaku Zasshi 8 (2), 168-175 (1975)
   PUBMED   69641
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Y14635.1.
            
            On Sep 26, 2003 this sequence version replaced NP_037024.1.
            
            Transcript Variant: The variant (MDEG2) encodes the longer protein
            (isoform MDEG2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y14635.1, KP294334.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..563
                     /product="acid-sensing ion channel 2 isoform MDEG2"
                     /note="degenerin; brain sodium channel 1; acid-sensing ion
                     channel 2; amiloride-sensitive brain sodium channel 2;
                     BNC1; acid-sensing proton-gated ion channel 2 short
                     variant MDEG2; acid-sensing (proton-gated) ion channel 2;
                     amiloride-sensitive cation channel 1, neuronal"
                     /calculated_mol_wt=62985
     Region          64..557
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     CDS             1..563
                     /gene="Asic2"
                     /gene_synonym="Accn1; BNaC1; BNC1k; MDEG; MDEG1; MDEG2"
                     /coded_by="NM_012892.2:16..1707"
                     /note="isoform MDEG2 is encoded by transcript variant
                     MDEG2"
                     /db_xref="GeneID:25364"
                     /db_xref="RGD:2017"
ORIGIN      
        1 msrsggarlp atalsgpgrf rmareqpapv avaaarqpgg drsgdpalqg pgvarrgrps
       61 lsrtklhglr hmcagrtaag gsfqrralwv lafctslgll lswssnrlly wlsfpshtrv
      121 hrewsrqlpf pavtvcnnnp lrfprlskgd lyyaghwlgl llpnrtarpl vsellrgdep
      181 rrqwfrklad frlflpprhf egisaafmdr lghqledmll sckyrgelcg phnfssvftk
      241 ygkcymfnsg edgkpllttv kggtgnglei mldiqqdeyl piwgeteett feagvkvqih
      301 sqseppfiqe lgfgvapgfq tfvatqeqrl tylpppwgec rssemgldff pvysitacri
      361 dcetryiven cncrmvhmpg dapfctpeqh kecaepalgl laekdsnycl crtpcnltry
      421 nkelsmvkip sktsakylek kfnksekyis enilvldiff ealnyetieq kkayevaall
      481 gdiggqmglf igaslltile lfdyiyelik eklldllgke eeegshdenm stcdtmpnhs
      541 etishtvnvp lqtalgtlee iac
//
LOCUS       NP_001007618             630 aa            linear   ROD 27-APR-2025
DEFINITION  NUAK family SNF1-like kinase 2 [Rattus norvegicus].
ACCESSION   NP_001007618 XP_223108
VERSION     NP_001007618.1
DBSOURCE    REFSEQ: accession NM_001007617.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Humbert,N., Navaratnam,N., Augert,A., Da Costa,M., Martien,S.,
            Wang,J., Martinez,D., Abbadie,C., Carling,D., de Launoit,Y., Gil,J.
            and Bernard,D.
  TITLE     Regulation of ploidy and senescence by the AMPK-related kinase
            NUAK1
  JOURNAL   EMBO J 29 (2), 376-386 (2010)
   PUBMED   19927127
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Lefebvre,D.L. and Rosen,C.F.
  TITLE     Regulation of SNARK activity in response to cellular stresses
  JOURNAL   Biochim Biophys Acta 1724 (1-2), 71-85 (2005)
   PUBMED   15893879
  REMARK    GeneRIF: SNARK (SNF1/AMP-activated protein kinase) activity is
            regulated by a broad range of cellular stresses in a
            cell-type-specific manner.
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Legembre,P., Schickel,R., Barnhart,B.C. and Peter,M.E.
  TITLE     Identification of SNF1/AMP kinase-related kinase as an
            NF-kappaB-regulated anti-apoptotic kinase involved in CD95-induced
            motility and invasiveness
  JOURNAL   J Biol Chem 279 (45), 46742-46747 (2004)
   PUBMED   15345718
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Lizcano,J.M., Goransson,O., Toth,R., Deak,M., Morrice,N.A.,
            Boudeau,J., Hawley,S.A., Udd,L., Makela,T.P., Hardie,D.G. and
            Alessi,D.R.
  TITLE     LKB1 is a master kinase that activates 13 kinases of the AMPK
            subfamily, including MARK/PAR-1
  JOURNAL   EMBO J 23 (4), 833-843 (2004)
   PUBMED   14976552
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Suzuki,A., Kusakai,G., Kishimoto,A., Minegichi,Y., Ogura,T. and
            Esumi,H.
  TITLE     Induction of cell-cell detachment during glucose starvation through
            F-actin conversion by SNARK, the fourth member of the AMP-activated
            protein kinase catalytic subunit family
  JOURNAL   Biochem Biophys Res Commun 311 (1), 156-161 (2003)
   PUBMED   14575707
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Lefebvre,D.L., Bai,Y., Shahmolky,N., Sharma,M., Poon,R.,
            Drucker,D.J. and Rosen,C.F.
  TITLE     Identification and characterization of a novel
            sucrose-non-fermenting protein kinase/AMP-activated protein
            kinase-related protein kinase, SNARK
  JOURNAL   Biochem J 355 (Pt 2), 297-305 (2001)
   PUBMED   11284715
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081899.1.
            
            On Nov 29, 2004 this sequence version replaced XP_223108.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081899.1, SRR8487231.5064.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..630
                     /product="NUAK family SNF1-like kinase 2"
                     /EC_number="2.7.11.1"
                     /note="SNF1/AMP kinase-related kinase; SNF1/AMP-activated
                     protein kinase; NUAK family, SNF1-like kinase, 2"
                     /calculated_mol_wt=69822
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H093; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     Region          53..307
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(63..66,69,71,83,85,117,133..136,179,183..184,186,
                     196..197)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271063"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H093; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     Region          361..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE5.1)"
     Region          521..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE5.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H093; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H093; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H093; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BZN4; propagated from
                     UniProtKB/Swiss-Prot (Q66HE5.1)"
     CDS             1..630
                     /gene="Nuak2"
                     /gene_synonym="1200013b22rik; Snark; UV126"
                     /coded_by="NM_001007617.1:73..1965"
                     /db_xref="GeneID:289419"
                     /db_xref="RGD:1359167"
ORIGIN      
        1 mesvalhrrg nlapsasala tesarpladr likspkplmk kqavkrhhhk hnlrhryefl
       61 etlgkgtygk vkkaressgr lvaiksirkd kikdeqdllh irreieimss lnhphiiaih
      121 evfensskiv ivmeyasrgd lydyiserpr lnerdarhff rqivsalhyc hqngivhrdl
      181 klenilldas gnikiadfgl snlyhkgkfl qtfcgsplya speivngkpy vgpevdswsl
      241 gvllyilvhg tmpfdgqdhk tlvkqissga yrepckpsda cglirwllmv npirratled
      301 vashwwvnwg ystrigeqea lregghpsgd sgrasmadwl rrssrpllen gakvcsffkq
      361 hvpgggstgp glerqhslkk srkendmaqt lqndpaedts srpgknslkl pkgilkkkas
      421 pssgevqegp qelrpvsntp gqpvpaipll prkgilkksr qresgyyssp epsesgelld
      481 agdvfvsgdp meqkspqasg rlhrkgilkl ngkfsrtale gtapstfgsl dqlasphpta
      541 rasrpsgavs edsilssesf dqldlperlp etplrgcvsv dnlrrleqpp seglkrwwqe
      601 slgdscfslt dcqevtaayr qalgicskls
//
LOCUS       NP_001014010             333 aa            linear   ROD 27-APR-2025
DEFINITION  starch-binding domain-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001014010 XP_223233
VERSION     NP_001014010.1
DBSOURCE    REFSEQ: accession NM_001013988.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Sun,T., Yi,H., Yang,C., Kishnani,P.S. and Sun,B.
  TITLE     Starch Binding Domain-containing Protein 1 Plays a Dominant Role in
            Glycogen Transport to Lysosomes in Liver
  JOURNAL   J Biol Chem 291 (32), 16479-16484 (2016)
   PUBMED   27358407
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Zhu,Y., Zhang,M., Kelly,A.R. and Cheng,A.
  TITLE     The carbohydrate-binding domain of overexpressed STBD1 is important
            for its stability and protein-protein interactions
  JOURNAL   Biosci Rep 34 (4), e00117 (2014)
   PUBMED   24837458
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Jiang,S., Wells,C.D. and Roach,P.J.
  TITLE     Starch-binding domain-containing protein 1 (Stbd1) and glycogen
            metabolism: Identification of the Atg8 family interacting motif
            (AIM) in Stbd1 required for interaction with GABARAPL1
  JOURNAL   Biochem Biophys Res Commun 413 (3), 420-425 (2011)
   PUBMED   21893048
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Jiang,S., Heller,B., Tagliabracci,V.S., Zhai,L., Irimia,J.M.,
            DePaoli-Roach,A.A., Wells,C.D., Skurat,A.V. and Roach,P.J.
  TITLE     Starch binding domain-containing protein 1/genethonin 1 is a novel
            participant in glycogen metabolism
  JOURNAL   J Biol Chem 285 (45), 34960-34971 (2010)
   PUBMED   20810658
  REMARK    GeneRIF: Stbd1 is involved in glycogen metabolism by binding to
            glycogen and anchoring it to membranes, thereby affecting its
            cellular localization and its intracellular trafficking to
            lysosomes.
            Erratum:[J Biol Chem. 2011 Nov 11;286(45):39673]
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Bouju,S., Lignon,M.F., Pietu,G., Le Cunff,M., Leger,J.J.,
            Auffray,C. and Dechesne,C.A.
  TITLE     Molecular cloning and functional expression of a novel human gene
            encoding two 41-43 kDa skeletal muscle internal membrane proteins
  JOURNAL   Biochem J 335 (Pt 3) (Pt 3), 549-556 (1998)
   PUBMED   9794794
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089867.1.
            
            On Apr 20, 2005 this sequence version replaced XP_223233.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089867.1, FN806271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..333
                     /product="starch-binding domain-containing protein 1"
                     /note="genethonin-1; glycophagy cargo receptor stbd1"
                     /calculated_mol_wt=35363
     Site            7..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Region          31..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Region          106..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95210; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Region          181..187
                     /region_name="LIR. /evidence=ECO:0000250|UniProtKB:O95210"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95210; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95210; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C7E7; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN1.1)"
     Region          239..333
                     /region_name="CBM20_genethonin_1"
                     /note="Genethonin-1, C-terminal CBM20
                     (carbohydrate-binding module, family 20) domain.
                     Genethonin-1 is a human skeletal muscle protein with no
                     known function. It contains a C-terminal CBM20 domain. The
                     CBM20 domain is found in a large number of starch...;
                     cd05813"
                     /db_xref="CDD:99887"
     Site            order(250..255,278,280,282)
                     /site_type="other"
                     /note="starch binding site 2 [chemical binding]"
                     /db_xref="CDD:99887"
     Site            order(268,297,309..310,314)
                     /site_type="other"
                     /note="starch binding site 1 [chemical binding]"
                     /db_xref="CDD:99887"
     CDS             1..333
                     /gene="Stbd1"
                     /gene_synonym="RGD1311800"
                     /coded_by="NM_001013988.1:57..1058"
                     /db_xref="GeneID:305234"
                     /db_xref="RGD:1311800"
ORIGIN      
        1 mgavwsallv ggglagalil wllrgdsgap gkdggaeplk dappgeaaap gggpggggsg
       61 glspepsdre lvskaehlre snghlisesk dlgnlteaqr lqnvgnarey vpvgkvpdth
      121 sransetsrn qspesrvgew rlpkghetav kvagsvaekl psssplmdra eaaslaqsag
      181 hedwevvsrh sswgsvglgg sleasrlsln qgmdesrnsl vgggwevdgk vvsvkprqvs
      241 iqfkvhysts tdvqfiavtg dheslggwnt yiplhyckdg lwshsvflpa dtvvewkfvl
      301 venkevtrwe ecsnrrlqtg hedkvvhgww gih
//
LOCUS       NP_955402                483 aa            linear   ROD 27-APR-2025
DEFINITION  keratin, type II cytoskeletal 8 [Rattus norvegicus].
ACCESSION   NP_955402 XP_343336
VERSION     NP_955402.1
DBSOURCE    REFSEQ: accession NM_199370.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Wang,D., Shang,Q., Mao,J., Gao,C., Wang,J., Wang,D., Wang,H.,
            Jia,H., Peng,P., Du,M., Luo,Z. and Yang,L.
  TITLE     Phosphorylation of KRT8 (keratin 8) by excessive mechanical
            load-activated PKN (protein kinase N) impairs autophagosome
            initiation and contributes to disc degeneration
  JOURNAL   Autophagy 19 (9), 2485-2503 (2023)
   PUBMED   36897022
  REMARK    GeneRIF: Phosphorylation of KRT8 (keratin 8) by excessive
            mechanical load-activated PKN (protein kinase N) impairs
            autophagosome initiation and contributes to disc degeneration.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Wogenstein,K.L., Szabo,S., Lunova,M., Wiche,G., Haybaeck,J.,
            Strnad,P., Boor,P., Wagner,M. and Fuchs,P.
  TITLE     Epiplakin deficiency aggravates murine caerulein-induced acute
            pancreatitis and favors the formation of acinar keratin granules
  JOURNAL   PLoS One 9 (9), e108323 (2014)
   PUBMED   25232867
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Bell,S.M., Zhang,L., Xu,Y., Besnard,V., Wert,S.E., Shroyer,N. and
            Whitsett,J.A.
  TITLE     Kruppel-like factor 5 controls villus formation and initiation of
            cytodifferentiation in the embryonic intestinal epithelium
  JOURNAL   Dev Biol 375 (2), 128-139 (2013)
   PUBMED   23266329
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Bordeleau,F., Myrand Lapierre,M.E., Sheng,Y. and Marceau,N.
  TITLE     Keratin 8/18 regulation of cell stiffness-extracellular matrix
            interplay through modulation of Rho-mediated actin cytoskeleton
            dynamics
  JOURNAL   PLoS One 7 (6), e38780 (2012)
   PUBMED   22685604
  REMARK    GeneRIF: Results indicate a keratins K8/K18 intermediate filament
            (IF) contribution to the cell stiffness-extracellular matrix (ECM)
            interplay through a modulation of Rho-dependent actin organization.
REFERENCE   5  (residues 1 to 483)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Caulin,C., Ware,C.F., Magin,T.M. and Oshima,R.G.
  TITLE     Keratin-dependent, epithelial resistance to tumor necrosis
            factor-induced apoptosis
  JOURNAL   J Cell Biol 149 (1), 17-22 (2000)
   PUBMED   10747083
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Ando,S., Tokui,T., Yano,T. and Inagaki,M.
  TITLE     Keratin 8 phosphorylation in vitro by cAMP-dependent protein kinase
            occurs within the amino- and carboxyl-terminal end domains
  JOURNAL   Biochem Biophys Res Commun 221 (1), 67-71 (1996)
   PUBMED   8660345
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Wang,X., Hsieh,J.T. and Zhau,H.E.
  TITLE     [Cloning and characterization of a specific cytokeratin-8 cDNA from
            rat prostatic epithelium]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 16 (1), 1-7 (1994)
   PUBMED   7525090
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Hsieh,J.T., Zhau,H.E., Wang,X.H., Liew,C.C. and Chung,L.W.
  TITLE     Regulation of basal and luminal cell-specific cytokeratin
            expression in rat accessory sex organs. Evidence for a new class of
            androgen-repressed genes and insight into their pairwise control
  JOURNAL   J Biol Chem 267 (4), 2303-2310 (1992)
   PUBMED   1370816
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Yano,T., Tokui,T., Nishi,Y., Nishizawa,K., Shibata,M., Kikuchi,K.,
            Tsuiki,S., Yamauchi,T. and Inagaki,M.
  TITLE     Phosphorylation of keratin intermediate filaments by protein kinase
            C, by calmodulin-dependent protein kinase and by cAMP-dependent
            protein kinase
  JOURNAL   Eur J Biochem 197 (2), 281-290 (1991)
   PUBMED   1709097
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY464139.1.
            
            On Jan 11, 2004 this sequence version replaced XP_343336.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY464139.1, BC097497.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132303, SAMD00132305
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..483
                     /product="keratin, type II cytoskeletal 8"
                     /note="K8; CK-8; cytokeratin-8; cytokeratin endo A;
                     type-II keratin Kb8; keratin complex 2, basic, gene 8;
                     keratin 8, type II"
                     /calculated_mol_wt=53888
     Region          1..90
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCE.
                     /evidence=ECO:0000305|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            23
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; Phosphoserine, by
                     PKC/PRKCE. /evidence=ECO:0000305|PubMed:8660345,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            32
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            40
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            49
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05787;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Region          <63..87
                     /region_name="Keratin_2_head"
                     /note="Keratin type II head; pfam16208"
                     /db_xref="CDD:465068"
     Region          90..401
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          91..126
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Region          127..143
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Region          144..235
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Region          236..259
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Region          260..398
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Region          261..382
                     /region_name="Necessary for interaction with PNN.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            325
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            342
                     /site_type="other"
                     /note="Stutter; propagated from UniProtKB/Swiss-Prot
                     (Q10758.3)"
     Region          399..483
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10758.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8660345; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05787; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q10758.3)"
     CDS             1..483
                     /gene="Krt8"
                     /gene_synonym="CYKER; Krt2-8"
                     /coded_by="NM_199370.1:1..1452"
                     /db_xref="GeneID:25626"
                     /db_xref="RGD:2984"
ORIGIN      
        1 msvrvtqksy kmstsgpraf ssrsftsgpg arissssfsr vgsssssfrg slggfggagv
       61 ggitavtvnq sllnplklev dpniqavrtq ekeqiktlnn kfasfidkvr fleqqnkmle
      121 tkwsllqqqk tsrsnmdnmf esyinnlrrq lealgqeklk levelgnmqg lvedfknkye
      181 deinkrteme nefvlikkdv deaymnkvel esrlegltde inflrqihee eirelqsqis
      241 dtsvvlsmdn srsldmdsii aevraqyeei anrsraeaet myqikyeelq tlagkhgddl
      301 rrskteisem nrnisrlqae idalkgqrat leaaiadaeq rgelavkdan akledlknal
      361 qkakqdmarq lreyqelmnv klaldieiat yrkllegees rlesgmqnms ihtkttsgya
      421 gglsssyggl tspgfsygms sfqpgfgsvg gsstysrtka vvvkkietrd gklvsessdi
      481 msk
//
LOCUS       NP_001004091             637 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-17 receptor E precursor [Rattus norvegicus].
ACCESSION   NP_001004091 XP_342739
VERSION     NP_001004091.1
DBSOURCE    REFSEQ: accession NM_001004091.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078742.1.
            
            On Sep 6, 2004 this sequence version replaced XP_342739.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132265, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..637
                     /product="interleukin-17 receptor E precursor"
                     /note="IL-17RE; IL-17 receptor E"
                     /calculated_mol_wt=68385
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2485
     mat_peptide     25..637
                     /product="Interleukin-17 receptor E. /id=PRO_0000309469"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AZ51.1)"
                     /calculated_mol_wt=68385
     Region          38..408
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AZ51.1)"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AZ51.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AZ51.1)"
     Region          448..570
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..637
                     /gene="Il17re"
                     /coded_by="NM_001004091.1:75..1988"
                     /db_xref="GeneID:362417"
                     /db_xref="RGD:735148"
ORIGIN      
        1 mgsprlaall lsqpllficl avsaqvacpc lprwtshcll afrvdkhfag lqcgwfpllv
       61 rksksshefe vcwrhwtpsp fqrkllgsps lsqeshrist hflaishrgl rtkrtqpsaa
      121 egiehlpgag sqkhggpefs fdllpevqai rvtippgpea nvrlcyqwal ecedmsspfd
      181 tqkivsgght vdlpyefllp cmcieasylq edtvrhkkcp frswpeaygs dfwksirftd
      241 ysqhsqmvma ltlrcplkle aslcwrqdpv tpckilpnat akesegwyil envdlhpqlc
      301 fkfsfenssh vecphqsgsl pswtvsmdtq aqqlilhfst rtyatfsaaw snpglgldss
      361 mtpvysisqt qgsvpvtlnl iipflrqgsc ilvwrsdvqf awkhllcpdv shrhlgllil
      421 allglttllg vvlvlfcrrl lpgpgrtrpv lllhaadsea qrrlvgalae llrtalgggr
      481 dvivdlwegt hvarigplpw lwaarervar eqgtvlllws cagpstacsg dpqtaslrtl
      541 scaaprqlll ayfsrlcakg dipgplralp ryrllrdlpr llraldarpa tlatswshlg
      601 akeclksrle lchlleleaa kddyhgstns pcgfscl
//
LOCUS       NP_036787                786 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Sp1 [Rattus norvegicus].
ACCESSION   NP_036787
VERSION     NP_036787.2
DBSOURCE    REFSEQ: accession NM_012655.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Vaghf,A., Sadegh,M., Khansarinejad,B. and Mondanizadeh,M.
  TITLE     MicroRNA-124-3p targets Sp1 transcription factor to regulate glioma
            progression in rats
  JOURNAL   Gene 930, 148858 (2024)
   PUBMED   39153708
  REMARK    GeneRIF: MicroRNA-124-3p targets Sp1 transcription factor to
            regulate glioma progression in rats.
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Shen,C., Peng,C., Zhang,S., Li,R., Liu,S., Kuang,Y., Su,F., Liu,Y.,
            Liang,L., Xiao,Y. and Xu,H.
  TITLE     Eukaryotic translation initiation factor 6-mediated ribosome
            biogenesis promotes synovial aggression and inflammation by
            increasing the translation of SP1 in rheumatoid arthritis
  JOURNAL   Int Immunopharmacol 142 (Pt B), 113164 (2024)
   PUBMED   39288622
  REMARK    GeneRIF: Eukaryotic translation initiation factor 6-mediated
            ribosome biogenesis promotes synovial aggression and inflammation
            by increasing the translation of SP1 in rheumatoid arthritis.
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Li,Y., Cheng,M., Jin,J., Zhang,D., Zhang,S., Bai,Y. and Xu,J.
  TITLE     Interaction of Sp1 and Setd8 promotes vascular smooth muscle cells
            apoptosis by activating Mark4 in vascular calcification
  JOURNAL   Aging (Albany NY) 16 (3), 2438-2456 (2024)
   PUBMED   38301049
  REMARK    GeneRIF: Interaction of Sp1 and Setd8 promotes vascular smooth
            muscle cells apoptosis by activating Mark4 in vascular
            calcification.
REFERENCE   4  (residues 1 to 786)
  AUTHORS   Xu,L.J., Yang,Y., Yuan,L.F., Liu,H., Xu,N.P., Yang,Y. and Huang,L.
  TITLE     SP1-stimulated miR-208a-5p aggravates sepsis-induced myocardial
            injury via targeting XIAP
  JOURNAL   Exp Cell Res 435 (1), 113905 (2024)
   PUBMED   38163563
  REMARK    GeneRIF: SP1-stimulated miR-208a-5p aggravates sepsis-induced
            myocardial injury via targeting XIAP.
REFERENCE   5  (residues 1 to 786)
  AUTHORS   Li,X.H., Fu,J.J., Shi,X.J., Zhang,Y.N., Shao,M., Yue,S.J., Li,C.
            and Luo,Z.Q.
  TITLE     Sp1 mediated the inhibitory effect of glutamate on pulmonary
            surfactant synthesis
  JOURNAL   PLoS One 18 (8), e0289530 (2023)
   PUBMED   37556489
  REMARK    GeneRIF: Sp1 mediated the inhibitory effect of glutamate on
            pulmonary surfactant synthesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 786)
  AUTHORS   Kovacs,P., Voigt,B. and Kloting,I.
  TITLE     Novel quantitative trait loci for blood pressure and related traits
            on rat chromosomes 1, 10, and 18
  JOURNAL   Biochem Biophys Res Commun 235 (2), 343-348 (1997)
   PUBMED   9199194
REFERENCE   7  (residues 1 to 786)
  AUTHORS   Rajput,B., Shaper,N.L. and Shaper,J.H.
  TITLE     Transcriptional regulation of murine beta1,4-galactosyltransferase
            in somatic cells. Analysis of a gene that serves both a
            housekeeping and a mammary gland-specific function
  JOURNAL   J Biol Chem 271 (9), 5131-5142 (1996)
   PUBMED   8617793
REFERENCE   8  (residues 1 to 786)
  AUTHORS   Imataka,H., Sogawa,K., Yasumoto,K., Kikuchi,Y., Sasano,K.,
            Kobayashi,A., Hayami,M. and Fujii-Kuriyama,Y.
  TITLE     Two regulatory proteins that bind to the basic transcription
            element (BTE), a GC box sequence in the promoter region of the rat
            P-4501A1 gene
  JOURNAL   EMBO J 11 (10), 3663-3671 (1992)
   PUBMED   1356762
REFERENCE   9  (residues 1 to 786)
  AUTHORS   Nehls,M.C., Grapilon,M.L. and Brenner,D.A.
  TITLE     NF-I/Sp1 switch elements regulate collagen alpha 1(I) gene
            expression
  JOURNAL   DNA Cell Biol 11 (6), 443-452 (1992)
   PUBMED   1524678
REFERENCE   10 (residues 1 to 786)
  AUTHORS   Mermod,N., Williams,T.J. and Tjian,R.
  TITLE     Enhancer binding factors AP-4 and AP-1 act in concert to activate
            SV40 late transcription in vitro
  JOURNAL   Nature 332 (6164), 557-561 (1988)
   PUBMED   2833704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Jan 1, 2008 this sequence version replaced NP_036787.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.219836.1,
                                           SRR26360176.172451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..786
                     /product="transcription factor Sp1"
                     /note="trans-acting transcription factor 1"
                     /calculated_mol_wt=80641
     Region          1..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          2..83
                     /region_name="Repressor domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          55..628
                     /region_name="SP1_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Protein (SP) 1; cd22539"
                     /db_xref="CDD:411775"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            64..65
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          110..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          147..252
                     /region_name="Transactivation domain A (Gln-rich).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          262..496
                     /region_name="Transactivation domain B (Gln-rich).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          281..303
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          332..397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1 and MAPK3.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          463..471
                     /region_name="9aaTAD.
                     /evidence=ECO:0000250|UniProtKB:P08047"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            492
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          497..611
                     /region_name="Transactivation domain C (highly charged).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          562..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            613
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          620..786
                     /region_name="VZV IE62-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Region          627..651
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          629..651
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(636,638,640,642..643,646..647,650,666,668,672..673,
                     676..677,680,694,696,698,700..701,704..705,708)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            641
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            642
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCZ, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          643..670
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCZ.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          659..681
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCZ.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          673..696
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCZ.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          687..709
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          689..709
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            699
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            703
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Site            704
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     Region          709..786
                     /region_name="Domain D. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01714.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1, MAPK3 and MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P08047; propagated from
                     UniProtKB/Swiss-Prot (Q01714.2)"
     CDS             1..786
                     /gene="Sp1"
                     /coded_by="NM_012655.2:39..2399"
                     /db_xref="GeneID:24790"
                     /db_xref="RGD:3738"
ORIGIN      
        1 msdqdhsmde vtavkiekgv ggnnggsgng ggaafsqtrs sstgsssssg ggggqesqps
       61 plallaatcs riespnensn nsqgpsqsgg tgeldltatq lsqgangwqi issssgatpt
      121 skeqsgnstn gsngsesskn rtvsggqyvv aatpnlqnqq vltglpgvmp niqyqvipqf
      181 qtvdgqqlqf aatgaqvqqd gsgqiqiipg anqqiitnrg sggniiaamp nllqqavplq
      241 glannvlsgq tqyvtnvpva lngnitllpv nsvsaatltp ssqagtisss gsqesgsqpv
      301 tsgtaissas lvssqassss fftnansyst ttttsnmgim nftssgssgt ssqgqtsqrv
      361 gglqgsdsln iqqnqtsggs lqgsqqkege qsqqtqqqqi liqpqlvqgg qalqalqaap
      421 lsgqtfttqa isqetlqnlq lqavqnsgpi iirtptvgpn gqvswqtlql qnlqvqnpqa
      481 qtitlapmqg vslgqtsssn ttltpiasaa sipagtvtvn aaqlssmpgl qtinlsalgt
      541 sgiqvhqlpg lplaiantpg dhgaqlglhg pggdgihdet aggeegensp dpqpqagrrt
      601 rreactcpyc kdsegrgsgd pgkkkqhich iqgcgkvygk tshlrahlrw htgerpfmcn
      661 wsycgkrftr sdelqrhkrt htgekkfacp ecpkrfmrsd hlskhikthq nkkggpgval
      721 svgtlpldsg agsegsgtat psalittnmv ameaicpegi arlansginv mqvtelqsin
      781 isgngf
//
LOCUS       NP_036899                 92 aa            linear   ROD 27-APR-2025
DEFINITION  progonadoliberin-1 precursor [Rattus norvegicus].
ACCESSION   NP_036899
VERSION     NP_036899.1
DBSOURCE    REFSEQ: accession NM_012767.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Zang,S., Yin,X. and Li,P.
  TITLE     FTO-mediated m6A demethylation regulates GnRH expression in the
            hypothalamus via the PLCbeta3/Ca2+/CAMK signalling pathway
  JOURNAL   Commun Biol 6 (1), 1297 (2023)
   PUBMED   38129517
  REMARK    GeneRIF: FTO-mediated m[6]A demethylation regulates GnRH expression
            in the hypothalamus via the PLCbeta3/Ca[2+]/CAMK signalling
            pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Laoharatchatathanin,T., Rieanrakwong,D., Hatsugai,Y., Terashima,R.,
            Yonezawa,T., Kurusu,S. and Kawaminami,M.
  TITLE     Mast Cell Dynamics in the Ovary Are Governed by GnRH and Prolactin
  JOURNAL   Endocrinology 164 (11) (2023)
   PUBMED   37797313
  REMARK    GeneRIF: Mast Cell Dynamics in the Ovary Are Governed by GnRH and
            Prolactin.
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Kanasaki,H., Tumurbaatar,T., Tumurgan,Z., Oride,A., Okada,H. and
            Kyo,S.
  TITLE     Mutual Interactions Between GnRH and Kisspeptin in GnRH- and
            Kiss-1-Expressing Immortalized Hypothalamic Cell Models
  JOURNAL   Reprod Sci 28 (12), 3380-3389 (2021)
   PUBMED   34268716
  REMARK    GeneRIF: Mutual Interactions Between GnRH and Kisspeptin in GnRH-
            and Kiss-1-Expressing Immortalized Hypothalamic Cell Models.
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Xu,W., Huang,J., Li,L., Zhang,X., Wang,Y., Tong,G. and Sun,Y.
  TITLE     Alterations of estradiol-induced histone H3 acetylation in the
            preoptic area and anteroventral periventricular nucleus of
            middle-aged female rats
  JOURNAL   Biochem Biophys Res Commun 516 (3), 894-899 (2019)
   PUBMED   31272713
  REMARK    GeneRIF: The data suggest that alterations of histone H3
            acetylation in the preoptic area and anteroventral periventricular
            nucleus and the inability of Ncoa2 and Crebbp to respond to
            estradiol in the middle-aged anterior hypothalamus partially
            contribute to the decline of GnRH neuron activation and estradiol
            target gene expression changes that occur in females along with
            reproductive aging.
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Melnikova,V.I., Lifantseva,N.V., Voronova,S.N. and Zakharova,L.A.
  TITLE     Gonadotropin-Releasing Hormone in Regulation of Thymic Development
            in Rats: Profile of Thymic Cytokines
  JOURNAL   Int J Mol Sci 20 (16), 4033 (2019)
   PUBMED   31430847
  REMARK    GeneRIF: The data obtained confirm the regulatory or morphogenetic
            effect of GnRH on fetal thymus development mediated by synthesis of
            thymic cytokines.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Maier,C.C., Marchetti,B., LeBoeuf,R.D. and Blalock,J.E.
  TITLE     Thymocytes express a mRNA that is identical to hypothalamic
            luteinizing hormone-releasing hormone mRNA
  JOURNAL   Cell Mol Neurobiol 12 (5), 447-454 (1992)
   PUBMED   1468115
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Tsuruo,Y., Kawano,H., Kagotani,Y., Hisano,S., Daikoku,S.,
            Chihara,K., Zhang,T. and Yanaihara,N.
  TITLE     Morphological evidence for neuronal regulation of luteinizing
            hormone-releasing hormone-containing neurons by neuropeptide Y in
            the rat septo-preoptic area
  JOURNAL   Neurosci Lett 110 (3), 261-266 (1990)
   PUBMED   2183089
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Bond,C.T., Hayflick,J.S., Seeburg,P.H. and Adelman,J.P.
  TITLE     The rat gonadotropin-releasing hormone: SH locus: structure and
            hypothalamic expression
  JOURNAL   Mol Endocrinol 3 (8), 1257-1262 (1989)
   PUBMED   2476669
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Merchenthaler,I., Culler,M.D., Negro-Vilar,A., Petrusz,P. and
            Flerko,B.
  TITLE     The Pro-LHRH system of the rat brain. Effects of changes in the
            endocrine background
  JOURNAL   Brain Res Bull 20 (6), 713-720 (1988)
   PUBMED   3044520
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Adelman,J.P., Mason,A.J., Hayflick,J.S. and Seeburg,P.H.
  TITLE     Isolation of the gene and hypothalamic cDNA for the common
            precursor of gonadotropin-releasing hormone and prolactin
            release-inhibiting factor in human and rat
  JOURNAL   Proc Natl Acad Sci U S A 83 (1), 179-183 (1986)
   PUBMED   2867548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M12579.1 and CR463456.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M12579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132302, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..92
                     /product="progonadoliberin-1 precursor"
                     /note="progonadoliberin-1; luteinizing hormone-releasing
                     hormone; progonadoliberin I; gonadotropin-releasing
                     hormone 1 (luteinizing-releasing hormone); Putative
                     protein SH"
                     /calculated_mol_wt=8109
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2409
     mat_peptide     24..92
                     /product="gonadotropin-releasing hormone 1"
                     /calculated_mol_wt=8109
     Site            24
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P01148; propagated from
                     UniProtKB/Swiss-Prot (P07490.1)"
     Site            26..27
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000250|UniProtKB:P01148; propagated from
                     UniProtKB/Swiss-Prot (P07490.1)"
     Site            26
                     /site_type="other"
                     /note="Appears to be essential for biological activity;
                     propagated from UniProtKB/Swiss-Prot (P07490.1)"
     Site            28..29
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000250|UniProtKB:P01148; propagated from
                     UniProtKB/Swiss-Prot (P07490.1)"
     Site            30..31
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000250|UniProtKB:P01148; propagated from
                     UniProtKB/Swiss-Prot (P07490.1)"
     Site            33..34
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000250|UniProtKB:P01148; propagated from
                     UniProtKB/Swiss-Prot (P07490.1)"
     Site            33
                     /site_type="amidation"
                     /note="Glycine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P07490.1)"
     CDS             1..92
                     /gene="Gnrh1"
                     /gene_synonym="Gnrh; Gnrha; Lhrh; Rgnrhg1; SH-4"
                     /coded_by="NM_012767.2:33..311"
                     /db_xref="GeneID:25194"
                     /db_xref="RGD:2720"
ORIGIN      
        1 metipklmaa vvlltvcleg cssqhwsygl rpggkrnteh lvdsfqemgk eedqmaepqn
       61 fectvhwprs plrdlrgale rlieeeagqk km
//
LOCUS       NP_446060                360 aa            linear   ROD 27-APR-2025
DEFINITION  inward rectifier potassium channel 13 [Rattus norvegicus].
ACCESSION   NP_446060
VERSION     NP_446060.1
DBSOURCE    REFSEQ: accession NM_053608.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Zietara,A., Palygin,O., Levchenko,V., Dissanayake,L.V.,
            Klemens,C.A., Geurts,A., Denton,J.S. and Staruschenko,A.
  TITLE     Kir7.1 knockdown and inhibition alter renal electrolyte handling
            but not the development of hypertension in Dahl salt-sensitive rats
  JOURNAL   Am J Physiol Renal Physiol 325 (2), F177-F187 (2023)
   PUBMED   37318990
  REMARK    GeneRIF: Kir7.1 knockdown and inhibition alter renal electrolyte
            handling but not the development of hypertension in Dahl
            salt-sensitive rats.
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Villanueva,S., Burgos,J., Lopez-Cayuqueo,K.I., Lai,K.M.,
            Valenzuela,D.M., Cid,L.P. and Sepulveda,F.V.
  TITLE     Cleft Palate, Moderate Lung Developmental Retardation and Early
            Postnatal Lethality in Mice Deficient in the Kir7.1 Inwardly
            Rectifying K+ Channel
  JOURNAL   PLoS One 10 (9), e0139284 (2015)
   PUBMED   26402555
  REMARK    GeneRIF: Kir7.1 is expressed in epithelial cells all along the
            respiratory tree.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Zhang,W., Zhang,X., Wang,H., Sharma,A.K., Edwards,A.O. and
            Hughes,B.A.
  TITLE     Characterization of the R162W Kir7.1 mutation associated with
            snowflake vitreoretinopathy
  JOURNAL   Am J Physiol Cell Physiol 304 (5), C440-C449 (2013)
   PUBMED   23255580
  REMARK    GeneRIF: Mutant subunits did not alter Kir7.1 channel selectivity.
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Tateno,T., Nakamura,N., Hirata,Y. and Hirose,S.
  TITLE     Role of C-terminus of Kir7.1 potassium channel in cell-surface
            expression
  JOURNAL   Cell Biol Int 30 (3), 270-277 (2006)
   PUBMED   16406822
  REMARK    GeneRIF: results suggest that the C-terminal length plays an
            important role in the plasma-membrane localization of Kir7.1
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Dong,K., Tang,L.Q., MacGregor,G.G., Leng,Q. and Hebert,S.C.
  TITLE     Novel nucleotide-binding sites in ATP-sensitive potassium channels
            formed at gating interfaces
  JOURNAL   EMBO J 24 (7), 1318-1329 (2005)
   PUBMED   15775962
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Suzuki,Y., Yasuoka,Y., Shimohama,T., Nishikitani,M., Nakamura,N.,
            Hirose,S. and Kawahara,K.
  TITLE     Expression of the K+ channel Kir7.1 in the developing rat kidney:
            role in K+ excretion
  JOURNAL   Kidney Int 63 (3), 969-975 (2003)
   PUBMED   12631077
  REMARK    GeneRIF: Kir7.1 is involved in the development of renal K+
            excretion between 14 and 21 days after birth under the condition of
            K+ overload.
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Doring,F. and Karschin,A.
  TITLE     Genomic structure and promoter analysis of the rat kir7.1 potassium
            channel gene (Kcnj13)
  JOURNAL   FEBS Lett 483 (2-3), 93-98 (2000)
   PUBMED   11042260
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Nakamura,N., Suzuki,Y., Ikeda,Y., Notoya,M. and Hirose,S.
  TITLE     Complex structure and regulation of expression of the rat gene for
            inward rectifier potassium channel Kir7.1
  JOURNAL   J Biol Chem 275 (36), 28276-28284 (2000)
   PUBMED   10871613
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Nakamura,N., Suzuki,Y., Sakuta,H., Ookata,K., Kawahara,K. and
            Hirose,S.
  TITLE     Inwardly rectifying K+ channel Kir7.1 is highly expressed in
            thyroid follicular cells, intestinal epithelial cells and choroid
            plexus epithelial cells: implication for a functional coupling with
            Na+,K+-ATPase
  JOURNAL   Biochem J 342 (Pt 2) (Pt 2), 329-336 (1999)
   PUBMED   10455019
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Doring,F., Derst,C., Wischmeyer,E., Karschin,C.,
            Schneggenburger,R., Daut,J. and Karschin,A.
  TITLE     The epithelial inward rectifier channel Kir7.1 displays unusual K+
            permeation properties
  JOURNAL   J Neurosci 18 (21), 8625-8636 (1998)
   PUBMED   9786970
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB013890.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV213333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..360
                     /product="inward rectifier potassium channel 13"
                     /note="inward rectifier K(+) channel Kir7.1; potassium
                     channel, inwardly rectifying subfamily J member 13;
                     potassium voltage-gated channel subfamily J member 13"
                     /calculated_mol_wt=40506
     Region          21..163
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            51..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70617.1)"
     Region          119..124
                     /region_name="Selectivity filter. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O70617.1)"
     Site            132..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70617.1)"
     Site            149
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O70617.1)"
     Region          170..331
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:O60928; propagated from
                     UniProtKB/Swiss-Prot (O70617.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:O60928; propagated from
                     UniProtKB/Swiss-Prot (O70617.1)"
     CDS             1..360
                     /gene="Kcnj13"
                     /gene_synonym="Kir7.1"
                     /coded_by="NM_053608.2:118..1200"
                     /db_xref="GeneID:94341"
                     /db_xref="RGD:621661"
ORIGIN      
        1 mdsrnckvna pllsqryrrm vtkdghstlq mdgaqrglvy lrdawgilmd mrwrwmmlvf
       61 sasfvvhwlv favlwyavae mngdleidhd vppenhticv khitsftaaf sfsletqlti
      121 gygtmfpsgd cpsaiallai qmllglmlea fitgafvaki arpknrafsi rftdlavvah
      181 kdgkpnlifq vantrpsplt svrvsavlyq erengelyqt svdfhldgis seecpffifp
      241 ltyyhtitps splatllqhe tpshfelvvf lsamqegtge icqrrtsylp seimlhhrfa
      301 almtrgskge yqvkmenfdk tvpehptpvv sksphrtdld ihingqsidn fqiaetglte
//
LOCUS       NP_036737                169 aa            linear   ROD 27-APR-2025
DEFINITION  myosin regulatory light chain 11 [Rattus norvegicus].
ACCESSION   NP_036737
VERSION     NP_036737.1
DBSOURCE    REFSEQ: accession NM_012605.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Wang,Y., Szczesna-Cordary,D., Craig,R., Diaz-Perez,Z., Guzman,G.,
            Miller,T. and Potter,J.D.
  TITLE     Fast skeletal muscle regulatory light chain is required for fast
            and slow skeletal muscle development
  JOURNAL   FASEB J 21 (9), 2205-2214 (2007)
   PUBMED   17356007
  REMARK    Erratum:[FASEB J. 2007 Aug;21(10):2633]
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Liu,X., Lindberg,R., Xiao,B.G., Steffensen,K.R., Leppert,D.,
            Link,H. and Huang,Y.M.
  TITLE     CD24 and myosin light polypeptide 2 are involved in prevention of
            experimental autoimmune encephalomyelitis by myelin basic
            protein-pulsed dendritic cells
  JOURNAL   J Neuroimmunol 172 (1-2), 137-144 (2006)
   PUBMED   16380169
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Leszczynski,J.K. and Esser,K.A.
  TITLE     The MEF2 site is necessary for induction of the myosin light chain
            2 slow promoter in overloaded regenerating plantaris muscle
  JOURNAL   Life Sci 73 (25), 3265-3276 (2003)
   PUBMED   14561531
  REMARK    GeneRIF: results demonstrate that the -270MLC2s promoter contains
            the elements necessary for expression of MLC2s in regenerating
            overloaded plantaris muscle
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Andersen,P.S., Havndrup,O., Bundgaard,H., Moolman-Smook,J.C.,
            Larsen,L.A., Mogensen,J., Brink,P.A., Borglum,A.D., Corfield,V.A.,
            Kjeldsen,K., Vuust,J. and Christiansen,M.
  TITLE     Myosin light chain mutations in familial hypertrophic
            cardiomyopathy: phenotypic presentation and frequency in Danish and
            South African populations
  JOURNAL   J Med Genet 38 (12), E43 (2001)
   PUBMED   11748309
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Flavigny,J., Richard,P., Isnard,R., Carrier,L., Charron,P.,
            Bonne,G., Forissier,J.F., Desnos,M., Dubourg,O., Komajda,M.,
            Schwartz,K. and Hainque,B.
  TITLE     Identification of two novel mutations in the ventricular regulatory
            myosin light chain gene (MYL2) associated with familial and
            classical forms of hypertrophic cardiomyopathy
  JOURNAL   J Mol Med (Berl) 76 (3-4), 208-214 (1998)
   PUBMED   9535554
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Nudel,U., Calvo,J.M., Shani,M. and Levy,Z.
  TITLE     The nucleotide sequence of a rat myosin light chain 2 gene
  JOURNAL   Nucleic Acids Res 12 (18), 7175-7186 (1984)
   PUBMED   6091059
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB770854.1, BI278596.1 and JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224781.1, FQ217368.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..169
                     /product="myosin regulatory light chain 11"
                     /note="G2; DTNB; MLC-2; fast skeletal myosin light chain
                     2; Myosin, light polypeptide 2, alkali; ventricular,
                     skeletal, slow; myosin light chain, phosphorylatable, fast
                     skeletal muscle"
                     /calculated_mol_wt=18838
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine.
                     /evidence=ECO:0000250|UniProtKB:P02608; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97457; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97457; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Region          21..157
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04466.2)"
     CDS             1..169
                     /gene="Myl11"
                     /gene_synonym="MLC2; Myl2; Mylpf; Myolc1"
                     /coded_by="NM_012605.2:42..551"
                     /db_xref="GeneID:24584"
                     /db_xref="RGD:3141"
ORIGIN      
        1 mapkkakrra aaegssnvfs mfdqtqiqef keaftvidqn rdgiidkedl rdtfaamgrl
       61 nvkneeldam mkeasgpinf tvfltmfgek lkgadpedvi tgafkvldpe gkgtikkqfl
      121 eellttqcdr fsqeeiknmw aafppdvggn vdyknicyvi thgdakdqe
//
LOCUS       NP_062158               1072 aa            linear   ROD 27-APR-2025
DEFINITION  adenylate cyclase type 4 [Rattus norvegicus].
ACCESSION   NP_062158
VERSION     NP_062158.2
DBSOURCE    REFSEQ: accession NM_019285.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Bagavandoss,P. and Grimshaw,S.
  TITLE     Distribution of adenylyl cyclases in the rat ovary by
            immunofluorescence microscopy
  JOURNAL   Anat Rec (Hoboken) 295 (10), 1717-1726 (2012)
   PUBMED   22899545
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Sadana,R. and Dessauer,C.W.
  TITLE     Physiological roles for G protein-regulated adenylyl cyclase
            isoforms: insights from knockout and overexpression studies
  JOURNAL   Neurosignals 17 (1), 5-22 (2009)
   PUBMED   18948702
  REMARK    Review article
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Rhim,J.H., Jang,I.S., Yeo,E.J., Song,K.Y. and Park,S.C.
  TITLE     Role of protein kinase C-dependent A-kinase anchoring proteins in
            lysophosphatidic acid-induced cAMP signaling in human diploid
            fibroblasts
  JOURNAL   Aging Cell 5 (6), 451-461 (2006)
   PUBMED   17081159
REFERENCE   4  (residues 1 to 1072)
  AUTHORS   Wang,H.Y. and Burns,L.H.
  TITLE     Gbetagamma that interacts with adenylyl cyclase in opioid tolerance
            originates from a Gs protein
  JOURNAL   J Neurobiol 66 (12), 1302-1310 (2006)
   PUBMED   16967511
REFERENCE   5  (residues 1 to 1072)
  AUTHORS   Ostrom,R.S., Naugle,J.E., Hase,M., Gregorian,C., Swaney,J.S.,
            Insel,P.A., Brunton,L.L. and Meszaros,J.G.
  TITLE     Angiotensin II enhances adenylyl cyclase signaling via
            Ca2+/calmodulin. Gq-Gs cross-talk regulates collagen production in
            cardiac fibroblasts
  JOURNAL   J Biol Chem 278 (27), 24461-24468 (2003)
   PUBMED   12711600
REFERENCE   6  (residues 1 to 1072)
  AUTHORS   Serazin-Leroy,V., Morot,M., de Mazancourt,P. and Giudicelli,Y.
  TITLE     Differences in type II, IV, V and VI adenylyl cyclase isoform
            expression between rat preadipocytes and adipocytes
  JOURNAL   Biochim Biophys Acta 1550 (1), 37-51 (2001)
   PUBMED   11738086
REFERENCE   7  (residues 1 to 1072)
  AUTHORS   Cote,M., Guillon,G., Payet,M.D. and Gallo-Payet,N.
  TITLE     Expression and regulation of adenylyl cyclase isoforms in the human
            adrenal gland
  JOURNAL   J Clin Endocrinol Metab 86 (9), 4495-4503 (2001)
   PUBMED   11549699
REFERENCE   8  (residues 1 to 1072)
  AUTHORS   Baker,L.P., Nielsen,M.D., Impey,S., Hacker,B.M., Poser,S.W.,
            Chan,M.Y. and Storm,D.R.
  TITLE     Regulation and immunohistochemical localization of
            betagamma-stimulated adenylyl cyclases in mouse hippocampus
  JOURNAL   J Neurosci 19 (1), 180-192 (1999)
   PUBMED   9870949
REFERENCE   9  (residues 1 to 1072)
  AUTHORS   Zimmermann,G. and Taussig,R.
  TITLE     Protein kinase C alters the responsiveness of adenylyl cyclases to
            G protein alpha and betagamma subunits
  JOURNAL   J Biol Chem 271 (43), 27161-27166 (1996)
   PUBMED   8900209
REFERENCE   10 (residues 1 to 1072)
  AUTHORS   Gao,B.N. and Gilman,A.G.
  TITLE     Cloning and expression of a widely distributed (type IV) adenylyl
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 88 (22), 10178-10182 (1991)
   PUBMED   1946437
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC081813.1.
            
            On Mar 8, 2007 this sequence version replaced NP_062158.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081813.1, M80633.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132291,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..1072
                     /product="adenylate cyclase type 4"
                     /EC_number="4.6.1.1"
                     /note="ATP pyrophosphate-lyase 4; adenylate cyclase type
                     IV; adenylyl cyclase 4"
                     /calculated_mol_wt=119656
     Site            29..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Region          40..453
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Site            61..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            94..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            120..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            141..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Region          264..430
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(276,278..283,318,320..322,325,387..389,393..394,
                     397..398,437)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(278,322)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(283,295,298..299,302,306,318..319,375,378,388..391,
                     394,437)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     Region          479..581
                     /region_name="Adcy_cons_dom"
                     /note="Adenylate cyclase, conserved domain; pfam06327"
                     /db_xref="CDD:461877"
     Region          498..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P26770.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P26770.1)"
     Site            583..604
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            608..630
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Region          648..1053
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
     Site            661..684
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            694
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26770.1)"
     Site            701
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26770.1)"
     Site            708..733
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            741..761
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Site            788..804
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26770.1)"
     Region          861..1060
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(873,875..880,922,924..926,929,1002..1004,1008..1009,
                     1012..1013,1049)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(875,926)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(880,896,899..900,903,907,922..923,990,993,
                     1003..1006,1009,1049)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..1072
                     /gene="Adcy4"
                     /coded_by="NM_019285.2:144..3362"
                     /db_xref="GeneID:54223"
                     /db_xref="RGD:2034"
ORIGIN      
        1 marlfsprpp psedlfyety yslsqqypll illlvivlca ivalpavawa sgreltsdps
       61 flttvlcalg gfslllglas reqqlqrwtr plsgliwaal lalgygflft ggvvsawdqv
      121 sfflfiiftv yamlplgmrd aaaagvissl shllvlglyl gwrpesqrdl lpqlaanavl
      181 flcgnvvgay hkalmeralr atfrealssl hsrrrldtek khqehlllsi lpaylaremk
      241 aeimarlqag qssrpentnn fhslyvkrhq gvsvlyadiv gftrlasecs pkelvlmlne
      301 lfgkfdqiak ehecmrikil gdcyycvsgl plslpdhain cvrmgldmcr airklrvatg
      361 vdinmrvgvh sgsvlcgvig lqkwqydvws hdvtlanhme aggvpgrvhi tgatlallag
      421 ayaveradme hrdpylrelg eptylvidpw aeeedekgte rgllsslegh tmrpsllmtr
      481 yleswgaakp fahlshvdsp aststplpek afspqwsldr srtprglhde ldtgdakffq
      541 vieqlnsqkq wkqskdfnll tlyfrekeme kqyrlsalpa fkyyaactfl vflsnftiqm
      601 lvttrppala ttysitfllf llllfvcfse hltkcvqkgp kmlhwlpals vlvatrpglr
      661 valgtatill vftmavvsll flpvssdcpf lapnvssvaf ntswelpasl plisipysmh
      721 ccvlgflscs lflhmsfelk llllllwlva scslflhsha wlsdcliarl yqgslgsrpg
      781 vlkepklmga iyffiffftl lvlarqneyy crldflwkkk lrqereetet menltrllle
      841 nvlpahvapq figqnrrned lyhqsyecvc vlfasipdfk efysesninh egleclrlln
      901 eiiadfdell skpkfsgvek iktigstyma atglnatpgq dtqqdaersc shlgtmvefa
      961 valgsklgvi nkhsfnnfrl rvglnhgpvv agvigaqkpq ydiwgntvnv asrmestgvl
     1021 gkiqvteeta ralqslgytc ysrgvikvkg kgqlctyfln tdltrtgsps as
//
LOCUS       NP_001153125             256 aa            linear   ROD 27-APR-2025
DEFINITION  SCG6 (secretogranin VI) isoform SCG6 precursor [Rattus norvegicus].
ACCESSION   NP_001153125 XP_001076436
VERSION     NP_001153125.1
DBSOURCE    REFSEQ: accession NM_001159653.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Taneera,J., Dhaiban,S., Mohammed,A.K., Mukhopadhyay,D.,
            Aljaibeji,H., Sulaiman,N., Fadista,J. and Salehi,A.
  TITLE     GNAS gene is an important regulator of insulin secretory capacity
            in pancreatic beta-cells
  JOURNAL   Gene 715, 144028 (2019)
   PUBMED   31374326
  REMARK    GeneRIF: GNAS is a crucial gene for the beta-cell insulin secretory
            capacity.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Masyuk,T.V., Masyuk,A.I., Lorenzo Pisarello,M., Howard,B.N.,
            Huang,B.Q., Lee,P.Y., Fung,X., Sergienko,E., Ardecky,R.J.,
            Chung,T.D.Y., Pinkerton,A.B. and LaRusso,N.F.
  TITLE     TGR5 contributes to hepatic cystogenesis in rodents with polycystic
            liver diseases through cyclic adenosine monophosphate/Galphas
            signaling
  JOURNAL   Hepatology 66 (4), 1197-1218 (2017)
   PUBMED   28543567
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Xue,N., Wei,C., Zhang,L., Liu,H., Wang,X. and Wang,L.
  TITLE     The Characteristics of Hepatic Gsalpha-cAMP Axis in HSHF Diet-Fed
            Obese Insulin Resistance Rats and Genetic Diabetic Mice
  JOURNAL   Biol Pharm Bull 40 (6), 774-781 (2017)
   PUBMED   28260721
  REMARK    GeneRIF: Our data revealed a positive correlation between hepatic
            Gsalpha-cAMP signal axis and fasting blood glucose (FBG) in slight
            insulin resistance stage of HIgh Sugar High Fat-diet rats and
            diabetic db/db mice. The current finding thus suggested hepatic
            Gsalpha-cAMP signal axis plays a central role in regulating of FBG
            during the developing and development of T2DM.
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Erb,S.J., Schappi,J.M. and Rasenick,M.M.
  TITLE     Antidepressants Accumulate in Lipid Rafts Independent of Monoamine
            Transporters to Modulate Redistribution of the G Protein, Galphas
  JOURNAL   J Biol Chem 291 (38), 19725-19733 (2016)
   PUBMED   27432886
  REMARK    GeneRIF: Translocation of Galphas, which shows delayed onset after
            chronic antidepressant treatment of rats or of C6 glioma cells,
            tracks with the delayed onset of therapeutic action of
            antidepressants
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Sarma,T., Koutsouris,A., Yu,J.Z., Krbanjevic,A., Hope,T.J. and
            Rasenick,M.M.
  TITLE     Activation of microtubule dynamics increases neuronal growth via
            the nerve growth factor (NGF)- and Galphas-mediated signaling
            pathways
  JOURNAL   J Biol Chem 290 (16), 10045-10056 (2015)
   PUBMED   25691569
  REMARK    GeneRIF: Activated Galpha s translocates from the plasma membrane
            and, through interaction with tubulin/microtubules in the cytosol,
            is important for neurite formation, development, and outgrowth.
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Eaton,S.A., Hough,T., Fischer-Colbrie,R. and Peters,J.
  TITLE     Maternal inheritance of the Gnas cluster mutation Ex1A-T affects
            size, implicating NESP55 in growth
  JOURNAL   Mamm Genome 24 (7-8), 276-285 (2013)
   PUBMED   23839232
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Swaroop,A., Agarwal,N., Gruen,J.R., Bick,D. and Weissman,S.M.
  TITLE     Differential expression of novel Gs alpha signal transduction
            protein cDNA species
  JOURNAL   Nucleic Acids Res 19 (17), 4725-4729 (1991)
   PUBMED   1716359
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Weinstein,L.S., Gejman,P.V., Friedman,E., Kadowaki,T.,
            Collins,R.M., Gershon,E.S. and Spiegel,A.M.
  TITLE     Mutations of the Gs alpha-subunit gene in Albright hereditary
            osteodystrophy detected by denaturing gradient gel electrophoresis
  JOURNAL   Proc Natl Acad Sci U S A 87 (21), 8287-8290 (1990)
   PUBMED   2122458
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Golf: an olfactory neuron specific-G protein involved in odorant
            signal transduction
  JOURNAL   Science 244 (4906), 790-795 (1989)
   PUBMED   2499043
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Votan-Bonamour,B., Plauchu,H. and Guibaud,P.
  TITLE     [Ectopic crystalline lens linked to its cause (homocyst inuria) by
            a simple geneological enquiry]
  JOURNAL   J Genet Hum 24 Suppl, 103-106 (1976)
   PUBMED   799727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB770483.1, AF105254.1 and
            BC168156.1.
            
            On Apr 30, 2009 this sequence version replaced XP_001076436.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            In addition, one of the transcripts contains a second overlapping
            ORF, which encodes a structurally unrelated protein - Alex.
            Alternative splicing of downstream exons is also observed, which
            results in different forms of the stimulatory G-protein alpha
            subunit, a key element of the classical signal transduction pathway
            linking receptor-ligand interactions with the activation of
            adenylyl cyclase and a variety of cellular reponses. Multiple
            transcript variants have been found for this gene. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (4) is maternally expressed. It
            has alternate 5' exons, as compared to variant 3. Variants 4 and 5
            both encode neuroendocrine secretory protein 55 (NESP55), which
            localizes to large secretory vesicles of endocrine cells and
            neurons. The coding regions of variants 4 and 5 do not overlap the
            coding regions used by other transcripts; thus NESP55 has no
            similarity to isoforms of the G-protein alpha subunit.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 23839232
            NMD candidate  :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..256
                     /product="SCG6 (secretogranin VI) isoform SCG6 precursor"
                     /note="GNAS complex locus XLas-like; guanine
                     nucleotide-binding protein G-s, alpha subunit; guanine
                     nucleotide binding protein alpha s; adenylate
                     cyclase-stimulating G alpha protein; GNAS (guanine
                     nucleotide binding protein, alpha stimulating) complex
                     locus; SCG6 (secretogranin VI)"
                     /calculated_mol_wt=23835
     Region          1..256
                     /region_name="NESP55"
                     /note="Neuroendocrine-specific golgi protein P55 (NESP55);
                     pfam06390"
                     /db_xref="CDD:115071"
     sig_peptide     1..46
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=5358
     mat_peptide     47..256
                     /product="Neuroendocrine secretory protein 55.
                     /id=PRO_0000253973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=23835
     Region          61..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
     mat_peptide     170..173
                     /product="LHAL tetrapeptide. /evidence=ECO:0000255,
                     ECO:0000303|PubMed:10729789. /id=PRO_0000253974"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=453
     mat_peptide     249..256
                     /product="GPIPIRRH peptide. /evidence=ECO:0000255,
                     ECO:0000303|PubMed:10729789. /id=PRO_0000253975"
                     /note="propagated from UniProtKB/Swiss-Prot (Q792G6.1)"
                     /calculated_mol_wt=945
     CDS             1..256
                     /gene="Gnas"
                     /gene_synonym="ALEX; G-alpha-8; Gnas1; Gnpas; Nesp55;
                     SCG6"
                     /coded_by="NM_001159653.1:249..1019"
                     /note="isoform SCG6 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:24896"
                     /db_xref="RGD:2716"
ORIGIN      
        1 mdrrsrahqw rrarhnyndl cppigrraat allwlscsia llralassna raqqraaqrr
       61 sflnahhrsa aaaaaaqvlp essesesdhe heeaepelar pecleydqdd yetetdsete
      121 pesdiqsete fetepetepe tapttepete pedergprga tfnqsltqrl halklqsada
      181 sprraqpttq epesasegee pqrepldedp rdpeeseelr eanrqprrck trrparrrdq
      241 spespprkgp ipirrh
//
LOCUS       NP_001013893             376 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 183 [Rattus norvegicus].
ACCESSION   NP_001013893 XP_213887
VERSION     NP_001013893.1
DBSOURCE    REFSEQ: accession NM_001013871.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079375.1.
            
            On Apr 20, 2005 this sequence version replaced XP_213887.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079375.1, FQ210515.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..376
                     /product="transmembrane protein 183"
                     /note="clone MNCb-2755"
                     /calculated_mol_wt=42851
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FS7.1)"
     Region          81..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FS7.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FS7.1)"
     CDS             1..376
                     /gene="Tmem183a"
                     /gene_synonym="RGD1309892; Tmem183"
                     /coded_by="NM_001013871.1:37..1167"
                     /db_xref="GeneID:289034"
                     /db_xref="RGD:1309892"
ORIGIN      
        1 margpgqlsg prpdtvtmpk rgkrlkfrah dacsgrvtva dyansdpavv rsgrvkkava
       61 navqqevksl cgleasqvpa eealsgvgep sdildssdem daqeestqer svsrkkkskr
      121 hkedldgagg eeypmdiwll lasyirpedi vnfslickna wtvtctaafw trlyrrhytl
      181 daslplrlrp esmeklrclr acvirslyhm yepfaarisk npaipestps tlknskcllf
      241 wcrkivgnrq epmwefnfkf kkqsprlksk cmerlqppiq yqdvhtnpdq dccllqvttl
      301 nfifipivmg miftlftinv stdmrhhrvr lvfqdspvrg gqhlrseqgv qvvldpvhsv
      361 rlfdwwhpqy pfslra
//
LOCUS       NP_001012218             545 aa            linear   ROD 27-APR-2025
DEFINITION  tripartite motif-containing protein 55 [Rattus norvegicus].
ACCESSION   NP_001012218 XP_345193
VERSION     NP_001012218.1
DBSOURCE    REFSEQ: accession NM_001012218.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Tan,J., Shen,J., Zhu,H., Gong,Y., Zhu,H., Li,J., Lin,S., Wu,G. and
            Sun,T.
  TITLE     miR-378a-3p inhibits ischemia/reperfusion-induced apoptosis in H9C2
            cardiomyocytes by targeting TRIM55 via the DUSP1-JNK1/2 signaling
            pathway
  JOURNAL   Aging (Albany NY) 12 (10), 8939-8952 (2020)
   PUBMED   32463795
  REMARK    GeneRIF: miR-378a-3p inhibits ischemia/reperfusion-induced
            apoptosis in H9C2 cardiomyocytes by targeting TRIM55 via the
            DUSP1-JNK1/2 signaling pathway.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Gralinski,L.E., Ferris,M.T., Aylor,D.L., Whitmore,A.C., Green,R.,
            Frieman,M.B., Deming,D., Menachery,V.D., Miller,D.R., Buus,R.J.,
            Bell,T.A., Churchill,G.A., Threadgill,D.W., Katze,M.G.,
            McMillan,L., Valdar,W., Heise,M.T., Pardo-Manuel de Villena,F. and
            Baric,R.S.
  TITLE     Genome Wide Identification of SARS-CoV Susceptibility Loci Using
            the Collaborative Cross
  JOURNAL   PLoS Genet 11 (10), e1005504 (2015)
   PUBMED   26452100
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Lomonosova,Iu.N., Turtikova,O.V. and Shenkman,B.S.
  TITLE     [Translocation of MuRF isoforms to nuclei in postural muscle during
            gravitational unloading]
  JOURNAL   Ross Fiziol Zh Im I M Sechenova 101 (1), 64-73 (2015)
   PUBMED   25868327
  REMARK    GeneRIF: MuRF1 and MuRF2 translocate to the nuclei in the soleus
            muscle during gravitational unloading.
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Perera,S., Holt,M.R., Mankoo,B.S. and Gautel,M.
  TITLE     Developmental regulation of MURF ubiquitin ligases and autophagy
            proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly
            and turnover
  JOURNAL   Dev Biol 351 (1), 46-61 (2011)
   PUBMED   21185285
  REMARK    GeneRIF: Neonatal rat cardiomyocytes expressing MURF2+3 specific
            siRNA have reduced expression of both MURF2 and -3
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Lange,S., Xiang,F., Yakovenko,A., Vihola,A., Hackman,P.,
            Rostkova,E., Kristensen,J., Brandmeier,B., Franzen,G., Hedberg,B.,
            Gunnarsson,L.G., Hughes,S.M., Marchand,S., Sejersen,T., Richard,I.,
            Edstrom,L., Ehler,E., Udd,B. and Gautel,M.
  TITLE     The kinase domain of titin controls muscle gene expression and
            protein turnover
  JOURNAL   Science 308 (5728), 1599-1603 (2005)
   PUBMED   15802564
REFERENCE   7  (residues 1 to 545)
  AUTHORS   McElhinny,A.S., Perry,C.N., Witt,C.C., Labeit,S. and Gregorio,C.C.
  TITLE     Muscle-specific RING finger-2 (MURF-2) is important for
            microtubule, intermediate filament and sarcomeric M-line
            maintenance in striated muscle development
  JOURNAL   J Cell Sci 117 (Pt 15), 3175-3188 (2004)
   PUBMED   15199100
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Pizon,V., Iakovenko,A., Van Der Ven,P.F., Kelly,R., Fatu,C.,
            Furst,D.O., Karsenti,E. and Gautel,M.
  TITLE     Transient association of titin and myosin with microtubules in
            nascent myofibrils directed by the MURF2 RING-finger protein
  JOURNAL   J Cell Sci 115 (Pt 23), 4469-4482 (2002)
   PUBMED   12414993
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087100.1.
            
            On Feb 11, 2005 this sequence version replaced XP_345193.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..545
                     /product="tripartite motif-containing protein 55"
                     /EC_number="2.3.2.27"
                     /note="muRF2; MURF-2; muscle-specific RING finger protein
                     2; ring finger protein 29"
                     /calculated_mol_wt=59849
     Region          21..84
                     /region_name="RING-HC_MuRF2"
                     /note="RING finger, HC subclass, found in muscle-specific
                     RING finger protein 2 (MuRF-2) and similar proteins;
                     cd16760"
                     /db_xref="CDD:438417"
     Region          122..166
                     /region_name="Bbox2_MuRF2_C-II"
                     /note="B-box-type 2 zinc finger found in muscle-specific
                     RING finger protein 2 (MuRF-2) and similar proteins;
                     cd19832"
                     /db_xref="CDD:380890"
     Region          <158..>323
                     /region_name="EzrA"
                     /note="Septation ring formation regulator, EzrA;
                     pfam06160"
                     /db_xref="CDD:428797"
     Region          324..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN5.1)"
     Region          406..528
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN5.1)"
     CDS             1..545
                     /gene="Trim55"
                     /gene_synonym="Rnf29"
                     /coded_by="NM_001012218.1:129..1766"
                     /db_xref="GeneID:365751"
                     /db_xref="RGD:1306943"
ORIGIN      
        1 mstslnyksf skeqqtmdnl ekqlicpicl emftkpvvil pcqhnlcrkc asdifqasnp
       61 ylptrggttv asggrfrcps crhevvldrh gvyglqrnll veniidiykq estrpekkld
      121 qpmceeheee riniyclnce vptcslckvf gahkdcqvap lthvfqrqks elsdgiavlv
      181 gsndrvqgvi sqledtckti eeccrkqkqd lcekfdhlys ileerktemt qaitrtqeek
      241 lehvrtlirk ysdhlenvsk lvesgiqfmd epemavflqn aktllqkite askafqmeki
      301 eqgyeimnnf tvnlnreeki ireidfsree ededdegevd eegegedave veeaenvqva
      361 ssgeeetlek aaepselaae iqaasgplla sspdsvsslp paadvlvtqg evvptdsqqt
      421 tqsetsgpsa aetadplfyp swykgqsrkm isnpphtpgg eglsqigpsa aedssvqsae
      481 vaeaaaneqa avsgkessst aatsqigfea sspqgqaaal gsgggadsep arhvfsfswl
      541 nslne
//
LOCUS       NP_037115               1006 aa            linear   ROD 27-APR-2025
DEFINITION  unconventional myosin-Id [Rattus norvegicus].
ACCESSION   NP_037115 XP_346404
VERSION     NP_037115.2
DBSOURCE    REFSEQ: accession NM_012983.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1006)
  AUTHORS   Yamazaki,R., Ishibashi,T., Baba,H. and Yamaguchi,Y.
  TITLE     Unconventional myosin ID is expressed in myelinating
            oligodendrocytes
  JOURNAL   J Neurosci Res 92 (10), 1286-1294 (2014)
   PUBMED   24903835
  REMARK    GeneRIF: This study demonistrated that myosin ID is expressed in
            myelinating oligodendrocytes in rat nerve system.
REFERENCE   2  (residues 1 to 1006)
  AUTHORS   Benesh,A.E., Fleming,J.T., Chiang,C., Carter,B.D. and Tyska,M.J.
  TITLE     Expression and localization of myosin-1d in the developing nervous
            system
  JOURNAL   Brain Res 1440, 9-22 (2012)
   PUBMED   22284616
REFERENCE   3  (residues 1 to 1006)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   4  (residues 1 to 1006)
  AUTHORS   McConnell,R.E., Benesh,A.E., Mao,S., Tabb,D.L. and Tyska,M.J.
  TITLE     Proteomic analysis of the enterocyte brush border
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 300 (5), G914-G926 (2011)
   PUBMED   21330445
REFERENCE   5  (residues 1 to 1006)
  AUTHORS   Benesh,A.E., Nambiar,R., McConnell,R.E., Mao,S., Tabb,D.L. and
            Tyska,M.J.
  TITLE     Differential localization and dynamics of class I myosins in the
            enterocyte microvillus
  JOURNAL   Mol Biol Cell 21 (6), 970-978 (2010)
   PUBMED   20089841
REFERENCE   6  (residues 1 to 1006)
  AUTHORS   Batters,C., Arthur,C.P., Lin,A., Porter,J., Geeves,M.A.,
            Milligan,R.A., Molloy,J.E. and Coluccio,L.M.
  TITLE     Myo1c is designed for the adaptation response in the inner ear
  JOURNAL   EMBO J 23 (7), 1433-1440 (2004)
   PUBMED   15014434
  REMARK    GeneRIF: Results support a model in which Myo1c possesses a
            strain-sensing ADP-release mechanism, which allows it to adapt to
            mechanical load.
REFERENCE   7  (residues 1 to 1006)
  AUTHORS   Kohler,D., Ruff,C., Meyhofer,E. and Bahler,M.
  TITLE     Different degrees of lever arm rotation control myosin step size
  JOURNAL   J Cell Biol 161 (2), 237-241 (2003)
   PUBMED   12719468
REFERENCE   8  (residues 1 to 1006)
  AUTHORS   Dumont,R.A., Zhao,Y.D., Holt,J.R., Bahler,M. and Gillespie,P.G.
  TITLE     Myosin-I isozymes in neonatal rodent auditory and vestibular
            epithelia
  JOURNAL   J Assoc Res Otolaryngol 3 (4), 375-389 (2002)
   PUBMED   12486594
  REMARK    GeneRIF: At apical surfaces of supporting cells surrounding hair
            cells in auditory epithelia of postnatal rats. In vestibular
            epithelia, in a ring within apical pole of hair cell. Prominent
            only immediately after birth.
REFERENCE   9  (residues 1 to 1006)
  AUTHORS   Huber,L.A., Fialka,I., Paiha,K., Hunziker,W., Sacks,D.B.,
            Bahler,M., Way,M., Gagescu,R. and Gruenberg,J.
  TITLE     Both calmodulin and the unconventional myosin Myr4 regulate
            membrane trafficking along the recycling pathway of MDCK cells
  JOURNAL   Traffic 1 (6), 494-503 (2000)
   PUBMED   11208135
REFERENCE   10 (residues 1 to 1006)
  AUTHORS   Bahler,M., Kroschewski,R., Stoffler,H.E. and Behrmann,T.
  TITLE     Rat myr 4 defines a novel subclass of myosin I: identification,
            distribution, localization, and mapping of calmodulin-binding sites
            with differential calcium sensitivity
  JOURNAL   J Cell Biol 126 (2), 375-389 (1994)
   PUBMED   8034741
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087027.1.
            
            On Dec 26, 2004 this sequence version replaced NP_037115.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087027.1, X71997.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1006
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..1006
                     /product="unconventional myosin-Id"
                     /note="myosin1C; myosin-Id; myosin heavy chain myr 4;
                     myosin 1C; Unconventional myosin from rat 4 for myosin I
                     heavy chain; myosin IC"
                     /calculated_mol_wt=115964
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O94832; propagated from
                     UniProtKB/Swiss-Prot (Q63357.3)"
     Region          24..682
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(50..53,58,102..109,151..161,383..388)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(50..53,58)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            102..109
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            151..161
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94832; propagated from
                     UniProtKB/Swiss-Prot (Q63357.3)"
     Site            383..388
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(412..423,426..433,435)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5SYD0; propagated from
                     UniProtKB/Swiss-Prot (Q63357.3)"
     Region          572..594
                     /region_name="Actin-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63357.3)"
     Site            614..624
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(626..652,669..682)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          776..896
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000269|PubMed:8034741"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63357.3)"
     Region          803..996
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1006
                     /gene="Myo1d"
                     /gene_synonym="Myo1c; Myr2; Myr4"
                     /coded_by="NM_012983.2:156..3176"
                     /db_xref="GeneID:25485"
                     /db_xref="RGD:621321"
ORIGIN      
        1 maeqeslefg kadfvlmdtv smpefmanlr lrfekgriyt figevvvsvn pykvlniygr
       61 dtieqykgre lyerpphlfa iadaaykamk rrskdtcimi sgesgagkte askyimqyia
      121 aitnpsqrae iervknmllk sncvleafgn aktnrndnss rfgkymdinf dfkgdpiggh
      181 innylleksr vivqqpgers fhsfyqllqg gseqmlhslh lqkslssyny irvgaqlkss
      241 indaaefkvv adamkvigfk peeiqtvyki laailhlgnl kfivdgdtpl iengkvvsvi
      301 aellstkadm vekallyrtv atgrdiidkq hteqeasygr dafakaiyer lfcwivtrin
      361 diievknydt tvhgkntvig vldiygfeif dnnsfeqfci nycneklqql fiqlvlkqeq
      421 eeyqregipw khidyfnnqi ivdlveqqhk giiailddac mnvgkvtdgm flealnsklg
      481 khghfssrkt casdkilefd rdfrirhyag dvvysvigfi dknkdtlfqd fkrlmynssn
      541 pvlknmwpeg klsitevtkr pltaatlfkn smialvdnla skepyyvrci kpndkkspqi
      601 fddercrhqv eylgllenvr vrragfafrq tyekflhryk miseftwpnh dlpsdkeavk
      661 kliercgfqd dvaygktkif irtprtlftl eelraqmlvr vvlflqkvwr gtlarmrykr
      721 tkaaltiiry yrrykvksyi hevarrfhgv knmrdygkhv kwptppkvlr rfeealqsif
      781 nrwrasqlik tipasdlpqv rakvaameml kgqradlglq rawegnylas kpdtpqtsgt
      841 fvpvanelkr kdkymnvlfs chvrkvnrfs kvedraifvt drhlykmdpt kqykvmktip
      901 lynltglsvs ngkdqlvvfh tkdnkdlivc lfskqpthes rigelvgvlv nhfksekrhl
      961 qvnvtnpvqc slhgkkctvs vetrlnqpqp dftknrsgfi lsvpgn
//
LOCUS       NP_036792                463 aa            linear   ROD 27-APR-2025
DEFINITION  elongation factor 1-alpha 2 [Rattus norvegicus].
ACCESSION   NP_036792
VERSION     NP_036792.2
DBSOURCE    REFSEQ: accession NM_012660.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Becker,M., Kuhse,J. and Kirsch,J.
  TITLE     Effects of two elongation factor 1A isoforms on the formation of
            gephyrin clusters at inhibitory synapses in hippocampal neurons
  JOURNAL   Histochem Cell Biol 140 (6), 603-609 (2013)
   PUBMED   23839781
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Jeganathan,S., Morrow,A., Amiri,A. and Lee,J.M.
  TITLE     Eukaryotic elongation factor 1A2 cooperates with
            phosphatidylinositol-4 kinase III beta to stimulate production of
            filopodia through increased phosphatidylinositol-4,5 bisphosphate
            generation
  JOURNAL   Mol Cell Biol 28 (14), 4549-4561 (2008)
   PUBMED   18474610
  REMARK    GeneRIF: Study finds that eEF1A2 stimulates formation of filopodia
            by increasing the cellular abundance of cytosolic and plasma
            membrane-bound phosphatidylinositol-4,5 bisphosphate.
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Moon,I.S., Cho,S.J., Lee,H., Seog,D.H., Jung,Y.W., Jin,I. and
            Walikonis,R.
  TITLE     Upregulation by KCl treatment of eukaryotic translation elongation
            factor 1A (eEF1A) mRNA in the dendrites of cultured rat hippocampal
            neurons
  JOURNAL   Mol Cells 25 (4), 538-544 (2008)
   PUBMED   18443410
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Jeganathan,S. and Lee,J.M.
  TITLE     Binding of elongation factor eEF1A2 to phosphatidylinositol
            4-kinase beta stimulates lipid kinase activity and
            phosphatidylinositol 4-phosphate generation
  JOURNAL   J Biol Chem 282 (1), 372-380 (2007)
   PUBMED   17088255
  REMARK    GeneRIF: there is a physical and functional relationship between
            eEF1A2 and PI4KIIIbeta
REFERENCE   6  (residues 1 to 463)
  AUTHORS   McClatchy,D.B., Knudsen,C.R., Clark,B.F., Kahn,R.A., Hall,R.A. and
            Levey,A.I.
  TITLE     Novel interaction between the M4 muscarinic acetylcholine receptor
            and elongation factor 1A2
  JOURNAL   J Biol Chem 277 (32), 29268-29274 (2002)
   PUBMED   12048193
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Ruest,L.B., Marcotte,R. and Wang,E.
  TITLE     Peptide elongation factor eEF1A-2/S1 expression in cultured
            differentiated myotubes and its protective effect against
            caspase-3-mediated apoptosis
  JOURNAL   J Biol Chem 277 (7), 5418-5425 (2002)
   PUBMED   11724805
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Kristensen,P., Lund,A., Clark,B.F., Cavallius,J. and Merrick,W.C.
  TITLE     Purification and characterisation of a tissue specific elongation
            factor 1 alpha (EF-1 alpha 2) from rabbit muscle
  JOURNAL   Biochem Biophys Res Commun 245 (3), 810-814 (1998)
   PUBMED   9588196
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Poirier,J., Beffert,U., Dea,D., Alonso,R., O'Donnell,D. and
            Boksa,P.
  TITLE     Increased levels of statin, a marker of cell cycle arrest, in
            response to hippocampal neuronal injury
  JOURNAL   Brain Res Mol Brain Res 34 (1), 57-64 (1995)
   PUBMED   8750861
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Ann,D.K., Moutsatsos,I.K., Nakamura,T., Lin,H.H., Mao,P.L.,
            Lee,M.J., Chin,S., Liem,R.K. and Wang,E.
  TITLE     Isolation and characterization of the rat chromosomal gene for a
            polypeptide (pS1) antigenically related to statin
  JOURNAL   J Biol Chem 266 (16), 10429-10437 (1991)
   PUBMED   1709933
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC074016.1.
            
            On Jul 8, 2004 this sequence version replaced NP_036792.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC074016.1, M62751.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..463
                     /product="elongation factor 1-alpha 2"
                     /note="eEF1A-2; EF-1-alpha-2; elongation factor 1 A-2;
                     statin-S1; eukaryotic elongation factor 1 A-2; Statin-like
                     protein"
                     /calculated_mol_wt=50323
     Region          1..460
                     /region_name="PTZ00141"
                     /note="elongation factor 1- alpha; Provisional"
                     /db_xref="CDD:185474"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylglycine.
                     /evidence=ECO:0000250|UniProtKB:P68104; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Region          14..21
                     /region_name="G1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            14..21
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206670"
     Site            order(15,17,21..22,25,28..29,76..77,95..96,119..120,169,
                     173)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206670"
     Site            order(17,19..22,153..154,156,194..196)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206670"
     Site            order(21,64,67..68,70,72,74..76,78,89,91,93..95,97,100)
                     /site_type="other"
                     /note="EF1Balpha binding site [polypeptide binding]"
                     /db_xref="CDD:206670"
     Site            36
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q05639;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q05639; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:Q05639;
                     propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            55
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q71V39;
                     N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q05639; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            66..76
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206670"
     Region          70..74
                     /region_name="G2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            72
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206670"
     Site            79
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q05639; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Region          91..94
                     /region_name="G3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            91..94
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206670"
     Site            93..111
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206670"
     Region          153..156
                     /region_name="G4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            153..156
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206670"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71V39; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            165
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate, by EEF1AKMT3.
                     /evidence=ECO:0000250|UniProtKB:Q05639;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q05639; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:Q05639;
                     propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q05639; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Region          194..196
                     /region_name="G5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     Site            194..196
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206670"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q71V39; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="5-glutamyl glycerylphosphorylethanolamine.
                     /evidence=ECO:0000250|UniProtKB:Q71V39; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="5-glutamyl glycerylphosphorylethanolamine.
                     /evidence=ECO:0000250|UniProtKB:Q71V39; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Site            439
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q05639; propagated from
                     UniProtKB/Swiss-Prot (P62632.1)"
     Region          444..463
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62632.1)"
     CDS             1..463
                     /gene="Eef1a2"
                     /gene_synonym="EEF1AL; Ps10; RATPS10; STN; Stnl"
                     /coded_by="NM_012660.2:328..1719"
                     /db_xref="GeneID:24799"
                     /db_xref="RGD:3781"
ORIGIN      
        1 mgkekthini vvighvdsgk stttghliyk cggidkrtie kfekeaaemg kgsfkyawvl
       61 dklkaererg itidislwkf ettkyyitii dapghrdfik nmitgtsqad cavlivaagv
      121 gefeagiskn gqtrehalla ytlgvkqliv gvnkmdstep aysekrydei vkevsayikk
      181 igynpatvpf vpisgwhgdn mlepspnmpw fkgwkverke gnasgvslle aldtilpptr
      241 ptdkplrlpl qdvykiggig tvpvgrvetg ilrpgmvvtf apvnittevk svemhheals
      301 ealpgdnvgf nvknvsvkdi rrgnvcgdsk adppqeaaqf tsqviilnhp gqisagyspv
      361 idchtahiac kfaelkekid rrsgkkledn pkslksgdaa ivemvpgkpm cvesfsqypp
      421 lgrfavrdmr qtvavgvikn vekksggagk vtksaqkaqk agk
//
LOCUS       NP_569110                474 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 1B precursor
            [Rattus norvegicus].
ACCESSION   NP_569110
VERSION     NP_569110.1
DBSOURCE    REFSEQ: accession NM_130426.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Keck,M., Flamant,M., Mougenot,N., Favier,S., Atassi,F., Barbier,C.,
            Nadaud,S., Lompre,A.M., Hulot,J.S. and Pavoine,C.
  TITLE     Cardiac inflammatory CD11b/c cells exert a protective role in
            hypertrophied cardiomyocyte by promoting TNFR2- and Orai3-
            dependent signaling
  JOURNAL   Sci Rep 9 (1), 6047 (2019)
   PUBMED   30988334
  REMARK    GeneRIF: Cardiac inflammatory CD11b/c cells exert a protective role
            in hypertrophied cardiomyocyte by promoting TNFR2- and Orai3-
            dependent signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Shen,G.Y., Ren,H., Huang,J.J., Zhang,Z.D., Zhao,W.H., Yu,X.,
            Shang,Q., Qiu,T., Zhang,Y.Z., Tang,J.J., Liang,D., Yang,Z.D. and
            Jiang,X.B.
  TITLE     Plastrum Testudinis Extracts Promote BMSC Proliferation and
            Osteogenic Differentiation by Regulating Let-7f-5p and the
            TNFR2/PI3K/AKT Signaling Pathway
  JOURNAL   Cell Physiol Biochem 47 (6), 2307-2318 (2018)
   PUBMED   29975930
  REMARK    GeneRIF: results suggested that PTE may promote BMSC proliferation
            and osteogenic differentiation via a mechanism associated with the
            regulation of Let-7f-5p and the TNFR2/PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Gao,H., Danzi,M.C., Choi,C.S., Taherian,M., Dalby-Hansen,C.,
            Ellman,D.G., Madsen,P.M., Bixby,J.L., Lemmon,V.P., Lambertsen,K.L.
            and Brambilla,R.
  TITLE     Opposing Functions of Microglial and Macrophagic TNFR2 in the
            Pathogenesis of Experimental Autoimmune Encephalomyelitis
  JOURNAL   Cell Rep 18 (1), 198-212 (2017)
   PUBMED   28052249
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Wang,M., Wang,L., Huang,C., Wang,I.W. and Turrentine,M.W.
  TITLE     Regulation of myocardial stromal cell-derived factor 1alpha/CXCL12
            by tumor necrosis factor signaling
  JOURNAL   J Surg Res 207, 155-163 (2017)
   PUBMED   27979472
  REMARK    GeneRIF: TNF plays an inhibitory role in modulating myocardial
            SDF-1 production and blockade of TNF signaling by ablation of TNFR1
            and TNFR2 genes increased SDF-1 expression in the heart. These data
            expand on TNF signaling-initiated mechanisms in myocardium, which
            may lend a more complete understanding of SDF-1 and TNFR-derived
            actions in hopes of advancing ischemic heart injury treatments.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Madsen,P.M., Motti,D., Karmally,S., Szymkowski,D.E.,
            Lambertsen,K.L., Bethea,J.R. and Brambilla,R.
  TITLE     Oligodendroglial TNFR2 Mediates Membrane TNF-Dependent Repair in
            Experimental Autoimmune Encephalomyelitis by Promoting
            Oligodendrocyte Differentiation and Remyelination
  JOURNAL   J Neurosci 36 (18), 5128-5143 (2016)
   PUBMED   27147664
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Sippy,B.D., Hofman,F.M., Wallach,D. and Hinton,D.R.
  TITLE     Increased expression of tumor necrosis factor-alpha receptors in
            the brains of patients with AIDS
  JOURNAL   J Acquir Immune Defic Syndr Hum Retrovirol 10 (5), 511-521 (1995)
   PUBMED   8548330
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Erickson,S.L., de Sauvage,F.J., Kikly,K., Carver-Moore,K.,
            Pitts-Meek,S., Gillett,N., Sheehan,K.C., Schreiber,R.D.,
            Goeddel,D.V. and Moore,M.W.
  TITLE     Decreased sensitivity to tumour-necrosis factor but normal T-cell
            development in TNF receptor-2-deficient mice
  JOURNAL   Nature 372 (6506), 560-563 (1994)
   PUBMED   7990930
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Aderka,D., Wysenbeek,A., Engelmann,H., Cope,A.P., Brennan,F.,
            Molad,Y., Hornik,V., Levo,Y., Maini,R.N., Feldmann,M. et al.
  TITLE     Correlation between serum levels of soluble tumor necrosis factor
            receptor and disease activity in systemic lupus erythematosus
  JOURNAL   Arthritis Rheum 36 (8), 1111-1120 (1993)
   PUBMED   8393677
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Aderka,D., Englemann,H., Hornik,V., Skornick,Y., Levo,Y.,
            Wallach,D. and Kushtai,G.
  TITLE     Increased serum levels of soluble receptors for tumor necrosis
            factor in cancer patients
  JOURNAL   Cancer Res 51 (20), 5602-5607 (1991)
   PUBMED   1655258
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Goodwin,R.G., Anderson,D., Jerzy,R., Davis,T., Brannan,C.I.,
            Copeland,N.G., Jenkins,N.A. and Smith,C.A.
  TITLE     Molecular cloning and expression of the type 1 and type 2 murine
            receptors for tumor necrosis factor
  JOURNAL   Mol Cell Biol 11 (6), 3020-3026 (1991)
   PUBMED   1645445
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF498039.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF498039.2, AY344841.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..474
                     /product="tumor necrosis factor receptor superfamily
                     member 1B precursor"
                     /note="p75; TNF-R2; TNF-RII; TNFR-II; p80 TNF-alpha
                     receptor; tumor necrosis factor receptor 2; tumor necrosis
                     factor receptor type II; tumor necrosis factor receptor
                     superfamily, member 1b"
                     /calculated_mol_wt=47789
     sig_peptide     1..22
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
                     /calculated_mol_wt=2378
     mat_peptide     23..474
                     /product="Tumor necrosis factor receptor superfamily
                     member 1B. /id=PRO_0000034551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
                     /calculated_mol_wt=47789
     Site            30
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P20333; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          39..77
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          40..203
                     /region_name="TNFRSF1B"
                     /note="Tumor necrosis factor receptor superfamily member
                     1B (TNFRSF1B), also known as TNFR2; cd10577"
                     /db_xref="CDD:276903"
     Region          40..76
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276903"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          78..119
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          79..119
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276903"
     Site            order(81,83,85..87,89..91,93..97,99..100,117,129,131..132,
                     137..138)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276903"
     Site            order(100..101,104,122,173..175,199,201)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:276903"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          120..164
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          121..145
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276903"
     Region          163..203
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276903"
     Region          165..203
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Site            208
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P20333; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          220..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Site            224
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P20333; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Site            259..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          321..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20333; propagated from
                     UniProtKB/Swiss-Prot (Q80WY6.1)"
     Region          397..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80WY6.1)"
     CDS             1..474
                     /gene="Tnfrsf1b"
                     /gene_synonym="Tnfr2"
                     /coded_by="NM_130426.4:70..1494"
                     /db_xref="GeneID:156767"
                     /db_xref="RGD:621238"
ORIGIN      
        1 mapaalwval vvelqlwatg htvpakvvlt pykpepgnqc qisqeyydkk aqmccakcpp
       61 gqyakhfcnk tsdtvcadca agmftqvwnh lhtclscsss csddqvethn ctkkqnrvca
      121 cnadsycalk lhsgncrqcm klskcgpgfg varsrtsngn vicsacapgt fsdttsstdv
      181 crphricsil aipgnastda vcasesptps avprtiyvsq peptrsqpmd qepgpsqtph
      241 ipvslgstpi iepsitggis lpiglivglt tlgllmlgla ncfilvqrkk kpsclqretm
      301 vphlpddksq daigleqqhl lttapsssss slessasagd rrappgghpq arvtaeaqgs
      361 qeacagsrss dsshgshgth vnvtcivnvc sssdhssqcs sqasttvgdp danpsgspkd
      421 eqvpfsqeec psqsqwette tlqnhdkpfp lgvpdvgmkp nqpgwydqia vkvp
//
LOCUS       NP_445842                215 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-12 subunit alpha precursor [Rattus norvegicus].
ACCESSION   NP_445842
VERSION     NP_445842.1
DBSOURCE    REFSEQ: accession NM_053390.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   He,X.P., Chen,P., Yang,K., Liu,B., Zhang,Y., Wang,F., Guo,Z.,
            Liu,X.D., Lou,J.X. and Chen,H.R.
  TITLE     Overexpression of miR-21 is involved in acute monocytic
            leukemia-associated angiogenesis by targeting IL-12
  JOURNAL   Mol Med Rep 18 (4), 4122-4128 (2018)
   PUBMED   30106099
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Khalil,M., El-Badawy,O., Sharaf-Eldin,A., Sadek,A. and Sabry,A.
  TITLE     Serum levels of Interleukins 1-Alpha & 12 as Predictors of Disease
            Progression in Hepatitis C Diabetic Patients
  JOURNAL   Egypt J Immunol 25 (1), 181-190 (2018)
   PUBMED   30243010
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Elsayed,H.M., Nabiel,Y. and Sheta,T.
  TITLE     IL12 Gene Polymorphism in Association with Hepatocellular Carcinoma
            in HCV-infected Egyptian Patients
  JOURNAL   Immunol Invest 46 (2), 123-133 (2017)
   PUBMED   27819525
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Li,P., Lu,G., Cui,Y., Wu,Z., Chen,S., Li,J., Wen,X., Zhang,H.,
            Mu,S., Zhang,F. and Li,Y.
  TITLE     Association of IL12A Expression Quantitative Trait Loci (eQTL) With
            Primary Biliary Cirrhosis in a Chinese Han Population
  JOURNAL   Medicine (Baltimore) 95 (19), e3665 (2016)
   PUBMED   27175695
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Houshmandi,N., Najafipour,H., Joukar,S., Dabiri,S., Abbasloo,E.,
            Abdi,E. and Safi,Z.
  TITLE     The effect of interleukins 27 and 35 and their role on mediating
            the action of insulin Like Growth Factor -1 on the inflammation and
            blood flow of chronically inflamed rat knee joint
  JOURNAL   Cytokine 81, 117-126 (2016)
   PUBMED   26994309
  REMARK    GeneRIF: Data show that endogenous interleukins IL-27 and IL-35
            (Ebi3 and Il-12p35 subunits) had inflammatory roles and insulin
            like growth factor -1 (IGF-1) had no effect.
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Hayes,M.P., Wang,J. and Norcross,M.A.
  TITLE     Regulation of interleukin-12 expression in human monocytes:
            selective priming by interferon-gamma of
            lipopolysaccharide-inducible p35 and p40 genes
  JOURNAL   Blood 86 (2), 646-650 (1995)
   PUBMED   7605994
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Ploemacher,R.E., van Soest,P.L., Boudewijn,A. and Neben,S.
  TITLE     Interleukin-12 enhances interleukin-3 dependent multilineage
            hematopoietic colony formation stimulated by interleukin-11 or
            steel factor
  JOURNAL   Leukemia 7 (9), 1374-1380 (1993)
   PUBMED   7690439
REFERENCE   8  (residues 1 to 215)
  AUTHORS   D'Andrea,A., Rengaraju,M., Valiante,N.M., Chehimi,J., Kubin,M.,
            Aste,M., Chan,S.H., Kobayashi,M., Young,D., Nickbarg,E. et al.
  TITLE     Production of natural killer cell stimulatory factor (interleukin
            12) by peripheral blood mononuclear cells
  JOURNAL   J Exp Med 176 (5), 1387-1398 (1992)
   PUBMED   1357073
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Gubler,U., Chua,A.O., Schoenhaut,D.S., Dwyer,C.M., McComas,W.,
            Motyka,R., Nabavi,N., Wolitzky,A.G., Quinn,P.M., Familletti,P.C. et
            al.
  TITLE     Coexpression of two distinct genes is required to generate secreted
            bioactive cytotoxic lymphocyte maturation factor
  JOURNAL   Proc Natl Acad Sci U S A 88 (10), 4143-4147 (1991)
   PUBMED   1674604
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Stern,A.S., Podlaski,F.J., Hulmes,J.D., Pan,Y.C., Quinn,P.M.,
            Wolitzky,A.G., Familletti,P.C., Stremlo,D.L., Truitt,T.,
            Chizzonite,R. et al.
  TITLE     Purification to homogeneity and partial characterization of
            cytotoxic lymphocyte maturation factor from human B-lymphoblastoid
            cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (17), 6808-6812 (1990)
   PUBMED   2204066
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF177031.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF177031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="DA"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q32"
     Protein         1..215
                     /product="interleukin-12 subunit alpha precursor"
                     /note="interleukin-12 subunit alpha; IL-12A; CLMF p35;
                     IL-12 subunit p35; cytotoxic lymphocyte maturation factor
                     35 kDa subunit; interleukin 12 p35 subunit"
                     /calculated_mol_wt=21756
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2508
     Region          17..215
                     /region_name="IL12"
                     /note="Interleukin-12 alpha subunit; pfam03039"
                     /db_xref="CDD:460785"
     mat_peptide     23..215
                     /product="Interleukin-12 subunit alpha.
                     /id=PRO_0000015611"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R103.1)"
                     /calculated_mol_wt=21756
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R103.1)"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R103.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R103.1)"
     CDS             1..215
                     /gene="Il12a"
                     /coded_by="NM_053390.1:35..682"
                     /db_xref="GeneID:84405"
                     /db_xref="RGD:620562"
ORIGIN      
        1 mcqsryllfl atlvllnhlt sarvipvsgp akclnqsqnl lkttddmvrt areklkhysc
       61 tagdidhedi trdktstlea clplelhkne sclatketss iirgsclppq ktslmmtlcl
      121 gsiyedlkmy qsefqainaa lqshnhqqit ldrnmlmaid elmrslnhsg etlhqkapmg
      181 eadpyrvkmk lcillhafst rvmtinrvmn ylsss
//
LOCUS       NP_001017458             517 aa            linear   ROD 27-APR-2025
DEFINITION  T-complex protein 11-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001017458 XP_234997
VERSION     NP_001017458.1
DBSOURCE    REFSEQ: accession NM_001017458.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC092644.1.
            
            On Apr 29, 2005 this sequence version replaced XP_234997.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092644.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..517
                     /product="T-complex protein 11-like protein 2"
                     /note="t-complex 11, testis-specific-like 2"
                     /calculated_mol_wt=57849
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Z0.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q568Z0.1)"
     Region          77..496
                     /region_name="Tcp11"
                     /note="T-complex protein 11; pfam05794"
                     /db_xref="CDD:461743"
     CDS             1..517
                     /gene="Tcp11l2"
                     /gene_synonym="RGD1307494"
                     /coded_by="NM_001017458.1:65..1618"
                     /db_xref="GeneID:314683"
                     /db_xref="RGD:1307494"
ORIGIN      
        1 mpfngekqyv nedqqsdses srfsestasl sdygcsrqsf tsdsssksss pastspprgi
       61 mfddvmaaak nlsdmtlahe iavnenfqlr pnalpensla gqvkrvvhqa fwdvleadls
      121 aeppqyeyai klfeeireil lsfltpggnr lhsqicevld idlirqqaeh savdiqglan
      181 yvistmgkic apvrdedire lkattnivem lrqifrvldl mrmdmtnfvi rnirphiqhh
      241 lveyernkfq evleetpnal sqttewlkes idkelfsetd vapgaehsst pslspltvln
      301 ncylkllqwd yqknvlpetl mtdgprlqel teklnqlkmi acvslitnnm vgavteglpe
      361 lanrlkrisa vllegmskqt fnlkealnsi gvqtcaevnk alkergsptl naevqanlvg
      421 qftsleekdn pvcalmdkri qlymksllcl pstqksrppv pggldviqqe levlgcqyan
      481 ivnlnkqvyg pfyanifrkl lfrdeamgki daslptn
//
LOCUS       NP_775128                271 aa            linear   ROD 27-APR-2025
DEFINITION  aquaporin-11 [Rattus norvegicus].
ACCESSION   NP_775128
VERSION     NP_775128.1
DBSOURCE    REFSEQ: accession NM_173105.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Ichikawa,R., Takeda,T., Kakigi,A., Ito,H., Kobayashi,T. and
            Hyodo,M.
  TITLE     Expression of AQP-10, -11 and -12 in the rat stria vascularis
  JOURNAL   Acta Otolaryngol 144 (2), 96-99 (2024)
   PUBMED   38511591
  REMARK    GeneRIF: Expression of AQP-10, -11 and -12 in the rat stria
            vascularis.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bestetti,S., Galli,M., Sorrentino,I., Pinton,P., Rimessi,A.,
            Sitia,R. and Medrano-Fernandez,I.
  TITLE     Human aquaporin-11 guarantees efficient transport of H2O2 across
            the endoplasmic reticulum membrane
  JOURNAL   Redox Biol 28, 101326 (2020)
   PUBMED   31546170
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Hoshino,Y., Sonoda,H., Nishimura,R., Mori,K., Ishibashi,K. and
            Ikeda,M.
  TITLE     Involvement of the NADPH oxidase 2 pathway in renal oxidative
            stress in Aqp11-/- mice
  JOURNAL   Biochem Biophys Rep 17, 169-176 (2019)
   PUBMED   30656220
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Xi,T., Jin,F., Zhu,Y., Wang,J., Tang,L., Wang,Y., Liebeskind,D.S.,
            Scalzo,F. and He,Z.
  TITLE     miR-27a-3p protects against blood-brain barrier disruption and
            brain injury after intracerebral hemorrhage by targeting
            endothelial aquaporin-11
  JOURNAL   J Biol Chem 293 (52), 20041-20050 (2018)
   PUBMED   30337368
  REMARK    GeneRIF: application of exogenous miR-27a-3p may protect against
            post-ICH complications by targeting AQP11 in the capillary
            endothelial cells of the brain.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Lee,P.J., Park,H.J., Cho,N. and Kim,H.P.
  TITLE     Aquaporin 11-Dependent Inhibition of Proliferation by Deuterium
            Oxide in Activated Hepatic Stellate Cells
  JOURNAL   Molecules 23 (12), 3209 (2018)
   PUBMED   30563120
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Tchekneva,E.E., Khuchua,Z., Davis,L.S., Kadkina,V., Dunn,S.R.,
            Bachman,S., Ishibashi,K., Rinchik,E.M., Harris,R.C., Dikov,M.M. and
            Breyer,M.D.
  TITLE     Single amino acid substitution in aquaporin 11 causes renal failure
  JOURNAL   J Am Soc Nephrol 19 (10), 1955-1964 (2008)
   PUBMED   18701606
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Okada,S., Misaka,T., Tanaka,Y., Matsumoto,I., Ishibashi,K.,
            Sasaki,S. and Abe,K.
  TITLE     Aquaporin-11 knockout mice and polycystic kidney disease animals
            share a common mechanism of cyst formation
  JOURNAL   FASEB J 22 (10), 3672-3684 (2008)
   PUBMED   18606867
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Yakata,K., Hiroaki,Y., Ishibashi,K., Sohara,E., Sasaki,S.,
            Mitsuoka,K. and Fujiyoshi,Y.
  TITLE     Aquaporin-11 containing a divergent NPA motif has normal water
            channel activity
  JOURNAL   Biochim Biophys Acta 1768 (3), 688-693 (2007)
   PUBMED   17178102
  REMARK    Erratum:[Biochim Biophys Acta. 2008 Jun;1778(6):1525]
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Gorelick,D.A., Praetorius,J., Tsunenari,T., Nielsen,S. and Agre,P.
  TITLE     Aquaporin-11: a channel protein lacking apparent transport function
            expressed in brain
  JOURNAL   BMC Biochem 7, 14 (2006)
   PUBMED   16650285
  REMARK    GeneRIF: AQP11 has a unique distribution in brain:  Purkinje cell
            dendrites, CA1 & CA2 neurons, & cerebral cortical neurons. It is
            functionally distinct from other proteins of the aquaporin
            superfamily and could represent a new aquaporin subfamily.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Morishita,Y., Matsuzaki,T., Hara-chikuma,M., Andoo,A., Shimono,M.,
            Matsuki,A., Kobayashi,K., Ikeda,M., Yamamoto,T., Verkman,A.,
            Kusano,E., Ookawara,S., Takata,K., Sasaki,S. and Ishibashi,K.
  TITLE     Disruption of aquaporin-11 produces polycystic kidneys following
            vacuolization of the proximal tubule
  JOURNAL   Mol Cell Biol 25 (17), 7770-7779 (2005)
   PUBMED   16107722
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB023644.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023644.1, BC078694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132266, SAMD00132294
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..271
                     /product="aquaporin-11"
                     /note="AQP-11"
                     /calculated_mol_wt=30237
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Region          42..259
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Region          99..101
                     /region_name="NPC. /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Region          216..218
                     /region_name="NPA. /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     Site            235..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHM1.2)"
     CDS             1..271
                     /gene="Aqp11"
                     /coded_by="NM_173105.1:229..1044"
                     /db_xref="GeneID:286758"
                     /db_xref="RGD:628763"
ORIGIN      
        1 msallglppe vqdtcislgl mllvvlfmgl arviarqqlh rpmvhafvle flatfqlcyc
       61 thelqllseq dsghptwtlt liyffslvhg ltlvgtasnp cgvmmqmilg gmspemgavr
      121 lmaqlvsalc srycisalws lsltkyhfdk rilacrnpin tdiskaiiie aicsfifhsa
      181 llhfqevrtk lrihvlaali tflayaggsl tgalfnpala lslhfpcfde sfykffvvyw
      241 vapslgvllm ilmfsfflpw lhnnqlsnkk e
//
LOCUS       NP_001006999             468 aa            linear   ROD 27-APR-2025
DEFINITION  aldehyde dehydrogenase family 3 member B1 [Rattus norvegicus].
ACCESSION   NP_001006999 XP_239017
VERSION     NP_001006999.1
DBSOURCE    REFSEQ: accession NM_001006998.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Kitamura,T., Takagi,S., Naganuma,T. and Kihara,A.
  TITLE     Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets
            via two C-terminal tryptophan residues and lipid modification
  JOURNAL   Biochem J 465 (1), 79-87 (2015)
   PUBMED   25286108
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Marchitti,S.A., Brocker,C., Orlicky,D.J. and Vasiliou,V.
  TITLE     Molecular characterization, expression analysis, and role of
            ALDH3B1 in the cellular protection against oxidative stress
  JOURNAL   Free Radic Biol Med 49 (9), 1432-1443 (2010)
   PUBMED   20699116
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Hsu,L.C., Chang,W.C. and Yoshida,A.
  TITLE     Cloning of a cDNA encoding human ALDH7, a new member of the
            aldehyde dehydrogenase family
  JOURNAL   Gene 151 (1-2), 285-289 (1994)
   PUBMED   7828891
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083850.1.
            
            On Nov 22, 2004 this sequence version replaced XP_239017.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083850.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..468
                     /product="aldehyde dehydrogenase family 3 member B1"
                     /EC_number="1.2.1.5"
                     /EC_number="1.2.1.28"
                     /EC_number="1.2.1.7"
                     /EC_number="1.2.1.48"
                     /note="aldehyde dehydrogenase 7; long-chain fatty aldehyde
                     dehydrogenase; medium-chain fatty aldehyde dehydrogenase"
                     /calculated_mol_wt=52016
     mat_peptide     1..465
                     /product="Aldehyde dehydrogenase family 3 member B1.
                     /id=PRO_0000056483"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI42.1)"
                     /calculated_mol_wt=51820
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P43353; propagated from
                     UniProtKB/Swiss-Prot (Q5XI42.1)"
     Region          5..447
                     /region_name="ALDH_F3AB"
                     /note="Aldehyde dehydrogenase family 3 members A1, A2, and
                     B1 and related proteins; cd07132"
                     /db_xref="CDD:143450"
     Site            order(57,87..88,92,99,103,105,180,182,190,194,197,204,224,
                     227,230..231,234,271,281,359..360,364,369,375,378,
                     381..390,396,401,404..405,407,410,424,426..427,429..433,
                     437,439..440,442..446)
                     /site_type="other"
                     /note="homodimeric interface [polypeptide binding]"
                     /db_xref="CDD:143450"
     Site            order(113..115,141,170,188,287,289..290,293,334,336)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143450"
     Site            order(115,210,241,244)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143450"
     Site            465
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q5XI42.1)"
     CDS             1..468
                     /gene="Aldh3b1"
                     /coded_by="NM_001006998.1:37..1443"
                     /db_xref="GeneID:309147"
                     /db_xref="RGD:1359546"
ORIGIN      
        1 mdsfedklqq lreafnagrt rsaefraaql qglshflrdn kqqlqealaq dlhksafese
       61 vseiaisqae vdlalrnlrs wmkdekvskn latqldsafi rkepfglvli ivpwnyplnl
      121 tlvplvgaia agncvvlkps eiskatekil aevlpryldq scfavvlggp qetgqllehr
      181 fdyifftgnt yvgkivmaaa akhltpitle lggknpcyvd dncdpqtvan rvawfryfna
      241 gqtcvapdyv lcsqemqerl vpalqnaitr fygdnpqtsp nlgriinqkh ferlqgllgc
      301 grvaiggqsd egeryiaptv lvdvqetepv mqeeifgpil plvtvtnlde aiefinrrek
      361 plalyafskr sqvikqvlar tssggfcgnd gfmhmtlssl pfggvgtsgm gryhgkfsfd
      421 tfsnqracll rspgmekind lryppytsrn lrvllvamek rccsctll
//
LOCUS       NP_112376                 95 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A10 [Rattus norvegicus].
ACCESSION   NP_112376
VERSION     NP_112376.1
DBSOURCE    REFSEQ: accession NM_031114.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Waltz,T.B., Chao,D., Prodoehl,E.K., Enders,J.D., Ehlers,V.L.,
            Dharanikota,B.S., Dahms,N.M., Isaeva,E., Hogan,Q.H., Pan,B. and
            Stucky,C.L.
  TITLE     Fabry disease Schwann cells release p11 to induce sensory neuron
            hyperactivity
  JOURNAL   JCI Insight 9 (8), e172869 (2024)
   PUBMED   38646936
  REMARK    GeneRIF: Fabry disease Schwann cells release p11 to induce sensory
            neuron hyperactivity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Guo,Y., Li,R. and Dang,X.
  TITLE     S100A10 regulates tumor necrosis factor alpha-induced apoptosis in
            chondrocytes via the reactive oxygen species/nuclear factor-kappa B
            pathway
  JOURNAL   Biotechnol Appl Biochem 69 (6), 2284-2295 (2022)
   PUBMED   34787893
  REMARK    GeneRIF: S100A10 regulates tumor necrosis factor alpha-induced
            apoptosis in chondrocytes via the reactive oxygen species/nuclear
            factor-kappa B pathway.
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Matsuoka,H., Pokorski,M., Harada,K., Yoshimura,R. and Inoue,M.
  TITLE     Expression of p11 and Heteromeric TASK Channels in Rat Carotid Body
            Glomus Cells and Nerve Growth Factor-differentiated PC12 Cells
  JOURNAL   J Histochem Cytochem 68 (10), 679-690 (2020)
   PUBMED   32886017
  REMARK    GeneRIF: Expression of p11 and Heteromeric TASK Channels in Rat
            Carotid Body Glomus Cells and Nerve Growth Factor-differentiated
            PC12 Cells.
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Theilmann,W., Kleimann,A., Rhein,M., Bleich,S., Frieling,H.,
            Loscher,W. and Brandt,C.
  TITLE     Behavioral differences of male Wistar rats from different vendors
            in vulnerability and resilience to chronic mild stress are
            reflected in epigenetic regulation and expression of p11
  JOURNAL   Brain Res 1642, 505-515 (2016)
   PUBMED   27103570
  REMARK    GeneRIF: Results suggest that there are breeder-dependent
            differences in vulnerability to stress in the chronic mild stress
            (CMS) model of depression, which might bear on the validity of the
            model and contribute to contradictory findings and difficulties of
            replication between laboratories. P11 mRNA expression seems to be
            differently regulated depending on the quality of the stress
            response evoked by CMS exposure.
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Benaud,C., Gentil,B.J., Assard,N., Court,M., Garin,J., Delphin,C.
            and Baudier,J.
  TITLE     AHNAK interaction with the annexin 2/S100A10 complex regulates cell
            membrane cytoarchitecture
  JOURNAL   J Cell Biol 164 (1), 133-144 (2004)
   PUBMED   14699089
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Malik-Hall,M., Poon,W.Y., Baker,M.D., Wood,J.N. and Okuse,K.
  TITLE     Sensory neuron proteins interact with the intracellular domains of
            sodium channel NaV1.8
  JOURNAL   Brain Res Mol Brain Res 110 (2), 298-304 (2003)
   PUBMED   12591166
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Girard,C., Tinel,N., Terrenoire,C., Romey,G., Lazdunski,M. and
            Borsotto,M.
  TITLE     p11, an annexin II subunit, an auxiliary protein associated with
            the background K+ channel, TASK-1
  JOURNAL   EMBO J 21 (17), 4439-4448 (2002)
   PUBMED   12198146
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Okuse,K., Malik-Hall,M., Baker,M.D., Poon,W.Y., Kong,H., Chao,M.V.
            and Wood,J.N.
  TITLE     Annexin II light chain regulates sensory neuron-specific sodium
            channel expression
  JOURNAL   Nature 417 (6889), 653-656 (2002)
   PUBMED   12050667
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Masiakowski,P. and Shooter,E.M.
  TITLE     Nerve growth factor induces the genes for two proteins related to a
            family of calcium-binding proteins in PC12 cells
  JOURNAL   Proc Natl Acad Sci U S A 85 (4), 1277-1281 (1988)
   PUBMED   3422491
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J03627.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J03627.1, BC091565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..95
                     /product="protein S100-A10"
                     /note="calpactin I light chain; annexin II ligand; p10
                     protein; calpactin-1 light chain; cellular ligand of
                     annexin II; nerve growth factor-induced protein 42C; S-100
                     related protein, clone 42C"
                     /calculated_mol_wt=10944
     Region          3..93
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Site            order(3..20,23..25,34..35,37..39,67..70,72..73,75..78,
                     80..87)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(20,22,25,30..31,60,62,64,66,68,71)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60903; propagated from
                     UniProtKB/Swiss-Prot (P05943.2)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60903; propagated from
                     UniProtKB/Swiss-Prot (P05943.2)"
     Site            54
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60903; propagated from
                     UniProtKB/Swiss-Prot (P05943.2)"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60903; propagated from
                     UniProtKB/Swiss-Prot (P05943.2)"
     Region          60..71
                     /region_name="Ancestral calcium site"
                     /note="propagated from UniProtKB/Swiss-Prot (P05943.2)"
     CDS             1..95
                     /gene="S100a10"
                     /gene_synonym="p11"
                     /coded_by="NM_031114.1:46..333"
                     /db_xref="GeneID:81778"
                     /db_xref="RGD:628655"
ORIGIN      
        1 mpsqmehame tmmltfhrfa geknyltked lrvlmerefp gflenqkdpl avdkimkdld
       61 qcrdgkvgfq sflslvagli iacndyfvvh mkqkk
//
LOCUS       NP_001008286             868 aa            linear   ROD 27-APR-2025
DEFINITION  spindle and centriole-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_001008286 XP_213622
VERSION     NP_001008286.1
DBSOURCE    REFSEQ: accession NM_001008285.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Archinti,M., Lacasa,C., Teixido-Travesa,N. and Luders,J.
  TITLE     SPICE--a previously uncharacterized protein required for centriole
            duplication and mitotic chromosome congression
  JOURNAL   J Cell Sci 123 (Pt 18), 3039-3046 (2010)
   PUBMED   20736305
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085954.1.
            
            On Dec 16, 2004 this sequence version replaced XP_213622.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085954.1, FQ210155.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..868
                     /product="spindle and centriole-associated protein 1"
                     /note="coiled-coil domain-containing protein 52;
                     coiled-coil domain containing 52"
                     /calculated_mol_wt=96192
     Region          35..434
                     /region_name="SPICE"
                     /note="Centriole duplication and mitotic chromosome
                     congression; pfam15678"
                     /db_xref="CDD:464796"
     Region          129..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          172..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          229..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N0Z3; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C804; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          291..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          630..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N0Z3; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          702..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N0Z3; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Region          805..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKG1.1)"
     Site            831
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C804; propagated from
                     UniProtKB/Swiss-Prot (Q5RKG1.1)"
     CDS             1..868
                     /gene="Spice1"
                     /gene_synonym="Ccdc52; RGD1310729"
                     /coded_by="NM_001008285.1:24..2630"
                     /db_xref="GeneID:288111"
                     /db_xref="RGD:1310729"
ORIGIN      
        1 mslirvnrfg prggarktlk vkkkaavrqe wdntvndltv hratpedlvr rhemhksknr
       61 alvhwelqek alkrkwkkqk petssiekrk lsimkeilsd qyqtqdvlek sdhlltaakg
      121 lfvdvprkrt gfpnvtmapg ssrspaginq dpgtqsilne siiepqalne vddggaesta
      181 hsqsedsese lpnslsphsn rnterflhql keenselinq lwtdiqqkia aqsqrtppgs
      241 psselsaedq kgalnatdav kriqaglqpe esaepvdssy vgqvlntrkp kpllskvkrk
      301 qdmralskqk knmlssstts adlassnnss ldvlkhmihe vehemeeyer wtgrevkglq
      361 ggqgltgftl slvsslcrlv rylkesetql rkevetrqql eqmlgdhrel idaltaeill
      421 lreengavqa rlqqymvttd eqlislthai kscpvinnsr qesqaperaa mgrrlvdnvg
      481 apvvnsnvsm plmlkgeemv dfpqeelpvk lsqgpppten lnlasnfpth ifepavmltp
      541 prqksnsefs plqdvlrrtv qtrpapripp tveviekeqt wekknlpidp diqnsseesr
      601 lftqrwrvsh mgddlenksq pqfvslsqpp qfvslsqppc ssppstqqsr npvfseeptv
      661 lgdgqqlgta dalmhrkdim ariaeltlqn samkahlnni tssggehgdg lrepsrqgna
      721 sevpanfpav qslmpssmee riaelnrqsm earskllqli eqqklvgltl ssspvspves
      781 plrawteegk rtievsvpgv easesskcnt vspvsgvssr rssgaisnsc splnatsgsg
      841 kftpvnprtk qtekqseegw falsahlp
//
LOCUS       NP_001103609             997 aa            linear   ROD 27-APR-2025
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase 2 isoform a
            [Rattus norvegicus].
ACCESSION   NP_001103609
VERSION     NP_001103609.1
DBSOURCE    REFSEQ: accession NM_001110139.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Chen,W., Li,M., Lei,X., Cheng,Y., Wu,X., Sun,X., Wu,Y., Li,Z.,
            Luo,G. and Wei,M.
  TITLE     Remote ischemic postconditioning alleviates cerebral ischemic
            injury through SERCA2/endoplasmic reticulum stress-mediated
            apoptosis
  JOURNAL   Microsc Res Tech 87 (3), 424-433 (2024)
   PUBMED   37897375
  REMARK    GeneRIF: Remote ischemic postconditioning alleviates cerebral
            ischemic injury through SERCA2/endoplasmic reticulum
            stress-mediated apoptosis.
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Gomez-Viquez,N.L., Balderas-Villalobos,J., Bello-Sanchez,M.D.,
            Mayorga-Luna,M., Mailloux-Salinas,P., Garcia-Castaneda,M.,
            Rios-Perez,E.B., Martinez-Avila,M.A., Camacho-Castillo,L.D.C.,
            Bravo,G., Avila,G., Altamirano,J. and Carvajal,K.
  TITLE     Oxidative stress in early metabolic syndrome impairs cardiac RyR2
            and SERCA2a activity and modifies the interplay of these proteins
            during Ca2+ waves
  JOURNAL   Arch Physiol Biochem 129 (5), 1058-1070 (2023)
   PUBMED   33689540
  REMARK    GeneRIF: Oxidative stress in early metabolic syndrome impairs
            cardiac RyR2 and SERCA2a activity and modifies the interplay of
            these proteins during Ca[2+] waves.
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Hu,T. and Liu,L.
  TITLE     Effects of MiR-214-3p Regulation of SERCA2a Expression on
            Contractility of Cardiomyocytes in Heart Failure Model
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 68 (4), 208-216 (2022)
   PUBMED   35988281
  REMARK    GeneRIF: Effects of MiR-214-3p Regulation of SERCA2a Expression on
            Contractility of Cardiomyocytes in Heart Failure Model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 997)
  AUTHORS   Chen,J., Liu,Y., Pan,D., Xu,T., Luo,Y., Wu,W., Wu,P., Zhu,H. and
            Li,D.
  TITLE     Estrogen inhibits endoplasmic reticulum stress and ameliorates
            myocardial ischemia/reperfusion injury in rats by upregulating
            SERCA2a
  JOURNAL   Cell Commun Signal 20 (1), 38 (2022)
   PUBMED   35331264
  REMARK    GeneRIF: Estrogen inhibits endoplasmic reticulum stress and
            ameliorates myocardial ischemia/reperfusion injury in rats by
            upregulating SERCA2a.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 997)
  AUTHORS   Celestino-Montes,A., Perez-Trevino,P., Sandoval-Herrera,M.D.,
            Gomez-Viquez,N.L. and Altamirano,J.
  TITLE     Relative role of T-tubules disruption and decreased SERCA2 on
            contractile dynamics of isolated rat ventricular myocytes
  JOURNAL   Life Sci 264, 118700 (2021)
   PUBMED   33130073
  REMARK    GeneRIF: Relative role of T-tubules disruption and decreased SERCA2
            on contractile dynamics of isolated rat ventricular myocytes.
REFERENCE   6  (residues 1 to 997)
  AUTHORS   Harrer,J.M., Haghighi,K., Kim,H.W., Ferguson,D.G. and Kranias,E.G.
  TITLE     Coordinate regulation of SR Ca(2+)-ATPase and phospholamban
            expression in developing murine heart
  JOURNAL   Am J Physiol 272 (1 Pt 2), H57-H66 (1997)
   PUBMED   9038922
REFERENCE   7  (residues 1 to 997)
  AUTHORS   Wu,K.D. and Lytton,J.
  TITLE     Molecular cloning and quantification of sarcoplasmic reticulum
            Ca(2+)-ATPase isoforms in rat muscles
  JOURNAL   Am J Physiol 264 (2 Pt 1), C333-C341 (1993)
   PUBMED   8447366
  REMARK    Erratum:[Am J Physiol 1994 Jul;267(1 Pt 1):section C followi]
REFERENCE   8  (residues 1 to 997)
  AUTHORS   Lompre,A.M., de la Bastie,D., Boheler,K.R. and Schwartz,K.
  TITLE     Characterization and expression of the rat heart sarcoplasmic
            reticulum Ca2+-ATPase mRNA
  JOURNAL   FEBS Lett 249 (1), 35-41 (1989)
   PUBMED   2542094
REFERENCE   9  (residues 1 to 997)
  AUTHORS   Komuro,I., Kurabayashi,M., Shibazaki,Y., Takaku,F. and Yazaki,Y.
  TITLE     Molecular cloning and characterization of a Ca2+ + Mg2+-dependent
            adenosine triphosphatase from rat cardiac sarcoplasmic reticulum.
            Regulation of its expression by pressure overload and developmental
            stage
  JOURNAL   J Clin Invest 83 (4), 1102-1108 (1989)
   PUBMED   2522936
REFERENCE   10 (residues 1 to 997)
  AUTHORS   Gunteski-Hamblin,A.M., Greeb,J. and Shull,G.E.
  TITLE     A novel Ca2+ pump expressed in brain, kidney, and stomach is
            encoded by an alternative transcript of the slow-twitch muscle
            sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs
            encoding Ca2+ and other cation-transporting ATPases using an
            oligonucleotide probe derived from the ATP-binding site
  JOURNAL   J Biol Chem 263 (29), 15032-15040 (1988)
   PUBMED   2844797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1, J04022.1, CK356454.1, J04024.1, EV765256.1,
            J04023.1 and CK356436.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding region compared to variant 3. The resulting isoform (a),
            also known as SERCA2A, has a shorter and distinct C-terminus
            compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J04023.1, X15635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..997
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase 2 isoform a"
                     /EC_number="7.2.2.10"
                     /note="ATPase, Ca++ transporting, slow twitch 2;
                     sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
                     calcium pump 2; SR Ca(2+)-ATPase 2; endoplasmic reticulum
                     class 1/2 Ca(2+) ATPase; sarco(endo)plasmic reticulum
                     Ca(2+)-dependent ATPase 2; ATPase, Ca++ transporting,
                     cardiac muscle, slow twitch 2"
                     /calculated_mol_wt=109551
     Region          5..988
                     /region_name="P-type_ATPase_SERCA"
                     /note="sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA),
                     similar to mammalian ATP2A1-3/SERCA1-3; cd02083"
                     /db_xref="CDD:319778"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            254..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            296..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            order(309,795,799)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Site            order(351..353,442,487,489,492,494,514..516,559,561,
                     624..626,677,683,702,705)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:319778"
     Site            351..357
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319778"
     Site            351
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319778"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64578; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55143; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Region          575..594
                     /region_name="Interaction with HAX1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16615; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            757..776
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            order(767,770,798..799,907)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Region          787..807
                     /region_name="Interaction with PLN.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            787..807
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            828..850
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            897..916
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            930..948
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Region          931..942
                     /region_name="Interaction with PLN.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            964..984
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     CDS             1..997
                     /gene="Atp2a2"
                     /gene_synonym="Serca2; SercaII"
                     /coded_by="NM_001110139.2:507..3500"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:29693"
                     /db_xref="RGD:2174"
ORIGIN      
        1 menahtktve evlghfgvne stglsleqvk klkerwgsne lpaeegktll elvieqfedl
       61 lvrilllaac isfvlawfee geetitafve pfvillilva naivgvwqer naenaiealk
      121 eyepemgkvy rqdrksvqri kakdivpgdi veiavgdkvp adirltsiks ttlrvdqsil
      181 tgesvsvikh tdpvpdprav nqdkknmlfs gtniaagkam gvvvatgvnt eigkirdemv
      241 ateqertplq qkldefgeql skvislicia vwiinighfn dpvhggswir gaiyyfkiav
      301 alavaaipeg lpavittcla lgtrrmakkn aivrslpsve tlgctsvics dktgtlttnq
      361 msvcrmfild kvegdtcsln eftitgstya pigevqkddk pvkchqydgl velaticalc
      421 ndsaldynea kgvyekvgea tetaltclve kmnvfdtelk glskierana cnsvikqlmk
      481 keftlefsrd rksmsvyctp nkpsrtsmsk mfvkgapegv idrcthirvg stkvpmtpgv
      541 kqkimsvire wgsgsdtlrc lalathdnpl rreemhleds anfikyetnl tfvgcvgmld
      601 pprievassv klcrqagirv imitgdnkgt avaicrrigi fgqdedvtsk aftgrefdel
      661 spsaqrdacl narcfarvep shkskivefl qsfdeitamt gdgvndapal kkseigiamg
      721 sgtavaktas emvladdnfs tivaaveegr aiynnmkqfi rylissnvge vvcifltaal
      781 gfpealipvq llwvnlvtdg lpatalgfnp pdldimnkpp rnpkeplisg wlffrylaig
      841 cyvgaatvga aawwfiaadg gprvsfyqls hflqckednp dfegvdcaif espypmtmal
      901 svlvtiemcn alnslsenqs llrmppweni wlvgsiclsm slhflilyve plplifqitp
      961 lnltqwlmvl kislpvilmd etlkfvarny lepaile
//
LOCUS       NP_001102252             266 aa            linear   ROD 27-APR-2025
DEFINITION  elongator complex protein 6 [Rattus norvegicus].
ACCESSION   NP_001102252 XP_001075724 XP_343490
VERSION     NP_001102252.1
DBSOURCE    REFSEQ: accession NM_001108782.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Close,P., Gillard,M., Ladang,A., Jiang,Z., Papuga,J., Hawkes,N.,
            Nguyen,L., Chapelle,J.P., Bouillenne,F., Svejstrup,J., Fillet,M.
            and Chariot,A.
  TITLE     DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and
            migration of melanoma cells as subunits of Elongator
  JOURNAL   J Biol Chem 287 (39), 32535-32545 (2012)
   PUBMED   22854966
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Bolukbasi,E., Vass,S., Cobbe,N., Nelson,B., Simossis,V.,
            Dunbar,D.R. and Heck,M.M.
  TITLE     Drosophila poly suggests a novel role for the Elongator complex in
            insulin receptor-target of rapamycin signalling
  JOURNAL   Open Biol 2 (1), 110031 (2012)
   PUBMED   22645656
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166773.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_343490.3, XP_001075724.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166773.1, EV770366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..266
                     /product="elongator complex protein 6"
                     /note="UPF0405 protein C3orf75 homolog; elongator complex
                     protein 6 homolog; transmembrane protein 103"
                     /calculated_mol_wt=29328
     Region          2..251
                     /region_name="ELP6"
                     /note="Elongation complex protein 6; pfam09807"
                     /db_xref="CDD:462909"
     CDS             1..266
                     /gene="Elp6"
                     /gene_synonym="RGD1305478; Tmem103"
                     /coded_by="NM_001108782.2:23..823"
                     /db_xref="GeneID:363150"
                     /db_xref="RGD:1305478"
ORIGIN      
        1 mfpelnnlls itpdrteqgk ltllcdaktd gsflvhhfls fylkanckvc fvalvqsfsh
       61 ynivgqklgv sltaarergq lvfleglkss vevlfhsqee phplqflrea gagnlqslyt
      121 fiqdtlkpad sgespwkcpv llvdnlsvll slgvgavavl dfmqycratv ccelkgnvva
      181 lvhdtegaed eennillngl shqshlilrt qglatgfckd vhgqlsilwr rssqptaqra
      241 rsltyqykiq dknvsffakg msravl
//
LOCUS       NP_001011925             819 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear pore complex protein Nup93 [Rattus norvegicus].
ACCESSION   NP_001011925 XP_214639
VERSION     NP_001011925.1
DBSOURCE    REFSEQ: accession NM_001011925.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Pan,L., Song,X.W., Song,J.C., Shi,C.Y., Wang,Z.K., Huang,S.Q.,
            Guo,Z.F., Li,S.H., Zhao,X.X. and Ge,J.B.
  TITLE     Downregulation of NUP93 aggravates hypoxia-induced death of
            cardiomyocytes in vitro through abnormal regulation of gene
            transcription
  JOURNAL   Acta Pharmacol Sin 44 (5), 969-983 (2023)
   PUBMED   36807413
  REMARK    GeneRIF: Downregulation of NUP93 aggravates hypoxia-induced death
            of cardiomyocytes in vitro through abnormal regulation of gene
            transcription.
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Braun,D.A., Sadowski,C.E., Kohl,S., Lovric,S., Astrinidis,S.A.,
            Pabst,W.L., Gee,H.Y., Ashraf,S., Lawson,J.A., Shril,S., Airik,M.,
            Tan,W., Schapiro,D., Rao,J., Choi,W.I., Hermle,T., Kemper,M.J.,
            Pohl,M., Ozaltin,F., Konrad,M., Bogdanovic,R., Buscher,R.,
            Helmchen,U., Serdaroglu,E., Lifton,R.P., Antonin,W. and
            Hildebrandt,F.
  TITLE     Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause
            steroid-resistant nephrotic syndrome
  JOURNAL   Nat Genet 48 (4), 457-465 (2016)
   PUBMED   26878725
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Krull,S., Thyberg,J., Bjorkroth,B., Rackwitz,H.R. and Cordes,V.C.
  TITLE     Nucleoporins as components of the nuclear pore complex core
            structure and Tpr as the architectural element of the nuclear
            basket
  JOURNAL   Mol Biol Cell 15 (9), 4261-4277 (2004)
   PUBMED   15229283
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Hase,M.E. and Cordes,V.C.
  TITLE     Direct interaction with nup153 mediates binding of Tpr to the
            periphery of the nuclear pore complex
  JOURNAL   Mol Biol Cell 14 (5), 1923-1940 (2003)
   PUBMED   12802065
  REMARK    Erratum:[Mol Biol Cell. 2003 Aug;14(8):preceding Table of Contents]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081925.1.
            
            On Feb 11, 2005 this sequence version replaced XP_214639.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081925.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..819
                     /product="nuclear pore complex protein Nup93"
                     /note="nucleoporin Nup93; 93 kDa nucleoporin; nucleoporin
                     93kDa"
                     /calculated_mol_wt=93171
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Region          218..810
                     /region_name="Nic96"
                     /note="Nup93/Nic96; pfam04097"
                     /db_xref="CDD:461172"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N1F7; propagated from
                     UniProtKB/Swiss-Prot (Q66HC5.1)"
     CDS             1..819
                     /gene="Nup93"
                     /coded_by="NM_001011925.1:78..2537"
                     /db_xref="GeneID:291874"
                     /db_xref="RGD:1311525"
ORIGIN      
        1 mdtegfgell qqaeqlaaet egiselphve rnlqeiqqag erlrsrtltr tsqetadvka
       61 svllgsrgld ishisqrles lsaattfepl epvkdtdiqg flknekdnal lsaieesrkr
      121 tfgmaeeyhr esmlveweqv kqrilhtlla sgedaldftq esepsyvsdv sppgrsslds
      181 iemayarqiy iynekivsgh lqpnlvdlca svaelddksi sdmwamvkqm tdvvltpatd
      241 alksrssvev rmdfvkqalg yleqsyknyt lvtvfgnlhq aqlggvpgty qlvrsflnik
      301 lpapspglqd geveghpvwa liyycmrcgd llaasqvvsr aqhqlgefkt wfqeymnskd
      361 rrlspatenk lrlhyrralr nntdpykrav yciigrcdit dnqsevadkt edylwlklnq
      421 vcfdddgtss pqdrltlsqf qkqlledyge shftvnqqpf lyfqvlflta qfeaaiaflf
      481 rmerlrchav hvalvlfelk lllkssgqsa qllshepgdp pcmrrlnfvr llmlytrkfe
      541 stdprealqy fyflrdekds qgenmflrcv selviesref dmilgklend gsrkpgvidk
      601 ftsdtkpiin kvasvaenkg lfeeaaklyd laknadkvle lmnkllspvv pqisapqsnk
      661 erlknmalsi aeryraqgis ankfvdstfy llldlitffd eyhsghidra fdiidrlklv
      721 plnqesmeer vaafrnfsde irhnlsevll atmnilftqf krlkgtspss atrpqrvied
      781 rdsqlrsqar alitfagmip yrtsgdtnar lvqmevlmn
//
LOCUS       NP_075213                617 aa            linear   ROD 27-APR-2025
DEFINITION  prothrombin precursor [Rattus norvegicus].
ACCESSION   NP_075213
VERSION     NP_075213.2
DBSOURCE    REFSEQ: accession NM_022924.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Zou,Y., Guo,H., Zhang,Y., Zhang,Z., Liu,Y., Wang,J., Lu,H. and
            Qian,Z.
  TITLE     Analysis of coagulation parameters in patients with COVID-19 in
            Shanghai, China
  JOURNAL   Biosci Trends 14 (4), 285-289 (2020)
   PUBMED   32350161
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Wan,S., Xiang,Y., Fang,W., Zheng,Y., Li,B., Hu,Y., Lang,C.,
            Huang,D., Sun,Q., Xiong,Y., Huang,X., Lv,J., Luo,Y., Shen,L.,
            Yang,H., Huang,G. and Yang,R.
  TITLE     Clinical features and treatment of COVID-19 patients in northeast
            Chongqing
  JOURNAL   J Med Virol 92 (7), 797-806 (2020)
   PUBMED   32198776
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Zheng,Y., Xu,H., Yang,M., Zeng,Y., Chen,H., Liu,R., Li,Q., Zhang,N.
            and Wang,D.
  TITLE     Epidemiological characteristics and clinical features of 32
            critical and 67 noncritical cases of COVID-19 in Chengdu
  JOURNAL   J Clin Virol 127, 104366 (2020)
   PUBMED   32302954
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Yan,Y., Yang,Y., Wang,F., Ren,H., Zhang,S., Shi,X., Yu,X. and
            Dong,K.
  TITLE     Clinical characteristics and outcomes of patients with severe
            covid-19 with diabetes
  JOURNAL   BMJ Open Diabetes Res Care 8 (1) (2020)
   PUBMED   32345579
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Lisman,T., Kleiss,S., Patel,V.C., Fisher,C., Adelmeijer,J., Bos,S.,
            Singanayagam,A., Stoy,S.H., Shawcross,D.L. and Bernal,W.
  TITLE     In vitro efficacy of pro- and anticoagulant strategies in
            compensated and acutely ill patients with cirrhosis
  JOURNAL   Liver Int 38 (11), 1988-1996 (2018)
   PUBMED   29768734
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Takahashi,H., Wada,K., Niwano,H. and Shibata,A.
  TITLE     Comparison of prothrombin fragment 1 + 2 with thrombin-antithrombin
            III complex in plasma of patients with disseminated intravascular
            coagulation
  JOURNAL   Blood Coagul Fibrinolysis 3 (6), 813-818 (1992)
   PUBMED   1336986
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Banfield,D.K. and MacGillivray,R.T.
  TITLE     Partial characterization of vertebrate prothrombin cDNAs:
            amplification and sequence analysis of the B chain of thrombin from
            nine different species
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2779-2783 (1992)
   PUBMED   1557383
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Iwahana,H., Yoshimoto,K., Shigekiyo,T., Shirakami,A., Saito,S. and
            Itakura,M.
  TITLE     Detection of a single base substitution of the gene for prothrombin
            Tokushima. The application of PCR-SSCP for the genetic and
            molecular analysis of dysprothrombinemia
  JOURNAL   Int J Hematol 55 (1), 93-100 (1992)
   PUBMED   1349838
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Vu,T.K., Hung,D.T., Wheaton,V.I. and Coughlin,S.R.
  TITLE     Molecular cloning of a functional thrombin receptor reveals a novel
            proteolytic mechanism of receptor activation
  JOURNAL   Cell 64 (6), 1057-1068 (1991)
   PUBMED   1672265
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Cavanaugh,K.P., Gurwitz,D., Cunningham,D.D. and Bradshaw,R.A.
  TITLE     Reciprocal modulation of astrocyte stellation by thrombin and
            protease nexin-1
  JOURNAL   J Neurochem 54 (5), 1735-1743 (1990)
   PUBMED   1691280
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EX492416.1, DY318887.1, DW392486.1, DW391550.1 and CO575133.1.
            
            On Nov 29, 2007 this sequence version replaced NP_075213.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X52835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..617
                     /product="prothrombin precursor"
                     /EC_number="3.4.21.5"
                     /note="prothrombin; coagulation factor 2; thrombin"
                     /calculated_mol_wt=68030
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2374
     Region          25..89
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     mat_peptide     44..617
                     /product="Prothrombin. /id=PRO_0000028178"
                     /note="propagated from UniProtKB/Swiss-Prot (P18292.1)"
                     /calculated_mol_wt=65788
     Site            50
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            51
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            58
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            60
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            63
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            64
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            69
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            70
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            73
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            76
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00735,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Region          107..189
                     /region_name="KR"
                     /note="Kringle domain; smart00130"
                     /db_xref="CDD:214527"
     Site            118
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            order(133,143,169,171,179)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            200..201
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Region          215..292
                     /region_name="Kringle"
                     /note="Kringle domain; pfam00051"
                     /db_xref="CDD:395005"
     Site            224
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(239,253,275,277,284)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Site            310..311
                     /site_type="cleavage"
                     /note="Cleavage, by factor Xa.
                     /evidence=ECO:0000250|UniProtKB:P00734; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Region          312..359
                     /region_name="Thrombin_light"
                     /note="Thrombin light chain; pfam09396"
                     /db_xref="CDD:430582"
     Site            359..360
                     /site_type="cleavage"
                     /note="Cleavage, by factor Xa.
                     /evidence=ECO:0000250|UniProtKB:P00734; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Region          360..612
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            360
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(402,458,564)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Region          547..569
                     /region_name="High affinity receptor-binding region which
                     is also known as the TP508 peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P18292.1)"
     Site            552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18292.1)"
     Site            order(558,585,587)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..617
                     /gene="F2"
                     /coded_by="NM_022924.2:16..1869"
                     /db_xref="GeneID:29251"
                     /db_xref="RGD:61996"
ORIGIN      
        1 mshvrglglp gclalaalas lvhsqhvfla pqqalsllqr vrransgfle elrkgnlere
       61 cveeqcsyee afealespqd tdvfwakytv cdsvrkpret fmdclegrca mdlglnyhgn
      121 vsvthtgiec qlwrsryphr pdinstthpg adlkenfcrn pdsstsgpwc yttdptvrre
      181 ecsipvcgqe grttvkmtpr srgskenlsp plgecllerg rlyqgnlavt tlgspclawd
      241 slptktlsky qnfdpevklv qnfcrnpdrd eegawcfvaq qpgfeycsln ycdeavgeen
      301 hdgdesiagr ttdaefhtff dertfglgea dcglrplfek ksltdkteke lldsyidgri
      361 vegwdaekgi apwqvmlfrk spqellcgas lisdrwvlta ahcilyppwd knftendllv
      421 rigkhsrtry ernvekisml ekiyihpryn wrenldrdia llklkkpvpf sdyihpvclp
      481 dkqtvtsllq agykgrvtgw gnlretwttn ineiqpsvlq vvnlpiverp vckastriri
      541 tdnmfcagfk vndtkrgdac egdsggpfvm kspynhrwyq mgivswgegc drngkygfyt
      601 hvfrlkrwmq kvidqhr
//
LOCUS       NP_599177                659 aa            linear   ROD 27-APR-2025
DEFINITION  interferon-induced GTP-binding protein Mx2 [Rattus norvegicus].
ACCESSION   NP_599177 NP_058724
VERSION     NP_599177.2
DBSOURCE    REFSEQ: accession NM_134350.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Redina,O.E., Smolenskaya,S.E., Fedoseeva,L.A. and Markel,A.L.
  TITLE     [Differentially expressed genes in the locus associated with
            relative kidney weight and resting blood pressure in hypertensive
            rats of the ISIAH strain]
  JOURNAL   Mol Biol (Mosk) 50 (6), 944-952 (2016)
   PUBMED   28064310
  REMARK    GeneRIF: Six differentially expressed genes (Kcne1, Rcan1, Mx1,
            Mx2, Tmprss2, and RGD1559516) were identified in the renal cortex,
            and three genes (Rcan1, Mx2, and Tmprss2) were identified in the
            renal medulla.
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Rennie,M.L., McKelvie,S.A., Bulloch,E.M. and Kingston,R.L.
  TITLE     Transient dimerization of human MxA promotes GTP hydrolysis,
            resulting in a mechanical power stroke
  JOURNAL   Structure 22 (10), 1433-1445 (2014)
   PUBMED   25295396
REFERENCE   3  (residues 1 to 659)
  AUTHORS   He,D.N., Zhang,X.M., Liu,K., Pang,R., Zhao,J., Zhou,B. and
            Chen,P.Y.
  TITLE     In vitro inhibition of the replication of classical swine fever
            virus by porcine Mx1 protein
  JOURNAL   Antiviral Res 104, 128-135 (2014)
   PUBMED   24500530
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Wisskirchen,C., Ludersdorfer,T.H., Muller,D.A., Moritz,E. and
            Pavlovic,J.
  TITLE     Interferon-induced antiviral protein MxA interacts with the
            cellular RNA helicases UAP56 and URH49
  JOURNAL   J Biol Chem 286 (40), 34743-34751 (2011)
   PUBMED   21859714
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Schoggins,J.W., Wilson,S.J., Panis,M., Murphy,M.Y., Jones,C.T.,
            Bieniasz,P. and Rice,C.M.
  TITLE     A diverse range of gene products are effectors of the type I
            interferon antiviral response
  JOURNAL   Nature 472 (7344), 481-485 (2011)
   PUBMED   21478870
  REMARK    Erratum:[Nature. 2015 Sep 3;525(7567):144. doi:
            10.1038/nature14554. PMID: 26153858]
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Andersson,I., Bladh,L., Mousavi-Jazi,M., Magnusson,K.E.,
            Lundkvist,A., Haller,O. and Mirazimi,A.
  TITLE     Human MxA protein inhibits the replication of Crimean-Congo
            hemorrhagic fever virus
  JOURNAL   J Virol 78 (8), 4323-4329 (2004)
   PUBMED   15047845
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Bridgen,A., Dalrymple,D.A., Weber,F. and Elliott,R.M.
  TITLE     Inhibition of Dugbe nairovirus replication by human MxA protein
  JOURNAL   Virus Res 99 (1), 47-50 (2004)
   PUBMED   14687945
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Johannes,L., Kambadur,R., Lee-Hellmich,H., Hodgkinson,C.A.,
            Arnheiter,H. and Meier,E.
  TITLE     Antiviral determinants of rat Mx GTPases map to the
            carboxy-terminal half
  JOURNAL   J Virol 71 (12), 9792-9795 (1997)
   PUBMED   9371647
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Meier,E., Kunz,G., Haller,O. and Arnheiter,H.
  TITLE     Activity of rat Mx proteins against a rhabdovirus
  JOURNAL   J Virol 64 (12), 6263-6269 (1990)
   PUBMED   2173790
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099808.1.
            
            On Jul 31, 2005 this sequence version replaced NP_599177.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099808.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q12"
     Protein         1..659
                     /product="interferon-induced GTP-binding protein Mx2"
                     /note="interferon-induced GTP-binding protein Mx3;
                     myxovirus resistance protein 2; myxovirus resistance
                     protein 3; myxovirus (influenza virus) resistance 3;
                     myxovirus (influenza virus) resistance 2"
                     /calculated_mol_wt=74818
     Region          66..338
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          75..82
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Site            75..82
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(76,78..83,95..96,101,176,246,248..249,277..281,284)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(77..78,180,193,218,220,222..225,227..228,249,
                     251..254,280..282)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          100..102
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Site            101
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            105..107
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          176..179
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Site            176..179
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(178..179,209..210)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          245..248
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Site            245..248
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          257..544
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          277..280
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Site            277..279
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          547..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18590.1)"
     Region          567..657
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..659
                     /gene="Mx2"
                     /gene_synonym="Mx3"
                     /coded_by="NM_134350.2:122..2101"
                     /db_xref="GeneID:286918"
                     /db_xref="RGD:628821"
ORIGIN      
        1 mvlsteenrs vdlvnlpsvp lpdgeagvge nnkdslnnlc sqyeekvrpc idlidslral
       61 gveqdlalpa iavigdqssg kssvlealsg valprgsgiv trcplvlklk klnqgeewkg
      121 kvtyddieve lsdpseveea intgqnhiag vglgisdkli sldvssphvp dltlidlpgi
      181 trvavgnqpa digrqikrli tnyiqkqeti nlvvvpsnvd iattealsma qkvdpdgdrt
      241 igiltkpdlv drgtedkvvd vvrnlvchlk kgymivkcrg qqdiqeqlsl aealqkeqvf
      301 fkehpqfral ledgkatvpc laerltmeli shickslpll enqikeshqs tseelqkyga
      361 dipedenekt lfliekinaf nqditaiveg eeivrekecr lftklrkeff lwseeiernf
      421 qkgsdalyke vytfemqyrg relpgfvnyk tfeniirrqi ktleepamem lhkvteivra
      481 afttvseknf seffnlhrtt kskledirle qeteaekair lhfqmeqiiy cqdqiyrkal
      541 qkvreeeaee eerkhgksrs aqspnlqtss mdeifqhlna yrqeahncis shipliiqyf
      601 ilkmfaeklq kgmlqllqdk dscswllkek sdtsekrrfl kerlarlaqa qrrlakfpg
//
LOCUS       NP_001002279             237 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF166 [Rattus norvegicus].
ACCESSION   NP_001002279 XP_344785
VERSION     NP_001002279.1
DBSOURCE    REFSEQ: accession NM_001002279.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY606065.1.
            
            On Aug 30, 2004 this sequence version replaced XP_344785.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY606065.1, BC100057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132290, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..237
                     /product="E3 ubiquitin-protein ligase RNF166"
                     /EC_number="2.3.2.27"
                     /note="RING-type E3 ubiquitin transferase RNF166"
                     /calculated_mol_wt=25933
     Region          30..76
                     /region_name="RING-HC_RNF166"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 166 (RNF166) and similar proteins; cd16549"
                     /db_xref="CDD:438211"
     Region          92..124
                     /region_name="zf_C2HC_14"
                     /note="C2HC Zing finger domain; pfam18574"
                     /db_xref="CDD:465807"
     Region          149..208
                     /region_name="zf-Di19"
                     /note="Drought induced 19 protein (Di19), zinc-binding;
                     pfam05605"
                     /db_xref="CDD:428539"
     CDS             1..237
                     /gene="Rnf166"
                     /coded_by="NM_001002279.1:52..765"
                     /db_xref="GeneID:365022"
                     /db_xref="RGD:1302950"
ORIGIN      
        1 mamfrslvas aqqrqppagp aggdsgleaq fscpiclevy hrpvaigscg htfcgeclqp
       61 clqvpsplcp lcrlpfdpkk vdkathvekq lssykapcrg cnkkvtlakm rahissclkv
      121 qeqmancpkf vpvvptsqpi psnipnrstf acpycgarnl dqqelvkhcv eshrsdpnrv
      181 vcpicsampw gdpsyksanf lqhllhrhkf sydtfvdysi deeaafqaal alslsen
//
LOCUS       NP_001008384             488 aa            linear   ROD 27-APR-2025
DEFINITION  dipeptidase 3 precursor [Rattus norvegicus].
ACCESSION   NP_001008384 XP_344762
VERSION     NP_001008384.1
DBSOURCE    REFSEQ: accession NM_001008383.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Yoshitake,H., Yanagida,M., Maruyama,M., Takamori,K., Hasegawa,A.
            and Araki,Y.
  TITLE     Molecular characterization and expression of dipeptidase 3, a
            testis-specific membrane-bound dipeptidase: complex formation with
            TEX101, a germ-cell-specific antigen in the mouse testis
  JOURNAL   J Reprod Immunol 90 (2), 202-213 (2011)
   PUBMED   21724266
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Kogo,H., Kowa-Sugiyama,H., Yamada,K., Bolor,H., Tsutsumi,M.,
            Ohye,T., Inagaki,H., Taniguchi,M., Toda,T. and Kurahashi,H.
  TITLE     Screening of genes involved in chromosome segregation during
            meiosis I: toward the identification of genes responsible for
            infertility in humans
  JOURNAL   J Hum Genet 55 (5), 293-299 (2010)
   PUBMED   20339383
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Habib,G.M., Shi,Z.Z., Cuevas,A.A. and Lieberman,M.W.
  TITLE     Identification of two additional members of the membrane-bound
            dipeptidase family
  JOURNAL   FASEB J 17 (10), 1313-1315 (2003)
   PUBMED   12738806
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085826.1.
            
            On Dec 16, 2004 this sequence version replaced XP_344762.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..488
                     /product="dipeptidase 3 precursor"
                     /EC_number="3.4.13.19"
                     /note="putative membrane-bound dipeptidase 3"
                     /calculated_mol_wt=49600
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X4.1)"
                     /calculated_mol_wt=3789
     mat_peptide     36..459
                     /product="Dipeptidase 3. /id=PRO_0000231615"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X4.1)"
                     /calculated_mol_wt=46608
     Region          41..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2X4.1)"
     Region          84..404
                     /region_name="Peptidase_M19"
                     /note="Membrane dipeptidase (Peptidase family M19);
                     pfam01244"
                     /db_xref="CDD:395996"
     Site            order(94,96,140,193,266,287,298,356,359)
                     /site_type="active"
                     /db_xref="CDD:238626"
     Site            order(142,151..153,155..156,159,163,203..204,206..207,
                     210..211)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238626"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U2X4.1)"
     CDS             1..488
                     /gene="Dpep3"
                     /coded_by="NM_001008383.1:116..1582"
                     /db_xref="GeneID:364994"
                     /db_xref="RGD:1305484"
ORIGIN      
        1 mqptgpegpr alslrplghr lsllgvllii pslwvtcnqt tpslssapts pgassamttp
       61 gipndtttsg vtsdprlreq alalmrdfpl vdghndlpll lrelfqnklq dvnlhnftrg
      121 qtsldrlrdg lvgaqfwsay ipcqtqdrda vrvaleqidl irrmcsaype lelvtsadgl
      181 nstqklacli glegghsldt slavlrsfye lgvryltltf tcstpwaesa tkfrhhfytn
      241 isgltsfgek vveemnrigm midlshasdt lvkqtleasr apvifshsaa rsvcdnllnv
      301 pddilqllkk nggivmvtls mgvlqcslla nvstvadhfd hirtvigsef igiggsydgs
      361 grfpqgledv stypvlleel lrrgwgeqel qgvlrgnllr vfrqveqvre kslgqspvev
      421 vfperqqsst chshllpqsq dahlkvtklp ssqvlqrask appcpllglv aavtspaftl
      481 wlccsghr
//
LOCUS       NP_596900                452 aa            linear   ROD 27-APR-2025
DEFINITION  scaffold protein ILK [Rattus norvegicus].
ACCESSION   NP_596900
VERSION     NP_596900.1
DBSOURCE    REFSEQ: accession NM_133409.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Yan,G., Sun,R., Chen,Z., Pan,X., Sheng,Z. and Tang,C.
  TITLE     PTBP1 Targets ILK to Regulate the Hypoxia-Induced Phenotypic
            Transformation of Pulmonary Artery Smooth Muscle Cells
  JOURNAL   Drug Des Devel Ther 15, 2025-2033 (2021)
   PUBMED   34012255
  REMARK    GeneRIF: PTBP1 Targets ILK to Regulate the Hypoxia-Induced
            Phenotypic Transformation of Pulmonary Artery Smooth Muscle Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Hou,J., Liu,B., Zhu,B., Wang,D., Qiao,Y., Luo,E., Nawabi,A.Q.,
            Yan,G. and Tang,C.
  TITLE     Role of integrin-linked kinase in the hypoxia-induced phenotypic
            transition of pulmonary artery smooth muscle cells: Implications
            for hypoxic pulmonary hypertension
  JOURNAL   Exp Cell Res 382 (2), 111476 (2019)
   PUBMED   31255599
  REMARK    GeneRIF: ILK initiates the phenotypic transition of pulmonary
            artery smooth muscle cells.
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Li,M., Zhou,H., Di,J., Yang,M. and Jia,F.
  TITLE     ILK participates in renal interstitial fibrosis by altering the
            phenotype of renal tubular epithelial cells via TGF-beta1/smad
            pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (1), 289-296 (2019)
   PUBMED   30657569
  REMARK    GeneRIF: Accompanied by the TGF-beta1-induced phenotype change in
            rat kidney epithelial cell line NRK-52E, both mRNA and protein
            levels of ILK were upregulated. Overexpression of ILK remarkably
            stimulated the phenotype change in NRK-52E cells. ILK is
            upregulated during renal fibrosis. ILK participates in the
            development of renal fibrosis by altering phenotypes of renal
            tubular epithelial cells via a TGF-beta1/smad pathway.
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Li,G., Li,Y.Y., Sun,J.E., Lin,W.H. and Zhou,R.X.
  TITLE     ILK-PI3K/AKT pathway participates in cutaneous wound contraction by
            regulating fibroblast migration and differentiation to
            myofibroblast
  JOURNAL   Lab Invest 96 (7), 741-751 (2016)
   PUBMED   27111285
  REMARK    GeneRIF: Investigated the role of ILK in cutaneous wound
            contraction. We found that ILK was involved in cutaneous wound
            healing, and ILK and PI3K/AKT inhibitors inhibited wound
            contraction and re-epithelialization, consequently delaying wound
            healing in vivo.
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Moraes,J.A., Frony,A.C., Dias,A.M., Renovato-Martins,M.,
            Rodrigues,G., Marcinkiewicz,C., Assreuy,J. and Barja-Fidalgo,C.
  TITLE     Alpha1beta1 and integrin-linked kinase interact and modulate
            angiotensin II effects in vascular smooth muscle cells
  JOURNAL   Atherosclerosis 243 (2), 477-485 (2015)
   PUBMED   26520903
  REMARK    GeneRIF: Alpha1beta1 and integrin-linked kinase interact and
            modulate angiotensin II effects on vascular smooth muscle cell
            proliferation/migration.
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Mulholland,D.J., Dedhar,S. and Vogl,A.W.
  TITLE     Rat seminiferous epithelium contains a unique junction (Ectoplasmic
            specialization) with signaling properties both of cell/cell and
            cell/matrix junctions
  JOURNAL   Biol Reprod 64 (1), 396-407 (2001)
   PUBMED   11133699
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Janji,B., Melchior,C., Vallar,L. and Kieffer,N.
  TITLE     Cloning of an isoform of integrin-linked kinase (ILK) that is
            upregulated in HT-144 melanoma cells following TGF-beta1
            stimulation
  JOURNAL   Oncogene 19 (27), 3069-3077 (2000)
   PUBMED   10871859
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Lynch,D.K., Ellis,C.A., Edwards,P.A. and Hiles,I.D.
  TITLE     Integrin-linked kinase regulates phosphorylation of serine 473 of
            protein kinase B by an indirect mechanism
  JOURNAL   Oncogene 18 (56), 8024-8032 (1999)
   PUBMED   10637513
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Li,F., Liu,J., Mayne,R. and Wu,C.
  TITLE     Identification and characterization of a mouse protein kinase that
            is highly homologous to human integrin-linked kinase
  JOURNAL   Biochim Biophys Acta 1358 (3), 215-220 (1997)
   PUBMED   9366252
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Hannigan,G.E., Leung-Hagesteijn,C., Fitz-Gibbon,L., Coppolino,M.G.,
            Radeva,G., Filmus,J., Bell,J.C. and Dedhar,S.
  TITLE     Regulation of cell adhesion and anchorage-dependent growth by a new
            beta 1-integrin-linked protein kinase
  JOURNAL   Nature 379 (6560), 91-96 (1996)
   PUBMED   8538749
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC062406.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062406.1, SRR8487227.44050.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..452
                     /product="scaffold protein ILK"
                     /EC_number="2.7.11.1"
                     /note="integrin-linked protein kinase;
                     beta-integrin-linked kinase; 59 kDa
                     serine/threonine-protein kinase; inactive integrin-linked
                     kinase"
                     /calculated_mol_wt=51242
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q13418; propagated from
                     UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          2..30
                     /region_name="ANK 1.
                     /evidence=ECO:0000250|UniProtKB:Q13418"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          <8..162
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          31..63
                     /region_name="ANK 2.
                     /evidence=ECO:0000250|UniProtKB:Q13418"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          33..139
                     /region_name="Interaction with LIMS1.
                     /evidence=ECO:0000250|UniProtKB:Q13418"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Site            order(33,35,39..40,43..45,47..48,52,55,64,66,68,72..73,
                     76..78,80..81,85,88,97,99,101,105..106,109..111,113..114,
                     118,121,130)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          33..64
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          66..97
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          99..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          130..174
                     /region_name="ANK 5.
                     /evidence=ECO:0000250|UniProtKB:Q13418"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13418; propagated from
                     UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          180..212
                     /region_name="PH-like, mediates interaction with TGFB1I1.
                     /evidence=ECO:0000250|UniProtKB:O55222"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13418; propagated from
                     UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          198..449
                     /region_name="PK_ILK"
                     /note="Pseudokinase domain of Integrin Linked Kinase;
                     cd14057"
                     /db_xref="CDD:270959"
     Site            order(200,202..204,207,218,220,269..272,279,323,326,339,
                     341)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270959"
     Site            order(225,348..351,361..364,396..399,401..403,406)
                     /site_type="other"
                     /note="Parvin interface [polypeptide binding]"
                     /db_xref="CDD:270959"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13418; propagated from
                     UniProtKB/Swiss-Prot (Q99J82.1)"
     Region          363..371
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q13418"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99J82.1)"
     Site            426
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55222; propagated from
                     UniProtKB/Swiss-Prot (Q99J82.1)"
     CDS             1..452
                     /gene="Ilk"
                     /gene_synonym="ILK-1; ILK-2; p59ILK"
                     /coded_by="NM_133409.2:64..1422"
                     /db_xref="GeneID:170922"
                     /db_xref="RGD:620063"
ORIGIN      
        1 mddiftqcre gnavavrlwl dntendlnqg ddhgfsplhw acregrsavv emlimrgari
       61 nvmnrgddtp lhlaashghr divqkllqyk adinavnehg nvplhyacfw gqdqvaedlv
      121 angalvsicn kygempvdka kaplrellre raekmgqnln ripykdtfwk gttrtrprng
      181 tlnkhsgidf kqlnflakln enhsgelwkg rwqgndivvk vlkvrdwstr ksrdfneecp
      241 rlrifshpnv lpvlgacqap paphptlith wmpygslynv lhegtnfvvd qsqavkfald
      301 margmaflht lepliprhal nsrsvmided mtarismadv kfsfqcpgrm yapawvapea
      361 lqkkpedtnr rsadmwsfav llwelvtrev pfadlsnmei gmkvaleglr ptippgisph
      421 vcklmkicmn edpakrpkfd mivpilekmq dk
//
LOCUS       NP_001029246             248 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.9cy [Rattus norvegicus].
ACCESSION   NP_001029246
VERSION     NP_001029246.1
DBSOURCE    REFSEQ: accession NM_001034074.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO562261.1, BC078780.1 and
            M34136.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.9, also known as variant 8)
            has multiple differences in the coding region, compared to variant
            1. These differences result in an isoform (Tpm1.9cy, also referred
            to as TM-5b) that is shorter and has distinct N- and C-termini
            compared to isoform a. Isoform Tpm1.9cy is the same length as
            isoforms Tpm1.8cy and Tpm1.13 but is the product of alternate
            splicing and contains short regions of sequence differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078780.1, M60669.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform Tpm1.9cy"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=28565
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001034074.1:152..898"
                     /note="isoform Tpm1.9cy is encoded by transcript variant
                     Tpm1.9"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeerags lqreldqerk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egqvrqleeq lrimdqtlka lmaaedkysq
      181 kedkyeeeik vlsdklkeae traefaersv tkleksiddl eekvahakee nlsmhqmldq
      241 tllelnnm
//
LOCUS       NP_037225                372 aa            linear   ROD 27-APR-2025
DEFINITION  homeobox protein Nkx-2.1 [Rattus norvegicus].
ACCESSION   NP_037225 XP_001079296 XP_216720
VERSION     NP_037225.1
DBSOURCE    REFSEQ: accession NM_013093.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Zang,S., Yin,X. and Li,P.
  TITLE     Downregulation of TTF1 in the rat hypothalamic ARC or AVPV nucleus
            inhibits Kiss1 and GnRH expression, leading to puberty delay
  JOURNAL   Reprod Biol Endocrinol 19 (1), 30 (2021)
   PUBMED   33622350
  REMARK    GeneRIF: Downregulation of TTF1 in the rat hypothalamic ARC or AVPV
            nucleus inhibits Kiss1 and GnRH expression, leading to puberty
            delay.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Xu,B., O'Donnell,M., O'Donnell,J., Yu,J., Zhang,Y., Sartor,M.A. and
            Koenig,R.J.
  TITLE     Adipogenic Differentiation of Thyroid Cancer Cells Through the
            Pax8-PPARgamma Fusion Protein Is Regulated by Thyroid Transcription
            Factor 1 (TTF-1)
  JOURNAL   J Biol Chem 291 (37), 19274-19286 (2016)
   PUBMED   27435678
  REMARK    GeneRIF: data indicate that TTF-1 interacts with PPFP to inhibit
            the pro-adipogenic response to pioglitazone, and that the ability
            of pioglitazone to decrease TTF-1 expression contributes to its
            pro-adipogenic action.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Koht,J., Lostegaard,S.O., Wedding,I., Vidailhet,M., Louha,M. and
            Tallaksen,C.M.
  TITLE     Benign hereditary chorea, not only chorea: a family case
            presentation
  JOURNAL   Cerebellum Ataxias 3, 3 (2016)
   PUBMED   26839702
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Uemae,Y., Sakamoto,J., Hidaka,Y., Hiratsuka,A., Susa,T., Kato,Y.
            and Suzuki,M.
  TITLE     Gene expression, function, and diversity of Nkx2-4 in the rainbow
            trout, Oncorhynchus mykiss
  JOURNAL   Gen Comp Endocrinol 206, 193-202 (2014)
   PUBMED   25051213
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Katagiri,N., Uemae,Y., Sakamoto,J., Hidaka,Y., Susa,T., Kato,Y.,
            Kimura,S. and Suzuki,M.
  TITLE     Molecular cloning and functional characterization of two forms of
            Pax8 in the rainbow trout, Oncorhynchus mykiss
  JOURNAL   Gen Comp Endocrinol 198, 22-31 (2014)
   PUBMED   24380675
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Yan,C., Sever,Z. and Whitsett,J.A.
  TITLE     Upstream enhancer activity in the human surfactant protein B gene
            is mediated by thyroid transcription factor 1
  JOURNAL   J Biol Chem 270 (42), 24852-24857 (1995)
   PUBMED   7559607
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Acebron,A., Aza-Blanc,P., Rossi,D.L., Lamas,L. and Santisteban,P.
  TITLE     Congenital human thyroglobulin defect due to low expression of the
            thyroid-specific transcription factor TTF-1
  JOURNAL   J Clin Invest 96 (2), 781-785 (1995)
   PUBMED   7635972
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Ikeda,K., Clark,J.C., Shaw-White,J.R., Stahlman,M.T., Boutell,C.J.
            and Whitsett,J.A.
  TITLE     Gene structure and expression of human thyroid transcription
            factor-1 in respiratory epithelial cells
  JOURNAL   J Biol Chem 270 (14), 8108-8114 (1995)
   PUBMED   7713914
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Abramowicz,M.J., Vassart,G. and Christophe,D.
  TITLE     Functional study of the human thyroid peroxidase gene promoter
  JOURNAL   Eur J Biochem 203 (3), 467-473 (1992)
   PUBMED   1735431
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Guazzi,S., Price,M., De Felice,M., Damante,G., Mattei,M.G. and Di
            Lauro,R.
  TITLE     Thyroid nuclear factor 1 (TTF-1) contains a homeodomain and
            displays a novel DNA binding specificity
  JOURNAL   EMBO J 9 (11), 3631-3639 (1990)
   PUBMED   1976511
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Nov 23, 2008 this sequence version replaced
            XP_216720.4, XP_001079296.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB894119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788, SAMN16676807
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..372
                     /product="homeobox protein Nkx-2.1"
                     /note="TTF-1; thyroid nuclear factor 1; thyroid
                     transcription factor 1 TTF-1 NK-2; thyroid-specific
                     transcription factor 1"
                     /calculated_mol_wt=38391
     Region          162..218
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          219..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23441.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P23441.1)"
     Region          269..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23441.1)"
     Region          312..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23441.1)"
     CDS             1..372
                     /gene="Nkx2-1"
                     /gene_synonym="Titf1; TTF1"
                     /coded_by="NM_013093.1:1..1119"
                     /db_xref="GeneID:25628"
                     /db_xref="RGD:3866"
ORIGIN      
        1 msmspkhttp fsvsdilspl eesykkvgme ggglgaplaa yrqgqaappa aamqqhavgh
       61 hgavtaayhm taagvpqlsh savggycngn lgnvselppy qdtmrnsasg pgwyganpdp
      121 rfpaisrfmg pasgmnmsgm gglgslgdvs knmaplpsap rrkrrvlfsq aqvyelerrf
      181 kqqkylsape rehlasmihl tptqvkiwfq nhrykmkrqa kdkaaqqqlq qdsggggggg
      241 ggagcpqqqq aqqqsprrva vpvlvkdgkp cqagapapga aslqghaqqq aqqqaqaaqa
      301 aaaaisvgsg gaglgahpgh qpgsagqspd lahhaaspaa lqgqvsslsh lnssgsdyga
      361 mscstllygr tw
//
LOCUS       NP_001019457             269 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor Spi-B [Rattus norvegicus].
ACCESSION   NP_001019457 XP_574441
VERSION     NP_001019457.1
DBSOURCE    REFSEQ: accession NM_001024286.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Dahl,R., Ramirez-Bergeron,D.L., Rao,S. and Simon,M.C.
  TITLE     Spi-B can functionally replace PU.1 in myeloid but not lymphoid
            development
  JOURNAL   EMBO J 21 (9), 2220-2230 (2002)
   PUBMED   11980719
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Rao,S., Matsumura,A., Yoon,J. and Simon,M.C.
  TITLE     SPI-B activates transcription via a unique proline, serine, and
            threonine domain and exhibits DNA binding affinity differences from
            PU.1
  JOURNAL   J Biol Chem 274 (16), 11115-11124 (1999)
   PUBMED   10196196
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089881.1.
            
            On May 27, 2005 this sequence version replaced XP_574441.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089881.1, CO555547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..269
                     /product="transcription factor Spi-B"
                     /note="Spi-B transcription factor (Spi-1/PU.1 related)"
                     /calculated_mol_wt=29269
     Region          1..32
                     /region_name="TAD1 (Acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA3.1)"
     Region          42..63
                     /region_name="TAD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EBA3.1)"
     Region          175..263
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..269
                     /gene="Spib"
                     /coded_by="NM_001024286.1:9..818"
                     /db_xref="GeneID:499146"
                     /db_xref="RGD:1565899"
ORIGIN      
        1 mlaleaaqld gphlsclqyp egvfydldsc ksfsypdsdg gpdstwgwte appapaiaay
       61 eafdpaataa fahtqavqlc yghgpspsty spvgtldpap sleasgpglq vypsedftsq
      121 tlgslayapy pspvlseeed illdspalev sdsesdeall agsegrgsea garkklrlyq
      181 fllelllrgd mrecvwwvep gagvfqfssk hkellarrwg qqkgnrkrmt yqklaralrn
      241 yaktgeirkv krkltyqfds allpaarra
//
LOCUS       NP_446334                562 aa            linear   ROD 27-APR-2025
DEFINITION  extracellular matrix protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_446334 XP_215645
VERSION     NP_446334.1
DBSOURCE    REFSEQ: accession NM_053882.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Li,Z., Zhang,Y., Liu,Z., Wu,X., Zheng,Y., Tao,Z., Mao,K., Wang,J.,
            Lin,G., Tian,L., Ji,Y., Qin,M., Sun,S., Zhu,X. and Sun,B.
  TITLE     ECM1 controls T(H)2 cell egress from lymph nodes through
            re-expression of S1P(1)
  JOURNAL   Nat Immunol 12 (2), 178-185 (2011)
   PUBMED   21217760
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Merregaert,J., Van Langen,J., Hansen,U., Ponsaerts,P., El
            Ghalbzouri,A., Steenackers,E., Van Ostade,X. and Sercu,S.
  TITLE     Phospholipid scramblase 1 is secreted by a lipid raft-dependent
            pathway and interacts with the extracellular matrix protein 1 in
            the dermal epidermal junction zone of human skin
  JOURNAL   J Biol Chem 285 (48), 37823-37837 (2010)
   PUBMED   20870722
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Kong,L., Tian,Q., Guo,F., Mucignat,M.T., Perris,R., Sercu,S.,
            Merregaert,J., Di Cesare,P.E. and Liu,C.J.
  TITLE     Interaction between cartilage oligomeric matrix protein and
            extracellular matrix protein 1 mediates endochondral bone growth
  JOURNAL   Matrix Biol 29 (4), 276-286 (2010)
   PUBMED   20138147
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Mongiat,M., Fu,J., Oldershaw,R., Greenhalgh,R., Gown,A.M. and
            Iozzo,R.V.
  TITLE     Perlecan protein core interacts with extracellular matrix protein 1
            (ECM1), a glycoprotein involved in bone formation and angiogenesis
  JOURNAL   J Biol Chem 278 (19), 17491-17499 (2003)
   PUBMED   12604605
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Hamada,T., McLean,W.H., Ramsay,M., Ashton,G.H., Nanda,A.,
            Jenkins,T., Edelstein,I., South,A.P., Bleck,O., Wessagowit,V.,
            Mallipeddi,R., Orchard,G.E., Wan,H., Dopping-Hepenstal,P.J.,
            Mellerio,J.E., Whittock,N.V., Munro,C.S., van Steensel,M.A.,
            Steijlen,P.M., Ni,J., Zhang,L., Hashimoto,T., Eady,R.A. and
            McGrath,J.A.
  TITLE     Lipoid proteinosis maps to 1q21 and is caused by mutations in the
            extracellular matrix protein 1 gene (ECM1)
  JOURNAL   Hum Mol Genet 11 (7), 833-840 (2002)
   PUBMED   11929856
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Han,Z., Ni,J., Smits,P., Underhill,C.B., Xie,B., Chen,Y., Liu,N.,
            Tylzanowski,P., Parmelee,D., Feng,P., Ding,I., Gao,F., Gentz,R.,
            Huylebroeck,D., Merregaert,J. and Zhang,L.
  TITLE     Extracellular matrix protein 1 (ECM1) has angiogenic properties and
            is expressed by breast tumor cells
  JOURNAL   FASEB J 15 (6), 988-994 (2001)
   PUBMED   11292659
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Deckers,M.M., Smits,P., Karperien,M., Ni,J., Tylzanowski,P.,
            Feng,P., Parmelee,D., Zhang,J., Bouffard,E., Gentz,R., Lowik,C.W.
            and Merregaert,J.
  TITLE     Recombinant human extracellular matrix protein 1 inhibits alkaline
            phosphatase activity and mineralization of mouse embryonic
            metatarsals in vitro
  JOURNAL   Bone 28 (1), 14-20 (2001)
   PUBMED   11165938
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Bhalerao,J., Tylzanowski,P., Filie,J.D., Kozak,C.A. and
            Merregaert,J.
  TITLE     Molecular cloning, characterization, and genetic mapping of the
            cDNA coding for a novel secretory protein of mouse. Demonstration
            of alternative splicing in skin and cartilage
  JOURNAL   J Biol Chem 270 (27), 16385-16394 (1995)
   PUBMED   7608209
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085879.1.
            
            On Nov 22, 2004 this sequence version replaced XP_215645.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085879.1, SRR8487227.274131.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132291,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..562
                     /product="extracellular matrix protein 1 precursor"
                     /note="secretory component p85"
                     /calculated_mol_wt=61405
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1862
     mat_peptide     20..562
                     /product="Extracellular matrix protein 1.
                     /id=PRO_0000043411"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62894.2)"
                     /calculated_mol_wt=61405
     Region          45..562
                     /region_name="ECM1"
                     /note="Extracellular matrix protein 1 (ECM1); pfam05782"
                     /db_xref="CDD:461739"
     Region          46..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62894.2)"
     Region          119..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62894.2)"
     Region          172..427
                     /region_name="2 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62894.2)"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62894.2)"
     Site            466
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62894.2)"
     Site            538
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62894.2)"
     Region          539..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62894.2)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62894.2)"
     CDS             1..562
                     /gene="Ecm1"
                     /coded_by="NM_053882.1:108..1796"
                     /db_xref="GeneID:116662"
                     /db_xref="RGD:620357"
ORIGIN      
        1 mgtirssali laclalasaa segafkvsdq remkpehlfq hlhevgyaap psppqtrrlq
       61 vhhsetsphd pplfeeqkev qppsspedip vyeeewltfl npnvgkvdpa lpqeaiplqk
      121 eqpppripie qkeidppvqh qeeivqsrqk eekpptltgq hppeprtwnp arhcqqgrrg
      181 iwghrldgfp pgrpspdnlk qiclperqhv vygpwnlpqt gyshlsrqge alnlletgys
      241 rccrcrsdtn rldcvklvwe damtqfceae fsvktrphlc ckqrgeerfs cfqkeaprpd
      301 yllrpcpihq tgissgtqlp fppglptpdn vknicllrrf rsvprnlpat daiqrqlqal
      361 trletefqrc crqghnhtct wkawedtldg ycdrelaikt hphscchypp spardecfah
      421 lapypnydrd lltvdlsrvt pnlmdhlcgn grvlskhkqi pgliqnmtvr ccelpypeqa
      481 ccgeeeklaf iedlcgprrn swkdpalcct lspgdkqanc fntnylrnva lvagdtgnat
      541 glgqqgptgg tnvgpapgsk ee
//
LOCUS       NP_001007609             163 aa            linear   ROD 27-APR-2025
DEFINITION  S-phase kinase-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_001007609 XP_213290
VERSION     NP_001007609.1
DBSOURCE    REFSEQ: accession NM_001007608.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Ye,B., Liu,B., Hao,L., Zhu,X., Yang,L., Wang,S., Xia,P., Du,Y.,
            Meng,S., Huang,G., Qin,X., Wang,Y., Yan,X., Li,C., Hao,J., Zhu,P.,
            He,L., Tian,Y. and Fan,Z.
  TITLE     Klf4 glutamylation is required for cell reprogramming and early
            embryonic development in mice
  JOURNAL   Nat Commun 9 (1), 1261 (2018)
   PUBMED   29593216
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Reiterer,V., Figueras-Puig,C., Le Guerroue,F., Confalonieri,S.,
            Vecchi,M., Jalapothu,D., Kanse,S.M., Deshaies,R.J., Di Fiore,P.P.,
            Behrends,C. and Farhan,H.
  TITLE     The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits
            SCFFBXW7 function
  JOURNAL   EMBO J 36 (3), 260-273 (2017)
   PUBMED   28007894
  REMARK    Erratum:[EMBO J. 2018 Mar 15;37(6):e99170. doi:
            10.15252/embj.201899170. PMID: 29545456]
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Chu,W.K., Payne,M.J., Beli,P., Hanada,K., Choudhary,C. and
            Hickson,I.D.
  TITLE     FBH1 influences DNA replication fork stability and homologous
            recombination through ubiquitylation of RAD51
  JOURNAL   Nat Commun 6, 5931 (2015)
   PUBMED   25585578
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Hayes,J.D. and Dinkova-Kostova,A.T.
  TITLE     The Nrf2 regulatory network provides an interface between redox and
            intermediary metabolism
  JOURNAL   Trends Biochem Sci 39 (4), 199-218 (2014)
   PUBMED   24647116
  REMARK    Review article
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Hirano,A., Yumimoto,K., Tsunematsu,R., Matsumoto,M., Oyama,M.,
            Kozuka-Hata,H., Nakagawa,T., Lanjakornsiripan,D., Nakayama,K.I. and
            Fukada,Y.
  TITLE     FBXL21 regulates oscillation of the circadian clock through
            ubiquitination and stabilization of cryptochromes
  JOURNAL   Cell 152 (5), 1106-1118 (2013)
   PUBMED   23452856
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Kim,J., Kim,J.H., Lee,S.H., Kim,D.H., Kang,H.Y., Bae,S.H., Pan,Z.Q.
            and Seo,Y.S.
  TITLE     The novel human DNA helicase hFBH1 is an F-box protein
  JOURNAL   J Biol Chem 277 (27), 24530-24537 (2002)
   PUBMED   11956208
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Kammen-Jolly,K., Scholtz,A.W., Kreczy,A., Gluckert,R., Thalmann,I.,
            Thalmann,R. and Schrott-Fischer,A.
  TITLE     OCP2 immunoreactivity in the human fetal cochlea at weeks 11, 17,
            20, and 28, and the human adult cochlea
  JOURNAL   Hear Res 167 (1-2), 102-109 (2002)
   PUBMED   12117534
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Heissmeyer,V., Krappmann,D., Hatada,E.N. and Scheidereit,C.
  TITLE     Shared pathways of IkappaB kinase-induced SCF(betaTrCP)-mediated
            ubiquitination and degradation for the NF-kappaB precursor p105 and
            IkappaBalpha
  JOURNAL   Mol Cell Biol 21 (4), 1024-1035 (2001)
   PUBMED   11158290
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Freed,E., Lacey,K.R., Huie,P., Lyapina,S.A., Deshaies,R.J.,
            Stearns,T. and Jackson,P.K.
  TITLE     Components of an SCF ubiquitin ligase localize to the centrosome
            and regulate the centrosome duplication cycle
  JOURNAL   Genes Dev 13 (17), 2242-2257 (1999)
   PUBMED   10485847
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC058152.1.
            
            On Nov 29, 2004 this sequence version replaced XP_213290.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058152.1, CF111133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..163
                     /product="S-phase kinase-associated protein 1"
                     /EC_number="3.1.1.3"
                     /note="organ of Corti protein 2; RNA polymerase II
                     elongation factor-like protein OCP2; cyclin
                     A/CDK2-associated p19; p19A; p19skp1;
                     cyclin-A/CDK2-associated protein p19; S-phase
                     kinase-associated protein 1A"
                     /calculated_mol_wt=18541
     Region          3..127
                     /region_name="BTB_POZ_SKP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ
                     (poxvirus and zinc finger) domain found in S-phase
                     kinase-associated protein 1 (SKP1) and similar proteins;
                     cd18322"
                     /db_xref="CDD:349631"
     Site            order(25..26,30,34,38,43..44,46,48..49,105,108..109,111)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349631"
     Region          63..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEC4.3)"
     Site            order(97,101,105,108,113,117,120..121,123..124,127)
                     /site_type="other"
                     /note="F-box protein binding site [polypeptide binding]"
                     /db_xref="CDD:349631"
     Region          104..163
                     /region_name="Interaction with the F-box domain of F-box
                     proteins. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PEC4.3)"
     Region          113..160
                     /region_name="Skp1"
                     /note="Skp1 family, dimerization domain; pfam01466"
                     /db_xref="CDD:460222"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PEC4.3)"
     CDS             1..163
                     /gene="Skp1"
                     /gene_synonym="Skp1a"
                     /coded_by="NM_001007608.2:84..575"
                     /db_xref="GeneID:287280"
                     /db_xref="RGD:1359648"
ORIGIN      
        1 mptiklqssd geifevdvei akqsvtiktm ledlgmddeg dddpvplpnv naailkkviq
       61 wcthhkddpp ppeddenkek rtddipvwdq eflkvdqgtl felilaanyl dikglldvtc
      121 ktvanmikgk tpeeirktfn ikndfteeee aqvrkenqwc eek
//
LOCUS       NP_001264189             260 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, slow skeletal muscle isoform 2 [Rattus norvegicus].
ACCESSION   NP_001264189
VERSION     NP_001264189.1
DBSOURCE    REFSEQ: accession NM_001277260.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Tsika,R.W., Schramm,C., Simmer,G., Fitzsimons,D.P., Moss,R.L. and
            Ji,J.
  TITLE     Overexpression of TEAD-1 in transgenic mouse striated muscles
            produces a slower skeletal muscle contractile phenotype
  JOURNAL   J Biol Chem 283 (52), 36154-36167 (2008)
   PUBMED   18978355
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Pinto,J.R., Parvatiyar,M.S., Jones,M.A., Liang,J. and Potter,J.D.
  TITLE     A troponin T mutation that causes infantile restrictive
            cardiomyopathy increases Ca2+ sensitivity of force development and
            impairs the inhibitory properties of troponin
  JOURNAL   J Biol Chem 283 (4), 2156-2166 (2008)
   PUBMED   18032382
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Kischel,P., Bastide,B., Muller,M., Dubail,F., Offredi,F., Jin,J.P.,
            Mounier,Y. and Martial,J.
  TITLE     Expression and functional properties of four slow skeletal troponin
            T isoforms in rat muscles
  JOURNAL   Am J Physiol Cell Physiol 289 (2), C437-C443 (2005)
   PUBMED   15788488
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Wang,X., Huang,Q.Q., Breckenridge,M.T., Chen,A., Crawford,T.O.,
            Morton,D.H. and Jin,J.P.
  TITLE     Cellular fate of truncated slow skeletal muscle troponin T produced
            by Glu180 nonsense mutation in amish nemaline myopathy
  JOURNAL   J Biol Chem 280 (14), 13241-13249 (2005)
   PUBMED   15665378
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Johnston,J.J., Kelley,R.I., Crawford,T.O., Morton,D.H.,
            Agarwala,R., Koch,T., Schaffer,A.A., Francomano,C.A. and
            Biesecker,L.G.
  TITLE     A novel nemaline myopathy in the Amish caused by a mutation in
            troponin T1
  JOURNAL   Am J Hum Genet 67 (4), 814-821 (2000)
   PUBMED   10952871
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Gahlmann,R., Troutt,A.B., Wade,R.P., Gunning,P. and Kedes,L.
  TITLE     Alternative splicing generates variants in important functional
            domains of human slow skeletal troponin T
  JOURNAL   J Biol Chem 262 (33), 16122-16126 (1987)
   PUBMED   2824479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and AY334080.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region, compared to variant 1. The encoded isoform
            (2) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..260
                     /product="troponin T, slow skeletal muscle isoform 2"
                     /note="troponin T, slow skeletal muscle; slow skeletal
                     muscle troponin T; troponin T1, skeletal, slow; troponin T
                     type 1 (skeletal, slow)"
                     /calculated_mol_wt=30955
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q7TNB2.3)"
     Region          67..203
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Region          107..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNB2.3)"
     Region          178..>236
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..260
                     /gene="Tnnt1"
                     /gene_synonym="Fang2; sTnT; tnTs"
                     /coded_by="NM_001277260.1:57..839"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171409"
                     /db_xref="RGD:621852"
ORIGIN      
        1 msdteeqeye eeqaedeeav eeeapeepep vaereerpkp srpvvpplip pkipegervd
       61 fddihrkrme kdllelqtli dvhfeqrkke eeelialkdr ierrraerae qqrfrteker
      121 erqaklaeek mrkeeeeakk raeddakkkk vlsnmgahfg gylvkaeqkr gkrqtgremk
      181 lrilserkkp lnidymgedq lrekaqelse wihqlesekf dlmeklkqqk yeinvlynri
      241 shaqkfrkga gkgrvggrwk
//
LOCUS       NP_058795                424 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 8 [Rattus
            norvegicus].
ACCESSION   NP_058795
VERSION     NP_058795.3
DBSOURCE    REFSEQ: accession NM_017099.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Brennan,S., Chen,S., Makwana,S., Esposito,S., McGuinness,L.R.,
            Alnaimi,A.I.M., Sims,M.W., Patel,M., Aziz,Q., Ojake,L.,
            Roberts,J.A., Sharma,P., Lodwick,D., Tinker,A., Barrett-Jolley,R.,
            Dart,C. and Rainbow,R.D.
  TITLE     Identification and characterisation of functional Kir6.1-containing
            ATP-sensitive potassium channels in the cardiac ventricular
            sarcolemmal membrane
  JOURNAL   Br J Pharmacol 181 (18), 3380-3400 (2024)
   PUBMED   38763521
  REMARK    GeneRIF: Identification and characterisation of functional
            Kir6.1-containing ATP-sensitive potassium channels in the cardiac
            ventricular sarcolemmal membrane.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Li,H., Chen,D., Sun,W., Chen,J., Luo,C., Xu,H., Ma,J.H. and Tang,S.
  TITLE     KATP Opener Attenuates Diabetic-Induced Muller Gliosis and
            Inflammation by Modulating Kir6.1 in Microglia
  JOURNAL   Invest Ophthalmol Vis Sci 62 (2), 3 (2021)
   PUBMED   33523201
  REMARK    GeneRIF: KATP Opener Attenuates Diabetic-Induced Muller Gliosis and
            Inflammation by Modulating Kir6.1 in Microglia.
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Peng,K., Hu,J., Xiao,J., Dan,G., Yang,L., Ye,F., Zou,Z., Cao,J. and
            Sai,Y.
  TITLE     Mitochondrial ATP-sensitive potassium channel regulates
            mitochondrial dynamics to participate in neurodegeneration of
            Parkinson's disease
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1864 (4 Pt A), 1086-1103 (2018)
   PUBMED   29353068
  REMARK    GeneRIF: it can be concluded that mitoKATP channels regulate
            mitochondrial dynamics to participate in rotenone-induced
            Parkinson's disease mainly attributes to the pore subunits of
            Kir6.1.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Cooper,P.E., McClenaghan,C., Chen,X., Stary-Weinzinger,A. and
            Nichols,C.G.
  TITLE     Conserved functional consequences of disease-associated mutations
            in the slide helix of Kir6.1 and Kir6.2 subunits of the
            ATP-sensitive potassium channel
  JOURNAL   J Biol Chem 292 (42), 17387-17398 (2017)
   PUBMED   28842488
  REMARK    GeneRIF: both Kir6.1(V65M) and Kir6.2(V64M) mutations essentially
            abolish high-affinity sensitivity to the KATP blocker glibenclamide
            in both intact cells and excised patches. This raises the
            possibility that, at least for some CS mutations, sulfonylurea
            therapy may not prove to be successful and highlights the need for
            detailed pharmacogenomic analyses of CS mutations.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Liu,X., Duan,P., Hu,X., Li,R. and Zhu,Q.
  TITLE     Altered KATP Channel Subunits Expression and Vascular Reactivity in
            Spontaneously Hypertensive Rats With Age
  JOURNAL   J Cardiovasc Pharmacol 68 (2), 143-149 (2016)
   PUBMED   27035370
  REMARK    GeneRIF: In vascular smooth muscle KATP channel subunits Kir6.1 and
            SUR2B contribute to modify the functionality of this channel in
            hypertension with age.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Vanoye,C.G., MacGregor,G.G., Dong,K., Tang,L., Buschmann,A.S.,
            Hall,A.E., Lu,M., Giebisch,G. and Hebert,S.C.
  TITLE     The carboxyl termini of K(ATP) channels bind nucleotides
  JOURNAL   J Biol Chem 277 (26), 23260-23270 (2002)
   PUBMED   11956191
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Light,P.E., Kanji,H.D., Fox,J.E. and French,R.J.
  TITLE     Distinct myoprotective roles of cardiac sarcolemmal and
            mitochondrial KATP channels during metabolic inhibition and
            recovery
  JOURNAL   FASEB J 15 (14), 2586-2594 (2001)
   PUBMED   11726534
  REMARK    GeneRIF: Data suggest that sarc and mitoKATP channel populations
            play distinct protective roles, triggered by PKC and/or adenosine,
            during chemically induced hypoxia/reoxygenation.
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Sgard,F., Faure,C., Drieu la Rochelle,C., Graham,D., O'Connor,S.E.,
            Janiak,P. and Besnard,F.
  TITLE     Regulation of ATP-sensitive potassium channel mRNA expression in
            rat kidney following ischemic injury
  JOURNAL   Biochem Biophys Res Commun 269 (2), 618-622 (2000)
   PUBMED   10708603
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Akao,M., Otani,H., Horie,M., Takano,M., Kuniyasu,A., Nakayama,H.,
            Kouchi,I., Murakami,T. and Sasayama,S.
  TITLE     Myocardial ischemia induces differential regulation of KATP channel
            gene expression in rat hearts
  JOURNAL   J Clin Invest 100 (12), 3053-3059 (1997)
   PUBMED   9399952
  REMARK    Erratum:[J Clin Invest 1998 Feb 15;101(4):915]
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Inagaki,N., Tsuura,Y., Namba,N., Masuda,K., Gonoi,T., Horie,M.,
            Seino,Y., Mizuta,M. and Seino,S.
  TITLE     Cloning and functional characterization of a novel ATP-sensitive
            potassium channel ubiquitously expressed in rat tissues, including
            pancreatic islets, pituitary, skeletal muscle, and heart
  JOURNAL   J Biol Chem 270 (11), 5691-5694 (1995)
   PUBMED   7890693
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D42145.1.
            
            On Jun 10, 2007 this sequence version replaced NP_058795.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D42145.1, BC078863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093047, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..424
                     /product="ATP-sensitive inward rectifier potassium channel
                     8"
                     /note="inwardly rectifier K(+) channel Kir6.1; potassium
                     channel, inwardly rectifying subfamily J member 8; inward
                     rectifier K(+) channel Kir6.1; Inwardly rectifying
                     potassium channel gene, subfamily J-8 (ATP sensitive);
                     potassium voltage-gated channel subfamily J member 8"
                     /calculated_mol_wt=47832
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97794; propagated from
                     UniProtKB/Swiss-Prot (Q63664.1)"
     Region          37..184
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            70..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63664.1)"
     Region          140..145
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63664.1)"
     Site            155..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63664.1)"
     Site            170
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q63664.1)"
     Region          191..363
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Region          374..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63664.1)"
     CDS             1..424
                     /gene="Kcnj8"
                     /gene_synonym="Kir6.1; uKATP-1; UKATP1"
                     /coded_by="NM_017099.4:177..1451"
                     /db_xref="GeneID:25472"
                     /db_xref="RGD:2960"
ORIGIN      
        1 mlarksiipe eyvlariaae nlrkprirdr lpkarfiaks gacnlahkni reqgrflqdi
       61 fttlvdlkwr htlviftmsf lcswllfaim wwlvafahgd iyaymekgit eksglesavc
      121 vtnvrsftsa flfsievqvt igfggrmmte ecplaitvli lqnivgliin avmlgcifmk
      181 taqahrraet lifsrhavia vrngklcfmf rvgdlrksmi isasvriqvv kktttpegev
      241 vpihqqdipv dnpiesnnif lvapliichv idkrsplydi satdlvnqdl evivilegvv
      301 ettgittqar tsyiaeeiqw ghrfvsivte eegvysvdys kfgntvrvaa prcsarelde
      361 kpsiliqtlq kselshqnsl rkrnsmrrnn smrrsnsirr nnsslmvpkv qfmtpegnqc
      421 pses
//
LOCUS       NP_620809                855 aa            linear   ROD 27-APR-2025
DEFINITION  pre-mRNA-splicing factor SYF1 [Rattus norvegicus].
ACCESSION   NP_620809
VERSION     NP_620809.1
DBSOURCE    REFSEQ: accession NM_139109.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Chanarat,S. and Strasser,K.
  TITLE     Splicing and beyond: the many faces of the Prp19 complex
  JOURNAL   Biochim Biophys Acta 1833 (10), 2126-2134 (2013)
   PUBMED   23742842
  REMARK    Review article
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Kamileri,I., Karakasilioti,I. and Garinis,G.A.
  TITLE     Nucleotide excision repair: new tricks with old bricks
  JOURNAL   Trends Genet 28 (11), 566-573 (2012)
   PUBMED   22824526
  REMARK    Review article
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Yonemasu,R., Minami,M., Nakatsu,Y., Takeuchi,M., Kuraoka,I.,
            Matsuda,Y., Higashi,Y., Kondoh,H. and Tanaka,K.
  TITLE     Disruption of mouse XAB2 gene involved in pre-mRNA splicing,
            transcription and transcription-coupled DNA repair results in
            preimplantation lethality
  JOURNAL   DNA Repair (Amst) 4 (4), 479-491 (2005)
   PUBMED   15725628
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Amada,N., Tezuka,T., Mayeda,A., Araki,K., Takei,N., Todokoro,K. and
            Nawa,H.
  TITLE     A novel rat orthologue and homologue for the Drosophila crooked
            neck gene in neural stem cells and their immediate descendants
  JOURNAL   J Biochem 133 (5), 615-623 (2003)
   PUBMED   12801913
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Nakatsu,Y., Asahina,H., Citterio,E., Rademakers,S., Vermeulen,W.,
            Kamiuchi,S., Yeo,J.P., Khaw,M.C., Saijo,M., Kodo,N., Matsuda,T.,
            Hoeijmakers,J.H. and Tanaka,K.
  TITLE     XAB2, a novel tetratricopeptide repeat protein involved in
            transcription-coupled DNA repair and transcription
  JOURNAL   J Biol Chem 275 (45), 34931-34937 (2000)
   PUBMED   10944529
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF277899.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF277899.1, BC081723.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..855
                     /product="pre-mRNA-splicing factor SYF1"
                     /note="adapter protein ATH-55"
                     /calculated_mol_wt=99867
     Region          15..47
                     /region_name="HAT 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          48..80
                     /region_name="HAT 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          55..>187
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          90..122
                     /region_name="HAT 3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          124..158
                     /region_name="HAT 4. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          160..192
                     /region_name="HAT 5. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          198..230
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          235..268
                     /region_name="HAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          259..584
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          270..305
                     /region_name="HAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          369..407
                     /region_name="HAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          389..424
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            420
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9HCS7; propagated from
                     UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          433..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          466..513
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          498..530
                     /region_name="HAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          518..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          532..566
                     /region_name="HAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          571..605
                     /region_name="HAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          643..677
                     /region_name="HAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          679..713
                     /region_name="HAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Region          808..855
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PK0.1)"
     Site            851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HCS7; propagated from
                     UniProtKB/Swiss-Prot (Q99PK0.1)"
     CDS             1..855
                     /gene="Xab2"
                     /gene_synonym="Ath55"
                     /coded_by="NM_139109.2:47..2614"
                     /db_xref="GeneID:245976"
                     /db_xref="RGD:621217"
ORIGIN      
        1 mvvmarvprp erpdlvfeee dlpyeeeimr nqfsvkcwlr yiefkqgapk prlnqlyera
       61 lkllpcsykl wyrylkarra qvkhrcvtdp ayedvnnche rafvfmhkmp rlwldycqfl
      121 mdqgrvthtr rtfdralral pitqhsriwp lylrflrshp lpetavrgyr rflklspesa
      181 eeyieylkss drldeaaqrl atvvnderfv skagksnyql whelcdlisq npdkvqslnv
      241 daiirggltr ftdqlgklwc sladyyirsg hfekardvye eairtvmtvr dftqvfdsya
      301 qfeesmiaak metaselgre eeddvdlelr larfeqlisr rplllnsvll rqnphhvhew
      361 hkrvalhqgr preiintyte avqtvdpfka tgkphtlwva fakfyedngq lddarvilek
      421 atkvnfkqvd dlasvwcqcg elelrhenyd ealkllrkat alparraeyf dgsepvqnrv
      481 ykslkvwsml adleeslgtf qstkavydri ldlriatpqi vinyamflee hkyfeesfka
      541 yergislfkw pnvsdiwsty ltkfisrygg rklerardlf eqaldgcppk yaktlyllya
      601 qleeewglar hamavydrat ravepaqqyd mfniyikraa eiygvthtrg iyqkaievls
      661 deharemclr fadmecklge idraraiysf csqicdprtt gafwqtwkdf evrhgnedti
      721 remlrirrsv qatyntqvnf masqmlkvsg satgtvsdla pgqsgmddmk lleqraeqla
      781 aeaerdqppr aqskiffvrs dasreelael aqqanpeeiq lgedededem dlepnevrle
      841 qqsvpaavfg slked
//
LOCUS       NP_598288                 89 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim9
            [Rattus norvegicus].
ACCESSION   NP_598288
VERSION     NP_598288.1
DBSOURCE    REFSEQ: accession NM_133604.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Webb,C.T., Gorman,M.A., Lazarou,M., Ryan,M.T. and Gulbis,J.M.
  TITLE     Crystal structure of the mitochondrial chaperone TIM9.10 reveals a
            six-bladed alpha-propeller
  JOURNAL   Mol Cell 21 (1), 123-133 (2006)
   PUBMED   16387659
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Muhlenbein,N., Hofmann,S., Rothbauer,U. and Bauer,M.F.
  TITLE     Organization and function of the small Tim complexes acting along
            the import pathway of metabolite carriers into mammalian
            mitochondria
  JOURNAL   J Biol Chem 279 (14), 13540-13546 (2004)
   PUBMED   14726512
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Paschen,S.A., Rothbauer,U., Kaldi,K., Bauer,M.F., Neupert,W. and
            Brunner,M.
  TITLE     The role of the TIM8-13 complex in the import of Tim23 into
            mitochondria
  JOURNAL   EMBO J 19 (23), 6392-6400 (2000)
   PUBMED   11101512
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1 and CB775939.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228524.1, DV215568.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840111,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..89
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim9"
                     /note="translocase of inner mitochondrial membrane 9
                     homolog"
                     /calculated_mol_wt=10245
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5J7; propagated from
                     UniProtKB/Swiss-Prot (Q9WV97.3)"
     Region          10..69
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          28..52
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV97.3)"
     CDS             1..89
                     /gene="Timm9"
                     /gene_synonym="Tim9; Tim9a; Timm9a"
                     /coded_by="NM_133604.1:247..516"
                     /db_xref="GeneID:171139"
                     /db_xref="RGD:621656"
ORIGIN      
        1 maaqipesdq ikqfkeflgt ynkltetcfl dcvkdfttre vkpeevtcse hclqkylkmt
       61 qrismrfqey hiqqnealaa kagllgqpr
//
LOCUS       NP_001257860             449 aa            linear   ROD 27-APR-2025
DEFINITION  hepatocyte nuclear factor 4-alpha isoform 2 [Rattus norvegicus].
ACCESSION   NP_001257860
VERSION     NP_001257860.1
DBSOURCE    REFSEQ: accession NM_001270931.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Melis,M., Marino,R., Tian,J., Johnson,C., Sethi,R., Oertel,M.,
            Fox,I.J. and Locker,J.
  TITLE     Mechanism and Effect of HNF4alpha Decrease in a Rat Model of
            Cirrhosis and Liver Failure
  JOURNAL   Cell Mol Gastroenterol Hepatol 17 (3), 453-479 (2024)
   PUBMED   37993018
  REMARK    GeneRIF: Mechanism and Effect of HNF4alpha Decrease in a Rat Model
            of Cirrhosis and Liver Failure.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhan,H., Zhang,Q., Zhang,C., Cheng,J., Yang,Y., Liu,C., Li,S.,
            Wang,C., Yang,J., Ge,H., Zhou,D., Li,B., Wei,H. and Hu,C.
  TITLE     Targeted Activation of HNF4alpha by AMPK Inhibits Apoptosis and
            Ameliorates Neurological Injury Caused by Cardiac Arrest in Rats
  JOURNAL   Neurochem Res 48 (10), 3129-3145 (2023)
   PUBMED   37338793
  REMARK    GeneRIF: Targeted Activation of HNF4alpha by AMPK Inhibits
            Apoptosis and Ameliorates Neurological Injury Caused by Cardiac
            Arrest in Rats.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Fan,J.Y., Dama,G., Liu,Y.L., Guo,W.Y. and Lin,J.T.
  TITLE     [Combinational Overexpression of Foxa3 and Hnf4alpha Enhance the
            Proliferation and Prolong the Functional Maintenance of Primary
            Hepatocytes]
  JOURNAL   Mol Biol (Mosk) 57 (4), 668-670 (2023)
   PUBMED   37528786
  REMARK    GeneRIF: [Combinational Overexpression of Foxa3 and Hnf4alpha
            Enhance the Proliferation and Prolong the Functional Maintenance of
            Primary Hepatocytes].
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Hu,C., Jing,R., Wen,C., Qi,T., Bai,X., Wang,Y., Shao,Y. and Pei,C.
  TITLE     HNF4A Negatively Regulated Posterior Capsular Opacification via
            Transcriptional Inhibition of MMP2
  JOURNAL   Curr Eye Res 48 (7), 627-638 (2023)
   PUBMED   36988559
  REMARK    GeneRIF: HNF4A Negatively Regulated Posterior Capsular
            Opacification via Transcriptional Inhibition of MMP2.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Zheng,X., Wang,G., Yuan,J., Li,N., Yan,B., Yan,J. and Sheng,Y.
  TITLE     hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion Injury Via
            Targeting HNF4alpha
  JOURNAL   Turk J Gastroenterol 33 (7), 596-605 (2022)
   PUBMED   35879917
  REMARK    GeneRIF: hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion
            Injury Via Targeting HNF4alpha.
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Ginsburg,G.S., Ozer,J. and Karathanasis,S.K.
  TITLE     Intestinal apolipoprotein AI gene transcription is regulated by
            multiple distinct DNA elements and is synergistically activated by
            the orphan nuclear receptor, hepatocyte nuclear factor 4
  JOURNAL   J Clin Invest 96 (1), 528-538 (1995)
   PUBMED   7615825
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Chen,W.S., Manova,K., Weinstein,D.C., Duncan,S.A., Plump,A.S.,
            Prezioso,V.R., Bachvarova,R.F. and Darnell,J.E. Jr.
  TITLE     Disruption of the HNF-4 gene, expressed in visceral endoderm, leads
            to cell death in embryonic ectoderm and impaired gastrulation of
            mouse embryos
  JOURNAL   Genes Dev 8 (20), 2466-2477 (1994)
   PUBMED   7958910
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Ang,S.L., Wierda,A., Wong,D., Stevens,K.A., Cascio,S., Rossant,J.
            and Zaret,K.S.
  TITLE     The formation and maintenance of the definitive endoderm lineage in
            the mouse: involvement of HNF3/forkhead proteins
  JOURNAL   Development 119 (4), 1301-1315 (1993)
   PUBMED   8306889
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Hata,S., Tsukamoto,T. and Osumi,T.
  TITLE     A novel isoform of rat hepatocyte nuclear factor 4 (HNF-4)
  JOURNAL   Biochim Biophys Acta 1131 (2), 211-213 (1992)
   PUBMED   1610903
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Sladek,F.M., Zhong,W.M., Lai,E. and Darnell,J.E. Jr.
  TITLE     Liver-enriched transcription factor HNF-4 is a novel member of the
            steroid hormone receptor superfamily
  JOURNAL   Genes Dev 4 (12B), 2353-2365 (1990)
   PUBMED   2279702
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FJ608817.1, EF193390.1, JAXUCZ010000003.1 and FQ095211.1.
            
            Transcript Variant: This variant (2) is the longest transcript. It
            differs in the 5' UTR and 5' coding region, compared to variant 1.
            The resulting isoform (2, also known as HNF4alpha11) is shorter and
            has a distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ608817.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="NEDH"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..449
                     /product="hepatocyte nuclear factor 4-alpha isoform 2"
                     /note="alpha transcription factor 4; HNF-4-alpha;
                     transcription factor 14; transcription factor HNF-4;
                     nuclear receptor subfamily 2 group A member 1; TCF-14;
                     hepatic nuclear factor 4, alpha"
                     /calculated_mol_wt=49828
     Region          35..110
                     /region_name="NR_DBD_HNF4A"
                     /note="DNA-binding domain of heptocyte nuclear factor 4
                     (HNF4) is composed of two C4-type zinc fingers; cd06960"
                     /db_xref="CDD:143518"
     Site            order(35,38,52,55,71,77,87,90)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143518"
     Site            order(41,45..47,53..54,56,58,60..61,64,84..85,88,91,
                     104..106,108)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143518"
     Site            order(72,85..86,88)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:143518"
     Region          126..348
                     /region_name="NR_LBD_HNF4_like"
                     /note="The ligand binding domain of heptocyte nuclear
                     factor 4, which is explosively expanded in nematodes;
                     cd06931"
                     /db_xref="CDD:132729"
     Site            order(159,165,169,203,207,210,220..221,239,329..330,333)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132729"
     Site            order(174,178,188..189,191..192,195..196,343..344,
                     347..348)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132729"
     Site            order(246,267,273,287..288,291..292,295..296,306..307,
                     309..311,313..314,316..318,320..321,324)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132729"
     CDS             1..449
                     /gene="Hnf4a"
                     /gene_synonym="Hnf4; Hnf4alpha"
                     /coded_by="NM_001270931.1:256..1605"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25735"
                     /db_xref="RGD:2810"
ORIGIN      
        1 msdrgqgflq dppdtspseg anlnssnslg vsalcaicgd ratgkhygas scdgckgffr
       61 rsvrknhmys crfsrqcvvd kdkrnqcryc rlkkcfragm kkeavqnerd ristrrssye
      121 dsslpsinal lqaevlsqqi tspisgingd irakrianit dvcesmkeql lvlvewakyi
      181 pafcellldd qvallrahag ehlllgatkr smvfkdvlll gndyivprhc pelaemsrvs
      241 irildelvlp fqelqiddne yaclkaiiff dpdakglsdp gkikrlrsqv qvsledyind
      301 rqydsrgrfg elllllptlq sitwqmieqi qfiklfgmak idnllqemll ggsasdapha
      361 hhplhphlmq ehmgtnviva ntmpshlsng qmcewprprg qaatpetpqp sppsgsgses
      421 ykllpgaitt ivkppsaipq ptitkqeai
//
LOCUS       NP_570090                317 aa            linear   ROD 27-APR-2025
DEFINITION  small ribosomal subunit protein RACK1 [Rattus norvegicus].
ACCESSION   NP_570090
VERSION     NP_570090.2
DBSOURCE    REFSEQ: accession NM_130734.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Zhao,L., Chen,Y., Li,H., Ding,X. and Li,J.
  TITLE     Deciphering the neuroprotective mechanisms of RACK1 in cerebral
            ischemia-reperfusion injury: Pioneering insights into mitochondrial
            autophagy and the PINK1/Parkin axis
  JOURNAL   CNS Neurosci Ther 30 (8), e14836 (2024)
   PUBMED   39097918
  REMARK    GeneRIF: Deciphering the neuroprotective mechanisms of RACK1 in
            cerebral ischemia-reperfusion injury: Pioneering insights into
            mitochondrial autophagy and the PINK1/Parkin axis.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Wang,C.Y., Li,M.Y., Li,S.Y., Wei,X.G., Dong,N.X., Liu,S.T.,
            Yuan,Z.W., Li,B., Pierro,A., Tang,X.B. and Bai,Y.Z.
  TITLE     Rack1-mediated ferroptosis affects hindgut development in rats with
            anorectal malformations: Spatial transcriptome insights
  JOURNAL   Cell Prolif 57 (7), e13618 (2024)
   PUBMED   38523594
  REMARK    GeneRIF: Rack1-mediated ferroptosis affects hindgut development in
            rats with anorectal malformations: Spatial transcriptome insights.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Ni,H., Kan,X., Rui,Q., Zhang,Y., Zhai,W., Zhang,B. and Yu,Z.
  TITLE     RACK1 promotes autophagy via the PERK signaling pathway to protect
            against traumatic brain injury in rats
  JOURNAL   CNS Neurosci Ther 30 (3), e14691 (2024)
   PUBMED   38532543
  REMARK    GeneRIF: RACK1 promotes autophagy via the PERK signaling pathway to
            protect against traumatic brain injury in rats.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Sun,C., Peng,S., Lv,Z., Guo,T. and Zhang,L.
  TITLE     Research of STEAP3 interaction with Rab7A and RACK1 to modulate the
            MAPK and JAK/STAT signaling in Osteoarthritis
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111034 (2023)
   PUBMED   37820423
  REMARK    GeneRIF: Research of STEAP3 interaction with Rab7A and RACK1 to
            modulate the MAPK and JAK/STAT signaling in Osteoarthritis.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   do Canto,A.M., Vieira,A.S., H B Matos,A., Carvalho,B.S.,
            Henning,B., Norwood,B.A., Bauer,S., Rosenow,F., Gilioli,R.,
            Cendes,F. and Lopes-Cendes,I.
  TITLE     Laser microdissection-based microproteomics of the hippocampus of a
            rat epilepsy model reveals regional differences in protein
            abundances
  JOURNAL   Sci Rep 10 (1), 4412 (2020)
   PUBMED   32157145
  REMARK    GeneRIF: Laser microdissection-based microproteomics of the
            hippocampus of a rat epilepsy model reveals regional differences in
            protein abundances.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Chang,B.Y., Chiang,M. and Cartwright,C.A.
  TITLE     The interaction of Src and RACK1 is enhanced by activation of
            protein kinase C and tyrosine phosphorylation of RACK1
  JOURNAL   J Biol Chem 276 (23), 20346-20356 (2001)
   PUBMED   11279199
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Mourton,T., Hellberg,C.B., Burden-Gulley,S.M., Hinman,J., Rhee,A.
            and Brady-Kalnay,S.M.
  TITLE     The PTPmu protein-tyrosine phosphatase binds and recruits the
            scaffolding protein RACK1 to cell-cell contacts
  JOURNAL   J Biol Chem 276 (18), 14896-14901 (2001)
   PUBMED   11278757
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Baumann,M., Gires,O., Kolch,W., Mischak,H., Zeidler,R., Pich,D. and
            Hammerschmidt,W.
  TITLE     The PKC targeting protein RACK1 interacts with the Epstein-Barr
            virus activator protein BZLF1
  JOURNAL   Eur J Biochem 267 (12), 3891-3901 (2000)
   PUBMED   10849009
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Chang,B.Y., Conroy,K.B., Machleder,E.M. and Cartwright,C.A.
  TITLE     RACK1, a receptor for activated C kinase and a homolog of the beta
            subunit of G proteins, inhibits activity of src tyrosine kinases
            and growth of NIH 3T3 cells
  JOURNAL   Mol Cell Biol 18 (6), 3245-3256 (1998)
   PUBMED   9584165
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Ron,D., Chen,C.H., Caldwell,J., Jamieson,L., Orr,E. and
            Mochly-Rosen,D.
  TITLE     Cloning of an intracellular receptor for protein kinase C: a
            homolog of the beta subunit of G proteins
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 839-843 (1994)
   PUBMED   8302854
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Feb 28;92(5):2016]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Sep 20, 2012 this sequence version replaced NP_570090.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219900.1, FQ229633.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..317
                     /product="small ribosomal subunit protein RACK1"
                     /note="guanine nucleotide binding protein (G protein),
                     beta polypeptide 2-like 1; guanine nucleotide-binding
                     protein subunit beta-2-like 1; receptor of activated
                     protein kinase C 1; guanine nucleotide binding protein,
                     beta polypeptide 2-like 1; guanine nucleotide binding
                     protein (G protein) beta polypeptide 2-like 1; protein
                     kinase C receptor; receptor for activated protein kinase
                     C; receptor of activated protein C kinase 1"
                     /calculated_mol_wt=34946
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Guanine nucleotide-binding
                     protein subunit beta-2-like 1, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          7..311
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          13..44
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Site            order(14,33,37,43..44,61..62,80,84,90..91,103..104,121,
                     126,132..133,147,166,171,177..178,190..191,209,213,
                     219..220,232,249,259..260,281..282,300,304,310..311)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          18..61
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          61..91
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          67..103
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          103..133
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          108..144
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            130
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          146..178
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          152..189
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P68040; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          190..220
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          195..231
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          231..260
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          236..279
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63244; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     Region          281..311
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P63245.3)"
     Region          286..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P68040; propagated from
                     UniProtKB/Swiss-Prot (P63245.3)"
     CDS             1..317
                     /gene="Rack1"
                     /gene_synonym="Gnb2l1"
                     /coded_by="NM_130734.2:134..1087"
                     /db_xref="GeneID:83427"
                     /db_xref="RGD:69229"
ORIGIN      
        1 mteqmtlrgt lkghngwvtq iattpqfpdm ilsasrdkti imwkltrdet nygipqralr
       61 ghshfvsdvv issdgqfals gswdgtlrlw dlttgtttrr fvghtkdvls vafssdnrqi
      121 vsgsrdktik lwntlgvcky tvqdeshsew vscvrfspns snpiivscgw dklvkvwnla
      181 ncklktnhig htgylntvtv spdgslcasg gkdgqamlwd lnegkhlytl dggdiinalc
      241 fspnrywlca atgpsikiwd legkiivdel kqevistssk aeppqctsla wsadgqtlfa
      301 gytdnlvrvw qvtigtr
//
LOCUS       NP_001263649            1998 aa            linear   ROD 27-APR-2025
DEFINITION  otoferlin [Rattus norvegicus].
ACCESSION   NP_001263649 XP_001062291 XP_001065408 XP_002726762 XP_002729659
            XP_003750166 XP_003754202
VERSION     NP_001263649.1
DBSOURCE    REFSEQ: accession NM_001276720.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1998)
  AUTHORS   Vogl,C., Panou,I., Yamanbaeva,G., Wichmann,C., Mangosing,S.J.,
            Vilardi,F., Indzhykulian,A.A., Pangrsic,T., Santarelli,R.,
            Rodriguez-Ballesteros,M., Weber,T., Jung,S., Cardenas,E., Wu,X.,
            Wojcik,S.M., Kwan,K.Y., Del Castillo,I., Schwappach,B.,
            Strenzke,N., Corey,D.P., Lin,S.Y. and Moser,T.
  TITLE     Tryptophan-rich basic protein (WRB) mediates insertion of the
            tail-anchored protein otoferlin and is required for hair cell
            exocytosis and hearing
  JOURNAL   EMBO J 35 (23), 2536-2552 (2016)
   PUBMED   27458190
REFERENCE   2  (residues 1 to 1998)
  AUTHORS   Wu,W., Rahman,M.N., Guo,J., Roy,N., Xue,L., Cahill,C.M., Zhang,S.
            and Jia,Z.
  TITLE     Function coupling of otoferlin with GAD65 acts to modulate
            GABAergic activity
  JOURNAL   J Mol Cell Biol 7 (2), 168-179 (2015)
   PUBMED   25701657
  REMARK    GeneRIF: otoferlin, through GAD65, modulates GABAergic activity.
REFERENCE   3  (residues 1 to 1998)
  AUTHORS   Vogl,C., Cooper,B.H., Neef,J., Wojcik,S.M., Reim,K., Reisinger,E.,
            Brose,N., Rhee,J.S., Moser,T. and Wichmann,C.
  TITLE     Unconventional molecular regulation of synaptic vesicle
            replenishment in cochlear inner hair cells
  JOURNAL   J Cell Sci 128 (4), 638-644 (2015)
   PUBMED   25609709
REFERENCE   4  (residues 1 to 1998)
  AUTHORS   Ramakrishnan,N.A., Drescher,M.J., Morley,B.J., Kelley,P.M. and
            Drescher,D.G.
  TITLE     Calcium regulates molecular interactions of otoferlin with soluble
            NSF attachment protein receptor (SNARE) proteins required for hair
            cell exocytosis
  JOURNAL   J Biol Chem 289 (13), 8750-8766 (2014)
   PUBMED   24478316
  REMARK    GeneRIF: a direct role for otoferlin in exocytosis and modulation
            of calcium-dependent membrane fusion
REFERENCE   5  (residues 1 to 1998)
  AUTHORS   Duncker,S.V., Franz,C., Kuhn,S., Schulte,U., Campanelli,D.,
            Brandt,N., Hirt,B., Fakler,B., Blin,N., Ruth,P., Engel,J.,
            Marcotti,W., Zimmermann,U. and Knipper,M.
  TITLE     Otoferlin couples to clathrin-mediated endocytosis in mature
            cochlear inner hair cells
  JOURNAL   J Neurosci 33 (22), 9508-9519 (2013)
   PUBMED   23719817
  REMARK    GeneRIF: otoferlin-AP-2 interaction drives Ca(2+)- and
            stimulus-dependent compensating clathrin-mediated endocytosis in
            mature inner hair
REFERENCE   6  (residues 1 to 1998)
  AUTHORS   Tekin,M., Akcayoz,D. and Incesulu,A.
  TITLE     A novel missense mutation in a C2 domain of OTOF results in
            autosomal recessive auditory neuropathy
  JOURNAL   Am J Med Genet A 138 (1), 6-10 (2005)
   PUBMED   16097006
REFERENCE   7  (residues 1 to 1998)
  AUTHORS   Rodriguez-Ballesteros,M., del Castillo,F.J., Martin,Y.,
            Moreno-Pelayo,M.A., Morera,C., Prieto,F., Marco,J., Morant,A.,
            Gallo-Teran,J., Morales-Angulo,C., Navas,C., Trinidad,G.,
            Tapia,M.C., Moreno,F. and del Castillo,I.
  TITLE     Auditory neuropathy in patients carrying mutations in the otoferlin
            gene (OTOF)
  JOURNAL   Hum Mutat 22 (6), 451-456 (2003)
   PUBMED   14635104
REFERENCE   8  (residues 1 to 1998)
  AUTHORS   Migliosi,V., Modamio-Hoybjor,S., Moreno-Pelayo,M.A.,
            Rodriguez-Ballesteros,M., Villamar,M., Telleria,D., Menendez,I.,
            Moreno,F. and Del Castillo,I.
  TITLE     Q829X, a novel mutation in the gene encoding otoferlin (OTOF), is
            frequently found in Spanish patients with prelingual non-syndromic
            hearing loss
  JOURNAL   J Med Genet 39 (7), 502-506 (2002)
   PUBMED   12114484
REFERENCE   9  (residues 1 to 1998)
  AUTHORS   Yasunaga,S., Grati,M., Chardenoux,S., Smith,T.N., Friedman,T.B.,
            Lalwani,A.K., Wilcox,E.R. and Petit,C.
  TITLE     OTOF encodes multiple long and short isoforms: genetic evidence
            that the long ones underlie recessive deafness DFNB9
  JOURNAL   Am J Hum Genet 67 (3), 591-600 (2000)
   PUBMED   10903124
REFERENCE   10 (residues 1 to 1998)
  AUTHORS   Yasunaga,S., Grati,M., Cohen-Salmon,M., El-Amraoui,A., Mustapha,M.,
            Salem,N., El-Zir,E., Loiselet,J. and Petit,C.
  TITLE     A mutation in OTOF, encoding otoferlin, a FER-1-like protein,
            causes DFNB9, a nonsyndromic form of deafness
  JOURNAL   Nat Genet 21 (4), 363-369 (1999)
   PUBMED   10192385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Mar 1, 2013 this sequence version replaced
            XP_002729659.1, XP_001062291.1, XP_003750166.1, XP_001065408.1,
            XP_002726762.1, XP_003754202.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1998
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..1998
                     /product="otoferlin"
                     /note="fer-1-like protein 2"
                     /calculated_mol_wt=226975
     Region          3..130
                     /region_name="C2A_Ferlin"
                     /note="C2 domain first repeat in Ferlin; cd08373"
                     /db_xref="CDD:176019"
     Region          251..362
                     /region_name="C2B_Ferlin"
                     /note="C2 domain second repeat in Ferlin; cd04011"
                     /db_xref="CDD:175978"
     Region          360..410
                     /region_name="FerI"
                     /note="FerI (NUC094) domain; pfam08151"
                     /db_xref="CDD:462377"
     Region          418..567
                     /region_name="C2C_Ferlin"
                     /note="C2 domain third repeat in Ferlin; cd04018"
                     /db_xref="CDD:175985"
     Site            order(447,453,501,503,514,516)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175985"
     Region          842..917
                     /region_name="FerB"
                     /note="FerB (NUC096) domain; pfam08150"
                     /db_xref="CDD:462376"
     Region          960..1097
                     /region_name="C2D_Ferlin"
                     /note="C2 domain fourth repeat in Ferlin; cd04017"
                     /db_xref="CDD:175984"
     Site            order(976,982,1038,1040)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175984"
     Region          1494..1617
                     /region_name="C2E_Ferlin"
                     /note="C2 domain fifth repeat in Ferlin; cd04037"
                     /db_xref="CDD:176002"
     Site            order(1509,1515,1564,1566,1571)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176002"
     Region          1734..1867
                     /region_name="C2F_Ferlin"
                     /note="C2 domain sixth repeat in Ferlin; cd08374"
                     /db_xref="CDD:176020"
     Region          1877..>1965
                     /region_name="Ferlin_C"
                     /note="Ferlin C-terminus; pfam16165"
                     /db_xref="CDD:435183"
     CDS             1..1998
                     /gene="Otof"
                     /coded_by="NM_001276720.1:110..6106"
                     /db_xref="GeneID:84573"
                     /db_xref="RGD:620646"
ORIGIN      
        1 malivhlktv selrgradri akvtfrgqsf ysrvlenced vadfdetfrw pvassidrne
       61 vleiqifnys kvfsnkligt frmvlqkvve enrvevsdtl iddnnaiikt slsmevryqa
      121 adgtvgpwdd gdflgdeslq eeekdsqetd gllpgsrpst rtpgeksfrr agrsvfsamk
      181 lgktrshkee pqrqdepavl emedldhlai rlgdgldpds vslasvtalt snvsnkrskp
      241 dikmepsagr pmdyqvsitv iearqlvgln mdpvvcvevg ddkkytsmke stncpyyney
      301 fvfdfhvspd vmfdkiikis vihsknllrs gtlvgsfkmd vgtvysqpeh qfhhkwails
      361 dpddisaglk gyvkcdvavv gkgdniktph kanetdeddi egnlllpegv pperqwarfy
      421 vkiyraeglp rmntslmanv kkafigenkd lvdpyvqvff agqkgktsvq kssyeplwne
      481 qvvftdlfpp lckrmkvqir dsdkvndvai gthfidlrki sndgdkgflp tlgpawvnmy
      541 gstrnytlld ehqdlneglg egvsfrarlm lglaveildt snpeltsste vqveqatpvs
      601 esctgrmeef flfgafleas midrkngdkp vtfevtigny gnevdgtsrp qrprprkepg
      661 deeevdliqn ssddegdeag dlasvsstpp mrpqitdrny fhlpylerkp ciyikswwpd
      721 qrrrlynani mdhiadklee glndvqemik teksyperrl rgvleelscg chrflslsdk
      781 dqghssrtrl drerlkscmr elesmgqqak slraqvkrht vrdklrlcqn flqklrflad
      841 epqhsipdvf iwmmsnnkri ayarvpskdl lfsiveeelg kdcakvktlf lklpgkrgfg
      901 sagwtvqakl elylwlglsk qrkdflcglp cgfeevkaaq glglhsfppi slvytkkqtf
      961 qlrahmyqar slfaadstgl sdpfarvffi nqsqctevln etlcptwdqm lvfdnlelyg
     1021 eahelrddpp iivieiydqd smgkadfmgr tfakplvkma deaycpprfp pqleyyqiyr
     1081 gnatagdlla afellqigps gkadlpping pvdmdrgpim pvpvgirpvl skyrvevlfw
     1141 glrdlkrvnl aqvdrprvdi ecagkgvqss lihnykknpn fntlvkwfev dlpenellhp
     1201 plnirvvdcr afgrytlvgs havsslrrfi yrppdrsaan wnttvrllrg yhmlcnggps
     1261 scptgevvvs mepevpvkkl etlvkldats davvkvdvae dekerkkkkk kgpseeaeee
     1321 epdesmldww skyfasidtm keqlrqhets gidleekeem dsteglkgpv knkeksraak
     1381 eekkkknqnp gpgqgseape kkkakidelk vypkelesef dnfedwlhtf nllrgktgdd
     1441 edgsteeeri vgrfkgslcv ykvplpedvs reagydptyg mfqgipsndp invlvriyvv
     1501 ratdlhpadi ngkadpyiai klgktdirdk enyiskqlnp vfgksfdiea sfpmesmltv
     1561 avydwdlvgt ddligetkid lenrfyskhr atcgiaqtys ihgyniwrdp mkpsqiltrl
     1621 ckegkvdgph fgphgrvkva nrvftgpsei edengqrkpt dehvalsalr hwediprvgc
     1681 rlvpehvetr pllnpdkpgi eqgrlelwvd mfpmdmpapg tpldisprkp kkyelrvivw
     1741 ntdevvledd dfftgekssd ifvrgwlkgq qedkqdtdvh yhsltgegnf nwrylfpfdy
     1801 laaeekivms kkesmfswde teykiparlt lqiwdadhfs addflgaiel dlnrfprgak
     1861 takqctmema tgevdvplvs ifkqkrvkgw wpllarnend efeltgkvea elhlltaeea
     1921 eknpvglarn epdplekpnr pdtsfiwfln plksaryflw htyrwlllkl llllllllll
     1981 alflyslpgy lakkilga
//
LOCUS       NP_596886                461 aa            linear   ROD 27-APR-2025
DEFINITION  serine incorporator 5 [Rattus norvegicus].
ACCESSION   NP_596886 XP_346611
VERSION     NP_596886.2
DBSOURCE    REFSEQ: accession NM_133395.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Rosa,A., Chande,A., Ziglio,S., De Sanctis,V., Bertorelli,R.,
            Goh,S.L., McCauley,S.M., Nowosielska,A., Antonarakis,S.E.,
            Luban,J., Santoni,F.A. and Pizzato,M.
  TITLE     HIV-1 Nef promotes infection by excluding SERINC5 from virion
            incorporation
  JOURNAL   Nature 526 (7572), 212-217 (2015)
   PUBMED   26416734
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Usami,Y., Wu,Y. and Gottlinger,H.G.
  TITLE     SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted
            by Nef
  JOURNAL   Nature 526 (7572), 218-223 (2015)
   PUBMED   26416733
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Fukazawa,N., Ayukawa,K., Nishikawa,K., Ohashi,H., Ichihara,N.,
            Hikawa,Y., Abe,T., Kudo,Y., Kiyama,H., Wada,K. and Aoki,S.
  TITLE     Identification and functional characterization of mouse TPO1 as a
            myelin membrane protein
  JOURNAL   Brain Res 1070 (1), 1-14 (2006)
   PUBMED   16405874
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Inuzuka,M., Hayakawa,M. and Ingi,T.
  TITLE     Serinc, an activity-regulated protein family, incorporates serine
            into membrane lipid synthesis
  JOURNAL   J Biol Chem 280 (42), 35776-35783 (2005)
   PUBMED   16120614
  REMARK    GeneRIF: Serinc proteins incorporate serine into membrane lipid
            synthesis
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Krueger,W.H., Gonye,G.E., Madison,D.L., Murray,K.E., Kumar,M.,
            Spoerel,N. and Pfeiffer,S.E.
  TITLE     TPO1, a member of a novel protein family, is developmentally
            regulated in cultured oligodendrocytes
  JOURNAL   J Neurochem 69 (4), 1343-1355 (1997)
   PUBMED   9326262
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Feb 6, 2015 this sequence version replaced NP_596886.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L20319.1, SRR26360194.1513994.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..461
                     /product="serine incorporator 5"
                     /note="developmentally regulated protein TPO1"
                     /calculated_mol_wt=51826
     Region          11..457
                     /region_name="Serinc"
                     /note="Serine incorporator (Serinc); pfam03348"
                     /db_xref="CDD:460891"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63175.1)"
     Site            125..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63175.1)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            392..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     Site            429..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63175.1)"
     CDS             1..461
                     /gene="Serinc5"
                     /gene_synonym="Tpo1"
                     /coded_by="NM_133395.2:156..1541"
                     /db_xref="GeneID:170907"
                     /db_xref="RGD:621571"
ORIGIN      
        1 msarccagql acccgsagca lccgccpkfr qsrstrfmyl fyftlviipc cvmmspsvmk
       61 qmtehipffe dfckgikagd tcenlvgysa vyrvcfgmac fffvfcvltf kvnnskscra
      121 sihngfwffk llllgamcsg affipdqetf lnvwryvgav gsffficiql llivefahkw
      181 nknwtagtvr nklwyaslsl atlimysiav gglalmavfy tqwddcmdnk illgvhgglc
      241 vlislaaisp cvqnrqphsg llqpgliscy vtyltfsalt skpekvvkde hgknvticvp
      301 dfgqdfrrde smvtwlgtll lvvcisyscl tsttrsssda lqrrygapel evarccfcfg
      361 pdgedteeqq nvkegprviy dekkgtvysy syfhfvllla slyvmmtlts wfhyenatie
      421 tffvgswsif wvkmascwmc vllylwtlva plccpsrqfs v
//
LOCUS       NP_001177749             619 aa            linear   ROD 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX59 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001177749
VERSION     NP_001177749.1
DBSOURCE    REFSEQ: accession NM_001190820.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY317721.1, DY310785.1, CO398251.1, BC081871.1 and CR477587.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132264 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..619
                     /product="probable ATP-dependent RNA helicase DDX59
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase DDX59; DEAD box
                     protein 59; DEAD (Asp-Glu-Ala-Asp) box polypeptide 59;
                     zinc finger HIT domain-containing protein 5"
                     /calculated_mol_wt=68068
     Region          89..593
                     /region_name="PLN00206"
                     /note="DEAD-box ATP-dependent RNA helicase; Provisional"
                     /db_xref="CDD:215103"
     CDS             1..619
                     /gene="Ddx59"
                     /coded_by="NM_001190820.1:140..1999"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289402"
                     /db_xref="RGD:1359520"
ORIGIN      
        1 mfvprslklk rnsnddlksc eakkskpeaa glqlegnret lvlesvtkea vtadrpgsas
       61 stsspscqla evcstgpdqg vkdshpseep vksfsktqrw pepgepvcvv cgrygeyicd
      121 ktdedvcsle ckakhllqvk eeegslkpss pqgaasepes pldafyvyke hpfivalrdd
      181 qietlkqqlg isvqgqevar piidfehcgf petlnqnlkk sgyevptpiq mqmipvgllg
      241 rdilasadtg sgktaafllp viiralpedk tpsaliltpt relaiqierq akelmrglpr
      301 mktvllvggl plppqlyrlq qhvkvviatp grlldiieqs svslsgikiv vvdeadtmlk
      361 mgfqqqvldv lehtpsdcqt vlvsatipds idqladqllh npvrivtgdk nlpcssvrqi
      421 ilwvedpakk kklfeilndq klfkppvlvf vdcklgadll seavqkitgl sstsihseks
      481 qverreilkg llegdyevvv stgilgrgld lvnvklvvnf dmpssldeyv hqvgrvgrlg
      541 qngtaitfin nnskrlfwdv akrvkptgsi lppqllnspy lheqkrkeqq kdrqtqsslv
      601 tganlmdiir kheksssqk
//
LOCUS       NP_068617               1144 aa            linear   ROD 27-APR-2025
DEFINITION  GNAS isoform XLas [Rattus norvegicus].
ACCESSION   NP_068617
VERSION     NP_068617.6
DBSOURCE    REFSEQ: accession NM_021845.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Taneera,J., Dhaiban,S., Mohammed,A.K., Mukhopadhyay,D.,
            Aljaibeji,H., Sulaiman,N., Fadista,J. and Salehi,A.
  TITLE     GNAS gene is an important regulator of insulin secretory capacity
            in pancreatic beta-cells
  JOURNAL   Gene 715, 144028 (2019)
   PUBMED   31374326
  REMARK    GeneRIF: GNAS is a crucial gene for the beta-cell insulin secretory
            capacity.
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Masyuk,T.V., Masyuk,A.I., Lorenzo Pisarello,M., Howard,B.N.,
            Huang,B.Q., Lee,P.Y., Fung,X., Sergienko,E., Ardecky,R.J.,
            Chung,T.D.Y., Pinkerton,A.B. and LaRusso,N.F.
  TITLE     TGR5 contributes to hepatic cystogenesis in rodents with polycystic
            liver diseases through cyclic adenosine monophosphate/Galphas
            signaling
  JOURNAL   Hepatology 66 (4), 1197-1218 (2017)
   PUBMED   28543567
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Xue,N., Wei,C., Zhang,L., Liu,H., Wang,X. and Wang,L.
  TITLE     The Characteristics of Hepatic Gsalpha-cAMP Axis in HSHF Diet-Fed
            Obese Insulin Resistance Rats and Genetic Diabetic Mice
  JOURNAL   Biol Pharm Bull 40 (6), 774-781 (2017)
   PUBMED   28260721
  REMARK    GeneRIF: Our data revealed a positive correlation between hepatic
            Gsalpha-cAMP signal axis and fasting blood glucose (FBG) in slight
            insulin resistance stage of HIgh Sugar High Fat-diet rats and
            diabetic db/db mice. The current finding thus suggested hepatic
            Gsalpha-cAMP signal axis plays a central role in regulating of FBG
            during the developing and development of T2DM.
REFERENCE   4  (residues 1 to 1144)
  AUTHORS   Erb,S.J., Schappi,J.M. and Rasenick,M.M.
  TITLE     Antidepressants Accumulate in Lipid Rafts Independent of Monoamine
            Transporters to Modulate Redistribution of the G Protein, Galphas
  JOURNAL   J Biol Chem 291 (38), 19725-19733 (2016)
   PUBMED   27432886
  REMARK    GeneRIF: Translocation of Galphas, which shows delayed onset after
            chronic antidepressant treatment of rats or of C6 glioma cells,
            tracks with the delayed onset of therapeutic action of
            antidepressants
REFERENCE   5  (residues 1 to 1144)
  AUTHORS   Sarma,T., Koutsouris,A., Yu,J.Z., Krbanjevic,A., Hope,T.J. and
            Rasenick,M.M.
  TITLE     Activation of microtubule dynamics increases neuronal growth via
            the nerve growth factor (NGF)- and Galphas-mediated signaling
            pathways
  JOURNAL   J Biol Chem 290 (16), 10045-10056 (2015)
   PUBMED   25691569
  REMARK    GeneRIF: Activated Galpha s translocates from the plasma membrane
            and, through interaction with tubulin/microtubules in the cytosol,
            is important for neurite formation, development, and outgrowth.
REFERENCE   6  (residues 1 to 1144)
  AUTHORS   Eaton,S.A., Hough,T., Fischer-Colbrie,R. and Peters,J.
  TITLE     Maternal inheritance of the Gnas cluster mutation Ex1A-T affects
            size, implicating NESP55 in growth
  JOURNAL   Mamm Genome 24 (7-8), 276-285 (2013)
   PUBMED   23839232
REFERENCE   7  (residues 1 to 1144)
  AUTHORS   Swaroop,A., Agarwal,N., Gruen,J.R., Bick,D. and Weissman,S.M.
  TITLE     Differential expression of novel Gs alpha signal transduction
            protein cDNA species
  JOURNAL   Nucleic Acids Res 19 (17), 4725-4729 (1991)
   PUBMED   1716359
REFERENCE   8  (residues 1 to 1144)
  AUTHORS   Weinstein,L.S., Gejman,P.V., Friedman,E., Kadowaki,T.,
            Collins,R.M., Gershon,E.S. and Spiegel,A.M.
  TITLE     Mutations of the Gs alpha-subunit gene in Albright hereditary
            osteodystrophy detected by denaturing gradient gel electrophoresis
  JOURNAL   Proc Natl Acad Sci U S A 87 (21), 8287-8290 (1990)
   PUBMED   2122458
REFERENCE   9  (residues 1 to 1144)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Golf: an olfactory neuron specific-G protein involved in odorant
            signal transduction
  JOURNAL   Science 244 (4906), 790-795 (1989)
   PUBMED   2499043
REFERENCE   10 (residues 1 to 1144)
  AUTHORS   Votan-Bonamour,B., Plauchu,H. and Guibaud,P.
  TITLE     [Ectopic crystalline lens linked to its cause (homocyst inuria) by
            a simple geneological enquiry]
  JOURNAL   J Genet Hum 24 Suppl, 103-106 (1976)
   PUBMED   799727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000003.1, X84047.1 and
            BC168156.1.
            
            On Jul 15, 2009 this sequence version replaced NP_068617.5.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            In addition, one of the transcripts contains a second overlapping
            ORF, which encodes a structurally unrelated protein - Alex.
            Alternative splicing of downstream exons is also observed, which
            results in different forms of the stimulatory G-protein alpha
            subunit, a key element of the classical signal transduction pathway
            linking receptor-ligand interactions with the activation of
            adenylyl cyclase and a variety of cellular reponses. Multiple
            transcript variants have been found for this gene. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (1, also known as GNASXL) is
            paternally expressed. It includes an alternate 5' exon, as compared
            to variant 3. This variant includes two overlapping open reading
            frames encoding XLas and Alex, respectively. This RefSeq represents
            XLas, also known as alpha s XXL, which is a neuroendocrine-specific
            G-protein alpha subunit; it has a distinct and much longer
            N-terminus, as compared to isoform GNASL.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X84047.1, SRR26360176.1619175.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 23839232
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..1144
                     /product="GNAS isoform XLas"
                     /note="GNAS complex locus XLas-like; guanine
                     nucleotide-binding protein G-s, alpha subunit; guanine
                     nucleotide binding protein alpha s; adenylate
                     cyclase-stimulating G alpha protein; GNAS (guanine
                     nucleotide binding protein, alpha stimulating) complex
                     locus; SCG6 (secretogranin VI)"
                     /calculated_mol_wt=122772
     Region          1..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Region          <122..560
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          316..558
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Region          622..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Region          735..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Region          741..>783
                     /region_name="UDM1_RNF168_RNF169-like"
                     /note="UDM1 (ubiquitin-dependent DSB recruitment module 1)
                     found in RING finger proteins RNF168, RNF169 and similar
                     proteins; cd22249"
                     /db_xref="CDD:409016"
     Site            order(742,744..745,750..751,754,762..763,766,769..770,
                     772..774,776..777,780)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:409016"
     Region          791..1138
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          792..805
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Site            order(797,802..804,954,973,976,1042..1043,1045,1115..1116)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            797..804
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(798..800,843,847,851,854,857..858,878,881,922,951,
                     976,984,988)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          818..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Site            949..957
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            954
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(955,957,959,970,972,976..978,980,983..984,986..989)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(957,982,985..986,989)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          969..978
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Site            973..976
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            974..990
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          1038..1045
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Site            1042..1045
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            1102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63803.3)"
     Site            order(1107..1118,1120..1123)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          1114..1119
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63803.3)"
     Site            1115..1117
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..1144
                     /gene="Gnas"
                     /gene_synonym="ALEX; G-alpha-8; Gnas1; Gnpas; Nesp55;
                     SCG6"
                     /coded_by="NM_021845.5:4..3438"
                     /note="isoform XLas is encoded by transcript variant 1"
                     /db_xref="GeneID:24896"
                     /db_xref="RGD:2716"
ORIGIN      
        1 mgmlnclhgn nmsgqhdipp evgdqpeqep leaqgaaapg agvgpaeeme tepsnnepip
       61 detdsevcgp pedsksdiqs psqafeevqv ggdyspppee ampfeiqqps lgdfwptleq
      121 pgpsgtpsgi kafnpailep gtptgahpgl gayspppeea mpfefnepaq edrcqpplqv
      181 pdlapggpea wvsralpaep gnlgfentgf redyspppee svpfqldgee fggdspppgl
      241 prvtpqigig gefptvavps tlclapaana pplwvqgaig rpfreavrsp nfaydispme
      301 itrplleigr astgvdddta vnmdsppias dgppievsga pvksehakrp plerqaaetg
      361 nspissttae eakvpslerg egsptqpetv hikpapvaes gtdsskadpd sathavlqig
      421 peevggvptm ptdlppased agpdvraepd ggtapatpae sednrepaaa aaaepaaepa
      481 aepaaepaae paaepaaeav pdteaesasg avpdtqeepa aaaasatpae paaraapvtp
      541 tepatravps arahpaagav pgasamsaaa raaaaraaya gplvwgarsl satpaarasl
      601 paraaaaara asaaravaag rsasaapsra hlrppspeiq vadpptprpa prpsawpdky
      661 ergrsccrye aasgiceies ssdeseegat gcfqwllrrn rrpgqprsht vgsnpvrnff
      721 arafgscfgl sectrsrsls pgkakdpmee rrkqmrkeam emreqkradk krsklidkql
      781 eeekmdymct hrllllgage sgkstivkqm rilhvngfng eggeedpqaa rsnsdgekat
      841 kvqdiknnlk eaietivaam snlvppvela npenqfrvdy ilsvmnvpnf dfppefyeha
      901 kalwedegvr acyersneyq lidcaqyfld kidvikqady vpsdqdllrc rvltsgifet
      961 kfqvdkvnfh mfdvggqrde rrkwiqcfnd vtaiifvvas ssynmvired nqtnrlqeal
     1021 nlfksiwnnr wlrtisvilf lnkqdllaek vlagkskied yfpefarytt pedatpepge
     1081 dprvtrakyf irdeflrist asgdgrhycy phftcavdte nirrvfndcr diiqrmhlrq
     1141 yell
//
LOCUS       NP_036742                425 aa            linear   ROD 27-APR-2025
DEFINITION  tumor necrosis factor receptor superfamily member 16 precursor
            [Rattus norvegicus].
ACCESSION   NP_036742 XP_001081319
VERSION     NP_036742.2
DBSOURCE    REFSEQ: accession NM_012610.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Yang,X.P., Dan-Dai, Chen,R.X., Li,Y.X., Rui Lv,X. and Li,Y.
  TITLE     The expression of ProBDNF and its high affinity receptor P75NTR in
            the neurons of emotion-related brain regions of post-stroke
            depression rats
  JOURNAL   Brain Res 1831, 148829 (2024)
   PUBMED   38423239
  REMARK    GeneRIF: The expression of ProBDNF and its high affinity receptor
            P75NTR in the neurons of emotion-related brain regions of
            post-stroke depression rats.
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Wu,Z., Yang,Y. and Wang,M.
  TITLE     Silencing p75NTR regulates osteogenic differentiation and
            angiogenesis of BMSCs to enhance bone healing in fractured rats
  JOURNAL   J Orthop Surg Res 19 (1), 192 (2024)
   PUBMED   38504358
  REMARK    GeneRIF: Silencing p75NTR regulates osteogenic differentiation and
            angiogenesis of BMSCs to enhance bone healing in fractured rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Crews,F.T., Fisher,R.P., Qin,L. and Vetreno,R.P.
  TITLE     HMGB1 neuroimmune signaling and REST-G9a gene repression contribute
            to ethanol-induced reversible suppression of the cholinergic neuron
            phenotype
  JOURNAL   Mol Psychiatry 28 (12), 5159-5172 (2023)
   PUBMED   37402853
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Joshi,S., Frondelli,M.J., Zanin,J.P., Levison,S.W. and
            Friedman,W.J.
  TITLE     Oligodendrocyte progenitor development from the postnatal rat
            subventricular zone is regulated by the p75 neurotrophin receptor
  JOURNAL   Glia 71 (10), 2383-2400 (2023)
   PUBMED   37334743
  REMARK    GeneRIF: Oligodendrocyte progenitor development from the postnatal
            rat subventricular zone is regulated by the p75 neurotrophin
            receptor.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Testa,G., Mainardi,M., Vannini,E., Pancrazi,L., Cattaneo,A. and
            Costa,M.
  TITLE     Disentangling the signaling complexity of nerve growth factor
            receptors by CRISPR/Cas9
  JOURNAL   FASEB J 36 (11), e22498 (2022)
   PUBMED   37036720
  REMARK    GeneRIF: Disentangling the signaling complexity of nerve growth
            factor receptors by CRISPR/Cas9.
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Metsis,M., Timmusk,T., Allikmets,R., Saarma,M. and Persson,H.
  TITLE     Regulatory elements and transcriptional regulation by testosterone
            and retinoic acid of the rat nerve growth factor receptor promoter
  JOURNAL   Gene 121 (2), 247-254 (1992)
   PUBMED   1446821
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Lee,K.F., Li,E., Huber,L.J., Landis,S.C., Sharpe,A.H., Chao,M.V.
            and Jaenisch,R.
  TITLE     Targeted mutation of the gene encoding the low affinity NGF
            receptor p75 leads to deficits in the peripheral sensory nervous
            system
  JOURNAL   Cell 69 (5), 737-749 (1992)
   PUBMED   1317267
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Parvinen,M., Pelto-Huikko,M., Soder,O., Schultz,R., Kaipia,A.,
            Mali,P., Toppari,J., Hakovirta,H., Lonnerberg,P., Ritzen,E.M. et
            al.
  TITLE     Expression of beta-nerve growth factor and its receptor in rat
            seminiferous epithelium: specific function at the onset of meiosis
  JOURNAL   J Cell Biol 117 (3), 629-641 (1992)
   PUBMED   1315318
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Mufson,E.J. and Kordower,J.H.
  TITLE     Nerve growth factor receptor expressing human basal forebrain
            neurons: pathologic alterations in Alzheimer's and Parkinson's
            disease
  JOURNAL   Prog Clin Biol Res 317, 401-414 (1989)
   PUBMED   2557638
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Radeke,M.J., Misko,T.P., Hsu,C., Herzenberg,L.A. and Shooter,E.M.
  TITLE     Gene transfer and molecular cloning of the rat nerve growth factor
            receptor
  JOURNAL   Nature 325 (6105), 593-597 (1987)
   PUBMED   3027580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB725789.1, X05137.1 and JAXUCZ010000010.1.
            
            On Mar 25, 2010 this sequence version replaced NP_036742.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X05137.1, SRR26360172.411174.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..425
                     /product="tumor necrosis factor receptor superfamily
                     member 16 precursor"
                     /note="nerve growth factor receptor, fast; low affinity
                     nerve growth factor receptor; tumor necrosis factor
                     receptor superfamily member 16; p75 ICD; gp80-LNGFR; NGF
                     receptor; nerve growth factor receptor (TNFR superfamily,
                     member 16); low affinity neurotrophin receptor p75NTR;
                     low-affinity nerve growth factor receptor p75NGR;
                     low-affinity nerve growth factor receptor p75NGFR"
                     /calculated_mol_wt=42451
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3005
     mat_peptide     30..425
                     /product="tumor necrosis factor receptor superfamily
                     member 16"
                     /calculated_mol_wt=42451
     Region          31..189
                     /region_name="TNFRSF16"
                     /note="Tumor necrosis factor receptor superfamily member
                     16 (TNFRSF16), also known as p75 neurotrophin receptor
                     (p75NTR) or CD271; cd13416"
                     /db_xref="CDD:276921"
     Region          32..65
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          33..65
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276921"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:20036257,
                     ECO:0007744|PDB:3BUK; propagated from UniProtKB/Swiss-Prot
                     (P07174.1)"
     Region          67..108
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          68..108
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276921"
     Site            order(69..70,96..99,101,104,107,112,135..136,148,163..167)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276921"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07174.1)"
     Region          109..147
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          110..147
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276921"
     Region          149..189
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          150..189
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276921"
     Region          193..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          247..284
                     /region_name="TNFR_16_TM"
                     /note="Tumor necrosis factor receptor member 16
                     trans-membrane domain; pfam18422"
                     /db_xref="CDD:436489"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          282..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08138; propagated from
                     UniProtKB/Swiss-Prot (P07174.1)"
     Region          327..342
                     /region_name="Mediates interaction with KIDINS220"
                     /note="propagated from UniProtKB/Swiss-Prot (P07174.1)"
     Region          341..416
                     /region_name="Death_p75NR"
                     /note="Death domain of p75 Neurotrophin Receptor; cd08311"
                     /db_xref="CDD:260025"
     CDS             1..425
                     /gene="Ngfr"
                     /gene_synonym="LNGFR; p75; p75NTR; RNNGFRR; Tnfrsf16"
                     /coded_by="NM_012610.2:114..1391"
                     /db_xref="GeneID:24596"
                     /db_xref="RGD:3177"
ORIGIN      
        1 mrragaacsa mdrlrlllll ilgmssggak etcstglyth sgecckacnl gegvaqpcga
       61 nqtvcepcld svtfsdvvsa tepckpctec lglqsmsapc veaddavcrc aygyyqdeet
      121 ghceacsvce vgsglvfscq dkqntvceec pegtysdean hvdpclpctv cedterqlre
      181 ctpwadaece eipgrwiprs tppegsdsta pstqepevpp eqdlvpstva dmvttvmgss
      241 qpvvtrgttd nlipvycsil aavvvglvay iafkrwnsck qnkqgansrp vnqtpppege
      301 klhsdsgisv dsqslhdqqt htqtasgqal kgdgnlyssl pltkreevek llngdtwrhl
      361 agelgyqpeh idsftheacp vrallaswga qdsatldall aalrriqrad iveslcsest
      421 atspv
//
LOCUS       NP_001258174             119 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 6 [Rattus norvegicus].
ACCESSION   NP_001258174
VERSION     NP_001258174.1
DBSOURCE    REFSEQ: accession NM_001271245.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 119)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 119)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Transcript Variant: This variant (6) differs in both UTR's and the
            coding region but maintains the reading frame, compared to variant
            3. This results in a protein (isoform 6) that is shorter at both
            the N- and C-termini, compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.223805.1,
                                           SRR26360190.1597411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..119
                     /product="cAMP-responsive element modulator isoform 6"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=13325
     Region          63..117
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          64..116
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(64,68,70..72,74..76,78..79,81..83)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(82,85,89..90,92..93,96..97,99..100,103,106..107,
                     110..111,113..114)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..119
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271245.1:110..469"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mmyphftdee tdlapshmaa atgdmptyqi rapttalpqg vvmaaspgsl hspqqlaeea
       61 trkrelrlmk nreaakecrr rkkeyvkcle srvavlevqn kklieeletl kdicspktd
//
LOCUS       NP_036796                307 aa            linear   ROD 27-APR-2025
DEFINITION  synaptophysin [Rattus norvegicus].
ACCESSION   NP_036796
VERSION     NP_036796.1
DBSOURCE    REFSEQ: accession NM_012664.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dandi,Epsilon., Theotokis,P., Petri,M.C., Sideropoulou,V.,
            Spandou,E. and Tata,D.A.
  TITLE     Environmental enrichment initiated in adolescence restores the
            reduced expression of synaptophysin and GFAP in the hippocampus of
            chronically stressed rats in a sex-specific manner
  JOURNAL   Dev Psychobiol 65 (7), e22422 (2023)
   PUBMED   37796476
  REMARK    GeneRIF: Environmental enrichment initiated in adolescence restores
            the reduced expression of synaptophysin and GFAP in the hippocampus
            of chronically stressed rats in a sex-specific manner.
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Jyothi,A.K., Thotakura,B., Priyadarshini,S.C., Patil,S.,
            Poojari,M.S. and Subramanian,M.
  TITLE     Paternal stress alters synaptic density and expression of GAP-43,
            GRIN1, M1 and SYP genes in the hippocampus and cortex of offspring
            of stress-induced male rats
  JOURNAL   Morphologie 107 (356), 67-79 (2023)
   PUBMED   35715368
  REMARK    GeneRIF: Paternal stress alters synaptic density and expression of
            GAP-43, GRIN1, M1 and SYP genes in the hippocampus and cortex of
            offspring of stress-induced male rats.
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Li,F., Liu,K., Wang,A., Harris,P.W.R., Vickers,M.H. and Guan,J.
  TITLE     Cyclic glycine-proline administration normalizes high-fat
            diet-induced synaptophysin expression in obese rats
  JOURNAL   Neuropeptides 76, 101935 (2019)
   PUBMED   31146894
  REMARK    GeneRIF: Cyclic glycine-proline administration normalizes high-fat
            diet-induced synaptophysin expression in obese rats.
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Zhu,X., Wang,P., Liu,H., Zhan,J., Wang,J., Li,M., Zeng,L. and Xu,P.
  TITLE     Changes and Significance of SYP and GAP-43 Expression in the
            Hippocampus of CIH Rats
  JOURNAL   Int J Med Sci 16 (3), 394-402 (2019)
   PUBMED   30911273
  REMARK    GeneRIF: SYP protein expression in the hippocampus in the chronic
            intermittent hypoxia rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Dandi,E., Kalamari,A., Touloumi,O., Lagoudaki,R., Nousiopoulou,E.,
            Simeonidou,C., Spandou,E. and Tata,D.A.
  TITLE     Beneficial effects of environmental enrichment on behavior, stress
            reactivity and synaptophysin/BDNF expression in hippocampus
            following early life stress
  JOURNAL   Int J Dev Neurosci 67, 19-32 (2018)
   PUBMED   29545098
  REMARK    GeneRIF: The environmental enrichment protected against the effects
            of maternal separation as indicated by the lower anxiety levels and
            the reversal of spatial memory deficits compared to animals housed
            in standard conditions. These changes were associated with
            increased synaptophysin expression in the hippocampus.
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Bargou,R.C. and Leube,R.E.
  TITLE     The synaptophysin-encoding gene in rat and man is specifically
            transcribed in neuroendocrine cells
  JOURNAL   Gene 99 (2), 197-204 (1991)
   PUBMED   1902431
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Buckley,K.M., Floor,E. and Kelly,R.B.
  TITLE     Cloning and sequence analysis of cDNA encoding p38, a major
            synaptic vesicle protein
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2447-2456 (1987)
   PUBMED   3121632
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Sudhof,T.C., Lottspeich,F., Greengard,P., Mehl,E. and Jahn,R.
  TITLE     The cDNA and derived amino acid sequences for rat and human
            synaptophysin
  JOURNAL   Nucleic Acids Res 15 (22), 9607 (1987)
   PUBMED   3120152
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Sudhof,T.C., Lottspeich,F., Greengard,P., Mehl,E. and Jahn,R.
  TITLE     A synaptic vesicle protein with a novel cytoplasmic domain and four
            transmembrane regions
  JOURNAL   Science 238 (4830), 1142-1144 (1987)
   PUBMED   3120313
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Leube,R.E., Kaiser,P., Seiter,A., Zimbelmann,R., Franke,W.W.,
            Rehm,H., Knaus,P., Prior,P., Betz,H., Reinke,H. et al.
  TITLE     Synaptophysin: molecular organization and mRNA expression as
            determined from cloned cDNA
  JOURNAL   EMBO J 6 (11), 3261-3268 (1987)
   PUBMED   3123215
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC099798.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099798.1, X06177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155304, SAMD00155321
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..307
                     /product="synaptophysin"
                     /note="major synaptic vesicle protein p38"
                     /calculated_mol_wt=33180
     Region          16..216
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            20..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07825.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07825.1)"
     Site            102..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Site            133..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Site            195..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P07825.1)"
     Region          233..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Region          249..298
                     /region_name="Repeats, Gly-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P07825.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P07825.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P07825.1)"
     CDS             1..307
                     /gene="Syp"
                     /gene_synonym="Syp1"
                     /coded_by="NM_012664.3:16..939"
                     /db_xref="GeneID:24804"
                     /db_xref="RGD:3802"
ORIGIN      
        1 mdvvnqlvag gqfrvvkepl gfvkvlqwvf aifafatcgs ytgelrlsve canktesaln
       61 ievefeypfr lhqvyfdaps cvkggttkif lvgdysssae ffvtvavfaf lysmgalaty
      121 iflqnkyren nkgpmmdfla tavfafmwlv sssawakgls dvkmatdpen iikempmcrq
      181 tgntckelrd pvtsglntsv vfgflnlvlw vgnlwfvfke tgwaapfmra ppgapekqpa
      241 pgdaygdagy gqgpggygpq dsygpqggyq pdygqpasgg ggygpqgdyg qqgygqqgap
      301 tsfsnqm
//
LOCUS       NP_001248317             225 aa            linear   ROD 27-APR-2025
DEFINITION  A-type potassium channel modulatory protein KCNIP1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001248317
VERSION     NP_001248317.1
DBSOURCE    REFSEQ: accession NM_001261388.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Del Pino,J., Frejo,M.T., Baselga,M.J.A., Capo,M.A., Moyano,P.,
            Garcia,J.M. and Diaz,M.J.
  TITLE     Neuroprotective or neurotoxic effects of 4-aminopyridine mediated
            by KChIP1 regulation through adjustment of Kv 4.3 potassium
            channels expression and GABA-mediated transmission in primary
            hippocampal cells
  JOURNAL   Toxicology 333, 107-117 (2015)
   PUBMED   25917026
  REMARK    GeneRIF: KChIP1 plays a neuroprotective role against 4-AP acute
            induced cell death in primary hippocampal cells through regulation
            of Kv 4.3 and GABA transmission but this is lost after long term
            exposure.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Rainnie,D.G., Hazra,R., Dabrowska,J., Guo,J.D., Li,C.C., Dewitt,S.
            and Muly,E.C.
  TITLE     Distribution and functional expression of Kv4 family alpha subunits
            and associated KChIP beta subunits in the bed nucleus of the stria
            terminalis
  JOURNAL   J Comp Neurol 522 (3), 609-625 (2014)
   PUBMED   24037673
  REMARK    GeneRIF: This study demonistrared that the expression and function
            of KCHIP1 channels in neurons of the rat bed nucleus of the stria
            terminalis.
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Dabrowska,J. and Rainnie,D.G.
  TITLE     Expression and distribution of Kv4 potassium channel subunits and
            potassium channel interacting proteins in subpopulations of
            interneurons in the basolateral amygdala
  JOURNAL   Neuroscience 171 (3), 721-733 (2010)
   PUBMED   20849929
  REMARK    GeneRIF: KChIP1 is selectively expressed in BLA interneurons where
            it may function to regulate the activity of A-type potassium
            channels. Hence, KChIP1 might be considered as a specific regulator
            of GABAergic inhibitory circuits in the basolateral amygdala.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   McCue,H.V., Haynes,L.P. and Burgoyne,R.D.
  TITLE     The diversity of calcium sensor proteins in the regulation of
            neuronal function
  JOURNAL   Cold Spring Harb Perspect Biol 2 (8), a004085 (2010)
   PUBMED   20668007
  REMARK    Review article
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Van Schijndel,J.E., Van Zweeden,M., Van Loo,K.M. and Martens,G.J.
  TITLE     Gene expression profiling in brain regions of a rat model
            displaying schizophrenia-related features
  JOURNAL   Behav Brain Res 207 (2), 476-479 (2010)
   PUBMED   19896980
  REMARK    GeneRIF: Aph1b and KCnIP1 are significantly differentially
            expressed in a number of brain tissues of a schizophrenia model;
            KCnIP1 is an attractive novel candidate gene that may play a role
            in the complex phenotype
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Boland,L.M., Jiang,M., Lee,S.Y., Fahrenkrug,S.C., Harnett,M.T. and
            O'Grady,S.M.
  TITLE     Functional properties of a brain-specific NH2-terminally spliced
            modulator of Kv4 channels
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C161-C170 (2003)
   PUBMED   12646414
  REMARK    GeneRIF: The features of KChIP1b modulation of Kv4 channels are
            likely to be conserved in mammals and demonstrate a role for the
            KChIP1 NH2-terminal region in the regulation of closed inactivation
            gating.
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Hilber,K., Sandtner,W., Kudlacek,O., Schreiner,B., Glaaser,I.,
            Schutz,W., Fozzard,H.A., Dudley,S.C. and Todt,H.
  TITLE     Interaction between fast and ultra-slow inactivation in the
            voltage-gated sodium channel. Does the inactivation gate stabilize
            the channel structure?
  JOURNAL   J Biol Chem 277 (40), 37105-37115 (2002)
   PUBMED   12138168
  REMARK    GeneRIF: hypothesis that occlusion of the inner vestibule of the
            Na(+) channel by the fast inactivation gate inhibits ultra-slow
            inactivation (mu1 sodium channel)
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Nakamura,T.Y., Nandi,S., Pountney,D.J., Artman,M., Rudy,B. and
            Coetzee,W.A.
  TITLE     Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4
            subfamily members, Kv4.1 and Kv4.2
  JOURNAL   FEBS Lett 499 (3), 205-209 (2001)
   PUBMED   11423117
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Ohya,S., Morohashi,Y., Muraki,K., Tomita,T., Watanabe,M.,
            Iwatsubo,T. and Imaizumi,Y.
  TITLE     Molecular cloning and expression of the novel splice variants of
            K(+) channel-interacting protein 2
  JOURNAL   Biochem Biophys Res Commun 282 (1), 96-102 (2001)
   PUBMED   11263977
REFERENCE   10 (residues 1 to 225)
  AUTHORS   An,W.F., Bowlby,M.R., Betty,M., Cao,J., Ling,H.P., Mendoza,G.,
            Hinson,J.W., Mattsson,K.I., Strassle,B.W., Trimmer,J.S. and
            Rhodes,K.J.
  TITLE     Modulation of A-type potassium channels by a family of calcium
            sensors
  JOURNAL   Nature 403 (6769), 553-556 (2000)
   PUBMED   10676964
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 5' coding
            region compared to variant 1. The resulting protein (isoform 2) is
            shorter but has the same N- and C- termini compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1488705.1,
                                           SRR26360176.1589830.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..225
                     /product="A-type potassium channel modulatory protein
                     KCNIP1 isoform 2"
                     /note="potassium channel-interacting protein 1; A-type
                     potassium channel modulatory protein 1; Kv
                     channel-interacting protein 1; A-type potassium channel
                     modulatory protein KCNIP1"
                     /calculated_mol_wt=26124
     Region          75..210
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..225
                     /gene="Kcnip1"
                     /gene_synonym="Kchip1"
                     /coded_by="NM_001261388.1:138..815"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65023"
                     /db_xref="RGD:70886"
ORIGIN      
        1 msgcskrcrl gfvkfaqtif klitgtlskd kieddlemtm vchrpegleq leaqtnftkr
       61 elqvlyrgfk necpsgvvne etfkqiyaqf fphgdastya hylfnafdtt qtgsvkfedf
      121 vtalsillrg tvheklrwtf nlydinkdgy inkeemmdiv kaiydmmgky typvlkedtp
      181 rqhvdvffqk mdknkdgivt ldeflescqe ddnimrslql fqnvm
//
LOCUS       NP_113831                393 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 1 [Rattus
            norvegicus].
ACCESSION   NP_113831
VERSION     NP_113831.1
DBSOURCE    REFSEQ: accession NM_031643.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Sun,M.H., Chen,X.C., Han,M., Yang,Y.N., Gao,X.M., Ma,X., Huang,Y.,
            Li,X.M., Gai,M.T., Liu,F., Ma,Y.T. and Chen,B.D.
  TITLE     Cardioprotective effects of constitutively active MEK1 against
            H2O2-induced apoptosis and autophagy in cardiomyocytes via the
            ERK1/2 signaling pathway
  JOURNAL   Biochem Biophys Res Commun 512 (1), 125-130 (2019)
   PUBMED   30876692
  REMARK    GeneRIF: used a constitutively active MEK1 gene (CaMEK)
            transfection strategy to investigate whether CaMEK provides a
            protective effect against apoptosis and autophagy induced by
            hydrogen peroxide (H2O2) in neonatal rat cardiac ventricular
            cardiomyocytes (NCMs) and the underlying mechanisms
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Giguere,H., Dumont,A.A., Berthiaume,J., Oliveira,V., Laberge,G. and
            Auger-Messier,M.
  TITLE     ADAP1 limits neonatal cardiomyocyte hypertrophy by reducing
            integrin cell surface expression
  JOURNAL   Sci Rep 8 (1), 13605 (2018)
   PUBMED   30206251
  REMARK    GeneRIF: Biotin labeling of cell surface proteins from
            cardiomyocytes overexpressing ADAP1 revealed that it reduces the
            surface expression of b1-integrin, an effect that is strongly
            potentiated by Mek1ca overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Lavoie,H., Sahmi,M., Maisonneuve,P., Marullo,S.A., Thevakumaran,N.,
            Jin,T., Kurinov,I., Sicheri,F. and Therrien,M.
  TITLE     MEK drives BRAF activation through allosteric control of KSR
            proteins
  JOURNAL   Nature 554 (7693), 549-553 (2018)
   PUBMED   29433126
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Zhang,C., Zhang,B., Wang,H., Tao,Q., Ge,S. and Zhai,Z.
  TITLE     Tumor necrosis factor alpha-stimulated gene-6 (TSG-6) inhibits the
            inflammatory response by inhibiting the activation of P38 and JNK
            signaling pathway and decreases the restenosis of vein grafts in
            rats
  JOURNAL   Heart Vessels 32 (12), 1536-1545 (2017)
   PUBMED   28975447
  REMARK    GeneRIF: TSG-6 can inhibit the inflammatory response of
            transplanted vein grafts in rats and reduce vascular injury by
            downregulation of P38 and JNK signaling pathway.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Ciribilli,Y. and Borlak,J.
  TITLE     Oncogenomics of c-Myc transgenic mice reveal novel regulators of
            extracellular signaling, angiogenesis and invasion with clinical
            significance for human lung adenocarcinoma
  JOURNAL   Oncotarget 8 (60), 101808-101831 (2017)
   PUBMED   29254206
  REMARK    Erratum:[Oncotarget. 2018 Dec 14;9(98):37269. doi:
            10.18632/oncotarget.26489. PMID: 30647859]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Catling,A.D., Schaeffer,H.J., Reuter,C.W., Reddy,G.R. and
            Weber,M.J.
  TITLE     A proline-rich sequence unique to MEK1 and MEK2 is required for raf
            binding and regulates MEK function
  JOURNAL   Mol Cell Biol 15 (10), 5214-5225 (1995)
   PUBMED   7565670
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Duan,R.D., Zheng,C.F., Guan,K.L. and Williams,J.A.
  TITLE     Activation of MAP kinase kinase (MEK) and Ras by cholecystokinin in
            rat pancreatic acini
  JOURNAL   Am J Physiol 268 (6 Pt 1), G1060-G1065 (1995)
   PUBMED   7611406
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Suzuki,T., Okumura-Noji,K. and Nishida,E.
  TITLE     ERK2-type mitogen-activated protein kinase (MAPK) and its
            substrates in postsynaptic density fractions from the rat brain
  JOURNAL   Neurosci Res 22 (3), 277-285 (1995)
   PUBMED   7478291
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Wu,J., Michel,H., Rossomando,A., Haystead,T., Shabanowitz,J.,
            Hunt,D.F. and Sturgill,T.W.
  TITLE     Renaturation and partial peptide sequencing of mitogen-activated
            protein kinase (MAP kinase) activator from rabbit skeletal muscle
  JOURNAL   Biochem J 285 (Pt 3) (Pt 3), 701-705 (1992)
   PUBMED   1379797
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Williams,A.F., Barclay,A.N., Letarte-Muirhead,M. and Morris,R.J.
  TITLE     Rat thy-1 antigens from thymus and brain: their tissue
            distribution, purification, and chemical composition
  JOURNAL   Cold Spring Harb Symp Quant Biol 41 Pt 1, 51-61 (1977)
   PUBMED   70317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI603089.1 and BC089772.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089772.1, D13341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..393
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 1"
                     /EC_number="2.7.12.2"
                     /note="MAPKK 1; MAPK/ERK kinase 1; MAP kinase kinase 1;
                     ERK activator kinase 1; MAP kinase/Erk kinase 1"
                     /calculated_mol_wt=43334
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01986.2)"
     Site            8..9
                     /site_type="cleavage"
                     /note="Cleavage, by anthrax lethal factor.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     Region          62..380
                     /region_name="PKc_MEK1"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-Activated Protein (MAP)/Extracellular
                     signal-Regulated Kinase (ERK) Kinase 1; cd06650"
                     /db_xref="CDD:270816"
     Site            order(74..78,82,95,97,127,143..146,149..150,153,190,
                     192..195,197,207..208,211,223..226,228,255,264)
                     /site_type="active"
                     /db_xref="CDD:270816"
     Site            order(74..78,80,82,95,97,127,143..146,149..150,152..153,
                     192,194..195,197,208)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270816"
     Site            order(77..78,190,192..194,211,223..226,228,255,264)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270816"
     Site            order(77..78,97,115,118,127,141,143,208..209,211..212,
                     215..216,219)
                     /site_type="other"
                     /note="noncompetitive inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:270816"
     Site            order(81,101..102,137,230,234..237,311,314..315,318..319)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270816"
     Site            207..228
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270816"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RAF.
                     /evidence=ECO:0000250|UniProtKB:Q02750; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     Site            order(221..226,228,230,234..237,309..311,314..315,318)
                     /site_type="other"
                     /note="KSR interface [polypeptide binding]"
                     /db_xref="CDD:270816"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RAF.
                     /evidence=ECO:0000250|UniProtKB:Q02750; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     Region          270..307
                     /region_name="RAF1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01986.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q02750; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:14993270; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0000269|PubMed:12876277,
                     ECO:0000269|PubMed:14993270; propagated from
                     UniProtKB/Swiss-Prot (Q01986.2)"
     CDS             1..393
                     /gene="Map2k1"
                     /gene_synonym="Mek1"
                     /coded_by="NM_031643.4:48..1229"
                     /db_xref="GeneID:170851"
                     /db_xref="RGD:70495"
ORIGIN      
        1 mpkkkptpiq lnpapdgsav ngtssaetnl ealqkkleel eldeqqrkrl eafltqkqkv
       61 gelkdddfek iselgagngg vvfkvshkps glvmarklih leikpairnq iirelqvlhe
      121 cnspyivgfy gafysdgeis icmehmdggs ldqvlkkagr ipeqilgkvs iavikgltyl
      181 rekhkimhrd vkpsnilvns rgeiklcdfg vsgqlidsma nsfvgtrsym sperlqgthy
      241 svqsdiwsmg lslvemavgr ypipppdake lellfgcqve gdaaetpprp rtpgrplssy
      301 gmdsrppmai felldyivne pppklpsgvf slefqdfvnk cliknpaera dlkqlmvhaf
      361 ikrsdaeevd fagwlcstig lnqpstptha asi
//
LOCUS       NP_001257985             836 aa            linear   ROD 27-APR-2025
DEFINITION  zinc fingers and homeoboxes protein 2 [Rattus norvegicus].
ACCESSION   NP_001257985 XP_235318
VERSION     NP_001257985.1
DBSOURCE    REFSEQ: accession NM_001271056.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Kawamura,Y., Yamanaka,K., Poh,B., Kuribayashi,H., Koso,H. and
            Watanabe,S.
  TITLE     The role of Zhx2 transcription factor in bipolar cell
            differentiation during mouse retinal development
  JOURNAL   Biochem Biophys Res Commun 503 (4), 3023-3030 (2018)
   PUBMED   30146259
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Wu,C., Qiu,R., Wang,J., Zhang,H., Murai,K. and Lu,Q.
  TITLE     ZHX2 Interacts with Ephrin-B and regulates neural progenitor
            maintenance in the developing cerebral cortex
  JOURNAL   J Neurosci 29 (23), 7404-7412 (2009)
   PUBMED   19515908
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Clement,L.C., Liu,G., Perez-Torres,I., Kanwar,Y.S., Avila-Casado,C.
            and Chugh,S.S.
  TITLE     Early changes in gene expression that influence the course of
            primary glomerular disease
  JOURNAL   Kidney Int 72 (3), 337-347 (2007)
   PUBMED   17457373
  REMARK    GeneRIF: Upregulation of B7.1 with the downregulation of GLEPP1,
            Wilms' tumor gene (WT1), megalin, and vascular endothelial growth
            factor started early and persisted through the course of primary
            glomerular disease.
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Liu,G., Clement,L.C., Kanwar,Y.S., Avila-Casado,C. and Chugh,S.S.
  TITLE     ZHX proteins regulate podocyte gene expression during the
            development of nephrotic syndrome
  JOURNAL   J Biol Chem 281 (51), 39681-39692 (2006)
   PUBMED   17056598
  REMARK    GeneRIF: ZHX proteins 1, 2 and 3 are major transcriptional
            mediators of podocyte disease
            Erratum:[J Biol Chem. 2007 Apr 27;282(17):13140]
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Kawata,H., Yamada,K., Shou,Z., Mizutani,T., Yazawa,T., Yoshino,M.,
            Sekiguchi,T., Kajitani,T. and Miyamoto,K.
  TITLE     Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX
            family, functions as a transcriptional repressor
  JOURNAL   Biochem J 373 (Pt 3), 747-757 (2003)
   PUBMED   12741956
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Peyton,D.K., Huang,M.C., Giglia,M.A., Hughes,N.K. and Spear,B.T.
  TITLE     The alpha-fetoprotein promoter is the target of Afr1-mediated
            postnatal repression
  JOURNAL   Genomics 63 (2), 173-180 (2000)
   PUBMED   10673330
REFERENCE   7  (residues 1 to 836)
  AUTHORS   Spear,B.T.
  TITLE     Mouse alpha-fetoprotein gene 5' regulatory elements are required
            for postnatal regulation by raf and Rif
  JOURNAL   Mol Cell Biol 14 (10), 6497-6505 (1994)
   PUBMED   7523852
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Vacher,J., Camper,S.A., Krumlauf,R., Compton,R.S. and Tilghman,S.M.
  TITLE     raf regulates the postnatal repression of the mouse
            alpha-fetoprotein gene at the posttranscriptional level
  JOURNAL   Mol Cell Biol 12 (2), 856-864 (1992)
   PUBMED   1370712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Aug 29, 2012 this sequence version replaced XP_235318.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ120734.1, FQ120518.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..836
                     /product="zinc fingers and homeoboxes protein 2"
                     /note="AFP regulator 1; regulator of AFP;
                     alpha-fetoprotein regulator 1; zinc finger and homeodomain
                     protein 2; transcription factor ZHX2"
                     /calculated_mol_wt=91977
     Region          24..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          27..77
                     /region_name="Interaction with EFNB1.
                     /evidence=ECO:0000250|UniProtKB:Q8C0C0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          106..158
                     /region_name="zf_C2H2_ZHX"
                     /note="Zinc-fingers and homeoboxes C2H2 finger domain;
                     pfam18387"
                     /db_xref="CDD:465737"
     Region          168..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          195..358
                     /region_name="Required for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6X8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          263..497
                     /region_name="Required for interaction with NFYA.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6X8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          263..446
                     /region_name="Required for repressor activity.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6X8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          272..321
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Region          317..446
                     /region_name="Required for nuclear localization.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6X8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          404..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Region          444..496
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(445,485,488..489,492)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          537..582
                     /region_name="HOX"
                     /note="Homeodomain; smart00389"
                     /db_xref="CDD:197696"
     Region          636..684
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Region          700..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80VX4.2)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0C0; propagated from
                     UniProtKB/Swiss-Prot (Q80VX4.2)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0C0; propagated from
                     UniProtKB/Swiss-Prot (Q80VX4.2)"
     CDS             1..836
                     /gene="Zhx2"
                     /coded_by="NM_001271056.1:345..2855"
                     /db_xref="GeneID:314988"
                     /db_xref="RGD:727926"
ORIGIN      
        1 maskrksttp cmvrtsqvve qdvleeadra kdkglgvpps dvskerwaae pepsskesev
       61 vevrsvgesq skklqggyec kycpystqnl neftehvdmq hpnvilnply vcaecnfttk
      121 kydslsdhns kfhpgetnfk lklikrnnqt vleqsieatn hvvsitasap gssdndpgvs
      181 vgktatvktg kqkadakkvp kkpdeaapdn hmegtarlvt dtaeilsrlg svellhdslg
      241 hvmpsvqlpp ninlvpkvpv plnttkynsa ldtnatmins fnkfpyptqa elswltaask
      301 hpeehiriwf atqrlkhgis wspeeveear kkmfngtiqs vpptitvlpa qltptkvsqp
      361 ilqtalpcqi lgqpslvltq vtsgstavsc spitlavagv tnhgqkrplv tpqaapepkr
      421 phiaqvpepp pkvantpltp asdrkktklq iahlkasflq sqfpddaevy rlievtglar
      481 seikkwfsdh ryrcqrgivh itseslakdq maitgtrhgr tyhvypdfaa qkfkeksqgq
      541 lktledsflk ssfptqaeve rlrvetklsr reidswfser rklrdsmeqa vldsmgsgkk
      601 gsdvvapnga lsrldqlsga qlagplpsps savvqnqeqv hllrstfart qwptpqeydq
      661 laaktglvrt eivrwfkenr cllktgtlsw leqyqrhhls ddhghdvasr ratkhvaesp
      721 kngsevahqy akdpkalgee eseklvprvk lvgdpskdcl agkpseatsd rsegsrdgqg
      781 seeneesgiv dfvevtvgee daisekwgsw sqrvaegtve radsdsdstp aeagqa
//
LOCUS       NP_036659                589 aa            linear   ROD 27-APR-2025
DEFINITION  muscarinic acetylcholine receptor M3 [Rattus norvegicus].
ACCESSION   NP_036659
VERSION     NP_036659.2
DBSOURCE    REFSEQ: accession NM_012527.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Liu,X., Ju,X., Hong,Q., Wang,X., Wu,M., Xing,W., Xu,M., Hu,C. and
            Hao,F.
  TITLE     Establishment of a CaCC-based Cell Model and Method for
            High-throughput Screening of M3 Receptor Drugs
  JOURNAL   Cell Biochem Biophys 81 (1), 49-58 (2023)
   PUBMED   36445617
  REMARK    GeneRIF: Establishment of a CaCC-based Cell Model and Method for
            High-throughput Screening of M3 Receptor Drugs.
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Wu,J., Li,X., Zhou,P. and Li,X.
  TITLE     M3 but not M4 muscarinic receptors in the rostromedial tegmental
            nucleus are involved in the acquisition of morphine-induced
            conditioned place preference
  JOURNAL   Eur J Pharmacol 882, 173274 (2020)
   PUBMED   32534071
  REMARK    GeneRIF: M3 but not M4 muscarinic receptors in the rostromedial
            tegmental nucleus are involved in the acquisition of
            morphine-induced conditioned place preference.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Deng,A.Y., deBlois,D., Laporte,S.A., Gelinas,D., Tardif,J.C.,
            Thorin,E., Shi,Y., Raignault,A. and Menard,A.
  TITLE     Novel Pathogenesis of Hypertension and Diastolic Dysfunction Caused
            by M3R (Muscarinic Cholinergic 3 Receptor) Signaling
  JOURNAL   Hypertension 72 (3), 755-764 (2018)
   PUBMED   30354759
  REMARK    GeneRIF: Eliminating muscarinic cholinergic 3 receptor (M3R) from
            Dahl salt sensitive (DSS) rats Improves diastolic dysfunction.
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Filatova,T.S., Naumenko,N., Galenko-Yaroshevsky,P.A. and
            Abramochkin,D.V.
  TITLE     M3 cholinoreceptors alter electrical activity of rat left atrium
            via suppression of L-type Ca2+ current without affecting K+
            conductance
  JOURNAL   J Physiol Biochem 73 (2), 167-174 (2017)
   PUBMED   27858307
  REMARK    GeneRIF: Data suggest that, in atrial myocardium (or isolated
            cardiomyocytes), activation of muscarinic receptors M3 (Chrm3)
            leads to shortening of action potentials via suppression of L-type
            calcium channels; the major potassium channels are not affected,
            but inwardly rectifying potassium channels are suppressed.
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Garcia,R.C., Dati,L.M., Torres,L.H., da Silva,M.A., Udo,M.S.,
            Abdalla,F.M., da Costa,J.L., Gorjao,R., Afeche,S.C., Yonamine,M.,
            Niswender,C.M., Conn,P.J., Camarini,R., Sandoval,M.R. and
            Marcourakis,T.
  TITLE     M1 and M3 muscarinic receptors may play a role in the neurotoxicity
            of anhydroecgonine methyl ester, a cocaine pyrolysis product
  JOURNAL   Sci Rep 5, 17555 (2015)
   PUBMED   26626425
  REMARK    GeneRIF: M1 and M3 muscarinic receptors may play a role in the
            neurotoxicity of anhydroecgonine methyl ester, a cocaine pyrolysis
            product.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Wess,J., Maggio,R., Palmer,J.R. and Vogel,Z.
  TITLE     Role of conserved threonine and tyrosine residues in acetylcholine
            binding and muscarinic receptor activation. A study with m3
            muscarinic receptor point mutants
  JOURNAL   J Biol Chem 267 (27), 19313-19319 (1992)
   PUBMED   1527051
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Wess,J., Gdula,D. and Brann,M.R.
  TITLE     Site-directed mutagenesis of the m3 muscarinic receptor:
            identification of a series of threonine and tyrosine residues
            involved in agonist but not antagonist binding
  JOURNAL   EMBO J 10 (12), 3729-3734 (1991)
   PUBMED   1657592
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Kurtenbach,E., Curtis,C.A., Pedder,E.K., Aitken,A., Harris,A.C. and
            Hulme,E.C.
  TITLE     Muscarinic acetylcholine receptors. Peptide sequencing identifies
            residues involved in antagonist binding and disulfide bond
            formation
  JOURNAL   J Biol Chem 265 (23), 13702-13708 (1990)
   PUBMED   2380182
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Braun,T., Schofield,P.R., Shivers,B.D., Pritchett,D.B. and
            Seeburg,P.H.
  TITLE     A novel subtype of muscarinic receptor identified by homology
            screening
  JOURNAL   Biochem Biophys Res Commun 149 (1), 125-132 (1987)
   PUBMED   3120722
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Bonner,T.I., Buckley,N.J., Young,A.C. and Brann,M.R.
  TITLE     Identification of a family of muscarinic acetylcholine receptor
            genes
  JOURNAL   Science 237 (4814), 527-532 (1987)
   PUBMED   3037705
  REMARK    Erratum:[Science 1987 Sep 25;237(4822):237]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Feb 14, 2013 this sequence version replaced NP_036659.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF408808.1, SRR26360176.481293.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..589
                     /product="muscarinic acetylcholine receptor M3"
                     /note="cholinergic receptor, muscarinic 3, cardiac"
                     /calculated_mol_wt=65935
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Site            15
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Region          65..>269
                     /region_name="7tmA_mAChR_M3"
                     /note="muscarinic acetylcholine receptor subtype M3,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15299"
                     /db_xref="CDD:320426"
     Site            67..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          69..95
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320426"
     Region          102..129
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320426"
     Site            104..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          140..170
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320426"
     Site            142..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          182..205
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320426"
     Site            184..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          227..256
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320426"
     Site            229..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          274..280
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          323..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERZ3; propagated from
                     UniProtKB/Swiss-Prot (P08483.1)"
     Region          <483..563
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          489..511
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320426"
     Site            491..513
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     Region          522..547
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320426"
     Site            526..545
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08483.1)"
     CDS             1..589
                     /gene="Chrm3"
                     /coded_by="NM_012527.2:548..2317"
                     /db_xref="GeneID:24260"
                     /db_xref="RGD:2343"
ORIGIN      
        1 mtlhsnstts plfpnisssw vhspseaglp lgtvtqlgsy nisqetgnfs sndtssdplg
       61 ghtiwqvvfi afltgflalv tiignilviv afkvnkqlkt vnnyfllsla cadliigvis
      121 mnlfttyiim nrwalgnlac dlwlsidyva snasvmnllv isfdryfsit rpltyrakrt
      181 tkragvmigl awvisfvlwa pailfwqyfv gkrtvppgec fiqflsepti tfgtaiaafy
      241 mpvtimtily wriyketekr tkelaglqas gteaeaenfv hptgssrscs syelqqqgvk
      301 rssrrkygrc hfwfttkswk psaeqmdqdh sssdswnnnd aaaslensas sdeedigset
      361 raiysivlkl pghssilnst klpssdnlqv snedlgtvdv ernahklqaq ksmgdgdncq
      421 kdftklpiql esavdtgkts dtnssadktt atlplsfkea tlakrfalkt rsqitkrkrm
      481 slikekkaaq tlsaillafi itwtpynimv lvntfcdsci pktywnlgyw lcyinstvnp
      541 vcyalcnktf rttfktlllc qcdkrkrrkq qyqqrqsvif hkrvpeqal
//
LOCUS       NP_001158178             154 aa            linear   ROD 27-APR-2025
DEFINITION  protein CutA isoform 2 [Rattus norvegicus].
ACCESSION   NP_001158178
VERSION     NP_001158178.1
DBSOURCE    REFSEQ: accession NM_001164706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Liang,D., Nunes-Tavares,N., Xie,H.Q., Carvalho,S., Bon,S. and
            Massoulie,J.
  TITLE     Protein CutA undergoes an unusual transfer into the secretory
            pathway and affects the folding, oligomerization, and secretion of
            acetylcholinesterase
  JOURNAL   J Biol Chem 284 (8), 5195-5207 (2009)
   PUBMED   19049969
  REMARK    GeneRIF: Protein CutA undergoes an unusual transfer into the
            secretory pathway and affects the folding, oligomerization, and
            secretion of acetylcholinesterase.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Arnesano,F., Banci,L., Benvenuti,M., Bertini,I., Calderone,V.,
            Mangani,S. and Viezzoli,M.S.
  TITLE     The evolutionarily conserved trimeric structure of CutA1 proteins
            suggests a role in signal transduction
  JOURNAL   J Biol Chem 278 (46), 45999-46006 (2003)
   PUBMED   12949080
  REMARK    GeneRIF: comparative x-ray crystallography analysis suggests CutA1
            proteins have a role in signal transduction through allosteric
            communications between subunits.
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Perrier,A.L., Cousin,X., Boschetti,N., Haas,R., Chatel,J.M.,
            Bon,S., Roberts,W.L., Pickett,S.R., Massoulie,J., Rosenberry,T.L.
            and Krejci,E.
  TITLE     Two distinct proteins are associated with tetrameric
            acetylcholinesterase on the cell surface
  JOURNAL   J Biol Chem 275 (44), 34260-34265 (2000)
   PUBMED   10954708
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Navaratnam,D.S., Fernando,F.S., Priddle,J.D., Giles,K., Clegg,S.M.,
            Pappin,D.J., Craig,I. and Smith,A.D.
  TITLE     Hydrophobic protein that copurifies with human brain
            acetylcholinesterase: amino acid sequence, genomic organization,
            and chromosomal localization
  JOURNAL   J Neurochem 74 (5), 2146-2153 (2000)
   PUBMED   10800960
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB586341.1 and BX883042.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            a downstream start codon compared to variant 1. Both variants 2 and
            3 encode the same protein (isoform 2), which is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB586341.1, BI296806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..154
                     /product="protein CutA isoform 2"
                     /note="protein CutA; brain acetylcholinesterase putative
                     membrane anchor; divalent cation tolerant protein CUTA"
                     /calculated_mol_wt=16282
     Region          47..141
                     /region_name="CutA1"
                     /note="CutA1 divalent ion tolerance protein; pfam03091"
                     /db_xref="CDD:460800"
     CDS             1..154
                     /gene="Cuta"
                     /gene_synonym="CutA1"
                     /coded_by="NM_001164706.1:107..571"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:294288"
                     /db_xref="RGD:1303306"
ORIGIN      
        1 mpallpvasr llllpralls masgsppsqp spasgsgyvp gsvsaafvtc pnekvakeia
       61 ravvekrlaa cvnlipqits iyewkgkiee dsevlmmikt qsslvpalte fvrsvhpyev
      121 aevialpveq gnppylhwvh qvtesvsgsg kalp
//
LOCUS       NP_072118                997 aa            linear   ROD 27-APR-2025
DEFINITION  golgin subfamily A member 2 [Rattus norvegicus].
ACCESSION   NP_072118
VERSION     NP_072118.2
DBSOURCE    REFSEQ: accession NM_022596.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Kuliyev,E., Gingras,S., Guy,C.S., Howell,S., Vogel,P. and
            Pelletier,S.
  TITLE     Overlapping Role of SCYL1 and SCYL3 in Maintaining Motor Neuron
            Viability
  JOURNAL   J Neurosci 38 (10), 2615-2630 (2018)
   PUBMED   29437892
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Zhang,D., Marlin,M.C., Liang,Z., Ahmad,M., Ashpole,N.M.,
            Sonntag,W.E., Zhao,Z.J. and Li,G.
  TITLE     The Protein Tyrosine Phosphatase MEG2 Regulates the Transport and
            Signal Transduction of Tropomyosin Receptor Kinase A
  JOURNAL   J Biol Chem 291 (46), 23895-23905 (2016)
   PUBMED   27655914
REFERENCE   4  (residues 1 to 997)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 997)
  AUTHORS   Urresti,J., Ruiz-Meana,M., Coccia,E., Arevalo,J.C., Castellano,J.,
            Fernandez-Sanz,C., Galenkamp,K.M., Planells-Ferrer,L.,
            Moubarak,R.S., Llecha-Cano,N., Reix,S., Garcia-Dorado,D.,
            Barneda-Zahonero,B. and Comella,J.X.
  TITLE     Lifeguard Inhibits Fas Ligand-mediated Endoplasmic
            Reticulum-Calcium Release Mandatory for Apoptosis in Type II
            Apoptotic Cells
  JOURNAL   J Biol Chem 291 (3), 1221-1234 (2016)
   PUBMED   26582200
REFERENCE   6  (residues 1 to 997)
  AUTHORS   Shorter,J., Watson,R., Giannakou,M.E., Clarke,M., Warren,G. and
            Barr,F.A.
  TITLE     GRASP55, a second mammalian GRASP protein involved in the stacking
            of Golgi cisternae in a cell-free system
  JOURNAL   EMBO J 18 (18), 4949-4960 (1999)
   PUBMED   10487747
REFERENCE   7  (residues 1 to 997)
  AUTHORS   Lowe,M., Rabouille,C., Nakamura,N., Watson,R., Jackman,M.,
            Jamsa,E., Rahman,D., Pappin,D.J. and Warren,G.
  TITLE     Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein
            GM130 and is required for Golgi fragmentation in mitosis
  JOURNAL   Cell 94 (6), 783-793 (1998)
   PUBMED   9753325
REFERENCE   8  (residues 1 to 997)
  AUTHORS   Nakamura,N., Lowe,M., Levine,T.P., Rabouille,C. and Warren,G.
  TITLE     The vesicle docking protein p115 binds GM130, a cis-Golgi matrix
            protein, in a mitotically regulated manner
  JOURNAL   Cell 89 (3), 445-455 (1997)
   PUBMED   9150144
REFERENCE   9  (residues 1 to 997)
  AUTHORS   Nakamura,N., Rabouille,C., Watson,R., Nilsson,T., Hui,N.,
            Slusarewicz,P., Kreis,T.E. and Warren,G.
  TITLE     Characterization of a cis-Golgi matrix protein, GM130
  JOURNAL   J Cell Biol 131 (6 Pt 2), 1715-1726 (1995)
   PUBMED   8557739
REFERENCE   10 (residues 1 to 997)
  AUTHORS   Fritzler,M.J., Hamel,J.C., Ochs,R.L. and Chan,E.K.
  TITLE     Molecular characterization of two human autoantigens: unique cDNAs
            encoding 95- and 160-kD proteins of a putative family in the Golgi
            complex
  JOURNAL   J Exp Med 178 (1), 49-62 (1993)
   PUBMED   8315394
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U35022.2, FN805927.1, FQ147221.1, JAXUCZ010000003.1, FN805702.1 and
            AA899518.1.
            
            On Aug 2, 2012 this sequence version replaced NP_072118.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..997
                     /product="golgin subfamily A member 2"
                     /note="golgi autoantigen, golgin subfamily a, 2; 130 kDa
                     cis-Golgi matrix protein; cis-Golgi matrix protein GM130"
                     /calculated_mol_wt=112684
     Region          1..86
                     /region_name="Interaction with p115/USO1.
                     /evidence=ECO:0000269|PubMed:9150144"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Site            18
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          26..49
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q08379"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Site            30
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:10769027,
                     ECO:0000269|PubMed:20699666, ECO:0000269|PubMed:9753325;
                     propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          <151..445
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          246..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          381..904
                     /region_name="GOLGA2L5"
                     /note="Putative golgin subfamily A member 2-like protein
                     5; pfam15070"
                     /db_xref="CDD:464485"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          443..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          948..993
                     /region_name="GM130_C"
                     /note="GM130 C-terminal binding motif; pfam19046"
                     /db_xref="CDD:465957"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08379; propagated from
                     UniProtKB/Swiss-Prot (Q62839.4)"
     Region          987..997
                     /region_name="Interaction with GORASP1/GRASP65.
                     /evidence=ECO:0000269|PubMed:9628863"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62839.4)"
     CDS             1..997
                     /gene="Golga2"
                     /gene_synonym="Gm130"
                     /coded_by="NM_022596.2:49..3042"
                     /db_xref="GeneID:64528"
                     /db_xref="RGD:620282"
ORIGIN      
        1 mwpprfpppr pgmseetrqs klaaakkklr eyqqknspgv pagakkkkki knghsperts
       61 asdcqsaenv ptdhtapapp staaatmflg vvpspdadli qshdagncsn lmeetktfss
      121 teslrqlsqq lnglvsests yingegltss nmkelesryq elavaldssy vtnkqlssti
      181 eelkqqnqdt ldqlekekkd yqqklakeqg alreqlqvhi qtigilvsek aelqtalaht
      241 qqaarqkage sedlasrlqs srqrvgeler tlstvstqqk qadrynkdlt kerdalklel
      301 ykngksnedl rqqnseleek lrvlvaekaa aqlgaeelqk klemselllq qfssqseasg
      361 sneqlqqame eraqleshvg qlmeslkqlq verdqyaenl kgesamwqqr vqqmaeqvha
      421 lkeekeqres qvqeleasla elrsqmeepp ppepptgpse aeerlqgeve qlqkeleglt
      481 gqlraqvqdn eslshlnreq egrllelere aqhwseqaee rkqilesmqs drttisrals
      541 qnrelkeqla elqngfvrlt nenmeitsal qseqhvkkel arklgelqer lgelketvel
      601 ksqeaqglqe qrdqclshlq qyaaayqqhl tayeqltsek ealhkqlllq tqlmdqlqhe
      661 evqgkmaaem arqelqeaqe rlkassqenq qlqaqlsllv lpgedmdqee qdeevpqpsl
      721 tipedlvsre amvafcnaai araeeeqarl rvqlreqkar crslahlaap vqsklekeav
      781 vprdmgdsvs eesnqalhva meklqnrfle vmqekvelke rveelehcci qlsgetdtig
      841 eyialyqnqr avlkarhlek eeyisrlaqd keemkvklle lqelvlrlvn ernewqgkfl
      901 avsqnpadvp apvptgsqef gaadqqdlre vsladdtepa qgeagvpapq enptaqqimq
      961 llreiqnpqe rpglgsnpci pffyradend evkimvi
//
LOCUS       NP_001258060             145 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL14m precursor [Rattus
            norvegicus].
ACCESSION   NP_001258060
VERSION     NP_001258060.1
DBSOURCE    REFSEQ: accession NM_001271131.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1 and FM100935.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM100935.1, CB798914.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676788, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..145
                     /product="large ribosomal subunit protein uL14m precursor"
                     /note="39S ribosomal protein L14, mitochondrial; 39S
                     ribosomal protein L32, mitochondrial; large ribosomal
                     subunit protein uL14m"
                     /calculated_mol_wt=12770
     transit_peptide 1..30
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:9857009; propagated from
                     UniProtKB/Swiss-Prot (Q7M0E7.2)"
                     /calculated_mol_wt=3161
     mat_peptide     31..145
                     /product="Large ribosomal subunit protein uL14m.
                     /id=PRO_0000261136"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M0E7.2)"
                     /calculated_mol_wt=12770
     Region          33..139
                     /region_name="Ribosomal_uL14"
                     /note="Ribosomal protein uL14; cd00337"
                     /db_xref="CDD:466774"
     CDS             1..145
                     /gene="Mrpl14"
                     /gene_synonym="L14mt; L32mt; MRP-L14; MRP-L32"
                     /coded_by="NM_001271131.1:93..530"
                     /db_xref="GeneID:301250"
                     /db_xref="RGD:1306240"
ORIGIN      
        1 mavltglfgf fayvrgavsq rcfstsgsls aiqkmtrvrv vdnsalgntp yhrpprcihv
       61 ynksgvgkvg dqillairgq kkkalivghr mpgsrmtpkf dsnnvvlied ngnpvgtrik
      121 ipiptslrrr egeyskvlai aqnfv
//
LOCUS       NP_001258229             230 aa            linear   ROD 27-APR-2025
DEFINITION  collagen triple helix repeat-containing protein 1 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001258229
VERSION     NP_001258229.1
DBSOURCE    REFSEQ: accession NM_001271300.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Zhu,B., Ekman,M., Svensson,D., Lindvall,J.M., Nilsson,B.O.,
            Uvelius,B. and Sward,K.
  TITLE     Array profiling reveals contribution of Cthrc1 to growth of the
            denervated rat urinary bladder
  JOURNAL   Am J Physiol Renal Physiol 314 (5), F893-F905 (2018)
   PUBMED   29357417
  REMARK    GeneRIF: Cthrc1 has role in bladder growth following denervation.
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Zhang,Q., Yin,Z.S., Zhang,F.W., Cao,K. and Sun,H.Y.
  TITLE     CTHRC1 mediates IL-1beta-induced apoptosis in chondrocytes via
            JNK1/2 signaling
  JOURNAL   Int J Mol Med 41 (4), 2270-2278 (2018)
   PUBMED   29393342
  REMARK    GeneRIF: CTHRC1 downregulation suppresses IL-1beta-induced JNK1/2
            activation.
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Wang,C., Gu,W., Sun,B., Zhang,Y., Ji,Y., Xu,X. and Wen,Y.
  TITLE     CTHRC1 promotes osteogenic differentiation of periodontal ligament
            stem cells by regulating TAZ
  JOURNAL   J Mol Histol 48 (4), 311-319 (2017)
   PUBMED   28647773
  REMARK    GeneRIF: Overexpression of CHTRC1 increased osteogenic
            differentiation of periodontal ligament stem cells, which could be
            abolished by TAZ siRNA.
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Kimura,H., Kwan,K.M., Zhang,Z., Deng,J.M., Darnay,B.G.,
            Behringer,R.R., Nakamura,T., de Crombrugghe,B. and Akiyama,H.
  TITLE     Cthrc1 is a positive regulator of osteoblastic bone formation
  JOURNAL   PLoS One 3 (9), e3174 (2008)
   PUBMED   18779865
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Yamamoto,S., Nishimura,O., Misaki,K., Nishita,M., Minami,Y.,
            Yonemura,S., Tarui,H. and Sasaki,H.
  TITLE     Cthrc1 selectively activates the planar cell polarity pathway of
            Wnt signaling by stabilizing the Wnt-receptor complex
  JOURNAL   Dev Cell 15 (1), 23-36 (2008)
   PUBMED   18606138
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Leclair,R.J., Wang,Q., Benson,M.A., Prudovsky,I. and Lindner,V.
  TITLE     Intracellular localization of Cthrc1 characterizes differentiated
            smooth muscle
  JOURNAL   Arterioscler Thromb Vasc Biol 28 (7), 1332-1338 (2008)
   PUBMED   18467647
  REMARK    GeneRIF: Intracellular localization of Cthrc1 characterizes
            differentiated smooth muscle.
REFERENCE   9  (residues 1 to 230)
  AUTHORS   LeClair,R.J., Durmus,T., Wang,Q., Pyagay,P., Terzic,A. and
            Lindner,V.
  TITLE     Cthrc1 is a novel inhibitor of transforming growth factor-beta
            signaling and neointimal lesion formation
  JOURNAL   Circ Res 100 (6), 826-833 (2007)
   PUBMED   17322174
  REMARK    GeneRIF: Cthrc1 is a cell-type-specific inhibitor of transforming
            growth factor-beta, which in turn impacts collagen type I and III
            deposition, neointimal formation, and dedifferentiation of smooth
            muscle cells.
            Erratum:[Circ Res. 2012 May 11;110(10):e72]
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Pyagay,P., Heroult,M., Wang,Q., Lehnert,W., Belden,J., Liaw,L.,
            Friesel,R.E. and Lindner,V.
  TITLE     Collagen triple helix repeat containing 1, a novel secreted protein
            in injured and diseased arteries, inhibits collagen expression and
            promotes cell migration
  JOURNAL   Circ Res 96 (2), 261-268 (2005)
   PUBMED   15618538
  REMARK    GeneRIF: CTHRC1 is transiently expressed in the arterial wall in
            response to injury where it may contribute to vascular remodeling
            by limiting collagen matrix deposition and promoting cell
            migration.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' coding region, compared to variant 1. It encodes isoform
            2, which is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220442.1, SRR26360194.654915.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16093050
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..230
                     /product="collagen triple helix repeat-containing protein
                     1 isoform 2 precursor"
                     /note="collagen triple helix repeat-containing protein 1"
                     /calculated_mol_wt=21309
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3356
     Region          <44..76
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     CDS             1..230
                     /gene="Cthrc1"
                     /coded_by="NM_001271300.1:115..807"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:282836"
                     /db_xref="RGD:628801"
ORIGIN      
        1 mhpqgraasp qlllglflvl llllqlsaps sasenpkyng mclqgpagvp grdgspgang
       61 ipgtpgipgr dgfkgekgec lresfeeswt pnykqcswss lnygidlgki aectftkmrs
      121 nsalrvlfsg slrlkcrnac cqrwyftfng aecsgplpie aiiyldqgsp elnstinihr
      181 tssveglceg igaglvdvai wvgtcsdypk gdastgwnsv sriiieelpk
//
LOCUS       NP_001257781             480 aa            linear   ROD 27-APR-2025
DEFINITION  aromatic-L-amino-acid decarboxylase isoform a [Rattus norvegicus].
ACCESSION   NP_001257781
VERSION     NP_001257781.1
DBSOURCE    REFSEQ: accession NM_001270852.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Seo,D.C., Ju,Y.H., Seo,J.J., Oh,S.J., Lee,C.J., Lee,S.E. and
            Nam,M.H.
  TITLE     DDC-Promoter-Driven Chemogenetic Activation of SNpc Dopaminergic
            Neurons Alleviates Parkinsonian Motor Symptoms
  JOURNAL   Int J Mol Sci 24 (3), 2491 (2023)
   PUBMED   36768816
  REMARK    GeneRIF: DDC-Promoter-Driven Chemogenetic Activation of SNpc
            Dopaminergic Neurons Alleviates Parkinsonian Motor Symptoms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Sizova,D., Velazquez,H., Sampaio-Maia,B., Quelhas-Santos,J.,
            Pestana,M. and Desir,G.V.
  TITLE     Renalase regulates renal dopamine and phosphate metabolism
  JOURNAL   Am J Physiol Renal Physiol 305 (6), F839-F844 (2013)
   PUBMED   23863468
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Voigt,A., Hubner,S., Lossow,K., Hermans-Borgmeyer,I., Boehm,U. and
            Meyerhof,W.
  TITLE     Genetic labeling of Tas1r1 and Tas2r131 taste receptor cells in
            mice
  JOURNAL   Chem Senses 37 (9), 897-911 (2012)
   PUBMED   23010799
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Rouzaud-Laborde,C., Hanoun,N., Baysal,I., Rech,J.S., Mias,C.,
            Calise,D., Sicard,P., Frugier,C., Seguelas,M.H., Parini,A. and
            Pizzinat,N.
  TITLE     Role of endothelial AADC in cardiac synthesis of serotonin and
            nitrates accumulation
  JOURNAL   PLoS One 7 (7), e34893 (2012)
   PUBMED   22829864
  REMARK    GeneRIF: The data show that endothelial AADC plays an important
            role in cardiac synthesis of 5-HT and possibly in 5-HT-dependent
            regulation of nitric oxide generation.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Brun,L., Ngu,L.H., Keng,W.T., Ch'ng,G.S., Choy,Y.S., Hwu,W.L.,
            Lee,W.T., Willemsen,M.A., Verbeek,M.M., Wassenberg,T., Regal,L.,
            Orcesi,S., Tonduti,D., Accorsi,P., Testard,H., Abdenur,J.E.,
            Tay,S., Allen,G.F., Heales,S., Kern,I., Kato,M., Burlina,A.,
            Manegold,C., Hoffmann,G.F. and Blau,N.
  TITLE     Clinical and biochemical features of aromatic L-amino acid
            decarboxylase deficiency
  JOURNAL   Neurology 75 (1), 64-71 (2010)
   PUBMED   20505134
  REMARK    Erratum:[Neurology. 2010 Aug 10;75(6):576. Dosage error in article
            text]
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Rorsman,F., Husebye,E.S., Winqvist,O., Bjork,E., Karlsson,F.A. and
            Kampe,O.
  TITLE     Aromatic-L-amino-acid decarboxylase, a pyridoxal
            phosphate-dependent enzyme, is a beta-cell autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8626-8629 (1995)
   PUBMED   7567987
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Eaton,M.J., Gudehithlu,K.P., Quach,T., Silvia,C.P.,
            Hadjiconstantinou,M. and Neff,N.H.
  TITLE     Distribution of aromatic L-amino acid decarboxylase mRNA in mouse
            brain by in situ hybridization histology
  JOURNAL   J Comp Neurol 337 (4), 640-654 (1993)
   PUBMED   7904615
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Albert,V.R., Lee,M.R., Bolden,A.H., Wurzburger,R.J. and Aguanno,A.
  TITLE     Distinct promoters direct neuronal and nonneuronal expression of
            rat aromatic L-amino acid decarboxylase
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12053-12057 (1992)
   PUBMED   1465439
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Tanaka,T., Horio,Y., Taketoshi,M., Imamura,I., Ando-Yamamoto,M.,
            Kangawa,K., Matsuo,H., Kuroda,M. and Wada,H.
  TITLE     Molecular cloning and sequencing of a cDNA of rat dopa
            decarboxylase: partial amino acid homologies with other enzymes
            synthesizing catecholamines
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8142-8146 (1989)
   PUBMED   2813383
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Yamazaki,N. and Sudo,J.
  TITLE     Activities of aromatic L-amino acid decarboxylase with L-dopa as
            substrate in brush-border- and basolateral membranes and cytoplasm
            obtained from rat renal cortex
  JOURNAL   Jpn J Pharmacol 46 (2), 193-196 (1988)
   PUBMED   3379830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1 and M27716.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 encode the same protein (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087032.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..480
                     /product="aromatic-L-amino-acid decarboxylase isoform a"
                     /EC_number="4.1.1.28"
                     /note="aromatic-L-amino-acid decarboxylase; L-Dopa
                     decarboxylase; dopa decarboxylase (aromatic L-amino acid
                     decarboxylase)"
                     /calculated_mol_wt=53923
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P80041; propagated from
                     UniProtKB/Swiss-Prot (P14173.1)"
     Region          35..414
                     /region_name="Pyridoxal_deC"
                     /note="Pyridoxal-dependent decarboxylase conserved domain;
                     pfam00282"
                     /db_xref="CDD:395219"
     Region          58..178
                     /region_name="2 X approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P14173.1)"
     Site            order(148..149,152,242,271,274,300,303)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99743"
     Site            303
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99743"
     CDS             1..480
                     /gene="Ddc"
                     /gene_synonym="AADC"
                     /coded_by="NM_001270852.1:34..1476"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:24311"
                     /db_xref="RGD:2494"
ORIGIN      
        1 mdsrefrrrg kemvdyiady ldgiegrpvy pdvepgylra lipttapqep etyediirdi
       61 ekiimpgvth whspyffayf ptassypaml admlcgaigc igfswaaspa cteletvmmd
      121 wlgkmlelpe aflagrageg ggviqgsase atlvallaar tkmirqlqaa speltqaalm
      181 eklvaytsdq ahssveragl iggvkikaip sdgnysmraa alrealerdk aaglipffvv
      241 vtlgttsccs fdnllevgpi cnqegvwlhi daayagsafi cpefryllng vefadsfnfn
      301 phkwllvnfd csamwvkkrt dlteafnmdp vylrhshqds glitdyrhwq iplgrrfrsl
      361 kmwfvfrmyg vkglqayirk hvklshefes lvrqdprfei ctevilglvc frlkgsnqln
      421 etllqrinsa kkihlvpcrl rdkfvlrfav csrtvesahv qlawehirdl assvlraeke
//
LOCUS       NP_001166905             272 aa            linear   ROD 27-APR-2025
DEFINITION  hereditary hemochromatosis protein homolog isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001166905
VERSION     NP_001166905.1
DBSOURCE    REFSEQ: accession NM_001173434.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Tamosauskaite,J., Atkins,J.L., Pilling,L.C., Kuo,C.L., Kuchel,G.A.,
            Ferrucci,L. and Melzer,D.
  TITLE     Hereditary Hemochromatosis Associations with Frailty, Sarcopenia
            and Chronic Pain: Evidence from 200,975 Older UK Biobank
            Participants
  JOURNAL   J Gerontol A Biol Sci Med Sci 74 (3), 337-342 (2019)
   PUBMED   30657865
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Smith,D.J., Klein,K., Hartel,G., Wainwright,C.E., Bell,S.C.,
            Anderson,G.J. and Reid,D.W.
  TITLE     Mutations in the HFE gene can be associated with increased lung
            disease severity in cystic fibrosis
  JOURNAL   Gene 683, 12-17 (2019)
   PUBMED   30291871
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Pilling,L.C., Tamosauskaite,J., Jones,G., Wood,A.R., Jones,L.,
            Kuo,C.L., Kuchel,G.A., Ferrucci,L. and Melzer,D.
  TITLE     Common conditions associated with hereditary haemochromatosis
            genetic variants: cohort study in UK Biobank
  JOURNAL   BMJ 364, k5222 (2019)
   PUBMED   30651232
  REMARK    Erratum:[BMJ. 2019 Oct 23;367:l6157. doi: 10.1136/bmj.l6157. PMID:
            31645331]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Frydlova,J., Rogalsky,D.W., Truksa,J., Traeger,L.,
            Steinbicker,A.U., Vokurka,M. and Krijt,J.
  TITLE     Liver HFE protein content is posttranscriptionally decreased in
            iron-deficient mice and rats
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 315 (4), G560-G568 (2018)
   PUBMED   29927322
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Lee,N.P., Wu,H., Ng,K.T.P., Luo,R., Lam,T.W., Lo,C.M. and Man,K.
  TITLE     Transcriptome Analysis of Acute Phase Liver Graft Injury in Liver
            Transplantation
  JOURNAL   Biomedicines 6 (2), 41 (2018)
   PUBMED   29642405
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Sanchez,M., Queralt,R., Bruguera,M., Rodes,J. and Oliva,R.
  TITLE     Cloning, sequencing and characterization of the rat hereditary
            hemochromatosis promoter: comparison of the human, mouse and rat
            HFE promoter regions
  JOURNAL   Gene 225 (1-2), 77-87 (1998)
   PUBMED   9931446
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Lebron,J.A., Bennett,M.J., Vaughn,D.E., Chirino,A.J., Snow,P.M.,
            Mintier,G.A., Feder,J.N. and Bjorkman,P.J.
  TITLE     Crystal structure of the hemochromatosis protein HFE and
            characterization of its interaction with transferrin receptor
  JOURNAL   Cell 93 (1), 111-123 (1998)
   PUBMED   9546397
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Feder,J.N., Penny,D.M., Irrinki,A., Lee,V.K., Lebron,J.A.,
            Watson,N., Tsuchihashi,Z., Sigal,E., Bjorkman,P.J. and
            Schatzman,R.C.
  TITLE     The hemochromatosis gene product complexes with the transferrin
            receptor and lowers its affinity for ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1472-1477 (1998)
   PUBMED   9465039
REFERENCE   9  (residues 1 to 272)
  AUTHORS   George,D.K., Goldwurm,S., MacDonald,G.A., Cowley,L.L., Walker,N.I.,
            Ward,P.J., Jazwinska,E.C. and Powell,L.W.
  TITLE     Increased hepatic iron concentration in nonalcoholic
            steatohepatitis is associated with increased fibrosis
  JOURNAL   Gastroenterology 114 (2), 311-318 (1998)
   PUBMED   9453491
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Feder,J.N., Gnirke,A., Thomas,W., Tsuchihashi,Z., Ruddy,D.A.,
            Basava,A., Dormishian,F., Domingo,R. Jr., Ellis,M.C., Fullan,A.,
            Hinton,L.M., Jones,N.L., Kimmel,B.E., Kronmal,G.S., Lauer,P.,
            Lee,V.K., Loeb,D.B., Mapa,F.A., McClelland,E., Meyer,N.C.,
            Mintier,G.A., Moeller,N., Moore,T., Morikang,E., Prass,C.E.,
            Quintana,L., Starnes,S.M., Schatzman,R.C., Brunke,K.J.,
            Drayna,D.T., Risch,N.J., Bacon,B.R. and Wolff,R.K.
  TITLE     A novel MHC class I-like gene is mutated in patients with
            hereditary haemochromatosis
  JOURNAL   Nat Genet 13 (4), 399-408 (1996)
   PUBMED   8696333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting protein (isoform 2) is
            shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219597.1, AF176534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..272
                     /product="hereditary hemochromatosis protein homolog
                     isoform 2 precursor"
                     /note="hereditary hemochromatosis protein homolog;
                     RT1-CAFE"
                     /calculated_mol_wt=28002
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2774
     Region          <40..127
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Region          129..222
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          146..150
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409612"
     Region          161..165
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409612"
     Region          193..197
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409612"
     Region          204..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409612"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409612"
     CDS             1..272
                     /gene="Hfe"
                     /coded_by="NM_001173434.1:81..899"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29199"
                     /db_xref="RGD:2793"
ORIGIN      
        1 mdrsaglpvr llllllllll wsvapqalrp vtklrvvpes hilqvilgce vhednstsgf
       61 wkygydgqdh lefcpktlnw saaeprawat kmeweehrir arqsrdylqr dcpqqlkqvl
      121 elqrgvlgqq vptlvkvtrh wastgtslrc qalnffpqni tmrwlkdsqp ldakdvnpen
      181 vlpngdgtyq gwltlavapg eetrfscqve hpgldqplta twepsrsqdm iigiisgiti
      241 caiffvgili lvlrkrkvsg gtmgdyvlte ce
//
LOCUS       NP_072109                511 aa            linear   ROD 27-APR-2025
DEFINITION  ectonucleoside triphosphate diphosphohydrolase 1 [Rattus
            norvegicus].
ACCESSION   NP_072109 XP_006231470 XP_346582
VERSION     NP_072109.2
DBSOURCE    REFSEQ: accession NM_022587.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Beckenkamp,L.R., Iser,I.C., Onzi,G.R., Fontoura,D.M.S.D.,
            Bertoni,A.P.S., Sevigny,J., Lenz,G. and Wink,M.R.
  TITLE     Characterization of soluble CD39 (SolCD39/NTPDase1) from PiggyBac
            nonviral system as a tool to control the nucleotides level
  JOURNAL   Biochem J 476 (11), 1637-1651 (2019)
   PUBMED   31085558
  REMARK    GeneRIF: PiggyBac transposon system proved to be a fast and
            efficient method to generate cells stably expressing SolCD39,
            producing high amounts of the enzyme from a limited number of cells
            and with high hydrolytic activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Cardoso,A.M., Manfredi,L.H., Zanini,D., Bagatini,M.D.,
            Gutierres,J.M., Carvalho,F., Tremblay,A., Bello-Klein,A.,
            Rubin,M.A., Morsch,V.M., Sevigny,J. and Schetinger,M.R.C.
  TITLE     Physical exercise prevents memory impairment in an animal model of
            hypertension through modulation of CD39 and CD73 activities and A2A
            receptor expression
  JOURNAL   J Hypertens 37 (1), 135-143 (2019)
   PUBMED   30507864
  REMARK    GeneRIF: Studied effect of exercise on memory and cerebral cortex
            physiology of NTPDase-1 (CD39), 5' nucleotidase ecto (CD73), and
            adenosine A2a receptor (A2ar).
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Doleski,P.H., Adefegha,S.A., Cabral,F.L. and Leal,D.B.
  TITLE     Characterization of E-NTPDase (EC 3.6.1.5) activity in hepatic
            lymphocytes: A different activity profile from peripheral
            lymphocytes
  JOURNAL   Cell Biochem Funct 35 (2), 105-112 (2017)
   PUBMED   28217922
  REMARK    GeneRIF: E-NTPDase activity in hepatic lymphocytes differs from its
            activity profile in peripheral lymphocytes.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   de Azevedo,M.I., Ferreiro,L., Da Silva,A.S., Tonin,A.A.,
            Ruchel,J.B., Rezer,J.F., Franca,R.T., Zimmermann,C.E., Leal,D.B.,
            Duarte,M.M., Lopes,S.T., Flores,M.M., Fighera,R. and Santurio,J.M.
  TITLE     E-NTPDase and E-ADA activities in rats experimental infected by
            Cryptococcus neoformans
  JOURNAL   Vet Microbiol 174 (1-2), 206-213 (2014)
   PUBMED   25278365
  REMARK    GeneRIF: E-NTPDase and E-ADA activities in rats experimental
            infected by Cryptococcus neoformans are involved in the
            pathogenesis of cryptococcosis.
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Brisevac,D., Bajic,A., Bjelobaba,I., Milosevic,M., Stojiljkovic,M.,
            Beyer,C., Clarner,T., Kipp,M. and Nedeljkovic,N.
  TITLE     Expression of ecto-nucleoside triphosphate diphosphohydrolase1-3
            (NTPDase1-3) by cortical astrocytes after exposure to
            pro-inflammatory factors in vitro
  JOURNAL   J Mol Neurosci 51 (3), 871-879 (2013)
   PUBMED   23990338
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Wang,T.F. and Guidotti,G.
  TITLE     Widespread expression of ecto-apyrase (CD39) in the central nervous
            system
  JOURNAL   Brain Res 790 (1-2), 318-322 (1998)
   PUBMED   9593967
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Kegel,B., Braun,N., Heine,P., Maliszewski,C.R. and Zimmermann,H.
  TITLE     An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in
            rat brain
  JOURNAL   Neuropharmacology 36 (9), 1189-1200 (1997)
   PUBMED   9364474
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Wang,T.F., Rosenberg,P.A. and Guidotti,G.
  TITLE     Characterization of brain ecto-apyrase: evidence for only one
            ecto-apyrase (CD39) gene
  JOURNAL   Brain Res Mol Brain Res 47 (1-2), 295-302 (1997)
   PUBMED   9221928
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Kaczmarek,E., Koziak,K., Sevigny,J., Siegel,J.B., Anrather,J.,
            Beaudoin,A.R., Bach,F.H. and Robson,S.C.
  TITLE     Identification and characterization of CD39/vascular ATP
            diphosphohydrolase
  JOURNAL   J Biol Chem 271 (51), 33116-33122 (1996)
   PUBMED   8955160
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Wang,T.F. and Guidotti,G.
  TITLE     CD39 is an ecto-(Ca2+,Mg2+)-apyrase
  JOURNAL   J Biol Chem 271 (17), 9898-9901 (1996)
   PUBMED   8626624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 28, 2015 this sequence version replaced NP_072109.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.5576.1,
                                           SRR26643299.7159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..511
                     /product="ectonucleoside triphosphate diphosphohydrolase
                     1"
                     /EC_number="3.6.1.5"
                     /note="ecto-apyrase; ATPDase; NTPDase 1; lymphoid cell
                     activation antigen; ecto-ATPase 1; ecto-ATPDase 1;
                     ecto-ATP diphosphohydrolase 1; NTPDase1; nucleoside
                     triphosphate diphosphohydrolase 1"
                     /calculated_mol_wt=57206
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97687.1)"
     Region          43..466
                     /region_name="ASKHA_NBD_NTPDase1"
                     /note="nucleotide-binding domain (NBD) of ectonucleoside
                     triphosphate diphosphohydrolase 1 (NTPDase1) and similar
                     proteins; cd24110"
                     /db_xref="CDD:466960"
     Region          46..171
                     /region_name="N-terminal lobe"
                     /note="propagated from UniProtKB/Swiss-Prot (P97687.1)"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Region          205..441
                     /region_name="C-terminal lobe"
                     /note="propagated from UniProtKB/Swiss-Prot (P97687.1)"
     Site            226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            429
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            458
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97687.1)"
     Site            479..499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97687.1)"
     CDS             1..511
                     /gene="Entpd1"
                     /gene_synonym="ATP-DPH; NTPDase-1"
                     /coded_by="NM_022587.2:62..1597"
                     /db_xref="GeneID:64519"
                     /db_xref="RGD:69265"
ORIGIN      
        1 medikdskvk rfcsknilii lgfssvlavi aliavgltqn kplpenvkyg ivldagssht
       61 nlyiykwpae kendtgvvqq leecqvkgpg iskyaqktde iaaylaecmk msteripask
      121 qhqtpvylga tagmrllrme skqsadevla avsrslksyp fdfqgakiit gqeegaygwi
      181 tinyllgrft qeqswlnfis dsqkqatfga ldlggastqi tfvplnstle apetslqfrl
      241 ygtdytvyth sflcygkdqa lwqklaqdiq vssggilkdp cfypgykkvv nvselygtpc
      301 tkrfekklpf nqfqvqgtgd yeqchqsilk lfnnshcpys qcafngvflp plqgsfgafs
      361 afyfvmdffk kmandsvssq ekmteitknf cskpweevka syptvkekyl seycfsgtyi
      421 lslllqgynf tgtswdqihf mgkikdsnag wtlgymlnlt nmipaeqpls pplphstyis
      481 lmvlfslvlv amvitglfif skpsyfwkea v
//
LOCUS       NP_598196                215 aa            linear   ROD 27-APR-2025
DEFINITION  NKG2-D type II integral membrane protein [Rattus norvegicus].
ACCESSION   NP_598196
VERSION     NP_598196.1
DBSOURCE    REFSEQ: accession NM_133512.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Pasanen,A., Karjalainen,M.K., Kummola,L., Waage,J., Bonnelykke,K.,
            Ruotsalainen,M., Piippo-Savolainen,E., Goksor,E., Nuolivirta,K.,
            Chawes,B., Vissing,N., Bisgaard,H., Jartti,T., Wennergren,G.,
            Junttila,I., Hallman,M., Korppi,M. and Ramet,M.
  TITLE     NKG2D gene variation and susceptibility to viral bronchiolitis in
            childhood
  JOURNAL   Pediatr Res 84 (3), 451-457 (2018)
   PUBMED   29967528
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nabekura,T., Gotthardt,D., Niizuma,K., Trsan,T., Jenus,T.,
            Jonjic,S. and Lanier,L.L.
  TITLE     Cutting Edge: NKG2D Signaling Enhances NK Cell Responses but Alone
            Is Insufficient To Drive Expansion during Mouse Cytomegalovirus
            Infection
  JOURNAL   J Immunol 199 (5), 1567-1571 (2017)
   PUBMED   28760883
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Xu,X., Zhang,J., Zhan,S., Li,Z., Liu,X., Zhang,H., Jiang,Y. and
            Hu,X.
  TITLE     TGF-beta1 improving abnormal pregnancy outcomes induced by
            Toxoplasma gondii infection: Regulating NKG2D/DAP10 and killer
            subset of decidual NK cells
  JOURNAL   Cell Immunol 317, 9-17 (2017)
   PUBMED   28438315
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Qu,M., Yuan,X., Liu,D., Ma,Y., Zhu,J., Cui,J., Yu,M., Li,C. and
            Guo,D.
  TITLE     Bone Marrow-Derived Mesenchymal Stem Cells Attenuate
            Immune-Mediated Liver Injury and Compromise Virus Control During
            Acute Hepatitis B Virus Infection in Mice
  JOURNAL   Stem Cells Dev 26 (11), 818-827 (2017)
   PUBMED   28318408
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Lenartic,M., Jelencic,V., Zafirova,B., Ozanic,M., Marecic,V.,
            Jurkovic,S., Sexl,V., Santic,M., Wensveen,F.M. and Polic,B.
  TITLE     NKG2D Promotes B1a Cell Development and Protection against
            Bacterial Infection
  JOURNAL   J Immunol 198 (4), 1531-1542 (2017)
   PUBMED   28087665
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Hayakawa,Y., Kelly,J.M., Westwood,J.A., Darcy,P.K., Diefenbach,A.,
            Raulet,D. and Smyth,M.J.
  TITLE     Cutting edge: tumor rejection mediated by NKG2D receptor-ligand
            interaction is dependent upon perforin
  JOURNAL   J Immunol 169 (10), 5377-5381 (2002)
   PUBMED   12421908
  REMARK    GeneRIF: NKG2D acts as a natural cytotoxicity receptor to stimulate
            perforin-mediated elimination of ligand-expressing tumor cells.
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Girardi,M., Oppenheim,D.E., Steele,C.R., Lewis,J.M., Glusac,E.,
            Filler,R., Hobby,P., Sutton,B., Tigelaar,R.E. and Hayday,A.C.
  TITLE     Regulation of cutaneous malignancy by gammadelta T cells
  JOURNAL   Science 294 (5542), 605-609 (2001)
   PUBMED   11567106
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Wu,J., Song,Y., Bakker,A.B., Bauer,S., Spies,T., Lanier,L.L. and
            Phillips,J.H.
  TITLE     An activating immunoreceptor complex formed by NKG2D and DAP10
  JOURNAL   Science 285 (5428), 730-732 (1999)
   PUBMED   10426994
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Berg,S.F., Dissen,E., Westgaard,I.H. and Fossum,S.
  TITLE     Molecular characterization of rat NKR-P2, a lectin-like receptor
            expressed by NK cells and resting T cells
  JOURNAL   Int Immunol 10 (4), 379-385 (1998)
   PUBMED   9620593
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Yarbrough,W.G., Quarmby,V.E., Simental,J.A., Joseph,D.R., Sar,M.,
            Lubahn,D.B., Olsen,K.L., French,F.S. and Wilson,E.M.
  TITLE     A single base mutation in the androgen receptor gene causes
            androgen insensitivity in the testicular feminized rat
  JOURNAL   J Biol Chem 265 (15), 8893-8900 (1990)
   PUBMED   2341409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ241294.1 and AF009511.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ241294.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..215
                     /product="NKG2-D type II integral membrane protein"
                     /note="NKLLR; NK cell receptor D; NK lectin-like receptor;
                     NKG2-D-activating NK receptor; NKR-P2, ortholog of human
                     NKG2D; killer cell lectin-like receptor subfamily K,
                     member 1"
                     /calculated_mol_wt=24307
     Region          14..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70215.1)"
     Site            52..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70215.1)"
     Region          98..212
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O70215.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O70215.1)"
     Site            order(151,178,196,198..199)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O70215.1)"
     CDS             1..215
                     /gene="Klrk1"
                     /gene_synonym="NKG2D; Nkrp2"
                     /coded_by="NM_133512.2:94..741"
                     /db_xref="GeneID:24934"
                     /db_xref="RGD:3180"
ORIGIN      
        1 mskchnydlk pakwdtsqeh qkqrsalpts rpgengiirr rssieelkis plfvvrvlva
       61 amtirftvit ltwlavfitl lcnkevsvss regycgpcpn dwichrnncy qffnenkawn
      121 qsqasclsqn ssllkiyske eqdflklvks yhwmglvqsp angswqwedg sslspneltl
      181 vktpsgtcav ygssfkayte dcsnpntyic mkrav
//
LOCUS       NP_001093986             861 aa            linear   ROD 27-APR-2025
DEFINITION  BTB/POZ domain-containing protein KCTD1 [Rattus norvegicus].
ACCESSION   NP_001093986 XP_001062225 XP_214617
VERSION     NP_001093986.1
DBSOURCE    REFSEQ: accession NM_001100516.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Smaldone,G., Pirone,L., Pedone,E., Marlovits,T., Vitagliano,L. and
            Ciccarelli,L.
  TITLE     The BTB domains of the potassium channel tetramerization domain
            proteins prevalently assume pentameric states
  JOURNAL   FEBS Lett 590 (11), 1663-1671 (2016)
   PUBMED   27152988
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Ding,X., Luo,C., Zhou,J., Zhong,Y., Hu,X., Zhou,F., Ren,K., Gan,L.,
            He,A., Zhu,J., Gao,X. and Zhang,J.
  TITLE     The interaction of KCTD1 with transcription factor AP-2alpha
            inhibits its transactivation
  JOURNAL   J Cell Biochem 106 (2), 285-295 (2009)
   PUBMED   19115315
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Li,H., Gu,X., Dawson,V.L. and Dawson,T.M.
  TITLE     Identification of calcium- and nitric oxide-regulated genes by
            differential analysis of library expression (DAzLE)
  JOURNAL   Proc Natl Acad Sci U S A 101 (2), 647-652 (2004)
   PUBMED   14701905
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Luk,J.M., Mok,B.W., Shum,C.K., Yeung,W.S., Tam,P.C., Tse,J.Y.,
            Chow,J.F., Woo,J., Kam,K. and Lee,K.F.
  TITLE     Identification of novel genes expressed during spermatogenesis in
            stage-synchronized rat testes by differential display
  JOURNAL   Biochem Biophys Res Commun 307 (4), 782-790 (2003)
   PUBMED   12878178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On or before Feb 16, 2013 this sequence version replaced
            XP_001062225.2, XP_214617.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the Celera
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.58958.1,
                                           SRR26643298.72600.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..861
                     /product="BTB/POZ domain-containing protein KCTD1"
                     /note="vitamin A-deficient testicular protein 6; vitamin
                     A-deficient testicular protein 5; potassium channel
                     tetramerisation domain containing 1"
                     /calculated_mol_wt=95977
     Region          279..435
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     Region          <489..635
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          632..736
                     /region_name="BTB_POZ_KCTD1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein 1
                     (KCTD1); cd18387"
                     /db_xref="CDD:349695"
     Site            order(633,635,637,639,641..642,644..648,651,671,673,676,
                     678,680,682..684,686,689,693,696..697,699,701,703..705,
                     707..708,711,714,717)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349695"
     CDS             1..861
                     /gene="Kctd1"
                     /gene_synonym="Vad; Vad5"
                     /coded_by="NM_001100516.1:1..2586"
                     /db_xref="GeneID:291772"
                     /db_xref="RGD:621566"
ORIGIN      
        1 marmpgsgdc ntsaggsaaa gaenngerge gergaggrgr rygrphycsa geeeeeeeee
       61 deiqevqitg deeedggggl eedeeeeeee emgmdweepl epedsageel epepvhmihm
      121 dqsaalepea pprllaprar agppgdsael dpdvlqrper arlsentrla tryavrifre
      181 ylsekaqspd fetmdkgalc rvlrsfyaea rsksgqlysk sslisirssl nrylneppyc
      241 rtldltkdpe lrsanltlaa virkleeqga gpvvqkqait radlrklyts svfstntpfg
      301 llnkvwfetc myfctrgren qreleedsfg lamdedgrkf vyfkslgpyh ksrssswskk
      361 raessdeenl prmyetgtef cpyasfvkyl skrnplckaf fqrprdhcse gdvtwyenka
      421 igknllgtrm qmlskaakls ktytnhciga vsiatlnsia gigtklgspa pqgcytdsln
      481 gsarhhshha pthpshhhrp qpsslgstyi lpkdsqvgpd vkseaapkra lyesvfgsge
      541 icgpsspkrl cirpssepvd avvvvsvkhd plpllpevng hrstnsptiv spaivsptqd
      601 srpnmsrpli trspasplnn qgiptpaqlt ksnapvhidv gghmytssla tltkypesri
      661 grlfdgtepi vldslkqhyf idrdgqmfry ilnflrtskl lipddfkdyt llyeeakyfq
      721 lqpmllemer wkqdretsrf srpceclvvr vapdlgerit lsgdksliee vfpeigdvmc
      781 nsvnagwnhd sthvirfpln gychlnsvqv lerlqqrgfe ivgscgggvd ssqfseyvlr
      841 relrrtprvp svirikqepl d
//
LOCUS       NP_446332                638 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_446332
VERSION     NP_446332.2
DBSOURCE    REFSEQ: accession NM_053880.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Inaba,Y., Shinohara,K., Botilde,Y., Nabeshima,R., Takaoka,K.,
            Ajima,R., Lamri,L., Takeda,H., Saga,Y., Nakamura,T. and Hamada,H.
  TITLE     Transport of the outer dynein arm complex to cilia requires a
            cytoplasmic protein Lrrc6
  JOURNAL   Genes Cells 21 (7), 728-739 (2016)
   PUBMED   27353389
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Blasier,K.R., Humsi,M.K., Ha,J., Ross,M.W., Smiley,W.R.,
            Inamdar,N.A., Mitchell,D.J., Lo,K.W. and Pfister,K.K.
  TITLE     Live cell imaging reveals differential modifications to cytoplasmic
            dynein properties by phospho- and dephosphomimic mutations of the
            intermediate chain 2C S84
  JOURNAL   J Neurosci Res 92 (9), 1143-1154 (2014)
   PUBMED   24798412
  REMARK    GeneRIF: The data of this study suggest that the IC-2C S84 has a
            role in modulating dynein properties.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Hirayama,M., Kobayashi,D., Mizuguchi,S., Morikawa,T., Nagayama,M.,
            Midorikawa,U., Wilson,M.M., Nambu,A.N., Yoshizawa,A.C., Kawano,S.
            and Araki,N.
  TITLE     Integrated proteomics identified novel activation of dynein
            IC2-GR-COX-1 signaling in neurofibromatosis type I (NF1) disease
            model cells
  JOURNAL   Mol Cell Proteomics 12 (5), 1377-1394 (2013)
   PUBMED   23358504
  REMARK    GeneRIF: Neurofibromatosis type I-related neural abnormalities are,
            in part, caused by up-regulation of dynein IC2-glucocorticoid
            receptor-COX-1 signaling.
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Allan,V.J.
  TITLE     Cytoplasmic dynein
  JOURNAL   Biochem Soc Trans 39 (5), 1169-1178 (2011)
   PUBMED   21936784
  REMARK    Review article
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Salata,M.W., Dillman,J.F. 3rd, Lye,R.J. and Pfister,K.K.
  TITLE     Growth factor regulation of cytoplasmic dynein intermediate chain
            subunit expression preceding neurite extension
  JOURNAL   J Neurosci Res 65 (5), 408-416 (2001)
   PUBMED   11536324
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Pfister,K.K., Salata,M.W., Dillman,J.F. 3rd, Torre,E. and Lye,R.J.
  TITLE     Identification and developmental regulation of a neuron-specific
            subunit of cytoplasmic dynein
  JOURNAL   Mol Biol Cell 7 (2), 331-343 (1996)
   PUBMED   8688562
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB733957.1, FM110655.1, JAXUCZ010000003.1, BC078764.1 and
            FM076575.1.
            
            On Jul 21, 2012 this sequence version replaced NP_446332.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: U39044.1, SRR26643298.16281.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q22"
     Protein         1..638
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 1"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2;
                     cytoplasmic dynein 1 intermediate chain 2; DH IC-2; dynein
                     intermediate chain 2, cytosolic; cytoplasmic dynein
                     intermediate chain 2; dynein, cytoplasmic, intermediate
                     chain 2; oncofetal protein (OFP)"
                     /calculated_mol_wt=71208
     Region          1..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11340075; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Region          133..165
                     /region_name="Interaction with DYNLT1.
                     /evidence=ECO:0000269|PubMed:27502274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          133..163
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          154..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          277..326
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          282..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <310..413
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          330..370
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          339..377
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          379..420
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          380..>605
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          385..426
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          429..469
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          434..481
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          474..519
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          489..521
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          527..565
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          568..607
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          573..599
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..638
                     /gene="Dync1i2"
                     /gene_synonym="Dnci2; Dncic2"
                     /coded_by="NM_053880.2:355..2271"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:116659"
                     /db_xref="RGD:620174"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keaavsvqee sdlekkrrea
       61 eallqsmglt tdspivfseh wvpppmspss ksvstpseag sqdsgdgavg srtlhwdtdp
      121 salqlhsdsd lgrgpiklgm akitqvdfpp reivtytket qtpvtaqpke deeeeddvaa
      181 pkppvepeee kilkkdeend skapphelte eekqqilhse eflsffdhst riveralseq
      241 iniffdysgr dledkegeiq agaklslnrq ffderwskhr vvscldwssq ypellvasyn
      301 nneeaphepd gvalvwnmky kkttpeyvfh cqsavmsatf akfhpnlvvg gtysgqivlw
      361 dnrsnkrtpv qrtplsaaah thpvycvnvv gtqnahnlis istdgkicsw sldmlshpqd
      421 smelvhkqsk avavtsmsfp vgdvnnfvvg seegsvytac rhgskagise mfeghqgpit
      481 gihchaavga vdfshlfvts sfdwtvklwt tknnkplysf ednsdyvydv mwspthpalf
      541 acvdgmgrld lwnlnndtev ptasisvegn palnrvrwth sgreiavgds egqiviydvg
      601 eqiavprnde warfgrtlae inasradaee eaatripa
//
LOCUS       NP_446272                584 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor COE1 [Rattus norvegicus].
ACCESSION   NP_446272 XP_001067993 XP_001068049 XP_001068094 XP_001068146
VERSION     NP_446272.2
DBSOURCE    REFSEQ: accession NM_053820.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Plessy,C., Pascarella,G., Bertin,N., Akalin,A., Carrieri,C.,
            Vassalli,A., Lazarevic,D., Severin,J., Vlachouli,C., Simone,R.,
            Faulkner,G.J., Kawai,J., Daub,C.O., Zucchelli,S., Hayashizaki,Y.,
            Mombaerts,P., Lenhard,B., Gustincich,S. and Carninci,P.
  TITLE     Promoter architecture of mouse olfactory receptor genes
  JOURNAL   Genome Res 22 (3), 486-497 (2012)
   PUBMED   22194471
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Merluzzi,S., Moretti,M., Altamura,S., Zwollo,P., Sigvardsson,M.,
            Vitale,G. and Pucillo,C.
  TITLE     CD40 stimulation induces Pax5/BSAP and EBF activation through a
            APE/Ref-1-dependent redox mechanism
  JOURNAL   J Biol Chem 279 (3), 1777-1786 (2004)
   PUBMED   14594818
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Sigvardsson,M., Clark,D.R., Fitzsimmons,D., Doyle,M., Akerblad,P.,
            Breslin,T., Bilke,S., Li,R., Yeamans,C., Zhang,G. and Hagman,J.
  TITLE     Early B-cell factor, E2A, and Pax-5 cooperate to activate the early
            B cell-specific mb-1 promoter
  JOURNAL   Mol Cell Biol 22 (24), 8539-8551 (2002)
   PUBMED   12446773
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Wang,S.S., Betz,A.G. and Reed,R.R.
  TITLE     Cloning of a novel Olf-1/EBF-like gene, O/E-4, by degenerate
            oligo-based direct selection
  JOURNAL   Mol Cell Neurosci 20 (3), 404-414 (2002)
   PUBMED   12139918
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Tsai,R.Y. and Reed,R.R.
  TITLE     Identification of DNA recognition sequences and protein interaction
            domains of the multiple-Zn-finger protein Roaz
  JOURNAL   Mol Cell Biol 18 (11), 6447-6456 (1998)
   PUBMED   9774661
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Tsai,R.Y. and Reed,R.R.
  TITLE     Cloning and functional characterization of Roaz, a zinc finger
            protein that interacts with O/E-1 to regulate gene expression:
            implications for olfactory neuronal development
  JOURNAL   J Neurosci 17 (11), 4159-4169 (1997)
   PUBMED   9151733
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Wang,M.M. and Reed,R.R.
  TITLE     Molecular cloning of the olfactory neuronal transcription factor
            Olf-1 by genetic selection in yeast
  JOURNAL   Nature 364 (6433), 121-126 (1993)
   PUBMED   8321284
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ175272.1, L24051.1, FQ232013.1 and FQ177833.1.
            
            On Aug 9, 2012 this sequence version replaced NP_446272.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L24051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..584
                     /product="transcription factor COE1"
                     /note="OE-1; o/E-1; olf-1; olfactory neuronal
                     transcription factor; early B-cell factor (olfactory
                     neuronal transcription factor 1); early B-cell factor 1"
                     /calculated_mol_wt=63519
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63398.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9UH73; propagated from
                     UniProtKB/Swiss-Prot (Q63398.2)"
     Region          21..247
                     /region_name="COE1_DBD"
                     /note="Transcription factor COE1 DNA-binding domain;
                     pfam16422"
                     /db_xref="CDD:435333"
     Site            order(63..67,157,160..163,169..172,174,197,199,201..205,
                     233,235..240)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212156"
     Region          63..66
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63398.2)"
     Site            163
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802; propagated from
                     UniProtKB/Swiss-Prot (Q63398.2)"
     Site            172
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802; propagated from
                     UniProtKB/Swiss-Prot (Q63398.2)"
     Region          197..204
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63398.2)"
     Region          236..239
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:Q07802"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63398.2)"
     Region          255..339
                     /region_name="IPT_COE"
                     /note="IPT domain of the COE family (Col/Olf-1/EBF) of
                     non-basic, helix-loop-helix (HLH)-containing transcription
                     factors. COE family proteins are all transcription factors
                     and play an important role in variety of developmental
                     processes. Mouse EBF is involved...; cd01175"
                     /db_xref="CDD:238580"
     Region          340..383
                     /region_name="COE1_HLH"
                     /note="Transcription factor COE1 helix-loop-helix domain;
                     pfam16423"
                     /db_xref="CDD:406751"
     Region          450..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63398.2)"
     CDS             1..584
                     /gene="Ebf1"
                     /gene_synonym="Ebf; Olf1"
                     /coded_by="NM_053820.2:289..2043"
                     /db_xref="GeneID:116543"
                     /db_xref="RGD:620953"
ORIGIN      
        1 mfgiqesiqr sgssmkeepl gsgmnavrtw mqgagvldan taaqsgvgla rahfekqpps
       61 nlrksnffhf vlalydrqgq pveiertafv gfvekekean sektnngihy rlqllysngi
      121 rteqdfyvrl idsmtkqaiv yegqdknpem crvlltheim csrccdkksc gnrnetpsdp
      181 viidrfflkf flkcnqnclk nagnprdmrr fqvvvsttvn vdghvlavsd nmfvhnnskh
      241 grrarrldps eaatpcikai spsegwttgg atviiigdnf fdglqvifgt mlvwselitp
      301 hairvqtppr hipgvvevtl sykskqfckg tpgrfiytal neptidygfq rlqkviprhp
      361 gdperlpkev ilkraadlve alygmphnnq eiilkraadi aealysvprn hnqlpalant
      421 svhagmmgvn sfsgqlavnv seasqatnqg ftrnsssvsp hgyvpsttpq qtnynsvtts
      481 mngygsaams nlggsptfln gsaanspyai vpssptmass tslpsncsss sgifsfspan
      541 mvsavkqksa fapvvrpqts ppptctstng nslqaisgmi vppm
//
LOCUS       NP_891998                313 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase Nek6 [Rattus norvegicus].
ACCESSION   NP_891998 XP_231188
VERSION     NP_891998.1
DBSOURCE    REFSEQ: accession NM_182953.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Vaz Meirelles,G., Ferreira Lanza,D.C., da Silva,J.C., Santana
            Bernachi,J., Paes Leme,A.F. and Kobarg,J.
  TITLE     Characterization of hNek6 interactome reveals an important role for
            its short N-terminal domain and colocalization with proteins at the
            centrosome
  JOURNAL   J Proteome Res 9 (12), 6298-6316 (2010)
   PUBMED   20873783
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rapley,J., Nicolas,M., Groen,A., Regue,L., Bertran,M.T.,
            Caelles,C., Avruch,J. and Roig,J.
  TITLE     The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a
            novel site necessary for mitotic spindle formation
  JOURNAL   J Cell Sci 121 (Pt 23), 3912-3921 (2008)
   PUBMED   19001501
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Yin,M.J., Shao,L., Voehringer,D., Smeal,T. and Jallal,B.
  TITLE     The serine/threonine kinase Nek6 is required for cell cycle
            progression through mitosis
  JOURNAL   J Biol Chem 278 (52), 52454-52460 (2003)
   PUBMED   14563848
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Belham,C., Roig,J., Caldwell,J.A., Aoyama,Y., Kemp,B.E., Comb,M.
            and Avruch,J.
  TITLE     A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the
            Nek6 and Nek7 kinases
  JOURNAL   J Biol Chem 278 (37), 34897-34909 (2003)
   PUBMED   12840024
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Hashimoto,Y., Akita,H., Hibino,M., Kohri,K. and Nakanishi,M.
  TITLE     Identification and characterization of Nek6 protein kinase, a
            potential human homolog of NIMA histone H3 kinase
  JOURNAL   Biochem Biophys Res Commun 293 (2), 753-758 (2002)
   PUBMED   12054534
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Belham,C., Comb,M.J. and Avruch,J.
  TITLE     Identification of the NIMA family kinases NEK6/7 as regulators of
            the p70 ribosomal S6 kinase
  JOURNAL   Curr Biol 11 (15), 1155-1167 (2001)
   PUBMED   11516946
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Kandli,M., Feige,E., Chen,A., Kilfin,G. and Motro,B.
  TITLE     Isolation and characterization of two evolutionarily conserved
            murine kinases (Nek6 and nek7) related to the fungal mitotic
            regulator, NIMA
  JOURNAL   Genomics 68 (2), 187-196 (2000)
   PUBMED   10964517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1 and BC160820.1.
            
            On Dec 17, 2003 this sequence version replaced XP_231188.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.12338.1,
                                           SRR26643290.11456.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..313
                     /product="serine/threonine-protein kinase Nek6"
                     /EC_number="2.7.11.34"
                     /note="nimA-related protein kinase 6; never in mitosis
                     A-related kinase 6; NIMA (never in mitosis gene a)-related
                     expressed kinase 6"
                     /calculated_mol_wt=35704
     Region          1..44
                     /region_name="Interaction with ARHGAP33, ANKRA2, CDC42,
                     PRDX3, RAD26L, RBBP6, RPS7 and TRIP4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Region          44..305
                     /region_name="STKc_Nek6_7"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Never In Mitosis gene A (NIMA)-related kinase 6 and 7;
                     cd08224"
                     /db_xref="CDD:270863"
     Site            order(51..55,59,72,74,106,122..125,129,131,172,174,
                     176..177,179,190,193,195,209..212)
                     /site_type="active"
                     /db_xref="CDD:270863"
     Site            order(51..52,54..55,59,72,74,106,123..125,129,177,179,195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270863"
     Site            order(55,129,131,172,174,176,193,209..212)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270863"
     Site            108
                     /site_type="other"
                     /note="Autoinhibitory. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P59895.1)"
     Site            189..212
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270863"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK9.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Region          267..270
                     /region_name="Interaction with APBB1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     CDS             1..313
                     /gene="Nek6"
                     /coded_by="NM_182953.2:126..1067"
                     /db_xref="GeneID:360161"
                     /db_xref="RGD:727779"
ORIGIN      
        1 magqpshmph ggspnhlchv lgpahppdpq rhpntlsfrc sladfqiekk igrgqfsevy
       61 katclldrkt valkkvqife mmdakarqdc vkeigllkql nhpniikyld sfiednelni
      121 vleladagdl sqmikyfkkq krlipertvw kyfvqlcsav ehmhsrrvmh rdikpanvfi
      181 tatgivklgd lglgrffsse ttaahslvgt pyymsperih engynfksdi wslgcllyem
      241 aalqspfygd kmnlfslcqk ieqcdypplp gehyseklre lvsmciypdp nhrpdieyvh
      301 qvakqmhvwt sst
//
LOCUS       NP_037159                 88 aa            linear   ROD 27-APR-2025
DEFINITION  selenoprotein W [Rattus norvegicus].
ACCESSION   NP_037159
VERSION     NP_037159.4
DBSOURCE    REFSEQ: accession NM_013027.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Gladyshev,V.N., Arner,E.S., Berry,M.J., Brigelius-Flohe,R.,
            Bruford,E.A., Burk,R.F., Carlson,B.A., Castellano,S., Chavatte,L.,
            Conrad,M., Copeland,P.R., Diamond,A.M., Driscoll,D.M., Ferreiro,A.,
            Flohe,L., Green,F.R., Guigo,R., Handy,D.E., Hatfield,D.L.,
            Hesketh,J., Hoffmann,P.R., Holmgren,A., Hondal,R.J., Howard,M.T.,
            Huang,K., Kim,H.Y., Kim,I.Y., Kohrle,J., Krol,A., Kryukov,G.V.,
            Lee,B.J., Lee,B.C., Lei,X.G., Liu,Q., Lescure,A., Lobanov,A.V.,
            Loscalzo,J., Maiorino,M., Mariotti,M., Sandeep Prabhu,K.,
            Rayman,M.P., Rozovsky,S., Salinas,G., Schmidt,E.E., Schomburg,L.,
            Schweizer,U., Simonovic,M., Sunde,R.A., Tsuji,P.A., Tweedie,S.,
            Ursini,F., Whanger,P.D. and Zhang,Y.
  TITLE     Selenoprotein Gene Nomenclature
  JOURNAL   J Biol Chem 291 (46), 24036-24040 (2016)
   PUBMED   27645994
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Mariotti,M., Ridge,P.G., Zhang,Y., Lobanov,A.V., Pringle,T.H.,
            Guigo,R., Hatfield,D.L. and Gladyshev,V.N.
  TITLE     Composition and evolution of the vertebrate and mammalian
            selenoproteomes
  JOURNAL   PLoS One 7 (3), e33066 (2012)
   PUBMED   22479358
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Noh,O.J., Park,Y.H., Chung,Y.W. and Kim,I.Y.
  TITLE     Transcriptional regulation of selenoprotein W by MyoD during early
            skeletal muscle differentiation
  JOURNAL   J Biol Chem 285 (52), 40496-40507 (2010)
   PUBMED   20956524
  REMARK    GeneRIF: SelW gene was activated by the binding of MyoD to a
            specific E-box during early skeletal muscle differentiation.
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Schriever,S.C., Barnes,K.M., Evenson,J.K., Raines,A.M. and
            Sunde,R.A.
  TITLE     Selenium requirements are higher for glutathione peroxidase-1 mRNA
            than gpx1 activity in rat testis
  JOURNAL   Exp Biol Med (Maywood) 234 (5), 513-521 (2009)
   PUBMED   19234057
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Amantana,A., Vorachek,W.R., Butler,J.A., Ream,W. and Whanger,P.D.
  TITLE     Identification of putative transcription factor binding sites in
            rodent selenoprotein W promoter
  JOURNAL   J Inorg Biochem 98 (9), 1513-1520 (2004)
   PUBMED   15337603
  REMARK    GeneRIF: the SeW gene may be a target for Sp1 whose binding to
            various regulatory sequences of the SeW promoter may activate or
            repress the transcription of SeW
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Jeong,D.W., Kim,E.H., Kim,T.S., Chung,Y.W., Kim,H. and Kim,I.Y.
  TITLE     Different distributions of selenoprotein W and thioredoxin during
            postnatal brain development and embryogenesis
  JOURNAL   Mol Cells 17 (1), 156-159 (2004)
   PUBMED   15055543
  REMARK    GeneRIF: Se-W plays an important role as an antioxidant in the
            developing brain and embryo
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Gu,Q.P., Beilstein,M.A., Vendeland,S.C., Lugade,A., Ream,W. and
            Whanger,P.D.
  TITLE     Conserved features of selenocysteine insertion sequence (SECIS)
            elements in selenoprotein W cDNAs from five species
  JOURNAL   Gene 193 (2), 187-196 (1997)
   PUBMED   9256076
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Vendeland,S.C., Beilstein,M.A., Yeh,J.Y., Ream,W. and Whanger,P.D.
  TITLE     Rat skeletal muscle selenoprotein W: cDNA clone and mRNA modulation
            by dietary selenium
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8749-8753 (1995)
   PUBMED   7568010
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Yeh,J.Y., Beilstein,M.A., Andrews,J.S. and Whanger,P.D.
  TITLE     Tissue distribution and influence of selenium status on levels of
            selenoprotein W
  JOURNAL   FASEB J 9 (5), 392-396 (1995)
   PUBMED   7896009
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Vendeland,S.C., Beilstein,M.A., Chen,C.L., Jensen,O.N., Barofsky,E.
            and Whanger,P.D.
  TITLE     Purification and properties of selenoprotein W from rat muscle
  JOURNAL   J Biol Chem 268 (23), 17103-17107 (1993)
   PUBMED   8349599
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI279050.1, BC087625.1 and
            BI281207.1.
            
            On Nov 9, 2012 this sequence version replaced NP_037159.3.
            
            Summary: This gene encodes a selenoprotein containing a
            selenocysteine (Sec) residue, which is encoded by the UGA codon
            that normally signals translation termination. The 3' UTRs of
            selenoprotein mRNAs contain a conserved stem-loop structure, the
            Sec insertion sequence (SECIS) element that is necessary for the
            recognition of UGA as a Sec codon rather than as a stop signal.
            This protein is highly expressed in skeletal muscle and brain. It
            belongs to the SelWTH family, which possesses a thioredoxin-like
            fold and a conserved CxxU (C is cysteine, U is Sec) motif,
            suggesting a redox function for this gene. Studies in mouse show
            that this selenoprotein is involved in muscle growth and
            differentiation, and in the protection of neurons from oxidative
            stress during neuronal development. A pseudogene of this locus has
            been identified on chromosome 10. [provided by RefSeq, Aug 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224556.1, FQ217426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:8349599)
            protein contains selenocysteine  :: PMID: 7568010
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..88
                     /product="selenoprotein W"
                     /note="selenoprotein W, muscle 1; selenoprotein W, 1"
                     /calculated_mol_wt=9556
     Region          5..77
                     /region_name="CXXU_selWTH"
                     /note="selT/selW/selH selenoprotein domain; TIGR02174"
                     /db_xref="CDD:274013"
     Site            13
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..88
                     /gene="Selenow"
                     /gene_synonym="SelW; Sepw1"
                     /coded_by="NM_013027.3:85..351"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:25545"
                     /db_xref="RGD:3661"
ORIGIN      
        1 malavrvvyc gaugykpkyl qlkeklehef pgcldicgeg tpqvtgffev tvagklvhsk
       61 krgdgyvdte skfrklvtai kaalaqcq
//
LOCUS       NP_001182761             715 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase DCLK2 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001182761
VERSION     NP_001182761.1
DBSOURCE    REFSEQ: accession NM_001195832.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Dijkmans,T.F., van Hooijdonk,L.W., Fitzsimons,C.P. and
            Vreugdenhil,E.
  TITLE     The doublecortin gene family and disorders of neuronal structure
  JOURNAL   Cent Nerv Syst Agents Med Chem 10 (1), 32-46 (2010)
   PUBMED   20236041
  REMARK    Review article
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Kerjan,G., Koizumi,H., Han,E.B., Dube,C.M., Djakovic,S.N.,
            Patrick,G.N., Baram,T.Z., Heinemann,S.F. and Gleeson,J.G.
  TITLE     Mice lacking doublecortin and doublecortin-like kinase 2 display
            altered hippocampal neuronal maturation and spontaneous seizures
  JOURNAL   Proc Natl Acad Sci U S A 106 (16), 6766-6771 (2009)
   PUBMED   19342486
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Tuy,F.P., Saillour,Y., Kappeler,C., Chelly,J. and Francis,F.
  TITLE     Alternative transcripts of Dclk1 and Dclk2 and their expression in
            doublecortin knockout mice
  JOURNAL   Dev Neurosci 30 (1-3), 171-186 (2008)
   PUBMED   18075264
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Ohmae,S., Takemoto-Kimura,S., Okamura,M., Adachi-Morishima,A.,
            Nonaka,M., Fuse,T., Kida,S., Tanji,M., Furuyashiki,T., Arakawa,Y.,
            Narumiya,S., Okuno,H. and Bito,H.
  TITLE     Molecular identification and characterization of a family of
            kinases with homology to Ca2+/calmodulin-dependent protein kinases
            I/IV
  JOURNAL   J Biol Chem 281 (29), 20427-20439 (2006)
   PUBMED   16684769
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Edelman,A.M., Kim,W.Y., Higgins,D., Goldstein,E.G., Oberdoerster,M.
            and Sigurdson,W.
  TITLE     Doublecortin kinase-2, a novel doublecortin-related protein kinase
            associated with terminal segments of axons and dendrites
  JOURNAL   J Biol Chem 280 (9), 8531-8543 (2005)
   PUBMED   15611072
  REMARK    GeneRIF: Doublecortin kinase-2 is associated with terminal segments
            of axons and dendrites
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. The protein encoded by
            this gene contains two N-terminal doublecortin domains, which bind
            microtubules and regulate microtubule polymerization, a C-terminal
            serine/threonine protein kinase domain, which shows substantial
            homology to Ca2+/calmoduline-dependent protein kinase, and a
            serine/proline-rich domain in between the doublecortin and the
            protein kinase domains, which mediates multiple protein-protein
            interactions. The microtubule-polymerizing activity of the encoded
            protein is independent of its protein kinase activity. Mouse
            studies show that this gene and the DCX gene, another family
            member, share function in the establishment of hippocampal
            organization and that their absence results in a severe epileptic
            phenotype and lethality, as described in human patients with
            lissencephaly. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (1) is an exon-5-containing and
            exon-17-containing transcript (PMIDs:15611072 and 18075264). It has
            an additional exon in the 3' region, which results in frame-shift,
            as compared to variant 2. The resulting isoform (a) has a shorter
            and different C-terminus, as compared to isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY673997.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..715
                     /product="serine/threonine-protein kinase DCLK2 isoform a"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase DCLK2; caMK-like
                     CREB regulatory kinase 2; doublecortin-like and CAM
                     kinase-like 2; doublecortin kinase 2"
                     /calculated_mol_wt=78263
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N568; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Region          70..154
                     /region_name="DCX1_DCLK2"
                     /note="Dublecortin-like domain 1 found in
                     doublecortin-like kinase 2 (DCLK2); cd17141"
                     /db_xref="CDD:340661"
     Site            order(70,81..83,89,94..95,97,105,113..115,117..118,121,
                     148)
                     /site_type="other"
                     /note="putative tubulin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340661"
     Site            order(85,130)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340661"
     Region          192..275
                     /region_name="DCX2"
                     /note="Dublecortin-like domain 2; cd17069"
                     /db_xref="CDD:340589"
     Site            order(194,205..207,213,218..219,221,229,238..239,242,269)
                     /site_type="other"
                     /note="putative DCX-stabilized microtubules [polypeptide
                     binding]"
                     /db_xref="CDD:340589"
     Site            order(209,250)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340589"
     Region          301..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N568; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Region          407..665
                     /region_name="STKc_DCKL2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Doublecortin-like kinase 2 (also called Doublecortin-like
                     and CAM kinase-like 2); cd14184"
                     /db_xref="CDD:271086"
     Site            order(415..419,423,436,438,468,484..487,491,493,529..530,
                     532,534..535,537,551..552,555,567..571,573)
                     /site_type="active"
                     /db_xref="CDD:271086"
     Site            order(415..418,423,436,438,468,484..487,491,534..535,537,
                     551..552)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271086"
     Site            order(419,491,493,529..530,532,534,555,567..571,573)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271086"
     Site            551..571
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271086"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     CDS             1..715
                     /gene="Dclk2"
                     /gene_synonym="CL2; CLICK-II; CLICK2; Dck2; RGD1308384"
                     /coded_by="NM_001195832.1:609..2756"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:310698"
                     /db_xref="RGD:1308384"
ORIGIN      
        1 mastrsiele hfeerdkrpr pgsrrgapss sggssisgpk gnglipspah sahcsfyrtr
       61 tlqalssekk akkarfyrng dryfkglvfa issdrfrsfd allieltrsl sdnvnlpqgv
      121 rtiytvdgsr kvtsldelle gesyvcasne pfrkvdytkn vnpnwsvnik ggttrtlava
      181 saksevkesk dfikpklvtv irsgvkprka vrillnkkta hsfeqvltdi teaikldsgv
      241 vkrlctldgk qvtclqdffg dddvfiacgp ekyryaqddf vldhsecrvl kssysrasaa
      301 kysgsrspgl srrskspasv kraghssays takspvngtp ssqlstpkst ksssssptsp
      361 gsfrglkqis aqgrsssnvn ggpeldrcms pegvngnrcs esftllekyr igkvigdgnf
      421 avvkecmdrs tgkefalkii dkakccgkeh lienevsilr rvkhpniiml veemetttel
      481 flvmelvkgg dlfdaitsst kyterdgsam vynlasalry lhglsivhrd ikpenllvce
      541 ypdgtkslkl gdfglatvve gplytvcgtp tyvapeiiae tgyglkvdvw aagvityill
      601 cgfppfrsen nlqedlfdqi lagklefpap ywdnitdsak elisqmlqvn vearctagei
      661 lshpwvsdda sqennmqaev tgklkqhfnn alpkqnsttt gvsvimvqgh ehgsr
//
LOCUS       NP_001257666             536 aa            linear   ROD 27-APR-2025
DEFINITION  testis-specific protein 10-interacting protein isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001257666
VERSION     NP_001257666.1
DBSOURCE    REFSEQ: accession NM_001270737.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC097254.1.
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (3) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097254.1, SRR26360186.2764519.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..536
                     /product="testis-specific protein 10-interacting protein
                     isoform 3"
                     /note="fibrous sheath protein; testis-specific protein
                     10-interacting protein; tsga10-interacting protein"
                     /calculated_mol_wt=59657
     Region          1..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66MI6.2)"
     Region          185..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66MI6.2)"
     Region          246..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66MI6.2)"
     Region          491..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66MI6.2)"
     CDS             1..536
                     /gene="Tsga10ip"
                     /coded_by="NM_001270737.1:39..1649"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361707"
                     /db_xref="RGD:1302964"
ORIGIN      
        1 mlntdqllvr aiserprkst eplvpgtptg lfsllsnisp eeqgrlgsgd slqsqscqqq
       61 rsysagqttk kerkprrrnk kgrgsaeaed lfssprkpsf pfqwawesfi idgqallqsg
      121 ssvavghrsl lfppaapqck trhksvanls edlrachkse vqnlgrryqp gawanlslpl
      181 gkaesqgler ptfwstgkgs gsecedvsev egqnadeaek slstgelpql pgqgltleee
      241 lisevmeeee hnrrkgssvn kgrnsgekgs eegelqshnq gsssnsnslr kspkgtsgak
      301 efkgpwdler lhrqlqeele sgpqkqtwka lraavqasar nrktpvtgee esfltanfpn
      361 rtfhkrqeat rnllqaweqq qlkekqqaem rrareqqvqq qvarclaayt pggnrgtlgp
      421 qrkleelrrk erqrfaeyqa elqgiqhrvq arpflfqqam qtnarltanr rfsqvlsalg
      481 vdeeqllaea gnaegiprkh rsyrsfgvem esspqsppkt eptssqpgrh psptld
//
LOCUS       NP_001008508             390 aa            linear   ROD 27-APR-2025
DEFINITION  protein-tyrosine sulfotransferase 2 [Rattus norvegicus].
ACCESSION   NP_001008508 XP_213800
VERSION     NP_001008508.2
DBSOURCE    REFSEQ: accession NM_001008508.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Teramoto,T., Fujikawa,Y., Kawaguchi,Y., Kurogi,K., Soejima,M.,
            Adachi,R., Nakanishi,Y., Mishiro-Sato,E., Liu,M.C., Sakakibara,Y.,
            Suiko,M., Kimura,M. and Kakuta,Y.
  TITLE     Crystal structure of human tyrosylprotein sulfotransferase-2
            reveals the mechanism of protein tyrosine sulfation reaction
  JOURNAL   Nat Commun 4, 1572 (2013)
   PUBMED   23481380
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Marcello,M.R., Jia,W., Leary,J.A., Moore,K.L. and Evans,J.P.
  TITLE     Lack of tyrosylprotein sulfotransferase-2 activity results in
            altered sperm-egg interactions and loss of ADAM3 and ADAM6 in
            epididymal sperm
  JOURNAL   J Biol Chem 286 (15), 13060-13070 (2011)
   PUBMED   21339297
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Hoffhines,A.J., Damoc,E., Bridges,K.G., Leary,J.A. and Moore,K.L.
  TITLE     Detection and purification of tyrosine-sulfated proteins using a
            novel anti-sulfotyrosine monoclonal antibody
  JOURNAL   J Biol Chem 281 (49), 37877-37887 (2006)
   PUBMED   17046811
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Ouyang,Y.B. and Moore,K.L.
  TITLE     Molecular cloning and expression of human and mouse tyrosylprotein
            sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue
            in Caenorhabditis elegans
  JOURNAL   J Biol Chem 273 (38), 24770-24774 (1998)
   PUBMED   9733778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Jun 16, 2015 this sequence version replaced NP_001008508.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.615989.1,
                                           SRR21887620.1930341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676787 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..390
                     /product="protein-tyrosine sulfotransferase 2"
                     /EC_number="2.8.2.20"
                     /calculated_mol_wt=43628
     Region          84..275
                     /region_name="Sulfotransfer_3"
                     /note="Sulfotransferase family; pfam13469"
                     /db_xref="CDD:463887"
     CDS             1..390
                     /gene="Tpst2"
                     /gene_synonym="TPST-2"
                     /coded_by="NM_001008508.3:156..1328"
                     /db_xref="GeneID:288719"
                     /db_xref="RGD:1305331"
ORIGIN      
        1 mrrapwlglr pwlgmrlsvr kvllavgcal alvlavqlgq qvlecravlg gvrsprrmqp
       61 eqeelvmlga dhveyrygkt mplifvggvp rsgttlmram ldahpevrcg eetriiprvl
      121 amrqawtksg reklrldeag vtdevldaam qafileviak hgeparvlcn kdpftlkssv
      181 ylarlfpnsk fllmvrdgra svhsmitrkv tiagfdlssy rdcltkwnka ievmyaqcme
      241 vgrdkclpvy yeqlvlhprr slkrildflg iawsdtvlhh edligkpggv slskierstd
      301 qvikpvnlea lskwtghipr dvvrdmaqia pmlarlgydp yanppnygnp dpivinnthr
      361 vlkgdyktpa nlkgyfqvnq nstsphlgss
//
LOCUS       NP_001257597             248 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 3 [Rattus norvegicus].
ACCESSION   NP_001257597
VERSION     NP_001257597.1
DBSOURCE    REFSEQ: accession NM_001270668.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons and uses an alternate exon in place of another exon in the 3'
            end of the gene, compared to variant 1. The resulting isoform (3)
            has the same N- and C-termini but is shorter and has a different
            internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224006.1, FQ215059.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..248
                     /product="troponin T, fast skeletal muscle isoform 3"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29195
     Region          52..188
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..248
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270668.1:117..863"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eeaqeeevqe eapepeekpr pkltapkipe gekvdfddiq kkrqnkdlme
       61 lqalidshfe arkkeeeeli alkeriekrr aeraeqqrir aekererqnr laeekarree
      121 edakrraedd lkkkkalssm ganyssylak adqkrgkkqt aremkkkila errkplnidh
      181 lsddklrdka kelwdtlyql etdkfefgek lkrqkydimt vrarvemlak fskkagatak
      241 gkvggrwk
//
LOCUS       NP_113800                 77 aa            linear   ROD 27-APR-2025
DEFINITION  apelin preproprotein [Rattus norvegicus].
ACCESSION   NP_113800
VERSION     NP_113800.1
DBSOURCE    REFSEQ: accession NM_031612.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Guo,Q., Liu,Q., Zhou,S., Lin,Y., Lv,A., Zhang,L., Li,L. and
            Huang,F.
  TITLE     Apelin regulates mitochondrial dynamics by inhibiting Mst1-JNK-Drp1
            signaling pathway to reduce neuronal apoptosis after spinal cord
            injury
  JOURNAL   Neurochem Int 180, 105885 (2024)
   PUBMED   39433147
  REMARK    GeneRIF: Apelin regulates mitochondrial dynamics by inhibiting
            Mst1-JNK-Drp1 signaling pathway to reduce neuronal apoptosis after
            spinal cord injury.
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Li,Y., Hu,Q. and Wang,B.
  TITLE     Effects of Apelin on the fibrosis of retinal tissues and Muller
            cells in diabetes retinopathy through the JAK2/STAT3 signalling
            pathway
  JOURNAL   Autoimmunity 56 (1), 2259129 (2023)
   PUBMED   37771168
  REMARK    GeneRIF: Effects of Apelin on the fibrosis of retinal tissues and
            Muller cells in diabetes retinopathy through the JAK2/STAT3
            signalling pathway.
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Cardoso Dos Santos,L.M., Azar,P., Brun,C., Konig,S., Roatti,A.,
            Baertschi,A.J., Chaabane,C. and Bochaton-Piallat,M.L.
  TITLE     Apelin is expressed in intimal smooth muscle cells and promotes
            their phenotypic transition
  JOURNAL   Sci Rep 13 (1), 18736 (2023)
   PUBMED   37907514
  REMARK    GeneRIF: Apelin is expressed in intimal smooth muscle cells and
            promotes their phenotypic transition.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Gemici,B., Birsen,I. and Izgut-Uysal,V.N.
  TITLE     The apelin-apela receptor APJ is necessary for formation and
            healing of ischemia reperfusion-induced gastric ulcer in rats
  JOURNAL   Peptides 166, 171027 (2023)
   PUBMED   37245722
  REMARK    GeneRIF: The apelin-apela receptor APJ is necessary for formation
            and healing of ischemia reperfusion-induced gastric ulcer in rats.
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Soleimani,A.H., Dehghani,A., Abbasnejad,M., Esmaeili-Mahani,S.,
            Raoof,M. and Lobbezoo,F.
  TITLE     Apelin signalling in the periaqueductal grey matter alleviates
            capsaicin-evoked pulpal nocifensive behaviour and capsaicin-induced
            spatial learning and memory impairments in rat
  JOURNAL   Int Endod J 56 (8), 968-979 (2023)
   PUBMED   37184417
  REMARK    GeneRIF: Apelin signalling in the periaqueductal grey matter
            alleviates capsaicin-evoked pulpal nocifensive behaviour and
            capsaicin-induced spatial learning and memory impairments in rat.
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Reaux,A., De Mota,N., Skultetyova,I., Lenkei,Z., El Messari,S.,
            Gallatz,K., Corvol,P., Palkovits,M. and Llorens-Cortes,C.
  TITLE     Physiological role of a novel neuropeptide, apelin, and its
            receptor in the rat brain
  JOURNAL   J Neurochem 77 (4), 1085-1096 (2001)
   PUBMED   11359874
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Kawamata,Y., Habata,Y., Fukusumi,S., Hosoya,M., Fujii,R.,
            Hinuma,S., Nishizawa,N., Kitada,C., Onda,H., Nishimura,O. and
            Fujino,M.
  TITLE     Molecular properties of apelin: tissue distribution and receptor
            binding
  JOURNAL   Biochim Biophys Acta 1538 (2-3), 162-171 (2001)
   PUBMED   11336787
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Lee,D.K., Cheng,R., Nguyen,T., Fan,T., Kariyawasam,A.P., Liu,Y.,
            Osmond,D.H., George,S.R. and O'Dowd,B.F.
  TITLE     Characterization of apelin, the ligand for the APJ receptor
  JOURNAL   J Neurochem 74 (1), 34-41 (2000)
   PUBMED   10617103
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Habata,Y., Fujii,R., Hosoya,M., Fukusumi,S., Kawamata,Y.,
            Hinuma,S., Kitada,C., Nishizawa,N., Murosaki,S., Kurokawa,T.,
            Onda,H., Tatemoto,K. and Fujino,M.
  TITLE     Apelin, the natural ligand of the orphan receptor APJ, is
            abundantly secreted in the colostrum
  JOURNAL   Biochim Biophys Acta 1452 (1), 25-35 (1999)
   PUBMED   10525157
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Tatemoto,K., Hosoya,M., Habata,Y., Fujii,R., Kakegawa,T., Zou,M.X.,
            Kawamata,Y., Fukusumi,S., Hinuma,S., Kitada,C., Kurokawa,T.,
            Onda,H. and Fujino,M.
  TITLE     Isolation and characterization of a novel endogenous peptide ligand
            for the human APJ receptor
  JOURNAL   Biochem Biophys Res Commun 251 (2), 471-476 (1998)
   PUBMED   9792798
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1 and BC080843.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC080843.1, SRR26360186.2774236.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676807,
                                           SAMN16676810 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..77
                     /product="apelin preproprotein"
                     /note="APJ endogenous ligand; apelin, AGTRL1 ligand"
                     /calculated_mol_wt=6299
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2396
     proprotein      23..77
                     /product="apelin proprotein"
                     /calculated_mol_wt=6299
     Region          23..77
                     /region_name="Apelin"
                     /note="APJ endogenous ligand; pfam15360"
                     /db_xref="CDD:464670"
     mat_peptide     42..77
                     /product="apelin"
                     /calculated_mol_wt=4201
     Region          45..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R0R3.1)"
     Site            75
                     /site_type="other"
                     /note="Important for the balance between G(i) and
                     beta-arrestin pathways induced by apelin-13-APLNR system.
                     /evidence=ECO:0000250|UniProtKB:Q9ULZ1; propagated from
                     UniProtKB/Swiss-Prot (Q9R0R3.1)"
     Site            77
                     /site_type="other"
                     /note="Important for the balance between G(i) and
                     beta-arrestin pathways induced by apelin-13-APLNR system.
                     /evidence=ECO:0000250|UniProtKB:Q9ULZ1; propagated from
                     UniProtKB/Swiss-Prot (Q9R0R3.1)"
     CDS             1..77
                     /gene="Apln"
                     /gene_synonym="Apel"
                     /coded_by="NM_031612.3:341..574"
                     /db_xref="GeneID:58812"
                     /db_xref="RGD:620672"
ORIGIN      
        1 mnlsfcvqal lllwlsltav cgvplmlppd gkgleegnmr ylvkprtsrt gpgawqggrr
       61 kfrrqrprls hkgpmpf
//
LOCUS       NP_001119749             694 aa            linear   ROD 27-APR-2025
DEFINITION  outer dynein arm-docking complex subunit 1 [Rattus norvegicus].
ACCESSION   NP_001119749 XP_001080782 XP_218574
VERSION     NP_001119749.1
DBSOURCE    REFSEQ: accession NM_001126277.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hjeij,R., Onoufriadis,A., Watson,C.M., Slagle,C.E., Klena,N.T.,
            Dougherty,G.W., Kurkowiak,M., Loges,N.T., Diggle,C.P.,
            Morante,N.F., Gabriel,G.C., Lemke,K.L., Li,Y., Pennekamp,P.,
            Menchen,T., Konert,F., Marthin,J.K., Mans,D.A., Letteboer,S.J.,
            Werner,C., Burgoyne,T., Westermann,C., Rutman,A., Carr,I.M.,
            O'Callaghan,C., Moya,E., Chung,E.M., Sheridan,E., Nielsen,K.G.,
            Roepman,R., Bartscherer,K., Burdine,R.D., Lo,C.W., Omran,H. and
            Mitchison,H.M.
  CONSRTM   UK10K Consortium
  TITLE     CCDC151 mutations cause primary ciliary dyskinesia by disruption of
            the outer dynein arm docking complex formation
  JOURNAL   Am J Hum Genet 95 (3), 257-274 (2014)
   PUBMED   25192045
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Onoufriadis,A., Paff,T., Antony,D., Shoemark,A., Micha,D., Kuyt,B.,
            Schmidts,M., Petridi,S., Dankert-Roelse,J.E., Haarman,E.G.,
            Daniels,J.M., Emes,R.D., Wilson,R., Hogg,C., Scambler,P.J.,
            Chung,E.M., Pals,G. and Mitchison,H.M.
  CONSRTM   UK10K
  TITLE     Splice-site mutations in the axonemal outer dynein arm docking
            complex gene CCDC114 cause primary ciliary dyskinesia
  JOURNAL   Am J Hum Genet 92 (1), 88-98 (2013)
   PUBMED   23261303
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Knowles,M.R., Leigh,M.W., Ostrowski,L.E., Huang,L., Carson,J.L.,
            Hazucha,M.J., Yin,W., Berg,J.S., Davis,S.D., Dell,S.D.,
            Ferkol,T.W., Rosenfeld,M., Sagel,S.D., Milla,C.E., Olivier,K.N.,
            Turner,E.H., Lewis,A.P., Bamshad,M.J., Nickerson,D.A., Shendure,J.
            and Zariwala,M.A.
  CONSRTM   Genetic Disorders of Mucociliary Clearance Consortium
  TITLE     Exome sequencing identifies mutations in CCDC114 as a cause of
            primary ciliary dyskinesia
  JOURNAL   Am J Hum Genet 92 (1), 99-106 (2013)
   PUBMED   23261302
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC160835.1.
            
            On or before May 7, 2008 this sequence version replaced
            XP_218574.4, XP_001080782.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..694
                     /product="outer dynein arm-docking complex subunit 1"
                     /note="coiled-coil domain-containing protein 114;
                     coiled-coil domain containing 114"
                     /calculated_mol_wt=78040
     Region          24..>319
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          271..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1H228.1)"
     Region          531..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1H228.1)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B1H228.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B1H228.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B1H228.1)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B1H228.1)"
     Region          571..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1H228.1)"
     CDS             1..694
                     /gene="Odad1"
                     /gene_synonym="Ccdc114; RGD1308141"
                     /coded_by="NM_001126277.2:170..2254"
                     /db_xref="GeneID:308594"
                     /db_xref="RGD:1308141"
ORIGIN      
        1 mrlglssrsa rseegseifl egpvdgelsr lhrqrkvmel erraysrevh qrirkqveei
       61 rqlemlrakl qmqinvaqtq vkrlgdkkrl admdhllkcr aqvqieieal qeqnralekq
      121 iqdwethilt qskdistpdv ildqkmkiqr ririledqld rvtchfdihl vrnaalreel
      181 ellriergry lnmdrklkke ihllqemvga lstsstsayt areeaktkmg mlqeraekel
      241 aqsdteaqil lrqishleql hrflklknhd rqpdpgvvqk eeqrawetse glrktsqekl
      301 vlryedtlnk laqltgesdp dllvekylel eernfaefnf ineqnselyh lqeeikemqe
      361 alvsehasqd kqslereqqc kvlqqdvekv cseserlear fqvlrvqlek iktdiqvlfd
      421 kaqcdnsvik dllgvktymr drdiglflst iekrlvqllt vqaflevqnn vpladaalla
      481 lgqsiqeppk kttplkppdt medssgvvik ddypmskeel lsqvmklvql qdeegspkkr
      541 dsspsltlss prislaaasv harkasvvpe silshktgrg rgtgsishvt fgdsasapgp
      601 vtlastsasg lpvsgrgsqg grgafkhtss ssylgstgyl etsrgresgt ggghsqsmgs
      661 emsrgfssgs gqtssaapas rpssatskds rgyn
//
LOCUS       NP_001166897             210 aa            linear   ROD 27-APR-2025
DEFINITION  RNA binding protein, mRNA processing factor 2 [Rattus norvegicus].
ACCESSION   NP_001166897 XP_001076681 XP_578738
VERSION     NP_001166897.1
DBSOURCE    REFSEQ: accession NM_001173426.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nakagaki-Silva,E.E., Gooding,C., Llorian,M., Jacob,A.G.,
            Richards,F., Buckroyd,A., Sinha,S. and Smith,C.W.J.
  TITLE     Identification of RBPMS as a mammalian smooth muscle master
            splicing regulator via proximity of its gene with super-enhancers
  JOURNAL   Elife 8, e46327 (2019)
   PUBMED   31283468
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Sagnol,S., Yang,Y., Bessin,Y., Allemand,F., Hapkova,I.,
            Notarnicola,C., Guichou,J.F., Faure,S., Labesse,G. and de Santa
            Barbara,P.
  TITLE     Homodimerization of RBPMS2 through a new RRM-interaction motif is
            necessary to control smooth muscle plasticity
  JOURNAL   Nucleic Acids Res 42 (15), 10173-10184 (2014)
   PUBMED   25064856
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Piri,N., Kwong,J.M., Song,M. and Caprioli,J.
  TITLE     Expression of hermes gene is restricted to the ganglion cells in
            the retina
  JOURNAL   Neurosci Lett 405 (1-2), 40-45 (2006)
   PUBMED   16870336
  REMARK    GeneRIF: specific expression of hermes in retinal ganglion cells
            qualifies this gene as a potential RGC marker in the retina.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC169038.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_578738.3, XP_001076681.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..210
                     /product="RNA binding protein, mRNA processing factor 2"
                     /note="RNA binding protein with multiple splicing 2"
                     /calculated_mol_wt=22570
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFF2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZRY4; propagated from
                     UniProtKB/Swiss-Prot (B5DFF2.1)"
     Region          30..105
                     /region_name="RRM_RBPMS2"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing 2 (RBP-MS2);
                     cd12683"
                     /db_xref="CDD:410084"
     Region          41..51
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:Q6ZRY4"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFF2.1)"
     CDS             1..210
                     /gene="Rbpms2"
                     /gene_synonym="RGD1561222"
                     /coded_by="NM_001173426.1:145..777"
                     /db_xref="GeneID:503214"
                     /db_xref="RGD:1561222"
ORIGIN      
        1 msnlkpdveh ctgagtgtgt gpsgpleeev rtlfvsglpv dikprelyll frpfkgyegs
       61 likltsrqpv gfvifdsrag aeaaknalng irfdpenpqt lrlefakant kmakskliat
      121 pnptsvhpal gahliardpy dlmgaalipa speawapypl ytteltpais httftypaat
      181 aaaaaalhaq vrwypssdta qqgwkyrqfc
//
LOCUS       NP_001257494             397 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3C [Rattus norvegicus].
ACCESSION   NP_001257494
VERSION     NP_001257494.1
DBSOURCE    REFSEQ: accession NM_001270565.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, CB735595.1 and
            BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (3) is alternatively spliced at
            the 3' end compared to variant 1, and encodes a shorter isoform
            (H3C, also known as H3(397)) containing 7 transmembrane domains,
            but missing part of the third intracellular loop compared to
            isoform H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132293,
                              SAMD00132299 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..397
                     /product="histamine H3 receptor isoform H3C"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=44084
     Region          48..375
                     /region_name="7tmA_Histamine_H3R"
                     /note="histamine receptor subtypes H3R and H3R-like,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15296"
                     /db_xref="CDD:320423"
     Region          69..96
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320423"
     Region          107..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320423"
     Site            order(110,114..115,118..119,190,199,202..203,206,323,
                     326..327,330,346,350,354)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320423"
     Region          152..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320423"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320423"
     Region          303..333
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320423"
     Region          343..368
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320423"
     CDS             1..397
                     /gene="Hrh3"
                     /coded_by="NM_001270565.1:338..1531"
                     /note="isoform H3C is encoded by transcript variant 3"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhrgskpsa ssaslekrmk mvsqsitqrf
      301 rlsrdkkvak slaiivsifg lcwapytllm iiraachgrc ipdywyetsf wllwansavn
      361 pvlyplchys frraftkllc pqklkvqphg sleqcwk
//
LOCUS       NP_775149                 60 aa            linear   ROD 27-APR-2025
DEFINITION  small integral membrane protein 3 [Rattus norvegicus].
ACCESSION   NP_775149
VERSION     NP_775149.1
DBSOURCE    REFSEQ: accession NM_173126.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Vician,L., Silver,A.L., Farias-Eisner,R. and Herschman,H.R.
  TITLE     NID67, a small putative membrane protein, is preferentially induced
            by NGF in PC12 pheochromocytoma cells
  JOURNAL   J Neurosci Res 64 (2), 108-120 (2001)
   PUBMED   11288140
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070515.1, EV780394.1 and AF313411.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070515.1, EV780394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..60
                     /product="small integral membrane protein 3"
                     /note="NGF-induced differentiation clone 67 protein;
                     putative small membrane protein NID67"
                     /calculated_mol_wt=6437
     Region          1..60
                     /region_name="Smim3"
                     /note="Small integral membrane protein 3; pfam17307"
                     /db_xref="CDD:407417"
     Site            19..20
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:26479776;
                     propagated from UniProtKB/Swiss-Prot (Q99PE6.1)"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PE6.1)"
     CDS             1..60
                     /gene="Smim3"
                     /gene_synonym="Nid67"
                     /coded_by="NM_173126.3:357..539"
                     /db_xref="GeneID:286910"
                     /db_xref="RGD:628864"
ORIGIN      
        1 mdaisqspvd vllpkhildi waivliilat vvimtslflc pataviiyrm rthpvlngav
//
LOCUS       NP_001017375             851 aa            linear   ROD 27-APR-2025
DEFINITION  M-phase phosphoprotein 8 [Rattus norvegicus].
ACCESSION   NP_001017375 XP_001062459 XP_214173
VERSION     NP_001017375.2
DBSOURCE    REFSEQ: accession NM_001017375.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Liu,N., Lee,C.H., Swigut,T., Grow,E., Gu,B., Bassik,M.C. and
            Wysocka,J.
  TITLE     Selective silencing of euchromatic L1s revealed by genome-wide
            screens for L1 regulators
  JOURNAL   Nature 553 (7687), 228-232 (2018)
   PUBMED   29211708
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Tchasovnikarova,I.A., Timms,R.T., Douse,C.H., Roberts,R.C.,
            Dougan,G., Kingston,R.E., Modis,Y. and Lehner,P.J.
  TITLE     Hyperactivation of HUSH complex function by Charcot-Marie-Tooth
            disease mutation in MORC2
  JOURNAL   Nat Genet 49 (7), 1035-1044 (2017)
   PUBMED   28581500
REFERENCE   3  (residues 1 to 851)
  AUTHORS   Tchasovnikarova,I.A., Timms,R.T., Matheson,N.J., Wals,K.,
            Antrobus,R., Gottgens,B., Dougan,G., Dawson,M.A. and Lehner,P.J.
  TITLE     GENE SILENCING. Epigenetic silencing by the HUSH complex mediates
            position-effect variegation in human cells
  JOURNAL   Science 348 (6242), 1481-1485 (2015)
   PUBMED   26022416
REFERENCE   4  (residues 1 to 851)
  AUTHORS   Murata,K., Sato,S., Haruta,M., Goshima,T., Chiba,Y., Takahashi,S.,
            Sharif,J., Koseki,H., Nakanishi,M. and Shimada,M.
  TITLE     Physical interaction between MPP8 and PRC1 complex and its
            implication for regulation of spermatogenesis
  JOURNAL   Biochem Biophys Res Commun 458 (3), 470-475 (2015)
   PUBMED   25660450
  REMARK    GeneRIF: These results indicate that MPP8 could have a role for
            silencing genes that are associated with differentiation of the
            testis and the mesoderm by interacting with epigenetic repressors
            modules such as the PRC1 complex.
REFERENCE   5  (residues 1 to 851)
  AUTHORS   Kokura,K., Sun,L., Bedford,M.T. and Fang,J.
  TITLE     Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing
            and promotes tumour cell motility and invasion
  JOURNAL   EMBO J 29 (21), 3673-3687 (2010)
   PUBMED   20871592
REFERENCE   6  (residues 1 to 851)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB700328.1, BC099116.1 and BP474651.1.
            
            On Oct 27, 2010 this sequence version replaced NP_001017375.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..851
                     /product="M-phase phosphoprotein 8"
                     /EC_number="2.4.2.30"
                     /note="M-phase phosphoprotein, mpp8"
                     /calculated_mol_wt=96653
     Region          21..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          58..108
                     /region_name="CD_MMP8"
                     /note="chromodomain of M-phase phosphoprotein 8; cd18633"
                     /db_xref="CDD:349283"
     Site            order(58..61,80,83,89,91,95..96,98..102)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349283"
     Site            59
                     /site_type="other"
                     /note="Interaction with histone H3K9me3.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          80..87
                     /region_name="Histone H3K9me3 binding.
                     /evidence=ECO:0000250|UniProtKB:Q99549"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          <105..463
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          133..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          240..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          315..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99549; propagated from
                     UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          <534..715
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          591..620
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          594..622
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(597..598,601..603,605..606,610,613,622,624,626,
                     630..631,634..636,638..639,643,646,655,657,659,663..664,
                     667..669,671..672,676,679)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          624..655
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          624..653
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          657..686
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          657..686
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     Region          690..719
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8T1.1)"
     CDS             1..851
                     /gene="Mphosph8"
                     /gene_synonym="AABR07018038.3; Ab2-008; RGD1305133"
                     /coded_by="NM_001017375.2:71..2626"
                     /db_xref="GeneID:290270"
                     /db_xref="RGD:1305133"
ORIGIN      
        1 maaateenms vaalvmsvpd nigrspeveg ggaageekda atkgtvavgd seedgedvfe
       61 verildmkce ggknlykvrw kgytsdddtw epevhledck evllefrkkv aenkakavrk
      121 diqklslnnd ifeadsdidq qgdtkedtsp rkkkkkikyk edkspddlrk krakmgklkd
      181 kfktelests eilgfdvktk krilevkeel kdskkpkkde iketkktkra dirdlkikir
      241 edvkdnrktk keryidsple sespndsftl edesedflsd nkekqnvrta kdktgqdtvq
      301 esifekhldd lisieeagtr vrrkkkqprk feepkeikkl entnnflerk mipkkqrnqd
      361 kgrsnpelsk lpspvfaqtm kslrlsgeek glkssdlaee ekerknepke kyqkrydfdk
      421 eekarkepkg lksfkeirna fdlfkktaee kndlennskr eeisldykit hdnktkdkcs
      481 lreerntrde tdtwayiaae gdqevsdsvc qtdessdgkq pilslgmdlq lewmkledfq
      541 khldgedepf itanripsnl lrdavkngdy iavkvalnsn eeynldqeds tgmtlvmlaa
      601 aggqddllrl litkgakvng rqkngttali haaeknfltt vailleagaf vnvqqsnget
      661 almkackrgn sdivrlviec gadcnilskh qnsalyfakq cnnvlvyell kshletlsrv
      721 aeetirdyfe srlallepvf piachrlceg pdfstdfnym ppqnmpegsg vllfifhanf
      781 lgkdviarlc gpcsvqavvl ndkfqlpvfl dshfvysfsp vagpnklfir lteapfakvk
      841 lligayrvql q
//
LOCUS       NP_073176                341 aa            linear   ROD 27-APR-2025
DEFINITION  GTP-binding protein REM 2 [Rattus norvegicus].
ACCESSION   NP_073176
VERSION     NP_073176.2
DBSOURCE    REFSEQ: accession NM_022685.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Moore,A.R., Richards,S.E., Kenny,K., Royer,L., Chan,U.,
            Flavahan,K., Van Hooser,S.D. and Paradis,S.
  TITLE     Rem2 stabilizes intrinsic excitability and spontaneous firing in
            visual circuits
  JOURNAL   Elife 7, e33092 (2018)
   PUBMED   29809135
  REMARK    GeneRIF: Rem2 stabilizes intrinsic excitability and spontaneous
            firing in visual circuits.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Parent,C., Wen,X., Dhir,S.K., Ryan,R., Diorio,J. and Zhang,T.Y.
  TITLE     Maternal care associates with differences in morphological
            complexity in the medial preoptic area
  JOURNAL   Behav Brain Res 326, 22-32 (2017)
   PUBMED   28259675
  REMARK    GeneRIF: When rats become maternal, they increase the expression of
            Rem2 in the medial preoptic area which inhibits dendritic
            complexity and associates with an enhancement of maternal
            responsiveness.
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Ghiretti,A.E., Moore,A.R., Brenner,R.G., Chen,L.F., West,A.E.,
            Lau,N.C., Van Hooser,S.D. and Paradis,S.
  TITLE     Rem2 is an activity-dependent negative regulator of dendritic
            complexity in vivo
  JOURNAL   J Neurosci 34 (2), 392-407 (2014)
   PUBMED   24403140
  REMARK    GeneRIF: Rem2 is regulated at the transcriptional level by calcium
            influx and inhibits dendritic arborization in cultured rat cortical
            neurons
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Reymond,P., Coquard,A., Chenon,M., Zeghouf,M., El Marjou,A.,
            Thompson,A. and Menetrey,J.
  TITLE     Structure of the GDP-bound G domain of the RGK protein Rem2
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 68 (Pt 6), 626-631
            (2012)
   PUBMED   22684057
  REMARK    GeneRIF: structure of the Rem2 G domain bound to GDP is reported
            here in a monoclinic crystal form at 2.66 A resolution
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Flynn,R., Labrie-Dion,E., Bernier,N., Colicos,M.A., De Koninck,P.
            and Zamponi,G.W.
  TITLE     Activity-dependent subcellular cotrafficking of the small GTPase
            Rem2 and Ca2+/CaM-dependent protein kinase IIalpha
  JOURNAL   PLoS One 7 (7), e41185 (2012)
   PUBMED   22815963
  REMARK    GeneRIF: Rem2 has a role in neuronal plasticity hrough
            co-trafficking with CaMKIIa
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Ghiretti,A.E. and Paradis,S.
  TITLE     The GTPase Rem2 regulates synapse development and dendritic
            morphology
  JOURNAL   Dev Neurobiol 71 (5), 374-389 (2011)
   PUBMED   21485012
  REMARK    GeneRIF: our results suggest that Rem2 regulates dendritic
            branching and synapse development
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Correll,R.N., Botzet,G.J., Satin,J., Andres,D.A. and Finlin,B.S.
  TITLE     Analysis of the Rem2 - voltage dependant calcium channel beta
            subunit interaction and Rem2 interaction with phosphorylated
            phosphatidylinositide lipids
  JOURNAL   Cell Signal 20 (2), 400-408 (2008)
   PUBMED   18068949
  REMARK    GeneRIF: Voltage dependant calcium channels blockade by Rem2 is
            likely to be controlled by both the localized concentration of
            membrane phosphorylated phosphatidylinositide lipids and direct
            14-3-3 binding to the Rem2 C-terminus.
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Chen,H., Puhl,H.L. 3rd, Niu,S.L., Mitchell,D.C. and Ikeda,S.R.
  TITLE     Expression of Rem2, an RGK family small GTPase, reduces N-type
            calcium current without affecting channel surface density
  JOURNAL   J Neurosci 25 (42), 9762-9772 (2005)
   PUBMED   16237180
  REMARK    GeneRIF: Rem2 localizes to the plasma membrane via a C-terminal
            motif and interacts with calcium channel beta subunits in the
            preassembled N-type channel, thereby forming a nonconducting
            species.
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Finlin,B.S., Shao,H., Kadono-Okuda,K., Guo,N. and Andres,D.A.
  TITLE     Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related
            GTPases
  JOURNAL   Biochem J 347 Pt 1 (Pt 1), 223-231 (2000)
   PUBMED   10727423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB706504.1 and BC127495.1.
            
            On Sep 25, 2009 this sequence version replaced NP_073176.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127495.1, AY916790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132269, SAMD00132270
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..341
                     /product="GTP-binding protein REM 2"
                     /EC_number="3.6.5.2"
                     /note="GEM, REM, Kir family small G-protein; rad and
                     Gem-like GTP-binding protein 2; GTP-binding protein REM2;
                     rad and gem related GTP binding protein 2; Ras-related
                     GTP-binding protein of the Rad/Gem/Kir family, member 2;
                     RAS (RAD and GEM) like GTP binding 2"
                     /calculated_mol_wt=37144
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTY2.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WTY2.2)"
     Region          84..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTY2.2)"
     Region          116..341
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            122..129
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(123..124,172..173)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(124..130,170,173,230..231,233,260..261)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(129..130,142,144,153..154,167..168,170,172..173,262)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(143..144,151..154)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(143..148,150..153)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            145
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            170..173
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(172..173,182..185,188..191)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            230..233
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            260..262
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Region          282..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WTY2.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WTY2.2)"
     Site            335..338
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..341
                     /gene="Rem2"
                     /coded_by="NM_022685.2:85..1110"
                     /db_xref="GeneID:64626"
                     /db_xref="RGD:69081"
ORIGIN      
        1 mhtdldtdmd adtetvalcs sssrqaspsg tptpeadttl lkqkpeklla eldrggpppa
       61 pgvprrrgsm pvpykhqlrr aqavdeldwp pqasssgssd slgsgeaala qkdgvfkvml
      121 lgesgvgkst lagtfgglqg dnahemense dtyerrimvd keevtlivyd iweqgdaggw
      181 lqdhclqtgd aflivfsvtd rrsfskvpet llrlragrph hdlpvilvgn ksdlarsrev
      241 sleegrhlag tlsckhiets aalhhntrel fegavrqirl rrgrghaggq rpepsspdgp
      301 apptrreslt kkakrflanl vprnakffkq rsrschdlsv l
//
LOCUS       NP_665724                 95 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim13
            [Rattus norvegicus].
ACCESSION   NP_665724
VERSION     NP_665724.1
DBSOURCE    REFSEQ: accession NM_145781.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Wang,Z., Fan,M., Candas,D., Zhang,T.Q., Qin,L., Eldridge,A.,
            Wachsmann-Hogiu,S., Ahmed,K.M., Chromy,B.A., Nantajit,D., Duru,N.,
            He,F., Chen,M., Finkel,T., Weinstein,L.S. and Li,J.J.
  TITLE     Cyclin B1/Cdk1 coordinates mitochondrial respiration for cell-cycle
            G2/M progression
  JOURNAL   Dev Cell 29 (2), 217-232 (2014)
   PUBMED   24746669
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Roesch,K., Curran,S.P., Tranebjaerg,L. and Koehler,C.M.
  TITLE     Human deafness dystonia syndrome is caused by a defect in assembly
            of the DDP1/TIMM8a-TIMM13 complex
  JOURNAL   Hum Mol Genet 11 (5), 477-486 (2002)
   PUBMED   11875042
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Bauer,M.F., Rothbauer,U., Muhlenbein,N., Smith,R.J., Gerbitz,K.,
            Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     The mitochondrial TIM22 preprotein translocase is highly conserved
            throughout the eukaryotic kingdom
  JOURNAL   FEBS Lett 464 (1-2), 41-47 (1999)
   PUBMED   10611480
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and AF144701.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF144701.1, BG666646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..95
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim13"
                     /note="translocase of inner mitochondrial membrane 13
                     homolog"
                     /calculated_mol_wt=10327
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5L4; propagated from
                     UniProtKB/Swiss-Prot (P62076.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5L4; propagated from
                     UniProtKB/Swiss-Prot (P62076.1)"
     Region          24..86
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          46..69
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P62076.1)"
     CDS             1..95
                     /gene="Timm13"
                     /coded_by="NM_145781.2:36..323"
                     /db_xref="GeneID:252928"
                     /db_xref="RGD:628845"
ORIGIN      
        1 mdsgfgsdfg gtgggkldpg aimeqvkvqi avanaqellq rmtdkcfrkc igkpggsldn
       61 seqkciamcm drymdawntv sraynsrlqr eranm
//
LOCUS       NP_001257600             253 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 5 [Rattus norvegicus].
ACCESSION   NP_001257600
VERSION     NP_001257600.1
DBSOURCE    REFSEQ: accession NM_001270671.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (5) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215897.1, FQ217900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..253
                     /product="troponin T, fast skeletal muscle isoform 5"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29812
     Region          57..193
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..253
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270671.1:117..878"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eeaqeeevqe eapepeevqe eekprpklta pkipegekvd fddiqkkrqn
       61 kdlmelqali dshfearkke eeelialker iekrraerae qqriraeker erqnrlaeek
      121 arreeedakr raeddlkkkk alssmganys sylakadqkr gkkqtaremk kkilaerrkp
      181 lnidhlsddk lrdkakelwd tlyqletdkf efgeklkrqk ydittlrsri dqaqkhskka
      241 gatakgkvgg rwk
//
LOCUS       NP_001106880            1249 aa            linear   ROD 27-APR-2025
DEFINITION  ras/Rap GTPase-activating protein SynGAP isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001106880
VERSION     NP_001106880.2
DBSOURCE    REFSEQ: accession NM_001113409.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1249)
  AUTHORS   Katsanevaki,D., Till,S.M., Buller-Peralta,I., Nawaz,M.S.,
            Louros,S.R., Kapgal,V., Tiwari,S., Walsh,D., Anstey,N.J.,
            Petrovic,N.G., Cormack,A., Salazar-Sanchez,V., Harris,A.,
            Farnworth-Rowson,W., Sutherland,A., Watson,T.C., Dimitrov,S.,
            Jackson,A.D., Arkell,D., Biswal,S., Dissanayake,K.N., Mizen,L.A.M.,
            Perentos,N., Jones,M.W., Cousin,M.A., Booker,S.A., Osterweil,E.K.,
            Chattarji,S., Wyllie,D.J.A., Gonzalez-Sulser,A., Hardt,O.,
            Wood,E.R. and Kind,P.C.
  TITLE     Key roles of C2/GAP domains in SYNGAP1-related pathophysiology
  JOURNAL   Cell Rep 43 (9), 114733 (2024)
   PUBMED   39269903
  REMARK    GeneRIF: Key roles of C2/GAP domains in SYNGAP1-related
            pathophysiology.
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Qvist,J.S., Scherma,M., Jayaram-Lindstrom,N., Fratta,W.,
            Kandel,D.B., Kandel,E.R., Fadda,P. and Melas,P.A.
  TITLE     Synaptoproteomic Analysis of the Prefrontal Cortex Reveals
            Spatio-Temporal Changes in SYNGAP1 Following Cannabinoid Exposure
            in Rat Adolescence
  JOURNAL   Int J Mol Sci 24 (1), 698 (2022)
   PUBMED   36614142
  REMARK    GeneRIF: Synaptoproteomic Analysis of the Prefrontal Cortex Reveals
            Spatio-Temporal Changes in SYNGAP1 Following Cannabinoid Exposure
            in Rat Adolescence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Zeng,M., Shang,Y., Araki,Y., Guo,T., Huganir,R.L. and Zhang,M.
  TITLE     Phase Transition in Postsynaptic Densities Underlies Formation of
            Synaptic Complexes and Synaptic Plasticity
  JOURNAL   Cell 166 (5), 1163-1175 (2016)
   PUBMED   27565345
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   Codocedo,J.F., Montecinos-Oliva,C. and Inestrosa,N.C.
  TITLE     Wnt-related SynGAP1 is a neuroprotective factor of glutamatergic
            synapses against Abeta oligomers
  JOURNAL   Front Cell Neurosci 9, 227 (2015)
   PUBMED   26124704
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Song,B., Meng,F., Yan,X., Guo,J. and Zhang,G.
  TITLE     Cerebral ischemia immediately increases serine phosphorylation of
            the synaptic RAS-GTPase activating protein SynGAP by
            calcium/calmodulin-dependent protein kinase II alpha in hippocampus
            of rats
  JOURNAL   Neurosci Lett 349 (3), 183-186 (2003)
   PUBMED   12951199
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Kim,J.H., Lee,H.K., Takamiya,K. and Huganir,R.L.
  TITLE     The role of synaptic GTPase-activating protein in neuronal
            development and synaptic plasticity
  JOURNAL   J Neurosci 23 (4), 1119-1124 (2003)
   PUBMED   12598599
REFERENCE   7  (residues 1 to 1249)
  AUTHORS   Komiyama,N.H., Watabe,A.M., Carlisle,H.J., Porter,K.,
            Charlesworth,P., Monti,J., Strathdee,D.J., O'Carroll,C.M.,
            Martin,S.J., Morris,R.G., O'Dell,T.J. and Grant,S.G.
  TITLE     SynGAP regulates ERK/MAPK signaling, synaptic plasticity, and
            learning in the complex with postsynaptic density 95 and NMDA
            receptor
  JOURNAL   J Neurosci 22 (22), 9721-9732 (2002)
   PUBMED   12427827
REFERENCE   8  (residues 1 to 1249)
  AUTHORS   Li,W., Okano,A., Tian,Q.B., Nakayama,K., Furihata,T., Nawa,H. and
            Suzuki,T.
  TITLE     Characterization of a novel synGAP isoform, synGAP-beta
  JOURNAL   J Biol Chem 276 (24), 21417-21424 (2001)
   PUBMED   11278737
REFERENCE   9  (residues 1 to 1249)
  AUTHORS   Chen,H.J., Rojas-Soto,M., Oguni,A. and Kennedy,M.B.
  TITLE     A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by
            CaM kinase II
  JOURNAL   Neuron 20 (5), 895-904 (1998)
   PUBMED   9620694
  REMARK    Erratum:[Neuron 2002 Jan 3;33(1):151]
REFERENCE   10 (residues 1 to 1249)
  AUTHORS   Kim,J.H., Liao,D., Lau,L.F. and Huganir,R.L.
  TITLE     SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90
            protein family
  JOURNAL   Neuron 20 (4), 683-691 (1998)
   PUBMED   9581761
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Sep 11, 2009 this sequence version replaced NP_001106880.1.
            
            Summary: This gene encodes a Ras GTPase activating protein that is
            a member of the N-methyl-D-aspartate receptor complex. The
            N-terminal domain of the protein contains a Ras-GAP domain, a
            pleckstrin homology domain, and a C2 domain that may be involved in
            binding of calcium and phospholipids. The C-terminal domain
            consists of a ten histidine repeat region, serine and tyrosine
            phosphorylation sites, and a T/SXV motif required for postsynaptic
            scaffold protein interaction. The encoded protein negatively
            regulates Ras, Rap and
            alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor
            trafficking to the postsynaptic membrane to regulate synaptic
            plasticity and neuronal homeostasis. Homozygous null mutations in
            mice result in early post-embryonic lethality, while heterozygous
            mutant mice display a variety of phenotypes that include learning
            and memory defects, hyperactivity, and audiogenic seizures.
            [provided by RefSeq, Nov 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF058790.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..1249
                     /product="ras/Rap GTPase-activating protein SynGAP isoform
                     2"
                     /note="ras GTPase-activating protein SynGAP; p135 SynGAP;
                     neuronal RasGAP; synaptic Ras-GAP 1; ras/Rap
                     GTPase-activating protein SynGAP"
                     /calculated_mol_wt=137129
     Region          63..254
                     /region_name="PH_SynGAP"
                     /note="Synaptic Ras-GTPase activating protein Pleckstrin
                     homology (PH) domain; cd13375"
                     /db_xref="CDD:270178"
     Region          193..355
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          346..669
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(385,422,424,426..427,429,432,436,528,536..537,
                     540..541,544,565,568..569,572,576,578,583..584)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Region          659..1236
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     CDS             1..1249
                     /gene="Syngap1"
                     /gene_synonym="Syngap"
                     /coded_by="NM_001113409.3:183..3932"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:192117"
                     /db_xref="RGD:621090"
ORIGIN      
        1 mglrpptptp sggsgsgslp ppshrqplrr rcssccfpge yhlgrsrrks vpggkqysme
       61 aapaapfrps qgflsrrlks sikrtksqpk ldrtssfrqi lprfrsadhd rarlmqsfke
      121 shshesllsp ssaaealeln ldedsiikpv hssilgqefc fevttssgtk cfacrsaaer
      181 dkwienlqra vkpnkdnsrr vdnvlklwii earelppkkr yycelclddm lyarttskpr
      241 sasgdtvfwg ehfefnnlpa vralrlhlyr dsdkkrkkdk agyvglvtvp vatlagrhft
      301 eqwypvtlpt gsggsggmgs gggggsgggs ggkgkggcpa vrlkaryqtm silpmelyke
      361 faeyvtnhyr mlcavlepal nvkgkeevas alvhilqstg kakdflsdma msevdrfmer
      421 ehlifrentl atkaieeymr ligqkylkda igefiralye seencevdpi kctasslaeh
      481 qanlrmccel alckvvnshc vfpgelkevf aswrlrcaer grediadrli saslflrflc
      541 paimspslfg lmqeypdeqt srtltliakv iqnlanfskf tskedflgfm neflelewgs
      601 mqqflyeisn ldtltnsssf egyidlgrel stlhallwev lpqlskeall klgplprlls
      661 distalrnpn iqrqpsrqse rarsqpmvlr gpsaemqgym mrdlnssidl qsfmarglns
      721 smdmarlpsp tkekpppppp gggkdlfyvs rpplarsspa yctsssdite peqkmlsvnk
      781 svsmldlqgd gpggrlnsss vsnlaavgdl lhssqaslta alglrpapag rlsqgsgssi
      841 taagmrlsqm gvttdgvpaq qlriplsfqn plfhmaadgp gppaghggss ghgppsshhh
      901 hhhhhhhrgg eppgdtfapf hgysksedls tgvpkppaas ilhshsysde fgpsgtdftr
      961 rqlslqdnlq hmlsppqiti gpqrpapsgp gggsgggsgg ggggqppplq rgksqqltvs
     1021 aaqkprpssg nllqspepsy gparprqqsl skegsiggsg gsgggggggl kpsitkqhsq
     1081 tpstlnptmp asertvawvs nmphlsadie sahiereeyk lkeysksmde srldrvkeye
     1141 eeihslkerl hmsnrkleey errllsqeeq tskilmqyqa rleqsekrlr qqqvekdsqi
     1201 ksiigrlmlv eeelrrdhpa maeplpepkk rlldaqrgsf ppwvqqtrv
//
LOCUS       NP_942076                245 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane and ubiquitin-like domain-containing protein 1
            [Rattus norvegicus].
ACCESSION   NP_942076 XP_342614
VERSION     NP_942076.2
DBSOURCE    REFSEQ: accession NM_198781.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Lan,X., Li,G., Liu,H., Fu,H., Chen,P. and Liu,M.
  TITLE     MiR-27a/b Regulates Liver Regeneration by Posttranscriptional
            Modification of Tmub1
  JOURNAL   Dig Dis Sci 63 (9), 2362-2372 (2018)
   PUBMED   29777440
  REMARK    GeneRIF: MiR-27a/b regulates hepatocyte proliferation by
            controlling posttranscriptional modification of Tmub1 during liver
            regeneration.
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Lan,X., Fu,H., Li,G., Zeng,W., Lin,X., Zhu,Y., Liu,M. and Chen,P.
  TITLE     TMUB1 Inhibits BRL-3A Hepatocyte Proliferation by Interfering with
            the Binding of CAML to Cyclophilin B through its TM1 Hydrophobic
            Domain
  JOURNAL   Sci Rep 8 (1), 9917 (2018)
   PUBMED   29967478
  REMARK    GeneRIF: TMUB1 regulates hepatocyte proliferation by interacting
            with CAML and further interferes with the binding of CAML to
            cyclophilin B.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Fu,H., Xu,J., Chen,J., Li,G., Zhao,X. and Chen,P.
  TITLE     Microarray analysis reveals Tmub1 as a cell cycle-associated
            protein in rat hepatocytes
  JOURNAL   Mol Med Rep 17 (3), 4337-4344 (2018)
   PUBMED   29344642
  REMARK    GeneRIF: The transcriptional profile and potential biological
            processes affected by Tmub1 expression in hepatocytes have been
            reported.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Liu,M., Yuan,T., Liu,H. and Chen,P.
  TITLE     CCAAT/enhancer-binding protein beta regulates interleukin-6-induced
            transmembrane and ubiquitin-like domain containing 1 gene
            expression in hepatocytes
  JOURNAL   Mol Med Rep 10 (4), 2177-2183 (2014)
   PUBMED   25109894
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Castelli,M., Piobbico,D., Bartoli,D., Pieroni,S., Brunacci,C.,
            Bellet,M.M., Chiacchiaretta,M., Della Fazia,M.A. and Servillo,G.
  TITLE     Different functions of HOPS isoforms in the cell: HOPS shuttling
            isoform is determined by RIP cleavage system
  JOURNAL   Cell Cycle 13 (2), 293-302 (2014)
   PUBMED   24240191
  REMARK    GeneRIF: HOPS has distinct, isoform-specific functions in the
            nucleolus, nucleus, and cytoplasm.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Liu,M., Liu,H., Wang,X., Chen,P. and Chen,H.
  TITLE     IL-6 induction of hepatocyte proliferation through the
            Tmub1-regulated gene pathway
  JOURNAL   Int J Mol Med 29 (6), 1106-1112 (2012)
   PUBMED   22426572
  REMARK    GeneRIF: Tmub1 plays a negative role in IL-6-induced hepatocyte
            proliferation.
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Jo,Y., Sguigna,P.V. and DeBose-Boyd,R.A.
  TITLE     Membrane-associated ubiquitin ligase complex containing gp78
            mediates sterol-accelerated degradation of
            3-hydroxy-3-methylglutaryl-coenzyme A reductase
  JOURNAL   J Biol Chem 286 (17), 15022-15031 (2011)
   PUBMED   21343306
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Zhang,W., Savelieva,K.V., Suwanichkul,A., Small,D.L.,
            Kirkpatrick,L.L., Xu,N., Lanthorn,T.H. and Ye,G.L.
  TITLE     Transmembrane and ubiquitin-like domain containing 1 (Tmub1)
            regulates locomotor activity and wakefulness in mice and interacts
            with CAMLG
  JOURNAL   PLoS One 5 (6), e11261 (2010)
   PUBMED   20582322
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Yang,H., Takagi,H., Konishi,Y., Ageta,H., Ikegami,K., Yao,I.,
            Sato,S., Hatanaka,K., Inokuchi,K., Seog,D.H. and Setou,M.
  TITLE     Transmembrane and ubiquitin-like domain-containing protein 1
            (Tmub1/HOPS) facilitates surface expression of GluR2-containing
            AMPA receptors
  JOURNAL   PLoS One 3 (7), e2809 (2008)
   PUBMED   18665261
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Della Fazia,M.A., Castelli,M., Bartoli,D., Pieroni,S.,
            Pettirossi,V., Piobbico,D., Viola-Magni,M. and Servillo,G.
  TITLE     HOPS: a novel cAMP-dependent shuttling protein involved in protein
            synthesis regulation
  JOURNAL   J Cell Sci 118 (Pt 14), 3185-3194 (2005)
   PUBMED   16014383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DY313123.1 and
            JAXUCZ010000004.1.
            
            On Jan 13, 2007 this sequence version replaced NP_942076.1.
            
            Summary: The protein encoded by this gene belongs to a group of
            integral ubiquitin-like domain containing proteins that are
            involved in a range of cellular processes. In mouse, the protein
            exists in uncleaved transmembrane forms as well as a cleaved form
            that shuttles between the nucleus and cytoplasm. During liver
            regeneration in rat, it has been shown that the protein shuttles
            from the cytoplasm to the nucleus to inhibit hepatocyte
            proliferation. Homozygous null mutant mice display normal
            development and physiology but exhibit a strong increase in
            locomoter activity during the dark phase of the light:dark cycle,
            indicating a function in behavioral regulation. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2015].
            
            Transcript Variant: This variant (1) uses an alternate exon in the
            5' UTR compared to variant 2. Variants 1 and 2 encode the same
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY313123.1, BC059162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..245
                     /product="transmembrane and ubiquitin-like
                     domain-containing protein 1"
                     /note="hepatocyte odd protein shuttling protein"
                     /calculated_mol_wt=26218
     Region          2..30
                     /region_name="Required to release iHOPS from membranes.
                     /evidence=ECO:0000250|UniProtKB:Q9JMG3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Region          34..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Region          101..171
                     /region_name="Ubl_TMUB1"
                     /note="ubiquitin-like (Ubl) domain found in transmembrane
                     and ubiquitin-like domain-containing protein 1 (TMUB1);
                     cd17131"
                     /db_xref="CDD:340651"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            194..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     CDS             1..245
                     /gene="Tmub1"
                     /gene_synonym="Hops"
                     /coded_by="NM_198781.3:83..820"
                     /db_xref="GeneID:362301"
                     /db_xref="RGD:735120"
ORIGIN      
        1 maliegvgde vtvlfsvlac llvlalawvs thttestdpl pqssgtttpa qpseamtaid
       61 sireeapgae spslrhrgps aqpepeagvt astppdspqe plllrlkfln dseqvarawp
      121 qdtigslkrt qfpgreqqvr liyqgqllgd dtqtlgslhl ppncvlhchv strvgpphpp
      181 cppgsepgps gleigslllp lllllllllw ycqiqyrpff pltatlglag ftlllsllaf
      241 amyrp
//
LOCUS       NP_037317                524 aa            linear   ROD 27-APR-2025
DEFINITION  tyrosine-protein kinase HCK [Rattus norvegicus].
ACCESSION   NP_037317
VERSION     NP_037317.2
DBSOURCE    REFSEQ: accession NM_013185.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Wang,J., Chen,R., Liu,X., Shen,J., Yan,Y., Gao,Y., Tao,T. and
            Shi,J.
  TITLE     Hck Promotes Neuronal Apoptosis Following Intracerebral Hemorrhage
  JOURNAL   Cell Mol Neurobiol 37 (2), 251-261 (2017)
   PUBMED   27053350
  REMARK    GeneRIF: Hck was up-regulated in neurons adjacent to the hematoma
            after intracerebral hemorrhage.
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Mehlitz,A., Banhart,S., Maurer,A.P., Kaushansky,A., Gordus,A.G.,
            Zielecki,J., Macbeath,G. and Meyer,T.F.
  TITLE     Tarp regulates early Chlamydia-induced host cell survival through
            interactions with the human adaptor protein SHC1
  JOURNAL   J Cell Biol 190 (1), 143-157 (2010)
   PUBMED   20624904
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Paliwal,P., Radha,V. and Swarup,G.
  TITLE     Regulation of p73 by Hck through kinase-dependent and independent
            mechanisms
  JOURNAL   BMC Mol Biol 8, 45 (2007)
   PUBMED   17535448
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Huang,Z.Y., Barreda,D.R., Worth,R.G., Indik,Z.K., Kim,M.K.,
            Chien,P. and Schreiber,A.D.
  TITLE     Differential kinase requirements in human and mouse Fc-gamma
            receptor phagocytosis and endocytosis
  JOURNAL   J Leukoc Biol 80 (6), 1553-1562 (2006)
   PUBMED   16921024
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Cougoule,C., Carreno,S., Castandet,J., Labrousse,A.,
            Astarie-Dequeker,C., Poincloux,R., Le Cabec,V. and
            Maridonneau-Parini,I.
  TITLE     Activation of the lysosome-associated p61Hck isoform triggers the
            biogenesis of podosomes
  JOURNAL   Traffic 6 (8), 682-694 (2005)
   PUBMED   15998323
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Howlett,C.J., Bisson,S.A., Resek,M.E., Tigley,A.W. and Robbins,S.M.
  TITLE     The proto-oncogene p120(Cbl) is a downstream substrate of the Hck
            protein-tyrosine kinase
  JOURNAL   Biochem Biophys Res Commun 257 (1), 129-138 (1999)
   PUBMED   10092522
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Robbins,S.M., Quintrell,N.A. and Bishop,J.M.
  TITLE     Myristoylation and differential palmitoylation of the HCK
            protein-tyrosine kinases govern their attachment to membranes and
            association with caveolae
  JOURNAL   Mol Cell Biol 15 (7), 3507-3515 (1995)
   PUBMED   7791757
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Lowell,C.A., Soriano,P. and Varmus,H.E.
  TITLE     Functional overlap in the src gene family: inactivation of hck and
            fgr impairs natural immunity
  JOURNAL   Genes Dev 8 (4), 387-398 (1994)
   PUBMED   8125254
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Okano,Y., Sugimoto,Y., Fukuoka,M., Matsui,A., Nagata,K. and
            Nozawa,Y.
  TITLE     Identification of rat cDNA encoding hck tyrosine kinase from
            megakaryocytes
  JOURNAL   Biochem Biophys Res Commun 181 (3), 1137-1144 (1991)
   PUBMED   1764064
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Lock,P., Ralph,S., Stanley,E., Boulet,I., Ramsay,R. and Dunn,A.R.
  TITLE     Two isoforms of murine hck, generated by utilization of alternative
            translational initiation codons, exhibit different patterns of
            subcellular localization
  JOURNAL   Mol Cell Biol 11 (9), 4363-4370 (1991)
   PUBMED   1875927
  REMARK    GeneRIF: Alternate protein isoforms arise through the use of a
            non-AUG (CUG), and a downstream in-frame AUG translation initiation
            codons, in mouse and human. Same is likely true for rat as there is
            strong sequence conservation amongst different species.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078890.1.
            
            On Sep 15, 2003 this sequence version replaced NP_037317.1.
            
            Summary: The protein encoded by this gene is a protein-tyrosine
            kinase that is predominantly expressed in hemopoietic cell
            types.The encoded protein may help couple the Fc receptor to the
            activation of the respiratory burst. In addition, it may play a
            role in neutrophil migration and in the degranulation of
            neutrophils. Alternate translation initiation site usage, including
            a non-AUG (CUG) codon, results in the production of two different
            isoforms in human and mouse. Based on strong sequence conservation
            amongst these species, this may also be true for rat. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078890.1, M83666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 10967098, 1875927
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..524
                     /product="tyrosine-protein kinase HCK"
                     /EC_number="2.7.10.2"
                     /note="p56-HCK; hemopoietic cell tyrosine kinase;
                     hematopoietic cell kinase; hemopoietic cell kinase"
                     /calculated_mol_wt=59023
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50545.4)"
     Region          22
                     /region_name="alternative AUG translation initiation site"
     Region          35..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50545.4)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P08631; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     Region          80..135
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(85,87,90,94,111..112,127,129..130)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          138..241
                     /region_name="SH2_Src_HCK"
                     /note="Src homology 2 (SH2) domain found in HCK; cd10363"
                     /db_xref="CDD:198226"
     Site            order(149,169,171..174,179,195,197,209..211,230)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198226"
     Site            order(149,169,195,197)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198226"
     Site            order(196,224)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198226"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08631; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08103; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     Region          252..522
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(266..269,272,274,286,288,316,331..334,379,383..384,
                     386,396..397)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P08631; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08631; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08631; propagated from
                     UniProtKB/Swiss-Prot (P50545.4)"
     CDS             1..524
                     /gene="Hck"
                     /gene_synonym="Hctk; p56Hck; p59Hck"
                     /coded_by="NM_013185.3:199..1773"
                     /note="non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:25734"
                     /db_xref="RGD:2785"
ORIGIN      
        1 mggrsscedp gcprgegrvp rmgcvksrfl regskaskie pnanqkgpvy vpdptspkkl
       61 gpnsinslpp gvvegsedti vvalydyeai hredlsfqkg dqmvvleesg ewwkarslat
      121 kkegyipsny varvnslete ewffkgisrk daerhllapg nmlgsfmird settkgsysl
      181 svrdfdpqhg dtvkhykirt ldsggfyisp rstfsslqel vvhykkgkdg lcqklsvpcv
      241 spkpqkpwek daweipresl qmekklgagq fgevwmatyn khtkvavktm kpgsmsveaf
      301 laeanlmktl qhdklvklha vvsqepifiv tefmakgsll dflkseegsk qplpklidfs
      361 aqisegmafi eqrnyihrdl raanilvsas lvckiadfgl ariiedneyt aregakfpik
      421 wtapeainfg sftiksdvws fgillmeivt ygripypgms npeviraleh gyrmprpdnc
      481 peelysimir cwknrpeerp tfeyiqsvld dfytatesqy qqqp
//
LOCUS       NP_445753                360 aa            linear   ROD 27-APR-2025
DEFINITION  hereditary hemochromatosis protein homolog isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_445753
VERSION     NP_445753.1
DBSOURCE    REFSEQ: accession NM_053301.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Tamosauskaite,J., Atkins,J.L., Pilling,L.C., Kuo,C.L., Kuchel,G.A.,
            Ferrucci,L. and Melzer,D.
  TITLE     Hereditary Hemochromatosis Associations with Frailty, Sarcopenia
            and Chronic Pain: Evidence from 200,975 Older UK Biobank
            Participants
  JOURNAL   J Gerontol A Biol Sci Med Sci 74 (3), 337-342 (2019)
   PUBMED   30657865
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Smith,D.J., Klein,K., Hartel,G., Wainwright,C.E., Bell,S.C.,
            Anderson,G.J. and Reid,D.W.
  TITLE     Mutations in the HFE gene can be associated with increased lung
            disease severity in cystic fibrosis
  JOURNAL   Gene 683, 12-17 (2019)
   PUBMED   30291871
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Pilling,L.C., Tamosauskaite,J., Jones,G., Wood,A.R., Jones,L.,
            Kuo,C.L., Kuchel,G.A., Ferrucci,L. and Melzer,D.
  TITLE     Common conditions associated with hereditary haemochromatosis
            genetic variants: cohort study in UK Biobank
  JOURNAL   BMJ 364, k5222 (2019)
   PUBMED   30651232
  REMARK    Erratum:[BMJ. 2019 Oct 23;367:l6157. doi: 10.1136/bmj.l6157. PMID:
            31645331]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Frydlova,J., Rogalsky,D.W., Truksa,J., Traeger,L.,
            Steinbicker,A.U., Vokurka,M. and Krijt,J.
  TITLE     Liver HFE protein content is posttranscriptionally decreased in
            iron-deficient mice and rats
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 315 (4), G560-G568 (2018)
   PUBMED   29927322
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Lee,N.P., Wu,H., Ng,K.T.P., Luo,R., Lam,T.W., Lo,C.M. and Man,K.
  TITLE     Transcriptome Analysis of Acute Phase Liver Graft Injury in Liver
            Transplantation
  JOURNAL   Biomedicines 6 (2), 41 (2018)
   PUBMED   29642405
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Sanchez,M., Queralt,R., Bruguera,M., Rodes,J. and Oliva,R.
  TITLE     Cloning, sequencing and characterization of the rat hereditary
            hemochromatosis promoter: comparison of the human, mouse and rat
            HFE promoter regions
  JOURNAL   Gene 225 (1-2), 77-87 (1998)
   PUBMED   9931446
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Lebron,J.A., Bennett,M.J., Vaughn,D.E., Chirino,A.J., Snow,P.M.,
            Mintier,G.A., Feder,J.N. and Bjorkman,P.J.
  TITLE     Crystal structure of the hemochromatosis protein HFE and
            characterization of its interaction with transferrin receptor
  JOURNAL   Cell 93 (1), 111-123 (1998)
   PUBMED   9546397
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Feder,J.N., Penny,D.M., Irrinki,A., Lee,V.K., Lebron,J.A.,
            Watson,N., Tsuchihashi,Z., Sigal,E., Bjorkman,P.J. and
            Schatzman,R.C.
  TITLE     The hemochromatosis gene product complexes with the transferrin
            receptor and lowers its affinity for ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1472-1477 (1998)
   PUBMED   9465039
REFERENCE   9  (residues 1 to 360)
  AUTHORS   George,D.K., Goldwurm,S., MacDonald,G.A., Cowley,L.L., Walker,N.I.,
            Ward,P.J., Jazwinska,E.C. and Powell,L.W.
  TITLE     Increased hepatic iron concentration in nonalcoholic
            steatohepatitis is associated with increased fibrosis
  JOURNAL   Gastroenterology 114 (2), 311-318 (1998)
   PUBMED   9453491
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Feder,J.N., Gnirke,A., Thomas,W., Tsuchihashi,Z., Ruddy,D.A.,
            Basava,A., Dormishian,F., Domingo,R. Jr., Ellis,M.C., Fullan,A.,
            Hinton,L.M., Jones,N.L., Kimmel,B.E., Kronmal,G.S., Lauer,P.,
            Lee,V.K., Loeb,D.B., Mapa,F.A., McClelland,E., Meyer,N.C.,
            Mintier,G.A., Moeller,N., Moore,T., Morikang,E., Prass,C.E.,
            Quintana,L., Starnes,S.M., Schatzman,R.C., Brunke,K.J.,
            Drayna,D.T., Risch,N.J., Bacon,B.R. and Wolff,R.K.
  TITLE     A novel MHC class I-like gene is mutated in patients with
            hereditary haemochromatosis
  JOURNAL   Nat Genet 13 (4), 399-408 (1996)
   PUBMED   8696333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ001517.1, SRR22582416.1465363.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..360
                     /product="hereditary hemochromatosis protein homolog
                     isoform 1 precursor"
                     /note="hereditary hemochromatosis protein homolog;
                     RT1-CAFE"
                     /calculated_mol_wt=38233
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2774
     mat_peptide     26..360
                     /product="Hereditary hemochromatosis protein homolog.
                     /id=PRO_0000018895"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
                     /calculated_mol_wt=38233
     Region          26..127
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
     Region          31..215
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35799.1)"
     Region          128..218
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35799.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35799.1)"
     Region          217..310
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          219..310
                     /region_name="Alpha-3"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
     Region          234..238
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35799.1)"
     Region          249..253
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          281..285
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          292..297
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          307..310
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          311..319
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35799.1)"
     CDS             1..360
                     /gene="Hfe"
                     /coded_by="NM_053301.4:81..1163"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29199"
                     /db_xref="RGD:2793"
ORIGIN      
        1 mdrsaglpvr llllllllll wsvapqalrp gshslrylfm gaskpdlglp ffealgyvdd
       61 qlfvsynhes rraeprapwi lgqtssqlwl qlsqslkgwd ymfivdfwti mgnynhskvt
      121 klrvvpeshi lqvilgcevh ednstsgfwk ygydgqdhle fcpktlnwsa aeprawatkm
      181 eweehrirar qsrdylqrdc pqqlkqvlel qrgvlgqqvp tlvkvtrhwa stgtslrcqa
      241 lnffpqnitm rwlkdsqpld akdvnpenvl pngdgtyqgw ltlavapgee trfscqvehp
      301 gldqpltatw epsrsqdmii giisgitica iffvgililv lrkrkvsggt mgdyvltece
//
LOCUS       NP_001164031            1621 aa            linear   ROD 27-APR-2025
DEFINITION  versican core protein isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001164031
VERSION     NP_001164031.1
DBSOURCE    REFSEQ: accession NM_001170560.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1621)
  AUTHORS   Harten,I.A., Kaber,G., Agarwal,K.J., Kang,I., Ibarrientos,S.R.,
            Workman,G., Chan,C.K., Nivison,M.P., Nagy,N., Braun,K.R.,
            Kinsella,M.G., Merrilees,M.J. and Wight,T.N.
  TITLE     The synthesis and secretion of versican isoform V3 by mammalian
            cells: A role for N-linked glycosylation
  JOURNAL   Matrix Biol 89, 27-42 (2020)
   PUBMED   32001344
  REMARK    GeneRIF: The synthesis and secretion of versican isoform V3 by
            mammalian cells: A role for N-linked glycosylation.
REFERENCE   2  (residues 1 to 1621)
  AUTHORS   Bogen,O., Bender,O., Alvarez,P., Kern,M., Tomiuk,S., Hucho,F. and
            Levine,J.D.
  TITLE     Expression of a novel versican variant in dorsal root ganglia from
            spared nerve injury rats
  JOURNAL   Mol Pain 15, 1744806919874557 (2019)
   PUBMED   31429356
  REMARK    GeneRIF: mRNAs of the versican gene with exon 8beta are predicted
            to be constitutively degraded by nonsense-mediated RNA decay.
REFERENCE   3  (residues 1 to 1621)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   4  (residues 1 to 1621)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 1621)
  AUTHORS   Carthy,J.M., Abraham,T., Meredith,A.J., Boroomand,S. and
            McManus,B.M.
  TITLE     Versican localizes to the nucleus in proliferating mesenchymal
            cells
  JOURNAL   Cardiovasc Pathol 24 (6), 368-374 (2015)
   PUBMED   26395512
  REMARK    GeneRIF: Versican localizes to the nucleus in proliferating
            mesenchymal cells and suggest role in mitotic spindle organization
            during cell division.
REFERENCE   6  (residues 1 to 1621)
  AUTHORS   Lemire,J.M., Merrilees,M.J., Braun,K.R. and Wight,T.N.
  TITLE     Overexpression of the V3 variant of versican alters arterial smooth
            muscle cell adhesion, migration, and proliferation in vitro
  JOURNAL   J Cell Physiol 190 (1), 38-45 (2002)
   PUBMED   11807809
  REMARK    GeneRIF: Overexpression of alternatively spliced V3 variant of
            versican alters arterial smooth muscle cell adhesion, migration,
            proliferation and cell shape
REFERENCE   7  (residues 1 to 1621)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
REFERENCE   8  (residues 1 to 1621)
  AUTHORS   Mjaatvedt,C.H., Yamamura,H., Capehart,A.A., Turner,D. and
            Markwald,R.R.
  TITLE     The Cspg2 gene, disrupted in the hdf mutant, is required for right
            cardiac chamber and endocardial cushion formation
  JOURNAL   Dev Biol 202 (1), 56-66 (1998)
   PUBMED   9758703
REFERENCE   9  (residues 1 to 1621)
  AUTHORS   Milev,P., Maurel,P., Chiba,A., Mevissen,M., Popp,S., Yamaguchi,Y.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Differential regulation of expression of hyaluronan-binding
            proteoglycans in developing brain: aggrecan, versican, neurocan,
            and brevican
  JOURNAL   Biochem Biophys Res Commun 247 (2), 207-212 (1998)
   PUBMED   9642104
REFERENCE   10 (residues 1 to 1621)
  AUTHORS   Pyke,C., Kristensen,P., Ostergaard,P.B., Oturai,P.S. and Romer,J.
  TITLE     Proteoglycan expression in the normal rat kidney
  JOURNAL   Nephron 77 (4), 461-470 (1997)
   PUBMED   9434070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF072892.1, JAXUCZ010000002.1, AF062402.1 and AY007691.1.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform 3, also referred to as V2), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data from several strains because no single
            transcript was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments and
            orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1475727.1,
                                           SRR26360194.2106605.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Rattus norvegicus"
                     /strain="WKY"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..1621
                     /product="versican core protein isoform 3 precursor"
                     /note="versican core protein; GHAP; PG-M; large fibroblast
                     proteoglycan; glial hyaluronate-binding protein;
                     chondroitin sulfate proteoglycan core protein 2;
                     chondroitin sulfate proteoglycan 2 (versican)"
                     /calculated_mol_wt=176918
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          <766..1193
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          1316..1350
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1352..1388
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1352,1355,1369)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1394..1517
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Site            order(1412,1444..1447,1476,1486,1494,1496,1502,1505,
                     1507..1509)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Site            order(1455,1459,1482,1488..1489)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(1459,1489)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(1479,1481,1488,1502..1503)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Region          1521..1577
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(1531,1551)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..1621
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
                     /coded_by="NM_001170560.1:281..5146"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:114122"
                     /db_xref="RGD:619940"
ORIGIN      
        1 mlinmngilw mcstllltha lhkakmeenp pvkgslsgkv ilpchfstlp tlppdyntse
       61 flrikwskie vdkngkdike ttvlvaqdgn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdagvyrc dvmygiedtq ntmslavdgv vfhyraatsr ytlnfesaqq acldigavia
      181 tpeqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec anrdarlatv gelhaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkpkq niseattiet
      361 ntlaetasps lskephmvpe ratpviplvt elpiftthfp pagnivnseq ksviysqait
      421 drvatespta agspinswda ddylpsgsgp lgkpdiseik eeglqsttvt sqhatashhg
      481 itedtqthes vtqieqievg plvtsmeitn hisfkeflet ktplestevt leqhqtdmpt
      541 vitspelatt shygvtlred dredialtvr sgqstrvfsq ipevitvskt sedttysqlg
      601 dlefvstati tmlgtdgslt degkepqtdd ktaedefgqs qptipfpsqh lteveslpys
      661 gdtisveris tvsypslqtd vtqgrertev prpglkkdpy avdeiqekit kdpfigtiee
      721 gfsgmslsts ssetsaerte svspaltiek ltvkpavasd vdemtiltrl etdvptsded
      781 vtsahlthst lnvevvtvlk wpgnednsts kplppterag ftksppvsls tvgivgkdke
      841 tpsftdggde ytlsldgtpk plekfseedl tsgefavtip tsisidsaek stlgepttgd
      901 rvlsttstkd lvinatvegs aldedmdask plftatpfvh tsdveesafv nysstqqptt
      961 yvdishtspl siipktewsv setsvplede vlgksdqdtl eqthleatms pealstievt
     1021 qgetqeepqt pgipfpalss tavmtketta feeegegsty tlsedrlmtd seivpslett
     1081 pvgtsypgga mtqqgvemdt mvtqmssirp tvvlstepev syeaegsspm efastlkpfg
     1141 tqvtqlveet teegkktpld ytdlgsglfe qprvtelpdf smtpsdisvf taidslhrtt
     1201 plrppspfte ephifekeps ekttgdiilp resvtqhplt tlmdiiakkt esdidheyhm
     1261 tskppvmqpt rpsvverktt skpqelstss ppagtkfhpd invyiievre nktgpdlckt
     1321 npclnggtcy ptetsyvctc apgysgdqce ldfdechsnp crngatcvdg lntfrclclp
     1381 syvgalceqd tetcdygwhk fqgqcykyfa hrrtwdaaer ecrlqgahlt silsheeqmf
     1441 vnrvghdyqw iglndkmfeh dfrwtdgsal qyenwrpnqp dsffsagedc vviiwhengq
     1501 wndvpcnyhl tytckkgtva cgqppvvena ktfgkmkpry einsliryhc kdgfiqrhlp
     1561 tirclgngrw ampkitcmnp sayqrtyskk ylknsssvkd nsintskheh rwsrrwqetr
     1621 r
//
LOCUS       NP_001291281             984 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 4 [Rattus
            norvegicus].
ACCESSION   NP_001291281 XP_006220766 XP_006246905
VERSION     NP_001291281.1
DBSOURCE    REFSEQ: accession NM_001304352.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Sasai,N., Nakao,M. and Defossez,P.A.
  TITLE     Sequence-specific recognition of methylated DNA by human
            zinc-finger proteins
  JOURNAL   Nucleic Acids Res 38 (15), 5015-5022 (2010)
   PUBMED   20403812
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Yamada,D., Perez-Torrado,R., Filion,G., Caly,M., Jammart,B.,
            Devignot,V., Sasai,N., Ravassard,P., Mallet,J., Sastre-Garau,X.,
            Schmitz,M.L. and Defossez,P.A.
  TITLE     The human protein kinase HIPK2 phosphorylates and downregulates the
            methyl-binding transcription factor ZBTB4
  JOURNAL   Oncogene 28 (27), 2535-2544 (2009)
   PUBMED   19448668
REFERENCE   4  (residues 1 to 984)
  AUTHORS   Filion,G.J., Zhenilo,S., Salozhin,S., Yamada,D., Prokhortchouk,E.
            and Defossez,P.A.
  TITLE     A family of human zinc finger proteins that bind methylated DNA and
            repress transcription
  JOURNAL   Mol Cell Biol 26 (1), 169-181 (2006)
   PUBMED   16354688
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Jan 21, 2015 this sequence version replaced
            XP_006246905.1, XP_006220766.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript was available for the full length
            of the gene. The extent of this transcript is supported by
            transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.35546.1,
                                           SRR26360194.1527943.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..984
                     /product="zinc finger and BTB domain-containing protein 4"
                     /calculated_mol_wt=103079
     Region          12..160
                     /region_name="BTB_POZ_ZBTB4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 4 (ZBTB4); cd18195"
                     /db_xref="CDD:349504"
     Region          71..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          165..324
                     /region_name="Interaction with CBFA2T3.
                     /evidence=ECO:0000250|UniProtKB:Q9P1Z0"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          172..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          211..233
                     /region_name="zf-C2HC_2"
                     /note="zinc-finger of a C2HC-type; pfam13913"
                     /db_xref="CDD:464037"
     Region          212..228
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          227..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(292,294,296,298..299,302..303,306,320,322,326..327,
                     330..331,334,348,350,352,354..355,358..359)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P1Z0; propagated from
                     UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          461..575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          593..696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          701..719
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          713..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          736..758
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          738..758
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          756..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q9P1Z0; propagated from
                     UniProtKB/Swiss-Prot (D4A8X0.1)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q9P1Z0; propagated from
                     UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          853..876
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Region          947..984
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8X0.1)"
     Site            955
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2.
                     /evidence=ECO:0000250|UniProtKB:Q9P1Z0; propagated from
                     UniProtKB/Swiss-Prot (D4A8X0.1)"
     CDS             1..984
                     /gene="Zbtb4"
                     /coded_by="NM_001304352.1:260..3214"
                     /db_xref="GeneID:287441"
                     /db_xref="RGD:1307184"
ORIGIN      
        1 mpppaevtdp shapavlrql neqrlrglfc dvtliagdtk fpahrsvlaa sspffreall
       61 asaplplppv tggsapspat ttaasssssp pppasphsss pprvlelpgv paaafsdvln
      121 fiysarlalp ggggdgaava eigalgrrlg isrlqglgeg gdtwvppaps smvtsepned
      181 slgpglrtdg gwegdkaepl tpdsqprrpf pcprcgksfi hpkrlqthea qcrrgsntrg
      241 saglgpggsg pggpagvdas alpqpvsfrd gpehvvkvvg ghvlyvcaac ersyvtlssl
      301 krhsnvhswr rkypcrycek vfalaeyrtk hevwhtgerr yqcifcwetf vtyynlkthq
      361 rafhgispgl lasektpngg ykpklntlkl yrllpmraak rpyktysqga peaplspslh
      421 tpvpavmpas pqpllpsvpe pgpphsvitf ahpapsvivh gssssgaagg gpvgtggsqa
      481 asvityttpp rppkkreypp pppepaatpt spastavipa taagpatate eakgrnlrag
      541 rtltytakpv ggvsgsggsp tgtgrgssql qappplcqit vrigeeaivk rrisetdlrp
      601 gelsgeevee seeeeeeeee edqedqeesk aggedqlwrp yysykpkrka gatasglsgl
      661 prgrrpprwr qklerrgwee tpavegpggr grgerrhrcg dcaqafatlr klrkhqeahs
      721 ggshnsrtgr rsstrftcph cakvcktaaa lnrhgqrhav erpggtptpv iayskgsigt
      781 rptdvkeeap qemqvssssg eagggsaaaa aaeasesasl qdpvisggee ppvaggggyv
      841 yppvqefpla liggsrdpga gkgkpgnegp vgasegnrme emgtakvtfy pepyplvygp
      901 qllaaypynf snlaalpval nmvlpdekgg galpflpgvf gyavnpqtap ptpptppppl
      961 plpvppkgvg emtgvertqk gdvg
//
LOCUS       NP_001004278             578 aa            linear   ROD 27-APR-2025
DEFINITION  testis-specific protein 10-interacting protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001004278 XP_341992
VERSION     NP_001004278.2
DBSOURCE    REFSEQ: accession NM_001004278.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC097254.1.
            
            On Oct 31, 2005 this sequence version replaced NP_001004278.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..578
                     /product="testis-specific protein 10-interacting protein
                     isoform 1"
                     /note="fibrous sheath protein; testis-specific protein
                     10-interacting protein; tsga10-interacting protein"
                     /calculated_mol_wt=64356
     CDS             1..578
                     /gene="Tsga10ip"
                     /coded_by="NM_001004278.3:39..1775"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361707"
                     /db_xref="RGD:1302964"
ORIGIN      
        1 mlntdqllvr aiserprkst eplvpgtptg lfsllsnisp eeqgrlgsgd slqsqscqqq
       61 rsysagqttk kerkprrrnk kgrgsaeaed lfssprkpsf pfqwawesfi idgqallqsg
      121 ssvavghrsl lfppaapqck trhksvanls edlrachkse vqnlgrryqp gawanlslpl
      181 gkaesqgler ptfwstgkgs gsecedvsev egqnadeaek slstgelpql pgqgltleee
      241 lisevmeeee hnrrkgssvn kgrnsgekgs eegelqshnq gsssnsnslr kspkgtsgak
      301 efkgpwdler lhrqlqeele sgpqkqtwka lraavqasar nrktpvtgee esfltanfpn
      361 rtfhkrqeat rtwalrdtyf fpqsltsgph appcylglpr apdphghppf ltrnllqawe
      421 qqqlkekqqa emrrareqqv qqqvarclaa ytpggnrgtl gpqrkleelr rkerqrfaey
      481 qaelqgiqhr vqarpflfqq amqtnarlta nrrfsqvlsa lgvdeeqlla eagnaegipr
      541 khrsyrsfgv emesspqspp kteptssqpg rhpsptld
//
LOCUS       NP_446224                 76 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor alpha [Rattus norvegicus].
ACCESSION   NP_446224
VERSION     NP_446224.1
DBSOURCE    REFSEQ: accession NM_053772.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Vetter,M.M., Zenn,H.M., Mendez,E., van den Boom,H., Herberg,F.W.
            and Skalhegg,B.S.
  TITLE     The testis-specific Calpha2 subunit of PKA is kinetically
            indistinguishable from the common Calpha1 subunit of PKA
  JOURNAL   BMC Biochem 12, 40 (2011)
   PUBMED   21812984
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Collins,S.P. and Uhler,M.D.
  TITLE     Characterization of PKIgamma, a novel isoform of the protein kinase
            inhibitor of cAMP-dependent protein kinase
  JOURNAL   J Biol Chem 272 (29), 18169-18178 (1997)
   PUBMED   9218452
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Wen,W., Taylor,S.S. and Meinkoth,J.L.
  TITLE     The expression and intracellular distribution of the heat-stable
            protein kinase inhibitor is cell cycle regulated
  JOURNAL   J Biol Chem 270 (5), 2041-2046 (1995)
   PUBMED   7836431
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Baude,E.J., Dignam,S.S., Olsen,S.R., Reimann,E.M. and Uhler,M.D.
  TITLE     Glutamic acid 203 of the cAMP-dependent protein kinase catalytic
            subunit participates in the inhibition by two isoforms of the
            protein kinase inhibitor
  JOURNAL   J Biol Chem 269 (3), 2316-2323 (1994)
   PUBMED   7905001
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Van Patten,S.M., Howard,P., Walsh,D.A. and Maurer,R.A.
  TITLE     The alpha- and beta-isoforms of the inhibitor protein of the
            3',5'-cyclic adenosine monophosphate-dependent protein kinase:
            characteristics and tissue- and developmental-specific expression
  JOURNAL   Mol Endocrinol 6 (12), 2114-2122 (1992)
   PUBMED   1491692
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Knighton,D.R., Zheng,J.H., Ten Eyck,L.F., Ashford,V.A., Xuong,N.H.,
            Taylor,S.S. and Sowadski,J.M.
  TITLE     Crystal structure of the catalytic subunit of cyclic adenosine
            monophosphate-dependent protein kinase
  JOURNAL   Science 253 (5018), 407-414 (1991)
   PUBMED   1862342
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM055544.1 and JAXUCZ010000002.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM055544.1, SRR26643299.9213.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..76
                     /product="cAMP-dependent protein kinase inhibitor alpha"
                     /note="PKI-alpha; protein kinase inhibitor, alpha; protein
                     kinase (cAMP-dependent, catalytic) inhibitor alpha"
                     /calculated_mol_wt=7829
     Region          2..70
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:P61925; propagated from
                     UniProtKB/Swiss-Prot (P63249.2)"
     Site            16
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P63249.2)"
     Site            19
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P63249.2)"
     Site            20
                     /site_type="other"
                     /note="Important for inhibition. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P63249.2)"
     Region          49..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63249.2)"
     CDS             1..76
                     /gene="Pkia"
                     /coded_by="NM_053772.2:377..607"
                     /db_xref="GeneID:114906"
                     /db_xref="RGD:621021"
ORIGIN      
        1 mtdvettyad fiasgrtgrr naihdilvss asgnsnelal klagldinkt egeddgqrss
       61 teqsgeaqge aakses
//
LOCUS       NP_001258005              73 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001258005
VERSION     NP_001258005.1
DBSOURCE    REFSEQ: accession NM_001271076.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 73)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 73)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 73)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 73)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 73)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 73)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 73)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 73)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 73)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 73)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1 and U60563.1.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN06621351, SAMN09345331
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..73
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..73
                     /product="amelogenin, X isoform isoform 4 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=6619
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          21..>73
                     /region_name="Amelogenin"
                     /note="pfam02948"
                     /db_xref="CDD:460761"
     CDS             1..73
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271076.1:67..288"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqpa fspmkwyqgt
       61 arhplnmett tek
//
LOCUS       NP_001257968             141 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 216 [Rattus norvegicus].
ACCESSION   NP_001257968 XP_002725830 XP_002728911
VERSION     NP_001257968.1
DBSOURCE    REFSEQ: accession NM_001271039.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Lee,J.H., Silhavy,J.L., Lee,J.E., Al-Gazali,L., Thomas,S.,
            Davis,E.E., Bielas,S.L., Hill,K.J., Iannicelli,M., Brancati,F.,
            Gabriel,S.B., Russ,C., Logan,C.V., Sharif,S.M., Bennett,C.P.,
            Abe,M., Hildebrandt,F., Diplas,B.H., Attie-Bitach,T., Katsanis,N.,
            Rajab,A., Koul,R., Sztriha,L., Waters,E.R., Ferro-Novick,S.,
            Woods,C.G., Johnson,C.A., Valente,E.M., Zaki,M.S. and Gleeson,J.G.
  TITLE     Evolutionarily assembled cis-regulatory module at a human
            ciliopathy locus
  JOURNAL   Science 335 (6071), 966-969 (2012)
   PUBMED   22282472
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Valente,E.M., Logan,C.V., Mougou-Zerelli,S., Lee,J.H.,
            Silhavy,J.L., Brancati,F., Iannicelli,M., Travaglini,L., Romani,S.,
            Illi,B., Adams,M., Szymanska,K., Mazzotta,A., Lee,J.E.,
            Tolentino,J.C., Swistun,D., Salpietro,C.D., Fede,C., Gabriel,S.,
            Russ,C., Cibulskis,K., Sougnez,C., Hildebrandt,F., Otto,E.A.,
            Held,S., Diplas,B.H., Davis,E.E., Mikula,M., Strom,C.M.,
            Ben-Zeev,B., Lev,D., Sagie,T.L., Michelson,M., Yaron,Y., Krause,A.,
            Boltshauser,E., Elkhartoufi,N., Roume,J., Shalev,S., Munnich,A.,
            Saunier,S., Inglehearn,C., Saad,A., Alkindy,A., Thomas,S.,
            Vekemans,M., Dallapiccola,B., Katsanis,N., Johnson,C.A.,
            Attie-Bitach,T. and Gleeson,J.G.
  TITLE     Mutations in TMEM216 perturb ciliogenesis and cause Joubert, Meckel
            and related syndromes
  JOURNAL   Nat Genet 42 (7), 619-625 (2010)
   PUBMED   20512146
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Edvardson,S., Shaag,A., Zenvirt,S., Erlich,Y., Hannon,G.J.,
            Shanske,A.L., Gomori,J.M., Ekstein,J. and Elpeleg,O.
  TITLE     Joubert syndrome 2 (JBTS2) in Ashkenazi Jews is associated with a
            TMEM216 mutation
  JOURNAL   Am J Hum Genet 86 (1), 93-97 (2010)
   PUBMED   20036350
  REMARK    Erratum:[Am J Hum Genet. 2010 Feb;86(2):294. Shanske, Alan L
            [added]]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Aug 31, 2012 this sequence version replaced
            XP_002728911.2, XP_002725830.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB568391.1, SRR26360186.1412169.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..141
                     /product="transmembrane protein 216"
                     /calculated_mol_wt=16042
     Region          15..121
                     /region_name="Transmemb_17"
                     /note="Predicted membrane protein; pfam09799"
                     /db_xref="CDD:462907"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6ID01.2)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6ID01.2)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6ID01.2)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B6ID01.2)"
     CDS             1..141
                     /gene="Tmem216"
                     /gene_synonym="RGD1304607"
                     /coded_by="NM_001271039.1:17..442"
                     /db_xref="GeneID:361727"
                     /db_xref="RGD:1304607"
ORIGIN      
        1 maprdkrlss tpleilffln gwyyatyfll elliflykgl llpyptanlv ldvvmlllyl
       61 gievirlffg tkgnlcqrkm plgisvaltf psammasyyl llqtyvlrle aimnsillff
      121 cgsellleml tlatfssmdr i
//
LOCUS       NP_064461                286 aa            linear   ROD 27-APR-2025
DEFINITION  3-hydroxyanthranilate 3,4-dioxygenase [Rattus norvegicus].
ACCESSION   NP_064461
VERSION     NP_064461.1
DBSOURCE    REFSEQ: accession NM_020076.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Berg,M., Polyzos,K.A., Agardh,H., Baumgartner,R., Forteza,M.J.,
            Kareinen,I., Gistera,A., Bottcher,G., Hurt-Camejo,E., Hansson,G.K.
            and Ketelhuth,D.F.J.
  TITLE     3-Hydroxyanthralinic acid metabolism controls the hepatic
            SREBP/lipoprotein axis, inhibits inflammasome activation in
            macrophages, and decreases atherosclerosis in Ldlr-/- mice
  JOURNAL   Cardiovasc Res 116 (12), 1948-1957 (2020)
   PUBMED   31589306
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Shi,H., Enriquez,A., Rapadas,M., Martin,E.M.M.A., Wang,R.,
            Moreau,J., Lim,C.K., Szot,J.O., Ip,E., Hughes,J.N., Sugimoto,K.,
            Humphreys,D.T., McInerney-Leo,A.M., Leo,P.J., Maghzal,G.J.,
            Halliday,J., Smith,J., Colley,A., Mark,P.R., Collins,F.,
            Sillence,D.O., Winlaw,D.S., Ho,J.W.K., Guillemin,G.J., Brown,M.A.,
            Kikuchi,K., Thomas,P.Q., Stocker,R., Giannoulatou,E., Chapman,G.,
            Duncan,E.L., Sparrow,D.B. and Dunwoodie,S.L.
  TITLE     NAD Deficiency, Congenital Malformations, and Niacin
            Supplementation
  JOURNAL   N Engl J Med 377 (6), 544-552 (2017)
   PUBMED   28792876
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Pidugu,L.S., Neu,H., Wong,T.L., Pozharski,E., Molloy,J.L.,
            Michel,S.L. and Toth,E.A.
  TITLE     Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase
            with native and non-native metals bound in the active site
  JOURNAL   Acta Crystallogr D Struct Biol 73 (Pt 4), 340-348 (2017)
   PUBMED   28375145
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Maddison,D.C. and Giorgini,F.
  TITLE     The kynurenine pathway and neurodegenerative disease
  JOURNAL   Semin Cell Dev Biol 40, 134-141 (2015)
   PUBMED   25773161
  REMARK    Review article
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Sathyasaikumar,K.V., Stachowski,E.K., Wonodi,I., Roberts,R.C.,
            Rassoulpour,A., McMahon,R.P. and Schwarcz,R.
  TITLE     Impaired kynurenine pathway metabolism in the prefrontal cortex of
            individuals with schizophrenia
  JOURNAL   Schizophr Bull 37 (6), 1147-1156 (2011)
   PUBMED   21036897
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Nakano,K., Asai,H. and Kitoh,J.
  TITLE     Abnormally high activity of 3-hydroxyanthranilate 3,4-dioxygenase
            in brain of epilepsy-prone El mice
  JOURNAL   Brain Res 572 (1-2), 1-4 (1992)
   PUBMED   1611505
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Schwarcz,R., Okuno,E. and White,R.J.
  TITLE     Basal ganglia lesions in the rat: effects on quinolinic acid
            metabolism
  JOURNAL   Brain Res 490 (1), 103-109 (1989)
   PUBMED   2527078
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Schwarcz,R., Okuno,E., White,R.J., Bird,E.D. and Whetsell,W.O. Jr.
  TITLE     3-Hydroxyanthranilate oxygenase activity is increased in the brains
            of Huntington disease victims
  JOURNAL   Proc Natl Acad Sci U S A 85 (11), 4079-4081 (1988)
   PUBMED   2967497
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Okuno,E., Kohler,C. and Schwarcz,R.
  TITLE     Rat 3-hydroxyanthranilic acid oxygenase: purification from the
            liver and immunocytochemical localization in the brain
  JOURNAL   J Neurochem 49 (3), 771-780 (1987)
   PUBMED   3112306
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Foster,A.C., White,R.J. and Schwarcz,R.
  TITLE     Synthesis of quinolinic acid by 3-hydroxyanthranilic acid oxygenase
            in rat brain tissue in vitro
  JOURNAL   J Neurochem 47 (1), 23-30 (1986)
   PUBMED   2940338
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D44494.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D44494.1, FQ219702.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..286
                     /product="3-hydroxyanthranilate 3,4-dioxygenase"
                     /EC_number="1.13.11.6"
                     /note="HAD; 3-HAO; 3-hydroxyanthranilate oxygenase;
                     3-hydroxyanthranilic acid dioxygenase"
                     /calculated_mol_wt=32451
     Region          1..160
                     /region_name="Domain A (catalytic).
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03019"
                     /note="propagated from UniProtKB/Swiss-Prot (P46953.2)"
     Region          10..159
                     /region_name="cupin_HAO"
                     /note="3-Hydroxyanthranilate-3,4-dioxygenase, cupin
                     domain; cd06123"
                     /db_xref="CDD:380378"
     Site            order(28,32,52,54,76,79..83,104,106)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:380378"
     Site            order(47,53,91,105)
                     /site_type="active"
                     /db_xref="CDD:380378"
     Region          161..177
                     /region_name="Linker.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03019"
                     /note="propagated from UniProtKB/Swiss-Prot (P46953.2)"
     Region          178..286
                     /region_name="Domain B.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03019"
                     /note="propagated from UniProtKB/Swiss-Prot (P46953.2)"
     Region          209..>259
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..286
                     /gene="Haao"
                     /coded_by="NM_020076.2:89..949"
                     /db_xref="GeneID:56823"
                     /db_xref="RGD:71071"
ORIGIN      
        1 mercvrvksw veenrasfqp pvcnklmhre qlkimfvggp ntrkdyhiee geevfyqleg
       61 dmvlrvleqg ehrdvvirqg eifllparvp hspqrfantm glvierrrme teldglryyv
      121 gdtedvlfek wfhckdlgtq lapiiqeffh seqyrtgkpn pdqllkeppf plstrsvmep
      181 mslkawlesh srelqagtsl slfgdsyetq viahgqgssk gprqdvdvwl wqlegsskvt
      241 mggqcvalap ddsllvpagf symweraqgs valsvtqdpa ckkplg
//
LOCUS       NP_113720                255 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 8 [Rattus norvegicus].
ACCESSION   NP_113720 XP_215128
VERSION     NP_113720.1
DBSOURCE    REFSEQ: accession NM_031532.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            On Apr 19, 2005 this sequence version replaced XP_215128.3.
            
            Transcript Variant: This variant (8) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (8) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ214833.1, FQ224892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..255
                     /product="troponin T, fast skeletal muscle isoform 8"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30225
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P02641; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          59..195
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          97..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          231..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     CDS             1..255
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_031532.2:117..884"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeeev qeeekprpkl tapkipegek vdfddiqkkr
       61 qnkdlmelqa lidshfeark keeeelialk eriekrraer aeqqriraek ererqnrlae
      121 ekarreeeda krraeddlkk kkalssmgan yssylakadq krgkkqtare mkkkilaerr
      181 kplnidhlsd dklrdkakel wdtlyqletd kfefgeklkr qkydittlrs ridqaqkhsk
      241 kagatakgkv ggrwk
//
LOCUS       NP_001258004              98 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001258004
VERSION     NP_001258004.1
DBSOURCE    REFSEQ: accession NM_001271075.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 98)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 98)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 98)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 98)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1 and U60564.1.
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site at the 5' end of an exon compared to variant 1. The
            resulting isoform (3) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U60564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984036 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..98
                     /product="amelogenin, X isoform isoform 3 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=9431
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          <18..74
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     Region          21..>47
                     /region_name="Amelogenin"
                     /note="pfam02948"
                     /db_xref="CDD:460761"
     CDS             1..98
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271075.1:67..363"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqpp lspilpelpl
       61 eawpatdktk reevafspmk wyqgtarhpl nmetttek
//
LOCUS       NP_997659                177 aa            linear   ROD 27-APR-2025
DEFINITION  protein CutA isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_997659 XP_215338
VERSION     NP_997659.2
DBSOURCE    REFSEQ: accession NM_212494.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Liang,D., Nunes-Tavares,N., Xie,H.Q., Carvalho,S., Bon,S. and
            Massoulie,J.
  TITLE     Protein CutA undergoes an unusual transfer into the secretory
            pathway and affects the folding, oligomerization, and secretion of
            acetylcholinesterase
  JOURNAL   J Biol Chem 284 (8), 5195-5207 (2009)
   PUBMED   19049969
  REMARK    GeneRIF: Protein CutA undergoes an unusual transfer into the
            secretory pathway and affects the folding, oligomerization, and
            secretion of acetylcholinesterase.
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Arnesano,F., Banci,L., Benvenuti,M., Bertini,I., Calderone,V.,
            Mangani,S. and Viezzoli,M.S.
  TITLE     The evolutionarily conserved trimeric structure of CutA1 proteins
            suggests a role in signal transduction
  JOURNAL   J Biol Chem 278 (46), 45999-46006 (2003)
   PUBMED   12949080
  REMARK    GeneRIF: comparative x-ray crystallography analysis suggests CutA1
            proteins have a role in signal transduction through allosteric
            communications between subunits.
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Perrier,A.L., Cousin,X., Boschetti,N., Haas,R., Chatel,J.M.,
            Bon,S., Roberts,W.L., Pickett,S.R., Massoulie,J., Rosenberry,T.L.
            and Krejci,E.
  TITLE     Two distinct proteins are associated with tetrameric
            acetylcholinesterase on the cell surface
  JOURNAL   J Biol Chem 275 (44), 34260-34265 (2000)
   PUBMED   10954708
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Navaratnam,D.S., Fernando,F.S., Priddle,J.D., Giles,K., Clegg,S.M.,
            Pappin,D.J., Craig,I. and Smith,A.D.
  TITLE     Hydrophobic protein that copurifies with human brain
            acetylcholinesterase: amino acid sequence, genomic organization,
            and chromosomal localization
  JOURNAL   J Neurochem 74 (5), 2146-2153 (2000)
   PUBMED   10800960
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883042.1.
            
            On Sep 11, 2009 this sequence version replaced NP_997659.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760400,
                              SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..177
                     /product="protein CutA isoform 1 precursor"
                     /note="protein CutA; brain acetylcholinesterase putative
                     membrane anchor; divalent cation tolerant protein CUTA"
                     /calculated_mol_wt=15533
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6MGD0.2)"
                     /calculated_mol_wt=3243
     mat_peptide     33..177
                     /product="Protein CutA. /id=PRO_0000006381"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGD0.2)"
                     /calculated_mol_wt=15533
     Region          70..164
                     /region_name="CutA1"
                     /note="CutA1 divalent ion tolerance protein; pfam03091"
                     /db_xref="CDD:460800"
     CDS             1..177
                     /gene="Cuta"
                     /gene_synonym="CutA1"
                     /coded_by="NM_212494.2:91..624"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:294288"
                     /db_xref="RGD:1303306"
ORIGIN      
        1 mnwgralgvl lgggatllls flcmpallpv asrllllpra llsmasgspp sqpspasgsg
       61 yvpgsvsaaf vtcpnekvak eiaravvekr laacvnlipq itsiyewkgk ieedsevlmm
      121 iktqsslvpa ltefvrsvhp yevaevialp veqgnppylh wvhqvtesvs gsgkalp
//
LOCUS       NP_001013904             184 aa            linear   ROD 27-APR-2025
DEFINITION  deoxycytidylate deaminase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001013904 XP_214348
VERSION     NP_001013904.2
DBSOURCE    REFSEQ: accession NM_001013882.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Maley,G.F., Lobo,A.P. and Maley,F.
  TITLE     Properties of an affinity-column-purified human deoxycytidylate
            deaminase
  JOURNAL   Biochim Biophys Acta 1162 (1-2), 161-170 (1993)
   PUBMED   8448179
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV776012.1 and BC087138.1.
            
            On Jun 4, 2009 this sequence version replaced NP_001013904.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087138.1, EV776012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..184
                     /product="deoxycytidylate deaminase isoform 1"
                     /EC_number="3.5.4.12"
                     /note="deoxycytidylate deaminase"
                     /calculated_mol_wt=20636
     Region          14..164
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
     CDS             1..184
                     /gene="Dctd"
                     /coded_by="NM_001013882.2:77..631"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290741"
                     /db_xref="RGD:1359671"
ORIGIN      
        1 mtytpnmsdi sckkrddyle wpeyfmavaf lsaqrskdps sqvgacivnt enkivgigyn
       61 gmpngcsddl lpwrrtaenk ldtkypyvch aelnaimnkn sadvkgcsmy valfpcneca
      121 kliiqagike vifmsdkyhd seettaarll fklagvtfrk ftpkyskivi dfdsinsrps
      181 qkpq
//
LOCUS       NP_446115               2391 aa            linear   ROD 27-APR-2025
DEFINITION  versican core protein isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_446115
VERSION     NP_446115.1
DBSOURCE    REFSEQ: accession NM_053663.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2391)
  AUTHORS   Harten,I.A., Kaber,G., Agarwal,K.J., Kang,I., Ibarrientos,S.R.,
            Workman,G., Chan,C.K., Nivison,M.P., Nagy,N., Braun,K.R.,
            Kinsella,M.G., Merrilees,M.J. and Wight,T.N.
  TITLE     The synthesis and secretion of versican isoform V3 by mammalian
            cells: A role for N-linked glycosylation
  JOURNAL   Matrix Biol 89, 27-42 (2020)
   PUBMED   32001344
  REMARK    GeneRIF: The synthesis and secretion of versican isoform V3 by
            mammalian cells: A role for N-linked glycosylation.
REFERENCE   2  (residues 1 to 2391)
  AUTHORS   Bogen,O., Bender,O., Alvarez,P., Kern,M., Tomiuk,S., Hucho,F. and
            Levine,J.D.
  TITLE     Expression of a novel versican variant in dorsal root ganglia from
            spared nerve injury rats
  JOURNAL   Mol Pain 15, 1744806919874557 (2019)
   PUBMED   31429356
  REMARK    GeneRIF: mRNAs of the versican gene with exon 8beta are predicted
            to be constitutively degraded by nonsense-mediated RNA decay.
REFERENCE   3  (residues 1 to 2391)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   4  (residues 1 to 2391)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 2391)
  AUTHORS   Carthy,J.M., Abraham,T., Meredith,A.J., Boroomand,S. and
            McManus,B.M.
  TITLE     Versican localizes to the nucleus in proliferating mesenchymal
            cells
  JOURNAL   Cardiovasc Pathol 24 (6), 368-374 (2015)
   PUBMED   26395512
  REMARK    GeneRIF: Versican localizes to the nucleus in proliferating
            mesenchymal cells and suggest role in mitotic spindle organization
            during cell division.
REFERENCE   6  (residues 1 to 2391)
  AUTHORS   Lemire,J.M., Merrilees,M.J., Braun,K.R. and Wight,T.N.
  TITLE     Overexpression of the V3 variant of versican alters arterial smooth
            muscle cell adhesion, migration, and proliferation in vitro
  JOURNAL   J Cell Physiol 190 (1), 38-45 (2002)
   PUBMED   11807809
  REMARK    GeneRIF: Overexpression of alternatively spliced V3 variant of
            versican alters arterial smooth muscle cell adhesion, migration,
            proliferation and cell shape
REFERENCE   7  (residues 1 to 2391)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
REFERENCE   8  (residues 1 to 2391)
  AUTHORS   Mjaatvedt,C.H., Yamamura,H., Capehart,A.A., Turner,D. and
            Markwald,R.R.
  TITLE     The Cspg2 gene, disrupted in the hdf mutant, is required for right
            cardiac chamber and endocardial cushion formation
  JOURNAL   Dev Biol 202 (1), 56-66 (1998)
   PUBMED   9758703
REFERENCE   9  (residues 1 to 2391)
  AUTHORS   Milev,P., Maurel,P., Chiba,A., Mevissen,M., Popp,S., Yamaguchi,Y.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Differential regulation of expression of hyaluronan-binding
            proteoglycans in developing brain: aggrecan, versican, neurocan,
            and brevican
  JOURNAL   Biochem Biophys Res Commun 247 (2), 207-212 (1998)
   PUBMED   9642104
REFERENCE   10 (residues 1 to 2391)
  AUTHORS   Pyke,C., Kristensen,P., Ostergaard,P.B., Oturai,P.S. and Romer,J.
  TITLE     Proteoglycan expression in the normal rat kidney
  JOURNAL   Nephron 77 (4), 461-470 (1997)
   PUBMED   9434070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473955.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform 2, also referred to as V1), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5756307, SAMEA5760383
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2391
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..2391
                     /product="versican core protein isoform 2 precursor"
                     /note="versican core protein; GHAP; PG-M; large fibroblast
                     proteoglycan; glial hyaluronate-binding protein;
                     chondroitin sulfate proteoglycan core protein 2;
                     chondroitin sulfate proteoglycan 2 (versican)"
                     /calculated_mol_wt=259563
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Region          2086..2120
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          2122..2158
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(2122,2125,2139)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          2164..2287
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Site            order(2182,2214..2217,2246,2256,2264,2266,2272,2275,
                     2277..2279)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Site            order(2225,2229,2252,2258..2259)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2229,2259)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(2249,2251,2258,2272..2273)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Region          2291..2347
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(2301,2321)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..2391
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
                     /coded_by="NM_053663.1:379..7554"
                     /note="gene_id=rCG44618.0 transcript_id=rCT44617.0
                     protein_id=rCP34867.0 isoform=CRA_b; isoform 2 precursor
                     is encoded by transcript variant 2"
                     /db_xref="GeneID:114122"
                     /db_xref="RGD:619940"
ORIGIN      
        1 mlinmngilw mcstllltha lhkakmeenp pvkgslsgkv ilpchfstlp tlppdyntse
       61 flrikwskie vdkngkdike ttvlvaqdgn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdagvyrc dvmygiedtq ntmslavdgv vfhyraatsr ytlnfesaqq acldigavia
      181 tpeqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec anrdarlatv gelhaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkrrm sdmvvnghpi
      361 dseskeeepc seetdplhdl faeilpelpd sfeidiyhse ededgeedcv natdvtttps
      421 vqyitgkphv ttvpknpeaa earrglyesv apsqnfsnts atdthqfipa etelsttmqf
      481 tkskeatell eitwkpetyp etpehfssge pdvfptlpsh dgkttkwsef itesnpnten
      541 pehkqpkpip lfpeefsgeg aidqasqqti fstatevalg ketdqsptis tssirsgsvs
      601 vhaleedpia ltgisqtdes mstveswvem tpsqtvefsg sssaptiegs geveeytnki
      661 fntvtdlpqr eptdtlipld msnimitdhh iytpattapl dsqlpstdar ptqfgiqttt
      721 sewvsstsfe grkteedker dtnaahtgev qpatersdrl lltselessn vaasspldtw
      781 egfvpettst vsekemantt pvftetsdva nletqsfehs sssqprvqee lttlsgkppl
      841 ifmdlgsgda stdmefitas sftldlesdt kvkkelpstl spsvetssss epiglapstv
      901 ldieivevmn qtskktlise lsgkptsqae vrdlypglge dfsgdsseyp tvssttmkee
      961 tvgmggsene rvkdtqtlss ipptsdninp vpdskgfgst vasttafpwe efmtsaegsg
     1021 eelssvrssv slvlplgvdi lpttespyfd qefeeaaavt eagkqsalpi avsgntvdlt
     1081 enrdievnst msvdlpqtme paklwskpev npekqeigse tvtqdkaqgq ksfeslhssl
     1141 apeqttlesq slietevqts yysmlttmkt yntneeveee gtsiahmstp gpgikglesy
     1201 pthpeatgks ysfsasalvt esgparsvvm dsstqeeesi klfqkdmilt hkesnsdlsf
     1261 sglgsgealp plpttsvslt dmgkinstly petshmeslg tsilgdnher mknvsnevrt
     1321 lisetgsisq dsteapnttl sdtrteestt splpfmklmd tehspkqtlr weeeiqthrp
     1381 qtmtgqitnd nssvseaeaa atsapaflpe tysvemtkaf atslsqtsdl fdansgegsg
     1441 evdgldlvyt srttqassqg dsmfashgfi ekhpevsrte tgatdgspta samflhqsey
     1501 nesslyptst lpstvtyesp segiadglqd hirfevstlk psrrkatesv iidldkedsk
     1561 dlglaitesa iveilpelts drniiididh tkpvyeyipg iqtdldsdip lgshgssees
     1621 levqekyeat inlspteeaf dgsgdalpag htqaiynesv tpsdgkqped isfsfatgip
     1681 vsstetelnt ffptvstlhi psklttaspe idkpnieais lddifesstl sdgqaiadqs
     1741 evistlghle ktqeeyeekk yggpsfqpef fsgvgevftd apayvsigrt ysvaqpltef
     1801 pnvvgqsdst hyteatsavs svtelspqtp sspspvyids gvseftevph ksaqpaptaa
     1861 ssqkliegsf kevranieat ikslgendhg tespsmspsp aldiseddsk pklledlets
     1921 ptktetsqds pnkandqipg ktagilagik ttesgpvvta addmelgdat qrphsasapa
     1981 afrvetsmvp qpipqeperp tfpsleinhe thtslfeesi latsekqvsq rildysnqat
     2041 vstldlnteh sippfsildn snetafligi seetvegtav ylpgpdlckt npclnggtcy
     2101 ptetsyvctc apgysgdqce ldfdechsnp crngatcvdg lntfrclclp syvgalceqd
     2161 tetcdygwhk fqgqcykyfa hrrtwdaaer ecrlqgahlt silsheeqmf vnrvghdyqw
     2221 iglndkmfeh dfrwtdgsal qyenwrpnqp dsffsagedc vviiwhengq wndvpcnyhl
     2281 tytckkgtva cgqppvvena ktfgkmkpry einsliryhc kdgfiqrhlp tirclgngrw
     2341 ampkitcmnp sayqrtyskk ylknsssvkd nsintskheh rwsrrwqetr r
//
LOCUS       NP_001178484            1189 aa            linear   ROD 27-APR-2025
DEFINITION  rab11 family-interacting protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178484 XP_002728473
VERSION     NP_001178484.1
DBSOURCE    REFSEQ: accession NM_001191555.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Carson,B.P., Del Bas,J.M., Moreno-Navarrete,J.M.,
            Fernandez-Real,J.M. and Mora,S.
  TITLE     The rab11 effector protein FIP1 regulates adiponectin trafficking
            and secretion
  JOURNAL   PLoS One 8 (9), e74687 (2013)
   PUBMED   24040321
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Eva,R., Dassie,E., Caswell,P.T., Dick,G., ffrench-Constant,C.,
            Norman,J.C. and Fawcett,J.W.
  TITLE     Rab11 and its effector Rab coupling protein contribute to the
            trafficking of beta 1 integrins during axon growth in adult dorsal
            root ganglion neurons and PC12 cells
  JOURNAL   J Neurosci 30 (35), 11654-11669 (2010)
   PUBMED   20810886
  REMARK    GeneRIF: An interaction with Rab11 is necessary for long-range
            targeting of beta1 integrins to the growth cone along axons and in
            neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC107469.1 and JAXUCZ010000016.1.
            
            On Oct 14, 2010 this sequence version replaced XP_002728473.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2824724.1,
                                           SRR26643429.50853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..1189
                     /product="rab11 family-interacting protein 1 isoform 1"
                     /note="rab11 family-interacting protein 1; rab-coupling
                     protein; RAB11 family interacting protein 1 (class I)"
                     /calculated_mol_wt=127712
     Region          20..150
                     /region_name="C2_Rab11-FIP_classI"
                     /note="C2 domain found in Rab11-family interacting
                     proteins (FIP) class I; cd08682"
                     /db_xref="CDD:176064"
     Region          164..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D620; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D620; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          <423..796
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          483..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          757..>1082
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1132..1179
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..1189
                     /gene="Rab11fip1"
                     /gene_synonym="Rab11-FIP1; RGD1562965"
                     /coded_by="NM_001191555.1:48..3617"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:498650"
                     /db_xref="RGD:1562965"
ORIGIN      
        1 mslaasagrg pgtmwspthv qvtvlqargl rakgpggtsd ayaviqvgke kyatsvsers
       61 lgapvwreea tfelppllss gtapaaaaat lqltvlhral lgldkflgra evdlrelhrd
      121 qsrrkkqwyt lkskpgkkdk ergeievdiq fmrnnmtasm fdlsmkdksr npfgklkdki
      181 kgknkdntsd tasaivpstt psvdsddesf skdkkkkski ktlfskpslq ktplsqsmsv
      241 lptskpdkvl lrpgdfqsrw gdegdnedes ssasevmsqk rtsstdhtqp nqsnfslpkk
      301 eglsflgglr skndslsrsn vcingnhvym eqpeakseir esspsnspsp qgfrkrhlfs
      361 stenlaarsp kepgegggms sdrrlsdsst kdsmksmslp syrplttads reglspanme
      421 vatketkdsk kqeskkssll slvtgkkdva kgsegeplpp vsekekgrkg vlveaqlree
      481 dlvrrpekda vpvasqwgss qnpfedaqis dleasveskc epkppvpvpr tpqtravkpr
      541 levspeaqpk arlpssdsap faaflsssaq apvlsdlrcd setqfsesps assfssplaa
      601 piststpveh wptdkgeada eepslllrai ssvtpaanag ssasrspceq lptperkgpq
      661 essggkares gtgkevgsde seksligqhe ellkipfper hwalggmtta tspvqeeeaa
      721 ssfhsvrpkh qemhqnasgg qrkakkrvsf seqlfveeet egptwleegd kghpqqlsqe
      781 gpvassmpsa gspesphteg tgqepvtiss esesflegpq seaspargtq llrdekddlm
      841 apcqskasdh egllsnplsd lpsasdlksp imadlslslp sipevasdde rfdetgdggk
      901 garladleag vsplnvspsi letagqtggr ahesvpvenq cdlrpqtpka apseqtaalg
      961 spkphlgkss svneeypgpd tvdeeklkgs grpgspldsp vrspslaetf pathsfpgsp
     1021 psdthhttva esqkqatadv ssnrvenfgk kkpllqawvt pseihpvpaq psagagaakh
     1081 rphpvkpmnt tapkitnssl gtatiisenl inealmkkyq psdpafayaq lthdeliqlv
     1141 lkqketiskk efqvreledy idnllvrvme etpnilrvpa qtgkkagkm
//
LOCUS       NP_001257585             864 aa            linear   ROD 27-APR-2025
DEFINITION  NT-3 growth factor receptor isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001257585
VERSION     NP_001257585.1
DBSOURCE    REFSEQ: accession NM_001270656.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Chen,Z., Huang,Z., Luo,Y., Zou,Q., Bai,L., Tang,G., Wang,X.,
            Cao,G., Huang,M., Xiang,J. and Yu,H.
  TITLE     Genome-wide analysis identifies critical DNA methylations within
            NTRKs genes in colorectal cancer
  JOURNAL   J Transl Med 19 (1), 73 (2021)
   PUBMED   33593392
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Tan,W., Dong,L., Shi,X., Tang,Q. and Jiang,D.
  TITLE     P75NTR Exacerbates SCI-induced Mitochondrial Damage and Neuronal
            Apoptosis Depending on NTRK3
  JOURNAL   Curr Neurovasc Res 18 (5), 552-564 (2021)
   PUBMED   34970951
  REMARK    GeneRIF: P75NTR Exacerbates SCI-induced Mitochondrial Damage and
            Neuronal Apoptosis Depending on NTRK3.
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Qiao,X., Yin,F., Ji,Y., Li,Y., Yan,P. and Lai,J.
  TITLE     5-Aza-2'-deoxycytidine in the medial prefrontal cortex regulates
            alcohol-related behavior and Ntf3-TrkC expression in rats
  JOURNAL   PLoS One 12 (6), e0179469 (2017)
   PUBMED   28614398
  REMARK    GeneRIF: Data show that 5-Aza-dc reversed the alcohol-induced
            downregulation of neurotrophin-3 (Ntf3), correspondingly the
            expression of its receptor-neurotrophic receptor tyrosine kinase 3
            (TrkC) was reduced.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Behrouz Sharif,S., Hashemzadeh,S., Mousavi Ardehaie,R.,
            Eftekharsadat,A., Ghojazadeh,M., Mehrtash,A.H., Estiar,M.A.,
            Teimoori-Toolabi,L. and Sakhinia,E.
  TITLE     Detection of aberrant methylated SEPT9 and NTRK3 genes in sporadic
            colorectal cancer patients as a potential diagnostic biomarker
  JOURNAL   Oncol Lett 12 (6), 5335-5343 (2016)
   PUBMED   28105243
REFERENCE   5  (residues 1 to 864)
  AUTHORS   Dmitrieva,V.G., Stavchansky,V.V., Povarova,O.V., Skvortsova,V.I.,
            Limborska,S.A. and Dergunova,L.V.
  TITLE     [Effects of ischemia on the expression of neurotrophins and their
            receptors in rat brain structures outside the lesion site,
            including on the opposite hemisphere]
  JOURNAL   Mol Biol (Mosk) 50 (5), 775-784 (2016)
   PUBMED   27830679
  REMARK    GeneRIF: It has been shown that ischemia influenced the expression
            of neurotrophins (Bdnf, Ngf, Nt-3) and their receptors (TrkB, TrkA,
            TrkC, p75) in brain structures outside the lesion focus, including
            the contralateral hemisphere.
REFERENCE   6  (residues 1 to 864)
  AUTHORS   Qian,X., Riccio,A., Zhang,Y. and Ginty,D.D.
  TITLE     Identification and characterization of novel substrates of Trk
            receptors in developing neurons
  JOURNAL   Neuron 21 (5), 1017-1029 (1998)
   PUBMED   9856458
REFERENCE   7  (residues 1 to 864)
  AUTHORS   Fernyhough,P., Diemel,L.T. and Tomlinson,D.R.
  TITLE     Target tissue production and axonal transport of neurotrophin-3 are
            reduced in streptozotocin-diabetic rats
  JOURNAL   Diabetologia 41 (3), 300-306 (1998)
   PUBMED   9541170
REFERENCE   8  (residues 1 to 864)
  AUTHORS   Tsoulfas,P., Soppet,D., Escandon,E., Tessarollo,L.,
            Mendoza-Ramirez,J.L., Rosenthal,A., Nikolics,K. and Parada,L.F.
  TITLE     The rat trkC locus encodes multiple neurogenic receptors that
            exhibit differential response to neurotrophin-3 in PC12 cells
  JOURNAL   Neuron 10 (5), 975-990 (1993)
   PUBMED   8494648
REFERENCE   9  (residues 1 to 864)
  AUTHORS   Valenzuela,D.M., Maisonpierre,P.C., Glass,D.J., Rojas,E., Nunez,L.,
            Kong,Y., Gies,D.R., Stitt,T.N., Ip,N.Y. and Yancopoulos,G.D.
  TITLE     Alternative forms of rat TrkC with different functional
            capabilities
  JOURNAL   Neuron 10 (5), 963-974 (1993)
   PUBMED   8494647
REFERENCE   10 (residues 1 to 864)
  AUTHORS   Merlio,J.P., Ernfors,P., Jaber,M. and Persson,H.
  TITLE     Molecular cloning of rat trkC and distribution of cells expressing
            messenger RNAs for members of the trk family in the rat central
            nervous system
  JOURNAL   Neuroscience 51 (3), 513-532 (1992)
   PUBMED   1488112
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L03813.1 and L14447.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcritp and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L14447.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..864
                     /product="NT-3 growth factor receptor isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="NT-3 growth factor receptor; trk-C; GP145-TrkC;
                     trkC tyrosine kinase; neurotrophic tyrosine kinase,
                     receptor, type 3; neural receptor protein-tyrosine kinase
                     (trkC)"
                     /calculated_mol_wt=93605
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3477
     Region          31..>51
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     mat_peptide     32..864
                     /product="NT-3 growth factor receptor. /id=PRO_0000016735"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03351.2)"
                     /calculated_mol_wt=93605
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          103..160
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          104..125
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03351.2)"
     Region          105..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          128..149
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03351.2)"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          152..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          163..208
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          214..299
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          227..231
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          240..244
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          266..270
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          281..286
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          304..396
                     /region_name="IgI_TrKABC_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptors
                     TrkA, TrkB, and TrkC; member of the I-set of Ig
                     superfamily (IgSF) domains; cd04971"
                     /db_xref="CDD:409360"
     Region          305..311
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409360"
     Region          313..316
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409360"
     Region          319..327
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409360"
     Site            328
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          330..337
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409360"
     Region          340..343
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409360"
     Region          348..354
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409360"
     Site            order(353,366..367,370)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          358..366
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409360"
     Region          374..382
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409360"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          385..393
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409360"
     Site            388
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            430..453
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03351.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6VNS1; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            516
                     /site_type="other"
                     /note="Interaction with SHC1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q03351.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q16288; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Region          532..857
                     /region_name="PTKc_TrkC"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tropomyosin Related Kinase C; cd05094"
                     /db_xref="CDD:270676"
     Site            order(544..548,552,570,572,617..620,623..624,679,683..684,
                     686,697,754..758,767,801)
                     /site_type="active"
                     /db_xref="CDD:270676"
     Site            order(544..545,547..548,552,570,572,617..620,623..624,
                     683..684,686,697)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270676"
     Site            order(679,683,754..758,767,801)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270676"
     Site            order(696..711,751..760)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270676"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            859
                     /site_type="other"
                     /note="Interaction with PLC-gamma-1.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q03351.2)"
     CDS             1..864
                     /gene="Ntrk3"
                     /gene_synonym="trkC"
                     /coded_by="NM_001270656.1:52..2646"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29613"
                     /db_xref="RGD:3214"
ORIGIN      
        1 mdvslcpakc sfwrifllgs vwldyvgsvl acpancvcsk teincrrpdd gnlfpllegq
       61 dsgnsngnas initdisrni tsihienwrg lhtlnavdme lytglqklti knsglrniqp
      121 rafaknphlr yinlssnrlt tlswqlfqtl slrelrleqn ffncscdirw mqlwqeqgea
      181 rldsqslyci sadgsqlplf rmnisqcdlp eisvshvnlt vregdnavit cngsgsplpd
      241 vdwivtglqs inthqtnlnw tnvhainltl vnvtsedngf tltciaenvv gmsnasvalt
      301 vyypprvvsl vepevrlehc iefvvrgnpt ptlhwlyngq plreskiihm dyyqegevse
      361 gcllfnkpth ynngnytlia knalgtanqt inghflkepf pestdffdfe sdasptppit
      421 vthkpeedtf gvsiavglaa facvllvvlf iminkygrrs kfgmkgpvav isgeedsasp
      481 lhhinhgitt pssldagpdt vvigmtripv ienpqyfrqg hnchkpdtyv qhikrrdivl
      541 krelgegafg kvflaecynl sptkdkmlva vkalkdptla arkdfqreae lltnlqhehi
      601 vkfygvcgdg dplimvfeym khgdlnkflr ahgpdamilv dgqprqakge lglsqmlhia
      661 sqiasgmvyl asqhfvhrdl atrnclvgan llvkigdfgm srdvystdyy regpyqkgpf
      721 svswqqqrla asaastlfnp sgndfciwce vgghtmlpir wmppesimyr kfttesdvws
      781 fgvilweift ygkqpwfqls nteviecitq grvlerprvc pkevydvmlg cwqrepqqrl
      841 nikeiykilh algkatpiyl dilg
//
LOCUS       NP_445991                283 aa            linear   ROD 27-APR-2025
DEFINITION  isopentenyl-diphosphate Delta-isomerase 1 [Rattus norvegicus].
ACCESSION   NP_445991
VERSION     NP_445991.2
DBSOURCE    REFSEQ: accession NM_053539.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Zheng,W., Sun,F., Bartlam,M., Li,X., Li,R. and Rao,Z.
  TITLE     The crystal structure of human isopentenyl diphosphate isomerase at
            1.7 A resolution reveals its catalytic mechanism in isoprenoid
            biosynthesis
  JOURNAL   J Mol Biol 366 (5), 1447-1458 (2007)
   PUBMED   17250851
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Clizbe,D.B., Owens,M.L., Masuda,K.R., Shackelford,J.E. and
            Krisans,S.K.
  TITLE     IDI2, a second isopentenyl diphosphate isomerase in mammals
  JOURNAL   J Biol Chem 282 (9), 6668-6676 (2007)
   PUBMED   17202134
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Kovacs,W.J., Tape,K.N., Shackelford,J.E., Duan,X., Kasumov,T.,
            Kelleher,J.K., Brunengraber,H. and Krisans,S.K.
  TITLE     Localization of the pre-squalene segment of the isoprenoid
            biosynthetic pathway in mammalian peroxisomes
  JOURNAL   Histochem Cell Biol 127 (3), 273-290 (2007)
   PUBMED   17180682
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Baur,J.A., Pearson,K.J., Price,N.L., Jamieson,H.A., Lerin,C.,
            Kalra,A., Prabhu,V.V., Allard,J.S., Lopez-Lluch,G., Lewis,K.,
            Pistell,P.J., Poosala,S., Becker,K.G., Boss,O., Gwinn,D., Wang,M.,
            Ramaswamy,S., Fishbein,K.W., Spencer,R.G., Lakatta,E.G., Le
            Couteur,D., Shaw,R.J., Navas,P., Puigserver,P., Ingram,D.K., de
            Cabo,R. and Sinclair,D.A.
  TITLE     Resveratrol improves health and survival of mice on a high-calorie
            diet
  JOURNAL   Nature 444 (7117), 337-342 (2006)
   PUBMED   17086191
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Waterham,H.R.
  TITLE     Defects of cholesterol biosynthesis
  JOURNAL   FEBS Lett 580 (23), 5442-5449 (2006)
   PUBMED   16876788
  REMARK    Review article
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Paton,V.G., Shackelford,J.E. and Krisans,S.K.
  TITLE     Cloning and subcellular localization of hamster and rat isopentenyl
            diphosphate dimethylallyl diphosphate isomerase. A PTS1 motif
            targets the enzyme to peroxisomes
  JOURNAL   J Biol Chem 272 (30), 18945-18950 (1997)
   PUBMED   9228075
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Hahn,F.M., Xuan,J.W., Chambers,A.F. and Poulter,C.D.
  TITLE     Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase:
            overproduction, purification, and characterization
  JOURNAL   Arch Biochem Biophys 332 (1), 30-34 (1996)
   PUBMED   8806705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089786.1, BP500454.1, FM059509.1, BP491941.1 and BF389837.1.
            
            On Aug 7, 2012 this sequence version replaced NP_445991.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089786.1, AF003835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..283
                     /product="isopentenyl-diphosphate Delta-isomerase 1"
                     /EC_number="5.3.3.2"
                     /note="IPPI1; IPP isomerase 1; isopentenyl pyrophosphate
                     isomerase 1"
                     /calculated_mol_wt=32371
     Region          56..283
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..283
                     /gene="Idi1"
                     /coded_by="NM_053539.2:237..1088"
                     /db_xref="GeneID:89784"
                     /db_xref="RGD:621835"
ORIGIN      
        1 mwrgralagv igsalkgrgl eaehaaesve vrrsaqlldt plwnrcvlgq irhsvtmpei
       61 nasnldekqv qllaemcili dendnkigad tkknchlnen idkglihraf svflfntenk
      121 lllqqrsdak itfpgcftns ccshplnnpg eleendamgv kraaqrrlka elgipleevd
      181 lnemnyltri yykaqsdgiw geheidyilf lrknvtlnpd pneiksycyv skeelkeilk
      241 keargeiklt pwfkiiadaf lfkwwdnlnh lspfvdheki hrm
//
LOCUS       NP_001178773             281 aa            linear   ROD 27-APR-2025
DEFINITION  very long chain fatty acid elongase 7 [Rattus norvegicus].
ACCESSION   NP_001178773 XP_342193
VERSION     NP_001178773.1
DBSOURCE    REFSEQ: accession NM_001191844.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Ohno,Y., Suto,S., Yamanaka,M., Mizutani,Y., Mitsutake,S.,
            Igarashi,Y., Sassa,T. and Kihara,A.
  TITLE     ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
            synthesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (43), 18439-18444 (2010)
   PUBMED   20937905
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Tamura,K., Makino,A., Hullin-Matsuda,F., Kobayashi,T., Furihata,M.,
            Chung,S., Ashida,S., Miki,T., Fujioka,T., Shuin,T., Nakamura,Y. and
            Nakagawa,H.
  TITLE     Novel lipogenic enzyme ELOVL7 is involved in prostate cancer growth
            through saturated long-chain fatty acid metabolism
  JOURNAL   Cancer Res 69 (20), 8133-8140 (2009)
   PUBMED   19826053
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_342193.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CO568810.1, SRR26643297.6682.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..281
                     /product="very long chain fatty acid elongase 7"
                     /EC_number="2.3.1.199"
                     /note="elongation of very long chain fatty acids protein
                     7; ELOVL FA elongase 7; 3-keto acyl-CoA synthase Elovl7;
                     very long chain 3-oxoacyl-CoA synthase 7; very long chain
                     3-ketoacyl-CoA synthase 7"
                     /calculated_mol_wt=33416
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:A1L3X0; propagated from
                     UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            28..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Region          29..269
                     /region_name="ELO"
                     /note="GNS1/SUR4 family; pfam01151"
                     /db_xref="CDD:460083"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            143..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Region          147..151
                     /region_name="HxxHH motif.
                     /evidence=ECO:0000250|UniProtKB:A1L3X0"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            177..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     Region          277..281
                     /region_name="Di-lysine motif.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03207"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ADY9.1)"
     CDS             1..281
                     /gene="Elovl7"
                     /coded_by="NM_001191844.1:1..846"
                     /db_xref="GeneID:361895"
                     /db_xref="RGD:1310560"
ORIGIN      
        1 mafsdltsrt vrfydnwikd adprvenwll mssplpqtii lglyvyfvts lgpklmenrk
       61 pfelkkamit ynffivlfsv ymcyefvmsg wgtgysfrcd ivdysqspra mrmvhtcwly
      121 yfskfielfd tiffvlrkkn sqvtflhvfh htimpwtwwf gvkfaagglg tfhallntav
      181 hvvmyfyygl camgpayqky lwwkkhltsl qlvqfvlvtv higqiffmed cnyqypvfly
      241 iimsygcifl llflhfwyra ytkgqrlpkt mengnckskh h
//
LOCUS       NP_001289140            1435 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 6 precursor [Rattus
            norvegicus].
ACCESSION   NP_001289140
VERSION     NP_001289140.1
DBSOURCE    REFSEQ: accession NM_001302211.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1435)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1435)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1435)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1435)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1435)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1435)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1435)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1435)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1435)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081152.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            Transcript Variant: This variant (6) lacks two in-frame exons in
            the 3' coding region, but maintains the reading frame, compared to
            variant 1. The resulting isoform (6) lacks two internal segments,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081152.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1435
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1435
                     /product="adhesion G protein-coupled receptor L2 isoform 6
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=158286
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          848..1120
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          1056..1078
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          1082..1107
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Region          1119..1435
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     CDS             1..1435
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001302211.1:463..4770"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleninny rvcdgyyntd lpgswvlgaf allcllgltw sfgllfvnee
     1081 tvvmaylfta fnafqglfif ifhcalqkkv rkeyakcfrh wyccgglpte sphssvkast
     1141 srtsaryssg tqsrirrmwn dtvrkqsess fisgdinsts tlnqghslnn trdtsamdtl
     1201 plngnfnnsy slrkadyhdg vqvvdcglsl ndtafekmii selvhnnlrg snkthnlelk
     1261 lpvkpviggs sseddaivad asslmhgdnp glefrhkele aplipqrths llyqpqkkvk
     1321 peatdsyvsq ltaeadehlq spnrdslyts mpnlrdspyp esspdmaedl spsrrsened
     1381 iyyksmpnlg agrqlqmcyq isrgnsdgyi ipinkegcip egdvregqmq lvtsl
//
LOCUS       NP_037269                910 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial discoidin domain-containing receptor 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_037269
VERSION     NP_037269.2
DBSOURCE    REFSEQ: accession NM_013137.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Wu,R., Pan,S., Chen,Y., Nakano,Y., Li,M., Balog,S. and Tsukamoto,H.
  TITLE     Fate and functional roles of Prominin 1+ cells in liver injury and
            cancer
  JOURNAL   Sci Rep 10 (1), 19412 (2020)
   PUBMED   33173221
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Romayor,I., Badiola,I., Benedicto,A., Marquez,J., Herrero,A.,
            Arteta,B. and Olaso,E.
  TITLE     Silencing of sinusoidal DDR1 reduces murine liver metastasis by
            colon carcinoma
  JOURNAL   Sci Rep 10 (1), 18398 (2020)
   PUBMED   33110221
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Lino,M., Ngai,D., Liu,A., Mohabeer,A., Harper,C., Caruso,L.L.,
            Schroer,S.A., Fu,F., McKee,T., Giacca,A., Woo,M. and Bendeck,M.P.
  TITLE     Discoidin domain receptor 1-deletion ameliorates fibrosis and
            promotes adipose tissue beiging, brown fat activity, and increased
            metabolic rate in a mouse model of cardiometabolic disease
  JOURNAL   Mol Metab 39, 101006 (2020)
   PUBMED   32360427
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Zhong,X., Zhang,W. and Sun,T.
  TITLE     DDR1 promotes breast tumor growth by suppressing antitumor immunity
  JOURNAL   Oncol Rep 42 (6), 2844-2854 (2019)
   PUBMED   31578591
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Chiusa,M., Hu,W., Liao,H.J., Su,Y., Borza,C.M., de Caestecker,M.P.,
            Skrypnyk,N.I., Fogo,A.B., Pedchenko,V., Li,X., Zhang,M.Z.,
            Hudson,B.G., Basak,T., Vanacore,R.M., Zent,R. and Pozzi,A.
  TITLE     The Extracellular Matrix Receptor Discoidin Domain Receptor 1
            Regulates Collagen Transcription by Translocating to the Nucleus
  JOURNAL   J Am Soc Nephrol 30 (9), 1605-1624 (2019)
   PUBMED   31383731
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Vogel,W.F., Aszodi,A., Alves,F. and Pawson,T.
  TITLE     Discoidin domain receptor 1 tyrosine kinase has an essential role
            in mammary gland development
  JOURNAL   Mol Cell Biol 21 (8), 2906-2917 (2001)
   PUBMED   11283268
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Chin,G.S., Lee,S., Hsu,M., Liu,W., Kim,W.J., Levinson,H. and
            Longaker,M.T.
  TITLE     Discoidin domain receptors and their ligand, collagen, are
            temporally regulated in fetal rat fibroblasts in vitro
  JOURNAL   Plast Reconstr Surg 107 (3), 769-776 (2001)
   PUBMED   11304604
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Bhatt,R.S., Tomoda,T., Fang,Y. and Hatten,M.E.
  TITLE     Discoidin domain receptor 1 functions in axon extension of
            cerebellar granule neurons
  JOURNAL   Genes Dev 14 (17), 2216-2228 (2000)
   PUBMED   10970885
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Sanchez,M.P., Tapley,P., Saini,S.S., He,B., Pulido,D. and
            Barbacid,M.
  TITLE     Multiple tyrosine protein kinases in rat hippocampal neurons:
            isolation of Ptk-3, a receptor expressed in proliferative zones of
            the developing brain
  JOURNAL   Proc Natl Acad Sci U S A 91 (5), 1819-1823 (1994)
   PUBMED   8127887
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN935615.1, BC166604.1 and BX883047.1.
            
            On Oct 3, 2009 this sequence version replaced NP_037269.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166604.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..910
                     /product="epithelial discoidin domain-containing receptor
                     1 precursor"
                     /EC_number="2.7.10.1"
                     /note="discoidin domain receptor family, member 1;
                     epithelial discoidin domain-containing receptor 1; cell
                     adhesion kinase; tyrosine kinase DDR; tyrosine-protein
                     kinase CAK; protein-tyrosine kinase PTK-3; CD167
                     antigen-like family member A; discoidin receptor tyrosine
                     kinase; epithelial discoidin domain receptor 1;
                     protein-tyrosine kinase 3; neurotrophic tyrosine kinase
                     receptor type 4"
                     /calculated_mol_wt=99271
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
                     /calculated_mol_wt=1915
     mat_peptide     20..910
                     /product="Epithelial discoidin domain-containing receptor
                     1. /id=PRO_0000016745"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
                     /calculated_mol_wt=99271
     Region          58..185
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(75,106,114)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Region          193..368
                     /region_name="DS-like domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Region          467..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Region          478..481
                     /region_name="PPxY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Region          601..904
                     /region_name="PTKc_DDR1"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 1; cd05096"
                     /db_xref="CDD:133227"
     Site            order(613..617,621,650,652,698..701,704..705,763,767..768,
                     770,781,799..803,812,847)
                     /site_type="active"
                     /db_xref="CDD:133227"
     Site            order(613..614,616..617,621,650,652,698..701,704..705,
                     767..768,770,781)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133227"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            order(763,767,799..803,812,847)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133227"
     Site            780..805
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133227"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     CDS             1..910
                     /gene="Ddr1"
                     /gene_synonym="Cak; Drd1; PTK3D"
                     /coded_by="NM_013137.2:189..2921"
                     /db_xref="GeneID:25678"
                     /db_xref="RGD:2252"
ORIGIN      
        1 mgtgtlssll lllllvtigd admkghfdpa kcryalgmqd rtipdsdisv ssswsdstaa
       61 rhsrlessdg dgawcpagpv fpkeeeylqv dlrrlhlval vgtqgrhagg lgkefsrsyr
      121 lrysrdgrrw mdwkdrwgqe visgnedpgg vvlkdlgppm varlvrfypr adrvmsvclr
      181 velygclwrd gllsytapvg qtmqlsemvy lndstydgyt agglqygglg qladgvvgld
      241 dfrqsqelrv wpgydyvgws nhsfpsgyve mefefdrlrs fqtmqvhcnn mhtlgarlpg
      301 gvecrfkrgp amawegepvr halggslgdp raraisvplg ghvgrflqcr flfagpwllf
      361 seisfisdvv ndssdtfppa pwwppgpppt nfsslelepr gqqpvakaeg sptailigcl
      421 vaiillllli ialmlwrlhw rrllskaerr vleeeltvhl svpgdtilin nrpgpreppp
      481 yqeprprgtp thsapcvpng salllsnpay rlllatyarp prgpgpptpa wakptntqac
      541 sgdymepekp gapllppppq nsvphyaead ivtlqgvtgg ntyavpalpp gavgdgpprv
      601 dfprsrlrfk eklgegqfge vhlcevedpq dlvtsdfpis vqkghpllva vkilrpdatk
      661 narndflkev kimsrlkdpn iirllgvcvq ddplcmitdy mengdlnqfl sahqlenkvt
      721 qglpgdresd qgptisypml lhvgaqiasg mrylatlnfv hrdlatrncl vgenftikia
      781 dfgmsrnlya gdyyrvqgra vlpirwmawe cilmgkftta sdvwafgvtl wevlmlcrsq
      841 pfgqltdeqv ienageffrd qgrqvylsrp pacpqtlyel mlrcwsrepe qrppfsqlhr
      901 fladdalntv
//
LOCUS       NP_001121069             566 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF168 [Rattus norvegicus].
ACCESSION   NP_001121069 XP_001065639 XP_001065698
VERSION     NP_001121069.2
DBSOURCE    REFSEQ: accession NM_001127597.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Panier,S. and Boulton,S.J.
  TITLE     Double-strand break repair: 53BP1 comes into focus
  JOURNAL   Nat Rev Mol Cell Biol 15 (1), 7-18 (2014)
   PUBMED   24326623
  REMARK    Review article
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Mosammaparast,N., Kim,H., Laurent,B., Zhao,Y., Lim,H.J.,
            Majid,M.C., Dango,S., Luo,Y., Hempel,K., Sowa,M.E., Gygi,S.P.,
            Steen,H., Harper,J.W., Yankner,B. and Shi,Y.
  TITLE     The histone demethylase LSD1/KDM1A promotes the DNA damage response
  JOURNAL   J Cell Biol 203 (3), 457-470 (2013)
   PUBMED   24217620
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Fradet-Turcotte,A., Canny,M.D., Escribano-Diaz,C., Orthwein,A.,
            Leung,C.C., Huang,H., Landry,M.C., Kitevski-LeBlanc,J.,
            Noordermeer,S.M., Sicheri,F. and Durocher,D.
  TITLE     53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin
            mark
  JOURNAL   Nature 499 (7456), 50-54 (2013)
   PUBMED   23760478
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Mattiroli,F., Vissers,J.H., van Dijk,W.J., Ikpa,P., Citterio,E.,
            Vermeulen,W., Marteijn,J.A. and Sixma,T.K.
  TITLE     RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage
            signaling
  JOURNAL   Cell 150 (6), 1182-1195 (2012)
   PUBMED   22980979
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Panier,S., Ichijima,Y., Fradet-Turcotte,A., Leung,C.C., Kaustov,L.,
            Arrowsmith,C.H. and Durocher,D.
  TITLE     Tandem protein interaction modules organize the ubiquitin-dependent
            response to DNA double-strand breaks
  JOURNAL   Mol Cell 47 (3), 383-395 (2012)
   PUBMED   22742833
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Shanbhag,N.M., Rafalska-Metcalf,I.U., Balane-Bolivar,C.,
            Janicki,S.M. and Greenberg,R.A.
  TITLE     ATM-dependent chromatin changes silence transcription in cis to DNA
            double-strand breaks
  JOURNAL   Cell 141 (6), 970-981 (2010)
   PUBMED   20550933
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Ramachandran,S., Chahwan,R., Nepal,R.M., Frieder,D., Panier,S.,
            Roa,S., Zaheen,A., Durocher,D., Scharff,M.D. and Martin,A.
  TITLE     The RNF8/RNF168 ubiquitin ligase cascade facilitates class switch
            recombination
  JOURNAL   Proc Natl Acad Sci U S A 107 (2), 809-814 (2010)
   PUBMED   20080757
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Pinato,S., Scandiuzzi,C., Arnaudo,N., Citterio,E., Gaudino,G. and
            Penengo,L.
  TITLE     RNF168, a new RING finger, MIU-containing protein that modifies
            chromatin by ubiquitination of histones H2A and H2AX
  JOURNAL   BMC Mol Biol 10, 55 (2009)
   PUBMED   19500350
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Doil,C., Mailand,N., Bekker-Jensen,S., Menard,P., Larsen,D.H.,
            Pepperkok,R., Ellenberg,J., Panier,S., Durocher,D., Bartek,J.,
            Lukas,J. and Lukas,C.
  TITLE     RNF168 binds and amplifies ubiquitin conjugates on damaged
            chromosomes to allow accumulation of repair proteins
  JOURNAL   Cell 136 (3), 435-446 (2009)
   PUBMED   19203579
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Stewart,G.S., Panier,S., Townsend,K., Al-Hakim,A.K., Kolas,N.K.,
            Miller,E.S., Nakada,S., Ylanko,J., Olivarius,S., Mendez,M.,
            Oldreive,C., Wildenhain,J., Tagliaferro,A., Pelletier,L.,
            Taubenheim,N., Durandy,A., Byrd,P.J., Stankovic,T., Taylor,A.M. and
            Durocher,D.
  TITLE     The RIDDLE syndrome protein mediates a ubiquitin-dependent
            signaling cascade at sites of DNA damage
  JOURNAL   Cell 136 (3), 420-434 (2009)
   PUBMED   19203578
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC166869.1 and JAXUCZ010000011.1.
            
            On Aug 30, 2012 this sequence version replaced NP_001121069.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166869.1, SRR26360172.548336.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..566
                     /product="E3 ubiquitin-protein ligase RNF168"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 168, E3 ubiquitin protein
                     ligase; RING-type E3 ubiquitin transferase RNF168"
                     /calculated_mol_wt=64533
     Region          16..63
                     /region_name="RING-HC_RNF168"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 168 (RNF168) and similar proteins; cd16550"
                     /db_xref="CDD:438212"
     Region          112..185
                     /region_name="UDM1_RNF168"
                     /note="UDM1 (ubiquitin-dependent DSB recruitment module 1)
                     domain found in RING finger protein 168; cd22265"
                     /db_xref="CDD:409018"
     Site            order(112..113,116,118..119,121..122,125,133..134,137,
                     140..141,143..145,147..148,151,156)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:409018"
     Region          432..482
                     /region_name="MIU2_RNF168"
                     /note="second motif interacting with ubiquitin domain
                     found in RING finger protein 168; cd21952"
                     /db_xref="CDD:409266"
     Site            order(444,446..448,450..452,454..455,457..459,475..478)
                     /site_type="other"
                     /note="putative histone/ubiquitin binding site
                     [polypeptide binding]"
                     /db_xref="CDD:409266"
     CDS             1..566
                     /gene="Rnf168"
                     /coded_by="NM_001127597.2:16..1716"
                     /db_xref="GeneID:690043"
                     /db_xref="RGD:1585168"
ORIGIN      
        1 mkmaapknsi pslaecqcgi cmeilvepvt lpcnhtlcnp cfqstvekan lccpfcrrrv
       61 sswtryhtrr nslvntdlwe iiqkhyakec klrisgqesk eivdeyqpvr llskpgelrr
      121 eyeeeiskve aerqaskeee nkaseeyiqr llaeeeeeek rrterrrsem eeqlrgdeel
      181 arrlstsins nyernilasp lssrksdpvt nksqkkntnk qknfgdiqry lspkskpgta
      241 wacktehged mcksketdss dtkspvlqdt dveesmpths pqtcpetqgq gpepltempv
      301 pwlcarnaeq clegkaeavs tnpddscivn dggpraivsn skeaavkppt kieneeysvs
      361 gvtqltggng vptesrvydl lvgkeisere nqesvfeevm dpcfsakrrk ifitssldqe
      421 etevnftqkl idlehmlfer hkqeeqdrll alqlqkeadk ekmvpnrqkg spdqyqlrts
      481 sppdgllngq rknvkdrnsp kqtadrsksq rsrkgeywet festwkgsvn gtkmptprkd
      541 scnvskracp lqhrsaqksi lqmfqr
//
LOCUS       NP_001258053             422 aa            linear   ROD 27-APR-2025
DEFINITION  pro-neuregulin-1, membrane-bound isoform isoform 7 [Rattus
            norvegicus].
ACCESSION   NP_001258053
VERSION     NP_001258053.1
DBSOURCE    REFSEQ: accession NM_001271124.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yuan,J., Xu,B., Ma,J., Pang,X., Fu,Y., Liang,M., Wang,M., Pan,Y.,
            Duan,Y., Tang,M., Zhu,B., Laher,I. and Li,S.
  TITLE     MOTS-c and aerobic exercise induce cardiac physiological adaptation
            via NRG1/ErbB4/CEBPbeta modification in rats
  JOURNAL   Life Sci 315, 121330 (2023)
   PUBMED   36584915
  REMARK    GeneRIF: MOTS-c and aerobic exercise induce cardiac physiological
            adaptation via NRG1/ErbB4/CEBPbeta modification in rats.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Wang,Y.K., Yang,W.X., Liu,R., Guo,J.B., Zhang,Y.M., Li,K., Lu,Y.
            and Wang,J.
  TITLE     Changes in Type II NRG-1 Expression during Regeneration Following
            Autologous Nerve Transplantation in Rats
  JOURNAL   Turk Neurosurg 33 (1), 18-24 (2023)
   PUBMED   35416257
  REMARK    GeneRIF: Changes in Type II NRG-1 Expression during Regeneration
            Following Autologous Nerve Transplantation in Rats.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Banerjee,S., Mishra,S., Xu,W., Thompson,W.E. and Chowdhury,I.
  TITLE     Neuregulin-1 signaling regulates cytokines and chemokines
            expression and secretion in granulosa cell
  JOURNAL   J Ovarian Res 15 (1), 86 (2022)
   PUBMED   35883098
  REMARK    GeneRIF: Neuregulin-1 signaling regulates cytokines and chemokines
            expression and secretion in granulosa cell.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Li,S., Wang,M., Ma,J., Pang,X., Yuan,J., Pan,Y., Fu,Y. and Laher,I.
  TITLE     MOTS-c and Exercise Restore Cardiac Function by Activating of
            NRG1-ErbB Signaling in Diabetic Rats
  JOURNAL   Front Endocrinol (Lausanne) 13, 812032 (2022)
   PUBMED   35370955
  REMARK    GeneRIF: MOTS-c and Exercise Restore Cardiac Function by Activating
            of NRG1-ErbB Signaling in Diabetic Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Xu,L., Li,Z., Rong,J. and Lang,L.
  TITLE     Effect of regulation of the NRG1/ErbB4 signaling pathway on the
            visual cortex synaptic plasticity of amblyopic adult rats
  JOURNAL   J Biochem Mol Toxicol 35 (9), e22841 (2021)
   PUBMED   34273906
  REMARK    GeneRIF: Effect of regulation of the NRG1/ErbB4 signaling pathway
            on the visual cortex synaptic plasticity of amblyopic adult rats.
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Meyer,D. and Birchmeier,C.
  TITLE     Multiple essential functions of neuregulin in development
  JOURNAL   Nature 378 (6555), 386-390 (1995)
   PUBMED   7477375
  REMARK    Erratum:[Nature 1995 Dec 14;378(6558):753]
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Sliwkowski,M.X., Schaefer,G., Akita,R.W., Lofgren,J.A.,
            Fitzpatrick,V.D., Nuijens,A., Fendly,B.M., Cerione,R.A.,
            Vandlen,R.L. and Carraway,K.L. 3rd.
  TITLE     Coexpression of erbB2 and erbB3 proteins reconstitutes a high
            affinity receptor for heregulin
  JOURNAL   J Biol Chem 269 (20), 14661-14665 (1994)
   PUBMED   7514177
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Wen,D., Suggs,S.V., Karunagaran,D., Liu,N., Cupples,R.L., Luo,Y.,
            Janssen,A.M., Ben-Baruch,N., Trollinger,D.B., Jacobsen,V.L. et al.
  TITLE     Structural and functional aspects of the multiplicity of Neu
            differentiation factors
  JOURNAL   Mol Cell Biol 14 (3), 1909-1919 (1994)
   PUBMED   7509448
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Wen,D., Peles,E., Cupples,R., Suggs,S.V., Bacus,S.S., Luo,Y.,
            Trail,G., Hu,S., Silbiger,S.M., Levy,R.B. et al.
  TITLE     Neu differentiation factor: a transmembrane glycoprotein containing
            an EGF domain and an immunoglobulin homology unit
  JOURNAL   Cell 69 (3), 559-572 (1992)
   PUBMED   1349853
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Peles,E., Bacus,S.S., Koski,R.A., Lu,H.S., Wen,D., Ogden,S.G.,
            Levy,R.B. and Yarden,Y.
  TITLE     Isolation of the neu/HER-2 stimulatory ligand: a 44 kd glycoprotein
            that induces differentiation of mammary tumor cells
  JOURNAL   Cell 69 (1), 205-216 (1992)
   PUBMED   1348215
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            coding sequence and the 3' UTR and coding sequence, lacks two
            alternate coding exons, and contains another alternate coding exon
            compared to variant 1. The resulting isoform (7) has a shorter and
            distinct N-terminus, a shorter C-terminus, and contains an
            alternate internal segment compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U02324.1, M92430.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..422
                     /product="pro-neuregulin-1, membrane-bound isoform isoform
                     7"
                     /note="neuregulin 1 type III beta 3; pro-NRG1; glial
                     growth factor"
                     /calculated_mol_wt=46192
     Region          37..129
                     /region_name="Ig_Pro_neuregulin-1"
                     /note="Immunoglobulin (Ig)-like domain found in neuregulin
                     (NRG)-1; cd05895"
                     /db_xref="CDD:409476"
     Region          37..43
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409476"
     Region          51..59
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409476"
     Region          66..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409476"
     Region          85..90
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409476"
     Region          95..99
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409476"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409476"
     Region          121..129
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409476"
     Region          <182..274
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     Region          190..220
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          267..>422
                     /region_name="Neuregulin"
                     /note="Neuregulin intracellular region; pfam02158"
                     /db_xref="CDD:426627"
     CDS             1..422
                     /gene="Nrg1"
                     /coded_by="NM_001271124.1:345..1613"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:112400"
                     /db_xref="RGD:621341"
ORIGIN      
        1 mserkegrgk gkgkkkdrgs rgkpgpaegd pspalpprlk emksqesaag sklvlrcets
       61 seysslrfkw fkngnelnrk nkpenikiqk kpgkselrin kasladsgey mckvisklgn
      121 dsasanitiv esnefitgmp astetayvss espirisvst egantsssts tsttgtshli
      181 kcaekektfc vnggecftvk dlsnpsrylc kcqpgftgar ctenvpmkvq tqekaeelyq
      241 krvltitgic iallvvgimc vvaycktkkq rqklhdrlrq slrsersnlv niangphhpn
      301 pppenvqlvn qyvsknviss ehiverevet sfstshytst ahhsttvtqt pshswsnght
      361 esiisesnsv immssvensr hsspaggprg rlhglggprd nsflrharet pdsyrdsphs
      421 er
//
LOCUS       NP_001094335             356 aa            linear   ROD 27-APR-2025
DEFINITION  septin-12 [Rattus norvegicus].
ACCESSION   NP_001094335 XP_001079122 XP_343860
VERSION     NP_001094335.1
DBSOURCE    REFSEQ: accession NM_001100865.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Kuo,Y.C., Shen,Y.R., Chen,H.I., Lin,Y.H., Wang,Y.Y., Chen,Y.R.,
            Wang,C.Y. and Kuo,P.L.
  TITLE     SEPT12 orchestrates the formation of mammalian sperm annulus by
            organizing core octameric complexes with other SEPT proteins
  JOURNAL   J Cell Sci 128 (5), 923-934 (2015)
   PUBMED   25588830
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Kuo,Y.C., Lin,Y.H., Chen,H.I., Wang,Y.Y., Chiou,Y.W., Lin,H.H.,
            Pan,H.A., Wu,C.M., Su,S.M., Hsu,C.C. and Kuo,P.L.
  TITLE     SEPT12 mutations cause male infertility with defective sperm
            annulus
  JOURNAL   Hum Mutat 33 (4), 710-719 (2012)
   PUBMED   22275165
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Ding,X., Yu,W., Liu,M., Shen,S., Chen,F., Cao,L., Wan,B. and Yu,L.
  TITLE     GTP binding is required for SEPT12 to form filaments and to
            interact with SEPT11
  JOURNAL   Mol Cells 25 (3), 385-389 (2008)
   PUBMED   18443421
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Ding,X., Yu,W., Liu,M., Shen,S., Chen,F., Wan,B. and Yu,L.
  TITLE     SEPT12 interacts with SEPT6 and this interaction alters the
            filament structure of SEPT6 in Hela cells
  JOURNAL   J Biochem Mol Biol 40 (6), 973-978 (2007)
   PUBMED   18047794
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Steels,J.D., Estey,M.P., Froese,C.D., Reynaud,D., Pace-Asciak,C.
            and Trimble,W.S.
  TITLE     Sept12 is a component of the mammalian sperm tail annulus
  JOURNAL   Cell Motil Cytoskeleton 64 (10), 794-807 (2007)
   PUBMED   17685441
  REMARK    GeneRIF: Study describes Sept12, a novel septin, identified in a
            yeast two hybrid screen using Sept5 as the bait; Sept12 protein
            levels rise upon sexual maturity and the Sept12 protein colocalizes
            with the annulus in isolated mature spermatozoa.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097401.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_001079122.1, XP_343860.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097401.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..356
                     /product="septin-12"
                     /calculated_mol_wt=40668
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Region          44..317
                     /region_name="Interaction with SEPTIN7.
                     /evidence=ECO:0000250|UniProtKB:Q8IYM1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Region          45..315
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          54..61
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Site            54..61
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(56..62,110,113,192..193,195,249..250)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            85..93
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            87
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          110..113
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Site            110..113
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            112..158
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          192..195
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Site            192..195
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            249..251
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Region          256..356
                     /region_name="Self-association (via N-terminus) to
                     polymerize octameric septin 12-7-6-2/4-2/4-6-7-12
                     filaments. /evidence=ECO:0000250|UniProtKB:Q8IYM1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     Region          330..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G5.2)"
     CDS             1..356
                     /gene="Septin12"
                     /gene_synonym="Sept12"
                     /coded_by="NM_001100865.1:78..1148"
                     /db_xref="GeneID:363542"
                     /db_xref="RGD:1565511"
ORIGIN      
        1 mderrtpspc ssrpssprtp pcemfgpvgi eavldqlrik amktgfefni mvvgqsglgk
       61 stmvntlfks kvwqspapnl dvpmpqtlel hsvthvieek glklkltvtd tpgfgdqinn
      121 dkcwdpilsy inqqyeqylq eellitrqrh ipdtrvhccv yfvpptghcl rpldieflrr
      181 lcrtvnvvpv iaradsltie erdafrsriq qnlknhcidv ypqqcfdedi ndrllnskir
      241 eqipfavvga drehivngrc vlgrktkwgi ievenmahce flllrdllir shlqdlkdit
      301 hnvhyenyrv lrlneshvlp rgpgwvnlap aspgqlmapg pekvrkrskd prddec
//
LOCUS       NP_073184                961 aa            linear   ROD 27-APR-2025
DEFINITION  SH3 domain-binding protein 4 [Rattus norvegicus].
ACCESSION   NP_073184
VERSION     NP_073184.3
DBSOURCE    REFSEQ: accession NM_022693.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Kim,Y.M. and Kim,D.H.
  TITLE     dRAGging amino acid-mTORC1 signaling by SH3BP4
  JOURNAL   Mol Cells 35 (1), 1-6 (2013)
   PUBMED   23274731
  REMARK    GeneRIF: SH3 binding protein 4 (SH3BP4) has been identified as a
            negative regulator of Rag GTPases under amino acid starvation. Rag
            GTPase heterodimers regulate the amino acid-mTORC1 pathway, a
            master regulator of cell growth and autophagy.
            Review article
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Kim,Y.M., Stone,M., Hwang,T.H., Kim,Y.G., Dunlevy,J.R.,
            Griffin,T.J. and Kim,D.H.
  TITLE     SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1
            signaling
  JOURNAL   Mol Cell 46 (6), 833-846 (2012)
   PUBMED   22575674
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 961)
  AUTHORS   Tosoni,D., Puri,C., Confalonieri,S., Salcini,A.E., De Camilli,P.,
            Tacchetti,C. and Di Fiore,P.P.
  TITLE     TTP specifically regulates the internalization of the transferrin
            receptor
  JOURNAL   Cell 123 (5), 875-888 (2005)
   PUBMED   16325581
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM034920.1 and JAXUCZ010000009.1.
            
            On Mar 2, 2013 this sequence version replaced NP_073184.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2068670.1,
                                           SRR26360176.2068888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..961
                     /product="SH3 domain-binding protein 4"
                     /calculated_mol_wt=107352
     Region          59..110
                     /region_name="SH3_SH3BP4"
                     /note="Src Homology 3 domain of SH3 domain-binding protein
                     4; cd11757"
                     /db_xref="CDD:212691"
     Site            order(64,66,69,73,91..92,105,107..108)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212691"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921I6; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0V3; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0V3; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Region          321..402
                     /region_name="ZU5"
                     /note="ZU5 domain; cl02517"
                     /db_xref="CDD:470600"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0V3; propagated from
                     UniProtKB/Swiss-Prot (Q9JJS5.2)"
     Region          656..720
                     /region_name="SH3_2"
                     /note="Variant SH3 domain; pfam07653"
                     /db_xref="CDD:429575"
     CDS             1..961
                     /gene="Sh3bp4"
                     /coded_by="NM_022693.4:383..3268"
                     /db_xref="GeneID:64634"
                     /db_xref="RGD:620219"
ORIGIN      
        1 maaqriraan ssglprckse gtlidlsegf setsfndvkv pspsallvdn ptpfgnakev
       61 iaikdycpnn fttlkfskgd hlyvldtsgg ewwyahntte mgyipssyvq plnyrnstls
      121 dsgmidnlpd spdevakeld llggwtddqk qsgrpysnnp fwngvrtnpf lngnaqpsmd
      181 elnpkstvdl llfdtgtssf tesssattns tgnifdelpa tngihleqpv krdnpffrsk
      241 rsyslselsv lqaksdappt ssfftglksp apeqfqsred frtawlnhrk larschdldl
      301 lgqspgwgqt qavetnivck ldssggsvql pdtsisihvp eghvapgetq qismkalldp
      361 pldlnsdrst sispvvevkl snlevstfii lemkvsaevk gdifskstvv lqclrsdske
      421 gpyapiplay sygdtiqvql dnlepcmyla ivaqgsnily pstvwdfihk rvtvglygpk
      481 hihpsfktvv tifghdcapk tllvtevtrq apspapvalq lwgkhqfils rpqdlrvcmf
      541 snmtnydvks neqakvvrgf qmklgkvsrl ifsvisqnpn elsdftlrvq vkddqdailt
      601 qfcvqtpqpp pksaikpsgq rrflkknevg kiilspfvvt tkyptfqdrp vsslkfgkll
      661 ktvvrqnksh ylleykkgdv vallseerir lkgqlwtkew yigyyqgkvg lvhtknvlvv
      721 gkarpslfsg pelstsvlle qilrpckflt yiyasvrtll menisswraf adalgygnlp
      781 ltffcraeld sepervasvl eklkedcnnp dnkdrksfqk elvmallkmd cqglvvrliq
      841 dfvllttave vaqrwrelae klakvskqqm dayesphrdr ngvvdseamw kpaydflltw
      901 shqigdsyrd viqelhigld kmknpitrrw khltgtlilv nsldilraaa fspadhddfv
      961 i
//
LOCUS       NP_001013146             204 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity protein phosphatase 18 [Rattus norvegicus].
ACCESSION   NP_001013146 XP_223560
VERSION     NP_001013146.2
DBSOURCE    REFSEQ: accession NM_001013128.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Jeong,D.G., Wei,C.H., Ku,B., Jeon,T.J., Chien,P.N., Kim,J.K.,
            Park,S.Y., Hwang,H.S., Ryu,S.Y., Park,H., Kim,D.S., Kim,S.J. and
            Ryu,S.E.
  TITLE     The family-wide structure and function of human dual-specificity
            protein phosphatases
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 421-435 (2014)
   PUBMED   24531476
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Rardin,M.J., Wiley,S.E., Murphy,A.N., Pagliarini,D.J. and
            Dixon,J.E.
  TITLE     Dual specificity phosphatases 18 and 21 target to opposing sides of
            the mitochondrial inner membrane
  JOURNAL   J Biol Chem 283 (22), 15440-15450 (2008)
   PUBMED   18385140
  REMARK    GeneRIF: Dual specificity phosphatases 18 and 21 target to opposing
            sides of the mitochondrial inner membrane
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Wu,Q., Gu,S., Dai,J., Dai,J., Wang,L., Li,Y., Zeng,L., Xu,J.,
            Ye,X., Zhao,W., Ji,C., Xie,Y. and Mao,Y.
  TITLE     Molecular cloning and characterization of a novel dual-specificity
            phosphatase18 gene from human fetal brain
  JOURNAL   Biochim Biophys Acta 1625 (3), 296-304 (2003)
   PUBMED   12591617
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Hood,K.L., Tobin,J.F. and Yoon,C.
  TITLE     Identification and characterization of two novel
            low-molecular-weight dual specificity phosphatases
  JOURNAL   Biochem Biophys Res Commun 298 (4), 545-551 (2002)
   PUBMED   12408986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1 and BC079285.1.
            
            On Mar 21, 2013 this sequence version replaced NP_001013146.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079285.1, SRR26360181.2687986.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 18385140
            NMD candidate                      :: PMID: 18385140
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..204
                     /product="dual specificity protein phosphatase 18"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /calculated_mol_wt=22595
     Region          19..176
                     /region_name="DUSP18_21"
                     /note="dual specificity protein phosphatases 18 and 21;
                     cd14573"
                     /db_xref="CDD:350421"
     Region          95..141
                     /region_name="Sufficient for mitochondrial localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW7.1)"
     CDS             1..204
                     /gene="Dusp18"
                     /coded_by="NM_001013128.2:226..840"
                     /db_xref="GeneID:305477"
                     /db_xref="RGD:1306929"
ORIGIN      
        1 mtspwsacpv qfpqpsisgl sqitkslfis ngaaandkll lssnqittvi nvsvevantf
       61 yediqyvqvp vvdapiarls dffdpiadhi hsvemkqgrt llhcaagvsr saalclaylm
      121 kyhamsllda hawtksrrpi irpnsgfweq lihyefqlfg kntmqmvnsp mglipdiyek
      181 etrmmiplst pdgafhkgke kall
//
LOCUS       NP_001184170             648 aa            linear   ROD 27-APR-2025
DEFINITION  rab11 family-interacting protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001184170 XP_001070627
VERSION     NP_001184170.1
DBSOURCE    REFSEQ: accession NM_001197241.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Carson,B.P., Del Bas,J.M., Moreno-Navarrete,J.M.,
            Fernandez-Real,J.M. and Mora,S.
  TITLE     The rab11 effector protein FIP1 regulates adiponectin trafficking
            and secretion
  JOURNAL   PLoS One 8 (9), e74687 (2013)
   PUBMED   24040321
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Eva,R., Dassie,E., Caswell,P.T., Dick,G., ffrench-Constant,C.,
            Norman,J.C. and Fawcett,J.W.
  TITLE     Rab11 and its effector Rab coupling protein contribute to the
            trafficking of beta 1 integrins during axon growth in adult dorsal
            root ganglion neurons and PC12 cells
  JOURNAL   J Neurosci 30 (35), 11654-11669 (2010)
   PUBMED   20810886
  REMARK    GeneRIF: An interaction with Rab11 is necessary for long-range
            targeting of beta1 integrins to the growth cone along axons and in
            neurons.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC107469.1 and JAXUCZ010000016.1.
            
            On Oct 15, 2010 this sequence version replaced XP_001070627.2.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107469.1, FQ221846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..648
                     /product="rab11 family-interacting protein 1 isoform 2"
                     /note="rab11 family-interacting protein 1; rab-coupling
                     protein; RAB11 family interacting protein 1 (class I)"
                     /calculated_mol_wt=71013
     Region          20..150
                     /region_name="C2_Rab11-FIP_classI"
                     /note="C2 domain found in Rab11-family interacting
                     proteins (FIP) class I; cd08682"
                     /db_xref="CDD:176064"
     Region          164..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D620; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D620; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4; propagated from
                     UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          483..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          516..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          584..648
                     /region_name="Necessary for interaction with RAB4A and
                     RAB11A, subcellular location and endosomal recycling.
                     /evidence=ECO:0000250|UniProtKB:Q6WKZ4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7T9.1)"
     Region          591..638
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..648
                     /gene="Rab11fip1"
                     /gene_synonym="Rab11-FIP1; RGD1562965"
                     /coded_by="NM_001197241.1:48..1994"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:498650"
                     /db_xref="RGD:1562965"
ORIGIN      
        1 mslaasagrg pgtmwspthv qvtvlqargl rakgpggtsd ayaviqvgke kyatsvsers
       61 lgapvwreea tfelppllss gtapaaaaat lqltvlhral lgldkflgra evdlrelhrd
      121 qsrrkkqwyt lkskpgkkdk ergeievdiq fmrnnmtasm fdlsmkdksr npfgklkdki
      181 kgknkdntsd tasaivpstt psvdsddesf skdkkkkski ktlfskpslq ktplsqsmsv
      241 lptskpdkvl lrpgdfqsrw gdegdnedes ssasevmsqk rtsstdhtqp nqsnfslpkk
      301 eglsflgglr skndslsrsn vcingnhvym eqpeakseir esspsnspsp qgfrkrhlfs
      361 stenlaarsp kepgegggms sdrrlsdsst kdsmksmslp syrplttads reglspanme
      421 vatketkdsk kqeskkssll slvtgkkdva kgsegeplpp vsekekgrkg vlveaqlree
      481 dlvrrpekda vpvasqwgss qnpfedaqis dleasveskc epkppvpvpr tpqtravkpr
      541 phpvkpmntt apkitnsslg tatiisenli nealmkkyqp sdpafayaql thdeliqlvl
      601 kqketiskke fqvreledyi dnllvrvmee tpnilrvpaq tgkkagkm
//
LOCUS       NP_001289139            1452 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 5 precursor [Rattus
            norvegicus].
ACCESSION   NP_001289139
VERSION     NP_001289139.1
DBSOURCE    REFSEQ: accession NM_001302210.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1452)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1452)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1452)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1452)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1452)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1452)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1452)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1452)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1452)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081148.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            Transcript Variant: This variant (5) lacks two consecutive exons
            and has an alternate splice site in the 3' coding region, but
            maintains the reading frame, compared to variant 1. The resulting
            isoform (5) lacks two internal segments, compared to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081148.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1452
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1452
                     /product="adhesion G protein-coupled receptor L2 isoform 5
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=159989
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          848..1105
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320672"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320672"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320672"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320672"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1041..1063
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1067..1092
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1104..1452
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     CDS             1..1452
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001302210.1:463..4821"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleniksw vlgafallcl lgltwsfgll fvneetvvma ylftafnafq
     1081 glfififhca lqkkvrkeya kcfrhwyccg glptesphss vkastsrtsa ryssgtqsri
     1141 rrmwndtvrk qsessfisgm tgnylltnpl lrphgtnnpy ntllaetvvc napsapvfns
     1201 pghslnntrd tsamdtlpln gnfnnsyslr kadyhdgvqv vdcglslndt afekmiisel
     1261 vhnnlrgsnk thnlelklpv kpviggssse ddaivadass lmhgdnpgle frhkeleapl
     1321 ipqrthslly qpqkkvkpea tdsyvsqlta eadehlqspn rdslytsmpn lrdspypess
     1381 pdmaedlsps rrsenediyy ksmpnlgagr qlqmcyqisr gnsdgyiipi nkegcipegd
     1441 vregqmqlvt sl
//
LOCUS       NP_001295183             815 aa            linear   ROD 27-APR-2025
DEFINITION  aryl hydrocarbon receptor isoform 2 [Rattus norvegicus].
ACCESSION   NP_001295183
VERSION     NP_001295183.1
DBSOURCE    REFSEQ: accession NM_001308254.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Andersen,M.E., Barutcu,A.R., Black,M.B. and Harrill,J.A.
  TITLE     Transcriptomic analysis of AHR wildtype and Knock-out rat livers
            supports TCDD's role in AHR/ARNT-mediated circadian disruption and
            hepatotoxicity
  JOURNAL   Toxicol Appl Pharmacol 487, 116956 (2024)
   PUBMED   38735589
  REMARK    GeneRIF: Transcriptomic analysis of AHR wildtype and Knock-out rat
            livers supports TCDD's role in AHR/ARNT-mediated circadian
            disruption and hepatotoxicity.
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Chausse,A.M., Roche,S.M., Moroldo,M., Hennequet-Antier,C.,
            Holbert,S., Kempf,F., Barilleau,E., Trotereau,J. and Velge,P.
  TITLE     Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis
  JOURNAL   Virulence 14 (1), 2158663 (2023)
   PUBMED   36600181
  REMARK    GeneRIF: Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis.
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Xu,J., Sun,X., Qin,F., Wang,X., Chen,Q. and Yan,R.
  TITLE     Protective effects of salvianolic acid B on intestinal
            ischemia/reperfusion injury in rats by regulating the
            AhR/IL-22/STAT6 axis
  JOURNAL   J Recept Signal Transduct Res 43 (3), 73-82 (2023)
   PUBMED   37387514
REFERENCE   4  (residues 1 to 815)
  AUTHORS   Kouno,T., Zeng,S., Wang,Y., Duan,Y., Lang,S., Gao,B., Hartmann,P.,
            Cabre,N., Llorente,C., Galbert,C., Emond,P., Sokol,H., James,M.,
            Chao,C.C., Gao,J.R., Perreault,M., Hava,D.L. and Schnabl,B.
  TITLE     Engineered bacteria producing aryl-hydrocarbon receptor agonists
            protect against ethanol-induced liver disease in mice
  JOURNAL   Alcohol Clin Exp Res (Hoboken) 47 (5), 856-867 (2023)
   PUBMED   36871955
REFERENCE   5  (residues 1 to 815)
  AUTHORS   Nori,P., Haghshenas,R., Aftabi,Y. and Akbari,H.
  TITLE     Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery
  JOURNAL   Sci Rep 13 (1), 3721 (2023)
   PUBMED   36879035
  REMARK    GeneRIF: Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 815)
  AUTHORS   Fernandez-Salguero,P., Pineau,T., Hilbert,D.M., McPhail,T.,
            Lee,S.S., Kimura,S., Nebert,D.W., Rudikoff,S., Ward,J.M. and
            Gonzalez,F.J.
  TITLE     Immune system impairment and hepatic fibrosis in mice lacking the
            dioxin-binding Ah receptor
  JOURNAL   Science 268 (5211), 722-726 (1995)
   PUBMED   7732381
REFERENCE   7  (residues 1 to 815)
  AUTHORS   Elferink,C.J. and Whitlock,J.P. Jr.
  TITLE     Dioxin-dependent, DNA sequence-specific binding of a multiprotein
            complex containing the Ah receptor
  JOURNAL   Receptor 4 (3), 157-173 (1994)
   PUBMED   7812217
REFERENCE   8  (residues 1 to 815)
  AUTHORS   Puga,A., Nebert,D.W. and Carrier,F.
  TITLE     Dioxin induces expression of c-fos and c-jun proto-oncogenes and a
            large increase in transcription factor AP-1
  JOURNAL   DNA Cell Biol 11 (4), 269-281 (1992)
   PUBMED   1605850
REFERENCE   9  (residues 1 to 815)
  AUTHORS   Ema,M., Sogawa,K., Watanabe,N., Chujoh,Y., Matsushita,N., Gotoh,O.,
            Funae,Y. and Fujii-Kuriyama,Y.
  TITLE     cDNA cloning and structure of mouse putative Ah receptor
  JOURNAL   Biochem Biophys Res Commun 184 (1), 246-253 (1992)
   PUBMED   1314586
REFERENCE   10 (residues 1 to 815)
  AUTHORS   Okino,S.T., Pendurthi,U.R. and Tukey,R.H.
  TITLE     Phorbol esters inhibit the dioxin receptor-mediated transcriptional
            activation of the mouse Cyp1a-1 and Cyp1a-2 genes by
            2,3,7,8-tetrachlorodibenzo-p-dioxin
  JOURNAL   J Biol Chem 267 (10), 6991-6998 (1992)
   PUBMED   1313028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            Transcript Variant: This variant (2) uses an alternate splice
            junction in the 3' end of the coding sequence compared to variant
            1. The resulting isoform (2) has a shorter and distinct C-terminus
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF082125.1, AM902285.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..815
                     /product="aryl hydrocarbon receptor isoform 2"
                     /note="ah receptor"
                     /calculated_mol_wt=92205
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          12..15
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          27..87
                     /region_name="bHLH-PAS_AhR"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in aryl hydrocarbon receptor (AhR) and
                     similar proteins; cd11436"
                     /db_xref="CDD:381442"
     Site            order(33..39,41,43,64..66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381442"
     Region          36..41
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          37..65
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Site            order(38,41..42,45..46,48..49,52..56,64..66,69..79,82,
                     85..86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381442"
     Region          49..81
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          63..71
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          111..>181
                     /region_name="PAS"
                     /note="PAS fold; pfam00989"
                     /db_xref="CDD:395786"
     Region          116..124
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P30561"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          264..266
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P30561"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          295..380
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(298,302,308,322..325,351,356)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(319,323,331,334..335,363,365)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          429..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     CDS             1..815
                     /gene="Ahr"
                     /coded_by="NM_001308254.1:29..2476"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25690"
                     /db_xref="RGD:2074"
ORIGIN      
        1 mssganitya srkrrkpvqk tvkpvpaegi ksnpskrhrd rlnteldrla sllpfpqdvi
       61 skldklsvlr lsvsylraks ffdvalkstp adrsrgqdqc raqvrdwqdl qegefllqal
      121 ngfvlvvtad alvfyassti qdylgfqqsd vihqsvyeli htedraefqr qlhwalnpsq
      181 ctdsaqgvde thglpqpavy ytpdqlppen tafmercfrc rlrclldnss gflamnfqgr
      241 lkylhgqnkk gkdgallppq lalfaiatpl qppsileirt knfifrtkhk ldftpigcda
      301 kgqlilgyte velcnkgsgy qfihaadmlh caeshirmik tgesgmtvfr llakhsrwrw
      361 vqsnarliyr ngrpdyiiat qrpltdeegr ehlqkrsmtl pfmfatgkav lyeisspfsp
      421 imdplpirtk sntsrkdwap qstpskdsfh pnslmsaliq qdesiylcpp sspapldshf
      481 lmdsmsecgs wqgsfaaasn eallkheeir htqdvnltls ggpselfpdn knndlysimr
      541 nlgidfedir smqneeffrt dssgevdfkd iditdeilty vqdslnnstl lnsacqqqpv
      601 sqhlscmlqe rlqleqqqql qqqhptqtle pqrqlcqvev pqhelgqktk hmqvngmfas
      661 wnpappvsfs cpqqerkhys lfsglqgtaq efpyksevds mpytqnfapc nqsllpehsk
      721 gtqldfpgrd ferslhpnas nledfvsclq vpenqrhgin sqsamvspqa yyagamsmyq
      781 cqagpqhtpv dqmqyspeip gsqaflskvr afyre
//
LOCUS       NP_001257883             280 aa            linear   ROD 27-APR-2025
DEFINITION  dexamethasone-induced Ras-related protein 1 [Rattus norvegicus].
ACCESSION   NP_001257883 XP_001077321 XP_340810
VERSION     NP_001257883.1
DBSOURCE    REFSEQ: accession NM_001270954.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Xin,Y., Chen,J., Zhang,H., Ostrowski,R.P., Liang,Y., Zhao,J.,
            Xiang,X., Liang,F., Fu,W., Huang,H., Wu,X., Su,J., Deng,J. and
            He,Z.
  TITLE     Dexras1 Induces Dysdifferentiation of Oligodendrocytes and Myelin
            Injury by Inhibiting the cAMP-CREB Pathway after Subarachnoid
            Hemorrhage
  JOURNAL   Cells 11 (19), 2976 (2022)
   PUBMED   36230939
  REMARK    GeneRIF: Dexras1 Induces Dysdifferentiation of Oligodendrocytes and
            Myelin Injury by Inhibiting the cAMP-CREB Pathway after
            Subarachnoid Hemorrhage.
            Erratum:[Cells. 2024 Nov 29;13(23):1975. doi:
            10.3390/cells13231975. PMID: 39682783]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Wang,L., Mitsui,T., Ishida,M., Izawa,M. and Arita,J.
  TITLE     Rasd1 is an estrogen-responsive immediate early gene and modulates
            expression of late genes in rat anterior pituitary cells
  JOURNAL   Endocr J 64 (11), 1063-1071 (2017)
   PUBMED   28835591
  REMARK    GeneRIF: Rasd1 is an estrogen-responsive immediate early gene and
            modulates E2 induction of at least several late genes in anterior
            pituitary cells.
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Greenwood,M.P., Greenwood,M., Mecawi,A.S., Antunes-Rodrigues,J.,
            Paton,J.F. and Murphy,D.
  TITLE     Rasd1, a small G protein with a big role in the hypothalamic
            response to neuronal activation
  JOURNAL   Mol Brain 9, 1 (2016)
   PUBMED   26739966
  REMARK    GeneRIF: two mechanisms of Rasd1 induction in the hypothalamus,
            were identified.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hahnova,K., Pacesova,D., Volfova,B., Cervena,K., Kasparova,D.,
            Zurmanova,J. and Bendova,Z.
  TITLE     Circadian Dexras1 in rats: Development, location and responsiveness
            to light
  JOURNAL   Chronobiol Int 33 (2), 141-150 (2016)
   PUBMED   26785766
  REMARK    GeneRIF: The Dexras1 protein is expressed predominantly in the
            dorsomedial part of thesuprachiasmatic nucleus and the light pulse
            has only a limited effect on its expression
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Wang,Y., Dong,X., Li,Z., Wang,W., Tian,J. and Chen,J.
  TITLE     Downregulated RASD1 and upregulated miR-375 are involved in
            protective effects of calycosin on cerebral ischemia/reperfusion
            rats
  JOURNAL   J Neurol Sci 339 (1-2), 144-148 (2014)
   PUBMED   24548484
  REMARK    GeneRIF: RASD1 is downregulated by calycosin in cerebral
            ischemia/reperfusion injury and provides a protective effect.
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Beigi,F., Oskouei,B.N., Zheng,M., Cooke,C.A., Lamirault,G. and
            Hare,J.M.
  TITLE     Cardiac nitric oxide synthase-1 localization within the
            cardiomyocyte is accompanied by the adaptor protein, CAPON
  JOURNAL   Nitric Oxide 21 (3-4), 226-233 (2009)
   PUBMED   19800018
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Lau,K.F., Chan,W.M., Perkinton,M.S., Tudor,E.L., Chang,R.C.,
            Chan,H.Y., McLoughlin,D.M. and Miller,C.C.
  TITLE     Dexras1 interacts with FE65 to regulate FE65-amyloid precursor
            protein-dependent transcription
  JOURNAL   J Biol Chem 283 (50), 34728-34737 (2008)
   PUBMED   18922798
  REMARK    GeneRIF: Dexras1 functions as a suppressor of FE65-APP-mediated
            transcription, and FE65 tyrosine 547 phosphorylation enhances
            FE65-APP-mediated transcription, at least in part, by modulating
            the interaction between FE65 and Dexras1
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Li,X., Cheng,C., Fei,M., Gao,S., Niu,S., Chen,M., Liu,Y., Guo,Z.,
            Wang,H., Zhao,J., Yu,X. and Shen,A.
  TITLE     Spatiotemporal expression of Dexras1 after spinal cord transection
            in rats
  JOURNAL   Cell Mol Neurobiol 28 (3), 371-388 (2008)
   PUBMED   18219571
  REMARK    GeneRIF: Transient high expression of Dexras1 which localized in
            apoptotic neurons and pathological oligodendrocytes after spinal
            cord transection.
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Shen,A., Chen,M., Niu,S., Sun,L., Gao,S., Shi,S., Li,X., Lv,Q.,
            Guo,Z. and Cheng,C.
  TITLE     Changes in mRNA for CAPON and Dexras1 in adult rat following
            sciatic nerve transection
  JOURNAL   J Chem Neuroanat 35 (1), 85-93 (2008)
   PUBMED   17768032
  REMARK    GeneRIF: Dexras1 is involved in various pathological conditions
            including nerve regeneration, neuron loss or survival and even pain
            processes via regulating nNOS activity or through the downstream
            targets of Dexras1.
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Fang,M., Jaffrey,S.R., Sawa,A., Ye,K., Luo,X. and Snyder,S.H.
  TITLE     Dexras1: a G protein specifically coupled to neuronal nitric oxide
            synthase via CAPON
  JOURNAL   Neuron 28 (1), 183-193 (2000)
   PUBMED   11086993
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099136.1.
            
            On or before Aug 17, 2012 this sequence version replaced
            XP_340810.1, XP_001077321.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099136.1, CV110404.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..280
                     /product="dexamethasone-induced Ras-related protein 1"
                     /EC_number="3.6.5.2"
                     /note="DEXRAS1 (Dexras1); RAS, dexamethasone-induced 1"
                     /calculated_mol_wt=31583
     mat_peptide     1..277
                     /product="Dexamethasone-induced Ras-related protein 1.
                     /id=PRO_0000082719"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF8.1)"
                     /calculated_mol_wt=31414
     Region          25..280
                     /region_name="Rhes_like"
                     /note="Ras homolog enriched in striatum (Rhes) and
                     activator of G-protein signaling 1 (Dexras1/AGS1);
                     cd04143"
                     /db_xref="CDD:133343"
     Site            31..38
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133343"
     Site            order(32..33,80..81)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133343"
     Site            order(33..39,78,81,145..146,148,177..178)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133343"
     Site            order(38..39,53,55,61..62,75..76,78,80..81,179)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133343"
     Region          53..61
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKF8.1)"
     Site            order(54..55,59..62)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133343"
     Site            54..61
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133343"
     Site            56
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133343"
     Site            78..81
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133343"
     Site            order(80..81,84..98)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133343"
     Site            145..148
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133343"
     Site            177..179
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133343"
     Site            277..280
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:133343"
     Site            277
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9JKF8.1)"
     CDS             1..280
                     /gene="Rasd1"
                     /coded_by="NM_001270954.1:90..932"
                     /db_xref="GeneID:64455"
                     /db_xref="RGD:619727"
ORIGIN      
        1 mklaamikkm cpsdselsip akncyrmvil gsskvgktai vsrfltgrfe daytptiedf
       61 hrkfysirge vyqldildts gnhpfpamrr lsiltgdvfi lvfsldnrds feevqrlkqq
      121 ildtksclkn ktkenvdvpl vicgnkgdrd fyreveqrei eqlvgddpqr cayfeisakk
      181 nssldqmfra lfamaklpse mspdlhrkvs vqycdvlhkk alrnkkllra gsggggdhgd
      241 afgilapfar rpsvhsdlmy irektsvssq akdkercvis
//
LOCUS       NP_001231796              77 aa            linear   ROD 27-APR-2025
DEFINITION  cysteine-rich protein 1 [Rattus norvegicus].
ACCESSION   NP_001231796
VERSION     NP_001231796.1
DBSOURCE    REFSEQ: accession NM_001244867.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Latonen,L., Jarvinen,P.M., Suomela,S., Moore,H.M.,
            Saarialho-Kere,U. and Laiho,M.
  TITLE     Ultraviolet B radiation regulates cysteine-rich protein 1 in human
            keratinocytes
  JOURNAL   Photodermatol Photoimmunol Photomed 26 (2), 70-77 (2010)
   PUBMED   20415737
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Chen,B., Young,J. and Leng,F.
  TITLE     DNA bending by the mammalian high-mobility group protein AT hook 2
  JOURNAL   Biochemistry 49 (8), 1590-1595 (2010)
   PUBMED   20108983
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Hao,J., Serohijos,A.W., Newton,G., Tassone,G., Wang,Z., Sgroi,D.C.,
            Dokholyan,N.V. and Basilion,J.P.
  TITLE     Identification and rational redesign of peptide ligands to CRIP1, a
            novel biomarker for cancers
  JOURNAL   PLoS Comput Biol 4 (8), e1000138 (2008)
   PUBMED   18670594
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Wang,Q., Williamson,M., Bott,S., Brookman-Amissah,N., Freeman,A.,
            Nariculam,J., Hubank,M.J., Ahmed,A. and Masters,J.R.
  TITLE     Hypomethylation of WNT5A, CRIP1 and S100P in prostate cancer
  JOURNAL   Oncogene 26 (45), 6560-6565 (2007)
   PUBMED   17486081
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Perez-Alvarado,G.C., Kosa,J.L., Louis,H.A., Beckerle,M.C.,
            Winge,D.R. and Summers,M.F.
  TITLE     Structure of the cysteine-rich intestinal protein, CRIP
  JOURNAL   J Mol Biol 257 (1), 153-174 (1996)
   PUBMED   8632452
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Tsui,S.K., Yam,N.Y., Lee,C.Y. and Waye,M.M.
  TITLE     Isolation and characterization of a cDNA that codes for a
            LIM-containing protein which is developmentally regulated in heart
  JOURNAL   Biochem Biophys Res Commun 205 (1), 497-505 (1994)
   PUBMED   7999070
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Levenson,C.W., Shay,N.F. and Cousins,R.J.
  TITLE     Cloning and initial characterization of the promoter region of the
            rat cysteine-rich intestinal protein gene
  JOURNAL   Biochem J 303 (Pt 3) (Pt 3), 731-736 (1994)
   PUBMED   7980439
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Hempe,J.M. and Cousins,R.J.
  TITLE     Cysteine-rich intestinal protein binds zinc during transmucosal
            zinc transport
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9671-9674 (1991)
   PUBMED   1946385
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Birkenmeier,E.H. and Gordon,J.I.
  TITLE     Developmental regulation of a gene that encodes a cysteine-rich
            intestinal protein and maps near the murine immunoglobulin heavy
            chain locus
  JOURNAL   Proc Natl Acad Sci U S A 83 (8), 2516-2520 (1986)
   PUBMED   3085096
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ223262.1 and AI716760.1.
            
            Transcript Variant: This variant (1) is the predominant transcript.
            Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223262.1, CB729183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..77
                     /product="cysteine-rich protein 1"
                     /note="cysteine-rich intestinal protein; cysteine-rich
                     protein 1 (intestinal)"
                     /calculated_mol_wt=8419
     Region          4..57
                     /region_name="LIM_CRIP"
                     /note="The LIM domain of Cysteine-Rich Intestinal Protein
                     (CRIP); cd09478"
                     /db_xref="CDD:188862"
     Site            order(4,7,25,28,31,34,52,56)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188862"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50238; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     Site            22
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63254; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     Site            68
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P63254; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     CDS             1..77
                     /gene="Crip1"
                     /gene_synonym="Crip; Crp-1"
                     /coded_by="NM_001244867.1:63..296"
                     /db_xref="GeneID:691657"
                     /db_xref="RGD:1597237"
ORIGIN      
        1 mpkcpkcdke vyfaervtsl gkdwhrpclk cekcgktlts gghaehegkp ycnhpcysam
       61 fgpkgfgrgg aeshtfk
//
LOCUS       NP_001178769             461 aa            linear   ROD 27-APR-2025
DEFINITION  transforming growth factor beta-1-induced transcript 1 protein
            [Rattus norvegicus].
ACCESSION   NP_001178769 XP_341935
VERSION     NP_001178769.1
DBSOURCE    REFSEQ: accession NM_001191840.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Miyauchi,A., Noguchi,M., Lei,X.F., Sakaki,M., Kobayashi-Tanabe,M.,
            Haraguchi,S., Miyazaki,A. and Kim-Kaneyama,J.R.
  TITLE     Knockdown of mechanosensitive adaptor Hic-5 ameliorates
            post-traumatic osteoarthritis in rats through repression of MMP-13
  JOURNAL   Sci Rep 13 (1), 7446 (2023)
   PUBMED   37156857
  REMARK    GeneRIF: Knockdown of mechanosensitive adaptor Hic-5 ameliorates
            post-traumatic osteoarthritis in rats through repression of MMP-13.
            Erratum:[Sci Rep. 2023 Jun 13;13(1):9589. doi:
            10.1038/s41598-023-36393-w. PMID: 37311826]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Varney,S.D., Betts,C.B., Zheng,R., Wu,L., Hinz,B., Zhou,J. and Van
            De Water,L.
  TITLE     Hic-5 is required for myofibroblast differentiation by regulating
            mechanically dependent MRTF-A nuclear accumulation
  JOURNAL   J Cell Sci 129 (4), 774-787 (2016)
   PUBMED   26759173
  REMARK    GeneRIF: the reciprocal regulation of MRTF-A localization by Hic-5
            and Hic-5 expression by MRTF-A, plays a crucial role in
            myofibroblast differentiation in response to TGF-beta.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Hornigold,N. and Mooney,A.
  TITLE     Extracellular matrix-induced Hic-5 expression in glomerular
            mesangial cells leads to a prosclerotic phenotype independent of
            TGF-beta
  JOURNAL   FASEB J 29 (12), 4956-4967 (2015)
   PUBMED   26405299
  REMARK    GeneRIF: data indicate that there is a prosclerotic feedback loop
            in mesangial cells dependent on matrix-derived signals in which
            Hic-5 is a pivotal signaling protein. This feedback loop is
            TGF-beta-independent
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Hornigold,N., Johnson,T.S., Huang,L., Haylor,J.L., Griffin,M. and
            Mooney,A.
  TITLE     Inhibition of collagen I accumulation reduces glomerulosclerosis by
            a Hic-5-dependent mechanism in experimental diabetic nephropathy
  JOURNAL   Lab Invest 93 (5), 553-565 (2013)
   PUBMED   23508044
  REMARK    GeneRIF: Hypothesized that reducing collagen I accumulation in
            glomerulosclerosis would lower Hic-5 expression,reducing apoptosis,
            and maintain glomerular integrity. NTU281 treatment reduced
            glomerular col I accumulation, Hic-5 and alpha-SMA expression, and
            apoptosis.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Shola,D.T., Wang,H., Wahdan-Alaswad,R. and Danielpour,D.
  TITLE     Hic-5 controls BMP4 responses in prostate cancer cells through
            interacting with Smads 1, 5 and 8
  JOURNAL   Oncogene 31 (19), 2480-2490 (2012)
   PUBMED   21996749
  REMARK    GeneRIF: these results provide the first evidence for a physical
            and mutual functional interaction between Hic-5 and the BMP
            signaling pathway.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Wang,H., Song,K., Sponseller,T.L. and Danielpour,D.
  TITLE     Novel function of androgen receptor-associated protein 55/Hic-5 as
            a negative regulator of Smad3 signaling
  JOURNAL   J Biol Chem 280 (7), 5154-5162 (2005)
   PUBMED   15561701
  REMARK    GeneRIF: the C terminus of ARA55 is critical for suppression of
            Smad3 activity
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Drori,S., Girnun,G.D., Tou,L., Szwaya,J.D., Mueller,E., Xia,K.,
            Shivdasani,R.A. and Spiegelman,B.M.
  TITLE     Hic-5 regulates an epithelial program mediated by PPARgamma
  JOURNAL   Genes Dev 19 (3), 362-375 (2005)
   PUBMED   15687259
  REMARK    Erratum:[Genes Dev. 2005 Apr 1;19(7):875. Kia, Xia [corrected to
            Xia, Kai]]
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Hagel,M., George,E.L., Kim,A., Tamimi,R., Opitz,S.L., Turner,C.E.,
            Imamoto,A. and Thomas,S.M.
  TITLE     The adaptor protein paxillin is essential for normal development in
            the mouse and is a critical transducer of fibronectin signaling
  JOURNAL   Mol Cell Biol 22 (3), 901-915 (2002)
   PUBMED   11784865
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Jia,Y., Ransom,R.F., Shibanuma,M., Liu,C., Welsh,M.J. and
            Smoyer,W.E.
  TITLE     Identification and characterization of hic-5/ARA55 as an hsp27
            binding protein
  JOURNAL   J Biol Chem 276 (43), 39911-39918 (2001)
   PUBMED   11546764
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Fujimoto,N., Yeh,S., Kang,H.Y., Inui,S., Chang,H.C., Mizokami,A.
            and Chang,C.
  TITLE     Cloning and characterization of androgen receptor coactivator,
            ARA55, in human prostate
  JOURNAL   J Biol Chem 274 (12), 8316-8321 (1999)
   PUBMED   10075738
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341935.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.4342.1,
                                           SRR26643299.4645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..461
                     /product="transforming growth factor beta-1-induced
                     transcript 1 protein"
                     /note="hydrogen peroxide-inducible clone 5 protein;
                     androgen receptor-associated protein of 55 kDa"
                     /calculated_mol_wt=49992
     Region          1..240
                     /region_name="Interaction with PTK2B/PYK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          1..200
                     /region_name="Transcription activation.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          1..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          3..15
                     /region_name="LD motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62219; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          <55..>106
                     /region_name="Paxillin"
                     /note="Paxillin family; pfam03535"
                     /db_xref="CDD:460962"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FAK2 and FYN.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          83..136
                     /region_name="Interaction with PTK2/FAK1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          92..104
                     /region_name="LD motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          116..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          157..168
                     /region_name="LD motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          171..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62219; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62219; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          203..215
                     /region_name="LD motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          228..280
                     /region_name="LIM1_Paxillin_like"
                     /note="The first LIM domain of the paxillin like protein
                     family; cd09336"
                     /db_xref="CDD:259830"
     Site            order(228,231,248,251,254,257,275,278)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259830"
     Region          287..338
                     /region_name="LIM2_Paxillin_like"
                     /note="The second LIM domain of the paxillin like protein
                     family; cd09337"
                     /db_xref="CDD:188723"
     Site            order(287,290,307,310,313,316,334,337)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188723"
     Region          346..398
                     /region_name="LIM3_Paxillin"
                     /note="The third LIM domain of paxillin; cd09409"
                     /db_xref="CDD:188793"
     Site            order(346,349,366,369,372,375,393,396)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188793"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     Region          405..456
                     /region_name="LIM4_Leupaxin"
                     /note="The fourth LIM domain of Leupaxin; cd09412"
                     /db_xref="CDD:188796"
     Site            order(405,408,425,428,431,434,452,455)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188796"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O43294; propagated from
                     UniProtKB/Swiss-Prot (Q99PD6.2)"
     CDS             1..461
                     /gene="Tgfb1i1"
                     /gene_synonym="Ara55; Hic-5"
                     /coded_by="NM_001191840.1:28..1413"
                     /db_xref="GeneID:84574"
                     /db_xref="RGD:620173"
ORIGIN      
        1 medldallsd letttshmsr lgapkerppe tltppppygh qpqtgsgess gasgdkdhly
       61 stvckprspk svapvappfs sssgvlgngl celdrllqel natqfnitde imsqfpsskm
      121 aegegkedqs edksittvps stfpapskps atsatqeldr lmaslsdfrv qnhlpasgpp
      181 qppavsptre gcpsppgqtn kgsldtmlgl lqsdlsrrgv ptqakglcgs cnkpiagqvv
      241 talgrawhpe hflcrgcstt lggssffekd gapfcpecyf erfsprcgfc nqpirhkmvt
      301 algthwhpeh fccvscgepf geegfhereg rpycrrdflq lfaprcqgcq gpildnyisa
      361 lsalwhpdcf vcreclapfs ggsffehegr plcenhfhaq rgslcatcgl pvtgrcvsal
      421 grrfhpdhft ctfclrpltk gsfqeraskp ycqpcflklf g
//
LOCUS       NP_001263691             331 aa            linear   ROD 27-APR-2025
DEFINITION  laforin [Rattus norvegicus].
ACCESSION   NP_001263691 XP_002725492 XP_003748696
VERSION     NP_001263691.1
DBSOURCE    REFSEQ: accession NM_001276762.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Rai,A., Mishra,R. and Ganesh,S.
  TITLE     Suppression of leptin signaling reduces polyglucosan inclusions and
            seizure susceptibility in a mouse model for Lafora disease
  JOURNAL   Hum Mol Genet 26 (24), 4778-4785 (2017)
   PUBMED   28973665
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Nitschke,F., Sullivan,M.A., Wang,P., Zhao,X., Chown,E.E.,
            Perri,A.M., Israelian,L., Juana-Lopez,L., Bovolenta,P., Rodriguez
            de Cordoba,S., Steup,M. and Minassian,B.A.
  TITLE     Abnormal glycogen chain length pattern, not hyperphosphorylation,
            is critical in Lafora disease
  JOURNAL   EMBO Mol Med 9 (7), 906-917 (2017)
   PUBMED   28536304
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Upadhyay,M., Agarwal,S., Bhadauriya,P. and Ganesh,S.
  TITLE     Loss of laforin or malin results in increased Drp1 level and
            concomitant mitochondrial fragmentation in Lafora disease mouse
            models
  JOURNAL   Neurobiol Dis 100, 39-51 (2017)
   PUBMED   28063983
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Munoz-Ballester,C., Berthier,A., Viana,R. and Sanz,P.
  TITLE     Homeostasis of the astrocytic glutamate transporter GLT-1 is
            altered in mouse models of Lafora disease
  JOURNAL   Biochim Biophys Acta 1862 (6), 1074-1083 (2016)
   PUBMED   26976331
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Jain,N., Mishra,R. and Ganesh,S.
  TITLE     FoxO3a-mediated autophagy is down-regulated in the laforin
            deficient mice, an animal model for Lafora progressive myoclonus
            epilepsy
  JOURNAL   Biochem Biophys Res Commun 474 (2), 321-327 (2016)
   PUBMED   27107699
  REMARK    Erratum:[Biochem Biophys Res Commun. 2018 Sep 5;503(2):1175-1176.
            doi: 10.1016/j.bbrc.2018.07.052. PMID: 30025895]
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Ganesh,S., Delgado-Escueta,A.V., Sakamoto,T., Avila,M.R.,
            Machado-Salas,J., Hoshii,Y., Akagi,T., Gomi,H., Suzuki,T.,
            Amano,K., Agarwala,K.L., Hasegawa,Y., Bai,D.S., Ishihara,T.,
            Hashikawa,T., Itohara,S., Cornford,E.M., Niki,H. and Yamakawa,K.
  TITLE     Targeted disruption of the Epm2a gene causes formation of Lafora
            inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and
            impaired behavioral response in mice
  JOURNAL   Hum Mol Genet 11 (11), 1251-1262 (2002)
   PUBMED   12019206
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Wang,J., Stuckey,J.A., Wishart,M.J. and Dixon,J.E.
  TITLE     A unique carbohydrate binding domain targets the lafora disease
            phosphatase to glycogen
  JOURNAL   J Biol Chem 277 (4), 2377-2380 (2002)
   PUBMED   11739371
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Ganesh,S., Agarwala,K.L., Amano,K., Suzuki,T., Delgado-Escueta,A.V.
            and Yamakawa,K.
  TITLE     Regional and developmental expression of Epm2a gene and its
            evolutionary conservation
  JOURNAL   Biochem Biophys Res Commun 283 (5), 1046-1053 (2001)
   PUBMED   11355878
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Ganesh,S., Agarwala,K.L., Ueda,K., Akagi,T., Shoda,K., Usui,T.,
            Hashikawa,T., Osada,H., Delgado-Escueta,A.V. and Yamakawa,K.
  TITLE     Laforin, defective in the progressive myoclonus epilepsy of Lafora
            type, is a dual-specificity phosphatase associated with
            polyribosomes
  JOURNAL   Hum Mol Genet 9 (15), 2251-2261 (2000)
   PUBMED   11001928
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Minassian,B.A., Lee,J.R., Herbrick,J.A., Huizenga,J., Soder,S.,
            Mungall,A.J., Dunham,I., Gardner,R., Fong,C.Y., Carpenter,S.,
            Jardim,L., Satishchandra,P., Andermann,E., Snead,O.C. 3rd,
            Lopes-Cendes,I., Tsui,L.C., Delgado-Escueta,A.V., Rouleau,G.A. and
            Scherer,S.W.
  TITLE     Mutations in a gene encoding a novel protein tyrosine phosphatase
            cause progressive myoclonus epilepsy
  JOURNAL   Nat Genet 20 (2), 171-174 (1998)
   PUBMED   9771710
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Mar 1, 2013 this sequence version replaced
            XP_002725492.1, XP_003748696.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF347030.1, SRR26643296.55.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..331
                     /product="laforin"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="LAFPTPase; lafora PTPase; epilepsy, progressive
                     myoclonic epilepsy, type 2 gene alpha; glucan phosphatase;
                     epilepsy, progressive myoclonus type 2A; EPM2A, laforin
                     glucan phosphatase"
                     /calculated_mol_wt=37013
     Region          1..129
                     /region_name="CBM20_laforin"
                     /note="Laforin protein tyrosine phosphatase, N-terminal
                     CBM20 (carbohydrate-binding module, family 20) domain.
                     Laforin, encoded by the EPM2A gene, is a dual-specificity
                     phosphatase that dephosphorylates complex carbohydrates.
                     Mutations in the gene encoding...; cd05806"
                     /db_xref="CDD:99881"
     Site            order(12..16,19,42,58,60)
                     /site_type="other"
                     /note="starch-binding site 2 [chemical binding]"
                     /db_xref="CDD:99881"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O95278; propagated from
                     UniProtKB/Swiss-Prot (Q91XQ2.2)"
     Site            order(32,87,99..100,104)
                     /site_type="other"
                     /note="starch-binding site 1 [chemical binding]"
                     /db_xref="CDD:99881"
     Region          155..312
                     /region_name="DSP_laforin-like"
                     /note="dual specificity phosphatase domain of laforin and
                     similar domains; cd14526"
                     /db_xref="CDD:350375"
     Region          266..272
                     /region_name="Glucan phosphatase signature motif CXAGXGR.
                     /evidence=ECO:0000250|UniProtKB:O95278"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XQ2.2)"
     Site            329
                     /site_type="other"
                     /note="Required for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O95278; propagated from
                     UniProtKB/Swiss-Prot (Q91XQ2.2)"
     CDS             1..331
                     /gene="Epm2a"
                     /coded_by="NM_001276762.1:1..996"
                     /db_xref="GeneID:114005"
                     /db_xref="RGD:71047"
ORIGIN      
        1 mlfrfgvvvp pavagtrlel llagsrpelg rweprgavrl rpagtaagaa alalqepglw
       61 laevelapee eaadgaepgr idtfwykflq repggelhwe gngphhdrcc tynennlvdg
      121 vyclpvghwi eatghtnemk httdfyfnia ghqamhysri lpniwlgscp rqlehvtikl
      181 khelgitavm nfqtewdiiq nssgcnrype pmtpdtmmkl ykeeglayiw mptpdmsteg
      241 rvqmlpqavc llhallengh tvyvhcnagv grstaavcgw lhyvigwslr kvqyfimakr
      301 pavyideeal aqaqqdffqk fgkvhssict l
//
LOCUS       NP_114471                353 aa            linear   ROD 27-APR-2025
DEFINITION  2-Hydroxyacid oxidase 2 [Rattus norvegicus].
ACCESSION   NP_114471
VERSION     NP_114471.1
DBSOURCE    REFSEQ: accession NM_032082.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Mattu,S., Fornari,F., Quagliata,L., Perra,A., Angioni,M.M.,
            Petrelli,A., Menegon,S., Morandi,A., Chiarugi,P.,
            Ledda-Columbano,G.M., Gramantieri,L., Terracciano,L., Giordano,S.
            and Columbano,A.
  TITLE     The metabolic gene HAO2 is downregulated in hepatocellular
            carcinoma and predicts metastasis and poor survival
  JOURNAL   J Hepatol 64 (4), 891-898 (2016)
   PUBMED   26658681
  REMARK    GeneRIF: Dysregulation of HAO2 is a very early event in the
            development of hepatocellular carcinoma (HCC).
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Cunane,L.M., Barton,J.D., Chen,Z.W., Le,K.H., Amar,D., Lederer,F.
            and Mathews,F.S.
  TITLE     Crystal structure analysis of recombinant rat kidney long chain
            hydroxy acid oxidase
  JOURNAL   Biochemistry 44 (5), 1521-1531 (2005)
   PUBMED   15683236
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Lee,S.J., Liu,J., Qi,N., Guarnera,R.A., Lee,S.Y. and Cicila,G.T.
  TITLE     Use of a panel of congenic strains to evaluate differentially
            expressed genes as candidate genes for blood pressure quantitative
            trait loci
  JOURNAL   Hypertens Res 26 (1), 75-87 (2003)
   PUBMED   12661916
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Jones,J.M., Morrell,J.C. and Gould,S.J.
  TITLE     Identification and characterization of HAOX1, HAOX2, and HAOX3,
            three human peroxisomal 2-hydroxy acid oxidases
  JOURNAL   J Biol Chem 275 (17), 12590-12597 (2000)
   PUBMED   10777549
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Belmouden,A., Le,K.H., Lederer,F. and Garchon,H.J.
  TITLE     Molecular cloning and nucleotide sequence of cDNA encoding rat
            kidney long-chain L-2-hydroxy acid oxidase. Expression of the
            catalytically active recombinant protein as a chimaera
  JOURNAL   Eur J Biochem 214 (1), 17-25 (1993)
   PUBMED   8508789
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Diep Le,K.H. and Lederer,F.
  TITLE     Amino acid sequence of long chain alpha-hydroxy acid oxidase from
            rat kidney, a member of the family of FMN-dependent alpha-hydroxy
            acid-oxidizing enzymes
  JOURNAL   J Biol Chem 266 (31), 20877-20881 (1991)
   PUBMED   1939137
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Urban,P., Chirat,I. and Lederer,F.
  TITLE     Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic
            comparison with flavocytochrome b2 from baker's yeast
  JOURNAL   Biochemistry 27 (19), 7365-7371 (1988)
   PUBMED   3061453
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X67156.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X67156.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..353
                     /product="2-Hydroxyacid oxidase 2"
                     /EC_number="1.1.3.15"
                     /note="HAOX2; long-chain L-2-hydroxy acid oxidase; long
                     chain alpha-hydroxy acid oxidase; (S)-2-hydroxy-acid
                     oxidase, peroxisomal; hydroxyacid oxidase 3
                     (medium-chain); hydroxyacid oxidase 2 (long chain)"
                     /calculated_mol_wt=39070
     Region          13..349
                     /region_name="FMN_dh"
                     /note="FMN-dependent dehydrogenase; pfam01070"
                     /db_xref="CDD:426029"
     Site            order(24,106,130,158,165,224,248,251,303)
                     /site_type="active"
                     /db_xref="CDD:239203"
     Site            order(24,130,165,248,251)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(106,130,158,224,248,251,303)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239203"
     Site            order(130,165,248)
                     /site_type="active"
                     /note="putative catalytic residues [active]"
                     /db_xref="CDD:239203"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q07523.2)"
     Region          351..353
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07523.2)"
     CDS             1..353
                     /gene="Hao2"
                     /gene_synonym="Hao3; LCHAO"
                     /coded_by="NM_032082.2:202..1263"
                     /db_xref="GeneID:84029"
                     /db_xref="RGD:70972"
ORIGIN      
        1 mplvcladfk ahaqkqlskt swdfiegead dgitysenia afkrirlrpr ylrdmskvdt
       61 rttiqgqeis apicisptaf hsiawpdgek staraaqean icyvissyas ysledivaaa
      121 pegfrwfqly mksdwdfnkq mvqraealgf kalvitidtp vlgnrrrdkr nqlnleanil
      181 lkdlralkee kptqsvpvsf pkasfcwndl sllqsitrlp iilkgiltke daelamkhnv
      241 qgivvsnhgg rqldevsasi dalrevvaav kgkievymdg gvrtgtdvlk alalgarcif
      301 lgrpilwgla ckgedgvkev ldiltaelhr cmtlsgcqsv aeispdliqf srl
//
LOCUS       NP_446420                 66 aa            linear   ROD 27-APR-2025
DEFINITION  metallothionein-3 [Rattus norvegicus].
ACCESSION   NP_446420
VERSION     NP_446420.1
DBSOURCE    REFSEQ: accession NM_053968.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Xiong,T., Li,Y., Yang,M., Huo,B., Guo,X., Liu,L., Huang,Y., Zhu,X.,
            Hu,Q., Wei,X., Jiang,D.S. and Yi,X.
  TITLE     Metallothionein 3 Potentiates Pulmonary Artery Smooth Muscle Cell
            Proliferation by Promoting Zinc-MTF1-ATG5 Axis-mediated
            Autophagosome Formation
  JOURNAL   Int J Biol Sci 20 (8), 2904-2921 (2024)
   PUBMED   38904023
  REMARK    GeneRIF: Metallothionein 3 Potentiates Pulmonary Artery Smooth
            Muscle Cell Proliferation by Promoting Zinc-MTF1-ATG5 Axis-mediated
            Autophagosome Formation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Scudiero,R., Cigliano,L. and Verderame,M.
  TITLE     Age-related changes of metallothionein 1/2 and metallothionein 3
            expression in rat brain
  JOURNAL   C R Biol 340 (1), 13-17 (2017)
   PUBMED   27939232
  REMARK    GeneRIF: After passing middle age we observe a huge increase in MT3
            transcripts in both cortical and hippocampal areas, while the MT1/2
            mRNA content increases slightly
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Tian,T., Ni,H. and Sun,B.L.
  TITLE     Neurobehavioral Deficits in a Rat Model of Recurrent Neonatal
            Seizures Are Prevented by a Ketogenic Diet and Correlate with
            Hippocampal Zinc/Lipid Transporter Signals
  JOURNAL   Biol Trace Elem Res 167 (2), 251-258 (2015)
   PUBMED   25778834
  REMARK    GeneRIF: rats treated with KD (EXP2) showed a significant
            down-regulated expression of ZnT-3, MT-3, ApoE, clusterin, and
            ACAT-1 in hippocampus
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Ni,H., Ren,S.Y., Zhang,L.L., Sun,Q., Tian,T. and Feng,X.
  TITLE     Expression profiles of hippocampal regenerative sprouting-related
            genes and their regulation by E-64d in a developmental rat model of
            penicillin-induced recurrent epilepticus
  JOURNAL   Toxicol Lett 217 (2), 162-169 (2013)
   PUBMED   23266720
REFERENCE   5  (residues 1 to 66)
  AUTHORS   Tsuruma,K., Shimazaki,H., Ohno,Y., Inoue,Y., Honda,A., Imai,S.,
            Lee,J., Shimazawa,M., Satoh,M. and Hara,H.
  TITLE     Metallothionein-III deficiency exacerbates light-induced retinal
            degeneration
  JOURNAL   Invest Ophthalmol Vis Sci 53 (12), 7896-7903 (2012)
   PUBMED   23132798
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 66)
  AUTHORS   Amoureux,M.C., Wurch,T. and Pauwels,P.J.
  TITLE     Modulation of metallothionein-III mRNA content and growth rate of
            rat C6-glial cells by transfection with human 5-HT1D receptor genes
  JOURNAL   Biochem Biophys Res Commun 214 (2), 639-645 (1995)
   PUBMED   7677777
REFERENCE   7  (residues 1 to 66)
  AUTHORS   Masters,B.A., Quaife,C.J., Erickson,J.C., Kelly,E.J.,
            Froelick,G.J., Zambrowicz,B.P., Brinster,R.L. and Palmiter,R.D.
  TITLE     Metallothionein III is expressed in neurons that sequester zinc in
            synaptic vesicles
  JOURNAL   J Neurosci 14 (10), 5844-5857 (1994)
   PUBMED   7931547
REFERENCE   8  (residues 1 to 66)
  AUTHORS   Erickson,J.C., Sewell,A.K., Jensen,L.T., Winge,D.R. and
            Palmiter,R.D.
  TITLE     Enhanced neurotrophic activity in Alzheimer's disease cortex is not
            associated with down-regulation of metallothionein-III (GIF)
  JOURNAL   Brain Res 649 (1-2), 297-304 (1994)
   PUBMED   7953645
REFERENCE   9  (residues 1 to 66)
  AUTHORS   Kobayashi,H., Uchida,Y., Ihara,Y., Nakajima,K., Kohsaka,S.,
            Miyatake,T. and Tsuji,S.
  TITLE     Molecular cloning of rat growth inhibitory factor cDNA and the
            expression in the central nervous system
  JOURNAL   Brain Res Mol Brain Res 19 (3), 188-194 (1993)
   PUBMED   8412560
REFERENCE   10 (residues 1 to 66)
  AUTHORS   Tsuji,S., Kobayashi,H., Uchida,Y., Ihara,Y. and Miyatake,T.
  TITLE     Molecular cloning of human growth inhibitory factor cDNA and its
            down-regulation in Alzheimer's disease
  JOURNAL   EMBO J 11 (13), 4843-4850 (1992)
   PUBMED   1464312
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC058453.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058453.1, BF556086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132292
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p12"
     Protein         1..66
                     /product="metallothionein-3"
                     /note="growth inhibitory factor; metallothionein III;
                     MT-III"
                     /calculated_mol_wt=6678
     Region          1..66
                     /region_name="Metallothio"
                     /note="Metallothionein; pfam00131"
                     /db_xref="CDD:395080"
     Region          1..30
                     /region_name="Beta"
                     /note="propagated from UniProtKB/Swiss-Prot (P37361.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P37359; propagated from
                     UniProtKB/Swiss-Prot (P37361.1)"
     Region          31..66
                     /region_name="Alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (P37361.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P28184; propagated from
                     UniProtKB/Swiss-Prot (P37361.1)"
     CDS             1..66
                     /gene="Mt3"
                     /gene_synonym="GIF; Mt-3"
                     /coded_by="NM_053968.3:64..264"
                     /db_xref="GeneID:117038"
                     /db_xref="RGD:621252"
ORIGIN      
        1 mdpetcpcpt ggsctcsdkc kckgckctnc kksccsccpa gcekcakdcv ckgeegakae
       61 kcsccq
//
LOCUS       NP_001128158             658 aa            linear   ROD 27-APR-2025
DEFINITION  cationic amino acid transporter 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001128158
VERSION     NP_001128158.1
DBSOURCE    REFSEQ: accession NM_001134686.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 658)
  AUTHORS   Hultstrom,M., Helle,F. and Iversen,B.M.
  TITLE     AT(1) receptor activation regulates the mRNA expression of CAT1,
            CAT2, arginase-1, and DDAH2 in preglomerular vessels from
            angiotensin II hypertensive rats
  JOURNAL   Am J Physiol Renal Physiol 297 (1), F163-F168 (2009)
   PUBMED   19386725
  REMARK    GeneRIF: CAT1, CAT2, DDAH2, and arginase-1 expression in renal
            resistance vessels is regulated through the AT(1) receptor.
REFERENCE   2  (residues 1 to 658)
  AUTHORS   Huang,T.Y., Tsai,P.S. and Huang,C.J.
  TITLE     HO-1 overexpression attenuates endotoxin effects on CAT-2 isozymes
            expression
  JOURNAL   J Surg Res 148 (2), 172-180 (2008)
   PUBMED   18028947
  REMARK    GeneRIF: HO-1 overexpression significantly attenuates
            endotoxin-induced increases in nitric oxide and l-arginine
            transport, as well as the expression of iNOS and CAT-2 isozymes in
            septic rats.
REFERENCE   3  (residues 1 to 658)
  AUTHORS   Schwartz,I.F., Chernichovsky,T., Hagin,D., Ingbir,M., Reshef,R.,
            Chernin,G., Levo,Y. and Schwartz,D.
  TITLE     Differential regulation of L-arginine transporters (cationic amino
            acid transporter-1 and -2) by peroxynitrite in rat mesangial cells
  JOURNAL   Nephrol Dial Transplant 21 (12), 3409-3414 (2006)
   PUBMED   16998217
REFERENCE   4  (residues 1 to 658)
  AUTHORS   Rothenberg,M.E., Doepker,M.P., Lewkowich,I.P., Chiaramonte,M.G.,
            Stringer,K.F., Finkelman,F.D., MacLeod,C.L., Ellies,L.G. and
            Zimmermann,N.
  TITLE     Cationic amino acid transporter 2 regulates inflammatory
            homeostasis in the lung
  JOURNAL   Proc Natl Acad Sci U S A 103 (40), 14895-14900 (2006)
   PUBMED   17003120
REFERENCE   5  (residues 1 to 658)
  AUTHORS   Yeramian,A., Martin,L., Arpa,L., Bertran,J., Soler,C., McLeod,C.,
            Modolell,M., Palacin,M., Lloberas,J. and Celada,A.
  TITLE     Macrophages require distinct arginine catabolism and transport
            systems for proliferation and for activation
  JOURNAL   Eur J Immunol 36 (6), 1516-1526 (2006)
   PUBMED   16703566
REFERENCE   6  (residues 1 to 658)
  AUTHORS   Stevens,B.R., Kakuda,D.K., Yu,K., Waters,M., Vo,C.B. and
            Raizada,M.K.
  TITLE     Induced nitric oxide synthesis is dependent on induced
            alternatively spliced CAT-2 encoding L-arginine transport in brain
            astrocytes
  JOURNAL   J Biol Chem 271 (39), 24017-24022 (1996)
   PUBMED   8798637
REFERENCE   7  (residues 1 to 658)
  AUTHORS   Gill,D.J., Low,B.C. and Grigor,M.R.
  TITLE     Interleukin-1 beta and tumor necrosis factor-alpha stimulate the
            cat-2 gene of the L-arginine transporter in cultured vascular
            smooth muscle cells
  JOURNAL   J Biol Chem 271 (19), 11280-11283 (1996)
   PUBMED   8626679
REFERENCE   8  (residues 1 to 658)
  AUTHORS   Kavanaugh,M.P., Wang,H., Zhang,Z., Zhang,W., Wu,Y.N., Dechant,E.,
            North,R.A. and Kabat,D.
  TITLE     Control of cationic amino acid transport and retroviral receptor
            functions in a membrane protein family
  JOURNAL   J Biol Chem 269 (22), 15445-15450 (1994)
   PUBMED   8195186
REFERENCE   9  (residues 1 to 658)
  AUTHORS   Kudo,H., Hirayoshi,K., Kitagawa,Y., Imamura,S. and Nagata,K.
  TITLE     Two collagen-binding proteins, osteonectin and HSP47, are
            coordinately induced in transformed keratinocytes by heat and other
            stresses
  JOURNAL   Exp Cell Res 212 (2), 219-224 (1994)
   PUBMED   8187816
REFERENCE   10 (residues 1 to 658)
  AUTHORS   Closs,E.I., Albritton,L.M., Kim,J.W. and Cunningham,J.M.
  TITLE     Identification of a low affinity, high capacity transporter of
            cationic amino acids in mouse liver
  JOURNAL   J Biol Chem 268 (10), 7538-7544 (1993)
   PUBMED   8385111
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF245002.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            exon in the coding region compared to variant 1. The resulting
            protein (isoform b) is longer but has the same N- and C-termini
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF245002.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..658
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..658
                     /product="cationic amino acid transporter 2 isoform b"
                     /note="low affinity cationic amino acid transporter 2;
                     CAT-2; cationic amino acid transporter-2A; solute carrier
                     family 7 (cationic amino acid transporter, y+ system),
                     member 2"
                     /calculated_mol_wt=71507
     Region          5..608
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     CDS             1..658
                     /gene="Slc7a2"
                     /gene_synonym="Cat2; Cat2a; Cat2b"
                     /coded_by="NM_001134686.2:180..2156"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:64554"
                     /db_xref="RGD:68387"
ORIGIN      
        1 mipcravltf trclirrkiv tldsledskl crclttmdli algvgstlga gvyvlageva
       61 kadsgpsivv sfliaalasv maglcyaefg arvpktgsay lytyvtvgel wafitgwnli
      121 lsyvigtssv arawsgtfde llnkqigqff ktyfkmnytg laeypdffav clvlllagll
      181 sfgvkesawv nkfftainil vllfvmvagf vkgnvanwki seeflknisa sareppseng
      241 tsiygaggfm pygftgtlag aatcfyafvg fdciattgee vrnpqkaipi givtsllvcf
      301 mayfgvsaal tlmmpyylld eksplpvafe yvgwgpakyv vaagslcals tsllgsifpm
      361 prviyamaed gllfkclaqi nsktktpiia tlssgavaav maflfdlkal vdmmsigtlm
      421 ayslvaacvl ilryqpglcy eqpkytpekd ilesctnats ksesqvtmlq gqgfslrtlf
      481 npsalptrqs aslvsflvgf lafliaglsi lttygvqaia rleawslall alflvlcaav
      541 iltiwrqpqn qqkvafmvpf lpflpafsil vniylmvqls adtwvrfsiw mvlgfliyfa
      601 ygirhslegn prdeeededv cpdnvnaaae eksamqandh hqrnlslpfi lhektsec
//
LOCUS       NP_001263694             671 aa            linear   ROD 27-APR-2025
DEFINITION  3',5'-cyclic-AMP phosphodiesterase 4C [Rattus norvegicus].
ACCESSION   NP_001263694 XP_001070301 XP_214325
VERSION     NP_001263694.1
DBSOURCE    REFSEQ: accession NM_001276765.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Acin-Perez,R., Russwurm,M., Gunnewig,K., Gertz,M., Zoidl,G.,
            Ramos,L., Buck,J., Levin,L.R., Rassow,J., Manfredi,G. and
            Steegborn,C.
  TITLE     A phosphodiesterase 2A isoform localized to mitochondria regulates
            respiration
  JOURNAL   J Biol Chem 286 (35), 30423-30432 (2011)
   PUBMED   21724846
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Choi,Y.H., Suzuki,A., Hajarnis,S., Ma,Z., Chapin,H.C., Caplan,M.J.,
            Pontoglio,M., Somlo,S. and Igarashi,P.
  TITLE     Polycystin-2 and phosphodiesterase 4C are components of a ciliary
            A-kinase anchoring protein complex that is disrupted in cystic
            kidney diseases
  JOURNAL   Proc Natl Acad Sci U S A 108 (26), 10679-10684 (2011)
   PUBMED   21670265
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Waddleton,D., Wu,W., Feng,Y., Thompson,C., Wu,M., Zhou,Y.P.,
            Howard,A., Thornberry,N., Li,J. and Mancini,J.A.
  TITLE     Phosphodiesterase 3 and 4 comprise the major cAMP metabolizing
            enzymes responsible for insulin secretion in INS-1 (832/13) cells
            and rat islets
  JOURNAL   Biochem Pharmacol 76 (7), 884-893 (2008)
   PUBMED   18706893
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Conti,M. and Beavo,J.
  TITLE     Biochemistry and physiology of cyclic nucleotide
            phosphodiesterases: essential components in cyclic nucleotide
            signaling
  JOURNAL   Annu Rev Biochem 76, 481-511 (2007)
   PUBMED   17376027
  REMARK    Review article
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Bolger,G.B., Rodgers,L. and Riggs,M.
  TITLE     Differential CNS expression of alternative mRNA isoforms of the
            mammalian genes encoding cAMP-specific phosphodiesterases
  JOURNAL   Gene 149 (2), 237-244 (1994)
   PUBMED   7958996
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Swinnen,J.V., Joseph,D.R. and Conti,M.
  TITLE     Molecular cloning of rat homologues of the Drosophila melanogaster
            dunce cAMP phosphodiesterase: evidence for a family of genes
  JOURNAL   Proc Natl Acad Sci U S A 86 (14), 5325-5329 (1989)
   PUBMED   2546153
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Mar 1, 2013 this sequence version replaced
            XP_214325.5, XP_001070301.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32399.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..671
                     /product="3',5'-cyclic-AMP phosphodiesterase 4C"
                     /EC_number="3.1.4.53"
                     /note="cAMP-specific 3',5'-cyclic phosphodiesterase 4C;
                     cAMP-specific 35-cyclic phosphodiesterase 4C;
                     phosphodiesterase 4C, cAMP-specific (phosphodiesterase E1
                     dunce homolog, Drosophila); cAMP-specific
                     phosphodiesterase 4C"
                     /calculated_mol_wt=74108
     Region          154..270
                     /region_name="PDE4_UCR"
                     /note="Phosphodiesterase 4 upstream conserved regions
                     (UCR); pfam18100"
                     /db_xref="CDD:465648"
     Region          388..628
                     /region_name="PDEase_I"
                     /note="3'5'-cyclic nucleotide phosphodiesterase;
                     pfam00233"
                     /db_xref="CDD:459723"
     CDS             1..671
                     /gene="Pde4c"
                     /gene_synonym="Dpde1"
                     /coded_by="NM_001276765.1:1..2016"
                     /db_xref="GeneID:290646"
                     /db_xref="RGD:727918"
ORIGIN      
        1 mrrsgttlsf lltervrepv dsgvapvshl gggvilrrfs gtlllpplss rlgssgeaes
       61 aapvvftigs rgtershgsa qssfdlengl psgrgpldaq sgsslgralq ppvhhgqrre
      121 sflyrsdsdh epspkavsrt ssaasdlhge dmivtpfaqv laslrtvrsn vaalahgags
      181 atrqallgtp pqssqqaapa eesglqlaqe tleeldwcle qletlqtrrs vgemasnkfk
      241 rmlnrelthl setsrsgnqv seyisqtfld qqaevelpap ptedhpwpma qitglrksch
      301 tslptaaipr fgvqtdqeeq lakeledtnk wgfdvfkvae lsgnrpltav ifsvlqerdl
      361 lktfqipadt llrylltleg hyhsnvayhn sihaadvvqs ahvllgtpal eavftdlevl
      421 aaifacaihd vdhpgvsnqf lintnselal myndssvlen hhlavgfkll qgencdifqn
      481 lstkqklslr rmvidmvlat dmskhmslla dlktmvetkk vtslgvllld nysdriqvlq
      541 slvhcadlsn pakplplyrq wterimaeff qqgdreresg ldispmcdkh tasveksqvg
      601 fidyiahplw etwadlvhpd aqelldtled nrewyqsrvp cspphaigpd rfkfeltlee
      661 teeeeeeder h
//
LOCUS       NP_001029086             640 aa            linear   ROD 27-APR-2025
DEFINITION  epsin-2 isoform b [Rattus norvegicus].
ACCESSION   NP_001029086
VERSION     NP_001029086.1
DBSOURCE    REFSEQ: accession NM_001033914.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Sakai,E., Miura,Y., Suzuki-Kouyama,E., Oka,K., Tachibana,M.,
            Kawabata,K., Sakurai,F. and Mizuguchi,H.
  TITLE     A mammalian mirtron miR-1224 promotes tube-formation of human
            primary endothelial cells by targeting anti-angiogenic factor
            epsin2
  JOURNAL   Sci Rep 7 (1), 5541 (2017)
   PUBMED   28717225
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Sen,A., Madhivanan,K., Mukherjee,D. and Aguilar,R.C.
  TITLE     The epsin protein family: coordinators of endocytosis and signaling
  JOURNAL   Biomol Concepts 3 (2), 117-126 (2012)
   PUBMED   22942912
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Chen,H., Ko,G., Zatti,A., Di Giacomo,G., Liu,L., Raiteri,E.,
            Perucco,E., Collesi,C., Min,W., Zeiss,C., De Camilli,P. and
            Cremona,O.
  TITLE     Embryonic arrest at midgestation and disruption of Notch signaling
            produced by the absence of both epsin 1 and epsin 2 in mice
  JOURNAL   Proc Natl Acad Sci U S A 106 (33), 13838-13843 (2009)
   PUBMED   19666558
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Hussain,N.K., Yamabhai,M., Bhakar,A.L., Metzler,M., Ferguson,S.S.,
            Hayden,M.R., McPherson,P.S. and Kay,B.K.
  TITLE     A role for epsin N-terminal homology/AP180 N-terminal homology
            (ENTH/ANTH) domains in tubulin binding
  JOURNAL   J Biol Chem 278 (31), 28823-28830 (2003)
   PUBMED   12750376
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Polo,S., Sigismund,S., Faretta,M., Guidi,M., Capua,M.R., Bossi,G.,
            Chen,H., De Camilli,P. and Di Fiore,P.P.
  TITLE     A single motif responsible for ubiquitin recognition and
            monoubiquitination in endocytic proteins
  JOURNAL   Nature 416 (6879), 451-455 (2002)
   PUBMED   11919637
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Rosenthal,J.A., Chen,H., Slepnev,V.I., Pellegrini,L., Salcini,A.E.,
            Di Fiore,P.P. and De Camilli,P.
  TITLE     The epsins define a family of proteins that interact with
            components of the clathrin coat and contain a new protein module
  JOURNAL   J Biol Chem 274 (48), 33959-33965 (1999)
   PUBMED   10567358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000010.1, CB583573.1
            and BC094524.1.
            
            Summary: The protein encoded by this gene is a member of the epsin
            protein family. Epsin proteins are endocytic adaptors that function
            in the formation of clatherin-coated vesicles. Epsins contain a
            highly conserved N-terminal homology domain that binds
            phosphatidylinositol 4,5-bisphosphate in the plasma membrane, two
            or three ubiquitin interacting motifs, two clathrin-binding motifs,
            a cluster of aspartate-proline-tryptophan/phenylalanine repeats,
            and two or three asparagine-proline-phenylalanine tripeptide
            repeats at the C-terminus. In mouse, simultaneous knockout of this
            gene and its paralog results in embryonic arrest due to disruption
            of Notch signaling, suggesting a role as a specialized endocytic
            adaptor. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR compared to variant 3. Variants 2 and 3 encode isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211939.1, BC094524.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..640
                     /product="epsin-2 isoform b"
                     /note="EPS-15-interacting protein 2; EH domain binding
                     protein epsin 2"
                     /calculated_mol_wt=68322
     Region          19..141
                     /region_name="ENTH_Epsin"
                     /note="Epsin N-Terminal Homology (ENTH) domain of Epsin
                     family; cd16990"
                     /db_xref="CDD:340787"
     Site            order(25,29..30,63,69,73)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:340787"
     CDS             1..640
                     /gene="Epn2"
                     /coded_by="NM_001033914.2:284..2206"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:60443"
                     /db_xref="RGD:619773"
ORIGIN      
        1 mttssirrqm knivnnysea eikvreatsn dpwgpssslm teiadltynv vafseimsmv
       61 wkrlndhgkn wrhvykaltl ldyliktgse rvaqqcreni faiqtlkdfq yidrdgkdqg
      121 invrekskql vallkdeerl kvervqalkt kermaqvatg vgsnqitfgr gssqpnlsts
      181 yseqeygkag gspasyhgsp easlcpqhrt gamlgqseel qplsqrhpcl phlglashpn
      241 gdwaqpcltc draaratspr vsseleqarp qtsgeeelql qlalamsrev aeqeerlrrg
      301 ddlrlqmale esrrdtvkvp kkkevkacck pgshsqqttl ldlmdalpss gpvaqktepw
      361 stgtpanqtn pwggtvapan isdpwpsfgt kpaasvdpwg vpttasiqsv pknsdpwaas
      421 qqpasdagkt adawgaakps pasgsfelfs nfngtvkddf sefdnlrtsk kpaesgasvp
      481 pqdsrttspd lfesqsltsa sskpssarkt pesflgpnaa lvnldslvtk pnppaqslnp
      541 flapgaaapa pvnpfqvnqp qpltlnqlrg spvlgssasf gsgpgvetva pmpsvaphsa
      601 lgatgssltp lgptamnmvg svgippsaaq pagttnpfll
//
LOCUS       NP_001257605             254 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 10 [Rattus norvegicus].
ACCESSION   NP_001257605
VERSION     NP_001257605.1
DBSOURCE    REFSEQ: accession NM_001270676.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (10) lacks an alternate in-frame
            exon and uses an alternate exon in place of another exon in the 3'
            end of the gene, compared to variant 1. The resulting isoform (10)
            has the same N- and C-termini but is shorter and has a different
            internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224839.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..254
                     /product="troponin T, fast skeletal muscle isoform 10"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30003
     Region          58..194
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..254
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270676.1:117..881"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeape peekprpklt apkipegekv dfddiqkkrq
       61 nkdlmelqal idshfearkk eeeelialke riekrraera eqqriraeke rerqnrlaee
      121 karreeedak rraeddlkkk kalssmgany ssylakadqk rgkkqtarem kkkilaerrk
      181 plnidhlsdd klrdkakelw dtlyqletdk fefgeklkrq kydimtvrar vemlakfskk
      241 agatakgkvg grwk
//
LOCUS       NP_001257971             484 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC domain-containing protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257971
VERSION     NP_001257971.1
DBSOURCE    REFSEQ: accession NM_001271042.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1 and BC100090.1.
            
            Transcript Variant: This variant (2) contains multiple differences
            in the coding region and its transcription extends past a splice
            site that is used in variant 1, resulting in a novel 3' coding
            region and 3' UTR compared to variant 1. It encodes isoform 2 which
            is shorter and has a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100090.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13p11"
     Protein         1..484
                     /product="zinc finger CCHC domain-containing protein 2
                     isoform 2"
                     /note="zinc finger CCHC domain-containing protein 2; tumor
                     necrosis factor receptor superfamily, member 11a"
                     /calculated_mol_wt=53269
     Region          356..456
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(385..387,408..409,424)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132793"
     CDS             1..484
                     /gene="Zcchc2"
                     /gene_synonym="Tnfrsf11a"
                     /coded_by="NM_001271042.1:383..1837"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304695"
                     /db_xref="RGD:1310626"
ORIGIN      
        1 mlrmklppks thpsepppda eepeadarpg akapprrrrd crpppppptg lprgpppppp
       61 spprgleppv asgptagagm pgggghaaal reqervyewf glvlgsaqrl eflcglldlc
      121 nplelrflgs cledlarkdy hylrdseaka nglsdpgsla dfrepavrsr livylallgs
      181 enreaagrlh rllpqvdavl rslratrveg srgsvedepg gddeqdaekd gpgpegggca
      241 klgtggglgf raqeellllf tmaslhpafs fhqrvtlreh lerlrsalrv epedaeveps
      301 nfagsraqnd sacgdyiqsn etglveqaqi pqdgltvaph raqreavhie kimlkgvqrr
      361 radkyweytf kvnwsdlsvt tvtkthqelq efllklpkef ssesfdktil kalnqgslrr
      421 eerrhpdlep ilrqlfstsp qaflqshkvr sffrsisses qhsfnvlqht iihkkhagks
      481 pagk
//
LOCUS       NP_001258009             704 aa            linear   ROD 27-APR-2025
DEFINITION  SH3KBP1-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_001258009 XP_214873
VERSION     NP_001258009.1
DBSOURCE    REFSEQ: accession NM_001271080.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Feng,L., Wang,J.T., Jin,H., Qian,K. and Geng,J.G.
  TITLE     SH3KBP1-binding protein 1 prevents epidermal growth factor receptor
            degradation by the interruption of c-Cbl-CIN85 complex
  JOURNAL   Cell Biochem Funct 29 (7), 589-596 (2011)
   PUBMED   21830225
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Borinstein,S.C., Hyatt,M.A., Sykes,V.W., Straub,R.E., Lipkowitz,S.,
            Boulter,J. and Bogler,O.
  TITLE     SETA is a multifunctional adapter protein with three SH3 domains
            that binds Grb2, Cbl, and the novel SB1 proteins
  JOURNAL   Cell Signal 12 (11-12), 769-779 (2000)
   PUBMED   11152963
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 31, 2012 this sequence version replaced XP_214873.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.1409.1,
                                           SRR26643287.808.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..704
                     /product="SH3KBP1-binding protein 1"
                     /note="SETA-binding protein 1"
                     /calculated_mol_wt=75841
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBC3; propagated from
                     UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          18..120
                     /region_name="BTB_POZ_SHKBP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in SH3KBP1-binding
                     protein 1 (SHKBP1); cd18393"
                     /db_xref="CDD:349701"
     Region          146..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBC3; propagated from
                     UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          233..280
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          283..322
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          324..359
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          428..466
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          548..586
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          609..704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          618..623
                     /region_name="PXXXPR. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBC3; propagated from
                     UniProtKB/Swiss-Prot (P0C5J9.1)"
     Site            646
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TBC3; propagated from
                     UniProtKB/Swiss-Prot (P0C5J9.1)"
     Region          678..683
                     /region_name="PXXXPR. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C5J9.1)"
     CDS             1..704
                     /gene="Shkbp1"
                     /gene_synonym="RGD1309281; Sb1"
                     /coded_by="NM_001271080.1:1..2115"
                     /db_xref="GeneID:292735"
                     /db_xref="RGD:1309281"
ORIGIN      
        1 mavpttaveg vrsrgapgev ihlnvggkrf stsrqtltwi pdsffsslls gristlkdet
       61 gaifidrdpt vfapilnflr tkeldprgvh gssllheaqf ygltplvrrl qvreeldrss
      121 cgnvlfngyl pppvfpvkrr nrhslvgpqq iggrpapvrr sntmppnlgn agllgrmldd
      181 rappspsgqp eepgmvrlvc ghhnwiavay thflvcyrlk easgwqlafs sprldwpier
      241 laltarvlgg apgehdkmva aatgseillw alqaqgggse igvfhlgvpv ealffvgnql
      301 iatshtgrig vwnavtkhwq vqevqpitsy daagsflllg csngsiyyvd vqkfplrmkd
      361 ndllvselyr dpaedgvtal svyltpktsd sgnwieiayg tssgvvrviv qhpetvgsgp
      421 qlfqtfsvhr spvtkimlse khlisvcadn nhvrtwsvtr frgmistqpg stplasfkil
      481 alesadglgg csagndigpy gerddqqvfi qkvvpnasql fvrlsstgqr vcsvrsvdgs
      541 attaftvlec egsrrlgsrp rrylltgqan gslamwdltt amdglgqtpa gglteeelmd
      601 qleqcelspl tssrasfpsp sprtsltslh sassntslcg hrgspsppqa garsrgagsf
      661 vdrfkelarg apelrgpptp aprpstslgn plilpkntln etsf
//
LOCUS       NP_113740                673 aa            linear   ROD 27-APR-2025
DEFINITION  gamma-adducin isoform 2 [Rattus norvegicus].
ACCESSION   NP_113740 XP_346590
VERSION     NP_113740.2
DBSOURCE    REFSEQ: accession NM_031552.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Fan,L., Gao,W., Liu,Y., Jefferson,J.R., Fan,F. and Roman,R.J.
  TITLE     Knockout of gamma-Adducin Promotes
            NG-Nitro-L-Arginine-Methyl-Ester-Induced Hypertensive Renal Injury
  JOURNAL   J Pharmacol Exp Ther 377 (1), 189-198 (2021)
   PUBMED   33414130
  REMARK    GeneRIF: Knockout of gamma-Adducin Promotes
            N(G)-Nitro-L-Arginine-Methyl-Ester-Induced Hypertensive Renal
            Injury.
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Gao,W., Liu,Y., Fan,L., Zheng,B., Jefferson,J.R., Wang,S.,
            Zhang,H., Fang,X., Nguyen,B.V., Zhu,T., Roman,R.J. and Fan,F.
  TITLE     Role of gamma-adducin in actin cytoskeleton rearrangements in
            podocyte pathophysiology
  JOURNAL   Am J Physiol Renal Physiol 320 (1), F97-F113 (2021)
   PUBMED   33308016
  REMARK    GeneRIF: Role of gamma-adducin in actin cytoskeleton rearrangements
            in podocyte pathophysiology.
            GeneRIF: Reduced ADD3 function in FHH rats alters baseline podocyte
            pathophysiology by rearrangement of the actin cytoskeleton at the
            onset of proteinuria in young animals.
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Fan,F., Geurts,A.M., Pabbidi,M.R., Ge,Y., Zhang,C., Wang,S.,
            Liu,Y., Gao,W., Guo,Y., Li,L., He,X., Lv,W., Muroya,Y., Hirata,T.,
            Prokop,J., Booz,G.W., Jacob,H.J. and Roman,R.J.
  TITLE     A Mutation in gamma-Adducin Impairs Autoregulation of Renal Blood
            Flow and Promotes the Development of Kidney Disease
  JOURNAL   J Am Soc Nephrol 31 (4), 687-700 (2020)
   PUBMED   32029431
  REMARK    GeneRIF: A Mutation in gamma-Adducin Impairs Autoregulation of
            Renal Blood Flow and Promotes the Development of Kidney Disease.
            GeneRIF: A mutation in ADD3 that alters ACTIN binding causes renal
            vascular dysfunction and promotes the susceptibility to kidney
            disease.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Fan,F., Pabbidi,M.R., Ge,Y., Li,L., Wang,S., Mims,P.N. and
            Roman,R.J.
  TITLE     Knockdown of Add3 impairs the myogenic response of renal afferent
            arterioles and middle cerebral arteries
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F971-F981 (2017)
   PUBMED   27927653
  REMARK    GeneRIF: Add3 may play a causal role in the impaired myogenic
            response and autoregulation in the renal and cerebral circulation
            in hypertensive rats.
            GeneRIF: Mutation of Add3 may play a causal role in the impaired
            myogenic response and blood flow autoregulation in the renal and
            cerebral circulation.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Tripodi,G., Szpirer,C., Reina,C., Szpirer,J. and Bianchi,G.
  TITLE     Polymorphism of gamma-adducin gene in genetic hypertension and
            mapping of the gene to rat chromosome 1q55
  JOURNAL   Biochem Biophys Res Commun 237 (3), 685-689 (1997)
   PUBMED   9299427
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Chapline,C., Ramsay,K., Klauck,T. and Jaken,S.
  TITLE     Interaction cloning of protein kinase C substrates
  JOURNAL   J Biol Chem 268 (10), 6858-6861 (1993)
   PUBMED   8463212
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Lebowitz,M.S. and Pedersen,P.L.
  TITLE     Regulation of the mitochondrial ATP synthase/ATPase complex: cDNA
            cloning, sequence, overexpression, and secondary structural
            characterization of a functional protein inhibitor
  JOURNAL   Arch Biochem Biophys 301 (1), 64-70 (1993)
   PUBMED   8442667
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Pinto-Correia,C., Goldstein,E.G., Bennett,V. and Sobel,J.S.
  TITLE     Immunofluorescence localization of an adducin-like protein in the
            chromosomes of mouse oocytes
  JOURNAL   Dev Biol 146 (2), 301-311 (1991)
   PUBMED   1864459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB757924.1, U35775.1, FM038946.1, FM072500.1, AW141606.1,
            CO402732.1, CK596161.1, FM059497.1, CF111029.1 and AA899625.1.
            
            On Aug 12, 2009 this sequence version replaced NP_113740.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The resulting
            isoform (2) lacks an internal segment near the C-terminus, compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U35775.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..673
                     /product="gamma-adducin isoform 2"
                     /note="potein kinase C binding protein 35H; adducin-like
                     protein 70; protein kinase C-binding protein 35H;
                     gamma-adducin; adducin 3 (gamma)"
                     /calculated_mol_wt=75245
     Region          137..385
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(143,147,155,180,182..183,233,235..236,241..243,251,
                     253..254,265,293,304,311,315,322,340)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(160,177..178,203..205,231,233,294)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(231,233,294)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..673
                     /gene="Add3"
                     /coded_by="NM_031552.2:217..2238"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25230"
                     /db_xref="RGD:2043"
ORIGIN      
        1 mssdtsqavi ttppppsmph keryfdrine sdpeylrern mspdlrqdfn mmeqrkrvtq
       61 ilqspafred lecliqeqmk kghdptglla lqqiadyima nsftgfsspp lslgmvtpin
      121 dlpgadtssy vkgekltrck laslyrladl fgwahlanty isvrvskeqd hiiiiprgls
      181 fseatasalv kvniigevvd qgstnlkidh sgfsphaaiy strpdvkcvi hihtlataav
      241 ssmkcgilpi sqeslilgdv ayydyqgsld eeeerielqk vlgpsckvlv lrnhgvvalg
      301 etleeafhyi fnvqmaceiq vqavagaggv dnllildlqk ykafthgvam tggggvnmgs
      361 hqkwkvgeie feglmrtldn lgyrtgyayr hplvrekprh ksdveipatv tafsfeddsv
      421 plsplkymaq rqqrektrwl nspntymkvn vpeesrnget sprtkitwmk aedpskvssg
      481 tpikiedpnq fvplntnpte vlekrnkire qnrydlktag pqsqllagiv vdkppstmrf
      541 edddqgppap pnpfshlmeg eleeytktie rkqqgldenh elfsksftsv dvpvivngkd
      601 emhdvedela qrvsrlttst tienieitik spdrteevls pdgspsksps kkkkkfrtps
      661 flkknkkkek vea
//
LOCUS       NP_001296230             218 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001296230
VERSION     NP_001296230.1
DBSOURCE    REFSEQ: accession NM_001309301.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   O'Donnell,B.M., Mackie,T.D., Subramanya,A.R. and Brodsky,J.L.
  TITLE     Endoplasmic reticulum-associated degradation of the renal potassium
            channel, ROMK, leads to type II Bartter syndrome
  JOURNAL   J Biol Chem 292 (31), 12813-12827 (2017)
   PUBMED   28630040
  REMARK    GeneRIF: Data suggest underlying pathology for some patients with
            type II Bartter syndrome is linked to stability of ROMK1 in ERAD
            pathway; using a yeast expression system, cells can be rescued by
            wild-type (rat) ROMK1 but not by ROMK1 containing any one of four
            mutations found in (human) type II Bartter syndrome; mutant ROMKs
            are significantly less stable than wild-type ROMK. (ERAD =
            endoplasmic reticulum-associated degradation)
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Araujo,M., Welch,W.J., Zhou,X., Sullivan,K., Walsh,S., Pasternak,A.
            and Wilcox,C.S.
  TITLE     Inhibition of ROMK blocks macula densa tubuloglomerular feedback
            yet causes renal vasoconstriction in anesthetized rats
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F1120-F1127 (2017)
   PUBMED   28228405
  REMARK    GeneRIF: Blockade of ROMK or Na(+)-K(+)-2Cl(-) transport inhibits
            tubuloglomerular feedback yet increases renal vascular resistance.
            The renal vasoconstriction was independent of volume depletion,
            blood pressure, TGF, or proximal tubule hydrostatic pressure.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Smoot,B., Kober,K.M., Paul,S.M., Levine,J.D., Abrams,G.,
            Mastick,J., Topp,K., Conley,Y.P. and Miaskowski,C.A.
  TITLE     Potassium Channel Candidate Genes Predict the Development of
            Secondary Lymphedema Following Breast Cancer Surgery
  JOURNAL   Nurs Res 66 (2), 85-94 (2017)
   PUBMED   28252570
  REMARK    GeneRIF: These preliminary findings suggest that K channel genes
            play a role in the development of secondary lymphedema
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Bollepalli,M.K., Fowler,P.W., Rapedius,M., Shang,L., Sansom,M.S.,
            Tucker,S.J. and Baukrowitz,T.
  TITLE     State-dependent network connectivity determines gating in a K+
            channel
  JOURNAL   Structure 22 (7), 1037-1046 (2014)
   PUBMED   24980796
  REMARK    GeneRIF: Data indicate that mutations in kir1.1 potassium channel
            preferentially increase pH sensitivity.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Hu,J., Qiu,S., Yang,F., Cao,Z., Li,W. and Wu,Y.
  TITLE     Unique mechanism of the interaction between honey bee toxin TPNQ
            and rKir1.1 potassium channel explored by computational
            simulations: insights into the relative insensitivity of channel
            towards animal toxins
  JOURNAL   PLoS One 8 (7), e67213 (2013)
   PUBMED   23874410
  REMARK    GeneRIF: The TPNQ toxin-rKir1.1 channel complex structure not only
            revealed their unique interaction mechanism, but also elucidate the
            relative insensitivity of rKir1.1 channel towards animal toxins.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Beesley,A.H., Ortega,B. and White,S.J.
  TITLE     Splicing of a retained intron within ROMK K+ channel RNA generates
            a novel set of isoforms in rat kidney
  JOURNAL   Am J Physiol 276 (3), C585-C592 (1999)
   PUBMED   10069985
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Derst,C., Konrad,M., Kockerling,A., Karolyi,L., Deschenes,G.,
            Daut,J., Karschin,A. and Seyberth,H.W.
  TITLE     Mutations in the ROMK gene in antenatal Bartter syndrome are
            associated with impaired K+ channel function
  JOURNAL   Biochem Biophys Res Commun 230 (3), 641-645 (1997)
   PUBMED   9015377
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Boim,M.A., Ho,K., Shuck,M.E., Bienkowski,M.J., Block,J.H.,
            Slightom,J.L., Yang,Y., Brenner,B.M. and Hebert,S.C.
  TITLE     ROMK inwardly rectifying ATP-sensitive K+ channel. II. Cloning and
            distribution of alternative forms
  JOURNAL   Am J Physiol 268 (6 Pt 2), F1132-F1140 (1995)
   PUBMED   7611454
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Zhou,H., Tate,S.S. and Palmer,L.G.
  TITLE     Primary structure and functional properties of an epithelial K
            channel
  JOURNAL   Am J Physiol 266 (3 Pt 1), C809-C824 (1994)
   PUBMED   8166245
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Ho,K., Nichols,C.G., Lederer,W.J., Lytton,J., Vassilev,P.M.,
            Kanazirska,M.V. and Hebert,S.C.
  TITLE     Cloning and expression of an inwardly rectifying ATP-regulated
            potassium channel
  JOURNAL   Nature 362 (6415), 31-38 (1993)
   PUBMED   7680431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            Transcript Variant: This variant (5, also known as ROMK1.1)
            contains an alternate exon in the 5' UTR, lacks a portion of the 5'
            coding region, and initiates translation at a downstream start
            codon, compared to variant 1. It encodes isoform 3 which has a
            shorter N-terminus compared to isoform 1. Variants 3, 4 and 5
            encode the same protein (isoform 3).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF081365.1, SRR26643287.19764.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN14984041,
                                           SAMN17050764 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..218
                     /product="ATP-sensitive inward rectifier potassium channel
                     1 isoform 3"
                     /note="K+ channel protein; ATP-sensitive inward rectifier
                     potassium channel 1; ATP-regulated potassium channel
                     ROM-K; potassium channel, inwardly rectifying subfamily J
                     member 1; inward rectifier K(+) channel Kir1.1"
                     /calculated_mol_wt=24513
     Region          19..191
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..218
                     /gene="Kcnj1"
                     /gene_synonym="KAB-1; Kcnj; Kcnj1_v1; Kcnj1_v3; kir1.1;
                     ROMK1; ROMK2; ROMK3"
                     /coded_by="NM_001309301.1:493..1149"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:24521"
                     /db_xref="RGD:2957"
ORIGIN      
        1 mcgailakis rpkkraktit fsknaviskr ggklcllirv anlrksllig shiygkllkt
       61 titpegetii ldqtninfvv dagnenlffi spltiyhiid hnspffhmaa etlsqqdfel
      121 vvfldgtves tsatcqvrts yvpeevlwgy rfvpivsktk egkyrvdfhn fgktvevetp
      181 hcamclynek dararmkrgy dnpnfvlsev detddtqm
//
LOCUS       NP_203502                366 aa            linear   ROD 27-APR-2025
DEFINITION  IgG receptor FcRn large subunit p51 precursor [Rattus norvegicus].
ACCESSION   NP_203502
VERSION     NP_203502.1
DBSOURCE    REFSEQ: accession NM_033351.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Yadav,S.P.S., Sandoval,R.M., Zhao,J., Huang,Y., Wang,E., Kumar,S.,
            Campos-Bilderback,S.B., Rhodes,G., Mechref,Y., Molitoris,B.A. and
            Wagner,M.C.
  TITLE     Mechanism of how carbamylation reduces albumin binding to FcRn
            contributing to increased vascular clearance
  JOURNAL   Am J Physiol Renal Physiol 320 (1), F114-F129 (2021)
   PUBMED   33283642
  REMARK    GeneRIF: Mechanism of how carbamylation reduces albumin binding to
            FcRn contributing to increased vascular clearance.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Wagner,M.C., Myslinski,J., Pratap,S., Flores,B., Rhodes,G.,
            Campos-Bilderback,S.B., Sandoval,R.M., Kumar,S., Patel,M., Ashish
            and Molitoris,B.A.
  TITLE     Mechanism of increased clearance of glycated albumin by proximal
            tubule cells
  JOURNAL   Am J Physiol Renal Physiol 310 (10), F1089-F1102 (2016)
   PUBMED   26887834
  REMARK    GeneRIF: significant structural changes occur to albumin with
            glycation, particularly in the FcRn-binding region, which could
            explain the reduced affinity to FcRn
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Abdiche,Y.N., Yeung,Y.A., Chaparro-Riggers,J., Barman,I., Strop,P.,
            Chin,S.M., Pham,A., Bolton,G., McDonough,D., Lindquist,K., Pons,J.
            and Rajpal,A.
  TITLE     The neonatal Fc receptor (FcRn) binds independently to both sites
            of the IgG homodimer with identical affinity
  JOURNAL   MAbs 7 (2), 331-343 (2015)
   PUBMED   25658443
  REMARK    GeneRIF: The neonatal Fc receptor (FcRn) binds independently to
            both sites of the IgG homodimer with identical affinity.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Neuber,T., Frese,K., Jaehrling,J., Jager,S., Daubert,D.,
            Felderer,K., Linnemann,M., Hohne,A., Kaden,S., Kolln,J., Tiller,T.,
            Brocks,B., Ostendorp,R. and Pabst,S.
  TITLE     Characterization and screening of IgG binding to the neonatal Fc
            receptor
  JOURNAL   MAbs 6 (4), 928-942 (2014)
   PUBMED   24802048
  REMARK    GeneRIF: Characterization and screening of IgG binding to the
            neonatal Fc receptor.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Kliwinski,C., Cooper,P.R., Perkinson,R., Mabus,J.R., Tam,S.H.,
            Wilkinson,T.M., Giles-Komar,J., Scallon,B., Powers,G.D. and
            Hornby,P.J.
  TITLE     Contribution of FcRn binding to intestinal uptake of IgG in
            suckling rat pups and human FcRn-transgenic mice
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 304 (3), G262-G270 (2013)
   PUBMED   23220220
  REMARK    GeneRIF: The suckling rat pup intestine is a mechanistic model of
            FcRn-IgG-mediated transcytosis
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Vaughn,D.E. and Bjorkman,P.J.
  TITLE     Structural basis of pH-dependent antibody binding by the neonatal
            Fc receptor
  JOURNAL   Structure 6 (1), 63-73 (1998)
   PUBMED   9493268
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Story,C.M., Mikulska,J.E. and Simister,N.E.
  TITLE     A major histocompatibility complex class I-like Fc receptor cloned
            from human placenta: possible role in transfer of immunoglobulin G
            from mother to fetus
  JOURNAL   J Exp Med 180 (6), 2377-2381 (1994)
   PUBMED   7964511
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Burmeister,W.P., Huber,A.H. and Bjorkman,P.J.
  TITLE     Crystal structure of the complex of rat neonatal Fc receptor with
            Fc
  JOURNAL   Nature 372 (6504), 379-383 (1994)
   PUBMED   7969498
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Simister,N.E. and Mostov,K.E.
  TITLE     An Fc receptor structurally related to MHC class I antigens
  JOURNAL   Nature 337 (6203), 184-187 (1989)
   PUBMED   2911353
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Simister,N.E. and Mostov,K.E.
  TITLE     Cloning and expression of the neonatal rat intestinal Fc receptor,
            a major histocompatibility complex class I antigen homolog
  JOURNAL   Cold Spring Harb Symp Quant Biol 54 Pt 1, 571-580 (1989)
   PUBMED   2534798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M35495.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M35495.1, SRR8487227.114136.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..366
                     /product="IgG receptor FcRn large subunit p51 precursor"
                     /note="neonatal Fc receptor; igG receptor FcRn large
                     subunit p51; igG Fc fragment receptor transporter alpha
                     chain; Fc fragment immunoglobulin G receptor; Fc receptor,
                     IgG, alpha chain transporter; Fc fragment of IgG,
                     receptor, transporter, alpha; Fc fragment of IgG receptor
                     and transporter"
                     /calculated_mol_wt=37833
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2354
     mat_peptide     23..366
                     /product="IgG receptor FcRn large subunit p51"
                     /calculated_mol_wt=37833
     Region          23..111
                     /region_name="Alpha-1.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Region          25..198
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          112..201
                     /region_name="Alpha-2.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          199..291
                     /region_name="IgC1_MHC-like_FcRn"
                     /note="immunoglobulin domain of neonatal Fc receptor,
                     major histocompatibility complex (MHC)-like; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd21011"
                     /db_xref="CDD:409602"
     Region          202..291
                     /region_name="Alpha-3.
                     /evidence=ECO:0000269|PubMed:7969498,
                     ECO:0000269|PubMed:9493268, ECO:0007744|PDB:1FRT,
                     ECO:0007744|PDB:3FRU"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Region          203..211
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409602"
     Site            order(207..210,219,221,223,225,258..261,263,265..266)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409602"
     Region          219..228
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409602"
     Region          232..238
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409602"
     Region          240..243
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409602"
     Region          245..253
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409602"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          258..266
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409602"
     Region          273..280
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409602"
     Region          287..290
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409602"
     Region          293..298
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            299..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55899; propagated from
                     UniProtKB/Swiss-Prot (P13599.1)"
     Region          344..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13599.1)"
     CDS             1..366
                     /gene="Fcgrt"
                     /gene_synonym="FcRn"
                     /coded_by="NM_033351.2:203..1303"
                     /db_xref="GeneID:29558"
                     /db_xref="RGD:61811"
ORIGIN      
        1 mgmsqpgvll slllvllpqt wgaeprlplm yhlaavsdls tglpsfwatg wlgaqqylty
       61 nnlrqeadpc gawiwenqvs wywekettdl kskeqlflea irtlenqing tftlqgllgc
      121 elapdnsslp tavfalngee fmrfnprtgn wsgewpetdi vgnlwmkqpe aarkesefll
      181 tscperllgh lergrqnlew keppsmrlka rpgnsgssvl tcaafsfypp elkfrflrng
      241 lasgsgncst gpngdgsfha wsllevkrgd ehhyqcqveh eglaqpltvd ldsparssvp
      301 vvgiilglll vvvaiaggvl lwnrmrsglp apwlslsgdd sgdllpggnl ppeaepqgvn
      361 afpats
//
LOCUS       NP_115851                256 aa            linear   ROD 27-APR-2025
DEFINITION  calsenilin [Rattus norvegicus].
ACCESSION   NP_115851
VERSION     NP_115851.1
DBSOURCE    REFSEQ: accession NM_032462.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Ismail,C.A.N., Suppian,R., Ab Aziz,C.B. and Long,I.
  TITLE     Ifenprodil Reduced Expression of Activated Microglia, BDNF and
            DREAM Proteins in the Spinal Cord Following Formalin Injection
            During the Early Stage of Painful Diabetic Neuropathy in Rats
  JOURNAL   J Mol Neurosci 71 (2), 379-393 (2021)
   PUBMED   32671697
  REMARK    GeneRIF: Ifenprodil Reduced Expression of Activated Microglia, BDNF
            and DREAM Proteins in the Spinal Cord Following Formalin Injection
            During the Early Stage of Painful Diabetic Neuropathy in Rats.
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Formisano,L., Laudati,G., Guida,N., Mascolo,L., Serani,A.,
            Cuomo,O., Cantile,M., Boscia,F., Molinaro,P., Anzilotti,S.,
            Pizzorusso,V., Di Renzo,G., Pignataro,G. and Annunziato,L.
  TITLE     HDAC4 and HDAC5 form a complex with DREAM that epigenetically
            down-regulates NCX3 gene and its pharmacological inhibition reduces
            neuronal stroke damage
  JOURNAL   J Cereb Blood Flow Metab 40 (10), 2081-2097 (2020)
   PUBMED   31696766
  REMARK    GeneRIF: HDAC4 and HDAC5 form a complex with DREAM that
            epigenetically down-regulates NCX3 gene and its pharmacological
            inhibition reduces neuronal stroke damage.
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Tian,N.X., Xu,Y., Yang,J.Y., Li,L., Sun,X.H., Wang,Y. and Zhang,Y.
  TITLE     KChIP3 N-Terminal 31-50 Fragment Mediates Its Association with
            TRPV1 and Alleviates Inflammatory Hyperalgesia in Rats
  JOURNAL   J Neurosci 38 (7), 1756-1773 (2018)
   PUBMED   29335353
  REMARK    GeneRIF: The KChIP3-TRPV1 interaction reduces the surface
            localization of TRPV1 and thus alleviates heat hyperalgesia and
            gait alterations induced by peripheral inflammation
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Qian,J., Lv,M. and Zhang,W.
  TITLE     The function of DREAM gene mediated by NF-kB signal pathway in the
            pathogenesis of osteosarcoma
  JOURNAL   J BUON 22 (4), 1068-1072 (2017)
   PUBMED   28952229
  REMARK    GeneRIF: NF-kB signal pathway promoted the expression of DREAM
            gene.
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Siran,R., Ahmad,A.H., Abdul Aziz,C.B. and Ismail,Z.
  TITLE     REM sleep deprivation induces changes of down regulatory antagonist
            modulator (DREAM) expression in the ventrobasal thalamic nuclei of
            sprague-dawley rats
  JOURNAL   J Physiol Biochem 70 (4), 877-889 (2014)
   PUBMED   25218926
  REMARK    GeneRIF: DREAM expression and REM sleep deprivation, as well as
            sleep recovery, are linked which may indicate potential involvement
            of DREAM in REM sleep-induced changes in gene expression,
            specifically in nociceptive processing.
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Leclerc,G.M., Leclerc,G.J., Shorte,S.L., Stephen Frawley,L. and
            Boockfor,F.R.
  TITLE     Cloning and mRNA expression of the Ca2+-binding DREAM protein in
            the pituitary
  JOURNAL   Gen Comp Endocrinol 129 (1), 45-55 (2002)
   PUBMED   12409095
  REMARK    GeneRIF: Findings of DREAM expression in the pituitary in a manner
            specific to pituitary endocrine cell type raises the possibility
            that this protein may play a role in determining specific pituitary
            cell function.[DREAM protein]
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Takimoto,K., Yang,E.K. and Conforti,L.
  TITLE     Palmitoylation of KChIP splicing variants is required for efficient
            cell surface expression of Kv4.3 channels
  JOURNAL   J Biol Chem 277 (30), 26904-26911 (2002)
   PUBMED   12006572
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Cheng,H.Y., Pitcher,G.M., Laviolette,S.R., Whishaw,I.Q., Tong,K.I.,
            Kockeritz,L.K., Wada,T., Joza,N.A., Crackower,M., Goncalves,J.,
            Sarosi,I., Woodgett,J.R., Oliveira-dos-Santos,A.J., Ikura,M., van
            der Kooy,D., Salter,M.W. and Penninger,J.M.
  TITLE     DREAM is a critical transcriptional repressor for pain modulation
  JOURNAL   Cell 108 (1), 31-43 (2002)
   PUBMED   11792319
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Ohya,S., Morohashi,Y., Muraki,K., Tomita,T., Watanabe,M.,
            Iwatsubo,T. and Imaizumi,Y.
  TITLE     Molecular cloning and expression of the novel splice variants of
            K(+) channel-interacting protein 2
  JOURNAL   Biochem Biophys Res Commun 282 (1), 96-102 (2001)
   PUBMED   11263977
REFERENCE   10 (residues 1 to 256)
  AUTHORS   An,W.F., Bowlby,M.R., Betty,M., Cao,J., Ling,H.P., Mendoza,G.,
            Hinson,J.W., Mattsson,K.I., Strassle,B.W., Trimmer,J.S. and
            Rhodes,K.J.
  TITLE     Modulation of A-type potassium channels by a family of calcium
            sensors
  JOURNAL   Nature 403 (6769), 553-556 (2000)
   PUBMED   10676964
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF297118.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF297118.1, AB043892.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /strain="CD IGS"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..256
                     /product="calsenilin"
                     /note="calsenilin, presenilin-binding protein, EF hand
                     transcription factor; A-type potassium channel modulating
                     protein 3; downstream regulatory element-antagonist
                     modulator; KChIP3; DRE-antagonist modulator; kv
                     channel-interacting protein 3; A-type potassium channel
                     modulatory protein 3; Kv channel interacting protein 3,
                     calsenilin"
                     /calculated_mol_wt=29339
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM47.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JM47.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXT8; propagated from
                     UniProtKB/Swiss-Prot (Q9JM47.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2W7; propagated from
                     UniProtKB/Swiss-Prot (Q9JM47.1)"
     Region          107..241
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          243..256
                     /region_name="Interaction with KCND2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JM47.1)"
     CDS             1..256
                     /gene="Kcnip3"
                     /gene_synonym="Csen; Dream; rKChIP3"
                     /coded_by="NM_032462.2:22..792"
                     /db_xref="GeneID:65199"
                     /db_xref="RGD:70888"
ORIGIN      
        1 mqrtkeamka sdgsllgdpg riplskregi kwqrprftrq almrcclikw ilssaapqgs
       61 dssdselels tvrhqpegld qlqaqtkftk kelqslyrgf knecptglvd edtfkliysq
      121 ffpqgdatty ahflfnafda dgngaihfed fvvglsillr gtvheklkwa fnlydinkdg
      181 yitkeemlai mksiydmmgr htypilrkda plehverffq kmdrnqdgvv tidefletcq
      241 kdenimssmq lfenvi
//
LOCUS       NP_001099199             387 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein neuro-d4 [Rattus norvegicus].
ACCESSION   NP_001099199 XP_001075457 XP_341823
VERSION     NP_001099199.2
DBSOURCE    REFSEQ: accession NM_001105729.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Staahl,B.T., Tang,J., Wu,W., Sun,A., Gitler,A.D., Yoo,A.S. and
            Crabtree,G.R.
  TITLE     Kinetic analysis of npBAF to nBAF switching reveals exchange of
            SS18 with CREST and integration with neural developmental pathways
  JOURNAL   J Neurosci 33 (25), 10348-10361 (2013)
   PUBMED   23785148
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Shain,A.H. and Pollack,J.R.
  TITLE     The spectrum of SWI/SNF mutations, ubiquitous in human cancers
  JOURNAL   PLoS One 8 (1), e55119 (2013)
   PUBMED   23355908
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Hargreaves,D.C. and Crabtree,G.R.
  TITLE     ATP-dependent chromatin remodeling: genetics, genomics and
            mechanisms
  JOURNAL   Cell Res 21 (3), 396-420 (2011)
   PUBMED   21358755
  REMARK    Review article
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Lessard,J., Wu,J.I., Ranish,J.A., Wan,M., Winslow,M.M.,
            Staahl,B.T., Wu,H., Aebersold,R., Graef,I.A. and Crabtree,G.R.
  TITLE     An essential switch in subunit composition of a chromatin
            remodeling complex during neural development
  JOURNAL   Neuron 55 (2), 201-215 (2007)
   PUBMED   17640523
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Buchman,V.L., Ninkina,N.N., Bogdanov,Y.D., Bortvin,A.L.,
            Akopian,H.N., Kiselev,S.L., Krylova,O.Yu., Anokhin,K.V. and
            Georgiev,G.P.
  TITLE     Differential splicing creates a diversity of transcripts from a
            neurospecific developmentally regulated gene encoding a protein
            with new zinc-finger motifs
  JOURNAL   Nucleic Acids Res 20 (21), 5579-5585 (1992)
   PUBMED   1454523
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO396551.1, BC159415.1 and JAXUCZ010000001.1.
            
            On Sep 27, 2011 this sequence version replaced NP_001099199.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC159415.1, SRR26643298.2217.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..387
                     /product="zinc finger protein neuro-d4"
                     /note="neuro-d4; neuronal d4 domain family member; BAF45B;
                     BRG1-associated factor 45B; D4, zinc and double PHD
                     fingers family 1"
                     /calculated_mol_wt=44093
     Region          12..78
                     /region_name="DPF1-3_N"
                     /note="DPF1-3, N-terminal; pfam14051"
                     /db_xref="CDD:464074"
     Region          <191..219
                     /region_name="SFP1"
                     /note="Putative transcriptional repressor regulating G2/M
                     transition [Transcription / Cell division and chromosome
                     partitioning]; COG5189"
                     /db_xref="CDD:227516"
     Region          269..326
                     /region_name="PHD1_DPF1"
                     /note="PHD finger 1 found in D4, zinc and double PHD
                     fingers family 1 (DPF1); cd15690"
                     /db_xref="CDD:277160"
     Site            order(273,275..276,278,293,298..300,305..307,320,322..324)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277160"
     Site            order(307..308,310..311,314..315,318,320..321,323,325)
                     /site_type="other"
                     /note="PHD2 interface [polypeptide binding]"
                     /db_xref="CDD:277160"
     Region          327..372
                     /region_name="PHD2_d4"
                     /note="PHD finger 2 found in d4 gene family proteins;
                     cd15530"
                     /db_xref="CDD:277005"
     Site            order(327,342..348)
                     /site_type="other"
                     /note="PHD1 interface [polypeptide binding]"
                     /db_xref="CDD:277005"
     Site            order(334,337..344,352,362..367)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277005"
     CDS             1..387
                     /gene="Dpf1"
                     /gene_synonym="Neud4"
                     /coded_by="NM_001105729.3:76..1239"
                     /db_xref="GeneID:50545"
                     /db_xref="RGD:61868"
ORIGIN      
        1 matvipspls lgedfyreai ehcrsynarl caerslrlpf ldsqtgvaqn ncyiwmekth
       61 rgpglapgqi ytyparcwrk krrlniledp rlrpceykid ceaplkkegg lpegpvleal
      121 lcaetgekkv elkeeetimd cqkqqllefp hdlevedlee diprrknrak gkaygigglr
      181 krqdnasled rdkpyvcdic gkryknrpgl syhyththla eeegeehter halpfhrknn
      241 hkqfykelaw vpeaqrkhta kkapdgtvip ngycdfclgg skktgcpedl iscadcgrsg
      301 hpsclqftvn mtaavrtyrw qcieckscsl cgtsenddql lfcddcdrgy hmyclsppma
      361 eppegswsch lclrhlkeka sayitlt
//
LOCUS       NP_001258187            2122 aa            linear   ROD 27-APR-2025
DEFINITION  YLP motif-containing protein 1 [Rattus norvegicus].
ACCESSION   NP_001258187 XP_001057111 XP_234416
VERSION     NP_001258187.1
DBSOURCE    REFSEQ: accession NM_001271258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2122)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 2122)
  AUTHORS   Ulke-Lemee,A., Trinkle-Mulcahy,L., Chaulk,S., Bernstein,N.K.,
            Morrice,N., Glover,M., Lamond,A.I. and Moorhead,G.B.
  TITLE     The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
            nucleoside kinase that complexes with SAM68, CIA, NF110/45, and
            HNRNP-G
  JOURNAL   Biochim Biophys Acta 1774 (10), 1339-1350 (2007)
   PUBMED   17890166
REFERENCE   3  (residues 1 to 2122)
  AUTHORS   Armstrong,L., Lako,M., van Herpe,I., Evans,J., Saretzki,G. and
            Hole,N.
  TITLE     A role for nucleoprotein Zap3 in the reduction of telomerase
            activity during embryonic stem cell differentiation
  JOURNAL   Mech Dev 121 (12), 1509-1522 (2004)
   PUBMED   15511642
REFERENCE   4  (residues 1 to 2122)
  AUTHORS   Peeraully,M.R., Jenkins,J.R. and Trayhurn,P.
  TITLE     NGF gene expression and secretion in white adipose tissue:
            regulation in 3T3-L1 adipocytes by hormones and inflammatory
            cytokines
  JOURNAL   Am J Physiol Endocrinol Metab 287 (2), E331-E339 (2004)
   PUBMED   15100092
REFERENCE   5  (residues 1 to 2122)
  AUTHORS   Tran,H.T., Ulke,A., Morrice,N., Johannes,C.J. and Moorhead,G.B.
  TITLE     Proteomic characterization of protein phosphatase complexes of the
            mammalian nucleus
  JOURNAL   Mol Cell Proteomics 3 (3), 257-265 (2004)
   PUBMED   14724321
REFERENCE   6  (residues 1 to 2122)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Sep 12, 2012 this sequence version replaced
            XP_234416.6, XP_001057111.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.28290.1,
                                           SRR26643290.23580.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2122
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..2122
                     /product="YLP motif-containing protein 1"
                     /note="Nuclear protein ZAP3"
                     /calculated_mol_wt=239048
     Region          1059..>1208
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          1812..>1947
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     CDS             1..2122
                     /gene="Ylpm1"
                     /gene_synonym="RGD1564946; Zap; Zap3"
                     /coded_by="NM_001271258.1:147..6515"
                     /db_xref="GeneID:299199"
                     /db_xref="RGD:1564946"
ORIGIN      
        1 mypnwgrygg sshyppppvp pppppvalpe aspgpgysss tapaapsssg fmsfreqhla
       61 qlqqlqqmhq kqmqcvlqph hlpppplppp pvmpgggygd wqpppppmpp ppgpalsyqk
      121 qqqykhqmih hqrdgppglv pmelesppes ppvppgsymp psqsympppq pppsyyppss
      181 aqpylppaqp spsqsppsqs ylaptpsyss ssssqsylsh sqpylppsqa spsrssqgps
      241 kpqlppppps ipsgnkttiq qepletgakn knaeqkqaap epdpstmtpq eqqqywyrqh
      301 llslqqrtkv hlpghkkglv takdvpepik eeapvpatsq iaeplaaeep plpppneemp
      361 pplppeepqs edpeedarlk qlqaaaahwq qhqqhrvgfq yqgimqrhtq lqqilqqyqq
      421 viqhsphiqt msldvqlrhy emqqqqfqrl yqewerefql weeqlhsyph kdqleeyekq
      481 wkswqghmra tqtylqekvt sfqavknqym gnmampppfv pysqmppplp tmpppvlpps
      541 lpppvmppal pstipppgmp ppvmppslpt svpppgmpps lssavlppps lssagpppvl
      601 pppslsgapp vlplpplssa tpppgipppg vpqgmppqlt apvppasssq nsqvpekprq
      661 allptpvsfg stppspyhpp pqseqgnskp lnkvfsseqg lgesssalsq sviaakdtpv
      721 ksgglladpp kgsflegprg prfdgprrfe dlgsrcegpr pkgprfegnr pdgprpryes
      781 hpaegtkskw gtiprgpasq fyitpntsls prqsgpqwkg hkatvgqqhq qqpkqqpksq
      841 aeplsgnkep ladtssnqqk nlkiqsaafs isadvkdtka aqsnenlsns qqeppksqvs
      901 eapiepsnwn qnsqsmetem dkaqgvtqpv slankpvpsq spfpskvgsm eggaavaaaa
      961 lsaddfkplg vglshsenhq ekalpqpdsr enrlegnkgs sssyrgpgqn rvedsrdkgl
     1021 vnrgrgqtin rgpglikqed fhdkmlgrre dsrekinkge gsrdrvfvrp gssrdkipgg
     1081 lqdsqdsran srergpprra gsqergpprr agsrervppq ragsrergpp rgpgsrergl
     1141 grpdfghdrv pfrpepgdgg dkmypyhrde psraswnhge ergheefpld grnvpierer
     1201 lddwdrkryw recerdyqdd tldsygredr fsappsrphd gdrrgpwwdd werdqdmdeg
     1261 ygrevdrdld rdvdrirrpv diydrnvdne wdrdygrpld eqesqfrerd ipslpplppl
     1321 ppldryrddr wreernrehg ydrdfrdrge lrireyperg dtwrekrdyv pdrmdwerer
     1381 lsdrwypsda erhspmaehm psshhssemm gsdanldsdq glggvmvlsq rqheiilkaa
     1441 qelkmlreqk eqlqklkdfg sepqtadhlp ppdsrlqnts rpgmypppgs yrppppmgkp
     1501 pgsivrpsap parscvpmtr ppvpippppp pppppppppp vikpktssvk qerwdedsff
     1561 glwdtnddqg lnsefkrdta aipsapvlpp ppvhpsippp gpmpmgmppm skpppvqhtv
     1621 dyghgrdmpt nkveqipyge ritlrpdplp ersafdadha gqrdrydrdr drepyfdrqs
     1681 nmtdhrdfkr drethrdrdr vldyerdrfd rerrprddrn qsyrdkkdhs ssrrggfdrp
     1741 sydrksdrpp yegppmfgge rrtypeermp lpapslghqp ppvprvekkp esknvddilk
     1801 ppgresrper ivvimrglpg sgkthvakli rdkevefggp aprvlslddy fiaevekeek
     1861 dpdsgkkvkk kvmeyeyead meetyrtsmf ktfkktlddg ffpfiildai ndrvrhfdqf
     1921 wsaaktkgfe vylaemsadn qtcgkrnihg rklkeinkma ehweaaprhm mrldirsllq
     1981 daaieeveme dfdaniedqk eekkdaeeee selgyipksk wemdtseakl dkldglrtgt
     2041 krkrdweaia srmedylqlp ddyetrasep gkkrvrwadl eekkdadrkr aigfvvgqtd
     2101 wekitdesgh laeralnrtk yi
//
LOCUS       NP_001100655            2416 aa            linear   ROD 27-APR-2025
DEFINITION  nucleoprotein TPR [Rattus norvegicus].
ACCESSION   NP_001100655 XP_001070158 XP_006250034 XP_222745
VERSION     NP_001100655.2
DBSOURCE    REFSEQ: accession NM_001107185.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2416)
  AUTHORS   Liu,J., Xu,D., Wang,H., Zhang,Y., Chang,Y., Zhang,J., Wang,J.,
            Li,C., Liu,H., Zhao,M., Lin,C., Zhan,Q., Huang,C. and Qian,H.
  TITLE     The subcellular distribution and function of MTA1 in cancer
            differentiation
  JOURNAL   Oncotarget 5 (13), 5153-5164 (2014)
   PUBMED   24970816
REFERENCE   2  (residues 1 to 2416)
  AUTHORS   Kaczmarczyk,M.M., Miller,M.J. and Freund,G.G.
  TITLE     The health benefits of dietary fiber: beyond the usual suspects of
            type 2 diabetes mellitus, cardiovascular disease and colon cancer
  JOURNAL   Metabolism 61 (8), 1058-1066 (2012)
   PUBMED   22401879
  REMARK    Review article
REFERENCE   3  (residues 1 to 2416)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 2416)
  AUTHORS   Rajanala,K. and Nandicoori,V.K.
  TITLE     Localization of nucleoporin Tpr to the nuclear pore complex is
            essential for Tpr mediated regulation of the export of unspliced
            RNA
  JOURNAL   PLoS One 7 (1), e29921 (2012)
   PUBMED   22253824
REFERENCE   5  (residues 1 to 2416)
  AUTHORS   Coyle,J.H., Bor,Y.C., Rekosh,D. and Hammarskjold,M.L.
  TITLE     The Tpr protein regulates export of mRNAs with retained introns
            that traffic through the Nxf1 pathway
  JOURNAL   RNA 17 (7), 1344-1356 (2011)
   PUBMED   21613532
REFERENCE   6  (residues 1 to 2416)
  AUTHORS   Frosst,P., Guan,T., Subauste,C., Hahn,K. and Gerace,L.
  TITLE     Tpr is localized within the nuclear basket of the pore complex and
            has a role in nuclear protein export
  JOURNAL   J Cell Biol 156 (4), 617-630 (2002)
   PUBMED   11839768
REFERENCE   7  (residues 1 to 2416)
  AUTHORS   Hase,M.E., Kuznetsov,N.V. and Cordes,V.C.
  TITLE     Amino acid substitutions of coiled-coil protein Tpr abrogate
            anchorage to the nuclear pore complex but not parallel, in-register
            homodimerization
  JOURNAL   Mol Biol Cell 12 (8), 2433-2452 (2001)
   PUBMED   11514627
REFERENCE   8  (residues 1 to 2416)
  AUTHORS   Bangs,P., Burke,B., Powers,C., Craig,R., Purohit,A. and Doxsey,S.
  TITLE     Functional analysis of Tpr: identification of nuclear pore complex
            association and nuclear localization domains and a role in mRNA
            export
  JOURNAL   J Cell Biol 143 (7), 1801-1812 (1998)
   PUBMED   9864356
REFERENCE   9  (residues 1 to 2416)
  AUTHORS   Cordes,V.C., Hase,M.E. and Muller,L.
  TITLE     Molecular segments of protein Tpr that confer nuclear targeting and
            association with the nuclear pore complex
  JOURNAL   Exp Cell Res 245 (1), 43-56 (1998)
   PUBMED   9828100
REFERENCE   10 (residues 1 to 2416)
  AUTHORS   Cordes,V.C., Reidenbach,S., Rackwitz,H.R. and Franke,W.W.
  TITLE     Identification of protein p270/Tpr as a constitutive component of
            the nuclear pore complex-attached intranuclear filaments
  JOURNAL   J Cell Biol 136 (3), 515-529 (1997)
   PUBMED   9024684
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Oct 17, 2014 this sequence version replaced
            XP_006250034.1, NP_001100655.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2416
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..2416
                     /product="nucleoprotein TPR"
                     /note="translocated promoter region (to activated MET
                     oncogene); megator; NPC-associated intranuclear protein;
                     translocated promoter region protein"
                     /calculated_mol_wt=272644
     Region          103..940
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          829..1674
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1096..1222
                     /region_name="TPR_MLP1_2"
                     /note="TPR/MLP1/MLP2-like protein; pfam07926"
                     /db_xref="CDD:462316"
     Region          <1694..1880
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..2416
                     /gene="Tpr"
                     /coded_by="NM_001107185.1:138..7388"
                     /db_xref="GeneID:304862"
                     /db_xref="RGD:1310664"
ORIGIN      
        1 mtsrgfdgsr rgslrragar etaseaadga aqasglrasp csfaspsaaa attpadmaav
       61 lqqvlerpel nklpkstqnk lekflaeqqs eidclkgrhe kfkveseqqy feiekrlsqs
      121 qerlvnetre cqnlrlelek lnnqvkvlte knkeletaqd rnlgiqsqft rakeeleaek
      181 rdlirtnerl sqeveylted vkrlneklke snttkgelql kldelqasdv tvkyrekrle
      241 qekellhnqn swlntelktk tdellalgre kgneilelkc tlenkkeevl rleeqmnglk
      301 tsnehlqkhv edlltklkea keqqasmeek fhnelnahik lsnlyksaad dseaksnelt
      361 ravdelhkll keageankti qdhllqvees kdqmekemle kigklekele nandllsatk
      421 rkgailseee laamsptaaa vakivkpgmk ltelynayve tqdqlllekl enkrinkyld
      481 eivkeveaka pilkrqreey eraqkavasl sakleqamke iqrlqedtdk ankhssvler
      541 dnqrmeiqik dlsqqirvll meleeargnh virdeevssa dissssevis qhlvsyrnie
      601 elqqqnqrll falrelgetr ereeqettss kiaelqnkle nslteleqlr esrqhqmqlv
      661 dsivrqrdmy rillsqttgm aiplqassld dislvstpkr sstsqtvstp apepiieste
      721 tieakaalkq lqeifenykk ekmdseklqn eqleklqeqv tdlrsqntki stqldfaskr
      781 yemlqdnveg yrreitslqe rnqkltattq kqeqiintmt qdlrganekl avaevraenl
      841 kkekemlkls evrlsqqres llaeqrgqnl lltnlqtiqg ilersetetk qrlssqiekl
      901 eheishlkkk leneveqrht ltrnldvqll dtkrqldtei nlhlntkell knaqkdiatl
      961 kqhlnnmeaq lasqstqrtg kgqpgdrddv ddlksqlrqa eeqvndlker lktsasnveq
     1021 yramvtsled slnkekqvte evhknievrl kesaefqtql ekklmeveke kqelqddkrk
     1081 aiesmeqqlt elkktlssvq sevqealqra stalsneqqa rrdcqeqaki aveaqnkyer
     1141 elmlhaadve alqaakeqvs kmasvrqhle ettqkaesql leckasweer ervlkdevsk
     1201 svsrcedlek qnrllhdqie klsdkvvtsm kevvqsplni slneegksqe qileilrfir
     1261 rekeiaetrf evaqveslry rqrvellere lqelqdslna erekvqvtak tmaqheelmk
     1321 ktetmnvvme tnkmlreeke rleqnlqqmq akvrkleldi lplqeanael seksgmlqae
     1381 kklleedvkr wkarnqhlin qqkdpdteey rkllsekeih tkriqqlnee vgrlkaeiar
     1441 snasltnnqn liqslkedls kvrtekesiq kdldakiidi qekvktitqv kkigrryktq
     1501 feelkaqqka metstqssgd hqeqhisvqe mqelkdnlsq setktksleg qvenlqktls
     1561 eketearslq eqtaqlqsel srlrqelqdk ttkeeqlrqq mnekdektwk aitvarskia
     1621 hlsgvkdqlt keneelkqrn galdqqkdel dvrmtalksq yegrisrler elrehqerhl
     1681 eqrdepqept nkapeqqrqi tlkttpasge rgiastsdpp tanikptpvv stpskvtaaa
     1741 magnkstpra sirpmvtpat vtnptttpta tvmpttqves qeamqsegpv ehvpvfgsts
     1801 gsvrstspnv qpsisqpllt vqqqtqataf vqptqqshpq iepanqelsp nivevvqssp
     1861 verpststav fgtvsatpss slpkrareee edstieagdq vsddtvempl pkklktvtpv
     1921 gteeevmaee stdgeaetqt ynqdsqdsig egvtqgdytp medseetsqs lqidlgplqs
     1981 dqqttssqdg qgkgddvivi dsddedddee ndgehedyee dededddeed dtgmgdeged
     2041 snegtgsadg ndgyeaddae ggdgtdpgte teesmggaes nqraadsqns gegntsaaes
     2101 sfsqevareq qptsaserqt pqapqsprrp phplpprlti happqelgpp vqriqmtrrq
     2161 svgrglqltp giggmqqhff ddedrtvpst ptlvvphrtd gfaeaihspq vagvprfrfg
     2221 ppedmpqtss shsdlgqlas qgglgmyetp lflaheeesg grsvpttplq vaapvtvfte
     2281 sttsdaseha sqsvpmvtts tgtlsttnet pagddgdevf vetesegiss eagleidsqq
     2341 eeepvqasde sdlpstsqdp pssssvdtss sqpkpfrrvr lqttlrqgvr grqfnrqrgi
     2401 shamggrggi nrgnin
//
LOCUS       NP_001263412              92 aa            linear   ROD 27-APR-2025
DEFINITION  small integral membrane protein 12 [Rattus norvegicus].
ACCESSION   NP_001263412 XP_001064606 XP_002726672
VERSION     NP_001263412.1
DBSOURCE    REFSEQ: accession NM_001276483.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Feb 17, 2013 this sequence version replaced
            XP_001064606.2, XP_002726672.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20901.1,
                                           SRR26643299.24333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..92
                     /product="small integral membrane protein 12"
                     /calculated_mol_wt=10678
     Region          1..87
                     /region_name="UPF0767"
                     /note="UPF0767 family; pfam15990"
                     /db_xref="CDD:464960"
     Site            15..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ACP2.1)"
     CDS             1..92
                     /gene="Smim12"
                     /coded_by="NM_001276483.1:85..363"
                     /db_xref="GeneID:685634"
                     /db_xref="RGD:1591379"
ORIGIN      
        1 mwpvlwtvvr tyapyvtfpv afvvgavgyh lewfirgkdp qpveeeksil erredrklde
       61 mlgkdhtqvv slkdklefap kavlnrnrpe kn
//
LOCUS       NP_001171166             612 aa            linear   ROD 27-APR-2025
DEFINITION  actin-binding LIM protein 2 isoform a [Rattus norvegicus].
ACCESSION   NP_001171166
VERSION     NP_001171166.1
DBSOURCE    REFSEQ: accession NM_001177695.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Barrientos,T., Frank,D., Kuwahara,K., Bezprozvannaya,S.,
            Pipes,G.C., Bassel-Duby,R., Richardson,J.A., Katus,H.A., Olson,E.N.
            and Frey,N.
  TITLE     Two novel members of the ABLIM protein family, ABLIM-2 and -3,
            associate with STARS and directly bind F-actin
  JOURNAL   J Biol Chem 282 (11), 8393-8403 (2007)
   PUBMED   17194709
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Klimov,E., Rud'ko,O., Rakhmanaliev,E. and Sulimova,G.
  TITLE     Genomic organisation and tissue specific expression of ABLIM2 gene
            in human, mouse and rat
  JOURNAL   Biochim Biophys Acta 1730 (1), 1-9 (2005)
   PUBMED   16005990
  REMARK    GeneRIF: The highest expression of both isoforms was observed in
            rat brain and eye and in mouse embryos. ABLIM2 protein was
            necessary for the normal functioning of neurons.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ703892.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ703892.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..612
                     /product="actin-binding LIM protein 2 isoform a"
                     /note="abLIM-2; actin-binding LIM protein 2"
                     /calculated_mol_wt=67879
     Region          24..75
                     /region_name="LIM1_abLIM"
                     /note="The first LIM domain of actin binding LIM (abLIM)
                     proteins; cd09327"
                     /db_xref="CDD:188713"
     Site            order(24,27,44,47,50,53,71,74)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188713"
     Region          80..135
                     /region_name="LIM2_abLIM"
                     /note="The second LIM domain on actin binding LIM (abLIM)
                     proteins; cd09328"
                     /db_xref="CDD:188714"
     Site            order(83,86,103,106,109,112,131,134)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188714"
     Region          153..204
                     /region_name="LIM3_abLIM"
                     /note="The third LIM domain of actin binding LIM (abLIM)
                     proteins; cd09329"
                     /db_xref="CDD:188715"
     Site            order(153,156,174,177,180,183,200,203)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188715"
     Region          212..267
                     /region_name="LIM4_abLIM"
                     /note="The fourth LIM domain of actin binding LIM (abLIM)
                     proteins; cd09330"
                     /db_xref="CDD:188716"
     Site            order(212,215,232,235,238,241,260,263)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188716"
     Region          269..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC51.1)"
     Region          276..562
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BL65; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Region          341..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BL65; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Region          471..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BL65; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     Region          577..612
                     /region_name="VHP"
                     /note="Villin headpiece domain; pfam02209"
                     /db_xref="CDD:460493"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6KC51.1)"
     CDS             1..612
                     /gene="Ablim2"
                     /coded_by="NM_001177695.1:159..1997"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:360958"
                     /db_xref="RGD:1303094"
ORIGIN      
        1 msavsqpqaa haplekpast ailcntcgnv ckgevlrvqn khfhircfvc kacgcdlaeg
       61 gffvrqgehi ctrdyqrlyg trcfscdcfi egevvsalgk tyhpdcfvca vcrlpfppgd
      121 rvtfngkdcm cqkcspptlv gnsahvaqgl rscggcglei kngqalvald khwhlgcfkc
      181 ktcgkllnae yiskdglpyc eadyhtkfgi rcdgcekyit grvleagekh yhpscalcvr
      241 cgqmfsegee mylqgssiwh pacrqaarte dksketrtss esivsvpass tsgspsrviy
      301 aklgdeildy rdlaalpknk aiynidrpdm isyspyishs avgdrqsyge gdqddrsykq
      361 crtsspssag svslghytpt srspqhysrp gsesgrstps lsvhsdsrpp sstyqqaprh
      421 fhvpdtgvkd niyrkppiyk qhaarrldve dssfdqdsrk kttwlllkgd adtrtnspdl
      481 dsqslslssg adqeplqrmp gdslysrfpy skpdtlpgpr kdgldlrnan lapcgadpda
      541 swgtreykiy pydslivtnr irvklpkdvd rtrlerhlsp eefqevfgms ieefdrlalw
      601 krndlkkkal lf
//
LOCUS       NP_001264191             250 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, slow skeletal muscle isoform 4 [Rattus norvegicus].
ACCESSION   NP_001264191
VERSION     NP_001264191.1
DBSOURCE    REFSEQ: accession NM_001277262.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Tsika,R.W., Schramm,C., Simmer,G., Fitzsimons,D.P., Moss,R.L. and
            Ji,J.
  TITLE     Overexpression of TEAD-1 in transgenic mouse striated muscles
            produces a slower skeletal muscle contractile phenotype
  JOURNAL   J Biol Chem 283 (52), 36154-36167 (2008)
   PUBMED   18978355
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Pinto,J.R., Parvatiyar,M.S., Jones,M.A., Liang,J. and Potter,J.D.
  TITLE     A troponin T mutation that causes infantile restrictive
            cardiomyopathy increases Ca2+ sensitivity of force development and
            impairs the inhibitory properties of troponin
  JOURNAL   J Biol Chem 283 (4), 2156-2166 (2008)
   PUBMED   18032382
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Kischel,P., Bastide,B., Muller,M., Dubail,F., Offredi,F., Jin,J.P.,
            Mounier,Y. and Martial,J.
  TITLE     Expression and functional properties of four slow skeletal troponin
            T isoforms in rat muscles
  JOURNAL   Am J Physiol Cell Physiol 289 (2), C437-C443 (2005)
   PUBMED   15788488
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Wang,X., Huang,Q.Q., Breckenridge,M.T., Chen,A., Crawford,T.O.,
            Morton,D.H. and Jin,J.P.
  TITLE     Cellular fate of truncated slow skeletal muscle troponin T produced
            by Glu180 nonsense mutation in amish nemaline myopathy
  JOURNAL   J Biol Chem 280 (14), 13241-13249 (2005)
   PUBMED   15665378
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Johnston,J.J., Kelley,R.I., Crawford,T.O., Morton,D.H.,
            Agarwala,R., Koch,T., Schaffer,A.A., Francomano,C.A. and
            Biesecker,L.G.
  TITLE     A novel nemaline myopathy in the Amish caused by a mutation in
            troponin T1
  JOURNAL   Am J Hum Genet 67 (4), 814-821 (2000)
   PUBMED   10952871
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Gahlmann,R., Troutt,A.B., Wade,R.P., Gunning,P. and Kedes,L.
  TITLE     Alternative splicing generates variants in important functional
            domains of human slow skeletal troponin T
  JOURNAL   J Biol Chem 262 (33), 16122-16126 (1987)
   PUBMED   2824479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and AY334081.1.
            
            Transcript Variant: This variant (4) lacks an exon in the coding
            region, compared to variant 1. The encoded isoform (4) is shorter,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY334081.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760386, SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..250
                     /product="troponin T, slow skeletal muscle isoform 4"
                     /note="troponin T, slow skeletal muscle; slow skeletal
                     muscle troponin T; troponin T1, skeletal, slow; troponin T
                     type 1 (skeletal, slow)"
                     /calculated_mol_wt=29879
     Region          57..193
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Region          168..>226
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..250
                     /gene="Tnnt1"
                     /gene_synonym="Fang2; sTnT; tnTs"
                     /coded_by="NM_001277262.2:57..809"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:171409"
                     /db_xref="RGD:621852"
ORIGIN      
        1 msdteeqeye eeqaedeeav eeeeeerpkp srpvvpplip pkipegervd fddihrkrme
       61 kdllelqtli dvhfeqrkke eeelialkdr ierrraerae qqrfrteker erqaklaeek
      121 mrkeeeeakk raeddakkkk vlsnmgahfg gylvkaeqkr gkrqtgremk lrilserkkp
      181 lnidymgedq lrekaqelse wihqlesekf dlmeklkqqk yeinvlynri shaqkfrkga
      241 gkgrvggrwk
//
LOCUS       NP_001300744            1517 aa            linear   ROD 27-APR-2025
DEFINITION  neurite extension and migration factor [Rattus norvegicus].
ACCESSION   NP_001300744
VERSION     NP_001300744.1
DBSOURCE    REFSEQ: accession NM_001313815.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1517)
  AUTHORS   Gilbert,J. and Man,H.Y.
  TITLE     The X-Linked Autism Protein KIAA2022/KIDLIA Regulates Neurite
            Outgrowth via N-Cadherin and delta-Catenin Signaling
  JOURNAL   eNeuro 3 (5) (2016)
   PUBMED   27822498
  REMARK    GeneRIF: Knockdown of KIAA2022/KIDLIA leads to altered neuron
            migration and a reduction in dendritic growth and disorganized
            apical dendrite projections in layer II/III cortical neurons. In
            cultured neurons loss of KIDLIA expression also leads to
            suppression of dendritic growth and branching. KIDLIA suppression
            leads to an increase in cell-surface N-cadherin and an elevated
            association of N-cadherin with delta-catenin.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1517)
  AUTHORS   Magome,T., Hattori,T., Taniguchi,M., Ishikawa,T., Miyata,S.,
            Yamada,K., Takamura,H., Matsuzaki,S., Ito,A., Tohyama,M. and
            Katayama,T.
  TITLE     XLMR protein related to neurite extension (Xpn/KIAA2022) regulates
            cell-cell and cell-matrix adhesion and migration
  JOURNAL   Neurochem Int 63 (6), 561-569 (2013)
   PUBMED   24071057
REFERENCE   3  (residues 1 to 1517)
  AUTHORS   Van Maldergem,L., Hou,Q., Kalscheuer,V.M., Rio,M., Doco-Fenzy,M.,
            Medeira,A., de Brouwer,A.P., Cabrol,C., Haas,S.A., Cacciagli,P.,
            Moutton,S., Landais,E., Motte,J., Colleaux,L., Bonnet,C.,
            Villard,L., Dupont,J. and Man,H.Y.
  TITLE     Loss of function of KIAA2022 causes mild to severe intellectual
            disability with an autism spectrum disorder and impairs neurite
            outgrowth
  JOURNAL   Hum Mol Genet 22 (16), 3306-3314 (2013)
   PUBMED   23615299
  REMARK    GeneRIF: Result showed that siRNA-mediated KIAA2022 knockdown
            resulted in marked impairment in neurite outgrowth including both
            the dendrites and the axons, suggesting a major role for KIAA2022
            in neuron development and brain function.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data to make the sequence consistent with the reference genome
            assembly. The genomic coordinates used for the transcript record
            were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840117,
                              SAMN12840130 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1517
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..1517
                     /product="neurite extension and migration factor"
                     /note="XLMR protein related to neurite extension"
                     /calculated_mol_wt=166532
     Region          291..691
                     /region_name="DUF4683"
                     /note="Domain of unknown function (DUF4683); pfam15735"
                     /db_xref="CDD:464832"
     Region          381..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          505..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          644..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          732..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          1065..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          1161..1228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     Region          1372..1422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZGX1.1)"
     CDS             1..1517
                     /gene="Nexmif"
                     /gene_synonym="KIAA2022; KIDLIA; RGD1561931; Xpn"
                     /coded_by="NM_001313815.1:104..4657"
                     /db_xref="GeneID:302396"
                     /db_xref="RGD:1561931"
ORIGIN      
        1 mdnqqdkvia asangennli ngvkendsee qdvamksfaa leastpiqpi pvvqkespmf
       61 prgllplpsk kpcmqsppsp lglieapdhs atgasvnais ltsgvakgln twslpnecek
      121 apfaimepag isalngdclm qpsrtclgcf meskeavdpe pgislkvgdl nrdyetcavs
      181 digiqcinag enlkygeqll sdqllgfplh ksragdrres ekpdidledp tqksyyeall
      241 ldkcnteeal lansnqdwgy fetfiseski elldlcskne lsvnlfseed venymfddde
      301 stlgsdvcsl kiryesfqdn vrdkttllmq edaqfnffps vfttcpkres ksgvlkqssd
      361 lsqfkvpdvs iiwgdedknl dkkkgkeevh edksiekkde kdngekpaln nkpcsgleve
      421 qfknlkpdhl tnsletsgnf sddssfievs ydamgeikdc srymardtns gssssqqnyg
      481 lrakrkvrys edylydvdsl egekvnerke wppggskeed ddewcpkkrr kvtrkeppvi
      541 ikyiiinrfk geknmlvklg kvdasettvn lsesqlskya klsplkgfwq kkkkqkngnt
      601 dsvktpfcqk qsfepgsfev sflpparkrk sklgnrhriq riqsmeasas skqvsfgsdq
      661 kqasnrkeeg glkgtpksal laapssangs hlrgligpds akvkaqdtef kgperkvlnk
      721 ikfksearlk skkiktgqen kpvvqmspvs edpsskanlk nevtpgtsns shmsefhetk
      781 vvknstflpt tcssemplss anvatnipvi pggylqtlld asdlsnntsi syftnhsaeq
      841 neaslsqtek afaplqsaqd cvlssssdsq lqqssqnfkm easnygslwp dkdtsgsqef
      901 mtevsgeiat sqssefeatq vvsmennlta ityspvclns ggsgcnkvly asvqdshlap
      961 ddsyqlchfn ngeicfpfqq gpisteddgq lfsfdsmtpl svssssycpl slkscekdgd
     1021 ddinddflah cspklviqqs ideiaplkes tdlldisnft pdkfrhssls emsppdtpsl
     1081 spqstrcesi ktlgtmkgfq egvpgslssm ekikwdcstl sqqvqaddgf tlnnhqfqfh
     1141 mfndedsvgl lqknpclstf depagqisan nkvsksrkkt spgksgavsq sssqkntrkk
     1201 spkasnkgve kppsktsrqv pksakkgkyv aavngekmqi gighsggqpn stssngktlt
     1261 eciqhggpva pmkipsqkgl sgdwalgkes rpgwndmsvv tntnnllddd qrefqepsyi
     1321 lsniasgmad vqrfmmasme plwepmehqg esntfyspds nslklktlki lagtpqeskk
     1381 kinngssgat knhrsikavs kssgkaavgd pghadvsgss edsrsaffdk kysnmntlgn
     1441 ngpthkklyr hksssktlrd ekykgkrver eqihkdeagt tcfeklrgss ynllkaetaf
     1501 gvlpvfeeet hifqkdi
//
LOCUS       NP_741993                292 aa            linear   ROD 27-APR-2025
DEFINITION  peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]
            [Rattus norvegicus].
ACCESSION   NP_741993
VERSION     NP_741993.1
DBSOURCE    REFSEQ: accession NM_171996.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Amery,L., Mannaerts,G.P., Subramani,S., Van Veldhoven,P.P. and
            Fransen,M.
  TITLE     Identification of a novel human peroxisomal 2,4-dienoyl-CoA
            reductase related protein using the M13 phage protein VI phage
            display technology
  JOURNAL   Comb Chem High Throughput Screen 4 (7), 545-552 (2001)
   PUBMED   11669066
REFERENCE   4  (residues 1 to 292)
  AUTHORS   De Nys,K., Meyhi,E., Mannaerts,G.P., Fransen,M. and Van
            Veldhoven,P.P.
  TITLE     Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase
  JOURNAL   Biochim Biophys Acta 1533 (1), 66-72 (2001)
   PUBMED   11514237
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Das,A.K., Uhler,M.D. and Hajra,A.K.
  TITLE     Molecular cloning and expression of mammalian peroxisomal
            trans-2-enoyl-coenzyme A reductase cDNAs
  JOURNAL   J Biol Chem 275 (32), 24333-24340 (2000)
   PUBMED   10811639
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Fransen,M., Van Veldhoven,P.P. and Subramani,S.
  TITLE     Identification of peroxisomal proteins by using M13 phage protein
            VI phage display: molecular evidence that mammalian peroxisomes
            contain a 2,4-dienoyl-CoA reductase
  JOURNAL   Biochem J 340 (Pt 2) (Pt 2), 561-568 (1999)
   PUBMED   10333503
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070959.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070959.1, AF044574.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..292
                     /product="peroxisomal 2,4-dienoyl-CoA reductase
                     [(3E)-enoyl-CoA-producing]"
                     /EC_number="1.3.1.124"
                     /note="putative peroxisomal 2,4-dienoyl-CoA reductase;
                     2-4-dienoyl-Coenzyme A reductase 2, peroxisomal; DCR-AKL;
                     pVI-AKL; putative peroxisomal 24-dienoyl-CoA reductase;
                     2,4-dienoyl CoA reductase 2, peroxisomal"
                     /calculated_mol_wt=31161
     Region          26..273
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(35,38..40,59..61,85..88,113..115,136,163..165,182,
                     208..211,213)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(60,88,115..118,126,128..129,132,165,167,178,210)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(90,121..123,125..127,130..131,134,138..139,142..143,
                     146,150,153,157,167,171..174,176,179..180,183..184,
                     187..188,190..197,199,210,234..236,238..240,244,247..248,
                     251,256,258..263,265..273)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(117,167,178,182)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(121..123,125,130..131,134,139,142..143,171..174,176,
                     179..180,183..184,187..188,191,194..195)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            151
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUI1; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2M4.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUI1; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2M4.1)"
     Region          290..292
                     /region_name="Microbody targeting signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2M4.1)"
     Site            291
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NUI1; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2M4.1)"
     CDS             1..292
                     /gene="Decr2"
                     /gene_synonym="Dcrakl;
                     putativeperoxisomal24-dienoyl-CoAreductase"
                     /coded_by="NM_171996.3:91..969"
                     /db_xref="GeneID:64461"
                     /db_xref="RGD:71002"
ORIGIN      
        1 mtqqppdvee ddclseyhhl fcpdllqdkv afitgggsgi gfriaeifmr hgchtvivsr
       61 slprvseaak klvaatgkrc lplsmdvrvp pavmaavdqa lkefgkidil incaagnflc
      121 pasalsfnaf ktvvdidtlg tfnvsrvlye kffrdhggvi vnitatlsmr gqvlqlhaga
      181 akaavdamtr hlavewgpqn irvnslapga isgteglrrl ggpkasskfk ylsspiprlg
      241 tkteiahsvl ylasplasyv sgivlvvdgg swmtlpndig rllefesssa kl
//
LOCUS       NP_001263637            1110 aa            linear   ROD 27-APR-2025
DEFINITION  sterol regulatory element-binding protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001263637
VERSION     NP_001263637.1
DBSOURCE    REFSEQ: accession NM_001276708.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1110)
  AUTHORS   Li,H., Liu,Y., Meng,F., Chen,J. and Han,X.
  TITLE     Adrenarche-accompanied rise of adrenal sex steroid precursors
            prevents NAFLD in Young Female rats by converting into active
            androgens and inactivating hepatic Srebf1 signaling
  JOURNAL   BMC Genomics 25 (1), 190 (2024)
   PUBMED   38369486
  REMARK    GeneRIF: Adrenarche-accompanied rise of adrenal sex steroid
            precursors prevents NAFLD in Young Female rats by converting into
            active androgens and inactivating hepatic Srebf1 signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1110)
  AUTHORS   Ma,P., Huang,J., Chen,B., Huang,M., Xiong,L., Chen,J., Huang,S. and
            Liu,Y.
  TITLE     Lanosterol Synthase Prevents EMT During Lens Epithelial Fibrosis
            Via Regulating SREBP1
  JOURNAL   Invest Ophthalmol Vis Sci 64 (15), 12 (2023)
   PUBMED   38079167
  REMARK    GeneRIF: Lanosterol Synthase Prevents EMT During Lens Epithelial
            Fibrosis Via Regulating SREBP1.
REFERENCE   3  (residues 1 to 1110)
  AUTHORS   Bian,C., Zhang,H., Gao,J., Wang,Y., Li,J., Guo,D., Wang,W.,
            Song,Y., Weng,Y. and Ren,H.
  TITLE     SIRT6 regulates SREBP1c-induced glucolipid metabolism in liver and
            pancreas via the AMPKalpha-mTORC1 pathway
  JOURNAL   Lab Invest 102 (5), 474-484 (2022)
   PUBMED   34923569
  REMARK    GeneRIF: SIRT6 regulates SREBP1c-induced glucolipid metabolism in
            liver and pancreas via the AMPKalpha-mTORC1 pathway.
REFERENCE   4  (residues 1 to 1110)
  AUTHORS   Yalcin,M. and Kacar,M.
  TITLE     Investigation of the hepatic mTOR/S6K1/SREBP1 signalling pathway in
            rats at different ages: from neonates to adults
  JOURNAL   Mol Biol Rep 48 (11), 7415-7422 (2021)
   PUBMED   34655015
  REMARK    GeneRIF: Investigation of the hepatic mTOR/S6K1/SREBP1 signalling
            pathway in rats at different ages: from neonates to adults.
REFERENCE   5  (residues 1 to 1110)
  AUTHORS   Kilby,E.L., Kelly,D.M. and Jones,T.H.
  TITLE     Testosterone stimulates cholesterol clearance from human
            macrophages by activating LXRalpha
  JOURNAL   Life Sci 269, 119040 (2021)
   PUBMED   33453241
REFERENCE   6  (residues 1 to 1110)
  AUTHORS   Boizard,M., Le Liepvre,X., Lemarchand,P., Foufelle,F., Ferre,P. and
            Dugail,I.
  TITLE     Obesity-related overexpression of fatty-acid synthase gene in
            adipose tissue involves sterol regulatory element-binding protein
            transcription factors
  JOURNAL   J Biol Chem 273 (44), 29164-29171 (1998)
   PUBMED   9786926
REFERENCE   7  (residues 1 to 1110)
  AUTHORS   Shimano,H., Shimomura,I., Hammer,R.E., Herz,J., Goldstein,J.L.,
            Brown,M.S. and Horton,J.D.
  TITLE     Elevated levels of SREBP-2 and cholesterol synthesis in livers of
            mice homozygous for a targeted disruption of the SREBP-1 gene
  JOURNAL   J Clin Invest 100 (8), 2115-2124 (1997)
   PUBMED   9329978
REFERENCE   8  (residues 1 to 1110)
  AUTHORS   Sawada,Y. and Noda,M.
  TITLE     An adipogenic basic helix-loop-helix-leucine zipper type
            transcription factor (ADD1) mRNA is expressed and regulated by
            retinoic acid in osteoblastic cells
  JOURNAL   Mol Endocrinol 10 (10), 1238-1248 (1996)
   PUBMED   9121491
REFERENCE   9  (residues 1 to 1110)
  AUTHORS   Kim,J.B., Spotts,G.D., Halvorsen,Y.D., Shih,H.M., Ellenberger,T.,
            Towle,H.C. and Spiegelman,B.M.
  TITLE     Dual DNA binding specificity of ADD1/SREBP1 controlled by a single
            amino acid in the basic helix-loop-helix domain
  JOURNAL   Mol Cell Biol 15 (5), 2582-2588 (1995)
   PUBMED   7739539
REFERENCE   10 (residues 1 to 1110)
  AUTHORS   Tontonoz,P., Kim,J.B., Graves,R.A. and Spiegelman,B.M.
  TITLE     ADD1: a novel helix-loop-helix transcription factor associated with
            adipocyte determination and differentiation
  JOURNAL   Mol Cell Biol 13 (8), 4753-4759 (1993)
   PUBMED   8336713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Transcript Variant: This variant (2) uses an alternate 5' exon
            structure, and initiates translation at an alternate start codon,
            compared to variant 1. The encoded isoform (2) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.24411.1,
                                           SRR26643286.30500.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1110
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..1110
                     /product="sterol regulatory element-binding protein 1
                     isoform 2"
                     /note="sterol regulatory element-binding protein 1;
                     adipocyte determination- and differentiation-dependent
                     factor 1"
                     /calculated_mol_wt=117896
     Region          34..>206
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          289..360
                     /region_name="bHLHzip_SREBP1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in sterol regulatory element-binding protein 1
                     (SREBP1) and similar proteins; cd18921"
                     /db_xref="CDD:381491"
     Site            order(289,295,297..299,301..302,304..306,310,328..329)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381491"
     Site            order(305,308..309,312..313,315..316,319,329..330,
                     333..334,337,339..341,343..344,346..347,350..351,353..354,
                     357..358)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381491"
     Region          <538..1047
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     CDS             1..1110
                     /gene="Srebf1"
                     /gene_synonym="ADD-1; ADD1; SREBP-1; SREBP-1c; Srebp1"
                     /coded_by="NM_001276708.1:40..3372"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:78968"
                     /db_xref="RGD:69423"
ORIGIN      
        1 mdctfedmlq linnqdsdfp glfdapyagg etgdtgpssp gasspesfss paslgsslea
       61 flggpkvtpa plspppsapt avkmypsvpp fspgpgikee pvpltilqpp apqpspgtll
      121 ppsfppppvq lspapvlgys slpsgfsgtl pgntqqtpss lplgstpgis ptplhtqvqs
      181 saaqqpppas aaprmstvas qiqqvpvvlq phfikadsll ltavktdtga tmktagintl
      241 apgtavqagp lqtlvsggti latvplvvdt dklpihrlaa ggkalgsaqs rgekrtahna
      301 iekryrssin dkivelkdlv vgteaklnks avlrkaidyi rflqhsnqkl kqenltlrsa
      361 hkskslkdlv sacgsgggtd vsmegmkpev vetltpppsd agspsqsspl slgsrgsssg
      421 gsdsepdspa fednqvkaqr lpshsrgmld rsrlalcvlv flcltcnpla slfgwgiltp
      481 sdasgvhrss grsmleaesr dgsnwtqwll pplvwlangl lvlaclallf vygepvtrph
      541 sgpavhfwrh rkqadldlar gdfaqaaqql wlalqalgrp lptsnldlac sllwnlvrhl
      601 lqrlwvgrwl agqagglqrd yrlrkdaras ardaavvyhk lhqlhamgky tgghlvasnl
      661 alsalnlaec agdaismatl aeiyvaaalr vktslpralh fltrfflssa rqaclaqsga
      721 vplamqwlch pvghrffvdg dwavhgapqe slysvagnpv dplaqvtrlf cehlleraln
      781 ciaqpspgaa dgdrefsdal gylqllnscs davgapacsf svsssmattt gtdpvakwwa
      841 sltavvihwl rrdeeaaerl yplvehipqv lqeterplpr aalysfkaar alldhrkves
      901 spaslaicek asgylrdsla ststassidk amqlllcdll lvartslwrr qqsaasaqga
      961 hgtsngpqas alelrgfqhd lsslrrlaqs frpamrrvfl heatarlmag asparthqll
     1021 drslrrrags sgkggaaael eprptwreht ealllascyl ppaflsapgq rvsmlaeaar
     1081 tveklgdhrl lldcqqmllr lgggttvtss
//
LOCUS       NP_001020302             285 aa            linear   ROD 27-APR-2025
DEFINITION  sulfotransferase 2A2 [Rattus norvegicus].
ACCESSION   NP_001020302 XP_341792
VERSION     NP_001020302.1
DBSOURCE    REFSEQ: accession NM_001025131.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Watabe,T., Ogura,K., Satsukawa,M., Okuda,H. and Hiratsuka,A.
  TITLE     Molecular cloning and functions of rat liver hydroxysteroid
            sulfotransferases catalysing covalent binding of carcinogenic
            polycyclic arylmethanols to DNA
  JOURNAL   Chem Biol Interact 92 (1-3), 87-105 (1994)
   PUBMED   8033273
  REMARK    Review article
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Song,C.S., Kim,J.M., Roy,A.K. and Chatterjee,B.
  TITLE     Structure and regulation of the senescence marker protein 2 gene
            promoter
  JOURNAL   Biochemistry 29 (2), 542-551 (1990)
   PUBMED   2302387
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D14989.1.
            
            On Jul 1, 2005 this sequence version replaced XP_341792.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D14989.1, FQ209413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..285
                     /product="sulfotransferase 2A2"
                     /EC_number="2.8.2.2"
                     /note="alcohol sulfotransferase; hydroxysteroid
                     sulfotransferase; ST; ST-60; alcohol
                     sulfotransferase-like; Probable alcohol sulfotransferase;
                     Androgen-repressible liver protein; Dehydroepiandrosterone
                     sulfotransferase; Senescence marker protein 2"
                     /calculated_mol_wt=33400
     Region          34..278
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     CDS             1..285
                     /gene="Sult2a2"
                     /gene_synonym="DST; SMP-2; ST2A2"
                     /coded_by="NM_001025131.2:30..887"
                     /db_xref="GeneID:361510"
                     /db_xref="RGD:1306542"
ORIGIN      
        1 mmsdytwfeg ipfpafwfsk eilensckkf vvkeddliil typksgtnwl ieivcliqtk
       61 gdpkwiqsmp iwdrspwiet gsgydkltkm egprlmtshl pmhlfskslf sskakviyli
      121 rnprdvlvsa yffwskiale kkpdslgtyv ewflkgnvay gswfehirgw lsmrewdnfl
      181 vlyyedmkkd tmgsikkicd flgkklepde lnlvlkyssf qvvkennmsn yslmekelil
      241 tgftfmrkgt tndwknhftv aqaeafdkvf qekmagfppg mfpwe
//
LOCUS       NP_001258031             113 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 5 [Rattus norvegicus].
ACCESSION   NP_001258031
VERSION     NP_001258031.1
DBSOURCE    REFSEQ: accession NM_001271102.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 113)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 113)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 113)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 113)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Transcript Variant: This variant (5) differs in 5' UTR and 5'
            coding region, compared to variant 3. This results in a protein
            (isoform 5) that is shorter and has a distinct N-terminus compared
            to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213544.1, FQ213052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..113
                     /product="cAMP-responsive element modulator isoform 5"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=12608
     Region          57..111
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          58..110
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(58,62,64..66,68..70,72..73,75..77)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(76,79,83..84,86..87,90..91,93..94,97,100..101,
                     104..105,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..113
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271102.1:46..387"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mqkpnmavtg detaatgdmp tyqiraptta lpqgvvmaas pgslhspqql aeeatrkrel
       61 rlmknreaar ecrrkkkeyv kclenrvavl enqnktliee lkalkdlych kae
//
LOCUS       NP_598222                385 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-13 receptor subunit alpha-2 precursor [Rattus
            norvegicus].
ACCESSION   NP_598222 XP_346868
VERSION     NP_598222.2
DBSOURCE    REFSEQ: accession NM_133538.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Li,L., Wei,K., Ding,Y., Ahati,P., Xu,H., Fang,H. and Wang,H.
  TITLE     M2a Macrophage-Secreted CHI3L1 Promotes Extracellular Matrix
            Metabolic Imbalances via Activation of IL-13Ralpha2/MAPK Pathway in
            Rat Intervertebral Disc Degeneration
  JOURNAL   Front Immunol 12, 666361 (2021)
   PUBMED   34168643
  REMARK    GeneRIF: M2a Macrophage-Secreted CHI3L1 Promotes Extracellular
            Matrix Metabolic Imbalances via Activation of IL-13Ralpha2/MAPK
            Pathway in Rat Intervertebral Disc Degeneration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hussein,Y.M., Ahmad,A.S., Ibrahem,M.M., Elsherbeny,H.M.,
            Shalaby,S.M., El-Shal,A.S. and Sabbah,N.A.
  TITLE     Interleukin 13 receptors as biochemical markers in atopic patients
  JOURNAL   J Investig Allergol Clin Immunol 21 (2), 101-107 (2011)
   PUBMED   21462799
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Sivaprasad,U., Warrier,M.R., Gibson,A.M., Chen,W., Tabata,Y.,
            Bass,S.A., Rothenberg,M.E. and Khurana Hershey,G.K.
  TITLE     IL-13Ralpha2 has a protective role in a mouse model of cutaneous
            inflammation
  JOURNAL   J Immunol 185 (11), 6802-6808 (2010)
   PUBMED   20971924
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Hecker,M., Zaslona,Z., Kwapiszewska,G., Niess,G., Zakrzewicz,A.,
            Hergenreider,E., Wilhelm,J., Marsh,L.M., Sedding,D., Klepetko,W.,
            Lohmeyer,J., Dimmeler,S., Seeger,W., Weissmann,N., Schermuly,R.T.,
            Kneidinger,N., Eickelberg,O. and Morty,R.E.
  TITLE     Dysregulation of the IL-13 receptor system: a novel pathomechanism
            in pulmonary arterial hypertension
  JOURNAL   Am J Respir Crit Care Med 182 (6), 805-818 (2010)
   PUBMED   20522789
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Chiba,Y., Onoda,S., Todoroki,M., Nishida,Y. and Misawa,M.
  TITLE     Upregulation of interleukin-13 receptor chains in bronchial smooth
            muscle tissues of mouse experimental asthma
  JOURNAL   J Smooth Muscle Res 46 (1), 49-55 (2010)
   PUBMED   20383033
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Fish,S.C., Donaldson,D.D., Goldman,S.J., Williams,C.M. and
            Kasaian,M.T.
  TITLE     IgE generation and mast cell effector function in mice deficient in
            IL-4 and IL-13
  JOURNAL   J Immunol 174 (12), 7716-7724 (2005)
   PUBMED   15944273
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Jakubzick,C., Choi,E.S., Carpenter,K.J., Kunkel,S.L., Evanoff,H.,
            Martinez,F.J., Flaherty,K.R., Toews,G.B., Colby,T.V., Travis,W.D.,
            Joshi,B.H., Puri,R.K. and Hogaboam,C.M.
  TITLE     Human pulmonary fibroblasts exhibit altered interleukin-4 and
            interleukin-13 receptor subunit expression in idiopathic
            interstitial pneumonia
  JOURNAL   Am J Pathol 164 (6), 1989-2001 (2004)
   PUBMED   15161635
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Wu,A.H. and Low,W.C.
  TITLE     Molecular cloning of the rat IL-13 alpha 2 receptor cDNA and its
            expression in rat tissues
  JOURNAL   J Neurooncol 59 (2), 99-105 (2002)
   PUBMED   12241113
  REMARK    GeneRIF: gene sequence and tissue distribution of IL-13Ralpha2 in
            the rat
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Kawakami,K., Kawakami,M., Snoy,P.J., Husain,S.R. and Puri,R.K.
  TITLE     In vivo overexpression of IL-13 receptor alpha2 chain inhibits
            tumorigenicity of human breast and pancreatic tumors in
            immunodeficient mice
  JOURNAL   J Exp Med 194 (12), 1743-1754 (2001)
   PUBMED   11748276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Feb 16, 2013 this sequence version replaced NP_598222.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF448818.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq34"
     Protein         1..385
                     /product="interleukin-13 receptor subunit alpha-2
                     precursor"
                     /note="IL-13R subunit alpha-2; IL-13 receptor subunit
                     alpha-2; interleukin 13 receptor, alpha 2"
                     /calculated_mol_wt=42142
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2512
     mat_peptide     24..385
                     /product="Interleukin-13 receptor subunit alpha-2.
                     /id=PRO_0000378453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK6.1)"
                     /calculated_mol_wt=42142
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK6.1)"
     Region          138..231
                     /region_name="IL6Ra-bind"
                     /note="Interleukin-6 receptor alpha chain, binding;
                     pfam09240"
                     /db_xref="CDD:401252"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK6.1)"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK6.1)"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8VHK6.1)"
     Region          318..322
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK6.1)"
     Site            337..357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHK6.1)"
     CDS             1..385
                     /gene="Il13ra2"
                     /gene_synonym="IL-13R-alpha-2"
                     /coded_by="NM_133538.2:617..1774"
                     /db_xref="GeneID:171060"
                     /db_xref="RGD:620838"
ORIGIN      
        1 malmavntrc lclfllctit ghsleikvnp pqdfeildpg llgylylqwk ppvvmdnfke
       61 ckleyelkyr nvdsdswkti itrnliykdg fdlnkgiegk irthlsehct ngsevqspwt
      121 easygiadeg slgtkiqdmk ciyynwqylv cswkpgktvh sdtnytmffw yegldhalqc
      181 adylqdnekn vgcklsnlds sdykdffirv ngssklepir ssymvfqlqn ivkplppefl
      241 hisvensidi rmkwstpggp ippscytyei vvreddiswe satdkndmkl krranesedl
      301 cffvrckini ycaddgiwse wseeecwegy tgpdskiifi vpvclffifl llllclivek
      361 edpeptlslh vdlnkemyay eetlc
//
LOCUS       NP_001029072             293 aa            linear   ROD 27-APR-2025
DEFINITION  neugrin precursor [Rattus norvegicus].
ACCESSION   NP_001029072 XP_218821
VERSION     NP_001029072.2
DBSOURCE    REFSEQ: accession NM_001033900.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Arroyo,J.D., Jourdain,A.A., Calvo,S.E., Ballarano,C.A.,
            Doench,J.G., Root,D.E. and Mootha,V.K.
  TITLE     A Genome-wide CRISPR Death Screen Identifies Genes Essential for
            Oxidative Phosphorylation
  JOURNAL   Cell Metab 24 (6), 875-885 (2016)
   PUBMED   27667664
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Ishigaki,S., Niwa,J., Yoshihara,T., Mitsuma,N., Doyu,M. and
            Sobue,G.
  TITLE     Two novel genes, human neugrin and mouse m-neugrin, are upregulated
            with neuronal differentiation in neuroblastoma cells
  JOURNAL   Biochem Biophys Res Commun 279 (2), 526-533 (2000)
   PUBMED   11118320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM062823.1, BC101926.1 and AA818112.1.
            
            On Jul 16, 2009 this sequence version replaced NP_001029072.1.
            
            Transcript Variant: This variant (2) encodes the functional
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM062823.1, FQ215222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..293
                     /product="neugrin precursor"
                     /note="neurite outgrowth-associated protein; mesenchymal
                     stem cell protein DSC92"
                     /calculated_mol_wt=31379
     sig_peptide     1..15
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3T1H2.3)"
                     /calculated_mol_wt=1591
     mat_peptide     16..293
                     /product="Neugrin. /id=PRO_0000294486"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T1H2.3)"
                     /calculated_mol_wt=31379
     Region          25..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T1H2.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPE2; propagated from
                     UniProtKB/Swiss-Prot (Q3T1H2.3)"
     Region          73..293
                     /region_name="Neugrin"
                     /note="pfam06413"
                     /db_xref="CDD:428925"
     Region          162..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3T1H2.3)"
     Site            270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3T1H2.3)"
     CDS             1..293
                     /gene="Ngrn"
                     /gene_synonym="Neugrin"
                     /coded_by="NM_001033900.2:52..933"
                     /db_xref="GeneID:499191"
                     /db_xref="RGD:1583734"
ORIGIN      
        1 malslslflg grvraavarc gfasqgvagp gsisrepdpd sdwepeerel qevesalkrq
       61 kkamrfqkir rqmeapgapp rtltweameq irylhkefae swsvprlaeg fdvstdvirr
      121 vlkskfiptl eqklkqdqkv lkkagitrvv wqlpvsedtl kplsaghpms gpllmpgdev
      181 ssnsqthsra lkvksnapsa eaqkkreekn krirvlaesl vptttalghq relqkytthd
      241 seadrrannh ilpsveklee leagepgdqn fsskvvqkgr effdsngnfl yri
//
LOCUS       NP_037044                181 aa            linear   ROD 27-APR-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-3 [Rattus
            norvegicus].
ACCESSION   NP_037044 XP_001068451
VERSION     NP_037044.1
DBSOURCE    REFSEQ: accession NM_012912.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Li,L., Fu,G., Liu,C. and Liu,Y.
  TITLE     ATF3/EGR1 regulates myocardial ischemia/reperfusion injury induced
            autophagy and inflammation in cardiomyocytes
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (3), 125-129 (2024)
   PUBMED   38650141
  REMARK    GeneRIF: ATF3/EGR1 regulates myocardial ischemia/reperfusion injury
            induced autophagy and inflammation in cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Kang,Q., Zhang,J., Xie,C., Fang,S. and Chai,W.
  TITLE     Circular RNA SLC8A1 triggers hippocampal neuronal ferroptosis by
            regulating FUS-mediated ATF3 mRNA stability in epilepsy
  JOURNAL   Exp Cell Res 434 (1), 113848 (2024)
   PUBMED   37918704
  REMARK    GeneRIF: Circular RNA SLC8A1 triggers hippocampal neuronal
            ferroptosis by regulating FUS-mediated ATF3 mRNA stability in
            epilepsy.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Jiang,W., Jia,Q., Ma,H., Han,S., Bi,S., Zhu,K., Chen,L. and
            Liang,G.
  TITLE     MicroRNA-124 conducts neuroprotective effect via inhibiting
            AK4/ATF3 after subarachnoid hemorrhage
  JOURNAL   Exp Brain Res 242 (1), 33-45 (2024)
   PUBMED   37932484
  REMARK    GeneRIF: MicroRNA-124 conducts neuroprotective effect via
            inhibiting AK4/ATF3 after subarachnoid hemorrhage.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Zhao,Y., Du,Y., Gao,Y., Xu,Z., Zhao,D. and Yang,M.
  TITLE     ATF3 Regulates Osteogenic Function by Mediating Osteoblast
            Ferroptosis in Type 2 Diabetic Osteoporosis
  JOURNAL   Dis Markers 2022, 9872243 (2022)
   PUBMED   36340581
  REMARK    GeneRIF: ATF3 Regulates Osteogenic Function by Mediating Osteoblast
            Ferroptosis in Type 2 Diabetic Osteoporosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Ma,N., Li,G. and Fu,X.
  TITLE     Protective role of activating transcription factor 3 against
            neuronal damage in rats with cerebral ischemia
  JOURNAL   Brain Behav 12 (4), e2522 (2022)
   PUBMED   35263513
  REMARK    GeneRIF: Protective role of activating transcription factor 3
            against neuronal damage in rats with cerebral ischemia.
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Allen-Jennings,A.E., Hartman,M.G., Kociba,G.J. and Hai,T.
  TITLE     The roles of ATF3 in liver dysfunction and the regulation of
            phosphoenolpyruvate carboxykinase gene expression
  JOURNAL   J Biol Chem 277 (22), 20020-20025 (2002)
   PUBMED   11916968
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Okamoto,Y., Chaves,A., Chen,J., Kelley,R., Jones,K., Weed,H.G.,
            Gardner,K.L., Gangi,L., Yamaguchi,M., Klomkleaw,W., Nakayama,T.,
            Hamlin,R.L., Carnes,C., Altschuld,R., Bauer,J. and Hai,T.
  TITLE     Transgenic mice with cardiac-specific expression of activating
            transcription factor 3, a stress-inducible gene, have conduction
            abnormalities and contractile dysfunction
  JOURNAL   Am J Pathol 159 (2), 639-650 (2001)
   PUBMED   11485922
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Chen,B.P., Wolfgang,C.D. and Hai,T.
  TITLE     Analysis of ATF3, a transcription factor induced by physiological
            stresses and modulated by gadd153/Chop10
  JOURNAL   Mol Cell Biol 16 (3), 1157-1168 (1996)
   PUBMED   8622660
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Hsu,J.C., Laz,T., Mohn,K.L. and Taub,R.
  TITLE     Identification of LRF-1, a leucine-zipper protein that is rapidly
            and highly induced in regenerating liver
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3511-3515 (1991)
   PUBMED   1902565
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Hai,T.W., Liu,F., Coukos,W.J. and Green,M.R.
  TITLE     Transcription factor ATF cDNA clones: an extensive family of
            leucine zipper proteins able to selectively form DNA-binding
            heterodimers
  JOURNAL   Genes Dev 3 (12B), 2083-2090 (1989)
   PUBMED   2516827
  REMARK    Erratum:[Genes Dev 1990 Apr;4(4):682]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078903.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001068451.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078903.1, M63282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN12840108
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q27"
     Protein         1..181
                     /product="cyclic AMP-dependent transcription factor ATF-3"
                     /note="liver regeneration factor 1; cAMP-dependent
                     transcription factor ATF-3; cyclic AMP-dependent
                     transcription factor ATF-3-like"
                     /calculated_mol_wt=20633
     Region          76..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29596.1)"
     Region          88..110
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P29596.1)"
     Region          96..149
                     /region_name="bZIP_ATF3"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-3 (ATF-3) and similar proteins: a
                     DNA-binding and dimerization domain; cd14722"
                     /db_xref="CDD:269870"
     Region          96..146
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269870"
     Site            order(107,110..111,114..115,117..118,121..122,124..125,
                     128..129,131..132,135..136,138..139,142..143,145..146)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269870"
     Region          114..142
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P29596.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P18847; propagated from
                     UniProtKB/Swiss-Prot (P29596.1)"
     CDS             1..181
                     /gene="Atf3"
                     /gene_synonym="LRF-1; LRFI"
                     /coded_by="NM_012912.2:158..703"
                     /db_xref="GeneID:25389"
                     /db_xref="RGD:2165"
ORIGIN      
        1 mmlqhpgqvs asevsataiv pclsppgslv fedfanltpf vkeelrfaiq nkhlchrmss
       61 alesvtinnr plemsvtkse vapeederkr rrrernkiaa akcrnkkkek teclqkesek
      121 lesvnaelka qieelknekq hliymlnlhr ptcivraqng rtpedernlf iqqikegtlq
      181 s
//
LOCUS       NP_075235                992 aa            linear   ROD 27-APR-2025
DEFINITION  disks large-associated protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_075235
VERSION     NP_075235.3
DBSOURCE    REFSEQ: accession NM_022946.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Tao-Cheng,J.H., Yang,Y., Reese,T.S. and Dosemeci,A.
  TITLE     Differential distribution of Shank and GKAP at the postsynaptic
            density
  JOURNAL   PLoS One 10 (3), e0118750 (2015)
   PUBMED   25775468
  REMARK    GeneRIF: Upon depolarization with high K+, neither the intensity
            nor distribution of label for GKAP changed, but labeling intensity
            for Shank at the postsynaptic density increased to ~150% of
            controls.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Tong,J., Yang,H. and Im,Y.J.
  TITLE     Crystallization and preliminary X-ray crystallographic analysis of
            the C-terminal domain of guanylate kinase-associated protein from
            Rattus norvegicus
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 7), 949-954 (2014)
   PUBMED   25005096
  REMARK    GeneRIF: The C-terminal helical domain of GKAP from Rattus
            norvegicus was purified and crystallized as a fusion protein.
REFERENCE   4  (residues 1 to 992)
  AUTHORS   Shin,S.M., Zhang,N., Hansen,J., Gerges,N.Z., Pak,D.T., Sheng,M. and
            Lee,S.H.
  TITLE     GKAP orchestrates activity-dependent postsynaptic protein
            remodeling and homeostatic scaling
  JOURNAL   Nat Neurosci 15 (12), 1655-1666 (2012)
   PUBMED   23143515
  REMARK    GeneRIF: Activity-dependent turnover of postsynnaptic density
            proteins orchestrated by GKAP is critical for homeostatic
            plasticity.
REFERENCE   5  (residues 1 to 992)
  AUTHORS   Chua,J.J., Schob,C., Rehbein,M., Gkogkas,C.G., Richter,D. and
            Kindler,S.
  TITLE     Synthesis of two SAPAP3 isoforms from a single mRNA is mediated via
            alternative translational initiation
  JOURNAL   Sci Rep 2, 484 (2012)
   PUBMED   22761992
REFERENCE   6  (residues 1 to 992)
  AUTHORS   Hirao,K., Hata,Y., Ide,N., Takeuchi,M., Irie,M., Yao,I.,
            Deguchi,M., Toyoda,A., Sudhof,T.C. and Takai,Y.
  TITLE     A novel multiple PDZ domain-containing molecule interacting with
            N-methyl-D-aspartate receptors and neuronal cell adhesion proteins
  JOURNAL   J Biol Chem 273 (33), 21105-21110 (1998)
   PUBMED   9694864
REFERENCE   7  (residues 1 to 992)
  AUTHORS   Kawashima,N., Takamiya,K., Sun,J., Kitabatake,A. and Sobue,K.
  TITLE     Differential expression of isoforms of PSD-95 binding protein
            (GKAP/SAPAP1) during rat brain development
  JOURNAL   FEBS Lett 418 (3), 301-304 (1997)
   PUBMED   9428732
REFERENCE   8  (residues 1 to 992)
  AUTHORS   Satoh,K., Yanai,H., Senda,T., Kohu,K., Nakamura,T., Okumura,N.,
            Matsumine,A., Kobayashi,S., Toyoshima,K. and Akiyama,T.
  TITLE     DAP-1, a novel protein that interacts with the guanylate
            kinase-like domains of hDLG and PSD-95
  JOURNAL   Genes Cells 2 (6), 415-424 (1997)
   PUBMED   9286858
REFERENCE   9  (residues 1 to 992)
  AUTHORS   Takeuchi,M., Hata,Y., Hirao,K., Toyoda,A., Irie,M. and Takai,Y.
  TITLE     SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
            postsynaptic density
  JOURNAL   J Biol Chem 272 (18), 11943-11951 (1997)
   PUBMED   9115257
REFERENCE   10 (residues 1 to 992)
  AUTHORS   Kim,E., Naisbitt,S., Hsueh,Y.P., Rao,A., Rothschild,A., Craig,A.M.
            and Sheng,M.
  TITLE     GKAP, a novel synaptic protein that interacts with the guanylate
            kinase-like domain of the PSD-95/SAP90 family of channel clustering
            molecules
  JOURNAL   J Cell Biol 136 (3), 669-678 (1997)
   PUBMED   9024696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jan 17, 2015 this sequence version replaced NP_075235.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript from the reference strain was
            available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..992
                     /product="disks large-associated protein 1 isoform 1"
                     /note="disks large-associated protein 1;
                     PSD-95/SAP90-binding protein 1; SAP90/PSD-95-associated
                     protein 1; PSD-95 binding protein; guanylate
                     kinase-associated protein; discs large homolog associated
                     protein 1"
                     /calculated_mol_wt=110117
     Region          154..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Region          355..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D415; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Region          660..992
                     /region_name="GKAP"
                     /note="Guanylate-kinase-associated protein (GKAP) protein;
                     pfam03359"
                     /db_xref="CDD:460897"
     Region          665..676
                     /region_name="Interaction with DYL2.
                     /evidence=ECO:0000269|PubMed:14760703"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     Region          687..698
                     /region_name="Interaction with DYL2.
                     /evidence=ECO:0000269|PubMed:14760703"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     Region          914..980
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97836.1)"
     Region          990..992
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P97836.1)"
     CDS             1..992
                     /gene="Dlgap1"
                     /gene_synonym="DAP-1; Gkap; GKAP/SAPAP1; rGKAP; SAPAP1"
                     /coded_by="NM_022946.3:267..3245"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65040"
                     /db_xref="RGD:620223"
ORIGIN      
        1 mkglsgsrsh hhgitcesac dslshhsdhk pyllspvdhh padhpyytqr nsfqaecvgp
       61 fsdplasstf prrhytsqqe lkdesalvpr tlatkanrlp tnlldqferq lplsrdgyht
      121 lqykrtaveh rsdspgrirh lvhsvqklft kshslegpsk ggvnggkasp dgsqtvrygk
      181 rskskerrse pkarsnasna sptspswwss ddnldgdmcl yhtpsgvmtm grcpdrsasq
      241 yfmeayntis eqavkasrsn ndvkcstcan lpvtldapll kksawsstlt vsrarevyqk
      301 asvnmdqavv kseacqqers cqylqvpqde wtgytprgkd deipcrrmrs gsyikamgde
      361 dsgdsdtspk pspkvaarre sylkatqpsl telttlkisn ehspklqirs hsylravsev
      421 sinrsldsld paglltspkf rsrnesymra mstisqvsem evngqfesvc esvfselesq
      481 avealdlpmp gcfrmrshsy vraiekgcsq ddecvslrss spprttttvr tiqsstgvik
      541 lssavevssc ittykktppp vpprtttkpf isitaqsste saqdaymdgq gqrgdmisqs
      601 glsnstesld smkaltaaie aanaqihgpa sqhmgsnaaa vtttttiatv ttedrkkdfk
      661 knrclsigiq vddaeesekm aesktsskfq svgvqveeek cfrrftrsns vttavqadld
      721 fhdnlensle siednscpgp marqfsrdas tstvsiqgsg nhyhacaadd dfdtdfdpsi
      781 lpppdpwids itedpleavq rsvchrdghw flkllqaerd rmegwckqme reerennlpe
      841 dilgkirtav gsaqllmaqk fyqfrelcee nlnpnahprp tsqdlagfwd mlqlsienis
      901 mkfdelhqlk annwkqmdpl dkkerrappp vpkkpakgpa plirersles sqrqearkrl
      961 maakraasvr qnsatesaes ieiyipeaqt rl
//
LOCUS       NP_579840                368 aa            linear   ROD 27-APR-2025
DEFINITION  oxidized low-density lipoprotein receptor 1 [Rattus norvegicus].
ACCESSION   NP_579840
VERSION     NP_579840.2
DBSOURCE    REFSEQ: accession NM_133306.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Arkelius,K., Wendt,T.S., Andersson,H., Arnou,A., Gottschalk,M.,
            Gonzales,R.J. and Ansar,S.
  TITLE     LOX-1 and MMP-9 Inhibition Attenuates the Detrimental Effects of
            Delayed rt-PA Therapy and Improves Outcomes After Acute Ischemic
            Stroke
  JOURNAL   Circ Res 134 (8), 954-969 (2024)
   PUBMED   38501247
  REMARK    GeneRIF: LOX-1 and MMP-9 Inhibition Attenuates the Detrimental
            Effects of Delayed rt-PA Therapy and Improves Outcomes After Acute
            Ischemic Stroke.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Lei,H., Guo,W., Pan,Y., Lu,X. and Zhang,Q.
  TITLE     LOX-1 regulation of H-type vascular endothelial cell regeneration
            in hyperglycemia
  JOURNAL   Acta Diabetol 61 (4), 515-524 (2024)
   PUBMED   38244081
  REMARK    GeneRIF: LOX-1 regulation of H-type vascular endothelial cell
            regeneration in hyperglycemia.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Aoki,Y., Dai,H., Furuta,F., Akamatsu,T., Oshima,T., Takahashi,N.,
            Goto,Y.I., Oka,A. and Itoh,M.
  TITLE     LOX-1 mediates inflammatory activation of microglial cells through
            the p38-MAPK/NF-kappaB pathways under hypoxic-ischemic conditions
  JOURNAL   Cell Commun Signal 21 (1), 126 (2023)
   PUBMED   37268943
  REMARK    GeneRIF: LOX-1 mediates inflammatory activation of microglial cells
            through the p38-MAPK/NF-kappaB pathways under hypoxic-ischemic
            conditions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhang,Y., Zhang,R., Lu,L., Zhou,N., Lv,X., Wang,X. and Feng,Z.
  TITLE     Knockdown of lectin-like oxidized low-density lipoprotein-1
            ameliorates alcoholic cardiomyopathy via inactivating the p38
            mitogen-activated protein kinase pathway
  JOURNAL   Bioengineered 13 (4), 8926-8936 (2022)
   PUBMED   35333694
  REMARK    GeneRIF: Knockdown of lectin-like oxidized low-density
            lipoprotein-1 ameliorates alcoholic cardiomyopathy via inactivating
            the p38 mitogen-activated protein kinase pathway.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Akamatsu,T., Sugiyama,T., Oshima,T., Aoki,Y., Mizukami,A.,
            Goishi,K., Shichino,H., Kato,N., Takahashi,N., Goto,Y.I., Oka,A.
            and Itoh,M.
  TITLE     Lectin-Like Oxidized Low-Density Lipoprotein Receptor-1-Related
            Microglial Activation in Neonatal Hypoxic-Ischemic Encephalopathy:
            Morphologic Consideration
  JOURNAL   Am J Pathol 191 (7), 1303-1313 (2021)
   PUBMED   33964218
  REMARK    GeneRIF: Lectin-Like Oxidized Low-Density Lipoprotein
            Receptor-1-Related Microglial Activation in Neonatal
            Hypoxic-Ischemic Encephalopathy: Morphologic Consideration.
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Lucarelli,M., Borrelli,V., Fiori,A., Cucina,A., Granata,F.,
            Potenza,R.L., Scarpa,S., Cavallaro,A. and Strom,R.
  TITLE     The expression of native and oxidized LDL receptors in brain
            microvessels is specifically enhanced by astrocytes-derived soluble
            factor(s)
  JOURNAL   FEBS Lett 522 (1-3), 19-23 (2002)
   PUBMED   12095612
  REMARK    GeneRIF: expression pattern of LOX1-R in brain microvessels
            endothelial cells and its modulation by astrocytes
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Li,D.Y., Chen,H.J., Staples,E.D., Ozaki,K., Annex,B., Singh,B.K.,
            Vermani,R. and Mehta,J.L.
  TITLE     Oxidized low-density lipoprotein receptor LOX-1 and apoptosis in
            human atherosclerotic lesions
  JOURNAL   J Cardiovasc Pharmacol Ther 7 (3), 147-153 (2002)
   PUBMED   12232563
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Nagase,M., Abe,J., Takahashi,K., Ando,J., Hirose,S. and Fujita,T.
  TITLE     Genomic organization and regulation of expression of the
            lectin-like oxidized low-density lipoprotein receptor (LOX-1) gene
  JOURNAL   J Biol Chem 273 (50), 33702-33707 (1998)
   PUBMED   9837956
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Hoshikawa,H., Sawamura,T., Kakutani,M., Aoyama,T., Nakamura,T. and
            Masaki,T.
  TITLE     High affinity binding of oxidized LDL to mouse lectin-like oxidized
            LDL receptor (LOX-1)
  JOURNAL   Biochem Biophys Res Commun 245 (3), 841-846 (1998)
   PUBMED   9588202
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Nagase,M., Hirose,S. and Fujita,T.
  TITLE     Unique repetitive sequence and unexpected regulation of expression
            of rat endothelial receptor for oxidized low-density lipoprotein
            (LOX-1)
  JOURNAL   Biochem J 330 (Pt 3) (Pt 3), 1417-1422 (1998)
   PUBMED   9494115
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1 and BC097290.1.
            
            On Sep 11, 2012 this sequence version replaced NP_579840.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB005900.1, BC097290.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..368
                     /product="oxidized low-density lipoprotein receptor 1"
                     /note="ox-LDL receptor 1; lectin-like oxLDL receptor 1;
                     lectin-like oxidized LDL receptor 1; lectin-type oxidized
                     LDL receptor 1; Lectin-like oxidized low-density
                     lipoprotein receptor-1; oxidised low density lipoprotein
                     (lectin-like) receptor 1; oxidized low density lipoprotein
                     (lectin-like) receptor 1; lectin-like oxidized low-density
                     lipoprotein receptor"
                     /calculated_mol_wt=42247
     Region          <59..>233
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          239..360
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            order(295,322,344,346..347)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     CDS             1..368
                     /gene="Olr1"
                     /gene_synonym="LOX-1; Oldlr1; Oldr1"
                     /coded_by="NM_133306.2:80..1186"
                     /db_xref="GeneID:140914"
                     /db_xref="RGD:620515"
ORIGIN      
        1 mnlemafddk mkpvngqpdq kscgkkpkgl hllsstwwcp aavtlailcl vlsvtlivqq
       61 tqllqvsdll kqyqanltqq dhilegqmsa qkkaenasqe skrelkeqid tltwklneks
      121 keqekllqqn qnlqealqra vnaseeskwe lkeqidilnw klngiskeqk ellqqnqnlq
      181 ealqkaekys eesqrelkeq idtlswklne kskeqeellq qnqnlqealq raanssgpcp
      241 qdwiwhkenc ylfhgpfnwe ksrenclsld aqllqisttd dlnfvlqats hstspfwmgl
      301 hrknpnhpwl wengsplsfq ffrtrgvslq myssgtcayi qggvvfaenc iltafsicqk
      361 kanllltq
//
LOCUS       NP_001289137            1467 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_001289137
VERSION     NP_001289137.1
DBSOURCE    REFSEQ: accession NM_001302208.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1467)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1467)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1467)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1467)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1467)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1467)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1467)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1467)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1467)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081151.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            Transcript Variant: This variant (3) lacks an in-frame exon and has
            an alternate splice site in the 3' coding region, compared to
            variant 1. The resulting isoform (3) is shorter and lacks two
            internal segments, compared to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081151.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1467
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1467
                     /product="adhesion G protein-coupled receptor L2 isoform 3
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=161707
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          422..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Site            791
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          792..841
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            828..829
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098; propagated
                     from UniProtKB/Swiss-Prot (O88923.2)"
     Region          848..1120
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            885..905
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            912..932
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            957..977
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            995..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1056..1078
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1057..1077
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1082..1107
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1082..1102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1119..1467
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     Region          1130..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1366..1408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     CDS             1..1467
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001302208.1:463..4866"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleninny rvcdgyyntd lpgswvlgaf allcllgltw sfgllfvnee
     1081 tvvmaylfta fnafqglfif ifhcalqkkv rkeyakcfrh wyccgglpte sphssvkast
     1141 srtsaryssg tqsrirrmwn dtvrkqsess fisgmtgnyl ltnpllrphg tnnpyntlla
     1201 etvvcnapsa pvfnspghsl nntrdtsamd tlplngnfnn syslrkadyh dgvqvvdcgl
     1261 slndtafekm iiselvhnnl rgsnkthnle lklpvkpvig gssseddaiv adasslmhgd
     1321 npglefrhke leaplipqrt hsllyqpqkk vkpeatdsyv sqltaeadeh lqspnrdsly
     1381 tsmpnlrdsp ypesspdmae dlspsrrsen ediyyksmpn lgagrqlqmc yqisrgnsdg
     1441 yiipinkegc ipegdvregq mqlvtsl
//
LOCUS       NP_997701                830 aa            linear   ROD 27-APR-2025
DEFINITION  mutS protein homolog 5 [Rattus norvegicus].
ACCESSION   NP_997701 XP_215314
VERSION     NP_997701.2
DBSOURCE    REFSEQ: accession NM_212536.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Liu,J.Y., Qian,C.Y., Gao,Y.F., Chen,J., Zhou,H.H. and Yin,J.Y.
  TITLE     Association between DNA mismatch repair gene polymorphisms and
            platinum-based chemotherapy toxicity in non-small cell lung cancer
            patients
  JOURNAL   Chin J Cancer 36 (1), 12 (2017)
   PUBMED   28093084
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Kolas,N.K., Svetlanov,A., Lenzi,M.L., Macaluso,F.P., Lipkin,S.M.,
            Liskay,R.M., Greally,J., Edelmann,W. and Cohen,P.E.
  TITLE     Localization of MMR proteins on meiotic chromosomes in mice
            indicates distinct functions during prophase I
  JOURNAL   J Cell Biol 171 (3), 447-458 (2005)
   PUBMED   16260499
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Di Giacomo,M., Barchi,M., Baudat,F., Edelmann,W., Keeney,S. and
            Jasin,M.
  TITLE     Distinct DNA-damage-dependent and -independent responses drive the
            loss of oocytes in recombination-defective mouse mutants
  JOURNAL   Proc Natl Acad Sci U S A 102 (3), 737-742 (2005)
   PUBMED   15640358
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   5  (residues 1 to 830)
  AUTHORS   Kolas,N.K. and Cohen,P.E.
  TITLE     Novel and diverse functions of the DNA mismatch repair family in
            mammalian meiosis and recombination
  JOURNAL   Cytogenet Genome Res 107 (3-4), 216-231 (2004)
   PUBMED   15467367
  REMARK    Review article
REFERENCE   6  (residues 1 to 830)
  AUTHORS   Kneitz,B., Cohen,P.E., Avdievich,E., Zhu,L., Kane,M.F., Hou,H. Jr.,
            Kolodner,R.D., Kucherlapati,R., Pollard,J.W. and Edelmann,W.
  TITLE     MutS homolog 4 localization to meiotic chromosomes is required for
            chromosome pairing during meiosis in male and female mice
  JOURNAL   Genes Dev 14 (9), 1085-1097 (2000)
   PUBMED   10809667
REFERENCE   7  (residues 1 to 830)
  AUTHORS   Fox,M. and Tottenham,R.C.
  TITLE     Urinary fistula from segmental infarction in a transplanted kidney:
            recovery following surgical repair
  JOURNAL   Br J Urol 44 (3), 336-338 (1972)
   PUBMED   4557077
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC083904.1.
            
            On Sep 30, 2009 this sequence version replaced NP_997701.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083904.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..830
                     /product="mutS protein homolog 5"
                     /calculated_mol_wt=92222
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG62.1)"
     Region          <242..809
                     /region_name="mutS1"
                     /note="DNA mismatch repair protein MutS; TIGR01070"
                     /db_xref="CDD:273427"
     Region          553..759
                     /region_name="ABC_MSH5_euk"
                     /note="ATP-binding cassette domain of eukaryotic MutS5
                     homolog; cd03281"
                     /db_xref="CDD:213248"
     Site            588..595
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213248"
     Site            order(591..592,594..596,632,667..668,704)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213248"
     Site            629..632
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213248"
     Site            637..650
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213248"
     Site            663..668
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213248"
     Site            671..674
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213248"
     Site            700..706
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213248"
     CDS             1..830
                     /gene="Msh5"
                     /coded_by="NM_212536.2:40..2532"
                     /db_xref="GeneID:294252"
                     /db_xref="RGD:1303008"
ORIGIN      
        1 mafratpgrt ppgpgpgvps asfsspqpam aapggieeed eeepaeihlc vlwssgylgi
       61 ayydtsdsti hfmpdapdhe slkllqrvld einpqsvvts akqdeamtqf lgklasqehr
      121 epkrpeiill psvdfgpeis kqrllsgnys fisesmtate kilflssiip fdcvltvral
      181 ggllkflsrr rvgveledys vgvpilgfkk fvlthlvsid qdtysvlqif kseshpsvyk
      241 vasglkegls lfgilnrcrc rwgqkllrlw ftrptrelre lnsrldvief flmpqnldma
      301 qmmhrllshi knvplilkrm klshtkvsdw qvlyktvysa lglrdacrsl pqsiqlfrdi
      361 tqefsddlhh iasligkvdf eeslaenrft vlpnidpeid akkrrlmglp sfltevaqke
      421 lenldscips csviyiplig fllsiprlsf mveasdfeie gldfmflsed klhyrsartk
      481 eldallgdlh ceirdqemll mhqlqcqvla rapvltrvld lasrldvlla lasaardygy
      541 srphyspciq gvrikngrhp lmelcartfv pnstdcggdq grvkvitgpn ssgksiylkq
      601 vglitfmalv gsfvpaeeae igvidaiftr ihscesislg lstfmidlnq vakavnnate
      661 hslvlidefg kgtnsvdgla lltavlrhwl algpscphif vatnflslvq lqllpqgplv
      721 qyltmetced gndlvffyql chgvasasha sytaaqaglp dpliargkev sdsirsgkpv
      781 kpmhelvrrt qmencqalvd kflkldledp sldldifisq evlpaattil
//
LOCUS       NP_113841               1263 aa            linear   ROD 27-APR-2025
DEFINITION  neurocan core protein precursor [Rattus norvegicus].
ACCESSION   NP_113841 XP_346488
VERSION     NP_113841.2
DBSOURCE    REFSEQ: accession NM_031653.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1263)
  AUTHORS   Yui,S., Fujita,N., Chung,C.S., Morita,M. and Nishimura,R.
  TITLE     Olfactory ensheathing cells (OECs) degrade neurocan in injured
            spinal cord by secreting matrix metalloproteinase-2 in a rat
            contusion model
  JOURNAL   Jpn J Vet Res 62 (4), 151-162 (2014)
   PUBMED   25597185
  REMARK    GeneRIF: In vitro results showed that MMP-2 was the dominant MMP
            expressed by olfactory ensheathing cells (OECs). In vivo results
            revealed that transplanted OECs secreted MMP-2 in injured spinal
            cord and that the transplantation decreased neurocan expression.
REFERENCE   2  (residues 1 to 1263)
  AUTHORS   Sajad,M., Zargan,J., Chawla,R., Umar,S. and Khan,H.A.
  TITLE     Upregulation of CSPG3 accompanies neuronal progenitor proliferation
            and migration in EAE
  JOURNAL   J Mol Neurosci 43 (3), 531-540 (2011)
   PUBMED   21107918
  REMARK    GeneRIF: Results report for the first time that extracellular
            matrix chondroitin sulphate proteoglycan, CSPG3 (neurocan) is
            upregulated after primary inflammatory injury.
REFERENCE   3  (residues 1 to 1263)
  AUTHORS   Shen,L.H., Li,Y., Gao,Q., Savant-Bhonsale,S. and Chopp,M.
  TITLE     Down-regulation of neurocan expression in reactive astrocytes
            promotes axonal regeneration and facilitates the neurorestorative
            effects of bone marrow stromal cells in the ischemic rat brain
  JOURNAL   Glia 56 (16), 1747-1754 (2008)
   PUBMED   18618668
  REMARK    GeneRIF: Our data suggest that BMSCs promote axonal regeneration by
            reducing neurocan expression in peri-infarct astrocytes.
REFERENCE   4  (residues 1 to 1263)
  AUTHORS   Deepa,S.S., Carulli,D., Galtrey,C., Rhodes,K., Fukuda,J.,
            Mikami,T., Sugahara,K. and Fawcett,J.W.
  TITLE     Composition of perineuronal net extracellular matrix in rat brain:
            a different disaccharide composition for the net-associated
            proteoglycans
  JOURNAL   J Biol Chem 281 (26), 17789-17800 (2006)
   PUBMED   16644727
REFERENCE   5  (residues 1 to 1263)
  AUTHORS   Cheng,D., Hoogenraad,C.C., Rush,J., Ramm,E., Schlager,M.A.,
            Duong,D.M., Xu,P., Wijayawardana,S.R., Hanfelt,J., Nakagawa,T.,
            Sheng,M. and Peng,J.
  TITLE     Relative and absolute quantification of postsynaptic density
            proteome isolated from rat forebrain and cerebellum
  JOURNAL   Mol Cell Proteomics 5 (6), 1158-1170 (2006)
   PUBMED   16507876
REFERENCE   6  (residues 1 to 1263)
  AUTHORS   Friedlander,D.R., Milev,P., Karthikeyan,L., Margolis,R.K.,
            Margolis,R.U. and Grumet,M.
  TITLE     The neuronal chondroitin sulfate proteoglycan neurocan binds to the
            neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and
            inhibits neuronal adhesion and neurite outgrowth
  JOURNAL   J Cell Biol 125 (3), 669-680 (1994)
   PUBMED   7513709
REFERENCE   7  (residues 1 to 1263)
  AUTHORS   Grumet,M., Milev,P., Sakurai,T., Karthikeyan,L., Bourdon,M.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Interactions with tenascin and differential effects on cell
            adhesion of neurocan and phosphacan, two major chondroitin sulfate
            proteoglycans of nervous tissue
  JOURNAL   J Biol Chem 269 (16), 12142-12146 (1994)
   PUBMED   7512960
REFERENCE   8  (residues 1 to 1263)
  AUTHORS   Rauch,U., Karthikeyan,L., Maurel,P., Margolis,R.U. and
            Margolis,R.K.
  TITLE     Cloning and primary structure of neurocan, a developmentally
            regulated, aggregating chondroitin sulfate proteoglycan of brain
  JOURNAL   J Biol Chem 267 (27), 19536-19547 (1992)
   PUBMED   1326557
REFERENCE   9  (residues 1 to 1263)
  AUTHORS   Rauch,U., Gao,P., Janetzko,A., Flaccus,A., Hilgenberg,L.,
            Tekotte,H., Margolis,R.K. and Margolis,R.U.
  TITLE     Isolation and characterization of developmentally regulated
            chondroitin sulfate and chondroitin/keratan sulfate proteoglycans
            of brain identified with monoclonal antibodies
  JOURNAL   J Biol Chem 266 (22), 14785-14801 (1991)
   PUBMED   1907283
REFERENCE   10 (residues 1 to 1263)
  AUTHORS   Hobbs,A.A. and Rosen,J.M.
  TITLE     Sequence of rat alpha- and gamma-casein mRNAs: evolutionary
            comparison of the calcium-dependent rat casein multigene family
  JOURNAL   Nucleic Acids Res 10 (24), 8079-8098 (1982)
   PUBMED   6298707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Sep 12, 2012 this sequence version replaced NP_113841.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M97161.1, SRR26643298.71098.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1263
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..1263
                     /product="neurocan core protein precursor"
                     /note="neurocan core protein; 245 kDa early postnatal core
                     glycoprotein; chondroitin sulfate proteoglycan 3; neurocan
                     core protein-like"
                     /calculated_mol_wt=133958
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2315
     Region          40..161
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          54..58
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          74..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          122..126
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          136..141
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          154..157
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          159..253
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            169..170
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          260..355
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            267..268
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          361..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55067.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          <381..709
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            410
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:O14594; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          453..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55067.1)"
     Region          556..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55067.1)"
     Region          689..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55067.1)"
     Site            743
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Site            950
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:1326557; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          959..989
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            973
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Region          993..1029
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(993,996,1010)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1035..1158
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(1129,1133,1135,1141,1143..1146,1149..1151)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153058"
     Region          1162..1218
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            1170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55067.1)"
     Site            order(1172,1192)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          1221..1263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55067.1)"
     CDS             1..1263
                     /gene="Ncan"
                     /gene_synonym="Cspg3"
                     /coded_by="NM_031653.2:77..3868"
                     /db_xref="GeneID:58982"
                     /db_xref="RGD:619941"
ORIGIN      
        1 mgaesvwasg llvlwllllv sgdqdtqdtt ttekglhmlk sgsgpiqaal aelvalpcff
       61 tlqprqsplg diprikwtkv qtasgqrqdl pilvakdnvv rvakgwqgrv slpayprhra
      121 natlllgplr asdsglyrcq vvkgiedeqd lvtlevtgvv fhyraardry altfaeaqea
      181 chlssatiaa prhlqaafed gfdncdagwl sdrtvrypit qsrpgcygdr sslpgvrsyg
      241 rrdpqelydv ycfarelgge vfyvgparrl tlagaralcq rqgaalasvg qlhlawhegl
      301 dqcdpgwlad gsvrypiqtp rrrcggsapg vrtvyrfanr tgfpapgarf daycfrahhh
      361 tpqrgdseip ssgdegeivs aegppapelk prlgeqevit pdfqeplvss gedepldltr
      421 tqasqetlas tpggptlasw psrekwlltg vtsstgvpsp sslgvdmeet tpsgtqvapt
      481 ptmrrgrfkg lngrhfqqqg pedqlleaae asaqpptlev tadhmgpsaa tealesdqsh
      541 spwailtnev dvpgagslgs rslpesrkws pslispstvp stdstpglkp gadeapgvks
      601 aihhppwlps epavpssips ealsavslqa spgdgspdfp ivamlrapkl wllphstlvp
      661 nvspiplspa splpssvpee qavrpvsfga edpetpfqtt maapgeashg speadsieie
      721 gissmqatkh pisgpwasld ssnvtvnpvp sdagilgtes gvldlpgspt sdgqatvdkv
      781 latwlplpgh gldtgsqstp meahgvtmsv eptvalegga tkdpmeatmd vvpstvdats
      841 gsepkssiss thvvvtaagd qgtptltpts segqvvaqes lgtltslpsh pwsslassmd
      901 evasvssgep tglwdipstl ipvslgldes dlkvvaespg legfweevas gqedptdpce
      961 nnpclhggtc rtngtmygcs cdqgyagenc eididdclcs pcenggtcid evngficlcl
     1021 psyggnlcek dtegcdrgwh kfqghcyryf ahrrawedae rdcrrraghl tsvhspeehk
     1081 finsfghens wiglndrtve rdfqwtdntg lqyenwrekq pdnffagged cvvmvaheng
     1141 rwndvpcnyn lpyvckkgtv lcgpppaven aslvgvrkvk ynvhatvryq cdegfsqhhv
     1201 atircrnngk wdrpqivctk prrshrmrrh hhhphrhhkp rkehrkhkrh paedwekdeg
     1261 dfc
//
LOCUS       NP_075245                384 aa            linear   ROD 27-APR-2025
DEFINITION  barH-like 2 homeobox protein [Rattus norvegicus].
ACCESSION   NP_075245
VERSION     NP_075245.1
DBSOURCE    REFSEQ: accession NM_022956.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Lin,S.C., Kao,S.Y., Chang,J.C., Liu,Y.C., Yu,E.H., Tseng,S.H.,
            Liu,C.J. and Chang,K.W.
  TITLE     Up-regulation of miR-187 modulates the advances of oral carcinoma
            by targeting BARX2 tumor suppressor
  JOURNAL   Oncotarget 7 (38), 61355-61365 (2016)
   PUBMED   27542258
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Mi,Y., Zhao,S., Zhang,W., Zhang,D., Weng,J., Huang,K., Sun,H.,
            Tang,H., Zhang,X., Sun,X., Peng,Z. and Wen,Y.
  TITLE     Down-regulation of Barx2 predicts poor survival in colorectal
            cancer
  JOURNAL   Biochem Biophys Res Commun 478 (1), 67-73 (2016)
   PUBMED   27453340
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Yamamoto,H., Watanabe,Y., Oikawa,R., Morita,R., Yoshida,Y.,
            Maehata,T., Yasuda,H. and Itoh,F.
  TITLE     BARHL2 Methylation Using Gastric Wash DNA or Gastric Juice Exosomal
            DNA is a Useful Marker For Early Detection of Gastric Cancer in an
            H. pylori-Independent Manner
  JOURNAL   Clin Transl Gastroenterol 7 (7), e184 (2016)
   PUBMED   27441821
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Chellappa,R., Li,S., Pauley,S., Jahan,I., Jin,K. and Xiang,M.
  TITLE     Barhl1 regulatory sequences required for cell-specific gene
            expression and autoregulation in the inner ear and central nervous
            system
  JOURNAL   Mol Cell Biol 28 (6), 1905-1914 (2008)
   PUBMED   18212062
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Mo,Z., Li,S., Yang,X. and Xiang,M.
  TITLE     Role of the Barhl2 homeobox gene in the specification of
            glycinergic amacrine cells
  JOURNAL   Development 131 (7), 1607-1618 (2004)
   PUBMED   14998930
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Saba,R., Nakatsuji,N. and Saito,T.
  TITLE     Mammalian BarH1 confers commissural neuron identity on dorsal cells
            in the spinal cord
  JOURNAL   J Neurosci 23 (6), 1987-1991 (2003)
   PUBMED   12657654
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Saito,T., Sawamoto,K., Okano,H., Anderson,D.J. and Mikoshiba,K.
  TITLE     Mammalian BarH homologue is a potential regulator of neural bHLH
            genes
  JOURNAL   Dev Biol 199 (2), 216-225 (1998)
   PUBMED   9698441
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB004056.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB004056.1, BF409413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..384
                     /product="barH-like 2 homeobox protein"
                     /note="homeobox protein B-H1; bar-class homeodomain
                     protein MBH1; BarH-class homeodomain transcription factor"
                     /calculated_mol_wt=41332
     Region          1..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88181.1)"
     Region          154..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88181.1)"
     Region          230..286
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          364..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88181.1)"
     CDS             1..384
                     /gene="Barhl2"
                     /gene_synonym="Barh; MBH1"
                     /coded_by="NM_022956.2:70..1224"
                     /db_xref="GeneID:65050"
                     /db_xref="RGD:620726"
ORIGIN      
        1 mtamegasgs sfgidtilsg agsgspgmmn gdfrslgear ttdfrsqatp spcseidtvg
       61 tapsspisvt leppephlvt dgpqhhhhlh hgqqppppsa ppaqslqpsp qqqpppqpqs
      121 aaqqlgsaaa aprtstssfl ikdilgdskp laacapysts vssphhtpkq ecnaahesfr
      181 pkleqedskt kldkredsqs dikchgtkee gdreitssre sppvrakkpr kartafsdhq
      241 lnqlersfer qkylsvqdrm dlaaalnltd tqvktwyqnr rtkwkrqtav glellaeagn
      301 ysalqrmfps pyfyhpsllg smdsttaaaa aaamyssmyr tppaphpqlq rplvprvlih
      361 glgpggqpal nplsnpipgt phpr
//
LOCUS       NP_001258020             404 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001258020
VERSION     NP_001258020.1
DBSOURCE    REFSEQ: accession NM_001271091.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1, CB585874.1 and CB713901.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY217032.1, SRR26360194.1612767.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..404
                     /product="protein NDRG4 isoform 1"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=44178
     Region          60..342
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..404
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_001271091.1:109..1323"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 mkvlghrlql ltglllhdvt maglqelrfp eekpllrgqd ateldnpdaf lsvvdtdwke
       61 hdietpygll hvvirgspkg nrpailtyhd vglnhklcfn tlfnledmqe itkhfvvchv
      121 dapgqqvgas qfpqgyqfps meqlatmlps vvqhfgfkyv igigvgagay vlakfalifp
      181 dlveglvlmn idpngkgwid waatklsglt stlpdtvlsh lfsqeelvnn telvqsyrqq
      241 issvvnqanl qlfwnmynsr rdldinrpgt vpnaktlrcp vmlvvgdnap aedgvvecns
      301 kldpttttfl kmadsgglpq vtqpgkltea fkyflqgmgy iahlkdrrls ggavpsasmt
      361 rlarsrtasl tsassvdgsr pqpcthsdss egmgqvnhtm evsc
//
LOCUS       NP_036851                391 aa            linear   ROD 27-APR-2025
DEFINITION  somatostatin receptor type 1 [Rattus norvegicus].
ACCESSION   NP_036851 XP_346771
VERSION     NP_036851.1
DBSOURCE    REFSEQ: accession NM_012719.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Bai,J., Liu,X., Le Goff,L., Gargala,G., Francois,A., Ballet,J.J.,
            Ducrotte,P., Favennec,L. and Towledahong,L.
  TITLE     Octreotide modulates the expression of somatostatin receptor
            subtypes in inflamed rat jejunum induced by Cryptosporidium parvum
  JOURNAL   PLoS One 13 (3), e0194058 (2018)
   PUBMED   29522573
  REMARK    GeneRIF: In the jejunums of Cryptosporidium-parvum-infected rats,
            daily octreotide therapy decreased mRNA levels of SSTR1 on day 14
            post-infection, although it increased mRNA levels of SSTR1 on day
            50 post-infection. Specific SSTRs may regulate the inflammatory
            pathway in the rat intestinal inflammation model.
            Erratum:[PLoS One. 2018 May 24;13(5):e0198377. doi:
            10.1371/journal.pone.0198377. PMID: 29795701]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Ludvigsen,E., Carlsson,C., Tiensuu Janson,E., Sandler,S. and
            Stridsberg,M.
  TITLE     Somatostatin receptor 1-5; expression profiles during rat
            development
  JOURNAL   Ups J Med Sci 120 (3), 157-168 (2015)
   PUBMED   25926390
  REMARK    GeneRIF: All SSTR1-5 proteins were observed at embryonal day 10 and
            increased with time in major structures, but the localization
            varied between the different subtypes. Only SSTR1 protein
            co-localized to a higher extent with the islet hormones studied.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Parks,G.S., Wang,L., Wang,Z. and Civelli,O.
  TITLE     Identification of neuropeptide receptors expressed by
            melanin-concentrating hormone neurons
  JOURNAL   J Comp Neurol 522 (17), 3817-3833 (2014)
   PUBMED   24978951
  REMARK    GeneRIF: This study demonistrated that sstr1 and
            Melanin-concentrating hormone colization in neuron in the lateral
            hypothalamus (LH) and zona incerta (ZI), but MCHR1 mRNA is widely
            expressed throughout the brain.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Yuan,D., Shen,J., Yan,Y., Wu,X., Li,A., Guo,A., Wu,Y., Duan,C.,
            Shen,J., Tang,C., Zhang,D. and Ji,Y.
  TITLE     Upregulated expression of SSTR1 is involved in neuronal apoptosis
            and is coupled to the reduction of bcl-2 following intracerebral
            hemorrhage in adult rats
  JOURNAL   Cell Mol Neurobiol 34 (7), 951-961 (2014)
   PUBMED   25035058
  REMARK    GeneRIF: up-regulated SSTR1 contributed to neuronal apoptosis after
            intracerebral hemorrhage, which was accompanied with reduced
            expression of bcl-2.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Gahete,M.D., Duran-Prado,M., Delgado-Niebla,E., Garrido,J.J.,
            Rhodes,S.J., Garcia-Navarro,S., Gracia-Navarro,F., Malagon,M.M.,
            Luque,R.M. and Castano,J.P.
  TITLE     Porcine sst1 can physically interact with other somatostatin
            receptors, and its expression is regulated by
            metabolic/inflammatory sensors
  JOURNAL   Am J Physiol Endocrinol Metab 306 (5), E483-E493 (2014)
   PUBMED   24368669
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Bruno,J.F., Xu,Y., Song,J. and Berelowitz,M.
  TITLE     Pituitary and hypothalamic somatostatin receptor subtype messenger
            ribonucleic acid expression in the food-deprived and diabetic rat
  JOURNAL   Endocrinology 135 (5), 1787-1792 (1994)
   PUBMED   7956902
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Fitzpatrick,V.D. and Vandlen,R.L.
  TITLE     6agonist selectivity determinants in somatostatin receptor subtypes
            I and II
  JOURNAL   J Biol Chem 269 (40), 24621-24626 (1994)
   PUBMED   7929134
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Li,X.J., Forte,M., North,R.A., Ross,C.A. and Snyder,S.H.
  TITLE     Cloning and expression of a rat somatostatin receptor enriched in
            brain
  JOURNAL   J Biol Chem 267 (30), 21307-21312 (1992)
   PUBMED   1400442
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Yamada,Y., Post,S.R., Wang,K., Tager,H.S., Bell,G.I. and Seino,S.
  TITLE     Cloning and functional characterization of a family of human and
            mouse somatostatin receptors expressed in brain, gastrointestinal
            tract, and kidney
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 251-255 (1992)
   PUBMED   1346068
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Meyerhof,W., Paust,H.J., Schonrock,C. and Richter,D.
  TITLE     Cloning of a cDNA encoding a novel putative G-protein-coupled
            receptor expressed in specific rat brain regions
  JOURNAL   DNA Cell Biol 10 (9), 689-694 (1991)
   PUBMED   1661599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346771.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. The exon structure and extent of
            this transcript is supported by orthologous data from mouse
            transcripts (NM_009216.3 and BY236756.1; GID 20605).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840106,
                              SAMN12840129 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..391
                     /product="somatostatin receptor type 1"
                     /note="SS1R; SRIF-2; SS1-R; SS-1-R; Somatostatin receptor
                     subtype 1; RNGPCRRNA"
                     /calculated_mol_wt=42615
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28646.1)"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28646.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28646.1)"
     Site            57..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Region          59..334
                     /region_name="7tmA_SSTR1"
                     /note="somatostatin receptor type 1, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15970"
                     /db_xref="CDD:320636"
     Region          60..86
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320636"
     Region          93..119
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320636"
     Site            95..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Site            order(114,117..118,130..135,137..138,141,186,188..192,220,
                     223..225,227..229,231..232,284,287..288,290..291,294,
                     301..302,304..306,309,312..313)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320636"
     Region          130..160
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320636"
     Site            132..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Region          172..194
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320636"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Region          220..249
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320636"
     Site            220..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Region          264..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320636"
     Site            271..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     Region          302..327
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320636"
     Site            304..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28646.1)"
     CDS             1..391
                     /gene="Sstr1"
                     /gene_synonym="Gpcrrna"
                     /coded_by="NM_012719.2:463..1638"
                     /db_xref="GeneID:25033"
                     /db_xref="RGD:3762"
ORIGIN      
        1 mfpngtapsp tsspssspgg cgegvcsrgp gsgaadgmee pgrnssqngt lsegqgsail
       61 isfiysvvcl vglcgnsmvi yvilryakmk tatniyilnl aiadellmls vpflvtstll
      121 rhwpfgallc rlvlsvdavn mftsiycltv lsvdryvavv hpikaaryrr ptvakvvnlg
      181 vwvlsllvil pivvfsrtaa nsdgtvacnm lmpepaqrwl vgfvlytflm gfllpvgaic
      241 lcyvliiakm rmvalkagwq qrkrserkit lmvmmvvmvf vicwmpfyvv qlvnvfaeqd
      301 datvsqlsvi lgyanscanp ilygflsdnf krsfqrilcl swmdnaaeep vdyyatalks
      361 raysvedfqp enlesggvfr ngtcasrist l
//
LOCUS       NP_037124                292 aa            linear   ROD 27-APR-2025
DEFINITION  nucleophosmin isoform 1 [Rattus norvegicus].
ACCESSION   NP_037124
VERSION     NP_037124.1
DBSOURCE    REFSEQ: accession NM_012992.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Pfister,J.A. and D'Mello,S.R.
  TITLE     Regulation of Neuronal Survival by Nucleophosmin 1 (NPM1) Is
            Dependent on Its Expression Level, Subcellular Localization, and
            Oligomerization Status
  JOURNAL   J Biol Chem 291 (39), 20787-20797 (2016)
   PUBMED   27510036
  REMARK    GeneRIF: study suggests that although neurons need NPM1 for
            survival, an increase in its expression beyond physiological levels
            and its translocation to the cytoplasm leads to death through
            abortive cell cycle induction.
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Kim,J.Y., Cho,Y.E. and Park,J.H.
  TITLE     The Nucleolar Protein GLTSCR2 Is an Upstream Negative Regulator of
            the Oncogenic Nucleophosmin-MYC Axis
  JOURNAL   Am J Pathol 185 (7), 2061-2068 (2015)
   PUBMED   25956029
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Kuzelova,K., Brodska,B., Fuchs,O., Dobrovolna,M., Soukup,P. and
            Cetkovsky,P.
  TITLE     Altered HLA Class I Profile Associated with Type A/D Nucleophosmin
            Mutation Points to Possible Anti-Nucleophosmin Immune Response in
            Acute Myeloid Leukemia
  JOURNAL   PLoS One 10 (5), e0127637 (2015)
   PUBMED   25992555
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Milochau,A., Lagree,V., Benassy,M.N., Chaignepain,S., Papin,J.,
            Garcia-Arcos,I., Lajoix,A., Monterrat,C., Coudert,L.,
            Schmitter,J.M., Ochoa,B. and Lang,J.
  TITLE     Synaptotagmin 11 interacts with components of the RNA-induced
            silencing complex RISC in clonal pancreatic beta-cells
  JOURNAL   FEBS Lett 588 (14), 2217-2222 (2014)
   PUBMED   24882364
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Mitrea,D.M., Grace,C.R., Buljan,M., Yun,M.K., Pytel,N.J.,
            Satumba,J., Nourse,A., Park,C.G., Madan Babu,M., White,S.W. and
            Kriwacki,R.W.
  TITLE     Structural polymorphism in the N-terminal oligomerization domain of
            NPM1
  JOURNAL   Proc Natl Acad Sci U S A 111 (12), 4466-4471 (2014)
   PUBMED   24616519
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Takemura,M., Ohta,N., Furuichi,Y., Takahashi,T., Yoshida,S.,
            Olson,M.O. and Umekawa,H.
  TITLE     Stimulation of calf thymus DNA polymerase alpha activity by
            nucleolar protein B23
  JOURNAL   Biochem Biophys Res Commun 199 (1), 46-51 (1994)
   PUBMED   8123045
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Biggiogera,M., Burki,K., Kaufmann,S.H., Shaper,J.H., Gas,N.,
            Amalric,F. and Fakan,S.
  TITLE     Nucleolar distribution of proteins B23 and nucleolin in mouse
            preimplantation embryos as visualized by immunoelectron microscopy
  JOURNAL   Development 110 (4), 1263-1270 (1990)
   PUBMED   2100262
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Chang,J.H. and Olson,M.O.
  TITLE     Structure of the gene for rat nucleolar protein B23
  JOURNAL   J Biol Chem 265 (30), 18227-18233 (1990)
   PUBMED   2211699
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Chang,J.H. and Olson,M.O.
  TITLE     A single gene codes for two forms of rat nucleolar protein B23 mRNA
  JOURNAL   J Biol Chem 264 (20), 11732-11737 (1989)
   PUBMED   2745414
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Chang,J.H., Dumbar,T.S. and Olson,M.O.
  TITLE     cDNA and deduced primary structure of rat protein B23, a nucleolar
            protein containing highly conserved sequences
  JOURNAL   J Biol Chem 263 (26), 12824-12827 (1988)
   PUBMED   3417636
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC060579.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060579.1, J03969.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16093048 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..292
                     /product="nucleophosmin isoform 1"
                     /note="nucleolar protein B23.1; NPM; numatrin; nucleolar
                     protein NO38; nucleolar phosphoprotein B23; nucleophosmin
                     (nucleolar phosphoprotein B23, numatrin)"
                     /calculated_mol_wt=32429
     Region          1..185
                     /region_name="Required for interaction with SENP3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Region          1..117
                     /region_name="Necessary for interaction with APEX1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1 and PLK2.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          18..117
                     /region_name="Nucleoplasmin"
                     /note="Nucleoplasmin/nucleophosmin domain; pfam03066"
                     /db_xref="CDD:460792"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            55
                     /site_type="other"
                     /note="Interaction between pentamers.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61937; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            80
                     /site_type="other"
                     /note="Interaction between pentamers.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          138..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            150
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          152..157
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          186..214
                     /region_name="Interaction with NOP2.
                     /evidence=ECO:0000250|UniProtKB:P06748"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Region          190..196
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1 and CDK2.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            211
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            227
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          241..292
                     /region_name="Required for nucleolar localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P13084.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Region          243..291
                     /region_name="NPM1-C"
                     /note="Nucleophosmin C-terminal domain; pfam16276"
                     /db_xref="CDD:465081"
     Site            248
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            255
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            271
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     Site            290
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06748; propagated from
                     UniProtKB/Swiss-Prot (P13084.1)"
     CDS             1..292
                     /gene="Npm1"
                     /gene_synonym="B23NP"
                     /coded_by="NM_012992.4:94..972"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25498"
                     /db_xref="RGD:3192"
ORIGIN      
        1 medsmdmdms plrpqnylfg celkadkdyh fkvdndeneh qlslrtvslg agakdelhiv
       61 eaeamnyegs pikvtlatlk msvqptvslg gfeitppvvl rlkcgsgpvh isgqhlvave
      121 edaesedede edvkllgmsg krsapgggnk vpqkkvklde dddeddedde ddeddddddf
      181 deeeteekvp vkksvrdtpa knaqksnqng kdlkpstprs kgqesfkkqe ktpktpkgps
      241 svedikakmq asiekggslp kveakfinyv kncfrmtdqe aiqdlwqwrk sl
//
LOCUS       NP_001257798             271 aa            linear   ROD 27-APR-2025
DEFINITION  neurotrophin-3 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001257798
VERSION     NP_001257798.1
DBSOURCE    REFSEQ: accession NM_001270869.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Briones-Vidal,M.G., Reyes-Garcia,S.E. and Escobar,M.L.
  TITLE     Neurotrophin-3 into the insular cortex strengthens conditioned
            taste aversion memory
  JOURNAL   Behav Brain Res 461, 114857 (2024)
   PUBMED   38211776
  REMARK    GeneRIF: Neurotrophin-3 into the insular cortex strengthens
            conditioned taste aversion memory.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zou,D., Wang,H., Hao,S. and Chen,F.
  TITLE     Repair effect of neurotrophic factor III (NT-3) on rats with spinal
            injury model and its mechanism
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (1), 56-61 (2024)
   PUBMED   38372112
  REMARK    GeneRIF: Repair effect of neurotrophic factor III (NT-3) on rats
            with spinal injury model and its mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Yang,Y., Xu,H.Y., Deng,Q.W., Wu,G.H., Zeng,X., Jin,H., Wang,L.J.,
            Lai,B.Q., Li,G., Ma,Y.H., Jiang,B., Ruan,J.W., Wang,Y.Q., Ding,Y.
            and Zeng,Y.S.
  TITLE     Electroacupuncture facilitates the integration of a grafted
            TrkC-modified mesenchymal stem cell-derived neural network into
            transected spinal cord in rats via increasing neurotrophin-3
  JOURNAL   CNS Neurosci Ther 27 (7), 776-791 (2021)
   PUBMED   33763978
  REMARK    GeneRIF: Electroacupuncture facilitates the integration of a
            grafted TrkC-modified mesenchymal stem cell-derived neural network
            into transected spinal cord in rats via increasing neurotrophin-3.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Xu,H., Yang,Y., Deng,Q.W., Zhang,B.B., Ruan,J.W., Jin,H.,
            Wang,J.H., Ren,J., Jiang,B., Sun,J.H., Zeng,Y.S. and Ding,Y.
  TITLE     Governor Vessel Electro-Acupuncture Promotes the Intrinsic Growth
            Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury
  JOURNAL   J Neurotrauma 38 (6), 734-745 (2021)
   PUBMED   33121345
  REMARK    GeneRIF: Governor Vessel Electro-Acupuncture Promotes the Intrinsic
            Growth Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Donsante,A., Xue,J., Poth,K.M., Hardcastle,N.S., Diniz,B.,
            O'Connor,D.M., Xia,Y. and Boulis,N.M.
  TITLE     Controlling the Release of Neurotrophin-3 and Chondroitinase ABC
            Enhances the Efficacy of Nerve Guidance Conduits
  JOURNAL   Adv Healthc Mater 9 (14), e2000200 (2020)
   PUBMED   32548984
  REMARK    GeneRIF: Controlling the Release of Neurotrophin-3 and
            Chondroitinase ABC Enhances the Efficacy of Nerve Guidance
            Conduits.
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Smith,M.A., Makino,S., Altemus,M., Michelson,D., Hong,S.K.,
            Kvetnansky,R. and Post,R.M.
  TITLE     Stress and antidepressants differentially regulate neurotrophin 3
            mRNA expression in the locus coeruleus
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8788-8792 (1995)
   PUBMED   7568018
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Le Beau,M.M., Espinosa,R. 3rd, Ip,N.Y.,
            Belluscio,L., de la Monte,S.M., Squinto,S., Furth,M.E. and
            Yancopoulos,G.D.
  TITLE     Human and rat brain-derived neurotrophic factor and neurotrophin-3:
            gene structures, distributions, and chromosomal localizations
  JOURNAL   Genomics 10 (3), 558-568 (1991)
   PUBMED   1889806
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Hallbook,F., Ibanez,C.F. and Persson,H.
  TITLE     Evolutionary studies of the nerve growth factor family reveal a
            novel member abundantly expressed in Xenopus ovary
  JOURNAL   Neuron 6 (5), 845-858 (1991)
   PUBMED   2025430
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Ernfors,P., Ibanez,C.F., Ebendal,T., Olson,L. and Persson,H.
  TITLE     Molecular cloning and neurotrophic activities of a protein with
            structural similarities to nerve growth factor: developmental and
            topographical expression in the brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5454-5458 (1990)
   PUBMED   2164684
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Belluscio,L., Squinto,S., Ip,N.Y., Furth,M.E.,
            Lindsay,R.M. and Yancopoulos,G.D.
  TITLE     Neurotrophin-3: a neurotrophic factor related to NGF and BDNF
  JOURNAL   Science 247 (4949 Pt 1), 1446-1451 (1990)
   PUBMED   2321006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1, FM101680.1, M34643.1 and BC070504.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM101680.1, FM080103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..271
                     /product="neurotrophin-3 isoform 1 precursor"
                     /note="HDNF; NT-3; NGF-2; neurotrophic factor; nerve
                     growth factor 2; neurotrophin-3 (HDNF/NT-3)"
                     /calculated_mol_wt=27558
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3490
     Region          33..146
                     /region_name="NTF3_N"
                     /note="Neutrophin-3 N-terminus; pfam19338"
                     /db_xref="CDD:437170"
     Region          158..269
                     /region_name="NGF"
                     /note="Nerve growth factor family; pfam00243"
                     /db_xref="CDD:459728"
     CDS             1..271
                     /gene="Ntf3"
                     /coded_by="NM_001270869.1:201..1016"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:81737"
                     /db_xref="RGD:619728"
ORIGIN      
        1 mvtsatilqv nkvmsilfyv iflaylrgiq gnnmdqrslp edslnsliik liqadilknk
       61 lskqmvdvke nyqstlpkae aprepeqgea trsefqpmia tdtellrqqr rynsprvlls
      121 dstplepppl ylmedyvgnp vvtnrtsprr kryaehkshr geysvcdses lwvtdkssai
      181 dirghqvtvl geiktgnspv kqyfyetrck earpvkngcr giddkhwnsq cktsqtyvra
      241 ltsennklvg wrwiridtsc vcalsrkigr t
//
LOCUS       NP_071790                489 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial-processing peptidase subunit beta precursor [Rattus
            norvegicus].
ACCESSION   NP_071790
VERSION     NP_071790.1
DBSOURCE    REFSEQ: accession NM_022395.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Mossmann,D., Meisinger,C. and Vogtle,F.N.
  TITLE     Processing of mitochondrial presequences
  JOURNAL   Biochim Biophys Acta 1819 (9-10), 1098-1106 (2012)
   PUBMED   22172993
  REMARK    Review article
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Greene,A.W., Grenier,K., Aguileta,M.A., Muise,S., Farazifard,R.,
            Haque,M.E., McBride,H.M., Park,D.S. and Fon,E.A.
  TITLE     Mitochondrial processing peptidase regulates PINK1 processing,
            import and Parkin recruitment
  JOURNAL   EMBO Rep 13 (4), 378-385 (2012)
   PUBMED   22354088
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Kitada,S., Yamasaki,E., Kojima,K. and Ito,A.
  TITLE     Determination of the cleavage site of the presequence by
            mitochondrial processing peptidase on the substrate binding
            scaffold and the multiple subsites inside a molecular cavity
  JOURNAL   J Biol Chem 278 (3), 1879-1885 (2003)
   PUBMED   12433926
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Kitada,S., Kojima,K. and Ito,A.
  TITLE     Glu(191) and Asp(195) in rat mitochondrial processing peptidase
            beta subunit are involved in effective cleavage of precursor
            protein through interaction with the proximal arginine
  JOURNAL   Biochem Biophys Res Commun 287 (3), 594-599 (2001)
   PUBMED   11563836
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Nagao,Y., Kitada,S., Kojima,K., Toh,H., Kuhara,S., Ogishima,T. and
            Ito,A.
  TITLE     Glycine-rich region of mitochondrial processing peptidase
            alpha-subunit is essential for binding and cleavage of the
            precursor proteins
  JOURNAL   J Biol Chem 275 (44), 34552-34556 (2000)
   PUBMED   10942759
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Kitada,S., Shimokata,K., Niidome,T., Ogishima,T. and Ito,A.
  TITLE     A putative metal-binding site in the beta subunit of rat
            mitochondrial processing peptidase is essential for its catalytic
            activity
  JOURNAL   J Biochem 117 (6), 1148-1150 (1995)
   PUBMED   7490252
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Paces,V., Rosenberg,L.E., Fenton,W.A. and Kalousek,F.
  TITLE     The beta subunit of the mitochondrial processing peptidase from rat
            liver: cloning and sequencing of a cDNA and comparison with a
            proposed family of metallopeptidases
  JOURNAL   Proc Natl Acad Sci U S A 90 (11), 5355-5358 (1993)
   PUBMED   8506385
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Kitada,S., Niidome,T., Nagano,T., Ogishima,T. and Ito,A.
  TITLE     Molecular cloning of the smaller subunit(P52) of rat liver
            mitochondrial processing protease
  JOURNAL   Biochem Biophys Res Commun 190 (1), 289-293 (1993)
   PUBMED   8422255
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L12965.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L12965.1, BC078826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..489
                     /product="mitochondrial-processing peptidase subunit beta
                     precursor"
                     /EC_number="3.4.24.64"
                     /function="proteolytic removal of mitochondrial leader
                     peptides"
                     /note="mitochondrial-processing peptidase subunit beta;
                     P-52; beta-MPP; peptidase, mitochondrial processing beta
                     subunit; mitochondrial processing peptidase beta subunit;
                     peptidase (mitochondrial processing) beta"
                     /calculated_mol_wt=49424
     transit_peptide 1..45
                     /function="mitochondrial leader peptide"
                     /note="putative"
                     /calculated_mol_wt=4913
     mat_peptide     46..489
                     /product="mitochondrial-processing peptidase subunit beta"
                     /EC_number="3.4.24.64"
                     /function="proteolytic removal of mitochondrial leader
                     peptides"
                     /standard_name="betaMPP"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /calculated_mol_wt=49424
     Region          47..472
                     /region_name="PqqL"
                     /note="Predicted Zn-dependent peptidase, M16 family
                     [General function prediction only]; COG0612"
                     /db_xref="CDD:440377"
     Site            191
                     /site_type="other"
                     /note="Required for the specific determination of the
                     substrate cleavage site.
                     /evidence=ECO:0000269|PubMed:12433926; propagated from
                     UniProtKB/Swiss-Prot (Q03346.3)"
     Site            195
                     /site_type="other"
                     /note="Required for the specific determination of the
                     substrate cleavage site.
                     /evidence=ECO:0000269|PubMed:12433926; propagated from
                     UniProtKB/Swiss-Prot (Q03346.3)"
     CDS             1..489
                     /gene="Pmpcb"
                     /gene_synonym="Mppb"
                     /coded_by="NM_022395.2:17..1486"
                     /db_xref="GeneID:64198"
                     /db_xref="RGD:621297"
ORIGIN      
        1 maaaavsrtl lpvagrrlwg ftrrlplraa aaqplyfggd rlrstqaapq vvlnvpetqv
       61 tclenglrva sensgistct vglwidagsr yeneknngta hflehmafkg tkkrsqldle
      121 leienmgahl naytsreqtv yyakafskdl praveiladi iqnstlgeae ierergvilr
      181 emqevetnlq evvfdylhat ayqntalgrt ilgpteniks isrkdlvdyi tthykgpriv
      241 laaaggvchn ellelakfhf gdslcahkgd vpalppckft gseirvrddk mplahlavai
      301 eavgwthpdt irlmvantli gnwdrsfggg mnlssklaql tchgnlchsf qsfntsytdt
      361 glwglymvce qatvadmlha vqkewmrlct avsesevara knllktnmll qldgstpice
      421 digrqmlcyn rripipelea ridavdaemv revctkyiyg kspaiaalgp ierlpdfnqi
      481 csnmrwtrd
//
LOCUS       NP_001257593             248 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 11 [Rattus norvegicus].
ACCESSION   NP_001257593
VERSION     NP_001257593.1
DBSOURCE    REFSEQ: accession NM_001270664.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (11) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (11) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215694.1, FQ215316.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..248
                     /product="troponin T, fast skeletal muscle isoform 11"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29197
     Region          52..188
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..248
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270664.1:117..863"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eeaqeeevqe eapepeekpr pkltapkipe gekvdfddiq kkrqnkdlme
       61 lqalidshfe arkkeeeeli alkeriekrr aeraeqqrir aekererqnr laeekarree
      121 edakrraedd lkkkkalssm ganyssylak adqkrgkkqt aremkkkila errkplnidh
      181 lsddklrdka kelwdtlyql etdkfefgek lkrqkyditt lrsridqaqk hskkagatak
      241 gkvggrwk
//
LOCUS       NP_112283                215 aa            linear   ROD 27-APR-2025
DEFINITION  casein kinase II subunit beta [Rattus norvegicus].
ACCESSION   NP_112283
VERSION     NP_112283.1
DBSOURCE    REFSEQ: accession NM_031021.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Li,X., Yang,Q., Jiang,P., Wen,J., Chen,Y., Huang,J., Tian,M.,
            Ren,J. and Yang,Q.
  TITLE     Inhibition of CK2 Diminishes Fibrotic Scar Formation and Improves
            Outcomes After Ischemic Stroke via Reducing BRD4 Phosphorylation
  JOURNAL   Neurochem Res 49 (5), 1254-1267 (2024)
   PUBMED   38381246
  REMARK    GeneRIF: Inhibition of CK2 Diminishes Fibrotic Scar Formation and
            Improves Outcomes After Ischemic Stroke via Reducing BRD4
            Phosphorylation.
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Barak-Broner,N., Singer-Lahat,D., Chikvashvili,D. and Lotan,I.
  TITLE     CK2 Phosphorylation Is Required for Regulation of Syntaxin 1A
            Activity in Ca2+-Triggered Release in Neuroendocrine Cells
  JOURNAL   Int J Mol Sci 22 (24), 13556 (2021)
   PUBMED   34948351
  REMARK    GeneRIF: CK2 Phosphorylation Is Required for Regulation of Syntaxin
            1A Activity in Ca(2+)-Triggered Release in Neuroendocrine Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Becker,A., Gotz,C., Montenarh,M. and Philipp,S.E.
  TITLE     Control of TRPM3 Ion Channels by Protein Kinase CK2-Mediated
            Phosphorylation in Pancreatic beta-Cells of the Line INS-1
  JOURNAL   Int J Mol Sci 22 (23), 13133 (2021)
   PUBMED   34884938
  REMARK    GeneRIF: Control of TRPM3 Ion Channels by Protein Kinase
            CK2-Mediated Phosphorylation in Pancreatic beta-Cells of the Line
            INS-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Lee,S.W., Rho,J.H., Lee,S.Y., Yoo,S.H., Kim,H.Y., Chung,W.T. and
            Yoo,Y.H.
  TITLE     Alpha B-Crystallin Protects Rat Articular Chondrocytes against
            Casein Kinase II Inhibition-Induced Apoptosis
  JOURNAL   PLoS One 11 (11), e0166450 (2016)
   PUBMED   27851782
  REMARK    GeneRIF: alphaB-crystallin protects rat articular chondrocytes
            against CK2 inhibition-induced apoptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Liu,S., Gao,Y., Yu,X., Zhao,B., Liu,L., Zhao,Y., Luo,Z. and Shi,J.
  TITLE     Annexin-1 Mediates Microglial Activation and Migration via the CK2
            Pathway during Oxygen-Glucose Deprivation/Reperfusion
  JOURNAL   Int J Mol Sci 17 (10), 1770 (2016)
   PUBMED   27782092
  REMARK    GeneRIF: ANXA1 promotes microglial activation and migration during
            oxygen-glucose deprivation/reperfusion via FPR, and CK2 target
            alpha-E-catenin phosphorylation is involved in this process.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Kulikova,O.G. and Reikhardt,B.A.
  TITLE     Role of autophosphorylation in regulation of protein kinase CK2
            from rat neuronal chromatin
  JOURNAL   Biochemistry (Mosc) 63 (12), 1400-1406 (1998)
   PUBMED   9916157
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Sarrouilhe,D., Filhol,O., Leroy,D., Bonello,G., Baudry,M.,
            Chambaz,E.M. and Cochet,C.
  TITLE     The tight association of protein kinase CK2 with plasma membranes
            is mediated by a specific domain of its regulatory beta-subunit
  JOURNAL   Biochim Biophys Acta 1403 (2), 199-210 (1998)
   PUBMED   9630630
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Zhang,P., Davis,A.T. and Ahmed,K.
  TITLE     Mechanism of protein kinase CK2 association with nuclear matrix:
            role of disulfide bond formation
  JOURNAL   J Cell Biochem 69 (2), 211-220 (1998)
   PUBMED   9548568
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Pancetti,F., Bosser,R., Itarte,E. and Bachs,O.
  TITLE     Changes in the activity of nuclear protein kinase CK2 during rat
            liver regeneration
  JOURNAL   Biochem Biophys Res Commun 218 (1), 35-39 (1996)
   PUBMED   8573159
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Ahmed,K., Davis,A., Hanten,J., Lambert,D., McIvor,R.S. and
            Goueli,S.A.
  TITLE     Cloning of cDNAs encoding the alpha and beta subunits of rat casein
            kinase 2 (CK-2): investigation of molecular regulation of CK-2 by
            androgens in rat ventral prostate
  JOURNAL   Cell Mol Biol Res 39 (5), 451-462 (1993)
   PUBMED   8173590
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883045.1 and EV778558.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224491.1, FQ214437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..215
                     /product="casein kinase II subunit beta"
                     /EC_number="2.7.11.1"
                     /note="phosvitin; CK II beta; casein kinase II beta
                     subunit; casein kinase 2, beta subunit; casein kinase 2,
                     beta polypeptide; Csnk2b-Ly6g5b"
                     /calculated_mol_wt=24811
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P67870, ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Region          8..191
                     /region_name="CK_II_beta"
                     /note="Casein kinase II regulatory subunit; smart01085"
                     /db_xref="CDD:198153"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Region          147..150
                     /region_name="KSSR motif.
                     /evidence=ECO:0000250|UniProtKB:P67870"
                     /note="propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Region          188..193
                     /region_name="Interaction with alpha subunit"
                     /note="propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     CDS             1..215
                     /gene="Csnk2b"
                     /gene_synonym="Ck2"
                     /coded_by="NM_031021.3:131..778"
                     /db_xref="GeneID:81650"
                     /db_xref="RGD:619978"
ORIGIN      
        1 mssseevswi swfcglrgne ffcevdedyi qdkfnltgln eqvphyrqal dmildlepde
       61 elednpnqsd lieqaaemly gliharyilt nrgiaqmlek yqqgdfgycp rvycenqpml
      121 piglsdipge amvklycpkc mdvytpkssr hhhtdgayfg tgfphmlfmv hpeyrpkrpa
      181 nqfvprlygf kihpmayqlq lqaasnfksp vktir
//
LOCUS       NP_036965               1541 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-binding cassette sub-family C member 2 [Rattus norvegicus].
ACCESSION   NP_036965 XP_346594
VERSION     NP_036965.1
DBSOURCE    REFSEQ: accession NM_012833.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1541)
  AUTHORS   Zecchinati,F., Barranco,M.M., Tocchetti,G.N., Dominguez,C.J.,
            Arana,M.R., Perdomo,V.G., Mottino,A.D., Garcia,F. and
            Villanueva,S.S.M.
  TITLE     Multidrug resistance-associated protein 2 is negatively regulated
            by oxidative stress in rat intestine via a posttranslational
            mechanism. Impact on its membrane barrier function
  JOURNAL   Toxicology 460, 152873 (2021)
   PUBMED   34303734
  REMARK    GeneRIF: Multidrug resistance-associated protein 2 is negatively
            regulated by oxidative stress in rat intestine via a
            posttranslational mechanism. Impact on its membrane barrier
            function.
REFERENCE   2  (residues 1 to 1541)
  AUTHORS   Tocchetti,G.N., Dominguez,C.J., Zecchinati,F., Arana,M.R.,
            Rigalli,J.P., Ruiz,M.L., Villanueva,S.S.M. and Mottino,A.D.
  TITLE     Intraluminal nutrients acutely strengthen rat intestinal MRP2
            barrier function by a glucagon-like peptide-2-mediated mechanism
  JOURNAL   Acta Physiol (Oxf) 230 (4), e13514 (2020)
   PUBMED   32476256
  REMARK    GeneRIF: Intraluminal nutrients acutely strengthen rat intestinal
            MRP2 barrier function by a glucagon-like peptide-2-mediated
            mechanism.
REFERENCE   3  (residues 1 to 1541)
  AUTHORS   Tocchetti,G.N., Arias,A., Arana,M.R., Rigalli,J.P., Dominguez,C.J.,
            Zecchinati,F., Ruiz,M.L., Villanueva,S.S.M. and Mottino,A.D.
  TITLE     Acute regulation of multidrug resistance-associated protein 2
            localization and activity by cAMP and
            estradiol-17beta-D-glucuronide in rat intestine and Caco-2 cells
  JOURNAL   Arch Toxicol 92 (2), 777-788 (2018)
   PUBMED   29052767
  REMARK    GeneRIF: we demonstrate redistribution of intestinal MRP2 between
            plasma membrane and intracellular membrane in rat jejunum and in
            Caco-2 cells in response to db-cAMP and
            estradiol-17beta-D-glucuronide
REFERENCE   4  (residues 1 to 1541)
  AUTHORS   Qu,X., Zhang,Y., Zhang,S., Zhai,J., Gao,H., Tao,L. and Song,Y.
  TITLE     Dysregulation of BSEP and MRP2 May Play an Important Role in
            Isoniazid-Induced Liver Injury via the SIRT1/FXR Pathway in Rats
            and HepG2 Cells
  JOURNAL   Biol Pharm Bull 41 (8), 1211-1218 (2018)
   PUBMED   30068870
  REMARK    GeneRIF: In conclusion, our data supports the hypothesis that
            isoniazid can induce liver injury via the down-regulation of
            hepatic efflux transporters BSEP and MRP2, and the SIRT1/FXR
            pathway may be the primary regulator with regard to the expression
            of transporters and the biosynthesis of bile acids in the liver.
REFERENCE   5  (residues 1 to 1541)
  AUTHORS   Arana,M.R., Tocchetti,G.N., Zecchinati,F., Londero,A.S.,
            Dominguez,C., Perdomo,V., Rigalli,J.P., Villanueva,S.S.M. and
            Mottino,A.D.
  TITLE     Glucagon-like peptide 2 prevents down-regulation of intestinal
            multidrug resistance-associated protein 2 and P-glycoprotein in
            endotoxemic rats
  JOURNAL   Toxicology 390, 22-31 (2017)
   PUBMED   28842383
  REMARK    GeneRIF: GLP-2 can prevent down-regulation of intestinal expression
            and activity of Mrp2 and P-gp in endotoxemic rats.
REFERENCE   6  (residues 1 to 1541)
  AUTHORS   Zhang,Y., Li,W. and Vore,M.
  TITLE     Translational regulation of rat multidrug resistance-associated
            protein 2 expression is mediated by upstream open reading frames in
            the 5' untranslated region
  JOURNAL   Mol Pharmacol 71 (1), 377-383 (2007)
   PUBMED   17065236
REFERENCE   7  (residues 1 to 1541)
  AUTHORS   Buchler,M., Konig,J., Brom,M., Kartenbeck,J., Spring,H., Horie,T.
            and Keppler,D.
  TITLE     cDNA cloning of the hepatocyte canalicular isoform of the multidrug
            resistance protein, cMrp, reveals a novel conjugate export pump
            deficient in hyperbilirubinemic mutant rats
  JOURNAL   J Biol Chem 271 (25), 15091-15098 (1996)
   PUBMED   8662992
REFERENCE   8  (residues 1 to 1541)
  AUTHORS   Paulusma,C.C., Bosma,P.J., Zaman,G.J., Bakker,C.T., Otter,M.,
            Scheffer,G.L., Scheper,R.J., Borst,P. and Oude Elferink,R.P.
  TITLE     Congenital jaundice in rats with a mutation in a multidrug
            resistance-associated protein gene
  JOURNAL   Science 271 (5252), 1126-1128 (1996)
   PUBMED   8599091
REFERENCE   9  (residues 1 to 1541)
  AUTHORS   Mayer,R., Kartenbeck,J., Buchler,M., Jedlitschky,G., Leier,I. and
            Keppler,D.
  TITLE     Expression of the MRP gene-encoded conjugate export pump in liver
            and its selective absence from the canalicular membrane in
            transport-deficient mutant hepatocytes
  JOURNAL   J Cell Biol 131 (1), 137-150 (1995)
   PUBMED   7559771
REFERENCE   10 (residues 1 to 1541)
  AUTHORS   Kojima,H., Omoto,Y., Hidaka,H., Aoki,T., Nakamura,T., Kawabata,T.,
            Konaka,K., Kashiwagi,A., Kikkawa,R. and Shigeta,Y.
  TITLE     Increased plasma post-heparin diamine oxidase activity and plant
            sterol levels in streptozotocin diabetic rat
  JOURNAL   Biochem Biophys Res Commun 186 (1), 398-404 (1992)
   PUBMED   1632778
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1, L49379.1 and
            X96393.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346594.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X96393.1, D86086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            regulatory uORF        :: PMID: 17065236
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..1541
                     /product="ATP-binding cassette sub-family C member 2"
                     /EC_number="7.6.2.2"
                     /EC_number="7.6.2.3"
                     /note="canalicular multispecific organic anion transporter
                     1; canalicular multidrug resistance protein; cMrp2/cMoat
                     canalicular apical conjugate export pump; multidrug
                     resistance-associated protein 2; ATP-binding cassette,
                     sub-family C (CFTR/MRP), member 2; calicular multispecific
                     organic anion transporter; ATP-binding cassette, subfamily
                     C (CFTR/MRP), member 2"
                     /calculated_mol_wt=173253
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Region          7..1533
                     /region_name="MRP_assoc_pro"
                     /note="multi drug resistance-associated protein (MRP);
                     TIGR00957"
                     /db_xref="CDD:188098"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            434..454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            458..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            584..604
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Region          862..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            874
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Region          901..923
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92887; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92887; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            968..988
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1010
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1011
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1030..1050
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1094..1114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1116..1136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1208..1228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1231..1251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63120.1)"
     Site            1434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92887; propagated from
                     UniProtKB/Swiss-Prot (Q63120.1)"
     CDS             1..1541
                     /gene="Abcc2"
                     /gene_synonym="Cmoat; cMRP; mrp; Mrp2"
                     /coded_by="NM_012833.2:214..4839"
                     /db_xref="GeneID:25303"
                     /db_xref="RGD:2366"
ORIGIN      
        1 mdkfcnstfw dlsllespea dlplcfeqtv lvwiplgflw llapwqlysv yrsrtkrssi
       61 tkfylakqvf vvfllilaai dlslaltedt gqatvppvry tnpilylctw llvlavqhsr
      121 qwcvrknswf lslfwilsvl cgvfqfqtli rallkdsksn maysylffvs ygfqivllil
      181 tafsgpsdst qtpsvtasfl ssitfswydr tvlkgykhpl tledvwdide gfktrsvtsk
      241 feaamtkdlq karqafqrrl qksqrkpeat lhglnkkqsq sqdvlvleea kkksekttkd
      301 ypkswliksl fktfhvvilk sfilklihdl lvflnpqllk lligfvkssn syvwfgyica
      361 ilmfavtliq sfclqsyfqh cfvlgmcvrt tvmssiykka ltlsnlarkq ytigetvnlm
      421 svdsqklmda tnymqlvwss viqitlsiff lwrelgpsil agvgvmvlli pvngvlatki
      481 rniqvqnmkn kdkrlkimne ilsgikilky fawepsfqeq vqgirkkelk nllrfgqlqs
      541 llifilqitp ilvsvvtfsv yvlvdsanvl naekaftsit lfnilrfpls mlpmvtssil
      601 qasvsvdrle rylggddldt sairrvsnfd kavkfseasf twdpdleati qdvnldikpg
      661 qlvavvgtvg sgksslvsam lgemenvhgh itiqgstayv pqqswiqngt ikdnilfgse
      721 ynekkyqqvl kacallpdle ilpggdmaei gekginlsgg qkqrvslara ayqdadiyil
      781 ddplsavdah vgkhifnkvv gpngllagkt rifvthgihf lpqvdeivvl gkgtilekgs
      841 yrdlldkkgv farnwktfmk hsgpegeatv nndseaeddd dgliptmeei pedaaslamr
      901 renslrrtls rssrsssrrg kslknslkik nvnvlkekek evegqklikk efvetgkvkf
      961 siylkylqav gwwsilfiil fyglnnvafi gsnlwlsawt sdsdnlngtn nssshrdmri
     1021 gvfgalglaq gicllistlw siyacrnask alhgqlltni lrapmrffdt tptgrivnrf
     1081 sgdistvddl lpqtlrswmm cffgiagtlv micmatpvfa iiiiplsily isvqvfyvat
     1141 srqlrrldsv tkspiyshfs etvtglpiir afehqqrfla wnekqidinq kcvfswitsn
     1201 rwlairlelv gnlvvfcsal llviyrktlt gdvvgfvlsn alnitqtlnw lvrmtseaet
     1261 nivaverise yinveneapw vtdkrppadw prhgeiqfnn yqvryrpeld lvlkgitcni
     1321 ksgekvgvvg rtgagksslt nclfrilesa ggqiiidgid vasiglhdlr erltiipqdp
     1381 ilfsgslrmn ldpfnkysde evwralelah lrsfvsglql gllsevtegg dnlsigqrql
     1441 lclgravlrk skilvldeat aavdletdsl iqttirkefs qctvitiahr lhtimdsdki
     1501 mvldngkive ygspeellsn rgsfylmake agienvnhte l
//
LOCUS       NP_001104252             668 aa            linear   ROD 27-APR-2025
DEFINITION  synapsin-1 isoform b [Rattus norvegicus].
ACCESSION   NP_001104252
VERSION     NP_001104252.1
DBSOURCE    REFSEQ: accession NM_001110782.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Ma,W., Lu,K., Liang,H.M. and Zhang,J.Y.
  TITLE     Synapsin 1 Ameliorates Cognitive Impairment and Neuroinflammation
            in Rats with Alzheimer's Disease: An Experimental and
            Bioinformatics Study
  JOURNAL   Curr Alzheimer Res 20 (9), 648-659 (2023)
   PUBMED   38213171
  REMARK    GeneRIF: Synapsin 1 Ameliorates Cognitive Impairment and
            Neuroinflammation in Rats with Alzheimer's Disease: An Experimental
            and Bioinformatics Study.
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Yang,H.J., Chen,P.C., Huang,C.T., Cheng,T.L., Hsu,S.P., Chen,C.Y.,
            Lu,J.C. and Wang,C.T.
  TITLE     The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core
            Vesicle Release
  JOURNAL   J Neurosci 41 (13), 2828-2841 (2021)
   PUBMED   33632727
  REMARK    GeneRIF: The Phosphoprotein Synapsin Ia Regulates the Kinetics of
            Dense-Core Vesicle Release.
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Zhang,S., Yan,M.L., Yang,L., An,X.B., Zhao,H.M., Xia,S.N., Jin,Z.,
            Huang,S.Y., Qu,Y. and Ai,J.
  TITLE     MicroRNA-153 impairs hippocampal synaptic vesicle trafficking via
            downregulation of synapsin I in rats following chronic cerebral
            hypoperfusion
  JOURNAL   Exp Neurol 332, 113389 (2020)
   PUBMED   32580014
  REMARK    GeneRIF: MicroRNA-153 impairs hippocampal synaptic vesicle
            trafficking via downregulation of synapsin I in rats following
            chronic cerebral hypoperfusion.
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Tao-Cheng,J.H.
  TITLE     Immunogold labeling of synaptic vesicle proteins in developing
            hippocampal neurons
  JOURNAL   Mol Brain 13 (1), 9 (2020)
   PUBMED   31959215
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Liu,X., Zhang,R., Wu,Z., Si,W., Ren,Z., Zhang,S., Zhou,J. and
            Chen,D.
  TITLE     miR-134-5p/Foxp2/Syn1 is involved in cognitive impairment in an
            early vascular dementia rat model
  JOURNAL   Int J Mol Med 44 (5), 1729-1740 (2019)
   PUBMED   31545395
  REMARK    GeneRIF: The miR1345p/Foxp2/Syn1 axis was found to contribute to
            cognitive impairment in a chronic ischemiainduced early VD model,
            which may enable the development of new therapeutic strategies for
            the prevention and treatment of VD.
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Li,L., Chin,L.S., Shupliakov,O., Brodin,L., Sihra,T.S., Hvalby,O.,
            Jensen,V., Zheng,D., McNamara,J.O., Greengard,P. et al.
  TITLE     Impairment of synaptic vesicle clustering and of synaptic
            transmission, and increased seizure propensity, in synapsin
            I-deficient mice
  JOURNAL   Proc Natl Acad Sci U S A 92 (20), 9235-9239 (1995)
   PUBMED   7568108
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Cho,K.O., Hunt,C.A. and Kennedy,M.B.
  TITLE     The rat brain postsynaptic density fraction contains a homolog of
            the Drosophila discs-large tumor suppressor protein
  JOURNAL   Neuron 9 (5), 929-942 (1992)
   PUBMED   1419001
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Sudhof,T.C., Czernik,A.J., Kao,H.T., Takei,K., Johnston,P.A.,
            Horiuchi,A., Kanazir,S.D., Wagner,M.A., Perin,M.S., De Camilli,P.
            et al.
  TITLE     Synapsins: mosaics of shared and individual domains in a family of
            synaptic vesicle phosphoproteins
  JOURNAL   Science 245 (4925), 1474-1480 (1989)
   PUBMED   2506642
  REMARK    Review article
REFERENCE   9  (residues 1 to 668)
  AUTHORS   McCaffery,C.A. and DeGennaro,L.J.
  TITLE     Determination and analysis of the primary structure of the nerve
            terminal specific phosphoprotein, synapsin I
  JOURNAL   EMBO J 5 (12), 3167-3173 (1986)
   PUBMED   3028773
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Huttner,W.B., Schiebler,W., Greengard,P. and De Camilli,P.
  TITLE     Synapsin I (protein I), a nerve terminal-specific phosphoprotein.
            III. Its association with synaptic vesicles studied in a highly
            purified synaptic vesicle preparation
  JOURNAL   J Cell Biol 96 (5), 1374-1388 (1983)
   PUBMED   6404912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ084192.1, M27924.1, CO401107.1, JAXUCZ010000021.1 and BG378858.1.
            
            Transcript Variant: This variant (2) uses an alternate acceptor
            splice site at the 3' terminal exon compared to variant 1, which
            results in a frame-shift, and a shorter isoform (b) with a distinct
            C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M27924.1, SRR26643298.30806.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..668
                     /product="synapsin-1 isoform b"
                     /note="synapsin-1"
                     /calculated_mol_wt=69779
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          1..27
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK1 and PKA.
                     /evidence=ECO:0000305|PubMed:10571231; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          15..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          29..112
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            55
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            56
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000305|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            87
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            96
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            103
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000305|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          113..420
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          115..212
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          214..416
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Site            261
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          421..655
                     /region_name="D, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            428
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            430
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            474
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          <496..668
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            516
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            524
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            532
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            545
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17599; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P17600; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            554
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            562
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; Phosphoserine, by
                     CaMK2. /evidence=ECO:0000305|PubMed:3118371,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            576
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000305|PubMed:3118371; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            620
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     CDS             1..668
                     /gene="Syn1"
                     /coded_by="NM_001110782.2:99..2105"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:24949"
                     /db_xref="RGD:3797"
ORIGIN      
        1 mnylrrrlsd snfmanlpng ymtdlqrpqp pppppsaasp gatpgsaaas aerastaapv
       61 aspaapspgs sggggffssl snavkqttaa aaatfseqvg ggsggagrgg aaarvllvid
      121 ephtdwakyf kgkkihgeid ikveqaefsd lnlvahangg fsvdmevlrn gvkvvrslkp
      181 dfvlirqhaf smarngdyrs lviglqyagi psvnslhsvy nfcdkpwvfa qmvrlhkklg
      241 teefplidqt fypnhkemls sttypvvvkm ghahsgmgkv kvdnqhdfqd iasvvaltkt
      301 yataepfida kydvrvqkig qnykaymrts vsgnwktntg samleqiams dryklwvdtc
      361 seifggldic avealhgkdg rdhiievvgs smpligdhqd edkqlivelv vnkmtqalpr
      421 qrdaspgrgs hsqtpspgal plgrqtsqqp agppaqqrpp pqggppqpgp gpqrqgpplq
      481 qrpppqgqqh lsglgppags plpqrlpspt aapqqsasqa tpmtqgqgrq srpvaggpga
      541 ppaarppasp spqrqagppq atrqasisgp appkvsgasp ggqqrqgppq kppgpagpir
      601 qasqagpgpr tgppttqqpr psgpgpagrp tkpqlaqkps qdvpppiiaa aggpphpqlk
      661 aspaqaqp
//
LOCUS       NP_001257515             652 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier organic anion transporter family member 1B2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001257515
VERSION     NP_001257515.1
DBSOURCE    REFSEQ: accession NM_001270586.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Chen,S., Li,K., Jiang,J., Wang,X., Chai,Y., Zhang,C., Deng,Q.,
            Shuai,L., Feng,K., Ma,K. and Zhang,L.
  TITLE     Low expression of organic anion-transporting polypeptide 1B3
            predicts a poor prognosis in hepatocellular carcinoma
  JOURNAL   World J Surg Oncol 18 (1), 127 (2020)
   PUBMED   32534581
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Ma,X., Shang,X., Qin,X., Lu,J., Liu,M. and Wang,X.
  TITLE     Characterization of organic anion transporting polypeptide 1b2
            knockout rats generated by CRISPR/Cas9: a novel model for drug
            transport and hyperbilirubinemia disease
  JOURNAL   Acta Pharm Sin B 10 (5), 850-860 (2020)
   PUBMED   32528832
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Alam,K., Farasyn,T., Ding,K. and Yue,W.
  TITLE     Characterization of Liver- and Cancer-type-Organic Anion
            Transporting Polypeptide (OATP) 1B3 Messenger RNA Expression in
            Normal and Cancerous Human Tissues
  JOURNAL   Drug Metab Lett 12 (1), 24-32 (2018)
   PUBMED   29577869
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Verboom,M.C., Kloth,J.S.L., Swen,J.J., van der Straaten,T.,
            Bovee,J.V.M.G., Sleijfer,S., Reyners,A.K.L., Mathijssen,R.H.J.,
            Guchelaar,H.J., Steeghs,N. and Gelderblom,H.
  TITLE     Genetic polymorphisms in angiogenesis-related genes are associated
            with worse progression-free survival of patients with advanced
            gastrointestinal stromal tumours treated with imatinib
  JOURNAL   Eur J Cancer 86, 226-232 (2017)
   PUBMED   29054076
REFERENCE   5  (residues 1 to 652)
  AUTHORS   Sun,B., Chen,Y., Xiang,T., Zhang,L., Chen,Z., Zhang,S., Zhou,H. and
            Chen,S.
  TITLE     The Chinese Herb Jianpijiedu Contributes to the Regulation of
            OATP1B2 and ABCC2 in a Rat Model of Orthotopic Transplantation
            Liver Cancer Pretreated with Food Restriction and Diarrhea
  JOURNAL   Biomed Res Int 2015, 752850 (2015)
   PUBMED   26665149
REFERENCE   6  (residues 1 to 652)
  AUTHORS   Cattori,V., van Montfoort,J.E., Stieger,B., Landmann,L.,
            Meijer,D.K., Winterhalter,K.H., Meier,P.J. and Hagenbuch,B.
  TITLE     Localization of organic anion transporting polypeptide 4 (Oatp4) in
            rat liver and comparison of its substrate specificity with Oatp1,
            Oatp2 and Oatp3
  JOURNAL   Pflugers Arch 443 (2), 188-195 (2001)
   PUBMED   11713643
REFERENCE   7  (residues 1 to 652)
  AUTHORS   Ismair,M.G., Stieger,B., Cattori,V., Hagenbuch,B., Fried,M.,
            Meier,P.J. and Kullak-Ublick,G.A.
  TITLE     Hepatic uptake of cholecystokinin octapeptide by organic
            anion-transporting polypeptides OATP4 and OATP8 of rat and human
            liver
  JOURNAL   Gastroenterology 121 (5), 1185-1190 (2001)
   PUBMED   11677211
REFERENCE   8  (residues 1 to 652)
  AUTHORS   Choudhuri,S., Ogura,K. and Klaassen,C.D.
  TITLE     Cloning of the full-length coding sequence of rat liver-specific
            organic anion transporter-1 (rlst-1) and a splice variant and
            partial characterization of the rat lst-1 gene
  JOURNAL   Biochem Biophys Res Commun 274 (1), 79-86 (2000)
   PUBMED   10903899
REFERENCE   9  (residues 1 to 652)
  AUTHORS   Cattori,V., Hagenbuch,B., Hagenbuch,N., Stieger,B., Ha,R.,
            Winterhalter,K.E. and Meier,P.J.
  TITLE     Identification of organic anion transporting polypeptide 4 (Oatp4)
            as a major full-length isoform of the liver-specific transporter-1
            (rlst-1) in rat liver
  JOURNAL   FEBS Lett 474 (2-3), 242-245 (2000)
   PUBMED   10838093
REFERENCE   10 (residues 1 to 652)
  AUTHORS   Kakyo,M., Unno,M., Tokui,T., Nakagomi,R., Nishio,T., Iwasashi,H.,
            Nakai,D., Seki,M., Suzuki,M., Naitoh,T., Matsuno,S., Yawo,H. and
            Abe,T.
  TITLE     Molecular characterization and functional regulation of a novel rat
            liver-specific organic anion transporter rlst-1
  JOURNAL   Gastroenterology 117 (4), 770-775 (1999)
   PUBMED   10500057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF217450.2, AF147740.1 and JAXUCZ010000004.1.
            
            Transcript Variant: This variant (2, also known as rlst-1b) uses an
            alternate in-frame splice junction at the 3' end of an exon
            compared to variant 1. The resulting isoform (2) has the same N-
            and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.15359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..652
                     /product="solute carrier organic anion transporter family
                     member 1B2 isoform 2"
                     /note="solute carrier family 21 member 10;
                     sodium-independent organic anion-transporting polypeptide
                     4; solute carrier organic anion transporter family, member
                     1b3; solute carrier family 21 (organic anion transporter)
                     member 10; solute carrier family (organic anion
                     transporter) member 10; organic anion transporting
                     polypeptide 4; liver-specific transporter-1;
                     liver-specific organic anion transporter 1"
                     /calculated_mol_wt=72636
     Region          29..580
                     /region_name="OATP"
                     /note="Organic Anion Transporter Polypeptide (OATP)
                     family; pfam03137"
                     /db_xref="CDD:460821"
     CDS             1..652
                     /gene="Slco1b2"
                     /gene_synonym="OATP-4; Oatp4; rlst-1; Slc21a10; Slco1b3"
                     /coded_by="NM_001270586.1:115..2073"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:58978"
                     /db_xref="RGD:69300"
ORIGIN      
        1 mdhtqqsrka aeaqpsrskq trfcdgfklf laalsfsyic kalggvvmks sitqierrfd
       61 ipssisglid ggfeignllv ivfvsyfgsk lhrpkligig cfimgigsil talphffmgy
      121 ykyakendig slgnstltcf inqmtsptgp speivekgce kglkshmwiy vlmgnmlrgi
      181 getpivplgi sylddfakeg htsmhlgtlh tiamigpilg fimssvfaki yvdvgyvdln
      241 svritpndar wvgawwlsfi vngllcitss ipffflpkip krsqeerkns vslhapktde
      301 ekkhmtnltk qeeqdpsnmt gflrslrsil tneiyvifli ltllqvsgfi gsftylfkfi
      361 eqqfgrtasq anfllgiiti ptmatamflg gyivkkfklt svgiakmnpv dshidvplsy
      421 cnsdcscdkn qwepicgeng vtyispclag cksfrgdkkp nntefydcsc isnsgnnsah
      481 lgecprykck tnyyfyiilq vtvsfftamg spslililmk svqpelksla mgfhsliira
      541 lggilapiyy gafidrtcik wsvtscgkrg acrlynsrlf gfsylglnla lktpplflyv
      601 vliyftkrky krndnktlen grqftdegnp dsvnkngyyc vpydeqsnet pl
//
LOCUS       NP_446083                 89 aa            linear   ROD 27-APR-2025
DEFINITION  barrier-to-autointegration factor [Rattus norvegicus].
ACCESSION   NP_446083
VERSION     NP_446083.1
DBSOURCE    REFSEQ: accession NM_053631.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Shen,Q., Eun,J.W., Lee,K., Kim,H.S., Yang,H.D., Kim,S.Y., Lee,E.K.,
            Kim,T., Kang,K., Kim,S., Min,D.H., Oh,S.N., Lee,Y.J., Moon,H.,
            Ro,S.W., Park,W.S., Lee,J.Y. and Nam,S.W.
  TITLE     Barrier to autointegration factor 1, procollagen-lysine,
            2-oxoglutarate 5-dioxygenase 3, and splicing factor 3b subunit 4 as
            early-stage cancer decision markers and drivers of hepatocellular
            carcinoma
  JOURNAL   Hepatology 67 (4), 1360-1377 (2018)
   PUBMED   29059470
  REMARK    Erratum:[Hepatology. 2018 Jul;68(1):391. doi: 10.1002/hep.30114.
            PMID: 29975814]
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Kim,W., Chakraborty,G., Kim,S., Shin,J., Park,C.H., Jeong,M.W.,
            Bharatham,N., Yoon,H.S. and Kim,K.T.
  TITLE     Macro histone H2A1.2 (macroH2A1) protein suppresses mitotic kinase
            VRK1 during interphase
  JOURNAL   J Biol Chem 287 (8), 5278-5289 (2012)
   PUBMED   22194607
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Brachner,A., Braun,J., Ghodgaonkar,M., Castor,D., Zlopasa,L.,
            Ehrlich,V., Jiricny,J., Gotzmann,J., Knasmuller,S. and Foisner,R.
  TITLE     The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA
            cleavage in vivo
  JOURNAL   J Cell Sci 125 (Pt 4), 1048-1057 (2012)
   PUBMED   22399800
REFERENCE   4  (residues 1 to 89)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Wiebe,M.S. and Traktman,P.
  TITLE     Poxviral B1 kinase overcomes barrier to autointegration factor, a
            host defense against virus replication
  JOURNAL   Cell Host Microbe 1 (3), 187-197 (2007)
   PUBMED   18005698
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Bradley,C.M., Ronning,D.R., Ghirlando,R., Craigie,R. and Dyda,F.
  TITLE     Structural basis for DNA bridging by barrier-to-autointegration
            factor
  JOURNAL   Nat Struct Mol Biol 12 (10), 935-936 (2005)
   PUBMED   16155580
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Dechat,T., Gajewski,A., Korbei,B., Gerlich,D., Daigle,N.,
            Haraguchi,T., Furukawa,K., Ellenberg,J. and Foisner,R.
  TITLE     LAP2alpha and BAF transiently localize to telomeres and specific
            regions on chromatin during nuclear assembly
  JOURNAL   J Cell Sci 117 (Pt 25), 6117-6128 (2004)
   PUBMED   15546916
  REMARK    GeneRIF: LAP2alpha and BAF transiently localize to telomeres and
            specific regions on chromatin during nuclear assembly
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Furukawa,K.
  TITLE     LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of
            LAP2-chromatin interaction
  JOURNAL   J Cell Sci 112 (Pt 15), 2485-2492 (1999)
   PUBMED   10393804
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Lee,M.S. and Craigie,R.
  TITLE     A previously unidentified host protein protects retroviral DNA from
            autointegration
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1528-1533 (1998)
   PUBMED   9465049
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB766065.1, BC084726.1 and JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084726.1, DV722875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..89
                     /product="barrier-to-autointegration factor"
                     /note="Lap2 binding protein 1; breakpoint cluster region
                     protein 1; BAF nuclear assembly factor 1; LAP2-binding
                     protein 1; barrier to autointegration factor 1; Breakpoint
                     cluster region protein, uterine leiomyoma, 1; barrier to
                     autointegration factor"
                     /calculated_mol_wt=9913
     Region          1..88
                     /region_name="BAF"
                     /note="Barrier to autointegration factor; pfam02961"
                     /db_xref="CDD:460766"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O75531; propagated from
                     UniProtKB/Swiss-Prot (Q9R1T1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Barrier-to-autointegration
                     factor, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:O75531; propagated from
                     UniProtKB/Swiss-Prot (Q9R1T1.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by VRK1 and VRK2.
                     /evidence=ECO:0000250|UniProtKB:O75531; propagated from
                     UniProtKB/Swiss-Prot (Q9R1T1.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by VRK1 and VRK2.
                     /evidence=ECO:0000250|UniProtKB:O75531; propagated from
                     UniProtKB/Swiss-Prot (Q9R1T1.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by VRK1 and VRK2.
                     /evidence=ECO:0000250|UniProtKB:O75531; propagated from
                     UniProtKB/Swiss-Prot (Q9R1T1.1)"
     CDS             1..89
                     /gene="Banf1"
                     /gene_synonym="Baf; Bcrp1; L2bp1; L2bp1/Baf"
                     /coded_by="NM_053631.3:98..367"
                     /db_xref="GeneID:114087"
                     /db_xref="RGD:620662"
ORIGIN      
        1 mttsqkhrdf vaepmgekpv gslagigdal gkrleergfd kayvvlgqfl vlkkdedlfr
       61 ewlkdtcgan akqsrdcfgc lrewcdafl
//
LOCUS       NP_001264531             293 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein C isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001264531
VERSION     NP_001264531.1
DBSOURCE    REFSEQ: accession NM_001277602.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Liu,N., Dai,Q., Zheng,G., He,C., Parisien,M. and Pan,T.
  TITLE     N(6)-methyladenosine-dependent RNA structural switches regulate
            RNA-protein interactions
  JOURNAL   Nature 518 (7540), 560-564 (2015)
   PUBMED   25719671
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Todd,M.A. and Picketts,D.J.
  TITLE     PHF6 interacts with the nucleosome remodeling and deacetylation
            (NuRD) complex
  JOURNAL   J Proteome Res 11 (8), 4326-4337 (2012)
   PUBMED   22720776
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Raffalli-Mathieu,F., Geneste,O. and Lang,M.A.
  TITLE     Characterization of two nuclear proteins that interact with
            cytochrome P-450 1A2 mRNA. Regulation of RNA binding and possible
            role in the expression of the Cyp1a2 gene
  JOURNAL   Eur J Biochem 245 (1), 17-24 (1997)
   PUBMED   9128719
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Sharp,Z.D., Smith,K.P., Cao,Z.D. and Helsel,S.
  TITLE     Cloning of the nucleic acid-binding domain of the rat HnRNP C-type
            protein
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 306-309 (1990)
   PUBMED   2088340
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            two alternate in-frame splice sites in the coding region compared
            to variant 1. It encodes isoform 3 which is shorter compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2221236.1,
                                           SRR26360186.239873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..293
                     /product="heterogeneous nuclear ribonucleoprotein C
                     isoform 3"
                     /note="hnRNP C protein C-terminal fragment (158 AA); hnRNP
                     core protein C; heterogeneous nuclear ribonucleoprotein C
                     (C1/C2); heterogeneous nuclear ribonucleoproteins C1/C2"
                     /calculated_mol_wt=32191
     Region          10..93
                     /region_name="RRM_hnRNPC"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP
                     C1/C2); cd12603"
                     /db_xref="CDD:410015"
     CDS             1..293
                     /gene="Hnrnpc"
                     /gene_synonym="hnRNP C; Hnrpc"
                     /coded_by="NM_001277602.1:191..1072"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:290046"
                     /db_xref="RGD:1309982"
ORIGIN      
        1 masnvtnktd prsmnsrvfi gnlntlvvkk sdveaifsky gkivgcsvhk gfafvqyvne
       61 rnaraavage dgrmiagqvl dinlaaepkv nrgkagvkrs aaemygssfd ldydfqrdyy
      121 drmysyparv pppppiarav vpskrqrvsg ntsrrgksgf nsksgqrgss sksgklkgdd
      181 lqaikkeltq ikqkvdslle slekiekeqs kqavemknek seeeqssasv kkdetnvkme
      241 seagaddsae egdllddddn edrgddqlel kddekepeeg eddrdsange dds
//
LOCUS       NP_001020042             388 aa            linear   ROD 27-APR-2025
DEFINITION  rab9 effector protein with kelch motifs [Rattus norvegicus].
ACCESSION   NP_001020042 XP_216042
VERSION     NP_001020042.2
DBSOURCE    REFSEQ: accession NM_001024871.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097415.1.
            
            On Jun 20, 2015 this sequence version replaced NP_001020042.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097415.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..388
                     /product="rab9 effector protein with kelch motifs"
                     /note="Rab9 effector p40"
                     /calculated_mol_wt=41700
     Region          29..282
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          102..151
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          155..206
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          209..254
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          272..317
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..388
                     /gene="Rabepk"
                     /coded_by="NM_001024871.1:384..1550"
                     /db_xref="GeneID:296649"
                     /db_xref="RGD:1310612"
ORIGIN      
        1 mptctqfqaa ltnlgtmkql pilepgdkpr kaawytltcp gdkpcprvgh scsyfppvge
       61 aekgkvfivg ganpnqsfsd vhtmdlgthr wdtatregll pryehasflp scsphsiwvf
      121 ggadqsgnrn clqvmnpear twstpevtgc ppsprtfhts saaignhlyv fgggergaqp
      181 vqdvklhvfd antltwaqpe thgsppsprh ghamvaagtk lfihgglagd rffddlhcid
      241 igdmswqklg ptgtapvgca ahaavavghh vyvfggmtat galntmykyh tekqhwtilq
      301 fdtslppgrl dhsmcvipwp vmsasdteds gsvilslqde kgdaaekpet rsggsreesp
      361 ttlllcfvfg gmntegeiyd dclvtvvd
//
LOCUS       NP_001004099             226 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction beta-2 protein [Rattus norvegicus].
ACCESSION   NP_001004099 XP_237945
VERSION     NP_001004099.1
DBSOURCE    REFSEQ: accession NM_001004099.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Moscato,S., Cabiati,M., Bianchi,F., Panetta,D., Burchielli,S.,
            Massimetti,G., Del Ry,S. and Mattii,L.
  TITLE     Heart and liver connexin expression related to the first stage of
            aging: A study on naturally aged animals
  JOURNAL   Acta Histochem 122 (8), 151651 (2020)
   PUBMED   33171391
  REMARK    GeneRIF: Heart and liver connexin expression related to the first
            stage of aging: A study on naturally aged animals.
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Lin,J., Huang,H., Lv,G., Xu,X., Lin,W., Xu,X., Cheng,J. and
            Zheng,M.
  TITLE     Chronic prenatal hypoxia impairs cochlear development, a mechanism
            involving connexin26 expression and promoter methylation
  JOURNAL   Int J Mol Med 41 (2), 852-858 (2018)
   PUBMED   29207085
  REMARK    GeneRIF: These results demonstrate that chronic prenatal hypoxia
            caused hearing impairment, and suggest that promoter region
            hypermethylation and expression downregulation of Cx26 underlie the
            mechanism of action
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Santolim,L.V., Amaral,M.E.C.D., Fachi,J.L., Mendes,M.F. and
            Oliveira,C.A.
  TITLE     Vitamin E and caloric restriction promote hepatic homeostasis
            through expression of connexin 26, N-cad, E-cad and cholesterol
            metabolism genes
  JOURNAL   J Nutr Biochem 39, 86-92 (2017)
   PUBMED   27816814
  REMARK    GeneRIF: Supplementation with vitamin E, with or without caloric
            restriction, upregulated the mRNA expression of Cx26, N-cad, E-cad
            and genes involved in cholesterol metabolism, suggesting the
            maintenance of hepatic homeostasis.
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Pinto,B.I., Garcia,I.E., Pupo,A., Retamal,M.A., Martinez,A.D.,
            Latorre,R. and Gonzalez,C.
  TITLE     Charged Residues at the First Transmembrane Region Contribute to
            the Voltage Dependence of the Slow Gate of Connexins
  JOURNAL   J Biol Chem 291 (30), 15740-15752 (2016)
   PUBMED   27143357
  REMARK    GeneRIF: the role of the charged residues at the end of TM-1 in
            voltage sensing in Cx26, Cx46, and Cx50.
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Adam,C. and Cyr,D.G.
  TITLE     Role of Specificity Protein-1 and Activating Protein-2
            Transcription Factors in the Regulation of the Gap Junction Protein
            Beta-2 Gene in the Epididymis of the Rat
  JOURNAL   Biol Reprod 94 (6), 120 (2016)
   PUBMED   27053364
  REMARK    GeneRIF: SP1 and TFAP2A regulate Gjb2 promoter activity during
            epididymal differentiation in rat.
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Bennett,B.C., Purdy,M.D., Baker,K.A., Acharya,C., McIntire,W.E.,
            Stevens,R.C., Zhang,Q., Harris,A.L., Abagyan,R. and Yeager,M.
  TITLE     An electrostatic mechanism for Ca(2+)-mediated regulation of gap
            junction channels
  JOURNAL   Nat Commun 7, 8770 (2016)
   PUBMED   26753910
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Sakamoto,H., Oyamada,M., Enomoto,K. and Mori,M.
  TITLE     Differential changes in expression of gap junction proteins
            connexin 26 and 32 during hepatocarcinogenesis in rats
  JOURNAL   Jpn J Cancer Res 83 (11), 1210-1215 (1992)
   PUBMED   1336494
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Winterhager,E., Stutenkemper,R., Traub,O., Beyer,E. and Willecke,K.
  TITLE     Expression of different connexin genes in rat uterus during
            decidualization and at term
  JOURNAL   Eur J Cell Biol 55 (1), 133-142 (1991)
   PUBMED   1655436
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Zhang,J.T. and Nicholson,B.J.
  TITLE     Sequence and tissue distribution of a second protein of hepatic gap
            junctions, Cx26, as deduced from its cDNA
  JOURNAL   J Cell Biol 109 (6 Pt 2), 3391-3401 (1989)
   PUBMED   2557354
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Nicholson,B., Dermietzel,R., Teplow,D., Traub,O., Willecke,K. and
            Revel,J.P.
  TITLE     Two homologous protein components of hepatic gap junctions
  JOURNAL   Nature 329 (6141), 732-734 (1987)
   PUBMED   2823143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC078952.1.
            
            On Sep 4, 2004 this sequence version replaced XP_237945.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078952.1, SRR26643287.31524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840116, SAMN12840127
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..226
                     /product="gap junction beta-2 protein"
                     /note="gap junction channel protein connexin 26; gap
                     junction membrane channel protein beta 2; connexin e"
                     /calculated_mol_wt=26320
     Region          2..215
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21994.1)"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21994.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21994.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21994.1)"
     CDS             1..226
                     /gene="Gjb2"
                     /gene_synonym="Cx26; CXN-26; Cxne"
                     /coded_by="NM_001004099.2:290..970"
                     /db_xref="GeneID:394266"
                     /db_xref="RGD:728891"
ORIGIN      
        1 mdwgtlqsil ggvnkhstsi gkiwltvlfi frimilvvaa kevwgdeqad fvcntlqpgc
       61 knvcydhyfp ishirlwalq limvstpall vamhvayrrh ekkrkfmkge iknefkdiee
      121 iktqkvrieg slwwtyttsi ffrvifeavf myvfyimyng ffmqrlvkcn awpcpntvdc
      181 fisrptektv ftvfmisvsg icillnitel cylfirycsg kskrpv
//
LOCUS       NP_001257606             244 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 12 [Rattus norvegicus].
ACCESSION   NP_001257606
VERSION     NP_001257606.1
DBSOURCE    REFSEQ: accession NM_001270677.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (12) lacks three alternate
            in-frame exons compared to variant 1. The resulting isoform (12)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760386,
                              SAMEA5760475 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..244
                     /product="troponin T, fast skeletal muscle isoform 12"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=28803
     Region          48..184
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..244
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270677.1:117..851"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eeaqeeeevq eeekprpklt apkipegekv dfddiqkkrq nkdlmelqal
       61 idshfearkk eeeelialke riekrraera eqqriraeke rerqnrlaee karreeedak
      121 rraeddlkkk kalssmgany ssylakadqk rgkkqtarem kkkilaerrk plnidhlsdd
      181 klrdkakelw dtlyqletdk fefgeklkrq kydittlrsr idqaqkhskk agatakgkvg
      241 grwk
//
LOCUS       NP_598200                123 aa            linear   ROD 27-APR-2025
DEFINITION  seminal vesicle secretory protein 5 precursor [Rattus norvegicus].
ACCESSION   NP_598200
VERSION     NP_598200.1
DBSOURCE    REFSEQ: accession NM_133516.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Williams,L., McDonald,C. and Higgins,S.
  TITLE     Sequence organisation of rat seminal vesicle F gene: location of
            transcriptional start point and sequence comparison with six other
            androgen-regulated genes
  JOURNAL   Nucleic Acids Res 13 (3), 659-672 (1985)
   PUBMED   2987804
REFERENCE   2  (residues 1 to 123)
  AUTHORS   McDonald,C.J., Eliopoulos,E. and Higgins,S.J.
  TITLE     Divergent protein coding regions in otherwise closely related
            androgen-regulated mRNAs
  JOURNAL   EMBO J 3 (11), 2517-2521 (1984)
   PUBMED   6548962
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Harris,S.E., Mansson,P.E., Tully,D.B. and Burkhart,B.
  TITLE     Seminal vesicle secretion IV gene: allelic difference due to a
            series of 20-base-pair direct tandem repeats within an intron
  JOURNAL   Proc Natl Acad Sci U S A 80 (21), 6460-6464 (1983)
   PUBMED   6579532
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X01115.1, SRR26643297.14320.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..123
                     /product="seminal vesicle secretory protein 5 precursor"
                     /note="SVS V; SVS protein F; seminal vesicle secretory
                     protein V; seminal vesicle secretion 5"
                     /calculated_mol_wt=11428
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2210
     mat_peptide     22..123
                     /product="Seminal vesicle secretory protein 5.
                     /id=PRO_0000022455"
                     /note="propagated from UniProtKB/Swiss-Prot (P04812.1)"
                     /calculated_mol_wt=11428
     Region          24..122
                     /region_name="Svs_4_5_6"
                     /note="Seminal vesicle secretory proteins 4/5/6;
                     pfam17381"
                     /db_xref="CDD:375165"
     Region          50..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04812.1)"
     CDS             1..123
                     /gene="Svs5"
                     /coded_by="NM_133516.2:23..394"
                     /db_xref="GeneID:171027"
                     /db_xref="RGD:620290"
ORIGIN      
        1 msptgffllt vllvlvteaa srgprekfsq saedpysenm nlkilasgrg ssstfgaysr
       61 sensrsnfks kspssitrek vneesrsems stsshfglkm rrshgggemn pfetkvktri
      121 trk
//
LOCUS       NP_001257901            1074 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger RNA-binding protein [Rattus norvegicus].
ACCESSION   NP_001257901 XP_345170
VERSION     NP_001257901.1
DBSOURCE    REFSEQ: accession NM_001270972.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 1074)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 1074)
  AUTHORS   Elvira,G., Massie,B. and DesGroseillers,L.
  TITLE     The zinc-finger protein ZFR is critical for Staufen 2 isoform
            specific nucleocytoplasmic shuttling in neurons
  JOURNAL   J Neurochem 96 (1), 105-117 (2006)
   PUBMED   16277607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Aug 16, 2012 this sequence version replaced XP_345170.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.2702.1,
                                           SRR26643288.8794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q16"
     Protein         1..1074
                     /product="zinc finger RNA-binding protein"
                     /calculated_mol_wt=116783
     Region          331..360
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          333..355
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(340..342,344..345,349,354,389,392..396,398..399)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          382..>551
                     /region_name="PHA03255"
                     /note="BDLF3; Provisional"
                     /db_xref="CDD:165513"
     Region          384..413
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          384..406
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          581..612
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          584..606
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          784..1038
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     CDS             1..1074
                     /gene="Zfr"
                     /coded_by="NM_001270972.1:243..3467"
                     /db_xref="GeneID:365703"
                     /db_xref="RGD:1311890"
ORIGIN      
        1 mipicpvvsf tyvpsrlged akmatgnyfg fthsgaaaaa aaaqysqqpa sgvayshptt
       61 vasytvhqap vaahtvtaay apaaatvava rpapvavaaa ataaayggyp tahtatdygy
      121 tqrqqeappp pppattqnyq dsysyvrsta pavaydskqy yqqptataaa vaaaaqpqps
      181 vaetyyqtap kagysqgatq ytqaqqarqv taikpatpsp atttfsiypv sstvqpvaaa
      241 atvvpsytqs atysttavty sgtsysgyea avysaassyy qqqqqqqkqa aaaaaaaaat
      301 aawtgttftk ktpfqnkqlk pkqppkppqi hycdvckisc agpqtykehl egqkhkkkea
      361 alkasqntss snnstrgtqn qlrcelcdvs ctgadayaah irgakhqkvv klhtklgkpi
      421 pstepnvvsq atsstavsas kptaspssig asnctlntss iattsvkgls ttgnsslnst
      481 sntkvsavpt nmaakktstp kinfvggnkl qstgnkaedl kgtdciknnp aasavqipev
      541 kqdavsepvt paslaalqsd vqpvghdyve evrndegkvi rfhcklcecs fndpnakemh
      601 lkgrrhrlqy kkkvnpdlqv evkpsirark iqeekmrkqm qkeeywrrre eeerwrmeir
      661 ryeedmywrr meeeqhhwdd rrrmpdggyp hgppgplgll gvrpgmppqp qgpaplrrpd
      721 ssddryvmtk hatiypteee lqavqkivsi teralklvsd slsehekskn kegddkkegg
      781 kdralkgvlr vgvlakglll rgdrnvnlvl lcsekpsksl lsriaenlpk qlavispeky
      841 dikcavseaa iilnscvepk mqvtitltsp iireenmreg dvtsgmvkdp pdvldrqkcl
      901 dalaalrhak wfqaranglq scviiirilr dlcqrvptws dfpswamell vekaissass
      961 pqspgdalrr vfecissgii lkgspglldp cekdpfdtla tmtdqqredi tssaqfalrl
     1021 lafrqihkvl gmdplpqmnq rfnihnnrkr rrdsdgvdgf eaegkkdkkd ydnf
//
LOCUS       NP_001017454             366 aa            linear   ROD 27-APR-2025
DEFINITION  IST1 homolog [Rattus norvegicus].
ACCESSION   NP_001017454 XP_226448
VERSION     NP_001017454.1
DBSOURCE    REFSEQ: accession NM_001017454.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gu,M., LaJoie,D., Chen,O.S., von Appen,A., Ladinsky,M.S.,
            Redd,M.J., Nikolova,L., Bjorkman,P.J., Sundquist,W.I., Ullman,K.S.
            and Frost,A.
  TITLE     LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in
            fission yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 114 (11), E2166-E2175 (2017)
   PUBMED   28242692
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Lee,S., Chang,J., Renvoise,B., Tipirneni,A., Yang,S. and
            Blackstone,C.
  TITLE     MITD1 is recruited to midbodies by ESCRT-III and participates in
            cytokinesis
  JOURNAL   Mol Biol Cell 23 (22), 4347-4361 (2012)
   PUBMED   23015756
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Renvoise,B., Stadler,J., Singh,R., Bakowska,J.C. and Blackstone,C.
  TITLE     Spg20-/- mice reveal multimodal functions for Troyer syndrome
            protein spartin in lipid droplet maintenance, cytokinesis and BMP
            signaling
  JOURNAL   Hum Mol Genet 21 (16), 3604-3618 (2012)
   PUBMED   22619377
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Li,Y., Zhang,Y., Qiu,F. and Qiu,Z.
  TITLE     Proteomic identification of exosomal LRG1: a potential urinary
            biomarker for detecting NSCLC
  JOURNAL   Electrophoresis 32 (15), 1976-1983 (2011)
   PUBMED   21557262
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Agromayor,M., Carlton,J.G., Phelan,J.P., Matthews,D.R.,
            Carlin,L.M., Ameer-Beg,S., Bowers,K. and Martin-Serrano,J.
  TITLE     Essential role of hIST1 in cytokinesis
  JOURNAL   Mol Biol Cell 20 (5), 1374-1387 (2009)
   PUBMED   19129480
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Bajorek,M., Morita,E., Skalicky,J.J., Morham,S.G., Babst,M. and
            Sundquist,W.I.
  TITLE     Biochemical analyses of human IST1 and its function in cytokinesis
  JOURNAL   Mol Biol Cell 20 (5), 1360-1373 (2009)
   PUBMED   19129479
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1 and BC092631.1.
            
            On Apr 29, 2005 this sequence version replaced XP_226448.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092631.1, SRR26643292.61473.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..366
                     /product="IST1 homolog"
                     /note="MAPK activating protein PM28; IST1, ESCRT-III
                     associated factor; increased sodium tolerance 1 homolog;
                     charged multivesicular body protein 8"
                     /calculated_mol_wt=39811
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53990; propagated from
                     UniProtKB/Swiss-Prot (Q568Z6.1)"
     Region          12..176
                     /region_name="Ist1"
                     /note="Regulator of Vps4 activity in the MVB pathway;
                     pfam03398"
                     /db_xref="CDD:460910"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P53990; propagated from
                     UniProtKB/Swiss-Prot (Q568Z6.1)"
     Region          297..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q568Z6.1)"
     CDS             1..366
                     /gene="Ist1"
                     /gene_synonym="CHMP8; RGD1307799"
                     /coded_by="NM_001017454.2:112..1212"
                     /db_xref="GeneID:307833"
                     /db_xref="RGD:1307799"
ORIGIN      
        1 mlgsgfkaer lrvnlrlvin rlkllekkkt elaqkarkei adylaagkde rarirvehii
       61 redylveame ilelycdlll arfgliqsmk eldsglaesv stliwaaprl qsevaelkiv
      121 adqlcakysk eygklcrtnq igtvndrlmh klsveappki lverylieia knynvpyepd
      181 svvmaeapvg vetdlidvgf tddvkkggpg rgggggftap vgapdgtmpm pmpmpmpmps
      241 pspnapfayp lpkgpsdfsg lpvgtyqafp nihppqipat ppsyesvddi nadknvssaq
      301 ivgpkpeapa kppsrpvdny ntfvlpelps vpdtlptasa gastsasedi dfddlsrrfe
      361 elkkkt
//
LOCUS       NP_620183                312 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein E precursor [Rattus norvegicus].
ACCESSION   NP_620183
VERSION     NP_620183.2
DBSOURCE    REFSEQ: accession NM_138828.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lee,B.H., Cevizci,M., Lieblich,S.E., Ibrahim,M., Wen,Y., Eid,R.S.,
            Lamers,Y., Duarte-Guterman,P. and Galea,L.A.M.
  TITLE     Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age
  JOURNAL   Brain Behav Immun 120, 54-70 (2024)
   PUBMED   38772427
  REMARK    GeneRIF: Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Chen,H., Zhao,S., Jian,Q., Yan,Y., Wang,S., Zhang,X. and Ji,Y.
  TITLE     The role of ApoE in fatty acid transport from neurons to astrocytes
            under ischemia/hypoxia conditions
  JOURNAL   Mol Biol Rep 51 (1), 320 (2024)
   PUBMED   38393618
  REMARK    GeneRIF: The role of ApoE in fatty acid transport from neurons to
            astrocytes under ischemia/hypoxia conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Matsuo,H., Kawakami,K., Ohara,H., Kaneko,T., Mashimo,T., Yamada,T.
            and Nabika,T.
  TITLE     Apolipoprotein E-depletion accelerates arterial fat deposition in
            the spontaneously hypertensive rat
  JOURNAL   Exp Anim 72 (4), 439-445 (2023)
   PUBMED   37081644
  REMARK    GeneRIF: Apolipoprotein E-depletion accelerates arterial fat
            deposition in the spontaneously hypertensive rat.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Jiang,C., Chen,Z., Wang,X., Zhang,Y., Guo,X., Fan,H., Huang,D.,
            He,Y., Tang,X., Ai,Y., Liu,Y., Yang,H. and Hao,D.
  TITLE     Curcumin-activated Olfactory Ensheathing Cells Improve Functional
            Recovery After Spinal Cord Injury by Modulating Microglia
            Polarization Through APOE/TREM2/NF-kappaB Signaling Pathway
  JOURNAL   J Neuroimmune Pharmacol 18 (3), 476-494 (2023)
   PUBMED   37658943
  REMARK    GeneRIF: Curcumin-activated Olfactory Ensheathing Cells Improve
            Functional Recovery After Spinal Cord Injury by Modulating
            Microglia Polarization Through APOE/TREM2/NF-kappaB Signaling
            Pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Nguyen,T.D., Watanabe,A., Burleigh,S., Ghaffarzadegan,T.,
            Kanklai,J., Prykhodko,O., Hallenius,F.F. and Nyman,M.
  TITLE     Monobutyrin and monovalerin improve gut-blood-brain biomarkers and
            alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats
  JOURNAL   Sci Rep 12 (1), 15454 (2022)
   PUBMED   36104381
  REMARK    GeneRIF: Monobutyrin and monovalerin improve gut-blood-brain
            biomarkers and alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Takahashi,S., Kawarabayasi,Y., Nakai,T., Sakai,J. and Yamamoto,T.
  TITLE     Rabbit very low density lipoprotein receptor: a low density
            lipoprotein receptor-like protein with distinct ligand specificity
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9252-9256 (1992)
   PUBMED   1384047
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Feussner,G., Funke,H., Weng,W., Assmann,G., Lackner,K.J. and
            Ziegler,R.
  TITLE     Severe type III hyperlipoproteinemia associated with unusual
            apolipoprotein E1 phenotype and epsilon 1/'null' genotype
  JOURNAL   Eur J Clin Invest 22 (9), 599-608 (1992)
   PUBMED   1360898
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Utermann,G., Hees,M. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E and occurrence of
            dysbetalipoproteinaemia in man
  JOURNAL   Nature 269 (5629), 604-607 (1977)
   PUBMED   199847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC086581.1.
            
            On Dec 11, 2007 this sequence version replaced NP_620183.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All five variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220752.1, FQ218972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..312
                     /product="apolipoprotein E precursor"
                     /note="apo-E"
                     /calculated_mol_wt=33845
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1927
     mat_peptide     19..312
                     /product="Apolipoprotein E. /id=PRO_0000001996"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
                     /calculated_mol_wt=33845
     Region          72..247
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          73..258
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          202..282
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          258..312
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          270..282
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     CDS             1..312
                     /gene="Apoe"
                     /gene_synonym="APOEA"
                     /coded_by="NM_138828.3:97..1035"
                     /db_xref="GeneID:25728"
                     /db_xref="RGD:2138"
ORIGIN      
        1 mkalwalllv plltgclaeg elevtdqlpg qsdqpweqal nrfwdylrwv qtlsdqvqee
       61 lqssqvtqel tvlmedtmte vkaykkelee qlgpvaeetr arlakevqaa qarlgadmed
      121 lrnrlgqyrn evntmlgqst eelrsrlsth lrkmrkrlmr daddlqkrla vykagaqega
      181 ergvsairer lgplveqgrq rtanlgagaa qplrdraqal sdrirgrlee vgnqardrle
      241 evreqmeevr skmeeqtqqi rlqaeifqar ikgwfeplve dmqrqwanlm ekiqasvatn
      301 siasttvple nq
//
LOCUS       NP_612556                322 aa            linear   ROD 27-APR-2025
DEFINITION  3-alpha-hydroxysteroid dehydrogenase [Rattus norvegicus].
ACCESSION   NP_612556 XP_346502 XP_579650
VERSION     NP_612556.1
DBSOURCE    REFSEQ: accession NM_138547.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Su,Y., Li,H., Chen,X., Wang,Y., Li,X., Sun,J. and Ge,R.S.
  TITLE     Ziram inhibits rat neurosteroidogenic 5alpha-reductase 1 and
            3alpha-hydroxysteroid dehydrogenase
  JOURNAL   Toxicol Mech Methods 28 (1), 38-44 (2018)
   PUBMED   28707553
  REMARK    GeneRIF: Ziram inhibited SRD5A1 and AKR1C14 activities, thus
            possibly interfering with neurosteroid production in rats.
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Wang,Y., Sun,J., Chen,L., Zhou,S., Lin,H., Wang,Y., Lin,N. and
            Ge,R.S.
  TITLE     Effects of resveratrol on rat neurosteroid synthetic enzymes
  JOURNAL   Fitoterapia 122, 61-66 (2017)
   PUBMED   28823883
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Guo,J., Li,L., Zhou,S., Su,Y., Li,X., Sun,J. and Ge,R.S.
  TITLE     Butylated hydroxyanisole alters rat 5alpha-reductase and
            3alpha-hydroxysteroid dehydrogenase: Implications for influences of
            neurosteroidogenesis
  JOURNAL   Neurosci Lett 653, 132-138 (2017)
   PUBMED   28552457
  REMARK    GeneRIF: Butylated hydroxyanisole alters rat 5alpha-reductase and
            3alpha-hydroxysteroid dehydrogenase: Implications for influences of
            neurosteroidogenesis.
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Kimoto,T., Ishii,H., Higo,S., Hojo,Y. and Kawato,S.
  TITLE     Semicomprehensive analysis of the postnatal age-related changes in
            the mRNA expression of sex steroidogenic enzymes and sex steroid
            receptors in the male rat hippocampus
  JOURNAL   Endocrinology 151 (12), 5795-5806 (2010)
   PUBMED   21047951
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Cheng,K.C.
  TITLE     Molecular cloning of rat liver 3alpha-hydroxysteroid dehydrogenase
            and identification of structurally related proteins from rat lung
            and kidney
  JOURNAL   J Steroid Biochem Mol Biol 43 (8), 1083-1088 (1992)
   PUBMED   22217852
  REMARK    GeneRIF: characterization of recombinant 3-alpha-hydroxysteroid
            dehydrogenase from liver: molecular weight; amino acid sequence;
            sequence alignment and homology with similar enzymes; inhibition by
            indomethacin
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Pawlowski,J., Huizinga,M. and Penning,T.M.
  TITLE     Isolation and partial characterization of a full-length cDNA clone
            for 3 alpha-hydroxysteroid dehydrogenase: a potential target enzyme
            for nonsteroidal anti-inflammatory drugs
  JOURNAL   Agents Actions 34 (1-2), 289-293 (1991)
   PUBMED   1793046
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Stolz,A., Rahimi-Kiani,M., Ameis,D., Chan,E., Ronk,M. and
            Shively,J.E.
  TITLE     Molecular structure of rat hepatic 3 alpha-hydroxysteroid
            dehydrogenase. A member of the oxidoreductase gene family
  JOURNAL   J Biol Chem 266 (23), 15253-15257 (1991)
   PUBMED   1714456
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Cheng,K.C., White,P.C. and Qin,K.N.
  TITLE     Molecular cloning and expression of rat liver 3
            alpha-hydroxysteroid dehydrogenase
  JOURNAL   Mol Endocrinol 5 (6), 823-828 (1991)
   PUBMED   1922097
REFERENCE   9  (residues 1 to 322)
  AUTHORS   Penning,T.M., Abrams,W.R. and Pawlowski,J.E.
  TITLE     Affinity labeling of 3 alpha-hydroxysteroid dehydrogenase with 3
            alpha-bromoacetoxyandrosterone and 11
            alpha-bromoacetoxyprogesterone. Isolation and sequence of active
            site peptides containing reactive cysteines; sequence confirmation
            using nucleotide sequence from a cDNA clone
  JOURNAL   J Biol Chem 266 (14), 8826-8834 (1991)
   PUBMED   2026597
REFERENCE   10 (residues 1 to 322)
  AUTHORS   Pawlowski,J.E., Huizinga,M. and Penning,T.M.
  TITLE     Cloning and sequencing of the cDNA for rat liver 3
            alpha-hydroxysteroid/dihydrodiol dehydrogenase
  JOURNAL   J Biol Chem 266 (14), 8820-8825 (1991)
   PUBMED   1840601
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1 and BC091123.1.
            
            On or before Feb 1, 2006 this sequence version replaced
            XP_579650.1, XP_346502.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091123.1, M64393.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMN16676784 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.2"
     Protein         1..322
                     /product="3-alpha-hydroxysteroid dehydrogenase"
                     /EC_number="1.1.1.50"
                     /note="3-alpha-HSD; hydroxyprostaglandin dehydrogenase;
                     steroid 3-alpha-dehydrogenase"
                     /calculated_mol_wt=36897
     Site            1
                     /site_type="blocked"
                     /note="Blocked amino end (Met); propagated from
                     UniProtKB/Swiss-Prot (P23457.1)"
     Region          7..308
                     /region_name="AKR_AKR1C1-35"
                     /note="AKR1C family of aldo-keto reductase (AKR); cd19108"
                     /db_xref="CDD:381334"
     Site            order(22..24,50,54..55,84,86,117..118,120,128..129,
                     166..167,190,216..222,224,227,236,253,268..273,276,
                     279..280,306,308)
                     /site_type="active"
                     /db_xref="CDD:381334"
     Site            order(50,55,84,117)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381334"
     Site            84
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P23457.1)"
     CDS             1..322
                     /gene="Akr1c14"
                     /gene_synonym="Akr1c9"
                     /coded_by="NM_138547.3:58..1026"
                     /db_xref="GeneID:191574"
                     /db_xref="RGD:708361"
ORIGIN      
        1 mdsislrval ndgnfipvlg fgttvpekva kdevikatki aidngfrhfd saylyeveee
       61 vgqairskie dgtvkredif ytsklwstfh rpelvrtcle ktlkstqldy vdlyiihfpm
      121 alqpgdiffp rdehgkllfe tvdicdtwea mekckdagla ksigvsnfnc rqlerilnkp
      181 glkykpvcnq vechlylnqs kmldyckskd iilvsyctlg ssrdktwvdq kspvllddpv
      241 lcaiakkykq tpalvalryq lqrgvvplir sfnakrikel tqvfefqlas edmkaldgln
      301 rnfrynnaky fddhpnhpft de
//
LOCUS       NP_001094254             440 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction gamma-2 protein [Rattus norvegicus].
ACCESSION   NP_001094254 XP_001076914 XP_002727761 XP_573100
VERSION     NP_001094254.1
DBSOURCE    REFSEQ: accession NM_001100784.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Jiang,L., Xu,D., Zhang,W.J., Tang,Y. and Peng,Y.
  TITLE     Astrocytes induce proliferation of oligodendrocyte progenitor cells
            via connexin 47-mediated activation of Chi3l1 expression
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (7), 3012-3020 (2019)
   PUBMED   31002152
  REMARK    GeneRIF: Astrocytes induce proliferation of oligodendrocyte
            progenitor cells via connexin 47-mediated activation of Chi3l1
            expression.
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Xu,D., Liu,Z., Wang,S., Peng,Y. and Sun,X.
  TITLE     Astrocytes regulate the expression of Sp1R3 on oligodendrocyte
            progenitor cells through Cx47 and promote their proliferation
  JOURNAL   Biochem Biophys Res Commun 490 (3), 670-675 (2017)
   PUBMED   28634078
  REMARK    GeneRIF: Astrocytes regulate the expression of S1pR3 in
            oligodendrocyte progenitor cells via Cx47, which could be a
            valuable approach for promoting oligodendrocyte progenitor cells
            proliferation.
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Liu,Z., Xu,D., Wang,S., Chen,Y., Li,Z., Gao,X., Jiang,L., Tang,Y.
            and Peng,Y.
  TITLE     Astrocytes induce proliferation of oligodendrocyte progenitor cells
            via connexin 47-mediated activation of the ERK/Id4 pathway
  JOURNAL   Cell Cycle 16 (7), 714-722 (2017)
   PUBMED   28278052
  REMARK    GeneRIF: Astrocytes can cause Ca(2+) signaling activation, ERK1/2
            phosphorylation, and Id4 expression stimulation in oligodendrocyte
            progenitor cells inducing proliferation of these cells, mainly
            through Cx47.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Mukhamedshina,Y.O., Shaymardanova,G.F., Garanina capital IE,
            Cyrilliccapital,I.E. Cyrillic, Salafutdinov,I.I., Rizvanov capital
            A, Cyrilliccapital,A. Cyrillic, Islamov,R.R. and Chelyshev,Y.A.
  TITLE     Adenoviral vector carrying glial cell-derived neurotrophic factor
            for direct gene therapy in comparison with human umbilical cord
            blood cell-mediated therapy of spinal cord injury in rat
  JOURNAL   Spinal Cord 54 (5), 347-359 (2016)
   PUBMED   26415641
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Cui,Y., Masaki,K., Yamasaki,R., Imamura,S., Suzuki,S.O.,
            Hayashi,S., Sato,S., Nagara,Y., Kawamura,M.F. and Kira,J.
  TITLE     Extensive dysregulations of oligodendrocytic and astrocytic
            connexins are associated with disease progression in an amyotrophic
            lateral sclerosis mouse model
  JOURNAL   J Neuroinflammation 11, 42 (2014)
   PUBMED   24597481
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Cruciani,V., Heintz,K.M., Husoy,T., Hovig,E., Warren,D.J. and
            Mikalsen,S.O.
  TITLE     The detection of hamster connexins: a comparison of expression
            profiles with wild-type mouse and the cancer-prone Min mouse
  JOURNAL   Cell Commun Adhes 11 (5-6), 155-171 (2004)
   PUBMED   16194882
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Kleopa,K.A., Orthmann,J.L., Enriquez,A., Paul,D.L. and Scherer,S.S.
  TITLE     Unique distributions of the gap junction proteins connexin29,
            connexin32, and connexin47 in oligodendrocytes
  JOURNAL   Glia 47 (4), 346-357 (2004)
   PUBMED   15293232
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Uhlenberg,B., Schuelke,M., Ruschendorf,F., Ruf,N., Kaindl,A.M.,
            Henneke,M., Thiele,H., Stoltenburg-Didinger,G., Aksu,F.,
            Topaloglu,H., Nurnberg,P., Hubner,C., Weschke,B. and Gartner,J.
  TITLE     Mutations in the gene encoding gap junction protein alpha 12
            (connexin 46.6) cause Pelizaeus-Merzbacher-like disease
  JOURNAL   Am J Hum Genet 75 (2), 251-260 (2004)
   PUBMED   15192806
  REMARK    Erratum:[Am J Hum Genet. 2004 Oct;5(4):737]
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Condorelli,D.F., Trovato-Salinaro,A., Mudo,G., Mirone,M.B. and
            Belluardo,N.
  TITLE     Cellular expression of connexins in the rat brain: neuronal
            localization, effects of kainate-induced seizures and expression in
            apoptotic neuronal cells
  JOURNAL   Eur J Neurosci 18 (7), 1807-1827 (2003)
   PUBMED   14622215
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Teubner,B., Odermatt,B., Guldenagel,M., Sohl,G., Degen,J.,
            Bukauskas,F., Kronengold,J., Verselis,V.K., Jung,Y.T., Kozak,C.A.,
            Schilling,K. and Willecke,K.
  TITLE     Functional expression of the new gap junction gene connexin47
            transcribed in mouse brain and spinal cord neurons
  JOURNAL   J Neurosci 21 (4), 1117-1126 (2001)
   PUBMED   11160382
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_573100.1, XP_002727761.1, XP_001076914.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.1454895.1, CB713303.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..440
                     /product="gap junction gamma-2 protein"
                     /note="connexin-47; gap junction alpha-12 protein; gap
                     junction membrane channel protein alpha 12; gap junction
                     protein, alpha 12"
                     /calculated_mol_wt=46859
     Region          5..290
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Site            79..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Region          108..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Region          368..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80XF7.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BQU6; propagated from
                     UniProtKB/Swiss-Prot (Q80XF7.2)"
     CDS             1..440
                     /gene="Gjc2"
                     /gene_synonym="Cx47; Gja12"
                     /coded_by="NM_001100784.1:82..1404"
                     /db_xref="GeneID:497913"
                     /db_xref="RGD:1562712"
ORIGIN      
        1 mtnmswsflt rlleeihnhs tfvgkvwltv lvvfrivlta vggesiysde qskftcntrq
       61 pgcdnvcyda faplshvrfw vfqivvistp svmylgyavh rlaraseqer rralrrrpgp
      121 rrlpraqlpp pppgwpdttd lgeaepilal eededeepga pegpgedtee ertedvaakg
      181 gggdgktvvt pgpagqhdgr rriqreglmr vyvaqlvvra afevaflvgq yllygfevpp
      241 ffacsrqpcp hvvdcfvsrp tektvfllvm yvvsclclll nlcemahlgl gsaqdavrgr
      301 rgasaagpgp aprpppcafp aaaaglacpp dyslvvraae rarahdqnla nlalqalrdg
      361 aavaavsadr dsppcsglna tsrgppragg pasgtgsats ggtvgeqgrs gaqeqlatkp
      421 rvgsekgstg srdgkatvwi
//
LOCUS       NP_058914               1339 aa            linear   ROD 27-APR-2025
DEFINITION  receptor tyrosine-protein kinase erbB-3 precursor [Rattus
            norvegicus].
ACCESSION   NP_058914
VERSION     NP_058914.2
DBSOURCE    REFSEQ: accession NM_017218.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1339)
  AUTHORS   Xu,L., Li,Z., Rong,J. and Lang,L.
  TITLE     Effect of regulation of the NRG1/ErbB4 signaling pathway on the
            visual cortex synaptic plasticity of amblyopic adult rats
  JOURNAL   J Biochem Mol Toxicol 35 (9), e22841 (2021)
   PUBMED   34273906
REFERENCE   2  (residues 1 to 1339)
  AUTHORS   Hu,Z., Hu,K., Wang,R., Gu,Y., Ouyang,W., Zhou,J. and Wen,Y.
  TITLE     Differentially expressed genes accompanying neurobehavioral
            deficits in a modified rat model of vascular dementia
  JOURNAL   Neurosci Lett 750, 135774 (2021)
   PUBMED   33640362
  REMARK    GeneRIF: Differentially expressed genes accompanying
            neurobehavioral deficits in a modified rat model of vascular
            dementia.
REFERENCE   3  (residues 1 to 1339)
  AUTHORS   Zhu,J., Zhu,Z., Ren,Y., Dong,Y., Li,Y. and Yang,X.
  TITLE     Role of the Nrdp1 in Brain Injury Induced by Chronic Intermittent
            Hypoxia in Rats via Regulating the Protein Levels of ErbB3
  JOURNAL   Neurotox Res 38 (1), 124-132 (2020)
   PUBMED   32200526
  REMARK    GeneRIF: Role of the Nrdp1 in Brain Injury Induced by Chronic
            Intermittent Hypoxia in Rats via Regulating the Protein Levels of
            ErbB3.
REFERENCE   4  (residues 1 to 1339)
  AUTHORS   Heim,P., Morandi,C., Brouwer,G.R., Xu,L., Montessuit,C. and
            Brink,M.
  TITLE     Neuregulin-1 triggers GLUT4 translocation and enhances glucose
            uptake independently of insulin receptor substrate and ErbB3 in
            neonatal rat cardiomyocytes
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1867 (3), 118562 (2020)
   PUBMED   31669265
  REMARK    GeneRIF: Treatment of neonatal rats with rhNRG-1 induced a
            signaling response comparable with that observed in vitro,
            including increased ErbB4-pTyr(1284), Akt-pThr(308) and
            Erk1/2-pThr(202)/Tyr(204).
REFERENCE   5  (residues 1 to 1339)
  AUTHORS   Yehya,N., Song,M.J., Lawrence,G.G. and Margulies,S.S.
  TITLE     HER2 Signaling Implicated in Regulating Alveolar Epithelial
            Permeability with Cyclic Stretch
  JOURNAL   Int J Mol Sci 20 (4), 948 (2019)
   PUBMED   30813222
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1339)
  AUTHORS   Carroll,S.L., Miller,M.L., Frohnert,P.W., Kim,S.S. and Corbett,J.A.
  TITLE     Expression of neuregulins and their putative receptors, ErbB2 and
            ErbB3, is induced during Wallerian degeneration
  JOURNAL   J Neurosci 17 (5), 1642-1659 (1997)
   PUBMED   9030624
REFERENCE   7  (residues 1 to 1339)
  AUTHORS   Zhu,X., Lai,C., Thomas,S. and Burden,S.J.
  TITLE     Neuregulin receptors, erbB3 and erbB4, are localized at
            neuromuscular synapses
  JOURNAL   EMBO J 14 (23), 5842-5848 (1995)
   PUBMED   8846777
REFERENCE   8  (residues 1 to 1339)
  AUTHORS   Hellyer,N.J., Kim,H.H., Greaves,C.H., Sierke,S.L. and Koland,J.G.
  TITLE     Cloning of the rat ErbB3 cDNA and characterization of the
            recombinant protein
  JOURNAL   Gene 165 (2), 279-284 (1995)
   PUBMED   8522190
REFERENCE   9  (residues 1 to 1339)
  AUTHORS   Moscoso,L.M., Chu,G.C., Gautam,M., Noakes,P.G., Merlie,J.P. and
            Sanes,J.R.
  TITLE     Synapse-associated expression of an acetylcholine receptor-inducing
            protein, ARIA/heregulin, and its putative receptors, ErbB2 and
            ErbB3, in developing mammalian muscle
  JOURNAL   Dev Biol 172 (1), 158-169 (1995)
   PUBMED   7589796
REFERENCE   10 (residues 1 to 1339)
  AUTHORS   Wallasch,C., Weiss,F.U., Niederfellner,G., Jallal,B., Issing,W. and
            Ullrich,A.
  TITLE     Heregulin-dependent regulation of HER2/neu oncogenic signaling by
            heterodimerization with HER3
  JOURNAL   EMBO J 14 (17), 4267-4275 (1995)
   PUBMED   7556068
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U29339.2.
            
            On Dec 10, 2001 this sequence version replaced NP_058914.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U29339.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132265 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1339
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..1339
                     /product="receptor tyrosine-protein kinase erbB-3
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-3; c-erbB3;
                     c-erbB-3; proto-oncogene-like protein c-ErbB-3; avian
                     erythroblastosis oncogene B 3; v-erb-b2 erythroblastic
                     leukemia viral oncogene homolog 3; v-erb-b2 avian
                     erythroblastic leukemia viral oncogene homolog 3"
                     /calculated_mol_wt=145514
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2051
     mat_peptide     20..1339
                     /product="Receptor tyrosine-protein kinase erbB-3.
                     /id=PRO_0000016673"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62799.3)"
                     /calculated_mol_wt=145514
     Region          56..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          182..329
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          353..474
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            437
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            469
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          499..630
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            566
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Site            616
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          638..674
                     /region_name="TM_ErbB3"
                     /note="Transmembrane domain of ErbB3, a Protein Tyrosine
                     Kinase; cd12095"
                     /db_xref="CDD:213056"
     Site            order(641,645,648,650..651,653..654,657,661..662,665)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213056"
     Site            644..662
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62799.3)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          699..977
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(713..716,719,721,738,740,770,785..788,832,836..837,
                     839,849..850)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173656"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21860; propagated from
                     UniProtKB/Swiss-Prot (Q62799.3)"
     Region          1023..1052
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62799.3)"
     Region          1078..1215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62799.3)"
     CDS             1..1339
                     /gene="Erbb3"
                     /gene_synonym="nuc-ErbB3"
                     /coded_by="NM_017218.3:139..4158"
                     /db_xref="GeneID:29496"
                     /db_xref="RGD:69323"
ORIGIN      
        1 mratgtlqvl cfllslargs emgnsqavcp gtlnglsvtg dadnqyqtly klyekcevvm
       61 gnleivltgh nadlsflqwi revtgyvlva mnefsvlplp nlrvvrgtqv ydgkfaifvm
      121 lnyntnssha lrqlkftqlt eilsggvyie kndklchmdt idwrdivrvr gaeivvknng
      181 ancppchevc kgrcwgpgpd dcqiltktic apqcngrcfg pnpnqcchde caggcsgpqd
      241 tdcfacrrfn dsgacvprcp eplvynkltf qlepnphtky qyggvcvasc phnfvvdqtf
      301 cvracppdkm evdkhglkmc epcgglcpka cegtgsgsry qtvdssnidg fvnctkilgn
      361 ldflitglnv dpwhkipald peklnvfrtv reitgylniq swpphmhnfs vfsnlttigg
      421 rslynrgfsl limknlnvts lgfrslkeis agrvyisanq qlcyhhslnw trllrgpsee
      481 rldikydrpl geclaegkvc dplcssggcw gpgpgqclsc rnysregvcv thcnflqgep
      541 refvheaqcf schpeclpme gtstcngsgs dacarcahfr dgphcvnscp hgilgakgpi
      601 ykypdaqnec rpchenctqg cngpelqdcl gqaevlmskp hlviavtvgl avilmilggs
      661 flywrgrriq nkramrryle rgesiepldp sekankvlar ifketelrkl kvlgsgvfgt
      721 vhkgiwipeg esikipvcik viedksgrqs fqavtdhmla vgsldhahiv rllglcpgss
      781 lqlvtqylpl gslldhvkqh retlgpqlll nwgvqiakgm yyleehsmvh rdlalrnvml
      841 kspsqvqvad fgvadllppd dkqllhseak tpikwmales ihfgkythqs dvwsygvtvw
      901 elmtfgaepy aglrlaeipd llekgerlaq pqictidvym vmvkcwmide nirptfkela
      961 neftrmardp prylvikras gpgtppaaep svlttkelqe aelepeldld ldleaeeegl
     1021 atslgsalsl ptgtltrprg sqsllspssg ympmnqsslg eacldsavlg greqfsrpis
     1081 lhpiprgrpa sesseghvtg seaelqekvs vcrsrsrsrs prprgdsayh sqrhslltpv
     1141 tplsppglee edgngyvmpd thlrgasssr egtlssvgls svlgteeede deeyeymnrk
     1201 rrgspprppr pgsleelgye ymdvgsdlsa slgstqscpl hpmaivpsag ttpdedyeym
     1261 nrrrgaggag gdyaamgacp aaeqgyeemr afqgpghhap hvryarlktl rsleatdsaf
     1321 dnpdywhsrl fpkanaqrt
//
LOCUS       NP_001263358              89 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim9
            [Rattus norvegicus].
ACCESSION   NP_001263358 XP_001072892 XP_001080501 XP_002726796 XP_002726797
            XP_002729679 XP_002729680 XP_003750227 XP_003754231
VERSION     NP_001263358.1
DBSOURCE    REFSEQ: accession NM_001276429.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Webb,C.T., Gorman,M.A., Lazarou,M., Ryan,M.T. and Gulbis,J.M.
  TITLE     Crystal structure of the mitochondrial chaperone TIM9.10 reveals a
            six-bladed alpha-propeller
  JOURNAL   Mol Cell 21 (1), 123-133 (2006)
   PUBMED   16387659
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Muhlenbein,N., Hofmann,S., Rothbauer,U. and Bauer,M.F.
  TITLE     Organization and function of the small Tim complexes acting along
            the import pathway of metabolite carriers into mammalian
            mitochondria
  JOURNAL   J Biol Chem 279 (14), 13540-13546 (2004)
   PUBMED   14726512
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Paschen,S.A., Rothbauer,U., Kaldi,K., Bauer,M.F., Neupert,W. and
            Brunner,M.
  TITLE     The role of the TIM8-13 complex in the import of Tim23 into
            mitochondria
  JOURNAL   EMBO J 19 (23), 6392-6400 (2000)
   PUBMED   11101512
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1 and FM052814.1.
            
            On or before Feb 14, 2013 this sequence version replaced
            XP_002726796.1, XP_002726797.1, XP_001080501.1, XP_003754231.1,
            XP_002729679.1, XP_002729680.1, XP_001072892.1, XP_003750227.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM052814.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760433,
                                           SAMEA5760434 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..89
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim9"
                     /note="translocase of inner mitochondrial membrane 9
                     homolog"
                     /calculated_mol_wt=10245
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5J7; propagated from
                     UniProtKB/Swiss-Prot (Q9WV97.3)"
     Region          10..69
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          28..52
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV97.3)"
     CDS             1..89
                     /gene="Timm9"
                     /gene_synonym="Tim9; Tim9a; Timm9a"
                     /coded_by="NM_001276429.1:176..445"
                     /db_xref="GeneID:171139"
                     /db_xref="RGD:621656"
ORIGIN      
        1 maaqipesdq ikqfkeflgt ynkltetcfl dcvkdfttre vkpeevtcse hclqkylkmt
       61 qrismrfqey hiqqnealaa kagllgqpr
//
LOCUS       NP_001257956             459 aa            linear   ROD 27-APR-2025
DEFINITION  serine protease HTRA3 precursor [Rattus norvegicus].
ACCESSION   NP_001257956 XP_001058037 XP_003751430 XP_003751431 XP_003752791
            XP_341238
VERSION     NP_001257956.1
DBSOURCE    REFSEQ: accession NM_001271027.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Shen,Z., Sun,F., Lu,Y., Yuan,L., Ge,S., Gong,Q. and Shi,H.
  TITLE     High temperature requirement A3 attenuates hypoxia/reoxygenation
            induced injury in H9C2 cells via suppressing inflammatory responses
  JOURNAL   Eur J Pharmacol 928, 175114 (2022)
   PUBMED   35764130
  REMARK    GeneRIF: High temperature requirement A3 attenuates
            hypoxia/reoxygenation induced injury in H9C2 cells via suppressing
            inflammatory responses.
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Glaza,P., Osipiuk,J., Wenta,T., Zurawa-Janicka,D., Jarzab,M.,
            Lesner,A., Banecki,B., Skorko-Glonek,J., Joachimiak,A. and
            Lipinska,B.
  TITLE     Structural and Functional Analysis of Human HtrA3 Protease and Its
            Subdomains
  JOURNAL   PLoS One 10 (6), e0131142 (2015)
   PUBMED   26110759
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Singh,H., Makino,S., Endo,Y., Li,Y., Stephens,A.N. and Nie,G.
  TITLE     Application of the wheat-germ cell-free translation system to
            produce high temperature requirement A3 (HtrA3) proteases
  JOURNAL   Biotechniques 52 (1), 23-28 (2012)
   PUBMED   22229724
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Ketteler,R., Sun,Z., Kovacs,K.F., He,W.W. and Seed,B.
  TITLE     A pathway sensor for genome-wide screens of intracellular
            proteolytic cleavage
  JOURNAL   Genome Biol 9 (4), R64 (2008)
   PUBMED   18387192
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Tocharus,J., Tsuchiya,A., Kajikawa,M., Ueta,Y., Oka,C. and
            Kawaichi,M.
  TITLE     Developmentally regulated expression of mouse HtrA3 and its role as
            an inhibitor of TGF-beta signaling
  JOURNAL   Dev Growth Differ 46 (3), 257-274 (2004)
   PUBMED   15206957
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000014.1.
            
            On or before Aug 29, 2012 this sequence version replaced
            XP_001058037.1, XP_003752791.1, XP_003751430.1, XP_341238.2,
            XP_003751431.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.52098.1,
                                           SRR26643291.35688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..459
                     /product="serine protease HTRA3 precursor"
                     /note="probable serine protease HTRA3; pregnancy-related
                     serine protease; high-temperature requirement factor A3"
                     /calculated_mol_wt=46980
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2296
     mat_peptide     24..459
                     /product="Serine protease HTRA3. /id=PRO_0000417598"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZA76.1)"
                     /calculated_mol_wt=46980
     Region          31..82
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     pfam00219"
                     /db_xref="CDD:459717"
     Region          <95..132
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          179..449
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
     Region          181..346
                     /region_name="Serine protease. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZA76.1)"
     CDS             1..459
                     /gene="Htra3"
                     /gene_synonym="RGD1308120"
                     /coded_by="NM_001271027.1:167..1546"
                     /db_xref="GeneID:360959"
                     /db_xref="RGD:1308120"
ORIGIN      
        1 mqarallpat latlatlavs vlareppaap cparcdvsrc psprcpggyv pdlcncclvc
       61 aasegepcgr pldspcgdsl ecvrgvcrcr wthtvcgtdg htyadvcalq aasrralqis
      121 gtpvrqlqkg acpsglhqlt sprykfnfia dvvekiapav vhielflrhp lfgrnvplss
      181 gsgfimseag livtnahvvs ssntasgrqq lkvqlqngda yeatiqdidk ksdiatilih
      241 pnkklpvlll ghsadlrpge fvvaigspfa lqntvttgiv staqrdgkel glrdsdmdyi
      301 qtdaiinygn sggplvnldg evigintlkv aagisfaips dritrflsef qdkhvkdwkk
      361 rfigirmrti tpslveelkt anpdfpavss giyvqevvpn spsqrggiqd gdiivkvngr
      421 plvdsselqe avlnesslll evrrgnddll fsimpevvm
//
LOCUS       NP_037249               1804 aa            linear   ROD 27-APR-2025
DEFINITION  collagen alpha-1(XI) chain precursor [Rattus norvegicus].
ACCESSION   NP_037249 XP_002726110 XP_002729150
VERSION     NP_037249.1
DBSOURCE    REFSEQ: accession NM_013117.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1804)
  AUTHORS   Katayama,K., Kuriki,M., Kamiya,T., Tochigi,Y. and Suzuki,H.
  TITLE     Giantin is required for coordinated production of aggrecan, link
            protein and type XI collagen during chondrogenesis
  JOURNAL   Biochem Biophys Res Commun 499 (3), 459-465 (2018)
   PUBMED   29577904
  REMARK    GeneRIF: giantin plays a pivotal role in coordinated production of
            aggrecan, link protein and type XI collagen in chondrocytes.
REFERENCE   2  (residues 1 to 1804)
  AUTHORS   Hering,T.M., Wirthlin,L., Ravindran,S. and McAlinden,A.
  TITLE     Changes in type II procollagen isoform expression during
            chondrogenesis by disruption of an alternative 5' splice site
            within Col2a1 exon 2
  JOURNAL   Matrix Biol 36, 51-63 (2014)
   PUBMED   24735995
REFERENCE   3  (residues 1 to 1804)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   4  (residues 1 to 1804)
  AUTHORS   Brafman,D.A., Phung,C., Kumar,N. and Willert,K.
  TITLE     Regulation of endodermal differentiation of human embryonic stem
            cells through integrin-ECM interactions
  JOURNAL   Cell Death Differ 20 (3), 369-381 (2013)
   PUBMED   23154389
REFERENCE   5  (residues 1 to 1804)
  AUTHORS   Wenstrup,R.J., Smith,S.M., Florer,J.B., Zhang,G., Beason,D.P.,
            Seegmiller,R.E., Soslowsky,L.J. and Birk,D.E.
  TITLE     Regulation of collagen fibril nucleation and initial fibril
            assembly involves coordinate interactions with collagens V and XI
            in developing tendon
  JOURNAL   J Biol Chem 286 (23), 20455-20465 (2011)
   PUBMED   21467034
REFERENCE   6  (residues 1 to 1804)
  AUTHORS   Cho,H., Yamada,Y. and Yoo,T.J.
  TITLE     Ultrastructural changes of cochlea in mice with hereditary
            chondrodysplasia (cho/cho)
  JOURNAL   Ann N Y Acad Sci 630, 259-261 (1991)
   PUBMED   1952599
REFERENCE   7  (residues 1 to 1804)
  AUTHORS   Seegmiller,R.E., Brown,K. and Chandrasekhar,S.
  TITLE     Histochemical, immunofluorescence, and ultrastructural differences
            in fetal cartilage among three genetically distinct
            chondrodystrophic mice
  JOURNAL   Teratology 38 (6), 579-592 (1988)
   PUBMED   3070812
REFERENCE   8  (residues 1 to 1804)
  AUTHORS   Bernard,M., Yoshioka,H., Rodriguez,E., Van der Rest,M., Kimura,T.,
            Ninomiya,Y., Olsen,B.R. and Ramirez,F.
  TITLE     Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA
            demonstrates that type XI belongs to the fibrillar class of
            collagens and reveals that the expression of the gene is not
            restricted to cartilagenous tissue
  JOURNAL   J Biol Chem 263 (32), 17159-17166 (1988)
   PUBMED   3182841
REFERENCE   9  (residues 1 to 1804)
  AUTHORS   Seegmiller,R.E. and Fraser,F.C.
  TITLE     Mandibular growth retardation as a cause of cleft palate in mice
            homozygous for the chondrodysplasia gene
  JOURNAL   J Embryol Exp Morphol 38, 227-238 (1977)
   PUBMED   886247
REFERENCE   10 (residues 1 to 1804)
  AUTHORS   Seegmiller,R., Fraser,F.C. and Sheldon,H.
  TITLE     A new chondrodystrophic mutant in mice. Electron microscopy of
            normal and abnormal chondrogenesis
  JOURNAL   J Cell Biol 48 (3), 580-593 (1971)
   PUBMED   4100752
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_002726110.1, XP_002729150.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.9843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1804
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..1804
                     /product="collagen alpha-1(XI) chain precursor"
                     /note="procollagen type XI alpha 1; collagen alpha-1(XI)
                     chain; collagen type a1(XI)6B-7; collagen type
                     a1(XI)6A-7-8; collagen, type XI, alpha 1"
                     /calculated_mol_wt=176794
     sig_peptide     1..34
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20909.2)"
                     /calculated_mol_wt=4252
     Region          37..228
                     /region_name="TSPN"
                     /note="Thrombospondin N-terminal -like domains;
                     smart00210"
                     /db_xref="CDD:214560"
     Region          229..417
                     /region_name="Nonhelical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Site            351
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20909.2)"
     Region          <418..>649
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          418..506
                     /region_name="Triple-helical region (interrupted)"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          437..506
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          507..509
                     /region_name="Short nonhelical segment"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          510..527
                     /region_name="Telopeptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     mat_peptide     512..1561
                     /product="Collagen alpha-1(XI) chain. /id=PRO_0000005780"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
                     /calculated_mol_wt=97421
     Region          526..1560
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          528..1540
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          <600..>901
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <789..>1042
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1003..>1280
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1251..>1481
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1443..>1573
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1541..1561
                     /region_name="Nonhelical region (C-terminal)"
                     /note="propagated from UniProtKB/Swiss-Prot (P20909.2)"
     Region          1573..1802
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; pfam01410"
                     /db_xref="CDD:460199"
     Site            1638
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20909.2)"
     Site            1707
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20909.2)"
     CDS             1..1804
                     /gene="Col11a1"
                     /coded_by="NM_013117.1:353..5767"
                     /db_xref="GeneID:25654"
                     /db_xref="RGD:2372"
ORIGIN      
        1 mepwsrwktk rwiwdltist lvltflfqar evrgaapvdi lkaldfhnsp vgiskttgfc
       61 tsrknskdpd iayrvteeaq isaptkqlfp ggifpqdfsi lftikpkkgt qafllslyne
      121 hgiqqlgvev grspvflfed htgkptpeny plfstvniad gkwhrvaisv ekktvtmivd
      181 ckkkitkpld rsersivdtn gimvfgtril etdvfqgdiq qflitgdpka aydycdhysp
      241 dcdltskaaq aqephideya pediieydye ygetdykeae svtemptvte etvaqteani
      301 vddfqdynyg tmetyqtesp rrvsgsnepn pveegfteey ltgedydvqr nisedilygn
      361 kgidgrdsdl lvdgdlgeyd fyeykeyeer tttspneefg pgvpaetdft etsinghgay
      421 gekgqkgepa vvepgmlveg ppgpagpagl mgppglqgps glpgdpgdrg ppgrpglpga
      481 dglpgppgtm lmlpfryggd gskgptisaq eaqaqailqq arialrgppg pmgltgrpgp
      541 vggpgsagak gesgdpgpqg prgvqgppgp tgkpgkrgrp gadggrgmpg epgskgdrgf
      601 dglpglpgdk ghrgergpqg ppglpgddgm rgedgeigpr glpgeagprg llgprgtpgp
      661 pgqpgiggid gpqgpkgnmg pqgepgppgq qgnpgpqglp gpqgpigppg ekgpqgkpgl
      721 aglpgadgpp ghpgkegqsg ekgalgppgp qgpigypgpr gvkgadgvrg lkgskgekge
      781 dgfpgfkgdm glkgdrgevg qvgprgedgp egpkgragpt gdpgpsgqag ekgklgvpgl
      841 pgypgrqgpk gstgfpgfpg angekgargi agkpgprgqr gptgprgsrg argptgkpgp
      901 kgtsggdgpp gppgergpqg pqgpvgfpgp kgppgpagkd glpghpgqrg etgfqgktgp
      961 pgpggvvgpq gptgetgpig erghpgtpgp pgeqglpgaa gkegakgdpg pqgisgkdgp
     1021 agirgfpger glpgaqgapg lkggegpqgp qgpigspger gsagtagpig lpgrpgpqgp
     1081 pgpagekgap gekgpqgpag rdgvqgpvgl pgpagpagsp gedgdkgeig epgqkgskgd
     1141 kgengppgpp glqgpvgapg iaggdgeagp rgqqgmfgqk gdegargfpg ppgpiglqgl
     1201 pgppgekgen gdvgpmgppg ppgprgpqgp ngadgpqgpp gsigsvggvg ekgepgeagn
     1261 pgppgeagsg gpkgergekg eagppgaagp pgikgppgdd gpkgnpgpvg fpgdpgppge
     1321 pgpagqdgvg gdkgedgdpg qpgppgpsge agppgppgkr gppgasgseg rqgekgakge
     1381 agaegppgkt gpvgpqgpsg kpgpeglrgi pgpvgeqglp gaagqdgppg plgppglpgl
     1441 kgdpgskgek ghpgliglig ppgeqgekgd rglpgtqgsp gakgdggipg pagpigppgp
     1501 pglpgpagpk gnkgssgptg qkgdsgmpgp pgppgppgev iqplpilspk ktrrhtesiq
     1561 adagdnildy sdgmeeifgs lnslkqdieh mkfpmgtqtn partckdlql shpdfpdgey
     1621 widpnqgcsg dsfkvycnft aggetciypd kksegvrlss wpkekpgswy sefkrgklls
     1681 yldvegnsin mvqmtflkll tasarqnfty nchqstawyd vlsgsydkal rflgsndeem
     1741 syennphika lydgcasrkg yektvieint pkidqvpiid vmindfgdqn qkfgfevgpa
     1801 cflg
//
LOCUS       NP_001030315             215 aa            linear   ROD 27-APR-2025
DEFINITION  casein kinase II subunit beta [Rattus norvegicus].
ACCESSION   NP_001030315
VERSION     NP_001030315.1
DBSOURCE    REFSEQ: accession NM_001035238.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Li,X., Yang,Q., Jiang,P., Wen,J., Chen,Y., Huang,J., Tian,M.,
            Ren,J. and Yang,Q.
  TITLE     Inhibition of CK2 Diminishes Fibrotic Scar Formation and Improves
            Outcomes After Ischemic Stroke via Reducing BRD4 Phosphorylation
  JOURNAL   Neurochem Res 49 (5), 1254-1267 (2024)
   PUBMED   38381246
  REMARK    GeneRIF: Inhibition of CK2 Diminishes Fibrotic Scar Formation and
            Improves Outcomes After Ischemic Stroke via Reducing BRD4
            Phosphorylation.
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Barak-Broner,N., Singer-Lahat,D., Chikvashvili,D. and Lotan,I.
  TITLE     CK2 Phosphorylation Is Required for Regulation of Syntaxin 1A
            Activity in Ca2+-Triggered Release in Neuroendocrine Cells
  JOURNAL   Int J Mol Sci 22 (24), 13556 (2021)
   PUBMED   34948351
  REMARK    GeneRIF: CK2 Phosphorylation Is Required for Regulation of Syntaxin
            1A Activity in Ca(2+)-Triggered Release in Neuroendocrine Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Becker,A., Gotz,C., Montenarh,M. and Philipp,S.E.
  TITLE     Control of TRPM3 Ion Channels by Protein Kinase CK2-Mediated
            Phosphorylation in Pancreatic beta-Cells of the Line INS-1
  JOURNAL   Int J Mol Sci 22 (23), 13133 (2021)
   PUBMED   34884938
  REMARK    GeneRIF: Control of TRPM3 Ion Channels by Protein Kinase
            CK2-Mediated Phosphorylation in Pancreatic beta-Cells of the Line
            INS-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Lee,S.W., Rho,J.H., Lee,S.Y., Yoo,S.H., Kim,H.Y., Chung,W.T. and
            Yoo,Y.H.
  TITLE     Alpha B-Crystallin Protects Rat Articular Chondrocytes against
            Casein Kinase II Inhibition-Induced Apoptosis
  JOURNAL   PLoS One 11 (11), e0166450 (2016)
   PUBMED   27851782
  REMARK    GeneRIF: alphaB-crystallin protects rat articular chondrocytes
            against CK2 inhibition-induced apoptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Liu,S., Gao,Y., Yu,X., Zhao,B., Liu,L., Zhao,Y., Luo,Z. and Shi,J.
  TITLE     Annexin-1 Mediates Microglial Activation and Migration via the CK2
            Pathway during Oxygen-Glucose Deprivation/Reperfusion
  JOURNAL   Int J Mol Sci 17 (10), 1770 (2016)
   PUBMED   27782092
  REMARK    GeneRIF: ANXA1 promotes microglial activation and migration during
            oxygen-glucose deprivation/reperfusion via FPR, and CK2 target
            alpha-E-catenin phosphorylation is involved in this process.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Kulikova,O.G. and Reikhardt,B.A.
  TITLE     Role of autophosphorylation in regulation of protein kinase CK2
            from rat neuronal chromatin
  JOURNAL   Biochemistry (Mosc) 63 (12), 1400-1406 (1998)
   PUBMED   9916157
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Sarrouilhe,D., Filhol,O., Leroy,D., Bonello,G., Baudry,M.,
            Chambaz,E.M. and Cochet,C.
  TITLE     The tight association of protein kinase CK2 with plasma membranes
            is mediated by a specific domain of its regulatory beta-subunit
  JOURNAL   Biochim Biophys Acta 1403 (2), 199-210 (1998)
   PUBMED   9630630
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Zhang,P., Davis,A.T. and Ahmed,K.
  TITLE     Mechanism of protein kinase CK2 association with nuclear matrix:
            role of disulfide bond formation
  JOURNAL   J Cell Biochem 69 (2), 211-220 (1998)
   PUBMED   9548568
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Pancetti,F., Bosser,R., Itarte,E. and Bachs,O.
  TITLE     Changes in the activity of nuclear protein kinase CK2 during rat
            liver regeneration
  JOURNAL   Biochem Biophys Res Commun 218 (1), 35-39 (1996)
   PUBMED   8573159
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Ahmed,K., Davis,A., Hanten,J., Lambert,D., McIvor,R.S. and
            Goueli,S.A.
  TITLE     Cloning of cDNAs encoding the alpha and beta subunits of rat casein
            kinase 2 (CK-2): investigation of molecular regulation of CK-2 by
            androgens in rat ventral prostate
  JOURNAL   Cell Mol Biol Res 39 (5), 451-462 (1993)
   PUBMED   8173590
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078807.1 and BX883045.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078807.1, CK595937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..215
                     /product="casein kinase II subunit beta"
                     /EC_number="2.7.11.1"
                     /note="phosvitin; CK II beta; casein kinase II beta
                     subunit; casein kinase 2, beta subunit; casein kinase 2,
                     beta polypeptide; Csnk2b-Ly6g5b"
                     /calculated_mol_wt=24811
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P67870, ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Region          8..191
                     /region_name="CK_II_beta"
                     /note="Casein kinase II regulatory subunit; smart01085"
                     /db_xref="CDD:198153"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Region          147..150
                     /region_name="KSSR motif.
                     /evidence=ECO:0000250|UniProtKB:P67870"
                     /note="propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Region          188..193
                     /region_name="Interaction with alpha subunit"
                     /note="propagated from UniProtKB/Swiss-Prot (P67874.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P67870; propagated from
                     UniProtKB/Swiss-Prot (P67874.1)"
     CDS             1..215
                     /gene="Csnk2b"
                     /gene_synonym="Ck2"
                     /coded_by="NM_001035238.2:80..727"
                     /db_xref="GeneID:81650"
                     /db_xref="RGD:619978"
ORIGIN      
        1 mssseevswi swfcglrgne ffcevdedyi qdkfnltgln eqvphyrqal dmildlepde
       61 elednpnqsd lieqaaemly gliharyilt nrgiaqmlek yqqgdfgycp rvycenqpml
      121 piglsdipge amvklycpkc mdvytpkssr hhhtdgayfg tgfphmlfmv hpeyrpkrpa
      181 nqfvprlygf kihpmayqlq lqaasnfksp vktir
//
LOCUS       NP_001162575             505 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated potassium channel regulatory subunit KCNF1 [Rattus
            norvegicus].
ACCESSION   NP_001162575 XP_001074279 XP_216678
VERSION     NP_001162575.1
DBSOURCE    REFSEQ: accession NM_001169104.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Kramer,J.W., Post,M.A., Brown,A.M. and Kirsch,G.E.
  TITLE     Modulation of potassium channel gating by coexpression of Kv2.1
            with regulatory Kv5.1 or Kv6.1 alpha-subunits
  JOURNAL   Am J Physiol 274 (6), C1501-C1510 (1998)
   PUBMED   9696692
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Salinas,M., Duprat,F., Heurteaux,C., Hugnot,J.P. and Lazdunski,M.
  TITLE     New modulatory alpha subunits for mammalian Shab K+ channels
  JOURNAL   J Biol Chem 272 (39), 24371-24379 (1997)
   PUBMED   9305895
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Drewe,J.A., Verma,S., Frech,G. and Joho,R.H.
  TITLE     Distinct spatial and temporal expression patterns of K+ channel
            mRNAs from different subfamilies
  JOURNAL   J Neurosci 12 (2), 538-548 (1992)
   PUBMED   1740690
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Dec 16, 2009 this sequence version replaced
            XP_001074279.1, XP_216678.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M81783.1, SRR26360194.1890302.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..505
                     /product="voltage-gated potassium channel regulatory
                     subunit KCNF1"
                     /note="potassium voltage-gated channel, subfamily F,
                     member 1; potassium channel, voltage-gated modifier
                     subfamily F, member 1; voltage-gated potassium channel
                     subunit Kv5.1"
                     /calculated_mol_wt=56789
     Region          35..150
                     /region_name="BTB_POZ_Kv5_KCNF1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in KCNF/Kv5
                     subfamily of potassium voltage-gated channels; cd18381"
                     /db_xref="CDD:349690"
     Site            order(40,42..49,52,90,92..93,96,99,103,106,109,111,
                     119..120,123)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349690"
     Region          193..429
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     CDS             1..505
                     /gene="Kcnf1"
                     /gene_synonym="Kh1; Kv5.1"
                     /coded_by="NM_001169104.1:500..2017"
                     /db_xref="GeneID:298908"
                     /db_xref="RGD:631414"
ORIGIN      
        1 mepglasept rsmdasaeqs lpepgsqdsv agddieivvn vggvrqvlyg dllsqypetr
       61 laelinclag gydtifslcd dydpgkrefy fdrdpdafkc vievyyfgev hmkkgicpic
      121 fknemdfwkv dlkflddcck shlsekreel eeiarrvqli lddlgvdaae grwrrcqkcv
      181 wkflekpess cparvvavls fllilvssvv mcmgtipelq vvdsegnrve hptlenveta
      241 cigwftleyl lrlfsspnkl hfalsfmniv dvlailpfyv sltlthlgar mmeltnvqqa
      301 vqalrimria rifklarhss glqtltyalk rsfkelglll mylavgifvf salgytmeqs
      361 hpetlfksip qsfwwaiitm ttvgygdiyp kttlgklnaa isflcgviai alpihpiinn
      421 fvryynkqrv letaakhele lmelnsssae skpggsrsdl dtlppepaar egpswgsrlk
      481 lshsdtfipl lteekhhrtr lqsck
//
LOCUS       NP_001077402             116 aa            linear   ROD 27-APR-2025
DEFINITION  spexin precursor [Rattus norvegicus].
ACCESSION   NP_001077402 XP_001074051
VERSION     NP_001077402.2
DBSOURCE    REFSEQ: accession NM_001083933.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   El-Saka,M.H., Abo El Gheit,R.E., El Saadany,A., Alghazaly,G.M.,
            Marea,K.E. and Madi,N.M.
  TITLE     Effect of spexin on renal dysfunction in experimentally obese rats:
            potential mitigating mechanisms via galanin receptor-2
  JOURNAL   Arch Physiol Biochem 129 (4), 933-942 (2023)
   PUBMED   33632048
  REMARK    GeneRIF: Effect of spexin on renal dysfunction in experimentally
            obese rats: potential mitigating mechanisms via galanin receptor-2.
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Palasz,A., Zarczynski,P., Bogus,K., Mordecka-Chamera,K., Della
            Vecchia,A., Skalbania,J., Worthington,J.J., Krzystanek,M. and
            Zarczynska,M.
  TITLE     Modulatory effect of olanzapine on SMIM20/phoenixin, NPQ/spexin and
            NUCB2/nesfatin-1 gene expressions in the rat brainstem
  JOURNAL   Pharmacol Rep 73 (4), 1188-1194 (2021)
   PUBMED   33928538
  REMARK    GeneRIF: Modulatory effect of olanzapine on SMIM20/phoenixin,
            NPQ/spexin and NUCB2/nesfatin-1 gene expressions in the rat
            brainstem.
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Liu,Y., Sun,L., Zheng,L., Su,M., Liu,H., Wei,Y., Li,D., Wang,Y.,
            Dai,C., Gong,Y., Zhao,C. and Li,Y.
  TITLE     Spexin protects cardiomyocytes from hypoxia-induced metabolic and
            mitochondrial dysfunction
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 393 (1), 25-33 (2020)
   PUBMED   31396649
  REMARK    GeneRIF: Spexin protects cardiomyocytes from hypoxia-induced
            metabolic and mitochondrial dysfunction.
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Walewski,J.L., Ge,F., Lobdell,H. 4th, Levin,N., Schwartz,G.J.,
            Vasselli,J.R., Pomp,A., Dakin,G. and Berk,P.D.
  TITLE     Spexin is a novel human peptide that reduces adipocyte uptake of
            long chain fatty acids and causes weight loss in rodents with
            diet-induced obesity
  JOURNAL   Obesity (Silver Spring) 22 (7), 1643-1652 (2014)
   PUBMED   24550067
  REMARK    GeneRIF: Spexin is a novel hormone involved in weight regulation,
            with potential for obesity therapy.
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Kim,D.K., Yun,S., Son,G.H., Hwang,J.I., Park,C.R., Kim,J.I.,
            Kim,K., Vaudry,H. and Seong,J.Y.
  TITLE     Coevolution of the spexin/galanin/kisspeptin family: Spexin
            activates galanin receptor type II and III
  JOURNAL   Endocrinology 155 (5), 1864-1873 (2014)
   PUBMED   24517231
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Toll,L., Khroyan,T.V., Sonmez,K., Ozawa,A., Lindberg,I.,
            McLaughlin,J.P., Eans,S.O., Shahien,A.A. and Kapusta,D.R.
  TITLE     Peptides derived from the prohormone proNPQ/spexin are potent
            central modulators of cardiovascular and renal function and
            nociception
  JOURNAL   FASEB J 26 (2), 947-954 (2012)
   PUBMED   22038051
  REMARK    GeneRIF: newly identified peptides derived from the NPQ/spexin
            precursor contribute to CNS-mediated control of arterial blood
            pressure and salt and water balance and modulate nociceptive
            responses
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Porzionato,A., Rucinski,M., Macchi,V., Stecco,C., Malendowicz,L.K.
            and De Caro,R.
  TITLE     Spexin expression in normal rat tissues
  JOURNAL   J Histochem Cytochem 58 (9), 825-837 (2010)
   PUBMED   20530460
  REMARK    GeneRIF: Spexin is probably involved in many different
            physiological functions; in particular, location of spexin in
            neurons and endocrine cells suggests its roles as
            neurotransmitter/neuromodulator and endocrine factor.
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Rucinski,M., Porzionato,A., Ziolkowska,A., Szyszka,M., Macchi,V.,
            De Caro,R. and Malendowicz,L.K.
  TITLE     Expression of the spexin gene in the rat adrenal gland and
            evidences suggesting that spexin inhibits adrenocortical cell
            proliferation
  JOURNAL   Peptides 31 (4), 676-682 (2010)
   PUBMED   20045034
  REMARK    GeneRIF: Results suggest direct involvement of spexin in the
            regulation of adrenocortical cell proliferation; however, the
            mechanism of action remains unknown.
REFERENCE   9  (residues 1 to 116)
  AUTHORS   Wan,B., Wang,X.R., Zhou,Y.B., Zhang,X., Huo,K. and Han,Z.G.
  TITLE     C12ORF39, a novel secreted protein with a typical amidation
            processing signal
  JOURNAL   Biosci Rep 30 (1), 1-10 (2009)
   PUBMED   19193193
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Mirabeau,O., Perlas,E., Severini,C., Audero,E., Gascuel,O.,
            Possenti,R., Birney,E., Rosenthal,N. and Gross,C.
  TITLE     Identification of novel peptide hormones in the human proteome by
            hidden Markov model screening
  JOURNAL   Genome Res 17 (3), 320-327 (2007)
   PUBMED   17284679
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 30, 2009 this sequence version replaced NP_001077402.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN14984036
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..116
                     /product="spexin precursor"
                     /note="LRRGT00060; neuropeptide Q; liver
                     regeneration-related protein LRRGT00060"
                     /calculated_mol_wt=10534
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2567
     mat_peptide     27..116
                     /product="Spexin. /id=PRO_0000430222"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R8L2.1)"
                     /calculated_mol_wt=10534
     Region          27..116
                     /region_name="Spexin"
                     /note="Neuropeptide secretory protein family, NPQ, spexin;
                     pfam15171"
                     /db_xref="CDD:464543"
     Site            35..36
                     /site_type="cleavage"
                     /note="Cleavage, by prohormone convertase 2.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (M0R8L2.1)"
     Site            49
                     /site_type="amidation"
                     /note="Glutamine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (M0R8L2.1)"
     Site            52..53
                     /site_type="cleavage"
                     /note="Cleavage, by prohormone convertase 2.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (M0R8L2.1)"
     Region          56..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R8L2.1)"
     Site            72..73
                     /site_type="cleavage"
                     /note="Cleavage, by prohormone convertase 2.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (M0R8L2.1)"
     CDS             1..116
                     /gene="Spx"
                     /gene_synonym="Npq"
                     /coded_by="NM_001083933.3:11..361"
                     /db_xref="GeneID:691138"
                     /db_xref="RGD:1587448"
ORIGIN      
        1 mkgpsilava alalllvlsv lenssgapqr lsekrnwtpq amlylkgaqg hrfisdqsrr
       61 keladrpppe rrnpnlqllt lpeaaalfla slekpqkdeg gdfdksklle drrfyw
//
LOCUS       NP_062105                431 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase Sgk1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_062105
VERSION     NP_062105.2
DBSOURCE    REFSEQ: accession NM_019232.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Li,Y.H., Sun,C.C., Chen,P.M. and Chen,H.H.
  TITLE     SGK1 Target Genes Involved in Heart and Blood Vessel Functions in
            PC12 Cells
  JOURNAL   Cells 12 (12), 1641 (2023)
   PUBMED   37371111
  REMARK    GeneRIF: SGK1 Target Genes Involved in Heart and Blood Vessel
            Functions in PC12 Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Zou,Z., Zhao,T., Zeng,Z. and An,Y.
  TITLE     Serum and glucocorticoid inducible kinase 1 modulates mitochondrial
            dysfunction and oxidative stress in doxorubicin-induced
            cardiomyocytes by regulating Hippo pathway via Neural precursor
            cell-expressed developmentally down-regulated 4 type 2
  JOURNAL   Hum Exp Toxicol 42, 9603271231158039 (2023)
   PUBMED   36781297
  REMARK    GeneRIF: Serum and glucocorticoid inducible kinase 1 modulates
            mitochondrial dysfunction and oxidative stress in
            doxorubicin-induced cardiomyocytes by regulating Hippo pathway via
            Neural precursor cell-expressed developmentally down-regulated 4
            type 2.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Wang,F. and Han,L.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1 (SGK1)
            ameliorates doxorubicin-induced cardiotoxic injury, apoptosis,
            inflammation and oxidative stress by suppressing glucose regulated
            protein 78 (GRP78)-mediated endoplasmic reticulum stress
  JOURNAL   Bioengineered 13 (1), 844-855 (2022)
   PUBMED   34898378
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 (SGK1) ameliorates doxorubicin-induced cardiotoxic injury,
            apoptosis, inflammation and oxidative stress by suppressing glucose
            regulated protein 78 (GRP78)-mediated endoplasmic reticulum stress.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Liu,B.W., Zhang,J., Hong,Y.S., Li,N.B., Liu,Y., Zhang,M., Wu,W.Y.,
            Zheng,H., Lampert,A. and Zhang,X.W.
  TITLE     NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation
  JOURNAL   Mol Neurobiol 58 (3), 964-982 (2021)
   PUBMED   33063281
  REMARK    GeneRIF: NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Lee,R.H., Grames,M.S., Wu,C.Y., Lien,C.F., Couto E Silva,A.,
            Possoit,H.E., Clemons,G.A., Citadin,C.T., Neumann,J.T., Pastore,D.,
            Lauro,D., Della-Morte,D. and Lin,H.W.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1
            exacerbates brain injury and neurological deficits after cardiac
            arrest
  JOURNAL   Am J Physiol Heart Circ Physiol 319 (5), H1044-H1050 (2020)
   PUBMED   32946263
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 exacerbates brain injury and neurological deficits after cardiac
            arrest.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Maiyar,A.C., Phu,P.T., Huang,A.J. and Firestone,G.L.
  TITLE     Repression of glucocorticoid receptor transactivation and DNA
            binding of a glucocorticoid response element within the
            serum/glucocorticoid-inducible protein kinase (sgk) gene promoter
            by the p53 tumor suppressor protein
  JOURNAL   Mol Endocrinol 11 (3), 312-329 (1997)
   PUBMED   9058378
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Maiyar,A.C., Huang,A.J., Phu,P.T., Cha,H.H. and Firestone,G.L.
  TITLE     p53 stimulates promoter activity of the sgk.
            serum/glucocorticoid-inducible serine/threonine protein kinase gene
            in rodent mammary epithelial cells
  JOURNAL   J Biol Chem 271 (21), 12414-12422 (1996)
   PUBMED   8647846
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Richards,J.S., Fitzpatrick,S.L., Clemens,J.W., Morris,J.K.,
            Alliston,T. and Sirois,J.
  TITLE     Ovarian cell differentiation: a cascade of multiple hormones,
            cellular signals, and regulated genes
  JOURNAL   Recent Prog Horm Res 50, 223-254 (1995)
   PUBMED   7740159
  REMARK    Review article
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Imaizumi,K., Tsuda,M., Wanaka,A., Tohyama,M. and Takagi,T.
  TITLE     Differential expression of sgk mRNA, a member of the Ser/Thr
            protein kinase gene family, in rat brain after CNS injury
  JOURNAL   Brain Res Mol Brain Res 26 (1-2), 189-196 (1994)
   PUBMED   7854047
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Webster,M.K., Goya,L., Ge,Y., Maiyar,A.C. and Firestone,G.L.
  TITLE     Characterization of sgk, a novel member of the serine/threonine
            protein kinase gene family which is transcriptionally induced by
            glucocorticoids and serum
  JOURNAL   Mol Cell Biol 13 (4), 2031-2040 (1993)
   PUBMED   8455596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM068981.1, FM123924.1 and BC078843.1.
            
            On Dec 11, 2007 this sequence version replaced NP_062105.1.
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter, 5' UTR, and 5' coding region, compared to variant 1. The
            resulting isoform (3) has a shorter and distinct N-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078843.1, L01624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676787, SAMN16676807
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..431
                     /product="serine/threonine-protein kinase Sgk1 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase Sgk1;
                     serine/threonine protein kinase SGK"
                     /calculated_mol_wt=48894
     Region          1..60
                     /region_name="Necessary for localization to the
                     mitochondria. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06226.1)"
     Region          66..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06226.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00141; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK7.
                     /evidence=ECO:0000269|PubMed:16006511; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Region          90..428
                     /region_name="STKc_SGK1"
                     /note="Catalytic domain of the Protein Serine/Threonine
                     Kinase, Serum- and Glucocorticoid-induced Kinase 1;
                     cd05602"
                     /db_xref="CDD:270753"
     Site            order(104..105,107..110,112,125,127,160,177,179,183,185,
                     222,224,226..227,229,239..240,243,257..262,289,295,298)
                     /site_type="active"
                     /db_xref="CDD:270753"
     Site            order(104..105,107..110,112,125,127,160,177,179,224,
                     226..227,229,239)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270753"
     Site            order(108,183,185,222,224,226,243,257..262,289,295,298)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270753"
     Region          131..141
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06226.1)"
     Site            239..262
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270753"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1.
                     /evidence=ECO:0000269|PubMed:10357815,
                     ECO:0000269|PubMed:16006511; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:O00141; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00141; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Site            397
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270753"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00141; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     Site            418..423
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270753"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16006511; propagated from
                     UniProtKB/Swiss-Prot (Q06226.1)"
     CDS             1..431
                     /gene="Sgk1"
                     /gene_synonym="Sgk"
                     /coded_by="NM_019232.3:61..1356"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:29517"
                     /db_xref="RGD:3668"
ORIGIN      
        1 mtvkteaars tltysrmrgm vailiafmkq rrmglndfiq klannsyack hpevqsylki
       61 sqpqepelmn anpspppsps qqinlgpssn phakpsdfhf lkvigkgsfg kvllarhkae
      121 eafyavkvlq kkailkkkee khimsernvl lknvkhpflv glhfsfqtad klyfvldyin
      181 ggelfyhlqr ercfleprar fyaaeiasal gylhslnivy rdlkpenill dsqghivltd
      241 fglckenieh ngttstfcgt peylapevlh kqpydrtvdw wclgavlyem lyglppfysr
      301 ntaemydnil nkplqlkpni tnsarhlleg llqkdrtkrl gakddfmeik shiffslinw
      361 ddlinkkitp pfnpnvsgps dlrhfdpeft eepvpssigr spdsilvtas vkeaaeaflg
      421 fsyappmdsf l
//
LOCUS       NP_446423                298 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein eL6 [Rattus norvegicus].
ACCESSION   NP_446423
VERSION     NP_446423.2
DBSOURCE    REFSEQ: accession NM_053971.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Behrmann,E., Loerke,J., Budkevich,T.V., Yamamoto,K., Schmidt,A.,
            Penczek,P.A., Vos,M.R., Burger,J., Mielke,T., Scheerer,P. and
            Spahn,C.M.
  TITLE     Structural snapshots of actively translating human ribosomes
  JOURNAL   Cell 161 (4), 845-857 (2015)
   PUBMED   25957688
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Voorhees,R.M., Fernandez,I.S., Scheres,S.H. and Hegde,R.S.
  TITLE     Structure of the mammalian ribosome-Sec61 complex to 3.4 A
            resolution
  JOURNAL   Cell 157 (7), 1632-1643 (2014)
   PUBMED   24930395
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Horne,Z. and Hesketh,J.
  TITLE     Immunological localization of ribosomes in striated rat muscle.
            Evidence for myofibrillar association and ontological changes in
            the subsarcolemmal:myofibrillar distribution
  JOURNAL   Biochem J 268 (1), 231-236 (1990)
   PUBMED   2188648
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Hultin,T.
  TITLE     Selective high-efficiency cross-linking of mammalian ribosomal
            proteins with cleavable thiol-directed heterobifunctional reagents:
            identification and binding directions of major protein complexes
  JOURNAL   Biochim Biophys Acta 872 (3), 226-235 (1986)
   PUBMED   3730400
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Ulbrich,N., Chan,Y.L., Huber,P.W. and Wool,I.G.
  TITLE     Separate binding sites on rat liver ribosomal protein L6 for 5 S
            and 5.8 S ribosomal ribonucleic acids and for transfer ribonucleic
            acids
  JOURNAL   J Biol Chem 257 (19), 11353-11357 (1982)
   PUBMED   7118887
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Ulbrich,N., Lin,A. and Wool,I.G.
  TITLE     Identification by affinity chromatography of the eukaryotic
            ribosomal proteins that bind to 5.8 S ribosomal ribonucleic acid
  JOURNAL   J Biol Chem 254 (17), 8641-8645 (1979)
   PUBMED   468846
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Wittmann-Liebold,B., Geissler,A.W., Lin,A. and Wool,I.G.
  TITLE     Sequence of the amino-terminal region of rat liver ribosomal
            proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and L39
  JOURNAL   J Supramol Struct 12 (4), 425-433 (1979)
   PUBMED   398910
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097295.1.
            
            On Dec 11, 2007 this sequence version replaced NP_446423.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097295.1, BC078761.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..298
                     /product="large ribosomal subunit protein eL6"
                     /note="60S ribosomal protein L6; neoplasm-related protein
                     C140"
                     /calculated_mol_wt=33431
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21533.5)"
     Region          51..105
                     /region_name="Ribosomal_L6e_N"
                     /note="Ribosomal protein L6, N-terminal domain; pfam03868"
                     /db_xref="CDD:427554"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02878; propagated from
                     UniProtKB/Swiss-Prot (P21533.5)"
     Region          146..298
                     /region_name="KOW_RPL6"
                     /note="KOW motif of Ribosomal Protein L6; cd13156"
                     /db_xref="CDD:240520"
     Site            order(146,148,164..168,170,181..182,189..193,195,197..200,
                     202..203,229,253,256..257,279,282..284,288..289)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240520"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02878; propagated from
                     UniProtKB/Swiss-Prot (P21533.5)"
     CDS             1..298
                     /gene="Rpl6"
                     /coded_by="NM_053971.3:3..899"
                     /db_xref="GeneID:117042"
                     /db_xref="RGD:619826"
ORIGIN      
        1 magekaekpd kkeqkpaakk aggdatapra lpagavkkss skakklrksk phcsrnpvlv
       61 rgigrysrsa mysrkalykr kysaaktkve kkkkkekvla tvtktvggdk nggtrvvklr
      121 kmpryypted vprkllshgk kpfsqhvrrl rssitpgtvl iiltgrhrgk rvvflkqlgs
      181 glllvtgpla lnrvplrrth qkfviatstk vdiskvkipk hltdayfkkk plrkprhqeg
      241 eifdtekeky eiteqrkadq kavdsqilpk ikavpqlqgy lrsqfsltng myphklvf
//
LOCUS       NP_001094123             831 aa            linear   ROD 27-APR-2025
DEFINITION  SID1 transmembrane family member 1 precursor [Rattus norvegicus].
ACCESSION   NP_001094123 XP_001067387 XP_221455
VERSION     NP_001094123.1
DBSOURCE    REFSEQ: accession NM_001100653.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Mendez-Acevedo,K.M., Valdes,V.J., Asanov,A. and Vaca,L.
  TITLE     A novel family of mammalian transmembrane proteins involved in
            cholesterol transport
  JOURNAL   Sci Rep 7 (1), 7450 (2017)
   PUBMED   28785058
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Li,W., Koutmou,K.S., Leahy,D.J. and Li,M.
  TITLE     Systemic RNA Interference Deficiency-1 (SID-1) Extracellular Domain
            Selectively Binds Long Double-stranded RNA and Is Required for RNA
            Transport by SID-1
  JOURNAL   J Biol Chem 290 (31), 18904-18913 (2015)
   PUBMED   26067272
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY562215.1, JAXUCZ010000011.1 and BE112870.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_221455.4, XP_001067387.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY562215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN16418971
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..831
                     /product="SID1 transmembrane family member 1 precursor"
                     /note="Msid2"
                     /calculated_mol_wt=91995
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2169
     mat_peptide     20..831
                     /product="SID1 transmembrane family member 1.
                     /id=PRO_0000032577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
                     /calculated_mol_wt=91995
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Region          184..810
                     /region_name="SID-1_RNA_chan"
                     /note="dsRNA-gated channel SID-1; pfam13965"
                     /db_xref="CDD:464057"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            309..329
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Region          354..408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            442..462
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            494..514
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            566
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            572..589
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            600..620
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            626..646
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            688..708
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            715..735
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            746..766
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            768
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     Site            796..816
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q3F5.2)"
     CDS             1..831
                     /gene="Sidt1"
                     /coded_by="NM_001100653.1:11..2506"
                     /db_xref="GeneID:288109"
                     /db_xref="RGD:1559616"
ORIGIN      
        1 mldcprlall calpwllraa vpghraeplk rsaelprnpr dpargadfdr vysgvvslst
       61 eniysfnhts hpgqvtavrv hvnsssdnld ypvlvvvrqq kqvlswqvpl pfqglyqrsy
      121 nyqevsrtlc pskatnetgp leqlifvdva smaphgahyk llvtkikhfq lrtnvafyft
      181 aspsqpqyfl ykfpedvdsv iikvvsekay pcsvvsvqni mcpvydldhd vefngvyqsm
      241 tkqaaitlqk dfpdeqffvv fvikpedyac ggsfsiqene nqtwnlqrsk nlkvtivpsv
      301 kgsvyvkssl fsvfvflsfy lgcllvvfvh hmrfqrkpvd gsfgsgdgsg nmavshpita
      361 stpegsnyga idesssspgr qmsssdggqp chsdtdssve esdfdtmpdi esdknvirtk
      421 mflylsdlsr kdrrivskky kiyfwniiti avfyalpvmq lvityqtvvn vtgnqdicyy
      481 nflcahplgv lsafnnilsn lghvllgflf llivlrrdll hrraleakdi fameygipkh
      541 fglfyamgia lmmegvlsac yhvcpnysnf qfdtsfmymi aglcmlklyq trhpdinasa
      601 ysayasfavv itltvlgvvf gkndvwfwii fsaihvlasl alstqiyymg rfkidvsdtd
      661 lgifrraamv fytdciqqcs rplymdrmvl livgnlvnws falfgliyrp rdfasymlgi
      721 ficnlllyla fyiimklrss ekvlplpvfc ivatavvwaa alyfffqnls swegtpaesr
      781 eknrecvllg ffddhdiwhf lsatalffsf lvlltldddl dvvrrdqipv f
//
LOCUS       NP_899157                148 aa            linear   ROD 27-APR-2025
DEFINITION  single-stranded DNA-binding protein, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_899157 XP_008761050 XP_342667
VERSION     NP_899157.2
DBSOURCE    REFSEQ: accession NM_183328.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Ciesielski,G.L., Bermek,O., Rosado-Ruiz,F.A., Hovde,S.L.,
            Neitzke,O.J., Griffith,J.D. and Kaguni,L.S.
  TITLE     Mitochondrial Single-stranded DNA-binding Proteins Stimulate the
            Activity of DNA Polymerase gamma by Organization of the Template
            DNA
  JOURNAL   J Biol Chem 290 (48), 28697-28707 (2015)
   PUBMED   26446790
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 148)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Korhonen,J.A., Pham,X.H., Pellegrini,M. and Falkenberg,M.
  TITLE     Reconstitution of a minimal mtDNA replisome in vitro
  JOURNAL   EMBO J 23 (12), 2423-2429 (2004)
   PUBMED   15167897
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Korhonen,J.A., Gaspari,M. and Falkenberg,M.
  TITLE     TWINKLE Has 5' -> 3' DNA helicase activity and is specifically
            stimulated by mitochondrial single-stranded DNA-binding protein
  JOURNAL   J Biol Chem 278 (49), 48627-48632 (2003)
   PUBMED   12975372
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Gupta,S. and Van Tuyle,G.C.
  TITLE     The gene and processed pseudogenes of the rat mitochondrial
            single-strand DNA-binding protein: structure and promoter strength
            analyses
  JOURNAL   Gene 212 (2), 269-278 (1998)
   PUBMED   9611270
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Tiranti,V., Rocchi,M., DiDonato,S. and Zeviani,M.
  TITLE     Cloning of human and rat cDNAs encoding the mitochondrial
            single-stranded DNA-binding protein (SSB)
  JOURNAL   Gene 126 (2), 219-225 (1993)
   PUBMED   8482537
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Hoke,G.D., Pavco,P.A., Ledwith,B.J. and Van Tuyle,G.C.
  TITLE     Structural and functional studies of the rat mitochondrial single
            strand DNA binding protein P16
  JOURNAL   Arch Biochem Biophys 282 (1), 116-124 (1990)
   PUBMED   2221914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM064958.1.
            
            On or before Apr 13, 2016 this sequence version replaced
            XP_008761050.1, NP_899157.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM064958.1, SRR8487227.26027.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..148
                     /product="single-stranded DNA-binding protein,
                     mitochondrial precursor"
                     /note="single-stranded DNA-binding protein, mitochondrial;
                     single strand DNA-binding protein P16; single-stranded DNA
                     binding protein 1, mitochondrial"
                     /calculated_mol_wt=15081
     transit_peptide 1..16
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:2221914; propagated from
                     UniProtKB/Swiss-Prot (P28042.2)"
                     /calculated_mol_wt=2108
     Region          27..>141
                     /region_name="Replication protein A, class 2b
                     aminoacyl-tRNA synthetases, and related proteins with
                     oligonucleotide/oligosaccharide (OB) fold."
                     /note="This superfamily includes two
                     oligonucleotide/oligosaccharide binding fold (OBF) domain
                     families. One of these contains the OBF domains of the
                     large (RPA1, 70kDa), middle (RPA2, RPA4, 32kDa) and small
                     (RPA3, 14 kDa) subunits of human heterotrimeric...;
                     cl09930"
                     /db_xref="CDD:471953"
     Site            order(33..36,61..63,83,85,107,116,127,130)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239942"
     Site            order(38..40,46,56,63..64,81..82,84,86,88,90,104..105,113,
                     115,117..118,131,133)
                     /site_type="other"
                     /note="ssDNA binding site [nucleotide binding]"
                     /db_xref="CDD:239942"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CYR0; propagated from
                     UniProtKB/Swiss-Prot (P28042.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04837; propagated from
                     UniProtKB/Swiss-Prot (P28042.2)"
     Site            order(107,109,111,138)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239942"
     Site            113
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q04837; propagated from
                     UniProtKB/Swiss-Prot (P28042.2)"
     CDS             1..148
                     /gene="Ssbp1"
                     /gene_synonym="Mt-SSB; mtSSB; Ssbp"
                     /coded_by="NM_183328.3:73..519"
                     /db_xref="GeneID:54304"
                     /db_xref="RGD:3760"
ORIGIN      
        1 mfrrpvlqvf rqfvrqesev asslvlersl nrvqllgrvg qdpvmrqveg knpvtifsla
       61 tnemwrsgdn eayqmgdvsq kttwhrisvf rpglrdvayq yvkkgarifv egkvdygeym
      121 dknnvrrqat tiiadniifl sdqarekp
//
LOCUS       NP_598225               2102 aa            linear   ROD 27-APR-2025
DEFINITION  general transcription factor 3C polypeptide 1 [Rattus norvegicus].
ACCESSION   NP_598225 XP_006230267
VERSION     NP_598225.2
DBSOURCE    REFSEQ: accession NM_133541.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2102)
  AUTHORS   Vannini,A.
  TITLE     A structural perspective on RNA polymerase I and RNA polymerase III
            transcription machineries
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 258-264 (2013)
   PUBMED   23031840
  REMARK    Review article
REFERENCE   2  (residues 1 to 2102)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 2102)
  AUTHORS   de Planell-Saguer,M., Schroeder,D.G., Rodicio,M.C., Cox,G.A. and
            Mourelatos,Z.
  TITLE     Biochemical and genetic evidence for a role of IGHMBP2 in the
            translational machinery
  JOURNAL   Hum Mol Genet 18 (12), 2115-2126 (2009)
   PUBMED   19299493
REFERENCE   4  (residues 1 to 2102)
  AUTHORS   Dumay-Odelot,H., Marck,C., Durrieu-Gaillard,S., Lefebvre,O.,
            Jourdain,S., Prochazkova,M., Pflieger,A. and Teichmann,M.
  TITLE     Identification, molecular cloning, and characterization of the
            sixth subunit of human transcription factor TFIIIC
  JOURNAL   J Biol Chem 282 (23), 17179-17189 (2007)
   PUBMED   17409385
REFERENCE   5  (residues 1 to 2102)
  AUTHORS   Lagna,G., Kovelman,R., Sukegawa,J. and Roeder,R.G.
  TITLE     Cloning and characterization of an evolutionarily divergent
            DNA-binding subunit of mammalian TFIIIC
  JOURNAL   Mol Cell Biol 14 (5), 3053-3064 (1994)
   PUBMED   8164661
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Sep 4, 2015 this sequence version replaced
            XP_006230267.1, NP_598225.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L28801.1, SRR26360194.1989805.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2102
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..2102
                     /product="general transcription factor 3C polypeptide 1"
                     /note="TFIIIC 220 kDa subunit; TFIIIC box B-binding
                     subunit; transcription factor IIIC subunit alpha;
                     transcription factor IIIC 220 kDa subunit; general
                     transcription factor III C 1; general transcription factor
                     IIIC, polypeptide 1, alpha"
                     /calculated_mol_wt=237455
     Region          174..250
                     /region_name="B-block_TFIIIC"
                     /note="B-block binding subunit of TFIIIC; pfam04182"
                     /db_xref="CDD:367858"
     Region          473..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Region          587..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Region          610..706
                     /region_name="Tau138_eWH"
                     /note="extended winged-helix domain of tau138 and related
                     proteins; cd16169"
                     /db_xref="CDD:320085"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12789; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     Region          717..771
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Region          818..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Site            1062
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12789; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     Region          1186..1238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Site            1195
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K284; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     Region          1597..1627
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Site            1624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12789; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     Region          1823..1881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Site            1853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12789; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     Region          1893..1928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63505.1)"
     Site            1893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K284; propagated from
                     UniProtKB/Swiss-Prot (Q63505.1)"
     CDS             1..2102
                     /gene="Gtf3c1"
                     /gene_synonym="TF3C-alpha; TFIIIC220"
                     /coded_by="NM_133541.2:53..6361"
                     /db_xref="GeneID:171063"
                     /db_xref="RGD:621048"
ORIGIN      
        1 mdalesllde valegldglc lpalwsrles rspafplple pytqeflwra lvthpgisfy
       61 eeprerpdlq lqdryeeidl etgilesrrd pvtledvypi hmilenkdgi qgscryfker
      121 kditssirsk clqprctmve afsrwgkkli ivasqdmryr aliglegdpd lklpdfsyci
      181 lerlgrsrwq gelqrdlhtt afkvdagklh yhrkilnkng litmqshvir lptgaqqhsi
      241 llllnrfhvd rrskydilme klsmmlstrs nqietlgklr eelglcertf krlyqymlna
      301 glakvvslpl qeihpecgpc ktkkgtdvmv rclkllkefr rkmeddhddd ddeeaiskav
      361 ppvdivferd mltqtyelie rrgtkgisqa eirvamnvgk learmlcrll qrfkvvkgfm
      421 edegrqrttk yiscvfaees dlsrqyarek argellttvs lasvqdeslm pegeeaflsd
      481 seseeesscs gkrrgrgsrg hsrasgdagp gsrphhstpa kggwkvlnlh plkkpksaav
      541 ersrrssacr dgldtsssse lnipfdphsm dshsgdiavi eevrldnpke gggsqkggrh
      601 gsgqdkphkt yrllkrrnli ieavtnlrli eslftiqkmi mdqekqegvs tkcckksiir
      661 lvrnlseegl lrlyrttviq dgikkkvdlv vhpsmdqndp lvrsaieqvr frisnsstan
      721 rvkvppapap qeeaeegnqe pevpsrsads eantsskpes trvkktdekm gitplknykp
      781 vivpglgrsi gflpkmprlr vmhlflwylv yghpashtge qptfhserkt gkqepsrpgv
      841 qpssgddwds seaknstess sweaemelst ervyvdeisw mryvppipih rdfgfgwalv
      901 sdillclpls ifvqvvqvsy kvdnledfln dplkkhtlir flprhirqql lykrryifsv
      961 venlqrlcym gllqfgptek fqdkdqvfvf lkknavivdt ticdphynla hssrpferrl
     1021 yvldsmqdve sywfdlqcic lntplgvvrc pcaqkicpdp gsdpegslrk eqesamdkhn
     1081 lerkcamley ttgsrevvde glvpgdglga agldssfyah lkrnwvwtsy iinkarknnt
     1141 sengltgrlq tflskrpmpl gsggsgrlpl wsegkadael cadkeehfel dreptpgrnr
     1201 kvrggksqkr krlkkepirk tkrrrrgehp eakskklryq deadqnalrm mtrlrvswsm
     1261 qedgllmlcr iasnvlntkv kgpfvtwqvv rdilhatfee sldktshsvg rraryivknp
     1321 qafmnykvcl aevyqdkalv gdfmsrkdny edpkvcakef kefveklkek fssglrnpnl
     1381 eipdtlqelf akyrvlaigd ekdrvrkede lnsvedihfl vlqnliqstl slsnsqsnsc
     1441 qsfqifrlyr efrepvlvra fmecqkrslv nrrrvshsqg pkknravpfv pmsyqlsqsy
     1501 yklftwrfpt tvctesfqfy drlrangild qpdhfsfkdm dsndpssdlv afsldspggh
     1561 cvtalalfsl gllsvdvrip eqivvvdssm vesevmkslg kdggldddde eedldegsgt
     1621 krqsvevkah qashtkyllm rgyytvpgmv strnlnpnds ivvnscqvkf rlrntpapth
     1681 lgptgptatp leelqagpsc lpasftslvd pqlhtrcpee fahqmaqsgy spedvaasle
     1741 ilqavaaadc fgvdreklsr qfsalekiad krtrtfldyi qdlleqqqvm evggntvrlv
     1801 amasaqpwll psvrlkdvei dtkasgddsq srlpagssie dhtsegapip pvssngtkkr
     1861 pycsiqspet daeeatrlpa kkptlqdvcv aasprpgtee qteaqaqfaa pedagaegpr
     1921 qesqesvgvs gleqlgcefq lpensedprg ltesnmaqva wesgcervcf vgrpwrgvdg
     1981 rlnmpvckgm meavlyhims rpgvpescll qyyqgvlqpv avlellrgle slgciqkrml
     2041 kkpasvslfs rpvveglgqa seaealscqg stvtfyeptl dctirlgrvf phdinwnkwi
     2101 hl
//
LOCUS       NP_001257862             439 aa            linear   ROD 27-APR-2025
DEFINITION  hepatocyte nuclear factor 4-alpha isoform 3 [Rattus norvegicus].
ACCESSION   NP_001257862
VERSION     NP_001257862.1
DBSOURCE    REFSEQ: accession NM_001270933.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Melis,M., Marino,R., Tian,J., Johnson,C., Sethi,R., Oertel,M.,
            Fox,I.J. and Locker,J.
  TITLE     Mechanism and Effect of HNF4alpha Decrease in a Rat Model of
            Cirrhosis and Liver Failure
  JOURNAL   Cell Mol Gastroenterol Hepatol 17 (3), 453-479 (2024)
   PUBMED   37993018
  REMARK    GeneRIF: Mechanism and Effect of HNF4alpha Decrease in a Rat Model
            of Cirrhosis and Liver Failure.
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhan,H., Zhang,Q., Zhang,C., Cheng,J., Yang,Y., Liu,C., Li,S.,
            Wang,C., Yang,J., Ge,H., Zhou,D., Li,B., Wei,H. and Hu,C.
  TITLE     Targeted Activation of HNF4alpha by AMPK Inhibits Apoptosis and
            Ameliorates Neurological Injury Caused by Cardiac Arrest in Rats
  JOURNAL   Neurochem Res 48 (10), 3129-3145 (2023)
   PUBMED   37338793
  REMARK    GeneRIF: Targeted Activation of HNF4alpha by AMPK Inhibits
            Apoptosis and Ameliorates Neurological Injury Caused by Cardiac
            Arrest in Rats.
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Fan,J.Y., Dama,G., Liu,Y.L., Guo,W.Y. and Lin,J.T.
  TITLE     [Combinational Overexpression of Foxa3 and Hnf4alpha Enhance the
            Proliferation and Prolong the Functional Maintenance of Primary
            Hepatocytes]
  JOURNAL   Mol Biol (Mosk) 57 (4), 668-670 (2023)
   PUBMED   37528786
  REMARK    GeneRIF: [Combinational Overexpression of Foxa3 and Hnf4alpha
            Enhance the Proliferation and Prolong the Functional Maintenance of
            Primary Hepatocytes].
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Hu,C., Jing,R., Wen,C., Qi,T., Bai,X., Wang,Y., Shao,Y. and Pei,C.
  TITLE     HNF4A Negatively Regulated Posterior Capsular Opacification via
            Transcriptional Inhibition of MMP2
  JOURNAL   Curr Eye Res 48 (7), 627-638 (2023)
   PUBMED   36988559
  REMARK    GeneRIF: HNF4A Negatively Regulated Posterior Capsular
            Opacification via Transcriptional Inhibition of MMP2.
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Zheng,X., Wang,G., Yuan,J., Li,N., Yan,B., Yan,J. and Sheng,Y.
  TITLE     hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion Injury Via
            Targeting HNF4alpha
  JOURNAL   Turk J Gastroenterol 33 (7), 596-605 (2022)
   PUBMED   35879917
  REMARK    GeneRIF: hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion
            Injury Via Targeting HNF4alpha.
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Ginsburg,G.S., Ozer,J. and Karathanasis,S.K.
  TITLE     Intestinal apolipoprotein AI gene transcription is regulated by
            multiple distinct DNA elements and is synergistically activated by
            the orphan nuclear receptor, hepatocyte nuclear factor 4
  JOURNAL   J Clin Invest 96 (1), 528-538 (1995)
   PUBMED   7615825
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Chen,W.S., Manova,K., Weinstein,D.C., Duncan,S.A., Plump,A.S.,
            Prezioso,V.R., Bachvarova,R.F. and Darnell,J.E. Jr.
  TITLE     Disruption of the HNF-4 gene, expressed in visceral endoderm, leads
            to cell death in embryonic ectoderm and impaired gastrulation of
            mouse embryos
  JOURNAL   Genes Dev 8 (20), 2466-2477 (1994)
   PUBMED   7958910
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Ang,S.L., Wierda,A., Wong,D., Stevens,K.A., Cascio,S., Rossant,J.
            and Zaret,K.S.
  TITLE     The formation and maintenance of the definitive endoderm lineage in
            the mouse: involvement of HNF3/forkhead proteins
  JOURNAL   Development 119 (4), 1301-1315 (1993)
   PUBMED   8306889
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Hata,S., Tsukamoto,T. and Osumi,T.
  TITLE     A novel isoform of rat hepatocyte nuclear factor 4 (HNF-4)
  JOURNAL   Biochim Biophys Acta 1131 (2), 211-213 (1992)
   PUBMED   1610903
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Sladek,F.M., Zhong,W.M., Lai,E. and Darnell,J.E. Jr.
  TITLE     Liver-enriched transcription factor HNF-4 is a novel member of the
            steroid hormone receptor superfamily
  JOURNAL   Genes Dev 4 (12B), 2353-2365 (1990)
   PUBMED   2279702
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FJ608816.1, EF193390.1, JAXUCZ010000003.1 and FQ095211.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and has
            two coding region differences, compared to variant 1. The resulting
            isoform (3, also known as HNF4alpha10) is shorter, has a distinct
            N-terminus and lacks an internal segment in the C-terminal region,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ608816.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Rattus norvegicus"
                     /strain="NEDH"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..439
                     /product="hepatocyte nuclear factor 4-alpha isoform 3"
                     /note="alpha transcription factor 4; HNF-4-alpha;
                     transcription factor 14; transcription factor HNF-4;
                     nuclear receptor subfamily 2 group A member 1; TCF-14;
                     hepatic nuclear factor 4, alpha"
                     /calculated_mol_wt=48663
     Region          35..110
                     /region_name="NR_DBD_HNF4A"
                     /note="DNA-binding domain of heptocyte nuclear factor 4
                     (HNF4) is composed of two C4-type zinc fingers; cd06960"
                     /db_xref="CDD:143518"
     Site            order(35,38,52,55,71,77,87,90)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143518"
     Site            order(41,45..47,53..54,56,58,60..61,64,84..85,88,91,
                     104..106,108)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143518"
     Site            order(72,85..86,88)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:143518"
     Region          126..348
                     /region_name="NR_LBD_HNF4_like"
                     /note="The ligand binding domain of heptocyte nuclear
                     factor 4, which is explosively expanded in nematodes;
                     cd06931"
                     /db_xref="CDD:132729"
     Site            order(159,165,169,203,207,210,220..221,239,329..330,333)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132729"
     Site            order(174,178,188..189,191..192,195..196,343..344,
                     347..348)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132729"
     Site            order(246,267,273,287..288,291..292,295..296,306..307,
                     309..311,313..314,316..318,320..321,324)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132729"
     CDS             1..439
                     /gene="Hnf4a"
                     /gene_synonym="Hnf4; Hnf4alpha"
                     /coded_by="NM_001270933.1:256..1575"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25735"
                     /db_xref="RGD:2810"
ORIGIN      
        1 msdrgqgflq dppdtspseg anlnssnslg vsalcaicgd ratgkhygas scdgckgffr
       61 rsvrknhmys crfsrqcvvd kdkrnqcryc rlkkcfragm kkeavqnerd ristrrssye
      121 dsslpsinal lqaevlsqqi tspisgingd irakrianit dvcesmkeql lvlvewakyi
      181 pafcellldd qvallrahag ehlllgatkr smvfkdvlll gndyivprhc pelaemsrvs
      241 irildelvlp fqelqiddne yaclkaiiff dpdakglsdp gkikrlrsqv qvsledyind
      301 rqydsrgrfg elllllptlq sitwqmieqi qfiklfgmak idnllqemll ggsasdapha
      361 hhplhphlmq ehmgtnviva ntmpshlsng qmstpetpqp sppsgsgses ykllpgaitt
      421 ivkppsaipq ptitkqeai
//
LOCUS       NP_690062                553 aa            linear   ROD 27-APR-2025
DEFINITION  homeobox and leucine zipper protein Homez [Rattus norvegicus].
ACCESSION   NP_690062
VERSION     NP_690062.3
DBSOURCE    REFSEQ: accession NM_152849.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Bayarsaihan,D., Enkhmandakh,B., Makeyev,A., Greally,J.M.,
            Leckman,J.F. and Ruddle,F.H.
  TITLE     Homez, a homeobox leucine zipper gene specific to the vertebrate
            lineage
  JOURNAL   Proc Natl Acad Sci U S A 100 (18), 10358-10363 (2003)
   PUBMED   12925734
  REMARK    GeneRIF: Homez is a homeobox leucine zipper gene specific to the
            vertebrate lineage.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC084701.1.
            
            On Sep 13, 2012 this sequence version replaced NP_690062.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC084701.1, BC085694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..553
                     /product="homeobox and leucine zipper protein Homez"
                     /note="homeodomain leucine zipper-containing factor;
                     homeodomain leucine zipper-encoding; homeodomain-leucine
                     zipper protein HOMEZ"
                     /calculated_mol_wt=61757
     Region          62..109
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Region          346..403
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(346..349,351,368,374,387,389..390,393..394,396..398,
                     400..401)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(347,350,390,393..394,397)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          448..495
                     /region_name="Homez"
                     /note="Homeodomain leucine-zipper encoding, Homez;
                     pfam11569"
                     /db_xref="CDD:463297"
     CDS             1..553
                     /gene="Homez"
                     /coded_by="NM_152849.2:26..1687"
                     /db_xref="GeneID:260325"
                     /db_xref="RGD:628904"
ORIGIN      
        1 mrtrhperav segykseqvm spnkdsssln ssgaglvclp pvseelqlvw tqavqtseld
       61 gnehllqafs yfpypsladi allclrhglq mekvktwfma qrlrcgisws seeieetrar
      121 vvyhrdqllf ksllsfthha vrppqemppv tppeqvalgl rplalseptq mkglkvepee
      181 pfqvsqlpln hqkvkeplmm gsrtlnhqsd cqdlqisgls keqagggpdq scgggtaswn
      241 hsiavhqpdk splislldns ckeesepsgt ppsssasspf qvlangttat pkplqplgyi
      301 pqsfspseqa lspqveplws qrlrnnsvps rvgpteylsp dmqhqrktkr ktkeqlailk
      361 sfflqcqwar redyhkleqi tglprpeiiq wfgdtryalk hgqlkwfrdn avlgtpsfqd
      421 paistsstrs lkewaktppl papppppdir plerywaahq qlqeadilkl sqasrlstqq
      481 vldwfdsrlp kpaevvvcld eeeeeedeel pedgeeeeee eeeedddgls cgqkdhgllt
      541 ngavergsll tvg
//
LOCUS       NP_446098                761 aa            linear   ROD 27-APR-2025
DEFINITION  neutral ceramidase [Rattus norvegicus].
ACCESSION   NP_446098
VERSION     NP_446098.1
DBSOURCE    REFSEQ: accession NM_053646.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Xu,Y.N., Wang,Z., Zhang,S.K., Xu,J.R., Pan,Z.X., Wei,X., Wen,H.H.,
            Luo,Y.S., Guo,M.J. and Zhu,Q.
  TITLE     Low-grade elevation of palmitate and lipopolysaccharide
            synergistically induced beta-cell damage via inhibition of neutral
            ceramidase
  JOURNAL   Mol Cell Endocrinol 539, 111473 (2022)
   PUBMED   34610358
  REMARK    GeneRIF: Low-grade elevation of palmitate and lipopolysaccharide
            synergistically induced beta-cell damage via inhibition of neutral
            ceramidase.
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Sakamoto,W., Coant,N., Canals,D., Obeid,L.M. and Hannun,Y.A.
  TITLE     Functions of neutral ceramidase in the Golgi apparatus
  JOURNAL   J Lipid Res 59 (11), 2116-2125 (2018)
   PUBMED   30154232
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Airola,M.V., Allen,W.J., Pulkoski-Gross,M.J., Obeid,L.M.,
            Rizzo,R.C. and Hannun,Y.A.
  TITLE     Structural Basis for Ceramide Recognition and Hydrolysis by Human
            Neutral Ceramidase
  JOURNAL   Structure 23 (8), 1482-1491 (2015)
   PUBMED   26190575
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Zhu,Q., Kang,J., Miao,H., Feng,Y., Xiao,L., Hu,Z., Liao,D.F.,
            Huang,Y., Jin,J. and He,S.
  TITLE     Low-dose cytokine-induced neutral ceramidase secretion from INS-1
            cells via exosomes and its anti-apoptotic effect
  JOURNAL   FEBS J 281 (12), 2861-2870 (2014)
   PUBMED   24798654
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Novgorodov,S.A., Wu,B.X., Gudz,T.I., Bielawski,J.,
            Ovchinnikova,T.V., Hannun,Y.A. and Obeid,L.M.
  TITLE     Novel pathway of ceramide production in mitochondria: thioesterase
            and neutral ceramidase produce ceramide from sphingosine and
            acyl-CoA
  JOURNAL   J Biol Chem 286 (28), 25352-25362 (2011)
   PUBMED   21613224
  REMARK    GeneRIF: Novel pathway of ceramide production in mitochondria:
            thioesterase and neutral ceramidase produce ceramide from
            sphingosine and acyl-CoA.
REFERENCE   6  (residues 1 to 761)
  AUTHORS   El Bawab,S., Birbes,H., Roddy,P., Szulc,Z.M., Bielawska,A. and
            Hannun,Y.A.
  TITLE     Biochemical characterization of the reverse activity of rat brain
            ceramidase. A CoA-independent and fumonisin B1-insensitive ceramide
            synthase
  JOURNAL   J Biol Chem 276 (20), 16758-16766 (2001)
   PUBMED   11278489
REFERENCE   7  (residues 1 to 761)
  AUTHORS   El Bawab,S., Roddy,P., Qian,T., Bielawska,A., Lemasters,J.J. and
            Hannun,Y.A.
  TITLE     Molecular cloning and characterization of a human mitochondrial
            ceramidase
  JOURNAL   J Biol Chem 275 (28), 21508-21513 (2000)
   PUBMED   10781606
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Tani,M., Okino,N., Mori,K., Tanigawa,T., Izu,H. and Ito,M.
  TITLE     Molecular cloning of the full-length cDNA encoding mouse neutral
            ceramidase. A novel but highly conserved gene family of
            neutral/alkaline ceramidases
  JOURNAL   J Biol Chem 275 (15), 11229-11234 (2000)
   PUBMED   10753931
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Tani,M., Okino,N., Mitsutake,S., Tanigawa,T., Izu,H. and Ito,M.
  TITLE     Purification and characterization of a neutral ceramidase from
            mouse liver. A single protein catalyzes the reversible reaction in
            which ceramide is both hydrolyzed and synthesized
  JOURNAL   J Biol Chem 275 (5), 3462-3468 (2000)
   PUBMED   10652340
REFERENCE   10 (residues 1 to 761)
  AUTHORS   El Bawab,S., Bielawska,A. and Hannun,Y.A.
  TITLE     Purification and characterization of a membrane-bound nonlysosomal
            ceramidase from rat brain
  JOURNAL   J Biol Chem 274 (39), 27948-27955 (1999)
   PUBMED   10488143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and AB057433.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB057433.1, SRR26643298.7743.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..761
                     /product="neutral ceramidase"
                     /EC_number="3.5.1.23"
                     /note="NCDase; acylsphingosine deacylase 2;
                     neutral/alkaline ceramidase; N-acylsphingosine
                     amidohydrolase (non-lysosomal ceramidase) 2"
                     /calculated_mol_wt=83357
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     Region          43..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            51
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            57
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            58
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            60
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            61
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            63
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            64
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            68
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            69
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            71
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            79..80
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000269|PubMed:12499379;
                     propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     mat_peptide     80..761
                     /product="Neutral ceramidase soluble form.
                     /evidence=ECO:0000269|PubMed:12499379. /id=PRO_0000247104"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
                     /calculated_mol_wt=74953
     Region          83..589
                     /region_name="Ceramidase_alk"
                     /note="Neutral/alkaline non-lysosomal ceramidase,
                     N-terminal; pfam04734"
                     /db_xref="CDD:461415"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q91XT9.1)"
     Region          591..758
                     /region_name="Ceramidse_alk_C"
                     /note="Neutral/alkaline non-lysosomal ceramidase,
                     C-terminal; pfam17048"
                     /db_xref="CDD:465340"
     Region          751..761
                     /region_name="Required for correct folding and
                     localization. /evidence=ECO:0000269|PubMed:15123644"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XT9.1)"
     CDS             1..761
                     /gene="Asah2"
                     /coded_by="NM_053646.2:122..2407"
                     /db_xref="GeneID:114104"
                     /db_xref="RGD:69410"
ORIGIN      
        1 makrtfssle aflifllvmm taitvalltl lfvtsgtien hkdsgnhwvs ttqgptttqs
       61 spttqtpttq tpdlppsqnf sgyyigvgra dctgqvsdin lmgygkngqn aqglltrlfs
      121 rafiladpdg snrmafvsve lcmisqrlrl evlkrlqsky gslyrrdnvi lsaththsgp
      181 agffqytlyi lasegfsnrt fqyivsgivk sidiahtnlk pgkvlinkgn vanvqinrsp
      241 ssylqnppse raryssdtdk emvvlklvdl ngedlglisw favhpvsmnn snhlvnsdnm
      301 gyaaylfeqe knrgylpgqg pfvagfassn lgdvspnilg phcvntgesc dndkstcpsg
      361 gpsmcmasgp gqdmfesthi igrviyqkak elhasasqev tgpvltahqw vnmtdvsvql
      421 nathtvktck aalgysfaag tidgvsglni tqgttegnlf wdtlrdqllg kpseeiiecq
      481 kpkpilihtg eltkphpwqp divdiqivtl gslaiaaipg efttmsgrrl reavkkefal
      541 ygmkdmtvvi aglsnvythy ittyeeyqaq ryeaastiyg phtlsayiql fralakaiat
      601 dtvanmssgp eppffknlig slipniadra pigkqfgdvl qpakpeyrvg evvevvfvga
      661 npknsaenqt hqtfltveky edsvanwqim hndaswetrf ywhkgvlgls natihwhipd
      721 talpgvyrir yfghnrkqel lkpavilafe gisspfeivt t
//
LOCUS       NP_001008884             264 aa            linear   ROD 27-APR-2025
DEFINITION  rano class II histocompatibility antigen, D-1 beta chain precursor
            [Rattus norvegicus].
ACCESSION   NP_001008884 XP_215333
VERSION     NP_001008884.1
DBSOURCE    REFSEQ: accession NM_001008884.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Toyo-Oka,L., Mahasirimongkol,S., Yanai,H., Mushiroda,T.,
            Wattanapokayakit,S., Wichukchinda,N., Yamada,N., Smittipat,N.,
            Juthayothin,T., Palittapongarnpim,P., Nedsuwan,S., Kantipong,P.,
            Takahashi,A., Kubo,M., Sawanpanyalert,P. and Tokunaga,K.
  TITLE     Strain-based HLA association analysis identified HLA-DRB1*09:01
            associated with modern strain tuberculosis
  JOURNAL   HLA 90 (3), 149-156 (2017)
   PUBMED   28612994
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Brill,L., Mandel,M., Karussis,D., Petrou,P., Miller,K., Ben-Hur,T.,
            Karni,A., Paltiel,O., Israel,S. and Vaknin-Dembinsky,A.
  TITLE     Increased occurrence of anti-AQP4 seropositivity and unique HLA
            Class II associations with neuromyelitis optica (NMO), among Muslim
            Arabs in Israel
  JOURNAL   J Neuroimmunol 293, 65-70 (2016)
   PUBMED   27049564
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Hernandez,E.G., Granados,J., Partida-Rodriguez,O., Valenzuela,O.,
            Rascon,E., Magana,U., Escamilla-Tilch,M., Lopez-Reyes,A.,
            Nieves-Ramirez,M., Gonzalez,E., Moran,P., Rojas,L., Valadez,A.,
            Luna,A., Estrada,F.J., Maldonado,C. and Ximenez,C.
  TITLE     Prevalent HLA Class II Alleles in Mexico City Appear to Confer
            Resistance to the Development of Amebic Liver Abscess
  JOURNAL   PLoS One 10 (5), e0126195 (2015)
   PUBMED   25938667
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Esmaeilzadeh,H., Nabavi,M., Amirzargar,A.A., Aryan,Z., Arshi,S.,
            Bemanian,M.H., Fallahpour,M., Mortazavi,N. and Rezaei,N.
  TITLE     HLA-DRB and HLA-DQ genetic variability in patients with
            aspirin-exacerbated respiratory disease
  JOURNAL   Am J Rhinol Allergy 29 (3), e63-e69 (2015)
   PUBMED   25975240
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Dunstan,S.J., Hue,N.T., Han,B., Li,Z., Tram,T.T., Sim,K.S.,
            Parry,C.M., Chinh,N.T., Vinh,H., Lan,N.P., Thieu,N.T., Vinh,P.V.,
            Koirala,S., Dongol,S., Arjyal,A., Karkey,A., Shilpakar,O.,
            Dolecek,C., Foo,J.N., Phuong le,T., Lanh,M.N., Do,T., Aung,T.,
            Hon,D.N., Teo,Y.Y., Hibberd,M.L., Anders,K.L., Okada,Y.,
            Raychaudhuri,S., Simmons,C.P., Baker,S., de Bakker,P.I.,
            Basnyat,B., Hien,T.T., Farrar,J.J. and Khor,C.C.
  TITLE     Variation at HLA-DRB1 is associated with resistance to enteric
            fever
  JOURNAL   Nat Genet 46 (12), 1333-1336 (2014)
   PUBMED   25383971
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Ghosh,P., Amaya,M., Mellins,E. and Wiley,D.C.
  TITLE     The structure of an intermediate in class II MHC maturation: CLIP
            bound to HLA-DR3
  JOURNAL   Nature 378 (6556), 457-462 (1995)
   PUBMED   7477400
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Riberdy,J.M., Newcomb,J.R., Surman,M.J., Barbosa,J.A. and
            Cresswell,P.
  TITLE     HLA-DR molecules from an antigen-processing mutant cell line are
            associated with invariant chain peptides
  JOURNAL   Nature 360 (6403), 474-477 (1992)
   PUBMED   1448172
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Mizuki,N., Inoko,H., Mizuki,N., Tanaka,H., Kera,J., Tsuiji,K. and
            Ohno,S.
  TITLE     Human leukocyte antigen serologic and DNA typing of Behcet's
            disease and its primary association with B51
  JOURNAL   Invest Ophthalmol Vis Sci 33 (12), 3332-3340 (1992)
   PUBMED   1358857
REFERENCE   9  (residues 1 to 264)
  AUTHORS   De Palma,J.
  TITLE     Cause & effect, or ... there are lies, damn lies, and statistics
  JOURNAL   Nephrol News Issues 6 (11), 27-28 (1992)
   PUBMED   1300424
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Syha-Jedelhauser,J. and Reske,K.
  TITLE     Sequence of rat cDNA clone pLR beta 112 coding for the RT1.D beta I
            chain
  JOURNAL   Nucleic Acids Res 18 (15), 4598 (1990)
   PUBMED   2388838
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO563535.1, AF084933.1 and CV111238.1.
            
            On Jan 6, 2005 this sequence version replaced XP_215333.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ233396.1, FQ233801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494, SAMN13663593
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..264
                     /product="rano class II histocompatibility antigen, D-1
                     beta chain precursor"
                     /note="rano class II histocompatibility antigen, D-1 beta
                     chain; RT1-D beta; MHC class II RT1D beta1 chain antigen;
                     RT1 class II histocompatibility antigen, D-1 beta chain"
                     /calculated_mol_wt=27581
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2638
     Region          40..111
                     /region_name="MHC_II_beta"
                     /note="Class II histocompatibility antigen, beta domain;
                     smart00921"
                     /db_xref="CDD:197989"
     Region          122..216
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          155..159
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          186..190
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          197..202
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          212..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..264
                     /gene="RT1-Db1"
                     /gene_synonym="Db1; RT1-Db; RT1-Db1n"
                     /coded_by="NM_001008884.2:65..859"
                     /db_xref="GeneID:294270"
                     /db_xref="RGD:1593282"
ORIGIN      
        1 mvwlardscv aavillltvl sppvalvrdp tprfleqyks ecyfyngtqr vrllvryiyn
       61 reeytrfdsd vgefravtel grrdteyynk qkeyierera avdticrhny eisdrflvpr
      121 tvepkvtvyp sktqplkhhn llvcsvsdfy pgsvevrwfr ngeeekdglv stglipngdw
      181 tfqllvmlem vpqggevytc qvehpsltsp vrvewkaqst saqnkkmsgv ggivlgllfl
      241 gaglfvyfrn qkgqsglqpt glln
//
LOCUS       NP_001258006             196 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 6 precursor [Rattus norvegicus].
ACCESSION   NP_001258006
VERSION     NP_001258006.1
DBSOURCE    REFSEQ: accession NM_001271077.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1 and U67130.1.
            
            Transcript Variant: This variant (6) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (6)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: U01245.2 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN06621351,
                                    SAMN09345331 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..196
                     /product="amelogenin, X isoform isoform 6 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=20292
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          28..196
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     CDS             1..196
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271077.1:67..657"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqpy psygyepmgg
       61 wlhhqiipvl sqqhppshtl qphhhlpvvp aqqpvapqqp mmpvpghhsm tptqhhqpni
      121 ppsaqqpfqq pfqpqaippq shqpmqpqsp lhpmqplapq pplpplfsmq plspilpelp
      181 leawpatdkt kreevd
//
LOCUS       NP_001005535             589 aa            linear   ROD 27-APR-2025
DEFINITION  probable ATP-dependent RNA helicase DDX59 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001005535 XP_213982
VERSION     NP_001005535.1
DBSOURCE    REFSEQ: accession NM_001005535.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY317721.1, DY310785.1, BC081871.1 and CR477587.1.
            
            On Oct 8, 2004 this sequence version replaced XP_213982.2.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment, compared to
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132288, SAMD00155312
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..589
                     /product="probable ATP-dependent RNA helicase DDX59
                     isoform 2"
                     /EC_number="3.6.4.13"
                     /note="probable ATP-dependent RNA helicase DDX59; DEAD box
                     protein 59; DEAD (Asp-Glu-Ala-Asp) box polypeptide 59;
                     zinc finger HIT domain-containing protein 5"
                     /calculated_mol_wt=64935
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG7.1)"
     Region          48..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG7.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T1V6; propagated from
                     UniProtKB/Swiss-Prot (Q66HG7.1)"
     Region          89..563
                     /region_name="PLN00206"
                     /note="DEAD-box ATP-dependent RNA helicase; Provisional"
                     /db_xref="CDD:215103"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T1V6; propagated from
                     UniProtKB/Swiss-Prot (Q66HG7.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T1V6; propagated from
                     UniProtKB/Swiss-Prot (Q66HG7.1)"
     Region          203..231
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG7.1)"
     Region          323..326
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG7.1)"
     CDS             1..589
                     /gene="Ddx59"
                     /coded_by="NM_001005535.2:140..1909"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289402"
                     /db_xref="RGD:1359520"
ORIGIN      
        1 mfvprslklk rnsnddlksc eakkskpeaa glqlegnret lvlesvtkea vtadrpgsas
       61 stsspscqla evcstgpdqg vkdshpseep vksfsktqrw pepgepvcvv cgrygeyicd
      121 ktdedvcsle ckakhllqvk eeegslkpss pqgaasepes pldafyvyke hpfivalrdd
      181 qietlkqqlg isvqgqevar piidfehcgf petlnqnlkk sgyevptpiq mqmipvgllg
      241 rdilasadtg sgktaafllp viiralpedk tpsaliltpt relaiqierq akelmrglpr
      301 mktvllvggl plppqlyrlq qhvkadtmlk mgfqqqvldv lehtpsdcqt vlvsatipds
      361 idqladqllh npvrivtgdk nlpcssvrqi ilwvedpakk kklfeilndq klfkppvlvf
      421 vdcklgadll seavqkitgl sstsihseks qverreilkg llegdyevvv stgilgrgld
      481 lvnvklvvnf dmpssldeyv hqvgrvgrlg qngtaitfin nnskrlfwdv akrvkptgsi
      541 lppqllnspy lheqkrkeqq kdrqtqsslv tganlmdiir kheksssqk
//
LOCUS       NP_062006                704 aa            linear   ROD 27-APR-2025
DEFINITION  synapsin-1 isoform a [Rattus norvegicus].
ACCESSION   NP_062006
VERSION     NP_062006.1
DBSOURCE    REFSEQ: accession NM_019133.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Ma,W., Lu,K., Liang,H.M. and Zhang,J.Y.
  TITLE     Synapsin 1 Ameliorates Cognitive Impairment and Neuroinflammation
            in Rats with Alzheimer's Disease: An Experimental and
            Bioinformatics Study
  JOURNAL   Curr Alzheimer Res 20 (9), 648-659 (2023)
   PUBMED   38213171
  REMARK    GeneRIF: Synapsin 1 Ameliorates Cognitive Impairment and
            Neuroinflammation in Rats with Alzheimer's Disease: An Experimental
            and Bioinformatics Study.
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Yang,H.J., Chen,P.C., Huang,C.T., Cheng,T.L., Hsu,S.P., Chen,C.Y.,
            Lu,J.C. and Wang,C.T.
  TITLE     The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core
            Vesicle Release
  JOURNAL   J Neurosci 41 (13), 2828-2841 (2021)
   PUBMED   33632727
  REMARK    GeneRIF: The Phosphoprotein Synapsin Ia Regulates the Kinetics of
            Dense-Core Vesicle Release.
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Zhang,S., Yan,M.L., Yang,L., An,X.B., Zhao,H.M., Xia,S.N., Jin,Z.,
            Huang,S.Y., Qu,Y. and Ai,J.
  TITLE     MicroRNA-153 impairs hippocampal synaptic vesicle trafficking via
            downregulation of synapsin I in rats following chronic cerebral
            hypoperfusion
  JOURNAL   Exp Neurol 332, 113389 (2020)
   PUBMED   32580014
  REMARK    GeneRIF: MicroRNA-153 impairs hippocampal synaptic vesicle
            trafficking via downregulation of synapsin I in rats following
            chronic cerebral hypoperfusion.
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Tao-Cheng,J.H.
  TITLE     Immunogold labeling of synaptic vesicle proteins in developing
            hippocampal neurons
  JOURNAL   Mol Brain 13 (1), 9 (2020)
   PUBMED   31959215
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Liu,X., Zhang,R., Wu,Z., Si,W., Ren,Z., Zhang,S., Zhou,J. and
            Chen,D.
  TITLE     miR-134-5p/Foxp2/Syn1 is involved in cognitive impairment in an
            early vascular dementia rat model
  JOURNAL   Int J Mol Med 44 (5), 1729-1740 (2019)
   PUBMED   31545395
  REMARK    GeneRIF: The miR1345p/Foxp2/Syn1 axis was found to contribute to
            cognitive impairment in a chronic ischemiainduced early VD model,
            which may enable the development of new therapeutic strategies for
            the prevention and treatment of VD.
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Li,L., Chin,L.S., Shupliakov,O., Brodin,L., Sihra,T.S., Hvalby,O.,
            Jensen,V., Zheng,D., McNamara,J.O., Greengard,P. et al.
  TITLE     Impairment of synaptic vesicle clustering and of synaptic
            transmission, and increased seizure propensity, in synapsin
            I-deficient mice
  JOURNAL   Proc Natl Acad Sci U S A 92 (20), 9235-9239 (1995)
   PUBMED   7568108
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Cho,K.O., Hunt,C.A. and Kennedy,M.B.
  TITLE     The rat brain postsynaptic density fraction contains a homolog of
            the Drosophila discs-large tumor suppressor protein
  JOURNAL   Neuron 9 (5), 929-942 (1992)
   PUBMED   1419001
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Sudhof,T.C., Czernik,A.J., Kao,H.T., Takei,K., Johnston,P.A.,
            Horiuchi,A., Kanazir,S.D., Wagner,M.A., Perin,M.S., De Camilli,P.
            et al.
  TITLE     Synapsins: mosaics of shared and individual domains in a family of
            synaptic vesicle phosphoproteins
  JOURNAL   Science 245 (4925), 1474-1480 (1989)
   PUBMED   2506642
  REMARK    Review article
REFERENCE   9  (residues 1 to 704)
  AUTHORS   McCaffery,C.A. and DeGennaro,L.J.
  TITLE     Determination and analysis of the primary structure of the nerve
            terminal specific phosphoprotein, synapsin I
  JOURNAL   EMBO J 5 (12), 3167-3173 (1986)
   PUBMED   3028773
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Huttner,W.B., Schiebler,W., Greengard,P. and De Camilli,P.
  TITLE     Synapsin I (protein I), a nerve terminal-specific phosphoprotein.
            III. Its association with synaptic vesicles studied in a highly
            purified synaptic vesicle preparation
  JOURNAL   J Cell Biol 96 (5), 1374-1388 (1983)
   PUBMED   6404912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ084192.1, M27812.1, CO401107.1, JAXUCZ010000021.1 and BG378858.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M27812.1, X04655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..704
                     /product="synapsin-1 isoform a"
                     /note="synapsin-1"
                     /calculated_mol_wt=73858
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          1..27
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK1 and PKA.
                     /evidence=ECO:0000305|PubMed:10571231; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          15..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          29..112
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            55
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            56
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000305|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            87
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            96
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            103
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000305|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          113..420
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          115..212
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          214..416
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Site            261
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          418..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Region          421..655
                     /region_name="D, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            428
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            430
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            474
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          <496..683
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            516
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995,
                     ECO:0000269|PubMed:12438562; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            524
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            532
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            545
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17599; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P17600; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            554
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            562
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; Phosphoserine, by
                     CaMK2. /evidence=ECO:0000305|PubMed:3118371,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            576
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:10386995; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000305|PubMed:3118371; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            620
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Region          656..704
                     /region_name="E"
                     /note="propagated from UniProtKB/Swiss-Prot (P09951.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            678
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88935; propagated from
                     UniProtKB/Swiss-Prot (P09951.3)"
     CDS             1..704
                     /gene="Syn1"
                     /coded_by="NM_019133.2:99..2213"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24949"
                     /db_xref="RGD:3797"
ORIGIN      
        1 mnylrrrlsd snfmanlpng ymtdlqrpqp pppppsaasp gatpgsaaas aerastaapv
       61 aspaapspgs sggggffssl snavkqttaa aaatfseqvg ggsggagrgg aaarvllvid
      121 ephtdwakyf kgkkihgeid ikveqaefsd lnlvahangg fsvdmevlrn gvkvvrslkp
      181 dfvlirqhaf smarngdyrs lviglqyagi psvnslhsvy nfcdkpwvfa qmvrlhkklg
      241 teefplidqt fypnhkemls sttypvvvkm ghahsgmgkv kvdnqhdfqd iasvvaltkt
      301 yataepfida kydvrvqkig qnykaymrts vsgnwktntg samleqiams dryklwvdtc
      361 seifggldic avealhgkdg rdhiievvgs smpligdhqd edkqlivelv vnkmtqalpr
      421 qrdaspgrgs hsqtpspgal plgrqtsqqp agppaqqrpp pqggppqpgp gpqrqgpplq
      481 qrpppqgqqh lsglgppags plpqrlpspt aapqqsasqa tpmtqgqgrq srpvaggpga
      541 ppaarppasp spqrqagppq atrqasisgp appkvsgasp ggqqrqgppq kppgpagpir
      601 qasqagpgpr tgppttqqpr psgpgpagrp tkpqlaqkps qdvpppiiaa aggpphpqln
      661 ksqsltnafn lpepapprps lsqdevkaet irslrksfas lfsd
//
LOCUS       NP_112395                326 aa            linear   ROD 27-APR-2025
DEFINITION  thrombopoietin precursor [Rattus norvegicus].
ACCESSION   NP_112395
VERSION     NP_112395.1
DBSOURCE    REFSEQ: accession NM_031133.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Chang,C., Yang,J., Li,X., Zhao,W., Li,Y., Guo,P., Wang,G. and Xu,C.
  TITLE     Thrombopoietin Signaling Pathway Regulates Hepatocyte Activation in
            Rat Liver Regeneration
  JOURNAL   Biochem Genet 53 (9-10), 244-259 (2015)
   PUBMED   26116151
  REMARK    GeneRIF: Fourteen channels of thrombopoietin signaling pathway
            participated in regulating hepatocyte activation during rat liver
            regeneration.
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Dasouki,M.J., Rafi,S.K., Olm-Shipman,A.J., Wilson,N.R.,
            Abhyankar,S., Ganter,B., Furness,L.M., Fang,J., Calado,R.T. and
            Saadi,I.
  TITLE     Exome sequencing reveals a thrombopoietin ligand mutation in a
            Micronesian family with autosomal recessive aplastic anemia
  JOURNAL   Blood 122 (20), 3440-3449 (2013)
   PUBMED   24085763
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Wang,X., Muramatsu,H., Sakaguchi,H., Xu,Y., Narita,A., Tsumura,Y.,
            Doisaki,S., Tanaka,M., Ismael,O., Shimada,A., Hama,A., Takahashi,Y.
            and Kojima,S.
  TITLE     Mutation in the THPO gene is not associated with aplastic anaemia
            in Japanese children
  JOURNAL   Br J Haematol 158 (4), 553-555 (2012)
   PUBMED   22686250
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Kostyak,J.C., Naik,M.U. and Naik,U.P.
  TITLE     Calcium- and integrin-binding protein 1 regulates megakaryocyte
            ploidy, adhesion, and migration
  JOURNAL   Blood 119 (3), 838-846 (2012)
   PUBMED   22128142
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Marcucci,R. and Romano,M.
  TITLE     Thrombopoietin and its splicing variants: structure and functions
            in thrombopoiesis and beyond
  JOURNAL   Biochim Biophys Acta 1782 (7-8), 427-432 (2008)
   PUBMED   18433726
  REMARK    Review article
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Yang,C., Li,Y.C. and Kuter,D.J.
  TITLE     The physiological response of thrombopoietin (c-Mpl ligand) to
            thrombocytopenia in the rat
  JOURNAL   Br J Haematol 105 (2), 478-485 (1999)
   PUBMED   10233424
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Ishikawa,T., Ichida,T., Matsuda,Y., Sugitani,S., Sugiyama,M.,
            Kato,T., Miyazaki,H. and Asakura,H.
  TITLE     Reduced expression of thrombopoietin is involved in
            thrombocytopenia in human and rat liver cirrhosis
  JOURNAL   J Gastroenterol Hepatol 13 (9), 907-913 (1998)
   PUBMED   9794189
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Kondo,T., Okabe,M., Sanada,M., Kurosawa,M., Suzuki,S.,
            Kobayashi,M., Hosokawa,M. and Asaka,M.
  TITLE     Familial essential thrombocythemia associated with one-base
            deletion in the 5'-untranslated region of the thrombopoietin gene
  JOURNAL   Blood 92 (4), 1091-1096 (1998)
   PUBMED   9694695
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Wiestner,A., Schlemper,R.J., van der Maas,A.P. and Skoda,R.C.
  TITLE     An activating splice donor mutation in the thrombopoietin gene
            causes hereditary thrombocythaemia
  JOURNAL   Nat Genet 18 (1), 49-52 (1998)
   PUBMED   9425899
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Ogami,K., Shimada,Y., Sohma,Y., Akahori,H., Kato,T., Kawamura,K.
            and Miyazaki,H.
  TITLE     The sequence of a rat cDNA encoding thrombopoietin
  JOURNAL   Gene 158 (2), 309-310 (1995)
   PUBMED   7607561
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D32207.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D32207.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..326
                     /product="thrombopoietin precursor"
                     /note="thrombopoietin"
                     /calculated_mol_wt=32261
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2313
     mat_peptide     22..326
                     /product="thrombopoietin"
                     /calculated_mol_wt=32261
     Region          25..164
                     /region_name="EPO_TPO"
                     /note="Erythropoietin/thrombopoietin; pfam00758"
                     /db_xref="CDD:459927"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49745.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49745.1)"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49745.1)"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49745.1)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P49745.1)"
     Region          307..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49745.1)"
     CDS             1..326
                     /gene="Thpol1"
                     /gene_synonym="Thpo"
                     /coded_by="NM_031133.2:172..1152"
                     /db_xref="GeneID:81811"
                     /db_xref="RGD:11455920"
ORIGIN      
        1 meltdlllva illltarltl sspvppacdp rllnkllrds yllhsrlsqc pdvnplsipv
       61 llpavdfslg ewktqteqsk aqdilgavsl llegvmaarg qlepsclssl lgqlsgqvrl
      121 llgalqgllg tqlppqgrtt ahkdpsalfl slqqllrgkv rflllvegpa lcvrrtlptt
      181 avpsrtsqll tlnkfpnrts glletnfsvv artagpglln rlqgfrakii pgqlnqtsgs
      241 ldqipgylng thepvngthg lfagtslqtl eapdvvpgaf nkgslplnlq sglppipsla
      301 adgytlfpps ptfptpgspp qlppvs
//
LOCUS       NP_077363                315 aa            linear   ROD 27-APR-2025
DEFINITION  heme oxygenase 2 [Rattus norvegicus].
ACCESSION   NP_077363
VERSION     NP_077363.1
DBSOURCE    REFSEQ: accession NM_024387.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Martinez-Gascon,L.E., Ortiz,M.C., Galindo,M., Sanchez,J.M.,
            Sancho-Rodriguez,N., Albaladejo-Oton,M.D., Rodriguez Mulero,M.D.
            and Rodriguez,F.
  TITLE     Role of heme oxygenase in the regulation of the renal hemodynamics
            in a model of sex-dependent programmed hypertension by maternal
            diabetes
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 322 (3), R181-R191 (2022)
   PUBMED   34984919
  REMARK    GeneRIF: Role of heme oxygenase in the regulation of the renal
            hemodynamics in a model of sex-dependent programmed hypertension by
            maternal diabetes.
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Takemoto,M., Sakamoto,H., Higashimoto,Y. and Taira,J.
  TITLE     Complex Formation of Heme Oxygenase-2 with Heme Is Competitively
            Inhibited by the Cytosolic Domain of Caveolin-1
  JOURNAL   Biochemistry 60 (29), 2300-2308 (2021)
   PUBMED   34223768
  REMARK    GeneRIF: Complex Formation of Heme Oxygenase-2 with Heme Is
            Competitively Inhibited by the Cytosolic Domain of Caveolin-1.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kilic-Toprak,E., Kilic-Erkek,O., Abban-Mete,G., Caner,V.,
            Baris,I.C., Turhan,G., Kucukatay,V., Senol,H., Kuru,O. and
            Bor-Kucukatay,M.
  TITLE     Contribution of Heme Oxygenase 2 to Blood Pressure Regulation in
            Response to Swimming Exercise and Detraining in Spontaneously
            Hypertensive Rats
  JOURNAL   Med Sci Monit 24, 5851-5859 (2018)
   PUBMED   30132448
  REMARK    GeneRIF: Aorta HO-2 histological scores (HSCORE) of hypertensive
            rats were lower, while SBP was higher. Swimming caused enhancement
            of HO-2 immunostaining in aorta endothelium and adventitia of SHR.
            Exercise induced elevation of blood COHb index in SHR. Synchronous
            BP lowering effect of exercise was observed.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Robison,C.L., McHenry,J.A. and Hull,E.M.
  TITLE     Increased expression of carbon monoxide-producing enzymes in the
            MPOA after sexual experience in male rats
  JOURNAL   Physiol Behav 171, 149-157 (2017)
   PUBMED   28088559
  REMARK    GeneRIF: This experiments shown here indicate that HO-2 and HO-1
            are differentially regulated across sexual experience and that the
            two CO-producing enzymes are expressed in distinct but overlapping
            populations of cells in medial preoptic area.
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Posa,A., Kupai,K., Menesi,R., Szalai,Z., Szabo,R., Pinter,Z.,
            Palfi,G., Gyongyosi,M., Berko,A., Pavo,I. and Varga,C.
  TITLE     Sexual dimorphism of cardiovascular ischemia susceptibility is
            mediated by heme oxygenase
  JOURNAL   Oxid Med Cell Longev 2013, 521563 (2013)
   PUBMED   24163720
  REMARK    GeneRIF: The increased HO activity and expression in females might
            play a role in the sexual dimorphism of cardiovascular ischemia
            susceptibility during the reproductive age.
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Remmers,E.F., Griffiths,M.M., Longman,R.E., Gulko,P.S.,
            Kawahito,Y., Chen,S., Chang,L., Shepard,J., Ge,L., Dracheva,S.,
            Wang,J.P., Joe,B., Cannon,G.W. and Wilder,R.L.
  TITLE     An integrated rat genetic map: analysis of linkage conservation
            with the mouse and human maps
  JOURNAL   Transplant Proc 31 (3), 1549-1554 (1999)
   PUBMED   10330996
REFERENCE   7  (residues 1 to 315)
  AUTHORS   McCoubrey,W.K. Jr. and Maines,M.D.
  TITLE     The structure, organization and differential expression of the gene
            encoding rat heme oxygenase-2
  JOURNAL   Gene 139 (2), 155-161 (1994)
   PUBMED   8112599
REFERENCE   8  (residues 1 to 315)
  AUTHORS   McCoubrey,W.K. Jr., Ewing,J.F. and Maines,M.D.
  TITLE     Human heme oxygenase-2: characterization and expression of a
            full-length cDNA and evidence suggesting that the two HO-2
            transcripts may differ by choice of polyadenylation signal
  JOURNAL   Arch Biochem Biophys 295 (1), 13-20 (1992)
   PUBMED   1575508
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Rotenberg,M.O. and Maines,M.D.
  TITLE     Isolation, characterization, and expression in Escherichia coli of
            a cDNA encoding rat heme oxygenase-2
  JOURNAL   J Biol Chem 265 (13), 7501-7506 (1990)
   PUBMED   2185251
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Cruse,I. and Maines,M.D.
  TITLE     Evidence suggesting that the two forms of heme oxygenase are
            products of different genes
  JOURNAL   J Biol Chem 263 (7), 3348-3353 (1988)
   PUBMED   3343248
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05405.1, SRR26360186.17153.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..315
                     /product="heme oxygenase 2"
                     /EC_number="1.14.14.18"
                     /note="heme oxygenase (decycling) 2"
                     /calculated_mol_wt=35631
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P30519; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30519; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Region          30..235
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(37,44,47..48,53,57,153..155,161..162,166,198,202,
                     226,229,233)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350856"
     Region          146..173
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350856"
     Site            159
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P09601; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Region          263..268
                     /region_name="HRM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Region          280..285
                     /region_name="HRM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Site            295..315
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     CDS             1..315
                     /gene="Hmox2"
                     /gene_synonym="Ho-2"
                     /coded_by="NM_024387.2:188..1135"
                     /db_xref="GeneID:79239"
                     /db_xref="RGD:67402"
ORIGIN      
        1 mssevetseg vdesennsta pekenhtkma dlsellkegt keahdraent qfvkdflkgn
       61 ikkelfklat talyftysal eeemdrnkdh pafaplyfpt elhrkealik dmeyffgenw
      121 eeqvkcseaa qkyvdrihyv gqnepellva haytrymgdl sggqvlkkva qralklpstg
      181 egtqfylfeh vdnaqqfkqf yrarmnaldl smktkerive eankafeynm qifseldqag
      241 smltketled glpvhdgkgd vrkcpfyaaq pdkgtlggsn cpfrtamavl rkpslqlila
      301 asvalvagll awyym
//
LOCUS       NP_001257784             203 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform b [Rattus norvegicus].
ACCESSION   NP_001257784
VERSION     NP_001257784.1
DBSOURCE    REFSEQ: accession NM_001270855.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC092646.1.
            
            Transcript Variant: This variant (2) has an alternate exon in the
            3' end compared to variant 1. This exon has an in-frame stop codon,
            resulting in an isoform (b) with a shorter and distinct C-terminus
            compared to isoform a. Variants 2 and 6 both encode the same
            isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092646.1, SRR26360176.2013392.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..203
                     /product="stathmin-4 isoform b"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=23587
     Region          76..198
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     CDS             1..203
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_001270855.1:180..791"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyegwcg rqcrrkgqsq rkgsadwrer
       61 reqadtvdln wcvisdmevi elnkctsgqs fevilkppsf dgvpefnasl prrrdpslee
      121 iqkkleaaee rrkyqeaell khlaekrehe reviqkaiee nnnfikmake klaqkmesnk
      181 enreahlaam lerlqekepp aar
//
LOCUS       NP_001014109             601 aa            linear   ROD 27-APR-2025
DEFINITION  deuterosome assembly protein 1 [Rattus norvegicus].
ACCESSION   NP_001014109 XP_235839
VERSION     NP_001014109.2
DBSOURCE    REFSEQ: accession NM_001014087.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Zhao,H., Zhu,L., Zhu,Y., Cao,J., Li,S., Huang,Q., Xu,T., Huang,X.,
            Yan,X. and Zhu,X.
  TITLE     The Cep63 paralogue Deup1 enables massive de novo centriole
            biogenesis for vertebrate multiciliogenesis
  JOURNAL   Nat Cell Biol 15 (12), 1434-1444 (2013)
   PUBMED   24240477
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC085333.1.
            
            On Oct 1, 2011 this sequence version replaced NP_001014109.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..601
                     /product="deuterosome assembly protein 1"
                     /note="coiled-coil domain-containing protein 67;
                     deuterosome protein 1; coiled-coil domain containing 67"
                     /calculated_mol_wt=69974
     Region          12..279
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          115..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Z6.2)"
     Region          <141..>423
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          188..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Z6.2)"
     Region          307..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U3Z6.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U3Z6.2)"
     CDS             1..601
                     /gene="Deup1"
                     /gene_synonym="Ccdc67; RGD1306632"
                     /coded_by="NM_001014087.1:131..1936"
                     /db_xref="GeneID:315438"
                     /db_xref="RGD:1306632"
ORIGIN      
        1 menqahttag aspceaelqe lmeqidimvs nkkldwerkm raletrldlr dqelanaqtc
       61 ldqkgqevgl lrqkldslek cnlvmtqnye gqlqtlkaqf skltnnfekl rlhqmkqnqs
      121 hrkeasnkde tpfelsslnq kieefraksr ewdkqeilyq thlvsldaqq kllsekcnqf
      181 qkqaqnyqtq lngkqqrped sspetprlvc esspgceatq rdefiieklk savseialsr
      241 nklqdenqkl lqelkmyqrq cqameaglse vknelqsrdd llriiemerl hlhrellkmg
      301 elqtvqdnrk rvessyspst keperkrkel fsvvsdqpnh ekelnkmrsq lyqeedlcse
      361 qermrneise ltqelhqkev tiatimkkaa llerqlkiel eikekmlakq qisdrrykav
      421 rtenthlkgm mgdldparyl tvdfsnkehs rhtsinkley enerlrsdla klhingkaaw
      481 snqssyegag ayiyqsqlkt etggdrised cemnrsptpl splpfqtkem tsplagdnev
      541 lplsppdisf raslaaqhfl meeekrakel ekllnthide lqrhteftln kytklkqsrh
      601 i
//
LOCUS       NP_001163906             132 aa            linear   ROD 27-APR-2025
DEFINITION  anaphase-promoting complex subunit 15 [Rattus norvegicus].
ACCESSION   NP_001163906
VERSION     NP_001163906.1
DBSOURCE    REFSEQ: accession NM_001170435.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Mansfeld,J., Collin,P., Collins,M.O., Choudhary,J.S. and Pines,J.
  TITLE     APC15 drives the turnover of MCC-CDC20 to make the spindle assembly
            checkpoint responsive to kinetochore attachment
  JOURNAL   Nat Cell Biol 13 (10), 1234-1243 (2011)
   PUBMED   21926987
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM103187.1, FM137052.1 and JAXUCZ010000001.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM103187.1, SRR22399481.816783.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..132
                     /product="anaphase-promoting complex subunit 15"
                     /calculated_mol_wt=15247
     Region          13..>73
                     /region_name="ANAPC15"
                     /note="Anaphase-promoting complex subunit 15; pfam15243"
                     /db_xref="CDD:464583"
     Region          58..132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZQX4.1)"
     CDS             1..132
                     /gene="Anapc15"
                     /gene_synonym="APC15; RGD1311634"
                     /coded_by="NM_001170435.1:79..477"
                     /db_xref="GeneID:293155"
                     /db_xref="RGD:1311634"
ORIGIN      
        1 mepglklslg amstlfpslf prvtetlwfn ldrpcveete lqqqeqqhqa wlqsiaekdn
       61 nlvpigkpas ehyddeeeed deddedseed seddedmqdm demndynesp ddgevnevdm
      121 egneqdqdqw mi
//
LOCUS       NP_112253                206 aa            linear   ROD 27-APR-2025
DEFINITION  synaptosomal-associated protein 25 isoform b [Rattus norvegicus].
ACCESSION   NP_112253 XP_346671
VERSION     NP_112253.1
DBSOURCE    REFSEQ: accession NM_030991.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Hu,A., Lan,H., Yao,Z. and Kong,X.
  TITLE     Carbohydrate response element-binding protein (ChREBP) mediates
            decreased SNAP25 expression in islets from diabetic Goto-Kakizaki
            (GK) rats
  JOURNAL   FEBS Open Bio 14 (11), 1864-1872 (2024)
   PUBMED   39300600
  REMARK    GeneRIF: Carbohydrate response element-binding protein (ChREBP)
            mediates decreased SNAP25 expression in islets from diabetic
            Goto-Kakizaki (GK) rats.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Polishchuk,A., Cilleros-Mane,V., Balanya-Segura,M., Just-Borras,L.,
            Fornies-Marine,A., Silvera-Simon,C., Tomas,M., Jami El Hirchi,M.,
            Hurtado,E., Tomas,J. and Lanuza,M.A.
  TITLE     BDNF/TrkB signalling, in cooperation with muscarinic signalling,
            retrogradely regulates PKA pathway to phosphorylate SNAP-25 and
            Synapsin-1 at the neuromuscular junction
  JOURNAL   Cell Commun Signal 22 (1), 371 (2024)
   PUBMED   39044222
  REMARK    GeneRIF: BDNF/TrkB signalling, in cooperation with muscarinic
            signalling, retrogradely regulates PKA pathway to phosphorylate
            SNAP-25 and Synapsin-1 at the neuromuscular junction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kong,X., Lin,C., Yang,C., Wang,X., Li,B., Yan,D., Yang,Y., Hu,A.,
            Chen,Y., Xu,X. and Ma,X.
  TITLE     GLP-1 signaling-regulated SNAP25 is involved in improved insulin
            secretion in diabetic GK rats after Roux-en-Y gastric bypass
            surgery
  JOURNAL   Mol Biol Rep 51 (1), 123 (2024)
   PUBMED   38227062
  REMARK    GeneRIF: GLP-1 signaling-regulated SNAP25 is involved in improved
            insulin secretion in diabetic GK rats after Roux-en-Y gastric
            bypass surgery.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Si,W., Sun,B., Luo,J., Li,Z., Dou,Y. and Wang,Q.
  TITLE     Snap25 attenuates neuronal injury via reducing ferroptosis in acute
            ischemic stroke
  JOURNAL   Exp Neurol 367, 114476 (2023)
   PUBMED   37393984
  REMARK    GeneRIF: Snap25 attenuates neuronal injury via reducing ferroptosis
            in acute ischemic stroke.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chilcote,T.J., Galli,T., Mundigl,O., Edelmann,L., McPherson,P.S.,
            Takei,K. and De Camilli,P.
  TITLE     Cellubrevin and synaptobrevins: similar subcellular localization
            and biochemical properties in PC12 cells
  JOURNAL   J Cell Biol 129 (1), 219-231 (1995)
   PUBMED   7698987
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Garcia,E.P., McPherson,P.S., Chilcote,T.J., Takei,K. and De
            Camilli,P.
  TITLE     rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the
            axon, but are not in a stable complex with syntaxin
  JOURNAL   J Cell Biol 129 (1), 105-120 (1995)
   PUBMED   7698978
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Hess,D.T., Slater,T.M., Wilson,M.C. and Skene,J.H.
  TITLE     The 25 kDa synaptosomal-associated protein SNAP-25 is the major
            methionine-rich polypeptide in rapid axonal transport and a major
            substrate for palmitoylation in adult CNS
  JOURNAL   J Neurosci 12 (12), 4634-4641 (1992)
   PUBMED   1281490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FQ214162.1 and BC087699.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346671.1.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein. It is essential for regulated exocytosis in neuronal
            cells. Alternative transcript variants encoding two different
            protein isoforms have been described for this gene. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (3, also known as b) has an
            alternate in-frame exon in the coding region, compared to variant
            1. The resulting isoform (b) is of the same length, but has a
            distinct internal segment, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform b"
                     /note="synaptosomal-associated protein, 25 kDa; SUP;
                     SNAP-25; super protein; synaptosomal-associated 25 kDa
                     protein; synaptosomal-associated protein 25"
                     /calculated_mol_wt=23184
     Region          1..75
                     /region_name="Interaction with CENPF.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60881.1)"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60881.1)"
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          111..120
                     /region_name="Interaction with ZDHHC13 and ZDHHC17.
                     /evidence=ECO:0000269|PubMed:26198635"
                     /note="propagated from UniProtKB/Swiss-Prot (P60881.1)"
     Region          111..120
                     /region_name="Interaction with ZDHHC17.
                     /evidence=ECO:0000250|UniProtKB:P60880"
                     /note="propagated from UniProtKB/Swiss-Prot (P60881.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC and PKA.
                     /evidence=ECO:0000269|PubMed:12459461; propagated from
                     UniProtKB/Swiss-Prot (P60881.1)"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60881.1)"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     Site            180..181
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type E (BoNT/E).
                     /evidence=ECO:0000269|PubMed:8243676,
                     ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915;
                     propagated from UniProtKB/Swiss-Prot (P60881.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:12459461; propagated from
                     UniProtKB/Swiss-Prot (P60881.1)"
     Site            197..198
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type A (BoNT/A, botA).
                     /evidence=ECO:0000269|PubMed:8243676,
                     ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915;
                     propagated from UniProtKB/Swiss-Prot (P60881.1)"
     CDS             1..206
                     /gene="Snap25"
                     /gene_synonym="SNAP-25a; SNAP-25B"
                     /coded_by="NM_030991.3:210..830"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:25012"
                     /db_xref="RGD:3728"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqleri
       61 eegmdqinkd mkeaeknltd lgkfcglcvc pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001094017             419 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity protein phosphatase 7 [Rattus norvegicus].
ACCESSION   NP_001094017 XP_001070874 XP_238551
VERSION     NP_001094017.1
DBSOURCE    REFSEQ: accession NM_001100547.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Ham,J.E., Oh,E.K., Kim,D.H. and Choi,S.H.
  TITLE     Differential expression profiles and roles of inducible DUSPs and
            ERK1/2-specific constitutive DUSP6 and DUSP7 in microglia
  JOURNAL   Biochem Biophys Res Commun 467 (2), 254-260 (2015)
   PUBMED   26435497
  REMARK    GeneRIF: The expression of DUSP6 and DUSP7 is mediated by ERK1/ERK2
            activity in microglia.
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Dowd,S., Sneddon,A.A. and Keyse,S.M.
  TITLE     Isolation of the human genes encoding the pyst1 and Pyst2
            phosphatases: characterisation of Pyst2 as a cytosolic
            dual-specificity MAP kinase phosphatase and its catalytic
            activation by both MAP and SAP kinases
  JOURNAL   J Cell Sci 111 (Pt 22), 3389-3399 (1998)
   PUBMED   9788880
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Muda,M., Boschert,U., Dickinson,R., Martinou,J.C., Martinou,I.,
            Camps,M., Schlegel,W. and Arkinstall,S.
  TITLE     MKP-3, a novel cytosolic protein-tyrosine phosphatase that
            exemplifies a new class of mitogen-activated protein kinase
            phosphatase
  JOURNAL   J Biol Chem 271 (8), 4319-4326 (1996)
   PUBMED   8626780
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Feb 16, 2013 this sequence version replaced
            XP_001070874.2, XP_238551.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.474808.1,
                                           SRR26360172.1500396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..419
                     /product="dual specificity protein phosphatase 7"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="MAP kinase phosphatase; dual specificity protein
                     phosphatase MKP-X"
                     /calculated_mol_wt=44936
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63340.2)"
     Region          55..186
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Site            101..103
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Region          216..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63340.2)"
     Region          240..388
                     /region_name="DSP_DUSP7"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 7; cd14643"
                     /db_xref="CDD:350491"
     CDS             1..419
                     /gene="Dusp7"
                     /gene_synonym="mkp-X"
                     /coded_by="NM_001100547.1:1..1260"
                     /db_xref="GeneID:300980"
                     /db_xref="RGD:735026"
ORIGIN      
        1 mknqlrgppv rahmstsgaa aaggtragse pgagsgssag igagattgag ampcksaewl
       61 qeeleargga slllldcrph elfesshiet ainlaipglm lrrlrkgnlp irsiipnhad
      121 kerfatrcka atvllydeat aewqpepgap asvlglllqk lrddgcqayy lqggfnkfqt
      181 eysehcetnv dsssspsgsp ptsvlglggl rissdcsdge sdrelpssat esdgspvpss
      241 qpafpvqilp ylylgcakds tnldvlgkyg ikyilnvtpn lpnafehgge ftykqipisd
      301 hwsqnlsqff peaisfidea rskkcgvlvh clagisrsvt vtvaylmqkm nlslndaydf
      361 vkrkksnisp nfnfmgqlld fertlglssp cdnhtpseql yfstptnhnl fpintlest
//
LOCUS       NP_599240                514 aa            linear   ROD 27-APR-2025
DEFINITION  nucleus accumbens-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_599240
VERSION     NP_599240.1
DBSOURCE    REFSEQ: accession NM_134413.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Nakayama,K., Nakayama,N., Wang,T.L. and Shih,Ie.M.
  TITLE     NAC-1 controls cell growth and survival by repressing transcription
            of Gadd45GIP1, a candidate tumor suppressor
  JOURNAL   Cancer Res 67 (17), 8058-8064 (2007)
   PUBMED   17804717
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Davidson,B., Berner,A., Trope',C.G., Wang,T.L. and Shih,I.M.
  TITLE     Expression and clinical role of the bric-a-brac tramtrack broad
            complex/poxvirus and zinc protein NAC-1 in ovarian carcinoma
            effusions
  JOURNAL   Hum Pathol 38 (7), 1030-1036 (2007)
   PUBMED   17391728
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Korutla,L., Degnan,R., Wang,P. and Mackler,S.A.
  TITLE     NAC1, a cocaine-regulated POZ/BTB protein interacts with CoREST
  JOURNAL   J Neurochem 101 (3), 611-618 (2007)
   PUBMED   17254023
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Nakayama,K., Nakayama,N., Davidson,B., Sheu,J.J., Jinawath,N.,
            Santillan,A., Salani,R., Bristow,R.E., Morin,P.J., Kurman,R.J.,
            Wang,T.L. and Shih,Ie.M.
  TITLE     A BTB/POZ protein, NAC-1, is related to tumor recurrence and is
            essential for tumor growth and survival
  JOURNAL   Proc Natl Acad Sci U S A 103 (49), 18739-18744 (2006)
   PUBMED   17130457
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Korutla,L., Wang,P.J. and Mackler,S.A.
  TITLE     The POZ/BTB protein NAC1 interacts with two different histone
            deacetylases in neuronal-like cultures
  JOURNAL   J Neurochem 94 (3), 786-793 (2005)
   PUBMED   16033423
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Korutla,L., Champtiaux,N., Shen,H.W., Klugmann,M., Kalivas,P.W. and
            Mackler,S.A.
  TITLE     Activity-dependent subcellular localization of NAC1
  JOURNAL   Eur J Neurosci 22 (2), 397-403 (2005)
   PUBMED   16045493
  REMARK    Erratum:[Eur J Neurosci. 2005 Sep;22(6):1552. Klugman, Matthias
            [corrected to Klugmann, Matthias]]
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Korutla,L., Neustadter,J.H., Fournier,K.M. and Mackler,S.A.
  TITLE     NAC1, a POZ/BTB protein present in the adult mammalian brain,
            triggers apoptosis after adenovirus-mediated overexpression in
            PC-12 cells
  JOURNAL   Neurosci Res 46 (1), 33-39 (2003)
   PUBMED   12725910
  REMARK    GeneRIF: aberrantly regulated NAC1 expression in the mammalian
            brain may contribute to programmed cell death
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Korutla,L., Wang,P.J., Lewis,D.M., Neustadter,J.H., Stromberg,M.F.
            and Mackler,S.A.
  TITLE     Differences in expression, actions and cocaine regulation of two
            isoforms for the brain transcriptional regulator NAC1
  JOURNAL   Neuroscience 110 (3), 421-429 (2002)
   PUBMED   11906783
  REMARK    GeneRIF: The two isoforms of NAC-1 may differentially affect
            neuronal functions, including the regulation of cocaine-induced
            locomotion. The longer isoform was the more abundant of the two
            NAC1 proteins and the ratio between them differed throughout the
            rat brain.
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Cha,X.Y., Pierce,R.C., Kalivas,P.W. and Mackler,S.A.
  TITLE     NAC-1, a rat brain mRNA, is increased in the nucleus accumbens
            three weeks after chronic cocaine self-administration
  JOURNAL   J Neurosci 17 (18), 6864-6871 (1997)
   PUBMED   9278521
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF015911.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF015911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..514
                     /product="nucleus accumbens-associated protein 1"
                     /note="nucleus accumbens-1; BTB/POZ domain-containing
                     protein 14B; BTB (POZ) domain containing 14B;
                     transcriptional repressor NAC1; nucleus accumbens
                     associated 1, BEN and BTB (POZ) domain containing"
                     /calculated_mol_wt=56319
     Region          3..125
                     /region_name="BTB_POZ_BTBD14B_NAC1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in nucleus
                     accumbens-associated protein 1 (NAC-1); cd18290"
                     /db_xref="CDD:349599"
     Site            order(3..9,11..14,16..17,19..20,23,29,44,46,49..51,56,
                     59..60,84..85,87..92,97,100..101,111..112)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349599"
     Region          183..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35260.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RE7; propagated from
                     UniProtKB/Swiss-Prot (O35260.1)"
     Region          241..279
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35260.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:16045493; propagated from
                     UniProtKB/Swiss-Prot (O35260.1)"
     Region          382..460
                     /region_name="BEN"
                     /note="The BEN domain is found in diverse animal proteins;
                     smart01025"
                     /db_xref="CDD:214981"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSZ8; propagated from
                     UniProtKB/Swiss-Prot (O35260.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSZ8; propagated from
                     UniProtKB/Swiss-Prot (O35260.1)"
     CDS             1..514
                     /gene="Nacc1"
                     /gene_synonym="Btbd14b; Nac-1; Nac1"
                     /coded_by="NM_134413.2:134..1678"
                     /db_xref="GeneID:171454"
                     /db_xref="RGD:621003"
ORIGIN      
        1 maqtlqmeip nfgnsilecl neqrlqglyc dvsvvvkgha fkahravlaa sssyfrdlfn
       61 ssrsavvelp aavqpqsfqq iltfcytgrl smnmgdqfll iytagflqiq eimekgteff
      121 lkvsspscds qglhpeeaps sepqspvaqi lgwpacstpl plvsrvkteq eldsvqctpm
      181 akrlwdssqk eaggsggnng srkmakfstp dlapnrmpqp vsvatataav avvavggcvs
      241 gpsmsertsp gtssaytsds pssyhneede eedageegtd eqyrqicnmy tmysmlnvgq
      301 tvekvealpe qvvleshsri rvrqdlaslp aelinqignr chpklydegd pseklelvtg
      361 tnvyitraql mnchvsagtr hkvllrrlla sffdrntlan scgtgirsst ndprrkplds
      421 rvlhavkyyc qnfapnfkes emnaiaadmc tnarrvvrks wlpktkplhl vegdnyssfi
      481 sdtgkiepdm msmehsfeta shdgeagpsa evlq
//
LOCUS       NP_001171976             116 aa            linear   ROD 27-APR-2025
DEFINITION  host cell factor C1 regulator 1 [Rattus norvegicus].
ACCESSION   NP_001171976
VERSION     NP_001171976.1
DBSOURCE    REFSEQ: accession NM_001185047.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB698538.1, BC168753.1 and BG373213.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..116
                     /product="host cell factor C1 regulator 1"
                     /note="HCF-1 beta-propeller-interacting protein; inhibitor
                     of four 2; host cell factor C1 regulator 1
                     (XPO1-dependent)"
                     /calculated_mol_wt=12860
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     Region          2..112
                     /region_name="HPIP"
                     /note="HCF-1 beta-propeller-interacting protein family;
                     pfam15226"
                     /db_xref="CDD:373659"
     Region          54..57
                     /region_name="Interaction with HCFC1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     Region          88..97
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     CDS             1..116
                     /gene="Hcfc1r1"
                     /gene_synonym="Hpip"
                     /coded_by="NM_001185047.1:106..456"
                     /db_xref="GeneID:287097"
                     /db_xref="RGD:727975"
ORIGIN      
        1 milqqplerg ppgrdpratt gvtlgldtre plhkhflsee nmathfsrls lhndhpycsp
       61 pvtfpealpp lrspcpelll wrypgslipe alrllrlgdn pspyysaspa geimel
//
LOCUS       NP_114451               2977 aa            linear   ROD 27-APR-2025
DEFINITION  kalirin [Rattus norvegicus].
ACCESSION   NP_114451
VERSION     NP_114451.2
DBSOURCE    REFSEQ: accession NM_032062.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2977)
  AUTHORS   Huang,H., Chen,L., Yuan,J., Zhang,H., Yang,J., Xu,Z. and Chen,Y.
  TITLE     Role and mechanism of EphB3 in epileptic seizures and
            epileptogenesis through Kalirin
  JOURNAL   Mol Cell Neurosci 128, 103915 (2024)
   PUBMED   38143048
  REMARK    GeneRIF: Role and mechanism of EphB3 in epileptic seizures and
            epileptogenesis through Kalirin.
REFERENCE   2  (residues 1 to 2977)
  AUTHORS   Wang,X., Weng,M., Ke,Y., Sapp,E., DiFiglia,M. and Li,X.
  TITLE     Kalirin Interacts with TRAPP and Regulates Rab11 and Endosomal
            Recycling
  JOURNAL   Cells 9 (5), 1132 (2020)
   PUBMED   32375403
  REMARK    GeneRIF: Kalirin Interacts with TRAPP and Regulates Rab11 and
            Endosomal Recycling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2977)
  AUTHORS   Paskus,J.D., Tian,C., Fingleton,E., Shen,C., Chen,X., Li,Y.,
            Myers,S.A., Badger,J.D. 2nd, Bemben,M.A., Herring,B.E. and
            Roche,K.W.
  TITLE     Synaptic Kalirin-7 and Trio Interactomes Reveal a GEF
            Protein-Dependent Neuroligin-1 Mechanism of Action
  JOURNAL   Cell Rep 29 (10), 2944-2952 (2019)
   PUBMED   31801062
REFERENCE   4  (residues 1 to 2977)
  AUTHORS   Li,M.X., Qiao,H., Zhang,M. and Ma,X.M.
  TITLE     Role of Cdk5 in Kalirin7-Mediated Formation of Dendritic Spines
  JOURNAL   Neurochem Res 44 (5), 1243-1251 (2019)
   PUBMED   30875016
  REMARK    GeneRIF: that Cdk5 affects the function of Kal-7 on spine
            morphology and function via GluN2B and GluA1 receptors during
            dendritic spine formation
REFERENCE   5  (residues 1 to 2977)
  AUTHORS   Xie,Z., Shapiro,L.P., Cahill,M.E., Russell,T.A., Lacor,P.N.,
            Klein,W.L. and Penzes,P.
  TITLE     Kalirin-7 prevents dendritic spine dysgenesis induced by amyloid
            beta-derived oligomers
  JOURNAL   Eur J Neurosci 49 (9), 1091-1101 (2019)
   PUBMED   30565792
  REMARK    GeneRIF: our results suggest that kalirin-7 may play a role in the
            early events leading to synapse degeneration
REFERENCE   6  (residues 1 to 2977)
  AUTHORS   Penzes,P., Johnson,R.C., Alam,M.R., Kambampati,V., Mains,R.E. and
            Eipper,B.A.
  TITLE     An isoform of kalirin, a brain-specific GDP/GTP exchange factor, is
            enriched in the postsynaptic density fraction
  JOURNAL   J Biol Chem 275 (9), 6395-6403 (2000)
   PUBMED   10692441
REFERENCE   7  (residues 1 to 2977)
  AUTHORS   Mains,R.E., Alam,M.R., Johnson,R.C., Darlington,D.N., Back,N.,
            Hand,T.A. and Eipper,B.A.
  TITLE     Kalirin, a multifunctional PAM COOH-terminal domain interactor
            protein, affects cytoskeletal organization and ACTH secretion from
            AtT-20 cells
  JOURNAL   J Biol Chem 274 (5), 2929-2937 (1999)
   PUBMED   9915831
REFERENCE   8  (residues 1 to 2977)
  AUTHORS   Colomer,V., Engelender,S., Sharp,A.H., Duan,K., Cooper,J.K.,
            Lanahan,A., Lyford,G., Worley,P. and Ross,C.A.
  TITLE     Huntingtin-associated protein 1 (HAP1) binds to a Trio-like
            polypeptide, with a rac1 guanine nucleotide exchange factor domain
  JOURNAL   Hum Mol Genet 6 (9), 1519-1525 (1997)
   PUBMED   9285789
REFERENCE   9  (residues 1 to 2977)
  AUTHORS   Alam,M.R., Johnson,R.C., Darlington,D.N., Hand,T.A., Mains,R.E. and
            Eipper,B.A.
  TITLE     Kalirin, a cytosolic protein with spectrin-like and GDP/GTP
            exchange factor-like domains that interacts with peptidylglycine
            alpha-amidating monooxygenase, an integral membrane
            peptide-processing enzyme
  JOURNAL   J Biol Chem 272 (19), 12667-12675 (1997)
   PUBMED   9139723
REFERENCE   10 (residues 1 to 2977)
  AUTHORS   Alam,M.R., Caldwell,B.D., Johnson,R.C., Darlington,D.N., Mains,R.E.
            and Eipper,B.A.
  TITLE     Novel proteins that interact with the COOH-terminal cytosolic
            routing determinants of an integral membrane peptide-processing
            enzyme
  JOURNAL   J Biol Chem 271 (45), 28636-28640 (1996)
   PUBMED   8910496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF230644.1 and AF232669.1.
            
            On Apr 23, 2010 this sequence version replaced NP_114451.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2977
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..2977
                     /product="kalirin"
                     /EC_number="2.7.11.1"
                     /note="P-CIP10; protein Duo; PAM COOH-terminal interactor
                     protein 10; huntingtin-associated protein-interacting
                     protein; serine/threonine kinase with Dbl- and pleckstrin
                     homology domain; serine/threonine-protein kinase with Dbl-
                     and pleckstrin homology domain; huntingtin-associated
                     protein interacting protein (duo); cyclin B1"
                     /calculated_mol_wt=339068
     Region          39..177
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     Region          190..410
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            309..314
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          311..536
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            417..422
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          537..766
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          783..997
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            889..894
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          891..1120
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            996..1001
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1126..1226
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Site            1228..1233
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1275..1445
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(1279,1283,1378,1399..1400,1403..1404,1406..1407,
                     1410..1411,1414..1415,1418,1441,1445)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1452..1574
                     /region_name="PH1_Kalirin_Trio_like"
                     /note="Triple functional domain pleckstrin homology
                     pleckstrin homology (PH) domain, repeat 1; cd13240"
                     /db_xref="CDD:270060"
     Site            order(1469,1509,1511)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270060"
     Region          1640..1699
                     /region_name="SH3_Kalirin_1"
                     /note="First Src homology 3 domain of the RhoGEF kinase,
                     Kalirin; cd11852"
                     /db_xref="CDD:212786"
     Site            order(1646,1648,1651,1655,1675..1676,1693,1695..1696)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212786"
     Region          1696..1880
                     /region_name="SH3-RhoG_link"
                     /note="SH3-RhoGEF linking unstructured region; pfam16609"
                     /db_xref="CDD:465196"
     Region          1923..2092
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          2097..2231
                     /region_name="PH2_Kalirin_Trio_p63RhoGEF"
                     /note="p63RhoGEF pleckstrin homology (PH) domain, repeat
                     2; cd13241"
                     /db_xref="CDD:270061"
     Site            order(2106,2141..2142,2166,2168,2218,2221..2223,
                     2225..2226,2228..2230)
                     /site_type="other"
                     /note="Galpha i/q binding site [polypeptide binding]"
                     /db_xref="CDD:270061"
     Region          2315..2373
                     /region_name="SH3_Kalirin_2"
                     /note="Second Src homology 3 domain of the RhoGEF kinase,
                     Kalirin; cd11853"
                     /db_xref="CDD:212787"
     Site            order(2320,2322,2325,2329,2347..2348,2367,2369..2370)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212787"
     Region          2462..2556
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          2479..2483
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          2492..2496
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          2522..2526
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          2536..2541
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          2549..2552
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          2560..2651
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(2560,2625,2640)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(2641..2642,2644..2645)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          2681..2928
                     /region_name="STKc_Kalirin_C"
                     /note="C-terminal kinase domain of the Large
                     Serine/Threonine Kinase and Rho Guanine Nucleotide
                     Exchange Factor, Kalirin; cd14115"
                     /db_xref="CDD:271017"
     Site            order(2681..2685,2687,2689,2702,2704,2732,2748..2749,2751,
                     2755,2757,2794,2796,2798..2799,2801,2814..2815,2818,
                     2833..2836)
                     /site_type="active"
                     /db_xref="CDD:271017"
     Site            order(2681..2685,2687,2689,2702,2704,2732,2748..2749,2751,
                     2755,2798..2799,2801,2814..2815)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271017"
     Site            order(2685,2755,2757,2794,2796,2798,2818,2833..2836)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271017"
     Site            order(2814..2822,2832..2836)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271017"
     CDS             1..2977
                     /gene="Kalrn"
                     /gene_synonym="Duo; Hapip; Kalirin"
                     /coded_by="NM_032062.2:1..8934"
                     /db_xref="GeneID:84009"
                     /db_xref="RGD:621865"
ORIGIN      
        1 mtdrfwdqwy lwylrllrll drgsfrndgl kasdvlpilk ekvafvsggr dkrggpiltf
       61 partnhdrir qedlrklvtn lasvpsedvc krgftviidm rgskwdlikp llktlqeafp
      121 aeihvaliik pdnfwqkqkt nfgsskfife tsmvsveglt klvdpsqlte efdgsldynh
      181 eewielrlsl eeffnsavhl lsrledlqem larkefpvdv egsrrlideh tqlkkkvlka
      241 pveeldregq rllqcircsd gfsgrncipg sadfqslvpk itslldklhs trqhlhqmwh
      301 vrklkldqcf qlrlfeqdae kmfdwishnk elflqshtei gvsyqhaldl qtqhnhfamn
      361 smnayvninr imsvasrlse aghyasqqik qistqldqew ksfaaalder stilamsavf
      421 hqkaeqflsg vdawckmcse gglpsemqdl elaihhhqsl yeqvtqayte vsqdgkalld
      481 vlqrplspgn sesltatany skavhqvldv vhevlhhqrr lesiwqhrkv rlhqrlqlcv
      541 fqqdvqqvld wienhgeafl skhtgvgksl hraralqkrh ddfeevaqnt ytnadkllea
      601 aeqlaqtgec dpeeiykaar hlevriqdfv rrveqrklll dmsvsfhtht kelwtwmedl
      661 qkevledvca dsvdavqeli kqfqqqqtat ldatlnvike gedliqqlrs appslgepte
      721 ardsavsnnk tphsssishi esvlqqldda qvqmeelfhe rkikldiflq lrifeqytie
      781 vtaeldawne dllrqmndfn tedltlaeqr lqrhterkla mnnmtfeviq qgqdlhqyim
      841 evqasgieli cekdvdlaaq vqelleflhe kqhelelnae qthkrleqcl qlrhlqaevk
      901 qvlgwirnge smlnaslvna sslseaeqlq reheqfqlai ekthqsalqv qqkaeallqa
      961 ghydadaire caekvalhwq qlmlkmedrl klvnasvafy ktseqvcsvl esleqeyrrd
     1021 edwcggrdkl gpaaemdhvi pllskhleqk eaflkactla rrnaevflky ihrnnvsmps
     1081 vashtrgpeq qvkailsell qrenrvlhfw tlkkrrldqc qqyvvfersa kqaldwiqet
     1141 geyylsthts tgetteetqe llkeygefrv pakqtkekvk lliqladsfv ekghihatei
     1201 rkwvttvdkh yrdfslrmgk yrytlekalg vntednkdle ldiipaslsd revklrdanh
     1261 evneekrksa rkkefimael lqtekayvrd lhecletylw emtsgveeip pgilnkehii
     1321 fgniqeiydf hnniflkele kyeqlpedvg hcfvtwadkf qmyvtycknk pdsnqlileh
     1381 agtffdeiqq rhglansiss ylikpvqrvt kyqlllkell tcceegkgel kdglevmlsv
     1441 pkkandamhv smlegfdenl dvqgelilqd afqvwdpksl irkgrerhlf lfeislvfsk
     1501 eikdssghtk yvyknkllts elgvtehveg dpckfalwsg rtpssdnktv lkasnietkq
     1561 ewiknirevi qeriihlkga lkepiqlpkt paklrnnskr dgvedgdsqg dgssqpdtis
     1621 iasrtsqntv esdklsggce ltvvlqdfsa ahsselsiqv gqtvellerp serpgwclvr
     1681 ttersppqeg lvpsstlcis hsrssvemdc ffplvkdsys hssgenggks esvanlqsqp
     1741 slnsihsspg pkrstntlkk wltspvrrln sgkadgnikk qkkvrdgrks fdlgspkpgd
     1801 ettpqgdsad ekskkgwged epdeeshtpl pppmkifdnd ptqdemssll aarqaptdvp
     1861 taadlvsaie klvkskltle ggsyrgslkd ptvclnegma pptpprnlee eqkakalrgr
     1921 mfvlnelvqt ekdyvkdlgi vvegfmkrie ekgvpedmrg kekivfgnih qiydwhkdff
     1981 laelekciqe qdrlaqlfik herklhiyvw ycqnkprsey ivaeydayfe evkqeinqrl
     2041 tlsdflikpi qritkyqlll kdflryseka glecsdieka velmclvpkr cndmmnlgrl
     2101 qgfegtltaq gkllqqdtfy vieldagmqs rtkerrvflf eqivifsell rkgsltpgym
     2161 fkrsikmnyl vleedvdddp ckfalmnret servilqaan sdiqqawvqd inqvletqrd
     2221 flnalqspie yqrkerstav irsqpprvpq asprpyssvp vgsekppkgs synpplpplk
     2281 istsngspgf dyhqpgdkfd askqndlggc ngtstmavik dyyalkenei cvsqgevvqv
     2341 lavnqqnmcl vyqpasdhsp aaegwvpgsi lapltkatap aessdesikk scswhtlrmr
     2401 kradventgk neatgprkpk dilgnkasvk etnsseesec ddldpntsme ilnpnfiqev
     2461 apeflvplvd vtcllgdtvl lqckacgrpk ptitwkgpdq nildtdnssa tytisscdsg
     2521 estlkicnlm pqdsgiytci atndhgtast satvkvqgvp aapnrpiaqe rsctsvilrw
     2581 lppastgnct isgytveyre egsqvwqqsv astldtylvi edlspgcpyq frvsasnpwg
     2641 islpsepsef vhlpeydaaa dgatiswken fdsaytelne igrgrfsivk kcihkatrkd
     2701 vavkfvskkm kkkeqaahea allqhlqhpq yvtlhdtyes ptsyililel mddgrlldyl
     2761 mnhdelmeek vafyirdime alqylhncrv ahldikpenl lidlripvpr vklidledav
     2821 qisghfhihh llgnpefaap eviqgipvsl gtdiwsigvl tyvmlsgvsp fldeskeetc
     2881 invcrvdfsf pheyfcgvsn aardfinvil qedfrrrpta atclqhpwlq phngsyskip
     2941 ldtsrlacfi errkhqndvr pipnvksyiv nrvnqgt
//
LOCUS       NP_036803                159 aa            linear   ROD 27-APR-2025
DEFINITION  protransforming growth factor alpha preproprotein [Rattus
            norvegicus].
ACCESSION   NP_036803
VERSION     NP_036803.1
DBSOURCE    REFSEQ: accession NM_012671.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Yu,Y., Chen,E., Weiss,R.M., Felder,R.B. and Wei,S.G.
  TITLE     Transforming Growth Factor-alpha Acts in Hypothalamic
            Paraventricular Nucleus to Upregulate ERK1/2 Signaling and
            Expression of Sympathoexcitatory Mediators in Heart Failure Rats
  JOURNAL   Neuroscience 483, 13-23 (2022)
   PUBMED   34968668
  REMARK    GeneRIF: Transforming Growth Factor-alpha Acts in Hypothalamic
            Paraventricular Nucleus to Upregulate ERK1/2 Signaling and
            Expression of Sympathoexcitatory Mediators in Heart Failure Rats.
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Naito,K., Moteki,H., Kimura,M., Natsume,H. and Ogihara,M.
  TITLE     Serotonin 5-HT2B Receptor-Stimulated DNA Synthesis and
            Proliferation Are Mediated by Autocrine Secretion of Transforming
            Growth Factor-alpha in Primary Cultures of Adult Rat Hepatocytes
  JOURNAL   Biol Pharm Bull 39 (4), 570-577 (2016)
   PUBMED   26804134
  REMARK    GeneRIF: 5-HT stimulates DNA synthesis and proliferation in primary
            cultures of adult rat hepatocytes by acting via autocrine secretion
            of TGF-alpha induced by the serotonin 5-HT2B receptor/Gq/PLC/Ca2+
            pathway.
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Ni,W., Lin,N., He,H., Zhu,J. and Zhang,Y.
  TITLE     Lipopolysaccharide induces up-regulation of TGF-alpha through HDAC2
            in a rat model of bronchopulmonary dysplasia
  JOURNAL   PLoS One 9 (3), e91083 (2014)
   PUBMED   24595367
  REMARK    GeneRIF: Lipopolysaccharide exposure led to a suppression of both
            HDAC1 and HDAC2 expression and activity, induced TGFa expression,
            and disrupted alveolar morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Wong,H.H. and Lemoine,N.R.
  TITLE     Pancreatic cancer: molecular pathogenesis and new therapeutic
            targets
  JOURNAL   Nat Rev Gastroenterol Hepatol 6 (7), 412-422 (2009)
   PUBMED   19506583
  REMARK    Review article
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Kimura,M., Okamoto,H., Natsume,H. and Ogihara,M.
  TITLE     IP receptor agonist-induced DNA synthesis and proliferation in
            primary cultures of adult rat hepatocytes: the involvement of
            endogenous transforming growth factor-alpha
  JOURNAL   J Pharmacol Sci 109 (4), 618-629 (2009)
   PUBMED   19346670
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Korc,M., Chandrasekar,B., Yamanaka,Y., Friess,H., Buchier,M. and
            Beger,H.G.
  TITLE     Overexpression of the epidermal growth factor receptor in human
            pancreatic cancer is associated with concomitant increases in the
            levels of epidermal growth factor and transforming growth factor
            alpha
  JOURNAL   J Clin Invest 90 (4), 1352-1360 (1992)
   PUBMED   1401070
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Luetteke,N.C. and Lee,D.C.
  TITLE     Transforming growth factor alpha: expression, regulation and
            biological action of its integral membrane precursor
  JOURNAL   Semin Cancer Biol 1 (4), 265-275 (1990)
   PUBMED   2103501
  REMARK    Review article
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Blasband,A.J., Rogers,K.T., Chen,X.R., Azizkhan,J.C. and Lee,D.C.
  TITLE     Characterization of the rat transforming growth factor alpha gene
            and identification of promoter sequences
  JOURNAL   Mol Cell Biol 10 (5), 2111-2121 (1990)
   PUBMED   2325647
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Gentry,L.E., Twardzik,D.R., Lim,G.J., Ranchalis,J.E. and Lee,D.C.
  TITLE     Expression and characterization of transforming growth factor alpha
            precursor protein in transfected mammalian cells
  JOURNAL   Mol Cell Biol 7 (5), 1585-1591 (1987)
   PUBMED   3299049
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Lee,D.C., Rose,T.M., Webb,N.R. and Todaro,G.J.
  TITLE     Cloning and sequence analysis of a cDNA for rat transforming growth
            factor-alpha
  JOURNAL   Nature 313 (6002), 489-491 (1985)
   PUBMED   3855503
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M31076.1 and JAXUCZ010000004.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M31076.1, SRR26643288.19572.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..159
                     /product="protransforming growth factor alpha
                     preproprotein"
                     /note="protransforming growth factor alpha"
                     /calculated_mol_wt=14742
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01134.2)"
                     /calculated_mol_wt=2236
     proprotein      23..159
                     /product="transforming growth factor alpha proprotein"
                     /calculated_mol_wt=14856
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01134.2)"
     mat_peptide     39..88
                     /product="transforming growth factor alpha"
                     /calculated_mol_wt=5623
     Region          <43..82
                     /region_name="PHA02887"
                     /note="EGF-like protein; Provisional"
                     /db_xref="CDD:165214"
     Region          <46..120
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     Site            98..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01134.2)"
     CDS             1..159
                     /gene="Tgfa"
                     /gene_synonym="RATTGFAA; TGFAA"
                     /coded_by="NM_012671.2:145..624"
                     /db_xref="GeneID:24827"
                     /db_xref="RGD:3849"
ORIGIN      
        1 mvpaagqlal lalgilvavc qalenstspl sdspvaaavv shfnkcpdsh tqycfhgtcr
       61 flvqeekpac vchsgyvgvr cehadllavv aasqkkqait alvvvsival avliitcvli
      121 hccqvrkhce wcralvcrhe kpsallkgrt acchsetvv
//
LOCUS       NP_001257601             250 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 6 [Rattus norvegicus].
ACCESSION   NP_001257601
VERSION     NP_001257601.1
DBSOURCE    REFSEQ: accession NM_001270672.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (6) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (6) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216784.1, FQ214722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..250
                     /product="troponin T, fast skeletal muscle isoform 6"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29610
     Region          54..190
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..250
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270672.1:117..869"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeeevqeeek prpkltapki pegekvdfdd iqkkrqnkdl
       61 melqalidsh fearkkeeee lialkeriek rraeraeqqr iraekererq nrlaeekarr
      121 eeedakrrae ddlkkkkals smganyssyl akadqkrgkk qtaremkkki laerrkplni
      181 dhlsddklrd kakelwdtly qletdkfefg eklkrqkydi ttlrsridqa qkhskkagat
      241 akgkvggrwk
//
LOCUS       NP_996733                433 aa            linear   ROD 27-APR-2025
DEFINITION  N-lysine methyltransferase SMYD2 [Rattus norvegicus].
ACCESSION   NP_996733 XP_001066311 XP_213972
VERSION     NP_996733.1
DBSOURCE    REFSEQ: accession NM_206851.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Li,Y., Wei,X., Xiao,R., Chen,Y., Xiong,T., Fang,Z.M., Huo,B.,
            Guo,X., Luo,H., Wu,X., Liu,L., Zhu,X.H., Hu,Q., Jiang,D.S. and
            Yi,X.
  TITLE     SMYD2-Methylated PPARgamma Facilitates Hypoxia-Induced Pulmonary
            Hypertension by Activating Mitophagy
  JOURNAL   Circ Res 135 (1), 93-109 (2024)
   PUBMED   38770649
  REMARK    GeneRIF: SMYD2-Methylated PPARgamma Facilitates Hypoxia-Induced
            Pulmonary Hypertension by Activating Mitophagy.
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Sun,X.L., Lv,J.L., Dou,L., Chen,D., Zhu,Y.C. and Hu,X.
  TITLE     LncRNA NEAT1 promotes cardiac hypertrophy through
            microRNA-19a-3p/SMYD2 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (3), 1367-1377 (2020)
   PUBMED   32096186
  REMARK    GeneRIF: LncRNA NEAT1 promotes cardiac hypertrophy through
            microRNA-19a-3p/SMYD2 axis.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Munkanatta Godage,D.N.P., VanHecke,G.C., Samarasinghe,K.T.G.,
            Feng,H.Z., Hiske,M., Holcomb,J., Yang,Z., Jin,J.P., Chung,C.S. and
            Ahn,Y.H.
  TITLE     SMYD2 glutathionylation contributes to degradation of sarcomeric
            proteins
  JOURNAL   Nat Commun 9 (1), 4341 (2018)
   PUBMED   30337525
  REMARK    GeneRIF: SMYD2 glutathionylation is a novel molecular mechanism by
            which reactive oxygen species contribute to sarcomere
            destabilization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Hamamoto,R., Toyokawa,G., Nakakido,M., Ueda,K. and Nakamura,Y.
  TITLE     SMYD2-dependent HSP90 methylation promotes cancer cell
            proliferation by regulating the chaperone complex formation
  JOURNAL   Cancer Lett 351 (1), 126-133 (2014)
   PUBMED   24880080
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Black,J.C., Van Rechem,C. and Whetstine,J.R.
  TITLE     Histone lysine methylation dynamics: establishment, regulation, and
            biological impact
  JOURNAL   Mol Cell 48 (4), 491-507 (2012)
   PUBMED   23200123
  REMARK    Review article
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Kruse,J.P. and Gu,W.
  TITLE     Modes of p53 regulation
  JOURNAL   Cell 137 (4), 609-622 (2009)
   PUBMED   19450511
  REMARK    Review article
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Chen,J., Jiang,H., Xu,L., Zhu,L.H., Wang,L., Wen,H.Z. and Hu,X.R.
  TITLE     Dysregulation of CREB binding protein triggers thrombin-induced
            proliferation of vascular smooth muscle cells
  JOURNAL   Mol Cell Biochem 315 (1-2), 123-130 (2008)
   PUBMED   18496732
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Huang,J., Perez-Burgos,L., Placek,B.J., Sengupta,R., Richter,M.,
            Dorsey,J.A., Kubicek,S., Opravil,S., Jenuwein,T. and Berger,S.L.
  TITLE     Repression of p53 activity by Smyd2-mediated methylation
  JOURNAL   Nature 444 (7119), 629-632 (2006)
   PUBMED   17108971
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Brown,M.A., Sims,R.J. 3rd, Gottlieb,P.D. and Tucker,P.W.
  TITLE     Identification and characterization of Smyd2: a split SET/MYND
            domain-containing histone H3 lysine 36-specific methyltransferase
            that interacts with the Sin3 histone deacetylase complex
  JOURNAL   Mol Cancer 5, 26 (2006)
   PUBMED   16805913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Oduru,S., Campbell,J.L., Karri,S., Hendry,W.J., Khan,S.A. and
            Williams,S.C.
  TITLE     Gene discovery in the hamster: a comparative genomics approach for
            gene annotation by sequencing of hamster testis cDNAs
  JOURNAL   BMC Genomics 4 (1), 22 (2003)
   PUBMED   12783626
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB726546.1, BK001057.1 and AW433707.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_001066311.1, XP_213972.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001057.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..433
                     /product="N-lysine methyltransferase SMYD2"
                     /EC_number="2.1.1.354"
                     /note="SET and MYND domain-containing protein 2; histone
                     methyltransferase SMYD2"
                     /calculated_mol_wt=49517
     Region          7..269
                     /region_name="SET_SMYD2"
                     /note="SET domain (including post-SET domain) found in SET
                     and MYND domain-containing protein 2 (SMYD2) and similar
                     proteins; cd19202"
                     /db_xref="CDD:380979"
     Site            order(16..19,105,135,137,141,145,149,177,179..185,196,
                     203..207,238..240,257..260)
                     /site_type="active"
                     /db_xref="CDD:380979"
     Site            order(16..19,135,137,181..182,203..207,240,258,260)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380979"
     Region          52..90
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     Site            order(105,141,145,149,177,179..185,196,203,238..240,
                     257..259)
                     /site_type="inhibition"
                     /note="inhibitor binding site [chemical binding]"
                     /db_xref="CDD:380979"
     Site            order(105,179,181..185,193,203,239..240,242,258)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380979"
     Site            order(209,262,264,267)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380979"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q7M6Z3.1)"
     Region          388..422
                     /region_name="TPR_10"
                     /note="Tetratricopeptide repeat; pfam13374"
                     /db_xref="CDD:463861"
     CDS             1..433
                     /gene="Smyd2"
                     /gene_synonym="HSKM-B"
                     /coded_by="NM_206851.1:35..1336"
                     /db_xref="GeneID:289372"
                     /db_xref="RGD:727785"
ORIGIN      
        1 mraearggle rfcsagkgrg lralrpfhvg dllfscpaya cvltvgergh hceccfarke
       61 glskcgrckq afycdvecqk edwplhklec ssmvvfgenw npsetvrlta rilakqkmhp
      121 ertpseklla vrefeshldk ldnekkdliq sdiaalhqfy skhlefpdhs slvvlfaqvn
      181 cngftiedee lshlgsaifp dvalmnhscc pnvivtykgt laevravqei hpgdevftsy
      241 idllyptedr ndrlrdsyff tcecrecttk dkdkakveir klsnppqaea irdmvryarn
      301 vieefrrakh ykspsellei celsqekmss vfedsnvyml hmmyqamgvc lymqdwegal
      361 kygqkiikpy skhypvysln vasmwlklgr lymglenkaa gekalkkaia imeiahgkdh
      421 pyiseikqei esh
//
LOCUS       NP_001296333             583 aa            linear   ROD 27-APR-2025
DEFINITION  small conductance calcium-activated potassium channel protein 2
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_001296333 XP_006254744
VERSION     NP_001296333.1
DBSOURCE    REFSEQ: accession NM_001309404.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Rahman,M.A., Orfali,R., Dave,N., Lam,E., Naguib,N., Nam,Y.W. and
            Zhang,M.
  TITLE     KCa 2.2 (KCNN2): A physiologically and therapeutically important
            potassium channel
  JOURNAL   J Neurosci Res 101 (11), 1699-1710 (2023)
   PUBMED   37466411
  REMARK    GeneRIF: KCa 2.2 (KCNN2): A physiologically and therapeutically
            important potassium channel.
            Review article
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Nam,Y.W., Rahman,M.A., Yang,G., Orfali,R., Cui,M. and Zhang,M.
  TITLE     Loss-of-function KCa2.2 mutations abolish channel activity
  JOURNAL   Am J Physiol Cell Physiol 324 (3), C658-C664 (2023)
   PUBMED   36717104
  REMARK    GeneRIF: Loss-of-function KCa2.2 mutations abolish channel
            activity.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Yang,B., Jiang,Q., He,S., Li,T., Ou,X., Chen,T., Fan,X., Jiang,F.,
            Zeng,X., Huang,C.L., Lei,M. and Tan,X.
  TITLE     Ventricular SK2 upregulation following angiotensin II challenge:
            Modulation by p21-activated kinase-1
  JOURNAL   J Mol Cell Cardiol 164, 110-125 (2022)
   PUBMED   34774547
  REMARK    GeneRIF: Ventricular SK2 upregulation following angiotensin II
            challenge: Modulation by p21-activated kinase-1.
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Autuori,E., Sedlak,P., Xu,L., C Ridder,M., Tedoldi,A. and Sah,P.
  TITLE     rSK1 in Rat Neurons: A Controller of Membrane rSK2?
  JOURNAL   Front Neural Circuits 13, 21 (2019)
   PUBMED   31001092
  REMARK    GeneRIF: rSK1 appears to act as chaperone for rSK2 channels and
            expression of rSK1 may control the level of functional SK current
            in rat neurons.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Ewin,S.E., Morgan,J.W., Niere,F., McMullen,N.P., Barth,S.H.,
            Almonte,A.G., Raab-Graham,K.F. and Weiner,J.L.
  TITLE     Chronic Intermittent Ethanol Exposure Selectively Increases
            Synaptic Excitability in the Ventral Domain of the Rat Hippocampus
  JOURNAL   Neuroscience 398, 144-157 (2019)
   PUBMED   30481568
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Schumacher,M.A., Crum,M. and Miller,M.C.
  TITLE     Crystal structures of apocalmodulin and an apocalmodulin/SK
            potassium channel gating domain complex
  JOURNAL   Structure 12 (5), 849-860 (2004)
   PUBMED   15130477
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Monaghan,A.S., Benton,D.C., Bahia,P.K., Hosseini,R., Shah,Y.A.,
            Haylett,D.G. and Moss,G.W.
  TITLE     The SK3 subunit of small conductance Ca2+-activated K+ channels
            interacts with both SK1 and SK2 subunits in a heterologous
            expression system
  JOURNAL   J Biol Chem 279 (2), 1003-1009 (2004)
   PUBMED   14559917
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Schumacher,M.A., Rivard,A.F., Bachinger,H.P. and Adelman,J.P.
  TITLE     Structure of the gating domain of a Ca2+-activated K+ channel
            complexed with Ca2+/calmodulin
  JOURNAL   Nature 410 (6832), 1120-1124 (2001)
   PUBMED   11323678
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Xia,X.M., Fakler,B., Rivard,A., Wayman,G., Johnson-Pais,T.,
            Keen,J.E., Ishii,T., Hirschberg,B., Bond,C.T., Lutsenko,S.,
            Maylie,J. and Adelman,J.P.
  TITLE     Mechanism of calcium gating in small-conductance calcium-activated
            potassium channels
  JOURNAL   Nature 395 (6701), 503-507 (1998)
   PUBMED   9774106
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Kohler,M., Hirschberg,B., Bond,C.T., Kinzie,J.M., Marrion,N.V.,
            Maylie,J. and Adelman,J.P.
  TITLE     Small-conductance, calcium-activated potassium channels from
            mammalian brain
  JOURNAL   Science 273 (5282), 1709-1714 (1996)
   PUBMED   8781233
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Jun 2, 2015 this sequence version replaced XP_006254744.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JN857942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418971 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..583
                     /product="small conductance calcium-activated potassium
                     channel protein 2 isoform 1"
                     /note="small conductance calcium-activated potassium
                     channel protein 2; small conductance calcium-activated
                     potassium channel protein 2-like; potassium
                     intermediate/small conductance calcium-activated channel,
                     subfamily N, member 2; potassium channel, calcium
                     activated intermediate/small conductance subfamily N
                     alpha, member 2"
                     /calculated_mol_wt=64072
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          88..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          122..231
                     /region_name="SK_channel"
                     /note="Calcium-activated SK potassium channel; pfam03530"
                     /db_xref="CDD:460958"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P70604.1)"
     Site            169..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          320..399
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          413..491
                     /region_name="CaMBD"
                     /note="Calmodulin binding domain; smart01053"
                     /db_xref="CDD:198121"
     Region          554..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     CDS             1..583
                     /gene="Kcnn2"
                     /gene_synonym="KCa2.2; SK2; SKCa 2; SKCa2"
                     /coded_by="NM_001309404.1:1..1752"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:54262"
                     /db_xref="RGD:2963"
ORIGIN      
        1 msscrynggv mrplsnlsss rrnlhemdse aqplqppasv vgggggassp saaaaasssa
       61 peivvskpeh nnsnnlalyg tggggstggg gggggggggs ghgsssgtks skkknqnigy
      121 klghrralfe krkrlsdyal ifgmfgivvm vietelswga ydkaslysla lkclislsti
      181 illgliivyh areiqlfmvd ngaddwriam tyerifficl eilvcaihpi pgnytftwta
      241 rlafsyapst ttadvdiils ipmflrlyli arvmllhskl ftdassrsig alnkinfntr
      301 fvmktlmtic pgtvllvfsi slwiiaawtv raceryhdqq dvtsnflgam wlisitflsi
      361 gygdmvpnty cgkgvclltg imgagctalv vavvarklel tkaekhvhnf mmdtqltkrv
      421 knaaanvlre twliykntkl vkkidhakvr khqrkflqai hqarklrsvk meqrklndqa
      481 ntlvdlaktq nimydmisdl nersedfekr ivtletklet ligsihalpg lisqtirqqq
      541 rdfietqmen ydkhvtynae rsrsssrrrr ssstapptss ess
//
LOCUS       NP_001014275             195 aa            linear   ROD 27-APR-2025
DEFINITION  thioredoxin reductase-like selenoprotein T precursor [Rattus
            norvegicus].
ACCESSION   NP_001014275 XP_345216
VERSION     NP_001014275.2
DBSOURCE    REFSEQ: accession NM_001014253.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   De Bartolo,A., Pasqua,T., Romeo,N., Rago,V., Perrotta,I.,
            Giordano,F., Granieri,M.C., Marrone,A., Mazza,R., Cerra,M.C.,
            Lefranc,B., Leprince,J., Anouar,Y., Angelone,T. and Rocca,C.
  TITLE     The redox-active defensive Selenoprotein T as a novel stress sensor
            protein playing a key role in the pathophysiology of heart failure
  JOURNAL   J Transl Med 22 (1), 375 (2024)
   PUBMED   38643121
  REMARK    GeneRIF: The redox-active defensive Selenoprotein T as a novel
            stress sensor protein playing a key role in the pathophysiology of
            heart failure.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Huang,J., Bao,D., Lei,C.T., Tang,H., Zhang,C.Y., Su,H. and Zhang,C.
  TITLE     Selenoprotein T protects against cisplatin-induced acute kidney
            injury through suppression of oxidative stress and apoptosis
  JOURNAL   FASEB J 34 (9), 11983-11996 (2020)
   PUBMED   32686857
  REMARK    GeneRIF: Selenoprotein T protects against cisplatin-induced acute
            kidney injury through suppression of oxidative stress and
            apoptosis.
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Abid,H., Cartier,D., Hamieh,A., Francois-Bellan,A.M., Bucharles,C.,
            Pothion,H., Manecka,D.L., Leprince,J., Adriouch,S., Boyer,O.,
            Anouar,Y. and Lihrmann,I.
  TITLE     AMPK Activation of PGC-1alpha/NRF-1-Dependent SELENOT Gene
            Transcription Promotes PACAP-Induced Neuroendocrine Cell
            Differentiation Through Tolerance to Oxidative Stress
  JOURNAL   Mol Neurobiol 56 (6), 4086-4101 (2019)
   PUBMED   30267375
  REMARK    GeneRIF: PACAP and cAMP-activated AMPK-PGC-1alpha/NRF-1 cascade is
            critical for the coupling of oxidative stress tolerance, via
            SELENOT gene expression, and mitochondrial biogenesis in order to
            achieve PC12 cell differentiation.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Gladyshev,V.N., Arner,E.S., Berry,M.J., Brigelius-Flohe,R.,
            Bruford,E.A., Burk,R.F., Carlson,B.A., Castellano,S., Chavatte,L.,
            Conrad,M., Copeland,P.R., Diamond,A.M., Driscoll,D.M., Ferreiro,A.,
            Flohe,L., Green,F.R., Guigo,R., Handy,D.E., Hatfield,D.L.,
            Hesketh,J., Hoffmann,P.R., Holmgren,A., Hondal,R.J., Howard,M.T.,
            Huang,K., Kim,H.Y., Kim,I.Y., Kohrle,J., Krol,A., Kryukov,G.V.,
            Lee,B.J., Lee,B.C., Lei,X.G., Liu,Q., Lescure,A., Lobanov,A.V.,
            Loscalzo,J., Maiorino,M., Mariotti,M., Sandeep Prabhu,K.,
            Rayman,M.P., Rozovsky,S., Salinas,G., Schmidt,E.E., Schomburg,L.,
            Schweizer,U., Simonovic,M., Sunde,R.A., Tsuji,P.A., Tweedie,S.,
            Ursini,F., Whanger,P.D. and Zhang,Y.
  TITLE     Selenoprotein Gene Nomenclature
  JOURNAL   J Biol Chem 291 (46), 24036-24040 (2016)
   PUBMED   27645994
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Li,J.P., Zhou,J.X., Wang,Q., Gu,G.Q., Yang,S.J., Li,C.Y., Qiu,C.W.,
            Deng,G.Z. and Guo,M.Y.
  TITLE     Se Enhances MLCK Activation by Regulating Selenoprotein T (SelT) in
            the Gastric Smooth Muscle of Rats
  JOURNAL   Biol Trace Elem Res 173 (1), 116-125 (2016)
   PUBMED   26779623
  REMARK    GeneRIF: Se plays a major role in regulating the contraction
            processes of gastric smooth muscle with the SelT.
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Boukhzar,L., Hamieh,A., Cartier,D., Tanguy,Y., Alsharif,I.,
            Castex,M., Arabo,A., El Hajji,S., Bonnet,J.J., Errami,M.,
            Falluel-Morel,A., Chagraoui,A., Lihrmann,I. and Anouar,Y.
  TITLE     Selenoprotein T Exerts an Essential Oxidoreductase Activity That
            Protects Dopaminergic Neurons in Mouse Models of Parkinson's
            Disease
  JOURNAL   Antioxid Redox Signal 24 (11), 557-574 (2016)
   PUBMED   26866473
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Guo,M., Gao,X., Zhang,N., Qiu,C., Li,C. and Deng,G.
  TITLE     Effects of Se on the Diversity of SelT Synthesis and Distribution
            in Different Smooth Muscle Tissues in Rats
  JOURNAL   Biol Trace Elem Res 170 (2), 340-347 (2016)
   PUBMED   26280902
  REMARK    GeneRIF: SelT may play a major role in the mechanisms underlying
            the biological activity of Se in smooth muscle tissues.
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Prevost,G., Arabo,A., Jian,L., Quelennec,E., Cartier,D., Hassan,S.,
            Falluel-Morel,A., Tanguy,Y., Gargani,S., Lihrmann,I.,
            Kerr-Conte,J., Lefebvre,H., Pattou,F. and Anouar,Y.
  TITLE     The PACAP-regulated gene selenoprotein T is abundantly expressed in
            mouse and human beta-cells and its targeted inactivation impairs
            glucose tolerance
  JOURNAL   Endocrinology 154 (10), 3796-3806 (2013)
   PUBMED   23913443
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Tanguy,Y., Falluel-Morel,A., Arthaud,S., Boukhzar,L., Manecka,D.L.,
            Chagraoui,A., Prevost,G., Elias,S., Dorval-Coiffec,I., Lesage,J.,
            Vieau,D., Lihrmann,I., Jegou,B. and Anouar,Y.
  TITLE     The PACAP-regulated gene selenoprotein T is highly induced in
            nervous, endocrine, and metabolic tissues during ontogenetic and
            regenerative processes
  JOURNAL   Endocrinology 152 (11), 4322-4335 (2011)
   PUBMED   21896670
  REMARK    GeneRIF: SelT induction is associated with ontogenesis, tissue
            maturation, and regenerative mechanisms, indicating that this
            PACAP-regulated selenoprotein may play a crucial role in cell
            growth and activity in nervous, endocrine, and metabolic tissues.
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Grumolato,L., Ghzili,H., Montero-Hadjadje,M., Gasman,S., Lesage,J.,
            Tanguy,Y., Galas,L., Ait-Ali,D., Leprince,J., Guerineau,N.C.,
            Elkahloun,A.G., Fournier,A., Vieau,D., Vaudry,H. and Anouar,Y.
  TITLE     Selenoprotein T is a PACAP-regulated gene involved in intracellular
            Ca2+ mobilization and neuroendocrine secretion
  JOURNAL   FASEB J 22 (6), 1756-1768 (2008)
   PUBMED   18198219
  REMARK    GeneRIF: role in the regulation of Ca(2+) homeostasis and
            neuroendocrine secretion in response to a cAMP-stimulating trophic
            factor.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000002.1, FM042340.1
            and FM061880.1.
            
            On Apr 6, 2007 this sequence version replaced NP_001014275.1.
            
            Summary: This gene encodes a selenoprotein, containing a
            selenocysteine (Sec) residue at the active site. Sec is encoded by
            the UGA codon that normally signals translation termination. The 3'
            UTRs of selenoprotein mRNAs contain a conserved stem-loop
            structure, the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon rather than as
            a stop signal. This protein is localized in the endoplasmic
            reticulum. It belongs to the SelWTH family that possesses a
            thioredoxin-like fold and a conserved CxxU (C is cysteine, U is
            Sec) motif found in several redox active proteins. Studies in rat
            indicate a role for this gene in the regulation of calcium
            homeostasis and smooth muscle contraction. High induction of this
            gene is also associated with ontogenetic and regenerative processes
            in nervous, endocrine, and metabolic tissues. A pseudogene of this
            locus has been identified on chromosome 4. [provided by RefSeq, Aug
            2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211813.1, SRR26643293.12308.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: inferred from conservation
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..195
                     /product="thioredoxin reductase-like selenoprotein T
                     precursor"
                     /EC_number="1.8.1.9"
                     /note="thioredoxin reductase-like enzyme; thioredoxin
                     reductase-like selenoprotein T"
                     /calculated_mol_wt=20285
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2026
     mat_peptide     20..195
                     /product="Thioredoxin reductase-like selenoprotein T.
                     /evidence=ECO:0000255. /id=PRO_0000252038"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1H5H1.2)"
                     /calculated_mol_wt=20285
     Region          41..179
                     /region_name="CXXU_selWTH"
                     /note="selT/selW/selH selenoprotein domain; TIGR02174"
                     /db_xref="CDD:274013"
     Site            49
                     /site_type="other"
                     /note="Selenocysteine"
     Site            85..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1H5H1.2)"
     CDS             1..195
                     /gene="Selenot"
                     /coded_by="NM_001014253.3:68..655"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:365802"
                     /db_xref="RGD:1359128"
ORIGIN      
        1 mrllllllva asavvrseas anlggvpskr lkmqyatgpl lkfqicvsug yrrvfeeymr
       61 visqrypdir iegenylpqp iyrhiasfls vfklvligli ivgkdpfaff gmqapsiwqw
      121 gqenkvyacm mvfflsnmie nqcmstgafe itlndvpvws klesghlpsm qqlvqildne
      181 mklnvhmdsi phhrs
//
LOCUS       NP_001263636            1134 aa            linear   ROD 27-APR-2025
DEFINITION  sterol regulatory element-binding protein 1 isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001263636 XP_001075680 XP_213329
VERSION     NP_001263636.1
DBSOURCE    REFSEQ: accession NM_001276707.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Li,H., Liu,Y., Meng,F., Chen,J. and Han,X.
  TITLE     Adrenarche-accompanied rise of adrenal sex steroid precursors
            prevents NAFLD in Young Female rats by converting into active
            androgens and inactivating hepatic Srebf1 signaling
  JOURNAL   BMC Genomics 25 (1), 190 (2024)
   PUBMED   38369486
  REMARK    GeneRIF: Adrenarche-accompanied rise of adrenal sex steroid
            precursors prevents NAFLD in Young Female rats by converting into
            active androgens and inactivating hepatic Srebf1 signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Ma,P., Huang,J., Chen,B., Huang,M., Xiong,L., Chen,J., Huang,S. and
            Liu,Y.
  TITLE     Lanosterol Synthase Prevents EMT During Lens Epithelial Fibrosis
            Via Regulating SREBP1
  JOURNAL   Invest Ophthalmol Vis Sci 64 (15), 12 (2023)
   PUBMED   38079167
  REMARK    GeneRIF: Lanosterol Synthase Prevents EMT During Lens Epithelial
            Fibrosis Via Regulating SREBP1.
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Bian,C., Zhang,H., Gao,J., Wang,Y., Li,J., Guo,D., Wang,W.,
            Song,Y., Weng,Y. and Ren,H.
  TITLE     SIRT6 regulates SREBP1c-induced glucolipid metabolism in liver and
            pancreas via the AMPKalpha-mTORC1 pathway
  JOURNAL   Lab Invest 102 (5), 474-484 (2022)
   PUBMED   34923569
  REMARK    GeneRIF: SIRT6 regulates SREBP1c-induced glucolipid metabolism in
            liver and pancreas via the AMPKalpha-mTORC1 pathway.
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Yalcin,M. and Kacar,M.
  TITLE     Investigation of the hepatic mTOR/S6K1/SREBP1 signalling pathway in
            rats at different ages: from neonates to adults
  JOURNAL   Mol Biol Rep 48 (11), 7415-7422 (2021)
   PUBMED   34655015
  REMARK    GeneRIF: Investigation of the hepatic mTOR/S6K1/SREBP1 signalling
            pathway in rats at different ages: from neonates to adults.
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Kilby,E.L., Kelly,D.M. and Jones,T.H.
  TITLE     Testosterone stimulates cholesterol clearance from human
            macrophages by activating LXRalpha
  JOURNAL   Life Sci 269, 119040 (2021)
   PUBMED   33453241
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   Boizard,M., Le Liepvre,X., Lemarchand,P., Foufelle,F., Ferre,P. and
            Dugail,I.
  TITLE     Obesity-related overexpression of fatty-acid synthase gene in
            adipose tissue involves sterol regulatory element-binding protein
            transcription factors
  JOURNAL   J Biol Chem 273 (44), 29164-29171 (1998)
   PUBMED   9786926
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Shimano,H., Shimomura,I., Hammer,R.E., Herz,J., Goldstein,J.L.,
            Brown,M.S. and Horton,J.D.
  TITLE     Elevated levels of SREBP-2 and cholesterol synthesis in livers of
            mice homozygous for a targeted disruption of the SREBP-1 gene
  JOURNAL   J Clin Invest 100 (8), 2115-2124 (1997)
   PUBMED   9329978
REFERENCE   8  (residues 1 to 1134)
  AUTHORS   Sawada,Y. and Noda,M.
  TITLE     An adipogenic basic helix-loop-helix-leucine zipper type
            transcription factor (ADD1) mRNA is expressed and regulated by
            retinoic acid in osteoblastic cells
  JOURNAL   Mol Endocrinol 10 (10), 1238-1248 (1996)
   PUBMED   9121491
REFERENCE   9  (residues 1 to 1134)
  AUTHORS   Kim,J.B., Spotts,G.D., Halvorsen,Y.D., Shih,H.M., Ellenberger,T.,
            Towle,H.C. and Spiegelman,B.M.
  TITLE     Dual DNA binding specificity of ADD1/SREBP1 controlled by a single
            amino acid in the basic helix-loop-helix domain
  JOURNAL   Mol Cell Biol 15 (5), 2582-2588 (1995)
   PUBMED   7739539
REFERENCE   10 (residues 1 to 1134)
  AUTHORS   Tontonoz,P., Kim,J.B., Graves,R.A. and Spiegelman,B.M.
  TITLE     ADD1: a novel helix-loop-helix transcription factor associated with
            adipocyte determination and differentiation
  JOURNAL   Mol Cell Biol 13 (8), 4753-4759 (1993)
   PUBMED   8336713
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Feb 28, 2013 this sequence version replaced
            XP_213329.5, XP_001075680.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.40892.1,
                                           SRR26643297.34196.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..1134
                     /product="sterol regulatory element-binding protein 1
                     isoform 1 precursor"
                     /note="sterol regulatory element-binding protein 1;
                     adipocyte determination- and differentiation-dependent
                     factor 1"
                     /calculated_mol_wt=120390
     mat_peptide     1..480
                     /product="Processed sterol regulatory element-binding
                     protein 1. /evidence=ECO:0000250|UniProtKB:Q12772.
                     /id=PRO_0000314031"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
                     /calculated_mol_wt=49463
     Region          1..60
                     /region_name="Transcriptional activation (acidic).
                     /evidence=ECO:0000250|UniProtKB:P36956"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Region          27..35
                     /region_name="9aaTAD.
                     /evidence=ECO:0000250|UniProtKB:P36956"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Region          46..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Region          58..>230
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Region          116..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P36956; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Region          227..487
                     /region_name="Interaction with LMNA.
                     /evidence=ECO:0000250|UniProtKB:Q9WTN3"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Region          313..384
                     /region_name="bHLHzip_SREBP1"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in sterol regulatory element-binding protein 1
                     (SREBP1) and similar proteins; cd18921"
                     /db_xref="CDD:381491"
     Site            order(313,319,321..323,325..326,328..330,334,352..353)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381491"
     Site            order(329,332..333,336..337,339..340,343,353..354,
                     357..358,361,363..365,367..368,370..371,374..375,377..378,
                     381..382)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381491"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SIK1.
                     /evidence=ECO:0000250|UniProtKB:Q9WTN3; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SIK1.
                     /evidence=ECO:0000250|UniProtKB:Q9WTN3; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Region          367..388
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q9WTN3; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SIK1.
                     /evidence=ECO:0000250|UniProtKB:Q9WTN3; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Region          415..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            451..452
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and caspase-7.
                     /evidence=ECO:0000250|UniProtKB:Q12772; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            480..481
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS2.
                     /evidence=ECO:0000250|UniProtKB:Q12772; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Site            519..520
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS1.
                     /evidence=ECO:0000250|UniProtKB:P36956; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     Site            537..557
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56720.3)"
     Region          <562..1071
                     /region_name="COG3899"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443106"
     Site            1047
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P36956; propagated from
                     UniProtKB/Swiss-Prot (P56720.3)"
     CDS             1..1134
                     /gene="Srebf1"
                     /gene_synonym="ADD-1; ADD1; SREBP-1; SREBP-1c; Srebp1"
                     /coded_by="NM_001276707.1:81..3485"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:78968"
                     /db_xref="RGD:69423"
ORIGIN      
        1 mdelpfgeaa leqalaevce mdaalltdie dmlqlinnqd sdfpglfdap yaggetgdtg
       61 psspgasspe sfsspaslgs sleaflggpk vtpaplsppp saptavkmyp svppfspgpg
      121 ikeepvplti lqppapqpsp gtllppsfpp ppvqlspapv lgysslpsgf sgtlpgntqq
      181 tpsslplgst pgisptplht qvqssaaqqp ppasaaprms tvasqiqqvp vvlqphfika
      241 dsllltavkt dtgatmktag intlapgtav qagplqtlvs ggtilatvpl vvdtdklpih
      301 rlaaggkalg saqsrgekrt ahnaiekryr ssindkivel kdlvvgteak lnksavlrka
      361 idyirflqhs nqklkqenlt lrsahksksl kdlvsacgsg ggtdvsmegm kpevvetltp
      421 ppsdagspsq ssplslgsrg sssggsdsep dspafednqv kaqrlpshsr gmldrsrlal
      481 cvlvflcltc nplaslfgwg iltpsdasgv hrssgrsmle aesrdgsnwt qwllpplvwl
      541 angllvlacl allfvygepv trphsgpavh fwrhrkqadl dlargdfaqa aqqlwlalqa
      601 lgrplptsnl dlacsllwnl vrhllqrlwv grwlagqagg lqrdyrlrkd arasardaav
      661 vyhklhqlha mgkytgghlv asnlalsaln laecagdais matlaeiyva aalrvktslp
      721 ralhfltrff lssarqacla qsgavplamq wlchpvghrf fvdgdwavhg apqeslysva
      781 gnpvdplaqv trlfcehlle ralnciaqps pgaadgdref sdalgylqll nscsdavgap
      841 acsfsvsssm atttgtdpva kwwasltavv ihwlrrdeea aerlyplveh ipqvlqeter
      901 plpraalysf kaaralldhr kvesspasla icekasgylr dslaststas sidkamqlll
      961 cdlllvarts lwrrqqsaas aqgahgtsng pqasalelrg fqhdlsslrr laqsfrpamr
     1021 rvflheatar lmagaspart hqlldrslrr ragssgkgga aaeleprptw rehteallla
     1081 scylppafls apgqrvsmla eaartveklg dhrllldcqq mllrlgggtt vtss
//
LOCUS       NP_001007660             263 aa            linear   ROD 27-APR-2025
DEFINITION  autophagy-related protein 101 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001007660 XP_217036
VERSION     NP_001007660.2
DBSOURCE    REFSEQ: accession NM_001007659.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Zhang,Z.J., Wang,K.P., Huang,Y.P., Jin,C., Jiang,H., Xiong,L.,
            Chen,Z.Y., Wen,Y., Liu,Z.T. and Mo,J.G.
  TITLE     Comprehensive Analysis of the Potential Immune-Related Biomarker
            ATG101 that Regulates Apoptosis of Cholangiocarcinoma Cells After
            Photodynamic Therapy
  JOURNAL   Front Pharmacol 13, 857774 (2022)
   PUBMED   35592424
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wang,Y., Lin,K., Xu,T., Wang,L., Fu,L., Zhang,G., Ai,J., Jiao,Y.,
            Zhu,R., Han,X. and Cai,H.
  TITLE     Development and validation of prognostic model based on the
            analysis of autophagy-related genes in colon cancer
  JOURNAL   Aging (Albany NY) 13 (14), 19028-19047 (2021)
   PUBMED   34315829
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Hosokawa,N., Sasaki,T., Iemura,S., Natsume,T., Hara,T. and
            Mizushima,N.
  TITLE     Atg101, a novel mammalian autophagy protein interacting with Atg13
  JOURNAL   Autophagy 5 (7), 973-979 (2009)
   PUBMED   19597335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC079170.1.
            
            On Sep 1, 2012 this sequence version replaced NP_001007660.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by {transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079170.1, SRR26643295.30286.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..263
                     /product="autophagy-related protein 101 isoform 1"
                     /note="autophagy-related protein 101"
                     /calculated_mol_wt=29752
     Region          56..213
                     /region_name="ATG101"
                     /note="Autophagy-related protein 101; pfam07855"
                     /db_xref="CDD:462290"
     CDS             1..263
                     /gene="Atg101"
                     /gene_synonym="RGD1359310"
                     /coded_by="NM_001007659.2:355..1146"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300240"
                     /db_xref="RGD:1359310"
ORIGIN      
        1 mnasltslgl rtgnleawpl adpkgwplrg vkrlvsrlcs ssscrmncrs evlevsvegr
       61 qveeamlavl htvllhrstg kfhykkegty sigtvgiqdv dcdfidftyv rvsseeldra
      121 lrkvvgefkd alrnsggdgl gqmslefyqk kksrwpfsde cipwevwtvk vhvvalateq
      181 erqicrekvg eklcekiini vevmsrheyl pkmptqseld nvfdtglrdv qpylykisfq
      241 itealgtsvt ttmrrlikdt lal
//
LOCUS       NP_037354                198 aa            linear   ROD 27-APR-2025
DEFINITION  FAD-linked sulfhydryl oxidase ALR [Rattus norvegicus].
ACCESSION   NP_037354
VERSION     NP_037354.2
DBSOURCE    REFSEQ: accession NM_013222.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Goyal,S., Tiwari,S., Seth,B., Tandon,A., Shankar,J., Sinha,M.,
            Singh,S.J., Priya,S. and Chaturvedi,R.K.
  TITLE     Bisphenol-A inhibits mitochondrial biogenesis via impairment of
            GFER mediated mitochondrial protein import in the rat brain
            hippocampus
  JOURNAL   Neurotoxicology 85, 18-32 (2021)
   PUBMED   33878312
  REMARK    GeneRIF: Bisphenol-A inhibits mitochondrial biogenesis via
            impairment of GFER mediated mitochondrial protein import in the rat
            brain hippocampus.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Mordas,A. and Tokatlidis,K.
  TITLE     The MIA pathway: a key regulator of mitochondrial oxidative protein
            folding and biogenesis
  JOURNAL   Acc Chem Res 48 (8), 2191-2199 (2015)
   PUBMED   26214018
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Chen,G.T., Zhang,L., Liao,X.H., Yan,R.Y., Li,Y., Sun,H., Guo,H. and
            Liu,Q.
  TITLE     Augmenter of liver regeneration ameliorates renal fibrosis in rats
            with obstructive nephropathy
  JOURNAL   Biosci Rep 34 (5), e00135 (2014)
   PUBMED   24844766
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Francavilla,A., Pesetti,B., Barone,M., Morgano,A., Bovenga,F.,
            Napoli,A., Resta,L., Russo,F., Linsalata,M., Minoia,M., Bianco,G.,
            Tafaro,A. and Polimeno,L.
  TITLE     Transient GFER knockdown in vivo impairs liver regeneration after
            partial hepatectomy
  JOURNAL   Int J Biochem Cell Biol 53, 343-351 (2014)
   PUBMED   24880092
  REMARK    GeneRIF: our results demonstrate that Growth Factor Erv1-Like gene
            knock-down, i.e., the lack of Augmenter of Liver Regeneration,
            modifies the expression of genes involved in cell apoptosis and
            inhibits early phase of DNA synthesis.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Gandhi,C.R., Kuddus,R., Subbotin,V.M., Prelich,J., Murase,N.,
            Rao,A.S., Nalesnik,M.A., Watkins,S.C., DeLeo,A., Trucco,M. and
            Starzl,T.E.
  TITLE     A fresh look at augmenter of liver regeneration in rats
  JOURNAL   Hepatology 29 (5), 1435-1445 (1999)
   PUBMED   10216127
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Suzuki,K., Koh,Y.H., Mizuno,H., Hamaoka,R. and Taniguchi,N.
  TITLE     Overexpression of aldehyde reductase protects PC12 cells from the
            cytotoxicity of methylglyoxal or 3-deoxyglucosone
  JOURNAL   J Biochem 123 (2), 353-357 (1998)
   PUBMED   9538214
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Francavilla,A., Vujanovic,N.L., Polimeno,L., Azzarone,A.,
            Iacobellis,A., Deleo,A., Hagiya,M., Whiteside,T.L. and Starzl,T.E.
  TITLE     The in vivo effect of hepatotrophic factors augmenter of liver
            regeneration, hepatocyte growth factor, and insulin-like growth
            factor-II on liver natural killer cell functions
  JOURNAL   Hepatology 25 (2), 411-415 (1997)
   PUBMED   9021955
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Hagiya,M., Francavilla,A., Polimeno,L., Ihara,I., Sakai,H.,
            Seki,T., Shimonishi,M., Porter,K.A. and Starzl,T.E.
  TITLE     Cloning and sequence analysis of the rat augmenter of liver
            regeneration (ALR) gene: expression of biologically active
            recombinant ALR and demonstration of tissue distribution
  JOURNAL   Proc Natl Acad Sci U S A 92 (7), 3076 (1995)
   PUBMED   7708779
  REMARK    Correction to:[Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8142-6.
            doi: 10.1073/pnas.91.17.8142. PMID: 8058770]
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Hagiya,M., Francavilla,A., Polimeno,L., Ihara,I., Sakai,H.,
            Seki,T., Shimonishi,M., Porter,K.A. and Starzl,T.E.
  TITLE     Cloning and sequence analysis of the rat augmenter of liver
            regeneration (ALR) gene: expression of biologically active
            recombinant ALR and demonstration of tissue distribution
  JOURNAL   Proc Natl Acad Sci U S A 91 (17), 8142-8146 (1994)
   PUBMED   8058770
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):3076. doi:
            10.1073/pnas.92.7.3076d. PMID: 7708779]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Sep 27, 2011 this sequence version replaced NP_037354.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D30735.1, SRR26360194.587100.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN12840129
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..198
                     /product="FAD-linked sulfhydryl oxidase ALR"
                     /EC_number="1.8.3.2"
                     /note="growth factor, erv1 homolog; growth factor,
                     erv1-like (augmenter of liver regeneration); FAD-linked
                     sulfhydryl oxidase ALR-like; translation initiation factor
                     IF-2-like"
                     /calculated_mol_wt=22706
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63042.2)"
     Region          97..189
                     /region_name="Evr1_Alr"
                     /note="Erv1 / Alr family; pfam04777"
                     /db_xref="CDD:461423"
     CDS             1..198
                     /gene="Gfer"
                     /gene_synonym="ALR"
                     /coded_by="NM_013222.2:82..678"
                     /db_xref="GeneID:27100"
                     /db_xref="RGD:61845"
ORIGIN      
        1 maapsepagf prgsrfsflp ggahsemtdd lvtdargrga rhrkdnapaa apapkglehg
       61 krpcracvdf kswmrtqqkr dikfredcpq dreelgrntw aflhtlaayy pdmptpeqqq
      121 dmaqfihifs kfypceecae dirkridrsq pdtstrvsfs qwlcrlhnev nrklgkpdfd
      181 csrvderwrd gwkdgscd
//
LOCUS       NP_446274                 89 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A8 [Rattus norvegicus].
ACCESSION   NP_446274
VERSION     NP_446274.2
DBSOURCE    REFSEQ: accession NM_053822.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   An,N., Zhang,Y., Xie,J., Li,J., Lin,J., Li,Q., Wang,Y., Liu,Y. and
            Yang,Y.
  TITLE     Study on the involvement of microglial S100A8 in neuroinflammation
            and microglia activation during migraine attacks
  JOURNAL   Mol Cell Neurosci 130, 103957 (2024)
   PUBMED   39111720
  REMARK    GeneRIF: Study on the involvement of microglial S100A8 in
            neuroinflammation and microglia activation during migraine attacks.
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Chen,J., Chen,C., Wang,L., Feng,X., Chen,Y., Zhang,R., Cheng,Y.,
            Liu,Z. and Chen,Q.
  TITLE     Identification of S100A8/A9 involved in thromboangiitis obliterans
            development using tandem mass tags-labeled quantitative proteomics
            analysis
  JOURNAL   Cell Signal 120, 111199 (2024)
   PUBMED   38697446
  REMARK    GeneRIF: Identification of S100A8/A9 involved in thromboangiitis
            obliterans development using tandem mass tags-labeled quantitative
            proteomics analysis.
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Guo,S., Liu,Q., Tan,T. and Chen,X.
  TITLE     MiR-24 regulates obstructive pulmonary disease in rats via S100A8
  JOURNAL   Exp Lung Res 50 (1), 172-183 (2024)
   PUBMED   39390946
  REMARK    GeneRIF: MiR-24 regulates obstructive pulmonary disease in rats via
            S100A8.
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Wang,M., Zhao,M., Zheng,Z., Pan,W., Zhang,J., Yin,Z., Wei,C., Xu,Y.
            and Wan,J.
  TITLE     TRPA1 deficiency aggravates dilated cardiomyopathy by promoting
            S100A8 expression to induce M1 macrophage polarization in rats
  JOURNAL   FASEB J 37 (6), e22982 (2023)
   PUBMED   37219522
  REMARK    GeneRIF: TRPA1 deficiency aggravates dilated cardiomyopathy by
            promoting S100A8 expression to induce M1 macrophage polarization in
            rats.
            Erratum:[FASEB J. 2023 Aug;37(8):e23065. doi: 10.1096/fj.202301205.
            PMID: 37477922]
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Chen,Y., Dong,Y., Zhang,Z.L., Han,J., Chen,F.S., Tong,X.Y. and
            Ma,H.
  TITLE     Fra-1 induces apoptosis and neuroinflammation by targeting S100A8
            to modulate TLR4 pathways in spinal cord ischemia/reperfusion
            injury
  JOURNAL   Brain Pathol 33 (1), e13113 (2023)
   PUBMED   36634215
  REMARK    GeneRIF: Fra-1 induces apoptosis and neuroinflammation by targeting
            S100A8 to modulate TLR4 pathways in spinal cord
            ischemia/reperfusion injury.
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Signor,L., Tigani,B., Beckmann,N., Falchetto,R. and Stoeckli,M.
  TITLE     Two-dimensional electrophoresis protein profiling and
            identification in rat bronchoalveolar lavage fluid following
            allergen and endotoxin challenge
  JOURNAL   Proteomics 4 (7), 2101-2110 (2004)
   PUBMED   15221771
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Ryckman,C., Vandal,K., Rouleau,P., Talbot,M. and Tessier,P.A.
  TITLE     Proinflammatory activities of S100: proteins S100A8, S100A9, and
            S100A8/A9 induce neutrophil chemotaxis and adhesion
  JOURNAL   J Immunol 170 (6), 3233-3242 (2003)
   PUBMED   12626582
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Raftery,M.J. and Geczy,C.L.
  TITLE     Identification of posttranslational modifications and cDNA
            sequencing errors in the rat S100 proteins MRP8 and 14 using
            electrospray ionization mass spectrometry
  JOURNAL   Anal Biochem 258 (2), 285-292 (1998)
   PUBMED   9570842
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Imamichi,T., Uchida,I., Wahl,S.M. and McCartney-Francis,N.
  TITLE     Expression and cloning of migration inhibitory factor-related
            protein (MRP)8 and MRP14 in arthritis-susceptible rats
  JOURNAL   Biochem Biophys Res Commun 194 (2), 819-825 (1993)
   PUBMED   8343166
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Tao,Y.X.
  TITLE     [Embryonic-origin interferons and maternal recognition of
            pregnancy]
  JOURNAL   Sheng Li Ke Xue Jin Zhan 23 (3), 240-243 (1992)
   PUBMED   1299962
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Dec 23, 2009 this sequence version replaced NP_446274.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR460662.1, CB701295.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..89
                     /product="protein S100-A8"
                     /note="p8; MRP-8; calgranulin-A; migration inhibitory
                     factor-related protein 8; S100 calcium binding protein A8
                     (calgranulin A)"
                     /calculated_mol_wt=10107
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:9570842; propagated from
                     UniProtKB/Swiss-Prot (P50115.3)"
     Region          3..86
                     /region_name="calgranulins"
                     /note="Calgranulins: S-100 domain found in proteins
                     belonging to the Calgranulin subgroup of the S100 family
                     of EF-hand calcium-modulated proteins, including S100A8,
                     S100A9, and S100A12 . Note that the S-100 hierarchy, to
                     which this Calgranulin group belongs; cd05030"
                     /db_xref="CDD:240156"
     Site            order(3,9,11,17,41,43,68,76,78)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240156"
     Site            order(20,25,28,33,59,61,63,65,70)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240156"
     CDS             1..89
                     /gene="S100a8"
                     /gene_synonym="Mrp8"
                     /coded_by="NM_053822.2:24..293"
                     /db_xref="GeneID:116547"
                     /db_xref="RGD:620265"
ORIGIN      
        1 matelekals nvievyhnys gikgnhhaly rddfrkmvtt ecpqfvqnkn teslfkeldv
       61 nsdnainfee flvlvirvgv aahkdshke
//
LOCUS       NP_001257499             344 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform 8 [Rattus norvegicus].
ACCESSION   NP_001257499
VERSION     NP_001257499.1
DBSOURCE    REFSEQ: accession NM_001270570.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1 and BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (8) is alternatively spliced at
            the 3' end and uses an alternate acceptor splice site at the 3'
            terminal exon compared to variant 1. The latter causes a
            frame-shift, and a shorter isoform (8) containing 6 transmembrane
            domains and missing part of the third intracellular loop compared
            to isoform H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680417, SAMN06680421
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..344
                     /product="histamine H3 receptor isoform 8"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=37716
     Region          48..344
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          70..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          309..331
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..344
                     /gene="Hrh3"
                     /coded_by="NM_001270570.1:338..1372"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhrgskpsa ssaslekrmk mvsqsitqrf
      301 rlsrdkkvak slaiivsifg lcwapytllm iiraachgrc ipdy
//
LOCUS       NP_001159494             910 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial discoidin domain-containing receptor 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001159494
VERSION     NP_001159494.1
DBSOURCE    REFSEQ: accession NM_001166022.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Wu,R., Pan,S., Chen,Y., Nakano,Y., Li,M., Balog,S. and Tsukamoto,H.
  TITLE     Fate and functional roles of Prominin 1+ cells in liver injury and
            cancer
  JOURNAL   Sci Rep 10 (1), 19412 (2020)
   PUBMED   33173221
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Romayor,I., Badiola,I., Benedicto,A., Marquez,J., Herrero,A.,
            Arteta,B. and Olaso,E.
  TITLE     Silencing of sinusoidal DDR1 reduces murine liver metastasis by
            colon carcinoma
  JOURNAL   Sci Rep 10 (1), 18398 (2020)
   PUBMED   33110221
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Lino,M., Ngai,D., Liu,A., Mohabeer,A., Harper,C., Caruso,L.L.,
            Schroer,S.A., Fu,F., McKee,T., Giacca,A., Woo,M. and Bendeck,M.P.
  TITLE     Discoidin domain receptor 1-deletion ameliorates fibrosis and
            promotes adipose tissue beiging, brown fat activity, and increased
            metabolic rate in a mouse model of cardiometabolic disease
  JOURNAL   Mol Metab 39, 101006 (2020)
   PUBMED   32360427
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Zhong,X., Zhang,W. and Sun,T.
  TITLE     DDR1 promotes breast tumor growth by suppressing antitumor immunity
  JOURNAL   Oncol Rep 42 (6), 2844-2854 (2019)
   PUBMED   31578591
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Chiusa,M., Hu,W., Liao,H.J., Su,Y., Borza,C.M., de Caestecker,M.P.,
            Skrypnyk,N.I., Fogo,A.B., Pedchenko,V., Li,X., Zhang,M.Z.,
            Hudson,B.G., Basak,T., Vanacore,R.M., Zent,R. and Pozzi,A.
  TITLE     The Extracellular Matrix Receptor Discoidin Domain Receptor 1
            Regulates Collagen Transcription by Translocating to the Nucleus
  JOURNAL   J Am Soc Nephrol 30 (9), 1605-1624 (2019)
   PUBMED   31383731
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Vogel,W.F., Aszodi,A., Alves,F. and Pawson,T.
  TITLE     Discoidin domain receptor 1 tyrosine kinase has an essential role
            in mammary gland development
  JOURNAL   Mol Cell Biol 21 (8), 2906-2917 (2001)
   PUBMED   11283268
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Chin,G.S., Lee,S., Hsu,M., Liu,W., Kim,W.J., Levinson,H. and
            Longaker,M.T.
  TITLE     Discoidin domain receptors and their ligand, collagen, are
            temporally regulated in fetal rat fibroblasts in vitro
  JOURNAL   Plast Reconstr Surg 107 (3), 769-776 (2001)
   PUBMED   11304604
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Bhatt,R.S., Tomoda,T., Fang,Y. and Hatten,M.E.
  TITLE     Discoidin domain receptor 1 functions in axon extension of
            cerebellar granule neurons
  JOURNAL   Genes Dev 14 (17), 2216-2228 (2000)
   PUBMED   10970885
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Sanchez,M.P., Tapley,P., Saini,S.S., He,B., Pulido,D. and
            Barbacid,M.
  TITLE     Multiple tyrosine protein kinases in rat hippocampal neurons:
            isolation of Ptk-3, a receptor expressed in proliferative zones of
            the developing brain
  JOURNAL   Proc Natl Acad Sci U S A 91 (5), 1819-1823 (1994)
   PUBMED   8127887
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883047.1, CB613563.1 and BC166604.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..910
                     /product="epithelial discoidin domain-containing receptor
                     1 precursor"
                     /EC_number="2.7.10.1"
                     /note="discoidin domain receptor family, member 1;
                     epithelial discoidin domain-containing receptor 1; cell
                     adhesion kinase; tyrosine kinase DDR; tyrosine-protein
                     kinase CAK; protein-tyrosine kinase PTK-3; CD167
                     antigen-like family member A; discoidin receptor tyrosine
                     kinase; epithelial discoidin domain receptor 1;
                     protein-tyrosine kinase 3; neurotrophic tyrosine kinase
                     receptor type 4"
                     /calculated_mol_wt=99271
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
                     /calculated_mol_wt=1915
     mat_peptide     20..910
                     /product="Epithelial discoidin domain-containing receptor
                     1. /id=PRO_0000016745"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
                     /calculated_mol_wt=99271
     Region          58..185
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(75,106,114)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Region          193..368
                     /region_name="DS-like domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Site            212
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Region          467..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Region          478..481
                     /region_name="PPxY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63474.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Region          601..904
                     /region_name="PTKc_DDR1"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 1; cd05096"
                     /db_xref="CDD:133227"
     Site            order(613..617,621,650,652,698..701,704..705,763,767..768,
                     770,781,799..803,812,847)
                     /site_type="active"
                     /db_xref="CDD:133227"
     Site            order(613..614,616..617,621,650,652,698..701,704..705,
                     767..768,770,781)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133227"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            order(763,767,799..803,812,847)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133227"
     Site            780..805
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133227"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q08345; propagated from
                     UniProtKB/Swiss-Prot (Q63474.1)"
     CDS             1..910
                     /gene="Ddr1"
                     /gene_synonym="Cak; Drd1; PTK3D"
                     /coded_by="NM_001166022.1:102..2834"
                     /db_xref="GeneID:25678"
                     /db_xref="RGD:2252"
ORIGIN      
        1 mgtgtlssll lllllvtigd admkghfdpa kcryalgmqd rtipdsdisv ssswsdstaa
       61 rhsrlessdg dgawcpagpv fpkeeeylqv dlrrlhlval vgtqgrhagg lgkefsrsyr
      121 lrysrdgrrw mdwkdrwgqe visgnedpgg vvlkdlgppm varlvrfypr adrvmsvclr
      181 velygclwrd gllsytapvg qtmqlsemvy lndstydgyt agglqygglg qladgvvgld
      241 dfrqsqelrv wpgydyvgws nhsfpsgyve mefefdrlrs fqtmqvhcnn mhtlgarlpg
      301 gvecrfkrgp amawegepvr halggslgdp raraisvplg ghvgrflqcr flfagpwllf
      361 seisfisdvv ndssdtfppa pwwppgpppt nfsslelepr gqqpvakaeg sptailigcl
      421 vaiillllli ialmlwrlhw rrllskaerr vleeeltvhl svpgdtilin nrpgpreppp
      481 yqeprprgtp thsapcvpng salllsnpay rlllatyarp prgpgpptpa wakptntqac
      541 sgdymepekp gapllppppq nsvphyaead ivtlqgvtgg ntyavpalpp gavgdgpprv
      601 dfprsrlrfk eklgegqfge vhlcevedpq dlvtsdfpis vqkghpllva vkilrpdatk
      661 narndflkev kimsrlkdpn iirllgvcvq ddplcmitdy mengdlnqfl sahqlenkvt
      721 qglpgdresd qgptisypml lhvgaqiasg mrylatlnfv hrdlatrncl vgenftikia
      781 dfgmsrnlya gdyyrvqgra vlpirwmawe cilmgkftta sdvwafgvtl wevlmlcrsq
      841 pfgqltdeqv ienageffrd qgrqvylsrp pacpqtlyel mlrcwsrepe qrppfsqlhr
      901 fladdalntv
//
LOCUS       NP_001094130            1217 aa            linear   ROD 27-APR-2025
DEFINITION  rho family-interacting cell polarization regulator 1 [Rattus
            norvegicus].
ACCESSION   NP_001094130 XP_001075785 XP_214666
VERSION     NP_001094130.1
DBSOURCE    REFSEQ: accession NM_001100660.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Mardakheh,F.K., Self,A. and Marshall,C.J.
  TITLE     RHO binding to FAM65A regulates Golgi reorientation during cell
            migration
  JOURNAL   J Cell Sci 129 (24), 4466-4479 (2016)
   PUBMED   27807006
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Gao,K., Tang,W., Li,Y., Zhang,P., Wang,D., Yu,L., Wang,C. and Wu,D.
  TITLE     Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
            leading edges polarizes neutrophils
  JOURNAL   J Cell Sci 128 (5), 992-1000 (2015)
   PUBMED   25588844
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Patrakka,J., Xiao,Z., Nukui,M., Takemoto,M., He,L., Oddsson,A.,
            Perisic,L., Kaukinen,A., Szigyarto,C.A., Uhlen,M., Jalanko,H.,
            Betsholtz,C. and Tryggvason,K.
  TITLE     Expression and subcellular distribution of novel
            glomerulus-associated proteins dendrin, ehd3, sh2d4a, plekhh2, and
            2310066E14Rik
  JOURNAL   J Am Soc Nephrol 18 (3), 689-697 (2007)
   PUBMED   17251388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ147070.1, BF524907.1 and AY724537.1.
            
            On or before Aug 29, 2012 this sequence version replaced
            XP_001075785.3, XP_214666.6.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132264 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..1217
                     /product="rho family-interacting cell polarization
                     regulator 1"
                     /note="protein FAM65A; family with sequence similarity 65,
                     member A"
                     /calculated_mol_wt=131601
     Region          17..365
                     /region_name="PL48"
                     /note="Filopodia upregulated, FAM65; pfam15903"
                     /db_xref="CDD:464930"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Region          138..205
                     /region_name="HR1"
                     /note="Protein kinase C-related kinase homology region 1
                     (HR1) domain that binds Rho family small GTPases; cl00087"
                     /db_xref="CDD:469609"
     Site            order(140,143,146..147,150..151,153..154,157..158,
                     160..161,184..185,188,191..192,195)
                     /site_type="other"
                     /note="Rho binding site 1 [polypeptide binding]"
                     /db_xref="CDD:212026"
     Site            order(148..149,151..152,155..156,158..159,162..163,
                     179..180,182)
                     /site_type="other"
                     /note="putative Rho binding site 2 [polypeptide binding]"
                     /db_xref="CDD:212026"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZS17; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZS17; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Region          371..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Region          <497..>747
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          565..762
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Region          850..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FE6; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FE6; propagated from
                     UniProtKB/Swiss-Prot (Q4FZU8.2)"
     Region          1063..1184
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          1091..1121
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1127..1153
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1217
                     /gene="Ripor1"
                     /gene_synonym="Fam65a; RGD1307772"
                     /coded_by="NM_001100660.1:128..3781"
                     /db_xref="GeneID:291974"
                     /db_xref="RGD:1307772"
ORIGIN      
        1 mmslsvrpqr rllsarvsrs qsfagvlgsq ergprnftvf sppgpqrkpl vlsrvsrmfs
       61 vahpapkvpq perldlvyaa lkrgltayle vhqqeqeklq rqikeskrns rlgflydldk
      121 qvksierflr rlefhaskid elyeaycvqr rlrdgaynmv raystgspgs reardslaea
      181 trghreytes mcllenelea qlgefhlrmk glagfarlcv gdqyeicmky grqrwklrgr
      241 iessgkqvwd seetvflpll teflsikvte lkglanhvvv gsvscetkdl faalpqvvav
      301 dindlgtikl sleviwspfd kddqpsaast vnkastvtkr fstysqsppd tpslreqafy
      361 nmlrrqeele ngtawslsse ssddssspql sgtarysstp kplvqqpepl pvqvtfrrpe
      421 slssgsmdee ppltpalvng hapysrtlsh iseasvdaal teameavdlk cpapgpsplv
      481 ypesthvehv ssvppvadng rsatspalst agpaptfidp asstqldlvh katdsgssel
      541 psithtmass tysavspins vpgltsttvg sthkpmpspl tstgsipsvt dsiqtttspt
      601 httpspthtt vspthstpsp thttvspsna alspsnatps lshsttsptq katmsthtts
      661 avgpvqttts pisttvspsp svdtaiisss savpsvpgpe arpcshptst pytkadptaa
      721 ctsspslass gpkpltspap dsleqilksp ssspssivpe pqrselslal vaqapvpeat
      781 ggagdrrlee alrtlmaald dyrgqfpelq gleqevtrle sllmqrqglt rsrasslsit
      841 vehalesfsf lnddedednd spgdrptssp evvaeerlds snaqclstgc saldatlvqh
      901 lyhcsclllk lgtfgplrcq eawalerllr earvlqevce hsklwgnavt saqevvqfsa
      961 srpgfltfwd qcteglnpfl cpveqvlltf csqygarlsl rqpglaeavc vkfledalgq
     1021 klprrphsgp geqltifqfw syvevldsps meayvtetae evllvqnlns ddqavvlkal
     1081 rlapegrlrk dglralssll vhgnskvmaa vstqlrslsl gpvfrerall cfldqleded
     1141 vqtrvagcla lgcikapegi eplvylcqtd teavreaarq slqqcgeegq sahrqleesl
     1201 dalpclfgps smastaf
//
LOCUS       NP_001257891             655 aa            linear   ROD 27-APR-2025
DEFINITION  A-type voltage-gated potassium channel KCND3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001257891
VERSION     NP_001257891.1
DBSOURCE    REFSEQ: accession NM_001270962.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Kanda,H., Ling,J., Chang,Y.T., Erol,F., Viatchenko-Karpinski,V.,
            Yamada,A., Noguchi,K. and Gu,J.G.
  TITLE     Kv4.3 Channel Dysfunction Contributes to Trigeminal Neuropathic
            Pain Manifested with Orofacial Cold Hypersensitivity in Rats
  JOURNAL   J Neurosci 41 (10), 2091-2105 (2021)
   PUBMED   33472822
  REMARK    GeneRIF: Kv4.3 Channel Dysfunction Contributes to Trigeminal
            Neuropathic Pain Manifested with Orofacial Cold Hypersensitivity in
            Rats.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Tao,B., Liu,Z., Wei,F., Fan,S., Cui,S., Xia,H. and Xu,L.
  TITLE     Over-expression of Kv4.3 gene reverses cardiac remodeling and
            transient-outward K+ current (Ito) reduction via CaMKII inhibition
            in myocardial infarction
  JOURNAL   Biomed Pharmacother 132, 110896 (2020)
   PUBMED   33254430
  REMARK    GeneRIF: Over-expression of Kv4.3 gene reverses cardiac remodeling
            and transient-outward K(+) current (Ito) reduction via CaMKII
            inhibition in myocardial infarction.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Alday,A., Ahyayauch,H., Fernandez-Lopez,V., Echeazarra,L.,
            Urrutia,J., Casis,O. and Gallego,M.
  TITLE     CaMKII Modulates the Cardiac Transient Outward K+ Current through
            its Association with Kv4 Channels in Non-Caveolar Membrane Rafts
  JOURNAL   Cell Physiol Biochem 54 (1), 27-39 (2020)
   PUBMED   31935048
  REMARK    GeneRIF: Immunogold staining and electron microscopy of heart
            vibrosections was performed to localize Kv4.2/Kv4.3 and
            Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) proteins.
            Patch-Clamp recordings in control conditions and after lipid raft
            or caveolae disruption show that the CaMKII-Kv4 channel complex
            must associate in non-caveolar lipid rafts to be functional.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Wang,Y., Keskanokwong,T. and Cheng,J.
  TITLE     Kv4.3 expression abrogates and reverses norepinephrine-induced
            myocyte hypertrophy by CaMKII inhibition
  JOURNAL   J Mol Cell Cardiol 126, 77-85 (2019)
   PUBMED   30462989
  REMARK    GeneRIF: Kv4.3 reduction is an important mediator in cardiac
            hypertrophy development via excessive CaMKII activation.
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Viatchenko-Karpinski,V., Ling,J. and Gu,J.G.
  TITLE     Down-regulation of Kv4.3 channels and a-type K+ currents in V2
            trigeminal ganglion neurons of rats following oxaliplatin treatment
  JOURNAL   Mol Pain 14, 1744806917750995 (2018)
   PUBMED   29313436
  REMARK    GeneRIF: down-regulation of Kv4.3 channels mediating A-type K(+)
            (IA) currents currents in nociceptive V2 trigeminal neurons is an
            underlying mechanism of oxaliplatin-induced orofacial neuropathic
            pain.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Ohya,S., Tanaka,M., Oku,T., Asai,Y., Watanabe,M., Giles,W.R. and
            Imaizumi,Y.
  TITLE     Molecular cloning and tissue distribution of an alternatively
            spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the
            rat
  JOURNAL   FEBS Lett 420 (1), 47-53 (1997)
   PUBMED   9450548
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Takimoto,K., Li,D., Hershman,K.M., Li,P., Jackson,E.K. and
            Levitan,E.S.
  TITLE     Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit
            mRNAs in ventricles of renovascular hypertensive rats
  JOURNAL   Circ Res 81 (4), 533-539 (1997)
   PUBMED   9314834
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Tsaur,M.L., Chou,C.C., Shih,Y.H. and Wang,H.L.
  TITLE     Cloning, expression and CNS distribution of Kv4.3, an A-type K+
            channel alpha subunit
  JOURNAL   FEBS Lett 400 (2), 215-220 (1997)
   PUBMED   9001401
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Dixon,J.E., Shi,W., Wang,H.S., McDonald,C., Yu,H., Wymore,R.S.,
            Cohen,I.S. and McKinnon,D.
  TITLE     Role of the Kv4.3 K+ channel in ventricular muscle. A molecular
            correlate for the transient outward current
  JOURNAL   Circ Res 79 (4), 659-668 (1996)
   PUBMED   8831489
  REMARK    Erratum:[Circ Res 1997 Jan;80(1):147]
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Serodio,P., Vega-Saenz de Miera,E. and Rudy,B.
  TITLE     Cloning of a novel component of A-type K+ channels operating at
            subthreshold potentials with unique expression in heart and brain
  JOURNAL   J Neurophysiol 75 (5), 2174-2179 (1996)
   PUBMED   8734615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Transcript Variant: This variant (1, also known as Kv4.3L and
            Kv4.3c) represents the longest transcript and encodes the longest
            isoform (1).
            
            Sequence Note: The RefSeq transcript was derived from the reference
            genome assembly. The genomic coordinates were determined from
            transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.8964.1,
                                           SRR26643298.12808.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..655
                     /product="A-type voltage-gated potassium channel KCND3
                     isoform 1"
                     /note="potassium voltage gated channel, Shal-related
                     family, member 3; voltage-gated potassium channel subunit
                     Kv4.3; potassium channel, voltage-gated Shal-related
                     subfamily D, member 3; potassium voltage-gated channel,
                     Shal-related subfamily, member 3; A-type voltage-gated
                     potassium channel KCND3"
                     /calculated_mol_wt=73355
     Region          6..143
                     /region_name="BTB_POZ_KCND3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily D member 3 (KCND3);
                     cd18419"
                     /db_xref="CDD:349726"
     Region          6..21
                     /region_name="Interaction with KCNIP1.
                     /evidence=ECO:0000250|UniProtKB:Q9UK17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            order(7..19,21..22,26..27,29,31,34,36..37,39,54)
                     /site_type="other"
                     /note="beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Site            order(41,45,47..54,57,83,85..87,89,92,96,99..100,102,104,
                     107..110,112..113,116,131..132)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Region          70..78
                     /region_name="Interaction with KCNIP1.
                     /evidence=ECO:0000250|UniProtKB:Q9UK17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62897.2)"
     Site            183..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Region          186..412
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            224..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            254..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            284..306
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            319..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Region          367..372
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            378..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V1; propagated from
                     UniProtKB/Swiss-Prot (Q62897.2)"
     Region          468..563
                     /region_name="DUF3399"
                     /note="Domain of unknown function (DUF3399); pfam11879"
                     /db_xref="CDD:463381"
     Region          470..487
                     /region_name="Interaction with KCNIP1 and KCNIP2.
                     /evidence=ECO:0000250|UniProtKB:Q9UK17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Region          474..489
                     /region_name="Mediates dendritic targeting.
                     /evidence=ECO:0000250|UniProtKB:Q63881"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Region          523..565
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2D.
                     /evidence=ECO:0000269|PubMed:15456698; propagated from
                     UniProtKB/Swiss-Prot (Q62897.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0V1; propagated from
                     UniProtKB/Swiss-Prot (Q62897.2)"
     Region          616..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62897.2)"
     CDS             1..655
                     /gene="Kcnd3"
                     /gene_synonym="Kv4.3"
                     /coded_by="NM_001270962.1:93..2060"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65195"
                     /db_xref="RGD:68394"
ORIGIN      
        1 maagvaawlp faraaaigwm pvancpmpla padknkrqde livlnvsgrr fqtwrttler
       61 ypdtllgste kefffnedtk eyffdrdpev frcvlnfyrt gklhypryec isayddelaf
      121 ygilpeiigd ccyeeykdrk renaerlmdd nesennqesm pslsfrqtmw rafenphtst
      181 lalvfyyvtg ffiavsvitn vvetvpcgtv pgskelpcge rysvaffcld tacvmiftve
      241 yllrlfaaps ryrfirsvms iidvvaimpy yiglvmtnne dvsgafvtlr vfrvfrifkf
      301 srhsqglril gytlkscase lgfllfsltm aiiifatvmf yaekgssask ftsipasfwy
      361 tivtmttlgy gdmvpktiag kifgsicsls gvlvialpvp vivsnfsriy hqnqradkrr
      421 aqkkarlari rvaktgssna ylhskrngll nealeltgtp eeehmgktts liesqhhhll
      481 hclekttgls ylvddpllsv rtstiknhef ideqmfeqnc messmqnyps trspslsshs
      541 gltttccsrr skktthlpns nlpatrlrsm qelstihiqg seqpslttsr sslnlkaddg
      601 lrpncktsqi ttaiisiptp paltpegesr pppaspgpnt nipsitsnvv kvsal
//
LOCUS       NP_001008320             396 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein transferase MAEA [Rattus norvegicus].
ACCESSION   NP_001008320 XP_216694
VERSION     NP_001008320.2
DBSOURCE    REFSEQ: accession NM_001008319.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Lampert,F., Stafa,D., Goga,A., Soste,M.V., Gilberto,S., Olieric,N.,
            Picotti,P., Stoffel,M. and Peter,M.
  TITLE     The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell
            proliferation and targets the transcription factor Hbp1 for
            degradation
  JOURNAL   Elife 7, e35528 (2018)
   PUBMED   29911972
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Francis,O., Han,F. and Adams,J.C.
  TITLE     Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in
            eukaryotic cells and dominated by homologous components, the
            muskelin/RanBPM/CTLH complex
  JOURNAL   PLoS One 8 (10), e75217 (2013)
   PUBMED   24143168
  REMARK    Erratum:[PLoS One. 2013 Nov 8;8(11). doi:
            10.1371/annotation/1e464689-3c86-4399-b229-1e00d65593a5. PMID:
            29161723]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Soni,S., Bala,S., Gwynn,B., Sahr,K.E., Peters,L.L. and Hanspal,M.
  TITLE     Absence of erythroblast macrophage protein (Emp) leads to failure
            of erythroblast nuclear extrusion
  JOURNAL   J Biol Chem 281 (29), 20181-20189 (2006)
   PUBMED   16707498
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Bala,S., Kumar,A., Soni,S., Sinha,S. and Hanspal,M.
  TITLE     Emp is a component of the nuclear matrix of mammalian cells and
            undergoes dynamic rearrangements during cell division
  JOURNAL   Biochem Biophys Res Commun 342 (4), 1040-1048 (2006)
   PUBMED   16510120
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Hanspal,M., Smockova,Y. and Uong,Q.
  TITLE     Molecular identification and functional characterization of a novel
            protein that mediates the attachment of erythroblasts to
            macrophages
  JOURNAL   Blood 92 (8), 2940-2950 (1998)
   PUBMED   9763581
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV109439.1 and BC085770.1.
            
            On Sep 30, 2011 this sequence version replaced NP_001008320.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085770.1, SRR8487226.189215.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..396
                     /product="E3 ubiquitin-protein transferase MAEA"
                     /EC_number="2.3.2.27"
                     /calculated_mol_wt=45205
     Region          1..124
                     /region_name="Extracellular and involved in cell to cell
                     contact. /evidence=ECO:0000250|UniProtKB:Q7L5Y9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5RKJ1.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7L5Y9; propagated from
                     UniProtKB/Swiss-Prot (Q5RKJ1.2)"
     Region          120..153
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          160..301
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Site            314
                     /site_type="other"
                     /note="Essential for ubiquitin ligase activity.
                     /evidence=ECO:0000250|UniProtKB:P40492; propagated from
                     UniProtKB/Swiss-Prot (Q5RKJ1.2)"
     Region          336..385
                     /region_name="RING-Ubox_Emp"
                     /note="U-box domain, a modified RING finger, found in
                     erythroblast macrophage protein (Emp) and similar
                     proteins; cd16659"
                     /db_xref="CDD:438321"
     CDS             1..396
                     /gene="Maea"
                     /coded_by="NM_001008319.2:34..1224"
                     /db_xref="GeneID:298982"
                     /db_xref="RGD:1309877"
ORIGIN      
        1 mavqesaaql smtlkvqeyp tlkvpyetln krfraaqkni dretshvtmv vaelektlss
       61 cpavdsvvsl ldgvveklsv lkrkavesiq aedesaklck rriehlkehs sdqpaaasmw
      121 krkrmdrmmv ehllrcgyyn tavklarqsg iedlvniemf ltakeveesl erretatcla
      181 wchdnksrlr kmksclefsl riqefielvr qnkrldavrh arkhfsqaeg sqldevrqvm
      241 gmlafppdth ispykdlldp arwrmliqqf rydnyrlhql gnssvftltl qaglsaiktp
      301 qcykedgssk spdcpvcsrs lnklaqplpm ahcansrlvc kisgdvmnen nppmmlpngy
      361 vygynsllsi rqddkvvcpr tkevfhfsqa ekvyim
//
LOCUS       NP_570842                383 aa            linear   ROD 27-APR-2025
DEFINITION  paralemmin-1 [Rattus norvegicus].
ACCESSION   NP_570842
VERSION     NP_570842.1
DBSOURCE    REFSEQ: accession NM_130829.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Arstikaitis,P., Gauthier-Campbell,C., Carolina Gutierrez
            Herrera,R., Huang,K., Levinson,J.N., Murphy,T.H., Kilimann,M.W.,
            Sala,C., Colicos,M.A. and El-Husseini,A.
  TITLE     Paralemmin-1, a modulator of filopodia induction is required for
            spine maturation
  JOURNAL   Mol Biol Cell 19 (5), 2026-2038 (2008)
   PUBMED   18287537
  REMARK    GeneRIF: This study identifies a key role for paralemmin-1 in spine
            maturation through modulation of filopodia induction.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Kutzleb,C., Petrasch-Parwez,E. and Kilimann,M.W.
  TITLE     Cellular and subcellular localization of paralemmin-1, a protein
            involved in cell shape control, in the rat brain, adrenal gland and
            kidney
  JOURNAL   Histochem Cell Biol 127 (1), 13-30 (2007)
   PUBMED   16847661
  REMARK    GeneRIF: analysis of the cellular and subcellular localization of
            paralemmin-1 in the rat tissues is consistent with a role for
            paralemmin-1 in the formation and stabilization of plasma membrane
            elaborations, in neurons as well as in other cell types
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Basile,M., Lin,R., Kabbani,N., Karpa,K., Kilimann,M., Simpson,I.
            and Kester,M.
  TITLE     Paralemmin interacts with D3 dopamine receptors: implications for
            membrane localization and cAMP signaling
  JOURNAL   Arch Biochem Biophys 446 (1), 60-68 (2006)
   PUBMED   16386234
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Gauthier-Campbell,C., Bredt,D.S., Murphy,T.H. and
            El-Husseini,Ael.-D.
  TITLE     Regulation of dendritic branching and filopodia formation in
            hippocampal neurons by specific acylated protein motifs
  JOURNAL   Mol Biol Cell 15 (5), 2205-2217 (2004)
   PUBMED   14978216
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Hu,B., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and Kilimann,M.W.
  TITLE     The paralemmin protein family: identification of paralemmin-2, an
            isoform differentially spliced to AKAP2/AKAP-KL, and of
            palmdelphin, a more distant cytosolic relative
  JOURNAL   Biochem Biophys Res Commun 285 (5), 1369-1376 (2001)
   PUBMED   11478809
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Kutzleb,C., Sanders,G., Yamamoto,R., Wang,X., Lichte,B.,
            Petrasch-Parwez,E. and Kilimann,M.W.
  TITLE     Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in
            neurons and implicated in plasma membrane dynamics and cell process
            formation
  JOURNAL   J Cell Biol 143 (3), 795-813 (1998)
   PUBMED   9813098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC072525.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072525.1, AB058889.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..383
                     /product="paralemmin-1"
                     /calculated_mol_wt=41796
     mat_peptide     1..380
                     /product="Paralemmin-1. /id=PRO_0000411054"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920Q0.1)"
                     /calculated_mol_wt=41610
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O75781; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Region          19..348
                     /region_name="Paralemmin"
                     /note="pfam03285"
                     /db_xref="CDD:460875"
     Region          51..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75781; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75781; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Region          242..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Region          333..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0P4; propagated from
                     UniProtKB/Swiss-Prot (Q920Q0.1)"
     Site            380
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q920Q0.1)"
     CDS             1..383
                     /gene="Palm"
                     /coded_by="NM_130829.2:133..1284"
                     /db_xref="GeneID:170673"
                     /db_xref="RGD:620341"
ORIGIN      
        1 mevlatdtvs qqerlqaiae krrkqaeies krrqleddrr qlqylkskal rerwllegtp
       61 ssasegdedm rkqmqedeqk arsleesitr lekeidvlef gesapaapke nsaapspirp
      121 hstspakeeq ksetmvnaqq tplgtpkenr kstpvrspgg stmmkaamys veitvekdkv
      181 tgetrvlsst tllprdplpq gvkvyedetk vvhavdglse ngiqplssse vdelihkade
      241 vtlseagstt gpaeprglae dvtrttpsrr eitgveaqpg eatsgppgiq pgqeppvtmv
      301 fmgyqnvede aetkkvlglq dtikaelvvi edsvtprepa plngsaaelp atkeenqtgp
      361 tttpsdtqdl dmkkprcrcc svm
//
LOCUS       NP_001007600             140 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL14 [Rattus norvegicus].
ACCESSION   NP_001007600 XP_213448
VERSION     NP_001007600.1
DBSOURCE    REFSEQ: accession NM_001007599.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Voorhees,R.M., Fernandez,I.S., Scheres,S.H. and Hegde,R.S.
  TITLE     Structure of the mammalian ribosome-Sec61 complex to 3.4 A
            resolution
  JOURNAL   Cell 157 (7), 1632-1643 (2014)
   PUBMED   24930395
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Plafker,S.M. and Macara,I.G.
  TITLE     Ribosomal protein L12 uses a distinct nuclear import pathway
            mediated by importin 11
  JOURNAL   Mol Cell Biol 22 (4), 1266-1275 (2002)
   PUBMED   11809816
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Chan,Y.L., Paz,V. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L23
  JOURNAL   Biochem Biophys Res Commun 178 (3), 1153-1159 (1991)
   PUBMED   1840488
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Hultin,T.
  TITLE     Selective high-efficiency cross-linking of mammalian ribosomal
            proteins with cleavable thiol-directed heterobifunctional reagents:
            identification and binding directions of major protein complexes
  JOURNAL   Biochim Biophys Acta 872 (3), 226-235 (1986)
   PUBMED   3730400
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Uchiumi,T., Terao,K. and Ogata,K.
  TITLE     Identification of neighboring protein pairs in rat liver 60S
            ribosomal subunits cross-linked with dimethyl suberimidate or
            dimethyl 3,3'-dithiobispropionimidate
  JOURNAL   J Biochem 88 (4), 1033-1044 (1980)
   PUBMED   7451403
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC058500.1.
            
            On Nov 29, 2004 this sequence version replaced XP_213448.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058500.1, FQ221693.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132292, SAMD00132301
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..140
                     /product="large ribosomal subunit protein uL14"
                     /note="60S ribosomal protein L23"
                     /calculated_mol_wt=14734
     Region          2..139
                     /region_name="PTZ00054"
                     /note="60S ribosomal protein L23; Provisional"
                     /db_xref="CDD:185418"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62829; propagated from
                     UniProtKB/Swiss-Prot (P62832.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62829; propagated from
                     UniProtKB/Swiss-Prot (P62832.1)"
     CDS             1..140
                     /gene="Rpl23"
                     /gene_synonym="RL23a"
                     /coded_by="NM_001007599.2:22..444"
                     /db_xref="GeneID:29282"
                     /db_xref="RGD:62067"
ORIGIN      
        1 mskrgrggss gakfrislgl pvgavincad ntgaknlyii svkgikgrln rlpaagvgdm
       61 vmatvkkgkp elrkkvhpav virqrksyrr kdgvflyfed nagvivnnkg emkgsaitgp
      121 vakecadlwp riasnagsia
//
LOCUS       NP_476493                620 aa            linear   ROD 27-APR-2025
DEFINITION  kelch-like ECH-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_476493
VERSION     NP_476493.2
DBSOURCE    REFSEQ: accession NM_057152.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Jiang,G., Shi,L.F., Li,L.J., Duan,X.J. and Zheng,Z.F.
  TITLE     Activation of the p62-Keap1-Nrf2 pathway improves pulmonary
            arterial hypertension in MCT-induced rats by inhibiting autophagy
  JOURNAL   FASEB J 38 (3), e23452 (2024)
   PUBMED   38308640
  REMARK    GeneRIF: Activation of the p62-Keap1-Nrf2 pathway improves
            pulmonary arterial hypertension in MCT-induced rats by inhibiting
            autophagy.
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Geng,W., Yan,S., Li,X., Liu,Q., Zhang,X., Gu,X., Tian,X. and
            Jiang,Y.
  TITLE     miR-432-5p Inhibits the Ferroptosis in Cardiomyocytes Induced by
            Hypoxia/Reoxygenation via Activating Nrf2/SLC7A11 Axis by Degrading
            Keap1
  JOURNAL   Anal Cell Pathol (Amst) 2023, 1293200 (2023)
   PUBMED   37822721
  REMARK    GeneRIF: miR-432-5p Inhibits the Ferroptosis in Cardiomyocytes
            Induced by Hypoxia/Reoxygenation via Activating Nrf2/SLC7A11 Axis
            by Degrading Keap1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Washimkar,K.R., Tomar,M.S., Ishteyaque,S., Kumar,A., Shrivastava,A.
            and Mugale,M.N.
  TITLE     Benzo[a]pyrene treatment modulates Nrf2/Keap1 axis and changes the
            metabolic profile in rat lung cancer
  JOURNAL   Chem Biol Interact 373, 110373 (2023)
   PUBMED   36736873
  REMARK    GeneRIF: Benzo[a]pyrene treatment modulates Nrf2/Keap1 axis and
            changes the metabolic profile in rat lung cancer.
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Xu,F., Zhang,J., Zhou,X. and Hao,H.
  TITLE     Lipoxin A4 and its analog attenuate high fat diet-induced
            atherosclerosis via Keap1/Nrf2 pathway
  JOURNAL   Exp Cell Res 412 (1), 113025 (2022)
   PUBMED   35026282
  REMARK    GeneRIF: Lipoxin A4 and its analog attenuate high fat diet-induced
            atherosclerosis via Keap1/Nrf2 pathway.
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Hu,X., Mu,L., Zhu,L., Chang,X., Nie,L., Wang,L. and Li,G.
  TITLE     Lycium barbarum polysaccharides attenuate cardiovascular oxidative
            stress injury by enhancing the Keap1/Nrf2 signaling pathway in
            exhaustive exercise rats
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278476
  REMARK    GeneRIF: Lycium barbarum polysaccharides attenuate cardiovascular
            oxidative stress injury by enhancing the Keap1/Nrf2 signaling
            pathway in exhaustive exercise rats.
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Velichkova,M. and Hasson,T.
  TITLE     Keap1 in adhesion complexes
  JOURNAL   Cell Motil Cytoskeleton 56 (2), 109-119 (2003)
   PUBMED   14506708
REFERENCE   7  (residues 1 to 620)
  AUTHORS   McMahon,M., Itoh,K., Yamamoto,M. and Hayes,J.D.
  TITLE     Keap1-dependent proteasomal degradation of transcription factor
            Nrf2 contributes to the negative regulation of antioxidant response
            element-driven gene expression
  JOURNAL   J Biol Chem 278 (24), 21592-21600 (2003)
   PUBMED   12682069
  REMARK    GeneRIF: Keap1 negatively regulates Nrf2 by both enhancing its rate
            of proteasomal degradation and altering its subcellular
            distribution
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Velichkova,M., Guttman,J., Warren,C., Eng,L., Kline,K., Vogl,A.W.
            and Hasson,T.
  TITLE     A human homologue of Drosophila kelch associates with myosin-VIIa
            in specialized adhesion junctions
  JOURNAL   Cell Motil Cytoskeleton 51 (3), 147-164 (2002)
   PUBMED   11921171
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Dhakshinamoorthy,S. and Jaiswal,A.K.
  TITLE     Functional characterization and role of INrf2 in antioxidant
            response element-mediated expression and antioxidant induction of
            NAD(P)H:quinone oxidoreductase1 gene
  JOURNAL   Oncogene 20 (29), 3906-3917 (2001)
   PUBMED   11439354
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Chu,C.C. and Paul,W.E.
  TITLE     Expressed genes in interleukin-4 treated B cells identified by cDNA
            representational difference analysis
  JOURNAL   Mol Immunol 35 (8), 487-502 (1998)
   PUBMED   9798653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 21, 2012 this sequence version replaced NP_476493.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212383.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..620
                     /product="kelch-like ECH-associated protein 1"
                     /note="cytosolic inhibitor of Nrf2"
                     /calculated_mol_wt=68928
     Region          56..180
                     /region_name="BTB_POZ_KLHL19_KEAP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     ECH-associated protein 1 (KEAP1); cd18248"
                     /db_xref="CDD:349557"
     Region          95..595
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Site            order(106,109..110,115..117,125..126,157,161..162)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349557"
     Site            order(129,131..132,147..148,150..151,154)
                     /site_type="other"
                     /note="modulator binding site [chemical binding]"
                     /db_xref="CDD:349557"
     Site            151
                     /site_type="other"
                     /note="Sensor for electrophilic agents.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X8; propagated from
                     UniProtKB/Swiss-Prot (P57790.1)"
     Site            253
                     /site_type="other"
                     /note="Sensor for electrophilic agents.
                     /evidence=ECO:0000250|UniProtKB:Q14145; propagated from
                     UniProtKB/Swiss-Prot (P57790.1)"
     Site            269
                     /site_type="other"
                     /note="Sensor for electrophilic agents.
                     /evidence=ECO:0000250|UniProtKB:Q14145; propagated from
                     UniProtKB/Swiss-Prot (P57790.1)"
     Site            284
                     /site_type="other"
                     /note="Sensor for electrophilic agents.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X8; propagated from
                     UniProtKB/Swiss-Prot (P57790.1)"
     Region          323..368
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     Region          358..405
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          369..419
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     Region          409..452
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          420..466
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     Site            430
                     /site_type="other"
                     /note="Sensor for electrophilic agents.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X8; propagated from
                     UniProtKB/Swiss-Prot (P57790.1)"
     Region          456..499
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          467..513
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     Region          503..547
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          515..560
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     Region          550..593
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          561..607
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P57790.1)"
     CDS             1..620
                     /gene="Keap1"
                     /gene_synonym="Inrf2"
                     /coded_by="NM_057152.2:324..2186"
                     /db_xref="GeneID:117519"
                     /db_xref="RGD:621619"
ORIGIN      
        1 mqpepkpsga prssqflplw skcpegagda vmyastecka evtpsqdgnr tfsytledht
       61 kqafgimnel rlsqqlcdvt lqvkyedipa aqfmahkvvl assspvfkam ftnglreqgm
      121 evvsiegihp kvmerliefa ytasisvgek cvlhvmngav myqidsvvra csdflvqqld
      181 psnaigianf aeqigctelh qrareyiymh fgeeeffnls hcqlatlisr ddlnvrcese
      241 vfhacidwvk ydcpqrrfyv qallravrch altprflqtq lqkceilqad arckdylvqi
      301 fqeltlhkpt qavpcrapkv grliytaggy frqslsylea ynpsngswlr ladlqvprsg
      361 lagcvvggll yavggrnnsp dgntdssald cynpmtnqws pcasmsvprn rigvgvidgh
      421 iyavggshgc ihhssverye pdrdewhlva pmltrrigvg vavlnrllya vggfdgtnrl
      481 nsaecyyper newrmitpmn tirsgagvcv lhsciyaagg ydgqdqlnsv erydvetetw
      541 tfvasmkhrr salgiavhqg riyvlggydg htfldsvecy dpdtdtwsev trltsgrsgv
      601 gvavtmepcr kqidqqnctc
//
LOCUS       NP_001019994             740 aa            linear   ROD 27-APR-2025
DEFINITION  ALEX isoform Alex [Rattus norvegicus].
ACCESSION   NP_001019994 XP_575296
VERSION     NP_001019994.4
DBSOURCE    REFSEQ: accession NM_001024823.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Taneera,J., Dhaiban,S., Mohammed,A.K., Mukhopadhyay,D.,
            Aljaibeji,H., Sulaiman,N., Fadista,J. and Salehi,A.
  TITLE     GNAS gene is an important regulator of insulin secretory capacity
            in pancreatic beta-cells
  JOURNAL   Gene 715, 144028 (2019)
   PUBMED   31374326
  REMARK    GeneRIF: GNAS is a crucial gene for the beta-cell insulin secretory
            capacity.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Masyuk,T.V., Masyuk,A.I., Lorenzo Pisarello,M., Howard,B.N.,
            Huang,B.Q., Lee,P.Y., Fung,X., Sergienko,E., Ardecky,R.J.,
            Chung,T.D.Y., Pinkerton,A.B. and LaRusso,N.F.
  TITLE     TGR5 contributes to hepatic cystogenesis in rodents with polycystic
            liver diseases through cyclic adenosine monophosphate/Galphas
            signaling
  JOURNAL   Hepatology 66 (4), 1197-1218 (2017)
   PUBMED   28543567
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Xue,N., Wei,C., Zhang,L., Liu,H., Wang,X. and Wang,L.
  TITLE     The Characteristics of Hepatic Gsalpha-cAMP Axis in HSHF Diet-Fed
            Obese Insulin Resistance Rats and Genetic Diabetic Mice
  JOURNAL   Biol Pharm Bull 40 (6), 774-781 (2017)
   PUBMED   28260721
  REMARK    GeneRIF: Our data revealed a positive correlation between hepatic
            Gsalpha-cAMP signal axis and fasting blood glucose (FBG) in slight
            insulin resistance stage of HIgh Sugar High Fat-diet rats and
            diabetic db/db mice. The current finding thus suggested hepatic
            Gsalpha-cAMP signal axis plays a central role in regulating of FBG
            during the developing and development of T2DM.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Erb,S.J., Schappi,J.M. and Rasenick,M.M.
  TITLE     Antidepressants Accumulate in Lipid Rafts Independent of Monoamine
            Transporters to Modulate Redistribution of the G Protein, Galphas
  JOURNAL   J Biol Chem 291 (38), 19725-19733 (2016)
   PUBMED   27432886
  REMARK    GeneRIF: Translocation of Galphas, which shows delayed onset after
            chronic antidepressant treatment of rats or of C6 glioma cells,
            tracks with the delayed onset of therapeutic action of
            antidepressants
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Sarma,T., Koutsouris,A., Yu,J.Z., Krbanjevic,A., Hope,T.J. and
            Rasenick,M.M.
  TITLE     Activation of microtubule dynamics increases neuronal growth via
            the nerve growth factor (NGF)- and Galphas-mediated signaling
            pathways
  JOURNAL   J Biol Chem 290 (16), 10045-10056 (2015)
   PUBMED   25691569
  REMARK    GeneRIF: Activated Galpha s translocates from the plasma membrane
            and, through interaction with tubulin/microtubules in the cytosol,
            is important for neurite formation, development, and outgrowth.
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Eaton,S.A., Hough,T., Fischer-Colbrie,R. and Peters,J.
  TITLE     Maternal inheritance of the Gnas cluster mutation Ex1A-T affects
            size, implicating NESP55 in growth
  JOURNAL   Mamm Genome 24 (7-8), 276-285 (2013)
   PUBMED   23839232
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Swaroop,A., Agarwal,N., Gruen,J.R., Bick,D. and Weissman,S.M.
  TITLE     Differential expression of novel Gs alpha signal transduction
            protein cDNA species
  JOURNAL   Nucleic Acids Res 19 (17), 4725-4729 (1991)
   PUBMED   1716359
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Weinstein,L.S., Gejman,P.V., Friedman,E., Kadowaki,T.,
            Collins,R.M., Gershon,E.S. and Spiegel,A.M.
  TITLE     Mutations of the Gs alpha-subunit gene in Albright hereditary
            osteodystrophy detected by denaturing gradient gel electrophoresis
  JOURNAL   Proc Natl Acad Sci U S A 87 (21), 8287-8290 (1990)
   PUBMED   2122458
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Golf: an olfactory neuron specific-G protein involved in odorant
            signal transduction
  JOURNAL   Science 244 (4906), 790-795 (1989)
   PUBMED   2499043
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Votan-Bonamour,B., Plauchu,H. and Guibaud,P.
  TITLE     [Ectopic crystalline lens linked to its cause (homocyst inuria) by
            a simple geneological enquiry]
  JOURNAL   J Genet Hum 24 Suppl, 103-106 (1976)
   PUBMED   799727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000003.1, X84047.1 and
            BC168156.1.
            
            On Jul 15, 2009 this sequence version replaced NP_001019994.3.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            In addition, one of the transcripts contains a second overlapping
            ORF, which encodes a structurally unrelated protein - Alex.
            Alternative splicing of downstream exons is also observed, which
            results in different forms of the stimulatory G-protein alpha
            subunit, a key element of the classical signal transduction pathway
            linking receptor-ligand interactions with the activation of
            adenylyl cyclase and a variety of cellular reponses. Multiple
            transcript variants have been found for this gene. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (1, also known as GNASXL) is
            paternally expressed. It includes an alternate 5' exon, as compared
            to variant 3. This variant includes two overlapping open reading
            frames encoding XLas and Alex, respectively. This RefSeq represents
            Alex, also known as alexX, which has no similarity to other
            isoforms encoded by this gene. It interacts with XLas, and their
            interaction is essential for G-protein signaling in neuroendocrine
            cells.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X84047.1, SRR26360176.1619175.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 23839232
            NMD candidate  :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..740
                     /product="ALEX isoform Alex"
                     /note="GNAS complex locus XLas-like; guanine
                     nucleotide-binding protein G-s, alpha subunit; guanine
                     nucleotide binding protein alpha s; adenylate
                     cyclase-stimulating G alpha protein; GNAS (guanine
                     nucleotide binding protein, alpha stimulating) complex
                     locus; SCG6 (secretogranin VI)"
                     /calculated_mol_wt=80581
     Region          <399..691
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..740
                     /gene="Gnas"
                     /gene_synonym="ALEX; G-alpha-8; Gnas1; Gnpas; Nesp55;
                     SCG6"
                     /coded_by="NM_001024823.4:170..2392"
                     /note="isoform Alex is encoded by transcript variant 1"
                     /db_xref="GeneID:24896"
                     /db_xref="RGD:2716"
ORIGIN      
        1 mspsptrltv rsvdplktpn ltsrapvrps rkskwaetta hlqrkpchsr snspaweisg
       61 ppwssldhlg phqaskpstq rfwspgpplv htqawepiap hqkklchlss mslprktvas
      121 lpcksqtlrq gvrkhgspel fprspgtsdl ktlasektta lhlknlchfs smeknsgaia
      181 hpqdsresrh ksalaassrq srsrvrsasl pprtrlpsgs rapladhsar lsdlltshtt
      241 fpqwrspdpc lrlaepplgs tttplsiwta pqsqvmarps ksrepqlras tqrdphlsdk
      301 qprqetalsa aplqrrqksp psseekdppp nlkqcissql llrspertlp kpirtqlhtq
      361 ffrsvlrkse esqpcppifr lllkmraqms gqnqtegqpq pplpspktte nqppppppsq
      421 ppsqplsqpp sqppsqppsq lprqsltpkp slppgqsptp krspqprqpl prrrslppgq
      481 ppsplrsplp glsllpepiq ppglslepqr cqpllgqppl eqpmqvlwsg epghsrllqp
      541 lghpslpaqq lppeqpllpa qslpagqplp pqagpildpp arrsrlltrl lrgllrgrvp
      601 gltntnvaea aagmrlrpas arssppamsr kkgplaassg fcgetaalas pgatqsgatr
      661 satsspepse aasvylsvpd hdpsapgrpr ilwkrganrc akkpwrcesr saqirnaass
      721 stsnwrrrrw ttcvhtaccf
//
LOCUS       NP_001026983             289 aa            linear   ROD 27-APR-2025
DEFINITION  growth hormone-regulated TBC protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001026983 XP_341464
VERSION     NP_001026983.1
DBSOURCE    REFSEQ: accession NM_001031813.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB315310.1 and BC097985.1.
            
            On Aug 19, 2005 this sequence version replaced XP_341464.2.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            CDS, as compared to variant 1. The resulting isoform (2) lacks an
            internal segment, as compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097985.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..289
                     /product="growth hormone-regulated TBC protein 1 isoform
                     2"
                     /note="GH regulated TBC protein 1"
                     /calculated_mol_wt=32798
     Region          67..231
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; pfam00566"
                     /db_xref="CDD:459855"
     CDS             1..289
                     /gene="Grtp1"
                     /gene_synonym="LRRGT00052"
                     /coded_by="NM_001031813.2:78..947"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361180"
                     /db_xref="RGD:1309210"
ORIGIN      
        1 mdpaeraqaa rarvpridpy gferpedfdy aayeeffsty lviltkraik wskllkgsgg
       61 vrksvtdlnr tfpdnvmfrk tadpclqktl ynvllayglh nqdvgycqgm nfiagylili
      121 tkneeesfwl ldalvgrilp dyyspamlgl ktdqevlael vrmklpavaa lmdghgvlwt
      181 llvsrwficl fvdilpvetv lriwdclfne gskiifrval tlikqhqefi leassvpdic
      241 dkfkqitkgd fvtechtfmq kifsepgsls matitrlres craalqaqs
//
LOCUS       NP_037076                387 aa            linear   ROD 27-APR-2025
DEFINITION  D(4) dopamine receptor [Rattus norvegicus].
ACCESSION   NP_037076
VERSION     NP_037076.2
DBSOURCE    REFSEQ: accession NM_012944.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Zhang,R., Dang,W., Zhang,J., He,R., Li,G., Zhang,L., Wang,Z.,
            Zong,H., Liu,N. and Jia,W.
  TITLE     Methylation quantitative locus rs3758653 in the DRD4 gene is
            associated with duration from first heroin exposure to addiction
  JOURNAL   Brain Res 1775, 147746 (2022)
   PUBMED   34864042
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Chmielowiec,K., Chmielowiec,J., Masiak,J., Czekaj,M., Krawczyk,P.,
            Soroka,E., Smiarowska,M., Musial,W., Pawlowski,T. and Grzywacz,A.
  TITLE     DRD4 Exon 3 Gene Polymorphisms in Patients Diagnosed with
            Polysubstance Use Disorder and Co-Occurrence of a Depressive
            Episode
  JOURNAL   Genes (Basel) 12 (11), 1834 (2021)
   PUBMED   34828440
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Sonia,J.A., Kabir,T., Islam,M.M.T. and Kabir,Y.
  TITLE     Catechol-O-methyltransferase and dopamine receptor D4 gene
            variants: Possible association with substance abuse in Bangladeshi
            male
  JOURNAL   PLoS One 16 (2), e0246462 (2021)
   PUBMED   33544778
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Hui,Y., Du,C., Xu,T., Zhang,Q., Tan,H. and Liu,J.
  TITLE     Dopamine D4 receptors in the lateral habenula regulate
            depression-related behaviors via a pre-synaptic mechanism in
            experimental Parkinson's disease
  JOURNAL   Neurochem Int 140, 104844 (2020)
   PUBMED   32891683
  REMARK    GeneRIF: Dopamine D4 receptors in the lateral habenula regulate
            depression-related behaviors via a pre-synaptic mechanism in
            experimental Parkinson's disease.
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Uysal,M.A., Sever,U., Nursal,A.F. and PehlIvan,S.
  CONSRTM   Yedikule Smoking Cessation Study Group
  TITLE     Dopamine D4 Receptor Gene Exon III VNTR Variant Influences Smoking
            Status in Turkish Population
  JOURNAL   Noro Psikiyatr Ars 56 (4), 248-252 (2019)
   PUBMED   31903031
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Nothen,M.M., Cichon,S., Hemmer,S., Hebebrand,J., Remschmidt,H.,
            Lehmkuhl,G., Poustka,F., Schmidt,M., Catalano,M., Fimmers,R. et al.
  TITLE     Human dopamine D4 receptor gene: frequent occurrence of a null
            allele and observation of homozygosity
  JOURNAL   Hum Mol Genet 3 (12), 2207-2212 (1994)
   PUBMED   7881421
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Chio,C.L., Drong,R.F., Riley,D.T., Gill,G.S., Slightom,J.L. and
            Huff,R.M.
  TITLE     D4 dopamine receptor-mediated signaling events determined in
            transfected Chinese hamster ovary cells
  JOURNAL   J Biol Chem 269 (16), 11813-11819 (1994)
   PUBMED   7512953
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Van Tol,H.H., Wu,C.M., Guan,H.C., Ohara,K., Bunzow,J.R.,
            Civelli,O., Kennedy,J., Seeman,P., Niznik,H.B. and Jovanovic,V.
  TITLE     Multiple dopamine D4 receptor variants in the human population
  JOURNAL   Nature 358 (6382), 149-152 (1992)
   PUBMED   1319557
REFERENCE   9  (residues 1 to 387)
  AUTHORS   O'Malley,K.L., Harmon,S., Tang,L. and Todd,R.D.
  TITLE     The rat dopamine D4 receptor: sequence, gene structure, and
            demonstration of expression in the cardiovascular system
  JOURNAL   New Biol 4 (2), 137-146 (1992)
   PUBMED   1554689
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Van Tol,H.H., Bunzow,J.R., Guan,H.C., Sunahara,R.K., Seeman,P.,
            Niznik,H.B. and Civelli,O.
  TITLE     Cloning of the gene for a human dopamine D4 receptor with high
            affinity for the antipsychotic clozapine
  JOURNAL   Nature 350 (6319), 610-614 (1991)
   PUBMED   1840645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 28, 2015 this sequence version replaced NP_037076.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M84009.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..387
                     /product="D(4) dopamine receptor"
                     /note="dopamine D4 receptor; d(2C) dopamine receptor;
                     dopamine receptor 4"
                     /calculated_mol_wt=41064
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30729.2)"
     Site            37..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          44..379
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          69..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            70..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          106..128
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            107..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Site            147..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          149..165
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          185..208
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            187..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          224..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          313..335
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            315..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     Region          347..372
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            347..369
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30729.2)"
     CDS             1..387
                     /gene="Drd4"
                     /gene_synonym="D4RA"
                     /coded_by="NM_012944.2:131..1294"
                     /db_xref="GeneID:25432"
                     /db_xref="RGD:2522"
ORIGIN      
        1 mgnssatgdg gllagrgpes lgtgtglgga gagaaalvgg vlligmvlag nslvcvsvas
       61 erilqtptny fivslaaadl llavlvlplf vyseggvwll sprlcdtlma mdvmlctasi
      121 fnlcaisvdr fvavtvplry nqqgqcqlll iaatwllsaa vaapvvcgln dvpgrdptvc
      181 cledrdyvvy ssicsfflpc plmlllywat frglrrweaa rhtklhsrap rrpsgpgppv
      241 sdptqgplfs dcpppspslr tsptvssrpe sdlsqspcsp gcllpdaala qppapssrrk
      301 rgakitgrer kamrvlpvvv gaflmcwtpf fvvhitralc pacfvsprlv savtwlgyvn
      361 salnpiiyti fnaefrsvfr ktlrlrc
//
LOCUS       NP_073203                761 aa            linear   ROD 27-APR-2025
DEFINITION  transferrin receptor protein 1 [Rattus norvegicus].
ACCESSION   NP_073203 XP_001072774 XP_341000
VERSION     NP_073203.1
DBSOURCE    REFSEQ: accession NM_022712.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Xing,P., Zhou,M., Sun,J., Wang,D., Huang,W. and An,P.
  TITLE     NAT10-mediated ac4C acetylation of TFRC promotes sepsis-induced
            pulmonary injury through regulating ferroptosis
  JOURNAL   Mol Med 30 (1), 140 (2024)
   PUBMED   39251905
  REMARK    GeneRIF: NAT10-mediated ac[4]C acetylation of TFRC promotes
            sepsis-induced pulmonary injury through regulating ferroptosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Ma,H., Huang,Y., Tian,W., Liu,J., Yan,X., Ma,L. and Lai,J.
  TITLE     Endothelial transferrin receptor 1 contributes to thrombogenesis
            through cascade ferroptosis
  JOURNAL   Redox Biol 70, 103041 (2024)
   PUBMED   38241836
  REMARK    GeneRIF: Endothelial transferrin receptor 1 contributes to
            thrombogenesis through cascade ferroptosis.
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Chen,L., Ma,Y., Ma,X., Liu,L., Jv,X., Li,A., Shen,Q., Jia,W.,
            Qu,L., Shi,L. and Xie,J.
  TITLE     TFEB regulates cellular labile iron and prevents ferroptosis in a
            TfR1-dependent manner
  JOURNAL   Free Radic Biol Med 208, 445-457 (2023)
   PUBMED   37683766
  REMARK    GeneRIF: TFEB regulates cellular labile iron and prevents
            ferroptosis in a TfR1-dependent manner.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Zhang,L., Wang,X., Che,W., Zhou,S. and Feng,Y.
  TITLE     METTL3 silenced inhibited the ferroptosis development via
            regulating the TFRC levels in the Intracerebral hemorrhage
            progression
  JOURNAL   Brain Res 1811, 148373 (2023)
   PUBMED   37105375
  REMARK    GeneRIF: METTL3 silenced inhibited the ferroptosis development via
            regulating the TFRC levels in the Intracerebral hemorrhage
            progression.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Wei,X.B., Jiang,W.Q., Zeng,J.H., Huang,L.Q., Ding,H.G., Jing,Y.W.,
            Han,Y.L., Li,Y.C. and Chen,S.L.
  TITLE     Exosome-Derived lncRNA NEAT1 Exacerbates Sepsis-Associated
            Encephalopathy by Promoting Ferroptosis Through Regulating
            miR-9-5p/TFRC and GOT1 Axis
  JOURNAL   Mol Neurobiol 59 (3), 1954-1969 (2022)
   PUBMED   35038133
  REMARK    GeneRIF: Exosome-Derived lncRNA NEAT1 Exacerbates Sepsis-Associated
            Encephalopathy by Promoting Ferroptosis Through Regulating
            miR-9-5p/TFRC and GOT1 Axis.
            Erratum:[Mol Neurobiol. 2022 Aug;59(8):5252. doi:
            10.1007/s12035-022-02931-2. PMID: 35727437]
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kennard,M.L., Richardson,D.R., Gabathuler,R., Ponka,P. and
            Jefferies,W.A.
  TITLE     A novel iron uptake mechanism mediated by GPI-anchored human p97
  JOURNAL   EMBO J 14 (17), 4178-4186 (1995)
   PUBMED   7556058
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Baynes,R.D., Shih,Y.J., Hudson,B.G. and Cook,J.D.
  TITLE     Characterization of transferrin receptor released by K562
            erythroleukemia cells
  JOURNAL   Proc Soc Exp Biol Med 197 (4), 416-423 (1991)
   PUBMED   1871153
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Mechtersheimer,G., Kruger,K.H., Born,I.A. and Moller,P.
  TITLE     Antigenic profile of mammary fibroadenoma and cystosarcoma
            phyllodes. A study using antibodies to estrogen- and progesterone
            receptors and to a panel of cell surface molecules
  JOURNAL   Pathol Res Pract 186 (4), 427-438 (1990)
   PUBMED   2174150
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Roberts,K.P. and Griswold,M.D.
  TITLE     Characterization of rat transferrin receptor cDNA: the regulation
            of transferrin receptor mRNA in testes and in Sertoli cells in
            culture
  JOURNAL   Mol Endocrinol 4 (4), 531-542 (1990)
   PUBMED   2126342
REFERENCE   10 (residues 1 to 761)
  AUTHORS   FitzGerald,D.J., Bjorn,M.J., Ferris,R.J., Winkelhake,J.L.,
            Frankel,A.E., Hamilton,T.C., Ozols,R.F., Willingham,M.C. and
            Pastan,I.
  TITLE     Antitumor activity of an immunotoxin in a nude mouse model of human
            ovarian cancer
  JOURNAL   Cancer Res 47 (5), 1407-1410 (1987)
   PUBMED   3493065
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB762571.1, CB809947.1, BP500872.1, FM033330.1, CB700894.1,
            CV117527.1, CV111368.1, CV117299.1, FM123390.1, CO398424.1,
            AI029320.1 and CA509549.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_341000.3, XP_001072774.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760396
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..761
                     /product="transferrin receptor protein 1"
                     /note="TR; tfR; tfR1"
                     /calculated_mol_wt=85746
     Region          1..67
                     /region_name="Mediates interaction with SH3BP4.
                     /evidence=ECO:0000250|UniProtKB:P02786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02786; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62351; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Region          20..23
                     /region_name="Endocytosis signal.
                     /evidence=ECO:0000250|UniProtKB:P02786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P02786; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02786; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02786; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Region          58..61
                     /region_name="Stop-transfer sequence.
                     /evidence=ECO:0000250|UniProtKB:P02786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Region          201..378
                     /region_name="PA_TfR"
                     /note="Protease-associated domain containing proteins like
                     transferrin receptor (TfR). This group contains various PA
                     domain-containing proteins similar to human TfR1 and TfR2.
                     TfR1 and TfR2 are type II membrane proteins, belonging to
                     the peptidase M28 family; cd02128"
                     /db_xref="CDD:239043"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            order(288,296..299,301,305..308,311,313..315)
                     /site_type="other"
                     /note="PA/protease-like domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239043"
     Site            order(306,312)
                     /site_type="other"
                     /note="PA/helical domain interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            order(311,314)
                     /site_type="other"
                     /note="Ca2+ binding [ion binding]"
                     /db_xref="CDD:239043"
     Site            order(315,317,321..322)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239043"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Region          386..611
                     /region_name="M28_TfR"
                     /note="M28 Zn-peptidase Transferrin Receptor family;
                     cd09848"
                     /db_xref="CDD:349946"
     Site            order(393,395,398,400..401,403,448,450,467,470..478)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349946"
     Region          570..761
                     /region_name="Ligand-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Region          638..751
                     /region_name="TFR_dimer"
                     /note="Transferrin receptor-like dimerization domain;
                     pfam04253"
                     /db_xref="CDD:461238"
     Region          647..649
                     /region_name="Cell attachment site, required for binding
                     to transferrin. /evidence=ECO:0000250|UniProtKB:P02786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99376.2)"
     Site            723
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     Site            728
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99376.2)"
     CDS             1..761
                     /gene="Tfrc"
                     /gene_synonym="Trfr"
                     /coded_by="NM_022712.1:134..2419"
                     /db_xref="GeneID:64678"
                     /db_xref="RGD:70488"
ORIGIN      
        1 mmdqarsafs nlfggeplsy trfslarqvd gdnshvemkl aadeeenads nmkasvrkpk
       61 rfngrlcfat iavvifflig fmigylgyck rveqkeecvr laeaeeadks endeteyvpk
      121 ssrlfwadlk tllseklnsi eftdiikqls qntytpreag sqkdenlayy ienlfhdfkf
      181 skvwrdehyv kiqvknsvsq nlvtinsgsn idpveapegy vafskagevt gklvhanfgt
      241 kkdfeelnys vngslvivra gkitfaekva naqsfnaigv liymdrntfp vveadlqffg
      301 hahlgtgdpy tpgfpsfnht qfppsqssgl psipvqtisr aaaeklfknm egncppswni
      361 dsscklelsq nqnvkltvnn vlketrilni fgvikgyeep dryivvgaqr dawgpgvaks
      421 svgtglllkl aqvfsdmisk dgfrpsrsii faswtagdyg avgatewleg ylsslhlkaf
      481 tyinldkvvl gtsnfkvsas pllytlmgki mqdvkhpidg kylyrdsnwi skieelsldn
      541 aafpflaysg ipavsfcfce dedypylgtk ldtyeiliqk vpqlnqmvrt aaevagqfii
      601 klthdieltl dyemynskll sfmkdlnqfk adikdmglsl qwlysargdy fratsrlttd
      661 fhnaektnrf vmreindrim kveyhflspy vsprespfrh ifwgsgshtl salvenlrlr
      721 qknitafnet lfrnqlalat wtiqgvanal sgdiwnidne f
//
LOCUS       NP_001257510             467 aa            linear   ROD 27-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform d precursor [Rattus norvegicus].
ACCESSION   NP_001257510
VERSION     NP_001257510.1
DBSOURCE    REFSEQ: accession NM_001270581.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1, D14908.1 and CR475040.1.
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons and differs in the 5' UTR compared to variant (1). The
            resulting isoform (d) has the same N- and C-termini but is shorter
            compared to isoform a. Variants 4 and 5 both encode the same
            isoform (d).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D14908.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..467
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform d precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=51258
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          149..416
                     /region_name="7tmB1_PACAP-R1"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type 1 receptor, member of the class B family of
                     seven-transmembrane G protein-coupled receptors; cd15987"
                     /db_xref="CDD:320653"
     Region          151..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320653"
     Site            order(156,160,202,205..206,209,226,233,304..305,307,309,
                     365,368,381,385)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320653"
     Region          185..207
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320653"
     Region          226..253
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320653"
     Region          265..285
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320653"
     Region          301..330
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320653"
     Region          346..373
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320653"
     Region          378..403
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320653"
     CDS             1..467
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_001270581.1:450..1853"
                     /note="isoform d precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiylrl arstlllipl
      361 fgihytvfaf spenvskrer lvfelglgsf qgfvvavlyc flngevqaei krkwrswkvn
      421 ryftmdfkhr hpslassgvn ggtqlsilsk sssqlrmssl padnlat
//
LOCUS       NP_001291216             692 aa            linear   ROD 27-APR-2025
DEFINITION  disks large-associated protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001291216 XP_008765653
VERSION     NP_001291216.1
DBSOURCE    REFSEQ: accession NM_001304287.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Rademacher,N., Schmerl,B., Lardong,J.A., Wahl,M.C. and
            Shoichet,S.A.
  TITLE     MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1
            cell adhesion molecules to core components of the postsynaptic
            density
  JOURNAL   Sci Rep 6, 35283 (2016)
   PUBMED   27756895
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Tao-Cheng,J.H., Yang,Y., Reese,T.S. and Dosemeci,A.
  TITLE     Differential distribution of Shank and GKAP at the postsynaptic
            density
  JOURNAL   PLoS One 10 (3), e0118750 (2015)
   PUBMED   25775468
  REMARK    GeneRIF: Upon depolarization with high K+, neither the intensity
            nor distribution of label for GKAP changed, but labeling intensity
            for Shank at the postsynaptic density increased to ~150% of
            controls.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Tong,J., Yang,H. and Im,Y.J.
  TITLE     Crystallization and preliminary X-ray crystallographic analysis of
            the C-terminal domain of guanylate kinase-associated protein from
            Rattus norvegicus
  JOURNAL   Acta Crystallogr F Struct Biol Commun 70 (Pt 7), 949-954 (2014)
   PUBMED   25005096
  REMARK    GeneRIF: The C-terminal helical domain of GKAP from Rattus
            norvegicus was purified and crystallized as a fusion protein.
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Shin,S.M., Zhang,N., Hansen,J., Gerges,N.Z., Pak,D.T., Sheng,M. and
            Lee,S.H.
  TITLE     GKAP orchestrates activity-dependent postsynaptic protein
            remodeling and homeostatic scaling
  JOURNAL   Nat Neurosci 15 (12), 1655-1666 (2012)
   PUBMED   23143515
  REMARK    GeneRIF: Activity-dependent turnover of postsynnaptic density
            proteins orchestrated by GKAP is critical for homeostatic
            plasticity.
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Chua,J.J., Schob,C., Rehbein,M., Gkogkas,C.G., Richter,D. and
            Kindler,S.
  TITLE     Synthesis of two SAPAP3 isoforms from a single mRNA is mediated via
            alternative translational initiation
  JOURNAL   Sci Rep 2, 484 (2012)
   PUBMED   22761992
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Hirao,K., Hata,Y., Ide,N., Takeuchi,M., Irie,M., Yao,I.,
            Deguchi,M., Toyoda,A., Sudhof,T.C. and Takai,Y.
  TITLE     A novel multiple PDZ domain-containing molecule interacting with
            N-methyl-D-aspartate receptors and neuronal cell adhesion proteins
  JOURNAL   J Biol Chem 273 (33), 21105-21110 (1998)
   PUBMED   9694864
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Kawashima,N., Takamiya,K., Sun,J., Kitabatake,A. and Sobue,K.
  TITLE     Differential expression of isoforms of PSD-95 binding protein
            (GKAP/SAPAP1) during rat brain development
  JOURNAL   FEBS Lett 418 (3), 301-304 (1997)
   PUBMED   9428732
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Satoh,K., Yanai,H., Senda,T., Kohu,K., Nakamura,T., Okumura,N.,
            Matsumine,A., Kobayashi,S., Toyoshima,K. and Akiyama,T.
  TITLE     DAP-1, a novel protein that interacts with the guanylate
            kinase-like domains of hDLG and PSD-95
  JOURNAL   Genes Cells 2 (6), 415-424 (1997)
   PUBMED   9286858
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Takeuchi,M., Hata,Y., Hirao,K., Toyoda,A., Irie,M. and Takai,Y.
  TITLE     SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
            postsynaptic density
  JOURNAL   J Biol Chem 272 (18), 11943-11951 (1997)
   PUBMED   9115257
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Kim,E., Naisbitt,S., Hsueh,Y.P., Rao,A., Rothschild,A., Craig,A.M.
            and Sheng,M.
  TITLE     GKAP, a novel synaptic protein that interacts with the guanylate
            kinase-like domain of the PSD-95/SAP90 family of channel clustering
            molecules
  JOURNAL   J Cell Biol 136 (3), 669-678 (1997)
   PUBMED   9024696
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jan 17, 2015 this sequence version replaced XP_008765653.1.
            
            Transcript Variant: This variant (2) lacks three 5' exons, contains
            an alternate 5' terminal exon, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript from the reference strain was
            available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212368.1, AB003594.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..692
                     /product="disks large-associated protein 1 isoform 2"
                     /note="disks large-associated protein 1;
                     PSD-95/SAP90-binding protein 1; SAP90/PSD-95-associated
                     protein 1; PSD-95 binding protein; guanylate
                     kinase-associated protein; discs large homolog associated
                     protein 1"
                     /calculated_mol_wt=76847
     Region          360..692
                     /region_name="GKAP"
                     /note="Guanylate-kinase-associated protein (GKAP) protein;
                     pfam03359"
                     /db_xref="CDD:460897"
     CDS             1..692
                     /gene="Dlgap1"
                     /gene_synonym="DAP-1; Gkap; GKAP/SAPAP1; rGKAP; SAPAP1"
                     /coded_by="NM_001304287.1:143..2221"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65040"
                     /db_xref="RGD:620223"
ORIGIN      
        1 midlfkaewv ssvcvqvsrn grtdqvpqde wtgytprgkd deipcrrmrs gsyikamgde
       61 dsgdsdtspk pspkvaarre sylkatqpsl telttlkisn ehspklqirs hsylravsev
      121 sinrsldsld paglltspkf rsrnesymra mstisqvsem evngqfesvc esvfselesq
      181 avealdlpmp gcfrmrshsy vraiekgcsq ddecvslrss spprttttvr tiqsstgvik
      241 lssavevssc ittykktppp vpprtttkpf isitaqsste saqdaymdgq gqrgdmisqs
      301 glsnstesld smkaltaaie aanaqihgpa sqhmgsnaaa vtttttiatv ttedrkkdfk
      361 knrclsigiq vddaeesekm aesktsskfq svgvqveeek cfrrftrsns vttavqadld
      421 fhdnlensle siednscpgp marqfsrdas tstvsiqgsg nhyhacaadd dfdtdfdpsi
      481 lpppdpwids itedpleavq rsvchrdghw flkllqaerd rmegwckqme reerennlpe
      541 dilgkirtav gsaqllmaqk fyqfrelcee nlnpnahprp tsqdlagfwd mlqlsienis
      601 mkfdelhqlk annwkqmdpl dkkerrappp vpkkpakgpa plirersles sqrqearkrl
      661 maakraasvr qnsatesaes ieiyipeaqt rl
//
LOCUS       NP_072141                657 aa            linear   ROD 27-APR-2025
DEFINITION  cationic amino acid transporter 2 isoform a [Rattus norvegicus].
ACCESSION   NP_072141
VERSION     NP_072141.2
DBSOURCE    REFSEQ: accession NM_022619.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Hultstrom,M., Helle,F. and Iversen,B.M.
  TITLE     AT(1) receptor activation regulates the mRNA expression of CAT1,
            CAT2, arginase-1, and DDAH2 in preglomerular vessels from
            angiotensin II hypertensive rats
  JOURNAL   Am J Physiol Renal Physiol 297 (1), F163-F168 (2009)
   PUBMED   19386725
  REMARK    GeneRIF: CAT1, CAT2, DDAH2, and arginase-1 expression in renal
            resistance vessels is regulated through the AT(1) receptor.
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Huang,T.Y., Tsai,P.S. and Huang,C.J.
  TITLE     HO-1 overexpression attenuates endotoxin effects on CAT-2 isozymes
            expression
  JOURNAL   J Surg Res 148 (2), 172-180 (2008)
   PUBMED   18028947
  REMARK    GeneRIF: HO-1 overexpression significantly attenuates
            endotoxin-induced increases in nitric oxide and l-arginine
            transport, as well as the expression of iNOS and CAT-2 isozymes in
            septic rats.
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Schwartz,I.F., Chernichovsky,T., Hagin,D., Ingbir,M., Reshef,R.,
            Chernin,G., Levo,Y. and Schwartz,D.
  TITLE     Differential regulation of L-arginine transporters (cationic amino
            acid transporter-1 and -2) by peroxynitrite in rat mesangial cells
  JOURNAL   Nephrol Dial Transplant 21 (12), 3409-3414 (2006)
   PUBMED   16998217
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Rothenberg,M.E., Doepker,M.P., Lewkowich,I.P., Chiaramonte,M.G.,
            Stringer,K.F., Finkelman,F.D., MacLeod,C.L., Ellies,L.G. and
            Zimmermann,N.
  TITLE     Cationic amino acid transporter 2 regulates inflammatory
            homeostasis in the lung
  JOURNAL   Proc Natl Acad Sci U S A 103 (40), 14895-14900 (2006)
   PUBMED   17003120
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Yeramian,A., Martin,L., Arpa,L., Bertran,J., Soler,C., McLeod,C.,
            Modolell,M., Palacin,M., Lloberas,J. and Celada,A.
  TITLE     Macrophages require distinct arginine catabolism and transport
            systems for proliferation and for activation
  JOURNAL   Eur J Immunol 36 (6), 1516-1526 (2006)
   PUBMED   16703566
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Stevens,B.R., Kakuda,D.K., Yu,K., Waters,M., Vo,C.B. and
            Raizada,M.K.
  TITLE     Induced nitric oxide synthesis is dependent on induced
            alternatively spliced CAT-2 encoding L-arginine transport in brain
            astrocytes
  JOURNAL   J Biol Chem 271 (39), 24017-24022 (1996)
   PUBMED   8798637
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Gill,D.J., Low,B.C. and Grigor,M.R.
  TITLE     Interleukin-1 beta and tumor necrosis factor-alpha stimulate the
            cat-2 gene of the L-arginine transporter in cultured vascular
            smooth muscle cells
  JOURNAL   J Biol Chem 271 (19), 11280-11283 (1996)
   PUBMED   8626679
REFERENCE   8  (residues 1 to 657)
  AUTHORS   Kavanaugh,M.P., Wang,H., Zhang,Z., Zhang,W., Wu,Y.N., Dechant,E.,
            North,R.A. and Kabat,D.
  TITLE     Control of cationic amino acid transport and retroviral receptor
            functions in a membrane protein family
  JOURNAL   J Biol Chem 269 (22), 15445-15450 (1994)
   PUBMED   8195186
REFERENCE   9  (residues 1 to 657)
  AUTHORS   Kudo,H., Hirayoshi,K., Kitagawa,Y., Imamura,S. and Nagata,K.
  TITLE     Two collagen-binding proteins, osteonectin and HSP47, are
            coordinately induced in transformed keratinocytes by heat and other
            stresses
  JOURNAL   Exp Cell Res 212 (2), 219-224 (1994)
   PUBMED   8187816
REFERENCE   10 (residues 1 to 657)
  AUTHORS   Closs,E.I., Albritton,L.M., Kim,J.W. and Cunningham,J.M.
  TITLE     Identification of a low affinity, high capacity transporter of
            cationic amino acids in mouse liver
  JOURNAL   J Biol Chem 268 (10), 7538-7544 (1993)
   PUBMED   8385111
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF245001.1.
            
            On Sep 4, 2008 this sequence version replaced NP_072141.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter protein (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF245001.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..657
                     /product="cationic amino acid transporter 2 isoform a"
                     /note="low affinity cationic amino acid transporter 2;
                     CAT-2; cationic amino acid transporter-2A; solute carrier
                     family 7 (cationic amino acid transporter, y+ system),
                     member 2"
                     /calculated_mol_wt=71563
     Region          5..607
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52569; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            164..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            340..360
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52569; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            490..510
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            524..544
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            555..575
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            582..602
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5D5N9.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B5D5N9.1)"
     CDS             1..657
                     /gene="Slc7a2"
                     /gene_synonym="Cat2; Cat2a; Cat2b"
                     /coded_by="NM_022619.3:180..2153"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:64554"
                     /db_xref="RGD:68387"
ORIGIN      
        1 mipcravltf trclirrkiv tldsledskl crclttmdli algvgstlga gvyvlageva
       61 kadsgpsivv sfliaalasv maglcyaefg arvpktgsay lytyvtvgel wafitgwnli
      121 lsyvigtssv arawsgtfde llnkqigqff ktyfkmnytg laeypdffav clvlllagll
      181 sfgvkesawv nkfftainil vllfvmvagf vkgnvanwki seeflknisa sareppseng
      241 tsiygaggfm pygftgtlag aatcfyafvg fdciattgee vrnpqkaipi givtsllvcf
      301 mayfgvsaal tlmmpyylld eksplpvafe yvgwgpakyv vaagslcals tsllgsmfpl
      361 prilfamard gllfrflarv skrqspvaat mtagvisavm aflfdlkalv dmmsigtlma
      421 yslvaacvli lryqpglcye qpkytpekdi lesctnatsk sesqvtmlqg qgfslrtlfn
      481 psalptrqsa slvsflvgfl afliaglsil ttygvqaiar leawslalla lflvlcaavi
      541 ltiwrqpqnq qkvafmvpfl pflpafsilv niylmvqlsa dtwvrfsiwm vlgfliyfay
      601 girhslegnp rdeeededvc pdnvnaaaee ksamqandhh qrnlslpfil hektsec
//
LOCUS       NP_001257505             206 aa            linear   ROD 27-APR-2025
DEFINITION  synaptosomal-associated protein 25 isoform a [Rattus norvegicus].
ACCESSION   NP_001257505
VERSION     NP_001257505.1
DBSOURCE    REFSEQ: accession NM_001270576.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Hu,A., Lan,H., Yao,Z. and Kong,X.
  TITLE     Carbohydrate response element-binding protein (ChREBP) mediates
            decreased SNAP25 expression in islets from diabetic Goto-Kakizaki
            (GK) rats
  JOURNAL   FEBS Open Bio 14 (11), 1864-1872 (2024)
   PUBMED   39300600
  REMARK    GeneRIF: Carbohydrate response element-binding protein (ChREBP)
            mediates decreased SNAP25 expression in islets from diabetic
            Goto-Kakizaki (GK) rats.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Polishchuk,A., Cilleros-Mane,V., Balanya-Segura,M., Just-Borras,L.,
            Fornies-Marine,A., Silvera-Simon,C., Tomas,M., Jami El Hirchi,M.,
            Hurtado,E., Tomas,J. and Lanuza,M.A.
  TITLE     BDNF/TrkB signalling, in cooperation with muscarinic signalling,
            retrogradely regulates PKA pathway to phosphorylate SNAP-25 and
            Synapsin-1 at the neuromuscular junction
  JOURNAL   Cell Commun Signal 22 (1), 371 (2024)
   PUBMED   39044222
  REMARK    GeneRIF: BDNF/TrkB signalling, in cooperation with muscarinic
            signalling, retrogradely regulates PKA pathway to phosphorylate
            SNAP-25 and Synapsin-1 at the neuromuscular junction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kong,X., Lin,C., Yang,C., Wang,X., Li,B., Yan,D., Yang,Y., Hu,A.,
            Chen,Y., Xu,X. and Ma,X.
  TITLE     GLP-1 signaling-regulated SNAP25 is involved in improved insulin
            secretion in diabetic GK rats after Roux-en-Y gastric bypass
            surgery
  JOURNAL   Mol Biol Rep 51 (1), 123 (2024)
   PUBMED   38227062
  REMARK    GeneRIF: GLP-1 signaling-regulated SNAP25 is involved in improved
            insulin secretion in diabetic GK rats after Roux-en-Y gastric
            bypass surgery.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Si,W., Sun,B., Luo,J., Li,Z., Dou,Y. and Wang,Q.
  TITLE     Snap25 attenuates neuronal injury via reducing ferroptosis in acute
            ischemic stroke
  JOURNAL   Exp Neurol 367, 114476 (2023)
   PUBMED   37393984
  REMARK    GeneRIF: Snap25 attenuates neuronal injury via reducing ferroptosis
            in acute ischemic stroke.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chilcote,T.J., Galli,T., Mundigl,O., Edelmann,L., McPherson,P.S.,
            Takei,K. and De Camilli,P.
  TITLE     Cellubrevin and synaptobrevins: similar subcellular localization
            and biochemical properties in PC12 cells
  JOURNAL   J Cell Biol 129 (1), 219-231 (1995)
   PUBMED   7698987
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Garcia,E.P., McPherson,P.S., Chilcote,T.J., Takei,K. and De
            Camilli,P.
  TITLE     rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the
            axon, but are not in a stable complex with syntaxin
  JOURNAL   J Cell Biol 129 (1), 105-120 (1995)
   PUBMED   7698978
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Hess,D.T., Slater,T.M., Wilson,M.C. and Skene,J.H.
  TITLE     The 25 kDa synaptosomal-associated protein SNAP-25 is the major
            methionine-rich polypeptide in rapid axonal transport and a major
            substrate for palmitoylation in adult CNS
  JOURNAL   J Neurosci 12 (12), 4634-4641 (1992)
   PUBMED   1281490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FM033263.1 and BC087699.1.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein. It is essential for regulated exocytosis in neuronal
            cells. Alternative transcript variants encoding two different
            protein isoforms have been described for this gene. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) has an alternate 5' UTR exon,
            compared to variant 1. Both variants 1 and 2 encode the same
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform a"
                     /note="synaptosomal-associated protein, 25 kDa; SUP;
                     SNAP-25; super protein; synaptosomal-associated 25 kDa
                     protein; synaptosomal-associated protein 25"
                     /calculated_mol_wt=23205
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     CDS             1..206
                     /gene="Snap25"
                     /gene_synonym="SNAP-25a; SNAP-25B"
                     /coded_by="NM_001270576.1:122..742"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:25012"
                     /db_xref="RGD:3728"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqldrv
       61 eegmnhinqd mkeaeknlkd lgkccglfic pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001101081            1207 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 20 [Rattus norvegicus].
ACCESSION   NP_001101081 XP_001062355 XP_220079
VERSION     NP_001101081.2
DBSOURCE    REFSEQ: accession NM_001107611.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Larson,E.J., Gregorich,Z.R., Zhang,Y., Li,B.H., Aballo,T.J.,
            Melby,J.A., Ge,Y. and Guo,W.
  TITLE     Rbm20 ablation is associated with changes in the expression of
            titin-interacting and metabolic proteins
  JOURNAL   Mol Omics 18 (7), 627-634 (2022)
   PUBMED   35762193
  REMARK    GeneRIF: Rbm20 ablation is associated with changes in the
            expression of titin-interacting and metabolic proteins.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Zhang,Y., Wang,C., Sun,M., Jin,Y., Braz,C.U., Khatib,H.,
            Hacker,T.A., Liss,M., Gotthardt,M., Granzier,H., Ge,Y. and Guo,W.
  TITLE     RBM20 phosphorylation and its role in nucleocytoplasmic transport
            and cardiac pathogenesis
  JOURNAL   FASEB J 36 (5), e22302 (2022)
   PUBMED   35394688
  REMARK    GeneRIF: RBM20 phosphorylation and its role in nucleocytoplasmic
            transport and cardiac pathogenesis.
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Maimaiti,R., Zhu,C., Zhang,Y., Ding,Q. and Guo,W.
  TITLE     RBM20-Mediated Pre-mRNA Splicing Has Muscle-Specificity and
            Differential Hormonal Responses between Muscles and in Muscle Cell
            Cultures
  JOURNAL   Int J Mol Sci 22 (6), 2928 (2021)
   PUBMED   33805770
  REMARK    GeneRIF: RBM20-Mediated Pre-mRNA Splicing Has Muscle-Specificity
            and Differential Hormonal Responses between Muscles and in Muscle
            Cell Cultures.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Schwahn,D.J., Pleitner,J.M. and Greaser,M.L.
  TITLE     Megaesophagus Is a Major Pathological Condition in Rats With a
            Large Deletion in the Rbm20 Gene
  JOURNAL   Vet Pathol 57 (1), 151-159 (2020)
   PUBMED   31221019
  REMARK    GeneRIF: Megaesophagus Is a Major Pathological Condition in Rats
            With a Large Deletion in the Rbm20 Gene.
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Morinaga,A., Ito,J., Niimi,T. and Maturana,A.D.
  TITLE     RBM20 Regulates CaV1.2 Surface Expression by Promoting Exon 9*
            Inclusion of CACNA1C in Neonatal Rat Cardiomyocytes
  JOURNAL   Int J Mol Sci 20 (22), 5591 (2019)
   PUBMED   31717392
  REMARK    GeneRIF: RBM20 specifically regulates the inclusion of exon 9* in
            CACNA1C mRNA, resulting in reduced cell-surface membrane expression
            of l-channels in cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Maatz,H., Jens,M., Liss,M., Schafer,S., Heinig,M., Kirchner,M.,
            Adami,E., Rintisch,C., Dauksaite,V., Radke,M.H., Selbach,M.,
            Barton,P.J., Cook,S.A., Rajewsky,N., Gotthardt,M., Landthaler,M.
            and Hubner,N.
  TITLE     RNA-binding protein RBM20 represses splicing to orchestrate cardiac
            pre-mRNA processing
  JOURNAL   J Clin Invest 124 (8), 3419-3430 (2014)
   PUBMED   24960161
  REMARK    GeneRIF: combined transcriptome-wide crosslinking
            immunoprecipitation, RNA-seq, and quantitative proteomics in cell
            culture and hearts to examine how RBM20 regulates alternative
            splicing in the heart
REFERENCE   7  (residues 1 to 1207)
  AUTHORS   Guo,W., Pleitner,J.M., Saupe,K.W. and Greaser,M.L.
  TITLE     Pathophysiological defects and transcriptional profiling in the
            RBM20-/- rat model
  JOURNAL   PLoS One 8 (12), e84281 (2013)
   PUBMED   24367651
  REMARK    GeneRIF: new insights on Rbm20 function and how its malfunction
            leads to cardiomyopathy
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1207)
  AUTHORS   Li,S., Guo,W., Dewey,C.N. and Greaser,M.L.
  TITLE     Rbm20 regulates titin alternative splicing as a splicing repressor
  JOURNAL   Nucleic Acids Res 41 (4), 2659-2672 (2013)
   PUBMED   23307558
REFERENCE   9  (residues 1 to 1207)
  AUTHORS   Guo,W., Schafer,S., Greaser,M.L., Radke,M.H., Liss,M.,
            Govindarajan,T., Maatz,H., Schulz,H., Li,S., Parrish,A.M.,
            Dauksaite,V., Vakeel,P., Klaassen,S., Gerull,B., Thierfelder,L.,
            Regitz-Zagrosek,V., Hacker,T.A., Saupe,K.W., Dec,G.W.,
            Ellinor,P.T., MacRae,C.A., Spallek,B., Fischer,R., Perrot,A.,
            Ozcelik,C., Saar,K., Hubner,N. and Gotthardt,M.
  TITLE     RBM20, a gene for hereditary cardiomyopathy, regulates titin
            splicing
  JOURNAL   Nat Med 18 (5), 766-773 (2012)
   PUBMED   22466703
  REMARK    GeneRIF: Deep sequencing of the human and rat cardiac transcriptome
            revealed an RBM20-dependent regulation of alternative splicing
REFERENCE   10 (residues 1 to 1207)
  AUTHORS   Brauch,K.M., Karst,M.L., Herron,K.J., de Andrade,M., Pellikka,P.A.,
            Rodeheffer,R.J., Michels,V.V. and Olson,T.M.
  TITLE     Mutations in ribonucleic acid binding protein gene cause familial
            dilated cardiomyopathy
  JOURNAL   J Am Coll Cardiol 54 (10), 930-941 (2009)
   PUBMED   19712804
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EU562301.1.
            
            On Aug 15, 2009 this sequence version replaced NP_001101081.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU562301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..1207
                     /product="RNA-binding protein 20"
                     /note="probable RNA-binding protein 20"
                     /calculated_mol_wt=130658
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Region          521..596
                     /region_name="RRM_RBM20"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein 20 (RBM20); cd12685"
                     /db_xref="CDD:410086"
     Site            order(524,526..527,552,554,557..559,561,592..596)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410086"
     Region          625..686
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Region          631..650
                     /region_name="RS. /evidence=ECO:0000250|UniProtKB:Q5T481"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Region          722..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T481; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T481; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Region          951..1110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            963
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            999
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1057
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1066
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UQS8; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UQS8; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1096
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Region          1139..1173
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          1181..1207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     Site            1192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35394688,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT37.1)"
     CDS             1..1207
                     /gene="Rbm20"
                     /coded_by="NM_001107611.2:103..3726"
                     /db_xref="GeneID:309544"
                     /db_xref="RGD:1307427"
ORIGIN      
        1 mvlaaamsqd adpsgpeqpd rdacivpgvq gppapqgqqg mqplppplpp ppqpqsslpq
       61 iiqnaaklld knpfsvssqn plltspasvq laqiqaqltl hrlkmaqtav tnntaaatvl
      121 nqvlskvams qplfnqlrhp svlgtthgpt gvsqhaatvp sahfpstaia fsppsqaggp
      181 gpsvslpsqp pnamvvhtfs gvvpqtpaqp avilsigkag ptpattgfyd ygkanpgqay
      241 gsetegqpgf lpasasaaas ggvtyeghys htgqdgqatf skdfygpsaq gshaaggfpa
      301 dqagsmkgdv ggllqgtnsq werpsgfsgq nkaditagpg lwappasqpy elydpeepts
      361 drappafgsr lnnskqgfnc scrrtkegqa mlsvrplqgh qlndfrglap lhlphicsic
      421 dkkvfdlkdw elhvkgklha qkcllfsesa glrsicatge gtlsasanst avynptgned
      481 ytstlgtsya aiptrafaqs npmfpsassg tnfaqrkgag rvvhicnlpe gsctendvin
      541 lglpfgkvtn yilmkstnqa flemayteaa qamvqyyqek palingekll irmstrykel
      601 qlkkpgknva aiiqdihsqr ercmlreadr ygperprsrs pmsrslsprs hsppgpsrad
      661 wgngrdsyaw rdedretvpr rengedkrdr ldvwahdrkh yprqldkael derleggrgy
      721 rekylksgsp gplhsasgyk gredgyhrke tkakldkhpk qqqqdvpgrs rrkeearlre
      781 prhphpedsg keedlepkvt rapegtkskq seksktkrad rdqegaddkk egrgaeneag
      841 teeqegmees pasvgtqqeg tessdpentr tkkgqdcdsg sepegdnwyp tnmeelvtvd
      901 evgeedfime pdipeleeiv pidqkdkilp eicpcvtatl gldlakdftk qgetlgngda
      961 elspklpgqv pststscpnd tdmemaglnl daerkpaese tglspevsnc yekeargaeg
     1021 sdvrlapaaq rmsspqpade rarqsspfld dckargsped gphevsplee kaspttesdl
     1081 qsqacqensr ytetrslnsr spefteaelk eplslpswep evfselsipl gvefvvprtg
     1141 fycklcglfy tseeaakvsh crstvhyrnl qkylsqlaee glketegvds pspersgigp
     1201 hlerkkl
//
LOCUS       NP_001257767             316 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group I member 3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001257767
VERSION     NP_001257767.1
DBSOURCE    REFSEQ: accession NM_001270838.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Yamada,T., Cohen,S.M. and Lake,B.G.
  TITLE     Critical evaluation of the human relevance of the mode of action
            for rodent liver tumor formation by activators of the constitutive
            androstane receptor (CAR)
  JOURNAL   Crit Rev Toxicol 51 (5), 373-394 (2021)
   PUBMED   34264181
  REMARK    GeneRIF: Critical evaluation of the human relevance of the mode of
            action for rodent liver tumor formation by activators of the
            constitutive androstane receptor (CAR).
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Gabbia,D., Pozza,A.D., Albertoni,L., Lazzari,R., Zigiotto,G.,
            Carrara,M., Baldo,V., Baldovin,T., Floreani,A. and Martin,S.
  TITLE     Pregnane X receptor and constitutive androstane receptor modulate
            differently CYP3A-mediated metabolism in early- and late-stage
            cholestasis
  JOURNAL   World J Gastroenterol 23 (42), 7519-7530 (2017)
   PUBMED   29204052
  REMARK    GeneRIF: nuclear expression virtually disappeared in the late stage
            of cholestatic injury, after an initial increase
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Forbes,K.P., Kouranova,E., Tinker,D., Janowski,K., Cortner,D.,
            McCoy,A. and Cui,X.
  TITLE     Creation and Preliminary Characterization of Pregnane X Receptor
            and Constitutive Androstane Receptor Knockout Rats
  JOURNAL   Drug Metab Dispos 45 (10), 1068-1076 (2017)
   PUBMED   28716828
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Fujino,C., Tamura,Y., Tange,S., Nakajima,H., Sanoh,S., Watanabe,Y.,
            Uramaru,N., Kojima,H., Yoshinari,K., Ohta,S. and Kitamura,S.
  TITLE     Metabolism of methiocarb and carbaryl by rat and human livers and
            plasma, and effect on their PXR, CAR and PPARalpha activities
  JOURNAL   J Toxicol Sci 41 (5), 677-691 (2016)
   PUBMED   27665777
  REMARK    GeneRIF: Metabolism of methiocarb and carbaryl does not alter CAR
            activity.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Shao,Y.Y., Huang,J., Ma,Y.R., Han,M., Ma,K., Qin,H.Y., Rao,Z. and
            Wu,X.A.
  TITLE     Serum serotonin reduced the expression of hepatic transporter Mrp2
            and P-gp via regulating nuclear receptor CAR in PI-IBS rats
  JOURNAL   Can J Physiol Pharmacol 93 (8), 633-639 (2015)
   PUBMED   26053941
  REMARK    GeneRIF: Serum 5-HT regulates the expression of Mrp2 and P-gp, and
            the underlying mechanism may be related to the altered expression
            of the nuclear receptor constitutive androstane receptor.
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Numazawa,S., Shindo,S., Maruyama,K., Chibana,F., Kawahara,Y.,
            Ashino,T., Tanaka,S. and Yoshida,T.
  TITLE     Impaired nuclear translocation of CAR in hepatic preneoplastic
            lesions: association with an attenuated CYP2B induction by
            phenobarbital
  JOURNAL   FEBS Lett 579 (17), 3560-3564 (2005)
   PUBMED   15953603
  REMARK    GeneRIF: CAR expressed in the hepatic preneoplastic lesions of rats
            is resistant to nuclear translocation and transactivation of the
            phenobarbital(PB) responsive enhancer module upon PB treatment.
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Yoshinari,K., Kobayashi,K., Moore,R., Kawamoto,T. and Negishi,M.
  TITLE     Identification of the nuclear receptor CAR:HSP90 complex in mouse
            liver and recruitment of protein phosphatase 2A in response to
            phenobarbital
  JOURNAL   FEBS Lett 548 (1-3), 17-20 (2003)
   PUBMED   12885400
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Gonzalez,M.M. and Carlberg,C.
  TITLE     Cross-repression, a functional consequence of the physical
            interaction of non-liganded nuclear receptors and POU domain
            transcription factors
  JOURNAL   J Biol Chem 277 (21), 18501-18509 (2002)
   PUBMED   11891224
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Yoshinari,K., Sueyoshi,T., Moore,R. and Negishi,M.
  TITLE     Nuclear receptor CAR as a regulatory factor for the sexually
            dimorphic induction of CYB2B1 gene by phenobarbital in rat livers
  JOURNAL   Mol Pharmacol 59 (2), 278-284 (2001)
   PUBMED   11160864
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Xie,W., Barwick,J.L., Simon,C.M., Pierce,A.M., Safe,S.,
            Blumberg,B., Guzelian,P.S. and Evans,R.M.
  TITLE     Reciprocal activation of xenobiotic response genes by nuclear
            receptors SXR/PXR and CAR
  JOURNAL   Genes Dev 14 (23), 3014-3023 (2000)
   PUBMED   11114890
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089763.1 and JAXUCZ010000013.1.
            
            Transcript Variant: This variant (3) uses an alternate splice
            junction at the 3' end of an exon that extends the exon to an
            in-frame stop codon compared to variant 1. The resulting isoform
            (3) is shorter at the C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.37119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..316
                     /product="nuclear receptor subfamily 1 group I member 3
                     isoform 3"
                     /note="constitutive androstane receptor; strain Fischer
                     nuclear receptor (CAR); nuclear receptor constitutive
                     active receptor"
                     /calculated_mol_wt=36105
     Region          21..92
                     /region_name="NR_DBD_VDR_like"
                     /note="The DNA-binding domain of vitamin D receptors (VDR)
                     like nuclear receptor family is composed of two C4-type
                     zinc fingers; cd07156"
                     /db_xref="CDD:143531"
     Site            order(21,24,38,41,57,63,73,76)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143531"
     Site            order(31..33,39..40,42,46..47,70..71,77,91..92)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143531"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q14994; propagated from
                     UniProtKB/Swiss-Prot (Q9QUS1.1)"
     Site            order(58..59,72,89..90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143531"
     Region          116..316
                     /region_name="NR_LBD"
                     /note="The ligand binding domain of nuclear receptors, a
                     family of ligand-activated transcription regulators;
                     cl11397"
                     /db_xref="CDD:472173"
     Site            order(171..172,175,178..179,208..209,212..213,216,219,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132726"
     Site            order(180,183,187,192,197..198,200..201,204..205)
                     /site_type="active"
                     /note="coregulator recognition site [active]"
                     /db_xref="CDD:132726"
     CDS             1..316
                     /gene="Nr1i3"
                     /gene_synonym="CAR"
                     /coded_by="NM_001270838.1:150..1100"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:65035"
                     /db_xref="RGD:621400"
ORIGIN      
        1 mtatltletm tseeeygprn cvvcgdratg yhfhaltceg ckgffrrtvs ktigpicpfa
       61 grcevskaqr rhcpacrlqk clnvgmrkdm ilsaealalr rarqarrraq kaslqlsqqq
      121 keliqtllga htrhvgpmfd qfvqfrppay lfshhrpfqp lapvlpllth fadintfmvq
      181 qiikftkdlp lfrsltmedq isllkgaave ilhislnttf clqtqnffcg plcykmedav
      241 hvgfqyefle liihfhktlk rlqlqepeya lmaamalfsp drpgvtqree idqlqeeval
      301 ilnnhimeqq srlqsr
//
LOCUS       NP_443211                131 aa            linear   ROD 27-APR-2025
DEFINITION  agouti-signaling protein precursor [Rattus norvegicus].
ACCESSION   NP_443211
VERSION     NP_443211.1
DBSOURCE    REFSEQ: accession NM_052979.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Sasamori,S., Wiewel,A.S., Thomson,V.A., Kobayashi,M., Nakata,K. and
            Suzuki,H.
  TITLE     Potential Causative Mutation for Melanism in Rats Identified in the
            Agouti Signaling Protein Gene (Asip) of the Rattus rattus Species
            Complex on Okinawa Island, Japan
  JOURNAL   Zoolog Sci 34 (6), 513-522 (2017)
   PUBMED   29219041
  REMARK    GeneRIF: These results suggest a possible in-situ mutation of the
            Asip gene, either within the RrC lineage II population on Okinawa
            or in an unsampled RrC lineage II population with biogeographic
            links to Okinawa, although incomplete lineage sorting could not be
            ruled out.
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Hellstrom,A.R., Watt,B., Fard,S.S., Tenza,D., Mannstrom,P.,
            Narfstrom,K., Ekesten,B., Ito,S., Wakamatsu,K., Larsson,J.,
            Ulfendahl,M., Kullander,K., Raposo,G., Kerje,S., Hallbook,F.,
            Marks,M.S. and Andersson,L.
  TITLE     Inactivation of Pmel alters melanosome shape but has only a subtle
            effect on visible pigmentation
  JOURNAL   PLoS Genet 7 (9), e1002285 (2011)
   PUBMED   21949658
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Prasolova,L.A., Os'kina,I.N., Pliusnina,I.Z. and Trut,L.N.
  TITLE     [Methyl-containing diet of mothers affects the AGOUTI gene
            expression in the offspring of rats with various behavioral types]
  JOURNAL   Genetika 45 (5), 670-676 (2009)
   PUBMED   19534427
  REMARK    GeneRIF: Aggressive offspring is more sensitive to the mother's
            methyl-containing diet: the percentage of animals that are darker
            than control rats is higher among aggressive animals than among
            tame ones
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Fujimoto,W., Shiuchi,T., Miki,T., Minokoshi,Y., Takahashi,Y.,
            Takeuchi,A., Kimura,K., Saito,M., Iwanaga,T. and Seino,S.
  TITLE     Dmbx1 is essential in agouti-related protein action
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15514-15519 (2007)
   PUBMED   17873059
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Kuramoto,T., Nomoto,T., Sugimura,T. and Ushijima,T.
  TITLE     Cloning of the rat agouti gene and identification of the rat
            nonagouti mutation
  JOURNAL   Mamm Genome 12 (6), 469-471 (2001)
   PUBMED   11353396
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Hirobe,T., Wakamatsu,K. and Ito,S.
  TITLE     Effects of genic substitution at the agouti, brown, albino, dilute,
            and pink-eyed dilution loci on the proliferation and
            differentiation of mouse epidermal melanocytes in serum-free
            culture
  JOURNAL   Eur J Cell Biol 75 (2), 184-191 (1998)
   PUBMED   9548375
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Kiefer,L.L., Veal,J.M., Mountjoy,K.G. and Wilkison,W.O.
  TITLE     Melanocortin receptor binding determinants in the agouti protein
  JOURNAL   Biochemistry 37 (4), 991-997 (1998)
   PUBMED   9454589
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Ozeki,H., Ito,S., Wakamatsu,K. and Hirobe,T.
  TITLE     Chemical characterization of hair melanins in various coat-color
            mutants of mice
  JOURNAL   J Invest Dermatol 105 (3), 361-366 (1995)
   PUBMED   7665913
REFERENCE   9  (residues 1 to 131)
  AUTHORS   Duhl,D.M., Vrieling,H., Miller,K.A., Wolff,G.L. and Barsh,G.S.
  TITLE     Neomorphic agouti mutations in obese yellow mice
  JOURNAL   Nat Genet 8 (1), 59-65 (1994)
   PUBMED   7987393
REFERENCE   10 (residues 1 to 131)
  AUTHORS   Markert,C.L. and Silvers,W.K.
  TITLE     The Effects of Genotype and Cell Environment on Melanoblast
            Differentiation in the House Mouse
  JOURNAL   Genetics 41 (3), 429-450 (1956)
   PUBMED   17247639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB045587.1.
            
            Summary: This gene is involved in hair pigmentation. In several
            strains (ACI, IS, LEA, LEC, NER, and WKAH) this gene encodes a
            functional protein while in others (BN, BUF, DON, F344, SD, SHR,
            TM, WKY, and WTC) it lacks a 19 nt indel and is non-protein coding.
            [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1, coding) represents the
            protein-coding allele.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB045587.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760434 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            polymorphic pseudogene :: PMID: 11353396
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..131
                     /product="agouti-signaling protein precursor"
                     /note="agouti switch protein; Agouti (coat color)"
                     /calculated_mol_wt=11844
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     Region          6..127
                     /region_name="Agouti"
                     /note="Agouti protein; smart00792"
                     /db_xref="CDD:197876"
     mat_peptide     23..131
                     /product="Agouti-signaling protein. /id=PRO_0000001031"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JA2.1)"
                     /calculated_mol_wt=11844
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99JA2.1)"
     Region          58..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JA2.1)"
     CDS             1..131
                     /gene="Asip"
                     /gene_synonym="ASP"
                     /coded_by="NM_052979.2:93..488"
                     /db_xref="GeneID:24152"
                     /db_xref="RGD:2003"
ORIGIN      
        1 mdvtrlllat lvgflcfltv hshlvfeetl gddrslksns sinsldfssv sivalnkksk
       61 kisrkeaekr krsskkkasi kkvarpppps pcvatrdsck ppapaccnpc ascqcrffgs
      121 actcrvlnpn c
//
LOCUS       NP_001257716             579 aa            linear   ROD 27-APR-2025
DEFINITION  glutaminase liver isoform, mitochondrial isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257716
VERSION     NP_001257716.1
DBSOURCE    REFSEQ: accession NM_001270787.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Zhou,X., Zhuo,M., Zhang,Y., Shi,E., Ma,X. and Li,H.
  TITLE     miR-190a-5p regulates cardiomyocytes response to ferroptosis via
            directly targeting GLS2
  JOURNAL   Biochem Biophys Res Commun 566, 9-15 (2021)
   PUBMED   34111670
  REMARK    GeneRIF: miR-190a-5p regulates cardiomyocytes response to
            ferroptosis via directly targeting GLS2.
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cardona,C., Sanchez-Mejias,E., Davila,J.C., Martin-Rufian,M.,
            Campos-Sandoval,J.A., Vitorica,J., Alonso,F.J., Mates,J.M.,
            Segura,J.A., Norenberg,M.D., Rama Rao,K.V., Jayakumar,A.R.,
            Gutierrez,A. and Marquez,J.
  TITLE     Expression of Gls and Gls2 glutaminase isoforms in astrocytes
  JOURNAL   Glia 63 (3), 365-382 (2015)
   PUBMED   25297978
  REMARK    GeneRIF: GABAergic neurons and astrocytes express Gls and Gls2
            isoenzymes in nucleus and mitochondria, in addition to
            glutamatergic neurons
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Savilov,P.N. and Yakovlev,V.N.
  TITLE     Phosphate-dependent glutaminase response to liver injury and
            hyperbaric oxygenation
  JOURNAL   Bull Exp Biol Med 157 (3), 299-301 (2014)
   PUBMED   25065305
  REMARK    GeneRIF: In animals with chronic hepatitis; hyperbaric oxygenation
            restricted the stimulating effect of hepatic resection on
            phosphate-dependent glutaminase activity.
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Martin-Rufian,M., Tosina,M., Campos-Sandoval,J.A., Manzanares,E.,
            Lobo,C., Segura,J.A., Alonso,F.J., Mates,J.M. and Marquez,J.
  TITLE     Mammalian glutaminase Gls2 gene encodes two functional alternative
            transcripts by a surrogate promoter usage mechanism
  JOURNAL   PLoS One 7 (6), e38380 (2012)
   PUBMED   22679499
  REMARK    GeneRIF: Study demonstrated expression of alternative transcripts
            of the mammalian Gls2 gene. Transcriptional mechanisms giving rise
            to GLS2 variants and isolation of novel GLS2 transcripts in human,
            rat and mouse are presented.
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Suzuki,S., Tanaka,T., Poyurovsky,M.V., Nagano,H., Mayama,T.,
            Ohkubo,S., Lokshin,M., Hosokawa,H., Nakayama,T., Suzuki,Y.,
            Sugano,S., Sato,E., Nagao,T., Yokote,K., Tatsuno,I. and Prives,C.
  TITLE     Phosphate-activated glutaminase (GLS2), a p53-inducible regulator
            of glutamine metabolism and reactive oxygen species
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7461-7466 (2010)
   PUBMED   20351271
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Chung-Bok,M.I., Vincent,N., Jhala,U. and Watford,M.
  TITLE     Rat hepatic glutaminase: identification of the full coding sequence
            and characterization of a functional promoter
  JOURNAL   Biochem J 324 (Pt 1) (Pt 1), 193-200 (1997)
   PUBMED   9164856
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Smith,E.M. and Watford,M.
  TITLE     Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence
            similarity to kidney-type glutaminase
  JOURNAL   J Biol Chem 265 (18), 10631-10636 (1990)
   PUBMED   2191954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC089776.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            at the 3' end of the first exon compared to variant 1. The
            resulting isoform (2) has a shorter and distinct N-terminus
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211735.1, SRR26643299.29278.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..579
                     /product="glutaminase liver isoform, mitochondrial isoform
                     2"
                     /EC_number="3.5.1.2"
                     /note="glutaminase 2 (liver, mitochondrial); GLS;
                     L-glutaminase; L-glutamine amidohydrolase; liver
                     mitochondrial glutaminase"
                     /calculated_mol_wt=63758
     Region          49..132
                     /region_name="EF-hand_14"
                     /note="EF-hand domain; pfam17959"
                     /db_xref="CDD:465587"
     Region          154..438
                     /region_name="Glutaminase"
                     /note="pfam04960"
                     /db_xref="CDD:461499"
     Region          <467..>549
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          467..493
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(468..469,472..474,476..477,481,484,493,495,497,
                     501..502,505..507,509..510,514,517,527,529,531,535..536,
                     539..541,543..544,548)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          495..527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..579
                     /gene="Gls2"
                     /gene_synonym="Ga"
                     /coded_by="NM_001270787.1:552..2291"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:192268"
                     /db_xref="RGD:620359"
ORIGIN      
        1 mpfpldvglw vrraravrcc ppgrafgqvg lrddacpsda snsgmlprlg dllfytiaeg
       61 qeripihkft talkatglqt sdprlqdcms kmqrmvqess sgglldrelf qkcvssnivl
      121 ltqafrkkfv ipdfeeftgh vdrifedake ltggkvaayi phlaksnpdl wgvslctvdg
      181 qrhsvghtki pfclqscvkp ltyaisvstl gtdyvhkfvg kepsglrynk lslneegiph
      241 npmvnagaiv vsslikmdcn kaekfdfvlq ylnkmagnef mgfsnatfqs eketgdrnya
      301 igyylkekkc fpkgvdmmaa ldlyfqlcsv evtcesgsvm aatlanggic pitgesvlsa
      361 eavrntlslm hscgmydfsg qfafhvglpa ksavsgaill vvpnvmgmmc lsppldklgn
      421 shrgisfcqk lvslfnfhny dnlrhcarkl dprreggevr nktvvnllfa aysgdvsalr
      481 rfalsavdme qkdydsrtal hvaaaeghid vvkflieack vnpfvkdrwg niplddavqf
      541 nhlevvkllq dyhdsymlse tqaevaaetl skenlesmv
//
LOCUS       NP_659563               1102 aa            linear   ROD 27-APR-2025
DEFINITION  voltage-gated delayed rectifier potassium channel KCNH8 [Rattus
            norvegicus].
ACCESSION   NP_659563 XP_234523
VERSION     NP_659563.1
DBSOURCE    REFSEQ: accession NM_145095.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1102)
  AUTHORS   Ono,A., Hirooka,K., Nakano,Y., Nitta,E., Nishiyama,A. and
            Tsujikawa,A.
  TITLE     Gene expression changes in the retina after systemic administration
            of aldosterone
  JOURNAL   Jpn J Ophthalmol 62 (4), 499-507 (2018)
   PUBMED   29713904
REFERENCE   2  (residues 1 to 1102)
  AUTHORS   Martin,S., Lino de Oliveira,C., Mello de Queiroz,F., Pardo,L.A.,
            Stuhmer,W. and Del Bel,E.
  TITLE     Eag1 potassium channel immunohistochemistry in the CNS of adult rat
            and selected regions of human brain
  JOURNAL   Neuroscience 155 (3), 833-844 (2008)
   PUBMED   18650019
  REMARK    GeneRIF: The results indicate that Eag1 protein expression greatly
            overlaps with mRNA distribution in rat.
REFERENCE   3  (residues 1 to 1102)
  AUTHORS   Zhang,C., Kavurma,M.M., Lai,A. and Khachigian,L.M.
  TITLE     Ets-1 protects vascular smooth muscle cells from undergoing
            apoptosis by activating p21WAF1/Cip1: ETS-1 regulates basal and and
            inducible p21WAF1/Cip: ETS-1 regulates basal and inducible
            p21WAF1/Cip1 transcription via distinct cis-acting elements in the
            p21WAF/Cip1 promoter
  JOURNAL   J Biol Chem 278 (30), 27903-27909 (2003)
   PUBMED   12740370
REFERENCE   4  (residues 1 to 1102)
  AUTHORS   Saganich,M.J., Machado,E. and Rudy,B.
  TITLE     Differential expression of genes encoding subthreshold-operating
            voltage-gated K+ channels in brain
  JOURNAL   J Neurosci 21 (13), 4609-4624 (2001)
   PUBMED   11425889
REFERENCE   5  (residues 1 to 1102)
  AUTHORS   Wulfsen,I., Hauber,H.P., Schiemann,D., Bauer,C.K. and Schwarz,J.R.
  TITLE     Expression of mRNA for voltage-dependent and inward-rectifying K
            channels in GH3/B6 cells and rat pituitary
  JOURNAL   J Neuroendocrinol 12 (3), 263-272 (2000)
   PUBMED   10718922
REFERENCE   6  (residues 1 to 1102)
  AUTHORS   Engeland,B., Neu,A., Ludwig,J., Roeper,J. and Pongs,O.
  TITLE     Cloning and functional expression of rat ether-a-go-go-like K+
            channel genes
  JOURNAL   J Physiol 513 (Pt 3) (Pt 3), 647-654 (1998)
   PUBMED   9824707
REFERENCE   7  (residues 1 to 1102)
  AUTHORS   Shi,W., Wang,H.S., Pan,Z., Wymore,R.S., Cohen,I.S., McKinnon,D. and
            Dixon,J.E.
  TITLE     Cloning of a mammalian elk potassium channel gene and EAG mRNA
            distribution in rat sympathetic ganglia
  JOURNAL   J Physiol 511 (Pt 3) (Pt 3), 675-682 (1998)
   PUBMED   9714851
REFERENCE   8  (residues 1 to 1102)
  AUTHORS   Bellacosa,A., Datta,K., Bear,S.E., Patriotis,C., Lazo,P.A.,
            Copeland,N.G., Jenkins,N.A. and Tsichlis,P.N.
  TITLE     Effects of provirus integration in the Tpl-1/Ets-1 locus in Moloney
            murine leukemia virus-induced rat T-cell lymphomas: levels of
            expression, polyadenylation, transcriptional initiation, and
            differential splicing of the Ets-1 mRNA
  JOURNAL   J Virol 68 (4), 2320-2330 (1994)
   PUBMED   8139017
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF061957.1.
            
            On Apr 19, 2005 this sequence version replaced XP_234523.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF061957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1102
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..1102
                     /product="voltage-gated delayed rectifier potassium
                     channel KCNH8"
                     /note="ether-a-go-go-like potassium channel 1; ELK channel
                     3; voltage-gated potassium channel subunit Kv12.1;
                     ether-a-go-go-like potassium channel 3; potassium channel,
                     voltage gated eag related subfamily H, member 8; potassium
                     voltage-gated channel, subfamily H (eag-related), member
                     8"
                     /calculated_mol_wt=123100
     Region          40..135
                     /region_name="PAS_9"
                     /note="PAS domain; pfam13426"
                     /db_xref="CDD:463873"
     Region          175..>615
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            320
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            328..348
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          434..439
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Site            449..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          551..668
                     /region_name="cNMP-binding domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00060"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          578..>656
                     /region_name="PRK11753"
                     /note="cAMP-activated global transcriptional regulator
                     CRP"
                     /db_xref="CDD:236969"
     Region          683..744
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          762..793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          818..845
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     Region          960..983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QWS8.2)"
     CDS             1..1102
                     /gene="Kcnh8"
                     /gene_synonym="Elk1; ELK3; Ets-1; RELK3"
                     /coded_by="NM_145095.2:49..3357"
                     /db_xref="GeneID:246325"
                     /db_xref="RGD:2549"
ORIGIN      
        1 mpvmkgllap qntfldtiat rfdgthsnfi lanaqvakgf pivycsdgfc elagfartev
       61 mqkscsckfl fgvetneqlm lqieksleek vefkgeimfy kkngapfwcl ldivpiknek
      121 gdvvlflasf kditdtkvki tsedkkedra kgrsragshf dsarrrsrav lyhisghlqr
      181 reknklkinn nvfvdkpafp eykvsdakks kfillhfstf kagwdwlill atfyvavtvp
      241 ynvcfigned lsttrsttvs diaveilfii diilnfrtty vsksgqvife arsicihyvt
      301 twfiidliaa lpfdllyafn vtvvslvhll ktvrllrllr llqkldrysq hstivltllm
      361 smfallahwm aciwyvigkm erednsllkw evgwlhelgk rlespyygnn tlggpsirsa
      421 yiaalyftls sltsvgfgnv santdaekif sictmligal mhalvfgnvt aiiqrmysrw
      481 slyhtrtkdl kdfirvhhlp qqlkqrmley fqttwsvnng idsnellkdf pdelrsditm
      541 hlnkeilqls lfecasrgcl rslslhikts fcapgeyllr qgdalqaiyf vcsgsmevlk
      601 dsmvlailgk gdliganlsi kdqviktnad vkaltycdlq ciilkglfev lglypeyahk
      661 fvediqhdlt ynlreghesd visrlsnkst vpqaepkgng sikkrlpsiv edeeeeevee
      721 eettslspiy trgssvshsk ktgssksylg lslkqltsgt vpfhspirvs sanspktkqe
      781 adppnhgtrk eknlkvqlcs lgtagtpels privdgiedg nsseetqtfd fgseqirpep
      841 rispslgese igaaflfika eetkqqinkl nsevttltqe vsqlgkdmrs imqllenils
      901 pqqpsqfcsl hptsicpsre sfqtrvswsa hqpclhlqan gahlyhgnvt sdiwsvdpsl
      961 vgsnpqrtea heqspvdsel hhspnlaysp shcqviqegh lqflrcisph sdttltplqs
     1021 isatlsssvc sssetslhlv lpsrseegsi thgpvssfsl enlpgswdre gmmsastepl
     1081 enfpvevvts tadvkdskai nv
//
LOCUS       NP_113790                379 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 10 [Rattus
            norvegicus].
ACCESSION   NP_113790
VERSION     NP_113790.2
DBSOURCE    REFSEQ: accession NM_031602.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Lu,S., Wang,J., Sun,T., Yan,H., Zou,W., Li,H., Qi,Q. and Sun,M.
  TITLE     [IL-6 promotes the activation of rat astrocytes and down-regulation
            of the expression of Kir4.1 channel]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 38 (4), 316-320 (2022)
   PUBMED   35583060
  REMARK    GeneRIF: [IL-6 promotes the activation of rat astrocytes and
            down-regulation of the expression of Kir4.1 channel].
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Peric,M., Nikolic,L., Andjus,P.R. and Bataveljic,D.
  TITLE     Dysfunction of oligodendrocyte inwardly rectifying potassium
            channel in a rat model of amyotrophic lateral sclerosis
  JOURNAL   Eur J Neurosci 54 (7), 6339-6354 (2021)
   PUBMED   34510584
  REMARK    GeneRIF: Dysfunction of oligodendrocyte inwardly rectifying
            potassium channel in a rat model of amyotrophic lateral sclerosis.
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Madadi,A., Wolfart,J., Lange,F., Brehme,H., Linnebacher,M.,
            Brauer,A.U., Buttner,A., Freiman,T., Henker,C., Einsle,A.,
            Rackow,S., Kohling,R., Kirschstein,T. and Muller,S.
  TITLE     Correlation between Kir4.1 expression and barium-sensitive currents
            in rat and human glioma cell lines
  JOURNAL   Neurosci Lett 741, 135481 (2021)
   PUBMED   33161102
  REMARK    GeneRIF: Correlation between Kir4.1 expression and barium-sensitive
            currents in rat and human glioma cell lines.
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Kinboshi,M., Shimizu,S., Mashimo,T., Serikawa,T., Ito,H., Ikeda,A.,
            Takahashi,R. and Ohno,Y.
  TITLE     Down-Regulation of Astrocytic Kir4.1 Channels during the Audiogenic
            Epileptogenesis in Leucine-Rich Glioma-Inactivated 1 (Lgi1) Mutant
            Rats
  JOURNAL   Int J Mol Sci 20 (5), 1013 (2019)
   PUBMED   30813600
  REMARK    GeneRIF: he down-regulation of Kir4.1 channels in astrocytes is
            involved in audiogenic epileptogenesis caused by Lgi1 mutation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Thompson,K., Chen,J., Luo,Q., Xiao,Y., Cummins,T.R. and
            Bhatwadekar,A.D.
  TITLE     Advanced glycation end (AGE) product modification of laminin
            downregulates Kir4.1 in retinal Muller cells
  JOURNAL   PLoS One 13 (2), e0193280 (2018)
   PUBMED   29474462
  REMARK    GeneRIF: studies suggest that AGE-modification of laminin is
            detrimental to Kir4.1 channels. By studying the role of AGEs in
            Kir4.1 channels we have identified a novel mechanism of Muller cell
            dysfunction and its subsequent involvement in Diabetic retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Kurschner,C. and Yuzaki,M.
  TITLE     Neuronal interleukin-16 (NIL-16): a dual function PDZ domain
            protein
  JOURNAL   J Neurosci 19 (18), 7770-7780 (1999)
   PUBMED   10479680
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Kurschner,C., Mermelstein,P.G., Holden,W.T. and Surmeier,D.J.
  TITLE     CIPP, a novel multivalent PDZ domain protein, selectively interacts
            with Kir4.0 family members, NMDA receptor subunits, neurexins, and
            neuroligins
  JOURNAL   Mol Cell Neurosci 11 (3), 161-172 (1998)
   PUBMED   9647694
REFERENCE   8  (residues 1 to 379)
  AUTHORS   Bredt,D.S., Wang,T.L., Cohen,N.A., Guggino,W.B. and Snyder,S.H.
  TITLE     Cloning and expression of two brain-specific inwardly rectifying
            potassium channels
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 6753-6757 (1995)
   PUBMED   7624316
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Takumi,T., Ishii,T., Horio,Y., Morishige,K., Takahashi,N.,
            Yamada,M., Yamashita,T., Kiyama,H., Sohmiya,K., Nakanishi,S. et al.
  TITLE     A novel ATP-dependent inward rectifier potassium channel expressed
            predominantly in glial cells
  JOURNAL   J Biol Chem 270 (27), 16339-16346 (1995)
   PUBMED   7608203
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Bond,C.T., Pessia,M., Xia,X.M., Lagrutta,A., Kavanaugh,M.P. and
            Adelman,J.P.
  TITLE     Cloning and expression of a family of inward rectifier potassium
            channels
  JOURNAL   Recept Channels 2 (3), 183-191 (1994)
   PUBMED   7874445
  REMARK    Erratum:[Receptors Channels 1994;2(4):following 350]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 28, 2015 this sequence version replaced NP_113790.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U27558.1, X86818.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..379
                     /product="ATP-sensitive inward rectifier potassium channel
                     10"
                     /note="BIR10; BIRK1; kir4.1; brain-specific inwardly
                     rectifying K(+) channel 1; ATP-sensitive inward rectifier
                     potassium channel KAB-2; potassium channel, inwardly
                     rectifying subfamily J member 10; inward rectifier K(+)
                     channel Kir4.1; potassium voltage-gated channel subfamily
                     J member 10"
                     /calculated_mol_wt=42349
     Region          31..172
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            62..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49655.1)"
     Region          128..133
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P49655.1)"
     Site            141..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49655.1)"
     Site            158
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P49655.1)"
     Region          179..354
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..379
                     /gene="Kcnj10"
                     /coded_by="NM_031602.2:135..1274"
                     /db_xref="GeneID:29718"
                     /db_xref="RGD:61822"
ORIGIN      
        1 mtsvakvyys qttqtesrpl vapgirrrrv ltkdgrsnvr mehiadkrfl ylkdlwttfi
       61 dmqwryklll fsatfagtwf lfgvvwylva vahgdllelg ppanhtpcvv qvhtltgafl
      121 fslesqttig ygfryiseec plaivlliaq lvlttileif itgtflakia rpkkraetir
      181 fsqhavvayh ngklclmirv anmrksllig cqvtgkllqt hqtkegenir lnqvnvtfqv
      241 dtasdspfli lpltfyhvvd etsplkdlpl rsgegdfelv lilsgtvest satcqvrtsy
      301 lpeeilwgye ftpaislsas gkyvadfslf dqvvkvaspg glrdstvryg dpeklklees
      361 lreqaekegs alsvrisnv
//
LOCUS       NP_001073622             245 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane and ubiquitin-like domain-containing protein 1
            [Rattus norvegicus].
ACCESSION   NP_001073622
VERSION     NP_001073622.1
DBSOURCE    REFSEQ: accession NM_001080153.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Lan,X., Li,G., Liu,H., Fu,H., Chen,P. and Liu,M.
  TITLE     MiR-27a/b Regulates Liver Regeneration by Posttranscriptional
            Modification of Tmub1
  JOURNAL   Dig Dis Sci 63 (9), 2362-2372 (2018)
   PUBMED   29777440
  REMARK    GeneRIF: MiR-27a/b regulates hepatocyte proliferation by
            controlling posttranscriptional modification of Tmub1 during liver
            regeneration.
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Lan,X., Fu,H., Li,G., Zeng,W., Lin,X., Zhu,Y., Liu,M. and Chen,P.
  TITLE     TMUB1 Inhibits BRL-3A Hepatocyte Proliferation by Interfering with
            the Binding of CAML to Cyclophilin B through its TM1 Hydrophobic
            Domain
  JOURNAL   Sci Rep 8 (1), 9917 (2018)
   PUBMED   29967478
  REMARK    GeneRIF: TMUB1 regulates hepatocyte proliferation by interacting
            with CAML and further interferes with the binding of CAML to
            cyclophilin B.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Fu,H., Xu,J., Chen,J., Li,G., Zhao,X. and Chen,P.
  TITLE     Microarray analysis reveals Tmub1 as a cell cycle-associated
            protein in rat hepatocytes
  JOURNAL   Mol Med Rep 17 (3), 4337-4344 (2018)
   PUBMED   29344642
  REMARK    GeneRIF: The transcriptional profile and potential biological
            processes affected by Tmub1 expression in hepatocytes have been
            reported.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Liu,M., Yuan,T., Liu,H. and Chen,P.
  TITLE     CCAAT/enhancer-binding protein beta regulates interleukin-6-induced
            transmembrane and ubiquitin-like domain containing 1 gene
            expression in hepatocytes
  JOURNAL   Mol Med Rep 10 (4), 2177-2183 (2014)
   PUBMED   25109894
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Castelli,M., Piobbico,D., Bartoli,D., Pieroni,S., Brunacci,C.,
            Bellet,M.M., Chiacchiaretta,M., Della Fazia,M.A. and Servillo,G.
  TITLE     Different functions of HOPS isoforms in the cell: HOPS shuttling
            isoform is determined by RIP cleavage system
  JOURNAL   Cell Cycle 13 (2), 293-302 (2014)
   PUBMED   24240191
  REMARK    GeneRIF: HOPS has distinct, isoform-specific functions in the
            nucleolus, nucleus, and cytoplasm.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Liu,M., Liu,H., Wang,X., Chen,P. and Chen,H.
  TITLE     IL-6 induction of hepatocyte proliferation through the
            Tmub1-regulated gene pathway
  JOURNAL   Int J Mol Med 29 (6), 1106-1112 (2012)
   PUBMED   22426572
  REMARK    GeneRIF: Tmub1 plays a negative role in IL-6-induced hepatocyte
            proliferation.
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Jo,Y., Sguigna,P.V. and DeBose-Boyd,R.A.
  TITLE     Membrane-associated ubiquitin ligase complex containing gp78
            mediates sterol-accelerated degradation of
            3-hydroxy-3-methylglutaryl-coenzyme A reductase
  JOURNAL   J Biol Chem 286 (17), 15022-15031 (2011)
   PUBMED   21343306
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Zhang,W., Savelieva,K.V., Suwanichkul,A., Small,D.L.,
            Kirkpatrick,L.L., Xu,N., Lanthorn,T.H. and Ye,G.L.
  TITLE     Transmembrane and ubiquitin-like domain containing 1 (Tmub1)
            regulates locomotor activity and wakefulness in mice and interacts
            with CAMLG
  JOURNAL   PLoS One 5 (6), e11261 (2010)
   PUBMED   20582322
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Yang,H., Takagi,H., Konishi,Y., Ageta,H., Ikegami,K., Yao,I.,
            Sato,S., Hatanaka,K., Inokuchi,K., Seog,D.H. and Setou,M.
  TITLE     Transmembrane and ubiquitin-like domain-containing protein 1
            (Tmub1/HOPS) facilitates surface expression of GluR2-containing
            AMPA receptors
  JOURNAL   PLoS One 3 (7), e2809 (2008)
   PUBMED   18665261
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Della Fazia,M.A., Castelli,M., Bartoli,D., Pieroni,S.,
            Pettirossi,V., Piobbico,D., Viola-Magni,M. and Servillo,G.
  TITLE     HOPS: a novel cAMP-dependent shuttling protein involved in protein
            synthesis regulation
  JOURNAL   J Cell Sci 118 (Pt 14), 3185-3194 (2005)
   PUBMED   16014383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000004.1 and
            DY313123.1.
            
            Summary: The protein encoded by this gene belongs to a group of
            integral ubiquitin-like domain containing proteins that are
            involved in a range of cellular processes. In mouse, the protein
            exists in uncleaved transmembrane forms as well as a cleaved form
            that shuttles between the nucleus and cytoplasm. During liver
            regeneration in rat, it has been shown that the protein shuttles
            from the cytoplasm to the nucleus to inhibit hepatocyte
            proliferation. Homozygous null mutant mice display normal
            development and physiology but exhibit a strong increase in
            locomoter activity during the dark phase of the light:dark cycle,
            indicating a function in behavioral regulation. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2015].
            
            Transcript Variant: This variant (2) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY603378.1, SRR26643288.17470.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..245
                     /product="transmembrane and ubiquitin-like
                     domain-containing protein 1"
                     /note="hepatocyte odd protein shuttling protein"
                     /calculated_mol_wt=26218
     Region          2..30
                     /region_name="Required to release iHOPS from membranes.
                     /evidence=ECO:0000250|UniProtKB:Q9JMG3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Region          34..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Region          101..171
                     /region_name="Ubl_TMUB1"
                     /note="ubiquitin-like (Ubl) domain found in transmembrane
                     and ubiquitin-like domain-containing protein 1 (TMUB1);
                     cd17131"
                     /db_xref="CDD:340651"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BVT8; propagated from
                     UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            194..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53AQ4.1)"
     CDS             1..245
                     /gene="Tmub1"
                     /gene_synonym="Hops"
                     /coded_by="NM_001080153.2:173..910"
                     /db_xref="GeneID:362301"
                     /db_xref="RGD:735120"
ORIGIN      
        1 maliegvgde vtvlfsvlac llvlalawvs thttestdpl pqssgtttpa qpseamtaid
       61 sireeapgae spslrhrgps aqpepeagvt astppdspqe plllrlkfln dseqvarawp
      121 qdtigslkrt qfpgreqqvr liyqgqllgd dtqtlgslhl ppncvlhchv strvgpphpp
      181 cppgsepgps gleigslllp lllllllllw ycqiqyrpff pltatlglag ftlllsllaf
      241 amyrp
//
LOCUS       NP_001257787             176 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform e [Rattus norvegicus].
ACCESSION   NP_001257787
VERSION     NP_001257787.1
DBSOURCE    REFSEQ: accession NM_001270858.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC092646.1.
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon and has an alternate exon in the 3' end compared to variant 1.
            This additional exon has an in-frame stop codon, resulting in an
            isoform (e) with a shorter and distinct C-terminus and lacking an
            alternate internal segment compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF026529.1, SRR22399492.1757457.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..176
                     /product="stathmin-4 isoform e"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=20299
     Region          49..171
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     CDS             1..176
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_001270858.1:180..710"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyeadtv dlnwcvisdm evielnkcts
       61 gqsfevilkp psfdgvpefn aslprrrdps leeiqkklea aeerrkyqea ellkhlaekr
      121 ehereviqka ieennnfikm akeklaqkme snkenreahl aamlerlqek eppaar
//
LOCUS       NP_001291463             145 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL24 [Rattus norvegicus].
ACCESSION   NP_001291463
VERSION     NP_001291463.1
DBSOURCE    REFSEQ: accession NM_001304534.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Henras,A.K., Plisson-Chastang,C., O'Donohue,M.F., Chakraborty,A.
            and Gleizes,P.E.
  TITLE     An overview of pre-ribosomal RNA processing in eukaryotes
  JOURNAL   Wiley Interdiscip Rev RNA 6 (2), 225-242 (2015)
   PUBMED   25346433
  REMARK    Review article
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Takagi,M., Absalon,M.J., McLure,K.G. and Kastan,M.B.
  TITLE     Regulation of p53 translation and induction after DNA damage by
            ribosomal protein L26 and nucleolin
  JOURNAL   Cell 123 (1), 49-63 (2005)
   PUBMED   16213212
  REMARK    Erratum:[Cell. 2005 Nov 4;123(3):536-7]
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Anthony,T.G., Reiter,A.K., Anthony,J.C., Kimball,S.R. and
            Jefferson,L.S.
  TITLE     Deficiency of dietary EAA preferentially inhibits mRNA translation
            of ribosomal proteins in liver of meal-fed rats
  JOURNAL   Am J Physiol Endocrinol Metab 281 (3), E430-E439 (2001)
   PUBMED   11500297
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Paz,V., Olvera,J., Chan,Y.L. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L26
  JOURNAL   FEBS Lett 251 (1-2), 89-93 (1989)
   PUBMED   2546830
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Marion,M.J. and Marion,C.
  TITLE     Localization of ribosomal proteins on the surface of mammalian 60S
            ribosomal subunits by means of immobilized enzymes. Correlation
            with chemical cross-linking data
  JOURNAL   Biochem Biophys Res Commun 149 (3), 1077-1083 (1987)
   PUBMED   3426607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript from the reference strain was
            available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211391.1, FQ223442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..145
                     /product="large ribosomal subunit protein uL24"
                     /note="60S ribosomal protein L26"
                     /calculated_mol_wt=17127
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12749.1)"
     Region          8..122
                     /region_name="Ribosomal_L26"
                     /note="Ribosomal proteins L26 eukaryotic, L24P archaeal;
                     pfam16906"
                     /db_xref="CDD:465307"
     Region          122..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12749.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P61254; propagated from
                     UniProtKB/Swiss-Prot (P12749.1)"
     CDS             1..145
                     /gene="Rpl26"
                     /coded_by="NM_001304534.1:65..502"
                     /db_xref="GeneID:287417"
                     /db_xref="RGD:1310607"
ORIGIN      
        1 mkfnpfvtsd rsknrkrhfn apshirrkim ssplskelrq kynvrsmpir kddevqvvrg
       61 hykgqqigkv vqvyrkkyvi yiervqreka ngttvhvgih pskvvitrlk ldkdrkkile
      121 rkaksrqvgk ekgkykeeti ekmqe
//
LOCUS       NP_001257508             523 aa            linear   ROD 27-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform a precursor [Rattus norvegicus].
ACCESSION   NP_001257508
VERSION     NP_001257508.1
DBSOURCE    REFSEQ: accession NM_001270579.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1, Z23272.1 and CR475040.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z23272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN12840108
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..523
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform a precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=57662
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     mat_peptide     20..523
                     /product="Pituitary adenylate cyclase-activating
                     polypeptide type I receptor. /id=PRO_0000012843"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
                     /calculated_mol_wt=57662
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32215.2)"
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32215.2)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32215.2)"
     Region          124..138
                     /region_name="Important for ADCYAP1/PACAP ligand binding
                     and specificity. /evidence=ECO:0000250|UniProtKB:P41586"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          124..138
                     /region_name="Important for ligand binding and
                     specificity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          149..472
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          152..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            152..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          185..206
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Site            223..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          226..248
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            267..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          267..283
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          301..324
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            302..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Site            347..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Region          407..429
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          434..459
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            435..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32215.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70205; propagated from
                     UniProtKB/Swiss-Prot (P32215.2)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70205; propagated from
                     UniProtKB/Swiss-Prot (P32215.2)"
     CDS             1..523
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_001270579.1:338..1909"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiyltn lrlrvpkktr
      361 edplpvpsdq hsppflscvq kcyckpqraq qhsckmsels titlrlarst llliplfgih
      421 ytvfafspen vskrerlvfe lglgsfqgfv vavlycflng evqaeikrkw rswkvnryft
      481 mdfkhrhpsl assgvnggtq lsilsksssq lrmsslpadn lat
//
LOCUS       NP_001264530             300 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein C isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001264530
VERSION     NP_001264530.1
DBSOURCE    REFSEQ: accession NM_001277601.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Liu,N., Dai,Q., Zheng,G., He,C., Parisien,M. and Pan,T.
  TITLE     N(6)-methyladenosine-dependent RNA structural switches regulate
            RNA-protein interactions
  JOURNAL   Nature 518 (7540), 560-564 (2015)
   PUBMED   25719671
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Todd,M.A. and Picketts,D.J.
  TITLE     PHF6 interacts with the nucleosome remodeling and deacetylation
            (NuRD) complex
  JOURNAL   J Proteome Res 11 (8), 4326-4337 (2012)
   PUBMED   22720776
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Raffalli-Mathieu,F., Geneste,O. and Lang,M.A.
  TITLE     Characterization of two nuclear proteins that interact with
            cytochrome P-450 1A2 mRNA. Regulation of RNA binding and possible
            role in the expression of the Cyp1a2 gene
  JOURNAL   Eur J Biochem 245 (1), 17-24 (1997)
   PUBMED   9128719
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Sharp,Z.D., Smith,K.P., Cao,Z.D. and Helsel,S.
  TITLE     Cloning of the nucleic acid-binding domain of the rat HnRNP C-type
            protein
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 306-309 (1990)
   PUBMED   2088340
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region compared to variant 1. It encodes
            isoform 2 which is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF110512.1, SRR22399489.1099025.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840108, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..300
                     /product="heterogeneous nuclear ribonucleoprotein C
                     isoform 2"
                     /note="hnRNP C protein C-terminal fragment (158 AA); hnRNP
                     core protein C; heterogeneous nuclear ribonucleoprotein C
                     (C1/C2); heterogeneous nuclear ribonucleoproteins C1/C2"
                     /calculated_mol_wt=32925
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P07910; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Region          10..93
                     /region_name="RRM_hnRNPC"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP
                     C1/C2); cd12603"
                     /db_xref="CDD:410015"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z204; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Region          142..148
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07910; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07910; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Z204; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Region          206..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z204; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07910; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07910; propagated from
                     UniProtKB/Swiss-Prot (G3V9R8.2)"
     CDS             1..300
                     /gene="Hnrnpc"
                     /gene_synonym="hnRNP C; Hnrpc"
                     /coded_by="NM_001277601.1:217..1119"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290046"
                     /db_xref="RGD:1309982"
ORIGIN      
        1 masnvtnktd prsmnsrvfi gnlntlvvkk sdveaifsky gkivgcsvhk gfafvqyvne
       61 rnaraavage dgrmiagqvl dinlaaepkv nrgkagvkrs aaemygssfd ldydfqrdyy
      121 drmysyparv pppppiarav vpskrqrvsg ntsrrgksgf nsksgqrgss sksgklkgdd
      181 lqaikkeltq ikqkvdslle slekiekeqs kqadlsfssp vemkneksee eqssasvkkd
      241 etnvkmesea gaddsaeegd llddddnedr gddqlelkdd ekepeegedd rdsangedds
//
LOCUS       NP_001257887             459 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor ROR-beta [Rattus norvegicus].
ACCESSION   NP_001257887 XP_219749
VERSION     NP_001257887.1
DBSOURCE    REFSEQ: accession NM_001270958.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Rudolf,G., Lesca,G., Mehrjouy,M.M., Labalme,A., Salmi,M., Bache,I.,
            Bruneau,N., Pendziwiat,M., Fluss,J., de Bellescize,J., Scholly,J.,
            Moller,R.S., Craiu,D., Tommerup,N., Valenti-Hirsch,M.P.,
            Schluth-Bolard,C., Sloan-Bena,F., Helbig,K.L., Weckhuysen,S.,
            Edery,P., Coulbaut,S., Abbas,M., Scheffer,I.E., Tang,S.,
            Myers,C.T., Stamberger,H., Carvill,G.L., Shinde,D.N., Mefford,H.C.,
            Neagu,E., Huether,R., Lu,H.M., Dica,A., Cohen,J.S., Iliescu,C.,
            Pomeran,C., Rubenstein,J., Helbig,I., Sanlaville,D., Hirsch,E. and
            Szepetowski,P.
  TITLE     Loss of function of the retinoid-related nuclear receptor (RORB)
            gene and epilepsy
  JOURNAL   Eur J Hum Genet 24 (12), 1761-1770 (2016)
   PUBMED   27352968
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Liu,H., Kim,S.Y., Fu,Y., Wu,X., Ng,L., Swaroop,A. and Forrest,D.
  TITLE     An isoform of retinoid-related orphan receptor beta directs
            differentiation of retinal amacrine and horizontal interneurons
  JOURNAL   Nat Commun 4, 1813 (2013)
   PUBMED   23652001
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Roforth,M.M., Liu,G., Khosla,S. and Monroe,D.G.
  TITLE     Examination of nuclear receptor expression in osteoblasts reveals
            Rorbeta as an important regulator of osteogenesis
  JOURNAL   J Bone Miner Res 27 (4), 891-901 (2012)
   PUBMED   22189870
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Jia,L., Oh,E.C., Ng,L., Srinivas,M., Brooks,M., Swaroop,A. and
            Forrest,D.
  TITLE     Retinoid-related orphan nuclear receptor RORbeta is an early-acting
            factor in rod photoreceptor development
  JOURNAL   Proc Natl Acad Sci U S A 106 (41), 17534-17539 (2009)
   PUBMED   19805139
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Hirokawa,J., Watakabe,A., Ohsawa,S. and Yamamori,T.
  TITLE     Analysis of area-specific expression patterns of RORbeta, ER81 and
            Nurr1 mRNAs in rat neocortex by double in situ hybridization and
            cortical box method
  JOURNAL   PLoS One 3 (9), e3266 (2008)
   PUBMED   18815614
  REMARK    GeneRIF: RORbeta, ER81 and Nurr1 are expressed in rat neocortex
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Andre,E., Gawlas,K. and Becker-Andre,M.
  TITLE     A novel isoform of the orphan nuclear receptor RORbeta is
            specifically expressed in pineal gland and retina
  JOURNAL   Gene 216 (2), 277-283 (1998)
   PUBMED   9729429
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Park,H.T., Baek,S.Y., Kim,B.S., Kim,J.B. and Kim,J.J.
  TITLE     Developmental expression of 'RZR beta, a putative nuclear-melatonin
            receptor' mRNA in the suprachiasmatic nucleus of the rat
  JOURNAL   Neurosci Lett 217 (1), 17-20 (1996)
   PUBMED   8905729
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Becker-Andre,M., Wiesenberg,I., Schaeren-Wiemers,N., Andre,E.,
            Missbach,M., Saurat,J.H. and Carlberg,C.
  TITLE     Pineal gland hormone melatonin binds and activates an orphan of the
            nuclear receptor superfamily
  JOURNAL   J Biol Chem 269 (46), 28531-28534 (1994)
   PUBMED   7961794
  REMARK    Erratum:[J Biol Chem 1997 Jun 27;272(26):16707]
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Carlberg,C., Hooft van Huijsduijnen,R., Staple,J.K.,
            DeLamarter,J.F. and Becker-Andre,M.
  TITLE     RZRs, a new family of retinoid-related orphan receptors that
            function as both monomers and homodimers
  JOURNAL   Mol Endocrinol 8 (6), 757-770 (1994)
   PUBMED   7935491
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Becker-Andre,M., Andre,E. and DeLamarter,J.F.
  TITLE     Identification of nuclear receptor mRNAs by RT-PCR amplification of
            conserved zinc-finger motif sequences
  JOURNAL   Biochem Biophys Res Commun 194 (3), 1371-1379 (1993)
   PUBMED   7916608
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 15, 2012 this sequence version replaced XP_219749.3.
            
            Summary: The protein encoded by this gene is a member of the NR1
            subfamily of nuclear hormone receptors. It is a DNA-binding protein
            that can bind as a monomer or as a homodimer to hormone response
            elements upstream of several genes to enhance the expression of
            those genes. The encoded protein has been shown to interact with
            NM23-2, a nucleoside diphosphate kinase involved in organogenesis
            and differentiation, and to help regulate the expression of some
            genes involved in circadian rhythm. [provided by RefSeq, Feb 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.7456.1,
                                           SRR26360194.1603623.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..459
                     /product="nuclear receptor ROR-beta"
                     /note="nuclear receptor RZR-beta; retinoid-related orphan
                     receptor-beta; nuclear receptor subfamily 1 group F member
                     2; RAR-related orphan receptor beta; transcription factor"
                     /calculated_mol_wt=51897
     Region          3..97
                     /region_name="NR_DBD_ROR"
                     /note="DNA-binding domain of Retinoid-related orphan
                     receptors (RORs) is composed of two C4-type zinc fingers;
                     cd06968"
                     /db_xref="CDD:143526"
     Site            order(10,13,27,30,46,52,62,65)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143526"
     Site            order(20..22,28..29,31,33,36,39,59..60,63,66,77,80)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143526"
     Region          210..450
                     /region_name="NR_LBD_ROR_like"
                     /note="The ligand binding domain of Retinoid-related
                     orphan receptors, of the nuclear receptor superfamily;
                     cd06939"
                     /db_xref="CDD:132737"
     Site            order(227..229,259,262..263,265..266,269,303,306..307,
                     309..310,318..320,330,333,342,423)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132737"
     Site            order(278,288,291..292,295..296,444..445,448..449)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132737"
     CDS             1..459
                     /gene="Rorb"
                     /coded_by="NM_001270958.1:626..2005"
                     /db_xref="GeneID:309288"
                     /db_xref="RGD:1306778"
ORIGIN      
        1 mraqievipc kicgdkssgi hygvitcegc kgffrrsqqn nasyscprqr nclidrtnrn
       61 rcqhcrlqkc lalgmsrdav kfgrmskkqr dslyaevqkh qqrlqeqrqq qsgeaealar
      121 vysssisngl snlntetggt yanghvidlp ksegyynids gqpspdqsgl dmtgikqikq
      181 epiydltsvp nlftyssfnn gqlapgitms eidriaqnii kshletcqyt meelhqlawq
      241 thtyeeikay qsksrealwq qcaiqithai qyvvefakri tgfmelcqnd qilllksgcl
      301 evvlvrmcra fnplnntvlf egkyggmqmf kalgsddlvn eafdfaknlc slqlteeeia
      361 lfssavlisp drawlleprk vqklqekiyf alqhviqknh lddetlakli akiptitavc
      421 nlhgeklqvf kqshpdivnt lfpplykelf npdcaavck
//
LOCUS       NP_001094107             574 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM23 [Rattus norvegicus].
ACCESSION   NP_001094107 XP_001064021 XP_001064069 XP_342184
VERSION     NP_001094107.1
DBSOURCE    REFSEQ: accession NM_001100637.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Chen,J., Zhang,R., Li,F., Lin,S. and Wang,J.
  TITLE     Integrated analysis and validation of TRIM23/p53 signaling pathway
            in hepatic stellate cells ferroptosis and liver fibrosis
  JOURNAL   Dig Liver Dis 56 (2), 281-290 (2024)
   PUBMED   37495427
  REMARK    GeneRIF: Integrated analysis and validation of TRIM23/p53 signaling
            pathway in hepatic stellate cells ferroptosis and liver fibrosis.
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Xue,W., Zhao,Y., Xiao,Z., Wu,X., Ma,D., Han,J., Li,X., Xue,X.,
            Yang,Y., Fang,Y., Fan,C., Liu,S., Xu,B., Han,S., Chen,B., Zhang,H.,
            Fan,Y., Liu,W., Dong,Q. and Dai,J.
  TITLE     Epidermal growth factor receptor-extracellular-regulated kinase
            blockade upregulates TRIM32 signaling cascade and promotes
            neurogenesis after spinal cord injury
  JOURNAL   Stem Cells 38 (1), 118-133 (2020)
   PUBMED   31621984
  REMARK    GeneRIF: Epidermal growth factor receptor-extracellular-regulated
            kinase blockade upregulates TRIM32 signaling cascade and promotes
            neurogenesis after spinal cord injury.
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Vichi,A., Payne,D.M., Pacheco-Rodriguez,G., Moss,J. and Vaughan,M.
  TITLE     E3 ubiquitin ligase activity of the trifunctional ARD1
            (ADP-ribosylation factor domain protein 1)
  JOURNAL   Proc Natl Acad Sci U S A 102 (6), 1945-1950 (2005)
   PUBMED   15684077
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Vitale,N., Horiba,K., Ferrans,V.J., Moss,J. and Vaughan,M.
  TITLE     Localization of ADP-ribosylation factor domain protein 1 (ARD1) in
            lysosomes and Golgi apparatus
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8613-8618 (1998)
   PUBMED   9671726
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Vitale,N., Moss,J. and Vaughan,M.
  TITLE     ARD1, a 64-kDa bifunctional protein containing an 18-kDa
            GTP-binding ADP-ribosylation factor domain and a 46-kDa
            GTPase-activating domain
  JOURNAL   Proc Natl Acad Sci U S A 93 (5), 1941-1944 (1996)
   PUBMED   8700863
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Mishima,K., Tsuchiya,M., Nightingale,M.S., Moss,J. and Vaughan,M.
  TITLE     ARD 1, a 64-kDa guanine nucleotide-binding protein with a
            carboxyl-terminal ADP-ribosylation factor domain
  JOURNAL   J Biol Chem 268 (12), 8801-8807 (1993)
   PUBMED   8473324
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB696360.1, FM052834.1, L04760.1, CK470479.1, FM085917.1,
            DV726798.1 and AA965268.1.
            
            On or before May 22, 2010 this sequence version replaced
            XP_342184.4, XP_001064069.1, XP_001064021.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L04760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132284, SAMD00132290
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..574
                     /product="E3 ubiquitin-protein ligase TRIM23"
                     /EC_number="2.3.2.27"
                     /note="GTP-binding protein ARD-1; tripartite
                     motif-containing protein 23; ADP-ribosylation factor
                     domain-containing protein 1; nucleotide binding protein;
                     tripartite motif protein 23; ADP-ribosylation factor
                     domain protein 1, 64kD; RING-type E3 ubiquitin transferase
                     TRIM23"
                     /calculated_mol_wt=63925
     Region          28..77
                     /region_name="mRING-HC-C3HC3D_TRIM23_C-IX"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tripartite motif-containing protein 23 (TRIM23)
                     and similar proteins; cd16645"
                     /db_xref="CDD:438307"
     Region          123..172
                     /region_name="Bbox2_TRIM23_C-IX_rpt1"
                     /note="first B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 23 (TRIM23) and similar proteins;
                     cd19773"
                     /db_xref="CDD:380831"
     Region          174..223
                     /region_name="Bbox2_TRIM23_C-IX_rpt2"
                     /note="second B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 23 (TRIM23) and similar proteins;
                     cd19774"
                     /db_xref="CDD:380832"
     Region          226..370
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          391..574
                     /region_name="ARF-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P36407.2)"
     Region          406..574
                     /region_name="ARD1"
                     /note="(ADP-ribosylation factor domain protein 1 (ARD1);
                     cd04158"
                     /db_xref="CDD:206723"
     Site            411..418
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206723"
     Site            order(413..419,434..435,457,513..514,516,547..549)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206723"
     Site            order(413..414,418,422,434..441,463,468)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206723"
     Site            423..438
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206723"
     Site            order(435..439,444,454,458,464,466..468)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206723"
     Site            435
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206723"
     Site            order(436..443,453,464,467..468)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206723"
     Site            439..453
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206723"
     Site            order(445..448,555..558)
                     /site_type="other"
                     /note="YxxL localization motifs"
                     /db_xref="CDD:206723"
     Site            454..471
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206723"
     Site            454..457
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206723"
     Site            513..516
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206723"
     Site            547..549
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206723"
     CDS             1..574
                     /gene="Trim23"
                     /gene_synonym="Ard1; Arfd1"
                     /coded_by="NM_001100637.1:90..1814"
                     /db_xref="GeneID:81002"
                     /db_xref="RGD:621587"
ORIGIN      
        1 maalavnkpg agvdsgrqgs rgtavvkvle cgvcedvfsl qgdkvprlll cghtvchdcl
       61 srlplhgrai rcpfdrqvtd lgdsgvwglk knfallelle rlqnghigqy gaaeealgis
      121 gesiircded eahvasvyct vcathlcsec sqvthstktl akhrrvplad kphektmccq
      181 hqvhaiefvc leeacqtspl mccvckeygk hqghkhsvle peanqirasi ldmahcirtf
      241 teeisdysrk lvgivqhieg geqivedgig mahtehvpgt aenarscvra yfsdlhetlc
      301 rqeemalsvv dahvrekliw lrqqqedmti llsqvstacl hcektlqqdd crvvlakqei
      361 trlletlqkq qqqftevadh iqldasipvt ftkdnrvyig pkmeirvvtl gldgagktti
      421 lfklkqdefm qpiptigfnv etveyknlkf tiwdvgekhk lrplwkhyyl ntqavvfvvd
      481 sshrdrisea hselakllte kelrdallli fankqdvaga lsveeitell slhklccgrs
      541 wyiqgcdars gmglyegldw lsrqlvaagv ldva
//
LOCUS       NP_001070021             109 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor beta isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001070021
VERSION     NP_001070021.1
DBSOURCE    REFSEQ: accession NM_001076553.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Cerone,M.A., Burgess,D.J., Naceur-Lombardelli,C., Lord,C.J. and
            Ashworth,A.
  TITLE     High-throughput RNAi screening reveals novel regulators of
            telomerase
  JOURNAL   Cancer Res 71 (9), 3328-3340 (2011)
   PUBMED   21531765
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Dahia,C.L. and Rao,A.J.
  TITLE     Regulation of FSH receptor, PKIbeta, IL-6 and calcium mobilization:
            Possible mediators of differential action of FSH
  JOURNAL   Mol Cell Endocrinol 247 (1-2), 73-81 (2006)
   PUBMED   16406266
  REMARK    GeneRIF: PKIbeta and calcium, which are the downstream signaling
            molecules, are involved in FSH regulated Sertoli cells
            proliferation.
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Kumar,P. and Walsh,D.A.
  TITLE     A dual-specificity isoform of the protein kinase inhibitor PKI
            produced by alternate gene splicing
  JOURNAL   Biochem J 362 (Pt 3), 533-537 (2002)
   PUBMED   11879178
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Andoh,Y., Kuramoto,T., Yokoi,N., Maihara,T., Kitada,K. and
            Serikawa,T.
  TITLE     Correlation between genetic and cytogenetic maps of the rat
  JOURNAL   Mamm Genome 9 (4), 287-293 (1998)
   PUBMED   9530624
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Baude,E.J., Dignam,S.S., Olsen,S.R., Reimann,E.M. and Uhler,M.D.
  TITLE     Glutamic acid 203 of the cAMP-dependent protein kinase catalytic
            subunit participates in the inhibition by two isoforms of the
            protein kinase inhibitor
  JOURNAL   J Biol Chem 269 (3), 2316-2323 (1994)
   PUBMED   7905001
REFERENCE   7  (residues 1 to 109)
  AUTHORS   Van Patten,S.M., Ng,D.C., Th'ng,J.P., Angelos,K.L., Smith,A.J. and
            Walsh,D.A.
  TITLE     Molecular cloning of a rat testis form of the inhibitor protein of
            cAMP-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5383-5387 (1991)
   PUBMED   2052616
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG666532.1, BG668634.1, BC078880.1 and FQ231722.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF413572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..109
                     /product="cAMP-dependent protein kinase inhibitor beta
                     isoform 1"
                     /note="PKI-beta; protein kinase inhibitor beta, cAMP
                     dependent, testis specific; protein kinase
                     (cAMP-dependent, catalytic) inhibitor beta; cAMP-dependent
                     protein kinase (catalytic subunit binding) inhibtor 2;
                     protein kinase inhibitor beta, cAMP dependent, catalytic;
                     protein kinase inhibitor beta, (cAMP-dependent, catalytic)
                     inhibitor beta; protein kinase inhibitor, beta"
                     /calculated_mol_wt=11295
     Region          40..108
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     CDS             1..109
                     /gene="Pkib"
                     /gene_synonym="PKINH; Prkacn2; RATPKINH"
                     /coded_by="NM_001076553.2:290..619"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24678"
                     /db_xref="RGD:3335"
ORIGIN      
        1 mdvhpdapgg qkktvengmg ggspgaqqds vmrtdssemt dvesvissfa ssaragrrna
       61 lpdiqsslat ggspdlalkl ealavkedak mkneekdqgq pkkpldedk
//
LOCUS       NP_113989                565 aa            linear   ROD 27-APR-2025
DEFINITION  deformed epidermal autoregulatory factor 1 homolog [Rattus
            norvegicus].
ACCESSION   NP_113989
VERSION     NP_113989.2
DBSOURCE    REFSEQ: accession NM_031801.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Szewczyk,B., Kotarska,K., Daigle,M., Misztak,P., Sowa-Kucma,M.,
            Rafalo,A., Curzytek,K., Kubera,M., Basta-Kaim,A., Nowak,G. and
            Albert,P.R.
  TITLE     Stress-induced alterations in 5-HT1A receptor transcriptional
            modulators NUDR and Freud-1
  JOURNAL   Int J Neuropsychopharmacol 17 (11), 1763-1775 (2014)
   PUBMED   24946016
  REMARK    GeneRIF: In pregnancy stress, prefrontal cortex Deaf1 levels were
            reduced in rats.
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Vulto-van Silfhout,A.T., Rajamanickam,S., Jensik,P.J., Vergult,S.,
            de Rocker,N., Newhall,K.J., Raghavan,R., Reardon,S.N., Jarrett,K.,
            McIntyre,T., Bulinski,J., Ownby,S.L., Huggenvik,J.I.,
            McKnight,G.S., Rose,G.M., Cai,X., Willaert,A., Zweier,C.,
            Endele,S., de Ligt,J., van Bon,B.W., Lugtenberg,D., de Vries,P.F.,
            Veltman,J.A., van Bokhoven,H., Brunner,H.G., Rauch,A., de
            Brouwer,A.P., Carvill,G.L., Hoischen,A., Mefford,H.C.,
            Eichler,E.E., Vissers,L.E., Menten,B., Collard,M.W. and de
            Vries,B.B.
  TITLE     Mutations affecting the SAND domain of DEAF1 cause intellectual
            disability with severe speech impairment and behavioral problems
  JOURNAL   Am J Hum Genet 94 (5), 649-661 (2014)
   PUBMED   24726472
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Kieran,N., Ou,X.M. and Iyo,A.H.
  TITLE     Chronic social defeat downregulates the 5-HT1A receptor but not
            Freud-1 or NUDR in the rat prefrontal cortex
  JOURNAL   Neurosci Lett 469 (3), 380-384 (2010)
   PUBMED   20026183
  REMARK    GeneRIF: chronic social defeat stress downregulates the 5-HT1A
            receptor mRNA but does not significantly alter the levels of
            Freud-1 and NUDR in PFC; this stress paradigm could offer a useful
            rodent model for depression and other stress related disorders
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Iyo,A.H., Kieran,N., Chandran,A., Albert,P.R., Wicks,I.,
            Bissette,G. and Austin,M.C.
  TITLE     Differential regulation of the serotonin 1 A transcriptional
            modulators five prime repressor element under dual repression-1 and
            nuclear-deformed epidermal autoregulatory factor by chronic stress
  JOURNAL   Neuroscience 163 (4), 1119-1127 (2009)
   PUBMED   19647046
  REMARK    GeneRIF: results point to the importance of understanding the
            mechanism for the differential regulation of 5-HT1AR, Freud-1 and
            NUDR in the prefrontal cortex as a basis for understanding the
            related effects of chronic stress and stress-related disorders
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Yip,L., Su,L., Sheng,D., Chang,P., Atkinson,M., Czesak,M.,
            Albert,P.R., Collier,A.R., Turley,S.J., Fathman,C.G. and
            Creusot,R.J.
  TITLE     Deaf1 isoforms control the expression of genes encoding peripheral
            tissue antigens in the pancreatic lymph nodes during type 1
            diabetes
  JOURNAL   Nat Immunol 10 (9), 1026-1033 (2009)
   PUBMED   19668219
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Barker,H.E., Smyth,G.K., Wettenhall,J., Ward,T.A., Bath,M.L.,
            Lindeman,G.J. and Visvader,J.E.
  TITLE     Deaf-1 regulates epithelial cell proliferation and side-branching
            in the mammary gland
  JOURNAL   BMC Dev Biol 8, 94 (2008)
   PUBMED   18826651
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Hahm,K., Sum,E.Y., Fujiwara,Y., Lindeman,G.J., Visvader,J.E. and
            Orkin,S.H.
  TITLE     Defective neural tube closure and anteroposterior patterning in
            mice lacking the LIM protein LMO4 or its interacting partner Deaf-1
  JOURNAL   Mol Cell Biol 24 (5), 2074-2082 (2004)
   PUBMED   14966286
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Sugihara,T.M., Bach,I., Kioussi,C., Rosenfeld,M.G. and Andersen,B.
  TITLE     Mouse deformed epidermal autoregulatory factor 1 recruits a LIM
            domain factor, LMO-4, and CLIM coregulators
  JOURNAL   Proc Natl Acad Sci U S A 95 (26), 15418-15423 (1998)
   PUBMED   9860983
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Huggenvik,J.I., Michelson,R.J., Collard,M.W., Ziemba,A.J.,
            Gurley,P. and Mowen,K.A.
  TITLE     Characterization of a nuclear deformed epidermal autoregulatory
            factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein
  JOURNAL   Mol Endocrinol 12 (10), 1619-1639 (1998)
   PUBMED   9773984
REFERENCE   10 (residues 1 to 565)
  AUTHORS   LeBoeuf,R.D., Ban,E.M., Green,M.M., Stone,A.S., Propst,S.M.,
            Blalock,J.E. and Tauber,J.D.
  TITLE     Molecular cloning, sequence analysis, expression, and tissue
            distribution of suppressin, a novel suppressor of cell cycle entry
  JOURNAL   J Biol Chem 273 (1), 361-368 (1998)
   PUBMED   9417089
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On May 28, 2015 this sequence version replaced NP_113989.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF055884.1, U59659.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMEA5760476 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..565
                     /product="deformed epidermal autoregulatory factor 1
                     homolog"
                     /note="nuclear DEAF-1-related transcriptional regulator;
                     suppressin; DEAF-1 related transcriptional regulator
                     (NUDR)"
                     /calculated_mol_wt=59431
     Region          29..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88450.1)"
     Region          162..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88450.1)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T5; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T5; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Region          201..273
                     /region_name="SAND"
                     /note="SAND domain; smart00258"
                     /db_xref="CDD:128554"
     Region          301..316
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O88450.1)"
     Region          403..478
                     /region_name="Interaction with LMO4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O88450.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75398; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (O88450.1)"
     Region          504..540
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..565
                     /gene="Deaf1"
                     /gene_synonym="NUDR"
                     /coded_by="NM_031801.2:103..1800"
                     /db_xref="GeneID:83632"
                     /db_xref="RGD:620671"
ORIGIN      
        1 medsdsaakq lglaeaaava aaaavaaaaa aaaeseaeep vlsrdedsee dadseaeret
       61 rrvtavavma aesghmdmgt ealpspdeaa aaaafaevtt vtvanvgssa dnvfttsvan
      121 aasisghvls grtalqigds lntekatliv vhtdgsivet tglkgpaapl tpgpqspptp
      181 lapgqekggt kynwdpsvyd selpvrcrni sgtlyksrlg sggrgrcikq genwysptef
      241 eamagrassk dwkrsiryag rplqcliqdg ilnphaasct caaccddmtl sgpvrlfvpy
      301 krrkkenelp ttpvkkdspk nitllpataa ttftvtpsgq ittsgaltfd rastveatav
      361 isespaqgdv fagatvqeag vqppcrvghp ephypgyqds cqiapfpeaa lptshpkivl
      421 tslpalavpp stptkavspt vvsglemseh rswlyleemv nsllntaqql ktlfeqakqa
      481 sscreaavtq armqvdaerk eqscvncgre amsectgchk vnycstfcqr kdwkdhqhvc
      541 gqsasvtvqa ddvhveesvi ekvtv
//
LOCUS       NP_001162001             801 aa            linear   ROD 27-APR-2025
DEFINITION  glycerol-3-phosphate acyltransferase 2, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001162001 XP_001078526 XP_238283
VERSION     NP_001162001.1
DBSOURCE    REFSEQ: accession NM_001168529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Shiromoto,Y., Kuramochi-Miyagawa,S., Daiba,A., Chuma,S.,
            Katanaya,A., Katsumata,A., Nishimura,K., Ohtaka,M., Nakanishi,M.,
            Nakamura,T., Yoshinaga,K., Asada,N., Nakamura,S., Yasunaga,T.,
            Kojima-Kita,K., Itou,D., Kimura,T. and Nakano,T.
  TITLE     GPAT2, a mitochondrial outer membrane protein, in piRNA biogenesis
            in germline stem cells
  JOURNAL   RNA 19 (6), 803-810 (2013)
   PUBMED   23611983
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Cattaneo,E.R., Pellon-Maison,M., Rabassa,M.E., Lacunza,E.,
            Coleman,R.A. and Gonzalez-Baro,M.R.
  TITLE     Glycerol-3-phosphate acyltransferase-2 is expressed in spermatic
            germ cells and incorporates arachidonic acid into triacylglycerols
  JOURNAL   PLoS One 7 (8), e42986 (2012)
   PUBMED   22905194
  REMARK    GeneRIF: GPAT2 expression is linked to arachidonoyl-CoA
            incorporation into TAG in spermatogenic germ cells
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Chen,Y.Q., Kuo,M.S., Li,S., Bui,H.H., Peake,D.A., Sanders,P.E.,
            Thibodeaux,S.J., Chu,S., Qian,Y.W., Zhao,Y., Bredt,D.S.,
            Moller,D.E., Konrad,R.J., Beigneux,A.P., Young,S.G. and Cao,G.
  TITLE     AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase
  JOURNAL   J Biol Chem 283 (15), 10048-10057 (2008)
   PUBMED   18238778
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Wang,S., Lee,D.P., Gong,N., Schwerbrock,N.M., Mashek,D.G.,
            Gonzalez-Baro,M.R., Stapleton,C., Li,L.O., Lewin,T.M. and
            Coleman,R.A.
  TITLE     Cloning and functional characterization of a novel mitochondrial
            N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase
            (GPAT2)
  JOURNAL   Arch Biochem Biophys 465 (2), 347-358 (2007)
   PUBMED   17689486
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Lewin,T.M., Schwerbrock,N.M., Lee,D.P. and Coleman,R.A.
  TITLE     Identification of a new glycerol-3-phosphate acyltransferase
            isoenzyme, mtGPAT2, in mitochondria
  JOURNAL   J Biol Chem 279 (14), 13488-13495 (2004)
   PUBMED   14724270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Dec 12, 2009 this sequence version replaced
            XP_238283.4, XP_001078526.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.962635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..801
                     /product="glycerol-3-phosphate acyltransferase 2,
                     mitochondrial"
                     /EC_number="2.3.1.51"
                     /EC_number="2.3.1.15"
                     /note="1-acylglycerol-3-phosphate O-acyltransferase GPAT2"
                     /calculated_mol_wt=88839
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZI76.1)"
     Region          176..387
                     /region_name="LPLAT_DHAPAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: GPAT-like; cd07993"
                     /db_xref="CDD:153255"
     Region          180..290
                     /region_name="Acyltransferase.
                     /evidence=ECO:0000250|UniProtKB:Q14DK4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZI76.1)"
     Site            order(205,208,210,231..234,291..293)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153255"
     Region          205..210
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q14DK4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZI76.1)"
     Site            306..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZI76.1)"
     Site            450..472
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZI76.1)"
     Region          <470..527
                     /region_name="ZF_RNaseIII_KREN_KREPB-like"
                     /note="C2H2 zinc finger and Ribonuclease III-like domain
                     of RNA-editing catalytic complex (RECC) proteins KREN1-3,
                     KREPB4-KREPB10, and related proteins; cl49632"
                     /db_xref="CDD:483972"
     CDS             1..801
                     /gene="Gpat2"
                     /gene_synonym="RGD1304904"
                     /coded_by="NM_001168529.1:66..2471"
                     /db_xref="GeneID:296130"
                     /db_xref="RGD:1304904"
ORIGIN      
        1 metmlksnpq mqqrnnhsgq etslwssgfg mkmeaitpfl gkyrpfmgrc cqtctpkswe
       61 slfhrsimdl gfcnvilvke entrfrgwlv rrlcyflwsl eqhiptssda sqmimentgv
      121 qnillgkvpg aagegqapdl vkkevqrilg hiqttprpfl lrlfswallw flnrlflnvq
      181 lhkgqmkmvh kaaqegsplv flsthkslld gfllpfvlfs qglgvlrval dsrtcspalr
      241 allrklgglf lppeanlsld ssegilarav vratveqllt sgqpllifle eapgypgprl
      301 salgqawlgl vvqavqagiv pdatlvpvat aydlvpdapc nmthdlaplg lwtgalaifr
      361 rlcncwgcnr rvcvrvhlaq pfslqeytin arscwgsrqt lehllqpivl gecsvvpdte
      421 keqewtppts lllalkeedq llvrrlsrhv lsasvassav mstaimatll llkhqkgvvl
      481 sqllgefswl teetllrgfd vgfsgqlrcl aqhtlsllra hvvllrvhqg dlvvvprpgp
      541 glthlarlsm ellptflsea vgacavrgll agrvppegpw elqgiellsq nelyrqilll
      601 lhllpqdlll pqpcqssycy cqevldrliq cgllvaeetp gsrpacdtgr qhlsakllwk
      661 psgdftdses ddfeepggrc frlsqqsrcp dfflflcrll spilkafaqa atflhlgqlp
      721 dsevgysekl lqflqacaqe egifecadpn laisaiwtfk dlgvlqqips ptgpqlhlsp
      781 tfasrdnqdk leqfirqfic s
//
LOCUS       NP_445802                670 aa            linear   ROD 27-APR-2025
DEFINITION  alkyldihydroxyacetonephosphate synthase, peroxisomal [Rattus
            norvegicus].
ACCESSION   NP_445802 XP_575153
VERSION     NP_445802.2
DBSOURCE    REFSEQ: accession NM_053350.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Roth,A.D., Leisewitz,A.V., Jung,J.E., Cassina,P., Barbeito,L.,
            Inestrosa,N.C. and Bronfman,M.
  TITLE     PPAR gamma activators induce growth arrest and process extension in
            B12 oligodendrocyte-like cells and terminal differentiation of
            cultured oligodendrocytes
  JOURNAL   J Neurosci Res 72 (4), 425-435 (2003)
   PUBMED   12704804
REFERENCE   6  (residues 1 to 670)
  AUTHORS   de Vet,E.C., Ijlst,L., Oostheim,W., Wanders,R.J. and van den
            Bosch,H.
  TITLE     Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome
            biogenesis disorders and identification of the point mutation
            underlying a single enzyme deficiency
  JOURNAL   J Biol Chem 273 (17), 10296-10301 (1998)
   PUBMED   9553082
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Zomer,A.W., de Weerd,W.F., Langeveld,J. and van den Bosch,H.
  TITLE     Ether lipid synthesis: purification and identification of alkyl
            dihydroxyacetone phosphate synthase from guinea-pig liver
  JOURNAL   Biochim Biophys Acta 1170 (2), 189-196 (1993)
   PUBMED   8399344
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Gunawan,J., Rabert,U., Volkl,A. and Debuch,H.
  TITLE     Kinetic studies of alkyl-dihydroxyacetone-phosphate
            (alkyl-glycerone-phosphate) synthase in peroxisomes of rat liver
  JOURNAL   Biol Chem Hoppe Seyler 371 (4), 339-344 (1990)
   PUBMED   2340111
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Singh,H., Usher,S. and Poulos,A.
  TITLE     Dihydroxyacetone phosphate acyltransferase and
            alkyldihydroxyacetone phosphate synthase activities in rat liver
            subcellular fractions and human skin fibroblasts
  JOURNAL   Arch Biochem Biophys 268 (2), 676-686 (1989)
   PUBMED   2464339
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Lee,T.C., Fitzgerald,V., Stephens,N. and Snyder,F.
  TITLE     Activities of enzymes involved in the metabolism of ether-linked
            lipids in normal and neoplastic tissues of rat
  JOURNAL   Biochim Biophys Acta 619 (2), 420-423 (1980)
   PUBMED   7407223
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF524961.1, AF121052.1 and BM389725.1.
            
            On May 2, 2010 this sequence version replaced NP_445802.1.
            
            Sequence Note: This RefSeq record was created from mixed strain
            transcript data because no single transcript from the same strain
            was available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF121052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..670
                     /product="alkyldihydroxyacetonephosphate synthase,
                     peroxisomal"
                     /EC_number="2.5.1.26"
                     /note="alkyl-DHAP synthase; alkyldihydroxyacetone
                     phosphate synthase; alkyl-dihydroxyacetonephosphate
                     synthase"
                     /calculated_mol_wt=74030
     Region          174..664
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     CDS             1..670
                     /gene="Agps"
                     /gene_synonym="Adap-s; Adps; Ads"
                     /coded_by="NM_053350.2:18..2030"
                     /db_xref="GeneID:84114"
                     /db_xref="RGD:620364"
ORIGIN      
        1 mvargaalsd lspapsglgr qhkaeamaea ageagaserd pdavrarrrl rvlsghllgr
       61 pqeapstnec karraasaag aspaaspaap esgtipkkrq elmkwngwgy ndskfllnkk
      121 gqveltgkry plsglalptl kdwiqntlgv nlehkttskp sinpseapps ivnedflqel
      181 keahisysqd addrvfrahg hclheifllr egmferipdi vvwptchddv vkivnlacky
      241 nlciipiggg tsvsyglmcp adetrtiisl dtsqmnrilw vdennltahv eagitgqdle
      301 rqlkesgyct ghepdslefs ivggwistra sgmkknvygn iedlvvhmkm vtprgvieks
      361 sqgprmstgp dihhfimgse gtlgviteat ikirptpeyq kygsvafpnf eqgvaclrei
      421 akqrcapasi rlmdnqqfqf ghalkpqvss iftsfldgfk kfyitkfkgf dpnqisvatl
      481 lfegdrekvl qhekqvydia akfgglaage dngqrgyllt yviaymrdlg leyyvvgesf
      541 etsapwdrvi dlcrnvkeri rreckergvq faplstcrvt qtydagaciy fyfafnyrgi
      601 sdpltvfeqt eaaardeila nggslshhhg vgklrkqwlk esisdvgfgm lksvkdyvdp
      661 snifgnrnll
//
LOCUS       NP_001257691             492 aa            linear   ROD 27-APR-2025
DEFINITION  ribonuclease inhibitor isoform a [Rattus norvegicus].
ACCESSION   NP_001257691
VERSION     NP_001257691.1
DBSOURCE    REFSEQ: accession NM_001270762.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Zhao,C., Ni,Y., Liu,Y., Liu,T., Yang,S., Liu,Z. and Liu,S.
  TITLE     Identification and distribution of rRNH1, a gene upregulated after
            spinal cord primary neuron injury
  JOURNAL   In Vitro Cell Dev Biol Anim 50 (3), 183-187 (2014)
   PUBMED   24288130
  REMARK    GeneRIF: RNH1 protein is upregulated after spinal cord injury.
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Zhao,C.F., Liu,Y., Que,H.P., Yang,S.G., Liu,T., Liu,Z.Q., Hui,H.D.
            and Liu,S.
  TITLE     Rnh1 promotes differentiation and myelination via RhoA in
            oligodendrocytes
  JOURNAL   Cell Tissue Res 353 (3), 381-389 (2013)
   PUBMED   23624614
  REMARK    GeneRIF: Rnh1-mediated RhoA inactivation enhances the
            differentiation and myelination in oligodendrocytes.
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Kawanomoto,M., Motojima,K., Sasaki,M., Hattori,H. and Goto,S.
  TITLE     cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue
            distribution of the mRNA
  JOURNAL   Biochim Biophys Acta 1129 (3), 335-338 (1992)
   PUBMED   1536887
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Shapiro,R. and Vallee,B.L.
  TITLE     Human placental ribonuclease inhibitor abolishes both angiogenic
            and ribonucleolytic activities of angiogenin
  JOURNAL   Proc Natl Acad Sci U S A 84 (8), 2238-2241 (1987)
   PUBMED   3470787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC070501.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X62528.1, SRR26643292.4647.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..492
                     /product="ribonuclease inhibitor isoform a"
                     /note="ribonuclease inhibitor"
                     /calculated_mol_wt=54003
     Region          37..356
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     Region          38..60
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(39,41,44,46,61,64,66,69,71,89,92,94,97,99,118,121,
                     123,126,128,146,149,151,154,156,175,178,180,183,185,203,
                     206,208,211,213,232,235,237,240,242,260,263,265,268,270,
                     289,292,294,297,299,317,320,322,325,327,346,349,351,354,
                     356)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          61..88
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(67..68,125,182,210,267,293,295,321,350)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          89..113
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          118..145
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          146..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          203..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          232..259
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          260..288
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          289..309
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <313..>455
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          317..336
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          374..402
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          403..430
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..492
                     /gene="Rnh1"
                     /gene_synonym="Rnh"
                     /coded_by="NM_001270762.1:11..1489"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:100360501"
                     /db_xref="RGD:621398"
ORIGIN      
        1 mfwgsrlplr vffgslpgll ntwqsvwtrr lhcaptmsld iqceqlsdar wtellpliqq
       61 yqvvrlddcg ltevrckdir saiqanpalt elslrtnelg dagvglvlqg lqnptckiqk
      121 lslqncslte agcgvlpdvl rslstlrelh lndnplgdeg lkllceglrd pqcrleklql
      181 eycnltatsc eplasvlrvk pdfkelvlsn ndfheagiht lcqglkdsac qleslklenc
      241 gitsanckdl cdvvaskasl qeldlgsnkl gntgiaalcs glllpscrlr tlwlwdcdvt
      301 aegckdlcrv lrakqslkel slagnelkde gaqllcesll epgcqleslw vktcsltaas
      361 cphfcsvltk nrslfelqms snplgdsgvv elckalgypd tvlrvlwlgd cdvtdsgcss
      421 latvllanrs lreldlsnnc mgdtgvlqll eslkqpscal qqlvlydiyw tdevedqlra
      481 leeerpslri is
//
LOCUS       NP_071516                474 aa            linear   ROD 27-APR-2025
DEFINITION  hepatocyte nuclear factor 4-alpha isoform 1 [Rattus norvegicus].
ACCESSION   NP_071516
VERSION     NP_071516.2
DBSOURCE    REFSEQ: accession NM_022180.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Melis,M., Marino,R., Tian,J., Johnson,C., Sethi,R., Oertel,M.,
            Fox,I.J. and Locker,J.
  TITLE     Mechanism and Effect of HNF4alpha Decrease in a Rat Model of
            Cirrhosis and Liver Failure
  JOURNAL   Cell Mol Gastroenterol Hepatol 17 (3), 453-479 (2024)
   PUBMED   37993018
  REMARK    GeneRIF: Mechanism and Effect of HNF4alpha Decrease in a Rat Model
            of Cirrhosis and Liver Failure.
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Zhan,H., Zhang,Q., Zhang,C., Cheng,J., Yang,Y., Liu,C., Li,S.,
            Wang,C., Yang,J., Ge,H., Zhou,D., Li,B., Wei,H. and Hu,C.
  TITLE     Targeted Activation of HNF4alpha by AMPK Inhibits Apoptosis and
            Ameliorates Neurological Injury Caused by Cardiac Arrest in Rats
  JOURNAL   Neurochem Res 48 (10), 3129-3145 (2023)
   PUBMED   37338793
  REMARK    GeneRIF: Targeted Activation of HNF4alpha by AMPK Inhibits
            Apoptosis and Ameliorates Neurological Injury Caused by Cardiac
            Arrest in Rats.
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Fan,J.Y., Dama,G., Liu,Y.L., Guo,W.Y. and Lin,J.T.
  TITLE     [Combinational Overexpression of Foxa3 and Hnf4alpha Enhance the
            Proliferation and Prolong the Functional Maintenance of Primary
            Hepatocytes]
  JOURNAL   Mol Biol (Mosk) 57 (4), 668-670 (2023)
   PUBMED   37528786
  REMARK    GeneRIF: [Combinational Overexpression of Foxa3 and Hnf4alpha
            Enhance the Proliferation and Prolong the Functional Maintenance of
            Primary Hepatocytes].
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Hu,C., Jing,R., Wen,C., Qi,T., Bai,X., Wang,Y., Shao,Y. and Pei,C.
  TITLE     HNF4A Negatively Regulated Posterior Capsular Opacification via
            Transcriptional Inhibition of MMP2
  JOURNAL   Curr Eye Res 48 (7), 627-638 (2023)
   PUBMED   36988559
  REMARK    GeneRIF: HNF4A Negatively Regulated Posterior Capsular
            Opacification via Transcriptional Inhibition of MMP2.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Zheng,X., Wang,G., Yuan,J., Li,N., Yan,B., Yan,J. and Sheng,Y.
  TITLE     hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion Injury Via
            Targeting HNF4alpha
  JOURNAL   Turk J Gastroenterol 33 (7), 596-605 (2022)
   PUBMED   35879917
  REMARK    GeneRIF: hsa-miR-34a-5p Ameliorates Hepatic Ischemia/Reperfusion
            Injury Via Targeting HNF4alpha.
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Ginsburg,G.S., Ozer,J. and Karathanasis,S.K.
  TITLE     Intestinal apolipoprotein AI gene transcription is regulated by
            multiple distinct DNA elements and is synergistically activated by
            the orphan nuclear receptor, hepatocyte nuclear factor 4
  JOURNAL   J Clin Invest 96 (1), 528-538 (1995)
   PUBMED   7615825
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Chen,W.S., Manova,K., Weinstein,D.C., Duncan,S.A., Plump,A.S.,
            Prezioso,V.R., Bachvarova,R.F. and Darnell,J.E. Jr.
  TITLE     Disruption of the HNF-4 gene, expressed in visceral endoderm, leads
            to cell death in embryonic ectoderm and impaired gastrulation of
            mouse embryos
  JOURNAL   Genes Dev 8 (20), 2466-2477 (1994)
   PUBMED   7958910
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Ang,S.L., Wierda,A., Wong,D., Stevens,K.A., Cascio,S., Rossant,J.
            and Zaret,K.S.
  TITLE     The formation and maintenance of the definitive endoderm lineage in
            the mouse: involvement of HNF3/forkhead proteins
  JOURNAL   Development 119 (4), 1301-1315 (1993)
   PUBMED   8306889
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Hata,S., Tsukamoto,T. and Osumi,T.
  TITLE     A novel isoform of rat hepatocyte nuclear factor 4 (HNF-4)
  JOURNAL   Biochim Biophys Acta 1131 (2), 211-213 (1992)
   PUBMED   1610903
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Sladek,F.M., Zhong,W.M., Lai,E. and Darnell,J.E. Jr.
  TITLE     Liver-enriched transcription factor HNF-4 is a novel member of the
            steroid hormone receptor superfamily
  JOURNAL   Genes Dev 4 (12B), 2353-2365 (1990)
   PUBMED   2279702
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM042560.1, CK483260.1, D10554.1, JAXUCZ010000003.1 and FQ095211.1.
            
            On Aug 10, 2012 this sequence version replaced NP_071516.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.10985.1,
                                           SRR26643288.16657.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..474
                     /product="hepatocyte nuclear factor 4-alpha isoform 1"
                     /note="alpha transcription factor 4; HNF-4-alpha;
                     transcription factor 14; transcription factor HNF-4;
                     nuclear receptor subfamily 2 group A member 1; TCF-14;
                     hepatic nuclear factor 4, alpha"
                     /calculated_mol_wt=52609
     Region          60..135
                     /region_name="NR_DBD_HNF4A"
                     /note="DNA-binding domain of heptocyte nuclear factor 4
                     (HNF4) is composed of two C4-type zinc fingers; cd06960"
                     /db_xref="CDD:143518"
     Site            order(60,63,77,80,96,102,112,115)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143518"
     Site            order(66,70..72,78..79,81,83,85..86,89,109..110,113,116,
                     129..131,133)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143518"
     Site            order(97,110..111,113)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:143518"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000305|PubMed:9234678; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000305|PubMed:9234678; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Region          151..373
                     /region_name="NR_LBD_HNF4_like"
                     /note="The ligand binding domain of heptocyte nuclear
                     factor 4, which is explosively expanded in nematodes;
                     cd06931"
                     /db_xref="CDD:132729"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            order(184,190,194,228,232,235,245..246,264,354..355,358)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132729"
     Site            order(199,203,213..214,216..217,220..221,368..369,
                     372..373)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132729"
     Site            order(271,292,298,312..313,316..317,320..321,331..332,
                     334..336,338..339,341..343,345..346,349)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132729"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Region          368..376
                     /region_name="9aaTAD.
                     /evidence=ECO:0000250|UniProtKB:P41235"
                     /note="propagated from UniProtKB/Swiss-Prot (P22449.3)"
     Region          413..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22449.3)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     Site            458
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P41235; propagated from
                     UniProtKB/Swiss-Prot (P22449.3)"
     CDS             1..474
                     /gene="Hnf4a"
                     /gene_synonym="Hnf4; Hnf4alpha"
                     /coded_by="NM_022180.2:141..1565"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25735"
                     /db_xref="RGD:2810"
ORIGIN      
        1 mrlsktladm dmadysaald payttlefen vqvltmgndt spseganlns snslgvsalc
       61 aicgdratgk hygasscdgc kgffrrsvrk nhmyscrfsr qcvvdkdkrn qcrycrlkkc
      121 fragmkkeav qnerdristr rssyedsslp sinallqaev lsqqitspis gingdirakr
      181 ianitdvces mkeqllvlve wakyipafce lllddqvall rahagehlll gatkrsmvfk
      241 dvlllgndyi vprhcpelae msrvsirild elvlpfqelq iddneyaclk aiiffdpdak
      301 glsdpgkikr lrsqvqvsle dyindrqyds rgrfgellll lptlqsitwq mieqiqfikl
      361 fgmakidnll qemllggsas daphahhplh phlmqehmgt nvivantmps hlsngqmcew
      421 prprgqaatp etpqpsppsg sgsesykllp gaittivkpp saipqptitk qeai
//
LOCUS       NP_001030111             243 aa            linear   ROD 27-APR-2025
DEFINITION  SOSS complex subunit B1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001030111 XP_343142
VERSION     NP_001030111.2
DBSOURCE    REFSEQ: accession NM_001034939.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Pandita,R.K., Chow,T.T., Udayakumar,D., Bain,A.L., Cubeddu,L.,
            Hunt,C.R., Shi,W., Horikoshi,N., Zhao,Y., Wright,W.E., Khanna,K.K.,
            Shay,J.W. and Pandita,T.K.
  TITLE     Single-strand DNA-binding protein SSB1 facilitates TERT recruitment
            to telomeres and maintains telomere G-overhangs
  JOURNAL   Cancer Res 75 (5), 858-869 (2015)
   PUBMED   25589350
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Gu,P., Deng,W., Lei,M. and Chang,S.
  TITLE     Single strand DNA binding proteins 1 and 2 protect newly replicated
            telomeres
  JOURNAL   Cell Res 23 (5), 705-719 (2013)
   PUBMED   23459151
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Li,Y., Bolderson,E., Kumar,R., Muniandy,P.A., Xue,Y., Richard,D.J.,
            Seidman,M., Pandita,T.K., Khanna,K.K. and Wang,W.
  TITLE     HSSB1 and hSSB2 form similar multiprotein complexes that
            participate in DNA damage response
  JOURNAL   J Biol Chem 284 (35), 23525-23531 (2009)
   PUBMED   19605351
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huang,J., Gong,Z., Ghosal,G. and Chen,J.
  TITLE     SOSS complexes participate in the maintenance of genomic stability
  JOURNAL   Mol Cell 35 (3), 384-393 (2009)
   PUBMED   19683501
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Richard,D.J., Bolderson,E., Cubeddu,L., Wadsworth,R.I., Savage,K.,
            Sharma,G.G., Nicolette,M.L., Tsvetanov,S., McIlwraith,M.J.,
            Pandita,R.K., Takeda,S., Hay,R.T., Gautier,J., West,S.C.,
            Paull,T.T., Pandita,T.K., White,M.F. and Khanna,K.K.
  TITLE     Single-stranded DNA-binding protein hSSB1 is critical for genomic
            stability
  JOURNAL   Nature 453 (7195), 677-681 (2008)
   PUBMED   18449195
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC104710.1.
            
            On Oct 1, 2011 this sequence version replaced NP_001030111.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC104710.1, SRR8487226.155799.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..243
                     /product="SOSS complex subunit B1 isoform 1"
                     /note="SOSS complex subunit B1; SOSS-B1; sensor of ssDNA
                     subunit B1; single-stranded DNA-binding protein 1; sensor
                     of single-strand DNA complex subunit B1;
                     oligonucleotide/oligosaccharide-binding fold-containing
                     protein 2B; oligonucleotide/oligosaccharide-binding fold
                     containing 2B"
                     /calculated_mol_wt=25503
     Region          50..127
                     /region_name="SoSSB_OBF"
                     /note="A subfamily of OB folds similar to the OB fold of
                     the crenarchaeote Sulfolobus solfataricus single-stranded
                     (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB
                     fold, and it physically and functionally interacts with
                     RNA polymerase. In vitro, SSoSSB...; cd04491"
                     /db_xref="CDD:239937"
     Site            order(50,99,101,103,125)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239937"
     Site            order(55..57,72..75,77,83..85,87,98,106..108,115..117)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239937"
     Region          <138..>219
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..243
                     /gene="Nabp2"
                     /gene_synonym="Obfc2b; RGD1308158"
                     /coded_by="NM_001034939.1:302..1033"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362813"
                     /db_xref="RGD:1308158"
ORIGIN      
        1 mgrpsgsmgq rlqalnlhlp fplpagchgs gsmttetfvk dikpglknln lifivletgr
       61 vtktkdghev rtckvadktg sinisvwddv gnliqpgdii rltkgyasvf kgcltlytgr
      121 ggdlqkigef cmvysevpnf sepnpeyntq qasnksvqnd ssptapqatt gppaaspase
      181 sqngnglstq pgpvggphps hapshppstr itrsqpnhtp sgppgpsssp vsngketrrs
      241 skr
//
LOCUS       NP_955425                609 aa            linear   ROD 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 11 [Rattus
            norvegicus].
ACCESSION   NP_955425 XP_231275
VERSION     NP_955425.2
DBSOURCE    REFSEQ: accession NM_199393.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Boskovski,M.T., Yuan,S., Pedersen,N.B., Goth,C.K., Makova,S.,
            Clausen,H., Brueckner,M. and Khokha,M.K.
  TITLE     The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
            type and laterality
  JOURNAL   Nature 504 (7480), 456-459 (2013)
   PUBMED   24226769
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Young,W.W. Jr., Holcomb,D.R., Ten Hagen,K.G. and Tabak,L.A.
  TITLE     Expression of UDP-GalNAc:polypeptide
            N-acetylgalactosaminyltransferase isoforms in murine tissues
            determined by real-time PCR: a new view of a large family
  JOURNAL   Glycobiology 13 (7), 549-557 (2003)
   PUBMED   12651884
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1 and BC062004.1.
            
            On Sep 15, 2012 this sequence version replaced NP_955425.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR,
            compared to variant 1. Both variants 1 and 2 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062004.1, SRR26360186.2140050.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..609
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     11"
                     /EC_number="2.4.1.41"
                     /note="galNAc-T11; pp-GaNTase 11; polypeptide GalNAc
                     transferase 11; protein-UDP
                     acetylgalactosaminyltransferase 11; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 11;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 11 (GalNAc-T11);
                     :polypeptide N-acetylgalactosaminyltransferase 11"
                     /calculated_mol_wt=69040
     Region          155..453
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(159..161,163,192,223,226,230,246..248,328..329,
                     351..352,354,379,382,387)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(246,248,379)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          479..605
                     /region_name="beta-trefoil_Ricin_GALNT11"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 11
                     (GALNT11) and similar proteins; cd23440"
                     /db_xref="CDD:467318"
     Site            order(496..499,509,511,514,519..520)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(539..542,550,552,555,560..561)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(581..584,593,595,598,602..603)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     CDS             1..609
                     /gene="Galnt11"
                     /coded_by="NM_199393.2:214..2043"
                     /db_xref="GeneID:311952"
                     /db_xref="RGD:735097"
ORIGIN      
        1 mmgsvtiryf cygclftsat wtvllfiyfn fsevtqplrn vpikgsgphg pfpkkfyprf
       61 trgpgrvlep qfkanrmddl mnnniedpdk glskssselg mifnerdqel rdlgyqkhaf
      121 nmlisnrlgy hrdvpdtrna ecrgksyptd lptasvvicf yneafsallr tvhsvvdrtp
      181 ahllheiilv ddssdfddlk geldeyiqry lpakvkvirn mkreglirgr migaahatge
      241 vlvfldshce vnvmwlqpll aiiledphtv vcpvidiisa dtlayssspv vrggfnwglh
      301 fkwdlvpvsd lggadsatap irsptmaggl famnrqyfnd lgqydsgmdi wggenleisf
      361 riwmcggklf iipcsrvghi frkrrpygsp egqdtmthns lrlahvwlde ykeqyfslrp
      421 dlktksfgni servelrkkl gcqsfkwyld nvypemqvsg pkarlqqpvf inrgpkrprv
      481 llrgrlyhlq tnkclvaqgr ssqkgglvll kacdygdptq vwiyneehel ilnnllcldm
      541 setrssdppr lmkchgsggs qqwtfgknnr lyqvsvgqcl rvvdqmdqkg yvgmaicdgs
      601 ssqqwrleg
//
LOCUS       NP_058924               1184 aa            linear   ROD 27-APR-2025
DEFINITION  atrophin-1 [Rattus norvegicus].
ACCESSION   NP_058924 XP_003750706 XP_006244699
VERSION     NP_058924.2
DBSOURCE    REFSEQ: accession NM_017228.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Zhang,F., Xu,D., Yuan,L., Sun,Y. and Xu,Z.
  TITLE     Epigenetic regulation of Atrophin1 by lysine-specific demethylase 1
            is required for cortical progenitor maintenance
  JOURNAL   Nat Commun 5, 5815 (2014)
   PUBMED   25519973
  REMARK    GeneRIF: Epigenetic regulation of ATN1 by LSD1 is required for
            cortical progenitor maintenance.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Yu,J., Ying,M., Zhuang,Y., Xu,T., Han,M., Wu,X. and Xu,R.
  TITLE     C-terminal deletion of the atrophin-1 protein results in growth
            retardation but not neurodegeneration in mice
  JOURNAL   Dev Dyn 238 (10), 2471-2478 (2009)
   PUBMED   19681162
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Hou,R. and Sibinga,N.E.
  TITLE     Atrophin proteins interact with the Fat1 cadherin and regulate
            migration and orientation in vascular smooth muscle cells
  JOURNAL   J Biol Chem 284 (11), 6955-6965 (2009)
   PUBMED   19131340
  REMARK    GeneRIF: Fat1 and Atrs 1,2 act in concert after vascular injury but
            show further that distinct Atr isoforms have disparate effects on
            VSMC directional migration.
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Redecker,P., Bockmann,J. and Bockers,T.M.
  TITLE     Secretory granules of hypophyseal and pancreatic endocrine cells
            contain proteins of the neuronal postsynaptic density
  JOURNAL   Cell Tissue Res 328 (1), 49-55 (2007)
   PUBMED   17120053
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Shen,Y., Lee,G., Choe,Y., Zoltewicz,J.S. and Peterson,A.S.
  TITLE     Functional architecture of atrophins
  JOURNAL   J Biol Chem 282 (7), 5037-5044 (2007)
   PUBMED   17150957
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Okamura-Oho,Y., Miyashita,T., Ohmi,K. and Yamada,M.
  TITLE     Dentatorubral-pallidoluysian atrophy protein interacts through a
            proline-rich region near polyglutamine with the SH3 domain of an
            insulin receptor tyrosine kinase substrate
  JOURNAL   Hum Mol Genet 8 (6), 947-957 (1999)
   PUBMED   10332026
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Ellerby,L.M., Andrusiak,R.L., Wellington,C.L., Hackam,A.S.,
            Propp,S.S., Wood,J.D., Sharp,A.H., Margolis,R.L., Ross,C.A.,
            Salvesen,G.S., Hayden,M.R. and Bredesen,D.E.
  TITLE     Cleavage of atrophin-1 at caspase site aspartic acid 109 modulates
            cytotoxicity
  JOURNAL   J Biol Chem 274 (13), 8730-8736 (1999)
   PUBMED   10085113
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Morris-Rosendahl,D.J., Burgert,E., Uyanik,G., Mayerova,A.,
            Duval,F., Macher,J.P. and Crocq,M.A.
  TITLE     Analysis of the CAG repeats in the SCA1 and B37 genes in
            schizophrenic and bipolar I disorder patients: tentative
            association between B37 and schizophrenia
  JOURNAL   Am J Med Genet 74 (3), 324-330 (1997)
   PUBMED   9184318
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Schmitt,I., Epplen,J.T. and Riess,O.
  TITLE     Predominant neuronal expression of the gene responsible for
            dentatorubral-pallidoluysian atrophy (DRPLA) in rat
  JOURNAL   Hum Mol Genet 4 (9), 1619-1624 (1995)
   PUBMED   8541849
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Loev,S.J., Margolis,R.L., Young,W.S., Li,S.H., Schilling,G.,
            Ashworth,R.G. and Ross,C.A.
  TITLE     Cloning and expression of the rat atrophin-I (DRPLA disease gene)
            homologue
  JOURNAL   Neurobiol Dis 2 (3), 129-138 (1995)
   PUBMED   9173996
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Apr 15, 2021 this sequence version replaced
            XP_003750706.1, XP_006244699.1, NP_058924.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U31777.1, SRR26643290.17925.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMEA5760475 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1184
                     /product="atrophin-1"
                     /note="dentatorubral pallidoluysian atrophy;
                     dentatorubral-pallidoluysian atrophy protein homolog;
                     atrophin-1-like"
                     /calculated_mol_wt=124776
     Region          1..1182
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          16..32
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Region          511..561
                     /region_name="Involved in binding BAIAP2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Region          618..761
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            635
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Region          781..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Region          873..888
                     /region_name="Required for interaction with FAT1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54259; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     Region          922..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Region          1027..1035
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54258.1)"
     Site            1109
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35126; propagated from
                     UniProtKB/Swiss-Prot (P54258.1)"
     CDS             1..1184
                     /gene="Atn1"
                     /gene_synonym="Drpla"
                     /coded_by="NM_017228.3:277..3831"
                     /db_xref="GeneID:29515"
                     /db_xref="RGD:61832"
ORIGIN      
        1 mktrqnkdsm smrsgrkkea pgpreelrsr graspggvst sssdgkaeks rqtakkarve
       61 etstpkankq grseeisese seetsapkkt kteelprpqs psdldsldgr sinddgssdp
      121 rdidqdnrst spsiyspgsv endsdsssgl sqgparpyhp pplfppsppp pdsiprqpes
      181 gfephpsvpp tgyhapmepp tsrlfqgppp gappphpqly pgsagggvls gppmgpkgga
      241 aassvgppsg gkqhpppttp ipisssgasg appakppntp vgagnlpsap ppatfphvtp
      301 nlppppalrp lnnasasppg mgaqpipghl psphamgqgm sglppgpekg ptlapsphpl
      361 ppasssapgp pmrypysscs sssvaassss saatsqypas qtlpsyphsf ppptsmsvsn
      421 qppkytqpsl psqavwsqgp pppppygrll pnnnthpgpf pptggqstah ppapahhhhq
      481 qqqqpqpqpq pqpqqhhhgn sgppppgayp hplessnshh ahpynmspsl gslrpyppgp
      541 ahlppshgqv sysqagpngp pvssssnssg sssqaayscs hpsssqgpqg asypfppvpp
      601 ittssatlst viatvasspa gyktasppgp pqyskrapsp gsyktatppg ykpgsppsfr
      661 tgtppgyrgt sppagpgtfk pgsptvgpgp lppagpssls slppppaapt tgppltatqi
      721 kqepaeeyet pespvppars pspppkvvdv pshasqsarf nkhldrgfns carsdlyfvp
      781 legsklakkr adlvekvrre aeqrareeke rererereke rerekerele rsvklaqegr
      841 apvecpslgp vphrppfepg savatvppyl gpdtpalrtl seyarphvms pgnrnhpfyv
      901 plgavdpgll gynvpalyss dpaarerere arerdlrdrl kpgfevkpse leplhgvpgp
      961 gldpfprhgg lalqpgppgl hpfpfhpslg plererlala agpalrpdms yaerlaaerq
     1021 haervaalgn dplarlqmln vtphhhqhsh ihshlhlhqq daihaasasv hplidplasg
     1081 shltripypa gtlpnpllph plhenevlrh qlfaapyrdl paslsapmsa ahqlqamhaq
     1141 saelqrlale qqqwlhahhp lhsvplpaqe dyyshlkkes dkpl
//
LOCUS       NP_001257799             258 aa            linear   ROD 27-APR-2025
DEFINITION  neurotrophin-3 isoform 3 precursor [Rattus norvegicus].
ACCESSION   NP_001257799
VERSION     NP_001257799.1
DBSOURCE    REFSEQ: accession NM_001270870.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Briones-Vidal,M.G., Reyes-Garcia,S.E. and Escobar,M.L.
  TITLE     Neurotrophin-3 into the insular cortex strengthens conditioned
            taste aversion memory
  JOURNAL   Behav Brain Res 461, 114857 (2024)
   PUBMED   38211776
  REMARK    GeneRIF: Neurotrophin-3 into the insular cortex strengthens
            conditioned taste aversion memory.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Zou,D., Wang,H., Hao,S. and Chen,F.
  TITLE     Repair effect of neurotrophic factor III (NT-3) on rats with spinal
            injury model and its mechanism
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (1), 56-61 (2024)
   PUBMED   38372112
  REMARK    GeneRIF: Repair effect of neurotrophic factor III (NT-3) on rats
            with spinal injury model and its mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Yang,Y., Xu,H.Y., Deng,Q.W., Wu,G.H., Zeng,X., Jin,H., Wang,L.J.,
            Lai,B.Q., Li,G., Ma,Y.H., Jiang,B., Ruan,J.W., Wang,Y.Q., Ding,Y.
            and Zeng,Y.S.
  TITLE     Electroacupuncture facilitates the integration of a grafted
            TrkC-modified mesenchymal stem cell-derived neural network into
            transected spinal cord in rats via increasing neurotrophin-3
  JOURNAL   CNS Neurosci Ther 27 (7), 776-791 (2021)
   PUBMED   33763978
  REMARK    GeneRIF: Electroacupuncture facilitates the integration of a
            grafted TrkC-modified mesenchymal stem cell-derived neural network
            into transected spinal cord in rats via increasing neurotrophin-3.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Xu,H., Yang,Y., Deng,Q.W., Zhang,B.B., Ruan,J.W., Jin,H.,
            Wang,J.H., Ren,J., Jiang,B., Sun,J.H., Zeng,Y.S. and Ding,Y.
  TITLE     Governor Vessel Electro-Acupuncture Promotes the Intrinsic Growth
            Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury
  JOURNAL   J Neurotrauma 38 (6), 734-745 (2021)
   PUBMED   33121345
  REMARK    GeneRIF: Governor Vessel Electro-Acupuncture Promotes the Intrinsic
            Growth Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury.
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Donsante,A., Xue,J., Poth,K.M., Hardcastle,N.S., Diniz,B.,
            O'Connor,D.M., Xia,Y. and Boulis,N.M.
  TITLE     Controlling the Release of Neurotrophin-3 and Chondroitinase ABC
            Enhances the Efficacy of Nerve Guidance Conduits
  JOURNAL   Adv Healthc Mater 9 (14), e2000200 (2020)
   PUBMED   32548984
  REMARK    GeneRIF: Controlling the Release of Neurotrophin-3 and
            Chondroitinase ABC Enhances the Efficacy of Nerve Guidance
            Conduits.
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Smith,M.A., Makino,S., Altemus,M., Michelson,D., Hong,S.K.,
            Kvetnansky,R. and Post,R.M.
  TITLE     Stress and antidepressants differentially regulate neurotrophin 3
            mRNA expression in the locus coeruleus
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8788-8792 (1995)
   PUBMED   7568018
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Maisonpierre,P.C., Le Beau,M.M., Espinosa,R. 3rd, Ip,N.Y.,
            Belluscio,L., de la Monte,S.M., Squinto,S., Furth,M.E. and
            Yancopoulos,G.D.
  TITLE     Human and rat brain-derived neurotrophic factor and neurotrophin-3:
            gene structures, distributions, and chromosomal localizations
  JOURNAL   Genomics 10 (3), 558-568 (1991)
   PUBMED   1889806
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Hallbook,F., Ibanez,C.F. and Persson,H.
  TITLE     Evolutionary studies of the nerve growth factor family reveal a
            novel member abundantly expressed in Xenopus ovary
  JOURNAL   Neuron 6 (5), 845-858 (1991)
   PUBMED   2025430
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Ernfors,P., Ibanez,C.F., Ebendal,T., Olson,L. and Persson,H.
  TITLE     Molecular cloning and neurotrophic activities of a protein with
            structural similarities to nerve growth factor: developmental and
            topographical expression in the brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5454-5458 (1990)
   PUBMED   2164684
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Maisonpierre,P.C., Belluscio,L., Squinto,S., Ip,N.Y., Furth,M.E.,
            Lindsay,R.M. and Yancopoulos,G.D.
  TITLE     Neurotrophin-3: a neurotrophic factor related to NGF and BDNF
  JOURNAL   Science 247 (4949 Pt 1), 1446-1451 (1990)
   PUBMED   2321006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV778881.1, BC070504.1 and M34643.1.
            
            Transcript Variant: This variant (4) lacks an exon in the 5'
            region, which causes translation initiation at a downstream AUG,
            compared to variant 1. The resulting isoform (3) has a shorter
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EV778881.1, EV780605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..258
                     /product="neurotrophin-3 isoform 3 precursor"
                     /note="HDNF; NT-3; NGF-2; neurotrophic factor; nerve
                     growth factor 2; neurotrophin-3 (HDNF/NT-3)"
                     /calculated_mol_wt=27558
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2105
     Region          20..133
                     /region_name="NTF3_N"
                     /note="Neutrophin-3 N-terminus; pfam19338"
                     /db_xref="CDD:437170"
     Region          60..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18280.1)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18280.1)"
     mat_peptide     140..258
                     /product="Neurotrophin-3. /id=PRO_0000019664"
                     /note="propagated from UniProtKB/Swiss-Prot (P18280.1)"
                     /calculated_mol_wt=13625
     Region          145..256
                     /region_name="NGF"
                     /note="Nerve growth factor family; pfam00243"
                     /db_xref="CDD:459728"
     CDS             1..258
                     /gene="Ntf3"
                     /coded_by="NM_001270870.1:212..988"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:81737"
                     /db_xref="RGD:619728"
ORIGIN      
        1 msilfyvifl aylrgiqgnn mdqrslpeds lnsliikliq adilknklsk qmvdvkenyq
       61 stlpkaeapr epeqgeatrs efqpmiatdt ellrqqrryn sprvllsdst pleppplylm
      121 edyvgnpvvt nrtsprrkry aehkshrgey svcdseslwv tdkssaidir ghqvtvlgei
      181 ktgnspvkqy fyetrckear pvkngcrgid dkhwnsqckt sqtyvralts ennklvgwrw
      241 iridtscvca lsrkigrt
//
LOCUS       NP_001166921             963 aa            linear   ROD 27-APR-2025
DEFINITION  AP2-associated protein kinase 1 [Rattus norvegicus].
ACCESSION   NP_001166921 XP_001070331 XP_575594
VERSION     NP_001166921.1
DBSOURCE    REFSEQ: accession NM_001173450.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Chen,Y., Gao,X. and Pei,H.
  TITLE     miRNA-384-3p alleviates sevoflurane-induced nerve injury by
            inhibiting Aak1 kinase in neonatal rats
  JOURNAL   Brain Behav 12 (7), e2556 (2022)
   PUBMED   35726359
  REMARK    GeneRIF: miRNA-384-3p alleviates sevoflurane-induced nerve injury
            by inhibiting Aak1 kinase in neonatal rats.
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Ultanir,S.K., Hertz,N.T., Li,G., Ge,W.P., Burlingame,A.L.,
            Pleasure,S.J., Shokat,K.M., Jan,L.Y. and Jan,Y.N.
  TITLE     Chemical genetic identification of NDR1/2 kinase substrates AAK1
            and Rabin8 Uncovers their roles in dendrite arborization and spine
            development
  JOURNAL   Neuron 73 (6), 1127-1142 (2012)
   PUBMED   22445341
  REMARK    GeneRIF: This study demonistrated that AAK1 contributes to dendrite
            growth regulation.
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Kuai,L., Ong,S.E., Madison,J.M., Wang,X., Duvall,J.R., Lewis,T.A.,
            Luce,C.J., Conner,S.D., Pearlman,D.A., Wood,J.L., Schreiber,S.L.,
            Carr,S.A., Scolnick,E.M. and Haggarty,S.J.
  TITLE     AAK1 identified as an inhibitor of neuregulin-1/ErbB4-dependent
            neurotrophic factor signaling using integrative chemical genomics
            and proteomics
  JOURNAL   Chem Biol 18 (7), 891-906 (2011)
   PUBMED   21802010
  REMARK    GeneRIF: AAK1 is a relevant target of K252a, that the loss of AAK1
            alters ErbB4 trafficking and expression levels, providing evidence
            for a previously unrecognized role for AAK1 in Nrg1-mediated
            neurotrophic factor signaling.
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Gupta-Rossi,N., Ortica,S., Meas-Yedid,V., Heuss,S., Moretti,J.,
            Olivo-Marin,J.C. and Israel,A.
  TITLE     The adaptor-associated kinase 1, AAK1, is a positive regulator of
            the Notch pathway
  JOURNAL   J Biol Chem 286 (21), 18720-18730 (2011)
   PUBMED   21464124
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Sorensen,E.B. and Conner,S.D.
  TITLE     AAK1 regulates Numb function at an early step in clathrin-mediated
            endocytosis
  JOURNAL   Traffic 9 (10), 1791-1800 (2008)
   PUBMED   18657069
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Henderson,D.M. and Conner,S.D.
  TITLE     A novel AAK1 splice variant functions at multiple steps of the
            endocytic pathway
  JOURNAL   Mol Biol Cell 18 (7), 2698-2706 (2007)
   PUBMED   17494869
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Conner,S.D., Schroter,T. and Schmid,S.L.
  TITLE     AAK1-mediated micro2 phosphorylation is stimulated by assembled
            clathrin
  JOURNAL   Traffic 4 (12), 885-890 (2003)
   PUBMED   14617351
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Conner,S.D. and Schmid,S.L.
  TITLE     Identification of an adaptor-associated kinase, AAK1, as a
            regulator of clathrin-mediated endocytosis
  JOURNAL   J Cell Biol 156 (5), 921-929 (2002)
   PUBMED   11877461
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before May 13, 2010 this sequence version replaced
            XP_575594.3, XP_001070331.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.23912.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..963
                     /product="AP2-associated protein kinase 1"
                     /EC_number="2.7.11.1"
                     /note="adaptor-associated kinase 1"
                     /calculated_mol_wt=103729
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          42..316
                     /region_name="STKc_NAK_like"
                     /note="Catalytic domain of Numb-Associated Kinase
                     (NAK)-like Serine/Threonine kinases; cd14037"
                     /db_xref="CDD:270939"
     Site            order(52..56,60,72,74,104,126..129,133,135,176,178,
                     180..181,183,194,197,221..224)
                     /site_type="active"
                     /db_xref="CDD:270939"
     Site            order(52..56,60,72,74,104,126..129,133,176,178,180..181,
                     183,194)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270939"
     Site            order(56,133,135,176,178,180,197,221..224)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270939"
     Site            order(193..207,208..224)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270939"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          <296..>427
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            391
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHJ0; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          665..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          825..962
                     /region_name="Clathrin-binding domain (CBD).
                     /evidence=ECO:0000250|UniProtKB:Q2M2I8"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          840..861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHJ0; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Region          926..947
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHJ0; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P0C1X8.1)"
     CDS             1..963
                     /gene="Aak1"
                     /gene_synonym="RGD1563580"
                     /coded_by="NM_001173450.1:537..3428"
                     /db_xref="GeneID:500244"
                     /db_xref="RGD:1305520"
ORIGIN      
        1 mkkffdsrre qgssglgsgs sggggsssgl gsgyigrvfg igrqqvtvde vlaeggfalv
       61 flvrtsngvk calkrmfvnn ehdlqvckre iqimrdlsgh knivgyidss innvssgdvw
      121 evlilmdfcr ggqvvnlmnq rlqtgftene vlqifcdtce avarlhqckt piihrdlkve
      181 nillhdrghy vlcdfgsatn kfqnpqaegv navedeikky ttlsyrapem vnlysgkiit
      241 tkadiwalgc llyklcyftl pfgesqvaic dgsftipdns rysqdmhcli rymlepdpdk
      301 rpdiyqvsyf sfkllkkecp vpnvqnspip tklpepvkas eaavkktqpk arltdpiptt
      361 etsiaprqrp kagqtqpnpg ilpiqpaltp rkratvqplp qatgpsnqps llasvsqpka
      421 qatpsqplqs sqpkqpqapp tpqqtpapqt qglptqaqat pqhqqqlllk qqqqqqqqqq
      481 qqqpqqptap pqpsgtfyqq qqpqqqqaqt qqfqavhpaa qqsvtaqfpv vsqggsqqql
      541 mqnfyqqqqq qqqqqqqlma qqaalqqkta vvvpqpqaqp atapqaaaaq epaqiqapar
      601 qqpkvqttpp ptiqgqkvgs ltppsspktq raghrrilsd vthsavfgvp askstqllha
      661 aaaeaslsks ksatttpsgs prtsqqnvsn asegstwnpf dddnfsklta eellnkdfak
      721 lgegklpekl ggsaeslipg fqatqgdafa tssfsagtae krkggqavds gipllsvsdp
      781 fiplqvpdap eklieglksp dtslllpdll pmtdpfgsts daviekadaa veslipglep
      841 pvaqrlpsht esvtsnrtds ltgedslldc sllsnptadl ldefapials asthkaaeds
      901 nlisgfgvae gsekvaedef dpipvlitkn tqgghsrnss gssesslpnl arslllvdql
      961 idl
//
LOCUS       NP_001257607             255 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 13 [Rattus norvegicus].
ACCESSION   NP_001257607
VERSION     NP_001257607.1
DBSOURCE    REFSEQ: accession NM_001270678.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (13) lacks an alternate in-frame
            exon and uses an alternate exon in place of another exon in the 3'
            end of the gene, compared to variant 1. The resulting isoform (13)
            has the same N- and C-termini but is shorter and has a different
            internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224966.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..255
                     /product="troponin T, fast skeletal muscle isoform 13"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30223
     Region          59..195
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..255
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270678.1:117..884"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeeev qeeekprpkl tapkipegek vdfddiqkkr
       61 qnkdlmelqa lidshfeark keeeelialk eriekrraer aeqqriraek ererqnrlae
      121 ekarreeeda krraeddlkk kkalssmgan yssylakadq krgkkqtare mkkkilaerr
      181 kplnidhlsd dklrdkakel wdtlyqletd kfefgeklkr qkydimtvra rvemlakfsk
      241 kagatakgkv ggrwk
//
LOCUS       NP_113803                794 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 148 [Rattus norvegicus].
ACCESSION   NP_113803
VERSION     NP_113803.1
DBSOURCE    REFSEQ: accession NM_031615.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Bai,L. and Merchant,J.L.
  TITLE     ATM phosphorylates ZBP-89 at Ser202 to potentiate p21waf1 induction
            by butyrate
  JOURNAL   Biochem Biophys Res Commun 359 (3), 817-821 (2007)
   PUBMED   17560543
  REMARK    GeneRIF: ataxia telangiectasia mutated protein phosphorylation of
            ZBP-89 contributes to Histone deacetylase inhibitors induction of
            p21(waf1) gene expression
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Bai,L. and Merchant,J.L.
  TITLE     Transcription factor ZBP-89 is required for STAT1 constitutive
            expression
  JOURNAL   Nucleic Acids Res 31 (24), 7264-7270 (2003)
   PUBMED   14654702
  REMARK    GeneRIF: ZBP-89 binds directly to the STAT1 promoter G-rich element
            Erratum:[Nucleic Acids Res. 2004 Feb 24;32(4):1615]
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Zhang,X., Diab,I.H. and Zehner,Z.E.
  TITLE     ZBP-89 represses vimentin gene transcription by interacting with
            the transcriptional activator, Sp1
  JOURNAL   Nucleic Acids Res 31 (11), 2900-2914 (2003)
   PUBMED   12771217
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Takeuchi,A., Mishina,Y., Miyaishi,O., Kojima,E., Hasegawa,T. and
            Isobe,K.
  TITLE     Heterozygosity with respect to Zfp148 causes complete loss of fetal
            germ cells during mouse embryogenesis
  JOURNAL   Nat Genet 33 (2), 172-176 (2003)
   PUBMED   12524542
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Hasegawa,T., Takeuchi,A., Miyaishi,O., Isobe,Ki. and de
            Crombrugghe,B.
  TITLE     Cloning and characterization of a transcription factor that binds
            to the proximal promoters of the two mouse type I collagen genes
  JOURNAL   J Biol Chem 272 (8), 4915-4923 (1997)
   PUBMED   9030551
REFERENCE   7  (residues 1 to 794)
  AUTHORS   Merchant,J.L., Iyer,G.R., Taylor,B.R., Kitchen,J.R.,
            Mortensen,E.R., Wang,Z., Flintoft,R.J., Michel,J.B. and
            Bassel-Duby,R.
  TITLE     ZBP-89, a Kruppel-like zinc finger protein, inhibits epidermal
            growth factor induction of the gastrin promoter
  JOURNAL   Mol Cell Biol 16 (12), 6644-6653 (1996)
   PUBMED   8943318
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U30381.1, SRR26360176.2171274.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..794
                     /product="zinc finger protein 148"
                     /note="transcription factor ZBP-89; zinc finger
                     DNA-binding protein 89"
                     /calculated_mol_wt=88617
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61624; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Region          171..193
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          173..193
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(178,180,182,184..185,188..189,192,206,208,212..213,
                     216..217,220,234,236,238,240..241,244..245,248)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          185..210
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQR1; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Region          201..221
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          214..238
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..266
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQR1; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Region          257..275
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62806.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61624; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Region          574..596
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62806.1)"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQR1; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UQR1; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62806.1)"
     CDS             1..794
                     /gene="Zfp148"
                     /gene_synonym="Zbp-89; Znf148"
                     /coded_by="NM_031615.2:447..2831"
                     /db_xref="GeneID:58820"
                     /db_xref="RGD:62063"
ORIGIN      
        1 mniddklegl flkcggidem qssramvvmg gvsgqsavsg elqesvlqdr slphqeilaa
       61 devlqesemr qqdmishdel mvheetvknd eeqtdtherl pqglqyalnv pisvkqeitf
      121 tdvseqlmrd kkqvrepvdl qkkkkrkqrs pakiltined gslglktpks hvcehcnaaf
      181 rtnyhlqrhv fihtgekpfq csqcdmrfiq kyllqrheki htgekpfrcd ecgmrfiqky
      241 hmerhkrths gekpyqceyc lqyfsrtdrv lkhkrmchen hdkklnrcai kgglltseed
      301 sgfstspkdn slpkkkrqkp ekkssgmdke svldksdtkk drndylplys sstkvkdeym
      361 vaeyavemph ssvggshled asgeihppkl vlkkinskrs lkqpleqsqt isplstyeds
      421 kvskyafelv dkqalldseg sadidqvdnl qegpskpvhs stnyddamqf lkkkrylqaa
      481 snnsreyaln vgtiasqpsv tqaavasvid enttasilds qalnveiksn hdknvipdev
      541 lqtlldhysh kangqheisf svadtevtss isinssdvpe vtqsenvgss sqasssdkan
      601 mlqeyskflq qaldrtsqnd aylnspslnf vtdnqtlpnp pafssidkqv yaampinsfr
      661 sgmnsplrtt pdkshfgliv gdsqhpfpfs gdetnhasat stadfldqvt sqkkaeaqpv
      721 hqayqmssfe qpfrapyhgs ragiatqfst angqvnlrgp gtsaefsefp lvnvndnrag
      781 mtsspdattg qtfg
//
LOCUS       NP_001128405              77 aa            linear   ROD 27-APR-2025
DEFINITION  cysteine-rich protein 1 [Rattus norvegicus].
ACCESSION   NP_001128405 XP_001073337 XP_001079173
VERSION     NP_001128405.1
DBSOURCE    REFSEQ: accession NM_001134933.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Latonen,L., Jarvinen,P.M., Suomela,S., Moore,H.M.,
            Saarialho-Kere,U. and Laiho,M.
  TITLE     Ultraviolet B radiation regulates cysteine-rich protein 1 in human
            keratinocytes
  JOURNAL   Photodermatol Photoimmunol Photomed 26 (2), 70-77 (2010)
   PUBMED   20415737
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Chen,B., Young,J. and Leng,F.
  TITLE     DNA bending by the mammalian high-mobility group protein AT hook 2
  JOURNAL   Biochemistry 49 (8), 1590-1595 (2010)
   PUBMED   20108983
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Hao,J., Serohijos,A.W., Newton,G., Tassone,G., Wang,Z., Sgroi,D.C.,
            Dokholyan,N.V. and Basilion,J.P.
  TITLE     Identification and rational redesign of peptide ligands to CRIP1, a
            novel biomarker for cancers
  JOURNAL   PLoS Comput Biol 4 (8), e1000138 (2008)
   PUBMED   18670594
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Wang,Q., Williamson,M., Bott,S., Brookman-Amissah,N., Freeman,A.,
            Nariculam,J., Hubank,M.J., Ahmed,A. and Masters,J.R.
  TITLE     Hypomethylation of WNT5A, CRIP1 and S100P in prostate cancer
  JOURNAL   Oncogene 26 (45), 6560-6565 (2007)
   PUBMED   17486081
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Perez-Alvarado,G.C., Kosa,J.L., Louis,H.A., Beckerle,M.C.,
            Winge,D.R. and Summers,M.F.
  TITLE     Structure of the cysteine-rich intestinal protein, CRIP
  JOURNAL   J Mol Biol 257 (1), 153-174 (1996)
   PUBMED   8632452
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Tsui,S.K., Yam,N.Y., Lee,C.Y. and Waye,M.M.
  TITLE     Isolation and characterization of a cDNA that codes for a
            LIM-containing protein which is developmentally regulated in heart
  JOURNAL   Biochem Biophys Res Commun 205 (1), 497-505 (1994)
   PUBMED   7999070
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Levenson,C.W., Shay,N.F. and Cousins,R.J.
  TITLE     Cloning and initial characterization of the promoter region of the
            rat cysteine-rich intestinal protein gene
  JOURNAL   Biochem J 303 (Pt 3) (Pt 3), 731-736 (1994)
   PUBMED   7980439
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Hempe,J.M. and Cousins,R.J.
  TITLE     Cysteine-rich intestinal protein binds zinc during transmucosal
            zinc transport
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9671-9674 (1991)
   PUBMED   1946385
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Birkenmeier,E.H. and Gordon,J.I.
  TITLE     Developmental regulation of a gene that encodes a cysteine-rich
            intestinal protein and maps near the murine immunoglobulin heavy
            chain locus
  JOURNAL   Proc Natl Acad Sci U S A 83 (8), 2516-2520 (1986)
   PUBMED   3085096
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB729209.1 and AI716760.1.
            
            On or before Sep 14, 2008 this sequence version replaced
            XP_001073337.1, XP_001079173.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB729209.1, SRR8487226.183804.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..77
                     /product="cysteine-rich protein 1"
                     /note="cysteine-rich intestinal protein; cysteine-rich
                     protein 1 (intestinal)"
                     /calculated_mol_wt=8419
     Region          4..57
                     /region_name="LIM_CRIP"
                     /note="The LIM domain of Cysteine-Rich Intestinal Protein
                     (CRIP); cd09478"
                     /db_xref="CDD:188862"
     Site            order(4,7,25,28,31,34,52,56)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188862"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50238; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     Site            22
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63254; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     Site            68
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P63254; propagated from
                     UniProtKB/Swiss-Prot (P63255.2)"
     CDS             1..77
                     /gene="Crip1"
                     /gene_synonym="Crip; Crp-1"
                     /coded_by="NM_001134933.2:115..348"
                     /db_xref="GeneID:691657"
                     /db_xref="RGD:1597237"
ORIGIN      
        1 mpkcpkcdke vyfaervtsl gkdwhrpclk cekcgktlts gghaehegkp ycnhpcysam
       61 fgpkgfgrgg aeshtfk
//
LOCUS       NP_001178029             236 aa            linear   ROD 27-APR-2025
DEFINITION  RNA-binding protein 24 [Rattus norvegicus].
ACCESSION   NP_001178029 XP_001073426
VERSION     NP_001178029.1
DBSOURCE    REFSEQ: accession NM_001191100.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Zhang,M., Zhang,Y., Xu,E., Mohibi,S., de Anda,D.M., Jiang,Y.,
            Zhang,J. and Chen,X.
  TITLE     Rbm24, a target of p53, is necessary for proper expression of p53
            and heart development
  JOURNAL   Cell Death Differ 25 (6), 1118-1130 (2018)
   PUBMED   29358667
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Lin,Y., Tan,K.T., Liu,J., Kong,X., Huang,Z. and Xu,X.Q.
  TITLE     Global profiling of Rbm24 bound RNAs uncovers a multi-tasking RNA
            binding protein
  JOURNAL   Int J Biochem Cell Biol 94, 10-21 (2018)
   PUBMED   29104163
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Ito,J., Iijima,M., Yoshimoto,N., Niimi,T., Kuroda,S. and
            Maturana,A.D.
  TITLE     RBM20 and RBM24 cooperatively promote the expression of short enh
            splice variants
  JOURNAL   FEBS Lett 590 (14), 2262-2274 (2016)
   PUBMED   27289039
  REMARK    GeneRIF: results suggest that, in healthy conditions, RBM20 and
            RBM24 cooperate to promote the expression of short ENH isoforms.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Zhang,T., Lin,Y., Liu,J., Zhang,Z.G., Fu,W., Guo,L.Y., Pan,L.,
            Kong,X., Zhang,M.K., Lu,Y.H., Huang,Z.R., Xie,Q., Li,W.H. and
            Xu,X.Q.
  TITLE     Rbm24 Regulates Alternative Splicing Switch in Embryonic Stem Cell
            Cardiac Lineage Differentiation
  JOURNAL   Stem Cells 34 (7), 1776-1789 (2016)
   PUBMED   26990106
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Grifone,R., Xie,X., Bourgeois,A., Saquet,A., Duprez,D. and Shi,D.L.
  TITLE     The RNA-binding protein Rbm24 is transiently expressed in myoblasts
            and is required for myogenic differentiation during vertebrate
            development
  JOURNAL   Mech Dev 134, 1-15 (2014)
   PUBMED   25217815
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Yang,J., Hung,L.H., Licht,T., Kostin,S., Looso,M., Khrameeva,E.,
            Bindereif,A., Schneider,A. and Braun,T.
  TITLE     RBM24 is a major regulator of muscle-specific alternative splicing
  JOURNAL   Dev Cell 31 (1), 87-99 (2014)
   PUBMED   25313962
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Xu,E., Zhang,J., Zhang,M., Jiang,Y., Cho,S.J. and Chen,X.
  TITLE     RNA-binding protein RBM24 regulates p63 expression via mRNA
            stability
  JOURNAL   Mol Cancer Res 12 (3), 359-369 (2014)
   PUBMED   24375645
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Jiang,Y., Zhang,M., Qian,Y., Xu,E., Zhang,J. and Chen,X.
  TITLE     Rbm24, an RNA-binding protein and a target of p53, regulates p21
            expression via mRNA stability
  JOURNAL   J Biol Chem 289 (6), 3164-3175 (2014)
   PUBMED   24356969
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Jin,D., Hidaka,K., Shirai,M. and Morisaki,T.
  TITLE     RNA-binding motif protein 24 regulates myogenin expression and
            promotes myogenic differentiation
  JOURNAL   Genes Cells 15 (11), 1158-1167 (2010)
   PUBMED   20977548
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000017.1.
            
            On Jul 17, 2010 this sequence version replaced XP_001073426.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.60458.1,
                                           SRR26643298.68874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840110, SAMN12840129
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..236
                     /product="RNA-binding protein 24"
                     /calculated_mol_wt=24721
     Region          11..86
                     /region_name="RRM_RBM24_RBM38_like"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     RNA-binding protein RBM24, RBM38 and similar proteins;
                     cd12384"
                     /db_xref="CDD:409818"
     Region          175..199
                     /region_name="Necessary for interaction with EIF4E.
                     /evidence=ECO:0000250|UniProtKB:Q9BX46"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R7T6.4)"
     CDS             1..236
                     /gene="Rbm24"
                     /coded_by="NM_001191100.1:86..796"
                     /db_xref="GeneID:690139"
                     /db_xref="RGD:1584029"
ORIGIN      
        1 mhttqkdtty tkifvgglpy httdaslrky fevfgdieea vvitdrqtgk srgygfvtma
       61 draaaerack dpnpiidgrk anvnlaylga kprimqpgfa fgvqqlhpal iqrpfgipah
      121 yvypqafvqp gvviphvqpt aaaasttpyi dytgaayaqy saaaaaaaaa aaydqypyaa
      181 spaatgyvtt ggysyavqqp itaaapgtaa aaaaaaaaaa afgqyqpqql qtdrmq
//
LOCUS       NP_001296976             321 aa            linear   ROD 27-APR-2025
DEFINITION  U5 small nuclear ribonucleoprotein TSSC4 [Rattus norvegicus].
ACCESSION   NP_001296976 XP_006230884
VERSION     NP_001296976.1
DBSOURCE    REFSEQ: accession NM_001310047.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 23, 2015 this sequence version replaced XP_006230884.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY562667.1, SRR26360181.44311.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..321
                     /product="U5 small nuclear ribonucleoprotein TSSC4"
                     /note="protein TSSC4; tumor-suppressing subchromosomal
                     transferable fragment 4"
                     /calculated_mol_wt=34196
     Region          95..211
                     /region_name="TSSC4"
                     /note="Tumour suppressing sub-chromosomal transferable
                     candidate 4; pfam15264"
                     /db_xref="CDD:434584"
     CDS             1..321
                     /gene="Tssc4"
                     /coded_by="NM_001310047.1:193..1158"
                     /db_xref="GeneID:361682"
                     /db_xref="RGD:1307043"
ORIGIN      
        1 msglmaetea gleveepted dtlpsdtvsl sdsdsdlslp sgvevqalsp erlsgesqed
       61 sgpddppshp tgipttavqp fhlrgmsstf sqrshsifdc lesaarqepc sapqtsvvdn
      121 csfkrpvapp sqtparslsr vhgntdptrv hpvpdyvshp erwtkysled vsetseqsnr
      181 daalaflssr sqasptdyvp ffnqdpsscg egrvvftkpv rgsearaerk rvlkkgvvsg
      241 aggeasvela hlagpeaeew sghqgqpevv vpseaarpes ssgpigmktv gfhgskkrsr
      301 dhfrnrdsnp egpgsergps v
//
LOCUS       NP_001258248             609 aa            linear   ROD 27-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 11 [Rattus
            norvegicus].
ACCESSION   NP_001258248
VERSION     NP_001258248.1
DBSOURCE    REFSEQ: accession NM_001271319.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Boskovski,M.T., Yuan,S., Pedersen,N.B., Goth,C.K., Makova,S.,
            Clausen,H., Brueckner,M. and Khokha,M.K.
  TITLE     The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia
            type and laterality
  JOURNAL   Nature 504 (7480), 456-459 (2013)
   PUBMED   24226769
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Young,W.W. Jr., Holcomb,D.R., Ten Hagen,K.G. and Tabak,L.A.
  TITLE     Expression of UDP-GalNAc:polypeptide
            N-acetylgalactosaminyltransferase isoforms in murine tissues
            determined by real-time PCR: a new view of a large family
  JOURNAL   Glycobiology 13 (7), 549-557 (2003)
   PUBMED   12651884
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ223626.1, SRR26643296.12324.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..609
                     /product="polypeptide N-acetylgalactosaminyltransferase
                     11"
                     /EC_number="2.4.1.41"
                     /note="galNAc-T11; pp-GaNTase 11; polypeptide GalNAc
                     transferase 11; protein-UDP
                     acetylgalactosaminyltransferase 11; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 11;
                     UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 11 (GalNAc-T11);
                     :polypeptide N-acetylgalactosaminyltransferase 11"
                     /calculated_mol_wt=69040
     Region          155..453
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(159..161,163,192,223,226,230,246..248,328..329,
                     351..352,354,379,382,387)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            order(246,248,379)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          479..605
                     /region_name="beta-trefoil_Ricin_GALNT11"
                     /note="ricin B-type lectin domain, beta-trefoil fold,
                     found in polypeptide N-acetylgalactosaminyltransferase 11
                     (GALNT11) and similar proteins; cd23440"
                     /db_xref="CDD:467318"
     Site            order(496..499,509,511,514,519..520)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(539..542,550,552,555,560..561)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     Site            order(581..584,593,595,598,602..603)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:467318"
     CDS             1..609
                     /gene="Galnt11"
                     /coded_by="NM_001271319.1:297..2126"
                     /db_xref="GeneID:311952"
                     /db_xref="RGD:735097"
ORIGIN      
        1 mmgsvtiryf cygclftsat wtvllfiyfn fsevtqplrn vpikgsgphg pfpkkfyprf
       61 trgpgrvlep qfkanrmddl mnnniedpdk glskssselg mifnerdqel rdlgyqkhaf
      121 nmlisnrlgy hrdvpdtrna ecrgksyptd lptasvvicf yneafsallr tvhsvvdrtp
      181 ahllheiilv ddssdfddlk geldeyiqry lpakvkvirn mkreglirgr migaahatge
      241 vlvfldshce vnvmwlqpll aiiledphtv vcpvidiisa dtlayssspv vrggfnwglh
      301 fkwdlvpvsd lggadsatap irsptmaggl famnrqyfnd lgqydsgmdi wggenleisf
      361 riwmcggklf iipcsrvghi frkrrpygsp egqdtmthns lrlahvwlde ykeqyfslrp
      421 dlktksfgni servelrkkl gcqsfkwyld nvypemqvsg pkarlqqpvf inrgpkrprv
      481 llrgrlyhlq tnkclvaqgr ssqkgglvll kacdygdptq vwiyneehel ilnnllcldm
      541 setrssdppr lmkchgsggs qqwtfgknnr lyqvsvgqcl rvvdqmdqkg yvgmaicdgs
      601 ssqqwrleg
//
LOCUS       NP_001007236            2748 aa            linear   ROD 27-APR-2025
DEFINITION  inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001007236 XP_342733
VERSION     NP_001007236.2
DBSOURCE    REFSEQ: accession NM_001007235.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2748)
  AUTHORS   Pan,D., Jiang,M., Tao,G., Shi,J., Song,Z., Chen,R. and Wang,D.
  TITLE     The role of Ca2+ signalling and InsP3R in the pathogenesis of
            intrahepatic cholestasis of pregnancy
  JOURNAL   J Obstet Gynaecol 44 (1), 2345276 (2024)
   PUBMED   38685831
  REMARK    GeneRIF: The role of Ca[2+] signalling and InsP3R in the
            pathogenesis of intrahepatic cholestasis of pregnancy.
REFERENCE   2  (residues 1 to 2748)
  AUTHORS   Shi,R., Liu,Z., Yue,H., Li,M., Liu,S., De,D., Li,R., Chen,Y.,
            Cheng,S., Gu,X., Jia,M., Li,J., Li,J., Zhang,S., Feng,N., Fan,R.,
            Fu,F., Liu,Y., Ding,M. and Pei,J.
  TITLE     IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin
  JOURNAL   Cell Mol Biol Lett 29 (1), 22 (2024)
   PUBMED   38308199
  REMARK    GeneRIF: IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2748)
  AUTHORS   Obaid,A.A., Almasmoum,H., Almaimani,R.A., El-Boshy,M., Aslam,A.,
            Idris,S., Ghaith,M.M., El-Readi,M.Z., Ahmad,J., Farrash,W.F.,
            Mujalli,A., Eid,S.Y., Elzubier,M.E. and Refaat,B.
  TITLE     Vitamin D and calcium co-therapy mitigates pre-established cadmium
            nephropathy by regulating renal calcium homeostatic molecules and
            improving anti-oxidative and anti-inflammatory activities in rat
  JOURNAL   J Trace Elem Med Biol 79, 127221 (2023)
   PUBMED   37244046
REFERENCE   4  (residues 1 to 2748)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   5  (residues 1 to 2748)
  AUTHORS   Fan,G., Baker,M.R., Terry,L.E., Arige,V., Chen,M., Seryshev,A.B.,
            Baker,M.L., Ludtke,S.J., Yule,D.I. and Serysheva,I.I.
  TITLE     Conformational motions and ligand-binding underlying gating and
            regulation in IP3R channel
  JOURNAL   Nat Commun 13 (1), 6942 (2022)
   PUBMED   36376291
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2748)
  AUTHORS   Zhang,S.X., Zhang,J.P., Fletcher,D.L., Zoeller,R.T. and Sun,G.Y.
  TITLE     In situ hybridization of mRNA expression for IP3 receptor and
            IP3-3-kinase in rat brain after transient focal cerebral ischemia
  JOURNAL   Brain Res Mol Brain Res 32 (2), 252-260 (1995)
   PUBMED   7500836
REFERENCE   7  (residues 1 to 2748)
  AUTHORS   Takei,K., Stukenbrok,H., Metcalf,A., Mignery,G.A., Sudhof,T.C.,
            Volpe,P. and De Camilli,P.
  TITLE     Ca2+ stores in Purkinje neurons: endoplasmic reticulum
            subcompartments demonstrated by the heterogeneous distribution of
            the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin
  JOURNAL   J Neurosci 12 (2), 489-505 (1992)
   PUBMED   1311032
REFERENCE   8  (residues 1 to 2748)
  AUTHORS   Suzuki,T., Abe-Dohmae,S. and Tanaka,R.
  TITLE     P400 protein is one of the major substrates for
            Ca2+/calmodulin-dependent protein kinase II in the postsynaptic
            density-enriched fraction isolated from rat cerebral cortex,
            hippocampus and cerebellum
  JOURNAL   Neurochem Int 20 (1), 61-67 (1992)
   PUBMED   1338970
REFERENCE   9  (residues 1 to 2748)
  AUTHORS   Danoff,S.K., Ferris,C.D., Donath,C., Fischer,G.A., Munemitsu,S.,
            Ullrich,A., Snyder,S.H. and Ross,C.A.
  TITLE     Inositol 1,4,5-trisphosphate receptors: distinct neuronal and
            nonneuronal forms derived by alternative splicing differ in
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2951-2955 (1991)
   PUBMED   1849282
REFERENCE   10 (residues 1 to 2748)
  AUTHORS   Mignery,G.A., Newton,C.L., Archer,B.T. 3rd and Sudhof,T.C.
  TITLE     Structure and expression of the rat inositol 1,4,5-trisphosphate
            receptor
  JOURNAL   J Biol Chem 265 (21), 12679-12685 (1990)
   PUBMED   2165071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J05510.1, BF402715.1,
            GQ233032.1 and BC091346.1.
            
            On Jul 20, 2012 this sequence version replaced NP_001007236.1.
            
            Summary: This gene belongs to the Insp3 receptor family. It encodes
            an intracellular receptor for inositol 1,4,5-trisphosphate. Upon
            stimulation by inositol 1,4,5-trisphosphate, this receptor mediates
            calcium release from the endoplasmic reticulum. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2748
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q41"
     Protein         1..2748
                     /product="inositol 1,4,5-trisphosphate-gated calcium
                     channel ITPR1 isoform 1"
                     /note="IP-3-R; type 1 InsP3 receptor; IP3 receptor; type 1
                     inositol 1,4,5-trisphosphate receptor; IP3R 1; inositol
                     1,4,5-triphosphate receptor, type 1; inositol
                     1,4,5-triphosphate receptor 1; inositol
                     1,4,5-trisphosphate-gated calcium channel ITPR1"
                     /calculated_mol_wt=312878
     Region          5..229
                     /region_name="Ins145_P3_rec"
                     /note="Inositol 1,4,5-trisphosphate/ryanodine receptor;
                     pfam08709"
                     /db_xref="CDD:462572"
     Region          224..445
                     /region_name="beta-trefoil_MIR_ITPR1"
                     /note="MIR domain, beta-trefoil fold, found in inositol
                     1,4,5-trisphosphate receptor type 1 (ITPR1) and similar
                     proteins; cd23287"
                     /db_xref="CDD:467758"
     Site            order(245..246,300,374,376,387,393,425..426)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467758"
     Site            order(265,267..269,275)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:467758"
     Region          476..670
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          1005..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1136..1167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1193..1312
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Site            1588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1750..1788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            1754
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1880..1905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1931..1951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1961..2068
                     /region_name="RIH_assoc"
                     /note="RyR and IP3R Homology associated; pfam08454"
                     /db_xref="CDD:462482"
     Site            2273..2293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2305..2325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2349..2599
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            2352..2372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2396..2416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2439..2459
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2462..2527
                     /region_name="Interaction with ERP44.
                     /evidence=ECO:0000250|UniProtKB:P11881"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2568..2588
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2721..2748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     CDS             1..2748
                     /gene="Itpr1"
                     /gene_synonym="I145TR; InsP3R; InsP3R1; IP3R1; P400"
                     /coded_by="NM_001007235.2:239..8485"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25262"
                     /db_xref="RGD:2933"
ORIGIN      
        1 msdkmssflh igdicslyae gstngfistl glvddrcvvq peagdlnnpp kkfrdclfkl
       61 cpmnrysaqk qfwkaakpga nsttdavlln klhhaadlek kqnetenrkl lgtviqygnv
      121 iqllhlksnk yltvnkrlpa lleknamrvt ldeagnegsw fyiqpfyklr sigdsvvigd
      181 kvvlnpvnag qplhasshql vdnpgcnevn svncntswki vlfmkwsdnk ddilkggdvv
      241 rlfhaeqekf ltcdehrkkq hvflrttgrq satsatsska lwevevvqhd pcrggagywn
      301 slfrfkhlat ghylaaevdp dfeeeclefq psvdpdqdas rsrlrnaqek mvyslvsvpe
      361 gndissifel dpttlrggds lvprnsyvrl rhlctntwvh stnipidkee ekpvmlkigt
      421 splkedkeaf aivpvspaev rdldfandas kvlgsiagkl ekgtitqner rsvtklledl
      481 vyfvtggtns gqdvlevvfs kpnrerqklm reqnilkqif kllqapftdc gdgpmlrlee
      541 lgdqrhapfr hicrlcyrvl rhsqqdyrkn qeyiakqfgf mqkqigydvl aedtitallh
      601 nnrkllekhi taaeidtfvs lvrknreprf ldylsdlcvs mnksipvtqe lickavlnpt
      661 nadilietkl vlsrfefegv stgenaleag edeeevwlfw rdsnkeirsk svrelaqdak
      721 egqkedrdvl syyryqlnlf armcldrqyl aineisgqld vdlilrcmsd enlpydlras
      781 fcrlmlhmhv drdpqeqvtp vkyarlwsei pseiaiddyd ssgaskdeik erfaqtmefv
      841 eeylrdvvcq rfpfsdkekn kltfevvnla rnliyfgfyn fsdllrltki llaildcvhv
      901 ttifpiskmt kgeenkgsnv mrsihgvgel mtqvvlrggg flpmtpmaaa pegnvkqaep
      961 ekedimvmdt klkiieilqf ilnvrldyri scllcifkre fdesnsqsse tssgnssqeg
     1021 psnvpgaldf ehieeqaegi fggseentpl dlddhggrtf lrvllhltmh dypplvsgal
     1081 qllfrhfsqr qevlqafkqv qllvtsqdvd nykqikqdld qlrsivekse lwvykgqgpd
     1141 epmdgasgen ehkkteegts kplkhestss ynyrvvkeil irlsklcvqe sasvrksrkq
     1201 qqrllrnmga havvlellqi pyekaedtkm qeimrlahef lqnfcagnqq nqallhkhin
     1261 lflnpgilea vtmqhifmnn fqlcseiner vvqhfvhcie thgrnvqyik flqtivkaeg
     1321 kfikkcqdmv maelvnsged vlvfyndras fqtliqmmrs erdrmdensp lmyhihlvel
     1381 lavctegknv yteikcnsll plddivrvvt hedcipevki ayinflnhcy vdtevemkei
     1441 ytsnhmwklf enflvdicra cnntsdrkha dsvlekyvte ivmsivttff sspfsdqstt
     1501 lqtrqpvfvq llqgvfrvyh cnwlmpsqka svescirvls dvaksraiai pvdldsqvnn
     1561 lflkshnivq ktamnwrlsa rnaarrdsvl aasrdyrnii erlqdivsal edrlrplvqa
     1621 elsvlvdvlh rpellfpent darrkcesgg ficklikhtk qlleeneekl cikvlqtlre
     1681 mmtkdrgyge kqisidelen aelpqppeae nsteelepsp plrqledhkr gealrqilvn
     1741 ryygnirpsg rresltsfgn gplspggpsk pggggggpgs gstsrgemsl aevqchldke
     1801 gasnlvidli mnassdrvfh esillaiall eggnttiqhs ffcrltedkk sekffkvfyd
     1861 rmkvaqqeik atvtvntsdl gnkkkddevd rdapsrkkak epttqiteev rdqlleasaa
     1921 trkafttfrr eadpddhyqs gegtqattdk akddlemsav itimqpilrf lqllcenhnr
     1981 dlqnflrcqn nktnynlvce tlqfldcicg sttgglgllg lyineknval inqtleslte
     2041 ycqgpchenq nciathesng idiitaliln dinplgkkrm dlvlelknna sklllaimes
     2101 rhdsenaeri lynmrpkelv evikkaymqg evefedgeng edgaasprnv ghniyilahq
     2161 larhnkelqt mlkpggqvdg dealefyakh taqieivrld rtmeqivfpv psicefltke
     2221 sklriyytte rdeqgskind fflrsedlfn emnwqkklra qpvlywcarn msfwssisfn
     2281 lavlmnllva ffypfkgvrg gtlephwsgl lwtamlisla ivialpkphg iraliastil
     2341 rlifsvglqp tlfllgafnv cnkiiflmsf vgncgtftrg yramvldvef lyhllyllic
     2401 amglfvheff yslllfdlvy reetllnvik svtrngrsii ltavlalilv ylfsivgylf
     2461 fkddfilevd rlpnetagpe tgeslandfl ysdvcrvetg enctspapke ellpveeteq
     2521 dkehtcetll mcivtvlshg lrsgggvgdv lrkpskeepl faarviydll fffmviiivl
     2581 nlifgviidt fadlrsekqk keeilkttcf icglerdkfd nktvtfeehi keehnmwhyl
     2641 cfivlvkvkd steytgpesy vaemirernl dwfprmrams lvssdsegeq nelrnlqekl
     2701 estmklvtnl sgqlselkdq mteqrkqkqr igllghpphm nvnpqqpa
//
LOCUS       NP_001154984             173 aa            linear   ROD 27-APR-2025
DEFINITION  deoxycytidylate deaminase isoform 2 [Rattus norvegicus].
ACCESSION   NP_001154984
VERSION     NP_001154984.1
DBSOURCE    REFSEQ: accession NM_001161512.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Maley,G.F., Lobo,A.P. and Maley,F.
  TITLE     Properties of an affinity-column-purified human deoxycytidylate
            deaminase
  JOURNAL   Biochim Biophys Acta 1162 (1-2), 161-170 (1993)
   PUBMED   8448179
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP504069.1, DY317307.1 and BC087138.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, and
            lacks an alternate exon in the 3' coding region that causes a
            frameshift, compared to variant 1. The encoded isoform (2) has a
            distinct C-terminus and is shorter than isoform 1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..173
                     /product="deoxycytidylate deaminase isoform 2"
                     /EC_number="3.5.4.12"
                     /note="deoxycytidylate deaminase"
                     /calculated_mol_wt=19176
     Region          14..>126
                     /region_name="ComEB"
                     /note="Deoxycytidylate deaminase [Nucleotide transport and
                     metabolism]; COG2131"
                     /db_xref="CDD:441734"
     CDS             1..173
                     /gene="Dctd"
                     /coded_by="NM_001161512.1:293..814"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290741"
                     /db_xref="RGD:1359671"
ORIGIN      
        1 mtytpnmsdi sckkrddyle wpeyfmavaf lsaqrskdps sqvgacivnt enkivgigyn
       61 gmpngcsddl lpwrrtaenk ldtkypyvch aelnaimnkn sadvkgcsmy valfpcneca
      121 kliiqaensh qstarlslis irliavrvrs lsefrapeed dtphtrgsls lss
//
LOCUS       NP_001257612             312 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein E precursor [Rattus norvegicus].
ACCESSION   NP_001257612
VERSION     NP_001257612.1
DBSOURCE    REFSEQ: accession NM_001270683.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lee,B.H., Cevizci,M., Lieblich,S.E., Ibrahim,M., Wen,Y., Eid,R.S.,
            Lamers,Y., Duarte-Guterman,P. and Galea,L.A.M.
  TITLE     Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age
  JOURNAL   Brain Behav Immun 120, 54-70 (2024)
   PUBMED   38772427
  REMARK    GeneRIF: Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Chen,H., Zhao,S., Jian,Q., Yan,Y., Wang,S., Zhang,X. and Ji,Y.
  TITLE     The role of ApoE in fatty acid transport from neurons to astrocytes
            under ischemia/hypoxia conditions
  JOURNAL   Mol Biol Rep 51 (1), 320 (2024)
   PUBMED   38393618
  REMARK    GeneRIF: The role of ApoE in fatty acid transport from neurons to
            astrocytes under ischemia/hypoxia conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Matsuo,H., Kawakami,K., Ohara,H., Kaneko,T., Mashimo,T., Yamada,T.
            and Nabika,T.
  TITLE     Apolipoprotein E-depletion accelerates arterial fat deposition in
            the spontaneously hypertensive rat
  JOURNAL   Exp Anim 72 (4), 439-445 (2023)
   PUBMED   37081644
  REMARK    GeneRIF: Apolipoprotein E-depletion accelerates arterial fat
            deposition in the spontaneously hypertensive rat.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Jiang,C., Chen,Z., Wang,X., Zhang,Y., Guo,X., Fan,H., Huang,D.,
            He,Y., Tang,X., Ai,Y., Liu,Y., Yang,H. and Hao,D.
  TITLE     Curcumin-activated Olfactory Ensheathing Cells Improve Functional
            Recovery After Spinal Cord Injury by Modulating Microglia
            Polarization Through APOE/TREM2/NF-kappaB Signaling Pathway
  JOURNAL   J Neuroimmune Pharmacol 18 (3), 476-494 (2023)
   PUBMED   37658943
  REMARK    GeneRIF: Curcumin-activated Olfactory Ensheathing Cells Improve
            Functional Recovery After Spinal Cord Injury by Modulating
            Microglia Polarization Through APOE/TREM2/NF-kappaB Signaling
            Pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Nguyen,T.D., Watanabe,A., Burleigh,S., Ghaffarzadegan,T.,
            Kanklai,J., Prykhodko,O., Hallenius,F.F. and Nyman,M.
  TITLE     Monobutyrin and monovalerin improve gut-blood-brain biomarkers and
            alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats
  JOURNAL   Sci Rep 12 (1), 15454 (2022)
   PUBMED   36104381
  REMARK    GeneRIF: Monobutyrin and monovalerin improve gut-blood-brain
            biomarkers and alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Takahashi,S., Kawarabayasi,Y., Nakai,T., Sakai,J. and Yamamoto,T.
  TITLE     Rabbit very low density lipoprotein receptor: a low density
            lipoprotein receptor-like protein with distinct ligand specificity
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9252-9256 (1992)
   PUBMED   1384047
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Feussner,G., Funke,H., Weng,W., Assmann,G., Lackner,K.J. and
            Ziegler,R.
  TITLE     Severe type III hyperlipoproteinemia associated with unusual
            apolipoprotein E1 phenotype and epsilon 1/'null' genotype
  JOURNAL   Eur J Clin Invest 22 (9), 599-608 (1992)
   PUBMED   1360898
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Utermann,G., Hees,M. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E and occurrence of
            dysbetalipoproteinaemia in man
  JOURNAL   Nature 269 (5629), 604-607 (1977)
   PUBMED   199847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC086581.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. All five variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219318.1, SRR26643286.841.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..312
                     /product="apolipoprotein E precursor"
                     /note="apo-E"
                     /calculated_mol_wt=33845
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1927
     mat_peptide     19..312
                     /product="Apolipoprotein E. /id=PRO_0000001996"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
                     /calculated_mol_wt=33845
     Region          72..247
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          73..258
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          202..282
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          258..312
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          270..282
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     CDS             1..312
                     /gene="Apoe"
                     /gene_synonym="APOEA"
                     /coded_by="NM_001270683.1:103..1041"
                     /db_xref="GeneID:25728"
                     /db_xref="RGD:2138"
ORIGIN      
        1 mkalwalllv plltgclaeg elevtdqlpg qsdqpweqal nrfwdylrwv qtlsdqvqee
       61 lqssqvtqel tvlmedtmte vkaykkelee qlgpvaeetr arlakevqaa qarlgadmed
      121 lrnrlgqyrn evntmlgqst eelrsrlsth lrkmrkrlmr daddlqkrla vykagaqega
      181 ergvsairer lgplveqgrq rtanlgagaa qplrdraqal sdrirgrlee vgnqardrle
      241 evreqmeevr skmeeqtqqi rlqaeifqar ikgwfeplve dmqrqwanlm ekiqasvatn
      301 siasttvple nq
//
LOCUS       NP_001309871             108 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial pyruvate carrier 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001309871 XP_006250189
VERSION     NP_001309871.1
DBSOURCE    REFSEQ: accession NM_001322942.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Wang,Y., Liu,Y., Yuan,Y., Zhang,Y., Luo,Y., Han,S., Yan,Y.,
            Wang,Z., Liu,X. and Zhao,L.
  TITLE     Downregulation of mitochondrial pyruvate carrier 2 aggravates
            neuronal injury in the cortex following cerebral ischemia in rat
  JOURNAL   Brain Res Bull 185, 193-202 (2022)
   PUBMED   35580702
  REMARK    GeneRIF: Downregulation of mitochondrial pyruvate carrier 2
            aggravates neuronal injury in the cortex following cerebral
            ischemia in rat.
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Vigueira,P.A., McCommis,K.S., Schweitzer,G.G., Remedi,M.S.,
            Chambers,K.T., Fu,X., McDonald,W.G., Cole,S.L., Colca,J.R.,
            Kletzien,R.F., Burgess,S.C. and Finck,B.N.
  TITLE     Mitochondrial pyruvate carrier 2 hypomorphism in mice leads to
            defects in glucose-stimulated insulin secretion
  JOURNAL   Cell Rep 7 (6), 2042-2053 (2014)
   PUBMED   24910426
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Bricker,D.K., Taylor,E.B., Schell,J.C., Orsak,T., Boutron,A.,
            Chen,Y.C., Cox,J.E., Cardon,C.M., Van Vranken,J.G., Dephoure,N.,
            Redin,C., Boudina,S., Gygi,S.P., Brivet,M., Thummel,C.S. and
            Rutter,J.
  TITLE     A mitochondrial pyruvate carrier required for pyruvate uptake in
            yeast, Drosophila, and humans
  JOURNAL   Science 337 (6090), 96-100 (2012)
   PUBMED   22628558
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Herzig,S., Raemy,E., Montessuit,S., Veuthey,J.L., Zamboni,N.,
            Westermann,B., Kunji,E.R. and Martinou,J.C.
  TITLE     Identification and functional expression of the mitochondrial
            pyruvate carrier
  JOURNAL   Science 337 (6090), 93-96 (2012)
   PUBMED   22628554
REFERENCE   5  (residues 1 to 108)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Tsou,A.P., Lai,C., Danielson,P., Noonan,D.J. and Sutcliffe,J.G.
  TITLE     Structural characterization of a heterogeneous family of rat brain
            mRNAs
  JOURNAL   Mol Cell Biol 6 (3), 768-778 (1986)
   PUBMED   3022128
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 15, 2016 this sequence version replaced XP_006250189.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE112736.1, FQ216993.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..108
                     /product="mitochondrial pyruvate carrier 2 isoform 2"
                     /note="protein 0-44; brain protein 44; solute carrier
                     family 54 member 2"
                     /calculated_mol_wt=11907
     Region          33..>81
                     /region_name="MPC"
                     /note="Mitochondrial pyruvate carriers; pfam03650"
                     /db_xref="CDD:427425"
     CDS             1..108
                     /gene="Mpc2"
                     /gene_synonym="Brp44; RGD1563422; SLC54A2"
                     /coded_by="NM_001322942.1:247..573"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100359982"
                     /db_xref="RGD:1563422"
ORIGIN      
        1 maaagarglr atyhrlmdkv elllpkklrp lynhpagprt vffwapimkw glvcagladm
       61 arpaeklsta qstvlmatdi iknsnlkess krvpdhlnil dvdrniet
//
LOCUS       NP_036987               1100 aa            linear   ROD 27-APR-2025
DEFINITION  tyrosine-protein kinase JAK3 [Rattus norvegicus].
ACCESSION   NP_036987
VERSION     NP_036987.2
DBSOURCE    REFSEQ: accession NM_012855.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Wang,Y.C., Cai,D., Cui,X.B., Chuang,Y.H., Fay,W.P. and Chen,S.Y.
  TITLE     Janus Kinase 3 Deficiency Promotes Vascular
            Reendothelialization-Brief Report
  JOURNAL   Arterioscler Thromb Vasc Biol 41 (6), 2019-2026 (2021)
   PUBMED   33910370
  REMARK    GeneRIF: Janus Kinase 3 Deficiency Promotes Vascular
            Reendothelialization-Brief Report.
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Hou,Y., Li,H. and Huo,W.
  TITLE     MicroRNA-495 alleviates ulcerative interstitial cystitis via
            inactivating the JAK-STAT signaling pathway by inhibiting JAK3
  JOURNAL   Int Urogynecol J 32 (5), 1253-1263 (2021)
   PUBMED   33416962
  REMARK    GeneRIF: MicroRNA-495 alleviates ulcerative interstitial cystitis
            via inactivating the JAK-STAT signaling pathway by inhibiting JAK3.
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Tan,S., Xu,J., Lai,A., Cui,R., Bai,R., Li,S., Liang,W., Zhang,G.,
            Jiang,S., Liu,S., Zheng,M. and Wang,W.
  TITLE     Curculigoside exerts significant anti-arthritic effects in vivo and
            in vitro via regulation of the JAK/STAT/NF-kappaB signaling pathway
  JOURNAL   Mol Med Rep 19 (3), 2057-2064 (2019)
   PUBMED   30664158
  REMARK    GeneRIF: treatment downregulated the expression of JAK1, JAK3 and
            STAT3, and upregulated cytosolic nuclear factor (NF)kappaB p65 and
            IkappaB. In conclusion, the results of the present study indicated
            that curculigoside exhibited significant antiarthritic effects in
            vivo and in vitro, and the molecular mechanism may be associated
            with the JAK/STAT/NFkappaB signaling pathway.
REFERENCE   4  (residues 1 to 1100)
  AUTHORS   Wang,Y.C., Cui,X.B., Chuang,Y.H. and Chen,S.Y.
  TITLE     Janus Kinase 3, a Novel Regulator for Smooth Muscle Proliferation
            and Vascular Remodeling
  JOURNAL   Arterioscler Thromb Vasc Biol 37 (7), 1352-1360 (2017)
   PUBMED   28473442
  REMARK    GeneRIF: JAK3 mediates smooth muscle cell proliferation and
            survival during injury-induced vascular remodeling.
REFERENCE   5  (residues 1 to 1100)
  AUTHORS   Ge,S., Zhang,J., Du,Y., Hu,B., Zhou,Z. and Lou,J.
  TITLE     Dynamic changes in the gene expression profile during rat oral
            carcinogenesis induced by 4-nitroquinoline 1-oxide
  JOURNAL   Mol Med Rep 13 (3), 2561-2569 (2016)
   PUBMED   26860129
REFERENCE   6  (residues 1 to 1100)
  AUTHORS   Tortolani,P.J., Lal,B.K., Riva,A., Johnston,J.A., Chen,Y.Q.,
            Reaman,G.H., Beckwith,M., Longo,D., Ortaldo,J.R., Bhatia,K.,
            McGrath,I., Kehrl,J., Tuscano,J., McVicar,D.W. and O'Shea,J.J.
  TITLE     Regulation of JAK3 expression and activation in human B cells and B
            cell malignancies
  JOURNAL   J Immunol 155 (11), 5220-5226 (1995)
   PUBMED   7594533
REFERENCE   7  (residues 1 to 1100)
  AUTHORS   Macchi,P., Villa,A., Giliani,S., Sacco,M.G., Frattini,A., Porta,F.,
            Ugazio,A.G., Johnston,J.A., Candotti,F., O'Shea,J.J. et al.
  TITLE     Mutations of Jak-3 gene in patients with autosomal severe combined
            immune deficiency (SCID)
  JOURNAL   Nature 377 (6544), 65-68 (1995)
   PUBMED   7659163
REFERENCE   8  (residues 1 to 1100)
  AUTHORS   Rolling,C., Treton,D., Beckmann,P., Galanaud,P. and Richard,Y.
  TITLE     JAK3 associates with the human interleukin 4 receptor and is
            tyrosine phosphorylated following receptor triggering
  JOURNAL   Oncogene 10 (9), 1757-1761 (1995)
   PUBMED   7538655
REFERENCE   9  (residues 1 to 1100)
  AUTHORS   Kirken,R.A., Rui,H., Malabarba,M.G. and Farrar,W.L.
  TITLE     Identification of interleukin-2 receptor-associated tyrosine kinase
            p116 as novel leukocyte-specific Janus kinase
  JOURNAL   J Biol Chem 269 (29), 19136-19141 (1994)
   PUBMED   7518451
REFERENCE   10 (residues 1 to 1100)
  AUTHORS   Witthuhn,B.A., Silvennoinen,O., Miura,O., Lai,K.S., Cwik,C.,
            Liu,E.T. and Ihle,J.N.
  TITLE     Involvement of the Jak-3 Janus kinase in signalling by interleukins
            2 and 4 in lymphoid and myeloid cells
  JOURNAL   Nature 370 (6485), 153-157 (1994)
   PUBMED   8022486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Jul 3, 2010 this sequence version replaced NP_036987.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D28508.1, SRR26360186.1636.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..1100
                     /product="tyrosine-protein kinase JAK3"
                     /EC_number="2.7.10.2"
                     /note="Janus kinase 3, protein-tyrosine kinase; JAK-3"
                     /calculated_mol_wt=122596
     Region          1..223
                     /region_name="cytokine/interferon/growth hormone
                     receptors. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63272.2)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62137; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     Region          41..114
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          126..245
                     /region_name="FERM_B-lobe"
                     /note="FERM domain B-lobe; cl46853"
                     /db_xref="CDD:481193"
     Region          250..359
                     /region_name="FERM_C_JAK3"
                     /note="FERM domain C-lobe of Janus kinase (JAK) 3;
                     cd13334"
                     /db_xref="CDD:275413"
     Site            order(258,275,277,288)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:275413"
     Site            order(292,297..300,339,343,346..347)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:275413"
     Site            339..350
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:275413"
     Region          359..455
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(379,399,424,426)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198243"
     Site            order(425,453)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198243"
     Region          517..774
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(523..526,529,531,550,552,581,596..599,643,647..648,
                     650,666..667)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P52333; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     Region          813..1095
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(824..827,830,832,849,851,880,898..901,945,949..950,
                     952,962..963)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P52333; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P52333; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P52333; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P52333; propagated from
                     UniProtKB/Swiss-Prot (Q63272.2)"
     CDS             1..1100
                     /gene="Jak3"
                     /gene_synonym="RATJAK3"
                     /coded_by="NM_012855.2:61..3363"
                     /db_xref="GeneID:25326"
                     /db_xref="RGD:2940"
ORIGIN      
        1 mappseetpl isqrscslss seagalhvll pprgpgppqr lsfsfgdyla edlcvraaka
       61 cgilpvyhsl falatedlsc wfppshifsi edvdtqvlvy rlrfyfpgwf gletchrfgl
      121 hkdltsaild vhvlehlfaq hrsdlvsgrl pvglslkdqg eflslavldl aqmarkqaqr
      181 pgellksvsy kaclppslrd liqgqsfvtr rrirrtvvqa lrrvvacqad ryalmakyil
      241 dlerlhpaat tesflvglpg aqeepgclrv tgdngiawss kdqelfqtfc dfpeivdvsi
      301 kqaprvgpag ehrlvtitrm dghileaefp glpealsfva lvdgyfrlic dsrhffckev
      361 apprlleeea elchgpitld faihklkaag slpgsyilrr spqdydsfll tacvqtplgp
      421 dykgclirqd psgafslvgl sqlhrslqel ltacwhsglq vdgtalnlts ccvprpkeks
      481 nlivvrrgrn ptpapghsps ccaltklsfh tipadslewh enlghgsftk ifhghrrevv
      541 dgethdtevl lkvmdsrhqn cmesfleaas lmsqvsyphl vllhgvcmag dsimvqefvy
      601 lgaidtylrk rghlvpaswk lqvtkqlaya lnyledkglp hgnvsarkvl laregvdgnp
      661 pfiklsdpgv sptvlsleml tdripwvape clqeagtlnl eadkwgfgat twevfsgapm
      721 hitslepakk lkfyedrgql palkwteleg liaqcmaydp grrpsfrail rdlnglitsd
      781 yellsdptpg ipnprdelcg gaqlyacqdp aifeerhlky isllgkgnfg svelcrydpl
      841 gdntgplvav kqlqhsgpeq qrdfqreiqi lkalhcdfiv kyrgvsygpg rqslrlvmey
      901 lpsgclrdfl qrhrarlhnd rlllfawqic kgmeylgarr cvhrdlaarn ilveseahvk
      961 iadfglakll plgkdyyvvr epgqspifwy apeslsdnif srqsdvwsfg vvlyelftys
     1021 dkscspstef lrmmgpereg splchllell aegrrlppps tcptevqelm qlcwspnpqd
     1081 rpafdtlspq ldalwrgspg
//
LOCUS       NP_001257602             254 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 7 [Rattus norvegicus].
ACCESSION   NP_001257602
VERSION     NP_001257602.1
DBSOURCE    REFSEQ: accession NM_001270673.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (7) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (7) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216208.1, FQ215252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..254
                     /product="troponin T, fast skeletal muscle isoform 7"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30005
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P02641; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          58..194
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          96..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          230..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     CDS             1..254
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270673.1:117..881"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeape peekprpklt apkipegekv dfddiqkkrq
       61 nkdlmelqal idshfearkk eeeelialke riekrraera eqqriraeke rerqnrlaee
      121 karreeedak rraeddlkkk kalssmgany ssylakadqk rgkkqtarem kkkilaerrk
      181 plnidhlsdd klrdkakelw dtlyqletdk fefgeklkrq kydittlrsr idqaqkhskk
      241 agatakgkvg grwk
//
LOCUS       NP_001159369             131 aa            linear   ROD 27-APR-2025
DEFINITION  interferon alpha responsive protein isoform a [Rattus norvegicus].
ACCESSION   NP_001159369
VERSION     NP_001159369.1
DBSOURCE    REFSEQ: accession NM_001165897.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Rose,A.E., Zhao,C., Turner,E.M., Steyer,A.M. and Schlieker,C.
  TITLE     Arresting a Torsin ATPase reshapes the endoplasmic reticulum
  JOURNAL   J Biol Chem 289 (1), 552-564 (2014)
   PUBMED   24275647
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Zhao,C., Brown,R.S., Chase,A.R., Eisele,M.R. and Schlieker,C.
  TITLE     Regulation of Torsin ATPases by LAP1 and LULL1
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), E1545-E1554 (2013)
   PUBMED   23569223
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Vander Heyden,A.B., Naismith,T.V., Snapp,E.L., Hodzic,D. and
            Hanson,P.I.
  TITLE     LULL1 retargets TorsinA to the nuclear envelope revealing an
            activity that is impaired by the DYT1 dystonia mutation
  JOURNAL   Mol Biol Cell 20 (11), 2661-2672 (2009)
   PUBMED   19339278
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Goodchild,R.E. and Dauer,W.T.
  TITLE     The AAA+ protein torsinA interacts with a conserved domain present
            in LAP1 and a novel ER protein
  JOURNAL   J Cell Biol 168 (6), 855-862 (2005)
   PUBMED   15767459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO565924.1, CK478392.1, CB804669.1, EV767100.1 and DV728294.1.
            
            Transcript Variant: This variant (3) shares a portion of its 5'
            UTR, but no coding sequence with variant 1. Variant 3 encodes a
            shorter protein, (interferon alpha responsive protein), which is
            distinct from torsin-1A-interacting protein 2. Variants 2 and 3
            encode the same protein, isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ222366.1, EV771821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..131
                     /product="interferon alpha responsive protein isoform a"
                     /note="interferon alpha responsive protein; torsin A
                     interacting protein 2"
                     /calculated_mol_wt=15147
     CDS             1..131
                     /gene="Tor1aip2"
                     /coded_by="NM_001165897.1:684..1079"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:304881"
                     /db_xref="RGD:735059"
ORIGIN      
        1 mfsdnshcpd cgqqwfpsle lghwlyqtel venecyqvfl drinradycp ecypdnpanr
       61 slvlpwsfpl ewapqnltrw tfekachpfl lgpplvrkki hdsrvagfnp alqlilsrtd
      121 ktlnkklgqs k
//
LOCUS       NP_077341                438 aa            linear   ROD 27-APR-2025
DEFINITION  5-hydroxytryptamine receptor 6 [Rattus norvegicus].
ACCESSION   NP_077341
VERSION     NP_077341.2
DBSOURCE    REFSEQ: accession NM_024365.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Farias,C.P., Leite,A.K.O., Schmidt,B.E., de Carvalho Myskiw,J. and
            Wyse,A.T.S.
  TITLE     The 5-HT2A, 5-HT5A, and 5-HT6 serotonergic receptors in the medial
            prefrontal cortex behave differently in extinction learning: Does
            social support play a role?
  JOURNAL   Behav Brain Res 463, 114922 (2024)
   PUBMED   38408524
  REMARK    GeneRIF: The 5-HT2A, 5-HT5A, and 5-HT6 serotonergic receptors in
            the medial prefrontal cortex behave differently in extinction
            learning: Does social support play a role?
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Rychtyk,J., Partyka,A., Gdula-Argasinska,J., Myslowska,K.,
            Wilczynska,N., Jastrzebska-Wiesek,M. and Wesolowska,A.
  TITLE     5-HT6 receptor agonist and antagonist improve memory impairments
            and hippocampal BDNF signaling alterations induced by MK-801
  JOURNAL   Brain Res 1722, 146375 (2019)
   PUBMED   31412259
  REMARK    GeneRIF: 5-HT6 receptor agonist and antagonist improve memory
            impairments and hippocampal BDNF signaling alterations induced by
            MK-801.
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Rahman,M.A., Kim,H., Lee,K.H., Yun,H.M., Hong,J.H., Kim,Y.,
            Choo,H., Park,M. and Rhim,H.
  TITLE     5-Hydroxytryptamine 6 Receptor (5-HT6R)-Mediated Morphological
            Changes via RhoA-Dependent Pathways
  JOURNAL   Mol Cells 40 (7), 495-502 (2017)
   PUBMED   28681593
  REMARK    GeneRIF: 5-HT6R plays an important role in the regulation of cell
            morphology via a RhoA-dependent pathway in mammalian cell lines and
            primary neurons.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Jastrzebska-Wiesek,M., Siwek,A., Partyka,A.,
            Antkiewicz-Michaluk,L., Michaluk,J., Romanska,I., Kolaczkowski,M.
            and Wesolowska,A.
  TITLE     Study of a mechanism responsible for potential antidepressant
            activity of EMD 386088, a 5-HT6 partial agonist in rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 389 (8), 839-849 (2016)
   PUBMED   27106213
  REMARK    GeneRIF: Dopaminergic system is involved in antidepressant-like
            activity of Htr6 partial agonist EMD386088.
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Brodsky,M., Gibson,A.W., Smirnov,D., Nair,S.G. and Neumaier,J.F.
  TITLE     Striatal 5-HT6 Receptors Regulate Cocaine Reinforcement in a
            Pathway-Selective Manner
  JOURNAL   Neuropsychopharmacology 41 (9), 2377-2387 (2016)
   PUBMED   27032690
  REMARK    GeneRIF: Study concludes that 5-HT6 receptors in medium spiny
            neurons in the direct and indirect pathway of the nucleus accumbens
            shell increase the sensitivity to the reinforcing properties of
            cocaine, particularly at low doses.
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Grimaldi,B., Bonnin,A., Fillion,M.P., Ruat,M., Traiffort,E. and
            Fillion,G.
  TITLE     Characterization of 5-ht6 receptor and expression of 5-ht6 mRNA in
            the rat brain during ontogenetic development
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 357 (4), 393-400 (1998)
   PUBMED   9606024
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Boess,F.G., Monsma,F.J. Jr., Carolo,C., Meyer,V., Rudler,A.,
            Zwingelstein,C. and Sleight,A.J.
  TITLE     Functional and radioligand binding characterization of rat 5-HT6
            receptors stably expressed in HEK293 cells
  JOURNAL   Neuropharmacology 36 (4-5), 713-720 (1997)
   PUBMED   9225298
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Kohen,R., Metcalf,M.A., Khan,N., Druck,T., Huebner,K.,
            Lachowicz,J.E., Meltzer,H.Y., Sibley,D.R., Roth,B.L. and
            Hamblin,M.W.
  TITLE     Cloning, characterization, and chromosomal localization of a human
            5-HT6 serotonin receptor
  JOURNAL   J Neurochem 66 (1), 47-56 (1996)
   PUBMED   8522988
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Ruat,M., Traiffort,E., Arrang,J.M., Tardivel-Lacombe,J., Diaz,J.,
            Leurs,R. and Schwartz,J.C.
  TITLE     A novel rat serotonin (5-HT6) receptor: molecular cloning,
            localization and stimulation of cAMP accumulation
  JOURNAL   Biochem Biophys Res Commun 193 (1), 268-276 (1993)
   PUBMED   8389146
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Monsma,F.J. Jr., Shen,Y., Ward,R.P., Hamblin,M.W. and Sibley,D.R.
  TITLE     Cloning and expression of a novel serotonin receptor with high
            affinity for tricyclic psychotropic drugs
  JOURNAL   Mol Pharmacol 43 (3), 320-327 (1993)
   PUBMED   7680751
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 30, 2015 this sequence version replaced NP_077341.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L19656.1, L03202.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..438
                     /product="5-hydroxytryptamine receptor 6"
                     /note="5-HT-6; ST-B17; serotonin receptor 6; 5-HT6;
                     5-hydroxytryptamine (serotonin) receptor 6, G
                     protein-coupled"
                     /calculated_mol_wt=46669
     Site            9
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31388.2)"
     Site            28..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Region          29..331
                     /region_name="7tmA_5-HT6"
                     /note="serotonin receptor subtype 6, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15054"
                     /db_xref="CDD:320182"
     Region          29..54
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320182"
     Region          61..87
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320182"
     Site            63..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Site            97..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Region          99..129
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320182"
     Site            order(102,106..107,110..111,182,189,192..193,196,281,
                     284..285,288,302,306,310)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320182"
     Region          141..164
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320182"
     Site            143..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Region          185..214
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320182"
     Site            186..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Region          261..291
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320182"
     Site            267..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     Region          299..324
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320182"
     Site            300..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31388.2)"
     CDS             1..438
                     /gene="Htr6"
                     /coded_by="NM_024365.2:319..1635"
                     /db_xref="GeneID:64354"
                     /db_xref="RGD:62044"
ORIGIN      
        1 mvpepgpvns stpawgpgpp papggsgwva aalcvvivlt aaansllivl ictqpalrnt
       61 snfflvslft sdlmvglvvm ppamlnalyg rwvlarglcl lwtafdvmcc sasilnlcli
      121 sldryllils plryklrmta pralalilga wslaalasfl plllgwhelg kartpapgqc
      181 rllaslpfvl vasgvtfflp sgaicftycr illaarkqav qvaslttgta gqaletlqvp
      241 rtprpgmesa dsrrlatkhs rkalkasltl gillgmffvt wlpffvania qavcdcispg
      301 lfdvltwlgy cnstmnpiiy plfmrdfkra lgrflpcvhc ppehraspas psmwtshsga
      361 rpglslqqvl plplppnsds dsasggtsgl qltaqlllpg eatrdppppt rattvvnffv
      421 tdsvepeirp hplsspvn
//
LOCUS       NP_997714                406 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RING1 [Rattus norvegicus].
ACCESSION   NP_997714 XP_228012
VERSION     NP_997714.2
DBSOURCE    REFSEQ: accession NM_212549.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Liu,H., Ji,W., Gong,P., Liu,C., Duan,C., Gao,Y., Liu,X., Zhang,D.,
            Zhu,S. and Gong,L.
  TITLE     Spatiotemporal Patterns of RING1 Expression after Rat Spinal Cord
            Injury
  JOURNAL   Neurochem Res 42 (4), 1191-1201 (2017)
   PUBMED   28032293
  REMARK    GeneRIF: RING1 protein levels were increased at day 3 after spinal
            cord injury and then decreased gradually.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Gil,J. and O'Loghlen,A.
  TITLE     PRC1 complex diversity: where is it taking us?
  JOURNAL   Trends Cell Biol 24 (11), 632-641 (2014)
   PUBMED   25065329
  REMARK    Review article
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Simon,J.A. and Kingston,R.E.
  TITLE     Occupying chromatin: Polycomb mechanisms for getting to genomic
            targets, stopping transcriptional traffic, and staying put
  JOURNAL   Mol Cell 49 (5), 808-824 (2013)
   PUBMED   23473600
  REMARK    Review article
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Takahashi,M. and Osumi,N.
  TITLE     Pax6 regulates boundary-cell specification in the rat hindbrain
  JOURNAL   Mech Dev 128 (5-6), 289-302 (2011)
   PUBMED   21501682
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
REFERENCE   6  (residues 1 to 406)
  AUTHORS   del Mar Lorente,M., Marcos-Gutierrez,C., Perez,C., Schoorlemmer,J.,
            Ramirez,A., Magin,T. and Vidal,M.
  TITLE     Loss- and gain-of-function mutations show a polycomb group function
            for Ring1A in mice
  JOURNAL   Development 127 (23), 5093-5100 (2000)
   PUBMED   11060235
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Walter,L. and Gunther,E.
  TITLE     Physical mapping and evolution of the centromeric class I
            gene-containing region of the rat MHC
  JOURNAL   Immunogenetics 51 (10), 829-837 (2000)
   PUBMED   10970097
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Schoorlemmer,J., Marcos-Gutierrez,C., Were,F., Martinez,R.,
            Garcia,E., Satijn,D.P., Otte,A.P. and Vidal,M.
  TITLE     Ring1A is a transcriptional repressor that interacts with the
            Polycomb-M33 protein and is expressed at rhombomere boundaries in
            the mouse hindbrain
  JOURNAL   EMBO J 16 (19), 5930-5942 (1997)
   PUBMED   9312051
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Walter,L., Fischer,K. and Gunther,E.
  TITLE     Physical mapping of the Ring1, Ring2, Ke6, Ke4, Rxrb, Col11a2, and
            RT1.Hb genes in the rat major histocompatibility complex
  JOURNAL   Immunogenetics 44 (3), 218-221 (1996)
   PUBMED   8662089
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1 and BC098635.1.
            
            On Aug 31, 2012 this sequence version replaced NP_997714.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098635.1, SRR22582424.1901320.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..406
                     /product="E3 ubiquitin-protein ligase RING1"
                     /EC_number="2.3.2.27"
                     /note="polycomb complex protein RING1; RING-type E3
                     ubiquitin transferase RING1"
                     /calculated_mol_wt=42530
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          30..234
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          43..112
                     /region_name="RING-HC_RING1"
                     /note="RING finger, HC subclass, found in really
                     interesting new gene 1 protein (RING1) and similar
                     proteins; cd16739"
                     /db_xref="CDD:438397"
     Site            order(45..46,60,62..63,65,67,74,78,82,90,92..95,98..100,
                     102..103,105..106,109..110)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438397"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          151..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          201..204
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          230..406
                     /region_name="Necessary for interaction with CBX2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06587; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB6.2)"
     Region          261..400
                     /region_name="RAWUL_RING1"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in really interesting new gene 1
                     protein (RING1); cd17166"
                     /db_xref="CDD:340686"
     Site            order(263..265,283..286,290,293..295,297..298,301..302,
                     392..394)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340686"
     Region          309..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGB6.2)"
     CDS             1..406
                     /gene="Ring1"
                     /gene_synonym="Ring1A"
                     /coded_by="NM_212549.2:197..1417"
                     /db_xref="GeneID:309626"
                     /db_xref="RGD:3576"
ORIGIN      
        1 mttpanaqna sktwelslye lhrtpqeaim dgteiavspr slhselmcpi cldmlkntmt
       61 tkeclhrfcs dcivtalrsg nkecptcrkk lvskrslrpd pnfdaliski ypsreeyeah
      121 qdrvlirlsr lhnqqalsss ieeglrmqam hraqrvrrpm pgsdqtttms ggegepgege
      181 gdgedissds apdsapgpap krprgggagg ssvgtgggaa ggacggagse dsgdrggtlg
      241 ggtlgppspp gapsppepgg eielvfrphp llvekgeycq tryvkttgna tvdhlskyla
      301 lrialerrqq qetvepggpg ggasdtggpd ggggergvsg ggegpeepal pslegvsekq
      361 ytiyiapggg afttlngslt lelvnekfwk vsrplelcya ptkdpk
//
LOCUS       NP_001263233             966 aa            linear   ROD 27-APR-2025
DEFINITION  disks large-associated protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001263233
VERSION     NP_001263233.1
DBSOURCE    REFSEQ: accession NM_001276304.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Chua,J.J., Schob,C., Rehbein,M., Gkogkas,C.G., Richter,D. and
            Kindler,S.
  TITLE     Synthesis of two SAPAP3 isoforms from a single mRNA is mediated via
            alternative translational initiation
  JOURNAL   Sci Rep 2, 484 (2012)
   PUBMED   22761992
  REMARK    GeneRIF: alternative translation initiation events appear to
            regulate relative expression of distinct SAPAP3 isoforms in
            different brain regions, which may function to influence synaptic
            plasticity.
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Welch,J.M., Lu,J., Rodriguiz,R.M., Trotta,N.C., Peca,J., Ding,J.D.,
            Feliciano,C., Chen,M., Adams,J.P., Luo,J., Dudek,S.M.,
            Weinberg,R.J., Calakos,N., Wetsel,W.C. and Feng,G.
  TITLE     Cortico-striatal synaptic defects and OCD-like behaviours in
            Sapap3-mutant mice
  JOURNAL   Nature 448 (7156), 894-900 (2007)
   PUBMED   17713528
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Castejon,O.J., Fuller,L. and Dailey,M.E.
  TITLE     Localization of synapsin-I and PSD-95 in developing postnatal rat
            cerebellar cortex
  JOURNAL   Brain Res Dev Brain Res 151 (1-2), 25-32 (2004)
   PUBMED   15246689
  REMARK    GeneRIF: During the first postnatal week,PSD-95 immunoreactive
            strongly concentrated in the Purkinje cell layer.By P14, PSD-95
            localized to many small puncta in the ML and to large clusters at
            mossy fiber rosettes in the glomerular layer.
REFERENCE   4  (residues 1 to 966)
  AUTHORS   Kindler,S., Rehbein,M., Classen,B., Richter,D. and Bockers,T.M.
  TITLE     Distinct spatiotemporal expression of SAPAP transcripts in the
            developing rat brain: a novel dendritically localized mRNA
  JOURNAL   Brain Res Mol Brain Res 126 (1), 14-21 (2004)
   PUBMED   15207911
REFERENCE   5  (residues 1 to 966)
  AUTHORS   Welch,J.M., Wang,D. and Feng,G.
  TITLE     Differential mRNA expression and protein localization of the
            SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of
            the mouse
  JOURNAL   J Comp Neurol 472 (1), 24-39 (2004)
   PUBMED   15024750
REFERENCE   6  (residues 1 to 966)
  AUTHORS   Kitano,J., Yamazaki,Y., Kimura,K., Masukado,T., Nakajima,Y. and
            Nakanishi,S.
  TITLE     Tamalin is a scaffold protein that interacts with multiple neuronal
            proteins in distinct modes of protein-protein association
  JOURNAL   J Biol Chem 278 (17), 14762-14768 (2003)
   PUBMED   12586822
REFERENCE   7  (residues 1 to 966)
  AUTHORS   Kawabe,H., Hata,Y., Takeuchi,M., Ide,N., Mizoguchi,A. and Takai,Y.
  TITLE     nArgBP2, a novel neural member of ponsin/ArgBP2/vinexin family that
            interacts with synapse-associated protein 90/postsynaptic
            density-95-associated protein (SAPAP)
  JOURNAL   J Biol Chem 274 (43), 30914-30918 (1999)
   PUBMED   10521485
REFERENCE   8  (residues 1 to 966)
  AUTHORS   Tu,J.C., Xiao,B., Naisbitt,S., Yuan,J.P., Petralia,R.S.,
            Brakeman,P., Doan,A., Aakalu,V.K., Lanahan,A.A., Sheng,M. and
            Worley,P.F.
  TITLE     Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
            postsynaptic density proteins
  JOURNAL   Neuron 23 (3), 583-592 (1999)
   PUBMED   10433269
REFERENCE   9  (residues 1 to 966)
  AUTHORS   Takeuchi,M., Hata,Y., Hirao,K., Toyoda,A., Irie,M. and Takai,Y.
  TITLE     SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
            postsynaptic density
  JOURNAL   J Biol Chem 272 (18), 11943-11951 (1997)
   PUBMED   9115257
REFERENCE   10 (residues 1 to 966)
  AUTHORS   Yehiely,F., Bamborough,P., Da Costa,M., Perry,B.J., Thinakaran,G.,
            Cohen,F.E., Carlson,G.A. and Prusiner,S.B.
  TITLE     Identification of candidate proteins binding to prion protein
  JOURNAL   Neurobiol Dis 3 (4), 339-355 (1997)
   PUBMED   9173930
  REMARK    Erratum:[Neurobiol Dis 2002 Jun;10(1):67-8]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            resulting isoform (2) is shorter compared to isoform 1. The 5' UTR
            and 5' coding region for variant 2 are identical to those of
            variant 1 so the synthesis of two isoforms based on alternate
            in-frame translation starts discussed in PMID: 227619920 for
            variant 1 may also occur.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY530299.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760393, SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..966
                     /product="disks large-associated protein 3 isoform 2"
                     /note="disks large-associated protein 3;
                     PSD-95/SAP90-binding protein 3; SAP90/PSD-95-associated
                     protein 3; PSD-95/SAP90-associated protein-3; discs large
                     homolog associated protein 3"
                     /calculated_mol_wt=104577
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Region          52..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Region          93
                     /region_name="alternative start codon"
     Region          137..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Region          181..289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Region          398..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Region          515..>607
                     /region_name="PHA03418"
                     /note="hypothetical E4 protein; Provisional"
                     /db_xref="CDD:177646"
     Region          529..582
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Region          626..966
                     /region_name="GKAP"
                     /note="Guanylate-kinase-associated protein (GKAP) protein;
                     pfam03359"
                     /db_xref="CDD:460897"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Region          739..788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Region          895..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97838.2)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     Site            954
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PFD5; propagated from
                     UniProtKB/Swiss-Prot (P97838.2)"
     CDS             1..966
                     /gene="Dlgap3"
                     /gene_synonym="DAP-3; Dap3; SAPAP3"
                     /coded_by="NM_001276304.1:138..3038"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:286923"
                     /db_xref="RGD:708349"
ORIGIN      
        1 mrgyhgdrgs hprparfadq qhmdvgpaar apyllgsrea fsteprfcap raglghlspe
       61 gplslsegps svgpeggpgg vgagggsstf prmypgqgpf dtcedcvghp qgkgatrlpp
      121 tlldqfekql pvqqdgfhtl pyqrgpagpg pgpgsgaape arsespsrir hlvhsvqklf
      181 akshsleapg krdyngpkae grsssggdsy sgpgsggppt shhhhhhhhh hhhqsrhgkr
      241 skskdrkgdg rhqtkatgww ssddnldsds gflggrppge pggpfcldap dgsyrdlsfk
      301 grsggsegrc lactgmsmsl dgqsvkrsaw htmmvsqgrd gypgagpgkg llgpetkaka
      361 rtyhylqvpq ddwggyptgg kdgeipcrrm rsgsyikamg deesgdsdgs pktspkalar
      421 rfasrrsssv dtarinccvp prihprssip gysrslttgq lseefnqqle avcgsvfgel
      481 esqavdaldl pgcfrmrshs ylraiqagcs qdddclplla apasvsgrpg ssfnfrkapp
      541 pippgsqapp risitaqsst dsahesftaa egparrcssa dgldgptmga rtlelapvpp
      601 raspkpptli iktipgreel rslarqrkwr psigvqveti sdsdtenrsr refhsigvqv
      661 eedkrrarfk rsnsvtagvq adleleglag latvatedka lqfgrsfqrh asepqpgpra
      721 ptysvfrtvh tqgqwayreg yplpyeppat dgspgpppvp apgpgsgrrd swmergsrsl
      781 pdsgrtspcp rdgewfikml raeveklehw cqqmereaed yelpeeilek irsavgstql
      841 llsqkvqqff rlcqqsldla gfwdllqlsi edvtlkflel qqlkanswkl lepkeekkvp
      901 ppipkkpsrg rgvpvkersl dsvdrqrqea rkrllaakra asfrhssate sadsieiyip
      961 eaqtrl
//
LOCUS       NP_001257604             250 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 9 [Rattus norvegicus].
ACCESSION   NP_001257604
VERSION     NP_001257604.1
DBSOURCE    REFSEQ: accession NM_001270675.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (9) lacks two alternate in-frame
            exons and uses an alternate exon in place of another exon in the 3'
            end of the gene, compared to variant 1. The resulting isoform (9)
            has the same N- and C-termini but is shorter and has a different
            internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..250
                     /product="troponin T, fast skeletal muscle isoform 9"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29609
     Region          54..190
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..250
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270675.1:117..869"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeeevqeeek prpkltapki pegekvdfdd iqkkrqnkdl
       61 melqalidsh fearkkeeee lialkeriek rraeraeqqr iraekererq nrlaeekarr
      121 eeedakrrae ddlkkkkals smganyssyl akadqkrgkk qtaremkkki laerrkplni
      181 dhlsddklrd kakelwdtly qletdkfefg eklkrqkydi mtvrarveml akfskkagat
      241 akgkvggrwk
//
LOCUS       NP_671694                221 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione peroxidase 6 precursor [Rattus norvegicus].
ACCESSION   NP_671694
VERSION     NP_671694.1
DBSOURCE    REFSEQ: accession NM_147165.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Cueto-Urena,C., Ramirez-Exposito,M.J., Mayas,M.D.,
            Carrera-Gonzalez,M.P., Godoy-Hurtado,A. and Martinez-Martos,J.M.
  TITLE     Glutathione Peroxidase gpx1 to gpx8 Genes Expression in
            Experimental Brain Tumors Reveals Gender-Dependent Patterns
  JOURNAL   Genes (Basel) 14 (9), 1674 (2023)
   PUBMED   37761814
  REMARK    GeneRIF: Glutathione Peroxidase gpx1 to gpx8 Genes Expression in
            Experimental Brain Tumors Reveals Gender-Dependent Patterns.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Sorolla,M.A., Reverter-Branchat,G., Tamarit,J., Ferrer,I., Ros,J.
            and Cabiscol,E.
  TITLE     Proteomic and oxidative stress analysis in human brain samples of
            Huntington disease
  JOURNAL   Free Radic Biol Med 45 (5), 667-678 (2008)
   PUBMED   18588971
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Dear,T.N., Campbell,K. and Rabbitts,T.H.
  TITLE     Molecular cloning of putative odorant-binding and
            odorant-metabolizing proteins
  JOURNAL   Biochemistry 30 (43), 10376-10382 (1991)
   PUBMED   1931961
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M76733.1 and JAXUCZ010000017.1.
            
            Summary: This gene encodes a member of the glutathione peroxidase
            family. Glutathione peroxidases catalyze the reduction of a variety
            of hydroperoxides using glutathione as a specific electron donor
            substrate, and thereby protect cells against oxidative damage.
            Expression of this gene is restricted to embryos and adult
            olfactory epithelium. The mouse and rat orthologs contain a
            cysteine (Cys) residue at the active site, unlike the human
            counterpart, which is a selenoprotein, containing selenocysteine
            (Sec) instead. [provided by RefSeq, Jul 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: M76733.1, SRR22582424.2047321.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q11"
     Protein         1..221
                     /product="glutathione peroxidase 6 precursor"
                     /EC_number="1.11.1.9"
                     /note="GPx-6; GSHPx-6; odorant-metabolizing protein RY2D1"
                     /calculated_mol_wt=22789
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     mat_peptide     20..221
                     /product="Glutathione peroxidase 6. /id=PRO_0000013083"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64625.1)"
                     /calculated_mol_wt=22789
     Region          39..211
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(73,107,181)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            order(106,109,111,114,117,121)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..221
                     /gene="Gpx6"
                     /gene_synonym="OBPII; Ry2d1"
                     /coded_by="NM_147165.2:46..711"
                     /db_xref="GeneID:259233"
                     /db_xref="RGD:628789"
ORIGIN      
        1 mtqqfwgpcl fslfmavlaq etldpqkskv dcnkgvagtv yeygantldg geyvqfqqya
       61 gkhilfvnva sfcgltatyp elntlqeelr pfnvsvlgfp cnqfgkqepg knseillglk
      121 yvrpgggfvp nfqlfekgdv ngdneqkvfs flksscppts ellgspehlf wdpmkvhdir
      181 wnfekflvgp dgapvmrwfh qtpvrvvqsd imeylnqtrt q
//
LOCUS       NP_001296189             883 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001296189 XP_006238246
VERSION     NP_001296189.1
DBSOURCE    REFSEQ: accession NM_001309260.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Carnegie,G.K., Means,C.K. and Scott,J.D.
  TITLE     A-kinase anchoring proteins: from protein complexes to physiology
            and disease
  JOURNAL   IUBMB Life 61 (4), 394-406 (2009)
   PUBMED   19319965
  REMARK    Review article
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Kinderman,F.S., Kim,C., von Daake,S., Ma,Y., Pham,B.Q.,
            Spraggon,G., Xuong,N.H., Jennings,P.A. and Taylor,S.S.
  TITLE     A dynamic mechanism for AKAP binding to RII isoforms of
            cAMP-dependent protein kinase
  JOURNAL   Mol Cell 24 (3), 397-408 (2006)
   PUBMED   17081990
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Tasken,K. and Aandahl,E.M.
  TITLE     Localized effects of cAMP mediated by distinct routes of protein
            kinase A
  JOURNAL   Physiol Rev 84 (1), 137-167 (2004)
   PUBMED   14715913
  REMARK    Review article
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Dong,F., Feldmesser,M., Casadevall,A. and Rubin,C.S.
  TITLE     Molecular characterization of a cDNA that encodes six isoforms of a
            novel murine A kinase anchor protein
  JOURNAL   J Biol Chem 273 (11), 6533-6541 (1998)
   PUBMED   9497389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On May 28, 2015 this sequence version replaced XP_006238246.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments and orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.15284.1,
                                           SRR26643295.21425.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..883
                     /product="A-kinase anchor protein 2 isoform 1"
                     /note="A-kinase anchor protein 2; A kinase (PRKA) anchor
                     protein 2; paralemmin 2; paralemmin-2-like; A-kinase
                     anchoring protein 2"
                     /calculated_mol_wt=97252
     Region          14..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          103..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          233..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          409..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          506..577
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          576..589
                     /region_name="PKA-RII subunit binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          595..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          <613..810
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          <721..875
                     /region_name="AKAP2_C"
                     /note="A-kinase anchor protein 2 C-terminus; pfam15304"
                     /db_xref="CDD:464630"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          740..814
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     CDS             1..883
                     /gene="Pakap"
                     /gene_synonym="AKAP-2; Akap2; Palm2"
                     /coded_by="NM_001309260.1:196..2847"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298024"
                     /db_xref="RGD:1305135"
ORIGIN      
        1 meigvsvaec ksvpgitstp hskdhsspfy spshnglltd hhesldndva reiqyldevl
       61 eanccdssvd gtyngisspe pgaailvssl gspahsatkv epiekasgrq lpphielsrs
      121 psdsmaeger anghstdqpq dmlgnslqap aspssstssh cssrdgeftl ttlkkeakfe
      181 lrafhedkkp sklfeedehe keqfcirkvr pseemielek errelirsqa vkknpgiaak
      241 wwnppqekti eeqldeehle shrkykerke kraqqeqlql qqqqqqqlqq lqqlqqqqqq
      301 qlstsqlcta paahehldsi ehtkedvvte qidfsaarkq fqqmensrqt lakgqstprl
      361 fsikpfykpl gsinsdkppt ilrpatiggt vedsstqaak eqkalcvses qsagagtgna
      421 atqgkegpys epskrgplsk lwaedgefts aravltvvkd edhgildqfs rsvnvsltqe
      481 eldsgldels vrsqdttvle tlsndfsmdn isdsgasnet pnalqensla dfslpqtpqt
      541 dnpsegregv sksfsdhgfy spsstlgdsp svddpleyqa gllvqnaiqq aiaeqvdkae
      601 vhtskegseq qepgamveea gsqapgsekp qgmfappqvs spvqekrdvl pkilpgedkt
      661 lrekgpsqpp tavqpsgpvn mketrpeggy fskyseaael rstasllatq esdvmvgpfk
      721 lrsrkqrtls mieeeiraaq ereeelkrqr qvrqstpspr aqnapslpsr ttcyktapgk
      781 iekvkpppsp ttegpslqpd lapeeaagaq rpknlmqtlm edyethkskr rermddssyt
      841 skllsckvts evleatrvnr rksalalrwe agiyanqeee dne
//
LOCUS       NP_073186                416 aa            linear   ROD 27-APR-2025
DEFINITION  neurotensin receptor type 2 [Rattus norvegicus].
ACCESSION   NP_073186
VERSION     NP_073186.1
DBSOURCE    REFSEQ: accession NM_022695.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Pandey,S. and Barson,J.R.
  TITLE     Heightened Exploratory Behavior Following Chronic Excessive Ethanol
            Drinking: Mediation by Neurotensin Receptor Type 2 in the Anterior
            Paraventricular Thalamus
  JOURNAL   Alcohol Clin Exp Res 44 (9), 1747-1759 (2020)
   PUBMED   32623746
  REMARK    GeneRIF: Heightened Exploratory Behavior Following Chronic
            Excessive Ethanol Drinking: Mediation by Neurotensin Receptor Type
            2 in the Anterior Paraventricular Thalamus.
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Steele,F.F. 3rd, Whitehouse,S.C., Aday,J.S. and Prus,A.J.
  TITLE     Neurotensin NTS1 and NTS2 receptor agonists produce anxiolytic-like
            effects in the 22-kHz ultrasonic vocalization model in rats
  JOURNAL   Brain Res 1658, 31-35 (2017)
   PUBMED   28089664
  REMARK    GeneRIF: Study suggests that NTS1 and NTS2 neurotensin receptor
            mechanisms appear involved in fear conditioning processes and that
            agonists for neurotensin receptors may be pursued as novel
            anxiolytic drugs.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Thomas,J.B., Giddings,A.M., Wiethe,R.W., Olepu,S., Warner,K.R.,
            Sarret,P., Gendron,L., Longpre,J.M., Zhang,Y., Runyon,S.P. and
            Gilmour,B.P.
  TITLE     Identification of
            N-[(5-{[(4-methylphenyl)sulfonyl]amino}-3-(trifluoroacetyl)-1H-
            indol-1-yl)acetyl]-l-leucine (NTRC-824), a neurotensin-like
            nonpeptide compound selective for the neurotensin receptor type 2
  JOURNAL   J Med Chem 57 (17), 7472-7477 (2014)
   PUBMED   25157640
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Buhler,A.V., Proudfit,H.K. and Gebhart,G.F.
  TITLE     Neurotensin-produced antinociception in the rostral ventromedial
            medulla is partially mediated by spinal cord norepinephrine
  JOURNAL   Pain 135 (3), 280-290 (2008)
   PUBMED   17664042
  REMARK    GeneRIF: These results also provide evidence that activation of
            NTR1 in the RVM produces antinociception through spinal release of
            norepinephrine (NE) and serotonin, and that activation of NTR2 in
            the RVM produces antinociception mediated by spinal release of NE.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Perron,A., Sharif,N., Sarret,P., Stroh,T. and Beaudet,A.
  TITLE     NTS2 modulates the intracellular distribution and trafficking of
            NTS1 via heterodimerization
  JOURNAL   Biochem Biophys Res Commun 353 (3), 582-590 (2007)
   PUBMED   17188644
  REMARK    GeneRIF: NTS1/NTS2 heterodimerization affects the intracellular
            distribution and trafficking of NTS1 by making it more similar to
            that of NTS2 as witnessed in cells expressing NTS2 alone.
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Gendron,L., Perron,A., Payet,M.D., Gallo-Payet,N., Sarret,P. and
            Beaudet,A.
  TITLE     Low-affinity neurotensin receptor (NTS2) signaling:
            internalization-dependent activation of extracellular
            signal-regulated kinases 1/2
  JOURNAL   Mol Pharmacol 66 (6), 1421-1430 (2004)
   PUBMED   15361549
  REMARK    GeneRIF: NTS2 is a bona fide NT receptor and that activation of
            this receptor by NT or NT analogs results in an
            internalization-dependent activation of the ERK1/2 signaling
            cascade.
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Sarret,P., Perron,A., Stroh,T. and Beaudet,A.
  TITLE     Immunohistochemical distribution of NTS2 neurotensin receptors in
            the rat central nervous system
  JOURNAL   J Comp Neurol 461 (4), 520-538 (2003)
   PUBMED   12746866
  REMARK    GeneRIF: The distribution of NTS2-like immunoreactivity largely
            exceeded that of neurotensin terminal fields, and some of the
            highest concentrations of the receptor were found in areas devoid
            of neurotensinergic inputs.
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Sarret,P., Gendron,L., Kilian,P., Nguyen,H.M., Gallo-Payet,N.,
            Payet,M.D. and Beaudet,A.
  TITLE     Pharmacology and functional properties of NTS2 neurotensin
            receptors in cerebellar granule cells
  JOURNAL   J Biol Chem 277 (39), 36233-36243 (2002)
   PUBMED   12084713
  REMARK    GeneRIF: Expression and function of NTR2 receptors in rat
            cerebellar granule cells
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Mazella,J., Botto,J.M., Guillemare,E., Coppola,T., Sarret,P. and
            Vincent,J.P.
  TITLE     Structure, functional expression, and cerebral localization of the
            levocabastine-sensitive neurotensin/neuromedin N receptor from
            mouse brain
  JOURNAL   J Neurosci 16 (18), 5613-5620 (1996)
   PUBMED   8795617
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Chalon,P., Vita,N., Kaghad,M., Guillemot,M., Bonnin,J., Delpech,B.,
            Le Fur,G., Ferrara,P. and Caput,D.
  TITLE     Molecular cloning of a levocabastine-sensitive neurotensin binding
            site
  JOURNAL   FEBS Lett 386 (2-3), 91-94 (1996)
   PUBMED   8647296
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X97121.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X97121.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..416
                     /product="neurotensin receptor type 2"
                     /note="high-affinity levocabastine-sensitive neurotensin
                     receptor; NT-R-2; NTR2 receptor"
                     /calculated_mol_wt=46135
     Region          33..369
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            33..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          35..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            65..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          69..91
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          109..131
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            110..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            155..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          204..227
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          296..318
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Region          337..362
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            338..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63384.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63384.1)"
     CDS             1..416
                     /gene="Ntsr2"
                     /coded_by="NM_022695.2:39..1289"
                     /db_xref="GeneID:64636"
                     /db_xref="RGD:70962"
ORIGIN      
        1 metsspwppr pspsaglsle arlgvdtrlw akvlftalys lifafgtagn alsvhvvlka
       61 ragrpgrlry hvlslalsal llllvsmpme lynfvwshyp wvfgdlgcrg yyfvrelcay
      121 atvlsvasls aerclavcqp lrarrlltpr rtrrllslvw vaslglalpm avimgqkhev
      181 esadgepepa srvctvlvsr atlqvfiqvn vlvsfalpla ltaflngitv nhlmalysqv
      241 psasaqvssi psrlellsee gllgfitwrk tlslgvqasl vrhkdasqir slqhsaqvlr
      301 aivavyvicw lpyharrlmy cyipddgwtn elydfyhyfy mvtntlfyvs savtpilyna
      361 vsssfrklfl eslgslcgeq hslvplpqea pesttstysf rlwgsprnps lgeiqv
//
LOCUS       NP_599230               1024 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat and BTB/POZ domain-containing protein 2 [Rattus
            norvegicus].
ACCESSION   NP_599230
VERSION     NP_599230.2
DBSOURCE    REFSEQ: accession NM_134403.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Roy,A. and Pahan,K.
  TITLE     Ankyrin repeat and BTB/POZ domain containing protein-2 inhibits the
            aggregation of alpha-synuclein: implications for Parkinson's
            disease
  JOURNAL   FEBS Lett 587 (21), 3567-3574 (2013)
   PUBMED   24076025
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Hayashi,Y., Ichinose,M., Yuasa,H., Tatematsu,M. and Ishibashi,M.
  TITLE     Cca3, the mRNA level of which transiently decreases before
            initiation of DNA synthesis in regenerating rat liver cells
  JOURNAL   FEBS Lett 406 (1-2), 147-150 (1997)
   PUBMED   9109406
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB609664.1, AB000216.1, CV110237.1, DY545654.1, CB714885.1 and
            BQ203018.1.
            
            On Jul 17, 2010 this sequence version replaced NP_599230.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000216.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q32"
     Protein         1..1024
                     /product="ankyrin repeat and BTB/POZ domain-containing
                     protein 2"
                     /note="ankyrin repeat and BTB (POZ) domain containing 2;
                     confluent 3Y1 cell-associated protein"
                     /calculated_mol_wt=113343
     Region          187..295
                     /region_name="HFD_ABTB2-like"
                     /note="histone-fold domain found in ankyrin repeat and
                     BTB/POZ domain-containing protein 2 (ABTB2) and similar
                     proteins; cd22913"
                     /db_xref="CDD:467038"
     Region          <498..670
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          521..550
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O08764.1)"
     Region          522..565
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(523,527..528,531..533,535..536,540,543,565,567,569,
                     573..574,577..579,581..582,586,589,604,606,608,612..613,
                     616..618,620..621,625,628)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          567..604
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          567..596
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O08764.1)"
     Region          606..635
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O08764.1)"
     Region          606..631
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          649..678
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O08764.1)"
     Region          820..953
                     /region_name="BTB_POZ_ABTB2_BPOZ2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Ankyrin repeat
                     and BTB/POZ domain-containing protein 2 (ABTB2); cd18350"
                     /db_xref="CDD:349659"
     Region          946..1024
                     /region_name="BACK_ABTB2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     ankyrin repeat and BTB/POZ domain-containing protein 2
                     (ABTB2); cd18526"
                     /db_xref="CDD:350601"
     CDS             1..1024
                     /gene="Abtb2"
                     /gene_synonym="Cca3"
                     /coded_by="NM_134403.2:401..3475"
                     /db_xref="GeneID:171440"
                     /db_xref="RGD:620724"
ORIGIN      
        1 magtysstlk tledltldsg ygagdscrsl slsssksnsq alnssapqhr gaawwcysgs
       61 mnsrhnswdt vntvlpedpe vadlfsrcpr lpeleefpwt egdvarvlrk svggrrlpsf
      121 saeavrrlag llrralirva reaqrlsvlh akctrfevqs avrlvhswal aescalaavk
      181 alslysmsag dglrrgksar cgltfsvgrf frwmvdtris vriheyaais ltacmenlve
      241 eirarvlasq spdgggaggg evsaealemv inndaelwgv lqpyehlicg knangvlslp
      301 ayfspynggs lghderaday aqlelrtleq sllatcvgsi selsdlvsra mhhmqgrhpl
      361 cpgtsparqa rqppqpitws pdalhtlyyf lrcpqmesme npnldpprmt lnnerpfmll
      421 pplmewmrva ityaehrrsl tvdsgdirqa arlllpgldc eprqlkpecc fssfrrldar
      481 aaterfnqdl gfrmlncgrt dlisqaieal gpdgvntmdd qgltplmyac atgdeamvqm
      541 lidaganldi qvpsnsprhp svhpdsrhwt sltfavlhgh isvvqlllda gahvegsavn
      601 sgedsyaetp lqlasaagny elvslllsrg adpllsmlea ngmasslhed mncfshsaah
      661 ghrnvlrkll tqpqqakadv lsleeilaeg veesdtssqg ssegpvrlsr trtkalqeam
      721 yysaehgyvd itmelralgv pwklhiwies lrtsfsqsry svvqgllrdf ssikeeeyne
      781 elvteglqlm fdilktsknd svlqqlatif thcygtspip sipeirktlp arldphflnn
      841 kemsdvtflv egklfyahkv llvtasnrfk tlmtnkseqd gdnsktieis dikyhifqml
      901 mqylyyggte smeiptadil qllsaanlfq ldalqrhcei lcsqtlsves avntykyaki
      961 hnapelalfc egfflkhmka lleqdafrql iygrsskvqg ldplqdlqst laervhsvyv
     1021 tsrv
//
LOCUS       NP_998730                406 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 57 [Rattus norvegicus].
ACCESSION   NP_998730 XP_342080
VERSION     NP_998730.2
DBSOURCE    REFSEQ: accession NM_213565.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Takahashi,N., Coluccio,A., Thorball,C.W., Planet,E., Shi,H.,
            Offner,S., Turelli,P., Imbeault,M., Ferguson-Smith,A.C. and
            Trono,D.
  TITLE     ZNF445 is a primary regulator of genomic imprinting
  JOURNAL   Genes Dev 33 (1-2), 49-54 (2019)
   PUBMED   30602440
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Buck-Koehntop,B.A. and Defossez,P.A.
  TITLE     On how mammalian transcription factors recognize methylated DNA
  JOURNAL   Epigenetics 8 (2), 131-137 (2013)
   PUBMED   23324617
  REMARK    Review article
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Gehrig,S.M., van der Poel,C., Sayer,T.A., Schertzer,J.D.,
            Henstridge,D.C., Church,J.E., Lamon,S., Russell,A.P., Davies,K.E.,
            Febbraio,M.A. and Lynch,G.S.
  TITLE     Hsp72 preserves muscle function and slows progression of severe
            muscular dystrophy
  JOURNAL   Nature 484 (7394), 394-398 (2012)
   PUBMED   22495301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Li,X., Ito,M., Zhou,F., Youngson,N., Zuo,X., Leder,P. and
            Ferguson-Smith,A.C.
  TITLE     A maternal-zygotic effect gene, Zfp57, maintains both maternal and
            paternal imprints
  JOURNAL   Dev Cell 15 (4), 547-557 (2008)
   PUBMED   18854139
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Mackay,D.J., Callaway,J.L., Marks,S.M., White,H.E., Acerini,C.L.,
            Boonen,S.E., Dayanikli,P., Firth,H.V., Goodship,J.A., Haemers,A.P.,
            Hahnemann,J.M., Kordonouri,O., Masoud,A.F., Oestergaard,E.,
            Storr,J., Ellard,S., Hattersley,A.T., Robinson,D.O. and Temple,I.K.
  TITLE     Hypomethylation of multiple imprinted loci in individuals with
            transient neonatal diabetes is associated with mutations in ZFP57
  JOURNAL   Nat Genet 40 (8), 949-951 (2008)
   PUBMED   18622393
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Alonso,M.B., Zoidl,G., Taveggia,C., Bosse,F., Zoidl,C., Rahman,M.,
            Parmantier,E., Dean,C.H., Harris,B.S., Wrabetz,L., Muller,H.W.,
            Jessen,K.R. and Mirsky,R.
  TITLE     Identification and characterization of ZFP-57, a novel zinc finger
            transcription factor in the mammalian peripheral nervous system
  JOURNAL   J Biol Chem 279 (24), 25653-25664 (2004)
   PUBMED   15070898
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Okazaki,S., Tanase,S., Choudhury,B.K., Setoyama,K., Miura,R.,
            Ogawa,M. and Setoyama,C.
  TITLE     A novel nuclear protein with zinc fingers down-regulated during
            early mammalian cell differentiation
  JOURNAL   J Biol Chem 269 (9), 6900-6907 (1994)
   PUBMED   8120052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CA511208.1 and BC127468.1.
            
            On Dec 7, 2007 this sequence version replaced NP_998730.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA511208.1, DY312591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..406
                     /product="zinc finger protein 57"
                     /note="zfp-57"
                     /calculated_mol_wt=46457
     Region          17..70
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          57..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPK3.1)"
     Region          92..134
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(97,99,101,103..104,107..108,114,147,149,153..154,
                     157..158,161,175,177,179,181..182,185..186,189)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          142..162
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          169..190
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          170..190
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            178
                     /site_type="other"
                     /note="Crucial for 5-methylcytosine recognition.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (A0JPK3.1)"
     Region          194..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPK3.1)"
     Region          272..292
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(277,279,281,283..284,287..288,291,309..310,313..314,
                     317,325,327,329,331..332,335..336)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          320..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          372..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPK3.1)"
     CDS             1..406
                     /gene="Zfp57"
                     /coded_by="NM_213565.4:265..1485"
                     /db_xref="GeneID:361783"
                     /db_xref="RGD:1302981"
ORIGIN      
        1 maakkqsksa kalrttvrye dvavsftqee weyltstqkt lyqkvmsetf knltfveskk
       61 kpqepnpnlk dkdddksstc tgvfkggpff fcltcgkcfk kntflfnhqf pvrsrrlavt
      121 kpqsrkalgh kpqhrgdrpf fcnlcgktyr dasglsrhrr ahvgyrprsc pecgkcfrdq
      181 sevnrhlkvh qnkkpvagsh vkvhqnkpva snqkqkgrvp pttrespapa lrhlkviqgp
      241 varakarssr asslevrsts vtvarprekv ycpycritft mrtcllnhlk ihfrrqpnqh
      301 fcckeshssn tlrmqkiync pvcdssfrgk esllnhlcsr rpirlskcwe ilghllgylr
      361 eplgnifkvr esrkrrrkri ssdssetegp sgsdevmevd tdsdls
//
LOCUS       NP_001012481             172 aa            linear   ROD 27-APR-2025
DEFINITION  adenylate kinase isoenzyme 6 [Rattus norvegicus].
ACCESSION   NP_001012481
VERSION     NP_001012481.1
DBSOURCE    REFSEQ: accession NM_001012463.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Santama,N., Ogg,S.C., Malekkou,A., Zographos,S.E., Weis,K. and
            Lamond,A.I.
  TITLE     Characterization of hCINAP, a novel coilin-interacting protein
            encoded by a transcript from the transcription factor TAFIID32
            locus
  JOURNAL   J Biol Chem 280 (43), 36429-36441 (2005)
   PUBMED   16079131
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Ren,H., Wang,L., Bennett,M., Liang,Y., Zheng,X., Lu,F., Li,L.,
            Nan,J., Luo,M., Eriksson,S., Zhang,C. and Su,X.D.
  TITLE     The crystal structure of human adenylate kinase 6: An adenylate
            kinase localized to the cell nucleus
  JOURNAL   Proc Natl Acad Sci U S A 102 (2), 303-308 (2005)
   PUBMED   15630091
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1, BC089989.1 and BQ205289.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215465.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089989.1, FM100045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..172
                     /product="adenylate kinase isoenzyme 6"
                     /EC_number="2.7.4.3"
                     /note="ATP-AMP transphosphorylase 6; dual activity
                     adenylate kinase/ATPase; coilin-interacting nuclear ATPase
                     protein"
                     /calculated_mol_wt=19813
     Region          6..>144
                     /region_name="Fap7"
                     /note="Broad-specificity NMP kinase [Nucleotide transport
                     and metabolism]; COG1936"
                     /db_xref="CDD:441539"
     Region          33..56
                     /region_name="NMPbind.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03173"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB68.1)"
     Region          108..118
                     /region_name="LID.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03173"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB68.1)"
     CDS             1..172
                     /gene="Ak6"
                     /gene_synonym="AK/ATPase"
                     /coded_by="NM_001012463.3:52..570"
                     /db_xref="GeneID:102238592"
                     /db_xref="RGD:7387335"
ORIGIN      
        1 mklpnilltg tpgvgkttlg kelasrsglk yvnvgdlare ghlydgydee ygcpildedr
       61 vvdelepqmt eggvivdyhg cdffperwfh ivfvlrtdng ilykrletrg yhekklqdni
      121 qceifqvlye eamasykeei vhqlpsnepe qledninqis kwieqwvkdh np
//
LOCUS       NP_001288665             245 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.12br [Rattus norvegicus].
ACCESSION   NP_001288665 XP_006243456
VERSION     NP_001288665.1
DBSOURCE    REFSEQ: accession NM_001301736.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000008.1.
            
            On Sep 11, 2014 this sequence version replaced XP_006243456.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.12, also known as variant
            12) differs in the 5' and 3' UTRs and has multiple differences in
            the coding region, compared to variant 1, resulting in a shorter
            protein (isoform Tpm1.12br). The resulting protein (isoform
            Tpm1.12br) is shorter than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.45007.1,
                                           SRR26360194.1230505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..245
                     /product="tropomyosin alpha-1 chain isoform Tpm1.12br"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=28212
     Region          12..244
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..245
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001301736.1:152..889"
                     /note="isoform Tpm1.12br is encoded by transcript variant
                     Tpm1.12"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeerags lqreldqerk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedkyeeeik vlsdklkeae traefaersv tkleksiddl edqlyhqleq nrrltnelkl
      241 alned
//
LOCUS       NP_036675                325 aa            linear   ROD 27-APR-2025
DEFINITION  D site-binding protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_036675
VERSION     NP_036675.1
DBSOURCE    REFSEQ: accession NM_012543.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Jiang,H., Li,J., He,X., Xue,J., Liang,S., Liu,S., Gao,F., Qu,N.,
            Liu,H. and Chen,L.
  TITLE     D-site binding protein regulates cell proliferation through
            mediating cell cycle progression in rat mesangial cells
  JOURNAL   Tissue Cell 61, 35-43 (2019)
   PUBMED   31759405
  REMARK    GeneRIF: DBP effectively inhibits the proliferation of mesangial
            cells through G1 phase arrest.
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Harbour,V.L., Weigl,Y., Robinson,B. and Amir,S.
  TITLE     Phase differences in expression of circadian clock genes in the
            central nucleus of the amygdala, dentate gyrus, and suprachiasmatic
            nucleus in the rat
  JOURNAL   PLoS One 9 (7), e103309 (2014)
   PUBMED   25068868
  REMARK    GeneRIF: Data show that the expression of clock genes Per2, Bmal1
            and Dbp follow a diurnal rhythm in the central nucleus of the
            amygdala, dentate gyrus, and suprachiasmatic nucleu but the phase
            and amplitude of the rhythms of each gene vary across the 3
            regions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Huang,X.M., Chen,W.L., Yuan,J.P., Yang,Y.H., Mei,Q.H. and
            Huang,L.X.
  TITLE     Altered diurnal variation and localization of clock proteins in the
            remnant kidney of 5/6 nephrectomy rats
  JOURNAL   Nephrology (Carlton) 18 (8), 555-562 (2013)
   PUBMED   23738784
  REMARK    GeneRIF: The localization and diurnal variation of BMAL1, DBP and
            PER2 are changed in remnant kidney of 5/6 nephrectomy rats and are
            involved in diurnal rhythm of renal function.
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Yamajuku,D., Shibata,Y., Kitazawa,M., Katakura,T., Urata,H.,
            Kojima,T., Takayasu,S., Nakata,O. and Hashimoto,S.
  TITLE     Cellular DBP and E4BP4 proteins are critical for determining the
            period length of the circadian oscillator
  JOURNAL   FEBS Lett 585 (14), 2217-2222 (2011)
   PUBMED   21635892
  REMARK    GeneRIF: Data show that knockdown of DBP, D-box positive regulator,
            led to a short-period phenotype, and overexpression of DBP produced
            a long-period rhythm, while knockdown and overexpression of E4BP4,
            D-box negative regulator, had the opposite effect of DBP.
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Xu,Z., Kaga,S., Tsubomizu,J., Fujisaki,J., Mochiduki,A., Sakai,T.,
            Tsukamura,H., Maeda,K., Inoue,K. and Adachi,A.A.
  TITLE     Circadian transcriptional factor DBP regulates expression of Kiss1
            in the anteroventral periventricular nucleus
  JOURNAL   Mol Cell Endocrinol 339 (1-2), 90-97 (2011)
   PUBMED   21458520
  REMARK    GeneRIF: Dbp and estrogen regulate the expression of Kiss1 in the
            anteroventral periventricular nucleus
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Brown,S.A., Zumbrunn,G., Fleury-Olela,F., Preitner,N. and
            Schibler,U.
  TITLE     Rhythms of mammalian body temperature can sustain peripheral
            circadian clocks
  JOURNAL   Curr Biol 12 (18), 1574-1583 (2002)
   PUBMED   12372249
  REMARK    GeneRIF: natural body temperature rhythms can affect circadian gene
            expression
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Brown,S.A. and Schibler,U.
  TITLE     The ins and outs of circadian timekeeping
  JOURNAL   Curr Opin Genet Dev 9 (5), 588-594 (1999)
   PUBMED   10508692
  REMARK    Review article
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Mueller,C.R., Maire,P. and Schibler,U.
  TITLE     DBP, a liver-enriched transcriptional activator, is expressed late
            in ontogeny and its tissue specificity is determined
            posttranscriptionally
  JOURNAL   Cell 61 (2), 279-291 (1990)
   PUBMED   2331750
  REMARK    Erratum:[Cell. 1991 May 31;65(5):915. PMID: 2040017]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Summary: The protein encoded by this gene is a member of the Par
            bZIP transcription factor family and binds to specific sequences in
            the promoters of several genes, such as albumin, Cyp2a4, and
            Cyp2a5. The encoded protein can bind DNA as a homo- or heterodimer
            and is involved in the regulation of some circadian rhythym genes.
            Three transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087668.1, J03179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..325
                     /product="D site-binding protein isoform 1"
                     /note="d site-binding protein; albumin D box-binding
                     protein; albumin D-element-binding protein; d site albumin
                     promoter-binding protein 1; D site albumin promoter
                     binding protein; D site of albumin promoter (albumin
                     D-box) binding protein"
                     /calculated_mol_wt=34305
     Region          1..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16443.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P16443.2)"
     Region          124..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16443.2)"
     Region          230..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16443.2)"
     Region          254..313
                     /region_name="bZIP_HLF"
                     /note="Basic leucine zipper (bZIP) domain of Hepatic
                     leukemia factor (HLF) and similar proteins: a DNA-binding
                     and dimerization domain; cd14695"
                     /db_xref="CDD:269843"
     Region          255..313
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269843"
     Region          257..279
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P16443.2)"
     Site            order(261..262,264..266,268..273,275..277)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269843"
     Site            order(276,279..280,283..284,286..287,290..291,293..294,
                     297..298,300..301,304..305,307..308)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269843"
     Region          283..297
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P16443.2)"
     CDS             1..325
                     /gene="Dbp"
                     /coded_by="NM_012543.3:402..1379"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24309"
                     /db_xref="RGD:2491"
ORIGIN      
        1 marplsdrtp gplllggpag appgggallg lrsllqgnsk pkepascllk ekerkatlps
       61 apvpgpvlet agpadaptga vsgggsprgr sgpvagpslf apllwertlp fgdveyvdld
      121 afllehglpp sppppgglsp apspartpap spgpgscsss sprsspghap aratlgaagg
      181 hragltsrdt pspvdpdtve vlmtfepdpa dlalssipgh etfdprrhrf seeelkpqpi
      241 mkkarkvqvp eeqkdekyws rryknneaak rsrdarrlke nqisvraafl ekenallrqe
      301 vvavrqelsh yravlsryqa qhgtl
//
LOCUS       NP_112406                375 aa            linear   ROD 27-APR-2025
DEFINITION  actin, cytoplasmic 1 [Rattus norvegicus].
ACCESSION   NP_112406
VERSION     NP_112406.1
DBSOURCE    REFSEQ: accession NM_031144.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Yang,C., Zhang,X., Ge,X., He,C., Liu,S., Yang,S. and Huang,C.
  TITLE     N-Acetylcysteine protects against cobalt chloride-induced
            endothelial dysfunction by enhancing glucose-6-phosphate
            dehydrogenase activity
  JOURNAL   FEBS Open Bio 12 (8), 1475-1488 (2022)
   PUBMED   35666067
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Soliman,M.M., Aldhahrani,A., Gaber,A., Alsanie,W.F., Shukry,M.,
            Mohamed,W.A., Metwally,M.M.M. and Mohamed,A.A.
  TITLE     Impacts of n-acetyl cysteine on gibberellic acid-induced testicular
            dysfunction through regulation of inflammatory cytokines, steroid
            and antioxidant activity
  JOURNAL   Andrologia 53 (5), e14036 (2021)
   PUBMED   33724537
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Zhou,F., Chen,X., Chen,G., Yan,J. and Xiao,Y.
  TITLE     Identification of SAA and ACTB as potential biomarker of patients
            with severe HFMD using iTRAQ quantitative proteomics
  JOURNAL   Clin Biochem 67, 1-6 (2019)
   PUBMED   30817906
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Park,F., Mattson,D.L., Roberts,L.A. and Cowley,A.W. Jr.
  TITLE     Evidence for the presence of smooth muscle alpha-actin within
            pericytes of the renal medulla
  JOURNAL   Am J Physiol 273 (5), R1742-R1748 (1997)
   PUBMED   9374818
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Shartava,A., Korn,W., Shah,A.K. and Goodman,S.R.
  TITLE     Irreversibly sickled cell beta-actin: defective filament formation
  JOURNAL   Am J Hematol 55 (2), 97-103 (1997)
   PUBMED   9209005
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Toyama,S. and Toyama,S.
  TITLE     A variant form of beta-actin in a mutant of KB cells resistant to
            cytochalasin B
  JOURNAL   Cell 37 (2), 609-614 (1984)
   PUBMED   6202424
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Nudel,U., Zakut,R., Shani,M., Neuman,S., Levy,Z. and Yaffe,D.
  TITLE     The nucleotide sequence of the rat cytoplasmic beta-actin gene
  JOURNAL   Nucleic Acids Res 11 (6), 1759-1771 (1983)
   PUBMED   6300777
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Bonham,G.S.
  TITLE     Prevalence of chronic skin and musculoskeletal conditions. United
            States-1976
  JOURNAL   Vital Health Stat 10 (124), i-iv,1-57 (1978)
   PUBMED   734918
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC063166.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063166.1, FQ231503.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..375
                     /product="actin, cytoplasmic 1"
                     /note="beta-actin; cytoplasmic beta-actin"
                     /calculated_mol_wt=41606
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P60709; propagated from
                     UniProtKB/Swiss-Prot (P60711.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylaspartate, in Actin, cytoplasmic 1,
                     N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P60709; propagated from
                     UniProtKB/Swiss-Prot (P60711.1)"
     Region          6..370
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     Site            73
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000269|PubMed:30526847; propagated from
                     UniProtKB/Swiss-Prot (P60711.1)"
     Site            84
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60709; propagated from
                     UniProtKB/Swiss-Prot (P60711.1)"
     CDS             1..375
                     /gene="Actb"
                     /gene_synonym="Actx"
                     /coded_by="NM_031144.3:79..1206"
                     /db_xref="GeneID:81822"
                     /db_xref="RGD:628837"
ORIGIN      
        1 mdddiaalvv dngsgmckag fagddaprav fpsivgrprh qgvmvgmgqk dsyvgdeaqs
       61 krgiltlkyp iehgivtnwd dmekiwhhtf ynelrvapee hpvllteapl npkanrekmt
      121 qimfetfntp amyvaiqavl slyasgrttg ivmdsgdgvt htvpiyegya lphailrldl
      181 agrdltdylm kiltergysf tttaereivr dikeklcyva ldfeqemata assssleksy
      241 elpdgqviti gnerfrcpea lfqpsflgme scgihettfn simkcdvdir kdlyantvls
      301 ggttmypgia drmqkeital apstmkikii apperkysvw iggsilasls tfqqmwiskq
      361 eydesgpsiv hrkcf
//
LOCUS       NP_112307                459 aa            linear   ROD 27-APR-2025
DEFINITION  inositol-trisphosphate 3-kinase A [Rattus norvegicus].
ACCESSION   NP_112307
VERSION     NP_112307.2
DBSOURCE    REFSEQ: accession NM_031045.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Lee,D., Lee,H.W., Hong,S., Choi,B.I., Kim,H.W., Han,S.B., Kim,I.H.,
            Bae,J.Y., Bae,Y.C., Rhyu,I.J., Sun,W. and Kim,H.
  TITLE     Inositol 1,4,5-trisphosphate 3-kinase A is a novel
            microtubule-associated protein: PKA-dependent phosphoregulation of
            microtubule binding affinity
  JOURNAL   J Biol Chem 287 (19), 15981-15995 (2012)
   PUBMED   22389500
  REMARK    GeneRIF: Data show that protein kinse A (PKA) phosphorylated
            Ser-119 within inositol 1,4,5-trisphosphate 3-kinase A (IP(3)K-A),
            leading to a significant reduction of microtubule binding affinity.
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Eva,R., Bouyoucef-Cherchalli,D., Patel,K., Cullen,P.J. and
            Banting,G.
  TITLE     IP3 3-kinase opposes NGF driven neurite outgrowth
  JOURNAL   PLoS One 7 (2), e32386 (2012)
   PUBMED   22384237
  REMARK    GeneRIF: IP3 3-kinase opposes NGF driven neurite outgrowth
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Johnson,H.W. and Schell,M.J.
  TITLE     Neuronal IP3 3-kinase is an F-actin-bundling protein: role in
            dendritic targeting and regulation of spine morphology
  JOURNAL   Mol Biol Cell 20 (24), 5166-5180 (2009)
   PUBMED   19846664
  REMARK    GeneRIF: These results suggest that, in addition to its ability to
            regulate intracellular Ca(2+) via Ins(1,4,5)P(3) metabolism, ITPKA
            regulates structural plasticity.
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Kim,I.H., Park,S.K., Hong,S.T., Jo,Y.S., Kim,E.J., Park,E.H.,
            Han,S.B., Shin,H.S., Sun,W., Kim,H.T., Soderling,S.H. and Kim,H.
  TITLE     Inositol 1,4,5-trisphosphate 3-kinase a functions as a scaffold for
            synaptic Rac signaling
  JOURNAL   J Neurosci 29 (44), 14039-14049 (2009)
   PUBMED   19890013
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Ferreri-Jacobia,M., Mak,D.O. and Foskett,J.K.
  TITLE     Translational mobility of the type 3 inositol 1,4,5-trisphosphate
            receptor Ca2+ release channel in endoplasmic reticulum membrane
  JOURNAL   J Biol Chem 280 (5), 3824-3831 (2005)
   PUBMED   15537642
  REMARK    GeneRIF: the large majority of InsP3R3 channels free to diffuse
            throughout the endoplasmic reticulum, at rates that are comparable
            with those measured for other polytopic ER integral membrane
            proteins
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Dupont,G., Koukoui,O., Clair,C., Erneux,C., Swillens,S. and
            Combettes,L.
  TITLE     Ca2+ oscillations in hepatocytes do not require the modulation of
            InsP3 3-kinase activity by Ca2+
  JOURNAL   FEBS Lett 534 (1-3), 101-105 (2003)
   PUBMED   12527368
  REMARK    GeneRIF: these results suggest that oscillations in InsP(3)
            concentration due to Ca(2+)-stimulated InsP(3) catabolism do not
            play a major role for the oscillations in Ca(2+) concentration.
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Jun,K., Choi,G., Yang,S.G., Choi,K.Y., Kim,H., Chan,G.C.,
            Storm,D.R., Albert,C., Mayr,G.W., Lee,C.J. and Shin,H.S.
  TITLE     Enhanced hippocampal CA1 LTP but normal spatial learning in
            inositol 1,4,5-trisphosphate 3-kinase(A)-deficient mice
  JOURNAL   Learn Mem 5 (4-5), 317-330 (1998)
   PUBMED   10454357
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Communi,D., Lecocq,R., Vanweyenberg,V. and Erneux,C.
  TITLE     Active site labelling of inositol 1,4,5-trisphosphate 3-kinase A by
            phenylglyoxal
  JOURNAL   Biochem J 310 (Pt 1) (Pt 1), 109-115 (1995)
   PUBMED   7646431
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Takazawa,K., Vandekerckhove,J., Dumont,J.E. and Erneux,C.
  TITLE     Cloning and expression in Escherichia coli of a rat brain cDNA
            encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate
            3-kinase
  JOURNAL   Biochem J 272 (1), 107-112 (1990)
   PUBMED   2176078
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Choi,K.Y., Kim,H.K., Lee,S.Y., Moon,K.H., Sim,S.S., Kim,J.W.,
            Chung,H.K. and Rhee,S.G.
  TITLE     Molecular cloning and expression of a complementary DNA for
            inositol 1,4,5-trisphosphate 3-kinase
  JOURNAL   Science 248 (4951), 64-66 (1990)
   PUBMED   2157285
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M29787.1, JAXUCZ010000003.1 and BQ204027.1.
            
            On Aug 4, 2012 this sequence version replaced NP_112307.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M29787.1, X56917.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..459
                     /product="inositol-trisphosphate 3-kinase A"
                     /EC_number="2.7.1.127"
                     /note="IP3K A; IP3 3-kinase A; insP 3-kinase A; inositol
                     145-triphosphate 3-kinase; inositol 1,4,5-triphosphate
                     3-kinase; inositol 1,4,5-trisphosphate 3-kinase A"
                     /calculated_mol_wt=50740
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17105.3)"
     Site            35
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P17105.3)"
     Region          49..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17105.3)"
     Site            55
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P17105.3)"
     Site            62
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R071; propagated from
                     UniProtKB/Swiss-Prot (P17105.3)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P17105.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23677; propagated from
                     UniProtKB/Swiss-Prot (P17105.3)"
     Region          243..453
                     /region_name="IPK"
                     /note="Inositol polyphosphate kinase; pfam03770"
                     /db_xref="CDD:397715"
     Region          285..293
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P17105.3)"
     CDS             1..459
                     /gene="Itpka"
                     /coded_by="NM_031045.2:46..1425"
                     /db_xref="GeneID:81677"
                     /db_xref="RGD:619950"
ORIGIN      
        1 mtlpghptgm arprgagpcs pgleraprrs vgelrllfea rcaavaaaaa ageprargak
       61 rrggqvpngl praapapvip qltvtseedv apaspgppdr egnwlpaags hlqqprrlst
      121 sslsstgsss lledseddll sdsesrsrgn vqletsedvg qkshwqkirt mvnlpvmspf
      181 kkryswvqla ghtgsfkaag tsglilkrss epehyclvrl madvlrgcvp afhgvverdg
      241 esylqlqdll dgfdgpcvld ckmgvrtyle eeltkarerp klrkdmykkm lavdpeapte
      301 eehaqravtk prymqwregi sssttlgfri egikkadgsc stdfkttrsr eqvtrvfeef
      361 mqgdaevlkr ylnrlqqird tleisdffrr hevigssllf vhdhchragv wlidfgkttp
      421 lpdgqildhr rpweegnred gyllgldnli gilanlaer
//
LOCUS       NP_001258087              78 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor beta isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001258087
VERSION     NP_001258087.1
DBSOURCE    REFSEQ: accession NM_001271158.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Cerone,M.A., Burgess,D.J., Naceur-Lombardelli,C., Lord,C.J. and
            Ashworth,A.
  TITLE     High-throughput RNAi screening reveals novel regulators of
            telomerase
  JOURNAL   Cancer Res 71 (9), 3328-3340 (2011)
   PUBMED   21531765
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Dahia,C.L. and Rao,A.J.
  TITLE     Regulation of FSH receptor, PKIbeta, IL-6 and calcium mobilization:
            Possible mediators of differential action of FSH
  JOURNAL   Mol Cell Endocrinol 247 (1-2), 73-81 (2006)
   PUBMED   16406266
  REMARK    GeneRIF: PKIbeta and calcium, which are the downstream signaling
            molecules, are involved in FSH regulated Sertoli cells
            proliferation.
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Kumar,P. and Walsh,D.A.
  TITLE     A dual-specificity isoform of the protein kinase inhibitor PKI
            produced by alternate gene splicing
  JOURNAL   Biochem J 362 (Pt 3), 533-537 (2002)
   PUBMED   11879178
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Andoh,Y., Kuramoto,T., Yokoi,N., Maihara,T., Kitada,K. and
            Serikawa,T.
  TITLE     Correlation between genetic and cytogenetic maps of the rat
  JOURNAL   Mamm Genome 9 (4), 287-293 (1998)
   PUBMED   9530624
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Baude,E.J., Dignam,S.S., Olsen,S.R., Reimann,E.M. and Uhler,M.D.
  TITLE     Glutamic acid 203 of the cAMP-dependent protein kinase catalytic
            subunit participates in the inhibition by two isoforms of the
            protein kinase inhibitor
  JOURNAL   J Biol Chem 269 (3), 2316-2323 (1994)
   PUBMED   7905001
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Van Patten,S.M., Ng,D.C., Th'ng,J.P., Angelos,K.L., Smith,A.J. and
            Walsh,D.A.
  TITLE     Molecular cloning of a rat testis form of the inhibitor protein of
            cAMP-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5383-5387 (1991)
   PUBMED   2052616
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078880.1 and FQ231722.1.
            
            Transcript Variant: This variant (3) contains an alternate 5'
            non-coding exon and lacks an internal exon compared to variant 1,
            which results in translation initiation from an in-frame downstream
            AUG and an isoform (2) with a shorter N-terminus compared to
            isoform 1. Variants 2 and 3 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078880.1, CK469096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..78
                     /product="cAMP-dependent protein kinase inhibitor beta
                     isoform 2"
                     /note="PKI-beta; protein kinase inhibitor beta, cAMP
                     dependent, testis specific; protein kinase
                     (cAMP-dependent, catalytic) inhibitor beta; cAMP-dependent
                     protein kinase (catalytic subunit binding) inhibtor 2;
                     protein kinase inhibitor beta, cAMP dependent, catalytic;
                     protein kinase inhibitor beta, (cAMP-dependent, catalytic)
                     inhibitor beta; protein kinase inhibitor, beta"
                     /calculated_mol_wt=8261
     Region          9..77
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     CDS             1..78
                     /gene="Pkib"
                     /gene_synonym="PKINH; Prkacn2; RATPKINH"
                     /coded_by="NM_001271158.1:218..454"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:24678"
                     /db_xref="RGD:3335"
ORIGIN      
        1 mrtdssemtd vesvissfas saragrrnal pdiqsslatg gspdlalkle alavkedakm
       61 kneekdqgqp kkpldedk
//
LOCUS       NP_114185                361 aa            linear   ROD 27-APR-2025
DEFINITION  Y-box-binding protein 3 [Rattus norvegicus].
ACCESSION   NP_114185 XP_001069862
VERSION     NP_114185.3
DBSOURCE    REFSEQ: accession NM_031979.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Hou,A., Fu,J., Shi,Y., Qiao,L., Li,J., Xing,Y. and Xue,X.
  TITLE     Decreased ZONAB expression promotes excessive transdifferentiation
            of alveolar epithelial cells in hyperoxia-induced bronchopulmonary
            dysplasia
  JOURNAL   Int J Mol Med 41 (4), 2339-2349 (2018)
   PUBMED   29393348
  REMARK    GeneRIF: These results suggest that Csda expression in alveolar
            epithelial cells type II decreases under hyperoxia conditions,
            which promotes transdifferentiation and inhibits proliferation of
            alveolar epithelial cells.
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Nie,M., Balda,M.S. and Matter,K.
  TITLE     Stress- and Rho-activated ZO-1-associated nucleic acid binding
            protein binding to p21 mRNA mediates stabilization, translation,
            and cell survival
  JOURNAL   Proc Natl Acad Sci U S A 109 (27), 10897-10902 (2012)
   PUBMED   22711822
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Berghella,L., De Angelis,L., De Buysscher,T., Mortazavi,A.,
            Biressi,S., Forcales,S.V., Sirabella,D., Cossu,G. and Wold,B.J.
  TITLE     A highly conserved molecular switch binds MSY-3 to regulate
            myogenin repression in postnatal muscle
  JOURNAL   Genes Dev 22 (15), 2125-2138 (2008)
   PUBMED   18676817
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Dieterich,D.C., Bockers,T.M., Gundelfinger,E.D. and Kreutz,M.R.
  TITLE     Screening for differentially expressed genes in the rat inner
            retina and optic nerve after optic nerve crush
  JOURNAL   Neurosci Lett 317 (1), 29-32 (2002)
   PUBMED   11750989
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Iuchi,Y., Kobayashi,T., Kaneko,T., Takahara,M., Ogino,T. and
            Fujii,J.
  TITLE     Expression of a Y-box protein, YB2/RYB-a, precedes protamine 2
            expression during spermatogenesis in rodents
  JOURNAL   Mol Hum Reprod 7 (11), 1023-1031 (2001)
   PUBMED   11675468
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Davies,H.G., Giorgini,F., Fajardo,M.A. and Braun,R.E.
  TITLE     A sequence-specific RNA binding complex expressed in murine germ
            cells contains MSY2 and MSY4
  JOURNAL   Dev Biol 221 (1), 87-100 (2000)
   PUBMED   10772793
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Sapru,M.K., Gao,J.P., Walke,W., Burmeister,M. and Goldman,D.
  TITLE     Cloning and characterization of a novel transcriptional repressor
            of the nicotinic acetylcholine receptor delta-subunit gene
  JOURNAL   J Biol Chem 271 (12), 7203-7211 (1996)
   PUBMED   8636158
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Ito,K., Tsutsumi,K., Kuzumaki,T., Gomez,P.F., Otsu,K. and
            Ishikawa,K.
  TITLE     A novel growth-inducible gene that encodes a protein with a
            conserved cold-shock domain
  JOURNAL   Nucleic Acids Res 22 (11), 2036-2041 (1994)
   PUBMED   8029009
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U22893.1.
            
            On May 9, 2012 this sequence version replaced NP_114185.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U22893.1, BC105778.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..361
                     /product="Y-box-binding protein 3"
                     /note="DNA-binding protein A; RYB-A; Y-box-binding protein
                     A; cold shock domain-containing protein A; muscle Y-box
                     protein YB2; cold shock domain protein A"
                     /calculated_mol_wt=38721
     Region          1..73
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62764.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P16989; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Region          83..152
                     /region_name="CSD"
                     /note="'Cold-shock' DNA-binding domain; pfam00313"
                     /db_xref="CDD:278729"
     Site            order(89,98,109,142)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239905"
     Site            order(95..101,108..111)
                     /site_type="active"
                     /note="RNA-binding motif [active]"
                     /db_xref="CDD:239905"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16989; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Region          173..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62764.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            243
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P16989; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16989; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            315
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P16989; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62764.1)"
     CDS             1..361
                     /gene="Ybx3"
                     /gene_synonym="Csda; Dbpa; Yb2"
                     /coded_by="NM_031979.3:184..1269"
                     /db_xref="GeneID:83807"
                     /db_xref="RGD:621056"
ORIGIN      
        1 mseageattg gttlpqaaad apaaappdpa pkspaasgap qapapaalla gspggdaapg
       61 papassapag sedaekkvla tkvlgtvkwf nvrngygfin rndtkedvfv hqtaikknnp
      121 rkylrsvgdg etvefdvveg ekgaeaanvt gpdgvpvegs ryaadrrryr rgyygrrrgp
      181 prnyageeee egsgssegfe ppaadgqfsg arnqlrrpqy rppyrqrrfp pyhvgqtfdr
      241 rsrvfphpnr mqageigemk dgvpegaqlq vhrnptyrpr frrgparprp apaigeaedk
      301 enqqaangpn qpsarrgfrr pynyrrrprp lnavsqdgke tkageapten papateqssa
      361 e
//
LOCUS       NP_037037                113 aa            linear   ROD 27-APR-2025
DEFINITION  striated muscle-specific serine/threonine-protein kinase isoform 4
            [Rattus norvegicus].
ACCESSION   NP_037037
VERSION     NP_037037.1
DBSOURCE    REFSEQ: accession NM_012905.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Kusic,D., Connolly,J., Kainulainen,H., Semenova,E.A., Borisov,O.V.,
            Larin,A.K., Popov,D.V., Generozov,E.V., Ahmetov,I.I., Britton,S.L.,
            Koch,L.G. and Burniston,J.G.
  TITLE     Striated muscle-specific serine/threonine-protein kinase beta
            segregates with high versus low responsiveness to endurance
            exercise training
  JOURNAL   Physiol Genomics 52 (1), 35-46 (2020)
   PUBMED   31790338
  REMARK    GeneRIF: Striated muscle-specific serine/threonine-protein kinase
            beta segregates with high versus low responsiveness to endurance
            exercise training.
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Liu,X., Ramjiganesh,T., Chen,Y.H., Chung,S.W., Hall,S.R.,
            Schissel,S.L., Padera,R.F. Jr., Liao,R., Ackerman,K.G.,
            Kajstura,J., Leri,A., Anversa,P., Yet,S.F., Layne,M.D. and
            Perrella,M.A.
  TITLE     Disruption of striated preferentially expressed gene locus leads to
            dilated cardiomyopathy in mice
  JOURNAL   Circulation 119 (2), 261-268 (2009)
   PUBMED   19118250
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Hsieh,C.M., Fukumoto,S., Layne,M.D., Maemura,K., Charles,H.,
            Patel,A., Perrella,M.A. and Lee,M.E.
  TITLE     Striated muscle preferentially expressed genes alpha and beta are
            two serine/threonine protein kinases derived from the same gene as
            the aortic preferentially expressed gene-1
  JOURNAL   J Biol Chem 275 (47), 36966-36973 (2000)
   PUBMED   10973969
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Hsieh,C.M., Yoshizumi,M., Endege,W.O., Kho,C.J., Jain,M.K.,
            Kashiki,S., de los Santos,R., Lee,W.S., Perrella,M.A. and Lee,M.E.
  TITLE     APEG-1, a novel gene preferentially expressed in aortic smooth
            muscle cells, is down-regulated by vascular injury
  JOURNAL   J Biol Chem 271 (29), 17354-17359 (1996)
   PUBMED   8663449
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EV763588.1 and
            BC087690.1.
            
            Transcript Variant: This variant (4) has multiple differences,
            compared to variant 1. These differences result in a distinct 5'
            UTR and cause translation initiation at a downstream start codon,
            compared to variant 1. The encoded protein (isoform 4) is shorter
            than isoform 1. This variant corresponds to the mouse APEG-1
            variant described in PubMed ID: 10973969.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U57097.1, EV763588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132293, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..113
                     /product="striated muscle-specific
                     serine/threonine-protein kinase isoform 4"
                     /EC_number="2.7.11.1"
                     /note="striated muscle-specific serine/threonine-protein
                     kinase; aortic preferentially expressed gene 1; aortic
                     preferentially expressed protein 1; SPEG complex locus"
                     /calculated_mol_wt=12537
     Region          20..110
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409567"
     Region          50..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409567"
     Region          76..80
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409567"
     Region          90..95
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409567"
     Region          103..106
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409567"
     CDS             1..113
                     /gene="Speg"
                     /gene_synonym="APEG-1; Apeg1"
                     /coded_by="NM_012905.2:194..535"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:363256"
                     /db_xref="RGD:2124"
ORIGIN      
        1 mkpspsqdrd ssdssskapp tfkvslmdqs vregqdvims irvqgepkpv vswlrnrqpv
       61 rpdqrrfaee aegglcrlri laaergdagf ytckavneyg arqcearlev rge
//
LOCUS       NP_001257554             612 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001257554
VERSION     NP_001257554.1
DBSOURCE    REFSEQ: accession NM_001270625.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Inaba,Y., Shinohara,K., Botilde,Y., Nabeshima,R., Takaoka,K.,
            Ajima,R., Lamri,L., Takeda,H., Saga,Y., Nakamura,T. and Hamada,H.
  TITLE     Transport of the outer dynein arm complex to cilia requires a
            cytoplasmic protein Lrrc6
  JOURNAL   Genes Cells 21 (7), 728-739 (2016)
   PUBMED   27353389
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Blasier,K.R., Humsi,M.K., Ha,J., Ross,M.W., Smiley,W.R.,
            Inamdar,N.A., Mitchell,D.J., Lo,K.W. and Pfister,K.K.
  TITLE     Live cell imaging reveals differential modifications to cytoplasmic
            dynein properties by phospho- and dephosphomimic mutations of the
            intermediate chain 2C S84
  JOURNAL   J Neurosci Res 92 (9), 1143-1154 (2014)
   PUBMED   24798412
  REMARK    GeneRIF: The data of this study suggest that the IC-2C S84 has a
            role in modulating dynein properties.
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Hirayama,M., Kobayashi,D., Mizuguchi,S., Morikawa,T., Nagayama,M.,
            Midorikawa,U., Wilson,M.M., Nambu,A.N., Yoshizawa,A.C., Kawano,S.
            and Araki,N.
  TITLE     Integrated proteomics identified novel activation of dynein
            IC2-GR-COX-1 signaling in neurofibromatosis type I (NF1) disease
            model cells
  JOURNAL   Mol Cell Proteomics 12 (5), 1377-1394 (2013)
   PUBMED   23358504
  REMARK    GeneRIF: Neurofibromatosis type I-related neural abnormalities are,
            in part, caused by up-regulation of dynein IC2-glucocorticoid
            receptor-COX-1 signaling.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Allan,V.J.
  TITLE     Cytoplasmic dynein
  JOURNAL   Biochem Soc Trans 39 (5), 1169-1178 (2011)
   PUBMED   21936784
  REMARK    Review article
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Salata,M.W., Dillman,J.F. 3rd, Lye,R.J. and Pfister,K.K.
  TITLE     Growth factor regulation of cytoplasmic dynein intermediate chain
            subunit expression preceding neurite extension
  JOURNAL   J Neurosci Res 65 (5), 408-416 (2001)
   PUBMED   11536324
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Pfister,K.K., Salata,M.W., Dillman,J.F. 3rd, Torre,E. and Lye,R.J.
  TITLE     Identification and developmental regulation of a neuron-specific
            subunit of cytoplasmic dynein
  JOURNAL   Mol Biol Cell 7 (2), 331-343 (1996)
   PUBMED   8688562
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB733957.1, FM110655.1, JAXUCZ010000003.1, BC078764.1 and
            FM076575.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U39046.1, SRR26643292.12686.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q22"
     Protein         1..612
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 3"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2;
                     cytoplasmic dynein 1 intermediate chain 2; DH IC-2; dynein
                     intermediate chain 2, cytosolic; cytoplasmic dynein
                     intermediate chain 2; dynein, cytoplasmic, intermediate
                     chain 2; oncofetal protein (OFP)"
                     /calculated_mol_wt=68232
     Region          107..137
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          250..572
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(253,270,284,290..291,303..304,323,328,334..335,
                     353..354,373,378,384..385,414,431,436,448..449,473,477,
                     483..484,496..497,515,520,526..527,542..543,561,565,
                     571..572)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          256..305
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          313..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..400
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          408..455
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..495
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          501..539
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..612
                     /gene="Dync1i2"
                     /gene_synonym="Dnci2; Dncic2"
                     /coded_by="NM_001270625.1:355..2193"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:116659"
                     /db_xref="RGD:620174"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keaavsvqee sdlekkrrea
       61 eallqsmglt tdspivpppm spssksvstp seagsqdsgd gavgsrrgpi klgmakitqv
      121 dfppreivty tketqtpvta qpkedeeeed dvaapkppve peeekilkkd eendskapph
      181 elteeekqqi lhseeflsff dhstrivera lseqiniffd ysgrdledke geiqagakls
      241 lnrqffderw skhrvvscld wssqypellv asynnneeap hepdgvalvw nmkykkttpe
      301 yvfhcqsavm satfakfhpn lvvggtysgq ivlwdnrsnk rtpvqrtpls aaahthpvyc
      361 vnvvgtqnah nlisistdgk icswsldmls hpqdsmelvh kqskavavts msfpvgdvnn
      421 fvvgseegsv ytacrhgska gisemfeghq gpitgihcha avgavdfshl fvtssfdwtv
      481 klwttknnkp lysfednsdy vydvmwspth palfacvdgm grldlwnlnn dtevptasis
      541 vegnpalnrv rwthsgreia vgdsegqivi ydvgeqiavp rndewarfgr tlaeinasra
      601 daeeeaatri pa
//
LOCUS       NP_001164029            3357 aa            linear   ROD 27-APR-2025
DEFINITION  versican core protein isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001164029 XP_001058160 XP_001058357 XP_215451
VERSION     NP_001164029.1
DBSOURCE    REFSEQ: accession NM_001170558.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3357)
  AUTHORS   Harten,I.A., Kaber,G., Agarwal,K.J., Kang,I., Ibarrientos,S.R.,
            Workman,G., Chan,C.K., Nivison,M.P., Nagy,N., Braun,K.R.,
            Kinsella,M.G., Merrilees,M.J. and Wight,T.N.
  TITLE     The synthesis and secretion of versican isoform V3 by mammalian
            cells: A role for N-linked glycosylation
  JOURNAL   Matrix Biol 89, 27-42 (2020)
   PUBMED   32001344
  REMARK    GeneRIF: The synthesis and secretion of versican isoform V3 by
            mammalian cells: A role for N-linked glycosylation.
REFERENCE   2  (residues 1 to 3357)
  AUTHORS   Bogen,O., Bender,O., Alvarez,P., Kern,M., Tomiuk,S., Hucho,F. and
            Levine,J.D.
  TITLE     Expression of a novel versican variant in dorsal root ganglia from
            spared nerve injury rats
  JOURNAL   Mol Pain 15, 1744806919874557 (2019)
   PUBMED   31429356
  REMARK    GeneRIF: mRNAs of the versican gene with exon 8beta are predicted
            to be constitutively degraded by nonsense-mediated RNA decay.
REFERENCE   3  (residues 1 to 3357)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   4  (residues 1 to 3357)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 3357)
  AUTHORS   Carthy,J.M., Abraham,T., Meredith,A.J., Boroomand,S. and
            McManus,B.M.
  TITLE     Versican localizes to the nucleus in proliferating mesenchymal
            cells
  JOURNAL   Cardiovasc Pathol 24 (6), 368-374 (2015)
   PUBMED   26395512
  REMARK    GeneRIF: Versican localizes to the nucleus in proliferating
            mesenchymal cells and suggest role in mitotic spindle organization
            during cell division.
REFERENCE   6  (residues 1 to 3357)
  AUTHORS   Lemire,J.M., Merrilees,M.J., Braun,K.R. and Wight,T.N.
  TITLE     Overexpression of the V3 variant of versican alters arterial smooth
            muscle cell adhesion, migration, and proliferation in vitro
  JOURNAL   J Cell Physiol 190 (1), 38-45 (2002)
   PUBMED   11807809
  REMARK    GeneRIF: Overexpression of alternatively spliced V3 variant of
            versican alters arterial smooth muscle cell adhesion, migration,
            proliferation and cell shape
REFERENCE   7  (residues 1 to 3357)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
REFERENCE   8  (residues 1 to 3357)
  AUTHORS   Mjaatvedt,C.H., Yamamura,H., Capehart,A.A., Turner,D. and
            Markwald,R.R.
  TITLE     The Cspg2 gene, disrupted in the hdf mutant, is required for right
            cardiac chamber and endocardial cushion formation
  JOURNAL   Dev Biol 202 (1), 56-66 (1998)
   PUBMED   9758703
REFERENCE   9  (residues 1 to 3357)
  AUTHORS   Milev,P., Maurel,P., Chiba,A., Mevissen,M., Popp,S., Yamaguchi,Y.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Differential regulation of expression of hyaluronan-binding
            proteoglycans in developing brain: aggrecan, versican, neurocan,
            and brevican
  JOURNAL   Biochem Biophys Res Commun 247 (2), 207-212 (1998)
   PUBMED   9642104
REFERENCE   10 (residues 1 to 3357)
  AUTHORS   Pyke,C., Kristensen,P., Ostergaard,P.B., Oturai,P.S. and Romer,J.
  TITLE     Proteoglycan expression in the normal rat kidney
  JOURNAL   Nephron 77 (4), 461-470 (1997)
   PUBMED   9434070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF072892.1, JAXUCZ010000002.1, AF062402.1 and AY007691.1.
            
            On or before May 29, 2010 this sequence version replaced
            XP_215451.5, XP_001058357.1, XP_001058160.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1, also referred to as
            V0).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data from several strains because no single
            transcript was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments and
            orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3357
                     /organism="Rattus norvegicus"
                     /strain="WKY"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..3357
                     /product="versican core protein isoform 1 precursor"
                     /note="versican core protein; GHAP; PG-M; large fibroblast
                     proteoglycan; glial hyaluronate-binding protein;
                     chondroitin sulfate proteoglycan core protein 2;
                     chondroitin sulfate proteoglycan 2 (versican)"
                     /calculated_mol_wt=364402
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          3052..3086
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          3088..3124
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(3088,3091,3105)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          3130..3253
                     /region_name="CLECT_CSPGs"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in chondroitin sulfate proteoglycan core proteins;
                     cd03588"
                     /db_xref="CDD:153058"
     Site            order(3148,3180..3183,3212,3222,3230,3232,3238,3241,
                     3243..3245)
                     /site_type="active"
                     /note="fibronectin type III repeats 3-5 binding site
                     [active]"
                     /db_xref="CDD:153058"
     Site            order(3191,3195,3218,3224..3225)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3195,3225)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153058"
     Site            order(3215,3217,3224,3238..3239)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153058"
     Region          3257..3313
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(3267,3287)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..3357
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
                     /coded_by="NM_001170558.1:281..10354"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:114122"
                     /db_xref="RGD:619940"
ORIGIN      
        1 mlinmngilw mcstllltha lhkakmeenp pvkgslsgkv ilpchfstlp tlppdyntse
       61 flrikwskie vdkngkdike ttvlvaqdgn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdagvyrc dvmygiedtq ntmslavdgv vfhyraatsr ytlnfesaqq acldigavia
      181 tpeqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec anrdarlatv gelhaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkpkq niseattiet
      361 ntlaetasps lskephmvpe ratpviplvt elpiftthfp pagnivnseq ksviysqait
      421 drvatespta agspinswda ddylpsgsgp lgkpdiseik eeglqsttvt sqhatashhg
      481 itedtqthes vtqieqievg plvtsmeitn hisfkeflet ktplestevt leqhqtdmpt
      541 vitspelatt shygvtlred dredialtvr sgqstrvfsq ipevitvskt sedttysqlg
      601 dlefvstati tmlgtdgslt degkepqtdd ktaedefgqs qptipfpsqh lteveslpys
      661 gdtisveris tvsypslqtd vtqgrertev prpglkkdpy avdeiqekit kdpfigtiee
      721 gfsgmslsts ssetsaerte svspaltiek ltvkpavasd vdemtiltrl etdvptsded
      781 vtsahlthst lnvevvtvlk wpgnednsts kplppterag ftksppvsls tvgivgkdke
      841 tpsftdggde ytlsldgtpk plekfseedl tsgefavtip tsisidsaek stlgepttgd
      901 rvlsttstkd lvinatvegs aldedmdask plftatpfvh tsdveesafv nysstqqptt
      961 yvdishtspl siipktewsv setsvplede vlgksdqdtl eqthleatms pealstievt
     1021 qgetqeepqt pgipfpalss tavmtketta feeegegsty tlsedrlmtd seivpslett
     1081 pvgtsypgga mtqqevemdt mvtqmssirp tvvlstepev syeaegsspm efastlkpfg
     1141 tqvtqlveet teegkktpld ytdlgsglfe qprvtelpdf smtpsdisvf taidslhrtt
     1201 plrppspfte ephifekeps ekttgdiilp resvtqhplt tlmdiiakkt esdidheyhm
     1261 tskppvmqpt rpsvverktt skpqelstsp ppagtkfhpd invyiievre nktgrmsdmv
     1321 vnghpidses keeepcseet dplhdlfaei lpelpdsfei diyhseeded geedcvnatd
     1381 vtttpsvqyi tgkphvttvp knpeaaearr glyesvapsq nfsntsatdt hqfipaetel
     1441 sttmqftksk eatelleitw kpetypetpe hfssgepdvf ptlpshdgkt tkwsefites
     1501 npntenpehk qpkpiplfpe efsgegaidq asqqtifsra tevalgketd qsptistssi
     1561 rsgsvsvhal eedpialtgi sqtdesmstv eswvemtpsq tvefsgsssa ptiegsgeve
     1621 eytnkifntv tdlpqreptd tlipldmsni mitdhhiytp attapldsql pstdarptqf
     1681 giqtttsewv sstsfegrkt eedkerdtna ahtgevqpat ersdrlllts elessnvaas
     1741 spldtwegfv pettstvsek emanttpvft etsdvanlet qsfehssssq prvqeelttl
     1801 sgkpplifmd lgsgdastdm efitassftl dlesdtkvkk elpstlspsv etssssepig
     1861 lapstvldie ivevmnqtsk ktliselsgk ptsqaevrdl ypglgedfsg dsseyptvss
     1921 ttmkeetvgm ggsenervkd tqtlssippt sdninpvpds kgfgstvast tafpweefmt
     1981 saegsgeels svrssvslvl plgvdilptt espyfdqefe eaaavteagk qsalpiavsg
     2041 ntvdltenrd ievnstmsvd lpqtmepakl wskpevnpek qeigsetvtq dkaqgqksfe
     2101 slhsslapeq ttlesqslie tevqtsyysm lttmktyntn eeveeegtsi ahmstpgpgi
     2161 kglesypthp eatgksysfs asalvtesgp arsvvmdsst qeeesiklfq kdmilthkes
     2221 nsdlsfsglg sgealpplpt tsvsltdmgk instlypets hmeslgtsil gdnhermknv
     2281 snevrtlise tgsisqdste apnttlsdtr teesttsplp fmklmdtehs pkqtlrweee
     2341 iqthrpqtmt gqmtndnssv seaeaaatsa paflpetysv emtkafatsp sqtsdlfdan
     2401 sgegsgevdg ldlvytsrtt qassqgdsmf ashgfiekhp evsrtetgat dgsptasamf
     2461 lhqseyness lyptstlpst vtyespsegi adglqdhirf evstlkpsrr katesviidl
     2521 dkedskdlgl aitesaivei lpeltsdrni iididhtkpv yeyipgiqtd ldsdiplgsh
     2581 gsseeslevq ekyeatinls pteeafdgsg dalpaghtqa iynesvtpsd gkqpedisfs
     2641 fatgipvsst etelntffpt vstlhipskl ttaspeidkp nieaislddi fesstlsdgq
     2701 aiadqsevis tlghlektqe eyeekkyggp sfqpeffsgv gevftdapay vsigrtysva
     2761 qpltefpnvv gqsdsthyte atsavssvte lspqtpssps pvyidsgvse ftevphksaq
     2821 paptaassqk liegsfkkvr anieatiksl gendhgtesp smspspaldi seddskpkll
     2881 edletsptkt etsqdspnka ndqipgktag ilagikttes gpvvtaaddm elgdatqrph
     2941 sasapaafrv etsmvpqpip qeperptfps leinhethts lfeesilats ekqvsqrild
     3001 ysnqatvstl dlntehsipp fsildnsnet afligiseet vegtavylpg pdlcktnpcl
     3061 nggtcyptet syvctcapgy sgdqceldfd echsnpcrng atcvdglntf rclclpsyvg
     3121 alceqdtetc dygwhkfqgq cykyfahrrt wdaaerecrl qgahltsils heeqmfvnrv
     3181 ghdyqwigln dkmfehdfrw tdgsalqyen wrpnqpdsff sagedcvvii whengqwndv
     3241 pcnyhltytc kkgtvacgqp pvvenaktfg kmkpryeins liryhckdgf iqrhlptirc
     3301 lgngrwampk itcmnpsayq rtyskkylkn sssvkdnsin tskhehrwsr rwqetrr
//
LOCUS       NP_542956                414 aa            linear   ROD 27-APR-2025
DEFINITION  COUP transcription factor 2 [Rattus norvegicus].
ACCESSION   NP_542956
VERSION     NP_542956.1
DBSOURCE    REFSEQ: accession NM_080778.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Han,S.H., Kim,Y.H., Park,S.J., Cho,J.G., Shin,Y.K., Hong,Y.B.,
            Yun,J., Han,J.Y., Park,H.T. and Park,J.I.
  TITLE     COUP-TFII plays a role in cAMP-induced Schwann cell differentiation
            and in vitro myelination by up-regulating Krox20
  JOURNAL   J Neurochem 165 (5), 660-681 (2023)
   PUBMED   36648143
  REMARK    GeneRIF: COUP-TFII plays a role in cAMP-induced Schwann cell
            differentiation and in vitro myelination by up-regulating Krox20.
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Kumarasamy,S., Waghulde,H., Gopalakrishnan,K., Mell,B., Morgan,E.
            and Joe,B.
  TITLE     Mutation within the hinge region of the transcription factor Nr2f2
            attenuates salt-sensitive hypertension
  JOURNAL   Nat Commun 6, 6252 (2015)
   PUBMED   25687237
  REMARK    GeneRIF: Nr2f2 mutation in the hinge region attenuates
            salt-sensitive hypertension
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Tornari,C., Towers,E.R., Gale,J.E. and Dawson,S.J.
  TITLE     Regulation of the orphan nuclear receptor Nr2f2 by the DFNA15
            deafness gene Pou4f3
  JOURNAL   PLoS One 9 (11), e112247 (2014)
   PUBMED   25372459
  REMARK    GeneRIF: These data demonstrate that Nr2f2 is a direct target of
            POU4F3 in vitro and that this regulatory relationship may be
            relevant to hair cell development and survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Howell,M., Li,R., Zhang,R., Li,Y., Chen,W. and Chen,G.
  TITLE     The expression of Apoc3 mRNA is regulated by HNF4alpha and
            COUP-TFII, but not acute retinoid treatments, in primary rat
            hepatocytes and hepatoma cells
  JOURNAL   Mol Cell Biochem 387 (1-2), 241-250 (2014)
   PUBMED   24234421
  REMARK    GeneRIF: Apoc3 expression is regulated by HNF4a and COUP-TFII but
            not by retinoic acid in rat hepatocytes.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Kim,B.J. and Scott,D.A.
  TITLE     Mouse model reveals the role of RERE in cerebellar foliation and
            the migration and maturation of Purkinje cells
  JOURNAL   PLoS One 9 (1), e87518 (2014)
   PUBMED   24466353
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Zhang,Y. and Dufau,M.L.
  TITLE     Repression of the luteinizing hormone receptor gene promoter by
            cross talk among EAR3/COUP-TFI, Sp1/Sp3, and TFIIB
  JOURNAL   Mol Cell Biol 23 (19), 6958-6972 (2003)
   PUBMED   12972613
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Kang,S., Spann,N.J., Hui,T.Y. and Davis,R.A.
  TITLE     ARP-1/COUP-TF II determines hepatoma phenotype by acting as both a
            transcriptional repressor of microsomal triglyceride transfer
            protein and an inducer of CYP7A1
  JOURNAL   J Biol Chem 278 (33), 30478-30486 (2003)
   PUBMED   12777384
  REMARK    GeneRIF: ARP-1/COUP-TFII acts as both a transcriptional repressor
            of microsomal triglyceride transfer protein and as a transcription
            activator of CYP7A1.
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Chu,K. and Zingg,H.H.
  TITLE     The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers
            of the human oxytocin gene promoter
  JOURNAL   J Mol Endocrinol 19 (2), 163-172 (1997)
   PUBMED   9343308
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Marcus,S.L., Winrow,C.J., Capone,J.P. and Rachubinski,R.A.
  TITLE     A p56(lck) ligand serves as a coactivator of an orphan nuclear
            hormone receptor
  JOURNAL   J Biol Chem 271 (44), 27197-27200 (1996)
   PUBMED   8910285
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Ben-Shushan,E., Sharir,H., Pikarsky,E. and Bergman,Y.
  TITLE     A dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and
            retinoic acid receptor:retinoid X receptor heterodimers regulates
            Oct-3/4 expression in embryonal carcinoma cells
  JOURNAL   Mol Cell Biol 15 (2), 1034-1048 (1995)
   PUBMED   7823919
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF003944.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF003944.1, EV770714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..414
                     /product="COUP transcription factor 2"
                     /note="ARP-1; COUPb; COUP-TF2; COUP-TF II; apolipoprotein
                     AI regulatory protein 1; ovalbumin upstream promoter beta
                     nuclear receptor; COUP transcription factor II;
                     apolipoprotein A-I regulatory protein 1"
                     /calculated_mol_wt=45470
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O09018.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P24468; propagated from
                     UniProtKB/Swiss-Prot (O09018.1)"
     Region          79..151
                     /region_name="NR_DBD_COUP_TF"
                     /note="DNA-binding domain of chicken ovalbumin upstream
                     promoter transcription factors (COUP-TFs) is composed of
                     two C4-type zinc fingers; cd06958"
                     /db_xref="CDD:143516"
     Site            order(79,82,96,99,115,121,131,134)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143516"
     Site            order(88..91,97..98,100,102,105,108,116,128..129,132,135,
                     146)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143516"
     Region          117..414
                     /region_name="Interaction with ZFPM2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O09018.1)"
     Region          177..411
                     /region_name="NR_LBD_COUP-TF"
                     /note="Ligand binding domain of chicken ovalbumin upstream
                     promoter transcription factors, a member of the nuclear
                     receptor family; cd06948"
                     /db_xref="CDD:132746"
     Site            order(211..212,216,250,254,257,271,292)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132746"
     Site            order(221,224,228,233,238..239,241..242,245..246)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132746"
     Region          337..414
                     /region_name="Important for dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (O09018.1)"
     CDS             1..414
                     /gene="Nr2f2"
                     /gene_synonym="Tfcoup2"
                     /coded_by="NM_080778.2:185..1429"
                     /db_xref="GeneID:113984"
                     /db_xref="RGD:69305"
ORIGIN      
        1 mamvvstwrd pqdevpgsqg sqasqappvp gpppgaphtp qtpgqggpas tpaqtaagsq
       61 ggpggpgsdk qqqqqhiecv vcgdkssgkh ygqftcegck sffkrsvrrn lsytcranrn
      121 cpidqhhrnq cqycrlkkcl kvgmrreavq rgrmpptqpt hgqfaltngd plnchsylsg
      181 yislllraep yptsrfgsqc mqpnnimgie nicelaarml fsavewarni pffpdlqitd
      241 qvallrltws elfvlnaaqc smplhvapll aaaglhaspm sadrvvafmd hirifqeqve
      301 klkalhvdsa eysclkaivl ftsdacglsd vahveslqek sqcaleeyvr sqypnqptrf
      361 gklllrlpsl rtvsssvieq lffvrlvgkt pietlirdml lsgssfnwpy maiq
//
LOCUS       NP_001041345             338 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial ornithine transporter 1 [Rattus norvegicus].
ACCESSION   NP_001041345 XP_001064456 XP_001064514 XP_001064627 XP_001064682
            XP_224969
VERSION     NP_001041345.1
DBSOURCE    REFSEQ: accession NM_001047880.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Fiermonte,G., Dolce,V., David,L., Santorelli,F.M., Dionisi-Vici,C.,
            Palmieri,F. and Walker,J.E.
  TITLE     The mitochondrial ornithine transporter. Bacterial expression,
            reconstitution, functional characterization, and tissue
            distribution of two human isoforms
  JOURNAL   J Biol Chem 278 (35), 32778-32783 (2003)
   PUBMED   12807890
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Camacho,J.A., Rioseco-Camacho,N., Andrade,D., Porter,J. and Kong,J.
  TITLE     Cloning and characterization of human ORNT2: a second mitochondrial
            ornithine transporter that can rescue a defective ORNT1 in patients
            with the hyperornithinemia-hyperammonemia-homocitrullinuria
            syndrome, a urea cycle disorder
  JOURNAL   Mol Genet Metab 79 (4), 257-271 (2003)
   PUBMED   12948741
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Morris,S.M. Jr. and Kepka-Lenhart,D.
  TITLE     Hormonal induction of hepatic mitochondrial ornithine/citrulline
            transporter mRNA
  JOURNAL   Biochem Biophys Res Commun 294 (4), 749-752 (2002)
   PUBMED   12061769
  REMARK    GeneRIF: Transcriptional Activation of ORNT1 mRNA by dexamethasone
            in hepatocytes.
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Tsujino,S., Kanazawa,N., Ohashi,T., Eto,Y., Saito,T., Kira,J. and
            Yamada,T.
  TITLE     Three novel mutations (G27E, insAAC, R179X) in the ORNT1 gene of
            Japanese patients with hyperornithinemia, hyperammonemia, and
            homocitrullinuria syndrome
  JOURNAL   Ann Neurol 47 (5), 625-631 (2000)
   PUBMED   10805333
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Camacho,J.A., Obie,C., Biery,B., Goodman,B.K., Hu,C.A.,
            Almashanu,S., Steel,G., Casey,R., Lambert,M., Mitchell,G.A. and
            Valle,D.
  TITLE     Hyperornithinaemia-hyperammonaemia-homocitrullinuria syndrome is
            caused by mutations in a gene encoding a mitochondrial ornithine
            transporter
  JOURNAL   Nat Genet 22 (2), 151-158 (1999)
   PUBMED   10369256
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Indiveri,C., Tonazzi,A., Stipani,I. and Palmieri,F.
  TITLE     The purified and reconstituted ornithine/citrulline carrier from
            rat liver mitochondria: electrical nature and coupling of the
            exchange reaction with H+ translocation
  JOURNAL   Biochem J 327 (Pt 2) (Pt 2), 349-355 (1997)
   PUBMED   9359400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CA339807.1, AY325139.1 and DY310527.1.
            
            On or before Sep 8, 2006 this sequence version replaced
            XP_224969.2, XP_001064514.1, XP_001064456.1, XP_001064682.1,
            XP_001064627.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY325139.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMD00132261,
                                    SAMD00132262 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..338
                     /product="mitochondrial ornithine transporter 1"
                     /note="ornithine transporter) member 15; solute carrier
                     family 25 (mitochondrial carrier; ornithine transporter)
                     member 15"
                     /calculated_mol_wt=36790
     Region          9..94
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          <122..198
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          205..332
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     CDS             1..338
                     /gene="Slc25a15"
                     /gene_synonym="Ab1-114; Ornt1"
                     /coded_by="NM_001047880.3:61..1077"
                     /db_xref="GeneID:306574"
                     /db_xref="RGD:1311488"
ORIGIN      
        1 mksnpaiqaa idltagaagg tacvltgqpf dtmkvkmqtf pdlyrgltdc clrtysqvgf
       61 rgfykgtspa lianiaensv lfmcygfcqq vvrkvvgldr qaklsdlqna aagsfasafa
      121 alvlcptelv kcrlqtmyem etsgkiaasq ntvwsvvkei frkdgplgfy hglsstllre
      181 vpgyffffgg yelsrsffas grskdelgpi plmlsggfgg iclwlavypv dciksriqvl
      241 smtgkqtgli rtflsivkne ggyrlsesrl ydvsfvqpkt clsgvhyvgi lklglregit
      301 alysglkptm irafpangal flayeysrkl mmsqleac
//
LOCUS       NP_001258021             391 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001258021
VERSION     NP_001258021.1
DBSOURCE    REFSEQ: accession NM_001271092.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1 and CB585874.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY217033.1, SRR26360172.2290769.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..391
                     /product="protein NDRG4 isoform 2"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=42834
     Region          60..342
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..391
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_001271092.1:109..1284"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 mkvlghrlql ltglllhdvt maglqelrfp eekpllrgqd ateldnpdaf lsvvdtdwke
       61 hdietpygll hvvirgspkg nrpailtyhd vglnhklcfn tlfnledmqe itkhfvvchv
      121 dapgqqvgas qfpqgyqfps meqlatmlps vvqhfgfkyv igigvgagay vlakfalifp
      181 dlveglvlmn idpngkgwid waatklsglt stlpdtvlsh lfsqeelvnn telvqsyrqq
      241 issvvnqanl qlfwnmynsr rdldinrpgt vpnaktlrcp vmlvvgdnap aedgvvecns
      301 kldpttttfl kmadsgglpq vtqpgkltea fkyflqgmgy mpsasmtrla rsrtasltsa
      361 ssvdgsrpqp cthsdssegm gqvnhtmevs c
//
LOCUS       NP_062187                580 aa            linear   ROD 27-APR-2025
DEFINITION  small conductance calcium-activated potassium channel protein 2
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_062187
VERSION     NP_062187.1
DBSOURCE    REFSEQ: accession NM_019314.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Rahman,M.A., Orfali,R., Dave,N., Lam,E., Naguib,N., Nam,Y.W. and
            Zhang,M.
  TITLE     KCa 2.2 (KCNN2): A physiologically and therapeutically important
            potassium channel
  JOURNAL   J Neurosci Res 101 (11), 1699-1710 (2023)
   PUBMED   37466411
  REMARK    GeneRIF: KCa 2.2 (KCNN2): A physiologically and therapeutically
            important potassium channel.
            Review article
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Nam,Y.W., Rahman,M.A., Yang,G., Orfali,R., Cui,M. and Zhang,M.
  TITLE     Loss-of-function KCa2.2 mutations abolish channel activity
  JOURNAL   Am J Physiol Cell Physiol 324 (3), C658-C664 (2023)
   PUBMED   36717104
  REMARK    GeneRIF: Loss-of-function KCa2.2 mutations abolish channel
            activity.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Yang,B., Jiang,Q., He,S., Li,T., Ou,X., Chen,T., Fan,X., Jiang,F.,
            Zeng,X., Huang,C.L., Lei,M. and Tan,X.
  TITLE     Ventricular SK2 upregulation following angiotensin II challenge:
            Modulation by p21-activated kinase-1
  JOURNAL   J Mol Cell Cardiol 164, 110-125 (2022)
   PUBMED   34774547
  REMARK    GeneRIF: Ventricular SK2 upregulation following angiotensin II
            challenge: Modulation by p21-activated kinase-1.
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Autuori,E., Sedlak,P., Xu,L., C Ridder,M., Tedoldi,A. and Sah,P.
  TITLE     rSK1 in Rat Neurons: A Controller of Membrane rSK2?
  JOURNAL   Front Neural Circuits 13, 21 (2019)
   PUBMED   31001092
  REMARK    GeneRIF: rSK1 appears to act as chaperone for rSK2 channels and
            expression of rSK1 may control the level of functional SK current
            in rat neurons.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Ewin,S.E., Morgan,J.W., Niere,F., McMullen,N.P., Barth,S.H.,
            Almonte,A.G., Raab-Graham,K.F. and Weiner,J.L.
  TITLE     Chronic Intermittent Ethanol Exposure Selectively Increases
            Synaptic Excitability in the Ventral Domain of the Rat Hippocampus
  JOURNAL   Neuroscience 398, 144-157 (2019)
   PUBMED   30481568
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Schumacher,M.A., Crum,M. and Miller,M.C.
  TITLE     Crystal structures of apocalmodulin and an apocalmodulin/SK
            potassium channel gating domain complex
  JOURNAL   Structure 12 (5), 849-860 (2004)
   PUBMED   15130477
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Monaghan,A.S., Benton,D.C., Bahia,P.K., Hosseini,R., Shah,Y.A.,
            Haylett,D.G. and Moss,G.W.
  TITLE     The SK3 subunit of small conductance Ca2+-activated K+ channels
            interacts with both SK1 and SK2 subunits in a heterologous
            expression system
  JOURNAL   J Biol Chem 279 (2), 1003-1009 (2004)
   PUBMED   14559917
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Schumacher,M.A., Rivard,A.F., Bachinger,H.P. and Adelman,J.P.
  TITLE     Structure of the gating domain of a Ca2+-activated K+ channel
            complexed with Ca2+/calmodulin
  JOURNAL   Nature 410 (6832), 1120-1124 (2001)
   PUBMED   11323678
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Xia,X.M., Fakler,B., Rivard,A., Wayman,G., Johnson-Pais,T.,
            Keen,J.E., Ishii,T., Hirschberg,B., Bond,C.T., Lutsenko,S.,
            Maylie,J. and Adelman,J.P.
  TITLE     Mechanism of calcium gating in small-conductance calcium-activated
            potassium channels
  JOURNAL   Nature 395 (6701), 503-507 (1998)
   PUBMED   9774106
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Kohler,M., Hirschberg,B., Bond,C.T., Kinzie,J.M., Marrion,N.V.,
            Maylie,J. and Adelman,J.P.
  TITLE     Small-conductance, calcium-activated potassium channels from
            mammalian brain
  JOURNAL   Science 273 (5282), 1709-1714 (1996)
   PUBMED   8781233
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. It encodes
            isoform 2 which is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U69882.1, SRR26643298.73944.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q11"
     Protein         1..580
                     /product="small conductance calcium-activated potassium
                     channel protein 2 isoform 2"
                     /note="small conductance calcium-activated potassium
                     channel protein 2; small conductance calcium-activated
                     potassium channel protein 2-like; potassium
                     intermediate/small conductance calcium-activated channel,
                     subfamily N, member 2; potassium channel, calcium
                     activated intermediate/small conductance subfamily N
                     alpha, member 2"
                     /calculated_mol_wt=63717
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          88..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          122..231
                     /region_name="SK_channel"
                     /note="Calcium-activated SK potassium channel; pfam03530"
                     /db_xref="CDD:460958"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P70604.1)"
     Site            169..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          320..399
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          413..489
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:11323678"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     Region          413..488
                     /region_name="CaMBD"
                     /note="Calmodulin binding domain; smart01053"
                     /db_xref="CDD:198121"
     Region          551..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P70604.1)"
     CDS             1..580
                     /gene="Kcnn2"
                     /gene_synonym="KCa2.2; SK2; SKCa 2; SKCa2"
                     /coded_by="NM_019314.2:1..1743"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:54262"
                     /db_xref="RGD:2963"
ORIGIN      
        1 msscrynggv mrplsnlsss rrnlhemdse aqplqppasv vgggggassp saaaaasssa
       61 peivvskpeh nnsnnlalyg tggggstggg gggggggggs ghgsssgtks skkknqnigy
      121 klghrralfe krkrlsdyal ifgmfgivvm vietelswga ydkaslysla lkclislsti
      181 illgliivyh areiqlfmvd ngaddwriam tyerifficl eilvcaihpi pgnytftwta
      241 rlafsyapst ttadvdiils ipmflrlyli arvmllhskl ftdassrsig alnkinfntr
      301 fvmktlmtic pgtvllvfsi slwiiaawtv raceryhdqq dvtsnflgam wlisitflsi
      361 gygdmvpnty cgkgvclltg imgagctalv vavvarklel tkaekhvhnf mmdtqltkrv
      421 knaaanvlre twliykntkl vkkidhakvr khqrkflqai hqlrsvkmeq rklndqantl
      481 vdlaktqnim ydmisdlner sedfekrivt letkletlig sihalpglis qtirqqqrdf
      541 ietqmenydk hvtynaersr sssrrrrsss tapptssess
//
LOCUS       NP_001258024             339 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 6 [Rattus norvegicus].
ACCESSION   NP_001258024
VERSION     NP_001258024.1
DBSOURCE    REFSEQ: accession NM_001271095.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1 and CB585874.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence and lacks an alternate in-frame exon compared to
            variant 1. The resulting isoform (6) has a shorter and distinct
            N-terminus and lacks an alternate internal segment compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY217029.1, SRR26360194.759550.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..339
                     /product="protein NDRG4 isoform 6"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=36985
     Region          8..290
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..339
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_001271095.1:130..1149"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 mpecwdgehd ietpygllhv virgspkgnr pailtyhdvg lnhklcfntl fnledmqeit
       61 khfvvchvda pgqqvgasqf pqgyqfpsme qlatmlpsvv qhfgfkyvig igvgagayvl
      121 akfalifpdl veglvlmnid pngkgwidwa atklsgltst lpdtvlshlf sqeelvnnte
      181 lvqsyrqqis svvnqanlql fwnmynsrrd ldinrpgtvp naktlrcpvm lvvgdnapae
      241 dgvvecnskl dpttttflkm adsgglpqvt qpgklteafk yflqgmgymp sasmtrlars
      301 rtasltsass vdgsrpqpct hsdssegmgq vnhtmevsc
//
LOCUS       NP_599201                352 aa            linear   ROD 27-APR-2025
DEFINITION  RING finger protein 39 [Rattus norvegicus].
ACCESSION   NP_599201
VERSION     NP_599201.1
DBSOURCE    REFSEQ: accession NM_134374.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Liu,J., Liu,W., Li,H., Deng,Q., Yang,M., Li,X. and Liang,Z.
  TITLE     Identification of key genes and pathways associated with
            cholangiocarcinoma development based on weighted gene correlation
            network analysis
  JOURNAL   PeerJ 7, e7968 (2019)
   PUBMED   31687280
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Matsuo,R., Asada,A., Fujitani,K. and Inokuchi,K.
  TITLE     LIRF, a gene induced during hippocampal long-term potentiation as
            an immediate-early gene, encodes a novel RING finger protein
  JOURNAL   Biochem Biophys Res Commun 289 (2), 479-484 (2001)
   PUBMED   11716498
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Matsuo,R., Murayama,A., Saitoh,Y., Sakaki,Y. and Inokuchi,K.
  TITLE     Identification and cataloging of genes induced by long-lasting
            long-term potentiation in awake rats
  JOURNAL   J Neurochem 74 (6), 2239-2249 (2000)
   PUBMED   10820183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883051.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB070897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..352
                     /product="RING finger protein 39"
                     /EC_number="2.3.2.27"
                     /note="LTP-induced RING finger protein"
                     /calculated_mol_wt=38214
     Region          14..71
                     /region_name="RING-HC_RNF39"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 39 (RNF39) and similar proteins; cd16592"
                     /db_xref="CDD:438254"
     Region          98..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q920M2.1)"
     Region          161..347
                     /region_name="SPRY"
                     /note="SPRY domain; cl02614"
                     /db_xref="CDD:470632"
     CDS             1..352
                     /gene="Rnf39"
                     /gene_synonym="Hzfw1; Lirf"
                     /coded_by="NM_134374.2:171..1229"
                     /db_xref="GeneID:171387"
                     /db_xref="RGD:628854"
ORIGIN      
        1 mevpelgpgl verleqlatc plcggpfedp vllacehsfc rsclarcwgs paapgseeat
       61 pscpccgqpc prrslrsnvr lavevrisrg lreklaepga rtgrrrggri ptmgcldpqg
      121 edmrktwrrf dvpvpkssns eedlpedypv vknmlhrlta dltldprtah rdllissdyr
      181 gvslappgtp vpldsperfd rlravlgaqg fasgrhcwev etaegacfrd slakdedage
      241 scyavgaage svtrkglikl cpseaiwave grggrlwalt apeptllgga rpppqrirvd
      301 ldwergrvaf ydgrsldllf afqapgplge rvfpllctcd praplrivpg ea
//
LOCUS       NP_001178036             586 aa            linear   ROD 27-APR-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            B [Rattus norvegicus].
ACCESSION   NP_001178036 XP_001074480
VERSION     NP_001178036.1
DBSOURCE    REFSEQ: accession NM_001191107.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Maletzki,C., Huehns,M., Bauer,I., Ripperger,T., Mork,M.M.,
            Vilar,E., Klocking,S., Zettl,H., Prall,F. and Linnebacher,M.
  TITLE     Frameshift mutational target gene analysis identifies similarities
            and differences in constitutional mismatch repair-deficiency and
            Lynch syndrome
  JOURNAL   Mol Carcinog 56 (7), 1753-1764 (2017)
   PUBMED   28218421
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     TFIIB-related factors in RNA polymerase I transcription
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 265-273 (2013)
   PUBMED   22960599
  REMARK    Review article
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Schneider,D.A.
  TITLE     RNA polymerase I activity is regulated at multiple steps in the
            transcription cycle: recent insights into factors that influence
            transcription elongation
  JOURNAL   Gene 493 (2), 176-184 (2012)
   PUBMED   21893173
  REMARK    Review article
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Naidu,S., Friedrich,J.K., Russell,J. and Zomerdijk,J.C.
  TITLE     TAF1B is a TFIIB-like component of the basal transcription
            machinery for RNA polymerase I
  JOURNAL   Science 333 (6049), 1640-1642 (2011)
   PUBMED   21921199
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I
            general transcription factors
  JOURNAL   Science 333 (6049), 1637-1640 (2011)
   PUBMED   21921198
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Jul 17, 2010 this sequence version replaced XP_001074480.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.484205.1,
                                           SRR26360190.19550.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..586
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit B"
                     /note="TBP-associated factor 1B; TATA box-binding
                     protein-associated factor 1B; TATA box binding protein
                     (Tbp)-associated factor, RNA polymerase I, B;
                     transcription initiation factor SL1/TIF-IB subunit B; RNA
                     polymerase I-specific TBP-associated factor 63 kDa"
                     /calculated_mol_wt=67891
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q53T94; propagated from
                     UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Region          12..37
                     /region_name="zf-RRN7"
                     /note="Zinc-finger of RNA-polymerase I-specific TFIIB,
                     Rrn7; pfam11781"
                     /db_xref="CDD:463348"
     Region          40..68
                     /region_name="B-reader. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Region          69..73
                     /region_name="B-linker. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Region          74..259
                     /region_name="N-terminal cyclin fold.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Region          158..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Region          260..370
                     /region_name="C-terminal cyclin fold.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZYB7.1)"
     Site            438
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q53T94; propagated from
                     UniProtKB/Swiss-Prot (D3ZYB7.1)"
     CDS             1..586
                     /gene="Taf1b"
                     /gene_synonym="TAFI63"
                     /coded_by="NM_001191107.1:1..1761"
                     /db_xref="GeneID:690450"
                     /db_xref="RGD:1596058"
ORIGIN      
        1 mdveqmkaft drcsqcaavs wgltdegkyy ctschnvtdr seevvstavi pntkinsisr
       61 glrqrskhek gwdwyvcegf qcilyhqaea letlgvspel knevlhsfwk rylqkskqay
      121 cknpvrtsgr kakvlednlq ssdwgsdfel lsdttcppes gaefqsdsqt pkpfpatkrs
      181 sksasvcsgs vdgveyserk ekgllkmtvp rtlalcylsl lwqretitls dllrfveedr
      241 ipyinafkvf peemkvygrd kgifaveswp dyediyknmi evavfldlpr fpditedcyl
      301 hpntlcmkyl levnlpeemy tltcqvvklt gigevdfltf dpiakmtrtv khdvqavavi
      361 vlvlkllfll ddklewsysd laeayneghk eetpqfdfrk wyqvmkktfd ekrrkweear
      421 akyvwktkrp lyrshidksv aykrremven lqkqfsalig sapeverqap ssfqlnwtge
      481 dtgspcfhgh slqglliskg qalitknsly wlsthkfcks yckhvttyee snfslsyqfi
      541 lnifsfllri ktsalheevs llekklfekk yneskrssrs kkvrrh
//
LOCUS       NP_071970                226 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione peroxidase 3 precursor [Rattus norvegicus].
ACCESSION   NP_071970 XP_346396
VERSION     NP_071970.2
DBSOURCE    REFSEQ: accession NM_022525.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Li,Y., Zhou,Y., Liu,D., Wang,Z., Qiu,J., Zhang,J., Chen,P.,
            Zeng,G., Guo,Y., Wang,X., DiSanto,M.E. and Zhang,X.
  TITLE     Glutathione Peroxidase 3 induced mitochondria-mediated apoptosis
            via AMPK /ERK1/2 pathway and resisted autophagy-related ferroptosis
            via AMPK/mTOR pathway in hyperplastic prostate
  JOURNAL   J Transl Med 21 (1), 575 (2023)
   PUBMED   37633909
  REMARK    GeneRIF: Glutathione Peroxidase 3 induced mitochondria-mediated
            apoptosis via AMPK /ERK1/2 pathway and resisted autophagy-related
            ferroptosis via AMPK/mTOR pathway in hyperplastic prostate.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Cueto-Urena,C., Ramirez-Exposito,M.J., Mayas,M.D.,
            Carrera-Gonzalez,M.P., Godoy-Hurtado,A. and Martinez-Martos,J.M.
  TITLE     Glutathione Peroxidase gpx1 to gpx8 Genes Expression in
            Experimental Brain Tumors Reveals Gender-Dependent Patterns
  JOURNAL   Genes (Basel) 14 (9), 1674 (2023)
   PUBMED   37761814
  REMARK    GeneRIF: Glutathione Peroxidase gpx1 to gpx8 Genes Expression in
            Experimental Brain Tumors Reveals Gender-Dependent Patterns.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Saleh,S., Ghanaatpisheh,A., Haghshenas,H., Parvin,N.,
            Mikaeiliagah,E., Kargar Jahromi,H. and Ebrahimi,B.
  TITLE     The effect of leaf hydroalcoholic extract of Ephedra pachyclada
            infertility in male rats treated with cyclophosphamide: An
            experimental study
  JOURNAL   Int J Reprod Biomed 21 (4), 285-294 (2023)
   PUBMED   37260555
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Pei,J., Tian,X., Yu,C., Luo,J., Zhang,J., Hua,Y. and Wei,G.
  TITLE     GPX3 and GSTT1 as biomarkers related to oxidative stress during
            renal ischemia reperfusion injuries and their relationship with
            immune infiltration
  JOURNAL   Front Immunol 14, 1136146 (2023)
   PUBMED   37033969
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Wu,X., Tang,S., Dai,Q., Yi,B., Yang,S., Sun,J., Zhong,Y., Lin,W.,
            Liu,J., Liu,Y., Wang,J., Liu,J., Liao,Q., Zhang,W. and Zhang,H.
  TITLE     Vitamin D-vitamin D receptor alleviates oxidative stress in
            ischemic acute kidney injury via upregulating glutathione
            peroxidase 3
  JOURNAL   FASEB J 37 (2), e22738 (2023)
   PUBMED   36583727
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Yoshimura,S., Watanabe,K., Suemizu,H., Onozawa,T., Mizoguchi,J.,
            Tsuda,K., Hatta,H. and Moriuchi,T.
  TITLE     Tissue specific expression of the plasma glutathione peroxidase
            gene in rat kidney
  JOURNAL   J Biochem 109 (6), 918-923 (1991)
   PUBMED   1939013
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Esworthy,R.S., Chu,F.F., Paxton,R.J., Akman,S. and Doroshow,J.H.
  TITLE     Characterization and partial amino acid sequence of human plasma
            glutathione peroxidase
  JOURNAL   Arch Biochem Biophys 286 (2), 330-336 (1991)
   PUBMED   1897960
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Avissar,N., Whitin,J.C., Allen,P.Z., Palmer,I.S. and Cohen,H.J.
  TITLE     Antihuman plasma glutathione peroxidase antibodies: immunologic
            investigations to determine plasma glutathione peroxidase protein
            and selenium content in plasma
  JOURNAL   Blood 73 (1), 318-323 (1989)
   PUBMED   2491950
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Maddipati,K.R. and Marnett,L.J.
  TITLE     Characterization of the major hydroperoxide-reducing activity of
            human plasma. Purification and properties of a selenium-dependent
            glutathione peroxidase
  JOURNAL   J Biol Chem 262 (36), 17398-17403 (1987)
   PUBMED   3693360
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Takahashi,K., Avissar,N., Whitin,J. and Cohen,H.
  TITLE     Purification and characterization of human plasma glutathione
            peroxidase: a selenoglycoprotein distinct from the known cellular
            enzyme
  JOURNAL   Arch Biochem Biophys 256 (2), 677-686 (1987)
   PUBMED   3619451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000010.1, FM059908.1,
            FM066296.1, FM067533.1, FM066354.1 and CK477403.1.
            
            On Jan 21, 2004 this sequence version replaced NP_071970.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by
            glutathione, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            is secreted and is predominantly expressed in rat kidney, which
            appears to be the major source of the enzyme in plasma.
            Dysregulation of this isozyme has been associated with
            obesity-related metabolic complications. This isozyme is also a
            selenoprotein, containing the rare amino acid selenocysteine (Sec)
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon, rather than as a stop signal.
            [provided by RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228545.1, FQ228965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            protein contains selenocysteine  :: PMID: 1939013
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..226
                     /product="glutathione peroxidase 3 precursor"
                     /EC_number="1.11.1.9"
                     /note="plasma glutathione peroxidase"
                     /calculated_mol_wt=22930
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23764.2)"
                     /calculated_mol_wt=2512
     mat_peptide     25..226
                     /product="Glutathione peroxidase 3. /id=PRO_0000013064"
                     /note="propagated from UniProtKB/Swiss-Prot (P23764.2)"
                     /calculated_mol_wt=22930
     Region          39..211
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(73,107,181)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            73
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(106,109,111,114,117,121)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..226
                     /gene="Gpx3"
                     /gene_synonym="GPx-3; GPx-P; Gpxp; GSHPx-3; GSHPx-P"
                     /coded_by="NM_022525.4:152..832"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:64317"
                     /db_xref="RGD:69224"
ORIGIN      
        1 marilrascl lslllagfvp pgrgqekskt dchggmsgti yeygaltidg eeyipfkqya
       61 gkyilfvnva syugltdqyl elnalqeelg pfglvilgfp cnqfgkqepg enseilpslk
      121 yvrpgggfvp nfqlfekgdv ngekeqkfyt flknscppta ellgspgrlf wepmkihdir
      181 wnfekflvgp dgipimrwyh rttvsnvkmd ilsymrrqaa lgargk
//
LOCUS       NP_001295227             949 aa            linear   ROD 27-APR-2025
DEFINITION  AP-1 complex subunit beta-1 [Rattus norvegicus].
ACCESSION   NP_001295227 NP_058973
VERSION     NP_001295227.1
DBSOURCE    REFSEQ: accession NM_001308298.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Piccoli,G., Condliffe,S.B., Bauer,M., Giesert,F., Boldt,K., De
            Astis,S., Meixner,A., Sarioglu,H., Vogt-Weisenhorn,D.M., Wurst,W.,
            Gloeckner,C.J., Matteoli,M., Sala,C. and Ueffing,M.
  TITLE     LRRK2 controls synaptic vesicle storage and mobilization within the
            recycling pool
  JOURNAL   J Neurosci 31 (6), 2225-2237 (2011)
   PUBMED   21307259
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Evers,D.M., Matta,J.A., Hoe,H.S., Zarkowsky,D., Lee,S.H.,
            Isaac,J.T. and Pak,D.T.
  TITLE     Plk2 attachment to NSF induces homeostatic removal of GluA2 during
            chronic overexcitation
  JOURNAL   Nat Neurosci 13 (10), 1199-1207 (2010)
   PUBMED   20802490
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Nijboer,C.H., Heijnen,C.J., Groenendaal,F., van Bel,F. and
            Kavelaars,A.
  TITLE     Alternate pathways preserve tumor necrosis factor-alpha production
            after nuclear factor-kappaB inhibition in neonatal cerebral
            hypoxia-ischemia
  JOURNAL   Stroke 40 (10), 3362-3368 (2009)
   PUBMED   19628795
  REMARK    GeneRIF: Our data indicate that the switch to JNK/AP-1 activation
            preserves HI-induced TNF-alpha expression and thereby might
            contribute to the neuroprotective effect of TAT-NBD possibly
            through a TNF-R2 dependent mechanism.
REFERENCE   4  (residues 1 to 949)
  AUTHORS   Jung,K.J., Lee,E.K., Kim,J.Y., Zou,Y., Sung,B., Heo,H.S., Kim,M.K.,
            Lee,J., Kim,N.D., Yu,B.P. and Chung,H.Y.
  TITLE     Effect of short term calorie restriction on pro-inflammatory NF-kB
            and AP-1 in aged rat kidney
  JOURNAL   Inflamm Res 58 (3), 143-150 (2009)
   PUBMED   19199090
  REMARK    GeneRIF: Results suggest that 10-day calorie restriction can
            attenuate the altered signal transduction for inflammatory
            processes which is mediated through reactive species-induced NF-kB
            and AP-1 in aged kidney.
REFERENCE   5  (residues 1 to 949)
  AUTHORS   Kim,K.S., Kim,H.Y., Joe,E.H. and Jou,I.
  TITLE     Matrix metalloproteinase-3 induction in rat brain astrocytes: focus
            on the role of two AP-1 elements
  JOURNAL   Biochem J 410 (3), 605-611 (2008)
   PUBMED   18072934
  REMARK    GeneRIF: results indicate that AP-1 could control MMP-3 induction
            in brain astrocytes and that its regulation through specific AP-1
            elements could be exploited in the treatment of brain pathologies
            in which increased expression of MMP-3 plays crucial roles
REFERENCE   6  (residues 1 to 949)
  AUTHORS   Helmig,S., Schuckenbohmer,P., Heger,J., Euler,G., Piper,H.M. and
            Schluter,K.D.
  TITLE     Direct effects of the angiotensin-converting enzyme inhibitor
            ramiprilat on adult rat ventricular cardiomyocytes
  JOURNAL   Acta Physiol (Oxf) 191 (4), 267-274 (2007)
   PUBMED   17825088
  REMARK    GeneRIF: Ramiprilat exerts direct, bradykinin-receptor independent
            effects on cardiomyocytes that improve cellular function without a
            corresponding effect on AP-1 activation or induction of AP-1
            dependent effects.
REFERENCE   7  (residues 1 to 949)
  AUTHORS   Peyrard,M., Fransson,I., Xie,Y.G., Han,F.Y., Ruttledge,M.H.,
            Swahn,S., Collins,J.E., Dunham,I., Collins,V.P. and Dumanski,J.P.
  TITLE     Characterization of a new member of the human beta-adaptin gene
            family from chromosome 22q12, a candidate meningioma gene
  JOURNAL   Hum Mol Genet 3 (8), 1393-1399 (1994)
   PUBMED   7987321
REFERENCE   8  (residues 1 to 949)
  AUTHORS   Gallusser,A. and Kirchhausen,T.
  TITLE     The beta 1 and beta 2 subunits of the AP complexes are the clathrin
            coat assembly components
  JOURNAL   EMBO J 12 (13), 5237-5244 (1993)
   PUBMED   8262066
REFERENCE   9  (residues 1 to 949)
  AUTHORS   Kirchhausen,T., Nathanson,K.L., Matsui,W., Vaisberg,A., Chow,E.P.,
            Burne,C., Keen,J.H. and Davis,A.E.
  TITLE     Structural and functional division into two domains of the large
            (100- to 115-kDa) chains of the clathrin-associated protein complex
            AP-2
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2612-2616 (1989)
   PUBMED   2495531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jan 18, 2018 this sequence version replaced NP_058973.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.57817.1,
                                           SRR26643298.55282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..949
                     /product="AP-1 complex subunit beta-1"
                     /note="beta-adaptin 1; golgi adaptor HA1/AP1 adaptin beta
                     subunit; clathrin assembly protein complex 1 beta large
                     chain; adaptor-related protein complex AP-1 beta 1
                     subunit; adaptor-related protein complex 1, beta 1
                     subunit"
                     /calculated_mol_wt=104409
     Region          11..534
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          51..75
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(67..68,71,74..75,104..105,108,111..112,139..140,143,
                     146..147,150,178..179,182,185..186,220..221,224,227..228)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          87..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          121..151
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          160..186
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          197..228
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q10567; propagated from
                     UniProtKB/Swiss-Prot (P52303.1)"
     Region          392..416
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          428..457
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          464..494
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          505..541
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          592..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52303.1)"
     Region          729..829
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          838..948
                     /region_name="B2-adapt-app_C"
                     /note="Beta2-adaptin appendage, C-terminal sub-domain;
                     smart01020"
                     /db_xref="CDD:198088"
     CDS             1..949
                     /gene="Ap1b1"
                     /gene_synonym="Adtb1"
                     /coded_by="NM_001308298.1:228..3077"
                     /db_xref="GeneID:29663"
                     /db_xref="RGD:2064"
ORIGIN      
        1 mtdskyfttt kkgeifelka elnsdkkekk keavkkvias mtvgkdvsal fpdvvncmqt
       61 dnlelkklvy lylmnyaksq pdmaimavnt fvkdcedpnp liralavrtm gcirvdkite
      121 ylceplrkcl kdedpyvrkt aavcvaklhd inaqlvedqg fldtlkdlis dsnpmvvana
      181 vaalseiaes hpssnlldln pqsinkllta lnectewgqi fildclanym pkddreaqsi
      241 cervtprlsh ansavvlsav kvlmkfmeml skdldyyatl lkklapplvt llsaepelqy
      301 valrninliv qkrpeilkhe mkvffvkynd piyvklekld imirlasqan iaqvlaelke
      361 yatevdvdfv rkavraigrc aikveqsaer cvstlldliq tkvnyvvqea ivvikdifrk
      421 ypnkyesvia tlcenldsld epearaamiw ivgeyaerid nadellesfl dgfhdestqv
      481 qlqlltaivk lflkkptetq elvqqvlsla tqdsdnpdlr drgyiywrll stdpvaakev
      541 vlaekplise etdlieptll delicyigtl asvyhkppna fveggrgvvh kslpprtass
      601 estespeaap agapasdqpd vipaqgdllg dllnldlgpp vsgpplaass vqmgavdllg
      661 ggldslmgde pegigdsnfg appasvaaaa parlgapvss glsdlfdlts gvgtlsgsyv
      721 apkavwlpam kakgleisgt ftrqvgsism dlqltnkalq vmtdfaiqfn rnsfglapaa
      781 plqvhaplsp nqtveislpl ntvgsvmkme plnnlqvavk nnidvfyfst lyplhvlfve
      841 dgkmdrqmfl atwkdipnen eaqfqirdcp lnteaasskl qssniftvak rtvegqdmly
      901 qslkltngiw vlaelriqpg npsftlslkc rapevsqhvy qayetilkn
//
LOCUS       NP_001296228             218 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001296228
VERSION     NP_001296228.1
DBSOURCE    REFSEQ: accession NM_001309299.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   O'Donnell,B.M., Mackie,T.D., Subramanya,A.R. and Brodsky,J.L.
  TITLE     Endoplasmic reticulum-associated degradation of the renal potassium
            channel, ROMK, leads to type II Bartter syndrome
  JOURNAL   J Biol Chem 292 (31), 12813-12827 (2017)
   PUBMED   28630040
  REMARK    GeneRIF: Data suggest underlying pathology for some patients with
            type II Bartter syndrome is linked to stability of ROMK1 in ERAD
            pathway; using a yeast expression system, cells can be rescued by
            wild-type (rat) ROMK1 but not by ROMK1 containing any one of four
            mutations found in (human) type II Bartter syndrome; mutant ROMKs
            are significantly less stable than wild-type ROMK. (ERAD =
            endoplasmic reticulum-associated degradation)
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Araujo,M., Welch,W.J., Zhou,X., Sullivan,K., Walsh,S., Pasternak,A.
            and Wilcox,C.S.
  TITLE     Inhibition of ROMK blocks macula densa tubuloglomerular feedback
            yet causes renal vasoconstriction in anesthetized rats
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F1120-F1127 (2017)
   PUBMED   28228405
  REMARK    GeneRIF: Blockade of ROMK or Na(+)-K(+)-2Cl(-) transport inhibits
            tubuloglomerular feedback yet increases renal vascular resistance.
            The renal vasoconstriction was independent of volume depletion,
            blood pressure, TGF, or proximal tubule hydrostatic pressure.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Smoot,B., Kober,K.M., Paul,S.M., Levine,J.D., Abrams,G.,
            Mastick,J., Topp,K., Conley,Y.P. and Miaskowski,C.A.
  TITLE     Potassium Channel Candidate Genes Predict the Development of
            Secondary Lymphedema Following Breast Cancer Surgery
  JOURNAL   Nurs Res 66 (2), 85-94 (2017)
   PUBMED   28252570
  REMARK    GeneRIF: These preliminary findings suggest that K channel genes
            play a role in the development of secondary lymphedema
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Bollepalli,M.K., Fowler,P.W., Rapedius,M., Shang,L., Sansom,M.S.,
            Tucker,S.J. and Baukrowitz,T.
  TITLE     State-dependent network connectivity determines gating in a K+
            channel
  JOURNAL   Structure 22 (7), 1037-1046 (2014)
   PUBMED   24980796
  REMARK    GeneRIF: Data indicate that mutations in kir1.1 potassium channel
            preferentially increase pH sensitivity.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Hu,J., Qiu,S., Yang,F., Cao,Z., Li,W. and Wu,Y.
  TITLE     Unique mechanism of the interaction between honey bee toxin TPNQ
            and rKir1.1 potassium channel explored by computational
            simulations: insights into the relative insensitivity of channel
            towards animal toxins
  JOURNAL   PLoS One 8 (7), e67213 (2013)
   PUBMED   23874410
  REMARK    GeneRIF: The TPNQ toxin-rKir1.1 channel complex structure not only
            revealed their unique interaction mechanism, but also elucidate the
            relative insensitivity of rKir1.1 channel towards animal toxins.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Beesley,A.H., Ortega,B. and White,S.J.
  TITLE     Splicing of a retained intron within ROMK K+ channel RNA generates
            a novel set of isoforms in rat kidney
  JOURNAL   Am J Physiol 276 (3), C585-C592 (1999)
   PUBMED   10069985
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Derst,C., Konrad,M., Kockerling,A., Karolyi,L., Deschenes,G.,
            Daut,J., Karschin,A. and Seyberth,H.W.
  TITLE     Mutations in the ROMK gene in antenatal Bartter syndrome are
            associated with impaired K+ channel function
  JOURNAL   Biochem Biophys Res Commun 230 (3), 641-645 (1997)
   PUBMED   9015377
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Boim,M.A., Ho,K., Shuck,M.E., Bienkowski,M.J., Block,J.H.,
            Slightom,J.L., Yang,Y., Brenner,B.M. and Hebert,S.C.
  TITLE     ROMK inwardly rectifying ATP-sensitive K+ channel. II. Cloning and
            distribution of alternative forms
  JOURNAL   Am J Physiol 268 (6 Pt 2), F1132-F1140 (1995)
   PUBMED   7611454
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Zhou,H., Tate,S.S. and Palmer,L.G.
  TITLE     Primary structure and functional properties of an epithelial K
            channel
  JOURNAL   Am J Physiol 266 (3 Pt 1), C809-C824 (1994)
   PUBMED   8166245
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Ho,K., Nichols,C.G., Lederer,W.J., Lytton,J., Vassilev,P.M.,
            Kanazirska,M.V. and Hebert,S.C.
  TITLE     Cloning and expression of an inwardly rectifying ATP-regulated
            potassium channel
  JOURNAL   Nature 362 (6415), 31-38 (1993)
   PUBMED   7680431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            Transcript Variant: This variant (4, also known as ROMK3.1)
            contains three alternate exons in the 5' UTR, lacks a portion of
            the 5' coding region, and initiates translation at a downstream
            start codon, compared to variant 1. It encodes isoform 3 which has
            a shorter N-terminus compared to isoform 1. Variants 3, 4 and 5
            encode the same protein (isoform 3).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF081367.1, SRR26643287.19735.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..218
                     /product="ATP-sensitive inward rectifier potassium channel
                     1 isoform 3"
                     /note="K+ channel protein; ATP-sensitive inward rectifier
                     potassium channel 1; ATP-regulated potassium channel
                     ROM-K; potassium channel, inwardly rectifying subfamily J
                     member 1; inward rectifier K(+) channel Kir1.1"
                     /calculated_mol_wt=24513
     Region          19..191
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..218
                     /gene="Kcnj1"
                     /gene_synonym="KAB-1; Kcnj; Kcnj1_v1; Kcnj1_v3; kir1.1;
                     ROMK1; ROMK2; ROMK3"
                     /coded_by="NM_001309299.1:598..1254"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:24521"
                     /db_xref="RGD:2957"
ORIGIN      
        1 mcgailakis rpkkraktit fsknaviskr ggklcllirv anlrksllig shiygkllkt
       61 titpegetii ldqtninfvv dagnenlffi spltiyhiid hnspffhmaa etlsqqdfel
      121 vvfldgtves tsatcqvrts yvpeevlwgy rfvpivsktk egkyrvdfhn fgktvevetp
      181 hcamclynek dararmkrgy dnpnfvlsev detddtqm
//
LOCUS       NP_062001                506 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-internexin [Rattus norvegicus].
ACCESSION   NP_062001
VERSION     NP_062001.2
DBSOURCE    REFSEQ: accession NM_019128.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Mages,B., Aleithe,S., Altmann,S., Blietz,A., Nitzsche,B.,
            Barthel,H., Horn,A.K.E., Hobusch,C., Hartig,W., Krueger,M. and
            Michalski,D.
  TITLE     Impaired Neurofilament Integrity and Neuronal Morphology in
            Different Models of Focal Cerebral Ischemia and Human Stroke Tissue
  JOURNAL   Front Cell Neurosci 12, 161 (2018)
   PUBMED   29967576
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yuan,A., Sershen,H., Veeranna, Basavarajappa,B.S., Kumar,A.,
            Hashim,A., Berg,M., Lee,J.H., Sato,Y., Rao,M.V., Mohan,P.S.,
            Dyakin,V., Julien,J.P., Lee,V.M. and Nixon,R.A.
  TITLE     Neurofilament subunits are integral components of synapses and
            modulate neurotransmission and behavior in vivo
  JOURNAL   Mol Psychiatry 20 (8), 986-994 (2015)
   PUBMED   25869803
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Karpova,A., Mikhaylova,M., Bera,S., Bar,J., Reddy,P.P.,
            Behnisch,T., Rankovic,V., Spilker,C., Bethge,P., Sahin,J.,
            Kaushik,R., Zuschratter,W., Kahne,T., Naumann,M., Gundelfinger,E.D.
            and Kreutz,M.R.
  TITLE     Encoding and transducing the synaptic or extrasynaptic origin of
            NMDA receptor signals to the nucleus
  JOURNAL   Cell 152 (5), 1119-1133 (2013)
   PUBMED   23452857
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Faussone-Pellegrini,M.S., Matini,P. and DeFelici,M.
  TITLE     The cytoskeleton of the myenteric neurons during murine embryonic
            life
  JOURNAL   Anat Embryol (Berl) 199 (5), 459-469 (1999)
   PUBMED   10221457
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Athlan,E.S. and Mushynski,W.E.
  TITLE     Heterodimeric associations between neuronal intermediate filament
            proteins
  JOURNAL   J Biol Chem 272 (49), 31073-31078 (1997)
   PUBMED   9388258
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Suzuki,T., Mitake,S., Okumura-Noji,K., Shimizu,H., Tada,T. and
            Fujii,T.
  TITLE     Excitable membranes and synaptic transmission: postsynaptic
            mechanisms. Localization of alpha-internexin in the postsynaptic
            density of the rat brain
  JOURNAL   Brain Res 765 (1), 74-80 (1997)
   PUBMED   9310396
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Ching,G.Y. and Liem,R.K.
  TITLE     Structure of the gene for the neuronal intermediate filament
            protein alpha-internexin and functional analysis of its promoter
  JOURNAL   J Biol Chem 266 (29), 19459-19468 (1991)
   PUBMED   1717465
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Fliegner,K.H., Ching,G.Y. and Liem,R.K.
  TITLE     The predicted amino acid sequence of alpha-internexin is that of a
            novel neuronal intermediate filament protein
  JOURNAL   EMBO J 9 (3), 749-755 (1990)
   PUBMED   2311576
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 1, 2015 this sequence version replaced NP_062001.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.8416.1,
                                           SRR26643288.7480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..506
                     /product="alpha-internexin"
                     /calculated_mol_wt=56127
     Region          1..87
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Region          10..92
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46660; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     Region          88..129
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Region          93..406
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          130..142
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Region          143..238
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46660; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     Region          239..262
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Region          263..408
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23565.2)"
     Site            290
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q16352; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16352; propagated from
                     UniProtKB/Swiss-Prot (P23565.2)"
     CDS             1..506
                     /gene="Ina"
                     /gene_synonym="alpha-Inx; Inexa; Intlaa; Nf66"
                     /coded_by="NM_019128.5:75..1595"
                     /db_xref="GeneID:24503"
                     /db_xref="RGD:2911"
ORIGIN      
        1 msfgsehylc sassyrkvfg dgsrlsarls gpggsgsfrs qslsrsnvas taacssassl
       61 glglayrrlp asdgldlsqa aartneykii rtnekeqlqg lndrfavfie kvhqletqnr
      121 aleaelaalr qrhaepsrvg elfqrelrel raqleeassa raqallerdg laeevqrlra
      181 rceeesrgre gaeralkaqq rdvdgatlar ldlekkvesl ldelafvrqv hdeevaella
      241 tlqassqaaa evdvavakpd ltsalreira qyeslaaknl qsaeewyksk fanlneqaar
      301 steairasre eiheyrrqlq artieieglr ganeslerqi leleerhsae vagyqdsigq
      361 lesdlrntks emarhlreyq dllnvkmald ieiaayrkll egeetrfsts glsisglnpl
      421 pnpsyllppr ilssttskvs saglslkkee eeeeeeeeeg askevtkkts kvgesfeetl
      481 eetvvstkkt ekstieeitt ssnqkm
//
LOCUS       NP_001258022             384 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001258022
VERSION     NP_001258022.1
DBSOURCE    REFSEQ: accession NM_001271093.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1, CB585874.1 and CB713901.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY217030.1, SRR26643289.42060.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..384
                     /product="protein NDRG4 isoform 3"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=41938
     Region          40..322
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..384
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_001271093.1:116..1270"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 maglqelrfp eekpllrgqd ateldnpdaf lsvvdtdwke hdietpygll hvvirgspkg
       61 nrpailtyhd vglnhklcfn tlfnledmqe itkhfvvchv dapgqqvgas qfpqgyqfps
      121 meqlatmlps vvqhfgfkyv igigvgagay vlakfalifp dlveglvlmn idpngkgwid
      181 waatklsglt stlpdtvlsh lfsqeelvnn telvqsyrqq issvvnqanl qlfwnmynsr
      241 rdldinrpgt vpnaktlrcp vmlvvgdnap aedgvvecns kldpttttfl kmadsgglpq
      301 vtqpgkltea fkyflqgmgy iahlkdrrls ggavpsasmt rlarsrtasl tsassvdgsr
      361 pqpcthsdss egmgqvnhtm evsc
//
LOCUS       NP_598248                409 aa            linear   ROD 27-APR-2025
DEFINITION  Z-DNA-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_598248 XP_001054526 XP_342595
VERSION     NP_598248.1
DBSOURCE    REFSEQ: accession NM_133564.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Shi,K., Wang,X., Ke,Z. and Li,J.
  TITLE     The role of ZBP1 in eccentric exercise-induced skeletal muscle
            necroptosis
  JOURNAL   J Muscle Res Cell Motil 44 (4), 311-323 (2023)
   PUBMED   37889396
  REMARK    GeneRIF: The role of ZBP1 in eccentric exercise-induced skeletal
            muscle necroptosis.
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Guo,H., Chen,R., Li,P., Yang,Q. and He,Y.
  TITLE     ZBP1 mediates the progression of Alzheimer's disease via pyroptosis
            by regulating IRF3
  JOURNAL   Mol Cell Biochem 478 (12), 2849-2860 (2023)
   PUBMED   36964897
  REMARK    GeneRIF: ZBP1 mediates the progression of Alzheimer's disease via
            pyroptosis by regulating IRF3.
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Qiannan-Di, Qianqian-Jiang, Jiahui-Sun, Haowei-Fu and Qian-Xu.
  TITLE     LncRNA PVT1 mediates the progression of liver necroptosis via ZBP1
            promoter methylation under nonylphenol exposure
  JOURNAL   Sci Total Environ 844, 157185 (2022)
   PUBMED   35803419
  REMARK    GeneRIF: LncRNA PVT1 mediates the progression of liver necroptosis
            via ZBP1 promoter methylation under nonylphenol exposure.
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Urbanska,A.S., Janusz-Kaminska,A., Switon,K., Hawthorne,A.L.,
            Perycz,M., Urbanska,M., Bassell,G.J. and Jaworski,J.
  TITLE     ZBP1 phosphorylation at serine 181 regulates its dendritic
            transport and the development of dendritic trees of hippocampal
            neurons
  JOURNAL   Sci Rep 7 (1), 1876 (2017)
   PUBMED   28500298
  REMARK    GeneRIF: Ser181 ZBP1 phosphorylation was essential for the proper
            dendritic branching of hippocampal neurons that were cultured in
            vitro and for the proper ZBP1 dendritic distribution and motility.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Kim,H.H., Lee,S.J., Gardiner,A.S., Perrone-Bizzozero,N.I. and
            Yoo,S.
  TITLE     Different motif requirements for the localization zipcode element
            of beta-actin mRNA binding by HuD and ZBP1
  JOURNAL   Nucleic Acids Res 43 (15), 7432-7446 (2015)
   PUBMED   26152301
  REMARK    GeneRIF: Both ZBP1 and HuD bind the zipcode element in rat
            beta-actin mRNA's 3' UTR. Differences between HuD and ZBP1 were
            observed in their binding preference to the element.
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Burckstummer,T., Baumann,C., Bluml,S., Dixit,E., Durnberger,G.,
            Jahn,H., Planyavsky,M., Bilban,M., Colinge,J., Bennett,K.L. and
            Superti-Furga,G.
  TITLE     An orthogonal proteomic-genomic screen identifies AIM2 as a
            cytoplasmic DNA sensor for the inflammasome
  JOURNAL   Nat Immunol 10 (3), 266-272 (2009)
   PUBMED   19158679
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Ha,S.C., Kim,D., Hwang,H.Y., Rich,A., Kim,Y.G. and Kim,K.K.
  TITLE     The crystal structure of the second Z-DNA binding domain of human
            DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to
            Z-DNA
  JOURNAL   Proc Natl Acad Sci U S A 105 (52), 20671-20676 (2008)
   PUBMED   19095800
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Takaoka,A., Wang,Z., Choi,M.K., Yanai,H., Negishi,H., Ban,T.,
            Lu,Y., Miyagishi,M., Kodama,T., Honda,K., Ohba,Y. and Taniguchi,T.
  TITLE     DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of
            innate immune response
  JOURNAL   Nature 448 (7152), 501-505 (2007)
   PUBMED   17618271
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Rothenburg,S., Schwartz,T., Koch-Nolte,F. and Haag,F.
  TITLE     Complex regulation of the human gene for the Z-DNA binding protein
            DLM-1
  JOURNAL   Nucleic Acids Res 30 (4), 993-1000 (2002)
   PUBMED   11842111
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Schwartz,T., Behlke,J., Lowenhaupt,K., Heinemann,U. and Rich,A.
  TITLE     Structure of the DLM-1-Z-DNA complex reveals a conserved family of
            Z-DNA-binding proteins
  JOURNAL   Nat Struct Biol 8 (9), 761-765 (2001)
   PUBMED   11524677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Feb 13, 2013 this sequence version replaced
            XP_342595.1, XP_001054526.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ302054.1, SRR26643288.17096.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..409
                     /product="Z-DNA-binding protein 1"
                     /note="tumor stroma and activated macrophage protein
                     DLM-1"
                     /calculated_mol_wt=43757
     Region          10..68
                     /region_name="z-alpha"
                     /note="Adenosine deaminase z-alpha domain; cl02659"
                     /db_xref="CDD:295419"
     Region          59..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDA5.1)"
     Region          85..149
                     /region_name="z-alpha"
                     /note="Adenosine deaminase z-alpha domain; cl02659"
                     /db_xref="CDD:295419"
     Region          183..207
                     /region_name="RIP homotypic interaction motif (RHIM) 1.
                     /evidence=ECO:0000250|UniProtKB:Q9QY24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDA5.1)"
     Region          184..204
                     /region_name="RHIM"
                     /note="RIP homotypic interaction motif; pfam12721"
                     /db_xref="CDD:463679"
     Region          241..265
                     /region_name="RIP homotypic interaction motif (RHIM) 2.
                     /evidence=ECO:0000250|UniProtKB:Q9QY24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDA5.1)"
     Region          269..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDA5.1)"
     Region          323..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VDA5.1)"
     CDS             1..409
                     /gene="Zbp1"
                     /gene_synonym="Dlm1"
                     /coded_by="NM_133564.1:1..1230"
                     /db_xref="GeneID:171091"
                     /db_xref="RGD:619956"
ORIGIN      
        1 maeasvdlgt gdnleqkilq vlsdagspvq idqllkklqv pkkilnqvly rlkkegrvss
       61 papatwslgg dgasgdgape ipedsaaqps leerilrfle tkgpqralhi akalgmttak
      121 evnpilysmr nkhlltvsdt qmwtiyrssq egqeracsgv gqespaviyq qnpinmicqq
      181 gpnslisisn skaiqighgn vmsrqticgd pgpgtphhap lpvledaaaq dtppgthgaq
      241 lihlnksmlr rvqlghgnem nlerdpvehp ifsfsssppe stttadpeta fnmqtpepgp
      301 hpeggttqiv hiksclledt tvgnnnkmti hrrskggake sadsqelked tgasseatpp
      361 rsclhtpsds tlltseltam algdgspqit esmlredevq aaetcqtqd
//
LOCUS       NP_001094199             569 aa            linear   ROD 27-APR-2025
DEFINITION  AP-4 complex accessory subunit tepsin [Rattus norvegicus].
ACCESSION   NP_001094199 XP_001074705 XP_001081796 XP_001081797 XP_340947
VERSION     NP_001094199.1
DBSOURCE    REFSEQ: accession NM_001100729.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Frazier,M.N., Davies,A.K., Voehler,M., Kendall,A.K., Borner,G.H.,
            Chazin,W.J., Robinson,M.S. and Jackson,L.P.
  TITLE     Molecular Basis for the Interaction Between AP4 beta4 and its
            Accessory Protein, Tepsin
  JOURNAL   Traffic 17 (4), 400-415 (2016)
   PUBMED   26756312
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Mattera,R., Guardia,C.M., Sidhu,S.S. and Bonifacino,J.S.
  TITLE     Bivalent Motif-Ear Interactions Mediate the Association of the
            Accessory Protein Tepsin with the AP-4 Adaptor Complex
  JOURNAL   J Biol Chem 290 (52), 30736-30749 (2015)
   PUBMED   26542808
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Borner,G.H., Antrobus,R., Hirst,J., Bhumbra,G.S., Kozik,P.,
            Jackson,L.P., Sahlender,D.A. and Robinson,M.S.
  TITLE     Multivariate proteomic profiling identifies novel accessory
            proteins of coated vesicles
  JOURNAL   J Cell Biol 197 (1), 141-160 (2012)
   PUBMED   22472443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1 and BC089956.1.
            
            On or before Feb 16, 2013 this sequence version replaced
            XP_340947.3, XP_001074705.1, XP_001081796.1, XP_001081797.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.272552.1,
                                           SRR26360176.302129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..569
                     /product="AP-4 complex accessory subunit tepsin"
                     /note="tetra-epsin; ENTH domain-containing protein 2; ENTH
                     domain containing 2"
                     /calculated_mol_wt=60150
     Region          16..134
                     /region_name="ENTH_like_Tepsin"
                     /note="Epsin N-Terminal Homology (ENTH)-like domain of
                     AP-4 complex accessory subunit Tepsin and similar domains;
                     cd03572"
                     /db_xref="CDD:340773"
     Site            order(21,25..26,60,64,68)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:340773"
     Region          196..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8Y7.1)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (G3V8Y7.1)"
     Region          467..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8Y7.1)"
     Region          525..535
                     /region_name="Interaction with AP4B1.
                     /evidence=ECO:0000250|UniProtKB:Q96N21"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8Y7.1)"
     Region          559..569
                     /region_name="Interaction with AP4E1.
                     /evidence=ECO:0000250|UniProtKB:Q96N21"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8Y7.1)"
     CDS             1..569
                     /gene="Tepsin"
                     /gene_synonym="Enthd2; RGD1307410"
                     /coded_by="NM_001100729.1:69..1778"
                     /db_xref="GeneID:360673"
                     /db_xref="RGD:1307410"
ORIGIN      
        1 maavpplrdr lsflhrlpil lkgtsdddip cpgylfeeia kisheslgss qclleyllnr
       61 ldsssghvkl kvlkillylc shgsssfmli lrrnsaliqe atafagppdp lhgnslyqkv
      121 raaaqdlgst lfsdalpqpp sqppqilppa gmgaqarphs alqgfgytke ssrtgsaget
      181 flstiqraae vvvnavrpgp dnpctkgplp hgdayqpavt psashthpnp gnllpaaiqg
      241 travkhqpgq agggwdemds spssqnssct snlsrasdsv srsgsdshsg asrepgdlae
      301 raegmapndc qqelnlvrtv tqgprvflsr eetqhfikec gllnceavle lllqqlvgts
      361 eceqmralca iasfgsadll pqehilllcr qqlqelgags pgpvtnkatk ilrhleascg
      421 qqfptlrpca qpnsaaavvg padlltspvp ppgsqvflqp lsstavvprs pvptpspdtl
      481 ppalqdpgel rtqlvcssep gtgseqrlen tdtpkdsssp cpwspnslfa gmelvactrl
      541 pcpsfqadlq kvtteppvse psafaflnm
//
LOCUS       NP_001071119             385 aa            linear   ROD 27-APR-2025
DEFINITION  ELAV-like protein 4 [Rattus norvegicus].
ACCESSION   NP_001071119 XP_001062986 XP_001063055 XP_001063104 XP_001063163
            XP_001063217 XP_001063277 XP_001063323 XP_001063372 XP_001063429
            XP_006238654
VERSION     NP_001071119.2
DBSOURCE    REFSEQ: accession NM_001077651.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Zheng,Z., Chen,B., Jin,Z., Gao,M., Tang,C., Mao,Y., Qu,Y. and
            Liu,Y.
  TITLE     Downregulation of P2Y2 and HuD during the development of the
            enteric nervous system in fetal rats with anorectal malformations
  JOURNAL   Mol Med Rep 20 (2), 1297-1305 (2019)
   PUBMED   31173231
  REMARK    GeneRIF: downregulation of P2Y2 and HuD may partly be related to
            the development of the enteric nervous system in anorectal
            malformations embryos.
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Gomes,C., Lee,S.J., Gardiner,A.S., Smith,T., Sahoo,P.K., Patel,P.,
            Thames,E., Rodriguez,R., Taylor,R., Yoo,S., Heise,T., Kar,A.N.,
            Perrone-Bizzozero,N. and Twiss,J.L.
  TITLE     Axonal localization of neuritin/CPG15 mRNA is limited by
            competition for HuD binding
  JOURNAL   J Cell Sci 130 (21), 3650-3662 (2017)
   PUBMED   28871047
  REMARK    GeneRIF: The data indicate that endogenous Nrn1 and Gap43 mRNAs
            compete for binding to HuD for their axonal localization and
            activity of the Nrn1 3'UTR.
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Kong,M., Wu,Y. and Liu,Y.
  TITLE     The impact of HuD protein on the intestinal nervous system in the
            terminal rectum of animal models of congenital anorectal
            malformation
  JOURNAL   Mol Med Rep 16 (4), 4797-4802 (2017)
   PUBMED   28849006
  REMARK    GeneRIF: the HuD protein is abnormally expressed in the nerve
            plexuses of the intestinal wall of the terminal rectum of ARM
            embryonic rats, which suggests that HuD may participate in the
            development and maturation of the ENS in ARM embryonic rats.
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Kim,H.H., Lee,S.J., Gardiner,A.S., Perrone-Bizzozero,N.I. and
            Yoo,S.
  TITLE     Different motif requirements for the localization zipcode element
            of beta-actin mRNA binding by HuD and ZBP1
  JOURNAL   Nucleic Acids Res 43 (15), 7432-7446 (2015)
   PUBMED   26152301
  REMARK    GeneRIF: Both ZBP1 and HuD bind the zipcode element in rat
            beta-actin mRNA's 3' UTR. Differences between HuD and ZBP1 were
            observed in their binding preference to the element.
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Sosanya,N.M., Cacheaux,L.P., Workman,E.R., Niere,F.,
            Perrone-Bizzozero,N.I. and Raab-Graham,K.F.
  TITLE     Mammalian Target of Rapamycin (mTOR) Tagging Promotes Dendritic
            Branch Variability through the Capture of Ca2+/Calmodulin-dependent
            Protein Kinase II alpha (CaMKIIalpha) mRNAs by the RNA-binding
            Protein HuD
  JOURNAL   J Biol Chem 290 (26), 16357-16371 (2015)
   PUBMED   25944900
  REMARK    GeneRIF: mTOR inhibition reduces HuD binding and promotes
            deadenylation of CaMKIIalpha mRNA.
REFERENCE   6  (residues 1 to 385)
  AUTHORS   King,P.H.
  TITLE     RNA-binding analyses of HuC and HuD with the VEGF and c-myc
            3'-untranslated regions using a novel ELISA-based assay
  JOURNAL   Nucleic Acids Res 28 (7), E20 (2000)
   PUBMED   10710437
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Aranda-Abreu,G.E., Behar,L., Chung,S., Furneaux,H. and Ginzburg,I.
  TITLE     Embryonic lethal abnormal vision-like RNA-binding proteins regulate
            neurite outgrowth and tau expression in PC12 cells
  JOURNAL   J Neurosci 19 (16), 6907-6917 (1999)
   PUBMED   10436048
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Clayton,G.H., Perez,G.M., Smith,R.L. and Owens,G.C.
  TITLE     Expression of mRNA for the elav-like neural-specific RNA binding
            protein, HuD, during nervous system development
  JOURNAL   Brain Res Dev Brain Res 109 (2), 271-280 (1998)
   PUBMED   9729424
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Dobashi,Y., Shoji,M., Wakata,Y. and Kameya,T.
  TITLE     Expression of HuD protein is essential for initial phase of
            neuronal differentiation in rat pheochromocytoma PC12 cells
  JOURNAL   Biochem Biophys Res Commun 244 (1), 226-229 (1998)
   PUBMED   9514914
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Steller,U., Kohls,S., Muller,B., Soller,R., Muller,R., Schlender,J.
            and Blohm,D.H.
  TITLE     The RNA binding protein HuD: rat cDNA and analysis of the
            alternative spliced mRNA in neuronal differentiating cell lines P19
            and PC12
  JOURNAL   Brain Res Mol Brain Res 35 (1-2), 285-296 (1996)
   PUBMED   8717365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1 and BC158558.1.
            
            On or before Jun 25, 2015 this sequence version replaced
            XP_006238654.1, NP_001071119.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.925747.1, BC158558.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..385
                     /product="ELAV-like protein 4"
                     /note="hu-antigen D; paraneoplastic encephalomyelitis
                     antigen HuD; ELAV (embryonic lethal, abnormal vision,
                     Drosophila)-like 4 (Hu antigen D); ELAV like
                     neuron-specific RNA binding protein 4"
                     /calculated_mol_wt=42237
     Region          12..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O09032.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61701; propagated from
                     UniProtKB/Swiss-Prot (O09032.2)"
     Region          48..384
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O09032.2)"
     Site            248
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by CARM1, alternate.
                     /evidence=ECO:0000269|PubMed:16508003;
                     Omega-N-methylarginine, by CARM1, alternate.
                     /evidence=ECO:0000269|PubMed:16508003; propagated from
                     UniProtKB/Swiss-Prot (O09032.2)"
     CDS             1..385
                     /gene="Elavl4"
                     /gene_synonym="HuD"
                     /coded_by="NM_001077651.2:133..1290"
                     /db_xref="GeneID:432358"
                     /db_xref="RGD:1560027"
ORIGIN      
        1 mewnglkmii stmepqvsng ptsntsngps snnrncpspm qtgaatddsk tnlivnylpq
       61 nmtqeefrsl fgsigeiesc klvrdkitgq slgygfvnyi dpkdaekain tlnglrlqtk
      121 tikvsyarps sasirdanly vsglpktmtq keleqlfsqy griitsrilv dqvtgvsrgv
      181 gfirfdkrie aeeaikglng qkpsgatepi tvkfannpsq kssqallsql yqspnrrypg
      241 plhhqaqrfr ldnllnmayg vkrlmsgpvp psacpprfsp itidgmtslv gmnipghtgt
      301 gwcifvynls pdsdesvlwq lfgpfgavnn vkvirdfntn kckgfgfvtm tnydeaamai
      361 aslngyrlgd rvlqvsfktn kahks
//
LOCUS       NP_001257768             298 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group I member 3 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001257768
VERSION     NP_001257768.1
DBSOURCE    REFSEQ: accession NM_001270839.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Yamada,T., Cohen,S.M. and Lake,B.G.
  TITLE     Critical evaluation of the human relevance of the mode of action
            for rodent liver tumor formation by activators of the constitutive
            androstane receptor (CAR)
  JOURNAL   Crit Rev Toxicol 51 (5), 373-394 (2021)
   PUBMED   34264181
  REMARK    GeneRIF: Critical evaluation of the human relevance of the mode of
            action for rodent liver tumor formation by activators of the
            constitutive androstane receptor (CAR).
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Gabbia,D., Pozza,A.D., Albertoni,L., Lazzari,R., Zigiotto,G.,
            Carrara,M., Baldo,V., Baldovin,T., Floreani,A. and Martin,S.
  TITLE     Pregnane X receptor and constitutive androstane receptor modulate
            differently CYP3A-mediated metabolism in early- and late-stage
            cholestasis
  JOURNAL   World J Gastroenterol 23 (42), 7519-7530 (2017)
   PUBMED   29204052
  REMARK    GeneRIF: nuclear expression virtually disappeared in the late stage
            of cholestatic injury, after an initial increase
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Forbes,K.P., Kouranova,E., Tinker,D., Janowski,K., Cortner,D.,
            McCoy,A. and Cui,X.
  TITLE     Creation and Preliminary Characterization of Pregnane X Receptor
            and Constitutive Androstane Receptor Knockout Rats
  JOURNAL   Drug Metab Dispos 45 (10), 1068-1076 (2017)
   PUBMED   28716828
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Fujino,C., Tamura,Y., Tange,S., Nakajima,H., Sanoh,S., Watanabe,Y.,
            Uramaru,N., Kojima,H., Yoshinari,K., Ohta,S. and Kitamura,S.
  TITLE     Metabolism of methiocarb and carbaryl by rat and human livers and
            plasma, and effect on their PXR, CAR and PPARalpha activities
  JOURNAL   J Toxicol Sci 41 (5), 677-691 (2016)
   PUBMED   27665777
  REMARK    GeneRIF: Metabolism of methiocarb and carbaryl does not alter CAR
            activity.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Shao,Y.Y., Huang,J., Ma,Y.R., Han,M., Ma,K., Qin,H.Y., Rao,Z. and
            Wu,X.A.
  TITLE     Serum serotonin reduced the expression of hepatic transporter Mrp2
            and P-gp via regulating nuclear receptor CAR in PI-IBS rats
  JOURNAL   Can J Physiol Pharmacol 93 (8), 633-639 (2015)
   PUBMED   26053941
  REMARK    GeneRIF: Serum 5-HT regulates the expression of Mrp2 and P-gp, and
            the underlying mechanism may be related to the altered expression
            of the nuclear receptor constitutive androstane receptor.
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Numazawa,S., Shindo,S., Maruyama,K., Chibana,F., Kawahara,Y.,
            Ashino,T., Tanaka,S. and Yoshida,T.
  TITLE     Impaired nuclear translocation of CAR in hepatic preneoplastic
            lesions: association with an attenuated CYP2B induction by
            phenobarbital
  JOURNAL   FEBS Lett 579 (17), 3560-3564 (2005)
   PUBMED   15953603
  REMARK    GeneRIF: CAR expressed in the hepatic preneoplastic lesions of rats
            is resistant to nuclear translocation and transactivation of the
            phenobarbital(PB) responsive enhancer module upon PB treatment.
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Yoshinari,K., Kobayashi,K., Moore,R., Kawamoto,T. and Negishi,M.
  TITLE     Identification of the nuclear receptor CAR:HSP90 complex in mouse
            liver and recruitment of protein phosphatase 2A in response to
            phenobarbital
  JOURNAL   FEBS Lett 548 (1-3), 17-20 (2003)
   PUBMED   12885400
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Gonzalez,M.M. and Carlberg,C.
  TITLE     Cross-repression, a functional consequence of the physical
            interaction of non-liganded nuclear receptors and POU domain
            transcription factors
  JOURNAL   J Biol Chem 277 (21), 18501-18509 (2002)
   PUBMED   11891224
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Yoshinari,K., Sueyoshi,T., Moore,R. and Negishi,M.
  TITLE     Nuclear receptor CAR as a regulatory factor for the sexually
            dimorphic induction of CYB2B1 gene by phenobarbital in rat livers
  JOURNAL   Mol Pharmacol 59 (2), 278-284 (2001)
   PUBMED   11160864
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Xie,W., Barwick,J.L., Simon,C.M., Pierce,A.M., Safe,S.,
            Blumberg,B., Guzelian,P.S. and Evans,R.M.
  TITLE     Reciprocal activation of xenobiotic response genes by nuclear
            receptors SXR/PXR and CAR
  JOURNAL   Genes Dev 14 (23), 3014-3023 (2000)
   PUBMED   11114890
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089763.1 and JAXUCZ010000013.1.
            
            Transcript Variant: This variant (4) uses an alternate splice site
            at the 5' end of an exon compared to variant 1, that causes a
            frameshift. The resulting isoform (4) has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB204899.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760400, SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..298
                     /product="nuclear receptor subfamily 1 group I member 3
                     isoform 4"
                     /note="constitutive androstane receptor; strain Fischer
                     nuclear receptor (CAR); nuclear receptor constitutive
                     active receptor"
                     /calculated_mol_wt=33928
     Region          21..92
                     /region_name="NR_DBD_VDR_like"
                     /note="The DNA-binding domain of vitamin D receptors (VDR)
                     like nuclear receptor family is composed of two C4-type
                     zinc fingers; cd07156"
                     /db_xref="CDD:143531"
     Site            order(21,24,38,41,57,63,73,76)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143531"
     Site            order(31..33,39..40,42,46..47,70..71,77,91..92)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143531"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q14994; propagated from
                     UniProtKB/Swiss-Prot (Q9QUS1.1)"
     Site            order(58..59,72,89..90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143531"
     Region          116..>281
                     /region_name="NR_LBD"
                     /note="The ligand binding domain of nuclear receptors, a
                     family of ligand-activated transcription regulators;
                     cl11397"
                     /db_xref="CDD:472173"
     Site            order(171..172,175,178..179,208..209,212..213,216,219,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132726"
     Site            order(180,183,187,192,197..198,200..201,204..205)
                     /site_type="active"
                     /note="coregulator recognition site [active]"
                     /db_xref="CDD:132726"
     CDS             1..298
                     /gene="Nr1i3"
                     /gene_synonym="CAR"
                     /coded_by="NM_001270839.1:150..1046"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:65035"
                     /db_xref="RGD:621400"
ORIGIN      
        1 mtatltletm tseeeygprn cvvcgdratg yhfhaltceg ckgffrrtvs ktigpicpfa
       61 grcevskaqr rhcpacrlqk clnvgmrkdm ilsaealalr rarqarrraq kaslqlsqqq
      121 keliqtllga htrhvgpmfd qfvqfrppay lfshhrpfqp lapvlpllth fadintfmvq
      181 qiikftkdlp lfrsltmedq isllkgaave ilhislnttf clqtqnffcg plcykmedav
      241 hvgfqyefle liihfhktlk rlqlqepeya lmaamalfsp glglpkekrl iscrkrsr
//
LOCUS       NP_599215                261 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, slow skeletal muscle isoform 1 [Rattus norvegicus].
ACCESSION   NP_599215
VERSION     NP_599215.2
DBSOURCE    REFSEQ: accession NM_134388.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Tsika,R.W., Schramm,C., Simmer,G., Fitzsimons,D.P., Moss,R.L. and
            Ji,J.
  TITLE     Overexpression of TEAD-1 in transgenic mouse striated muscles
            produces a slower skeletal muscle contractile phenotype
  JOURNAL   J Biol Chem 283 (52), 36154-36167 (2008)
   PUBMED   18978355
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Pinto,J.R., Parvatiyar,M.S., Jones,M.A., Liang,J. and Potter,J.D.
  TITLE     A troponin T mutation that causes infantile restrictive
            cardiomyopathy increases Ca2+ sensitivity of force development and
            impairs the inhibitory properties of troponin
  JOURNAL   J Biol Chem 283 (4), 2156-2166 (2008)
   PUBMED   18032382
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Kischel,P., Bastide,B., Muller,M., Dubail,F., Offredi,F., Jin,J.P.,
            Mounier,Y. and Martial,J.
  TITLE     Expression and functional properties of four slow skeletal troponin
            T isoforms in rat muscles
  JOURNAL   Am J Physiol Cell Physiol 289 (2), C437-C443 (2005)
   PUBMED   15788488
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Wang,X., Huang,Q.Q., Breckenridge,M.T., Chen,A., Crawford,T.O.,
            Morton,D.H. and Jin,J.P.
  TITLE     Cellular fate of truncated slow skeletal muscle troponin T produced
            by Glu180 nonsense mutation in amish nemaline myopathy
  JOURNAL   J Biol Chem 280 (14), 13241-13249 (2005)
   PUBMED   15665378
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Johnston,J.J., Kelley,R.I., Crawford,T.O., Morton,D.H.,
            Agarwala,R., Koch,T., Schaffer,A.A., Francomano,C.A. and
            Biesecker,L.G.
  TITLE     A novel nemaline myopathy in the Amish caused by a mutation in
            troponin T1
  JOURNAL   Am J Hum Genet 67 (4), 814-821 (2000)
   PUBMED   10952871
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Gahlmann,R., Troutt,A.B., Wade,R.P., Gunning,P. and Kedes,L.
  TITLE     Alternative splicing generates variants in important functional
            domains of human slow skeletal troponin T
  JOURNAL   J Biol Chem 262 (33), 16122-16126 (1987)
   PUBMED   2824479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and AY334079.1.
            
            On Mar 27, 2013 this sequence version replaced NP_599215.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF399874.1, AY334079.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760386, SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..261
                     /product="troponin T, slow skeletal muscle isoform 1"
                     /note="troponin T, slow skeletal muscle; slow skeletal
                     muscle troponin T; troponin T1, skeletal, slow; troponin T
                     type 1 (skeletal, slow)"
                     /calculated_mol_wt=31084
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNB2.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q7TNB2.3)"
     Region          68..204
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Region          108..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TNB2.3)"
     Region          179..>237
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..261
                     /gene="Tnnt1"
                     /gene_synonym="Fang2; sTnT; tnTs"
                     /coded_by="NM_134388.2:57..842"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171409"
                     /db_xref="RGD:621852"
ORIGIN      
        1 msdteeqeye eeqaedeeav eeeapeepep vaereeerpk psrpvvppli ppkipegerv
       61 dfddihrkrm ekdllelqtl idvhfeqrkk eeeelialkd rierrraera eqqrfrteke
      121 rerqaklaee kmrkeeeeak kraeddakkk kvlsnmgahf ggylvkaeqk rgkrqtgrem
      181 klrilserkk plnidymged qlrekaqels ewihqlesek fdlmeklkqq kyeinvlynr
      241 ishaqkfrkg agkgrvggrw k
//
LOCUS       NP_446084                648 aa            linear   ROD 27-APR-2025
DEFINITION  phosphatidylinositol polyphosphate 5-phosphatase type IV [Rattus
            norvegicus].
ACCESSION   NP_446084 XP_002726118 XP_002729191
VERSION     NP_446084.1
DBSOURCE    REFSEQ: accession NM_053632.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Badgandi,H.B., Hwang,S.H., Shimada,I.S., Loriot,E. and
            Mukhopadhyay,S.
  TITLE     Tubby family proteins are adapters for ciliary trafficking of
            integral membrane proteins
  JOURNAL   J Cell Biol 216 (3), 743-760 (2017)
   PUBMED   28154160
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Travaglini,L., Brancati,F., Silhavy,J., Iannicelli,M.,
            Nickerson,E., Elkhartoufi,N., Scott,E., Spencer,E., Gabriel,S.,
            Thomas,S., Ben-Zeev,B., Bertini,E., Boltshauser,E., Chaouch,M.,
            Cilio,M.R., de Jong,M.M., Kayserili,H., Ogur,G., Poretti,A.,
            Signorini,S., Uziel,G., Zaki,M.S., Johnson,C., Attie-Bitach,T.,
            Gleeson,J.G. and Valente,E.M.
  CONSRTM   International JSRD Study Group
  TITLE     Phenotypic spectrum and prevalence of INPP5E mutations in Joubert
            syndrome and related disorders
  JOURNAL   Eur J Hum Genet 21 (10), 1074-1078 (2013)
   PUBMED   23386033
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Bertelli,D.F., Coope,A., Caricilli,A.M., Prada,P.O., Saad,M.J.,
            Velloso,L.A. and Araujo,E.P.
  TITLE     Inhibition of 72 kDa inositol polyphosphate 5-phosphatase E
            improves insulin signal transduction in diet-induced obesity
  JOURNAL   J Endocrinol 217 (2), 131-140 (2013)
   PUBMED   23349329
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Wang,F., Ijuin,T., Itoh,T. and Takenawa,T.
  TITLE     Regulation of IGF-1/PI3K/Akt signalling by the phosphoinositide
            phosphatase pharbin
  JOURNAL   J Biochem 150 (1), 83-93 (2011)
   PUBMED   21436142
  REMARK    GeneRIF: pharbin is an important negative regulator of
            IGF-1/PI3K/Akt signalling and protein synthesis.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Jacoby,M., Cox,J.J., Gayral,S., Hampshire,D.J., Ayub,M.,
            Blockmans,M., Pernot,E., Kisseleva,M.V., Compere,P.,
            Schiffmann,S.N., Gergely,F., Riley,J.H., Perez-Morga,D., Woods,C.G.
            and Schurmans,S.
  TITLE     INPP5E mutations cause primary cilium signaling defects, ciliary
            instability and ciliopathies in human and mouse
  JOURNAL   Nat Genet 41 (9), 1027-1031 (2009)
   PUBMED   19668215
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Kong,A.M., Speed,C.J., O'Malley,C.J., Layton,M.J., Meehan,T.,
            Loveland,K.L., Cheema,S., Ooms,L.M. and Mitchell,C.A.
  TITLE     Cloning and characterization of a 72-kDa inositol-polyphosphate
            5-phosphatase localized to the Golgi network
  JOURNAL   J Biol Chem 275 (31), 24052-24064 (2000)
   PUBMED   10806194
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Asano,T., Mochizuki,Y., Matsumoto,K., Takenawa,T. and Endo,T.
  TITLE     Pharbin, a novel inositol polyphosphate 5-phosphatase, induces
            dendritic appearances in fibroblasts
  JOURNAL   Biochem Biophys Res Commun 261 (1), 188-195 (1999)
   PUBMED   10405344
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Feb 9, 2013 this sequence version replaced
            XP_002729191.1, XP_002726118.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB026288.1, SRR26360190.1680612.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..648
                     /product="phosphatidylinositol polyphosphate 5-phosphatase
                     type IV"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="72 kDa inositol polyphosphate 5-phosphatase;
                     5-phosphatase that induces arborization;
                     phosphatidylinositol-4,5-bisphosphate 5-phosphatase;
                     pharbin; phosphatidylinositol-3,4,5-trisphosphate
                     5-phosphatase"
                     /calculated_mol_wt=71909
     mat_peptide     1..645
                     /product="Phosphatidylinositol polyphosphate 5-phosphatase
                     type IV. /evidence=ECO:0000250|UniProtKB:Q9NRR6.
                     /id=PRO_0000209749"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR1.3)"
                     /calculated_mol_wt=71753
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Region          59..243
                     /region_name="4 X 4 AA repeats of P-X-X-P"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Region          99..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NRR6; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JII1; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JII1; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR1.3)"
     Region          299..597
                     /region_name="INPP5c_INPP5E-like"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Inositol polyphosphate-5-phosphatase E
                     and related proteins; cd09095"
                     /db_xref="CDD:197329"
     Site            order(311,313,344,407..408,428,431..432,481,483,485,
                     538..539,554,560,587..588)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197329"
     Site            order(311,344,428,481,483,560,587..588)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197329"
     Site            order(344,407..408,428,431..432,485,538..539,554,587)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197329"
     Site            order(344,587)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197329"
     Site            order(428,483,588)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197329"
     Site            645
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:Q9NRR6; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR1.3)"
     CDS             1..648
                     /gene="Inpp5e"
                     /coded_by="NM_053632.1:591..2537"
                     /db_xref="GeneID:114089"
                     /db_xref="RGD:620478"
ORIGIN      
        1 mpsksaclrh teapgqlegr mlqgqlsnpe kkliptsasl paadsqssqt nsmpplsmpa
       61 kpsnqnlqak anlitpqppi rpklertlsl ddkgwrrrrf rgsqedltvq ngaspcrgsl
      121 qdsvaqspay srplpclsts lqeipkprra tgseggspsl wsdclsgmis tsldllhrea
      181 asggphsrla slrathtppa mdlniasssl rtankvdpeh tdyklrmqnr lvrahsnlgp
      241 srprsplagd dhsihsarss fsllapirtk dirsrsyleg sllasgallg adelaryfpd
      301 rnmalfvatw nmqgqkelpa sldefllpte adytqdlyvi gvqegcsdrr ewetrlqetl
      361 gpqyvllssa ahgvlymslf irrdliwfcs eveystvttr ivsqiktkga lgvsftffgt
      421 sflfitshft sgdgkvaerl ldynrtiqal alprnvpdtn pyrssagdvt trfdevfwfg
      481 dfnfrlsggr vaveaflkqd pevdvlallq hdqltremkk gsifkgfeea eihflpsykf
      541 digkdtydst skqrtpsytd rvlyksrhkg dicpmkyssc pgiktsdhrp vyglfrvkvr
      601 pgrdniplaa gkfdrelyli gikrriskei qrqealksqs ssavctvs
//
LOCUS       NP_036747                461 aa            linear   ROD 27-APR-2025
DEFINITION  ornithine decarboxylase [Rattus norvegicus].
ACCESSION   NP_036747 XP_006239968
VERSION     NP_036747.1
DBSOURCE    REFSEQ: accession NM_012615.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Liu,W., Wu,Y.H., Zhang,L., Liu,X.Y., Wang,Y., Xue,B., Liu,B.,
            Cai,Y., Zhang,B. and Ji,Y.
  TITLE     Effects of lentivirus-mediated ornithine decarboxylase gene on the
            proliferation and apoptosis of fibroblast-like synoviocytes in rats
            with arthritis
  JOURNAL   Life Sci 194, 224-230 (2018)
   PUBMED   28986097
  REMARK    GeneRIF: The results indicated that overexpression of ODC gene
            promotes the proliferation while suppressing apoptosis of
            fibroblast-like synoviocytes in rats with rheumatoid arthritis.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Ramos-Molina,B., Lambertos,A., Lopez-Contreras,A.J., Kasprzak,J.M.,
            Czerwoniec,A., Bujnicki,J.M., Cremades,A. and Penafiel,R.
  TITLE     Structural and degradative aspects of ornithine decarboxylase
            antizyme inhibitor 2
  JOURNAL   FEBS Open Bio 4, 510-521 (2014)
   PUBMED   24967154
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Zhang,H., Xue,G., Zhang,W., Wang,L., Li,H., Zhang,L., Lu,F.,
            Bai,S., Lin,Y., Lou,Y., Xu,C. and Zhao,Y.
  TITLE     Akt and Erk1/2 activate the ornithine decarboxylase/polyamine
            system in cardioprotective ischemic preconditioning in rats: the
            role of mitochondrial permeability transition pores
  JOURNAL   Mol Cell Biochem 390 (1-2), 133-142 (2014)
   PUBMED   24464033
  REMARK    GeneRIF: These results suggest that IPC upregulates the Ornithine
            decarboxylase/polyamine system and mediates preconditioning
            cardioprotection.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Passariello,C.L., Gottardi,D., Cetrullo,S., Zini,M., Campana,G.,
            Tantini,B., Pignatti,C., Flamigni,F., Guarnieri,C., Caldarera,C.M.
            and Stefanelli,C.
  TITLE     Evidence that AMP-activated protein kinase can negatively modulate
            ornithine decarboxylase activity in cardiac myoblasts
  JOURNAL   Biochim Biophys Acta 1823 (4), 800-807 (2012)
   PUBMED   22230191
  REMARK    GeneRIF: The modulation of ODC activity by AMPK represents a
            mechanism that may contribute to control cell growth processes.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Wang,J.Y., Viar,M.J., McCormack,S.A. and Johnson,L.R.
  TITLE     Effect of putrescine on S-adenosylmethionine decarboxylase in a
            small intestinal crypt cell line
  JOURNAL   Am J Physiol 263 (4 Pt 1), G494-G501 (1992)
   PUBMED   1415709
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Van Steeg,H., Van Oostrom,C.T., Hodemaekers,H.M., Peters,L. and
            Thomas,A.A.
  TITLE     The translation in vitro of rat ornithine decarboxylase mRNA is
            blocked by its 5' untranslated region in a polyamine-independent
            way
  JOURNAL   Biochem J 274 (Pt 2) (Pt 2), 521-526 (1991)
   PUBMED   2006916
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Eloranta,T.O., Khomutov,A.R., Khomutov,R.M. and Hyvonen,T.
  TITLE     Aminooxy analogues of spermidine as inhibitors of spermine synthase
            and substrates of hepatic polyamine acetylating activity
  JOURNAL   J Biochem 108 (4), 593-598 (1990)
   PUBMED   2292587
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Manzella,J.M. and Blackshear,P.J.
  TITLE     Regulation of rat ornithine decarboxylase mRNA translation by its
            5'-untranslated region
  JOURNAL   J Biol Chem 265 (20), 11817-11822 (1990)
   PUBMED   2365701
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Wen,L., Huang,J.K. and Blackshear,P.J.
  TITLE     Rat ornithine decarboxylase gene. Nucleotide sequence, potential
            regulatory elements, and comparison to the mouse gene
  JOURNAL   J Biol Chem 264 (15), 9016-9021 (1989)
   PUBMED   2722815
REFERENCE   10 (residues 1 to 461)
  AUTHORS   van Steeg,H., van Oostrom,T.M., van Kranen,H.J. and van Kreijl,C.F.
  TITLE     Nucleotide sequence of the rat ornithine decarboxylase gene
  JOURNAL   Nucleic Acids Res 16 (16), 8173-8174 (1988)
   PUBMED   3419906
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M16982.1, BC078882.1, DV728774.1 and FQ151473.1.
            
            On Sep 26, 2014 this sequence version replaced XP_006239968.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M16982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            regulatory uORF        :: PMID: 2365701
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..461
                     /product="ornithine decarboxylase"
                     /EC_number="4.1.1.17"
                     /note="Ornitine decarboxylase"
                     /calculated_mol_wt=50916
     Region          37..408
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(38,69,90..91,93..94,116,121,134,137,141,168..170,
                     291,293..294,315,317,319,322..323,331,333,357,359,361,364,
                     393,395,397..399,401)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,332,360,389)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,360,389)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(69,360)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            197
                     /site_type="other"
                     /note="Stacks against the aromatic ring of pyridoxal
                     phosphate and stabilizes reaction intermediates.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P09057.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P09057.1)"
     Site            order(331..332,360..361,389,397)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
     CDS             1..461
                     /gene="Odc1"
                     /gene_synonym="Odc"
                     /coded_by="NM_012615.3:305..1690"
                     /db_xref="GeneID:24609"
                     /db_xref="RGD:3227"
ORIGIN      
        1 mgsftkeefd childegfta kdildqkine vsssddkdaf yvadlgdvlk khlrwlkalp
       61 rvtpfyavkc ndsraivstl aaigtgfdca skteiqlvqg lgvpperiiy anpckqvsqi
      121 kyaasngvqm mtfdseielm kvarahpkak lvlriatdds kavcrlsvkf gatlktsrll
      181 lerakelnid vigvsfhvgs gctdpetfvq avsdarcvfd mgtevgfsmy lldigggfpg
      241 sedtklkfee itsvinpald kyfpsdsgvr iiaepgryyv asaftlavni iakktvwkeq
      301 tgsddedesn eqtlmyyvnd gvygsfncil ydhahvkall qkrpkpdeky ysssiwgptc
      361 dgldriverc slpemhvgdw mlfenmgayt vaaastfngf qrpniyyvms rsmwqlmkqi
      421 qshgfppeve eqdvgtlpms caqesgmdrh paacasasin v
//
LOCUS       NP_446063                 80 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear protein 1 [Rattus norvegicus].
ACCESSION   NP_446063 XP_003749035 XP_006223565
VERSION     NP_446063.1
DBSOURCE    REFSEQ: accession NM_053611.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Kolanowski,T.J., Wargocka-Matuszewska,W., Zimna,A., Cheda,L.,
            Zyprych-Walczak,J., Rugowska,A., Drabik,M., Fiedorowicz,M.,
            Krajewski,S., Steczek,L., Kozanecki,C., Rogulski,Z., Rozwadowska,N.
            and Kurpisz,M.
  TITLE     Multiparametric Evaluation of Post-MI Small Animal Models Using
            Metabolic ([18F]FDG) and Perfusion-Based (SYN1) Heart Viability
            Tracers
  JOURNAL   Int J Mol Sci 22 (22), 12591 (2021)
   PUBMED   34830471
  REMARK    GeneRIF: Multiparametric Evaluation of Post-MI Small Animal Models
            Using Metabolic ([(18)F]FDG) and Perfusion-Based (SYN1) Heart
            Viability Tracers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Huo,W., Li,H., Zhang,Y. and Li,H.
  TITLE     Epigenetic silencing of microRNA-874-3p implicates in erectile
            dysfunction in diabetic rats by activating the Nupr1/Chop-mediated
            pathway
  JOURNAL   FASEB J 34 (1), 1695-1709 (2020)
   PUBMED   31914690
  REMARK    GeneRIF: Nupr1 silencing also reduced CSMC apoptosis.
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Santofimia-Castano,P., Lan,W., Bintz,J., Gayet,O., Carrier,A.,
            Lomberk,G., Neira,J.L., Gonzalez,A., Urrutia,R., Soubeyran,P. and
            Iovanna,J.
  TITLE     Inactivation of NUPR1 promotes cell death by coupling ER-stress
            responses with necrosis
  JOURNAL   Sci Rep 8 (1), 16999 (2018)
   PUBMED   30451898
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Xu,X., Huang,E., Tai,Y., Zhao,X., Chen,X., Chen,C., Chen,R.,
            Liu,C., Lin,Z., Wang,H. and Xie,W.B.
  TITLE     Nupr1 Modulates Methamphetamine-Induced Dopaminergic Neuronal
            Apoptosis and Autophagy through CHOP-Trib3-Mediated Endoplasmic
            Reticulum Stress Signaling Pathway
  JOURNAL   Front Mol Neurosci 10, 203 (2017)
   PUBMED   28694771
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 80)
  AUTHORS   Galichon,P., Bataille,A., Vandermeersch,S., Wetzstein,M.,
            Xu-Dubois,Y.C., Legouis,D., Hertig,A., Buob,D., Placier,S.,
            Bige,N., Lefevre,G., Jouanneau,C., Martin,C., Iovanna,J.L. and
            Rondeau,E.
  TITLE     Stress Response Gene Nupr1 Alleviates Cyclosporin A Nephrotoxicity
            In Vivo
  JOURNAL   J Am Soc Nephrol 28 (2), 545-556 (2017)
   PUBMED   27451286
REFERENCE   6  (residues 1 to 80)
  AUTHORS   Vasseur,S., Hoffmeister,A., Garcia-Montero,A., Mallo,G.V., Feil,R.,
            Kuhbandner,S., Dagorn,J.C. and Iovanna,J.L.
  TITLE     p8-deficient fibroblasts grow more rapidly and are more resistant
            to adriamycin-induced apoptosis
  JOURNAL   Oncogene 21 (11), 1685-1694 (2002)
   PUBMED   11896600
REFERENCE   7  (residues 1 to 80)
  AUTHORS   Encinar,J.A., Mallo,G.V., Mizyrycki,C., Giono,L.,
            Gonzalez-Ros,J.M., Rico,M., Canepa,E., Moreno,S., Neira,J.L. and
            Iovanna,J.L.
  TITLE     Human p8 is a HMG-I/Y-like protein with DNA binding activity
            enhanced by phosphorylation
  JOURNAL   J Biol Chem 276 (4), 2742-2751 (2001)
   PUBMED   11056169
REFERENCE   8  (residues 1 to 80)
  AUTHORS   Vasseur,S., Vidal Mallo,G., Fiedler,F., Bodeker,H., Canepa,E.,
            Moreno,S. and Iovanna,J.L.
  TITLE     Cloning and expression of the human p8, a nuclear protein with
            mitogenic activity
  JOURNAL   Eur J Biochem 259 (3), 670-675 (1999)
   PUBMED   10092851
REFERENCE   9  (residues 1 to 80)
  AUTHORS   Mallo,G.V., Fiedler,F., Calvo,E.L., Ortiz,E.M., Vasseur,S.,
            Keim,V., Morisset,J. and Iovanna,J.L.
  TITLE     Cloning and expression of the rat p8 cDNA, a new gene activated in
            pancreas during the acute phase of pancreatitis, pancreatic
            development, and regeneration, and which promotes cellular growth
  JOURNAL   J Biol Chem 272 (51), 32360-32369 (1997)
   PUBMED   9405444
REFERENCE   10 (residues 1 to 80)
  AUTHORS   Lee,N.H., Weinstock,K.G., Kirkness,E.F., Earle-Hughes,J.A.,
            Fuldner,R.A., Marmaros,S., Glodek,A., Gocayne,J.D., Adams,M.D.,
            Kerlavage,A.R. et al.
  TITLE     Comparative expressed-sequence-tag analysis of differential gene
            expression profiles in PC-12 cells before and after nerve growth
            factor treatment
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8303-8307 (1995)
   PUBMED   7667285
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AA685246.1 and AF014503.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006223565.1, XP_003749035.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB584041.1, FQ106387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..80
                     /product="nuclear protein 1"
                     /note="protein p8; candidate of metastasis 1; nuclear
                     proten 1; nuclear protein 1-like; nuclear transcriptional
                     regulator protein 1; nuclear protein, transcriptional
                     regulator, 1; nuclear protein, transcriptional regulator,
                     1-like 1"
                     /calculated_mol_wt=8824
     Region          24..77
                     /region_name="Phospho_p8"
                     /note="DNA-binding nuclear phosphoprotein p8; pfam10195"
                     /db_xref="CDD:462991"
     Region          40..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54842.1)"
     Region          64..80
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O54842.1)"
     CDS             1..80
                     /gene="Nupr1"
                     /gene_synonym="Nupr1l1; p8"
                     /coded_by="NM_053611.2:87..329"
                     /db_xref="GeneID:100912108"
                     /db_xref="RGD:69363"
ORIGIN      
        1 matlpptaht sqqpvniede dgildeydqy slaqsyvvgg grkgrtkrea aantnrpspg
       61 gherklltkf qnserkkawr
//
LOCUS       NP_067595                 56 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase DCLK1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_067595
VERSION     NP_067595.1
DBSOURCE    REFSEQ: accession NM_021584.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 56)
  AUTHORS   Vitali,F., Tortora,K., Di Paola,M., Bartolucci,G., Menicatti,M., De
            Filippo,C. and Caderni,G.
  TITLE     Intestinal microbiota profiles in a genetic model of colon
            tumorigenesis correlates with colon cancer biomarkers
  JOURNAL   Sci Rep 12 (1), 1432 (2022)
   PUBMED   35082322
  REMARK    GeneRIF: Intestinal microbiota profiles in a genetic model of colon
            tumorigenesis correlates with colon cancer biomarkers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 56)
  AUTHORS   Nakane,T., Matsumoto,S., Iida,S., Ido,A., Fukunaga,K., Murao,K. and
            Sugiyama,Y.
  TITLE     Candidate plasticity gene 16 and jun dimerization protein 2 are
            involved in the suppression of insulin gene expression in rat
            pancreatic INS-1 beta-cells
  JOURNAL   Mol Cell Endocrinol 527, 111240 (2021)
   PUBMED   33676985
  REMARK    GeneRIF: Candidate plasticity gene 16 and jun dimerization protein
            2 are involved in the suppression of insulin gene expression in rat
            pancreatic INS-1 beta-cells.
REFERENCE   3  (residues 1 to 56)
  AUTHORS   Nakane,T., Ido,A., Higuchi,T., Todaka,H., Morisawa,K., Nagamine,T.,
            Fukunaga,K., Sakamoto,S., Murao,K. and Sugiyama,Y.
  TITLE     Candidate plasticity gene 16 mediates suppression of insulin gene
            expression in rat insulinoma INS-1cells under glucotoxic conditions
  JOURNAL   Biochem Biophys Res Commun 512 (2), 189-195 (2019)
   PUBMED   30879761
  REMARK    GeneRIF: These results suggest that CPG16 plays a role in the
            suppression of insulin gene expression in pancreatic beta-cells
            under glucotoxic conditions.
REFERENCE   4  (residues 1 to 56)
  AUTHORS   Quan,X., Huang,L., Yang,Y., Ma,T., Liu,Z., Ge,J., Huang,J. and
            Luo,Z.
  TITLE     Potential Mechanism of Neurite Outgrowth Enhanced by Electrical
            Stimulation: Involvement of MicroRNA-363-5p Targeting DCLK1
            Expression in Rat
  JOURNAL   Neurochem Res 42 (2), 513-525 (2017)
   PUBMED   27900578
  REMARK    GeneRIF: Electrical stimulated-neurite outgrowth is regulated by
            MicroRNA-363-5p through targeting of DCLK1.
REFERENCE   5  (residues 1 to 56)
  AUTHORS   Lipka,J., Kapitein,L.C., Jaworski,J. and Hoogenraad,C.C.
  TITLE     Microtubule-binding protein doublecortin-like kinase 1 (DCLK1)
            guides kinesin-3-mediated cargo transport to dendrites
  JOURNAL   EMBO J 35 (3), 302-318 (2016)
   PUBMED   26758546
  REMARK    GeneRIF: The authors found that microtubule-binding protein
            doublecortin-like kinase 1 (DCLK1) labels a subset of dendritic
            microtubules and is required for KIF1-dependent dense-core vesicles
            (DCVs) trafficking into dendrites and dendrite development.
REFERENCE   6  (residues 1 to 56)
  AUTHORS   Lin,P.T., Gleeson,J.G., Corbo,J.C., Flanagan,L. and Walsh,C.A.
  TITLE     DCAMKL1 encodes a protein kinase with homology to doublecortin that
            regulates microtubule polymerization
  JOURNAL   J Neurosci 20 (24), 9152-9161 (2000)
   PUBMED   11124993
REFERENCE   7  (residues 1 to 56)
  AUTHORS   Mizuguchi,M., Qin,J., Yamada,M., Ikeda,K. and Takashima,S.
  TITLE     High expression of doublecortin and KIAA0369 protein in fetal brain
            suggests their specific role in neuronal migration
  JOURNAL   Am J Pathol 155 (5), 1713-1721 (1999)
   PUBMED   10550327
REFERENCE   8  (residues 1 to 56)
  AUTHORS   Vreugdenhil,E., Datson,N., Engels,B., de Jong,J., van
            Koningsbruggen,S., Schaaf,M. and de Kloet,E.R.
  TITLE     Kainate-elicited seizures induce mRNA encoding a CaMK-related
            peptide: a putative modulator of kinase activity in rat hippocampus
  JOURNAL   J Neurobiol 39 (1), 41-50 (1999)
   PUBMED   10213452
REFERENCE   9  (residues 1 to 56)
  AUTHORS   Berke,J.D., Paletzki,R.F., Aronson,G.J., Hyman,S.E. and Gerfen,C.R.
  TITLE     A complex program of striatal gene expression induced by
            dopaminergic stimulation
  JOURNAL   J Neurosci 18 (14), 5301-5310 (1998)
   PUBMED   9651213
REFERENCE   10 (residues 1 to 56)
  AUTHORS   Hevroni,D., Rattner,A., Bundman,M., Lederfein,D., Gabarah,A.,
            Mangelus,M., Silverman,M.A., Kedar,H., Naor,C., Kornuc,M.,
            Hanoch,T., Seger,R., Theill,L.E., Nedivi,E., Richter-Levin,G. and
            Citri,Y.
  TITLE     Hippocampal plasticity involves extensive gene induction and
            multiple cellular mechanisms
  JOURNAL   J Mol Neurosci 10 (2), 75-98 (1998)
   PUBMED   9699150
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. The typical protein
            encoded by this gene contains two N-terminal doublecortin domains,
            which bind microtubules and regulate microtubule polymerization, a
            C-terminal serine/threonine protein kinase domain, which shows
            substantial homology to Ca2+/calmodulin-dependent protein kinase,
            and a serine/proline-rich domain in between the doublecortin and
            the protein kinase domains, which mediates multiple protein-protein
            interactions. The microtubule-polymerizing activity of the protein
            is independent of its protein kinase activity. This gene is
            involved in several different cellular processes, including
            neuronal migration, retrograde transport, neuronal apoptosis and
            neurogenesis. Multiple transcript variants generated by two
            alternative promoter usage and alternative splicing have been
            found, but the full-length nature of the variant produced from the
            5' promoter has not been determined. Current reference sequence
            data represents two alternatively spliced transcript variants
            produced from the 3' promoter and their protein products lack the
            doublecortin domain.[provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (2) is produced from the 3'
            promoter. It lacks multiple 3' exons but has an alternate 3' exon,
            as compared to variant 1. The resulting isoform [2, also known as
            ania-4, or CARP (CaMK-related peptide)] is only 56 aa long and
            mainly consists of the serine/proline-rich domain.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF045469.1, AF030089.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..56
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..56
                     /product="serine/threonine-protein kinase DCLK1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="double cortin and calcium/calmodulin-dependent
                     protein kinase-like 1; serine/threonine-protein kinase
                     DCLK1; doublecortin-like and CAM kinase-like 1"
                     /calculated_mol_wt=5782
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     CDS             1..56
                     /gene="Dclk1"
                     /gene_synonym="Ania4; Cpg16; Dcamkl1"
                     /coded_by="NM_021584.2:147..317"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:83825"
                     /db_xref="RGD:68437"
ORIGIN      
        1 mlelievngt pgsqlstprs gkspspspts pgslrkqrdl yrplssddld svgdsv
//
LOCUS       NP_036677                480 aa            linear   ROD 27-APR-2025
DEFINITION  aromatic-L-amino-acid decarboxylase isoform a [Rattus norvegicus].
ACCESSION   NP_036677
VERSION     NP_036677.1
DBSOURCE    REFSEQ: accession NM_012545.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Seo,D.C., Ju,Y.H., Seo,J.J., Oh,S.J., Lee,C.J., Lee,S.E. and
            Nam,M.H.
  TITLE     DDC-Promoter-Driven Chemogenetic Activation of SNpc Dopaminergic
            Neurons Alleviates Parkinsonian Motor Symptoms
  JOURNAL   Int J Mol Sci 24 (3), 2491 (2023)
   PUBMED   36768816
  REMARK    GeneRIF: DDC-Promoter-Driven Chemogenetic Activation of SNpc
            Dopaminergic Neurons Alleviates Parkinsonian Motor Symptoms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Sizova,D., Velazquez,H., Sampaio-Maia,B., Quelhas-Santos,J.,
            Pestana,M. and Desir,G.V.
  TITLE     Renalase regulates renal dopamine and phosphate metabolism
  JOURNAL   Am J Physiol Renal Physiol 305 (6), F839-F844 (2013)
   PUBMED   23863468
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Voigt,A., Hubner,S., Lossow,K., Hermans-Borgmeyer,I., Boehm,U. and
            Meyerhof,W.
  TITLE     Genetic labeling of Tas1r1 and Tas2r131 taste receptor cells in
            mice
  JOURNAL   Chem Senses 37 (9), 897-911 (2012)
   PUBMED   23010799
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Rouzaud-Laborde,C., Hanoun,N., Baysal,I., Rech,J.S., Mias,C.,
            Calise,D., Sicard,P., Frugier,C., Seguelas,M.H., Parini,A. and
            Pizzinat,N.
  TITLE     Role of endothelial AADC in cardiac synthesis of serotonin and
            nitrates accumulation
  JOURNAL   PLoS One 7 (7), e34893 (2012)
   PUBMED   22829864
  REMARK    GeneRIF: The data show that endothelial AADC plays an important
            role in cardiac synthesis of 5-HT and possibly in 5-HT-dependent
            regulation of nitric oxide generation.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Brun,L., Ngu,L.H., Keng,W.T., Ch'ng,G.S., Choy,Y.S., Hwu,W.L.,
            Lee,W.T., Willemsen,M.A., Verbeek,M.M., Wassenberg,T., Regal,L.,
            Orcesi,S., Tonduti,D., Accorsi,P., Testard,H., Abdenur,J.E.,
            Tay,S., Allen,G.F., Heales,S., Kern,I., Kato,M., Burlina,A.,
            Manegold,C., Hoffmann,G.F. and Blau,N.
  TITLE     Clinical and biochemical features of aromatic L-amino acid
            decarboxylase deficiency
  JOURNAL   Neurology 75 (1), 64-71 (2010)
   PUBMED   20505134
  REMARK    Erratum:[Neurology. 2010 Aug 10;75(6):576. Dosage error in article
            text]
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Rorsman,F., Husebye,E.S., Winqvist,O., Bjork,E., Karlsson,F.A. and
            Kampe,O.
  TITLE     Aromatic-L-amino-acid decarboxylase, a pyridoxal
            phosphate-dependent enzyme, is a beta-cell autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8626-8629 (1995)
   PUBMED   7567987
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Eaton,M.J., Gudehithlu,K.P., Quach,T., Silvia,C.P.,
            Hadjiconstantinou,M. and Neff,N.H.
  TITLE     Distribution of aromatic L-amino acid decarboxylase mRNA in mouse
            brain by in situ hybridization histology
  JOURNAL   J Comp Neurol 337 (4), 640-654 (1993)
   PUBMED   7904615
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Albert,V.R., Lee,M.R., Bolden,A.H., Wurzburger,R.J. and Aguanno,A.
  TITLE     Distinct promoters direct neuronal and nonneuronal expression of
            rat aromatic L-amino acid decarboxylase
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12053-12057 (1992)
   PUBMED   1465439
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Tanaka,T., Horio,Y., Taketoshi,M., Imamura,I., Ando-Yamamoto,M.,
            Kangawa,K., Matsuo,H., Kuroda,M. and Wada,H.
  TITLE     Molecular cloning and sequencing of a cDNA of rat dopa
            decarboxylase: partial amino acid homologies with other enzymes
            synthesizing catecholamines
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8142-8146 (1989)
   PUBMED   2813383
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Yamazaki,N. and Sudo,J.
  TITLE     Activities of aromatic L-amino acid decarboxylase with L-dopa as
            substrate in brush-border- and basolateral membranes and cytoplasm
            obtained from rat renal cortex
  JOURNAL   Jpn J Pharmacol 46 (2), 193-196 (1988)
   PUBMED   3379830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M27716.1 and JAXUCZ010000014.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 3
            encode the same protein (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219697.1, SRR26360181.907442.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..480
                     /product="aromatic-L-amino-acid decarboxylase isoform a"
                     /EC_number="4.1.1.28"
                     /note="aromatic-L-amino-acid decarboxylase; L-Dopa
                     decarboxylase; dopa decarboxylase (aromatic L-amino acid
                     decarboxylase)"
                     /calculated_mol_wt=53923
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P80041; propagated from
                     UniProtKB/Swiss-Prot (P14173.1)"
     Region          35..414
                     /region_name="Pyridoxal_deC"
                     /note="Pyridoxal-dependent decarboxylase conserved domain;
                     pfam00282"
                     /db_xref="CDD:395219"
     Region          58..178
                     /region_name="2 X approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P14173.1)"
     Site            order(148..149,152,242,271,274,300,303)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99743"
     Site            303
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99743"
     CDS             1..480
                     /gene="Ddc"
                     /gene_synonym="AADC"
                     /coded_by="NM_012545.4:74..1516"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24311"
                     /db_xref="RGD:2494"
ORIGIN      
        1 mdsrefrrrg kemvdyiady ldgiegrpvy pdvepgylra lipttapqep etyediirdi
       61 ekiimpgvth whspyffayf ptassypaml admlcgaigc igfswaaspa cteletvmmd
      121 wlgkmlelpe aflagrageg ggviqgsase atlvallaar tkmirqlqaa speltqaalm
      181 eklvaytsdq ahssveragl iggvkikaip sdgnysmraa alrealerdk aaglipffvv
      241 vtlgttsccs fdnllevgpi cnqegvwlhi daayagsafi cpefryllng vefadsfnfn
      301 phkwllvnfd csamwvkkrt dlteafnmdp vylrhshqds glitdyrhwq iplgrrfrsl
      361 kmwfvfrmyg vkglqayirk hvklshefes lvrqdprfei ctevilglvc frlkgsnqln
      421 etllqrinsa kkihlvpcrl rdkfvlrfav csrtvesahv qlawehirdl assvlraeke
//
LOCUS       NP_001276912             188 aa            linear   ROD 27-APR-2025
DEFINITION  D site-binding protein isoform 3 [Rattus norvegicus].
ACCESSION   NP_001276912
VERSION     NP_001276912.1
DBSOURCE    REFSEQ: accession NM_001289983.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Jiang,H., Li,J., He,X., Xue,J., Liang,S., Liu,S., Gao,F., Qu,N.,
            Liu,H. and Chen,L.
  TITLE     D-site binding protein regulates cell proliferation through
            mediating cell cycle progression in rat mesangial cells
  JOURNAL   Tissue Cell 61, 35-43 (2019)
   PUBMED   31759405
  REMARK    GeneRIF: DBP effectively inhibits the proliferation of mesangial
            cells through G1 phase arrest.
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Harbour,V.L., Weigl,Y., Robinson,B. and Amir,S.
  TITLE     Phase differences in expression of circadian clock genes in the
            central nucleus of the amygdala, dentate gyrus, and suprachiasmatic
            nucleus in the rat
  JOURNAL   PLoS One 9 (7), e103309 (2014)
   PUBMED   25068868
  REMARK    GeneRIF: Data show that the expression of clock genes Per2, Bmal1
            and Dbp follow a diurnal rhythm in the central nucleus of the
            amygdala, dentate gyrus, and suprachiasmatic nucleu but the phase
            and amplitude of the rhythms of each gene vary across the 3
            regions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Huang,X.M., Chen,W.L., Yuan,J.P., Yang,Y.H., Mei,Q.H. and
            Huang,L.X.
  TITLE     Altered diurnal variation and localization of clock proteins in the
            remnant kidney of 5/6 nephrectomy rats
  JOURNAL   Nephrology (Carlton) 18 (8), 555-562 (2013)
   PUBMED   23738784
  REMARK    GeneRIF: The localization and diurnal variation of BMAL1, DBP and
            PER2 are changed in remnant kidney of 5/6 nephrectomy rats and are
            involved in diurnal rhythm of renal function.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Yamajuku,D., Shibata,Y., Kitazawa,M., Katakura,T., Urata,H.,
            Kojima,T., Takayasu,S., Nakata,O. and Hashimoto,S.
  TITLE     Cellular DBP and E4BP4 proteins are critical for determining the
            period length of the circadian oscillator
  JOURNAL   FEBS Lett 585 (14), 2217-2222 (2011)
   PUBMED   21635892
  REMARK    GeneRIF: Data show that knockdown of DBP, D-box positive regulator,
            led to a short-period phenotype, and overexpression of DBP produced
            a long-period rhythm, while knockdown and overexpression of E4BP4,
            D-box negative regulator, had the opposite effect of DBP.
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Xu,Z., Kaga,S., Tsubomizu,J., Fujisaki,J., Mochiduki,A., Sakai,T.,
            Tsukamura,H., Maeda,K., Inoue,K. and Adachi,A.A.
  TITLE     Circadian transcriptional factor DBP regulates expression of Kiss1
            in the anteroventral periventricular nucleus
  JOURNAL   Mol Cell Endocrinol 339 (1-2), 90-97 (2011)
   PUBMED   21458520
  REMARK    GeneRIF: Dbp and estrogen regulate the expression of Kiss1 in the
            anteroventral periventricular nucleus
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Brown,S.A., Zumbrunn,G., Fleury-Olela,F., Preitner,N. and
            Schibler,U.
  TITLE     Rhythms of mammalian body temperature can sustain peripheral
            circadian clocks
  JOURNAL   Curr Biol 12 (18), 1574-1583 (2002)
   PUBMED   12372249
  REMARK    GeneRIF: natural body temperature rhythms can affect circadian gene
            expression
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Brown,S.A. and Schibler,U.
  TITLE     The ins and outs of circadian timekeeping
  JOURNAL   Curr Opin Genet Dev 9 (5), 588-594 (1999)
   PUBMED   10508692
  REMARK    Review article
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Mueller,C.R., Maire,P. and Schibler,U.
  TITLE     DBP, a liver-enriched transcriptional activator, is expressed late
            in ontogeny and its tissue specificity is determined
            posttranscriptionally
  JOURNAL   Cell 61 (2), 279-291 (1990)
   PUBMED   2331750
  REMARK    Erratum:[Cell. 1991 May 31;65(5):915. PMID: 2040017]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Summary: The protein encoded by this gene is a member of the Par
            bZIP transcription factor family and binds to specific sequences in
            the promoters of several genes, such as albumin, Cyp2a4, and
            Cyp2a5. The encoded protein can bind DNA as a homo- or heterodimer
            and is involved in the regulation of some circadian rhythym genes.
            Three transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY518349.1, SRR22582419.1999356.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..188
                     /product="D site-binding protein isoform 3"
                     /note="d site-binding protein; albumin D box-binding
                     protein; albumin D-element-binding protein; d site albumin
                     promoter-binding protein 1; D site albumin promoter
                     binding protein; D site of albumin promoter (albumin
                     D-box) binding protein"
                     /calculated_mol_wt=20909
     Region          117..176
                     /region_name="bZIP_HLF"
                     /note="Basic leucine zipper (bZIP) domain of Hepatic
                     leukemia factor (HLF) and similar proteins: a DNA-binding
                     and dimerization domain; cd14695"
                     /db_xref="CDD:269843"
     Region          118..176
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269843"
     Site            order(124..125,127..129,131..136,138..140)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269843"
     Site            order(139,142..143,146..147,149..150,153..154,156..157,
                     160..161,163..164,167..168,170..171)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269843"
     CDS             1..188
                     /gene="Dbp"
                     /coded_by="NM_001289983.1:402..968"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24309"
                     /db_xref="RGD:2491"
ORIGIN      
        1 marplsdrtp gplllggpag appgggallg lrsllqgnsk pkepasclts rdtpspvdpd
       61 tvevlmtfep dpadlalssi pghetfdprr hrfseeelkp qpimkkarkv qvpeeqkdek
      121 ywsrryknne aakrsrdarr lkenqisvra aflekenall rqevvavrqe lshyravlsr
      181 yqaqhgtl
//
LOCUS       NP_446358                410 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione reductase [Rattus norvegicus].
ACCESSION   NP_446358 XP_344529
VERSION     NP_446358.2
DBSOURCE    REFSEQ: accession NM_053906.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Bessieres,B., Cruz,E. and Alberini,C.M.
  TITLE     Metabolomic profiling reveals a differential role for hippocampal
            glutathione reductase in infantile memory formation
  JOURNAL   Elife 10, e68590 (2021)
   PUBMED   34825649
  REMARK    GeneRIF: Metabolomic profiling reveals a differential role for
            hippocampal glutathione reductase in infantile memory formation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Kim,J.S., Kwon,W.Y., Suh,G.J., Kim,K.S., Jung,Y.S., Kim,S.H. and
            Lee,S.E.
  TITLE     Plasma glutathione reductase activity and prognosis of septic shock
  JOURNAL   J Surg Res 200 (1), 298-307 (2016)
   PUBMED   26316444
  REMARK    GeneRIF: Plasma glutathione reductase (GR) activity was correlated
            with erythrocyte GR activity and the erythrocyte reduced
            glutathione/glutathione disulfide ratio. A decrease in plasma GR
            activity was associated with an increase in mortality in septic
            shock.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Nidhi,B., Sharavana,G., Ramaprasad,T.R. and Vallikannan,B.
  TITLE     Lutein derived fragments exhibit higher antioxidant and
            anti-inflammatory properties than lutein in lipopolysaccharide
            induced inflammation in rats
  JOURNAL   Food Funct 6 (2), 450-460 (2015)
   PUBMED   25469663
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Abd El Tawab,A.M., Shahin,N.N. and AbdelMohsen,M.M.
  TITLE     Protective effect of Satureja montana extract on
            cyclophosphamide-induced testicular injury in rats
  JOURNAL   Chem Biol Interact 224, 196-205 (2014)
   PUBMED   25446862
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Yeung,J.H.
  TITLE     Effects of glycerol-induced acute renal failure on tissue
            glutathione and glutathione-dependent enzymes in the rat
  JOURNAL   Methods Find Exp Clin Pharmacol 13 (1), 23-28 (1991)
   PUBMED   1870354
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for thymidine kinase and galactokinase to
            Mus musculus chromosome 11 and the preferential segregation of this
            chromosome in Chinese hamster/mouse somatic cell hybrids
  JOURNAL   Somatic Cell Genet 3 (2), 121-133 (1977)
   PUBMED   204065
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Loos,H., Roos,D., Weening,R. and Houwerzijl,J.
  TITLE     Familial deficiency of glutathione reductase in human blood cells
  JOURNAL   Blood 48 (1), 53-62 (1976)
   PUBMED   947404
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Kozak,C., Nichols,E. and Ruddle,F.H.
  TITLE     Gene linkage analysis in the mouse by somatic cell hybridization:
            assignment of adenine phosphoribosyltransferase to chromosome 8 and
            alpha-galactosidase to the X chromosome
  JOURNAL   Somatic Cell Genet 1 (4), 371-382 (1975)
   PUBMED   1235912
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Carlberg,I. and Mannervik,B.
  TITLE     Purification and characterization of the flavoenzyme glutathione
            reductase from rat liver
  JOURNAL   J Biol Chem 250 (14), 5475-5480 (1975)
   PUBMED   237922
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM035154.1, CK357934.1 and JAXUCZ010000016.1.
            
            On Oct 20, 2010 this sequence version replaced NP_446358.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.32873.1,
                                           SRR26643291.38408.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..410
                     /product="glutathione reductase"
                     /EC_number="1.8.1.7"
                     /note="GR; GRase; glutathione reductase, mitochondrial"
                     /calculated_mol_wt=44658
     Region          1..410
                     /region_name="Pyr_redox_2"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     cl39093"
                     /db_xref="CDD:476868"
     CDS             1..410
                     /gene="Gsr"
                     /coded_by="NM_053906.2:57..1289"
                     /db_xref="GeneID:116686"
                     /db_xref="RGD:621747"
ORIGIN      
        1 mwntavhsef ihdhvdygfq nckskfnwhv ikekrdayvs rlnniyqnnl tkshievihg
       61 yatfadgpqp tvevngkkft aphiliatgg vptvphenqi pgaslgitsd gffqledlps
      121 rsvivgagyi aveiagilsa lgsktslmir hdkvlrsfds lissncteel enagvevlkf
      181 sqvkevkktp sglelhvvta lpgrkptvtt ipdvdcllwa igrdpnskgl nlnklgiqtd
      241 dkghilvdef qntnvkgvya vgdvcgkall tpvaiaagrk lahrlfegke dsrldydnip
      301 tvvfshppig tvgltedeav hkygkdnvki ystaftpmyh avttrktkcv mkmvcankee
      361 kvvgihmqgi gcdemlqgfa vavkmgatka dfdntvaihp tsseelvtlr
//
LOCUS       NP_112335                271 aa            linear   ROD 27-APR-2025
DEFINITION  neurotrophin-3 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_112335
VERSION     NP_112335.3
DBSOURCE    REFSEQ: accession NM_031073.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Briones-Vidal,M.G., Reyes-Garcia,S.E. and Escobar,M.L.
  TITLE     Neurotrophin-3 into the insular cortex strengthens conditioned
            taste aversion memory
  JOURNAL   Behav Brain Res 461, 114857 (2024)
   PUBMED   38211776
  REMARK    GeneRIF: Neurotrophin-3 into the insular cortex strengthens
            conditioned taste aversion memory.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zou,D., Wang,H., Hao,S. and Chen,F.
  TITLE     Repair effect of neurotrophic factor III (NT-3) on rats with spinal
            injury model and its mechanism
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (1), 56-61 (2024)
   PUBMED   38372112
  REMARK    GeneRIF: Repair effect of neurotrophic factor III (NT-3) on rats
            with spinal injury model and its mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Yang,Y., Xu,H.Y., Deng,Q.W., Wu,G.H., Zeng,X., Jin,H., Wang,L.J.,
            Lai,B.Q., Li,G., Ma,Y.H., Jiang,B., Ruan,J.W., Wang,Y.Q., Ding,Y.
            and Zeng,Y.S.
  TITLE     Electroacupuncture facilitates the integration of a grafted
            TrkC-modified mesenchymal stem cell-derived neural network into
            transected spinal cord in rats via increasing neurotrophin-3
  JOURNAL   CNS Neurosci Ther 27 (7), 776-791 (2021)
   PUBMED   33763978
  REMARK    GeneRIF: Electroacupuncture facilitates the integration of a
            grafted TrkC-modified mesenchymal stem cell-derived neural network
            into transected spinal cord in rats via increasing neurotrophin-3.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Xu,H., Yang,Y., Deng,Q.W., Zhang,B.B., Ruan,J.W., Jin,H.,
            Wang,J.H., Ren,J., Jiang,B., Sun,J.H., Zeng,Y.S. and Ding,Y.
  TITLE     Governor Vessel Electro-Acupuncture Promotes the Intrinsic Growth
            Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury
  JOURNAL   J Neurotrauma 38 (6), 734-745 (2021)
   PUBMED   33121345
  REMARK    GeneRIF: Governor Vessel Electro-Acupuncture Promotes the Intrinsic
            Growth Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Donsante,A., Xue,J., Poth,K.M., Hardcastle,N.S., Diniz,B.,
            O'Connor,D.M., Xia,Y. and Boulis,N.M.
  TITLE     Controlling the Release of Neurotrophin-3 and Chondroitinase ABC
            Enhances the Efficacy of Nerve Guidance Conduits
  JOURNAL   Adv Healthc Mater 9 (14), e2000200 (2020)
   PUBMED   32548984
  REMARK    GeneRIF: Controlling the Release of Neurotrophin-3 and
            Chondroitinase ABC Enhances the Efficacy of Nerve Guidance
            Conduits.
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Smith,M.A., Makino,S., Altemus,M., Michelson,D., Hong,S.K.,
            Kvetnansky,R. and Post,R.M.
  TITLE     Stress and antidepressants differentially regulate neurotrophin 3
            mRNA expression in the locus coeruleus
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8788-8792 (1995)
   PUBMED   7568018
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Le Beau,M.M., Espinosa,R. 3rd, Ip,N.Y.,
            Belluscio,L., de la Monte,S.M., Squinto,S., Furth,M.E. and
            Yancopoulos,G.D.
  TITLE     Human and rat brain-derived neurotrophic factor and neurotrophin-3:
            gene structures, distributions, and chromosomal localizations
  JOURNAL   Genomics 10 (3), 558-568 (1991)
   PUBMED   1889806
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Hallbook,F., Ibanez,C.F. and Persson,H.
  TITLE     Evolutionary studies of the nerve growth factor family reveal a
            novel member abundantly expressed in Xenopus ovary
  JOURNAL   Neuron 6 (5), 845-858 (1991)
   PUBMED   2025430
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Ernfors,P., Ibanez,C.F., Ebendal,T., Olson,L. and Persson,H.
  TITLE     Molecular cloning and neurotrophic activities of a protein with
            structural similarities to nerve growth factor: developmental and
            topographical expression in the brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5454-5458 (1990)
   PUBMED   2164684
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Belluscio,L., Squinto,S., Ip,N.Y., Furth,M.E.,
            Lindsay,R.M. and Yancopoulos,G.D.
  TITLE     Neurotrophin-3: a neurotrophic factor related to NGF and BDNF
  JOURNAL   Science 247 (4949 Pt 1), 1446-1451 (1990)
   PUBMED   2321006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070504.1 and M34643.1.
            
            On Aug 4, 2012 this sequence version replaced NP_112335.2.
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070504.1, CK365049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..271
                     /product="neurotrophin-3 isoform 1 precursor"
                     /note="HDNF; NT-3; NGF-2; neurotrophic factor; nerve
                     growth factor 2; neurotrophin-3 (HDNF/NT-3)"
                     /calculated_mol_wt=27558
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3490
     Region          33..146
                     /region_name="NTF3_N"
                     /note="Neutrophin-3 N-terminus; pfam19338"
                     /db_xref="CDD:437170"
     Region          158..269
                     /region_name="NGF"
                     /note="Nerve growth factor family; pfam00243"
                     /db_xref="CDD:459728"
     CDS             1..271
                     /gene="Ntf3"
                     /coded_by="NM_031073.3:283..1098"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:81737"
                     /db_xref="RGD:619728"
ORIGIN      
        1 mvtsatilqv nkvmsilfyv iflaylrgiq gnnmdqrslp edslnsliik liqadilknk
       61 lskqmvdvke nyqstlpkae aprepeqgea trsefqpmia tdtellrqqr rynsprvlls
      121 dstplepppl ylmedyvgnp vvtnrtsprr kryaehkshr geysvcdses lwvtdkssai
      181 dirghqvtvl geiktgnspv kqyfyetrck earpvkngcr giddkhwnsq cktsqtyvra
      241 ltsennklvg wrwiridtsc vcalsrkigr t
//
LOCUS       NP_037074                503 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 7A1 [Rattus norvegicus].
ACCESSION   NP_037074
VERSION     NP_037074.1
DBSOURCE    REFSEQ: accession NM_012942.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Duan,Y., Zhang,F., Yuan,W., Wei,Y., Wei,M., Zhou,Y., Yang,Y.,
            Chang,Y. and Wu,X.
  TITLE     Hepatic cholesterol accumulation ascribed to the activation of
            ileum Fxr-Fgf15 pathway inhibiting hepatic Cyp7a1 in high-fat
            diet-induced obesity rats
  JOURNAL   Life Sci 232, 116638 (2019)
   PUBMED   31288013
  REMARK    GeneRIF: The increased CDCAs concentrations activated Fxr-Fgf15
            pathway in ileum to result in the mRNA expression of Cyp7a1 in
            liver down-regulation, which inhibited cholesterol metabolizing
            into primary BAs to contribute to the cholesterol level increase in
            liver tissue in HFD-induced obesity rats.
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Hao,C.L., Lin,H.L., Ke,L.Y., Yen,H.W. and Shen,K.P.
  TITLE     Pre-germinated brown rice extract ameliorates high-fat diet-induced
            metabolic syndrome
  JOURNAL   J Food Biochem 43 (3), e12769 (2019)
   PUBMED   31353547
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Hu,Y.B., Liu,X.Y. and Zhan,W.
  TITLE     Farnesoid X receptor agonist INT-767 attenuates liver steatosis and
            inflammation in rat model of nonalcoholic steatohepatitis
  JOURNAL   Drug Des Devel Ther 12, 2213-2221 (2018)
   PUBMED   30038487
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Huo,X.K., Liu,J., Yu,Z.L., Wang,Y.F., Wang,C., Tian,X.G., Ning,J.,
            Feng,L., Sun,C.P., Zhang,B.J. and Ma,X.C.
  TITLE     Alisma orientale extract exerts the reversing cholestasis effect by
            activation of farnesoid X receptor
  JOURNAL   Phytomedicine 42, 34-42 (2018)
   PUBMED   29655695
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Han,H., Xu,L., Xiong,K., Zhang,T. and Wang,Z.
  TITLE     Exploration of Hepatoprotective Effect of Gentiopicroside on
            Alpha-Naphthylisothiocyanate-Induced Cholestatic Liver Injury in
            Rats by Comprehensive Proteomic and Metabolomic Signatures
  JOURNAL   Cell Physiol Biochem 49 (4), 1304-1319 (2018)
   PUBMED   30223280
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Chiang,J.Y., Yang,T.P. and Wang,D.P.
  TITLE     Cloning and 5'-flanking sequence of a rat cholesterol 7
            alpha-hydroxylase gene
  JOURNAL   Biochim Biophys Acta 1132 (3), 337-339 (1992)
   PUBMED   1420318
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Nishimoto,M., Gotoh,O., Okuda,K. and Noshiro,M.
  TITLE     Structural analysis of the gene encoding rat cholesterol
            alpha-hydroxylase, the key enzyme for bile acid biosynthesis
  JOURNAL   J Biol Chem 266 (10), 6467-6471 (1991)
   PUBMED   2007596
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Jelinek,D.F. and Russell,D.W.
  TITLE     Structure of the rat gene encoding cholesterol 7 alpha-hydroxylase
  JOURNAL   Biochemistry 29 (34), 7781-7785 (1990)
   PUBMED   2261433
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Li,Y.C., Wang,D.P. and Chiang,J.Y.
  TITLE     Regulation of cholesterol 7 alpha-hydroxylase in the liver.
            Cloning, sequencing, and regulation of cholesterol 7
            alpha-hydroxylase mRNA
  JOURNAL   J Biol Chem 265 (20), 12012-12019 (1990)
   PUBMED   1694852
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Noshiro,M., Nishimoto,M. and Okuda,K.
  TITLE     Rat liver cholesterol 7 alpha-hydroxylase. Pretranslational
            regulation for circadian rhythm
  JOURNAL   J Biol Chem 265 (17), 10036-10041 (1990)
   PUBMED   1693613
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J05460.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05460.1, J05430.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Rattus norvegicus"
                     /strain="WKA"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..503
                     /product="cytochrome P450 7A1"
                     /EC_number="1.14.14.23"
                     /EC_number="1.14.14.26"
                     /note="cholesterol 7-alpha-monooxygenase; CYPVII;
                     cholesterol 7-alpha-hydroxylase; cytochrome P450
                     (cholesterol hydroxylase 7 alpha); cytochrome P450, 7a1;
                     cytochrome P450, family 7, subfamily a, polypeptide 1;
                     24-hydroxycholesterol 7-alpha-hydroxylase"
                     /calculated_mol_wt=56752
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18125.1)"
     Region          55..497
                     /region_name="CYP7A1"
                     /note="cytochrome P450 family 7, subfamily A, polypeptide
                     1; cd20631"
                     /db_xref="CDD:410724"
     Site            order(101,129,285..286,289..290,293,360,362,436..437,442,
                     444..446,449..450,453,488)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410724"
     Site            order(101,104..105,114,125,129,260,281,284..285,289,
                     360..361,485..487)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410724"
     CDS             1..503
                     /gene="Cyp7a1"
                     /gene_synonym="CHAP; CYP7; CYP7S1"
                     /coded_by="NM_012942.2:35..1546"
                     /db_xref="GeneID:25428"
                     /db_xref="RGD:2482"
ORIGIN      
        1 mmtisliwgi avlvscciwf ivgirrrkag epplenglip ylgcalkfgs npleflranq
       61 rkhghvftck lmgkyvhfit nslsyhkvlc hgkyfdwkkf hyttsakafg hrsidpndgn
      121 tteninntft ktlqgdalcs lseammqnlq svmrppglpk sksnawvteg myafcyrvmf
      181 eagyltlfgr disktdtqka lilnnldnfk qfdqvfpalv aglpihlfkt ahkareklae
      241 glkhknlcvr dqvselirlr mflndtlstf ddmekakthl ailwasqant ipatfwslfq
      301 mirspeamka aseevsgalq sagqelssgg saiyldqvql ndlpvldsii kealrlssas
      361 lnirtakedf tlhledgsyn irkddmialy pqlmhldpei ypdpltfkyd ryldesgkak
      421 ttfysngnkl kcfympfgsg aticpgrlfa vqeikqflil mlscfelefv esqvkcppld
      481 qsraglgilp plhdiefkyk lkh
//
LOCUS       NP_001288265             284 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.1st [Rattus norvegicus].
ACCESSION   NP_001288265 XP_006243449
VERSION     NP_001288265.1
DBSOURCE    REFSEQ: accession NM_001301336.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000008.1.
            
            On Sep 4, 2014 this sequence version replaced XP_006243449.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.1st, also known as variant
            10) contains a alternate 3' exon compared to variant 1. The
            resulting protein (isoform Tpm1.1st) is shorter and has a distinct
            C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216683.1, FQ214868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.1st"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32550
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04692.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P09493; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     Region          116..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04692.3)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DAPK1.
                     /evidence=ECO:0000250|UniProtKB:P09493; propagated from
                     UniProtKB/Swiss-Prot (P04692.3)"
     CDS             1..284
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001301336.1:107..961"
                     /note="isoform Tpm1.1st is encoded by transcript variant
                     Tpm1.1"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsi
//
LOCUS       NP_001170792             251 aa            linear   ROD 27-APR-2025
DEFINITION  tissue factor pathway inhibitor isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001170792
VERSION     NP_001170792.1
DBSOURCE    REFSEQ: accession NM_001177321.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Muto,M., Chakraborty,D., Varberg,K.M., Moreno-Irusta,A., Iqbal,K.,
            Scott,R.L., McNally,R.P., Choudhury,R.H., Aplin,J.D., Okae,H.,
            Arima,T., Matsumoto,S., Ema,M., Mast,A.E., Grundberg,E. and
            Soares,M.J.
  TITLE     Intersection of regulatory pathways controlling hemostasis and
            hemochorial placentation
  JOURNAL   Proc Natl Acad Sci U S A 118 (50) (2021)
   PUBMED   34876522
  REMARK    GeneRIF: Intersection of regulatory pathways controlling hemostasis
            and hemochorial placentation.
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Smith,S.A., Travers,R.J. and Morrissey,J.H.
  TITLE     How it all starts: Initiation of the clotting cascade
  JOURNAL   Crit Rev Biochem Mol Biol 50 (4), 326-336 (2015)
   PUBMED   26018600
  REMARK    Review article
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Parunov,L.A., Soshitova,N.P., Fadeeva,O.A., Balandina,A.N.,
            Kopylov,K.G., Kumskova,M.A., Gilbert,J.C., Schaub,R.G.,
            McGinness,K.E., Ataullakhanov,F.I. and Panteleev,M.A.
  TITLE     Drug-drug interaction of the anti-TFPI aptamer BAX499 and factor
            VIII: studies of spatial dynamics of fibrin clot formation in
            hemophilia A
  JOURNAL   Thromb Res 133 (1), 112-119 (2014)
   PUBMED   24263002
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Ogiwara,K., Nogami,K., Matsumoto,T. and Shima,M.
  TITLE     Tissue factor pathway inhibitor in activated prothrombin complex
            concentrates (aPCC) moderates the effectiveness of therapy in some
            severe hemophilia A patients with inhibitor
  JOURNAL   Int J Hematol 99 (5), 577-587 (2014)
   PUBMED   24687919
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Mukai,Y. and Sato,S.
  TITLE     Effect of nitric oxide deficiency on tissue-type plasminogen
            activator expression in the umbilical cord in a pregnancy-induced
            hypertension rat model
  JOURNAL   Pregnancy Hypertens 2 (1), 53-58 (2012)
   PUBMED   26104991
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Elsayed,Y.A., Nakagawa,K., Kamikubo,Y.I., Enjyoji,K.I., Kato,H. and
            Sueishi,K.
  TITLE     Effects of recombinant human tissue factor pathway inhibitor on
            thrombus formation and its in vivo distribution in a rat DIC model
  JOURNAL   Am J Clin Pathol 106 (5), 574-583 (1996)
   PUBMED   8929465
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Saito,M., Morishita,E., Asakura,H., Jokaji,H., Uotani,C.,
            Kumabashiri,I., Yamazaki,M., Aoshima,K. and Matsuda,T.
  TITLE     [Analysis of behaviors of plasma tissue factor and tissue factor
            pathway inhibitor in patients with various diseases]
  JOURNAL   Rinsho Ketsueki 37 (9), 794-798 (1996)
   PUBMED   8914465
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Kobayashi,M., Wada,H., Wakita,Y., Shimura,M., Nakase,T.,
            Hiyoyama,K., Nagaya,S., Minami,N., Nakano,T. and Shiku,H.
  TITLE     Decreased plasma tissue factor pathway inhibitor levels in patients
            with thrombotic thrombocytopenic purpura
  JOURNAL   Thromb Haemost 73 (1), 10-14 (1995)
   PUBMED   7740478
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Bregengard,C., Nordfang,O., Wildgoose,P., Svendsen,O., Hedner,U.
            and Diness,V.
  TITLE     The effect of two-domain tissue factor pathway inhibitor on
            endotoxin-induced disseminated intravascular coagulation in rabbits
  JOURNAL   Blood Coagul Fibrinolysis 4 (5), 699-706 (1993)
   PUBMED   8292719
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Enjyoji,K., Emi,M., Mukai,T. and Kato,H.
  TITLE     cDNA cloning and expression of rat tissue factor pathway inhibitor
            (TFPI)
  JOURNAL   J Biochem 111 (5), 681-687 (1992)
   PUBMED   1639767
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087020.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, 3' UTR,
            and 3' coding sequence compared to variant 1. The resulting isoform
            (2) has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087020.1, SRR8487226.142775.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676809 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..251
                     /product="tissue factor pathway inhibitor isoform 2
                     precursor"
                     /note="EPI; LACI; extrinsic pathway inhibitor;
                     lipoprotein-associated coagulation inhibitor"
                     /calculated_mol_wt=25477
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3140
     mat_peptide     29..251
                     /product="tissue factor pathway inhibitor isoform 2"
                     /calculated_mol_wt=25477
     Region          50..104
                     /region_name="Kunitz_TFPI1_1-like"
                     /note="Kunitz protease inhibitor (KPI) domain 1 (KPI-1 or
                     K1) of tissue factor pathway inhibitor (TFPI); cd22613"
                     /db_xref="CDD:438656"
     Site            order(51..52,62,64,66,68,83..90,92..95,98,101..102)
                     /site_type="other"
                     /note="antibody binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            order(59..68,82..87,92)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438656"
     Site            63..64
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02445.1)"
     Region          120..175
                     /region_name="Kunitz_TFPI1_2-like"
                     /note="Kunitz protease inhibitor (KPI) domain 2 (KPI-2 or
                     K2) of tissue factor pathway inhibitor (TFPI); cd22614"
                     /db_xref="CDD:438657"
     Site            order(132..136,155,157..158)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438657"
     Site            134..135
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02445.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02445.1)"
     CDS             1..251
                     /gene="Tfpi"
                     /coded_by="NM_001177321.1:161..916"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29436"
                     /db_xref="RGD:61914"
ORIGIN      
        1 mtnklkkdha fwaavcllls ivpellnalp eedddtintd selrpmkplh tfcamkaedg
       61 pckamirsyy fnmnshqcee fiyggcrgnk nrfdtleecr ktcipgykkt tikttsgaek
      121 pdfcfleedp gicrgfmtry fynnqskqce qfkyggclgn snnfetleec rntcedpvne
      181 vqkgdyvtnq itvtdrttvn nvvipqatka psqwvtkeet nggwknadct yqgslssfyi
      241 hvlgffvfri g
//
LOCUS       NP_001099995             504 aa            linear   ROD 27-APR-2025
DEFINITION  syntaphilin [Rattus norvegicus].
ACCESSION   NP_001099995 XP_001060677 XP_230716
VERSION     NP_001099995.1
DBSOURCE    REFSEQ: accession NM_001106525.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Salam,S., Tacconelli,S., Smith,B.N., Mitchell,J.C., Glennon,E.,
            Nikolaou,N., Houart,C. and Vance,C.
  TITLE     Identification of a novel interaction of FUS and syntaphilin may
            explain synaptic and mitochondrial abnormalities caused by ALS
            mutations
  JOURNAL   Sci Rep 11 (1), 13613 (2021)
   PUBMED   34193962
  REMARK    GeneRIF: Identification of a novel interaction of FUS and
            syntaphilin may explain synaptic and mitochondrial abnormalities
            caused by ALS mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Lin,M.Y., Cheng,X.T., Tammineni,P., Xie,Y., Zhou,B., Cai,Q. and
            Sheng,Z.H.
  TITLE     Releasing Syntaphilin Removes Stressed Mitochondria from Axons
            Independent of Mitophagy under Pathophysiological Conditions
  JOURNAL   Neuron 94 (3), 595-610 (2017)
   PUBMED   28472658
  REMARK    GeneRIF: Stressed mitochondria are removed from axons triggered by
            the bulk release of mitochondrial anchoring protein syntaphilin via
            a new class of mitochondria-derived cargos independent of Parkin,
            Drp1, and autophagy.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Lin,M.Y. and Sheng,Z.H.
  TITLE     Regulation of mitochondrial transport in neurons
  JOURNAL   Exp Cell Res 334 (1), 35-44 (2015)
   PUBMED   25612908
  REMARK    Review article
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Fong,K.W., Leung,J.W., Li,Y., Wang,W., Feng,L., Ma,W., Liu,D.,
            Songyang,Z. and Chen,J.
  TITLE     MTR120/KIAA1383, a novel microtubule-associated protein, promotes
            microtubule stability and ensures cytokinesis
  JOURNAL   J Cell Sci 126 (Pt 3), 825-837 (2013)
   PUBMED   23264731
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Su,Q., Cai,Q., Gerwin,C., Smith,C.L. and Sheng,Z.H.
  TITLE     Syntabulin is a microtubule-associated protein implicated in
            syntaxin transport in neurons
  JOURNAL   Nat Cell Biol 6 (10), 941-953 (2004)
   PUBMED   15459722
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Boczan,J., Leenders,A.G. and Sheng,Z.H.
  TITLE     Phosphorylation of syntaphilin by cAMP-dependent protein kinase
            modulates its interaction with syntaxin-1 and annuls its inhibitory
            effect on vesicle exocytosis
  JOURNAL   J Biol Chem 279 (18), 18911-18919 (2004)
   PUBMED   14985338
  REMARK    GeneRIF: syntaphilin was identified as a molecular clamp that
            controls free syntaxin-1 and dynamin-1 availability and thereby
            regulates synaptic vesicle exocytosis and endocytosis. PKA
            phosphorylation of syntaphilin decreases its binding to syntaxin-1A
            in vitro.
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Das,S., Gerwin,C. and Sheng,Z.H.
  TITLE     Syntaphilin binds to dynamin-1 and inhibits dynamin-dependent
            endocytosis
  JOURNAL   J Biol Chem 278 (42), 41221-41226 (2003)
   PUBMED   12896979
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Das,S., Boczan,J., Gerwin,C., Zald,P.B. and Sheng,Z.H.
  TITLE     Regional and developmental regulation of syntaphilin expression in
            the brain: a candidate molecular element of synaptic functional
            differentiation
  JOURNAL   Brain Res Mol Brain Res 116 (1-2), 38-49 (2003)
   PUBMED   12941459
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Lao,G., Scheuss,V., Gerwin,C.M., Su,Q., Mochida,S., Rettig,J. and
            Sheng,Z.H.
  TITLE     Syntaphilin: a syntaxin-1 clamp that controls SNARE assembly
  JOURNAL   Neuron 25 (1), 191-201 (2000)
   PUBMED   10707983
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC168917.1 and JAXUCZ010000003.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_230716.4, XP_001060677.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.19335.1,
                                           SRR26643293.19448.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..504
                     /product="syntaphilin"
                     /calculated_mol_wt=54363
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF41.1)"
     Region          20..329
                     /region_name="Syntaphilin"
                     /note="Golgi-localized syntaxin-1-binding clamp;
                     pfam15290"
                     /db_xref="CDD:464617"
     Region          191..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80U23; propagated from
                     UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80U23; propagated from
                     UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (B5DF41.1)"
     Site            437..456
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF41.1)"
     CDS             1..504
                     /gene="Snph"
                     /coded_by="NM_001106525.3:325..1839"
                     /db_xref="GeneID:296267"
                     /db_xref="RGD:1305867"
ORIGIN      
        1 mamslqgsrr asagsrrrts ppvsvrdayg taslssssns gsckgsdssp tprrsmkytl
       61 csdnhgikpp tpeqyltplq qkevcirhlk arlkdtqdrl qdrdteiddl ktqlsrmqed
      121 wieeechrve aqlalkeark eirqlkqvid tvknnlidkd kglqkyfvdi niqnkkletl
      181 lhsmevaqng vakeegtges aggsparslt rsstytklsd pavcgdrqag dpsntpaedr
      241 adsgfvaadd tlsrtealea ssllssgvdc gfeeaslhss fnlgprfpas ntyekllcgm
      301 eaavqascmq eraiqtdfvq yqpdlntile kvgqaqgcss vlkdrhseld lhpsgprdpd
      361 savvvtvgde peapepitrg paihrpavns npglpvsvvc pveeeeeaaa aaaaaaaatt
      421 tttttekepk sywsrhyivd llavvvpavp tvawlcrsqr rqgqpiynis sllrgcctva
      481 lhsirriscs lsqpsagssg gsql
//
LOCUS       NP_001093628             411 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic initiation factor 4A-III [Rattus norvegicus].
ACCESSION   NP_001093628 XP_001081786
VERSION     NP_001093628.1
DBSOURCE    REFSEQ: accession NM_001100158.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wang,Y., Zhang,Y., Qu,Y., Li,S., Xi,W., Liu,B. and Ye,L.
  TITLE     eIF4A3-mediated circEHMT1 regulation in retinal microvascular
            endothelial dysfunction in diabetic retinopathy
  JOURNAL   Microvasc Res 151, 104612 (2024)
   PUBMED   37839527
  REMARK    GeneRIF: eIF4A3-mediated circEHMT1 regulation in retinal
            microvascular endothelial dysfunction in diabetic retinopathy.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhan,X., Yan,C., Zhang,X., Lei,J. and Shi,Y.
  TITLE     Structure of a human catalytic step I spliceosome
  JOURNAL   Science 359 (6375), 537-545 (2018)
   PUBMED   29301961
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Favaro,F.P., Alvizi,L., Zechi-Ceide,R.M., Bertola,D., Felix,T.M.,
            de Souza,J., Raskin,S., Twigg,S.R., Weiner,A.M., Armas,P.,
            Margarit,E., Calcaterra,N.B., Andersen,G.R., McGowan,S.J.,
            Wilkie,A.O., Richieri-Costa,A., de Almeida,M.L. and
            Passos-Bueno,M.R.
  TITLE     A noncoding expansion in EIF4A3 causes Richieri-Costa-Pereira
            syndrome, a craniofacial disorder associated with limb defects
  JOURNAL   Am J Hum Genet 94 (1), 120-128 (2014)
   PUBMED   24360810
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Nguyen,L.S., Kim,H.G., Rosenfeld,J.A., Shen,Y., Gusella,J.F.,
            Lacassie,Y., Layman,L.C., Shaffer,L.G. and Gecz,J.
  TITLE     Contribution of copy number variants involving nonsense-mediated
            mRNA decay pathway genes to neuro-developmental disorders
  JOURNAL   Hum Mol Genet 22 (9), 1816-1825 (2013)
   PUBMED   23376982
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Barker-Haliski,M.L., Pastuzyn,E.D. and Keefe,K.A.
  TITLE     Expression of the core exon-junction complex factor eukaryotic
            initiation factor 4A3 is increased during spatial exploration and
            striatally-mediated learning
  JOURNAL   Neuroscience 226, 51-61 (2012)
   PUBMED   22982623
  REMARK    GeneRIF: These findings thus further implicate eIF4A3 as a key
            mediator of Arc protein mRNA availability underlying learning and
            memory processes in vivo
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Xia,Q., Kong,X.T., Zhang,G.A., Hou,X.J., Qiang,H. and Zhong,R.Q.
  TITLE     Proteomics-based identification of DEAD-box protein 48 as a novel
            autoantigen, a prospective serum marker for pancreatic cancer
  JOURNAL   Biochem Biophys Res Commun 330 (2), 526-532 (2005)
   PUBMED   15796914
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Tange,T.O., Nott,A. and Moore,M.J.
  TITLE     The ever-increasing complexities of the exon junction complex
  JOURNAL   Curr Opin Cell Biol 16 (3), 279-284 (2004)
   PUBMED   15145352
  REMARK    Review article
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Li,Q., Imataka,H., Morino,S., Rogers,G.W. Jr., Richter-Cook,N.J.,
            Merrick,W.C. and Sonenberg,N.
  TITLE     Eukaryotic translation initiation factor 4AIII (eIF4AIII) is
            functionally distinct from eIF4AI and eIF4AII
  JOURNAL   Mol Cell Biol 19 (11), 7336-7346 (1999)
   PUBMED   10523622
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CO559861.1 and
            BC105875.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001081786.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105875.1, SRR8487230.55187.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..411
                     /product="eukaryotic initiation factor 4A-III"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 48; ATP-dependent RNA helicase
                     DDX48; ATP-dependent RNA helicase eIF4A-3; eIF-4A-III"
                     /calculated_mol_wt=46710
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine, in Eukaryotic initiation factor
                     4A-III, N-terminally processed.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60842; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Region          35..411
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          38..66
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            order(40,56,58..62,65,83..90,187..188)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350803"
     Site            order(63,67,83,86,222..224,227)
                     /site_type="other"
                     /note="Mago interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     Site            order(106,150..151,154..155,174,177..179,201..202,
                     205..210,230..234)
                     /site_type="other"
                     /note="Barentsz interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     Site            order(114..116,142..143,163..166,169,172,197,200)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350803"
     Site            124
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60842; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Region          187..190
                     /region_name="DEAD box. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60843; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P38919; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q2.1)"
     CDS             1..411
                     /gene="Eif4a3"
                     /gene_synonym="eIF4A-III"
                     /coded_by="NM_001100158.2:61..1296"
                     /db_xref="GeneID:688288"
                     /db_xref="RGD:1591139"
ORIGIN      
        1 maatatmats gsarkrllke edmtkvefet seevdvtptf dtmglredll rgiyaygfek
       61 psaiqqraik qiikgrdvia qsqsgtgkta tfsisvlqcl diqvretqal ilaptrelav
      121 qiqkgllalg dymnvqchac iggtnvgedi rkldygqhvv agtpgrvfdm irrrslrtra
      181 ikmlvldead emlnkgfkeq iydvyrylpp atqvvlisat lpheilemtn kfmtdpiril
      241 vkrdeltleg ikqffvaver eewkfdtlcd lydtltitqa vifcntkrkv dwltekmrea
      301 nftvssmhgd mpqkeresim kefrsgasrv listdvwarg ldvpqvslii nydlpnnrel
      361 yihrigrsgr ygrkgvainf vknddirilr dieqyystqi dempmnvadl i
//
LOCUS       NP_001264161             313 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase Nek6 [Rattus norvegicus].
ACCESSION   NP_001264161
VERSION     NP_001264161.1
DBSOURCE    REFSEQ: accession NM_001277232.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Vaz Meirelles,G., Ferreira Lanza,D.C., da Silva,J.C., Santana
            Bernachi,J., Paes Leme,A.F. and Kobarg,J.
  TITLE     Characterization of hNek6 interactome reveals an important role for
            its short N-terminal domain and colocalization with proteins at the
            centrosome
  JOURNAL   J Proteome Res 9 (12), 6298-6316 (2010)
   PUBMED   20873783
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Rapley,J., Nicolas,M., Groen,A., Regue,L., Bertran,M.T.,
            Caelles,C., Avruch,J. and Roig,J.
  TITLE     The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a
            novel site necessary for mitotic spindle formation
  JOURNAL   J Cell Sci 121 (Pt 23), 3912-3921 (2008)
   PUBMED   19001501
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Yin,M.J., Shao,L., Voehringer,D., Smeal,T. and Jallal,B.
  TITLE     The serine/threonine kinase Nek6 is required for cell cycle
            progression through mitosis
  JOURNAL   J Biol Chem 278 (52), 52454-52460 (2003)
   PUBMED   14563848
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Belham,C., Roig,J., Caldwell,J.A., Aoyama,Y., Kemp,B.E., Comb,M.
            and Avruch,J.
  TITLE     A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the
            Nek6 and Nek7 kinases
  JOURNAL   J Biol Chem 278 (37), 34897-34909 (2003)
   PUBMED   12840024
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Hashimoto,Y., Akita,H., Hibino,M., Kohri,K. and Nakanishi,M.
  TITLE     Identification and characterization of Nek6 protein kinase, a
            potential human homolog of NIMA histone H3 kinase
  JOURNAL   Biochem Biophys Res Commun 293 (2), 753-758 (2002)
   PUBMED   12054534
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Belham,C., Comb,M.J. and Avruch,J.
  TITLE     Identification of the NIMA family kinases NEK6/7 as regulators of
            the p70 ribosomal S6 kinase
  JOURNAL   Curr Biol 11 (15), 1155-1167 (2001)
   PUBMED   11516946
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Kandli,M., Feige,E., Chen,A., Kilfin,G. and Motro,B.
  TITLE     Isolation and characterization of two evolutionarily conserved
            murine kinases (Nek6 and nek7) related to the fungal mitotic
            regulator, NIMA
  JOURNAL   Genomics 68 (2), 187-196 (2000)
   PUBMED   10964517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1 and BC160820.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC160820.1, SRR22399481.1188112.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..313
                     /product="serine/threonine-protein kinase Nek6"
                     /EC_number="2.7.11.34"
                     /note="nimA-related protein kinase 6; never in mitosis
                     A-related kinase 6; NIMA (never in mitosis gene a)-related
                     expressed kinase 6"
                     /calculated_mol_wt=35704
     Region          1..44
                     /region_name="Interaction with ARHGAP33, ANKRA2, CDC42,
                     PRDX3, RAD26L, RBBP6, RPS7 and TRIP4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Region          44..305
                     /region_name="STKc_Nek6_7"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Never In Mitosis gene A (NIMA)-related kinase 6 and 7;
                     cd08224"
                     /db_xref="CDD:270863"
     Site            order(51..55,59,72,74,106,122..125,129,131,172,174,
                     176..177,179,190,193,195,209..212)
                     /site_type="active"
                     /db_xref="CDD:270863"
     Site            order(51..52,54..55,59,72,74,106,123..125,129,177,179,195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270863"
     Site            order(55,129,131,172,174,176,193,209..212)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270863"
     Site            108
                     /site_type="other"
                     /note="Autoinhibitory. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P59895.1)"
     Site            189..212
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270863"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK9.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9HC98; propagated from
                     UniProtKB/Swiss-Prot (P59895.1)"
     Region          267..270
                     /region_name="Interaction with APBB1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P59895.1)"
     CDS             1..313
                     /gene="Nek6"
                     /coded_by="NM_001277232.1:74..1015"
                     /db_xref="GeneID:360161"
                     /db_xref="RGD:727779"
ORIGIN      
        1 magqpshmph ggspnhlchv lgpahppdpq rhpntlsfrc sladfqiekk igrgqfsevy
       61 katclldrkt valkkvqife mmdakarqdc vkeigllkql nhpniikyld sfiednelni
      121 vleladagdl sqmikyfkkq krlipertvw kyfvqlcsav ehmhsrrvmh rdikpanvfi
      181 tatgivklgd lglgrffsse ttaahslvgt pyymsperih engynfksdi wslgcllyem
      241 aalqspfygd kmnlfslcqk ieqcdypplp gehyseklre lvsmciypdp nhrpdieyvh
      301 qvakqmhvwt sst
//
LOCUS       NP_954521                308 aa            linear   ROD 27-APR-2025
DEFINITION  uridine diphosphate glucose pyrophosphatase NUDT22 [Rattus
            norvegicus].
ACCESSION   NP_954521 XP_215188
VERSION     NP_954521.1
DBSOURCE    REFSEQ: accession NM_199090.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Carter,M., Jemth,A.S., Carreras-Puigvert,J., Herr,P., Martinez
            Carranza,M., Vallin,K.S.A., Throup,A., Helleday,T. and Stenmark,P.
  TITLE     Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a
            Unique Structural Fold
  JOURNAL   Structure 26 (2), 295-303 (2018)
   PUBMED   29413322
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC060593.1.
            
            On Jan 1, 2004 this sequence version replaced XP_215188.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060593.1, FQ212766.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..308
                     /product="uridine diphosphate glucose pyrophosphatase
                     NUDT22"
                     /EC_number="3.6.1.45"
                     /note="nucleoside diphosphate-linked moiety X motif 22;
                     nudix motif 22; nudix (nucleoside diphosphate linked
                     moiety X)-type motif 22; UGPPase; UDPG pyrophosphatase"
                     /calculated_mol_wt=33361
     Region          174..195
                     /region_name="Nudix box.
                     /evidence=ECO:0000250|UniProtKB:Q9BRQ3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P9U1.1)"
     CDS             1..308
                     /gene="Nudt22"
                     /coded_by="NM_199090.2:120..1046"
                     /db_xref="GeneID:293703"
                     /db_xref="RGD:735224"
ORIGIN      
        1 mdpevslmll cppgglsqeq vsvelspahd rrplpegdkt itaiwetrlq aqpwifdapk
       61 frlhsatlas sspepqlllh lgltsyrdfl gtnwsssasw lrqqgatdwg dkqayladpl
      121 gvgaalvtad dflvflrrsq qvaeapglvd vpgghpepqa lcsgsipqhe dlpgelvvre
      181 lfssvlqevc devnlplhtl sqplllgiac netsagrasa efyvqcslts eevrnyylsg
      241 gpeanestgi ifvetqrvqr lqetemwaql cpsakgaill ynrhpplqsg agkshlshps
      301 vpalslql
//
LOCUS       NP_001164220             594 aa            linear   ROD 27-APR-2025
DEFINITION  ankyrin repeat and SOCS box protein 14 [Rattus norvegicus].
ACCESSION   NP_001164220 XP_001057650
VERSION     NP_001164220.1
DBSOURCE    REFSEQ: accession NM_001170749.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW919055.1, FM122942.1 and JAXUCZ010000016.1.
            
            On Jan 1, 2010 this sequence version replaced XP_001057650.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760386, SAMEA5760475
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..594
                     /product="ankyrin repeat and SOCS box protein 14"
                     /note="Ankyrin repeat and SOCS box-containing protein 14"
                     /calculated_mol_wt=65783
     Region          81..354
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          88..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(189,191,195..196,199..201,203..204,208,211,220,222,
                     224,228..229,232..234,236..237,241,244,253,255,257,
                     261..262,265..267,269..270,274,277)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          189..220
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          222..253
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          255..284
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          274..>453
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          323..360
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(326..327,330..332,334..335,339,342,360,362,364,
                     368..369,372..374,376..377,381,384,392,394,398..399,
                     402..404,406..407,411,414)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          362..392
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          394..420
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          423..453
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          536..592
                     /region_name="SOCS_ASB14"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB14-like proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. The
                     general function of the SOCS box is the recruitment of the
                     ubiquitin-transferase system; cd03730"
                     /db_xref="CDD:239700"
     Site            order(537..542,548,561,567,572)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239700"
     CDS             1..594
                     /gene="Asb14"
                     /coded_by="NM_001170749.1:113..1897"
                     /db_xref="GeneID:680076"
                     /db_xref="RGD:1596812"
ORIGIN      
        1 mklskrpmdq qssdedadtd fdtqiiiqqs lldaykpelt grtpedersq sfssedykki
       61 veaietgked alasfakyhp afdeangsgw lplhkaavql nknileitln askpsaweqt
      121 trngetplfl avsssllena hflllngcdp naknfegnsp lltavlkdsy dmatllinhg
      181 anvnlrcane rtalheaakl grqdmvklml ssganpdars sygftplala aqgghtetmq
      241 lllqkgadvh sqasdsssvl leavrggdpd svsllleyga danipkssgh lpihvaadkg
      301 hflalkvlvp vtdiaaikrs gisplhcaaa gahpqcldll iragfdvnfm ldqrvrkhyd
      361 dqrksalyfa vsngdlssvk lllsagalpn qdpvnclqia lrmgnyelin lllrhganvn
      421 yfcrvnplhf psalqytlkd evmlrmllny gydtercfdc phgervhrcc tfegwtstvi
      481 kdtmfcevit lswlqhlsgk vvrvmldyvd qvqicsklka vlekqklwpe ihviltnprs
      541 lqhlcrlkir kcmgrlrlrc pvfmsflplp nllkayvlyk eydlygqgss tgtr
//
LOCUS       NP_001164030             655 aa            linear   ROD 27-APR-2025
DEFINITION  versican core protein isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001164030
VERSION     NP_001164030.1
DBSOURCE    REFSEQ: accession NM_001170559.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Harten,I.A., Kaber,G., Agarwal,K.J., Kang,I., Ibarrientos,S.R.,
            Workman,G., Chan,C.K., Nivison,M.P., Nagy,N., Braun,K.R.,
            Kinsella,M.G., Merrilees,M.J. and Wight,T.N.
  TITLE     The synthesis and secretion of versican isoform V3 by mammalian
            cells: A role for N-linked glycosylation
  JOURNAL   Matrix Biol 89, 27-42 (2020)
   PUBMED   32001344
  REMARK    GeneRIF: The synthesis and secretion of versican isoform V3 by
            mammalian cells: A role for N-linked glycosylation.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Bogen,O., Bender,O., Alvarez,P., Kern,M., Tomiuk,S., Hucho,F. and
            Levine,J.D.
  TITLE     Expression of a novel versican variant in dorsal root ganglia from
            spared nerve injury rats
  JOURNAL   Mol Pain 15, 1744806919874557 (2019)
   PUBMED   31429356
  REMARK    GeneRIF: mRNAs of the versican gene with exon 8beta are predicted
            to be constitutively degraded by nonsense-mediated RNA decay.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Carthy,J.M., Abraham,T., Meredith,A.J., Boroomand,S. and
            McManus,B.M.
  TITLE     Versican localizes to the nucleus in proliferating mesenchymal
            cells
  JOURNAL   Cardiovasc Pathol 24 (6), 368-374 (2015)
   PUBMED   26395512
  REMARK    GeneRIF: Versican localizes to the nucleus in proliferating
            mesenchymal cells and suggest role in mitotic spindle organization
            during cell division.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Lemire,J.M., Merrilees,M.J., Braun,K.R. and Wight,T.N.
  TITLE     Overexpression of the V3 variant of versican alters arterial smooth
            muscle cell adhesion, migration, and proliferation in vitro
  JOURNAL   J Cell Physiol 190 (1), 38-45 (2002)
   PUBMED   11807809
  REMARK    GeneRIF: Overexpression of alternatively spliced V3 variant of
            versican alters arterial smooth muscle cell adhesion, migration,
            proliferation and cell shape
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Lemire,J.M., Braun,K.R., Maurel,P., Kaplan,E.D., Schwartz,S.M. and
            Wight,T.N.
  TITLE     Versican/PG-M isoforms in vascular smooth muscle cells
  JOURNAL   Arterioscler Thromb Vasc Biol 19 (7), 1630-1639 (1999)
   PUBMED   10397680
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Mjaatvedt,C.H., Yamamura,H., Capehart,A.A., Turner,D. and
            Markwald,R.R.
  TITLE     The Cspg2 gene, disrupted in the hdf mutant, is required for right
            cardiac chamber and endocardial cushion formation
  JOURNAL   Dev Biol 202 (1), 56-66 (1998)
   PUBMED   9758703
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Milev,P., Maurel,P., Chiba,A., Mevissen,M., Popp,S., Yamaguchi,Y.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Differential regulation of expression of hyaluronan-binding
            proteoglycans in developing brain: aggrecan, versican, neurocan,
            and brevican
  JOURNAL   Biochem Biophys Res Commun 247 (2), 207-212 (1998)
   PUBMED   9642104
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Pyke,C., Kristensen,P., Ostergaard,P.B., Oturai,P.S. and Romer,J.
  TITLE     Proteoglycan expression in the normal rat kidney
  JOURNAL   Nephron 77 (4), 461-470 (1997)
   PUBMED   9434070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF072892.1 and AY007691.1.
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons, compared to variant 1, resulting in a shorter protein
            (isoform 4, also referred to as V3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5756307, SAMEA5760383
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..655
                     /product="versican core protein isoform 4 precursor"
                     /note="versican core protein; GHAP; PG-M; large fibroblast
                     proteoglycan; glial hyaluronate-binding protein;
                     chondroitin sulfate proteoglycan core protein 2;
                     chondroitin sulfate proteoglycan 2 (versican)"
                     /calculated_mol_wt=72218
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          26..152
                     /region_name="Ig_Versican"
                     /note="Immunoglobulin (Ig)-like domain of the chondroitin
                     sulfate proteoglycan core protein (CSPG), versican;
                     cd05901"
                     /db_xref="CDD:409482"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409482"
     Region          32..34
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409482"
     Region          38..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409482"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          63..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409482"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409482"
     Region          101..106
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409482"
     Region          112..118
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409482"
     Region          126..133
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409482"
     Region          143..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409482"
     Region          150..244
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            160..161
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          251..346
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            258..259
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ERB4.2)"
     Region          350..384
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          386..422
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(386,389,403)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          428..551
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(522,526,528,534,536..539,542..544)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          555..611
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(565,585)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     CDS             1..655
                     /gene="Vcan"
                     /gene_synonym="Cspg2"
                     /coded_by="NM_001170559.1:281..2248"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:114122"
                     /db_xref="RGD:619940"
ORIGIN      
        1 mlinmngilw mcstllltha lhkakmeenp pvkgslsgkv ilpchfstlp tlppdyntse
       61 flrikwskie vdkngkdike ttvlvaqdgn ikigqdykgr vsvpthpddv gdasltmvkl
      121 rasdagvyrc dvmygiedtq ntmslavdgv vfhyraatsr ytlnfesaqq acldigavia
      181 tpeqlfaaye dgfeqcdagw lsdqtvrypi rapregcygd mmgkegvrty gfrspqetyd
      241 vycyvdhldg dvfhitapsk ftfeeaeaec anrdarlatv gelhaawrng fdqcdygwls
      301 dasvrhpvtv araqcgggll gvrtlyrfen qtcfplpdsr fdaycfkrpd lcktnpclng
      361 gtcyptetsy vctcapgysg dqceldfdec hsnpcrngat cvdglntfrc lclpsyvgal
      421 ceqdtetcdy gwhkfqgqcy kyfahrrtwd aaerecrlqg ahltsilshe eqmfvnrvgh
      481 dyqwiglndk mfehdfrwtd gsalqyenwr pnqpdsffsa gedcvviiwh engqwndvpc
      541 nyhltytckk gtvacgqppv venaktfgkm kpryeinsli ryhckdgfiq rhlptirclg
      601 ngrwampkit cmnpsayqrt yskkylknss svkdnsints khehrwsrrw qetrr
//
LOCUS       NP_071627                432 aa            linear   ROD 27-APR-2025
DEFINITION  neuropeptide FF receptor 1 [Rattus norvegicus].
ACCESSION   NP_071627
VERSION     NP_071627.2
DBSOURCE    REFSEQ: accession NM_022291.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Badgandi,H.B., Hwang,S.H., Shimada,I.S., Loriot,E. and
            Mukhopadhyay,S.
  TITLE     Tubby family proteins are adapters for ciliary trafficking of
            integral membrane proteins
  JOURNAL   J Cell Biol 216 (3), 743-760 (2017)
   PUBMED   28154160
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Jorgensen,S.R., Andersen,M.D., Overgaard,A. and Mikkelsen,J.D.
  TITLE     Changes in RFamide-related peptide-1 (RFRP-1)-immunoreactivity
            during postnatal development and the estrous cycle
  JOURNAL   Endocrinology 155 (11), 4402-4410 (2014)
   PUBMED   25144921
  REMARK    GeneRIF: Adult females, as compared with males, have significantly
            more RFRP-1-ir per cell, and these cells are regulated during the
            estrous cycle.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Gojska,N.M. and Belsham,D.D.
  TITLE     Glucocorticoid receptor-mediated regulation of Rfrp (GnIH) and
            Gpr147 (GnIH-R) synthesis in immortalized hypothalamic neurons
  JOURNAL   Mol Cell Endocrinol 384 (1-2), 23-31 (2014)
   PUBMED   24412804
  REMARK    GeneRIF: Rfrp (GnIH)-expressing neurons serve as potential upstream
            mediators of stress-induced effects through Gpr147
            (GnIH-R)-dependent mechanisms.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Sukhbaatar,U., Kanasaki,H., Mijiddorj,T., Oride,A. and Miyazaki,K.
  TITLE     Expression of gonadotropin-inhibitory hormone receptors in mouse
            pituitary gonadotroph LbetaT2 cells and hypothalamic
            gonadotropin-releasing hormone-producing GT1-7 cells
  JOURNAL   Endocr J 61 (1), 25-34 (2014)
   PUBMED   24088662
  REMARK    GeneRIF: two central controllers of reproductive function,
            gonadotropin-releasing hormone (GnRH) and kisspeptin, stimulate the
            expression of Gonadotropin-inhibitory hormone (GnIH) receptors in
            pituitary gonadotroph cells and hypothalamic GnRH neurons
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Kovacs,A., Laszlo,K., Galosi,R., Toth,K., Ollmann,T., Peczely,L.
            and Lenard,L.
  TITLE     Microinjection of RFRP-1 in the central nucleus of amygdala
            decreases food intake in the rat
  JOURNAL   Brain Res Bull 88 (6), 589-595 (2012)
   PUBMED   22691952
  REMARK    GeneRIF: RFRP-1 injected into the central nucleus of the rat
            amygdala decreases food intake. This is a NPFF-1 linked effect,
            because it could be prevented by NPFF-receptor antagonist RF9.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Quennell,J.H., Rizwan,M.Z., Relf,H.L. and Anderson,G.M.
  TITLE     Developmental and steroidogenic effects on the gene expression of
            RFamide related peptides and their receptor in the rat brain and
            pituitary gland
  JOURNAL   J Neuroendocrinol 22 (4), 309-316 (2010)
   PUBMED   20136694
  REMARK    GeneRIF: Developmental and steroidogenic effects on the gene
            expression of RFamide related peptides and their receptor in the
            rat brain and pituitary gland.
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Gouarderes,C., Puget,A. and Zajac,J.M.
  TITLE     Detailed distribution of neuropeptide FF receptors (NPFF1 and
            NPFF2) in the rat, mouse, octodon, rabbit, guinea pig, and marmoset
            monkey brains: a comparative autoradiographic study
  JOURNAL   Synapse 51 (4), 249-269 (2004)
   PUBMED   14696013
  REMARK    GeneRIF: The constant presence of NPFF1 receptors in the septum,
            the nucleus of the tractus solitarius, and the hypothalamus suggest
            its participation in neuroendocrine functions.
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Bonini,J.A., Jones,K.A., Adham,N., Forray,C., Artymyshyn,R.,
            Durkin,M.M., Smith,K.E., Tamm,J.A., Boteju,L.W., Lakhlani,P.P.,
            Raddatz,R., Yao,W.J., Ogozalek,K.L., Boyle,N., Kouranova,E.V.,
            Quan,Y., Vaysse,P.J., Wetzel,J.M., Branchek,T.A., Gerald,C. and
            Borowsky,B.
  TITLE     Identification and characterization of two G protein-coupled
            receptors for neuropeptide FF
  JOURNAL   J Biol Chem 275 (50), 39324-39331 (2000)
   PUBMED   11024015
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Hinuma,S., Shintani,Y., Fukusumi,S., Iijima,N., Matsumoto,Y.,
            Hosoya,M., Fujii,R., Watanabe,T., Kikuchi,K., Terao,Y., Yano,T.,
            Yamamoto,T., Kawamata,Y., Habata,Y., Asada,M., Kitada,C.,
            Kurokawa,T., Onda,H., Nishimura,O., Tanaka,M., Ibata,Y. and
            Fujino,M.
  TITLE     New neuropeptides containing carboxy-terminal RFamide and their
            receptor in mammals
  JOURNAL   Nat Cell Biol 2 (10), 703-708 (2000)
   PUBMED   11025660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Apr 14, 2010 this sequence version replaced NP_071627.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2273217.1,
                                           SRR26360194.1717379.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN14984027
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..432
                     /product="neuropeptide FF receptor 1"
                     /note="G-protein coupled receptor 147; RFamide-related
                     peptide receptor OT7T022"
                     /calculated_mol_wt=48175
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP86.1)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          44..342
                     /region_name="7tmA_NPFFR1"
                     /note="neuropeptide FF receptor 1, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15981"
                     /db_xref="CDD:320647"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          45..71
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320647"
     Region          78..104
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320647"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Site            order(100,103..104,116..121,123..124,127,170,172..176,213,
                     216..218,220..222,224..225,285,288..289,291..292,295,
                     309..310,312..314,317,320..321)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320647"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          116..146
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320647"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          157..178
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320647"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          213..242
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320647"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          265..295
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320647"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          310..335
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320647"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     Region          380..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP86.1)"
     CDS             1..432
                     /gene="Npffr1"
                     /gene_synonym="Gpr147; NPFF1; OT7T022"
                     /coded_by="NM_022291.2:9..1307"
                     /db_xref="GeneID:64107"
                     /db_xref="RGD:621570"
ORIGIN      
        1 meaepsqppn gswplgqngs dvetsiatsl tfssyyqhss pvaamfiaay vlifllcmvg
       61 ntlvcfivlk nrhmrtvtnm filnlavsdl lvgifcmptt lvdnlitgwp fdnatckmsg
      121 lvqgmsvsas vftlvaiave rfrcivhpfr ekltlrkalf tiaviwalal limcpsavtl
      181 tvtreehhfm ldarnrsypl yscweawpek gmrkvytavl fahiylvpla livvmyvria
      241 rklcqapgpa rdteeavaeg grtsrrrarv vhmlvmvalf ftlswlplwv llllidygel
      301 selqlhllsv yafplahwla ffhssanpii ygyfnenfrr gfqaafraql cwppwaahkq
      361 ayserpnrll rrrvvvdvqp sdsglpsesg pssgvpgpgr lplrngrvah qdgpgegpgc
      421 nhmpltipaw ni
//
LOCUS       NP_001099387             426 aa            linear   ROD 27-APR-2025
DEFINITION  actin-like protein 6B [Rattus norvegicus].
ACCESSION   NP_001099387 XP_001069085 XP_213739
VERSION     NP_001099387.2
DBSOURCE    REFSEQ: accession NM_001105917.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Bell,S., Rousseau,J., Peng,H., Aouabed,Z., Priam,P., Theroux,J.F.,
            Jefri,M., Tanti,A., Wu,H., Kolobova,I., Silviera,H.,
            Manzano-Vargas,K., Ehresmann,S., Hamdan,F.F., Hettige,N., Zhang,X.,
            Antonyan,L., Nassif,C., Ghaloul-Gonzalez,L., Sebastian,J.,
            Vockley,J., Begtrup,A.G., Wentzensen,I.M., Crunk,A., Nicholls,R.D.,
            Herman,K.C., Deignan,J.L., Al-Hertani,W., Efthymiou,S.,
            Salpietro,V., Miyake,N., Makita,Y., Matsumoto,N., Ostern,R.,
            Houge,G., Hafstrom,M., Fassi,E., Houlden,H., Klein
            Wassink-Ruiter,J.S., Nelson,D., Goldstein,A., Dabir,T., van
            Gils,J., Bourgeron,T., Delorme,R., Cooper,G.M., Martinez,J.E.,
            Finnila,C.R., Carmant,L., Lortie,A., Oegema,R., van Gassen,K.,
            Mehta,S.G., Huhle,D., Abou Jamra,R., Martin,S., Brunner,H.G.,
            Lindhout,D., Au,M., Graham,J.M. Jr., Coubes,C., Turecki,G.,
            Gravel,S., Mechawar,N., Rossignol,E., Michaud,J.L., Lessard,J.,
            Ernst,C. and Campeau,P.M.
  TITLE     Mutations in ACTL6B Cause Neurodevelopmental Deficits and Epilepsy
            and Lead to Loss of Dendrites in Human Neurons
  JOURNAL   Am J Hum Genet 104 (5), 815-834 (2019)
   PUBMED   31031012
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Singh,A.P. and Archer,T.K.
  TITLE     Analysis of the SWI/SNF chromatin-remodeling complex during early
            heart development and BAF250a repression cardiac gene transcription
            during P19 cell differentiation
  JOURNAL   Nucleic Acids Res 42 (5), 2958-2975 (2014)
   PUBMED   24335282
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Wei,X., Li,H., Miao,J., Liu,B., Zhan,Y., Wu,D., Zhang,Y., Wang,L.,
            Fan,Y., Gu,H., Wang,W. and Yuan,Z.
  TITLE     miR-9*- and miR-124a-Mediated switching of chromatin remodelling
            complexes is altered in rat spina bifida aperta
  JOURNAL   Neurochem Res 38 (8), 1605-1615 (2013)
   PUBMED   23677776
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Staahl,B.T., Tang,J., Wu,W., Sun,A., Gitler,A.D., Yoo,A.S. and
            Crabtree,G.R.
  TITLE     Kinetic analysis of npBAF to nBAF switching reveals exchange of
            SS18 with CREST and integration with neural developmental pathways
  JOURNAL   J Neurosci 33 (25), 10348-10361 (2013)
   PUBMED   23785148
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Shain,A.H. and Pollack,J.R.
  TITLE     The spectrum of SWI/SNF mutations, ubiquitous in human cancers
  JOURNAL   PLoS One 8 (1), e55119 (2013)
   PUBMED   23355908
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Kuroda,Y., Oma,Y., Nishimori,K., Ohta,T. and Harata,M.
  TITLE     Brain-specific expression of the nuclear actin-related protein
            ArpNalpha and its involvement in mammalian SWI/SNF chromatin
            remodeling complex
  JOURNAL   Biochem Biophys Res Commun 299 (2), 328-334 (2002)
   PUBMED   12437990
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Olave,I., Wang,W., Xue,Y., Kuo,A. and Crabtree,G.R.
  TITLE     Identification of a polymorphic, neuron-specific chromatin
            remodeling complex
  JOURNAL   Genes Dev 16 (19), 2509-2517 (2002)
   PUBMED   12368262
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Otsuki,T., Furukawa,Y., Ikeda,K., Endo,H., Yamashita,T.,
            Shinohara,A., Iwamatsu,A., Ozawa,K. and Liu,J.M.
  TITLE     Fanconi anemia protein, FANCA, associates with BRG1, a component of
            the human SWI/SNF complex
  JOURNAL   Hum Mol Genet 10 (23), 2651-2660 (2001)
   PUBMED   11726552
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Harata,M., Mochizuki,R. and Mizuno,S.
  TITLE     Two isoforms of a human actin-related protein show nuclear
            localization and mutually selective expression between brain and
            other tissues
  JOURNAL   Biosci Biotechnol Biochem 63 (5), 917-923 (1999)
   PUBMED   10380635
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473973.1.
            
            On Nov 20, 2009 this sequence version replaced NP_001099387.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760433
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..426
                     /product="actin-like protein 6B"
                     /note="BAF53B; BRG1-associated factor 53B; actin-like 6"
                     /calculated_mol_wt=46761
     Region          8..417
                     /region_name="ASKHA_NBD_Arp4_ACTL6-like"
                     /note="nucleotide-binding domain (NBD) of the
                     actin-related protein 4 (Arp4)-like subfamily; cd13395"
                     /db_xref="CDD:466846"
     Region          39..82
                     /region_name="Essential for mediating its function in
                     dendritic development, may contribute to neuronal-specific
                     targeting. /evidence=ECO:0000250|UniProtKB:Q99MR0"
                     /note="propagated from UniProtKB/Swiss-Prot (P86173.2)"
     CDS             1..426
                     /gene="Actl6b"
                     /gene_synonym="Actl6"
                     /coded_by="NM_001105917.1:81..1361"
                     /db_xref="GeneID:288563"
                     /db_xref="RGD:1307763"
ORIGIN      
        1 msggvyggde vgalvfdigs fsvragyage dcpkadfptt vgllaaeegg glelegekek
       61 kgkifhidtn alhvprdgae vmsplkngmi edwecfrail dhtyskhvks epnlhpvlms
      121 eapwntrakr ekltelmfeq ynipafflck tavltafang rstglvldsg athttaipvh
      181 dgyvlqqgiv ksplagdfis mqcrelfqem aidiippymi aakepvrega ppnwkkkekl
      241 pqvskswhny mcneviqdfq asvlqvsdsp ydeqvaaqmp tvhyempngy ntdygaerlr
      301 ipeglfdpsn vkglsgntml gvghvvttsi gmcdidirpg lygsvivtgg ntllqgftdr
      361 lnrelsqktp psmrlklias nstmerkfsp wiggsilasl gtfqqmwisk qeyeeggkqc
      421 verkcp
//
LOCUS       NP_001094358             525 aa            linear   ROD 27-APR-2025
DEFINITION  beta-galactoside alpha-2,6-sialyltransferase 2 [Rattus norvegicus].
ACCESSION   NP_001094358 XP_001058146 XP_236826
VERSION     NP_001094358.1
DBSOURCE    REFSEQ: accession NM_001100888.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Harduin-Lepers,A., Mollicone,R., Delannoy,P. and Oriol,R.
  TITLE     The animal sialyltransferases and sialyltransferase-related genes:
            a phylogenetic approach
  JOURNAL   Glycobiology 15 (8), 805-817 (2005)
   PUBMED   15843597
  REMARK    Erratum:[Glycobiology. 2005 Sep;15(9):21G]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Takashima,S., Tsuji,S. and Tsujimoto,M.
  TITLE     Comparison of the enzymatic properties of mouse beta-galactoside
            alpha2,6-sialyltransferases, ST6Gal I and II
  JOURNAL   J Biochem 134 (2), 287-296 (2003)
   PUBMED   12966079
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Takashima,S., Tsuji,S. and Tsujimoto,M.
  TITLE     Characterization of the second type of human beta-galactoside alpha
            2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta
            1,4GlcNAc structures on oligosaccharides preferentially. Genomic
            analysis of human sialyltransferase genes
  JOURNAL   J Biol Chem 277 (48), 45719-45728 (2002)
   PUBMED   12235148
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Feb 16, 2013 this sequence version replaced
            XP_236826.2, XP_001058146.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB605923.1, SRR26360194.2300751.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..525
                     /product="beta-galactoside alpha-2,6-sialyltransferase 2"
                     /EC_number="2.4.3.1"
                     /note="ST6Gal II; alpha 2,6-ST 2;
                     CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,
                     6-sialyltransferase 2; ST6 beta-galactosamide
                     alpha-2,6-sialyltranferase 2"
                     /calculated_mol_wt=59786
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q701R3.1)"
     Region          85..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q701R3.1)"
     Region          145..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q701R3.1)"
     Region          243..510
                     /region_name="GT29_ST6GAL2"
                     /note="beta-galactoside alpha-2,6-sialyltransferase 2;
                     cd23986"
                     /db_xref="CDD:467714"
     Site            order(296..298,319..320,341,431..433,451..452,461..463,
                     479)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:467714"
     Site            303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q701R3.1)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q701R3.1)"
     Site            521
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q701R3.1)"
     CDS             1..525
                     /gene="St6gal2"
                     /gene_synonym="ST6Gal-II; ST6GalII"
                     /coded_by="NM_001100888.1:223..1800"
                     /db_xref="GeneID:301155"
                     /db_xref="RGD:1559663"
ORIGIN      
        1 mkphlkqwrq rmlfaifvwg llflaifiyf tnsnpaapmp ssfsflesrg llpvqgkqrv
       61 imgalqepsl prslepskvl mdghsaspfn swpgdpqkgd qaqdgfdngd efftsqvgrk
      121 sqsafypeed nyffvagqpg lyhhrqgalg lpspgesswq sgpgqpkqek lrhprrgslp
      181 eeaydsdmls tsmsraflyr lwkgtvsskm lnprlqkamr yymsfnkhgv rfsrrgrrea
      241 rrtgpellce mrkrvrvrtl dgkeapfsgl gwrplvpgvp lsqlhprglr scavvmsaga
      301 ilnsslgeei dshdavlrfn saptrgyekd vgnkttvrii nsqilanpsh hfidsslykd
      361 vilvawdpap ysanlnlwyk kpdynlftpy iqhrlkyptq pfyilhpkfi wqlwdiiqen
      421 trekiqpnpp ssgfigilvm msmcqevhvy eyipsvrqte lchyhelyyd aactlgayhp
      481 llyekllvqr lntgtqadlh hkgkvvlpgf qtlrcpvtrp nntnt
//
LOCUS       NP_775172                307 aa            linear   ROD 27-APR-2025
DEFINITION  hepatitis A virus cellular receptor 1 homolog precursor [Rattus
            norvegicus].
ACCESSION   NP_775172 XP_213280
VERSION     NP_775172.1
DBSOURCE    REFSEQ: accession NM_173149.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Obaid,A.A., Almasmoum,H., Almaimani,R.A., El-Boshy,M., Aslam,A.,
            Idris,S., Ghaith,M.M., El-Readi,M.Z., Ahmad,J., Farrash,W.F.,
            Mujalli,A., Eid,S.Y., Elzubier,M.E. and Refaat,B.
  TITLE     Vitamin D and calcium co-therapy mitigates pre-established cadmium
            nephropathy by regulating renal calcium homeostatic molecules and
            improving anti-oxidative and anti-inflammatory activities in rat
  JOURNAL   J Trace Elem Med Biol 79, 127221 (2023)
   PUBMED   37244046
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Ramdin,S., Naicker,T., Baijnath,S. and Govender,N.
  TITLE     Kidney injury molecule-1 and podocalyxin dysregulation in an
            arginine vasopressin induced rodent model of preeclampsia
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 284, 58-65 (2023)
   PUBMED   36934678
  REMARK    GeneRIF: Kidney injury molecule-1 and podocalyxin dysregulation in
            an arginine vasopressin induced rodent model of preeclampsia.
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Edosuyi,O., Choi,M., Edosuyi,V., Igbe,I. and Oyekan,A.
  TITLE     Malate reduced kidney injury molecule (KIM-1) expression and
            selectively upregulated the renal nitric oxide production in
            obstructive nephropathy
  JOURNAL   Bratisl Lek Listy 124 (2), 151-157 (2023)
   PUBMED   36598304
  REMARK    GeneRIF: Malate reduced kidney injury molecule (KIM-1) expression
            and selectively upregulated the renal nitric oxide production in
            obstructive nephropathy.
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wang,T., Dai,L., Shen,S., Yang,Y., Yang,M., Yang,X., Qiu,Y. and
            Wang,W.
  TITLE     Comprehensive Molecular Analyses of a Macrophage-Related Gene
            Signature With Regard to Prognosis, Immune Features, and Biomarkers
            for Immunotherapy in Hepatocellular Carcinoma Based on WGCNA and
            the LASSO Algorithm
  JOURNAL   Front Immunol 13, 843408 (2022)
   PUBMED   35693827
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Li,X., Chen,S., Feng,D., Fu,Y., Wu,H., Lu,J. and Bao,J.
  TITLE     Calcium-sensing receptor promotes calcium oxalate crystal adhesion
            and renal injury in Wistar rats by promoting ROS production and
            subsequent regulation of PS ectropion, OPN, KIM-1, and ERK
            expression
  JOURNAL   Ren Fail 43 (1), 465-476 (2021)
   PUBMED   33678127
  REMARK    GeneRIF: Calcium-sensing receptor promotes calcium oxalate crystal
            adhesion and renal injury in Wistar rats by promoting ROS
            production and subsequent regulation of PS ectropion, OPN, KIM-1,
            and ERK expression.
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Graves,P.E., Siroux,V., Guerra,S., Klimecki,W.T. and Martinez,F.D.
  TITLE     Association of atopy and eczema with polymorphisms in T-cell
            immunoglobulin domain and mucin domain-IL-2-inducible T-cell kinase
            gene cluster in chromosome 5 q 33
  JOURNAL   J Allergy Clin Immunol 116 (3), 650-656 (2005)
   PUBMED   16159638
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Khademi,M., Illes,Z., Gielen,A.W., Marta,M., Takazawa,N.,
            Baecher-Allan,C., Brundin,L., Hannerz,J., Martin,C., Harris,R.A.,
            Hafler,D.A., Kuchroo,V.K., Olsson,T., Piehl,F. and Wallstrom,E.
  TITLE     T Cell Ig- and mucin-domain-containing molecule-3 (TIM-3) and TIM-1
            molecules are differentially expressed on human Th1 and Th2 cells
            and in cerebrospinal fluid-derived mononuclear cells in multiple
            sclerosis
  JOURNAL   J Immunol 172 (11), 7169-7176 (2004)
   PUBMED   15153541
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Kuehn,E.W., Park,K.M., Somlo,S. and Bonventre,J.V.
  TITLE     Kidney injury molecule-1 expression in murine polycystic kidney
            disease
  JOURNAL   Am J Physiol Renal Physiol 283 (6), F1326-F1336 (2002)
   PUBMED   12388382
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Han,W.K., Bailly,V., Abichandani,R., Thadhani,R. and Bonventre,J.V.
  TITLE     Kidney Injury Molecule-1 (KIM-1): a novel biomarker for human renal
            proximal tubule injury
  JOURNAL   Kidney Int 62 (1), 237-244 (2002)
   PUBMED   12081583
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Ichimura,T., Bonventre,J.V., Bailly,V., Wei,H., Hession,C.A.,
            Cate,R.L. and Sanicola,M.
  TITLE     Kidney injury molecule-1 (KIM-1), a putative epithelial cell
            adhesion molecule containing a novel immunoglobulin domain, is
            up-regulated in renal cells after injury
  JOURNAL   J Biol Chem 273 (7), 4135-4142 (1998)
   PUBMED   9461608
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF035963.1.
            
            On Jan 12, 2005 this sequence version replaced XP_213280.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF035963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680445, SAMN09345331
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..307
                     /product="hepatitis A virus cellular receptor 1 homolog
                     precursor"
                     /note="hepatitis A virus cellular receptor 1 homolog;
                     TIMD-1; HAVcr-1; t cell immunoglobulin and mucin
                     domain-containing protein 1; kidney injury molecule 1"
                     /calculated_mol_wt=31752
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2230
     mat_peptide     22..307
                     /product="Hepatitis A virus cellular receptor 1 homolog.
                     /id=PRO_0000014983"
                     /note="propagated from UniProtKB/Swiss-Prot (O54947.1)"
                     /calculated_mol_wt=31752
     Region          25..127
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          33..37
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          47..51
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          91..95
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          105..110
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..123
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          129..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54947.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O54947.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O54947.1)"
     CDS             1..307
                     /gene="Havcr1"
                     /gene_synonym="KIM-1; Kim1"
                     /coded_by="NM_173149.2:601..1524"
                     /db_xref="GeneID:286934"
                     /db_xref="RGD:708425"
ORIGIN      
        1 mvqlqvfisg lllllpgsvd syevvkgvvg hpvtipctys trggitttcw grgqcpyssc
       61 qniliwtngy qvtyrssgry nikgrisegd vsltiensvd sdsglyccrv eipgwfndqk
      121 mtfslevkpe iptspptrpt ttrptttrpt tistrsthvp tstrvststp tpeqtqthkp
      181 eittfyahet taevtetpsy tpadwngtvt sseeawnnht vriplrkpqr nptkgfyvgm
      241 svaallllll astvvvtryi iirkkmgsls fvafhvsksr alqnaaivhp raedniyiie
      301 drsrgae
//
LOCUS       NP_445790                307 aa            linear   ROD 27-APR-2025
DEFINITION  GTP-binding protein RAD [Rattus norvegicus].
ACCESSION   NP_445790
VERSION     NP_445790.2
DBSOURCE    REFSEQ: accession NM_053338.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Oda,T., Niikura,T., Fukui,T., Arakura,M., Oe,K., Mifune,Y.,
            Hayashi,S., Matsumoto,T., Matsushita,T. and Kuroda,R.
  TITLE     Ras associated with diabetes may play a role in fracture nonunion
            development in rats
  JOURNAL   BMC Musculoskelet Disord 20 (1), 602 (2019)
   PUBMED   31830958
  REMARK    GeneRIF: expression increased significantly in the nonunions,
            compared to that in the standard healing fractures, at
            post-fracture days 14, 21, and 28
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Zhang,J., Chang,L., Chen,C., Zhang,M., Luo,Y., Hamblin,M.,
            Villacorta,L., Xiong,J.W., Chen,Y.E., Zhang,J. and Zhu,X.
  TITLE     Rad GTPase inhibits cardiac fibrosis through connective tissue
            growth factor
  JOURNAL   Cardiovasc Res 91 (1), 90-98 (2011)
   PUBMED   21382976
  REMARK    GeneRIF: Rad GTPase inhibits cardiac fibrosis through connective
            tissue growth factor in failing hearts.
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Sun,Z., Zhang,J., Zhang,J., Chen,C., Du,Q., Chang,L., Cao,C.,
            Zheng,M., Garcia-Barrio,M.T., Chen,Y.E., Xiao,R.P., Mao,J. and
            Zhu,X.
  TITLE     Rad GTPase induces cardiomyocyte apoptosis through the activation
            of p38 mitogen-activated protein kinase
  JOURNAL   Biochem Biophys Res Commun 409 (1), 52-57 (2011)
   PUBMED   21549102
  REMARK    GeneRIF: Rad-triggered apoptosis was mediated by the activation of
            p38 MAPK.
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Luo,Y., Zhang,M., Zhang,J., Zhang,J., Chen,C., Chen,Y.E.,
            Xiong,J.W. and Zhu,X.
  TITLE     Platelet-derived growth factor induces Rad expression through Egr-1
            in vascular smooth muscle cells
  JOURNAL   PLoS One 6 (4), e19408 (2011)
   PUBMED   21559360
  REMARK    GeneRIF: Rad is regulated by PDGF through the transcriptional
            factor Egr-1 in RASMCs
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Wang,G., Zhu,X., Xie,W., Han,P., Li,K., Sun,Z., Wang,Y., Chen,C.,
            Song,R., Cao,C., Zhang,J., Wu,C., Liu,J. and Cheng,H.
  TITLE     Rad as a novel regulator of excitation-contraction coupling and
            beta-adrenergic signaling in heart
  JOURNAL   Circ Res 106 (2), 317-327 (2010)
   PUBMED   19926875
  REMARK    GeneRIF: Results establish Rad as a novel endogenous regulator of
            cardiac EC coupling and betaAR signaling and support a parsimonious
            model in which Rad buffers Ca(v)beta to modulate LCC activity, EC
            coupling, and betaAR responsiveness.
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Yada,H., Murata,M., Shimoda,K., Yuasa,S., Kawaguchi,H., Ieda,M.,
            Adachi,T., Murata,M., Ogawa,S. and Fukuda,K.
  TITLE     Dominant negative suppression of Rad leads to QT prolongation and
            causes ventricular arrhythmias via modulation of L-type Ca2+
            channels in the heart
  JOURNAL   Circ Res 101 (1), 69-77 (2007)
   PUBMED   17525370
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Ilany,J., Bilan,P.J., Kapur,S., Caldwell,J.S., Patti,M.E.,
            Marette,A. and Kahn,C.R.
  TITLE     Overexpression of Rad in muscle worsens diet-induced insulin
            resistance and glucose intolerance and lowers plasma triglyceride
            level
  JOURNAL   Proc Natl Acad Sci U S A 103 (12), 4481-4486 (2006)
   PUBMED   16537411
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Wang,G.Y., Niu,T.H., Chen,C.Z., Li,Q.F. and Xu,X.P.
  TITLE     A novel Rad gene polymorphism combined with obesity increases risk
            for type 2 diabetes mellitus
  JOURNAL   Chin Med J (Engl) 117 (5), 770-771 (2004)
   PUBMED   15161552
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Yuan,X., Yamada,K., Ishiyama-Shigemoto,S., Koyama,W. and Nonaka,K.
  TITLE     Analysis of trinucleotide-repeat combination polymorphism at the
            rad gene in patients with type 2 diabetes mellitus
  JOURNAL   Metabolism 48 (2), 173-175 (1999)
   PUBMED   10024077
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Caldwell,J.S., Moyers,J.S., Doria,A., Reynet,C. and Kahn,R.C.
  TITLE     Molecular cloning of the human rad gene: gene structure and
            complete nucleotide sequence
  JOURNAL   Biochim Biophys Acta 1316 (3), 145-148 (1996)
   PUBMED   8781531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM054321.1, CK602305.1, FM055705.1 and CK840773.1.
            
            On Aug 4, 2012 this sequence version replaced NP_445790.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U12187.1, EV767675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p14"
     Protein         1..307
                     /product="GTP-binding protein RAD"
                     /EC_number="3.6.5.2"
                     /note="RAD1; ras associated with diabetes; Ras-related
                     associated with diabetes"
                     /calculated_mol_wt=33151
     Region          91..307
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            97..104
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(98..99,145..146)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(99..105,143,146,202..203,205,232..233)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(104..105,117,119,126..127,140..141,143,145..146,234)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(118..119,124..127)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(118..123,124..126)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            120
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            143..146
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(145..146,154..157,160..163)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            202..205
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            232..234
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Site            301..304
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..307
                     /gene="Rrad"
                     /coded_by="NM_053338.2:173..1096"
                     /db_xref="GeneID:83521"
                     /db_xref="RGD:69357"
ORIGIN      
        1 mtlnggsgag gsrsagrerd rrrgstpwgp applhrrsmp vderdlqaal tpgslaataa
       61 gtrtqgqrld wpegssdsls sgdsgsedgv ykvlllgapg vgksalarif ggiedgpeae
      121 aaghtydrsi tvdgeeaslm vydiweqdgg cwlpghcmam gdayvivysi tdkgsfekas
      181 elrvqlrrar qtdnvpiilv gnksdlvrsr evsvdegrac avvfdckfie tsaalhhnvq
      241 alfegvvrqi rlrrdskedn arrqagtrrr eslgkkakrf lgrivarnsr kmafraksks
      301 chdlsvl
//
LOCUS       NP_445958                445 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3A [Rattus norvegicus].
ACCESSION   NP_445958
VERSION     NP_445958.1
DBSOURCE    REFSEQ: accession NM_053506.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, CB735595.1 and
            BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform H3A (also known as H3L or H3(445)),
            which contains 7 transmembrane domains.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB015646.1, AY009370.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132268
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..445
                     /product="histamine H3 receptor isoform H3A"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=48457
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          48..423
                     /region_name="7tmA_Histamine_H3R"
                     /note="histamine receptor subtypes H3R and H3R-like,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15296"
                     /db_xref="CDD:320423"
     Region          69..96
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320423"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          107..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320423"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Site            order(110,114..115,118..119,190,199,202..203,206,371,
                     374..375,378,394,398,402)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320423"
     Region          152..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320423"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320423"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          234..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          286..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          351..381
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320423"
     Site            360..380
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          391..416
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320423"
     Site            397..417
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58406; propagated from
                     UniProtKB/Swiss-Prot (Q9QYN8.1)"
     CDS             1..445
                     /gene="Hrh3"
                     /coded_by="NM_053506.2:338..1675"
                     /note="isoform H3A is encoded by transcript variant 1"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhrygvgea gpgveageaa lgggsgggaa
      301 asptsssgss srgterprsl krgskpsass aslekrmkmv sqsitqrfrl srdkkvaksl
      361 aiivsifglc wapytllmii raachgrcip dywyetsfwl lwansavnpv lyplchysfr
      421 raftkllcpq klkvqphgsl eqcwk
//
LOCUS       NP_001258203             403 aa            linear   ROD 27-APR-2025
DEFINITION  motor neuron and pancreas homeobox 1 [Rattus norvegicus].
ACCESSION   NP_001258203 XP_001059733 XP_003749718
VERSION     NP_001258203.1
DBSOURCE    REFSEQ: accession NM_001271274.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Desai,S.S., Modali,S.D., Parekh,V.I., Kebebew,E. and Agarwal,S.K.
  TITLE     GSK-3beta protein phosphorylates and stabilizes HLXB9 protein in
            insulinoma cells to form a targetable mechanism of controlling
            insulinoma cell proliferation
  JOURNAL   J Biol Chem 289 (9), 5386-5398 (2014)
   PUBMED   24425879
  REMARK    GeneRIF: Both pHLXB9 and active GSK-3beta are elevated in beta
            cells with menin knockdown, in MEN1-associated beta cell tumors
            (insulinomas)
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Kelly,C.E., Thymiakou,E., Dixon,J.E., Tanaka,S., Godwin,J. and
            Episkopou,V.
  TITLE     Rnf165/Ark2C enhances BMP-Smad signaling to mediate motor axon
            extension
  JOURNAL   PLoS Biol 11 (4), e1001538 (2013)
   PUBMED   23610558
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Cho,A., Ko,H.W. and Eggenschwiler,J.T.
  TITLE     FKBP8 cell-autonomously controls neural tube patterning through a
            Gli2- and Kif3a-dependent mechanism
  JOURNAL   Dev Biol 321 (1), 27-39 (2008)
   PUBMED   18590716
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Lee,S., Lee,B., Joshi,K., Pfaff,S.L., Lee,J.W. and Lee,S.K.
  TITLE     A regulatory network to segregate the identity of neuronal subtypes
  JOURNAL   Dev Cell 14 (6), 877-889 (2008)
   PUBMED   18539116
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Winseck,A.K. and Oppenheim,R.W.
  TITLE     An in vivo analysis of Schwann cell programmed cell death in
            embryonic mice: the role of axons, glial growth factor, and the
            pro-apoptotic gene Bax
  JOURNAL   Eur J Neurosci 24 (8), 2105-2117 (2006)
   PUBMED   17042795
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Yang,X., Arber,S., William,C., Li,L., Tanabe,Y., Jessell,T.M.,
            Birchmeier,C. and Burden,S.J.
  TITLE     Patterning of muscle acetylcholine receptor gene expression in the
            absence of motor innervation
  JOURNAL   Neuron 30 (2), 399-410 (2001)
   PUBMED   11395002
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Li,H., Arber,S., Jessell,T.M. and Edlund,H.
  TITLE     Selective agenesis of the dorsal pancreas in mice lacking homeobox
            gene Hlxb9
  JOURNAL   Nat Genet 23 (1), 67-70 (1999)
   PUBMED   10471501
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Arber,S., Han,B., Mendelsohn,M., Smith,M., Jessell,T.M. and
            Sockanathan,S.
  TITLE     Requirement for the homeobox gene Hb9 in the consolidation of motor
            neuron identity
  JOURNAL   Neuron 23 (4), 659-674 (1999)
   PUBMED   10482234
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474057.1.
            
            On or before Sep 13, 2012 this sequence version replaced
            XP_001059733.1, XP_003749718.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760434,
                              SAMN12840114 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..403
                     /product="motor neuron and pancreas homeobox 1"
                     /note="homeobox gene HB9; motor neuron and pancreas
                     homeobox protein 1; homeobox protein HB9"
                     /calculated_mol_wt=41053
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P50219; propagated from
                     UniProtKB/Swiss-Prot (M0R6D8.2)"
     Region          32..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R6D8.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50219; propagated from
                     UniProtKB/Swiss-Prot (M0R6D8.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50219; propagated from
                     UniProtKB/Swiss-Prot (M0R6D8.2)"
     Region          242..298
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          299..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (M0R6D8.2)"
     CDS             1..403
                     /gene="Mnx1"
                     /gene_synonym="Hlxb9"
                     /coded_by="NM_001271274.1:38..1249"
                     /db_xref="GeneID:682076"
                     /db_xref="RGD:1588091"
ORIGIN      
        1 meksknfrid allavdppra astqsaplal vtslaatpsg pgrggsgggg tssgasrscs
       61 passeataap gdrlraesps pprlltahca llpkpgflga gggggaaggp gtphhhahpg
      121 aaaaaaaaaa aaaagglalg lhpggaqgga glpaqaalyg hpvysysaaa aaaalagqhp
      181 alsysypqvq gahpahpadp iklgagtfql dqwlrastag milpkmpdfs sqaqsnllgk
      241 crrprtafts qqllelehqf klnkylsrpk rfevatslml tetqvkiwfq nrrmkwkrsk
      301 kakeqaaqea ekqkgsggga gkggteekte eellgppvsg dkasgrrlrd lrdsdpdede
      361 ddeedhfpys ngvgahaass dcsseddspp prpggpghqp lpq
//
LOCUS       NP_074047                485 aa            linear   ROD 27-APR-2025
DEFINITION  NGFI-A-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_074047
VERSION     NP_074047.2
DBSOURCE    REFSEQ: accession NM_022856.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Mager,G.M., Ward,R.M., Srinivasan,R., Jang,S.W., Wrabetz,L. and
            Svaren,J.
  TITLE     Active gene repression by the Egr2.NAB complex during peripheral
            nerve myelination
  JOURNAL   J Biol Chem 283 (26), 18187-18197 (2008)
   PUBMED   18456662
  REMARK    GeneRIF: Egr2 directly represses genes during myelination in
            conjunction with NAB corepressors
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Le,N., Nagarajan,R., Wang,J.Y., Svaren,J., LaPash,C., Araki,T.,
            Schmidt,R.E. and Milbrandt,J.
  TITLE     Nab proteins are essential for peripheral nervous system
            myelination
  JOURNAL   Nat Neurosci 8 (7), 932-940 (2005)
   PUBMED   16136673
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Snyder-Keller,A., Chandra,R., Lin,Y. and Mitchell,E.S.
  TITLE     Basal EGR-1 (zif268, NGFI-A, Krox-24) expression in developing
            striatal patches: role of dopamine and glutamate
  JOURNAL   Brain Res 958 (2), 297-304 (2002)
   PUBMED   12470865
  REMARK    GeneRIF: NGFI-A protein expression in the developing striatum
            appears to be driven first by dopaminergic afferents, and then
            later in development by excitatory glutamatergic afferents.
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Swirnoff,A.H., Apel,E.D., Svaren,J., Sevetson,B.R., Zimonjic,D.B.,
            Popescu,N.C. and Milbrandt,J.
  TITLE     Nab1, a corepressor of NGFI-A (Egr-1), contains an active
            transcriptional repression domain
  JOURNAL   Mol Cell Biol 18 (1), 512-524 (1998)
   PUBMED   9418898
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Svaren,J., Sevetson,B.R., Apel,E.D., Zimonjic,D.B., Popescu,N.C.
            and Milbrandt,J.
  TITLE     NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by
            proliferative and differentiative stimuli
  JOURNAL   Mol Cell Biol 16 (7), 3545-3553 (1996)
   PUBMED   8668170
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Russo,M.W., Sevetson,B.R. and Milbrandt,J.
  TITLE     Identification of NAB1, a repressor of NGFI-A- and Krox20-mediated
            transcription
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 6873-6877 (1995)
   PUBMED   7624335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Aug 11, 2009 this sequence version replaced NP_074047.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.31526.1,
                                           SRR26643290.32365.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..485
                     /product="NGFI-A-binding protein 1"
                     /note="EGR-1-binding protein 1"
                     /calculated_mol_wt=53895
     Region          4..82
                     /region_name="NCD1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62722.2)"
     Region          5..83
                     /region_name="NCD1"
                     /note="NAB conserved region 1 (NCD1); pfam04904"
                     /db_xref="CDD:461473"
     Region          160..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62722.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q62722.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q62722.2)"
     Region          189..317
                     /region_name="NCD2"
                     /note="NAB conserved region 2 (NCD2); pfam04905"
                     /db_xref="CDD:461474"
     Region          220..309
                     /region_name="NCD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62722.2)"
     Region          321..484
                     /region_name="Nab1"
                     /note="Conserved region in Nab1; pfam04902"
                     /db_xref="CDD:461472"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13506; propagated from
                     UniProtKB/Swiss-Prot (Q62722.2)"
     Region          391..422
                     /region_name="Necessary for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62722.2)"
     Region          398..431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62722.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61122; propagated from
                     UniProtKB/Swiss-Prot (Q62722.2)"
     CDS             1..485
                     /gene="Nab1"
                     /coded_by="NM_022856.5:198..1655"
                     /db_xref="GeneID:64824"
                     /db_xref="RGD:70882"
ORIGIN      
        1 matalprtlg elqlyrilqk anllsyfdaf iqqggddvqq lceageeefl eimalvgmas
       61 kplhvrrlqk alrdwvtnpg lfnqpltslp vssipiyklp egsptwlgis cnsyersssa
      121 rephlkvpkc aattcvqslg qgksevgsla lqsvsesrlw qghhtteseh slspadlgsp
      181 aspkesseal daaaalsvae cvermaptlp ksdlnevkel lknnkklakm ighifemsde
      241 dphkeeeirk ysaiygrfds krkdgkhltl heltvneaaa qlcvkdnall trrdelfala
      301 rqvsrevtyk ytyrttrlkc gerdelspkr ikmedgfpdf qesvptlfqq arakseelag
      361 lssqaekgma kqmellcaqa gyerlqqerr lmaglyrqss geqspdgglp sdgsdgqger
      421 plnlripsvq nrqphhfvvd gelsrlysne vkshsseslg ilkdyphsaf tlekkvikte
      481 pedsr
//
LOCUS       NP_067728                416 aa            linear   ROD 27-APR-2025
DEFINITION  plasminogen activator inhibitor 2 type A [Rattus norvegicus].
ACCESSION   NP_067728
VERSION     NP_067728.1
DBSOURCE    REFSEQ: accession NM_021696.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Longstaff,C. and Kolev,K.
  TITLE     Basic mechanisms and regulation of fibrinolysis
  JOURNAL   J Thromb Haemost 13 Suppl 1, S98-S105 (2015)
   PUBMED   26149056
  REMARK    Review article
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Xiao,Y., Li,H., Bunn,C. and Bartold,P.M.
  TITLE     The expression of plasminogen activator system in a rat model of
            periodontal wound healing
  JOURNAL   J Periodontol 72 (7), 849-857 (2001)
   PUBMED   11495131
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Bohn,H., Winckler,W. and Grundmann,U.
  TITLE     Immunochemically detected placental proteins and their biological
            functions
  JOURNAL   Arch Gynecol Obstet 249 (3), 107-118 (1991)
   PUBMED   1772263
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X64563.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X64563.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13p11"
     Protein         1..416
                     /product="plasminogen activator inhibitor 2 type A"
                     /note="PAI-2; serpin peptidase inhibitor, clade B
                     (ovalbumin), member 2; serpin B2; serine (or cysteine)
                     peptidase inhibitor, clade B, member 2; serine (or
                     cysteine) proteinase inhibitor, clade B, member 2"
                     /calculated_mol_wt=47117
     Region          2..416
                     /region_name="serpinB2_PAI-2"
                     /note="serpin family B member 2, plasminogen activator
                     inhibitor 2; cd19562"
                     /db_xref="CDD:381029"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29524.1)"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29524.1)"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29524.1)"
     Site            364..394
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381029"
     Site            381..382
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P29524.1)"
     Site            402
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29524.1)"
     CDS             1..416
                     /gene="Serpinb2"
                     /gene_synonym="Pai2a"
                     /coded_by="NM_021696.2:24..1274"
                     /db_xref="GeneID:60325"
                     /db_xref="RGD:621823"
ORIGIN      
        1 meelsmantm falnllkqie qsnstqnifi spwsisstla ivflgaqant eeqmakvlnf
       61 dkigsydltp gnpenfhgcd faqhiqrdny pvailqaqar dkihsafssl sstintprlg
      121 dyllesankl fgeksarfke eyiqrckkyy stepeavdfl ecanearkki nswvktqtkg
      181 eipnllpegs vdedtkmvlv ntiyfkgrwk tpfqkrlngl ypfrvnlnes kpvqmmylre
      241 klnigyikdl ktqilelpyi gnismflllp deiedsstgl emlereinfd nfnkwisket
      301 ldeddvlvyi pkfklaqnye lkpilqrmgm edafnkgkad fsgmsesndl flsevfhqat
      361 vdvneegtva aggtgavmtg rtghggpqfv adhpflffim nnitrtilfv grfssp
//
LOCUS       NP_001008831             255 aa            linear   ROD 27-APR-2025
DEFINITION  rano class II histocompatibility antigen, B alpha chain precursor
            [Rattus norvegicus].
ACCESSION   NP_001008831
VERSION     NP_001008831.1
DBSOURCE    REFSEQ: accession NM_001008831.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Kozuka,R., Enomoto,M., Sato-Matsubara,M., Yoshida,K., Motoyama,H.,
            Hagihara,A., Fujii,H., Uchida-Kobayashi,S., Morikawa,H., Tamori,A.,
            Kawada,N. and Murakami,Y.
  TITLE     Association between HLA-DQA1/DRB1 polymorphism and development of
            hepatocellular carcinoma during entecavir treatment
  JOURNAL   J Gastroenterol Hepatol 34 (5), 937-946 (2019)
   PUBMED   30160782
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Karra,V.K., Chowdhury,S.J., Ruttala,R., Gumma,P.K., Polipalli,S.K.,
            Chakravarti,A. and Kar,P.
  TITLE     HLA-DQA1 & DQB1 variants associated with hepatitis B virus-related
            chronic hepatitis, cirrhosis & hepatocellular carcinoma
  JOURNAL   Indian J Med Res 147 (6), 573-580 (2018)
   PUBMED   30168489
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Shen,J., Shi,S. and Lai,Z.
  TITLE     Identification of HLA-DQA1 as a Susceptibility Gene for Spinal
            Tuberculosis by Exome Sequencing
  JOURNAL   Med Sci Monit 24, 3442-3449 (2018)
   PUBMED   29795056
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Ishibashi,M., Yamaguchi,H., Hirotani,Y., Sakurada,A., Endo,T.,
            Sugitani,M., Takayama,T., Makishima,M. and Esumi,M.
  TITLE     Contradictory intrahepatic immune responses activated in high-load
            hepatitis C virus livers compared with low-load livers
  JOURNAL   Arch Virol 163 (4), 855-865 (2018)
   PUBMED   29248968
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Gray,L.A., D'Antoine,H.A., Tong,S.Y.C., McKinnon,M., Bessarab,D.,
            Brown,N., Remenyi,B., Steer,A., Syn,G., Blackwell,J.M., Inouye,M.
            and Carapetis,J.R.
  TITLE     Genome-Wide Analysis of Genetic Risk Factors for Rheumatic Heart
            Disease in Aboriginal Australians Provides Support for Pathogenic
            Molecular Mimicry
  JOURNAL   J Infect Dis 216 (11), 1460-1470 (2017)
   PUBMED   29029143
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Syha,J., Henkes,W. and Reske,K.
  TITLE     Complete cDNA sequence coding for the MHC class II RT1.B alpha
            chain of the Lewis rat
  JOURNAL   Nucleic Acids Res 17 (10), 3985 (1989)
   PUBMED   2499874
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Henkes,W. and Reske,K.
  TITLE     Translation in Xenopus laevis oocytes of hybrid selected LEW rat
            RT1.B alpha- and beta-chain transcripts results in serologically
            discrete class II polypeptide chain complexes
  JOURNAL   Mol Immunol 26 (2), 171-179 (1989)
   PUBMED   2465490
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Barran,P.A. and McMaster,W.R.
  TITLE     DNA sequence analysis of the rat RT1.B alpha gene
  JOURNAL   Immunogenetics 26 (1-2), 56-62 (1987)
   PUBMED   3610254
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Wallis,A.E. and McMaster,W.R.
  TITLE     Sequence of a cDNA coding for a rat class II A alpha chain:
            extensive DNA and protein sequence identity to H-2 A alpha and
            HLA-DC1 alpha chains
  JOURNAL   Immunogenetics 19 (1), 53-62 (1984)
   PUBMED   6319276
REFERENCE   10 (residues 1 to 255)
  AUTHORS   McMaster,W.R.
  TITLE     Purification and molecular cloning of rat Ia antigens
  JOURNAL   Methods Enzymol 108, 558-581 (1984)
   PUBMED   6084802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883043.1 and BC086448.1.
            
            On Jan 5, 2005 this sequence version replaced XP_228005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ225365.1, FQ233598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..255
                     /product="rano class II histocompatibility antigen, B
                     alpha chain precursor"
                     /note="RT1 class II antigen, Ba chain; Rano class II
                     histocompatibility antigen, B alpha chain; activated B
                     cell RT1Bl alpha chain; MHC class II antigen RT1.B alpha
                     chain; RT1-B alpha; MHC class I antigen"
                     /calculated_mol_wt=26158
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2098
     Region          30..109
                     /region_name="MHC_II_alpha"
                     /note="Class II histocompatibility antigen, alpha domain;
                     pfam00993"
                     /db_xref="CDD:460019"
     Region          111..205
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          129..133
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          144..148
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          175..179
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          186..191
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          201..204
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..255
                     /gene="RT1-Ba"
                     /gene_synonym="BA1"
                     /coded_by="NM_001008831.3:63..830"
                     /db_xref="GeneID:309621"
                     /db_xref="RGD:1595867"
ORIGIN      
        1 mplsralilg vlalttmlsp cggqddiead hvaayginmy qyyesrgqyt hefdgdeefy
       61 vdldkketiw ripefgqlts fdpqgglqei atakynleil mksnstpatn kvpeatvfsk
      121 spvllgqpnt licfvdnifp painitwlrn skpvtegtfe tsflsnpdhs fhkmayltfi
      181 psnddiydck vehwgldepv lkhwepeipa pmseltetvv calglsvglv givvgtifii
      241 qglrsggpsr hpgpl
//
LOCUS       NP_036703                413 aa            linear   ROD 27-APR-2025
DEFINITION  aspartate aminotransferase, cytoplasmic [Rattus norvegicus].
ACCESSION   NP_036703
VERSION     NP_036703.2
DBSOURCE    REFSEQ: accession NM_012571.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wei,X.B., Jiang,W.Q., Zeng,J.H., Huang,L.Q., Ding,H.G., Jing,Y.W.,
            Han,Y.L., Li,Y.C. and Chen,S.L.
  TITLE     Exosome-Derived lncRNA NEAT1 Exacerbates Sepsis-Associated
            Encephalopathy by Promoting Ferroptosis Through Regulating
            miR-9-5p/TFRC and GOT1 Axis
  JOURNAL   Mol Neurobiol 59 (3), 1954-1969 (2022)
   PUBMED   35038133
  REMARK    GeneRIF: Exosome-Derived lncRNA NEAT1 Exacerbates Sepsis-Associated
            Encephalopathy by Promoting Ferroptosis Through Regulating
            miR-9-5p/TFRC and GOT1 Axis.
            Erratum:[Mol Neurobiol. 2022 Aug;59(8):5252. doi:
            10.1007/s12035-022-02931-2. PMID: 35727437]
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Athmouni,K., Belhaj,D., El Feki,A. and Ayadi,H.
  TITLE     Optimization, antioxidant properties and GC-MS analysis of
            Periploca angustifolia polysaccharides and chelation therapy on
            cadmium-induced toxicity in human HepG2 cells line and rat liver
  JOURNAL   Int J Biol Macromol 108, 853-862 (2018)
   PUBMED   29101047
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Wang,C., Chen,H. and Ying,W.
  TITLE     Cytosolic aspartate aminotransferase mediates the mitochondrial
            membrane potential and cell survival by maintaining the calcium
            homeostasis of BV2 microglia
  JOURNAL   Neuroreport 29 (2), 99-105 (2018)
   PUBMED   29215467
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Li,J., Ghazwani,M., Liu,K., Huang,Y., Chang,N., Fan,J., He,F.,
            Li,L., Bu,S., Xie,W., Ma,X. and Li,S.
  TITLE     Regulation of hepatic stellate cell proliferation and activation by
            glutamine metabolism
  JOURNAL   PLoS One 12 (8), e0182679 (2017)
   PUBMED   28797105
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Laloy,J., Lozano,O., Alpan,L., Mejia,J., Toussaint,O., Masereel,B.,
            Dogne,J.M. and Lucas,S.
  TITLE     Can TiC nanoparticles produce toxicity in oral administration to
            rats?
  JOURNAL   Toxicol Rep 1, 172-187 (2014)
   PUBMED   28962237
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Sato,A., Nagai,M., Tagami,A., Natori,Y. and Okada,M.
  TITLE     Effect of pyridoxine-deficiency on degradation of cytosolic
            aspartate aminotransferase in rat liver lysosomes
  JOURNAL   J Nutr Sci Vitaminol (Tokyo) 37 (4), 419-424 (1991)
   PUBMED   1765846
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Yasue,M., Serikawa,T. and Yamada,J.
  TITLE     Chromosomal assignments of 23 biochemical loci of the rat by using
            rat x mouse somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 57 (2-3), 142-148 (1991)
   PUBMED   1914521
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Doyle,J.M., Schinina,M.E., Bossa,F. and Doonan,S.
  TITLE     The amino acid sequence of cytosolic aspartate aminotransferase
            from human liver
  JOURNAL   Biochem J 270 (3), 651-657 (1990)
   PUBMED   2241899
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Watazu,Y., Uji,Y., Sugiuchi,H., Okabe,H. and Murao,S.
  TITLE     New automated measurement of mitochondrial aspartate
            aminotransferase with use of protease 401
  JOURNAL   Clin Chem 36 (4), 687-689 (1990)
   PUBMED   2182221
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Pave-Preux,M., Aggerbeck,M., Veyssier,C., Bousquet-Lemercier,B.,
            Hanoune,J. and Barouki,R.
  TITLE     Hormonal discrimination among transcription start sites of
            aspartate aminotransferase
  JOURNAL   J Biol Chem 265 (8), 4444-4448 (1990)
   PUBMED   2307672
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK600227.1, FM055803.1, CB578328.1, FN802619.1 and
            JAXUCZ010000001.1.
            
            On Aug 16, 2012 this sequence version replaced NP_036703.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061877.1, J04171.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..413
                     /product="aspartate aminotransferase, cytoplasmic"
                     /EC_number="2.6.1.1"
                     /EC_number="2.6.1.3"
                     /note="cytosolic aspartate aminotransferase; transaminase
                     A; glutamate oxaloacetate transaminase 1, soluble;
                     cysteine transaminase, cytoplasmic; cysteine
                     aminotransferase, cytoplasmic; aspartate aminotransferase
                     1; glutamic-oxaloacetic transaminase 1, soluble"
                     /calculated_mol_wt=46298
     Region          5..411
                     /region_name="PTZ00376"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:240390"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P13221.3)"
     Site            order(108..110,141,195,226,256,258..259,267)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(111,151,219,265..267,303,306)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P13221.3)"
     Site            259
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     CDS             1..413
                     /gene="Got1"
                     /gene_synonym="AAT1; ASAT; Aspat; cAspAT; cCAT; Gaspat"
                     /coded_by="NM_012571.2:86..1327"
                     /db_xref="GeneID:24401"
                     /db_xref="RGD:2721"
ORIGIN      
        1 mappsffaqv pqappvlvfk liadfrddpd prkvnlgvga yrtddsqpwv lpvvrkveqk
       61 iandhslnhe ylpilglaef rscasqlvlg dnspalrenr vggvqslggt galrigadfl
      121 grwyngtdnk ntpvyvsspt wenhngvfsa agfkdirsyr ywdaekrgld lqgflndlen
      181 apefsifvlh acahnptgtd pteeewkqia avmkrrflfp ffdsayqgfa sgdlekdawa
      241 iryfvsegfe lfcaqsfskn fglynervgn ltvvgkehds vlrvlsqmek ivritwsnpp
      301 aqgarivatt lsnpelfkew kgnvktmadr iltmrselra rlealktpgt wshiteqigm
      361 fsftglnpkq veylvnekhi ylmpsgrinm cglttknldy vatsineavt kfq
//
LOCUS       NP_001020571             238 aa            linear   ROD 27-APR-2025
DEFINITION  survival of motor neuron-related-splicing factor 30 [Rattus
            norvegicus].
ACCESSION   NP_001020571 XP_213506
VERSION     NP_001020571.1
DBSOURCE    REFSEQ: accession NM_001025400.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097986.1, BC098697.1, CV106705.1 and CB726049.1.
            
            On Jul 15, 2005 this sequence version replaced XP_213506.3.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097986.1, SRR8487227.156098.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..238
                     /product="survival of motor neuron-related-splicing factor
                     30"
                     /note="survival motor neuron domain-containing protein 1"
                     /calculated_mol_wt=26652
     Region          73..128
                     /region_name="Tudor_SPF30"
                     /note="Tudor domain found in survival of motor
                     neuron-related-splicing factor 30 (SPF30) and similar
                     proteins; cd20399"
                     /db_xref="CDD:410470"
     Site            order(83,88,90,108,111,113)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410470"
     Region          142..160
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU6.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75940; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU6.1)"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75940; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU6.1)"
     CDS             1..238
                     /gene="Smndc1"
                     /coded_by="NM_001025400.3:30..746"
                     /db_xref="GeneID:287768"
                     /db_xref="RGD:1309151"
ORIGIN      
        1 msedlakqla sykaqlqqve aalsgngene dllklkkdlq evieltkdll stqpsetlts
       61 sdsfastqpt hswkvgdkcm avwsedgqcy eaeieeidee ngtaaitfav ygnaevtpll
      121 nlkpveegrk akedsgnkpm skkemiaqqr eykkkkalkk aqrikeleqe redqkvkwqq
      181 fnnraysknk kgqvkrsifa spesvtgkvg vgtcgiadkp mtqyqdtsky nvrhlmpq
//
LOCUS       NP_001257785             189 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform c [Rattus norvegicus].
ACCESSION   NP_001257785
VERSION     NP_001257785.1
DBSOURCE    REFSEQ: accession NM_001270856.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC092646.1.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (c) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213134.1, FQ212976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..189
                     /product="stathmin-4 isoform c"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=21956
     Region          49..183
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     Region          168..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63043.1)"
     CDS             1..189
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_001270856.1:180..749"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyeadtv dlnwcvisdm evielnkcts
       61 gqsfevilkp psfdgvpefn aslprrrdps leeiqkklea aeerrkyqea ellkhlaekr
      121 ehereviqka ieennnfikm akeklaqkme snkenreahl aamlerlqek dkhaeevrkn
      181 kelkeeasr
//
LOCUS       NP_620805                456 aa            linear   ROD 27-APR-2025
DEFINITION  ribonuclease inhibitor isoform b [Rattus norvegicus].
ACCESSION   NP_620805 XP_002728885 XP_002728886 XP_002728887
VERSION     NP_620805.2
DBSOURCE    REFSEQ: accession NM_139105.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhao,C., Ni,Y., Liu,Y., Liu,T., Yang,S., Liu,Z. and Liu,S.
  TITLE     Identification and distribution of rRNH1, a gene upregulated after
            spinal cord primary neuron injury
  JOURNAL   In Vitro Cell Dev Biol Anim 50 (3), 183-187 (2014)
   PUBMED   24288130
  REMARK    GeneRIF: RNH1 protein is upregulated after spinal cord injury.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhao,C.F., Liu,Y., Que,H.P., Yang,S.G., Liu,T., Liu,Z.Q., Hui,H.D.
            and Liu,S.
  TITLE     Rnh1 promotes differentiation and myelination via RhoA in
            oligodendrocytes
  JOURNAL   Cell Tissue Res 353 (3), 381-389 (2013)
   PUBMED   23624614
  REMARK    GeneRIF: Rnh1-mediated RhoA inactivation enhances the
            differentiation and myelination in oligodendrocytes.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Kawanomoto,M., Motojima,K., Sasaki,M., Hattori,H. and Goto,S.
  TITLE     cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue
            distribution of the mRNA
  JOURNAL   Biochim Biophys Acta 1129 (3), 335-338 (1992)
   PUBMED   1536887
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Shapiro,R. and Vallee,B.L.
  TITLE     Human placental ribonuclease inhibitor abolishes both angiogenic
            and ribonucleolytic activities of angiogenin
  JOURNAL   Proc Natl Acad Sci U S A 84 (8), 2238-2241 (1987)
   PUBMED   3470787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC070501.1.
            
            On or before Feb 13, 2011 this sequence version replaced
            XP_002728885.1, XP_002728886.1, XP_002728887.1, NP_620805.1.
            
            Transcript Variant: This variant (2) has an alternate exon in place
            of the first exon compared to variant 1. The resulting isoform (b)
            is shorter at the N-terminus compared to isoform a. Variants 2 and
            3 both encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070501.1, SRR22399489.1080245.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..456
                     /product="ribonuclease inhibitor isoform b"
                     /note="ribonuclease inhibitor"
                     /calculated_mol_wt=49788
     Region          1..320
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P10775; propagated from
                     UniProtKB/Swiss-Prot (P29315.2)"
     Region          2..24
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(3,5,8,10,25,28,30,33,35,53,56,58,61,63,82,85,87,90,
                     92,110,113,115,118,120,139,142,144,147,149,167,170,172,
                     175,177,196,199,201,204,206,224,227,229,232,234,253,256,
                     258,261,263,281,284,286,289,291,310,313,315,318,320)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          15..43
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          25..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(31..32,89,146,174,231,257,259,285,314)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          44..71
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          53..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          72..100
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          82..109
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13489; propagated from
                     UniProtKB/Swiss-Prot (P29315.2)"
     Region          101..128
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          110..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..157
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          139..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..185
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          167..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..214
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          196..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          215..242
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          224..252
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..271
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          253..273
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          272..299
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          <277..>419
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          281..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          300..328
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          329..356
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          338..366
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          357..385
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          367..394
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          386..413
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          414..442
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     CDS             1..456
                     /gene="Rnh1"
                     /gene_synonym="Rnh"
                     /coded_by="NM_139105.3:134..1504"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:100360501"
                     /db_xref="RGD:621398"
ORIGIN      
        1 msldiqceql sdarwtellp liqqyqvvrl ddcgltevrc kdirsaiqan paltelslrt
       61 nelgdagvgl vlqglqnptc kiqklslqnc slteagcgvl pdvlrslstl relhlndnpl
      121 gdeglkllce glrdpqcrle klqleycnlt atsceplasv lrvkpdfkel vlsnndfhea
      181 gihtlcqglk dsacqleslk lencgitsan ckdlcdvvas kaslqeldlg snklgntgia
      241 alcsglllps crlrtlwlwd cdvtaegckd lcrvlrakqs lkelslagne lkdegaqllc
      301 esllepgcql eslwvktcsl taascphfcs vltknrslfe lqmssnplgd sgvvelckal
      361 gypdtvlrvl wlgdcdvtds gcsslatvll anrslreldl snncmgdtgv lqlleslkqp
      421 scalqqlvly diywtdeved qlraleeerp slriis
//
LOCUS       NP_758836                245 aa            linear   ROD 27-APR-2025
DEFINITION  collagen triple helix repeat-containing protein 1 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_758836
VERSION     NP_758836.1
DBSOURCE    REFSEQ: accession NM_172333.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zhu,B., Ekman,M., Svensson,D., Lindvall,J.M., Nilsson,B.O.,
            Uvelius,B. and Sward,K.
  TITLE     Array profiling reveals contribution of Cthrc1 to growth of the
            denervated rat urinary bladder
  JOURNAL   Am J Physiol Renal Physiol 314 (5), F893-F905 (2018)
   PUBMED   29357417
  REMARK    GeneRIF: Cthrc1 has role in bladder growth following denervation.
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Zhang,Q., Yin,Z.S., Zhang,F.W., Cao,K. and Sun,H.Y.
  TITLE     CTHRC1 mediates IL-1beta-induced apoptosis in chondrocytes via
            JNK1/2 signaling
  JOURNAL   Int J Mol Med 41 (4), 2270-2278 (2018)
   PUBMED   29393342
  REMARK    GeneRIF: CTHRC1 downregulation suppresses IL-1beta-induced JNK1/2
            activation.
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Wang,C., Gu,W., Sun,B., Zhang,Y., Ji,Y., Xu,X. and Wen,Y.
  TITLE     CTHRC1 promotes osteogenic differentiation of periodontal ligament
            stem cells by regulating TAZ
  JOURNAL   J Mol Histol 48 (4), 311-319 (2017)
   PUBMED   28647773
  REMARK    GeneRIF: Overexpression of CHTRC1 increased osteogenic
            differentiation of periodontal ligament stem cells, which could be
            abolished by TAZ siRNA.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Kimura,H., Kwan,K.M., Zhang,Z., Deng,J.M., Darnay,B.G.,
            Behringer,R.R., Nakamura,T., de Crombrugghe,B. and Akiyama,H.
  TITLE     Cthrc1 is a positive regulator of osteoblastic bone formation
  JOURNAL   PLoS One 3 (9), e3174 (2008)
   PUBMED   18779865
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Yamamoto,S., Nishimura,O., Misaki,K., Nishita,M., Minami,Y.,
            Yonemura,S., Tarui,H. and Sasaki,H.
  TITLE     Cthrc1 selectively activates the planar cell polarity pathway of
            Wnt signaling by stabilizing the Wnt-receptor complex
  JOURNAL   Dev Cell 15 (1), 23-36 (2008)
   PUBMED   18606138
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Leclair,R.J., Wang,Q., Benson,M.A., Prudovsky,I. and Lindner,V.
  TITLE     Intracellular localization of Cthrc1 characterizes differentiated
            smooth muscle
  JOURNAL   Arterioscler Thromb Vasc Biol 28 (7), 1332-1338 (2008)
   PUBMED   18467647
  REMARK    GeneRIF: Intracellular localization of Cthrc1 characterizes
            differentiated smooth muscle.
REFERENCE   9  (residues 1 to 245)
  AUTHORS   LeClair,R.J., Durmus,T., Wang,Q., Pyagay,P., Terzic,A. and
            Lindner,V.
  TITLE     Cthrc1 is a novel inhibitor of transforming growth factor-beta
            signaling and neointimal lesion formation
  JOURNAL   Circ Res 100 (6), 826-833 (2007)
   PUBMED   17322174
  REMARK    GeneRIF: Cthrc1 is a cell-type-specific inhibitor of transforming
            growth factor-beta, which in turn impacts collagen type I and III
            deposition, neointimal formation, and dedifferentiation of smooth
            muscle cells.
            Erratum:[Circ Res. 2012 May 11;110(10):e72]
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Pyagay,P., Heroult,M., Wang,Q., Lehnert,W., Belden,J., Liaw,L.,
            Friesel,R.E. and Lindner,V.
  TITLE     Collagen triple helix repeat containing 1, a novel secreted protein
            in injured and diseased arteries, inhibits collagen expression and
            promotes cell migration
  JOURNAL   Circ Res 96 (2), 261-268 (2005)
   PUBMED   15618538
  REMARK    GeneRIF: CTHRC1 is transiently expressed in the arterial wall in
            response to injury where it may contribute to vascular remodeling
            by limiting collagen matrix deposition and promoting cell
            migration.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY136824.1, SRR26643294.29101.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680414
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..245
                     /product="collagen triple helix repeat-containing protein
                     1 isoform 1 precursor"
                     /note="collagen triple helix repeat-containing protein 1"
                     /calculated_mol_wt=23086
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3356
     mat_peptide     33..245
                     /product="Collagen triple helix repeat-containing protein
                     1. /id=PRO_0000021040"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG08.1)"
                     /calculated_mol_wt=23086
     Region          <59..91
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          64..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CG08.1)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CG08.1)"
     CDS             1..245
                     /gene="Cthrc1"
                     /coded_by="NM_172333.2:115..852"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:282836"
                     /db_xref="RGD:628801"
ORIGIN      
        1 mhpqgraasp qlllglflvl llllqlsaps sasenpkvkq kalirqrevv dlyngmclqg
       61 pagvpgrdgs pgangipgtp gipgrdgfkg ekgeclresf eeswtpnykq cswsslnygi
      121 dlgkiaectf tkmrsnsalr vlfsgslrlk crnaccqrwy ftfngaecsg plpieaiiyl
      181 dqgspelnst inihrtssve glcegigagl vdvaiwvgtc sdypkgdast gwnsvsriii
      241 eelpk
//
LOCUS       NP_001041321             256 aa            linear   ROD 27-APR-2025
DEFINITION  swi5-dependent recombination DNA repair protein 1 homolog [Rattus
            norvegicus].
ACCESSION   NP_001041321 XP_001069953 XP_001070047 XP_215260
VERSION     NP_001041321.2
DBSOURCE    REFSEQ: accession NM_001047856.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Feng,Y., Singleton,D., Guo,C., Gardner,A., Pakala,S., Kumar,R.,
            Jensen,E., Zhang,J. and Khan,S.
  TITLE     DNA homologous recombination factor SFR1 physically and
            functionally interacts with estrogen receptor alpha
  JOURNAL   PLoS One 8 (7), e68075 (2013)
   PUBMED   23874500
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Yuan,J. and Chen,J.
  TITLE     The role of the human SWI5-MEI5 complex in homologous recombination
            repair
  JOURNAL   J Biol Chem 286 (11), 9888-9893 (2011)
   PUBMED   21252223
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Akamatsu,Y. and Jasin,M.
  TITLE     Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair
            through homologous recombination
  JOURNAL   PLoS Genet 6 (10), e1001160 (2010)
   PUBMED   20976249
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM118556.1 and JAXUCZ010000001.1.
            
            On Mar 4, 2011 this sequence version replaced NP_001041321.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ214391.1, FM118556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..256
                     /product="swi5-dependent recombination DNA repair protein
                     1 homolog"
                     /note="meiosis protein 5 homolog; liver
                     regeneration-related protein LRRGT00030; MEI5 meiotic
                     recombination protein homolog; MEI5 recombination repair
                     protein homolog; SWI5-dependent recombination repair 1"
                     /calculated_mol_wt=28885
     Region          41..247
                     /region_name="Mei5"
                     /note="Double-strand recombination repair protein;
                     pfam10376"
                     /db_xref="CDD:431242"
     CDS             1..256
                     /gene="Sfr1"
                     /gene_synonym="LRRGT00030; Meir5; RGD1305481"
                     /coded_by="NM_001047856.2:65..835"
                     /db_xref="GeneID:294030"
                     /db_xref="RGD:1305481"
ORIGIN      
        1 maeeegnqei tskmenpsds astspdipqt senppsppts pdkpqtsenp pslhsnssgk
       61 qpmsgtlker lkkarassqp fcsvvkrikv eneendqtls epgesskeen cskaqeslen
      121 kdnepekess edkntsesks ldtgsssvlq kdstektikq tlkeekaklt rqvqekedll
      181 rrlklvkmyr ikndvteled likkwrrcgq rllcelqsim sededekltl telidyygid
      241 dkllhynrte eeftgv
//
LOCUS       NP_001025068             794 aa            linear   ROD 27-APR-2025
DEFINITION  striatin-3 [Rattus norvegicus].
ACCESSION   NP_001025068 XP_343060
VERSION     NP_001025068.1
DBSOURCE    REFSEQ: accession NM_001029897.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Bisoyi,P., Ratna,D., Kumar,G., Mallick,B.N. and Goswami,S.K.
  TITLE     In the Rat Midbrain, SG2NA and DJ-1 have Common Interactome,
            Including Mitochondrial Electron Transporters that are Comodulated
            Under Oxidative Stress
  JOURNAL   Cell Mol Neurobiol 43 (7), 3061-3080 (2023)
   PUBMED   37165139
  REMARK    GeneRIF: In the Rat Midbrain, SG2NA and DJ-1 have Common
            Interactome, Including Mitochondrial Electron Transporters that are
            Comodulated Under Oxidative Stress.
            Review article
            Erratum:[Cell Mol Neurobiol. 2023 Oct;43(7):3081. doi:
            10.1007/s10571-023-01369-x. PMID: 37278863]
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Lant,B., Yu,B., Goudreault,M., Holmyard,D., Knight,J.D., Xu,P.,
            Zhao,L., Chin,K., Wallace,E., Zhen,M., Gingras,A.C. and Derry,W.B.
  TITLE     CCM-3/STRIPAK promotes seamless tube extension through endocytic
            recycling
  JOURNAL   Nat Commun 6, 6449 (2015)
   PUBMED   25743393
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Tan,B., Long,X., Nakshatri,H., Nephew,K.P. and Bigsby,R.M.
  TITLE     Striatin-3 gamma inhibits estrogen receptor activity by recruiting
            a protein phosphatase
  JOURNAL   J Mol Endocrinol 40 (5), 199-210 (2008)
   PUBMED   18434427
  REMARK    GeneRIF: A rat STRN3 gamma-protein phosphatase 2A complex is
            recruited to agonist-activated estrogen receptor alpha, thereby
            leading to its dephosphorylation and inhibiting transcription.
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Gaillard,S., Bailly,Y., Benoist,M., Rakitina,T., Kessler,J.P.,
            Fronzaroli-Molinieres,L., Dargent,B. and Castets,F.
  TITLE     Targeting of proteins of the striatin family to dendritic spines:
            role of the coiled-coil domain
  JOURNAL   Traffic 7 (1), 74-84 (2006)
   PUBMED   16445688
REFERENCE   7  (residues 1 to 794)
  AUTHORS   Blondeau,C., Gaillard,S., Ternaux,J.P., Monneron,A. and Baude,A.
  TITLE     Expression and distribution of phocein and members of the striatin
            family in neurones of rat peripheral ganglia
  JOURNAL   Histochem Cell Biol 119 (2), 131-138 (2003)
   PUBMED   12610732
REFERENCE   8  (residues 1 to 794)
  AUTHORS   Zhu,W., Chan,E.K., Li,J., Hemmerich,P. and Tan,E.M.
  TITLE     Transcription activating property of autoantigen SG2NA and
            modulating effect of WD-40 repeats
  JOURNAL   Exp Cell Res 269 (2), 312-321 (2001)
   PUBMED   11570823
REFERENCE   9  (residues 1 to 794)
  AUTHORS   Baillat,G., Moqrich,A., Castets,F., Baude,A., Bailly,Y.,
            Benmerah,A. and Monneron,A.
  TITLE     Molecular cloning and characterization of phocein, a protein found
            from the Golgi complex to dendritic spines
  JOURNAL   Mol Biol Cell 12 (3), 663-673 (2001)
   PUBMED   11251078
REFERENCE   10 (residues 1 to 794)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Jul 28, 2005 this sequence version replaced XP_343060.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.35478.1,
                                           SRR22582424.1325165.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..794
                     /product="striatin-3"
                     /note="striatin-3-gamma; s/G2 antigen; cell cycle
                     autoantigen SG2NA; nuclear autoantigen; striatin,
                     calmodulin binding protein 3"
                     /calculated_mol_wt=86981
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q13033; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Region          64..188
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          70..78
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Region          164..181
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERG2; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13033; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Region          309..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P58405.2)"
     Region          472..793
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          475..514
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Site            order(476,494,498,504..505,528..529,547,551,557..558,
                     581..582,599,604,610..611,626,646,650,656..657,669..670,
                     695,699,705..706,718..719,736,741,747..748,760..761,783,
                     787,793)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          482..528
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          528..567
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Region          534..572
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          581..620
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Region          586..623
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          632..668
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          676..715
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Region          681..717
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          718..757
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Region          723..762
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          764..794
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P58405.2)"
     Region          769..793
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..794
                     /gene="Strn3"
                     /gene_synonym="Gs2na; Sg2na"
                     /coded_by="NM_001029897.3:217..2601"
                     /db_xref="GeneID:114520"
                     /db_xref="RGD:621827"
ORIGIN      
        1 mdelaggggg qgmavpprpq qgpggnlslp pgangapggg gppaaetagp pagpelsrpq
       61 qytipgilhy iqhewarfem erahwevera elqariaflq gerkgqenlk kdlvrrikml
      121 eyalkqerak yhklkygtel nqgdlkmptf eseetkdaea ppaqnsqltw kqgrqllrqy
      181 lqevgytdti ldvrsqrvrs llglsnsepn gsieaknleq ilnggespkq kgqeikrpsg
      241 dvletfnfle naddsdeeen dmiegipegk dklrihkhki gneglaadlt ddpdteealk
      301 efdflvtaed gegagearss gdgtewdkdd lsptaevwdv dqglmsklke qykkerkgkr
      361 gakrvnrtnl cdmitdlgdd elphipsgii nqsrsastrm tdhegsraee aepitfpsgg
      421 gksfimgsdd vllsvlglgd ladltvtnda dysydlpank dalrktwnpk ytlrshfdgv
      481 ralafhpvep vlvtasedht lklwnlqktv pakksasldv epiytfrahi gpvlslaiss
      541 ngeqcfsggi datiqwwnmp spnvdpydty eshvlagtlv ahtdavwgla ysgiknqlls
      601 csadgtirlw npqeklpcic tyngdkehgi ptsvdfigcd pahmvtsfnt gsaiiydlet
      661 sqslvmlssq vdsglqssnh inrvvshptl pvtitahedr hikffdnktg kmihsmvahl
      721 davtslavdp ngiylmsgsh dcsirlwnld sktcvqeita hrkkldesiy dvafhpskay
      781 iasagadala kvfv
//
LOCUS       NP_001264529             313 aa            linear   ROD 27-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein C isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001264529
VERSION     NP_001264529.1
DBSOURCE    REFSEQ: accession NM_001277600.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Liu,N., Dai,Q., Zheng,G., He,C., Parisien,M. and Pan,T.
  TITLE     N(6)-methyladenosine-dependent RNA structural switches regulate
            RNA-protein interactions
  JOURNAL   Nature 518 (7540), 560-564 (2015)
   PUBMED   25719671
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Todd,M.A. and Picketts,D.J.
  TITLE     PHF6 interacts with the nucleosome remodeling and deacetylation
            (NuRD) complex
  JOURNAL   J Proteome Res 11 (8), 4326-4337 (2012)
   PUBMED   22720776
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Raffalli-Mathieu,F., Geneste,O. and Lang,M.A.
  TITLE     Characterization of two nuclear proteins that interact with
            cytochrome P-450 1A2 mRNA. Regulation of RNA binding and possible
            role in the expression of the Cyp1a2 gene
  JOURNAL   Eur J Biochem 245 (1), 17-24 (1997)
   PUBMED   9128719
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Faura,M., Renau-Piqueras,J., Bachs,O. and Bosser,R.
  TITLE     Differential distribution of heterogeneous nuclear
            ribonucleoproteins in rat tissues
  JOURNAL   Biochem Biophys Res Commun 217 (2), 554-560 (1995)
   PUBMED   7503735
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Sharp,Z.D., Smith,K.P., Cao,Z.D. and Helsel,S.
  TITLE     Cloning of the nucleic acid-binding domain of the rat HnRNP C-type
            protein
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 306-309 (1990)
   PUBMED   2088340
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and CB582273.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF109530.1, SRR26360186.638872.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676786
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..313
                     /product="heterogeneous nuclear ribonucleoprotein C
                     isoform 1"
                     /note="hnRNP C protein C-terminal fragment (158 AA); hnRNP
                     core protein C; heterogeneous nuclear ribonucleoprotein C
                     (C1/C2); heterogeneous nuclear ribonucleoproteins C1/C2"
                     /calculated_mol_wt=34254
     Region          10..93
                     /region_name="RRM_hnRNPC"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP
                     C1/C2); cd12603"
                     /db_xref="CDD:410015"
     CDS             1..313
                     /gene="Hnrnpc"
                     /gene_synonym="hnRNP C; Hnrpc"
                     /coded_by="NM_001277600.1:217..1158"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290046"
                     /db_xref="RGD:1309982"
ORIGIN      
        1 masnvtnktd prsmnsrvfi gnlntlvvkk sdveaifsky gkivgcsvhk gfafvqyvne
       61 rnaraavage dgrmiagqvl dinlaaepkv nrgkagvkrs aaemygsvpe hpspspllss
      121 sfdldydfqr dyydrmysyp arvpppppia ravvpskrqr vsgntsrrgk sgfnsksgqr
      181 gsssksgklk gddlqaikke ltqikqkvds lleslekiek eqskqadlsf sspvemknek
      241 seeeqssasv kkdetnvkme seagaddsae egdllddddn edrgddqlel kddekepeeg
      301 eddrdsange dds
//
LOCUS       NP_001094045             576 aa            linear   ROD 27-APR-2025
DEFINITION  MAGUK p55 subfamily member 7 [Rattus norvegicus].
ACCESSION   NP_001094045 XP_001061081 XP_003753053 XP_225473
VERSION     NP_001094045.1
DBSOURCE    REFSEQ: accession NM_001100575.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Yang,X., Xie,X., Chen,L., Zhou,H., Wang,Z., Zhao,W., Tian,R.,
            Zhang,R., Tian,C., Long,J. and Shen,Y.
  TITLE     Structural basis for tandem L27 domain-mediated polymerization
  JOURNAL   FASEB J 24 (12), 4806-4815 (2010)
   PUBMED   20702775
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Stucke,V.M., Timmerman,E., Vandekerckhove,J., Gevaert,K. and
            Hall,A.
  TITLE     The MAGUK protein MPP7 binds to the polarity protein hDlg1 and
            facilitates epithelial tight junction formation
  JOURNAL   Mol Biol Cell 18 (5), 1744-1755 (2007)
   PUBMED   17332497
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Bohl,J., Brimer,N., Lyons,C. and Vande Pol,S.B.
  TITLE     The stardust family protein MPP7 forms a tripartite complex with
            LIN7 and DLG1 that regulates the stability and localization of DLG1
            to cell junctions
  JOURNAL   J Biol Chem 282 (13), 9392-9400 (2007)
   PUBMED   17237226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On or before Aug 19, 2012 this sequence version replaced
            XP_225473.4, XP_001061081.1, XP_003753053.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.55878.1,
                                           SRR26643295.54831.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..576
                     /product="MAGUK p55 subfamily member 7"
                     /note="membrane protein, palmitoylated 7 (MAGUK p55
                     subfamily member 7); membrane palmitoylated protein 7"
                     /calculated_mol_wt=65492
     Region          16..68
                     /region_name="L27"
                     /note="domain in receptor targeting proteins Lin-2 and
                     Lin-7; smart00569"
                     /db_xref="CDD:197794"
     Region          <88..125
                     /region_name="L27"
                     /note="domain in receptor targeting proteins Lin-2 and
                     Lin-7; smart00569"
                     /db_xref="CDD:197794"
     Region          138..218
                     /region_name="PDZ_MPP3-MPP4-MPP7-like"
                     /note="PDZ domain of membrane palmitoylated proteins 3
                     (MPP3), MPP4, and MPP7, and related domains; cd06799"
                     /db_xref="CDD:467260"
     Site            order(148..154,165,168,198,202,205..206)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467260"
     Region          232..292
                     /region_name="SH3_MPP7"
                     /note="Src Homology 3 domain of Membrane Protein,
                     Palmitoylated 7 (or MAGUK p55 subfamily member 7);
                     cd12033"
                     /db_xref="CDD:212966"
     Site            order(234,258..259)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212966"
     Site            order(237,239,242,253,271..272,289,291..292)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212966"
     Region          289..383
                     /region_name="Phospho-regulated basic and hydrophobic
                     (PRBH) motif. /evidence=ECO:0000250|UniProtKB:Q5T2T1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2Y3.2)"
     Region          384..563
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5T2T1; propagated from
                     UniProtKB/Swiss-Prot (Q5U2Y3.2)"
     CDS             1..576
                     /gene="Mpp7"
                     /coded_by="NM_001100575.1:114..1844"
                     /db_xref="GeneID:307035"
                     /db_xref="RGD:1305675"
ORIGIN      
        1 mpalatgsac dtglyellaa lpaqlqphvd sqedltflwd mfgekslhsl vkiheklhyy
       61 ekqspvpilh gaaaladdla delqnkppns eirellklls kpnvkallsv hdtvaqksyd
      121 pvlppmpddi ddeedsvkii rlvknreplg atikkdeqtg aitvarimrg gaadrsglih
      181 vgdelrevng ipvedkrpee iiqilsqsqg aitfkiipst keeipskegk ifikalfdyd
      241 pkedkaipck eaglsfrkgd ilqimsqdda twwqakhegd tnpraglips khfqerrlal
      301 rrpeivvqpl klsnrkssgf rrsfrlsrkd kktnksmyec kkseqydtad vptyeevtpy
      361 rrqthdkyrl vvlvgpvgvg lnelkrkllm sdtqhygvtv phttrarrsq esdgveyifi
      421 skhlfetdvq nnkfieygey knnyygtsid svrsvlaknk vclldvqpht vkhlrtlefk
      481 pyvifikpps ierlretrkn akiissrddq gtakpfteed fqemiksaqi mesqyghlfd
      541 kiiinddltv afnelkttfd kletdahwvp vswlhs
//
LOCUS       NP_001257911             419 aa            linear   ROD 27-APR-2025
DEFINITION  serine protease inhibitor A3M precursor [Rattus norvegicus].
ACCESSION   NP_001257911 XP_216782
VERSION     NP_001257911.1
DBSOURCE    REFSEQ: accession NM_001270982.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Vanni,S., Moda,F., Zattoni,M., Bistaffa,E., De Cecco,E., Rossi,M.,
            Giaccone,G., Tagliavini,F., Haik,S., Deslys,J.P., Zanusso,G.,
            Ironside,J.W., Ferrer,I., Kovacs,G.G. and Legname,G.
  TITLE     Differential overexpression of SERPINA3 in human prion diseases
  JOURNAL   Sci Rep 7 (1), 15637 (2017)
   PUBMED   29142239
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Horvath,A.J., Forsyth,S.L. and Coughlin,P.B.
  TITLE     Expression patterns of murine antichymotrypsin-like genes reflect
            evolutionary divergence at the Serpina3 locus
  JOURNAL   J Mol Evol 59 (4), 488-497 (2004)
   PUBMED   15638460
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Ohkubo,K., Ogata,S., Misumi,Y., Takami,N., Sinohara,H. and
            Ikehara,Y.
  TITLE     Cloning, structure and expression of cDNA for mouse contrapsin and
            a related protein
  JOURNAL   Biochem J 276 (Pt 2) (Pt 2), 337-342 (1991)
   PUBMED   2049065
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Aug 17, 2012 this sequence version replaced XP_216782.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.20842.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMEA5760476 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..419
                     /product="serine protease inhibitor A3M precursor"
                     /note="serine protease inhibitor 2.4; serine (or cysteine)
                     proteinase inhibitor, clade A, member 3M; serpin A3M;
                     serine protease inhibitor A3M"
                     /calculated_mol_wt=44927
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1932
     Region          37..416
                     /region_name="serpinA3_A1AC"
                     /note="serpin family A member 3, alpha 1-antichymotrypsin;
                     cd19551"
                     /db_xref="CDD:381019"
     Site            order(365..377,379..383,386..394)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381019"
     CDS             1..419
                     /gene="Serpina3m"
                     /gene_synonym="SPI-2.4"
                     /coded_by="NM_001270982.1:103..1362"
                     /db_xref="GeneID:299276"
                     /db_xref="RGD:735068"
ORIGIN      
        1 mafiaalgll magicpavlg fpdgtlgndt llhkdqdkgt qldsltlesi ntdfafslyk
       61 mlalknpdkn vvfsplsisa alaivslgak gntleeilev lrfnltesye tdihqgfghl
      121 lqrlsqpgdq vkiitgnalf idknlqvlae fqektralyq veaftadfqq prvteklind
      181 yvrnqtqgki qelvsglker tsmvlvnyll frgkwkvpfd pdytfesefy vdekrsvkvs
      241 mmkieelttp yfrdeelscs vlelkytgns salfilpdkg rmqqveaslq petlkkwkds
      301 lrprkidely lprlsistdy sleevlpelg irdvfsqqad lsritgakdl svsqvvhkvv
      361 ldvnetgtea aaatganlvp rsgrppmivw fnrpfliavs hthgqtilfm akvinpvga
//
LOCUS       NP_037221                704 aa            linear   ROD 27-APR-2025
DEFINITION  glycogen [starch] synthase, liver [Rattus norvegicus].
ACCESSION   NP_037221
VERSION     NP_037221.2
DBSOURCE    REFSEQ: accession NM_013089.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Ros,S., Zafra,D., Valles-Ortega,J., Garcia-Rocha,M., Forrow,S.,
            Dominguez,J., Calbo,J. and Guinovart,J.J.
  TITLE     Hepatic overexpression of a constitutively active form of liver
            glycogen synthase improves glucose homeostasis
  JOURNAL   J Biol Chem 285 (48), 37170-37177 (2010)
   PUBMED   20841354
  REMARK    GeneRIF: Transgenic LGS rat showed enhanced glycogen storage and an
            mproved glucose tolerance.
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Ros,S., Garcia-Rocha,M., Dominguez,J., Ferrer,J.C. and
            Guinovart,J.J.
  TITLE     Control of liver glycogen synthase activity and intracellular
            distribution by phosphorylation
  JOURNAL   J Biol Chem 284 (10), 6370-6378 (2009)
   PUBMED   19124463
  REMARK    GeneRIF: LGS translocation is strictly dependent on glycogen
            synthesis.
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Kadotani,A., Fujimura,M., Nakamura,T., Ohyama,S., Harada,N.,
            Maruki,H., Tamai,Y., Kanatani,A., Eiki,J. and Nagata,Y.
  TITLE     Metabolic impact of overexpression of liver glycogen synthase with
            serine-to-alanine substitutions in rat primary hepatocytes
  JOURNAL   Arch Biochem Biophys 466 (2), 283-289 (2007)
   PUBMED   17880910
  REMARK    GeneRIF: elevation of glycogen synthase activity has an inhibitory
            effect on glucose production in hepatocytes by shunting
            gluconeogenic precursors into glycogen.
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Fang,Y., Studer,E., Mitchell,C., Grant,S., Pandak,W.M.,
            Hylemon,P.B. and Dent,P.
  TITLE     Conjugated bile acids regulate hepatocyte glycogen synthase
            activity in vitro and in vivo via Galphai signaling
  JOURNAL   Mol Pharmacol 71 (4), 1122-1128 (2007)
   PUBMED   17200418
  REMARK    GeneRIF: bile acids are physiological regulators of glycogen
            synthase in rat liver and conjugated bile acids use a
            Galpha(i)-coupled G protein-coupled receptor to regulate GS
            activity in vitro and in vivo
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Fujimoto,Y., Donahue,E.P. and Shiota,M.
  TITLE     Defect in glucokinase translocation in Zucker diabetic fatty rats
  JOURNAL   Am J Physiol Endocrinol Metab 287 (3), E414-E423 (2004)
   PUBMED   15138155
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Westphal,S.A. and Nuttall,F.Q.
  TITLE     Comparative characterization of human and rat liver glycogen
            synthase
  JOURNAL   Arch Biochem Biophys 292 (2), 479-486 (1992)
   PUBMED   1731614
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Carabaza,A., Ciudad,C.J., Baque,S. and Guinovart,J.J.
  TITLE     Glucose has to be phosphorylated to activate glycogen synthase, but
            not to inactivate glycogen phosphorylase in hepatocytes
  JOURNAL   FEBS Lett 296 (2), 211-214 (1992)
   PUBMED   1733780
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Wera,S., Bollen,M. and Stalmans,W.
  TITLE     Purification and characterization of the glycogen-bound protein
            phosphatase from rat liver
  JOURNAL   J Biol Chem 266 (1), 339-345 (1991)
   PUBMED   1898724
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Bai,G., Zhang,Z.J., Werner,R., Nuttall,F.Q., Tan,A.W. and Lee,E.Y.
  TITLE     The primary structure of rat liver glycogen synthase deduced by
            cDNA cloning. Absence of phosphorylation sites 1a and 1b
  JOURNAL   J Biol Chem 265 (14), 7843-7848 (1990)
   PUBMED   2110561
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Katz,J., Golden,S. and Wals,P.A.
  TITLE     Glycogen synthesis by rat hepatocytes
  JOURNAL   Biochem J 180 (2), 389-402 (1979)
   PUBMED   114169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Feb 5, 2015 this sequence version replaced NP_037221.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05446.1, AF346902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..704
                     /product="glycogen [starch] synthase, liver"
                     /EC_number="2.4.1.11"
                     /note="Glycogen synthase 2 (liver)"
                     /calculated_mol_wt=80589
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Region          32..660
                     /region_name="Glycogen_syn"
                     /note="Glycogen synthase; pfam05693"
                     /db_xref="CDD:399009"
     Region          620..704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17625.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54840; propagated from
                     UniProtKB/Swiss-Prot (P17625.2)"
     CDS             1..704
                     /gene="Gys2"
                     /gene_synonym="GLYSN"
                     /coded_by="NM_013089.2:230..2344"
                     /db_xref="GeneID:25623"
                     /db_xref="RGD:2773"
ORIGIN      
        1 mlrgrslsvt slgglpawea erlpvedlll fevswevtnk vggictviqs kakttanewg
       61 enyfligpyf ehnvktqvep cepandavrk avdamnkhgc qvhfgrwlie gspyvvlfdi
      121 sssawnldrw kgdfweacgv giphddrean dmlifgslta wflkevtdha dgkhviaqfh
      181 ewqagtglil srarklpiat iftthatllg rylcaanidf ynqldkfnid keagerqiyh
      241 rycmerasvh cahvfttvse itaieaehml krkpdvvtpn glnvkkfsav hefqnlhaty
      301 kariqdfvrg hfyghldfdl ektlflfiag ryefsnkgad ifleslsrln fllrmhksnv
      361 tvvvffimpa ktnnfnvetl kgqavrkqlw dtvhcmkekf gkklydgllr geipdmnsil
      421 drddltimkr aifstqrhsl ppvtthnmid dstdpilsti rriglfnnrt drvkvilhpe
      481 flsstspllp mdyeefvrgc hlgvfpsyye pwgytpaect vmgipsvttn lsgfgcfmqe
      541 hvadptaygi yivdrrfrsp ddscnqltqf lygfckqsrr qriiqrnrte rlsdlldwry
      601 lgryyqharh ltlsrafpdk fhleptsppt tdgfkyprps svppspsgsq tsspqssdve
      661 negdederyd eeeeaerdrl nikspfslnh ipkgkkklhg eykn
//
LOCUS       NP_036680                202 aa            linear   ROD 27-APR-2025
DEFINITION  endothelin-1 preproprotein [Rattus norvegicus].
ACCESSION   NP_036680
VERSION     NP_036680.1
DBSOURCE    REFSEQ: accession NM_012548.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Wang,Z., Wu,Z., Hu,Z., Zheng,H. and Chen,Z.
  TITLE     ET1 acts as a potential plasma biomarker and therapeutic target in
            deep venous thrombosis rat model
  JOURNAL   J Thromb Thrombolysis 57 (6), 1067-1075 (2024)
   PUBMED   38824487
  REMARK    GeneRIF: ET1 acts as a potential plasma biomarker and therapeutic
            target in deep venous thrombosis rat model.
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Xu,H., Yu,X., Xie,R., Wang,Y. and Li,C.
  TITLE     RCOR1 improves neurobehaviors and neuron injury in rat cerebral
            palsy by Endothelin-1 targeting-induced Akt/GSK-3beta pathway
            upregulation
  JOURNAL   Brain Dev 46 (2), 93-102 (2024)
   PUBMED   37978036
  REMARK    GeneRIF: RCOR1 improves neurobehaviors and neuron injury in rat
            cerebral palsy by Endothelin-1 targeting-induced Akt/GSK-3beta
            pathway upregulation.
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Yang,T.C., Lu,M.H., Wang,W.J. and Chen,J.Y.
  TITLE     CEBPB/POU2F2 modulates endothelin 1 expression in prehypertensive
            SHR vascular smooth muscle cells
  JOURNAL   J Mol Endocrinol 71 (1), e220178 (2023)
   PUBMED   36942826
  REMARK    GeneRIF: CEBPB/POU2F2 modulates endothelin 1 expression in
            prehypertensive SHR vascular smooth muscle cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Costello,H.M., Juffre,A., Cheng,K.Y., Bratanatawira,P.,
            Crislip,G.R., Zietara,A., Spires,D.R., Staruschenko,A., Douma,L.G.
            and Gumz,M.L.
  TITLE     The circadian clock protein PER1 is important in maintaining
            endothelin axis regulation in Dahl salt-sensitive rats
  JOURNAL   Can J Physiol Pharmacol 101 (3), 136-146 (2023)
   PUBMED   36450128
  REMARK    GeneRIF: The circadian clock protein PER1 is important in
            maintaining endothelin axis regulation in Dahl salt-sensitive rats.
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Matsumoto,T., Takayanagi,K., Kojima,M., Taguchi,K. and Kobayashi,T.
  TITLE     Indoxyl sulfate enhances endothelin-1-induced contraction via
            impairment of NO/cGMP signaling in rat aorta
  JOURNAL   Pflugers Arch 473 (8), 1247-1259 (2021)
   PUBMED   34021781
  REMARK    GeneRIF: Indoxyl sulfate enhances endothelin-1-induced contraction
            via impairment of NO/cGMP signaling in rat aorta.
            Erratum:[Pflugers Arch. 2021 Aug;473(8):1329. doi:
            10.1007/s00424-021-02587-2. PMID: 34137923]
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Samson,W.K. and Skala,K.D.
  TITLE     Comparison of the pituitary effects of the mammalian endothelins:
            vasoactive intestinal contractor (endothelin-beta, rat
            endothelin-2) is a potent inhibitor of prolactin secretion
  JOURNAL   Endocrinology 130 (5), 2964-2970 (1992)
   PUBMED   1533364
REFERENCE   7  (residues 1 to 202)
  AUTHORS   D'Orleans-Juste,P., Telemaque,S., Claing,A., Ihara,M. and Yano,M.
  TITLE     Human big-endothelin-1 and endothelin-1 release prostacyclin via
            the activation of ET1 receptors in the rat perfused lung
  JOURNAL   Br J Pharmacol 105 (4), 773-775 (1992)
   PUBMED   1324048
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Simmet,T., Pritze,S., Thelen,K.I. and Peskar,B.A.
  TITLE     Release of endothelin in the oleic acid-induced respiratory
            distress syndrome in rats
  JOURNAL   Eur J Pharmacol 211 (3), 319-322 (1992)
   PUBMED   1618274
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Sakamoto,A., Yanagisawa,M., Sakurai,T., Takuwa,Y., Yanagisawa,H.
            and Masaki,T.
  TITLE     Cloning and functional expression of human cDNA for the ETB
            endothelin receptor
  JOURNAL   Biochem Biophys Res Commun 178 (2), 656-663 (1991)
   PUBMED   1713452
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Sakurai,T., Yanagisawa,M., Inoue,A., Ryan,U.S., Kimura,S.,
            Mitsui,Y., Goto,K. and Masaki,T.
  TITLE     cDNA cloning, sequence analysis and tissue distribution of rat
            preproendothelin-1 mRNA
  JOURNAL   Biochem Biophys Res Commun 175 (1), 44-47 (1991)
   PUBMED   1840483
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M64711.1, SRR26643289.39672.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676788
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..202
                     /product="endothelin-1 preproprotein"
                     /note="ET-1; PPET1; preproendothelin-1"
                     /calculated_mol_wt=21159
     sig_peptide     1..17
                     /calculated_mol_wt=1994
     proprotein      18..202
                     /product="endothelin-1 proprotein"
                     /calculated_mol_wt=21159
     Region          28..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22388.2)"
     Region          49..77
                     /region_name="Endothelin"
                     /note="Endothelin family; pfam00322"
                     /db_xref="CDD:425606"
     mat_peptide     53..73
                     /product="endothelin-1"
                     /calculated_mol_wt=2496
     Site            73..74
                     /site_type="cleavage"
                     /note="Cleavage, by KEL.
                     /evidence=ECO:0000250|UniProtKB:P05305; propagated from
                     UniProtKB/Swiss-Prot (P22388.2)"
     Region          109..130
                     /region_name="END"
                     /note="Endothelin; smart00272"
                     /db_xref="CDD:197618"
     Region          110..124
                     /region_name="Endothelin-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P22388.2)"
     CDS             1..202
                     /gene="Edn1"
                     /gene_synonym="Et1"
                     /coded_by="NM_012548.2:190..798"
                     /db_xref="GeneID:24323"
                     /db_xref="RGD:2532"
ORIGIN      
        1 mdyfpvifsl lfvafqgape tavlgaelsp raekevqspp pstswrprrs krcscsslmd
       61 kecvyfchld iiwvntperv vpyglgspsr skrslkdllp tkttdqgnrc qcahqkdkkc
      121 wnfcqadkel raqstmqkgv kdfkkgkpcp klgkkciyqq lvegrklrrl eaisnsikts
      181 frvaklkael yrdqklihnr ah
//
LOCUS       NP_001100360             145 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL14m precursor [Rattus
            norvegicus].
ACCESSION   NP_001100360 XP_001067192 XP_217350
VERSION     NP_001100360.1
DBSOURCE    REFSEQ: accession NM_001106890.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001067192.1, XP_217350.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB709167.1, CB709152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676785, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG   :: downstream AUG is associated
                                                  with N-terminal localization
                                                  signal
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..145
                     /product="large ribosomal subunit protein uL14m precursor"
                     /note="39S ribosomal protein L14, mitochondrial; 39S
                     ribosomal protein L32, mitochondrial; large ribosomal
                     subunit protein uL14m"
                     /calculated_mol_wt=12770
     transit_peptide 1..30
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:9857009; propagated from
                     UniProtKB/Swiss-Prot (Q7M0E7.2)"
                     /calculated_mol_wt=3161
     mat_peptide     31..145
                     /product="Large ribosomal subunit protein uL14m.
                     /id=PRO_0000261136"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7M0E7.2)"
                     /calculated_mol_wt=12770
     Region          33..139
                     /region_name="Ribosomal_uL14"
                     /note="Ribosomal protein uL14; cd00337"
                     /db_xref="CDD:466774"
     CDS             1..145
                     /gene="Mrpl14"
                     /gene_synonym="L14mt; L32mt; MRP-L14; MRP-L32"
                     /coded_by="NM_001106890.2:137..574"
                     /db_xref="GeneID:301250"
                     /db_xref="RGD:1306240"
ORIGIN      
        1 mavltglfgf fayvrgavsq rcfstsgsls aiqkmtrvrv vdnsalgntp yhrpprcihv
       61 ynksgvgkvg dqillairgq kkkalivghr mpgsrmtpkf dsnnvvlied ngnpvgtrik
      121 ipiptslrrr egeyskvlai aqnfv
//
LOCUS       NP_110459                132 aa            linear   ROD 27-APR-2025
DEFINITION  fatty acid-binding protein, brain [Rattus norvegicus].
ACCESSION   NP_110459
VERSION     NP_110459.1
DBSOURCE    REFSEQ: accession NM_030832.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Han,X., Li,H., Zhang,Y., Qin,J., Yang,Q., Wang,L., Yuan,M. and
            Xia,C.
  TITLE     Brain lipid-binding protein promotes proliferation and modulates
            cell cycle in C6 rat glioma cells
  JOURNAL   Int J Oncol 51 (5), 1439-1448 (2017)
   PUBMED   29048614
  REMARK    GeneRIF: The results of the xenograft model assay showed that
            exogenous BLBP also stimulated tumor formation and downregulated
            p21 and p16. In conclusion, our study demonstrated that exogenous
            BLBP promoted proliferation of the C6 cells in vitro and
            facilitated tumor formation in vivo. Therefore, BLBP expression in
            glioma cells may promote cell growth by inhibiting the tumor
            suppressors.
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Serinagaoglu,Y., Pare,J., Giovannini,M. and Cao,X.
  TITLE     Nf2-Yap signaling controls the expansion of DRG progenitors and
            glia during DRG development
  JOURNAL   Dev Biol 398 (1), 97-109 (2015)
   PUBMED   25433207
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Young,J.K., Heinbockel,T. and Gondre-Lewis,M.C.
  TITLE     Astrocyte fatty acid binding protein-7 is a marker for neurogenic
            niches in the rat hippocampus
  JOURNAL   Hippocampus 23 (12), 1476-1483 (2013)
   PUBMED   23996503
  REMARK    GeneRIF: The data of this study suggested that regional
            accumulations of FABP7+ astrocytes may represent reservoirs of
            cells having the potential for neurogenesis.
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Watanabe,A., Toyota,T., Owada,Y., Hayashi,T., Iwayama,Y.,
            Matsumata,M., Ishitsuka,Y., Nakaya,A., Maekawa,M., Ohnishi,T.,
            Arai,R., Sakurai,K., Yamada,K., Kondo,H., Hashimoto,K., Osumi,N.
            and Yoshikawa,T.
  TITLE     Fabp7 maps to a quantitative trait locus for a schizophrenia
            endophenotype
  JOURNAL   PLoS Biol 5 (11), e297 (2007)
   PUBMED   18001149
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Arai,Y., Funatsu,N., Numayama-Tsuruta,K., Nomura,T., Nakamura,S.
            and Osumi,N.
  TITLE     Role of Fabp7, a downstream gene of Pax6, in the maintenance of
            neuroepithelial cells during early embryonic development of the rat
            cortex
  JOURNAL   J Neurosci 25 (42), 9752-9761 (2005)
   PUBMED   16237179
  REMARK    GeneRIF: Fabp7 is a downstream gene of Pax6 transcription factor in
            the developing rat cortex and essential for maintenance of
            neuroepithelial cells during early cortical development.
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Eiraku,M., Tohgo,A., Ono,K., Kaneko,M., Fujishima,K., Hirano,T. and
            Kengaku,M.
  TITLE     DNER acts as a neuron-specific Notch ligand during Bergmann glial
            development
  JOURNAL   Nat Neurosci 8 (7), 873-880 (2005)
   PUBMED   15965470
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Liang,Y., Diehn,M., Watson,N., Bollen,A.W., Aldape,K.D.,
            Nicholas,M.K., Lamborn,K.R., Berger,M.S., Botstein,D., Brown,P.O.
            and Israel,M.A.
  TITLE     Gene expression profiling reveals molecularly and clinically
            distinct subtypes of glioblastoma multiforme
  JOURNAL   Proc Natl Acad Sci U S A 102 (16), 5814-5819 (2005)
   PUBMED   15827123
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Williams,S.E., Mann,F., Erskine,L., Sakurai,T., Wei,S., Rossi,D.J.,
            Gale,N.W., Holt,C.E., Mason,C.A. and Henkemeyer,M.
  TITLE     Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic
            chiasm
  JOURNAL   Neuron 39 (6), 919-935 (2003)
   PUBMED   12971893
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Hartfuss,E., Galli,R., Heins,N. and Gotz,M.
  TITLE     Characterization of CNS precursor subtypes and radial glia
  JOURNAL   Dev Biol 229 (1), 15-30 (2001)
   PUBMED   11133151
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Bennett,E., Stenvers,K.L., Lund,P.K. and Popko,B.
  TITLE     Cloning and characterization of a cDNA encoding a novel fatty acid
            binding protein from rat brain
  JOURNAL   J Neurochem 63 (5), 1616-1624 (1994)
   PUBMED   7931318
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U02096.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U02096.1, CB719459.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..132
                     /product="fatty acid-binding protein, brain"
                     /note="BLBP; B-FABP; brain lipid-binding protein;
                     brain-type fatty acid-binding protein; fatty acid binding
                     protein 7, brain"
                     /calculated_mol_wt=14733
     Region          2..131
                     /region_name="lipocalin_FABP"
                     /note="lipocalin/cytosolic fatty acid-binding protein
                     family; cl10502"
                     /db_xref="CDD:471979"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline.
                     /evidence=ECO:0000250|UniProtKB:Q09139; propagated from
                     UniProtKB/Swiss-Prot (P55051.2)"
     Site            order(5,9,41,43,50,52,54,61,63,65,94,96,103,105,107,114,
                     116,118,125,127,129)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381182"
     CDS             1..132
                     /gene="Fabp7"
                     /coded_by="NM_030832.2:82..480"
                     /db_xref="GeneID:80841"
                     /db_xref="RGD:69312"
ORIGIN      
        1 mvdafcatwk ltdsqnfdey mkalgvgfat rqvgnvtkpt viisqeggkv virtqctfkn
       61 teisfqlgee feetsiddrn cksvirldgd klihvqkwdg ketncvreik dgkmvvtltf
      121 gdvvavrcye ka
//
LOCUS       NP_596896                594 aa            linear   ROD 27-APR-2025
DEFINITION  cryptochrome-2 [Rattus norvegicus].
ACCESSION   NP_596896 XP_006234609
VERSION     NP_596896.2
DBSOURCE    REFSEQ: accession NM_133405.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Sokolowska,E., Viitanen,R., Misiewicz,Z., Mennesson,M., Saarnio,S.,
            Kulesskaya,N., Kangsep,S., Liljenback,H., Marjamaki,P., Autio,A.,
            Callan,S.A., Nuutila,P., Roivainen,A., Partonen,T. and Hovatta,I.
  TITLE     The circadian gene Cryptochrome 2 influences stress-induced brain
            activity and depressive-like behavior in mice
  JOURNAL   Genes Brain Behav 20 (4), e12708 (2021)
   PUBMED   33070440
  REMARK    GeneRIF: The circadian gene Cryptochrome 2 influences
            stress-induced brain activity and depressive-like behavior in mice.
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Wong,J.C.Y., Smyllie,N.J., Banks,G.T., Pothecary,C.A.,
            Barnard,A.R., Maywood,E.S., Jagannath,A., Hughes,S., van der
            Horst,G.T.J., MacLaren,R.E., Hankins,M.W., Hastings,M.H.,
            Nolan,P.M., Foster,R.G. and Peirson,S.N.
  TITLE     Differential roles for cryptochromes in the mammalian retinal clock
  JOURNAL   FASEB J 32 (8), 4302-4314 (2018)
   PUBMED   29561690
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Kriebs,A., Jordan,S.D., Soto,E., Henriksson,E., Sandate,C.R.,
            Vaughan,M.E., Chan,A.B., Duglan,D., Papp,S.J., Huber,A.L.,
            Afetian,M.E., Yu,R.T., Zhao,X., Downes,M., Evans,R.M. and
            Lamia,K.A.
  TITLE     Circadian repressors CRY1 and CRY2 broadly interact with nuclear
            receptors and modulate transcriptional activity
  JOURNAL   Proc Natl Acad Sci U S A 114 (33), 8776-8781 (2017)
   PUBMED   28751364
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Jordan,S.D., Kriebs,A., Vaughan,M., Duglan,D., Fan,W.,
            Henriksson,E., Huber,A.L., Papp,S.J., Nguyen,M., Afetian,M.,
            Downes,M., Yu,R.T., Kralli,A., Evans,R.M. and Lamia,K.A.
  TITLE     CRY1/2 Selectively Repress PPARdelta and Limit Exercise Capacity
  JOURNAL   Cell Metab 26 (1), 243-255 (2017)
   PUBMED   28683290
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Goriki,A., Hatanaka,F., Myung,J., Kim,J.K., Yoritaka,T., Tanoue,S.,
            Abe,T., Kiyonari,H., Fujimoto,K., Kato,Y., Todo,T., Matsubara,A.,
            Forger,D. and Takumi,T.
  TITLE     A novel protein, CHRONO, functions as a core component of the
            mammalian circadian clock
  JOURNAL   PLoS Biol 12 (4), e1001839 (2014)
   PUBMED   24736997
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 594)
  AUTHORS   van der Horst,G.T., Muijtjens,M., Kobayashi,K., Takano,R.,
            Kanno,S., Takao,M., de Wit,J., Verkerk,A., Eker,A.P., van
            Leenen,D., Buijs,R., Bootsma,D., Hoeijmakers,J.H. and Yasui,A.
  TITLE     Mammalian Cry1 and Cry2 are essential for maintenance of circadian
            rhythms
  JOURNAL   Nature 398 (6728), 627-630 (1999)
   PUBMED   10217146
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Kobayashi,K., Kanno,S., Smit,B., van der Horst,G.T., Takao,M. and
            Yasui,A.
  TITLE     Characterization of photolyase/blue-light receptor homologs in
            mouse and human cells
  JOURNAL   Nucleic Acids Res 26 (22), 5086-5092 (1998)
   PUBMED   9801304
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Ishibashi,K., Miyamoto,K., Taketani,Y., Morita,K., Takeda,E.,
            Sasaki,S. and Imai,M.
  TITLE     Molecular cloning of a second human stanniocalcin homologue (STC2)
  JOURNAL   Biochem Biophys Res Commun 250 (2), 252-258 (1998)
   PUBMED   9753616
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Zhao,S. and Sancar,A.
  TITLE     Human blue-light photoreceptor hCRY2 specifically interacts with
            protein serine/threonine phosphatase 5 and modulates its activity
  JOURNAL   Photochem Photobiol 66 (5), 727-731 (1997)
   PUBMED   9383998
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Hsu,D.S., Zhao,X., Zhao,S., Kazantsev,A., Wang,R.P., Todo,T.,
            Wei,Y.F. and Sancar,A.
  TITLE     Putative human blue-light photoreceptors hCRY1 and hCRY2 are
            flavoproteins
  JOURNAL   Biochemistry 35 (44), 13871-13877 (1996)
   PUBMED   8909283
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166416.1.
            
            On or before Feb 5, 2014 this sequence version replaced
            XP_006234609.1, NP_596896.1.
            
            Summary: This gene encodes a flavin adenine dinucleotide-binding
            protein that is a key component of the circadian core oscillator
            complex, which regulates the circadian clock. This gene is
            upregulated by Clock/Arntl heterodimers but then represses this
            upregulation in a feedback loop using Per/Cry heterodimers to
            interact with Clock/Arntl. Polymorphisms in this gene have been
            associated with altered sleep patterns. The encoded protein is
            widely conserved across plants and animals. [provided by RefSeq,
            Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166416.1, FQ211347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..594
                     /product="cryptochrome-2"
                     /note="cryptochrome 2 (photolyase-like); cryptochrome
                     circadian clock 2"
                     /calculated_mol_wt=66977
     Region          23..505
                     /region_name="PhrB"
                     /note="Deoxyribodipyrimidine photolyase [Replication,
                     recombination and repair]; COG0415"
                     /db_xref="CDD:440184"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q923I8.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:Q9R194; propagated from
                     UniProtKB/Swiss-Prot (Q923I8.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97784; propagated from
                     UniProtKB/Swiss-Prot (Q923I8.1)"
     Region          389..488
                     /region_name="Required for inhibition of
                     CLOCK-BMAL1-mediated transcription.
                     /evidence=ECO:0000250|UniProtKB:Q9R194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923I8.1)"
     Region          532..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q923I8.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:Q9R194; propagated from
                     UniProtKB/Swiss-Prot (Q923I8.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK1A and MAPK.
                     /evidence=ECO:0000250|UniProtKB:Q9R194; propagated from
                     UniProtKB/Swiss-Prot (Q923I8.1)"
     CDS             1..594
                     /gene="Cry2"
                     /coded_by="NM_133405.2:3..1787"
                     /db_xref="GeneID:170917"
                     /db_xref="RGD:620935"
ORIGIN      
        1 maaaavvaat vpaqsmgadg assvhwfrkg lrlhdnpall aavrgarcvr cvyildpwfa
       61 asssvginrw rfllqsledl dtslrklnsr lfvvrgqpad vfprlfkewg vtrltfeyds
      121 epfgkerdaa imkmakeagv evvtenshtl ydldriieln gqkppltykr fqalisrmel
      181 pkkpvgavss qhmencraei qenhddtygv psleelgfpt eglgpavwqg getealarld
      241 khlerkawva nyerprmnan sllasptgls pylrfgclsc rlfyyrlwdl yrkvkrnstp
      301 plslfgqllw reffytaatn nprfdrmegn piciqipwdr npealakwae gktgfpwida
      361 imtqlrqegw ihhlarhava cfltrgdlwv swesgvrvfd ellldadfsv nagswmwlsc
      421 saffqqffhc ycpvgfgrrt dpsgdyirry lpklkgfpsr yiyepwnape svqkaakcii
      481 gvdyprpivn haetsrlnie rmkqiyqqls ryrglcllas vpscvedlsh pvaepgssqa
      541 gsisntgprp lssgpaspkr kleaaeeppg eelskrarvt vtqmpaqepp skds
//
LOCUS       NP_001178509            1312 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase RNF123 [Rattus norvegicus].
ACCESSION   NP_001178509 XP_002730009
VERSION     NP_001178509.1
DBSOURCE    REFSEQ: accession NM_001191580.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1312)
  AUTHORS   Yuan,Y., Wang,Y.Y., Liu,X., Luo,B., Zhang,L., Zheng,F., Li,X.Y.,
            Guo,L.Y., Wang,L., Jiang,M., Pan,Y.M., Yan,Y.W., Yang,J.Y.,
            Chen,S.Y., Wang,J.N. and Tang,J.M.
  TITLE     KPC1 alleviates hypoxia/reoxygenation-induced apoptosis in rat
            cardiomyocyte cells though BAX degradation
  JOURNAL   J Cell Physiol 234 (12), 22921-22934 (2019)
   PUBMED   31148189
  REMARK    GeneRIF: Bax can be a novel target for the antiapoptotic effects of
            KPC1 on I/R-induced cardiomyocyte apoptosis and render mechanistic
            penetration into at least a subset of the mitochondrial effects of
            KPC1.
REFERENCE   2  (residues 1 to 1312)
  AUTHORS   Zhao,J., Zhang,S., Wu,X., Huan,W., Liu,Z., Wei,H., Shen,A. and
            Teng,H.
  TITLE     KPC1 expression and essential role after acute spinal cord injury
            in adult rat
  JOURNAL   Neurochem Res 36 (3), 549-558 (2011)
   PUBMED   21229311
  REMARK    GeneRIF: results suggest that KPC1 (Kip1 ubiquitylation-promoting
            complex 1) is related to the down-regulation of p27(kip1); this
            event may be involved in the proliferation of astrocytes after
            spinal cord injury
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_002730009.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.24068.1,
                                           SRR26643292.35432.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1312
                     /product="E3 ubiquitin-protein ligase RNF123"
                     /EC_number="2.3.2.27"
                     /note="kip1 ubiquitination-promoting complex protein 1;
                     RING-type E3 ubiquitin transferase RNF123"
                     /calculated_mol_wt=148162
     Region          121..248
                     /region_name="SPRY_RNF123"
                     /note="SPRY domain at N-terminus of ring finger protein
                     123; cd12882"
                     /db_xref="CDD:293940"
     Region          459..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXK7.1)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZXK7.1)"
     Site            681
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5XPI3; propagated from
                     UniProtKB/Swiss-Prot (D3ZXK7.1)"
     Region          966..972
                     /region_name="Interaction with NFKB1.
                     /evidence=ECO:0000250|UniProtKB:Q5XPI4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXK7.1)"
     Region          1250..1293
                     /region_name="RING-HC_RNF123"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 123 (RNF123) and similar proteins; cd16541"
                     /db_xref="CDD:438203"
     CDS             1..1312
                     /gene="Rnf123"
                     /coded_by="NM_001191580.1:505..4443"
                     /db_xref="GeneID:100190936"
                     /db_xref="RGD:2301394"
ORIGIN      
        1 mtskgaamsf srksyrltsd aeksrvtgiv qekllsdyly rifsspdhgt paatsrkpln
       61 fhnlpehvdq llqvddeesq gqvegrlgps tvvldhtggf eglllvdddl lgvighsnfg
      121 tirsstcvyk gkwvyevlis sqglmqigwc tincrfnqee gvgdthnsya ydgnrvrkwn
      181 vtttnygkaw aagdivscli dlddgtlsfc lngvslgtaf enlsrglgma yfpaislsfk
      241 esvafnfgsr plrypvagfr plqdppfadl vraqrllgcf qtvlsveldp vegrlvekes
      301 sewqlhgqpt vlltlahifh hfapllrkvy lveavlmsfl lgivekgtpe qaqsvvhqil
      361 dllwlfmedy evqdclkqlm msllrlyrfs pivpdlglqi hylrltmavl rheksrkfll
      421 snvlfdmlrs vvffyikspl rveeaglkel ipttwwphrs sregrdgqea keetteerqr
      481 rrayergcqr lkkrievvee lqvqilklll dnkddnggea sryifltkfr kflqenasgr
      541 gntpvlcppe ymvcflhrlv salrfywdey kasnprasfs deayippqif yngkvdyfdl
      601 qrlggllshl rktlkddlas kanividple lqaatmddld edeepaptaa qrpvqalaig
      661 galplprpgw lssptlgran rflstaavsl mtprrllstm ekvkvrslnv eqrtredieg
      721 shwneglllg rppeeperpl tensllevld gtvmmyslsv hqqlgkmvgv sddvneyama
      781 lrdtedklrr cpkrrkdila eltksqkvfs ekldhlsrrl awvhatvysq ekmldiywll
      841 rvclqtiehg drtgslfafm pefylsvain sysalknyfg pvhsmeelpg yeetltrlaa
      901 ilakhfadpr ivgtdirdsl mqalasyvcy phslraveri peeqriamvr nllapyeqrp
      961 waqtnwilvr lwrgcgfgyr ytrlphllkt kpedanlpsl qkpcpstllq qhmadllrqg
     1021 sdvapsflns vlnqlnwafs efigmiqeiq qaaerlernf vdsrqlkvca tcfdlsvsll
     1081 rvlemtitlv peifldwsrp tsemllrrla qllnqvlnrv taernlfdrv vtlrlpgles
     1141 vdhypilvav tgilvrllah gpsseteqat svlladpcfq lrsiryllgq peplapgsal
     1201 papdrkrfsl qsyadyisae elaqvermla hltaasaqaa aaslptneed lcpicyahpi
     1261 savfqpcghk sckacinqhl mnnkdcffck ativsvedwd kaastsatss aa
//
LOCUS       NP_113786                146 aa            linear   ROD 27-APR-2025
DEFINITION  phospholipase A2, membrane associated precursor [Rattus
            norvegicus].
ACCESSION   NP_113786
VERSION     NP_113786.3
DBSOURCE    REFSEQ: accession NM_031598.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Quindlen-Hotek,J.C., Kartha,S. and Winkelstein,B.A.
  TITLE     Immediate inhibition of spinal secretory phospholipase A2 prevents
            the pain and elevated spinal neuronal hyperexcitability and
            neuroimmune regulatory genes that develop with nerve root
            compression
  JOURNAL   Neuroreport 31 (15), 1084-1089 (2020)
   PUBMED   32881777
  REMARK    GeneRIF: Immediate inhibition of spinal secretory phospholipase A2
            prevents the pain and elevated spinal neuronal hyperexcitability
            and neuroimmune regulatory genes that develop with nerve root
            compression.
REFERENCE   2  (residues 1 to 146)
  AUTHORS   El Hadri,K., Denoyelle,C., Ravaux,L., Viollet,B., Foretz,M.,
            Friguet,B., Rouis,M. and Raymondjean,M.
  TITLE     AMPK Signaling Involvement for the Repression of the
            IL-1beta-Induced Group IIA Secretory Phospholipase A2 Expression in
            VSMCs
  JOURNAL   PLoS One 10 (7), e0132498 (2015)
   PUBMED   26162096
  REMARK    GeneRIF: The present study was designed to determine the
            relationship between phenformin coupling AMP-activated protein
            kinase (AMPK) function and the molecular mechanism by which the
            sPLA2 IIA expression was modulated in vascular smooth muscle cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Boudreau,L.H., Duchez,A.C., Cloutier,N., Soulet,D., Martin,N.,
            Bollinger,J., Pare,A., Rousseau,M., Naika,G.S., Levesque,T.,
            Laflamme,C., Marcoux,G., Lambeau,G., Farndale,R.W., Pouliot,M.,
            Hamzeh-Cognasse,H., Cognasse,F., Garraud,O., Nigrovic,P.A.,
            Guderley,H., Lacroix,S., Thibault,L., Semple,J.W., Gelb,M.H. and
            Boilard,E.
  TITLE     Platelets release mitochondria serving as substrate for
            bactericidal group IIA-secreted phospholipase A2 to promote
            inflammation
  JOURNAL   Blood 124 (14), 2173-2183 (2014)
   PUBMED   25082876
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Sharma,P., Thakran,S., Deng,X., Elam,M.B. and Park,E.A.
  TITLE     Nuclear corepressors mediate the repression of phospholipase A2
            group IIa gene transcription by thyroid hormone
  JOURNAL   J Biol Chem 288 (23), 16321-16333 (2013)
   PUBMED   23629656
  REMARK    GeneRIF: a novel inverse recruitment mechanism in which liganded
            TRbeta recruits corepressors to inhibit PLA2g2a expression.
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Ohara,O., Ishizaki,J., Nakano,T., Arita,H. and Teraoka,H.
  TITLE     A simple and sensitive method for determining transcription
            initiation site: identification of two transcription initiation
            sites in rat group II phospholipase A2 gene
  JOURNAL   Nucleic Acids Res 18 (23), 6997-7002 (1990)
   PUBMED   2263458
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Kusunoki,C., Satoh,S., Kobayashi,M. and Niwa,M.
  TITLE     Structure of genomic DNA for rat platelet phospholipase A2
  JOURNAL   Biochim Biophys Acta 1087 (1), 95-97 (1990)
   PUBMED   2400792
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Komada,M., Kudo,I. and Inoue,K.
  TITLE     Structure of gene coding for rat group II phospholipase A2
  JOURNAL   Biochem Biophys Res Commun 168 (3), 1059-1065 (1990)
   PUBMED   2346480
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Komada,M., Kudo,I., Mizushima,H., Kitamura,N. and Inoue,K.
  TITLE     Structure of cDNA coding for rat platelet phospholipase A2
  JOURNAL   J Biochem 106 (4), 545-547 (1989)
   PUBMED   2606907
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Aarsman,A.J., de Jong,J.G., Arnoldussen,E., Neys,F.W., van
            Wassenaar,P.D. and Van den Bosch,H.
  TITLE     Immunoaffinity purification, partial sequence, and subcellular
            localization of rat liver phospholipase A2
  JOURNAL   J Biol Chem 264 (17), 10008-10014 (1989)
   PUBMED   2722857
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M25148.1, X74364.1 and CB772812.1.
            
            On Mar 27, 2010 this sequence version replaced NP_113786.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ227448.1, D00523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..146
                     /product="phospholipase A2, membrane associated precursor"
                     /EC_number="3.1.1.4"
                     /note="phospholipase A2, membrane associated; platelet
                     phospholipase A2; GIIC sPLA2; group IIA phospholipase A2;
                     phosphatidylcholine 2-acylhydrolase 2A; eted enzyme type
                     IIA phospholipase A2; phospholipase A2, group IIA
                     (platelets, synovial fluid)"
                     /calculated_mol_wt=14081
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2231
     mat_peptide     22..146
                     /product="Phospholipase A2, membrane associated.
                     /id=PRO_0000022752"
                     /note="propagated from UniProtKB/Swiss-Prot (P14423.2)"
                     /calculated_mol_wt=14081
     Region          22..139
                     /region_name="PA2c"
                     /note="Phospholipase A2; smart00085"
                     /db_xref="CDD:214508"
     Site            order(23,26,30,40,51,83)
                     /site_type="active"
                     /note="putative hydrophobic channel [active]"
                     /db_xref="CDD:153091"
     Site            order(48,50,52,69)
                     /site_type="other"
                     /note="primary metal binding site"
                     /db_xref="CDD:153091"
     Site            order(50,68..69,72,87,113)
                     /site_type="active"
                     /note="catalytic network [active]"
                     /db_xref="CDD:153091"
     Site            122
                     /site_type="other"
                     /note="Important for integrin binding.
                     /evidence=ECO:0000250|UniProtKB:P14555; propagated from
                     UniProtKB/Swiss-Prot (P14423.2)"
     CDS             1..146
                     /gene="Pla2g2a"
                     /gene_synonym="sPLA2"
                     /coded_by="NM_031598.3:58..498"
                     /db_xref="GeneID:29692"
                     /db_xref="RGD:620857"
ORIGIN      
        1 mkvllllavv imafgsiqvq gsllefgqmi lfktgkradv sygfygchcg vggrgspkda
       61 tdwccvthdc cynrlekrgc gtkfltykfs yrggqiscst nqdscrkqlc qcdkaaaecf
      121 arnkksyslk yqfypnkfck gktpsc
//
LOCUS       NP_665886                212 aa            linear   ROD 27-APR-2025
DEFINITION  suppressor of cytokine signaling 1 [Rattus norvegicus].
ACCESSION   NP_665886
VERSION     NP_665886.2
DBSOURCE    REFSEQ: accession NM_145879.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Wu,L., Ning,P., Liang,Y., Wang,T., Chen,L., Lu,D. and Tang,H.
  TITLE     Methyltransferase METTL3 regulates neuropathic pain through m6A
            methylation modification of SOCS1
  JOURNAL   Neuropharmacology 261, 110176 (2024)
   PUBMED   39357736
  REMARK    GeneRIF: Methyltransferase METTL3 regulates neuropathic pain
            through m6A methylation modification of SOCS1.
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Shao,Y., Li,Y., Jiang,Y., Li,H., Wang,J. and Zhang,D.
  TITLE     Circulating exosomal miR-155-5p contributes to severe acute
            pancreatitis-associated intestinal barrier injury by targeting
            SOCS1 to activate NLRP3 inflammasome-mediated pyroptosis
  JOURNAL   FASEB J 37 (6), e23003 (2023)
   PUBMED   37219532
  REMARK    GeneRIF: Circulating exosomal miR-155-5p contributes to severe
            acute pancreatitis-associated intestinal barrier injury by
            targeting SOCS1 to activate NLRP3 inflammasome-mediated pyroptosis.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Chen,X., Li,P., Huang,R., Zhang,J., Ouyang,X. and Tan,D.
  TITLE     Ulinastatin affects focal cerebral ischemia-reperfusion injury via
            SOCS1-mediated JAK2/STAT3 signalling pathway
  JOURNAL   Clin Exp Pharmacol Physiol 50 (1), 107-116 (2023)
   PUBMED   36222378
  REMARK    GeneRIF: Ulinastatin affects focal cerebral ischemia-reperfusion
            injury via SOCS1-mediated JAK2/STAT3 signalling pathway.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zhang,Y., Jing,Z., Cao,X., Wei,Q., He,W., Zhang,N., Liu,Y.,
            Yuan,Q., Zhuang,Z., Dong,Y., Hong,Z., Li,J., Li,P., Zhang,L.,
            Wang,H. and Li,W.
  TITLE     SOCS1, the feedback regulator of STAT1/3, inhibits the osteogenic
            differentiation of rat bone marrow mesenchymal stem cells
  JOURNAL   Gene 821, 146190 (2022)
   PUBMED   35124149
  REMARK    GeneRIF: SOCS1, the feedback regulator of STAT1/3, inhibits the
            osteogenic differentiation of rat bone marrow mesenchymal stem
            cells.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Yang,J., Zhu,X., Hu,H. and Lin,X.
  TITLE     The inhibitory effect of Gualou Guizhi Decoction on post-ischemic
            neuroinflammation via miR-155 in MCAO rats
  JOURNAL   Ann Palliat Med 10 (2), 1370-1379 (2021)
   PUBMED   33081480
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Schluter,G., Boinska,D. and Nieman-Seyde,S.C.
  TITLE     Evidence for translational repression of the SOCS-1 major open
            reading frame by an upstream open reading frame
  JOURNAL   Biochem Biophys Res Commun 268 (2), 255-261 (2000)
   PUBMED   10679190
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Dey,B.R., Spence,S.L., Nissley,P. and Furlanetto,R.W.
  TITLE     Interaction of human suppressor of cytokine signaling (SOCS)-2 with
            the insulin-like growth factor-I receptor
  JOURNAL   J Biol Chem 273 (37), 24095-24101 (1998)
   PUBMED   9727029
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Naka,T., Narazaki,M., Hirata,M., Matsumoto,T., Minamoto,S.,
            Aono,A., Nishimoto,N., Kajita,T., Taga,T., Yoshizaki,K., Akira,S.
            and Kishimoto,T.
  TITLE     Structure and function of a new STAT-induced STAT inhibitor
  JOURNAL   Nature 387 (6636), 924-929 (1997)
   PUBMED   9202127
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Endo,T.A., Masuhara,M., Yokouchi,M., Suzuki,R., Sakamoto,H.,
            Mitsui,K., Matsumoto,A., Tanimura,S., Ohtsubo,M., Misawa,H.,
            Miyazaki,T., Leonor,N., Taniguchi,T., Fujita,T., Kanakura,Y.,
            Komiya,S. and Yoshimura,A.
  TITLE     A new protein containing an SH2 domain that inhibits JAK kinases
  JOURNAL   Nature 387 (6636), 921-924 (1997)
   PUBMED   9202126
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Schluter,G., Celik,A., Obata,R., Schlicker,M., Hofferbert,S.,
            Schlung,A., Adham,I.M. and Engel,W.
  TITLE     Sequence analysis of the conserved protamine gene cluster shows
            that it contains a fourth expressed gene
  JOURNAL   Mol Reprod Dev 43 (1), 1-6 (1996)
   PUBMED   8720108
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW917497.1 and JAXUCZ010000010.1.
            
            On Mar 13, 2014 this sequence version replaced NP_665886.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW917497.1, CB557066.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            regulatory uORF        :: PMID: 10679190
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..212
                     /product="suppressor of cytokine signaling 1"
                     /note="cytokine inducible SH2-containing protein 1"
                     /calculated_mol_wt=23610
     Region          1..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX78.1)"
     Region          56..67
                     /region_name="Kinase inhibitory region (KIR)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX78.1)"
     Region          68..79
                     /region_name="Extended SH2 subdomain (ESS)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX78.1)"
     Region          69..166
                     /region_name="SH2_SOCS1"
                     /note="Src homology 2 (SH2) domain found in suppressor of
                     cytokine signaling (SOCS) proteins; cd10382"
                     /db_xref="CDD:198245"
     Site            order(87,105,107,115,128)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198245"
     Site            order(138,140,155)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198245"
     Region          170..212
                     /region_name="SOCS"
                     /note="SOCS (suppressors of cytokine signaling) box. The
                     SOCS box is found in the C-terminal region of CIS/SOCS
                     family proteins (in combination with a SH2 domain), ASBs
                     (ankyrin repeat-containing proteins with a SOCS box), SSBs
                     (SPRY domain-containing proteins...; cl02533"
                     /db_xref="CDD:470605"
     Site            order(171..176,182,189,195)
                     /site_type="active"
                     /note="elongin B/C interaction [active]"
                     /db_xref="CDD:239704"
     Region          174..183
                     /region_name="Interaction with Elongin BC complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX78.1)"
     CDS             1..212
                     /gene="Socs1"
                     /gene_synonym="Cish1; Socs-1"
                     /coded_by="NM_145879.2:133..771"
                     /db_xref="GeneID:252971"
                     /db_xref="RGD:69272"
ORIGIN      
        1 mvarnqvaad naispasepr rrpepsssss ssspaaparp rpcpvvpapa pgdthfrtfr
       61 shsdyrritr tsalldacgf ywgplsvhga herlraepvg tflvrdsrqr ncffalsvkm
      121 asgptsirvh fqagrfhldg sretfdclfe llehyvaapr rmlgaplrqr rvrplqelcr
      181 qrivaavgre nlariplnpv lrdylssfpf qi
//
LOCUS       NP_001093962             116 aa            linear   ROD 27-APR-2025
DEFINITION  host cell factor C1 regulator 1 [Rattus norvegicus].
ACCESSION   NP_001093962 XP_001055621 XP_002724706 XP_002724707 XP_573052
VERSION     NP_001093962.1
DBSOURCE    REFSEQ: accession NM_001100492.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM050402.1, AY245001.1, BC168753.1 and BG373213.1.
            
            On or before May 30, 2010 this sequence version replaced
            XP_002724706.1, XP_001055621.1, XP_002724707.1, XP_573052.3.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Both variants 1 and 2 encode the same
            protein.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..116
                     /product="host cell factor C1 regulator 1"
                     /note="HCF-1 beta-propeller-interacting protein; inhibitor
                     of four 2; host cell factor C1 regulator 1
                     (XPO1-dependent)"
                     /calculated_mol_wt=12860
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     Region          2..112
                     /region_name="HPIP"
                     /note="HCF-1 beta-propeller-interacting protein family;
                     pfam15226"
                     /db_xref="CDD:373659"
     Region          54..57
                     /region_name="Interaction with HCFC1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     Region          88..97
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80V38.2)"
     CDS             1..116
                     /gene="Hcfc1r1"
                     /gene_synonym="Hpip"
                     /coded_by="NM_001100492.1:49..399"
                     /db_xref="GeneID:287097"
                     /db_xref="RGD:727975"
ORIGIN      
        1 milqqplerg ppgrdpratt gvtlgldtre plhkhflsee nmathfsrls lhndhpycsp
       61 pvtfpealpp lrspcpelll wrypgslipe alrllrlgdn pspyysaspa geimel
//
LOCUS       NP_001257782             440 aa            linear   ROD 27-APR-2025
DEFINITION  aromatic-L-amino-acid decarboxylase isoform b [Rattus norvegicus].
ACCESSION   NP_001257782
VERSION     NP_001257782.1
DBSOURCE    REFSEQ: accession NM_001270853.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Seo,D.C., Ju,Y.H., Seo,J.J., Oh,S.J., Lee,C.J., Lee,S.E. and
            Nam,M.H.
  TITLE     DDC-Promoter-Driven Chemogenetic Activation of SNpc Dopaminergic
            Neurons Alleviates Parkinsonian Motor Symptoms
  JOURNAL   Int J Mol Sci 24 (3), 2491 (2023)
   PUBMED   36768816
  REMARK    GeneRIF: DDC-Promoter-Driven Chemogenetic Activation of SNpc
            Dopaminergic Neurons Alleviates Parkinsonian Motor Symptoms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Sizova,D., Velazquez,H., Sampaio-Maia,B., Quelhas-Santos,J.,
            Pestana,M. and Desir,G.V.
  TITLE     Renalase regulates renal dopamine and phosphate metabolism
  JOURNAL   Am J Physiol Renal Physiol 305 (6), F839-F844 (2013)
   PUBMED   23863468
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Voigt,A., Hubner,S., Lossow,K., Hermans-Borgmeyer,I., Boehm,U. and
            Meyerhof,W.
  TITLE     Genetic labeling of Tas1r1 and Tas2r131 taste receptor cells in
            mice
  JOURNAL   Chem Senses 37 (9), 897-911 (2012)
   PUBMED   23010799
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Rouzaud-Laborde,C., Hanoun,N., Baysal,I., Rech,J.S., Mias,C.,
            Calise,D., Sicard,P., Frugier,C., Seguelas,M.H., Parini,A. and
            Pizzinat,N.
  TITLE     Role of endothelial AADC in cardiac synthesis of serotonin and
            nitrates accumulation
  JOURNAL   PLoS One 7 (7), e34893 (2012)
   PUBMED   22829864
  REMARK    GeneRIF: The data show that endothelial AADC plays an important
            role in cardiac synthesis of 5-HT and possibly in 5-HT-dependent
            regulation of nitric oxide generation.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Brun,L., Ngu,L.H., Keng,W.T., Ch'ng,G.S., Choy,Y.S., Hwu,W.L.,
            Lee,W.T., Willemsen,M.A., Verbeek,M.M., Wassenberg,T., Regal,L.,
            Orcesi,S., Tonduti,D., Accorsi,P., Testard,H., Abdenur,J.E.,
            Tay,S., Allen,G.F., Heales,S., Kern,I., Kato,M., Burlina,A.,
            Manegold,C., Hoffmann,G.F. and Blau,N.
  TITLE     Clinical and biochemical features of aromatic L-amino acid
            decarboxylase deficiency
  JOURNAL   Neurology 75 (1), 64-71 (2010)
   PUBMED   20505134
  REMARK    Erratum:[Neurology. 2010 Aug 10;75(6):576. Dosage error in article
            text]
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Rorsman,F., Husebye,E.S., Winqvist,O., Bjork,E., Karlsson,F.A. and
            Kampe,O.
  TITLE     Aromatic-L-amino-acid decarboxylase, a pyridoxal
            phosphate-dependent enzyme, is a beta-cell autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8626-8629 (1995)
   PUBMED   7567987
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Eaton,M.J., Gudehithlu,K.P., Quach,T., Silvia,C.P.,
            Hadjiconstantinou,M. and Neff,N.H.
  TITLE     Distribution of aromatic L-amino acid decarboxylase mRNA in mouse
            brain by in situ hybridization histology
  JOURNAL   J Comp Neurol 337 (4), 640-654 (1993)
   PUBMED   7904615
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Albert,V.R., Lee,M.R., Bolden,A.H., Wurzburger,R.J. and Aguanno,A.
  TITLE     Distinct promoters direct neuronal and nonneuronal expression of
            rat aromatic L-amino acid decarboxylase
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12053-12057 (1992)
   PUBMED   1465439
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Tanaka,T., Horio,Y., Taketoshi,M., Imamura,I., Ando-Yamamoto,M.,
            Kangawa,K., Matsuo,H., Kuroda,M. and Wada,H.
  TITLE     Molecular cloning and sequencing of a cDNA of rat dopa
            decarboxylase: partial amino acid homologies with other enzymes
            synthesizing catecholamines
  JOURNAL   Proc Natl Acad Sci U S A 86 (20), 8142-8146 (1989)
   PUBMED   2813383
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Yamazaki,N. and Sudo,J.
  TITLE     Activities of aromatic L-amino acid decarboxylase with L-dopa as
            substrate in brush-border- and basolateral membranes and cytoplasm
            obtained from rat renal cortex
  JOURNAL   Jpn J Pharmacol 46 (2), 193-196 (1988)
   PUBMED   3379830
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JF273828.1, M27716.1 and JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate in-frame exon in the coding region compared to
            variant 1. The resulting protein (isoform b) is shorter but has the
            same N- and C-termini compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: JF273828.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..440
                     /product="aromatic-L-amino-acid decarboxylase isoform b"
                     /EC_number="4.1.1.28"
                     /note="aromatic-L-amino-acid decarboxylase; L-Dopa
                     decarboxylase; dopa decarboxylase (aromatic L-amino acid
                     decarboxylase)"
                     /calculated_mol_wt=49790
     Region          35..374
                     /region_name="Pyridoxal_deC"
                     /note="Pyridoxal-dependent decarboxylase conserved domain;
                     pfam00282"
                     /db_xref="CDD:395219"
     Site            order(109,112,202,231,234,260,263)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99743"
     Site            263
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99743"
     CDS             1..440
                     /gene="Ddc"
                     /gene_synonym="AADC"
                     /coded_by="NM_001270853.1:48..1370"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:24311"
                     /db_xref="RGD:2494"
ORIGIN      
        1 mdsrefrrrg kemvdyiady ldgiegrpvy pdvepgylra lipttapqep etyediirdi
       61 ekiimpgvth whspyffayf ptassypaml admlcgaigc igfswgsase atlvallaar
      121 tkmirqlqaa speltqaalm eklvaytsdq ahssveragl iggvkikaip sdgnysmraa
      181 alrealerdk aaglipffvv vtlgttsccs fdnllevgpi cnqegvwlhi daayagsafi
      241 cpefryllng vefadsfnfn phkwllvnfd csamwvkkrt dlteafnmdp vylrhshqds
      301 glitdyrhwq iplgrrfrsl kmwfvfrmyg vkglqayirk hvklshefes lvrqdprfei
      361 ctevilglvc frlkgsnqln etllqrinsa kkihlvpcrl rdkfvlrfav csrtvesahv
      421 qlawehirdl assvlraeke
//
LOCUS       NP_114173                352 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 5 [Rattus norvegicus].
ACCESSION   NP_114173
VERSION     NP_114173.2
DBSOURCE    REFSEQ: accession NM_031967.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1, CB585874.1 and CB713901.1.
            
            On Aug 31, 2012 this sequence version replaced NP_114173.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (5)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY255791.1, AF045564.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..352
                     /product="protein NDRG4 isoform 5"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=38329
     Region          8..290
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2L9.1)"
     Region          301..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2L9.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2L9.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTG7; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2L9.1)"
     CDS             1..352
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_031967.2:130..1188"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 mpecwdgehd ietpygllhv virgspkgnr pailtyhdvg lnhklcfntl fnledmqeit
       61 khfvvchvda pgqqvgasqf pqgyqfpsme qlatmlpsvv qhfgfkyvig igvgagayvl
      121 akfalifpdl veglvlmnid pngkgwidwa atklsgltst lpdtvlshlf sqeelvnnte
      181 lvqsyrqqis svvnqanlql fwnmynsrrd ldinrpgtvp naktlrcpvm lvvgdnapae
      241 dgvvecnskl dpttttflkm adsgglpqvt qpgklteafk yflqgmgyia hlkdrrlsgg
      301 avpsasmtrl arsrtaslts assvdgsrpq pcthsdsseg mgqvnhtmev sc
//
LOCUS       NP_036958                296 aa            linear   ROD 27-APR-2025
DEFINITION  zinc-alpha-2-glycoprotein precursor [Rattus norvegicus].
ACCESSION   NP_036958
VERSION     NP_036958.2
DBSOURCE    REFSEQ: accession NM_012826.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kim,S.H., Oh,J.M., Roh,H., Lee,K.W., Lee,J.H. and Lee,W.J.
  TITLE     Zinc-Alpha-2-Glycoprotein Peptide Downregulates Type I and III
            Collagen Expression via Suppression of TGF-beta and p-Smad 2/3
            Pathway in Keloid Fibroblasts and Rat Incisional Model
  JOURNAL   Tissue Eng Regen Med 21 (7), 1079-1092 (2024)
   PUBMED   39105875
  REMARK    GeneRIF: Zinc-Alpha-2-Glycoprotein Peptide Downregulates Type I and
            III Collagen Expression via Suppression of TGF-beta and p-Smad 2/3
            Pathway in Keloid Fibroblasts and Rat Incisional Model.
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Jain,A., Kotimoole,C.N., Ghoshal,S., Bakshi,J., Chatterjee,A.,
            Prasad,T.S.K. and Pal,A.
  TITLE     Identification of potential salivary biomarker panels for oral
            squamous cell carcinoma
  JOURNAL   Sci Rep 11 (1), 3365 (2021)
   PUBMED   33564003
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Tan,C., Liu,X., Peng,W., Wang,H., Zhou,W., Jiang,J., Wei,X., Mo,L.,
            Chen,Y. and Chen,L.
  TITLE     Seizure-induced impairment in neuronal ketogenesis: Role of
            zinc-alpha2-glycoprotein in mitochondria
  JOURNAL   J Cell Mol Med 24 (12), 6833-6845 (2020)
   PUBMED   32340079
  REMARK    GeneRIF: Seizure-induced impairment in neuronal ketogenesis: Role
            of zinc-alpha2-glycoprotein in mitochondria.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Yu,W., Ling,J., Yu,H., Du,J. and Liu,T.
  TITLE     AZGP1 suppresses the process of colorectal cancer after
            upregulating FASN expression via mTOR signal pathway
  JOURNAL   Gen Physiol Biophys 39 (3), 239-248 (2020)
   PUBMED   32525817
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Wei,X., Liu,X., Tan,C., Mo,L., Wang,H., Peng,W., Zhou,W., Jiang,J.,
            Deng,F. and Chen,L.
  TITLE     Insulin attenuates epileptiform discharge-induced oxidative stress
            by increasing zinc-alpha2-glycoprotein in primary cultured cortical
            neurons
  JOURNAL   Neuroreport 30 (8), 580-585 (2019)
   PUBMED   30950934
  REMARK    GeneRIF: Insulin attenuates epileptiform discharge-induced
            oxidative stress by increasing zinc-alpha2-glycoprotein in primary
            cultured cortical neurons.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Hale,L.P., Price,D.T., Sanchez,L.M., Demark-Wahnefried,W. and
            Madden,J.F.
  TITLE     Zinc alpha-2-glycoprotein is expressed by malignant prostatic
            epithelium and may serve as a potential serum marker for prostate
            cancer
  JOURNAL   Clin Cancer Res 7 (4), 846-853 (2001)
   PUBMED   11309332
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Ogikubo,O., Maeda,T., Yamane,T., Ohtsuka,T., Ohkubo,I.,
            Takahashi,S., Ohnishi,S. and Matsui,N.
  TITLE     Regulation of Zn-alpha2-glycoprotein-mediated cell adhesion by
            kininogens and their derivatives
  JOURNAL   Biochem Biophys Res Commun 252 (1), 257-262 (1998)
   PUBMED   9813179
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Uria,J.A., Fueyo,A., Balbin,M., Velasco,G., Pendas,A.M. and
            Lopez-Otin,C.
  TITLE     Alternative splicing gives rise to two novel long isoforms of
            Zn-alpha 2-glycoprotein, a member of the immunoglobulin superfamily
  JOURNAL   Gene 169 (2), 233-236 (1996)
   PUBMED   8647453
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Ueyama,H., Naitoh,H. and Ohkubo,I.
  TITLE     Structure and expression of rat and mouse mRNAs for Zn-alpha
            2-glycoprotein
  JOURNAL   J Biochem 116 (3), 677-681 (1994)
   PUBMED   7852290
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Fueyo,A., Uria,J.A., Freije,J.M. and Lopez-Otin,C.
  TITLE     Cloning and expression analysis of the cDNA encoding rat Zn-alpha
            2-glycoprotein
  JOURNAL   Gene 145 (2), 245-249 (1994)
   PUBMED   8056339
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105822.1.
            
            On Aug 18, 2012 this sequence version replaced NP_036958.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105822.1, FQ219362.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q11"
     Protein         1..296
                     /product="zinc-alpha-2-glycoprotein precursor"
                     /note="zinc-alpha-2-glycoprotein; zn-alpha-2-GP;
                     zn-alpha-2-glycoprotein; alpha-2 - glycoprotein 1, zinc;
                     Zn - alpha2 - glycoprotein; alpha-2-glycoprotein 1, zinc"
                     /calculated_mol_wt=32306
     sig_peptide     1..17
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q63678.1)"
                     /calculated_mol_wt=1745
     mat_peptide     18..296
                     /product="Zinc-alpha-2-glycoprotein. /id=PRO_0000019014"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63678.1)"
                     /calculated_mol_wt=32306
     Site            18
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P25311; propagated from
                     UniProtKB/Swiss-Prot (Q63678.1)"
     Region          21..196
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; cl08246"
                     /db_xref="CDD:471794"
     Site            123
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63678.1)"
     Region          198..290
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          216..220
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          231..235
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63678.1)"
     Region          261..265
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          272..277
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          287..290
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..296
                     /gene="Azgp1"
                     /gene_synonym="ZA2GA; Zna2gp"
                     /coded_by="NM_012826.2:19..909"
                     /db_xref="GeneID:25294"
                     /db_xref="RGD:2187"
ORIGIN      
        1 mvpvllslpl llgpavlqet gsysliflyt glsrpskgll rfqataflnd qaffhynsns
       61 gkaepvepws hvegmedwek esqlqraree iflvtlkdim dyyedstgsh tfqgmfgcei
      121 tnnrssgavw ryaydgedfi efnkeipawi pldpaaantk lkweaekvyv qrakayleee
      181 cptmlkkylt ysrshldrtd pptvkitsrv apgrnrifrc laydfypqri slhwnqaskk
      241 lasepergvf pngngtylsw mevevppqnr dpfvchiehk glsqslsvqw dekskv
//
LOCUS       NP_001258368            1015 aa            linear   ROD 27-APR-2025
DEFINITION  PHD finger protein 20-like protein 1 [Rattus norvegicus].
ACCESSION   NP_001258368 XP_003754357
VERSION     NP_001258368.1
DBSOURCE    REFSEQ: accession NM_001271439.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Sep 25, 2012 this sequence version replaced XP_003754357.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..1015
                     /product="PHD finger protein 20-like protein 1"
                     /note="tudor domain-containing protein PHF20L1"
                     /calculated_mol_wt=113954
     Region          13..72
                     /region_name="MBT_PHF20L1-like"
                     /note="malignant brain tumor (MBT) repeat found in PHD
                     finger protein 20-like protein 1 (PHF20L1) and similar
                     domains; cd20104"
                     /db_xref="CDD:439094"
     Site            order(23,26..27,29,47,50,54)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439094"
     Region          86..143
                     /region_name="Tudor_PHF20L1"
                     /note="Tudor domain found in PHD finger protein 20-like
                     protein 1 (PHF20L1) and similar proteins; cd20454"
                     /db_xref="CDD:410525"
     Region          183..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          197..300
                     /region_name="DUF3776"
                     /note="Protein of unknown function (DUF3776); pfam12618"
                     /db_xref="CDD:463645"
     Region          309..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          <315..519
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          318..383
                     /region_name="PHD20L1_u1"
                     /note="PHD finger protein 20-like protein 1; pfam16660"
                     /db_xref="CDD:465222"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          389..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A8MW92; propagated from
                     UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          478..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          539..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Region          683..728
                     /region_name="PHD_PHF20L1"
                     /note="PHD finger found in PHD finger protein 20-like
                     protein 1 (P20L1); cd15633"
                     /db_xref="CDD:277103"
     Site            order(683,694..698,702,721)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277103"
     Region          859..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V9H5.2)"
     Site            907
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A8MW92; propagated from
                     UniProtKB/Swiss-Prot (Q4V9H5.2)"
     CDS             1..1015
                     /gene="Phf20l1"
                     /coded_by="NM_001271439.1:319..3366"
                     /db_xref="GeneID:314964"
                     /db_xref="RGD:1560141"
ORIGIN      
        1 mskkppnrpg itfeigarle aldylqkwyp sriekidyee gkmlvhferw shrydewiyw
       61 dsnrlrpler pslrkeglkd eedlfdfkag eevlarwtdc ryypakieai nkegtftvqf
      121 ydgvirclkr mhikampeda kgqvksqhpl swccpidpag scnqsmgsed wialvkaaaa
      181 aaaknktgsk prtsansnke kerdggkwfk vpskkaetst civtaeiekk eelptssepf
      241 glhidsvpki vfpqpestlt nkrknnqgns fqakrarlnk itgllaskav gvdgaekked
      301 csatapvleq aispkpqsqk kneavisssa ntqkpallss tlssgkarsk kckhesgess
      361 gcikapkspl apeliqakdl tlvsqlssvi nktsspqpvn pprpckhser rrrsqrlatl
      421 pmpddslekl sssssatdgk vfsissqnqq essvpevpai ayvplqklgp clpldlscgs
      481 evtgsqapds sypggecpre ekeetplfan ptskvvsdvk gaaaatgilk tekkvkleek
      541 tstafgkrke kdkerkekrd kdhykpkqkk kkkkkkkskq hdysdyedss ldflercssp
      601 ltrssgssla prstftektt tyqyprails vdlsgenlsd veflddsste slllsgdeyn
      661 qdfdstnfee sqdeddalne ivrcicelde engfmiqcee clcwqhsvcm glledsipeq
      721 yicyicrdpp gqrwnakyry dkewlnngrm yglsfvkeny shlnakkivs thhlladvyg
      781 itevlhglql kigilknkhh pdlrlwaysg krkdqdqvva gaerkvilqd tansegrkyv
      841 qnhkepplkm eetyitsehs yqkpqsfsqd chsltdpgss ddddvssfee dgelhvadns
      901 hllysvkerg vseknpasen kvfvyndkkg megpgdahlq wqlnllthie nvqnevtsrm
      961 dliekevdvl eswldftgel eppdplarlp qlkrhikqll ldmgkvqqia tlcsv
//
LOCUS       NP_001289141            1420 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 7 precursor [Rattus
            norvegicus].
ACCESSION   NP_001289141
VERSION     NP_001289141.1
DBSOURCE    REFSEQ: accession NM_001302212.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1420)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1420)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1420)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1420)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1420)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1420)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1420)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1420)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1420)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081149.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            Transcript Variant: This variant (7) lacks three exons in the 3'
            coding region, but maintains the reading frame, compared to variant
            1. The resulting isoform (7) lacks two internal segments, compared
            to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081149.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1420
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1420
                     /product="adhesion G protein-coupled receptor L2 isoform 7
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=156568
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          848..1105
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320672"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320672"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320672"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320672"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1041..1063
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1067..1092
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320672"
     Region          1104..1420
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     CDS             1..1420
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001302212.1:463..4725"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleniksw vlgafallcl lgltwsfgll fvneetvvma ylftafnafq
     1081 glfififhca lqkkvrkeya kcfrhwyccg glptesphss vkastsrtsa ryssgtqsri
     1141 rrmwndtvrk qsessfisgd inststlnqg hslnntrdts amdtlplngn fnnsyslrka
     1201 dyhdgvqvvd cglslndtaf ekmiiselvh nnlrgsnkth nlelklpvkp viggsssedd
     1261 aivadasslm hgdnpglefr hkeleaplip qrthsllyqp qkkvkpeatd syvsqltaea
     1321 dehlqspnrd slytsmpnlr dspypesspd maedlspsrr senediyyks mpnlgagrql
     1381 qmcyqisrgn sdgyiipink egcipegdvr egqmqlvtsl
//
LOCUS       NP_036789                416 aa            linear   ROD 27-APR-2025
DEFINITION  serine protease inhibitor A3K precursor [Rattus norvegicus].
ACCESSION   NP_036789
VERSION     NP_036789.2
DBSOURCE    REFSEQ: accession NM_012657.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Sanchez-Navarro,A., Murillo-de-Ozores,A.R., Perez-Villalva,R.,
            Linares,N., Carbajal-Contreras,H., Flores,M.E., Gamba,G.,
            Castaneda-Bueno,M. and Bobadilla,N.A.
  TITLE     Transient response of serpinA3 during cellular stress
  JOURNAL   FASEB J 36 (3), e22190 (2022)
   PUBMED   35147994
  REMARK    GeneRIF: Transient response of serpinA3 during cellular stress.
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Dai,Z., Lu,L., Yang,Z., Mao,Y., Lu,J., Li,C., Qi,W., Chen,Y.,
            Yao,Y., Li,L., Chen,S., Zhang,Y., Cai,W., Yang,X. and Gao,G.
  TITLE     Kallikrein-binding protein inhibits LPS-induced TNF-alpha by
            upregulating SOCS3 expression
  JOURNAL   J Cell Biochem 114 (5), 1020-1028 (2013)
   PUBMED   23129128
  REMARK    GeneRIF: KBP suppressed lipopolysaccharide-induced TNF-alpha
            production via upregulating SOCS3 expression.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hoffmann,D.C., Textoris,C., Oehme,F., Klaassen,T., Goppelt,A.,
            Romer,A., Fugmann,B., Davidson,J.M., Werner,S., Krieg,T. and
            Eming,S.A.
  TITLE     Pivotal role for alpha1-antichymotrypsin in skin repair
  JOURNAL   J Biol Chem 286 (33), 28889-28901 (2011)
   PUBMED   21693707
  REMARK    GeneRIF: Pivotal role for alpha1-antichymotrypsin in skin repair
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Zhang,B., Zhou,K.K. and Ma,J.X.
  TITLE     Inhibition of connective tissue growth factor overexpression in
            diabetic retinopathy by SERPINA3K via blocking the WNT/beta-catenin
            pathway
  JOURNAL   Diabetes 59 (7), 1809-1816 (2010)
   PUBMED   20299474
  REMARK    GeneRIF: SERPINA3K is an antifibrogenic factor, and its
            antifibrogenic activity is through blocking the Wnt pathway.
            Decreased SERPINA3K levels may contribute to the fibrosis in
            diabetic retinopathy.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Zhang,B., Abreu,J.G., Zhou,K., Chen,Y., Hu,Y., Zhou,T., He,X. and
            Ma,J.X.
  TITLE     Blocking the Wnt pathway, a unifying mechanism for an angiogenic
            inhibitor in the serine proteinase inhibitor family
  JOURNAL   Proc Natl Acad Sci U S A 107 (15), 6900-6905 (2010)
   PUBMED   20351274
  REMARK    GeneRIF: SERPINA3K is a high-affinity, endogenous antagonist of
            LRP6
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Chai,K.X., Ma,J.X., Murray,S.R., Chao,J. and Chao,L.
  TITLE     Molecular cloning and analysis of the rat kallikrein-binding
            protein gene
  JOURNAL   J Biol Chem 266 (24), 16029-16036 (1991)
   PUBMED   1874745
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Ohkubo,K., Ogata,S., Misumi,Y., Takami,N. and Ikehara,Y.
  TITLE     Molecular cloning and characterization of rat contrapsin-like
            protease inhibitor and related proteins
  JOURNAL   J Biochem 109 (2), 243-250 (1991)
   PUBMED   1864837
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Pages,G., Rouayrenc,J.F., Rossi,V., Le Cam,G., Mariller,M.,
            Szpirer,J., Szpirer,C., Levan,G. and Le Cam,A.
  TITLE     Primary structure and assignment to chromosome 6 of three related
            rat genes encoding liver serine protease inhibitors
  JOURNAL   Gene 94 (2), 273-282 (1990)
   PUBMED   2258058
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Chao,J., Chai,K.X., Chen,L.M., Xiong,W., Chao,S.,
            Woodley-Miller,C., Wang,L.X., Lu,H.S. and Chao,L.
  TITLE     Tissue kallikrein-binding protein is a serpin. I. Purification,
            characterization, and distribution in normotensive and
            spontaneously hypertensive rats
  JOURNAL   J Biol Chem 265 (27), 16394-16401 (1990)
   PUBMED   2398056
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Pages,G., Rouayrenc,J.F., Le Cam,G., Mariller,M. and Le Cam,A.
  TITLE     Molecular characterization of three rat liver serine-protease
            inhibitors affected by inflammation and hypophysectomy. Protein and
            mRNA analysis and cDNA cloning
  JOURNAL   Eur J Biochem 190 (2), 385-391 (1990)
   PUBMED   1694763
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC062236.1, CO560755.1 and JAXUCZ010000006.1.
            
            On Sep 27, 2011 this sequence version replaced NP_036789.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062236.1, FQ210286.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..416
                     /product="serine protease inhibitor A3K precursor"
                     /note="serine protease inhibitor 2b; serine protease
                     inhibitor A3K; thyroid hormone-regulated protein;
                     kallistatin; serine (or cysteine) peptidase inhibitor,
                     clade A, member 3K; serpin A3K; kallikrein-binding
                     protein; contrapsin-like protease inhibitor 1; growth
                     hormone-regulated proteinase inhibitor"
                     /calculated_mol_wt=44517
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1979
     mat_peptide     21..416
                     /product="Serine protease inhibitor A3K.
                     /id=PRO_0000032421"
                     /note="propagated from UniProtKB/Swiss-Prot (P05545.3)"
                     /calculated_mol_wt=44517
     Region          36..416
                     /region_name="serpinA3_A1AC"
                     /note="serpin family A member 3, alpha 1-antichymotrypsin;
                     cd19551"
                     /db_xref="CDD:381019"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05545.3)"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05545.3)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05545.3)"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05545.3)"
     Site            order(363..375,377..381,385..393)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381019"
     Region          365..392
                     /region_name="RCL"
                     /note="propagated from UniProtKB/Swiss-Prot (P05545.3)"
     Site            379..380
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P05545.3)"
     CDS             1..416
                     /gene="Serpina3c"
                     /gene_synonym="CPi-21; GHR-P63; Kbp; Klkbp; Serpina3k;
                     SPI-2; SPI-2.3; SPI2; Spin2; Spin2b"
                     /coded_by="NM_012657.2:95..1345"
                     /db_xref="GeneID:24794"
                     /db_xref="RGD:2972"
ORIGIN      
        1 mafiaalgll magicpavlc dgilgrdtlp hedqgkgrql hsltlasint dftlslykkl
       61 alrnpdknvv fsplsisaal ailslgakds tmeeileglk fnlteiteee ihqgfghllq
      121 rlsqpedqae intgsalfid keqpilsefq ektralyqae afvadfkqcn eakkfindyv
      181 snqtqgkiae lfsdlderts mvlvnyllfk gkwkvpfnpn dtfesefyld ekrsvkvpmm
      241 kikdlttpyv rdeelscsvl elkytgnasa lfilpdqgkm qqvesslqpe tlkkwkdslr
      301 priiselrmp kfsistdynl eevlpelgir kifsqqadls ritgtknlhv sqvvhkavld
      361 vdetgtegaa atavtaalks lpqtvpllnf nrpfmlvitd nngqsvffmg kvtnpm
//
LOCUS       NP_077334               2471 aa            linear   ROD 27-APR-2025
DEFINITION  neurogenic locus notch homolog protein 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_077334
VERSION     NP_077334.2
DBSOURCE    REFSEQ: accession NM_024358.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2471)
  AUTHORS   Deng,J., Liang,J., Cao,Y., Tong,X. and Li,H.
  TITLE     CCL2- and Notch2-mediated Central Sensitization in a Rat Chronic
            Pelvic Pain Model
  JOURNAL   In Vivo 38 (1), 205-212 (2024)
   PUBMED   38148075
  REMARK    GeneRIF: CCL2- and Notch2-mediated Central Sensitization in a Rat
            Chronic Pelvic Pain Model.
REFERENCE   2  (residues 1 to 2471)
  AUTHORS   Li,S., Huang,C., Tu,C., Chen,R., Ren,X., Qi,L. and Li,Z.
  TITLE     Bone marrow mesenchymal stem cell-derived exosomes shuttling
            miR-150-5p alleviates mechanical allodynia in rats by targeting
            NOTCH2 in microglia
  JOURNAL   Mol Med 28 (1), 133 (2022)
   PUBMED   36348269
  REMARK    GeneRIF: Bone marrow mesenchymal stem cell-derived exosomes
            shuttling miR-150-5p alleviates mechanical allodynia in rats by
            targeting NOTCH2 in microglia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2471)
  AUTHORS   Wang,X., Xu,Q. and Wang,S.
  TITLE     Overexpression of miR-149-5p Attenuates Cerebral
            Ischemia/Reperfusion (I/R) Injury by Targeting Notch2
  JOURNAL   Neuromolecular Med 24 (3), 279-289 (2022)
   PUBMED   34581980
  REMARK    GeneRIF: Overexpression of miR-149-5p Attenuates Cerebral
            Ischemia/Reperfusion (I/R) Injury by Targeting Notch2.
REFERENCE   4  (residues 1 to 2471)
  AUTHORS   Fang,Y., Che,X., You,M., Xu,Y. and Wang,Y.
  TITLE     Perinatal exposure to nonylphenol promotes proliferation of granule
            cell precursors in offspring cerebellum: Involvement of the
            activation of Notch2 signaling
  JOURNAL   Neurochem Int 140, 104843 (2020)
   PUBMED   32866557
  REMARK    GeneRIF: Perinatal exposure to nonylphenol promotes proliferation
            of granule cell precursors in offspring cerebellum: Involvement of
            the activation of Notch2 signaling.
REFERENCE   5  (residues 1 to 2471)
  AUTHORS   Huang,K.C., Chuang,P.Y., Yang,T.Y., Huang,T.W. and Chang,S.F.
  TITLE     Hyperglycemia inhibits osteoblastogenesis of rat bone marrow
            stromal cells via activation of the Notch2 signaling pathway
  JOURNAL   Int J Med Sci 16 (5), 696-703 (2019)
   PUBMED   31217737
  REMARK    GeneRIF: Hyperglycemia might inhibit osteoblastogenesis of
            mesenchymal progenitors via activation of the Notch2 signaling
            pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2471)
  AUTHORS   Irvin,D.K., Zurcher,S.D., Nguyen,T., Weinmaster,G. and
            Kornblum,H.I.
  TITLE     Expression patterns of Notch1, Notch2, and Notch3 suggest multiple
            functional roles for the Notch-DSL signaling system during brain
            development
  JOURNAL   J Comp Neurol 436 (2), 167-181 (2001)
   PUBMED   11438922
REFERENCE   7  (residues 1 to 2471)
  AUTHORS   Sriuranpong,V., Borges,M.W., Ravi,R.K., Arnold,D.R., Nelkin,B.D.,
            Baylin,S.B. and Ball,D.W.
  TITLE     Notch signaling induces cell cycle arrest in small cell lung cancer
            cells
  JOURNAL   Cancer Res 61 (7), 3200-3205 (2001)
   PUBMED   11306509
REFERENCE   8  (residues 1 to 2471)
  AUTHORS   Blaumueller,C.M., Qi,H., Zagouras,P. and Artavanis-Tsakonas,S.
  TITLE     Intracellular cleavage of Notch leads to a heterodimeric receptor
            on the plasma membrane
  JOURNAL   Cell 90 (2), 281-291 (1997)
   PUBMED   9244302
REFERENCE   9  (residues 1 to 2471)
  AUTHORS   Weinmaster,G., Roberts,V.J. and Lemke,G.
  TITLE     Notch2: a second mammalian Notch gene
  JOURNAL   Development 116 (4), 931-941 (1992)
   PUBMED   1295745
REFERENCE   10 (residues 1 to 2471)
  AUTHORS   Stifani,S., Blaumueller,C.M., Redhead,N.J., Hill,R.E. and
            Artavanis-Tsakonas,S.
  TITLE     Human homologs of a Drosophila Enhancer of split gene product
            define a novel family of nuclear proteins
  JOURNAL   Nat Genet 2 (2), 119-127 (1992)
   PUBMED   1303260
  REMARK    Erratum:[Nat Genet. 1992 Dec;2(4):343. doi: 10.1038/ng1292-343a.
            PMID: 1303292]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Mar 11, 2015 this sequence version replaced NP_077334.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.3326.1,
                                           SRR26643290.9332.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2471
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2471
                     /product="neurogenic locus notch homolog protein 2
                     precursor"
                     /note="neurogenic locus notch homolog protein 2; notch
                     gene homolog 2; notch 2"
                     /calculated_mol_wt=262498
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     mat_peptide     26..2471
                     /product="Neurogenic locus notch homolog protein 2.
                     /id=PRO_0000007689"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
                     /calculated_mol_wt=262498
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          109..143
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          182..218
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(182,185,200)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          260..296
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(260,263,277)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          298..335
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(298,301,317)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          415..454
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(415,418,435)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          456..492
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(456,459,473)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          495..530
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          532..567
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(532,535,549)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          570..604
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(570,573,586)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          608..643
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            613
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O35516; O-linked (Xyl...)
                     serine, alternate. /evidence=ECO:0000250|UniProtKB:O35516;
                     propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            614
                     /site_type="other"
                     /note="Essential for O-xylosylation.
                     /evidence=ECO:0000250|UniProtKB:O35516; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          645..679
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(645,648,661)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          682..717
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(682,685,699)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            733
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          757..793
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(757,760,774)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          795..831
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(795,798,812)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          873..909
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(873,876,890)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          911..947
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(911,914,928)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          949..985
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(949,952,966)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          987..1022
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(987,990,1004)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1025..1061
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1025,1028,1042)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1117..1147
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1151..1185
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1188..1223
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1225..1262
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1225,1228,1243)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1264..1302
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1264,1267,1283)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          <1312..1343
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1423..1456
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1425..1677
                     /region_name="Negative regulatory region (NRR).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1463..1497
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Site            1465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1501..1534
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1539..1594
                     /region_name="NOD"
                     /note="NOTCH protein; pfam06816"
                     /db_xref="CDD:462014"
     Region          1618..1673
                     /region_name="NODP"
                     /note="NOTCH protein; pfam07684"
                     /db_xref="CDD:462229"
     Region          1659..1740
                     /region_name="JMTM_Notch2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in neurogenic locus notch homolog protein 2 (Notch2) and
                     similar proteins; cd21703"
                     /db_xref="CDD:411986"
     Site            order(1661..1663,1666..1668,1682..1683,1685,1687..1703)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411986"
     mat_peptide     1666..2471
                     /product="Notch 2 extracellular truncation.
                     /evidence=ECO:0000250|UniProtKB:Q01705.
                     /id=PRO_0000007690"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
                     /calculated_mol_wt=86356
     Site            1678..1698
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     mat_peptide     1697..2471
                     /product="Notch 2 intracellular domain.
                     /evidence=ECO:0000250|UniProtKB:O35516.
                     /id=PRO_0000007691"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
                     /calculated_mol_wt=82993
     Site            1716
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1751..1788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35516; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1794..1813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1802
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1808
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1827..1874
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1827..1871
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1842
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35516; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            1845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          <1851..2066
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1876..1905
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1877..1907
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1909..1939
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            order(1943,1945,1949..1950,1953..1955,1957..1958,1962,
                     1965,1974,1976,1978,1982..1983,1986..1988,1990..1991,1995,
                     1998,2007,2009,2011,2015..2016,2019..2021,2023..2024,2028,
                     2031,2040)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1943..1974
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1943..1972
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          1976..2007
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1976..2005
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          2009..2040
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          2009..2038
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            2070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            2078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11577080; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            2081
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          2097..2116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     Site            2097
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04721; propagated from
                     UniProtKB/Swiss-Prot (Q9QW30.1)"
     Region          2105..>2422
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          2380..2471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QW30.1)"
     CDS             1..2471
                     /gene="Notch2"
                     /coded_by="NM_024358.2:163..7578"
                     /db_xref="GeneID:29492"
                     /db_xref="RGD:3188"
ORIGIN      
        1 mpalrpaalr allwlwlcga gpahalqcrg gqepcvnegt cvtyhngtgy crcpegflge
       61 ycqhrdpcek nrcqnggtcv tqamlgkatc rcapgftged cqystshpcf vsrpcqnggt
      121 chmlswdtye ctcqvgftgk qcqwtdvcls hpcengstcs svanqfscrc pagitgqkcd
      181 adinecdipg rcqhggtcln lpgsyrcqcp qgftgqhcds pyvpcapspc vnggtcrqtg
      241 dftsechclp gfegsncern iddcpnhkcq nggvcvdgvn tyncrcppqw tgqfctedvd
      301 ecllqpnacq nggtctnrng gygcvcvngw sgddcsenid dcafasctpg stcidrvasf
      361 sclcpegkag llchlddaci snpchkgalc dtnplngqyi ctcpqgykga dctedvdeca
      421 mansnpceha gkcvntdgaf hceclkgyag prcemdinec hsdpcqndat cldkiggftc
      481 lcmpgfkgvh celevnecqs npcvnngqcv dkvnrfqclc ppgftgpvcq ididdcsstp
      541 clngakcidh pngyecqcat gftgtlcden idncdpdpch hgqcqdgids ytcicnpgym
      601 gaicsdqide cysspclndg rcidlvngyq cncqpgtsgl nceinfddca snpclhgacv
      661 dginryscvc spgftgqrcn ididecasnp crkgatcind vngfrcmcpe gphhpscysq
      721 vneclsspci hgnctgglsg ykclcdagwv gincevdkne clsnpcqngg tcnnlvngyr
      781 ctckkgfkgy ncqvnideca snpclnqgtc lddvsgytch cmlpytgknc qtvlapcspn
      841 pcenaavcke apnfesftcl capgwqgqrc tvdvdecvsk pcmnngichn tqgsymcecp
      901 pgfsgmdcee dindclanpc qnggscvdkv ntfsclclpg fvgdkcqtdm neclsepckn
      961 ggtcsdyvns ytctcpagfh gvhcennide ctesscfngg tcvdginsfs clcpvgftgp
     1021 fclhdinecs snpclnsgtc vdglgtyrct cplgytgknc qtlvnlcsps pcknkgtcaq
     1081 ekarprclcp pgwdgaycdv lnvsckaaal qkgvpvehlc qhsgicinag nthhcqcplg
     1141 ytgsyceeql decasnpcqh gatcsdfigg yrcecvpgyq gvnceyevde cqnqpcqngg
     1201 tcidlvnhfk cscppgtrgl lceeniddca ggphclnggq cvdriggysc rclpgfager
     1261 cegdinecls npcssegsld ciqlknnyqc vcrsaftgrh cetfldvcpq kpclnggtca
     1321 vasnvpdgfi crcppgfsga rcqsscgqvk crrgeqcvht asgphcfcln rkdcesgcas
     1381 npcqhggtcy pqrqppyysc rcsppfwgsh cesytaptst ppatclsqyc adkardgicd
     1441 eacnshacqw dggdcsltme dpwanctssl rcweyinnqc delcntaecl fdnfecqrns
     1501 ktckydkyca dhfkdnhcdk gcnneecgwd gldcaadqpe nlaegilviv vllppeqllq
     1561 dsrsflralg tllhtnlrik qdsqgalmvy pyygeksaam kkqkvarrsl pdeqeqeiig
     1621 skvfleidnr qcvqdsdqcf kntdaaaall ashaiqgtls yplvsvvses edprntplly
     1681 llavavviil flillgvima krkrkhgflw lpegftlrrd ssnhkrrepv gqdavglknl
     1741 svqvseanli gsttsehwgd degpqpkkak aeddeallse ddpvdrrpwt qqhleaadir
     1801 rtpslaltpp qaeqevdvld vnvrgpdgct plmlaslrgg ssdlsdeded aedssaniit
     1861 dlvyqgaslq aqtdrtgema lhlaarysra daakrlldag adanaqdnmg rcplhaavaa
     1921 daqgvfqili rnrvtdldar mndgttplil aarlavegmv aelincqadv navddhgksa
     1981 lhwaaavnnv eatllllkng anrdmqdnke etplflaare gsyeaakill dhfanrditd
     2041 hmdrlprdva rdrmhhdivr lldeynvtps ppgtvltsal spvlcgpnrs flslkhtpmg
     2101 kkarrpntks tmptslpnla keakdvkgsr rkkclnekvq lsessvtlsp vdslesphty
     2161 vsdatsspmi tspgilqasp tpllaaapaa pvhaqhalsf snlhemqpla pgastvlpsv
     2221 sqllshhhiv ppgsgsagsl grlhsvpvps dwmnrvemse tqysemfgmv lapaegthpg
     2281 maapqsrape gkpiptqrep lppivtfqli pkgslaqaag apqtqsgcpp avagplpsmy
     2341 qipemarlps vafpptmmpq qegqvaqtiv ptyhpfpasv gkyptppsqh syassnaaer
     2401 tpnhgghlqg ehpyltpspe spdqwssssp hsasdwsdvt tsptpggggg gqrgpgthms
     2461 epphsnmqvy a
//
LOCUS       NP_072107                448 aa            linear   ROD 27-APR-2025
DEFINITION  antizyme inhibitor 1 [Rattus norvegicus].
ACCESSION   NP_072107
VERSION     NP_072107.2
DBSOURCE    REFSEQ: accession NM_022585.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Okugawa,Y., Toiyama,Y., Shigeyasu,K., Yamamoto,A., Shigemori,T.,
            Yin,C., Ichikawa,T., Yasuda,H., Fujikawa,H., Yoshiyama,S., Hiro,J.,
            Ohi,M., Araki,T., Kusunoki,M. and Goel,A.
  TITLE     Enhanced AZIN1 RNA editing and overexpression of its regulatory
            enzyme ADAR1 are important prognostic biomarkers in gastric cancer
  JOURNAL   J Transl Med 16 (1), 366 (2018)
   PUBMED   30563560
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Shigeyasu,K., Okugawa,Y., Toden,S., Miyoshi,J., Toiyama,Y.,
            Nagasaka,T., Takahashi,N., Kusunoki,M., Takayama,T., Yamada,Y.,
            Fujiwara,T., Chen,L. and Goel,A.
  TITLE     AZIN1 RNA editing confers cancer stemness and enhances oncogenic
            potential in colorectal cancer
  JOURNAL   JCI Insight 3 (12), 99976 (2018)
   PUBMED   29925690
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Fernandes,J.R.D., Jain,S. and Banerjee,A.
  TITLE     Expression of ODC1, SPD, SPM and AZIN1 in the hypothalamus, ovary
            and uterus during rat estrous cycle
  JOURNAL   Gen Comp Endocrinol 246, 9-22 (2017)
   PUBMED   28315656
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Zhu,D., Zhang,L., Cheng,L., Ren,L., Tang,J. and Sun,D.
  TITLE     Pancreatic Kininogenase Ameliorates Renal Fibrosis in
            Streptozotocin Induced-Diabetic Nephropathy Rat
  JOURNAL   Kidney Blood Press Res 41 (1), 9-17 (2016)
   PUBMED   26751697
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Greenwood,M.P., Greenwood,M., Paton,J.F. and Murphy,D.
  TITLE     Control of Polyamine Biosynthesis by Antizyme Inhibitor 1 Is
            Important for Transcriptional Regulation of Arginine Vasopressin in
            the Male Rat Hypothalamus
  JOURNAL   Endocrinology 156 (8), 2905-2917 (2015)
   PUBMED   25961839
  REMARK    GeneRIF: Identification of AZIN1, and hence by inference,
            polyamines as novel regulators of the expression of the Arginine
            vasopressin gene.
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Mangold,U., Hayakawa,H., Coughlin,M., Munger,K. and Zetter,B.R.
  TITLE     Antizyme, a mediator of ubiquitin-independent proteasomal
            degradation and its inhibitor localize to centrosomes and modulate
            centriole amplification
  JOURNAL   Oncogene 27 (5), 604-613 (2008)
   PUBMED   17667942
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Lopez-Contreras,A.J., Lopez-Garcia,C., Jimenez-Cervantes,C.,
            Cremades,A. and Penafiel,R.
  TITLE     Mouse ornithine decarboxylase-like gene encodes an antizyme
            inhibitor devoid of ornithine and arginine decarboxylating activity
  JOURNAL   J Biol Chem 281 (41), 30896-30906 (2006)
   PUBMED   16916800
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Kim,S.W., Mangold,U., Waghorne,C., Mobascher,A., Shantz,L.,
            Banyard,J. and Zetter,B.R.
  TITLE     Regulation of cell proliferation by the antizyme inhibitor:
            evidence for an antizyme-independent mechanism
  JOURNAL   J Cell Sci 119 (Pt 12), 2583-2591 (2006)
   PUBMED   16735445
  REMARK    GeneRIF: Wild-type antizyme inhibitor and the AZI(DeltaY) mutant
            are capable of direct interaction with cyclin D1 suggesting a
            potential mechanism for the antizyme-independent effects, and a
            novel function for antizyme inhibitor in cellular growth control.
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Murakami,Y., Ichiba,T., Matsufuji,S. and Hayashi,S.
  TITLE     Cloning of antizyme inhibitor, a highly homologous protein to
            ornithine decarboxylase
  JOURNAL   J Biol Chem 271 (7), 3340-3342 (1996)
   PUBMED   8631929
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Kitani,T. and Fujisawa,H.
  TITLE     Purification and characterization of antizyme inhibitor of
            ornithine decarboxylase from rat liver
  JOURNAL   Biochim Biophys Acta 991 (1), 44-49 (1989)
   PUBMED   2713421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            On Sep 5, 2014 this sequence version replaced NP_072107.1.
            
            Summary: The protein encoded by this gene belongs to the antizyme
            inhibitor family, which plays a role in cell growth and
            proliferation by maintaining polyamine homeostasis within the cell.
            Antizyme inhibitors are homologs of ornithine decarboxylase (ODC,
            the key enzyme in polyamine biosynthesis) that have lost the
            ability to decarboxylase ornithine; however, retain the ability to
            bind to antizymes. Antizymes negatively regulate intracellular
            polyamine levels by binding to ODC and targeting it for
            degradation, as well as by inhibiting polyamine uptake. Antizyme
            inhibitors function as positive regulators of polyamine levels by
            sequestering antizymes and neutralizing their effect. This gene
            encodes antizyme inhibitor 1, the first member of this gene family
            that is ubiquitously expressed, and is localized in the nucleus and
            cytoplasm. Overexpression of antizyme inhibitor 1 gene has been
            associated with increased proliferation, cellular transformation
            and tumorigenesis. Gene knockout studies showed that homozygous
            mutant mice lacking functional antizyme inhibitor 1 gene died at
            birth with abnormal liver morphology. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D89983.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..448
                     /product="antizyme inhibitor 1"
                     /note="ornithine decarboxylase antizyme inhibitor; AZI"
                     /calculated_mol_wt=49188
     Region          26..419
                     /region_name="PLPDE_III_ODC_like_AZI"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor;
                     cd06831"
                     /db_xref="CDD:143504"
     Site            69
                     /site_type="other"
                     /note="Not modified.
                     /evidence=ECO:0000250|UniProtKB:O35484; propagated from
                     UniProtKB/Swiss-Prot (Q63764.1)"
     Site            order(91..93,119,141,288,329,358,360,391,394,397)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143504"
     CDS             1..448
                     /gene="Azin1"
                     /gene_synonym="Oazi; Oazin"
                     /coded_by="NM_022585.2:783..2129"
                     /db_xref="GeneID:58961"
                     /db_xref="RGD:61934"
ORIGIN      
        1 mkgfiddany svglldegtn lgnvidnyvy ehtltgknaf fvgdlgkivk khsqwqnvva
       61 qikpfymvkc nstpavleil aalgtgfacs sknemalvqe lgvspeniiy tspckqasqi
      121 kyaakvgvni mtcdnevelk kiarnhpnak vllhiatedn iggedgnmkf gttlkncrhl
      181 lecakeldvq iigvkfhiss ackeyqvyvh alsdarcvfd magefgftmn mldigggftg
      241 teiqleevnh visplldiyf pegsgiqiis epgsyyvssa ftlavniiak kvvendklss
      301 gvekngsdep afvyymndgv ygsfasklse dlntvpevhk kykedeplft sslwgpscde
      361 ldqivescll pelsvgdwli fdnmgadslh gpsafsdtqr paiyfmmsls dwyemqdagi
      421 tsdammknff fapsciqlsq ednfstea
//
LOCUS       NP_001257599             253 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 4 [Rattus norvegicus].
ACCESSION   NP_001257599
VERSION     NP_001257599.1
DBSOURCE    REFSEQ: accession NM_001270670.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon and uses an alternate exon in place of another exon in the 3'
            end of the gene, compared to variant 1. The resulting isoform (4)
            has the same N- and C-termini but is shorter and has a different
            internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216694.1, FQ215374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..253
                     /product="troponin T, fast skeletal muscle isoform 4"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=29810
     Region          57..193
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..253
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270670.1:117..878"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eeaqeeevqe eapepeevqe eekprpklta pkipegekvd fddiqkkrqn
       61 kdlmelqali dshfearkke eeelialker iekrraerae qqriraeker erqnrlaeek
      121 arreeedakr raeddlkkkk alssmganys sylakadqkr gkkqtaremk kkilaerrkp
      181 lnidhlsddk lrdkakelwd tlyqletdkf efgeklkrqk ydimtvrarv emlakfskka
      241 gatakgkvgg rwk
//
LOCUS       NP_596887                570 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity testis-specific protein kinase 2 [Rattus
            norvegicus].
ACCESSION   NP_596887
VERSION     NP_596887.1
DBSOURCE    REFSEQ: accession NM_133396.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Toshima,J., Toshima,J.Y., Takeuchi,K., Mori,R. and Mizuno,K.
  TITLE     Cofilin phosphorylation and actin reorganization activities of
            testicular protein kinase 2 and its predominant expression in
            testicular Sertoli cells
  JOURNAL   J Biol Chem 276 (33), 31449-31458 (2001)
   PUBMED   11418599
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Rosok,O., Pedeutour,F., Ree,A.H. and Aasheim,H.C.
  TITLE     Identification and characterization of TESK2, a novel member of the
            LIMK/TESK family of protein kinases, predominantly expressed in
            testis
  JOURNAL   Genomics 61 (1), 44-54 (1999)
   PUBMED   10512679
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB049402.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB049402.1, BC128727.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132306
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..570
                     /product="dual specificity testis-specific protein kinase
                     2"
                     /EC_number="2.7.12.1"
                     /note="testicular protein kinase 2; testis-specific kinase
                     2"
                     /calculated_mol_wt=63428
     Region          64..316
                     /region_name="PKc_TESK"
                     /note="Catalytic domain of the Dual-specificity protein
                     kinase, Testicular protein kinase; cd14155"
                     /db_xref="CDD:271057"
     Site            order(64..68,72,85,87,114,130..133,137,139,176,178,
                     180..181,183,197,200,218..221)
                     /site_type="active"
                     /db_xref="CDD:271057"
     Site            order(64..68,72,85,87,114,130..133,137,176,178,180..181,
                     183,197)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271057"
     Site            order(68,137,139,176,178,180,200,218..221)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271057"
     Site            order(196..206,208..221)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271057"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q924U5.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96S53; propagated from
                     UniProtKB/Swiss-Prot (Q924U5.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96S53; propagated from
                     UniProtKB/Swiss-Prot (Q924U5.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCT9; propagated from
                     UniProtKB/Swiss-Prot (Q924U5.1)"
     Region          513..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924U5.1)"
     CDS             1..570
                     /gene="Tesk2"
                     /coded_by="NM_133396.2:354..2066"
                     /db_xref="GeneID:170908"
                     /db_xref="RGD:619984"
ORIGIN      
        1 mdrskrnsia gfpprverle efegggggdg ntvqvgrvss ssyraiisaf srltslddft
       61 rekigsgffs evfkvrhras gqvmalkmnt lssnranllk emqlmnrlsh pnilrfmgvc
      121 vhqgqlhalt eyinsgnleq lldsnlylpw tvrvklaydi avglsylhfk gifhrdltsk
      181 nclikrdeng ysavvadfgl aekipdasig seklavvgsp fwmapevlrd epynekadvf
      241 sygiilceii ariqadpdyl prtenfgldy dafqhmvgdc psdflqltfn ccnmdpklrp
      301 sfeeigktle eimsrlqeee lerdrklqpt akgllekvpg gkrlsslddk iphksprprr
      361 tiwlsrsqsd ifsrkpprtv nvldpyyqpr dgathtpkvn pfsarqdlkg gkvkffdlps
      421 ksvislvfdl dapgpgtvsl adcqeplaps srrwrslpgs peflhqacpf vgceeslsdg
      481 ppprlsslky rvreippfrt salsatsahe amdcsnpqee ngfvprpkgt spcsgaasee
      541 meveeerprr apvhfsisgi slqtqgeqdg
//
LOCUS       NP_741992               1140 aa            linear   ROD 27-APR-2025
DEFINITION  DNA damage-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_741992 XP_342025
VERSION     NP_741992.2
DBSOURCE    REFSEQ: accession NM_171995.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Liu,Y., Qu,H.Q., Chang,X., Qu,J., Mentch,F.D., Nguyen,K., Tian,L.,
            Glessner,J., Sleiman,P.M.A. and Hakonarson,H.
  TITLE     Mutation burden analysis of six common mental disorders in African
            Americans by whole genome sequencing
  JOURNAL   Hum Mol Genet 31 (22), 3769-3776 (2022)
   PUBMED   35642741
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Faust,T.B., Yoon,H., Nowak,R.P., Donovan,K.A., Li,Z., Cai,Q.,
            Eleuteri,N.A., Zhang,T., Gray,N.S. and Fischer,E.S.
  TITLE     Structural complementarity facilitates E7820-mediated degradation
            of RBM39 by DCAF15
  JOURNAL   Nat Chem Biol 16 (1), 7-14 (2020)
   PUBMED   31686031
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Mo,Y., Lin,R., Liu,P., Tan,M., Xiong,Y., Guan,K.L. and Yuan,H.X.
  TITLE     SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3
            ligase complexes
  JOURNAL   FEBS J 284 (21), 3619-3636 (2017)
   PUBMED   28886238
REFERENCE   4  (residues 1 to 1140)
  AUTHORS   Tong,X., Zhang,D., Charney,N., Jin,E., VanDommelen,K., Stamper,K.,
            Gupta,N., Saldate,J. and Yin,L.
  TITLE     DDB1-Mediated CRY1 Degradation Promotes FOXO1-Driven
            Gluconeogenesis in Liver
  JOURNAL   Diabetes 66 (10), 2571-2582 (2017)
   PUBMED   28790135
  REMARK    Erratum:[Diabetes. 2017 Dec;66(12):3144. doi: 10.2337/db17-er12e.
            PMID: 28993340]
REFERENCE   5  (residues 1 to 1140)
  AUTHORS   Uehara,T., Minoshima,Y., Sagane,K., Sugi,N.H., Mitsuhashi,K.O.,
            Yamamoto,N., Kamiyama,H., Takahashi,K., Kotake,Y., Uesugi,M.,
            Yokoi,A., Inoue,A., Yoshida,T., Mabuchi,M., Tanaka,A. and Owa,T.
  TITLE     Selective degradation of splicing factor CAPERalpha by anticancer
            sulfonamides
  JOURNAL   Nat Chem Biol 13 (6), 675-680 (2017)
   PUBMED   28437394
REFERENCE   6  (residues 1 to 1140)
  AUTHORS   Wertz,I.E., O'Rourke,K.M., Zhang,Z., Dornan,D., Arnott,D.,
            Deshaies,R.J. and Dixit,V.M.
  TITLE     Human De-etiolated-1 regulates c-Jun by assembling a CUL4A
            ubiquitin ligase
  JOURNAL   Science 303 (5662), 1371-1374 (2004)
   PUBMED   14739464
REFERENCE   7  (residues 1 to 1140)
  AUTHORS   Groisman,R., Polanowska,J., Kuraoka,I., Sawada,J., Saijo,M.,
            Drapkin,R., Kisselev,A.F., Tanaka,K. and Nakatani,Y.
  TITLE     The ubiquitin ligase activity in the DDB2 and CSA complexes is
            differentially regulated by the COP9 signalosome in response to DNA
            damage
  JOURNAL   Cell 113 (3), 357-367 (2003)
   PUBMED   12732143
REFERENCE   8  (residues 1 to 1140)
  AUTHORS   Sun,N.K., Lu,H.P. and Chao,C.C.
  TITLE     Identification of rat DDB1, a putative DNA repair protein, and
            functional correlation with its damaged-DNA recognition activity
  JOURNAL   J Biomed Sci 9 (4), 371-380 (2002)
   PUBMED   12145536
  REMARK    GeneRIF: role in UV-damaged-DNA recognition activity in mammalian
            tissues and cell lines
REFERENCE   9  (residues 1 to 1140)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
REFERENCE   10 (residues 1 to 1140)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1, FM035228.1, FN804617.1, CB777486.1, CV111529.1,
            FN805433.1, FM065862.1, FM131388.1, FM101956.1 and CV108212.1.
            
            On Nov 10, 2012 this sequence version replaced NP_741992.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2437783.1,
                                           SRR26360194.1155074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1140
                     /product="DNA damage-binding protein 1"
                     /note="damage-specific DNA binding protein 1, 127kDa"
                     /calculated_mol_wt=126810
     Region          2..768
                     /region_name="Interaction with CDT1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q16531; propagated from
                     UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Region          13..356
                     /region_name="WD repeat beta-propeller A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Region          75..543
                     /region_name="MMS1_N"
                     /note="Mono-functional DNA-alkylating methyl
                     methanesulfonate N-term; pfam10433"
                     /db_xref="CDD:463091"
     Region          391..708
                     /region_name="WD repeat beta-propeller B, Interaction with
                     CUL4A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Region          709..1043
                     /region_name="WD repeat beta-propeller C.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Region          771..1140
                     /region_name="Interaction with CDT1 and CUL4A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Region          789..1099
                     /region_name="CPSF_A"
                     /note="CPSF A subunit region; pfam03178"
                     /db_xref="CDD:427182"
     Site            1067
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q16531; propagated from
                     UniProtKB/Swiss-Prot (Q9ESW0.1)"
     Site            1125
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESW0.1)"
     CDS             1..1140
                     /gene="Ddb1"
                     /coded_by="NM_171995.2:170..3592"
                     /db_xref="GeneID:64470"
                     /db_xref="RGD:621889"
ORIGIN      
        1 msynyvvtaq kptavngcvt ghftsaedln lliakntrle iyvvtaeglr pvkevgmygk
       61 iavmelfrpk geskdllfil takynacile ykqsgesidi itrahgnvqd rigrpsetgi
      121 igiidpecrm iglrlydglf kvipldrdnk elkafnirle elhvidvkfl ygcqapticf
      181 vyqdpqgrhv ktyevslrek efnkgpwkqe nveaeasmvi avpepfggai iigqesityh
      241 ngdkylaiap piikqstivc hnrvdpngsr yllgdmegrl fmlllekeeq mdgtvtlkdl
      301 rvellgetsi aecltyldng vvfvgsrlgd sqlvklnvds neqgsyvvam etftnlgpiv
      361 dmcvvdlerq gqgqlvtcsg afkegslrii rngigiheha sidlpgikgl wplrsdpsre
      421 tddtlvlsfv gqtrvlmlng eeveetelmg fvddqqtffc gnvahqqliq itsasvrlvs
      481 qepkalvsew kepqgknisv ascnssqvvv avgralyylq ihpqelrqis htemehevac
      541 lditplgesn glsplcaigl wtdisarilk lpsfellhke mlggeiiprs ilmttfessh
      601 yllcalgdga lfyfglniet gllsdrkkvt lgtqptvlrt frslsttnvf acsdrptviy
      661 ssnhklvfsn vnlkevnymc plnsdgypds lalannstlt igtideiqkl hirtvplyes
      721 prkicyqevs qcfgvlssri evqdtsggtt alrpsastqa lsssvssskl fssstaphet
      781 sfgeevevhn lliidqhtfe vlhahqflqn eyalslvsck lgkdpntyfi vgtamvypee
      841 aepkqgrivv fqysdgklqt vaekevkgav ysmvefngkl lasinstvrl yewttekelr
      901 tecnhynnim alylktkgdf ilvgdlmrsv lllaykpmeg nfeeiardfn pnwmsaveil
      961 dddnflgaen afnlfvcqkd saattdeerq hlqevglfhl gefvnvfchg slvmqnlget
     1021 stptqgsvlf gtvngmiglv tslseswynl lldmqnrlnk viksvgkieh sfwrsfhter
     1081 ktepatgfid gdliesfldi srpkmqevva nlqyddgsgm kreataddli kvveeltrih
//
LOCUS       NP_001009691             767 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase DCLK2 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001009691 XP_227490
VERSION     NP_001009691.3
DBSOURCE    REFSEQ: accession NM_001009691.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Dijkmans,T.F., van Hooijdonk,L.W., Fitzsimons,C.P. and
            Vreugdenhil,E.
  TITLE     The doublecortin gene family and disorders of neuronal structure
  JOURNAL   Cent Nerv Syst Agents Med Chem 10 (1), 32-46 (2010)
   PUBMED   20236041
  REMARK    Review article
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Kerjan,G., Koizumi,H., Han,E.B., Dube,C.M., Djakovic,S.N.,
            Patrick,G.N., Baram,T.Z., Heinemann,S.F. and Gleeson,J.G.
  TITLE     Mice lacking doublecortin and doublecortin-like kinase 2 display
            altered hippocampal neuronal maturation and spontaneous seizures
  JOURNAL   Proc Natl Acad Sci U S A 106 (16), 6766-6771 (2009)
   PUBMED   19342486
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Tuy,F.P., Saillour,Y., Kappeler,C., Chelly,J. and Francis,F.
  TITLE     Alternative transcripts of Dclk1 and Dclk2 and their expression in
            doublecortin knockout mice
  JOURNAL   Dev Neurosci 30 (1-3), 171-186 (2008)
   PUBMED   18075264
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Ohmae,S., Takemoto-Kimura,S., Okamura,M., Adachi-Morishima,A.,
            Nonaka,M., Fuse,T., Kida,S., Tanji,M., Furuyashiki,T., Arakawa,Y.,
            Narumiya,S., Okuno,H. and Bito,H.
  TITLE     Molecular identification and characterization of a family of
            kinases with homology to Ca2+/calmodulin-dependent protein kinases
            I/IV
  JOURNAL   J Biol Chem 281 (29), 20427-20439 (2006)
   PUBMED   16684769
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Edelman,A.M., Kim,W.Y., Higgins,D., Goldstein,E.G., Oberdoerster,M.
            and Sigurdson,W.
  TITLE     Doublecortin kinase-2, a novel doublecortin-related protein kinase
            associated with terminal segments of axons and dendrites
  JOURNAL   J Biol Chem 280 (9), 8531-8543 (2005)
   PUBMED   15611072
  REMARK    GeneRIF: Doublecortin kinase-2 is associated with terminal segments
            of axons and dendrites
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            On Oct 1, 2010 this sequence version replaced NP_001009691.2.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. The protein encoded by
            this gene contains two N-terminal doublecortin domains, which bind
            microtubules and regulate microtubule polymerization, a C-terminal
            serine/threonine protein kinase domain, which shows substantial
            homology to Ca2+/calmoduline-dependent protein kinase, and a
            serine/proline-rich domain in between the doublecortin and the
            protein kinase domains, which mediates multiple protein-protein
            interactions. The microtubule-polymerizing activity of the encoded
            protein is independent of its protein kinase activity. Mouse
            studies show that this gene and the DCX gene, another family
            member, share function in the establishment of hippocampal
            organization and that their absence results in a severe epileptic
            phenotype and lethality, as described in human patients with
            lissencephaly. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (2) is an exon-5-containing
            transcript (PMIDs:15611072 and 18075264). It encodes the longer
            isoform (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY673998.1, AY674000.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..767
                     /product="serine/threonine-protein kinase DCLK2 isoform b"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase DCLK2; caMK-like
                     CREB regulatory kinase 2; doublecortin-like and CAM
                     kinase-like 2; doublecortin kinase 2"
                     /calculated_mol_wt=83885
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N568; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Region          70..154
                     /region_name="DCX1_DCLK2"
                     /note="Dublecortin-like domain 1 found in
                     doublecortin-like kinase 2 (DCLK2); cd17141"
                     /db_xref="CDD:340661"
     Site            order(70,81..83,89,94..95,97,105,113..115,117..118,121,
                     148)
                     /site_type="other"
                     /note="putative tubulin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340661"
     Site            order(85,130)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340661"
     Region          192..275
                     /region_name="DCX2"
                     /note="Dublecortin-like domain 2; cd17069"
                     /db_xref="CDD:340589"
     Site            order(194,205..207,213,218..219,221,229,238..239,242,269)
                     /site_type="other"
                     /note="putative DCX-stabilized microtubules [polypeptide
                     binding]"
                     /db_xref="CDD:340589"
     Site            order(209,250)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340589"
     Region          301..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N568; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Region          407..665
                     /region_name="STKc_DCKL2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Doublecortin-like kinase 2 (also called Doublecortin-like
                     and CAM kinase-like 2); cd14184"
                     /db_xref="CDD:271086"
     Site            order(415..419,423,436,438,468,484..487,491,493,529..530,
                     532,534..535,537,551..552,555,567..571,573)
                     /site_type="active"
                     /db_xref="CDD:271086"
     Site            order(415..418,423,436,438,468,484..487,491,534..535,537,
                     551..552)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271086"
     Site            order(419,491,493,529..530,532,534,555,567..571,573)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271086"
     Site            551..571
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271086"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5MPA9.2)"
     Region          721..767
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MPA9.2)"
     CDS             1..767
                     /gene="Dclk2"
                     /gene_synonym="CL2; CLICK-II; CLICK2; Dck2; RGD1308384"
                     /coded_by="NM_001009691.3:609..2912"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:310698"
                     /db_xref="RGD:1308384"
ORIGIN      
        1 mastrsiele hfeerdkrpr pgsrrgapss sggssisgpk gnglipspah sahcsfyrtr
       61 tlqalssekk akkarfyrng dryfkglvfa issdrfrsfd allieltrsl sdnvnlpqgv
      121 rtiytvdgsr kvtsldelle gesyvcasne pfrkvdytkn vnpnwsvnik ggttrtlava
      181 saksevkesk dfikpklvtv irsgvkprka vrillnkkta hsfeqvltdi teaikldsgv
      241 vkrlctldgk qvtclqdffg dddvfiacgp ekyryaqddf vldhsecrvl kssysrasaa
      301 kysgsrspgl srrskspasv kraghssays takspvngtp ssqlstpkst ksssssptsp
      361 gsfrglkqis aqgrsssnvn ggpeldrcms pegvngnrcs esftllekyr igkvigdgnf
      421 avvkecmdrs tgkefalkii dkakccgkeh lienevsilr rvkhpniiml veemetttel
      481 flvmelvkgg dlfdaitsst kyterdgsam vynlasalry lhglsivhrd ikpenllvce
      541 ypdgtkslkl gdfglatvve gplytvcgtp tyvapeiiae tgyglkvdvw aagvityill
      601 cgfppfrsen nlqedlfdqi lagklefpap ywdnitdsak elisqmlqvn vearctagei
      661 lshpwvsdda sqennmqaev tgklkqhfnn alpkqnsttt gvsvimntal dkegqvfcsk
      721 hcrdsskssr eqtsareapp ppesprppgp patsgcdpag twrrhrd
//
LOCUS       NP_001257594             259 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 1 [Rattus norvegicus].
ACCESSION   NP_001257594
VERSION     NP_001257594.1
DBSOURCE    REFSEQ: accession NM_001270665.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (1) and variant 2 represent the
            longest transcripts and encode the longest isoforms (1 and 2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224813.1, FQ215723.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..259
                     /product="troponin T, fast skeletal muscle isoform 1"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30619
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P02641; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          63..199
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          101..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P09739.2)"
     Region          235..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09739.2)"
     CDS             1..259
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270665.1:117..896"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeape peevqeeekp rpkltapkip egekvdfddi
       61 qkkrqnkdlm elqalidshf earkkeeeel ialkeriekr raeraeqqri raekererqn
      121 rlaeekarre eedakrraed dlkkkkalss mganyssyla kadqkrgkkq taremkkkil
      181 aerrkplnid hlsddklrdk akelwdtlyq letdkfefge klkrqkydit tlrsridqaq
      241 khskkagata kgkvggrwk
//
LOCUS       NP_001157575             705 aa            linear   ROD 27-APR-2025
DEFINITION  gamma-adducin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001157575
VERSION     NP_001157575.1
DBSOURCE    REFSEQ: accession NM_001164103.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Fan,L., Gao,W., Liu,Y., Jefferson,J.R., Fan,F. and Roman,R.J.
  TITLE     Knockout of gamma-Adducin Promotes
            NG-Nitro-L-Arginine-Methyl-Ester-Induced Hypertensive Renal Injury
  JOURNAL   J Pharmacol Exp Ther 377 (1), 189-198 (2021)
   PUBMED   33414130
  REMARK    GeneRIF: Knockout of gamma-Adducin Promotes
            N(G)-Nitro-L-Arginine-Methyl-Ester-Induced Hypertensive Renal
            Injury.
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Gao,W., Liu,Y., Fan,L., Zheng,B., Jefferson,J.R., Wang,S.,
            Zhang,H., Fang,X., Nguyen,B.V., Zhu,T., Roman,R.J. and Fan,F.
  TITLE     Role of gamma-adducin in actin cytoskeleton rearrangements in
            podocyte pathophysiology
  JOURNAL   Am J Physiol Renal Physiol 320 (1), F97-F113 (2021)
   PUBMED   33308016
  REMARK    GeneRIF: Role of gamma-adducin in actin cytoskeleton rearrangements
            in podocyte pathophysiology.
            GeneRIF: Reduced ADD3 function in FHH rats alters baseline podocyte
            pathophysiology by rearrangement of the actin cytoskeleton at the
            onset of proteinuria in young animals.
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Fan,F., Geurts,A.M., Pabbidi,M.R., Ge,Y., Zhang,C., Wang,S.,
            Liu,Y., Gao,W., Guo,Y., Li,L., He,X., Lv,W., Muroya,Y., Hirata,T.,
            Prokop,J., Booz,G.W., Jacob,H.J. and Roman,R.J.
  TITLE     A Mutation in gamma-Adducin Impairs Autoregulation of Renal Blood
            Flow and Promotes the Development of Kidney Disease
  JOURNAL   J Am Soc Nephrol 31 (4), 687-700 (2020)
   PUBMED   32029431
  REMARK    GeneRIF: A Mutation in gamma-Adducin Impairs Autoregulation of
            Renal Blood Flow and Promotes the Development of Kidney Disease.
            GeneRIF: A mutation in ADD3 that alters ACTIN binding causes renal
            vascular dysfunction and promotes the susceptibility to kidney
            disease.
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Fan,F., Pabbidi,M.R., Ge,Y., Li,L., Wang,S., Mims,P.N. and
            Roman,R.J.
  TITLE     Knockdown of Add3 impairs the myogenic response of renal afferent
            arterioles and middle cerebral arteries
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F971-F981 (2017)
   PUBMED   27927653
  REMARK    GeneRIF: Add3 may play a causal role in the impaired myogenic
            response and autoregulation in the renal and cerebral circulation
            in hypertensive rats.
            GeneRIF: Mutation of Add3 may play a causal role in the impaired
            myogenic response and blood flow autoregulation in the renal and
            cerebral circulation.
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Tripodi,G., Szpirer,C., Reina,C., Szpirer,J. and Bianchi,G.
  TITLE     Polymorphism of gamma-adducin gene in genetic hypertension and
            mapping of the gene to rat chromosome 1q55
  JOURNAL   Biochem Biophys Res Commun 237 (3), 685-689 (1997)
   PUBMED   9299427
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Chapline,C., Ramsay,K., Klauck,T. and Jaken,S.
  TITLE     Interaction cloning of protein kinase C substrates
  JOURNAL   J Biol Chem 268 (10), 6858-6861 (1993)
   PUBMED   8463212
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Lebowitz,M.S. and Pedersen,P.L.
  TITLE     Regulation of the mitochondrial ATP synthase/ATPase complex: cDNA
            cloning, sequence, overexpression, and secondary structural
            characterization of a functional protein inhibitor
  JOURNAL   Arch Biochem Biophys 301 (1), 64-70 (1993)
   PUBMED   8442667
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Pinto-Correia,C., Goldstein,E.G., Bennett,V. and Sobel,J.S.
  TITLE     Immunofluorescence localization of an adducin-like protein in the
            chromosomes of mouse oocytes
  JOURNAL   Dev Biol 146 (2), 301-311 (1991)
   PUBMED   1864459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB757924.1, U35775.1, FM038946.1, FM072500.1, AW141606.1,
            CB725075.1, CK596161.1, FM059497.1, CF111029.1 and AA899625.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..705
                     /product="gamma-adducin isoform 1"
                     /note="potein kinase C binding protein 35H; adducin-like
                     protein 70; protein kinase C-binding protein 35H;
                     gamma-adducin; adducin 3 (gamma)"
                     /calculated_mol_wt=78687
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB5; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Region          137..385
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(143,147,155,180,182..183,233,235..236,241..243,251,
                     253..254,265,293,304,311,315,322,340)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(160,177..178,203..205,231,233,294)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(231,233,294)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Site            357
                     /site_type="cleavage"
                     /note="Cleavage by asparagine endopeptidase (AEP).
                     /evidence=ECO:0000250|UniProtKB:Q9QYB5; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB5; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Region          472..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     Region          535..556
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     Region          572..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB5; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Region          658..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB5; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q9UEY8; propagated from
                     UniProtKB/Swiss-Prot (Q62847.3)"
     Region          683..700
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62847.3)"
     CDS             1..705
                     /gene="Add3"
                     /coded_by="NM_001164103.1:217..2334"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25230"
                     /db_xref="RGD:2043"
ORIGIN      
        1 mssdtsqavi ttppppsmph keryfdrine sdpeylrern mspdlrqdfn mmeqrkrvtq
       61 ilqspafred lecliqeqmk kghdptglla lqqiadyima nsftgfsspp lslgmvtpin
      121 dlpgadtssy vkgekltrck laslyrladl fgwahlanty isvrvskeqd hiiiiprgls
      181 fseatasalv kvniigevvd qgstnlkidh sgfsphaaiy strpdvkcvi hihtlataav
      241 ssmkcgilpi sqeslilgdv ayydyqgsld eeeerielqk vlgpsckvlv lrnhgvvalg
      301 etleeafhyi fnvqmaceiq vqavagaggv dnllildlqk ykafthgvam tggggvnmgs
      361 hqkwkvgeie feglmrtldn lgyrtgyayr hplvrekprh ksdveipatv tafsfeddsv
      421 plsplkymaq rqqrektrwl nspntymkvn vpeesrnget sprtkitwmk aedpskvssg
      481 tpikiedpnq fvplntnpte vlekrnkire qnrydlktag pqsqllagiv vdkppstmrf
      541 edddqgppap pnpfshlmeg eleeytktie rkqqglddae qeslsddaas vsqiqsqtqs
      601 pqsvperlee nhelfsksft svdvpvivng kdemhdvede laqrvsrltt sttienieit
      661 ikspdrteev lspdgspsks pskkkkkfrt psflkknkkk ekvea
//
LOCUS       NP_001178892            1262 aa            linear   ROD 27-APR-2025
DEFINITION  synaptopodin-2 [Rattus norvegicus].
ACCESSION   NP_001178892 XP_575030
VERSION     NP_001178892.1
DBSOURCE    REFSEQ: accession NM_001191963.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1262)
  AUTHORS   Kai,F. and Duncan,R.
  TITLE     Prostate cancer cell migration induced by myopodin isoforms is
            associated with formation of morphologically and biochemically
            distinct actin networks
  JOURNAL   FASEB J 27 (12), 5046-5058 (2013)
   PUBMED   24005909
REFERENCE   2  (residues 1 to 1262)
  AUTHORS   Ulbricht,A., Eppler,F.J., Tapia,V.E., van der Ven,P.F., Hampe,N.,
            Hersch,N., Vakeel,P., Stadel,D., Haas,A., Saftig,P., Behrends,C.,
            Furst,D.O., Volkmer,R., Hoffmann,B., Kolanus,W. and Hohfeld,J.
  TITLE     Cellular mechanotransduction relies on tension-induced and
            chaperone-assisted autophagy
  JOURNAL   Curr Biol 23 (5), 430-435 (2013)
   PUBMED   23434281
REFERENCE   3  (residues 1 to 1262)
  AUTHORS   Kai,F., Tanner,K., King,C. and Duncan,R.
  TITLE     Myopodin isoforms alter the chemokinetic response of PC3 cells in
            response to different migration stimuli via differential effects on
            Rho-ROCK signaling pathways
  JOURNAL   Carcinogenesis 33 (11), 2100-2107 (2012)
   PUBMED   22915763
REFERENCE   4  (residues 1 to 1262)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 1262)
  AUTHORS   Linnemann,A., van der Ven,P.F., Vakeel,P., Albinus,B., Simonis,D.,
            Bendas,G., Schenk,J.A., Micheel,B., Kley,R.A. and Furst,D.O.
  TITLE     The sarcomeric Z-disc component myopodin is a multiadapter protein
            that interacts with filamin and alpha-actinin
  JOURNAL   Eur J Cell Biol 89 (9), 681-692 (2010)
   PUBMED   20554076
REFERENCE   6  (residues 1 to 1262)
  AUTHORS   Faul,C., Dhume,A., Schecter,A.D. and Mundel,P.
  TITLE     Protein kinase A, Ca2+/calmodulin-dependent kinase II, and
            calcineurin regulate the intracellular trafficking of myopodin
            between the Z-disc and the nucleus of cardiac myocytes
  JOURNAL   Mol Cell Biol 27 (23), 8215-8227 (2007)
   PUBMED   17923693
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_575030.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.10032.1,
                                           SRR26643297.9434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..1262
                     /product="synaptopodin-2"
                     /note="myopodin"
                     /calculated_mol_wt=135895
     Region          1..174
                     /region_name="Interaction with VPS18.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          8..85
                     /region_name="PDZ_SYNPO2-like"
                     /note="PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin
                     2-like protein (SYNPO2L), and related domains; cd10820"
                     /db_xref="CDD:467264"
     Site            order(16..22,34,37,66,70,73..74)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467264"
     Region          89..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          239..276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          323..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          392..400
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          477..658
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          503..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          530..658
                     /region_name="F-actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          554..560
                     /region_name="Interaction with YWHAB.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          592..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          602..809
                     /region_name="Interaction with YWHAB.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA and CaMK2.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          610..621
                     /region_name="Interaction with BAG3.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          614..617
                     /region_name="PPPY motif.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          <651..1101
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          659..922
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          659..914
                     /region_name="F-actin bundling activity.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          659..801
                     /region_name="F-actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          741..799
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          745..898
                     /region_name="Actin binding.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YE8; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          808..1153
                     /region_name="Interaction with FLNC.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          833..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          899..1153
                     /region_name="Interaction with ACTN2.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Region          933..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Region          999..1018
                     /region_name="Interaction with ZYX.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1055
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UMS6; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A702.2)"
     CDS             1..1262
                     /gene="Synpo2"
                     /gene_synonym="RGD1564779"
                     /coded_by="NM_001191963.1:120..3908"
                     /db_xref="GeneID:499702"
                     /db_xref="RGD:1564779"
ORIGIN      
        1 mgtgdficis mtggapwgfr lqggkeekqp lqvakirsqs kasdsglcvg devvsingnp
       61 cadltypevi klmesitdsl hllikrptsg tsealdsete ntnhqhlphg gpmesttlqi
      121 qhaaktqgkd fllasvqtsa prtedqgnaw gyaecttedq vsqmpgsqeg hlveevilrk
      181 kpeagqpghv velqlslske rqrctsdpiv tllgnekfks pdpdwgtqhg rtvhinsipa
      241 pekadtslts gttvqtssgr eltviqgrdp ggtglpqvev ildcsdrlka eecrlqagrg
      301 cvaspveggr seappslvsf avssegteqg edqrsgkdqg rphkhrarha rlrrseslse
      361 kqvkeakskc ksiallltda pnpnskgvlm fkkrrrrark ytlvsygtge lereeeeedq
      421 eagdkdeisd laflgtsese vdeellsdvd dntqvvnfdw dsglvdiekr lnrgdkmeml
      481 pdttgkgalm fakrrermeq ftaqneeekt gglagggsda lqtdglrtmt syqrkeesvr
      541 mqssvsessf qmgrslgsvp qqngfsgvse tagpqrmipm nrtakpflgs vnqtaapfsp
      601 tqsvtspipd fpapppysav spppeafsrg isspvagpaq pppwpqpapw sqpafydsse
      661 qiasrderia vpakrtgilq eakrrgttkp mftfketkvs pnpellsllq naegkrgtga
      721 ggdsgpeedy lslgaeacnf mqssakqktp ppvapkpavk tssssqpvap vspvwspgva
      781 paqgpafstt nppnppqvta vssikiaqpt cpparpasal nlagpfkgpq aavvshnytp
      841 kpsaptplvn aapagaggps nelpgmsgkg aqlfakrqsr mekyvvdsdt vqahtvraqs
      901 ptpslpaswk yssnvrappp vaynpihsps yplaaiksqp pgaqasktsk kkgkkplntl
      961 dvmkhqpyql naslftfqpp dskdglpqks tvkvssvapa mkqalpprqa digsptnaka
     1021 ssvysvpayt sqpnffaeat spvsaspvpv svptspkqet tstsyfvapr pkfsakksgv
     1081 tvqenwrsls lpgraappim sappwlcqpa ysysskptle qekankrptp weaaaksplg
     1141 lvdeafrprn ieesivanvv saarrkvfag sqedwkerls fvpqtqktsm sfserreynv
     1201 pspvnshvss hslyssqlpy vcyrkesrnd lkamsmdtrs eyclplggyd ynphprgwrh
     1261 qp
//
LOCUS       NP_001166943              72 aa            linear   ROD 27-APR-2025
DEFINITION  UPF0729 protein C18orf32 homolog [Rattus norvegicus].
ACCESSION   NP_001166943
VERSION     NP_001166943.1
DBSOURCE    REFSEQ: accession NM_001173472.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Bersuker,K., Peterson,C.W.H., To,M., Sahl,S.J., Savikhin,V.,
            Grossman,E.A., Nomura,D.K. and Olzmann,J.A.
  TITLE     A Proximity Labeling Strategy Provides Insights into the
            Composition and Dynamics of Lipid Droplet Proteomes
  JOURNAL   Dev Cell 44 (1), 97-112 (2018)
   PUBMED   29275994
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB568734.1 and BC162045.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC162045.1, FQ217314.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..72
                     /product="UPF0729 protein C18orf32 homolog"
                     /calculated_mol_wt=8038
     Region          1..33
                     /region_name="Necessary for its localzation to the
                     endoplasmic reticulum and lipid droplets.
                     /evidence=ECO:0000250|UniProtKB:Q8TCD1"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC88.1)"
     Region          2..>38
                     /region_name="DUF4512"
                     /note="Domain of unknown function (DUF4512); pfam14975"
                     /db_xref="CDD:405640"
     Region          45..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC88.1)"
     CDS             1..72
                     /gene="C18h18orf32"
                     /gene_synonym="RGD1562987"
                     /coded_by="NM_001173472.1:140..358"
                     /db_xref="GeneID:498886"
                     /db_xref="RGD:1562987"
ORIGIN      
        1 mvcipcivip vllwifkkfl epyiypvvsr iwprkavqql dnkntgkvdc kgadtngfst
       61 kgptevsdkk kd
//
LOCUS       NP_001257797             271 aa            linear   ROD 27-APR-2025
DEFINITION  neurotrophin-3 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001257797
VERSION     NP_001257797.1
DBSOURCE    REFSEQ: accession NM_001270868.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Briones-Vidal,M.G., Reyes-Garcia,S.E. and Escobar,M.L.
  TITLE     Neurotrophin-3 into the insular cortex strengthens conditioned
            taste aversion memory
  JOURNAL   Behav Brain Res 461, 114857 (2024)
   PUBMED   38211776
  REMARK    GeneRIF: Neurotrophin-3 into the insular cortex strengthens
            conditioned taste aversion memory.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zou,D., Wang,H., Hao,S. and Chen,F.
  TITLE     Repair effect of neurotrophic factor III (NT-3) on rats with spinal
            injury model and its mechanism
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (1), 56-61 (2024)
   PUBMED   38372112
  REMARK    GeneRIF: Repair effect of neurotrophic factor III (NT-3) on rats
            with spinal injury model and its mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Yang,Y., Xu,H.Y., Deng,Q.W., Wu,G.H., Zeng,X., Jin,H., Wang,L.J.,
            Lai,B.Q., Li,G., Ma,Y.H., Jiang,B., Ruan,J.W., Wang,Y.Q., Ding,Y.
            and Zeng,Y.S.
  TITLE     Electroacupuncture facilitates the integration of a grafted
            TrkC-modified mesenchymal stem cell-derived neural network into
            transected spinal cord in rats via increasing neurotrophin-3
  JOURNAL   CNS Neurosci Ther 27 (7), 776-791 (2021)
   PUBMED   33763978
  REMARK    GeneRIF: Electroacupuncture facilitates the integration of a
            grafted TrkC-modified mesenchymal stem cell-derived neural network
            into transected spinal cord in rats via increasing neurotrophin-3.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Xu,H., Yang,Y., Deng,Q.W., Zhang,B.B., Ruan,J.W., Jin,H.,
            Wang,J.H., Ren,J., Jiang,B., Sun,J.H., Zeng,Y.S. and Ding,Y.
  TITLE     Governor Vessel Electro-Acupuncture Promotes the Intrinsic Growth
            Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury
  JOURNAL   J Neurotrauma 38 (6), 734-745 (2021)
   PUBMED   33121345
  REMARK    GeneRIF: Governor Vessel Electro-Acupuncture Promotes the Intrinsic
            Growth Ability of Spinal Neurons through Activating Calcitonin
            Gene-Related Peptide/alpha-Calcium/Calmodulin-Dependent Protein
            Kinase/Neurotrophin-3 Pathway after Spinal Cord Injury.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Donsante,A., Xue,J., Poth,K.M., Hardcastle,N.S., Diniz,B.,
            O'Connor,D.M., Xia,Y. and Boulis,N.M.
  TITLE     Controlling the Release of Neurotrophin-3 and Chondroitinase ABC
            Enhances the Efficacy of Nerve Guidance Conduits
  JOURNAL   Adv Healthc Mater 9 (14), e2000200 (2020)
   PUBMED   32548984
  REMARK    GeneRIF: Controlling the Release of Neurotrophin-3 and
            Chondroitinase ABC Enhances the Efficacy of Nerve Guidance
            Conduits.
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Smith,M.A., Makino,S., Altemus,M., Michelson,D., Hong,S.K.,
            Kvetnansky,R. and Post,R.M.
  TITLE     Stress and antidepressants differentially regulate neurotrophin 3
            mRNA expression in the locus coeruleus
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8788-8792 (1995)
   PUBMED   7568018
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Le Beau,M.M., Espinosa,R. 3rd, Ip,N.Y.,
            Belluscio,L., de la Monte,S.M., Squinto,S., Furth,M.E. and
            Yancopoulos,G.D.
  TITLE     Human and rat brain-derived neurotrophic factor and neurotrophin-3:
            gene structures, distributions, and chromosomal localizations
  JOURNAL   Genomics 10 (3), 558-568 (1991)
   PUBMED   1889806
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Hallbook,F., Ibanez,C.F. and Persson,H.
  TITLE     Evolutionary studies of the nerve growth factor family reveal a
            novel member abundantly expressed in Xenopus ovary
  JOURNAL   Neuron 6 (5), 845-858 (1991)
   PUBMED   2025430
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Ernfors,P., Ibanez,C.F., Ebendal,T., Olson,L. and Persson,H.
  TITLE     Molecular cloning and neurotrophic activities of a protein with
            structural similarities to nerve growth factor: developmental and
            topographical expression in the brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5454-5458 (1990)
   PUBMED   2164684
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Maisonpierre,P.C., Belluscio,L., Squinto,S., Ip,N.Y., Furth,M.E.,
            Lindsay,R.M. and Yancopoulos,G.D.
  TITLE     Neurotrophin-3: a neurotrophic factor related to NGF and BDNF
  JOURNAL   Science 247 (4949 Pt 1), 1446-1451 (1990)
   PUBMED   2321006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1, FM074856.1, M34643.1 and BC070504.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and 5'
            coding region, compared to variant 1. The resulting isoform (2) is
            of the same size but has a distinct N-terminus, compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM074856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680421, SAMN06680441
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..271
                     /product="neurotrophin-3 isoform 2 precursor"
                     /note="HDNF; NT-3; NGF-2; neurotrophic factor; nerve
                     growth factor 2; neurotrophin-3 (HDNF/NT-3)"
                     /calculated_mol_wt=27558
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3590
     Region          33..146
                     /region_name="NTF3_N"
                     /note="Neutrophin-3 N-terminus; pfam19338"
                     /db_xref="CDD:437170"
     Region          158..269
                     /region_name="NGF"
                     /note="Nerve growth factor family; pfam00243"
                     /db_xref="CDD:459728"
     CDS             1..271
                     /gene="Ntf3"
                     /coded_by="NM_001270868.1:239..1054"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:81737"
                     /db_xref="RGD:619728"
ORIGIN      
        1 mlgflkilqv nkvmsilfyv iflaylrgiq gnnmdqrslp edslnsliik liqadilknk
       61 lskqmvdvke nyqstlpkae aprepeqgea trsefqpmia tdtellrqqr rynsprvlls
      121 dstplepppl ylmedyvgnp vvtnrtsprr kryaehkshr geysvcdses lwvtdkssai
      181 dirghqvtvl geiktgnspv kqyfyetrck earpvkngcr giddkhwnsq cktsqtyvra
      241 ltsennklvg wrwiridtsc vcalsrkigr t
//
LOCUS       NP_001257342             840 aa            linear   ROD 27-APR-2025
DEFINITION  KN motif and ankyrin repeat domain-containing protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001257342 XP_002729921
VERSION     NP_001257342.1
DBSOURCE    REFSEQ: accession NM_001270413.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Li,L., Li,Z.B., Jia,M. and Chu,H.T.
  TITLE     Therapeutic effects of KANK2 in myocardial infarction rats might be
            associated with the NF-kappaB p65 inhibition
  JOURNAL   Int Immunopharmacol 86, 106687 (2020)
   PUBMED   32570033
  REMARK    GeneRIF: Therapeutic effects of KANK2 in myocardial infarction rats
            might be associated with the NF-kappaB p65 inhibition.
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Jurewicz,E., Miazga,K., Fabczak,H., Slawinska,U. and Filipek,A.
  TITLE     CacyBP/SIP in the rat spinal cord in norm and after transection -
            Influence on the phosphorylation state of ERK1/2 and p38 kinases
  JOURNAL   Neurochem Int 138, 104757 (2020)
   PUBMED   32544715
  REMARK    GeneRIF: CacyBP/SIP in the rat spinal cord in norm and after
            transection - Influence on the phosphorylation state of ERK1/2 and
            p38 kinases.
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Gee,H.Y., Zhang,F., Ashraf,S., Kohl,S., Sadowski,C.E.,
            Vega-Warner,V., Zhou,W., Lovric,S., Fang,H., Nettleton,M.,
            Zhu,J.Y., Hoefele,J., Weber,L.T., Podracka,L., Boor,A.,
            Fehrenbach,H., Innis,J.W., Washburn,J., Levy,S., Lifton,R.P.,
            Otto,E.A., Han,Z. and Hildebrandt,F.
  TITLE     KANK deficiency leads to podocyte dysfunction and nephrotic
            syndrome
  JOURNAL   J Clin Invest 125 (6), 2375-2384 (2015)
   PUBMED   25961457
  REMARK    GeneRIF: In rats, KANK1, KANK2, and KANK4 all localized to
            podocytes in glomeruli, and KANK1 partially colocalized with
            synaptopodin.
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Ramot,Y., Molho-Pessach,V., Meir,T., Alper-Pinus,R., Siam,I.,
            Tams,S., Babay,S. and Zlotogorski,A.
  TITLE     Mutation in KANK2, encoding a sequestering protein for steroid
            receptor coactivators, causes keratoderma and woolly hair
  JOURNAL   J Med Genet 51 (6), 388-394 (2014)
   PUBMED   24671081
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Wang,D., Liang,J., Zhang,Y., Gui,B., Wang,F., Yi,X., Sun,L., Yao,Z.
            and Shang,Y.
  TITLE     Steroid receptor coactivator-interacting protein (SIP) inhibits
            caspase-independent apoptosis by preventing apoptosis-inducing
            factor (AIF) from being released from mitochondria
  JOURNAL   J Biol Chem 287 (16), 12612-12621 (2012)
   PUBMED   22371500
REFERENCE   6  (residues 1 to 840)
  AUTHORS   Zhang,Y., Zhang,H., Liang,J., Yu,W. and Shang,Y.
  TITLE     SIP, a novel ankyrin repeat containing protein, sequesters steroid
            receptor coactivators in the cytoplasm
  JOURNAL   EMBO J 26 (11), 2645-2657 (2007)
   PUBMED   17476305
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 4, 2012 this sequence version replaced XP_002729921.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760386, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..840
                     /product="KN motif and ankyrin repeat domain-containing
                     protein 2"
                     /calculated_mol_wt=90092
     Region          1..72
                     /region_name="Interaction with AIFM1.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          31..>59
                     /region_name="KN_motif"
                     /note="KN motif; pfam12075"
                     /db_xref="CDD:432311"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            105
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          161..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          <425..573
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Region          495..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3; propagated from
                     UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          603..640
                     /region_name="ANK 0, degenerate.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          617..653
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <639..814
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          655..724
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          655..685
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          658..824
                     /region_name="Interaction with NCOA1.
                     /evidence=ECO:0000250|UniProtKB:Q63ZY3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZD05.2)"
     Region          728..758
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(729,733..734,737..739,741..742,746,749,758,760,762,
                     766..767,770..772,774..775,779,782,792,794,796,800..801,
                     804..806,808..809,813,816)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          760..792
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..840
                     /gene="Kank2"
                     /gene_synonym="RGD1563532"
                     /coded_by="NM_001270413.1:160..2682"
                     /db_xref="GeneID:100361376"
                     /db_xref="RGD:2320289"
ORIGIN      
        1 maqvlhvpap fpgtpgqass aafpnkepdp pysvetpygy rldldflkyv ddiekghtlr
       61 rvpvqrrprl gslprgpgsw wtsteslcsd asgdsrhsay sycgrgfypq ygaletrsgt
      121 nprvertlld arrrledqaa apssgglgsl tpsaagstss lagvgllppt prssglstpv
      181 apsaghlahv reqmagalrk lrqleeqvkl ipvlqvklsv lqeekrqltv qlksqkflgh
      241 psgtrsrsel cldlpeapdd pavletrsvg twvrerdlgi pdgeaalvak vavletqlkk
      301 alqelraaqt qqvdlqpqaw pppdtqvrvd tvrvvegpre vevaastaag apaqraqsle
      361 pygaglkala tsaentlvfr shevvetmcp lptastsnmh takkisiter nctgaarmae
      421 pspsspypaa epenpapaaq dttdreltrp vasqdsqaae gaggaslgvq salkrkevpa
      481 dpdvhqrnlq fvginggyes ssedsstaen sehestenea peppvrvlst aegpqlrplg
      541 pavgktsqde rqlsqesqrv peakvapgpd peeeirmdls pdlisaclal ekylenpnal
      601 terelkvayt tvlqewlrla crsdahpelv rrhlvtfram sarlldyvvn iadsngntal
      661 hysvshanfp vvrqlldsgv cqvdklnrag yspimltala tlktqddidt ilqlfrlgnv
      721 nakasqagqt almlavshgr vdvvkallac evdvnmqded gstalmcace hghkeitgll
      781 lavpscdisl tdrdgstalm valdagqsei asmlysrmni kcsfapmsdy espasssaee
//
LOCUS       NP_001264190             249 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, slow skeletal muscle isoform 3 [Rattus norvegicus].
ACCESSION   NP_001264190
VERSION     NP_001264190.1
DBSOURCE    REFSEQ: accession NM_001277261.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Tsika,R.W., Schramm,C., Simmer,G., Fitzsimons,D.P., Moss,R.L. and
            Ji,J.
  TITLE     Overexpression of TEAD-1 in transgenic mouse striated muscles
            produces a slower skeletal muscle contractile phenotype
  JOURNAL   J Biol Chem 283 (52), 36154-36167 (2008)
   PUBMED   18978355
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Pinto,J.R., Parvatiyar,M.S., Jones,M.A., Liang,J. and Potter,J.D.
  TITLE     A troponin T mutation that causes infantile restrictive
            cardiomyopathy increases Ca2+ sensitivity of force development and
            impairs the inhibitory properties of troponin
  JOURNAL   J Biol Chem 283 (4), 2156-2166 (2008)
   PUBMED   18032382
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Kischel,P., Bastide,B., Muller,M., Dubail,F., Offredi,F., Jin,J.P.,
            Mounier,Y. and Martial,J.
  TITLE     Expression and functional properties of four slow skeletal troponin
            T isoforms in rat muscles
  JOURNAL   Am J Physiol Cell Physiol 289 (2), C437-C443 (2005)
   PUBMED   15788488
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Wang,X., Huang,Q.Q., Breckenridge,M.T., Chen,A., Crawford,T.O.,
            Morton,D.H. and Jin,J.P.
  TITLE     Cellular fate of truncated slow skeletal muscle troponin T produced
            by Glu180 nonsense mutation in amish nemaline myopathy
  JOURNAL   J Biol Chem 280 (14), 13241-13249 (2005)
   PUBMED   15665378
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Johnston,J.J., Kelley,R.I., Crawford,T.O., Morton,D.H.,
            Agarwala,R., Koch,T., Schaffer,A.A., Francomano,C.A. and
            Biesecker,L.G.
  TITLE     A novel nemaline myopathy in the Amish caused by a mutation in
            troponin T1
  JOURNAL   Am J Hum Genet 67 (4), 814-821 (2000)
   PUBMED   10952871
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Gahlmann,R., Troutt,A.B., Wade,R.P., Gunning,P. and Kedes,L.
  TITLE     Alternative splicing generates variants in important functional
            domains of human slow skeletal troponin T
  JOURNAL   J Biol Chem 262 (33), 16122-16126 (1987)
   PUBMED   2824479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and AY334082.1.
            
            Transcript Variant: This variant (3) lacks an exon and uses an
            alternate splice site in the coding region, compared to variant 1.
            The encoded isoform (3) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY334082.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760386, SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..249
                     /product="troponin T, slow skeletal muscle isoform 3"
                     /note="troponin T, slow skeletal muscle; slow skeletal
                     muscle troponin T; troponin T1, skeletal, slow; troponin T
                     type 1 (skeletal, slow)"
                     /calculated_mol_wt=29750
     Region          56..192
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     Region          167..>225
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..249
                     /gene="Tnnt1"
                     /gene_synonym="Fang2; sTnT; tnTs"
                     /coded_by="NM_001277261.2:57..806"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:171409"
                     /db_xref="RGD:621852"
ORIGIN      
        1 msdteeqeye eeqaedeeav eeeeerpkps rpvvpplipp kipegervdf ddihrkrmek
       61 dllelqtlid vhfeqrkkee eelialkdri errraeraeq qrfrtekere rqaklaeekm
      121 rkeeeeakkr aeddakkkkv lsnmgahfgg ylvkaeqkrg krqtgremkl rilserkkpl
      181 nidymgedql rekaqelsew ihqlesekfd lmeklkqqky einvlynris haqkfrkgag
      241 kgrvggrwk
//
LOCUS       NP_036678                446 aa            linear   ROD 27-APR-2025
DEFINITION  D(1A) dopamine receptor [Rattus norvegicus].
ACCESSION   NP_036678
VERSION     NP_036678.3
DBSOURCE    REFSEQ: accession NM_012546.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Andreska,T., Luningschror,P., Wolf,D., McFleder,R.L.,
            Ayon-Olivas,M., Rattka,M., Drechsler,C., Perschin,V., Blum,R.,
            Aufmkolk,S., Granado,N., Moratalla,R., Sauer,M., Monoranu,C.,
            Volkmann,J., Ip,C.W., Stigloher,C. and Sendtner,M.
  TITLE     DRD1 signaling modulates TrkB turnover and BDNF sensitivity in
            direct pathway striatal medium spiny neurons
  JOURNAL   Cell Rep 42 (6), 112575 (2023)
   PUBMED   37252844
  REMARK    GeneRIF: DRD1 signaling modulates TrkB turnover and BDNF
            sensitivity in direct pathway striatal medium spiny neurons.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Witt,K.M., Harper,D.N. and Ellenbroek,B.A.
  TITLE     Dopamine D1 receptor and effort-based decision making in rats: The
            moderating effect of sex
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 120, 110651 (2023)
   PUBMED   36191805
  REMARK    GeneRIF: Dopamine D1 receptor and effort-based decision making in
            rats: The moderating effect of sex.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Babushkina,N. and Manahan-Vaughan,D.
  TITLE     Frequency-dependency of the involvement of dopamine D1/D5 and
            beta-adrenergic receptors in hippocampal LTD triggered by locus
            coeruleus stimulation
  JOURNAL   Hippocampus 32 (6), 449-465 (2022)
   PUBMED   35478421
  REMARK    GeneRIF: Frequency-dependency of the involvement of dopamine D1/D5
            and beta-adrenergic receptors in hippocampal LTD triggered by locus
            coeruleus stimulation.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Mesgar,S., Jameie,S.B., Aliaghaei,A., Parvardeh,S., Torabi,A. and
            Haghparast,A.
  TITLE     Dopamine D1 Receptor-Mediated Regulation of Per1, Per2, CLOCK, and
            BMAL1 Expression in the Suprachiasmatic Nucleus in Adult Male Rats
  JOURNAL   J Mol Neurosci 72 (3), 618-625 (2022)
   PUBMED   34751875
  REMARK    GeneRIF: Dopamine D1 Receptor-Mediated Regulation of Per1, Per2,
            CLOCK, and BMAL1 Expression in the Suprachiasmatic Nucleus in Adult
            Male Rats.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Ramires Lima,K., de Souza da Rosa,A.C., Severo Picua,S., Souza E
            Silva,S., Marks Soares,N. and Billig Mello-Carpes,P.
  TITLE     One single physical exercise session improves memory persistence by
            hippocampal activation of D1 dopamine receptors and PKA signaling
            in rats
  JOURNAL   Brain Res 1762, 147439 (2021)
   PUBMED   33753064
  REMARK    GeneRIF: One single physical exercise session improves memory
            persistence by hippocampal activation of D1 dopamine receptors and
            PKA signaling in rats.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Zhou,Q.Y., Li,C. and Civelli,O.
  TITLE     Characterization of gene organization and promoter region of the
            rat dopamine D1 receptor gene
  JOURNAL   J Neurochem 59 (5), 1875-1883 (1992)
   PUBMED   1402930
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Liu,Y.F., Civelli,O., Zhou,Q.Y. and Albert,P.R.
  TITLE     Cholera toxin-sensitive 3',5'-cyclic adenosine monophosphate and
            calcium signals of the human dopamine-D1 receptor: selective
            potentiation by protein kinase A
  JOURNAL   Mol Endocrinol 6 (11), 1815-1824 (1992)
   PUBMED   1282671
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Salkovic,M. and Lackovic,Z.
  TITLE     Brain D1 dopamine receptor in alloxan-induced diabetes
  JOURNAL   Diabetes 41 (9), 1119-1121 (1992)
   PUBMED   1386820
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Tiberi,M., Jarvie,K.R., Silvia,C., Falardeau,P., Gingrich,J.A.,
            Godinot,N., Bertrand,L., Yang-Feng,T.L., Fremeau,R.T. Jr. and
            Caron,M.G.
  TITLE     Cloning, molecular characterization, and chromosomal assignment of
            a gene encoding a second D1 dopamine receptor subtype: differential
            expression pattern in rat brain compared with the D1A receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7491-7495 (1991)
   PUBMED   1831904
REFERENCE   10 (residues 1 to 446)
  AUTHORS   O'Dowd,B.F., Nguyen,T., Tirpak,A., Jarvie,K.R., Israel,Y.,
            Seeman,P. and Niznik,H.B.
  TITLE     Cloning of two additional catecholamine receptors from rat brain
  JOURNAL   FEBS Lett 262 (1), 8-12 (1990)
   PUBMED   2138567
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Feb 3, 2015 this sequence version replaced NP_036678.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M35077.1, SRR21887623.1696807.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..446
                     /product="D(1A) dopamine receptor"
                     /note="Dopamine-1A receptor; dopamine receptor D1A"
                     /calculated_mol_wt=49321
     Site            4
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18901.2)"
     Region          22..341
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            23..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Region          25..49
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320443"
     Region          59..81
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320443"
     Site            60..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Region          96..118
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320443"
     Site            96..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Site            138..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Region          141..157
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320443"
     Region          192..215
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320443"
     Site            193..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Region          271..293
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320443"
     Site            273..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     Region          310..335
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320443"
     Site            313..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18901.2)"
     CDS             1..446
                     /gene="Drd1"
                     /gene_synonym="D1a; Drd-1; Drd1a"
                     /coded_by="NM_012546.3:439..1779"
                     /db_xref="GeneID:24316"
                     /db_xref="RGD:2518"
ORIGIN      
        1 mapntstmde aglpaerdfs friltacfls llilstllgn tlvcaavirf rhlrskvtnf
       61 fvislavsdl lvavlvmpwk avaeiagfwp fgsfcniwva fdimcstasi lnlcvisvdr
      121 ywaisspfqy erkmtpkaaf ilisvawtls vlisfipvql swhkakptwp ldgnftsled
      181 teddncdtrl srtyaisssl isfyipvaim ivtytsiyri aqkqirrisa leraavhakn
      241 cqttagngnp vecaqsessf kmsfkretkv lktlsvimgv fvccwlpffi sncmvpfcgs
      301 eetqpfcids itfdvfvwfg wansslnpii yafnadfqka fstllgcyrl cpttnnaiet
      361 vsinnngavv fsshheprgs iskdcnlvyl iphavgssed lkkeeaggia kpleklspal
      421 svildydtdv slekiqpvth sgqhst
//
LOCUS       NP_037308                707 aa            linear   ROD 27-APR-2025
DEFINITION  transcription factor 12 [Rattus norvegicus].
ACCESSION   NP_037308 XP_346830
VERSION     NP_037308.1
DBSOURCE    REFSEQ: accession NM_013176.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Wu,K., Li,S., Bodhinathan,K., Meyers,C., Chen,W.,
            Campbell-Thompson,M., McIntyre,L., Foster,T.C., Muzyczka,N. and
            Kumar,A.
  TITLE     Enhanced expression of Pctk1, Tcf12 and Ccnd1 in hippocampus of
            rats: Impact on cognitive function, synaptic plasticity and
            pathology
  JOURNAL   Neurobiol Learn Mem 97 (1), 69-80 (2012)
   PUBMED   21982980
  REMARK    GeneRIF: The learning and memory deficits in Tcf12 animals are
            likely due to neuropathology associated with Tcf12 gene expression.
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Yoon,S.J., Wills,A.E., Chuong,E., Gupta,R. and Baker,J.C.
  TITLE     HEB and E2A function as SMAD/FOXH1 cofactors
  JOURNAL   Genes Dev 25 (15), 1654-1661 (2011)
   PUBMED   21828274
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Jia,J., Dai,M. and Zhuang,Y.
  TITLE     E proteins are required to activate germline transcription of the
            TCR Vbeta8.2 gene
  JOURNAL   Eur J Immunol 38 (10), 2806-2820 (2008)
   PUBMED   18958875
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Ravanpay,A.C. and Olson,J.M.
  TITLE     E protein dosage influences brain development more than family
            member identity
  JOURNAL   J Neurosci Res 86 (7), 1472-1481 (2008)
   PUBMED   18214987
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Wissmuller,S., Kosian,T., Wolf,M., Finzsch,M. and Wegner,M.
  TITLE     The high-mobility-group domain of Sox proteins interacts with
            DNA-binding domains of many transcription factors
  JOURNAL   Nucleic Acids Res 34 (6), 1735-1744 (2006)
   PUBMED   16582099
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Lin,H.H., Li,W.Y. and Ann,D.K.
  TITLE     The helix-loop-helix proteins (salivary-specific cAMP response
            element-binding proteins) can modulate cAMP-inducible RP4 gene
            expression in salivary cells
  JOURNAL   J Biol Chem 268 (14), 10214-10220 (1993)
   PUBMED   7683670
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Klein,E.S., Simmons,D.M., Swanson,L.W. and Rosenfeld,M.G.
  TITLE     Tissue-specific RNA splicing generates an ankyrin-like domain that
            affects the dimerization and DNA-binding properties of a bHLH
            protein
  JOURNAL   Genes Dev 7 (1), 55-71 (1993)
   PUBMED   8422988
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Nielsen,A.L., Pallisgaard,N., Pedersen,F.S. and Jorgensen,P.
  TITLE     Murine helix-loop-helix transcriptional activator proteins binding
            to the E-box motif of the Akv murine leukemia virus enhancer
            identified by cDNA cloning
  JOURNAL   Mol Cell Biol 12 (8), 3449-3459 (1992)
   PUBMED   1321336
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Sun,X.H., Copeland,N.G., Jenkins,N.A. and Baltimore,D.
  TITLE     Id proteins Id1 and Id2 selectively inhibit DNA binding by one
            class of helix-loop-helix proteins
  JOURNAL   Mol Cell Biol 11 (11), 5603-5611 (1991)
   PUBMED   1922066
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L09656.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346830.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L09656.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..707
                     /product="transcription factor 12"
                     /note="E-box-binding protein; DNA-binding protein HTF4;
                     transcription factor HTF-4; salivary-specific cAMP
                     response element-binding protein alpha; TCF-12;
                     SCBP-alpha"
                     /calculated_mol_wt=75765
     Region          25..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Region          119..140
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61286; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Region          140..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Region          249..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Region          275..>411
                     /region_name="CytochromB561_N"
                     /note="Cytochrome B561, N terminal; cl46356"
                     /db_xref="CDD:480696"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Region          349..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Region          521..605
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99081; propagated from
                     UniProtKB/Swiss-Prot (P51514.1)"
     Region          596..680
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(604,608,610..612,614,619,640..641)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(617..618,621..622,624..625,628,632,642,645,649,652,
                     655..660)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     Region          657..680
                     /region_name="Class A specific domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     Region          675..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51514.1)"
     CDS             1..707
                     /gene="Tcf12"
                     /gene_synonym="SCBP alpha; SCBPA"
                     /coded_by="NM_013176.2:204..2327"
                     /db_xref="GeneID:25720"
                     /db_xref="RGD:3829"
ORIGIN      
        1 mnpqqqrmaa igtdkelsdl ldfsamfspp vnsgktrptt lgssqfsgsg mderggttsw
       61 gtsgqpspsy dssrgftdsp hysdhlndsr lgtheglspt pfmnsnligk tsergsfsly
      121 srdsglsgcq ssllrqdlgl gspaqlsssg kpgtpyysfs atssrrrplh dsvaldplqa
      181 kkvrkvppgl pssvyapspn sddfnresps ypspkpptsm fastffmqdg thsssdlwss
      241 sngmsqpgfg gilgtstshm sqsssygslh shdrlsypph svsptdints lppmssfhrg
      301 stssspyvaa shtppingsd silgtrgnaa gssqtgdalg kalasiyspd htsssfpsnp
      361 stpvgspspl tagtsqwpra ggqapsspsy enslhslknr veqqlhehlq damsflkdvc
      421 eqsrmedrld rlddaihvlr nhavgpstsl ptshsdihsl lgpshnapig nlnsnyggss
      481 lvtnsrsasm vgthredsvs lngnhsvlss tvaasnteln hktpesfrgg vqnqsgsvvp
      541 teiktenkek denlheppss ddmksddess qkdikvssrg rtsstneded lnpeqkiere
      601 kerrmannar erlrvrdine afkelgrmcq lhlksekpqt kllilhqava vilsleqqvr
      661 ernlnpkaac lkrreeekvs aasaeppttl pgthpglset tnpmghl
//
LOCUS       NP_001273954             171 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione S-transferase alpha-5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001273954
VERSION     NP_001273954.1
DBSOURCE    REFSEQ: accession NM_001287025.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Xiao,Y., Zhang,Z., Fu,Y., Shan,H., Cui,S. and Wu,J.
  TITLE     GSTA3 regulates TGF-beta1-induced renal interstitial fibrosis in
            NRK-52E cells as a component of the PI3K-Keap1/Nrf2 pathway
  JOURNAL   J Int Med Res 47 (11), 5787-5801 (2019)
   PUBMED   31617428
  REMARK    GeneRIF: The PI3K-KEAP1/Nrf2-GSTA3 signaling pathway is a possible
            mechanism of resisting external stimulation of renal fibrosis
            factors.
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Chen,H., Gan,Q., Yang,C., Peng,X., Qin,J., Qiu,S., Jiang,Y., Tu,S.,
            He,Y., Li,S., Yang,H., Tao,L. and Peng,Y.
  TITLE     A novel role of glutathione S-transferase A3 in inhibiting hepatic
            stellate cell activation and rat hepatic fibrosis
  JOURNAL   J Transl Med 17 (1), 280 (2019)
   PUBMED   31443720
  REMARK    GeneRIF: GSTA3 inhibited hepatic stellate cell activation and liver
            fibrosis
            Erratum:[J Transl Med. 2020 Apr 30;18(1):182. doi:
            10.1186/s12967-020-02346-4. PMID: 32354374]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Xiao,Y., Liu,J., Peng,Y., Xiong,X., Huang,L., Yang,H., Zhang,J. and
            Tao,L.
  TITLE     GSTA3 Attenuates Renal Interstitial Fibrosis by Inhibiting
            TGF-Beta-Induced Tubular Epithelial-Mesenchymal Transition and
            Fibronectin Expression
  JOURNAL   PLoS One 11 (9), e0160855 (2016)
   PUBMED   27602565
  REMARK    GeneRIF: Protein and mRNA expression of GSTA3 in UUO rats and
            NRK-52E cells were determined by Western blot and RT-PCR. siRNA and
            overexpression plasmid were transfected specifically to assess the
            role of GSTA3 in renal interstitial fibrosis
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Ilic,Z., Crawford,D., Vakharia,D., Egner,P.A. and Sell,S.
  TITLE     Glutathione-S-transferase A3 knockout mice are sensitive to acute
            cytotoxic and genotoxic effects of aflatoxin B1
  JOURNAL   Toxicol Appl Pharmacol 242 (3), 241-246 (2010)
   PUBMED   19850059
  REMARK    Erratum:[Toxicol Appl Pharmacol. 2010 Jun 1;245(2):280. doi:
            10.1016/j.taap.2010.03.018. PMID: 20852735]
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Caruana,G., Cullen-McEwen,L., Nelson,A.L., Kostoulias,X., Woods,K.,
            Gardiner,B., Davis,M.J., Taylor,D.F., Teasdale,R.D., Grimmond,S.M.,
            Little,M.H. and Bertram,J.F.
  TITLE     Spatial gene expression in the T-stage mouse metanephros
  JOURNAL   Gene Expr Patterns 6 (8), 807-825 (2006)
   PUBMED   16545622
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Pulford,D.J. and Hayes,J.D.
  TITLE     Characterization of the rat glutathione S-transferase Yc2 subunit
            gene, GSTA5: identification of a putative antioxidant-responsive
            element in the 5'-flanking region of rat GSTA5 that may mediate
            chemoprotection against aflatoxin B1
  JOURNAL   Biochem J 318 (Pt 1) (Pt 1), 75-84 (1996)
   PUBMED   8761455
REFERENCE   7  (residues 1 to 171)
  AUTHORS   Hayes,J.D., Nguyen,T., Judah,D.J., Petersson,D.G. and Neal,G.E.
  TITLE     Cloning of cDNAs from fetal rat liver encoding glutathione
            S-transferase Yc polypeptides. The Yc2 subunit is expressed in
            adult rat liver resistant to the hepatocarcinogen aflatoxin B1
  JOURNAL   J Biol Chem 269 (32), 20707-20717 (1994)
   PUBMED   8051171
REFERENCE   8  (residues 1 to 171)
  AUTHORS   Klinga-Levan,K., Andersson,A., Hanson,C., Ridderstrom,M.,
            Stenberg,G., Mannervik,B., Vajdy,M., Szpirer,J., Szpirer,C. and
            Levan,G.
  TITLE     Mapping of glutathione transferase (GST) genes in the rat
  JOURNAL   Hereditas 119 (3), 285-296 (1993)
   PUBMED   8144363
REFERENCE   9  (residues 1 to 171)
  AUTHORS   Hayes,J.D., Judah,D.J., McLellan,L.I., Kerr,L.A., Peacock,S.D. and
            Neal,G.E.
  TITLE     Ethoxyquin-induced resistance to aflatoxin B1 in the rat is
            associated with the expression of a novel alpha-class glutathione
            S-transferase subunit, Yc2, which possesses high catalytic activity
            for aflatoxin B1-8,9-epoxide
  JOURNAL   Biochem J 279 (Pt 2) (Pt 2), 385-398 (1991)
   PUBMED   1953636
REFERENCE   10 (residues 1 to 171)
  AUTHORS   Pickett,C.B., Telakowski-Hopkins,C.A., Ding,G.J., Argenbright,L.
            and Lu,A.Y.
  TITLE     Rat liver glutathione S-transferases. Complete nucleotide sequence
            of a glutathione S-transferase mRNA and the regulation of the Ya,
            Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital
  JOURNAL   J Biol Chem 259 (8), 5182-5188 (1984)
   PUBMED   6325423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Transcript Variant: This variant (3) lacks an alternate 5' exon
            compared to variant 1 that results in the use of a downstream
            translation initiation codon. The resulting protein (isoform 2) is
            shorter and has a distinct N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the Celera
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210706.1, SRR26643288.36971.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..171
                     /product="glutathione S-transferase alpha-5 isoform 2"
                     /EC_number="2.5.1.18"
                     /note="glutathione S-transferase alpha-5; GST Yc2; GST
                     A5-5; glutathione S-transferase Yc2 subunit; glutathione
                     S-transferase A3"
                     /calculated_mol_wt=19502
     Region          <1..32
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Region          36..170
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(36..37,39,43..45,47..48,51,81)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(47,54,57,60..61,81..82,85,102..105,108,111..112,
                     115..116,119,143..144,146..151)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(51,57,61,81,158,166,170)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     CDS             1..171
                     /gene="Gsta3"
                     /gene_synonym="Gsta5; Yc2"
                     /coded_by="NM_001287025.1:241..756"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:494500"
                     /db_xref="RGD:1591980"
ORIGIN      
        1 mfeqvpmvei dgmklvqtka ilnyiatkyn lygkdmkera lidmyaegva dlelmvlyyp
       61 ymppgekeas lakikdkarn ryfpayekvl kshgqdylvg nklsradvsl vellyhveem
      121 dpgivdnfpl lkalrtrvsn lptvkkflqp gsqrkpfdde kcvesakkif s
//
LOCUS       NP_001231748             211 aa            linear   ROD 27-APR-2025
DEFINITION  SOSS complex subunit B1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001231748
VERSION     NP_001231748.1
DBSOURCE    REFSEQ: accession NM_001244819.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Pandita,R.K., Chow,T.T., Udayakumar,D., Bain,A.L., Cubeddu,L.,
            Hunt,C.R., Shi,W., Horikoshi,N., Zhao,Y., Wright,W.E., Khanna,K.K.,
            Shay,J.W. and Pandita,T.K.
  TITLE     Single-strand DNA-binding protein SSB1 facilitates TERT recruitment
            to telomeres and maintains telomere G-overhangs
  JOURNAL   Cancer Res 75 (5), 858-869 (2015)
   PUBMED   25589350
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Gu,P., Deng,W., Lei,M. and Chang,S.
  TITLE     Single strand DNA binding proteins 1 and 2 protect newly replicated
            telomeres
  JOURNAL   Cell Res 23 (5), 705-719 (2013)
   PUBMED   23459151
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Li,Y., Bolderson,E., Kumar,R., Muniandy,P.A., Xue,Y., Richard,D.J.,
            Seidman,M., Pandita,T.K., Khanna,K.K. and Wang,W.
  TITLE     HSSB1 and hSSB2 form similar multiprotein complexes that
            participate in DNA damage response
  JOURNAL   J Biol Chem 284 (35), 23525-23531 (2009)
   PUBMED   19605351
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Huang,J., Gong,Z., Ghosal,G. and Chen,J.
  TITLE     SOSS complexes participate in the maintenance of genomic stability
  JOURNAL   Mol Cell 35 (3), 384-393 (2009)
   PUBMED   19683501
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Richard,D.J., Bolderson,E., Cubeddu,L., Wadsworth,R.I., Savage,K.,
            Sharma,G.G., Nicolette,M.L., Tsvetanov,S., McIlwraith,M.J.,
            Pandita,R.K., Takeda,S., Hay,R.T., Gautier,J., West,S.C.,
            Paull,T.T., Pandita,T.K., White,M.F. and Khanna,K.K.
  TITLE     Single-stranded DNA-binding protein hSSB1 is critical for genomic
            stability
  JOURNAL   Nature 453 (7195), 677-681 (2008)
   PUBMED   18449195
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV214819.1 and BC104710.1.
            
            Transcript Variant: This variant (2) contains different sequence
            for its 5' end, which results in the use of a downstream start
            codon, compared to variant 1. The resulting protein (isoform 2) is
            shorter when it is compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219805.1, CO400924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..211
                     /product="SOSS complex subunit B1 isoform 2"
                     /note="SOSS complex subunit B1; SOSS-B1; sensor of ssDNA
                     subunit B1; single-stranded DNA-binding protein 1; sensor
                     of single-strand DNA complex subunit B1;
                     oligonucleotide/oligosaccharide-binding fold-containing
                     protein 2B; oligonucleotide/oligosaccharide-binding fold
                     containing 2B"
                     /calculated_mol_wt=22246
     Region          18..95
                     /region_name="SoSSB_OBF"
                     /note="A subfamily of OB folds similar to the OB fold of
                     the crenarchaeote Sulfolobus solfataricus single-stranded
                     (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB
                     fold, and it physically and functionally interacts with
                     RNA polymerase. In vitro, SSoSSB...; cd04491"
                     /db_xref="CDD:239937"
     Site            order(18,67,69,71,93)
                     /site_type="active"
                     /note="generic binding surface II [active]"
                     /db_xref="CDD:239937"
     Site            order(23..25,40..43,45,51..53,55,66,74..76,83..85)
                     /site_type="active"
                     /note="generic binding surface I [active]"
                     /db_xref="CDD:239937"
     Region          <106..>187
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          110..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWT1.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM.
                     /evidence=ECO:0000250|UniProtKB:Q9BQ15; propagated from
                     UniProtKB/Swiss-Prot (Q3SWT1.1)"
     CDS             1..211
                     /gene="Nabp2"
                     /gene_synonym="Obfc2b; RGD1308158"
                     /coded_by="NM_001244819.1:121..756"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362813"
                     /db_xref="RGD:1308158"
ORIGIN      
        1 mttetfvkdi kpglknlnli fivletgrvt ktkdghevrt ckvadktgsi nisvwddvgn
       61 liqpgdiirl tkgyasvfkg cltlytgrgg dlqkigefcm vysevpnfse pnpeyntqqa
      121 snksvqndss ptapqattgp paaspasesq ngnglstqpg pvggphpsha pshppstrit
      181 rsqpnhtpsg ppgpssspvs ngketrrssk r
//
LOCUS       NP_036688                127 aa            linear   ROD 27-APR-2025
DEFINITION  fatty acid-binding protein, liver [Rattus norvegicus].
ACCESSION   NP_036688
VERSION     NP_036688.1
DBSOURCE    REFSEQ: accession NM_012556.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Ohata,K., Sugaya,T., Nguyen,H.N., Hatanaka,Y., Uno,K., Tohma,M.,
            Oikawa,T., Nagabukuro,H., Kuniyeda,K., Kamijo-Ikemori,A.,
            Suzuki-Kemuriyama,N., Nakae,D., Noiri,E. and Miyajima,K.
  TITLE     Urinary liver-type fatty acid binding protein is increased in the
            early stages of the disease with a risk of acute kidney injury
            induced by histone
  JOURNAL   Nephrology (Carlton) 28 (6), 345-355 (2023)
   PUBMED   37076661
  REMARK    GeneRIF: Urinary liver-type fatty acid binding protein is increased
            in the early stages of the disease with a risk of acute kidney
            injury induced by histone.
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Tanabe,J., Ogura,Y., Kosaki,K., Nagai,Y., Sugaya,T., Ohata,K.,
            Watanabe,S., Ichikawa,D., Inoue,K., Hoshino,S., Kimura,K.,
            Maeda,S., Shibagaki,Y. and Kamijo-Ikemori,A.
  TITLE     Relationship between Urinary Liver-Type Fatty Acid-Binding Protein
            (L-FABP) and Sarcopenia in Spontaneously Diabetic Torii Fatty Rats
  JOURNAL   J Diabetes Res 2020, 7614035 (2020)
   PUBMED   32405506
  REMARK    GeneRIF: Relationship between Urinary Liver-Type Fatty Acid-Binding
            Protein (L-FABP) and Sarcopenia in Spontaneously Diabetic Torii
            Fatty Rats.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Schroeder,F., McIntosh,A.L., Martin,G.G., Huang,H., Landrock,D.,
            Chung,S., Landrock,K.K., Dangott,L.J., Li,S., Kaczocha,M.,
            Murphy,E.J., Atshaves,B.P. and Kier,A.B.
  TITLE     Fatty Acid Binding Protein-1 (FABP1) and the Human FABP1 T94A
            Variant: Roles in the Endocannabinoid System and Dyslipidemias
  JOURNAL   Lipids 51 (6), 655-676 (2016)
   PUBMED   27117865
  REMARK    GeneRIF: Studies show that despite overall tertiary structure
            similarity, the hFABP1 differs significantly from rat FABP1 in
            secondary structure, much larger ligand binding cavity, and
            affinities/specificities for some ligands. Moreover, while both
            mouse and hFABP1 mediate ligand induction of PPARA, they differ
            markedly in genes induced.
            Review article
REFERENCE   4  (residues 1 to 127)
  AUTHORS   McIntosh,A.L., Petrescu,A.D., Hostetler,H.A., Kier,A.B. and
            Schroeder,F.
  TITLE     Liver-type fatty acid binding protein interacts with hepatocyte
            nuclear factor 4alpha
  JOURNAL   FEBS Lett 587 (23), 3787-3791 (2013)
   PUBMED   24140341
  REMARK    GeneRIF: L-FABP structurally and functionally interacts with
            HNF4alpha.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Lagakos,W.S., Guan,X., Ho,S.Y., Sawicki,L.R., Corsico,B.,
            Kodukula,S., Murota,K., Stark,R.E. and Storch,J.
  TITLE     Liver fatty acid-binding protein binds monoacylglycerol in vitro
            and in mouse liver cytosol
  JOURNAL   J Biol Chem 288 (27), 19805-19815 (2013)
   PUBMED   23658011
  REMARK    GeneRIF: These results provide strong support for monoacylglycerol
            as a physiological ligand for LFABP and further suggest that LFABP
            functions in the efficient intracellular transport of MG
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Myszka,D.G. and Swenson,R.P.
  TITLE     Identification by photoaffinity labeling of fatty acid-binding
            protein as a potential warfarin receptor in rat liver
  JOURNAL   J Biol Chem 266 (31), 20725-20731 (1991)
   PUBMED   1939124
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Worrall,A.F., Evans,C. and Wilton,D.C.
  TITLE     Synthesis of a gene for rat liver fatty-acid-binding protein and
            its expression in Escherichia coli
  JOURNAL   Biochem J 278 (Pt 2) (Pt 2), 365-368 (1991)
   PUBMED   1898328
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Bassuk,J.A., Tsichlis,P.N. and Sorof,S.
  TITLE     Liver fatty acid binding protein is the mitosis-associated
            polypeptide target of a carcinogen in rat hepatocytes
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7547-7551 (1987)
   PUBMED   3478711
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Sweetser,D.A., Lowe,J.B. and Gordon,J.I.
  TITLE     The nucleotide sequence of the rat liver fatty acid-binding protein
            gene. Evidence that exon 1 encodes an oligopeptide domain shared by
            a family of proteins which bind hydrophobic ligands
  JOURNAL   J Biol Chem 261 (12), 5553-5561 (1986)
   PUBMED   3007511
REFERENCE   10 (residues 1 to 127)
  AUTHORS   McGuire,D.M., Chan,L., Smith,L.C., Towle,H.C. and Dempsey,M.E.
  TITLE     Translational control of the circadian rhythm of liver sterol
            carrier protein. Analysis of mRNA sequences with a specific cDNA
            probe
  JOURNAL   J Biol Chem 260 (9), 5435-5439 (1985)
   PUBMED   3838749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC086947.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086947.1, FQ209859.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..127
                     /product="fatty acid-binding protein, liver"
                     /note="Z-protein; squalene- and sterol-carrier protein;
                     liver-type fatty acid-binding protein; fatty acid binding
                     protein 1, liver"
                     /calculated_mol_wt=14141
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:6641731,
                     ECO:0000269|PubMed:7084456; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Region          2..127
                     /region_name="FABP1"
                     /note="fatty acid-binding protein 1; cd19444"
                     /db_xref="CDD:381219"
     Site            order(3,15,18..19,22,28..29,31..32,35,37,39,41,48,50,52,
                     54..57,59,61,63,71..74,91,93,100,102,109,111,113,122,124)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381219"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07148; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Site            84
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P12710; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12710; propagated from
                     UniProtKB/Swiss-Prot (P02692.1)"
     CDS             1..127
                     /gene="Fabp1"
                     /gene_synonym="Fabplg; L-FABP; p14; SCP; SCP."
                     /coded_by="NM_012556.2:39..422"
                     /db_xref="GeneID:24360"
                     /db_xref="RGD:2590"
ORIGIN      
        1 mnfsgkyqvq sqenfepfmk amglpedliq kgkdikgvse ivhegkkvkl titygskvih
       61 neftlgeece letmtgekvk avvkmegdnk mvttfkgiks vtefngdtit ntmtlgdivy
      121 krvskri
//
LOCUS       NP_001257553             632 aa            linear   ROD 27-APR-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257553
VERSION     NP_001257553.1
DBSOURCE    REFSEQ: accession NM_001270624.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Inaba,Y., Shinohara,K., Botilde,Y., Nabeshima,R., Takaoka,K.,
            Ajima,R., Lamri,L., Takeda,H., Saga,Y., Nakamura,T. and Hamada,H.
  TITLE     Transport of the outer dynein arm complex to cilia requires a
            cytoplasmic protein Lrrc6
  JOURNAL   Genes Cells 21 (7), 728-739 (2016)
   PUBMED   27353389
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Blasier,K.R., Humsi,M.K., Ha,J., Ross,M.W., Smiley,W.R.,
            Inamdar,N.A., Mitchell,D.J., Lo,K.W. and Pfister,K.K.
  TITLE     Live cell imaging reveals differential modifications to cytoplasmic
            dynein properties by phospho- and dephosphomimic mutations of the
            intermediate chain 2C S84
  JOURNAL   J Neurosci Res 92 (9), 1143-1154 (2014)
   PUBMED   24798412
  REMARK    GeneRIF: The data of this study suggest that the IC-2C S84 has a
            role in modulating dynein properties.
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Hirayama,M., Kobayashi,D., Mizuguchi,S., Morikawa,T., Nagayama,M.,
            Midorikawa,U., Wilson,M.M., Nambu,A.N., Yoshizawa,A.C., Kawano,S.
            and Araki,N.
  TITLE     Integrated proteomics identified novel activation of dynein
            IC2-GR-COX-1 signaling in neurofibromatosis type I (NF1) disease
            model cells
  JOURNAL   Mol Cell Proteomics 12 (5), 1377-1394 (2013)
   PUBMED   23358504
  REMARK    GeneRIF: Neurofibromatosis type I-related neural abnormalities are,
            in part, caused by up-regulation of dynein IC2-glucocorticoid
            receptor-COX-1 signaling.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Allan,V.J.
  TITLE     Cytoplasmic dynein
  JOURNAL   Biochem Soc Trans 39 (5), 1169-1178 (2011)
   PUBMED   21936784
  REMARK    Review article
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Salata,M.W., Dillman,J.F. 3rd, Lye,R.J. and Pfister,K.K.
  TITLE     Growth factor regulation of cytoplasmic dynein intermediate chain
            subunit expression preceding neurite extension
  JOURNAL   J Neurosci Res 65 (5), 408-416 (2001)
   PUBMED   11536324
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Pfister,K.K., Salata,M.W., Dillman,J.F. 3rd, Torre,E. and Lye,R.J.
  TITLE     Identification and developmental regulation of a neuron-specific
            subunit of cytoplasmic dynein
  JOURNAL   Mol Biol Cell 7 (2), 331-343 (1996)
   PUBMED   8688562
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB733957.1, FM110655.1, JAXUCZ010000003.1, BC078764.1 and
            FM076575.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U39045.1, BC078764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q22"
     Protein         1..632
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 2"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2;
                     cytoplasmic dynein 1 intermediate chain 2; DH IC-2; dynein
                     intermediate chain 2, cytosolic; cytoplasmic dynein
                     intermediate chain 2; dynein, cytoplasmic, intermediate
                     chain 2; oncofetal protein (OFP)"
                     /calculated_mol_wt=70423
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11340075; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62871.1)"
     Region          127..159
                     /region_name="Interaction with DYNLT1.
                     /evidence=ECO:0000269|PubMed:27502274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          127..157
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          148..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          270..592
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          271..320
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Site            order(273,290,304,310..311,323..324,343,348,354..355,
                     373..374,393,398,404..405,434,451,456,468..469,493,497,
                     503..504,516..517,535,540,546..547,562..563,581,585,
                     591..592)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          276..325
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          324..364
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          333..371
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          373..414
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          379..420
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          423..463
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          428..475
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          468..513
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          483..515
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          521..559
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          562..601
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62871.1)"
     Region          567..593
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..632
                     /gene="Dync1i2"
                     /gene_synonym="Dnci2; Dncic2"
                     /coded_by="NM_001270624.1:355..2253"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:116659"
                     /db_xref="RGD:620174"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keaavsvqee sdlekkrrea
       61 eallqsmglt tdspivpppm spssksvstp seagsqdsgd gavgsrtlhw dtdpsalqlh
      121 sdsdlgrgpi klgmakitqv dfppreivty tketqtpvta qpkedeeeed dvaapkppve
      181 peeekilkkd eendskapph elteeekqqi lhseeflsff dhstrivera lseqiniffd
      241 ysgrdledke geiqagakls lnrqffderw skhrvvscld wssqypellv asynnneeap
      301 hepdgvalvw nmkykkttpe yvfhcqsavm satfakfhpn lvvggtysgq ivlwdnrsnk
      361 rtpvqrtpls aaahthpvyc vnvvgtqnah nlisistdgk icswsldmls hpqdsmelvh
      421 kqskavavts msfpvgdvnn fvvgseegsv ytacrhgska gisemfeghq gpitgihcha
      481 avgavdfshl fvtssfdwtv klwttknnkp lysfednsdy vydvmwspth palfacvdgm
      541 grldlwnlnn dtevptasis vegnpalnrv rwthsgreia vgdsegqivi ydvgeqiavp
      601 rndewarfgr tlaeinasra daeeeaatri pa
//
LOCUS       NP_446120                585 aa            linear   ROD 27-APR-2025
DEFINITION  MAGUK p55 subfamily member 3 [Rattus norvegicus].
ACCESSION   NP_446120 XP_001081482 XP_340912
VERSION     NP_446120.1
DBSOURCE    REFSEQ: accession NM_053668.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Leonoudakis,D., Conti,L.R., Anderson,S., Radeke,C.M., McGuire,L.M.,
            Adams,M.E., Froehner,S.C., Yates,J.R. 3rd and Vandenberg,C.A.
  TITLE     Protein trafficking and anchoring complexes revealed by proteomic
            analysis of inward rectifier potassium channel (Kir2.x)-associated
            proteins
  JOURNAL   J Biol Chem 279 (21), 22331-22346 (2004)
   PUBMED   15024025
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Karnak,D., Lee,S. and Margolis,B.
  TITLE     Identification of multiple binding partners for the amino-terminal
            domain of synapse-associated protein 97
  JOURNAL   J Biol Chem 277 (48), 46730-46735 (2002)
   PUBMED   12351654
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Butz,S., Okamoto,M. and Sudhof,T.C.
  TITLE     A tripartite protein complex with the potential to couple synaptic
            vesicle exocytosis to cell adhesion in brain
  JOURNAL   Cell 94 (6), 773-782 (1998)
   PUBMED   9753324
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Feb 10, 2013 this sequence version replaced
            XP_340912.2, XP_001081482.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211573.1, SRR26643298.64264.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..585
                     /product="MAGUK p55 subfamily member 3"
                     /note="protein Dlgh3; discs large homolog 3; protein MPP3;
                     membrane palmitoylated protein 3; membrane protein,
                     palmitoylated 3 (MAGUK p55 subfamily member 3)"
                     /calculated_mol_wt=66458
     Region          11..62
                     /region_name="L27"
                     /note="L27 domain; pfam02828"
                     /db_xref="CDD:460717"
     Region          71..121
                     /region_name="L27"
                     /note="domain in receptor targeting proteins Lin-2 and
                     Lin-7; smart00569"
                     /db_xref="CDD:197794"
     Region          136..216
                     /region_name="PDZ_MPP3-MPP4-MPP7-like"
                     /note="PDZ domain of membrane palmitoylated proteins 3
                     (MPP3), MPP4, and MPP7, and related domains; cd06799"
                     /db_xref="CDD:467260"
     Site            order(146..152,163,166,196,200,203..204)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467260"
     Region          230..291
                     /region_name="SH3_MPP3"
                     /note="Src Homology 3 domain of Membrane Protein,
                     Palmitoylated 3 (or MAGUK p55 subfamily member 3);
                     cd12039"
                     /db_xref="CDD:212972"
     Site            order(232,256..257)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212972"
     Site            order(235,237,240,251,269..270,287,289..290)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212972"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88954.3)"
     Site            order(392,398,415,422,425,434,457,462)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:238026"
     Site            order(392,398)
                     /site_type="other"
                     /note="G-X2-G-X-G-K"
                     /db_xref="CDD:238026"
     Region          395..571
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Region          510..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88954.3)"
     CDS             1..585
                     /gene="Mpp3"
                     /gene_synonym="CSG18; Dlg3; Dusp3"
                     /coded_by="NM_053668.1:149..1906"
                     /db_xref="GeneID:114202"
                     /db_xref="RGD:620015"
ORIGIN      
        1 mpvlsedsgl hetlalltsq lrpdsnhree mgflrdvfse kslgylmkih eklryyerqs
       61 ptpvlhsama laedvmeelq aasvhsdere llqllstphl ravlmvhdtv aqknfdpvlp
      121 plpdnidedf eeesvkivrl vknkeplgat irrdehsgav vvarimrgga adrsglvhvg
      181 delrevngit vlhkrpdeis qilaqsqgsi tlkiipatqe edrfkeskvf mralfhydpr
      241 edraipcqea glpfqqrqvl evvsqddptw wqakrvgdtn lraglipskq fqerrlsyrr
      301 ttgtipspqn lrkplydqpc dketcdcdgy fkghyvaglr rsfrlgcrer ltgsqevkvp
      361 vgaesqvllt yeevaryqhq pgersrlvvl igslgahlhe lkqrvvaedp qhfgvavpht
      421 trprkshere gveyhfvskq afeadiqhnk flehgehken lygtsleaiq tvmaknkvcl
      481 vdvepealrh lrtpefkpyv ifvkpaiqek rktppvspds edpatpldeq qqemaasaaf
      541 idqhyghlid tvlvrqdlqs vcsqlravie slskdtywvp iswvr
//
LOCUS       NP_001257665             540 aa            linear   ROD 27-APR-2025
DEFINITION  testis-specific protein 10-interacting protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257665
VERSION     NP_001257665.1
DBSOURCE    REFSEQ: accession NM_001270736.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC097254.1.
            
            Transcript Variant: This variant (2) has an alternate in-frame exon
            and uses alternate in-frame splice junctions at the 5' ends of two
            other exons compared to variant 1. The resulting isoform (2)
            contains an alternate segment and lacks two other alternate
            segments compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1465873.1,
                                           SRR26643293.7206.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..540
                     /product="testis-specific protein 10-interacting protein
                     isoform 2"
                     /note="fibrous sheath protein; testis-specific protein
                     10-interacting protein; tsga10-interacting protein"
                     /calculated_mol_wt=60024
     CDS             1..540
                     /gene="Tsga10ip"
                     /coded_by="NM_001270736.1:39..1661"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361707"
                     /db_xref="RGD:1302964"
ORIGIN      
        1 mlntdqllvr aiserprkst eplvpgtptg lfsllsnisp eeqgrlgsgd slqsqscqqq
       61 rsysagqttk kerkprrrnk kgrgsaeaed lfssprkpsf pfqwawesfi idgqallqsg
      121 ssvavghrsl lfppaapqck trhksvanls edlrachkse vqnlgrryqp gawanlslpl
      181 gkaesqgler ptfwstgkgs gsecedvsev egqnadeaek slstgelpql pgqgltleee
      241 lisevmeeee hnrrkgssvn kgrnsgekgs eegelqshnq gsssnsnslr kspkgtsgak
      301 efkgpwdler lhrqlqeele sgpqkqtwka lraavqasar nrktpvtgee esfltanfpn
      361 rtfhkrqeat rhvsttaqvr ssedslrknl lqaweqqqlk ekqqaemrra reqqvqqqva
      421 rclaaytpgg nrgtlgpqrk leelrrkerq rfaeyqaelq giqhrvqarp flfqqamqvl
      481 salgvdeeql laeagnaegi prkhrsyrsf gvemesspqs ppkteptssq pgrhpsptld
//
LOCUS       NP_058936               1935 aa            linear   ROD 27-APR-2025
DEFINITION  myosin-7 [Rattus norvegicus].
ACCESSION   NP_058936
VERSION     NP_058936.1
DBSOURCE    REFSEQ: accession NM_017240.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1935)
  AUTHORS   Forini,F., Nicolini,G., Kusmic,C., D'Aurizio,R., Mercatanti,A.,
            Iervasi,G. and Pitto,L.
  TITLE     T3 Critically Affects the Mhrt/Brg1 Axis to Regulate the Cardiac
            MHC Switch: Role of an Epigenetic Cross-Talk
  JOURNAL   Cells 9 (10), 2155 (2020)
   PUBMED   32987653
  REMARK    GeneRIF: T3 Critically Affects the Mhrt/Brg1 Axis to Regulate the
            Cardiac MHC Switch: Role of an Epigenetic Cross-Talk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1935)
  AUTHORS   Guo,Z., Lu,J., Li,J., Wang,P., Li,Z., Zhong,Y., Guo,K., Wang,J.,
            Ye,J. and Liu,P.
  TITLE     JMJD3 inhibition protects against isoproterenol-induced cardiac
            hypertrophy by suppressing beta-MHC expression
  JOURNAL   Mol Cell Endocrinol 477, 1-14 (2018)
   PUBMED   29753027
  REMARK    GeneRIF: JMJD3 may be a key epigenetic regulator of beta-MHC
            expression in cardiomyocytes and a potential therapeutic target for
            cardiac hypertrophy.
REFERENCE   3  (residues 1 to 1935)
  AUTHORS   Tomita-Mitchell,A., Stamm,K.D., Mahnke,D.K., Kim,M.S.,
            Hidestrand,P.M., Liang,H.L., Goetsch,M.A., Hidestrand,M.,
            Simpson,P., Pelech,A.N., Tweddell,J.S., Benson,D.W., Lough,J.W. and
            Mitchell,M.E.
  TITLE     Impact of MYH6 variants in hypoplastic left heart syndrome
  JOURNAL   Physiol Genomics 48 (12), 912-921 (2016)
   PUBMED   27789736
REFERENCE   4  (residues 1 to 1935)
  AUTHORS   Ji,Y.X., Zhang,P., Zhang,X.J., Zhao,Y.C., Deng,K.Q., Jiang,X.,
            Wang,P.X., Huang,Z. and Li,H.
  TITLE     The ubiquitin E3 ligase TRAF6 exacerbates pathological cardiac
            hypertrophy via TAK1-dependent signalling
  JOURNAL   Nat Commun 7, 11267 (2016)
   PUBMED   27249171
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1935)
  AUTHORS   Zhang,Y., Si,Y. and Ma,N.
  TITLE     Meis1 promotes poly (rC)-binding protein 2 expression and inhibits
            angiotensin II-induced cardiomyocyte hypertrophy
  JOURNAL   IUBMB Life 68 (1), 13-22 (2016)
   PUBMED   26597775
REFERENCE   6  (residues 1 to 1935)
  AUTHORS   O'Neill,L., Holbrook,N.J., Fargnoli,J. and Lakatta,E.G.
  TITLE     Progressive changes from young adult age to senescence in mRNA for
            rat cardiac myosin heavy chain genes
  JOURNAL   Cardioscience 2 (1), 1-5 (1991)
   PUBMED   1888877
REFERENCE   7  (residues 1 to 1935)
  AUTHORS   Schuyler,G.T. and Yarbrough,L.R.
  TITLE     Changes in myosin and creatine kinase mRNA levels with cardiac
            hypertrophy and hypothyroidism
  JOURNAL   Basic Res Cardiol 85 (5), 481-494 (1990)
   PUBMED   1703406
REFERENCE   8  (residues 1 to 1935)
  AUTHORS   McNally,E.M., Kraft,R., Bravo-Zehnder,M., Taylor,D.A. and
            Leinwand,L.A.
  TITLE     Full-length rat alpha and beta cardiac myosin heavy chain
            sequences. Comparisons suggest a molecular basis for functional
            differences
  JOURNAL   J Mol Biol 210 (3), 665-671 (1989)
   PUBMED   2614840
REFERENCE   9  (residues 1 to 1935)
  AUTHORS   Kraft,R., Bravo-Zehnder,M., Taylor,D.A. and Leinwand,L.A.
  TITLE     Complete nucleotide sequence of full length cDNA for rat beta
            cardiac myosin heavy chain
  JOURNAL   Nucleic Acids Res 17 (18), 7529-7530 (1989)
   PUBMED   2798112
REFERENCE   10 (residues 1 to 1935)
  AUTHORS   Izumo,S., Lompre,A.M., Matsuoka,R., Koren,G., Schwartz,K.,
            Nadal-Ginard,B. and Mahdavi,V.
  TITLE     Myosin heavy chain messenger RNA and protein isoform transitions
            during cardiac hypertrophy. Interaction between hemodynamic and
            thyroid hormone-induced signals
  JOURNAL   J Clin Invest 79 (3), 970-977 (1987)
   PUBMED   2950137
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X15939.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X15939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1935
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p13"
     Protein         1..1935
                     /product="myosin-7"
                     /note="myosin heavy chain, cardiac muscle, fetal; beta
                     myosin heavy chain; myosin, heavy polypeptide 7, cardiac
                     muscle, beta; myosin heavy chain, polypeptide 7; myosin
                     heavy chain polypeptide 7 cardiac muscle fetal; myosin,
                     heavy chain 7, cardiac muscle, beta"
                     /calculated_mol_wt=222953
     Region          32..76
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Region          99..766
                     /region_name="MYSc_class_II"
                     /note="class II myosins, motor domain; cd01377"
                     /db_xref="CDD:276951"
     Site            order(126..134,178..185,233..243,461..466)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276951"
     Site            126..134
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276951"
     Site            129
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P02564.2)"
     Site            178..185
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276951"
     Site            233..243
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276951"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            461..466
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276951"
     Site            490..513
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276951"
     Region          655..677
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P02564.2)"
     Site            697..706
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276951"
     Site            order(709..725,755..766)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276951"
     Region          757..771
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P02564.2)"
     Region          846..1923
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Site            1137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02566; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1308
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Site            1513
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02563; propagated from
                     UniProtKB/Swiss-Prot (P02564.2)"
     Region          1915..1935
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02564.2)"
     CDS             1..1935
                     /gene="Myh7"
                     /gene_synonym="Bmyo; myHC-beta; myHC-slow; Myhcb"
                     /coded_by="NM_017240.2:9..5816"
                     /db_xref="GeneID:29557"
                     /db_xref="RGD:62030"
ORIGIN      
        1 madremaafg agapflrkse kerleaqtrp fdlkkdvfvp ddkeefvkak ivsreggkvt
       61 aetengktvt vkedqvmqqn ppkfdkiedm amltflhepa vlynlkerya swmiytysgl
      121 fcvtvnpykw lpvynaqvva ayrgkkrsea pphifsisdn ayqymltdre nqsilitges
      181 gagktvntkr viqyfaviaa igdrskkdqt pgkgtledqi iqanpaleaf gnaktvrndn
      241 ssrfgkfiri hfgatgklas adietyllek srvifqlkae rdyhifyqil snkkpelldm
      301 llitnnpydy affsqgettv asiddseehm atdsafdvlg ftpeeknsiy kltgaimhfg
      361 nmkfkqkqre eqaepdgtee adksaylmgl nsadllkglc hprvkvgney vtkgqnvqqv
      421 ayaigalaks vyekmfnwmv trinatletk qprqyfigvl diagfeifdf nsfeqlcinf
      481 tneklqqffn hhmfvleqee ykkegiewtf idfgmdlqac idliekpmgi msileeecmf
      541 pkatdmtfka klydnhlgks nnfqkprnik gkqeahfsli hyagtvdyni lgwlqknkdp
      601 lnetvvglyq ksslkllsnl fanyagadap vdkgkgkakk gssfqtvsal hrenlnklmt
      661 nlrsthphfv rciipnetks pgvmdnplvm hqlrcngvle giricrkgfp nrilygdfrq
      721 ryrilnpaai pegqfidsrk gaekllgsld idhnqykfgh tkvffkagll glleemrder
      781 lsriitriqa qsrgvlsrme fkkllerrds lliiqwnira fmgvknwpwm klyfkikpll
      841 ksaetekema nmkeefgrvk daleksearr keleekmvsl lqekndlqlq vqaeqdnlad
      901 aeercdqlik nkiqleakvk emterledee emnaeltakk rkledecsel krdiddlelt
      961 lakvekekha tenkvknlte emagldeiiv kltkekkalq eahqqalddl qaeedkvntl
     1021 tkakvkleqq vddlegsldq dkkvrmdler akrklegdlk ltqesimdle ndkqqlderl
     1081 kkkdfelnal nariedeqal gsqlqkklke lqarieelee eleaertara kveklrsdls
     1141 releeiserl eeaggatsvq iemnkkreae fqkmrrdlee atlqheataa alrkkhadsv
     1201 aelgeqidnl qrvkqkleke ksefkleldd vtsnmeqiik akanlekmcr tledqmnehr
     1261 skaeetqrsv ndltrqrakl qtengelsrq ldekealisq ltrgkltytq qledlkrqle
     1321 eevkaknala halqsarhdc dllreqyeee teakaelqrv lskansevaq wrtkyetdai
     1381 qrteeleeak kklaqrlqda eeaveavnak csslektkhr lqneiedlmv dversnaaaa
     1441 aldkkqrnfd kilvewkqky eesqseless qkearslste lfklknayee slehletfkr
     1501 enknlqeeis dlteqlgstg ksihelekir kqleaeklel qsaleeaeas leheegkilr
     1561 aqlefnqika eierklaekd eemeqakrnh lrvvdslqts ldaetrsrne alrvkkkmeg
     1621 dlnemeiqls hanrmaaeaq kqvkslqsll kdtqiqldda vranddlken iaiverrnnl
     1681 lqaeleelra vveqtersrk laeqeliets ervqllhsqn tslinqkkkm dadlsqlqte
     1741 veeavqecrn aeekakkait daammaeelk keqdtsahle rmknnmeqti kdlqhrldea
     1801 eqialkggkk qlqklearvr eleneleaeq krnaesvkgm rkserrikel tyqteedrkn
     1861 llrlqdlvdk lqlkvkaykr qaeeaeeqan tnlskfrkvq heldeaeera diaesqvnkl
     1921 raksrdigak glnee
//
LOCUS       NP_543182                229 aa            linear   ROD 27-APR-2025
DEFINITION  DNA damage-inducible transcript 4 protein [Rattus norvegicus].
ACCESSION   NP_543182
VERSION     NP_543182.1
DBSOURCE    REFSEQ: accession NM_080906.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Li,L., Xi,L., Wu,J., Zhao,Z., Chen,Y., Liu,W., Pan,Z., Liu,M.,
            Yang,D., Chen,Z. and Fang,Y.
  TITLE     The regulatory roles of DDIT4 in TDCIPP-induced autophagy and
            apoptosis in PC12 cells
  JOURNAL   J Environ Sci (China) 125, 823-830 (2023)
   PUBMED   36375964
  REMARK    GeneRIF: The regulatory roles of DDIT4 in TDCIPP-induced autophagy
            and apoptosis in PC12 cells.
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Guo,X., Wang,Y., Zheng,D., Cheng,X. and Sun,Y.
  TITLE     LncRNA-MIAT promotes neural cell autophagy and apoptosis in
            ischemic stroke by up-regulating REDD1
  JOURNAL   Brain Res 1763, 147436 (2021)
   PUBMED   33745924
  REMARK    GeneRIF: LncRNA-MIAT promotes neural cell autophagy and apoptosis
            in ischemic stroke by up-regulating REDD1.
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Martin-Flores,N., Perez-Sisques,L., Creus-Muncunill,J., Masana,M.,
            Gines,S., Alberch,J., Perez-Navarro,E. and Malagelada,C.
  TITLE     Synaptic RTP801 contributes to motor-learning dysfunction in
            Huntington's disease
  JOURNAL   Cell Death Dis 11 (7), 569 (2020)
   PUBMED   32732871
  REMARK    GeneRIF: Synaptic RTP801 contributes to motor-learning dysfunction
            in Huntington's disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Park,J.A. and Lee,C.H.
  TITLE     Time-Course Change of Redd1 Expressions in the Hippocampal CA1
            Region Following Chronic Cerebral Hypoperfusion
  JOURNAL   Cell Mol Neurobiol 37 (3), 563-569 (2017)
   PUBMED   27233899
  REMARK    GeneRIF: Redd1 expressions is markedly changed in the hippocampal
            CA1 region following chronic cerebral hypoperfusion.
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Chen,Q., Zhou,Y., Richards,A.M. and Wang,P.
  TITLE     Up-regulation of miRNA-221 inhibits hypoxia/reoxygenation-induced
            autophagy through the DDIT4/mTORC1 and Tp53inp1/p62 pathways
  JOURNAL   Biochem Biophys Res Commun 474 (1), 168-174 (2016)
   PUBMED   27105917
  REMARK    GeneRIF: In conclusion, miRNA-221 exerts cytoprotective effects in
            hypoxia-reoxygenation injury in association with alterations in
            autophagic cell injury. Mir-221 may constitute is a novel
            therapeutic target in the treatment of cardiac I/R injury.
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Wang,H., Kubica,N., Ellisen,L.W., Jefferson,L.S. and Kimball,S.R.
  TITLE     Dexamethasone represses signaling through the mammalian target of
            rapamycin in muscle cells by enhancing expression of REDD1
  JOURNAL   J Biol Chem 281 (51), 39128-39134 (2006)
   PUBMED   17074751
  REMARK    GeneRIF: REDD1 functions upstream of Tuberin and Rheb to
            down-regulate mTOR signaling in response to dexamethasone
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Malagelada,C., Ryu,E.J., Biswas,S.C., Jackson-Lewis,V. and
            Greene,L.A.
  TITLE     RTP801 is elevated in Parkinson brain substantia nigral neurons and
            mediates death in cellular models of Parkinson's disease by a
            mechanism involving mammalian target of rapamycin inactivation
  JOURNAL   J Neurosci 26 (39), 9996-10005 (2006)
   PUBMED   17005863
  REMARK    GeneRIF: In a PC12 model of Parkinson disease, RTP801
            overexpression is sufficient to promote death but does not further
            elevate death caused by 6-OHDA.
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Ellisen,L.W., Ramsayer,K.D., Johannessen,C.M., Yang,A., Beppu,H.,
            Minda,K., Oliner,J.D., McKeon,F. and Haber,D.A.
  TITLE     REDD1, a developmentally regulated transcriptional target of p63
            and p53, links p63 to regulation of reactive oxygen species
  JOURNAL   Mol Cell 10 (5), 995-1005 (2002)
   PUBMED   12453409
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Jiang,Y., Wu,J., Keep,R.F., Hua,Y., Hoff,J.T. and Xi,G.
  TITLE     Hypoxia-inducible factor-1alpha accumulation in the brain after
            experimental intracerebral hemorrhage
  JOURNAL   J Cereb Blood Flow Metab 22 (6), 689-696 (2002)
   PUBMED   12045667
  REMARK    GeneRIF: Thrombin and erythrocyte lysate are involved in HIF-1alpha
            upregulation through reducing HIF-1alpha degradation.
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Shoshani,T., Faerman,A., Mett,I., Zelin,E., Tenne,T., Gorodin,S.,
            Moshel,Y., Elbaz,S., Budanov,A., Chajut,A., Kalinski,H., Kamer,I.,
            Rozen,A., Mor,O., Keshet,E., Leshkowitz,D., Einat,P., Skaliter,R.
            and Feinstein,E.
  TITLE     Identification of a novel hypoxia-inducible factor 1-responsive
            gene, RTP801, involved in apoptosis
  JOURNAL   Mol Cell Biol 22 (7), 2283-2293 (2002)
   PUBMED   11884613
  REMARK    GeneRIF: Identification of a novel hypoxia-inducible factor
            1-responsive gene, RTP801, involved in apoptosis
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF334162.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF334162.1, BC062021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..229
                     /product="DNA damage-inducible transcript 4 protein"
                     /note="REDD-1; HIF-1 responsive protein RTP801; protein
                     regulated in development and DNA damage response 1; HIF-1
                     responsive RTP801"
                     /calculated_mol_wt=24754
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VHZ9.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NX09; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ9.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NX09; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ9.1)"
     Region          101..220
                     /region_name="RTP801_C"
                     /note="RTP801 C-terminal region; pfam07809"
                     /db_xref="CDD:462274"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NX09; propagated from
                     UniProtKB/Swiss-Prot (Q8VHZ9.1)"
     CDS             1..229
                     /gene="Ddit4"
                     /gene_synonym="Rtp801"
                     /coded_by="NM_080906.2:183..872"
                     /db_xref="GeneID:140942"
                     /db_xref="RGD:621731"
ORIGIN      
        1 mpslwdrfss ssssssssrt paadrpprsa wgsaareegl drcaslessd cesldssnsg
       61 fgpeedssyl dgvslpdfel lsdpedehlc anlmqllqes lsqarlgsrr parllmpsql
      121 lsqvgkellr laysepcglr galldvcveq gkschsvaql aldpslvptf qltlvlrlds
      181 rlwpkiqgll ssansslvpg ysqsltlstg frvikkklys seqllieec
//
LOCUS       NP_001180498             417 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase Sgk1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001180498
VERSION     NP_001180498.1
DBSOURCE    REFSEQ: accession NM_001193569.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Li,Y.H., Sun,C.C., Chen,P.M. and Chen,H.H.
  TITLE     SGK1 Target Genes Involved in Heart and Blood Vessel Functions in
            PC12 Cells
  JOURNAL   Cells 12 (12), 1641 (2023)
   PUBMED   37371111
  REMARK    GeneRIF: SGK1 Target Genes Involved in Heart and Blood Vessel
            Functions in PC12 Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Zou,Z., Zhao,T., Zeng,Z. and An,Y.
  TITLE     Serum and glucocorticoid inducible kinase 1 modulates mitochondrial
            dysfunction and oxidative stress in doxorubicin-induced
            cardiomyocytes by regulating Hippo pathway via Neural precursor
            cell-expressed developmentally down-regulated 4 type 2
  JOURNAL   Hum Exp Toxicol 42, 9603271231158039 (2023)
   PUBMED   36781297
  REMARK    GeneRIF: Serum and glucocorticoid inducible kinase 1 modulates
            mitochondrial dysfunction and oxidative stress in
            doxorubicin-induced cardiomyocytes by regulating Hippo pathway via
            Neural precursor cell-expressed developmentally down-regulated 4
            type 2.
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Wang,F. and Han,L.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1 (SGK1)
            ameliorates doxorubicin-induced cardiotoxic injury, apoptosis,
            inflammation and oxidative stress by suppressing glucose regulated
            protein 78 (GRP78)-mediated endoplasmic reticulum stress
  JOURNAL   Bioengineered 13 (1), 844-855 (2022)
   PUBMED   34898378
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 (SGK1) ameliorates doxorubicin-induced cardiotoxic injury,
            apoptosis, inflammation and oxidative stress by suppressing glucose
            regulated protein 78 (GRP78)-mediated endoplasmic reticulum stress.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Liu,B.W., Zhang,J., Hong,Y.S., Li,N.B., Liu,Y., Zhang,M., Wu,W.Y.,
            Zheng,H., Lampert,A. and Zhang,X.W.
  TITLE     NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation
  JOURNAL   Mol Neurobiol 58 (3), 964-982 (2021)
   PUBMED   33063281
  REMARK    GeneRIF: NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Lee,R.H., Grames,M.S., Wu,C.Y., Lien,C.F., Couto E Silva,A.,
            Possoit,H.E., Clemons,G.A., Citadin,C.T., Neumann,J.T., Pastore,D.,
            Lauro,D., Della-Morte,D. and Lin,H.W.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1
            exacerbates brain injury and neurological deficits after cardiac
            arrest
  JOURNAL   Am J Physiol Heart Circ Physiol 319 (5), H1044-H1050 (2020)
   PUBMED   32946263
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 exacerbates brain injury and neurological deficits after cardiac
            arrest.
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Maiyar,A.C., Phu,P.T., Huang,A.J. and Firestone,G.L.
  TITLE     Repression of glucocorticoid receptor transactivation and DNA
            binding of a glucocorticoid response element within the
            serum/glucocorticoid-inducible protein kinase (sgk) gene promoter
            by the p53 tumor suppressor protein
  JOURNAL   Mol Endocrinol 11 (3), 312-329 (1997)
   PUBMED   9058378
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Maiyar,A.C., Huang,A.J., Phu,P.T., Cha,H.H. and Firestone,G.L.
  TITLE     p53 stimulates promoter activity of the sgk.
            serum/glucocorticoid-inducible serine/threonine protein kinase gene
            in rodent mammary epithelial cells
  JOURNAL   J Biol Chem 271 (21), 12414-12422 (1996)
   PUBMED   8647846
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Richards,J.S., Fitzpatrick,S.L., Clemens,J.W., Morris,J.K.,
            Alliston,T. and Sirois,J.
  TITLE     Ovarian cell differentiation: a cascade of multiple hormones,
            cellular signals, and regulated genes
  JOURNAL   Recent Prog Horm Res 50, 223-254 (1995)
   PUBMED   7740159
  REMARK    Review article
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Imaizumi,K., Tsuda,M., Wanaka,A., Tohyama,M. and Takagi,T.
  TITLE     Differential expression of sgk mRNA, a member of the Ser/Thr
            protein kinase gene family, in rat brain after CNS injury
  JOURNAL   Brain Res Mol Brain Res 26 (1-2), 189-196 (1994)
   PUBMED   7854047
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Webster,M.K., Goya,L., Ge,Y., Maiyar,A.C. and Firestone,G.L.
  TITLE     Characterization of sgk, a novel member of the serine/threonine
            protein kinase gene family which is transcriptionally induced by
            glucocorticoids and serum
  JOURNAL   Mol Cell Biol 13 (4), 2031-2040 (1993)
   PUBMED   8455596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB814192.1 and BC078843.1.
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter, 5' UTR, and 5' coding region, compared to variant 1. The
            resulting isoform (2) has a shorter and distinct N-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132263
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..417
                     /product="serine/threonine-protein kinase Sgk1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase Sgk1;
                     serine/threonine protein kinase SGK"
                     /calculated_mol_wt=47496
     Region          76..414
                     /region_name="STKc_SGK1"
                     /note="Catalytic domain of the Protein Serine/Threonine
                     Kinase, Serum- and Glucocorticoid-induced Kinase 1;
                     cd05602"
                     /db_xref="CDD:270753"
     Site            order(90..91,93..96,98,111,113,146,163,165,169,171,208,
                     210,212..213,215,225..226,229,243..248,275,281,284)
                     /site_type="active"
                     /db_xref="CDD:270753"
     Site            order(90..91,93..96,98,111,113,146,163,165,210,212..213,
                     215,225)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270753"
     Site            order(94,169,171,208,210,212,229,243..248,275,281,284)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270753"
     Site            225..248
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270753"
     Site            383
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270753"
     Site            404..409
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270753"
     CDS             1..417
                     /gene="Sgk1"
                     /gene_synonym="Sgk"
                     /coded_by="NM_001193569.1:129..1382"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29517"
                     /db_xref="RGD:3668"
ORIGIN      
        1 mreealrspw kafmkqrrmg lndfiqklan nsyackhpev qsylkisqpq epelmnanps
       61 pppspsqqin lgpssnphak psdfhflkvi gkgsfgkvll arhkaeeafy avkvlqkkai
      121 lkkkeekhim sernvllknv khpflvglhf sfqtadklyf vldyinggel fyhlqrercf
      181 leprarfyaa eiasalgylh slnivyrdlk penilldsqg hivltdfglc keniehngtt
      241 stfcgtpeyl apevlhkqpy drtvdwwclg avlyemlygl ppfysrntae mydnilnkpl
      301 qlkpnitnsa rhllegllqk drtkrlgakd dfmeikshif fslinwddli nkkitppfnp
      361 nvsgpsdlrh fdpefteepv pssigrspds ilvtasvkea aeaflgfsya ppmdsfl
//
LOCUS       NP_036972                105 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome c, testis-specific [Rattus norvegicus].
ACCESSION   NP_036972
VERSION     NP_036972.1
DBSOURCE    REFSEQ: accession NM_012840.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Liu,Z., Lin,H., Ye,S., Liu,Q.Y., Meng,Z., Zhang,C.M., Xia,Y.,
            Margoliash,E., Rao,Z. and Liu,X.J.
  TITLE     Remarkably high activities of testicular cytochrome c in destroying
            reactive oxygen species and in triggering apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 103 (24), 8965-8970 (2006)
   PUBMED   16757556
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Matsuki,S., Iuchi,Y., Ikeda,Y., Sasagawa,I., Tomita,Y. and Fujii,J.
  TITLE     Suppression of cytochrome c release and apoptosis in testes with
            heat stress by minocycline
  JOURNAL   Biochem Biophys Res Commun 312 (3), 843-849 (2003)
   PUBMED   14680842
  REMARK    GeneRIF: These findings suggest that heat stress of testes triggers
            the release of cytochrome c from mitochondria in spermatogenic
            cells, leading to the activation of an apoptotic pathway.
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Virbasius,J.V. and Scarpulla,R.C.
  TITLE     Structure and expression of rodent genes encoding the
            testis-specific cytochrome c. Differences in gene structure and
            evolution between somatic and testicular variants
  JOURNAL   J Biol Chem 263 (14), 6791-6796 (1988)
   PUBMED   2834389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1 and M20623.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.17265.1,
                                           SRR26360181.642152.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            regulatory uORF                    :: PMID: 2834389
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..105
                     /product="cytochrome c, testis-specific"
                     /note="Cytochrome C testis specific"
                     /calculated_mol_wt=11611
     Region          2..101
                     /region_name="Cyc7"
                     /note="Cytochrome c2 [Energy production and conversion];
                     COG3474"
                     /db_xref="CDD:442697"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000250|UniProtKB:P00015; propagated from
                     UniProtKB/Swiss-Prot (P10715.2)"
     CDS             1..105
                     /gene="Cyct"
                     /gene_synonym="CYCTA"
                     /coded_by="NM_012840.3:232..549"
                     /db_xref="GeneID:25310"
                     /db_xref="RGD:2452"
ORIGIN      
        1 mgdaeagkki fiqkcaqcht vekggkhktg pnlwglfgrk tgqapgfsyt danknkgviw
       61 teetlmeyle npkkyipgtk mifagikkks eredliqylk eatss
//
LOCUS       NP_001029370             246 aa            linear   ROD 27-APR-2025
DEFINITION  transmembrane protein 33 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001029370
VERSION     NP_001029370.1
DBSOURCE    REFSEQ: accession NM_001034198.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Sakabe,I., Hu,R., Jin,L., Clarke,R. and Kasid,U.N.
  TITLE     TMEM33: a new stress-inducible endoplasmic reticulum transmembrane
            protein and modulator of the unfolded protein response signaling
  JOURNAL   Breast Cancer Res Treat 153 (2), 285-297 (2015)
   PUBMED   26268696
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Urade,T., Yamamoto,Y., Zhang,X., Ku,Y. and Sakisaka,T.
  TITLE     Identification and characterization of TMEM33 as a
            reticulon-binding protein
  JOURNAL   Kobe J Med Sci 60 (3), E57-E65 (2014)
   PUBMED   25612671
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Chi,A., Valencia,J.C., Hu,Z.Z., Watabe,H., Yamaguchi,H.,
            Mangini,N.J., Huang,H., Canfield,V.A., Cheng,K.C., Yang,F., Abe,R.,
            Yamagishi,S., Shabanowitz,J., Hearing,V.J., Wu,C., Appella,E. and
            Hunt,D.F.
  TITLE     Proteomic and bioinformatic characterization of the biogenesis and
            function of melanosomes
  JOURNAL   J Proteome Res 5 (11), 3135-3144 (2006)
   PUBMED   17081065
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Nakadai,T., Kishimoto,T., Kokura,K., Ohkawa,N., Makino,Y.,
            Muramatsu,M. and Tamura,T.
  TITLE     Cloning of a novel rat gene, DB83, that encodes a putative membrane
            protein
  JOURNAL   DNA Res 5 (5), 315-317 (1998)
   PUBMED   9872456
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region that results in a frameshift compared to
            variant 1. The resulting protein (isoform 2) is shorter and has a
            distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2543449.1,
                                           SRR26360176.1484998.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..246
                     /product="transmembrane protein 33 isoform 2"
                     /note="db83"
                     /calculated_mol_wt=27753
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P57088; propagated from
                     UniProtKB/Swiss-Prot (Q9Z142.1)"
     Region          9..245
                     /region_name="TMEM33_Pom33"
                     /note="Transmembrane protein 33/Nucleoporin POM33;
                     pfam03661"
                     /db_xref="CDD:461009"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z142.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z142.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z142.1)"
     CDS             1..246
                     /gene="Tmem33"
                     /coded_by="NM_001034198.2:165..905"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:59303"
                     /db_xref="RGD:708371"
ORIGIN      
        1 madttpngpq gagavqfmmt nkldtamwls rlftvycsal fvlpllglhe aasfyqrall
       61 analtsalrl hqrlphfqls raflaqalle dschyllysl ifvnsypvtm sifpvllfsl
      121 lhaatytkkv ldakgsnslp llrsvldkls tnqqnilkfi acneiflmpa tvfmlfsgqg
      181 sllqpfiyyr fltlryssrr npycrnlfne lrivvehiim kpscplfvrr lclqsiafis
      241 rlapta
//
LOCUS       NP_001257786             188 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform d [Rattus norvegicus].
ACCESSION   NP_001257786
VERSION     NP_001257786.1
DBSOURCE    REFSEQ: accession NM_001270857.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC092646.1.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon and uses an alternate in-frame splice junction at the 5' end
            of the next exon compared to variant 1. The resulting isoform (d)
            has the same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399492.2258889.1,
                                           SRR22399481.222842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..188
                     /product="stathmin-4 isoform d"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=21885
     Region          48..182
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P63043.1)"
     Region          167..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63043.1)"
     CDS             1..188
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_001270857.1:180..746"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyedtvd lnwcvisdme vielnkctsg
       61 qsfevilkpp sfdgvpefna slprrrdpsl eeiqkkleaa eerrkyqeae llkhlaekre
      121 hereviqkai eennnfikma keklaqkmes nkenreahla amlerlqekd khaeevrknk
      181 elkeeasr
//
LOCUS       NP_001101529             427 aa            linear   ROD 27-APR-2025
DEFINITION  ETS domain-containing protein Elk-1 [Rattus norvegicus].
ACCESSION   NP_001101529 XP_001055949 XP_001078496
VERSION     NP_001101529.1
DBSOURCE    REFSEQ: accession NM_001108059.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Wei,S., Ling,D., Zhong,J., Chang,R., Ling,X., Chen,Z. and Duan,R.
  TITLE     Elk1 enhances inflammatory cell infiltration and exacerbates acute
            lung injury/acute respiratory distress syndrome by suppressing
            Fcgr2b transcription
  JOURNAL   Mol Med 30 (1), 53 (2024)
   PUBMED   38649840
  REMARK    GeneRIF: Elk1 enhances inflammatory cell infiltration and
            exacerbates acute lung injury/acute respiratory distress syndrome
            by suppressing Fcgr2b transcription.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Lu,Z., Miao,Z., Zhu,J. and Zhu,G.
  TITLE     ETS-domain containing protein (Elk1) suppression protects cortical
            neurons against oxygen-glucose deprivation injury
  JOURNAL   Exp Cell Res 371 (1), 42-49 (2018)
   PUBMED   30053446
  REMARK    GeneRIF: Elk1 suppression protects cortical neurons against
            oxygen-glucose deprivation injury.
            Erratum:[Exp Cell Res. 2018 Nov 1;372(1):83. doi:
            10.1016/j.yexcr.2018.09.007. PMID: 30266209]
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Sobrier,M.L., Tsai,Y.C., Perez,C., Leheup,B., Bouceba,T.,
            Duquesnoy,P., Copin,B., Sizova,D., Penzo,A., Stanger,B.Z.,
            Cooke,N.E., Liebhaber,S.A. and Amselem,S.
  TITLE     Functional characterization of a human POU1F1 mutation associated
            with isolated growth hormone deficiency: a novel etiology for IGHD
  JOURNAL   Hum Mol Genet 25 (3), 472-483 (2016)
   PUBMED   26612202
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Mahajan,M.A. and Stanley,F.M.
  TITLE     Insulin-activated Elk-1 recruits the TIP60/NuA4 complex to increase
            prolactin gene transcription
  JOURNAL   Mol Cell Endocrinol 382 (1), 159-169 (2014)
   PUBMED   24075908
  REMARK    GeneRIF: insulin activates prolactin gene transcription by
            activating Elk-1 that recruits the NuA4 complex to the promoter.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Rahim,G., Araud,T., Jaquier-Gubler,P. and Curran,J.
  TITLE     Alternative splicing within the elk-1 5' untranslated region serves
            to modulate initiation events downstream of the highly conserved
            upstream open reading frame 2
  JOURNAL   Mol Cell Biol 32 (9), 1745-1756 (2012)
   PUBMED   22354998
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Sharrocks,A.D.
  TITLE     Complexities in ETS-domain transcription factor function and
            regulation: lessons from the TCF (ternary complex factor)
            subfamily. The Colworth Medal Lecture
  JOURNAL   Biochem Soc Trans 30 (2), 1-9 (2002)
   PUBMED   12023815
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Vanhoutte,P., Nissen,J.L., Brugg,B., Gaspera,B.D., Besson,M.J.,
            Hipskind,R.A. and Caboche,J.
  TITLE     Opposing roles of Elk-1 and its brain-specific isoform, short
            Elk-1, in nerve growth factor-induced PC12 differentiation
  JOURNAL   J Biol Chem 276 (7), 5189-5196 (2001)
   PUBMED   11050086
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Kyosseva,S.V., Elbein,A.D., Hutton,T.L., Griffin,S.T., Mrak,R.E.,
            Sturner,W.Q. and Karson,C.N.
  TITLE     Increased levels of transcription factors Elk-1, cyclic adenosine
            monophosphate response element-binding protein, and activating
            transcription factor 2 in the cerebellar vermis of schizophrenic
            patients
  JOURNAL   Arch Gen Psychiatry 57 (7), 685-691 (2000)
   PUBMED   10891039
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Kaminska,B., Kaczmarek,L., Zangenehpour,S. and Chaudhuri,A.
  TITLE     Rapid phosphorylation of Elk-1 transcription factor and activation
            of MAP kinase signal transduction pathways in response to visual
            stimulation
  JOURNAL   Mol Cell Neurosci 13 (6), 405-414 (1999)
   PUBMED   10383826
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Sgambato,V., Vanhoutte,P., Pages,C., Rogard,M., Hipskind,R.,
            Besson,M.J. and Caboche,J.
  TITLE     In vivo expression and regulation of Elk-1, a target of the
            extracellular-regulated kinase signaling pathway, in the adult rat
            brain
  JOURNAL   J Neurosci 18 (1), 214-226 (1998)
   PUBMED   9412502
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FM043339.1 and
            JAXUCZ010000021.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001078496.1, XP_001055949.1.
            
            Summary: This gene is a member of the Ets family of transcription
            factors and of the ternary complex factor (TCF) subfamily. Proteins
            of the TCF subfamily form a ternary complex by binding to the the
            serum response factor and the serum response element in the
            promoter of the c-fos proto-oncogene. The protein encoded by this
            gene is a nuclear target for the ras-raf-MAPK signaling cascade.
            Multiple isoforms are produced from this gene by the use of
            alternative translational start codons. [provided by RefSeq, Mar
            2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1163361.1,
                                           SRR21887622.2108921.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            regulatory uORF        :: PMID: 22354998
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..427
                     /product="ETS domain-containing protein Elk-1"
                     /note="ELK1, member of ETS oncogene family; ELK1, ETS
                     transcription factor"
                     /calculated_mol_wt=45141
     Region          4..89
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     Region          55
                     /region_name="alternative start codon, AUG sELK-1; start
                     of brain-specific isoform sELK-1; PMID:11050086"
     Region          <100..427
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          112..>246
                     /region_name="PHA03132"
                     /note="thymidine kinase; Provisional"
                     /db_xref="CDD:222997"
     Region          116..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GTP4.1)"
     Region          166..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GTP4.1)"
     Region          226..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GTP4.1)"
     Region          300..350
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Region          348..398
                     /region_name="Sufficient for interaction with MAD2L2.
                     /evidence=ECO:0000250|UniProtKB:P19419"
                     /note="propagated from UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            380
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1 and MAPK8.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:P19419; propagated from
                     UniProtKB/Swiss-Prot (A4GTP4.1)"
     CDS             1..427
                     /gene="Elk1"
                     /coded_by="NM_001108059.3:203..1486"
                     /db_xref="GeneID:314436"
                     /db_xref="RGD:1598663"
ORIGIN      
        1 mdpsvtlwqf llqllreqgn ghiiswtsrd ggefklvdae evarlwglrk nktnmnydkl
       61 sralryyydk niirkvsgqk fvykfvsype vagcstedcp pqpevsvtsa vamapatvhs
      121 gpgdnatgkp gtpkgagmtg qgglarssrn eymrsglyst ftiqslqpqp plhprpasvl
      181 pnttpagvpa ppsgsrstsp npleacleae eaglplqvil tppeapnqks eelslnpgfg
      241 rpqppevkve gpkeelevte vggfspeavk aeqevspseg llarlpailt entaqvcgls
      301 tstteitqpq kgrkprdlel plspsllggq gpertpgsgt ssglqaqgpa ltpsllptht
      361 ltpvlltpss lppsihfwst lspiaprspa klsfqfpssg saqvhipsis vdglstpvvl
      421 spgpqkp
//
LOCUS       NP_058829                961 aa            linear   ROD 27-APR-2025
DEFINITION  thrombospondin-4 precursor [Rattus norvegicus].
ACCESSION   NP_058829 XP_001066338 XP_003753555 XP_342173
VERSION     NP_058829.1
DBSOURCE    REFSEQ: accession NM_017133.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Zeng,H., Lan,B., Li,B., Xie,H., Zhao,E., Liu,X., Xue,X., Sun,J.,
            Su,L. and Zhang,Y.
  TITLE     The role and mechanism of thrombospondin-4 in pulmonary arterial
            hypertension associated with congenital heart disease
  JOURNAL   Respir Res 25 (1), 313 (2024)
   PUBMED   39154161
  REMARK    GeneRIF: The role and mechanism of thrombospondin-4 in pulmonary
            arterial hypertension associated with congenital heart disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Meng,X.M., Pang,Q.Y., Zhou,Z.F., Yuan,J.H., You,L., Feng,Q.P. and
            Zhu,B.M.
  TITLE     Histone methyltransferase MLL4 protects against pressure
            overload-induced heart failure via a THBS4-mediated protection in
            ER stress
  JOURNAL   Pharmacol Res 205, 107263 (2024)
   PUBMED   38876442
  REMARK    GeneRIF: Histone methyltransferase MLL4 protects against pressure
            overload-induced heart failure via a THBS4-mediated protection in
            ER stress.
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Guo,Y., Zhang,Z., Wu,H.E., Luo,Z.D., Hogan,Q.H. and Pan,B.
  TITLE     Increased thrombospondin-4 after nerve injury mediates disruption
            of intracellular calcium signaling in primary sensory neurons
  JOURNAL   Neuropharmacology 117, 292-304 (2017)
   PUBMED   28232180
  REMARK    GeneRIF: Results show that TSP4 regulates Ca2+ homeostasis in
            primary sensory neurons by affecting Ca2+ influx and buffering,
            including SERCA and PMCA, via PKC signaling after binding to
            Cavalpha2delta1. Elevated TSP4 expression may be a key factor that
            disrupts Ca2+ homeostasis after neuronal injury, and may serve as a
            valuable target for treatment of neuropathic pain.
REFERENCE   4  (residues 1 to 961)
  AUTHORS   Yang,H.J., Ma,S.P., Ju,F., Zhang,Y.P., Li,Z.C., Zhang,B.B.,
            Lian,J.J., Wang,L., Cheng,B.F., Wang,M. and Feng,Z.W.
  TITLE     Thrombospondin-4 Promotes Neuronal Differentiation of NG2 Cells via
            the ERK/MAPK Pathway
  JOURNAL   J Mol Neurosci 60 (4), 517-524 (2016)
   PUBMED   27647309
  REMARK    GeneRIF: TSP4 promoted neuronal differentiation of NG2 cells by
            inhibiting ERK/MAPK signaling.
REFERENCE   5  (residues 1 to 961)
  AUTHORS   Krawczyk,K.K., Ekman,M., Rippe,C., Grossi,M., Nilsson,B.O.,
            Albinsson,S., Uvelius,B. and Sward,K.
  TITLE     Assessing the contribution of thrombospondin-4 induction and
            ATF6alpha activation to endoplasmic reticulum expansion and
            phenotypic modulation in bladder outlet obstruction
  JOURNAL   Sci Rep 6, 32449 (2016)
   PUBMED   27581066
  REMARK    GeneRIF: The findings demonstrate reciprocal regulation of the
            unfolded protein response, including ATF6alpha activation and
            endoplasmic reticulum expansion, and reduced contractile
            differentiation in bladder outlet obstruction occurring
            independently of thrombospondin-4, which however is a sensitive
            indicator of obstruction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 961)
  AUTHORS   Stenina,O.I., Desai,S.Y., Krukovets,I., Kight,K., Janigro,D.,
            Topol,E.J. and Plow,E.F.
  TITLE     Thrombospondin-4 and its variants: expression and differential
            effects on endothelial cells
  JOURNAL   Circulation 108 (12), 1514-1519 (2003)
   PUBMED   12952849
REFERENCE   7  (residues 1 to 961)
  AUTHORS   Narouz-Ott,L., Maurer,P., Nitsche,D.P., Smyth,N. and Paulsson,M.
  TITLE     Thrombospondin-4 binds specifically to both collagenous and
            non-collagenous extracellular matrix proteins via its C-terminal
            domains
  JOURNAL   J Biol Chem 275 (47), 37110-37117 (2000)
   PUBMED   10956668
REFERENCE   8  (residues 1 to 961)
  AUTHORS   Arber,S. and Caroni,P.
  TITLE     Thrombospondin-4, an extracellular matrix protein expressed in the
            developing and adult nervous system promotes neurite outgrowth
  JOURNAL   J Cell Biol 131 (4), 1083-1094 (1995)
   PUBMED   7490284
REFERENCE   9  (residues 1 to 961)
  AUTHORS   Lawler,J., McHenry,K., Duquette,M. and Derick,L.
  TITLE     Characterization of human thrombospondin-4
  JOURNAL   J Biol Chem 270 (6), 2809-2814 (1995)
   PUBMED   7852353
REFERENCE   10 (residues 1 to 961)
  AUTHORS   Adams,J.C. and Lawler,J.
  TITLE     Cell-type specific adhesive interactions of skeletal myoblasts with
            thrombospondin-1
  JOURNAL   Mol Biol Cell 5 (4), 423-437 (1994)
   PUBMED   7519904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_001066338.3, XP_003753555.1, XP_342173.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.5055.1,
                                           SRR26643299.8155.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676784 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..961
                     /product="thrombospondin-4 precursor"
                     /calculated_mol_wt=103423
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2644
     Region          24..192
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Region          219..262
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:293926"
     Region          219..262
                     /region_name="TSP-4cc"
                     /note="Coiled coil region of thrombospondin-4 (TSP-4);
                     cd16080"
                     /db_xref="CDD:293926"
     Site            order(219..224,226..231,234,236..238,240..242,244..245,
                     247..252,254..256,258..261)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293926"
     Site            order(230,241,244)
                     /site_type="other"
                     /note="chemical substrate binding site [chemical binding]"
                     /db_xref="CDD:293926"
     Region          290..320
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          326..360
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(326,329,343)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          379..413
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(379,382,396)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          <464..695
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          496..531
                     /region_name="TSP_3"
                     /note="Thrombospondin type 3 repeat; pfam02412"
                     /db_xref="CDD:367074"
     Region          496..531
                     /region_name="TSP3 repeat_long"
                     /note="TSP3 repeat_long [structural motif]"
                     /db_xref="CDD:275366"
     Region          532..554
                     /region_name="TSP3 repeat_short"
                     /note="TSP3 repeat_short [structural motif]"
                     /db_xref="CDD:275366"
     Region          555..590
                     /region_name="TSP3 repeat_long"
                     /note="TSP3 repeat_long [structural motif]"
                     /db_xref="CDD:275365"
     Region          591..613
                     /region_name="TSP3 repeat_short"
                     /note="TSP3 repeat_short [structural motif]"
                     /db_xref="CDD:275365"
     Region          614..651
                     /region_name="TSP3 repeat_long"
                     /note="TSP3 repeat_long [structural motif]"
                     /db_xref="CDD:275365"
     Region          615..651
                     /region_name="TSP_3"
                     /note="Thrombospondin type 3 repeat; pfam02412"
                     /db_xref="CDD:367074"
     Region          652..691
                     /region_name="TSP3 repeat_short"
                     /note="TSP3 repeat_short [structural motif]"
                     /db_xref="CDD:275366"
     Region          692..726
                     /region_name="TSP_3"
                     /note="Thrombospondin type 3 repeat; pfam02412"
                     /db_xref="CDD:367074"
     Region          692..723
                     /region_name="TSP3 repeat_long"
                     /note="TSP3 repeat_long [structural motif]"
                     /db_xref="CDD:275365"
     Region          745..942
                     /region_name="TSP_C"
                     /note="Thrombospondin C-terminal region; pfam05735"
                     /db_xref="CDD:461725"
     CDS             1..961
                     /gene="Thbs4"
                     /coded_by="NM_017133.1:175..3060"
                     /db_xref="GeneID:29220"
                     /db_xref="RGD:62046"
ORIGIN      
        1 mlapraaafl llhlvlqpwq ragaqatpqv fdllpsssqr lnpaalqpvl tdptlhelyv
       61 istfklqsks satifglyss sdnskyfeft vmgrlnkail rylkddgkih lvvfnnlqla
      121 dgrrhrillr lsnlqrgags velyldcvqv dsvnnlpraf sgltqnpqai elrtfqrkpq
      181 dfleelklvv rgslfqvasl qdcflqqsep laatgtgdfn rqflgqmtql nqllgevkdl
      241 lrqqvketsf lrntiaecqa cgplsfqspt pntlvpiapp apptrptrrc dsspcfrgvr
      301 ctdtrdgfqc gpcpdgytgn gitcsdvdec kyhpcypgvr ctnlapgfrc dacpvgftgp
      361 mvqgvginfa ktnkqvctdv decrngacvl nsicintlgs yrcgpckpgy tgdqtrgcrt
      421 erscrnpeqn pcsvhaqcie erqgdvtcvc gvgwagdgyv cgkdvdidsy pdeelpcsar
      481 nckkdnckyv pnsgqedadr dgigdacded adgdgilneq dncvlthnvd qrntdkdifg
      541 dacdncrgvl nndqkdtdgd gkgdacdddm dgdgiknild ncprvpnrdq qdrdgdgvgd
      601 acdscpdvsn pnqsdvdndl vgdscdtnqd sdgdghqdst dncptvinsa qldtdkdgig
      661 decdddddnd gipdlvppgp dncrlvpnpa qedsnndgvg diceadfdqd kvidridvcp
      721 enaeitltdf rayqtvvldp egdaqidpnw vvlnqgmeiv qtmnsdpgla vgytafngvd
      781 fegtfhvntq tdddyagfif gyqdsssfyv vmwkqteqty wqatpfrava epgiqlkavk
      841 sktgpgehlr nslwhtgdts dqvrllwkds rnvgwkdkvs yrwflqhrpq vgyirvrfye
      901 gselvadsgv tidttmrggr lgvfcfsqen iiwsnlkyrc ndtipedfqe fqiqtfdrld
      961 n
//
LOCUS       NP_001296975             321 aa            linear   ROD 27-APR-2025
DEFINITION  U5 small nuclear ribonucleoprotein TSSC4 [Rattus norvegicus].
ACCESSION   NP_001296975 XP_006230882
VERSION     NP_001296975.1
DBSOURCE    REFSEQ: accession NM_001310046.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 23, 2015 this sequence version replaced XP_006230882.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DN937524.1, SRR26360172.1767196.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..321
                     /product="U5 small nuclear ribonucleoprotein TSSC4"
                     /note="protein TSSC4; tumor-suppressing subchromosomal
                     transferable fragment 4"
                     /calculated_mol_wt=34196
     Region          95..211
                     /region_name="TSSC4"
                     /note="Tumour suppressing sub-chromosomal transferable
                     candidate 4; pfam15264"
                     /db_xref="CDD:434584"
     CDS             1..321
                     /gene="Tssc4"
                     /coded_by="NM_001310046.1:223..1188"
                     /db_xref="GeneID:361682"
                     /db_xref="RGD:1307043"
ORIGIN      
        1 msglmaetea gleveepted dtlpsdtvsl sdsdsdlslp sgvevqalsp erlsgesqed
       61 sgpddppshp tgipttavqp fhlrgmsstf sqrshsifdc lesaarqepc sapqtsvvdn
      121 csfkrpvapp sqtparslsr vhgntdptrv hpvpdyvshp erwtkysled vsetseqsnr
      181 daalaflssr sqasptdyvp ffnqdpsscg egrvvftkpv rgsearaerk rvlkkgvvsg
      241 aggeasvela hlagpeaeew sghqgqpevv vpseaarpes ssgpigmktv gfhgskkrsr
      301 dhfrnrdsnp egpgsergps v
//
LOCUS       NP_543167                730 aa            linear   ROD 27-APR-2025
DEFINITION  death domain-associated protein 6 [Rattus norvegicus].
ACCESSION   NP_543167
VERSION     NP_543167.2
DBSOURCE    REFSEQ: accession NM_080891.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Chen,C., Sun,X., Xie,W., Chen,S., Hu,Y., Xing,D., Xu,J., Chen,X.,
            Zhao,Z., Han,Z., Xue,X., Shen,X. and Lin,K.
  TITLE     Opposing biological functions of the cytoplasm and nucleus DAXX
            modified by SUMO-2/3 in gastric cancer
  JOURNAL   Cell Death Dis 11 (7), 514 (2020)
   PUBMED   32641734
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Wu,C., Ding,H., Wang,S., Li,Y., Liu,S.B., Wang,X., Zheng,J.,
            Xue,T., Amin,H.M., Song,Y.H. and Zhou,J.
  TITLE     DAXX inhibits cancer stemness and epithelial-mesenchymal transition
            in gastric cancer
  JOURNAL   Br J Cancer 122 (10), 1477-1485 (2020)
   PUBMED   32203224
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Liu,Y., Guo,F., Zhu,X., Guo,W., Fu,T. and Wang,W.
  TITLE     Death Domain-Associated Protein Promotes Colon Cancer Metastasis
            through Direct Interaction with ZEB1
  JOURNAL   J Cancer 11 (3), 750-758 (2020)
   PUBMED   31942198
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 730)
  AUTHORS   LaFramboise,W.A., Pai,R.K., Petrosko,P., Belsky,M.A., Dhir,A.,
            Howard,P.G., Becich,M.J., Holtzman,M.P., Ahrendt,S.A.,
            Pingpank,J.F., Zeh,H.J., Dhir,R., Bartlett,D.L. and Choudry,H.A.
  TITLE     Discrimination of low- and high-grade appendiceal mucinous
            neoplasms by targeted sequencing of cancer-related variants
  JOURNAL   Mod Pathol 32 (8), 1197-1209 (2019)
   PUBMED   30962504
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Ziv,E., Rice,S.L., Filtes,J., Yarmohammadi,H., Boas,F.E.,
            Erinjeri,J.P., Petre,E.N., Brody,L.A., Brown,K.T., Covey,A.M.,
            Getrajdman,G.I., Maybody,M., Raj,N., Sofocleous,C.T., Solomon,S.B.
            and Reidy-Lagunes,D.
  TITLE     DAXX Mutation Status of Embolization-Treated Neuroendocrine Tumors
            Predicts Shorter Time to Hepatic Progression
  JOURNAL   J Vasc Interv Radiol 29 (11), 1519-1526 (2018)
   PUBMED   30342802
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Li,H., Leo,C., Zhu,J., Wu,X., O'Neil,J., Park,E.J. and Chen,J.D.
  TITLE     Sequestration and inhibition of Daxx-mediated transcriptional
            repression by PML
  JOURNAL   Mol Cell Biol 20 (5), 1784-1796 (2000)
   PUBMED   10669754
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Zhong,S., Salomoni,P., Ronchetti,S., Guo,A., Ruggero,D. and
            Pandolfi,P.P.
  TITLE     Promyelocytic leukemia protein (PML) and Daxx participate in a
            novel nuclear pathway for apoptosis
  JOURNAL   J Exp Med 191 (4), 631-640 (2000)
   PUBMED   10684855
REFERENCE   8  (residues 1 to 730)
  AUTHORS   Li,R., Pei,H., Watson,D.K. and Papas,T.S.
  TITLE     EAP1/Daxx interacts with ETS1 and represses transcriptional
            activation of ETS1 target genes
  JOURNAL   Oncogene 19 (6), 745-753 (2000)
   PUBMED   10698492
REFERENCE   9  (residues 1 to 730)
  AUTHORS   Everett,R.D., Earnshaw,W.C., Pluta,A.F., Sternsdorf,T.,
            Ainsztein,A.M., Carmena,M., Ruchaud,S., Hsu,W.L. and Orr,A.
  TITLE     A dynamic connection between centromeres and ND10 proteins
  JOURNAL   J Cell Sci 112 (Pt 20), 3443-3454 (1999)
   PUBMED   10504293
REFERENCE   10 (residues 1 to 730)
  AUTHORS   Michaelson,J.S., Bader,D., Kuo,F., Kozak,C. and Leder,P.
  TITLE     Loss of Daxx, a promiscuously interacting protein, results in
            extensive apoptosis in early mouse development
  JOURNAL   Genes Dev 13 (15), 1918-1923 (1999)
   PUBMED   10444590
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC128729.1.
            
            On Sep 12, 2009 this sequence version replaced NP_543167.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128729.1, SRR8487226.83983.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..730
                     /product="death domain-associated protein 6"
                     /note="Fas death domain-associated protein"
                     /calculated_mol_wt=80581
     Region          1..158
                     /region_name="Necessary for interaction with USP7 and
                     ATRX. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          56..144
                     /region_name="Daxx"
                     /note="Daxx N-terminal Rassf1C-interacting domain;
                     pfam03344"
                     /db_xref="CDD:460889"
     Site            order(81,83..84,87..88,91,121..122,124..125,127..128,
                     131..132,135,140)
                     /site_type="other"
                     /note="Rassf1C interface [polypeptide binding]"
                     /db_xref="CDD:240522"
     Region          147..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          181..414
                     /region_name="Interaction with histone H3.3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          181..385
                     /region_name="DAXX_histone_binding"
                     /note="Histone binding domain of the death-domain
                     associated protein (DAXX); cd13150"
                     /db_xref="CDD:240523"
     Site            order(193..194,197,200..201,203..209,213..216,218..221,
                     223..224,227,230..231,234,247..249,281..285,288,315,
                     319..320,323,326,329..330,333..334,336..338,340,367,
                     370..371,374..375,377..378,381..382,385)
                     /site_type="other"
                     /note="Histone H3.3 interface [polypeptide binding]"
                     /db_xref="CDD:240523"
     Site            order(207,281,283,286,327,330..331,334,339,346..349,352,
                     355,359,362,366,369..370,373..374,377,381)
                     /site_type="other"
                     /note="Histone H4 interface [polypeptide binding]"
                     /db_xref="CDD:240523"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          391..395
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O35613; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35613; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            502
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          616..730
                     /region_name="Interaction with SPOP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35613; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          621..627
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35613; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          662..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Region          723..730
                     /region_name="Sumo interaction motif (SIM).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UER7; propagated from
                     UniProtKB/Swiss-Prot (Q8VIB2.1)"
     CDS             1..730
                     /gene="Daxx"
                     /coded_by="NM_080891.2:97..2289"
                     /db_xref="GeneID:140926"
                     /db_xref="RGD:621227"
ORIGIN      
        1 matddsiivl ddddedeaaa qpgpsnpasn pvspgpeasg pseshgdggs snsgsrkcyk
       61 leneklfeef lelckmqtsd hpevvpflhk lqqraqsafl asaefrnils rvlsrsrnrp
      121 aklyvyinel ctvlkahsik kklnlapaas aessgdnppt dppsdltnte ttaseasrtr
      181 gsrrqiqrle qllalyvaei qrlqekeldl selddpdssy lqearlkrkl irlfgrlcel
      241 kdcssltgrv ieqripyrgt rypevnrrie rlinkpgpdt fpdygdvlra vekaatrhsl
      301 glprqqlqll aqdafrdvgv rlqerrhldl iynfgchltd dyrpgvdpal tdptlarrlr
      361 enrtlamsrl deviskyamm qdkseegerq krrarllats qssdlpkass dsgegpsgva
      421 sqedpttpka etedeeddee sddeeeeeee eeeeateded edleqlqedq ddeeeeegdn
      481 eddksptsps pifrrrnsap teglrspeeq qergltgtpa spleaspglp stdaessgeq
      541 lqerllages pvsqlseldm ealpeetips peergisssr rksdsslpti lengaamvts
      601 tsfngrvssh pcrdasppsk rfrkekkqlg pgplensyvk kqtmaqqdsg wkisvlstps
      661 splasvgpva dsstrvdsps helvtsslcn pspslilqtp qsqsprpciy ktsvatqcdp
      721 eeiivlsdsd
//
LOCUS       NP_001257692             456 aa            linear   ROD 27-APR-2025
DEFINITION  ribonuclease inhibitor isoform b [Rattus norvegicus].
ACCESSION   NP_001257692
VERSION     NP_001257692.1
DBSOURCE    REFSEQ: accession NM_001270763.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhao,C., Ni,Y., Liu,Y., Liu,T., Yang,S., Liu,Z. and Liu,S.
  TITLE     Identification and distribution of rRNH1, a gene upregulated after
            spinal cord primary neuron injury
  JOURNAL   In Vitro Cell Dev Biol Anim 50 (3), 183-187 (2014)
   PUBMED   24288130
  REMARK    GeneRIF: RNH1 protein is upregulated after spinal cord injury.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhao,C.F., Liu,Y., Que,H.P., Yang,S.G., Liu,T., Liu,Z.Q., Hui,H.D.
            and Liu,S.
  TITLE     Rnh1 promotes differentiation and myelination via RhoA in
            oligodendrocytes
  JOURNAL   Cell Tissue Res 353 (3), 381-389 (2013)
   PUBMED   23624614
  REMARK    GeneRIF: Rnh1-mediated RhoA inactivation enhances the
            differentiation and myelination in oligodendrocytes.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Kawanomoto,M., Motojima,K., Sasaki,M., Hattori,H. and Goto,S.
  TITLE     cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue
            distribution of the mRNA
  JOURNAL   Biochim Biophys Acta 1129 (3), 335-338 (1992)
   PUBMED   1536887
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Shapiro,R. and Vallee,B.L.
  TITLE     Human placental ribonuclease inhibitor abolishes both angiogenic
            and ribonucleolytic activities of angiogenin
  JOURNAL   Proc Natl Acad Sci U S A 84 (8), 2238-2241 (1987)
   PUBMED   3470787
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC070501.1.
            
            Transcript Variant: This variant (3) has an alternate exon in place
            of the first exon compared to variant 1. The resulting isoform (b)
            is shorter at the N-terminus compared to isoform a. Variants 2 and
            3 both encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ233708.1, FQ218714.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..456
                     /product="ribonuclease inhibitor isoform b"
                     /note="ribonuclease inhibitor"
                     /calculated_mol_wt=49788
     Region          1..320
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P10775; propagated from
                     UniProtKB/Swiss-Prot (P29315.2)"
     Region          2..24
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(3,5,8,10,25,28,30,33,35,53,56,58,61,63,82,85,87,90,
                     92,110,113,115,118,120,139,142,144,147,149,167,170,172,
                     175,177,196,199,201,204,206,224,227,229,232,234,253,256,
                     258,261,263,281,284,286,289,291,310,313,315,318,320)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          15..43
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          25..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(31..32,89,146,174,231,257,259,285,314)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          44..71
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          53..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          72..100
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          82..109
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13489; propagated from
                     UniProtKB/Swiss-Prot (P29315.2)"
     Region          101..128
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          110..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..157
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          139..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..185
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          167..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..214
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          196..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          215..242
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          224..252
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..271
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          253..273
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          272..299
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          <277..>419
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          281..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          300..328
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          329..356
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          338..366
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          357..385
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          367..394
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          386..413
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     Region          414..442
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P29315.2)"
     CDS             1..456
                     /gene="Rnh1"
                     /gene_synonym="Rnh"
                     /coded_by="NM_001270763.1:125..1495"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:100360501"
                     /db_xref="RGD:621398"
ORIGIN      
        1 msldiqceql sdarwtellp liqqyqvvrl ddcgltevrc kdirsaiqan paltelslrt
       61 nelgdagvgl vlqglqnptc kiqklslqnc slteagcgvl pdvlrslstl relhlndnpl
      121 gdeglkllce glrdpqcrle klqleycnlt atsceplasv lrvkpdfkel vlsnndfhea
      181 gihtlcqglk dsacqleslk lencgitsan ckdlcdvvas kaslqeldlg snklgntgia
      241 alcsglllps crlrtlwlwd cdvtaegckd lcrvlrakqs lkelslagne lkdegaqllc
      301 esllepgcql eslwvktcsl taascphfcs vltknrslfe lqmssnplgd sgvvelckal
      361 gypdtvlrvl wlgdcdvtds gcsslatvll anrslreldl snncmgdtgv lqlleslkqp
      421 scalqqlvly diywtdeved qlraleeerp slriis
//
LOCUS       NP_001013212             321 aa            linear   ROD 27-APR-2025
DEFINITION  U5 small nuclear ribonucleoprotein TSSC4 [Rattus norvegicus].
ACCESSION   NP_001013212 XP_341966
VERSION     NP_001013212.2
DBSOURCE    REFSEQ: accession NM_001013194.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 23, 2015 this sequence version replaced NP_001013212.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083775.1, SRR22582416.1567159.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..321
                     /product="U5 small nuclear ribonucleoprotein TSSC4"
                     /note="protein TSSC4; tumor-suppressing subchromosomal
                     transferable fragment 4"
                     /calculated_mol_wt=34196
     Region          95..211
                     /region_name="TSSC4"
                     /note="Tumour suppressing sub-chromosomal transferable
                     candidate 4; pfam15264"
                     /db_xref="CDD:434584"
     CDS             1..321
                     /gene="Tssc4"
                     /coded_by="NM_001013194.2:303..1268"
                     /db_xref="GeneID:361682"
                     /db_xref="RGD:1307043"
ORIGIN      
        1 msglmaetea gleveepted dtlpsdtvsl sdsdsdlslp sgvevqalsp erlsgesqed
       61 sgpddppshp tgipttavqp fhlrgmsstf sqrshsifdc lesaarqepc sapqtsvvdn
      121 csfkrpvapp sqtparslsr vhgntdptrv hpvpdyvshp erwtkysled vsetseqsnr
      181 daalaflssr sqasptdyvp ffnqdpsscg egrvvftkpv rgsearaerk rvlkkgvvsg
      241 aggeasvela hlagpeaeew sghqgqpevv vpseaarpes ssgpigmktv gfhgskkrsr
      301 dhfrnrdsnp egpgsergps v
//
LOCUS       NP_001158179             154 aa            linear   ROD 27-APR-2025
DEFINITION  protein CutA isoform 2 [Rattus norvegicus].
ACCESSION   NP_001158179
VERSION     NP_001158179.1
DBSOURCE    REFSEQ: accession NM_001164707.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Liang,D., Nunes-Tavares,N., Xie,H.Q., Carvalho,S., Bon,S. and
            Massoulie,J.
  TITLE     Protein CutA undergoes an unusual transfer into the secretory
            pathway and affects the folding, oligomerization, and secretion of
            acetylcholinesterase
  JOURNAL   J Biol Chem 284 (8), 5195-5207 (2009)
   PUBMED   19049969
  REMARK    GeneRIF: Protein CutA undergoes an unusual transfer into the
            secretory pathway and affects the folding, oligomerization, and
            secretion of acetylcholinesterase.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Arnesano,F., Banci,L., Benvenuti,M., Bertini,I., Calderone,V.,
            Mangani,S. and Viezzoli,M.S.
  TITLE     The evolutionarily conserved trimeric structure of CutA1 proteins
            suggests a role in signal transduction
  JOURNAL   J Biol Chem 278 (46), 45999-46006 (2003)
   PUBMED   12949080
  REMARK    GeneRIF: comparative x-ray crystallography analysis suggests CutA1
            proteins have a role in signal transduction through allosteric
            communications between subunits.
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Perrier,A.L., Cousin,X., Boschetti,N., Haas,R., Chatel,J.M.,
            Bon,S., Roberts,W.L., Pickett,S.R., Massoulie,J., Rosenberry,T.L.
            and Krejci,E.
  TITLE     Two distinct proteins are associated with tetrameric
            acetylcholinesterase on the cell surface
  JOURNAL   J Biol Chem 275 (44), 34260-34265 (2000)
   PUBMED   10954708
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Navaratnam,D.S., Fernando,F.S., Priddle,J.D., Giles,K., Clegg,S.M.,
            Pappin,D.J., Craig,I. and Smith,A.D.
  TITLE     Hydrophobic protein that copurifies with human brain
            acetylcholinesterase: amino acid sequence, genomic organization,
            and chromosomal localization
  JOURNAL   J Neurochem 74 (5), 2146-2153 (2000)
   PUBMED   10800960
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP501235.1, DV717217.1 and BX883042.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            a downstream start codon compared to variant 1. Both variants 2 and
            3 encode the same protein (isoform 2), which is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP501235.1, DV717217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..154
                     /product="protein CutA isoform 2"
                     /note="protein CutA; brain acetylcholinesterase putative
                     membrane anchor; divalent cation tolerant protein CUTA"
                     /calculated_mol_wt=16282
     Region          47..141
                     /region_name="CutA1"
                     /note="CutA1 divalent ion tolerance protein; pfam03091"
                     /db_xref="CDD:460800"
     CDS             1..154
                     /gene="Cuta"
                     /gene_synonym="CutA1"
                     /coded_by="NM_001164707.1:160..624"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:294288"
                     /db_xref="RGD:1303306"
ORIGIN      
        1 mpallpvasr llllpralls masgsppsqp spasgsgyvp gsvsaafvtc pnekvakeia
       61 ravvekrlaa cvnlipqits iyewkgkiee dsevlmmikt qsslvpalte fvrsvhpyev
      121 aevialpveq gnppylhwvh qvtesvsgsg kalp
//
LOCUS       NP_001295184             810 aa            linear   ROD 27-APR-2025
DEFINITION  aryl hydrocarbon receptor isoform 3 [Rattus norvegicus].
ACCESSION   NP_001295184
VERSION     NP_001295184.1
DBSOURCE    REFSEQ: accession NM_001308255.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Andersen,M.E., Barutcu,A.R., Black,M.B. and Harrill,J.A.
  TITLE     Transcriptomic analysis of AHR wildtype and Knock-out rat livers
            supports TCDD's role in AHR/ARNT-mediated circadian disruption and
            hepatotoxicity
  JOURNAL   Toxicol Appl Pharmacol 487, 116956 (2024)
   PUBMED   38735589
  REMARK    GeneRIF: Transcriptomic analysis of AHR wildtype and Knock-out rat
            livers supports TCDD's role in AHR/ARNT-mediated circadian
            disruption and hepatotoxicity.
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Chausse,A.M., Roche,S.M., Moroldo,M., Hennequet-Antier,C.,
            Holbert,S., Kempf,F., Barilleau,E., Trotereau,J. and Velge,P.
  TITLE     Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis
  JOURNAL   Virulence 14 (1), 2158663 (2023)
   PUBMED   36600181
  REMARK    GeneRIF: Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Xu,J., Sun,X., Qin,F., Wang,X., Chen,Q. and Yan,R.
  TITLE     Protective effects of salvianolic acid B on intestinal
            ischemia/reperfusion injury in rats by regulating the
            AhR/IL-22/STAT6 axis
  JOURNAL   J Recept Signal Transduct Res 43 (3), 73-82 (2023)
   PUBMED   37387514
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Kouno,T., Zeng,S., Wang,Y., Duan,Y., Lang,S., Gao,B., Hartmann,P.,
            Cabre,N., Llorente,C., Galbert,C., Emond,P., Sokol,H., James,M.,
            Chao,C.C., Gao,J.R., Perreault,M., Hava,D.L. and Schnabl,B.
  TITLE     Engineered bacteria producing aryl-hydrocarbon receptor agonists
            protect against ethanol-induced liver disease in mice
  JOURNAL   Alcohol Clin Exp Res (Hoboken) 47 (5), 856-867 (2023)
   PUBMED   36871955
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Nori,P., Haghshenas,R., Aftabi,Y. and Akbari,H.
  TITLE     Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery
  JOURNAL   Sci Rep 13 (1), 3721 (2023)
   PUBMED   36879035
  REMARK    GeneRIF: Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Fernandez-Salguero,P., Pineau,T., Hilbert,D.M., McPhail,T.,
            Lee,S.S., Kimura,S., Nebert,D.W., Rudikoff,S., Ward,J.M. and
            Gonzalez,F.J.
  TITLE     Immune system impairment and hepatic fibrosis in mice lacking the
            dioxin-binding Ah receptor
  JOURNAL   Science 268 (5211), 722-726 (1995)
   PUBMED   7732381
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Elferink,C.J. and Whitlock,J.P. Jr.
  TITLE     Dioxin-dependent, DNA sequence-specific binding of a multiprotein
            complex containing the Ah receptor
  JOURNAL   Receptor 4 (3), 157-173 (1994)
   PUBMED   7812217
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Puga,A., Nebert,D.W. and Carrier,F.
  TITLE     Dioxin induces expression of c-fos and c-jun proto-oncogenes and a
            large increase in transcription factor AP-1
  JOURNAL   DNA Cell Biol 11 (4), 269-281 (1992)
   PUBMED   1605850
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Ema,M., Sogawa,K., Watanabe,N., Chujoh,Y., Matsushita,N., Gotoh,O.,
            Funae,Y. and Fujii-Kuriyama,Y.
  TITLE     cDNA cloning and structure of mouse putative Ah receptor
  JOURNAL   Biochem Biophys Res Commun 184 (1), 246-253 (1992)
   PUBMED   1314586
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Okino,S.T., Pendurthi,U.R. and Tukey,R.H.
  TITLE     Phorbol esters inhibit the dioxin receptor-mediated transcriptional
            activation of the mouse Cyp1a-1 and Cyp1a-2 genes by
            2,3,7,8-tetrachlorodibenzo-p-dioxin
  JOURNAL   J Biol Chem 267 (10), 6991-6998 (1992)
   PUBMED   1313028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction in the 3' end of the coding sequence compared to
            variant 1. The resulting isoform (3) has the same N- and C-termini
            but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF082124.1, AM902281.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..810
                     /product="aryl hydrocarbon receptor isoform 3"
                     /note="ah receptor"
                     /calculated_mol_wt=91364
     Region          27..87
                     /region_name="bHLH-PAS_AhR"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in aryl hydrocarbon receptor (AhR) and
                     similar proteins; cd11436"
                     /db_xref="CDD:381442"
     Site            order(33..39,41,43,64..66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381442"
     Site            order(38,41..42,45..46,48..49,52..56,64..66,69..79,82,
                     85..86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381442"
     Region          111..>181
                     /region_name="PAS"
                     /note="PAS fold; pfam00989"
                     /db_xref="CDD:395786"
     Region          295..380
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(298,302,308,322..325,351,356)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(319,323,331,334..335,363,365)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     CDS             1..810
                     /gene="Ahr"
                     /coded_by="NM_001308255.1:29..2461"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25690"
                     /db_xref="RGD:2074"
ORIGIN      
        1 mssganitya srkrrkpvqk tvkpvpaegi ksnpskrhrd rlnteldrla sllpfpqdvi
       61 skldklsvlr lsvsylraks ffdvalkstp adrsrgqdqc raqvrdwqdl qegefllqal
      121 ngfvlvvtad alvfyassti qdylgfqqsd vihqsvyeli htedraefqr qlhwalnpsq
      181 ctdsaqgvde thglpqpavy ytpdqlppen tafmercfrc rlrclldnss gflamnfqgr
      241 lkylhgqnkk gkdgallppq lalfaiatpl qppsileirt knfifrtkhk ldftpigcda
      301 kgqlilgyte velcnkgsgy qfihaadmlh caeshirmik tgesgmtvfr llakhsrwrw
      361 vqsnarliyr ngrpdyiiat qrpltdeegr ehlqkrsmtl pfmfatgkav lyeisspfsp
      421 imdplpirtk sntsrkdwap qstpskdsfh pnslmsaliq qdesiylcpp sspapldshf
      481 lmdsmsecgs wqgsfaaasn eallkheeir htqdvnltls ggpselfpdn knndlysimr
      541 nlgidfedir smqneeffrt dssgevdfkd iditdeilty vqdslnnstl lnsacqqqpv
      601 sqhlscmlqe rlqleqqqql qqqhptqtle pqrqlcqvev pqhelgqktk hmqvngmfas
      661 wnpappvsfs cpqqerkhys lfsglqgtaq efpyksevds mpytqnfapc nqsllpehsk
      721 gtqldfpgrd ferslhpnas nledfvsclq vpenqrhgin sqsamfqsps ilneaysadl
      781 ssighlqtaa hlprlaeaqp lpditpsgfl
//
LOCUS       NP_001030311             238 aa            linear   ROD 27-APR-2025
DEFINITION  survival of motor neuron-related-splicing factor 30 [Rattus
            norvegicus].
ACCESSION   NP_001030311
VERSION     NP_001030311.1
DBSOURCE    REFSEQ: accession NM_001035234.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            EV778425.1, BC098697.1, CV106705.1 and CB726049.1.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1 and 2 both encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EV771001.1, DN933061.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..238
                     /product="survival of motor neuron-related-splicing factor
                     30"
                     /note="survival motor neuron domain-containing protein 1"
                     /calculated_mol_wt=26652
     Region          73..128
                     /region_name="Tudor_SPF30"
                     /note="Tudor domain found in survival of motor
                     neuron-related-splicing factor 30 (SPF30) and similar
                     proteins; cd20399"
                     /db_xref="CDD:410470"
     Site            order(83,88,90,108,111,113)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410470"
     Region          142..160
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QQU6.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75940; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU6.1)"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75940; propagated from
                     UniProtKB/Swiss-Prot (Q4QQU6.1)"
     CDS             1..238
                     /gene="Smndc1"
                     /coded_by="NM_001035234.2:192..908"
                     /db_xref="GeneID:287768"
                     /db_xref="RGD:1309151"
ORIGIN      
        1 msedlakqla sykaqlqqve aalsgngene dllklkkdlq evieltkdll stqpsetlts
       61 sdsfastqpt hswkvgdkcm avwsedgqcy eaeieeidee ngtaaitfav ygnaevtpll
      121 nlkpveegrk akedsgnkpm skkemiaqqr eykkkkalkk aqrikeleqe redqkvkwqq
      181 fnnraysknk kgqvkrsifa spesvtgkvg vgtcgiadkp mtqyqdtsky nvrhlmpq
//
LOCUS       NP_001102068             244 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity protein phosphatase 15 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102068 XP_001060408 XP_342546
VERSION     NP_001102068.2
DBSOURCE    REFSEQ: accession NM_001108598.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Rodriguez-Molina,J.F., Lopez-Anido,C., Ma,K.H., Zhang,C., Olson,T.,
            Muth,K.N., Weider,M. and Svaren,J.
  TITLE     Dual specificity phosphatase 15 regulates Erk activation in Schwann
            cells
  JOURNAL   J Neurochem 140 (3), 368-382 (2017)
   PUBMED   27891578
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Jeong,D.G., Wei,C.H., Ku,B., Jeon,T.J., Chien,P.N., Kim,J.K.,
            Park,S.Y., Hwang,H.S., Ryu,S.Y., Park,H., Kim,D.S., Kim,S.J. and
            Ryu,S.E.
  TITLE     The family-wide structure and function of human dual-specificity
            protein phosphatases
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 421-435 (2014)
   PUBMED   24531476
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Schmidt,F., van den Eijnden,M., Pescini Gobert,R., Saborio,G.P.,
            Carboni,S., Alliod,C., Pouly,S., Staugaitis,S.M., Dutta,R.,
            Trapp,B. and Hooft van Huijsduijnen,R.
  TITLE     Identification of VHY/Dusp15 as a regulator of oligodendrocyte
            differentiation through a systematic genomics approach
  JOURNAL   PLoS One 7 (7), e40457 (2012)
   PUBMED   22792334
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Friedberg,I., Nika,K., Tautz,L., Saito,K., Cerignoli,F.,
            Friedberg,I., Godzik,A. and Mustelin,T.
  TITLE     Identification and characterization of DUSP27, a novel
            dual-specific protein phosphatase
  JOURNAL   FEBS Lett 581 (13), 2527-2533 (2007)
   PUBMED   17498703
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB585518.1, CB576376.1 and BC168211.1.
            
            On Oct 1, 2011 this sequence version replaced NP_001102068.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB576376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..244
                     /product="dual specificity protein phosphatase 15 isoform
                     1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="dual specificity protein phosphatase 15; dual
                     specificity phosphatase-like 15"
                     /calculated_mol_wt=27005
     Region          1..154
                     /region_name="DSP_DUSP15"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 15; cd14582"
                     /db_xref="CDD:350430"
     CDS             1..244
                     /gene="Dusp15"
                     /coded_by="NM_001108598.2:207..941"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362238"
                     /db_xref="RGD:1305990"
ORIGIN      
        1 mgngmtkvlp glylgnfida kdpdqlgrnk ithivsihes pqpllqdity lrisvsdtpe
       61 vpikkhfkec vhfihscrln ggnclvhcls ftsgsffagi srsttvviay vmtvtglgwq
      121 evleaikasr pianpnpgfr qqleefgwan sqklrrqlee rfgeipfrde edlrallplc
      181 rrcrqgpgts apsattassa asegtlqrlv prspreshrp lpllarvkqt ffclprclsr
      241 kggk
//
LOCUS       NP_001263363             402 aa            linear   ROD 27-APR-2025
DEFINITION  high mobility group nucleosome-binding domain-containing protein 5
            [Rattus norvegicus].
ACCESSION   NP_001263363 XP_003752142 XP_003754848
VERSION     NP_001263363.1
DBSOURCE    REFSEQ: accession NM_001276434.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Ciappio,E.D., Krausz,K.W., Rochman,M., Furusawa,T., Bonzo,J.A.,
            Tessarollo,L., Gonzalez,F.J. and Bustin,M.
  TITLE     Metabolomics reveals a role for the chromatin-binding protein HMGN5
            in glutathione metabolism
  JOURNAL   PLoS One 9 (1), e84583 (2014)
   PUBMED   24392144
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Rochman,M., Taher,L., Kurahashi,T., Cherukuri,S., Uversky,V.N.,
            Landsman,D., Ovcharenko,I. and Bustin,M.
  TITLE     Effects of HMGN variants on the cellular transcription profile
  JOURNAL   Nucleic Acids Res 39 (10), 4076-4087 (2011)
   PUBMED   21278158
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Jiang,N., Zhou,L.Q. and Zhang,X.Y.
  TITLE     Downregulation of the nucleosome-binding protein 1 (NSBP1) gene can
            inhibit the in vitro and in vivo proliferation of prostate cancer
            cells
  JOURNAL   Asian J Androl 12 (5), 709-717 (2010)
   PUBMED   20531280
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Shirakawa,H., Rochman,M., Furusawa,T., Kuehn,M.R., Horigome,S.,
            Haketa,K., Sugita,Y., Inada,T., Komai,M. and Bustin,M.
  TITLE     The nucleosomal binding protein NSBP1 is highly expressed in the
            placenta and modulates the expression of differentiation markers in
            placental Rcho-1 cells
  JOURNAL   J Cell Biochem 106 (4), 651-658 (2009)
   PUBMED   19160411
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Shirakawa,H., Landsman,D., Postnikov,Y.V. and Bustin,M.
  TITLE     NBP-45, a novel nucleosomal binding protein with a tissue-specific
            and developmentally regulated expression
  JOURNAL   J Biol Chem 275 (9), 6368-6374 (2000)
   PUBMED   10692437
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Feb 22, 2013 this sequence version replaced
            XP_003754848.1, XP_003752142.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..402
                     /product="high mobility group nucleosome-binding
                     domain-containing protein 5"
                     /note="nucleosome-binding protein 1"
                     /calculated_mol_wt=45330
     Region          2..96
                     /region_name="HMG14_17"
                     /note="HMG14 and HMG17; pfam01101"
                     /db_xref="CDD:460064"
     Region          <218..400
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     CDS             1..402
                     /gene="Hmgn5"
                     /gene_synonym="Nsbp1"
                     /coded_by="NM_001276434.1:179..1387"
                     /db_xref="GeneID:100910616"
                     /db_xref="RGD:6497694"
ORIGIN      
        1 mpkrkaagda sqepkrrsar lsampvpftp elkpkrasts rktkttnvve eskdagatti
       61 petkpevvkg ecnmenaeng eakiieapis kmeteevkeq inedtegdgg ekkeavvtkg
      121 kndeleaniq dvekdedeke hedtgeeged geregglkek pdvaeiedak eakddeeked
      181 kekeddkggd gkkeeekdde geaeteeevk eqqkeetegd dgkckveenk egrkesqhee
      241 egkeelheed gkedlheedg kedlheedgk edlheeegke dlheeegked lheeegkedl
      301 heeegkedlh eeegkedlhe eegkedlhee egkedlheed gkegqheedg kkkadgnedr
      361 keeeeqeaat egndenkvev eeeadnkdfk edgekgepvs tv
//
LOCUS       NP_036759                 78 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-dependent protein kinase inhibitor beta isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_036759
VERSION     NP_036759.2
DBSOURCE    REFSEQ: accession NM_012627.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Cerone,M.A., Burgess,D.J., Naceur-Lombardelli,C., Lord,C.J. and
            Ashworth,A.
  TITLE     High-throughput RNAi screening reveals novel regulators of
            telomerase
  JOURNAL   Cancer Res 71 (9), 3328-3340 (2011)
   PUBMED   21531765
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Dahia,C.L. and Rao,A.J.
  TITLE     Regulation of FSH receptor, PKIbeta, IL-6 and calcium mobilization:
            Possible mediators of differential action of FSH
  JOURNAL   Mol Cell Endocrinol 247 (1-2), 73-81 (2006)
   PUBMED   16406266
  REMARK    GeneRIF: PKIbeta and calcium, which are the downstream signaling
            molecules, are involved in FSH regulated Sertoli cells
            proliferation.
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Xiao,H.S., Huang,Q.H., Zhang,F.X., Bao,L., Lu,Y.J., Guo,C.,
            Yang,L., Huang,W.J., Fu,G., Xu,S.H., Cheng,X.P., Yan,Q., Zhu,Z.D.,
            Zhang,X., Chen,Z., Han,Z.G. and Zhang,X.
  TITLE     Identification of gene expression profile of dorsal root ganglion
            in the rat peripheral axotomy model of neuropathic pain
  JOURNAL   Proc Natl Acad Sci U S A 99 (12), 8360-8365 (2002)
   PUBMED   12060780
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Kumar,P. and Walsh,D.A.
  TITLE     A dual-specificity isoform of the protein kinase inhibitor PKI
            produced by alternate gene splicing
  JOURNAL   Biochem J 362 (Pt 3), 533-537 (2002)
   PUBMED   11879178
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Andoh,Y., Kuramoto,T., Yokoi,N., Maihara,T., Kitada,K. and
            Serikawa,T.
  TITLE     Correlation between genetic and cytogenetic maps of the rat
  JOURNAL   Mamm Genome 9 (4), 287-293 (1998)
   PUBMED   9530624
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Baude,E.J., Dignam,S.S., Olsen,S.R., Reimann,E.M. and Uhler,M.D.
  TITLE     Glutamic acid 203 of the cAMP-dependent protein kinase catalytic
            subunit participates in the inhibition by two isoforms of the
            protein kinase inhibitor
  JOURNAL   J Biol Chem 269 (3), 2316-2323 (1994)
   PUBMED   7905001
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Van Patten,S.M., Ng,D.C., Th'ng,J.P., Angelos,K.L., Smith,A.J. and
            Walsh,D.A.
  TITLE     Molecular cloning of a rat testis form of the inhibitor protein of
            cAMP-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5383-5387 (1991)
   PUBMED   2052616
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG666532.1, BC078880.1 and FQ231722.1.
            
            On Oct 3, 2006 this sequence version replaced NP_036759.1.
            
            Transcript Variant: This variant (2) lacks an internal exon
            compared to variant 1, which results in translation initiation from
            an in-frame downstream AUG and an isoform (2) with a shorter
            N-terminus compared to isoform 1. Variants 2 and 3 encode the same
            isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ231722.1, M64092.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..78
                     /product="cAMP-dependent protein kinase inhibitor beta
                     isoform 2"
                     /note="PKI-beta; protein kinase inhibitor beta, cAMP
                     dependent, testis specific; protein kinase
                     (cAMP-dependent, catalytic) inhibitor beta; cAMP-dependent
                     protein kinase (catalytic subunit binding) inhibtor 2;
                     protein kinase inhibitor beta, cAMP dependent, catalytic;
                     protein kinase inhibitor beta, (cAMP-dependent, catalytic)
                     inhibitor beta; protein kinase inhibitor, beta"
                     /calculated_mol_wt=8261
     Region          9..77
                     /region_name="PKI"
                     /note="cAMP-dependent protein kinase inhibitor; pfam02827"
                     /db_xref="CDD:460716"
     CDS             1..78
                     /gene="Pkib"
                     /gene_synonym="PKINH; Prkacn2; RATPKINH"
                     /coded_by="NM_012627.3:278..514"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24678"
                     /db_xref="RGD:3335"
ORIGIN      
        1 mrtdssemtd vesvissfas saragrrnal pdiqsslatg gspdlalkle alavkedakm
       61 kneekdqgqp kkpldedk
//
LOCUS       NP_001009920             221 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione S-transferase alpha-5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001009920 XP_579318
VERSION     NP_001009920.1
DBSOURCE    REFSEQ: accession NM_001009920.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Xiao,Y., Zhang,Z., Fu,Y., Shan,H., Cui,S. and Wu,J.
  TITLE     GSTA3 regulates TGF-beta1-induced renal interstitial fibrosis in
            NRK-52E cells as a component of the PI3K-Keap1/Nrf2 pathway
  JOURNAL   J Int Med Res 47 (11), 5787-5801 (2019)
   PUBMED   31617428
  REMARK    GeneRIF: The PI3K-KEAP1/Nrf2-GSTA3 signaling pathway is a possible
            mechanism of resisting external stimulation of renal fibrosis
            factors.
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Chen,H., Gan,Q., Yang,C., Peng,X., Qin,J., Qiu,S., Jiang,Y., Tu,S.,
            He,Y., Li,S., Yang,H., Tao,L. and Peng,Y.
  TITLE     A novel role of glutathione S-transferase A3 in inhibiting hepatic
            stellate cell activation and rat hepatic fibrosis
  JOURNAL   J Transl Med 17 (1), 280 (2019)
   PUBMED   31443720
  REMARK    GeneRIF: GSTA3 inhibited hepatic stellate cell activation and liver
            fibrosis
            Erratum:[J Transl Med. 2020 Apr 30;18(1):182. doi:
            10.1186/s12967-020-02346-4. PMID: 32354374]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Xiao,Y., Liu,J., Peng,Y., Xiong,X., Huang,L., Yang,H., Zhang,J. and
            Tao,L.
  TITLE     GSTA3 Attenuates Renal Interstitial Fibrosis by Inhibiting
            TGF-Beta-Induced Tubular Epithelial-Mesenchymal Transition and
            Fibronectin Expression
  JOURNAL   PLoS One 11 (9), e0160855 (2016)
   PUBMED   27602565
  REMARK    GeneRIF: Protein and mRNA expression of GSTA3 in UUO rats and
            NRK-52E cells were determined by Western blot and RT-PCR. siRNA and
            overexpression plasmid were transfected specifically to assess the
            role of GSTA3 in renal interstitial fibrosis
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ilic,Z., Crawford,D., Vakharia,D., Egner,P.A. and Sell,S.
  TITLE     Glutathione-S-transferase A3 knockout mice are sensitive to acute
            cytotoxic and genotoxic effects of aflatoxin B1
  JOURNAL   Toxicol Appl Pharmacol 242 (3), 241-246 (2010)
   PUBMED   19850059
  REMARK    Erratum:[Toxicol Appl Pharmacol. 2010 Jun 1;245(2):280. doi:
            10.1016/j.taap.2010.03.018. PMID: 20852735]
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Caruana,G., Cullen-McEwen,L., Nelson,A.L., Kostoulias,X., Woods,K.,
            Gardiner,B., Davis,M.J., Taylor,D.F., Teasdale,R.D., Grimmond,S.M.,
            Little,M.H. and Bertram,J.F.
  TITLE     Spatial gene expression in the T-stage mouse metanephros
  JOURNAL   Gene Expr Patterns 6 (8), 807-825 (2006)
   PUBMED   16545622
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Pulford,D.J. and Hayes,J.D.
  TITLE     Characterization of the rat glutathione S-transferase Yc2 subunit
            gene, GSTA5: identification of a putative antioxidant-responsive
            element in the 5'-flanking region of rat GSTA5 that may mediate
            chemoprotection against aflatoxin B1
  JOURNAL   Biochem J 318 (Pt 1) (Pt 1), 75-84 (1996)
   PUBMED   8761455
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Hayes,J.D., Nguyen,T., Judah,D.J., Petersson,D.G. and Neal,G.E.
  TITLE     Cloning of cDNAs from fetal rat liver encoding glutathione
            S-transferase Yc polypeptides. The Yc2 subunit is expressed in
            adult rat liver resistant to the hepatocarcinogen aflatoxin B1
  JOURNAL   J Biol Chem 269 (32), 20707-20717 (1994)
   PUBMED   8051171
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Klinga-Levan,K., Andersson,A., Hanson,C., Ridderstrom,M.,
            Stenberg,G., Mannervik,B., Vajdy,M., Szpirer,J., Szpirer,C. and
            Levan,G.
  TITLE     Mapping of glutathione transferase (GST) genes in the rat
  JOURNAL   Hereditas 119 (3), 285-296 (1993)
   PUBMED   8144363
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Hayes,J.D., Judah,D.J., McLellan,L.I., Kerr,L.A., Peacock,S.D. and
            Neal,G.E.
  TITLE     Ethoxyquin-induced resistance to aflatoxin B1 in the rat is
            associated with the expression of a novel alpha-class glutathione
            S-transferase subunit, Yc2, which possesses high catalytic activity
            for aflatoxin B1-8,9-epoxide
  JOURNAL   Biochem J 279 (Pt 2) (Pt 2), 385-398 (1991)
   PUBMED   1953636
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Pickett,C.B., Telakowski-Hopkins,C.A., Ding,G.J., Argenbright,L.
            and Lu,A.Y.
  TITLE     Rat liver glutathione S-transferases. Complete nucleotide sequence
            of a glutathione S-transferase mRNA and the regulation of the Ya,
            Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital
  JOURNAL   J Biol Chem 259 (8), 5182-5188 (1984)
   PUBMED   6325423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Apr 21, 2005 this sequence version replaced XP_579318.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the Celera
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X78847.1, SRR23984936.1089117.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..221
                     /product="glutathione S-transferase alpha-5 isoform 1"
                     /EC_number="2.5.1.18"
                     /note="glutathione S-transferase alpha-5; GST Yc2; GST
                     A5-5; glutathione S-transferase Yc2 subunit; glutathione
                     S-transferase A3"
                     /calculated_mol_wt=25216
     Region          4..82
                     /region_name="GST_N_Alpha"
                     /note="GST_N family, Class Alpha subfamily; GSTs are
                     cytosolic dimeric proteins involved in cellular
                     detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of endogenous and
                     xenobiotic alkylating agents, including carcinogens;
                     cd03077"
                     /db_xref="CDD:239375"
     Site            order(11,13,15,17..18,21,24..25,32,36,69,72..73)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Site            order(45,54..55,67..68)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:239375"
     Site            order(52..53,61,66..67,69..70,73..74,78)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Region          86..220
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(86..87,89,93..95,97..98,101,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(97,104,107,110..111,131..132,135,152..155,158,
                     161..162,165..166,169,193..194,196..201)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(101,107,111,131,208,216,220)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     CDS             1..221
                     /gene="Gsta3"
                     /gene_synonym="Gsta5; Yc2"
                     /coded_by="NM_001009920.2:229..894"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:494500"
                     /db_xref="RGD:1591980"
ORIGIN      
        1 mpgkpvlhyf dgrgrmepir wllaaagvef eenflktrdd larlrsdgsl mfeqvpmvei
       61 dgmklvqtka ilnyiatkyn lygkdmkera lidmyaegva dlelmvlyyp ymppgekeas
      121 lakikdkarn ryfpayekvl kshgqdylvg nklsradvsl vellyhveem dpgivdnfpl
      181 lkalrtrvsn lptvkkflqp gsqrkpfdde kcvesakkif s
//
LOCUS       NP_446259                837 aa            linear   ROD 27-APR-2025
DEFINITION  GRIP1-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_446259
VERSION     NP_446259.1
DBSOURCE    REFSEQ: accession NM_053807.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Mele,M., De Luca,P., Santos,A.R., Vieira,M., Salazar,I.L.,
            Pinheiro,P.S. and Duarte,C.B.
  TITLE     GRASP1 ubiquitination regulates AMPA receptor surface expression
            and synaptic activity in cultured hippocampal neurons
  JOURNAL   FASEB J 35 (8), e21763 (2021)
   PUBMED   34245609
  REMARK    GeneRIF: GRASP1 ubiquitination regulates AMPA receptor surface
            expression and synaptic activity in cultured hippocampal neurons.
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Hoogenraad,C.C., Popa,I., Futai,K., Martinez-Sanchez,E., Wulf,P.S.,
            van Vlijmen,T., Dortland,B.R., Oorschot,V., Govers,R., Monti,M.,
            Heck,A.J., Sheng,M., Klumperman,J., Rehmann,H., Jaarsma,D.,
            Kapitein,L.C. and van der Sluijs,P.
  TITLE     Neuron specific Rab4 effector GRASP-1 coordinates membrane
            specialization and maturation of recycling endosomes
  JOURNAL   PLoS Biol 8 (1), e1000283 (2010)
   PUBMED   20098723
  REMARK    Erratum:[PLoS Biol. 2010;8(9)
            doi:10.1371/annotation/b17dfb99-8809-4c5a-86c2-c2a0f7ca7f5e.
            Sanchez-Martinez, Emma [corrected to Martinez-Sanchez, Emma]]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Ye,B., Liao,D., Zhang,X., Zhang,P., Dong,H. and Huganir,R.L.
  TITLE     GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP
            complex
  JOURNAL   Neuron 26 (3), 603-617 (2000)
   PUBMED   10896157
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1 and BQ780554.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF274057.2, SRR26360176.768612.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..837
                     /product="GRIP1-associated protein 1"
                     /note="GRASP-1; GRIP-associated protein 1"
                     /calculated_mol_wt=95943
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q4V328; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Region          38..>337
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          161..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Region          <193..>717
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          555..577
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            594..595
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:10896157; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Region          647..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4V328; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4V328; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Region          677..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4V328; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JHZ4.1)"
     CDS             1..837
                     /gene="Gripap1"
                     /gene_synonym="Grasp1"
                     /coded_by="NM_053807.2:20..2533"
                     /db_xref="GeneID:116493"
                     /db_xref="RGD:621249"
ORIGIN      
        1 maqalseeef qrmqtqllel rtnnyqlsde lrkngvelss lrqkvayldk efskaqkals
       61 kskkaqevev llsekemlqa klhsqeedfr lqnstlmaef sklcsqleql elenrqlkeg
      121 vpgaagphvd gellrlqaen talqknmaal qerygkeavr psavsegqgd ppgdvlpisl
      181 spmplaevel kwemereekk llweqlqgle sskqaetsrl qeelaklsek lkkkqesfcr
      241 lqteketlfn dsrnkieelq qrkeadlkaq lartqklqqe leaanqslae lrdqrqgerl
      301 ehaaalralq dqvssqsada qeqvegllae nnalrtslaa leqiqtaktq elnmlreqnt
      361 elaaelkhrq adyeelmgqk ddlnsqlqes lransrlleq lqemgqekeq liqdlqeark
      421 saekrkvmld elametlqek sqhkeelgav rlrhekemlg vraryerelr elhedkkrqe
      481 eelrgqiree kartrelenl qhtveelqaq vhsmdgakgw ferrlkeaee sllqqeqeqe
      541 etlkqcreqh aaelkgkeee lqnvrdqlqq aqeerdghvk tisnlkqevk dtvdgqrile
      601 kkgsavlkdl krqlhlerkr adklqerlqe iltnsksrtg leelvlsemn spsrtqtgds
      661 ssvssfsyre ilkekessai parslssspq aqpprpaels deevaelfqr laetqqekwm
      721 leekvkhlev ssasmaedlc rksaiietyv mdsridvsva aghtdrsglg svlrdlvkpg
      781 denlremnkk lqnmleeqlt knmhlhkdme vlsqeivrls kecvgspdpd lepgean
//
LOCUS       NP_758833                545 aa            linear   ROD 27-APR-2025
DEFINITION  zona pellucida sperm-binding protein 4 precursor [Rattus
            norvegicus].
ACCESSION   NP_758833
VERSION     NP_758833.2
DBSOURCE    REFSEQ: accession NM_172330.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Zeng,M.H., Wang,Y., Huang,H.L., Quan,R.P., Yang,J.T., Guo,D.,
            Sun,Y., Lv,C., Li,T.Y., Wang,L., Tan,H.J., Long,P.P., Deng,H.W. and
            Xiao,H.M.
  TITLE     Zp4 is completely dispensable for fertility in female ratsdagger
  JOURNAL   Biol Reprod 104 (6), 1282-1291 (2021)
   PUBMED   33709118
  REMARK    GeneRIF: Zp4 is completely dispensable for fertility in female
            ratsdagger.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Lv,C., Huang,H.L., Yi,D.J., Peng,T.L., Tan,H.J., Quan,R.P.,
            Deng,H.W. and Xiao,H.M.
  TITLE     Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the zona
            pellucida, resulting in zona absence and female infertility in
            ratsdagger
  JOURNAL   Biol Reprod 104 (6), 1262-1270 (2021)
   PUBMED   33624742
  REMARK    GeneRIF: Mutant Zp1 impedes incorporation of ZP3 and ZP4 in the
            zona pellucida, resulting in zona absence and female infertility in
            ratsdagger.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Dai,C., Hu,L., Gong,F., Tan,Y., Cai,S., Zhang,S., Dai,J., Lu,C.,
            Chen,J., Chen,Y., Lu,G., Du,J. and Lin,G.
  TITLE     ZP2 pathogenic variants cause in vitro fertilization failure and
            female infertility
  JOURNAL   Genet Med 21 (2), 431-440 (2019)
   PUBMED   29895852
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Louros,N.N., Chrysina,E.D., Baltatzis,G.E., Patsouris,E.S.,
            Hamodrakas,S.J. and Iconomidou,V.A.
  TITLE     A common 'aggregation-prone' interface possibly participates in the
            self-assembly of human zona pellucida proteins
  JOURNAL   FEBS Lett 590 (5), 619-630 (2016)
   PUBMED   26879157
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Jose,O., Hernandez-Hernandez,O., Chirinos,M.,
            Gonzalez-Gonzalez,M.E., Larrea,F., Almanza,A., Felix,R., Darszon,A.
            and Trevino,C.L.
  TITLE     Recombinant human ZP3-induced sperm acrosome reaction: evidence for
            the involvement of T- and L-type voltage-gated calcium channels
  JOURNAL   Biochem Biophys Res Commun 395 (4), 530-534 (2010)
   PUBMED   20394732
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Choudhury,S., Ganguly,A., Chakrabarti,K., Sharma,R.K. and
            Gupta,S.K.
  TITLE     DNA vaccine encoding chimeric protein encompassing epitopes of
            human ZP3 and ZP4: immunogenicity and characterization of
            antibodies
  JOURNAL   J Reprod Immunol 79 (2), 137-147 (2009)
   PUBMED   19004505
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Chiu,P.C., Wong,B.S., Chung,M.K., Lam,K.K., Pang,R.T., Lee,K.F.,
            Sumitro,S.B., Gupta,S.K. and Yeung,W.S.
  TITLE     Effects of native human zona pellucida glycoproteins 3 and 4 on
            acrosome reaction and zona pellucida binding of human spermatozoa
  JOURNAL   Biol Reprod 79 (5), 869-877 (2008)
   PUBMED   18667750
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Furlong,L.I., Harris,J.D. and Vazquez-Levin,M.H.
  TITLE     Binding of recombinant human proacrosin/acrosin to zona pellucida
            (ZP) glycoproteins. I. Studies with recombinant human ZPA, ZPB, and
            ZPC
  JOURNAL   Fertil Steril 83 (6), 1780-1790 (2005)
   PUBMED   15950651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Sep 13, 2012 this sequence version replaced NP_758833.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF456325.1, SRR26643429.52747.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..545
                     /product="zona pellucida sperm-binding protein 4
                     precursor"
                     /note="zona pellucida sperm-binding protein 4; zona
                     pellucida protein B; zona pellucida 4; zona pellucida B
                     glycoprotein"
                     /calculated_mol_wt=56718
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3148
     mat_peptide     29..471
                     /product="Zona pellucida sperm-binding protein 4.
                     /id=PRO_0000041733"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH34.1)"
                     /calculated_mol_wt=48539
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Region          150..191
                     /region_name="Trefoil"
                     /note="Trefoil (P-type) domain; pfam00088"
                     /db_xref="CDD:459666"
     Site            order(164,186..187)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(179,186)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     Region          198..469
                     /region_name="Zona_pellucida"
                     /note="Zona pellucida-like domain; pfam00100"
                     /db_xref="CDD:459673"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Site            312
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Site            483
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CH34.1)"
     Site            519..539
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CH34.1)"
     CDS             1..545
                     /gene="Zp4"
                     /gene_synonym="Zp-4"
                     /coded_by="NM_172330.3:26..1663"
                     /db_xref="GeneID:282833"
                     /db_xref="RGD:628708"
ORIGIN      
        1 marqalrstl wllpsillcf pfclplsgqh vtelpgvlhc glqsfqfavn lsleaespvl
       61 ttwdsqglph rlkndsdcgt wvmdspdgfl vleasysgcy vtlegshyim tvgvqeadva
      121 ghvagtrqrl ltcplalqgk apdtpsakvc spvpvkerlp casstisrgd ceelgccyss
      181 eeegadscyy gntvtshctk eghfsiavsr dvtspplrld slrlgfrnit tgcdpvmkts
      241 tfvlfqfplt scgttqritg dqamyenelv airdvqawgr ssitrdsnfr lrvsctysih
      301 simspvnmqv wtlppplpkt qpgplslelq iaqdknyssy ygtdayplvk flqdpiyvev
      361 silhrtdpsl sllleqcwat pgsnpfhqpq wpilvkgcpy agdnyqtkri pvqkasdvfp
      421 shhqrfsist fsfmsagrek qvlggqvylh csasvcqpag mpsctvicpa srrrrksely
      481 fdnstsissk gpvillqatk dpavmlhkhs gthadsptlw vmglsasmvi tgvlvvsyla
      541 trkqr
//
LOCUS       NP_113892                355 aa            linear   ROD 27-APR-2025
DEFINITION  syntaxin-5 [Rattus norvegicus].
ACCESSION   NP_113892
VERSION     NP_113892.2
DBSOURCE    REFSEQ: accession NM_031704.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Hernandez-Zimbron,L.F. and Rivas-Arancibia,S.
  TITLE     Syntaxin 5 Overexpression and beta-Amyloid 1-42 Accumulation in
            Endoplasmic Reticulum of Hippocampal Cells in Rat Brain Induced by
            Ozone Exposure
  JOURNAL   Biomed Res Int 2016, 2125643 (2016)
   PUBMED   27366738
  REMARK    GeneRIF: O3 exposure (0.25 ppm) induced a significant increase of
            Syntaxin 5 and accumulation of betaA42 peptide in the reticulum in
            cells of the dentate gyrus
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Suga,K., Saito,A. and Akagawa,K.
  TITLE     ER stress response in NG108-15 cells involves upregulation of
            syntaxin 5 expression and reduced amyloid beta peptide secretion
  JOURNAL   Exp Cell Res 332 (1), 11-23 (2015)
   PUBMED   25596448
  REMARK    GeneRIF: Syx5 plays important roles in beta-amyloid precursor
            protein processing and in the endoplasmic reticulum stress
            response.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Renna,M., Schaffner,C., Winslow,A.R., Menzies,F.M., Peden,A.A.,
            Floto,R.A. and Rubinsztein,D.C.
  TITLE     Autophagic substrate clearance requires activity of the syntaxin-5
            SNARE complex
  JOURNAL   J Cell Sci 124 (Pt 3), 469-482 (2011)
   PUBMED   21242315
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Laufman,O., Kedan,A., Hong,W. and Lev,S.
  TITLE     Direct interaction between the COG complex and the SM protein,
            Sly1, is required for Golgi SNARE pairing
  JOURNAL   EMBO J 28 (14), 2006-2017 (2009)
   PUBMED   19536132
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Rabouille,C., Kondo,H., Newman,R., Hui,N., Freemont,P. and
            Warren,G.
  TITLE     Syntaxin 5 is a common component of the NSF- and p97-mediated
            reassembly pathways of Golgi cisternae from mitotic Golgi fragments
            in vitro
  JOURNAL   Cell 92 (5), 603-610 (1998)
   PUBMED   9506515
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Tang,B.L., Low,D.Y., Lee,S.S., Tan,A.E. and Hong,W.
  TITLE     Molecular cloning and localization of human syntaxin 16, a member
            of the syntaxin family of SNARE proteins
  JOURNAL   Biochem Biophys Res Commun 242 (3), 673-679 (1998)
   PUBMED   9464276
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Okamoto,M. and Sudhof,T.C.
  TITLE     Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
  JOURNAL   J Biol Chem 272 (50), 31459-31464 (1997)
   PUBMED   9395480
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Hui,N., Nakamura,N., Sonnichsen,B., Shima,D.T., Nilsson,T. and
            Warren,G.
  TITLE     An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic
            reticulum retrieval signal
  JOURNAL   Mol Biol Cell 8 (9), 1777-1787 (1997)
   PUBMED   9307973
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Bennett,M.K., Garcia-Arraras,J.E., Elferink,L.A., Peterson,K.,
            Fleming,A.M., Hazuka,C.D. and Scheller,R.H.
  TITLE     The syntaxin family of vesicular transport receptors
  JOURNAL   Cell 74 (5), 863-873 (1993)
   PUBMED   7690687
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC127489.1.
            
            On Apr 9, 2013 this sequence version replaced NP_113892.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127489.1, SRR8487227.35556.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..355
                     /product="syntaxin-5"
                     /note="syntaxin 5a"
                     /calculated_mol_wt=39620
     Region          52..74
                     /region_name="Syntaxin-5_N"
                     /note="Syntaxin-5 N-terminal, Sly1p-binding domain;
                     pfam11416"
                     /db_xref="CDD:463276"
     Region          80..324
                     /region_name="COG5325"
                     /note="t-SNARE complex subunit, syntaxin [Intracellular
                     trafficking and secretion]"
                     /db_xref="CDD:227635"
     Region          245..247
                     /region_name="IxM motif, signal for cargo packaging into
                     COPII-coated vesicles.
                     /evidence=ECO:0000250|UniProtKB:Q13190"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08851.2)"
     Region          266..338
                     /region_name="SNARE_syntaxin5"
                     /note="SNARE motif of syntaxin 5; cd15844"
                     /db_xref="CDD:277197"
     Site            order(267,269..270,272..277,279..281,283..284,286..288,
                     290..291,293..295,297..298,300..305,307..312,314..319,
                     321..323)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277197"
     Site            297
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277197"
     Site            334..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08851.2)"
     CDS             1..355
                     /gene="Stx5"
                     /gene_synonym="Stx5a"
                     /coded_by="NM_031704.2:138..1205"
                     /db_xref="GeneID:65134"
                     /db_xref="RGD:68426"
ORIGIN      
        1 miprkrygsk ntdqgvylgl sktqvlspat ainsssdiap lptpvalvps ppdtmscrdr
       61 tqeflsacks lqsrqngiqt nkpalhatrq cseftlmarr igkdlsntfa klekltilak
      121 rkslfddkav eieeltyiik qdinslnkqi aqlqdfvrak gsqsgrhlqt hsntivvslq
      181 sklasmsndf ksvlevrten lkqqrnrreq fsrapvsalp lapnnlgggp ivlggesras
      241 rdvaidmmdp rtsqqlqlid eqdsyiqsra dtmqniesti velgsifqql ahmvkeqeet
      301 iqridenvlg aqldveaahs eilkyfqsvt snrwlmvkif lilivffiif vvfla
//
LOCUS       NP_001159368             131 aa            linear   ROD 27-APR-2025
DEFINITION  interferon alpha responsive protein isoform a [Rattus norvegicus].
ACCESSION   NP_001159368
VERSION     NP_001159368.1
DBSOURCE    REFSEQ: accession NM_001165896.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Rose,A.E., Zhao,C., Turner,E.M., Steyer,A.M. and Schlieker,C.
  TITLE     Arresting a Torsin ATPase reshapes the endoplasmic reticulum
  JOURNAL   J Biol Chem 289 (1), 552-564 (2014)
   PUBMED   24275647
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Zhao,C., Brown,R.S., Chase,A.R., Eisele,M.R. and Schlieker,C.
  TITLE     Regulation of Torsin ATPases by LAP1 and LULL1
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), E1545-E1554 (2013)
   PUBMED   23569223
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Vander Heyden,A.B., Naismith,T.V., Snapp,E.L., Hodzic,D. and
            Hanson,P.I.
  TITLE     LULL1 retargets TorsinA to the nuclear envelope revealing an
            activity that is impaired by the DYT1 dystonia mutation
  JOURNAL   Mol Biol Cell 20 (11), 2661-2672 (2009)
   PUBMED   19339278
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Goodchild,R.E. and Dauer,W.T.
  TITLE     The AAA+ protein torsinA interacts with a conserved domain present
            in LAP1 and a novel ER protein
  JOURNAL   J Cell Biol 168 (6), 855-862 (2005)
   PUBMED   15767459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO565924.1, CV107022.1, CB804669.1, EV767100.1 and DV728294.1.
            
            Transcript Variant: This variant (2) shares a portion of its 5'
            UTR, but no coding sequence with variant 1. Variant 2 encodes a
            shorter protein (interferon alpha responsive protein), which is
            distinct from torsin-1A-interacting protein 2. Variants 2 and 3
            encode the same protein, isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CO565924.1, FQ225160.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..131
                     /product="interferon alpha responsive protein isoform a"
                     /note="interferon alpha responsive protein; torsin A
                     interacting protein 2"
                     /calculated_mol_wt=15147
     CDS             1..131
                     /gene="Tor1aip2"
                     /coded_by="NM_001165896.1:744..1139"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:304881"
                     /db_xref="RGD:735059"
ORIGIN      
        1 mfsdnshcpd cgqqwfpsle lghwlyqtel venecyqvfl drinradycp ecypdnpanr
       61 slvlpwsfpl ewapqnltrw tfekachpfl lgpplvrkki hdsrvagfnp alqlilsrtd
      121 ktlnkklgqs k
//
LOCUS       NP_598237                371 aa            linear   ROD 27-APR-2025
DEFINITION  beta-1,3-galactosyltransferase 4 precursor [Rattus norvegicus].
ACCESSION   NP_598237
VERSION     NP_598237.2
DBSOURCE    REFSEQ: accession NM_133553.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Amado,M., Almeida,R., Carneiro,F., Levery,S.B., Holmes,E.H.,
            Nomoto,M., Hollingsworth,M.A., Hassan,H., Schwientek,T.,
            Nielsen,P.A., Bennett,E.P. and Clausen,H.
  TITLE     A family of human beta3-galactosyltransferases. Characterization of
            four members of a
            UDP-galactose:beta-N-acetyl-glucosamine/beta-nacetyl-galactosamine
            beta-1,3-galactosyltransferase family
  JOURNAL   J Biol Chem 273 (21), 12770-12778 (1998)
   PUBMED   9582303
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Miyazaki,H., Fukumoto,S., Okada,M., Hasegawa,T. and Furukawa,K.
  TITLE     Expression cloning of rat cDNA encoding UDP-galactose:GD2
            beta1,3-galactosyltransferase that determines the expression of
            GD1b/GM1/GA1
  JOURNAL   J Biol Chem 272 (40), 24794-24799 (1997)
   PUBMED   9312075
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126083.1 and BX883042.1.
            
            On Sep 12, 2009 this sequence version replaced NP_598237.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC126083.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..371
                     /product="beta-1,3-galactosyltransferase 4 precursor"
                     /EC_number="2.4.1.62"
                     /note="GAL-T2; b3Gal-T4; beta3Gal-T4; beta-1,3-GalTase 4;
                     ganglioside galactosyltransferase;
                     UDP-galactose:beta-N-acetyl-galactosamine-beta-1,
                     3-galactosyltransferase; beta3GalT4; UDP-Gal:betaGlcNAc
                     beta 1,3-galactosyltransferase, polypeptide 4"
                     /calculated_mol_wt=38020
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3210
     Site            5..25
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88178.1)"
     Region          85..301
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; pfam01762"
                     /db_xref="CDD:426415"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88178.1)"
     Region          187..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88178.1)"
     CDS             1..371
                     /gene="B3galt4"
                     /coded_by="NM_133553.2:224..1339"
                     /db_xref="GeneID:171079"
                     /db_xref="RGD:620328"
ORIGIN      
        1 mplslfrrll lavlllviiw tlfgpsglge ellslslasl lpapaspgpp lalprllipn
       61 pqacggsgpp pfllilvcta pehlnqrnai rgswgairea rgfrvqtlfl lgepmgqqfa
      121 dlasesaaqg dvlqasfqds yrnltlktlt glnwvnkycp maryilktdd dvyvnvpelv
      181 seliqrggps eqwqkgkepq eettavhkeh kgqavpllyl grvhwrvrpt rtpesrhhvs
      241 eelwpenwgp fppyasgtgy vlsisavqli lkvasrapyl pledvfvgvs arrgglapth
      301 cvklagathy pldrccygkf lltshkvdpw kmqeawklvr glngrrtepf cswlqgflgt
      361 lrcrfiawln s
//
LOCUS       NP_001258035             928 aa            linear   ROD 27-APR-2025
DEFINITION  G-protein coupled receptor family C group 6 member A precursor
            [Rattus norvegicus].
ACCESSION   NP_001258035 XP_228164
VERSION     NP_001258035.1
DBSOURCE    REFSEQ: accession NM_001271106.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Jacobsen,S.E., Ammendrup-Johnsen,I., Jansen,A.M., Gether,U.,
            Madsen,K.L. and Brauner-Osborne,H.
  TITLE     The GPRC6A receptor displays constitutive internalization and
            sorting to the slow recycling pathway
  JOURNAL   J Biol Chem 292 (17), 6910-6926 (2017)
   PUBMED   28280242
  REMARK    GeneRIF: GPRC6A predominantly undergoes constitutive
            internalization with the early endosome marker Rab5 and the long
            loop recycling endosome marker Rab11 and to a much lesser extent
            with the late endosome marker Rab7
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Wellendorph,P., Burhenne,N., Christiansen,B., Walter,B., Schmale,H.
            and Brauner-Osborne,H.
  TITLE     The rat GPRC6A: cloning and characterization
  JOURNAL   Gene 396 (2), 257-267 (2007)
   PUBMED   17478059
  REMARK    GeneRIF: cloning and characterization of rat GPRC6A
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Pi,M., Faber,P., Ekema,G., Jackson,P.D., Ting,A., Wang,N.,
            Fontilla-Poole,M., Mays,R.W., Brunden,K.R., Harrington,J.J. and
            Quarles,L.D.
  TITLE     Identification of a novel extracellular cation-sensing
            G-protein-coupled receptor
  JOURNAL   J Biol Chem 280 (48), 40201-40209 (2005)
   PUBMED   16199532
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Wellendorph,P. and Brauner-Osborne,H.
  TITLE     Molecular cloning, expression, and sequence analysis of GPRC6A, a
            novel family C G-protein-coupled receptor
  JOURNAL   Gene 335, 37-46 (2004)
   PUBMED   15194188
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Aug 31, 2012 this sequence version replaced XP_228164.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ535460.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..928
                     /product="G-protein coupled receptor family C group 6
                     member A precursor"
                     /note="G-protein coupled receptor family C group 6 member
                     A"
                     /calculated_mol_wt=102104
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2268
     mat_peptide     21..928
                     /product="G-protein coupled receptor family C group 6
                     member A. /id=PRO_0000043198"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
                     /calculated_mol_wt=102104
     Region          37..506
                     /region_name="PBP1_GPC6A-like"
                     /note="ligand-binding domain of the promiscuous
                     L-alpha-amino acid receptor GPRC6A which is a
                     broad-spectrum amino acid-sensing receptor; cd06361"
                     /db_xref="CDD:380584"
     Site            order(69,170..171,415)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380584"
     Site            order(107,110..111,114,157,161,183,237,501..502,506)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380584"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          520..572
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Site            555
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q70VB1.1)"
     Site            595..615
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          604..841
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          630..651
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320408"
     Site            631..651
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          660..682
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320408"
     Site            670..690
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          706..722
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320408"
     Site            707..727
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          748..771
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320408"
     Site            751..771
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          783..805
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320408"
     Site            785..805
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     Region          810..835
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320408"
     Site            813..833
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70VB1.1)"
     CDS             1..928
                     /gene="Gprc6a"
                     /coded_by="NM_001271106.1:25..2811"
                     /db_xref="GeneID:294394"
                     /db_xref="RGD:735077"
ORIGIN      
        1 malsfvfitc fmilldtsqs chtpddfvai tspghimigg lfaihekmls sddhprqpqi
       61 qkcvgfeisv flqtlamihs ieminnssll sgvklgyeiy dtctevtaam aatlrflskf
      121 ncsretvifq cdyssyvprv kaiigagyse ismavsrmln lqlmpqvsye staeilsdki
      181 rfpsflrtvp sdfyqtkama hlirqsgwnw vgaittdddy grlalntfai qaaennvcia
      241 fkevlpafls dntievrinq tlekiiaeaq vnvivvflrk fhvfnlfnka ierkiskiwi
      301 asdnwstaak iitipnvkkl gkvvgftfrr gnmssfhsfl qtlhmypsdn nkplhefaml
      361 fsackhikdg dlsqcisnys qatwtydttk tiethlfkrn dflwhytepg lihsiqlavl
      421 alghairdlc qdrdcqkpna fqpwellavl knvtftdgkn sfhfdahgdl ntgyevvlwk
      481 etnglmtvtk maeydlqhdv fittnqetkh efrklkqils kcskecipgq mkkatgsqhs
      541 ccyecvncpe nhysnetdmd hclvcnneth wapvrstmcf ekeveyldwd dslalllial
      601 sllgiafvla vgiiftrnlk tpvvkssggl vvcyvmlach alnfastgff igepqdftck
      661 trqtlfgvsf tlcvsciltk slkillafsf dptlktflkc lyrpvpivlt ctgiqvvict
      721 lwlvlaaptv eentslprvi ileceegsal afgtmlgyia vlaficfvfa fkgrklpeny
      781 neakfltfgm liyfiawitf ipvyattfgk ylpaveiivi lisnygilcc tffpkcyiil
      841 ckqktntksv flqmvynysa hsvdslalsh vsldsashst attnprpgnk taacqnykhl
      901 pvqvlahtgm ektmhasktl hqkrsssi
//
LOCUS       NP_001258032            2414 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor corepressor 1 [Rattus norvegicus].
ACCESSION   NP_001258032 XP_001077495 XP_577103
VERSION     NP_001258032.1
DBSOURCE    REFSEQ: accession NM_001271103.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2414)
  AUTHORS   Hong-Wei,G., Lan,L., De-Guo,X., Zhong-Hao,L., Peng,R.,
            Zhi-Qiang,L., Guo-Qiang,S. and Ming-Zhi,G.
  TITLE     NCoR negatively regulates adipogenic differentiation of mesenchymal
            stem cells
  JOURNAL   In Vitro Cell Dev Biol Anim 51 (7), 749-758 (2015)
   PUBMED   26019118
  REMARK    GeneRIF: NCoR negatively regulates adipogenic differentiation of
            mesenchymal stem cells.
REFERENCE   2  (residues 1 to 2414)
  AUTHORS   Aninye,I.O., Matsumoto,S., Sidhaye,A.R. and Wondisford,F.E.
  TITLE     Circadian regulation of Tshb gene expression by Rev-Erbalpha
            (NR1D1) and nuclear corepressor 1 (NCOR1)
  JOURNAL   J Biol Chem 289 (24), 17070-17077 (2014)
   PUBMED   24794873
REFERENCE   3  (residues 1 to 2414)
  AUTHORS   Vella,K.R., Ramadoss,P., Costa-E-Sousa,R.H., Astapova,I., Ye,F.D.,
            Holtz,K.A., Harris,J.C. and Hollenberg,A.N.
  TITLE     Thyroid hormone signaling in vivo requires a balance between
            coactivators and corepressors
  JOURNAL   Mol Cell Biol 34 (9), 1564-1575 (2014)
   PUBMED   24550004
REFERENCE   4  (residues 1 to 2414)
  AUTHORS   Soriano,F.X., Chawla,S., Skehel,P. and Hardingham,G.E.
  TITLE     SMRT-mediated co-shuttling enables export of class IIa HDACs
            independent of their CaM kinase phosphorylation sites
  JOURNAL   J Neurochem 124 (1), 26-35 (2013)
   PUBMED   23083128
  REMARK    GeneRIF: SMRT-mediated co-shuttling enables export of class IIa
            HDACs independent of their CaM kinase phosphorylation sites.
REFERENCE   5  (residues 1 to 2414)
  AUTHORS   Qu,F., Wang,F.F., Yin,R., Ding,G.L., El-Prince,M., Gao,Q.,
            Shi,B.W., Pan,H.H., Huang,Y.T., Jin,M., Leung,P.C., Sheng,J.Z. and
            Huang,H.F.
  TITLE     A molecular mechanism underlying ovarian dysfunction of polycystic
            ovary syndrome: hyperandrogenism induces epigenetic alterations in
            the granulosa cells
  JOURNAL   J Mol Med (Berl) 90 (8), 911-923 (2012)
   PUBMED   22349439
  REMARK    GeneRIF: PCOS rat models also showed alterations of PPARG1, NCOR1,
            and HDAC3 mRNA expression and methylation changes of PPARG1 and
            NCOR1, consistent with the results from humans.
REFERENCE   6  (residues 1 to 2414)
  AUTHORS   Harding,H.P., Atkins,G.B., Jaffe,A.B., Seo,W.J. and Lazar,M.A.
  TITLE     Transcriptional activation and repression by RORalpha, an orphan
            nuclear receptor required for cerebellar development
  JOURNAL   Mol Endocrinol 11 (11), 1737-1746 (1997)
   PUBMED   9328355
REFERENCE   7  (residues 1 to 2414)
  AUTHORS   Heinzel,T., Lavinsky,R.M., Mullen,T.M., Soderstrom,M.,
            Laherty,C.D., Torchia,J., Yang,W.M., Brard,G., Ngo,S.D.,
            Davie,J.R., Seto,E., Eisenman,R.N., Rose,D.W., Glass,C.K. and
            Rosenfeld,M.G.
  TITLE     A complex containing N-CoR, mSin3 and histone deacetylase mediates
            transcriptional repression
  JOURNAL   Nature 387 (6628), 43-48 (1997)
   PUBMED   9139820
REFERENCE   8  (residues 1 to 2414)
  AUTHORS   Seol,W., Mahon,M.J., Lee,Y.K. and Moore,D.D.
  TITLE     Two receptor interacting domains in the nuclear hormone receptor
            corepressor RIP13/N-CoR
  JOURNAL   Mol Endocrinol 10 (12), 1646-1655 (1996)
   PUBMED   8961273
REFERENCE   9  (residues 1 to 2414)
  AUTHORS   Horlein,A.J., Naar,A.M., Heinzel,T., Torchia,J., Gloss,B.,
            Kurokawa,R., Ryan,A., Kamei,Y., Soderstrom,M., Glass,C.K. et al.
  TITLE     Ligand-independent repression by the thyroid hormone receptor
            mediated by a nuclear receptor co-repressor
  JOURNAL   Nature 377 (6548), 397-404 (1995)
   PUBMED   7566114
REFERENCE   10 (residues 1 to 2414)
  AUTHORS   Seol,W., Choi,H.S. and Moore,D.D.
  TITLE     Isolation of proteins that interact specifically with the retinoid
            X receptor: two novel orphan receptors
  JOURNAL   Mol Endocrinol 9 (1), 72-85 (1995)
   PUBMED   7760852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_577103.4, XP_001077495.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2414
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q23"
     Protein         1..2414
                     /product="nuclear receptor corepressor 1"
                     /note="N-CoR; N-CoR1; N-Cor/SMRT corepressor, Rip13; NCoR"
                     /calculated_mol_wt=266241
     Region          150..239
                     /region_name="GPS2_interact"
                     /note="G-protein pathway suppressor 2-interacting domain;
                     pfam15784"
                     /db_xref="CDD:464868"
     Region          441..483
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(441,470..471,473..474,476..478,480..482)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          <708..874
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Region          <1943..>2128
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     CDS             1..2414
                     /gene="Ncor1"
                     /gene_synonym="Rxrip13"
                     /coded_by="NM_001271103.1:230..7474"
                     /db_xref="GeneID:54299"
                     /db_xref="RGD:3612"
ORIGIN      
        1 msssgyppnq gafsteqsry psqsvqytfp strhqqefav pdyrsshiev sqasqllqqq
       61 qqqqqlrrrp sllsefhpgs drpqerrtgy eqfhsgpspv dhdsleskrp rlepvsdahf
      121 qrvsaavlpl vhtlpeglra sadakkdsaf ggkheapssp lagqpcgddq naspsklske
      181 eliqsmdrvd reiakveqqi lklkkkqqql eeeaakppep ekpvspppve qkhrsivqii
      241 ydenrkkaee ahkifeglgp kvelplynqp sdtkvyheni ktnqvmrkkl ilffkrrnha
      301 rkqreqkicq rydqlmeawe kkvdriennp rrkakesktr eyyekqfpei rkqreqqerf
      361 qrvgqrgagl satiarsehe iseiidglse qennekqmrq lsvippmmfd aeqrrvkfin
      421 mnglmedpmk vykdrqfmnv wtdhekeifk dkfiqhpknf gliasylerk svpdcvlyyy
      481 ltkknenyka lvrrnygkrr grnqqiarps qeekveekee dkaekmekke eekkddeekd
      541 ekeeskettk ekdrteatae eteereqvtp rgrktansqg rrkgritrsm tseaaaasaa
      601 aaateepppp lppppepvst epvetsrwte eemevakkgn iqqciiynsa srkpreerdv
      661 sqcesvastv saqedediea sneeenpeds egaenssdte sapspspvea akssedssen
      721 aasrgntepv aeleattdpa pcaspssavp ttkpaesesv eaqvtdsasv etaepmdvdh
      781 eecgaqgssv ldppaptkad svdpeiqvpe ntaskgegda kdrdlesase kteardedlv
      841 vaeqmqrpep qsdndssatc sadedvdgep erqrvfpmda kpsllnppgs ilisspikpn
      901 pldlpqlqhr aavippmvsc tpcnipigtp vsgyalyqrh ikamhesall eeqrqrqeqi
      961 dlecrsstsp cgtskspnre wevlqpaphq vitnlpegvr lpttrptrpp pplipssktt
     1021 vasekpsfim ggsisqgtpg tyltshsqay tpeaakpsvg sislglprqq estksaplty
     1081 ikqeefsprs qnsqpegllv raqhegvvrg tagavqegsi trgtpaskis vesisslrgs
     1141 itqgtpalpq agiptealvk gpvsrmpiee sspekvreea askghviyeg ksghilsydn
     1201 iknaregtrs prtahemslk rsyesvegnv kqgmsmresp vsaapleert vlsgsimqgt
     1261 prataesfed glkypkqikr esppsrafeg aitkgkpydg ittikemgrs iheiprqdil
     1321 tqesrktpev vqstrpiieg sisqgtpikf dnnsgqsaik hnvkslitgp sklprgmlei
     1381 vpenikvver gkyedvkage pvrprhtsvv ssgpsvlrst lheapkaqls pgiyddssar
     1441 rtpvsyqnti srgspmmnrt sdgsssktts herksaltpt qresvpaksp vpavdsvvsh
     1501 spfdphhrst tagevyrshl pthldpampf hraldpaaay lfqrqlsptp gypsqyqlya
     1561 mentrqtiln dyitsqqmqv nlrpdvargl spreqplglp ypatrgiidl tnmpptilvp
     1621 haggtstppm drityipgtq itfpprpyna aslspghpth laaaasaere rererekere
     1681 rerererere rerererere rereritaap tdlylrpgse qpgrpgshgy vrspspsvrt
     1741 qetmlqqrps vfqgtngtsv itpldptaql rimplpsggp sisqglpasr yntaadalaa
     1801 lvdaaasapq mdvsktkesk heaarlednv rsrsaavseq qqleqknlev ekrsvqcvct
     1861 ssalpsgkpq phasvvysea gkdkgpppks ryeeelrtrg kttitaanfi dviitrqias
     1921 dkdarergsq ssdsssslss hryeapsdai evispasspa ppqekpqayq pemvkanqae
     1981 nespqqyegp lhhyrsqqgs pspqqqpplp pssqaegmgq vprthrlitl adhicqiitq
     2041 dfarnqvpsq pststfqtsp salsstpvrt kpssryspes qsqtvlhprp gprvspenlv
     2101 dksrgsrpgk spershipse pyepisppqg pavhekqdsm lllsqrgmdp aeqrsdsrsp
     2161 gsisylpsff tklestspmv kskkqeifrk lnssgggdsd maaaqpgtei fnlpavttsg
     2221 avssrshsfa dpasnlgled iirkalmgsf ddkvedhgvv mphpvgvvpg sastsvvtss
     2281 etrrdegdps phsgvckpkl inksnsrksk spipgqnylg terpssvssv hsegdyhrqt
     2341 pgwawedrps stgstqfpyn pltirmlsst pptpiacaps aitqaaphqq sriwerepap
     2401 llsaqyetls dsdd
//
LOCUS       NP_001178572             395 aa            linear   ROD 27-APR-2025
DEFINITION  RNA demethylase ALKBH5 [Rattus norvegicus].
ACCESSION   NP_001178572 XP_220525
VERSION     NP_001178572.1
DBSOURCE    REFSEQ: accession NM_001191643.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Song,K., Cao,Q., Yang,Y., Zuo,Y. and Wu,X.
  TITLE     ALKBH5 modulates bone cancer pain in a rat model by suppressing
            NR2B expression
  JOURNAL   Biotechnol Appl Biochem 71 (5), 1105-1115 (2024)
   PUBMED   38764325
  REMARK    GeneRIF: ALKBH5 modulates bone cancer pain in a rat model by
            suppressing NR2B expression.
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhou,J., Tang,J., Zhang,C., Li,G., Lin,X., Liao,S., Luo,J., Yu,G.,
            Zheng,F., Guo,Z., Shao,W., Hu,H., Xu,L., Wu,S. and Li,H.
  TITLE     ALKBH5 targets ACSL4 mRNA stability to modulate ferroptosis in
            hyperbilirubinemia-induced brain damage
  JOURNAL   Free Radic Biol Med 220, 271-287 (2024)
   PUBMED   38734267
  REMARK    GeneRIF: ALKBH5 targets ACSL4 mRNA stability to modulate
            ferroptosis in hyperbilirubinemia-induced brain damage.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Fan,D., Geng,Q., Wang,B., Wang,X., Xia,Y., Yang,L., Zhang,Q.,
            Deng,T., Xu,Y., Zhao,H., Liu,B., Lu,C., Gu,X. and Xiao,C.
  TITLE     Hypoxia-induced ALKBH5 aggravates synovial aggression and
            inflammation in rheumatoid arthritis by regulating the m6A
            modification of CH25H
  JOURNAL   Clin Immunol 261, 109929 (2024)
   PUBMED   38331303
  REMARK    GeneRIF: Hypoxia-induced ALKBH5 aggravates synovial aggression and
            inflammation in rheumatoid arthritis by regulating the m6A
            modification of CH25H.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Huang,Z., Zhang,Y., Wang,S., Qi,R., Tao,Y., Sun,Y., Jiang,D.,
            Jiang,X. and Tao,J.
  TITLE     FOXD3-mediated transactivation of ALKBH5 promotes neuropathic pain
            via m6A-dependent stabilization of 5-HT3A mRNA in sensory neurons
  JOURNAL   Proc Natl Acad Sci U S A 121 (6), e2312861121 (2024)
   PUBMED   38285939
  REMARK    GeneRIF: FOXD3-mediated transactivation of ALKBH5 promotes
            neuropathic pain via m[6]A-dependent stabilization of 5-HT3A mRNA
            in sensory neurons.
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Kuang,Y., Li,R., Wang,J., Xu,S., Qiu,Q., Lin,S., Liu,D., Shen,C.,
            Liu,Y., Xu,M., Lin,W., Zhang,S., Liang,L., Xu,H. and Xiao,Y.
  TITLE     ALKBH5-Mediated RNA m6 A Methylation Regulates the Migration,
            Invasion, and Proliferation of Rheumatoid Fibroblast-Like
            Synoviocytes
  JOURNAL   Arthritis Rheumatol 76 (2), 192-205 (2024)
   PUBMED   37584615
  REMARK    GeneRIF: ALKBH5-Mediated RNA m[6] A Methylation Regulates the
            Migration, Invasion, and Proliferation of Rheumatoid
            Fibroblast-Like Synoviocytes.
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Zheng,G., Dahl,J.A., Niu,Y., Fedorcsak,P., Huang,C.M., Li,C.J.,
            Vagbo,C.B., Shi,Y., Wang,W.L., Song,S.H., Lu,Z., Bosmans,R.P.,
            Dai,Q., Hao,Y.J., Yang,X., Zhao,W.M., Tong,W.M., Wang,X.J.,
            Bogdan,F., Furu,K., Fu,Y., Jia,G., Zhao,X., Liu,J., Krokan,H.E.,
            Klungland,A., Yang,Y.G. and He,C.
  TITLE     ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism
            and mouse fertility
  JOURNAL   Mol Cell 49 (1), 18-29 (2013)
   PUBMED   23177736
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Thalhammer,A., Bencokova,Z., Poole,R., Loenarz,C., Adam,J.,
            O'Flaherty,L., Schodel,J., Mole,D., Giaslakiotis,K.,
            Schofield,C.J., Hammond,E.M., Ratcliffe,P.J. and Pollard,P.J.
  TITLE     Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent
            oxygenase and a direct target of hypoxia-inducible factor 1alpha
            (HIF-1alpha)
  JOURNAL   PLoS One 6 (1), e16210 (2011)
   PUBMED   21264265
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Simon,G.M. and Cravatt,B.F.
  TITLE     Endocannabinoid biosynthesis proceeding through
            glycerophospho-N-acyl ethanolamine and a role for
            alpha/beta-hydrolase 4 in this pathway
  JOURNAL   J Biol Chem 281 (36), 26465-26472 (2006)
   PUBMED   16818490
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Sep 17, 2011 this sequence version replaced XP_220525.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.36905.1,
                                           SRR26643289.27904.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..395
                     /product="RNA demethylase ALKBH5"
                     /EC_number="1.14.11.53"
                     /note="alkylated DNA repair protein alkB homolog 5;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 5;
                     alkB, alkylation repair homolog 5; AlkB family member 5,
                     RNA demethylase"
                     /calculated_mol_wt=44322
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Region          47..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            133
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Region          <137..271
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     Site            236
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Region          294..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            360
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TSG4; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P6C2; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TSG4; propagated from
                     UniProtKB/Swiss-Prot (D3ZKD3.1)"
     CDS             1..395
                     /gene="Alkbh5"
                     /gene_synonym="RGD1309496"
                     /coded_by="NM_001191643.1:1..1188"
                     /db_xref="GeneID:303193"
                     /db_xref="RGD:1309496"
ORIGIN      
        1 maaasgytdl reklksmtsr dnykagsrea aaaaaaavaa aaaaaaaaep ypvsgttkrk
       61 yqedsdpers dyeehqlqke eearkvksgi rqirlfsqde cskiearide vvsraekgly
      121 nehtvdrapl rnkyffgegy tygaqlqkrg pgqerlyppg dvdeipewvh qlviqklveh
      181 rvipegfvns avindyqpgg civshvdpih iferpivsvs ffsdsalcfg ckfqfkpirv
      241 sepvlslpvr rgsvtvlsgy aadeithcir pqdikerrav iilrktrlda prletkslss
      301 stlppsyasd rlsgntrdpa lkpkrshrka dpdaahrpri lemdkeenrr svllpthrrr
      361 gsfssenywr ksyessedcp eaassptrkv kmrrh
//
LOCUS       NP_001032856             153 aa            linear   ROD 27-APR-2025
DEFINITION  actin-related protein 2/3 complex subunit 5-like protein [Rattus
            norvegicus].
ACCESSION   NP_001032856 XP_216047
VERSION     NP_001032856.2
DBSOURCE    REFSEQ: accession NM_001037767.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Biesemann,C., Gronborg,M., Luquet,E., Wichert,S.P., Bernard,V.,
            Bungers,S.R., Cooper,B., Varoqueaux,F., Li,L., Byrne,J.A.,
            Urlaub,H., Jahn,O., Brose,N. and Herzog,E.
  TITLE     Proteomic screening of glutamatergic mouse brain synaptosomes
            isolated by fluorescence activated sorting
  JOURNAL   EMBO J 33 (2), 157-170 (2014)
   PUBMED   24413018
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM029541.1 and BC127445.1.
            
            On Mar 5, 2010 this sequence version replaced NP_001032856.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127445.1, CO555020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..153
                     /product="actin-related protein 2/3 complex subunit 5-like
                     protein"
                     /note="ARC16-2; arp2/3 complex 16 kDa subunit 2; actin
                     related protein 2/3 complex, subunit 5-like 1"
                     /calculated_mol_wt=16879
     Region          9..151
                     /region_name="P16-Arc"
                     /note="ARP2/3 complex 16 kDa subunit (p16-Arc); pfam04699"
                     /db_xref="CDD:461399"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1L108.2)"
     CDS             1..153
                     /gene="Arpc5l"
                     /gene_synonym="Arpc5l1"
                     /coded_by="NM_001037767.2:60..521"
                     /db_xref="GeneID:296710"
                     /db_xref="RGD:1308867"
ORIGIN      
        1 marntlssrf rrvdidefde nkfvdeheea aaasgepgpd pcevdgllrq gdmlrafhaa
       61 lrnspintkn qavkeraqgi vlkvltnfks seieqavqsl drngidllmk yiykgfekpt
      121 enssavllqw hekalavggl gsiirvltar ktv
//
LOCUS       NP_062049                216 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform a [Rattus norvegicus].
ACCESSION   NP_062049 XP_001067575 XP_001067632 XP_001074337 XP_341342
VERSION     NP_062049.1
DBSOURCE    REFSEQ: accession NM_019176.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1 and BC092646.1.
            
            On or before Oct 23, 2008 this sequence version replaced
            XP_001067575.1, XP_001067632.1, XP_341342.3, XP_001074337.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF026530.1, SRR26360194.2398061.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..216
                     /product="stathmin-4 isoform a"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=25244
     Region          76..210
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     CDS             1..216
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_019176.2:180..830"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyegwcg rqcrrkgqsq rkgsadwrer
       61 reqadtvdln wcvisdmevi elnkctsgqs fevilkppsf dgvpefnasl prrrdpslee
      121 iqkkleaaee rrkyqeaell khlaekrehe reviqkaiee nnnfikmake klaqkmesnk
      181 enreahlaam lerlqekdkh aeevrknkel keeasr
//
LOCUS       NP_997676                123 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein uL29 [Rattus norvegicus].
ACCESSION   NP_997676 XP_216052
VERSION     NP_997676.1
DBSOURCE    REFSEQ: accession NM_212511.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Voorhees,R.M., Fernandez,I.S., Scheres,S.H. and Hegde,R.S.
  TITLE     Structure of the mammalian ribosome-Sec61 complex to 3.4 A
            resolution
  JOURNAL   Cell 157 (7), 1632-1643 (2014)
   PUBMED   24930395
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Shahmolky,N., Lefebvre,D.L., Poon,R., Bai,Y., Sharma,M. and
            Rosen,C.F.
  TITLE     UVB and gamma-radiation induce the expression of mRNAs encoding the
            ribosomal subunit L13A in rat keratinocytes
  JOURNAL   Photochem Photobiol 70 (3), 341-347 (1999)
   PUBMED   10483362
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Chan,Y.L., Devi,K.R., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein S3
  JOURNAL   Arch Biochem Biophys 283 (2), 546-550 (1990)
   PUBMED   2275563
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Suzuki,K., Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L35
  JOURNAL   Biochem Biophys Res Commun 167 (3), 1377-1382 (1990)
   PUBMED   2322279
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Lee,J.C. and Henry,B.
  TITLE     Binding of rat ribosomal proteins to yeast 5.8S ribosomal
            ribonucleic acid
  JOURNAL   Nucleic Acids Res 10 (7), 2199-2207 (1982)
   PUBMED   7045808
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Tsurugi,K., Collatz,E., Todokoro,K. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of 60 S ribosomal subunit proteins L3, L6, L7',
            L8, L10, L15, L17, L18, L19, L23', L25, L27', L28, L29, L31, L32,
            L34, L35, L36, L36', and L37'
  JOURNAL   J Biol Chem 252 (11), 3961-3969 (1977)
   PUBMED   863909
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC058499.1.
            
            On Aug 30, 2004 this sequence version replaced XP_216052.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058499.1, CB314854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132300
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..123
                     /product="large ribosomal subunit protein uL29"
                     /note="60S ribosomal protein L35"
                     /calculated_mol_wt=14421
     Region          8..63
                     /region_name="Ribosomal_L29"
                     /note="Ribosomal L29 protein; pfam00831"
                     /db_xref="CDD:459954"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P42766; propagated from
                     UniProtKB/Swiss-Prot (P17078.3)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42766; propagated from
                     UniProtKB/Swiss-Prot (P17078.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P42766; propagated from
                     UniProtKB/Swiss-Prot (P17078.3)"
     Region          100..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17078.3)"
     CDS             1..123
                     /gene="Rpl35"
                     /coded_by="NM_212511.2:40..411"
                     /db_xref="GeneID:296709"
                     /db_xref="RGD:1303007"
ORIGIN      
        1 makikardlr gkkkeellkq lddlkvelsq lrvakvtgga asklskirvv rksiarvltv
       61 inqtqkenlr kfykgkkykp ldlrpkktra mrrrltkhee klktkkqqrk erlyplrkya
      121 vka
//
LOCUS       NP_647541                434 aa            linear   ROD 27-APR-2025
DEFINITION  gamma-enolase [Rattus norvegicus].
ACCESSION   NP_647541 XP_003750705
VERSION     NP_647541.1
DBSOURCE    REFSEQ: accession NM_139325.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Owusu,L., Xu,C., Chen,H., Liu,G., Zhang,G., Zhang,J., Tang,Z.,
            Sun,Z. and Yi,X.
  TITLE     Gamma-enolase predicts lung damage in severe acute
            pancreatitis-induced acute lung injury
  JOURNAL   J Mol Histol 49 (4), 347-356 (2018)
   PUBMED   29728894
  REMARK    GeneRIF: gamma-enolase may signal and correlate lung tissue damage
            well before obvious physical pathological tissue damage and might
            be a candidate diagnostic and/or prognostic marker.
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Shinohara,Y., Ohtani,T., Konno,A. and Hirai,H.
  TITLE     Viral Vector-Based Evaluation of Regulatory Regions in the
            Neuron-Specific Enolase (NSE) Promoter in Mouse Cerebellum In Vivo
  JOURNAL   Cerebellum 16 (5-6), 913-922 (2017)
   PUBMED   28508170
  REMARK    GeneRIF: Study analyzed the regions that regulate the promoter
            strength and cellular specificity of the 1.8 kb rNSE promoter in
            the cerebellum in vivo. The rNSE promoter was divided into three
            regions (A, B, and C). Our results showed that region C was
            indispensable for the promoter activity in mouse cerebellum and
            served as an interneuron-predominant basal promoter.
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Sawada,Y., Konno,A., Nagaoka,J. and Hirai,H.
  TITLE     Inflammation-induced reversible switch of the neuron-specific
            enolase promoter from Purkinje neurons to Bergmann glia
  JOURNAL   Sci Rep 6, 27758 (2016)
   PUBMED   27291422
  REMARK    GeneRIF: Study showed that the NSE promoter was activated in
            astrocytes, including Bergmann glia (BG), but not Purkinje cells
            (PCs), in the traumatic region of the cerebellar cortex. This PC to
            BG switch was associated with local microglial invasion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Hwang,P.T., Kwon,O.D., Kim,H.J., Kim,B.G., Kim,S.H., Jang,Y.W.,
            Kim,P.K., Han,G.Y. and Kim,C.W.
  TITLE     Hyperglycemia decreases the expression of ATP synthase beta subunit
            and enolase 2 in glomerular epithelial cells
  JOURNAL   Tohoku J Exp Med 231 (1), 45-56 (2013)
   PUBMED   24042457
  REMARK    GeneRIF: Hyperglycemia may impair mitochondrial function and alter
            glycolysis in glomerular epithelial cells by down-regulating the
            expression of ATP synthase beta subunit and enolase 2.
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Sakimura,K., Kushiya,E., Takahashi,Y. and Suzuki,Y.
  TITLE     The structure and expression of neuron-specific enolase gene
  JOURNAL   Gene 60 (1), 103-113 (1987)
   PUBMED   2450052
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Sakimura,K., Kushiya,E., Obinata,M., Odani,S. and Takahashi,Y.
  TITLE     Molecular cloning and the nucleotide sequence of cDNA for
            neuron-specific enolase messenger RNA of rat brain
  JOURNAL   Proc Natl Acad Sci U S A 82 (21), 7453-7457 (1985)
   PUBMED   2865729
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Sakimura,K., Kushiya,E., Obinata,M. and Takahashi,Y.
  TITLE     Molecular cloning and the nucleotide sequence of cDNA to mRNA for
            non-neuronal enolase (alpha alpha enolase) of rat brain and liver
  JOURNAL   Nucleic Acids Res 13 (12), 4365-4378 (1985)
   PUBMED   2989793
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Marangos,P.J., Schmechel,D., Parma,A.M., Clark,R.L. and
            Goodwin,F.K.
  TITLE     Measurement of neuron-specific (NSE) and non-neuronal (NNE)
            isoenzymes of enolase in rat, monkey and human nervous tissue
  JOURNAL   J Neurochem 33 (1), 319-329 (1979)
   PUBMED   110910
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Fletcher,L., Rider,C.C. and Taylor,C.B.
  TITLE     Enolase isoenzymes. III. Chromatographic and immunological
            characteristics of rat brain enolase
  JOURNAL   Biochim Biophys Acta 452 (1), 245-252 (1976)
   PUBMED   990313
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1 and CB615520.1.
            
            On Jun 23, 2021 this sequence version replaced XP_003750705.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF019973.1, M11931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..434
                     /product="gamma-enolase"
                     /EC_number="4.2.1.11"
                     /note="neuron-specific enolase; neural enolase;
                     2-phospho-D-glycerate hydro-lyase; gamma-enolase-like;
                     enolase 2, gamma, neuronal"
                     /calculated_mol_wt=47010
     Region          2..432
                     /region_name="PLN00191"
                     /note="enolase"
                     /db_xref="CDD:215095"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P09104; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P09104; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P17182; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            64
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17183; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17183; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            202
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P17182; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            256
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P06733; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17182; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            343
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17182; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     Site            406
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17182; propagated from
                     UniProtKB/Swiss-Prot (P07323.2)"
     CDS             1..434
                     /gene="Eno2"
                     /gene_synonym="NSE; RNEN3"
                     /coded_by="NM_139325.4:69..1373"
                     /db_xref="GeneID:24334"
                     /db_xref="RGD:2554"
ORIGIN      
        1 msiqkiware ildsrgnptv evdlhtakgl fraavpsgas tgiyealelr dgdkqrylgk
       61 gvlkavdhin stiapaliss glsvveqekl dnlmleldgt enkskfgana ilgvslavck
      121 agaaekdlpl yrhiaqlagn sdlilpvpaf nvinggshag nklamqefmi lpvgaesfrd
      181 amrlgaevyh tlkgvikdky gkdatnvgde ggfapnilen sealelvkea idkagytekm
      241 vigmdvaase fyrdgkydld fkspadpsrc itgdqlgaly qdfvrnypvv siedpfdqdd
      301 waawskftan vgiqivgddl tvtnpkrier aveekacncl llkvnqigsv teaiqackla
      361 qengwgvmvs hrsgetedtf iadlvvglct gqiktgapcr serlakynql mrieeelgee
      421 arfaghnfrn psvl
//
LOCUS       NP_001119845             377 aa            linear   ROD 27-APR-2025
DEFINITION  histone deacetylase 8 [Rattus norvegicus].
ACCESSION   NP_001119845 XP_001070606 XP_343805
VERSION     NP_001119845.2
DBSOURCE    REFSEQ: accession NM_001126373.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wang,P., Mao,Z., Pan,Q., Lu,R., Huang,X., Shang,X., Zhang,R. and
            You,H.
  TITLE     Histone deacetylase-4 and histone deacetylase-8 regulate
            interleukin-1beta-induced cartilage catabolic degradation through
            MAPK/JNK and ERK pathways
  JOURNAL   Int J Mol Med 41 (4), 2117-2127 (2018)
   PUBMED   29393346
  REMARK    GeneRIF: These results suggest that HDAC4 and HDAC8 may serve as
            key upstream mediators of MAPK in regulating the IL1betainduced
            cartilage catabolic and degradation.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Nakayama,T. and Akagawa,K.
  TITLE     Transcription regulation mechanism of the syntaxin 1A gene via
            protein kinase A
  JOURNAL   Biochem J 474 (14), 2465-2473 (2017)
   PUBMED   28559304
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Kee,H.J., Kim,G.R., Lin,M.Q., Choi,S.Y., Ryu,Y., Jin,L., Piao,Z.H.
            and Jeong,M.H.
  TITLE     Expression of Class I and Class II a/b Histone Deacetylase is
            Dysregulated in Hypertensive Animal Models
  JOURNAL   Korean Circ J 47 (3), 392-400 (2017)
   PUBMED   28567090
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Li,R.F., Cao,S.S., Fang,W.J., Song,Y., Luo,X.T., Wang,H.Y. and
            Wang,J.G.
  TITLE     Roles of HDAC2 and HDAC8 in Cardiac Remodeling in Renovascular
            Hypertensive Rats and the Effects of Valproic Acid Sodium
  JOURNAL   Pharmacology 99 (1-2), 27-39 (2017)
   PUBMED   27673327
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Nakayama,T., Mikoshiba,K. and Akagawa,K.
  TITLE     The cell- and tissue-specific transcription mechanism of the
            TATA-less syntaxin 1A gene
  JOURNAL   FASEB J 30 (2), 525-543 (2016)
   PUBMED   26391271
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Deardorff,M.A., Bando,M., Nakato,R., Watrin,E., Itoh,T.,
            Minamino,M., Saitoh,K., Komata,M., Katou,Y., Clark,D., Cole,K.E.,
            De Baere,E., Decroos,C., Di Donato,N., Ernst,S., Francey,L.J.,
            Gyftodimou,Y., Hirashima,K., Hullings,M., Ishikawa,Y., Jaulin,C.,
            Kaur,M., Kiyono,T., Lombardi,P.M., Magnaghi-Jaulin,L.,
            Mortier,G.R., Nozaki,N., Petersen,M.B., Seimiya,H., Siu,V.M.,
            Suzuki,Y., Takagaki,K., Wilde,J.J., Willems,P.J., Prigent,C.,
            Gillessen-Kaesbach,G., Christianson,D.W., Kaiser,F.J.,
            Jackson,L.G., Hirota,T., Krantz,I.D. and Shirahige,K.
  TITLE     HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin
            acetylation cycle
  JOURNAL   Nature 489 (7415), 313-317 (2012)
   PUBMED   22885700
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Peserico,A. and Simone,C.
  TITLE     Physical and functional HAT/HDAC interplay regulates protein
            acetylation balance
  JOURNAL   J Biomed Biotechnol 2011, 371832 (2011)
   PUBMED   21151613
  REMARK    Review article
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Lee,H., Sengupta,N., Villagra,A., Rezai-Zadeh,N. and Seto,E.
  TITLE     Histone deacetylase 8 safeguards the human ever-shorter telomeres
            1B (hEST1B) protein from ubiquitin-mediated degradation
  JOURNAL   Mol Cell Biol 26 (14), 5259-5269 (2006)
   PUBMED   16809764
  REMARK    Erratum:[Mol Cell Biol. 2006 Oct;26(19):7342]
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Wedel,T., Van Eys,G.J., Waltregny,D., Glenisson,W., Castronovo,V.
            and Vanderwinden,J.M.
  TITLE     Novel smooth muscle markers reveal abnormalities of the intestinal
            musculature in severe colorectal motility disorders
  JOURNAL   Neurogastroenterol Motil 18 (7), 526-538 (2006)
   PUBMED   16771768
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Ito,K., Ito,M., Elliott,W.M., Cosio,B., Caramori,G., Kon,O.M.,
            Barczyk,A., Hayashi,S., Adcock,I.M., Hogg,J.C. and Barnes,P.J.
  TITLE     Decreased histone deacetylase activity in chronic obstructive
            pulmonary disease
  JOURNAL   N Engl J Med 352 (19), 1967-1976 (2005)
   PUBMED   15888697
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM086081.1 and BC162023.1.
            
            On Dec 5, 2009 this sequence version replaced NP_001119845.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC162023.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..377
                     /product="histone deacetylase 8"
                     /EC_number="3.5.1.98"
                     /note="protein deacetylase HDAC8; protein decrotonylase
                     HDAC8"
                     /calculated_mol_wt=41623
     Region          14..324
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WC68.1)"
     Region          16..377
                     /region_name="HDAC8"
                     /note="Histone deacetylase 8 (HDAC8); cd10000"
                     /db_xref="CDD:212524"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BY41; propagated from
                     UniProtKB/Swiss-Prot (B1WC68.1)"
     Site            order(100..101,141..143,151..152,178,180,208,267,274,304,
                     306)
                     /site_type="active"
                     /db_xref="CDD:212524"
     CDS             1..377
                     /gene="Hdac8"
                     /gene_synonym="HD8; RGD1562895"
                     /coded_by="NM_001126373.2:334..1467"
                     /db_xref="GeneID:363481"
                     /db_xref="RGD:1562895"
ORIGIN      
        1 meipeepans ghslppvyiy speyvsicds lvkvpkrasm vhslieayal hkqmrivkpk
       61 vasmeematf htdaylqhlq kvsqegdedh pdsieyglgy dcpategifd yaaaigggti
      121 taaqclidgk ckvainwsgg whhakkdeas gfcylndavl gilrlrrkfd rilyvdldlh
      181 hgdgvedafs ftskvmtvsl hkfspgffpg tgdmsdvglg kgryysvnvp iqdgiqdeky
      241 yhicesvlke vyqafnpkav vlqlgadtia gdpmcsfnmt pvgigkclky vlqwqlatli
      301 lggggynlan tarcwtyltg vilgktlsse ipdhefftay gpdyvleitp scrpdrneph
      361 riqqilnyik gnlkhvv
//
LOCUS       NP_001180497             445 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase Sgk1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001180497
VERSION     NP_001180497.1
DBSOURCE    REFSEQ: accession NM_001193568.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Li,Y.H., Sun,C.C., Chen,P.M. and Chen,H.H.
  TITLE     SGK1 Target Genes Involved in Heart and Blood Vessel Functions in
            PC12 Cells
  JOURNAL   Cells 12 (12), 1641 (2023)
   PUBMED   37371111
  REMARK    GeneRIF: SGK1 Target Genes Involved in Heart and Blood Vessel
            Functions in PC12 Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zou,Z., Zhao,T., Zeng,Z. and An,Y.
  TITLE     Serum and glucocorticoid inducible kinase 1 modulates mitochondrial
            dysfunction and oxidative stress in doxorubicin-induced
            cardiomyocytes by regulating Hippo pathway via Neural precursor
            cell-expressed developmentally down-regulated 4 type 2
  JOURNAL   Hum Exp Toxicol 42, 9603271231158039 (2023)
   PUBMED   36781297
  REMARK    GeneRIF: Serum and glucocorticoid inducible kinase 1 modulates
            mitochondrial dysfunction and oxidative stress in
            doxorubicin-induced cardiomyocytes by regulating Hippo pathway via
            Neural precursor cell-expressed developmentally down-regulated 4
            type 2.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Wang,F. and Han,L.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1 (SGK1)
            ameliorates doxorubicin-induced cardiotoxic injury, apoptosis,
            inflammation and oxidative stress by suppressing glucose regulated
            protein 78 (GRP78)-mediated endoplasmic reticulum stress
  JOURNAL   Bioengineered 13 (1), 844-855 (2022)
   PUBMED   34898378
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 (SGK1) ameliorates doxorubicin-induced cardiotoxic injury,
            apoptosis, inflammation and oxidative stress by suppressing glucose
            regulated protein 78 (GRP78)-mediated endoplasmic reticulum stress.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Liu,B.W., Zhang,J., Hong,Y.S., Li,N.B., Liu,Y., Zhang,M., Wu,W.Y.,
            Zheng,H., Lampert,A. and Zhang,X.W.
  TITLE     NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation
  JOURNAL   Mol Neurobiol 58 (3), 964-982 (2021)
   PUBMED   33063281
  REMARK    GeneRIF: NGF-Induced Nav1.7 Upregulation Contributes to Chronic
            Post-surgical Pain by Activating SGK1-Dependent Nedd4-2
            Phosphorylation.
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Lee,R.H., Grames,M.S., Wu,C.Y., Lien,C.F., Couto E Silva,A.,
            Possoit,H.E., Clemons,G.A., Citadin,C.T., Neumann,J.T., Pastore,D.,
            Lauro,D., Della-Morte,D. and Lin,H.W.
  TITLE     Upregulation of serum and glucocorticoid-regulated kinase 1
            exacerbates brain injury and neurological deficits after cardiac
            arrest
  JOURNAL   Am J Physiol Heart Circ Physiol 319 (5), H1044-H1050 (2020)
   PUBMED   32946263
  REMARK    GeneRIF: Upregulation of serum and glucocorticoid-regulated kinase
            1 exacerbates brain injury and neurological deficits after cardiac
            arrest.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Maiyar,A.C., Phu,P.T., Huang,A.J. and Firestone,G.L.
  TITLE     Repression of glucocorticoid receptor transactivation and DNA
            binding of a glucocorticoid response element within the
            serum/glucocorticoid-inducible protein kinase (sgk) gene promoter
            by the p53 tumor suppressor protein
  JOURNAL   Mol Endocrinol 11 (3), 312-329 (1997)
   PUBMED   9058378
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Maiyar,A.C., Huang,A.J., Phu,P.T., Cha,H.H. and Firestone,G.L.
  TITLE     p53 stimulates promoter activity of the sgk.
            serum/glucocorticoid-inducible serine/threonine protein kinase gene
            in rodent mammary epithelial cells
  JOURNAL   J Biol Chem 271 (21), 12414-12422 (1996)
   PUBMED   8647846
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Richards,J.S., Fitzpatrick,S.L., Clemens,J.W., Morris,J.K.,
            Alliston,T. and Sirois,J.
  TITLE     Ovarian cell differentiation: a cascade of multiple hormones,
            cellular signals, and regulated genes
  JOURNAL   Recent Prog Horm Res 50, 223-254 (1995)
   PUBMED   7740159
  REMARK    Review article
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Imaizumi,K., Tsuda,M., Wanaka,A., Tohyama,M. and Takagi,T.
  TITLE     Differential expression of sgk mRNA, a member of the Ser/Thr
            protein kinase gene family, in rat brain after CNS injury
  JOURNAL   Brain Res Mol Brain Res 26 (1-2), 189-196 (1994)
   PUBMED   7854047
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Webster,M.K., Goya,L., Ge,Y., Maiyar,A.C. and Firestone,G.L.
  TITLE     Characterization of sgk, a novel member of the serine/threonine
            protein kinase gene family which is transcriptionally induced by
            glucocorticoids and serum
  JOURNAL   Mol Cell Biol 13 (4), 2031-2040 (1993)
   PUBMED   8455596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM042519.1 and BC078843.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16676807
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..445
                     /product="serine/threonine-protein kinase Sgk1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase Sgk1;
                     serine/threonine protein kinase SGK"
                     /calculated_mol_wt=50496
     Region          104..442
                     /region_name="STKc_SGK1"
                     /note="Catalytic domain of the Protein Serine/Threonine
                     Kinase, Serum- and Glucocorticoid-induced Kinase 1;
                     cd05602"
                     /db_xref="CDD:270753"
     Site            order(118..119,121..124,126,139,141,174,191,193,197,199,
                     236,238,240..241,243,253..254,257,271..276,303,309,312)
                     /site_type="active"
                     /db_xref="CDD:270753"
     Site            order(118..119,121..124,126,139,141,174,191,193,238,
                     240..241,243,253)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270753"
     Site            order(122,197,199,236,238,240,257,271..276,303,309,312)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270753"
     Site            253..276
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270753"
     Site            411
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270753"
     Site            432..437
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270753"
     CDS             1..445
                     /gene="Sgk1"
                     /gene_synonym="Sgk"
                     /coded_by="NM_001193568.1:107..1444"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29517"
                     /db_xref="RGD:3668"
ORIGIN      
        1 mgemqgalar arlesllrpr hkkrveaqkr sesvllsgla fmkqrrmgln dfiqklanns
       61 yackhpevqs ylkisqpqep elmnanpspp pspsqqinlg pssnphakps dfhflkvigk
      121 gsfgkvllar hkaeeafyav kvlqkkailk kkeekhimse rnvllknvkh pflvglhfsf
      181 qtadklyfvl dyinggelfy hlqrercfle prarfyaaei asalgylhsl nivyrdlkpe
      241 nilldsqghi vltdfglcke niehngttst fcgtpeylap evlhkqpydr tvdwwclgav
      301 lyemlyglpp fysrntaemy dnilnkplql kpnitnsarh llegllqkdr tkrlgakddf
      361 meikshiffs linwddlink kitppfnpnv sgpsdlrhfd pefteepvps sigrspdsil
      421 vtasvkeaae aflgfsyapp mdsfl
//
LOCUS       NP_620259                535 aa            linear   ROD 27-APR-2025
DEFINITION  glutaminase liver isoform, mitochondrial isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_620259
VERSION     NP_620259.2
DBSOURCE    REFSEQ: accession NM_138904.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Zhou,X., Zhuo,M., Zhang,Y., Shi,E., Ma,X. and Li,H.
  TITLE     miR-190a-5p regulates cardiomyocytes response to ferroptosis via
            directly targeting GLS2
  JOURNAL   Biochem Biophys Res Commun 566, 9-15 (2021)
   PUBMED   34111670
  REMARK    GeneRIF: miR-190a-5p regulates cardiomyocytes response to
            ferroptosis via directly targeting GLS2.
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Cardona,C., Sanchez-Mejias,E., Davila,J.C., Martin-Rufian,M.,
            Campos-Sandoval,J.A., Vitorica,J., Alonso,F.J., Mates,J.M.,
            Segura,J.A., Norenberg,M.D., Rama Rao,K.V., Jayakumar,A.R.,
            Gutierrez,A. and Marquez,J.
  TITLE     Expression of Gls and Gls2 glutaminase isoforms in astrocytes
  JOURNAL   Glia 63 (3), 365-382 (2015)
   PUBMED   25297978
  REMARK    GeneRIF: GABAergic neurons and astrocytes express Gls and Gls2
            isoenzymes in nucleus and mitochondria, in addition to
            glutamatergic neurons
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Savilov,P.N. and Yakovlev,V.N.
  TITLE     Phosphate-dependent glutaminase response to liver injury and
            hyperbaric oxygenation
  JOURNAL   Bull Exp Biol Med 157 (3), 299-301 (2014)
   PUBMED   25065305
  REMARK    GeneRIF: In animals with chronic hepatitis; hyperbaric oxygenation
            restricted the stimulating effect of hepatic resection on
            phosphate-dependent glutaminase activity.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Martin-Rufian,M., Tosina,M., Campos-Sandoval,J.A., Manzanares,E.,
            Lobo,C., Segura,J.A., Alonso,F.J., Mates,J.M. and Marquez,J.
  TITLE     Mammalian glutaminase Gls2 gene encodes two functional alternative
            transcripts by a surrogate promoter usage mechanism
  JOURNAL   PLoS One 7 (6), e38380 (2012)
   PUBMED   22679499
  REMARK    GeneRIF: Study demonstrated expression of alternative transcripts
            of the mammalian Gls2 gene. Transcriptional mechanisms giving rise
            to GLS2 variants and isolation of novel GLS2 transcripts in human,
            rat and mouse are presented.
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Suzuki,S., Tanaka,T., Poyurovsky,M.V., Nagano,H., Mayama,T.,
            Ohkubo,S., Lokshin,M., Hosokawa,H., Nakayama,T., Suzuki,Y.,
            Sugano,S., Sato,E., Nagao,T., Yokote,K., Tatsuno,I. and Prives,C.
  TITLE     Phosphate-activated glutaminase (GLS2), a p53-inducible regulator
            of glutamine metabolism and reactive oxygen species
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7461-7466 (2010)
   PUBMED   20351271
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Chung-Bok,M.I., Vincent,N., Jhala,U. and Watford,M.
  TITLE     Rat hepatic glutaminase: identification of the full coding sequence
            and characterization of a functional promoter
  JOURNAL   Biochem J 324 (Pt 1) (Pt 1), 193-200 (1997)
   PUBMED   9164856
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Smith,E.M. and Watford,M.
  TITLE     Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence
            similarity to kidney-type glutaminase
  JOURNAL   J Biol Chem 265 (18), 10631-10636 (1990)
   PUBMED   2191954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC089776.1.
            
            On Aug 1, 2012 this sequence version replaced NP_620259.1.
            
            Transcript Variant: This variant (3) lacks the first exon and
            extends 5' into intronic sequence compared to variant 1. The
            resulting isoform (3) is shorter at the N-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05499.1, SRR26643286.21274.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..535
                     /product="glutaminase liver isoform, mitochondrial isoform
                     3"
                     /EC_number="3.5.1.2"
                     /note="glutaminase 2 (liver, mitochondrial); GLS;
                     L-glutaminase; L-glutamine amidohydrolase; liver
                     mitochondrial glutaminase"
                     /calculated_mol_wt=59073
     Region          5..88
                     /region_name="EF-hand_14"
                     /note="EF-hand domain; pfam17959"
                     /db_xref="CDD:465587"
     Region          110..394
                     /region_name="Glutaminase"
                     /note="pfam04960"
                     /db_xref="CDD:461499"
     Region          <423..>505
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          423..449
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(424..425,428..430,432..433,437,440,449,451,453,
                     457..458,461..463,465..466,470,473,483,485,487,491..492,
                     495..497,499..500,504)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          451..483
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..535
                     /gene="Gls2"
                     /gene_synonym="Ga"
                     /coded_by="NM_138904.2:133..1740"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:192268"
                     /db_xref="RGD:620359"
ORIGIN      
        1 mlprlgdllf ytiaegqeri pihkfttalk atglqtsdpr lqdcmskmqr mvqesssggl
       61 ldrelfqkcv ssnivlltqa frkkfvipdf eeftghvdri fedakeltgg kvaayiphla
      121 ksnpdlwgvs lctvdgqrhs vghtkipfcl qscvkpltya isvstlgtdy vhkfvgkeps
      181 glrynklsln eegiphnpmv nagaivvssl ikmdcnkaek fdfvlqylnk magnefmgfs
      241 natfqseket gdrnyaigyy lkekkcfpkg vdmmaaldly fqlcsvevtc esgsvmaatl
      301 anggicpitg esvlsaeavr ntlslmhscg mydfsgqfaf hvglpaksav sgaillvvpn
      361 vmgmmclspp ldklgnshrg isfcqklvsl fnfhnydnlr hcarkldprr eggevrnktv
      421 vnllfaaysg dvsalrrfal savdmeqkdy dsrtalhvaa aeghidvvkf lieackvnpf
      481 vkdrwgnipl ddavqfnhle vvkllqdyhd symlsetqae vaaetlsken lesmv
//
LOCUS       NP_001257788             203 aa            linear   ROD 27-APR-2025
DEFINITION  stathmin-4 isoform b [Rattus norvegicus].
ACCESSION   NP_001257788
VERSION     NP_001257788.1
DBSOURCE    REFSEQ: accession NM_001270859.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Nakazawa,T., Morii,H., Tamai,M. and Mori,N.
  TITLE     Selective upregulation of RB3/stathmin4 by ciliary neurotrophic
            factor following optic nerve axotomy
  JOURNAL   Brain Res 1061 (2), 97-106 (2005)
   PUBMED   16256088
  REMARK    GeneRIF: RB3 is the unique response protein in the stathmin-related
            proteins following optic nerve axotomy and the induced RB3 may play
            a critical role in the CNTF-induced response on the axotomized
            retinal ganglion cells
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nakao,C., Itoh,T.J., Hotani,H. and Mori,N.
  TITLE     Modulation of the stathmin-like microtubule destabilizing activity
            of RB3, a neuron-specific member of the SCG10 family, by its
            N-terminal domain
  JOURNAL   J Biol Chem 279 (22), 23014-23021 (2004)
   PUBMED   15039434
  REMARK    GeneRIF: regulatory role of the unique N-terminal domain of RB3 in
            microtubule dynamics would contribute to the physiological
            regulation of neuronal morphogenesis
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Ozon,S., El Mestikawy,S. and Sobel,A.
  TITLE     Differential, regional, and cellular expression of the stathmin
            family transcripts in the adult rat brain
  JOURNAL   J Neurosci Res 56 (5), 553-564 (1999)
   PUBMED   10369222
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Gavet,O., Ozon,S., Manceau,V., Lawler,S., Curmi,P. and Sobel,A.
  TITLE     The stathmin phosphoprotein family: intracellular localization and
            effects on the microtubule network
  JOURNAL   J Cell Sci 111 (Pt 22), 3333-3346 (1998)
   PUBMED   9788875
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Ozon,S., Byk,T. and Sobel,A.
  TITLE     SCLIP: a novel SCG10-like protein of the stathmin family expressed
            in the nervous system
  JOURNAL   J Neurochem 70 (6), 2386-2396 (1998)
   PUBMED   9603203
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Ozon,S., Maucuer,A. and Sobel,A.
  TITLE     The stathmin family -- molecular and biological characterization of
            novel mammalian proteins expressed in the nervous system
  JOURNAL   Eur J Biochem 248 (3), 794-806 (1997)
   PUBMED   9342231
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB580507.1 and BC092646.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and has
            an alternate exon in the 3' end compared to variant 1. This exon
            has an in-frame stop codon, resulting in an isoform (b) with a
            shorter and distinct C-terminus compared to isoform a. Variants 2
            and 6 both encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC092646.1, CO398144.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760389, SAMEA5760393 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..203
                     /product="stathmin-4 isoform b"
                     /note="stathmin-like protein B3; stathmin-like-protein
                     RB3; stathmin-like 4"
                     /calculated_mol_wt=23587
     Region          76..198
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     CDS             1..203
                     /gene="Stmn4"
                     /gene_synonym="Lagl; Rb3"
                     /coded_by="NM_001270859.1:111..722"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:79423"
                     /db_xref="RGD:69349"
ORIGIN      
        1 mtlaaykekm kelplvslfc scflsdplnk ssykyegwcg rqcrrkgqsq rkgsadwrer
       61 reqadtvdln wcvisdmevi elnkctsgqs fevilkppsf dgvpefnasl prrrdpslee
      121 iqkkleaaee rrkyqeaell khlaekrehe reviqkaiee nnnfikmake klaqkmesnk
      181 enreahlaam lerlqekepp aar
//
LOCUS       NP_036955                324 aa            linear   ROD 27-APR-2025
DEFINITION  annexin A3 [Rattus norvegicus].
ACCESSION   NP_036955
VERSION     NP_036955.2
DBSOURCE    REFSEQ: accession NM_012823.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Nie,P., Wang,H., Yu,D., Wu,H., Ni,B., Kong,J. and Zhang,Z.
  TITLE     NIX Mediates Mitophagy in Spinal Cord Injury in Rats by Interacting
            with LC3
  JOURNAL   Cell Mol Neurobiol 42 (6), 1983-1994 (2022)
   PUBMED   33779883
  REMARK    GeneRIF: NIX Mediates Mitophagy in Spinal Cord Injury in Rats by
            Interacting with LC3.
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Mondaca-Ruff,D., Quiroga,C., Norambuena-Soto,I., Riquelme,J.A., San
            Martin,A., Bustamante,M., Lavandero,S. and Chiong,M.
  TITLE     Regulation of total LC3 levels by angiotensin II in vascular smooth
            muscle cells
  JOURNAL   J Cell Mol Med 26 (5), 1710-1713 (2022)
   PUBMED   35118791
  REMARK    GeneRIF: Regulation of total LC3 levels by angiotensin II in
            vascular smooth muscle cells.
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Zhang,Z., Li,Z., Ma,Z., Deng,M., Xing,M., Wu,J., Jiang,S., Wang,Q.,
            Guo,Q. and Zou,W.
  TITLE     Annexin A3 as a Marker Protein for Microglia in the Central Nervous
            System of Rats
  JOURNAL   Neural Plast 2021, 5575090 (2021)
   PUBMED   34221002
  REMARK    GeneRIF: Annexin A3 as a Marker Protein for Microglia in the
            Central Nervous System of Rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Zhang,X. and Wang,R.Y.
  TITLE     [Effects of high-load exercise induced skeletal muscle injury on
            autophagy ultrastructure and Beclin1 and LC3-II / I in rats]
  JOURNAL   Zhongguo Ying Yong Sheng Li Xue Za Zhi 36 (4), 296-300 (2020)
   PUBMED   33167086
  REMARK    GeneRIF: [Effects of high-load exercise induced skeletal muscle
            injury on autophagy ultrastructure and Beclin1 and LC3-II / I in
            rats].
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Meng,H., Zhang,Y., An,S.T. and Chen,Y.
  TITLE     Annexin A3 gene silencing promotes myocardial cell repair through
            activation of the PI3K/Akt signaling pathway in rats with acute
            myocardial infarction
  JOURNAL   J Cell Physiol 234 (7), 10535-10546 (2019)
   PUBMED   30456911
  REMARK    GeneRIF: our study provides evidence that the downregulation of
            ANXA3 promotes the repair and healing of myocardial tissues by
            activating the PI3K/Akt signaling pathway.
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Naciff,J.M., Kaetzel,M.A., Behbehani,M.M. and Dedman,J.R.
  TITLE     Differential expression of annexins I-VI in the rat dorsal root
            ganglia and spinal cord
  JOURNAL   J Comp Neurol 368 (3), 356-370 (1996)
   PUBMED   8725344
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Le Cabec,V. and Maridonneau-Parini,I.
  TITLE     Annexin 3 is associated with cytoplasmic granules in neutrophils
            and monocytes and translocates to the plasma membrane in activated
            cells
  JOURNAL   Biochem J 303 (Pt 2) (Pt 2), 481-487 (1994)
   PUBMED   7526843
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Ernst,J.D., Hoye,E., Blackwood,R.A. and Jaye,D.
  TITLE     Purification and characterization of an abundant cytosolic protein
            from human neutrophils that promotes Ca2(+)-dependent aggregation
            of isolated specific granules
  JOURNAL   J Clin Invest 85 (4), 1065-1071 (1990)
   PUBMED   2138632
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Blackwood,R.A. and Ernst,J.D.
  TITLE     Characterization of Ca2(+)-dependent phospholipid binding, vesicle
            aggregation and membrane fusion by annexins
  JOURNAL   Biochem J 266 (1), 195-200 (1990)
   PUBMED   2138016
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Pepinsky,R.B., Tizard,R., Mattaliano,R.J., Sinclair,L.K.,
            Miller,G.T., Browning,J.L., Chow,E.P., Burne,C., Huang,K.S.,
            Pratt,D. et al.
  TITLE     Five distinct calcium and phospholipid binding proteins share
            homology with lipocortin I
  JOURNAL   J Biol Chem 263 (22), 10799-10811 (1988)
   PUBMED   2968983
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1 and BC081856.1.
            
            On Aug 18, 2012 this sequence version replaced NP_036955.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.730687.1,
                                           SRR26360172.2367786.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676786, SAMN16676787
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..324
                     /product="annexin A3"
                     /EC_number="3.1.4.43"
                     /note="PAP-III; annexin-3; 35-alpha calcimedin; placental
                     anticoagulant protein III; lipocortin III; Annexin III
                     (Lipocortin III)"
                     /calculated_mol_wt=36232
     Region          19..90
                     /region_name="Annexin 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P14669.4)"
     Region          24..88
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          91..162
                     /region_name="Annexin 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P14669.4)"
     Region          95..160
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          174..246
                     /region_name="Annexin 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P14669.4)"
     Site            178
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35639; propagated from
                     UniProtKB/Swiss-Prot (P14669.4)"
     Region          179..244
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Region          250..321
                     /region_name="Annexin 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01245"
                     /note="propagated from UniProtKB/Swiss-Prot (P14669.4)"
     Region          256..319
                     /region_name="Annexin"
                     /note="pfam00191"
                     /db_xref="CDD:395139"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P14669.4)"
     CDS             1..324
                     /gene="Anxa3"
                     /gene_synonym="Anx3; LC3; LRRGT00047"
                     /coded_by="NM_012823.2:137..1111"
                     /db_xref="GeneID:25291"
                     /db_xref="RGD:2119"
ORIGIN      
        1 maaslwvgpr gtinnypgfn psvdaeairk aikgigtdek tlinilters naqrqlivkq
       61 yqeayeqalk adlkgdlsgh fehvmvalit apavfdakql kksmrgmgtd edtlieiltt
      121 rtsrqmkeis qayytaykkn lrddissets gdfrkalltl adggrdeslk vdehlakkda
      181 qtlydagekk wgtdedkfte ilclrsfpql kltfdeyrni sqkdiedsik gelsghfedl
      241 llavvrctrn tpaflagrlh qalkgagtde ftlnrimvsr seidlldirr efkkhygcsl
      301 ysaiqsdtsg dyrtvllkic ggdd
//
LOCUS       NP_001257613             312 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein E precursor [Rattus norvegicus].
ACCESSION   NP_001257613
VERSION     NP_001257613.1
DBSOURCE    REFSEQ: accession NM_001270684.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lee,B.H., Cevizci,M., Lieblich,S.E., Ibrahim,M., Wen,Y., Eid,R.S.,
            Lamers,Y., Duarte-Guterman,P. and Galea,L.A.M.
  TITLE     Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age
  JOURNAL   Brain Behav Immun 120, 54-70 (2024)
   PUBMED   38772427
  REMARK    GeneRIF: Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Chen,H., Zhao,S., Jian,Q., Yan,Y., Wang,S., Zhang,X. and Ji,Y.
  TITLE     The role of ApoE in fatty acid transport from neurons to astrocytes
            under ischemia/hypoxia conditions
  JOURNAL   Mol Biol Rep 51 (1), 320 (2024)
   PUBMED   38393618
  REMARK    GeneRIF: The role of ApoE in fatty acid transport from neurons to
            astrocytes under ischemia/hypoxia conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Matsuo,H., Kawakami,K., Ohara,H., Kaneko,T., Mashimo,T., Yamada,T.
            and Nabika,T.
  TITLE     Apolipoprotein E-depletion accelerates arterial fat deposition in
            the spontaneously hypertensive rat
  JOURNAL   Exp Anim 72 (4), 439-445 (2023)
   PUBMED   37081644
  REMARK    GeneRIF: Apolipoprotein E-depletion accelerates arterial fat
            deposition in the spontaneously hypertensive rat.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Jiang,C., Chen,Z., Wang,X., Zhang,Y., Guo,X., Fan,H., Huang,D.,
            He,Y., Tang,X., Ai,Y., Liu,Y., Yang,H. and Hao,D.
  TITLE     Curcumin-activated Olfactory Ensheathing Cells Improve Functional
            Recovery After Spinal Cord Injury by Modulating Microglia
            Polarization Through APOE/TREM2/NF-kappaB Signaling Pathway
  JOURNAL   J Neuroimmune Pharmacol 18 (3), 476-494 (2023)
   PUBMED   37658943
  REMARK    GeneRIF: Curcumin-activated Olfactory Ensheathing Cells Improve
            Functional Recovery After Spinal Cord Injury by Modulating
            Microglia Polarization Through APOE/TREM2/NF-kappaB Signaling
            Pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Nguyen,T.D., Watanabe,A., Burleigh,S., Ghaffarzadegan,T.,
            Kanklai,J., Prykhodko,O., Hallenius,F.F. and Nyman,M.
  TITLE     Monobutyrin and monovalerin improve gut-blood-brain biomarkers and
            alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats
  JOURNAL   Sci Rep 12 (1), 15454 (2022)
   PUBMED   36104381
  REMARK    GeneRIF: Monobutyrin and monovalerin improve gut-blood-brain
            biomarkers and alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Takahashi,S., Kawarabayasi,Y., Nakai,T., Sakai,J. and Yamamoto,T.
  TITLE     Rabbit very low density lipoprotein receptor: a low density
            lipoprotein receptor-like protein with distinct ligand specificity
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9252-9256 (1992)
   PUBMED   1384047
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Feussner,G., Funke,H., Weng,W., Assmann,G., Lackner,K.J. and
            Ziegler,R.
  TITLE     Severe type III hyperlipoproteinemia associated with unusual
            apolipoprotein E1 phenotype and epsilon 1/'null' genotype
  JOURNAL   Eur J Clin Invest 22 (9), 599-608 (1992)
   PUBMED   1360898
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Utermann,G., Hees,M. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E and occurrence of
            dysbetalipoproteinaemia in man
  JOURNAL   Nature 269 (5629), 604-607 (1977)
   PUBMED   199847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC086581.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. All five variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV216405.1, SRR22582416.1131004.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..312
                     /product="apolipoprotein E precursor"
                     /note="apo-E"
                     /calculated_mol_wt=33845
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1927
     mat_peptide     19..312
                     /product="Apolipoprotein E. /id=PRO_0000001996"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
                     /calculated_mol_wt=33845
     Region          72..247
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          73..258
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          202..282
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          258..312
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          270..282
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     CDS             1..312
                     /gene="Apoe"
                     /gene_synonym="APOEA"
                     /coded_by="NM_001270684.1:79..1017"
                     /db_xref="GeneID:25728"
                     /db_xref="RGD:2138"
ORIGIN      
        1 mkalwalllv plltgclaeg elevtdqlpg qsdqpweqal nrfwdylrwv qtlsdqvqee
       61 lqssqvtqel tvlmedtmte vkaykkelee qlgpvaeetr arlakevqaa qarlgadmed
      121 lrnrlgqyrn evntmlgqst eelrsrlsth lrkmrkrlmr daddlqkrla vykagaqega
      181 ergvsairer lgplveqgrq rtanlgagaa qplrdraqal sdrirgrlee vgnqardrle
      241 evreqmeevr skmeeqtqqi rlqaeifqar ikgwfeplve dmqrqwanlm ekiqasvatn
      301 siasttvple nq
//
LOCUS       NP_113787               1108 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2-alpha kinase 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_113787
VERSION     NP_113787.1
DBSOURCE    REFSEQ: accession NM_031599.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Yuan,Z., Xiao-Wei,L., Juan,W., Xiu-Juan,L., Nian-Yun,Z. and Lei,S.
  TITLE     HIIT and MICT attenuate high-fat diet-induced hepatic lipid
            accumulation and ER stress via the PERK-ATF4-CHOP signaling pathway
  JOURNAL   J Physiol Biochem 78 (3), 641-652 (2022)
   PUBMED   35315506
  REMARK    GeneRIF: HIIT and MICT attenuate high-fat diet-induced hepatic
            lipid accumulation and ER stress via the PERK-ATF4-CHOP signaling
            pathway.
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Liu,H., Li,J., Jiang,C., Yuan,T. and Ma,H.
  TITLE     Cellular communication network factor 1 (CCN1) knockdown exerts a
            protective effect for hepatic ischemia/reperfusion injury by
            deactivating the MEK/ERK pathway
  JOURNAL   Clin Res Hepatol Gastroenterol 45 (5), 101737 (2021)
   PUBMED   34144219
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Nouri,H., Sheikholeslami-Vatani,D. and Moloudi,M.R.
  TITLE     Changes in UPR-PERK pathway and muscle hypertrophy following
            resistance training and creatine supplementation in rats
  JOURNAL   J Physiol Biochem 77 (2), 331-339 (2021)
   PUBMED   33635524
  REMARK    GeneRIF: Changes in UPR-PERK pathway and muscle hypertrophy
            following resistance training and creatine supplementation in rats.
REFERENCE   4  (residues 1 to 1108)
  AUTHORS   Zhang,R., Jiang,M., Zhang,J., Qiu,Y., Li,D., Li,S., Liu,J., Liu,C.,
            Fang,Z. and Cao,F.
  TITLE     Regulation of the cerebrovascular smooth muscle cell phenotype by
            mitochondrial oxidative injury and endoplasmic reticulum stress in
            simulated microgravity rats via the PERK-eIF2alpha-ATF4-CHOP
            pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (8), 165799 (2020)
   PUBMED   32304741
  REMARK    GeneRIF: Regulation of the cerebrovascular smooth muscle cell
            phenotype by mitochondrial oxidative injury and endoplasmic
            reticulum stress in simulated microgravity rats via the
            PERK-eIF2alpha-ATF4-CHOP pathway.
REFERENCE   5  (residues 1 to 1108)
  AUTHORS   Manaud,G., Nossent,E.J., Lambert,M., Ghigna,M.R., Boet,A.,
            Vinhas,M.C., Ranchoux,B., Dumas,S.J., Courboulin,A., Girerd,B.,
            Soubrier,F., Bignard,J., Claude,O., Lecerf,F., Hautefort,A.,
            Florio,M., Sun,B., Nadaud,S., Verleden,S.E., Remy,S., Anegon,I.,
            Bogaard,H.J., Mercier,O., Fadel,E., Simonneau,G., Vonk
            Noordegraaf,A., Grunberg,K., Humbert,M., Montani,D., Dorfmuller,P.,
            Antigny,F. and Perros,F.
  TITLE     Comparison of Human and Experimental Pulmonary Veno-Occlusive
            Disease
  JOURNAL   Am J Respir Cell Mol Biol 63 (1), 118-131 (2020)
   PUBMED   32209028
REFERENCE   6  (residues 1 to 1108)
  AUTHORS   Bertolotti,A., Zhang,Y., Hendershot,L.M., Harding,H.P. and Ron,D.
  TITLE     Dynamic interaction of BiP and ER stress transducers in the
            unfolded-protein response
  JOURNAL   Nat Cell Biol 2 (6), 326-332 (2000)
   PUBMED   10854322
REFERENCE   7  (residues 1 to 1108)
  AUTHORS   Sood,R., Porter,A.C., Ma,K., Quilliam,L.A. and Wek,R.C.
  TITLE     Pancreatic eukaryotic initiation factor-2alpha kinase (PEK)
            homologues in humans, Drosophila melanogaster and Caenorhabditis
            elegans that mediate translational control in response to
            endoplasmic reticulum stress
  JOURNAL   Biochem J 346 Pt 2 (Pt 2), 281-293 (2000)
   PUBMED   10677345
REFERENCE   8  (residues 1 to 1108)
  AUTHORS   Shi,Y., An,J., Liang,J., Hayes,S.E., Sandusky,G.E., Stramm,L.E. and
            Yang,N.N.
  TITLE     Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and
            co-localization with somatostatin in islet delta cells
  JOURNAL   J Biol Chem 274 (9), 5723-5730 (1999)
   PUBMED   10026192
REFERENCE   9  (residues 1 to 1108)
  AUTHORS   Harding,H.P., Zhang,Y. and Ron,D.
  TITLE     Protein translation and folding are coupled by an
            endoplasmic-reticulum-resident kinase
  JOURNAL   Nature 397 (6716), 271-274 (1999)
   PUBMED   9930704
  REMARK    Erratum:[Nature 1999 Mar 4;398(6722):90]
REFERENCE   10 (residues 1 to 1108)
  AUTHORS   Shi,Y., Vattem,K.M., Sood,R., An,J., Liang,J., Stramm,L. and
            Wek,R.C.
  TITLE     Identification and characterization of pancreatic eukaryotic
            initiation factor 2 alpha-subunit kinase, PEK, involved in
            translational control
  JOURNAL   Mol Cell Biol 18 (12), 7499-7509 (1998)
   PUBMED   9819435
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF096835.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF096835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132285, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..1108
                     /product="eukaryotic translation initiation factor 2-alpha
                     kinase 3 precursor"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="pancreatic eIF2-alpha kinase; PRKR-like endoplasmic
                     reticulum kinase; protein tyrosine kinase EIF2AK3"
                     /calculated_mol_wt=121906
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
                     /calculated_mol_wt=2883
     mat_peptide     28..1108
                     /product="Eukaryotic translation initiation factor 2-alpha
                     kinase 3. /id=PRO_0000024324"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
                     /calculated_mol_wt=121906
     Region          71..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          99..412
                     /region_name="Luminal_EIF2AK3"
                     /note="The Luminal domain, a dimerization domain, of the
                     Serine/Threonine protein kinase, eukaryotic translation
                     Initiation Factor 2-Alpha Kinase 3; cd09768"
                     /db_xref="CDD:188874"
     Site            order(179..183,188,190..193,195..197,209,211..213,
                     234..235,243,245,260,262..264)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:188874"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Site            507..527
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          542..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          579..>667
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9NZJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          639..880
                     /region_name="Insert loop.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2B5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          772..818
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2B5; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          832..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Region          <868..1067
                     /region_name="STKc_EIF2AK3_PERK"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     eukaryotic translation Initiation Factor 2-Alpha Kinase 3
                     or PKR-like Endoplasmic Reticulum Kinase; cd14048"
                     /db_xref="CDD:270950"
     Site            order(946..955,957..981)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270950"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2B5; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Site            order(979..981,1012,1014..1021)
                     /site_type="other"
                     /note="eIF2alpha (substrate) binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270950"
     Region          1080..1108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NZJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z1.1)"
     CDS             1..1108
                     /gene="Eif2ak3"
                     /gene_synonym="PEK"
                     /coded_by="NM_031599.2:212..3538"
                     /db_xref="GeneID:29702"
                     /db_xref="RGD:70884"
ORIGIN      
        1 meratqprpr allllflllg caagisavar arsllaptsd tafglgaaaa ptsaarvpav
       61 ataevtveda ealpaasgeq esratesddd velrprgrsl viistldgri aaldaenhgk
      121 kqwdldvgsg slvssslskp evfgnkmiip sldgdlfqwd rdresmeavp ftveslless
      181 ykfgddvvlv ggkslttygl saysgklryi csalgcrrwd sdemeeeedi lllqrtqktv
      241 ravgprsgse kwnfsvghfe lryipdmetr agfiestfkl ggnkedskii sdveeqdvdt
      301 vikvsvadwk vmafskkggr leweyqfctp iasawlvrdg kvipislfdd tsytaneevl
      361 edeediveaa rgatensvyl gmyrgqlylq ssvrvsekfp trpkalesvn gesaiiplpt
      421 ikwkplihsp srtpvlvgsd efdkclsndk ysheeysnga lsilqypydn gyylpyykre
      481 rnkrstqitv rfldsphysk nirkkdpill lhwwkeifgt illcivattf ivrrlfhpqp
      541 hrqrkesetq cqteskydsv sadnsdnswn dikhsgyvsr yltdfepiqc mgrggfgvvf
      601 eaknkvddcn yaikrirlpn relarekvmr evkalakleh pgivryfnaw letppekwqe
      661 emdeiwlkde stdwplssps pmdapsvkir qmdpfstkeq ieviapsper srsfsvgisc
      721 grtsssesqf splefsgtdc gdnsdsedaa hnlqdscltd cdmedgtvdg ddeghsfelc
      781 pseaspytrs regtsssivf edsgcdnass kedprmnrlh nghhyvnklt efkhsssrss
      841 seatlstspt rpttlsldft rntvdrlqps spkvylyiqm qlcrkenlkd wmnrrcsmed
      901 rehrvclhif lqiaeavqfl hskglmhrdl kpsnifftmd dvvkvgdfgl vtamdqdeee
      961 qtvltpmpay athtgqvgtk lymspeqihg nnyshkvdif slglilfell ypfstqmerv
     1021 rtltdvrnlk fpplftqkyp qehmmvqdml spspmerpea tdiienavfe nlefpgktvl
     1081 rqrsrslsss gtkhsrqpss tfsplpgn
//
LOCUS       NP_001029064             601 aa            linear   ROD 27-APR-2025
DEFINITION  integrator complex subunit 11 [Rattus norvegicus].
ACCESSION   NP_001029064 XP_216603
VERSION     NP_001029064.2
DBSOURCE    REFSEQ: accession NM_001033892.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Jodoin,J.N., Sitaram,P., Albrecht,T.R., May,S.B., Shboul,M.,
            Lee,E., Reversade,B., Wagner,E.J. and Lee,L.A.
  TITLE     Nuclear-localized Asunder regulates cytoplasmic dynein localization
            via its role in the integrator complex
  JOURNAL   Mol Biol Cell 24 (18), 2954-2965 (2013)
   PUBMED   23904267
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1 and BC105303.1.
            
            On Jun 20, 2015 this sequence version replaced NP_001029064.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105303.1, SRR26643429.22251.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..601
                     /product="integrator complex subunit 11"
                     /EC_number="3.1.27.-"
                     /note="CPSF3-like protein; cleavage and
                     polyadenylation-specific factor 3-like protein; cleavage
                     and polyadenylation specific factor 3-like"
                     /calculated_mol_wt=67841
     Region          5..447
                     /region_name="COG1782"
                     /note="Predicted metal-dependent RNase, contains
                     metallo-beta-lactamase and KH domains [General function
                     prediction only]"
                     /db_xref="CDD:441388"
     Region          7..205
                     /region_name="INTS11-like_MBL-fold"
                     /note="Integrator complex subunit 11, and related
                     proteins; MBL-fold metallo-hydrolase domain; cd16291"
                     /db_xref="CDD:293849"
     Site            order(16,69,71,73..74,158,179)
                     /site_type="active"
                     /db_xref="CDD:293849"
     Site            order(142..144,150,166,168,173,196)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:293849"
     CDS             1..601
                     /gene="Ints11"
                     /gene_synonym="Cpsf3l; int11"
                     /coded_by="NM_001033892.2:108..1913"
                     /db_xref="GeneID:298688"
                     /db_xref="RGD:1306841"
ORIGIN      
        1 mmpeirvtpl gagqdvgrsc ilvsisgknv mldcgmhmgy nddrrfpdfs yitqsgrltd
       61 fldcviishf hldhcgalpy fsemvgydgp iymthptqai cpilledyrk iavdkkgean
      121 fftsqmikdc mkkvvavhlh qtvqvddele ikayyaghvl gaamfqikvg sesvvytgdy
      181 nmtpdrhlga awidkcrpnl litestyatt irdskrcrer dflkkvhetv erggkvlipv
      241 falgraqelc illetfwerm nlkvpiyfst gltekanhyy klfitwtnqk irktfvqrnm
      301 fefkhikafd rtfadnpgpm vvfatpgmlh agqslqifrk wagneknmvi mpgycvqgtv
      361 ghkilsgqrk lemegrqmle vkmqveymsf sahadakgim qlvgqaepes vllvhgeakk
      421 meflrqkieq efrvscympa ngetvtlpts psipvgislg llkremvqgl lpeakkprll
      481 hgtlimkdnn frlvsseqal kelglaehql rftcrvhlqd trkeqetalr vyshlkstlk
      541 dhcvqhlpdg svtvesiliq aaahsedpgt kvllvswtyq deelgsflta llknglpqap
      601 s
//
LOCUS       NP_001288271             284 aa            linear   ROD 27-APR-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.2st [Rattus norvegicus].
ACCESSION   NP_001288271 XP_008764428
VERSION     NP_001288271.1
DBSOURCE    REFSEQ: accession NM_001301342.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ji,M., Su,L., Liu,L., Zhuang,M., Xiao,J., Guan,Y., Zhu,S., Ma,L.
            and Pu,H.
  TITLE     CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms
  JOURNAL   Sci Rep 13 (1), 5827 (2023)
   PUBMED   37037889
  REMARK    GeneRIF: CaMKII regulates the proteins TPM1 and MYOM2 and promotes
            diacetylmorphine-induced abnormal cardiac rhythms.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Ly,T., Pappas,C.T., Johnson,D., Schlecht,W., Colpan,M.,
            Galkin,V.E., Gregorio,C.C., Dong,W.J. and Kostyukova,A.S.
  TITLE     Effects of cardiomyopathy-linked mutations K15N and R21H in
            tropomyosin on thin-filament regulation and pointed-end dynamics
  JOURNAL   Mol Biol Cell 30 (2), 268-281 (2019)
   PUBMED   30462572
  REMARK    GeneRIF: the R21H mutation causes a twofold decrease in
            tropomyosin's affinity for F-actin and affects leiomodin's
            function.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Chen,C.C., Hsia,C.W., Ho,C.W., Liang,C.M., Chen,C.M., Huang,K.L.,
            Kang,B.H. and Chen,Y.H.
  TITLE     Hypoxia and hyperoxia differentially control proliferation of rat
            neural crest stem cells via distinct regulatory pathways of the
            HIF1alpha-CXCR4 and TP53-TPM1 proteins
  JOURNAL   Dev Dyn 246 (3), 162-185 (2017)
   PUBMED   28002632
  REMARK    GeneRIF: Hypoxia and hyperoxia differentially control proliferation
            of rat neural crest stem cells via distinct regulatory pathways of
            the HIF1alpha-CXCR4 and TP53-TPM1 proteins
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Kirwan,J.P. and Hodges,R.S.
  TITLE     Transmission of stability information through the N-domain of
            tropomyosin is interrupted by a stabilizing mutation (A109L) in the
            hydrophobic core of the stability control region (residues 97-118)
  JOURNAL   J Biol Chem 289 (7), 4356-4366 (2014)
   PUBMED   24362038
  REMARK    GeneRIF: Transmission of stability information through the N-domain
            of tropomyosin is interrupted by a stabilizing mutation (A109L) in
            the hydrophobic core of the stability control region (residues
            97-118).
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Yar,S., Chowdhury,S.A.K., Davis,R.T. 3rd, Kobayashi,M.,
            Monasky,M.M., Rajan,S., Wolska,B.M., Gaponenko,V., Kobayashi,T.,
            Wieczorek,D.F. and Solaro,R.J.
  TITLE     Conserved Asp-137 is important for both structure and regulatory
            functions of cardiac alpha-tropomyosin (alpha-TM) in a novel
            transgenic mouse model expressing alpha-TM-D137L
  JOURNAL   J Biol Chem 288 (23), 16235-16246 (2013)
   PUBMED   23609439
  REMARK    GeneRIF: the link between flexibility of TM and its function in
            ejecting hearts.
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Goodwin,L.O., Lees-Miller,J.P., Leonard,M.A., Cheley,S.B. and
            Helfman,D.M.
  TITLE     Four fibroblast tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene via alternative RNA splicing and the use of
            two promoters
  JOURNAL   J Biol Chem 266 (13), 8408-8415 (1991)
   PUBMED   2022655
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P., Goodwin,L.O. and Helfman,D.M.
  TITLE     Three novel brain tropomyosin isoforms are expressed from the rat
            alpha-tropomyosin gene through the use of alternative promoters and
            alternative RNA processing
  JOURNAL   Mol Cell Biol 10 (4), 1729-1742 (1990)
   PUBMED   2320008
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Wieczorek,D.F., Smith,C.W. and Nadal-Ginard,B.
  TITLE     The rat alpha-tropomyosin gene generates a minimum of six different
            mRNAs coding for striated, smooth, and nonmuscle isoforms by
            alternative splicing
  JOURNAL   Mol Cell Biol 8 (2), 679-694 (1988)
   PUBMED   3352602
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ruiz-Opazo,N. and Nadal-Ginard,B.
  TITLE     Alpha-tropomyosin gene organization. Alternative splicing of
            duplicated isotype-specific exons accounts for the production of
            smooth and striated muscle isoforms
  JOURNAL   J Biol Chem 262 (10), 4755-4765 (1987)
   PUBMED   3558368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FQ074026.1, CF108680.1,
            FQ217616.1 and AI603512.1.
            
            On Aug 24, 2014 this sequence version replaced XP_008764428.1.
            
            SUMMARY: This gene is a member of the tropomyosin family and
            encodes a protein that heterodimerizes with a beta subunit, binding
            actin in both muscle and nonmuscle cells. In both smooth and
            striated muscle cells, it plays a role in calcium
            dependent-regulation of muscle contraction. In nonmuscle cells, it
            stabilizes cytoskeleton actin filaments. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (Tpm1.2, also known as variant 11)
            has multiple differences in the coding region, compared to variant
            1, resulting in a shorter protein (isoform Tpm1.2st). The resulting
            protein (isoform Tpm1.2st) is shorter and has a distinct C-terminus
            compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF108680.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.2st"
                     /note="smooth muscle alpha-tropomyosin; striated muscle
                     alpha-tropomyosin; hepatoma alpha tropomyosin; tropomyosin
                     1, alpha; tropomyosin 3 alpha; tropomyosin-alpha"
                     /calculated_mol_wt=32494
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="Tpm1"
                     /gene_synonym="Alpha-tm; Tma2; Tmsa"
                     /coded_by="NM_001301342.1:107..961"
                     /note="isoform Tpm1.2st is encoded by transcript variant
                     Tpm1.2"
                     /db_xref="GeneID:24851"
                     /db_xref="RGD:3898"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle edisakekll rasederdrv
       61 leelhkaeds llaadetaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedk yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsi
//
LOCUS       NP_068624                583 aa            linear   ROD 27-APR-2025
DEFINITION  epsin-2 isoform a [Rattus norvegicus].
ACCESSION   NP_068624
VERSION     NP_068624.2
DBSOURCE    REFSEQ: accession NM_021852.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Sakai,E., Miura,Y., Suzuki-Kouyama,E., Oka,K., Tachibana,M.,
            Kawabata,K., Sakurai,F. and Mizuguchi,H.
  TITLE     A mammalian mirtron miR-1224 promotes tube-formation of human
            primary endothelial cells by targeting anti-angiogenic factor
            epsin2
  JOURNAL   Sci Rep 7 (1), 5541 (2017)
   PUBMED   28717225
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Sen,A., Madhivanan,K., Mukherjee,D. and Aguilar,R.C.
  TITLE     The epsin protein family: coordinators of endocytosis and signaling
  JOURNAL   Biomol Concepts 3 (2), 117-126 (2012)
   PUBMED   22942912
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Chen,H., Ko,G., Zatti,A., Di Giacomo,G., Liu,L., Raiteri,E.,
            Perucco,E., Collesi,C., Min,W., Zeiss,C., De Camilli,P. and
            Cremona,O.
  TITLE     Embryonic arrest at midgestation and disruption of Notch signaling
            produced by the absence of both epsin 1 and epsin 2 in mice
  JOURNAL   Proc Natl Acad Sci U S A 106 (33), 13838-13843 (2009)
   PUBMED   19666558
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Hussain,N.K., Yamabhai,M., Bhakar,A.L., Metzler,M., Ferguson,S.S.,
            Hayden,M.R., McPherson,P.S. and Kay,B.K.
  TITLE     A role for epsin N-terminal homology/AP180 N-terminal homology
            (ENTH/ANTH) domains in tubulin binding
  JOURNAL   J Biol Chem 278 (31), 28823-28830 (2003)
   PUBMED   12750376
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Polo,S., Sigismund,S., Faretta,M., Guidi,M., Capua,M.R., Bossi,G.,
            Chen,H., De Camilli,P. and Di Fiore,P.P.
  TITLE     A single motif responsible for ubiquitin recognition and
            monoubiquitination in endocytic proteins
  JOURNAL   Nature 416 (6879), 451-455 (2002)
   PUBMED   11919637
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Rosenthal,J.A., Chen,H., Slepnev,V.I., Pellegrini,L., Salcini,A.E.,
            Di Fiore,P.P. and De Camilli,P.
  TITLE     The epsins define a family of proteins that interact with
            components of the clathrin coat and contain a new protein module
  JOURNAL   J Biol Chem 274 (48), 33959-33965 (1999)
   PUBMED   10567358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094524.1 and
            JAXUCZ010000010.1.
            
            On Oct 3, 2005 this sequence version replaced NP_068624.1.
            
            Summary: The protein encoded by this gene is a member of the epsin
            protein family. Epsin proteins are endocytic adaptors that function
            in the formation of clatherin-coated vesicles. Epsins contain a
            highly conserved N-terminal homology domain that binds
            phosphatidylinositol 4,5-bisphosphate in the plasma membrane, two
            or three ubiquitin interacting motifs, two clathrin-binding motifs,
            a cluster of aspartate-proline-tryptophan/phenylalanine repeats,
            and two or three asparagine-proline-phenylalanine tripeptide
            repeats at the C-terminus. In mouse, simultaneous knockout of this
            gene and its paralog results in embryonic arrest due to disruption
            of Notch signaling, suggesting a role as a specialized endocytic
            adaptor. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (1) differs in its 5' UTR and
            lacks an alternate in-frame exon in the 5' coding region compared
            to variant 3. It encodes isoform a, which is shorter than isoform
            b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.42880.1,
                                           SRR26643297.34322.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..583
                     /product="epsin-2 isoform a"
                     /note="EPS-15-interacting protein 2; EH domain binding
                     protein epsin 2"
                     /calculated_mol_wt=62185
     Region          19..141
                     /region_name="ENTH_Epsin"
                     /note="Epsin N-Terminal Homology (ENTH) domain of Epsin
                     family; cd16990"
                     /db_xref="CDD:340787"
     Site            order(25,29..30,63,69,73)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:340787"
     Region          165..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CHU3; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95208; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Region          293..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Region          301..377
                     /region_name="6 X 3 AA repeats of [DE]-P-W"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Region          335..>399
                     /region_name="TM_PBP2"
                     /note="Transmembrane subunit (TM) found in Periplasmic
                     Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC)
                     transporters which generally bind type 2 PBPs. These types
                     of transporters consist of a PBP, two TMs, and two
                     cytoplasmic ABC ATPase subunits, and...; cl00427"
                     /db_xref="CDD:444901"
     Region          411..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Region          482..581
                     /region_name="3 X 3 AA repeats of N-P-F"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95208; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1Z3.1)"
     CDS             1..583
                     /gene="Epn2"
                     /coded_by="NM_021852.3:164..1915"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:60443"
                     /db_xref="RGD:619773"
ORIGIN      
        1 mttssirrqm knivnnysea eikvreatsn dpwgpssslm teiadltynv vafseimsmv
       61 wkrlndhgkn wrhvykaltl ldyliktgse rvaqqcreni faiqtlkdfq yidrdgkdqg
      121 invrekskql vallkdeerl kvervqalkt kermaqvatg vgsnqitfgr gssqpnlsts
      181 yseqeygkag gspasyhgst sprvsseleq arpqtsgeee lqlqlalams revaeqeerl
      241 rrgddlrlqm aleesrrdtv kvpkkkevka cckpgshsqq ttlldlmdal pssgpvaqkt
      301 epwstgtpan qtnpwggtva panisdpwps fgtkpaasvd pwgvpttasi qsvpknsdpw
      361 aasqqpasda gktadawgaa kpspasgsfe lfsnfngtvk ddfsefdnlr tskkpaesga
      421 svppqdsrtt spdlfesqsl tsasskpssa rktpesflgp naalvnldsl vtkpnppaqs
      481 lnpflapgaa apapvnpfqv nqpqpltlnq lrgspvlgss asfgsgpgve tvapmpsvap
      541 hsalgatgss ltplgptamn mvgsvgipps aaqpagttnp fll
//
LOCUS       NP_001013930             418 aa            linear   ROD 27-APR-2025
DEFINITION  trafficking protein particle complex subunit 13 [Rattus
            norvegicus].
ACCESSION   NP_001013930 XP_215475
VERSION     NP_001013930.2
DBSOURCE    REFSEQ: accession NM_001013908.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY312499.1, BC088172.1 and CO397574.1.
            
            On Sep 30, 2011 this sequence version replaced NP_001013930.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088172.1, FQ217190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..418
                     /product="trafficking protein particle complex subunit 13"
                     /note="UPF0533 protein C5orf44 homolog; trafficking
                     protein particle complex 13"
                     /calculated_mol_wt=46389
     Region          65..298
                     /region_name="DUF974"
                     /note="Protein of unknown function (DUF974); pfam06159"
                     /db_xref="CDD:461841"
     CDS             1..418
                     /gene="Trappc13"
                     /gene_synonym="RGD1306583"
                     /coded_by="NM_001013908.2:276..1532"
                     /db_xref="GeneID:294709"
                     /db_xref="RGD:1306583"
ORIGIN      
        1 mevnppkqeh llalkvmrlt kptlftnipv tceekdlpgd lfnqlmkddp stvngaeilm
       61 lgemltlpqn fgniflgetf ssyisvhnds nqvvkdilvk adlqtssqrl nlsasnaava
      121 elkpdccidd vihhevkeig thilvcavsy ttqggekmyf rkffkfqvlk pldvktkfyn
      181 aesdlssvtd evfleaqiqn ittspmfmek vslepsimyn vtelnsvnqa gecvstfgsr
      241 gylqpmdtrq ylyclkpkke faekagiikg vtvigkldiv wktnlgergr lqtsqlqrma
      301 pgygdvrlsl eaipdtvnle epfhitckit ncssertmdl vlemcnttsi hwcgisgrql
      361 gklhpssslc laltllssvq glqsvsglrl tdtflkrtye yddiaqvcvv saavevea
//
LOCUS       NP_113767                173 aa            linear   ROD 27-APR-2025
DEFINITION  protein tyrosine phosphatase type IVA 1 [Rattus norvegicus].
ACCESSION   NP_113767 XP_003750721
VERSION     NP_113767.1
DBSOURCE    REFSEQ: accession NM_031579.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Park,H., Seok,J., You,J.H., Kim,J.Y., Lim,J.Y. and Kim,G.J.
  TITLE     Increased phosphatase regenerating liver-1 trigger vascular
            remodeling in injured ovary via platelet-derived growth factor
            signaling pathway
  JOURNAL   Stem Cell Res Ther 13 (1), 95 (2022)
   PUBMED   35255961
  REMARK    GeneRIF: Increased phosphatase regenerating liver-1 trigger
            vascular remodeling in injured ovary via platelet-derived growth
            factor signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Kim,S.H., Kim,J.Y., Park,S.Y., Jeong,W.T., Kim,J.M., Bae,S.H. and
            Kim,G.J.
  TITLE     Activation of the EGFR-PI3K-CaM pathway by PRL-1-overexpressing
            placenta-derived mesenchymal stem cells ameliorates liver cirrhosis
            via ER stress-dependent calcium
  JOURNAL   Stem Cell Res Ther 12 (1), 551 (2021)
   PUBMED   34689832
  REMARK    GeneRIF: Activation of the EGFR-PI3K-CaM pathway by
            PRL-1-overexpressing placenta-derived mesenchymal stem cells
            ameliorates liver cirrhosis via ER stress-dependent calcium.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Schmidt,J., de Avila,J. and McLean,D.
  TITLE     Regulation of protein tyrosine phosphatase 4a1, B-cell
            translocation gene 2, nuclear receptor subfamily 4a1 and
            diacylglycerol O-acyltransferase 1 by follicle stimulating hormone
            in the rat ovary
  JOURNAL   Reprod Fertil Dev 18 (7), 757-765 (2006)
   PUBMED   17032584
  REMARK    GeneRIF: genes induced by FSH in rat Sertoli cells would also show
            hormonal regulation during rat folliculogenesis
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Sun,J.P., Wang,W.Q., Yang,H., Liu,S., Liang,F., Fedorov,A.A.,
            Almo,S.C. and Zhang,Z.Y.
  TITLE     Structure and biochemical properties of PRL-1, a phosphatase
            implicated in cell growth, differentiation, and tumor invasion
  JOURNAL   Biochemistry 44 (36), 12009-12021 (2005)
   PUBMED   16142898
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Wang,S.F., Liang,Q., Li,G.W. and Gao,K.
  TITLE     Gene expression profile in rat small intestinal allografts after
            cold preservation/reperfusion
  JOURNAL   World J Gastroenterol 11 (6), 885-889 (2005)
   PUBMED   15682487
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Zeng,Q., Dong,J.M., Guo,K., Li,J., Tan,H.X., Koh,V., Pallen,C.J.,
            Manser,E. and Hong,W.
  TITLE     PRL-3 and PRL-1 promote cell migration, invasion, and metastasis
  JOURNAL   Cancer Res 63 (11), 2716-2722 (2003)
   PUBMED   12782572
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Scarlato,M., Beesley,J. and Pleasure,D.
  TITLE     Analysis of oligodendroglial differentiation using cDNA arrays
  JOURNAL   J Neurosci Res 59 (3), 430-435 (2000)
   PUBMED   10679780
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Takano,S., Fukuyama,H., Fukumoto,M., Kimura,J., Xue,J.H., Ohashi,H.
            and Fujita,J.
  TITLE     PRL-1, a protein tyrosine phosphatase, is expressed in neurons and
            oligodendrocytes in the brain and induced in the cerebral cortex
            following transient forebrain ischemia
  JOURNAL   Brain Res Mol Brain Res 40 (1), 105-115 (1996)
   PUBMED   8840018
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Diamond,R.H., Cressman,D.E., Laz,T.M., Abrams,C.S. and Taub,R.
  TITLE     PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell
            growth
  JOURNAL   Mol Cell Biol 14 (6), 3752-3762 (1994)
   PUBMED   8196618
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097307.1 and JAXUCZ010000009.1.
            
            On Jun 26, 2012 this sequence version replaced XP_003750721.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097307.1, L27843.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..173
                     /product="protein tyrosine phosphatase type IVA 1"
                     /EC_number="3.1.3.48"
                     /note="protein-tyrosine phosphatase of regenerating liver
                     1; protein tyrosine phosphatase 4a1-like; protein tyrosine
                     phosphatase type IVA, member 1"
                     /calculated_mol_wt=19684
     mat_peptide     1..170
                     /product="Protein tyrosine phosphatase type IVA 1.
                     /id=PRO_0000094784"
                     /note="propagated from UniProtKB/Swiss-Prot (Q78EG7.1)"
                     /calculated_mol_wt=19471
     Region          1..167
                     /region_name="PTP-IVa1"
                     /note="protein tyrosine phosphatase type IVA 1; cd18537"
                     /db_xref="CDD:350513"
     Site            order(5,7,72..73,108..110,137..140,142,144)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350513"
     Site            order(47,53..54,56,59,64..68)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:350513"
     Region          97..132
                     /region_name="Interaction with ATF5.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q78EG7.1)"
     Site            170
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q78EG7.1)"
     CDS             1..173
                     /gene="Ptp4a1"
                     /gene_synonym="PRL-1"
                     /coded_by="NM_031579.3:718..1239"
                     /db_xref="GeneID:29463"
                     /db_xref="RGD:61970"
ORIGIN      
        1 marmnrpapv evtyknmrfl ithnptnatl nkfieelkky gvttivrvce atydttlvek
       61 egihvldwpf ddgappsnqi vddwlslvki kfreepgcci avhcvaglgr apvlvalali
      121 eggmkyedav qfirqkrrga fnskqllyle kyrpkmrlrf kdsnghrnnc ciq
//
LOCUS       NP_445795                433 aa            linear   ROD 27-APR-2025
DEFINITION  serine/threonine-protein kinase DCLK1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_445795
VERSION     NP_445795.1
DBSOURCE    REFSEQ: accession NM_053343.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Vitali,F., Tortora,K., Di Paola,M., Bartolucci,G., Menicatti,M., De
            Filippo,C. and Caderni,G.
  TITLE     Intestinal microbiota profiles in a genetic model of colon
            tumorigenesis correlates with colon cancer biomarkers
  JOURNAL   Sci Rep 12 (1), 1432 (2022)
   PUBMED   35082322
  REMARK    GeneRIF: Intestinal microbiota profiles in a genetic model of colon
            tumorigenesis correlates with colon cancer biomarkers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Nakane,T., Matsumoto,S., Iida,S., Ido,A., Fukunaga,K., Murao,K. and
            Sugiyama,Y.
  TITLE     Candidate plasticity gene 16 and jun dimerization protein 2 are
            involved in the suppression of insulin gene expression in rat
            pancreatic INS-1 beta-cells
  JOURNAL   Mol Cell Endocrinol 527, 111240 (2021)
   PUBMED   33676985
  REMARK    GeneRIF: Candidate plasticity gene 16 and jun dimerization protein
            2 are involved in the suppression of insulin gene expression in rat
            pancreatic INS-1 beta-cells.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Nakane,T., Ido,A., Higuchi,T., Todaka,H., Morisawa,K., Nagamine,T.,
            Fukunaga,K., Sakamoto,S., Murao,K. and Sugiyama,Y.
  TITLE     Candidate plasticity gene 16 mediates suppression of insulin gene
            expression in rat insulinoma INS-1cells under glucotoxic conditions
  JOURNAL   Biochem Biophys Res Commun 512 (2), 189-195 (2019)
   PUBMED   30879761
  REMARK    GeneRIF: These results suggest that CPG16 plays a role in the
            suppression of insulin gene expression in pancreatic beta-cells
            under glucotoxic conditions.
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Quan,X., Huang,L., Yang,Y., Ma,T., Liu,Z., Ge,J., Huang,J. and
            Luo,Z.
  TITLE     Potential Mechanism of Neurite Outgrowth Enhanced by Electrical
            Stimulation: Involvement of MicroRNA-363-5p Targeting DCLK1
            Expression in Rat
  JOURNAL   Neurochem Res 42 (2), 513-525 (2017)
   PUBMED   27900578
  REMARK    GeneRIF: Electrical stimulated-neurite outgrowth is regulated by
            MicroRNA-363-5p through targeting of DCLK1.
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Lipka,J., Kapitein,L.C., Jaworski,J. and Hoogenraad,C.C.
  TITLE     Microtubule-binding protein doublecortin-like kinase 1 (DCLK1)
            guides kinesin-3-mediated cargo transport to dendrites
  JOURNAL   EMBO J 35 (3), 302-318 (2016)
   PUBMED   26758546
  REMARK    GeneRIF: The authors found that microtubule-binding protein
            doublecortin-like kinase 1 (DCLK1) labels a subset of dendritic
            microtubules and is required for KIF1-dependent dense-core vesicles
            (DCVs) trafficking into dendrites and dendrite development.
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Lin,P.T., Gleeson,J.G., Corbo,J.C., Flanagan,L. and Walsh,C.A.
  TITLE     DCAMKL1 encodes a protein kinase with homology to doublecortin that
            regulates microtubule polymerization
  JOURNAL   J Neurosci 20 (24), 9152-9161 (2000)
   PUBMED   11124993
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Mizuguchi,M., Qin,J., Yamada,M., Ikeda,K. and Takashima,S.
  TITLE     High expression of doublecortin and KIAA0369 protein in fetal brain
            suggests their specific role in neuronal migration
  JOURNAL   Am J Pathol 155 (5), 1713-1721 (1999)
   PUBMED   10550327
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Vreugdenhil,E., Datson,N., Engels,B., de Jong,J., van
            Koningsbruggen,S., Schaaf,M. and de Kloet,E.R.
  TITLE     Kainate-elicited seizures induce mRNA encoding a CaMK-related
            peptide: a putative modulator of kinase activity in rat hippocampus
  JOURNAL   J Neurobiol 39 (1), 41-50 (1999)
   PUBMED   10213452
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Berke,J.D., Paletzki,R.F., Aronson,G.J., Hyman,S.E. and Gerfen,C.R.
  TITLE     A complex program of striatal gene expression induced by
            dopaminergic stimulation
  JOURNAL   J Neurosci 18 (14), 5301-5310 (1998)
   PUBMED   9651213
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Hevroni,D., Rattner,A., Bundman,M., Lederfein,D., Gabarah,A.,
            Mangelus,M., Silverman,M.A., Kedar,H., Naor,C., Kornuc,M.,
            Hanoch,T., Seger,R., Theill,L.E., Nedivi,E., Richter-Levin,G. and
            Citri,Y.
  TITLE     Hippocampal plasticity involves extensive gene induction and
            multiple cellular mechanisms
  JOURNAL   J Mol Neurosci 10 (2), 75-98 (1998)
   PUBMED   9699150
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000002.1.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. The typical protein
            encoded by this gene contains two N-terminal doublecortin domains,
            which bind microtubules and regulate microtubule polymerization, a
            C-terminal serine/threonine protein kinase domain, which shows
            substantial homology to Ca2+/calmodulin-dependent protein kinase,
            and a serine/proline-rich domain in between the doublecortin and
            the protein kinase domains, which mediates multiple protein-protein
            interactions. The microtubule-polymerizing activity of the protein
            is independent of its protein kinase activity. This gene is
            involved in several different cellular processes, including
            neuronal migration, retrograde transport, neuronal apoptosis and
            neurogenesis. Multiple transcript variants generated by two
            alternative promoter usage and alternative splicing have been
            found, but the full-length nature of the variant produced from the
            5' promoter has not been determined. Current reference sequence
            data represents two alternatively spliced transcript variants
            produced from the 3' promoter and their protein products lack the
            doublecortin domain.[provided by RefSeq, Sep 2010].
            
            Transcript Variant: Transcript Variant: This variant [1, also known
            as DCLK-short-A, DCK-beta2, KIAA0369-BL or cpg16 (candidate
            plasticity gene 16)] is produced from the 3' promoter. It encodes
            isoform 1, which contains a serine/proline-rich domain and a
            protein kinase domain.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U78857.1, SRR26643298.10973.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..433
                     /product="serine/threonine-protein kinase DCLK1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="double cortin and calcium/calmodulin-dependent
                     protein kinase-like 1; serine/threonine-protein kinase
                     DCLK1; doublecortin-like and CAM kinase-like 1"
                     /calculated_mol_wt=47550
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08875.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Region          82..339
                     /region_name="STKc_DCKL"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Doublecortin-like kinase (also called Doublecortin-like
                     and CAM kinase-like); cd14095"
                     /db_xref="CDD:270997"
     Site            order(89..93,97,110,112,142,158..161,165,167,203..204,206,
                     208..209,211,225..226,229,241..245,247)
                     /site_type="active"
                     /db_xref="CDD:270997"
     Site            order(89..92,97,110,112,142,158..161,165,208..209,211,
                     225..226)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270997"
     Site            order(93,165,167,203..204,206,208,229,241..245,247)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270997"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            order(225..234,237..245)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270997"
     Region          388..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08875.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLM8; propagated from
                     UniProtKB/Swiss-Prot (O08875.1)"
     CDS             1..433
                     /gene="Dclk1"
                     /gene_synonym="Ania4; Cpg16; Dcamkl1"
                     /coded_by="NM_053343.3:147..1448"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:83825"
                     /db_xref="RGD:68437"
ORIGIN      
        1 mlelievngt pgsqlstprs gkspspspts pgslrkqris qhggsstsls stkvcssmde
       61 ndgpgeeesd egfqipatit erykvgrtig dgnfavvkec ierstareya lkiikkskcr
      121 gkehmiqnev silrrvkhpn ivllieemdv ptelylvmel vkggdlfdai tstskyterd
      181 asgmlynlas aikylhslni vhrdikpenl lvyehqdgsk slklgdfgla tivdgplytv
      241 cgtptyvape iiaetgyglk vdiwaagvit yillcgfppf rgsgddqevl fdqilmgqvd
      301 fpspywdnvs dsakelinmm llvnvdqrfs avqvlehpwv nddglpeneh qlsvagkikk
      361 hfntgpkpss taagvsviat taldkerqvf rrrrnqdvrg rykaqpappe lnsesedysp
      421 sssetvrspn spf
//
LOCUS       NP_001185733             937 aa            linear   ROD 27-APR-2025
DEFINITION  diacylglycerol kinase theta [Rattus norvegicus].
ACCESSION   NP_001185733 XP_002728115
VERSION     NP_001185733.1
DBSOURCE    REFSEQ: accession NM_001198804.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Goldschmidt,H.L., Tu-Sekine,B., Volk,L., Anggono,V., Huganir,R.L.
            and Raben,D.M.
  TITLE     DGKtheta; Catalytic Activity Is Required for Efficient Recycling of
            Presynaptic Vesicles at Excitatory Synapses
  JOURNAL   Cell Rep 14 (2), 200-207 (2016)
   PUBMED   26748701
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Cai,K., Lucki,N.C. and Sewer,M.B.
  TITLE     Silencing diacylglycerol kinase-theta expression reduces steroid
            hormone biosynthesis and cholesterol metabolism in human
            adrenocortical cells
  JOURNAL   Biochim Biophys Acta 1841 (4), 552-562 (2014)
   PUBMED   24369117
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Cai,K. and Sewer,M.B.
  TITLE     Diacylglycerol kinase theta; couples farnesoid X receptor-dependent
            bile acid signalling to Akt activation and glucose homoeostasis in
            hepatocytes
  JOURNAL   Biochem J 454 (2), 267-274 (2013)
   PUBMED   23767959
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Cai,K. and Sewer,M.B.
  TITLE     cAMP-stimulated transcription of DGKtheta; requires steroidogenic
            factor 1 and sterol regulatory element binding protein 1
  JOURNAL   J Lipid Res 54 (8), 2121-2132 (2013)
   PUBMED   23610160
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Tu-Sekine,B. and Raben,D.M.
  TITLE     Dual regulation of diacylglycerol kinase (DGK)-theta;: polybasic
            proteins promote activation by phospholipids and increase substrate
            affinity
  JOURNAL   J Biol Chem 287 (50), 41619-41627 (2012)
   PUBMED   23091060
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Tabellini,G., Billi,A.M., Fala,F., Cappellini,A., Evagelisti,C.,
            Manzoli,L., Cocco,L. and Martelli,A.M.
  TITLE     Nuclear diacylglycerol kinase-theta is activated in response to
            nerve growth factor stimulation of PC12 cells
  JOURNAL   Cell Signal 16 (11), 1263-1271 (2004)
   PUBMED   15337525
  REMARK    GeneRIF: nuclear DGK-theta is a down-stream target of nerve growth
            factor signaling in PC12 cells.
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Tabellini,G., Bortul,R., Santi,S., Riccio,M., Baldini,G.,
            Cappellini,A., Billi,A.M., Berezney,R., Ruggeri,A., Cocco,L. and
            Martelli,A.M.
  TITLE     Diacylglycerol kinase-theta is localized in the speckle domains of
            the nucleus
  JOURNAL   Exp Cell Res 287 (1), 143-154 (2003)
   PUBMED   12799190
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Bregoli,L., Baldassare,J.J. and Raben,D.M.
  TITLE     Nuclear diacylglycerol kinase-theta is activated in response to
            alpha-thrombin
  JOURNAL   J Biol Chem 276 (26), 23288-23295 (2001)
   PUBMED   11309392
  REMARK    Erratum:[J Biol Chem 2002 Mar 29;277(13):11614-5]
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Houssa,B., de Widt,J., Kranenburg,O., Moolenaar,W.H. and van
            Blitterswijk,W.J.
  TITLE     Diacylglycerol kinase theta binds to and is negatively regulated by
            active RhoA
  JOURNAL   J Biol Chem 274 (11), 6820-6822 (1999)
   PUBMED   10066731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Nov 11, 2010 this sequence version replaced XP_002728115.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.48043.1,
                                           SRR26643299.53668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..937
                     /product="diacylglycerol kinase theta"
                     /EC_number="2.7.1.107"
                     /EC_number="2.7.1.93"
                     /note="DGKtheta; DAG kinase theta"
                     /calculated_mol_wt=102415
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P5E8; propagated from
                     UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P5E8; propagated from
                     UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Region          54..107
                     /region_name="C1_DGKtheta_typeV_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in type V diacylglycerol kinase, DAG kinase
                     theta, and similar proteins; cd20803"
                     /db_xref="CDD:410353"
     Region          111..166
                     /region_name="C1_DGKtheta_typeV_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in type V diacylglycerol kinase, DAG kinase
                     theta, and similar proteins; cd20804"
                     /db_xref="CDD:410354"
     Region          178..240
                     /region_name="C1_DGKtheta_typeV_rpt3"
                     /note="third protein kinase C conserved region 1 (C1
                     domain) found in type V diacylglycerol kinase, DAG kinase
                     theta, and similar proteins; cd20854"
                     /db_xref="CDD:410404"
     Region          293..389
                     /region_name="RA1_DAGK-theta"
                     /note="Ras-associating (RA) domain 1 found in
                     diacylgylcerol kinase theta (DAGK-theta) and similar
                     proteins; cd17111"
                     /db_xref="CDD:340631"
     Region          359..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Region          392..486
                     /region_name="RA2_DAGK-theta"
                     /note="Ras-associating (RA) domain 2 found in
                     diacylgylcerol kinase theta (DAGK-theta) and similar
                     proteins; cd01783"
                     /db_xref="CDD:340481"
     Region          550..554
                     /region_name="LXXLL motif 1.
                     /evidence=ECO:0000250|UniProtKB:P52824"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Region          569..573
                     /region_name="LXXLL motif 2.
                     /evidence=ECO:0000250|UniProtKB:P52824"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZEY4.1)"
     Region          585..709
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          736..888
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          911..937
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZEY4.1)"
     CDS             1..937
                     /gene="Dgkq"
                     /coded_by="NM_001198804.1:88..2901"
                     /db_xref="GeneID:100361138"
                     /db_xref="RGD:2320722"
ORIGIN      
        1 mataaesgar twpgsgsprl gspagspvlg isgrarpgsg pertgraigs vapghsfrkv
       61 tltkptfchl csdfiwglag flcdvcnfms hekclkqvkt pctsiapslv rvpvahcfgs
      121 lglykrkfcv vcrkslevpa frcevcelhv hpdcvpfacs dcrqchqdgq hdydtyhhhw
      181 regnlpsgar cevcrktcgs sdvlagvrce wcgvqahsvc staltpectf grlrsmvlpp
      241 scvrllsrnf skmhcfripe tmvlelgdgd dgldgsaavg tgrevsaate stkqtlkifd
      301 gndsmrknqf rlvtvsrlar neevmeaalr ayyinedpkd fqlqalpltl lsgnaqalgk
      361 agtteeetsk dsgpgdsvpe awvirslprt qeilkiypdw lkvgvayvsi rvnsqstars
      421 vvqevlplfg rqvedqerfq lievlmssrq vqrtvlvdee plldrlrdir qtsvrqasqt
      481 rfyvaearav tphvslfvgg lppglspqdy snllheamat kaavvsvshv yslqgavvld
      541 vtcfaeaerl ymlardtavh grpltalvlp dvlhtklppd ccpllvfvnp ksgglkgrel
      601 lcsfrkllnp hqvfeltngg plpgfhlfsq vpcfrvlvcg gdgtvgwvla aleetrrhla
      661 cpepsvailp lgtgndlgrv lrwgagysge dpfsvlvsvd eadavlmdrw tilldaheid
      721 stennvvete ppkivqmnny cgigidaels ldfhqareee pgkftsrfhn kgvyvrvglq
      781 kishsrslhk eirlqveqqe velpsiegli finipswgsg adlwgsdsds rfekpriddg
      841 llevvgvtgv vhmgqvqggl rsgiriaqgs yfrvtllkat pvqvdgepwi qapghmiisa
      901 tapkvhmlrk akqkprkaga irdtrvdtlp apegnpl
//
LOCUS       NP_001257769             315 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group I member 3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257769
VERSION     NP_001257769.1
DBSOURCE    REFSEQ: accession NM_001270840.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Yamada,T., Cohen,S.M. and Lake,B.G.
  TITLE     Critical evaluation of the human relevance of the mode of action
            for rodent liver tumor formation by activators of the constitutive
            androstane receptor (CAR)
  JOURNAL   Crit Rev Toxicol 51 (5), 373-394 (2021)
   PUBMED   34264181
  REMARK    GeneRIF: Critical evaluation of the human relevance of the mode of
            action for rodent liver tumor formation by activators of the
            constitutive androstane receptor (CAR).
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Gabbia,D., Pozza,A.D., Albertoni,L., Lazzari,R., Zigiotto,G.,
            Carrara,M., Baldo,V., Baldovin,T., Floreani,A. and Martin,S.
  TITLE     Pregnane X receptor and constitutive androstane receptor modulate
            differently CYP3A-mediated metabolism in early- and late-stage
            cholestasis
  JOURNAL   World J Gastroenterol 23 (42), 7519-7530 (2017)
   PUBMED   29204052
  REMARK    GeneRIF: nuclear expression virtually disappeared in the late stage
            of cholestatic injury, after an initial increase
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Forbes,K.P., Kouranova,E., Tinker,D., Janowski,K., Cortner,D.,
            McCoy,A. and Cui,X.
  TITLE     Creation and Preliminary Characterization of Pregnane X Receptor
            and Constitutive Androstane Receptor Knockout Rats
  JOURNAL   Drug Metab Dispos 45 (10), 1068-1076 (2017)
   PUBMED   28716828
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Fujino,C., Tamura,Y., Tange,S., Nakajima,H., Sanoh,S., Watanabe,Y.,
            Uramaru,N., Kojima,H., Yoshinari,K., Ohta,S. and Kitamura,S.
  TITLE     Metabolism of methiocarb and carbaryl by rat and human livers and
            plasma, and effect on their PXR, CAR and PPARalpha activities
  JOURNAL   J Toxicol Sci 41 (5), 677-691 (2016)
   PUBMED   27665777
  REMARK    GeneRIF: Metabolism of methiocarb and carbaryl does not alter CAR
            activity.
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Shao,Y.Y., Huang,J., Ma,Y.R., Han,M., Ma,K., Qin,H.Y., Rao,Z. and
            Wu,X.A.
  TITLE     Serum serotonin reduced the expression of hepatic transporter Mrp2
            and P-gp via regulating nuclear receptor CAR in PI-IBS rats
  JOURNAL   Can J Physiol Pharmacol 93 (8), 633-639 (2015)
   PUBMED   26053941
  REMARK    GeneRIF: Serum 5-HT regulates the expression of Mrp2 and P-gp, and
            the underlying mechanism may be related to the altered expression
            of the nuclear receptor constitutive androstane receptor.
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Numazawa,S., Shindo,S., Maruyama,K., Chibana,F., Kawahara,Y.,
            Ashino,T., Tanaka,S. and Yoshida,T.
  TITLE     Impaired nuclear translocation of CAR in hepatic preneoplastic
            lesions: association with an attenuated CYP2B induction by
            phenobarbital
  JOURNAL   FEBS Lett 579 (17), 3560-3564 (2005)
   PUBMED   15953603
  REMARK    GeneRIF: CAR expressed in the hepatic preneoplastic lesions of rats
            is resistant to nuclear translocation and transactivation of the
            phenobarbital(PB) responsive enhancer module upon PB treatment.
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Yoshinari,K., Kobayashi,K., Moore,R., Kawamoto,T. and Negishi,M.
  TITLE     Identification of the nuclear receptor CAR:HSP90 complex in mouse
            liver and recruitment of protein phosphatase 2A in response to
            phenobarbital
  JOURNAL   FEBS Lett 548 (1-3), 17-20 (2003)
   PUBMED   12885400
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Gonzalez,M.M. and Carlberg,C.
  TITLE     Cross-repression, a functional consequence of the physical
            interaction of non-liganded nuclear receptors and POU domain
            transcription factors
  JOURNAL   J Biol Chem 277 (21), 18501-18509 (2002)
   PUBMED   11891224
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Yoshinari,K., Sueyoshi,T., Moore,R. and Negishi,M.
  TITLE     Nuclear receptor CAR as a regulatory factor for the sexually
            dimorphic induction of CYB2B1 gene by phenobarbital in rat livers
  JOURNAL   Mol Pharmacol 59 (2), 278-284 (2001)
   PUBMED   11160864
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Xie,W., Barwick,J.L., Simon,C.M., Pierce,A.M., Safe,S.,
            Blumberg,B., Guzelian,P.S. and Evans,R.M.
  TITLE     Reciprocal activation of xenobiotic response genes by nuclear
            receptors SXR/PXR and CAR
  JOURNAL   Genes Dev 14 (23), 3014-3023 (2000)
   PUBMED   11114890
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089763.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            at the 5' end of an exon and uses an alternate splice junction at
            the 3' end of an exon that extends the exon to an in-frame stop
            codon compared to variant 1. The resulting isoform (2) is shorter
            at the C-terminus and lacks a single internal aa compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..315
                     /product="nuclear receptor subfamily 1 group I member 3
                     isoform 2"
                     /note="constitutive androstane receptor; strain Fischer
                     nuclear receptor (CAR); nuclear receptor constitutive
                     active receptor"
                     /calculated_mol_wt=36006
     Region          21..92
                     /region_name="NR_DBD_VDR_like"
                     /note="The DNA-binding domain of vitamin D receptors (VDR)
                     like nuclear receptor family is composed of two C4-type
                     zinc fingers; cd07156"
                     /db_xref="CDD:143531"
     Site            order(21,24,38,41,57,63,73,76)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143531"
     Site            order(31..33,39..40,42,46..47,70..71,77,91..92)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143531"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q14994; propagated from
                     UniProtKB/Swiss-Prot (Q9QUS1.1)"
     Site            order(58..59,72,89..90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143531"
     Region          116..315
                     /region_name="NR_LBD"
                     /note="The ligand binding domain of nuclear receptors, a
                     family of ligand-activated transcription regulators;
                     cl11397"
                     /db_xref="CDD:472173"
     Site            order(171..172,175,178..179,208..209,212..213,216,219,251)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132726"
     Site            order(180,183,187,192,197..198,200..201,204..205)
                     /site_type="active"
                     /note="coregulator recognition site [active]"
                     /db_xref="CDD:132726"
     CDS             1..315
                     /gene="Nr1i3"
                     /gene_synonym="CAR"
                     /coded_by="NM_001270840.1:150..1097"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65035"
                     /db_xref="RGD:621400"
ORIGIN      
        1 mtatltletm tseeeygprn cvvcgdratg yhfhaltceg ckgffrrtvs ktigpicpfa
       61 grcevskaqr rhcpacrlqk clnvgmrkdm ilsaealalr rarqarrraq kaslqlsqqq
      121 keliqtllga htrhvgpmfd qfvqfrppay lfshhrpfqp lapvlpllth fadintfmvq
      181 qiikftkdlp lfrsltmedq isllkgaave ilhislnttf clqtqnffcg plcykmedav
      241 hgfqyeflel iihfhktlkr lqlqepeyal maamalfspd rpgvtqreei dqlqeevali
      301 lnnhimeqqs rlqsr
//
LOCUS       NP_001258052             241 aa            linear   ROD 27-APR-2025
DEFINITION  pro-neuregulin-1, membrane-bound isoform isoform 6 [Rattus
            norvegicus].
ACCESSION   NP_001258052
VERSION     NP_001258052.1
DBSOURCE    REFSEQ: accession NM_001271123.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Yuan,J., Xu,B., Ma,J., Pang,X., Fu,Y., Liang,M., Wang,M., Pan,Y.,
            Duan,Y., Tang,M., Zhu,B., Laher,I. and Li,S.
  TITLE     MOTS-c and aerobic exercise induce cardiac physiological adaptation
            via NRG1/ErbB4/CEBPbeta modification in rats
  JOURNAL   Life Sci 315, 121330 (2023)
   PUBMED   36584915
  REMARK    GeneRIF: MOTS-c and aerobic exercise induce cardiac physiological
            adaptation via NRG1/ErbB4/CEBPbeta modification in rats.
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Wang,Y.K., Yang,W.X., Liu,R., Guo,J.B., Zhang,Y.M., Li,K., Lu,Y.
            and Wang,J.
  TITLE     Changes in Type II NRG-1 Expression during Regeneration Following
            Autologous Nerve Transplantation in Rats
  JOURNAL   Turk Neurosurg 33 (1), 18-24 (2023)
   PUBMED   35416257
  REMARK    GeneRIF: Changes in Type II NRG-1 Expression during Regeneration
            Following Autologous Nerve Transplantation in Rats.
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Banerjee,S., Mishra,S., Xu,W., Thompson,W.E. and Chowdhury,I.
  TITLE     Neuregulin-1 signaling regulates cytokines and chemokines
            expression and secretion in granulosa cell
  JOURNAL   J Ovarian Res 15 (1), 86 (2022)
   PUBMED   35883098
  REMARK    GeneRIF: Neuregulin-1 signaling regulates cytokines and chemokines
            expression and secretion in granulosa cell.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Li,S., Wang,M., Ma,J., Pang,X., Yuan,J., Pan,Y., Fu,Y. and Laher,I.
  TITLE     MOTS-c and Exercise Restore Cardiac Function by Activating of
            NRG1-ErbB Signaling in Diabetic Rats
  JOURNAL   Front Endocrinol (Lausanne) 13, 812032 (2022)
   PUBMED   35370955
  REMARK    GeneRIF: MOTS-c and Exercise Restore Cardiac Function by Activating
            of NRG1-ErbB Signaling in Diabetic Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Xu,L., Li,Z., Rong,J. and Lang,L.
  TITLE     Effect of regulation of the NRG1/ErbB4 signaling pathway on the
            visual cortex synaptic plasticity of amblyopic adult rats
  JOURNAL   J Biochem Mol Toxicol 35 (9), e22841 (2021)
   PUBMED   34273906
  REMARK    GeneRIF: Effect of regulation of the NRG1/ErbB4 signaling pathway
            on the visual cortex synaptic plasticity of amblyopic adult rats.
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Meyer,D. and Birchmeier,C.
  TITLE     Multiple essential functions of neuregulin in development
  JOURNAL   Nature 378 (6555), 386-390 (1995)
   PUBMED   7477375
  REMARK    Erratum:[Nature 1995 Dec 14;378(6558):753]
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Sliwkowski,M.X., Schaefer,G., Akita,R.W., Lofgren,J.A.,
            Fitzpatrick,V.D., Nuijens,A., Fendly,B.M., Cerione,R.A.,
            Vandlen,R.L. and Carraway,K.L. 3rd.
  TITLE     Coexpression of erbB2 and erbB3 proteins reconstitutes a high
            affinity receptor for heregulin
  JOURNAL   J Biol Chem 269 (20), 14661-14665 (1994)
   PUBMED   7514177
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Wen,D., Suggs,S.V., Karunagaran,D., Liu,N., Cupples,R.L., Luo,Y.,
            Janssen,A.M., Ben-Baruch,N., Trollinger,D.B., Jacobsen,V.L. et al.
  TITLE     Structural and functional aspects of the multiplicity of Neu
            differentiation factors
  JOURNAL   Mol Cell Biol 14 (3), 1909-1919 (1994)
   PUBMED   7509448
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Wen,D., Peles,E., Cupples,R., Suggs,S.V., Bacus,S.S., Luo,Y.,
            Trail,G., Hu,S., Silbiger,S.M., Levy,R.B. et al.
  TITLE     Neu differentiation factor: a transmembrane glycoprotein containing
            an EGF domain and an immunoglobulin homology unit
  JOURNAL   Cell 69 (3), 559-572 (1992)
   PUBMED   1349853
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Peles,E., Bacus,S.S., Koski,R.A., Lu,H.S., Wen,D., Ogden,S.G.,
            Levy,R.B. and Yarden,Y.
  TITLE     Isolation of the neu/HER-2 stimulatory ligand: a 44 kd glycoprotein
            that induces differentiation of mammary tumor cells
  JOURNAL   Cell 69 (1), 205-216 (1992)
   PUBMED   1348215
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence and the 3' UTR and coding sequence compared to
            variant 1. The resulting isoform (6) has shorter and distinct N-
            and C-termini compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U02315.1, SRR26643294.54107.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..241
                     /product="pro-neuregulin-1, membrane-bound isoform isoform
                     6"
                     /note="neuregulin 1 type III beta 3; pro-NRG1; glial
                     growth factor"
                     /calculated_mol_wt=26081
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43322.1)"
     Region          37..129
                     /region_name="Ig_Pro_neuregulin-1"
                     /note="Immunoglobulin (Ig)-like domain found in neuregulin
                     (NRG)-1; cd05895"
                     /db_xref="CDD:409476"
     Region          37..43
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409476"
     Region          51..59
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409476"
     Region          66..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409476"
     Region          85..90
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409476"
     Region          95..99
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409476"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409476"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43322.1)"
     Region          121..129
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409476"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43322.1)"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43322.1)"
     Region          190..220
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     CDS             1..241
                     /gene="Nrg1"
                     /coded_by="NM_001271123.1:345..1070"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:112400"
                     /db_xref="RGD:621341"
ORIGIN      
        1 mserkegrgk gkgkkkdrgs rgkpgpaegd pspalpprlk emksqesaag sklvlrcets
       61 seysslrfkw fkngnelnrk nkpenikiqk kpgkselrin kasladsgey mckvisklgn
      121 dsasanitiv esnefitgmp astetayvss espirisvst egantsssts tsttgtshli
      181 kcaekektfc vnggecftvk dlsnpsrylc kcpneftgdr cqnyvmasfy ststpflslp
      241 e
//
LOCUS       NP_001178610             299 aa            linear   ROD 27-APR-2025
DEFINITION  N-acetylaspartate synthetase [Rattus norvegicus].
ACCESSION   NP_001178610 XP_223538
VERSION     NP_001178610.1
DBSOURCE    REFSEQ: accession NM_001191681.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Di Pietro,V., Amorini,A.M., Tavazzi,B., Vagnozzi,R., Logan,A.,
            Lazzarino,G., Signoretti,S., Lazzarino,G. and Belli,A.
  TITLE     The molecular mechanisms affecting N-acetylaspartate homeostasis
            following experimental graded traumatic brain injury
  JOURNAL   Mol Med 20 (1), 147-157 (2014)
   PUBMED   24515258
  REMARK    GeneRIF: The decrease in N-acetylaspartate following severe
            traumatic brain injury was characterized by profound mitochondrial
            malfunctioning, dramatic repression of Nat8l gene and concomitant
            increase in the ASPA gene and protein levels.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Becker,I., Lodder,J., Gieselmann,V. and Eckhardt,M.
  TITLE     Molecular characterization of N-acetylaspartylglutamate synthetase
  JOURNAL   J Biol Chem 285 (38), 29156-29164 (2010)
   PUBMED   20643647
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Ariyannur,P.S., Moffett,J.R., Manickam,P., Pattabiraman,N.,
            Arun,P., Nitta,A., Nabeshima,T., Madhavarao,C.N. and
            Namboodiri,A.M.
  TITLE     Methamphetamine-induced neuronal protein NAT8L is the NAA
            biosynthetic enzyme: implications for specialized acetyl coenzyme A
            metabolism in the CNS
  JOURNAL   Brain Res 1335, 1-13 (2010)
   PUBMED   20385109
  REMARK    GeneRIF: Asp-NAT/NAT8L and NAA immunoreactivities correlate very
            well in rat brain, with primary localization in neurons, including
            cortical pyramidal neurons and granule cells of the hippocampus.
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wiame,E., Tyteca,D., Pierrot,N., Collard,F., Amyere,M., Noel,G.,
            Desmedt,J., Nassogne,M.C., Vikkula,M., Octave,J.N., Vincent,M.F.,
            Courtoy,P.J., Boltshauser,E. and van Schaftingen,E.
  TITLE     Molecular identification of aspartate N-acetyltransferase and its
            mutation in hypoacetylaspartia
  JOURNAL   Biochem J 425 (1), 127-136 (2009)
   PUBMED   19807691
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Arun,P., Moffett,J.R. and Namboodiri,A.M.
  TITLE     Evidence for mitochondrial and cytoplasmic N-acetylaspartate
            synthesis in SH-SY5Y neuroblastoma cells
  JOURNAL   Neurochem Int 55 (4), 219-225 (2009)
   PUBMED   19524112
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Niwa,M., Nitta,A., Cen,X., Kitaichi,K., Ozaki,N., Yamada,K. and
            Nabeshima,T.
  TITLE     A novel molecule 'shati' increases dopamine uptake via the
            induction of tumor necrosis factor-alpha in pheochromocytoma-12
            cells
  JOURNAL   J Neurochem 107 (6), 1697-1708 (2008)
   PUBMED   19014384
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Ariyannur,P.S., Madhavarao,C.N. and Namboodiri,A.M.
  TITLE     N-acetylaspartate synthesis in the brain: mitochondria vs.
            microsomes
  JOURNAL   Brain Res 1227, 34-41 (2008)
   PUBMED   18621030
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jul 17, 2010 this sequence version replaced XP_223538.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.44766.1,
                                           SRR26643298.54952.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840114 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..299
                     /product="N-acetylaspartate synthetase"
                     /EC_number="2.3.1.17"
                     /note="NAA synthetase; N-acetyltransferase 8-like protein"
                     /calculated_mol_wt=32588
     Region          44..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVU9.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZVU9.1)"
     Region          169..269
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     CDS             1..299
                     /gene="Nat8l"
                     /gene_synonym="RGD1305719"
                     /coded_by="NM_001191681.1:1..900"
                     /db_xref="GeneID:289727"
                     /db_xref="RGD:1305719"
ORIGIN      
        1 mhcgppdmvc etkivatedh ealpgakkda llaaagamwp plpaapgpaa apppaagpqp
       61 hggtggagpp egrgvciref raaeqeaarr ifydgileri pntafrglrq hprtqllyal
      121 laalcfavtr sllltclvpa gllalryyys rkvilaylec alhtdmadie qyymkppgsc
      181 fwvavldgnv vgivaarahe edntvellrm svdsrfrgkg iakalgrrvl efamlhnysa
      241 vvlgttavkv aahklyeslg frhmgasdhy vlpgmtlsla erlffqvryh ryrlqlree
//
LOCUS       NP_001258176             119 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 8 [Rattus norvegicus].
ACCESSION   NP_001258176
VERSION     NP_001258176.1
DBSOURCE    REFSEQ: accession NM_001271247.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 119)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 119)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1 and FM033648.1.
            
            Transcript Variant: This variant (8) differs in 5' UTR and 5'
            coding region, compared to variant 3. This results in a protein
            (isoform 8) that has a shorter N-terminus compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM033648.1, SRR26360172.21687.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..119
                     /product="cAMP-responsive element modulator isoform 8"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=13409
     Region          63..117
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          64..116
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(64,68,70..72,74..76,78..79,81..83)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(82,85,89..90,92..93,96..97,99..100,103,106..107,
                     110..111,113..114)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..119
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271247.1:218..577"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mmyphftdee tdlapshmaa atgdmptyqi rapttalpqg vvmaaspgsl hspqqlaeea
       61 trkrelrlmk nreaarecrr kkkeyvkcle nrvavlenqn ktlieelkal kdlychkae
//
LOCUS       NP_001248316             236 aa            linear   ROD 27-APR-2025
DEFINITION  A-type potassium channel modulatory protein KCNIP1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001248316
VERSION     NP_001248316.1
DBSOURCE    REFSEQ: accession NM_001261387.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Del Pino,J., Frejo,M.T., Baselga,M.J.A., Capo,M.A., Moyano,P.,
            Garcia,J.M. and Diaz,M.J.
  TITLE     Neuroprotective or neurotoxic effects of 4-aminopyridine mediated
            by KChIP1 regulation through adjustment of Kv 4.3 potassium
            channels expression and GABA-mediated transmission in primary
            hippocampal cells
  JOURNAL   Toxicology 333, 107-117 (2015)
   PUBMED   25917026
  REMARK    GeneRIF: KChIP1 plays a neuroprotective role against 4-AP acute
            induced cell death in primary hippocampal cells through regulation
            of Kv 4.3 and GABA transmission but this is lost after long term
            exposure.
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Rainnie,D.G., Hazra,R., Dabrowska,J., Guo,J.D., Li,C.C., Dewitt,S.
            and Muly,E.C.
  TITLE     Distribution and functional expression of Kv4 family alpha subunits
            and associated KChIP beta subunits in the bed nucleus of the stria
            terminalis
  JOURNAL   J Comp Neurol 522 (3), 609-625 (2014)
   PUBMED   24037673
  REMARK    GeneRIF: This study demonistrared that the expression and function
            of KCHIP1 channels in neurons of the rat bed nucleus of the stria
            terminalis.
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Dabrowska,J. and Rainnie,D.G.
  TITLE     Expression and distribution of Kv4 potassium channel subunits and
            potassium channel interacting proteins in subpopulations of
            interneurons in the basolateral amygdala
  JOURNAL   Neuroscience 171 (3), 721-733 (2010)
   PUBMED   20849929
  REMARK    GeneRIF: KChIP1 is selectively expressed in BLA interneurons where
            it may function to regulate the activity of A-type potassium
            channels. Hence, KChIP1 might be considered as a specific regulator
            of GABAergic inhibitory circuits in the basolateral amygdala.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   McCue,H.V., Haynes,L.P. and Burgoyne,R.D.
  TITLE     The diversity of calcium sensor proteins in the regulation of
            neuronal function
  JOURNAL   Cold Spring Harb Perspect Biol 2 (8), a004085 (2010)
   PUBMED   20668007
  REMARK    Review article
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Van Schijndel,J.E., Van Zweeden,M., Van Loo,K.M. and Martens,G.J.
  TITLE     Gene expression profiling in brain regions of a rat model
            displaying schizophrenia-related features
  JOURNAL   Behav Brain Res 207 (2), 476-479 (2010)
   PUBMED   19896980
  REMARK    GeneRIF: Aph1b and KCnIP1 are significantly differentially
            expressed in a number of brain tissues of a schizophrenia model;
            KCnIP1 is an attractive novel candidate gene that may play a role
            in the complex phenotype
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Boland,L.M., Jiang,M., Lee,S.Y., Fahrenkrug,S.C., Harnett,M.T. and
            O'Grady,S.M.
  TITLE     Functional properties of a brain-specific NH2-terminally spliced
            modulator of Kv4 channels
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C161-C170 (2003)
   PUBMED   12646414
  REMARK    GeneRIF: The features of KChIP1b modulation of Kv4 channels are
            likely to be conserved in mammals and demonstrate a role for the
            KChIP1 NH2-terminal region in the regulation of closed inactivation
            gating.
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Hilber,K., Sandtner,W., Kudlacek,O., Schreiner,B., Glaaser,I.,
            Schutz,W., Fozzard,H.A., Dudley,S.C. and Todt,H.
  TITLE     Interaction between fast and ultra-slow inactivation in the
            voltage-gated sodium channel. Does the inactivation gate stabilize
            the channel structure?
  JOURNAL   J Biol Chem 277 (40), 37105-37115 (2002)
   PUBMED   12138168
  REMARK    GeneRIF: hypothesis that occlusion of the inner vestibule of the
            Na(+) channel by the fast inactivation gate inhibits ultra-slow
            inactivation (mu1 sodium channel)
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Nakamura,T.Y., Nandi,S., Pountney,D.J., Artman,M., Rudy,B. and
            Coetzee,W.A.
  TITLE     Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4
            subfamily members, Kv4.1 and Kv4.2
  JOURNAL   FEBS Lett 499 (3), 205-209 (2001)
   PUBMED   11423117
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Ohya,S., Morohashi,Y., Muraki,K., Tomita,T., Watanabe,M.,
            Iwatsubo,T. and Imaizumi,Y.
  TITLE     Molecular cloning and expression of the novel splice variants of
            K(+) channel-interacting protein 2
  JOURNAL   Biochem Biophys Res Commun 282 (1), 96-102 (2001)
   PUBMED   11263977
REFERENCE   10 (residues 1 to 236)
  AUTHORS   An,W.F., Bowlby,M.R., Betty,M., Cao,J., Ling,H.P., Mendoza,G.,
            Hinson,J.W., Mattsson,K.I., Strassle,B.W., Trimmer,J.S. and
            Rhodes,K.J.
  TITLE     Modulation of A-type potassium channels by a family of calcium
            sensors
  JOURNAL   Nature 403 (6769), 553-556 (2000)
   PUBMED   10676964
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760393, SAMEA5760433
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..236
                     /product="A-type potassium channel modulatory protein
                     KCNIP1 isoform 1"
                     /note="potassium channel-interacting protein 1; A-type
                     potassium channel modulatory protein 1; Kv
                     channel-interacting protein 1; A-type potassium channel
                     modulatory protein KCNIP1"
                     /calculated_mol_wt=27698
     Region          86..221
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..236
                     /gene="Kcnip1"
                     /gene_synonym="Kchip1"
                     /coded_by="NM_001261387.1:138..848"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65023"
                     /db_xref="RGD:70886"
ORIGIN      
        1 msgcskrcrl gfvkfaqtif klitgtlskd iawwyyqyqr dkieddlemt mvchrpegle
       61 qleaqtnftk relqvlyrgf knecpsgvvn eetfkqiyaq ffphgdasty ahylfnafdt
      121 tqtgsvkfed fvtalsillr gtvheklrwt fnlydinkdg yinkeemmdi vkaiydmmgk
      181 ytypvlkedt prqhvdvffq kmdknkdgiv tldeflescq eddnimrslq lfqnvm
//
LOCUS       NP_001178765             450 aa            linear   ROD 27-APR-2025
DEFINITION  guanine nucleotide-binding protein G(olf) subunit alpha [Rattus
            norvegicus].
ACCESSION   NP_001178765 XP_341627
VERSION     NP_001178765.1
DBSOURCE    REFSEQ: accession NM_001191836.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   El Atiallah,I., Ponterio,G., Meringolo,M., Martella,G.,
            Sciamanna,G., Tassone,A., Montanari,M., Mancini,M., Castagno,A.N.,
            Yu-Taeger,L., Nguyen,H.H.P., Bonsi,P. and Pisani,A.
  TITLE     Loss-of-function of GNAL dystonia gene impairs striatal dopamine
            receptors-mediated adenylyl cyclase/ cyclic AMP signaling pathway
  JOURNAL   Neurobiol Dis 191, 106403 (2024)
   PUBMED   38182074
  REMARK    GeneRIF: Loss-of-function of GNAL dystonia gene impairs striatal
            dopamine receptors-mediated adenylyl cyclase/ cyclic AMP signaling
            pathway.
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Makeyeva,Y., Nicol,C., Ledger,W.L. and Ryugo,D.K.
  TITLE     Immunocytochemical Localization of Olfactory-signaling Molecules in
            Human and Rat Spermatozoa
  JOURNAL   J Histochem Cytochem 68 (7), 491-513 (2020)
   PUBMED   32603211
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yu-Taeger,L., Ott,T., Bonsi,P., Tomczak,C., Wassouf,Z.,
            Martella,G., Sciamanna,G., Imbriani,P., Ponterio,G., Tassone,A.,
            Schulze-Hentrich,J.M., Goodchild,R., Riess,O., Pisani,A.,
            Grundmann-Hauser,K. and Nguyen,H.P.
  TITLE     Impaired dopamine- and adenosine-mediated signaling and plasticity
            in a novel rodent model for DYT25 dystonia
  JOURNAL   Neurobiol Dis 134, 104634 (2020)
   PUBMED   31678405
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Song,H., Fang,S., Gao,J., Wang,J., Cao,Z., Guo,Z., Huang,Q., Qu,Y.,
            Zhou,H. and Yu,J.
  TITLE     Quantitative Proteomic Study Reveals Up-Regulation of cAMP
            Signaling Pathway-Related Proteins in Mild Traumatic Brain Injury
  JOURNAL   J Proteome Res 17 (2), 858-869 (2018)
   PUBMED   29215295
  REMARK    GeneRIF: cAMP signaling pathway-related proteins, Pde10a and Gnal,
            may play important roles in the pathogenesis and recovery of mild
            traumatic brain injury.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Goncalves,I., Hubbard,P.C., Tomas,J., Quintela,T., Tavares,G.,
            Caria,S., Barreiros,D. and Santos,C.R.
  TITLE     'Smelling' the cerebrospinal fluid: olfactory signaling molecules
            are expressed in and mediate chemosensory signaling from the
            choroid plexus
  JOURNAL   FEBS J 283 (9), 1748-1766 (2016)
   PUBMED   26934374
  REMARK    GeneRIF: The major components of the olfactory transduction pathway
            in the rat choroid plexus have been determined, including odorant
            receptors, Galphaolf, adenylate cyclase 3 and CNGA2.
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Belluscio,L., Gold,G.H., Nemes,A. and Axel,R.
  TITLE     Mice deficient in G(olf) are anosmic
  JOURNAL   Neuron 20 (1), 69-81 (1998)
   PUBMED   9459443
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Lelianova,V.G., Davletov,B.A., Sterling,A., Rahman,M.A.,
            Grishin,E.V., Totty,N.F. and Ushkaryov,Y.A.
  TITLE     Alpha-latrotoxin receptor, latrophilin, is a novel member of the
            secretin family of G protein-coupled receptors
  JOURNAL   J Biol Chem 272 (34), 21504-21508 (1997)
   PUBMED   9261169
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Herve,D., Rogard,M. and Levi-Strauss,M.
  TITLE     Molecular analysis of the multiple Golf alpha subunit mRNAs in the
            rat brain
  JOURNAL   Brain Res Mol Brain Res 32 (1), 125-134 (1995)
   PUBMED   7494450
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Menco,B.P., Tekula,F.D., Farbman,A.I. and Danho,W.
  TITLE     Developmental expression of G-proteins and adenylyl cyclase in
            peripheral olfactory systems. Light microscopic and
            freeze-substitution electron microscopic immunocytochemistry
  JOURNAL   J Neurocytol 23 (11), 708-727 (1994)
   PUBMED   7861185
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Jones,D.T. and Reed,R.R.
  TITLE     Golf: an olfactory neuron specific-G protein involved in odorant
            signal transduction
  JOURNAL   Science 244 (4906), 790-795 (1989)
   PUBMED   2499043
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1 and S80376.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341627.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.74464.1,
                                           SRR26643299.63174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..450
                     /product="guanine nucleotide-binding protein G(olf)
                     subunit alpha"
                     /note="guanine nucleotide-binding protein G(olf), alpha
                     subunit; adenylate cyclase-stimulating G alpha protein,
                     olfactory type; Olf-alpha protein (olfactory
                     neuron-specific G protein); guanine nucleotide binding
                     protein, alpha stimulating, olfactory type; guanine
                     nucleotide binding protein, alpha activating activity
                     polypeptide, olfactory type"
                     /calculated_mol_wt=51541
     Region          112..444
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(118,123..125,260,279,282,348..349,351,421..422)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            118..125
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(119..121,149,153,157,160,163..164,184,187,228,257,
                     282,290,294)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            255..263
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            260
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(261,263,265,276,278,282..284,286,289..290,292..295)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(263,288,291..292,295)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            279..282
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            280..296
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            348..351
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(413..424,426..429)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            421..423
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..450
                     /gene="Gnal"
                     /gene_synonym="Golf; Olf; RGD1305940"
                     /coded_by="NM_001191836.2:175..1527"
                     /db_xref="GeneID:24611"
                     /db_xref="RGD:2715"
ORIGIN      
        1 mglcyslrpl lfgssgdapc edsepcaeda qpsaarapap apipapapvg tllrrgdgri
       61 pasarspvel qnrrrqeqlr aeereaakea rkvsrgidrm lreqkrdlqq thrllllgag
      121 esgkstivkq mrilhvngfn peekkqkild irknvkdaiv tivsamstii ppvplanpen
      181 qfrsdyiksi apitdfeysq effdhvkklw ddegvkacfe rsneyqlidc aqyflerids
      241 vslvdytptd qdllrcrvlt sgifetrfqv dkvnfhmfdv ggqrderrkw iqcfndvtai
      301 iyvaacssyn mvirednntn rlresldlfe siwnnrwlrt isiilflnkq dmlaekvlag
      361 kskiedyfpe yanytvpeda tpdagedpkv trakffirdl flristatgd gkhycyphft
      421 cavdtenirr vfndcrdiiq rmhlkqyell
//
LOCUS       NP_001258013              76 aa            linear   ROD 27-APR-2025
DEFINITION  small VCP/p97-interacting protein [Rattus norvegicus].
ACCESSION   NP_001258013 XP_001080929 XP_574455
VERSION     NP_001258013.1
DBSOURCE    REFSEQ: accession NM_001271084.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Jia,D., Wang,Y.Y., Wang,P., Huang,Y., Liang,D.Y., Wang,D.,
            Cheng,C., Zhang,C., Guo,L., Liang,P., Wang,Y., Jia,Y. and Li,C.
  TITLE     SVIP alleviates CCl4-induced liver fibrosis via activating
            autophagy and protecting hepatocytes
  JOURNAL   Cell Death Dis 10 (2), 71 (2019)
   PUBMED   30683843
  REMARK    GeneRIF: SVIP is closely associated with the level of autophagy
            during the development of CCl4-induced hepatic fibrosis. SVIP can
            induce autophagy and suspend hepatic fibrosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Tiwari,S., Siddiqi,S., Zhelyabovska,O. and Siddiqi,S.A.
  TITLE     Silencing of Small Valosin-containing Protein-interacting Protein
            (SVIP) Reduces Very Low Density Lipoprotein (VLDL) Secretion from
            Rat Hepatocytes by Disrupting Its Endoplasmic Reticulum
            (ER)-to-Golgi Trafficking
  JOURNAL   J Biol Chem 291 (24), 12514-12526 (2016)
   PUBMED   27129256
  REMARK    GeneRIF: Data sugggest that small valosin-containing
            protein-interacting protein (SVIP) acts as a regulator of VLDL
            transport vesicle (VTV) formation by interacting with its cargo and
            coat proteins.
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Zhong,Y., Shen,H., Wang,Y., Yang,Y., Yang,P. and Fang,S.
  TITLE     Identification of ERAD components essential for dislocation of the
            null Hong Kong variant of alpha-1-antitrypsin (NHK)
  JOURNAL   Biochem Biophys Res Commun 458 (2), 424-428 (2015)
   PUBMED   25660456
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Wu,J., Peng,D., Voehler,M., Sanders,C.R. and Li,J.
  TITLE     Structure and expression of a novel compact myelin protein - small
            VCP-interacting protein (SVIP)
  JOURNAL   Biochem Biophys Res Commun 440 (1), 173-178 (2013)
   PUBMED   24055875
  REMARK    GeneRIF: SVIP and valosin containing protein were seen to be
            co-localized in neuronal cell bodies.
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Wang,Y., Ballar,P., Zhong,Y., Zhang,X., Liu,C., Zhang,Y.J.,
            Monteiro,M.J., Li,J. and Fang,S.
  TITLE     SVIP induces localization of p97/VCP to the plasma and lysosomal
            membranes and regulates autophagy
  JOURNAL   PLoS One 6 (8), e24478 (2011)
   PUBMED   21909394
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Ballar,P., Zhong,Y., Nagahama,M., Tagaya,M., Shen,Y. and Fang,S.
  TITLE     Identification of SVIP as an endogenous inhibitor of endoplasmic
            reticulum-associated degradation
  JOURNAL   J Biol Chem 282 (47), 33908-33914 (2007)
   PUBMED   17872946
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Wang,Q., Li,L. and Ye,Y.
  TITLE     Regulation of retrotranslocation by p97-associated deubiquitinating
            enzyme ataxin-3
  JOURNAL   J Cell Biol 174 (7), 963-971 (2006)
   PUBMED   17000876
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Nagahama,M., Suzuki,M., Hamada,Y., Hatsuzawa,K., Tani,K.,
            Yamamoto,A. and Tagaya,M.
  TITLE     SVIP is a novel VCP/p97-interacting protein whose expression causes
            cell vacuolation
  JOURNAL   Mol Biol Cell 14 (1), 262-273 (2003)
   PUBMED   12529442
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_001080929.1, XP_574455.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB607646.1, SRR26360172.1831049.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN16676810
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..76
                     /product="small VCP/p97-interacting protein"
                     /calculated_mol_wt=8117
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0A9.1)"
     Region          1..70
                     /region_name="SVIP"
                     /note="Small VCP/p97-interacting protein; pfam15811"
                     /db_xref="CDD:464888"
     Region          21..33
                     /region_name="VCP/p97-interacting motif (VIM).
                     /evidence=ECO:0000250|UniProtKB:Q8NHG7"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C0A9.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NHG7; propagated from
                     UniProtKB/Swiss-Prot (P0C0A9.1)"
     CDS             1..76
                     /gene="Svip"
                     /gene_synonym="RGD1565432"
                     /coded_by="NM_001271084.1:122..352"
                     /db_xref="GeneID:499157"
                     /db_xref="RGD:1565432"
ORIGIN      
        1 mglcfpcpae sappspspee kraklaeaae rrqkeaasrg ildiqsveak kkkkeqlekq
       61 metsgppagg lrwtvs
//
LOCUS       NP_036653                 79 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-G [Rattus norvegicus].
ACCESSION   NP_036653
VERSION     NP_036653.1
DBSOURCE    REFSEQ: accession NM_012521.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Wang,W., Knosp,E., Tai,G., Zhao,Y., Liang,Q. and Guo,Y.
  TITLE     Differential effects of estrogen and estrogen receptor antagonist,
            ICI 182 780, on the expression of calbindin-D9k in rat pituitary
            prolactinoma GH cells
  JOURNAL   Int J Clin Exp Pathol 7 (12), 8498-8505 (2014)
   PUBMED   25674214
  REMARK    GeneRIF: Estrogen-induced CaBP-9k directly combines with ERalpha,
            suggesting that CaBP-9k is involved in the biological effects
            mediated by an ER pathway in the GH3 rat pituitary prolactinoma
            cell line
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Ahn,H.J., An,B.S., Jung,E.M., Yang,H., Choi,K.C. and Jeung,E.B.
  TITLE     Parabens inhibit the early phase of folliculogenesis and
            steroidogenesis in the ovaries of neonatal rats
  JOURNAL   Mol Reprod Dev 79 (9), 626-636 (2012)
   PUBMED   22777679
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Rios,M., Parada-Bustamante,A., Velasquez,L.A., Croxatto,H.B. and
            Orihuela,P.A.
  TITLE     Participation of the oviductal s100 calcium binding protein G in
            the genomic effect of estradiol that accelerates oviductal embryo
            transport in mated rats
  JOURNAL   Reprod Biol Endocrinol 9, 69 (2011)
   PUBMED   21605449
  REMARK    GeneRIF: S100 g is a functional component of E2 genomic effect that
            accelerates egg transport.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 79)
  AUTHORS   Schwaller,B.
  TITLE     Cytosolic Ca2+ buffers
  JOURNAL   Cold Spring Harb Perspect Biol 2 (11), a004051 (2010)
   PUBMED   20943758
  REMARK    Review article
REFERENCE   6  (residues 1 to 79)
  AUTHORS   Krisinger,J., Darwish,H., Maeda,N. and DeLuca,H.F.
  TITLE     Structure and nucleotide sequence of the rat intestinal vitamin
            D-dependent calcium binding protein gene
  JOURNAL   Proc Natl Acad Sci U S A 85 (23), 8988-8992 (1988)
   PUBMED   3194402
REFERENCE   7  (residues 1 to 79)
  AUTHORS   Perret,C., Lomri,N., Gouhier,N., Auffray,C. and Thomasset,M.
  TITLE     The rat vitamin-D-dependent calcium-binding protein (9-kDa CaBP)
            gene. Complete nucleotide sequence and structural organization
  JOURNAL   Eur J Biochem 172 (1), 43-51 (1988)
   PUBMED   3345761
REFERENCE   8  (residues 1 to 79)
  AUTHORS   Darwish,H.M., Krisinger,J., Strom,M. and DeLuca,H.F.
  TITLE     Molecular cloning of the cDNA and chromosomal gene for vitamin
            D-dependent calcium-binding protein of rat intestine
  JOURNAL   Proc Natl Acad Sci U S A 84 (17), 6108-6111 (1987)
   PUBMED   3476932
REFERENCE   9  (residues 1 to 79)
  AUTHORS   MacManus,J.P., Watson,D.C. and Yaguchi,M.
  TITLE     The purification and complete amino acid sequence of the 9000-Mr
            Ca2+-binding protein from rat placenta. Identity with the vitamin
            D-dependent intestinal Ca2+-binding protein
  JOURNAL   Biochem J 235 (2), 585-595 (1986)
   PUBMED   3741407
REFERENCE   10 (residues 1 to 79)
  AUTHORS   Desplan,C., Heidmann,O., Lillie,J.W., Auffray,C. and Thomasset,M.
  TITLE     Sequence of rat intestinal vitamin D-dependent calcium-binding
            protein derived from a cDNA clone. Evolutionary implications
  JOURNAL   J Biol Chem 258 (22), 13502-13505 (1983)
   PUBMED   6315698
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J02954.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02954.1, BC059153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132298, SAMN06680422
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq14"
     Protein         1..79
                     /product="protein S100-G"
                     /note="calcium-binding protein, intestinal, vitamin
                     D-dependent (9-kDa CaBP); 9 kDa CaBP; cholecalcin; vitamin
                     D-dependent calcium-binding protein, intestinal;
                     calbindin-D9K; calbindin 3, (vitamin D-dependent calcium
                     binding protein)"
                     /calculated_mol_wt=8907
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:3741407; propagated from
                     UniProtKB/Swiss-Prot (P02634.3)"
     Region          12..79
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(18,23,26,31..32,58,60,62,64,66,69)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02634.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02634.3)"
     CDS             1..79
                     /gene="S100g"
                     /gene_synonym="Cabp; Calb3; Cbpi; Rncalbd9"
                     /coded_by="NM_012521.2:62..301"
                     /db_xref="GeneID:24249"
                     /db_xref="RGD:2253"
ORIGIN      
        1 msakkspeem ksifqkyaak egdpnqlske elklliqsef psllkasstl dnlfkeldkn
       61 gdgevsyeef evffkklsq
//
LOCUS       NP_058836                446 aa            linear   ROD 27-APR-2025
DEFINITION  D(3) dopamine receptor [Rattus norvegicus].
ACCESSION   NP_058836
VERSION     NP_058836.1
DBSOURCE    REFSEQ: accession NM_017140.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Shen,H., Ma,Z., Hans,E., Duan,Y., Bi,G.H., Chae,Y.C., Bonifazi,A.,
            Battiti,F.O., Newman,A.H., Xi,Z.X. and Yang,Y.
  TITLE     Involvement of dopamine D3 receptor in impulsive choice
            decision-making in male rats
  JOURNAL   Neuropharmacology 257, 110051 (2024)
   PUBMED   38917939
  REMARK    GeneRIF: Involvement of dopamine D3 receptor in impulsive choice
            decision-making in male rats.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Chen,B., Xu,J., Chen,S., Mou,T., Wang,Y., Wang,H., Zhang,Z.,
            Ren,F., Wang,Z., Jin,K. and Lu,J.
  TITLE     Dysregulation of striatal dopamine D2/D3 receptor-mediated by
            hypocretin induces depressive behaviors in rats
  JOURNAL   J Affect Disord 325, 256-263 (2023)
   PUBMED   36638964
  REMARK    GeneRIF: Dysregulation of striatal dopamine D2/D3 receptor-mediated
            by hypocretin induces depressive behaviors in rats.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Budzinski,J., Maschauer,S., Kobayashi,H., Couvineau,P., Vogt,H.,
            Gmeiner,P., Roggenhofer,A., Prante,O., Bouvier,M. and Weikert,D.
  TITLE     Bivalent ligands promote endosomal trafficking of the dopamine D3
            receptor-neurotensin receptor 1 heterodimer
  JOURNAL   Commun Biol 4 (1), 1062 (2021)
   PUBMED   34508168
  REMARK    GeneRIF: Bivalent ligands promote endosomal trafficking of the
            dopamine D3 receptor-neurotensin receptor 1 heterodimer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Lanza,K., Centner,A., Coyle,M., Del Priore,I., Manfredsson,F.P. and
            Bishop,C.
  TITLE     Genetic suppression of the dopamine D3 receptor in striatal D1
            cells reduces the development of L-DOPA-induced dyskinesia
  JOURNAL   Exp Neurol 336, 113534 (2021)
   PUBMED   33249031
  REMARK    GeneRIF: Genetic suppression of the dopamine D3 receptor in
            striatal D1 cells reduces the development of L-DOPA-induced
            dyskinesia.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Bahi,A. and Dreyer,J.L.
  TITLE     Lentiviral-mediated up-regulation of let-7d microRNA decreases
            alcohol intake through down-regulating the dopamine D3 receptor
  JOURNAL   Eur Neuropsychopharmacol 37, 70-81 (2020)
   PUBMED   32646740
  REMARK    GeneRIF: Lentiviral-mediated up-regulation of let-7d microRNA
            decreases alcohol intake through down-regulating the dopamine D3
            receptor.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Crocq,M.A., Mant,R., Asherson,P., Williams,J., Hode,Y.,
            Mayerova,A., Collier,D., Lannfelt,L., Sokoloff,P., Schwartz,J.C. et
            al.
  TITLE     Association between schizophrenia and homozygosity at the dopamine
            D3 receptor gene
  JOURNAL   J Med Genet 29 (12), 858-860 (1992)
   PUBMED   1362221
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Livingstone,C.D., Strange,P.G. and Naylor,L.H.
  TITLE     Molecular modelling of D2-like dopamine receptors
  JOURNAL   Biochem J 287 (Pt 1) (Pt 1), 277-282 (1992)
   PUBMED   1358063
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Snyder,L.A., Roberts,J.L. and Sealfon,S.C.
  TITLE     Alternative transcripts of the rat and human dopamine D3 receptor
  JOURNAL   Biochem Biophys Res Commun 180 (2), 1031-1035 (1991)
   PUBMED   1953708
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Giros,B., Martres,M.P., Pilon,C., Sokoloff,P. and Schwartz,J.C.
  TITLE     Shorter variants of the D3 dopamine receptor produced through
            various patterns of alternative splicing
  JOURNAL   Biochem Biophys Res Commun 176 (3), 1584-1592 (1991)
   PUBMED   2039532
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Sokoloff,P., Giros,B., Martres,M.P., Bouthenet,M.L. and
            Schwartz,J.C.
  TITLE     Molecular cloning and characterization of a novel dopamine receptor
            (D3) as a target for neuroleptics
  JOURNAL   Nature 347 (6289), 146-151 (1990)
   PUBMED   1975644
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X53944.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..446
                     /product="D(3) dopamine receptor"
                     /note="dopaminergic receptor D3"
                     /calculated_mol_wt=49385
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19020.1)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19020.1)"
     Region          30..440
                     /region_name="7tmA_D3_dopamine_R"
                     /note="D3 subtype of the D2-like family of dopamine
                     receptors, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15310"
                     /db_xref="CDD:320436"
     Region          31..57
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320436"
     Site            33..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Region          64..87
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320436"
     Site            66..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19020.1)"
     Region          103..133
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320436"
     Site            105..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Site            order(106,110..111,114,189,192..193,391..392,395,411,415,
                     419)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:320436"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Region          150..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320436"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19020.1)"
     Region          185..210
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320436"
     Site            188..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Region          368..398
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320436"
     Site            376..397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     Region          408..433
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320436"
     Site            413..432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19020.1)"
     CDS             1..446
                     /gene="Drd3"
                     /coded_by="NM_017140.2:82..1422"
                     /db_xref="GeneID:29238"
                     /db_xref="RGD:2521"
ORIGIN      
        1 maplsqisth lnstcgaens tgvnrarpha yyalsycali laiifgnglv caavlreral
       61 qtttnylvvs lavadllvat lvmpwvvyle vtggvwnfsr iccdvfvtld vmmctasiln
      121 lcaisidryt avvmpvhyqh gtgqsscrrv almitavwvl afavscpllf gfnttgdpsi
      181 csisnpdfvi yssvvsfyvp fgvtvlvyar iyivlrqrqr kriltrqnsq cisirpgfpq
      241 qssclrlhpi rqfsirarfl sdatgqmehi edkqypqkcq dpllshlqpp spgqthgglk
      301 ryysicqdta lrhpslegga gmspvertrn slsptmapkl slevrklsng rlstslrlgp
      361 lqprgvplre kkatqmvviv lgafivcwlp fflthvlnth cqachvspel yrattwlgyv
      421 nsalnpviyt tfnvefrkaf lkilsc
//
LOCUS       NP_001257497             449 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3F [Rattus norvegicus].
ACCESSION   NP_001257497
VERSION     NP_001257497.1
DBSOURCE    REFSEQ: accession NM_001270568.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1 and BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (6) is alternatively spliced at
            the 3' end compared to variant 1, which results in a frame-shift,
            and a longer isoform (H3F) containing 6 transmembrane domains and a
            distinct C-terminus compared to isoform H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..449
                     /product="histamine H3 receptor isoform H3F"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=49718
     Region          48..347
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          70..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320423"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320423"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320423"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320423"
     Region          309..331
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320423"
     CDS             1..449
                     /gene="Hrh3"
                     /coded_by="NM_001270568.1:338..1687"
                     /note="isoform H3F is encoded by transcript variant 6"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhrgskpsa ssaslekrmk mvsqsitqrf
      301 rlsrdkkvak slaiivsifg lcwapytllm iiraachgrc ipdycverlg kleaslllpl
      361 wmfsgrwrrr khvceldvpw mfnqerqncr gargwigrcg lprpppsvlq lpaeprqlll
      421 papppglgrw pcpacpvcti riwgwvvmg
//
LOCUS       NP_001288631             448 aa            linear   ROD 27-APR-2025
DEFINITION  antizyme inhibitor 1 [Rattus norvegicus].
ACCESSION   NP_001288631 XP_006241629
VERSION     NP_001288631.1
DBSOURCE    REFSEQ: accession NM_001301702.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Okugawa,Y., Toiyama,Y., Shigeyasu,K., Yamamoto,A., Shigemori,T.,
            Yin,C., Ichikawa,T., Yasuda,H., Fujikawa,H., Yoshiyama,S., Hiro,J.,
            Ohi,M., Araki,T., Kusunoki,M. and Goel,A.
  TITLE     Enhanced AZIN1 RNA editing and overexpression of its regulatory
            enzyme ADAR1 are important prognostic biomarkers in gastric cancer
  JOURNAL   J Transl Med 16 (1), 366 (2018)
   PUBMED   30563560
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Shigeyasu,K., Okugawa,Y., Toden,S., Miyoshi,J., Toiyama,Y.,
            Nagasaka,T., Takahashi,N., Kusunoki,M., Takayama,T., Yamada,Y.,
            Fujiwara,T., Chen,L. and Goel,A.
  TITLE     AZIN1 RNA editing confers cancer stemness and enhances oncogenic
            potential in colorectal cancer
  JOURNAL   JCI Insight 3 (12), 99976 (2018)
   PUBMED   29925690
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Fernandes,J.R.D., Jain,S. and Banerjee,A.
  TITLE     Expression of ODC1, SPD, SPM and AZIN1 in the hypothalamus, ovary
            and uterus during rat estrous cycle
  JOURNAL   Gen Comp Endocrinol 246, 9-22 (2017)
   PUBMED   28315656
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Zhu,D., Zhang,L., Cheng,L., Ren,L., Tang,J. and Sun,D.
  TITLE     Pancreatic Kininogenase Ameliorates Renal Fibrosis in
            Streptozotocin Induced-Diabetic Nephropathy Rat
  JOURNAL   Kidney Blood Press Res 41 (1), 9-17 (2016)
   PUBMED   26751697
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Greenwood,M.P., Greenwood,M., Paton,J.F. and Murphy,D.
  TITLE     Control of Polyamine Biosynthesis by Antizyme Inhibitor 1 Is
            Important for Transcriptional Regulation of Arginine Vasopressin in
            the Male Rat Hypothalamus
  JOURNAL   Endocrinology 156 (8), 2905-2917 (2015)
   PUBMED   25961839
  REMARK    GeneRIF: Identification of AZIN1, and hence by inference,
            polyamines as novel regulators of the expression of the Arginine
            vasopressin gene.
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Mangold,U., Hayakawa,H., Coughlin,M., Munger,K. and Zetter,B.R.
  TITLE     Antizyme, a mediator of ubiquitin-independent proteasomal
            degradation and its inhibitor localize to centrosomes and modulate
            centriole amplification
  JOURNAL   Oncogene 27 (5), 604-613 (2008)
   PUBMED   17667942
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Lopez-Contreras,A.J., Lopez-Garcia,C., Jimenez-Cervantes,C.,
            Cremades,A. and Penafiel,R.
  TITLE     Mouse ornithine decarboxylase-like gene encodes an antizyme
            inhibitor devoid of ornithine and arginine decarboxylating activity
  JOURNAL   J Biol Chem 281 (41), 30896-30906 (2006)
   PUBMED   16916800
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Kim,S.W., Mangold,U., Waghorne,C., Mobascher,A., Shantz,L.,
            Banyard,J. and Zetter,B.R.
  TITLE     Regulation of cell proliferation by the antizyme inhibitor:
            evidence for an antizyme-independent mechanism
  JOURNAL   J Cell Sci 119 (Pt 12), 2583-2591 (2006)
   PUBMED   16735445
  REMARK    GeneRIF: Wild-type antizyme inhibitor and the AZI(DeltaY) mutant
            are capable of direct interaction with cyclin D1 suggesting a
            potential mechanism for the antizyme-independent effects, and a
            novel function for antizyme inhibitor in cellular growth control.
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Murakami,Y., Ichiba,T., Matsufuji,S. and Hayashi,S.
  TITLE     Cloning of antizyme inhibitor, a highly homologous protein to
            ornithine decarboxylase
  JOURNAL   J Biol Chem 271 (7), 3340-3342 (1996)
   PUBMED   8631929
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Kitani,T. and Fujisawa,H.
  TITLE     Purification and characterization of antizyme inhibitor of
            ornithine decarboxylase from rat liver
  JOURNAL   Biochim Biophys Acta 991 (1), 44-49 (1989)
   PUBMED   2713421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            On Sep 5, 2014 this sequence version replaced XP_006241629.1.
            
            Summary: The protein encoded by this gene belongs to the antizyme
            inhibitor family, which plays a role in cell growth and
            proliferation by maintaining polyamine homeostasis within the cell.
            Antizyme inhibitors are homologs of ornithine decarboxylase (ODC,
            the key enzyme in polyamine biosynthesis) that have lost the
            ability to decarboxylase ornithine; however, retain the ability to
            bind to antizymes. Antizymes negatively regulate intracellular
            polyamine levels by binding to ODC and targeting it for
            degradation, as well as by inhibiting polyamine uptake. Antizyme
            inhibitors function as positive regulators of polyamine levels by
            sequestering antizymes and neutralizing their effect. This gene
            encodes antizyme inhibitor 1, the first member of this gene family
            that is ubiquitously expressed, and is localized in the nucleus and
            cytoplasm. Overexpression of antizyme inhibitor 1 gene has been
            associated with increased proliferation, cellular transformation
            and tumorigenesis. Gene knockout studies showed that homozygous
            mutant mice lacking functional antizyme inhibitor 1 gene died at
            birth with abnormal liver morphology. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (2) lacks an internal 5'
            non-coding exon, thus has a shorter 5' UTR compared to variant 1.
            Variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.40949.1, D50734.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..448
                     /product="antizyme inhibitor 1"
                     /note="ornithine decarboxylase antizyme inhibitor; AZI"
                     /calculated_mol_wt=49188
     Region          26..419
                     /region_name="PLPDE_III_ODC_like_AZI"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase-like Antizyme Inhibitor;
                     cd06831"
                     /db_xref="CDD:143504"
     Site            69
                     /site_type="other"
                     /note="Not modified.
                     /evidence=ECO:0000250|UniProtKB:O35484; propagated from
                     UniProtKB/Swiss-Prot (Q63764.1)"
     Site            order(91..93,119,141,288,329,358,360,391,394,397)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143504"
     CDS             1..448
                     /gene="Azin1"
                     /gene_synonym="Oazi; Oazin"
                     /coded_by="NM_001301702.1:625..1971"
                     /db_xref="GeneID:58961"
                     /db_xref="RGD:61934"
ORIGIN      
        1 mkgfiddany svglldegtn lgnvidnyvy ehtltgknaf fvgdlgkivk khsqwqnvva
       61 qikpfymvkc nstpavleil aalgtgfacs sknemalvqe lgvspeniiy tspckqasqi
      121 kyaakvgvni mtcdnevelk kiarnhpnak vllhiatedn iggedgnmkf gttlkncrhl
      181 lecakeldvq iigvkfhiss ackeyqvyvh alsdarcvfd magefgftmn mldigggftg
      241 teiqleevnh visplldiyf pegsgiqiis epgsyyvssa ftlavniiak kvvendklss
      301 gvekngsdep afvyymndgv ygsfasklse dlntvpevhk kykedeplft sslwgpscde
      361 ldqivescll pelsvgdwli fdnmgadslh gpsafsdtqr paiyfmmsls dwyemqdagi
      421 tsdammknff fapsciqlsq ednfstea
//
LOCUS       NP_001258007              75 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 7 precursor [Rattus norvegicus].
ACCESSION   NP_001258007
VERSION     NP_001258007.1
DBSOURCE    REFSEQ: accession NM_001271078.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 75)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 75)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 75)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 75)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 75)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 75)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 75)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1, U60564.1 and U67130.1.
            
            Transcript Variant: This variant (7) uses an alternate in-frame
            splice site at the 5' end of an exon and differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (7)
            lacks an alternate internal segment and has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: U07054.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN06621351,
                                    SAMN09345331 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..75
                     /product="amelogenin, X isoform isoform 7 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=6739
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          <18..75
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     Region          21..>47
                     /region_name="Amelogenin"
                     /note="pfam02948"
                     /db_xref="CDD:460761"
     CDS             1..75
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271078.1:67..294"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqpp lspilpelpl
       61 eawpatdktk reevd
//
LOCUS       NP_001257516             654 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier organic anion transporter family member 1B2 isoform
            3 [Rattus norvegicus].
ACCESSION   NP_001257516
VERSION     NP_001257516.1
DBSOURCE    REFSEQ: accession NM_001270587.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Chen,S., Li,K., Jiang,J., Wang,X., Chai,Y., Zhang,C., Deng,Q.,
            Shuai,L., Feng,K., Ma,K. and Zhang,L.
  TITLE     Low expression of organic anion-transporting polypeptide 1B3
            predicts a poor prognosis in hepatocellular carcinoma
  JOURNAL   World J Surg Oncol 18 (1), 127 (2020)
   PUBMED   32534581
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Ma,X., Shang,X., Qin,X., Lu,J., Liu,M. and Wang,X.
  TITLE     Characterization of organic anion transporting polypeptide 1b2
            knockout rats generated by CRISPR/Cas9: a novel model for drug
            transport and hyperbilirubinemia disease
  JOURNAL   Acta Pharm Sin B 10 (5), 850-860 (2020)
   PUBMED   32528832
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Alam,K., Farasyn,T., Ding,K. and Yue,W.
  TITLE     Characterization of Liver- and Cancer-type-Organic Anion
            Transporting Polypeptide (OATP) 1B3 Messenger RNA Expression in
            Normal and Cancerous Human Tissues
  JOURNAL   Drug Metab Lett 12 (1), 24-32 (2018)
   PUBMED   29577869
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Verboom,M.C., Kloth,J.S.L., Swen,J.J., van der Straaten,T.,
            Bovee,J.V.M.G., Sleijfer,S., Reyners,A.K.L., Mathijssen,R.H.J.,
            Guchelaar,H.J., Steeghs,N. and Gelderblom,H.
  TITLE     Genetic polymorphisms in angiogenesis-related genes are associated
            with worse progression-free survival of patients with advanced
            gastrointestinal stromal tumours treated with imatinib
  JOURNAL   Eur J Cancer 86, 226-232 (2017)
   PUBMED   29054076
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Sun,B., Chen,Y., Xiang,T., Zhang,L., Chen,Z., Zhang,S., Zhou,H. and
            Chen,S.
  TITLE     The Chinese Herb Jianpijiedu Contributes to the Regulation of
            OATP1B2 and ABCC2 in a Rat Model of Orthotopic Transplantation
            Liver Cancer Pretreated with Food Restriction and Diarrhea
  JOURNAL   Biomed Res Int 2015, 752850 (2015)
   PUBMED   26665149
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Cattori,V., van Montfoort,J.E., Stieger,B., Landmann,L.,
            Meijer,D.K., Winterhalter,K.H., Meier,P.J. and Hagenbuch,B.
  TITLE     Localization of organic anion transporting polypeptide 4 (Oatp4) in
            rat liver and comparison of its substrate specificity with Oatp1,
            Oatp2 and Oatp3
  JOURNAL   Pflugers Arch 443 (2), 188-195 (2001)
   PUBMED   11713643
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Ismair,M.G., Stieger,B., Cattori,V., Hagenbuch,B., Fried,M.,
            Meier,P.J. and Kullak-Ublick,G.A.
  TITLE     Hepatic uptake of cholecystokinin octapeptide by organic
            anion-transporting polypeptides OATP4 and OATP8 of rat and human
            liver
  JOURNAL   Gastroenterology 121 (5), 1185-1190 (2001)
   PUBMED   11677211
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Choudhuri,S., Ogura,K. and Klaassen,C.D.
  TITLE     Cloning of the full-length coding sequence of rat liver-specific
            organic anion transporter-1 (rlst-1) and a splice variant and
            partial characterization of the rat lst-1 gene
  JOURNAL   Biochem Biophys Res Commun 274 (1), 79-86 (2000)
   PUBMED   10903899
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Cattori,V., Hagenbuch,B., Hagenbuch,N., Stieger,B., Ha,R.,
            Winterhalter,K.E. and Meier,P.J.
  TITLE     Identification of organic anion transporting polypeptide 4 (Oatp4)
            as a major full-length isoform of the liver-specific transporter-1
            (rlst-1) in rat liver
  JOURNAL   FEBS Lett 474 (2-3), 242-245 (2000)
   PUBMED   10838093
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Kakyo,M., Unno,M., Tokui,T., Nakagomi,R., Nishio,T., Iwasashi,H.,
            Nakai,D., Seki,M., Suzuki,M., Naitoh,T., Matsuno,S., Yawo,H. and
            Abe,T.
  TITLE     Molecular characterization and functional regulation of a novel rat
            liver-specific organic anion transporter rlst-1
  JOURNAL   Gastroenterology 117 (4), 770-775 (1999)
   PUBMED   10500057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF217450.2 and JAXUCZ010000004.1.
            
            Transcript Variant: This variant (3, also known as rlst-1c) lacks
            an alternate in-frame exon compared to variant 1. The resulting
            isoform (3) has the same N- and C-termini but is shorter compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF217450.2, SRR26643286.15360.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..654
                     /product="solute carrier organic anion transporter family
                     member 1B2 isoform 3"
                     /note="solute carrier family 21 member 10;
                     sodium-independent organic anion-transporting polypeptide
                     4; solute carrier organic anion transporter family, member
                     1b3; solute carrier family 21 (organic anion transporter)
                     member 10; solute carrier family (organic anion
                     transporter) member 10; organic anion transporting
                     polypeptide 4; liver-specific transporter-1;
                     liver-specific organic anion transporter 1"
                     /calculated_mol_wt=73113
     Region          29..582
                     /region_name="OATP"
                     /note="Organic Anion Transporter Polypeptide (OATP)
                     family; pfam03137"
                     /db_xref="CDD:460821"
     CDS             1..654
                     /gene="Slco1b2"
                     /gene_synonym="OATP-4; Oatp4; rlst-1; Slc21a10; Slco1b3"
                     /coded_by="NM_001270587.1:115..2079"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:58978"
                     /db_xref="RGD:69300"
ORIGIN      
        1 mdhtqqsrka aeaqpsrskq trfcdgfklf laalsfsyic kalggvvmks sitqierrfd
       61 ipssisglid ggfeignllv ivfvsyfgsk lhrpkligig cfimgigsil talphffmgy
      121 ykyakendig slgnstltcf inqmtsptgp speivekgce kglkshmwiy vlmgnmlrgi
      181 getpivplgi sylddfakeg htsmhldsvr itpndarwvg awwlsfivng llcitssipf
      241 fflpkipkrs qeerknsvsl hapktdeekk hmtnltkqee qdpsnmtgfl rslrsiltne
      301 iyvifliltl lqvsgfigsf tylfkfieqq fgrtasqanf llgiitiptm atamflggyi
      361 vkkfkltsvg iakfvfftss vayafqflyf pllcenkpfa gltltydgmn pvdshidvpl
      421 sycnsdcscd knqwepicge ngvtyispcl agcksfrgdk kpnntefydc scisnsgnns
      481 ahlgecpryk cktnyyfyii lqvtvsffta mgspslilil mksvqpelks lamgfhslii
      541 ralggilapi yygafidrtc ikwsvtscgk rgacrlynsr lfgfsylgln lalktpplfl
      601 yvvliyftkr kykrndnktl engrqftdeg npdsvnkngy ycvpydeqsn etpl
//
LOCUS       NP_775155                333 aa            linear   ROD 27-APR-2025
DEFINITION  testin-2 precursor [Rattus norvegicus].
ACCESSION   NP_775155
VERSION     NP_775155.1
DBSOURCE    REFSEQ: accession NM_173132.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Su,L., Wang,Z., Xie,S., Hu,D., Cheng,Y.C., Mruk,D.D. and Guan,Y.
  TITLE     Testin regulates the blood-testis barrier via disturbing
            occludin/ZO-1 association and actin organization
  JOURNAL   J Cell Physiol 235 (9), 6127-6138 (2020)
   PUBMED   31975378
  REMARK    GeneRIF: Testin regulates the blood-testis barrier via disturbing
            occludin/ZO-1 association and actin organization.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Grima,J., Zhu,L.J., Zong,S.D., Catterall,J.F., Bardin,C.W. and
            Cheng,C.Y.
  TITLE     Rat testin is a newly identified component of the junctional
            complexes in various tissues whose mRNA is predominantly expressed
            in the testis and ovary
  JOURNAL   Biol Reprod 52 (2), 340-355 (1995)
   PUBMED   7711203
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Cheng,C.Y., Morris,I. and Bardin,C.W.
  TITLE     Testins are structurally related to the mouse cysteine proteinase
            precursor but devoid of any protease/anti-protease activity
  JOURNAL   Biochem Biophys Res Commun 191 (1), 224-231 (1993)
   PUBMED   8447824
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Cheng,C.Y., Grima,J., Stahler,M.S., Lockshin,R.A. and Bardin,C.W.
  TITLE     Testins are structurally related Sertoli cell proteins whose
            secretion is tightly coupled to the presence of germ cells
  JOURNAL   J Biol Chem 264 (35), 21386-21393 (1989)
   PUBMED   2592382
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U16858.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U16858.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..333
                     /product="testin-2 precursor"
                     /note="testin-2; CMB-23"
                     /calculated_mol_wt=36200
     sig_peptide     1..17
                     /note="/evidence=ECO:0000269|PubMed:2592382; propagated
                     from UniProtKB/Swiss-Prot (P15242.2)"
                     /calculated_mol_wt=1851
     mat_peptide     18..333
                     /product="Testin-2. /id=PRO_0000026291"
                     /note="propagated from UniProtKB/Swiss-Prot (P15242.2)"
                     /calculated_mol_wt=36200
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Region          114..332
                     /region_name="Peptidase_C1"
                     /note="Papain family cysteine protease; pfam00112"
                     /db_xref="CDD:425470"
     Site            order(132,138,276,300)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            138
                     /site_type="other"
                     /note="Ancestral active site; propagated from
                     UniProtKB/Swiss-Prot (P15242.2)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15242.2)"
     Site            order(182..183,248,274,277,327)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     CDS             1..333
                     /gene="Testin"
                     /coded_by="NM_173132.2:93..1094"
                     /db_xref="GeneID:286916"
                     /db_xref="RGD:708447"
ORIGIN      
        1 miavlflail clevdstapt pdpsldvewn ewrtkhgkty nmneerlkra vweknfkmie
       61 lhnweylegr hdftmamnaf gdltniefvk mmtgfqrqki kkthifqdhq flyvpkrvdw
      121 rqlgyvtpvk nqghcasswa fsatgslegq mfrkterlip lseqnlldcm gsnvthgcsg
      181 gfmqyafqyv kdngglatee sypyrgqgre cryhaensaa nvrdfvqipg seealmkava
      241 kvgpisvavd ashgsfqfyg sgiyyepqck rvhlnhavlv vgygfegees dgnsfwlvkn
      301 swgeewgmkg ymklakdwsn hcgiatysty piv
//
LOCUS       NP_037281                853 aa            linear   ROD 27-APR-2025
DEFINITION  aryl hydrocarbon receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_037281 XP_346770
VERSION     NP_037281.3
DBSOURCE    REFSEQ: accession NM_013149.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Andersen,M.E., Barutcu,A.R., Black,M.B. and Harrill,J.A.
  TITLE     Transcriptomic analysis of AHR wildtype and Knock-out rat livers
            supports TCDD's role in AHR/ARNT-mediated circadian disruption and
            hepatotoxicity
  JOURNAL   Toxicol Appl Pharmacol 487, 116956 (2024)
   PUBMED   38735589
  REMARK    GeneRIF: Transcriptomic analysis of AHR wildtype and Knock-out rat
            livers supports TCDD's role in AHR/ARNT-mediated circadian
            disruption and hepatotoxicity.
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Chausse,A.M., Roche,S.M., Moroldo,M., Hennequet-Antier,C.,
            Holbert,S., Kempf,F., Barilleau,E., Trotereau,J. and Velge,P.
  TITLE     Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis
  JOURNAL   Virulence 14 (1), 2158663 (2023)
   PUBMED   36600181
  REMARK    GeneRIF: Epithelial cell invasion by salmonella typhimurium induces
            modulation of genes controlled by aryl hydrocarbon receptor
            signaling and involved in extracellular matrix biogenesis.
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Xu,J., Sun,X., Qin,F., Wang,X., Chen,Q. and Yan,R.
  TITLE     Protective effects of salvianolic acid B on intestinal
            ischemia/reperfusion injury in rats by regulating the
            AhR/IL-22/STAT6 axis
  JOURNAL   J Recept Signal Transduct Res 43 (3), 73-82 (2023)
   PUBMED   37387514
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Kouno,T., Zeng,S., Wang,Y., Duan,Y., Lang,S., Gao,B., Hartmann,P.,
            Cabre,N., Llorente,C., Galbert,C., Emond,P., Sokol,H., James,M.,
            Chao,C.C., Gao,J.R., Perreault,M., Hava,D.L. and Schnabl,B.
  TITLE     Engineered bacteria producing aryl-hydrocarbon receptor agonists
            protect against ethanol-induced liver disease in mice
  JOURNAL   Alcohol Clin Exp Res (Hoboken) 47 (5), 856-867 (2023)
   PUBMED   36871955
REFERENCE   5  (residues 1 to 853)
  AUTHORS   Nori,P., Haghshenas,R., Aftabi,Y. and Akbari,H.
  TITLE     Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery
  JOURNAL   Sci Rep 13 (1), 3721 (2023)
   PUBMED   36879035
  REMARK    GeneRIF: Comparison of moderate-intensity continuous training and
            high-intensity interval training effects on the Ido1-KYN-Ahr axis
            in the heart tissue of rats with occlusion of the left anterior
            descending artery.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Fernandez-Salguero,P., Pineau,T., Hilbert,D.M., McPhail,T.,
            Lee,S.S., Kimura,S., Nebert,D.W., Rudikoff,S., Ward,J.M. and
            Gonzalez,F.J.
  TITLE     Immune system impairment and hepatic fibrosis in mice lacking the
            dioxin-binding Ah receptor
  JOURNAL   Science 268 (5211), 722-726 (1995)
   PUBMED   7732381
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Elferink,C.J. and Whitlock,J.P. Jr.
  TITLE     Dioxin-dependent, DNA sequence-specific binding of a multiprotein
            complex containing the Ah receptor
  JOURNAL   Receptor 4 (3), 157-173 (1994)
   PUBMED   7812217
REFERENCE   8  (residues 1 to 853)
  AUTHORS   Puga,A., Nebert,D.W. and Carrier,F.
  TITLE     Dioxin induces expression of c-fos and c-jun proto-oncogenes and a
            large increase in transcription factor AP-1
  JOURNAL   DNA Cell Biol 11 (4), 269-281 (1992)
   PUBMED   1605850
REFERENCE   9  (residues 1 to 853)
  AUTHORS   Ema,M., Sogawa,K., Watanabe,N., Chujoh,Y., Matsushita,N., Gotoh,O.,
            Funae,Y. and Fujii-Kuriyama,Y.
  TITLE     cDNA cloning and structure of mouse putative Ah receptor
  JOURNAL   Biochem Biophys Res Commun 184 (1), 246-253 (1992)
   PUBMED   1314586
REFERENCE   10 (residues 1 to 853)
  AUTHORS   Okino,S.T., Pendurthi,U.R. and Tukey,R.H.
  TITLE     Phorbol esters inhibit the dioxin receptor-mediated transcriptional
            activation of the mouse Cyp1a-1 and Cyp1a-2 genes by
            2,3,7,8-tetrachlorodibenzo-p-dioxin
  JOURNAL   J Biol Chem 267 (10), 6991-6998 (1992)
   PUBMED   1313028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Apr 28, 2015 this sequence version replaced NP_037281.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AM902286.1, AJ821851.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..853
                     /product="aryl hydrocarbon receptor isoform 1"
                     /note="ah receptor"
                     /calculated_mol_wt=96040
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     mat_peptide     10..853
                     /product="Aryl hydrocarbon receptor. /id=PRO_0000013465"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
                     /calculated_mol_wt=95246
     Region          12..15
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          27..87
                     /region_name="bHLH-PAS_AhR"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in aryl hydrocarbon receptor (AhR) and
                     similar proteins; cd11436"
                     /db_xref="CDD:381442"
     Site            order(33..39,41,43,64..66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381442"
     Region          36..41
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          37..65
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Site            order(38,41..42,45..46,48..49,52..56,64..66,69..79,82,
                     85..86)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381442"
     Region          49..81
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          63..71
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:P35869"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          111..>181
                     /region_name="PAS"
                     /note="PAS fold; pfam00989"
                     /db_xref="CDD:395786"
     Region          116..124
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P30561"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          264..266
                     /region_name="Required for maintaining the overall
                     integrity of the AHR:ARNT heterodimer and its
                     transcriptional activity.
                     /evidence=ECO:0000250|UniProtKB:P30561"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     Region          295..380
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(298,302,308,322..325,351,356)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(319,323,331,334..335,363,365)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          429..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41738.2)"
     CDS             1..853
                     /gene="Ahr"
                     /coded_by="NM_013149.3:29..2590"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25690"
                     /db_xref="RGD:2074"
ORIGIN      
        1 mssganitya srkrrkpvqk tvkpvpaegi ksnpskrhrd rlnteldrla sllpfpqdvi
       61 skldklsvlr lsvsylraks ffdvalkstp adrsrgqdqc raqvrdwqdl qegefllqal
      121 ngfvlvvtad alvfyassti qdylgfqqsd vihqsvyeli htedraefqr qlhwalnpsq
      181 ctdsaqgvde thglpqpavy ytpdqlppen tafmercfrc rlrclldnss gflamnfqgr
      241 lkylhgqnkk gkdgallppq lalfaiatpl qppsileirt knfifrtkhk ldftpigcda
      301 kgqlilgyte velcnkgsgy qfihaadmlh caeshirmik tgesgmtvfr llakhsrwrw
      361 vqsnarliyr ngrpdyiiat qrpltdeegr ehlqkrsmtl pfmfatgkav lyeisspfsp
      421 imdplpirtk sntsrkdwap qstpskdsfh pnslmsaliq qdesiylcpp sspapldshf
      481 lmdsmsecgs wqgsfaaasn eallkheeir htqdvnltls ggpselfpdn knndlysimr
      541 nlgidfedir smqneeffrt dssgevdfkd iditdeilty vqdslnnstl lnsacqqqpv
      601 sqhlscmlqe rlqleqqqql qqqhptqtle pqrqlcqvev pqhelgqktk hmqvngmfas
      661 wnpappvsfs cpqqerkhys lfsglqgtaq efpyksevds mpytqnfapc nqsllpehsk
      721 gtqldfpgrd ferslhpnas nledfvsclq vpenqrhgin sqsamvspqa yyagamsmyq
      781 cqagpqhtpv dqmqyspeip gsqaflskfq spsilneays adlssighlq taahlprlae
      841 aqplpditps gfl
//
LOCUS       NP_062074                430 aa            linear   ROD 27-APR-2025
DEFINITION  C-terminal-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_062074 XP_001062979 XP_001063046 XP_001063097
VERSION     NP_062074.2
DBSOURCE    REFSEQ: accession NM_019201.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ivanova,D., Imig,C., Camacho,M., Reinhold,A., Guhathakurta,D.,
            Montenegro-Venegas,C., Cousin,M.A., Gundelfinger,E.D.,
            Rosenmund,C., Cooper,B. and Fejtova,A.
  TITLE     CtBP1-Mediated Membrane Fission Contributes to Effective Recycling
            of Synaptic Vesicles
  JOURNAL   Cell Rep 30 (7), 2444-2459 (2020)
   PUBMED   32075774
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Hu,K., Li,Y., Yu,H. and Hu,Y.
  TITLE     CTBP1 Confers Protection for Hippocampal and Cortical Neurons in
            Rat Models of Alzheimer's Disease
  JOURNAL   Neuroimmunomodulation 26 (3), 139-152 (2019)
   PUBMED   31340205
  REMARK    GeneRIF: CTBP1 Confers Protection for Hippocampal and Cortical
            Neurons in Rat Models of Alzheimer's Disease.
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Rocca,D.L., Wilkinson,K.A. and Henley,J.M.
  TITLE     SUMOylation of FOXP1 regulates transcriptional repression via CtBP1
            to drive dendritic morphogenesis
  JOURNAL   Sci Rep 7 (1), 877 (2017)
   PUBMED   28408745
  REMARK    GeneRIF: Results shed light on the binding of CtBP1 protein to
            SUMOylated Foxp1 to repress the genetic transcription and drive
            dendritic morphogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Chinnadurai,G.
  TITLE     CtBP, an unconventional transcriptional corepressor in development
            and oncogenesis
  JOURNAL   Mol Cell 9 (2), 213-224 (2002)
   PUBMED   11864595
  REMARK    GeneRIF: CtBp proteins repress transcription in a histone
            deacetylase dependent or independent manner.
            Review article
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Riefler,G.M. and Firestein,B.L.
  TITLE     Binding of neuronal nitric-oxide synthase (nNOS) to
            carboxyl-terminal-binding protein (CtBP) changes the localization
            of CtBP from the nucleus to the cytosol: a novel function for
            targeting by the PDZ domain of nNOS
  JOURNAL   J Biol Chem 276 (51), 48262-48268 (2001)
   PUBMED   11590170
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Spano,S., Silletta,M.G., Colanzi,A., Alberti,S., Fiucci,G.,
            Valente,C., Fusella,A., Salmona,M., Mironov,A., Luini,A. and
            Corda,D.
  TITLE     Molecular cloning and functional characterization of brefeldin
            A-ADP-ribosylated substrate. A novel protein involved in the
            maintenance of the Golgi structure
  JOURNAL   J Biol Chem 274 (25), 17705-17710 (1999)
   PUBMED   10364211
  REMARK    Erratum:[J Biol Chem 1999 Aug 27;274(35):25188. Spanfo S [corrected
            to Spano S]]
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Di Girolamo,M., Silletta,M.G., De Matteis,M.A., Braca,A.,
            Colanzi,A., Pawlak,D., Rasenick,M.M., Luini,A. and Corda,D.
  TITLE     Evidence that the 50-kDa substrate of brefeldin A-dependent
            ADP-ribosylation binds GTP and is modulated by the G-protein beta
            gamma subunit complex
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7065-7069 (1995)
   PUBMED   7624370
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Belgrader,P., Dey,R. and Berezney,R.
  TITLE     Molecular cloning of matrin 3. A 125-kilodalton protein of the
            nuclear matrix contains an extensive acidic domain
  JOURNAL   J Biol Chem 266 (15), 9893-9899 (1991)
   PUBMED   2033075
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF067795.2.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001062979.1, XP_001063046.1, XP_001063097.1, NP_062074.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF067795.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..430
                     /product="C-terminal-binding protein 1"
                     /note="C-terminus binding protein 3/brefeldin A (BFA)
                     adenosine diphosphate-ribosylated substrate; ctBP3;
                     C-terminal-binding protein 3; 50 kDa BFA-dependent
                     ADP-ribosylation substrate; brefeldin A-ADP-riboslyated
                     substrate; 50-kDa BFA-induced ADP-ribosylated substrate"
                     /calculated_mol_wt=46497
     Region          1..59
                     /region_name="Interaction with GLIS2 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Region          17..335
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(86,89..90,255,304,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(89,117,169..170,172..174,192..196,225..227,229,232,
                     253..255,279..280,304,306..307)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          277..349
                     /region_name="Interaction with GLIS2 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13363; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Site            364..365
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1.
                     /evidence=ECO:0000250|UniProtKB:Q13363; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Site            377..378
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1.
                     /evidence=ECO:0000250|UniProtKB:Q13363; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Region          398..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Site            399..400
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1 and CAPN3.
                     /evidence=ECO:0000250|UniProtKB:Q13363; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13363; propagated from
                     UniProtKB/Swiss-Prot (Q9Z2F5.3)"
     CDS             1..430
                     /gene="Ctbp1"
                     /gene_synonym="50-kDaBFA-inducedADP-ribosylatedsubstrate;
                     Bars; BARS-50; CtBP3/BARS"
                     /coded_by="NM_019201.3:383..1675"
                     /db_xref="GeneID:29382"
                     /db_xref="RGD:2441"
ORIGIN      
        1 msgvrppimn gpmhprplva lldgrdctve mpilkdvatv afcdaqstqe ihekvlneav
       61 galmyhtitl tredlekfka lriivrigsg fdnidiksag dlgiavcnvp aasveetads
      121 tlchilnlyr rttwlhqalr egtrvqsveq irevasgaar irgetlgiig lgrvgqaval
      181 rakafgfnvl fydpylsdgi eralglqrvs tlqdllfhsd cvtlhcglne hnhhlindft
      241 vkqmrqgafl vntargglvd ekalaqalke grirgaaldv hesepfsfsq gplkdapnli
      301 ctphaawyse qasiemreea areirraitg ripdslkncv nkdhltaath wasmdpavvh
      361 pelngaaysr yppgvvsvap tgipaavegi vpsamslshg lppvahppha pspgqtvkpe
      421 adrdhttdql
//
LOCUS       NP_071971                102 aa            linear   ROD 27-APR-2025
DEFINITION  death-associated protein 1 [Rattus norvegicus].
ACCESSION   NP_071971
VERSION     NP_071971.1
DBSOURCE    REFSEQ: accession NM_022526.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Koren,I., Reem,E. and Kimchi,A.
  TITLE     DAP1, a novel substrate of mTOR, negatively regulates autophagy
  JOURNAL   Curr Biol 20 (12), 1093-1098 (2010)
   PUBMED   20537536
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Feinstein,E., Druck,T., Kastury,K., Berissi,H., Goodart,S.A.,
            Overhauser,J., Kimchi,A. and Huebner,K.
  TITLE     Assignment of DAP1 and DAPK--genes that positively mediate
            programmed cell death triggered by IFN-gamma--to chromosome regions
            5p12.2 and 9q34.1, respectively
  JOURNAL   Genomics 29 (1), 305-307 (1995)
   PUBMED   8530096
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Deiss,L.P., Feinstein,E., Berissi,H., Cohen,O. and Kimchi,A.
  TITLE     Identification of a novel serine/threonine kinase and a novel 15-kD
            protein as potential mediators of the gamma interferon-induced cell
            death
  JOURNAL   Genes Dev 9 (1), 15-30 (1995)
   PUBMED   7828849
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Shah,A.
  TITLE     Tuberculous pleural effusion: a diagnostic problem
  JOURNAL   Indian J Chest Dis Allied Sci 34 (3), 115-116 (1992)
   PUBMED   1302217
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Belokrylov,G.A. and Zhitnukhin,Iu.L.
  TITLE     [Effect of antibodies to rat and human cerebral cortex and white
            matter on heterologous T- and B-cells]
  JOURNAL   Zh Mikrobiol Epidemiol Immunobiol (9), 66-70 (1976)
   PUBMED   1087798
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1, BC060569.1 and FM053394.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U05334.1, FQ228865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..102
                     /product="death-associated protein 1"
                     /note="DAP-1"
                     /calculated_mol_wt=11034
     Region          1..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QX67.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P51397; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000250|UniProtKB:P51397; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     Region          12..101
                     /region_name="DAP"
                     /note="Death-associated protein; pfam15228"
                     /db_xref="CDD:464571"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91XC8; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51397; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51397; propagated from
                     UniProtKB/Swiss-Prot (Q9QX67.3)"
     CDS             1..102
                     /gene="Dap"
                     /gene_synonym="Rap7a"
                     /coded_by="NM_022526.2:193..501"
                     /db_xref="GeneID:64322"
                     /db_xref="RGD:620641"
ORIGIN      
        1 mssppegkle tkaghppavk vagirivqkh phtgdgkekk dkddqewest sppkptvyis
       61 gviargdkdf ppaaaqvahq kphasmdkhv sprtqhiqqp rk
//
LOCUS       NP_037067                175 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-crystallin B chain [Rattus norvegicus].
ACCESSION   NP_037067
VERSION     NP_037067.1
DBSOURCE    REFSEQ: accession NM_012935.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Bartelt-Kirbach,B. and Golenhofen,N.
  TITLE     Regulation of rat HspB5/alphaB-Crystallin by microRNAs miR-101a-3p,
            miR-140-5p, miR-330-5p, and miR-376b-3p
  JOURNAL   Cell Stress Chaperones 28 (6), 787-799 (2023)
   PUBMED   37584866
  REMARK    GeneRIF: Regulation of rat HspB5/alphaB-Crystallin by microRNAs
            miR-101a-3p, miR-140-5p, miR-330-5p, and miR-376b-3p.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Bartelt-Kirbach,B., Wiegreffe,C., Birk,S., Baur,T., Moron,M.,
            Britsch,S. and Golenhofen,N.
  TITLE     HspB5/alphaB-crystallin phosphorylation at S45 and S59 is essential
            for protection of the dendritic tree of rat hippocampal neurons
  JOURNAL   J Neurochem 157 (6), 2055-2069 (2021)
   PUBMED   33220080
  REMARK    GeneRIF: HspB5/alphaB-crystallin phosphorylation at S45 and S59 is
            essential for protection of the dendritic tree of rat hippocampal
            neurons.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Wang,L., Nie,Q., Gao,M., Yang,L., Xiang,J.W., Xiao,Y., Liu,F.Y.,
            Gong,X.D., Fu,J.L., Wang,Y., Nguyen,Q.D., Liu,Y., Liu,M. and
            Li,D.W.
  TITLE     The transcription factor CREB acts as an important regulator
            mediating oxidative stress-induced apoptosis by suppressing
            alphaB-crystallin expression
  JOURNAL   Aging (Albany NY) 12 (13), 13594-13617 (2020)
   PUBMED   32554860
  REMARK    GeneRIF: The transcription factor CREB acts as an important
            regulator mediating oxidative stress-induced apoptosis by
            suppressing alphaB-crystallin expression.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Hang,L.H., Chen,H.M., Yu,J.M., Xu,Y. and Li,S.N.
  TITLE     Evidence of the involvement of spinal alphaB-crystallin in the
            maintenance of bone cancer pain in rats
  JOURNAL   Pharmacol Rep 72 (1), 208-213 (2020)
   PUBMED   32016842
  REMARK    GeneRIF: Evidence of the involvement of spinal alphaB-crystallin in
            the maintenance of bone cancer pain in rats.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Roquemore,E.P., Chevrier,M.R., Cotter,R.J. and Hart,G.W.
  TITLE     Dynamic O-GlcNAcylation of the small heat shock protein alpha
            B-crystallin
  JOURNAL   Biochemistry 35 (11), 3578-3586 (1996)
   PUBMED   8639509
  REMARK    GeneRIF: Alpha crystallin is a moonlighting protein that functions
            as a heat shock protein as well as a lens crystallin.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Atomi,Y., Yamada,S. and Nishida,T.
  TITLE     Early changes of alpha B-crystallin mRNA in rat skeletal muscle to
            mechanical tension and denervation
  JOURNAL   Biochem Biophys Res Commun 181 (3), 1323-1330 (1991)
   PUBMED   1764082
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Bhat,S.P., Horwitz,J., Srinivasan,A. and Ding,L.
  TITLE     Alpha B-crystallin exists as an independent protein in the heart
            and in the lens
  JOURNAL   Eur J Biochem 202 (3), 775-781 (1991)
   PUBMED   1765091
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Atomi,Y., Yamada,S., Strohman,R. and Nonomura,Y.
  TITLE     Alpha B-crystallin in skeletal muscle: purification and
            localization
  JOURNAL   J Biochem 110 (5), 812-822 (1991)
   PUBMED   1783614
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Iwaki,A., Iwaki,T., Goldman,J.E. and Liem,R.K.
  TITLE     Multiple mRNAs of rat brain alpha-crystallin B chain result from
            alternative transcriptional initiation
  JOURNAL   J Biol Chem 265 (36), 22197-22203 (1990)
   PUBMED   2176207
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Bhat,S.P. and Nagineni,C.N.
  TITLE     alpha B subunit of lens-specific protein alpha-crystallin is
            present in other ocular and non-ocular tissues
  JOURNAL   Biochem Biophys Res Commun 158 (1), 319-325 (1989)
   PUBMED   2912453
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M55534.1 and CK357656.1.
            
            Summary: This gene encodes subunit b, one of two subunits of
            alpha-crystallin, which is a high molecular weight, soluble
            aggregate and is a member of the small heat shock protein family.
            The encoded protein has been identified as a moonlighting protein
            based on its ability to perform mechanistically distinct functions.
            It acts as a molecular chaperone and is the major protein in the
            eye lens, maintaining the transparency and refractive index of the
            lens. Alternate promoter usage results in different transcript
            variants encoding the same protein. [provided by RefSeq, Sep 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228589.1, M55534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 8639509
            RefSeq Select criteria          :: based on conservation,
                                               expression, longest protein
            regulatory uORF                 :: PMID: 2176207
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q23"
     Protein         1..175
                     /product="alpha-crystallin B chain"
                     /note="alpha(B)-crystallin; Crystallin, alpha polypeptide
                     2"
                     /calculated_mol_wt=19958
     Region          1..55
                     /region_name="Crystallin"
                     /note="Alpha crystallin A chain, N terminal; pfam00525"
                     /db_xref="CDD:425732"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P02510, ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P23928.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02510; propagated from
                     UniProtKB/Swiss-Prot (P23928.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02510; propagated from
                     UniProtKB/Swiss-Prot (P23928.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P23928.1)"
     Region          67..150
                     /region_name="ACD_alphaB-crystallin_HspB5"
                     /note="Alpha-crystallin domain found in the small heat
                     shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa).
                     sHsps are molecular chaperones that suppress protein
                     aggregation and protect against cell stress, and are
                     generally active as large oligomers...; cd06498"
                     /db_xref="CDD:107246"
     Site            order(68..72,78,80,82..83,120,141..142)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107246"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02511; propagated from
                     UniProtKB/Swiss-Prot (P23928.1)"
     Region          142..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23928.1)"
     Site            166
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02511; propagated from
                     UniProtKB/Swiss-Prot (P23928.1)"
     Site            170
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:8639509. /id=CAR_000058;
                     propagated from UniProtKB/Swiss-Prot (P23928.1)"
     CDS             1..175
                     /gene="Cryab"
                     /gene_synonym="AACRYA"
                     /coded_by="NM_012935.4:330..857"
                     /db_xref="GeneID:25420"
                     /db_xref="RGD:2414"
ORIGIN      
        1 mdiaihhpwi rrpffpfhsp srlfdqffge hllesdlfst atslspfylr ppsflrapsw
       61 idtglsemrm ekdrfsvnld vkhfspeelk vkvlgdviev hgkheerqde hgfisrefhr
      121 kyripadvdp ltitsslssd gvltvngprk qasgpertip itreekpavt aapkk
//
LOCUS       NP_001292557             640 aa            linear   ROD 27-APR-2025
DEFINITION  epsin-2 isoform b [Rattus norvegicus].
ACCESSION   NP_001292557 XP_006246584
VERSION     NP_001292557.1
DBSOURCE    REFSEQ: accession NM_001305628.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Sakai,E., Miura,Y., Suzuki-Kouyama,E., Oka,K., Tachibana,M.,
            Kawabata,K., Sakurai,F. and Mizuguchi,H.
  TITLE     A mammalian mirtron miR-1224 promotes tube-formation of human
            primary endothelial cells by targeting anti-angiogenic factor
            epsin2
  JOURNAL   Sci Rep 7 (1), 5541 (2017)
   PUBMED   28717225
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Sen,A., Madhivanan,K., Mukherjee,D. and Aguilar,R.C.
  TITLE     The epsin protein family: coordinators of endocytosis and signaling
  JOURNAL   Biomol Concepts 3 (2), 117-126 (2012)
   PUBMED   22942912
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Chen,H., Ko,G., Zatti,A., Di Giacomo,G., Liu,L., Raiteri,E.,
            Perucco,E., Collesi,C., Min,W., Zeiss,C., De Camilli,P. and
            Cremona,O.
  TITLE     Embryonic arrest at midgestation and disruption of Notch signaling
            produced by the absence of both epsin 1 and epsin 2 in mice
  JOURNAL   Proc Natl Acad Sci U S A 106 (33), 13838-13843 (2009)
   PUBMED   19666558
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Hussain,N.K., Yamabhai,M., Bhakar,A.L., Metzler,M., Ferguson,S.S.,
            Hayden,M.R., McPherson,P.S. and Kay,B.K.
  TITLE     A role for epsin N-terminal homology/AP180 N-terminal homology
            (ENTH/ANTH) domains in tubulin binding
  JOURNAL   J Biol Chem 278 (31), 28823-28830 (2003)
   PUBMED   12750376
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Polo,S., Sigismund,S., Faretta,M., Guidi,M., Capua,M.R., Bossi,G.,
            Chen,H., De Camilli,P. and Di Fiore,P.P.
  TITLE     A single motif responsible for ubiquitin recognition and
            monoubiquitination in endocytic proteins
  JOURNAL   Nature 416 (6879), 451-455 (2002)
   PUBMED   11919637
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Rosenthal,J.A., Chen,H., Slepnev,V.I., Pellegrini,L., Salcini,A.E.,
            Di Fiore,P.P. and De Camilli,P.
  TITLE     The epsins define a family of proteins that interact with
            components of the clathrin coat and contain a new protein module
  JOURNAL   J Biol Chem 274 (48), 33959-33965 (1999)
   PUBMED   10567358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000010.1, CB583573.1
            and BC094524.1.
            
            On Mar 24, 2015 this sequence version replaced XP_006246584.1.
            
            Summary: The protein encoded by this gene is a member of the epsin
            protein family. Epsin proteins are endocytic adaptors that function
            in the formation of clatherin-coated vesicles. Epsins contain a
            highly conserved N-terminal homology domain that binds
            phosphatidylinositol 4,5-bisphosphate in the plasma membrane, two
            or three ubiquitin interacting motifs, two clathrin-binding motifs,
            a cluster of aspartate-proline-tryptophan/phenylalanine repeats,
            and two or three asparagine-proline-phenylalanine tripeptide
            repeats at the C-terminus. In mouse, simultaneous knockout of this
            gene and its paralog results in embryonic arrest due to disruption
            of Notch signaling, suggesting a role as a specialized endocytic
            adaptor. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longer isoform (b). Variants 2 and 3
            encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211574.1, SRR26360190.60415.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..640
                     /product="epsin-2 isoform b"
                     /note="EPS-15-interacting protein 2; EH domain binding
                     protein epsin 2"
                     /calculated_mol_wt=68322
     Region          19..141
                     /region_name="ENTH_Epsin"
                     /note="Epsin N-Terminal Homology (ENTH) domain of Epsin
                     family; cd16990"
                     /db_xref="CDD:340787"
     Site            order(25,29..30,63,69,73)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:340787"
     CDS             1..640
                     /gene="Epn2"
                     /coded_by="NM_001305628.1:354..2276"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:60443"
                     /db_xref="RGD:619773"
ORIGIN      
        1 mttssirrqm knivnnysea eikvreatsn dpwgpssslm teiadltynv vafseimsmv
       61 wkrlndhgkn wrhvykaltl ldyliktgse rvaqqcreni faiqtlkdfq yidrdgkdqg
      121 invrekskql vallkdeerl kvervqalkt kermaqvatg vgsnqitfgr gssqpnlsts
      181 yseqeygkag gspasyhgsp easlcpqhrt gamlgqseel qplsqrhpcl phlglashpn
      241 gdwaqpcltc draaratspr vsseleqarp qtsgeeelql qlalamsrev aeqeerlrrg
      301 ddlrlqmale esrrdtvkvp kkkevkacck pgshsqqttl ldlmdalpss gpvaqktepw
      361 stgtpanqtn pwggtvapan isdpwpsfgt kpaasvdpwg vpttasiqsv pknsdpwaas
      421 qqpasdagkt adawgaakps pasgsfelfs nfngtvkddf sefdnlrtsk kpaesgasvp
      481 pqdsrttspd lfesqsltsa sskpssarkt pesflgpnaa lvnldslvtk pnppaqslnp
      541 flapgaaapa pvnpfqvnqp qpltlnqlrg spvlgssasf gsgpgvetva pmpsvaphsa
      601 lgatgssltp lgptamnmvg svgippsaaq pagttnpfll
//
LOCUS       NP_001003402            1977 aa            linear   ROD 27-APR-2025
DEFINITION  echinoderm microtubule-associated protein-like 5 [Rattus
            norvegicus].
ACCESSION   NP_001003402 XP_243280
VERSION     NP_001003402.2
DBSOURCE    REFSEQ: accession NM_001003402.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1977)
  AUTHORS   Takizawa,C., Minematsu,T., Nakagami,G., Kitamura,A., Koudounas,S.,
            Kunimitsu,M. and Sanada,H.
  TITLE     Expression levels of NPPB, ITGB6, CPNE4, EML5, and ITSN1 in fresh
            exudates swabbed from critically colonised and infected
            full-thickness wounds in rats
  JOURNAL   Int Wound J 20 (4), 1088-1097 (2023)
   PUBMED   36307995
  REMARK    GeneRIF: Expression levels of NPPB, ITGB6, CPNE4, EML5, and ITSN1
            in fresh exudates swabbed from critically colonised and infected
            full-thickness wounds in rats.
REFERENCE   2  (residues 1 to 1977)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   3  (residues 1 to 1977)
  AUTHORS   O'Connor,V., Houtman,S.H., De Zeeuw,C.I., Bliss,T.V. and
            French,P.J.
  TITLE     Eml5, a novel WD40 domain protein expressed in rat brain
  JOURNAL   Gene 336 (1), 127-137 (2004)
   PUBMED   15225882
  REMARK    GeneRIF: Eml5 may play a role in the regulation of cytoskeletal
            rearrangements during neuronal development and in adult brain.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Aug 30, 2012 this sequence version replaced NP_001003402.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1977
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..1977
                     /product="echinoderm microtubule-associated protein-like
                     5"
                     /note="EMAP-5; EMAP-like protein 5; echinoderm microtubule
                     associated protein like 5"
                     /calculated_mol_wt=219658
     Region          <2..49
                     /region_name="HELP"
                     /note="HELP motif; pfam03451"
                     /db_xref="CDD:460922"
     Region          58..438
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          59..100
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          64..104
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          104..145
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          110..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..187
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          153..201
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..233
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          203..233
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          235..273
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          240..273
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          280..321
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          286..321
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          321..592
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(323,342,346,352..353,364..365,383,387,393..394,
                     406..407,424,429,435..436,450,467,470,478..479,508..509,
                     534,539,545..546,561..562,580,585,591..592)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          323..362
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          328..352
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          364..403
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          369..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          406..445
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          411..451
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          449..488
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          522..560
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          561..601
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          609..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          <672..715
                     /region_name="HELP"
                     /note="HELP motif; pfam03451"
                     /db_xref="CDD:460922"
     Region          720..1140
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          725..766
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          730..769
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          770..811
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          775..852
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          814..853
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          857..900
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          861..900
                     /region_name="WD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          901..940
                     /region_name="WD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          907..994
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          941..992
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          996..1035
                     /region_name="WD 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1001..1035
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1038..1077
                     /region_name="WD 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1043..1069
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1080..1120
                     /region_name="WD 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1085..1110
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1128..1166
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1178..1236
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1236..1276
                     /region_name="WD 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1241..1266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1274..1299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1323..1363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          <1363..1410
                     /region_name="HELP"
                     /note="HELP motif; pfam03451"
                     /db_xref="CDD:460922"
     Region          1420..1471
                     /region_name="WD 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1426..1475
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1428..1815
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          1475..1516
                     /region_name="WD 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1480..1518
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1519..1558
                     /region_name="WD 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1525..1566
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1568..1606
                     /region_name="WD 24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1573..1605
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1608..1654
                     /region_name="WD 25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1613..1676
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1697..1970
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          1699..1739
                     /region_name="WD 26"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1705..1743
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1741..1782
                     /region_name="WD 27"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1783..1822
                     /region_name="WD 28"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1788..1821
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1834..1892
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1895..1934
                     /region_name="WD 29"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     Region          1900..1939
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1940..1977
                     /region_name="WD 30"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ED65.2)"
     CDS             1..1977
                     /gene="Eml5"
                     /coded_by="NM_001003402.2:380..6313"
                     /db_xref="GeneID:444982"
                     /db_xref="RGD:1303275"
ORIGIN      
        1 maarsapsch lrlewvygyr ghqcrnnlyy taakeivyfv agvgvvyspr ehrqkfyrgh
       61 sddiislalh pervlvatgq vgkepyicvw dsytvqtvsv lkdvhthgia clafdldgqr
      121 lvsvgldskn avcvwdwkrg kmlsmapght drifdiswdl yqpnklvscg vkhikfwslc
      181 gnaltpkrgv fgktgdlqti lclacardel tysgalngdi yvwkginlir tiqgahtagi
      241 fsmnaceegf atggrdgcir lwdltfkpit vidlreteqg ykglsvrsvc wrgdhilvgt
      301 qdseifeivv hernkpflim qghcegelwa lavhptkpla vtgsddrsvr iwslvdhali
      361 arcnmdepir caavnadgvh lalgmkdgsl tvlrvrdmte vvhikdrkea ihelkyspdg
      421 tylavgcnds svdiygvaqr ykkvgecvgs lsfithldws sdskylqtnd gsgkrllykm
      481 pggkevtske evkgmhwasw tcvaglevng iwpkysdind insvdgnyvg qvlvtaddyg
      541 vvklfrypcl rkgakfrkyi ghsahvtnvr wshdyqwvis iggadhsvfq wkfiperklk
      601 dalhiapqes ltesnsdesd sdlsdvpeld seieqetqlt yhrqvykedl pqlkeqckek
      661 qksatskrre rapgnsirlh fihgyrgydc rsnlfytqig eivyhvaavg viynrqqntq
      721 rfylghdddi lclaihplkd yvatgqvgrd psihvwdtet ikplsilkgy hqygicavdf
      781 sadgkrlasv giddshtivl wdwkkgekls vargskdkif vvkmnpyvpd klitagikhm
      841 kfwrragggl igrkgyvgtl gkndtmmcav ygwteemafs gtstgdvciw rdvflvktvk
      901 ahdgpvfsmh alekgfvtgg kdgvvalwdd sferclktya ikradlapgs kglllednps
      961 iraislghgh ilvgtkngei levdksgpvt llvqghmege vwglathpyl picatvsddk
     1021 tlriwdlsps hcmlavrklk kggrcccfsp dgkalavgln dgsflmanad tledlvsfhh
     1081 rkdvisdiqf spgsgkylav ashdsfvdiy nvtsskrvgv ckgatsyith idwdsrgkll
     1141 qvntgakeql ffeaprgkkq tipsveveki swatwtsvlg lccegiwpii gevtdvtasc
     1201 ltsdkmvlat gddlgfvklf rypakgkfgk fkkyvahsth vtnvrwtydd smlvtlggad
     1261 mslmvwtsev erhrekkncd seesdtdsee dggydsdvtr eneisytira lstnirpmfg
     1321 vkphlqqkep svderqgvvr gsrppvsrap pqpeklqsnn vgkkkrpied lvlelafgyr
     1381 grdcrnnvhy lndgddiiyh tasvgilhnv atgtqsfyqe hnddilcltv nqhpkfiniv
     1441 atgqvgdsad msatapsvhi wdavnkqtls ilrcshskgv csvsfsatgk lllsvgldpe
     1501 htvtiwrwqe gakiasrggh nqrifvaefr pdsdtqfvsv gikhvkfwtl agrallskkg
     1561 llstledarm qtmlavafga nnltftgtis gdvcvwkdhi lcrvvarahn gpvfamyttl
     1621 rdglivtggk erpskeggav klwdqelrrc rafrletgqv tdcvrsvcrg kgkilvgtrn
     1681 seiievgekn aacnilvngh vdgpiwglat hpsrdfflsa aedgtvrlwd iadkkmlnkv
     1741 nlghaartvc yspegdmvai gmkngefiil lvsslkiwgk krdrrcaihd irfspdsryl
     1801 avgssensvd fydltlgptl nrisyckdip sfviqmdfsa dsrhlqvssg cykrhvyevp
     1861 sgkhlvdhaa idritwatwt silgdevmgi wsrhaekadv tcacvshsgi slvtgddfgm
     1921 vklydfpcpe kfakhkrflg hsphvtnirf tsgdrhvvsa ggddcsllvw kcvhtph
//
LOCUS       NP_001240847             100 aa            linear   ROD 27-APR-2025
DEFINITION  noncompact myelin-associated protein [Rattus norvegicus].
ACCESSION   NP_001240847 XP_001072162 XP_002726685 XP_002726686
VERSION     NP_001240847.1
DBSOURCE    REFSEQ: accession NM_001253918.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Ryu,E.J., Yang,M., Gustin,J.A., Chang,L.W., Freimuth,R.R.,
            Nagarajan,R. and Milbrandt,J.
  TITLE     Analysis of peripheral nerve expression profiles identifies a novel
            myelin glycoprotein, MP11
  JOURNAL   J Neurosci 28 (30), 7563-7573 (2008)
   PUBMED   18650334
  REMARK    GeneRIF: This study identified an evolutionarily conserved novel
            component of myelin called Mp11. The Mp11 genomic locus contains
            multiple conserved Egr binding sites, and Mp11 induction is
            regulated by the expression of Egr2. and expression in peripheral
            nerve.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB782535.1.
            
            On or before Dec 11, 2011 this sequence version replaced
            XP_001072162.1, XP_002726685.1, XP_002726686.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB782535.1, CB608200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..100
                     /product="noncompact myelin-associated protein"
                     /note="myelin protein of 11 kDa"
                     /calculated_mol_wt=10640
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M2Z5.2)"
     Region          58..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1M2Z5.2)"
     CDS             1..100
                     /gene="Ncmap"
                     /gene_synonym="Mp11"
                     /coded_by="NM_001253918.1:159..461"
                     /db_xref="GeneID:689826"
                     /db_xref="RGD:1587554"
ORIGIN      
        1 mttattlgda vfslnmtrge dilykssgai vaaivvvvvi ivtlvlillk mynrrmrtrr
       61 elepkspkpp vppaldpnsn gsqqpaavts dpadvpvetr
//
LOCUS       NP_068538                261 aa            linear   ROD 27-APR-2025
DEFINITION  oligodendrocyte transcription factor 1 [Rattus norvegicus].
ACCESSION   NP_068538
VERSION     NP_068538.2
DBSOURCE    REFSEQ: accession NM_021770.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Zhao,H., Gao,X.Y., Liu,Z.H., Lin,J.W., Wang,S.P., Wang,D.X. and
            Zhang,Y.B.
  TITLE     Effects of the transcription factor Olig1 on the differentiation
            and remyelination of oligodendrocyte precursor cells after focal
            cerebral ischemia in rats
  JOURNAL   Mol Med Rep 20 (5), 4603-4611 (2019)
   PUBMED   31702031
  REMARK    GeneRIF: The data of the present study may help clinicians
            understand the expression pattern of Olig1 and its potential role
            in endogenous remyelination after ischemia, which may have
            implications for the treatment of diseases that lead to
            demyelination.
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Song,P., Xia,X., Han,T., Fang,H., Wang,Y., Dong,F., Zhang,R., Ge,P.
            and Shen,C.
  TITLE     BMSCs promote the differentiation of NSCs into oligodendrocytes via
            mediating Id2 and Olig expression through BMP/Smad signaling
            pathway
  JOURNAL   Biosci Rep 38 (5) (2018)
   PUBMED   30143582
  REMARK    GeneRIF: these data strongly suggest that bone marrow stromal cells
            (BMSCs) can promote the differentiation of Neural stem cells (NSCs)
            into oligodendrocytes through mediating Id2 and Olig1/2 expression
            by blocking the BMP/Smad signaling pathway
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Dai,J., Bercury,K.K., Ahrendsen,J.T. and Macklin,W.B.
  TITLE     Olig1 function is required for oligodendrocyte differentiation in
            the mouse brain
  JOURNAL   J Neurosci 35 (10), 4386-4402 (2015)
   PUBMED   25762682
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Zhu,W.H., Gao,Y., Lou,L.X. and Zhu,L.Q.
  TITLE     [Effect of Yishen Daluo Decoction on the expression of PLP, Olig1,
            and Olig2 in mice with experimental autoimmune encephalomyelitis]
  JOURNAL   Zhongguo Zhong Xi Yi Jie He Za Zhi 34 (5), 562-565 (2014)
   PUBMED   24941845
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Fang,F., Zhang,H., Zhang,Y., Xu,H., Huang,Q., Adilijiang,A.,
            Wang,J., Zhang,Z., Zhang,D., Tan,Q., He,J., Kong,L., Liu,Y. and
            Li,X.M.
  TITLE     Antipsychotics promote the differentiation of oligodendrocyte
            progenitor cells by regulating oligodendrocyte lineage
            transcription factors 1 and 2
  JOURNAL   Life Sci 93 (12-14), 429-434 (2013)
   PUBMED   23973956
  REMARK    GeneRIF: Olig1 and Olig2 expression are enhanced during
            antipsychotic drug induced differentiation of oligodendrocyte
            progenitor cells.
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Cheng,X., Wang,Y., He,Q., Qiu,M., Whittemore,S.R. and Cao,Q.
  TITLE     Bone morphogenetic protein signaling and olig1/2 interact to
            regulate the differentiation and maturation of adult
            oligodendrocyte precursor cells
  JOURNAL   Stem Cells 25 (12), 3204-3214 (2007)
   PUBMED   17872503
  REMARK    GeneRIF: Overexpression of olig1 and olig2 inhibits astrocyte
            differentiation and promotes oligodendrocyte differentiation of
            adult oligodendrocyte precursor cells.
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Lu,Q.R., Sun,T., Zhu,Z., Ma,N., Garcia,M., Stiles,C.D. and
            Rowitch,D.H.
  TITLE     Common developmental requirement for Olig function indicates a
            motor neuron/oligodendrocyte connection
  JOURNAL   Cell 109 (1), 75-86 (2002)
   PUBMED   11955448
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Zhou,Q. and Anderson,D.J.
  TITLE     The bHLH transcription factors OLIG2 and OLIG1 couple neuronal and
            glial subtype specification
  JOURNAL   Cell 109 (1), 61-73 (2002)
   PUBMED   11955447
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Wegner,M.
  TITLE     Expression of transcription factors during oligodendroglial
            development
  JOURNAL   Microsc Res Tech 52 (6), 746-752 (2001)
   PUBMED   11276127
  REMARK    Review article
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Lu,Q.R., Yuk,D., Alberta,J.A., Zhu,Z., Pawlitzky,I., Chan,J.,
            McMahon,A.P., Stiles,C.D. and Rowitch,D.H.
  TITLE     Sonic hedgehog--regulated oligodendrocyte lineage genes encoding
            bHLH proteins in the mammalian central nervous system
  JOURNAL   Neuron 25 (2), 317-329 (2000)
   PUBMED   10719888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On May 19, 2009 this sequence version replaced NP_068538.1.
            
            Summary: This gene is a member of the oligodendrocyte lineage gene
            family which encode basic helix-loop-helix transcription factors.
            Studies in mice show that it is coexpressed with Olig2 in neural
            progenitors, and has a role in the development and maturation of
            oligodendrocytes. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR22399484.1377726.1,
                                        SRR26643298.66116.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..261
                     /product="oligodendrocyte transcription factor 1"
                     /note="Olg-1 bHLH protein"
                     /calculated_mol_wt=27107
     Region          41..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WUQ3.2)"
     Region          96..165
                     /region_name="bHLH_TS_OLIG1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     oligodendrocyte transcription factor 1 (Oligo1) and
                     similar proteins; cd18942"
                     /db_xref="CDD:381512"
     Site            order(97,101,103..105,107,112,137..140)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381512"
     Site            order(110..111,114..115,117..118,141,144,148,150..151,155,
                     157..158)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381512"
     CDS             1..261
                     /gene="Olig1"
                     /gene_synonym="Olg1; oligo1"
                     /coded_by="NM_021770.4:94..879"
                     /db_xref="GeneID:60394"
                     /db_xref="RGD:621129"
ORIGIN      
        1 myyavsqarv naapatmlrp qrpgdvqlga slyelvgyrq ppisssssts ssstasllpk
       61 parekpeapl aeprgpapes ggaradakee qqqqqlrrki nsrerkrmqd lnlamdalre
      121 vilpysaahc qgapgrklsk iatlllarny illlgsslqe lrralgdgag paaprlllag
      181 lpllaaapgs vllapgavgp petlrptkyl slaldeppcg qfalpaggag spglcscavc
      241 kfphlvpagl glaavqaqfs k
//
LOCUS       NP_001258002             195 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001258002
VERSION     NP_001258002.1
DBSOURCE    REFSEQ: accession NM_001271073.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site at the 5' end of an exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U60562.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351,
                                           SAMN12840105 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..195
                     /product="amelogenin, X isoform isoform 2 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=20201
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          28..171
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     CDS             1..195
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271073.1:67..654"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqph ppshtlqphh
       61 hlpvvpaqqp vapqqpmmpv pghhsmtptq hhqpnippsa qqpfqqpfqp qaippqshqp
      121 mqpqsplhpm qplapqpplp plfsmqplsp ilpelpleaw patdktkree vafspmkwyq
      181 gtarhplnme tttek
//
LOCUS       NP_001007605             114 aa            linear   ROD 27-APR-2025
DEFINITION  large ribosomal subunit protein P1 [Rattus norvegicus].
ACCESSION   NP_001007605 XP_343404
VERSION     NP_001007605.1
DBSOURCE    REFSEQ: accession NM_001007604.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Perucho,L., Artero-Castro,A., Guerrero,S., Ramon y Cajal,S.,
            LLeonart,M.E. and Wang,Z.Q.
  TITLE     RPLP1, a crucial ribosomal protein for embryonic development of the
            nervous system
  JOURNAL   PLoS One 9 (6), e99956 (2014)
   PUBMED   24959908
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Mikula,M., Dzwonek,A., Karczmarski,J., Rubel,T., Dadlez,M.,
            Wyrwicz,L.S., Bomsztyk,K. and Ostrowski,J.
  TITLE     Landscape of the hnRNP K protein-protein interactome
  JOURNAL   Proteomics 6 (8), 2395-2406 (2006)
   PUBMED   16518874
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Vard,C., Guillot,D., Bargis,P., Lavergne,J.P. and Reboud,J.P.
  TITLE     A specific role for the phosphorylation of mammalian acidic
            ribosomal protein P2
  JOURNAL   J Biol Chem 272 (32), 20259-20262 (1997)
   PUBMED   9242705
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Wool,I.G., Chan,Y.L., Gluck,A. and Suzuki,K.
  TITLE     The primary structure of rat ribosomal proteins P0, P1, and P2 and
            a proposal for a uniform nomenclature for mammalian and yeast
            ribosomal proteins
  JOURNAL   Biochimie 73 (7-8), 861-870 (1991)
   PUBMED   1742361
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Ikeda,M., Saito,T., Endo,T., Tsurugi,K. and Onaya,T.
  TITLE     Thyrotropin stimulates the expression of an acidic ribosomal
            protein, P0, messenger ribonucleic acid in cultured rat thyroid
            (FRTL) cells
  JOURNAL   Endocrinology 128 (5), 2540-2547 (1991)
   PUBMED   1850354
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Lin,A., Wittmann-Liebold,B., McNally,J. and Wool,I.G.
  TITLE     The primary structure of the acidic phosphoprotein P2 from rat
            liver 60 S ribosomal subunits. Comparison with ribosomal 'A'
            proteins from other species
  JOURNAL   J Biol Chem 257 (15), 9189-9197 (1982)
   PUBMED   7096359
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC058151.1.
            
            On Nov 29, 2004 this sequence version replaced XP_343404.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058151.1, FQ120533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..114
                     /product="large ribosomal subunit protein P1"
                     /note="60S acidic ribosomal protein P1; ribosomal protein,
                     large, P1"
                     /calculated_mol_wt=11367
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P05386; propagated from
                     UniProtKB/Swiss-Prot (P19944.1)"
     Region          6..>63
                     /region_name="Ribosomal_P1"
                     /note="Ribosomal protein P1. This subfamily represents the
                     eukaryotic large ribosomal protein P1. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P1 is located in
                     the L12 stalk, with proteins...; cd05831"
                     /db_xref="CDD:100109"
     Region          69..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19944.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05386; propagated from
                     UniProtKB/Swiss-Prot (P19944.1)"
     CDS             1..114
                     /gene="Rplp1"
                     /coded_by="NM_001007604.2:112..456"
                     /db_xref="GeneID:140661"
                     /db_xref="RGD:621774"
ORIGIN      
        1 masvselaci ysalilhdde vtvtedkina likaagvnve pfwpglfaka lanvnigsli
       61 cnvgaggpap aagaapaggp apsaaaapae ekkveakkee seeseddmgf glfd
//
LOCUS       NP_001257955             169 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger CCHC domain-containing protein 10 [Rattus norvegicus].
ACCESSION   NP_001257955 XP_001073035 XP_346888
VERSION     NP_001257955.1
DBSOURCE    REFSEQ: accession NM_001271026.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089894.1.
            
            On or before Aug 29, 2012 this sequence version replaced
            XP_001073035.1, XP_346888.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089894.1, FQ227271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..169
                     /product="zinc finger CCHC domain-containing protein 10"
                     /note="zinc finger, CCHC domain containing 10"
                     /calculated_mol_wt=18183
     Region          13..50
                     /region_name="zf-CCHC_3"
                     /note="Zinc knuckle; pfam13917"
                     /db_xref="CDD:404753"
     CDS             1..169
                     /gene="Zcchc10"
                     /coded_by="NM_001271026.1:11..520"
                     /db_xref="GeneID:360524"
                     /db_xref="RGD:1308149"
ORIGIN      
        1 mhrliarrqa eankqhvrcq kclefghwty eckgkrkylh rpsrtaelkk alkekenrll
       61 qqsmgetnte rktkkkrrpk svtstsssds sasesssese tsasssseds dadgslssss
      121 sssaysssss ssssssssss dsdsssssss ssssesssdd eppkkrkkk
//
LOCUS       NP_113836                 95 aa            linear   ROD 27-APR-2025
DEFINITION  phospholemman precursor [Rattus norvegicus].
ACCESSION   NP_113836
VERSION     NP_113836.2
DBSOURCE    REFSEQ: accession NM_031648.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Hafver,T.L., Hodne,K., Wanichawan,P., Aronsen,J.M., Dalhus,B.,
            Lunde,P.K., Lunde,M., Martinsen,M., Enger,U.H., Fuller,W.,
            Sjaastad,I., Louch,W.E., Sejersted,O.M. and Carlson,C.R.
  TITLE     Protein Phosphatase 1c Associated with the Cardiac Sodium Calcium
            Exchanger 1 Regulates Its Activity by Dephosphorylating Serine
            68-phosphorylated Phospholemman
  JOURNAL   J Biol Chem 291 (9), 4561-4579 (2016)
   PUBMED   26668322
  REMARK    GeneRIF: Data suggest Ncx1 (sodium-calcium exchanger 1) is
            substrate-specifying Pp1c (protein phosphatase 1c) regulator
            protein, regulating Ncx1 activity via Ser-68-Plm dephosphorylation
            in cardiomyocytes; Plm/Ncx1/Pp1c complex is up-regulated in heart
            failure.
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Correll,R.N., Eder,P., Burr,A.R., Despa,S., Davis,J., Bers,D.M. and
            Molkentin,J.D.
  TITLE     Overexpression of the Na+/K+ ATPase alpha2 but not alpha1 isoform
            attenuates pathological cardiac hypertrophy and remodeling
  JOURNAL   Circ Res 114 (2), 249-256 (2014)
   PUBMED   24218169
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Wypijewski,K.J., Howie,J., Reilly,L., Tulloch,L.B., Aughton,K.L.,
            McLatchie,L.M., Shattock,M.J., Calaghan,S.C. and Fuller,W.
  TITLE     A separate pool of cardiac phospholemman that does not regulate or
            associate with the sodium pump: multimers of phospholemman in
            ventricular muscle
  JOURNAL   J Biol Chem 288 (19), 13808-13820 (2013)
   PUBMED   23532852
  REMARK    GeneRIF: PLM exists as a pump-inhibiting monomer and an
            unassociated oligomer.
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Chibalin,A.V., Heiny,J.A., Benziane,B., Prokofiev,A.V.,
            Vasiliev,A.V., Kravtsova,V.V. and Krivoi,I.I.
  TITLE     Chronic nicotine modifies skeletal muscle Na,K-ATPase activity
            through its interaction with the nicotinic acetylcholine receptor
            and phospholemman
  JOURNAL   PLoS One 7 (3), e33719 (2012)
   PUBMED   22442718
  REMARK    GeneRIF: Chronic nicotine modifies skeletal muscle Na,K-ATPase
            activity through its interaction with the nicotinic acetylcholine
            receptor and phospholemman.
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Tulloch,L.B., Howie,J., Wypijewski,K.J., Wilson,C.R., Bernard,W.G.,
            Shattock,M.J. and Fuller,W.
  TITLE     The inhibitory effect of phospholemman on the sodium pump requires
            its palmitoylation
  JOURNAL   J Biol Chem 286 (41), 36020-36031 (2011)
   PUBMED   21868384
  REMARK    GeneRIF: palmitoylation of PLM controls its turnover, and
            palmitoylated PLM inhibits the sodium pump.
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Moran,J., Morales-Mulia,M. and Pasantes-Morales,H.
  TITLE     Reduction of phospholemman expression decreases osmosensitive
            taurine efflux in astrocytes
  JOURNAL   Biochim Biophys Acta 1538 (2-3), 313-320 (2001)
   PUBMED   11336802
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Sweadner,K.J. and Rael,E.
  TITLE     The FXYD gene family of small ion transport regulators or channels:
            cDNA sequence, protein signature sequence, and expression
  JOURNAL   Genomics 68 (1), 41-56 (2000)
   PUBMED   10950925
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Chen,Z., Jones,L.R., O'Brian,J.J., Moorman,J.R. and Cala,S.E.
  TITLE     Structural domains in phospholemman: a possible role for the
            carboxyl terminus in channel inactivation
  JOURNAL   Circ Res 82 (3), 367-374 (1998)
   PUBMED   9486665
  REMARK    Review article
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Chen,L.S., Lo,C.F., Numann,R. and Cuddy,M.
  TITLE     Characterization of the human and rat phospholemman (PLM) cDNAs and
            localization of the human PLM gene to chromosome 19q13.1
  JOURNAL   Genomics 41 (3), 435-443 (1997)
   PUBMED   9169143
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Palmer,C.J., Scott,B.T. and Jones,L.R.
  TITLE     Purification and complete sequence determination of the major
            plasma membrane substrate for cAMP-dependent protein kinase and
            protein kinase C in myocardium
  JOURNAL   J Biol Chem 266 (17), 11126-11130 (1991)
   PUBMED   1710217
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB712570.1 and FM109156.1.
            
            On May 10, 2012 this sequence version replaced NP_113836.1.
            
            Summary: This gene encodes a member of a family of small membrane
            proteins that share a 35-amino acid signature sequence domain,
            beginning with the sequence PFXYD and containing 7 invariant and 6
            highly conserved amino acids. The approved human gene nomenclature
            for the family is FXYD-domain containing ion transport regulator.
            Mouse FXYD5 has been termed RIC (Related to Ion Channel). FXYD2,
            also known as the gamma subunit of the Na,K-ATPase, regulates the
            properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma),
            FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to
            induce channel activity in experimental expression systems.
            Transmembrane topology has been established for two family members
            (FXYD1 and FXYD2), with the N-terminus extracellular and the
            C-terminus on the cytoplasmic side of the membrane. The protein
            encoded by this gene is a plasma membrane substrate for several
            kinases, including protein kinase A, protein kinase C, NIMA kinase,
            and myotonic dystrophy kinase. It is thought to form an ion channel
            or regulate ion channel activity. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211349.1, CK476741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..95
                     /product="phospholemman precursor"
                     /note="phospholemman; sodium/potassium-transporting ATPase
                     subunit FXYD1"
                     /calculated_mol_wt=8367
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          26..89
                     /region_name="FXYD1"
                     /note="FXYD domain-containing ion transport regulator 1;
                     cd20317"
                     /db_xref="CDD:410556"
     Site            order(32,34,36,39..40,43..44,46..47,50,53..55,57..58,60)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410556"
     CDS             1..95
                     /gene="Fxyd1"
                     /gene_synonym="Plm"
                     /coded_by="NM_031648.2:78..365"
                     /db_xref="GeneID:58971"
                     /db_xref="RGD:69306"
ORIGIN      
        1 mgamaspghi livcvcllsm asaeapqepd pftydyhtlr iggltiagil filgiliils
       61 krcrckfnqq qrtgepdeee gtfrssirrl strrr
//
LOCUS       NP_001014843             426 aa            linear   ROD 27-APR-2025
DEFINITION  immunoglobulin mu Fc receptor precursor [Rattus norvegicus].
ACCESSION   NP_001014843
VERSION     NP_001014843.1
DBSOURCE    REFSEQ: accession NM_001014843.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Song,Y. and Jacob,C.O.
  TITLE     The mouse cell surface protein TOSO regulates Fas/Fas
            ligand-induced apoptosis through its binding to Fas-associated
            death domain
  JOURNAL   J Biol Chem 280 (10), 9618-9626 (2005)
   PUBMED   15632112
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC088197.1 and JAXUCZ010000013.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088197.1, SRR26643284.16114.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..426
                     /product="immunoglobulin mu Fc receptor precursor"
                     /note="regulator of Fas-induced apoptosis Toso; Fas
                     apoptotic inhibitory molecule 3; IgM Fc fragment receptor;
                     Fc fragment of IgM receptor; immunoglobulin mu Fc
                     receptor"
                     /calculated_mol_wt=46120
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M871.1)"
                     /calculated_mol_wt=1953
     mat_peptide     17..426
                     /product="Immunoglobulin mu Fc receptor.
                     /id=PRO_0000284423"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M871.1)"
                     /calculated_mol_wt=46120
     Region          18..120
                     /region_name="IgV_pIgR_like"
                     /note="Immunoglobulin (Ig)-like domain in the polymeric Ig
                     receptor (pIgR) and similar proteins; cd05716"
                     /db_xref="CDD:409381"
     Region          18..37
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409381"
     Region          18..20
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409381"
     Region          23..29
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409381"
     Region          31..38
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409381"
     Region          38..44
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409381"
     Region          44..49
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409381"
     Site            44..46
                     /site_type="other"
                     /note="CDR1-dIgA binding residues [polypeptide binding]"
                     /db_xref="CDD:409381"
     Region          45..49
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409381"
     Region          50..69
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409381"
     Region          59..63
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409381"
     Region          67..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409381"
     Region          74..105
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409381"
     Region          74..80
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409381"
     Region          84..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409381"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5M871.1)"
     Region          98..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409381"
     Region          106..114
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409381"
     Region          114..120
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409381"
     Region          114..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409381"
     Region          178..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M871.1)"
     Site            267..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M871.1)"
     Site            268
                     /site_type="other"
                     /note="Receptor capping.
                     /evidence=ECO:0000250|UniProtKB:O60667; propagated from
                     UniProtKB/Swiss-Prot (Q5M871.1)"
     Region          306..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M871.1)"
     Site            386
                     /site_type="other"
                     /note="Receptor-mediated endocytosis.
                     /evidence=ECO:0000250|UniProtKB:O60667; propagated from
                     UniProtKB/Swiss-Prot (Q5M871.1)"
     Region          401..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M871.1)"
     Site            405
                     /site_type="other"
                     /note="Receptor-mediated endocytosis.
                     /evidence=ECO:0000250|UniProtKB:O60667; propagated from
                     UniProtKB/Swiss-Prot (Q5M871.1)"
     CDS             1..426
                     /gene="Fcmr"
                     /gene_synonym="Faim3; FAIM3g; IgM FcR; Toso"
                     /coded_by="NM_001014843.2:96..1376"
                     /db_xref="GeneID:548326"
                     /db_xref="RGD:1359282"
ORIGIN      
        1 mnlwlwllyf lpvsgtlkvl pevrlevelg gsvfiecplp qthvrmylcr qmtnpaicat
       61 vvsnifvkke ykrrvtlkps lnkklflvem tqltkddegi yacgvgtntd lgktqkvtln
      121 vrnefpeype pfwddeptse psprwwlhry peelpwlkmg ehaspsgfid kvttlspkte
      181 appvhqpstn tsvsrhprvy gassetptkp sallpattaf ktsarqasrl leasyshhtr
      241 lhgertphyg sqygredrgl hisipefhil iptflgflll vllglvvkra iqrrrafsrr
      301 vgrmarrmrg rgpsrqiptq rrdapqrprs qnnvysacpr rarepdnvgs aealllnapa
      361 sappalplvi etswphtpsl kmsceyvslg hqpavnvedq dsndyinipg lphlpskppg
      421 prpsrq
//
LOCUS       NP_036647                169 aa            linear   ROD 27-APR-2025
DEFINITION  translocator protein [Rattus norvegicus].
ACCESSION   NP_036647
VERSION     NP_036647.1
DBSOURCE    REFSEQ: accession NM_012515.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Guillemain,G., Khemtemourian,L., Brehat,J., Morin,D., Movassat,J.,
            Tourrel-Cuzin,C. and Lacapere,J.J.
  TITLE     TSPO in pancreatic beta cells and its possible involvement in type
            2 diabetes
  JOURNAL   Biochimie 224, 104-113 (2024)
   PUBMED   38908539
  REMARK    GeneRIF: TSPO in pancreatic beta cells and its possible involvement
            in type 2 diabetes.
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Brehat,J., Leick,S., Musman,J., Su,J.B., Eychenne,N., Giton,F.,
            Rivard,M., Barel,L.A., Tropeano,C., Vitarelli,F., Caccia,C.,
            Leoni,V., Ghaleh,B., Pons,S. and Morin,D.
  TITLE     Identification of a mechanism promoting mitochondrial sterol
            accumulation during myocardial ischemia-reperfusion: role of TSPO
            and STAR
  JOURNAL   Basic Res Cardiol 119 (3), 481-503 (2024)
   PUBMED   38517482
  REMARK    GeneRIF: Identification of a mechanism promoting mitochondrial
            sterol accumulation during myocardial ischemia-reperfusion: role of
            TSPO and STAR.
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Mahemuti,Y., Kadeer,K., Su,R., Abula,A., Aili,Y., Maimaiti,A.,
            Abulaiti,S., Maimaitituerxun,M., Miao,T., Jiang,S., Axier,A.,
            Aisha,M., Wang,Y. and Cheng,X.
  TITLE     TSPO exacerbates acute cerebral ischemia/reperfusion injury by
            inducing autophagy dysfunction
  JOURNAL   Exp Neurol 369, 114542 (2023)
   PUBMED   37717810
  REMARK    GeneRIF: TSPO exacerbates acute cerebral ischemia/reperfusion
            injury by inducing autophagy dysfunction.
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Ceyzeriat,K., Nicolaides,A., Amosse,Q., Fossey,C., Cailly,T.,
            Fabis,F., Garibotto,V., Escartin,C., Tournier,B.B. and Millet,P.
  TITLE     Reactive astrocytes mediate TSPO overexpression in response to
            sustained CNTF exposure in the rat striatum
  JOURNAL   Mol Brain 16 (1), 57 (2023)
   PUBMED   37408083
  REMARK    GeneRIF: Reactive astrocytes mediate TSPO overexpression in
            response to sustained CNTF exposure in the rat striatum.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Gao,N., Ma,B., Jia,H., Hao,C., Jin,T. and Liu,X.
  TITLE     Translocator protein alleviates allodynia and improves Schwann cell
            function against diabetic peripheral neuropathy via activation of
            the Nrf2-dependent antioxidant system and promoting autophagy
  JOURNAL   Diabet Med 40 (6), e15090 (2023)
   PUBMED   37013248
  REMARK    GeneRIF: Translocator protein alleviates allodynia and improves
            Schwann cell function against diabetic peripheral neuropathy via
            activation of the Nrf2-dependent antioxidant system and promoting
            autophagy.
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Lacor,P., Benavides,J. and Ferzaz,B.
  TITLE     Enhanced expression of the peripheral benzodiazepine receptor (PBR)
            and its endogenous ligand octadecaneuropeptide (ODN) in the
            regenerating adult rat sciatic nerve
  JOURNAL   Neurosci Lett 220 (1), 61-65 (1996)
   PUBMED   8977149
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Masonis,A.E. and McCarthy,M.P.
  TITLE     Direct interactions of androgenic/anabolic steroids with the
            peripheral benzodiazepine receptor in rat brain: implications for
            the psychological and physiological manifestations of
            androgenic/anabolic steroid abuse
  JOURNAL   J Steroid Biochem Mol Biol 58 (5-6), 551-555 (1996)
   PUBMED   8918981
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Bar-Ami,S., Amiri,Z., Fares,F. and Gavish,M.
  TITLE     Modulation of peripheral benzodiazepine receptors in female rat
            genital organs by various gonadal steroids
  JOURNAL   Life Sci 54 (25), 1965-1975 (1994)
   PUBMED   8201845
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Casalotti,S.O., Pelaia,G., Yakovlev,A.G., Csikos,T., Grayson,D.R.
            and Krueger,K.E.
  TITLE     Structure of the rat gene encoding the mitochondrial benzodiazepine
            receptor
  JOURNAL   Gene 121 (2), 377-382 (1992)
   PUBMED   1332914
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Sprengel,R., Werner,P., Seeburg,P.H., Mukhin,A.G., Santi,M.R.,
            Grayson,D.R., Guidotti,A. and Krueger,K.E.
  TITLE     Molecular cloning and expression of cDNA encoding a peripheral-type
            benzodiazepine receptor
  JOURNAL   J Biol Chem 264 (34), 20415-20421 (1989)
   PUBMED   2555358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM047408.1, J05122.1 and BQ194961.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ228784.1, AW913934.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..169
                     /product="translocator protein"
                     /note="PBR; PKBS; mitochondrial benzodiazepine receptor;
                     peripheral-type benzodiazepine receptor; Benzodiazepin
                     receptor (peripheral); benzodiazepine receptor,
                     peripheral"
                     /calculated_mol_wt=18809
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16257.1)"
     Region          12..156
                     /region_name="TspO_MBR"
                     /note="TspO/MBR family; pfam03073"
                     /db_xref="CDD:460795"
     Site            order(14..15,17..18,20..21,24,68,80,82..84,86..87,89..91,
                     93..94,97..98,117)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:320706"
     Site            order(23,49..50,52..53,95,143,146..147,150)
                     /site_type="lipid-binding"
                     /note="lipid binding site [chemical binding]"
                     /db_xref="CDD:320706"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16257.1)"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16257.1)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16257.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16257.1)"
     CDS             1..169
                     /gene="Tspo"
                     /gene_synonym="Bzrp; MBR; Ptbzr; PTBZR02; RATPTBZR02"
                     /coded_by="NM_012515.2:92..601"
                     /db_xref="GeneID:24230"
                     /db_xref="RGD:2228"
ORIGIN      
        1 msqswvpavg ltlvpslggf mgayfvrgeg lrwyaslqkp swhpprwtla piwgtlysam
       61 gygsyiiwke lggfteeamv plglytgqla lnwawppiff garqmgwalv dlmlvsgvat
      121 attlawhrvs ppaarllypy lawlafatml nyyvwrdnsg rrggsrlte
//
LOCUS       NP_114461                534 aa            linear   ROD 27-APR-2025
DEFINITION  NEDD8-activating enzyme E1 regulatory subunit [Rattus norvegicus].
ACCESSION   NP_114461
VERSION     NP_114461.3
DBSOURCE    REFSEQ: accession NM_032072.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Joo,Y., Lee,S.H., Ha,S., Hong,B.H., Kim,J.H., Suh,Y.H. and Kim,H.S.
  TITLE     Focal transient ischemia increases APP-BP1 expression in neural
            progenitor cells
  JOURNAL   Neuroreport 22 (5), 200-205 (2011)
   PUBMED   21386696
  REMARK    GeneRIF: The upregulation of APP-BP1 expression in neural
            progenitor cells after focal transient ischemia suggests that this
            protein contributes to the neurogenesis induced by transient
            ischemia and reperfusion
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Joo,Y., Ha,S., Hong,B.H., Kim,Ja., Chang,K.A., Liew,H., Kim,S.,
            Sun,W., Kim,J.H., Chong,Y.H., Suh,Y.H. and Kim,H.S.
  TITLE     Amyloid precursor protein binding protein-1 modulates cell cycle
            progression in fetal neural stem cells
  JOURNAL   PLoS One 5 (12), e14203 (2010)
   PUBMED   21151996
  REMARK    GeneRIF: APP-BP1 plays an important role in the cell cycle
            progression of fetal neural stem cells
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Park,Y., Yoon,S.K. and Yoon,J.B.
  TITLE     TRIP12 functions as an E3 ubiquitin ligase of APP-BP1
  JOURNAL   Biochem Biophys Res Commun 374 (2), 294-298 (2008)
   PUBMED   18627766
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Laifenfeld,D., Patzek,L.J., McPhie,D.L., Chen,Y., Levites,Y.,
            Cataldo,A.M. and Neve,R.L.
  TITLE     Rab5 mediates an amyloid precursor protein signaling pathway that
            leads to apoptosis
  JOURNAL   J Neurosci 27 (27), 7141-7153 (2007)
   PUBMED   17611268
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Chen,Y., Liu,W., McPhie,D.L., Hassinger,L. and Neve,R.L.
  TITLE     APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is
            increased in Alzheimer's disease brain
  JOURNAL   J Cell Biol 163 (1), 27-33 (2003)
   PUBMED   14557245
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Walden,H., Podgorski,M.S. and Schulman,B.A.
  TITLE     Insights into the ubiquitin transfer cascade from the structure of
            the activating enzyme for NEDD8
  JOURNAL   Nature 422 (6929), 330-334 (2003)
   PUBMED   12646924
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Chen,Y., McPhie,D.L., Hirschberg,J. and Neve,R.L.
  TITLE     The amyloid precursor protein-binding protein APP-BP1 drives the
            cell cycle through the S-M checkpoint and causes apoptosis in
            neurons
  JOURNAL   J Biol Chem 275 (12), 8929-8935 (2000)
   PUBMED   10722740
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Gong,L. and Yeh,E.T.
  TITLE     Identification of the activating and conjugating enzymes of the
            NEDD8 conjugation pathway
  JOURNAL   J Biol Chem 274 (17), 12036-12042 (1999)
   PUBMED   10207026
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Osaka,F., Kawasaki,H., Aida,N., Saeki,M., Chiba,T., Kawashima,S.,
            Tanaka,K. and Kato,S.
  TITLE     A new NEDD8-ligating system for cullin-4A
  JOURNAL   Genes Dev 12 (15), 2263-2268 (1998)
   PUBMED   9694792
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Chow,N., Korenberg,J.R., Chen,X.N. and Neve,R.L.
  TITLE     APP-BP1, a novel protein that binds to the carboxyl-terminal region
            of the amyloid precursor protein
  JOURNAL   J Biol Chem 271 (19), 11339-11346 (1996)
   PUBMED   8626687
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC127481.1.
            
            On Sep 25, 2014 this sequence version replaced NP_114461.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127481.1, U90829.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p14"
     Protein         1..534
                     /product="NEDD8-activating enzyme E1 regulatory subunit"
                     /note="amyloid beta precursor protein-binding protein 1,
                     59 kDa; APP-binding protein 1"
                     /calculated_mol_wt=60221
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13564; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1A5.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13564; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1A5.1)"
     Region          11..532
                     /region_name="APPBP1_RUB"
                     /note="Ubiquitin activating enzyme (E1) subunit APPBP1.
                     APPBP1 is part of the heterodimeric activating enzyme
                     (E1), specific for the Rub family of ubiquitin-like
                     proteins (Ubls). E1 enzymes are part of a conjugation
                     cascade to attach Ub or Ubls, covalently to...; cd01493"
                     /db_xref="CDD:238770"
     Site            order(11..12,14..20,22,44,47..48,51,67..68,70..72,74,81,
                     92,95..96,158,495,499,503,525)
                     /site_type="other"
                     /note="dimer interaction [polypeptide binding]"
                     /db_xref="CDD:238770"
     Site            211
                     /site_type="other"
                     /note="Interaction with UBA3. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9Z1A5.1)"
     Region          331..344
                     /region_name="Interaction with UBA3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1A5.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VBW6; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1A5.1)"
     CDS             1..534
                     /gene="Nae1"
                     /gene_synonym="Appbp1; RGD1563180"
                     /coded_by="NM_032072.4:44..1648"
                     /db_xref="GeneID:84019"
                     /db_xref="RGD:619945"
ORIGIN      
        1 maqqgkilke qkydrqlrlw gdhgqeales ahvclinata tgteilknlv lpgigsftii
       61 dgnqvsgedv gnnfflqkcs igknraqaam eflqelnsdv sgsfveespe nlldndpsff
      121 crftivvatq llestllrla dvlwnsqipl licrtyglvg ymriiikehp vieshpdnal
      181 edlrldkpfp elrehfqsyd ldhmekkdhs htpwiviiak ylaqwysetn gripksykek
      241 edfrelirqg ilknengape deenfeeaik nvntalnttq ipssiedifn ddrcinitkq
      301 tpsfwilara lkefvakegq gnlpvrgtip dmiadsskyi klqnvyreka kkdaaavgnh
      361 vakllqsvgq apesisekel kllcsnsafl rvvrcrslae eyglhtvnkd eiissmdnpd
      421 neivlylmlr avdrfhkqhg rypgvsnyqv eedigklksc ltgflqeygl svmvkddyvh
      481 efcrygaaep htvaaflgga aaqevikiit kqfvifnnty iysgmsqtsa tfql
//
LOCUS       NP_001094230             541 aa            linear   ROD 27-APR-2025
DEFINITION  reticulophagy regulator 2 [Rattus norvegicus].
ACCESSION   NP_001094230 XP_001057799 XP_343593
VERSION     NP_001094230.1
DBSOURCE    REFSEQ: accession NM_001100760.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Aug 30, 2012 this sequence version replaced
            XP_343593.4, XP_001057799.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC104673.1, SRR22399481.2555817.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q33"
     Protein         1..541
                     /product="reticulophagy regulator 2"
                     /note="protein FAM134A; family with sequence similarity
                     134, member A"
                     /calculated_mol_wt=57528
     Region          46..244
                     /region_name="RETR2_RHD"
                     /note="N-terminal reticulon-homology domain of
                     Reticulophagy regulator 2; cd22561"
                     /db_xref="CDD:411700"
     Site            75..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            99..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          249..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NC44; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NC44; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NC44; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NC44; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS82; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          331..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS82; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          403..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          459..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          485..490
                     /region_name="LIR motif.
                     /evidence=ECO:0000250|UniProtKB:Q9H6L5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     Region          496..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MHU5.2)"
     CDS             1..541
                     /gene="Retreg2"
                     /gene_synonym="Fam134a; RGD1306844"
                     /coded_by="NM_001100760.1:72..1697"
                     /db_xref="GeneID:363252"
                     /db_xref="RGD:1306844"
ORIGIN      
        1 massgggntg aggtsglglg lglglcmgea tgdaeeeaaa aeavgrlats lwlrlrgwea
       61 vlaaaqrllv wekplhslvt aatlnglfwl lsssslrpff llsislltyf lldlwhprfl
      121 pdvsapppee phsdsegags gaqphllsvp elcrylaesw ltfqihlqel lqykrqnpaq
      181 fcarvcsgca vlavlghyvp gimisyivll sillwplvvy heliqrmytr lepllmqldy
      241 smkaeadalh hkhdkrkrqg knappagdep laetesesea elagfspvvd vkktalalai
      301 tdselsdeea silesggfsv srattpqltd vsedldqqsl psepeealsr elgdgeetel
      361 appedllsap palskqaldt eeegaadket llqlssplhf vnthfngags pqegvkcppg
      421 gpvetlspea vsgdlmapss tlspqlclae sgpvtllsps vlpslpqdsp qaltapeeee
      481 alttedfell dqgeleqlna elglgpempp kppdvlpppp lgpdshslvq sdqeahavve
      541 p
//
LOCUS       NP_058854                490 aa            linear   ROD 27-APR-2025
DEFINITION  cytochrome P450 2C7 [Rattus norvegicus].
ACCESSION   NP_058854 XP_577864
VERSION     NP_058854.1
DBSOURCE    REFSEQ: accession NM_017158.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Sun,D., Jiang,H., Wu,H., Yang,Y., Kaley,G. and Huang,A.
  TITLE     A novel vascular EET synthase: role of CYP2C7
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 301 (6), R1723-R1730 (2011)
   PUBMED   21940400
  REMARK    GeneRIF: CYP2C7 is an endothelial epoxyeicosatrienoic acid (EET)
            synthase in the female rat vasculature, by which, in nitric oxide
            deficiency, shear stress stimulates the release of EETs to initiate
            vasodilation.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Agrawal,A.K. and Shapiro,B.H.
  TITLE     Neonatal phenobarbital imprints overexpression of cytochromes P450
            with associated increase in tumorigenesis and reduced life span
  JOURNAL   FASEB J 19 (3), 470-472 (2005)
   PUBMED   15634872
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Fan,L.Q., Brown-Borg,H., Brown,S., Westin,S., Mode,A. and
            Corton,J.C.
  TITLE     PPARalpha activators down-regulate CYP2C7, a retinoic acid and
            testosterone hydroxylase
  JOURNAL   Toxicology 203 (1-3), 41-48 (2004)
   PUBMED   15363580
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Wu,C.C., MacCoss,M.J., Mardones,G., Finnigan,C., Mogelsvang,S.,
            Yates,J.R. 3rd and Howell,K.E.
  TITLE     Organellar proteomics reveals Golgi arginine dimethylation
  JOURNAL   Mol Biol Cell 15 (6), 2907-2919 (2004)
   PUBMED   15047867
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Oinonen,T., Ronis,M., Wigell,T., Tohmo,K., Badger,T. and
            Lindros,K.O.
  TITLE     Growth hormone-regulated periportal expression of CYP2C7 in rat
            liver
  JOURNAL   Biochem Pharmacol 59 (5), 583-589 (2000)
   PUBMED   10660124
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Henderson,C.J., Russell,A.L., Allan,J.A. and Wolf,C.R.
  TITLE     Sexual differentiation and regulation of cytochrome P-450 CYP2C7
  JOURNAL   Biochim Biophys Acta 1118 (2), 99-106 (1992)
   PUBMED   1370375
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Westin,S., Strom,A., Gustafsson,J.A. and Zaphiropoulos,P.G.
  TITLE     Growth hormone regulation of the cytochrome P-450IIC subfamily in
            the rat: inductive, repressive, and transcriptional effects on
            P-450f (IIC7) and P-450PB1 (IIC6) gene expression
  JOURNAL   Mol Pharmacol 38 (2), 192-197 (1990)
   PUBMED   2385231
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Kimura,H., Yoshioka,H., Sogawa,K., Sakai,Y. and Fujii-Kuriyama,Y.
  TITLE     Complementary DNA cloning of cytochrome P-450s related to
            P-450(M-1) from the complementary DNA library of female rat livers.
            Predicted primary structures for P-450f, PB-1, and PB-1-related
            protein with a bizarre replacement block and their mode of
            transcriptional expression
  JOURNAL   J Biol Chem 263 (2), 701-707 (1988)
   PUBMED   3335521
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Favreau,L.V., Malchoff,D.M., Mole,J.E. and Schenkman,J.B.
  TITLE     Responses to insulin by two forms of rat hepatic microsomal
            cytochrome P-450 that undergo major (RLM6) and minor (RLM5b)
            elevations in diabetes
  JOURNAL   J Biol Chem 262 (29), 14319-14326 (1987)
   PUBMED   3308889
REFERENCE   10 (residues 1 to 490)
  AUTHORS   Gonzalez,F.J., Kimura,S., Song,B.J., Pastewka,J., Gelboin,H.V. and
            Hardwick,J.P.
  TITLE     Sequence of two related P-450 mRNAs transcriptionally increased
            during rat development. An R.dre.1 sequence occupies the complete
            3' untranslated region of a liver mRNA
  JOURNAL   J Biol Chem 261 (23), 10667-10672 (1986)
   PUBMED   3015936
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M18335.1.
            
            On May 4, 2006 this sequence version replaced XP_577864.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: M18335.1, BC127503.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5756307, SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..490
                     /product="cytochrome P450 2C7"
                     /EC_number="1.14.14.1"
                     /note="PTF1; P450F; CYPIIC7; cytochrome P450F; cytochrome
                     P450, 2c39; cytochrome P450 2C7-like"
                     /calculated_mol_wt=56056
     Region          61..485
                     /region_name="CYP2C-like"
                     /note="cytochrome P450 family 2, subfamily C, and similar
                     cytochrome P450s; cd20665"
                     /db_xref="CDD:410758"
     Site            order(97,112..113,120,124,294,297..298,301..302,305,356,
                     361..362,365..366,368,427..429,433,435..437,441,444)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410758"
     Site            order(108,113..114,204..205,208,214,233,237,240,292..293,
                     296..297,300..301,362,366,476..477)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410758"
     Site            144
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000269|PubMed:15047867; propagated from
                     UniProtKB/Swiss-Prot (P05179.2)"
     CDS             1..490
                     /gene="Cyp2c7"
                     /gene_synonym="Cyp2c39"
                     /coded_by="NM_017158.2:22..1494"
                     /db_xref="GeneID:29298"
                     /db_xref="RGD:620379"
ORIGIN      
        1 mdlvtflvlt lsslillslw rqssrrrklp pgptplpiig nflqidvkni sqsltkfskt
       61 ygpvftlylg sqptvilhgy eaikealidn gekfsgrgsy pmnenvtkgf givfsngnrw
      121 kemrrftimn frnlgigkrn iedrvqeeaq clveelrktk gspcdpslil ncapcnvics
      181 itfqnhfdyk dkemltfmek vnenlkimss pwmqvcnsfp slidyfpgth hkiakninym
      241 ksyllkkiee hqesldvtnp rdfvdyylik qkqannieqs eyshenltcs imdligagte
      301 tmsttlryal lllmkyphvt akvqeeidrv igrhrspcmq drkhmpytda mihevqrfin
      361 fvptnlphav tcdikfrnyl ipkgtkvlts ltsvlhdske fpnpemfdpg hfldengnfk
      421 ksdyflpfsa gkracvgegl armqlflflt tilqnfnlks lvhpkdidtm pvlngfaslp
      481 ptyqlcfips
//
LOCUS       NP_036644                119 aa            linear   ROD 27-APR-2025
DEFINITION  beta-2-microglobulin precursor [Rattus norvegicus].
ACCESSION   NP_036644
VERSION     NP_036644.1
DBSOURCE    REFSEQ: accession NM_012512.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Wu,Z., Yan,M., Zhang,M., Wu,N., Ma,G., Wang,B., Fan,Y., Du,X.,
            Ding,C. and Liu,Y.
  TITLE     beta2-microglobulin as a biomarker of pulmonary fibrosis
            development in COPD patients
  JOURNAL   Aging (Albany NY) 13 (1), 1251-1263 (2020)
   PUBMED   33472168
  REMARK    GeneRIF: beta2-microglobulin as a biomarker of pulmonary fibrosis
            development in COPD patients.
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Kohsari,M., Khadem Ansari,M.H. and Rasmi,Y.
  TITLE     Serum level of Xanthine oxidase, Uric Acid, and NADPH oxidase1 in
            Stage I of Multiple Myeloma
  JOURNAL   Asian Pac J Cancer Prev 21 (8), 2237-2242 (2020)
   PUBMED   32856850
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Shimbo,A., Kosaki,Y., Ito,I. and Watanabe,S.
  TITLE     Mice lacking hippocampal left-right asymmetry show non-spatial
            learning deficits
  JOURNAL   Behav Brain Res 336, 156-165 (2018)
   PUBMED   28864206
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Marcinko,T.M., Dong,J., LeBlanc,R., Daborowski,K.V. and Vachet,R.W.
  TITLE     Small molecule-mediated inhibition of beta-2-microglobulin-based
            amyloid fibril formation
  JOURNAL   J Biol Chem 292 (25), 10630-10638 (2017)
   PUBMED   28468825
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Gao,N., Wang,Y., Zheng,C.M., Gao,Y.L., Li,H., Li,Y., Fu,T.T.,
            Xu,L.L., Wang,W., Ying,S. and Huang,K.
  TITLE     beta2-Microglobulin participates in development of lung emphysema
            by inducing lung epithelial cell senescence
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 312 (5), L669-L677 (2017)
   PUBMED   28213472
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Griffin,D.E., Ward,B.J., Juaregui,E., Johnson,R.T. and Vaisberg,A.
  TITLE     Immune activation during measles: beta 2-microglobulin in plasma
            and cerebrospinal fluid in complicated and uncomplicated disease
  JOURNAL   J Infect Dis 166 (5), 1170-1173 (1992)
   PUBMED   1402029
REFERENCE   7  (residues 1 to 119)
  AUTHORS   Attaya,M., Jameson,S., Martinez,C.K., Hermel,E., Aldrich,C.,
            Forman,J., Lindahl,K.F., Bevan,M.J. and Monaco,J.J.
  TITLE     Ham-2 corrects the class I antigen-processing defect in RMA-S cells
  JOURNAL   Nature 355 (6361), 647-649 (1992)
   PUBMED   1538753
REFERENCE   8  (residues 1 to 119)
  AUTHORS   Koller,B.H., Marrack,P., Kappler,J.W. and Smithies,O.
  TITLE     Normal development of mice deficient in beta 2M, MHC class I
            proteins, and CD8+ T cells
  JOURNAL   Science 248 (4960), 1227-1230 (1990)
   PUBMED   2112266
REFERENCE   9  (residues 1 to 119)
  AUTHORS   Cole,T., Dickson,P.W., Esnard,F., Averill,S., Risbridger,G.P.,
            Gauthier,F. and Schreiber,G.
  TITLE     The cDNA structure and expression analysis of the genes for the
            cysteine proteinase inhibitor cystatin C and for beta
            2-microglobulin in rat brain
  JOURNAL   Eur J Biochem 186 (1-2), 35-42 (1989)
   PUBMED   2689174
REFERENCE   10 (residues 1 to 119)
  AUTHORS   Simister,N.E. and Mostov,K.E.
  TITLE     An Fc receptor structurally related to MHC class I antigens
  JOURNAL   Nature 337 (6203), 184-187 (1989)
   PUBMED   2911353
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM032790.1, FM042487.1, FM080788.1 and CB714511.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM032790.1, FQ227468.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..119
                     /product="beta-2-microglobulin precursor"
                     /note="beta-2-microglobulin C-terminal fragment (55 AA)"
                     /calculated_mol_wt=11636
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2102
     mat_peptide     21..119
                     /product="Beta-2-microglobulin. /id=PRO_0000018790"
                     /note="propagated from UniProtKB/Swiss-Prot (P07151.1)"
                     /calculated_mol_wt=11636
     Region          23..116
                     /region_name="IgC1_beta2m"
                     /note="Class I major histocompatibility complex (MHC)
                     beta-2-microglobulin; member of the C1-set of Ig
                     superfamily (IgSF) domains; cd05770"
                     /db_xref="CDD:409427"
     Region          24..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409427"
     Site            order(28,30..32,44,46,48,73..76,80,82..83)
                     /site_type="other"
                     /note="MHC classI alpha interface [polypeptide binding]"
                     /db_xref="CDD:409427"
     Site            order(28,32..34,41,46,53..54,73..77,79..80,83)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:409427"
     Region          41..48
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409427"
     Region          54..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409427"
     Region          63..65
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409427"
     Region          70..77
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409427"
     Region          82..90
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409427"
     Region          97..104
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409427"
     Region          111..115
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409427"
     CDS             1..119
                     /gene="B2m"
                     /coded_by="NM_012512.2:21..380"
                     /db_xref="GeneID:24223"
                     /db_xref="RGD:2189"
ORIGIN      
        1 marsvtvifl vlvslavvla iqktpqiqvy srhppengkp nflncyvsqf hppqieiell
       61 kngkkipnie msdlsfskdw sfyilahtef tptetdvyac rvkhvtlkep ktvtwdrdm
//
LOCUS       NP_001162584             360 aa            linear   ROD 27-APR-2025
DEFINITION  alpha-2-macroglobulin receptor-associated protein precursor [Rattus
            norvegicus].
ACCESSION   NP_001162584 XP_001058156 XP_341240
VERSION     NP_001162584.1
DBSOURCE    REFSEQ: accession NM_001169113.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Zhao,Z., Sagare,A.P., Ma,Q., Halliday,M.R., Kong,P., Kisler,K.,
            Winkler,E.A., Ramanathan,A., Kanekiyo,T., Bu,G., Owens,N.C.,
            Rege,S.V., Si,G., Ahuja,A., Zhu,D., Miller,C.A., Schneider,J.A.,
            Maeda,M., Maeda,T., Sugawara,T., Ichida,J.K. and Zlokovic,B.V.
  TITLE     Central role for PICALM in amyloid-beta blood-brain barrier
            transcytosis and clearance
  JOURNAL   Nat Neurosci 18 (7), 978-987 (2015)
   PUBMED   26005850
  REMARK    Erratum:[Nat Neurosci. 2024 Jan;27(1):208. doi:
            10.1038/s41593-023-01509-y. PMID: 37985802]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Zhang,R.K., Yang,L.K., Huang,L.J., Zhao,Q. and Cai,D.Z.
  TITLE     [Expression of lipoprotein related genes in subchondral bone of
            early experimental osteoarthritis]
  JOURNAL   Zhongguo Gu Shang 27 (1), 54-57 (2014)
   PUBMED   24754147
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Rushworth,J.V., Griffiths,H.H., Watt,N.T. and Hooper,N.M.
  TITLE     Prion protein-mediated toxicity of amyloid-beta oligomers requires
            lipid rafts and the transmembrane LRP1
  JOURNAL   J Biol Chem 288 (13), 8935-8951 (2013)
   PUBMED   23386614
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Bell,R.D., Deane,R., Chow,N., Long,X., Sagare,A., Singh,I.,
            Streb,J.W., Guo,H., Rubio,A., Van Nostrand,W., Miano,J.M. and
            Zlokovic,B.V.
  TITLE     SRF and myocardin regulate LRP-mediated amyloid-beta clearance in
            brain vascular cells
  JOURNAL   Nat Cell Biol 11 (2), 143-153 (2009)
   PUBMED   19098903
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Pandey,P., Pradhan,S. and Mittal,B.
  TITLE     LRP-associated protein gene (LRPAP1) and susceptibility to
            degenerative dementia
  JOURNAL   Genes Brain Behav 7 (8), 943-950 (2008)
   PUBMED   18721259
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Willnow,T.E., Armstrong,S.A., Hammer,R.E. and Herz,J.
  TITLE     Functional expression of low density lipoprotein receptor-related
            protein is controlled by receptor-associated protein in vivo
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4537-4541 (1995)
   PUBMED   7538675
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Abbate,M., Bachinsky,D.R., McCluskey,R.T. and Brown,D.
  TITLE     Expression of gp330 and gp330/alpha 2-macroglobulin
            receptor-associated protein in renal tubular differentiation
  JOURNAL   J Am Soc Nephrol 4 (12), 2003-2015 (1994)
   PUBMED   7522607
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Kanalas,J.J. and Makker,S.P.
  TITLE     Analysis of a 45-kDa protein that binds to the Heymann nephritis
            autoantigen GP330
  JOURNAL   J Biol Chem 268 (11), 8188-8192 (1993)
   PUBMED   7681839
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Herz,J., Goldstein,J.L., Strickland,D.K., Ho,Y.K. and Brown,M.S.
  TITLE     39-kDa protein modulates binding of ligands to low density
            lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
  JOURNAL   J Biol Chem 266 (31), 21232-21238 (1991)
   PUBMED   1718973
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Pietromonaco,S., Kerjaschki,D., Binder,S., Ullrich,R. and
            Farquhar,M.G.
  TITLE     Molecular cloning of a cDNA encoding a major pathogenic domain of
            the Heymann nephritis antigen gp330
  JOURNAL   Proc Natl Acad Sci U S A 87 (5), 1811-1815 (1990)
   PUBMED   2408041
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM055449.1, BC098947.1 and M31051.1.
            
            On or before Dec 16, 2009 this sequence version replaced
            XP_001058156.1, XP_341240.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M31051.1, Z11994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..360
                     /product="alpha-2-macroglobulin receptor-associated
                     protein precursor"
                     /note="alpha-2-macroglobulin receptor-associated protein;
                     RAP; alpha-2-MRAP; gp330-binding 45 kDa protein; low
                     density lipoprotein receptor-related protein-associated
                     protein 1"
                     /calculated_mol_wt=38419
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3631
     Region          31..134
                     /region_name="Alpha-2-MRAP_N"
                     /note="Alpha-2-macroglobulin RAP, N-terminal domain;
                     pfam06400"
                     /db_xref="CDD:461898"
     mat_peptide     34..360
                     /product="Alpha-2-macroglobulin receptor-associated
                     protein. /id=PRO_0000020726"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99068.2)"
                     /calculated_mol_wt=38419
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99068.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55302; propagated from
                     UniProtKB/Swiss-Prot (Q99068.2)"
     Region          149..360
                     /region_name="Alpha-2-MRAP_C"
                     /note="Alpha-2-macroglobulin RAP, C-terminal domain;
                     pfam06401"
                     /db_xref="CDD:461899"
     Region          240..356
                     /region_name="LDL receptor binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99068.2)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99068.2)"
     Region          357..360
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000250|UniProtKB:P30533"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99068.2)"
     CDS             1..360
                     /gene="Lrpap1"
                     /coded_by="NM_001169113.1:34..1116"
                     /db_xref="GeneID:116565"
                     /db_xref="RGD:620700"
ORIGIN      
        1 maplrdrvst lprlqllvll llplllvpqp iaghggkysr eknepemaak resgeefrme
       61 klnqlwekak rlhlspvrla elhsdlkiqe rdelnwkklk vegldgdgek eaklvhnlnv
      121 ilarygldgr kdtqtvhsna lnedtqdelg dprleklwhk aktsgkfsse eldklwrefl
      181 hykekiheyn vlldtlsrae egyenllsps dmthiksdtl askhselkdr lrsinqgldr
      241 lrkvshqgyg patefeeprv idlwdlaqsa nftekelesf reelkhfeak iekhnhyqkq
      301 leishqklkh vesigdpehi srnkekyvll eektkelgyk vkkhlqdlss rvsrarhnel
//
LOCUS       NP_001296226             372 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001296226 XP_008764268
VERSION     NP_001296226.1
DBSOURCE    REFSEQ: accession NM_001309297.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   O'Donnell,B.M., Mackie,T.D., Subramanya,A.R. and Brodsky,J.L.
  TITLE     Endoplasmic reticulum-associated degradation of the renal potassium
            channel, ROMK, leads to type II Bartter syndrome
  JOURNAL   J Biol Chem 292 (31), 12813-12827 (2017)
   PUBMED   28630040
  REMARK    GeneRIF: Data suggest underlying pathology for some patients with
            type II Bartter syndrome is linked to stability of ROMK1 in ERAD
            pathway; using a yeast expression system, cells can be rescued by
            wild-type (rat) ROMK1 but not by ROMK1 containing any one of four
            mutations found in (human) type II Bartter syndrome; mutant ROMKs
            are significantly less stable than wild-type ROMK. (ERAD =
            endoplasmic reticulum-associated degradation)
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Araujo,M., Welch,W.J., Zhou,X., Sullivan,K., Walsh,S., Pasternak,A.
            and Wilcox,C.S.
  TITLE     Inhibition of ROMK blocks macula densa tubuloglomerular feedback
            yet causes renal vasoconstriction in anesthetized rats
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F1120-F1127 (2017)
   PUBMED   28228405
  REMARK    GeneRIF: Blockade of ROMK or Na(+)-K(+)-2Cl(-) transport inhibits
            tubuloglomerular feedback yet increases renal vascular resistance.
            The renal vasoconstriction was independent of volume depletion,
            blood pressure, TGF, or proximal tubule hydrostatic pressure.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Smoot,B., Kober,K.M., Paul,S.M., Levine,J.D., Abrams,G.,
            Mastick,J., Topp,K., Conley,Y.P. and Miaskowski,C.A.
  TITLE     Potassium Channel Candidate Genes Predict the Development of
            Secondary Lymphedema Following Breast Cancer Surgery
  JOURNAL   Nurs Res 66 (2), 85-94 (2017)
   PUBMED   28252570
  REMARK    GeneRIF: These preliminary findings suggest that K channel genes
            play a role in the development of secondary lymphedema
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Bollepalli,M.K., Fowler,P.W., Rapedius,M., Shang,L., Sansom,M.S.,
            Tucker,S.J. and Baukrowitz,T.
  TITLE     State-dependent network connectivity determines gating in a K+
            channel
  JOURNAL   Structure 22 (7), 1037-1046 (2014)
   PUBMED   24980796
  REMARK    GeneRIF: Data indicate that mutations in kir1.1 potassium channel
            preferentially increase pH sensitivity.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Hu,J., Qiu,S., Yang,F., Cao,Z., Li,W. and Wu,Y.
  TITLE     Unique mechanism of the interaction between honey bee toxin TPNQ
            and rKir1.1 potassium channel explored by computational
            simulations: insights into the relative insensitivity of channel
            towards animal toxins
  JOURNAL   PLoS One 8 (7), e67213 (2013)
   PUBMED   23874410
  REMARK    GeneRIF: The TPNQ toxin-rKir1.1 channel complex structure not only
            revealed their unique interaction mechanism, but also elucidate the
            relative insensitivity of rKir1.1 channel towards animal toxins.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Beesley,A.H., Ortega,B. and White,S.J.
  TITLE     Splicing of a retained intron within ROMK K+ channel RNA generates
            a novel set of isoforms in rat kidney
  JOURNAL   Am J Physiol 276 (3), C585-C592 (1999)
   PUBMED   10069985
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Derst,C., Konrad,M., Kockerling,A., Karolyi,L., Deschenes,G.,
            Daut,J., Karschin,A. and Seyberth,H.W.
  TITLE     Mutations in the ROMK gene in antenatal Bartter syndrome are
            associated with impaired K+ channel function
  JOURNAL   Biochem Biophys Res Commun 230 (3), 641-645 (1997)
   PUBMED   9015377
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Boim,M.A., Ho,K., Shuck,M.E., Bienkowski,M.J., Block,J.H.,
            Slightom,J.L., Yang,Y., Brenner,B.M. and Hebert,S.C.
  TITLE     ROMK inwardly rectifying ATP-sensitive K+ channel. II. Cloning and
            distribution of alternative forms
  JOURNAL   Am J Physiol 268 (6 Pt 2), F1132-F1140 (1995)
   PUBMED   7611454
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Zhou,H., Tate,S.S. and Palmer,L.G.
  TITLE     Primary structure and functional properties of an epithelial K
            channel
  JOURNAL   Am J Physiol 266 (3 Pt 1), C809-C824 (1994)
   PUBMED   8166245
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Ho,K., Nichols,C.G., Lederer,W.J., Lytton,J., Vassilev,P.M.,
            Kanazirska,M.V. and Hebert,S.C.
  TITLE     Cloning and expression of an inwardly rectifying ATP-regulated
            potassium channel
  JOURNAL   Nature 362 (6415), 31-38 (1993)
   PUBMED   7680431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jun 9, 2015 this sequence version replaced XP_008764268.1.
            
            Transcript Variant: This variant (2, also known as ROMK2) contains
            an alternate exon in the 5' UTR, lacks a portion of the 5' coding
            region, and initiates translation at a downstream start codon,
            compared to variant 1. It encodes isoform 2 which has a shorter
            N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.19752.1,
                                           SRR22582416.675168.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..372
                     /product="ATP-sensitive inward rectifier potassium channel
                     1 isoform 2"
                     /note="K+ channel protein; ATP-sensitive inward rectifier
                     potassium channel 1; ATP-regulated potassium channel
                     ROM-K; potassium channel, inwardly rectifying subfamily J
                     member 1; inward rectifier K(+) channel Kir1.1"
                     /calculated_mol_wt=42645
     Region          24..166
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Region          173..345
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..372
                     /gene="Kcnj1"
                     /gene_synonym="KAB-1; Kcnj; Kcnj1_v1; Kcnj1_v3; kir1.1;
                     ROMK1; ROMK2; ROMK3"
                     /coded_by="NM_001309297.1:190..1308"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24521"
                     /db_xref="RGD:2957"
ORIGIN      
        1 mfkhlrrwfv thifgrsrqr arlvskegrc niefgnvdaq srfiffvdiw ttvldlkwry
       61 kmtvfitafl gswflfgllw yvvayvhkdl pefyppdnrt pcveningmt saflfsletq
      121 vtigygfrfv teqcataifl lifqsilgvi insfmcgail akisrpkkra ktitfsknav
      181 iskrggklcl lirvanlrks lligshiygk llkttitpeg etiildqtni nfvvdagnen
      241 lffispltiy hiidhnspff hmaaetlsqq dfelvvfldg tvestsatcq vrtsyvpeev
      301 lwgyrfvpiv sktkegkyrv dfhnfgktve vetphcamcl ynekdararm krgydnpnfv
      361 lsevdetddt qm
//
LOCUS       NP_001257892             636 aa            linear   ROD 27-APR-2025
DEFINITION  A-type voltage-gated potassium channel KCND3 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257892
VERSION     NP_001257892.1
DBSOURCE    REFSEQ: accession NM_001270963.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Kanda,H., Ling,J., Chang,Y.T., Erol,F., Viatchenko-Karpinski,V.,
            Yamada,A., Noguchi,K. and Gu,J.G.
  TITLE     Kv4.3 Channel Dysfunction Contributes to Trigeminal Neuropathic
            Pain Manifested with Orofacial Cold Hypersensitivity in Rats
  JOURNAL   J Neurosci 41 (10), 2091-2105 (2021)
   PUBMED   33472822
  REMARK    GeneRIF: Kv4.3 Channel Dysfunction Contributes to Trigeminal
            Neuropathic Pain Manifested with Orofacial Cold Hypersensitivity in
            Rats.
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Tao,B., Liu,Z., Wei,F., Fan,S., Cui,S., Xia,H. and Xu,L.
  TITLE     Over-expression of Kv4.3 gene reverses cardiac remodeling and
            transient-outward K+ current (Ito) reduction via CaMKII inhibition
            in myocardial infarction
  JOURNAL   Biomed Pharmacother 132, 110896 (2020)
   PUBMED   33254430
  REMARK    GeneRIF: Over-expression of Kv4.3 gene reverses cardiac remodeling
            and transient-outward K(+) current (Ito) reduction via CaMKII
            inhibition in myocardial infarction.
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Alday,A., Ahyayauch,H., Fernandez-Lopez,V., Echeazarra,L.,
            Urrutia,J., Casis,O. and Gallego,M.
  TITLE     CaMKII Modulates the Cardiac Transient Outward K+ Current through
            its Association with Kv4 Channels in Non-Caveolar Membrane Rafts
  JOURNAL   Cell Physiol Biochem 54 (1), 27-39 (2020)
   PUBMED   31935048
  REMARK    GeneRIF: Immunogold staining and electron microscopy of heart
            vibrosections was performed to localize Kv4.2/Kv4.3 and
            Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) proteins.
            Patch-Clamp recordings in control conditions and after lipid raft
            or caveolae disruption show that the CaMKII-Kv4 channel complex
            must associate in non-caveolar lipid rafts to be functional.
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Wang,Y., Keskanokwong,T. and Cheng,J.
  TITLE     Kv4.3 expression abrogates and reverses norepinephrine-induced
            myocyte hypertrophy by CaMKII inhibition
  JOURNAL   J Mol Cell Cardiol 126, 77-85 (2019)
   PUBMED   30462989
  REMARK    GeneRIF: Kv4.3 reduction is an important mediator in cardiac
            hypertrophy development via excessive CaMKII activation.
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Viatchenko-Karpinski,V., Ling,J. and Gu,J.G.
  TITLE     Down-regulation of Kv4.3 channels and a-type K+ currents in V2
            trigeminal ganglion neurons of rats following oxaliplatin treatment
  JOURNAL   Mol Pain 14, 1744806917750995 (2018)
   PUBMED   29313436
  REMARK    GeneRIF: down-regulation of Kv4.3 channels mediating A-type K(+)
            (IA) currents currents in nociceptive V2 trigeminal neurons is an
            underlying mechanism of oxaliplatin-induced orofacial neuropathic
            pain.
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Ohya,S., Tanaka,M., Oku,T., Asai,Y., Watanabe,M., Giles,W.R. and
            Imaizumi,Y.
  TITLE     Molecular cloning and tissue distribution of an alternatively
            spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the
            rat
  JOURNAL   FEBS Lett 420 (1), 47-53 (1997)
   PUBMED   9450548
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Takimoto,K., Li,D., Hershman,K.M., Li,P., Jackson,E.K. and
            Levitan,E.S.
  TITLE     Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit
            mRNAs in ventricles of renovascular hypertensive rats
  JOURNAL   Circ Res 81 (4), 533-539 (1997)
   PUBMED   9314834
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Tsaur,M.L., Chou,C.C., Shih,Y.H. and Wang,H.L.
  TITLE     Cloning, expression and CNS distribution of Kv4.3, an A-type K+
            channel alpha subunit
  JOURNAL   FEBS Lett 400 (2), 215-220 (1997)
   PUBMED   9001401
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Dixon,J.E., Shi,W., Wang,H.S., McDonald,C., Yu,H., Wymore,R.S.,
            Cohen,I.S. and McKinnon,D.
  TITLE     Role of the Kv4.3 K+ channel in ventricular muscle. A molecular
            correlate for the transient outward current
  JOURNAL   Circ Res 79 (4), 659-668 (1996)
   PUBMED   8831489
  REMARK    Erratum:[Circ Res 1997 Jan;80(1):147]
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Serodio,P., Vega-Saenz de Miera,E. and Rudy,B.
  TITLE     Cloning of a novel component of A-type K+ channels operating at
            subthreshold potentials with unique expression in heart and brain
  JOURNAL   J Neurophysiol 75 (5), 2174-2179 (1996)
   PUBMED   8734615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Transcript Variant: This variant (2, also known as Kv4.3M and
            Kv4.3a) lacks an in-frame exon in the 3' coding region, compared to
            variant 1. This results in a shorter protein (isoform 2), compared
            to isoform 1.
            
            Sequence Note: The RefSeq transcript was derived from the reference
            genome assembly. The genomic coordinates were determined from
            transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.12809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..636
                     /product="A-type voltage-gated potassium channel KCND3
                     isoform 2"
                     /note="potassium voltage gated channel, Shal-related
                     family, member 3; voltage-gated potassium channel subunit
                     Kv4.3; potassium channel, voltage-gated Shal-related
                     subfamily D, member 3; potassium voltage-gated channel,
                     Shal-related subfamily, member 3; A-type voltage-gated
                     potassium channel KCND3"
                     /calculated_mol_wt=71295
     Region          6..143
                     /region_name="BTB_POZ_KCND3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily D member 3 (KCND3);
                     cd18419"
                     /db_xref="CDD:349726"
     Site            order(7..19,21..22,26..27,29,31,34,36..37,39,54)
                     /site_type="other"
                     /note="beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Site            order(41,45,47..54,57,83,85..87,89,92,96,99..100,102,104,
                     107..110,112..113,116,131..132)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Region          186..412
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          468..544
                     /region_name="DUF3399"
                     /note="Domain of unknown function (DUF3399); pfam11879"
                     /db_xref="CDD:463381"
     CDS             1..636
                     /gene="Kcnd3"
                     /gene_synonym="Kv4.3"
                     /coded_by="NM_001270963.1:93..2003"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65195"
                     /db_xref="RGD:68394"
ORIGIN      
        1 maagvaawlp faraaaigwm pvancpmpla padknkrqde livlnvsgrr fqtwrttler
       61 ypdtllgste kefffnedtk eyffdrdpev frcvlnfyrt gklhypryec isayddelaf
      121 ygilpeiigd ccyeeykdrk renaerlmdd nesennqesm pslsfrqtmw rafenphtst
      181 lalvfyyvtg ffiavsvitn vvetvpcgtv pgskelpcge rysvaffcld tacvmiftve
      241 yllrlfaaps ryrfirsvms iidvvaimpy yiglvmtnne dvsgafvtlr vfrvfrifkf
      301 srhsqglril gytlkscase lgfllfsltm aiiifatvmf yaekgssask ftsipasfwy
      361 tivtmttlgy gdmvpktiag kifgsicsls gvlvialpvp vivsnfsriy hqnqradkrr
      421 aqkkarlari rvaktgssna ylhskrngll nealeltgtp eeehmgktts liesqhhhll
      481 hclekttnhe fideqmfeqn cmessmqnyp strspslssh sgltttccsr rskktthlpn
      541 snlpatrlrs mqelstihiq gseqpsltts rsslnlkadd glrpncktsq ittaiisipt
      601 ppaltpeges rpppaspgpn tnipsitsnv vkvsal
//
LOCUS       NP_036750                101 aa            linear   ROD 27-APR-2025
DEFINITION  protein S100-A4 [Rattus norvegicus].
ACCESSION   NP_036750
VERSION     NP_036750.1
DBSOURCE    REFSEQ: accession NM_012618.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Yang,L., Liu,J., Yin,J., Li,Y., Liu,J., Liu,D., Wang,Z.,
            DiSanto,M.E., Zhang,W. and Zhang,X.
  TITLE     S100A4 modulates cell proliferation, apoptosis and fibrosis in the
            hyperplastic prostate
  JOURNAL   Int J Biochem Cell Biol 169, 106551 (2024)
   PUBMED   38360265
  REMARK    GeneRIF: S100A4 modulates cell proliferation, apoptosis and
            fibrosis in the hyperplastic prostate.
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Xi,P., Zhu,W., Zhang,Y., Wang,M., Liang,H., Wang,H. and Tian,D.
  TITLE     Upregulation of hypothalamic TRPV4 via S100a4/AMPKalpha signaling
            pathway promotes the development of diet-induced obesity
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (1), 166883 (2024)
   PUBMED   37683711
  REMARK    GeneRIF: Upregulation of hypothalamic TRPV4 via S100a4/AMPKalpha
            signaling pathway promotes the development of diet-induced obesity.
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Pankratova,S., Klingelhofer,J., Dmytriyeva,O., Owczarek,S.,
            Renziehausen,A., Syed,N., Porter,A.E., Dexter,D.T. and Kiryushko,D.
  TITLE     The S100A4 Protein Signals through the ErbB4 Receptor to Promote
            Neuronal Survival
  JOURNAL   Theranostics 8 (14), 3977-3990 (2018)
   PUBMED   30083275
  REMARK    GeneRIF: These data suggest that the S100-ErbB axis may be an
            important mechanism regulating neuronal survival and plasticity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Choe,N., Kwon,D.H., Shin,S., Kim,Y.S., Kim,Y.K., Kim,J., Ahn,Y.,
            Eom,G.H. and Kook,H.
  TITLE     The microRNA miR-124 inhibits vascular smooth muscle cell
            proliferation by targeting S100 calcium-binding protein A4 (S100A4)
  JOURNAL   FEBS Lett 591 (7), 1041-1052 (2017)
   PUBMED   28235243
  REMARK    GeneRIF: Data indicate that microRNA miR-124 targets S100
            calcium-binding protein A4 (S100A4) 3' UTR and regulates vascular
            smooth muscle cell proliferation.
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Flynn,A.M., Rudland,P.S. and Barraclough,R.
  TITLE     Protein interactions between S100A4 (p9Ka) and other cellular
            proteins identified using in vitro methods
  JOURNAL   Biochem Soc Trans 24 (3), 341S (1996)
   PUBMED   8878885
REFERENCE   7  (residues 1 to 101)
  AUTHORS   De Vouge,M.W. and Mukherjee,B.B.
  TITLE     Transformation of normal rat kidney cells by v-K-ras enhances
            expression of transin 2 and an S-100-related calcium-binding
            protein
  JOURNAL   Oncogene 7 (1), 109-119 (1992)
   PUBMED   1741158
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Barraclough,R., Gibbs,F., Smith,J.A., Haynes,G.A. and Rudland,P.S.
  TITLE     Calcium-ion binding by the potential calcium-ion-binding protein,
            p9Ka
  JOURNAL   Biochem Biophys Res Commun 169 (2), 660-666 (1990)
   PUBMED   2357224
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Masiakowski,P. and Shooter,E.M.
  TITLE     Nerve growth factor induces the genes for two proteins related to a
            family of calcium-binding proteins in PC12 cells
  JOURNAL   Proc Natl Acad Sci U S A 85 (4), 1277-1281 (1988)
   PUBMED   3422491
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Barraclough,R., Savin,J., Dube,S.K. and Rudland,P.S.
  TITLE     Molecular cloning and sequence of the gene for p9Ka. A cultured
            myoepithelial cell protein with strong homology to S-100, a
            calcium-binding protein
  JOURNAL   J Mol Biol 198 (1), 13-20 (1987)
   PUBMED   3430604
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J03628.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J03628.1, FQ215053.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..101
                     /product="protein S100-A4"
                     /note="P9K; placental calcium-binding protein; nerve
                     growth factor-induced protein 42A; calvasculin;
                     metastasin; Protein 9 Ka homologous to calcium-binding
                     protein"
                     /calculated_mol_wt=11645
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P35466; propagated from
                     UniProtKB/Swiss-Prot (P05942.1)"
     Region          4..90
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(4..20,26..28,37..38,40..42,70..73,75..76,78..81,
                     83..90)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(20,25,28,33..34,63,65,67,69,71,74)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P26447; propagated from
                     UniProtKB/Swiss-Prot (P05942.1)"
     CDS             1..101
                     /gene="S100a4"
                     /gene_synonym="18A2; 42A; CAPL; MTS1; P9ka; PEL98; RNP9KA"
                     /coded_by="NM_012618.2:53..358"
                     /db_xref="GeneID:24615"
                     /db_xref="RGD:3245"
ORIGIN      
        1 marpleeald vivstfhkys gnegdkfkln ktelkelltr elpsflgrrt deaafqklmn
       61 nldsnrdnev dfqeycvfls ciammcneff egcpdkeprk k
//
LOCUS       NP_058719                391 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_058719
VERSION     NP_058719.2
DBSOURCE    REFSEQ: accession NM_017023.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   O'Donnell,B.M., Mackie,T.D., Subramanya,A.R. and Brodsky,J.L.
  TITLE     Endoplasmic reticulum-associated degradation of the renal potassium
            channel, ROMK, leads to type II Bartter syndrome
  JOURNAL   J Biol Chem 292 (31), 12813-12827 (2017)
   PUBMED   28630040
  REMARK    GeneRIF: Data suggest underlying pathology for some patients with
            type II Bartter syndrome is linked to stability of ROMK1 in ERAD
            pathway; using a yeast expression system, cells can be rescued by
            wild-type (rat) ROMK1 but not by ROMK1 containing any one of four
            mutations found in (human) type II Bartter syndrome; mutant ROMKs
            are significantly less stable than wild-type ROMK. (ERAD =
            endoplasmic reticulum-associated degradation)
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Araujo,M., Welch,W.J., Zhou,X., Sullivan,K., Walsh,S., Pasternak,A.
            and Wilcox,C.S.
  TITLE     Inhibition of ROMK blocks macula densa tubuloglomerular feedback
            yet causes renal vasoconstriction in anesthetized rats
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F1120-F1127 (2017)
   PUBMED   28228405
  REMARK    GeneRIF: Blockade of ROMK or Na(+)-K(+)-2Cl(-) transport inhibits
            tubuloglomerular feedback yet increases renal vascular resistance.
            The renal vasoconstriction was independent of volume depletion,
            blood pressure, TGF, or proximal tubule hydrostatic pressure.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Smoot,B., Kober,K.M., Paul,S.M., Levine,J.D., Abrams,G.,
            Mastick,J., Topp,K., Conley,Y.P. and Miaskowski,C.A.
  TITLE     Potassium Channel Candidate Genes Predict the Development of
            Secondary Lymphedema Following Breast Cancer Surgery
  JOURNAL   Nurs Res 66 (2), 85-94 (2017)
   PUBMED   28252570
  REMARK    GeneRIF: These preliminary findings suggest that K channel genes
            play a role in the development of secondary lymphedema
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Bollepalli,M.K., Fowler,P.W., Rapedius,M., Shang,L., Sansom,M.S.,
            Tucker,S.J. and Baukrowitz,T.
  TITLE     State-dependent network connectivity determines gating in a K+
            channel
  JOURNAL   Structure 22 (7), 1037-1046 (2014)
   PUBMED   24980796
  REMARK    GeneRIF: Data indicate that mutations in kir1.1 potassium channel
            preferentially increase pH sensitivity.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hu,J., Qiu,S., Yang,F., Cao,Z., Li,W. and Wu,Y.
  TITLE     Unique mechanism of the interaction between honey bee toxin TPNQ
            and rKir1.1 potassium channel explored by computational
            simulations: insights into the relative insensitivity of channel
            towards animal toxins
  JOURNAL   PLoS One 8 (7), e67213 (2013)
   PUBMED   23874410
  REMARK    GeneRIF: The TPNQ toxin-rKir1.1 channel complex structure not only
            revealed their unique interaction mechanism, but also elucidate the
            relative insensitivity of rKir1.1 channel towards animal toxins.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Beesley,A.H., Ortega,B. and White,S.J.
  TITLE     Splicing of a retained intron within ROMK K+ channel RNA generates
            a novel set of isoforms in rat kidney
  JOURNAL   Am J Physiol 276 (3), C585-C592 (1999)
   PUBMED   10069985
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Derst,C., Konrad,M., Kockerling,A., Karolyi,L., Deschenes,G.,
            Daut,J., Karschin,A. and Seyberth,H.W.
  TITLE     Mutations in the ROMK gene in antenatal Bartter syndrome are
            associated with impaired K+ channel function
  JOURNAL   Biochem Biophys Res Commun 230 (3), 641-645 (1997)
   PUBMED   9015377
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Boim,M.A., Ho,K., Shuck,M.E., Bienkowski,M.J., Block,J.H.,
            Slightom,J.L., Yang,Y., Brenner,B.M. and Hebert,S.C.
  TITLE     ROMK inwardly rectifying ATP-sensitive K+ channel. II. Cloning and
            distribution of alternative forms
  JOURNAL   Am J Physiol 268 (6 Pt 2), F1132-F1140 (1995)
   PUBMED   7611454
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Zhou,H., Tate,S.S. and Palmer,L.G.
  TITLE     Primary structure and functional properties of an epithelial K
            channel
  JOURNAL   Am J Physiol 266 (3 Pt 1), C809-C824 (1994)
   PUBMED   8166245
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Ho,K., Nichols,C.G., Lederer,W.J., Lytton,J., Vassilev,P.M.,
            Kanazirska,M.V. and Hebert,S.C.
  TITLE     Cloning and expression of an inwardly rectifying ATP-regulated
            potassium channel
  JOURNAL   Nature 362 (6415), 31-38 (1993)
   PUBMED   7680431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jun 9, 2015 this sequence version replaced NP_058719.1.
            
            Transcript Variant: This variant (1, also known as ROMK1)
            represents the longest transcript and encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X72341.1, SRR26643287.19760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984041 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..391
                     /product="ATP-sensitive inward rectifier potassium channel
                     1 isoform 1"
                     /note="K+ channel protein; ATP-sensitive inward rectifier
                     potassium channel 1; ATP-regulated potassium channel
                     ROM-K; potassium channel, inwardly rectifying subfamily J
                     member 1; inward rectifier K(+) channel Kir1.1"
                     /calculated_mol_wt=44818
     Region          43..185
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000250|UniProtKB:P48048; propagated from
                     UniProtKB/Swiss-Prot (P35560.1)"
     Site            78..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35560.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35560.1)"
     Region          141..146
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:Q63472"
                     /note="propagated from UniProtKB/Swiss-Prot (P35560.1)"
     Site            156..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35560.1)"
     Site            171
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P35560.1)"
     Region          180..207
                     /region_name="Polyphosphoinositide (PIP2)-binding.
                     /evidence=ECO:0000269|PubMed:9486652"
                     /note="propagated from UniProtKB/Swiss-Prot (P35560.1)"
     Region          192..364
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..391
                     /gene="Kcnj1"
                     /gene_synonym="KAB-1; Kcnj; Kcnj1_v1; Kcnj1_v3; kir1.1;
                     ROMK1; ROMK2; ROMK3"
                     /coded_by="NM_017023.2:150..1325"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24521"
                     /db_xref="RGD:2957"
ORIGIN      
        1 mgasersvfr vliralterm fkhlrrwfvt hifgrsrqra rlvskegrcn iefgnvdaqs
       61 rfiffvdiwt tvldlkwryk mtvfitaflg swflfgllwy vvayvhkdlp efyppdnrtp
      121 cveningmts aflfsletqv tigygfrfvt eqcataifll ifqsilgvii nsfmcgaila
      181 kisrpkkrak titfsknavi skrggklcll irvanlrksl ligshiygkl lkttitpege
      241 tiildqtnin fvvdagnenl ffispltiyh iidhnspffh maaetlsqqd felvvfldgt
      301 vestsatcqv rtsyvpeevl wgyrfvpivs ktkegkyrvd fhnfgktvev etphcamcly
      361 nekdararmk rgydnpnfvl sevdetddtq m
//
LOCUS       NP_001008725             918 aa            linear   ROD 27-APR-2025
DEFINITION  interleukin-6 receptor subunit beta precursor [Rattus norvegicus].
ACCESSION   NP_001008725 XP_215483
VERSION     NP_001008725.2
DBSOURCE    REFSEQ: accession NM_001008725.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Ishibashi,T., Inagaki,T., Okazawa,M., Yamagishi,A., Ohta-Ogo,K.,
            Asano,R., Masaki,T., Kotani,Y., Ding,X., Chikaishi-Kirino,T.,
            Maedera,N., Shirai,M., Hatakeyama,K., Kubota,Y., Kishimoto,T. and
            Nakaoka,Y.
  TITLE     IL-6/gp130 signaling in CD4+ T cells drives the pathogenesis of
            pulmonary hypertension
  JOURNAL   Proc Natl Acad Sci U S A 121 (16), e2315123121 (2024)
   PUBMED   38602915
  REMARK    GeneRIF: IL-6/gp130 signaling in CD4[+] T cells drives the
            pathogenesis of pulmonary hypertension.
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Gao,M., Yin,D., Chen,J. and Qu,X.
  TITLE     Activating the interleukin-6-Gp130-STAT3 pathway ameliorates
            ventricular electrical stability in myocardial infarction rats by
            modulating neurotransmitters in the paraventricular nucleus
  JOURNAL   BMC Cardiovasc Disord 20 (1), 60 (2020)
   PUBMED   32024466
  REMARK    GeneRIF: Activating the interleukin-6-Gp130-STAT3 pathway
            ameliorates ventricular electrical stability in myocardial
            infarction rats by modulating neurotransmitters in the
            paraventricular nucleus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Tamura,Y., Phan,C., Tu,L., Le Hiress,M., Thuillet,R., Jutant,E.M.,
            Fadel,E., Savale,L., Huertas,A., Humbert,M. and Guignabert,C.
  TITLE     Ectopic upregulation of membrane-bound IL6R drives vascular
            remodeling in pulmonary arterial hypertension
  JOURNAL   J Clin Invest 128 (5), 1956-1970 (2018)
   PUBMED   29629897
  REMARK    GeneRIF: Ectopic upregulation of membrane-bound IL6R drives
            vascular remodeling in pulmonary arterial hypertension.
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Thompson,L.C., Holland,N.A., Snyder,R.J., Luo,B., Becak,D.P.,
            Odom,J.T., Harrison,B.S., Brown,J.M., Gowdy,K.M. and Wingard,C.J.
  TITLE     Pulmonary instillation of MWCNT increases lung permeability,
            decreases gp130 expression in the lungs, and initiates
            cardiovascular IL-6 transsignaling
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 310 (2), L142-L154 (2016)
   PUBMED   26589480
  REMARK    GeneRIF: pulmonary exposure to MWCNT can manifest as a reduced
            epithelial barrier and activator of vascular gp130-associated
            transsignaling that may promote susceptibility to cardiovascular
            derangements
REFERENCE   5  (residues 1 to 918)
  AUTHORS   Bradesi,S., Karagiannides,I., Bakirtzi,K., Joshi,S.M., Koukos,G.,
            Iliopoulos,D., Pothoulakis,C. and Mayer,E.A.
  TITLE     Identification of Spinal Cord MicroRNA and Gene Signatures in a
            Model of Chronic Stress-Induced Visceral Hyperalgesia in Rat
  JOURNAL   PLoS One 10 (7), e0130938 (2015)
   PUBMED   26222740
  REMARK    GeneRIF: findings suggest a link between miR-17-5p increased
            expression and gp130/STAT3 activation providing new insight into
            the possible mechanisms mediating the effect of chronic stress on
            neuroinflammation
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 918)
  AUTHORS   Hilton,D.J., Hilton,A.A., Raicevic,A., Rakar,S., Harrison-Smith,M.,
            Gough,N.M., Begley,C.G., Metcalf,D., Nicola,N.A. and Willson,T.A.
  TITLE     Cloning of a murine IL-11 receptor alpha-chain; requirement for
            gp130 for high affinity binding and signal transduction
  JOURNAL   EMBO J 13 (20), 4765-4775 (1994)
   PUBMED   7957045
REFERENCE   7  (residues 1 to 918)
  AUTHORS   Narazaki,M., Yasukawa,K., Saito,T., Ohsugi,Y., Fukui,H.,
            Koishihara,Y., Yancopoulos,G.D., Taga,T. and Kishimoto,T.
  TITLE     Soluble forms of the interleukin-6 signal-transducing receptor
            component gp130 in human serum possessing a potential to inhibit
            signals through membrane-anchored gp130
  JOURNAL   Blood 82 (4), 1120-1126 (1993)
   PUBMED   8353278
REFERENCE   8  (residues 1 to 918)
  AUTHORS   Stahl,N., Davis,S., Wong,V., Taga,T., Kishimoto,T., Ip,N.Y. and
            Yancopoulos,G.D.
  TITLE     Cross-linking identifies leukemia inhibitory factor-binding protein
            as a ciliary neurotrophic factor receptor component
  JOURNAL   J Biol Chem 268 (11), 7628-7631 (1993)
   PUBMED   8385113
REFERENCE   9  (residues 1 to 918)
  AUTHORS   Wang,Y., Nesbitt,J.E., Fuentes,N.L. and Fuller,G.M.
  TITLE     Molecular cloning and characterization of the rat liver IL-6 signal
            transducing molecule, gp130
  JOURNAL   Genomics 14 (3), 666-672 (1992)
   PUBMED   1427893
REFERENCE   10 (residues 1 to 918)
  AUTHORS   Hibi,M., Murakami,M., Saito,M., Hirano,T., Taga,T. and Kishimoto,T.
  TITLE     Molecular cloning and expression of an IL-6 signal transducer,
            gp130
  JOURNAL   Cell 63 (6), 1149-1157 (1990)
   PUBMED   2261637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 8, 2010 this sequence version replaced NP_001008725.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data to make the sequence consistent with the reference genome
            assembly. The genomic coordinates used for the transcript record
            were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M92340.1, JQ013730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..918
                     /product="interleukin-6 receptor subunit beta precursor"
                     /note="membrane glycoprotein 130; oncostatin-M receptor
                     subunit alpha; IL-6R subunit beta; IL-6 receptor subunit
                     beta; interleukin 6 signal transducer"
                     /calculated_mol_wt=100106
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2508
     mat_peptide     23..918
                     /product="Interleukin-6 receptor subunit beta.
                     /id=PRO_0000010901"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
                     /calculated_mol_wt=100106
     Region          26..112
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          125..214
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          <197..434
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          221..320
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(221,290,305)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          309..313
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Site            order(309..310,312..313)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            477
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          518..598
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            order(518,583,598)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            619..640
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Region          650..658
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Region          659..679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40189; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40189; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          720..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Region          773..795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40189; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00560; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Region          817..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40190.1)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40189; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     Site            838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P40190.1)"
     CDS             1..918
                     /gene="Il6st"
                     /gene_synonym="Ac1055; Gp130; Il-6rb"
                     /coded_by="NM_001008725.3:17..2773"
                     /db_xref="GeneID:25205"
                     /db_xref="RGD:2903"
ORIGIN      
        1 msalriwlmq alliflttes igqlvepcgy iypefpvvqr gsnftatcvl kekclqvysv
       61 natyivwktn hvavpkeqvt vinrtassvt ftdvvfqnvq ltcnilsfgq ieqnvygiti
      121 lsgyppdipt nlscivnegk nmlcqwdpgr etyletnytl ksewatekfp dcrtkhgtss
      181 cmmgytpiyf vnievwveae nalgnvssep infdpvdkvk pspphnlsvt nseelssilk
      241 lawvnsglds ilrlksdiqy rtkdastwiq vpledtvspr tsftvqdlkp fteyvfrirs
      301 ikengkgyws dwseeasgtt yedrpskaps fwykvnanhp qeyrsarliw ktlplseang
      361 kildyevvlt qsksvsqtyt vngtelivnl tnnryvasla arnvvgkspa tvltipgshf
      421 kashpvvdlk afpkdnllwv ewtppskpvn kyilewcvls enspcipdwq qedgtvnrth
      481 lrgslleskc ylitvtpvfp ggpgspesmk aylkqaapsk gptvrtkkvg kneavlewdh
      541 lpvdvqngfi rnysisyrts vgkemvvrvd sshteytlss lssdtlymvh maayteeggk
      601 dgpeftfttl kfaqgeieai vvpvclafll ttllgvlfcf nkrdlikkhi wpnvpdpsks
      661 hiaqwsphtp prhnfnskdq mysdanftdv svveieannk kpcpddlksl dlfkkekist
      721 eghssgiggs scmsssrpsi ssseenesaq stastvqyst vvhsgyrhqv psvqvfsrse
      781 stqplldsee rpedlqlvds vdsgdeilpr qqyfkqscsq pgaspdvshf erssqvpsgs
      841 eedfvrlkqq qvsdhisepy gseqrrlfqe gsvadalgtg tdgqierfes vgmetamded
      901 isksylpqtv rqggympq
//
LOCUS       NP_001257498             410 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform 7 [Rattus norvegicus].
ACCESSION   NP_001257498
VERSION     NP_001257498.1
DBSOURCE    REFSEQ: accession NM_001270569.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, AY009371.1,
            CB735595.1 and BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (7) is alternatively spliced at
            the 3' end compared to variant 1, and encodes a shorter isoform (7,
            also known as H3(410)) containing 7 transmembrane domains, but
            missing part of the third intracellular loop compared to isoform
            H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680412,
                              SAMN06680424 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..410
                     /product="histamine H3 receptor isoform 7"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=45526
     Region          48..388
                     /region_name="7tmA_Histamine_H3R"
                     /note="histamine receptor subtypes H3R and H3R-like,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15296"
                     /db_xref="CDD:320423"
     Region          69..96
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320423"
     Region          107..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320423"
     Site            order(110,114..115,118..119,190,199,202..203,206,336,
                     339..340,343,359,363,367)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320423"
     Region          152..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320423"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320423"
     Region          316..346
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320423"
     Region          356..381
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320423"
     CDS             1..410
                     /gene="Hrh3"
                     /coded_by="NM_001270569.1:338..1570"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhsssrgte rprslkrgsk psassaslek
      301 rmkmvsqsit qrfrlsrdkk vakslaiivs ifglcwapyt llmiiraach grcipdywye
      361 tsfwllwans avnpvlyplc hysfrraftk llcpqklkvq phgsleqcwk
//
LOCUS       NP_853660                304 aa            linear   ROD 27-APR-2025
DEFINITION  small glutamine-rich tetratricopeptide repeat-containing protein
            beta [Rattus norvegicus].
ACCESSION   NP_853660
VERSION     NP_853660.1
DBSOURCE    REFSEQ: accession NM_181629.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Cao,M., Xu,W., Yu,J., Zheng,H., Tan,X., Li,L., Rui,Y., Xu,G.,
            Cui,G., Xu,J., Cao,J., Tao,T., Ke,K. and Wu,Q.
  TITLE     Up-regulation of SGTB is associated with neuronal apoptosis after
            neuroinflammation induced by lipopolysaccharide
  JOURNAL   J Mol Histol 44 (5), 507-518 (2013)
   PUBMED   23820636
  REMARK    GeneRIF: Up-regulation of SGTB is associated with neuronal
            apoptosis in the rat neuroinflammation model.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Tobaben,S., Varoqueaux,F., Brose,N., Stahl,B. and Meyer,G.
  TITLE     A brain-specific isoform of small glutamine-rich tetratricopeptide
            repeat-containing protein binds to Hsc70 and the cysteine string
            protein
  JOURNAL   J Biol Chem 278 (40), 38376-38383 (2003)
   PUBMED   12878599
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF368280.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF368280.1, FQ212215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132264, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..304
                     /product="small glutamine-rich tetratricopeptide
                     repeat-containing protein beta"
                     /note="beta-SGT; small glutamine-rich tetratricopeptide
                     repeat (TPR)-containing, beta; small glutamine rich
                     tetratricopeptide repeat containing beta; small
                     glutamine-rich protein with tetratricopeptide repeats 2"
                     /calculated_mol_wt=33357
     Region          5..64
                     /region_name="SGTA_dimer"
                     /note="Homodimerization domain of SGTA; pfam16546"
                     /db_xref="CDD:465168"
     Region          15..49
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W98.1)"
     Region          85..118
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W98.1)"
     Region          85..113
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(86,89..90,93..94,96,120,123..124,127..128,130..131,
                     154,157..158,161..162,165)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..>200
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          118..148
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          120..152
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W98.1)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q80W98.1)"
     Region          153..186
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W98.1)"
     Region          153..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q80W98.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ0; propagated from
                     UniProtKB/Swiss-Prot (Q80W98.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ0; propagated from
                     UniProtKB/Swiss-Prot (Q80W98.1)"
     CDS             1..304
                     /gene="Sgtb"
                     /gene_synonym="Sgt2"
                     /coded_by="NM_181629.3:102..1016"
                     /db_xref="GeneID:294708"
                     /db_xref="RGD:727976"
ORIGIN      
        1 mssvkplvya virflreqsq mdaytsdeqe slevaiqcle tvfkispedt hlavsqplte
       61 mftnsvcknd irplsnsvpe dvgkadqlkd egnnhmkeen yaaavdcytq aieldpnnav
      121 yycnraaaqs klshytdaik dcekaiaids kyskaygrmg laltamnkfe eavtsyqkal
      181 dldpendsyk snlkiaeqkl revssptgtg ltfdmaslin npafitmaas lmqnpqvqql
      241 msgmmtnaig gpaagvgglt dlssliqagq qfaqqiqqqn pelieqlrnh irsrsfssst
      301 eehs
//
LOCUS       NP_113812                340 aa            linear   ROD 27-APR-2025
DEFINITION  immunoglobulin-binding protein 1 [Rattus norvegicus].
ACCESSION   NP_113812 XP_346877
VERSION     NP_113812.1
DBSOURCE    REFSEQ: accession NM_031624.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Cowan,J., Longman,M.R. and Snabaitis,A.K.
  TITLE     Regulation of cardiomyocyte DNA damage and cell death by the type
            2A protein phosphatase regulatory protein alpha4
  JOURNAL   Sci Rep 11 (1), 6293 (2021)
   PUBMED   33737606
  REMARK    GeneRIF: Regulation of cardiomyocyte DNA damage and cell death by
            the type 2A protein phosphatase regulatory protein alpha4.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Eleftheriadou,O., Boguslavskyi,A., Longman,M.R., Cowan,J.,
            Francois,A., Heads,R.J., Wadzinski,B.E., Ryan,A., Shattock,M.J. and
            Snabaitis,A.K.
  TITLE     Expression and regulation of type 2A protein phosphatases and
            alpha4 signalling in cardiac health and hypertrophy
  JOURNAL   Basic Res Cardiol 112 (4), 37 (2017)
   PUBMED   28526910
  REMARK    GeneRIF: Report the significance and altered activity of the type
            2A protein phosphatase-alpha4 complex in healthy and hypertrophied
            myocardium.
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Aranda-Orgilles,B., Aigner,J., Kunath,M., Lurz,R., Schneider,R. and
            Schweiger,S.
  TITLE     Active transport of the ubiquitin ligase MID1 along the
            microtubules is regulated by protein phosphatase 2A
  JOURNAL   PLoS One 3 (10), e3507 (2008)
   PUBMED   18949047
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Prickett,T.D. and Brautigan,D.L.
  TITLE     Cytokine activation of p38 mitogen-activated protein kinase and
            apoptosis is opposed by alpha-4 targeting of protein phosphatase 2A
            for site-specific dephosphorylation of MEK3
  JOURNAL   Mol Cell Biol 27 (12), 4217-4227 (2007)
   PUBMED   17438131
REFERENCE   5  (residues 1 to 340)
  AUTHORS   O'Malley,P.G., Sangster,S.M., Abdelmagid,S.A., Bearne,S.L. and
            Too,C.K.
  TITLE     Characterization of a novel, cytokine-inducible carboxypeptidase D
            isoform in haematopoietic tumour cells
  JOURNAL   Biochem J 390 (Pt 3), 665-673 (2005)
   PUBMED   15918796
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Kong,M., Fox,C.J., Mu,J., Solt,L., Xu,A., Cinalli,R.M.,
            Birnbaum,M.J., Lindsten,T. and Thompson,C.B.
  TITLE     The PP2A-associated protein alpha4 is an essential inhibitor of
            apoptosis
  JOURNAL   Science 306 (5696), 695-698 (2004)
   PUBMED   15499020
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Short,K.M., Hopwood,B., Yi,Z. and Cox,T.C.
  TITLE     MID1 and MID2 homo- and heterodimerise to tether the
            rapamycin-sensitive PP2A regulatory subunit, alpha 4, to
            microtubules: implications for the clinical variability of X-linked
            Opitz GBBB syndrome and other developmental disorders
  JOURNAL   BMC Cell Biol 3, 1 (2002)
   PUBMED   11806752
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Nanahoshi,M., Nishiuma,T., Tsujishita,Y., Hara,K., Inui,S.,
            Sakaguchi,N. and Yonezawa,K.
  TITLE     Regulation of protein phosphatase 2A catalytic activity by alpha4
            protein and its yeast homolog Tap42
  JOURNAL   Biochem Biophys Res Commun 251 (2), 520-526 (1998)
   PUBMED   9792806
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Too,C.K.
  TITLE     Differential expression of elongation factor-2, alpha4
            phosphoprotein and Cdc5-like protein in
            prolactin-dependent/independent rat lymphoid cells
  JOURNAL   Mol Cell Endocrinol 131 (2), 221-232 (1997)
   PUBMED   9296381
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC068202.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346877.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068202.1, FQ222671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..340
                     /product="immunoglobulin-binding protein 1"
                     /note="alpha4 phosphoprotein; CD79a-binding protein 1;
                     protein phosphatase 2/4/6 regulatory subunit;
                     immunoglobulin (CD79A) binding protein 1"
                     /calculated_mol_wt=39004
     Region          17..330
                     /region_name="TAP42"
                     /note="TAP42-like family; pfam04177"
                     /db_xref="CDD:461209"
     Region          99..203
                     /region_name="Interaction with PPP2CA.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08836.2)"
     Region          221..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08836.2)"
     Region          226..291
                     /region_name="Interaction with MID1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O08836.2)"
     Site            242
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P78318; propagated from
                     UniProtKB/Swiss-Prot (O08836.2)"
     Site            256..257
                     /site_type="cleavage"
                     /note="Cleavage, by calpain. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O08836.2)"
     Region          281..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08836.2)"
     CDS             1..340
                     /gene="Igbp1"
                     /coded_by="NM_031624.3:13..1035"
                     /db_xref="GeneID:58845"
                     /db_xref="RGD:62011"
ORIGIN      
        1 maaseeelll prlpelfets kklleeleva teptgsrtiq dkvskglell ekaagmlsql
       61 dlfsrnedle eiasidlkyl mvpalqgalt mkqvnpskrl dhlqrarehf ihfltqchcy
      121 hvaefqlpqt knnsaennta rssmaypnlv amasqrqaki erykqkkeve hrlsalksav
      181 esgqadderv reyyllhlrr wigisleeie sidqeikilk dkdspreesa cqsslpekpp
      241 mkpfiltrnk aqakvfgtgy pslatmtvsd wyeqhqkyga lpdrgiakpp sadfqraaqq
      301 qedqeqkdee neekalhrmr ewddwkdthp rgygnrqnmg
//
LOCUS       NP_001104330             357 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 3 [Rattus norvegicus].
ACCESSION   NP_001104330
VERSION     NP_001104330.1
DBSOURCE    REFSEQ: accession NM_001110860.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078899.1 and JAXUCZ010000017.1.
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.72287.1,
                                           SRR26360172.2781698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..357
                     /product="cAMP-responsive element modulator isoform 3"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=38450
     Region          112..151
                     /region_name="pKID"
                     /note="pKID domain; pfam02173"
                     /db_xref="CDD:396650"
     Region          301..355
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          302..354
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(302,306,308..310,312..314,316..317,319..321)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(320,323,327..328,330..331,334..335,337..338,341,
                     344..345,348..349,351..352)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..357
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001110860.2:360..1433"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mskcgrkkym rtnvrqmtme tvesqqdrsv thsvaehssa hmqtgqisvp tlaqvsvags
       61 gtgrgspavt lvqlpsgqtv qvqgviqtph psviqspqiq tvqvatiaet ddsadsevid
      121 shkrreilsr rpsyrkilne lssdvpgipk ieeekseeeg tppniatmav ptsiyqtstg
      181 qyiaiaqggt iqisnpgsdg vqglqaltmt nsgapppgat ivqyaaqsad gtqqffvpgs
      241 qvvvqdeetd lapshmaaat gdmptyqira pttalpqgvv maaspgslhs pqqlaeeatr
      301 krelrlmknr eaarecrrkk keyvkclenr vavlenqnkt lieelkalkd lychkae
//
LOCUS       NP_001276911             225 aa            linear   ROD 27-APR-2025
DEFINITION  D site-binding protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001276911
VERSION     NP_001276911.1
DBSOURCE    REFSEQ: accession NM_001289982.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Jiang,H., Li,J., He,X., Xue,J., Liang,S., Liu,S., Gao,F., Qu,N.,
            Liu,H. and Chen,L.
  TITLE     D-site binding protein regulates cell proliferation through
            mediating cell cycle progression in rat mesangial cells
  JOURNAL   Tissue Cell 61, 35-43 (2019)
   PUBMED   31759405
  REMARK    GeneRIF: DBP effectively inhibits the proliferation of mesangial
            cells through G1 phase arrest.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Harbour,V.L., Weigl,Y., Robinson,B. and Amir,S.
  TITLE     Phase differences in expression of circadian clock genes in the
            central nucleus of the amygdala, dentate gyrus, and suprachiasmatic
            nucleus in the rat
  JOURNAL   PLoS One 9 (7), e103309 (2014)
   PUBMED   25068868
  REMARK    GeneRIF: Data show that the expression of clock genes Per2, Bmal1
            and Dbp follow a diurnal rhythm in the central nucleus of the
            amygdala, dentate gyrus, and suprachiasmatic nucleu but the phase
            and amplitude of the rhythms of each gene vary across the 3
            regions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Huang,X.M., Chen,W.L., Yuan,J.P., Yang,Y.H., Mei,Q.H. and
            Huang,L.X.
  TITLE     Altered diurnal variation and localization of clock proteins in the
            remnant kidney of 5/6 nephrectomy rats
  JOURNAL   Nephrology (Carlton) 18 (8), 555-562 (2013)
   PUBMED   23738784
  REMARK    GeneRIF: The localization and diurnal variation of BMAL1, DBP and
            PER2 are changed in remnant kidney of 5/6 nephrectomy rats and are
            involved in diurnal rhythm of renal function.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Yamajuku,D., Shibata,Y., Kitazawa,M., Katakura,T., Urata,H.,
            Kojima,T., Takayasu,S., Nakata,O. and Hashimoto,S.
  TITLE     Cellular DBP and E4BP4 proteins are critical for determining the
            period length of the circadian oscillator
  JOURNAL   FEBS Lett 585 (14), 2217-2222 (2011)
   PUBMED   21635892
  REMARK    GeneRIF: Data show that knockdown of DBP, D-box positive regulator,
            led to a short-period phenotype, and overexpression of DBP produced
            a long-period rhythm, while knockdown and overexpression of E4BP4,
            D-box negative regulator, had the opposite effect of DBP.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Xu,Z., Kaga,S., Tsubomizu,J., Fujisaki,J., Mochiduki,A., Sakai,T.,
            Tsukamura,H., Maeda,K., Inoue,K. and Adachi,A.A.
  TITLE     Circadian transcriptional factor DBP regulates expression of Kiss1
            in the anteroventral periventricular nucleus
  JOURNAL   Mol Cell Endocrinol 339 (1-2), 90-97 (2011)
   PUBMED   21458520
  REMARK    GeneRIF: Dbp and estrogen regulate the expression of Kiss1 in the
            anteroventral periventricular nucleus
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Brown,S.A., Zumbrunn,G., Fleury-Olela,F., Preitner,N. and
            Schibler,U.
  TITLE     Rhythms of mammalian body temperature can sustain peripheral
            circadian clocks
  JOURNAL   Curr Biol 12 (18), 1574-1583 (2002)
   PUBMED   12372249
  REMARK    GeneRIF: natural body temperature rhythms can affect circadian gene
            expression
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Szpirer,C., Van Vooren,P., Riviere,M., Scohy,S., Collau,G. and
            Szpirer,J.
  TITLE     Localization of 54 rat genes, and definition of new synteny groups
            conserved in the human and the rat
  JOURNAL   Mamm Genome 11 (9), 729-735 (2000)
   PUBMED   10967130
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Brown,S.A. and Schibler,U.
  TITLE     The ins and outs of circadian timekeeping
  JOURNAL   Curr Opin Genet Dev 9 (5), 588-594 (1999)
   PUBMED   10508692
  REMARK    Review article
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Mueller,C.R., Maire,P. and Schibler,U.
  TITLE     DBP, a liver-enriched transcriptional activator, is expressed late
            in ontogeny and its tissue specificity is determined
            posttranscriptionally
  JOURNAL   Cell 61 (2), 279-291 (1990)
   PUBMED   2331750
  REMARK    Erratum:[Cell. 1991 May 31;65(5):915. PMID: 2040017]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Summary: The protein encoded by this gene is a member of the Par
            bZIP transcription factor family and binds to specific sequences in
            the promoters of several genes, such as albumin, Cyp2a4, and
            Cyp2a5. The encoded protein can bind DNA as a homo- or heterodimer
            and is involved in the regulation of some circadian rhythym genes.
            Three transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction at the 3' end of an exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY518348.1, SRR26360186.1061199.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..225
                     /product="D site-binding protein isoform 2"
                     /note="d site-binding protein; albumin D box-binding
                     protein; albumin D-element-binding protein; d site albumin
                     promoter-binding protein 1; D site albumin promoter
                     binding protein; D site of albumin promoter (albumin
                     D-box) binding protein"
                     /calculated_mol_wt=24474
     Region          154..213
                     /region_name="bZIP_HLF"
                     /note="Basic leucine zipper (bZIP) domain of Hepatic
                     leukemia factor (HLF) and similar proteins: a DNA-binding
                     and dimerization domain; cd14695"
                     /db_xref="CDD:269843"
     Region          155..213
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269843"
     Site            order(161..162,164..166,168..173,175..177)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269843"
     Site            order(176,179..180,183..184,186..187,190..191,193..194,
                     197..198,200..201,204..205,207..208)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269843"
     CDS             1..225
                     /gene="Dbp"
                     /coded_by="NM_001289982.1:402..1079"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24309"
                     /db_xref="RGD:2491"
ORIGIN      
        1 marplsdrtp gplllggpag appgggallg lrsllqgnsk pkepascllk ekerkatlps
       61 apvpgpvlet agpadaptga vsggltsrdt pspvdpdtve vlmtfepdpa dlalssipgh
      121 etfdprrhrf seeelkpqpi mkkarkvqvp eeqkdekyws rryknneaak rsrdarrlke
      181 nqisvraafl ekenallrqe vvavrqelsh yravlsryqa qhgtl
//
LOCUS       NP_001258030             357 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 4 [Rattus norvegicus].
ACCESSION   NP_001258030
VERSION     NP_001258030.1
DBSOURCE    REFSEQ: accession NM_001271101.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC078899.1 and JAXUCZ010000017.1.
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 3' coding region, compared to variant 3. This results in
            protein (isoform 4) that is the same length but has a distinct
            C-terminus, compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078899.1, SRR26643293.72289.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..357
                     /product="cAMP-responsive element modulator isoform 4"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=38366
     Region          112..151
                     /region_name="pKID"
                     /note="pKID domain; pfam02173"
                     /db_xref="CDD:396650"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27699; propagated from
                     UniProtKB/Swiss-Prot (Q03061.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03060; propagated from
                     UniProtKB/Swiss-Prot (Q03061.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03060,
                     ECO:0000255|PROSITE-ProRule:PRU00312; propagated from
                     UniProtKB/Swiss-Prot (Q03061.2)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03060,
                     ECO:0000255|PROSITE-ProRule:PRU00312; propagated from
                     UniProtKB/Swiss-Prot (Q03061.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03060,
                     ECO:0000255|PROSITE-ProRule:PRU00312; propagated from
                     UniProtKB/Swiss-Prot (Q03061.2)"
     Region          300..325
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03061.2)"
     Region          301..355
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          302..354
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(302,306,308..310,312..314,316..317,319..321)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(320,323,327..328,330..331,334..335,337..338,341,
                     344..345,348..349,351..352)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     Region          327..348
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03061.2)"
     CDS             1..357
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271101.1:360..1433"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mskcgrkkym rtnvrqmtme tvesqqdrsv thsvaehssa hmqtgqisvp tlaqvsvags
       61 gtgrgspavt lvqlpsgqtv qvqgviqtph psviqspqiq tvqvatiaet ddsadsevid
      121 shkrreilsr rpsyrkilne lssdvpgipk ieeekseeeg tppniatmav ptsiyqtstg
      181 qyiaiaqggt iqisnpgsdg vqglqaltmt nsgapppgat ivqyaaqsad gtqqffvpgs
      241 qvvvqdeetd lapshmaaat gdmptyqira pttalpqgvv maaspgslhs pqqlaeeatr
      301 krelrlmknr eaakecrrrk keyvkclesr vavlevqnkk lieeletlkd icspktd
//
LOCUS       NP_113838                687 aa            linear   ROD 27-APR-2025
DEFINITION  solute carrier organic anion transporter family member 1B2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_113838
VERSION     NP_113838.1
DBSOURCE    REFSEQ: accession NM_031650.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Chen,S., Li,K., Jiang,J., Wang,X., Chai,Y., Zhang,C., Deng,Q.,
            Shuai,L., Feng,K., Ma,K. and Zhang,L.
  TITLE     Low expression of organic anion-transporting polypeptide 1B3
            predicts a poor prognosis in hepatocellular carcinoma
  JOURNAL   World J Surg Oncol 18 (1), 127 (2020)
   PUBMED   32534581
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Ma,X., Shang,X., Qin,X., Lu,J., Liu,M. and Wang,X.
  TITLE     Characterization of organic anion transporting polypeptide 1b2
            knockout rats generated by CRISPR/Cas9: a novel model for drug
            transport and hyperbilirubinemia disease
  JOURNAL   Acta Pharm Sin B 10 (5), 850-860 (2020)
   PUBMED   32528832
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Alam,K., Farasyn,T., Ding,K. and Yue,W.
  TITLE     Characterization of Liver- and Cancer-type-Organic Anion
            Transporting Polypeptide (OATP) 1B3 Messenger RNA Expression in
            Normal and Cancerous Human Tissues
  JOURNAL   Drug Metab Lett 12 (1), 24-32 (2018)
   PUBMED   29577869
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Verboom,M.C., Kloth,J.S.L., Swen,J.J., van der Straaten,T.,
            Bovee,J.V.M.G., Sleijfer,S., Reyners,A.K.L., Mathijssen,R.H.J.,
            Guchelaar,H.J., Steeghs,N. and Gelderblom,H.
  TITLE     Genetic polymorphisms in angiogenesis-related genes are associated
            with worse progression-free survival of patients with advanced
            gastrointestinal stromal tumours treated with imatinib
  JOURNAL   Eur J Cancer 86, 226-232 (2017)
   PUBMED   29054076
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Sun,B., Chen,Y., Xiang,T., Zhang,L., Chen,Z., Zhang,S., Zhou,H. and
            Chen,S.
  TITLE     The Chinese Herb Jianpijiedu Contributes to the Regulation of
            OATP1B2 and ABCC2 in a Rat Model of Orthotopic Transplantation
            Liver Cancer Pretreated with Food Restriction and Diarrhea
  JOURNAL   Biomed Res Int 2015, 752850 (2015)
   PUBMED   26665149
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Cattori,V., van Montfoort,J.E., Stieger,B., Landmann,L.,
            Meijer,D.K., Winterhalter,K.H., Meier,P.J. and Hagenbuch,B.
  TITLE     Localization of organic anion transporting polypeptide 4 (Oatp4) in
            rat liver and comparison of its substrate specificity with Oatp1,
            Oatp2 and Oatp3
  JOURNAL   Pflugers Arch 443 (2), 188-195 (2001)
   PUBMED   11713643
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Ismair,M.G., Stieger,B., Cattori,V., Hagenbuch,B., Fried,M.,
            Meier,P.J. and Kullak-Ublick,G.A.
  TITLE     Hepatic uptake of cholecystokinin octapeptide by organic
            anion-transporting polypeptides OATP4 and OATP8 of rat and human
            liver
  JOURNAL   Gastroenterology 121 (5), 1185-1190 (2001)
   PUBMED   11677211
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Choudhuri,S., Ogura,K. and Klaassen,C.D.
  TITLE     Cloning of the full-length coding sequence of rat liver-specific
            organic anion transporter-1 (rlst-1) and a splice variant and
            partial characterization of the rat lst-1 gene
  JOURNAL   Biochem Biophys Res Commun 274 (1), 79-86 (2000)
   PUBMED   10903899
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Cattori,V., Hagenbuch,B., Hagenbuch,N., Stieger,B., Ha,R.,
            Winterhalter,K.E. and Meier,P.J.
  TITLE     Identification of organic anion transporting polypeptide 4 (Oatp4)
            as a major full-length isoform of the liver-specific transporter-1
            (rlst-1) in rat liver
  JOURNAL   FEBS Lett 474 (2-3), 242-245 (2000)
   PUBMED   10838093
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Kakyo,M., Unno,M., Tokui,T., Nakagomi,R., Nishio,T., Iwasashi,H.,
            Nakai,D., Seki,M., Suzuki,M., Naitoh,T., Matsuno,S., Yawo,H. and
            Abe,T.
  TITLE     Molecular characterization and functional regulation of a novel rat
            liver-specific organic anion transporter rlst-1
  JOURNAL   Gastroenterology 117 (4), 770-775 (1999)
   PUBMED   10500057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF208545.2 and JAXUCZ010000004.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ271682.1, AF208545.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..687
                     /product="solute carrier organic anion transporter family
                     member 1B2 isoform 1"
                     /note="solute carrier family 21 member 10;
                     sodium-independent organic anion-transporting polypeptide
                     4; solute carrier organic anion transporter family, member
                     1b3; solute carrier family 21 (organic anion transporter)
                     member 10; solute carrier family (organic anion
                     transporter) member 10; organic anion transporting
                     polypeptide 4; liver-specific transporter-1;
                     liver-specific organic anion transporter 1"
                     /calculated_mol_wt=76636
     Region          28..555
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            29..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            order(41..42,45..46,49,81,182..183,185..187,190,210,
                     213..214,217,342,345..346,349..351,354,383,387,428..429,
                     433,437,500,503..504,507)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            95..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            166..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            253..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Region          286..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJL3; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            329..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            371..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            399..422
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            511
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            532..554
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            564..589
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            624..641
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QZX8.2)"
     CDS             1..687
                     /gene="Slco1b2"
                     /gene_synonym="OATP-4; Oatp4; rlst-1; Slc21a10; Slco1b3"
                     /coded_by="NM_031650.3:115..2178"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:58978"
                     /db_xref="RGD:69300"
ORIGIN      
        1 mdhtqqsrka aeaqpsrskq trfcdgfklf laalsfsyic kalggvvmks sitqierrfd
       61 ipssisglid ggfeignllv ivfvsyfgsk lhrpkligig cfimgigsil talphffmgy
      121 ykyakendig slgnstltcf inqmtsptgp speivekgce kglkshmwiy vlmgnmlrgi
      181 getpivplgi sylddfakeg htsmhlgtlh tiamigpilg fimssvfaki yvdvgyvdln
      241 svritpndar wvgawwlsfi vngllcitss ipffflpkip krsqeerkns vslhapktde
      301 ekkhmtnltk qeeqdpsnmt gflrslrsil tneiyvifli ltllqvsgfi gsftylfkfi
      361 eqqfgrtasq anfllgiiti ptmatamflg gyivkkfklt svgiakfvff tssvayafqf
      421 lyfpllcenk pfagltltyd gmnpvdshid vplsycnsdc scdknqwepi cgengvtyis
      481 pclagcksfr gdkkpnntef ydcscisnsg nnsahlgecp rykcktnyyf yiilqvtvsf
      541 ftamgspsli lilmksvqpe lkslamgfhs liiralggil apiyygafid rtcikwsvts
      601 cgkrgacrly nsrlfgfsyl glnlalktpp lflyvvliyf tkrkykrndn ktlengrqft
      661 degnpdsvnk ngyycvpyde qsnetpl
//
LOCUS       NP_001104293            1043 aa            linear   ROD 27-APR-2025
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase 2 isoform b
            [Rattus norvegicus].
ACCESSION   NP_001104293 XP_001079470
VERSION     NP_001104293.1
DBSOURCE    REFSEQ: accession NM_001110823.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Chen,W., Li,M., Lei,X., Cheng,Y., Wu,X., Sun,X., Wu,Y., Li,Z.,
            Luo,G. and Wei,M.
  TITLE     Remote ischemic postconditioning alleviates cerebral ischemic
            injury through SERCA2/endoplasmic reticulum stress-mediated
            apoptosis
  JOURNAL   Microsc Res Tech 87 (3), 424-433 (2024)
   PUBMED   37897375
  REMARK    GeneRIF: Remote ischemic postconditioning alleviates cerebral
            ischemic injury through SERCA2/endoplasmic reticulum
            stress-mediated apoptosis.
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Gomez-Viquez,N.L., Balderas-Villalobos,J., Bello-Sanchez,M.D.,
            Mayorga-Luna,M., Mailloux-Salinas,P., Garcia-Castaneda,M.,
            Rios-Perez,E.B., Martinez-Avila,M.A., Camacho-Castillo,L.D.C.,
            Bravo,G., Avila,G., Altamirano,J. and Carvajal,K.
  TITLE     Oxidative stress in early metabolic syndrome impairs cardiac RyR2
            and SERCA2a activity and modifies the interplay of these proteins
            during Ca2+ waves
  JOURNAL   Arch Physiol Biochem 129 (5), 1058-1070 (2023)
   PUBMED   33689540
  REMARK    GeneRIF: Oxidative stress in early metabolic syndrome impairs
            cardiac RyR2 and SERCA2a activity and modifies the interplay of
            these proteins during Ca[2+] waves.
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Hu,T. and Liu,L.
  TITLE     Effects of MiR-214-3p Regulation of SERCA2a Expression on
            Contractility of Cardiomyocytes in Heart Failure Model
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 68 (4), 208-216 (2022)
   PUBMED   35988281
  REMARK    GeneRIF: Effects of MiR-214-3p Regulation of SERCA2a Expression on
            Contractility of Cardiomyocytes in Heart Failure Model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Chen,J., Liu,Y., Pan,D., Xu,T., Luo,Y., Wu,W., Wu,P., Zhu,H. and
            Li,D.
  TITLE     Estrogen inhibits endoplasmic reticulum stress and ameliorates
            myocardial ischemia/reperfusion injury in rats by upregulating
            SERCA2a
  JOURNAL   Cell Commun Signal 20 (1), 38 (2022)
   PUBMED   35331264
  REMARK    GeneRIF: Estrogen inhibits endoplasmic reticulum stress and
            ameliorates myocardial ischemia/reperfusion injury in rats by
            upregulating SERCA2a.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Celestino-Montes,A., Perez-Trevino,P., Sandoval-Herrera,M.D.,
            Gomez-Viquez,N.L. and Altamirano,J.
  TITLE     Relative role of T-tubules disruption and decreased SERCA2 on
            contractile dynamics of isolated rat ventricular myocytes
  JOURNAL   Life Sci 264, 118700 (2021)
   PUBMED   33130073
  REMARK    GeneRIF: Relative role of T-tubules disruption and decreased SERCA2
            on contractile dynamics of isolated rat ventricular myocytes.
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Harrer,J.M., Haghighi,K., Kim,H.W., Ferguson,D.G. and Kranias,E.G.
  TITLE     Coordinate regulation of SR Ca(2+)-ATPase and phospholamban
            expression in developing murine heart
  JOURNAL   Am J Physiol 272 (1 Pt 2), H57-H66 (1997)
   PUBMED   9038922
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   Wu,K.D. and Lytton,J.
  TITLE     Molecular cloning and quantification of sarcoplasmic reticulum
            Ca(2+)-ATPase isoforms in rat muscles
  JOURNAL   Am J Physiol 264 (2 Pt 1), C333-C341 (1993)
   PUBMED   8447366
  REMARK    Erratum:[Am J Physiol 1994 Jul;267(1 Pt 1):section C followi]
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Lompre,A.M., de la Bastie,D., Boheler,K.R. and Schwartz,K.
  TITLE     Characterization and expression of the rat heart sarcoplasmic
            reticulum Ca2+-ATPase mRNA
  JOURNAL   FEBS Lett 249 (1), 35-41 (1989)
   PUBMED   2542094
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   Komuro,I., Kurabayashi,M., Shibazaki,Y., Takaku,F. and Yazaki,Y.
  TITLE     Molecular cloning and characterization of a Ca2+ + Mg2+-dependent
            adenosine triphosphatase from rat cardiac sarcoplasmic reticulum.
            Regulation of its expression by pressure overload and developmental
            stage
  JOURNAL   J Clin Invest 83 (4), 1102-1108 (1989)
   PUBMED   2522936
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Gunteski-Hamblin,A.M., Greeb,J. and Shull,G.E.
  TITLE     A novel Ca2+ pump expressed in brain, kidney, and stomach is
            encoded by an alternative transcript of the slow-twitch muscle
            sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs
            encoding Ca2+ and other cation-transporting ATPases using an
            oligonucleotide probe derived from the ATP-binding site
  JOURNAL   J Biol Chem 263 (29), 15032-15040 (1988)
   PUBMED   2844797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            J04022.1, BE119640.1, J04024.1, CK356454.1, CK358684.1 and
            AA900747.1.
            
            Transcript Variant: This variant (3) encodes the longer isoform
            (b), also known as SERCA2B.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J04024.1, J04022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..1043
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase 2 isoform b"
                     /EC_number="7.2.2.10"
                     /note="ATPase, Ca++ transporting, slow twitch 2;
                     sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
                     calcium pump 2; SR Ca(2+)-ATPase 2; endoplasmic reticulum
                     class 1/2 Ca(2+) ATPase; sarco(endo)plasmic reticulum
                     Ca(2+)-dependent ATPase 2; ATPase, Ca++ transporting,
                     cardiac muscle, slow twitch 2"
                     /calculated_mol_wt=114637
     Region          5..988
                     /region_name="P-type_ATPase_SERCA"
                     /note="sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA),
                     similar to mammalian ATP2A1-3/SERCA1-3; cd02083"
                     /db_xref="CDD:319778"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            254..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            296..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            order(309,795,799)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Site            order(351..353,442,487,489,492,494,514..516,559,561,
                     624..626,677,683,702,705)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:319778"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64578; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55143; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Region          575..594
                     /region_name="Interaction with HAX1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16615; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P11507.1)"
     Site            757..776
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            order(767,770,798..799,907)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319778"
     Region          787..807
                     /region_name="Interaction with PLN.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            787..807
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Region          788..1043
                     /region_name="Interaction with TMEM64 and PDIA3.
                     /evidence=ECO:0000250|UniProtKB:O55143"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            828..850
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            897..916
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            930..948
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Region          931..942
                     /region_name="Interaction with PLN.
                     /evidence=ECO:0000250|UniProtKB:P04191"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     Site            964..984
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11507.1)"
     CDS             1..1043
                     /gene="Atp2a2"
                     /gene_synonym="Serca2; SercaII"
                     /coded_by="NM_001110823.2:507..3638"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:29693"
                     /db_xref="RGD:2174"
ORIGIN      
        1 menahtktve evlghfgvne stglsleqvk klkerwgsne lpaeegktll elvieqfedl
       61 lvrilllaac isfvlawfee geetitafve pfvillilva naivgvwqer naenaiealk
      121 eyepemgkvy rqdrksvqri kakdivpgdi veiavgdkvp adirltsiks ttlrvdqsil
      181 tgesvsvikh tdpvpdprav nqdkknmlfs gtniaagkam gvvvatgvnt eigkirdemv
      241 ateqertplq qkldefgeql skvislicia vwiinighfn dpvhggswir gaiyyfkiav
      301 alavaaipeg lpavittcla lgtrrmakkn aivrslpsve tlgctsvics dktgtlttnq
      361 msvcrmfild kvegdtcsln eftitgstya pigevqkddk pvkchqydgl velaticalc
      421 ndsaldynea kgvyekvgea tetaltclve kmnvfdtelk glskierana cnsvikqlmk
      481 keftlefsrd rksmsvyctp nkpsrtsmsk mfvkgapegv idrcthirvg stkvpmtpgv
      541 kqkimsvire wgsgsdtlrc lalathdnpl rreemhleds anfikyetnl tfvgcvgmld
      601 pprievassv klcrqagirv imitgdnkgt avaicrrigi fgqdedvtsk aftgrefdel
      661 spsaqrdacl narcfarvep shkskivefl qsfdeitamt gdgvndapal kkseigiamg
      721 sgtavaktas emvladdnfs tivaaveegr aiynnmkqfi rylissnvge vvcifltaal
      781 gfpealipvq llwvnlvtdg lpatalgfnp pdldimnkpp rnpkeplisg wlffrylaig
      841 cyvgaatvga aawwfiaadg gprvsfyqls hflqckednp dfegvdcaif espypmtmal
      901 svlvtiemcn alnslsenqs llrmppweni wlvgsiclsm slhflilyve plplifqitp
      961 lnltqwlmvl kislpvilmd etlkfvarny lepgkecaqp atkpscslsa ctdgiswpfv
     1021 llimplvvwv ystdtnfsdm fws
//
LOCUS       NP_059060                407 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 260 [Rattus norvegicus].
ACCESSION   NP_059060
VERSION     NP_059060.1
DBSOURCE    REFSEQ: accession NM_017364.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Debrus,S., Rahbani,L., Marttila,M., Delorme,B., Paradis,P. and
            Nemer,M.
  TITLE     The zinc finger-only protein Zfp260 is a novel cardiac regulator
            and a nuclear effector of alpha1-adrenergic signaling
  JOURNAL   Mol Cell Biol 25 (19), 8669-8682 (2005)
   PUBMED   16166646
  REMARK    GeneRIF: Zfp260 is a novel transcriptional regulator in normal and
            pathological heart development and a nuclear effector of
            alpha1-adrenergic signaling
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Ferbus,D., Bovin,C., Validire,P. and Goubin,G.
  TITLE     The zinc finger protein OZF (ZNF146) is overexpressed in colorectal
            cancer
  JOURNAL   J Pathol 200 (2), 177-182 (2003)
   PUBMED   12754738
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ206124.1, FQ189505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..407
                     /product="zinc finger protein 260"
                     /note="pancreas-only zinc finger protein 1; zinc finger
                     protein 146"
                     /calculated_mol_wt=46453
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62981.1)"
     Region          21..401
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          25..45
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          53..73
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          81..101
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          161..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(194,196,198,200..201,204..205,208,222,224,228..229,
                     232..233,236,250,252,254,256..257,260..261,264)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(334,336,338,340..341,344..345,348,362,364,368..369,
                     372..373,376,390,392,394,396..397,400..401,404)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..407
                     /gene="Zfp260"
                     /gene_synonym="OZF; POZF-1; Znf146; Znf260"
                     /coded_by="NM_017364.4:511..1734"
                     /db_xref="GeneID:53982"
                     /db_xref="RGD:621205"
ORIGIN      
        1 mleslqpese llhdepdpge kvyecdecrk tfsleqhfve hkkthggeks pectgcgeef
       61 skassltrhl rsrsrresyk cgncgrtfsq rgnflshqkq haeerpsesk ktpvpmttiv
      121 rnqrnagnkp yackecgkaf ngksylkehe kihtgekpfe cnqcgrafsq kqylikhqnv
      181 hsgkkpfkcn ecgkafsqke nliihqriht gekpyeckgc gkafiqkssl irhqrshtge
      241 kpytckecgk afsgksnlte hekihigekp ykcnecgtif rqkqylikhh nihtgekpye
      301 cnkcgkafsr itslivhvri htgdkpyeck vcgkafcqss sltvhmrsht gekpygcnec
      361 gkafsqfstl alhmrihtge kpyqcsecgk afsqkshhir hqrihih
//
LOCUS       NP_001258045              65 aa            linear   ROD 27-APR-2025
DEFINITION  sarcoplasmic/endoplasmic reticulum calcium ATPase regulator ARLN
            [Rattus norvegicus].
ACCESSION   NP_001258045 XP_001079712 XP_002726083 XP_003753706
VERSION     NP_001258045.1
DBSOURCE    REFSEQ: accession NM_001271116.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Anderson,D.M., Makarewich,C.A., Anderson,K.M., Shelton,J.M.,
            Bezprozvannaya,S., Bassel-Duby,R. and Olson,E.N.
  TITLE     Widespread control of calcium signaling by a family of
            SERCA-inhibiting micropeptides
  JOURNAL   Sci Signal 9 (457), ra119 (2016)
   PUBMED   27923914
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100074.1.
            
            On or before Sep 3, 2012 this sequence version replaced
            XP_002726083.1, XP_003753706.1, XP_001079712.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100074.1, FQ213976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..65
                     /product="sarcoplasmic/endoplasmic reticulum calcium
                     ATPase regulator ARLN"
                     /note="uncharacterized protein C4orf3 homolog;
                     another-regulin; SERCA regulator ALN;
                     sarcoplasmic/endoplasmic reticulum calcium ATPase
                     regulator ALN; SERCA regulator ARLN"
                     /calculated_mol_wt=7239
     Region          1..65
                     /region_name="DUF5542"
                     /note="Family of unknown function (DUF5542); pfam17696"
                     /db_xref="CDD:465462"
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498U0.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q8WVX3; propagated from
                     UniProtKB/Swiss-Prot (Q498U0.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99M08; propagated from
                     UniProtKB/Swiss-Prot (Q498U0.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q498U0.1)"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498U0.1)"
     CDS             1..65
                     /gene="Arln"
                     /gene_synonym="ALN; C2h4orf3"
                     /coded_by="NM_001271116.1:116..313"
                     /db_xref="GeneID:691807"
                     /db_xref="RGD:1594660"
ORIGIN      
        1 mevgqaasgt dgvrerrgss aarrrsqdep vqsgmngipk hsywldlwlf ilfdlalfif
       61 vyllp
//
LOCUS       NP_387502                526 aa            linear   ROD 27-APR-2025
DEFINITION  amine oxidase [flavin-containing] A [Rattus norvegicus].
ACCESSION   NP_387502 XP_001058993 XP_343765
VERSION     NP_387502.1
DBSOURCE    REFSEQ: accession NM_033653.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Merce,A.P., Ionica,L.N., Bina,A.M., Popescu,S., Lighezan,R.,
            Petrescu,L., Borza,C., Sturza,A., Muntean,D.M. and Cretu,O.M.
  TITLE     Monoamine oxidase is a source of cardiac oxidative stress in obese
            rats: the beneficial role of metformin
  JOURNAL   Mol Cell Biochem 478 (1), 59-67 (2023)
   PUBMED   35723772
  REMARK    GeneRIF: Monoamine oxidase is a source of cardiac oxidative stress
            in obese rats: the beneficial role of metformin.
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Tseilikman,V., Lapshin,M., Klebanov,I., Chrousos,G., Vasilieva,M.,
            Pashkov,A., Fedotova,J., Tseilikman,D., Shatilov,V., Manukhina,E.,
            Tseilikman,O., Sarapultsev,A. and Downey,H.F.
  TITLE     The Link between Activities of Hepatic 11beta-Hydroxysteroid
            Dehydrogenase-1 and Monoamine Oxidase-A in the Brain Following
            Repeated Predator Stress: Focus on Heightened Anxiety
  JOURNAL   Int J Mol Sci 23 (9), 4881 (2022)
   PUBMED   35563271
  REMARK    GeneRIF: The Link between Activities of Hepatic
            11beta-Hydroxysteroid Dehydrogenase-1 and Monoamine Oxidase-A in
            the Brain Following Repeated Predator Stress: Focus on Heightened
            Anxiety.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Cho,H.U., Kim,S., Sim,J., Yang,S., An,H., Nam,M.H., Jang,D.P. and
            Lee,C.J.
  TITLE     Redefining differential roles of MAO-A in dopamine degradation and
            MAO-B in tonic GABA synthesis
  JOURNAL   Exp Mol Med 53 (7), 1148-1158 (2021)
   PUBMED   34244591
  REMARK    GeneRIF: Redefining differential roles of MAO-A in dopamine
            degradation and MAO-B in tonic GABA synthesis.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Sun,X.Q., Peters,E.L., Schalij,I., Axelsen,J.B., Andersen,S.,
            Kurakula,K., Gomez-Puerto,M.C., Szulcek,R., Pan,X., da Silva
            Goncalves Bos,D., Schiepers,R.E.J., Andersen,A., Goumans,M.J., Vonk
            Noordegraaf,A., van der Laarse,W.J., de Man,F.S. and Bogaard,H.J.
  TITLE     Increased MAO-A Activity Promotes Progression of Pulmonary Arterial
            Hypertension
  JOURNAL   Am J Respir Cell Mol Biol 64 (3), 331-343 (2021)
   PUBMED   33264068
  REMARK    GeneRIF: Increased MAO-A Activity Promotes Progression of Pulmonary
            Arterial Hypertension.
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Sturza,A., Vaduva,A., Utu,D., Ratiu,C., Pop,N., Duicu,O.,
            Popoiu,C., Boia,E., Matusz,P., Muntean,D.M. and Olariu,S.
  TITLE     Vitamin D improves vascular function and decreases monoamine
            oxidase A expression in experimental diabetes
  JOURNAL   Mol Cell Biochem 453 (1-2), 33-40 (2019)
   PUBMED   30167938
  REMARK    GeneRIF: MAO-A is induced in diabetic aortas and vitamin D can
            improve diabetes-induced endothelial dysfunction by modulating the
            MAO-A expression.
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Heron,P., Cousins,K., Boyd,C. and Daya,S.
  TITLE     Paradoxical effects of copper and manganese on brain mitochondrial
            function
  JOURNAL   Life Sci 68 (14), 1575-1583 (2001)
   PUBMED   11263670
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Jones,S.R., Gainetdinov,R.R., Jaber,M., Giros,B., Wightman,R.M. and
            Caron,M.G.
  TITLE     Profound neuronal plasticity in response to inactivation of the
            dopamine transporter
  JOURNAL   Proc Natl Acad Sci U S A 95 (7), 4029-4034 (1998)
   PUBMED   9520487
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Tsugeno,Y. and Ito,A.
  TITLE     A key amino acid responsible for substrate selectivity of monoamine
            oxidase A and B
  JOURNAL   J Biol Chem 272 (22), 14033-14036 (1997)
   PUBMED   9162023
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Sherif,F., Gottfries,C.G., Alafuzoff,I. and Oreland,L.
  TITLE     Brain gamma-aminobutyrate aminotransferase (GABA-T) and monoamine
            oxidase (MAO) in patients with Alzheimer's disease
  JOURNAL   J Neural Transm Park Dis Dement Sect 4 (3), 227-240 (1992)
   PUBMED   1627256
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Kuwahara,T., Takamoto,S. and Ito,A.
  TITLE     Primary structure of rat monoamine oxidase A deduced from cDNA and
            its expression in rat tissues
  JOURNAL   Agric Biol Chem 54 (1), 253-257 (1990)
   PUBMED   1368522
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM101032.1, FM044630.1, FM037037.1, FM117485.1, FM132632.1,
            FM031063.1 and FM098276.1.
            
            On or before Dec 6, 2009 this sequence version replaced
            XP_343765.1, XP_001058993.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166508.1, SRR8487231.148175.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..526
                     /product="amine oxidase [flavin-containing] A"
                     /EC_number="1.4.3.4"
                     /EC_number="1.4.3.21"
                     /note="MAO-A; monoamine oxidase type A"
                     /calculated_mol_wt=59390
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P21397; propagated from
                     UniProtKB/Swiss-Prot (P21396.1)"
     Region          11..464
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
     Site            335
                     /site_type="other"
                     /note="Important for substrate specificity; propagated
                     from UniProtKB/Swiss-Prot (P21396.1)"
     Site            374
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P21396.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P21396.1)"
     Site            498..518
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21396.1)"
     Region          520..522
                     /region_name="Interaction with membrane phospholipid
                     headgroups. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P21396.1)"
     CDS             1..526
                     /gene="Maoa"
                     /gene_synonym="Mao"
                     /coded_by="NM_033653.1:1..1581"
                     /db_xref="GeneID:29253"
                     /db_xref="RGD:61898"
ORIGIN      
        1 mtdlekpnla ghmfdvvvig ggisglaaak llseykinvl vleardrvgg rtytvrnehv
       61 kwvdvggayv gptqnrilrl skelgietyk vnvnerlvqy vkgktypfrg afppvwnpla
      121 yldynnlwrt mdemgkeipv dapwqarhaq ewdkmtmkdl idkicwtkta refaylfvni
      181 nvtsephevs alwflwyvrq cggtarifsv tnggqerkfv ggsgqvseqi mgllgdkvkl
      241 sspvtyidqt ddniivetln hehyeckyvi saippiltak ihfkpelppe rnqliqrlpm
      301 gavikcmvyy keafwkkkdy cgcmiiedee apiaitlddt kpdgslpaim gfilarkadr
      361 laklhkdirk rkicelyakv lgsqealypv hyeeknwcee qysggcytay fppgimtqyg
      421 rvirqpvgri yfagtetatq wsgymegave ageraarevl nalgkvakkd iwveepeskd
      481 vpaieithtf lernlpsvpg llkitgvsts vallcfvlyk ikklpc
//
LOCUS       NP_001257610             312 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein E precursor [Rattus norvegicus].
ACCESSION   NP_001257610
VERSION     NP_001257610.1
DBSOURCE    REFSEQ: accession NM_001270681.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lee,B.H., Cevizci,M., Lieblich,S.E., Ibrahim,M., Wen,Y., Eid,R.S.,
            Lamers,Y., Duarte-Guterman,P. and Galea,L.A.M.
  TITLE     Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age
  JOURNAL   Brain Behav Immun 120, 54-70 (2024)
   PUBMED   38772427
  REMARK    GeneRIF: Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Chen,H., Zhao,S., Jian,Q., Yan,Y., Wang,S., Zhang,X. and Ji,Y.
  TITLE     The role of ApoE in fatty acid transport from neurons to astrocytes
            under ischemia/hypoxia conditions
  JOURNAL   Mol Biol Rep 51 (1), 320 (2024)
   PUBMED   38393618
  REMARK    GeneRIF: The role of ApoE in fatty acid transport from neurons to
            astrocytes under ischemia/hypoxia conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Matsuo,H., Kawakami,K., Ohara,H., Kaneko,T., Mashimo,T., Yamada,T.
            and Nabika,T.
  TITLE     Apolipoprotein E-depletion accelerates arterial fat deposition in
            the spontaneously hypertensive rat
  JOURNAL   Exp Anim 72 (4), 439-445 (2023)
   PUBMED   37081644
  REMARK    GeneRIF: Apolipoprotein E-depletion accelerates arterial fat
            deposition in the spontaneously hypertensive rat.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Jiang,C., Chen,Z., Wang,X., Zhang,Y., Guo,X., Fan,H., Huang,D.,
            He,Y., Tang,X., Ai,Y., Liu,Y., Yang,H. and Hao,D.
  TITLE     Curcumin-activated Olfactory Ensheathing Cells Improve Functional
            Recovery After Spinal Cord Injury by Modulating Microglia
            Polarization Through APOE/TREM2/NF-kappaB Signaling Pathway
  JOURNAL   J Neuroimmune Pharmacol 18 (3), 476-494 (2023)
   PUBMED   37658943
  REMARK    GeneRIF: Curcumin-activated Olfactory Ensheathing Cells Improve
            Functional Recovery After Spinal Cord Injury by Modulating
            Microglia Polarization Through APOE/TREM2/NF-kappaB Signaling
            Pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Nguyen,T.D., Watanabe,A., Burleigh,S., Ghaffarzadegan,T.,
            Kanklai,J., Prykhodko,O., Hallenius,F.F. and Nyman,M.
  TITLE     Monobutyrin and monovalerin improve gut-blood-brain biomarkers and
            alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats
  JOURNAL   Sci Rep 12 (1), 15454 (2022)
   PUBMED   36104381
  REMARK    GeneRIF: Monobutyrin and monovalerin improve gut-blood-brain
            biomarkers and alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Takahashi,S., Kawarabayasi,Y., Nakai,T., Sakai,J. and Yamamoto,T.
  TITLE     Rabbit very low density lipoprotein receptor: a low density
            lipoprotein receptor-like protein with distinct ligand specificity
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9252-9256 (1992)
   PUBMED   1384047
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Feussner,G., Funke,H., Weng,W., Assmann,G., Lackner,K.J. and
            Ziegler,R.
  TITLE     Severe type III hyperlipoproteinemia associated with unusual
            apolipoprotein E1 phenotype and epsilon 1/'null' genotype
  JOURNAL   Eur J Clin Invest 22 (9), 599-608 (1992)
   PUBMED   1360898
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Utermann,G., Hees,M. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E and occurrence of
            dysbetalipoproteinaemia in man
  JOURNAL   Nature 269 (5629), 604-607 (1977)
   PUBMED   199847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC086581.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All five variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220125.1, FQ209400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..312
                     /product="apolipoprotein E precursor"
                     /note="apo-E"
                     /calculated_mol_wt=33845
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1927
     mat_peptide     19..312
                     /product="Apolipoprotein E. /id=PRO_0000001996"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
                     /calculated_mol_wt=33845
     Region          72..247
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          73..258
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          202..282
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          258..312
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          270..282
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     CDS             1..312
                     /gene="Apoe"
                     /gene_synonym="APOEA"
                     /coded_by="NM_001270681.1:137..1075"
                     /db_xref="GeneID:25728"
                     /db_xref="RGD:2138"
ORIGIN      
        1 mkalwalllv plltgclaeg elevtdqlpg qsdqpweqal nrfwdylrwv qtlsdqvqee
       61 lqssqvtqel tvlmedtmte vkaykkelee qlgpvaeetr arlakevqaa qarlgadmed
      121 lrnrlgqyrn evntmlgqst eelrsrlsth lrkmrkrlmr daddlqkrla vykagaqega
      181 ergvsairer lgplveqgrq rtanlgagaa qplrdraqal sdrirgrlee vgnqardrle
      241 evreqmeevr skmeeqtqqi rlqaeifqar ikgwfeplve dmqrqwanlm ekiqasvatn
      301 siasttvple nq
//
LOCUS       NP_001263359              89 aa            linear   ROD 27-APR-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim9
            [Rattus norvegicus].
ACCESSION   NP_001263359
VERSION     NP_001263359.1
DBSOURCE    REFSEQ: accession NM_001276430.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Webb,C.T., Gorman,M.A., Lazarou,M., Ryan,M.T. and Gulbis,J.M.
  TITLE     Crystal structure of the mitochondrial chaperone TIM9.10 reveals a
            six-bladed alpha-propeller
  JOURNAL   Mol Cell 21 (1), 123-133 (2006)
   PUBMED   16387659
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Muhlenbein,N., Hofmann,S., Rothbauer,U. and Bauer,M.F.
  TITLE     Organization and function of the small Tim complexes acting along
            the import pathway of metabolite carriers into mammalian
            mitochondria
  JOURNAL   J Biol Chem 279 (14), 13540-13546 (2004)
   PUBMED   14726512
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Paschen,S.A., Rothbauer,U., Kaldi,K., Bauer,M.F., Neupert,W. and
            Brunner,M.
  TITLE     The role of the TIM8-13 complex in the import of Tim23 into
            mitochondria
  JOURNAL   EMBO J 19 (23), 6392-6400 (2000)
   PUBMED   11101512
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1 and FM056491.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.16160.1, FM056491.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840111,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..89
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim9"
                     /note="translocase of inner mitochondrial membrane 9
                     homolog"
                     /calculated_mol_wt=10245
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5J7; propagated from
                     UniProtKB/Swiss-Prot (Q9WV97.3)"
     Region          10..69
                     /region_name="zf-Tim10_DDP"
                     /note="Tim10/DDP family zinc finger; pfam02953"
                     /db_xref="CDD:460764"
     Region          28..52
                     /region_name="Twin CX3C motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WV97.3)"
     CDS             1..89
                     /gene="Timm9"
                     /gene_synonym="Tim9; Tim9a; Timm9a"
                     /coded_by="NM_001276430.1:161..430"
                     /db_xref="GeneID:171139"
                     /db_xref="RGD:621656"
ORIGIN      
        1 maaqipesdq ikqfkeflgt ynkltetcfl dcvkdfttre vkpeevtcse hclqkylkmt
       61 qrismrfqey hiqqnealaa kagllgqpr
//
LOCUS       NP_001161138             472 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 3, Y-linked
            [Rattus norvegicus].
ACCESSION   NP_001161138 XP_003749296 XP_003753627
VERSION     NP_001161138.1
DBSOURCE    REFSEQ: accession NM_001167666.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Cortez,D., Marin,R., Toledo-Flores,D., Froidevaux,L., Liechti,A.,
            Waters,P.D., Grutzner,F. and Kaessmann,H.
  TITLE     Origins and functional evolution of Y chromosomes across mammals
  JOURNAL   Nature 508 (7497), 488-493 (2014)
   PUBMED   24759410
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Pink,C.J., Swaminathan,S.K., Dunham,I., Rogers,J., Ward,A. and
            Hurst,L.D.
  TITLE     Evidence that replication-associated mutation alone does not
            explain between-chromosome differences in substitution rates
  JOURNAL   Genome Biol Evol 1, 13-22 (2009)
   PUBMED   20333173
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158736.1.
            
            On or before Jun 26, 2012 this sequence version replaced
            XP_003753627.1, XP_003749296.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158736.1, GATN01000003.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="Y"
                     /map="Yq11"
     Protein         1..472
                     /product="eukaryotic translation initiation factor 2
                     subunit 3, Y-linked"
                     /EC_number="3.6.5.3"
                     /note="eIF-2-gamma Y; eukaryotic translation initiation
                     factor 2 subunit gamma, Y-linked; eukaryotic translation
                     initiation factor 2, subunit 3 gamma"
                     /calculated_mol_wt=51023
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P41091; propagated from
                     UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          13..466
                     /region_name="PTZ00327"
                     /note="eukaryotic translation initiation factor 2 gamma
                     subunit; Provisional"
                     /db_xref="CDD:240362"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0N1; propagated from
                     UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          48..55
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          76..80
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          134..137
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          190..193
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (C9WPN6.2)"
     Region          225..227
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (C9WPN6.2)"
     CDS             1..472
                     /gene="Eif2s3y"
                     /coded_by="NM_001167666.1:6..1424"
                     /db_xref="GeneID:100312984"
                     /db_xref="RGD:2314438"
ORIGIN      
        1 maggeagvtl gqphlsrqdl atldvtkltp lsheiisrqa tinigtighv ahgkstvvka
       61 isgvhtvrfk nelernitik lgyanakiyk lddsscprpe cyrscgsstp defpsdipgi
      121 kgnfrlvrhv sfvdcpghdi lmatmlngaa vmdaalllia gnescpqpqt sehlaaieim
      181 klkhililqn kidlvkesqa keqyeqilaf vqgtvaegap iipisaqlky nievvceyiv
      241 kkipvplrdf tseprlivir sfdvnkpgce vddlkggvag gsilkgvlkv gqeievrpgi
      301 vskdsegklm ckpifskivs lfaehndlqy aapggligvg tkidptlcra drmvgqvlga
      361 vgalpeifte leisyfllrr llgvrtegdk kaakvqklsk nevlmvnigs lstggrvsav
      421 kadlgkivlt npvctevgek ialsrrvekh wrligwgqir rgvtikptid de
//
LOCUS       NP_062154                321 aa            linear   ROD 27-APR-2025
DEFINITION  gap junction delta-2 protein [Rattus norvegicus].
ACCESSION   NP_062154
VERSION     NP_062154.1
DBSOURCE    REFSEQ: accession NM_019281.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Singhal,P., Senecal,J.M.M. and Nagy,J.I.
  TITLE     Expression of the gap junction protein connexin36 in small
            intensely fluorescent (SIF) cells in cardiac parasympathetic
            ganglia of rodents
  JOURNAL   Neurosci Lett 793, 136989 (2023)
   PUBMED   36471528
  REMARK    GeneRIF: Expression of the gap junction protein connexin36 in small
            intensely fluorescent (SIF) cells in cardiac parasympathetic
            ganglia of rodents.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Brown,C.A., Del Corsso,C., Zoidl,C., Donaldson,L.W., Spray,D.C. and
            Zoidl,G.
  TITLE     Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and
            Strength of Electrical Synapses
  JOURNAL   Cells 8 (10), 1146 (2019)
   PUBMED   31557934
  REMARK    GeneRIF: Tubulin-dependent transport of Cx36 potentiates synaptic
            strength by delivering channels to Gap-junction plaques,
            reinforcing the role of protein transport at chemical and
            electrical synapses to fine-tune communication between neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Wang,P., Wang,S.C., Li,D., Li,T., Yang,H.P., Wang,L., Wang,Y.F. and
            Parpura,V.
  TITLE     Role of Connexin 36 in Autoregulation of Oxytocin Neuronal Activity
            in Rat Supraoptic Nucleus
  JOURNAL   ASN Neuro 11, 1759091419843762 (2019)
   PUBMED   31091986
  REMARK    GeneRIF: Cx36-mediated junctional communication plays a crucial
            role in autoregulatory control of oxytocin neuronal activity
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Li,J., Zhang,S., Liu,X., Han,D., Xu,J. and Ma,Y.
  TITLE     Neuroprotective effects of leonurine against oxygen-glucose
            deprivation by targeting Cx36/CaMKII in PC12 cells
  JOURNAL   PLoS One 13 (7), e0200705 (2018)
   PUBMED   30016355
  REMARK    GeneRIF: these results suggest that leonurine might have a
            protective effect on OGD-induced PC12 cells through targeting the
            Cx36/CaMKII pathway. Thus, leonurine appears to have potential as a
            preventive or therapeutic drug against ischemic-induced neuronal
            injury.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Ouachikh,O., Hafidi,A., Boucher,Y. and Dieb,W.
  TITLE     Electrical Synapses are Involved in Orofacial Neuropathic Pain
  JOURNAL   Neuroscience 382, 69-79 (2018)
   PUBMED   29746991
  REMARK    GeneRIF: our findings demonstrated that Cx36 play an important role
            in mechanical allodynia by coupling GABA cells
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Le Gurun,S., Martin,D., Formenton,A., Maechler,P., Caille,D.,
            Waeber,G., Meda,P. and Haefliger,J.A.
  TITLE     Connexin-36 contributes to control function of insulin-producing
            cells
  JOURNAL   J Biol Chem 278 (39), 37690-37697 (2003)
   PUBMED   12766175
  REMARK    GeneRIF: Connexin-36 contributes to control function of
            insulin-producing cells.
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Deans,M.R., Gibson,J.R., Sellitto,C., Connors,B.W. and Paul,D.L.
  TITLE     Synchronous activity of inhibitory networks in neocortex requires
            electrical synapses containing connexin36
  JOURNAL   Neuron 31 (3), 477-485 (2001)
   PUBMED   11516403
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Calabrese,A., Guldenagel,M., Charollais,A., Mas,C., Caton,D.,
            Bauquis,J., Serre-Beinier,V., Caille,D., Sohl,G., Teubner,B., Le
            Gurun,S., Trovato-Salinaro,A., Condorelli,D.F., Haefliger,J.A.,
            Willecke,K. and Meda,P.
  TITLE     Cx36 and the function of endocrine pancreas
  JOURNAL   Cell Commun Adhes 8 (4-6), 387-391 (2001)
   PUBMED   12064624
  REMARK    GeneRIF: data provide evidence that connexin 36-dependent signaling
            contributes to regulate the function of native and tumoral
            insulin-producing cells
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Rash,J.E., Yasumura,T., Davidson,K.G., Furman,C.S., Dudek,F.E. and
            Nagy,J.I.
  TITLE     Identification of cells expressing Cx43, Cx30, Cx26, Cx32 and Cx36
            in gap junctions of rat brain and spinal cord
  JOURNAL   Cell Commun Adhes 8 (4-6), 315-320 (2001)
   PUBMED   12064610
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Sohl,G., Degen,J., Teubner,B. and Willecke,K.
  TITLE     The murine gap junction gene connexin36 is highly expressed in
            mouse retina and regulated during brain development
  JOURNAL   FEBS Lett 428 (1-2), 27-31 (1998)
   PUBMED   9645468
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Y16898.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y16898.1, AJ296282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..321
                     /product="gap junction delta-2 protein"
                     /function="gap junction protein"
                     /note="gap junction membrane channel protein alpha 9;
                     connexin-36; connexin s; gap junction alpha-9 protein"
                     /calculated_mol_wt=35921
     Region          3..277
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            20..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70610.1)"
     Site            76..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70610.1)"
     Region          120..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70610.1)"
     Site            198..220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70610.1)"
     Site            253..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70610.1)"
     CDS             1..321
                     /gene="Gjd2"
                     /gene_synonym="Cx36; Cxns; Gja9"
                     /coded_by="NM_019281.2:116..1081"
                     /db_xref="GeneID:50564"
                     /db_xref="RGD:2694"
ORIGIN      
        1 mgewtilerl leaavqqhst migrilltvv vifrilivai vgetvyddeq tmfvcntlqp
       61 gcnqacydra fpishirywv fqiimvctps lcfitysvhq sakqrerrys tvflaldrdp
      121 aesiggpggt ggggsggskr edkklqnaiv ngvlqntett sketepdcle vkelaphpsg
      181 lrtaarsklr rqegisrfyi iqvvfrnale igflvgqyfl ygfsvpglye cnrypcikev
      241 ecyvsrptek tvflvfmfav sgicvvlnla elnhlgwrki klavrgaqak rksvyeirnk
      301 dlprvsvpnf grtqssdsay v
//
LOCUS       NP_071979                427 aa            linear   ROD 27-APR-2025
DEFINITION  transcobalamin-2 precursor [Rattus norvegicus].
ACCESSION   NP_071979
VERSION     NP_071979.2
DBSOURCE    REFSEQ: accession NM_022534.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Alam,A., Woo,J.S., Schmitz,J., Prinz,B., Root,K., Chen,F.,
            Bloch,J.S., Zenobi,R. and Locher,K.P.
  TITLE     Structural basis of transcobalamin recognition by human CD320
            receptor
  JOURNAL   Nat Commun 7, 12100 (2016)
   PUBMED   27411955
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Orozco-Barrios,C.E., Battaglia-Hsu,S.F., Arango-Rodriguez,M.L.,
            Ayala-Davila,J., Chery,C., Alberto,J.M., Schroeder,H., Daval,J.L.,
            Martinez-Fong,D. and Gueant,J.L.
  TITLE     Vitamin B12-impaired metabolism produces apoptosis and Parkinson
            phenotype in rats expressing the transcobalamin-oleosin chimera in
            substantia nigra
  JOURNAL   PLoS One 4 (12), e8268 (2009)
   PUBMED   20027219
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Pereira,A.C., Lourenco,D.M., Maffei,F.H., Morelli,V.M., Rollo,H.A.,
            Zago,M.A., Vannucchi,H. and Franco,R.F.
  TITLE     A transcobalamin gene polymorphism and the risk of venous
            thrombosis. The BRATROS (Brazilian Thrombosis Study)
  JOURNAL   Thromb Res 119 (2), 183-188 (2007)
   PUBMED   16530812
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Wuerges,J., Garau,G., Geremia,S., Fedosov,S.N., Petersen,T.E. and
            Randaccio,L.
  TITLE     Structural basis for mammalian vitamin B12 transport by
            transcobalamin
  JOURNAL   Proc Natl Acad Sci U S A 103 (12), 4386-4391 (2006)
   PUBMED   16537422
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Li,N., Rosenblatt,D.S., Kamen,B.A., Seetharam,S. and Seetharam,B.
  TITLE     Identification of two mutant alleles of transcobalamin II in an
            affected family
  JOURNAL   Hum Mol Genet 3 (10), 1835-1840 (1994)
   PUBMED   7849710
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Quadros,E.V., Sai,P. and Rothenberg,S.P.
  TITLE     Functional human transcobalamin II isoproteins are secreted by
            insect cells using the baculovirus expression system
  JOURNAL   Blood 81 (5), 1239-1245 (1993)
   PUBMED   8443384
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Biosca,M., Encabo,G., Garcia-Bragado,F., Mane,S., Ruibal,A. and
            Vilardell,Y.M.
  TITLE     Transcobalamin II. A specific marker of renal involvement in
            essential mixed cryoglobulinemia
  JOURNAL   Nephron 45 (3), 255-256 (1987)
   PUBMED   3574578
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Fiedler-Nagy,C., Rowley,G.R., Coffey,J.W. and Miller,O.N.
  TITLE     Binding of vitamin B12--rat transcobalamin II and free vitamin B12
            to plasma membranes isolated from rat liver
  JOURNAL   Br J Haematol 31 (3), 311-321 (1975)
   PUBMED   1201244
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Zittoun,J., Zittoun,R., Marquet,J. and Sultan,C.
  TITLE     The three transcobalamins in myeloproliferative disorders and acute
            leukaemia
  JOURNAL   Br J Haematol 31 (3), 287-298 (1975)
   PUBMED   1059479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Apr 28, 2015 this sequence version replaced NP_071979.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF054810.1, SRR26643285.39070.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..427
                     /product="transcobalamin-2 precursor"
                     /note="transcobalamin II; TC-2; TCII; TC II"
                     /calculated_mol_wt=45710
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1825
     Region          19..325
                     /region_name="Cobalamin_bind"
                     /note="Eukaryotic cobalamin-binding protein; pfam01122"
                     /db_xref="CDD:460073"
     Region          352..424
                     /region_name="DUF4430"
                     /note="Domain of unknown function (DUF4430); pfam14478"
                     /db_xref="CDD:433979"
     CDS             1..427
                     /gene="Tcn2"
                     /gene_synonym="Tc2; Tcn2p"
                     /coded_by="NM_022534.2:71..1354"
                     /db_xref="GeneID:64365"
                     /db_xref="RGD:620681"
ORIGIN      
        1 mellkallll sgvlgalaef cvipkmdgql veklgqrllp wmdrlsseql npsiyvglrl
       61 ssmqagtken lylhnlklhy qqcllrstss ddnsgcqtki sggslalyll alrancellg
      121 srkgdrmvsq lkwfledekk aighhheghp htsyyqygls ilalcvhrkr vhdsvvgkll
      181 yavehdyfty qghlsvdtea maglaftcle rfnfnsdlrp rittaietvr ekilkaqape
      241 gyfgniystp lalqmlmtsp gvglgpaclk arkslllslq dgafqnpmmi sqllpvlnhk
      301 tylnlispdc qaprvmlvpa tedpvhlsev svtlkvssvl ppyertvsvf agasledvlk
      361 rardlgefty gtqaslsgpy ltsvlgkeag dreywqllrv pdtpllqgia dykpkngeti
      421 elrlvrw
//
LOCUS       NP_075230                358 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group I member 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_075230
VERSION     NP_075230.1
DBSOURCE    REFSEQ: accession NM_022941.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Yamada,T., Cohen,S.M. and Lake,B.G.
  TITLE     Critical evaluation of the human relevance of the mode of action
            for rodent liver tumor formation by activators of the constitutive
            androstane receptor (CAR)
  JOURNAL   Crit Rev Toxicol 51 (5), 373-394 (2021)
   PUBMED   34264181
  REMARK    GeneRIF: Critical evaluation of the human relevance of the mode of
            action for rodent liver tumor formation by activators of the
            constitutive androstane receptor (CAR).
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Gabbia,D., Pozza,A.D., Albertoni,L., Lazzari,R., Zigiotto,G.,
            Carrara,M., Baldo,V., Baldovin,T., Floreani,A. and Martin,S.
  TITLE     Pregnane X receptor and constitutive androstane receptor modulate
            differently CYP3A-mediated metabolism in early- and late-stage
            cholestasis
  JOURNAL   World J Gastroenterol 23 (42), 7519-7530 (2017)
   PUBMED   29204052
  REMARK    GeneRIF: nuclear expression virtually disappeared in the late stage
            of cholestatic injury, after an initial increase
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Forbes,K.P., Kouranova,E., Tinker,D., Janowski,K., Cortner,D.,
            McCoy,A. and Cui,X.
  TITLE     Creation and Preliminary Characterization of Pregnane X Receptor
            and Constitutive Androstane Receptor Knockout Rats
  JOURNAL   Drug Metab Dispos 45 (10), 1068-1076 (2017)
   PUBMED   28716828
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Fujino,C., Tamura,Y., Tange,S., Nakajima,H., Sanoh,S., Watanabe,Y.,
            Uramaru,N., Kojima,H., Yoshinari,K., Ohta,S. and Kitamura,S.
  TITLE     Metabolism of methiocarb and carbaryl by rat and human livers and
            plasma, and effect on their PXR, CAR and PPARalpha activities
  JOURNAL   J Toxicol Sci 41 (5), 677-691 (2016)
   PUBMED   27665777
  REMARK    GeneRIF: Metabolism of methiocarb and carbaryl does not alter CAR
            activity.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Shao,Y.Y., Huang,J., Ma,Y.R., Han,M., Ma,K., Qin,H.Y., Rao,Z. and
            Wu,X.A.
  TITLE     Serum serotonin reduced the expression of hepatic transporter Mrp2
            and P-gp via regulating nuclear receptor CAR in PI-IBS rats
  JOURNAL   Can J Physiol Pharmacol 93 (8), 633-639 (2015)
   PUBMED   26053941
  REMARK    GeneRIF: Serum 5-HT regulates the expression of Mrp2 and P-gp, and
            the underlying mechanism may be related to the altered expression
            of the nuclear receptor constitutive androstane receptor.
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Numazawa,S., Shindo,S., Maruyama,K., Chibana,F., Kawahara,Y.,
            Ashino,T., Tanaka,S. and Yoshida,T.
  TITLE     Impaired nuclear translocation of CAR in hepatic preneoplastic
            lesions: association with an attenuated CYP2B induction by
            phenobarbital
  JOURNAL   FEBS Lett 579 (17), 3560-3564 (2005)
   PUBMED   15953603
  REMARK    GeneRIF: CAR expressed in the hepatic preneoplastic lesions of rats
            is resistant to nuclear translocation and transactivation of the
            phenobarbital(PB) responsive enhancer module upon PB treatment.
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Yoshinari,K., Kobayashi,K., Moore,R., Kawamoto,T. and Negishi,M.
  TITLE     Identification of the nuclear receptor CAR:HSP90 complex in mouse
            liver and recruitment of protein phosphatase 2A in response to
            phenobarbital
  JOURNAL   FEBS Lett 548 (1-3), 17-20 (2003)
   PUBMED   12885400
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Gonzalez,M.M. and Carlberg,C.
  TITLE     Cross-repression, a functional consequence of the physical
            interaction of non-liganded nuclear receptors and POU domain
            transcription factors
  JOURNAL   J Biol Chem 277 (21), 18501-18509 (2002)
   PUBMED   11891224
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Yoshinari,K., Sueyoshi,T., Moore,R. and Negishi,M.
  TITLE     Nuclear receptor CAR as a regulatory factor for the sexually
            dimorphic induction of CYB2B1 gene by phenobarbital in rat livers
  JOURNAL   Mol Pharmacol 59 (2), 278-284 (2001)
   PUBMED   11160864
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Xie,W., Barwick,J.L., Simon,C.M., Pierce,A.M., Safe,S.,
            Blumberg,B., Guzelian,P.S. and Evans,R.M.
  TITLE     Reciprocal activation of xenobiotic response genes by nuclear
            receptors SXR/PXR and CAR
  JOURNAL   Genes Dev 14 (23), 3014-3023 (2000)
   PUBMED   11114890
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089763.1 and JAXUCZ010000013.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB104736.1, SRR26643286.37120.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..358
                     /product="nuclear receptor subfamily 1 group I member 3
                     isoform 1"
                     /note="constitutive androstane receptor; strain Fischer
                     nuclear receptor (CAR); nuclear receptor constitutive
                     active receptor"
                     /calculated_mol_wt=40792
     Region          21..92
                     /region_name="NR_DBD_VDR_like"
                     /note="The DNA-binding domain of vitamin D receptors (VDR)
                     like nuclear receptor family is composed of two C4-type
                     zinc fingers; cd07156"
                     /db_xref="CDD:143531"
     Site            order(21,24,38,41,57,63,73,76)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143531"
     Site            order(31..33,39..40,42,46..47,70..71,77,91..92)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143531"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q14994; propagated from
                     UniProtKB/Swiss-Prot (Q9QUS1.1)"
     Site            order(58..59,72,89..90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143531"
     Region          116..356
                     /region_name="NR_LBD"
                     /note="The ligand binding domain of nuclear receptors, a
                     family of ligand-activated transcription regulators;
                     cl11397"
                     /db_xref="CDD:472173"
     Site            order(171..172,175,178..179,208..209,212..213,216,219,252)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132726"
     Site            order(180,183,187,192,197..198,200..201,204..205)
                     /site_type="active"
                     /note="coregulator recognition site [active]"
                     /db_xref="CDD:132726"
     CDS             1..358
                     /gene="Nr1i3"
                     /gene_synonym="CAR"
                     /coded_by="NM_022941.4:150..1226"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:65035"
                     /db_xref="RGD:621400"
ORIGIN      
        1 mtatltletm tseeeygprn cvvcgdratg yhfhaltceg ckgffrrtvs ktigpicpfa
       61 grcevskaqr rhcpacrlqk clnvgmrkdm ilsaealalr rarqarrraq kaslqlsqqq
      121 keliqtllga htrhvgpmfd qfvqfrppay lfshhrpfqp lapvlpllth fadintfmvq
      181 qiikftkdlp lfrsltmedq isllkgaave ilhislnttf clqtqnffcg plcykmedav
      241 hvgfqyefle liihfhktlk rlqlqepeya lmaamalfsp drpgvtqree idqlqeeval
      301 ilnnhimeqq srlqsrflya klmgllaelr sinsaysyei hriqglsamm pllgeics
//
LOCUS       NP_001258003             219 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001258003
VERSION     NP_001258003.1
DBSOURCE    REFSEQ: accession NM_001271074.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U51195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..219
                     /product="amelogenin, X isoform isoform 1 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=22985
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Region          28..195
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     CDS             1..219
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_001271074.1:67..726"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyevltplk wyqsmirqpy psygyepmgg
       61 wlhhqiipvl sqqhppshtl qphhhlpvvp aqqpvapqqp mmpvpghhsm tptqhhqpni
      121 ppsaqqpfqq pfqpqaippq shqpmqpqsp lhpmqplapq pplpplfsmq plspilpelp
      181 leawpatdkt kreevafspm kwyqgtarhp lnmetttek
//
LOCUS       NP_001289012             461 aa            linear   ROD 27-APR-2025
DEFINITION  ornithine decarboxylase [Rattus norvegicus].
ACCESSION   NP_001289012 XP_008762795
VERSION     NP_001289012.1
DBSOURCE    REFSEQ: accession NM_001302083.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Liu,W., Wu,Y.H., Zhang,L., Liu,X.Y., Wang,Y., Xue,B., Liu,B.,
            Cai,Y., Zhang,B. and Ji,Y.
  TITLE     Effects of lentivirus-mediated ornithine decarboxylase gene on the
            proliferation and apoptosis of fibroblast-like synoviocytes in rats
            with arthritis
  JOURNAL   Life Sci 194, 224-230 (2018)
   PUBMED   28986097
  REMARK    GeneRIF: The results indicated that overexpression of ODC gene
            promotes the proliferation while suppressing apoptosis of
            fibroblast-like synoviocytes in rats with rheumatoid arthritis.
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Ramos-Molina,B., Lambertos,A., Lopez-Contreras,A.J., Kasprzak,J.M.,
            Czerwoniec,A., Bujnicki,J.M., Cremades,A. and Penafiel,R.
  TITLE     Structural and degradative aspects of ornithine decarboxylase
            antizyme inhibitor 2
  JOURNAL   FEBS Open Bio 4, 510-521 (2014)
   PUBMED   24967154
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Zhang,H., Xue,G., Zhang,W., Wang,L., Li,H., Zhang,L., Lu,F.,
            Bai,S., Lin,Y., Lou,Y., Xu,C. and Zhao,Y.
  TITLE     Akt and Erk1/2 activate the ornithine decarboxylase/polyamine
            system in cardioprotective ischemic preconditioning in rats: the
            role of mitochondrial permeability transition pores
  JOURNAL   Mol Cell Biochem 390 (1-2), 133-142 (2014)
   PUBMED   24464033
  REMARK    GeneRIF: These results suggest that IPC upregulates the Ornithine
            decarboxylase/polyamine system and mediates preconditioning
            cardioprotection.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Passariello,C.L., Gottardi,D., Cetrullo,S., Zini,M., Campana,G.,
            Tantini,B., Pignatti,C., Flamigni,F., Guarnieri,C., Caldarera,C.M.
            and Stefanelli,C.
  TITLE     Evidence that AMP-activated protein kinase can negatively modulate
            ornithine decarboxylase activity in cardiac myoblasts
  JOURNAL   Biochim Biophys Acta 1823 (4), 800-807 (2012)
   PUBMED   22230191
  REMARK    GeneRIF: The modulation of ODC activity by AMPK represents a
            mechanism that may contribute to control cell growth processes.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Wang,J.Y., Viar,M.J., McCormack,S.A. and Johnson,L.R.
  TITLE     Effect of putrescine on S-adenosylmethionine decarboxylase in a
            small intestinal crypt cell line
  JOURNAL   Am J Physiol 263 (4 Pt 1), G494-G501 (1992)
   PUBMED   1415709
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Van Steeg,H., Van Oostrom,C.T., Hodemaekers,H.M., Peters,L. and
            Thomas,A.A.
  TITLE     The translation in vitro of rat ornithine decarboxylase mRNA is
            blocked by its 5' untranslated region in a polyamine-independent
            way
  JOURNAL   Biochem J 274 (Pt 2) (Pt 2), 521-526 (1991)
   PUBMED   2006916
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Eloranta,T.O., Khomutov,A.R., Khomutov,R.M. and Hyvonen,T.
  TITLE     Aminooxy analogues of spermidine as inhibitors of spermine synthase
            and substrates of hepatic polyamine acetylating activity
  JOURNAL   J Biochem 108 (4), 593-598 (1990)
   PUBMED   2292587
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Manzella,J.M. and Blackshear,P.J.
  TITLE     Regulation of rat ornithine decarboxylase mRNA translation by its
            5'-untranslated region
  JOURNAL   J Biol Chem 265 (20), 11817-11822 (1990)
   PUBMED   2365701
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Wen,L., Huang,J.K. and Blackshear,P.J.
  TITLE     Rat ornithine decarboxylase gene. Nucleotide sequence, potential
            regulatory elements, and comparison to the mouse gene
  JOURNAL   J Biol Chem 264 (15), 9016-9021 (1989)
   PUBMED   2722815
REFERENCE   10 (residues 1 to 461)
  AUTHORS   van Steeg,H., van Oostrom,T.M., van Kranen,H.J. and van Kreijl,C.F.
  TITLE     Nucleotide sequence of the rat ornithine decarboxylase gene
  JOURNAL   Nucleic Acids Res 16 (16), 8173-8174 (1988)
   PUBMED   3419906
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M16982.1, J04791.1, DV728774.1 and FQ151473.1.
            
            On Sep 26, 2014 this sequence version replaced XP_008762795.1.
            
            Transcript Variant: This variant (2) has two alternate splice sites
            in the 5' UTR, compared to variant 1. Variants 1 and 2 encode the
            same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J04791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 2365701
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..461
                     /product="ornithine decarboxylase"
                     /EC_number="4.1.1.17"
                     /note="Ornitine decarboxylase"
                     /calculated_mol_wt=50916
     Region          37..408
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(38,69,90..91,93..94,116,121,134,137,141,168..170,
                     291,293..294,315,317,319,322..323,331,333,357,359,361,364,
                     393,395,397..399,401)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,332,360,389)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(67,69,88,154,197,200,236..237,274..277,360,389)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(69,360)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            197
                     /site_type="other"
                     /note="Stacks against the aromatic ring of pyridoxal
                     phosphate and stabilizes reaction intermediates.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P09057.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:P00860; propagated from
                     UniProtKB/Swiss-Prot (P09057.1)"
     Site            order(331..332,360..361,389,397)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
     CDS             1..461
                     /gene="Odc1"
                     /gene_synonym="Odc"
                     /coded_by="NM_001302083.1:275..1660"
                     /db_xref="GeneID:24609"
                     /db_xref="RGD:3227"
ORIGIN      
        1 mgsftkeefd childegfta kdildqkine vsssddkdaf yvadlgdvlk khlrwlkalp
       61 rvtpfyavkc ndsraivstl aaigtgfdca skteiqlvqg lgvpperiiy anpckqvsqi
      121 kyaasngvqm mtfdseielm kvarahpkak lvlriatdds kavcrlsvkf gatlktsrll
      181 lerakelnid vigvsfhvgs gctdpetfvq avsdarcvfd mgtevgfsmy lldigggfpg
      241 sedtklkfee itsvinpald kyfpsdsgvr iiaepgryyv asaftlavni iakktvwkeq
      301 tgsddedesn eqtlmyyvnd gvygsfncil ydhahvkall qkrpkpdeky ysssiwgptc
      361 dgldriverc slpemhvgdw mlfenmgayt vaaastfngf qrpniyyvms rsmwqlmkqi
      421 qshgfppeve eqdvgtlpms caqesgmdrh paacasasin v
//
LOCUS       NP_001257509             495 aa            linear   ROD 27-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform c precursor [Rattus norvegicus].
ACCESSION   NP_001257509
VERSION     NP_001257509.1
DBSOURCE    REFSEQ: accession NM_001270580.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1, Z23273.1 and CR475040.1.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant (1). The resulting isoform (c) has the
            same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z23273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN12840105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..495
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform c precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=54478
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          149..444
                     /region_name="7tmB1_PACAP-R1"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type 1 receptor, member of the class B family of
                     seven-transmembrane G protein-coupled receptors; cd15987"
                     /db_xref="CDD:320653"
     Region          151..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320653"
     Site            order(156,160,202,205..206,209,226,233,304..305,307,309,
                     393,396,409,413)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320653"
     Region          185..207
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320653"
     Region          226..253
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320653"
     Region          265..285
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320653"
     Region          301..330
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320653"
     Region          346..401
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320653"
     Region          406..431
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320653"
     CDS             1..495
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_001270580.1:338..1825"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiyltn lrlrvpkktr
      361 edplpvpsdq hsppflrlar stllliplfg ihytvfafsp envskrerlv felglgsfqg
      421 fvvavlycfl ngevqaeikr kwrswkvnry ftmdfkhrhp slassgvngg tqlsilskss
      481 sqlrmsslpa dnlat
//
LOCUS       NP_001099293             857 aa            linear   ROD 27-APR-2025
DEFINITION  GAS2-like protein 2 [Rattus norvegicus].
ACCESSION   NP_001099293 XP_001081061 XP_220783
VERSION     NP_001099293.2
DBSOURCE    REFSEQ: accession NM_001105823.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Bustamante-Marin,X.M., Yin,W.N., Sears,P.R., Werner,M.E.,
            Brotslaw,E.J., Mitchell,B.J., Jania,C.M., Zeman,K.L., Rogers,T.D.,
            Herring,L.E., Refabert,L., Thomas,L., Amselem,S., Escudier,E.,
            Legendre,M., Grubb,B.R., Knowles,M.R., Zariwala,M.A. and
            Ostrowski,L.E.
  TITLE     Lack of GAS2L2 Causes PCD by Impairing Cilia Orientation and
            Mucociliary Clearance
  JOURNAL   Am J Hum Genet 104 (2), 229-245 (2019)
   PUBMED   30665704
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Stroud,M.J., Nazgiewicz,A., McKenzie,E.A., Wang,Y., Kammerer,R.A.
            and Ballestrem,C.
  TITLE     GAS2-like proteins mediate communication between microtubules and
            actin through interactions with end-binding proteins
  JOURNAL   J Cell Sci 127 (Pt 12), 2672-2682 (2014)
   PUBMED   24706950
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Wu,Y.C., Lai,H.L., Chang,W.C., Lin,J.T., Liu,Y.J. and Chern,Y.
  TITLE     A novel Galphas-binding protein, Gas-2 like 2, facilitates the
            signaling of the A2A adenosine receptor
  JOURNAL   Biochim Biophys Acta 1833 (12), 3145-3154 (2013)
   PUBMED   23994616
  REMARK    GeneRIF: G2L2 is a new effector that controls the action of A2AR by
            modulating its ability to regulate the Galphas-mediated cAMP
            contents.
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Goriounov,D., Leung,C.L. and Liem,R.K.
  TITLE     Protein products of human Gas2-related genes on chromosomes 17 and
            22 (hGAR17 and hGAR22) associate with both microfilaments and
            microtubules
  JOURNAL   J Cell Sci 116 (Pt 6), 1045-1058 (2003)
   PUBMED   12584248
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Lee,K.K., Cai,D.Q., Tang,M.K., Tsang,K.F., Kwong,W.H. and Chow,P.H.
  TITLE     Growth arrest-specific 2 gene expression during patellar tendon
            healing
  JOURNAL   Cells Tissues Organs 173 (3), 138-146 (2003)
   PUBMED   12673096
  REMARK    GeneRIF: GAS2 gene might play a role in regulating tenocyte
            proliferation during tendon healing.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Sep 2, 2010 this sequence version replaced
            XP_220783.3, XP_001081061.1, NP_001099293.1.
            
            This RefSeq record was created from genomic sequence data because
            no single transcript was available for the full length of the gene.
            The extent of this transcript is supported by alignments and
            orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.38088.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..857
                     /product="GAS2-like protein 2"
                     /calculated_mol_wt=94149
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUE1.1)"
     Region          23..163
                     /region_name="CH_GAS2L1_2"
                     /note="calponin homology (CH) domain found in GAS2-like
                     protein 1 (GAS2L1), GAS2L2, and similar proteins; cd21268"
                     /db_xref="CDD:409117"
     Site            order(34,38,109,111..112,115..116,118,129..137,143,
                     145..146,148..149,152..153,156)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409117"
     Region          206..274
                     /region_name="GAS2"
                     /note="Growth-Arrest-Specific Protein 2 Domain; pfam02187"
                     /db_xref="CDD:460480"
     Region          278..>527
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          282..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUE1.1)"
     Region          432..857
                     /region_name="Interaction with ADORA2A.
                     /evidence=ECO:0000250|UniProtKB:Q5SSG4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUE1.1)"
     Region          670..716
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUE1.1)"
     Region          759..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUE1.1)"
     CDS             1..857
                     /gene="Gas2l2"
                     /gene_synonym="Gas2"
                     /coded_by="NM_001105823.2:1..2574"
                     /db_xref="GeneID:287570"
                     /db_xref="RGD:1307868"
ORIGIN      
        1 msqhvghgrk prtpgppvrs irpfksseqy levmkedlae wlrdlygldi daanflrvle
       61 tglvlcrhan tvteaalafl aeapervqki pmpqvgvfcn gaaqpgtfqa rdnisnfiqw
      121 crkemgiqev lmfetedlvl rknvksvvlc llelgrrawr fgvaapslvy leeeieeelr
      181 rdldlpspdp pppvpparrp chfhnldqmv qslvshctcp vqfsmvkisd gkyrvgdsnt
      241 lifirilrsh vmvrvgggwd tlghyldkhd pcrctslshk pgsflkppgp pvqhevkvqd
      301 gpsqpqplmt isrsqsplpp vdwktytsss rklrpptpss sgprsefpar artpremapf
      361 lrsqekptls qrmsspgpql sspcrgpdlq stlserrvnr spgelprgrt ptswvpkead
      421 sqgahtkapi pqrlqipett skktpargps ppprssslas phtiwlpdqg aspeisepms
      481 aqssspgkgl tkipirlspa rpptpgrgsl gtegggsmqr gslssralag nldrsthghh
      541 svdvskdhqk viqissgted prslgtqerk erytslplgr trepalydnl keelvanmkl
      601 levgaactqg trsqaiprsg vyvpslggmw peprgpydkv iqelvqgppr llkvdlkawk
      661 vgseclprpi vnpgspkeeq vsrergtrrk arpsaqgttv kttspargqd cstlpvsanl
      721 kapthscsdp ssdkakvclg kgkrtlrkpq kvpsiyklkl rprirprrdh rpekrpsrip
      781 kplvypflgp artapgsrll katlggtggd vngvgkkeee kkketsisle ssiqpsesre
      841 pmqldgtplp peeeswv
//
LOCUS       NP_058906                304 aa            linear   ROD 27-APR-2025
DEFINITION  thyroxine 5-deiodinase [Rattus norvegicus].
ACCESSION   NP_058906
VERSION     NP_058906.3
DBSOURCE    REFSEQ: accession NM_017210.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wang,G., Duan,J., Cao,K., Gao,T., Jiang,A., Xu,Y., Zhu,Z. and Yu,W.
  TITLE     [Inhibition of type 3 deiodinase expression can improve
            mitochondrial function in skeletal muscle of sepsis by
            up-regulating peroxisome proliferator-activated receptor-gamma
            coactivator-1alpha]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 36 (8), 841-847 (2024)
   PUBMED   39238408
  REMARK    GeneRIF: [Inhibition of type 3 deiodinase expression can improve
            mitochondrial function in skeletal muscle of sepsis by
            up-regulating peroxisome proliferator-activated receptor-gamma
            coactivator-1alpha].
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Di Munno,C., Busiello,R.A., Calonne,J., Salzano,A.M.,
            Miles-Chan,J., Scaloni,A., Ceccarelli,M., de Lange,P., Lombardi,A.,
            Senese,R., Cioffi,F., Visser,T.J., Peeters,R.P., Dulloo,A.G. and
            Silvestri,E.
  TITLE     Adaptive Thermogenesis Driving Catch-Up Fat Is Associated With
            Increased Muscle Type 3 and Decreased Hepatic Type 1 Iodothyronine
            Deiodinase Activities: A Functional and Proteomic Study
  JOURNAL   Front Endocrinol (Lausanne) 12, 631176 (2021)
   PUBMED   33746903
  REMARK    GeneRIF: Adaptive Thermogenesis Driving Catch-Up Fat Is Associated
            With Increased Muscle Type 3 and Decreased Hepatic Type 1
            Iodothyronine Deiodinase Activities: A Functional and Proteomic
            Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Schweizer,U., Schlicker,C., Braun,D., Kohrle,J. and Steegborn,C.
  TITLE     Crystal structure of mammalian selenocysteine-dependent
            iodothyronine deiodinase suggests a peroxiredoxin-like catalytic
            mechanism
  JOURNAL   Proc Natl Acad Sci U S A 111 (29), 10526-10531 (2014)
   PUBMED   25002520
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Tunc-Ozcan,E., Ullmann,T.M., Shukla,P.K. and Redei,E.E.
  TITLE     Low-dose thyroxine attenuates autism-associated adverse effects of
            fetal alcohol in male offspring's social behavior and hippocampal
            gene expression
  JOURNAL   Alcohol Clin Exp Res 37 (11), 1986-1995 (2013)
   PUBMED   23763370
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Hernandez,A., Garcia,B. and Obregon,M.J.
  TITLE     Gene expression from the imprinted Dio3 locus is associated with
            cell proliferation of cultured brown adipocytes
  JOURNAL   Endocrinology 148 (8), 3968-3976 (2007)
   PUBMED   17510246
  REMARK    GeneRIF: genomic imprinting and gene expression at the Dlk1/Dio3
            imprinted domain may play a role in the regulation of adipocyte
            proliferation and differentiation
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Hernandez,A., Martinez,M.E., Fiering,S., Galton,V.A. and St
            Germain,D.
  TITLE     Type 3 deiodinase is critical for the maturation and function of
            the thyroid axis
  JOURNAL   J Clin Invest 116 (2), 476-484 (2006)
   PUBMED   16410833
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Wasco,E.C., Martinez,E., Grant,K.S., St Germain,E.A., St
            Germain,D.L. and Galton,V.A.
  TITLE     Determinants of iodothyronine deiodinase activities in rodent
            uterus
  JOURNAL   Endocrinology 144 (10), 4253-4261 (2003)
   PUBMED   12959985
  REMARK    GeneRIF: Induction of D3 activity begins immediately after
            implantation and increases markedly over next 72 hours. In
            spontaneously cycling female rats, both D2 and D3 were observed to
            be 3- to 8-fold higher in proestrus, compared with diestrus.
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Friedrichsen,S., Christ,S., Heuer,H., Schafer,M.K., Mansouri,A.,
            Bauer,K. and Visser,T.J.
  TITLE     Regulation of iodothyronine deiodinases in the Pax8-/- mouse model
            of congenital hypothyroidism
  JOURNAL   Endocrinology 144 (3), 777-784 (2003)
   PUBMED   12586753
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Hernandez,A., Fiering,S., Martinez,E., Galton,V.A. and St
            Germain,D.
  TITLE     The gene locus encoding iodothyronine deiodinase type 3 (Dio3) is
            imprinted in the fetus and expresses antisense transcripts
  JOURNAL   Endocrinology 143 (11), 4483-4486 (2002)
   PUBMED   12399446
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Croteau,W., Whittemore,S.L., Schneider,M.J. and St Germain,D.L.
  TITLE     Cloning and expression of a cDNA for a mammalian type III
            iodothyronine deiodinase
  JOURNAL   J Biol Chem 270 (28), 16569-16575 (1995)
   PUBMED   7622463
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000006.1.
            
            On Aug 15, 2009 this sequence version replaced NP_058906.2.
            
            Summary: This is an intronless, imprinted gene that is
            preferentially expressed from the paternal allele. The encoded
            protein belongs to the iodothyronine deiodinase family, and
            catalyzes the inactivation of thyroid hormone by inner ring
            deiodination of the prohormone thyroxine (T4) and the bioactive
            hormone 3,3',5-triiodothyronine (T3) to inactive metabolites,
            3,3',5' triiodothyronine (RT3) and 3,3'-diiodothyronine (T2),
            respectively. It is highly expressed in placenta, fetal and
            neonatal tissues, and thought to prevent premature exposure of
            developing fetal tissues to adult levels of thyroid hormones. It
            thus plays a critical role in mammalian development by regulating
            circulating fetal thyroid hormone concentration. This protein is a
            selenoprotein, containing the rare selenocysteine (Sec) amino acid
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon rather than as a stop signal.
            [provided by RefSeq, Jun 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: U24282.1, SRR26643429.25078.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene                  :: PMID: 17510246
            protein contains selenocysteine :: PMID: 7622463
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..304
                     /product="thyroxine 5-deiodinase"
                     /EC_number="1.21.99.3"
                     /note="type III iodothyronine deiodinase; type 3 DI;
                     type-III 5'-deiodinase; deiodinase, iodothyronine, type 3;
                     deiodinase, iodothyronine, type III"
                     /calculated_mol_wt=33965
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49897.3)"
     Region          39..293
                     /region_name="T4_deiodinase"
                     /note="Iodothyronine deiodinase; pfam00837"
                     /db_xref="CDD:279210"
     Site            43..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49897.3)"
     Site            170
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..304
                     /gene="Dio3"
                     /gene_synonym="5DIII; DIOIII"
                     /coded_by="NM_017210.4:3..917"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="GeneID:29475"
                     /db_xref="RGD:68420"
ORIGIN      
        1 mprqaasrlv vgegegppga sgpaatmlrs lllhslrlca qtasclvlfp rflgtafmlw
       61 lldflcirkh flrrrhpdhp epevelnseg eemppddppi cvsddnrlct laslkavwhg
      121 qkldffkqah eggpapnsev vrpdgfqsqr ildyaqgtrp lvlnfgsctu ppfmarmsaf
      181 qrlvtkyqrd vdfliiyiee ahpsdgwvtt dspyvipqhr sledrvsaar vlqqgapgca
      241 lvldtmanss ssaygayfer lyviqsgtim yqggrgpdgy qvselrtwle rydeqlhgtr
      301 prrl
//
LOCUS       NP_001258043             218 aa            linear   ROD 27-APR-2025
DEFINITION  autophagy-related protein 101 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001258043
VERSION     NP_001258043.1
DBSOURCE    REFSEQ: accession NM_001271114.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Zhang,Z.J., Wang,K.P., Huang,Y.P., Jin,C., Jiang,H., Xiong,L.,
            Chen,Z.Y., Wen,Y., Liu,Z.T. and Mo,J.G.
  TITLE     Comprehensive Analysis of the Potential Immune-Related Biomarker
            ATG101 that Regulates Apoptosis of Cholangiocarcinoma Cells After
            Photodynamic Therapy
  JOURNAL   Front Pharmacol 13, 857774 (2022)
   PUBMED   35592424
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Wang,Y., Lin,K., Xu,T., Wang,L., Fu,L., Zhang,G., Ai,J., Jiao,Y.,
            Zhu,R., Han,X. and Cai,H.
  TITLE     Development and validation of prognostic model based on the
            analysis of autophagy-related genes in colon cancer
  JOURNAL   Aging (Albany NY) 13 (14), 19028-19047 (2021)
   PUBMED   34315829
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Hosokawa,N., Sasaki,T., Iemura,S., Natsume,T., Hara,T. and
            Mizushima,N.
  TITLE     Atg101, a novel mammalian autophagy protein interacting with Atg13
  JOURNAL   Autophagy 5 (7), 973-979 (2009)
   PUBMED   19597335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BU670996.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks a portion of the 5' coding region compared to variant 1.
            These differences cause translation initiation at a downstream AUG
            and result in an isoform (2) with a shorter N-terminus, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript from the same
            strain was available for the full length of the gene. The extent of
            this transcript is supported by {transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY553592.1, CF109006.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..218
                     /product="autophagy-related protein 101 isoform 2"
                     /note="autophagy-related protein 101"
                     /calculated_mol_wt=24885
     Region          11..168
                     /region_name="ATG101"
                     /note="Autophagy-related protein 101; pfam07855"
                     /db_xref="CDD:462290"
     Region          152..156
                     /region_name="Important for interaction with ATG13.
                     /evidence=ECO:0000250|UniProtKB:Q9BSB4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY69.1)"
     CDS             1..218
                     /gene="Atg101"
                     /gene_synonym="RGD1359310"
                     /coded_by="NM_001271114.1:315..971"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300240"
                     /db_xref="RGD:1359310"
ORIGIN      
        1 mncrsevlev svegrqveea mlavlhtvll hrstgkfhyk kegtysigtv giqdvdcdfi
       61 dftyvrvsse eldralrkvv gefkdalrns ggdglgqmsl efyqkkksrw pfsdecipwe
      121 vwtvkvhvva lateqerqic rekvgeklce kiinivevms rheylpkmpt qseldnvfdt
      181 glrdvqpyly kisfqiteal gtsvtttmrr likdtlal
//
LOCUS       NP_001004221             268 aa            linear   ROD 27-APR-2025
DEFINITION  ER membrane protein complex subunit 10 precursor [Rattus
            norvegicus].
ACCESSION   NP_001004221 XP_214946
VERSION     NP_001004221.2
DBSOURCE    REFSEQ: accession NM_001004221.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Reboll,M.R., Korf-Klingebiel,M., Klede,S., Polten,F., Brinkmann,E.,
            Reimann,I., Schonfeld,H.J., Bobadilla,M., Faix,J., Kensah,G.,
            Gruh,I., Klintschar,M., Gaestel,M., Niessen,H.W., Pich,A.,
            Bauersachs,J., Gogos,J.A., Wang,Y. and Wollert,K.C.
  TITLE     EMC10 (Endoplasmic Reticulum Membrane Protein Complex Subunit 10)
            Is a Bone Marrow-Derived Angiogenic Growth Factor Promoting Tissue
            Repair After Myocardial Infarction
  JOURNAL   Circulation 136 (19), 1809-1823 (2017)
   PUBMED   28931551
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Wang,X., Gong,W., Liu,Y., Yang,Z., Zhou,W., Wang,M., Yang,Z.,
            Wen,J. and Hu,R.
  TITLE     Molecular cloning of a novel secreted peptide, INM02, and
            regulation of its expression by glucose
  JOURNAL   J Endocrinol 202 (3), 355-364 (2009)
   PUBMED   19570817
  REMARK    GeneRIF: as a novel secreted protein, INM02 (MGC93975) is
            associated with functions of pancreatic islets, especially of
            beta-cells
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC079041.1.
            
            On Jun 18, 2015 this sequence version replaced NP_001004221.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079041.1, SRR26360172.652078.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..268
                     /product="ER membrane protein complex subunit 10
                     precursor"
                     /note="UPF0510 protein INM02"
                     /calculated_mol_wt=24535
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3487
     Region          62..206
                     /region_name="EMC10"
                     /note="ER membrane protein complex subunit 10 and similar
                     proteins; cd22209"
                     /db_xref="CDD:412067"
     Site            order(117,119,124,137..141,143,159,161..162,165..168,170,
                     200..206)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:412067"
     CDS             1..268
                     /gene="Emc10"
                     /gene_synonym="Inm02"
                     /coded_by="NM_001004221.2:64..870"
                     /db_xref="GeneID:292878"
                     /db_xref="RGD:1303214"
ORIGIN      
        1 malgssqrfg mvaagagvtq llvlllmvaa vpsrargsgc rvgaaargvg adgheaegcg
       61 tvalllehsf eigdganfqk rgsllwnqqd gtlsatqrql seeergrlrd vaavnglyrv
      121 rvprrpgtld gseagghvss fvpacslves hlsdqltlhv dvagnvvgls vvvypggcrg
      181 sevededlel fntsvhlrpp gtapgpetaa fierlemeqa qkaknpqeqk sffakywmyi
      241 ipvvlflmms gapdaggqgg gggggssr
//
LOCUS       NP_536323               1836 aa            linear   ROD 27-APR-2025
DEFINITION  inaD-like protein [Rattus norvegicus].
ACCESSION   NP_536323 XP_006238485
VERSION     NP_536323.1
DBSOURCE    REFSEQ: accession NM_080398.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1836)
  AUTHORS   Kim,J.Y., Song,J.Y., Karnam,S., Park,J.Y., Lee,J.J., Kim,S. and
            Cho,S.H.
  TITLE     Common and distinctive localization patterns of Crumbs polarity
            complex proteins in the mammalian eye
  JOURNAL   Gene Expr Patterns 17 (1), 31-37 (2015)
   PUBMED   25636444
REFERENCE   2  (residues 1 to 1836)
  AUTHORS   Zhang,J., Yang,X., Wang,Z., Zhou,H., Xie,X., Shen,Y. and Long,J.
  TITLE     Structure of an L27 domain heterotrimer from cell polarity complex
            Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly
            mode
  JOURNAL   J Biol Chem 287 (14), 11132-11140 (2012)
   PUBMED   22337881
  REMARK    GeneRIF: the crystal structure of a 4-L27 domain-containing
            heterotrimer derived from the tripartite complex Patj/Pals1/Mals2
REFERENCE   3  (residues 1 to 1836)
  AUTHORS   Nakajima,H. and Tanoue,T.
  TITLE     Lulu2 regulates the circumferential actomyosin tensile system in
            epithelial cells through p114RhoGEF
  JOURNAL   J Cell Biol 195 (2), 245-261 (2011)
   PUBMED   22006950
REFERENCE   4  (residues 1 to 1836)
  AUTHORS   Du,D., Xu,F., Yu,L., Zhang,C., Lu,X., Yuan,H., Huang,Q., Zhang,F.,
            Bao,H., Jia,L., Wu,X., Zhu,X., Zhang,X., Zhang,Z. and Chen,Z.
  TITLE     The tight junction protein, occludin, regulates the directional
            migration of epithelial cells
  JOURNAL   Dev Cell 18 (1), 52-63 (2010)
   PUBMED   20152177
REFERENCE   5  (residues 1 to 1836)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 1836)
  AUTHORS   Duning,K., Schurek,E.M., Schluter,M., Bayer,M., Reinhardt,H.C.,
            Schwab,A., Schaefer,L., Benzing,T., Schermer,B., Saleem,M.A.,
            Huber,T.B., Bachmann,S., Kremerskothen,J., Weide,T. and
            Pavenstadt,H.
  TITLE     KIBRA modulates directional migration of podocytes
  JOURNAL   J Am Soc Nephrol 19 (10), 1891-1903 (2008)
   PUBMED   18596123
REFERENCE   7  (residues 1 to 1836)
  AUTHORS   Wong,E.W., Mruk,D.D., Lee,W.M. and Cheng,C.Y.
  TITLE     Par3/Par6 polarity complex coordinates apical ectoplasmic
            specialization and blood-testis barrier restructuring during
            spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 105 (28), 9657-9662 (2008)
   PUBMED   18621709
REFERENCE   8  (residues 1 to 1836)
  AUTHORS   Santillan,G., Baldi,C., Katz,S., Vazquez,G. and Boland,R.
  TITLE     Evidence that TRPC3 is a molecular component of the
            1alpha,25(OH)2D3-activated capacitative calcium entry (CCE) in
            muscle and osteoblast cells
  JOURNAL   J Steroid Biochem Mol Biol 89-90 (1-5), 291-295 (2004)
   PUBMED   15225788
REFERENCE   9  (residues 1 to 1836)
  AUTHORS   Chae,T.H., Kim,S., Marz,K.E., Hanson,P.I. and Walsh,C.A.
  TITLE     The hyh mutation uncovers roles for alpha Snap in apical protein
            localization and control of neural cell fate
  JOURNAL   Nat Genet 36 (3), 264-270 (2004)
   PUBMED   14758363
  REMARK    Erratum:[Nat Genet. 2004 Apr;36(4):427]
REFERENCE   10 (residues 1 to 1836)
  AUTHORS   Lemmers,C., Medina,E., Delgrossi,M.H., Michel,D., Arsanto,J.P. and
            Le Bivic,A.
  TITLE     hINADl/PATJ, a homolog of discs lost, interacts with crumbs and
            localizes to tight junctions in human epithelial cells
  JOURNAL   J Biol Chem 277 (28), 25408-25415 (2002)
   PUBMED   11964389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 21, 2015 this sequence version replaced XP_006238485.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.15508.1,
                                           SRR26643287.13554.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1836
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q33"
     Protein         1..1836
                     /product="inaD-like protein"
                     /note="PDZ domain protein; InaD-like 2; protein associated
                     to tight junctions; pals1-associated tight junction
                     protein; channel-interacting PDZ domain-containing
                     protein"
                     /calculated_mol_wt=199337
     Region          8..65
                     /region_name="L27_2"
                     /note="pfam09045"
                     /db_xref="CDD:312549"
     Region          118..219
                     /region_name="PDZ1_MUPP1-like"
                     /note="PDZ domain 1 of multi-PDZ-domain protein 1 (MUPP1)
                     and PATJ (protein-associated tight junction), and related
                     domains; cd06689"
                     /db_xref="CDD:467176"
     Site            order(144..150,165,168,199,203,206..207)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467176"
     Region          247..326
                     /region_name="PDZ2_MUPP1-like"
                     /note="PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1)
                     and PATJ (protein-associated tight junction) and similar
                     domains; cd06667"
                     /db_xref="CDD:467155"
     Site            order(257..263,273,276,306,310,313..314)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467155"
     Region          362..451
                     /region_name="PDZ3_MUPP1-like"
                     /note="PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1)
                     and PATJ (protein-associated tight junction) and related
                     domains; cd06791"
                     /db_xref="CDD:467253"
     Site            order(375..381,398,401,431,435,438..439)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467253"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZW7; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          456..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAD2.2)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NI35; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZW7; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          555..639
                     /region_name="PDZ4_MUPP1-like"
                     /note="PDZ domain 4 of multi-PDZ-domain protein 1 (MUPP1)
                     and PATJ (protein-associated tight junction) and related
                     domains; cd06668"
                     /db_xref="CDD:467156"
     Site            order(569..575,586,589,619,623,626..627)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467156"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZW7; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          678..774
                     /region_name="PDZ5_MUPP1-like"
                     /note="PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1),
                     PATJ (protein-associated tight junction) and related
                     domains; cd06669"
                     /db_xref="CDD:467157"
     Site            order(696..702,718,721,751,755,758..759)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467157"
     Region          1073..1168
                     /region_name="PDZ7_MUPP1-PD6_PATJ-like"
                     /note="PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1),
                     PDZ domain 6 of PATJ (protein-associated tight junction)
                     and related domains; cd06671"
                     /db_xref="CDD:467159"
     Site            order(1086..1092,1113,1116,1146,1150,1153..1154)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467159"
     Region          1173..1232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAD2.2)"
     Site            1217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63ZW7; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          1245..1328
                     /region_name="PDZ8_MUPP1-PDZ7_PATJ-PDZ2_INAD-like"
                     /note="PDZ domain 8 of multi-PDZ-domain protein 1 (MUPP1),
                     PDZ domain 7 of protein-associated tight junction (PATJ),
                     PDZ domain 2 of Drosophila melanogaster
                     inactivation-no-after-potential D (INAD), and related
                     domains; cd06672"
                     /db_xref="CDD:467160"
     Site            order(1256..1262,1275,1278,1308,1312,1315..1316)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467160"
     Region          1341..1448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          1400..1470
                     /region_name="MPDZ_u10"
                     /note="Unstructured region 10 on multiple PDZ protein;
                     pfam16667"
                     /db_xref="CDD:435500"
     Region          1470..1555
                     /region_name="PDZ10_MUPP1-PDZ8_PATJ-like"
                     /note="PDZ domain 10 of multi-PDZ-domain protein 1
                     (MUPP1), domain 8 of PATJ (protein-associated tight
                     junction) and similar domains; cd06673"
                     /db_xref="CDD:467161"
     Site            order(1483..1489,1502,1505,1535,1539,1542..1543)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467161"
     Site            1545
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8NI35; propagated from
                     UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          1566..1652
                     /region_name="PDZ11_MUPP1-PDZ9_PATJ-like"
                     /note="PDZ domain 11 of MUPP1 of multi-PDZ-domain protein
                     1 (MUPP1), domain 9 of PATJ (protein-associated tight
                     junction) and related domains; cd06674"
                     /db_xref="CDD:467162"
     Site            order(1580..1586,1597,1600,1630,1634,1637..1638)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467162"
     Region          1657..1678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAD2.2)"
     Region          1710..1795
                     /region_name="PDZ12_MUPP1-like"
                     /note="PDZ domain 12 of multi-PDZ-domain protein 1
                     (MUPP1), PDZ domain 10 of protein-associated tight
                     junction (PATJ, and related domains; cd06675"
                     /db_xref="CDD:467163"
     Site            order(1721..1727,1742,1745,1775,1779,1782..1783)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467163"
     Region          1813..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1MAD2.2)"
     CDS             1..1836
                     /gene="Patj"
                     /gene_synonym="Inadl; Inadl2; RGD1565362"
                     /coded_by="NM_080398.1:113..5623"
                     /db_xref="GeneID:140581"
                     /db_xref="RGD:1565362"
ORIGIN      
        1 mpenpaaekm qvlqvldrlr gklqekgdtt qneklsafye tlksplfnqi ltlqqsikql
       61 kgqlshipsd csanfdfsrk gllvftdgsi tngnahrpcs sitaseslpw tqrsgnedft
      121 sviqqmaqgr hieyidierp stgglgfsvv alrsqslgli difvkevhpg svadrdqrlk
      181 endqilaind tpldqnishq qaiallqqat gslrlvvare vghtqsrtst ssadttlpet
      241 vrwghtedve lindgsglgf givggkssgv vvrtivpggl adrdgrlqtg dhilkigstn
      301 vqgmtseqva qvlrncgnsv rmlvardpvg eiavtpptpa slpvalpvva trtlgsdssp
      361 fetynvelvk kdgqslgiri vgyvgtahpg easgiyvksi ipgsaayhng qiqvndkiva
      421 vdgvniqgfa nqdvvevlrn agqvvhltlv rrktslsasp feqpssreav aeppevpelt
      481 gslkpetnsr meaeeigerl dnlrkdtvqa lekpdvyped ipgcpenelk srwenllgpd
      541 yevmvatldt qiaddeelqk yskllpihtl rlgmevdsfd ghhyissiap ggpvdtlnll
      601 qpedellevn gvqlygksrr eavsflkevp ppftlvccrr lfddeasvde prtvepslle
      661 aevdrsvdvs tedddgelal wspevktvel vkdckglgfs ildyqdpldp mrsvivirsl
      721 vadgvaersg ellpgdrlvs vnefsldnat laeavevlka vppgvvhlgi ckplveeeke
      781 ekeehfifhs nnngdnsesp etvheihssl ileapqgfrd epyleelvde pfldlgkslq
      841 fqqkdmdsss eawemhefls prlerrgeer emlvdeeyei yqdrlrdmea hpppphirep
      901 tsasprldlq agpqwlhadl sggeilechd tesmmtaypq emqdysfstt dmmketfgld
      961 srppmpsseg ngqhgrfddl ehlhslvshg ldlgmmtpsd lqgpgvlvdl pavtqrreqe
     1021 elplyrlpsa rvvtkpsshv gmvssrhana acelpereeg egeetpnfsh wgppriveif
     1081 repnvslgis ivggqtvikr lkngeelkgi fikqvledsp agktkalktg dkilevsgvd
     1141 lqnashaeav eaiksagnpv vfvvqslsst prvipsvnnk gktppqnqdq ntqekkakrh
     1201 gtapppmklp ppyrapsadt eeseedsalt dkkirqryad lpgelhiiel ekdknglgls
     1261 lagnkdrsrm sifvvginpd gpaaadgrmr vgdelleinn qilygrshqn asaiiktapt
     1321 rvklvfirne davnqmavap fpvpshspsp vedlggtepv sseedssvda kplperessk
     1381 pedltqavdd smvaeqekas espdsaarqm kqpgysaqvs sssqeipsap aplcqsthad
     1441 vtgsgnfqap lsvdpaplsv dpatcpivpg qemiieiskg rsglglsivg gkdtpldaiv
     1501 ihevyeegaa ardgrlwagd qilevngvdl rsssheeait alrqtpqkvr lviyrdeaqy
     1561 rdeenlevfl vdlqkktgrg lglsivgkrs gsgvfisdiv kggaadldgr lirgdqilsv
     1621 ngedvrqasq etvatilkcv qglvqleigr lragswassr ktsqnsqgdq hsahsscrps
     1681 fapvitslqn lvgtkrssdp pqkcteeepr tveiirelsd algvsiaggk gsplgdipif
     1741 iamiqangva artqklkvgd rivsingqpl dglshtdavn llknafgrii lqvvadtnis
     1801 aiatqlemms agsqlgspta drhpqdpeel lqrtad
//
LOCUS       NP_001257495             497 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3D [Rattus norvegicus].
ACCESSION   NP_001257495
VERSION     NP_001257495.1
DBSOURCE    REFSEQ: accession NM_001270566.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, DQ112342.1 and
            BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (4) is alternatively spliced at
            the 3' end compared to variant 1, which results in a frame-shift,
            and a longer isoform (H3D) containing 6 transmembrane domains and a
            distinct C-terminus compared to isoform H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ112342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132300, SAMD00132302
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..497
                     /product="histamine H3 receptor isoform H3D"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=54091
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          48..395
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          70..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          234..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          286..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     Region          357..379
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            360..380
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYN8.1)"
     CDS             1..497
                     /gene="Hrh3"
                     /coded_by="NM_001270566.1:338..1831"
                     /note="isoform H3D is encoded by transcript variant 4"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhrygvgea gpgveageaa lgggsgggaa
      301 asptsssgss srgterprsl krgskpsass aslekrmkmv sqsitqrfrl srdkkvaksl
      361 aiivsifglc wapytllmii raachgrcip dycverlgkl easlllplwm fsgrwrrrkh
      421 vceldvpwmf nqerqncrga rgwigrcglp rpppsvlqlp aeprqlllpa pppglgrwpc
      481 pacpvctiri wgwvvmg
//
LOCUS       NP_775117                508 aa            linear   ROD 27-APR-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_775117
VERSION     NP_775117.2
DBSOURCE    REFSEQ: accession NM_173094.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wang,Y., Ping,L.F., Bai,F.Y., Zhang,X.H. and Li,G.H.
  TITLE     Hmgcs2 is the hub gene in diabetic cardiomyopathy and is negatively
            regulated by Hmgcs2, promoting high glucose-induced cardiomyocyte
            injury
  JOURNAL   Immun Inflamm Dis 12 (3), e1191 (2024)
   PUBMED   38477658
  REMARK    GeneRIF: Hmgcs2 is the hub gene in diabetic cardiomyopathy and is
            negatively regulated by Hmgcs2, promoting high glucose-induced
            cardiomyocyte injury.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Tan,W., Bao,H., Liu,Z., Liu,Y., Hong,L. and Shao,L.
  TITLE     Protein PDK4 Interacts with HMGCS2 to Facilitate High
            Glucoseinduced Myocardial Injuries
  JOURNAL   Curr Mol Med 23 (10), 1104-1115 (2023)
   PUBMED   36281857
  REMARK    GeneRIF: Protein PDK4 Interacts with HMGCS2 to Facilitate High
            Glucoseinduced Myocardial Injuries.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Su,S.G., Yang,M., Zhang,M.F., Peng,Q.Z., Li,M.Y., Liu,L.P. and
            Bao,S.Y.
  TITLE     miR-107-mediated decrease of HMGCS2 indicates poor outcomes and
            promotes cell migration in hepatocellular carcinoma
  JOURNAL   Int J Biochem Cell Biol 91 (Pt A), 53-59 (2017)
   PUBMED   28867541
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Wang,F., Xiang,H., Fischer,G., Liu,Z., Dupont,M.J., Hogan,Q.H. and
            Yu,H.
  TITLE     HMG-CoA synthase isoenzymes 1 and 2 localize to satellite glial
            cells in dorsal root ganglia and are differentially regulated by
            peripheral nerve injury
  JOURNAL   Brain Res 1652, 62-70 (2016)
   PUBMED   27671501
  REMARK    GeneRIF: Results identify 3-hydroxy-3-methylglutaryl coenzyme A
            synthase isoenzymes 1 and 2 as the alternative markers for
            satellite glial cells (SGCs) in dorsal root ganglia (DRGs).
            Downregulated HMGCS1 expression in DRGs after spinal nerve injury
            may reflect a potential role of abnormal sterol metabolism of SGCs
            in the nerve injured-induced neuropathic pain.
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Martin,J., Balmer,M.L., Rajendran,S., Maurhofer,O., Dufour,J.F. and
            St-Pierre,M.V.
  TITLE     Nutritional stress exacerbates hepatic steatosis induced by
            deletion of the histidine nucleotide-binding (Hint2) mitochondrial
            protein
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 310 (7), G497-G509 (2016)
   PUBMED   26767982
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Serra,D., Casals,N., Asins,G., Royo,T., Ciudad,C.J. and
            Hegardt,F.G.
  TITLE     Regulation of mitochondrial 3-hydroxy-3-methylglutaryl-coenzyme A
            synthase protein by starvation, fat feeding, and diabetes
  JOURNAL   Arch Biochem Biophys 307 (1), 40-45 (1993)
   PUBMED   7902069
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Ayte,J., Gil-Gomez,G. and Hegardt,F.G.
  TITLE     Methylation of the regulatory region of the mitochondrial
            3-hydroxy-3-methylglutaryl-CoA synthase gene leads to its
            transcriptional inactivation
  JOURNAL   Biochem J 295 (Pt 3) (Pt 3), 807-812 (1993)
   PUBMED   7694571
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Quant,P.A., Tubbs,P.K. and Brand,M.D.
  TITLE     Glucagon activates mitochondrial 3-hydroxy-3-methylglutaryl-CoA
            synthase in vivo by decreasing the extent of succinylation of the
            enzyme
  JOURNAL   Eur J Biochem 187 (1), 169-174 (1990)
   PUBMED   1967579
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Patel,T.B. and Clark,J.B.
  TITLE     Acetoacetate metabolism in rat brain. Development of
            acetoacetyl-coenzyme A deacylase and
            3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochem J 176 (3), 951-958 (1978)
   PUBMED   34385
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083543.1.
            
            On Aug 16, 2012 this sequence version replaced NP_775117.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083543.1, M33648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..508
                     /product="hydroxymethylglutaryl-CoA synthase,
                     mitochondrial precursor"
                     /EC_number="2.3.3.10"
                     /note="hydroxymethylglutaryl-CoA synthase 2;
                     hydroxymethylglutaryl-CoA synthase, mitochondrial; HMG-CoA
                     synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase;
                     3-hydroxy-3-methylglutary-Coenzyme A synthase 2;
                     3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2
                     (mitochondrial); 3-hydroxy-3-methylglutaryl-CoA synthase 2
                     (mitochondrial)"
                     /calculated_mol_wt=52689
     transit_peptide 1..37
                     /note="Mitochondrion. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P22791.2)"
                     /calculated_mol_wt=4215
     mat_peptide     38..508
                     /product="Hydroxymethylglutaryl-CoA synthase,
                     mitochondrial. /id=PRO_0000013486"
                     /note="propagated from UniProtKB/Swiss-Prot (P22791.2)"
                     /calculated_mol_wt=52689
     Region          50..506
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            83
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            243
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            256
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            306
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            310
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            327
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            342
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            350
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            354
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            358
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            427
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54868; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            437
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            447
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            473
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P54869; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P22791.2)"
     CDS             1..508
                     /gene="Hmgcs2"
                     /gene_synonym="Hmgcs1; Mt3h3mg"
                     /coded_by="NM_173094.2:32..1558"
                     /db_xref="GeneID:24450"
                     /db_xref="RGD:2804"
ORIGIN      
        1 mqrllaparr vlqvkrvmqe sslspahllp aaqqrfstip paplaktdtw pkdvgilale
       61 vyfpaqyvdq tdlekfnnve agkytvglgq trmgfcsvqe dinslcltvv qrlmertklp
      121 wdavgrlevg tetiidkska vktvlmelfq dsgntdiegi dttnacyggt aslfnaanwm
      181 essywdgrya lvvcgdiavy psgnarptgg agavamligp kaplvleqgl rgthmenayd
      241 fykpnlasey plvdgklsiq cylraldrcy aayrrkiqnq wkqagnnqpf tlddvqymif
      301 htpfckmvqk slarlmfndf lssssdkqnn lykgleafkg lkleetytnk dvdkallkas
      361 ldmfnkktka slylstnngn mytsslygcl asllshhsaq elagsrigaf sygsglaasf
      421 fsfrvskdas pgspleklvs svsdlpkrld srrrmspeef teimnqreqf yhkvnfsppg
      481 dtsnlfpgtw ylervdemhr rkyarrpv
//
LOCUS       NP_114445                703 aa            linear   ROD 27-APR-2025
DEFINITION  antigen peptide transporter 2 [Rattus norvegicus].
ACCESSION   NP_114445 XP_003751977 XP_006256094
VERSION     NP_114445.2
DBSOURCE    REFSEQ: accession NM_032056.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Tuncel,J., Haag,S., Yau,A.C., Norin,U., Baud,A., Lonnblom,E.,
            Maratou,K., Ytterberg,A.J., Ekman,D., Thordardottir,S.,
            Johannesson,M., Gillett,A., Stridh,P., Jagodic,M., Olsson,T.,
            Fernandez-Teruel,A., Zubarev,R.A., Mott,R., Aitman,T.J., Flint,J.
            and Holmdahl,R.
  CONSRTM   EURATRANS Consortium
  TITLE     Natural polymorphisms in Tap2 influence negative selection and
            CD4ratioCD8 lineage commitment in the rat
  JOURNAL   PLoS Genet 10 (2), e1004151 (2014)
   PUBMED   24586191
  REMARK    GeneRIF: Variants of Tap2 have previously been shown to influence
            the antigenicity of MHC class I molecules . Our results show that a
            restricted peptide repertoire on MHC class I molecules leads to
            reduced negative selection of CD8SP cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Kim,J.H., Park,B.L., Pasaje,C.F., Bae,J.S., Park,J.S., Park,S.W.,
            Uh,S.T., Kim,M.K., Choi,I.S., Cho,S.H., Choi,B.W., Park,C.S. and
            Shin,H.D.
  TITLE     Genetic association analysis of TAP1 and TAP2 polymorphisms with
            aspirin exacerbated respiratory disease and its FEV1 decline
  JOURNAL   J Hum Genet 56 (9), 652-659 (2011)
   PUBMED   21796142
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Feng,M., Yin,B., Shen,T., Ma,Q., Liu,L., Zheng,J., Zhao,Y., Qian,K.
            and Liu,D.
  TITLE     TAP1 and TAP2 polymorphisms associated with ankylosing spondylitis
            in genetically homogenous Chinese Han population
  JOURNAL   Hum Immunol 70 (4), 257-261 (2009)
   PUBMED   19480848
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Liu,Q., Hao,C., Su,P. and Shi,J.
  TITLE     Down-regulation of HLA class I antigen-processing machinery
            components in esophageal squamous cell carcinomas: association with
            disease progression
  JOURNAL   Scand J Gastroenterol 44 (8), 960-969 (2009)
   PUBMED   19492245
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Masserano,G., Montanaro,M., Poggi,G., Rusca,L. and Vignali,F.
  TITLE     [Rehabilitative evaluation of 18 cases of anterior cruciate
            ligament lesions surgically treated by the Kenneth-Jones technique]
  JOURNAL   Minerva Med 83 (12 Suppl 1), 89-91 (1992)
   PUBMED   1300480
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Powis,S.J., Deverson,E.V., Coadwell,W.J., Ciruela,A.,
            Huskisson,N.S., Smith,H., Butcher,G.W. and Howard,J.C.
  TITLE     Effect of polymorphism of an MHC-linked transporter on the peptides
            assembled in a class I molecule
  JOURNAL   Nature 357 (6375), 211-215 (1992)
   PUBMED   1350326
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Attaya,M., Jameson,S., Martinez,C.K., Hermel,E., Aldrich,C.,
            Forman,J., Lindahl,K.F., Bevan,M.J. and Monaco,J.J.
  TITLE     Ham-2 corrects the class I antigen-processing defect in RMA-S cells
  JOURNAL   Nature 355 (6361), 647-649 (1992)
   PUBMED   1538753
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Kelly,A., Powis,S.H., Kerr,L.A., Mockridge,I., Elliott,T.,
            Bastin,J., Uchanska-Ziegler,B., Ziegler,A., Trowsdale,J. and
            Townsend,A.
  TITLE     Assembly and function of the two ABC transporter proteins encoded
            in the human major histocompatibility complex
  JOURNAL   Nature 355 (6361), 641-644 (1992)
   PUBMED   1538751
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Caillat-Zucman,S., Bertin,E., Timsit,J., Boitard,C., Assan,R. and
            Bach,J.F.
  TITLE     TAP1 and TAP2 transporter genes and predisposition to insulin
            dependent diabetes mellitus
  JOURNAL   C R Acad Sci III 315 (13), 535-539 (1992)
   PUBMED   1300236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X63854.1 and BC091140.1.
            
            On or before Dec 15, 2013 this sequence version replaced
            XP_006256094.1, XP_003751977.1, NP_114445.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X75305.1, X75306.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..703
                     /product="antigen peptide transporter 2"
                     /EC_number="7.4.2.14"
                     /note="APT2; ATP-binding cassette sub-family B member 3;
                     Transporter 2 ABC (ATP binding cassette); transporter 2
                     ATP-binding cassette sub-family B; transporter 2,
                     ATP-binding cassette, sub-family B (MDR/TAP)"
                     /calculated_mol_wt=77620
     Region          1..697
                     /region_name="3a01208"
                     /note="Conjugate Transporter-2 (CT2) Family protein;
                     TIGR00958"
                     /db_xref="CDD:273363"
     CDS             1..703
                     /gene="Tap2"
                     /gene_synonym="Abcb3; Cim"
                     /coded_by="NM_032056.3:90..2201"
                     /db_xref="GeneID:24812"
                     /db_xref="RGD:3818"
ORIGIN      
        1 malsyprpwa slllvdlall gllqrslgtl lppglpglwl egtlrlgvlw gllkvggllr
       61 lvgtflpllc lttplffslr alvgstmsts vlrvasaswg wllagyvaaa lslavwavls
      121 pagaqekepg qennralmir llrlskpdlp flivafifla mavwgetlip hysgrvidil
      181 ggdfdpdafa saiffmclfs vgsslsagcr ggsflftmsr inlrireqlf ssllrqdlaf
      241 fqetktgeln srlssdtslm srwlpfnani llrslvkvvg lyyfmlqvsp rltflslldl
      301 pltiaaekvy nprhqavlke iqdvvakagq vvreavgglq tvrsfgaeeq evsrykeale
      361 rcrqlwwrrd lekelylvir rvmalgmqvl ilncgvqqil agevtrggll sfllyqeevg
      421 hhvrnlvymy gdmlsnvgaa ekvfsyldrr pnlpkpgtla pprvegrvef qdvsfsypsr
      481 pekpvlqglt ftlhpgkvta lvgpngsgks tvaallqnly qptggkvlld geplvqydhh
      541 ylhrqvvlvg qepvlfsgsv kdniayglrn cedaqvmaaa qaacaddfig emtngintei
      601 gergsqlavg qkqrlaiara lvrnprvlil deatsaldae ceqalqtwrs qedrtmlvia
      661 hrlhtvqnad qvlvlkqgql vehdqlrdeq dvyahlvqqr lea
//
LOCUS       NP_001009720             221 aa            linear   ROD 27-APR-2025
DEFINITION  serine/arginine-rich splicing factor 2 [Rattus norvegicus].
ACCESSION   NP_001009720
VERSION     NP_001009720.1
DBSOURCE    REFSEQ: accession NM_001009720.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kiefer,K.C., Cremer,S., Pardali,E., Assmus,B., Abou-El-Ardat,K.,
            Kirschbaum,K., Dorsheimer,L., Rasper,T., Berkowitsch,A., Serve,H.,
            Dimmeler,S., Zeiher,A.M. and Rieger,M.A.
  TITLE     Full spectrum of clonal haematopoiesis-driver mutations in chronic
            heart failure and their associations with mortality
  JOURNAL   ESC Heart Fail 8 (3), 1873-1884 (2021)
   PUBMED   33779075
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Zhang,C., Shen,L., Yuan,W., Liu,Y., Guo,R., Luo,Y., Zhan,Z.,
            Xie,Z., Wu,G., Wu,W. and Feng,Y.
  TITLE     Loss of SRSF2 triggers hepatic progenitor cell activation and tumor
            development in mice
  JOURNAL   Commun Biol 3 (1), 210 (2020)
   PUBMED   32372053
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Wang,P., Guo,L., Li,K., Ning,S., Shi,W., Liu,Z. and Chen,Y.
  TITLE     Serine/arginine rich splicing factor 2 expression and clinic
            pathological features indicating a prognostic factor in human
            hepatocellular carcinoma patients
  JOURNAL   Cancer Biomark 21 (3), 681-687 (2018)
   PUBMED   29278882
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Luo,C., Cheng,Y., Liu,Y., Chen,L., Liu,L., Wei,N., Xie,Z., Wu,W.
            and Feng,Y.
  TITLE     SRSF2 Regulates Alternative Splicing to Drive Hepatocellular
            Carcinoma Development
  JOURNAL   Cancer Res 77 (5), 1168-1178 (2017)
   PUBMED   28082404
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Derlig,K., Giessl,A., Brandstatter,J.H., Enz,R. and Dahlhaus,R.
  TITLE     Special characteristics of the transcription and splicing machinery
            in photoreceptor cells of the mammalian retina
  JOURNAL   Cell Tissue Res 362 (2), 281-294 (2015)
   PUBMED   26013685
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Xu,G.M. and Arnaout,M.A.
  TITLE     WAC, a novel WW domain-containing adapter with a coiled-coil
            region, is colocalized with splicing factor SC35
  JOURNAL   Genomics 79 (1), 87-94 (2002)
   PUBMED   11827461
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Muralikrishna,B., Dhawan,J., Rangaraj,N. and Parnaik,V.K.
  TITLE     Distinct changes in intranuclear lamin A/C organization during
            myoblast differentiation
  JOURNAL   J Cell Sci 114 (Pt 22), 4001-4011 (2001)
   PUBMED   11739632
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Berke,J.D., Sgambato,V., Zhu,P.P., Lavoie,B., Vincent,M., Krause,M.
            and Hyman,S.E.
  TITLE     Dopamine and glutamate induce distinct striatal splice forms of
            Ania-6, an RNA polymerase II-associated cyclin
  JOURNAL   Neuron 32 (2), 277-287 (2001)
   PUBMED   11683997
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Potter,G.B., Beaudoin,G.M. 3rd, DeRenzo,C.L., Zarach,J.M.,
            Chen,S.H. and Thompson,C.C.
  TITLE     The hairless gene mutated in congenital hair loss disorders encodes
            a novel nuclear receptor corepressor
  JOURNAL   Genes Dev 15 (20), 2687-2701 (2001)
   PUBMED   11641275
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Sahlas,D.J., Milankov,K., Park,P.C. and De Boni,U.
  TITLE     Distribution of snRNPs, splicing factor SC-35 and actin in
            interphase nuclei: immunocytochemical evidence for differential
            distribution during changes in functional states
  JOURNAL   J Cell Sci 105 (Pt 2), 347-357 (1993)
   PUBMED   8408269
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC058508.1, SRR26643287.26220.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840108, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.2"
     Protein         1..221
                     /product="serine/arginine-rich splicing factor 2"
                     /note="SC-35; splicing factor SC35; splicing component, 35
                     kDa; splicing factor, arginine/serine-rich 2"
                     /calculated_mol_wt=25345
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Region          16..88
                     /region_name="RRM_SRSF2_SRSF8"
                     /note="RNA recognition motif (RRM) found in
                     serine/arginine-rich splicing factor SRSF2, SRSF8 and
                     similar proteins; cd12311"
                     /db_xref="CDD:409751"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Region          92..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01130; propagated from
                     UniProtKB/Swiss-Prot (Q6PDU1.3)"
     CDS             1..221
                     /gene="Srsf2"
                     /gene_synonym="Sfrs2"
                     /coded_by="NM_001009720.2:164..829"
                     /db_xref="GeneID:494445"
                     /db_xref="RGD:1359422"
ORIGIN      
        1 msygrpppdv egmtslkvdn ltyrtspdtl rrvfekygrv gdvyiprdry tkesrgfafv
       61 rfhdkrdaed amdamdgavl dgrelrvqma rygrppdshh srrgppprry ggggygrrsr
      121 sprrrrrsrs rsrsrsrsrs rsrysrsksr srtrsrsrst sksrsarrsk sksssvsrsr
      181 srsrsrsrsr spppvskres ksrsrskspp kspeeegavs s
//
LOCUS       NP_001166906             172 aa            linear   ROD 27-APR-2025
DEFINITION  hereditary hemochromatosis protein homolog isoform 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_001166906
VERSION     NP_001166906.1
DBSOURCE    REFSEQ: accession NM_001173435.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Tamosauskaite,J., Atkins,J.L., Pilling,L.C., Kuo,C.L., Kuchel,G.A.,
            Ferrucci,L. and Melzer,D.
  TITLE     Hereditary Hemochromatosis Associations with Frailty, Sarcopenia
            and Chronic Pain: Evidence from 200,975 Older UK Biobank
            Participants
  JOURNAL   J Gerontol A Biol Sci Med Sci 74 (3), 337-342 (2019)
   PUBMED   30657865
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Smith,D.J., Klein,K., Hartel,G., Wainwright,C.E., Bell,S.C.,
            Anderson,G.J. and Reid,D.W.
  TITLE     Mutations in the HFE gene can be associated with increased lung
            disease severity in cystic fibrosis
  JOURNAL   Gene 683, 12-17 (2019)
   PUBMED   30291871
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Pilling,L.C., Tamosauskaite,J., Jones,G., Wood,A.R., Jones,L.,
            Kuo,C.L., Kuchel,G.A., Ferrucci,L. and Melzer,D.
  TITLE     Common conditions associated with hereditary haemochromatosis
            genetic variants: cohort study in UK Biobank
  JOURNAL   BMJ 364, k5222 (2019)
   PUBMED   30651232
  REMARK    Erratum:[BMJ. 2019 Oct 23;367:l6157. doi: 10.1136/bmj.l6157. PMID:
            31645331]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Frydlova,J., Rogalsky,D.W., Truksa,J., Traeger,L.,
            Steinbicker,A.U., Vokurka,M. and Krijt,J.
  TITLE     Liver HFE protein content is posttranscriptionally decreased in
            iron-deficient mice and rats
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 315 (4), G560-G568 (2018)
   PUBMED   29927322
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Lee,N.P., Wu,H., Ng,K.T.P., Luo,R., Lam,T.W., Lo,C.M. and Man,K.
  TITLE     Transcriptome Analysis of Acute Phase Liver Graft Injury in Liver
            Transplantation
  JOURNAL   Biomedicines 6 (2), 41 (2018)
   PUBMED   29642405
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Sanchez,M., Queralt,R., Bruguera,M., Rodes,J. and Oliva,R.
  TITLE     Cloning, sequencing and characterization of the rat hereditary
            hemochromatosis promoter: comparison of the human, mouse and rat
            HFE promoter regions
  JOURNAL   Gene 225 (1-2), 77-87 (1998)
   PUBMED   9931446
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Lebron,J.A., Bennett,M.J., Vaughn,D.E., Chirino,A.J., Snow,P.M.,
            Mintier,G.A., Feder,J.N. and Bjorkman,P.J.
  TITLE     Crystal structure of the hemochromatosis protein HFE and
            characterization of its interaction with transferrin receptor
  JOURNAL   Cell 93 (1), 111-123 (1998)
   PUBMED   9546397
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Feder,J.N., Penny,D.M., Irrinki,A., Lee,V.K., Lebron,J.A.,
            Watson,N., Tsuchihashi,Z., Sigal,E., Bjorkman,P.J. and
            Schatzman,R.C.
  TITLE     The hemochromatosis gene product complexes with the transferrin
            receptor and lowers its affinity for ligand binding
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1472-1477 (1998)
   PUBMED   9465039
REFERENCE   9  (residues 1 to 172)
  AUTHORS   George,D.K., Goldwurm,S., MacDonald,G.A., Cowley,L.L., Walker,N.I.,
            Ward,P.J., Jazwinska,E.C. and Powell,L.W.
  TITLE     Increased hepatic iron concentration in nonalcoholic
            steatohepatitis is associated with increased fibrosis
  JOURNAL   Gastroenterology 114 (2), 311-318 (1998)
   PUBMED   9453491
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Feder,J.N., Gnirke,A., Thomas,W., Tsuchihashi,Z., Ruddy,D.A.,
            Basava,A., Dormishian,F., Domingo,R. Jr., Ellis,M.C., Fullan,A.,
            Hinton,L.M., Jones,N.L., Kimmel,B.E., Kronmal,G.S., Lauer,P.,
            Lee,V.K., Loeb,D.B., Mapa,F.A., McClelland,E., Meyer,N.C.,
            Mintier,G.A., Moeller,N., Moore,T., Morikang,E., Prass,C.E.,
            Quintana,L., Starnes,S.M., Schatzman,R.C., Brunke,K.J.,
            Drayna,D.T., Risch,N.J., Bacon,B.R. and Wolff,R.K.
  TITLE     A novel MHC class I-like gene is mutated in patients with
            hereditary haemochromatosis
  JOURNAL   Nat Genet 13 (4), 399-408 (1996)
   PUBMED   8696333
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons compared to variant 1. The resulting protein (isoform 3) is
            shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF176535.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p11"
     Protein         1..172
                     /product="hereditary hemochromatosis protein homolog
                     isoform 3 precursor"
                     /note="hereditary hemochromatosis protein homolog;
                     RT1-CAFE"
                     /calculated_mol_wt=16256
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2774
     Region          31..122
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          46..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409612"
     Region          61..65
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409612"
     Region          93..97
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409612"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409612"
     Region          119..122
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409612"
     CDS             1..172
                     /gene="Hfe"
                     /coded_by="NM_001173435.1:81..599"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:29199"
                     /db_xref="RGD:2793"
ORIGIN      
        1 mdrsaglpvr llllllllll wsvapqalrp vptlvkvtrh wastgtslrc qalnffpqni
       61 tmrwlkdsqp ldakdvnpen vlpngdgtyq gwltlavapg eetrfscqve hpgldqplta
      121 twepsrsqdm iigiisgiti caiffvgili lvlrkrkvsg gtmgdyvlte ce
//
LOCUS       NP_001153211             221 aa            linear   ROD 27-APR-2025
DEFINITION  glutathione S-transferase alpha-5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001153211
VERSION     NP_001153211.1
DBSOURCE    REFSEQ: accession NM_001159739.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Xiao,Y., Zhang,Z., Fu,Y., Shan,H., Cui,S. and Wu,J.
  TITLE     GSTA3 regulates TGF-beta1-induced renal interstitial fibrosis in
            NRK-52E cells as a component of the PI3K-Keap1/Nrf2 pathway
  JOURNAL   J Int Med Res 47 (11), 5787-5801 (2019)
   PUBMED   31617428
  REMARK    GeneRIF: The PI3K-KEAP1/Nrf2-GSTA3 signaling pathway is a possible
            mechanism of resisting external stimulation of renal fibrosis
            factors.
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Chen,H., Gan,Q., Yang,C., Peng,X., Qin,J., Qiu,S., Jiang,Y., Tu,S.,
            He,Y., Li,S., Yang,H., Tao,L. and Peng,Y.
  TITLE     A novel role of glutathione S-transferase A3 in inhibiting hepatic
            stellate cell activation and rat hepatic fibrosis
  JOURNAL   J Transl Med 17 (1), 280 (2019)
   PUBMED   31443720
  REMARK    GeneRIF: GSTA3 inhibited hepatic stellate cell activation and liver
            fibrosis
            Erratum:[J Transl Med. 2020 Apr 30;18(1):182. doi:
            10.1186/s12967-020-02346-4. PMID: 32354374]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Xiao,Y., Liu,J., Peng,Y., Xiong,X., Huang,L., Yang,H., Zhang,J. and
            Tao,L.
  TITLE     GSTA3 Attenuates Renal Interstitial Fibrosis by Inhibiting
            TGF-Beta-Induced Tubular Epithelial-Mesenchymal Transition and
            Fibronectin Expression
  JOURNAL   PLoS One 11 (9), e0160855 (2016)
   PUBMED   27602565
  REMARK    GeneRIF: Protein and mRNA expression of GSTA3 in UUO rats and
            NRK-52E cells were determined by Western blot and RT-PCR. siRNA and
            overexpression plasmid were transfected specifically to assess the
            role of GSTA3 in renal interstitial fibrosis
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Ilic,Z., Crawford,D., Vakharia,D., Egner,P.A. and Sell,S.
  TITLE     Glutathione-S-transferase A3 knockout mice are sensitive to acute
            cytotoxic and genotoxic effects of aflatoxin B1
  JOURNAL   Toxicol Appl Pharmacol 242 (3), 241-246 (2010)
   PUBMED   19850059
  REMARK    Erratum:[Toxicol Appl Pharmacol. 2010 Jun 1;245(2):280. doi:
            10.1016/j.taap.2010.03.018. PMID: 20852735]
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Caruana,G., Cullen-McEwen,L., Nelson,A.L., Kostoulias,X., Woods,K.,
            Gardiner,B., Davis,M.J., Taylor,D.F., Teasdale,R.D., Grimmond,S.M.,
            Little,M.H. and Bertram,J.F.
  TITLE     Spatial gene expression in the T-stage mouse metanephros
  JOURNAL   Gene Expr Patterns 6 (8), 807-825 (2006)
   PUBMED   16545622
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Pulford,D.J. and Hayes,J.D.
  TITLE     Characterization of the rat glutathione S-transferase Yc2 subunit
            gene, GSTA5: identification of a putative antioxidant-responsive
            element in the 5'-flanking region of rat GSTA5 that may mediate
            chemoprotection against aflatoxin B1
  JOURNAL   Biochem J 318 (Pt 1) (Pt 1), 75-84 (1996)
   PUBMED   8761455
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Hayes,J.D., Nguyen,T., Judah,D.J., Petersson,D.G. and Neal,G.E.
  TITLE     Cloning of cDNAs from fetal rat liver encoding glutathione
            S-transferase Yc polypeptides. The Yc2 subunit is expressed in
            adult rat liver resistant to the hepatocarcinogen aflatoxin B1
  JOURNAL   J Biol Chem 269 (32), 20707-20717 (1994)
   PUBMED   8051171
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Klinga-Levan,K., Andersson,A., Hanson,C., Ridderstrom,M.,
            Stenberg,G., Mannervik,B., Vajdy,M., Szpirer,J., Szpirer,C. and
            Levan,G.
  TITLE     Mapping of glutathione transferase (GST) genes in the rat
  JOURNAL   Hereditas 119 (3), 285-296 (1993)
   PUBMED   8144363
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Hayes,J.D., Judah,D.J., McLellan,L.I., Kerr,L.A., Peacock,S.D. and
            Neal,G.E.
  TITLE     Ethoxyquin-induced resistance to aflatoxin B1 in the rat is
            associated with the expression of a novel alpha-class glutathione
            S-transferase subunit, Yc2, which possesses high catalytic activity
            for aflatoxin B1-8,9-epoxide
  JOURNAL   Biochem J 279 (Pt 2) (Pt 2), 385-398 (1991)
   PUBMED   1953636
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Pickett,C.B., Telakowski-Hopkins,C.A., Ding,G.J., Argenbright,L.
            and Lu,A.Y.
  TITLE     Rat liver glutathione S-transferases. Complete nucleotide sequence
            of a glutathione S-transferase mRNA and the regulation of the Ya,
            Yb, and Yc mRNAs by 3-methylcholanthrene and phenobarbital
  JOURNAL   J Biol Chem 259 (8), 5182-5188 (1984)
   PUBMED   6325423
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the Celera
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ219557.1, FQ231428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q13"
     Protein         1..221
                     /product="glutathione S-transferase alpha-5 isoform 1"
                     /EC_number="2.5.1.18"
                     /note="glutathione S-transferase alpha-5; GST Yc2; GST
                     A5-5; glutathione S-transferase Yc2 subunit; glutathione
                     S-transferase A3"
                     /calculated_mol_wt=25216
     Region          4..82
                     /region_name="GST_N_Alpha"
                     /note="GST_N family, Class Alpha subfamily; GSTs are
                     cytosolic dimeric proteins involved in cellular
                     detoxification by catalyzing the conjugation of
                     glutathione (GSH) with a wide range of endogenous and
                     xenobiotic alkylating agents, including carcinogens;
                     cd03077"
                     /db_xref="CDD:239375"
     Site            order(11,13,15,17..18,21,24..25,32,36,69,72..73)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Site            order(45,54..55,67..68)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:239375"
     Site            order(52..53,61,66..67,69..70,73..74,78)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239375"
     Region          86..220
                     /region_name="GST_C_Alpha"
                     /note="C-terminal, alpha helical domain of Class Alpha
                     Glutathione S-transferases; cd03208"
                     /db_xref="CDD:198317"
     Site            order(86..87,89,93..95,97..98,101,131)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(97,104,107,110..111,131..132,135,152..155,158,
                     161..162,165..166,169,193..194,196..201)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198317"
     Site            order(101,107,111,131,208,216,220)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198317"
     CDS             1..221
                     /gene="Gsta3"
                     /gene_synonym="Gsta5; Yc2"
                     /coded_by="NM_001159739.2:199..864"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:494500"
                     /db_xref="RGD:1591980"
ORIGIN      
        1 mpgkpvlhyf dgrgrmepir wllaaagvef eenflktrdd larlrsdgsl mfeqvpmvei
       61 dgmklvqtka ilnyiatkyn lygkdmkera lidmyaegva dlelmvlyyp ymppgekeas
      121 lakikdkarn ryfpayekvl kshgqdylvg nklsradvsl vellyhveem dpgivdnfpl
      181 lkalrtrvsn lptvkkflqp gsqrkpfdde kcvesakkif s
//
LOCUS       NP_058824                424 aa            linear   ROD 27-APR-2025
DEFINITION  inhibin beta A chain preproprotein [Rattus norvegicus].
ACCESSION   NP_058824
VERSION     NP_058824.1
DBSOURCE    REFSEQ: accession NM_017128.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Zheng,J., Zhang,T., Han,S., Liu,C., Liu,M., Li,S. and Li,J.
  TITLE     Activin A improves the neurological outcome after ischemic stroke
            in mice by promoting oligodendroglial ACVR1B-mediated white matter
            remyelination
  JOURNAL   Exp Neurol 337, 113574 (2021)
   PUBMED   33345977
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Xian,S., Chen,A., Wu,X., Lu,C., Wu,Y., Huang,F. and Zeng,Z.
  TITLE     Activation of activin/Smad2 and 3 signaling pathway and
            the&nbsp;potential involvement of endothelial-mesenchymal
            transition in the valvular damage due to rheumatic heart disease
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33179113
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Wang,Y., Shuang,L., Yujie,S., Xiaohui,M., Wei,W. and Jidong,W.
  TITLE     Activin A overexpression promotes rat follicular development
            through SCF-kit-mediated cell signals
  JOURNAL   Gynecol Endocrinol 36 (12), 1070-1073 (2020)
   PUBMED   32133888
  REMARK    GeneRIF: Activin A overexpression promotes rat follicular
            development through SCF-kit-mediated cell signals.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Szabo,Z., Vainio,L., Lin,R., Swan,J., Hulmi,J.J., Rahtu-Korpela,L.,
            Serpi,R., Laitinen,M., Pasternack,A., Ritvos,O., Kerkela,R. and
            Magga,J.
  TITLE     Systemic blockade of ACVR2B ligands attenuates muscle wasting in
            ischemic heart failure without compromising cardiac function
  JOURNAL   FASEB J 34 (8), 9911-9924 (2020)
   PUBMED   32427381
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Magga,J., Vainio,L., Kilpio,T., Hulmi,J.J., Taponen,S., Lin,R.,
            Rasanen,M., Szabo,Z., Gao,E., Rahtu-Korpela,L., Alakoski,T.,
            Ulvila,J., Laitinen,M., Pasternack,A., Koch,W.J., Alitalo,K.,
            Kivela,R., Ritvos,O. and Kerkela,R.
  TITLE     Systemic Blockade of ACVR2B Ligands Protects Myocardium from Acute
            Ischemia-Reperfusion Injury
  JOURNAL   Mol Ther 27 (3), 600-610 (2019)
   PUBMED   30765322
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Verschueren,K., Dewulf,N., Goumans,M.J., Lonnoy,O., Feijen,A.,
            Grimsby,S., Vandi Spiegle,K., ten Dijke,P., Moren,A.,
            Vanscheeuwijck,P., Heldin,C.H., Miyazono,K., Mummery,C., Van Den
            Eijnden-Van Raaij,J. and Huylebroeck,D.
  TITLE     Expression of type I and type IB receptors for activin in
            midgestation mouse embryos suggests distinct functions in
            organogenesis
  JOURNAL   Mech Dev 52 (1), 109-123 (1995)
   PUBMED   7577669
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Shao,L., Frigon,N.L. Jr., Young,A.L., Yu,A.L., Mathews,L.S.,
            Vaughan,J., Vale,W. and Yu,J.
  TITLE     Effect of activin A on globin gene expression in purified human
            erythroid progenitors
  JOURNAL   Blood 79 (3), 773-781 (1992)
   PUBMED   1310063
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Mathews,L.S. and Vale,W.W.
  TITLE     Expression cloning of an activin receptor, a predicted
            transmembrane serine kinase
  JOURNAL   Cell 65 (6), 973-982 (1991)
   PUBMED   1646080
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Mason,A.J., Berkemeier,L.M., Schmelzer,C.H. and Schwall,R.H.
  TITLE     Activin B: precursor sequences, genomic structure and in vitro
            activities
  JOURNAL   Mol Endocrinol 3 (9), 1352-1358 (1989)
   PUBMED   2575216
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Woodruff,T.K., Meunier,H., Jones,P.B., Hsueh,A.J. and Mayo,K.E.
  TITLE     Rat inhibin: molecular cloning of alpha- and beta-subunit
            complementary deoxyribonucleic acids and expression in the ovary
  JOURNAL   Mol Endocrinol 1 (8), 561-568 (1987)
   PUBMED   3153478
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M37482.1, SRR26643285.48847.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN16093046
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..424
                     /product="inhibin beta A chain preproprotein"
                     /note="inhibin beta A chain; activin beta-A chain; activin
                     A; inhibin beta-A; inhibin beta A subunit"
                     /calculated_mol_wt=44337
     sig_peptide     1..28
                     /calculated_mol_wt=3088
     proprotein      29..424
                     /product="inhibin beta A chain proprotein"
                     /calculated_mol_wt=44337
     Region          56..291
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18331.1)"
     Region          264..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18331.1)"
     mat_peptide     309..424
                     /product="inhibin beta A chain"
                     /calculated_mol_wt=12976
     Region          317..424
                     /region_name="TGF_beta_INHBA"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in inhibin beta A chain (INHBA) and similar
                     proteins; cd19404"
                     /db_xref="CDD:381674"
     Site            order(325,338,340,344,395,398..400,402,408,410,412,419)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381674"
     Site            order(387..388,390,411,414..415,424)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381674"
     CDS             1..424
                     /gene="Inhba"
                     /coded_by="NM_017128.2:171..1445"
                     /db_xref="GeneID:29200"
                     /db_xref="RGD:62074"
ORIGIN      
        1 mpllwlrgfl lascwiivrs sptpgseghg aapdcpscal atlpkdgpns qpemveavkk
       61 hilnmlhlkk rpdvtqpvpk aallnairkl hvgkvgengy veieddigrr aemnelmeqt
      121 seiitfaesg tarktlhfei skegsdlsvv eraevwlflk vpkanrtrtk vtirlfqqqk
      181 hpqgsldmgd eaeemglkge rselllsekv vdarkstwhi fpvsssiqrl ldqgkssldv
      241 riaceqcqes gaslvllgkk kkkevdgdgk kkdgsdggle eekeqshrpf lmlqarqsed
      301 hphrrrrrgl ecdgkvnicc kkqffvsfkd igwndwiiap sgyhanyceg ecpshiagts
      361 gsslsfhstv inhyrmrghs pfanlksccv ptklrpmsml yyddgqniik kdiqnmivee
      421 cgcs
//
LOCUS       NP_001258023             371 aa            linear   ROD 27-APR-2025
DEFINITION  protein NDRG4 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001258023
VERSION     NP_001258023.1
DBSOURCE    REFSEQ: accession NM_001271094.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Zhu,H., Wang,X. and Chen,S.
  TITLE     Downregulation of MiR-218-5p Protects Against Oxygen-Glucose
            Deprivation/Reperfusion-Induced Injuries of PC12 Cells via
            Upregulating N-myc Downstream Regulated Gene 4 (NDRG4)
  JOURNAL   Med Sci Monit 26, e920101 (2020)
   PUBMED   32048632
  REMARK    GeneRIF: Downregulation of MiR-218-5p Protects Against
            Oxygen-Glucose Deprivation/Reperfusion-Induced Injuries of PC12
            Cells via Upregulating N-myc Downstream Regulated Gene 4 (NDRG4).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Wen,L., Liu,L., Li,J., Tong,L., Zhang,K., Zhang,Q. and Li,C.
  TITLE     NDRG4 protects against cerebral ischemia injury by inhibiting
            p53-mediated apoptosis
  JOURNAL   Brain Res Bull 146, 104-111 (2019)
   PUBMED   30593880
  REMARK    GeneRIF: Authors found that NDRG4 expression was upregulated during
            the early stage and decreased 24 h after ischemia/reperfusion (I/R)
            injury, and NDRG4 overexpression decreased the infarct size and
            mitigated the neurological deficits induced by I/R injury by
            inhibiting apoptosis.
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Xing,Y., Tang,B., Zhu,C., Li,W., Li,Z., Zhao,J., Gong,W.D.,
            Wu,Z.Q., Zhu,C.C. and Zhang,Y.Q.
  TITLE     N-myc downstream-regulated gene 4, up-regulated by tumor necrosis
            factor-alpha and nuclear factor kappa B, aggravates cardiac
            ischemia/reperfusion injury by inhibiting reperfusion injury
            salvage kinase pathway
  JOURNAL   Basic Res Cardiol 111 (2), 11 (2016)
   PUBMED   26780215
  REMARK    GeneRIF: expression increased in injured neonatal ventricular
            myocytes
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Benesh,E.C., Miller,P.M., Pfaltzgraff,E.R., Grega-Larson,N.E.,
            Hager,H.A., Sung,B.H., Qu,X., Baldwin,H.S., Weaver,A.M. and
            Bader,D.M.
  TITLE     Bves and NDRG4 regulate directional epicardial cell migration
            through autocrine extracellular matrix deposition
  JOURNAL   Mol Biol Cell 24 (22), 3496-3510 (2013)
   PUBMED   24048452
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Ding,W., Zhang,J., Yoon,J.G., Shi,D., Foltz,G. and Lin,B.
  TITLE     NDRG4 is downregulated in glioblastoma and inhibits cell
            proliferation
  JOURNAL   OMICS 16 (5), 263-267 (2012)
   PUBMED   22489821
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Maeda,A., Hongo,S. and Miyazaki,A.
  TITLE     Genomic organization, expression, and comparative analysis of
            noncoding region of the rat Ndrg4 gene
  JOURNAL   Gene 324, 149-158 (2004)
   PUBMED   14693380
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Nishimoto,S., Tawara,J., Toyoda,H., Kitamura,K. and Komurasaki,T.
  TITLE     A novel homocysteine-responsive gene, smap8, modulates mitogenesis
            in rat vascular smooth muscle cells
  JOURNAL   Eur J Biochem 270 (11), 2521-2531 (2003)
   PUBMED   12755708
  REMARK    GeneRIF: smap8 is involved in the regulation of mitogenic
            signalling in vascular smooth muscle cells, possibly in response to
            a homocysteine-induced injury [SMAP8]
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Ohki,T., Hongo,S., Nakada,N., Maeda,A. and Takeda,M.
  TITLE     Inhibition of neurite outgrowth by reduced level of NDRG4 protein
            in antisense transfected PC12 cells
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 55-63 (2002)
   PUBMED   11978393
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Nakada,N., Hongo,S., Ohki,T., Maeda,A. and Takeda,M.
  TITLE     Molecular characterization of NDRG4/Bdm1 protein isoforms that are
            differentially regulated during rat brain development
  JOURNAL   Brain Res Dev Brain Res 135 (1-2), 45-53 (2002)
   PUBMED   11978392
  REMARK    GeneRIF: Molecular characterization of NDRG4 protein isoforms that
            are differentially regulated during rat brain development.
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Yamauchi,Y., Hongo,S., Ohashi,T., Shioda,S., Zhou,C., Nakai,Y.,
            Nishinaka,N., Takahashi,R., Takeda,F. and Takeda,M.
  TITLE     Molecular cloning and characterization of a novel developmentally
            regulated gene, Bdm1, showing predominant expression in postnatal
            rat brain
  JOURNAL   Brain Res Mol Brain Res 68 (1-2), 149-158 (1999)
   PUBMED   10320792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1, FM054107.1 and CB585874.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence and lacks an alternate in-frame exon compared to
            variant 1. The resulting isoform (4) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY217031.1, SRR26643289.42062.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..371
                     /product="protein NDRG4 isoform 4"
                     /note="development-related protein; N-myc downstream
                     regulated 4; protein NDRG4; brain development-related
                     molecule 1; N-myc downstream regulated gene 4"
                     /calculated_mol_wt=40594
     Region          40..322
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..371
                     /gene="Ndrg4"
                     /gene_synonym="Bdm1; Ndr4; smap8"
                     /coded_by="NM_001271094.1:116..1231"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64457"
                     /db_xref="RGD:621593"
ORIGIN      
        1 maglqelrfp eekpllrgqd ateldnpdaf lsvvdtdwke hdietpygll hvvirgspkg
       61 nrpailtyhd vglnhklcfn tlfnledmqe itkhfvvchv dapgqqvgas qfpqgyqfps
      121 meqlatmlps vvqhfgfkyv igigvgagay vlakfalifp dlveglvlmn idpngkgwid
      181 waatklsglt stlpdtvlsh lfsqeelvnn telvqsyrqq issvvnqanl qlfwnmynsr
      241 rdldinrpgt vpnaktlrcp vmlvvgdnap aedgvvecns kldpttttfl kmadsgglpq
      301 vtqpgkltea fkyflqgmgy mpsasmtrla rsrtasltsa ssvdgsrpqp cthsdssegm
      361 gqvnhtmevs c
//
LOCUS       NP_058815                258 aa            linear   ROD 27-APR-2025
DEFINITION  granzyme K precursor [Rattus norvegicus].
ACCESSION   NP_058815
VERSION     NP_058815.1
DBSOURCE    REFSEQ: accession NM_017119.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Sayers,T.J., Wiltrout,T.A., Smyth,M.J., Ottaway,K.S., Pilaro,A.M.,
            Sowder,R., Henderson,L.E., Sprenger,H. and Lloyd,A.R.
  TITLE     Purification and cloning of a novel serine protease, RNK-Tryp-2,
            from the granules of a rat NK cell leukemia
  JOURNAL   J Immunol 152 (5), 2289-2297 (1994)
   PUBMED   8133042
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L19694.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L19694.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Rattus norvegicus"
                     /strain="F344"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..258
                     /product="granzyme K precursor"
                     /EC_number="3.4.21.-"
                     /note="NK-Tryp-2; NK-tryptase-2; RNK-Tryp-2"
                     /calculated_mol_wt=25755
     sig_peptide     1..25
                     /note="putative"
                     /calculated_mol_wt=2728
     mat_peptide     26..258
                     /product="granzyme K"
                     /note="serine protease family (granzymes)"
                     /calculated_mol_wt=25755
     Region          26..251
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            26
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(66,110,208)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(202,223,225)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..258
                     /gene="Gzmk"
                     /coded_by="NM_017119.2:25..801"
                     /db_xref="GeneID:29165"
                     /db_xref="RGD:68401"
ORIGIN      
        1 msfsssalvf lvagiymsse sfhteiiggr evqphsrpfm asiqyrgkhi cggvlihpqw
       61 vltaahcysr ghsptvvlga hslsknepmk qtfeikefip fsgfksgtnd imliklrtaa
      121 elnkhvqllh lrsknyirdg tkcqvtgwgs tkpdvlttsd tlqevtvtii srkrcnsqsy
      181 ynhkpvitkd micagdrrge kdsckgdsgg plickgvfha lvsggykcgi snkpgvytll
      241 tkkyqtwiks klapssah
//
LOCUS       NP_001006958             248 aa            linear   ROD 27-APR-2025
DEFINITION  eukaryotic translation initiation factor 4H [Rattus norvegicus].
ACCESSION   NP_001006958 XP_213755 XP_347155
VERSION     NP_001006958.1
DBSOURCE    REFSEQ: accession NM_001006957.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Capossela,S., Muzio,L., Bertolo,A., Bianchi,V., Dati,G.,
            Chaabane,L., Godi,C., Politi,L.S., Biffo,S., D'Adamo,P.,
            Mallamaci,A. and Pannese,M.
  TITLE     Growth defects and impaired cognitive-behavioral abilities in mice
            with knockout for Eif4h, a gene located in the mouse homolog of the
            Williams-Beuren syndrome critical region
  JOURNAL   Am J Pathol 180 (3), 1121-1135 (2012)
   PUBMED   22234171
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Parsyan,A., Svitkin,Y., Shahbazian,D., Gkogkas,C., Lasko,P.,
            Merrick,W.C. and Sonenberg,N.
  TITLE     mRNA helicases: the tacticians of translational control
  JOURNAL   Nat Rev Mol Cell Biol 12 (4), 235-245 (2011)
   PUBMED   21427765
  REMARK    Review article
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Martindale,D.W., Wilson,M.D., Wang,D., Burke,R.D., Chen,X.,
            Duronio,V. and Koop,B.F.
  TITLE     Comparative genomic sequence analysis of the Williams syndrome
            region (LIMK1-RFC2) of human chromosome 7q11.23
  JOURNAL   Mamm Genome 11 (10), 890-898 (2000)
   PUBMED   11003705
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Richter-Cook,N.J., Dever,T.E., Hensold,J.O. and Merrick,W.C.
  TITLE     Purification and characterization of a new eukaryotic protein
            translation factor. Eukaryotic initiation factor 4H
  JOURNAL   J Biol Chem 273 (13), 7579-7587 (1998)
   PUBMED   9516461
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Osborne,L.R., Martindale,D., Scherer,S.W., Shi,X.M., Huizenga,J.,
            Heng,H.H., Costa,T., Pober,B., Lew,L., Brinkman,J., Rommens,J.,
            Koop,B. and Tsui,L.C.
  TITLE     Identification of genes from a 500-kb region at 7q11.23 that is
            commonly deleted in Williams syndrome patients
  JOURNAL   Genomics 36 (2), 328-336 (1996)
   PUBMED   8812460
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB718613.1 and BC083818.1.
            
            On or before Nov 22, 2004 this sequence version replaced
            XP_213755.2, XP_347155.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083818.1, FQ099171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..248
                     /product="eukaryotic translation initiation factor 4H"
                     /note="eIF-4H; williams-Beuren syndrome chromosomal region
                     1 protein homolog; Williams-Beuren syndrome chromosome
                     region 1 homolog"
                     /calculated_mol_wt=27193
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            19
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUK2; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            22
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUK2; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Region          37..120
                     /region_name="RRM_eIF4H"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     translation initiation factor 4H (eIF-4H) and similar
                     proteins; cd12401"
                     /db_xref="CDD:409835"
     Region          <40..>227
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          121..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            136
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUK2; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            166
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            175
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUK2; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15056; propagated from
                     UniProtKB/Swiss-Prot (Q5XI72.1)"
     CDS             1..248
                     /gene="Eif4h"
                     /gene_synonym="Wbscr1"
                     /coded_by="NM_001006957.2:39..785"
                     /db_xref="GeneID:288599"
                     /db_xref="RGD:1359222"
ORIGIN      
        1 madfdtyddr ayssfgggrg srgsagghgs rsqkelptep pytayvgnlp fntvqgdida
       61 ifkdlsirsv rlvrdkdtdk fkgfcyvefd evdslkealt ydgallgdrs lrvdiaegrk
      121 qdkggfgfrk ggpddrgmgg sreprggwds rddfssgyrd dflggrggsr pgdrragppm
      181 gsrfrdgppl rgsnmdfrep teeeraqrpr lqlkprtvat plnqvanpns aifggarpre
      241 evvqkeqe
//
LOCUS       NP_036794                111 aa            linear   ROD 27-APR-2025
DEFINITION  seminal vesicle secretory protein 4 precursor [Rattus norvegicus].
ACCESSION   NP_036794
VERSION     NP_036794.1
DBSOURCE    REFSEQ: accession NM_012662.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Prevete,N., Rossi,F.W., Triggiani,M., Marone,G., de Paulis,A.,
            Metafora,V., De Maria,S., Carteni,M., Ragone,R., Ravagnan,G. and
            Metafora,S.
  TITLE     Antiapoptotic seminal vesicle protein IV induces histamine release
            from human FcepsilonRI+ cells
  JOURNAL   Int Arch Allergy Immunol 151 (4), 318-330 (2010)
   PUBMED   19851073
  REMARK    GeneRIF: induces histamine release from human FcepsilonRI+ cells
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Metafora,V., Stiuso,P., Ferranti,P., Giannattasio,A., Dicitore,A.,
            Ravagnan,G., De Maria,S., Pontoni,G., Carteni,M. and Metafora,S.
  TITLE     In vitro stimulatory effect of anti-apoptotic seminal vesicle
            protein 4 on purified peroxidase enzymes
  JOURNAL   FEBS J 275 (15), 3870-3883 (2008)
   PUBMED   18616464
  REMARK    GeneRIF: native seminal vesicle protein 4 was shown by
            spectrophotometric and electrospray-MS analysis to interact with
            NADPH, an electron donor substrate of the selenium-dependent
            glutathione peroxidase/glutathione reductase redox system
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Fuggetta,M.P., Lanzilli,G., Cottarelli,A., Ravagnan,G., Carteni,M.,
            De Maria,S., Metafora,B.M., Metafora,V. and Metafora,S.
  TITLE     Anti-apoptotic seminal vesicle protein IV inhibits cell-mediated
            immunity
  JOURNAL   J Reprod Immunol 78 (2), 85-93 (2008)
   PUBMED   18243331
  REMARK    GeneRIF: findings indicate that seminal vesicle protein IV has a
            marked in vitro inhibitory effect on natural killer cell,
            lymphokine-activated killer cell and cytotoxic T lymphocyte
            cytotoxicity
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Vilasi,S. and Ragone,R.
  TITLE     Abundance of intrinsic disorder in SV-IV, a multifunctional
            androgen-dependent protein secreted from rat seminal vesicle
  JOURNAL   FEBS J 275 (4), 763-774 (2008)
   PUBMED   18215165
  REMARK    GeneRIF: Data strongly suggest that SV-IV needs large plasticity to
            efficiently interact with the different targets that characterize
            its multifaceted biological function, and should therefore be
            better classified as an intrinsically disordered protein.
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Morelli,F., Peluso,G., Petillo,O., Giannattasio,A., Filosa,S.,
            Motta,C.M., Tammaro,S., Zatterale,A., Calzone,R., Budillon,A.,
            Carteni,M., de Maria,S., Costanza,M.R., Nigro,A., Petrazzuolo,M.,
            Buommino,E., Rizzo,M., Capasso,G., Baiano,S., Moscatiello,F.,
            Ravagnan,G., Fuggetta,M.P., Tajana,G., Stiuso,P., Metafora,B.M.,
            Metafora,V. and Metafora,S.
  TITLE     The immunomodulatory protein SV-IV protects serum-deprived cells
            against apoptosis but not against G0/G1 arrest: possible
            implications for the survival of implanting embryo
  JOURNAL   J Cell Physiol 212 (3), 610-625 (2007)
   PUBMED   17458892
  REMARK    GeneRIF: Seminal vesicle protein 4 act as a cell survival factor,
            preventing apoptosis but not cell cycle arrest. May be involved in
            survival of implanting embryos.
REFERENCE   6  (residues 1 to 111)
  AUTHORS   McDonald,C.J., Eliopoulos,E. and Higgins,S.J.
  TITLE     Divergent protein coding regions in otherwise closely related
            androgen-regulated mRNAs
  JOURNAL   EMBO J 3 (11), 2517-2521 (1984)
   PUBMED   6548962
REFERENCE   7  (residues 1 to 111)
  AUTHORS   Harris,S.E., Mansson,P.E., Tully,D.B. and Burkhart,B.
  TITLE     Seminal vesicle secretion IV gene: allelic difference due to a
            series of 20-base-pair direct tandem repeats within an intron
  JOURNAL   Proc Natl Acad Sci U S A 80 (21), 6460-6464 (1983)
   PUBMED   6579532
REFERENCE   8  (residues 1 to 111)
  AUTHORS   Kandala,J.C., Kistler,M.K., Lawther,R.P. and Kistler,W.S.
  TITLE     Characterization of a genomic clone for rat seminal vesicle
            secretory protein IV
  JOURNAL   Nucleic Acids Res 11 (10), 3169-3186 (1983)
   PUBMED   6304626
REFERENCE   9  (residues 1 to 111)
  AUTHORS   Mansson,P.E., Sugino,A. and Harris,S.E.
  TITLE     Use of a cloned double stranded cDNA coding for a major androgen
            dependent protein in rat seminal vesicle secretion: the effect of
            testosterone in gene expression
  JOURNAL   Nucleic Acids Res 9 (4), 935-946 (1981)
   PUBMED   6164983
REFERENCE   10 (residues 1 to 111)
  AUTHORS   Pan,Y.C., Silverberg,A.B., Harris,S.E. and Li,S.S.
  TITLE     Complete amino acid sequence of a major secretory protein from rat
            seminal vesicle
  JOURNAL   Int J Pept Protein Res 16 (2), 143-146 (1980)
   PUBMED   7007263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X01114.1, BF417050.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..111
                     /product="seminal vesicle secretory protein 4 precursor"
                     /note="seminal vesicle protein 4; SVS protein S; Seminal
                     vesicle protein-4; seminal vesicle protein 2;
                     androgen-dependent protein; seminal vesicle secretory
                     protein IV"
                     /calculated_mol_wt=9769
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2181
     Region          24..107
                     /region_name="Svs_4_5_6"
                     /note="Seminal vesicle secretory proteins 4/5/6;
                     pfam17381"
                     /db_xref="CDD:375165"
     CDS             1..111
                     /gene="Svs4"
                     /gene_synonym="ADP; RNSVSP4U; Svp4; SVS IV; SVSIV1"
                     /coded_by="NM_012662.3:52..387"
                     /db_xref="GeneID:24802"
                     /db_xref="RGD:3791"
ORIGIN      
        1 mkstslflcs lllllvtgai grktkekysq seevvsesfa sgpssgssde lvrdkpygpk
       61 vsggsfgeea seeissrrsk hisrssggsn megessyakk krsrfaqdvl n
//
LOCUS       NP_001257493             413 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3B [Rattus norvegicus].
ACCESSION   NP_001257493
VERSION     NP_001257493.1
DBSOURCE    REFSEQ: accession NM_001270564.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, AY009371.1,
            CB735595.1 and BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) is alternatively spliced at
            the 3' end compared to variant 1, and encodes a shorter isoform
            (H3B, also known as H3S or H3(413)) containing 7 transmembrane
            domains, but missing part of the third intracellular loop compared
            to isoform H3A. This isoform is thought to function as the
            histamine autoreceptor (PMID:22356432).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY009371.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132280, SAMD00132300
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..413
                     /product="histamine H3 receptor isoform H3B"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=45758
     Region          48..391
                     /region_name="7tmA_Histamine_H3R"
                     /note="histamine receptor subtypes H3R and H3R-like,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15296"
                     /db_xref="CDD:320423"
     Region          69..96
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320423"
     Region          107..137
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320423"
     Site            order(110,114..115,118..119,190,199,202..203,206,339,
                     342..343,346,362,366,370)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320423"
     Region          152..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320423"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320423"
     Region          319..349
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320423"
     Region          359..384
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320423"
     CDS             1..413
                     /gene="Hrh3"
                     /coded_by="NM_001270564.1:338..1579"
                     /note="isoform H3B is encoded by transcript variant 2"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhssgsssr gterprslkr gskpsassas
      301 lekrmkmvsq sitqrfrlsr dkkvakslai ivsifglcwa pytllmiira achgrcipdy
      361 wyetsfwllw ansavnpvly plchysfrra ftkllcpqkl kvqphgsleq cwk
//
LOCUS       NP_001257526            2709 aa            linear   ROD 27-APR-2025
DEFINITION  inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001257526
VERSION     NP_001257526.1
DBSOURCE    REFSEQ: accession NM_001270597.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2709)
  AUTHORS   Pan,D., Jiang,M., Tao,G., Shi,J., Song,Z., Chen,R. and Wang,D.
  TITLE     The role of Ca2+ signalling and InsP3R in the pathogenesis of
            intrahepatic cholestasis of pregnancy
  JOURNAL   J Obstet Gynaecol 44 (1), 2345276 (2024)
   PUBMED   38685831
  REMARK    GeneRIF: The role of Ca[2+] signalling and InsP3R in the
            pathogenesis of intrahepatic cholestasis of pregnancy.
REFERENCE   2  (residues 1 to 2709)
  AUTHORS   Shi,R., Liu,Z., Yue,H., Li,M., Liu,S., De,D., Li,R., Chen,Y.,
            Cheng,S., Gu,X., Jia,M., Li,J., Li,J., Zhang,S., Feng,N., Fan,R.,
            Fu,F., Liu,Y., Ding,M. and Pei,J.
  TITLE     IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin
  JOURNAL   Cell Mol Biol Lett 29 (1), 22 (2024)
   PUBMED   38308199
  REMARK    GeneRIF: IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2709)
  AUTHORS   Obaid,A.A., Almasmoum,H., Almaimani,R.A., El-Boshy,M., Aslam,A.,
            Idris,S., Ghaith,M.M., El-Readi,M.Z., Ahmad,J., Farrash,W.F.,
            Mujalli,A., Eid,S.Y., Elzubier,M.E. and Refaat,B.
  TITLE     Vitamin D and calcium co-therapy mitigates pre-established cadmium
            nephropathy by regulating renal calcium homeostatic molecules and
            improving anti-oxidative and anti-inflammatory activities in rat
  JOURNAL   J Trace Elem Med Biol 79, 127221 (2023)
   PUBMED   37244046
REFERENCE   4  (residues 1 to 2709)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   5  (residues 1 to 2709)
  AUTHORS   Fan,G., Baker,M.R., Terry,L.E., Arige,V., Chen,M., Seryshev,A.B.,
            Baker,M.L., Ludtke,S.J., Yule,D.I. and Serysheva,I.I.
  TITLE     Conformational motions and ligand-binding underlying gating and
            regulation in IP3R channel
  JOURNAL   Nat Commun 13 (1), 6942 (2022)
   PUBMED   36376291
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2709)
  AUTHORS   Zhang,S.X., Zhang,J.P., Fletcher,D.L., Zoeller,R.T. and Sun,G.Y.
  TITLE     In situ hybridization of mRNA expression for IP3 receptor and
            IP3-3-kinase in rat brain after transient focal cerebral ischemia
  JOURNAL   Brain Res Mol Brain Res 32 (2), 252-260 (1995)
   PUBMED   7500836
REFERENCE   7  (residues 1 to 2709)
  AUTHORS   Takei,K., Stukenbrok,H., Metcalf,A., Mignery,G.A., Sudhof,T.C.,
            Volpe,P. and De Camilli,P.
  TITLE     Ca2+ stores in Purkinje neurons: endoplasmic reticulum
            subcompartments demonstrated by the heterogeneous distribution of
            the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin
  JOURNAL   J Neurosci 12 (2), 489-505 (1992)
   PUBMED   1311032
REFERENCE   8  (residues 1 to 2709)
  AUTHORS   Suzuki,T., Abe-Dohmae,S. and Tanaka,R.
  TITLE     P400 protein is one of the major substrates for
            Ca2+/calmodulin-dependent protein kinase II in the postsynaptic
            density-enriched fraction isolated from rat cerebral cortex,
            hippocampus and cerebellum
  JOURNAL   Neurochem Int 20 (1), 61-67 (1992)
   PUBMED   1338970
REFERENCE   9  (residues 1 to 2709)
  AUTHORS   Danoff,S.K., Ferris,C.D., Donath,C., Fischer,G.A., Munemitsu,S.,
            Ullrich,A., Snyder,S.H. and Ross,C.A.
  TITLE     Inositol 1,4,5-trisphosphate receptors: distinct neuronal and
            nonneuronal forms derived by alternative splicing differ in
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2951-2955 (1991)
   PUBMED   1849282
REFERENCE   10 (residues 1 to 2709)
  AUTHORS   Mignery,G.A., Newton,C.L., Archer,B.T. 3rd and Sudhof,T.C.
  TITLE     Structure and expression of the rat inositol 1,4,5-trisphosphate
            receptor
  JOURNAL   J Biol Chem 265 (21), 12679-12685 (1990)
   PUBMED   2165071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J05510.1, BF402715.1, U38653.1,
            GQ233032.1 and BC091346.1.
            
            Summary: This gene belongs to the Insp3 receptor family. It encodes
            an intracellular receptor for inositol 1,4,5-trisphosphate. Upon
            stimulation by inositol 1,4,5-trisphosphate, this receptor mediates
            calcium release from the endoplasmic reticulum. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (3) lacks three consecutive exons
            in the coding region, but maintains the reading frame, compared to
            variant 1. The resulting isoform (3) lacks an internal segment,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760384 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2709
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q41"
     Protein         1..2709
                     /product="inositol 1,4,5-trisphosphate-gated calcium
                     channel ITPR1 isoform 3"
                     /note="IP-3-R; type 1 InsP3 receptor; IP3 receptor; type 1
                     inositol 1,4,5-trisphosphate receptor; IP3R 1; inositol
                     1,4,5-triphosphate receptor, type 1; inositol
                     1,4,5-triphosphate receptor 1; inositol
                     1,4,5-trisphosphate-gated calcium channel ITPR1"
                     /calculated_mol_wt=308416
     Region          5..229
                     /region_name="Ins145_P3_rec"
                     /note="Inositol 1,4,5-trisphosphate/ryanodine receptor;
                     pfam08709"
                     /db_xref="CDD:462572"
     Region          224..445
                     /region_name="beta-trefoil_MIR_ITPR1"
                     /note="MIR domain, beta-trefoil fold, found in inositol
                     1,4,5-trisphosphate receptor type 1 (ITPR1) and similar
                     proteins; cd23287"
                     /db_xref="CDD:467758"
     Site            order(245..246,300,374,376,387,393,425..426)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467758"
     Site            order(265,267..269,275)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:467758"
     Region          476..670
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          1005..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1136..1167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1193..1312
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Site            1588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1711..1749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            1715
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1841..1866
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1892..1912
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1922..2029
                     /region_name="RIH_assoc"
                     /note="RyR and IP3R Homology associated; pfam08454"
                     /db_xref="CDD:462482"
     Site            2234..2254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2266..2286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2310..2560
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            2313..2333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2357..2377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2400..2420
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2423..2488
                     /region_name="Interaction with ERP44.
                     /evidence=ECO:0000250|UniProtKB:P11881"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2529..2549
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2682..2709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     CDS             1..2709
                     /gene="Itpr1"
                     /gene_synonym="I145TR; InsP3R; InsP3R1; IP3R1; P400"
                     /coded_by="NM_001270597.1:239..8368"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25262"
                     /db_xref="RGD:2933"
ORIGIN      
        1 msdkmssflh igdicslyae gstngfistl glvddrcvvq peagdlnnpp kkfrdclfkl
       61 cpmnrysaqk qfwkaakpga nsttdavlln klhhaadlek kqnetenrkl lgtviqygnv
      121 iqllhlksnk yltvnkrlpa lleknamrvt ldeagnegsw fyiqpfyklr sigdsvvigd
      181 kvvlnpvnag qplhasshql vdnpgcnevn svncntswki vlfmkwsdnk ddilkggdvv
      241 rlfhaeqekf ltcdehrkkq hvflrttgrq satsatsska lwevevvqhd pcrggagywn
      301 slfrfkhlat ghylaaevdp dfeeeclefq psvdpdqdas rsrlrnaqek mvyslvsvpe
      361 gndissifel dpttlrggds lvprnsyvrl rhlctntwvh stnipidkee ekpvmlkigt
      421 splkedkeaf aivpvspaev rdldfandas kvlgsiagkl ekgtitqner rsvtklledl
      481 vyfvtggtns gqdvlevvfs kpnrerqklm reqnilkqif kllqapftdc gdgpmlrlee
      541 lgdqrhapfr hicrlcyrvl rhsqqdyrkn qeyiakqfgf mqkqigydvl aedtitallh
      601 nnrkllekhi taaeidtfvs lvrknreprf ldylsdlcvs mnksipvtqe lickavlnpt
      661 nadilietkl vlsrfefegv stgenaleag edeeevwlfw rdsnkeirsk svrelaqdak
      721 egqkedrdvl syyryqlnlf armcldrqyl aineisgqld vdlilrcmsd enlpydlras
      781 fcrlmlhmhv drdpqeqvtp vkyarlwsei pseiaiddyd ssgaskdeik erfaqtmefv
      841 eeylrdvvcq rfpfsdkekn kltfevvnla rnliyfgfyn fsdllrltki llaildcvhv
      901 ttifpiskmt kgeenkgsnv mrsihgvgel mtqvvlrggg flpmtpmaaa pegnvkqaep
      961 ekedimvmdt klkiieilqf ilnvrldyri scllcifkre fdesnsqsse tssgnssqeg
     1021 psnvpgaldf ehieeqaegi fggseentpl dlddhggrtf lrvllhltmh dypplvsgal
     1081 qllfrhfsqr qevlqafkqv qllvtsqdvd nykqikqdld qlrsivekse lwvykgqgpd
     1141 epmdgasgen ehkkteegts kplkhestss ynyrvvkeil irlsklcvqe sasvrksrkq
     1201 qqrllrnmga havvlellqi pyekaedtkm qeimrlahef lqnfcagnqq nqallhkhin
     1261 lflnpgilea vtmqhifmnn fqlcseiner vvqhfvhcie thgrnvqyik flqtivkaeg
     1321 kfikkcqdmv maelvnsged vlvfyndras fqtliqmmrs erdrmdensp lmyhihlvel
     1381 lavctegknv yteikcnsll plddivrvvt hedcipevki ayinflnhcy vdtevemkei
     1441 ytsnhmwklf enflvdicra cnntsdrkha dsvlekyvte ivmsivttff sspfsdqstt
     1501 lqtrqpvfvq llqgvfrvyh cnwlmpsqka svescirvls dvaksraiai pvdldsqvnn
     1561 lflkshnivq ktamnwrlsa rnaarrdsvl aasrdyrnii erlqdivsal edrlrplvqa
     1621 elsvlvdvlh rpellfpent darrkcesgg ficklikhtk qlleeneekl cikvlqtlre
     1681 mmtkdrgyge kgealrqilv nryygnirps grresltsfg ngplspggps kpggggggpg
     1741 sgstsrgems laevqchldk egasnlvidl imnassdrvf hesillaial leggnttiqh
     1801 sffcrltedk ksekffkvfy drmkvaqqei katvtvntsd lgnkkkddev drdapsrkka
     1861 kepttqitee vrdqlleasa atrkafttfr readpddhyq sgegtqattd kakddlemsa
     1921 vitimqpilr flqllcenhn rdlqnflrcq nnktnynlvc etlqfldcic gsttgglgll
     1981 glyineknva linqtleslt eycqgpchen qnciathesn gidiitalil ndinplgkkr
     2041 mdlvlelknn asklllaime srhdsenaer ilynmrpkel vevikkaymq gevefedgen
     2101 gedgaasprn vghniyilah qlarhnkelq tmlkpggqvd gdealefyak htaqieivrl
     2161 drtmeqivfp vpsicefltk esklriyytt erdeqgskin dfflrsedlf nemnwqkklr
     2221 aqpvlywcar nmsfwssisf nlavlmnllv affypfkgvr ggtlephwsg llwtamlisl
     2281 aivialpkph giraliasti lrlifsvglq ptlfllgafn vcnkiiflms fvgncgtftr
     2341 gyramvldve flyhllylli camglfvhef fyslllfdlv yreetllnvi ksvtrngrsi
     2401 iltavlalil vylfsivgyl ffkddfilev drlpnetagp etgeslandf lysdvcrvet
     2461 genctspapk eellpveete qdkehtcetl lmcivtvlsh glrsgggvgd vlrkpskeep
     2521 lfaarviydl lfffmviiiv lnlifgviid tfadlrsekq kkeeilkttc ficglerdkf
     2581 dnktvtfeeh ikeehnmwhy lcfivlvkvk dsteytgpes yvaemirern ldwfprmram
     2641 slvssdsege qnelrnlqek lestmklvtn lsgqlselkd qmteqrkqkq rigllghpph
     2701 mnvnpqqpa
//
LOCUS       NP_001258175             102 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 7 [Rattus norvegicus].
ACCESSION   NP_001258175
VERSION     NP_001258175.1
DBSOURCE    REFSEQ: accession NM_001271246.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 102)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 102)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 102)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1 and FM089481.1.
            
            Transcript Variant: This variant (7) differs in 5' UTR and 5'
            coding region, compared to variant 3. This results in a protein
            (isoform 7) that has a shorter N-terminus compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM099298.1, FM089481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..102
                     /product="cAMP-responsive element modulator isoform 7"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=11406
     Region          46..100
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          47..99
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(47,51,53..55,57..59,61..62,64..66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(65,68,72..73,75..76,79..80,82..83,86,89..90,93..94,
                     96..97)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..102
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271246.1:223..531"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 maaatgdmpt yqirapttal pqgvvmaasp gslhspqqla eeatrkrelr lmknreaare
       61 crrkkkeyvk clenrvavle nqnktlieel kalkdlychk ae
//
LOCUS       NP_001177404            1478 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001177404
VERSION     NP_001177404.2
DBSOURCE    REFSEQ: accession NM_001190475.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1478)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1478)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1478)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1478)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1478)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1478)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1478)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1478)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1478)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081153.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            On Oct 7, 2014 this sequence version replaced NP_001177404.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            3' coding region, compared to variant 1. The resulting isoform (2)
            is shorter, compared to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081153.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1478
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1478
                     /product="adhesion G protein-coupled receptor L2 isoform 2
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=162838
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          422..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Site            791
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          792..841
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            828..829
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098; propagated
                     from UniProtKB/Swiss-Prot (O88923.2)"
     Region          848..1120
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            885..905
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            912..932
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            957..977
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            995..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1056..1078
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1057..1077
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1082..1107
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1082..1102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1119..1478
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     Region          1130..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1377..1419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            1393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     CDS             1..1478
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001190475.2:463..4899"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleninny rvcdgyyntd lpgswvlgaf allcllgltw sfgllfvnee
     1081 tvvmaylfta fnafqglfif ifhcalqkkv rkeyakcfrh wyccgglpte sphssvkast
     1141 srtsaryssg tqsrirrmwn dtvrkqsess fisgdinsts tlnqgmtgny lltnpllrph
     1201 gtnnpyntll aetvvcnaps apvfnspghs lnntrdtsam dtlplngnfn nsyslrkady
     1261 hdgvqvvdcg lslndtafek miiselvhnn lrgsnkthnl elklpvkpvi ggssseddai
     1321 vadasslmhg dnpglefrhk eleaplipqr thsllyqpqk kvkpeatdsy vsqltaeade
     1381 hlqspnrdsl ytsmpnlrds pypesspdma edlspsrrse nediyyksmp nlgagrqlqm
     1441 cyqisrgnsd gyiipinkeg cipegdvreg qmqlvtsl
//
LOCUS       NP_001100814             445 aa            linear   ROD 27-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MYLIP [Rattus norvegicus].
ACCESSION   NP_001100814 XP_001059193 XP_225220
VERSION     NP_001100814.2
DBSOURCE    REFSEQ: accession NM_001107344.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Wang,W., Zhang,Z.Z., Wu,Y., Wang,R.Q., Chen,J.W., Chen,J.,
            Zhang,Y., Chen,Y.J., Geng,M., Xu,Z.D., Dai,M., Li,J.H. and Pan,L.L.
  TITLE     (-)-Epigallocatechin-3-Gallate Ameliorates Atherosclerosis and
            Modulates Hepatic Lipid Metabolic Gene Expression in Apolipoprotein
            E Knockout Mice: Involvement of TTC39B
  JOURNAL   Front Pharmacol 9, 195 (2018)
   PUBMED   29593532
  REMARK    Erratum:[Front Pharmacol. 2018 May 01;9:459. doi:
            10.3389/fphar.2018.00459. PMID: 29745376]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Liu,S. and Vaziri,N.D.
  TITLE     Role of PCSK9 and IDOL in the pathogenesis of acquired LDL receptor
            deficiency and hypercholesterolemia in nephrotic syndrome
  JOURNAL   Nephrol Dial Transplant 29 (3), 538-543 (2014)
   PUBMED   24166456
  REMARK    GeneRIF: LDLR deficiency, hypercholesterolemia and elevated plasma
            LDL in NS are associated with upregulation of PCSK9 and IDOL.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Do,H.T., Bruelle,C., Tselykh,T., Jalonen,P., Korhonen,L. and
            Lindholm,D.
  TITLE     Reciprocal regulation of very low density lipoprotein receptors
            (VLDLRs) in neurons by brain-derived neurotrophic factor (BDNF) and
            Reelin: involvement of the E3 ligase Mylip/Idol
  JOURNAL   J Biol Chem 288 (41), 29613-29620 (2013)
   PUBMED   23990472
  REMARK    GeneRIF: Data indicate that down-regulation of Mylip/Idol using
            shRNAs abrogated the decrease in VLDLRs induced by Reelin.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Zhang,L., Fairall,L., Goult,B.T., Calkin,A.C., Hong,C.,
            Millard,C.J., Tontonoz,P. and Schwabe,J.W.
  TITLE     The IDOL-UBE2D complex mediates sterol-dependent degradation of the
            LDL receptor
  JOURNAL   Genes Dev 25 (12), 1262-1274 (2011)
   PUBMED   21685362
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Zelcer,N., Hong,C., Boyadjian,R. and Tontonoz,P.
  TITLE     LXR regulates cholesterol uptake through Idol-dependent
            ubiquitination of the LDL receptor
  JOURNAL   Science 325 (5936), 100-104 (2009)
   PUBMED   19520913
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Bornhauser,B.C., Johansson,C. and Lindholm,D.
  TITLE     Functional activities and cellular localization of the ezrin,
            radixin, moesin (ERM) and RING zinc finger domains in MIR
  JOURNAL   FEBS Lett 553 (1-2), 195-199 (2003)
   PUBMED   14550572
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Olsson,P.A., Korhonen,L., Mercer,E.A. and Lindholm,D.
  TITLE     MIR is a novel ERM-like protein that interacts with myosin
            regulatory light chain and inhibits neurite outgrowth
  JOURNAL   J Biol Chem 274 (51), 36288-36292 (1999)
   PUBMED   10593918
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Sep 21, 2012 this sequence version replaced NP_001100814.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1061984.1,
                                           SRR26360190.1841985.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..445
                     /product="E3 ubiquitin-protein ligase MYLIP"
                     /EC_number="2.3.2.27"
                     /note="idol; inducible degrader of the LDL-receptor;
                     RING-type E3 ubiquitin transferase MYLIP"
                     /calculated_mol_wt=49759
     Region          1..81
                     /region_name="FERM_F1_MYLIP"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in E3 ubiquitin-protein
                     ligase MYLIP and similar proteins; cd17104"
                     /db_xref="CDD:340624"
     Region          5..190
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          185..295
                     /region_name="FERM_C_MYLIP_IDOL"
                     /note="FERM domain C-lobe of E3 ubiquitin ligase myosin
                     regulatory light chain-interacting protein (MYLIP; also
                     called inducible degrader of the LDL receptor, IDOL);
                     cd13195"
                     /db_xref="CDD:270016"
     Site            order(194,211,213,220)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270016"
     Site            order(224,229..232,265,269,272..273)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270016"
     Site            265..276
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270016"
     Region          341..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZDI6.1)"
     Region          383..434
                     /region_name="RING-HC_MYLIP"
                     /note="RING finger, HC subclass, found in myosin
                     regulatory light chain interacting protein (MYLIP) and
                     similar proteins; cd16523"
                     /db_xref="CDD:438186"
     Site            order(383,388..392,414..415,419,422)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438186"
     Site            order(384,399..405,430..434)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438186"
     Region          431..433
                     /region_name="Critical for homodimerization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZDI6.1)"
     CDS             1..445
                     /gene="Mylip"
                     /gene_synonym="MIR"
                     /coded_by="NM_001107344.2:227..1564"
                     /db_xref="GeneID:306825"
                     /db_xref="RGD:1305761"
ORIGIN      
        1 mlcyvtrpda vlmeveveak angedclnqv crrlgiievd yfglqftgsk geslwlnlrn
       61 risqqmdgla pyrlklrvkf fvephlilqe qtrhifflhi kesllaghlq cspeqavels
      121 allaqtkfgd ynqntaqysy edlcekelss stlnsivgkh kelegisqas aeyqvlqivs
      181 amenygiewh avrdsegqkl ligvgpegis ickedfspin riaypvvqma tqsgknvylt
      241 vtkesgnsiv llfkmistra asglyraite thafyrcdtv tsavmmqysr dlkghlaslf
      301 lneninlgkk yvfdikrtsk evydharral ynagvvdlvs rndqsppssp lkssdssmsc
      361 ssceglscqq trvlqeklrk lkeamlcmvc ceeeinstfc pcghtvcces caaqlqscpv
      421 crsrvehvqh vylpthtsll nltvi
//
LOCUS       NP_001292101            1172 aa            linear   ROD 27-APR-2025
DEFINITION  protein diaphanous homolog 3 [Rattus norvegicus].
ACCESSION   NP_001292101 XP_001074393 XP_002728345
VERSION     NP_001292101.1
DBSOURCE    REFSEQ: accession NM_001305172.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1172)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1172)
  AUTHORS   Baarlink,C., Wang,H. and Grosse,R.
  TITLE     Nuclear actin network assembly by formins regulates the SRF
            coactivator MAL
  JOURNAL   Science 340 (6134), 864-867 (2013)
   PUBMED   23558171
REFERENCE   3  (residues 1 to 1172)
  AUTHORS   Schoen,C.J., Emery,S.B., Thorne,M.C., Ammana,H.R., Sliwerska,E.,
            Arnett,J., Hortsch,M., Hannan,F., Burmeister,M. and Lesperance,M.M.
  TITLE     Increased activity of Diaphanous homolog 3 (DIAPH3)/diaphanous
            causes hearing defects in humans with auditory neuropathy and in
            Drosophila
  JOURNAL   Proc Natl Acad Sci U S A 107 (30), 13396-13401 (2010)
   PUBMED   20624953
  REMARK    GeneRIF: Data suggest that genetic testing for DIAPH3 may be useful
            for individuals with recessive as well as dominant inheritance of
            nonsyndromic auditory neuropathy.
REFERENCE   4  (residues 1 to 1172)
  AUTHORS   Miki,T., Okawa,K., Sekimoto,T., Yoneda,Y., Watanabe,S., Ishizaki,T.
            and Narumiya,S.
  TITLE     mDia2 shuttles between the nucleus and the cytoplasm through the
            importin-{alpha}/{beta}- and CRM1-mediated nuclear transport
            mechanism
  JOURNAL   J Biol Chem 284 (9), 5753-5762 (2009)
   PUBMED   19117945
REFERENCE   5  (residues 1 to 1172)
  AUTHORS   Mironova,E. and Millette,C.F.
  TITLE     Expression of the diaphanous-related formin proteins mDia1 and
            mDia2 in the rat testis
  JOURNAL   Dev Dyn 237 (8), 2170-2176 (2008)
   PUBMED   18651670
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On or before Feb 27, 2015 this sequence version replaced
            XP_002728345.2, XP_001074393.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760389
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1172
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q12"
     Protein         1..1172
                     /product="protein diaphanous homolog 3"
                     /note="diaphanous homolog 3"
                     /calculated_mol_wt=133703
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          16..39
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q9Z207"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LVW7.4)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSV4; propagated from
                     UniProtKB/Swiss-Prot (F1LVW7.4)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSV4; propagated from
                     UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          57..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          94..277
                     /region_name="Drf_GBD"
                     /note="Diaphanous GTPase-binding Domain; pfam06371"
                     /db_xref="CDD:461886"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSV4; propagated from
                     UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          285..472
                     /region_name="Drf_FH3"
                     /note="Diaphanous FH3 Domain; pfam06367"
                     /db_xref="CDD:461885"
     Region          535..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          616..988
                     /region_name="FH2"
                     /note="Formin Homology 2 Domain; pfam02181"
                     /db_xref="CDD:396655"
     Region          1000..>1062
                     /region_name="Casc1_N"
                     /note="Cancer susceptibility candidate 1 N-terminus;
                     pfam15927"
                     /db_xref="CDD:464947"
     Site            1073
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSV4; propagated from
                     UniProtKB/Swiss-Prot (F1LVW7.4)"
     Site            1158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NSV4; propagated from
                     UniProtKB/Swiss-Prot (F1LVW7.4)"
     Region          1163..1172
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:Q9Z207"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LVW7.4)"
     CDS             1..1172
                     /gene="Diaph3"
                     /gene_synonym="Diap3; DRF3; mDIA2"
                     /coded_by="NM_001305172.1:65..3583"
                     /db_xref="GeneID:290396"
                     /db_xref="RGD:1593287"
ORIGIN      
        1 mekhraralg rdskasrrkg lpsappagpy elgekrpklh lnirtltddm ldkfasirip
       61 kgskkerppl pqlktvsgss dyssvssetm ennpkslsen evlklfekmm edmnlnedkk
      121 aplrekdfsi kkemvmqyin tasktgslrs srqispqefi helkmgytge rlftyleslr
      181 vsltsnpvsw vqnfgheglg llldilekli ngqiqekvvk ktqhkviqcl ralmntqygl
      241 erimsdersl sllakamdpk qpsmmadvvk llsavcivge esileevlea ltsageerki
      301 drffsivegl rhnsvqlqva cmqlinalvt spddldfrlh lrnefmrcgl keilpnlkgi
      361 kndgldiqlk vfdehkeedl sefshrfedi raefdeasdv ysvvwdtvke traeghfvsi
      421 lqhlllirnd rfirqqyfkl idecvsqivl hrdgidpdft yrkrldldls qfvdvcidqa
      481 kleeweekas ehckkfekec tdhqetqaql qkkeakinel qaelqafksq fgalppgtki
      541 plqtsakgep gpsafppapp algagvpppp pppppppppl pgmampfggp vppppplgfl
      601 ggqnfiplnl pfglkpkkef kpeismrrln wlkigpnems encfwikvne nkyenkdllc
      661 klentfccle kekrdtndfd ekkvikkrmk elkfldpkia qnlsiflssf rvpyekirtm
      721 ilevdeaqls esmiqnlmkh lpdeeqlksl sqfrsdynsl cepeqfavvm snvkrlrprl
      781 tailfklqfe eqvnninpdi mavstaceei kksksfskll elvllmgnym nagsrnaqtf
      841 gfdlsslckl kdtksadqkt tllhflvdvc eekhpdilpf vddlahldka srvsvemlek
      901 slkqmgrqll qleknletfp ppedlhdkfv ikmssfiita kehygklstl ldnmtqlyqs
      961 vmsyyavdtk kvsveeffnd lnnfrtsfmq alkenirkre aaekekrari akeraekerl
     1021 erqqekkrll emktegdetg vmdsllealq sgaafrdrrk rtpklkdirq slspmsqrpv
     1081 lkvcnhenqk mqlsegsrph hsinctstrt pvakelncnl dthtstgrik avekeacnae
     1141 snrkkemell gsvsksesvp eveallarlr al
//
LOCUS       NP_446249                690 aa            linear   ROD 27-APR-2025
DEFINITION  crooked neck-like protein 1 [Rattus norvegicus].
ACCESSION   NP_446249 NP_001316818 XP_003749628 XP_003753853
VERSION     NP_446249.1
DBSOURCE    REFSEQ: accession NM_053797.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Jayaraman,S.S., Rayhan,D.J., Hazany,S. and Kolodney,M.S.
  TITLE     Mutational landscape of basal cell carcinomas by whole-exome
            sequencing
  JOURNAL   J Invest Dermatol 134 (1), 213-220 (2014)
   PUBMED   23774526
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Chanarat,S. and Strasser,K.
  TITLE     Splicing and beyond: the many faces of the Prp19 complex
  JOURNAL   Biochim Biophys Acta 1833 (10), 2126-2134 (2013)
   PUBMED   23742842
  REMARK    Review article
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 690)
  AUTHORS   Amada,N., Tezuka,T., Mayeda,A., Araki,K., Takei,N., Todokoro,K. and
            Nawa,H.
  TITLE     A novel rat orthologue and homologue for the Drosophila crooked
            neck gene in neural stem cells and their immediate descendants
  JOURNAL   J Biochem 133 (5), 615-623 (2003)
   PUBMED   12801913
REFERENCE   6  (residues 1 to 690)
  AUTHORS   Raisin-Tani,S. and Leopold,P.
  TITLE     Drosophila crooked-neck protein co-fractionates in a multiprotein
            complex with splicing factors
  JOURNAL   Biochem Biophys Res Commun 296 (2), 288-292 (2002)
   PUBMED   12163015
REFERENCE   7  (residues 1 to 690)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
REFERENCE   8  (residues 1 to 690)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC085718.1.
            
            On or before May 21, 2021 this sequence version replaced
            NP_001316818.1, XP_003749628.1, XP_003753853.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC085718.1 [ECO:0000345]
            RNAseq introns           :: mixed sample support SAMD00132261,
                                        SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..690
                     /product="crooked neck-like protein 1"
                     /note="crooked neck homolog; Crn, crooked neck-like 1;
                     crooked neck-like protein 1-like; crooked neck pre-mRNA
                     splicing factor-like 1; crooked neck-like 1 protein-like"
                     /calculated_mol_wt=83285
     Region          61..93
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          84..109
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(85..86,89..90,92,116,119..120,123..124,126..127,150,
                     153..154,157..158,161)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..281
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          95..127
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          114..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          129..161
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          149..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..194
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          196..227
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          196..227
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          229..264
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          250..467
                     /region_name="Mediates interaction with HSP90.
                     /evidence=ECO:0000250|UniProtKB:P63154"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          319..563
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZJ0; propagated from
                     UniProtKB/Swiss-Prot (P63155.1)"
     Region          412..440
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(413,416..417,420..421,423,446,449..450,453..454,
                     456..457,480,483..484,487..488,491)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          445..474
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          459..491
                     /region_name="HAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          479..507
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          493..527
                     /region_name="HAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          529..560
                     /region_name="HAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          565..606
                     /region_name="HAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          608..646
                     /region_name="HAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          618..626
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          648..673
                     /region_name="HAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Region          667..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63155.1)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63154; propagated from
                     UniProtKB/Swiss-Prot (P63155.1)"
     CDS             1..690
                     /gene="Crnkl1"
                     /gene_synonym="Crn"
                     /coded_by="NM_053797.2:87..2159"
                     /db_xref="GeneID:100910202"
                     /db_xref="RGD:620507"
ORIGIN      
        1 maastaagkq ripkvakvkn kapaevqita eqllreaker elellppppq qkitdeeeln
       61 dyklrkrktf ednirknrtv isnwikyaqw eeslkeiqra rsiyeraldv dyrnitlwlk
      121 yaememknrq vnharniwdr aittlprvnq fwykytymee mlgnvagarq vferwmewqp
      181 eeqawhsyin felrykever artiyerfvl vhpavknwik yarfeekhay faharkvyer
      241 aveffgdehm dehlyvafak feenqkefer vrviykyald riskqeaqel fknytifekk
      301 fgdrrgiedi ivskrrfqye eevkanphny dawfdylrlv esdaeadtvr evyeraianv
      361 ppiqekrhwk ryiylwvnya lyeeleakdp ertrqvyqas leliphkkft fakmwlyyaq
      421 feirqknlpf arralgtsig kcpknklfkg yielelqlre fdrcrklyek flefgpenct
      481 swikfaelet ilgdierara iyelaisqpr ldmpevlwks yidfeieqee tertrnlyrq
      541 llqrtqhvkv wisfaqfels sgkegsvakc rqiyeeankt mrnceekeer lmlleswrsf
      601 edefgtvsdk ervdklmpek vkkrrkvqad dgsdagweey ydyifpedaa nqpnlkllam
      661 aklwkkqqqe reaaeqdpdk didesesssf
//
LOCUS       NP_598302                475 aa            linear   ROD 27-APR-2025
DEFINITION  trifunctional enzyme subunit beta, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_598302
VERSION     NP_598302.1
DBSOURCE    REFSEQ: accession NM_133618.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Seo,J.Y., Yaneva,R., Hinson,E.R. and Cresswell,P.
  TITLE     Human cytomegalovirus directly induces the antiviral protein
            viperin to enhance infectivity
  JOURNAL   Science 332 (6033), 1093-1097 (2011)
   PUBMED   21527675
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Asano,J., Kudo,T., Shimizu,T., Fan,Y., Nanashima,N., Yamana,D.,
            Miura,T., Yamada,T. and Tsuchida,S.
  TITLE     Histone acetylation and steroid receptor coactivator expression
            during clofibrate-induced rat hepatocarcinogenesis
  JOURNAL   Cancer Sci 101 (4), 869-875 (2010)
   PUBMED   20132223
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Liu,X., Wu,L., Deng,G., Li,N., Chu,X., Guo,F. and Li,D.
  TITLE     Characterization of mitochondrial trifunctional protein and its
            inactivation study for medicine development
  JOURNAL   Biochim Biophys Acta 1784 (11), 1742-1749 (2008)
   PUBMED   18640292
  REMARK    GeneRIF: The catalytic residues of the MTP beta-subunit are
            positioned in the active site similarly to those of monofunctional
            3-ketoacyl-CoA thiolase.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Bogenhagen,D.F., Rousseau,D. and Burke,S.
  TITLE     The layered structure of human mitochondrial DNA nucleoids
  JOURNAL   J Biol Chem 283 (6), 3665-3675 (2008)
   PUBMED   18063578
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Frackowiak,J., Mazur-Kolecka,B., Kaczmarski,W. and Dickson,D.
  TITLE     Deposition of Alzheimer's vascular amyloid-beta is associated with
            decreased expression of brain L-3-hydroxyacyl-coenzyme A
            dehydrogenase (ERAB)
  JOURNAL   Brain Res 907 (1-2), 44-53 (2001)
   PUBMED   11430884
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Eaton,S., Bursby,T., Middleton,B., Pourfarzam,M., Mills,K.,
            Johnson,A.W. and Bartlett,K.
  TITLE     The mitochondrial trifunctional protein: centre of a beta-oxidation
            metabolon?
  JOURNAL   Biochem Soc Trans 28 (2), 177-182 (2000)
   PUBMED   10816122
  REMARK    Review article
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Ushikubo,S., Aoyama,T., Kamijo,T., Wanders,R.J., Rinaldo,P.,
            Vockley,J. and Hashimoto,T.
  TITLE     Molecular characterization of mitochondrial trifunctional protein
            deficiency: formation of the enzyme complex is important for
            stabilization of both alpha- and beta-subunits
  JOURNAL   Am J Hum Genet 58 (5), 979-988 (1996)
   PUBMED   8651282
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Kamijo,T., Aoyama,T., Miyazaki,J. and Hashimoto,T.
  TITLE     Molecular cloning of the cDNAs for the subunits of rat
            mitochondrial fatty acid beta-oxidation multienzyme complex.
            Structural and functional relationships to other mitochondrial and
            peroxisomal beta-oxidation enzymes
  JOURNAL   J Biol Chem 268 (35), 26452-26460 (1993)
   PUBMED   8253773
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Uchida,Y., Izai,K., Orii,T. and Hashimoto,T.
  TITLE     Novel fatty acid beta-oxidation enzymes in rat liver mitochondria.
            II. Purification and properties of enoyl-coenzyme A (CoA)
            hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase
            trifunctional protein
  JOURNAL   J Biol Chem 267 (2), 1034-1041 (1992)
   PUBMED   1730633
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM050540.1, FM038662.1, JAXUCZ010000006.1, FM105991.1 and
            FM118580.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060545.1, D16479.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..475
                     /product="trifunctional enzyme subunit beta, mitochondrial
                     precursor"
                     /EC_number="2.3.1.16"
                     /EC_number="2.3.1.155"
                     /note="trifunctional enzyme subunit beta, mitochondrial;
                     mitochondrial trifunctional protein, beta subunit;
                     hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA
                     thiolase/enoyl-CoA hydratase (trifunctional protein), beta
                     subunit; hydroxyacyl-Coenzyme A
                     dehydrogenase/3-ketoacyl-Coenzyme A
                     thiolase/enoyl-Coenzyme A hydratase (trifunctional
                     protein), beta subunit"
                     /calculated_mol_wt=47584
     transit_peptide 1..34
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q60587.1)"
                     /calculated_mol_wt=3848
     mat_peptide     35..475
                     /product="Trifunctional enzyme subunit beta,
                     mitochondrial. /id=PRO_0000034084"
                     /note="propagated from UniProtKB/Swiss-Prot (Q60587.1)"
                     /calculated_mol_wt=47584
     Region          56..472
                     /region_name="thiolase"
                     /note="Thiolase are ubiquitous enzymes that catalyze the
                     reversible thiolytic cleavage of 3-ketoacyl-CoA into
                     acyl-CoA and acetyl-CoA, a 2-step reaction involving a
                     covalent intermediate formed with a catalytic cysteine.
                     They are found in prokaryotes and...; cd00751"
                     /db_xref="CDD:238383"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P55084; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            order(74,101,115,118,122,133..136,144,151..152,155,170,
                     341,343,345,366,462..463)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238383"
     Site            order(139,429,459)
                     /site_type="active"
                     /db_xref="CDD:238383"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P55084; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            294
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99JY0; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99JY0; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            333
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99JY0; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            349
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99JY0; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            362
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99JY0; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     Site            429
                     /site_type="other"
                     /note="Increases nucleophilicity of active site Cys.
                     /evidence=ECO:0000250|UniProtKB:P55084; propagated from
                     UniProtKB/Swiss-Prot (Q60587.1)"
     CDS             1..475
                     /gene="Hadhb"
                     /gene_synonym="TP-beta"
                     /coded_by="NM_133618.3:89..1516"
                     /db_xref="GeneID:171155"
                     /db_xref="RGD:620513"
ORIGIN      
        1 mttiltstfr nlsttskwal rfsvrplscs sqvqsapavq tkskktlakp nlknivvveg
       61 vripfllsgt sykdlmphdl araalsglly rtnipkdvvd yiifgtviqe vktsnvarea
      121 algagfsdkt pahtvtmaci ssnqamttav gliasgqcdv vvaggvelms dvpirhsrnm
      181 rkmmldlnka ktlaqrlsll tkfrlnflsp elpavaefst netmghsadr laaafavsrm
      241 eqdkyalrsh slakkaqdeg hlsdivpfkv pgkdtvskdn girpssleqm aklkpafikp
      301 ygtvtaanss fltdgasaml imsedralam gykpkaylrd fiyvsqdpkd qlllgptyat
      361 pkvlekaglt mndidafefh eafsgqilan fkamdsdwfa qnymgrktkv gapplekfni
      421 wggslslghp fgatgcrlvm aaanrlrkdg gqyalvaaca aggqghamiv eaypk
//
LOCUS       NP_001231713             236 aa            linear   ROD 27-APR-2025
DEFINITION  dual specificity protein phosphatase 15 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001231713
VERSION     NP_001231713.1
DBSOURCE    REFSEQ: accession NM_001244784.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Rodriguez-Molina,J.F., Lopez-Anido,C., Ma,K.H., Zhang,C., Olson,T.,
            Muth,K.N., Weider,M. and Svaren,J.
  TITLE     Dual specificity phosphatase 15 regulates Erk activation in Schwann
            cells
  JOURNAL   J Neurochem 140 (3), 368-382 (2017)
   PUBMED   27891578
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jeong,D.G., Wei,C.H., Ku,B., Jeon,T.J., Chien,P.N., Kim,J.K.,
            Park,S.Y., Hwang,H.S., Ryu,S.Y., Park,H., Kim,D.S., Kim,S.J. and
            Ryu,S.E.
  TITLE     The family-wide structure and function of human dual-specificity
            protein phosphatases
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 2), 421-435 (2014)
   PUBMED   24531476
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schmidt,F., van den Eijnden,M., Pescini Gobert,R., Saborio,G.P.,
            Carboni,S., Alliod,C., Pouly,S., Staugaitis,S.M., Dutta,R.,
            Trapp,B. and Hooft van Huijsduijnen,R.
  TITLE     Identification of VHY/Dusp15 as a regulator of oligodendrocyte
            differentiation through a systematic genomics approach
  JOURNAL   PLoS One 7 (7), e40457 (2012)
   PUBMED   22792334
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Friedberg,I., Nika,K., Tautz,L., Saito,K., Cerignoli,F.,
            Friedberg,I., Godzik,A. and Mustelin,T.
  TITLE     Identification and characterization of DUSP27, a novel
            dual-specific protein phosphatase
  JOURNAL   FEBS Lett 581 (13), 2527-2533 (2007)
   PUBMED   17498703
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB736780.1 and BC168211.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. The resulting isoform (2)
            lacks an internal segment, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168211.1, CK597849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..236
                     /product="dual specificity protein phosphatase 15 isoform
                     2"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="dual specificity protein phosphatase 15; dual
                     specificity phosphatase-like 15"
                     /calculated_mol_wt=26178
     Region          1..146
                     /region_name="DSP_DUSP15"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 15; cd14582"
                     /db_xref="CDD:350430"
     Region          178..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7B7.1)"
     CDS             1..236
                     /gene="Dusp15"
                     /coded_by="NM_001244784.1:207..917"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362238"
                     /db_xref="RGD:1305990"
ORIGIN      
        1 mgngmtkvlp glylgnfida kdpdqlgrnk ithivsihes pqpllqdity lrisvsdtpe
       61 vpikkhfkec vhfihscrln ggnclvhcfa gisrsttvvi ayvmtvtglg wqevleaika
      121 srpianpnpg frqqleefgw ansqklrrql eerfgeipfr deedlrallp lcrrcrqgpg
      181 tsapsattas saasegtlqr lvprspresh rplpllarvk qtffclprcl srkggk
//
LOCUS       NP_001011974             870 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001011974 XP_216383
VERSION     NP_001011974.2
DBSOURCE    REFSEQ: accession NM_001011974.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Carnegie,G.K., Means,C.K. and Scott,J.D.
  TITLE     A-kinase anchoring proteins: from protein complexes to physiology
            and disease
  JOURNAL   IUBMB Life 61 (4), 394-406 (2009)
   PUBMED   19319965
  REMARK    Review article
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Kinderman,F.S., Kim,C., von Daake,S., Ma,Y., Pham,B.Q.,
            Spraggon,G., Xuong,N.H., Jennings,P.A. and Taylor,S.S.
  TITLE     A dynamic mechanism for AKAP binding to RII isoforms of
            cAMP-dependent protein kinase
  JOURNAL   Mol Cell 24 (3), 397-408 (2006)
   PUBMED   17081990
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Tasken,K. and Aandahl,E.M.
  TITLE     Localized effects of cAMP mediated by distinct routes of protein
            kinase A
  JOURNAL   Physiol Rev 84 (1), 137-167 (2004)
   PUBMED   14715913
  REMARK    Review article
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Dong,F., Feldmesser,M., Casadevall,A. and Rubin,C.S.
  TITLE     Molecular characterization of a cDNA that encodes six isoforms of a
            novel murine A kinase anchor protein
  JOURNAL   J Biol Chem 273 (11), 6533-6541 (1998)
   PUBMED   9497389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On May 28, 2015 this sequence version replaced NP_001011974.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. This results in
            a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085790.1, SRR21887623.179007.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..870
                     /product="A-kinase anchor protein 2 isoform 2"
                     /note="A-kinase anchor protein 2; A kinase (PRKA) anchor
                     protein 2; paralemmin 2; paralemmin-2-like; A-kinase
                     anchoring protein 2"
                     /calculated_mol_wt=95811
     Region          14..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          103..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          233..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          409..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          506..577
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          576..589
                     /region_name="PKA-RII subunit binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          595..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          <613..810
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          <721..862
                     /region_name="AKAP2_C"
                     /note="A-kinase anchor protein 2 C-terminus; pfam15304"
                     /db_xref="CDD:464630"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Region          740..814
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2D5; propagated from
                     UniProtKB/Swiss-Prot (Q5U301.1)"
     CDS             1..870
                     /gene="Pakap"
                     /gene_synonym="AKAP-2; Akap2; Palm2"
                     /coded_by="NM_001011974.2:196..2808"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298024"
                     /db_xref="RGD:1305135"
ORIGIN      
        1 meigvsvaec ksvpgitstp hskdhsspfy spshnglltd hhesldndva reiqyldevl
       61 eanccdssvd gtyngisspe pgaailvssl gspahsatkv epiekasgrq lpphielsrs
      121 psdsmaeger anghstdqpq dmlgnslqap aspssstssh cssrdgeftl ttlkkeakfe
      181 lrafhedkkp sklfeedehe keqfcirkvr pseemielek errelirsqa vkknpgiaak
      241 wwnppqekti eeqldeehle shrkykerke kraqqeqlql qqqqqqqlqq lqqlqqqqqq
      301 qlstsqlcta paahehldsi ehtkedvvte qidfsaarkq fqqmensrqt lakgqstprl
      361 fsikpfykpl gsinsdkppt ilrpatiggt vedsstqaak eqkalcvses qsagagtgna
      421 atqgkegpys epskrgplsk lwaedgefts aravltvvkd edhgildqfs rsvnvsltqe
      481 eldsgldels vrsqdttvle tlsndfsmdn isdsgasnet pnalqensla dfslpqtpqt
      541 dnpsegregv sksfsdhgfy spsstlgdsp svddpleyqa gllvqnaiqq aiaeqvdkae
      601 vhtskegseq qepgamveea gsqapgsekp qgmfappqvs spvqekrdvl pkilpgedkt
      661 lrekgpsqpp tavqpsgpvn mketrpeggy fskyseaael rstasllatq esdvmvgpfk
      721 lrsrkqrtls mieeeiraaq ereeelkrqr qvrqstpspr aqnapslpsr ttcyktapgk
      781 iekvkpppsp ttegpslqpd lapeeaagaq rpknlmqtlm edyethkskr rermddssvl
      841 eatrvnrrks alalrweagi yanqeeedne
//
LOCUS       NP_001012069             475 aa            linear   ROD 27-APR-2025
DEFINITION  tesmin [Rattus norvegicus].
ACCESSION   NP_001012069 XP_219583
VERSION     NP_001012069.2
DBSOURCE    REFSEQ: accession NM_001012069.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Sutou,S., Miwa,K., Matsuura,T., Kawasaki,Y., Ohinata,Y. and
            Mitsui,Y.
  TITLE     Native tesmin is a 60-kilodalton protein that undergoes dynamic
            changes in its localization during spermatogenesis in mice
  JOURNAL   Biol Reprod 68 (5), 1861-1869 (2003)
   PUBMED   12606435
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB708158.1 and BC083920.1.
            
            On Oct 4, 2011 this sequence version replaced NP_001012069.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132295, SAMD00132302
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q42"
     Protein         1..475
                     /product="tesmin"
                     /note="metallothionein-like 5, testis-specific (tesmin)"
                     /calculated_mol_wt=50338
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XHX9.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XHX9.2)"
     Region          334..371
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     CDS             1..475
                     /gene="Tesmin"
                     /gene_synonym="Mtl5"
                     /coded_by="NM_001012069.2:39..1466"
                     /db_xref="GeneID:309142"
                     /db_xref="RGD:1309788"
ORIGIN      
        1 medallgamt gpedelgael fgserafadg lalspaggaa drdelpvlad aylgatepge
       61 pllralsppp gaevpaallg dfpglpelrs sddaapppay svhvlssllp gargpallpl
      121 sagvrvipve ikeagggvpg sspedaafqa plaqescckf sssqeaeeas gcprkkdssp
      181 mvicqlkgga qmlcidncga relkalhllp qyddqssfpq selpkpmttl vgrllpvpak
      241 lnlitqvdng alpsavngaa fpsgpalqgp pkialagycd cfssgdfcns cscnnlrhel
      301 erfkaikacl drnpeafqpk mgkgrlgaak lrhskgcnck rsgclknyce cyeakitcss
      361 ickciackny eesperkmlm stphymepgd fesshhlspa kfsgpprlrk nrqafscisw
      421 evveatcacl laqgeeaeqe rcspslaeqm vleefgrcls qilhiefksk glkie
//
LOCUS       NP_001181880             121 aa            linear   ROD 27-APR-2025
DEFINITION  chromosome transmission fidelity protein 8 homolog [Rattus
            norvegicus].
ACCESSION   NP_001181880
VERSION     NP_001181880.1
DBSOURCE    REFSEQ: accession NM_001194951.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Bermudez,V.P., Maniwa,Y., Tappin,I., Ozato,K., Yokomori,K. and
            Hurwitz,J.
  TITLE     The alternative Ctf18-Dcc1-Ctf8-replication factor C complex
            required for sister chromatid cohesion loads proliferating cell
            nuclear antigen onto DNA
  JOURNAL   Proc Natl Acad Sci U S A 100 (18), 10237-10242 (2003)
   PUBMED   12930902
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI044989.1 and JAXUCZ010000019.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.64553.1,
                                           SRR26643297.51601.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840112 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..121
                     /product="chromosome transmission fidelity protein 8
                     homolog"
                     /note="chromosome transmission fidelity factor 8 homolog;
                     CTF8, chromosome transmission fidelity factor 8 homolog"
                     /calculated_mol_wt=13197
     Region          13..113
                     /region_name="Ctf8"
                     /note="pfam09696"
                     /db_xref="CDD:430758"
     CDS             1..121
                     /gene="Chtf8"
                     /gene_synonym="Ctf8; Derpc; RGD1306894"
                     /coded_by="NM_001194951.1:49..414"
                     /db_xref="GeneID:364996"
                     /db_xref="RGD:1306894"
ORIGIN      
        1 mvqivisstg aeglaewvlm elqgeieary stglagnllg dlhyttegip vlivghhily
       61 gkiihlekpf avlvkhtpgk qdcdelgret gtqylvtali knkilfktrp kpiitnvpkk
      121 v
//
LOCUS       NP_542947                202 aa            linear   ROD 27-APR-2025
DEFINITION  lymphotoxin-alpha precursor [Rattus norvegicus].
ACCESSION   NP_542947 XP_001077049
VERSION     NP_542947.1
DBSOURCE    REFSEQ: accession NM_080769.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   James Bates,R.E., Browne,E., Schalks,R., Jacobs,H., Tan,L.,
            Parekh,P., Magliozzi,R., Calabrese,M., Mazarakis,N.D. and
            Reynolds,R.
  TITLE     Lymphotoxin-alpha expression in the meninges causes lymphoid tissue
            formation and neurodegeneration
  JOURNAL   Brain 145 (12), 4287-4307 (2022)
   PUBMED   35776111
  REMARK    GeneRIF: Lymphotoxin-alpha expression in the meninges causes
            lymphoid tissue formation and neurodegeneration.
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Guo,Z., Qiu,C., Mecca,C., Zhang,Y., Bian,J., Wang,Y., Wu,X.,
            Wang,T., Su,W., Li,X., Zhang,W., Chen,B. and Xiang,H.
  TITLE     Elevated lymphotoxin-alpha (TNFbeta) is associated with
            intervertebral disc degeneration
  JOURNAL   BMC Musculoskelet Disord 22 (1), 77 (2021)
   PUBMED   33441130
  REMARK    GeneRIF: Elevated lymphotoxin-alpha (TNFbeta) is associated with
            intervertebral disc degeneration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Suna,S., Sakata,Y., Nakatani,D., Okuda,K., Shimizu,M., Usami,M.,
            Matsumoto,S., Hara,M., Ozaki,K., Mizuno,H., Minamino,T.,
            Takashima,S., Nishino,M., Matsumura,Y., Takeda,H., Tanaka,T.,
            Sato,H., Hori,M. and Komuro,I.
  TITLE     Decreased mortality associated with statin treatment in patients
            with acute myocardial infarction and lymphotoxin-alpha C804A
            polymorphism
  JOURNAL   Atherosclerosis 227 (2), 373-379 (2013)
   PUBMED   23398946
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Murdaca,G., Colombo,B.M., Contini,P. and Puppo,F.
  TITLE     Determination of lymphotoxin-alpha levels in patients with
            psoriatic arthritis undergoing etanercept treatment
  JOURNAL   J Interferon Cytokine Res 32 (6), 277-279 (2012)
   PUBMED   22480318
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Peric,A., Vojvodic,D. and Vukomanovic-Durdevid,B.
  TITLE     Influence of allergy on clinical, immunological and histological
            characteristics of nasal polyposis
  JOURNAL   B-ENT 8 (1), 25-32 (2012)
   PUBMED   22545387
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Issazadeh,S., Ljungdahl,A., Hojeberg,B., Mustafa,M. and Olsson,T.
  TITLE     Cytokine production in the central nervous system of Lewis rats
            with experimental autoimmune encephalomyelitis: dynamics of mRNA
            expression for interleukin-10, interleukin-12, cytolysin, tumor
            necrosis factor alpha and tumor necrosis factor beta
  JOURNAL   J Neuroimmunol 61 (2), 205-212 (1995)
   PUBMED   7593556
REFERENCE   7  (residues 1 to 202)
  AUTHORS   Badenhoop,K., Schwarz,G., Schleusener,H., Weetman,A.P., Recks,S.,
            Peters,H., Bottazzo,G.F. and Usadel,K.H.
  TITLE     Tumor necrosis factor beta gene polymorphisms in Graves' disease
  JOURNAL   J Clin Endocrinol Metab 74 (2), 287-291 (1992)
   PUBMED   1346144
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Liu,S.K., Jakowatz,J.G., Pollack,R.B., Ceraldi,C., Yamamoto,R.,
            Dett,C., Lopez,F., Camacho,C., Carson,W.E., Sentovich,S.M. et al.
  TITLE     Effects of intracarotid and intravenous infusion of human TNF and
            LT on established intracerebral rat gliomas
  JOURNAL   Lymphokine Cytokine Res 10 (3), 189-194 (1991)
   PUBMED   1883913
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Imagawa,D.K., Millis,J.M., Olthoff,K.M., Seu,P., Dempsey,R.A.,
            Hart,J., Terasaki,P.I. and Busuttil,R.W.
  TITLE     Anti-tumor necrosis factor antibody enhances allograft survival in
            rats
  JOURNAL   J Surg Res 48 (4), 345-348 (1990)
   PUBMED   2338821
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Namba,Y. and Waksman,B.H.
  TITLE     Regulatory substances produced by lymphocytes. II. Lymphotoxin in
            the rat
  JOURNAL   J Immunol 115 (4), 1018-1022 (1975)
   PUBMED   1080770
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883046.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001077049.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..202
                     /product="lymphotoxin-alpha precursor"
                     /note="tumor necrosis factor beta; LT-alpha; TNF-beta;
                     tumor necrosis factor ligand superfamily member 1;
                     lymphotoxin A; lymphotoxin alpha (TNF superfamily, member
                     1); lymphotoxin-alpha-like"
                     /calculated_mol_wt=18651
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3478
     mat_peptide     34..202
                     /product="Lymphotoxin-alpha. /id=PRO_0000034471"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06332.1)"
                     /calculated_mol_wt=18651
     Site            order(63,105,107,165,170,196,200)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Region          74..202
                     /region_name="TNF"
                     /note="TNF(Tumour Necrosis Factor) family; pfam00229"
                     /db_xref="CDD:425540"
     Site            order(77..78,83,129,136,141)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06332.1)"
     CDS             1..202
                     /gene="Lta"
                     /gene_synonym="Tnfb"
                     /coded_by="NM_080769.2:152..760"
                     /db_xref="GeneID:25008"
                     /db_xref="RGD:3020"
ORIGIN      
        1 mtplgrlhll rvlstppvfl lglllalplg aqglsgvrfs asrtahqppq khlthgllkp
       61 aahlvgypsk qnsllwrant draflrhgfs lnnnsllipt sglyfvysqv vfsgescspr
      121 aiptpiylah evqlfssqyp fhvpllsaqk svypglqgpw vrsmyqgavf llskgdqlst
      181 htdgishlhf spstvffgaf al
//
LOCUS       NP_001292924             376 aa            linear   ROD 27-APR-2025
DEFINITION  A-kinase anchor protein 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001292924
VERSION     NP_001292924.1
DBSOURCE    REFSEQ: accession NM_001305995.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Carnegie,G.K., Means,C.K. and Scott,J.D.
  TITLE     A-kinase anchoring proteins: from protein complexes to physiology
            and disease
  JOURNAL   IUBMB Life 61 (4), 394-406 (2009)
   PUBMED   19319965
  REMARK    Review article
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Kinderman,F.S., Kim,C., von Daake,S., Ma,Y., Pham,B.Q.,
            Spraggon,G., Xuong,N.H., Jennings,P.A. and Taylor,S.S.
  TITLE     A dynamic mechanism for AKAP binding to RII isoforms of
            cAMP-dependent protein kinase
  JOURNAL   Mol Cell 24 (3), 397-408 (2006)
   PUBMED   17081990
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Tasken,K. and Aandahl,E.M.
  TITLE     Localized effects of cAMP mediated by distinct routes of protein
            kinase A
  JOURNAL   Physiol Rev 84 (1), 137-167 (2004)
   PUBMED   14715913
  REMARK    Review article
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Dong,F., Feldmesser,M., Casadevall,A. and Rubin,C.S.
  TITLE     Molecular characterization of a cDNA that encodes six isoforms of a
            novel murine A kinase anchor protein
  JOURNAL   J Biol Chem 273 (11), 6533-6541 (1998)
   PUBMED   9497389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.16603.1,
                                           SRR26360194.819909.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..376
                     /product="A-kinase anchor protein 2 isoform 3"
                     /note="A-kinase anchor protein 2; A kinase (PRKA) anchor
                     protein 2; paralemmin 2; paralemmin-2-like; A-kinase
                     anchoring protein 2"
                     /calculated_mol_wt=41924
     Region          15..333
                     /region_name="Paralemmin"
                     /note="pfam03285"
                     /db_xref="CDD:460875"
     CDS             1..376
                     /gene="Pakap"
                     /gene_synonym="AKAP-2; Akap2; Palm2"
                     /coded_by="NM_001305995.1:208..1338"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:298024"
                     /db_xref="RGD:1305135"
ORIGIN      
        1 maeaelhker lqaiaekrkr qteiegkrqq ldeqvlllqh skskvlrekw llqgvpagta
       61 eeeearrrqs eedefkvkql edniqrleqe iqaleseesq isakeqiile klketeksfk
      121 dlqksfstad gaiyameinv ekdkqtgetk ilsastigpe gvhqrgvkvy ddgtkvvyev
      181 hsggtvveng vhklsakdve eliqkagqss frghmsertv vadgslghpk ehmlckeakl
      241 emvqksrkdq ssgnpghqaq ppstegpevn ldqpvtmifm gyqniedeee tkkvlgydet
      301 ikaelvlide ddekslrekt vtdvstidgn aaelvsgrpm sdttepsspe dkeeslatdp
      361 apgtqkkkrc qccvvm
//
LOCUS       NP_113932                490 aa            linear   ROD 27-APR-2025
DEFINITION  monocarboxylate transporter 3 [Rattus norvegicus].
ACCESSION   NP_113932
VERSION     NP_113932.2
DBSOURCE    REFSEQ: accession NM_031744.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Wilson,M.C., Meredith,D., Fox,J.E., Manoharan,C., Davies,A.J. and
            Halestrap,A.P.
  TITLE     Basigin (CD147) is the target for organomercurial inhibition of
            monocarboxylate transporter isoforms 1 and 4: the ancillary protein
            for the insensitive MCT2 is EMBIGIN (gp70)
  JOURNAL   J Biol Chem 280 (29), 27213-27221 (2005)
   PUBMED   15917240
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Philp,N.J., Yoon,H. and Grollman,E.F.
  TITLE     Monocarboxylate transporter MCT1 is located in the apical membrane
            and MCT3 in the basal membrane of rat RPE
  JOURNAL   Am J Physiol 274 (6), R1824-R1828 (1998)
   PUBMED   9841555
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On May 9, 2012 this sequence version replaced NP_113932.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760433, SAMN06621351
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..490
                     /product="monocarboxylate transporter 3"
                     /note="solute carrier family 16 (monocarboxylic acid
                     transporters), member 8; solute carrier family 16, member
                     8 (monocarboxylic acid transporter 3); solute carrier
                     family 16 (monocarboxylate transporter), member 8"
                     /calculated_mol_wt=51152
     Region          14..440
                     /region_name="2A0113"
                     /note="monocarboxylate transporter 1; TIGR00892"
                     /db_xref="CDD:273325"
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            173..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            319..339
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            353..373
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Site            387..407
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Region          419..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Region          426..460
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000250|UniProtKB:O95907"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     Region          461..480
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000250|UniProtKB:O95907"
                     /note="propagated from UniProtKB/Swiss-Prot (O70461.2)"
     CDS             1..490
                     /gene="Slc16a8"
                     /gene_synonym="Mct3"
                     /coded_by="NM_031744.2:212..1684"
                     /db_xref="GeneID:65200"
                     /db_xref="RGD:69282"
ORIGIN      
        1 mgaggprrga gppdggwgwv vlgacfvitg faygfpkavs vffrelkrdf gagysdtawv
       61 ssimlamlyg tgplssilvt rfgcrpvmla ggllasagmi lasfasrlle lyltagvltg
      121 lglalnfqps limlglyfer rrplanglaa agspvflstl splgqllger fgwrggfllf
      181 gglllhccac gavmrpppgp qprpdpappg grarhrqlld lavctdrtfm vymvtkflma
      241 lglfvpaill vnyakdagvp daeaafllsi vgfvdivarp acgalaglgr lrphvpylfs
      301 lallangltd lisararsyg tlvafciafg lsygmvgalq fevlmatvga prfpsalglv
      361 llveavavli gppsagrlvd alknyeiify lagsevvlag vfmavttycc qrcskdippg
      421 psaeggtsdt edveaerdse pmpasteepg slealevlsp ragspepeee avpdlshesv
      481 ggheahgqna
//
LOCUS       NP_001071136             205 aa            linear   ROD 27-APR-2025
DEFINITION  dr1-associated corepressor [Rattus norvegicus].
ACCESSION   NP_001071136 XP_001073347 XP_215177
VERSION     NP_001071136.1
DBSOURCE    REFSEQ: accession NM_001077668.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Iratni,R., Yan,Y.T., Chen,C., Ding,J., Zhang,Y., Price,S.M.,
            Reinberg,D. and Shen,M.M.
  TITLE     Inhibition of excess nodal signaling during mouse gastrulation by
            the transcriptional corepressor DRAP1
  JOURNAL   Science 298 (5600), 1996-1999 (2002)
   PUBMED   12471260
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127524.1.
            
            On or before Nov 15, 2006 this sequence version replaced
            XP_215177.1, XP_001073347.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127524.1, CB324434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..205
                     /product="dr1-associated corepressor"
                     /note="NC2-alpha; Dr1 associated protein 1 (negative
                     cofactor 2 alpha); dr1-associated protein 1; negative
                     co-factor 2-alpha; negative cofactor 2-alpha"
                     /calculated_mol_wt=22195
     Region          9..83
                     /region_name="HFD_DRAP1"
                     /note="histone-fold domain found in Dr1-associated protein
                     1 (DRAP1) and similar proteins; cd22906"
                     /db_xref="CDD:467031"
     Site            order(10,12..13,16,19..21,23..24,26..27,29..31,34,36..37,
                     40..42,44..47,50..51,54,64..67,70..71,74)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467031"
     Region          <13..163
                     /region_name="HAP5"
                     /note="CCAAT-binding factor, subunit C [Transcription];
                     COG5208"
                     /db_xref="CDD:227533"
     Site            order(15,18..19,29)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:467031"
     Site            order(22,24,26..29)
                     /site_type="other"
                     /note="TBP binding site [polypeptide binding]"
                     /db_xref="CDD:467031"
     Region          91..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP1.1)"
     CDS             1..205
                     /gene="Drap1"
                     /coded_by="NM_001077668.2:206..823"
                     /db_xref="GeneID:293674"
                     /db_xref="RGD:1308477"
ORIGIN      
        1 mpskkkkyna rfpparikki mqtdeeigkv aaavpviisr alelflesll kkacqvtqsr
       61 naktmttshl kqcieleqqf dflkdlvasv pdmqgdgedn htdgdkgprr grkpgssgrk
      121 nggtgskskd kklsgtdseq edesedtdtd geeetpqapp qashppahfq spptpfmpft
      181 splplppapp gpsapeaede edyds
//
LOCUS       NP_001257595             259 aa            linear   ROD 27-APR-2025
DEFINITION  troponin T, fast skeletal muscle isoform 2 [Rattus norvegicus].
ACCESSION   NP_001257595
VERSION     NP_001257595.1
DBSOURCE    REFSEQ: accession NM_001270666.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schilder,R.J., Kimball,S.R., Marden,J.H. and Jefferson,L.S.
  TITLE     Body weight-dependent troponin T alternative splicing is
            evolutionarily conserved from insects to mammals and is partially
            impaired in skeletal muscle of obese rats
  JOURNAL   J Exp Biol 214 (Pt 9), 1523-1532 (2011)
   PUBMED   21490260
  REMARK    GeneRIF: Weight-dependent quantitative variation in Tnnt3
            alternative splicing appears to be an evolutionarily conserved
            feature of skeletal muscle.
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Robinson,P., Lipscomb,S., Preston,L.C., Altin,E., Watkins,H.,
            Ashley,C.C. and Redwood,C.S.
  TITLE     Mutations in fast skeletal troponin I, troponin T, and
            beta-tropomyosin that cause distal arthrogryposis all increase
            contractile function
  JOURNAL   FASEB J 21 (3), 896-905 (2007)
   PUBMED   17194691
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Gallon,C.E., Tschirgi,M.L. and Chandra,M.
  TITLE     Differences in myofilament calcium sensitivity in rat psoas fibers
            reconstituted with troponin T isoforms containing the alpha- and
            beta-exons
  JOURNAL   Arch Biochem Biophys 456 (2), 127-134 (2006)
   PUBMED   16839517
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Brotto,M.A., Biesiadecki,B.J., Brotto,L.S., Nosek,T.M. and Jin,J.P.
  TITLE     Coupled expression of troponin T and troponin I isoforms in single
            skeletal muscle fibers correlates with contractility
  JOURNAL   Am J Physiol Cell Physiol 290 (2), C567-C576 (2006)
   PUBMED   16192301
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Mukhopadhyay,S., Langsetmo,K., Stafford,W.F. 3rd, Henry,G.D.,
            Baleja,J.D. and Sarkar,S.
  TITLE     Identification of a region of fast skeletal troponin T required for
            stabilization of the coiled-coil formation with troponin I
  JOURNAL   J Biol Chem 280 (1), 538-547 (2005)
   PUBMED   15507453
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Behrens,O., Wedeking-Schohl,H., Mesrogli,M., Degenhardt,F. and
            Schneider,J.
  TITLE     [Doppler ultrasound in monitoring twin pregnancies with early
            discordant growth]
  JOURNAL   Z Geburtshilfe Perinatol 196 (5), 209-212 (1992)
   PUBMED   1299083
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Breitbart,R.E. and Nadal-Ginard,B.
  TITLE     Complete nucleotide sequence of the fast skeletal troponin T gene.
            Alternatively spliced exons exhibit unusual interspecies divergence
  JOURNAL   J Mol Biol 188 (3), 313-324 (1986)
   PUBMED   3735424
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Breitbart,R.E., Nguyen,H.T., Medford,R.M., Destree,A.T., Mahdavi,V.
            and Nadal-Ginard,B.
  TITLE     Intricate combinatorial patterns of exon splicing generate multiple
            regulated troponin T isoforms from a single gene
  JOURNAL   Cell 41 (1), 67-82 (1985)
   PUBMED   2986851
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Medford,R.M., Nguyen,H.T., Destree,A.T., Summers,E. and
            Nadal-Ginard,B.
  TITLE     A novel mechanism of alternative RNA splicing for the
            developmentally regulated generation of troponin T isoforms from a
            single gene
  JOURNAL   Cell 38 (2), 409-421 (1984)
   PUBMED   6205765
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Garfinkel,L.I., Periasamy,M. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of cDNA sequences corresponding to
            myosin light chains 1, 2, and 3, troponin-C, troponin-T,
            alpha-tropomyosin, and alpha-actin
  JOURNAL   J Biol Chem 257 (18), 11078-11086 (1982)
   PUBMED   6179945
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and CB612473.1.
            
            Transcript Variant: This variant (2) and variant 1 represent the
            longest transcripts and encode the longest isoforms (2 and 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..259
                     /product="troponin T, fast skeletal muscle isoform 2"
                     /note="troponin T, fast skeletal muscle; fTnT; tnTf; fast
                     skeletal muscle troponin T; troponin T type 3 (skeletal,
                     fast); troponin T3, skeletal, fast"
                     /calculated_mol_wt=30618
     Region          63..199
                     /region_name="Troponin"
                     /note="pfam00992"
                     /db_xref="CDD:460018"
     CDS             1..259
                     /gene="Tnnt3"
                     /gene_synonym="Tnt"
                     /coded_by="NM_001270666.1:117..896"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24838"
                     /db_xref="RGD:3883"
ORIGIN      
        1 msdeeteqve eqyeeeeeaq eeevqeeape peevqeeekp rpkltapkip egekvdfddi
       61 qkkrqnkdlm elqalidshf earkkeeeel ialkeriekr raeraeqqri raekererqn
      121 rlaeekarre eedakrraed dlkkkkalss mganyssyla kadqkrgkkq taremkkkil
      181 aerrkplnid hlsddklrdk akelwdtlyq letdkfefge klkrqkydim tvrarvemla
      241 kfskkagata kgkvggrwk
//
LOCUS       NP_001296227             218 aa            linear   ROD 27-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001296227
VERSION     NP_001296227.1
DBSOURCE    REFSEQ: accession NM_001309298.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   O'Donnell,B.M., Mackie,T.D., Subramanya,A.R. and Brodsky,J.L.
  TITLE     Endoplasmic reticulum-associated degradation of the renal potassium
            channel, ROMK, leads to type II Bartter syndrome
  JOURNAL   J Biol Chem 292 (31), 12813-12827 (2017)
   PUBMED   28630040
  REMARK    GeneRIF: Data suggest underlying pathology for some patients with
            type II Bartter syndrome is linked to stability of ROMK1 in ERAD
            pathway; using a yeast expression system, cells can be rescued by
            wild-type (rat) ROMK1 but not by ROMK1 containing any one of four
            mutations found in (human) type II Bartter syndrome; mutant ROMKs
            are significantly less stable than wild-type ROMK. (ERAD =
            endoplasmic reticulum-associated degradation)
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Araujo,M., Welch,W.J., Zhou,X., Sullivan,K., Walsh,S., Pasternak,A.
            and Wilcox,C.S.
  TITLE     Inhibition of ROMK blocks macula densa tubuloglomerular feedback
            yet causes renal vasoconstriction in anesthetized rats
  JOURNAL   Am J Physiol Renal Physiol 312 (6), F1120-F1127 (2017)
   PUBMED   28228405
  REMARK    GeneRIF: Blockade of ROMK or Na(+)-K(+)-2Cl(-) transport inhibits
            tubuloglomerular feedback yet increases renal vascular resistance.
            The renal vasoconstriction was independent of volume depletion,
            blood pressure, TGF, or proximal tubule hydrostatic pressure.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Smoot,B., Kober,K.M., Paul,S.M., Levine,J.D., Abrams,G.,
            Mastick,J., Topp,K., Conley,Y.P. and Miaskowski,C.A.
  TITLE     Potassium Channel Candidate Genes Predict the Development of
            Secondary Lymphedema Following Breast Cancer Surgery
  JOURNAL   Nurs Res 66 (2), 85-94 (2017)
   PUBMED   28252570
  REMARK    GeneRIF: These preliminary findings suggest that K channel genes
            play a role in the development of secondary lymphedema
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Bollepalli,M.K., Fowler,P.W., Rapedius,M., Shang,L., Sansom,M.S.,
            Tucker,S.J. and Baukrowitz,T.
  TITLE     State-dependent network connectivity determines gating in a K+
            channel
  JOURNAL   Structure 22 (7), 1037-1046 (2014)
   PUBMED   24980796
  REMARK    GeneRIF: Data indicate that mutations in kir1.1 potassium channel
            preferentially increase pH sensitivity.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Hu,J., Qiu,S., Yang,F., Cao,Z., Li,W. and Wu,Y.
  TITLE     Unique mechanism of the interaction between honey bee toxin TPNQ
            and rKir1.1 potassium channel explored by computational
            simulations: insights into the relative insensitivity of channel
            towards animal toxins
  JOURNAL   PLoS One 8 (7), e67213 (2013)
   PUBMED   23874410
  REMARK    GeneRIF: The TPNQ toxin-rKir1.1 channel complex structure not only
            revealed their unique interaction mechanism, but also elucidate the
            relative insensitivity of rKir1.1 channel towards animal toxins.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Beesley,A.H., Ortega,B. and White,S.J.
  TITLE     Splicing of a retained intron within ROMK K+ channel RNA generates
            a novel set of isoforms in rat kidney
  JOURNAL   Am J Physiol 276 (3), C585-C592 (1999)
   PUBMED   10069985
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Derst,C., Konrad,M., Kockerling,A., Karolyi,L., Deschenes,G.,
            Daut,J., Karschin,A. and Seyberth,H.W.
  TITLE     Mutations in the ROMK gene in antenatal Bartter syndrome are
            associated with impaired K+ channel function
  JOURNAL   Biochem Biophys Res Commun 230 (3), 641-645 (1997)
   PUBMED   9015377
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Boim,M.A., Ho,K., Shuck,M.E., Bienkowski,M.J., Block,J.H.,
            Slightom,J.L., Yang,Y., Brenner,B.M. and Hebert,S.C.
  TITLE     ROMK inwardly rectifying ATP-sensitive K+ channel. II. Cloning and
            distribution of alternative forms
  JOURNAL   Am J Physiol 268 (6 Pt 2), F1132-F1140 (1995)
   PUBMED   7611454
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Zhou,H., Tate,S.S. and Palmer,L.G.
  TITLE     Primary structure and functional properties of an epithelial K
            channel
  JOURNAL   Am J Physiol 266 (3 Pt 1), C809-C824 (1994)
   PUBMED   8166245
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Ho,K., Nichols,C.G., Lederer,W.J., Lytton,J., Vassilev,P.M.,
            Kanazirska,M.V. and Hebert,S.C.
  TITLE     Cloning and expression of an inwardly rectifying ATP-regulated
            potassium channel
  JOURNAL   Nature 362 (6415), 31-38 (1993)
   PUBMED   7680431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            Transcript Variant: This variant (3, also known as ROMK6.1)
            contains two alternate exons in the 5' UTR, lacks a portion of the
            5' coding region, and initiates translation at a downstream start
            codon, compared to variant 1. It encodes isoform 3 which has a
            shorter N-terminus compared to isoform 1. Variants 3, 4 and 5
            encode the same protein (isoform 3).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF081368.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..218
                     /product="ATP-sensitive inward rectifier potassium channel
                     1 isoform 3"
                     /note="K+ channel protein; ATP-sensitive inward rectifier
                     potassium channel 1; ATP-regulated potassium channel
                     ROM-K; potassium channel, inwardly rectifying subfamily J
                     member 1; inward rectifier K(+) channel Kir1.1"
                     /calculated_mol_wt=24513
     Region          19..191
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..218
                     /gene="Kcnj1"
                     /gene_synonym="KAB-1; Kcnj; Kcnj1_v1; Kcnj1_v3; kir1.1;
                     ROMK1; ROMK2; ROMK3"
                     /coded_by="NM_001309298.1:615..1271"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24521"
                     /db_xref="RGD:2957"
ORIGIN      
        1 mcgailakis rpkkraktit fsknaviskr ggklcllirv anlrksllig shiygkllkt
       61 titpegetii ldqtninfvv dagnenlffi spltiyhiid hnspffhmaa etlsqqdfel
      121 vvfldgtves tsatcqvrts yvpeevlwgy rfvpivsktk egkyrvdfhn fgktvevetp
      181 hcamclynek dararmkrgy dnpnfvlsev detddtqm
//
LOCUS       NP_075415               1186 aa            linear   ROD 27-APR-2025
DEFINITION  arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
            [Rattus norvegicus].
ACCESSION   NP_075415 XP_001054911 XP_576238
VERSION     NP_075415.2
DBSOURCE    REFSEQ: accession NM_023026.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1186)
  AUTHORS   Jiang,Y., Liao,L., Shrestha,C., Ji,S., Chen,Y., Peng,J., Wang,L.,
            Liao,E. and Xie,Z.
  TITLE     Reduced expression of E-cadherin and p120-catenin and elevated
            expression of PLC-gamma1 and PIKE are associated with
            aggressiveness of oral squamous cell carcinoma
  JOURNAL   Int J Clin Exp Pathol 8 (8), 9042-9051 (2015)
   PUBMED   26464646
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1186)
  AUTHORS   Chan,C.B., Liu,X., Zhao,L., Liu,G., Lee,C.W., Feng,Y. and Ye,K.
  TITLE     PIKE is essential for oligodendroglia development and CNS
            myelination
  JOURNAL   Proc Natl Acad Sci U S A 111 (5), 1993-1998 (2014)
   PUBMED   24449917
  REMARK    GeneRIF: PIKE plays pivotal roles to advance oligodendroglia
            development and myelinogenesis through Akt/mTOR activation.
REFERENCE   3  (residues 1 to 1186)
  AUTHORS   Dwane,S., Durack,E., O'Connor,R. and Kiely,P.A.
  TITLE     RACK1 promotes neurite outgrowth by scaffolding AGAP2 to FAK
  JOURNAL   Cell Signal 26 (1), 9-18 (2014)
   PUBMED   24056044
  REMARK    GeneRIF: RACK1 scaffolds AGAP2 to FAK to regulate FAK activity and
            cell adhesion during the differentiation process.
REFERENCE   4  (residues 1 to 1186)
  AUTHORS   Chan,C.B., Chen,Y., Liu,X., Papale,L., Escayg,A., Mei,L. and Ye,K.
  TITLE     Essential role of PIKE GTPases in neuronal protection against
            excitotoxic insults
  JOURNAL   Adv Biol Regul 52 (1), 66-76 (2012)
   PUBMED   21925531
REFERENCE   5  (residues 1 to 1186)
  AUTHORS   Chan,C.B., Chen,Y., Liu,X., Tang,X., Lee,C.W., Mei,L. and Ye,K.
  TITLE     PIKE-mediated PI3-kinase activity is required for AMPA receptor
            surface expression
  JOURNAL   EMBO J 30 (20), 4274-4286 (2011)
   PUBMED   21847098
  REMARK    GeneRIF: PIKE is a critical factor in controlling synaptic AMPA
            receptor insertion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1186)
  AUTHORS   Xia,C., Ma,W., Stafford,L.J., Liu,C., Gong,L., Martin,J.F. and
            Liu,M.
  TITLE     GGAPs, a new family of bifunctional GTP-binding and
            GTPase-activating proteins
  JOURNAL   Mol Cell Biol 23 (7), 2476-2488 (2003)
   PUBMED   12640130
REFERENCE   7  (residues 1 to 1186)
  AUTHORS   Nie,Z., Stanley,K.T., Stauffer,S., Jacques,K.M., Hirsch,D.S.,
            Takei,J. and Randazzo,P.A.
  TITLE     AGAP1, an endosome-associated, phosphoinositide-dependent
            ADP-ribosylation factor GTPase-activating protein that affects
            actin cytoskeleton
  JOURNAL   J Biol Chem 277 (50), 48965-48975 (2002)
   PUBMED   12388557
REFERENCE   8  (residues 1 to 1186)
  AUTHORS   Ye,K., Aghdasi,B., Luo,H.R., Moriarity,J.L., Wu,F.Y., Hong,J.J.,
            Hurt,K.J., Bae,S.S., Suh,P.G. and Snyder,S.H.
  TITLE     Phospholipase C gamma 1 is a physiological guanine nucleotide
            exchange factor for the nuclear GTPase PIKE
  JOURNAL   Nature 415 (6871), 541-544 (2002)
   PUBMED   11823862
REFERENCE   9  (residues 1 to 1186)
  AUTHORS   Ye,K., Hurt,K.J., Wu,F.Y., Fang,M., Luo,H.R., Hong,J.J.,
            Blackshaw,S., Ferris,C.D. and Snyder,S.H.
  TITLE     Pike. A nuclear gtpase that enhances PI3kinase activity and is
            regulated by protein 4.1N
  JOURNAL   Cell 103 (6), 919-930 (2000)
   PUBMED   11136977
REFERENCE   10 (residues 1 to 1186)
  AUTHORS   Yamane,O., Hayashi,T., Sako,S., Kihara,T. and Koyama,M.
  TITLE     Studies on hemorrhagic diathesis of experimental bovine bracken
            poisoning. I. Detection of circulating anticoagulants
  JOURNAL   Nihon Juigaku Zasshi 37 (4), 335-340 (1975)
   PUBMED   1238857
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF280816.1, AY128688.1 and JAXUCZ010000007.1.
            
            On or before Sep 25, 2009 this sequence version replaced
            XP_001054911.1, XP_576238.2, NP_075415.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY128688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1186
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..1186
                     /product="arf-GAP with GTPase, ANK repeat and PH
                     domain-containing protein 2"
                     /note="centaurin, gamma 1; AGAP-2; cnt-g1; nuclear GTPase
                     PIKE; phosphatidylinositol 3-kinase enhancer"
                     /calculated_mol_wt=124307
     Region          1..23
                     /region_name="Interaction with EPB41L1.
                     /evidence=ECO:0000269|PubMed:11136977"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          24..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          <37..174
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          180..225
                     /region_name="Interactions with HOMER1 and NF2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          262..384
                     /region_name="Interaction with PLCG1.
                     /evidence=ECO:0000269|PubMed:11823862"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          399..566
                     /region_name="G domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          401..560
                     /region_name="Centaurin_gamma"
                     /note="Centaurin gamma (CENTG) GTPase; cd04103"
                     /db_xref="CDD:133303"
     Site            407..414
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133303"
     Site            order(409..415,453,456,509..510,512,542..543)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133303"
     Site            428..436
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133303"
     Site            431
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133303"
     Site            453..456
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133303"
     Site            455..468
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133303"
     Site            509..512
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133303"
     Site            542..544
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133303"
     Region          576..613
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          628..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99490; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          668..908
                     /region_name="PH_AGAP"
                     /note="Arf-GAP with GTPase, ANK repeat and PH
                     domain-containing protein Pleckstrin homology (PH) domain;
                     cd01250"
                     /db_xref="CDD:241281"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          759..784
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          800..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            921
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          926..1033
                     /region_name="ArfGap_AGAP"
                     /note="ArfGAP with GTPase domain, ANK repeat and PH
                     domains; cd08836"
                     /db_xref="CDD:350065"
     Site            order(940,943,960,963,968)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350065"
     Site            order(940,943,960,963)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350065"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHD9; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          <1082..>1141
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1084..1115
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1084..1113
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          1117..1146
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Region          1117..1142
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1145..1174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CGU4.1)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8CGU4.1)"
     CDS             1..1186
                     /gene="Agap2"
                     /gene_synonym="Centg1; Pike"
                     /coded_by="NM_023026.2:1..3561"
                     /db_xref="GeneID:65218"
                     /db_xref="RGD:628844"
ORIGIN      
        1 msrgagalqr rtttylislt lvklesvppp ppspsaaavg apgargsepr dpgsprgaee
       61 pgkkrherlf hrqdalwist ssagaggaep palspapasp arpvspapgr rlslwaappg
      121 pplsgglspd skpggapsss rrpllsspsw ggpepegrtg ggvpgsssph pgtgsrrlkv
      181 appppapkpf ktvttsgaka gggkgagsrl swpesegkpr vkgskstagt gasavaaggg
      241 gsaavttsgg vgagagargk lsprkgkskt ldnsdlhpgp sagsppltvp aipvpatsvt
      301 aastqplgpa ppitleppap glkrgreggr astrdrkmlk fisgiftkst ggppgpgplp
      361 gpqglssssg srellgaelr aspkavvnsq ewtlsrsipe lrlgvlgdvr sgksslihrf
      421 ltgsyqvlek peseqykkem lvdgqthlvl ireeagapda kfsgwadavi fvfsledess
      481 fqavshlhgq lislrgegrg glalalvgtq drisassprv vgdararalc tdmkrcsyye
      541 tcatyglnvd rvfqevaqkv vtlrkqqqll aackslpssp shsaastpva gqasngghts
      601 dyssslpssp nvghrelrae aaavaglstp gslhraakrr tslfanrrgs dsekrsldsr
      661 gettgsgrai pikqsfllkr sgnslnkewk kkyvtlssng fllyhpsind yihsthgkem
      721 dllrttvkvp gkrppraisa fgpsasingl vkdmstvqmg egpeastpmp spspspsslq
      781 lptdqtskhl lkpdrnlara lstdctpsgd lsplsreppp spmvkkqrrk klstpskteg
      841 savqaeakrk mwklksfgsl rniykaeenf eflivsstgq twhfeaasfe erdawvqaie
      901 sqilaslqcc esskvklrtd sqseavaiqa irnakgnstc vdcgapnptw aslnlgalic
      961 iecsgihrnl gthlsrvrsl dlddwprelt lvltaigndt anrvwesdtr grakptrdss
     1021 reereswira kyeqllflap lgtteeplgr qlwaaveaqd vaavllllah arhgpldtsv
     1081 edpqlrsplh laaelahvvi tqlllwygad vaardaqgrt alfyarqags qlcadillqh
     1141 gcpgeggsta ttpsaattps itatpsprrr ssaaslgrvd ttialv
//
LOCUS       NP_001139227            1218 aa            linear   ROD 27-APR-2025
DEFINITION  NACHT, LRR and PYD domains-containing protein 1a allele 1 [Rattus
            norvegicus].
ACCESSION   NP_001139227 XP_001080037 XP_340836
VERSION     NP_001139227.2
DBSOURCE    REFSEQ: accession NM_001145755.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1218)
  AUTHORS   Jia,J., Liu,H., Sun,L., Xu,Y. and Zeng,X.
  TITLE     Thioredoxin-1 Protects Neurons Through Inhibiting NLRP1-Mediated
            Neuronal Pyroptosis in Models of Alzheimer's Disease
  JOURNAL   Mol Neurobiol 61 (11), 9723-9734 (2024)
   PUBMED   38976128
  REMARK    GeneRIF: Thioredoxin-1 Protects Neurons Through Inhibiting
            NLRP1-Mediated Neuronal Pyroptosis in Models of Alzheimer's
            Disease.
            Erratum:[Mol Neurobiol. 2025 May;62(5):6626. doi:
            10.1007/s12035-024-04523-8. PMID: 39333348]
REFERENCE   2  (residues 1 to 1218)
  AUTHORS   Liu,X., Song,W., Yu,Y., Su,J., Shi,X., Yang,X., Wang,H., Liu,P. and
            Zou,L.
  TITLE     Inhibition of NLRP1-Dependent Pyroptosis Prevents Glycogen Synthase
            Kinase-3beta Overactivation-Induced Hyperphosphorylated Tau in Rats
  JOURNAL   Neurotox Res 40 (5), 1163-1173 (2022)
   PUBMED   35951283
  REMARK    GeneRIF: Inhibition of NLRP1-Dependent Pyroptosis Prevents Glycogen
            Synthase Kinase-3beta Overactivation-Induced Hyperphosphorylated
            Tau in Rats.
REFERENCE   3  (residues 1 to 1218)
  AUTHORS   Huang,M., Zhang,X., Toh,G.A., Gong,Q., Wang,J., Han,Z., Wu,B.,
            Zhong,F. and Chai,J.
  TITLE     Structural and biochemical mechanisms of NLRP1 inhibition by DPP9
  JOURNAL   Nature 592 (7856), 773-777 (2021)
   PUBMED   33731929
  REMARK    GeneRIF: Structural and biochemical mechanisms of NLRP1 inhibition
            by DPP9.
REFERENCE   4  (residues 1 to 1218)
  AUTHORS   Zong,J., Zhang,H., Li,F.F., Liang,K., Liu,J.L., Xu,L.H. and
            Qian,W.H.
  TITLE     NLRP1 promotes TGF-beta1-induced myofibroblast differentiation in
            neonatal rat cardiac fibroblasts
  JOURNAL   J Mol Histol 49 (5), 509-518 (2018)
   PUBMED   30120609
  REMARK    GeneRIF: NLRP1 promoted myofibroblast differentiation and excessive
            ECM production in TGF-beta1-induced neonatal cardiac fibroblasts
            through directly targeting TGF-beta1/Smad signaling pathways.
REFERENCE   5  (residues 1 to 1218)
  AUTHORS   Zhong,F.L., Mamai,O., Sborgi,L., Boussofara,L., Hopkins,R.,
            Robinson,K., Szeverenyi,I., Takeichi,T., Balaji,R., Lau,A., Tye,H.,
            Roy,K., Bonnard,C., Ahl,P.J., Jones,L.A., Baker,P.J., Lacina,L.,
            Otsuka,A., Fournie,P.R., Malecaze,F., Lane,E.B., Akiyama,M.,
            Kabashima,K., Connolly,J.E., Masters,S.L., Soler,V.J., Omar,S.S.,
            McGrath,J.A., Nedelcu,R., Gribaa,M., Denguezli,M., Saad,A.,
            Hiller,S. and Reversade,B.
  TITLE     Germline NLRP1 Mutations Cause Skin Inflammatory and Cancer
            Susceptibility Syndromes via Inflammasome Activation
  JOURNAL   Cell 167 (1), 187-202 (2016)
   PUBMED   27662089
REFERENCE   6  (residues 1 to 1218)
  AUTHORS   Munding,C., Keller,M., Niklaus,G., Papin,S., Tschopp,J., Werner,S.
            and Beer,H.D.
  TITLE     The estrogen-responsive B box protein: a novel enhancer of
            interleukin-1beta secretion
  JOURNAL   Cell Death Differ 13 (11), 1938-1949 (2006)
   PUBMED   16575408
REFERENCE   7  (residues 1 to 1218)
  AUTHORS   Boyden,E.D. and Dietrich,W.F.
  TITLE     Nalp1b controls mouse macrophage susceptibility to anthrax lethal
            toxin
  JOURNAL   Nat Genet 38 (2), 240-244 (2006)
   PUBMED   16429160
REFERENCE   8  (residues 1 to 1218)
  AUTHORS   Liu,F., Lo,C.F., Ning,X., Kajkowski,E.M., Jin,M., Chiriac,C.,
            Gonzales,C., Naureckiene,S., Lock,Y.W., Pong,K., Zaleska,M.M.,
            Jacobsen,J.S., Silverman,S. and Ozenberger,B.A.
  TITLE     Expression of NALP1 in cerebellar granule neurons stimulates
            apoptosis
  JOURNAL   Cell Signal 16 (9), 1013-1021 (2004)
   PUBMED   15212762
REFERENCE   9  (residues 1 to 1218)
  AUTHORS   Martinon,F., Burns,K. and Tschopp,J.
  TITLE     The inflammasome: a molecular platform triggering activation of
            inflammatory caspases and processing of proIL-beta
  JOURNAL   Mol Cell 10 (2), 417-426 (2002)
   PUBMED   12191486
REFERENCE   10 (residues 1 to 1218)
  AUTHORS   Hlaing,T., Guo,R.F., Dilley,K.A., Loussia,J.M., Morrish,T.A.,
            Shi,M.M., Vincenz,C. and Ward,P.A.
  TITLE     Molecular cloning and characterization of DEFCAP-L and -S, two
            isoforms of a novel member of the mammalian Ced-4 family of
            apoptosis proteins
  JOURNAL   J Biol Chem 276 (12), 9230-9238 (2001)
   PUBMED   11076957
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Feb 16, 2013 this sequence version replaced NP_001139227.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript from the same strain was
            available for the full length of the gene. The extent of this
            transcript is supported by transcript alignments and orthologous
            data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM060637.1, HM060634.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1218
                     /product="NACHT, LRR and PYD domains-containing protein 1a
                     allele 1"
                     /note="resistant anthrax lethal toxin; NACHT, leucine rich
                     repeat and PYD containing 1; NLR family, pyrin domain
                     containing 1; NLR family protein 1; NACHT, LRR and PYD
                     domains-containing protein 1; NACHT, LRR and PYD
                     domains-containing protein 1a"
                     /calculated_mol_wt=138262
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          175..344
                     /region_name="NACHT"
                     /note="NACHT domain; pfam05729"
                     /db_xref="CDD:428606"
     Region          343..364
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          414..468
                     /region_name="NOD2_WH"
                     /note="NOD2 winged helix domain; pfam17779"
                     /db_xref="CDD:465501"
     Region          470..581
                     /region_name="NLRC4_HD2"
                     /note="NLRC4 helical domain HD2; pfam17776"
                     /db_xref="CDD:465499"
     Region          <664..>785
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          673..693
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          674..695
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          703..730
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          730..750
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          731..759
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          760..780
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          799..842
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          835..968
                     /region_name="ZU5. /evidence=ECO:0000250|UniProtKB:Q9C000"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          856..1108
                     /region_name="FIIND"
                     /note="Function to find; pfam13553"
                     /db_xref="CDD:463919"
     Site            942
                     /site_type="other"
                     /note="Trigger for autolytic processing.
                     /evidence=ECO:0000269|PubMed:33731929; propagated from
                     UniProtKB/Swiss-Prot (D9I2F9.1)"
     Site            968..969
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01174,
                     ECO:0000269|PubMed:33731929; propagated from
                     UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          969..1118
                     /region_name="UPA. /evidence=ECO:0000250|UniProtKB:Q9C000"
                     /note="propagated from UniProtKB/Swiss-Prot (D9I2F9.1)"
     Region          1128..1208
                     /region_name="CARD_ASC_NALP1"
                     /note="Caspase activation and recruitment domain found in
                     Human ASC, NALP1, and similar proteins; cd08330"
                     /db_xref="CDD:260039"
     CDS             1..1218
                     /gene="Nlrp1a"
                     /gene_synonym="Nalp1; Nlrp1"
                     /coded_by="NM_001145755.2:43..3699"
                     /db_xref="GeneID:360557"
                     /db_xref="RGD:1310963"
ORIGIN      
        1 meesqskqes ntrvaqhgsq qdvdptfqtk ralekerskp rprplprvql qslpgwssts
       61 ndvplsqlir emdhesrrci hrskkkldrs ehisqgtipe iyekrketis htqsmeqkyl
      121 fqnftkllll qkccpggsek lvreswhpcv peegghmiei qdlfdpnldt ekkpqlviie
      181 gaagigkstl arqvkrawde gqlyrdrfqh vfffscrela qckqlslael iaqgqevpta
      241 ptrqilsrpe kllfildgid epawvledqn pelcvhwsqa qpvhtllgsl lgksilpeas
      301 lmltarttal qklvpslgqp hrvevlgfse ferkdyfyky fakerntiid fnligsipvl
      361 ltlcevpwvc wllctclekq mqqgevlslt sqtttalclk ylsltipgqh lstqlrtlcs
      421 laaegicqrr tlfsksdlck qglaedaiat flkigvlqrq psslsysfah lclqeffaam
      481 syiledseea hgdmgndrtv etlverygrq nlfeaptvrf llgllntrem remenifack
      541 fpwetklkll qsiigepfcq pchlglfhcl yenqeeellt etmlcfplta sgpnhmeatv
      601 fqtnvkrlvi qtdmelmvvt fcitfshvrs lrlkgkgqqe ykltapamvl yrwtpiseas
      661 wkvlfsnlkc trnleeldls gnplsysavr slctalrqpg crlktlwlvd cgltsrccsf
      721 lasmlsahsr laeldlrlnd lgdngvrqlc eglrnpacnl silrldqasl seqvitelra
      781 letknpklfi sstwmshmtm ptentdgees ltsskqqqqq sgdkhmeplg tdddfwgpsg
      841 pvstevvdre rnlyrvrlpm agsyhcpstg lhfvvtravt ieigfcawsq flhetplqhs
      901 hmvagplfdi kaehgavtav clphfvslqe gkvdsslfhv ahfqdhgmvl etparvephf
      961 avlenpsfsp mgvllrmipa vghfipitsi tliyyrlyle ditfhlylvp ndctirkaid
     1021 eeelkfqfvr inkpppvdal yvgsryivss skeveilpke lelcyrspre sqlfseiyvg
     1081 nigsginlql tdkkymnliw eallkpgdlr palprmasap kdapallhfv dqhreqlvar
     1141 vtsvdplldk lhglvlseed yetvraeatn qdkmrklfrg srswswdckd hfyqalketh
     1201 phlimdllek sggvsvrl
//
LOCUS       NP_001007092             350 aa            linear   ROD 27-APR-2025
DEFINITION  renin receptor precursor [Rattus norvegicus].
ACCESSION   NP_001007092 XP_001060853 XP_217592
VERSION     NP_001007092.1
DBSOURCE    REFSEQ: accession NM_001007091.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Taguchi,T., Kimura,K., Suzuki,A., Fujishima,R., Shimizu,N.,
            Hoshiyama,A., Masaki,T., Inoue,M., Kato,Y., Satomi,T., Takano,K.,
            Imada,T., Sasaki,S. and Miyatsuka,T.
  TITLE     ATP6AP2 is robustly expressed in pancreatic beta cells and
            neuroendocrine tumors, and plays a role in maintaining cellular
            viability
  JOURNAL   Sci Rep 13 (1), 9260 (2023)
   PUBMED   37286698
  REMARK    GeneRIF: ATP6AP2 is robustly expressed in pancreatic beta cells and
            neuroendocrine tumors, and plays a role in maintaining cellular
            viability.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Yildirim,D., Bender,O., Karagoz,Z.F., Helvacioglu,F., Bilgic,M.A.,
            Akcay,A. and Ruzgaresen,N.B.
  TITLE     Role of autophagy and evaluation the effects of microRNAs 214, 132,
            34c and prorenin receptor in a rat model of focal segmental
            glomerulosclerosis
  JOURNAL   Life Sci 280, 119671 (2021)
   PUBMED   34087284
  REMARK    GeneRIF: Role of autophagy and evaluation the effects of microRNAs
            214, 132, 34c and prorenin receptor in a rat model of focal
            segmental glomerulosclerosis.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Figueiredo,M., Daryadel,A., Sihn,G., Muller,D.N., Popova,E.,
            Rouselle,A., Nguyen,G., Bader,M. and Wagner,C.A.
  TITLE     The (pro)renin receptor (ATP6ap2) facilitates receptor-mediated
            endocytosis and lysosomal function in the renal proximal tubule
  JOURNAL   Pflugers Arch 473 (8), 1229-1246 (2021)
   PUBMED   34228176
  REMARK    GeneRIF: The (pro)renin receptor (ATP6ap2) facilitates
            receptor-mediated endocytosis and lysosomal function in the renal
            proximal tubule.
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Yu,S., Dong,X., Yang,M., Yu,Q., Xiong,J., Chen,J., Dong,B. and
            Su,Q.
  TITLE     (Pro)renin receptor involves in myocardial fibrosis and oxidative
            stress in diabetic cardiomyopathy via the PRR-YAP pathway
  JOURNAL   Sci Rep 11 (1), 3259 (2021)
   PUBMED   33547400
  REMARK    GeneRIF: (Pro)renin receptor involves in myocardial fibrosis and
            oxidative stress in diabetic cardiomyopathy via the PRR-YAP
            pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Urushihara,M., Kondo,S., Kinoshita,Y., Ozaki,N., Jamba,A.,
            Nagai,T., Fujioka,K., Hattori,T. and Kagami,S.
  TITLE     (Pro)renin receptor promotes crescent formation via the ERK1/2 and
            Wnt/beta-catenin pathways in glomerulonephritis
  JOURNAL   Am J Physiol Renal Physiol 319 (4), F571-F578 (2020)
   PUBMED   32830537
  REMARK    GeneRIF: (Pro)renin receptor promotes crescent formation via the
            ERK1/2 and Wnt/beta-catenin pathways in glomerulonephritis.
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Muller,D.N., Klanke,B., Feldt,S., Cordasic,N., Hartner,A.,
            Schmieder,R.E., Luft,F.C. and Hilgers,K.F.
  TITLE     (Pro)renin receptor peptide inhibitor 'handle-region' peptide does
            not affect hypertensive nephrosclerosis in Goldblatt rats
  JOURNAL   Hypertension 51 (3), 676-681 (2008)
   PUBMED   18212268
  REMARK    GeneRIF: Blockade of the (pro)renin receptor (P)RR with
            'handle-region' peptide (HRP) does not improve target organ damage
            in renovascular hypertensive rats.
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Huang,Y., Wongamorntham,S., Kasting,J., McQuillan,D., Owens,R.T.,
            Yu,L., Noble,N.A. and Border,W.
  TITLE     Renin increases mesangial cell transforming growth factor-beta1 and
            matrix proteins through receptor-mediated, angiotensin
            II-independent mechanisms
  JOURNAL   Kidney Int 69 (1), 105-113 (2006)
   PUBMED   16374430
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Ramser,J., Abidi,F.E., Burckle,C.A., Lenski,C., Toriello,H.,
            Wen,G., Lubs,H.A., Engert,S., Stevenson,R.E., Meindl,A.,
            Schwartz,C.E. and Nguyen,G.
  TITLE     A unique exonic splice enhancer mutation in a family with X-linked
            mental retardation and epilepsy points to a novel role of the renin
            receptor
  JOURNAL   Hum Mol Genet 14 (8), 1019-1027 (2005)
   PUBMED   15746149
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Ichihara,A., Hayashi,M., Kaneshiro,Y., Suzuki,F., Nakagawa,T.,
            Tada,Y., Koura,Y., Nishiyama,A., Okada,H., Uddin,M.N., Nabi,A.H.,
            Ishida,Y., Inagami,T. and Saruta,T.
  TITLE     Inhibition of diabetic nephropathy by a decoy peptide corresponding
            to the 'handle' region for nonproteolytic activation of prorenin
  JOURNAL   J Clin Invest 114 (8), 1128-1135 (2004)
   PUBMED   15489960
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Nguyen,G., Delarue,F., Burckle,C., Bouzhir,L., Giller,T. and
            Sraer,J.D.
  TITLE     Pivotal role of the renin/prorenin receptor in angiotensin II
            production and cellular responses to renin
  JOURNAL   J Clin Invest 109 (11), 1417-1427 (2002)
   PUBMED   12045255
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB188298.1.
            
            On or before Sep 18, 2011 this sequence version replaced
            XP_217592.5, XP_001060853.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB188298.1, BC079339.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..350
                     /product="renin receptor precursor"
                     /note="renin receptor; renin/prorenin receptor; ATPase,
                     H(+)-transporting, lysosomal-interacting protein 2;
                     ATPase, H+ transporting, lysosomal accessory protein 2"
                     /calculated_mol_wt=37427
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1673
     mat_peptide     18..350
                     /product="Renin receptor. /id=PRO_0000022206"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS4.1)"
                     /calculated_mol_wt=37427
     Region          255..350
                     /region_name="Renin_r"
                     /note="Renin receptor-like protein; pfam07850"
                     /db_xref="CDD:462287"
     Site            276..277
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000250|UniProtKB:O75787; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS4.1)"
     Site            278..279
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000250|UniProtKB:O75787; propagated from
                     UniProtKB/Swiss-Prot (Q6AXS4.1)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS4.1)"
     Region          346..350
                     /region_name="Mediates retrograde transport to the ER.
                     /evidence=ECO:0000250|UniProtKB:O75787"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXS4.1)"
     CDS             1..350
                     /gene="Atp6ap2"
                     /coded_by="NM_001007091.1:86..1138"
                     /db_xref="GeneID:302526"
                     /db_xref="RGD:1561269"
ORIGIN      
        1 mavlvvllss lvssalanef silrspgsvv frngnwpipg dripdvaals mgfsvkedls
       61 wpglavgnlf hrpratimvt vkgvdklalp tgsvisyple navpfsldsv ansihslfse
      121 etpvvlqlap seervymvgk ansvfedlsv tlrqlrnrlf qensvlnslp lnslsrnnev
      181 dllflselqv lhdissllsr hkhlakdhsp dlyslelagl delgkryged seqfrdasri
      241 lvdalqkfad dmyslyggna vvelvtvksf dtslvrksrt iletkqentq spynlaykyn
      301 leysvvfnlv lwimtglala viitsyniwn mdpgydsiiy rmtnqkirmd
//
LOCUS       NP_671743                578 aa            linear   ROD 27-APR-2025
DEFINITION  nuclear receptor subfamily 1 group D member 2 [Rattus norvegicus].
ACCESSION   NP_671743 XP_006251772
VERSION     NP_671743.2
DBSOURCE    REFSEQ: accession NM_147210.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Noh,S.G., Jung,H.J., Kim,S., Arulkumar,R., Kim,D.H., Park,D. and
            Chung,H.Y.
  TITLE     Regulation of Circadian Genes Nr1d1 and Nr1d2 in Sex-Different
            Manners during Liver Aging
  JOURNAL   Int J Mol Sci 23 (17), 10032 (2022)
   PUBMED   36077427
  REMARK    GeneRIF: Regulation of Circadian Genes Nr1d1 and Nr1d2 in
            Sex-Different Manners during Liver Aging.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Pariollaud,M., Gibbs,J.E., Hopwood,T.W., Brown,S., Begley,N.,
            Vonslow,R., Poolman,T., Guo,B., Saer,B., Jones,D.H., Tellam,J.P.,
            Bresciani,S., Tomkinson,N.C., Wojno-Picon,J., Cooper,A.W.,
            Daniels,D.A., Trump,R.P., Grant,D., Zuercher,W., Willson,T.M.,
            MacDonald,A.S., Bolognese,B., Podolin,P.L., Sanchez,Y., Loudon,A.S.
            and Ray,D.W.
  TITLE     Circadian clock component REV-ERBalpha controls homeostatic
            regulation of pulmonary inflammation
  JOURNAL   J Clin Invest 128 (6), 2281-2296 (2018)
   PUBMED   29533925
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Amador,A., Campbell,S., Kazantzis,M., Lan,G., Burris,T.P. and
            Solt,L.A.
  TITLE     Distinct roles for REV-ERBalpha and REV-ERBbeta in oxidative
            capacity and mitochondrial biogenesis in skeletal muscle
  JOURNAL   PLoS One 13 (5), e0196787 (2018)
   PUBMED   29723273
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Ohba,Y. and Tei,H.
  TITLE     Phosphorylation of N-terminal regions of REV-ERBs regulates their
            intracellular localization
  JOURNAL   Genes Cells 23 (4), 285-293 (2018)
   PUBMED   29508494
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Yang,F., Inoue,I., Kumagai,M., Takahashi,S., Nakajima,Y. and
            Ikeda,M.
  TITLE     Real-time analysis of the circadian oscillation of the Rev-Erb beta
            promoter
  JOURNAL   J Atheroscler Thromb 20 (3), 267-276 (2013)
   PUBMED   23221024
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Giambiagi,N., Cassia,R., Petropoulos,I., Part,D., Cereghini,S.,
            Zakin,M.M. and Ochoa,A.
  TITLE     Rev-erb beta 2, a novel isoform of the Rev-erb family of orphan
            nuclear receptors
  JOURNAL   Biochem Mol Biol Int 37 (6), 1091-1102 (1995)
   PUBMED   8747539
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Enmark,E., Kainu,T., Pelto-Huikko,M. and Gustafsson,J.A.
  TITLE     Identification of a novel member of the nuclear receptor
            superfamily which is closely related to Rev-ErbA
  JOURNAL   Biochem Biophys Res Commun 204 (1), 49-56 (1994)
   PUBMED   7945391
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Forman,B.M., Chen,J., Blumberg,B., Kliewer,S.A., Henshaw,R.,
            Ong,E.S. and Evans,R.M.
  TITLE     Cross-talk among ROR alpha 1 and the Rev-erb family of orphan
            nuclear receptors
  JOURNAL   Mol Endocrinol 8 (9), 1253-1261 (1994)
   PUBMED   7838158
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Retnakaran,R., Flock,G. and Giguere,V.
  TITLE     Identification of RVR, a novel orphan nuclear receptor that acts as
            a negative transcriptional regulator
  JOURNAL   Mol Endocrinol 8 (9), 1234-1244 (1994)
   PUBMED   7838156
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Pena de Ortiz,S., Cannon,M.M. and Jamieson,G.A. Jr.
  TITLE     Expression of nuclear hormone receptors within the rat hippocampus:
            identification of novel orphan receptors
  JOURNAL   Brain Res Mol Brain Res 23 (3), 278-283 (1994)
   PUBMED   7914660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On or before Feb 11, 2014 this sequence version replaced
            XP_006251772.1, NP_671743.1.
            
            Summary: This gene encodes a member of the nuclear hormone receptor
            family, specifically the NR1 subfamily of receptors. The encoded
            protein functions as a transcriptional repressor and may play a
            role in circadian rhythms and carbohydrate and lipid metabolism.
            [provided by RefSeq, Feb 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.39821.1, X82777.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..578
                     /product="nuclear receptor subfamily 1 group D member 2"
                     /note="orphan receptor; EAR4; rev-erb-beta; orphan nuclear
                     receptor HZF-2; Rev-ErbA-beta; Rev-erb-Beta2"
                     /calculated_mol_wt=64061
     Region          1..99
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Region          1..60
                     /region_name="Required for phosphorylation by CSNK1E and
                     cytoplasmic localization.
                     /evidence=ECO:0000250|UniProtKB:Q60674"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Region          13..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Region          98..186
                     /region_name="NR_DBD_REV_ERB"
                     /note="DNA-binding domain of REV-ERB receptor-like is
                     composed of two C4-type zinc fingers; cd07166"
                     /db_xref="CDD:143540"
     Site            order(103,106,120,123,140,146,156,159)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143540"
     Site            order(112..115,121..122,124,126,128..129,153..154,157,160,
                     171,174..180)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143540"
     Site            162
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT5.
                     /evidence=ECO:0000250|UniProtKB:Q14995; propagated from
                     UniProtKB/Swiss-Prot (Q63504.1)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT5.
                     /evidence=ECO:0000250|UniProtKB:Q14995; propagated from
                     UniProtKB/Swiss-Prot (Q63504.1)"
     Site            order(171..172,176)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143540"
     Region          214..247
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Region          388..576
                     /region_name="NR_LBD_REV_ERB"
                     /note="The ligand binding domain of REV-ERB receptors,
                     members of the nuclear receptor superfamily; cd06940"
                     /db_xref="CDD:132738"
     Region          396..578
                     /region_name="Interaction with ZNHIT1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63504.1)"
     Site            order(401,404,408,412,442,445..446,449,453,481..482,485,
                     567,570..571,574)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132738"
     Site            order(491,514..516,525,528..529,550..551,554..555,
                     558..559,561..562,565..566)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:132738"
     CDS             1..578
                     /gene="Nr1d2"
                     /gene_synonym="HZF-2"
                     /coded_by="NM_147210.2:209..1945"
                     /db_xref="GeneID:259241"
                     /db_xref="RGD:628828"
ORIGIN      
        1 melnaggvia yisssssass paschsegse nsfqsssssv psspnssncd angnpkntdv
       61 ssidgvlksd rtdcpvktgk pgapgmtksh sgmtkfsgmv llckvcgdva sgfhygvhac
      121 egckgffrrs iqqniqykkc lknencsimr mnrnrcqqcr fkkclsvgms rdavrfgrip
      181 krekqrmlie mqsamktmms tqfgghlqsd tlaepheqsv ppaqeqlrpk pqleqeniks
      241 tpppsdfake evigmvtrah kdtflynqeh renssesmpp hrgeriprnv eqynlnhdhr
      301 ggglhshfpc sesqqhlsgq ykgrnmmhyp nghtvcisng hcvnfssayp qrvcdripvg
      361 gcsqtesrns ylcstggrmh lvcpmskspy vdpqksghei weefsmsftp avkevvefak
      421 ripgfrdlsq hdqvnllkag tfevlmvrfa slfdakertv tflsgkkysv ddlhsmgagd
      481 llssmfefse klnglqlsde emslftavvl vsadrsgien vnsvealqet liralrtlim
      541 knhpneasif tklllklpdl rslnnmhsee llafkvhp
//
LOCUS       NP_511175                927 aa            linear   ROD 27-APR-2025
DEFINITION  sodium/calcium exchanger 3 precursor [Rattus norvegicus].
ACCESSION   NP_511175 XP_346775
VERSION     NP_511175.1
DBSOURCE    REFSEQ: accession NM_078620.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Chen,M., Wang,X., Hu,B., Zhou,J., Wang,X., Wei,W. and Zhou,H.
  TITLE     Protective effects of echinacoside against anoxia/reperfusion
            injury in H9c2 cells via up-regulating p-AKT and SLC8A3
  JOURNAL   Biomed Pharmacother 104, 52-59 (2018)
   PUBMED   29763795
  REMARK    GeneRIF: This cardioprotective effect was potentially achieved via
            up-regulating p-AKT and SLC8A3.
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Moriguchi,S., Kita,S., Fukaya,M., Osanai,M., Inagaki,R., Sasaki,Y.,
            Izumi,H., Horie,K., Takeda,J., Saito,T., Sakagami,H., Saido,T.C.,
            Iwamoto,T. and Fukunaga,K.
  TITLE     Reduced expression of Na+/Ca2+ exchangers is associated with
            cognitive deficits seen in Alzheimer's disease model mice
  JOURNAL   Neuropharmacology 131, 291-303 (2018)
   PUBMED   29274751
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Giladi,M., Lee,S.Y., Ariely,Y., Teldan,Y., Granit,R.,
            Strulovich,R., Haitin,Y., Chung,K.Y. and Khananshvili,D.
  TITLE     Structure-based dynamic arrays in regulatory domains of
            sodium-calcium exchanger (NCX) isoforms
  JOURNAL   Sci Rep 7 (1), 993 (2017)
   PUBMED   28428550
  REMARK    GeneRIF: Data show a general mechanism for regulatory coupling
            associated with Ca2+ interactions with regulatory CBD domains of
            NCX1, NCX2, and NCX3 isoforms and their splice variants, where the
            dynamic effects of alternative splicing on conformational dynamics
            of the two-domain regulatory tandem (CBD12) control the
            contribution of a given isoform/splice variant to dynamic handling
            of cytosolic Ca2+ oscillations in many cell type.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 927)
  AUTHORS   Tal,I., Kozlovsky,T., Brisker,D., Giladi,M. and Khananshvili,D.
  TITLE     Kinetic and equilibrium properties of regulatory Ca(2+)-binding
            domains in sodium-calcium exchangers 2 and 3
  JOURNAL   Cell Calcium 59 (4), 181-188 (2016)
   PUBMED   26924806
  REMARK    GeneRIF: analyze the equilibrium and kinetic properties of Ca(2+)
            binding to purified preparations of CBD1, CBD2, and CBD12 from NCX2
            and from NCX3 splice variants
REFERENCE   5  (residues 1 to 927)
  AUTHORS   Sun,D., Xiao,J.H., Bai,Y., Chen,M.S., Hu,J.S., Wu,G.F., Mao,B.,
            Wu,S.H. and Hu,Y.
  TITLE     Na (+) /Ca (2+) Exchanger 3 is Downregulated in the Hippocampus and
            Cerebrocortex of Rats with Hyperthermia-induced Convulsion
  JOURNAL   Chin Med J (Engl) 128 (22), 3083-3087 (2015)
   PUBMED   26608990
  REMARK    GeneRIF: There is a significant reduction in NCX3 expression in
            rats with febrile convulsions.
REFERENCE   6  (residues 1 to 927)
  AUTHORS   Lu,J., Tong,X.Y. and Wang,X.L.
  TITLE     Altered gene expression of Na+/Ca2+ exchanger isoforms NCX1, NCX2
            and NCX3 in chronic ischemic rat brain
  JOURNAL   Neurosci Lett 332 (1), 21-24 (2002)
   PUBMED   12377375
  REMARK    GeneRIF: Brain ischemia regulates gene expression levels of
            Na+/Ca2+ exchanger isoform NCX3, especially in cerebral cortex.
REFERENCE   7  (residues 1 to 927)
  AUTHORS   Fraysse,B., Rouaud,T., Millour,M., Fontaine-Perus,J.,
            Gardahaut,M.F. and Levitsky,D.O.
  TITLE     Expression of the Na(+)/Ca(2+) exchanger in skeletal muscle
  JOURNAL   Am J Physiol Cell Physiol 280 (1), C146-C154 (2001)
   PUBMED   11121386
REFERENCE   8  (residues 1 to 927)
  AUTHORS   Sakaue,M., Nakamura,H., Kaneko,I., Kawasaki,Y., Arakawa,N.,
            Hashimoto,H., Koyama,Y., Baba,A. and Matsuda,T.
  TITLE     Na(+)-Ca(2+) exchanger isoforms in rat neuronal preparations:
            different changes in their expression during postnatal development
  JOURNAL   Brain Res 881 (2), 212-216 (2000)
   PUBMED   11036162
REFERENCE   9  (residues 1 to 927)
  AUTHORS   Linck,B., Qiu,Z., He,Z., Tong,Q., Hilgemann,D.W. and Philipson,K.D.
  TITLE     Functional comparison of the three isoforms of the Na+/Ca2+
            exchanger (NCX1, NCX2, NCX3)
  JOURNAL   Am J Physiol 274 (2), C415-C423 (1998)
   PUBMED   9486131
REFERENCE   10 (residues 1 to 927)
  AUTHORS   Nicoll,D.A., Quednau,B.D., Qui,Z., Xia,Y.R., Lusis,A.J. and
            Philipson,K.D.
  TITLE     Cloning of a third mammalian Na+-Ca2+ exchanger, NCX3
  JOURNAL   J Biol Chem 271 (40), 24914-24921 (1996)
   PUBMED   8798769
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346775.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..927
                     /product="sodium/calcium exchanger 3 precursor"
                     /note="sodium/calcium exchanger 3; Na(+)/Ca(2+)-exchange
                     protein 3; solute carrier family 8 (sodium/calcium
                     exchanger), member 3"
                     /calculated_mol_wt=99748
     Region          1..927
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70549.1)"
                     /calculated_mol_wt=3433
     mat_peptide     31..927
                     /product="Sodium/calcium exchanger 3. /id=PRO_0000019385"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
                     /calculated_mol_wt=99748
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70549.1)"
     Site            74..94
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Region          140..180
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            203..223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            231..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Region          253..272
                     /region_name="Putative calmodulin-binding region.
                     /evidence=ECO:0000250|UniProtKB:P23685"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            727..747
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            755..775
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            779..799
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Region          796..832
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            823
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70549.1)"
     Site            829..849
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            861..881
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     Site            904..924
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70549.1)"
     CDS             1..927
                     /gene="Slc8a3"
                     /gene_synonym="Ncx3"
                     /coded_by="NM_078620.2:379..3162"
                     /db_xref="GeneID:140448"
                     /db_xref="RGD:620197"
ORIGIN      
        1 mawlrlqplt saflhfglvt fvlflnglra eagdlrdvps agqnnescsg ssdckegvil
       61 piwypenpsl gdkiarvivy fvaliymflg vsiiadrfma sievitsqer evtikkpnge
      121 tstttirvwn etvsnltlma lgssapeill slievcghgf iagdlgpsti vgsaafnmfi
      181 iigicvyvip dgetrkikhl rvffvtaaws vfayiwlymi lavfspgvvq vweglltlff
      241 fpvcvllawv adkrllfyky mhkryrtdkh rgiiietege hpkgiemdgk mmnshfldgn
      301 liplegkevd esrremiril kdlkqkhpek dldqlveman yyalshqqks rafyriqatr
      361 mmtgagnilk khaaeqakkt asmsevhtde pedfaskvff dpcsyqclen cgavlltvvr
      421 kggdisktmy vdyktedgsa nagadyefte gtvvlkpget qkefsvgiid ddifeedehf
      481 fvrlsnvrve eeqleegmtp ailnslplpr avlaspcvat vtildddhag iftfecdtih
      541 vsesigvmev kvlrtsgarg tvivpfrtve gtakgggedf edtygelefk ndetvktirv
      601 kivdeeeyer qenffialge pkwmergisa lllspevtdr kltmeeeeak riaemgkpvl
      661 gehpklevii eesyefkstv dklikktnla lvvgthswrd qfmeaitvsa agdeeedesg
      721 eerlpscfdy vmhfltvfwk vlfacvppte ychgwacfvv siliigmlta iigdlashfg
      781 ctiglkdsvt avvfvafgts vpdtfaskaa alqdvyadas ignvtgsnav nvflgiglaw
      841 svaaiywamq gqefhvsagt lafsvtlfti fafvclsvll yrrrphlgge lggprgckla
      901 ttwlfvslwl lyvlfatlea ycyikgf
//
LOCUS       NP_001165273              86 aa            linear   ROD 27-APR-2025
DEFINITION  triple QxxK/R motif-containing protein [Rattus norvegicus].
ACCESSION   NP_001165273
VERSION     NP_001165273.1
DBSOURCE    REFSEQ: accession NM_001171802.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB805415.1, BC089993.1 and CA507504.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089993.1, CO399939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132283, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..86
                     /product="triple QxxK/R motif-containing protein"
                     /note="protein TRIQK; triple repetitive-sequence of QXXK/R
                     protein homolog"
                     /calculated_mol_wt=9546
     Region          1..>52
                     /region_name="TRIQK"
                     /note="Triple QxxK/R motif-containing protein family;
                     pfam15168"
                     /db_xref="CDD:464542"
     Site            51..71
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5EB66.1)"
     CDS             1..86
                     /gene="Triqk"
                     /coded_by="NM_001171802.1:295..555"
                     /db_xref="GeneID:500413"
                     /db_xref="RGD:1561260"
ORIGIN      
        1 mgrkdssttk lpvdqyrkqi gkqdykktkp ilratklkae akktaigike vglmlaaila
       61 lllafyaffy lrlstnidad ldpded
//
LOCUS       NP_001014283             459 aa            linear   ROD 27-APR-2025
DEFINITION  antizyme inhibitor 2 [Rattus norvegicus].
ACCESSION   NP_001014283 XP_345584
VERSION     NP_001014283.2
DBSOURCE    REFSEQ: accession NM_001014261.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Lambertos,A., Ramos-Molina,B., Lopez-Contreras,A.J., Cremades,A.
            and Penafiel,R.
  TITLE     New insights of polyamine metabolism in testicular physiology: A
            role of ornithine decarboxylase antizyme inhibitor 2 (AZIN2) in the
            modulation of testosterone levels and sperm motility
  JOURNAL   PLoS One 13 (12), e0209202 (2018)
   PUBMED   30566531
  REMARK    GeneRIF: Study found a close ontogenic similarity in the mRNA
            levels of antizymes and antizyme inhibitors (AZiIN2) between mice
            and rats, but an opposite expression pattern of ornithine
            decarboxylase activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Li,X., He,X., Wang,H., Li,M., Huang,S., Chen,G., Jing,Y., Wang,S.,
            Chen,Y., Liao,W., Liao,Y. and Bin,J.
  TITLE     Loss of AZIN2 splice variant facilitates endogenous cardiac
            regeneration
  JOURNAL   Cardiovasc Res 114 (12), 1642-1655 (2018)
   PUBMED   29584819
  REMARK    GeneRIF: AZIN2 splice variant suppressed endogenous cardiac
            regeneration by targeting the PTEN/Akt pathway.
            Erratum:[Cardiovasc Res. 2018 Oct 1;114(12):1628. doi:
            10.1093/cvr/cvy194. PMID: 30137261]
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Wang,S., Lv,Q., Yang,Y., Guo,L.H., Wan,B., Ren,X. and Zhang,H.
  TITLE     Arginine decarboxylase: A novel biological target of mercury
            compounds identified in PC12 cells
  JOURNAL   Biochem Pharmacol 118, 109-120 (2016)
   PUBMED   27565891
  REMARK    GeneRIF: Data suggest that inhibition of Adc (arginine
            decarboxylase) in agmatinergic neurons (here, pheochromocytoma/PC12
            cell line) is target of mercury compounds (here, MeHg, EtHg, PhHg,
            and HgCl2); upon cell exposure, mercury compounds enter the cell,
            inhibit Adc decarboxylation of arginine, and thereby decrease the
            level of agmatine, an endogenous neuroprotective/neurorescue agent.
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Ramos-Molina,B., Lambertos,A., Lopez-Contreras,A.J., Kasprzak,J.M.,
            Czerwoniec,A., Bujnicki,J.M., Cremades,A. and Penafiel,R.
  TITLE     Structural and degradative aspects of ornithine decarboxylase
            antizyme inhibitor 2
  JOURNAL   FEBS Open Bio 4, 510-521 (2014)
   PUBMED   24967154
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Kanerva,K., Makitie,L.T., Back,N. and Andersson,L.C.
  TITLE     Ornithine decarboxylase antizyme inhibitor 2 regulates
            intracellular vesicle trafficking
  JOURNAL   Exp Cell Res 316 (11), 1896-1906 (2010)
   PUBMED   20188728
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Lopez-Contreras,A.J., Sanchez-Laorden,B.L., Ramos-Molina,B., de la
            Morena,M.E., Cremades,A. and Penafiel,R.
  TITLE     Subcellular localization of antizyme inhibitor 2 in mammalian
            cells: Influence of intrinsic sequences and interaction with
            antizymes
  JOURNAL   J Cell Biochem 107 (4), 732-740 (2009)
   PUBMED   19449338
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Lopez-Contreras,A.J., Ramos-Molina,B., Cremades,A. and Penafiel,R.
  TITLE     Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in
            mammalian cells
  JOURNAL   J Biol Chem 283 (30), 20761-20769 (2008)
   PUBMED   18508777
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Kanerva,K., Makitie,L.T., Pelander,A., Heiskala,M. and
            Andersson,L.C.
  TITLE     Human ornithine decarboxylase paralogue (ODCp) is an antizyme
            inhibitor but not an arginine decarboxylase
  JOURNAL   Biochem J 409 (1), 187-192 (2008)
   PUBMED   17900240
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Lopez-Contreras,A.J., Lopez-Garcia,C., Jimenez-Cervantes,C.,
            Cremades,A. and Penafiel,R.
  TITLE     Mouse ornithine decarboxylase-like gene encodes an antizyme
            inhibitor devoid of ornithine and arginine decarboxylating activity
  JOURNAL   J Biol Chem 281 (41), 30896-30906 (2006)
   PUBMED   16916800
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Iyo,A.H., Zhu,M.Y., Ordway,G.A. and Regunathan,S.
  TITLE     Expression of arginine decarboxylase in brain regions and neuronal
            cells
  JOURNAL   J Neurochem 96 (4), 1042-1050 (2006)
   PUBMED   16445852
  REMARK    GeneRIF: Arginine decarboxylase is expressed in rat brain regions,
            is regulated in neuronal cells, and down-regulation of its activity
            by specific siRNA leads to lower agmatine production.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CK470797.1, HQ413774.1 and
            BC078981.1.
            
            On Jun 11, 2014 this sequence version replaced NP_001014283.1.
            
            Summary: The protein encoded by this gene belongs to the antizyme
            inhibitor family, which plays a role in cell growth and
            proliferation by maintaining polyamine homeostasis within the cell.
            Antizyme inhibitors are homologs of ornithine decarboxylase (ODC,
            the key enzyme in polyamine biosynthesis) that have lost the
            ability to decarboxylase ornithine; however, retain the ability to
            bind to antizymes. Antizymes negatively regulate intracellular
            polyamine levels by binding to ODC and targeting it for
            degradation, as well as by inhibiting polyamine uptake. Antizyme
            inhibitors function as positive regulators of polyamine levels by
            sequestering antizymes and neutralizing their effect. This gene
            encodes antizyme inhibitor 2, the second member of this gene
            family. Like antizyme inhibitor 1, antizyme inhibitor 2 interacts
            with all 3 antizymes and stimulates ODC activity and polyamine
            uptake. However, unlike antizyme inhibitor 1, which is ubiquitously
            expressed and localized in the nucleus and cytoplasm, antizyme
            inhibitor 2 is predominantly expressed in the brain and testis and
            localized in the endoplasmic reticulum-golgi intermediate
            compartment. Recent studies indicate that antizyme inhibitor 2 is
            also expressed in specific cell types in ovaries, adrenal glands
            and pancreas, and in mast cells. The exact function of this gene is
            not known, however, available data suggest its role in cell growth,
            spermiogenesis, vesicular trafficking and secretion. There has been
            confusion in literature and databases over the nomenclature of this
            gene, stemming from an earlier report that a human cDNA clone
            (identical to ODCp/AZIN2) had arginine decarboxylase (ADC) activity
            (PMID:14738999). Subsequent studies in human and mouse showed that
            antizyme inhibitor 2 was devoid of arginine decarboxylase activity
            (PMID:19956990). [provided by RefSeq, Sep 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: HQ413774.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..459
                     /product="antizyme inhibitor 2"
                     /note="arginine decarboxylase; ODC-like protein; ornithine
                     decarboxylase paralog; ornithine decarboxylase-like
                     protein"
                     /calculated_mol_wt=49289
     Region          40..407
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(68,70,89,155,198,201,237..238,275..278,332,360,389)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(68,70,89,155,198,201,237..238,275..278,360,389)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(70,91..92,94..95,117,122,135,138,142,169..171,292,
                     294..295,315,317,319,322..323,331,333,357,359,361,364,393,
                     395,397..399,401)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(70,360)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            order(331..332,360..361,389,397)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
     CDS             1..459
                     /gene="Azin2"
                     /gene_synonym="Adc; AzI2; ODC-p; RGD1564776"
                     /coded_by="NM_001014261.3:340..1719"
                     /db_xref="GeneID:366473"
                     /db_xref="RGD:1564776"
ORIGIN      
        1 magylsesdf vmveegfstr dlleeltlga sqattgkvaa ffvadlgavv rkhfcflkyl
       61 prvrpfyavr cnsslgvlkv laelglgfsc askaemelvq higvpaskii canpckqvaq
      121 ikyaakhgvr llsfdnevel akvvkshpsa kmvlciatqd shslnhlslr fgaslkscrh
      181 llenakqshv evvgvsfhig sgcpdpqaya qsiadarlvf qmgaelghtm nildlgggfp
      241 glegakvrfe emasvinsal dlyfpegcgv dilaelgryy vtsaftvavs ivakkevldq
      301 psreeqtgaa pksivyhlde gvygvfnsvl fdntcptpal qkkpsadqpl yssslwgpav
      361 dgcdcvaegl wlpqlqvgdw lvfdnmgayt vdtksllggt qacrvtyams rlawealqgq
      421 llpaeedqda egvckplscg weitdslcvg pvftpasim
//
LOCUS       NP_001257496             465 aa            linear   ROD 27-APR-2025
DEFINITION  histamine H3 receptor isoform H3E [Rattus norvegicus].
ACCESSION   NP_001257496
VERSION     NP_001257496.1
DBSOURCE    REFSEQ: accession NM_001270567.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Vazquez-Vazquez,H., Gonzalez-Sandoval,C., Vega,A.V.,
            Arias-Montano,J.A. and Barral,J.
  TITLE     Histamine H3 Receptor Activation Modulates Glutamate Release in the
            Corticostriatal Synapse by Acting at CaV2.1 (P/Q-Type) Calcium
            Channels and GIRK (KIR3) Potassium Channels
  JOURNAL   Cell Mol Neurobiol 42 (3), 817-828 (2022)
   PUBMED   33068216
  REMARK    GeneRIF: Histamine H3 Receptor Activation Modulates Glutamate
            Release in the Corticostriatal Synapse by Acting at CaV2.1
            (P/Q-Type) Calcium Channels and GIRK (KIR3) Potassium Channels.
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Coslovich,T., Della Mora,A., D'Angelo,G., Ortolani,F. and
            Taccola,G.
  TITLE     Histamine H3 Receptors Expressed in Ventral Horns Modulate Spinal
            Motor Output
  JOURNAL   Cell Mol Neurobiol 41 (1), 185-190 (2021)
   PUBMED   32211996
  REMARK    GeneRIF: Histamine H3 Receptors Expressed in Ventral Horns Modulate
            Spinal Motor Output.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yu,C., Li,L., Xia,Q. and Tang,Y.
  TITLE     Expression and localization of histamine H1, H2, and H3 receptors
            in rat olfactory epithelium
  JOURNAL   Int J Pediatr Otorhinolaryngol 101, 102-106 (2017)
   PUBMED   28964277
  REMARK    GeneRIF: indicate that histamine H1, H2, and H3 receptors are
            present in rat olfactory epithelium and may play a physiological
            role in olfactory transmission.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Gbahou,F., Rouleau,A. and Arrang,J.M.
  TITLE     The histamine autoreceptor is a short isoform of the H receptor
  JOURNAL   Br J Pharmacol 166 (6), 1860-1871 (2012)
   PUBMED   22356432
  REMARK    GeneRIF: Finsings show that short, but not long, isoforms fulfill
            the function of autoreceptor and thereby confirm the hypothesis
            that H3 receptor isoforms have distinct functional roles in the
            brain
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Bakker,R.A., Lozada,A.F., van Marle,A., Shenton,F.C., Drutel,G.,
            Karlstedt,K., Hoffmann,M., Lintunen,M., Yamamoto,Y., van Rijn,R.M.,
            Chazot,P.L., Panula,P. and Leurs,R.
  TITLE     Discovery of naturally occurring splice variants of the rat
            histamine H3 receptor that act as dominant-negative isoforms
  JOURNAL   Mol Pharmacol 69 (4), 1194-1206 (2006)
   PUBMED   16415177
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Morisset,S., Sasse,A., Gbahou,F., Heron,A., Ligneau,X.,
            Tardivel-Lacombe,J., Schwartz,J.C. and Arrang,J.M.
  TITLE     The rat H3 receptor: gene organization and multiple isoforms
  JOURNAL   Biochem Biophys Res Commun 280 (1), 75-80 (2001)
   PUBMED   11162480
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Drutel,G., Peitsaro,N., Karlstedt,K., Wieland,K., Smit,M.J.,
            Timmerman,H., Panula,P. and Leurs,R.
  TITLE     Identification of rat H3 receptor isoforms with different brain
            expression and signaling properties
  JOURNAL   Mol Pharmacol 59 (1), 1-8 (2001)
   PUBMED   11125017
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Lovenberg,T.W., Roland,B.L., Wilson,S.J., Jiang,X., Pyati,J.,
            Huvar,A., Jackson,M.R. and Erlander,M.G.
  TITLE     Cloning and functional expression of the human histamine H3
            receptor
  JOURNAL   Mol Pharmacol 55 (6), 1101-1107 (1999)
   PUBMED   10347254
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Godlewski,G., Malinowska,B., Buczko,W. and Schlicker,E.
  TITLE     Inhibitory H3 receptors on sympathetic nerves of the pithed rat:
            activation by endogenous histamine and operation in spontaneously
            hypertensive rats
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 355 (2), 261-266 (1997)
   PUBMED   9050021
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Fujimoto,K., Mizuguchi,H., Fukui,H. and Wada,H.
  TITLE     Presynaptic localization of histamine H3-receptors in rat brain
  JOURNAL   Biochem Biophys Res Commun 177 (3), 907-912 (1991)
   PUBMED   1647769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB015646.1, DQ112343.1 and
            BC087707.1.
            
            Summary: This gene encodes a histamine H3 receptor that belongs to
            the superfamily of G-protein coupled receptors. This protein
            functions as a presynaptic autoreceptor on histamine neurons in the
            brain, and a presynaptic heteroreceptor in nonhistamine-containing
            neurons in both the central and peripheral nervous systems. It is
            deemed a great target for the development of therapeutics for
            numerous disorders, including obesity, epilepsy, and such cognitive
            diseases as attention deficit hyperactivity disorder and
            Alzheimer's disease. Several alternatively spliced transcript
            variants encoding different isoforms, with different brain
            expression patterns and signaling properties, have been described
            for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (5) is alternatively spliced at
            the 3' end compared to variant 1, which results in a frame-shift,
            and a longer isoform (H3E) containing 6 transmembrane domains and a
            distinct C-terminus compared to isoform H3A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ112343.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132300, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..465
                     /product="histamine H3 receptor isoform H3E"
                     /note="histamine H3 receptor; HH3R; H3R"
                     /calculated_mol_wt=51392
     Region          48..363
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          70..92
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          108..130
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          154..170
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          196..219
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          325..347
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..465
                     /gene="Hrh3"
                     /coded_by="NM_001270567.1:338..1735"
                     /note="isoform H3E is encoded by transcript variant 5"
                     /db_xref="GeneID:85268"
                     /db_xref="RGD:620630"
ORIGIN      
        1 merappdglm nasgtlagea aaaggargfs aawtavlaal mallivatvl gnalvmlafv
       61 adsslrtqnn ffllnlaisd flvgafcipl yvpyvltgrw tfgrglcklw lvvdyllcas
      121 svfnivlisy drflsvtrav syraqqgdtr ravrkmalvw vlafllygpa ilsweylsgg
      181 ssipeghcya effynwyfli tastlefftp flsvtffnls iylniqrrtr lrldggreag
      241 pepppdaqps pppappscwg cwpkghgeam plhssgsssr gterprslkr gskpsassas
      301 lekrmkmvsq sitqrfrlsr dkkvakslai ivsifglcwa pytllmiira achgrcipdy
      361 cverlgklea slllplwmfs grwrrrkhvc eldvpwmfnq erqncrgarg wigrcglprp
      421 ppsvlqlpae prqlllpapp pglgrwpcpa cpvctiriwg wvvmg
//
LOCUS       NP_001257801             985 aa            linear   ROD 27-APR-2025
DEFINITION  adhesion G-protein coupled receptor G2 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001257801
VERSION     NP_001257801.1
DBSOURCE    REFSEQ: accession NM_001270872.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Obermann,H., Samalecos,A., Osterhoff,C., Schroder,B., Heller,R. and
            Kirchhoff,C.
  TITLE     HE6, a two-subunit heptahelical receptor associated with apical
            membranes of efferent and epididymal duct epithelia
  JOURNAL   Mol Reprod Dev 64 (1), 13-26 (2003)
   PUBMED   12420295
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF538959.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq14"
     Protein         1..985
                     /product="adhesion G-protein coupled receptor G2 isoform
                     3"
                     /note="G-protein coupled receptor 64; re6 receptor;
                     epididymis-specific protein 6"
                     /calculated_mol_wt=107810
     Region          536..580
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          593..862
                     /region_name="7tmB2_GPR64"
                     /note="orphan adhesion receptor GPR64 and related
                     proteins, member of subfamily B2 of the class B
                     secretin-like receptors of seven-transmembrane G
                     protein-coupled receptors; cd15444"
                     /db_xref="CDD:320560"
     Region          595..620
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320560"
     Site            order(600,604,647,650..651,654,663,670,754..755,757,759,
                     814,817,829,833)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320560"
     Region          630..652
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320560"
     Region          663..690
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320560"
     Region          705..721
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320560"
     Region          751..774
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320560"
     Region          797..822
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320560"
     Region          826..851
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320560"
     CDS             1..985
                     /gene="Adgrg2"
                     /gene_synonym="Gpr64; He6; Re6"
                     /coded_by="NM_001270872.1:50..3007"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:266735"
                     /db_xref="RGD:628618"
ORIGIN      
        1 mlfsggqysp vgrpeevlli ykiflviicf hailvtslkd aasevlstln rtekskitil
       61 ktfnasgvks qrnicnlssi csdsvffrge ivfqhddhyn vtqnqdivns tfagvlslse
      121 lkrtelnktl qtlsetyfiv cataeaqntl nctftvklne tmnvcammvt fksvqirpme
      181 qcccsprtpc psspeelekl qcdlqdpivc ladqphgppv sssskpvpvv pqatifshva
      241 sdfslaepld halmtsstps laqetrlpsp qptisltssp aidlpvqhvv assslpqtdl
      301 shtlspvqss ipspttaaps vpekvvaist ppgetvvnts svpdleaqvs qmekalslgs
      361 lepnlagemv nrvskllhsp lallaplaqr llkvvdaigl qlnfssttis ltspslalav
      421 irvnasnfnt ttfaaqdpan lqvsleaqap knsigaitlp sslmsnlpas evelasrvqf
      481 nffetpalfq dpslenlsli syvisssvtn mtiknltrnv tvalkhinps qddltvkcvf
      541 wdlnrnggrg gwssdgcsvk ekrmnetict cshltsfgil ldlsrtslpp sqmmaltfit
      601 yigcglssif lsvtlvtyia fekirrdyps kiliqlcaal lllnlvflld swialynarg
      661 fcisvavflh yfllvsftwm gleafhmyla lvkvfntyir kyilkfcivg wgipavvvsi
      721 vltispdnyg igsygkfpng tpddfcwins svvfyitvvg yfcvifllnv smfivvlvql
      781 crikkkkqlg aqrktsiqdl rsiagltfll gitwgfaffa wgpvnltfmy lfaifntlqg
      841 ffififycaa kenvrkqwrr ylccgklrla ensdwsktat nglkkqtvnq gvssssnslq
      901 sscnstnstt llvnsdcsvh asgngnaste rngvsfsvqn gdvclhdltg kqhmfsdked
      961 scngksrmal rrtskrgslh fieqm
//
LOCUS       NP_071625                344 aa            linear   ROD 27-APR-2025
DEFINITION  sorting nexin-16 [Rattus norvegicus].
ACCESSION   NP_071625
VERSION     NP_071625.2
DBSOURCE    REFSEQ: accession NM_022289.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Choi,J.H., Hong,W.P., Kim,M.J., Kim,J.H., Ryu,S.H. and Suh,P.G.
  TITLE     Sorting nexin 16 regulates EGF receptor trafficking by
            phosphatidylinositol-3-phosphate interaction with the Phox domain
  JOURNAL   J Cell Sci 117 (Pt 18), 4209-4218 (2004)
   PUBMED   15292396
  REMARK    GeneRIF: SNX16 directs the sorting of EGFR to the endosomal
            compartment and thus regulates EGF-induced cell signaling.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Hanson,B.J. and Hong,W.
  TITLE     Evidence for a role of SNX16 in regulating traffic between the
            early and later endosomal compartments
  JOURNAL   J Biol Chem 278 (36), 34617-34630 (2003)
   PUBMED   12813048
  REMARK    GeneRIF: SNX16 is a sorting nexin that may function in the
            trafficking of proteins between the early and late endosomal
            compartments
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061554.1.
            
            On Dec 20, 2003 this sequence version replaced NP_071625.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061554.1, AF305780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132269
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q23"
     Protein         1..344
                     /product="sorting nexin-16"
                     /calculated_mol_wt=38718
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57769.2)"
     Region          83..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57769.2)"
     Region          105..214
                     /region_name="PX_SNX16"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 16; cd07276"
                     /db_xref="CDD:132809"
     Site            order(144..146,169..170,184)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132809"
     Region          <222..>278
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C080; propagated from
                     UniProtKB/Swiss-Prot (P57769.2)"
     CDS             1..344
                     /gene="Snx16"
                     /coded_by="NM_022289.3:289..1323"
                     /db_xref="GeneID:64088"
                     /db_xref="RGD:620295"
ORIGIN      
        1 matpyvpvpm pignsassft nnrnqrsssf gsvstssnss kgqledssvg tckhtnvqdq
       61 mdsassvcgs plirtkftgt dssieysarp rdteeqhpda lnwedrpstp tilgyevmee
      121 rakftvykil vkespeeswv vfrrytdfsr lndklkemfp gfrlalppkr wfkdnynadf
      181 ledrqlglqa flqnlvahkd ianclavref lclddppgpf dsleesrafc etleetnyhl
      241 qrellekqke veslkkllge kqlhidalet rirtlslepg aslyvsraeg gqilrvqssv
      301 lqvnrdvlde esradhkphf nsreagsaia dievaqlayn aedd
//
LOCUS       NP_955417                509 aa            linear   ROD 27-APR-2025
DEFINITION  dihydrolipoyl dehydrogenase, mitochondrial precursor [Rattus
            norvegicus].
ACCESSION   NP_955417 XP_216682
VERSION     NP_955417.1
DBSOURCE    REFSEQ: accession NM_199385.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Wang,Y., Guo,Y.R., Liu,K., Yin,Z., Liu,R., Xia,Y., Tan,L., Yang,P.,
            Lee,J.H., Li,X.J., Hawke,D., Zheng,Y., Qian,X., Lyu,J., He,J.,
            Xing,D., Tao,Y.J. and Lu,Z.
  TITLE     KAT2A coupled with the alpha-KGDH complex acts as a histone H3
            succinyltransferase
  JOURNAL   Nature 552 (7684), 273-277 (2017)
   PUBMED   29211711
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Wu,J., Jin,Z. and Yan,L.J.
  TITLE     Redox imbalance and mitochondrial abnormalities in the diabetic
            lung
  JOURNAL   Redox Biol 11, 51-59 (2017)
   PUBMED   27888691
  REMARK    GeneRIF: These results, together with the findings that the protein
            contents of DLDH, sirt3, and NQO1 all are decreased in the diabetic
            lung, demonstrate that redox imbalance, mitochondrial abnormality,
            and oxidative stress contribute to lung injury in diabetes.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Ji,X., Li,Z., Chen,H., Li,J., Tian,H., Li,Z., Gao,X., Xiang,Q.,
            Su,Z., Huang,Y. and Zhang,Q.
  TITLE     Cytotoxic mechanism related to dihydrolipoamide dehydrogenase in
            Leydig cells exposed to heavy metals
  JOURNAL   Toxicology 334, 22-32 (2015)
   PUBMED   25981801
  REMARK    GeneRIF: DLD is down-regulation and related to steroid biosynthesis
            in Leyig cells exposed to heavy metals; cAMP/PKA act as downstream
            effector molecules of DLD, which activate phosphorylation of ERK1/2
            to initiate the steroidogenesis.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Tibbetts,A.S. and Appling,D.R.
  TITLE     Compartmentalization of Mammalian folate-mediated one-carbon
            metabolism
  JOURNAL   Annu Rev Nutr 30, 57-81 (2010)
   PUBMED   20645850
  REMARK    Review article
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Harris,R.A., Bowker-Kinley,M.M., Wu,P., Jeng,J. and Popov,K.M.
  TITLE     Dihydrolipoamide dehydrogenase-binding protein of the human
            pyruvate dehydrogenase complex. DNA-derived amino acid sequence,
            expression, and reconstitution of the pyruvate dehydrogenase
            complex
  JOURNAL   J Biol Chem 272 (32), 19746-19751 (1997)
   PUBMED   9242632
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Haramaki,N., Han,D., Handelman,G.J., Tritschler,H.J. and Packer,L.
  TITLE     Cytosolic and mitochondrial systems for NADH- and NADPH-dependent
            reduction of alpha-lipoic acid
  JOURNAL   Free Radic Biol Med 22 (3), 535-542 (1997)
   PUBMED   8981046
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Maury,J., Kerbey,A.L., Priestman,D.A., Patel,M.S., Girard,J. and
            Ferre,P.
  TITLE     Pretranslational regulation of pyruvate dehydrogenase complex
            subunits in white adipose tissue during the suckling-weaning
            transition in the rat
  JOURNAL   Biochem J 311 (Pt 2) (Pt 2), 531-535 (1995)
   PUBMED   7487891
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Kunz,W.S.
  TITLE     Spectral properties of fluorescent flavoproteins of isolated rat
            liver mitochondria
  JOURNAL   FEBS Lett 195 (1-2), 92-96 (1986)
   PUBMED   3753688
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM100976.1, FM093110.1, FM046215.1, FM087994.1, FM044626.1 and
            FM139628.1.
            
            On Jan 12, 2004 this sequence version replaced XP_216682.1.
            
            Summary: This gene encodes a member of the class-I pyridine
            nucleotide-disulfide oxidoreductase family. A similar protein in
            human, mouse, and pig has been identified as a moonlighting protein
            based on its ability to perform mechanistically distinct functions.
            In homodimeric form, the protein functions as a dehydrogenase and
            is found in several multi-enzyme complexes that regulate energy
            metabolism. However, as a monomer, the protein can function as a
            protease. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215299.1, BC062069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            multifunctional gene product(s)    :: inferred from conservation
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..509
                     /product="dihydrolipoyl dehydrogenase, mitochondrial
                     precursor"
                     /EC_number="1.8.1.4"
                     /note="dihydrolipoyl dehydrogenase, mitochondrial;
                     dihydrolipoamide dehydrogenase (E3 component of pyruvate
                     dehydrogenase complex, 2-oxo-glutarate complex, branched
                     chain keto acid dehydrogenase complex)"
                     /calculated_mol_wt=50090
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q6P6R2.1)"
                     /calculated_mol_wt=3967
     mat_peptide     36..509
                     /product="Dihydrolipoyl dehydrogenase, mitochondrial.
                     /id=PRO_0000260228"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P6R2.1)"
                     /calculated_mol_wt=50090
     Region          40..501
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            122
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            132
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            143
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            346
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            410
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            420
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            448
                     /site_type="other"
                     /note="Important for interaction with PDHX and activity of
                     pyruvate dehydrogenase complex.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            473
                     /site_type="other"
                     /note="Important for interaction with PDHX and activity of
                     pyruvate dehydrogenase complex.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09622; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     Site            505
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O08749; propagated from
                     UniProtKB/Swiss-Prot (Q6P6R2.1)"
     CDS             1..509
                     /gene="Dld"
                     /coded_by="NM_199385.2:84..1613"
                     /db_xref="GeneID:298942"
                     /db_xref="RGD:735073"
ORIGIN      
        1 mqswsrvycs lakkghfnrl shglqgassv plrtysdqpi dadvtvigsg pggyvaaika
       61 aqlgfktvci eknetlggtc lnvgcipska llnnshyyhl ahgkdfasrg ieipevrlnl
      121 ekmmeqkrsa vkaltggiah lfkqnkvvhv ngfgkitgkn qvtattadgs tqvigtknil
      181 iatgsevtpf pgitidedti vsstgalslk kvpeklvvig agvigvelgs vwqrlgadvt
      241 aveflghvgg igidmeiskn fqrilqkqgf kfklntkvtg atkksdgkid vsveaasggk
      301 aevitcdvll vcigrrpftq nlgleelgie ldpkgripvn trfqtkipni faigdvvagp
      361 mlahkaedeg iicvegmagg avhidyncvp sviythpeva wvgkseeqlk eegvefkvgk
      421 fpfaansrak tnadtdgmvk ilghkstdri lgahilgpga gemvneaala leygascedv
      481 arvchahptl seafreanla asfgkpinf
//
LOCUS       NP_001257611             312 aa            linear   ROD 27-APR-2025
DEFINITION  apolipoprotein E precursor [Rattus norvegicus].
ACCESSION   NP_001257611
VERSION     NP_001257611.1
DBSOURCE    REFSEQ: accession NM_001270682.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Lee,B.H., Cevizci,M., Lieblich,S.E., Ibrahim,M., Wen,Y., Eid,R.S.,
            Lamers,Y., Duarte-Guterman,P. and Galea,L.A.M.
  TITLE     Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age
  JOURNAL   Brain Behav Immun 120, 54-70 (2024)
   PUBMED   38772427
  REMARK    GeneRIF: Exploring the parity paradox: Differential effects on
            neuroplasticity and inflammation by APOEe4 genotype at middle age.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Chen,H., Zhao,S., Jian,Q., Yan,Y., Wang,S., Zhang,X. and Ji,Y.
  TITLE     The role of ApoE in fatty acid transport from neurons to astrocytes
            under ischemia/hypoxia conditions
  JOURNAL   Mol Biol Rep 51 (1), 320 (2024)
   PUBMED   38393618
  REMARK    GeneRIF: The role of ApoE in fatty acid transport from neurons to
            astrocytes under ischemia/hypoxia conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Matsuo,H., Kawakami,K., Ohara,H., Kaneko,T., Mashimo,T., Yamada,T.
            and Nabika,T.
  TITLE     Apolipoprotein E-depletion accelerates arterial fat deposition in
            the spontaneously hypertensive rat
  JOURNAL   Exp Anim 72 (4), 439-445 (2023)
   PUBMED   37081644
  REMARK    GeneRIF: Apolipoprotein E-depletion accelerates arterial fat
            deposition in the spontaneously hypertensive rat.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Jiang,C., Chen,Z., Wang,X., Zhang,Y., Guo,X., Fan,H., Huang,D.,
            He,Y., Tang,X., Ai,Y., Liu,Y., Yang,H. and Hao,D.
  TITLE     Curcumin-activated Olfactory Ensheathing Cells Improve Functional
            Recovery After Spinal Cord Injury by Modulating Microglia
            Polarization Through APOE/TREM2/NF-kappaB Signaling Pathway
  JOURNAL   J Neuroimmune Pharmacol 18 (3), 476-494 (2023)
   PUBMED   37658943
  REMARK    GeneRIF: Curcumin-activated Olfactory Ensheathing Cells Improve
            Functional Recovery After Spinal Cord Injury by Modulating
            Microglia Polarization Through APOE/TREM2/NF-kappaB Signaling
            Pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Nguyen,T.D., Watanabe,A., Burleigh,S., Ghaffarzadegan,T.,
            Kanklai,J., Prykhodko,O., Hallenius,F.F. and Nyman,M.
  TITLE     Monobutyrin and monovalerin improve gut-blood-brain biomarkers and
            alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats
  JOURNAL   Sci Rep 12 (1), 15454 (2022)
   PUBMED   36104381
  REMARK    GeneRIF: Monobutyrin and monovalerin improve gut-blood-brain
            biomarkers and alter gut microbiota composition in high-fat fed
            apolipoprotein-E-knockout rats.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Takahashi,S., Kawarabayasi,Y., Nakai,T., Sakai,J. and Yamamoto,T.
  TITLE     Rabbit very low density lipoprotein receptor: a low density
            lipoprotein receptor-like protein with distinct ligand specificity
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9252-9256 (1992)
   PUBMED   1384047
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Feussner,G., Funke,H., Weng,W., Assmann,G., Lackner,K.J. and
            Ziegler,R.
  TITLE     Severe type III hyperlipoproteinemia associated with unusual
            apolipoprotein E1 phenotype and epsilon 1/'null' genotype
  JOURNAL   Eur J Clin Invest 22 (9), 599-608 (1992)
   PUBMED   1360898
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Innerarity,T.L., Mahley,R.W., Weisgraber,K.H. and Bersot,T.P.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. II.
            Receptor binding activity of a high density lipoprotein subfraction
            modulated by the apo(E--A-II) complex
  JOURNAL   J Biol Chem 253 (17), 6289-6295 (1978)
   PUBMED   210175
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Utermann,G., Hees,M. and Steinmetz,A.
  TITLE     Polymorphism of apolipoprotein E and occurrence of
            dysbetalipoproteinaemia in man
  JOURNAL   Nature 269 (5629), 604-607 (1977)
   PUBMED   199847
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC086581.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. All five variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ218891.1, SRR22399492.1538954.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..312
                     /product="apolipoprotein E precursor"
                     /note="apo-E"
                     /calculated_mol_wt=33845
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1927
     mat_peptide     19..312
                     /product="Apolipoprotein E. /id=PRO_0000001996"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
                     /calculated_mol_wt=33845
     Region          72..247
                     /region_name="8 X 22 AA approximate tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          73..258
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL and other lipoprotein receptors binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          150..160
                     /region_name="LDL receptor binding.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          202..282
                     /region_name="Lipid-binding and lipoprotein association.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          258..312
                     /region_name="Homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     Region          270..282
                     /region_name="Specificity for association with VLDL.
                     /evidence=ECO:0000250|UniProtKB:P02649"
                     /note="propagated from UniProtKB/Swiss-Prot (P02650.2)"
     CDS             1..312
                     /gene="Apoe"
                     /gene_synonym="APOEA"
                     /coded_by="NM_001270682.1:116..1054"
                     /db_xref="GeneID:25728"
                     /db_xref="RGD:2138"
ORIGIN      
        1 mkalwalllv plltgclaeg elevtdqlpg qsdqpweqal nrfwdylrwv qtlsdqvqee
       61 lqssqvtqel tvlmedtmte vkaykkelee qlgpvaeetr arlakevqaa qarlgadmed
      121 lrnrlgqyrn evntmlgqst eelrsrlsth lrkmrkrlmr daddlqkrla vykagaqega
      181 ergvsairer lgplveqgrq rtanlgagaa qplrdraqal sdrirgrlee vgnqardrle
      241 evreqmeevr skmeeqtqqi rlqaeifqar ikgwfeplve dmqrqwanlm ekiqasvatn
      301 siasttvple nq
//
LOCUS       NP_001257715             602 aa            linear   ROD 27-APR-2025
DEFINITION  glutaminase liver isoform, mitochondrial isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001257715
VERSION     NP_001257715.1
DBSOURCE    REFSEQ: accession NM_001270786.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Zhou,X., Zhuo,M., Zhang,Y., Shi,E., Ma,X. and Li,H.
  TITLE     miR-190a-5p regulates cardiomyocytes response to ferroptosis via
            directly targeting GLS2
  JOURNAL   Biochem Biophys Res Commun 566, 9-15 (2021)
   PUBMED   34111670
  REMARK    GeneRIF: miR-190a-5p regulates cardiomyocytes response to
            ferroptosis via directly targeting GLS2.
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Cardona,C., Sanchez-Mejias,E., Davila,J.C., Martin-Rufian,M.,
            Campos-Sandoval,J.A., Vitorica,J., Alonso,F.J., Mates,J.M.,
            Segura,J.A., Norenberg,M.D., Rama Rao,K.V., Jayakumar,A.R.,
            Gutierrez,A. and Marquez,J.
  TITLE     Expression of Gls and Gls2 glutaminase isoforms in astrocytes
  JOURNAL   Glia 63 (3), 365-382 (2015)
   PUBMED   25297978
  REMARK    GeneRIF: GABAergic neurons and astrocytes express Gls and Gls2
            isoenzymes in nucleus and mitochondria, in addition to
            glutamatergic neurons
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Savilov,P.N. and Yakovlev,V.N.
  TITLE     Phosphate-dependent glutaminase response to liver injury and
            hyperbaric oxygenation
  JOURNAL   Bull Exp Biol Med 157 (3), 299-301 (2014)
   PUBMED   25065305
  REMARK    GeneRIF: In animals with chronic hepatitis; hyperbaric oxygenation
            restricted the stimulating effect of hepatic resection on
            phosphate-dependent glutaminase activity.
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Martin-Rufian,M., Tosina,M., Campos-Sandoval,J.A., Manzanares,E.,
            Lobo,C., Segura,J.A., Alonso,F.J., Mates,J.M. and Marquez,J.
  TITLE     Mammalian glutaminase Gls2 gene encodes two functional alternative
            transcripts by a surrogate promoter usage mechanism
  JOURNAL   PLoS One 7 (6), e38380 (2012)
   PUBMED   22679499
  REMARK    GeneRIF: Study demonstrated expression of alternative transcripts
            of the mammalian Gls2 gene. Transcriptional mechanisms giving rise
            to GLS2 variants and isolation of novel GLS2 transcripts in human,
            rat and mouse are presented.
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Suzuki,S., Tanaka,T., Poyurovsky,M.V., Nagano,H., Mayama,T.,
            Ohkubo,S., Lokshin,M., Hosokawa,H., Nakayama,T., Suzuki,Y.,
            Sugano,S., Sato,E., Nagao,T., Yokote,K., Tatsuno,I. and Prives,C.
  TITLE     Phosphate-activated glutaminase (GLS2), a p53-inducible regulator
            of glutamine metabolism and reactive oxygen species
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7461-7466 (2010)
   PUBMED   20351271
REFERENCE   7  (residues 1 to 602)
  AUTHORS   Chung-Bok,M.I., Vincent,N., Jhala,U. and Watford,M.
  TITLE     Rat hepatic glutaminase: identification of the full coding sequence
            and characterization of a functional promoter
  JOURNAL   Biochem J 324 (Pt 1) (Pt 1), 193-200 (1997)
   PUBMED   9164856
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Smith,E.M. and Watford,M.
  TITLE     Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence
            similarity to kidney-type glutaminase
  JOURNAL   J Biol Chem 265 (18), 10631-10636 (1990)
   PUBMED   2191954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1 and BC089776.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089776.1, SRR26643286.21266.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..602
                     /product="glutaminase liver isoform, mitochondrial isoform
                     1"
                     /EC_number="3.5.1.2"
                     /note="glutaminase 2 (liver, mitochondrial); GLS;
                     L-glutaminase; L-glutamine amidohydrolase; liver
                     mitochondrial glutaminase"
                     /calculated_mol_wt=64661
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28492.3)"
     transit_peptide 1..14
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P28492.3)"
                     /calculated_mol_wt=1605
     mat_peptide     15..602
                     /product="Glutaminase liver isoform, mitochondrial.
                     /id=PRO_0000011627"
                     /note="propagated from UniProtKB/Swiss-Prot (P28492.3)"
                     /calculated_mol_wt=64661
     Region          46..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28492.3)"
     Region          72..155
                     /region_name="EF-hand_14"
                     /note="EF-hand domain; pfam17959"
                     /db_xref="CDD:465587"
     Region          177..461
                     /region_name="Glutaminase"
                     /note="pfam04960"
                     /db_xref="CDD:461499"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q571F8; propagated from
                     UniProtKB/Swiss-Prot (P28492.3)"
     Site            284
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q571F8; propagated from
                     UniProtKB/Swiss-Prot (P28492.3)"
     Site            329
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q571F8; propagated from
                     UniProtKB/Swiss-Prot (P28492.3)"
     Region          <490..>572
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          490..516
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(491..492,495..497,499..500,504,507,516,518,520,
                     524..525,528..530,532..533,537,540,550,552,554,558..559,
                     562..564,566..567,571)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          518..551
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P28492.3)"
     Region          518..550
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          552..585
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P28492.3)"
     CDS             1..602
                     /gene="Gls2"
                     /gene_synonym="Ga"
                     /coded_by="NM_001270786.1:237..2045"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:192268"
                     /db_xref="RGD:620359"
ORIGIN      
        1 mrsmralqna lsragshgqr ggwghpsrgp llgggvryyf geaaaqgrgt phshqpqhsd
       61 hdasnsgmlp rlgdllfyti aegqeripih kfttalkatg lqtsdprlqd cmskmqrmvq
      121 esssgglldr elfqkcvssn ivlltqafrk kfvipdfeef tghvdrifed akeltggkva
      181 ayiphlaksn pdlwgvslct vdgqrhsvgh tkipfclqsc vkpltyaisv stlgtdyvhk
      241 fvgkepsglr ynklslneeg iphnpmvnag aivvsslikm dcnkaekfdf vlqylnkmag
      301 nefmgfsnat fqseketgdr nyaigyylke kkcfpkgvdm maaldlyfql csvevtcesg
      361 svmaatlang gicpitgesv lsaeavrntl slmhscgmyd fsgqfafhvg lpaksavsga
      421 illvvpnvmg mmclsppldk lgnshrgisf cqklvslfnf hnydnlrhca rkldprregg
      481 evrnktvvnl lfaaysgdvs alrrfalsav dmeqkdydsr talhvaaaeg hidvvkflie
      541 ackvnpfvkd rwgnipldda vqfnhlevvk llqdyhdsym lsetqaevaa etlskenles
      601 mv
//
LOCUS       NP_058830                323 aa            linear   ROD 27-APR-2025
DEFINITION  arginase-1 [Rattus norvegicus].
ACCESSION   NP_058830
VERSION     NP_058830.2
DBSOURCE    REFSEQ: accession NM_017134.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Zhang,M., Wu,Z., Salas,S.S., Aguilar,M.M., Trillos-Almanza,M.C.,
            Buist-Homan,M. and Moshage,H.
  TITLE     Arginase 1 expression is increased during hepatic stellate cell
            activation and facilitates collagen synthesis
  JOURNAL   J Cell Biochem 124 (6), 808-817 (2023)
   PUBMED   37042199
  REMARK    GeneRIF: Arginase 1 expression is increased during hepatic stellate
            cell activation and facilitates collagen synthesis.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Kim,J., Yang,Y.L., Jeong,Y. and Jang,Y.S.
  TITLE     Middle East Respiratory Syndrome-Coronavirus Infection into
            Established hDPP4-Transgenic Mice Accelerates Lung Damage Via
            Activation of the Pro-Inflammatory Response and Pulmonary Fibrosis
  JOURNAL   J Microbiol Biotechnol 30 (3), 427-438 (2020)
   PUBMED   31838832
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Grandvuillemin,I., Buffat,C., Boubred,F., Lamy,E., Fromonot,J.,
            Charpiot,P., Simoncini,S., Sabatier,F., Dignat-George,F.,
            Peyter,A.C., Simeoni,U. and Yzydorczyk,C.
  TITLE     Arginase upregulation and eNOS uncoupling contribute to impaired
            endothelium-dependent vasodilation in a rat model of intrauterine
            growth restriction
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 315 (3), R509-R520 (2018)
   PUBMED   29741931
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Sepa-Kishi,D.M., Katsnelson,G., Bikopoulos,G., Iqbal,A. and
            Ceddia,R.B.
  TITLE     Cold acclimation reduces hepatic protein Kinase B and AMP-activated
            protein kinase phosphorylation and increases gluconeogenesis in
            Rats
  JOURNAL   Physiol Rep 6 (5) (2018)
   PUBMED   29504286
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Kanyo,Z.F., Chen,C.Y., Daghigh,F., Ash,D.E. and Christianson,D.W.
  TITLE     Crystallization and oligomeric structure of rat liver arginase
  JOURNAL   J Mol Biol 224 (4), 1175-1177 (1992)
   PUBMED   1569574
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Takiguchi,M. and Mori,M.
  TITLE     In vitro analysis of the rat liver-type arginase promoter
  JOURNAL   J Biol Chem 266 (14), 9186-9193 (1991)
   PUBMED   2026618
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Yagi,Y., Saheki,T., Imamura,Y., Kobayashi,K., Sase,M., Nakano,K.,
            Matuo,S., Inoue,I., Hagihara,S. and Noda,T.
  TITLE     The heterogeneous distribution of argininosuccinate synthetase in
            the liver of type II citrullinemic patients. Its specificity and
            possible clinical implications
  JOURNAL   Am J Clin Pathol 89 (6), 735-741 (1988)
   PUBMED   3369364
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Ohtake,A., Takiguchi,M., Shigeto,Y., Amaya,Y., Kawamoto,S. and
            Mori,M.
  TITLE     Structural organization of the gene for rat liver-type arginase
  JOURNAL   J Biol Chem 263 (5), 2245-2249 (1988)
   PUBMED   2892837
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Kawamoto,S., Amaya,Y., Murakami,K., Tokunaga,F., Iwanaga,S.,
            Kobayashi,K., Saheki,T., Kimura,S. and Mori,M.
  TITLE     Complete nucleotide sequence of cDNA and deduced amino acid
            sequence of rat liver arginase
  JOURNAL   J Biol Chem 262 (13), 6280-6283 (1987)
   PUBMED   3571256
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1, FM100195.1 and FM120421.1.
            
            On Jan 25, 2008 this sequence version replaced NP_058830.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091158.1, FQ219159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:3571256)
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..323
                     /product="arginase-1"
                     /EC_number="3.5.3.1"
                     /note="type I arginase; liver-type arginase; AI type I
                     arginase; arginase, liver"
                     /calculated_mol_wt=34842
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07824.2)"
     Region          9..303
                     /region_name="Arginase-like"
                     /note="Arginase types I and II and arginase-like family;
                     cd11587"
                     /db_xref="CDD:212536"
     Site            order(14,17,25..26,29,32,49,52..53,242,246,250,254..255,
                     291,294..295,298,302)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:212536"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07824.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61176; propagated from
                     UniProtKB/Swiss-Prot (P07824.2)"
     Site            order(101,124,126,128,141,232,234,277)
                     /site_type="active"
                     /db_xref="CDD:212536"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05089; propagated from
                     UniProtKB/Swiss-Prot (P07824.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05089; propagated from
                     UniProtKB/Swiss-Prot (P07824.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07824.2)"
     CDS             1..323
                     /gene="Arg1"
                     /coded_by="NM_017134.3:146..1117"
                     /db_xref="GeneID:29221"
                     /db_xref="RGD:2150"
ORIGIN      
        1 msskpkpiei igapfskgqp rggvekgpaa lrkaglvekl keteynvrdh gdlafvdvpn
       61 dspfqivknp rsvgkaneql aavvaetqkn gtisvvlggd hsmaigsisg harvhpdlcv
      121 iwvdahtdin tplttssgnl hgqpvafllk elkgkfpdvp gfswvtpcis akdivyiglr
      181 dvdpgehyii ktlgikyfsm tevdklgigk vmeetfsyll grkkrpihls fdvdgldpvf
      241 tpatgtpvvg glsyreglyi teeiyktgll sgldimevnp tlgktpeevt rtvntavalt
      301 lscfgtkreg nhkpetdylk ppk
//
LOCUS       NP_001257504             206 aa            linear   ROD 27-APR-2025
DEFINITION  synaptosomal-associated protein 25 isoform a [Rattus norvegicus].
ACCESSION   NP_001257504
VERSION     NP_001257504.1
DBSOURCE    REFSEQ: accession NM_001270575.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Hu,A., Lan,H., Yao,Z. and Kong,X.
  TITLE     Carbohydrate response element-binding protein (ChREBP) mediates
            decreased SNAP25 expression in islets from diabetic Goto-Kakizaki
            (GK) rats
  JOURNAL   FEBS Open Bio 14 (11), 1864-1872 (2024)
   PUBMED   39300600
  REMARK    GeneRIF: Carbohydrate response element-binding protein (ChREBP)
            mediates decreased SNAP25 expression in islets from diabetic
            Goto-Kakizaki (GK) rats.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Polishchuk,A., Cilleros-Mane,V., Balanya-Segura,M., Just-Borras,L.,
            Fornies-Marine,A., Silvera-Simon,C., Tomas,M., Jami El Hirchi,M.,
            Hurtado,E., Tomas,J. and Lanuza,M.A.
  TITLE     BDNF/TrkB signalling, in cooperation with muscarinic signalling,
            retrogradely regulates PKA pathway to phosphorylate SNAP-25 and
            Synapsin-1 at the neuromuscular junction
  JOURNAL   Cell Commun Signal 22 (1), 371 (2024)
   PUBMED   39044222
  REMARK    GeneRIF: BDNF/TrkB signalling, in cooperation with muscarinic
            signalling, retrogradely regulates PKA pathway to phosphorylate
            SNAP-25 and Synapsin-1 at the neuromuscular junction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kong,X., Lin,C., Yang,C., Wang,X., Li,B., Yan,D., Yang,Y., Hu,A.,
            Chen,Y., Xu,X. and Ma,X.
  TITLE     GLP-1 signaling-regulated SNAP25 is involved in improved insulin
            secretion in diabetic GK rats after Roux-en-Y gastric bypass
            surgery
  JOURNAL   Mol Biol Rep 51 (1), 123 (2024)
   PUBMED   38227062
  REMARK    GeneRIF: GLP-1 signaling-regulated SNAP25 is involved in improved
            insulin secretion in diabetic GK rats after Roux-en-Y gastric
            bypass surgery.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Si,W., Sun,B., Luo,J., Li,Z., Dou,Y. and Wang,Q.
  TITLE     Snap25 attenuates neuronal injury via reducing ferroptosis in acute
            ischemic stroke
  JOURNAL   Exp Neurol 367, 114476 (2023)
   PUBMED   37393984
  REMARK    GeneRIF: Snap25 attenuates neuronal injury via reducing ferroptosis
            in acute ischemic stroke.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chilcote,T.J., Galli,T., Mundigl,O., Edelmann,L., McPherson,P.S.,
            Takei,K. and De Camilli,P.
  TITLE     Cellubrevin and synaptobrevins: similar subcellular localization
            and biochemical properties in PC12 cells
  JOURNAL   J Cell Biol 129 (1), 219-231 (1995)
   PUBMED   7698987
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Garcia,E.P., McPherson,P.S., Chilcote,T.J., Takei,K. and De
            Camilli,P.
  TITLE     rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the
            axon, but are not in a stable complex with syntaxin
  JOURNAL   J Cell Biol 129 (1), 105-120 (1995)
   PUBMED   7698978
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Hess,D.T., Slater,T.M., Wilson,M.C. and Skene,J.H.
  TITLE     The 25 kDa synaptosomal-associated protein SNAP-25 is the major
            methionine-rich polypeptide in rapid axonal transport and a major
            substrate for palmitoylation in adult CNS
  JOURNAL   J Neurosci 12 (12), 4634-4641 (1992)
   PUBMED   1281490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FQ214162.1, DY315301.1 and
            BC087699.1.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein. It is essential for regulated exocytosis in neuronal
            cells. Alternative transcript variants encoding two different
            protein isoforms have been described for this gene. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1, also known as a) encodes
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform a"
                     /note="synaptosomal-associated protein, 25 kDa; SUP;
                     SNAP-25; super protein; synaptosomal-associated 25 kDa
                     protein; synaptosomal-associated protein 25"
                     /calculated_mol_wt=23205
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     CDS             1..206
                     /gene="Snap25"
                     /gene_synonym="SNAP-25a; SNAP-25B"
                     /coded_by="NM_001270575.1:210..830"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:25012"
                     /db_xref="RGD:3728"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqldrv
       61 eegmnhinqd mkeaeknlkd lgkccglfic pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_434690               1492 aa            linear   ROD 27-APR-2025
DEFINITION  copper-transporting ATPase 1 [Rattus norvegicus].
ACCESSION   NP_434690
VERSION     NP_434690.1
DBSOURCE    REFSEQ: accession NM_052803.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1492)
  AUTHORS   Ashino,T., Kohno,T., Sudhahar,V., Ash,D., Ushio-Fukai,M. and
            Fukai,T.
  TITLE     Copper transporter ATP7A interacts with IQGAP1, a Rac1 binding
            scaffolding protein: role in PDGF-induced VSMC migration and
            vascular remodeling
  JOURNAL   Am J Physiol Cell Physiol 315 (6), C850-C862 (2018)
   PUBMED   30257103
  REMARK    GeneRIF: In cultured rat aortic SMCs, PDGF stimulation rapidly
            promoted ATP7A association with IQGAP1 and Rac1 and their
            translocation to the lipid rafts and leading edge. Cotransfection
            assay revealed that ATP7A directly bound to NH2-terminal domain of
            IQGAP1
REFERENCE   2  (residues 1 to 1492)
  AUTHORS   Platonova,N.A., Orlov,I.A., Klotchenko,S.A., Babich,V.S.,
            Ilyechova,E.Y., Babich,P.S., Garmai,Y.P., Vasin,A.V.,
            Tsymbalenko,N.V. and Puchkova,L.V.
  TITLE     Ceruloplasmin gene expression profile changes in the rat mammary
            gland during pregnancy, lactation and involution
  JOURNAL   J Trace Elem Med Biol 43, 126-134 (2017)
   PUBMED   28089327
REFERENCE   3  (residues 1 to 1492)
  AUTHORS   Perez-Siles,G., Grant,A., Ellis,M., Ly,C., Kidambi,A., Khalil,M.,
            Llanos,R.M., Fontaine,S.L., Strickland,A.V., Zuchner,S., Bermeo,S.,
            Neist,E., Brennan-Speranza,T.C., Takata,R.I., Speck-Martins,C.E.,
            Mercer,J.F., Nicholson,G.A. and Kennerson,M.L.
  TITLE     Characterizing the molecular phenotype of an Atp7a(T985I)
            conditional knock in mouse model for X-linked distal hereditary
            motor neuropathy (dHMNX)
  JOURNAL   Metallomics 8 (9), 981-992 (2016)
   PUBMED   27293072
REFERENCE   4  (residues 1 to 1492)
  AUTHORS   Han,M., Chang,J. and Kim,J.
  TITLE     Loss of divalent metal transporter 1 function promotes brain copper
            accumulation and increases impulsivity
  JOURNAL   J Neurochem 138 (6), 918-928 (2016)
   PUBMED   27331785
REFERENCE   5  (residues 1 to 1492)
  AUTHORS   Cao,Z., Zhang,Y., Sun,T., Zhang,S., Yu,W. and Zhu,J.
  TITLE     Homocysteine induces cardiac hypertrophy by up-regulating ATP7a
            expression
  JOURNAL   Int J Clin Exp Pathol 8 (10), 12829-12836 (2015)
   PUBMED   26722473
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1492)
  AUTHORS   Starcher,B., Madaras,J.A., Fisk,D., Perry,E.F. and Hill,C.H.
  TITLE     Abnormal cellular copper metabolism in the blotchy mouse
  JOURNAL   J Nutr 108 (8), 1229-1233 (1978)
   PUBMED   27591
REFERENCE   7  (residues 1 to 1492)
  AUTHORS   Starcher,B.C., Madaras,J.A. and Tepper,A.S.
  TITLE     Lysyl oxidase deficiency in lung and fibroblasts from mice with
            hereditary emphysema
  JOURNAL   Biochem Biophys Res Commun 78 (2), 706-712 (1977)
   PUBMED   20889
REFERENCE   8  (residues 1 to 1492)
  AUTHORS   Rowe,D.W., McGoodwin,E.B., Martin,G.R. and Grahn,D.
  TITLE     Decreased lysyl oxidase activity in the aneurysm-prone, mottled
            mouse
  JOURNAL   J Biol Chem 252 (3), 939-942 (1977)
   PUBMED   14140
REFERENCE   9  (residues 1 to 1492)
  AUTHORS   Hunt,D.M.
  TITLE     Catecholamine biosynthesis and the activity of a number of
            copper-dependent enzymes in the copper deficient mottled mouse
            mutants
  JOURNAL   Comp Biochem Physiol C Comp Pharmacol 57 (1), 79-83 (1977)
   PUBMED   17511
REFERENCE   10 (residues 1 to 1492)
  AUTHORS   Hunt,D.M.
  TITLE     A study of copper treatment and tissue copper levels in the murine
            congenital copper deficiency, mottled
  JOURNAL   Life Sci 19 (12), 1913-1919 (1976)
   PUBMED   187892
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U59245.1.
            
            Summary: This gene encodes a transmembrane protein that functions
            in copper transport across membranes. The protein localizes to the
            trans-Golgi network, where it is predicted to supply copper to
            copper-dependent enzymes in the secretory pathway. The protein
            relocalizes to the plasma membrane under conditions of elevated
            extracellular copper and functions in the efflux of copper from
            cells. In human, mutations in this gene result in Menkes disease,
            X-linked cutis laxa, and occipital horn syndrome. [provided by
            RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U59245.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1492
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..1492
                     /product="copper-transporting ATPase 1"
                     /EC_number="7.2.2.8"
                     /function="pump copper out of cells"
                     /note="copper pump 1; menkes disease-associated protein
                     homolog; ATPase, Cu++ transporting, alpha polypeptide"
                     /calculated_mol_wt=161963
     Region          11..73
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(17..19,22)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          174..236
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(180..182,185)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          280..337
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(286..288,291)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64430; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          380..442
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(386..388,391)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          484..545
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(489..491,494)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          559..622
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(565..567,570)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          646..1380
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            646..667
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            678
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            707..726
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            734..754
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            774..794
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            928..951
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            982..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            order(992,994,1357)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(1036..1038,1106,1174..1176,1206,1246..1248,1268,
                     1271,1274,1293,1296)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            1204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1349..1366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            1378..1397
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            1422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          1459..1460
                     /region_name="Endocytosis signal.
                     /evidence=ECO:0000250|UniProtKB:Q64430"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            1461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04656; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64430; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          1478..1492
                     /region_name="PDZD11-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     Site            1478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64430; propagated from
                     UniProtKB/Swiss-Prot (P70705.1)"
     Region          1479..1480
                     /region_name="Endocytosis signal.
                     /evidence=ECO:0000250|UniProtKB:Q64430"
                     /note="propagated from UniProtKB/Swiss-Prot (P70705.1)"
     CDS             1..1492
                     /gene="Atp7a"
                     /gene_synonym="Mnk"
                     /coded_by="NM_052803.2:22..4500"
                     /db_xref="GeneID:24941"
                     /db_xref="RGD:2179"
ORIGIN      
        1 mepnmdansi titvegmtci scvrtieqqi gkvngvhhik vsleeksatv iynpklqtpk
       61 tlqeaiddmg fdallhnanp lpvltntvfl tvtaplalpw dhiqstllkt kgvtgvkisp
      121 qqrsavvtii psvvsanqiv elvpdlsldm gtqekksgts eehstpqage vllkmrvegm
      181 tchsctstie gkvgklqgvq rikvsldnqe ativyqphli taeeikkqie avgfpafikk
      241 qpkylklgai dverlkstpv kssegsqqks paypsdsait ftidgmhcks cvsniesals
      301 tlqyvssivv slenrsaivk ynaslvtpei lrkaieavsp gqyrvsisse vesptsspss
      361 sslqkmplnl vsqpltqevv iningmtcns cvqsiegvis kkpgvksihv sltnstgtie
      421 ydplltspep lreaiedmgf davlpadmke plvviaqpsl etpllpstte penvmtpvqn
      481 kcyiqvsgmt cascvanier nlrreegiys vlvalmagka evrynpaviq prviaelire
      541 lgfgavvmen agegngilel vvrgmtcasc vhkiestltk hkgifycsva latnkahiky
      601 dpeiigprdi ihtignlgfe aslvkkdrsa nhldhkreik qwrgsflvsl ffcipvmglm
      661 iymmvmdhhl atlnhnqnms neeminmhss mflerqilpg lsimnllsll lclpvqfcgg
      721 wyfyiqayka lrhktanmdv livlattiaf ayslvillva myerakvnpi tffdtppmlf
      781 vfialgrwle hiakgktsea laklislqat eativtlnse nlllseeqvd velvqrgdii
      841 kvvpggkfpv dgrvieghsm vdeslitgea mpvakkpgst viagsinqng sllirathvg
      901 adttlsqivk lveeaqtska piqqfadkls gyfvpfivlv sivtllvwii igfqnfeive
      961 ayfpgynrsi srtetiirfa fqasitvlci acpcslglat ptavmvgtgv gaqngilikg
     1021 geplemahkv kvvvfdktgt ithgtpvvnq vkvlvesnki srnkilaivg taesnsehpl
     1081 gaavtkyckq eldtetlgtc tdfqvvpgcg isckvtnieg llhksnlkie enniknaslv
     1141 qidaineqss psssmiidah lsnavntqqy kvlignrewm irnglvisnd vdesmieher
     1201 rgrtavlvti ddelcgliai adtvkpeael avhilksmgl evvlmtgdns ktarsiasqv
     1261 gitkvfaevl pshkvakvkq lqeegkrvam vgdgindspa lamasvgiai gtgtdvaiea
     1321 advvlirndl ldvvasidls rktvkririn fvfaliynli gipiaagvfl piglvlqpwm
     1381 gsaamaassv svvlsslflk lyrkptydny elrprshtgq rspseisvhv giddtsrnsp
     1441 rlglldrivn ysrasinsll sdkrslnsvv tsepdkhsll vgdfredddt tl
//
LOCUS       NP_001258177              95 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 9 [Rattus norvegicus].
ACCESSION   NP_001258177
VERSION     NP_001258177.1
DBSOURCE    REFSEQ: accession NM_001271248.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 95)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 95)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 95)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 95)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 95)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 95)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 95)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1 and CO556486.1.
            
            Transcript Variant: This variant (9) differs in both UTR's and the
            coding region but maintains the reading frame, compared to variant
            3. This results in a protein (isoform 9) that is shorter at both
            the N- and C-termini, compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.449459.1, CO556486.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..95
                     /product="cAMP-responsive element modulator isoform 9"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=10705
     Region          39..93
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          40..92
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(40,44,46..48,50..52,54..55,57..59)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(58,61,65..66,68..69,72..73,75..76,79,82..83,86..87,
                     89..90)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..95
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_001271248.1:208..495"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mptyqirapt talpqgvvma aspgslhspq qlaeeatrkr elrlmknrea akecrrrkke
       61 yvkclesrva vlevqnkkli eeletlkdic spktd
//
LOCUS       NP_445859                394 aa            linear   ROD 27-APR-2025
DEFINITION  acid ceramidase precursor [Rattus norvegicus].
ACCESSION   NP_445859
VERSION     NP_445859.2
DBSOURCE    REFSEQ: accession NM_053407.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Gulbins,E., Palmada,M., Reichel,M., Luth,A., Bohmer,C., Amato,D.,
            Muller,C.P., Tischbirek,C.H., Groemer,T.W., Tabatabai,G.,
            Becker,K.A., Tripal,P., Staedtler,S., Ackermann,T.F., van
            Brederode,J., Alzheimer,C., Weller,M., Lang,U.E., Kleuser,B.,
            Grassme,H. and Kornhuber,J.
  TITLE     Acid sphingomyelinase-ceramide system mediates effects of
            antidepressant drugs
  JOURNAL   Nat Med 19 (7), 934-938 (2013)
   PUBMED   23770692
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Lucki,N.C., Li,D., Bandyopadhyay,S., Wang,E., Merrill,A.H. and
            Sewer,M.B.
  TITLE     Acid ceramidase (ASAH1) represses steroidogenic factor 1-dependent
            gene transcription in H295R human adrenocortical cells by binding
            to the receptor
  JOURNAL   Mol Cell Biol 32 (21), 4419-4431 (2012)
   PUBMED   22927646
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Lucki,N.C., Bandyopadhyay,S., Wang,E., Merrill,A.H. and Sewer,M.B.
  TITLE     Acid ceramidase (ASAH1) is a global regulator of steroidogenic
            capacity and adrenocortical gene expression
  JOURNAL   Mol Endocrinol 26 (2), 228-243 (2012)
   PUBMED   22261821
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Strelow,A., Bernardo,K., Adam-Klages,S., Linke,T., Sandhoff,K.,
            Kronke,M. and Adam,D.
  TITLE     Overexpression of acid ceramidase protects from tumor necrosis
            factor-induced cell death
  JOURNAL   J Exp Med 192 (5), 601-612 (2000)
   PUBMED   10974027
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Li,C.M., Park,J.H., He,X., Levy,B., Chen,F., Arai,K., Adler,D.A.,
            Disteche,C.M., Koch,J., Sandhoff,K. and Schuchman,E.H.
  TITLE     The human acid ceramidase gene (ASAH): structure, chromosomal
            location, mutation analysis, and expression
  JOURNAL   Genomics 62 (2), 223-231 (1999)
   PUBMED   10610716
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Li,C.M., Hong,S.B., Kopal,G., He,X., Linke,T., Hou,W.S., Koch,J.,
            Gatt,S., Sandhoff,K. and Schuchman,E.H.
  TITLE     Cloning and characterization of the full-length cDNA and genomic
            sequences encoding murine acid ceramidase
  JOURNAL   Genomics 50 (2), 267-274 (1998)
   PUBMED   9653654
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Longo,C.A., Tyler,D. and Mallampalli,R.K.
  TITLE     Sphingomyelin metabolism is developmentally regulated in rat lung
  JOURNAL   Am J Respir Cell Mol Biol 16 (5), 605-612 (1997)
   PUBMED   9160843
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Bernardo,K., Hurwitz,R., Zenk,T., Desnick,R.J., Ferlinz,K.,
            Schuchman,E.H. and Sandhoff,K.
  TITLE     Purification, characterization, and biosynthesis of human acid
            ceramidase
  JOURNAL   J Biol Chem 270 (19), 11098-11102 (1995)
   PUBMED   7744740
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061540.1.
            
            On Dec 20, 2003 this sequence version replaced NP_445859.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061540.1, AF214647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..394
                     /product="acid ceramidase precursor"
                     /EC_number="3.5.1.23"
                     /note="acid ceramidase; AC; acylsphingosine deacylase;
                     ACDase; acid CDase; N-acylsphingosine amidohydrolase (acid
                     ceramidase) 1; N-acylethanolamine hydrolase ASAH1"
                     /calculated_mol_wt=42386
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2076
     mat_peptide     21..394
                     /product="Acid ceramidase. /id=PRO_0000378102"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7S1.1)"
                     /calculated_mol_wt=42386
     Region          44..107
                     /region_name="NAAA-beta"
                     /note="beta subunit of N-acylethanolamine-hydrolyzing acid
                     amidase; pfam15508"
                     /db_xref="CDD:464754"
     Region          133..377
                     /region_name="Ntn_AC_NAAA"
                     /note="AC_NAAA This conserved domain includes two closely
                     related proteins, acid ceramidase (AC, also known as
                     N-acylsphingosine amidohydrolase), and
                     N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC
                     catalyzes the hydrolysis of ceramide to sphingosine
                     and...; cd01903"
                     /db_xref="CDD:238886"
     Site            161
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:Q13510; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            319
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:Q13510; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            332
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:Q13510; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P7S1.1)"
     CDS             1..394
                     /gene="Asah1"
                     /gene_synonym="Asah"
                     /coded_by="NM_053407.3:35..1219"
                     /db_xref="GeneID:84431"
                     /db_xref="RGD:621568"
ORIGIN      
        1 mlgrslltwv laaavtcaqa qqvppwtedc rkstyppsgp tyrgpvpwyt inldlppykr
       61 whellahkap vlrtlvnsis nlvnafvpsg kimqmvdekl pgligsipgp fgeemrgiad
      121 vtgiplgeii sfnifyelft mctsiitedg kghllhgrnm dfgiflgwni nnntwvvtee
      181 lkpltvnldf qrnnktvfka tsfagyvgml tgfkpgllsl tlnerfslng gylgilewmf
      241 gkknaqwvgf itrsvlenst syeeaknilt ktkitapayf ilggnqsgeg cvitrerkes
      301 ldvyeldpkh grwyvvqtny drwkntlfld drrtpakkcl nhttqknlsf atiydvlstk
      361 pvlnkltvft tlidvtkdqf eshlrdcpdp cigw
//
LOCUS       NP_058768               1500 aa            linear   ROD 27-APR-2025
DEFINITION  carbamoyl-phosphate synthase [ammonia], mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_058768 XP_346853
VERSION     NP_058768.1
DBSOURCE    REFSEQ: accession NM_017072.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1500)
  AUTHORS   Cao,Y., Ding,W., Zhang,J., Gao,Q., Yang,H., Cao,W., Wang,Z.,
            Fang,L. and Du,R.
  TITLE     Significant Down-Regulation of Urea Cycle Generates Clinically
            Relevant Proteomic Signature in Hepatocellular Carcinoma Patients
            with Macrovascular Invasion
  JOURNAL   J Proteome Res 18 (5), 2032-2044 (2019)
   PUBMED   30901224
REFERENCE   2  (residues 1 to 1500)
  AUTHORS   Khoja,S., Nitzahn,M., Hermann,K., Truong,B., Borzone,R., Willis,B.,
            Rudd,M., Palmer,D.J., Ng,P., Brunetti-Pierri,N. and Lipshutz,G.S.
  TITLE     Conditional disruption of hepatic carbamoyl phosphate synthetase 1
            in mice results in hyperammonemia without orotic aciduria and can
            be corrected by liver-directed gene therapy
  JOURNAL   Mol Genet Metab 124 (4), 243-253 (2018)
   PUBMED   29801986
REFERENCE   3  (residues 1 to 1500)
  AUTHORS   Martin,J., Balmer,M.L., Rajendran,S., Maurhofer,O., Dufour,J.F. and
            St-Pierre,M.V.
  TITLE     Nutritional stress exacerbates hepatic steatosis induced by
            deletion of the histidine nucleotide-binding (Hint2) mitochondrial
            protein
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 310 (7), G497-G509 (2016)
   PUBMED   26767982
REFERENCE   4  (residues 1 to 1500)
  AUTHORS   Carter,W.G., Vigneswara,V., Newlaczyl,A., Wayne,D., Ahmed,B.,
            Saddington,S., Brewer,C., Raut,N., Gerdes,H.K., Erdozain,A.M.,
            Tooth,D., Bolt,E.L., Osna,N.A., Tuma,D.J. and Kharbanda,K.K.
  TITLE     Isoaspartate, carbamoyl phosphate synthase-1, and carbonic
            anhydrase-III as biomarkers of liver injury
  JOURNAL   Biochem Biophys Res Commun 458 (3), 626-631 (2015)
   PUBMED   25684186
  REMARK    GeneRIF: The results suggest that elevated isoaspartate and CPS-1,
            and reduced CA-III levels could serve as biomarkers of
            hepatocellular injury.
REFERENCE   5  (residues 1 to 1500)
  AUTHORS   Takakusa,H., Mohar,I., Kavanagh,T.J., Kelly,E.J., Kaspera,R. and
            Nelson,S.D.
  TITLE     Protein tyrosine nitration of mitochondrial carbamoyl phosphate
            synthetase 1 and its functional consequences
  JOURNAL   Biochem Biophys Res Commun 420 (1), 54-60 (2012)
   PUBMED   22402285
REFERENCE   6  (residues 1 to 1500)
  AUTHORS   Brandt,M.A. and Powers-Lee,S.G.
  TITLE     The interaction of cardiolipin with rat liver carbamoyl phosphate
            synthetase I
  JOURNAL   Arch Biochem Biophys 290 (1), 14-20 (1991)
   PUBMED   1898084
REFERENCE   7  (residues 1 to 1500)
  AUTHORS   Moorman,A.F., de Boer,P.A., Charles,R. and Lamers,W.H.
  TITLE     Diet- and hormone-induced reversal of the carbamoylphosphate
            synthetase mRNA gradient in the rat liver lobulus
  JOURNAL   FEBS Lett 276 (1-2), 9-13 (1990)
   PUBMED   1979948
REFERENCE   8  (residues 1 to 1500)
  AUTHORS   de Groot,C.J., ten Voorde,G.H., van Andel,R.E., te Kortschot,A.,
            Gaasbeek Janzen,J.W., Wilson,R.H., Moorman,A.F., Charles,R. and
            Lamers,W.H.
  TITLE     Reciprocal regulation of glutamine synthetase and
            carbamoylphosphate synthetase levels in rat liver
  JOURNAL   Biochim Biophys Acta 908 (3), 231-240 (1987)
   PUBMED   2882780
REFERENCE   9  (residues 1 to 1500)
  AUTHORS   Nyunoya,H., Broglie,K.E., Widgren,E.E. and Lusty,C.J.
  TITLE     Characterization and derivation of the gene coding for
            mitochondrial carbamyl phosphate synthetase I of rat
  JOURNAL   J Biol Chem 260 (16), 9346-9356 (1985)
   PUBMED   2991241
REFERENCE   10 (residues 1 to 1500)
  AUTHORS   Karsai,T., Rady,P., Nagy,Z. and Szondy,Z.
  TITLE     Effect of dimethylnitrosamine upon carbamoyl phosphate and
            ornithine utilization in rat liver
  JOURNAL   Anticancer Res 5 (4), 441-444 (1985)
   PUBMED   2864015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346853.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.37897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1500
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..1500
                     /product="carbamoyl-phosphate synthase [ammonia],
                     mitochondrial precursor"
                     /EC_number="6.3.4.16"
                     /note="carbamoyl-phosphate synthase [ammonia],
                     mitochondrial; carboamyl-phosphate synthetase 1;
                     carbamoyl-phosphate synthetase 1, mitochondrial; CPSase I;
                     carbamoyl-phosphate synthetase I; carbamyl phosphate
                     synthetase I; carbamyl-phosphate synthetase"
                     /calculated_mol_wt=160319
     transit_peptide 1..38
                     /note="Mitochondrion; propagated from UniProtKB/Swiss-Prot
                     (P07756.1)"
                     /calculated_mol_wt=4280
     mat_peptide     39..1500
                     /product="Carbamoyl-phosphate synthase [ammonia],
                     mitochondrial. /id=PRO_0000029899"
                     /note="propagated from UniProtKB/Swiss-Prot (P07756.1)"
                     /calculated_mol_wt=160319
     Region          39..218
                     /region_name="Anthranilate phosphoribosyltransferase
                     homolog"
                     /note="propagated from UniProtKB/Swiss-Prot (P07756.1)"
     Region          46..400
                     /region_name="CPSaseIIsmall"
                     /note="carbamoyl-phosphate synthase, small subunit;
                     TIGR01368"
                     /db_xref="CDD:273580"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            157
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            214
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            228
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            280
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            287
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            310
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            412
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Region          419..1477
                     /region_name="CPSaseII_lrg"
                     /note="carbamoyl-phosphate synthase, large subunit;
                     TIGR01369"
                     /db_xref="CDD:273581"
     Site            453
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            458
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            522
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            527
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            532
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            537
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000269|PubMed:24098488; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            553
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            560
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31327; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            575
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            603
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            612
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            630
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            751
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            757
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            772
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            793
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            811
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            831
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            841
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            856
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            875
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            889
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            892
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            908
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            915
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            919
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            935
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1036
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1074
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31327; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1100
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1183
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31327; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1222
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1232
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1269
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1291
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1331
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24098488; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1332
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:24098488; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1356
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31327; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1444
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1471
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1479
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     Site            1486
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8C196; propagated from
                     UniProtKB/Swiss-Prot (P07756.1)"
     CDS             1..1500
                     /gene="Cps1"
                     /gene_synonym="cps; cps-1"
                     /coded_by="NM_017072.2:336..4838"
                     /db_xref="GeneID:497840"
                     /db_xref="RGD:2395"
ORIGIN      
        1 mtriltackv vktlksgfgl anvtskrqwd fsrpgirlls vkaqtahivl edgtkmkgys
       61 fghpssvage vvfntglggy sealtdpayk gqiltmanpi ignggapdtt ardelglnky
      121 mesdgikvag llvlnyshdy nhwlatkslg qwlqeekvpa iygvdtrmlt kiirdkgtml
      181 gkiefegqsv dfvdpnkqnl iaevstkdvk vfgkgnptkv vavdcgiknn virllvkrga
      241 evhlvpwnhd ftqmdydgll iaggpgnpal aqpliqnvkk ilesdrkepl fgistgniit
      301 glaagaksyk msmanrgqnq pvlnitnrqa fitaqnhgya ldntlpagwk plfvnvndqt
      361 negimheskp ffavqfhpev spgptdteyl fdsffslikk gkgttitsvl pkpalvasrv
      421 evskvlilgs gglsigqage fdysgsqavk amkeenvktv lmnpniasvq tnevglkqad
      481 avyflpitpq fvtevikaer pdglilgmgg qtalncgvel fkrgvlkeyg vkvlgtsves
      541 imatedrqlf sdklneinek iapsfavesm edalkaadti gypvmirsay algglgsgic
      601 pnketlmdlg tkafamtnqi lversvtgwk eieyevvrda ddncvtvcnm envdamgvht
      661 gdsvvvapaq tlsnaefqml rrtsinvvrh lgivgecniq falhptsmey ciievnarls
      721 rssalaskat gyplafiaak ialgiplpei knvvsgktsa cfepsldymv tkiprwdldr
      781 fhgtssrigs smksvgevma igrtfeesfq kalrmchpsv dgftprlpmn kewpanldlr
      841 kelsepsstr iyaiakalen nmsldeivkl tsidkwflyk mrdilnmdkt lkglnsesvt
      901 eetlrqakei gfsdkqiskc lglteaqtre lrlkknihpw vkqidtlaae ypsvtnylyv
      961 tyngqehdik fdehgimvlg cgpyhigssv efdwcavssi rtlrqlgkkt vvvncnpetv
     1021 stdfdecdkl yfeelsleri ldiyhqeacn gciisvggqi pnnlavplyk ngvkimgtsp
     1081 lqidraedrs ifsavldelk vaqapwkavn tlnealefan svgypcllrp syvlsgsamn
     1141 vvfsedemkr fleeatrvsq ehpvvltkfi egarevemda vgkegrvish aisehvedag
     1201 vhsgdatlml ptqtisqgai ekvkdatrki akafaisgpf nvqflvkgnd vlviecnlra
     1261 srsfpfvskt lgvdfidvat kvmigesvde khlptleqpi ipsdyvaika pmfswprlrd
     1321 adpilrcema stgevacfge gihtaflkam lstgfkipqk giligiqqsf rprflgvaeq
     1381 lhnegfklfa teatsdwlna nnvpatpvaw psqegqnpsl ssirklirdg sidlvinlpn
     1441 nntkfvhdny virrtavdsg ialltnfqvt klfaeavqka rtvdskslfh yrqysagkaa
//
LOCUS       NP_001029178             770 aa            linear   ROD 27-APR-2025
DEFINITION  arf-GAP with coiled-coil, ANK repeat and PH domain-containing
            protein 2 [Rattus norvegicus].
ACCESSION   NP_001029178 XP_001073652
VERSION     NP_001029178.1
DBSOURCE    REFSEQ: accession NM_001034006.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Etoh,K. and Fukuda,M.
  TITLE     Structure-function analyses of the small GTPase Rab35 and its
            effector protein centaurin-beta2/ACAP2 during neurite outgrowth of
            PC12 cells
  JOURNAL   J Biol Chem 290 (14), 9064-9074 (2015)
   PUBMED   25694427
  REMARK    GeneRIF: showed by knockdown-rescue approaches that neither a
            centaurin-beta2 binding-deficient Rab35(T76S/T81A) mutant nor a
            Rab35 binding-deficient centaurin-beta2(N610A/N691A) mutant
            supported neurite outgrowth of PC12 cells
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Miyamoto,Y., Yamamori,N., Torii,T., Tanoue,A. and Yamauchi,J.
  TITLE     Rab35, acting through ACAP2 switching off Arf6, negatively
            regulates oligodendrocyte differentiation and myelination
  JOURNAL   Mol Biol Cell 25 (9), 1532-1542 (2014)
   PUBMED   24600047
  REMARK    GeneRIF: Rab35/ACAP2 and cytohesin-2 antagonistically control
            oligodendrocyte differentiation and myelination through Arf6
            regulation.
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Kobayashi,H. and Fukuda,M.
  TITLE     Rab35 establishes the EHD1-association site by coordinating two
            distinct effectors during neurite outgrowth
  JOURNAL   J Cell Sci 126 (Pt 11), 2424-2435 (2013)
   PUBMED   23572513
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Kobayashi,H. and Fukuda,M.
  TITLE     Rab35 regulates Arf6 activity through centaurin-beta2 (ACAP2)
            during neurite outgrowth
  JOURNAL   J Cell Sci 125 (Pt 9), 2235-2243 (2012)
   PUBMED   22344257
  REMARK    GeneRIF: Rab35 regulates Arf6 activity through centaurin-beta2
            (ACAP2) during neurite outgrowth.
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Jackson,T.R., Brown,F.D., Nie,Z., Miura,K., Foroni,L., Sun,J.,
            Hsu,V.W., Donaldson,J.G. and Randazzo,P.A.
  TITLE     ACAPs are arf6 GTPase-activating proteins that function in the cell
            periphery
  JOURNAL   J Cell Biol 151 (3), 627-638 (2000)
   PUBMED   11062263
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001073652.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090073.1, SRR26643291.31392.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..770
                     /product="arf-GAP with coiled-coil, ANK repeat and PH
                     domain-containing protein 2"
                     /note="centaurin-beta-2"
                     /calculated_mol_wt=87099
     Region          18..217
                     /region_name="BAR_ACAP2"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     Coiled-coil, ANK repeat and PH domain containing protein
                     2; cd07638"
                     /db_xref="CDD:153322"
     Site            order(27,30..31,35,37..38,41..42,44..45,55..56,58..59,
                     62..63,65..66,69,83,86..87,178,181..182,184,189,192..193,
                     195..196,199..200,203..204,206..207,210..211,213..214)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153322"
     Region          269..365
                     /region_name="PH_ACAP"
                     /note="ArfGAP with coiled-coil, ankyrin repeat and PH
                     domains Pleckstrin homology (PH) domain; cd13250"
                     /db_xref="CDD:270070"
     Region          371..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15057; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQK5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Region          399..513
                     /region_name="ArfGap_ACAP2"
                     /note="ArfGAP domain of ACAP2 (ArfGAP with Coiled-coil,
                     ANK repeat and PH domains 2); cd08851"
                     /db_xref="CDD:350076"
     Site            order(414,417,434,437,442)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350076"
     Site            order(414,417,434,437)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350076"
     Site            order(439,442..443,452,456..457,496)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350076"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Region          548..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15057; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6ZQK5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Region          <602..733
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(607..609,611..612,616,619,628,630,634,638..639,
                     642..644,646..647,651,654,663,665,667,671..672,675..677,
                     679..680,684,687,696)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          630..663
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          632..661
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Region          665..696
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          665..694
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Region          698..727
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q15057; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15057; propagated from
                     UniProtKB/Swiss-Prot (Q5FVC7.1)"
     CDS             1..770
                     /gene="Acap2"
                     /gene_synonym="Centb2; cnt-b2"
                     /coded_by="NM_001034006.2:286..2598"
                     /db_xref="GeneID:619382"
                     /db_xref="RGD:1562939"
ORIGIN      
        1 mkmtvdfeec lkdsprfraa leevegdvae lelkldklvk lciamidtgk afcaankqfm
       61 ngirdlaqys sndavvetsl tkfsdslqem infhtilfdq tqrsikaqlq nfvkedlrkf
      121 kdakkqfekv seekenalvk naqvqrnkqh eveeaanilt atrkcfrhia ldyvlqinvl
      181 qskrrseilk smlsfmyahl affhqgydlf selgpymkdl gaqldrlvvd aakekremeq
      241 khstiqqkdf ssddskleyn vdaangivme gylfkrasna fktwnrrwfs iqnnqlvyqk
      301 kfkdsptvvv edlrlctvkh cedierrfcf evvsptkscm lqadseklrq awikavqtsi
      361 atayrekgde sekldkkssp stgsldsgse skekllkges alqrvqcipg ntsccdcgla
      421 dprwasinlg itlciecsgi hrslgvhfsk vrsltldtwe pellklmcel gndvinrvye
      481 aklekmgvkk pqpgqrqeke ayirakyver kfvdkystll spseqekrii skscedqrls
      541 htrvsvhtpv ksndsgiqqc sddgreslps tvsanslyep egerqessvf ldskhlnpgl
      601 qlyrasyekn lpkmaealah gadvnwansd enqatpliqa vlggslvtce fllqnganvn
      661 qrdvqgrgpl hhatvlghtg qvclflkrga nqhatdeegk dplsiaveaa nadivtllrl
      721 armneemres eglygqpgde tyqdifrdfs qmasnnpekl nrfqqdsqkf
//
LOCUS       NP_001257525            2733 aa            linear   ROD 27-APR-2025
DEFINITION  inositol 1,4,5-trisphosphate-gated calcium channel ITPR1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001257525
VERSION     NP_001257525.1
DBSOURCE    REFSEQ: accession NM_001270596.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2733)
  AUTHORS   Pan,D., Jiang,M., Tao,G., Shi,J., Song,Z., Chen,R. and Wang,D.
  TITLE     The role of Ca2+ signalling and InsP3R in the pathogenesis of
            intrahepatic cholestasis of pregnancy
  JOURNAL   J Obstet Gynaecol 44 (1), 2345276 (2024)
   PUBMED   38685831
  REMARK    GeneRIF: The role of Ca[2+] signalling and InsP3R in the
            pathogenesis of intrahepatic cholestasis of pregnancy.
REFERENCE   2  (residues 1 to 2733)
  AUTHORS   Shi,R., Liu,Z., Yue,H., Li,M., Liu,S., De,D., Li,R., Chen,Y.,
            Cheng,S., Gu,X., Jia,M., Li,J., Li,J., Zhang,S., Feng,N., Fan,R.,
            Fu,F., Liu,Y., Ding,M. and Pei,J.
  TITLE     IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin
  JOURNAL   Cell Mol Biol Lett 29 (1), 22 (2024)
   PUBMED   38308199
  REMARK    GeneRIF: IP3R1-mediated MAMs formation contributes to mechanical
            trauma-induced hepatic injury and the protective effect of
            melatonin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2733)
  AUTHORS   Obaid,A.A., Almasmoum,H., Almaimani,R.A., El-Boshy,M., Aslam,A.,
            Idris,S., Ghaith,M.M., El-Readi,M.Z., Ahmad,J., Farrash,W.F.,
            Mujalli,A., Eid,S.Y., Elzubier,M.E. and Refaat,B.
  TITLE     Vitamin D and calcium co-therapy mitigates pre-established cadmium
            nephropathy by regulating renal calcium homeostatic molecules and
            improving anti-oxidative and anti-inflammatory activities in rat
  JOURNAL   J Trace Elem Med Biol 79, 127221 (2023)
   PUBMED   37244046
REFERENCE   4  (residues 1 to 2733)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   5  (residues 1 to 2733)
  AUTHORS   Fan,G., Baker,M.R., Terry,L.E., Arige,V., Chen,M., Seryshev,A.B.,
            Baker,M.L., Ludtke,S.J., Yule,D.I. and Serysheva,I.I.
  TITLE     Conformational motions and ligand-binding underlying gating and
            regulation in IP3R channel
  JOURNAL   Nat Commun 13 (1), 6942 (2022)
   PUBMED   36376291
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2733)
  AUTHORS   Zhang,S.X., Zhang,J.P., Fletcher,D.L., Zoeller,R.T. and Sun,G.Y.
  TITLE     In situ hybridization of mRNA expression for IP3 receptor and
            IP3-3-kinase in rat brain after transient focal cerebral ischemia
  JOURNAL   Brain Res Mol Brain Res 32 (2), 252-260 (1995)
   PUBMED   7500836
REFERENCE   7  (residues 1 to 2733)
  AUTHORS   Takei,K., Stukenbrok,H., Metcalf,A., Mignery,G.A., Sudhof,T.C.,
            Volpe,P. and De Camilli,P.
  TITLE     Ca2+ stores in Purkinje neurons: endoplasmic reticulum
            subcompartments demonstrated by the heterogeneous distribution of
            the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin
  JOURNAL   J Neurosci 12 (2), 489-505 (1992)
   PUBMED   1311032
REFERENCE   8  (residues 1 to 2733)
  AUTHORS   Suzuki,T., Abe-Dohmae,S. and Tanaka,R.
  TITLE     P400 protein is one of the major substrates for
            Ca2+/calmodulin-dependent protein kinase II in the postsynaptic
            density-enriched fraction isolated from rat cerebral cortex,
            hippocampus and cerebellum
  JOURNAL   Neurochem Int 20 (1), 61-67 (1992)
   PUBMED   1338970
REFERENCE   9  (residues 1 to 2733)
  AUTHORS   Danoff,S.K., Ferris,C.D., Donath,C., Fischer,G.A., Munemitsu,S.,
            Ullrich,A., Snyder,S.H. and Ross,C.A.
  TITLE     Inositol 1,4,5-trisphosphate receptors: distinct neuronal and
            nonneuronal forms derived by alternative splicing differ in
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2951-2955 (1991)
   PUBMED   1849282
REFERENCE   10 (residues 1 to 2733)
  AUTHORS   Mignery,G.A., Newton,C.L., Archer,B.T. 3rd and Sudhof,T.C.
  TITLE     Structure and expression of the rat inositol 1,4,5-trisphosphate
            receptor
  JOURNAL   J Biol Chem 265 (21), 12679-12685 (1990)
   PUBMED   2165071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J05510.1, BF402715.1,
            GQ233032.1 and BC091346.1.
            
            Summary: This gene belongs to the Insp3 receptor family. It encodes
            an intracellular receptor for inositol 1,4,5-trisphosphate. Upon
            stimulation by inositol 1,4,5-trisphosphate, this receptor mediates
            calcium release from the endoplasmic reticulum. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. The resulting isoform (2)
            lacks an internal segment, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2733
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q41"
     Protein         1..2733
                     /product="inositol 1,4,5-trisphosphate-gated calcium
                     channel ITPR1 isoform 2"
                     /note="IP-3-R; type 1 InsP3 receptor; IP3 receptor; type 1
                     inositol 1,4,5-trisphosphate receptor; IP3R 1; inositol
                     1,4,5-triphosphate receptor, type 1; inositol
                     1,4,5-triphosphate receptor 1; inositol
                     1,4,5-trisphosphate-gated calcium channel ITPR1"
                     /calculated_mol_wt=311112
     Region          5..229
                     /region_name="Ins145_P3_rec"
                     /note="Inositol 1,4,5-trisphosphate/ryanodine receptor;
                     pfam08709"
                     /db_xref="CDD:462572"
     Region          224..430
                     /region_name="beta-trefoil_MIR_ITPR1"
                     /note="MIR domain, beta-trefoil fold, found in inositol
                     1,4,5-trisphosphate receptor type 1 (ITPR1) and similar
                     proteins; cd23287"
                     /db_xref="CDD:467758"
     Site            order(245..246,300,359,361,372,378,410..411)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467758"
     Site            order(265,267..269,275)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:467758"
     Region          461..655
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          990..1011
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1121..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1178..1297
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Site            1573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1735..1773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:12939273,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P29994.2)"
     Region          1865..1890
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1916..1936
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          1946..2053
                     /region_name="RIH_assoc"
                     /note="RyR and IP3R Homology associated; pfam08454"
                     /db_xref="CDD:462482"
     Site            2258..2278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2290..2310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2334..2584
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            2337..2357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2381..2401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2424..2444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2447..2512
                     /region_name="Interaction with ERP44.
                     /evidence=ECO:0000250|UniProtKB:P11881"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Site            2553..2573
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     Region          2706..2733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29994.2)"
     CDS             1..2733
                     /gene="Itpr1"
                     /gene_synonym="I145TR; InsP3R; InsP3R1; IP3R1; P400"
                     /coded_by="NM_001270596.1:239..8440"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25262"
                     /db_xref="RGD:2933"
ORIGIN      
        1 msdkmssflh igdicslyae gstngfistl glvddrcvvq peagdlnnpp kkfrdclfkl
       61 cpmnrysaqk qfwkaakpga nsttdavlln klhhaadlek kqnetenrkl lgtviqygnv
      121 iqllhlksnk yltvnkrlpa lleknamrvt ldeagnegsw fyiqpfyklr sigdsvvigd
      181 kvvlnpvnag qplhasshql vdnpgcnevn svncntswki vlfmkwsdnk ddilkggdvv
      241 rlfhaeqekf ltcdehrkkq hvflrttgrq satsatsska lwevevvqhd pcrggagywn
      301 slfrfkhlat ghylaaevdp dqdasrsrlr naqekmvysl vsvpegndis sifeldpttl
      361 rggdslvprn syvrlrhlct ntwvhstnip idkeeekpvm lkigtsplke dkeafaivpv
      421 spaevrdldf andaskvlgs iagklekgti tqnerrsvtk lledlvyfvt ggtnsgqdvl
      481 evvfskpnre rqklmreqni lkqifkllqa pftdcgdgpm lrleelgdqr hapfrhicrl
      541 cyrvlrhsqq dyrknqeyia kqfgfmqkqi gydvlaedti tallhnnrkl lekhitaaei
      601 dtfvslvrkn reprfldyls dlcvsmnksi pvtqelicka vlnptnadil ietklvlsrf
      661 efegvstgen aleagedeee vwlfwrdsnk eirsksvrel aqdakegqke drdvlsyyry
      721 qlnlfarmcl drqylainei sgqldvdlil rcmsdenlpy dlrasfcrlm lhmhvdrdpq
      781 eqvtpvkyar lwseipseia iddydssgas kdeikerfaq tmefveeylr dvvcqrfpfs
      841 dkeknkltfe vvnlarnliy fgfynfsdll rltkillail dcvhvttifp iskmtkgeen
      901 kgsnvmrsih gvgelmtqvv lrgggflpmt pmaaapegnv kqaepekedi mvmdtklkii
      961 eilqfilnvr ldyriscllc ifkrefdesn sqssetssgn ssqegpsnvp galdfehiee
     1021 qaegifggse entpldlddh ggrtflrvll hltmhdyppl vsgalqllfr hfsqrqevlq
     1081 afkqvqllvt sqdvdnykqi kqdldqlrsi vekselwvyk gqgpdepmdg asgenehkkt
     1141 eegtskplkh estssynyrv vkeilirlsk lcvqesasvr ksrkqqqrll rnmgahavvl
     1201 ellqipyeka edtkmqeimr laheflqnfc agnqqnqall hkhinlflnp gileavtmqh
     1261 ifmnnfqlcs einervvqhf vhciethgrn vqyikflqti vkaegkfikk cqdmvmaelv
     1321 nsgedvlvfy ndrasfqtli qmmrserdrm densplmyhi hlvellavct egknvyteik
     1381 cnsllplddi vrvvthedci pevkiayinf lnhcyvdtev emkeiytsnh mwklfenflv
     1441 dicracnnts drkhadsvle kyvteivmsi vttffsspfs dqsttlqtrq pvfvqllqgv
     1501 frvyhcnwlm psqkasvesc irvlsdvaks raiaipvdld sqvnnlflks hnivqktamn
     1561 wrlsarnaar rdsvlaasrd yrniierlqd ivsaledrlr plvqaelsvl vdvlhrpell
     1621 fpentdarrk cesggfickl ikhtkqllee neeklcikvl qtlremmtkd rgygekqisi
     1681 delenaelpq ppeaenstee lepspplrql edhkrgealr qilvnryygn irpsgrresl
     1741 tsfgngplsp ggpskpgggg ggpgsgstsr gemslaevqc hldkegasnl vidlimnass
     1801 drvfhesill aialleggnt tiqhsffcrl tedkksekff kvfydrmkva qqeikatvtv
     1861 ntsdlgnkkk ddevdrdaps rkkakepttq iteevrdqll easaatrkaf ttfrreadpd
     1921 dhyqsgegtq attdkakddl emsavitimq pilrflqllc enhnrdlqnf lrcqnnktny
     1981 nlvcetlqfl dcicgsttgg lgllglyine knvalinqtl eslteycqgp chenqnciat
     2041 hesngidiit alilndinpl gkkrmdlvle lknnasklll aimesrhdse naerilynmr
     2101 pkelvevikk aymqgevefe dgengedgaa sprnvghniy ilahqlarhn kelqtmlkpg
     2161 gqvdgdeale fyakhtaqie ivrldrtmeq ivfpvpsice fltkesklri yytterdeqg
     2221 skindfflrs edlfnemnwq kklraqpvly wcarnmsfws sisfnlavlm nllvaffypf
     2281 kgvrggtlep hwsgllwtam lislaivial pkphgirali astilrlifs vglqptlfll
     2341 gafnvcnkii flmsfvgncg tftrgyramv ldveflyhll yllicamglf vheffyslll
     2401 fdlvyreetl lnviksvtrn grsiiltavl alilvylfsi vgylffkddf ilevdrlpne
     2461 tagpetgesl andflysdvc rvetgencts papkeellpv eeteqdkeht cetllmcivt
     2521 vlshglrsgg gvgdvlrkps keeplfaarv iydllfffmv iiivlnlifg viidtfadlr
     2581 sekqkkeeil kttcficgle rdkfdnktvt feehikeehn mwhylcfivl vkvkdsteyt
     2641 gpesyvaemi rernldwfpr mramslvssd segeqnelrn lqeklestmk lvtnlsgqls
     2701 elkdqmteqr kqkqrigllg hpphmnvnpq qpa
//
LOCUS       NP_113927                611 aa            linear   ROD 27-APR-2025
DEFINITION  A-type voltage-gated potassium channel KCND3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_113927 XP_001081919
VERSION     NP_113927.2
DBSOURCE    REFSEQ: accession NM_031739.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Kanda,H., Ling,J., Chang,Y.T., Erol,F., Viatchenko-Karpinski,V.,
            Yamada,A., Noguchi,K. and Gu,J.G.
  TITLE     Kv4.3 Channel Dysfunction Contributes to Trigeminal Neuropathic
            Pain Manifested with Orofacial Cold Hypersensitivity in Rats
  JOURNAL   J Neurosci 41 (10), 2091-2105 (2021)
   PUBMED   33472822
  REMARK    GeneRIF: Kv4.3 Channel Dysfunction Contributes to Trigeminal
            Neuropathic Pain Manifested with Orofacial Cold Hypersensitivity in
            Rats.
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Tao,B., Liu,Z., Wei,F., Fan,S., Cui,S., Xia,H. and Xu,L.
  TITLE     Over-expression of Kv4.3 gene reverses cardiac remodeling and
            transient-outward K+ current (Ito) reduction via CaMKII inhibition
            in myocardial infarction
  JOURNAL   Biomed Pharmacother 132, 110896 (2020)
   PUBMED   33254430
  REMARK    GeneRIF: Over-expression of Kv4.3 gene reverses cardiac remodeling
            and transient-outward K(+) current (Ito) reduction via CaMKII
            inhibition in myocardial infarction.
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Alday,A., Ahyayauch,H., Fernandez-Lopez,V., Echeazarra,L.,
            Urrutia,J., Casis,O. and Gallego,M.
  TITLE     CaMKII Modulates the Cardiac Transient Outward K+ Current through
            its Association with Kv4 Channels in Non-Caveolar Membrane Rafts
  JOURNAL   Cell Physiol Biochem 54 (1), 27-39 (2020)
   PUBMED   31935048
  REMARK    GeneRIF: Immunogold staining and electron microscopy of heart
            vibrosections was performed to localize Kv4.2/Kv4.3 and
            Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) proteins.
            Patch-Clamp recordings in control conditions and after lipid raft
            or caveolae disruption show that the CaMKII-Kv4 channel complex
            must associate in non-caveolar lipid rafts to be functional.
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Wang,Y., Keskanokwong,T. and Cheng,J.
  TITLE     Kv4.3 expression abrogates and reverses norepinephrine-induced
            myocyte hypertrophy by CaMKII inhibition
  JOURNAL   J Mol Cell Cardiol 126, 77-85 (2019)
   PUBMED   30462989
  REMARK    GeneRIF: Kv4.3 reduction is an important mediator in cardiac
            hypertrophy development via excessive CaMKII activation.
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Viatchenko-Karpinski,V., Ling,J. and Gu,J.G.
  TITLE     Down-regulation of Kv4.3 channels and a-type K+ currents in V2
            trigeminal ganglion neurons of rats following oxaliplatin treatment
  JOURNAL   Mol Pain 14, 1744806917750995 (2018)
   PUBMED   29313436
  REMARK    GeneRIF: down-regulation of Kv4.3 channels mediating A-type K(+)
            (IA) currents currents in nociceptive V2 trigeminal neurons is an
            underlying mechanism of oxaliplatin-induced orofacial neuropathic
            pain.
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Ohya,S., Tanaka,M., Oku,T., Asai,Y., Watanabe,M., Giles,W.R. and
            Imaizumi,Y.
  TITLE     Molecular cloning and tissue distribution of an alternatively
            spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the
            rat
  JOURNAL   FEBS Lett 420 (1), 47-53 (1997)
   PUBMED   9450548
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Takimoto,K., Li,D., Hershman,K.M., Li,P., Jackson,E.K. and
            Levitan,E.S.
  TITLE     Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit
            mRNAs in ventricles of renovascular hypertensive rats
  JOURNAL   Circ Res 81 (4), 533-539 (1997)
   PUBMED   9314834
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Tsaur,M.L., Chou,C.C., Shih,Y.H. and Wang,H.L.
  TITLE     Cloning, expression and CNS distribution of Kv4.3, an A-type K+
            channel alpha subunit
  JOURNAL   FEBS Lett 400 (2), 215-220 (1997)
   PUBMED   9001401
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Dixon,J.E., Shi,W., Wang,H.S., McDonald,C., Yu,H., Wymore,R.S.,
            Cohen,I.S. and McKinnon,D.
  TITLE     Role of the Kv4.3 K+ channel in ventricular muscle. A molecular
            correlate for the transient outward current
  JOURNAL   Circ Res 79 (4), 659-668 (1996)
   PUBMED   8831489
  REMARK    Erratum:[Circ Res 1997 Jan;80(1):147]
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Serodio,P., Vega-Saenz de Miera,E. and Rudy,B.
  TITLE     Cloning of a novel component of A-type K+ channels operating at
            subthreshold potentials with unique expression in heart and brain
  JOURNAL   J Neurophysiol 75 (5), 2174-2179 (1996)
   PUBMED   8734615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Apr 5, 2007 this sequence version replaced NP_113927.1.
            
            Transcript Variant: This variant (3, also known as Kv4.3S and
            Kv4.3b) lacks an in-frame exon in the 3' coding region, and lacks a
            segment in the 3' coding region, which results in a frameshift
            compared to variant 1. The encoded isoform (3) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript was derived from the reference
            genome assembly. The genomic coordinates were determined from
            transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L48619.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..611
                     /product="A-type voltage-gated potassium channel KCND3
                     isoform 3"
                     /note="potassium voltage gated channel, Shal-related
                     family, member 3; voltage-gated potassium channel subunit
                     Kv4.3; potassium channel, voltage-gated Shal-related
                     subfamily D, member 3; potassium voltage-gated channel,
                     Shal-related subfamily, member 3; A-type voltage-gated
                     potassium channel KCND3"
                     /calculated_mol_wt=69163
     Region          6..143
                     /region_name="BTB_POZ_KCND3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily D member 3 (KCND3);
                     cd18419"
                     /db_xref="CDD:349726"
     Site            order(7..19,21..22,26..27,29,31,34,36..37,39,54)
                     /site_type="other"
                     /note="beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Site            order(41,45,47..54,57,83,85..87,89,92,96,99..100,102,104,
                     107..110,112..113,116,131..132)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349726"
     Region          186..412
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          468..544
                     /region_name="DUF3399"
                     /note="Domain of unknown function (DUF3399); pfam11879"
                     /db_xref="CDD:463381"
     CDS             1..611
                     /gene="Kcnd3"
                     /gene_synonym="Kv4.3"
                     /coded_by="NM_031739.3:93..1928"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:65195"
                     /db_xref="RGD:68394"
ORIGIN      
        1 maagvaawlp faraaaigwm pvancpmpla padknkrqde livlnvsgrr fqtwrttler
       61 ypdtllgste kefffnedtk eyffdrdpev frcvlnfyrt gklhypryec isayddelaf
      121 ygilpeiigd ccyeeykdrk renaerlmdd nesennqesm pslsfrqtmw rafenphtst
      181 lalvfyyvtg ffiavsvitn vvetvpcgtv pgskelpcge rysvaffcld tacvmiftve
      241 yllrlfaaps ryrfirsvms iidvvaimpy yiglvmtnne dvsgafvtlr vfrvfrifkf
      301 srhsqglril gytlkscase lgfllfsltm aiiifatvmf yaekgssask ftsipasfwy
      361 tivtmttlgy gdmvpktiag kifgsicsls gvlvialpvp vivsnfsriy hqnqradkrr
      421 aqkkarlari rvaktgssna ylhskrngll nealeltgtp eeehmgktts liesqhhhll
      481 hclekttnhe fideqmfeqn cmessmqnyp strspslssh sgltttccsr rskktthlpn
      541 snlpatrlrs mqelstihiq gseqpsltts rsslnlkadd glrpncktqd qeqprgrvvt
      601 ckqeeiitlc i
//
LOCUS       NP_001074376             485 aa            linear   ROD 27-APR-2025
DEFINITION  zinc finger protein 639 [Rattus norvegicus].
ACCESSION   NP_001074376 XP_001066236
VERSION     NP_001074376.1
DBSOURCE    REFSEQ: accession NM_001080907.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Bruce,J.W., Hierl,M., Young,J.A. and Ahlquist,P.
  TITLE     Cellular transcription factor ZASC1 regulates murine leukemia virus
            transcription
  JOURNAL   J Virol 84 (15), 7473-7483 (2010)
   PUBMED   20484494
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Bogaerts,S., Vanlandschoot,A., van Hengel,J. and van Roy,F.
  TITLE     Nuclear translocation of alphaN-catenin by the novel zinc finger
            transcriptional repressor ZASC1
  JOURNAL   Exp Cell Res 311 (1), 1-13 (2005)
   PUBMED   16182284
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Imoto,I., Yuki,Y., Sonoda,I., Ito,T., Shimada,Y., Imamura,M. and
            Inazawa,J.
  TITLE     Identification of ZASC1 encoding a Kruppel-like zinc finger protein
            as a novel target for 3q26 amplification in esophageal squamous
            cell carcinomas
  JOURNAL   Cancer Res 63 (18), 5691-5696 (2003)
   PUBMED   14522885
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087704.1.
            
            On Jan 30, 2007 this sequence version replaced XP_001066236.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087704.1, FQ149402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..485
                     /product="zinc finger protein 639"
                     /calculated_mol_wt=55401
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPG4.1)"
     Region          54..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPG4.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG4.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UID6; propagated from
                     UniProtKB/Swiss-Prot (Q5PPG4.1)"
     Region          235..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(240,242,244,246..247,250..251,254,268,272,273..274,
                     277..278,282,296,298,300,302..303,306..307)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          262..283
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          291..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..455
                     /region_name="Interaction with CTNNA2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPG4.1)"
     Region          376..397
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          405..425
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(410,412,414,416..417,420..421,424,438,440,444..445,
                     448..449,453,467,469,471,473..474,477..478,481)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          433..454
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          462..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..485
                     /gene="Zfp639"
                     /gene_synonym="Znf639"
                     /coded_by="NM_001080907.2:288..1745"
                     /db_xref="GeneID:683504"
                     /db_xref="RGD:1585689"
ORIGIN      
        1 mseypkkrkr ktlhpsrysd ssgisriadg vsgifsdhcy svcsmrqpdl kyfdnkddds
       61 dpetandlpk ftdgtkarsr sqsclvpspv lrilehtvfs tekpadveic deecgspesg
      121 hqhtheespi evhtsedvpi avevhaised ydieaennss eslldqtdee ppaklckild
      181 ksqasnvtaq qkwpllrans sglykcelce fnskyfsdlk qhvilkhkrt dsnvcrvcke
      241 sfstnmllie haklheedpy ickycdyktv ifenlsqhia dthfsdhlyw ceqcdvqfss
      301 sselylhfqe hsrdeqylcq fcehetgdpe dlhshvvneh arrlielsdk cgsgghgqcs
      361 llskitfdkc knffvcqvcg frsrlhtnvn rhvaiehtki fphvcddcgk gfssmleyck
      421 hlnshlsegi ylcqyceyst gqiedlkihl dfkhsadlph kcsdclmrfg nerelishlp
      481 vhett
//
LOCUS       NP_037309                430 aa            linear   ROD 27-APR-2025
DEFINITION  aspartate aminotransferase, mitochondrial [Rattus norvegicus].
ACCESSION   NP_037309
VERSION     NP_037309.1
DBSOURCE    REFSEQ: accession NM_013177.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Liu,X., Li,X. and Zhou,H.
  TITLE     Changes in glutamic oxaloacetic transaminase 2 during rat
            physiological and pathological cardiomyocyte hypertrophy
  JOURNAL   BMC Cardiovasc Disord 23 (1), 595 (2023)
   PUBMED   38053021
  REMARK    GeneRIF: Changes in glutamic oxaloacetic transaminase 2 during rat
            physiological and pathological cardiomyocyte hypertrophy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Xu,J., Khoury,N., Jackson,C.W., Escobar,I., Stegelmann,S.D.,
            Dave,K.R. and Perez-Pinzon,M.A.
  TITLE     Ischemic Neuroprotectant PKCepsilon Restores Mitochondrial
            Glutamate Oxaloacetate Transaminase in the Neuronal NADH Shuttle
            after Ischemic Injury
  JOURNAL   Transl Stroke Res 11 (3), 418-432 (2020)
   PUBMED   31473978
  REMARK    GeneRIF: Ischemic Neuroprotectant PKCepsilon Restores Mitochondrial
            Glutamate Oxaloacetate Transaminase in the Neuronal NADH Shuttle
            after Ischemic Injury.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Zhang,Y., Kallenberg,C., Hyatt,H.W., Kavazis,A.N. and Hood,W.R.
  TITLE     Change in the Lipid Transport Capacity of the Liver and Blood
            during Reproduction in Rats
  JOURNAL   Front Physiol 8, 517 (2017)
   PUBMED   28798692
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Yang,L., Shen,Z.Y., Wang,R.R., Yin,M.L., Zheng,W.P., Wu,B., Liu,T.
            and Song,H.L.
  TITLE     Effects of heme oxygenase-1-modified bone marrow mesenchymal stem
            cells on microcirculation and energy metabolism following liver
            transplantation
  JOURNAL   World J Gastroenterol 23 (19), 3449-3467 (2017)
   PUBMED   28596681
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Rodriguez-Cruz,M., Gonzalez,R.S., Maldonado,J., Lopez-Alarcon,M.
            and Bernabe-Garcia,M.
  TITLE     The effect of gestational age on expression of genes involved in
            uptake, trafficking and synthesis of fatty acids in the rat
            placenta
  JOURNAL   Gene 591 (2), 403-410 (2016)
   PUBMED   27317891
REFERENCE   6  (residues 1 to 430)
  AUTHORS   von Deimling,O.H., Groning,J. and Gaa,A.
  TITLE     Genetic and biochemical characterization of a new chymotrypsin
            isozyme of the house mouse, CTRA-1
  JOURNAL   Biochem Genet 29 (11-12), 545-557 (1991)
   PUBMED   1820020
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Watazu,Y., Uji,Y., Sugiuchi,H., Okabe,H. and Murao,S.
  TITLE     New automated measurement of mitochondrial aspartate
            aminotransferase with use of protease 401
  JOURNAL   Clin Chem 36 (4), 687-689 (1990)
   PUBMED   2182221
REFERENCE   8  (residues 1 to 430)
  AUTHORS   White,R.A., Birkenmeier,C.S., Lux,S.E. and Barker,J.E.
  TITLE     Ankyrin and the hemolytic anemia mutation, nb, map to mouse
            chromosome 8: presence of the nb allele is associated with a
            truncated erythrocyte ankyrin
  JOURNAL   Proc Natl Acad Sci U S A 87 (8), 3117-3121 (1990)
   PUBMED   2139228
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Peters,J. and Nash,H.R.
  TITLE     Polymorphism of esterase 11 in Mus musculus, a further esterase
            locus on chromosome 8
  JOURNAL   Biochem Genet 15 (3-4), 217-226 (1977)
   PUBMED   869894
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Nichols,E.A. and Ruddle,F.H.
  TITLE     Polymorphism and linkage of glutathione reductase in Mus musculus
  JOURNAL   Biochem Genet 13 (5-6), 323-329 (1975)
   PUBMED   1180875
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM056810.1, BC061792.1 and CB607680.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M18467.1, BC061792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..430
                     /product="aspartate aminotransferase, mitochondrial"
                     /EC_number="2.6.1.1"
                     /EC_number="2.6.1.7"
                     /note="FABP-1; FABPpm; mAspAT; transaminase A; fatty
                     acid-binding protein; plasma membrane-associated fatty
                     acid-binding protein; Glutamate oxaloacetate transaminase
                     2, mitochondrial (aspartate aminotransferase 2);
                     glutamic-oxaloacetic transaminase 2, mitochondrial
                     (aspartate aminotransferase 2); kynurenine
                     aminotransferase 4; kynurenine aminotransferase IV;
                     kynurenine--oxoglutarate transaminase 4;
                     kynurenine--oxoglutarate transaminase IV"
                     /calculated_mol_wt=44526
     transit_peptide 1..29
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:17442055,
                     ECO:0000269|PubMed:7309704, ECO:0000269|PubMed:7470110,
                     ECO:0000269|PubMed:8238519; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
                     /calculated_mol_wt=2806
     mat_peptide     30..430
                     /product="Aspartate aminotransferase, mitochondrial.
                     /id=PRO_0000001218"
                     /note="propagated from UniProtKB/Swiss-Prot (P00507.2)"
                     /calculated_mol_wt=44526
     Region          32..430
                     /region_name="PLN02397"
                     /note="aspartate transaminase"
                     /db_xref="CDD:215222"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            73
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            107
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            122
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            order(133..135,162,215,246,276,278..279,287)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(136,172,239,285..287,323,326)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            159
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            234
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            279
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            313
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            338
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            345
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            387
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P05202; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            396
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     Site            404
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00505; propagated from
                     UniProtKB/Swiss-Prot (P00507.2)"
     CDS             1..430
                     /gene="Got2"
                     /gene_synonym="ASPATA; mAAT"
                     /coded_by="NM_013177.2:119..1411"
                     /db_xref="GeneID:25721"
                     /db_xref="RGD:2722"
ORIGIN      
        1 mallhsgrvl sgmaaafhpg laaaasaras swwthvemgp pdpilgvtea fkrdtnskkm
       61 nlgvgayrdd ngkpyvlpsv rkaeaqiagk nldkeylpig gladfckasa elalgensev
      121 lksgrfvtvq tisgtgalrv gasflqrffk fsrdvflpkp swgnhtpifr dagmqlqgyr
      181 yydpktcgfd fsgaledisk ipeqsvlllh acahnptgvd prpeqwkema avvkkknlfa
      241 ffdmayqgfa sgdgdkdawa vrhfieqgin vclcqsyakn mglygervga ftvvckdaee
      301 akrvesqlki lirplysnpp lngariaati ltspdlrkqw lqevkgmadr iismrtqlvs
      361 nlkkegsshn wqhitdqigm fcftglkpeq verltkefsv ymtkdgrisv agvtsgnvgy
      421 lahaihqvtk
//
LOCUS       NP_001264002             315 aa            linear   ROD 27-APR-2025
DEFINITION  heme oxygenase 2 [Rattus norvegicus].
ACCESSION   NP_001264002
VERSION     NP_001264002.1
DBSOURCE    REFSEQ: accession NM_001277073.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Martinez-Gascon,L.E., Ortiz,M.C., Galindo,M., Sanchez,J.M.,
            Sancho-Rodriguez,N., Albaladejo-Oton,M.D., Rodriguez Mulero,M.D.
            and Rodriguez,F.
  TITLE     Role of heme oxygenase in the regulation of the renal hemodynamics
            in a model of sex-dependent programmed hypertension by maternal
            diabetes
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 322 (3), R181-R191 (2022)
   PUBMED   34984919
  REMARK    GeneRIF: Role of heme oxygenase in the regulation of the renal
            hemodynamics in a model of sex-dependent programmed hypertension by
            maternal diabetes.
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Takemoto,M., Sakamoto,H., Higashimoto,Y. and Taira,J.
  TITLE     Complex Formation of Heme Oxygenase-2 with Heme Is Competitively
            Inhibited by the Cytosolic Domain of Caveolin-1
  JOURNAL   Biochemistry 60 (29), 2300-2308 (2021)
   PUBMED   34223768
  REMARK    GeneRIF: Complex Formation of Heme Oxygenase-2 with Heme Is
            Competitively Inhibited by the Cytosolic Domain of Caveolin-1.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Kilic-Toprak,E., Kilic-Erkek,O., Abban-Mete,G., Caner,V.,
            Baris,I.C., Turhan,G., Kucukatay,V., Senol,H., Kuru,O. and
            Bor-Kucukatay,M.
  TITLE     Contribution of Heme Oxygenase 2 to Blood Pressure Regulation in
            Response to Swimming Exercise and Detraining in Spontaneously
            Hypertensive Rats
  JOURNAL   Med Sci Monit 24, 5851-5859 (2018)
   PUBMED   30132448
  REMARK    GeneRIF: Aorta HO-2 histological scores (HSCORE) of hypertensive
            rats were lower, while SBP was higher. Swimming caused enhancement
            of HO-2 immunostaining in aorta endothelium and adventitia of SHR.
            Exercise induced elevation of blood COHb index in SHR. Synchronous
            BP lowering effect of exercise was observed.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Robison,C.L., McHenry,J.A. and Hull,E.M.
  TITLE     Increased expression of carbon monoxide-producing enzymes in the
            MPOA after sexual experience in male rats
  JOURNAL   Physiol Behav 171, 149-157 (2017)
   PUBMED   28088559
  REMARK    GeneRIF: This experiments shown here indicate that HO-2 and HO-1
            are differentially regulated across sexual experience and that the
            two CO-producing enzymes are expressed in distinct but overlapping
            populations of cells in medial preoptic area.
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Posa,A., Kupai,K., Menesi,R., Szalai,Z., Szabo,R., Pinter,Z.,
            Palfi,G., Gyongyosi,M., Berko,A., Pavo,I. and Varga,C.
  TITLE     Sexual dimorphism of cardiovascular ischemia susceptibility is
            mediated by heme oxygenase
  JOURNAL   Oxid Med Cell Longev 2013, 521563 (2013)
   PUBMED   24163720
  REMARK    GeneRIF: The increased HO activity and expression in females might
            play a role in the sexual dimorphism of cardiovascular ischemia
            susceptibility during the reproductive age.
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Remmers,E.F., Griffiths,M.M., Longman,R.E., Gulko,P.S.,
            Kawahito,Y., Chen,S., Chang,L., Shepard,J., Ge,L., Dracheva,S.,
            Wang,J.P., Joe,B., Cannon,G.W. and Wilder,R.L.
  TITLE     An integrated rat genetic map: analysis of linkage conservation
            with the mouse and human maps
  JOURNAL   Transplant Proc 31 (3), 1549-1554 (1999)
   PUBMED   10330996
REFERENCE   7  (residues 1 to 315)
  AUTHORS   McCoubrey,W.K. Jr. and Maines,M.D.
  TITLE     The structure, organization and differential expression of the gene
            encoding rat heme oxygenase-2
  JOURNAL   Gene 139 (2), 155-161 (1994)
   PUBMED   8112599
REFERENCE   8  (residues 1 to 315)
  AUTHORS   McCoubrey,W.K. Jr., Ewing,J.F. and Maines,M.D.
  TITLE     Human heme oxygenase-2: characterization and expression of a
            full-length cDNA and evidence suggesting that the two HO-2
            transcripts may differ by choice of polyadenylation signal
  JOURNAL   Arch Biochem Biophys 295 (1), 13-20 (1992)
   PUBMED   1575508
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Rotenberg,M.O. and Maines,M.D.
  TITLE     Isolation, characterization, and expression in Escherichia coli of
            a cDNA encoding rat heme oxygenase-2
  JOURNAL   J Biol Chem 265 (13), 7501-7506 (1990)
   PUBMED   2185251
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Cruse,I. and Maines,M.D.
  TITLE     Evidence suggesting that the two forms of heme oxygenase are
            products of different genes
  JOURNAL   J Biol Chem 263 (7), 3348-3353 (1988)
   PUBMED   3343248
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1, FM134576.1, FM139649.1, FM110439.1 and
            BF283242.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062061.1, FQ225862.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..315
                     /product="heme oxygenase 2"
                     /EC_number="1.14.14.18"
                     /note="heme oxygenase (decycling) 2"
                     /calculated_mol_wt=35631
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P30519; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P30519; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Region          30..235
                     /region_name="Heme_oxygenase"
                     /note="Heme oxygenase; pfam01126"
                     /db_xref="CDD:395895"
     Site            order(37,44,47..48,53,57,153..155,161..162,166,198,202,
                     226,229,233)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:350856"
     Region          146..173
                     /region_name="kinked helix"
                     /note="kinked helix [structural motif]"
                     /db_xref="CDD:350856"
     Site            159
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P09601; propagated from
                     UniProtKB/Swiss-Prot (P23711.1)"
     Region          263..268
                     /region_name="HRM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Region          280..285
                     /region_name="HRM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     Site            295..315
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23711.1)"
     CDS             1..315
                     /gene="Hmox2"
                     /gene_synonym="Ho-2"
                     /coded_by="NM_001277073.1:144..1091"
                     /db_xref="GeneID:79239"
                     /db_xref="RGD:67402"
ORIGIN      
        1 mssevetseg vdesennsta pekenhtkma dlsellkegt keahdraent qfvkdflkgn
       61 ikkelfklat talyftysal eeemdrnkdh pafaplyfpt elhrkealik dmeyffgenw
      121 eeqvkcseaa qkyvdrihyv gqnepellva haytrymgdl sggqvlkkva qralklpstg
      181 egtqfylfeh vdnaqqfkqf yrarmnaldl smktkerive eankafeynm qifseldqag
      241 smltketled glpvhdgkgd vrkcpfyaaq pdkgtlggsn cpfrtamavl rkpslqlila
      301 asvalvagll awyym
//
LOCUS       NP_620228                750 aa            linear   ROD 27-APR-2025
DEFINITION  nibrin [Rattus norvegicus].
ACCESSION   NP_620228
VERSION     NP_620228.1
DBSOURCE    REFSEQ: accession NM_138873.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Gao,L., Lv,Q., Huang,Y., Fan,Y., Zhao,L., Zhao,Y., Wang,X., Mo,D.,
            Lu,H. and Wang,D.
  TITLE     Effect of silencing SSB1 gene on the expression of NBS1 in
            irradiated rat submandibular gland cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (1), 110-118 (2024)
   PUBMED   38372104
  REMARK    GeneRIF: Effect of silencing SSB1 gene on the expression of NBS1 in
            irradiated rat submandibular gland cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Rivera,T., Haggblom,C., Cosconati,S. and Karlseder,J.
  TITLE     A balance between elongation and trimming regulates telomere
            stability in stem cells
  JOURNAL   Nat Struct Mol Biol 24 (1), 30-39 (2017)
   PUBMED   27918544
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Naccarati,A., Rosa,F., Vymetalkova,V., Barone,E., Jiraskova,K., Di
            Gaetano,C., Novotny,J., Levy,M., Vodickova,L., Gemignani,F.,
            Buchler,T., Landi,S., Vodicka,P. and Pardini,B.
  TITLE     Double-strand break repair and colorectal cancer: gene variants
            within 3' UTRs and microRNAs binding as modulators of cancer risk
            and clinical outcome
  JOURNAL   Oncotarget 7 (17), 23156-23169 (2016)
   PUBMED   26735576
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Chang,F.T., McGhie,J.D., Chan,F.L., Tang,M.C., Anderson,M.A.,
            Mann,J.R., Andy Choo,K.H. and Wong,L.H.
  TITLE     PML bodies provide an important platform for the maintenance of
            telomeric chromatin integrity in embryonic stem cells
  JOURNAL   Nucleic Acids Res 41 (8), 4447-4458 (2013)
   PUBMED   23444137
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Lovric,J., Mano,M., Zentilin,L., Eulalio,A., Zacchigna,S. and
            Giacca,M.
  TITLE     Terminal differentiation of cardiac and skeletal myocytes induces
            permissivity to AAV transduction by relieving inhibition imposed by
            DNA damage response proteins
  JOURNAL   Mol Ther 20 (11), 2087-2097 (2012)
   PUBMED   22850678
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Zhu,X.D., Kuster,B., Mann,M., Petrini,J.H. and de Lange,T.
  TITLE     Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and
            human telomeres
  JOURNAL   Nat Genet 25 (3), 347-352 (2000)
   PUBMED   10888888
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Lombard,D.B. and Guarente,L.
  TITLE     Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear
            bodies and meiotic telomeres
  JOURNAL   Cancer Res 60 (9), 2331-2334 (2000)
   PUBMED   10811102
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Lim,D.S., Kim,S.T., Xu,B., Maser,R.S., Lin,J., Petrini,J.H. and
            Kastan,M.B.
  TITLE     ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway
  JOURNAL   Nature 404 (6778), 613-617 (2000)
   PUBMED   10766245
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Carney,J.P., Maser,R.S., Olivares,H., Davis,E.M., Le Beau,M.,
            Yates,J.R. 3rd, Hays,L., Morgan,W.F. and Petrini,J.H.
  TITLE     The hMre11/hRad50 protein complex and Nijmegen breakage syndrome:
            linkage of double-strand break repair to the cellular DNA damage
            response
  JOURNAL   Cell 93 (3), 477-486 (1998)
   PUBMED   9590181
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Varon,R., Vissinga,C., Platzer,M., Cerosaletti,K.M.,
            Chrzanowska,K.H., Saar,K., Beckmann,G., Seemanova,E., Cooper,P.R.,
            Nowak,N.J., Stumm,M., Weemaes,C.M., Gatti,R.A., Wilson,R.K.,
            Digweed,M., Rosenthal,A., Sperling,K., Concannon,P. and Reis,A.
  TITLE     Nibrin, a novel DNA double-strand break repair protein, is mutated
            in Nijmegen breakage syndrome
  JOURNAL   Cell 93 (3), 467-476 (1998)
   PUBMED   9590180
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF218575.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF218575.1, BC085700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132274, SAMD00132279
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..750
                     /product="nibrin"
                     /function="required for MRE11, RAD50 and NBS1
                     colocalization at nuclear foci in response to DNA
                     double-strand breaks"
                     /note="nijmegen breakage syndrome protein 1 homolog"
                     /calculated_mol_wt=83173
     Region          2..110
                     /region_name="FHA_NBN"
                     /note="forkhead associated (FHA) domain found in nibrin
                     and similar proteins; cd22667"
                     /db_xref="CDD:438719"
     Site            order(28,39..43,73..74,101)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438719"
     Region          111..328
                     /region_name="Mediates interaction with SP100.
                     /evidence=ECO:0000250|UniProtKB:Q9R207"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          111..184
                     /region_name="BRCT_nibrin"
                     /note="BRCT domain of nibrin and similar proteins;
                     cd17741"
                     /db_xref="CDD:349372"
     Region          217..325
                     /region_name="NIBRIN_BRCT_II"
                     /note="Second BRCT domain on Nijmegen syndrome breakage
                     protein; pfam16508"
                     /db_xref="CDD:465151"
     Region          221..403
                     /region_name="Interaction with MTOR, MAPKAP1 and RICTOR.
                     /evidence=ECO:0000250|UniProtKB:O60934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60934; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000250|UniProtKB:O60934; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60934; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          429..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          461..467
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O60934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          494..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60934; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60934; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          581..622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     Region          680..741
                     /region_name="Nbs1_C"
                     /note="DNA damage repair protein Nbs1; pfam08599"
                     /db_xref="CDD:462531"
     Region          737..746
                     /region_name="FxF/Y motif.
                     /evidence=ECO:0000250|UniProtKB:O60934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL9.2)"
     CDS             1..750
                     /gene="Nbn"
                     /gene_synonym="Nbs1"
                     /coded_by="NM_138873.2:36..2288"
                     /db_xref="GeneID:85482"
                     /db_xref="RGD:621420"
ORIGIN      
        1 mwkllpaasa apgepcrlla gveyivgrkn cailiendqs isrnhavlrv nfpvtslsqt
       61 deiptliikd nskygtfine ekmqnglsst lktgdrvtfg vfeskfrvey eplvvcsscl
      121 dvsgktvlnq ailqlgglta nswteecthl amssvkvtik ticalicgrp ivkpeyfsef
      181 lkavesktqp peiesfyppi depaignksv dlsgrrerkq ifkgktfvfl nakqhkklgs
      241 avvfgggear lmaeggeeeq sffsapgtcv vdvgitntql iitdsqrkwi hlimdilqrh
      301 dlrpipeaei glavifmtte sycnpqgqpc tevktttpgp slsqglsang kvipsapmnm
      361 ttyvadtese padtcmslse rpeevkifgl dqnsrkllqg tcniketsnq ssnsnnaasn
      421 tlvrgkapny qlspmkcpaa sknkdwssqq qlnsiknyfq pcsrkrerde enpeqsscks
      481 srvelscsll eqtqpaepsl wkskdhesqs etlgrasnas svggidikpn gkspdsksfs
      541 tedlrarkrk evdlsteeev leellrstkp elavqvkvek qeadvsirkk prmdaernqh
      601 lnggpvpesn salqedetek kdelqieaws tkrevsntde lqdsseelpr kllltefrsl
      661 vvhnnssrnl cplngrgelk nfkkfkkatc pgagklphii ggsdlighha rknteleewl
      721 khemevqkqq akedsladdl frynpnvkrr
//
LOCUS       NP_579834                428 aa            linear   ROD 27-APR-2025
DEFINITION  spliceosome RNA helicase Ddx39b [Rattus norvegicus].
ACCESSION   NP_579834 XP_346596 XP_347363
VERSION     NP_579834.2
DBSOURCE    REFSEQ: accession NM_133300.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ishizuka,A., Hasegawa,Y., Ishida,K., Yanaka,K. and Nakagawa,S.
  TITLE     Formation of nuclear bodies by the lncRNA Gomafu-associating
            proteins Celf3 and SF1
  JOURNAL   Genes Cells 19 (9), 704-721 (2014)
   PUBMED   25145264
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Chang,T.H., Tung,L., Yeh,F.L., Chen,J.H. and Chang,S.L.
  TITLE     Functions of the DExD/H-box proteins in nuclear pre-mRNA splicing
  JOURNAL   Biochim Biophys Acta 1829 (8), 764-774 (2013)
   PUBMED   23454554
  REMARK    Review article
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Sahni,A., Wang,N. and Alexis,J.
  TITLE     UAP56 is an important mediator of angiotensin II/platelet derived
            growth factor induced vascular smooth muscle cell DNA synthesis and
            proliferation
  JOURNAL   Biochem Biophys Res Commun 431 (3), 636-640 (2013)
   PUBMED   23246467
  REMARK    GeneRIF: These findings suggest that UAP56 is a regulator of VSMC
            proliferation and identify UAP56 as a target for preventing
            vascular proliferative disease.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Lambracht-Washington,D. and Fischer Lindahl,K.
  TITLE     Does the rat have an H2-D orthologue next to Bat1?
  JOURNAL   Immunogenetics 53 (12), 1039-1046 (2002)
   PUBMED   11904681
  REMARK    GeneRIF: To determine whether the rat possesses an H2-D orthologue,
            we sequenced a cosmid clone that contains rat Bat1 and an adjacent
            class I gene, RT1.46 (l).
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Cheong,K.Y., Allcock,R.J., Eerligh,P., Witt,C.S.,
            Christiansen,F.T., McCann,V. and Price,P.
  TITLE     Localization of central MHC genes influencing type I diabetes
  JOURNAL   Hum Immunol 62 (12), 1363-1370 (2001)
   PUBMED   11756005
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Gohshi,T., Shimada,M., Kawahire,S., Imai,N., Ichimura,T., Omata,S.
            and Horigome,T.
  TITLE     Molecular cloning of mouse p47, a second group mammalian RuvB DNA
            helicase-like protein: homology with those from human and
            Saccharomyces cerevisiae
  JOURNAL   J Biochem 125 (5), 939-946 (1999)
   PUBMED   10220587
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Helou,K., Yan,Q., Yuan,X.J., Kunz,H.W., Levan,G. and Gill,T.J. 3rd.
  TITLE     Cytogenetic localization of the growth and reproduction complex
            (Grc) in the rat and in the mouse and its position in relation to
            RT1.EC and other loci in the rat MHC
  JOURNAL   Hereditas 130 (2), 105-109 (1999)
   PUBMED   10479997
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Nair,S., Dey,R., Sanford,J.P. and Doyle,D.
  TITLE     Molecular cloning and analysis of an eIF-4A-related rat liver
            nuclear protein
  JOURNAL   J Biol Chem 267 (18), 12928-12935 (1992)
   PUBMED   1618789
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY309526.1 and BC080243.1.
            
            On Aug 29, 2004 this sequence version replaced NP_579834.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212901.1, BC080243.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN16676807
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..428
                     /product="spliceosome RNA helicase Ddx39b"
                     /EC_number="3.6.4.13"
                     /note="spliceosome RNA helicase Bat1; DEAD box protein
                     UAP56; ATP-dependent RNA helicase p47; 56 kDa
                     U2AF65-associated protein; DEAD-box helicase 39B; Nuclear
                     RNA helicase; D20H6S81e; D17H6S81E-1; HLA-B associated
                     transcript 1; HLA-B-associated transcript 1A; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 39B"
                     /calculated_mol_wt=48904
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63413.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q13838; propagated from
                     UniProtKB/Swiss-Prot (Q63413.3)"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13838; propagated from
                     UniProtKB/Swiss-Prot (Q63413.3)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13838; propagated from
                     UniProtKB/Swiss-Prot (Q63413.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13838; propagated from
                     UniProtKB/Swiss-Prot (Q63413.3)"
     Region          44..251
                     /region_name="DEADc_DDX39"
                     /note="DEAD-box helicase domain of DEAD box protein 39;
                     cd17950"
                     /db_xref="CDD:350708"
     Region          45..73
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63413.3)"
     Site            order(47,65,67..69,72,91..97,196..197)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350708"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13838; propagated from
                     UniProtKB/Swiss-Prot (Q63413.3)"
     Region          196..199
                     /region_name="DECD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63413.3)"
     Region          262..391
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(350,352,377,380..381)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..428
                     /gene="Ddx39b"
                     /gene_synonym="Bat1; Bat1a; p47"
                     /coded_by="NM_133300.3:195..1481"
                     /db_xref="GeneID:114612"
                     /db_xref="RGD:70923"
ORIGIN      
        1 maendvdnel ldyeddevet aagadgteap akkdvkgsyv sihssgfrdf llkpellrai
       61 vdcgfehpse vqhecipqai lgmdvlcqak sgmgktavfv latlqqlepv tgqvsvlvmc
      121 htrelafqis keyerfskym pnvkvavffg glsikkdeev lkkncphivv gtpgrilala
      181 rnkslnlkhi khfildecdk mleqldmrrd vqeifrmtph ekqvmmfsat lskeirpvcr
      241 kfmqdpmeif vddetkltlh glqqyyvklk dneknrklfd lldvlefnqv vifvksvqrc
      301 ialaqllveq nfpaiaihrg mpqeerlsry qqfkdfqrri lvatnlfgrg mdiervniaf
      361 nydmpedsdt ylhrvaragr fgtkglaitf vsdendakil ndvqdrfevn iselpdeidi
      421 ssyieqtr
//
LOCUS       NP_001020807             188 aa            linear   ROD 27-APR-2025
DEFINITION  spermatogenesis-associated protein 24 [Rattus norvegicus].
ACCESSION   NP_001020807 XP_214584
VERSION     NP_001020807.2
DBSOURCE    REFSEQ: accession NM_001025636.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Brancorsini,S., Davidson,I. and Sassone-Corsi,P.
  TITLE     TIPT, a male germ cell-specific partner of TRF2, is
            chromatin-associated and interacts with HP1
  JOURNAL   Cell Cycle 7 (10), 1415-1422 (2008)
   PUBMED   18418073
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Song,X.X., Li,Y.C., Shi,Y.Q., Hu,X.Q., Hu,Z.Y., Han,C.S. and
            Liu,Y.X.
  TITLE     Cloning and characterization of a novel spermiogenesis-related
            gene, T6441, in rat testis
  JOURNAL   Front Biosci 11, 143-150 (2006)
   PUBMED   16146721
  REMARK    GeneRIF: the T6441 gene may play a role in cytoplasm movement and
            removal during spermiogenesis
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DQ080016.1, BQ207964.1 and CR463891.1.
            
            On Sep 30, 2011 this sequence version replaced NP_001020807.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ080016.1, BE096042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..188
                     /product="spermatogenesis-associated protein 24"
                     /note="testis protein T6441"
                     /calculated_mol_wt=20881
     Region          22..>128
                     /region_name="SPATA24"
                     /note="Spermatogenesis-associated protein 24; pfam15175"
                     /db_xref="CDD:464544"
     CDS             1..188
                     /gene="Spata24"
                     /gene_synonym="RGD1311742"
                     /coded_by="NM_001025636.2:7..573"
                     /db_xref="GeneID:291676"
                     /db_xref="RGD:1311742"
ORIGIN      
        1 matplgwsqg gsgsvclafd qlrdviesqe elihqlrnvm vlqdenfvsk eefqevekkl
       61 vdekaahakt kallakeeek lqfalgevev lskqlekekm afekalssvk srvlqesskk
      121 dqlitkcngr rearaapqvn ihglfsnspm mvpkaglypn fcprlriqas pggshlrkcl
      181 qgpgrprk
//
LOCUS       NP_001257512             494 aa            linear   ROD 27-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform e precursor [Rattus norvegicus].
ACCESSION   NP_001257512
VERSION     NP_001257512.1
DBSOURCE    REFSEQ: accession NM_001270583.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1, Z23275.1 and CR475040.1.
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon and uses an alternate in-frame splice junction at the 5' end
            of an exon compared to variant (1). The resulting isoform (e) has
            the same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z23275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..494
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform e precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=54388
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          149..443
                     /region_name="7tmB1_PACAP-R1"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type 1 receptor, member of the class B family of
                     seven-transmembrane G protein-coupled receptors; cd15987"
                     /db_xref="CDD:320653"
     Region          151..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320653"
     Site            order(156,160,202,205..206,209,226,233,304..305,307,309,
                     392,395,408,412)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320653"
     Region          185..207
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320653"
     Region          226..253
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320653"
     Region          265..285
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320653"
     Region          301..330
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320653"
     Region          346..400
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320653"
     Region          405..430
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320653"
     CDS             1..494
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_001270583.1:338..1822"
                     /note="isoform e precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiyfcv qkcyckpqra
      361 qqhsckmsel stitlrlars tllliplfgi hytvfafspe nvskrerlvf elglgsfqgf
      421 vvavlycfln gevqaeikrk wrswkvnryf tmdfkhrhps lassgvnggt qlsilsksss
      481 qlrmsslpad nlat
//
LOCUS       NP_446384                377 aa            linear   ROD 27-APR-2025
DEFINITION  lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
            [Rattus norvegicus].
ACCESSION   NP_446384 XP_001060426 XP_344041
VERSION     NP_446384.1
DBSOURCE    REFSEQ: accession NM_053932.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Henion,T.R., Zhou,D., Wolfer,D.P., Jungalwala,F.B. and Hennet,T.
  TITLE     Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase
            GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding
            the key regulator of lacto-series glycolipid biosynthesis
  JOURNAL   J Biol Chem 276 (32), 30261-30269 (2001)
   PUBMED   11384981
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Togayachi,A., Akashima,T., Ookubo,R., Kudo,T., Nishihara,S.,
            Iwasaki,H., Natsume,A., Mio,H., Inokuchi,J., Irimura,T., Sasaki,K.
            and Narimatsu,H.
  TITLE     Molecular cloning and characterization of
            UDP-GlcNAc:lactosylceramide beta
            1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential
            enzyme for the expression of HNK-1 and Lewis X epitopes on
            glycolipids
  JOURNAL   J Biol Chem 276 (25), 22032-22040 (2001)
   PUBMED   11283017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_344041.2, XP_001060426.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.67614.1,
                                           SRR26643297.38779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..377
                     /product="lactosylceramide
                     1,3-N-acetyl-beta-D-glucosaminyltransferase"
                     /EC_number="2.4.1.206"
                     /note="BGnT-5; beta3Gn-T5; lc3 synthase; beta-1,3-Gn-T5;
                     lc(3)Cer synthase; lactotriaosylceramide synthase;
                     beta-1,3-N-acetylglucosaminyltransferase 5;
                     UDP-GlcNAc:beta-Gal
                     beta-1,3-N-acetylglucosaminyltransferase 5"
                     /calculated_mol_wt=44000
     Site            15..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99NB2.2)"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99NB2.2)"
     Region          101..298
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     CDS             1..377
                     /gene="B3gnt5"
                     /coded_by="NM_053932.1:669..1802"
                     /db_xref="GeneID:116740"
                     /db_xref="RGD:70955"
ORIGIN      
        1 mrvfvssrrv krwqffhlfa icfilsfmvf wgpinnyims hmksysyryl insydfvnds
       61 lslkhssvqp hhpylinhre kcqaqdvlll lfiktapeny errsairktw gnenyvqsql
      121 nanikilfal gtphplkgke lqkrliwedq vyhdiiqqdf tdsfhnltfk fllqfgwant
      181 fcpharflmt adddifihmp nlieylqgle qvgvrdfwig hvhrggppvr dksskyyvpy
      241 emykwpaypd ytagaayvvs ndvaakiyea sqtlnssmyi ddvfmglcan kvgvvpqdhv
      301 ffsgegkipy hpciyekmit shghsqdlqd lwveatdpkv kdiskgffgq iycrlikivl
      361 lcrltyrnsy pcraafa
//
LOCUS       NP_059030                125 aa            linear   ROD 27-APR-2025
DEFINITION  cAMP-responsive element modulator isoform 2 [Rattus norvegicus].
ACCESSION   NP_059030
VERSION     NP_059030.2
DBSOURCE    REFSEQ: accession NM_017334.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Xu,K., Liu,Z., Wang,L., Wu,G. and Liu,T.
  TITLE     Influence of hippocampal low-frequency stimulation on GABAA R
            alpha1, ICER and BNDF expression level in brain tissues of
            amygdala-kindled drug-resistant temporal lobe epileptic rats
  JOURNAL   Brain Res 1698, 195-203 (2018)
   PUBMED   30118718
  REMARK    GeneRIF: Expression levels of ICER and BDNF were increased
            remarkably but the GABAA R alpha1 subunit decreased significantly
            in the drug-resistant epileptic rats. However, the expression
            levels of ICER, BDNF were decreased and the expression of the GABAA
            R alpha1 subunit increased significantly in the drug-resistant
            epileptic rats after two weeks of Hip-LFS.
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Miller,M.L., Ren,Y., Szutorisz,H., Warren,N.A., Tessereau,C.,
            Egervari,G., Mlodnicka,A., Kapoor,M., Chaarani,B., Morris,C.V.,
            Schumann,G., Garavan,H., Goate,A.M., Bannon,M.J., Halperin,J.M. and
            Hurd,Y.L.
  CONSRTM   IMAGEN Consortium
  TITLE     Ventral striatal regulation of CREM mediates impulsive action and
            drug addiction vulnerability
  JOURNAL   Mol Psychiatry 23 (5), 1328-1335 (2018)
   PUBMED   28439100
  REMARK    GeneRIF: Using an ADHD rat model, we demonstrate that impulsive
            animals are neurochemically and behaviorally more sensitive to
            heroin and exhibit reduced Crem expression in the nucleus accumbens
            core.
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Zhang,J., Zhu,Y., Liang,C., Qie,M., Niu,R., Sun,Z., Wang,J. and
            Wang,J.
  TITLE     Effects of Fluoride on Expression of P450, CREM and ACT Proteins in
            Rat Testes
  JOURNAL   Biol Trace Elem Res 175 (1), 156-160 (2017)
   PUBMED   27234251
  REMARK    GeneRIF: These data suggest that fluoride can impair male
            reproduction by affecting expression of P450, CREM, and ACT in the
            testes.
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Bitar,M.S. and Al-Mulla,F.
  TITLE     Upregulation of CREM/ICER suppresses wound endothelial
            CRE-HIF-1alpha-VEGF-dependent signaling and impairs angiogenesis in
            type 2 diabetes
  JOURNAL   Dis Model Mech 8 (1), 65-80 (2015)
   PUBMED   25381014
  REMARK    GeneRIF: CREM/ICER is a negative regulator of endothelial function
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Shin,S.Y., Kim,T., Lee,H.S., Kang,J.H., Lee,J.Y., Cho,K.H. and
            Kim,D.H.
  TITLE     The switching role of beta-adrenergic receptor signalling in cell
            survival or death decision of cardiomyocytes
  JOURNAL   Nat Commun 5, 5777 (2014)
   PUBMED   25517116
  REMARK    GeneRIF: The ERK1/2 and ICER-mediated feed forward loop is the
            hidden design principle underlying the switching role of
            beta-adrenergic receptor signaling in cell survival or death
            decision of cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Inada,A., Yamada,Y., Someya,Y., Kubota,A., Yasuda,K., Ihara,Y.,
            Kagimoto,S., Kuroe,A., Tsuda,K. and Seino,Y.
  TITLE     Transcriptional repressors are increased in pancreatic islets of
            type 2 diabetic rats
  JOURNAL   Biochem Biophys Res Commun 253 (3), 712-718 (1998)
   PUBMED   9918792
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Walker,W.H., Sanborn,B.M. and Habener,J.F.
  TITLE     An isoform of transcription factor CREM expressed during
            spermatogenesis lacks the phosphorylation domain and represses
            cAMP-induced transcription
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12423-12427 (1994)
   PUBMED   7809053
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Fujimoto,T., Fujisawa,J. and Yoshida,M.
  TITLE     Novel isoforms of human cyclic AMP-responsive element modulator
            (hCREM) mRNA
  JOURNAL   J Biochem 115 (2), 298-303 (1994)
   PUBMED   8206879
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Stehle,J.H., Foulkes,N.S., Molina,C.A., Simonneaux,V., Pevet,P. and
            Sassone-Corsi,P.
  TITLE     Adrenergic signals direct rhythmic expression of transcriptional
            repressor CREM in the pineal gland
  JOURNAL   Nature 365 (6444), 314-320 (1993)
   PUBMED   8397338
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Meyer,T.E. and Habener,J.F.
  TITLE     Cyclic AMP response element binding protein CREB and modulator
            protein CREM are products of distinct genes
  JOURNAL   Nucleic Acids Res 20 (22), 6106 (1992)
   PUBMED   1461747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Aug 31, 2012 this sequence version replaced NP_059030.1.
            
            Transcript Variant: This variant (2) differs in both UTR's and the
            coding region but maintains the reading frame, compared to variant
            3. This results in a protein (isoform 2) that is shorter at both
            the N- and C-termini, compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.69528.1,
                                           SRR26643294.55842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.1"
     Protein         1..125
                     /product="cAMP-responsive element modulator isoform 2"
                     /note="inducible cyclic AMP early repressor; CRE
                     modulator; cAMP responsive element moderator"
                     /calculated_mol_wt=13821
     Region          69..123
                     /region_name="bZIP_CREB1"
                     /note="Basic leucine zipper (bZIP) domain of Cyclic
                     AMP-responsive element-binding protein 1 (CREB1) and
                     similar proteins: a DNA-binding and dimerization domain;
                     cd14690"
                     /db_xref="CDD:269838"
     Region          70..122
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269838"
     Site            order(70,74,76..78,80..82,84..85,87..89)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269838"
     Site            order(88,91,95..96,98..99,102..103,105..106,109,112..113,
                     116..117,119..120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269838"
     CDS             1..125
                     /gene="Crem"
                     /gene_synonym="Icer"
                     /coded_by="NM_017334.2:46..423"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25620"
                     /db_xref="RGD:2402"
ORIGIN      
        1 mqkpnmavtg detdeetdla pshmaaatgd mptyqirapt talpqgvvma aspgslhspq
       61 qlaeeatrkr elrlmknrea akecrrrkke yvkclesrva vlevqnkkli eeletlkdic
      121 spktd
//
LOCUS       NP_058742                650 aa            linear   ROD 27-APR-2025
DEFINITION  epithelial sodium channel subunit gamma [Rattus norvegicus].
ACCESSION   NP_058742
VERSION     NP_058742.2
DBSOURCE    REFSEQ: accession NM_017046.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Yin,L.P., Zhu,H., Zhu,R.Y. and Huang,L.
  TITLE     A novel SCNN1G mutation in a PHA I infant patient correlates with
            nephropathy
  JOURNAL   Biochem Biophys Res Commun 519 (2), 415-421 (2019)
   PUBMED   31522814
  REMARK    GeneRIF: The SCNN1G defects triggered programmed cell death via
            inhibiting miR-21 and upregulating PTEN, which then orchestrated
            the key downstream regulators, including Bcl2, Bax2, and cleaved
            Caspse-3 in a way that favors cell apoptosis.
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Sharma,S. and Hanukoglu,I.
  TITLE     Mapping the sites of localization of epithelial sodium channel
            (ENaC) and CFTR in segments of the mammalian epididymis
  JOURNAL   J Mol Histol 50 (2), 141-154 (2019)
   PUBMED   30659401
  REMARK    GeneRIF: Based on the widespread presence of ENaC along the
            epididymis we suggest that mutations in ENaC subunits may also be
            associated with male infertility.
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Garcia-Caballero,A., Gandini,M.A., Huang,S., Chen,L., Souza,I.A.,
            Dang,Y.L., Stutts,M.J. and Zamponi,G.W.
  TITLE     Cav3.2 calcium channel interactions with the epithelial sodium
            channel ENaC
  JOURNAL   Mol Brain 12 (1), 12 (2019)
   PUBMED   30736831
  REMARK    GeneRIF: these findings reveal ENaC as an interactor and potential
            regulator of Cav3.2 calcium channels expressed in neuronal tissues.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Zachar,R., Al-Mashhadi,A., Dimke,H., Svenningsen,P., Jensen,B.L.
            and Carlstrom,M.
  TITLE     Hydronephrosis is associated with elevated plasmin in urine in
            pediatric patients and rats and changes in NCC and gamma-ENaC
            abundance in rat kidney
  JOURNAL   Am J Physiol Renal Physiol 315 (3), F547-F557 (2018)
   PUBMED   29767556
  REMARK    GeneRIF: The presence of active plasmin in urine in hydronephrosis
            could cause abnormal proteolytic activation of ENaC-gamma and
            impaired ability to excrete Na via NCC.
REFERENCE   5  (residues 1 to 650)
  AUTHORS   Loh,S.Y., Giribabu,N. and Salleh,N.
  TITLE     Changes in plasma aldosterone and electrolytes levels, kidney
            epithelial sodium channel (ENaC) and blood pressure in normotensive
            WKY and hypertensive SHR rats following gonadectomy and chronic
            testosterone treatment
  JOURNAL   Steroids 128, 128-135 (2017)
   PUBMED   28954214
  REMARK    GeneRIF: Decreased in plasma aldosterone, Na(+) and ENaC levels in
            kidneys under testosterone influence indicated that
            testosterone-induced increased in mean arterial pressure (MAP) were
            not due to increased plasma aldosterone and ENaC levels in kidneys,
            and thus the testosterone effect on MAP likely involve other
            mechanisms.
REFERENCE   6  (residues 1 to 650)
  AUTHORS   Strautnieks,S.S., Thompson,R.J., Gardiner,R.M. and Chung,E.
  TITLE     A novel splice-site mutation in the gamma subunit of the epithelial
            sodium channel gene in three pseudohypoaldosteronism type 1
            families
  JOURNAL   Nat Genet 13 (2), 248-250 (1996)
   PUBMED   8640238
REFERENCE   7  (residues 1 to 650)
  AUTHORS   Staub,O., Dho,S., Henry,P., Correa,J., Ishikawa,T., McGlade,J. and
            Rotin,D.
  TITLE     WW domains of Nedd4 bind to the proline-rich PY motifs in the
            epithelial Na+ channel deleted in Liddle's syndrome
  JOURNAL   EMBO J 15 (10), 2371-2380 (1996)
   PUBMED   8665844
REFERENCE   8  (residues 1 to 650)
  AUTHORS   Hansson,J.H., Nelson-Williams,C., Suzuki,H., Schild,L.,
            Shimkets,R., Lu,Y., Canessa,C., Iwasaki,T., Rossier,B. and
            Lifton,R.P.
  TITLE     Hypertension caused by a truncated epithelial sodium channel gamma
            subunit: genetic heterogeneity of Liddle syndrome
  JOURNAL   Nat Genet 11 (1), 76-82 (1995)
   PUBMED   7550319
REFERENCE   9  (residues 1 to 650)
  AUTHORS   Lingueglia,E., Renard,S., Waldmann,R., Voilley,N., Champigny,G.,
            Plass,H., Lazdunski,M. and Barbry,P.
  TITLE     Different homologous subunits of the amiloride-sensitive Na+
            channel are differently regulated by aldosterone
  JOURNAL   J Biol Chem 269 (19), 13736-13739 (1994)
   PUBMED   8188647
REFERENCE   10 (residues 1 to 650)
  AUTHORS   Canessa,C.M., Schild,L., Buell,G., Thorens,B., Gautschi,I.,
            Horisberger,J.D. and Rossier,B.C.
  TITLE     Amiloride-sensitive epithelial Na+ channel is made of three
            homologous subunits
  JOURNAL   Nature 367 (6462), 463-467 (1994)
   PUBMED   8107805
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Sep 13, 2018 this sequence version replaced NP_058742.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X77933.1, X78034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418971, SAMN16418986
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..650
                     /product="epithelial sodium channel subunit gamma"
                     /note="amiloride-sensitive sodium channel subunit gamma;
                     amiloride sensitive sodium channel gamma1 subunit; SCNEG;
                     gamma-ENaC; gamma-NaCH; pithelial Na(+) channel subunit
                     gamma; epithelial Na(+) channel subunit gamma;
                     nonvoltage-gated sodium channel 1 subunit gamma; Sodium
                     channel, nonvoltage-gated 1, gamma (epithelial); sodium
                     channel, nonvoltage-gated, type I, gamma; epithelial
                     sodium channel gamma subunit; sodium channel,
                     non-voltage-gated 1, gamma subunit; sodium channel
                     epithelial 1 gamma subunit"
                     /calculated_mol_wt=73934
     Region          24..631
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     Region          135..222
                     /region_name="Gating release of inhibition by proteolysis
                     (GRIP), protease-sensitive region that is responsible for
                     the proteolytic activation of the channel.
                     /evidence=ECO:0000250|UniProtKB:P51170"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     Site            138..139
                     /site_type="cleavage"
                     /note="Cleavage, by furin.
                     /evidence=ECO:0000250|UniProtKB:Q9WU39; propagated from
                     UniProtKB/Swiss-Prot (P37091.2)"
     Site            181..182
                     /site_type="cleavage"
                     /note="Cleavage, by PRSS8.
                     /evidence=ECO:0000250|UniProtKB:Q9WU39; propagated from
                     UniProtKB/Swiss-Prot (P37091.2)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37091.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37091.2)"
     Site            498
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P37091.2)"
     Site            543..563
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     Region          577..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     Region          624..628
                     /region_name="PY motif, mediates interaction,
                     ubiquitination and inhibition by NEDD4 and NEDD4L.
                     /evidence=ECO:0000269|PubMed:12654927"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     Region          624..628
                     /region_name="PY motif, recruits WW domain-containing
                     proteins and is thereby required for ubiquitination and
                     inhibition of the channel by NEDD4 and NEDD4L.
                     /evidence=ECO:0000250|UniProtKB:P51170"
                     /note="propagated from UniProtKB/Swiss-Prot (P37091.2)"
     CDS             1..650
                     /gene="Scnn1g"
                     /gene_synonym="ENaC"
                     /coded_by="NM_017046.2:82..2034"
                     /db_xref="GeneID:24768"
                     /db_xref="RGD:3641"
ORIGIN      
        1 mapgekikak ikknlpvrgp qaptikdlmh wycmntnthg crrivvsrgr lrrllwiaft
       61 ltavaliiwq callvfsfyt vsvsikvhfq kldfpavtic ninpykysav sdlltdldse
      121 tkqallslyg vkesrkrrea gsmpstlegt pprffklipl lvfnenekgk ardfftgrkr
      181 kisgkiihka snvmhvhesk klvgfqlcsn dtsdcatytf ssginaiqew yklhymnima
      241 qvplekkinm sysakellvt cffdgmscda rnftlfhhpm ygncytfnnk enatilstsm
      301 ggseyglqvi lyinedeynp flvsstgakv lihqqneypf iedvgmeiet amstsigmhl
      361 tesfklsepy sqctedgsdv pvtniynaay slqiclyscf qtkmvekcgc aqysqplppa
      421 anycnyqqhp nwmycyyqly qafvreelgc qsvckqscsf kewtlttsla qwpseasekw
      481 llnvltwdqs qqinkklnkt dlakllifyk dlnqrsimes pansiemlls nfggqlglwm
      541 scsvvcviei ievffidffs iiarrqwhka kdwwarrqtp pstetpssrq gqdnpaldtd
      601 ddlptftsam rlppapgstv pgtppprynt lrldrafssq ltdtqltnel
//
LOCUS       NP_062027                210 aa            linear   ROD 27-APR-2025
DEFINITION  amelogenin, X isoform isoform 5 precursor [Rattus norvegicus].
ACCESSION   NP_062027
VERSION     NP_062027.1
DBSOURCE    REFSEQ: accession NM_019154.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Buchko,G.W., Lin,G., Tarasevich,B.J. and Shaw,W.J.
  TITLE     A solution NMR investigation into the impaired self-assembly
            properties of two murine amelogenins containing the point mutations
            T21-->I or P41-->T
  JOURNAL   Arch Biochem Biophys 537 (2), 217-224 (2013)
   PUBMED   23896516
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Le Norcy,E., Kwak,S.Y., Wiedemann-Bidlack,F.B., Beniash,E.,
            Yamakoshi,Y., Simmer,J.P. and Margolis,H.C.
  TITLE     Leucine-rich amelogenin peptides regulate mineralization in vitro
  JOURNAL   J Dent Res 90 (9), 1091-1097 (2011)
   PUBMED   21653221
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Buchko,G.W., Tarasevich,B.J., Roberts,J., Snead,M.L. and Shaw,W.J.
  TITLE     A solution NMR investigation into the murine amelogenin
            splice-variant LRAP (Leucine-Rich Amelogenin Protein)
  JOURNAL   Biochim Biophys Acta 1804 (9), 1768-1774 (2010)
   PUBMED   20304108
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Deshpande,A.S., Fang,P.A., Simmer,J.P., Margolis,H.C. and
            Beniash,E.
  TITLE     Amelogenin-collagen interactions regulate calcium phosphate
            mineralization in vitro
  JOURNAL   J Biol Chem 285 (25), 19277-19287 (2010)
   PUBMED   20404336
  REMARK    GeneRIF: interactions between collagen and amelogenin might play an
            important role in the formation of the DEB providing structural
            continuity between dentin and enamel
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Biz,M.T., Marques,M.R., Crema,V.O., Moriscot,A.S. and dos
            Santos,M.F.
  TITLE     GTPases RhoA and Rac1 are important for amelogenin and DSPP
            expression during differentiation of ameloblasts and odontoblasts
  JOURNAL   Cell Tissue Res 340 (3), 459-470 (2010)
   PUBMED   20387077
  REMARK    GeneRIF: The aim of this study was to verify the expression,
            distribution and role of Rho GTPases in ameloblasts and
            odontoblasts during tooth development in correlation with actin and
            tubulin arrangements and amelogenin and dentin sialophosphoprotein
            expression.
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Bonass,W.A., Kirkham,J., Brookes,S.J., Shore,R.C. and Robinson,C.
  TITLE     Isolation and characterisation of an alternatively-spliced rat
            amelogenin cDNA: LRAP--a highly conserved, functional
            alternatively-spliced amelogenin?
  JOURNAL   Biochim Biophys Acta 1219 (3), 690-692 (1994)
   PUBMED   7948026
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Aldred,M.J., Crawford,P.J., Roberts,E. and Thomas,N.S.
  TITLE     Identification of a nonsense mutation in the amelogenin gene
            (AMELX) in a family with X-linked amelogenesis imperfecta (AIH1)
  JOURNAL   Hum Genet 90 (4), 413-416 (1992)
   PUBMED   1483698
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Salido,E.C., Yen,P.H., Koprivnikar,K., Yu,L.C. and Shapiro,L.J.
  TITLE     The human enamel protein gene amelogenin is expressed from both the
            X and the Y chromosomes
  JOURNAL   Am J Hum Genet 50 (2), 303-316 (1992)
   PUBMED   1734713
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Lagerstrom,M., Dahl,N., Nakahori,Y., Nakagome,Y., Backman,B.,
            Landegren,U. and Pettersson,U.
  TITLE     A deletion in the amelogenin gene (AMG) causes X-linked
            amelogenesis imperfecta (AIH1)
  JOURNAL   Genomics 10 (4), 971-975 (1991)
   PUBMED   1916828
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Fincham,A.G., Hu,Y.Y., Pavlova,Z., Slavkin,H.C. and Snead,M.L.
  TITLE     Human amelogenins: sequences of 'TRAP' molecules
  JOURNAL   Calcif Tissue Int 45 (4), 243-250 (1989)
   PUBMED   2509010
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60562.1 and U67130.1.
            
            Transcript Variant: This variant (5) contains an alternate in-frame
            exon and differs in the 3' UTR and coding sequence compared to
            variant 1. The resulting isoform (5) contains an alternate internal
            segment and has a shorter and distinct C-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: U67130.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMN06621351,
                                    SAMN09345331 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..210
                     /product="amelogenin, X isoform isoform 5 precursor"
                     /note="leucine-rich amelogenin peptide; amelogenin X
                     chromosome"
                     /calculated_mol_wt=21816
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1685
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02817; propagated from
                     UniProtKB/Swiss-Prot (P63278.1)"
     Region          49..210
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     Region          109..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63278.1)"
     CDS             1..210
                     /gene="Amelx"
                     /gene_synonym="Amel; LRAP"
                     /coded_by="NM_019154.2:67..699"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:29160"
                     /db_xref="RGD:2107"
ORIGIN      
        1 mgtwilfacl lgaafamplp phpgspgyin lsyekshsqa intdrtalvl tplkwyqsmi
       61 rqpypsygye pmggwlhhqi ipvlsqqhpp shtlqphhhl pvvpaqqpva pqqpmmpvpg
      121 hhsmtptqhh qpnippsaqq pfqqpfqpqa ippqshqpmq pqsplhpmqp lapqpplppl
      181 fsmqplspil pelpleawpa tdktkreevd
//
LOCUS       NP_001034938             253 aa            linear   ROD 27-APR-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase isoform B [Rattus
            norvegicus].
ACCESSION   NP_001034938
VERSION     NP_001034938.1
DBSOURCE    REFSEQ: accession NM_001039849.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Chen,B., Fan,P., Song,X. and Duan,M.
  TITLE     The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury
  JOURNAL   BMC Cardiovasc Disord 24 (1), 531 (2024)
   PUBMED   39354361
  REMARK    GeneRIF: The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Liu,D., Ren,L. and Liu,J.
  TITLE     METTL14 promotes chondrocyte ferroptosis in osteoarthritis via m6A
            modification of GPX4
  JOURNAL   Int J Rheum Dis 27 (8), e15297 (2024)
   PUBMED   39175261
  REMARK    GeneRIF: METTL14 promotes chondrocyte ferroptosis in osteoarthritis
            via m6A modification of GPX4.
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Chen,D., Tang,Q., Song,W. and He,Y.
  TITLE     Platelet-derived exosomes alleviate tendon stem/progenitor cell
            senescence and ferroptosis by regulating AMPK/Nrf2/GPX4 signaling
            and improve tendon-bone junction regeneration in rats
  JOURNAL   J Orthop Surg Res 19 (1), 382 (2024)
   PUBMED   38943181
  REMARK    GeneRIF: Platelet-derived exosomes alleviate tendon stem/progenitor
            cell senescence and ferroptosis by regulating AMPK/Nrf2/GPX4
            signaling and improve tendon-bone junction regeneration in rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Pfeifer,H., Conrad,M., Roethlein,D., Kyriakopoulos,A.,
            Brielmeier,M., Bornkamm,G.W. and Behne,D.
  TITLE     Identification of a specific sperm nuclei selenoenzyme necessary
            for protamine thiol cross-linking during sperm maturation
  JOURNAL   FASEB J 15 (7), 1236-1238 (2001)
   PUBMED   11344099
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Ursini,F., Heim,S., Kiess,M., Maiorino,M., Roveri,A., Wissing,J.
            and Flohe,L.
  TITLE     Dual function of the selenoprotein PHGPx during sperm maturation
  JOURNAL   Science 285 (5432), 1393-1396 (1999)
   PUBMED   10464096
  REMARK    GeneRIF: Rat Gpx4 is a moonlighting protein that functions both as
            a peroxidase, as well as a structural protein.
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Arai,M., Imai,H., Koumura,T., Yoshida,M., Emoto,K., Umeda,M.,
            Chiba,N. and Nakagawa,Y.
  TITLE     Mitochondrial phospholipid hydroperoxide glutathione peroxidase
            plays a major role in preventing oxidative injury to cells
  JOURNAL   J Biol Chem 274 (8), 4924-4933 (1999)
   PUBMED   9988735
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Pushpa-Rekha,T.R., Burdsall,A.L., Oleksa,L.M., Chisolm,G.M. and
            Driscoll,D.M.
  TITLE     Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning
            and identification of multiple transcription and translation start
            sites
  JOURNAL   J Biol Chem 270 (45), 26993-26999 (1995)
   PUBMED   7592947
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Imai,H., Sumi,D., Hanamoto,A., Arai,M. and Sugiyama,A.
  TITLE     Molecular cloning and functional expression of a cDNA for rat
            phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated
            region of the gene is necessary for functional expression
  JOURNAL   J Biochem 118 (5), 1061-1067 (1995)
   PUBMED   8749327
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Roveri,A., Casasco,A., Maiorino,M., Dalan,P., Calligaro,A. and
            Ursini,F.
  TITLE     Phospholipid hydroperoxide glutathione peroxidase of rat testis.
            Gonadotropin dependence and immunocytochemical identification
  JOURNAL   J Biol Chem 267 (9), 6142-6146 (1992)
   PUBMED   1556123
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Thomas,J.P., Geiger,P.G., Maiorino,M., Ursini,F. and Girotti,A.W.
  TITLE     Enzymatic reduction of phospholipid and cholesterol hydroperoxides
            in artificial bilayers and lipoproteins
  JOURNAL   Biochim Biophys Acta 1045 (3), 252-260 (1990)
   PUBMED   2386798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Disruption of this gene in mouse spermatocytes
            is associated with male infertility. This isozyme is also a
            selenoprotein, containing the rare amino acid selenocysteine (Sec)
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon, rather than as a stop signal.
            Transcript variants resulting from alternative splicing or use of
            alternate promoters have been described to encode isoforms with
            different subcellular localization. Pseudogenes of this locus have
            been identified on chromosomes 1, 10 and 14. [provided by RefSeq,
            Jan 2019].
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon compared to variant 1. The resulting isoform (B, also
            know as snGPx) has a longer and a distinct N-terminus compared to
            isoform A. This isoform has been reported to be localized in the
            sperm nucleus (PMID:11344099).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB072798.1, SRR26643293.38622.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 9988735
            multifunctional gene product(s)    :: PMID: 10464096
            protein contains selenocysteine    :: PMID: 8749327
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..253
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase isoform B"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxide glutathione peroxidase,
                     nuclear; phospholipid hydroperoxide glutathione
                     peroxidase, mitochondrial"
                     /calculated_mol_wt=29204
     Region          96..249
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(129,164,219)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            129
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(163,166,168,171,174,178)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..253
                     /gene="Gpx4"
                     /gene_synonym="gpx-4; Gshpx-4; Phgpx; snGpx"
                     /coded_by="NM_001039849.3:13..774"
                     /note="UGA stop codon recoded as selenocysteine; isoform B
                     is encoded by transcript variant 2"
                     /db_xref="GeneID:29328"
                     /db_xref="RGD:69226"
ORIGIN      
        1 mgraaarkrg rcrqrgrspg grrrrepgrq sprkrpgprr rrararrrrr arprrmepip
       61 epfnprpllq dlpqtsnshe flglcasrdd wrcarsmhef aakdidghmv cldkyrgcvc
      121 ivtnvasqug ktdvnytqlv dlharyaecg lrilafpcnq fgrqepgsnq eikefaagyn
      181 vrfdmyskic vngddahplw kwmkvqpkgr gmlgnaikwn ftkflidkng cvvkrygpme
      241 epqviekdlp cyl
//
LOCUS       NP_001163948             342 aa            linear   ROD 27-APR-2025
DEFINITION  growth hormone-regulated TBC protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001163948
VERSION     NP_001163948.1
DBSOURCE    REFSEQ: accession NM_001170477.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1089109.1,
                                           SRR23984936.264060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..342
                     /product="growth hormone-regulated TBC protein 1 isoform
                     1"
                     /note="GH regulated TBC protein 1"
                     /calculated_mol_wt=38922
     Region          71..284
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..342
                     /gene="Grtp1"
                     /gene_synonym="LRRGT00052"
                     /coded_by="NM_001170477.2:78..1106"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361180"
                     /db_xref="RGD:1309210"
ORIGIN      
        1 mdpaeraqaa rarvpridpy gferpedfdy aayeeffsty lviltkraik wskllkgsgg
       61 vrksvtvkry vrkgiplehr arvwmavsga qaqmdqnpgy yhrllegess srleeairtd
      121 lnrtfpdnvm frktadpclq ktlynvllay glhnqdvgyc qgmnfiagyl ilitkneees
      181 fwlldalvgr ilpdyyspam lglktdqevl aelvrmklpa vaalmdghgv lwtllvsrwf
      241 iclfvdilpv etvlriwdcl fnegskiifr valtlikqhq efileassvp dicdkfkqit
      301 kgdfvtecht fmqkifsepg slsmatitrl rescraalqa qs
//
LOCUS       NP_113908                262 aa            linear   ROD 27-APR-2025
DEFINITION  type II iodothyronine deiodinase [Rattus norvegicus].
ACCESSION   NP_113908
VERSION     NP_113908.4
DBSOURCE    REFSEQ: accession NM_031720.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Bai,Z., Chai,X.R., Yoon,M.J., Kim,H.J., Lo,K.A., Zhang,Z.C., Xu,D.,
            Siang,D.T.C., Walet,A.C.E., Xu,S.H., Chia,S.Y., Chen,P., Yang,H.,
            Ghosh,S. and Sun,L.
  TITLE     Dynamic transcriptome changes during adipose tissue energy
            expenditure reveal critical roles for long noncoding RNA regulators
  JOURNAL   PLoS Biol 15 (8), e2002176 (2017)
   PUBMED   28763438
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Martinez-deMena,R., Calvo,R.M., Garcia,L. and Obregon,M.J.
  TITLE     Effect of glucocorticoids on the activity, expression and proximal
            promoter of type II deiodinase in rat brown adipocytes
  JOURNAL   Mol Cell Endocrinol 428, 58-67 (2016)
   PUBMED   26994513
  REMARK    GeneRIF: Glucocorticoids inhibited the adrenergic stimulation of
            Dio2 at the transcriptional level in brown adipocytes.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   da Conceicao,R.R., Laureano-Melo,R., Oliveira,K.C., de Carvalho
            Melo,M.C., Kasamatsu,T.S., de Barros Maciel,R.M., de Souza,J.S. and
            Giannocco,G.
  TITLE     Antidepressant behavior in thyroidectomized Wistar rats is induced
            by hippocampal hypothyroidism
  JOURNAL   Physiol Behav 157, 158-164 (2016)
   PUBMED   26861177
  REMARK    GeneRIF: This study demonstrated that reduction of the Dio2 mRNA
            expression in hippocampus of thyroidectomized Wistar rats.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Werneck de Castro,J.P., Fonseca,T.L., Ueta,C.B., McAninch,E.A.,
            Abdalla,S., Wittmann,G., Lechan,R.M., Gereben,B. and Bianco,A.C.
  TITLE     Differences in hypothalamic type 2 deiodinase ubiquitination
            explain localized sensitivity to thyroxine
  JOURNAL   J Clin Invest 125 (2), 769-781 (2015)
   PUBMED   25555216
  REMARK    GeneRIF: These studies reveal that tissue-specific differences in
            D2 ubiquitination are an inherent property of the TRH/TSH feedback
            mechanism
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Mariotti,M., Ridge,P.G., Zhang,Y., Lobanov,A.V., Pringle,T.H.,
            Guigo,R., Hatfield,D.L. and Gladyshev,V.N.
  TITLE     Composition and evolution of the vertebrate and mammalian
            selenoproteomes
  JOURNAL   PLoS One 7 (3), e33066 (2012)
   PUBMED   22479358
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Salvatore,D., Harney,J.W. and Larsen,P.R.
  TITLE     Mutation of the Secys residue 266 in human type 2 selenodeiodinase
            alters 75Se incorporation without affecting its biochemical
            properties
  JOURNAL   Biochimie 81 (5), 535-538 (1999)
   PUBMED   10403186
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Remmers,E.F., Griffiths,M.M., Longman,R.E., Gulko,P.S.,
            Kawahito,Y., Chen,S., Chang,L., Shepard,J., Ge,L., Dracheva,S.,
            Wang,J.P., Joe,B., Cannon,G.W. and Wilder,R.L.
  TITLE     An integrated rat genetic map: analysis of linkage conservation
            with the mouse and human maps
  JOURNAL   Transplant Proc 31 (3), 1549-1554 (1999)
   PUBMED   10330996
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Gondou,A., Toyoda,N., Nishikawa,M., Tabata,S., Yonemoto,T.,
            Ogawa,Y., Tokoro,T., Sakaguchi,N., Wang,F. and Inada,M.
  TITLE     Induction of type 2 deiodinase activity by cyclic guanosine
            3',5'-monophosphate in cultured rat glial cells
  JOURNAL   Thyroid 8 (7), 615-622 (1998)
   PUBMED   9709916
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Croteau,W., Davey,J.C., Galton,V.A. and St Germain,D.L.
  TITLE     Cloning of the mammalian type II iodothyronine deiodinase. A
            selenoprotein differentially expressed and regulated in human and
            rat brain and other tissues
  JOURNAL   J Clin Invest 98 (2), 405-417 (1996)
   PUBMED   8755651
  REMARK    GeneRIF: The proteins encoded by rat and human Dio2 (deiodinase,
            iodothyronine, type II) genes are selenoproteins.
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Nowak,F.V.
  TITLE     Cloning of two hypothalamic cDNAs encoding tissue-specific
            transcripts in the preoptic area and testis
  JOURNAL   Mol Endocrinol 4 (8), 1205-1210 (1990)
   PUBMED   2293025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000006.1.
            
            On Oct 9, 2018 this sequence version replaced NP_113908.3.
            
            Summary: The protein encoded by this gene belongs to the
            iodothyronine deiodinase family. It catalyzes the conversion of
            prohormone thyroxine (3,5,3',5'-tetraiodothyronine, T4) to the
            bioactive thyroid hormone (3,5,3'-triiodothyronine, T3) by outer
            ring 5'-deiodination. This gene is expressed in a few tissues in
            rat, including brain, pituitary and brown adipose tissue. It is
            thought to be responsible for the 'local' production of T3, and
            thus important in influencing thyroid hormone action in these
            tissues. Studies in rat suggest that this gene may play an
            important role in the regulation of lipid metabolism and
            thermogenesis, and in osteoarthritis pathogenesis by enhancing the
            chondrocyte hypertrophy and inflammatory response. This protein is
            a selenoprotein containing the non-standard amino acid,
            selenocysteine (Sec), which is encoded by the UGA codon that
            normally signals translation termination. The 3' UTRs of
            selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. Unlike the other two members (DIO1 and DIO3) of this
            enzyme family, the mRNA for this gene contains an additional
            in-frame UGA codon that has been reported (in human) to function
            either as a Sec or a stop codon, resulting in two potential
            isoforms with one or two Sec residues; however, only the upstream
            Sec (conserved with the single Sec residue found at the active site
            in DIO1 and DIO3) was shown to be essential for enzyme activity
            (PMID:10403186). In addition, the lack of conservation of the
            protein extension past the second TGA codon suggests that the
            one-Sec containing isoform represents the canonical form. [provided
            by RefSeq, Oct 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U53505.1, SRR26360190.907832.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: PMID: 8755651
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..262
                     /product="type II iodothyronine deiodinase"
                     /EC_number="1.21.99.4"
                     /note="type 2 DI; type-II 5'-deiodinase; deiodinase,
                     iodothyronine, type 2; deiodinase, iodothyronine, type II"
                     /calculated_mol_wt=29248
     Region          4..259
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Site            10..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P70551.4)"
     Site            130
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..262
                     /gene="Dio2"
                     /gene_synonym="5DII; DIOII"
                     /coded_by="NM_031720.5:564..1352"
                     /db_xref="GeneID:65162"
                     /db_xref="RGD:68418"
ORIGIN      
        1 mgllsvdlli tlqilpvffs nclflalyds villkhvall lsrskstrge wrrmltsegl
       61 rcvwnsflld aykqvklged apnssvvhvs npeagnncas ektadgaech lldfasaerp
      121 lvvnfgsatu ppftrqlpaf rqlveefssv adfllvyide ahpsdgwavp gdssmsfevk
      181 khrnqedrca aahqllerfs lppqcqvvad rmdnnanvay gvafervciv qrrkiaylgg
      241 kgpfsynlqe vrswleknfs kr
//
LOCUS       NP_001020819              82 aa            linear   ROD 27-APR-2025
DEFINITION  SNARE-associated protein Snapin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001020819 XP_215602
VERSION     NP_001020819.1
DBSOURCE    REFSEQ: accession NM_001025648.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Somanath,S., Partridge,C.J., Marshall,C., Rowe,T. and Turner,M.D.
  TITLE     Snapin mediates insulin secretory granule docking, but not
            trans-SNARE complex formation
  JOURNAL   Biochem Biophys Res Commun 473 (2), 403-407 (2016)
   PUBMED   26946359
  REMARK    GeneRIF: In pancreatic beta-cells the SNAP-25 accessory protein,
            snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal
            Sn-1 domain.
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Pu,J., Schindler,C., Jia,R., Jarnik,M., Backlund,P. and
            Bonifacino,J.S.
  TITLE     BORC, a multisubunit complex that regulates lysosome positioning
  JOURNAL   Dev Cell 33 (2), 176-188 (2015)
   PUBMED   25898167
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Yun,H.J., Park,J., Ho,D.H., Kim,H., Kim,C.H., Oh,H., Ga,I., Seo,H.,
            Chang,S., Son,I. and Seol,W.
  TITLE     LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with
            SNAP-25
  JOURNAL   Exp Mol Med 45 (8), e36 (2013)
   PUBMED   23949442
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Kim,H.J., Zhong,Q., Sheng,Z.H., Yoshimori,T., Liang,C. and
            Jung,J.U.
  TITLE     Beclin-1-interacting autophagy protein Atg14L targets the
            SNARE-associated protein Snapin to coordinate endocytic trafficking
  JOURNAL   J Cell Sci 125 (Pt 20), 4740-4750 (2012)
   PUBMED   22797916
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Lee,H.H., Nemecek,D., Schindler,C., Smith,W.J., Ghirlando,R.,
            Steven,A.C., Bonifacino,J.S. and Hurley,J.H.
  TITLE     Assembly and architecture of biogenesis of lysosome-related
            organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 287 (8), 5882-5890 (2012)
   PUBMED   22203680
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Vites,O., Rhee,J.S., Schwarz,M., Rosenmund,C. and Jahn,R.
  TITLE     Reinvestigation of the role of snapin in neurotransmitter release
  JOURNAL   J Biol Chem 279 (25), 26251-26256 (2004)
   PUBMED   15084593
  REMARK    GeneRIF: snapin may not have a role as a SNARE regulator in
            neurotransmitter release, as had been previously thought [SNAPIN]
REFERENCE   8  (residues 1 to 82)
  AUTHORS   Buxton,P., Zhang,X.M., Walsh,B., Sriratana,A., Schenberg,I.,
            Manickam,E. and Rowe,T.
  TITLE     Identification and characterization of Snapin as a ubiquitously
            expressed SNARE-binding protein that interacts with SNAP23 in
            non-neuronal cells
  JOURNAL   Biochem J 375 (Pt 2), 433-440 (2003)
   PUBMED   12877659
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Chheda,M.G., Ashery,U., Thakur,P., Rettig,J. and Sheng,Z.H.
  TITLE     Phosphorylation of Snapin by PKA modulates its interaction with the
            SNARE complex
  JOURNAL   Nat Cell Biol 3 (4), 331-338 (2001)
   PUBMED   11283605
REFERENCE   10 (residues 1 to 82)
  AUTHORS   Ilardi,J.M., Mochida,S. and Sheng,Z.H.
  TITLE     Snapin: a SNARE-associated protein implicated in synaptic
            transmission
  JOURNAL   Nat Neurosci 2 (2), 119-124 (1999)
   PUBMED   10195194
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1 and FN803363.1.
            
            On Jul 22, 2005 this sequence version replaced XP_215602.1.
            
            Transcript Variant: This variant (2) contains an additional segment
            in the 5' region and initiates translation at a downstream start
            codon compared to variant 1. These differences produce a unique 5'
            UTR and a protein (isoform 2) with a shorter and distinct
            N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.572162.1,
                                           SRR26360172.554291.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840108, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..82
                     /product="SNARE-associated protein Snapin isoform 2"
                     /note="SNARE associated protein snapin;
                     synaptosomal-associated protein 25-binding protein; BLOC-1
                     subunit 7; biogenesis of lysosome-related organelles
                     complex 1 subunit 7"
                     /calculated_mol_wt=9324
     Region          <9..56
                     /region_name="Snapin_Pallidin"
                     /note="Snapin/Pallidin; pfam14712"
                     /db_xref="CDD:464275"
     CDS             1..82
                     /gene="Snapin"
                     /gene_synonym="Snapap"
                     /coded_by="NM_001025648.2:456..704"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:295217"
                     /db_xref="RGD:1560377"
ORIGIN      
        1 mlvahflfte lcrinedqkv aldldpyvkk llnarrrvvl vnnilqnaqe rlrrlnhsva
       61 ketarrraml dsgvyppgsp sk
//
LOCUS       NP_037015                295 aa            linear   ROD 27-APR-2025
DEFINITION  sulfotransferase 1E1 [Rattus norvegicus].
ACCESSION   NP_037015 NP_001007719 XP_001081145 XP_346462
VERSION     NP_037015.2
DBSOURCE    REFSEQ: accession NM_012883.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Ihunnah,C.A., Wada,T., Philips,B.J., Ravuri,S.K., Gibbs,R.B.,
            Kirisci,L., Rubin,J.P., Marra,K.G. and Xie,W.
  TITLE     Estrogen sulfotransferase/SULT1E1 promotes human adipogenesis
  JOURNAL   Mol Cell Biol 34 (9), 1682-1694 (2014)
   PUBMED   24567372
REFERENCE   2  (residues 1 to 295)
  AUTHORS   McGill,M.R. and Jaeschke,H.
  TITLE     Metabolism and disposition of acetaminophen: recent advances in
            relation to hepatotoxicity and diagnosis
  JOURNAL   Pharm Res 30 (9), 2174-2187 (2013)
   PUBMED   23462933
  REMARK    Review article
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Kurogi,K., Davidson,G., Mohammed,Y.I., Williams,F.E., Liu,M.Y.,
            Sakakibara,Y., Suiko,M. and Liu,M.C.
  TITLE     Ethanol sulfation by the human cytosolic sulfotransferases: a
            systematic analysis
  JOURNAL   Biol Pharm Bull 35 (12), 2180-2185 (2012)
   PUBMED   23207770
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Purohit,A., Woo,L.W. and Potter,B.V.
  TITLE     Steroid sulfatase: a pivotal player in estrogen synthesis and
            metabolism
  JOURNAL   Mol Cell Endocrinol 340 (2), 154-160 (2011)
   PUBMED   21693170
  REMARK    Review article
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Brand,W., Boersma,M.G., Bik,H., Hoek-van den Hil,E.F., Vervoort,J.,
            Barron,D., Meinl,W., Glatt,H., Williamson,G., van Bladeren,P.J. and
            Rietjens,I.M.
  TITLE     Phase II metabolism of hesperetin by individual
            UDP-glucuronosyltransferases and sulfotransferases and rat and
            human tissue samples
  JOURNAL   Drug Metab Dispos 38 (4), 617-625 (2010)
   PUBMED   20056724
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Song,W.C., Qian,Y., Sun,X. and Negishi,M.
  TITLE     Cellular localization and regulation of expression of testicular
            estrogen sulfotransferase
  JOURNAL   Endocrinology 138 (11), 5006-5012 (1997)
   PUBMED   9348232
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Rikke,B.A. and Roy,A.K.
  TITLE     Structural relationships among members of the mammalian
            sulfotransferase gene family
  JOURNAL   Biochim Biophys Acta 1307 (3), 331-338 (1996)
   PUBMED   8688469
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Falany,J.L., Krasnykh,V., Mikheeva,G. and Falany,C.N.
  TITLE     Isolation and expression of an isoform of rat estrogen
            sulfotransferase
  JOURNAL   J Steroid Biochem Mol Biol 52 (1), 35-44 (1995)
   PUBMED   7857871
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Demyan,W.F., Song,C.S., Kim,D.S., Her,S., Gallwitz,W., Rao,T.R.,
            Slomczynska,M., Chatterjee,B. and Roy,A.K.
  TITLE     Estrogen sulfotransferase of the rat liver: complementary DNA
            cloning and age- and sex-specific regulation of messenger RNA
  JOURNAL   Mol Endocrinol 6 (4), 589-597 (1992)
   PUBMED   1374839
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Bajoriniene,D., Balkevicius,B., Rockiene,A. and Dautartiene,A.
  TITLE     Trichinellosis in Lithuania (1978-1987)
  JOURNAL   Wiad Parazytol 38 (3-4), 151-152 (1992)
   PUBMED   1299062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Sep 13, 2018 this sequence version replaced NP_037015.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088157.1, M86758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..295
                     /product="sulfotransferase 1E1"
                     /EC_number="2.8.2.4"
                     /note="estrone sulfotransferase; sulfotransferase,
                     estrogen-preferring; sulfotransferase family 1E,
                     estrogen-preferring, member 1; estrogen sulfotransferase"
                     /calculated_mol_wt=35231
     Region          38..288
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P52844.2)"
     CDS             1..295
                     /gene="Sult1e1"
                     /gene_synonym="EST-1; EST-2; EST-3; EST-6; ESTSUL; rEST-6;
                     ST1E1; Ste; Ste1; ste2"
                     /coded_by="NM_012883.2:116..1003"
                     /db_xref="GeneID:360268"
                     /db_xref="RGD:3776"
ORIGIN      
        1 metsmpeyye vfgdfhgvlm dklftkywed vetfsarpdd llvvtypksg stwigeivdm
       61 iykegdvekc kedaifnrip ylecrnedli ngikqlkeke sprivkthlp akllpasfwe
      121 knckiiylcr nakdvvvsyy yffliiksyp npksfsefve kfmegqvpyg swydhvksww
      181 eksknsrvlf mfyedmkedi rrevvklief lerdplaelv dkiiqhtsfq emknnpctny
      241 smlpetmidl kvspfmrkgi vgdwrnhfpe alrerfeehy qrhmkdcpvk frael
//
LOCUS       NP_001354972             170 aa            linear   ROD 27-APR-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase isoform C [Rattus
            norvegicus].
ACCESSION   NP_001354972
VERSION     NP_001354972.1
DBSOURCE    REFSEQ: accession NM_001368043.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Chen,B., Fan,P., Song,X. and Duan,M.
  TITLE     The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury
  JOURNAL   BMC Cardiovasc Disord 24 (1), 531 (2024)
   PUBMED   39354361
  REMARK    GeneRIF: The role and possible mechanism of the ferroptosis-related
            SLC7A11/GSH/GPX4 pathway in myocardial ischemia-reperfusion injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Liu,D., Ren,L. and Liu,J.
  TITLE     METTL14 promotes chondrocyte ferroptosis in osteoarthritis via m6A
            modification of GPX4
  JOURNAL   Int J Rheum Dis 27 (8), e15297 (2024)
   PUBMED   39175261
  REMARK    GeneRIF: METTL14 promotes chondrocyte ferroptosis in osteoarthritis
            via m6A modification of GPX4.
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Chen,D., Tang,Q., Song,W. and He,Y.
  TITLE     Platelet-derived exosomes alleviate tendon stem/progenitor cell
            senescence and ferroptosis by regulating AMPK/Nrf2/GPX4 signaling
            and improve tendon-bone junction regeneration in rats
  JOURNAL   J Orthop Surg Res 19 (1), 382 (2024)
   PUBMED   38943181
  REMARK    GeneRIF: Platelet-derived exosomes alleviate tendon stem/progenitor
            cell senescence and ferroptosis by regulating AMPK/Nrf2/GPX4
            signaling and improve tendon-bone junction regeneration in rats.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Pfeifer,H., Conrad,M., Roethlein,D., Kyriakopoulos,A.,
            Brielmeier,M., Bornkamm,G.W. and Behne,D.
  TITLE     Identification of a specific sperm nuclei selenoenzyme necessary
            for protamine thiol cross-linking during sperm maturation
  JOURNAL   FASEB J 15 (7), 1236-1238 (2001)
   PUBMED   11344099
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Ursini,F., Heim,S., Kiess,M., Maiorino,M., Roveri,A., Wissing,J.
            and Flohe,L.
  TITLE     Dual function of the selenoprotein PHGPx during sperm maturation
  JOURNAL   Science 285 (5432), 1393-1396 (1999)
   PUBMED   10464096
  REMARK    GeneRIF: Rat Gpx4 is a moonlighting protein that functions both as
            a peroxidase, as well as a structural protein.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Arai,M., Imai,H., Koumura,T., Yoshida,M., Emoto,K., Umeda,M.,
            Chiba,N. and Nakagawa,Y.
  TITLE     Mitochondrial phospholipid hydroperoxide glutathione peroxidase
            plays a major role in preventing oxidative injury to cells
  JOURNAL   J Biol Chem 274 (8), 4924-4933 (1999)
   PUBMED   9988735
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Pushpa-Rekha,T.R., Burdsall,A.L., Oleksa,L.M., Chisolm,G.M. and
            Driscoll,D.M.
  TITLE     Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning
            and identification of multiple transcription and translation start
            sites
  JOURNAL   J Biol Chem 270 (45), 26993-26999 (1995)
   PUBMED   7592947
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Imai,H., Sumi,D., Hanamoto,A., Arai,M. and Sugiyama,A.
  TITLE     Molecular cloning and functional expression of a cDNA for rat
            phospholipid hydroperoxide glutathione peroxidase: 3'-untranslated
            region of the gene is necessary for functional expression
  JOURNAL   J Biochem 118 (5), 1061-1067 (1995)
   PUBMED   8749327
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Roveri,A., Casasco,A., Maiorino,M., Dalan,P., Calligaro,A. and
            Ursini,F.
  TITLE     Phospholipid hydroperoxide glutathione peroxidase of rat testis.
            Gonadotropin dependence and immunocytochemical identification
  JOURNAL   J Biol Chem 267 (9), 6142-6146 (1992)
   PUBMED   1556123
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Thomas,J.P., Geiger,P.G., Maiorino,M., Ursini,F. and Girotti,A.W.
  TITLE     Enzymatic reduction of phospholipid and cholesterol hydroperoxides
            in artificial bilayers and lipoproteins
  JOURNAL   Biochim Biophys Acta 1045 (3), 252-260 (1990)
   PUBMED   2386798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Disruption of this gene in mouse spermatocytes
            is associated with male infertility. This isozyme is also a
            selenoprotein, containing the rare amino acid selenocysteine (Sec)
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon, rather than as a stop signal.
            Transcript variants resulting from alternative splicing or use of
            alternate promoters have been described to encode isoforms with
            different subcellular localization. Pseudogenes of this locus have
            been identified on chromosomes 1, 10 and 14. [provided by RefSeq,
            Jan 2019].
            
            Transcript Variant: This variant (3) uses an alternate promoter,
            which results in translation initiation from an in-frame downstream
            AUG start codon compared to variant 1. The encoded isoform (C, also
            known as the S-form) has a shorter N-terminus compared to isoform A
            and is localized in the cytoplasm (PMIDs:7592947, 9988735).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ221899.1, FQ234630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 9988735
            multifunctional gene product(s)    :: PMID: 10464096
            protein contains selenocysteine    :: PMID: 8749327
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..170
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase isoform C"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxide glutathione peroxidase,
                     nuclear; phospholipid hydroperoxide glutathione
                     peroxidase, mitochondrial"
                     /calculated_mol_wt=19359
     Region          13..166
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(46,81,136)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            46
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(80,83,85,88,91,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..170
                     /gene="Gpx4"
                     /gene_synonym="gpx-4; Gshpx-4; Phgpx; snGpx"
                     /coded_by="NM_001368043.1:56..568"
                     /note="UGA stop codon recoded as selenocysteine; isoform C
                     is encoded by transcript variant 3"
                     /db_xref="GeneID:29328"
                     /db_xref="RGD:69226"
ORIGIN      
        1 mcasrddwrc arsmhefaak didghmvcld kyrgcvcivt nvasqugktd vnytqlvdlh
       61 aryaecglri lafpcnqfgr qepgsnqeik efaagynvrf dmyskicvng ddahplwkwm
      121 kvqpkgrgml gnaikwnftk flidkngcvv krygpmeepq viekdlpcyl
//
LOCUS       NP_112518                368 aa            linear   ROD 27-APR-2025
DEFINITION  endophilin-A2 [Rattus norvegicus].
ACCESSION   NP_112518
VERSION     NP_112518.1
DBSOURCE    REFSEQ: accession NM_031239.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Norin,U., Rintisch,C., Meng,L., Forster,F., Ekman,D., Tuncel,J.,
            Klocke,K., Backlund,J., Yang,M., Bonner,M.Y., Lahore,G.F.,
            James,J., Shchetynsky,K., Bergquist,M., Gjertsson,I., Hubner,N.,
            Backdahl,L. and Holmdahl,R.
  TITLE     Endophilin A2 deficiency protects rodents from autoimmune arthritis
            by modulating T cell activation
  JOURNAL   Nat Commun 12 (1), 610 (2021)
   PUBMED   33504785
  REMARK    GeneRIF: Endophilin A2 deficiency protects rodents from autoimmune
            arthritis by modulating T cell activation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Liu,Y., Shen,H.J., Wang,X.Q., Liu,H.Q., Zheng,L.Y. and Luo,J.D.
  TITLE     EndophilinA2 protects against angiotensin II-induced cardiac
            hypertrophy by inhibiting angiotensin II type 1 receptor
            trafficking in neonatal rat cardiomyocytes
  JOURNAL   J Cell Biochem 119 (10), 8290-8303 (2018)
   PUBMED   29923351
  REMARK    GeneRIF: EndophilinA2 protects against angiotensin II-induced
            cardiac hypertrophy by inhibiting angiotensin II type 1 receptor
            trafficking in neonatal rat cardiomyocytes.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Liu,Y., Liu,H.Q., Xiao,J.Y., Ma,K.T., Wang,X.Q., Shen,H.J. and
            Luo,J.D.
  TITLE     Autophagy is involved in the protective effect of endophilin A2 on
            H2O2-induced apoptosis in H9C2 cardiomyocytes
  JOURNAL   Biochem Biophys Res Commun 499 (2), 299-306 (2018)
   PUBMED   29574155
  REMARK    GeneRIF: EndoA2 inhibited hydrogen peroxide-induced apoptosis in
            H9C2 cardiomyocytes.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhang,J., Yin,Y., Ji,Z., Cai,Z., Zhao,B., Li,J., Tan,M. and Guo,G.
  TITLE     Endophilin2 Interacts with GluA1 to Mediate AMPA Receptor
            Endocytosis Induced by Oligomeric Amyloid-beta
  JOURNAL   Neural Plast 2017, 8197085 (2017)
   PUBMED   28758034
  REMARK    GeneRIF: Study demonstrates that endophilin2 does not contribute to
            constitutive AMPA receptor endocytosis.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Wuertenberger,S. and Groemping,Y.
  TITLE     A single PXXP motif in the C-terminal region of srGAP3 mediates
            binding to multiple SH3 domains
  JOURNAL   FEBS Lett 589 (10), 1156-1163 (2015)
   PUBMED   25819436
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Ralser,M., Nonhoff,U., Albrecht,M., Lengauer,T., Wanker,E.E.,
            Lehrach,H. and Krobitsch,S.
  TITLE     Ataxin-2 and huntingtin interact with endophilin-A complexes to
            function in plastin-associated pathways
  JOURNAL   Hum Mol Genet 14 (19), 2893-2909 (2005)
   PUBMED   16115810
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Chen,Y., Deng,L., Maeno-Hikichi,Y., Lai,M., Chang,S., Chen,G. and
            Zhang,J.F.
  TITLE     Formation of an endophilin-Ca2+ channel complex is critical for
            clathrin-mediated synaptic vesicle endocytosis
  JOURNAL   Cell 115 (1), 37-48 (2003)
   PUBMED   14532001
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Ringstad,N., Nemoto,Y. and De Camilli,P.
  TITLE     Differential expression of endophilin 1 and 2 dimers at central
            nervous system synapses
  JOURNAL   J Biol Chem 276 (44), 40424-40430 (2001)
   PUBMED   11518713
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Nemoto,Y., Wenk,M.R., Watanabe,M., Daniell,L., Murakami,T.,
            Ringstad,N., Yamada,H., Takei,K. and De Camilli,P.
  TITLE     Identification and characterization of a synaptojanin 2 splice
            isoform predominantly expressed in nerve terminals
  JOURNAL   J Biol Chem 276 (44), 41133-41142 (2001)
   PUBMED   11498538
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Ringstad,N., Nemoto,Y. and De Camilli,P.
  TITLE     The SH3p4/Sh3p8/SH3p13 protein family: binding partners for
            synaptojanin and dynamin via a Grb2-like Src homology 3 domain
  JOURNAL   Proc Natl Acad Sci U S A 94 (16), 8569-8574 (1997)
   PUBMED   9238017
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB615317.1 and BC070893.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070893.1, AB008161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..368
                     /product="endophilin-A2"
                     /note="endophilin-2; SH3 domain protein 2B; SH3
                     domain-containing GRB2-like protein 1; SH3-domain
                     GRB2-like 1; SH3 domain-containing GRB2-like 1"
                     /calculated_mol_wt=41361
     Region          1..21
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          25..247
                     /region_name="BAR_Endophilin_A"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of
                     Endophilin-A; cd07592"
                     /db_xref="CDD:153276"
     Site            order(38..39,42..43,45..46,49..50,53,57,60..61,89..90,
                     92..93,96..97,100,103..104,108..110,113..114,208..209,
                     211..213,215..216,219,222..223,225..227,229..230,233..234,
                     236..237,240,244)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153276"
     Site            order(45,53,65,152,156,159,164..165,173..174,177,184)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153276"
     Region          60..87
                     /region_name="Required for dimerization upon membrane
                     association. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          218..254
                     /region_name="Interaction with ARC.
                     /evidence=ECO:0000269|PubMed:17088211"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Region          243..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35964.1)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99961; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     Region          309..363
                     /region_name="SH3_Endophilin_A"
                     /note="Src homology 3 domain of Endophilin-A; cd11803"
                     /db_xref="CDD:212737"
     Site            order(315,317,320,324,342..343,356,358..359)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212737"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62419; propagated from
                     UniProtKB/Swiss-Prot (O35964.1)"
     CDS             1..368
                     /gene="Sh3gl1"
                     /gene_synonym="SH3P8"
                     /coded_by="NM_031239.3:142..1248"
                     /db_xref="GeneID:81922"
                     /db_xref="RGD:708456"
ORIGIN      
        1 msvaglkkqf ykasqlvsek vggaegtkld ddfremekkv ditskavaev lvrtieylqp
       61 npasrakltm lntvskirgq vknpgypqse gllgecmvrh gkelggesnf gdalldages
      121 mkrlaevkds ldievkqnfi dplqnlcdkd lkeiqhhlkk legrrldfdy kkkrqgkipd
      181 eelrqalekf eeskevaets mhnlletdie qvsqlsalvd aqldyhrqav qileeladkl
      241 krrvreassr prrefkprpq epfelgeleq pnggfpcasa pkitasssfr sgdkptrtps
      301 ksmppldqps ckalydfepe ndgelgfreg dlitltnqid enwyegmlhg qsgffplsyv
      361 qvlvplpq
//
LOCUS       NP_001013210             402 aa            linear   ROD 27-APR-2025
DEFINITION  olfactomedin-like protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001013210 XP_341900
VERSION     NP_001013210.1
DBSOURCE    REFSEQ: accession NM_001013192.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081972.1.
            
            On Mar 26, 2005 this sequence version replaced XP_341900.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081972.1, FM129944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..402
                     /product="olfactomedin-like protein 1 precursor"
                     /note="olfactomedin-like protein 1"
                     /calculated_mol_wt=42709
     sig_peptide     1..28
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
                     /calculated_mol_wt=2910
     mat_peptide     29..402
                     /product="Olfactomedin-like protein 1. /id=PRO_0000020091"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H86.1)"
                     /calculated_mol_wt=42709
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     Region          145..395
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; pfam02191"
                     /db_xref="CDD:460482"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H86.1)"
     CDS             1..402
                     /gene="Olfml1"
                     /coded_by="NM_001013192.2:304..1512"
                     /db_xref="GeneID:361621"
                     /db_xref="RGD:1311854"
ORIGIN      
        1 mmvalpgasa slvlflaafl pplqhaqdpa mvhyiyqrfq vleqglekca qttrayiqdf
       61 qefsknlstm lgrcqthtne yrsavdnlal rveraqreid ylqylresdf cveseektsa
      121 ekvlqeaeee kkirtllnts cdnmlmaiks lkivkktvdp egswmkdags tsakvyllag
      181 srnntvwefa nlrafmedsv kpgprkltlp lswqgsgqvv yqsflffhnq gtsneiikyn
      241 lqkktvedrm llpggagrap iyqhslstyi dlavdehglw aihsgpgiqg hlvltkieag
      301 tlgiehswdt pcrsqdaeas fllcgvlyvv yssggqgphr itcvydplgt vreehlpnlf
      361 fprrarshsm ihynprdkql yawnegyqii yklqtkkklp le
//
LOCUS       NP_001352080             686 aa            linear   ROD 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001352080 XP_006251146
VERSION     NP_001352080.1
DBSOURCE    REFSEQ: accession NM_001365151.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Liu,Y. and Xu,Y.J.
  TITLE     LKB1 and CRMP1 cooperatively promote the repair of the sciatic
            nerve injury
  JOURNAL   Dev Neurobiol 84 (1), 18-31 (2024)
   PUBMED   38105470
  REMARK    GeneRIF: LKB1 and CRMP1 cooperatively promote the repair of the
            sciatic nerve injury.
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Cruz Hernandez,J.H., Rosado Loman,W.N., Gomez-Crisostomo,N.P., De
            la Cruz-Hernandez,E.N., Guzman Garcia,L.M., Gomez Gomez,M.,
            Hernandez Del Angel,N.A., Aguilar Gamas,C.F., Cruz Hernandez,V.S.
            and Martinez-Abundis,E.
  TITLE     High sugar but not high fat diet consumption induces hepatic
            metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity
  JOURNAL   Arch Physiol Biochem 129 (1), 233-240 (2023)
   PUBMED   32880477
  REMARK    GeneRIF: High sugar but not high fat diet consumption induces
            hepatic metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity.
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Chua,J.Y., Ng,S.J., Yagensky,O., Wanker,E.E. and Chua,J.J.E.
  TITLE     FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon and
            Dendrite Development
  JOURNAL   eNeuro 8 (2) (2021)
   PUBMED   33771901
  REMARK    GeneRIF: FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon
            and Dendrite Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Nakamura,F., Kumeta,K., Hida,T., Isono,T., Nakayama,Y.,
            Kuramata-Matsuoka,E., Yamashita,N., Uchida,Y., Ogura,K.,
            Gengyo-Ando,K., Mitani,S., Ogino,T. and Goshima,Y.
  TITLE     Amino- and carboxyl-terminal domains of Filamin-A interact with
            CRMP1 to mediate Sema3A signalling
  JOURNAL   Nat Commun 5, 5325 (2014)
   PUBMED   25358863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Chen,T.C., Lee,S.A., Hong,T.M., Shih,J.Y., Lai,J.M., Chiou,H.Y.,
            Yang,S.C., Chan,C.H., Kao,C.Y., Yang,P.C. and Huang,C.Y.
  TITLE     From midbody protein-protein interaction network construction to
            novel regulators in cytokinesis
  JOURNAL   J Proteome Res 8 (11), 4943-4953 (2009)
   PUBMED   19799413
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Bevers,M.B., Lawrence,E., Maronski,M., Starr,N., Amesquita,M. and
            Neumar,R.W.
  TITLE     Knockdown of m-calpain increases survival of primary hippocampal
            neurons following NMDA excitotoxicity
  JOURNAL   J Neurochem 108 (5), 1237-1250 (2009)
   PUBMED   19141074
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Bretin,S., Reibel,S., Charrier,E., Maus-Moatti,M., Auvergnon,N.,
            Thevenoux,A., Glowinski,J., Rogemond,V., Premont,J., Honnorat,J.
            and Gauchy,C.
  TITLE     Differential expression of CRMP1, CRMP2A, CRMP2B, and CRMP5 in
            axons or dendrites of distinct neurons in the mouse brain
  JOURNAL   J Comp Neurol 486 (1), 1-17 (2005)
   PUBMED   15834957
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Fukada,M., Watakabe,I., Yuasa-Kawada,J., Kawachi,H., Kuroiwa,A.,
            Matsuda,Y. and Noda,M.
  TITLE     Molecular characterization of CRMP5, a novel member of the
            collapsin response mediator protein family
  JOURNAL   J Biol Chem 275 (48), 37957-37965 (2000)
   PUBMED   10956643
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Wang,L.H. and Strittmatter,S.M.
  TITLE     A family of rat CRMP genes is differentially expressed in the
            nervous system
  JOURNAL   J Neurosci 16 (19), 6197-6207 (1996)
   PUBMED   8815901
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Aug 1, 2018 this sequence version replaced XP_006251146.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.57286.1,
                                           SRR22399481.2524281.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..686
                     /product="dihydropyrimidinase-related protein 1 isoform 1"
                     /note="dihydropyrimidinase-related protein 1; DRP-1;
                     CRMP-1; inactive dihydropyrimidinase"
                     /calculated_mol_wt=74118
     Region          131..580
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(142..143,145,158..159,294,315,318,321,344,348,352,
                     355,382..383,385..386,504,509,514)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(187,189,279,312,368,446)
                     /site_type="active"
                     /db_xref="CDD:238639"
     CDS             1..686
                     /gene="Crmp1"
                     /coded_by="NM_001365151.1:95..2155"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25415"
                     /db_xref="RGD:2407"
ORIGIN      
        1 maerrrawnt eddlpvylar pgsaaqtprq kyggmfaave gayenktidf daysvgrrgs
       61 artprsagrp davglpcpgg sedtasdvse psgsavsspg drddrppalr ircpaprdlp
      121 lgrdngqsdr llirggriin ddqsfyadvy ledglikqig enlivpggvk tieangrmvi
      181 pggidvntyl qkpsqgmtsa ddffqgtraa laggttmiid hvvpepgssl ltsfekwhea
      241 adtksccdys lhvditswyd gvreelevlv qdkgvnsfqv ymaykdlyqm sdsqlyeaft
      301 flkglgavil vhaengdlia qeqkrilemg itgpeghals rpeeleaeav fraiaiagri
      361 ncpvyitkvm sksaadiial arkkgplvfg epiaaslgtd gthywsknwa kaaafvtspp
      421 lspdpttpdy ltsllacgdl qvtgsghcpy staqkavgkd nftlipegvn gieermtvvw
      481 dkavatgkmd enqfvavtst naakifnlyp rkgriavgsd advviwdpdk mktltakshk
      541 stveynifeg mechgsplvv isqgkivfed gnisvskgmg rfiprkpfpe hlyqrvrirs
      601 kvfglhsvsr gmydgpvyev patpkhaapa psaksspskh qpppirnlhq snfslsgaqi
      661 ddnnprrtgh rivappggrs nitslg
//
LOCUS       NP_077343                893 aa            linear   ROD 27-APR-2025
DEFINITION  ephrin type-A receptor 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_077343
VERSION     NP_077343.1
DBSOURCE    REFSEQ: accession NM_024367.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Song,H., Zheng,Y., Cai,F., Ma,Y., Yang,J. and Wu,Y.
  TITLE     c-Fos downregulation positively regulates EphA5 expression in a
            congenital hypothyroidism rat model
  JOURNAL   J Mol Histol 49 (2), 147-155 (2018)
   PUBMED   29330744
  REMARK    GeneRIF: c-fos overexpression could upregulate EphA5 expression in
            hippocampal neurons of rats with congenital hypothyroidism.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Liu,T.T., Xiao,B., Li,S.Y., Li,G.L., Lu,X.Q. and Liu,W.P.
  TITLE     [Changes in the expression of EphA5/ephrinA5 in the CA3 region of
            the hippocampus in rats with epilepsy and their role in the
            pathogenesis of temporal lobe epilepsy]
  JOURNAL   Zhongguo Dang Dai Er Ke Za Zhi 19 (12), 1272-1277 (2017)
   PUBMED   29237529
  REMARK    GeneRIF: Downregulation of ephrinA5 and EphA5 in the CA3 region of
            the hippocampus may participate in the mechanism of mossy fiber
            sprouting and is closely associated with the development and
            progression of epilepsy.
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Wu,Y., Song,H., Sun,B., Xu,M. and Shi,J.
  TITLE     DNA Methylation of the EphA5 Promoter Is Associated with Rat
            Congenital Hypothyroidism
  JOURNAL   J Mol Neurosci 57 (2), 203-210 (2015)
   PUBMED   26109526
  REMARK    GeneRIF: EphA5 promoter methylation in the hippocampus of rats with
            congenital hypothyroidism is associated with the levels of EphA5
            expression.
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Szepietowska,B., Horvath,T.L. and Sherwin,R.S.
  TITLE     Role of synaptic plasticity and EphA5-ephrinA5 interaction within
            the ventromedial hypothalamus in response to recurrent hypoglycemia
  JOURNAL   Diabetes 63 (3), 1140-1147 (2014)
   PUBMED   24222347
  REMARK    GeneRIF: changes in ephrinA5/EphA5 interactions and synaptic
            plasticity within the ventromedial hypothalamus may contribute to
            the impairment in glucagon secretion and counterregulatory
            responses caused by recurrent hypoglycemia.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Buensuceso,A.V. and Deroo,B.J.
  TITLE     The ephrin signaling pathway regulates morphology and adhesion of
            mouse granulosa cells in vitro
  JOURNAL   Biol Reprod 88 (1), 25 (2013)
   PUBMED   23242526
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Bruce,V., Olivieri,G., Eickelberg,O. and Miescher,G.C.
  TITLE     Functional activation of EphA5 receptor does not promote cell
            proliferation in the aberrant EphA5 expressing human glioblastoma
            U-118 MG cell line
  JOURNAL   Brain Res 821 (1), 169-176 (1999)
   PUBMED   10064801
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Taylor,V., Miescher,G.C., Pfarr,S., Honegger,P., Breitschopf,H.,
            Lassmann,H. and Steck,A.J.
  TITLE     Expression and developmental regulation of Ehk-1, a neuronal
            Elk-like receptor tyrosine kinase in brain
  JOURNAL   Neuroscience 63 (1), 163-178 (1994)
   PUBMED   7898646
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Maisonpierre,P.C., Barrezueta,N.X. and Yancopoulos,G.D.
  TITLE     Ehk-1 and Ehk-2: two novel members of the Eph receptor-like
            tyrosine kinase family with distinctive structures and neuronal
            expression
  JOURNAL   Oncogene 8 (12), 3277-3288 (1993)
   PUBMED   7504232
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region and uses an alternate splice
            pattern in the 3' coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment and has a shorter
            and distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X78689.1, SRR26360176.1696901.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..893
                     /product="ephrin type-A receptor 5 isoform 2"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; EPH homology kinase 1;
                     tyrosine-protein kinase receptor EHK-1; eck-like sequence
                     1"
                     /calculated_mol_wt=98905
     Region          62..234
                     /region_name="EphR_LBD"
                     /note="Ligand Binding Domain of Ephrin Receptors; cl02704"
                     /db_xref="CDD:470656"
     Site            order(74,86..89,91..92,97,99,102,135,137,185,193..195,
                     222..224,226)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198439"
     Region          359..449
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(359,422,437)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(438..439,441..442)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          465..562
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          560..826
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(571,573..575,579,595,597,643..644,646,690,694..695,
                     697,708,727..731,740,774)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(571..575,579,595,597,643..646,649..650,694..695,697,
                     708)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(690,694,727..731,740,774)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            707..733
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          855..>893
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     CDS             1..893
                     /gene="Epha5"
                     /gene_synonym="EHK-1; Els1; Els1."
                     /coded_by="NM_024367.2:358..3039"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79208"
                     /db_xref="RGD:620831"
ORIGIN      
        1 mrgsgprgag rrrtqgrggg gdtprvpasl agcysaplkg plwtclllca alrtllasps
       61 nevnlldsrt vlgdlgwiaf pkngweeige vdenyapiht yqvckvmeqn qnnwlltswi
      121 snegasrifi elkftlrdcn slpgglgtck etfnmyyfes ddengrnike nqyikidtia
      181 adesfteldl gdrvmklnte vrdvgplskk gfylafqdvg acialvsvrv yykkcpsvvr
      241 hlavfpdtit gadssqllev sgscvnhsvt ddppkmhcsa egewlvpigk cmckagyeek
      301 ngtcqvcrpg ffkasphsqt cskcpphsyt heeastscvc ekdyfrresd pptmacttps
      361 pvtnvkkgki aknsislswq epdrpngiil eyeikyfekd qetsytiiks kettitaegl
      421 kpasvyvfqi rartaagygv fsrrfefett pvfaasndqs qipiiavsvt vgvillavmi
      481 gfllsgscce cgcgrasslc avahpsliwr cgyskakqdp eeekmhfhng hiklpgvrty
      541 idphtyedpt qavhefakei eascitierv igagefgevc sgrlklpgkr elpvaiktlk
      601 vgytekqrrd flseasimgq fdhpniihle gvvtkskpvm ivteymengs ldtflkkndg
      661 qftviqlvgm lrgiaagmky lsdmgyvhrd laarnilins nlvckvsdfg lsrvleddpe
      721 aayttrggki pirwtapeai afrkftsasd vwsygivmwe vvsygerpyw emtnqdvika
      781 veegyrlpsp mdcpaalyql mldcwqkdrn srpkfddivn mldklirnps slktlvnass
      841 rvstllaehg slgsgayrsv gewleaikmg ryteifmeng yssmdavaqv tle
//
LOCUS       NP_037064                572 aa            linear   ROD 27-APR-2025
DEFINITION  dihydropyrimidinase-related protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_037064
VERSION     NP_037064.1
DBSOURCE    REFSEQ: accession NM_012932.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Liu,Y. and Xu,Y.J.
  TITLE     LKB1 and CRMP1 cooperatively promote the repair of the sciatic
            nerve injury
  JOURNAL   Dev Neurobiol 84 (1), 18-31 (2024)
   PUBMED   38105470
  REMARK    GeneRIF: LKB1 and CRMP1 cooperatively promote the repair of the
            sciatic nerve injury.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Cruz Hernandez,J.H., Rosado Loman,W.N., Gomez-Crisostomo,N.P., De
            la Cruz-Hernandez,E.N., Guzman Garcia,L.M., Gomez Gomez,M.,
            Hernandez Del Angel,N.A., Aguilar Gamas,C.F., Cruz Hernandez,V.S.
            and Martinez-Abundis,E.
  TITLE     High sugar but not high fat diet consumption induces hepatic
            metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity
  JOURNAL   Arch Physiol Biochem 129 (1), 233-240 (2023)
   PUBMED   32880477
  REMARK    GeneRIF: High sugar but not high fat diet consumption induces
            hepatic metabolic disruption and up-regulation of mitochondrial
            fission-associated protein Drp1 in a model of moderate obesity.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Chua,J.Y., Ng,S.J., Yagensky,O., Wanker,E.E. and Chua,J.J.E.
  TITLE     FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon and
            Dendrite Development
  JOURNAL   eNeuro 8 (2) (2021)
   PUBMED   33771901
  REMARK    GeneRIF: FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon
            and Dendrite Development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Nakamura,F., Kumeta,K., Hida,T., Isono,T., Nakayama,Y.,
            Kuramata-Matsuoka,E., Yamashita,N., Uchida,Y., Ogura,K.,
            Gengyo-Ando,K., Mitani,S., Ogino,T. and Goshima,Y.
  TITLE     Amino- and carboxyl-terminal domains of Filamin-A interact with
            CRMP1 to mediate Sema3A signalling
  JOURNAL   Nat Commun 5, 5325 (2014)
   PUBMED   25358863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Chen,T.C., Lee,S.A., Hong,T.M., Shih,J.Y., Lai,J.M., Chiou,H.Y.,
            Yang,S.C., Chan,C.H., Kao,C.Y., Yang,P.C. and Huang,C.Y.
  TITLE     From midbody protein-protein interaction network construction to
            novel regulators in cytokinesis
  JOURNAL   J Proteome Res 8 (11), 4943-4953 (2009)
   PUBMED   19799413
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Bevers,M.B., Lawrence,E., Maronski,M., Starr,N., Amesquita,M. and
            Neumar,R.W.
  TITLE     Knockdown of m-calpain increases survival of primary hippocampal
            neurons following NMDA excitotoxicity
  JOURNAL   J Neurochem 108 (5), 1237-1250 (2009)
   PUBMED   19141074
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Bretin,S., Reibel,S., Charrier,E., Maus-Moatti,M., Auvergnon,N.,
            Thevenoux,A., Glowinski,J., Rogemond,V., Premont,J., Honnorat,J.
            and Gauchy,C.
  TITLE     Differential expression of CRMP1, CRMP2A, CRMP2B, and CRMP5 in
            axons or dendrites of distinct neurons in the mouse brain
  JOURNAL   J Comp Neurol 486 (1), 1-17 (2005)
   PUBMED   15834957
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Fukada,M., Watakabe,I., Yuasa-Kawada,J., Kawachi,H., Kuroiwa,A.,
            Matsuda,Y. and Noda,M.
  TITLE     Molecular characterization of CRMP5, a novel member of the
            collapsin response mediator protein family
  JOURNAL   J Biol Chem 275 (48), 37957-37965 (2000)
   PUBMED   10956643
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Wang,L.H. and Strittmatter,S.M.
  TITLE     A family of rat CRMP genes is differentially expressed in the
            nervous system
  JOURNAL   J Neurosci 16 (19), 6197-6207 (1996)
   PUBMED   8815901
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon and initiates translation at an alternate start codon
            compared to variant 1. The encoded isoform (2) is shorter with a
            distinct N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U52102.2, SRR26643289.35085.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..572
                     /product="dihydropyrimidinase-related protein 1 isoform 2"
                     /note="dihydropyrimidinase-related protein 1; DRP-1;
                     CRMP-1; inactive dihydropyrimidinase"
                     /calculated_mol_wt=62065
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          17..466
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(28..29,31,44..45,180,201,204,207,230,234,238,241,
                     268..269,271..272,390,395,400)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(73,75,165,198,254,332)
                     /site_type="active"
                     /db_xref="CDD:238639"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14194; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14194; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          246..247
                     /region_name="Required for interaction with FLNA.
                     /evidence=ECO:0000250|UniProtKB:Q14194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62950.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Region          509..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62950.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97427; propagated from
                     UniProtKB/Swiss-Prot (Q62950.1)"
     CDS             1..572
                     /gene="Crmp1"
                     /coded_by="NM_012932.3:212..1930"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25415"
                     /db_xref="RGD:2407"
ORIGIN      
        1 mshqgkksip hitsdrllir ggriinddqs fyadvyledg likqigenli vpggvktiea
       61 ngrmvipggi dvntylqkps qgmtsaddff qgtraalagg ttmiidhvvp epgsslltsf
      121 ekwheaadtk sccdyslhvd itswydgvre elevlvqdkg vnsfqvymay kdlyqmsdsq
      181 lyeaftflkg lgavilvhae ngdliaqeqk rilemgitgp eghalsrpee leaeavfrai
      241 aiagrincpv yitkvmsksa adiialarkk gplvfgepia aslgtdgthy wsknwakaaa
      301 fvtspplspd pttpdyltsl lacgdlqvtg sghcpystaq kavgkdnftl ipegvngiee
      361 rmtvvwdkav atgkmdenqf vavtstnaak ifnlyprkgr iavgsdadvv iwdpdkmktl
      421 takshkstve ynifegmech gsplvvisqg kivfedgnis vskgmgrfip rkpfpehlyq
      481 rvrirskvfg lhsvsrgmyd gpvyevpatp khaapapsak sspskhqppp irnlhqsnfs
      541 lsgaqiddnn prrtghriva ppggrsnits lg
//
LOCUS       NP_001164047             136 aa            linear   ROD 27-APR-2025
DEFINITION  SNARE-associated protein Snapin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001164047
VERSION     NP_001164047.1
DBSOURCE    REFSEQ: accession NM_001170576.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Somanath,S., Partridge,C.J., Marshall,C., Rowe,T. and Turner,M.D.
  TITLE     Snapin mediates insulin secretory granule docking, but not
            trans-SNARE complex formation
  JOURNAL   Biochem Biophys Res Commun 473 (2), 403-407 (2016)
   PUBMED   26946359
  REMARK    GeneRIF: In pancreatic beta-cells the SNAP-25 accessory protein,
            snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal
            Sn-1 domain.
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Pu,J., Schindler,C., Jia,R., Jarnik,M., Backlund,P. and
            Bonifacino,J.S.
  TITLE     BORC, a multisubunit complex that regulates lysosome positioning
  JOURNAL   Dev Cell 33 (2), 176-188 (2015)
   PUBMED   25898167
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Yun,H.J., Park,J., Ho,D.H., Kim,H., Kim,C.H., Oh,H., Ga,I., Seo,H.,
            Chang,S., Son,I. and Seol,W.
  TITLE     LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with
            SNAP-25
  JOURNAL   Exp Mol Med 45 (8), e36 (2013)
   PUBMED   23949442
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Kim,H.J., Zhong,Q., Sheng,Z.H., Yoshimori,T., Liang,C. and
            Jung,J.U.
  TITLE     Beclin-1-interacting autophagy protein Atg14L targets the
            SNARE-associated protein Snapin to coordinate endocytic trafficking
  JOURNAL   J Cell Sci 125 (Pt 20), 4740-4750 (2012)
   PUBMED   22797916
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Lee,H.H., Nemecek,D., Schindler,C., Smith,W.J., Ghirlando,R.,
            Steven,A.C., Bonifacino,J.S. and Hurley,J.H.
  TITLE     Assembly and architecture of biogenesis of lysosome-related
            organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 287 (8), 5882-5890 (2012)
   PUBMED   22203680
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Vites,O., Rhee,J.S., Schwarz,M., Rosenmund,C. and Jahn,R.
  TITLE     Reinvestigation of the role of snapin in neurotransmitter release
  JOURNAL   J Biol Chem 279 (25), 26251-26256 (2004)
   PUBMED   15084593
  REMARK    GeneRIF: snapin may not have a role as a SNARE regulator in
            neurotransmitter release, as had been previously thought [SNAPIN]
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Buxton,P., Zhang,X.M., Walsh,B., Sriratana,A., Schenberg,I.,
            Manickam,E. and Rowe,T.
  TITLE     Identification and characterization of Snapin as a ubiquitously
            expressed SNARE-binding protein that interacts with SNAP23 in
            non-neuronal cells
  JOURNAL   Biochem J 375 (Pt 2), 433-440 (2003)
   PUBMED   12877659
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Chheda,M.G., Ashery,U., Thakur,P., Rettig,J. and Sheng,Z.H.
  TITLE     Phosphorylation of Snapin by PKA modulates its interaction with the
            SNARE complex
  JOURNAL   Nat Cell Biol 3 (4), 331-338 (2001)
   PUBMED   11283605
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Ilardi,J.M., Mochida,S. and Sheng,Z.H.
  TITLE     Snapin: a SNARE-associated protein implicated in synaptic
            transmission
  JOURNAL   Nat Neurosci 2 (2), 119-124 (1999)
   PUBMED   10195194
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DY315040.1 and BC098864.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY315040.1, CO401616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..136
                     /product="SNARE-associated protein Snapin isoform 1"
                     /note="SNARE associated protein snapin;
                     synaptosomal-associated protein 25-binding protein; BLOC-1
                     subunit 7; biogenesis of lysosome-related organelles
                     complex 1 subunit 7"
                     /calculated_mol_wt=14773
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Region          23..110
                     /region_name="Snapin_Pallidin"
                     /note="Snapin/Pallidin; pfam14712"
                     /db_xref="CDD:464275"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q9Z266; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Region          83..136
                     /region_name="Interaction with TOR1A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60192.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95295; propagated from
                     UniProtKB/Swiss-Prot (P60192.1)"
     CDS             1..136
                     /gene="Snapin"
                     /gene_synonym="Snapap"
                     /coded_by="NM_001170576.2:32..442"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:295217"
                     /db_xref="RGD:1560377"
ORIGIN      
        1 maaagsaavs gagtpvagpt grdlfaegll eflrpavqql dshvhavres qvelreqidn
       61 latelcrine dqkvaldldp yvkkllnarr rvvlvnnilq naqerlrrln hsvaketarr
      121 ramldsgvyp pgspsk
//
LOCUS       NP_001128100             396 aa            linear   ROD 28-APR-2025
DEFINITION  S100P-binding protein [Rattus norvegicus].
ACCESSION   NP_001128100 XP_001060653 XP_575913
VERSION     NP_001128100.1
DBSOURCE    REFSEQ: accession NM_001134628.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Dowen,S.E., Crnogorac-Jurcevic,T., Gangeswaran,R., Hansen,M.,
            Eloranta,J.J., Bhakta,V., Brentnall,T.A., Luttges,J., Kloppel,G.
            and Lemoine,N.R.
  TITLE     Expression of S100P and its novel binding partner S100PBPR in early
            pancreatic cancer
  JOURNAL   Am J Pathol 166 (1), 81-92 (2005)
   PUBMED   15632002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 4, 2008 this sequence version replaced
            XP_001060653.1, XP_575913.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.29134.1,
                                           SRR26360194.436156.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..396
                     /product="S100P-binding protein"
                     /calculated_mol_wt=44280
     Region          21..382
                     /region_name="S100PBPR"
                     /note="S100P-binding protein; pfam15427"
                     /db_xref="CDD:464711"
     CDS             1..396
                     /gene="S100pbp"
                     /gene_synonym="RGD1564943"
                     /coded_by="NM_001134628.2:240..1430"
                     /db_xref="GeneID:500551"
                     /db_xref="RGD:1564943"
ORIGIN      
        1 mtcsllpseq ssgtsflpkd nasfswgssd edelddslle fsdgeeddgh fsfteeeiem
       61 llkdddgghn eyrarksqil phtpqensly slgpaaetpg flklpqlsps vghgptpsks
      121 lnrhfvlekn likvtvvapf nptvcdpvld kdkidssket ekpaslqeqt reddlhpnes
      181 krctepegvs pnnsawdgpl lsspsnnnie qtasdknipe skkptpvfsq isnhsevpnr
      241 knsgshksgc evripvvsss snrhafdkds geakgerrlg kvipvlqtrt rmfsqsdlek
      301 qkdiylskvi ahiedpgdsn qgalgeldal mdqvhmqnpd wqhpsdlttr nyarfrqrpl
      361 qryslsqwvd rnkrshhrfq rlpdfsyspy vsphpq
//
LOCUS       NP_001030027             569 aa            linear   ROD 28-APR-2025
DEFINITION  probable G-protein coupled receptor 153 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001030027
VERSION     NP_001030027.1
DBSOURCE    REFSEQ: accession NM_001034855.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Sreedharan,S., Almen,M.S., Carlini,V.P., Haitina,T.,
            Stephansson,O., Sommer,W.H., Heilig,M., de Barioglio,S.R.,
            Fredriksson,R. and Schioth,H.B.
  TITLE     The G protein coupled receptor Gpr153 shares common evolutionary
            origin with Gpr162 and is highly expressed in central regions
            including the thalamus, cerebellum and the arcuate nucleus
  JOURNAL   FEBS J 278 (24), 4881-4894 (2011)
   PUBMED   21981325
  REMARK    GeneRIF: antisense oligodeoxynucleotide knockdown of Gpr153 caused
            a slight reduction in food intake and elevated plus maze test
            showed significant reduction in the percentage of time spent in
            centre square, which points towards probable role in decision
            making.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105872.1, SRR21887623.125130.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..569
                     /product="probable G-protein coupled receptor 153 isoform
                     2"
                     /note="probable G-protein coupled receptor 153"
                     /calculated_mol_wt=61415
     Region          8..248
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          10..34
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320573"
     Region          43..63
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320573"
     Region          84..106
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320573"
     Region          129..145
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320573"
     Region          168..191
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320573"
     Region          216..241
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320573"
     CDS             1..569
                     /gene="Gpr153"
                     /coded_by="NM_001034855.2:376..2085"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:619550"
                     /db_xref="RGD:1564170"
ORIGIN      
        1 msderrlpgs avgwlacggl sllanawgil svgakqkkwk plefllctla athmlnvavp
       61 iatyavvqlr rqrpdyewne glckvfvstf ytltlatcfs vtsisyhrmw mvrwpvnyrl
      121 snakkqavht vmgiwmvsfi lsalpavgwh dtserfythg crfivaeigl gfgvcflllv
      181 ggsvamgvvc taialfqtla tqvvsfsslr adasapwmvl cvlwcsvtqa lllplflwtc
      241 dryradlkav wekcvalman dedsdnetsl egsispdlvl ersldyggdf valdrmakye
      301 lsalegglpq lyplrplqed rmqylqgagr hrcgfpggqp cfspagcsqv pptrrfshdd
      361 advwaaiplp tflprwssge dlaalahlml pagsdrrrgs llaftedapp frprrrsaes
      421 llslqpssld ggprraqdsp pgspcrrpgp garsasvsll pdafaltafd repqplrrvp
      481 aparpfpaap dgtetaeipt ppggraqrsq grraarahag plqsslsasw gepggllaag
      541 cgstssflss psessgyvtl hsdslgsas
//
LOCUS       NP_001426064             480 aa            linear   ROD 28-APR-2025
DEFINITION  endothelial transcription factor GATA-2 [Rattus norvegicus].
ACCESSION   NP_001426064 XP_017447969
VERSION     NP_001426064.1
DBSOURCE    REFSEQ: accession NM_001439135.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Whigham,C.A., MacDonald,T.M., Walker,S.P., Pritchard,N.,
            Hannan,N.J., Cannon,P., Nguyen,T.V., Hastie,R., Tong,S. and
            Kaitu'u-Lino,T.J.
  TITLE     Circulating GATA2 mRNA is decreased among women destined to develop
            preeclampsia and may be of endothelial origin
  JOURNAL   Sci Rep 9 (1), 235 (2019)
   PUBMED   30659233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Hartmann,D., Fiedler,J., Sonnenschein,K., Just,A., Pfanne,A.,
            Zimmer,K., Remke,J., Foinquinos,A., Butzlaff,M., Schimmel,K.,
            Maegdefessel,L., Hilfiker-Kleiner,D., Lachmann,N., Schober,A.,
            Froese,N., Heineke,J., Bauersachs,J., Batkai,S. and Thum,T.
  TITLE     MicroRNA-Based Therapy of GATA2-Deficient Vascular Disease
  JOURNAL   Circulation 134 (24), 1973-1990 (2016)
   PUBMED   27780851
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Peters,I., Dubrowinskaja,N., Tezval,H., Kramer,M.W., von Klot,C.A.,
            Hennenlotter,J., Stenzl,A., Scherer,R., Kuczyk,M.A. and Serth,J.
  TITLE     Decreased mRNA expression of GATA1 and GATA2 is associated with
            tumor aggressiveness and poor outcome in clear cell renal cell
            carcinoma
  JOURNAL   Target Oncol 10 (2), 267-275 (2015)
   PUBMED   25230694
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Hou,H.A., Lin,Y.C., Kuo,Y.Y., Chou,W.C., Lin,C.C., Liu,C.Y.,
            Chen,C.Y., Lin,L.I., Tseng,M.H., Huang,C.F., Chiang,Y.C., Liu,M.C.,
            Liu,C.W., Tang,J.L., Yao,M., Huang,S.Y., Ko,B.S., Hsu,S.C.,
            Wu,S.J., Tsay,W., Chen,Y.C. and Tien,H.F.
  TITLE     GATA2 mutations in patients with acute myeloid leukemia-paired
            samples analyses show that the mutation is unstable during disease
            evolution
  JOURNAL   Ann Hematol 94 (2), 211-221 (2015)
   PUBMED   25241285
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Choi,M., Wang,S.E., Ko,S.Y., Kang,H.J., Chae,S.Y., Lee,S.H.,
            Kim,Y.S., Duman,R.S. and Son,H.
  TITLE     Overexpression of human GATA-1 and GATA-2 interferes with spine
            formation and produces depressive behavior in rats
  JOURNAL   PLoS One 9 (10), e109253 (2014)
   PUBMED   25340772
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Zhou,Y., Lim,K.C., Onodera,K., Takahashi,S., Ohta,J., Minegishi,N.,
            Tsai,F.Y., Orkin,S.H., Yamamoto,M. and Engel,J.D.
  TITLE     Rescue of the embryonic lethal hematopoietic defect reveals a
            critical role for GATA-2 in urogenital development
  JOURNAL   EMBO J 17 (22), 6689-6700 (1998)
   PUBMED   9822612
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Gordon,D.F., Lewis,S.R., Haugen,B.R., James,R.A., McDermott,M.T.,
            Wood,W.M. and Ridgway,E.C.
  TITLE     Pit-1 and GATA-2 interact and functionally cooperate to activate
            the thyrotropin beta-subunit promoter
  JOURNAL   J Biol Chem 272 (39), 24339-24347 (1997)
   PUBMED   9305891
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Ma,G.T., Roth,M.E., Groskopf,J.C., Tsai,F.Y., Orkin,S.H.,
            Grosveld,F., Engel,J.D. and Linzer,D.I.
  TITLE     GATA-2 and GATA-3 regulate trophoblast-specific gene expression in
            vivo
  JOURNAL   Development 124 (4), 907-914 (1997)
   PUBMED   9043071
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Ng,Y.K., George,K.M., Engel,J.D. and Linzer,D.I.
  TITLE     GATA factor activity is required for the trophoblast-specific
            transcriptional regulation of the mouse placental lactogen I gene
  JOURNAL   Development 120 (11), 3257-3266 (1994)
   PUBMED   7720565
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Tsai,F.Y., Keller,G., Kuo,F.C., Weiss,M., Chen,J., Rosenblatt,M.,
            Alt,F.W. and Orkin,S.H.
  TITLE     An early haematopoietic defect in mice lacking the transcription
            factor GATA-2
  JOURNAL   Nature 371 (6494), 221-226 (1994)
   PUBMED   8078582
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 28, 2025 this sequence version replaced XP_017447969.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212304.1, SRR26643297.16780.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..480
                     /product="endothelial transcription factor GATA-2"
                     /note="GATA-bindning protein 2"
                     /calculated_mol_wt=50333
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Site            86
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Region          166..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924Y4.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Region          294..344
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Site            order(295,298,316,319)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238123"
     Site            order(304..305,307,316..326,343)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Region          349..398
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Site            order(349,352,370,373)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238123"
     Site            order(358..359,361,370..380,396,398)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Region          457..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924Y4.1)"
     CDS             1..480
                     /gene="Gata2"
                     /coded_by="NM_001439135.1:466..1908"
                     /db_xref="GeneID:25159"
                     /db_xref="RGD:2664"
ORIGIN      
        1 mevapeqprw mahpavlnaq hpdshhpgla hnymepaqll ppdevdvffn hldsqgnpyy
       61 anpahararv syspaharlt ggqmcrphll hspglpwldg gkaalsaaaa hhhspwtvsp
      121 fsktplhpsa agapggplsv ypgaaggsgg gsgssvaslt ptaahsgshl fgfpptppke
      181 vspdpsttga aspaspsagg svargedkdg vkyqvslses mkmeggsplr pglapmgtqp
      241 athhpiptyp syvpasahey gsglfhpggf lggpassftp kqrskarscs egrecvncga
      301 tatplwrrdg tghylcnacg lyhkmngqnr plikpkrrls aarragtcca ncqtttttlw
      361 rrnangdpvc nacglyyklh nvnrpltmkk egiqtrnrkm sskskkskkg aecfeelskc
      421 mqeksspfsa aalaghmapv ghlppfshsg hilptptpih pssslsfghp hpssmvtamg
//
LOCUS       NP_001037740             279 aa            linear   ROD 28-APR-2025
DEFINITION  very long chain fatty acid elongase 1 [Rattus norvegicus].
ACCESSION   NP_001037740 XP_001053380
VERSION     NP_001037740.1
DBSOURCE    REFSEQ: accession NM_001044275.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Sassa,T., Ohno,Y., Suzuki,S., Nomura,T., Nishioka,C., Kashiwagi,T.,
            Hirayama,T., Akiyama,M., Taguchi,R., Shimizu,H., Itohara,S. and
            Kihara,A.
  TITLE     Impaired epidermal permeability barrier in mice lacking elovl1, the
            gene responsible for very-long-chain fatty acid production
  JOURNAL   Mol Cell Biol 33 (14), 2787-2796 (2013)
   PUBMED   23689133
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Ohno,Y., Suto,S., Yamanaka,M., Mizutani,Y., Mitsutake,S.,
            Igarashi,Y., Sassa,T. and Kihara,A.
  TITLE     ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
            synthesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (43), 18439-18444 (2010)
   PUBMED   20937905
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Ofman,R., Dijkstra,I.M., van Roermund,C.W., Burger,N.,
            Turkenburg,M., van Cruchten,A., van Engen,C.E., Wanders,R.J. and
            Kemp,S.
  TITLE     The role of ELOVL1 in very long-chain fatty acid homeostasis and
            X-linked adrenoleukodystrophy
  JOURNAL   EMBO Mol Med 2 (3), 90-97 (2010)
   PUBMED   20166112
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Leonard,A.E., Bobik,E.G., Dorado,J., Kroeger,P.E., Chuang,L.T.,
            Thurmond,J.M., Parker-Barnes,J.M., Das,T., Huang,Y.S. and
            Mukerji,P.
  TITLE     Cloning of a human cDNA encoding a novel enzyme involved in the
            elongation of long-chain polyunsaturated fatty acids
  JOURNAL   Biochem J 350 Pt 3 (Pt 3), 765-770 (2000)
   PUBMED   10970790
REFERENCE   6  (residues 1 to 279)
  AUTHORS   LORCH,J.
  TITLE     Note on the cytological localization of alkaline phosphatase
  JOURNAL   Q J Microsc Sci 88 (Pt 2), 159-161 (1947)
   PUBMED   20253178
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001053380.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085795.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..279
                     /product="very long chain fatty acid elongase 1"
                     /EC_number="2.3.1.199"
                     /note="elongation of very long chain fatty acids protein
                     1; elongation of very long chain fatty acids (FEN1/Elo2,
                     SUR4/Elo3, yeast)-like 1"
                     /calculated_mol_wt=32508
     Region          23..262
                     /region_name="ELO"
                     /note="GNS1/SUR4 family; pfam01151"
                     /db_xref="CDD:460083"
     CDS             1..279
                     /gene="Elovl1"
                     /coded_by="NM_001044275.2:153..992"
                     /db_xref="GeneID:679532"
                     /db_xref="RGD:1587151"
ORIGIN      
        1 meavvnlyqe lmkcadpriq nyplmgspll itsilltyvy fvlslgprim anrkpfqlrg
       61 fmivynfslv tlslyivyef lmsgwlstyt wrcdpvdfsn npealrmvrv awlfmlskvi
      121 elmdtvifil rkkdgqvtfl hvfhhsvlpw swwwgikiap ggmgsfhami nssvhvvmyl
      181 yyglsalgpv aqpylwwkkh mtaiqliqfv lvslhisqyy fmpscnyqyp iiihliwmyg
      241 tiffilfsnf wyhsytkgkr lpravqqnga aasmkvkan
//
LOCUS       NP_001426067             480 aa            linear   ROD 28-APR-2025
DEFINITION  endothelial transcription factor GATA-2 [Rattus norvegicus].
ACCESSION   NP_001426067 XP_038963019
VERSION     NP_001426067.1
DBSOURCE    REFSEQ: accession NM_001439138.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Whigham,C.A., MacDonald,T.M., Walker,S.P., Pritchard,N.,
            Hannan,N.J., Cannon,P., Nguyen,T.V., Hastie,R., Tong,S. and
            Kaitu'u-Lino,T.J.
  TITLE     Circulating GATA2 mRNA is decreased among women destined to develop
            preeclampsia and may be of endothelial origin
  JOURNAL   Sci Rep 9 (1), 235 (2019)
   PUBMED   30659233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Hartmann,D., Fiedler,J., Sonnenschein,K., Just,A., Pfanne,A.,
            Zimmer,K., Remke,J., Foinquinos,A., Butzlaff,M., Schimmel,K.,
            Maegdefessel,L., Hilfiker-Kleiner,D., Lachmann,N., Schober,A.,
            Froese,N., Heineke,J., Bauersachs,J., Batkai,S. and Thum,T.
  TITLE     MicroRNA-Based Therapy of GATA2-Deficient Vascular Disease
  JOURNAL   Circulation 134 (24), 1973-1990 (2016)
   PUBMED   27780851
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Peters,I., Dubrowinskaja,N., Tezval,H., Kramer,M.W., von Klot,C.A.,
            Hennenlotter,J., Stenzl,A., Scherer,R., Kuczyk,M.A. and Serth,J.
  TITLE     Decreased mRNA expression of GATA1 and GATA2 is associated with
            tumor aggressiveness and poor outcome in clear cell renal cell
            carcinoma
  JOURNAL   Target Oncol 10 (2), 267-275 (2015)
   PUBMED   25230694
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Hou,H.A., Lin,Y.C., Kuo,Y.Y., Chou,W.C., Lin,C.C., Liu,C.Y.,
            Chen,C.Y., Lin,L.I., Tseng,M.H., Huang,C.F., Chiang,Y.C., Liu,M.C.,
            Liu,C.W., Tang,J.L., Yao,M., Huang,S.Y., Ko,B.S., Hsu,S.C.,
            Wu,S.J., Tsay,W., Chen,Y.C. and Tien,H.F.
  TITLE     GATA2 mutations in patients with acute myeloid leukemia-paired
            samples analyses show that the mutation is unstable during disease
            evolution
  JOURNAL   Ann Hematol 94 (2), 211-221 (2015)
   PUBMED   25241285
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Choi,M., Wang,S.E., Ko,S.Y., Kang,H.J., Chae,S.Y., Lee,S.H.,
            Kim,Y.S., Duman,R.S. and Son,H.
  TITLE     Overexpression of human GATA-1 and GATA-2 interferes with spine
            formation and produces depressive behavior in rats
  JOURNAL   PLoS One 9 (10), e109253 (2014)
   PUBMED   25340772
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Zhou,Y., Lim,K.C., Onodera,K., Takahashi,S., Ohta,J., Minegishi,N.,
            Tsai,F.Y., Orkin,S.H., Yamamoto,M. and Engel,J.D.
  TITLE     Rescue of the embryonic lethal hematopoietic defect reveals a
            critical role for GATA-2 in urogenital development
  JOURNAL   EMBO J 17 (22), 6689-6700 (1998)
   PUBMED   9822612
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Gordon,D.F., Lewis,S.R., Haugen,B.R., James,R.A., McDermott,M.T.,
            Wood,W.M. and Ridgway,E.C.
  TITLE     Pit-1 and GATA-2 interact and functionally cooperate to activate
            the thyrotropin beta-subunit promoter
  JOURNAL   J Biol Chem 272 (39), 24339-24347 (1997)
   PUBMED   9305891
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Ma,G.T., Roth,M.E., Groskopf,J.C., Tsai,F.Y., Orkin,S.H.,
            Grosveld,F., Engel,J.D. and Linzer,D.I.
  TITLE     GATA-2 and GATA-3 regulate trophoblast-specific gene expression in
            vivo
  JOURNAL   Development 124 (4), 907-914 (1997)
   PUBMED   9043071
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Ng,Y.K., George,K.M., Engel,J.D. and Linzer,D.I.
  TITLE     GATA factor activity is required for the trophoblast-specific
            transcriptional regulation of the mouse placental lactogen I gene
  JOURNAL   Development 120 (11), 3257-3266 (1994)
   PUBMED   7720565
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Tsai,F.Y., Keller,G., Kuo,F.C., Weiss,M., Chen,J., Rosenblatt,M.,
            Alt,F.W. and Orkin,S.H.
  TITLE     An early haematopoietic defect in mice lacking the transcription
            factor GATA-2
  JOURNAL   Nature 371 (6494), 221-226 (1994)
   PUBMED   8078582
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 28, 2025 this sequence version replaced XP_038963019.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.16784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..480
                     /product="endothelial transcription factor GATA-2"
                     /note="GATA-bindning protein 2"
                     /calculated_mol_wt=50333
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Site            86
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Region          166..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924Y4.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23769; propagated from
                     UniProtKB/Swiss-Prot (Q924Y4.1)"
     Region          294..344
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Site            order(295,298,316,319)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238123"
     Site            order(304..305,307,316..326,343)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Region          349..398
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Site            order(349,352,370,373)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238123"
     Site            order(358..359,361,370..380,396,398)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Region          457..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q924Y4.1)"
     CDS             1..480
                     /gene="Gata2"
                     /coded_by="NM_001439138.1:674..2116"
                     /db_xref="GeneID:25159"
                     /db_xref="RGD:2664"
ORIGIN      
        1 mevapeqprw mahpavlnaq hpdshhpgla hnymepaqll ppdevdvffn hldsqgnpyy
       61 anpahararv syspaharlt ggqmcrphll hspglpwldg gkaalsaaaa hhhspwtvsp
      121 fsktplhpsa agapggplsv ypgaaggsgg gsgssvaslt ptaahsgshl fgfpptppke
      181 vspdpsttga aspaspsagg svargedkdg vkyqvslses mkmeggsplr pglapmgtqp
      241 athhpiptyp syvpasahey gsglfhpggf lggpassftp kqrskarscs egrecvncga
      301 tatplwrrdg tghylcnacg lyhkmngqnr plikpkrrls aarragtcca ncqtttttlw
      361 rrnangdpvc nacglyyklh nvnrpltmkk egiqtrnrkm sskskkskkg aecfeelskc
      421 mqeksspfsa aalaghmapv ghlppfshsg hilptptpih pssslsfghp hpssmvtamg
//
LOCUS       NP_001417281             493 aa            linear   ROD 28-APR-2025
DEFINITION  solute carrier family 22 member 22 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001417281 XP_063119325
VERSION     NP_001417281.1
DBSOURCE    REFSEQ: accession NM_001430352.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Hatano,R., Onoe,K., Obara,M., Matsubara,M., Kanai,Y., Muto,S. and
            Asano,S.
  TITLE     Sex hormones induce a gender-related difference in renal expression
            of a novel prostaglandin transporter, OAT-PG, influencing basal
            PGE2 concentration
  JOURNAL   Am J Physiol Renal Physiol 302 (3), F342-F349 (2012)
   PUBMED   22031854
  REMARK    GeneRIF: OAT-PG is involved in local PGE(2) clearance in the renal
            cortex.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On May 10, 2024 this sequence version replaced XP_063119325.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.18369.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..493
                     /product="solute carrier family 22 member 22 isoform 3"
                     /note="prostaglandin transporter OAT-PG; solute carrier
                     family 22 (organic cation transporter), member 22"
                     /calculated_mol_wt=55185
     Region          47..454
                     /region_name="MFS_OAT"
                     /note="Organic anion transporters of the Major Facilitator
                     Superfamily of transporters; cd17374"
                     /db_xref="CDD:340932"
     Site            order(64..65,68..69,72,98,148..149,151..153,156,172,
                     175..176,179,295,298..299,302..304,307,327,331,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340932"
     CDS             1..493
                     /gene="Slc22a22"
                     /gene_synonym="oat-pg; RGD1304605"
                     /coded_by="NM_001430352.1:139..1620"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:299944"
                     /db_xref="RGD:1304605"
ORIGIN      
        1 mamnltteam mkvsipmgpn qkpeqcrrfr hpqwqfidsn istsnstele tepcldgwty
       61 dhsvftstiv tewdlvcdfq sfkyyaqats laghfvaapf cgiisdrfgr kpllmycsla
      121 ygilgtccaf vpnfslycvl rflssasast vgmnclilvl eetsvqwhat vivlsglfss
      181 tglaglggla yvlsdwhliq ltsalpyfif filfcwvpes arwlmitgkt dqalkelqri
      241 asingkkdia qnlttedlrs kvkedvcstv khfsikdiii npmirkivlc yssvlfaelf
      301 sifgllldvh mlgknifvtq illgvidips ksltyfilrn vrrrpliafl lfatggciti
      361 tmflsedmyv lrlaifilgk gcfaafisin taycnelspv plrstlngiy isvarlasvl
      421 saltlvtrky fvllpmifcg vlpivatini yflpetfnhp itdtikdmek rnrlmsknis
      481 ekegqdflet tnc
//
LOCUS       NP_001421160            1065 aa            linear   ROD 28-APR-2025
DEFINITION  pumilio homolog 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001421160 XP_006239942
VERSION     NP_001421160.1
DBSOURCE    REFSEQ: accession NM_001434231.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1065)
  AUTHORS   Yu,S., Wang,M., Xie,Y., Wang,B. and Xu,Y.
  TITLE     MiR-495-3p promotes cardiac hypertrophy by targeting Pum2
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (8), 116-120 (2024)
   PUBMED   39262254
  REMARK    GeneRIF: MiR-495-3p promotes cardiac hypertrophy by targeting Pum2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1065)
  AUTHORS   Yoon,D.S., Choi,Y., Lee,K.M., Ko,E.A., Kim,E.J., Park,K.H. and
            Lee,J.W.
  TITLE     Downregulation of the RNA-binding protein PUM2 facilitates
            MSC-driven bone regeneration and prevents OVX-induced bone loss
  JOURNAL   J Biomed Sci 30 (1), 26 (2023)
   PUBMED   37088847
  REMARK    GeneRIF: Downregulation of the RNA-binding protein PUM2 facilitates
            MSC-driven bone regeneration and prevents OVX-induced bone loss.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1065)
  AUTHORS   Cao,Y., Liu,C., Wang,Q., Wang,W., Tao,E. and Wan,L.
  TITLE     Pum2 mediates Sirt1 mRNA decay and exacerbates
            hypoxia/reoxygenation-induced cardiomyocyte apoptosis
  JOURNAL   Exp Cell Res 393 (1), 112058 (2020)
   PUBMED   32437714
  REMARK    GeneRIF: Pum2 mediates Sirt1 mRNA decay and exacerbates
            hypoxia/reoxygenation-induced cardiomyocyte apoptosis.
REFERENCE   4  (residues 1 to 1065)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
  REMARK    GeneRIF: These results reveal that Pum2 shapes axonal
            transcriptomes by preventing the transport of Pumilio-binding
            elements -containing mRNAs into axons
REFERENCE   5  (residues 1 to 1065)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   6  (residues 1 to 1065)
  AUTHORS   Fiore,R., Khudayberdiev,S., Christensen,M., Siegel,G.,
            Flavell,S.W., Kim,T.K., Greenberg,M.E. and Schratt,G.
  TITLE     Mef2-mediated transcription of the miR379-410 cluster regulates
            activity-dependent dendritogenesis by fine-tuning Pumilio2 protein
            levels
  JOURNAL   EMBO J 28 (6), 697-710 (2009)
   PUBMED   19197241
  REMARK    GeneRIF: Mef2-induced expression of at least three individual
            miRNAs of the miR379-410 cluster is required for activity-dependent
            dendritic outgrowth of hippocampal neurons.
REFERENCE   7  (residues 1 to 1065)
  AUTHORS   Ginter-Matuszewska,B., Spik,A., Rembiszewska,A., Koyias,C.,
            Kupryjanczyk,J. and Jaruzelska,J.
  TITLE     The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1
            proteins in human male germ cells
  JOURNAL   Mol Hum Reprod 15 (3), 173-179 (2009)
   PUBMED   19168546
REFERENCE   8  (residues 1 to 1065)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1065)
  AUTHORS   Vessey,J.P., Vaccani,A., Xie,Y., Dahm,R., Karra,D., Kiebler,M.A.
            and Macchi,P.
  TITLE     Dendritic localization of the translational repressor Pumilio 2 and
            its contribution to dendritic stress granules
  JOURNAL   J Neurosci 26 (24), 6496-6508 (2006)
   PUBMED   16775137
REFERENCE   10 (residues 1 to 1065)
  AUTHORS   White,E.K., Moore-Jarrett,T. and Ruley,H.E.
  TITLE     PUM2, a novel murine puf protein, and its consensus RNA-binding
            site
  JOURNAL   RNA 7 (12), 1855-1866 (2001)
   PUBMED   11780640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 24, 2024 this sequence version replaced XP_006239942.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.34469.1,
                                           SRR26643292.25472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1065
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..1065
                     /product="pumilio homolog 2 isoform 2"
                     /note="pumilio 2"
                     /calculated_mol_wt=114017
     Region          722..1043
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(778..779,782,814..815,818,851,854,886..887,890,
                     919..920,922..923,926,955..956,958..959,962,998..999,
                     1001..1002,1005,1035,1038)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1065
                     /gene="Pum2"
                     /coded_by="NM_001434231.1:238..3435"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298874"
                     /db_xref="RGD:1311024"
ORIGIN      
        1 mnhdfqalal esrgmgellp tkkfwepdds tkdgqkgifl gddewretaw gtshhsmsqp
       61 imvqrrsgqs fhgnsevnai lsprsesggl gvsmveyvls sspadkldsr frkgtfgtrd
      121 aetdgpekgd qkgkaspfee dqnrdlkqdd edskingrgl pngmdadckd fnrtpgsrqa
      181 sptevverlg pstnppeglg plpnptankp lveefsnpet qnldamdqvg ldslqfdypg
      241 nqvpmdssga tvglfdynsq qqlfqrtnal tvqqltaaqq qqyalaaaqq phiagvfsag
      301 lapaafvpnp yiisaappgt dpytaaglaa aatlagpavv ppqyygvpwg vypanlfqqq
      361 aaaaasntan qqaasqaqpg qqqvlrpgag qrpitpsqgq qgqqaeslaa aaaanptlaf
      421 gqslaagmpg yqvlaptayy dqtgalvvgp gartglgapv rlmaptpvli ssaaaqaaaa
      481 aaaaggtans ltgstnglfr pigtqppqqq qqqqpstnlq snsfygsssl tnssqssslf
      541 shgpgqpgsa slgfgsgssl gaaigsalsg fgssvgssas ssatrresls tssdlykrss
      601 sslapigqpf ynslgfsssp spigmplpsq tpghsltppp slsshgssss lhlggltngs
      661 gryisaapga eakyrsasst sslfssssql fppsrlrynr sdimpsgrsr lledfrnnrf
      721 pnlqlrdlmg hivefsqdqh gsrfiqqkle ratpaerqmv fneivqaayq lmtdvfgnyv
      781 iqkffefgsl dqklalanri rghvlplalq mygcrviqka lesissdqqs emvkeldghv
      841 lkcvkdqngn hvvqkciecv qpqslqfiid afkgqvfvls thpygcrviq rilehctaeq
      901 tlpileelhq hteqlvqdqy gnyviqhvle hgrpedkski vseirgkvla lsqhkfasnv
      961 vekcvthasr aerallidev ccqndgphsa lytmmkdqya nyvvqkmidm aepaqrkiim
     1021 hkirphittl rkytygkhil aklekyylkn spdlgpiggp pngml
//
LOCUS       NP_001101210             932 aa            linear   ROD 28-APR-2025
DEFINITION  catenin delta-1 isoform c [Rattus norvegicus].
ACCESSION   NP_001101210 XP_001064294 XP_242062
VERSION     NP_001101210.1
DBSOURCE    REFSEQ: accession NM_001107740.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Xiao,Z.P., Zhao,J.L., Rong,W.L., Jiang,J.W. and Li,M.H.
  TITLE     Role of Vascular Endothelial-Cadherin and p120-Catenin in the
            Formation of Experimental Intracranial Aneurysm in Animals
  JOURNAL   World Neurosurg 128, e177-e184 (2019)
   PUBMED   30995547
  REMARK    GeneRIF: Decreased expression of p120-catenin was detected in
            intracranial aneurysm endothelium.
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Caldwell,J.M., Collins,M.H., Kemme,K.A., Sherrill,J.D., Wen,T.,
            Rochman,M., Stucke,E.M., Amin,L., Tai,H., Putnam,P.E.,
            Jimenez-Dalmaroni,M.J., Wormald,M.R., Porollo,A., Abonia,J.P. and
            Rothenberg,M.E.
  TITLE     Cadherin 26 is an alpha integrin-binding epithelial receptor
            regulated during allergic inflammation
  JOURNAL   Mucosal Immunol 10 (5), 1190-1201 (2017)
   PUBMED   28051089
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Jiang,Y., Liao,L., Shrestha,C., Ji,S., Chen,Y., Peng,J., Wang,L.,
            Liao,E. and Xie,Z.
  TITLE     Reduced expression of E-cadherin and p120-catenin and elevated
            expression of PLC-gamma1 and PIKE are associated with
            aggressiveness of oral squamous cell carcinoma
  JOURNAL   Int J Clin Exp Pathol 8 (8), 9042-9051 (2015)
   PUBMED   26464646
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Ranchoux,B., Antigny,F., Rucker-Martin,C., Hautefort,A.,
            Pechoux,C., Bogaard,H.J., Dorfmuller,P., Remy,S., Lecerf,F.,
            Plante,S., Chat,S., Fadel,E., Houssaini,A., Anegon,I., Adnot,S.,
            Simonneau,G., Humbert,M., Cohen-Kaminsky,S. and Perros,F.
  TITLE     Endothelial-to-mesenchymal transition in pulmonary hypertension
  JOURNAL   Circulation 131 (11), 1006-1018 (2015)
   PUBMED   25593290
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 932)
  AUTHORS   Chen,Y.M., Lee,N.P., Mruk,D.D., Lee,W.M. and Cheng,C.Y.
  TITLE     Fer kinase/FerT and adherens junction dynamics in the testis: an in
            vitro and in vivo study
  JOURNAL   Biol Reprod 69 (2), 656-672 (2003)
   PUBMED   12700184
REFERENCE   7  (residues 1 to 932)
  AUTHORS   Katafiasz,B.J., Nieman,M.T., Wheelock,M.J. and Johnson,K.R.
  TITLE     Characterization of cadherin-24, a novel alternatively spliced type
            II cadherin
  JOURNAL   J Biol Chem 278 (30), 27513-27519 (2003)
   PUBMED   12734196
REFERENCE   8  (residues 1 to 932)
  AUTHORS   Chauvet,N., Prieto,M., Fabre,C., Noren,N.K. and Privat,A.
  TITLE     Distribution of p120 catenin during rat brain development:
            potential role in regulation of cadherin-mediated adhesion and
            actin cytoskeleton organization
  JOURNAL   Mol Cell Neurosci 22 (4), 467-486 (2003)
   PUBMED   12727444
REFERENCE   9  (residues 1 to 932)
  AUTHORS   Holsinger,L.J., Ward,K., Duffield,B., Zachwieja,J. and Jallal,B.
  TITLE     The transmembrane receptor protein tyrosine phosphatase DEP1
            interacts with p120(ctn)
  JOURNAL   Oncogene 21 (46), 7067-7076 (2002)
   PUBMED   12370829
REFERENCE   10 (residues 1 to 932)
  AUTHORS   Golenhofen,N. and Drenckhahn,D.
  TITLE     The catenin, p120ctn, is a common membrane-associated protein in
            various epithelial and non-epithelial cells and tissues
  JOURNAL   Histochem Cell Biol 114 (2), 147-155 (2000)
   PUBMED   11052263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064294.1, XP_242062.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.12193.1,
                                           SRR26643298.16765.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760476 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..932
                     /product="catenin delta-1 isoform c"
                     /note="catenin src; catenin (cadherin associated protein),
                     delta 1; p120 catenin"
                     /calculated_mol_wt=103941
     Region          368..393
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(384,388,392,426,430,434,470,474,478)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          397..437
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          401..437
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          440..481
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          444..479
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          486..537
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          650..687
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          697..732
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          697..731
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          787..823
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..932
                     /gene="Ctnnd1"
                     /gene_synonym="Catns; P120"
                     /coded_by="NM_001107740.2:388..3186"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:311163"
                     /db_xref="RGD:1305643"
ORIGIN      
        1 mddsevesta silasvkeqe aqfekltral eeerrhvsaq lervrvspqd anslmangtl
       61 trrhqngrfv gdadlerqkf sdlklngpqd hnhllystip rmqepgqive tyteedpega
      121 msvvsvetsd dgttrrtett vkkvvktmtt rtvqpvpmgp dglpvdasav snnyiqtlgr
      181 dfrkngnggp gpyvgqagta tlprnfhypp dgygrhyedg ypggsdnygs lsrvtrieer
      241 yrpsmegyra psrqdvygpq pqvrvggssv dlhrfhpepy gleddqrsmg yddldygmms
      301 dygtarrtgt psdprrrlrs yedmigeevp pdqyywapla qhergslasl dslrkgmppp
      361 pnwrqpelpe viamlgfrld avksnaaayl qhlcyrndkv ktdvrklkgi pilvglldhp
      421 kkevhlgacg alknisfgrd qdnkiaiknc dgvpalvrll rkardmdlte vitgtlwnls
      481 shdsikmeiv dhalhaltde viiphsgwer epnedckprh iewesvltnt agclrnvsse
      541 rsearrklre cdglvdalif ivqaeigqkd sdsklvencv cllrnlsyqv hreipqaery
      601 qealpsvans tgphaascfg akkgkgkkpt edpandtvdf pkrtspargy ellfqpevvr
      661 iyisllkesk tpaileasag aiqnlcagrw tygryirsal rqekalsaia dlltseherv
      721 vkaasgalrn lavdarnkel igkhaipnlv knlpggqqns swnfsedtvv silntinevi
      781 aenleaakkl retqgieklv linksgnrse kevraaalvl qtiwgykelr kplekegwkk
      841 sdfqvnlnna srsqsshsyd dstlplidrn qksdkkpdre eipmsnmgsn tksldnnyst
      901 lnergdhnrt ldrsgdlgdm eplkgaplmq ki
//
LOCUS       NP_001419887             535 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain containing 149 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001419887 XP_038948685
VERSION     NP_001419887.1
DBSOURCE    REFSEQ: accession NM_001432958.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Aug 5, 2024 this sequence version replaced XP_038948685.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.54472.1,
                                           SRR26360194.1747355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..535
                     /product="coiled-coil domain containing 149 isoform 1"
                     /note="coiled-coil domain-containing protein 149"
                     /calculated_mol_wt=60055
     Region          21..333
                     /region_name="CC149"
                     /note="Coiled-coil domain-containing protein 149-A;
                     pfam09789"
                     /db_xref="CDD:462902"
     CDS             1..535
                     /gene="Ccdc149"
                     /coded_by="NM_001432958.1:146..1753"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:688939"
                     /db_xref="RGD:1582968"
ORIGIN      
        1 mdgdrtesdw qglvseylvc krkleskkea llilskeldt cqqerdqykl manqlrerhq
       61 slkkkyreli dgdpslppek rkqanlaqll resqdrnkhl geeikelrqr lgevqgdnkl
      121 lrmtiakqrl gdeeigvrhf aaheredlve qlerakeqie slehdlqasv delqdvkeer
      181 asyqdkvdrl nqelnhilgg henriidvda lcmenrylqe rlkqlheevs llksniakyk
      241 nalerrknsk tqgksnssal tgvlsakqvq dllsedhgcs lpatpqsiad lkslatalle
      301 tiheknmviq hqrqtnrilg nrvaelekkl rtlevsglws lpglsynvsv gfgrgkdtil
      361 lsdqtlptiq kskspllkfv eqpteskesa rdgeiqtqer desraaaeal tvpedagrpa
      421 vsspappsna nqhsdfhhpp vpqplseevn tvggreitql tdgqeatdle evpreaptee
      481 qrcepqpsps slsqeecivt lqdhlpsmqp evkatstggd rgiseggdtr stvqt
//
LOCUS       NP_001389081             538 aa            linear   ROD 28-APR-2025
DEFINITION  brain-specific angiogenesis inhibitor 1-associated protein 2-like
            protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001389081 XP_038935824
VERSION     NP_001389081.1
DBSOURCE    REFSEQ: accession NM_001402152.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Pykalainen,A., Boczkowska,M., Zhao,H., Saarikangas,J., Rebowski,G.,
            Jansen,M., Hakanen,J., Koskela,E.V., Peranen,J., Vihinen,H.,
            Jokitalo,E., Salminen,M., Ikonen,E., Dominguez,R. and
            Lappalainen,P.
  TITLE     Pinkbar is an epithelial-specific BAR domain protein that generates
            planar membrane structures
  JOURNAL   Nat Struct Mol Biol 18 (8), 902-907 (2011)
   PUBMED   21743456
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Veltman,D.M., Auciello,G., Spence,H.J., Machesky,L.M.,
            Rappoport,J.Z. and Insall,R.H.
  TITLE     Functional analysis of Dictyostelium IBARa reveals a conserved role
            of the I-BAR domain in endocytosis
  JOURNAL   Biochem J 436 (1), 45-52 (2011)
   PUBMED   21401524
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Mar 8, 2022 this sequence version replaced XP_038935824.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..538
                     /product="brain-specific angiogenesis inhibitor
                     1-associated protein 2-like protein 2 isoform 1"
                     /note="brain-specific angiogenesis inhibitor 1-associated
                     protein 2-like protein 2; rCG60233-like; BAI1-associated
                     protein 2-like 2"
                     /calculated_mol_wt=59854
     Region          <7..143
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Region          250..308
                     /region_name="SH3_BAIAP2L2"
                     /note="Src Homology 3 domain of Brain-specific
                     Angiogenesis Inhibitor 1-Associated Protein 2-Like 2;
                     cd11914"
                     /db_xref="CDD:212847"
     Site            order(255..256,258,265..266,278..279,284..286,288,
                     298..299,301..304)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212847"
     CDS             1..538
                     /gene="Baiap2l2"
                     /gene_synonym="RGD1308786"
                     /coded_by="NM_001402152.1:308..1924"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:685357"
                     /db_xref="RGD:1595091"
ORIGIN      
        1 mllgwwlsrd teghevqtfh gdllqhmekn tkldmqfikd scqhyeieyr hraanlekcm
       61 selwrmerkr dknaremkes vnrlhaqmqa fvseskraae leekrryrfl aekhlllsnt
      121 flqflgrarg mlqnrvllwk eqseasrsps rahspgllgp algppypsgr ltptrldmpp
      181 rplgeygspr srhgsgsygp epsearsasq lepdrrslpr tpsasslyas ntqrsrsnsf
      241 gerlggggar rvralvshse ganhtllrfs agdvvevlvp eaqngwlygk legssasgwf
      301 peayvkplee mpmnpmnpva pmnsmapmsp mnelpsrsyp lrgshslddl ldrpgnpaas
      361 sdywdsqsrs rtpsrvpsra pspappplpn rrssvgsmga atdvkgyqsl chreaashch
      421 qrplstphpl rrssplgpev aqhthpelfq ptaaavdlrc qaptqgtilt plpqprislr
      481 lglatwsrqk wveaqsswlf lgpkdssrdp asclpssfcl cpdrkhpfsh lcpsctpa
//
LOCUS       NP_001178507            1381 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology-like domain family B member 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001178507 XP_002729962
VERSION     NP_001178507.1
DBSOURCE    REFSEQ: accession NM_001191578.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1381)
  AUTHORS   Nakaya,Y., Sukowati,E.W. and Sheng,G.
  TITLE     Epiblast integrity requires CLASP and Dystroglycan-mediated
            microtubule anchoring to the basal cortex
  JOURNAL   J Cell Biol 202 (4), 637-651 (2013)
   PUBMED   23940118
REFERENCE   2  (residues 1 to 1381)
  AUTHORS   Levi,L., Hanukoglu,I., Raikhinstein,M., Kohen,F. and Koch,Y.
  TITLE     Cloning of LL5, a novel protein encoding cDNA from a rat pituitary
            library
  JOURNAL   Biochim Biophys Acta 1216 (2), 342-344 (1993)
   PUBMED   8241284
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_002729962.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1381
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..1381
                     /product="pleckstrin homology-like domain family B member
                     1 isoform 1"
                     /note="protein LL5-alpha"
                     /calculated_mol_wt=151302
     Region          24..142
                     /region_name="FHA_PHLB1"
                     /note="forkhead associated (FHA) domain found in
                     pleckstrin homology-like domain family B member 1 (PHLDB1)
                     and similar proteins; cd22713"
                     /db_xref="CDD:438765"
     Region          143..>547
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <681..>1240
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          <684..>897
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1259..1374
                     /region_name="PH_PHLDB1_2"
                     /note="Pleckstrin homology-like domain-containing family B
                     member 2 pleckstrin homology (PH) domain; cd14673"
                     /db_xref="CDD:270192"
     CDS             1..1381
                     /gene="Phldb1"
                     /gene_synonym="Ll5"
                     /coded_by="NM_001191578.3:99..4244"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171434"
                     /db_xref="RGD:620878"
ORIGIN      
        1 matlnrnqlg pgcktqavvq kgpldlietg qglkvqtdkp hlvslgsgrl staitllple
       61 egrtvigsaa rdislqgpgl apehcyienl rgtltlypcg nactidglpv rqptrltqgc
      121 mlclgqstfl rfnhpaeakw mksmipaggr apgstyspgs aeseslvngn htaqpatrap
      181 pacashsslv ssiekdlqei mdslvleepg aagkkpaats plspvanggr yllspptspg
      241 amsvgssyen tspafsplss passgscash spsgqepgps vpplvparss syhlalqppq
      301 srpsgsrsse sprlgrkggh erppspglrg lltdspaatv laearrttes prlggqlpvv
      361 aislseypss garsqptsip gspkfqspvp aprnkigtlq drppspfrep pgtervltts
      421 psrqlvgrtf sdgsatrtlq ppesprlgrr gldsmrelpp lspslsrral splpartapd
      481 pklsrevaes prprrwaahg tspedfsltl gargrrtrsp sptlgeslap rkgsfsgrls
      541 payslgsltg asprqsphaq rklssgdlrv piprerknsi teisdneddl leyhrrqrqe
      601 rlreqemerl erqrletiln lcaeysradg gpetgelpsi geataalala grrpsrglag
      661 aivvsgrsge esggasqrlw esmersdeen lkeecsstes tqqehedaps tklqgevlav
      721 eeeraqvlgr veqlkvrvke leqqlqeaar eaemerallq gereaerall qkeqramdql
      781 qeklvaletg iqkerdkead aletetklfe dlefqqlere srveeerela gqgllrskae
      841 llrsvskrke rlavldsqag qiraqavqes erlareknav lqllqkekek ltvlerryhs
      901 ltggrsfpkt tstlkemekl llpavdleqw yqelmaglgt glaaasprss ppplpakasr
      961 qlqvyrskmn gdmasplprt rsgplpsssg ssssssqlsv atlgrspspk sallaqngts
     1021 slprnlaatl qdietkrqla lqqkghqvie eqrrrlaelk qkaaaeaqcq wdalhgaaaf
     1081 pagpsgfptl mhhsilhhlp agrergeege haydtlsles sdsmetsist ggnsacspdn
     1141 mssasgldmg kieemekmlk eahaeksrlm esreremelr rqaleeerrr reqverrlqs
     1201 esarrqqlve kevklrekqf sqarpltryl pnrkedfdlk thiessghgv dtclhvvlss
     1261 kvcrgylikm ggkikswkkr wfvfdrlkrt lsyyvdkhet klkgviyfqa ieevyydhlr
     1321 saakkrffhf tmvtespnpa ltfcvkthdr lyymvapsae amriwmdviv tgaegytqfm
     1381 n
//
LOCUS       NP_001102683             188 aa            linear   ROD 28-APR-2025
DEFINITION  long intergenic non-protein coding RNA 176 precursor [Rattus
            norvegicus].
ACCESSION   NP_001102683 XP_001057102 XP_580040
VERSION     NP_001102683.1
DBSOURCE    REFSEQ: accession NM_001109213.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474066.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_580040.2, XP_001057102.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF111612.1, SRR8487226.200188.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..188
                     /product="long intergenic non-protein coding RNA 176
                     precursor"
                     /calculated_mol_wt=18146
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2461
     CDS             1..188
                     /gene="Linc00176"
                     /gene_synonym="RGD1561282"
                     /coded_by="NM_001109213.1:123..689"
                     /db_xref="GeneID:499958"
                     /db_xref="RGD:1561282"
ORIGIN      
        1 mvplkpafyl lllllaflgs algwpgsqsc svqevlrhyq avifqdlqaa mqwagmgvqr
       61 tepgsrhhrf iqknltgagg gqgqpgtscg aqkessills ieslgqtllg svagvphnaf
      121 ekaawtvavr teavmrrhcr isyriqqpkk qavqprssrr rlllralyav atcweklfal
      181 salatgef
//
LOCUS       NP_942029                311 aa            linear   ROD 28-APR-2025
DEFINITION  protein YIF1B isoform a [Rattus norvegicus].
ACCESSION   NP_942029 XP_214879
VERSION     NP_942029.2
DBSOURCE    REFSEQ: accession NM_198734.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Alterio,J., Masson,J., Diaz,J., Chachlaki,K., Salman,H., Areias,J.,
            Al Awabdh,S., Emerit,M.B. and Darmon,M.
  TITLE     Yif1B Is Involved in the Anterograde Traffic Pathway and the Golgi
            Architecture
  JOURNAL   Traffic 16 (9), 978-993 (2015)
   PUBMED   26077767
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Al Awabdh,S., Miserey-Lenkei,S., Bouceba,T., Masson,J., Kano,F.,
            Marinach-Patrice,C., Hamon,M., Emerit,M.B. and Darmon,M.
  TITLE     A new vesicular scaffolding complex mediates the G-protein-coupled
            5-HT1A receptor targeting to neuronal dendrites
  JOURNAL   J Neurosci 32 (41), 14227-14241 (2012)
   PUBMED   23055492
  REMARK    GeneRIF: A new protein trafficking pathway model is proposed in
            which Yif1B is the scaffold protein recruiting the 5-HT1A receptor
            complex.
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Carrel,D., Masson,J., Al Awabdh,S., Capra,C.B., Lenkei,Z.,
            Hamon,M., Emerit,M.B. and Darmon,M.
  TITLE     Targeting of the 5-HT1A serotonin receptor to neuronal dendrites is
            mediated by Yif1B
  JOURNAL   J Neurosci 28 (32), 8063-8073 (2008)
   PUBMED   18685031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 7, 2005 this sequence version replaced NP_942029.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213940.1, SRR22582419.447515.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..311
                     /product="protein YIF1B isoform a"
                     /note="protein YIF1B; YIP1-interacting factor homolog B"
                     /calculated_mol_wt=33872
     Region          73..306
                     /region_name="YIF1"
                     /note="pfam03878"
                     /db_xref="CDD:461081"
     CDS             1..311
                     /gene="Yif1b"
                     /gene_synonym="Yip1b"
                     /coded_by="NM_198734.3:42..977"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:292768"
                     /db_xref="RGD:735199"
ORIGIN      
        1 mhatglaapa gtprlrkwps krrvpvsqpg madphqffdd tssapsrgyg gqpspgslgy
       61 ptssseaafl aapmsnmama ygsslaaqgk elvdknidrf ipvsklkyyf avdtvyvgkk
      121 lgllvfpylh qdwevqyqqd tpvaprfdin apdlyipama fityilvagl algtqdrfsp
      181 dllglqassa lawltlevva illslylvtv ntdlttidlv aflgykyvgm iggvltgllf
      241 gkigyylvla wccvsifvfm irtlrlkila qaaaegvpvr garnqlrmyl tmavaaaqpv
      301 lmywltfhlv r
//
LOCUS       NP_690060                526 aa            linear   ROD 28-APR-2025
DEFINITION  sorting nexin-27 isoform b [Rattus norvegicus].
ACCESSION   NP_690060
VERSION     NP_690060.2
DBSOURCE    REFSEQ: accession NM_152847.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Yong,X.L.H., Zhang,L., Yang,L., Chen,X., Tan,J.Z.A., Yu,X.,
            Chandra,M., Livingstone,E., Widagdo,J., Vieira,M.M., Roche,K.W.,
            Lynch,J.W., Keramidas,A., Collins,B.M. and Anggono,V.
  TITLE     Regulation of NMDA receptor trafficking and gating by
            activity-dependent CaMKIIalpha phosphorylation of the GluN2A
            subunit
  JOURNAL   Cell Rep 36 (1), 109338 (2021)
   PUBMED   34233182
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Choi,H.J., Jang,H.J., Park,E., Tingskov,S.J., Norregaard,R.,
            Jung,H.J. and Kwon,T.H.
  TITLE     Sorting Nexin 27 Regulates the Lysosomal Degradation of Aquaporin-2
            Protein in the Kidney Collecting Duct
  JOURNAL   Cells 9 (5), 1208 (2020)
   PUBMED   32413996
  REMARK    GeneRIF: Sorting Nexin 27 Regulates the Lysosomal Degradation of
            Aquaporin-2 Protein in the Kidney Collecting Duct.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Halff,E.F., Szulc,B.R., Lesept,F. and Kittler,J.T.
  TITLE     SNX27-Mediated Recycling of Neuroligin-2 Regulates Inhibitory
            Signaling
  JOURNAL   Cell Rep 29 (9), 2599-2607 (2019)
   PUBMED   31775031
  REMARK    GeneRIF: SNX27-Mediated Recycling of Neuroligin-2 Regulates
            Inhibitory Signaling.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Binda,C.S., Nakamura,Y., Henley,J.M. and Wilkinson,K.A.
  TITLE     Sorting nexin 27 rescues neuroligin 2 from lysosomal degradation to
            control inhibitory synapse number
  JOURNAL   Biochem J 476 (2), 293-306 (2019)
   PUBMED   30602588
  REMARK    GeneRIF: these data indicate that NLGs are SNX27-retromer cargoes
            and suggest that SNX27-retromer controls inhibitory synapse number,
            at least in part through trafficking of NLG2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Lin,T.B., Lai,C.Y., Hsieh,M.C., Wang,H.H., Cheng,J.K., Chau,Y.P.,
            Chen,G.D. and Peng,H.Y.
  TITLE     VPS26A-SNX27 Interaction-Dependent mGluR5 Recycling in Dorsal Horn
            Neurons Mediates Neuropathic Pain in Rats
  JOURNAL   J Neurosci 35 (44), 14943-14955 (2015)
   PUBMED   26538661
  REMARK    GeneRIF: The regulation of the VPS26A-SNX27 interaction modifies
            mGluR5 trafficking which mediates neuropathic pain.
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Lunn,M.L., Nassirpour,R., Arrabit,C., Tan,J., McLeod,I.,
            Arias,C.M., Sawchenko,P.E., Yates,J.R. 3rd and Slesinger,P.A.
  TITLE     A unique sorting nexin regulates trafficking of potassium channels
            via a PDZ domain interaction
  JOURNAL   Nat Neurosci 10 (10), 1249-1259 (2007)
   PUBMED   17828261
  REMARK    GeneRIF: SNX27 promotes the endosomal movement of Kir3 (GIRK)
            channels, leading to reduced surface expression, increased
            degradation and smaller Kir3 potassium currents.
REFERENCE   7  (residues 1 to 526)
  AUTHORS   MacNeil,A.J. and Pohajdak,B.
  TITLE     Polarization of endosomal SNX27 in migrating and tumor-engaged
            natural killer cells
  JOURNAL   Biochem Biophys Res Commun 361 (1), 146-150 (2007)
   PUBMED   17644068
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Lee,K.H., Ryu,C.J., Hong,H.J., Kim,J. and Lee,E.H.
  TITLE     CDNA microarray analysis of nerve growth factor-regulated gene
            expression profile in rat PC12 cells
  JOURNAL   Neurochem Res 30 (4), 533-540 (2005)
   PUBMED   16076023
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Fujiyama,K., Kajii,Y., Hiraoka,S. and Nishikawa,T.
  TITLE     Differential regulation by stimulants of neocortical expression of
            mrt1, arc, and homer1a mRNA in the rats treated with repeated
            methamphetamine
  JOURNAL   Synapse 49 (3), 143-149 (2003)
   PUBMED   12774298
  REMARK    GeneRIF: These findings suggest the differential regulation by
            stimulant of neocortical mrt1 expression and supports the view that
            stimulant induction of mrt1 may be involved in the early molecular
            signalings for stimulant sensitization.
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Kajii,Y., Muraoka,S., Hiraoka,S., Fujiyama,K., Umino,A. and
            Nishikawa,T.
  TITLE     A developmentally regulated and psychostimulant-inducible novel rat
            gene mrt1 encoding PDZ-PX proteins isolated in the neocortex
  JOURNAL   Mol Psychiatry 8 (4), 434-444 (2003)
   PUBMED   12740601
  REMARK    GeneRIF: Gene is developmentally regulated and stimulated by
            methamphetamine in the neocortex.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB051816.1, BF524912.1 and AC133978.2.
            
            On Oct 26, 2007 this sequence version replaced NP_690060.1.
            
            Transcript Variant: This variant (2) uses an alternate splice
            junction at the 5' end of a coding exon compared to variant 1. The
            resulting isoform (b) is shorter and has a distinct C-terminus
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..526
                     /product="sorting nexin-27 isoform b"
                     /note="PDZ-protein Mrt1; MAP-responsive gene protein;
                     methamphetamine-responsive transcript 1 protein;
                     methamphetamine (MAP) responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=59399
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          40..132
                     /region_name="PDZ_SNX27-like"
                     /note="PDZ domain of sorting nexin-27 (SNX27), and related
                     domains; cd23070"
                     /db_xref="CDD:467283"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Site            order(50..56,80,83,112,116,119..120)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467283"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96L92; propagated from
                     UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          158..263
                     /region_name="PX_SNX27"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 27; cd06886"
                     /db_xref="CDD:132796"
     Site            order(194..196,219..220,233)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          271..363
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          271..360
                     /region_name="FERM-like region F1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          371..419
                     /region_name="FERM-like region F2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          423..524
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     Region          423..523
                     /region_name="FERM-like region F3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     CDS             1..526
                     /gene="Snx27"
                     /gene_synonym="Mrt1"
                     /coded_by="NM_152847.2:121..1701"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:260323"
                     /db_xref="RGD:628705"
ORIGIN      
        1 madedgegih psaphrnggg gggsglhcag ngggggggpr vvrivksesg ygfnvrgqvs
       61 eggqlrsing elyaplqhvs avlpggaadr agvrkgdril evngvnvega thkqvvdlir
      121 agekeliltv lsvppheadn ldpsddslgq sfydytekqa vpisvptykh veqngekfvv
      181 ynvymagrql cskryrefai lhqnlkrefa nftfprlpgk wpfslseqql darrrgleey
      241 lekvcsirvi gesdimqefl sesdenyngv sdvelrvalp dgatvtvrvk knsttdqvyq
      301 aiaakvgmds ttvnyfalfe vinhsfvrkl apnefphkly vqnytsavpg tcltirkwlf
      361 tteeevllnd ndlavtyffh qavddvkkgy ikaeeksyql qklyeqrkmv mylnmlrtce
      421 gyneiifphc acdsrrkghv itaisithfk lhacteegql enqviafewd emqrwdtdee
      481 gmafcfeyar gekkprwvki ftpyfnymhe cfervfcelk wrkeey
//
LOCUS       NP_001416595             296 aa            linear   ROD 28-APR-2025
DEFINITION  forkhead box protein R1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001416595 XP_006243031
VERSION     NP_001416595.1
DBSOURCE    REFSEQ: accession NM_001429666.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 25, 2024 this sequence version replaced XP_006243031.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..296
                     /product="forkhead box protein R1 isoform 1"
                     /note="forkhead box protein R1"
                     /calculated_mol_wt=33858
     Region          173..261
                     /region_name="FH_FOXR"
                     /note="Forkhead (FH) domain found in the Forkhead box
                     protein R (FOXR) subfamily; cd20036"
                     /db_xref="CDD:410810"
     Site            order(180,198..199,202,221..222,224..225,228,235,249..251,
                     253)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410810"
     CDS             1..296
                     /gene="Foxr1"
                     /coded_by="NM_001429666.1:433..1323"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315601"
                     /db_xref="RGD:1309739"
ORIGIN      
        1 mgnecflsft tshlseaeqk lalyrlrive ppklplekip npdkdgpdik pnlwmwvnpn
       61 ivyppgklev avkkedsssa ppasqsalke edscseasei paqqpppprk qkrkqkekhi
      121 asspsiweep teeeeakdrd dsfsvalpsl ptraplqnrw rlrqaispeg rlwsrpplhy
      181 fhlialalrn sppcglsvqq iynftrehfp ffrtapeawk ntvrhnlcfr dsfekvpvsk
      241 qgeastrprs clwklteegh rrfseeartl astrlqsiqq cmsqpdvmpf lfdlqe
//
LOCUS       NP_001386539             190 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 428 isoform a [Rattus norvegicus].
ACCESSION   NP_001386539 XP_006228509
VERSION     NP_001386539.1
DBSOURCE    REFSEQ: accession NM_001399610.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 12, 2022 this sequence version replaced XP_006228509.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399484.1353447.1, CB782877.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..190
                     /product="zinc finger protein 428 isoform a"
                     /calculated_mol_wt=20405
     CDS             1..190
                     /gene="Zfp428"
                     /gene_synonym="RGD1564862"
                     /coded_by="NM_001399610.1:473..1045"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:361519"
                     /db_xref="RGD:1564862"
ORIGIN      
        1 mtetreptet ggyasleedd edlspgpehs sdseytlsep dseeeeeeee eeettddpey
       61 dpgykvkqri gggrggpsrr apratqpagp paqpcqlcgr salgeappgt ppcrlccpat
      121 atqeapapes ralgeeeeep srtgenrpag rdgdededeg gtyhcteced sfdnlgelhg
      181 hfmlhargev
//
LOCUS       NP_001388729             322 aa            linear   ROD 28-APR-2025
DEFINITION  transmembrane protein 171 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001388729
VERSION     NP_001388729.1
DBSOURCE    REFSEQ: accession NM_001401800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2049767.1,
                                           SRR26360186.2394514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..322
                     /product="transmembrane protein 171 isoform 2"
                     /note="parturition-related protein 2; proline-rich protein
                     PRP2"
                     /calculated_mol_wt=34526
     Region          2..317
                     /region_name="TMEM171"
                     /note="Transmembrane protein family 171; pfam15471"
                     /db_xref="CDD:464734"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     CDS             1..322
                     /gene="Tmem171"
                     /gene_synonym="Prp2"
                     /coded_by="NM_001401800.1:115..1083"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293634"
                     /db_xref="RGD:1359492"
ORIGIN      
        1 mssvgtaepd gdqrdrqvsk lifflfvfga vllcvgilis ifgyqacqyk plshcsmvlk
       61 iagpscavmg lgtvilarsr arlqlrerqr qghqdpdqsf fcgesrqfaq clifgflflt
      121 sgmlisilgi wvpgcgsdwa qeplnetnsg egepqicsfl slqimgpliv lvglcffvva
      181 hvkkksnlss srdtseiegg hthstepvhi tvgdsviifp pppppyfaes saaapspgan
      241 slhrienpps ysslfnlrtp tpenqgaase rdreviytis gpgsssessh tghlpldlpp
      301 ryeeketapa tplgapsess pp
//
LOCUS       NP_001423948             535 aa            linear   ROD 28-APR-2025
DEFINITION  biotinidase isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001423948 XP_006252671
VERSION     NP_001423948.1
DBSOURCE    REFSEQ: accession NM_001437019.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252671.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.53236.1,
                                           SRR26643429.49824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..535
                     /product="biotinidase isoform 1 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55781
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4055
     Region          50..353
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(104,204,208,210,237..238,240..241,263)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(104,204,237)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            order(205..209,216..218,238,240..244,247..248,269..270,
                     272..274,276..277,301..302,349..353)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          385..534
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     CDS             1..535
                     /gene="Btd"
                     /coded_by="NM_001437019.1:268..1875"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 mrriffpkrf tvcimsgart ahalvfllgc salalgvcsa slehgeaeyy vaavyehrsv
       61 lspnplelss rqqalelmkq nldvyeqqvm aaaqkgahii vfpedgihgf nftrtsiypf
      121 ldlmpsprlv swnpclepfr fndtevlqrl scmaikgkmf lvanlgtkqp clgsdpgcpq
      181 dgryqfntnv afsdngtlvg ryrkhnlyfe eafdspadvd lttfdtpfag kfgmftcfdi
      241 lffdpavrll rdfevkhiay ptawmnqlpl laaieiqkaf atafgvtvla anihhptlgm
      301 tgsgihtplk sfwyhnmddp eghliiarva tnpqglvgte nttsemdpsh rkflkvlsgd
      361 pycekdaqev rcdeaakwnl napptfhsem mydnftlvpv wgkeghlqvc snslcchllf
      421 erpalskely algvfdglht vhgtyyvqac alvkcggagf etcgqeisea eglfdfhlwg
      481 nfstlyvfpl fltsgmtldt pdqlgwesdh yflrkrglss glvtaalygr lyern
//
LOCUS       NP_001419388             753 aa            linear   ROD 28-APR-2025
DEFINITION  anoctamin 9 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001419388 XP_063137092
VERSION     NP_001419388.1
DBSOURCE    REFSEQ: accession NM_001432459.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Suzuki,J., Fujii,T., Imao,T., Ishihara,K., Kuba,H. and Nagata,S.
  TITLE     Calcium-dependent phospholipid scramblase activity of TMEM16
            protein family members
  JOURNAL   J Biol Chem 288 (19), 13305-13316 (2013)
   PUBMED   23532839
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Tian,Y., Schreiber,R. and Kunzelmann,K.
  TITLE     Anoctamins are a family of Ca2+-activated Cl- channels
  JOURNAL   J Cell Sci 125 (Pt 21), 4991-4998 (2012)
   PUBMED   22946059
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Scudieri,P., Sondo,E., Ferrera,L. and Galietta,L.J.
  TITLE     The anoctamin family: TMEM16A and TMEM16B as calcium-activated
            chloride channels
  JOURNAL   Exp Physiol 97 (2), 177-183 (2012)
   PUBMED   21984732
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Ousingsawat,J., Kongsuphol,P., Schreiber,R. and Kunzelmann,K.
  TITLE     CFTR and TMEM16A are separate but functionally related Cl- channels
  JOURNAL   Cell Physiol Biochem 28 (4), 715-724 (2011)
   PUBMED   22178883
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Schreiber,R., Uliyakina,I., Kongsuphol,P., Warth,R., Mirza,M.,
            Martins,J.R. and Kunzelmann,K.
  TITLE     Expression and function of epithelial anoctamins
  JOURNAL   J Biol Chem 285 (10), 7838-7845 (2010)
   PUBMED   20056604
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_063137092.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.3914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..753
                     /product="anoctamin 9 isoform 1"
                     /calculated_mol_wt=87663
     Region          180..735
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     CDS             1..753
                     /gene="Ano9"
                     /gene_synonym="RGD1560565"
                     /coded_by="NM_001432459.1:68..2329"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:499287"
                     /db_xref="RGD:1560565"
ORIGIN      
        1 mqvdeslqil vgsegdhlpl memgsckpea sdqwdcvlva dlqtqksqkh vqrqqqflek
       61 lerngfhfkv lkdqkkvffg iradsavidm yrtllmkped prsrakqnfn iattririvn
      121 fvvnskkrls gelrwadtfe dlvkdgvfet mfllhkgeed lsrewaqwrn vfqpqpidki
      181 reyfgekval yftwlgwyty mlvpaavvgl ivflsgfalf dssqiskeic saddifmcpl
      241 gdnsrryqrl semctfaklt hlfdnegtvi faifmalwat vfleiwkrkr arevqswely
      301 ewdeeeeema lelinsphye lkkhhhsyls stiililslf miclmigmah llvvyrvlaa
      361 alfssfleqq vttavvvtga vvhyviivim tkvnkcvalk lckfeeprtf seqeskftvk
      421 ffilqffahf ssliyiafil gringhpgks trlaglwkle echlsgcmmd lfiqmaiimg
      481 lkqtlsncie ylypllahkc rsvqayrhgr kskdpelaew qrnyhmnpvn tfslfdefme
      541 mmiqygftti fvaafplapl lalfsnlvei rldaikmvrl qrrlvprkak digtwlqvle
      601 tigvlavian gmviaftsef iprvvykyhy gpcrknqtft ddclkdyvnh slsvfytkdf
      661 qdhgrmegqe nvtvcryrdy rndhdynlse qfwfilairl afvilfehva lcikliaawf
      721 vpdvpqsvkn evleekyqri rgrmcfssrs tdv
//
LOCUS       NP_001421144             526 aa            linear   ROD 28-APR-2025
DEFINITION  male-specific lethal 3 homolog isoform 5 [Rattus norvegicus].
ACCESSION   NP_001421144 XP_006256898
VERSION     NP_001421144.1
DBSOURCE    REFSEQ: accession NM_001434215.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Basilicata,M.F., Bruel,A.L., Semplicio,G., Valsecchi,C.I.K.,
            Aktas,T., Duffourd,Y., Rumpf,T., Morton,J., Bache,I.,
            Szymanski,W.G., Gilissen,C., Vanakker,O., Ounap,K., Mittler,G., van
            der Burgt,I., El Chehadeh,S., Cho,M.T., Pfundt,R., Tan,T.Y.,
            Kirchhoff,M., Menten,B., Vergult,S., Lindstrom,K., Reis,A.,
            Johnson,D.S., Fryer,A., McKay,V., Fisher,R.B., Thauvin-Robinet,C.,
            Francis,D., Roscioli,T., Pajusalu,S., Radtke,K., Ganesh,J.,
            Brunner,H.G., Wilson,M., Faivre,L., Kalscheuer,V.M., Thevenon,J.
            and Akhtar,A.
  CONSRTM   DDD Study
  TITLE     De novo mutations in MSL3 cause an X-linked syndrome marked by
            impaired histone H4 lysine 16 acetylation
  JOURNAL   Nat Genet 50 (10), 1442-1451 (2018)
   PUBMED   30224647
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Kim,D., Blus,B.J., Chandra,V., Huang,P., Rastinejad,F. and
            Khorasanizadeh,S.
  TITLE     Corecognition of DNA and a methylated histone tail by the MSL3
            chromodomain
  JOURNAL   Nat Struct Mol Biol 17 (8), 1027-1029 (2010)
   PUBMED   20657587
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Oct 22, 2024 this sequence version replaced XP_006256898.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.284410.1,
                                           SRR26643289.44668.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..526
                     /product="male-specific lethal 3 homolog isoform 5"
                     /note="male-specific lethal-3 homolog 1"
                     /calculated_mol_wt=60226
     Region          15..82
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(26..27,31..34,54,56..59,64,66..69,71..73,76..77)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(31,56,59,64)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(53,55..60,62,64..67)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(53,56,60,62,67)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          167..511
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..526
                     /gene="Msl3"
                     /gene_synonym="Msl31; Msl3l1"
                     /coded_by="NM_001434215.1:33..1613"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:317464"
                     /db_xref="RGD:1549763"
ORIGIN      
        1 msaskgmkfq fhsgekvlcf epdptkarvl ydakiidvii gkdekgrkip eylihfngwn
       61 ssswdrwaae dhvlhdtden rrlqrklakk aiarlrgtgk kkrrcrlpgv dsvlksvpvk
      121 ektkndensi sstchescge knggikehrq rrikvktkgk kkvlslrsrk dmdertitie
      181 ipevlkkqle ddcyyinrrk rlvklpcqtn iitilesyvk hfainaafsa nerprhhham
      241 mhahmnvhyv paeknvdlck emvdglritf dytlplvlly pyeqtqykrv tsskfflpik
      301 esttttnrsq eelspsppll npstpqstes qpptgepatp krrkaepeal qslrrstrhs
      361 tncdrlsess sspqpkrrqq dtstsmpklf lhlekktpvh srssspiplt pskdgsavfa
      421 gfegrrtnei nevlswklvp dnyppgdqpp ppsyiygaqh llrlfvklpe ilgkmsfsek
      481 nlkallkhfd lflrflaeyh ddffpesayv aaceahystk npraiy
//
LOCUS       NP_001289138            1463 aa            linear   ROD 28-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 4 precursor [Rattus
            norvegicus].
ACCESSION   NP_001289138
VERSION     NP_001289138.1
DBSOURCE    REFSEQ: accession NM_001302209.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1463)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1463)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1463)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1463)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1463)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1463)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1463)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1463)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1463)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF081150.1, FM039554.1, CB579130.1, AF063102.1, CO556290.1,
            FM099106.1, FM068641.1 and AA899882.1.
            
            Transcript Variant: This variant (4) lacks two consecutive exons in
            the 3' coding region, but maintains the reading frame, compared to
            variant 1. The resulting isoform (4) lacks an internal segment,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF081150.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1463
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1463
                     /product="adhesion G protein-coupled receptor L2 isoform 4
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=161120
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          422..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Site            791
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          792..841
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            828..829
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098; propagated
                     from UniProtKB/Swiss-Prot (O88923.2)"
     Region          848..1105
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            885..905
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            912..932
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            957..977
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            995..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1041..1063
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1042..1062
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1067..1092
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1067..1087
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1104..1463
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     Region          1115..1136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1362..1404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     CDS             1..1463
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_001302209.1:463..4854"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleniksw vlgafallcl lgltwsfgll fvneetvvma ylftafnafq
     1081 glfififhca lqkkvrkeya kcfrhwyccg glptesphss vkastsrtsa ryssgtqsri
     1141 rrmwndtvrk qsessfisgd inststlnqg mtgnylltnp llrphgtnnp yntllaetvv
     1201 cnapsapvfn spghslnntr dtsamdtlpl ngnfnnsysl rkadyhdgvq vvdcglslnd
     1261 tafekmiise lvhnnlrgsn kthnlelklp vkpviggsss eddaivadas slmhgdnpgl
     1321 efrhkeleap lipqrthsll yqpqkkvkpe atdsyvsqlt aeadehlqsp nrdslytsmp
     1381 nlrdspypes spdmaedlsp srrsenediy yksmpnlgag rqlqmcyqis rgnsdgyiip
     1441 inkegcipeg dvregqmqlv tsl
//
LOCUS       NP_001101328             977 aa            linear   ROD 28-APR-2025
DEFINITION  ephrin type-A receptor 1 precursor [Rattus norvegicus].
ACCESSION   NP_001101328 XP_001072130 XP_231658
VERSION     NP_001101328.1
DBSOURCE    REFSEQ: accession NM_001107858.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Chen,G., Wang,Y., Zhou,M., Shi,H., Yu,Z., Zhu,Y. and Yu,F.
  TITLE     EphA1 receptor silencing by small interfering RNA has
            antiangiogenic and antitumor efficacy in hepatocellular carcinoma
  JOURNAL   Oncol Rep 23 (2), 563-570 (2010)
   PUBMED   20043122
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Yamazaki,T., Masuda,J., Omori,T., Usui,R., Akiyama,H. and Maru,Y.
  TITLE     EphA1 interacts with integrin-linked kinase and regulates cell
            morphology and motility
  JOURNAL   J Cell Sci 122 (Pt 2), 243-255 (2009)
   PUBMED   19118217
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Masuda,J., Usui,R. and Maru,Y.
  TITLE     Fibronectin type I repeat is a nonactivating ligand for EphA1 and
            inhibits ATF3-dependent angiogenesis
  JOURNAL   J Biol Chem 283 (19), 13148-13155 (2008)
   PUBMED   18308734
  REMARK    GeneRIF: I 12 acquired a higher affinity toward EphA2 with K(d) 18
            nm and inhibited vascular endothelial growth factor-dependent
            angiogenic invasion in a Matrigel plug assay
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Ogita,H., Kunimoto,S., Kamioka,Y., Sawa,H., Masuda,M. and
            Mochizuki,N.
  TITLE     EphA4-mediated Rho activation via Vsm-RhoGEF expressed specifically
            in vascular smooth muscle cells
  JOURNAL   Circ Res 93 (1), 23-31 (2003)
   PUBMED   12775584
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473959.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001072130.1, XP_231658.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132271, SAMEA5756307
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..977
                     /product="ephrin type-A receptor 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin receptor EphA1; ephrin type-A receptor 1"
                     /calculated_mol_wt=105731
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2842
     Region          28..204
                     /region_name="EphR_LBD_A1"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 1;
                     cd10479"
                     /db_xref="CDD:198447"
     Site            order(53,55..59,65..66,68,70,103,105,110..111,155,
                     159..160,163..165,192..194,196)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198447"
     Region          335..426
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          454..536
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(525..526,528..529)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          <596..622
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          620..885
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(631..634,637,639,655,657,687,703..706,750,754..755,
                     757,767..768)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270629"
     Region          913..975
                     /region_name="SAM_EPH-A1"
                     /note="SAM domain of EPH-A1 subfamily of tyrosine kinase
                     receptors; cd09542"
                     /db_xref="CDD:188941"
     Site            order(931,964)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188941"
     CDS             1..977
                     /gene="Epha1"
                     /coded_by="NM_001107858.1:60..2993"
                     /db_xref="GeneID:312279"
                     /db_xref="RGD:1304680"
ORIGIN      
        1 merrwplgla llllllcapl ppgaraeevt lmdtstaqge lgwlldppet gwsevqqmln
       61 gtplymyqdc piqeggdtdh wlrsnwiyrg eeasrvhvel qftvrdcksf pggagplgck
      121 etfnlfymes dqdvgiqlrr plfqkvttva adqsftirdl asgsvklnve hcslghltrr
      181 glylafhnpg scvalvsvrv fyqrcaetvh glahfphtlp gptglvevag tclshaqisl
      241 gssgtprmhc spdgewlvpv gqcqcepgye esggsvgcta cptgfyrmdm ntlhclkcpq
      301 hsvaesegst ictcenghyr apgegpqvac trppsapqnl sfsasgtqls lrwepprdtg
      361 grqdirysve clqcrgiaqd ggpcqpcgkg vhfspaasgl tastvqvegl epyanytfti
      421 ksqnrvsgld ssspssasls inmgqaesls glslklvkke prqleltwag srlqnpggnl
      481 syelhvlnqd eewhqmvlep rvlltklqpd ttyivrvrtl tplgpgpfsp dhefrtsppv
      541 srsltggeiv aiifglllgi alligiyvfr srrgqrqrqq rqrerttnvd redklwlkpy
      601 vdlqayedpa qgaldfaqel dpawlivdtv igegefgevy rgalripsqd cktvaiktlk
      661 dtspdgywwn flreatimgq fnhphilrle gvitkrkpim iitefmenga ldaflkered
      721 qlvpgqlvam llgiasgmny lsghnyvhrd laarnilvnq nlcckvsdfg ltrllddfdg
      781 tyetqggkip irwtapeaia hrifttasdv wsfgivmwev lsfgdkpyge msnqevmksi
      841 edgyrlpppv dcpaplyelm kncwaydrar rphflqlqah leqlltdphs lrtianfdpr
      901 vtlrlpslsg sdgipyrsvs ewlesirmkr yilhfrsagl dtmecvlelt aedltqmgit
      961 lpghqkrilc siqgfkd
//
LOCUS       NP_001011996             706 aa            linear   ROD 28-APR-2025
DEFINITION  phospholipid transfer protein C2CD2L isoform 3 [Rattus norvegicus].
ACCESSION   NP_001011996 XP_217129
VERSION     NP_001011996.1
DBSOURCE    REFSEQ: accession NM_001011996.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Lees,J.A., Messa,M., Sun,E.W., Wheeler,H., Torta,F., Wenk,M.R., De
            Camilli,P. and Reinisch,K.M.
  TITLE     Lipid transport by TMEM24 at ER-plasma membrane contacts regulates
            pulsatile insulin secretion
  JOURNAL   Science 355 (6326) (2017)
   PUBMED   28209843
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Pottekat,A., Becker,S., Spencer,K.R., Yates,J.R. 3rd, Manning,G.,
            Itkin-Ansari,P. and Balch,W.E.
  TITLE     Insulin biosynthetic interaction network component, TMEM24,
            facilitates insulin reserve pool release
  JOURNAL   Cell Rep 4 (5), 921-930 (2013)
   PUBMED   24012759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Feb 11, 2005 this sequence version replaced XP_217129.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085925.1, SRR26643287.19894.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..706
                     /product="phospholipid transfer protein C2CD2L isoform 3"
                     /note="transmembrane protein 24; C2 domain-containing
                     protein 2-like; C2 calcium-dependent domain containing
                     2-like; phospholipid transfer protein C2CD2L"
                     /calculated_mol_wt=75930
     Region          84..260
                     /region_name="SMP_C2CD2L"
                     /note="synaptotagmin-like mitochondrial-lipid-binding
                     protein (SMP) domain found in C2 domain-containing protein
                     2-like (C2CD2L); cd21683"
                     /db_xref="CDD:439239"
     Site            order(98,101..102,106,110,130,135,156,161,163,165,185,187,
                     191,193,205,207,209,219,242,245..246,251,253..256)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:439239"
     Region          288..412
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     CDS             1..706
                     /gene="C2cd2l"
                     /gene_synonym="Tmem24"
                     /coded_by="NM_001011996.2:395..2515"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:300666"
                     /db_xref="RGD:1310281"
ORIGIN      
        1 mdpdwgqrdv gwaallvlfa aslltvlgwl lqyarglwls ragggrdsrp asaaepggsl
       61 relgvwrsll rlratrssap eeagvrglla slfafksfre nwqrawvral neqacrdgss
      121 iqiafeeipq lpprasishv tcvdqsertm vlhcqlaaee vrfpisvtqq spaavsmety
      181 hvtltlpptq levsleeipd egllvswaft drpdlslkvl pksqtrerde eqpelstvee
      241 likdaivstq pammvnlrac sapgglvpse kpptmsqaqp siprptrlfl rqlrashlgs
      301 elggteelcc aaeldnpmqq kwtkptrags evewaedlal dlgpqsrelt lkvlrssscg
      361 daellgqatl pvgspskpls rrqvcpltpg pgkslspaai vtvelhyeqg sprnlgtpts
      421 stprpsitpt kkieldrtim pdgtivttvt tvqsrprvdg kldspsrsps kvevtekmtt
      481 vlsessgpsn ashsssresh lsngldpvae tairqlteps graakktptk rstliisgvs
      541 kvpiaqdela lslgyaasle asmqddagas ggpssppsdp satspgpvda lssptsvqea
      601 dettrsdise rpsvddvese tgstgaletr slkdhkvsfl rsgtklifrr rprqkeagls
      661 qshddlsntt atpsvrkkag sfsrrlikrf sfkskpkang npspql
//
LOCUS       NP_001424450             848 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-3 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424450 XP_006250204
VERSION     NP_001424450.1
DBSOURCE    REFSEQ: accession NM_001437521.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Reubold,T.F., Faelber,K., Plattner,N., Posor,Y., Ketel,K.,
            Curth,U., Schlegel,J., Anand,R., Manstein,D.J., Noe,F., Haucke,V.,
            Daumke,O. and Eschenburg,S.
  TITLE     Crystal structure of the dynamin tetramer
  JOURNAL   Nature 525 (7569), 404-408 (2015)
   PUBMED   26302298
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Li,J., Zhang,D.S., Ye,J.C., Li,C.M., Qi,M., Liang,D.D., Xu,X.R.,
            Xu,L., Liu,Y., Zhang,H., Zhang,Y.Y., Deng,F.F., Feng,J., Shi,D.,
            Chen,J.J., Li,L., Chen,G., Sun,Y.F., Peng,L.Y. and Chen,Y.H.
  TITLE     Dynamin-2 mediates heart failure by modulating Ca2+ -dependent
            cardiomyocyte apoptosis
  JOURNAL   Int J Cardiol 168 (3), 2109-2119 (2013)
   PUBMED   23410488
  REMARK    GeneRIF: DNM2 mediates HF by modulating Ca(2+)-dependent apoptotic
            death of cardiomyocyte.
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Ikeuchi,Y., de la Torre-Ubieta,L., Matsuda,T., Steen,H., Okazawa,H.
            and Bonni,A.
  TITLE     The XLID protein PQBP1 and the GTPase Dynamin 2 define a signaling
            link that orchestrates ciliary morphogenesis in postmitotic neurons
  JOURNAL   Cell Rep 4 (5), 879-889 (2013)
   PUBMED   23994472
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Grossman,G.H., Ebke,L.A., Beight,C.D., Jang,G.F., Crabb,J.W. and
            Hagstrom,S.A.
  TITLE     Protein partners of dynamin-1 in the retina
  JOURNAL   Vis Neurosci 30 (4), 129-139 (2013)
   PUBMED   23746204
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Tanifuji,S., Funakoshi-Tago,M., Ueda,F., Kasahara,T. and Mochida,S.
  TITLE     Dynamin isoforms decode action potential firing for synaptic
            vesicle recycling
  JOURNAL   J Biol Chem 288 (26), 19050-19059 (2013)
   PUBMED   23687302
  REMARK    GeneRIF: dynamin isoforms select appropriate vesicle reuse pathways
            associated with specific neuronal firing patterns
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Gray,N.W., Fourgeaud,L., Huang,B., Chen,J., Cao,H., Oswald,B.J.,
            Hemar,A. and McNiven,M.A.
  TITLE     Dynamin 3 is a component of the postsynapse, where it interacts
            with mGluR5 and Homer
  JOURNAL   Curr Biol 13 (6), 510-515 (2003)
   PUBMED   12646135
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Zhang,Y., Moheban,D.B., Conway,B.R., Bhattacharyya,A. and
            Segal,R.A.
  TITLE     Cell surface Trk receptors mediate NGF-induced survival while
            internalized receptors regulate NGF-induced differentiation
  JOURNAL   J Neurosci 20 (15), 5671-5678 (2000)
   PUBMED   10908605
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Cao,H., Garcia,F. and McNiven,M.A.
  TITLE     Differential distribution of dynamin isoforms in mammalian cells
  JOURNAL   Mol Biol Cell 9 (9), 2595-2609 (1998)
   PUBMED   9725914
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Cook,T., Mesa,K. and Urrutia,R.
  TITLE     Three dynamin-encoding genes are differentially expressed in
            developing rat brain
  JOURNAL   J Neurochem 67 (3), 927-931 (1996)
   PUBMED   8752097
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Nakata,T., Takemura,R. and Hirokawa,N.
  TITLE     A novel member of the dynamin family of GTP-binding proteins is
            expressed specifically in the testis
  JOURNAL   J Cell Sci 105 (Pt 1), 1-5 (1993)
   PUBMED   8360266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006250204.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D14076.1, SRR26643429.44925.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..848
                     /product="dynamin-3 isoform 4"
                     /EC_number="3.6.5.5"
                     /note="T-dynamin; dynamin, testicular; testicular dynamin"
                     /calculated_mol_wt=95465
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          514..625
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(516,518..519,521,538,607..608,611,614..615,618)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          645..735
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          <743..833
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     CDS             1..848
                     /gene="Dnm3"
                     /gene_synonym="dynamin-2"
                     /coded_by="NM_001437521.1:172..2718"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:171574"
                     /db_xref="RGD:727949"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqvirkg wltvsnigim kggskgywfv
      541 ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr nvykdyrsle
      601 lacdsqedvd swkasllrag vypdksften dengqaenfs mdpqlerqve tirnlvdsym
      661 siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesve qaqrrdemlr
      721 myqalkeala iigdintvtv stpapppvdd swlqhsrrsp ppspttqrrl tlsaplprpa
      781 ssrgpapaip spgphsgapp vpfrpgplpp fpnssdsyga ppqvpsrptr appsvprfga
      841 vkeeavep
//
LOCUS       NP_001419017             491 aa            linear   ROD 28-APR-2025
DEFINITION  IQ motif containing M like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419017 XP_063134588
VERSION     NP_001419017.1
DBSOURCE    REFSEQ: accession NM_001432088.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 25, 2024 this sequence version replaced XP_063134588.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC078986.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..491
                     /product="IQ motif containing M like 1 isoform 2"
                     /note="IQ domain-containing protein M-like"
                     /calculated_mol_wt=57626
     CDS             1..491
                     /gene="Iqcml1"
                     /coded_by="NM_001432088.1:453..1928"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:102554391"
                     /db_xref="RGD:7680597"
ORIGIN      
        1 mataeaipev vegpllettq rdflqeaksl iaqhykrvne nkahgtsidv fknkhqkpkt
       61 gqfipfeikk seilnvveeh rlvlrsissp kdtakcsnlt easqqtslke qhvpniknky
      121 qpvdllkkek vklgkimddi esvskrmeke kemnlrkyrm sepfhsqigl slhnatshlg
      181 llkeladrtl ydqrsaalmr sshlphesaq tlsgasiifk dyyirplkkk eiqpikkelk
      241 plnkrsqiiv kpdkinnkvk rigphieifq lfqgrkrlif tkrivkliii iqafirgwle
      301 rkrlqrlksk alyhgpnlka vikmyrslih rvrhrlglwr trqiiyfgel eewmdrkkfy
      361 etmfakredw qglersellk yfndcghfpt qkqidelwdl fhrysegkys evirkssaie
      421 llftlyppqg arvnagtrlr stwlrplvdg eegykyivtg hpilkranir tvgklvarsi
      481 rerkmrqfyk s
//
LOCUS       NP_001395888            1114 aa            linear   ROD 28-APR-2025
DEFINITION  IQ motif and SEC7 domain-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001395888 XP_038964683
VERSION     NP_001395888.1
DBSOURCE    REFSEQ: accession NM_001408959.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Elagabani,M.N., Brisevac,D., Kintscher,M., Pohle,J., Kohr,G.,
            Schmitz,D. and Kornau,H.C.
  TITLE     Subunit-selective N-Methyl-d-aspartate (NMDA) Receptor Signaling
            through Brefeldin A-resistant Arf Guanine Nucleotide Exchange
            Factors BRAG1 and BRAG2 during Synapse Maturation
  JOURNAL   J Biol Chem 291 (17), 9105-9118 (2016)
   PUBMED   26884337
  REMARK    GeneRIF: both Arf6 activation through GluN2B-BRAG1 during early
            development and the transition from BRAG1- to BRAG2-dependent Arf6
            signaling induced by the GluN2 subunit switch are critical for the
            development of mature glutamatergic synapses.
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Yue,J., Xie,M., Gou,X., Lee,P., Schneider,M.D. and Wu,X.
  TITLE     Microtubules regulate focal adhesion dynamics through MAP4K4
  JOURNAL   Dev Cell 31 (5), 572-585 (2014)
   PUBMED   25490267
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Oka,S., Uramoto,H., Shimokawa,H., Yamada,S. and Tanaka,F.
  TITLE     Epidermal growth factor receptor-GEP100-Arf6 axis affects the
            prognosis of lung adenocarcinoma
  JOURNAL   Oncology 86 (5-6), 263-270 (2014)
   PUBMED   24902879
REFERENCE   4  (residues 1 to 1114)
  AUTHORS   Sakagami,H., Katsumata,O., Hara,Y., Tamaki,H., Watanabe,M.,
            Harvey,R.J. and Fukaya,M.
  TITLE     Distinct synaptic localization patterns of brefeldin A-resistant
            guanine nucleotide exchange factors BRAG2 and BRAG3 in the mouse
            retina
  JOURNAL   J Comp Neurol 521 (4), 860-876 (2013)
   PUBMED   22886754
REFERENCE   5  (residues 1 to 1114)
  AUTHORS   Dmitriev,A.A., Kashuba,V.I., Haraldson,K., Senchenko,V.N.,
            Pavlova,T.V., Kudryavtseva,A.V., Anedchenko,E.A., Krasnov,G.S.,
            Pronina,I.V., Loginov,V.I., Kondratieva,T.T., Kazubskaya,T.P.,
            Braga,E.A., Yenamandra,S.P., Ignatjev,I., Ernberg,I., Klein,G.,
            Lerman,M.I. and Zabarovsky,E.R.
  TITLE     Genetic and epigenetic analysis of non-small cell lung cancer with
            NotI-microarrays
  JOURNAL   Epigenetics 7 (5), 502-513 (2012)
   PUBMED   22491060
REFERENCE   6  (residues 1 to 1114)
  AUTHORS   Xie,C.G., Wei,S.M., Chen,J.M., Xu,X.F., Cai,J.T., Chen,Q.Y. and
            Jia,L.T.
  TITLE     Down-regulation of GEP100 causes increase in E-cadherin levels and
            inhibits pancreatic cancer cell invasion
  JOURNAL   PLoS One 7 (5), e37854 (2012)
   PUBMED   22662237
REFERENCE   7  (residues 1 to 1114)
  AUTHORS   Menju,T., Hashimoto,S., Hashimoto,A., Otsuka,Y., Handa,H.,
            Ogawa,E., Toda,Y., Wada,H., Date,H. and Sabe,H.
  TITLE     Engagement of overexpressed Her2 with GEP100 induces autonomous
            invasive activities and provides a biomarker for metastases of lung
            adenocarcinoma
  JOURNAL   PLoS One 6 (9), e25301 (2011)
   PUBMED   21966491
REFERENCE   8  (residues 1 to 1114)
  AUTHORS   Scholz,R., Berberich,S., Rathgeber,L., Kolleker,A., Kohr,G. and
            Kornau,H.C.
  TITLE     AMPA receptor signaling through BRAG2 and Arf6 critical for
            long-term synaptic depression
  JOURNAL   Neuron 66 (5), 768-780 (2010)
   PUBMED   20547133
REFERENCE   9  (residues 1 to 1114)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 1114)
  AUTHORS   Morishige,M., Hashimoto,S., Ogawa,E., Toda,Y., Kotani,H.,
            Hirose,M., Wei,S., Hashimoto,A., Yamada,A., Yano,H., Mazaki,Y.,
            Kodama,H., Nio,Y., Manabe,T., Wada,H., Kobayashi,H. and Sabe,H.
  TITLE     GEP100 links epidermal growth factor receptor signalling to Arf6
            activation to induce breast cancer invasion
  JOURNAL   Nat Cell Biol 10 (1), 85-92 (2008)
   PUBMED   18084281
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 5, 2022 this sequence version replaced XP_038964683.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760475, SAMN12840107
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..1114
                     /product="IQ motif and SEC7 domain-containing protein 1
                     isoform 1"
                     /note="IQ motif and SEC7 domain-containing protein 1; IQ
                     motif and Sec7 domain 1"
                     /calculated_mol_wt=124011
     Region          523..711
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          743..872
                     /region_name="IQ_SEC7_PH"
                     /note="PH domain; pfam16453"
                     /db_xref="CDD:465120"
     CDS             1..1114
                     /gene="Iqsec1"
                     /coded_by="NM_001408959.1:130..3474"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:686590"
                     /db_xref="RGD:1596313"
ORIGIN      
        1 mkgdggavwg lmwkycisvr tlsvegeaps setgtsldsp sayhqgplvp gsslspdhye
       61 htsvgaygly agpgpqqrtr rprlqhstsv lrkqaeeeai krsrslsesy elssdlqdkq
      121 vemlerkygg rlvtrhaart iqtafrqyqm nknferlrss msenrmsrri vlsnmrmqfs
      181 fegpekvhss yfegkqvsvt ndgsqlgalv psecgdlsdp alkspapssd fadaiteled
      241 afsrqvksla esiddalncr slhseevpas dtarardtep kpglhgmdhr kldemtasys
      301 dvtlyideee lspplplsqa gdrpsstesd lrlrsggaaq dywalahked kadtdtscrs
      361 tpslerpepr lrvehlpllt ieppsdssve lsdrsdrssl krqsayersl ggqqgspkhg
      421 phggppkglp reepelrprp prpleshlai ngsanrqsks esdysdgdnd sinstsnsnd
      481 tincssesss rdslreqtls kqtyhketrn swdspafsnd virkrhyrig lnlfnkkpek
      541 giqyliergf vpdtpvgvah fllqrkglsr qmigeflgnr qkqfnrdvld cvvdemdfsa
      601 meldealrkf qahirvqgea qkverlieaf sqrycvcnpg vvrqfrnpdt ifilafaiil
      661 lntdmyspnv kperkmkled fvknlrgvdd gedipretli giyerirkre lktnedhvsq
      721 vqkveklivg kkpigslhhg lgcvlslphr rlvcycrlfe vpdpnkpqkl glhqreiflf
      781 ndllvvtkif qkkknsvtys frqsfslygm qvllfenqyy pngirltsav pgadikvlin
      841 fnapnpqdrk kftddlresv aevqemekhr ieselekqkg vvrpsmsqcs slkkesgngt
      901 lsraclddsy asgeglkrsa lssslrdlse agkrgrrssa gslesnvegs iissphmrrr
      961 atstrecpsr ppqpvpnsss llgslfgsrr gkpppqahpp sapppappha hhpgpsegpl
     1021 hghhaqycha qqnpppyhhh hhyhppphlq hthqyhhgph sghppygaha hshpplptah
     1081 pghaghsahh hgqppapppp tsskakpsgi stvv
//
LOCUS       NP_001102022             761 aa            linear   ROD 28-APR-2025
DEFINITION  tripartite motif-containing protein 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102022 XP_001065758 XP_001065860 XP_342269
VERSION     NP_001102022.1
DBSOURCE    REFSEQ: accession NM_001108552.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Xu,K., Li,S., Yang,Q., Zhou,Z., Fu,M., Yang,X., Hao,K., Liu,Y. and
            Ji,H.
  TITLE     MicroRNA-145-5p targeting of TRIM2 mediates the apoptosis of
            retinal ganglion cells via the PI3K/AKT signaling pathway in
            glaucoma
  JOURNAL   J Gene Med 23 (11), e3378 (2021)
   PUBMED   34291866
  REMARK    GeneRIF: MicroRNA-145-5p targeting of TRIM2 mediates the apoptosis
            of retinal ganglion cells via the PI3K/AKT signaling pathway in
            glaucoma.
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Thompson,S., Pearson,A.N., Ashley,M.D., Jessick,V., Murphy,B.M.,
            Gafken,P., Henshall,D.C., Morris,K.T., Simon,R.P. and Meller,R.
  TITLE     Identification of a novel Bcl-2-interacting mediator of cell death
            (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and
            its role in rapid ischemic tolerance-induced neuroprotection
  JOURNAL   J Biol Chem 286 (22), 19331-19339 (2011)
   PUBMED   21478148
  REMARK    GeneRIF: a role for TRIM2 in mediating the p42/p44 MAPK-dependent
            ubiquitination of Bim in rapid ischemic tolerance.
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Balastik,M., Ferraguti,F., Pires-da Silva,A., Lee,T.H.,
            Alvarez-Bolado,G., Lu,K.P. and Gruss,P.
  TITLE     Deficiency in ubiquitin ligase TRIM2 causes accumulation of
            neurofilament light chain and neurodegeneration
  JOURNAL   Proc Natl Acad Sci U S A 105 (33), 12016-12021 (2008)
   PUBMED   18687884
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342269.3, XP_001065758.1, XP_001065860.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.11574.1,
                                           SRR26360172.2211236.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..761
                     /product="tripartite motif-containing protein 2 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 2; E3 ubiquitin-protein
                     ligase TRIM2; tripartite motif-containing protein 2;
                     RING-type E3 ubiquitin transferase TRIM2"
                     /calculated_mol_wt=83172
     Region          24..>126
                     /region_name="RAD18"
                     /note="RING-finger-containing E3 ubiquitin ligase [Signal
                     transduction mechanisms]; COG5432"
                     /db_xref="CDD:227719"
     Region          32..82
                     /region_name="RING-HC_TRIM2"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 2 (TRIM2); cd16767"
                     /db_xref="CDD:438423"
     Region          132..173
                     /region_name="Bbox2_TRIM2_C-VII"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 2 (TRIM2) and similar proteins;
                     cd19824"
                     /db_xref="CDD:380882"
     Region          178..304
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Site            order(182,185..186,188..190,193,196,210..211,214,217..218,
                     221..222,225,232..233,236,239..240,243..244,247,257..258,
                     261,265,268..269,272..273,275..276,284,287..288,291,
                     294..295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467844"
     Region          342..438
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          488..761
                     /region_name="NHL_TRIM2_like"
                     /note="NHL repeat domain of the tripartite
                     motif-containing protein 2 (TRIM2) and related proteins;
                     cd14960"
                     /db_xref="CDD:271330"
     Region          506..545
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          553..592
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          595..632
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          639..680
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          686..728
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          731..757
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     CDS             1..761
                     /gene="Trim2"
                     /coded_by="NM_001108552.3:244..2529"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361970"
                     /db_xref="RGD:1310981"
ORIGIN      
        1 mqragsrtag ptcqwsrmas egasipspvv rqidkqflic sicleryknp kvlpclhtfc
       61 erclqnyipa hsltlscpvc rqtsilpekg vaalqnnffi tnlmdvlqrt pgsngedpsi
      121 lqtvtavaag kplscpnhdg nvmefycqsc etamcrecte gehaehptvp lkdvveqhka
      181 slqvqldavn krlpeidsal qfiseiihql tnqkasivdd ihstfdelqk tlnvrksvll
      241 melevnyglk hkvlqsqldt llqgqesiks csnftaqaln hgtetevllv kkqmseklne
      301 ladqdfplhp rendqldfiv eteglkksih nlgtilttna vasetvatge glrqtiigqp
      361 msvtittkdk dgelcktgna yltaelstpd gsvadgeild nkngtyefly tvqkegdftl
      421 slrlydqhir gspfklkvir sadvsptteg vkrrvkspgs ghvkqkavkr pasmystgkr
      481 kenpieddli frvgtkgrnk geftnlqgva astsgkilia dsnnqcvqif sndgqfksrf
      541 girgrspgql qrptgvavhp sgdiiiadyd nkwvsifsnd gkfktkigsg klmgpkgvsv
      601 drnghiivvd nkaccvfifq pngkivtrfg srgngdrqfa gphfaavnss neiiitdfhn
      661 hsvkvfnqeg efmlkfgsng egngqfnapt gvavdsngni ivadwgnsri qvfdgsgsfl
      721 syintsadpl ygpqglalts dghvvvadsg nhcfkvyryl q
//
LOCUS       NP_001103621             539 aa            linear   ROD 28-APR-2025
DEFINITION  sorting nexin-27 isoform a [Rattus norvegicus].
ACCESSION   NP_001103621
VERSION     NP_001103621.1
DBSOURCE    REFSEQ: accession NM_001110151.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Yong,X.L.H., Zhang,L., Yang,L., Chen,X., Tan,J.Z.A., Yu,X.,
            Chandra,M., Livingstone,E., Widagdo,J., Vieira,M.M., Roche,K.W.,
            Lynch,J.W., Keramidas,A., Collins,B.M. and Anggono,V.
  TITLE     Regulation of NMDA receptor trafficking and gating by
            activity-dependent CaMKIIalpha phosphorylation of the GluN2A
            subunit
  JOURNAL   Cell Rep 36 (1), 109338 (2021)
   PUBMED   34233182
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Choi,H.J., Jang,H.J., Park,E., Tingskov,S.J., Norregaard,R.,
            Jung,H.J. and Kwon,T.H.
  TITLE     Sorting Nexin 27 Regulates the Lysosomal Degradation of Aquaporin-2
            Protein in the Kidney Collecting Duct
  JOURNAL   Cells 9 (5), 1208 (2020)
   PUBMED   32413996
  REMARK    GeneRIF: Sorting Nexin 27 Regulates the Lysosomal Degradation of
            Aquaporin-2 Protein in the Kidney Collecting Duct.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Halff,E.F., Szulc,B.R., Lesept,F. and Kittler,J.T.
  TITLE     SNX27-Mediated Recycling of Neuroligin-2 Regulates Inhibitory
            Signaling
  JOURNAL   Cell Rep 29 (9), 2599-2607 (2019)
   PUBMED   31775031
  REMARK    GeneRIF: SNX27-Mediated Recycling of Neuroligin-2 Regulates
            Inhibitory Signaling.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Binda,C.S., Nakamura,Y., Henley,J.M. and Wilkinson,K.A.
  TITLE     Sorting nexin 27 rescues neuroligin 2 from lysosomal degradation to
            control inhibitory synapse number
  JOURNAL   Biochem J 476 (2), 293-306 (2019)
   PUBMED   30602588
  REMARK    GeneRIF: these data indicate that NLGs are SNX27-retromer cargoes
            and suggest that SNX27-retromer controls inhibitory synapse number,
            at least in part through trafficking of NLG2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Lin,T.B., Lai,C.Y., Hsieh,M.C., Wang,H.H., Cheng,J.K., Chau,Y.P.,
            Chen,G.D. and Peng,H.Y.
  TITLE     VPS26A-SNX27 Interaction-Dependent mGluR5 Recycling in Dorsal Horn
            Neurons Mediates Neuropathic Pain in Rats
  JOURNAL   J Neurosci 35 (44), 14943-14955 (2015)
   PUBMED   26538661
  REMARK    GeneRIF: The regulation of the VPS26A-SNX27 interaction modifies
            mGluR5 trafficking which mediates neuropathic pain.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Lunn,M.L., Nassirpour,R., Arrabit,C., Tan,J., McLeod,I.,
            Arias,C.M., Sawchenko,P.E., Yates,J.R. 3rd and Slesinger,P.A.
  TITLE     A unique sorting nexin regulates trafficking of potassium channels
            via a PDZ domain interaction
  JOURNAL   Nat Neurosci 10 (10), 1249-1259 (2007)
   PUBMED   17828261
  REMARK    GeneRIF: SNX27 promotes the endosomal movement of Kir3 (GIRK)
            channels, leading to reduced surface expression, increased
            degradation and smaller Kir3 potassium currents.
REFERENCE   7  (residues 1 to 539)
  AUTHORS   MacNeil,A.J. and Pohajdak,B.
  TITLE     Polarization of endosomal SNX27 in migrating and tumor-engaged
            natural killer cells
  JOURNAL   Biochem Biophys Res Commun 361 (1), 146-150 (2007)
   PUBMED   17644068
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Lee,K.H., Ryu,C.J., Hong,H.J., Kim,J. and Lee,E.H.
  TITLE     CDNA microarray analysis of nerve growth factor-regulated gene
            expression profile in rat PC12 cells
  JOURNAL   Neurochem Res 30 (4), 533-540 (2005)
   PUBMED   16076023
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Fujiyama,K., Kajii,Y., Hiraoka,S. and Nishikawa,T.
  TITLE     Differential regulation by stimulants of neocortical expression of
            mrt1, arc, and homer1a mRNA in the rats treated with repeated
            methamphetamine
  JOURNAL   Synapse 49 (3), 143-149 (2003)
   PUBMED   12774298
  REMARK    GeneRIF: These findings suggest the differential regulation by
            stimulant of neocortical mrt1 expression and supports the view that
            stimulant induction of mrt1 may be involved in the early molecular
            signalings for stimulant sensitization.
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Kajii,Y., Muraoka,S., Hiraoka,S., Fujiyama,K., Umino,A. and
            Nishikawa,T.
  TITLE     A developmentally regulated and psychostimulant-inducible novel rat
            gene mrt1 encoding PDZ-PX proteins isolated in the neocortex
  JOURNAL   Mol Psychiatry 8 (4), 434-444 (2003)
   PUBMED   12740601
  REMARK    GeneRIF: Gene is developmentally regulated and stimulated by
            methamphetamine in the neocortex.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB051816.1, BF524912.1 and AC133978.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..539
                     /product="sorting nexin-27 isoform a"
                     /note="PDZ-protein Mrt1; MAP-responsive gene protein;
                     methamphetamine-responsive transcript 1 protein;
                     methamphetamine (MAP) responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=60854
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          40..132
                     /region_name="PDZ_SNX27-like"
                     /note="PDZ domain of sorting nexin-27 (SNX27), and related
                     domains; cd23070"
                     /db_xref="CDD:467283"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Site            order(50..56,80,83,112,116,119..120)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467283"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96L92; propagated from
                     UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          158..263
                     /region_name="PX_SNX27"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 27; cd06886"
                     /db_xref="CDD:132796"
     Site            order(194..196,219..220,233)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          271..363
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          271..360
                     /region_name="FERM-like region F1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          371..419
                     /region_name="FERM-like region F2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     Region          423..524
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     Region          423..523
                     /region_name="FERM-like region F3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4V4.2)"
     CDS             1..539
                     /gene="Snx27"
                     /gene_synonym="Mrt1"
                     /coded_by="NM_001110151.1:121..1740"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:260323"
                     /db_xref="RGD:628705"
ORIGIN      
        1 madedgegih psaphrnggg gggsglhcag ngggggggpr vvrivksesg ygfnvrgqvs
       61 eggqlrsing elyaplqhvs avlpggaadr agvrkgdril evngvnvega thkqvvdlir
      121 agekeliltv lsvppheadn ldpsddslgq sfydytekqa vpisvptykh veqngekfvv
      181 ynvymagrql cskryrefai lhqnlkrefa nftfprlpgk wpfslseqql darrrgleey
      241 lekvcsirvi gesdimqefl sesdenyngv sdvelrvalp dgatvtvrvk knsttdqvyq
      301 aiaakvgmds ttvnyfalfe vinhsfvrkl apnefphkly vqnytsavpg tcltirkwlf
      361 tteeevllnd ndlavtyffh qavddvkkgy ikaeeksyql qklyeqrkmv mylnmlrtce
      421 gyneiifphc acdsrrkghv itaisithfk lhacteegql enqviafewd emqrwdtdee
      481 gmafcfeyar gekkprwvki ftpyfnymhe cfervfcelk wrkenifqma rsqqrdvat
//
LOCUS       NP_001178925             498 aa            linear   ROD 28-APR-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF4 [Rattus
            norvegicus].
ACCESSION   NP_001178925 XP_576397
VERSION     NP_001178925.1
DBSOURCE    REFSEQ: accession NM_001191996.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Pouly,D., Chenaux,S., Martin,V., Babis,M., Koch,R., Nagoshi,E.,
            Katanaev,V.L., Gachon,F. and Staub,O.
  TITLE     USP2-45 Is a Circadian Clock Output Effector Regulating Calcium
            Absorption at the Post-Translational Level
  JOURNAL   PLoS One 11 (1), e0145155 (2016)
   PUBMED   26756164
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Zachos,N.C., Hodson,C., Kovbasnjuk,O., Li,X., Thelin,W.R., Cha,B.,
            Milgram,S. and Donowitz,M.
  TITLE     Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
            (NHERF4) dependent mechanism
  JOURNAL   Cell Physiol Biochem 22 (5-6), 693-704 (2008)
   PUBMED   19088451
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Scott,R.O., Thelin,W.R. and Milgram,S.L.
  TITLE     A novel PDZ protein regulates the activity of guanylyl cyclase C,
            the heat-stable enterotoxin receptor
  JOURNAL   J Biol Chem 277 (25), 22934-22941 (2002)
   PUBMED   11950846
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Gisler,S.M., Stagljar,I., Traebert,M., Bacic,D., Biber,J. and
            Murer,H.
  TITLE     Interaction of the type IIa Na/Pi cotransporter with PDZ proteins
  JOURNAL   J Biol Chem 276 (12), 9206-9213 (2001)
   PUBMED   11099500
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_576397.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.22689.1,
                                           SRR26643288.33331.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..498
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF4"
                     /note="PDZ domain containing 3"
                     /calculated_mol_wt=53463
     Region          48..127
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(59..65,76,79,108,112,115..116)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          156..233
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(166..170,181,184,213,217,220..221)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          262..344
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(272..278,292,295,324,328,331..332)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          <414..475
                     /region_name="PDZ"
                     /note="Domain present in PSD-95, Dlg, and ZO-1/2;
                     smart00228"
                     /db_xref="CDD:214570"
     CDS             1..498
                     /gene="Nherf4"
                     /gene_synonym="Pdzd3; RGD1559807"
                     /coded_by="NM_001191996.1:1..1497"
                     /db_xref="GeneID:500986"
                     /db_xref="RGD:1559807"
ORIGIN      
        1 meaaadlrdt alltlkfkfn prlgidnpvl slaedqdqsd pwnlhrprfc llskeeeksf
       61 gfhlqqqlgk adhvvcrvdp gssaqrqglr egdrilavnn nivehedyav vvryirasgp
      121 rvlltvlaqh vydvtraqqg neafpcptla sgvrprlchv vkdeggfgfs vthgargpfw
      181 lvlsaggaae ragvppgarl levngicvek ftynqlnrkl cqsgdrvtll vagpeveeqc
      241 hqlgmplaap laegwalpak prclniekgp qgfgfllree kgpdgrlgqf lwevdpglpa
      301 dkagmkagdr lvavagesmd glgheetvsr iraqgscvsl vvvdpeadrf fsmvrlspll
      361 flenteiaaa plaetkdlpv edtvepsgla gsrqcflypg pgggygfrlr cvasgpclfi
      421 sqvtpggsaa raglqmgdai levngcpvgg dsdldtlqql aeaepplrlk laprnsqgse
      481 awislesged wplasell
//
LOCUS       NP_001386685             291 aa            linear   ROD 28-APR-2025
DEFINITION  homeobox protein Hox-D8 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001386685 XP_038962311
VERSION     NP_001386685.1
DBSOURCE    REFSEQ: accession NM_001399756.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   van den Akker,E., Fromental-Ramain,C., de Graaff,W., Le
            Mouellic,H., Brulet,P., Chambon,P. and Deschamps,J.
  TITLE     Axial skeletal patterning in mice lacking all paralogous group 8
            Hox genes
  JOURNAL   Development 128 (10), 1911-1921 (2001)
   PUBMED   11311170
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Zappavigna,V., Renucci,A., Izpisua-Belmonte,J.C., Urier,G.,
            Peschle,C. and Duboule,D.
  TITLE     HOX4 genes encode transcription factors with potential auto- and
            cross-regulatory capacities
  JOURNAL   EMBO J 10 (13), 4177-4187 (1991)
   PUBMED   1756725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 13, 2022 this sequence version replaced XP_038962311.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.17199.1,
                                           SRR26643290.11916.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..291
                     /product="homeobox protein Hox-D8 isoform 2"
                     /note="homeobox protein Hox-D8-like"
                     /calculated_mol_wt=31384
     Region          143..275
                     /region_name="COG5576"
                     /note="Homeodomain-containing transcription factor
                     [Transcription]"
                     /db_xref="CDD:227863"
     Region          199..255
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..291
                     /gene="Hoxd8"
                     /coded_by="NM_001399756.1:204..1079"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100912936"
                     /db_xref="RGD:6489440"
ORIGIN      
        1 mssyfvnply skykaaaaaa aaaaaaaaag eainptyydc hfapevsgrh aaalqlygns
       61 aagfphappq ahahphpspp pgcgggggpg pgqnyfhaga gspvaayqaa ppppphpppp
      121 pppppcggia chgepakfyg ydnlqrqpif ttqqeaelvq ypdcksssgn igedpdhlnq
      181 ssspsqmfpw mrpqapgrrr grqtysrfqt lelekeflfn pyltrkrrie vshtlalter
      241 qvkiwfqnrr mkwkkennrd kfpasrpeak dgdpkkevsg leedgaegpt n
//
LOCUS       NP_001424727             691 aa            linear   ROD 28-APR-2025
DEFINITION  heat shock 70 kDa protein 12A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424727 XP_017444569
VERSION     NP_001424727.1
DBSOURCE    REFSEQ: accession NM_001437798.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_017444569.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.7347.1,
                                           SRR26643298.8715.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..691
                     /product="heat shock 70 kDa protein 12A isoform 1"
                     /note="heat shock 70kDa protein 12A; heat shock protein
                     12A"
                     /calculated_mol_wt=76640
     Region          73..539
                     /region_name="ASKHA_NBD_HSP70_HSPA12A"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 12A (HSPA12A) and similar proteins; cd11735"
                     /db_xref="CDD:466841"
     CDS             1..691
                     /gene="Hspa12a"
                     /coded_by="NM_001437798.1:239..2314"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:307997"
                     /db_xref="RGD:1305531"
ORIGIN      
        1 mmesvgvygf cgckgkskvk cdsrweitaa etaptsayss parslgdtgi tplspshiln
       61 dadpvseqqt flvvvaidfg ttssgyaysf tkepecihvm rrweggdpgv snqktpttil
      121 ltperkfhsf gyaardfyhd ldpneakqwl ylekfkmklh ttgdltmdtd ltaangkkvk
      181 aleiftyalq yfkeqalkel sdqagsdfen sdvrwvitvp aiwkqpakqf mreaayqagl
      241 aspenseqli ialepeaasi ycrklrlhqm ielsskavvn gysasdtvga gfaqakehvr
      301 rnrqsrtflv envigeiwse leegdkyvvv dsgggtvdlt vhqirlpegh lkelykatgg
      361 pygslgvdye fekllckifg edfieqfkik rpaawvdlmi afesrkraaa pdrtnplnit
      421 lpfsfidyyk kfrghsveha lrksnvdfvk wssqgmlrms pdamnalfkp tidsiiehlr
      481 dlfqkpevst vkflflvggf aeapllqqav qaafgdkcri iipqdvglti lkgavlfgld
      541 pavikvrrsp ltygvgvlnr yvegkhppek llvkdgtrwc tdvfdkfisa dqsvalgelv
      601 krsytpakps qlviiiniys senddvsfit dpgvkkcgtl rldltgtsga avparreiqt
      661 lmqfgdteik atavdiatsk svkvgidfln y
//
LOCUS       NP_001402776             632 aa            linear   ROD 28-APR-2025
DEFINITION  myotonin-protein kinase isoform 1 [Rattus norvegicus].
ACCESSION   NP_001402776 XP_008757265
VERSION     NP_001402776.1
DBSOURCE    REFSEQ: accession NM_001415847.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Damanafshan,A., Elzenaar,I., Samson-Couterie,B., van der Made,I.,
            Bourajjaj,M., van den Hoogenhof,M.M., van Veen,H.A., Picavet,D.I.,
            Beqqali,A., Ehler,E., De Windt,L.J., Pinto,Y.M. and van Oort,R.J.
  TITLE     The MEF2 transcriptional target DMPK induces loss of sarcomere
            structure and cardiomyopathy
  JOURNAL   Cardiovasc Res 114 (11), 1474-1486 (2018)
   PUBMED   29648621
  REMARK    GeneRIF: MEF2-induced loss of sarcomeres is mediated by DMPK via a
            decrease in sarcomeric gene expression by interfering with SRF
            transcriptional activity, leading to adverse cardiomyocyte
            remodelling and heart failure.
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Harmon,E.B., Harmon,M.L., Larsen,T.D., Yang,J., Glasford,J.W. and
            Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase is critical for nuclear envelope
            integrity
  JOURNAL   J Biol Chem 286 (46), 40296-40306 (2011)
   PUBMED   21949239
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Forner,F., Furlan,S. and Salvatori,S.
  TITLE     Mass spectrometry analysis of complexes formed by myotonic
            dystrophy protein kinase (DMPK)
  JOURNAL   Biochim Biophys Acta 1804 (6), 1334-1341 (2010)
   PUBMED   20188867
  REMARK    GeneRIF: DMPK peptides were identified by high-resolution mass
            spectrometry together with several putative DMPK-binding proteins,
            including several heat shock proteins such as HSP20/HSPB6,
            HSP60/CPN60, HSP70 and HSP90.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Harmon,E.B., Harmon,M.L., Larsen,T.D., Paulson,A.F. and
            Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase is expressed in embryonic
            myocytes and is required for myotube formation
  JOURNAL   Dev Dyn 237 (9), 2353-2366 (2008)
   PUBMED   18729234
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Andrade,A., de Leon,M.B., Hernandez-Hernandez,O., Cisneros,B. and
            Felix,R.
  TITLE     Myotonic dystrophy CTG repeat expansion alters Ca2+ channel
            functional expression in PC12 cells
  JOURNAL   FEBS Lett 581 (23), 4430-4438 (2007)
   PUBMED   17719582
  REMARK    GeneRIF: Data suggest modifications in the processing of N-type
            Ca(2+) channels in PC12 cells expressing the DM1 mutation.
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Mistry,D.J., Moorman,J.R., Reddy,S. and Mounsey,J.P.
  TITLE     Skeletal muscle Na currents in mice heterozygous for Six5
            deficiency
  JOURNAL   Physiol Genomics 6 (3), 153-158 (2001)
   PUBMED   11526199
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Muranyi,A., Zhang,R., Liu,F., Hirano,K., Ito,M., Epstein,H.F. and
            Hartshorne,D.J.
  TITLE     Myotonic dystrophy protein kinase phosphorylates the myosin
            phosphatase targeting subunit and inhibits myosin phosphatase
            activity
  JOURNAL   FEBS Lett 493 (2-3), 80-84 (2001)
   PUBMED   11287000
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Bush,E.W., Helmke,S.M., Birnbaum,R.A. and Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase domains mediate localization,
            oligomerization, novel catalytic activity, and autoinhibition
  JOURNAL   Biochemistry 39 (29), 8480-8490 (2000)
   PUBMED   10913253
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Benders,A.A., Groenen,P.J., Oerlemans,F.T., Veerkamp,J.H. and
            Wieringa,B.
  TITLE     Myotonic dystrophy protein kinase is involved in the modulation of
            the Ca2+ homeostasis in skeletal muscle cells
  JOURNAL   J Clin Invest 100 (6), 1440-1447 (1997)
   PUBMED   9294109
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Boucher,C.A., King,S.K., Carey,N., Krahe,R., Winchester,C.L.,
            Rahman,S., Creavin,T., Meghji,P., Bailey,M.E., Chartier,F.L. et al.
  TITLE     A novel homeodomain-encoding gene is associated with a large CpG
            island interrupted by the myotonic dystrophy unstable (CTG)n repeat
  JOURNAL   Hum Mol Genet 4 (10), 1919-1925 (1995)
   PUBMED   8595416
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 4, 2023 this sequence version replaced XP_008757265.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399481.774153.1,
                                           SRR22399481.1760942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..632
                     /product="myotonin-protein kinase isoform 1"
                     /EC_number="2.7.11.1"
                     /note="dystrophia myotonica kinase, B15; dystrophia
                     myotonica-protein kinase; myotonin-protein kinase"
                     /calculated_mol_wt=70094
     Region          69..406
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(77..80,83,85,98,100,132,148..151,195,199..200,202,
                     212..213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          472..532
                     /region_name="DMPK_coil"
                     /note="DMPK coiled coil domain like; pfam08826"
                     /db_xref="CDD:117396"
     CDS             1..632
                     /gene="Dmpk"
                     /gene_synonym="Dm15"
                     /coded_by="NM_001415847.1:138..2036"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308405"
                     /db_xref="RGD:1309825"
ORIGIN      
        1 msaevrlrql qqlvldpgfl gleplldlll gvhqelgash laqdkyvadf lqwvepiaar
       61 lkevrlqrdd feilkvigrg afsevavvkm kqtgqvyamk imnkwdmlkr gevscfreer
      121 dvlvkgdrrw itqlhfafqd enylylvmey yvggdlltll skfgeripae marfylaeiv
      181 maidsvhrlg yvhrdikpdn illdrcghir ladfgsclkl qpdgtvrslv avgtpdylsp
      241 eilqavgggp gagsygpecd wwalgvfaye mfygqtpfya dstaetyaki vhyrehlslp
      301 radmgvpeea qdlirgllcp aeirlgrgga gdfqkhpfff gldweglrds vppftpdfeg
      361 atdtcnfdvv edrltamvsg ggetlsdmqe dmalgvhlpf vgysyscmas rdnqvtdptp
      421 melealqlpv sdlqgldlpp pvsppdqaae eadpaavpvp paetetmvtl relqealeee
      481 vltrqslsre leairtanqn fssqlqeaev rnrdleahvr qlqermemlq apgaaavtgv
      541 pspratdpps hmaprpwlwa sarwwgqapc tavtccslpg slglayprri acscspllwl
      601 lpphwaalgw wpipavspqs gvsreppspp ep
//
LOCUS       NP_001028238             855 aa            linear   ROD 28-APR-2025
DEFINITION  phospholipase DDHD1 isoform 7 [Rattus norvegicus].
ACCESSION   NP_001028238 XP_223930
VERSION     NP_001028238.1
DBSOURCE    REFSEQ: accession NM_001033066.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Sep 9, 2005 this sequence version replaced XP_223930.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103649.1, SRR26643296.34070.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..855
                     /product="phospholipase DDHD1 isoform 7"
                     /note="phospholipase DDHD1"
                     /calculated_mol_wt=95043
     Region          594..840
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..855
                     /gene="Ddhd1"
                     /coded_by="NM_001033066.3:34..2601"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:305816"
                     /db_xref="RGD:1308576"
ORIGIN      
        1 mnypgrgapr sperngrggg awelgsdaag vfggggccfe hqpgdgvpls llraeplhla
       61 pgaddlshla ldpclsdeny dfssaesgss lryysegesa gggssssppp plvapnsggg
      121 gaagggpgdr krsrpggcaa rhryevvtel gpeevrwfyk edkktwkpfi gydslriela
      181 frsllqttgs rarsadrdgd rvcgptssfr eddedracgf cpravgpepe meelvtiepv
      241 cvrgglyevd vtqgecypvy wnqadkipvm rgqwfidgtw qpleeeesnl ieqehlscfr
      301 gqqmqenfdi emsksidgkd avhsfklsrn hvdwhsmdev ylysdattsk iartvtqklg
      361 fskasssgtr lhrgyveeat ledkpsqtsh ivfvvhgigq kmdqgriikn tammreaark
      421 ieekhfanha thveflpvew rskltldgdt vdsitpdkvr glrdmlnssa mdimyytspl
      481 yrdelvkglq qelnrlyslf csrnpdfeek ggkvsivshs lgcvitydim mgwnpvrlye
      541 qllqkeeelp derwmsyeer hlldelyitk rrlreiedrl hglkapsgsq tpalkfkven
      601 ffcmgsplav flalrgirpg ntgsqdhilp reicnrllni fhptdpvayr leplilkhys
      661 nispvqihwy ntsnplpyeh mkpnflnpak eptsasesen iaaipspvts pvlsrrhyge
      721 sitnigkasi lgaasigkgl ggmlfsrfgr sstpqpseps kdsaeeekkp vsspstttva
      781 tqtlphsssg fldsaleleh ridfelregl vesrywsavt shtaywssld valflltfmy
      841 khehdseakt sldsi
//
LOCUS       NP_001099380            1024 aa            linear   ROD 28-APR-2025
DEFINITION  delphilin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001099380 XP_001063541 XP_239604
VERSION     NP_001099380.2
DBSOURCE    REFSEQ: accession NM_001105910.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Takeuchi,T., Ohtsuki,G., Yoshida,T., Fukaya,M., Wainai,T.,
            Yamashita,M., Yamazaki,Y., Mori,H., Sakimura,K., Kawamoto,S.,
            Watanabe,M., Hirano,T. and Mishina,M.
  TITLE     Enhancement of both long-term depression induction and optokinetic
            response adaptation in mice lacking delphilin
  JOURNAL   PLoS One 3 (5), e2297 (2008)
   PUBMED   18509461
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Chaki,S., Yoshikawa,R. and Okuyama,S.
  TITLE     Group II metabotropic glutamate receptor-mediated regulation of
            dopamine release from slices of rat nucleus accumbens
  JOURNAL   Neurosci Lett 404 (1-2), 182-186 (2006)
   PUBMED   16781059
  REMARK    GeneRIF: Group II mGluRs may play a significant role in regulating
            dopamine release in the nucleus accumbens.
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Yamashita,T., Miyagi,Y., Ono,M., Ito,H., Watanabe,K., Sonoda,T.,
            Tsuzuki,K., Ozawa,S., Aoki,I., Okuda,K., Mishina,M. and Kawamoto,S.
  TITLE     Identification and characterization of a novel Delphilin variant
            with an alternative N-terminus
  JOURNAL   Brain Res Mol Brain Res 141 (1), 83-94 (2005)
   PUBMED   16168524
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   Miyagi,Y., Yamashita,T., Fukaya,M., Sonoda,T., Okuno,T., Yamada,K.,
            Watanabe,M., Nagashima,Y., Aoki,I., Okuda,K., Mishina,M. and
            Kawamoto,S.
  TITLE     Delphilin: a novel PDZ and formin homology domain-containing
            protein that synaptically colocalizes and interacts with glutamate
            receptor delta 2 subunit
  JOURNAL   J Neurosci 22 (3), 803-814 (2002)
   PUBMED   11826110
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Dec 7, 2020 this sequence version replaced NP_001099380.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.79647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418986, SAMN16418988
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..1024
                     /product="delphilin isoform 1"
                     /note="delphilin; glutamate receptor, ionotropic, delta 2
                     (Grid2) interacting protein 1"
                     /calculated_mol_wt=112299
     Region          90..163
                     /region_name="PDZ2_L-delphilin-like"
                     /note="PDZ domain 2 of delphilin (L-delphilin isoform),
                     and related domains; cd06744"
                     /db_xref="CDD:467226"
     Site            order(98..104,112,115,144,148,151..152)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467226"
     Region          199..278
                     /region_name="HN_L-delphilin-R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of
                     L-delphilin, and related domains; cd07355"
                     /db_xref="CDD:259821"
     Site            order(200,203,207,220,223,226..227,230)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259821"
     Region          633..1001
                     /region_name="FH2"
                     /note="Formin Homology 2 Domain; pfam02181"
                     /db_xref="CDD:396655"
     CDS             1..1024
                     /gene="Grid2ip"
                     /coded_by="NM_001105910.2:55..3129"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:288484"
                     /db_xref="RGD:1310492"
ORIGIN      
        1 msclgifipk khrarfdevv sqgllgklcr arraqgaqrl rrsrseerpe rllvstrasa
       61 aprrpdeppp rkaasllggr tgpggprrtv rvykgnksfg ftlrghgpvw iesvlpgspa
      121 enaslksgdr ilflngldmr ncshdkvvsm lqgsgamptl vveegpvpfa sdsdsldspt
      181 rasaltslqw vadilpssir vqgrtfsqql dhlltppery gvcralesff qhrsidtliv
      241 dvypvldtpa kqvlwqflyq lltyeeqelc qekiacflgy taitepessl dlepestpep
      301 tpepqprssl rassmcrrsl rsqgleasls cgpgdcsemp lplipgerqa gdgtslpetp
      361 npkmmsavya elesrlnsgf kgkigtvsks rasppvpslv gtsgprtlsg vswpgdrllp
      421 spcydplcsg glaspssses hpyasldssr apspqpglgs ihpdsppspd pirppsrrkl
      481 fafsrpvrsr dtdrfldvls eqlgprvtiv ddfltpendy eemsfhddqg sfvtnerssa
      541 secvssseeg ssltyssisd hipppplspp pppplpfhdp kpssrtsdgp rgppqsltkp
      601 ltqishpvpp ppppplpppv pcappmisrg vghrrsetsh msvkrlrweq vensegtiwg
      661 qlgedsdydk lsdmvkyldl elhfgtqkpp kpvpgpepfr kkevveilsh kkayntsill
      721 ahlkltpgel rqvlmsmepr rlepahlaql llfapdadee qryqafreap grlsepdqfv
      781 lqmlsvpeyk trlrslhfqa tlqekteeir gsleclrqas lelknsrkla kilefvlamg
      841 nylndgqpkt nkttgfkinf ltelnstktv dgkstflhil akslsqhfpe llgfaqdlpt
      901 vplaakvnqr altvdladlh dtvseiqvac qsmvpssedr favvmtsfle taqpalrald
      961 glqreameel gkalaffged skattseaff gifsefmskf eralsdlqag dgprssgmvs
     1021 plaw
//
LOCUS       NP_001418959            1615 aa            linear   ROD 28-APR-2025
DEFINITION  androglobin isoform 3 [Rattus norvegicus].
ACCESSION   NP_001418959 XP_063136864
VERSION     NP_001418959.1
DBSOURCE    REFSEQ: accession NM_001432030.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 24, 2024 this sequence version replaced XP_063136864.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.65.1,
                                           SRR26360181.439916.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1615
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..1615
                     /product="androglobin isoform 3"
                     /calculated_mol_wt=183677
     Region          86..>293
                     /region_name="CysPc"
                     /note="Calpains, domains IIa, IIb; calcium-dependent
                     cytoplasmic cysteine proteinases, papain-like. Functions
                     in cytoskeletal remodeling processes, cell
                     differentiation, apoptosis and signal transduction;
                     cl00051"
                     /db_xref="CDD:469591"
     Region          773..1185
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          774..780
                     /region_name="globin helix C"
                     /note="globin helix C [structural motif]"
                     /db_xref="CDD:412094"
     Region          789..794
                     /region_name="globin helix D"
                     /note="globin helix D [structural motif]"
                     /db_xref="CDD:412094"
     Region          796..816
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          827..836
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          849..867
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          876..899
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          922..940
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     Region          949..965
                     /region_name="globin helix A"
                     /note="globin helix A [structural motif]"
                     /db_xref="CDD:412094"
     Region          966..979
                     /region_name="globin helix B"
                     /note="globin helix B [structural motif]"
                     /db_xref="CDD:412094"
     Region          1304..>1599
                     /region_name="Caldesmon"
                     /note="pfam02029"
                     /db_xref="CDD:460421"
     CDS             1..1615
                     /gene="Adgb"
                     /gene_synonym="RGD1564259"
                     /coded_by="NM_001432030.1:78..4925"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:292477"
                     /db_xref="RGD:1564259"
ORIGIN      
        1 mtskqakrke vhrinsahgs dkskdnvppg sseqkrgkfp iwpewseadi naekwdagkg
       61 gkekdktgks pifhffedpe gkielpqslk vfswkrpqdf ifsripvvvk nemtfdlfss
      121 nghllcselm rwiiseiyav wkifnggils nyykgnsgel pilpwkpweh iyslckaakg
      181 hmplfnsygk yvvklywmgc wrkitvddfl pfdednnlll pattydfelw pmllskaiik
      241 lanvdihvah rrelgeltvi haltgwlpev iplhpayvdk vwellkeilp efklteepss
      301 eskitvienk lkeptkenkd vkdgkdgkdg kdgkeakdgk etkdgketkd akdfkpeisl
      361 ttlkapekgd raakekadak dlgkknkkdg ekekerfkfs lhgsrpssdv qysmqslsdc
      421 ssaiqspqmv vyatftplyl fenkiftlek mansaeklre yglshicshp vlvtrsrscp
      481 lvappkpppl pawklirhkk etvitdeaqd avpkkpeqfl eisspflnyr mapftiptet
      541 hfvqsvikkg tplgsslppl vesdlaasts qgemsiiagn qsqanialqt tpgkdepsep
      601 aladahqlea islerdlisl ttatldksqe elavnesvsk eiwldfedfc vcfhhiyifh
      661 kpnsyclnfq ksefkfmeer vpyylfvdsl kpiellvcfs alvrwgesga ltkesppvep
      721 glltaeaitw kslkplsvvl rihtyatkas mvrlpvgrhm llfnayspvg haihvcsmtt
      781 fvigdedvvl pnfepesyrf teqsvmimka ignvianfkd rgklpaalrd lqaahypipl
      841 nnkeltlqhf rvfhislwrl mkksqvakpp lnfkfafram vldtdlldsf sedaslaewv
      901 dlkysmpvne keyspeeiaa avkiqsmwkg nyvrllmkar tpetkenisv adtlqkiwav
      961 lemnleqyal sllrlmfksk cksmesypcy qdeetklafa dhtvnytdqp pnswfivfre
     1021 tflvpqdiil lpkvyttlqi cmlhvinndt leqvpkvfqk vvpylysknk kgytfvaeay
     1081 tgdsfvsgsr wklrligsyn plpflardtp cstftikeir dyyipndkki lfrysikvtm
     1141 aqsitiqvrt skpdafiklq vleseeiims tvgkgqalip afyflgneka lssqsskqvl
     1201 lthtlpkkep evltkkkagq pgqksfkgrt gggmtetgmp lleeevmsvp tieensstpq
     1261 qcykyiiqcl vlfnswplne tqltfvqalk dmekidikah vekheepapm gspdshavse
     1321 gqksvgmpkt trkgkersae keksarekqt prfepqqmqv ptaahsqqed pnkpywtlrl
     1381 vsehtdseyv dvkkdterad eiramkqawe ttepgraika sqarlkyltq fikkppetsa
     1441 patspealsv tqsqikssee vvvqsrspti letspqqirk alefldfnhy vrktadeavl
     1501 qtdelskhqa mqkaeeihqf rqyrarilsi rdidqeervk lkdevldmyg emrdsvdear
     1561 qkifdireey rnklleaerl rmealaaqea avkleaekkt aasdpqkkkk ggkkk
//
LOCUS       NP_001420019            1524 aa            linear   ROD 28-APR-2025
DEFINITION  glutamate-rich 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001420019 XP_017446848
VERSION     NP_001420019.1
DBSOURCE    REFSEQ: accession NM_001433090.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Aug 6, 2024 this sequence version replaced XP_017446848.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.16910.1,
                                           SRR26360172.754875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760433, SAMN12840107
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1524
                     /product="glutamate-rich 3 isoform 1"
                     /note="glutamate-rich protein 3"
                     /calculated_mol_wt=168017
     Region          299..414
                     /region_name="DUF4590"
                     /note="Domain of unknown function (DUF4590); pfam15257"
                     /db_xref="CDD:464597"
     Region          <979..1255
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <1217..1507
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     CDS             1..1524
                     /gene="Erich3"
                     /coded_by="NM_001433090.1:481..5055"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:295528"
                     /db_xref="RGD:1593279"
ORIGIN      
        1 mshshpagll atynsltdkh lagyfnntri rrhllrsgli trsgrilsek eykvnnmkqd
       61 hqkyirecla raifhkvldm eryrqleikr klddlarrer iqrlkgehtr rfiednmpil
      121 tphppagpkt nrghsvlaee grsspltlta prpytapgnm qppvrlqpll snrqirngsk
      181 itsgskpktl lleseapfpl agkkammkfr nymdnsqked lyqlphinsy qipvppspqp
      241 qaksfrenrl eawrrkrlrp itaphglepl ftkdpgriyk taphsnavit mvyfgknvhv
      301 syddidfrde ikiyqqhcgg enlcvykgkl lekdtfqfis krhhgypfsl tfylngiqvn
      361 rissccefkh rrssrlggkr gyfgfvcvek aspcyrciia mgldrkpssm kpkkdkiaek
      421 keeslkknqg klrkdrenap skrnemerke ssvsaafsae eiklgvkevr taieemewkg
      481 righsvweed qdnavkyvfg hecrstltvh fgadyeedfe idelkqdeke dgedqdddqm
      541 srgtkspteg ekdnlnpeke letssekald ardsenfedt gcsdseeddr qdlkttssis
      601 srshpysses edestevgge adsvnseges skssssqdlr ensdpgklhf paeeylgtei
      661 eeqeitkldg dngpwltels gthvteekpt kgsqallese pkesrqvass evraksellk
      721 eaglpwveev gqitgeaqkp ghgrstppgp sptddgvtpm rkpevnldrv veekavlssn
      781 eqpvqaaqem rtlkeeamek depsqsedtd asvglrekae mgedgtcrpq dadmdggpre
      841 kagmledgtc hpqdadtdgg lrekagiskv plgersptge qqasaeqvte tgqyplrias
      901 eveagtegsr rhgeeqlisi ekvaagasvf lsveqgvdrq rdedpdrqas lqtgmeegrt
      961 vsqgeqelek aaftdstgls setlgeaail keagtsevke aeremgspkp dgdqgkegal
     1021 aelevmgpvv dtgperedgs eeaalggera argrkeflea etpfssstge pqaspwedfp
     1081 gnheelsked taregiitdt esteerdvra vfpgelaaag gmekaerptp plretgsdre
     1141 eetgaevlkt edllehkvkg eeegtvrevg feeeacassh eteadtenae ptgatesgev
     1201 tklpeelpee rtitlfeatp qfekspeesa atntehqgge elpgqeseap wpqerglshd
     1261 gegllgapgp epadkaqgpe giftargeew aaeepdshve perleengpl qvqggdimrr
     1321 tqgnlpkerl travvcreae vekpqgegdg dkecspgtet vglivqnwit ggstveaqed
     1381 pqegeiedsa ewrevseesk sadgipmass sadaqqetwd ragealgeta neertltedm
     1441 tpraekvavv eevtsagama etqqeqapev qysrpgedre ggeakasqhp gmageetgat
     1501 rkdeehqtga agefrgsvsq seta
//
LOCUS       NP_058859                615 aa            linear   ROD 28-APR-2025
DEFINITION  sodium-dependent neutral amino acid transporter B(0)AT3 [Rattus
            norvegicus].
ACCESSION   NP_058859
VERSION     NP_058859.2
DBSOURCE    REFSEQ: accession NM_017163.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Fairweather,S.J., Broer,A., Subramanian,N., Tumer,E., Cheng,Q.,
            Schmoll,D., O'Mara,M.L. and Broer,S.
  TITLE     Molecular basis for the interaction of the mammalian amino acid
            transporters B0AT1 and B0AT3 with their ancillary protein
            collectrin
  JOURNAL   J Biol Chem 290 (40), 24308-24325 (2015)
   PUBMED   26240152
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Singer,D., Camargo,S.M., Huggel,K., Romeo,E., Danilczyk,U.,
            Kuba,K., Chesnov,S., Caron,M.G., Penninger,J.M. and Verrey,F.
  TITLE     Orphan transporter SLC6A18 is renal neutral amino acid transporter
            B0AT3
  JOURNAL   J Biol Chem 284 (30), 19953-19960 (2009)
   PUBMED   19478081
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Danilczyk,U., Sarao,R., Remy,C., Benabbas,C., Stange,G.,
            Richter,A., Arya,S., Pospisilik,J.A., Singer,D., Camargo,S.M.,
            Makrides,V., Ramadan,T., Verrey,F., Wagner,C.A. and Penninger,J.M.
  TITLE     Essential role for collectrin in renal amino acid transport
  JOURNAL   Nature 444 (7122), 1088-1091 (2006)
   PUBMED   17167413
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Baba,T., Nonoguchi,H., Itoh,K., Nakayama,Y., Kohda,Y., Inoue,T. and
            Tomita,K.
  TITLE     Gene regulation of renal-osmotic stress-induced Na-CL organic
            solute cotransporter
  JOURNAL   Nephron Exp Nephrol 96 (3), e89-e96 (2004)
   PUBMED   15056985
  REMARK    GeneRIF: Regulation of ROSIT mRNA levels in nephrons.
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Nash,S.R., Giros,B., Kingsmore,S.F., Kim,K.M., el-Mestikawy,S.,
            Dong,Q., Fumagalli,F., Seldin,M.F. and Caron,M.G.
  TITLE     Cloning, gene structure and genomic localization of an orphan
            transporter from mouse kidney with six alternatively-spliced
            isoforms
  JOURNAL   Recept Channels 6 (2), 113-128 (1998)
   PUBMED   9932288
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Wasserman,J.C., Delpire,E., Tonidandel,W., Kojima,R. and
            Gullans,S.R.
  TITLE     Molecular characterization of ROSIT, a renal osmotic stress-induced
            Na(+)-Cl(-)-organic solute cotransporter
  JOURNAL   Am J Physiol 267 (4 Pt 2), F688-F694 (1994)
   PUBMED   7943364
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Nov 26, 2020 this sequence version replaced NP_058859.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U12973.1, SRR26643287.271.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..615
                     /product="sodium-dependent neutral amino acid transporter
                     B(0)AT3"
                     /note="b(0)AT3; system B(0) neutral amino acid transporter
                     AT3; solute carrier family 6 (neutral amino acid
                     transporter), member 18; sodium- and chloride-dependent
                     transporter XTRP2; renal osmotic stress-induced Na-Cl
                     organic solute cotransporter; X transporter protein 2;
                     solute carrier family 6 (neurotransmitter transporter),
                     member 18"
                     /calculated_mol_wt=69436
     Region          16..591
                     /region_name="SLC6sbd_B0AT3"
                     /note="glycine transporter, B0AT3; solute-binding domain;
                     cd11517"
                     /db_xref="CDD:212086"
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            order(32,35,412,415..416)
                     /site_type="other"
                     /note="Na binding site 2 [ion binding]"
                     /db_xref="CDD:212086"
     Site            order(33..34,36..39,114,262..263,268,270,416,419..420)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:212086"
     Site            order(34,39,263,295)
                     /site_type="other"
                     /note="Na binding site 1 [ion binding]"
                     /db_xref="CDD:212086"
     Site            order(41..42,113,117,120,381,385)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:212086"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            398..418
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            443..463
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            473..493
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            521..541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     Site            572..592
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62687.1)"
     CDS             1..615
                     /gene="Slc6a18"
                     /gene_synonym="Rosit; Xtrp2"
                     /coded_by="NM_017163.2:31..1878"
                     /db_xref="GeneID:29323"
                     /db_xref="RGD:69352"
ORIGIN      
        1 maqasgmdpl vdiederpkw dnklqyllsc igfavglgni wrfpylchth gggaflipyf
       61 ialvfegipl fyielaigqr lrrgsigvwk tispylggvg lgcfsvsflv slyyntillw
      121 vlwfflnsfq hplpwstcpl dlnrtgfvqe cqssgtvsyf wyrqtlnits disntgtiqw
      181 klflclvacw ttvylcvirg iestgkviyf talfpylvlt iflirgltlp gategltylf
      241 tpnmkilqnp rvwldaatqi ffslslafgg hiafasynqp rnncekdavt ialvnsmtsl
      301 yasitifsim gfkasndygr cldrnilsli nefdfpelsi srdeypsvlm ylnatqperv
      361 arlplktchl edfldksasg pglafivfte avlhmpgasv wsvlffgmlf tlglssmfgn
      421 megvitplfd mgilpkgvpk etmtgvvcfi cflsaicftl qsgsywleif dsfaaslnli
      481 ifafmevvgv ihvygikrfc ddiewmtgrr pslywqvtwr vvspmllfgi flsyivllaq
      541 sspsykawnp qyehfpsree klypgwvqvt cvllsflpsl wvpgialaql lfqyrqrwkn
      601 thlesalkpq esrgc
//
LOCUS       NP_001092974             864 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor, 79 [Rattus norvegicus].
ACCESSION   NP_001092974 XP_001058868 XP_236799
VERSION     NP_001092974.1
DBSOURCE    REFSEQ: accession NM_001099504.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000009.1.
            
            On or before Aug 18, 2007 this sequence version replaced
            XP_001058868.1, XP_236799.4.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..864
                     /product="vomeronasal 2 receptor, 79"
                     /calculated_mol_wt=97971
     Region          47..506
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(74,171..172,396)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(112,115,158,245)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          514..576
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          597..847
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          597..621
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(599,602..603,606..607,609..610,644,648,651..652,660,
                     664)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          633..654
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(653,665..666,669..670,673,753,758,761..762,765,799,
                     802..803,806,810,818..819,822,825,829)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          663..687
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          711..727
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          754..780
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          788..811
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          816..841
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..864
                     /gene="Vom2r79"
                     /coded_by="NM_001099504.1:1..2595"
                     /db_xref="GeneID:301137"
                     /db_xref="RGD:1588571"
ORIGIN      
        1 mltmytlipy fltltlamll cnlvlpkcsi sltenvykeg dmvlnfflpl yvyqtsqhte
       61 gaesthiypr islnnyqfvm allfateein knslllpnms lgysiyiagp tqkdtvhnll
      121 twltgqenfl pnynckkeek svaaitgqtw eislligtvl glykypqlti gpfepkmndp
      181 vkfpslyqma tkesslalgm vslivhfrwn wvglitsddd kavhfvsdli pelerntvcv
      241 afiemisvth mffmnvndvy nspivrksak viiiygdsds slgvffrrwe hilpwriwvt
      301 tsqwevttam rhfmldsfhg tlifsqhhge iitfkdfvkt vtpakysndi flarlweiyf
      361 dcalsngtck sskncssrgs lewlpwyhfd mamspvsyhv ynavyavahs lhkivmqqid
      421 meemrnggrm kispwklnpi lkniqftnpg gdavtlnpse klhedydiln fwnfpqglgy
      481 kekvgtfsty fppgqqlsls edriqwntgd eqiptsvcse ncspgfrksf hegkyaccfe
      541 cslcpeneis ngtgkcmhaw kmyiddcvkc pedhyantvr thclrkavif ltyknslgmt
      601 fsgialclsl lttlvlgifv khqktpvvka nnitfsyill islifcflcs flfigepntp
      661 icilqqtvfg ivftvavstv laktitvvla fkisspgrrm kgllillapk fiilictliq
      721 iffcgiwlgt sppfvdkdsk sehgkiiilc nkgsvtafyc vlgylgslsi vtftvaflar
      781 nlpdmfneak fltfsmlifc svwitflpvy hsskgrimvv levlsiltss tgllgciffp
      841 kcyiillrpd rnslkvmkdn ilwk
//
LOCUS       NP_001388336             694 aa            linear   ROD 28-APR-2025
DEFINITION  THO complex subunit 5 homolog isoform 2 [Rattus norvegicus].
ACCESSION   NP_001388336 XP_006251400
VERSION     NP_001388336.1
DBSOURCE    REFSEQ: accession NM_001401407.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Wang,L., Miao,Y.L., Zheng,X., Lackford,B., Zhou,B., Han,L., Yao,C.,
            Ward,J.M., Burkholder,A., Lipchina,I., Fargo,D.C., Hochedlinger,K.,
            Shi,Y., Williams,C.J. and Hu,G.
  TITLE     The THO complex regulates pluripotency gene mRNA export and
            controls embryonic stem cell self-renewal and somatic cell
            reprogramming
  JOURNAL   Cell Stem Cell 13 (6), 676-690 (2013)
   PUBMED   24315442
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Katahira,J.
  TITLE     mRNA export and the TREX complex
  JOURNAL   Biochim Biophys Acta 1819 (6), 507-513 (2012)
   PUBMED   22178508
  REMARK    Review article
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Dominguez-Sanchez,M.S., Barroso,S., Gomez-Gonzalez,B., Luna,R. and
            Aguilera,A.
  TITLE     Genome instability and transcription elongation impairment in human
            cells depleted of THO/TREX
  JOURNAL   PLoS Genet 7 (12), e1002386 (2011)
   PUBMED   22144908
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Mancini,A., Niemann-Seyde,S.C., Pankow,R., El Bounkari,O.,
            Klebba-Farber,S., Koch,A., Jaworska,E., Spooncer,E., Gruber,A.D.,
            Whetton,A.D. and Tamura,T.
  TITLE     THOC5/FMIP, an mRNA export TREX complex protein, is essential for
            hematopoietic primitive cell survival in vivo
  JOURNAL   BMC Biol 8, 1 (2010)
   PUBMED   20051105
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Sjoblom,T., Jones,S., Wood,L.D., Parsons,D.W., Lin,J., Barber,T.D.,
            Mandelker,D., Leary,R.J., Ptak,J., Silliman,N., Szabo,S.,
            Buckhaults,P., Farrell,C., Meeh,P., Markowitz,S.D., Willis,J.,
            Dawson,D., Willson,J.K., Gazdar,A.F., Hartigan,J., Wu,L., Liu,C.,
            Parmigiani,G., Park,B.H., Bachman,K.E., Papadopoulos,N.,
            Vogelstein,B., Kinzler,K.W. and Velculescu,V.E.
  TITLE     The consensus coding sequences of human breast and colorectal
            cancers
  JOURNAL   Science 314 (5797), 268-274 (2006)
   PUBMED   16959974
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Masuda,S., Das,R., Cheng,H., Hurt,E., Dorman,N. and Reed,R.
  TITLE     Recruitment of the human TREX complex to mRNA during splicing
  JOURNAL   Genes Dev 19 (13), 1512-1517 (2005)
   PUBMED   15998806
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Guo,S., Hakimi,M.A., Baillat,D., Chen,X., Farber,M.J.,
            Klein-Szanto,A.J., Cooch,N.S., Godwin,A.K. and Shiekhattar,R.
  TITLE     Linking transcriptional elongation and messenger RNA export to
            metastatic breast cancers
  JOURNAL   Cancer Res 65 (8), 3011-3016 (2005)
   PUBMED   15833825
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Mancini,A., Koch,A., Whetton,A.D. and Tamura,T.
  TITLE     The M-CSF receptor substrate and interacting protein FMIP is
            governed in its subcellular localization by protein kinase
            C-mediated phosphorylation, and thereby potentiates M-CSF-mediated
            differentiation
  JOURNAL   Oncogene 23 (39), 6581-6589 (2004)
   PUBMED   15221008
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Tamura,T., Mancini,A., Joos,H., Koch,A., Hakim,C., Dumanski,J.,
            Weidner,K.M. and Niemann,H.
  TITLE     FMIP, a novel Fms-interacting protein, affects
            granulocyte/macrophage differentiation
  JOURNAL   Oncogene 18 (47), 6488-6495 (1999)
   PUBMED   10597251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 11, 2022 this sequence version replaced XP_006251400.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.745237.1,
                                           SRR26360194.1866911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..694
                     /product="THO complex subunit 5 homolog isoform 2"
                     /note="THO complex subunit 5 homolog; fms-interacting
                     protein; Fms interacting protein; THO complex 5"
                     /calculated_mol_wt=79879
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          2..199
                     /region_name="Interaction with THOC7.
                     /evidence=ECO:0000250|UniProtKB:Q13769"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          2..144
                     /region_name="Interaction with CSF1R.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          7..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          103..463
                     /region_name="FmiP_Thoc5"
                     /note="Fms-interacting protein/Thoc5; pfam09766"
                     /db_xref="CDD:462889"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     CDS             1..694
                     /gene="Thoc5"
                     /gene_synonym="Fmip"
                     /coded_by="NM_001401407.1:61..2145"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360972"
                     /db_xref="RGD:1304991"
ORIGIN      
        1 mssesskkrk pkvirsdgtp tegkrnrsdt eqegryysee aevdlrdpgr dyelykytcq
       61 elqrlmaeiq dlkskgskdv aieieerriq scvhfmtlkk lnrlahirlk kgrdqtheak
      121 qkvdayhlql qnllyevmhl qkeitkclef kskheeidlv sleefyseap pniskaeitm
      181 gdphqqtlar ldweleqrkr laekyrecls nkekilkeie vkkeylsslq prlnsimqas
      241 lpvqeylfmp fdqahkqyet arhlppplyv lfvqataygq acahmtssqp prqdktlsva
      301 iegsvdeaka lfkppedsqd desdsdaeee qttkrrrptl gvqlddkrke mlkrhplsvl
      361 ldlkckdnsv lhltffylmn lnimtvkakv ttamelitpi sagdllspds vlsclypgdh
      421 gkktpnpanq yqfdkvgilt lrdyvlelgh pylwvqklgg lhfpkeqpqh tvmadhsqsa
      481 shmettmkll ktrvqsrlal hkqfaslehg ivpvtsecqy lfpakvvsrl vkwmimahed
      541 ymelhftkdi veaglagdtn lyylalierg taklqaavvl npgyssippv frlclnwkge
      601 ktnsnddnir amesevnvcy relcgprpsh qlltnqlqrl cvlldvylet eshddsvegp
      661 kefpqekmcl rlfrgpsrmk pfkynhpqgf fshr
//
LOCUS       NP_001380623            1738 aa            linear   ROD 28-APR-2025
DEFINITION  sodium leak channel NALCN isoform 2 [Rattus norvegicus].
ACCESSION   NP_001380623
VERSION     NP_001380623.1
DBSOURCE    REFSEQ: accession NM_001393694.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1738)
  AUTHORS   Kang,Y., Wu,J.X. and Chen,L.
  TITLE     Structure of voltage-modulated sodium-selective NALCN-FAM155A
            channel complex
  JOURNAL   Nat Commun 11 (1), 6199 (2020)
   PUBMED   33273469
  REMARK    GeneRIF: Structure of voltage-modulated sodium-selective
            NALCN-FAM155A channel complex.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1738)
  AUTHORS   Al-Sayed,M.D., Al-Zaidan,H., Albakheet,A., Hakami,H., Kenana,R.,
            Al-Yafee,Y., Al-Dosary,M., Qari,A., Al-Sheddi,T., Al-Muheiza,M.,
            Al-Qubbaj,W., Lakmache,Y., Al-Hindi,H., Ghaziuddin,M., Colak,D. and
            Kaya,N.
  TITLE     Mutations in NALCN cause an autosomal-recessive syndrome with
            severe hypotonia, speech impairment, and cognitive delay
  JOURNAL   Am J Hum Genet 93 (4), 721-726 (2013)
   PUBMED   24075186
REFERENCE   3  (residues 1 to 1738)
  AUTHORS   Koroglu,C., Seven,M. and Tolun,A.
  TITLE     Recessive truncating NALCN mutation in infantile neuroaxonal
            dystrophy with facial dysmorphism
  JOURNAL   J Med Genet 50 (8), 515-520 (2013)
   PUBMED   23749988
REFERENCE   4  (residues 1 to 1738)
  AUTHORS   Lu,B., Su,Y., Das,S., Liu,J., Xia,J. and Ren,D.
  TITLE     The neuronal channel NALCN contributes resting sodium permeability
            and is required for normal respiratory rhythm
  JOURNAL   Cell 129 (2), 371-383 (2007)
   PUBMED   17448995
REFERENCE   5  (residues 1 to 1738)
  AUTHORS   Nash,H.A., Scott,R.L., Lear,B.C. and Allada,R.
  TITLE     An unusual cation channel mediates photic control of locomotion in
            Drosophila
  JOURNAL   Curr Biol 12 (24), 2152-2158 (2002)
   PUBMED   12498692
REFERENCE   6  (residues 1 to 1738)
  AUTHORS   Lee,J.H., Cribbs,L.L. and Perez-Reyes,E.
  TITLE     Cloning of a novel four repeat protein related to voltage-gated
            sodium and calcium channels
  JOURNAL   FEBS Lett 445 (2-3), 231-236 (1999)
   PUBMED   10094463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY555273.1, SRR26643298.58590.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1738
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q25"
     Protein         1..1738
                     /product="sodium leak channel NALCN isoform 2"
                     /note="sodium leak channel non-selective protein; sodium
                     leak channel NALCN; brain voltage-gated cation channel;
                     voltage gated channel-like protein 1; four domain-type
                     voltage-gated ion channel alpha-1 subunit; voltage gated
                     channel like 1; rb21-channel"
                     /calculated_mol_wt=200320
     Region          36..331
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            66..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            107..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            174..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            295..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          383..603
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            417..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            448..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            473..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            503..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            570..599
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          762..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          887..1161
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            887..906
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            916..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            948..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            981..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1016..1039
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            1130..1159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          1209..1458
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1211..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1237..1260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1272..1293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1297..1318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1332..1357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1421..1447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          1611..1679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     CDS             1..1738
                     /gene="Nalcn"
                     /gene_synonym="Vgcnl1"
                     /coded_by="NM_001393694.1:317..5533"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:266760"
                     /db_xref="RGD:628710"
ORIGIN      
        1 mlkrkqssrv eaqpvtdfgp deslsdnadi lwinkpwvhs llricaiisv isvcmntpmt
       61 fehypplqyv tftldtllmf lytaemiakm hirgivkgds syvkdrwcvf dgfmvfclwv
      121 slvlqvfeia divdqmspwg mlriprplim irafriyfrf elprtritni lkrsgeqiws
      181 vsifllffll lygilgvqmf gtftyhcvvn dtkpgnvtwn slaipdthcs peleegyqcp
      241 pgfkcmdled lglsrqelgy sgfneigtsi ftvyeassqe gwvflmyrai dsfprwrsyf
      301 yfitliffla wlvknvfiav iietfaeirv qfqqmwgtrs sttstattqm fhedaaggwq
      361 lvavdvnkpq grapaclqkm mrssvfhmfi lsmvtvdviv aasnyykgen frrqydefyl
      421 aevaftvlfd leallkiwcl gftgyisssl hkfelllvig ttlhvypdly hsqftyfqvl
      481 rvvrlikisp aledfvykif gpgkklgslv vftasllivm saislqmfcf veeldrfttf
      541 prafmsmfqi ltqegwvdvm dqtlnavghm waplvaiyfi lyhlfatlil lslfvavild
      601 nleldedlkk lkqlkqsean adtkeklplr lrifekfpnr pqmvkisklp sdftvpkire
      661 sfmkqfidrq qqdtcclfri lpstsssscd npkrptvedn kyidqklrks vfsirarnll
      721 eketavtkil ractrqrmls gsfegqpake rsilsvqhhi rqerrslrhg snsqrisrgk
      781 sletltqdhs ntvryrnaqr edseikmiqe kkeqaemkrk vqeeelrenh pyfdkplfiv
      841 grehrfrnfc rvvvrarfna sktdpvtgav kntkyhqlyd llglvtyldw vmitvticsc
      901 ismmfespfr rvmhaptlqi aeyvfvifms ielnlkimad glfftptavi rdfggvmdif
      961 iylvsliflc wmpqnvpaes gaqllmvlrc lrplrifklv pqmrkvvrel fsgfkeiflv
     1021 sillltlmlv fasfgvqlfa gklakcndpn iirredcngi frinvsvskn lnlklrpgek
     1081 kpgfwvprvw anprnfnfdn vgnamlalfe vlslkgwvev rdviihrvgp ihgiyihvfv
     1141 flgcmigltl fvgvvianfn enkgtalltv dqrrwedlks rlkiaqplhl pprpdndgfr
     1201 akmyditqhp ffkrtiallv laqsvllsvk wdvedpvtvp latmsvvftf ifvlevtmki
     1261 iamspagfwq srrnrydllv tslgvvwvvl hfallnayty mmgacvivfr ffsicgkhvt
     1321 lkmllltvvv smyksffiiv gmfllllcya fagvvlfgtv kygeninrha nfssagkait
     1381 vlfrivtged wnkimhdcmv qppfctpdef tywatdcgny agalmyfcsf yviiayimln
     1441 llvaiivenf slfysteedq llsyndlrhf qiiwnmvddk regviptfrv kfllrllrgr
     1501 levdldkdkl lfkhmcyeme rlhnggdvtf hdvlsmlsyr svdirkslql eellareqle
     1561 ytieeevakq tirmwlkkcl krirakqqqs csiihslres qqqelsrfln ppsiettqps
     1621 edtnansqdh ntqpesssqq qllsptlsdr ggsrqdaadt gkpqrkigqw rlpsapkpis
     1681 hsvssvnlrf ggrttmksvv ckmnpmpdta scgsevkkww trqltvesde sgddlldi
//
LOCUS       NP_001388306             803 aa            linear   ROD 28-APR-2025
DEFINITION  protein enabled homolog isoform 1 [Rattus norvegicus].
ACCESSION   NP_001388306 XP_038946855
VERSION     NP_001388306.1
DBSOURCE    REFSEQ: accession NM_001401377.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Deng,G., Luo,Y., Zhang,Y., Zhang,J. and He,Z.
  TITLE     Enabled homolog (ENAH) regulated by RNA binding protein splicing
            factor 3b subunit 4 (SF3B4) exacerbates the proliferation, invasion
            and migration of hepatocellular carcinoma cells via Notch signaling
            pathway
  JOURNAL   Bioengineered 13 (2), 2194-2206 (2022)
   PUBMED   35030977
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Wang,D.D., Chen,Y.B., Zhao,J.J., Zhang,X.F., Zhu,G.C., Weng,D.S.,
            Pan,K., Lv,L., Pan,Q.Z., Jiang,S.S., Wang,L.L. and Xia,J.C.
  TITLE     TES functions as a Mena-dependent tumor suppressor in gastric
            cancer carcinogenesis and metastasis
  JOURNAL   Cancer Commun (Lond) 39 (1), 3 (2019)
   PUBMED   30728082
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: The tetramerization domain (TD) at the C-termini of
            enabled/VASP proteins conferred the observed selectivity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 803)
  AUTHORS   Ram,R., Wescott,A.P., Varandas,K., Dirksen,R.T. and Blaxall,B.C.
  TITLE     Mena associates with Rac1 and modulates connexin 43 remodeling in
            cardiomyocytes
  JOURNAL   Am J Physiol Heart Circ Physiol 306 (1), H154-H159 (2014)
   PUBMED   24186093
  REMARK    GeneRIF: Mena is associated with active Rac1 in cardiomyocytes.
            Knockdown of Mena increased Rac1 activity, connexin43 expression
            and localization.
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Giesemann,T., Schwarz,G., Nawrotzki,R., Berhorster,K.,
            Rothkegel,M., Schluter,K., Schrader,N., Schindelin,H., Mendel,R.R.,
            Kirsch,J. and Jockusch,B.M.
  TITLE     Complex formation between the postsynaptic scaffolding protein
            gephyrin, profilin, and Mena: a possible link to the microfilament
            system
  JOURNAL   J Neurosci 23 (23), 8330-8339 (2003)
   PUBMED   12967995
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Tani,K., Sato,S., Sukezane,T., Kojima,H., Hirose,H., Hanafusa,H.
            and Shishido,T.
  TITLE     Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
            enabled (Mena) by c-Abl kinase
  JOURNAL   J Biol Chem 278 (24), 21685-21692 (2003)
   PUBMED   12672821
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Lanier,L.M., Gates,M.A., Witke,W., Menzies,A.S., Wehman,A.M.,
            Macklis,J.D., Kwiatkowski,D., Soriano,P. and Gertler,F.B.
  TITLE     Mena is required for neurulation and commissure formation
  JOURNAL   Neuron 22 (2), 313-325 (1999)
   PUBMED   10069337
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Yamabhai,M. and Kay,B.K.
  TITLE     Examining the specificity of Src homology 3 domain--ligand
            interactions with alkaline phosphatase fusion proteins
  JOURNAL   Anal Biochem 247 (1), 143-151 (1997)
   PUBMED   9126384
REFERENCE   10 (residues 1 to 803)
  AUTHORS   Gertler,F.B., Niebuhr,K., Reinhard,M., Wehland,J. and Soriano,P.
  TITLE     Mena, a relative of VASP and Drosophila Enabled, is implicated in
            the control of microfilament dynamics
  JOURNAL   Cell 87 (2), 227-239 (1996)
   PUBMED   8861907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Feb 10, 2022 this sequence version replaced XP_038946855.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..803
                     /product="protein enabled homolog isoform 1"
                     /note="protein enabled homolog"
                     /calculated_mol_wt=86152
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          <260..536
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          618..644
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(625..626,628..629,632,634..638)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          634..637
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          765..799
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..803
                     /gene="Enah"
                     /coded_by="NM_001401377.1:397..2808"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:360891"
                     /db_xref="RGD:1307666"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqeaaqsk
      121 vtatqdstnl rcifcgptlp rqnsqlpaqv qngpsqeeme iqrrqlqeqq rqkelererm
      181 ererlererl ererlererl eqeqlerqrq erehverler erlerlerer qdrerererl
      241 eqlereqvew ererrmsnaa pssdsslysa plpeysscqp psapppsyak visapvsdaa
      301 pdyavvtalp ptstpptppl rhsatrfats lgsafhpvlp hyatvprpln rnsrpsspvn
      361 tpssqppaak scawptsnfs plppsppimi ssppgkatgp rpvlpvcvss pvpqmppspt
      421 apngsldsvt ypvsppptsg paappppppp pppppppppp pplpplasls hcgsqasppp
      481 gtplastpss kpsvlpspsa aapasvetpl npelgdssas epglqaasqp aetpapqghv
      541 lgppappppp plpsgpayas alppppgppp ppplpsagpp pppppppplp nqvppppppp
      601 papplpasgi fsgsmsednr pltglaaaia gaklrkvsrv edgsfpsggn tvsvnlassk
      661 tdsgrgngpl plggsglmee msallarrrr iaekgstiet eqkedrseda epvtskaast
      721 stpeptrkpw ertntmngsk spvisrpkst pssqpsangv qtegldydrl kqdildemrk
      781 elaklkeeli dairqelsks nta
//
LOCUS       NP_001424031             608 aa            linear   ROD 28-APR-2025
DEFINITION  SLAIN motif-containing protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424031 XP_006250960
VERSION     NP_001424031.1
DBSOURCE    REFSEQ: accession NM_001437102.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   van der Vaart,B., Manatschal,C., Grigoriev,I., Olieric,V.,
            Gouveia,S.M., Bjelic,S., Demmers,J., Vorobjev,I., Hoogenraad,C.C.,
            Steinmetz,M.O. and Akhmanova,A.
  TITLE     SLAIN2 links microtubule plus end-tracking proteins and controls
            microtubule growth in interphase
  JOURNAL   J Cell Biol 193 (6), 1083-1099 (2011)
   PUBMED   21646404
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006250960.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.35311.1,
                                           SRR21887620.477105.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..608
                     /product="SLAIN motif-containing protein 2 isoform 2"
                     /note="SLAIN motif-containing protein 2"
                     /calculated_mol_wt=65300
     Region          130..608
                     /region_name="SLAIN"
                     /note="SLAIN motif-containing family; pfam15301"
                     /db_xref="CDD:464627"
     CDS             1..608
                     /gene="Slain2"
                     /gene_synonym="RGD1311593"
                     /coded_by="NM_001437102.1:197..2023"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305310"
                     /db_xref="RGD:1311593"
ORIGIN      
        1 medvnsnvna dqevrklqel vkklekqneq lrsrsgavqs agllgpgspa ragvstpssg
       61 aasprgfplg lgakasggag sgprrtssed lrdatsllaa gegglldeve plrpdelerl
      121 sgweeeeesw lysspkkklt pmqksvsplv wcrqvldyps pdvecakksl ihkldqtmsa
      181 lkrqnlynnp fnsmsysspy spnasspyss gfnspsstpv rppivkqlil pgnsgnfkss
      241 sdrnpplspq ssidselsas eldedsigsn yklndvtdvq ilarmqeesl rqeyaattsr
      301 rssgsscnst rrgtfsdqel daqslddedd smhhavypav nrfspsprns prpspkqspr
      361 nsprsrspar gieysraspq pmisrlqqpr lslqghptdl qtsnvkneek lrrslpnlsr
      421 tsntqvdsvk ssrsdsnfqv pnggiprmqp qasatasqrl kslprtplka kqvlptpstn
      481 rvpspgkfrs paapsplalr qpvkafsnhg sgsgsqettq ftqttsspgp pvvqntapan
      541 pssninsatl trpagtaamr sglprpsaps aggipvprsk lvqpvrrslp apktygsmkd
      601 dswkdgcy
//
LOCUS       NP_001416085             284 aa            linear   ROD 28-APR-2025
DEFINITION  receptor expression-enhancing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001416085 XP_008761214
VERSION     NP_001416085.1
DBSOURCE    REFSEQ: accession NM_001429156.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Hashimoto,Y., Shirane,M., Matsuzaki,F., Saita,S., Ohnishi,T. and
            Nakayama,K.I.
  TITLE     Protrudin regulates endoplasmic reticulum morphology and function
            associated with the pathogenesis of hereditary spastic paraplegia
  JOURNAL   J Biol Chem 289 (19), 12946-12961 (2014)
   PUBMED   24668814
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Bjork,S., Hurt,C.M., Ho,V.K. and Angelotti,T.
  TITLE     REEPs are membrane shaping adapter proteins that modulate specific
            g protein-coupled receptor trafficking by affecting ER cargo
            capacity
  JOURNAL   PLoS One 8 (10), e76366 (2013)
   PUBMED   24098485
  REMARK    Erratum:[PLoS One. 2013;8(12).
            doi:10.1371/annotation/6f86410c-63c3-4fcd-b1cb-9fd8d2ea95d0]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Park,S.H., Zhu,P.P., Parker,R.L. and Blackstone,C.
  TITLE     Hereditary spastic paraplegia proteins REEP1, spastin, and
            atlastin-1 coordinate microtubule interactions with the tubular ER
            network
  JOURNAL   J Clin Invest 120 (4), 1097-1110 (2010)
   PUBMED   20200447
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Saito,H., Kubota,M., Roberts,R.W., Chi,Q. and Matsunami,H.
  TITLE     RTP family members induce functional expression of mammalian
            odorant receptors
  JOURNAL   Cell 119 (5), 679-691 (2004)
   PUBMED   15550249
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 10, 2024 this sequence version replaced XP_008761214.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ217879.1, SRR26643296.13387.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..284
                     /product="receptor expression-enhancing protein 1 isoform
                     2"
                     /note="receptor expression-enhancing protein 1"
                     /calculated_mol_wt=31691
     Region          19..94
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     CDS             1..284
                     /gene="Reep1"
                     /gene_synonym="RGD1305230"
                     /coded_by="NM_001429156.1:102..956"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362384"
                     /db_xref="RGD:1305230"
ORIGIN      
        1 mvswiisrlv vlifgtlypa yysykavksk dikeyvkwmm ywiifalftt aetftdiflc
       61 wfpfyyelki afvawllspy tkgssllyrk fvhptlsske keiddclvqa kdrsydalvh
      121 fgkrglnvaa taavmaaskg qgalserlrs fsmqdlttir gdgapapsgp pppgsgrssg
      181 khgqpkmsrs asesagssvc tccstcrtrk vvegdvsegg vkswephqvq nplafsdeee
      241 edllefiyky kaprrtefpl eapprtlrsr frkkstsssa tett
//
LOCUS       NP_001402062             538 aa            linear   ROD 28-APR-2025
DEFINITION  monocarboxylate transporter 7 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001402062 XP_008766597
VERSION     NP_001402062.1
DBSOURCE    REFSEQ: accession NM_001415133.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Higuchi,K., Sugiyama,K., Tomabechi,R., Kishimoto,H. and Inoue,K.
  TITLE     Mammalian monocarboxylate transporter 7 (MCT7/Slc16a6) is a novel
            facilitative taurine transporter
  JOURNAL   J Biol Chem 298 (4), 101800 (2022)
   PUBMED   35257743
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Price,N.T., Jackson,V.N. and Halestrap,A.P.
  TITLE     Cloning and sequencing of four new mammalian monocarboxylate
            transporter (MCT) homologues confirms the existence of a
            transporter family with an ancient past
  JOURNAL   Biochem J 329 (Pt 2) (Pt 2), 321-328 (1998)
   PUBMED   9425115
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Dec 21, 2022 this sequence version replaced XP_008766597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1549423.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..538
                     /product="monocarboxylate transporter 7 isoform 2"
                     /note="monocarboxylate transporter 7B; solute carrier
                     family 16 (monocarboxylic acid transporters), member 6;
                     solute carrier family 16, member 6 (monocarboxylic acid
                     transporter 7); monocarboxylate transporter 6"
                     /calculated_mol_wt=59056
     Region          40..487
                     /region_name="MFS_MCT7"
                     /note="Monocarboxylate transporter 7 of the Major
                     Facilitator Superfamily of transporters; cd17422"
                     /db_xref="CDD:340980"
     Site            order(51..52,55..56,59,94,145..146,148..150,153,172,
                     175..176,179,316,319..320,323..325,328,355,359,410..411,
                     415,419,437,440..441,444..445,448)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340980"
     CDS             1..538
                     /gene="Slc16a6"
                     /gene_synonym="MCT 6; MCT 7; Mct7B"
                     /coded_by="NM_001415133.2:21..1637"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:303772"
                     /db_xref="RGD:735117"
ORIGIN      
        1 mklparhqse msersrmtqk nsklcsranv ytqvpdggwg wvvaasfffi evftygviks
       61 fgvffndlmd sfdesnskis wiisicvfim tftaplstil tnrfghrlvv mgggllisvg
      121 miaasfsqrv yqmyisigiv sglgycfsfl ptvtilsqyf dkrrsmvtav astgecfamf
      181 afapaitalk ehigwrysll fvgllqlnvm vcgallrpii ikgpgspkai pleprrevqy
      241 mlenektrts idsidsgvel ttspknvpse akreqevrve qqqtlvvgpk hsqkraplld
      301 fsilkdrsfi cytlfglfat lgffapslyi iplgislgih pdraafllst maiaevfgri
      361 gmglvlnrep irkiyielic villtvslfa ftfatefwgl mlcsvffgsm vgtiggthip
      421 llaeddvvgi ekmssaagvy vfiqsisgla gpplagllvd qskiysrafy scaagmalaa
      481 vclalvrpck kglcqnphsg enqtdghrgk alqdipedfl emdlgkcepr ahmkmdpv
//
LOCUS       NP_001421087             906 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 512B isoform 1 [Rattus norvegicus].
ACCESSION   NP_001421087
VERSION     NP_001421087.1
DBSOURCE    REFSEQ: accession NM_001434158.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 906)
  AUTHORS   Balestri,F., Barsotti,C., Lutzemberger,L., Camici,M. and Ipata,P.L.
  TITLE     Key role of uridine kinase and uridine phosphorylase in the
            homeostatic regulation of purine and pyrimidine salvage in brain
  JOURNAL   Neurochem Int 51 (8), 517-523 (2007)
   PUBMED   17643556
  REMARK    GeneRIF: At relatively high UTP and CTP levels the inhibition of
            uridine kinase channels uridine towards phosphorolysis. The
            ribose-1-phosphate is then transformed into PRPP, which is used for
            purine salvage synthesis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.10115.1,
                                           SRR26643293.20950.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..906
                     /product="zinc finger protein 512B isoform 1"
                     /note="uridine kinase-like 1"
                     /calculated_mol_wt=99053
     Region          <146..505
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          610..631
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          646..667
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..906
                     /gene="Zfp512b"
                     /gene_synonym="Urkl1; Znf512b"
                     /coded_by="NM_001434158.1:356..3076"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:311721"
                     /db_xref="RGD:1305284"
ORIGIN      
        1 mtesfcvggg rrlqgssksg pgkggsrkev qlpllqdppk lgmpvvhsgh tvpsqaplcf
       61 dpgnsasdkt egkkkgrpka enqalrdipl slmnqwkdef kahsrvkcpn sgcwlefpsi
      121 yglkyhyqrc qgvrgcgsgk rrpggasgqr ppgphptpal paqgaisdrl afpcpfceaa
      181 ftsktqlekh riwnhmdhpl papkpgpvsr pvtinrpvgv skpigvskpv tvgkpvgvsk
      241 pigiskpvtv srpipvtkpv tvsrpmqvsr pvpvtkpipi tkpvpltkhm pvtklvtvsk
      301 pvpltkpvpv srpivvskpv pvsrpiaisr htppckmvll sksenktlra tgknsnkkra
      361 adsldtcpil pkqarqenge ygpstvdqsv tfqlstdpsn ssllpgsrpl mgkealrpig
      421 pvsqpeedpe rtkhrrkqkt pkkftgeqps isgtfglkgl akaedkarvh rskkqegsgs
      481 eevrkkvlat pvtvskeapt pvahpapggp eeqwqraihe rgeavcptcn vvtrktlvgl
      541 kkhmevchkl qealkcqhcr kqfkskagln yhtmaehsak ptdaeasegg eqeererlrk
      601 vlkqmgrlrc pqegcgaafs slmgyqyhqr rcgkppcevd spsfpcthcg ktyrskaghd
      661 yhvrsehtap ppeeptdkip eaedllgver tpsgrirrts aqvavfhlqe iaedelardw
      721 tkrrmkddlv petarlnytr pglptlnpql leawknevke kghvncpndc ceaiyssvsg
      781 lkahfascsk gdhlvgkyrc llcpkefsse sgvkyhilkt hgenwfrtsa dppskhksqd
      841 slmprkekkk slsggkkrgr kpkersseep asklppnrdd wppggrdrga rsstgkkaga
      901 gkapek
//
LOCUS       NP_001420881            2639 aa            linear   ROD 28-APR-2025
DEFINITION  filamin-A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001420881 XP_006229632
VERSION     NP_001420881.1
DBSOURCE    REFSEQ: accession NM_001433952.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2639)
  AUTHORS   Shi,Y., Qiu,T., Wu,C., Yuan,W., Yao,X., Jiang,L., Wang,N., Wang,L.,
            Han,Q., Yang,G., Liu,X. and Sun,X.
  TITLE     Filamin A facilitates NLRP3 inflammasome activation during
            arsenic-induced nonalcoholic steatohepatitis
  JOURNAL   Environ Sci Pollut Res Int 30 (49), 107703-107715 (2023)
   PUBMED   37740811
  REMARK    GeneRIF: Filamin A facilitates NLRP3 inflammasome activation during
            arsenic-induced nonalcoholic steatohepatitis.
REFERENCE   2  (residues 1 to 2639)
  AUTHORS   Zou,M., Huang,C., Li,X., He,X., Chen,Y., Liao,W., Liao,Y., Sun,J.,
            Liu,Z., Zhong,L. and Bin,J.
  TITLE     Circular RNA expression profile and potential function of
            hsa_circRNA_101238 in human thoracic aortic dissection
  JOURNAL   Oncotarget 8 (47), 81825-81837 (2017)
   PUBMED   29137225
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2639)
  AUTHORS   Segura,I., Lange,C., Knevels,E., Moskalyuk,A., Pulizzi,R.,
            Eelen,G., Chaze,T., Tudor,C., Boulegue,C., Holt,M., Daelemans,D.,
            Matondo,M., Ghesquiere,B., Giugliano,M., Ruiz de Almodovar,C.,
            Dewerchin,M. and Carmeliet,P.
  TITLE     The Oxygen Sensor PHD2 Controls Dendritic Spines and Synapses via
            Modification of Filamin A
  JOURNAL   Cell Rep 14 (11), 2653-2667 (2016)
   PUBMED   26972007
REFERENCE   4  (residues 1 to 2639)
  AUTHORS   Tirupula,K.C., Ithychanda,S.S., Mohan,M.L., Naga Prasad,S.V.,
            Qin,J. and Karnik,S.S.
  TITLE     G protein-coupled receptors directly bind filamin A with high
            affinity and promote filamin phosphorylation
  JOURNAL   Biochemistry 54 (44), 6673-6683 (2015)
   PUBMED   26460884
REFERENCE   5  (residues 1 to 2639)
  AUTHORS   Cho,Y., Park,D. and Cavalli,V.
  TITLE     Filamin A is required in injured axons for HDAC5 activity and axon
            regeneration
  JOURNAL   J Biol Chem 290 (37), 22759-22770 (2015)
   PUBMED   26157139
REFERENCE   6  (residues 1 to 2639)
  AUTHORS   Liu,G., Thomas,L., Warren,R.A., Enns,C.A., Cunningham,C.C.,
            Hartwig,J.H. and Thomas,G.
  TITLE     Cytoskeletal protein ABP-280 directs the intracellular trafficking
            of furin and modulates proprotein processing in the endocytic
            pathway
  JOURNAL   J Cell Biol 139 (7), 1719-1733 (1997)
   PUBMED   9412467
REFERENCE   7  (residues 1 to 2639)
  AUTHORS   Ohta,Y., Stossel,T.P. and Hartwig,J.H.
  TITLE     Ligand-sensitive binding of actin-binding protein to immunoglobulin
            G Fc receptor I (Fc gamma RI)
  JOURNAL   Cell 67 (2), 275-282 (1991)
   PUBMED   1833070
REFERENCE   8  (residues 1 to 2639)
  AUTHORS   Gorlin,J.B., Yamin,R., Egan,S., Stewart,M., Stossel,T.P.,
            Kwiatkowski,D.J. and Hartwig,J.H.
  TITLE     Human endothelial actin-binding protein (ABP-280, nonmuscle
            filamin): a molecular leaf spring
  JOURNAL   J Cell Biol 111 (3), 1089-1105 (1990)
   PUBMED   2391361
REFERENCE   9  (residues 1 to 2639)
  AUTHORS   Ezzell,R.M., Kenney,D.M., Egan,S., Stossel,T.P. and Hartwig,J.H.
  TITLE     Localization of the domain of actin-binding protein that binds to
            membrane glycoprotein Ib and actin in human platelets
  JOURNAL   J Biol Chem 263 (26), 13303-13309 (1988)
   PUBMED   3138234
REFERENCE   10 (residues 1 to 2639)
  AUTHORS   Fox,J.E.
  TITLE     Identification of actin-binding protein as the protein linking the
            membrane skeleton to glycoproteins on platelet plasma membranes
  JOURNAL   J Biol Chem 260 (22), 11970-11977 (1985)
   PUBMED   4044584
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Oct 16, 2024 this sequence version replaced XP_006229632.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.61791.1,
                                           SRR26643285.23242.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2639
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..2639
                     /product="filamin-A isoform 2"
                     /note="actin binding protein 280; filamin, alpha;
                     Endothelial actin-binding protein 280); filamin A, alpha"
                     /calculated_mol_wt=280365
     Region          25..153
                     /region_name="CH_FLNA_rpt1"
                     /note="first calponin homology (CH) domain found in
                     filamin-A (FLN-A) and similar proteins; cd21308"
                     /db_xref="CDD:409157"
     Site            order(30..35,41..42,45,49,91..94,99..102,104..105,
                     108..109,111,120..128,133,135..136,138..139,142..143,146)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409157"
     Site            order(51,54..55,58..59,61,63,65..66,68..70,73,76,97..98)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409157"
     Region          156..269
                     /region_name="CH_FLNA_rpt2"
                     /note="second calponin homology (CH) domain found in
                     filamin-A (FLN-A) and similar proteins; cd21312"
                     /db_xref="CDD:409161"
     Site            order(168,172,220,222..223,226..227,229,238..246,253,
                     255..256,258..259,262..263,266)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409161"
     Site            order(226,230,233..235,240,244)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409161"
     Region          281..375
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          381..477
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          480..571
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          577..659
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          672..766
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          769..869
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          872..968
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          972..1064
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1067..1156
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1160..1252
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1256..1352
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1355..1442
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1448..1542
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1545..1639
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1642..1735
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          <1789..1853
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1860..1946
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2039..2128
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2230..2320
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2324..2415
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2421..2511
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2550..2638
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     CDS             1..2639
                     /gene="Flna"
                     /gene_synonym="RGD1560614"
                     /coded_by="NM_001433952.1:221..8140"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293860"
                     /db_xref="RGD:1560614"
ORIGIN      
        1 mssshsrsgq saagaspagg idtrdaempa tekdlaedap wkkiqqntft rwcnehlkcv
       61 skrianlqtd lsdglrlial levlsqkkmh rkhnqrptfr qmqlenvsva lefldresik
      121 lvsidskaiv dgnlklilgl iwtlilhysi smpmwdeeed eeakkqtpkq rllgwiqnkl
      181 pqlpitnfsr dwqsgralga lvdscapglc pdwdswdask pvnnareamq qaddwlgipq
      241 vitpeeivdp nvdehsvmty lsqfpkaklk pgaplrpkln pkkaraygpg ieptgnmvkk
      301 raeftvetrs agqgevlvyv edpaghqeea kvtanndknr tfsvwyvpev tgthkvtvlf
      361 agqhiakspf evyvdksqgd askvtaqgpg lepsgniank ttyfeiftag agigevevvi
      421 qdptgqkgtv epqleargds tyrcsyqptm egvhtvhvtf agvpiprspy tvtvgqacnp
      481 tacravgrgl qpkgvrvket adfkvytkga gsgelkvtvk gpkgeervkq kdlgdgvygf
      541 eyyptipgty tvtitwggqn igrspfevkv gtecgnqkvr awgpgleggi vgksadfvve
      601 aigddvgtlg fsvegpsqak iecddkgdgs cdvrywpqea geyavhvlcn sedirlspfm
      661 adireapqdf hpdrvkargp glektgvain kpaeftvdak hagkaplrvq vqdneghsve
      721 ttvkdngngt yscsyvprkp vkhtamvswg gvsipnspfr vnvgagshpn kvkvygpgva
      781 ktglkahept yftvdcteag qgdvsigikc apgvvgptea didfdiirnd ndtftvkytp
      841 cgagsytimv lfadqatpts pirvkvepsh daskvkaegp glnrtgvelg kpthftvnak
      901 tagkgkldvq fsglakgdav rdvdiidhhd ntytvkytpv qqgpvgvsvt yggdhipksp
      961 fsvgvspsld lskikvsglv dkvdvgkdqe ftvkskgagg qgkvaskivs psgaavpckv
     1021 epglgadnsv vrfvpreegp yevevtydgv pvpgspfpve avaptkpskv kafgpglqgg
     1081 nagsparfti dtkgagtggl gltvegpcea qlecldngdg tcsvsyvpte pgdyninilf
     1141 adthipgspf kahvvpcfda skvkcsgpgl eratagevgq fqvdcssags aeltieicse
     1201 aglpaevyiq dhgdgthtit yiplcpgayt vtikyggqpv pnfpsklqve pavdtsgvqc
     1261 ygpgiegqgv freattefsv daraltqtgg phvkarvanp sgnltdtyvq dcgdgtykve
     1321 ytpyeegvhs vdvtydgspv psspfqvpvt egcdpsrvrv hgpgiqsgtt nkpnkftvet
     1381 rgagtgglgl avegpseakm scmdnkdgsc sveyipyeag tyslnvtygg hqvpgspfkv
     1441 pvhdvtdask vkcsgpglsp gmvranlpqs fqvdtskagv aplqvkvqgp kglvepvdvv
     1501 dnadgtqtvn yvpsregsys isvlygeeev prspfkvkvl pthdaskvka sgpglnttgv
     1561 paslpvefti dakdagegll avqitdpegk pkkthiqdnh dgtytvayvp dvtgrytili
     1621 kyggdeipfs pyrvravptg daskctvtga gigptiqige etvitvdtka agkgkvtctv
     1681 ctpdgsevdv dvvenedgtf difytapqpg kyvicvrfgg ehvpnspfqv talagdqptv
     1741 qtplrpqqlp sqytypqgsq qtwiperpmv gvngldvtsl rpfdlvipft ikkgeitgev
     1801 rmpsgkvaqp sitdnkdgtv tvryspseag lhemdirydn mhipgsplqf yvdyvncghi
     1861 taygpglthg vvnkpatftv ntkdageggl slaiegpska eisctdnqdg tcsvsylpvl
     1921 pgdysilvky ndqhipgspf tarvtgddsm rmshlkvgsa adipiniset dlslltatvv
     1981 ppsgreepcl lkrlrnghvg isfvpketge hlvhvkkngq hvasspipvv isqseigdas
     2041 rvrvsgqglh eghtfepaef iidtrdagyg glslsiegps kvdintedle dgtcrvtycp
     2101 tepgnyiini kfadqhvpgs pfsvkvtgeg rvkesitrrr rapsvanvgs hcdlslkipe
     2161 isiqdmtaqv tspsgkthea eivegenhty cirfvpaemg mhtvsvkykg qhvpgspfqf
     2221 tvgplgegga hkvraggpgl eraeagvpae fgiwtreaga gglaiavegp skaeisfedr
     2281 kdgscgvayv vqepgdyevs vkfneehipd spfvvpvasp sgdarrltvs slqesglkvn
     2341 qpasfavsln gakgaidakv hspsgaleec yvteidqdky avrfipreng vylidvkfng
     2401 thipgspfki rvgepghggd pglvsaygag leggvtgspa efivntsnag agalsvtidg
     2461 pskvkmdcqe cpegyrvtyt pmapgsylis ikyggpyhig gspfkakvtg prlvsnhslh
     2521 etssvfvdsl tkvatvpqha tsgpgpadvs kvvakglgls kayvgqksnf tvdcskagnn
     2581 mllvgvhgpr tpceeilvkh mgsrlysvsy llkdkgeytl vvkwgdehip gspyrimvp
//
LOCUS       NP_001092934             859 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor, 8 [Rattus norvegicus].
ACCESSION   NP_001092934 XP_001064636
VERSION     NP_001092934.1
DBSOURCE    REFSEQ: accession NM_001099464.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 19, 2007 this sequence version replaced XP_001064636.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..859
                     /product="vomeronasal 2 receptor, 8"
                     /calculated_mol_wt=99042
     Region          43..503
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          511..564
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          584..835
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          584..609
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(587,590..591,594..595,597..598,632,636,639..640,648,
                     652)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          621..642
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(641,653..654,657..658,661,741,746,749..750,753,787,
                     790..791,794,798,806..807,810,813,817)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          651..675
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          699..715
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          742..768
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          776..799
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          804..829
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..859
                     /gene="Vom2r8"
                     /coded_by="NM_001099464.1:1..2580"
                     /db_xref="GeneID:685641"
                     /db_xref="RGD:1591372"
ORIGIN      
        1 mfswifiqll lhlpnffcvf itfniskcyy kiteafhqkg dvvigaffpi htyytgnkip
       61 hsflpyyyvd nylqynfkny qyilalifai eeinenpnll snislgfdfy nvrftekdtl
      121 mnaciwltah rekyilpnyk cgkkhftaal tgtswttsaq mgtlfqlfkf pqlsfgpydh
      181 ilsdrnqyss lyqmapmass lslgivsllv hfrwswvgli lpddhkgnti lsdfrnemer
      241 kgvciaflkm ipatwmshfn kfwknmdetn viiiygdids leglmrnigq rlltwkvwvm
      301 niephviady fmldsfhgsl ifthhyteri eftnfvqtvn pykypediyl pklwylffkc
      361 sfsdidcqll nncqfnasld ilprhifdvs msdesisiyn avyavahslh emrlqqvqmq
      421 pyengeeimf fpwqvisfll ycnvsilidq rsldwrqkfn teydiinlwn lpnglgrkvk
      481 vgsfstnapq ghqlslteqi iqwpeefsei prsvcsescg hgfrklaleg kavccykctp
      541 cadneisnet dvdqclkcpe shyanteknh clqkavsfla yqdplgmsla sialclstlt
      601 afvigifvky rdtpivkann qalsyillit ltfcflcslt figqpnkdtc imqqitfgvv
      661 ftvalatvla kaitvviafk atfpgrmirw lmksrapnyi ipictliqvf icgiwmatsp
      721 pfidqdfhae hghiiifcnk gssvafhctl gylcflalgg ytmaflsrtl pdsfneskfl
      781 slsllvffcv witflpvyhs tmgkfmvate ifsilassia llsfifapkc yiilfrpnen
      841 tfhyirdkmh srrnkslkt
//
LOCUS       NP_001418483             520 aa            linear   ROD 28-APR-2025
DEFINITION  methyl-CpG-binding protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001418483 XP_038955462
VERSION     NP_001418483.1
DBSOURCE    REFSEQ: accession NM_001431554.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Lee,C.C., Park,K.B., Kim,M.S. and Jeon,Y.D.
  TITLE     CBP Expression Contributes to Neuropathic Pain via CREB and MeCP2
            Regulation in the Spared Nerve Injury Rat Model
  JOURNAL   Medicina (Kaunas) 60 (6), 989 (2024)
   PUBMED   38929606
  REMARK    GeneRIF: CBP Expression Contributes to Neuropathic Pain via CREB
            and MeCP2 Regulation in the Spared Nerve Injury Rat Model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Zuo,C., Fan,P., Yang,Y. and Hu,C.
  TITLE     MiR-488-3p facilitates wound healing through CYP1B1-mediated
            Wnt/beta-catenin signaling pathway by targeting MeCP2
  JOURNAL   J Diabetes Investig 15 (2), 145-158 (2024)
   PUBMED   37961023
  REMARK    GeneRIF: MiR-488-3p facilitates wound healing through
            CYP1B1-mediated Wnt/beta-catenin signaling pathway by targeting
            MeCP2.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Xu,M., Qi,S., Calhoun,V., Dai,J., Yu,B., Zhang,K., Pei,M., Li,C.,
            Wei,Y., Jiang,R., Zhi,D., Huang,Z., Qiu,Z., Liang,Z. and Sui,J.
  TITLE     Aberrant brain functional and structural developments in MECP2
            duplication rats
  JOURNAL   Neurobiol Dis 173, 105838 (2022)
   PUBMED   35985556
  REMARK    GeneRIF: Aberrant brain functional and structural developments in
            MECP2 duplication rats.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Choi,M., Ko,S.Y., Seo,J.Y., Kim,D.G., Lee,H., Chung,H. and Son,H.
  TITLE     Autistic-like social deficits in hippocampal MeCP2 knockdown rat
            models are rescued by ketamine
  JOURNAL   BMB Rep 55 (5), 238-243 (2022)
   PUBMED   35410641
  REMARK    GeneRIF: Autistic-like social deficits in hippocampal MeCP2
            knockdown rat models are rescued by ketamine.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Mao,X. and Yin,Z.
  TITLE     Inhibition of miR-205 promotes proliferation, migration and
            fibrosis of tenocytes through targeting MECP2: Implications for
            rotator cuff injury
  JOURNAL   Adv Clin Exp Med 31 (4), 437-443 (2022)
   PUBMED   35166074
  REMARK    GeneRIF: Inhibition of miR-205 promotes proliferation, migration
            and fibrosis of tenocytes through targeting MECP2: Implications for
            rotator cuff injury.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Rountree,M.R., Bachman,K.E. and Baylin,S.B.
  TITLE     DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex
            at replication foci
  JOURNAL   Nat Genet 25 (3), 269-277 (2000)
   PUBMED   10888872
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Coy,J.F., Sedlacek,Z., Bachner,D., Delius,H. and Poustka,A.
  TITLE     A complex pattern of evolutionary conservation and alternative
            polyadenylation within the long 3'-untranslated region of the
            methyl-CpG-binding protein 2 gene (MeCP2) suggests a regulatory
            role in gene expression
  JOURNAL   Hum Mol Genet 8 (7), 1253-1262 (1999)
   PUBMED   10369871
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Nan,X., Campoy,F.J. and Bird,A.
  TITLE     MeCP2 is a transcriptional repressor with abundant binding sites in
            genomic chromatin
  JOURNAL   Cell 88 (4), 471-481 (1997)
   PUBMED   9038338
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Tate,P., Skarnes,W. and Bird,A.
  TITLE     The methyl-CpG binding protein MeCP2 is essential for embryonic
            development in the mouse
  JOURNAL   Nat Genet 12 (2), 205-208 (1996)
   PUBMED   8563762
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Lewis,J.D., Meehan,R.R., Henzel,W.J., Maurer-Fogy,I., Jeppesen,P.,
            Klein,F. and Bird,A.
  TITLE     Purification, sequence, and cellular localization of a novel
            chromosomal protein that binds to methylated DNA
  JOURNAL   Cell 69 (6), 905-914 (1992)
   PUBMED   1606614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 18, 2024 this sequence version replaced XP_038955462.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2062536.1,
                                           SRR26643296.41138.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN16676807,
                                           SAMN16676810 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..520
                     /product="methyl-CpG-binding protein 2 isoform 1"
                     /note="meCP-2 protein"
                     /calculated_mol_wt=54951
     Region          120..197
                     /region_name="MBD"
                     /note="Methyl-CpG binding domain; smart00391"
                     /db_xref="CDD:128673"
     Site            order(135,137,139,147,149,158,161,165)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     CDS             1..520
                     /gene="Mecp2"
                     /gene_synonym="MECP2_e1"
                     /coded_by="NM_001431554.1:10..1572"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29386"
                     /db_xref="RGD:3075"
ORIGIN      
        1 maaaaaaaaa aaaaaaaaaa aaaaapsggg ggeeerleek sedqdlqglk ekplkfkkvk
       61 kdkkedkegk heplqpsahh saepaeagka etsessgsap avpeasaspk qrrsiirdrg
      121 pmyddptlpe gwtrklkqrk sgrsagkydv ylinpqgkaf rskveliayf ekvgdtsldp
      181 ndfdftvtgr gspsrreqkp pkkpkspkap gtgrgrgrpk gsgtgrpkaa asegvqvkrv
      241 lekspgkllv kmpfqaspgg kgegggatts aqvmvikrpg rkrkaeadpq aipkkrgrkp
      301 gsvvaaaaae akkkavkess irsvqetvlp ikkrktretv sievkevvkp llvstlgeks
      361 gkglktcksp grkskesspk grsssasspp kkehhhhhhh aespkapmpl lppppppepq
      421 ssedpisppe pqdlsssick eekmpragsl esdgcpkepa ktqpmvaaaa tttttttttv
      481 aekykhrgeg erkdivsssm prpnreepvd srtpvtervs
//
LOCUS       NP_001382022             955 aa            linear   ROD 28-APR-2025
DEFINITION  AP-2 complex subunit alpha-1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001382022 XP_006229127
VERSION     NP_001382022.1
DBSOURCE    REFSEQ: accession NM_001395093.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Capella,P., Asensio,J., Troncoso,M., Sosa,M.A. and Seltzer,A.M.
  TITLE     Evidence on differential role for alpha 1 and alpha 2 subtypes of
            AP-2 adaptin in the central nervous system
  JOURNAL   Neurosci Lett 808, 137282 (2023)
   PUBMED   37127089
  REMARK    GeneRIF: Evidence on differential role for alpha 1 and alpha 2
            subtypes of AP-2 adaptin in the central nervous system.
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Moulakakis,C., Steinhauser,C., Biedziak,D., Freundt,K., Reiling,N.
            and Stamme,C.
  TITLE     Surfactant Protein A Enhances Constitutive Immune Functions of
            Clathrin Heavy Chain and Clathrin Adaptor Protein 2
  JOURNAL   Am J Respir Cell Mol Biol 55 (1), 92-104 (2016)
   PUBMED   26771574
  REMARK    GeneRIF: SP-A transiently enhances the basal protein expression of
            CHC and alpha-adaptin.
REFERENCE   4  (residues 1 to 955)
  AUTHORS   Zhao,Z., Sagare,A.P., Ma,Q., Halliday,M.R., Kong,P., Kisler,K.,
            Winkler,E.A., Ramanathan,A., Kanekiyo,T., Bu,G., Owens,N.C.,
            Rege,S.V., Si,G., Ahuja,A., Zhu,D., Miller,C.A., Schneider,J.A.,
            Maeda,M., Maeda,T., Sugawara,T., Ichida,J.K. and Zlokovic,B.V.
  TITLE     Central role for PICALM in amyloid-beta blood-brain barrier
            transcytosis and clearance
  JOURNAL   Nat Neurosci 18 (7), 978-987 (2015)
   PUBMED   26005850
  REMARK    Erratum:[Nat Neurosci. 2024 Jan;27(1):208. doi:
            10.1038/s41593-023-01509-y. PMID: 37985802]
REFERENCE   5  (residues 1 to 955)
  AUTHORS   Onishi,K., Shafer,B., Lo,C., Tissir,F., Goffinet,A.M. and Zou,Y.
  TITLE     Antagonistic functions of Dishevelleds regulate Frizzled3
            endocytosis via filopodia tips in Wnt-mediated growth cone guidance
  JOURNAL   J Neurosci 33 (49), 19071-19085 (2013)
   PUBMED   24305805
REFERENCE   6  (residues 1 to 955)
  AUTHORS   Di Paolo,G., Sankaranarayanan,S., Wenk,M.R., Daniell,L.,
            Perucco,E., Caldarone,B.J., Flavell,R., Picciotto,M.R., Ryan,T.A.,
            Cremona,O. and De Camilli,P.
  TITLE     Decreased synaptic vesicle recycling efficiency and cognitive
            deficits in amphiphysin 1 knockout mice
  JOURNAL   Neuron 33 (5), 789-804 (2002)
   PUBMED   11879655
REFERENCE   7  (residues 1 to 955)
  AUTHORS   Kamiguchi,H. and Yoshihara,F.
  TITLE     The role of endocytic l1 trafficking in polarized adhesion and
            migration of nerve growth cones
  JOURNAL   J Neurosci 21 (23), 9194-9203 (2001)
   PUBMED   11717353
REFERENCE   8  (residues 1 to 955)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   9  (residues 1 to 955)
  AUTHORS   Chen,H., Slepnev,V.I., Di Fiore,P.P. and De Camilli,P.
  TITLE     The interaction of epsin and Eps15 with the clathrin adaptor AP-2
            is inhibited by mitotic phosphorylation and enhanced by
            stimulation-dependent dephosphorylation in nerve terminals
  JOURNAL   J Biol Chem 274 (6), 3257-3260 (1999)
   PUBMED   9920862
REFERENCE   10 (residues 1 to 955)
  AUTHORS   Slepnev,V.I., Ochoa,G.C., Butler,M.H., Grabs,D. and De Camilli,P.
  TITLE     Role of phosphorylation in regulation of the assembly of endocytic
            coat complexes
  JOURNAL   Science 281 (5378), 821-824 (1998)
   PUBMED   9694653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 3, 2021 this sequence version replaced XP_006229127.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN12840115, SAMN16676788
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..955
                     /product="AP-2 complex subunit alpha-1 isoform 2"
                     /note="AP-2 complex subunit alpha-1; adaptor protein
                     complex AP-2, alpha 1 subunit; alpha-adaptin A;
                     adaptor-related protein complex 2, alpha 1 subunit"
                     /calculated_mol_wt=105321
     Region          29..591
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          332..355
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          369..398
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          408..434
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          733..836
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          842..950
                     /region_name="Alpha_adaptin_C"
                     /note="Alpha adaptin AP2, C-terminal domain; pfam02296"
                     /db_xref="CDD:426707"
     CDS             1..955
                     /gene="Ap2a1"
                     /coded_by="NM_001395093.1:114..2981"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308578"
                     /db_xref="RGD:1306254"
ORIGIN      
        1 mpavskgdgm rglavfisdi rnckskeaei krinkelani rskfkgdkal dgyskkkyvc
       61 kllfifllgh didfghmeav nllssnkyte kqigylfisv lvnsnselir linnaikndl
      121 asrnptfmcl alhcianvgs remgeafaad iprilvagds mdsvkqsaal cllrlykasp
      181 dlvpmgewta rvvhllndqh mgvvtaavsl itclckknpd dfktcvslav srlsrivssa
      241 stdlqdytyy fvpapwlsvk llrllqcypp pedaavkgrl vecletvlnk aqeppkskkv
      301 qhsnaknail fetisliihy dsepnllvra cnqlgqflqh retnlrylal esmctlasse
      361 fsheavkthi dtvinalkte rdvsvrqraa dllyamcdrs nakqivseml ryletadyai
      421 reeivlkvai laekyavdys wyvdtilnli riagdyvsee vwyrvlqivt nrddvqgyaa
      481 ktvfealqap achenmvkvg gyilgefgnl iagdprsspp vqfsllhskf hlcsvatral
      541 llstyikfin lfpetkatiq gvlragsqlr nadvelqqra veyltlssva stdvlatvle
      601 emppfperes silaklkrkk gpgaasaldd srrdtssndi nggveptpsn vstpspsadl
      661 lglraapppa appapvggnl lvdvfsdgpt aqpslgptpe eaflspgped igppipeade
      721 llnkfvckns gvlfenqllq igvksefrqn lgrmylfygn ktsvqfqsfl ptvvhpgdlq
      781 tqlavqtkrv aaqvdggaqv qqvlnieclr dfltppllsv rfryggtaqs ltlklpvtin
      841 kffqptemaa qdffqrwkql slplqeaqki fkanhpmdae vtkakllgfg salldnvdpn
      901 penfvgagii qtkalqvgcl lrlepnaqaq myrltlrtsk epvsrhlcel laqqf
//
LOCUS       NP_036982                423 aa            linear   ROD 28-APR-2025
DEFINITION  growth hormone-releasing hormone receptor isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_036982 XP_346704 XP_347373
VERSION     NP_036982.1
DBSOURCE    REFSEQ: accession NM_012850.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Florea,V., Majid,S.S., Kanashiro-Takeuchi,R.M., Cai,R.Z.,
            Block,N.L., Schally,A.V., Hare,J.M. and Rodrigues,C.O.
  TITLE     Agonists of growth hormone-releasing hormone stimulate self-renewal
            of cardiac stem cells and promote their survival
  JOURNAL   Proc Natl Acad Sci U S A 111 (48), 17260-17265 (2014)
   PUBMED   25404316
  REMARK    GeneRIF: Data show that cardiac stem cells (CSCs) isolated from
            mouse, rat and pig myocardium express growth hormone-releasing
            hormone receptor (GHRH-R) and agonists of GHRH-R stimulate their
            proliferation and survival.
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Epitacio-Pereira,C.C., Silva,G.M., Salvatori,R., Santana,J.A.,
            Pereira,F.A., Gois-Junior,M.B., Britto,A.V., Oliveira,C.R.,
            Souza,A.H., Santos,E.G., Campos,V.C., Pereira,R.M., Valenca,E.H.,
            Barbosa,R.A., Farias,M.I., de Paula,F.J., Ribeiro,T.V.,
            Oliveira,M.C. and Aguiar-Oliveira,M.H.
  TITLE     Isolated GH deficiency due to a GHRH receptor mutation causes hip
            joint problems and genu valgum, and reduces size but not density of
            trabecular and mixed bone
  JOURNAL   J Clin Endocrinol Metab 98 (11), E1710-E1715 (2013)
   PUBMED   24057284
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Leggett,J., Harper,E., Waite,E., Marks,P., Martinez,A. and
            Lightman,S.
  TITLE     GHRH receptor-targeted botulinum neurotoxin selectively inhibits
            pulsatile GH secretion in male rats
  JOURNAL   Endocrinology 154 (9), 3305-3318 (2013)
   PUBMED   23825127
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Weigent,D.A.
  TITLE     Expression of lymphocyte-derived growth hormone (GH) and
            GH-releasing hormone receptors in aging rats
  JOURNAL   Cell Immunol 282 (2), 71-78 (2013)
   PUBMED   23770714
  REMARK    GeneRIF: Data show alterations in growth hormone (GH) synthesis and
            expression of GH-releasing hormone receptor (GHRH receptor) on
            cells of the immune system that may play a role in the immune
            response in aging.
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Penna,C., Settanni,F., Tullio,F., Trovato,L., Pagliaro,P.,
            Alloatti,G., Ghigo,E. and Granata,R.
  TITLE     GH-releasing hormone induces cardioprotection in isolated male rat
            heart via activation of RISK and SAFE pathways
  JOURNAL   Endocrinology 154 (4), 1624-1635 (2013)
   PUBMED   23417421
  REMARK    GeneRIF: GHRH protects the heart from I/R injury through
            GHRHR-mediated mechanisms, leading to activation of RISK and SAFE
            pathways, which converge on mitochondria and possibly on
            AMP-activated protein kinase.
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Lin,C., Lin,S.C., Chang,C.P. and Rosenfeld,M.G.
  TITLE     Pit-1-dependent expression of the receptor for growth hormone
            releasing factor mediates pituitary cell growth
  JOURNAL   Nature 360 (6406), 765-768 (1992)
   PUBMED   1334535
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Mayo,K.E.
  TITLE     Molecular cloning and expression of a pituitary-specific receptor
            for growth hormone-releasing hormone
  JOURNAL   Mol Endocrinol 6 (10), 1734-1744 (1992)
   PUBMED   1333056
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Wilson,D.B. and Wyatt,D.P.
  TITLE     Adrenocorticotropic cell distribution in adult and embryonic
            pituitaries of the little (lit) mutant mouse
  JOURNAL   Anat Embryol (Berl) 186 (4), 347-353 (1992)
   PUBMED   1329576
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Beamer,W.H. and Eicher,E.M.
  TITLE     Stimulation of growth in the little mouse
  JOURNAL   J Endocrinol 71 (1), 37-45 (1976)
   PUBMED   978118
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Eicher,E.M. and Beamer,W.G.
  TITLE     Inherited ateliotic dwarfism in mice. Characteristics of the
            mutation, little, on chromosome 6
  JOURNAL   J Hered 67 (2), 87-91 (1976)
   PUBMED   1270792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On or before Dec 17, 2003 this sequence version replaced
            XP_346704.1, XP_347373.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L01407.1, SRR26360172.1980141.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..423
                     /product="growth hormone-releasing hormone receptor
                     isoform 1 precursor"
                     /note="GRFR; GRF receptor; GHRH receptor; growth
                     hormone-releasing factor receptor; Growth hormone -
                     releasing receptor"
                     /calculated_mol_wt=44460
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2475
     Region          54..112
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          126..393
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          129..153
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          162..183
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          203..225
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          244..260
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          278..301
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          328..350
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          355..380
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..423
                     /gene="Ghrhr"
                     /gene_synonym="GHRHREC"
                     /coded_by="NM_012850.3:86..1357"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25321"
                     /db_xref="RGD:2688"
ORIGIN      
        1 mdsllwatwv lcllnlwgva lghlhlecdf itqlrddela clqaaegtnn ssmgcpgtwd
       61 gllcwpptgs gqwvslpcpe ffshfgsdpg avkrdctitg wsdpfppypv acpvplellt
      121 eeksyfstvk iiyttghsis ivalcvaiai lvalrrlhcp rnyihtqlfa tfilkasavf
      181 lkdaavfqgd stdhcsmsti lckvsvavsh fatmtnfswl laeavylscl lastsprskp
      241 afwwlvlagw glpvlctgtw vgcklafedt acwdlddssp ywwiikgpiv lsvgvnfglf
      301 lniicillrk lgpaqgglht raqywrlsks tllliplfgi hyiifnflpd saglgirlpl
      361 elglgsfqgf vvavlycfln qevrteisrk wyghdpellp arrtctewtt pprsrvkvlt
      421 sec
//
LOCUS       NP_001421221             575 aa            linear   ROD 28-APR-2025
DEFINITION  far upstream element-binding protein 3 isoform a [Rattus
            norvegicus].
ACCESSION   NP_001421221 XP_006233983
VERSION     NP_001421221.1
DBSOURCE    REFSEQ: accession NM_001434292.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Zivraj,K.H., Rehbein,M., Olschlager-Schutt,J., Schob,C., Falley,K.,
            Buck,F., Schweizer,M., Schepis,A., Kremmer,E., Richter,D.,
            Kreienkamp,H.J. and Kindler,S.
  TITLE     The RNA-binding protein MARTA2 regulates dendritic targeting of
            MAP2 mRNAs in rat neurons
  JOURNAL   J Neurochem 124 (5), 670-684 (2013)
   PUBMED   23121659
  REMARK    GeneRIF: in neurons MARTA2 appears to represent a key trans-acting
            factor involved in dendritic targeting of MAP2 mRNAs.
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Weber,A., Kristiansen,I., Johannsen,M., Oelrich,B., Scholmann,K.,
            Gunia,S., May,M., Meyer,H.A., Behnke,S., Moch,H. and Kristiansen,G.
  TITLE     The FUSE binding proteins FBP1 and FBP3 are potential c-myc
            regulators in renal, but not in prostate and bladder cancer
  JOURNAL   BMC Cancer 8, 369 (2008)
   PUBMED   19087307
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Davis-Smyth,T., Duncan,R.C., Zheng,T., Michelotti,G. and Levens,D.
  TITLE     The far upstream element-binding proteins comprise an ancient
            family of single-strand DNA-binding transactivators
  JOURNAL   J Biol Chem 271 (49), 31679-31687 (1996)
   PUBMED   8940189
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Wu,C., Narayan,P. and Puett,D.
  TITLE     Protein engineering of a novel constitutively active
            hormone-receptor complex
  JOURNAL   J Biol Chem 271 (49), 31638-31642 (1996)
   PUBMED   8940183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 24, 2024 this sequence version replaced XP_006233983.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.9823.1,
                                           SRR26643299.13377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..575
                     /product="far upstream element-binding protein 3 isoform
                     a"
                     /note="MAP2 RNA trans-acting protein 2; far upstream
                     element (FUSE) binding protein 3"
                     /calculated_mol_wt=61819
     Region          78..148
                     /region_name="KH-I_FUBP3_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22480"
                     /db_xref="CDD:411908"
     Site            order(87,89..91,93..97,100..101,104..105,110..113)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411908"
     Region          159..241
                     /region_name="KH-I_FUBP3_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22483"
                     /db_xref="CDD:411911"
     Site            order(172,174..176,178..182,185..186,189..190,195..198)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411911"
     Region          252..321
                     /region_name="KH-I_FUBP3_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22486"
                     /db_xref="CDD:411914"
     Site            order(262..267,269..273,276..277,286,288..289,299)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411914"
     Region          356..424
                     /region_name="KH-I_FUBP3_rpt4"
                     /note="fourth type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22489"
                     /db_xref="CDD:411917"
     Site            order(363..364,366..368,370..371,373..374,377..378,382,
                     387,389..390,392,403)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411917"
     CDS             1..575
                     /gene="Fubp3"
                     /gene_synonym="Marta2"
                     /coded_by="NM_001434292.1:81..1808"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:362106"
                     /db_xref="RGD:1307004"
ORIGIN      
        1 maelvqgqsa pvglkaedfv dalhrvrqia akidsiphln nstplvdpsv ygygvqkrpl
       61 ddgvgnqlga lvhqravite efkvpdkmvg fiigrggeqi sriqaesgck iqiasessgi
      121 perpcvltgt pesieqakrl lgqivdrcrn gpgfhndidg nstiqellip askvglvigk
      181 ggetikqlqe rtgvkmvmiq dgplptgadk plritgdpfk vqqaremvle iirekdqadf
      241 rgvrsdftsr agggsievsv prfvvgivig rngemikkiq ndagvriqfk pddgispera
      301 aqvmgppdrc qhaariinel iltaqereil ggltgtrgrg rgrgdwsvgt pggiqeityt
      361 vpadkcglvi gkggeniksi nqqsgahvel qrnpppntdp nlriftirga pqqievarhl
      421 idekvggasl gaptafgqsp fsqppaaphq ntfpprafpn iaakvngnph stpvsgppaf
      481 ltqgwgstyq awqqptqqvp sqqsqpqnsq pdyskawedy ykkqghttsa apqassppdy
      541 tmawaeyyrq qaafygqtlg qaqahsqvcs qspap
//
LOCUS       NP_001387845             721 aa            linear   ROD 28-APR-2025
DEFINITION  putative methyltransferase NSUN7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001387845 XP_006251008
VERSION     NP_001387845.1
DBSOURCE    REFSEQ: accession NM_001400916.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Harris,T., Marquez,B., Suarez,S. and Schimenti,J.
  TITLE     Sperm motility defects and infertility in male mice with a mutation
            in Nsun7, a member of the Sun domain-containing family of putative
            RNA methyltransferases
  JOURNAL   Biol Reprod 77 (2), 376-382 (2007)
   PUBMED   17442852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jan 28, 2022 this sequence version replaced XP_006251008.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1743851.1,
                                           SRR26643293.56921.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..721
                     /product="putative methyltransferase NSUN7 isoform 1"
                     /note="Williams-Beuren syndrome critical region protein
                     20; NOL1/NOP2/Sun domain family, member 7; putative
                     methyltransferase NSUN7"
                     /calculated_mol_wt=81003
     CDS             1..721
                     /gene="Nsun7"
                     /gene_synonym="RGD1310137"
                     /coded_by="NM_001400916.1:525..2690"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305339"
                     /db_xref="RGD:1310137"
ORIGIN      
        1 mldpnsamdf fdqenmeels qlaslemsgd lvskrkpsaa lekssypdsv yvtaanifqg
       61 iriqrpadkv iinygdellp sswtqaeeds fqrlsyelaf stlkyqdile silidtdifs
      121 sttipdqlns liivmlydfq drkfqprvlp ndavtipevq evenllnsfk tklaaalarc
      181 rikhdalsiy hilpetvrkq eqrastlply awinigkvsl eevyddlrkk gfdkvksiay
      241 lndkvfavdq hcfnvlifps hfkrellnid likdyklifq dksrslavhs vkalinmddd
      301 ilmvntgswy tvahmsilts gntskifvcg ieseekdsda kklftkmgce nieilhetfl
      361 siepkdqrlq nvkvilllpr csslgvsnpv efilnehedt sllqdlsqgg lpkdklqifa
      421 qqqfeqltha mkfakaqaiv yctcsvseee neevvkkale fqspalklqp yrlsppvlpl
      481 cslkeielsm drffrlepsd itngcflsil trerdpsetv svkdvlaraa akglldgvev
      541 gktlkrdkkr kkakaplpka ppqadlahdh ssvtgadnsi qmkiteflhr eskasavktp
      601 lpakpvpqva assqirkpsk plstplvrtt rpsekagsfg rprpegkgip lkpveiilpp
      661 vtfpfsspqg prfqmpgthf yyrfigskvg vpshltsmsr rkekakesvp ssfvrhprpw
      721 l
//
LOCUS       NP_942055                522 aa            linear   ROD 28-APR-2025
DEFINITION  monocarboxylate transporter 7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_942055 XP_221245
VERSION     NP_942055.1
DBSOURCE    REFSEQ: accession NM_198760.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Higuchi,K., Sugiyama,K., Tomabechi,R., Kishimoto,H. and Inoue,K.
  TITLE     Mammalian monocarboxylate transporter 7 (MCT7/Slc16a6) is a novel
            facilitative taurine transporter
  JOURNAL   J Biol Chem 298 (4), 101800 (2022)
   PUBMED   35257743
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Price,N.T., Jackson,V.N. and Halestrap,A.P.
  TITLE     Cloning and sequencing of four new mammalian monocarboxylate
            transporter (MCT) homologues confirms the existence of a
            transporter family with an ancient past
  JOURNAL   Biochem J 329 (Pt 2) (Pt 2), 321-328 (1998)
   PUBMED   9425115
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Feb 10, 2005 this sequence version replaced XP_221245.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY325107.1, SRR26360194.2284374.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..522
                     /product="monocarboxylate transporter 7 isoform 1"
                     /note="monocarboxylate transporter 7B; solute carrier
                     family 16 (monocarboxylic acid transporters), member 6;
                     solute carrier family 16, member 6 (monocarboxylic acid
                     transporter 7); monocarboxylate transporter 6"
                     /calculated_mol_wt=57130
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Region          24..471
                     /region_name="MFS_MCT7"
                     /note="Monocarboxylate transporter 7 of the Major
                     Facilitator Superfamily of transporters; cd17422"
                     /db_xref="CDD:340980"
     Site            order(35..36,39..40,43,78,129..130,132..134,137,156,
                     159..160,163,300,303..304,307..309,312,339,343,394..395,
                     399,403,421,424..425,428..429,432)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340980"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            92..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AT66; propagated from
                     UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15403; propagated from
                     UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15403; propagated from
                     UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15403; propagated from
                     UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            358..378
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            423..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     Site            452..472
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TMR7.1)"
     CDS             1..522
                     /gene="Slc16a6"
                     /gene_synonym="MCT 6; MCT 7; Mct7B"
                     /coded_by="NM_198760.3:55..1623"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303772"
                     /db_xref="RGD:735117"
ORIGIN      
        1 mtqknsklcs ranvytqvpd ggwgwvvaas fffievftyg viksfgvffn dlmdsfdesn
       61 skiswiisic vfimtftapl stiltnrfgh rlvvmgggll isvgmiaasf sqrvyqmyis
      121 igivsglgyc fsflptvtil sqyfdkrrsm vtavastgec famfafapai talkehigwr
      181 ysllfvgllq lnvmvcgall rpiiikgpgs pkaipleprr evqymlenek trtsidsids
      241 gvelttspkn vpseakreqe vrveqqqtlv vgpkhsqkra plldfsilkd rsficytlfg
      301 lfatlgffap slyiiplgis lgihpdraaf llstmaiaev fgrigmglvl nrepirkiyi
      361 elicvilltv slfaftfate fwglmlcsvf fgsmvgtigg thipllaedd vvgiekmssa
      421 agvyvfiqsi sglagpplag llvdqskiys rafyscaagm alaavclalv rpckkglcqn
      481 phsgenqtdg hrgkalqdip edflemdlgk ceprahmkmd pv
//
LOCUS       NP_001385713             966 aa            linear   ROD 28-APR-2025
DEFINITION  neutral alpha-glucosidase AB isoform 1 [Rattus norvegicus].
ACCESSION   NP_001385713 XP_006231038
VERSION     NP_001385713.1
DBSOURCE    REFSEQ: accession NM_001398784.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Tian,W., Jiang,X., Sung,Y.K., Shuffle,E., Wu,T.H., Kao,P.N.,
            Tu,A.B., Dorfmuller,P., Cao,A., Wang,L., Peng,G., Kim,Y., Zhang,P.,
            Chappell,J., Pasupneti,S., Dahms,P., Maguire,P., Chaib,H.,
            Zamanian,R., Peters-Golden,M., Snyder,M.P., Voelkel,N.F.,
            Humbert,M., Rabinovitch,M. and Nicolls,M.R.
  TITLE     Phenotypically Silent Bone Morphogenetic Protein Receptor 2
            Mutations Predispose Rats to Inflammation-Induced Pulmonary
            Arterial Hypertension by Enhancing the Risk for Neointimal
            Transformation
  JOURNAL   Circulation 140 (17), 1409-1425 (2019)
   PUBMED   31462075
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Besse,W., Dong,K., Choi,J., Punia,S., Fedeles,S.V., Choi,M.,
            Gallagher,A.R., Huang,E.B., Gulati,A., Knight,J., Mane,S.,
            Tahvanainen,E., Tahvanainen,P., Sanna-Cherchi,S., Lifton,R.P.,
            Watnick,T., Pei,Y.P., Torres,V.E. and Somlo,S.
  TITLE     Isolated polycystic liver disease genes define effectors of
            polycystin-1 function
  JOURNAL   J Clin Invest 127 (5), 1772-1785 (2017)
   PUBMED   28375157
  REMARK    Erratum:[J Clin Invest. 2017 Sep 1;127(9):3558. doi:
            10.1172/JCI96729. PMID: 28862642]
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Caputo,A.T., Alonzi,D.S., Marti,L., Reca,I.B., Kiappes,J.L.,
            Struwe,W.B., Cross,A., Basu,S., Lowe,E.D., Darlot,B., Santino,A.,
            Roversi,P. and Zitzmann,N.
  TITLE     Structures of mammalian ER alpha-glucosidase II capture the binding
            modes of broad-spectrum iminosugar antivirals
  JOURNAL   Proc Natl Acad Sci U S A 113 (32), E4630-E4638 (2016)
   PUBMED   27462106
REFERENCE   4  (residues 1 to 966)
  AUTHORS   Porath,B., Gainullin,V.G., Cornec-Le Gall,E., Dillinger,E.K.,
            Heyer,C.M., Hopp,K., Edwards,M.E., Madsen,C.D., Mauritz,S.R.,
            Banks,C.J., Baheti,S., Reddy,B., Herrero,J.I., Banales,J.M.,
            Hogan,M.C., Tasic,V., Watnick,T.J., Chapman,A.B., Vigneau,C.,
            Lavainne,F., Audrezet,M.P., Ferec,C., Le Meur,Y., Torres,V.E. and
            Harris,P.C.
  CONSRTM   Genkyst Study Group, HALT Progression of Polycystic Kidney Disease
            Group; Consortium for Radiologic Imaging Studies of Polycystic
            Kidney Disease
  TITLE     Mutations in GANAB, Encoding the Glucosidase IIalpha Subunit, Cause
            Autosomal-Dominant Polycystic Kidney and Liver Disease
  JOURNAL   Am J Hum Genet 98 (6), 1193-1207 (2016)
   PUBMED   27259053
REFERENCE   5  (residues 1 to 966)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   6  (residues 1 to 966)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 966)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   8  (residues 1 to 966)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 966)
  AUTHORS   Pelletier,M.F., Marcil,A., Sevigny,G., Jakob,C.A., Tessier,D.C.,
            Chevet,E., Menard,R., Bergeron,J.J. and Thomas,D.Y.
  TITLE     The heterodimeric structure of glucosidase II is required for its
            activity, solubility, and localization in vivo
  JOURNAL   Glycobiology 10 (8), 815-827 (2000)
   PUBMED   10929008
REFERENCE   10 (residues 1 to 966)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 23, 2021 this sequence version replaced XP_006231038.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.5142.1,
                                           SRR26643429.4863.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..966
                     /product="neutral alpha-glucosidase AB isoform 1"
                     /EC_number="3.2.1.84"
                     /note="neutral alpha-glucosidase AB; alpha glucosidase 2
                     alpha neutral subunit; neutral AB; glucosidase, alpha;
                     neutral AB"
                     /calculated_mol_wt=109328
     Region          264..406
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            305
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          406..873
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(451,564,624,637,640,673,698)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     CDS             1..966
                     /gene="Ganab"
                     /gene_synonym="G2an"
                     /coded_by="NM_001398784.2:15..2915"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293721"
                     /db_xref="RGD:1309775"
ORIGIN      
        1 maaiaavaar rrrswlslvl aylgvclgit lavdrsnfkt ceessfckrq rsirpglspy
       61 ralldtlqlg pdaltvhlth evtkvllvle lqglqknmtr irideleprr pryrvpdvlv
      121 adpatarlsi sgrddnsvel tvaegpykii ltakpfrldl ledrslllsv narglmafeh
      181 qraprvpfsd kvsltlgsmw dkiknlfsrq epkdaaegng aepearpgdg dkpeetqeka
      241 ekdepgawee tfkthsdskp ygptsvgldf slpgmehvyg ipehadslrl kvteggepyr
      301 lynldvfqye lnnpmalygs vpvllahsfh rdlgifwlna aetwvdissn tagktlfgkm
      361 ldylqgsget pqtdirwmse sgivdvflml gpsvldvfrq hasltgtqal pplfslgyhq
      421 srwnyrdead vlevdqgfdd hnmpcdviwl diehadgkry ftwdptrfpq plnmlehlas
      481 krrklvaivd phikvdsgyr vheelrnhgl yvktrdgsdy egwcwpgsas ypdftnpqmr
      541 awwanmfnfh nyegsapnlf vwndmnepsv fngpevtmlk davhyggweh rdihniygly
      601 vhmatadgli qrsggierpf vlsraffsgs qrfgavwtgd ntaewdhlki sipmclslal
      661 vglsfcgadv ggffknpepe llvrwyqmga yqpffrahah ldtgrrepwl lasqyqdair
      721 dalfqrysll pfwytlfyqa hqegfpvmrp lwvqypedms tfsmedqfml gdallihpvs
      781 dagahgvqvy lpgeeevwyd iqsyqkhhgp qtlylpvtls sipvfqrggt ivprwmrvrr
      841 ssdcmkedpi tlfvalsaqg taqgelfldd ghtfnyqnrh efllrrfsfs gntlvsssad
      901 pkghletpvw iervvimgag kpaavvlqtk gspesrlsfq hdpetsvltl rkpgvnvasd
      961 wsihlr
//
LOCUS       NP_001423361             897 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423361 XP_008764216
VERSION     NP_001423361.1
DBSOURCE    REFSEQ: accession NM_001436432.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_008764216.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2969327.1,
                                           SRR26360194.2416796.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..897
                     /product="interleukin enhancer-binding factor 3 isoform 3"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=95728
     Region          52..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          88..342
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Site            100
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKR.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          363..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          371..389
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          398..470
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(403,406..407,410..411,413,427..428,430,432,449..451,
                     454)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          466..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          520..591
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(527,529..530,533,546,549..551,555,571..574)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     Region          609..897
                     /region_name="Interaction with PRMT1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          624..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Region          720..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     Site            818
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q12906; propagated from
                     UniProtKB/Swiss-Prot (Q9JIL3.2)"
     CDS             1..897
                     /gene="Ilf3"
                     /coded_by="NM_001436432.1:240..2933"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 mrpmrifvnd drhvmakhss vyptqeelea vqnmvshter alkavsdwid eqekgnsels
       61 eaenmdtppd deskegageq kaehmtrtlr gvmrvglvak glllkgdldl elvllckekp
      121 ttalldkvad nlaiqlttvt edkyeilqsv ddaaiviknt kepplsltih ltspvvreem
      181 ekvlagetls vndppdvldr qkclaalasl rhakwfqara nglkscvivi rvlrdlctrv
      241 ptwgplrgwp lellceksig tanrpmgage alrrvlecla sgivmpdgsg iydpcekeat
      301 daighldrqq reditqsaqh alrlaafgql hkvlgmdplp skmpkkpkne npvdytvqip
      361 psttyaitpm krpmeedgee kspskkkkki qkkeekaepp qamnalmrln qlkpglqykl
      421 isqtgpvhap iftmsvevdg stfeasgpsk ktaklhvavk vlqdmglptg aegrdsskge
      481 dsaeesdgkp avvapppvve avsnpssvfp sdatteqgpi ltkhgknpvm elnekrrglk
      541 yelisetggs hdkrfvmeve vdgqkfqgag snkkvakaya alaaleklfp daplaleank
      601 kkrapvpvrg gpkfaakphn pgfgmggpmh neappppnir grgrggnirg rgrgrgfggt
      661 nhgggymnag agygsygyss nsatagysqf ysngghsgna ggggsggggg sssyssyyqg
      721 dsynspvppk hagkkplhgg qqkpsyssgy qshqgqqqpy nqsqyssygt pqgkqkgygh
      781 gqgsyssysn synspggggg sdysydskfn ysgsggrsgg nsygssgssy ntgshggyga
      841 gsggsssyqg kqggyssqsn ysspgssqsy sgpassyqss qggysrnteh smnyqyr
//
LOCUS       NP_001417096            1149 aa            linear   ROD 28-APR-2025
DEFINITION  Fas binding factor 1 isoform 4 [Rattus norvegicus].
ACCESSION   NP_001417096 XP_063126254
VERSION     NP_001417096.1
DBSOURCE    REFSEQ: accession NM_001430167.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Ye,X., Zeng,H., Ning,G., Reiter,J.F. and Liu,A.
  TITLE     C2cd3 is critical for centriolar distal appendage assembly and
            ciliary vesicle docking in mammals
  JOURNAL   Proc Natl Acad Sci U S A 111 (6), 2164-2169 (2014)
   PUBMED   24469809
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Tanos,B.E., Yang,H.J., Soni,R., Wang,W.J., Macaluso,F.P.,
            Asara,J.M. and Tsou,M.F.
  TITLE     Centriole distal appendages promote membrane docking, leading to
            cilia initiation
  JOURNAL   Genes Dev 27 (2), 163-168 (2013)
   PUBMED   23348840
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Sugimoto,M., Inoko,A., Shiromizu,T., Nakayama,M., Zou,P.,
            Yonemura,S., Hayashi,Y., Izawa,I., Sasoh,M., Uji,Y., Kaibuchi,K.,
            Kiyono,T. and Inagaki,M.
  TITLE     The keratin-binding protein Albatross regulates polarization of
            epithelial cells
  JOURNAL   J Cell Biol 183 (1), 19-28 (2008)
   PUBMED   18838552
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 7, 2024 this sequence version replaced XP_063126254.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.67458.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..1149
                     /product="Fas binding factor 1 isoform 4"
                     /note="Fas (TNFRSF6) binding factor 1"
                     /calculated_mol_wt=127586
     Region          <103..553
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <580..>1065
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1149
                     /gene="Fbf1"
                     /coded_by="NM_001430167.1:119..3568"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:287836"
                     /db_xref="RGD:1310662"
ORIGIN      
        1 malkakkglk gsiddvlgdl lgddillekp vetashakdt ssspqwlssk akflpkdsag
       61 glaaadaevs sdsdadpqvf lqnmkdldsm dddlfgrmks hppsgkgtak asgkevpskp
      121 kpagtltade kgdaiptkkp ppassrfglq ykkfsfedfe dplagllsde eeetakkppa
      181 tesklapksp staagqgpsv pltpgdtpir kkeplfdegd dimttlgfed spkaerkkag
      241 dqegplpars kldellgrgt aakllprpgt gerrefkldk kyqkpedked swddeiltfg
      301 ayqptvasse grqsrrqsvr flgeggpdlk getlsfkqsp ppasspihpr kggadwlglk
      361 dddldllsps pvqkaqqeds amtpsllppt nqpsapephs vptglpsaak ppakgarpsv
      421 kasqvsspka seekeddwls hvisqkksqn lareertgps kdlnspgsrs qipasslpia
      481 stqvleqasa geasrpttqg iaavrpavtg apvswsqatt vvpvddpkrg tasasgdfss
      541 repavyiphs qeptglsvpi qtllpesmmq sllpgsgfqk qllaaqgqlq sstaqlqvel
      601 lqsqtklsel eaqvrklele rsqhrmlles lqqrhqadle liedahrshv kvletsyqqr
      661 eeqlrrekev lsaqhasycq eaerartelv aqhqrqmama eqekdqevar lrelqqasil
      721 emrkdhehql qrlkmlkdqe idavtsatsh trslngiieq mekfssslnt lssrveashv
      781 ttsqerelgi rqqdeqlral qerlgrqqrd meeersrlqe vigkmevrls eqsrlleqer
      841 wrvaaekska esaqrtleeq rkimvqqvam ereeleraks alleeqksvm nkcgeerrrl
      901 aaewaefftq qklskeraer eaeramhadt qrestiislt keqaeltvra celrakeekl
      961 iaerealere rqelrlekdr lhkaslrlqa raqevehmsk vaskkyeege qalqearqmq
     1021 teqqgrlqvv qrqqewlrqq eqrvhqehls laqqrlqldr vrqeapsslp glppraqgpa
     1081 assldavqap astapqrsqt aavqmpthll akllllkhta eedhdflene qffletlkka
     1141 pynmayhsa
//
LOCUS       NP_001417176             367 aa            linear   ROD 28-APR-2025
DEFINITION  T-cell immunoglobulin and mucin domain containing 4 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001417176 XP_038943083
VERSION     NP_001417176.1
DBSOURCE    REFSEQ: accession NM_001430247.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Kawano,M. and Nagata,S.
  TITLE     Lupus-like autoimmune disease caused by a lack of Xkr8, a
            caspase-dependent phospholipid scramblase
  JOURNAL   Proc Natl Acad Sci U S A 115 (9), 2132-2137 (2018)
   PUBMED   29440417
REFERENCE   2  (residues 1 to 367)
  AUTHORS   DICKIES,M.M.
  TITLE     A new viable yellow mutation in the house mouse
  JOURNAL   J Hered 53, 84-86 (1962)
   PUBMED   13886198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 8, 2024 this sequence version replaced XP_038943083.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.42207.1,
                                           SRR26643292.39990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..367
                     /product="T-cell immunoglobulin and mucin domain
                     containing 4 isoform 2 precursor"
                     /note="T-cell immunoglobulin and mucin domain-containing
                     protein 4"
                     /calculated_mol_wt=37663
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2702
     Region          29..129
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          51..55
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          95..99
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          124..127
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..367
                     /gene="Timd4"
                     /gene_synonym="AABR07072096.1; RGD1564516"
                     /coded_by="NM_001430247.1:14..1117"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:497891"
                     /db_xref="RGD:1564516"
ORIGIN      
        1 mskgllllwl vmelwllclt paasedtiig flgqsvtlpc qysswsqsrn smcwgrgscp
       61 gskcngellr tdgtrtisrk sgkytlwgsi rlgdvsltis ntnqddsgvy ccrievpgwf
      121 ndvkktvrle lrratttkrp ttttrlttrp ttqpttrptt tpyltttpep lpttvmttpd
      181 ptttaqpqtl attavgtavt mypstmpgsf sqkttsfstt eiftkgsait aesetlsafn
      241 nsqrsgmtis tdtalvrptg skawilssts qlmtqkttlt attrresskk tgelykiedr
      301 qtniliiacc vgfvlmvllf lafllrgkva eanclrrhrr pdntedsksv lndmsqgrdd
      361 edgiftl
//
LOCUS       NP_001385490             286 aa            linear   ROD 28-APR-2025
DEFINITION  protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform a
            [Rattus norvegicus].
ACCESSION   NP_001385490 NP_001385492
VERSION     NP_001385490.1
DBSOURCE    REFSEQ: accession NM_001398561.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Dung,T.T., Yi,Y.S., Heo,J., Yang,W.S., Kim,J.H., Kim,H.G.,
            Park,J.G., Yoo,B.C., Cho,J.Y. and Hong,S.
  TITLE     Critical role of protein L-isoaspartyl methyltransferase in basic
            fibroblast growth factor-mediated neuronal cell differentiation
  JOURNAL   BMB Rep 49 (8), 437-442 (2016)
   PUBMED   26973341
  REMARK    GeneRIF: PIMT was critical for bFGF-mediated neuronal
            differentiation of PC12 cells and regulated the MAPK and Akt
            signaling pathways.
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Kapadia,B., Viswakarma,N., Parsa,K.V., Kain,V., Behera,S.,
            Suraj,S.K., Babu,P.P., Kar,A., Panda,S., Zhu,Y.J., Jia,Y.,
            Thimmapaya,B., Reddy,J.K. and Misra,P.
  TITLE     ERK2-mediated phosphorylation of transcriptional coactivator
            binding protein PIMT/NCoA6IP at Ser298 augments hepatic
            gluconeogenesis
  JOURNAL   PLoS One 8 (12), e83787 (2013)
   PUBMED   24358311
  REMARK    GeneRIF: ERK2-mediated phosphorylation of transcriptional
            coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic
            gluconeogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Yan,G., Qin,Q., Yi,B., Chuprun,K., Sun,H., Huang,S. and Sun,J.
  TITLE     Protein-L-isoaspartate (D-aspartate) O-methyltransferase protects
            cardiomyocytes against hypoxia induced apoptosis through inhibiting
            proapoptotic kinase Mst1
  JOURNAL   Int J Cardiol 168 (4), 3291-3299 (2013)
   PUBMED   23647599
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Boivin,D., Bilodeau,D. and Beliveau,R.
  TITLE     Immunochemical characterization of L-isoaspartyl-protein carboxyl
            methyltransferase from mammalian tissues
  JOURNAL   Biochem J 309 (Pt 3) (Pt 3), 993-998 (1995)
   PUBMED   7639720
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Shirasawa,T., Endoh,R., Zeng,Y.X., Sakamoto,K. and Mori,H.
  TITLE     Protein L-isoaspartyl methyltransferase: developmentally regulated
            gene expression and protein localization in the central nervous
            system of aged rat
  JOURNAL   Neurosci Lett 188 (1), 37-40 (1995)
   PUBMED   7783974
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Mizobuchi,M., Murao,K., Takeda,R. and Kakimoto,Y.
  TITLE     Tissue-specific expression of isoaspartyl protein carboxyl
            methyltransferase gene in rat brain and testis
  JOURNAL   J Neurochem 62 (1), 322-328 (1994)
   PUBMED   8263531
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Cassidy,E.M., Wakim,B.T., Ferguson,A.G. and Samarel,A.M.
  TITLE     Asparaginyl deamidation-methylation of rat ventricular myosin light
            chains
  JOURNAL   J Mol Cell Cardiol 23 (5), 589-601 (1991)
   PUBMED   1886138
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Sato,M., Yoshida,T. and Tuboi,S.
  TITLE     Primary structure of rat brain protein carboxyl methyltransferase
            deduced from cDNA sequence
  JOURNAL   Biochem Biophys Res Commun 161 (1), 342-347 (1989)
   PUBMED   2730663
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 23, 2021 this sequence version replaced NP_001385492.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22399489.3078733.1,
                                           SRR23984936.507049.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..286
                     /product="protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase isoform a"
                     /EC_number="2.1.1.77"
                     /note="protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase; PIMT; protein-beta-aspartate
                     methyltransferase; L-isoaspartyl protein carboxyl
                     methyltransferase; protein L-isoaspartyl/D-aspartyl
                     methyltransferase"
                     /calculated_mol_wt=30291
     Region          66..274
                     /region_name="PCMT"
                     /note="Protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase (PCMT); pfam01135"
                     /db_xref="CDD:395902"
     CDS             1..286
                     /gene="Pcmt1"
                     /gene_synonym="PCM"
                     /coded_by="NM_001398561.1:294..1154"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:25604"
                     /db_xref="RGD:3268"
ORIGIN      
        1 mpgarsggsg sdgsnsgrss gdtsgavtvw evvsllgkll gtvaalkvvl yllrvcfama
       61 wksggashse lihnlrkngi iktdkvfevm latdrshyak snpymdspqs igfqatisap
      121 hmhayalell fdqlhegaka ldvgsgsgil tacfarmvgh sgkvigidhi kelvddsitn
      181 vkkddpmlls sgrvrlvvgd grmgfaeeap ydaihvgaaa pvvpqalidq lkpggrlilp
      241 vgpaggnqml eqydklqdgs vkmkplmgvi yvpltdkekq wsrdel
//
LOCUS       NP_001423359             910 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin enhancer-binding factor 3 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423359 XP_008764214
VERSION     NP_001423359.1
DBSOURCE    REFSEQ: accession NM_001436430.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Tan,X., Ye,P., Li,W.Y., Gao,Y., Leng,Y.Q., Duan,W., Wang,Y.K. and
            Wang,W.Z.
  TITLE     The interleukin-enhanced binding factor 3-mediated inhibition of
            nitric oxide production via phosphoinositide 3-kinase/protein
            kinase B pathway contributes to central cardiovascular regulation
            in the rostral ventrolateral medulla in hypertension
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 323 (6), R861-R874 (2022)
   PUBMED   36222883
  REMARK    GeneRIF: The interleukin-enhanced binding factor 3-mediated
            inhibition of nitric oxide production via phosphoinositide
            3-kinase/protein kinase B pathway contributes to central
            cardiovascular regulation in the rostral ventrolateral medulla in
            hypertension.
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Zhang,J.Y., Yang,Z., Fang,K., Shi,Z.L., Ren,D.H. and Sun,J.
  TITLE     Long noncoding RNA ILF3-AS1 regulates myocardial infarction via the
            miR-212-3p/SIRT1 axis and PI3K/Akt signaling pathway
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2647-2658 (2020)
   PUBMED   32196615
  REMARK    GeneRIF: Long noncoding RNA ILF3-AS1 regulates myocardial
            infarction via the miR-212-3p/SIRT1 axis and PI3K/Akt signaling
            pathway.
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Yang,R.H., Tan,X., Ge,L.J., Sun,J.C., Peng,X.D. and Wang,W.Z.
  TITLE     Interleukin enhancement binding factor 3 inhibits cardiac
            hypertrophy by targeting asymmetric dimethylarginine-nitric oxide
  JOURNAL   Nitric Oxide 93, 44-52 (2019)
   PUBMED   31536826
  REMARK    GeneRIF: ILF3 protein inhibits cardiac hypertrophy by targeting
            asymmetric dimethylarginine-nitric oxide.  Its expression is
            regulated by angiotensin II.
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Reichman,T.W., Muniz,L.C. and Mathews,M.B.
  TITLE     The RNA binding protein nuclear factor 90 functions as both a
            positive and negative regulator of gene expression in mammalian
            cells
  JOURNAL   Mol Cell Biol 22 (1), 343-356 (2002)
   PUBMED   11739746
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Satoh,M., Shaheen,V.M., Kao,P.N., Okano,T., Shaw,M., Yoshida,H.,
            Richards,H.B. and Reeves,W.H.
  TITLE     Autoantibodies define a family of proteins with conserved
            double-stranded RNA-binding domains as well as DNA binding activity
  JOURNAL   J Biol Chem 274 (49), 34598-34604 (1999)
   PUBMED   10574923
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Kao,P.N., Chen,L., Brock,G., Ng,J., Kenny,J., Smith,A.J. and
            Corthesy,B.
  TITLE     Cloning and expression of cyclosporin A- and FK506-sensitive
            nuclear factor of activated T-cells: NF45 and NF90
  JOURNAL   J Biol Chem 269 (32), 20691-20699 (1994)
   PUBMED   7519613
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 12, 2025 this sequence version replaced XP_008764214.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2162798.1,
                                           SRR26360176.1939260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..910
                     /product="interleukin enhancer-binding factor 3 isoform 1"
                     /note="M phase phosphoprotein 4"
                     /calculated_mol_wt=97473
     Region          101..355
                     /region_name="DZF"
                     /note="domain in DSRM or ZnF_C2H2 domain containing
                     proteins; smart00572"
                     /db_xref="CDD:128842"
     Region          411..483
                     /region_name="DSRM_ILF3_rpt1"
                     /note="first double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19910"
                     /db_xref="CDD:380739"
     Site            order(416,419..420,423..424,426,440..441,443,445,462..464,
                     467)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380739"
     Region          533..604
                     /region_name="DSRM_ILF3_rpt2"
                     /note="second double-stranded RNA binding motif of
                     interleukin enhancer-binding factor 3 (ILF3) and similar
                     proteins; cd19912"
                     /db_xref="CDD:380741"
     Site            order(540,542..543,546,559,562..564,568,584..587)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380741"
     CDS             1..910
                     /gene="Ilf3"
                     /coded_by="NM_001436430.1:240..2972"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:84472"
                     /db_xref="RGD:619734"
ORIGIN      
        1 malyhhhfit rrrrrpmrif vnddrhvmak hssvyptqee leavqnmvsh teralkavsd
       61 wideqekgns elseaenmdt ppddeskega geqkaehmtr tlrgvmrvgl vakglllkgd
      121 ldlelvllck ekpttalldk vadnlaiqlt tvtedkyeil qsvddaaivi kntkepplsl
      181 tihltspvvr eemekvlage tlsvndppdv ldrqkclaal aslrhakwfq aranglkscv
      241 ivirvlrdlc trvptwgplr gwplellcek sigtanrpmg agealrrvle clasgivmpd
      301 gsgiydpcek eatdaighld rqqreditqs aqhalrlaaf gqlhkvlgmd plpskmpkkp
      361 knenpvdytv qippsttyai tpmkrpmeed geekspskkk kkiqkkeeka eppqamnalm
      421 rlnqlkpglq yklisqtgpv hapiftmsve vdgstfeasg pskktaklhv avkvlqdmgl
      481 ptgaegrdss kgedsaeesd gkpavvappp vveavsnpss vfpsdatteq gpiltkhgkn
      541 pvmelnekrr glkyeliset ggshdkrfvm evevdgqkfq gagsnkkvak ayaalaalek
      601 lfpdaplale ankkkrapvp vrggpkfaak phnpgfgmgg pmhneapppp nirgrgrggn
      661 irgrgrgrgf ggtnhgggym nagagygsyg yssnsatagy sqfysngghs gnaggggsgg
      721 gggsssyssy yqgdsynspv ppkhagkkpl hggqqkpsys sgyqshqgqq qpynqsqyss
      781 ygtpqgkqkg yghgqgsyss ysnsynspgg gggsdysyds kfnysgsggr sggnsygssg
      841 ssyntgshgg ygagsggsss yqgkqggyss qsnysspgss qsysgpassy qssqggysrn
      901 tehsmnyqyr
//
LOCUS       NP_001102202             103 aa            linear   ROD 28-APR-2025
DEFINITION  U6 snRNA-associated Sm-like protein LSm7 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001102202 XP_001076086 XP_343158
VERSION     NP_001102202.1
DBSOURCE    REFSEQ: accession NM_001108732.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Agafonov,D.E., Kastner,B., Dybkov,O., Hofele,R.V., Liu,W.T.,
            Urlaub,H., Luhrmann,R. and Stark,H.
  TITLE     Molecular architecture of the human U4/U6.U5 tri-snRNP
  JOURNAL   Science 351 (6280), 1416-1420 (2016)
   PUBMED   26912367
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Wahl,M.C., Will,C.L. and Luhrmann,R.
  TITLE     The spliceosome: design principles of a dynamic RNP machine
  JOURNAL   Cell 136 (4), 701-718 (2009)
   PUBMED   19239890
  REMARK    Review article
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Achsel,T., Brahms,H., Kastner,B., Bachi,A., Wilm,M. and Luhrmann,R.
  TITLE     A doughnut-shaped heteromer of human Sm-like proteins binds to the
            3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in
            vitro
  JOURNAL   EMBO J 18 (20), 5789-5802 (1999)
   PUBMED   10523320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_343158.1, XP_001076086.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM058686.1, SRR26360181.3007895.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..103
                     /product="U6 snRNA-associated Sm-like protein LSm7 isoform
                     1"
                     /note="U6 snRNA-associated Sm-like protein LSm7; LSM7
                     homolog, U6 small nuclear RNA associated; LSM7 U6 small
                     nuclear RNA and mRNA degradation associated"
                     /calculated_mol_wt=11487
     Region          9..97
                     /region_name="LSm7"
                     /note="Like-Sm protein 7; cd01729"
                     /db_xref="CDD:212476"
     Site            order(13,15,18..19,24,26..28,31,33,38..45,47,69,71,73..86)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:212476"
     Site            order(23..29,31..43,45..49)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212476"
     Site            order(41,43,77)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212476"
     Site            73..84
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212476"
     CDS             1..103
                     /gene="Lsm7"
                     /coded_by="NM_001108732.2:24..335"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362829"
                     /db_xref="RGD:1305354"
ORIGIN      
        1 madkekkkke sildlskyid ktirvkfqgg reasgilkgf dpllnlvldg tieymrdpdd
       61 qykltedtrq lglvvcrgts vvlicpqdgm eaipnpfvqq qdt
//
LOCUS       NP_001396206             806 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 431-like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001396206 XP_038940828
VERSION     NP_001396206.1
DBSOURCE    REFSEQ: accession NM_001409277.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jul 12, 2022 this sequence version replaced XP_038940828.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1512334.1,
                                           SRR26360186.2936159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..806
                     /product="zinc finger protein 431-like isoform 2"
                     /calculated_mol_wt=92608
     Region          11..51
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          71..485
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          85..104
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          112..132
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          140..160
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          169..188
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          196..216
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(201,203,205,207..208,211..212,215,229,231,235..236,
                     239..240,243,257,259,261,263..264,267..268,271)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          224..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          304..718
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(313,315,317,319..320,323..324,327,341,343,347..348,
                     351..352,355,369,371,373,375..376,379..380,383)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          560..580
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(565,567,569,571..572,575..576,579,593,595,599..600,
                     603..604,607,621,623,625,627..628,631..632,635)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          588..608
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          616..636
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          644..664
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          672..692
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          700..720
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          712..737
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          728..748
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(733,735,737,739..740,743..744,747,761,763,767..768,
                     771..772,775,789,791,793,795..796,799..800,803)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          752..>806
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          756..776
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          768..793
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          784..804
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..806
                     /gene="LOC120094815"
                     /coded_by="NM_001409277.1:144..2564"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:120094815"
                     /db_xref="RGD:41247165"
ORIGIN      
        1 mrmefnakda ltyddvhvnf treewalldp sqkslykdvm letyrnltai gynwedhtid
       61 ehcqsfrrhg rherchpgek psentqcgka faqqshlqrh ksthtgekly eckphdkaft
      121 ydsqlqtler ihtgekpykc nqcgkaferr cnlgrhklih tgrksykynq cgkdfaglsh
      181 lkthgithtg gkpykcdqcg kafayhsslq vhkrihtgek pyvcdqcgka faqlghlqvh
      241 githtgekpy kcdqcgkafa hhsylqvhkr ihtgeklcec dqcgkaflsh sylqvhkrih
      301 tgenlyecdq cgkaftshsy lqvhkrihtg eklyecdqcg kaftshsylq vhkrihtgek
      361 pyvcdqcgka farlsylkth githtgekpy kcdqcgkafe hrcnlgshkl ihtgekpykc
      421 dqcgkafssh sylqvhkrih tgeklcecdq cgkafsshsy lqvhkrihtg qnlyecdqcg
      481 kafashsylq vhkrihtgek lcecdqcgka fsshsylqvh krihtgekly ecdqcgkafa
      541 shsylqvhkr ihtgenlyec dqcskafash sylqvhkrih tgekpyvcdw cnkafayhsy
      601 lqvhkrihtg ekpyvcdqcg kdfvvpselk rhkrihtgek pykcnecgka fvgqndlkkh
      661 rrthtgekpy kcnecgkafv fnfnlrahkv ihtgekpykc secgkafacn tslrthkaih
      721 tgvkpfeckq cgkafacnts lqthraihtg vkpfeckqcg kafvgqndlk rherihtgek
      781 pyecnecgka fsqssqlqlh krthty
//
LOCUS       NP_001102537             452 aa            linear   ROD 28-APR-2025
DEFINITION  protein FAM222A [Rattus norvegicus].
ACCESSION   NP_001102537 XP_001080384 XP_573412
VERSION     NP_001102537.1
DBSOURCE    REFSEQ: accession NM_001109067.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473973.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_573412.2, XP_001080384.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM031426.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..452
                     /product="protein FAM222A"
                     /calculated_mol_wt=47108
     Region          35..452
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..452
                     /gene="Fam222a"
                     /gene_synonym="RGD1565883"
                     /coded_by="NM_001109067.1:449..1807"
                     /db_xref="GeneID:498193"
                     /db_xref="RGD:1565883"
ORIGIN      
        1 mlaclqrtqn ppgqhltcps kslelrkces vassmpssry pspaeldaya ekvansplsi
       61 kifptnirvp qhkhlsrtvn gydtsgqryn pypqhttgyq gllaivkaav sstaatpagh
      121 tksvlksveg krtklspatv qvgiapypvp stlgplaypk ppeapapppn lpaaatatsv
      181 iplpgrglpl ppsnlpsihs ilyqlnqqcq apgvapsacq gvavphpspa khgpvpsfpr
      241 vaysataglp dcrkgtelsq gatpaltlag atkpagyseg gldyllwpqk ppppppqplr
      301 aygssstvas kspetcsgra ferangsphn cgmglpggft vgqyfaapwn svlvtptsdc
      361 ynaaaaavvt elgpgaarel agppvdtlsg ltsksvcnta vlssslqsle ylindirppc
      421 ikeqmlgkgy etvavprlld hqhahirlpv yr
//
LOCUS       NP_001425359             460 aa            linear   ROD 28-APR-2025
DEFINITION  activating transcription factor 7-interacting protein 2 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001425359 XP_006245790
VERSION     NP_001425359.1
DBSOURCE    REFSEQ: accession NM_001438430.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006245790.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2025093.1,
                                           SRR26643293.61369.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..460
                     /product="activating transcription factor 7-interacting
                     protein 2 isoform 1"
                     /calculated_mol_wt=51418
     Region          70..278
                     /region_name="ATF7IP_BD"
                     /note="ATF-interacting protein binding domain; pfam16788"
                     /db_xref="CDD:465271"
     Region          353..450
                     /region_name="fn3_4"
                     /note="Fibronectin-III type domain; pfam16794"
                     /db_xref="CDD:465273"
     CDS             1..460
                     /gene="Atf7ip2"
                     /coded_by="NM_001438430.1:78..1460"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:497859"
                     /db_xref="RGD:1583744"
ORIGIN      
        1 mespdrkrrk vlkakktmpt scrkqmeiln qsknveapkt tvvtnipngn qslgtgfias
       61 hnqkmfsenk envkvmktse qinenaceal erhtalleqv khwirqeict incnlfdkkl
      121 nelnerigkt qcrskheaia gelfikirrl qkriktvlss qgnclepntl psntvckvtd
      181 svnlsvtqrs vksqskrmss vnhtpfnsse kasrkinlps acvefvsesn ddvmlisven
      241 pnlttpiasd pteirkntsr nvssspnars evvpvekkfd fvidltregl ssysiespsf
      301 tlkstskavl rskeiipvae ngnegfgsfe hlpplpeppa plpemadkiq dtlppqkpel
      361 kvkqvlrpss ialtwnipkv npkcapvesy hlflyyegsn hltwkkvaei kalplpmact
      421 lsqmlastky yfavqskdif grygpfcnik cipgfsenlt
//
LOCUS       NP_001258065            1354 aa            linear   ROD 28-APR-2025
DEFINITION  misshapen-like kinase 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001258065 XP_001079459
VERSION     NP_001258065.1
DBSOURCE    REFSEQ: accession NM_001271136.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1354)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   2  (residues 1 to 1354)
  AUTHORS   Kaneko,S., Chen,X., Lu,P., Yao,X., Wright,T.G., Rajurkar,M.,
            Kariya,K., Mao,J., Ip,Y.T. and Xu,L.
  TITLE     Smad inhibition by the Ste20 kinase Misshapen
  JOURNAL   Proc Natl Acad Sci U S A 108 (27), 11127-11132 (2011)
   PUBMED   21690388
REFERENCE   3  (residues 1 to 1354)
  AUTHORS   Hussain,N.K., Hsin,H., Huganir,R.L. and Sheng,M.
  TITLE     MINK and TNIK differentially act on Rap2-mediated signal
            transduction to regulate neuronal structure and AMPA receptor
            function
  JOURNAL   J Neurosci 30 (44), 14786-14794 (2010)
   PUBMED   21048137
REFERENCE   4  (residues 1 to 1354)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 1354)
  AUTHORS   Nonaka,H., Takei,K., Umikawa,M., Oshiro,M., Kuninaka,K.,
            Bayarjargal,M., Asato,T., Yamashiro,Y., Uechi,Y., Endo,S.,
            Suzuki,T. and Kariya,K.I.
  TITLE     MINK is a Rap2 effector for phosphorylation of the postsynaptic
            scaffold protein TANC1
  JOURNAL   Biochem Biophys Res Commun 377 (2), 573-578 (2008)
   PUBMED   18930710
REFERENCE   6  (residues 1 to 1354)
  AUTHORS   McCarty,N., Paust,S., Ikizawa,K., Dan,I., Li,X. and Cantor,H.
  TITLE     Signaling by the kinase MINK is essential in the negative selection
            of autoreactive thymocytes
  JOURNAL   Nat Immunol 6 (1), 65-72 (2005)
   PUBMED   15608642
  REMARK    Erratum:[Nat Immunol. 2005 Feb;6(2):219]
REFERENCE   7  (residues 1 to 1354)
  AUTHORS   Hu,Y., Leo,C., Yu,S., Huang,B.C., Wang,H., Shen,M., Luo,Y.,
            Daniel-Issakani,S., Payan,D.G. and Xu,X.
  TITLE     Identification and functional characterization of a novel human
            misshapen/Nck interacting kinase-related kinase, hMINK beta
  JOURNAL   J Biol Chem 279 (52), 54387-54397 (2004)
   PUBMED   15469942
  REMARK    Erratum:[J Biol Chem. 2005 Feb 11;280(6):5128]
REFERENCE   8  (residues 1 to 1354)
  AUTHORS   Dan,I., Watanabe,N.M., Kobayashi,T., Yamashita-Suzuki,K.,
            Fukagaya,Y., Kajikawa,E., Kimura,W.K., Nakashima,T.M.,
            Matsumoto,K., Ninomiya-Tsuji,J. and Kusumi,A.
  TITLE     Molecular cloning of MINK, a novel member of mammalian GCK family
            kinases, which is up-regulated during postnatal mouse cerebral
            development
  JOURNAL   FEBS Lett 469 (1), 19-23 (2000)
   PUBMED   10708748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Sep 2, 2012 this sequence version replaced XP_001079459.3.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1354
                     /product="misshapen-like kinase 1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="MEK kinase kinase 6; GCK family kinase MiNK;
                     misshapen/NIK-related kinase; MAPK/ERK kinase kinase
                     kinase 6; mitogen-activated protein kinase kinase kinase
                     kinase 6"
                     /calculated_mol_wt=152372
     Region          8..289
                     /region_name="STKc_MAP4K4_6_N"
                     /note="N-terminal Catalytic domain of the Serine/Threonine
                     Kinases, Mitogen-Activated Protein Kinase Kinase Kinase
                     Kinase 4 and 6; cd06636"
                     /db_xref="CDD:270806"
     Site            order(31..35,39,52,54,83,105..108,111..112,115,153,
                     155..158,160,170..171,174,188..191,193,225,234)
                     /site_type="active"
                     /db_xref="CDD:270806"
     Site            order(31..35,39,52,54,83,105..108,111..112,115,157..158,
                     160,171)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270806"
     Site            order(34..35,153,155..157,174,188..191,193,225,234)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270806"
     Site            170..193
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270806"
     Region          299..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM52; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM52; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Region          363..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            513
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM52; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Region          520..>816
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            521
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4C8; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            654
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4C8; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4C8; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8N4C8; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Region          888..1354
                     /region_name="Mediates interaction with RAP2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LP90.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JM52; propagated from
                     UniProtKB/Swiss-Prot (F1LP90.2)"
     Region          927..964
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LP90.2)"
     Region          1036..1334
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..1354
                     /gene="Mink1"
                     /gene_synonym="MEKKK 6"
                     /coded_by="NM_001271136.2:203..4267"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:303259"
                     /db_xref="RGD:1359135"
ORIGIN      
        1 mgdpaparsl ddidlsalrd pagifelvev vgngtygqvy kgrhvktgql aaikvmdvte
       61 deeeeikqei nmlkkyshhr niatyygafi kksppgnddq lwlvmefcga gsvtdlvknt
      121 kgnalkedci ayicreilrg lahlhahkvi hrdikgqnvl ltenaevklv dfgvsaqldr
      181 tvgrrntfig tpywmapevi acdenpdaty dyrsdiwslg itaiemaega pplcdmhpmr
      241 alfliprnpp prlkskkwsk kftdfidtcl iktylsrppt eqllkfpfir dqpterqvri
      301 qlkdhidrsr kkrgekeete yeysgseeed dshgeegeps simnvpgest lrreflrlqq
      361 enksnsealk qqqqlqqqqq rdpeahikhl lhqrqrriee qkeerrrvee qqrrereqrk
      421 lqekeqqrrl edmqalrree errqaereqe ykrkqleeqr qserlqrqlq qehaylkslq
      481 qqqqqqqqlq kqqqqqqqqq qqqqqqqilp gdrkplyhyg rginpadkpa wareveerar
      541 mnkqqnspla ktkpssagpe ppipqaspsp pgplsqtppm qrpvepqegp hkslvahrvp
      601 lkpyaapvpr sqslqdqptr nlaafpashd pdpaavptpt atpsargavi rqnsdptseg
      661 pgpspnppsw vrpdneappk vpqrtssiat alntsgaggs rpaqavrarp rsnsawqiyl
      721 qrraergtpk ppgppaqppg ppntssnpdl rrsdpgwers dsvlpashgh lpqagslern
      781 rnrvgastkl dsspvlspgn kakpedhrsr pgrpasykra igedfvllke rtldeapkpp
      841 kkamdyssss eevessedee eegdgepseg srdtpggrdg dtdsvstmvv hdveevsgtq
      901 psygggtmvv qrtpeeersl lladsngytn lpdvvqpshs ptensqgqsp ptkdgggdyq
      961 srglvkapgk ssftmfvdlg iyqpggsgdt ipitalvgge ggrldqlqfd vrkgsvvnvn
     1021 ptntrahset peirkykkrf nseilcaalw gvnllvgten glmlldrsgq gkvygligrr
     1081 rfqqmdvleg lnllitisgk rnklrvyyls wlrnkilhnd pevekkqgwt tvgdmegcgh
     1141 yrvvkyerik flvialknsv evyawapkpy hkfmafksfa dlphrpllvd ltveegqrlk
     1201 viygssagfh avdvdsgnsy diyipvhiqs qitphaivfl pntdgmemll cyedegvyvn
     1261 tygriikdvv lqwgemptsv ayicsnqimg wgekaieirs vetghldgvf mhkraqrlkf
     1321 lcerndkvff asvrsggssq vyfmtlnrnc imnw
//
LOCUS       NP_001416686             574 aa            linear   ROD 28-APR-2025
DEFINITION  [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1,
            mitochondrial isoform 3 [Rattus norvegicus].
ACCESSION   NP_001416686 XP_006237969
VERSION     NP_001416686.1
DBSOURCE    REFSEQ: accession NM_001429757.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Feng,X., Lu,J., Wu,Y. and Xu,H.
  TITLE     MiR-18a-3p improves cartilage matrix remodeling and inhibits
            inflammation in osteoarthritis by suppressing PDP1
  JOURNAL   J Physiol Sci 72 (1), 3 (2022)
   PUBMED   35148687
  REMARK    GeneRIF: MiR-18a-3p improves cartilage matrix remodeling and
            inhibits inflammation in osteoarthritis by suppressing PDP1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Xing,G., Ren,M., O'Neill,J.T., Sharma,P., Verma,A. and Watson,W.D.
  TITLE     Pyruvate dehydrogenase phosphatase1 mRNA expression is divergently
            and dynamically regulated between rat cerebral cortex, hippocampus
            and thalamus after traumatic brain injury: a potential biomarker of
            TBI-induced hyper- and hypo-glycaemia and neuronal vulnerability
  JOURNAL   Neurosci Lett 525 (2), 140-145 (2012)
   PUBMED   22884618
  REMARK    GeneRIF: divergent alterations of PDP1 mRNA expression were found
            in different brain regions following traumatic brain injury.
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Voss,M., Paterson,J., Kelsall,I.R., Martin-Granados,C.,
            Hastie,C.J., Peggie,M.W. and Cohen,P.T.
  TITLE     Ppm1E is an in cellulo AMP-activated protein kinase phosphatase
  JOURNAL   Cell Signal 23 (1), 114-124 (2011)
   PUBMED   20801214
  REMARK    Erratum:[Cell Signal. 2011 May;23(5):947]
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Leblanc,P.J., Mulligan,M., Antolic,A., Macpherson,L., Inglis,J.G.,
            Martin,D., Roy,B.D. and Peters,S.J.
  TITLE     Skeletal muscle type comparison of pyruvate dehydrogenase
            phosphatase activity and isoform expression: effects of obesity and
            endurance training
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 295 (4), R1224-R1230 (2008)
   PUBMED   18716035
  REMARK    GeneRIF: Results suggest that decreased PDP activity in oxidative
            skeletal muscles may play a role in the impairment of carbohydrate
            metabolism in obese rats, which is reversible with endurance
            training.
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Vassylyev,D.G. and Symersky,J.
  TITLE     Crystal structure of pyruvate dehydrogenase phosphatase 1 and its
            functional implications
  JOURNAL   J Mol Biol 370 (3), 417-426 (2007)
   PUBMED   17532339
  REMARK    GeneRIF: Results report the crystal structure of the rat pyruvate
            dehydrogenase phosphatase 1 catalytic subunit at 1.8 A resolution.
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Piccinini,M., Mostert,M., Alberto,G., Ramondetti,C., Novi,R.F.,
            Dalmasso,P. and Rinaudo,M.T.
  TITLE     Down-regulation of pyruvate dehydrogenase phosphatase in obese
            subjects is a defect that signals insulin resistance
  JOURNAL   Obes Res 13 (4), 678-686 (2005)
   PUBMED   15897476
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Wang,M.Y. and Unger,R.H.
  TITLE     Role of PP2C in cardiac lipid accumulation in obese rodents and its
            prevention by troglitazone
  JOURNAL   Am J Physiol Endocrinol Metab 288 (1), E216-E221 (2005)
   PUBMED   15367397
  REMARK    GeneRIF: role of PP2C and AMPK in the derangements of cardiac lipid
            metabolism in obesity
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Karpova,T., Danchuk,S., Huang,B. and Popov,K.M.
  TITLE     Probing a putative active site of the catalytic subunit of pyruvate
            dehydrogenase phosphatase 1 (PDP1c) by site-directed mutagenesis
  JOURNAL   Biochim Biophys Acta 1700 (1), 43-51 (2004)
   PUBMED   15210124
  REMARK    GeneRIF: Asp445 might be involved in the control of interactions
            between PDP1c and the protein substrate pyruvate dehydrogenase
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Huang,B., Wu,P., Popov,K.M. and Harris,R.A.
  TITLE     Starvation and diabetes reduce the amount of pyruvate dehydrogenase
            phosphatase in rat heart and kidney
  JOURNAL   Diabetes 52 (6), 1371-1376 (2003)
   PUBMED   12765946
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Huang,B., Gudi,R., Wu,P., Harris,R.A., Hamilton,J. and Popov,K.M.
  TITLE     Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino
            acid sequences, expression, and regulation
  JOURNAL   J Biol Chem 273 (28), 17680-17688 (1998)
   PUBMED   9651365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 26, 2024 this sequence version replaced XP_006237969.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129095.1, SRR26643296.14716.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107, SAMN12840129
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG   :: upstream AUG and CDS
                                                  extension is not conserved
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..574
                     /product="[Pyruvate dehydrogenase
                     [acetyl-transferring]]-phosphatase 1, mitochondrial
                     isoform 3"
                     /EC_number="3.1.3.43"
                     /note="[Pyruvate dehydrogenase
                     [acetyl-transferring]]-phosphatase 1, mitochondrial;
                     pyruvate dehydrogenase phosphatase isoenzyme 1; protein
                     phosphatase 2C, magnesium dependent, catalytic subunit;
                     pyruvate dehyrogenase phosphatase catalytic subunit 1"
                     /calculated_mol_wt=64953
     Region          145..561
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(156,160..161,180..182,454,552)
                     /site_type="active"
                     /db_xref="CDD:238083"
     CDS             1..574
                     /gene="Pdp1"
                     /gene_synonym="PDPC 1; Ppm2c"
                     /coded_by="NM_001429757.1:47..1771"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:54705"
                     /db_xref="RGD:620393"
ORIGIN      
        1 mlsapccddr rmcvcpgprr igipvrtssl plfsdampap tqlffplvrn celsriygta
       61 cychhkhlcc sppyipqnrl rytphpayat fcrprenwwq ytqgrryast pqkfyltppq
      121 vnsilkaney sfkvpefdgk nvssilgfds nqlpanapie drrsaatclq trgmllgvfd
      181 ghagcacsqa vserlfyyia vsllphetll eienavesgr allpilqwhk hpndyfskea
      241 sklyfnslrt ywqelidlnt gesadidvke alinafkrld ndisleaqvg dpnsflnylv
      301 lrvafsgata cvahvdgvdl hvantgdsra mlgvqeedgs wsavtlsndh naqnereler
      361 lklehpknea ksvvkqdrll gllmpfrafg dvkfkwsidl qkrviesgpd qlndneytkf
      421 ippnyhtppy ltaepevtyh rlrpqdkflv latdglwetm hrqdvvrivg eyltgmhhqq
      481 piavggykvt lgqmhgllte rrakmssvfe dqnaathlir havgnnefga vdherlskml
      541 slpeelarmy rdditiivvq fnshvvgayq nqeq
//
LOCUS       NP_001077055             526 aa            linear   ROD 28-APR-2025
DEFINITION  CUGBP Elav-like family member 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001077055
VERSION     NP_001077055.2
DBSOURCE    REFSEQ: accession NM_001083586.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Liu,Y., Wang,H., Wang,J., Wei,B., Zhang,X., Zhang,M., Cao,D.,
            Dai,J., Wang,Z., Nyirimigabo,E. and Ji,G.
  TITLE     A positive feedback regulation of Heme oxygenase 1 by CELF1 in
            cardiac myoblast cells
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1862 (2), 209-218 (2019)
   PUBMED   30508596
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Bai,Z., Chai,X.R., Yoon,M.J., Kim,H.J., Lo,K.A., Zhang,Z.C., Xu,D.,
            Siang,D.T.C., Walet,A.C.E., Xu,S.H., Chia,S.Y., Chen,P., Yang,H.,
            Ghosh,S. and Sun,L.
  TITLE     Dynamic transcriptome changes during adipose tissue energy
            expenditure reveal critical roles for long noncoding RNA regulators
  JOURNAL   PLoS Biol 15 (8), e2002176 (2017)
   PUBMED   28763438
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Del Pino Sans,J., Krishnan,S., Aggison,L.K., Adams,H.L.,
            Shrikant,M.M., Lopez-Giraldez,F. and Petersen,S.L.
  TITLE     Microarray analysis of neonatal rat anteroventral periventricular
            transcriptomes identifies the proapoptotic Cugbp2 gene as
            sex-specific and regulated by estradiol
  JOURNAL   Neuroscience 303, 312-322 (2015)
   PUBMED   26166732
  REMARK    GeneRIF: This study demonstrated that Cugbp2 regulates splicing and
            translation of mRNAs linked to sexual differentiation in rats.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Moraes,K.C., Monteiro,C.J. and Pacheco-Soares,C.
  TITLE     A novel function for CUGBP2 in controlling the pro-inflammatory
            stimulus in H9c2 cells: subcellular trafficking of messenger
            molecules
  JOURNAL   Cell Biol Int 37 (10), 1129-1138 (2013)
   PUBMED   23661609
  REMARK    GeneRIF: a regulatory connection between COX-2 and CUGBP2 in the
            cardiac cells, was demonstrated.
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Mukhopadhyay,D., Houchen,C.W., Kennedy,S., Dieckgraefe,B.K. and
            Anant,S.
  TITLE     Coupled mRNA stabilization and translational silencing of
            cyclooxygenase-2 by a novel RNA binding protein, CUGBP2
  JOURNAL   Mol Cell 11 (1), 113-126 (2003)
   PUBMED   12535526
  REMARK    GeneRIF: These findings identify a novel paradigm for RNA binding
            proteins such as CUGBP2 in facilitating opposing functions of mRNA
            stability and translation inhibition and reveal a mechanism for
            inhibiting cyclooxygenase-2 expression in cancer cells.
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Zhang,W., Liu,H., Han,K. and Grabowski,P.J.
  TITLE     Region-specific alternative splicing in the nervous system:
            implications for regulation by the RNA-binding protein NAPOR
  JOURNAL   RNA 8 (5), 671-685 (2002)
   PUBMED   12022233
  REMARK    GeneRIF: tissue-specific distribution of NAPOR, CUG-BP, and other
            highly related proteins within the nervous system
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Levers,T.E., Tait,S., Birling,M.C., Brophy,P.J. and Price,D.J.
  TITLE     Etr-r3/mNapor, encoding an ELAV-type RNA binding protein, is
            expressed in differentiating cells in the developing rodent
            forebrain
  JOURNAL   Mech Dev 112 (1-2), 191-193 (2002)
   PUBMED   11850193
  REMARK    GeneRIF: Etr-r3/mNapor, encoding an ELAV-type RNA binding protein,
            is expressed in differentiating cells in the developing rodent
            forebrain
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Ladd,A.N., Charlet,N. and Cooper,T.A.
  TITLE     The CELF family of RNA binding proteins is implicated in
            cell-specific and developmentally regulated alternative splicing
  JOURNAL   Mol Cell Biol 21 (4), 1285-1296 (2001)
   PUBMED   11158314
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Choi,D.K., Ito,T., Tsukahara,F., Hirai,M. and Sakaki,Y.
  TITLE     Developmentally-regulated expression of mNapor encoding an
            apoptosis-induced ELAV-type RNA binding protein
  JOURNAL   Gene 237 (1), 135-142 (1999)
   PUBMED   10524244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Feb 2, 2010 this sequence version replaced NP_001077055.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF090695.1, SRR26360194.445132.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..526
                     /product="CUGBP Elav-like family member 2 isoform 2"
                     /note="RNA-binding protein Brunol3; Cugbp- and Etr3-like
                     factor 2; CUG-BP- and ETR-3-like factor 2; bruno-like
                     protein 3; neuroblastoma apoptosis-related RNA-binding
                     protein; RNA-binding protein BRUNOL-3; elav-type
                     RNA-binding protein 3; CUG triplet repeat, RNA binding
                     protein 2"
                     /calculated_mol_wt=56197
     Region          57..140
                     /region_name="RRM1_CELF1_2_Bruno"
                     /note="RNA recognition motif 1 (RRM1) found in CUGBP
                     Elav-like family member CELF-1, CELF-2, Drosophila
                     melanogaster Bruno protein and similar proteins; cd12631"
                     /db_xref="CDD:410040"
     Site            order(61,63..64,67,88..91,93..94,101..103,105,135,137,
                     139..140)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410040"
     Region          149..229
                     /region_name="RRM2_CELF1_2"
                     /note="RNA recognition motif 2 (RRM2) found in CUGBP
                     Elav-like family member CELF-1, CELF-2 and similar
                     proteins; cd12634"
                     /db_xref="CDD:410042"
     Site            order(151,153,155..156,159,178,180,182,190..192,194,
                     220..221,224,226,228..229)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410042"
     Region          434..525
                     /region_name="RRM3_CELF1_2"
                     /note="RNA recognition motif 3 (RRM3) found in CUGBP
                     Elav-like family member CELF-1, CELF-2 and similar
                     proteins; cd12638"
                     /db_xref="CDD:241082"
     CDS             1..526
                     /gene="Celf2"
                     /gene_synonym="Brunol3; Cugbp2; Etr3; Napor"
                     /coded_by="NM_001083586.3:180..1760"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29428"
                     /db_xref="RGD:68347"
ORIGIN      
        1 mfertselaf vetisvesmr cpksavtmrn eelllsngta nkmngaldhs dqpdpdaikm
       61 fvgqiprsws ekelkelfep ygavyqinvl rdrsqnppqs kgccfvtfyt rkaaleaqna
      121 lhniktlpgm hhpiqmkpad seksnavedr klfigmvskk cnendirvmf spfgqieecr
      181 ilrgpdglsr gcafvtfstr amaqnaikam hqsqtmegcs spivvkfadt qkdkeqrrlq
      241 qqlaqqmqql ntatwgnltg lggltpqyla llqqatsssn lgafsgiqqm agmnalqlqn
      301 latlaaaaaa aqtsatstna nplsstssal galtspvaas tpnstagaam nsltslgtlq
      361 glagatvgln ninalagmaa lngglgatgl tngtagtmda ltqaysgiqq yaaaalptly
      421 sqsllqqqsa agsqkegpeg anlfiyhlpq efgdqdilqm fmpfgnvisa kvfidkqtnl
      481 skcfgfvsyd npvsaqaaiq amngfqigmk rlkvqlkrsk ndskpy
//
LOCUS       NP_001389320             252 aa            linear   ROD 28-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 45 [Rattus norvegicus].
ACCESSION   NP_001389320
VERSION     NP_001389320.1
DBSOURCE    REFSEQ: accession NM_001402391.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000013.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.52590.1,
                                           SRR26360181.1380629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..252
                     /product="ankyrin repeat domain-containing protein 45"
                     /calculated_mol_wt=28135
     Region          <62..207
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          76..106
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(77,81..82,85..87,89..90,94,97,106,108,110,114..115,
                     118..120,122..123,127,130,139,141,143,147..148,151..153,
                     155..156,160,163)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          108..139
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          141..166
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <185..239
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     CDS             1..252
                     /gene="Ankrd45"
                     /gene_synonym="RGD1311153"
                     /coded_by="NM_001402391.1:44..802"
                     /db_xref="GeneID:289152"
                     /db_xref="RGD:1311153"
ORIGIN      
        1 mepeealese ssekslfssr hdyeesqead etgtenpllq ptltgdvegl qkifedpenp
       61 hhenavqlll eedivgrnll yaacmagksd viralakygv nlnektargy tllhcaaawg
      121 rletlkalve ldvdiealnf rgekardvaa rysqaecvhf ldradarlil kkfitkssli
      181 itdpektpgk lfkedknail nacrmknewl eshpeasise lfvqkqqled ivspiiakms
      241 tprqvksars vi
//
LOCUS       NP_001382571             318 aa            linear   ROD 28-APR-2025
DEFINITION  ETS translocation variant 3-like protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001382571
VERSION     NP_001382571.1
DBSOURCE    REFSEQ: accession NM_001395642.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.12711.1,
                                           SRR26360181.257190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..318
                     /product="ETS translocation variant 3-like protein isoform
                     2"
                     /note="ets variant gene 3-like; ETS translocation variant
                     3-like protein; ets variant 3-like"
                     /calculated_mol_wt=35704
     Region          39..125
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..318
                     /gene="Etv3l"
                     /gene_synonym="RGD1562620"
                     /coded_by="NM_001395642.1:488..1444"
                     /note="isoform 2 is encoded by transcript variant w"
                     /db_xref="GeneID:499651"
                     /db_xref="RGD:1562620"
ORIGIN      
        1 mycncfsegi raapvnywis glafpdwayk aesspgsrqi qlwhfilell qkeefrhvia
       61 wqqgeygefv ikdpdevarl wgrrkckpqm nydklsralr yyynkrilhk tkgkrftykf
      121 nfsklivadc ppwkvwtpst pclllrppal cqtalvpvae qseplrsmlc tratgtqpar
      181 ertppqppea sgdkdsssfs sfgsvlgpgw qnpcccfwnh qgdlpsfasf apvpclccnw
      241 ahlsgpilpp lsseqplles lkpgprlpgp mwmpgawhfp glhllarlrq gteapevpqa
      301 pgiggkswpr akqapgfq
//
LOCUS       NP_001424448             859 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424448 XP_006250203
VERSION     NP_001424448.1
DBSOURCE    REFSEQ: accession NM_001437519.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Reubold,T.F., Faelber,K., Plattner,N., Posor,Y., Ketel,K.,
            Curth,U., Schlegel,J., Anand,R., Manstein,D.J., Noe,F., Haucke,V.,
            Daumke,O. and Eschenburg,S.
  TITLE     Crystal structure of the dynamin tetramer
  JOURNAL   Nature 525 (7569), 404-408 (2015)
   PUBMED   26302298
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Li,J., Zhang,D.S., Ye,J.C., Li,C.M., Qi,M., Liang,D.D., Xu,X.R.,
            Xu,L., Liu,Y., Zhang,H., Zhang,Y.Y., Deng,F.F., Feng,J., Shi,D.,
            Chen,J.J., Li,L., Chen,G., Sun,Y.F., Peng,L.Y. and Chen,Y.H.
  TITLE     Dynamin-2 mediates heart failure by modulating Ca2+ -dependent
            cardiomyocyte apoptosis
  JOURNAL   Int J Cardiol 168 (3), 2109-2119 (2013)
   PUBMED   23410488
  REMARK    GeneRIF: DNM2 mediates HF by modulating Ca(2+)-dependent apoptotic
            death of cardiomyocyte.
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Ikeuchi,Y., de la Torre-Ubieta,L., Matsuda,T., Steen,H., Okazawa,H.
            and Bonni,A.
  TITLE     The XLID protein PQBP1 and the GTPase Dynamin 2 define a signaling
            link that orchestrates ciliary morphogenesis in postmitotic neurons
  JOURNAL   Cell Rep 4 (5), 879-889 (2013)
   PUBMED   23994472
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Grossman,G.H., Ebke,L.A., Beight,C.D., Jang,G.F., Crabb,J.W. and
            Hagstrom,S.A.
  TITLE     Protein partners of dynamin-1 in the retina
  JOURNAL   Vis Neurosci 30 (4), 129-139 (2013)
   PUBMED   23746204
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Tanifuji,S., Funakoshi-Tago,M., Ueda,F., Kasahara,T. and Mochida,S.
  TITLE     Dynamin isoforms decode action potential firing for synaptic
            vesicle recycling
  JOURNAL   J Biol Chem 288 (26), 19050-19059 (2013)
   PUBMED   23687302
  REMARK    GeneRIF: dynamin isoforms select appropriate vesicle reuse pathways
            associated with specific neuronal firing patterns
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Gray,N.W., Fourgeaud,L., Huang,B., Chen,J., Cao,H., Oswald,B.J.,
            Hemar,A. and McNiven,M.A.
  TITLE     Dynamin 3 is a component of the postsynapse, where it interacts
            with mGluR5 and Homer
  JOURNAL   Curr Biol 13 (6), 510-515 (2003)
   PUBMED   12646135
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Zhang,Y., Moheban,D.B., Conway,B.R., Bhattacharyya,A. and
            Segal,R.A.
  TITLE     Cell surface Trk receptors mediate NGF-induced survival while
            internalized receptors regulate NGF-induced differentiation
  JOURNAL   J Neurosci 20 (15), 5671-5678 (2000)
   PUBMED   10908605
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Cao,H., Garcia,F. and McNiven,M.A.
  TITLE     Differential distribution of dynamin isoforms in mammalian cells
  JOURNAL   Mol Biol Cell 9 (9), 2595-2609 (1998)
   PUBMED   9725914
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Cook,T., Mesa,K. and Urrutia,R.
  TITLE     Three dynamin-encoding genes are differentially expressed in
            developing rat brain
  JOURNAL   J Neurochem 67 (3), 927-931 (1996)
   PUBMED   8752097
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Nakata,T., Takemura,R. and Hirokawa,N.
  TITLE     A novel member of the dynamin family of GTP-binding proteins is
            expressed specifically in the testis
  JOURNAL   J Cell Sci 105 (Pt 1), 1-5 (1993)
   PUBMED   8360266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Apr 3, 2025 this sequence version replaced XP_006250203.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.820707.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..859
                     /product="dynamin-3 isoform 2"
                     /EC_number="3.6.5.5"
                     /note="T-dynamin; dynamin, testicular; testicular dynamin"
                     /calculated_mol_wt=96719
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          514..625
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(516,518..519,521,538,607..608,611,614..615,618)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50570; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Region          645..735
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          742..859
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08877.2)"
     Region          <743..831
                     /region_name="MISS"
                     /note="MAPK-interacting and spindle-stabilising
                     protein-like; pfam15822"
                     /db_xref="CDD:318115"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     Site            843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17376771; propagated from
                     UniProtKB/Swiss-Prot (Q08877.2)"
     CDS             1..859
                     /gene="Dnm3"
                     /gene_synonym="dynamin-2"
                     /coded_by="NM_001437519.1:172..2751"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171574"
                     /db_xref="RGD:727949"
ORIGIN      
        1 mgnremeeli plvnrlqdaf salgqsclle lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvtskaey aeflhckgkk ftdfdevrhe ieaetdrvtg mnkgissvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqirdmi mqfitrencl ilavtpantd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yvgvvnrsqk
      241 didgkkdika amlaerkffl shpayrhiad rmgtphlqkv lnqqltnhir dtlpnfrnkl
      301 qgqllsiehe veafknfkpe dptrktkall qmvqqfavdf ekriegsgdq vdtlelsgga
      361 kinrifherf pfeivkmefn ekelrreisy aiknihgirt glftpdmafe aivkkqivkl
      421 kgpslksvdl vmqelintvk kctkrlanfp rlceeteriv anhireregk tkdqvlllid
      481 iqvsyintnh edfigfanaq qrssqvhkks tignqvirkg wltvsnigim kggskgywfv
      541 ltaeslswyk ddeekekkym lpldnlkvrd vekgfmsskh vfalfnteqr nvykdyrsle
      601 lacdsqedvd swkasllrag vypdksften dengqaenfs mdpqlerqve tirnlvdsym
      661 siinkcirdl ipktimhlmi nnvkdfinse llaqlyssed qntlmeesve qaqrrdemlr
      721 myqalkeala iigdintvtv stpapppvdd swlqhsrrsp ppspttqrrl tlsaplprpa
      781 ssrgpapaip spgphsgapp vpfrpgplpp fpnssdsyga ppqvpsrptr appsvpsrrp
      841 ppsptrptii rplesslld
//
LOCUS       NP_001420299             938 aa            linear   ROD 28-APR-2025
DEFINITION  catenin delta-1 isoform b [Rattus norvegicus].
ACCESSION   NP_001420299 XP_038960802
VERSION     NP_001420299.1
DBSOURCE    REFSEQ: accession NM_001433370.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Xiao,Z.P., Zhao,J.L., Rong,W.L., Jiang,J.W. and Li,M.H.
  TITLE     Role of Vascular Endothelial-Cadherin and p120-Catenin in the
            Formation of Experimental Intracranial Aneurysm in Animals
  JOURNAL   World Neurosurg 128, e177-e184 (2019)
   PUBMED   30995547
  REMARK    GeneRIF: Decreased expression of p120-catenin was detected in
            intracranial aneurysm endothelium.
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Caldwell,J.M., Collins,M.H., Kemme,K.A., Sherrill,J.D., Wen,T.,
            Rochman,M., Stucke,E.M., Amin,L., Tai,H., Putnam,P.E.,
            Jimenez-Dalmaroni,M.J., Wormald,M.R., Porollo,A., Abonia,J.P. and
            Rothenberg,M.E.
  TITLE     Cadherin 26 is an alpha integrin-binding epithelial receptor
            regulated during allergic inflammation
  JOURNAL   Mucosal Immunol 10 (5), 1190-1201 (2017)
   PUBMED   28051089
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Jiang,Y., Liao,L., Shrestha,C., Ji,S., Chen,Y., Peng,J., Wang,L.,
            Liao,E. and Xie,Z.
  TITLE     Reduced expression of E-cadherin and p120-catenin and elevated
            expression of PLC-gamma1 and PIKE are associated with
            aggressiveness of oral squamous cell carcinoma
  JOURNAL   Int J Clin Exp Pathol 8 (8), 9042-9051 (2015)
   PUBMED   26464646
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Ranchoux,B., Antigny,F., Rucker-Martin,C., Hautefort,A.,
            Pechoux,C., Bogaard,H.J., Dorfmuller,P., Remy,S., Lecerf,F.,
            Plante,S., Chat,S., Fadel,E., Houssaini,A., Anegon,I., Adnot,S.,
            Simonneau,G., Humbert,M., Cohen-Kaminsky,S. and Perros,F.
  TITLE     Endothelial-to-mesenchymal transition in pulmonary hypertension
  JOURNAL   Circulation 131 (11), 1006-1018 (2015)
   PUBMED   25593290
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Chen,Y.M., Lee,N.P., Mruk,D.D., Lee,W.M. and Cheng,C.Y.
  TITLE     Fer kinase/FerT and adherens junction dynamics in the testis: an in
            vitro and in vivo study
  JOURNAL   Biol Reprod 69 (2), 656-672 (2003)
   PUBMED   12700184
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Katafiasz,B.J., Nieman,M.T., Wheelock,M.J. and Johnson,K.R.
  TITLE     Characterization of cadherin-24, a novel alternatively spliced type
            II cadherin
  JOURNAL   J Biol Chem 278 (30), 27513-27519 (2003)
   PUBMED   12734196
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Chauvet,N., Prieto,M., Fabre,C., Noren,N.K. and Privat,A.
  TITLE     Distribution of p120 catenin during rat brain development:
            potential role in regulation of cadherin-mediated adhesion and
            actin cytoskeleton organization
  JOURNAL   Mol Cell Neurosci 22 (4), 467-486 (2003)
   PUBMED   12727444
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Holsinger,L.J., Ward,K., Duffield,B., Zachwieja,J. and Jallal,B.
  TITLE     The transmembrane receptor protein tyrosine phosphatase DEP1
            interacts with p120(ctn)
  JOURNAL   Oncogene 21 (46), 7067-7076 (2002)
   PUBMED   12370829
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Golenhofen,N. and Drenckhahn,D.
  TITLE     The catenin, p120ctn, is a common membrane-associated protein in
            various epithelial and non-epithelial cells and tissues
  JOURNAL   Histochem Cell Biol 114 (2), 147-155 (2000)
   PUBMED   11052263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Aug 9, 2024 this sequence version replaced XP_038960802.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760389, SAMEA5760476
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..938
                     /product="catenin delta-1 isoform b"
                     /note="catenin src; catenin (cadherin associated protein),
                     delta 1; p120 catenin"
                     /calculated_mol_wt=104762
     Region          368..393
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(384,388,392,426,430,434,470,474,478)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          397..437
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          401..437
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          440..481
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          444..479
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          486..537
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          632..>740
                     /region_name="Syo1_like"
                     /note="Fungal symportin 1 (syo1) and similar proteins;
                     cl23709"
                     /db_xref="CDD:474028"
     Region          656..693
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          703..738
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          703..737
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          793..829
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..938
                     /gene="Ctnnd1"
                     /gene_synonym="Catns; P120"
                     /coded_by="NM_001433370.1:388..3204"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:311163"
                     /db_xref="RGD:1305643"
ORIGIN      
        1 mddsevesta silasvkeqe aqfekltral eeerrhvsaq lervrvspqd anslmangtl
       61 trrhqngrfv gdadlerqkf sdlklngpqd hnhllystip rmqepgqive tyteedpega
      121 msvvsvetsd dgttrrtett vkkvvktmtt rtvqpvpmgp dglpvdasav snnyiqtlgr
      181 dfrkngnggp gpyvgqagta tlprnfhypp dgygrhyedg ypggsdnygs lsrvtrieer
      241 yrpsmegyra psrqdvygpq pqvrvggssv dlhrfhpepy gleddqrsmg yddldygmms
      301 dygtarrtgt psdprrrlrs yedmigeevp pdqyywapla qhergslasl dslrkgmppp
      361 pnwrqpelpe viamlgfrld avksnaaayl qhlcyrndkv ktdvrklkgi pilvglldhp
      421 kkevhlgacg alknisfgrd qdnkiaiknc dgvpalvrll rkardmdlte vitgtlwnls
      481 shdsikmeiv dhalhaltde viiphsgwer epnedckprh iewesvltnt agclrnvsse
      541 rsearrklre cdglvdalif ivqaeigqkd sdsklvencv cllrnlsyqv hreipqaery
      601 qealpsvans tgphaascfg akkgkdewfs rgkkptedpa ndtvdfpkrt spargyellf
      661 qpevvriyis llkesktpai leasagaiqn lcagrwtygr yirsalrqek alsaiadllt
      721 sehervvkaa sgalrnlavd arnkeligkh aipnlvknlp ggqqnsswnf sedtvvsiln
      781 tineviaenl eaakklretq gieklvlink sgnrsekevr aaalvlqtiw gykelrkple
      841 kegwkksdfq vnlnnasrsq sshsyddstl plidrnqksd kkpdreeipm snmgsntksl
      901 dnnystlner gdhnrtldrs gdlgdmeplk gaplmqki
//
LOCUS       NP_001423802             925 aa            linear   ROD 28-APR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001423802 XP_006252864
VERSION     NP_001423802.1
DBSOURCE    REFSEQ: accession NM_001436873.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006252864.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.37983.1,
                                           SRR26643295.52214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..925
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 1"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=100902
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..925
                     /gene="Eps15l1"
                     /coded_by="NM_001436873.1:35..2812"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskp ppsgpfsssl ggtgfsddpf kskqdtpalp
      781 pkkpapprpk ppseaaagqk gsvvytllgg qstpvsqlgs safpespdpf qpleadsgdp
      841 fqnkkgfgdp fsgkdpfaps ssakppkass sgfadftsfg neeqqlawak resekaeqer
      901 larlrrqeqe dlelaialsk admpa
//
LOCUS       NP_001420210             514 aa            linear   ROD 28-APR-2025
DEFINITION  ankyrin repeat and ubiquitin domain containing 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001420210 XP_063138778
VERSION     NP_001420210.1
DBSOURCE    REFSEQ: accession NM_001433281.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Aug 8, 2024 this sequence version replaced XP_063138778.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1833419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..514
                     /product="ankyrin repeat and ubiquitin domain containing 1
                     isoform 2"
                     /note="no mechanoreceptor potential C-like"
                     /calculated_mol_wt=58031
     Region          <3..50
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          52..134
                     /region_name="Ubl2_ANKUB1"
                     /note="ubiquitin-like (Ubl) domain 2 found in Ankyrin
                     repeat and ubiquitin domain-containing 1 (ANKUB1) and
                     similar proteins; cd17051"
                     /db_xref="CDD:340571"
     Region          167..204
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          168..268
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(169..170,173..175,177..178,182,185,204,206,208,
                     217..218,221..223,225..226,230,233,243,245,247,251..252,
                     255..257,259..260,264,267)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          206..243
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..514
                     /gene="Ankub1"
                     /coded_by="NM_001433281.1:425..1969"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100361272"
                     /db_xref="RGD:2320491"
ORIGIN      
        1 mvdyfhipls edkqgrwyle ltyagaalkn nwslsdvgis fcstlkcfvk kedkptlyvf
       61 navtqetmai kenmsildrk vsdlrmlvtl scgfpvsvyc lrtpaglemy dcntlkdyqt
      121 digttlrldv wdgwkeflmg cllgqkpkvq rylskegpvl kyqkrvalyi aafhghtelt
      181 ewalkqgaqp heavgvhpcr awchealhtd vsncpihaaa eagqllilka fvnfsvlcle
      241 cknaagqspl aiaskhqhkd cvlyllskiw stvsflklsv pmriyikikq wilraqtrrc
      301 hksqpsrarv sgakvgdtvm vdgftkpkmt skswykaedk swhtaqsklp pckqqpsrkp
      361 igslpmsqhd tkkqiftfps lvdaknfsev qsyqqenqkk iaaparkekn iknpylpqvp
      421 lppvsrvhya hpqfyctpps gdcllrslfk sfsehsgrtp renaiyclav asafkekrwl
      481 qqleiarvla krsisnltvk ggpakcenyp esvl
//
LOCUS       NP_001256968             585 aa            linear   ROD 28-APR-2025
DEFINITION  ankyrin repeat domain-containing protein 55 [Rattus norvegicus].
ACCESSION   NP_001256968 XP_001066855 XP_342196
VERSION     NP_001256968.1
DBSOURCE    REFSEQ: accession NM_001270039.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   denDekker,A.D., Xu,X., Vaughn,M.D., Puckett,A.H., Gardner,L.L.,
            Lambring,C.J., Deschenes,L. and Samuelson,D.J.
  TITLE     Rat Mcs1b is concordant to the genome-wide association-identified
            breast cancer risk locus at human 5q11.2 and MIER3 is a candidate
            cancer susceptibility gene
  JOURNAL   Cancer Res 72 (22), 6002-6012 (2012)
   PUBMED   22993404
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from JQ013731.1.
            
            On or before Jun 27, 2012 this sequence version replaced
            XP_342196.5, XP_001066855.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ013731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..585
                     /product="ankyrin repeat domain-containing protein 55"
                     /calculated_mol_wt=64188
     Region          <29..238
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          31..62
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(64,66,70..71,74..76,78..79,83,86,95,97,99,103..104,
                     107..109,111..112,116,119,130,132,134,138..139,142..144,
                     146..147,151,154,163)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          64..95
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          97..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          132..163
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          165..233
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          201..226
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          207..288
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          235..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..585
                     /gene="Ankrd55"
                     /gene_synonym="RGD1307735"
                     /coded_by="NM_001270039.1:907..2664"
                     /db_xref="GeneID:361898"
                     /db_xref="RGD:1307735"
ORIGIN      
        1 mvyqaasngd vnsltavire dpsileccds egctplmhav sgrqvdtvkl llkmganint
       61 qdaygrtslc latylgwleg cvsllrngak hnipdkngrl plhaataepd vrllivllqq
      121 sslseinhqd tegmtplhwa afhnrpqhtq mllkkgadpt lvdkdfktal hwavqsgnri
      181 lcsiilshrq gpsiinydde sgktcvhiaa asgfgdiihd lakvpecnlq aldvddrtpl
      241 hwaaaagkae cvqslldlgm dsnlrdines tplayalycg htacvrllsr egraeparsl
      301 psqnsqpqkk egrfsvlnqi fcknkkeeqk ahqkeqsrar pkeedtsevn diiatfdsvv
      361 dtncqdqpgd qvdmvvfkkr tsenskyllp ekkslarkgl ppirtqslpp itlgsnflta
      421 shgatshagl nsglqhtaqr sqksrseqdl lnnrtgcqvs ldnpwkgdtr qafsckawtv
      481 sssdklldrm ftgqpghqel sgpphlphlp npspgqglqh lspnrpkvrd fpftrnslap
      541 lpdqkflsge plrtnrvlpa ipsqrghdpp aeesewsssp thden
//
LOCUS       NP_001380783             617 aa            linear   ROD 28-APR-2025
DEFINITION  SLAIN motif-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001380783 XP_038949461
VERSION     NP_001380783.1
DBSOURCE    REFSEQ: accession NM_001393854.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Mar 18, 2021 this sequence version replaced XP_038949461.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2158181.1,
                                           SRR26643298.58315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..617
                     /product="SLAIN motif-containing protein 1 isoform 1"
                     /note="SLAIN motif-containing protein 1"
                     /calculated_mol_wt=65903
     Region          185..617
                     /region_name="SLAIN"
                     /note="SLAIN motif-containing family; pfam15301"
                     /db_xref="CDD:464627"
     CDS             1..617
                     /gene="Slain1"
                     /gene_synonym="RGD1308626"
                     /coded_by="NM_001393854.1:187..2040"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361087"
                     /db_xref="RGD:1308626"
ORIGIN      
        1 mmaeqvkcas pvagsgagpg pvvnaelevk klqelvrkle kqneqlrsra asaaaaphll
       61 llqppppsap ppagacsplt thrapastts pgpgalgpaf pgtyclpspa psllcslqpa
      121 dapfvyskpa agffagggsp epwtagtppg eaatpplppp tlldevepld leslaawsed
      181 ddytwlyigs sktftlseks lsplqwcrhv ldnptpemea arrslrfrle qasrwrslfs
      241 spaslafpys pvarlspysn gistpssskt snkailtper tgytsrgspl spqssidsel
      301 stseleddsi smgyklqdlt dvqimarlqe eslrqdcast sgsvsrnsst islssgkkgt
      361 csdqeydrys ledeeefdhl pppqprlprc spfqrgiphs qtfssirdcr rspssqyfps
      421 nnfqqpqyys pqaqtpdqqp nrtngdklrr smpnlarmps ttavssnlss pvtvrssqsf
      481 dsslhgagsg vsrvpscips pgqiqhrvhs vghfpvpirq plkatayvsp tvqgssssmp
      541 lsngtqlysn tgiptpnkaa asgimgrsal prpslaings nlprskiaqp vrsflqppkp
      601 lsslstlrdg nwrdgcy
//
LOCUS       NP_001418958            1621 aa            linear   ROD 28-APR-2025
DEFINITION  androglobin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001418958 XP_038954415
VERSION     NP_001418958.1
DBSOURCE    REFSEQ: accession NM_001432029.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 24, 2024 this sequence version replaced XP_038954415.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.810728.1,
                                           SRR26643293.70.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..1621
                     /product="androglobin isoform 2"
                     /calculated_mol_wt=184342
     Region          92..>299
                     /region_name="CysPc"
                     /note="Calpains, domains IIa, IIb; calcium-dependent
                     cytoplasmic cysteine proteinases, papain-like. Functions
                     in cytoskeletal remodeling processes, cell
                     differentiation, apoptosis and signal transduction;
                     cl00051"
                     /db_xref="CDD:469591"
     Region          779..1191
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          780..786
                     /region_name="globin helix C"
                     /note="globin helix C [structural motif]"
                     /db_xref="CDD:412094"
     Region          795..800
                     /region_name="globin helix D"
                     /note="globin helix D [structural motif]"
                     /db_xref="CDD:412094"
     Region          802..822
                     /region_name="globin helix E"
                     /note="globin helix E [structural motif]"
                     /db_xref="CDD:412094"
     Region          833..842
                     /region_name="globin helix F"
                     /note="globin helix F [structural motif]"
                     /db_xref="CDD:412094"
     Region          855..873
                     /region_name="globin helix G"
                     /note="globin helix G [structural motif]"
                     /db_xref="CDD:412094"
     Region          882..905
                     /region_name="globin helix H"
                     /note="globin helix H [structural motif]"
                     /db_xref="CDD:412094"
     Region          928..946
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     Region          955..971
                     /region_name="globin helix A"
                     /note="globin helix A [structural motif]"
                     /db_xref="CDD:412094"
     Region          972..985
                     /region_name="globin helix B"
                     /note="globin helix B [structural motif]"
                     /db_xref="CDD:412094"
     Region          1310..>1605
                     /region_name="Caldesmon"
                     /note="pfam02029"
                     /db_xref="CDD:460421"
     CDS             1..1621
                     /gene="Adgb"
                     /gene_synonym="RGD1564259"
                     /coded_by="NM_001432029.1:78..4943"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:292477"
                     /db_xref="RGD:1564259"
ORIGIN      
        1 mtskqakrke vhrinsahgs dkskdlypfg snvppgsseq krgkfpiwpe wseadinaek
       61 wdagkggkek dktgkspifh ffedpegkie lpqslkvfsw krpqdfifsr ipvvvknemt
      121 fdlfssnghl lcselmrwii seiyavwkif nggilsnyyk gnsgelpilp wkpwehiysl
      181 ckaakghmpl fnsygkyvvk lywmgcwrki tvddflpfde dnnlllpatt ydfelwpmll
      241 skaiiklanv dihvahrrel geltvihalt gwlpeviplh payvdkvwel lkeilpefkl
      301 teepsseski tvienklkep tkenkdvkdg kdgkdgkdgk eakdgketkd gketkdakdf
      361 kpeislttlk apekgdraak ekadakdlgk knkkdgekek erfkfslhgs rpssdvqysm
      421 qslsdcssai qspqmvvyat ftplylfenk iftlekmans aeklreygls hicshpvlvt
      481 rsrscplvap pkppplpawk lirhkketvi tdeaqdavpk kpeqfleiss pflnyrmapf
      541 tiptethfvq svikkgtplg sslpplvesd laastsqgem siiagnqsqa nialqttpgk
      601 depsepalad ahqleaisle rdlislttat ldksqeelav nesvskeiwl dfedfcvcfh
      661 hiyifhkpns yclnfqksef kfmeervpyy lfvdslkpie llvcfsalvr wgesgaltke
      721 sppvepgllt aeaitwkslk plsvvlriht yatkasmvrl pvgrhmllfn ayspvghaih
      781 vcsmttfvig dedvvlpnfe pesyrfteqs vmimkaignv ianfkdrgkl paalrdlqaa
      841 hypiplnnke ltlqhfrvfh islwrlmkks qvakpplnfk faframvldt dlldsfseda
      901 slaewvdlky smpvnekeys peeiaaavki qsmwkgnyvr llmkartpet kenisvadtl
      961 qkiwavlemn leqyalsllr lmfkskcksm esypcyqdee tklafadhtv nytdqppnsw
     1021 fivfretflv pqdiillpkv yttlqicmlh vinndtleqv pkvfqkvvpy lysknkkgyt
     1081 fvaeaytgds fvsgsrwklr ligsynplpf lardtpcstf tikeirdyyi pndkkilfry
     1141 sikvtmaqsi tiqvrtskpd afiklqvles eeiimstvgk gqalipafyf lgnekalssq
     1201 sskqvlltht lpkkepevlt kkkagqpgqk sfkgrtgggm tetgmpllee evmsvptiee
     1261 nsstpqqcyk yiiqclvlfn swplnetqlt fvqalkdmek idikahvekh eepapmgspd
     1321 shavsegqks vgmpkttrkg kersaekeks arekqtprfe pqqmqvptaa hsqqedpnkp
     1381 ywtlrlvseh tdseyvdvkk dteradeira mkqawettep graikasqar lkyltqfikk
     1441 ppetsapats pealsvtqsq iksseevvvq srsptilets pqqirkalef ldfnhyvrkt
     1501 adeavlqtde lskhqamqka eeihqfrqyr arilsirdid qeervklkde vldmygemrd
     1561 svdearqkif direeyrnkl leaerlrmea laaqeaavkl eaekktaasd pqkkkkggkk
     1621 k
//
LOCUS       NP_058965               1237 aa            linear   ROD 28-APR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase eta isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_058965 XP_346664
VERSION     NP_058965.3
DBSOURCE    REFSEQ: accession NM_017269.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Dorofejeva,O. and Barr,A.J.
  TITLE     Defining the molecular basis of interaction between R3
            receptor-type protein tyrosine phosphatases and VE-cadherin
  JOURNAL   PLoS One 12 (9), e0184574 (2017)
   PUBMED   28926625
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Shintani,T., Higashi,S., Takeuchi,Y., Gaudio,E., Trapasso,F.,
            Fusco,A. and Noda,M.
  TITLE     The R3 receptor-like protein tyrosine phosphatase subfamily
            inhibits insulin signalling by dephosphorylating the insulin
            receptor at specific sites
  JOURNAL   J Biochem 158 (3), 235-243 (2015)
   PUBMED   26063811
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Petermann,A., Haase,D., Wetzel,A., Balavenkatraman,K.K., Tenev,T.,
            Guhrs,K.H., Friedrich,S., Nakamura,M., Mawrin,C. and Bohmer,F.D.
  TITLE     Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives
            meningioma cell motility
  JOURNAL   Brain Pathol 21 (4), 405-418 (2011)
   PUBMED   21091576
REFERENCE   4  (residues 1 to 1237)
  AUTHORS   Omerovic,J., Clague,M.J. and Prior,I.A.
  TITLE     Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent
            negative regulators of PKB/Akt activation in Ras-mutated cancer
            cells
  JOURNAL   Biochem J 426 (1), 65-72 (2010)
   PUBMED   19922411
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1237)
  AUTHORS   Tarcic,G., Boguslavsky,S.K., Wakim,J., Kiuchi,T., Liu,A.,
            Reinitz,F., Nathanson,D., Takahashi,T., Mischel,P.S., Ng,T. and
            Yarden,Y.
  TITLE     An unbiased screen identifies DEP-1 tumor suppressor as a
            phosphatase controlling EGFR endocytosis
  JOURNAL   Curr Biol 19 (21), 1788-1798 (2009)
   PUBMED   19836242
REFERENCE   6  (residues 1 to 1237)
  AUTHORS   Baker,J.E., Majeti,R., Tangye,S.G. and Weiss,A.
  TITLE     Protein tyrosine phosphatase CD148-mediated inhibition of T-cell
            receptor signal transduction is associated with reduced LAT and
            phospholipase Cgamma1 phosphorylation
  JOURNAL   Mol Cell Biol 21 (7), 2393-2403 (2001)
   PUBMED   11259588
REFERENCE   7  (residues 1 to 1237)
  AUTHORS   Kovalenko,M., Denner,K., Sandstrom,J., Persson,C., Gross,S.,
            Jandt,E., Vilella,R., Bohmer,F. and Ostman,A.
  TITLE     Site-selective dephosphorylation of the platelet-derived growth
            factor beta-receptor by the receptor-like protein-tyrosine
            phosphatase DEP-1
  JOURNAL   J Biol Chem 275 (21), 16219-16226 (2000)
   PUBMED   10821867
REFERENCE   8  (residues 1 to 1237)
  AUTHORS   Tangye,S.G., Wu,J., Aversa,G., de Vries,J.E., Lanier,L.L. and
            Phillips,J.H.
  TITLE     Negative regulation of human T cell activation by the receptor-type
            protein tyrosine phosphatase CD148
  JOURNAL   J Immunol 161 (8), 3803-3807 (1998)
   PUBMED   9780142
REFERENCE   9  (residues 1 to 1237)
  AUTHORS   de la Fuente-Garcia,M.A., Nicolas,J.M., Freed,J.H., Palou,E.,
            Thomas,A.P., Vilella,R., Vives,J. and Gaya,A.
  TITLE     CD148 is a membrane protein tyrosine phosphatase present in all
            hematopoietic lineages and is involved in signal transduction on
            lymphocytes
  JOURNAL   Blood 91 (8), 2800-2809 (1998)
   PUBMED   9531590
REFERENCE   10 (residues 1 to 1237)
  AUTHORS   Borges,L.G., Seifert,R.A., Grant,F.J., Hart,C.E., Disteche,C.M.,
            Edelhoff,S., Solca,F.F., Lieberman,M.A., Lindner,V., Fischer,E.H.,
            Lok,S. and Bowen-Pope,D.F.
  TITLE     Cloning and characterization of rat density-enhanced phosphatase-1,
            a protein tyrosine phosphatase expressed by vascular cells
  JOURNAL   Circ Res 79 (3), 570-580 (1996)
   PUBMED   8781490
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 4, 2022 this sequence version replaced NP_058965.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760386, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..1237
                     /product="receptor-type tyrosine-protein phosphatase eta
                     isoform 1 precursor"
                     /EC_number="3.1.3.48"
                     /note="density enhanced phosphatase-1; receptor-type
                     tyrosine-protein phosphatase eta"
                     /calculated_mol_wt=132356
     sig_peptide     1..36
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4010
     Region          57..547
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          530..607
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          738..868
                     /region_name="PTP_tm"
                     /note="TM proximal of protein tyrosine phosphatase,
                     receptor type J; pfam18861"
                     /db_xref="CDD:465889"
     Region          969..1197
                     /region_name="R-PTPc-J"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase J; cd14615"
                     /db_xref="CDD:350463"
     CDS             1..1237
                     /gene="Ptprj"
                     /gene_synonym="DEP-1"
                     /coded_by="NM_017269.4:345..4058"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29645"
                     /db_xref="RGD:3454"
ORIGIN      
        1 mkpaaretrt pprspglrwa llplllllrq gqvvcagaap spvfdveavt sptsvvltwk
       61 hndsatseyk inegntlryt vknqtsfnit glspatsykf sitlgtvnet sgkptyknit
      121 tepwpvsdlq vayigvtqal lawsnangta syrmqivelt tnssggisdl kpgthkslav
      181 qgsnetqhdl wvtegvsdan gtegspvani sqlhknslas adppsardps ltevlltelk
      241 pdtqykvtiy sqaadgtegq pgnkvfktnp iqvsdiravn isdsnmtltw ksnnneshas
      301 ftykiyvagg sdsinetvne tqavirglss stlynitvlp flgqtagipg flqvytsprp
      361 vsdfrvtnvs lreiglawrs ndsesfeifi tqegsekrwn astgdlsyiv enlkpgtsyq
      421 feifprgpng tegpsqtvvg rtdcsavtdi rvvsvsttei qlewqntdsa sgytyhlvle
      481 sengsiktns sqkwitvggl tpgtlynvti fpevdqmegn sssitqytrp snvsyievnt
      541 nttvaaiqwk nldaasasys ysvlilkagd gsnvtsrvrd ipsvtipgli pgvsyevkif
      601 tkirntevgn evpgqklfcm epaqvdslhc evvpkepalv lkwacppgmn sgfelgvrsd
      661 awdnmthlen ctldndtecr tevtylnfst synisiatls cgkmalptqs tcttgitdpp
      721 ppdgspnits vshnsvkvkf sgfeashgpi kayavllttg eagqpstdvl kytyedfkkg
      781 asdtyvtyli rieekgqsqg lsealnyeid vgnqsttlgy yngrleplgs yracvagftn
      841 itynlqndgl ingdesyvsf spyseavslp qdpgvicgav fgcifgalai vavggfifwr
      901 kkrkdaknne vsfsqikskl irvenfeayf kkqqadsncg faeeyedlkl igislpkyaa
      961 eiaenrgknr ynnvlpydis rvklsvqths tddyinanym pgyhskkdfi atqgplpntl
     1021 kdfwrmvwek nvyaivmltk cveqgrtkce eywpskqaqd ygditvamts evvlpewtir
     1081 dfvvknmqss eshplrqfhf tswpdhgvpd ttdllinfry lvrdymkqip pespilvhcs
     1141 agvgrtgtfi aidrliyqie nentvdvygi vydlrmhrpl mvqtedqyvf lnqcvldiir
     1201 aqkdskvdli yqnttamtiy enlepvsmfg ktngyia
//
LOCUS       NP_001420207             276 aa            linear   ROD 28-APR-2025
DEFINITION  meiotic recombination protein REC114 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001420207 XP_006243219
VERSION     NP_001420207.1
DBSOURCE    REFSEQ: accession NM_001433278.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Aug 8, 2024 this sequence version replaced XP_006243219.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.19488.1,
                                           SRR26360186.648802.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..276
                     /product="meiotic recombination protein REC114 isoform 1"
                     /note="meiotic recombination protein REC114"
                     /calculated_mol_wt=29880
     Region          20..271
                     /region_name="REC114-like"
                     /note="Meiotic recombination protein REC114-like;
                     pfam15165"
                     /db_xref="CDD:464541"
     CDS             1..276
                     /gene="Rec114"
                     /gene_synonym="RGD1311874"
                     /coded_by="NM_001433278.1:36..866"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300751"
                     /db_xref="RGD:1311874"
ORIGIN      
        1 maeagnvasg lglpgevsqw plrrygrfml ldngespgps saaaaapspt wkvrpegqkg
       61 ppaarspgkv fesseesgcl vltivvsghf fisqgqtlle gfsligsknw lkivrrmdcl
      121 lfgttikdks rmfrvqfsge sqeealehcc gcvqtltqyv tvqepdritq elqqspgpre
      181 agesqgkdpl qqgsslileq hvcmaagtgl leertsvthl aqsilapekl tlayegsswg
      241 aeelgpflrl clmdqnfpaf veevekelkk itglrn
//
LOCUS       NP_001103377             489 aa            linear   ROD 28-APR-2025
DEFINITION  double-stranded RNA-binding protein Staufen homolog 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001103377
VERSION     NP_001103377.1
DBSOURCE    REFSEQ: accession NM_001109907.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Lee,K., Yoo,K.S., Park,Y.S. and Kim,H.K.
  TITLE     Activity of Arhgef4 is modulated through Staufen1 in neurons
  JOURNAL   Neurosci Lett 756, 135962 (2021)
   PUBMED   34022264
  REMARK    GeneRIF: Activity of Arhgef4 is modulated through Staufen1 in
            neurons.
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Xue,Y., Guo,Y., Luo,S., Zhou,W., Xiang,J., Zhu,Y., Xiang,Z. and
            Shen,J.
  TITLE     Aberrantly Methylated-Differentially Expressed Genes Identify Novel
            Atherosclerosis Risk Subtypes
  JOURNAL   Front Genet 11, 569572 (2020)
   PUBMED   33381146
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Blackham,S.L. and McGarvey,M.J.
  TITLE     A host cell RNA-binding protein, Staufen1, has a role in hepatitis
            C virus replication before virus assembly
  JOURNAL   J Gen Virol 94 (Pt 11), 2429-2436 (2013)
   PUBMED   23907398
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Ghoujal,B., Milev,M.P., Ajamian,L., Abel,K. and Mouland,A.J.
  TITLE     ESCRT-II's involvement in HIV-1 genomic RNA trafficking and
            assembly
  JOURNAL   Biol Cell 104 (12), 706-721 (2012)
   PUBMED   22978549
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Villace,P., Marion,R.M. and Ortin,J.
  TITLE     The composition of Staufen-containing RNA granules from human cells
            indicates their role in the regulated transport and translation of
            messenger RNAs
  JOURNAL   Nucleic Acids Res 32 (8), 2411-2420 (2004)
   PUBMED   15121898
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Macchi,P., Kroening,S., Palacios,I.M., Baldassa,S., Grunewald,B.,
            Ambrosino,C., Goetze,B., Lupas,A., St Johnston,D. and Kiebler,M.
  TITLE     Barentsz, a new component of the Staufen-containing
            ribonucleoprotein particles in mammalian cells, interacts with
            Staufen in an RNA-dependent manner
  JOURNAL   J Neurosci 23 (13), 5778-5788 (2003)
   PUBMED   12843282
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Monshausen,M., Rehbein,M., Richter,D. and Kindler,S.
  TITLE     The RNA-binding protein Staufen from rat brain interacts with
            protein phosphatase-1
  JOURNAL   J Neurochem 81 (3), 557-564 (2002)
   PUBMED   12065664
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Monshausen,M., Putz,U., Rehbein,M., Schweizer,M.,
            DesGroseillers,L., Kuhl,D., Richter,D. and Kindler,S.
  TITLE     Two rat brain staufen isoforms differentially bind RNA
  JOURNAL   J Neurochem 76 (1), 155-165 (2001)
   PUBMED   11145988
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Kiebler,M.A., Hemraj,I., Verkade,P., Kohrmann,M., Fortes,P.,
            Marion,R.M., Ortin,J. and Dotti,C.G.
  TITLE     The mammalian staufen protein localizes to the somatodendritic
            domain of cultured hippocampal neurons: implications for its
            involvement in mRNA transport
  JOURNAL   J Neurosci 19 (1), 288-297 (1999)
   PUBMED   9870958
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN932990.1 and BC081755.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region, compared to variant 1, resulting in a shorter
            protein (isoform 2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF290989.1, BC101858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..489
                     /product="double-stranded RNA-binding protein Staufen
                     homolog 1 isoform 2"
                     /note="staufen RNA binding protein homolog 1;
                     double-stranded RNA-binding protein Staufen homolog 1"
                     /calculated_mol_wt=53997
     Region          1..70
                     /region_name="DSRM_SF"
                     /note="double-stranded RNA binding motif (DSRM)
                     superfamily; cl00054"
                     /db_xref="CDD:444671"
     Site            order(16..17,19,39,56..58,61)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380679"
     Region          95..161
                     /region_name="DSRM_STAU1_rpt3"
                     /note="third double-stranded RNA binding motif of
                     double-stranded RNA-binding protein Staufen homolog 1
                     (Staufen 1) and similar proteins; cd19883"
                     /db_xref="CDD:380712"
     Site            order(95,100,103..104,106..107,121..126,146,150)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380712"
     Region          188..273
                     /region_name="DSRM_STAU1_rpt4"
                     /note="fourth double-stranded RNA binding motif of
                     double-stranded RNA-binding protein Staufen homolog 1
                     (Staufen 1) and similar proteins; cd19885"
                     /db_xref="CDD:380714"
     Site            order(202,205..206,208..209,224..229,249,253)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380714"
     Region          360..469
                     /region_name="Staufen_C"
                     /note="Staufen C-terminal domain; pfam16482"
                     /db_xref="CDD:465131"
     CDS             1..489
                     /gene="Stau1"
                     /gene_synonym="Stau"
                     /coded_by="NM_001109907.1:240..1709"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84496"
                     /db_xref="RGD:621778"
ORIGIN      
        1 mykpvdphsr mqstysygmr ggayppryfy pfpvppllyq velsvggqqf ngkgkmrppv
       61 khdataralr tlqseplper levngresee enlnkseisq vfeialkrnl pvnfevares
      121 gpphmknfvt rvsvgefvge gegkskkisk knaaravleq lrrlpplpav ervkprikkk
      181 sqptcklqta pdygqgmnpi srlaqiqqak kekepeymll terglprrre fvmqvkvghh
      241 taegagtnkk vakrnaaenm leilgfkvpq aqpakpalks eektpvkkpg dgrkvtffep
      301 spgdengtsn kedefrmpyl shqqlpagil pmvpevaqav gvsqghhtkd faraapnpak
      361 atvtamiare llyggtspta etilksniss ghvphgprtr pseqlyylsr aqgfqveykd
      421 fpknnknecv slincssqpp lvshgigkdv eschdmaaln ilkllseldq qstemprtgn
      481 gpvsacgrc
//
LOCUS       NP_001418509            1250 aa            linear   ROD 28-APR-2025
DEFINITION  neural cell adhesion molecule L1 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001418509 XP_017457630
VERSION     NP_001418509.1
DBSOURCE    REFSEQ: accession NM_001431580.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1250)
  AUTHORS   Gallo,P.N., Mihelc,E., Eisert,R., Bradshaw,G.A., Dimek,F.,
            Leffler,A., Kalocsay,M. and Moiseenkova-Bell,V.
  TITLE     The dynamic TRPV2 ion channel proximity proteome reveals functional
            links of calcium flux with cellular adhesion factors NCAM and L1CAM
            in neurite outgrowth
  JOURNAL   Cell Calcium 121, 102894 (2024)
   PUBMED   38728789
  REMARK    GeneRIF: The dynamic TRPV2 ion channel proximity proteome reveals
            functional links of calcium flux with cellular adhesion factors
            NCAM and L1CAM in neurite outgrowth.
REFERENCE   2  (residues 1 to 1250)
  AUTHORS   Platek,R., Grycz,K., Wieckowska,A., Czarkowska-Bauch,J. and Skup,M.
  TITLE     L1 Cell Adhesion Molecule Overexpression Down Regulates Phosphacan
            and Up Regulates Structural Plasticity-Related Genes Rostral and
            Caudal to the Complete Spinal Cord Transection
  JOURNAL   J Neurotrauma 37 (3), 534-554 (2020)
   PUBMED   31426714
  REMARK    GeneRIF: L1 Cell Adhesion Molecule Overexpression Down Regulates
            Phosphacan and Up Regulates Structural Plasticity-Related Genes
            Rostral and Caudal to the Complete Spinal Cord Transection.
REFERENCE   3  (residues 1 to 1250)
  AUTHORS   Emmert,A.S., Vuong,S.M., Shula,C., Lindquist,D., Yuan,W., Hu,Y.C.,
            Mangano,F.T. and Goto,J.
  TITLE     Characterization of a novel rat model of X-linked hydrocephalus by
            CRISPR-mediated mutation in L1cam
  JOURNAL   J Neurosurg 132 (3), 945-958 (2019)
   PUBMED   30738385
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1250)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   5  (residues 1 to 1250)
  AUTHORS   White,K.M., Sabatino,J.A., He,M., Davis,N., Tang,N. and Bearer,C.F.
  TITLE     Toluene disruption of the functions of L1 cell adhesion molecule at
            concentrations associated with occupational exposures
  JOURNAL   Pediatr Res 80 (1), 145-150 (2016)
   PUBMED   27027721
  REMARK    GeneRIF: toluene inhibits L1-lipid raft interactions at
            occupationally relevant concentrations and may lead to a fetal
            solvent spectrum disorder similar to fetal alcohol spectrum
            disorder
REFERENCE   6  (residues 1 to 1250)
  AUTHORS   Shults,C.W., Alberti,L., Kimber,T.A. and Stallcup,W.B.
  TITLE     Mesostriatal dopaminergic axons transiently express high levels of
            NILE during development
  JOURNAL   Exp Neurol 116 (3), 275-285 (1992)
   PUBMED   1350253
REFERENCE   7  (residues 1 to 1250)
  AUTHORS   Tocco,M.D., Fujita,K. and Guroff,G.
  TITLE     Effect of dexamethasone on the nerve growth factor-induced increase
            in the NILE glycoprotein in PC12 cells
  JOURNAL   J Neurosci Res 31 (1), 28-32 (1992)
   PUBMED   1377284
REFERENCE   8  (residues 1 to 1250)
  AUTHORS   Miura,M., Kobayashi,M., Asou,H. and Uyemura,K.
  TITLE     Molecular cloning of cDNA encoding the rat neural cell adhesion
            molecule L1. Two L1 isoforms in the cytoplasmic region are produced
            by differential splicing
  JOURNAL   FEBS Lett 289 (1), 91-95 (1991)
   PUBMED   1894011
REFERENCE   9  (residues 1 to 1250)
  AUTHORS   Prince,J.T., Milona,N. and Stallcup,W.B.
  TITLE     Characterization of a partial cDNA clone for the NILE glycoprotein
            and identification of the encoded polypeptide domain
  JOURNAL   J Neurosci 9 (5), 1825-1834 (1989)
   PUBMED   2723751
REFERENCE   10 (residues 1 to 1250)
  AUTHORS   Prince,J.T., Milona,N. and Stallcup,W.B.
  TITLE     Characterization of a partial cDNA clone for the NILE glycoprotein
            and identification of the encoded polypeptide domain
  JOURNAL   J Neurosci 9 (3), 876-883 (1989)
   PUBMED   2466966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 19, 2024 this sequence version replaced XP_017457630.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.38488.1,
                                           SRR26643299.69041.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1250
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..1250
                     /product="neural cell adhesion molecule L1 isoform 2
                     precursor"
                     /note="NILE; nerve-growth factor-inducible large external
                     glycoprotein; NCAM-L1; N-CAM-L1; neuron-glia cell adhesion
                     molecule; neural cell adhesion molecule L1"
                     /calculated_mol_wt=137564
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2239
     Region          30..125
                     /region_name="IgI_L1-CAM_like"
                     /note="Immunoglobulin (Ig)-like domain of the L1 cell
                     adhesion molecule (CAM) and similar proteins; member of
                     the I-set of Ig superfamily (IgSF) domains; cd05733"
                     /db_xref="CDD:409396"
     Region          30..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409396"
     Region          39..43
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409396"
     Region          48..55
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409396"
     Region          61..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409396"
     Region          69..71
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409396"
     Region          78..81
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409396"
     Region          88..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409396"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          104..112
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409396"
     Region          115..125
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409396"
     Region          134..224
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          148..152
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          162..166
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          185..189
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          200..205
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Region          216..219
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          242..324
                     /region_name="Ig3_L1-CAM"
                     /note="Third immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05876"
                     /db_xref="CDD:409460"
     Region          254..258
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409460"
     Region          267..271
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409460"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          289..293
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409460"
     Region          303..308
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409460"
     Region          316..319
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409460"
     Region          328..416
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          344..348
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409453"
     Region          357..361
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409453"
     Region          381..385
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409453"
     Region          395..400
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409453"
     Region          408..411
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409453"
     Region          422..508
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          438..442
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          451..455
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Region          474..478
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Site            484
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          488..493
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Site            499
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          501..504
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          510..606
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          529..533
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409359"
     Region          544..548
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409359"
     Region          548..550
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          557..559
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          568..572
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409359"
     Region          582..587
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409359"
     Region          595..598
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409359"
     Region          606..703
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(606,675,690)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            665
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            order(691..692,694..695)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          692..719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          712..793
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            720
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            771
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          819..901
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            819
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            843
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            870
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            order(897..898,900..901)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(912,979,994)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          915..997
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            963
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            973
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1016
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1024
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1067
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1118..1140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          1141..1226
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Site            1160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32004; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          1219..1250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32004; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     CDS             1..1250
                     /gene="L1cam"
                     /gene_synonym="Hsas; Hyd; N-CAM L1; NCAML1; NgCAM"
                     /coded_by="NM_001431580.1:255..4007"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:50687"
                     /db_xref="RGD:619777"
ORIGIN      
        1 mvmmlwyvlp lllcspclli qipdellepp viteqsprrl vvfptddisl kceargrpqv
       61 efrwtkdgih fkpkeelgvv vheapysgsf tiegnnsfaq rfqgiyrcya snnlgtamsh
      121 eiqlvaegap kwpketvkpv eveegesvvl pcnpppsaap lriywmnski lhikqdervs
      181 mgqngdlyfa nvltsdnhsd yicnahfpgt rtiiqkepid lrvkptnsmi drkprllfpt
      241 nssshlvalq gqslilecia egfptptikw lhpsdpmptd rviyqnhnkt lqllnvgeed
      301 dgeytclaen slgsarhayy vtveaapywl qkpqshlygp getarldcqv qgrpqpevtw
      361 ringmsiekv nkdqkyrieq gslilsnvqp sdtmvtqcea rnqhglllan ayiyvvqlpa
      421 riltkdnqty mavegstayl lckafgapvp svqwldeegt tvlqderffp yangtlgird
      481 lqandtgryf cqaandqnnv tilanlqvke atqitqgprs tiekkgarvt ftcqasfdps
      541 lqasitwrgd grdlqergds dkyfiedgql viqsldysdq gnyscvaste ldevesraql
      601 lvvgspgpvp hlelsdrhll kqsqvhlsws paedhnspie kydiefedke mapekwfslg
      661 kvpgnqtstt lklspyvhyt frvtainkyg sgepspvset vvtpeaapek npvdvrgegn
      721 etnnmvitwk plrwmdwnap qiqyrvqwrp lgkqetwkeq tvsdpflvvs ntstfvpyei
      781 kvqavnnqgk gpepqvtigy sgedypqvsp eleditifns stvlvrwrpv dlaqvkghlr
      841 gynvtywwkg sqrkhskrhv hkshmvvpan ttsailsglr pyssyhvevq afngrglgpa
      901 sewtfstpeg vpghpealhl ecqsdtslll hwqpplshng vltgyllsyh pldgeskeql
      961 ffnlsdpelr thnltnlnpd lqyrfqlqat tqqgpgeaiv reggtmalfg kpdfgnisvt
     1021 agenysvvsw vpregqcnfr fhilfkalpe gkvspdhqpq pqyvsynqss ytqwdlqpdt
     1081 kyeihlmrek vllhhlavkt ngtgpvrvst tgsfasegwf iafvsaiill llillilcfi
     1141 krskggkysv kdkedtqvds earpmkdetf geysdneeka fgssqpslng dikplgsdds
     1201 ladyggsvdv qfnedgsfig qysgkkekea aggndssgat spinpavale
//
LOCUS       NP_001419846             489 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 420 isoform b [Rattus norvegicus].
ACCESSION   NP_001419846 XP_006228811
VERSION     NP_001419846.1
DBSOURCE    REFSEQ: accession NM_001432917.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Beckerman,R. and Prives,C.
  TITLE     Transcriptional regulation by p53
  JOURNAL   Cold Spring Harb Perspect Biol 2 (8), a000935 (2010)
   PUBMED   20679336
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 5, 2024 this sequence version replaced XP_006228811.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2783667.1,
                                           SRR26643429.1538.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..489
                     /product="zinc finger protein 420 isoform b"
                     /note="zinc finger protein 383; Zinc finger protein
                     420-like"
                     /calculated_mol_wt=55894
     Region          27..87
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          186..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          201..223
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          226..251
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <245..489
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(331,333,335,337..338,341..342,345,359,361,365..366,
                     369..370,373,387,389,391,393..394,397..398,401)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          438..458
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          466..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..489
                     /gene="Zfp420"
                     /coded_by="NM_001432917.1:144..1613"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:103690163"
                     /db_xref="RGD:2323829"
ORIGIN      
        1 msalplqryp verggmaadh akhkkqvafs dvsldfsqee waclgpaqra lykdvmleny
       61 shllsvglhi pkpqvislle qgkepwmvgk eltrglcsal esmcesklls lkkevyeles
      121 cqrefmrltk qgldypgfrd vlecgsqlqn ghgsqeplar eymptfvqqt fltlhqiind
      181 ekpyeckkcr kvftqnsqfi qhqrihigek syeckecgkf fscgshvtrh lkihtgekpf
      241 eckdcgkafs cssylsqhqr ihtgkkpyec kdcgkafsyc snlidhqrih tgekpyackv
      301 cgkaftkssq lfqhvrvhtg ekpyeckecg kaftqssklv qhqrihtgek pyeckecgka
      361 fssgsaltnh qrihtgekpy eckdcgkaft qssqlrqhqr ihagekpfec lecgkaftqn
      421 sqlfqhqrvh sdekpyecnk cgkafnkcsn ltrhlrthrd dkpcscnecg ktfsneseli
      481 rhqevhsne
//
LOCUS       NP_001386049            1216 aa            linear   ROD 28-APR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase eta isoform 2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001386049 XP_038960586
VERSION     NP_001386049.1
DBSOURCE    REFSEQ: accession NM_001399120.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Dorofejeva,O. and Barr,A.J.
  TITLE     Defining the molecular basis of interaction between R3
            receptor-type protein tyrosine phosphatases and VE-cadherin
  JOURNAL   PLoS One 12 (9), e0184574 (2017)
   PUBMED   28926625
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Shintani,T., Higashi,S., Takeuchi,Y., Gaudio,E., Trapasso,F.,
            Fusco,A. and Noda,M.
  TITLE     The R3 receptor-like protein tyrosine phosphatase subfamily
            inhibits insulin signalling by dephosphorylating the insulin
            receptor at specific sites
  JOURNAL   J Biochem 158 (3), 235-243 (2015)
   PUBMED   26063811
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Petermann,A., Haase,D., Wetzel,A., Balavenkatraman,K.K., Tenev,T.,
            Guhrs,K.H., Friedrich,S., Nakamura,M., Mawrin,C. and Bohmer,F.D.
  TITLE     Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives
            meningioma cell motility
  JOURNAL   Brain Pathol 21 (4), 405-418 (2011)
   PUBMED   21091576
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Omerovic,J., Clague,M.J. and Prior,I.A.
  TITLE     Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent
            negative regulators of PKB/Akt activation in Ras-mutated cancer
            cells
  JOURNAL   Biochem J 426 (1), 65-72 (2010)
   PUBMED   19922411
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Tarcic,G., Boguslavsky,S.K., Wakim,J., Kiuchi,T., Liu,A.,
            Reinitz,F., Nathanson,D., Takahashi,T., Mischel,P.S., Ng,T. and
            Yarden,Y.
  TITLE     An unbiased screen identifies DEP-1 tumor suppressor as a
            phosphatase controlling EGFR endocytosis
  JOURNAL   Curr Biol 19 (21), 1788-1798 (2009)
   PUBMED   19836242
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Baker,J.E., Majeti,R., Tangye,S.G. and Weiss,A.
  TITLE     Protein tyrosine phosphatase CD148-mediated inhibition of T-cell
            receptor signal transduction is associated with reduced LAT and
            phospholipase Cgamma1 phosphorylation
  JOURNAL   Mol Cell Biol 21 (7), 2393-2403 (2001)
   PUBMED   11259588
REFERENCE   7  (residues 1 to 1216)
  AUTHORS   Kovalenko,M., Denner,K., Sandstrom,J., Persson,C., Gross,S.,
            Jandt,E., Vilella,R., Bohmer,F. and Ostman,A.
  TITLE     Site-selective dephosphorylation of the platelet-derived growth
            factor beta-receptor by the receptor-like protein-tyrosine
            phosphatase DEP-1
  JOURNAL   J Biol Chem 275 (21), 16219-16226 (2000)
   PUBMED   10821867
REFERENCE   8  (residues 1 to 1216)
  AUTHORS   Tangye,S.G., Wu,J., Aversa,G., de Vries,J.E., Lanier,L.L. and
            Phillips,J.H.
  TITLE     Negative regulation of human T cell activation by the receptor-type
            protein tyrosine phosphatase CD148
  JOURNAL   J Immunol 161 (8), 3803-3807 (1998)
   PUBMED   9780142
REFERENCE   9  (residues 1 to 1216)
  AUTHORS   de la Fuente-Garcia,M.A., Nicolas,J.M., Freed,J.H., Palou,E.,
            Thomas,A.P., Vilella,R., Vives,J. and Gaya,A.
  TITLE     CD148 is a membrane protein tyrosine phosphatase present in all
            hematopoietic lineages and is involved in signal transduction on
            lymphocytes
  JOURNAL   Blood 91 (8), 2800-2809 (1998)
   PUBMED   9531590
REFERENCE   10 (residues 1 to 1216)
  AUTHORS   Borges,L.G., Seifert,R.A., Grant,F.J., Hart,C.E., Disteche,C.M.,
            Edelhoff,S., Solca,F.F., Lieberman,M.A., Lindner,V., Fischer,E.H.,
            Lok,S. and Bowen-Pope,D.F.
  TITLE     Cloning and characterization of rat density-enhanced phosphatase-1,
            a protein tyrosine phosphatase expressed by vascular cells
  JOURNAL   Circ Res 79 (3), 570-580 (1996)
   PUBMED   8781490
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 4, 2022 this sequence version replaced XP_038960586.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U40790.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..1216
                     /product="receptor-type tyrosine-protein phosphatase eta
                     isoform 2 precursor"
                     /EC_number="3.1.3.48"
                     /note="density enhanced phosphatase-1; receptor-type
                     tyrosine-protein phosphatase eta"
                     /calculated_mol_wt=130346
     sig_peptide     1..36
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4010
     Region          36..523
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          506..583
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          714..844
                     /region_name="PTP_tm"
                     /note="TM proximal of protein tyrosine phosphatase,
                     receptor type J; pfam18861"
                     /db_xref="CDD:465889"
     Region          948..1176
                     /region_name="R-PTPc-J"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase J; cd14615"
                     /db_xref="CDD:350463"
     CDS             1..1216
                     /gene="Ptprj"
                     /gene_synonym="DEP-1"
                     /coded_by="NM_001399120.1:345..3995"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29645"
                     /db_xref="RGD:3454"
ORIGIN      
        1 mkpaaretrt pprspglrwa llplllllrq gqvvcagaap spvfdveavt sptsvvltwk
       61 hndsatseyk inegntlryt vknqtsfnit glspatsykf sitlgtvnet sgkptyknit
      121 tepwpvsdlq vayigvtqal lawsnangta syrmqivelt tnssggisdl kpgthkslav
      181 qgsnetqhdl wvtegvsdpp sardpsltev lltelkpdtq ykvtiysqaa dgtegqpgnk
      241 vfktnpiqvs diravnisds nmtltwksnn neshasftyk iyvaggsdsi netvnetqav
      301 irglssstly nitvlpflgq tagipgflqv ytsprpvsdf rvtnvslrei glawrsndse
      361 sfeifitqeg sekrwnastg dlsyivenlk pgtsyqfeif prgpngtegp sqtvvgrtdc
      421 savtdirvvs vstteiqlew qntdsasgyt yhlvleseng siktnssqkw itvggltpgt
      481 lynvtifpev dqmegnsssi tqytrpsnvs yievntnttv aaiqwknlda asasysysvl
      541 ilkagdgsnv tsrvrdipsv tipglipgvs yevkiftkir ntevgnevpg qklfcmepaq
      601 vdslhcevvp kepalvlkwa cppgmnsgfe lgvrsdawdn mthlenctld ndtecrtevt
      661 ylnfstsyni siatlscgkm alptqstctt gitdppppdg spnitsvshn svkvkfsgfe
      721 ashgpikaya vllttgeagq pstdvlkyty edfkkgasdt yvtyliriee kgqsqglsea
      781 lnyeidvgnq sttlgyyngr leplgsyrac vagftnityn lqndglingd esyvsfspys
      841 eavslpqdpg vicgavfgci fgalaivavg gfifwrkkrk daknnevsfs qikpkkskli
      901 rvenfeayfk kqqadsncgf aeeyedlkli gislpkyaae iaenrgknry nnvlpydisr
      961 vklsvqthst ddyinanymp gyhskkdfia tqgplpntlk dfwrmvwekn vyaivmltkc
     1021 veqgrtkcee ywpskqaqdy gditvamtse vvlpewtird fvvknmqsse shplrqfhft
     1081 swpdhgvpdt tdllinfryl vrdymkqipp espilvhcsa gvgrtgtfia idrliyqien
     1141 entvdvygiv ydlrmhrplm vqtedqyvfl nqcvldiira qkdskvdliy qnttamtiye
     1201 nlepvsmfgk tngyia
//
LOCUS       NP_001416687             563 aa            linear   ROD 28-APR-2025
DEFINITION  [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1,
            mitochondrial isoform 1 [Rattus norvegicus].
ACCESSION   NP_001416687 XP_006237971
VERSION     NP_001416687.1
DBSOURCE    REFSEQ: accession NM_001429758.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Feng,X., Lu,J., Wu,Y. and Xu,H.
  TITLE     MiR-18a-3p improves cartilage matrix remodeling and inhibits
            inflammation in osteoarthritis by suppressing PDP1
  JOURNAL   J Physiol Sci 72 (1), 3 (2022)
   PUBMED   35148687
  REMARK    GeneRIF: MiR-18a-3p improves cartilage matrix remodeling and
            inhibits inflammation in osteoarthritis by suppressing PDP1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Xing,G., Ren,M., O'Neill,J.T., Sharma,P., Verma,A. and Watson,W.D.
  TITLE     Pyruvate dehydrogenase phosphatase1 mRNA expression is divergently
            and dynamically regulated between rat cerebral cortex, hippocampus
            and thalamus after traumatic brain injury: a potential biomarker of
            TBI-induced hyper- and hypo-glycaemia and neuronal vulnerability
  JOURNAL   Neurosci Lett 525 (2), 140-145 (2012)
   PUBMED   22884618
  REMARK    GeneRIF: divergent alterations of PDP1 mRNA expression were found
            in different brain regions following traumatic brain injury.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Voss,M., Paterson,J., Kelsall,I.R., Martin-Granados,C.,
            Hastie,C.J., Peggie,M.W. and Cohen,P.T.
  TITLE     Ppm1E is an in cellulo AMP-activated protein kinase phosphatase
  JOURNAL   Cell Signal 23 (1), 114-124 (2011)
   PUBMED   20801214
  REMARK    Erratum:[Cell Signal. 2011 May;23(5):947]
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Leblanc,P.J., Mulligan,M., Antolic,A., Macpherson,L., Inglis,J.G.,
            Martin,D., Roy,B.D. and Peters,S.J.
  TITLE     Skeletal muscle type comparison of pyruvate dehydrogenase
            phosphatase activity and isoform expression: effects of obesity and
            endurance training
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 295 (4), R1224-R1230 (2008)
   PUBMED   18716035
  REMARK    GeneRIF: Results suggest that decreased PDP activity in oxidative
            skeletal muscles may play a role in the impairment of carbohydrate
            metabolism in obese rats, which is reversible with endurance
            training.
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Vassylyev,D.G. and Symersky,J.
  TITLE     Crystal structure of pyruvate dehydrogenase phosphatase 1 and its
            functional implications
  JOURNAL   J Mol Biol 370 (3), 417-426 (2007)
   PUBMED   17532339
  REMARK    GeneRIF: Results report the crystal structure of the rat pyruvate
            dehydrogenase phosphatase 1 catalytic subunit at 1.8 A resolution.
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Piccinini,M., Mostert,M., Alberto,G., Ramondetti,C., Novi,R.F.,
            Dalmasso,P. and Rinaudo,M.T.
  TITLE     Down-regulation of pyruvate dehydrogenase phosphatase in obese
            subjects is a defect that signals insulin resistance
  JOURNAL   Obes Res 13 (4), 678-686 (2005)
   PUBMED   15897476
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Wang,M.Y. and Unger,R.H.
  TITLE     Role of PP2C in cardiac lipid accumulation in obese rodents and its
            prevention by troglitazone
  JOURNAL   Am J Physiol Endocrinol Metab 288 (1), E216-E221 (2005)
   PUBMED   15367397
  REMARK    GeneRIF: role of PP2C and AMPK in the derangements of cardiac lipid
            metabolism in obesity
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Karpova,T., Danchuk,S., Huang,B. and Popov,K.M.
  TITLE     Probing a putative active site of the catalytic subunit of pyruvate
            dehydrogenase phosphatase 1 (PDP1c) by site-directed mutagenesis
  JOURNAL   Biochim Biophys Acta 1700 (1), 43-51 (2004)
   PUBMED   15210124
  REMARK    GeneRIF: Asp445 might be involved in the control of interactions
            between PDP1c and the protein substrate pyruvate dehydrogenase
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Huang,B., Wu,P., Popov,K.M. and Harris,R.A.
  TITLE     Starvation and diabetes reduce the amount of pyruvate dehydrogenase
            phosphatase in rat heart and kidney
  JOURNAL   Diabetes 52 (6), 1371-1376 (2003)
   PUBMED   12765946
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Huang,B., Gudi,R., Wu,P., Harris,R.A., Hamilton,J. and Popov,K.M.
  TITLE     Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino
            acid sequences, expression, and regulation
  JOURNAL   J Biol Chem 273 (28), 17680-17688 (1998)
   PUBMED   9651365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Apr 26, 2024 this sequence version replaced XP_006237971.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887620.1776891.1,
                                           SRR26643293.26688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840107 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..563
                     /product="[Pyruvate dehydrogenase
                     [acetyl-transferring]]-phosphatase 1, mitochondrial
                     isoform 1"
                     /EC_number="3.1.3.43"
                     /note="[Pyruvate dehydrogenase
                     [acetyl-transferring]]-phosphatase 1, mitochondrial;
                     pyruvate dehydrogenase phosphatase isoenzyme 1; protein
                     phosphatase 2C, magnesium dependent, catalytic subunit;
                     pyruvate dehyrogenase phosphatase catalytic subunit 1"
                     /calculated_mol_wt=63705
     Region          134..550
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(145,149..150,169..171,443,541)
                     /site_type="active"
                     /db_xref="CDD:238083"
     CDS             1..563
                     /gene="Pdp1"
                     /gene_synonym="PDPC 1; Ppm2c"
                     /coded_by="NM_001429758.1:120..1811"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:54705"
                     /db_xref="RGD:620393"
ORIGIN      
        1 mcvcpgprri gipvrtsslp lfsdampapt qlffplvrnc elsriygtac ychhkhlccs
       61 ppyipqnrlr ytphpayatf crprenwwqy tqgrryastp qkfyltppqv nsilkaneys
      121 fkvpefdgkn vssilgfdsn qlpanapied rrsaatclqt rgmllgvfdg hagcacsqav
      181 serlfyyiav sllphetlle ienavesgra llpilqwhkh pndyfskeas klyfnslrty
      241 wqelidlntg esadidvkea linafkrldn disleaqvgd pnsflnylvl rvafsgatac
      301 vahvdgvdlh vantgdsram lgvqeedgsw savtlsndhn aqnerelerl klehpkneak
      361 svvkqdrllg llmpfrafgd vkfkwsidlq krviesgpdq lndneytkfi ppnyhtppyl
      421 taepevtyhr lrpqdkflvl atdglwetmh rqdvvrivge yltgmhhqqp iavggykvtl
      481 gqmhgllter rakmssvfed qnaathlirh avgnnefgav dherlskmls lpeelarmyr
      541 dditiivvqf nshvvgayqn qeq
//
LOCUS       NP_001418978             787 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 606 isoform a [Rattus norvegicus].
ACCESSION   NP_001418978 XP_038956593
VERSION     NP_001418978.1
DBSOURCE    REFSEQ: accession NM_001432049.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Gebelein,B., Mesa,K. and Urrutia,R.
  TITLE     A novel profile of expressed sequence tags for zinc finger encoding
            genes from the poorly differentiated exocrine pancreatic cell line
            AR4IP
  JOURNAL   Cancer Lett 105 (2), 225-231 (1996)
   PUBMED   8697448
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 25, 2024 this sequence version replaced XP_038956593.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.561545.1,
                                           SRR26360186.2261764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..787
                     /product="zinc finger protein 606 isoform a"
                     /calculated_mol_wt=91053
     Region          57..116
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          386..785
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          399..418
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          426..446
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          454..474
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(459,461,463,465..466,469..470,473,487,489,493..494,
                     497..498,501,515,517,519,521..522,525..526,529)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          482..502
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          510..530
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          538..558
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          566..586
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          594..614
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          622..642
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(627,629,631,633..634,637..638,641,655,657,661..662,
                     665..666,669,683,685,687,689..690,693..694,697)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          650..670
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          678..698
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          706..726
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          734..754
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          762..782
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..787
                     /gene="Zfp606"
                     /gene_synonym="Znf606"
                     /coded_by="NM_001432049.1:190..2553"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:292610"
                     /db_xref="RGD:1309810"
ORIGIN      
        1 maainpwpsw gtlmdqsdps vswalcpqdp awhiegspee srrqadglqt aqdqepvtfk
       61 dvavaftqee weqldlvqrt lyrdvmlety ghllsvgnqi akpevislle qeepwsleqg
      121 ypksscpewm rnveskalip aqsvfeeeqs sngmvleryi wdnpwlsrlg vlgygdqiem
      181 yhmnqnagmr emvfmqkqvl sqrgsefckl gteysqslnl ippqrvsqle hfyksdthle
      241 twrcnsaimy adkvtcenid yekafcqsvq pvypaklqtr dnmfkctdav ksfnhiiqfg
      301 dhkavhtgek lygykeyhqi fnqspslieh prfqiggnqy ekykeygnif yfssfmehqn
      361 iggvekayky newekvfgyd sllaqhtsty taekpyefnk cgtsfiwssy liqhkkthpg
      421 dkpyecdkcr kvfrnrsalt kherthtgik pyecnkcgka fswnshlivh trihtgekpy
      481 vcnecgksfn wnshlighqr thtgekpfec tecgksfsws shliahmrmh tgekpfkcde
      541 cekafrdysa lskherthsg akpykctecg ksfswsshli ahqrthtgek pyncqecgka
      601 frersaltkh eiihsgikpy ecnkcgkscs qmahlvrhqr thtgekpyec nkcgksfsqs
      661 chlvahrrih tgekpykcnq cersfncssh liahrrthtg ekpyrcnecg kafnesssli
      721 vhlrnhtgek pykcihceka fcknssliih qrmhsgekrf icnqcgrafs ghsallqhqk
      781 nhseekl
//
LOCUS       NP_001399481             495 aa            linear   ROD 28-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 3
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001399481 XP_006237357
VERSION     NP_001399481.1
DBSOURCE    REFSEQ: accession NM_001412552.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Dakic,T., Lakic,I., Zec,M., Takic,M., Stojiljkovic,M. and
            Jevdjovic,T.
  TITLE     Fructose-rich diet and walnut supplementation differently regulate
            rat hypothalamic and hippocampal glucose transporters expression
  JOURNAL   J Sci Food Agric 101 (14), 5984-5991 (2021)
   PUBMED   33856052
  REMARK    GeneRIF: Fructose-rich diet and walnut supplementation differently
            regulate rat hypothalamic and hippocampal glucose transporters
            expression.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   von Leden,R.E., Moritz,K.E., Bermudez,S., Jaiswal,S., Wilson,C.M.,
            Dardzinski,B.J. and Byrnes,K.R.
  TITLE     Aging alters glucose uptake in the naive and injured rodent spinal
            cord
  JOURNAL   Neurosci Lett 690, 23-28 (2019)
   PUBMED   30296507
  REMARK    GeneRIF: findings show that age alters glucose uptake and GLUT3/4
            expression profiles before and after Spinal Cord Injury.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Solis-Maldonado,M., Miro,M.P., Acuna,A.I., Covarrubias-Pinto,A.,
            Loaiza,A., Mayorga,G., Beltran,F.A., Cepeda,C., Levine,M.S.,
            Concha,I.I., Batiz,L.F., Carrasco,M.A. and Castro,M.A.
  TITLE     Altered lactate metabolism in Huntington's disease is dependent on
            GLUT3 expression
  JOURNAL   CNS Neurosci Ther 24 (4), 343-352 (2018)
   PUBMED   29582588
  REMARK    GeneRIF: Study found no differences in mRNA or protein levels of
            neuronal monocarboxylate transporters (MCTs). Functional analyses
            revealed that neuronal MCT2 had high catalytic efficiency in
            Huntington's disease (HD) cells. Ascorbic acid did not stimulate
            lactate uptake in HD cells; and was unable to inhibit glucose
            transport in HD cells because they exhibit decreased expression of
            the neuronal glucose transporter GLUT3.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Pearson-Leary,J. and McNay,E.C.
  TITLE     Novel Roles for the Insulin-Regulated Glucose Transporter-4 in
            Hippocampally Dependent Memory
  JOURNAL   J Neurosci 36 (47), 11851-11864 (2016)
   PUBMED   27881773
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Deng,D., Sun,P., Yan,C., Ke,M., Jiang,X., Xiong,L., Ren,W.,
            Hirata,K., Yamamoto,M., Fan,S. and Yan,N.
  TITLE     Molecular basis of ligand recognition and transport by glucose
            transporters
  JOURNAL   Nature 526 (7573), 391-396 (2015)
   PUBMED   26176916
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Campbell,I.W., Dominiczak,A.F., Livingstone,C. and Gould,G.W.
  TITLE     Analysis of the glucose transporter compliment of metabolically
            important tissues from the Milan hypertensive rat
  JOURNAL   Biochem Biophys Res Commun 211 (3), 780-791 (1995)
   PUBMED   7598707
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Krishnan,S.N. and Haddad,G.G.
  TITLE     Cloning of glucose transporter-3 (GLUT3) cDNA from rat brain
  JOURNAL   Life Sci 56 (14), 1193-1197 (1995)
   PUBMED   7475896
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Simpson,I.A., Chundu,K.R., Davies-Hill,T., Honer,W.G. and Davies,P.
  TITLE     Decreased concentrations of GLUT1 and GLUT3 glucose transporters in
            the brains of patients with Alzheimer's disease
  JOURNAL   Ann Neurol 35 (5), 546-551 (1994)
   PUBMED   8179300
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Nagamatsu,S., Sawa,H., Kamada,K., Nakamichi,Y., Yoshimoto,K. and
            Hoshino,T.
  TITLE     Neuron-specific glucose transporter (NSGT): CNS distribution of
            GLUT3 rat glucose transporter (RGT3) in rat central neurons
  JOURNAL   FEBS Lett 334 (3), 289-295 (1993)
   PUBMED   8243635
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Colville,C.A., Seatter,M.J., Jess,T.J., Gould,G.W. and Thomas,H.M.
  TITLE     Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3)
            glucose transporters in Xenopus oocytes: substrate specificities
            and effects of transport inhibitors
  JOURNAL   Biochem J 290 (Pt 3) (Pt 3), 701-706 (1993)
   PUBMED   8457197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 5, 2022 this sequence version replaced XP_006237357.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.1820582.1,
                                           SRR26360181.3318918.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..495
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 3 isoform 2"
                     /note="GLUT-3; glucose transporter type 3, brain; solute
                     carrier family 2, facilitated glucose transporter member
                     3-like; solute carrier family 2 (facilitated glucose
                     transporter), member 3; solute carrier family 2, member 2;
                     Solute carrier family 2 A3 (neuron glucose transporter)"
                     /calculated_mol_wt=53775
     Region          14..458
                     /region_name="MFS_GLUT_Class1"
                     /note="Class 1 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17431"
                     /db_xref="CDD:340989"
     Site            order(26,30,161,164..165,168,282..283,287..288,291,317,
                     379..380,384,388,411,415)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340989"
     CDS             1..495
                     /gene="Slc2a3"
                     /gene_synonym="GLUT3"
                     /coded_by="NM_001412552.1:206..1693"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25551"
                     /db_xref="RGD:3706"
ORIGIN      
        1 mesnkqnvtp slvfavtvat igsfqfgynt gvinapetii kdflnytlee rledlpsegl
       61 lttlwslcva ifsvggmigs fsvglfvnrf grrnsmllvn liailggclm gfakiaesve
      121 mlilgrliig ifcglctgfv pmyigevspt alrgafgtln qlgivvgilv aqvfgldfil
      181 gseelwpgll gltiipailq saalpfcpes prfllinrke edqateilqr lwgtpdviqe
      241 iqemkdesir msqekqvtvl elfkspsyfq pllisvvlql sqqfsginav fyystgifqd
      301 agvqepiyat igagvvntif tvvslflver agrrtlhmig lggmavcsvf mtislllkde
      361 yeamsfvciv ailvyvaffe igpgpipwfi vaelfsqgpr paamavagcs nwtsnflvgm
      421 ffpsaaaylg ayvfiifaaf lvffliftff kvpetkgrtf editrafegq aqsgkgsagv
      481 elnsmqpvke tpgna
//
LOCUS       NP_001101997             313 aa            linear   ROD 28-APR-2025
DEFINITION  sideroflexin-4 [Rattus norvegicus].
ACCESSION   NP_001101997 XP_001073930 XP_342073
VERSION     NP_001101997.1
DBSOURCE    REFSEQ: accession NM_001108527.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Kory,N., Wyant,G.A., Prakash,G., Uit de Bos,J., Bottanelli,F.,
            Pacold,M.E., Chan,S.H., Lewis,C.A., Wang,T., Keys,H.R., Guo,Y.E.
            and Sabatini,D.M.
  TITLE     SFXN1 is a mitochondrial serine transporter required for one-carbon
            metabolism
  JOURNAL   Science 362 (6416) (2018)
   PUBMED   30442778
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_342073.2, XP_001073930.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215895.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..313
                     /product="sideroflexin-4"
                     /note="solute carrier family 64 member 4"
                     /calculated_mol_wt=35614
     Region          2..312
                     /region_name="SFXNs"
                     /note="Sideroflexins; cl04275"
                     /db_xref="CDD:470990"
     CDS             1..313
                     /gene="Sfxn4"
                     /gene_synonym="SLC64A4"
                     /coded_by="NM_001108527.1:99..1040"
                     /db_xref="GeneID:361778"
                     /db_xref="RGD:1306088"
ORIGIN      
        1 mepnlhfwis erqsffrrfc qwmdlldpvn vfisvesiek srqllftted apkhyldnqr
       61 vkdawnksls tvhpdsskli phlfrpaafl pvtapmvllm mmpdtgiksi iltqgclygy
      121 ttafnitngn asyshgpver tllgagvfas stffgsiphl fqlkyplnnl wlkrflpiif
      181 laqisgmnvf asrsfenhrg ievmdkeghv igysrkagrk aiketaksra vlfgtsalap
      241 elfihifkrt rfypqtllas vilrmsstlf mmglmvpvsf smfpqigqiq csqleemirs
      301 steekelfyy rgv
//
LOCUS       NP_001424112             797 aa            linear   ROD 28-APR-2025
DEFINITION  alpha-adducin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424112 XP_017454553
VERSION     NP_001424112.1
DBSOURCE    REFSEQ: accession NM_001437183.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_017454553.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.54864.1,
                                           SRR26360194.975320.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..797
                     /product="alpha-adducin isoform 2"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=86982
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Region          619..>768
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     CDS             1..797
                     /gene="Add1"
                     /coded_by="NM_001437183.1:181..2574"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kvwtnithdh
      481 vkpllqslss gvcvpscitn clwtkedghr tstsavpnlf vplntnpkev qemrnkireq
      541 nlqdiktagp qsqvlcgvmm drslvqdapl sdctetiegl erteqtfspa ksvsfrkgel
      601 vtaskaiiek eyqphvivst tgpnpfntlt dreleeyrre verkqkgsee nldetreqke
      661 ksppdqsavp ntppstpvkl egglpqepts rdgsdattsk ptppdlspde psealafptv
      721 aeeahaspdt tqplaeadpe pasasapgae evaspateeg spmdpgsdgs pgkspskkkk
      781 kfrtpsflkk skkksds
//
LOCUS       NP_001420284             484 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 385B isoform b [Rattus norvegicus].
ACCESSION   NP_001420284 XP_017447191
VERSION     NP_001420284.1
DBSOURCE    REFSEQ: accession NM_001433355.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Iijima,K., Yamada,H., Miharu,M., Imadome,K., Miyagawa,Y.,
            Akimoto,S., Kobayashi,K., Okita,H., Nakazawa,A., Fujiwara,S.,
            Fujimoto,J. and Kiyokawa,N.
  TITLE     ZNF385B is characteristically expressed in germinal center B cells
            and involved in B-cell apoptosis
  JOURNAL   Eur J Immunol 42 (12), 3405-3415 (2012)
   PUBMED   22945289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Aug 9, 2024 this sequence version replaced XP_017447191.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.16565.1,
                                           SRR26643293.17290.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..484
                     /product="zinc finger protein 385B isoform b"
                     /note="zinc finger protein 533"
                     /calculated_mol_wt=51322
     Region          35..65
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          36..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          173..195
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          173..195
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          299..323
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          301..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(308..310,312..313,317,362,369,372..376,378..379)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          362..386
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          364..386
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..484
                     /gene="Zfp385b"
                     /gene_synonym="Zfp533"
                     /coded_by="NM_001433355.1:445..1899"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:311137"
                     /db_xref="RGD:1311181"
ORIGIN      
        1 mnmasflrgf eekglkndrp gdqfskekkk ilfsfcdvcn iqlnsaaqaq vhydgkshrk
       61 rvkqlsdgqp pppaqgsvpl laspcpgpgp gpgtntstgs achtttlpal vrtptlmmqp
      121 sldikpfmsf pvdsssavgl fpnfntmdpv qkavinhtfg vsippkkkqv iscnvcqlrf
      181 nsdsqaeahy tgskhakkvk aleatknkpk mvpskdsaka npscsvrpgt gdssdksedk
      241 gkikatsssq psgseggsff lksgttpltl gaiaspskst ngapgsvaes eeekakklly
      301 cslckvavns lsqleahntg skhktmvear ngagpiksyp rpgsrlkvqn gskgsglqnk
      361 tfhceicdvh vnseiqlkqh issrrhkdrv agkplkpkys pynklqrsps ilaaklafqk
      421 dlmkplaptf lssplaaaav stalslpprp saslfqaaai ppallrpghg piratptsil
      481 fapy
//
LOCUS       NP_001382021             977 aa            linear   ROD 28-APR-2025
DEFINITION  AP-2 complex subunit alpha-1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001382021 XP_006229126
VERSION     NP_001382021.1
DBSOURCE    REFSEQ: accession NM_001395092.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Capella,P., Asensio,J., Troncoso,M., Sosa,M.A. and Seltzer,A.M.
  TITLE     Evidence on differential role for alpha 1 and alpha 2 subtypes of
            AP-2 adaptin in the central nervous system
  JOURNAL   Neurosci Lett 808, 137282 (2023)
   PUBMED   37127089
  REMARK    GeneRIF: Evidence on differential role for alpha 1 and alpha 2
            subtypes of AP-2 adaptin in the central nervous system.
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Taoufiq,Z., Ninov,M., Villar-Briones,A., Wang,H.Y., Sasaki,T.,
            Roy,M.C., Beauchain,F., Mori,Y., Yoshida,T., Takamori,S., Jahn,R.
            and Takahashi,T.
  TITLE     Hidden proteome of synaptic vesicles in the mammalian brain
  JOURNAL   Proc Natl Acad Sci U S A 117 (52), 33586-33596 (2020)
   PUBMED   33376223
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Moulakakis,C., Steinhauser,C., Biedziak,D., Freundt,K., Reiling,N.
            and Stamme,C.
  TITLE     Surfactant Protein A Enhances Constitutive Immune Functions of
            Clathrin Heavy Chain and Clathrin Adaptor Protein 2
  JOURNAL   Am J Respir Cell Mol Biol 55 (1), 92-104 (2016)
   PUBMED   26771574
  REMARK    GeneRIF: SP-A transiently enhances the basal protein expression of
            CHC and alpha-adaptin.
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Zhao,Z., Sagare,A.P., Ma,Q., Halliday,M.R., Kong,P., Kisler,K.,
            Winkler,E.A., Ramanathan,A., Kanekiyo,T., Bu,G., Owens,N.C.,
            Rege,S.V., Si,G., Ahuja,A., Zhu,D., Miller,C.A., Schneider,J.A.,
            Maeda,M., Maeda,T., Sugawara,T., Ichida,J.K. and Zlokovic,B.V.
  TITLE     Central role for PICALM in amyloid-beta blood-brain barrier
            transcytosis and clearance
  JOURNAL   Nat Neurosci 18 (7), 978-987 (2015)
   PUBMED   26005850
  REMARK    Erratum:[Nat Neurosci. 2024 Jan;27(1):208. doi:
            10.1038/s41593-023-01509-y. PMID: 37985802]
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Onishi,K., Shafer,B., Lo,C., Tissir,F., Goffinet,A.M. and Zou,Y.
  TITLE     Antagonistic functions of Dishevelleds regulate Frizzled3
            endocytosis via filopodia tips in Wnt-mediated growth cone guidance
  JOURNAL   J Neurosci 33 (49), 19071-19085 (2013)
   PUBMED   24305805
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Di Paolo,G., Sankaranarayanan,S., Wenk,M.R., Daniell,L.,
            Perucco,E., Caldarone,B.J., Flavell,R., Picciotto,M.R., Ryan,T.A.,
            Cremona,O. and De Camilli,P.
  TITLE     Decreased synaptic vesicle recycling efficiency and cognitive
            deficits in amphiphysin 1 knockout mice
  JOURNAL   Neuron 33 (5), 789-804 (2002)
   PUBMED   11879655
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Kamiguchi,H. and Yoshihara,F.
  TITLE     The role of endocytic l1 trafficking in polarized adhesion and
            migration of nerve growth cones
  JOURNAL   J Neurosci 21 (23), 9194-9203 (2001)
   PUBMED   11717353
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Chen,H., Slepnev,V.I., Di Fiore,P.P. and De Camilli,P.
  TITLE     The interaction of epsin and Eps15 with the clathrin adaptor AP-2
            is inhibited by mitotic phosphorylation and enhanced by
            stimulation-dependent dephosphorylation in nerve terminals
  JOURNAL   J Biol Chem 274 (6), 3257-3260 (1999)
   PUBMED   9920862
REFERENCE   10 (residues 1 to 977)
  AUTHORS   Slepnev,V.I., Ochoa,G.C., Butler,M.H., Grabs,D. and De Camilli,P.
  TITLE     Role of phosphorylation in regulation of the assembly of endocytic
            coat complexes
  JOURNAL   Science 281 (5378), 821-824 (1998)
   PUBMED   9694653
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jun 3, 2021 this sequence version replaced XP_006229126.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMN12840115, SAMN16676788
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..977
                     /product="AP-2 complex subunit alpha-1 isoform 1"
                     /note="AP-2 complex subunit alpha-1; adaptor protein
                     complex AP-2, alpha 1 subunit; alpha-adaptin A;
                     adaptor-related protein complex 2, alpha 1 subunit"
                     /calculated_mol_wt=107535
     Region          29..591
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          755..858
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     Region          864..972
                     /region_name="Alpha_adaptin_C"
                     /note="Alpha adaptin AP2, C-terminal domain; pfam02296"
                     /db_xref="CDD:426707"
     CDS             1..977
                     /gene="Ap2a1"
                     /coded_by="NM_001395092.1:114..3047"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308578"
                     /db_xref="RGD:1306254"
ORIGIN      
        1 mpavskgdgm rglavfisdi rnckskeaei krinkelani rskfkgdkal dgyskkkyvc
       61 kllfifllgh didfghmeav nllssnkyte kqigylfisv lvnsnselir linnaikndl
      121 asrnptfmcl alhcianvgs remgeafaad iprilvagds mdsvkqsaal cllrlykasp
      181 dlvpmgewta rvvhllndqh mgvvtaavsl itclckknpd dfktcvslav srlsrivssa
      241 stdlqdytyy fvpapwlsvk llrllqcypp pedaavkgrl vecletvlnk aqeppkskkv
      301 qhsnaknail fetisliihy dsepnllvra cnqlgqflqh retnlrylal esmctlasse
      361 fsheavkthi dtvinalkte rdvsvrqraa dllyamcdrs nakqivseml ryletadyai
      421 reeivlkvai laekyavdys wyvdtilnli riagdyvsee vwyrvlqivt nrddvqgyaa
      481 ktvfealqap achenmvkvg gyilgefgnl iagdprsspp vqfsllhskf hlcsvatral
      541 llstyikfin lfpetkatiq gvlragsqlr nadvelqqra veyltlssva stdvlatvle
      601 emppfperes silaklkrkk gpgaasaldd srrdtssndi nggveptpsn vstpspsadl
      661 lglraapppa appapvggnl lvdvfsdgpt aqpslgptpe eaflselepp apespmtlla
      721 dpapaadpgp edigppipea dellnkfvck nsgvlfenql lqigvksefr qnlgrmylfy
      781 gnktsvqfqs flptvvhpgd lqtqlavqtk rvaaqvdgga qvqqvlniec lrdfltppll
      841 svrfryggta qsltlklpvt inkffqptem aaqdffqrwk qlslplqeaq kifkanhpmd
      901 aevtkakllg fgsalldnvd pnpenfvgag iiqtkalqvg cllrlepnaq aqmyrltlrt
      961 skepvsrhlc ellaqqf
//
LOCUS       NP_001425065             555 aa            linear   ROD 28-APR-2025
DEFINITION  tubby-related protein 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001425065 XP_063122823
VERSION     NP_001425065.1
DBSOURCE    REFSEQ: accession NM_001438136.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122823.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3148.1,
                                           SRR26360181.3178544.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..555
                     /product="tubby-related protein 2 isoform 3"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=62191
     Region          39..>212
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          308..550
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..555
                     /gene="Tulp2"
                     /coded_by="NM_001438136.1:16..1683"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mdregprgpr rgtsqeneqw kketledefs gvrlqkleqq rqlfekkqrr krqeplmvqa
       61 npdaslrhrr prrgeerfqs dsswglgvgs pflqenvpqa hlpsgahsal vtmsyvgdgs
      121 gerapllspr gavytrgngp avrhlcwlpd ssdsdveevt medipvisrp pkthlanrrr
      181 gwlaspgpgi seeeevepkd arvedktpsp dpdptensdr vhgdsascnm eentakknie
      241 tasgigdedp ekkeateste tnnalvaskv lqgdgdtsnh sawnmtcpmp rtpgprlged
      301 meayvllpap rehmvqcriv rnkhgvdkgm fpsyylylea edgvahflla grkrkrskts
      361 nylisldpkd msrngnnfvg kvrsnvlgtk ftifdngvnp ernywipdsa rireelgvvc
      421 yetnvlgfrg prkmtvilpg mdsrkqrmkv qpqndqdsil srvqkgarhg llllqnkaps
      481 wsdesgayvl nfhgrvtras vknfqivhpd epdhlvlqfg rvapniftmd fryplcplqa
      541 faiclssfdg klaff
//
LOCUS       NP_001382634            1206 aa            linear   ROD 28-APR-2025
DEFINITION  PAN2-PAN3 deadenylation complex catalytic subunit Pan2 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001382634 NP_001008862 XP_006240846
VERSION     NP_001382634.1
DBSOURCE    REFSEQ: accession NM_001395705.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1206)
  AUTHORS   Wahle,E. and Winkler,G.S.
  TITLE     RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3
            complexes
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 561-570 (2013)
   PUBMED   23337855
REFERENCE   2  (residues 1 to 1206)
  AUTHORS   Zheng,D., Ezzeddine,N., Chen,C.Y., Zhu,W., He,X. and Shyu,A.B.
  TITLE     Deadenylation is prerequisite for P-body formation and mRNA decay
            in mammalian cells
  JOURNAL   J Cell Biol 182 (1), 89-101 (2008)
   PUBMED   18625844
REFERENCE   3  (residues 1 to 1206)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   4  (residues 1 to 1206)
  AUTHORS   Uchida,N., Hoshino,S. and Katada,T.
  TITLE     Identification of a human cytoplasmic poly(A) nuclease complex
            stimulated by poly(A)-binding protein
  JOURNAL   J Biol Chem 279 (2), 1383-1391 (2004)
   PUBMED   14583602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Jul 30, 2021 this sequence version replaced
            NP_001008862.1, XP_006240846.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1206
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..1206
                     /product="PAN2-PAN3 deadenylation complex catalytic
                     subunit Pan2 isoform 1"
                     /EC_number="3.1.13.4"
                     /note="PAB-dependent poly(A)-specific ribonuclease subunit
                     2; ubiquitin specific peptidase 52; ubiquitin specific
                     protease 52; PAN2 polyA specific ribonuclease subunit
                     homolog; PAN deadenylation complex subunit 2; PAN2 poly(A)
                     specific ribonuclease subunit; PAB1P-dependent
                     poly(A)-specific ribonuclease; poly(A)-nuclease
                     deadenylation complex subunit 2; PAN2-PAN3 deadenylation
                     complex catalytic subunit Pan2; inactive ubiquitin
                     carboxyl-terminal hydrolase 52; PAB-dependent
                     poly(A)-specific ribonuclease subunit PAN2;
                     PAB1P-dependent poly(A)-nuclease; PAN deadenylation
                     complex catalytic subunit 2"
                     /calculated_mol_wt=135616
     Region          75..357
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(90,94,99,114..115,142,148..149,153..154,171,176,182,
                     195,210,215,221..222,234..235,251,264,270..271,283..284,
                     303,319,325,347,351,357)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          153..193
                     /region_name="WD 1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          195..231
                     /region_name="WD 2.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          244..280
                     /region_name="WD 3.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          328..367
                     /region_name="WD 4.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          368..484
                     /region_name="Linker.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          516..902
                     /region_name="UCH_1"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam13423"
                     /db_xref="CDD:463872"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q504Q3; propagated from
                     UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          979..1152
                     /region_name="PAN2_exo"
                     /note="DEDDh 3'-5' exonuclease domain of the eukaryotic
                     exoribonuclease PAN2; cd06143"
                     /db_xref="CDD:99846"
     Site            order(982..985,987,1043,1047,1086..1087,1089..1091,1138,
                     1143)
                     /site_type="active"
                     /db_xref="CDD:99846"
     Site            order(982..985,987,1043,1047,1086..1087,1089..1090,1138,
                     1143)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99846"
     Site            order(982,984,1091,1138,1143)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99846"
     Site            1193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q504Q3; propagated from
                     UniProtKB/Swiss-Prot (Q6IE70.1)"
     CDS             1..1206
                     /gene="Pan2"
                     /gene_synonym="Usp52"
                     /coded_by="NM_001395705.1:256..3876"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:408200"
                     /db_xref="RGD:1303301"
ORIGIN      
        1 mnfegldpgl aefspamhst ldpvldahln psllqnveld pegvalealp vqesvhimeg
       61 vyselhsvva evgvpvsvsh fdlqeemlwv gshgghatsf fgpaleryss fqvngsddir
      121 qiqslengil fltknnlkym arggliifdy lldesedmhs llladnntll vgglqnhvle
      181 idlntvqetq kyavetpgvt imrqtnrfff cghtsgkvsl rdlrsfkveh efdafsgsls
      241 dfdvhgnlla acgfssrltg lacdrflkvy dlrmmraitp lqvhvdpafl rfiptytsrl
      301 aiisqsgqcq fceptglanp adifhvnpvg pllmtfdvsa skqalafgds egcvhlwtds
      361 pepsfnpysr etefalpclv dslpaldwsq dllplslipv plttdallsd wpaansapap
      421 rrappvdaei lrtmkkvgfi gyapnprtrl rnqipyrlke sdhefdnfsq vtesptgree
      481 eplhtvskky rkvtikyskl gledfdfkhy nktlfaglep hipnaycncm iqvlyflepv
      541 rcliqnhlcq kefclacelg flfhmldlsr gdpcqgsnfl rafrtipeas algliladsd
      601 easgkgslar liqrwnrfil tqlhqdmqel evpqayrgag gsfcssgdsi igqlfsceme
      661 ncslcrcgse tvrasstllf tlsypegsic dktgknydfa qvlkrsicle qntqawcdsc
      721 ekyqptiqtr nirhlpdilv incevnsske adfwrlqaev afkiavkkfg gevkskefal
      781 adrkelrspe gflccssmee lknvwlpfsi rmkmtknkgl dvcnwadehe lsslgtpsqw
      841 gparaeeehg vyvydlmatv vhildsrtgg slvahikvge tyhqrkegvt hqqwylfndf
      901 liepidkyea vqfdmnwkvp ailyyvkrnl nsrynlnikn pieasvllae aslarkqrkt
      961 httfiplmln empqvgdlvg ldaefvtlne eeaelrsdgt kstikpsqms varitcvrgq
     1021 gpnegipfid dyistqeqvv dyltqysgik pgdldakiss khlttlksty lklrflidig
     1081 vkfvghglqk dfrvinlmvp kdqvldtvyl fhmprkrmis lrflawyfld lkiqgethds
     1141 iedartalql yrkylelskn gaepesfhkv lkglyekgrk mdwkvpepes qsspknaavf
     1201 psvlal
//
LOCUS       NP_001418099            1839 aa            linear   ROD 28-APR-2025
DEFINITION  Ecm29 proteasome adaptor and scaffold isoform c [Rattus
            norvegicus].
ACCESSION   NP_001418099 XP_056841528
VERSION     NP_001418099.1
DBSOURCE    REFSEQ: accession NM_001431170.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1839)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   2  (residues 1 to 1839)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 1839)
  AUTHORS   Gorbea,C., Goellner,G.M., Teter,K., Holmes,R.K. and Rechsteiner,M.
  TITLE     Characterization of mammalian Ecm29, a 26 S proteasome-associated
            protein that localizes to the nucleus and membrane vesicles
  JOURNAL   J Biol Chem 279 (52), 54849-54861 (2004)
   PUBMED   15496406
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 9, 2024 this sequence version replaced XP_056841528.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.19417.1,
                                           SRR26643295.21441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1839
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..1839
                     /product="Ecm29 proteasome adaptor and scaffold isoform c"
                     /note="proteasome adapter and scaffold protein ECM29"
                     /calculated_mol_wt=203790
     Region          10..516
                     /region_name="Ecm29"
                     /note="Proteasome stabilizer; pfam13001"
                     /db_xref="CDD:463769"
     Region          390..422
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          434..460
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          469..500
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          509..535
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1078..1101
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(1093..1094,1097,1100..1101,1134,1137,1140..1141,
                     1146,1174..1175,1178,1181..1182,1185,1216..1217,1220,
                     1223..1224,1266..1267,1270,1273..1274)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          1113..1146
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1156..1186
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1195..1224
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1245..1275
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1392..1421
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1839
                     /gene="Ecpas"
                     /gene_synonym="RGD1306148"
                     /coded_by="NM_001431170.1:354..5873"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:313196"
                     /db_xref="RGD:1306148"
ORIGIN      
        1 myhidcrdql ervflrlgha etdeqlqnii skflppvllk lsstqegvrk kvmellvhln
       61 kriksrpkiq lpvetllvqy qdpaavsfvt nftiiyvkmg yprlpvekqc elaptlltam
      121 egkpqpqqds lmhlliptlf hmkypaessk saspfnlaek pktvqllldf mldvllmpyg
      181 yvlnesqsrq nssssqgsss nsggssgipq pppgmsfyaa krvigdnpwt peqleqcklg
      241 ivkfieaeqv peleavlhlv iassdtrhsv ataadlelks kqslidwnnp aiinkmykvy
      301 lgdiplktke gavlkpelkr dpvstrvklk ivphllrsrq aaetfpaniq vvydglfgtn
      361 tnsklrtlsl qfvhhicitc peikikplgp mllngltkli neykedpkll smaysavgkl
      421 ssrmphlftk dialvqqlfe alckeepetr laiqealsmm vgaystlega qrtlmealva
      481 sylikpevqv rqvavkfast vfpsdhipsr yllllaagdp reevhgeaqr vlrclpgrnk
      541 kesaskqmps fpemvyyiqe kashrmktpv kymtgttvlp fnpaafgeiv lylrmclahs
      601 agvvptsqsl admqdhapai gryirtlmss sqatasscnk sgetnpvqiy igllqqllag
      661 vgglpvmycl leavsvypek latkfvdkte wikslmsssk eemrelaalf ysvvvstvsg
      721 kelksmveql ikatkdnhsp evqhgsllal gftvgrylak krvrmaeqhd letdddllpe
      781 qeevirsate tigsfldsts pllaiaacta lgeigrngpl pipsegsgft klhlveslln
      841 ripssketnk mkeraiqtlg yfpvgdgdfp hqklllqglm dsveakqiel qftigeaits
      901 aaigtssvaa rdawlvteee yippagakvn dvvpwvldvi lnkhiispnp hvrqaaciwl
      961 lslvrklsth vevkshlkei qsafvsvlse ndelsqdvas kglglvydlg seqdqqelvs
     1021 tlvdtlrtgk rvkhevsget vvfqggglgk tpdgqglsty kelcslasdl sqpdlvykfm
     1081 nlanhhamwn srkgaafgfn viatrageql apflpqlvpr lyryqfdpnl girqamtsiw
     1141 nalvtdksmv dkylkeilqd liknltsnmw rvressclal ndllrgrpld dvidklpemw
     1201 etlfrvqddi kesvrkaael alktlskvcv kmcdpakgaa gqrtiavllp clldkgmmsp
     1261 vtevralsin tlvkisksag amlkphapkl ipalleslsv lepqvlnyls lrateqekda
     1321 mdsarlsaak sspmmetinm clqyldvsvl gelvprlcel irsgvglgtk ggcasvivsl
     1381 ttqcpqdltp ysgklmsall sgltdrnsvi qkscafamgh lvrtsrdsst ekllqkltaw
     1441 ymekeepiyk tscaltihai gryspdvlkn hakevlplaf lgmheiadee ksekeecnmw
     1501 tevwqenvpg sfggirlylq elititqkal qsqswkmkaq gaiamasiak qtsslvppyl
     1561 gmilsalvqg lagrtwagke ellkaiacvv tassteleks vpnqpttnei lqavlkecck
     1621 enlkykivai scaadvlkat kedrfqefsd ivmplikkns lesmgvrttk aedenekere
     1681 lqlesllgaf eslgkawprn pdtqrcyrqe mcklmcerlr lstwkvqlgv lqsmnaffqg
     1741 lmlleeehad pealaeille tcqsitysle nktyssvrte alsvielllk kleegkqwes
     1801 ltaecrrlli eslatmetdn rpelqekasv lkktlesle
//
LOCUS       NP_001102377             173 aa            linear   ROD 28-APR-2025
DEFINITION  calcium-binding protein 5 [Rattus norvegicus].
ACCESSION   NP_001102377 XP_001061080 XP_344864
VERSION     NP_001102377.1
DBSOURCE    REFSEQ: accession NM_001108907.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   McCue,H.V., Burgoyne,R.D. and Haynes,L.P.
  TITLE     Membrane targeting of the EF-hand containing calcium-sensing
            proteins CaBP7 and CaBP8
  JOURNAL   Biochem Biophys Res Commun 380 (4), 825-831 (2009)
   PUBMED   19338761
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474105.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_344864.2, XP_001061080.1.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..173
                     /product="calcium-binding protein 5"
                     /calculated_mol_wt=19626
     Region          25..171
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..173
                     /gene="Cabp5"
                     /coded_by="NM_001108907.1:188..709"
                     /db_xref="GeneID:365194"
                     /db_xref="RGD:1308108"
ORIGIN      
        1 mqfpmgpaci flrkgiaekq rerplgqdei delreaflef dkdrdgfisy kdlgnlmrtm
       61 gymptemelt elgqqirmnl ggrvdfedfv elmtpkllae tagmigvqem rdafkefdan
      121 gdgeitlael qqamqrllge kltpreiaev vqeadingdg tvdfeefvkm msr
//
LOCUS       NP_001418890            1274 aa            linear   ROD 28-APR-2025
DEFINITION  DENN domain containing 5B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001418890 XP_038964852
VERSION     NP_001418890.1
DBSOURCE    REFSEQ: accession NM_001431961.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1274)
  AUTHORS   Gordon,S.M., Neufeld,E.B., Yang,Z., Pryor,M., Freeman,L.A., Fan,X.,
            Kullo,I.J., Biesecker,L.G. and Remaley,A.T.
  TITLE     DENND5B Regulates Intestinal Triglyceride Absorption and Body Mass
  JOURNAL   Sci Rep 9 (1), 3597 (2019)
   PUBMED   30837651
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1274)
  AUTHORS   Yoshimura,S., Gerondopoulos,A., Linford,A., Rigden,D.J. and
            Barr,F.A.
  TITLE     Family-wide characterization of the DENN domain Rab GDP-GTP
            exchange factors
  JOURNAL   J Cell Biol 191 (2), 367-381 (2010)
   PUBMED   20937701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 24, 2024 this sequence version replaced XP_038964852.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.25990.1,
                                           SRR26643289.14573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1274
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..1274
                     /product="DENN domain containing 5B isoform 2"
                     /note="DENN/MADD domain containing 5B; DENN
                     domain-containing protein 5B"
                     /calculated_mol_wt=144517
     Region          19..120
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Region          187..375
                     /region_name="DENN"
                     /note="DENN (AEX-3) domain; pfam02141"
                     /db_xref="CDD:460461"
     Region          499..574
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     Region          727..932
                     /region_name="RUN1_DENND5B"
                     /note="RUN1 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17691"
                     /db_xref="CDD:439053"
     Site            order(744,748,751,755,758,907,911,914..915,917,921..922)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439053"
     Region          936..1044
                     /region_name="PLAT_RAB6IP1"
                     /note="PLAT/LH2 domain present in RAB6 interacting protein
                     1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an
                     eight stranded beta-barrel. In RabIP1 this domain may
                     participate in lipid-mediated modulation of Rab6IP1's
                     function via it's generally proposed...; cd01757"
                     /db_xref="CDD:238855"
     Region          1091..1269
                     /region_name="RUN2_DENND5B"
                     /note="RUN2 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17693"
                     /db_xref="CDD:439055"
     CDS             1..1274
                     /gene="Dennd5b"
                     /coded_by="NM_001431961.1:257..4081"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100365679"
                     /db_xref="RGD:2318606"
ORIGIN      
        1 msgsgaapgp gsgsspaacr fahyfvlcgi dadsglepde lagenfdqsp lrrtfkskvl
       61 ahypqniewn pfdqdavnml cmpkglsfrt qadnkdpqfh sfiitredgs rtygfvltfy
      121 eevtskqict amqtlyqmhn aeqyssvyas sscsmdslas sidegdatsl lklqrynsyd
      181 inrdtlyvsk siclitplpf mqacrkfllq lhkavtsqqp pplplesyih nilyevplpp
      241 pgrslkfygv yepvicqrpg pnelplsdyp lreacellgl enlvqvftcv llemqillys
      301 qdyqrlmtva egittllfpf qwqhvyvpil pasllhflda pvpylmglqs kegtdrskle
      361 lpqeanlcfv didnhfielp eefpqfpnkv dfiqelsevl lqfgippegs lhcsesatkl
      421 knmvlkdlan dkkngnvptn nvsvyellkg setiarlqal akrtgvtvgk idfpaslsek
      481 ekdlklqcee adlrdsqlnv qlrevfanrf tqmfadyeaf viqtaqdmes wltsreqmqn
      541 fdkasflsdq pepylpflsr fietqmfatf idnkimsqwe ekdpllrvfd sriekmrlyn
      601 vraptlrtsi yqkcsslkea aqsieqrlmk mdhtaihphl ldmkigqgky eqgffpklqs
      661 dvlatgpann nrwvsrstta qrrkerlrqn aehigldsdl rekymqears lgknlrqpkl
      721 sdlspaviaq tnwkfvegll kecrmktkrm lvekmgheav elghgeanit gleentlias
      781 lcdlleriws hgllvkqgks alwshliqfq dreekqehlt dspvalgper rksdsgvmlp
      841 tlrvsliqdm rhvqnmteik tdvgrarawi rlslekklls qhlkqllsnq pltkklykry
      901 aflrceeere qflyhllsln avdyfcftsv fttimipyrs viipikklsn aiitsnpwic
      961 vsgelgdtgv mqipknllem tfecqnlgkl ttvqighdns gllakwlvdc vmvrneitgh
     1021 tyrfpcgrwl gkgvddgsle riligelmts asdedlgkqc rtppqqkspt ttrrlsitsl
     1081 tgkpakpnag qiqegigeav nnivkhfhkp ekergsltvl lcgenglvaa leqvfhhgfk
     1141 sarifhknvf iwdfvekava yfestdqild neddmliqkp scktfchyvn avntaprnig
     1201 kdgkfqilvc lgtrdhllpq wipllaecpa itrmyeenal lrdhmtvnsl irilqtiqdf
     1261 tivlegslik gvdv
//
LOCUS       NP_001423422            1297 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001423422 XP_006242821
VERSION     NP_001423422.1
DBSOURCE    REFSEQ: accession NM_001436493.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1297)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1297)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1297)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006242821.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.34341.1,
                                           SRR26643298.43434.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1297
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1297
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 3"
                     /calculated_mol_wt=138683
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          392..478
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <683..887
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <982..>1188
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     CDS             1..1297
                     /gene="Nfrkb"
                     /coded_by="NM_001436493.1:108..4001"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deedlsswlp ssparspspa vplrvvptls
      241 ttdmktadki elgdsdlklm lkkhhekrkh qpdhpdlltg dltlsdimtr vnagrkgsla
      301 alydlavlkk kvkekeekkk kkikliksea edlaeplsnt egvptlsqap splaissike
      361 epledikpcl gineisssff sllleillle sqaslpmled rvldwqsspa sslnswfsaa
      421 pnwaelvlpa lqylagesra vpssfspfve fkektqqwkl lgqsqdneke laalfhlwle
      481 tkdqafckqe nedssdamtp vprvrtdyvv rpstgeekrv fqeqeryrys qphkaftfrm
      541 hgfesvvgpv kgvfdketsl nkarehsllr sdrpayvtil slvrdaaarl pngegtraei
      601 cellkdsqfl apdvtstqvn tvvsgaldrl hyekdpcvky digrklwiyl hrdrseeefe
      661 rihqaqaaaa karkalqqkp kppskvkssn kegsvkglsg psepsqmsls dssmpptpvt
      721 pvtpttpalp tpispppvsa vsrsgsttvs epaksssgvl lvssptmpql gtmlspasiq
      781 tppssqttar vvshsssagl pqvrvvaqps lpavsqqsvg paqplpqmpa gpqirvpvta
      841 tqtkvvpqav vatvpvkgqt taasvqrpgp aqtgltvtsl paavspgskt amsspgssap
      901 sasttaviqn vtgqniikqv sitgqlgvkp qtgnsiplta tnfriqgkdv lrlppssitt
      961 dakgqtvlri tpdmmatlak sqvttvkltq dlfgagsgta gkgisatlhv tsnpvhaads
     1021 pakapsasvp ssapagttvv kvtpdlkpte tsssafrlmp algvsvadqk gkntvassea
     1081 kpaatirivq glgvmppkag qtitvaahak qgasvaggsg tvhsstvslp sinatvsktv
     1141 avasgatstp isigtgaptv rqvpvnttvv stsqsgklpt ritvplsvis qpmkgksvvt
     1201 apiikgnlga nlsglgrnii lttmpagakl iagnkpvsfl taqqlqqlqq qgqatqvriq
     1261 tvpashlqqg tasgsskavs tvvvttapsp kqapeqq
//
LOCUS       NP_001417419             544 aa            linear   ROD 28-APR-2025
DEFINITION  nucleolar protein 4-like isoform 3 [Rattus norvegicus].
ACCESSION   NP_001417419 XP_038962604
VERSION     NP_001417419.1
DBSOURCE    REFSEQ: accession NM_001430490.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On May 14, 2024 this sequence version replaced XP_038962604.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.19726.1,
                                           SRR26360181.1586758.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..544
                     /product="nucleolar protein 4-like isoform 3"
                     /calculated_mol_wt=59418
     Region          <15..50
                     /region_name="Integrase_H2C2"
                     /note="Integrase zinc binding domain; pfam17921"
                     /db_xref="CDD:465569"
     CDS             1..544
                     /gene="Nol4l"
                     /gene_synonym="RGD1563510"
                     /coded_by="NM_001430490.1:927..2561"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362240"
                     /db_xref="RGD:1563510"
ORIGIN      
        1 mhvessaepg kapkhagqkk tyraiaetya flpreavtrf lmsctecqkr mhfnssgpep
       61 keneppsplv sgiidynmpl tstylkqmkl rvmnsqeqde tsvssedfdm ndstwmsadp
      121 hlasslspnq eermrspqnl hsqedddsss esgsgngsst lnpstssstq gdpafpemng
      181 ngaaapmdft asaedqpinl ceklppgtal gtpsypsdgc gtdglrsrvk ygvkstpesp
      241 pyssgsydsi ktevsgcped ltvgrapaad dddddhddhe dndkmndseg mdperlkafn
      301 mfvrlfvden ldrmvpiskq pkekiqaiie scsrqfpefq erarkrirty lkscrrmkkn
      361 gmemtrptpp hltsamaeni laaacesetr kaakrmrlei yqssqeepia ldkqhprdst
      421 aithstyslp asaysqdpvy vngglnysyr gygslssnlq psaslqtgsh sngptdlsmk
      481 ggastptppt ptpssnstsr tmptaqlspt eisavrqlia gyresaafll rsadelenli
      541 lqqn
//
LOCUS       NP_001416978             551 aa            linear   ROD 28-APR-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 3
            isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416978
VERSION     NP_001416978.1
DBSOURCE    REFSEQ: accession NM_001430049.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Rai,A.K., Chen,J.X., Selbach,M. and Pelkmans,L.
  TITLE     Kinase-controlled phase transition of membraneless organelles in
            mitosis
  JOURNAL   Nature 559 (7713), 211-216 (2018)
   PUBMED   29973724
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Kim,K., Cha,J.S., Cho,Y.S., Kim,H., Chang,N., Kim,H.J. and Cho,H.S.
  TITLE     Crystal Structure of Human Dual-Specificity Tyrosine-Regulated
            Kinase 3 Reveals New Structural Features and Insights into its
            Auto-phosphorylation
  JOURNAL   J Mol Biol 430 (10), 1521-1530 (2018)
   PUBMED   29634919
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Wippich,F., Bodenmiller,B., Trajkovska,M.G., Wanka,S., Aebersold,R.
            and Pelkmans,L.
  TITLE     Dual specificity kinase DYRK3 couples stress granule
            condensation/dissolution to mTORC1 signaling
  JOURNAL   Cell 152 (4), 791-805 (2013)
   PUBMED   23415227
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Guo,X., Williams,J.G., Schug,T.T. and Li,X.
  TITLE     DYRK1A and DYRK3 promote cell survival through phosphorylation and
            activation of SIRT1
  JOURNAL   J Biol Chem 285 (17), 13223-13232 (2010)
   PUBMED   20167603
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Wojchowski,D.M., Menon,M.P., Sathyanarayana,P., Fang,J., Karur,V.,
            Houde,E., Kapelle,W. and Bogachev,O.
  TITLE     Erythropoietin-dependent erythropoiesis: New insights and questions
  JOURNAL   Blood Cells Mol Dis 36 (2), 232-238 (2006)
   PUBMED   16524748
  REMARK    Review article
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Li,K., Zhao,S., Karur,V. and Wojchowski,D.M.
  TITLE     DYRK3 activation, engagement of protein kinase A/cAMP response
            element-binding protein, and modulation of progenitor cell survival
  JOURNAL   J Biol Chem 277 (49), 47052-47060 (2002)
   PUBMED   12356771
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Lord,K.A., Creasy,C.L., King,A.G., King,C., Burns,B.M., Lee,J.C.
            and Dillon,S.B.
  TITLE     REDK, a novel human regulatory erythroid kinase
  JOURNAL   Blood 95 (9), 2838-2846 (2000)
   PUBMED   10779429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.3121331.1,
                                           SRR26643293.53129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..551
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 3 isoform 2"
                     /EC_number="2.7.12.1"
                     /note="dual-specificity tyrosine-(Y)-phosphorylation
                     regulated kinase 3"
                     /calculated_mol_wt=61713
     Region          107..486
                     /region_name="PKc_DYRK2_3"
                     /note="Catalytic domain of the protein kinases,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinases 2 and 3; cd14224"
                     /db_xref="CDD:271126"
     Site            order(179..183,187,200,202,216,236,252..255,258,260..261,
                     299,301,303..304,306,319,322,331,333..336,338,375)
                     /site_type="active"
                     /db_xref="CDD:271126"
     Site            order(179..183,187,200,202,236,252..255,258,299,301,
                     303..304,306,319)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271126"
     Site            order(216,260,299,301,322,331,333..336,338,375)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271126"
     Site            318..338
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271126"
     CDS             1..551
                     /gene="Dyrk3"
                     /coded_by="NM_001430049.1:352..2007"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304775"
                     /db_xref="RGD:1310924"
ORIGIN      
        1 mmidetkcpp ytntlcnpse apvsrrlnit tepftrghtq hfvsggvmkv eqlfqefgsr
       61 rtstlqsdgv snseksspas qgkssdslgt vkcslssrps kvlpltpeqa lkqykhhlta
      121 yekleiisyp eiyfvgpnak krqgviggpn nggyddadga yihvprdhla yryevlkiig
      181 kgsfgqvarv ydhklrqyva lkmvrnekrf hrqaaeeiri lehlkkqdkt gsmnvihmle
      241 sftfrnhvcm afellsidly elikknkfqg fsvqlvrkfa qsilqsldal hknkiihcdl
      301 kpenillkhh grsatkvidf gsscfeyqkl ytyiqsrfyr apeiilgcry stpidiwsfg
      361 cilaelltgq plfpgedegd qlacmmellg mppqklleqs krakyfinsk glprycsvtt
      421 qtdgrvvllg grsrrgkkrg ppgskdwaaa lkgcddylfi eflkrclqwd psarltpaqa
      481 lrhpwisksa prplttdkvs gkrvvnptna fqglgsklpp vvgiasklka nlmsetsgsi
      541 plcsvlpkli s
//
LOCUS       NP_001417075             165 aa            linear   ROD 28-APR-2025
DEFINITION  disks large homolog 5-like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001417075
VERSION     NP_001417075.1
DBSOURCE    REFSEQ: accession NM_001430146.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.683547.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8"
     Protein         1..165
                     /product="disks large homolog 5-like isoform 2"
                     /calculated_mol_wt=19183
     Region          48..>99
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..165
                     /gene="LOC134480019"
                     /coded_by="NM_001430146.1:73..570"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:134480019"
                     /db_xref="RGD:402460855"
ORIGIN      
        1 mfsrlrknfg rvnadfgqtg vresrlsski ndgqrklawg mlndgrltss pgpvvinkea
       61 ntenteeqrl irqlqsatee rnelrdllty vteryrnnrn lpsrihmdki cmqkklfpfr
      121 kegkteqlds apllqkflfd lnkkdkdeqe ktsnlqtkqh ldntt
//
LOCUS       NP_001106836             714 aa            linear   ROD 28-APR-2025
DEFINITION  TBC1 domain family member 14 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001106836
VERSION     NP_001106836.1
DBSOURCE    REFSEQ: accession NM_001113365.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Longatti,A., Lamb,C.A., Razi,M., Yoshimura,S., Barr,F.A. and
            Tooze,S.A.
  TITLE     TBC1D14 regulates autophagosome formation via Rab11- and
            ULK1-positive recycling endosomes
  JOURNAL   J Cell Biol 197 (5), 659-675 (2012)
   PUBMED   22613832
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Fuchs,E., Haas,A.K., Spooner,R.A., Yoshimura,S., Lord,J.M. and
            Barr,F.A.
  TITLE     Specific Rab GTPase-activating proteins define the Shiga toxin and
            epidermal growth factor uptake pathways
  JOURNAL   J Cell Biol 177 (6), 1133-1143 (2007)
   PUBMED   17562788
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Yamano,Y., Ohyama,K., Ohta,M., Sano,T., Ritani,A., Shimada,J.,
            Ashida,N., Yoshida,E., Ikehara,K. and Morishima,I.
  TITLE     A novel spermatogenesis related factor-2 (SRF-2) gene expression
            affected by TCDD treatment
  JOURNAL   Endocr J 52 (1), 75-81 (2005)
   PUBMED   15758561
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Horiba,N., Masuda,S., Takeuchi,A., Saito,H., Okuda,M. and Inui,K.
  TITLE     Gene expression variance based on random sequencing in rat remnant
            kidney
  JOURNAL   Kidney Int 66 (1), 29-45 (2004)
   PUBMED   15200410
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB117752.1 and BC099760.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB117752.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..714
                     /product="TBC1 domain family member 14 isoform 3"
                     /note="Up-regulated in nephrectomized rat kidney #2;
                     spermatogenesis-related factor 2"
                     /calculated_mol_wt=80612
     Region          350..>389
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          419..651
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..714
                     /gene="Tbc1d14"
                     /gene_synonym="SRF-2; UR-NR#2"
                     /coded_by="NM_001113365.1:318..2462"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:360956"
                     /db_xref="RGD:1309993"
ORIGIN      
        1 mrlyldrfwg lmvkvsswtk mtdgnlstsm ngvalmgild grpgdslqel qhlsikavpr
       61 slsvpdygpt lklgaledrh slqsvdsgip tleignpepv pcsvvhvkrk qseseiiper
      121 afqsacplps ctpsaptgse reqavrksst fprtgydsvk lysptskals rsddvsvcsv
      181 sslgtelstt lsvsnedild lmvtsnssai vtlendddpq ftdvtlssik etsdlhqqdc
      241 vaeteegrkl rllqpfshff trnllarkqn arldrqrdlg wklfgkvplr etaqkdskkt
      301 qkeyedkagr psrppspkqn vrknldfepl sttaliledr panlpakpae eaqkhrqqye
      361 emvvqakkre lkeaqrrkkq leerckvees ignavltwnn eilpnwetmw cskkvrdlww
      421 qgippsvrgk vwslaignel nithelfdic larakerwrs lstggseven edagfsaadr
      481 easlelikld isrtfpnlci fqqggpyhdm lhsilgaytc yrpdvgyvqg msfiaavlil
      541 nldtadafia fsnllnkpcq maffrvdhgl mltyfaafev ffeenlpklf ahfkknnlta
      601 diylidwift lyskslpldl acriwdvfcr dgeeflfrta lgilklfedi ltrmdfihsa
      661 qfltrlpedl paddvfaais tvqmqsrnkk waqvlsalqk dsremekgsp slrh
//
LOCUS       NP_001092981             853 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor, 42 precursor [Rattus norvegicus].
ACCESSION   NP_001092981 XP_001053488
VERSION     NP_001092981.1
DBSOURCE    REFSEQ: accession NM_001099511.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 26, 2007 this sequence version replaced XP_001053488.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..853
                     /product="vomeronasal 2 receptor, 42 precursor"
                     /calculated_mol_wt=95424
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2700
     Region          44..504
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(73,169..170,394)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(111,112,153,243)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          512..565
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          585..836
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          585..610
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(588,591..592,595..596,598..599,633,637,640..641,649,
                     653)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          622..643
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(642,654..655,658..659,662,742,747,750..751,754,788,
                     791..792,795,799,807..808,811,814,818)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          652..676
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          700..716
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          743..769
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          777..800
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          805..830
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..853
                     /gene="Vom2r42"
                     /coded_by="NM_001099511.1:1..2562"
                     /db_xref="GeneID:679557"
                     /db_xref="RGD:1587126"
ORIGIN      
        1 mikmftflfa flvlklsfll cssidnrcfw rlktktpwee dkdidcfffi ytkfghvkne
       61 qfsgnldkrl ttknihlilt lyfaleeinm npnilpnisl lvkiecslld dwrinslssk
      121 reeylpnyyc inqrsylivl tgpmcetntl ysrffmlflt fyglqlyygp fhpllssqel
      181 ypylyqmapk dtslalamvs llvhfswnwv gavvsdddpg yefilelrre mqrnsvclaf
      241 vsiiisdekl flksiniyyk qitmssakvv iiygdkdspl qlnfrlwnll diqriwvtts
      301 qwdmiikngk slltsfygtl tfshhysels gfktfiqtaf psnysddisl arlwwmyfnc
      361 slslsdcnnl qncsnenivr wlfrhhfems lsdttydlyn svyavahtlq qmlvqqedtw
      421 hiddgkelef dswqmvsflk ntqfinpagd kvnlnhkekp dteydihytm dfwpnlvfkl
      481 kmetfsqnlq hgqqlnmlke miewitghqq sptsicsipc spgfrkspqq gkpvccfdct
      541 pcpedeisnm tnmnqcikcl ddeyanpggt ncfkkliafl gyedplgmsl tilalcfsal
      601 tafvfgiflk hqesptvkan nrtlsyvllt sliscflcsl lfighpnfat cimqqttfav
      661 vftvaastvl aktiivilaf kvtntsrkmr wllvsgapkf iipictmiql ilcgiwlgts
      721 ppfvdadghv ekghilifcn kgsvlafyci lgylgsiaig sftlaflarn lpntfneaky
      781 ltfsmlvfcs vwitflpvyh stkgksmvav evfcilassa gllfcifapk cfiillrpek
      841 kssqkfqnih skm
//
LOCUS       NP_001102216             151 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC362881 precursor [Rattus norvegicus].
ACCESSION   NP_001102216 XP_001080967 XP_343210
VERSION     NP_001102216.1
DBSOURCE    REFSEQ: accession NM_001108746.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473960.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001080967.1, XP_343210.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB811061.1, CB779224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..151
                     /product="uncharacterized protein LOC362881 precursor"
                     /note="lysozyme f1"
                     /calculated_mol_wt=14802
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2196
     Region          22..149
                     /region_name="LYZ_C"
                     /note="C-type lysozyme; cd16897"
                     /db_xref="CDD:340383"
     Site            order(67,74,79..81,84..85,123,125,129..131)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:340383"
     Site            order(67,74,79..81,84..85,123,125,129..131)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:340383"
     CDS             1..151
                     /gene="RGD1306474"
                     /gene_synonym="Lyzf1"
                     /coded_by="NM_001108746.1:76..531"
                     /db_xref="GeneID:362881"
                     /db_xref="RGD:1306474"
ORIGIN      
        1 mkalptlltl gllllsitvq gkvlnrclla rtlqrfglgg fkgislanwi claksvsgyd
       61 tkaikynhed rstnygifqi ssrywcndsk tpgsknfcrv sckallknni kasvtcakri
      121 vkdprgittw eawrkncehk nlfqyvqgcs l
//
LOCUS       NP_001418516             672 aa            linear   ROD 28-APR-2025
DEFINITION  sciellin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001418516 XP_006252490
VERSION     NP_001418516.1
DBSOURCE    REFSEQ: accession NM_001431587.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Chou,C.K., Fan,C.C., Lin,P.S., Liao,P.Y., Tung,J.C., Hsieh,C.H.,
            Hung,M.C., Chen,C.H. and Chang,W.C.
  TITLE     Sciellin mediates mesenchymal-to-epithelial transition in
            colorectal cancer hepatic metastasis
  JOURNAL   Oncotarget 7 (18), 25742-25754 (2016)
   PUBMED   27013588
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Pyle,A.L., Li,B., Maupin,A.B., Guzman,R.J., Crimmins,D.L.,
            Olson,S., Atkinson,J.B. and Young,P.P.
  TITLE     Biomechanical stress induces novel arterial intima-enriched genes:
            implications for vascular adaptation to stress
  JOURNAL   Cardiovasc Pathol 19 (2), e13-e20 (2010)
   PUBMED   19211270
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Champliaud,M.F., Viel,A. and Baden,H.P.
  TITLE     The expression of vitamin D-upregulated protein 1 in skin and its
            interaction with sciellin in cultured keratinocytes
  JOURNAL   J Invest Dermatol 121 (4), 781-785 (2003)
   PUBMED   14632196
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Champliaud,M.F., Baden,H.P., Koch,M., Jin,W., Burgeson,R.E. and
            Viel,A.
  TITLE     Gene characterization of sciellin (SCEL) and protein localization
            in vertebrate epithelia displaying barrier properties
  JOURNAL   Genomics 70 (2), 264-268 (2000)
   PUBMED   11112355
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Champliaud,M.F., Burgeson,R.E., Jin,W., Baden,H.P. and Olson,P.F.
  TITLE     cDNA cloning and characterization of sciellin, a LIM domain protein
            of the keratinocyte cornified envelope
  JOURNAL   J Biol Chem 273 (47), 31547-31554 (1998)
   PUBMED   9813070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Jul 19, 2024 this sequence version replaced XP_006252490.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.51569.1,
                                           SRR26643299.57622.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..672
                     /product="sciellin isoform 1"
                     /calculated_mol_wt=74760
     Region          604..662
                     /region_name="LIM"
                     /note="Zinc-binding domain present in Lin-11, Isl-1,
                     Mec-3; smart00132"
                     /db_xref="CDD:214528"
     Site            order(605,608,628,631,634,637,659,662)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..672
                     /gene="Scel"
                     /coded_by="NM_001431587.1:148..2166"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361086"
                     /db_xref="RGD:1305102"
ORIGIN      
        1 msnfssrkks pvgndpkstq gaalrqqgfh dvnkrraflq dnswikklpe eekdenygrv
       61 vlsrhnshda ldrkiterde pkatisryrs edmldrslst frtpestktp agssfsantt
      121 apstpattpv kkkrqswfpp pppghnapps tgasrrdppl hpplppkpcs piaspkqlrq
      181 shrqmhmata gacgeadrha arnirtedld diirvaaalq ktdkgeeldn lirmnkslnr
      241 nqgldglfra nlkaqqldkr aqslesliym ntqmdrdgkg nqafgsfkki nqradtergs
      301 qdqrsiirtn amaerssrrg kdldsvmkis pkghesatgk qdlgglinvn petnksmkrg
      361 qslenlikvt levnrsskgg qsldnfikav patdranqgs qgldslmkvt psanksnqhs
      421 ldelvntspk avkttaghqd ldkfikvnad vltnnqrnhd ldnsirgnpt vnrcdqshdl
      481 dnlikvkpsa lrntngdqdl kgltevnsrv sedknervdg qangvtnslr kesprtsvys
      541 hetktslssn sgtrnagpkd tvvytrtyve nskspkdgyq enisgkyiqt vystsdrsvi
      601 erdmctycrk plgvetkmil delqicchst cfkceickrp lenlqagdsi wiyrqtihce
      661 pcyskvmakw iq
//
LOCUS       NP_001419376            1264 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology domain-containing family A member 7 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001419376 XP_038957080
VERSION     NP_001419376.1
DBSOURCE    REFSEQ: accession NM_001432447.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   Shah,J., Rouaud,F., Guerrera,D., Vasileva,E., Popov,L.M.,
            Kelley,W.L., Rubinstein,E., Carette,J.E., Amieva,M.R. and Citi,S.
  TITLE     A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
            Promote alpha-Toxin Cytotoxicity
  JOURNAL   Cell Rep 25 (8), 2132-2147 (2018)
   PUBMED   30463011
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Endres,B.T., Priestley,J.R., Palygin,O., Flister,M.J.,
            Hoffman,M.J., Weinberg,B.D., Grzybowski,M., Lombard,J.H.,
            Staruschenko,A., Moreno,C., Jacob,H.J. and Geurts,A.M.
  TITLE     Mutation of Plekha7 attenuates salt-sensitive hypertension in the
            rat
  JOURNAL   Proc Natl Acad Sci U S A 111 (35), 12817-12822 (2014)
   PUBMED   25136115
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Kurita,S., Yamada,T., Rikitsu,E., Ikeda,W. and Takai,Y.
  TITLE     Binding between the junctional proteins afadin and PLEKHA7 and
            implication in the formation of adherens junction in epithelial
            cells
  JOURNAL   J Biol Chem 288 (41), 29356-29368 (2013)
   PUBMED   23990464
REFERENCE   4  (residues 1 to 1264)
  AUTHORS   Pulimeno,P., Paschoud,S. and Citi,S.
  TITLE     A role for ZO-1 and PLEKHA7 in recruiting paracingulin to tight and
            adherens junctions of epithelial cells
  JOURNAL   J Biol Chem 286 (19), 16743-16750 (2011)
   PUBMED   21454477
  REMARK    GeneRIF: ZO-1 and PLEKHA7 are paracingulin-interacting proteins
            that are involved in its recruitment to epithelial tight and
            adherens junctions, respectively
REFERENCE   5  (residues 1 to 1264)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 1264)
  AUTHORS   Meng,W., Mushika,Y., Ichii,T. and Takeichi,M.
  TITLE     Anchorage of microtubule minus ends to adherens junctions regulates
            epithelial cell-cell contacts
  JOURNAL   Cell 135 (5), 948-959 (2008)
   PUBMED   19041755
REFERENCE   7  (residues 1 to 1264)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_038957080.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.2006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..1264
                     /product="pleckstrin homology domain-containing family A
                     member 7 isoform 2"
                     /note="pleckstrin homology domain containing, family A
                     member 7"
                     /calculated_mol_wt=143612
     Region          55..84
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          158..280
                     /region_name="PH_PEPP1_2_3"
                     /note="Phosphoinositol 3-phosphate binding proteins 1, 2,
                     and 3 pleckstrin homology (PH) domain; cd13248"
                     /db_xref="CDD:270068"
     Site            order(172,174..175,182,184,195,257)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270068"
     Region          707..>807
                     /region_name="CCDC90-like"
                     /note="Coiled-coil domain-containing protein 90-like;
                     pfam07798"
                     /db_xref="CDD:462268"
     Region          <834..940
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1264
                     /gene="Plekha7"
                     /gene_synonym="RGD1304650"
                     /coded_by="NM_001432447.1:16..3810"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:499249"
                     /db_xref="RGD:1598216"
ORIGIN      
        1 maaavgrdtl pehwsygvcr dgrvffindq lrcttwlhpr tgepvnsghm irsdlprgwe
       61 egfteegasf fidhnqqttt frhpvtgqfs senseyvlre ephphmskqe rnqrpssmvs
      121 etstagttst leakpgpkii kssskvhsfg krdqairrnl nvpvvvrgwl hkqdssgmrl
      181 wkrrwfvlad yclfyykdsr eeavlgsipl psyvispvap edrisrkysf kavhtgmral
      241 iystttagsq aehsgmrtyy fsadtledmn awvramnqaa qvlsrsslkr dkverqampq
      301 anhtdacqec ghvgpghsrd cprrgyedai vfdrreqeee rfrsqrdtle grrdrskars
      361 pylpaeedal fvdlpggprg qqaqpqraer nglppyglge qngtsgysrt appranlekh
      421 sqrktnlaqt ehwakaqkgd grslpldqtl prqgpsqpps flenyqtlpr ntrypsgsss
      481 ppprnlpsdy kyaqdrashl kmsseerrah rdgtvwqlye wqqrqqfrhg sptapigags
      541 pefteqgrsr sllevprsis vppspsdipp pgpprpfppr rphtpaervt vkppdqrrsv
      601 dislggsprk arghavknss hvdrrsmpsm gymthtvsap slhgksaddt ylqlkkdley
      661 ldlkmtgrdl lkdrslkpmk iaesdtdvkl sifceqdril qdledkiral kenkdqlesv
      721 levlhrqteq yrdqpqhlek itcqqrllqe dlvhiraelc restemenaw neylklekdv
      781 eqlkqtlqeq hrrafffqek sqiqkdlwri edvmaglsvn kenyrvlvgs vknperktvp
      841 lfphpsvpsl spteskpalq pspptspvrt plevrlfpql qtyvpyrphp pqlrkvvspl
      901 qsptkatpqa edeapprppl pelyspedqp pavpplprea tiirhtsvrg lkrqsderkr
      961 dreqgqcvng dlkvelrsyv sepelasfsg dvprpslglv gsesryqtlp grglsgstsr
     1021 lqqsstiapy vtlrrglnae nssvtfsrpk salerlysgd hqrgkmsaee qlermkrhqk
     1081 alvrerkrtl sqgertglls arylsqplpg dlgswkreqe fdlqlleraa qgdrkdkeeg
     1141 wlkvqatpvm eldlepqdyd ldinrelskp ekvsiperyv evdpeeppsv eelqaryqka
     1201 ekirnilars smcnlqppgq drnsladldt qmqeqeriin isyalaseas qrskqvaaqa
     1261 vtdp
//
LOCUS       NP_001417418             579 aa            linear   ROD 28-APR-2025
DEFINITION  nucleolar protein 4-like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001417418 XP_038962602
VERSION     NP_001417418.1
DBSOURCE    REFSEQ: accession NM_001430489.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On May 14, 2024 this sequence version replaced XP_038962602.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.496216.1,
                                           SRR26643293.19734.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..579
                     /product="nucleolar protein 4-like isoform 2"
                     /calculated_mol_wt=63200
     Region          31..85
                     /region_name="Integrase_H2C2"
                     /note="Integrase zinc binding domain; pfam17921"
                     /db_xref="CDD:465569"
     CDS             1..579
                     /gene="Nol4l"
                     /gene_synonym="RGD1563510"
                     /coded_by="NM_001430489.1:265..2004"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362240"
                     /db_xref="RGD:1563510"
ORIGIN      
        1 mnvsrgqgad glsepegisl krvavvedff diiysmhves saepgkapkh agqkktyrai
       61 aetyaflpre avtrflmsct ecqkrmhfns sgpepkenep psplvsgiid ynmpltstyl
      121 kqmklrvmns qeqdetsvss edfdmndstw msadphlass lspnqeermr spqnlhsqed
      181 ddsssesgsg ngsstlnpst ssstqgdpaf pemngngaaa pmdftasaed qpinlceklp
      241 pgtalgtpsy psdgcgtdgl rsrvkygvks tpesppyssg sydsiktevs gcpedltvgr
      301 apaadddddd hddhedndkm ndsegmdper lkafnmfvrl fvdenldrmv piskqpkeki
      361 qaiiescsrq fpefqerark rirtylkscr rmkkngmemt rptpphltsa maenilaaac
      421 esetrkaakr mrleiyqssq eepialdkqh prdstaiths tyslpasays qdpvyvnggl
      481 nysyrgygsl ssnlqpsasl qtgshsngpt dlsmkggast ptpptptpss nstsrtmpta
      541 qlspteisav rqliagyres aafllrsade lenlilqqn
//
LOCUS       NP_001100480            1211 aa            linear   ROD 28-APR-2025
DEFINITION  CST complex subunit CTC1 [Rattus norvegicus].
ACCESSION   NP_001100480 XP_001078525 XP_220595
VERSION     NP_001100480.1
DBSOURCE    REFSEQ: accession NM_001107010.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Chen,L.Y., Redon,S. and Lingner,J.
  TITLE     The human CST complex is a terminator of telomerase activity
  JOURNAL   Nature 488 (7412), 540-544 (2012)
   PUBMED   22763445
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Gu,P., Min,J.N., Wang,Y., Huang,C., Peng,T., Chai,W. and Chang,S.
  TITLE     CTC1 deletion results in defective telomere replication, leading to
            catastrophic telomere loss and stem cell exhaustion
  JOURNAL   EMBO J 31 (10), 2309-2321 (2012)
   PUBMED   22531781
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Surovtseva,Y.V., Churikov,D., Boltz,K.A., Song,X., Lamb,J.C.,
            Warrington,R., Leehy,K., Heacock,M., Price,C.M. and Shippen,D.E.
  TITLE     Conserved telomere maintenance component 1 interacts with STN1 and
            maintains chromosome ends in higher eukaryotes
  JOURNAL   Mol Cell 36 (2), 207-218 (2009)
   PUBMED   19854131
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_220595.4, XP_001078525.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1211
                     /product="CST complex subunit CTC1"
                     /note="CTS telomere maintenance complex component 1"
                     /calculated_mol_wt=133781
     Region          61..1195
                     /region_name="CTC1"
                     /note="CST, telomere maintenance, complex subunit CTC1;
                     pfam15489"
                     /db_xref="CDD:464744"
     CDS             1..1211
                     /gene="Ctc1"
                     /gene_synonym="RGD1563106"
                     /coded_by="NM_001107010.1:221..3856"
                     /db_xref="GeneID:303238"
                     /db_xref="RGD:1563106"
ORIGIN      
        1 maacraqppt seeawleaaq afiqetlcpv deepneqvtr svidcvketw lsqgenqdlt
       61 lplsysfvsv qnlktnqhlp ccshlswsdn ayqawtrgag pggsvlpreq llllgtlvdl
      121 lgdleqesrs gglyvrdntg tldcelidld lswlghlflf pswsylppak rnslgaghle
      181 lwgtpvpvfp ltvspgpltp ipvlypekas yllryrkkck ikelnlagkl vhlsalmvtq
      241 nkryfimtlg elaqagsqvs vivqipaqmv whrvlrpgra yvltklritk trghrsciwt
      301 tipsstlmpl rpgyvqelel dvafadaghk plpeptssrd srgqeglvrg skvlhylgtv
      361 tdvlnesasl yildgqlilc layqkihglr rvirpgvcle lrdvhllqgl gggttkpvla
      421 lclhgtvrlq gfsclkpqnl psykvhgasl yeqlvwkcql glplylwatk aleelvyklc
      481 phvlrcqqfl khsspgkpsl glqllapswd vlippgspir hahseileep hncplqkytp
      541 lqtpytfpti lalaeegqhr awatfdpral lpfpeafhlt scqlnrrlaw swlclpssmf
      601 qpapvllgvl vasshkgclq lrdvrgslpc iplpessqpl idpkligclv rvekfqlvve
      661 revrssfpsw eelgmasliq kkqarvyvqf yladalilpv prptvgleps etasscpegp
      721 qvgqsrlfll fykealmkrn fcllpgdssr paeptlsfrv sgtwlcgtqk regsgwsppe
      781 slaaenkdqk vffiflgssv qwfpflypnq vyrlvapdst palfetnhss gtphrplelt
      841 dyvscltiqe dwtlelgssq dipnvlevpr tlsesslahl lsdnspnflv sfsaevlsri
      901 lcepplalrr ikpgnagaik agvkltvale medcdypphl diyiedphlp ppigllpgar
      961 vhfsqlekki srsnvvyccf rsttsvqvls fppetkasap lphiclaell qgdrppfqat
     1021 tschivyvls lqilwvcahc tsicpqgkcs rqdpscpsqr aisqasirll vedgtaeatv
     1081 tcrnhhvatt lglspsewsn vldrargpgr valqfkgpga qtesasktge pltlllqtlc
     1141 tspfvlrpik lsfalerrpc ditpiepprl qqfqcgelpl ltrvnprlrl vclslqepel
     1201 psppqasaaa s
//
LOCUS       NP_851602                920 aa            linear   ROD 28-APR-2025
DEFINITION  whirlin isoform 1 [Rattus norvegicus].
ACCESSION   NP_851602
VERSION     NP_851602.2
DBSOURCE    REFSEQ: accession NM_181088.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Ebrahim,S., Ingham,N.J., Lewis,M.A., Rogers,M.J.C., Cui,R.,
            Kachar,B., Pass,J.C. and Steel,K.P.
  TITLE     Alternative Splice Forms Influence Functions of Whirlin in
            Mechanosensory Hair Cell Stereocilia
  JOURNAL   Cell Rep 15 (5), 935-943 (2016)
   PUBMED   27117407
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Ciardo,M.G., Andres-Borderia,A., Cuesta,N., Valente,P.,
            Camprubi-Robles,M., Yang,J., Planells-Cases,R. and
            Ferrer-Montiel,A.
  TITLE     Whirlin increases TRPV1 channel expression and cellular stability
  JOURNAL   Biochim Biophys Acta 1863 (1), 115-127 (2016)
   PUBMED   26516054
  REMARK    GeneRIF: findings indicate that Whirlin and TRPV1 are associated in
            a subset of nociceptors and that TRPV1 protein stability is
            increased through the interaction with the cytoskeletal scaffold
            protein.
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Chen,Q., Zou,J., Shen,Z., Zhang,W. and Yang,J.
  TITLE     Whirlin and PDZ domain-containing 7 (PDZD7) proteins are both
            required to form the quaternary protein complex associated with
            Usher syndrome type 2
  JOURNAL   J Biol Chem 289 (52), 36070-36088 (2014)
   PUBMED   25406310
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Zou,J., Zheng,T., Ren,C., Askew,C., Liu,X.P., Pan,B., Holt,J.R.,
            Wang,Y. and Yang,J.
  TITLE     Deletion of PDZD7 disrupts the Usher syndrome type 2 protein
            complex in cochlear hair cells and causes hearing loss in mice
  JOURNAL   Hum Mol Genet 23 (9), 2374-2390 (2014)
   PUBMED   24334608
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Green,J.A., Yang,J., Grati,M., Kachar,B. and Bhat,M.A.
  TITLE     Whirlin, a cytoskeletal scaffolding protein, stabilizes the
            paranodal region and axonal cytoskeleton in myelinated axons
  JOURNAL   BMC Neurosci 14, 96 (2013)
   PUBMED   24011083
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Kikkawa,Y., Mburu,P., Morse,S., Kominami,R., Townsend,S. and
            Brown,S.D.
  TITLE     Mutant analysis reveals whirlin as a dynamic organizer in the
            growing hair cell stereocilium
  JOURNAL   Hum Mol Genet 14 (3), 391-400 (2005)
   PUBMED   15590699
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Delprat,B., Michel,V., Goodyear,R., Yamasaki,Y., Michalski,N.,
            El-Amraoui,A., Perfettini,I., Legrain,P., Richardson,G.,
            Hardelin,J.P. and Petit,C.
  TITLE     Myosin XVa and whirlin, two deafness gene products required for
            hair bundle growth, are located at the stereocilia tips and
            interact directly
  JOURNAL   Hum Mol Genet 14 (3), 401-410 (2005)
   PUBMED   15590698
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Mburu,P., Mustapha,M., Varela,A., Weil,D., El-Amraoui,A.,
            Holme,R.H., Rump,A., Hardisty,R.E., Blanchard,S., Coimbra,R.S.,
            Perfettini,I., Parkinson,N., Mallon,A.M., Glenister,P.,
            Rogers,M.J., Paige,A.J., Moir,L., Clay,J., Rosenthal,A., Liu,X.Z.,
            Blanco,G., Steel,K.P., Petit,C. and Brown,S.D.
  TITLE     Defects in whirlin, a PDZ domain molecule involved in stereocilia
            elongation, cause deafness in the whirler mouse and families with
            DFNB31
  JOURNAL   Nat Genet 34 (4), 421-428 (2003)
   PUBMED   12833159
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Yap,C.C., Liang,F., Yamazaki,Y., Muto,Y., Kishida,H., Hayashida,T.,
            Hashikawa,T. and Yano,R.
  TITLE     CIP98, a novel PDZ domain protein, is expressed in the central
            nervous system and interacts with calmodulin-dependent serine
            kinase
  JOURNAL   J Neurochem 85 (1), 123-134 (2003)
   PUBMED   12641734
  REMARK    GeneRIF: CIP98, a novel protein (98 kDa) consisting of three PDZ
            domains and a proline-rich region, is widely expressed in the
            central nervous system and interacts with CASK
            (calmodulin-dependent serine kinase)
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Holme,R.H., Kiernan,B.W., Brown,S.D. and Steel,K.P.
  TITLE     Elongation of hair cell stereocilia is defective in the mouse
            mutant whirler
  JOURNAL   J Comp Neurol 450 (1), 94-102 (2002)
   PUBMED   12124769
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Dec 8, 2020 this sequence version replaced NP_851602.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY227205.1, SRR26360181.3147462.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..920
                     /product="whirlin isoform 1"
                     /note="CASK-interacting protein CIP98; deafness, autosomal
                     recessive 31"
                     /calculated_mol_wt=98090
     Region          38..113
                     /region_name="HN_L-whirlin_R1_like"
                     /note="first harmonin_N_like domain (repeat 1) of the long
                     isoform of whirlin, and related domains; cd07356"
                     /db_xref="CDD:259822"
     Site            order(40,44,57,60,63..64,67)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259822"
     Region          139..220
                     /region_name="PDZ1_FL-whirlin"
                     /note="PDZ domain 1 of the full-length isoform of whirlin
                     and related domains; cd06740"
                     /db_xref="CDD:467222"
     Site            order(152..158,170,173,202,206,209..210)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467222"
     Region          241..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          276..359
                     /region_name="PDZ2_FL-whirlin"
                     /note="PDZ domain 2 of the full-length isoform of whirlin
                     and related domains; cd06741"
                     /db_xref="CDD:467223"
     Site            order(288..294,306,309,338,342,345..346)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467223"
     Region          418..498
                     /region_name="HN_L-whirlin_R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of the
                     long isoform of whirlin, and related domains; cd07357"
                     /db_xref="CDD:259823"
     Site            order(419,422,426,439,442,445..446,449)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259823"
     Region          502..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          561..603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          630..730
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P202; propagated from
                     UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          752..828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          827..917
                     /region_name="PDZ3_FL-whirlin-like"
                     /note="PDZ domain 3 of the full-length isoform of whirlin,
                     PDZ domain 1 of the short isoform of whirlin, and related
                     domains; cd06742"
                     /db_xref="CDD:467224"
     Site            order(838..844,857,860,890,894,897..898)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467224"
     CDS             1..920
                     /gene="Whrn"
                     /gene_synonym="Cip98; Dfnb31"
                     /coded_by="NM_181088.2:752..3514"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:313255"
                     /db_xref="RGD:631330"
ORIGIN      
        1 mnaqldglsv sssstgslgs aaaaaggggg aglrllsanv rqlhqaltal lsepereqft
       61 hclnayharr nvfdlvrtlr vlldspvkrr llpmlrlvip rsdqllfdqy taeglylpat
      121 tpyrqpawaa pdgagpgevr lvslrrakah eglgfsirgg sehgvgiyvs lvepgslaek
      181 eglrvgdqil rvndkslarv thaeavkalk gskklvlsvy sagripggyv tnhiytwvdp
      241 qgrstsppss lphgstlrqh eddrrsalhl lqsgdekkvn lvlgdgrslg ltirggaeyg
      301 lgiyitgvdp gseaessglk vgdqilevng rsflsilhde avkllkssrh liltvkdvgr
      361 lpharttvdq tkwiassrig esitnsagfp gdlteegtnk pgfykgpags qvtlsslgnq
      421 trallddqar hllteqerat mmyyldqyrg gtisvealvm alfellntha kfsllsevrg
      481 iispqdldrf dhlvlrreie smkarqppgp gvgdtysmvs ysdtgsstgs hgtsttvssa
      541 rerllwlidl mentldlegt gettqgstna lpdvsvddvr spsedlpgik ppppppplaq
      601 ghdrllgqtr kpvredsapl ssaahsgivf saprnrsppp ppgiaptptp gpssardsps
      661 spiyasisha npssrkpldt hlalvnqhpi gpfprvqspp hlksppaeap gagaglppps
      721 psehadavga nqhfvlvevh rpdsepdvne vralpqtrta stlsqlsdsg qtlsedsgvd
      781 ageteastsg rgrqtantkn kngkelpqte rttegankpp glleptstli rvrksaatlg
      841 iaieggantr qplprivtiq rggsahncgq lkvghvilev ngqtlrgkeh reaarviaea
      901 fktkerdyid flvtefnvml
//
LOCUS       NP_001099954             759 aa            linear   ROD 28-APR-2025
DEFINITION  fidgetin [Rattus norvegicus].
ACCESSION   NP_001099954 XP_001055272 XP_001055328 XP_229979
VERSION     NP_001099954.1
DBSOURCE    REFSEQ: accession NM_001106484.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Ma,C., Wang,J., Tu,Q., Wu,R., Lai,X., Lin,G., Dong,Z., Guan,T.,
            Qiang,L., Liu,Y. and Liu,M.
  TITLE     Fidgetin impacts axonal growth and branching in a local mTOR signal
            dependent manner
  JOURNAL   Exp Neurol 361, 114315 (2023)
   PUBMED   36586551
  REMARK    GeneRIF: Fidgetin impacts axonal growth and branching in a local
            mTOR signal dependent manner.
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Yang,Y., Mahaffey,C.L., Berube,N. and Frankel,W.N.
  TITLE     Interaction between fidgetin and protein kinase A-anchoring protein
            AKAP95 is critical for palatogenesis in the mouse
  JOURNAL   J Biol Chem 281 (31), 22352-22359 (2006)
   PUBMED   16751186
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473949.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001055272.1, XP_001055328.1, XP_229979.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760396,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..759
                     /product="fidgetin"
                     /calculated_mol_wt=81956
     Region          487..650
                     /region_name="RecA-like_fidgetin"
                     /note="ATPase domain of fidgetin; cd19523"
                     /db_xref="CDD:410931"
     Site            order(488..491,528..534)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:410931"
     Region          675..>706
                     /region_name="AAA_lid_3"
                     /note="AAA+ lid domain; pfam17862"
                     /db_xref="CDD:465537"
     Region          <723..756
                     /region_name="Vps4_C"
                     /note="Vps4 C terminal oligomerization domain; pfam09336"
                     /db_xref="CDD:462762"
     CDS             1..759
                     /gene="Fign"
                     /coded_by="NM_001106484.1:315..2594"
                     /db_xref="GeneID:295649"
                     /db_xref="RGD:1308174"
ORIGIN      
        1 misstsvygl kmqwtpehaq wpeqhfdits ttrspahkve ayrghlqrty qyawanddis
       61 altasnllkk yaekysgile gpvdrpvlsn ysdtpsglvn grkndsepwq sslnseavyp
      121 mncvpdvita skagvssalp pvdvsasigs spgvasnlte psyssstcgs htvpslhagl
      181 psqeyapgyn gsylhstyss qptpalpsph psplhssgll qppppppppp alvpgyngts
      241 nlssysypsa syppqtavgs gyspggappp psaylpsgip aptplppttv pgytyqghgl
      301 tpiapsaltn ssasslkrka fymagqgdmd ssygnysygq qrstqspmyr mpdnsisnsn
      361 rgngfdrnae tsslafkptk qlmpseqqrk fssqssralt ppsystakns lgsrssesfg
      421 kytspvmseh gddhrqllah piqgpglraa tssnhsvdeq lkntdthlid lvtneiitqg
      481 ppvdwsdiag ldlvkavike evlwpvlrsd afsgltalpr sillfgprgt gktllgrcia
      541 sqlgatffki agsglvakwl geaekiihas flvarcrqps vifvsdidml lssqvseehs
      601 pvsrmrtefl mqldtvltsa edqivvicat skpeeidesl rryfmkrlli plpdstarhq
      661 iivqllsqhn yclndkefal lvqrtegfsg ldvahlcqea avgplhampa tdlsaimpsq
      721 lrpityqdfe nafckiqpsi sqkeldmyve wnkmfgcsq
//
LOCUS       NP_001101946             177 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 428 isoform b [Rattus norvegicus].
ACCESSION   NP_001101946 XP_001068393 XP_341802
VERSION     NP_001101946.1
DBSOURCE    REFSEQ: accession NM_001108476.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001068393.1, XP_341802.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP482613.1, SRR22399484.831385.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..177
                     /product="zinc finger protein 428 isoform b"
                     /calculated_mol_wt=19014
     CDS             1..177
                     /gene="Zfp428"
                     /gene_synonym="RGD1564862"
                     /coded_by="NM_001108476.2:473..1006"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:361519"
                     /db_xref="RGD:1564862"
ORIGIN      
        1 mtetreptet ggyasleedd edlspepdse eeeeeeeeee ttddpeydpg ykvkqriggg
       61 rggpsrrapr atqpagppaq pcqlcgrsal geappgtppc rlccpatatq eapapesral
      121 geeeeepsrt genrpagrdg dededeggty hctecedsfd nlgelhghfm lhargev
//
LOCUS       NP_001388300             914 aa            linear   ROD 28-APR-2025
DEFINITION  tetratricopeptide repeat protein 7B isoform 1 [Rattus norvegicus].
ACCESSION   NP_001388300
VERSION     NP_001388300.1
DBSOURCE    REFSEQ: accession NM_001401371.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Baskin,J.M., Wu,X., Christiano,R., Oh,M.S., Schauder,C.M.,
            Gazzerro,E., Messa,M., Baldassari,S., Assereto,S., Biancheri,R.,
            Zara,F., Minetti,C., Raimondi,A., Simons,M., Walther,T.C.,
            Reinisch,K.M. and De Camilli,P.
  TITLE     The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P
            synthesis at the plasma membrane
  JOURNAL   Nat Cell Biol 18 (1), 132-138 (2016)
   PUBMED   26571211
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Nakatsu,F., Baskin,J.M., Chung,J., Tanner,L.B., Shui,G., Lee,S.Y.,
            Pirruccello,M., Hao,M., Ingolia,N.T., Wenk,M.R. and De Camilli,P.
  TITLE     PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its
            impact on plasma membrane identity
  JOURNAL   J Cell Biol 199 (6), 1003-1016 (2012)
   PUBMED   23229899
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.18437.1,
                                           SRR26643295.26298.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..914
                     /product="tetratricopeptide repeat protein 7B isoform 1"
                     /note="tetratricopeptide repeat protein 7B"
                     /calculated_mol_wt=101722
     Region          1..386
                     /region_name="TTC7_N"
                     /note="Tetratricopeptide repeat protein 7 N-terminal;
                     pfam19440"
                     /db_xref="CDD:466084"
     Region          365..391
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          371..611
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          431..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          549..577
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          766..>899
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          767..795
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          801..829
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(802,805..806,809..810,812,836,839..840,843..844,
                     846..847,870,873..874,877..878,881)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          834..864
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          869..897
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..914
                     /gene="Ttc7b"
                     /coded_by="NM_001401371.1:147..2891"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362768"
                     /db_xref="RGD:1305920"
ORIGIN      
        1 matrkagsrl eteiercrse cqweripelv kqlsaklian ddmaelllge skleqhlkek
       61 plrqgasprg prpqltevrk hltaaldrgn lkseflqesn lvmaklnyve gdykealniy
      121 arvglddlpl mavppyrlrm iaeayatkgl cleklpvsss tsnlhvdreq dvitcyekag
      181 diallylqei erviltniqn rspkpgpaph dqelgfflet glqrahvlyf kngnltrgvg
      241 rfrellrave trttqnlrmt iarqlaeill rgmceqsywn pleeppcqsp lddplrkgan
      301 tktytlprra rvysgenifc pqenteeall lllisesman rdavlsripe hksdrlislq
      361 sasvvydllt ialgrrgqye mlsecleram kfafeefhlw yqfalslmaa gksaravkvl
      421 kecirlkpdd atipllaakl cvgslhwlee aekfaktvvd vgektsefka kgylalglty
      481 slqatdaslr gmqevlqrka llalqrahsl sptdhqaafy lalqlaisrq ipealgyvrq
      541 alqlqgddan slhllallls aqkhhhdaln iidmalseyp enfillfskv kleslcrgpd
      601 ealltckhml qiwkscynlt npsdsgrgss lldrtiadrr qlntitlpdf sdpetvsdss
      661 ssssisrtes plhlfvsspl hshpkpdifv wppaahslsd pgphrepslc nspeahfhgf
      721 pslfsvssvh atsvaasrve qalsevassl qssapkqgpl hpwmtlaqiw lhaaevyigi
      781 gkpaeatact qeaanlfpms hnvlymrgqv aelrgnfdea rrwyeealsi spthvksmqr
      841 lalvlhqlgr yslaekilrd avqvnstahe vwnglgevlq aqgndaaate cfltalelea
      901 sspavpftvi prvl
//
LOCUS       NP_001399833             227 aa            linear   ROD 28-APR-2025
DEFINITION  transmembrane protein 40 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001399833
VERSION     NP_001399833.1
DBSOURCE    REFSEQ: accession NM_001412904.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.19328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..227
                     /product="transmembrane protein 40 isoform 2"
                     /calculated_mol_wt=24870
     Region          107..226
                     /region_name="TMEM40"
                     /note="Transmembrane protein 40 family; pfam15817"
                     /db_xref="CDD:464892"
     CDS             1..227
                     /gene="Tmem40"
                     /gene_synonym="RGD1306976"
                     /coded_by="NM_001412904.1:45..728"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:680858"
                     /db_xref="RGD:1587025"
ORIGIN      
        1 measgsssqs pnssavhret edlnhpetef hkqhgkarer yerdksssss ssssssssss
       61 sssssssssd ssdedkhsrg prkhrrkshr dsspgadhge levlkdelql yggaagemvl
      121 agesglrrrg sgsaegevea sqlnrlnikk ddeffhfvll cfaigallvc yhyysdwfms
      181 lgvglltfas letigiyfgl vyrihsvlqg fipllqkfrl pgfrrtn
//
LOCUS       NP_001420991             379 aa            linear   ROD 28-APR-2025
DEFINITION  Golgi-associated RAB2 interactor protein 2 isoform 8 [Rattus
            norvegicus].
ACCESSION   NP_001420991 XP_017449748
VERSION     NP_001420991.1
DBSOURCE    REFSEQ: accession NM_001434062.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 18, 2024 this sequence version replaced XP_017449748.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2956305.1,
                                           SRR26360181.1822637.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..379
                     /product="Golgi-associated RAB2 interactor protein 2
                     isoform 8"
                     /note="family with sequence similarity 71, member D;
                     Golgi-associated RAB2 interactor protein 2"
                     /calculated_mol_wt=43127
     Region          115..185
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     CDS             1..379
                     /gene="Garin2"
                     /gene_synonym="Fam71d"
                     /coded_by="NM_001434062.1:233..1372"
                     /note="isoform 8 is encoded by transcript variant 11"
                     /db_xref="GeneID:366671"
                     /db_xref="RGD:1564393"
ORIGIN      
        1 mkknkskskk lvnkqdalci phyyrlghlk nildggeyap yvsppilesn fiqvnrrges
       61 iylhnranwv tvgicssnhv fktpnmmlla hlttearkeq eplfktilks sspgnlvltr
      121 fiplqfvtis vhsaknmrlk vklingrsyy lqlcapmykq diifsqwvdl ipllnqekak
      181 ttqvseissl seitnstdit gslditdita lpelqtmcsk tqrcpcnime sedfseytda
      241 tdvtdvtdvl enevtdvqdi kivtevtevs evqistnvsg vkivfenddi iknkqeekdn
      301 nlkhrslrdt ktkndyrdsp khvsisnrtl aledeetfqt tltpvksked ickeiydets
      361 eekmislqnt hlkatesrw
//
LOCUS       NP_001316831            2552 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin specific peptidase 9, Y-linked [Rattus norvegicus].
ACCESSION   NP_001316831
VERSION     NP_001316831.1
DBSOURCE    REFSEQ: accession NM_001329902.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2552)
  AUTHORS   Bellott,D.W., Hughes,J.F., Skaletsky,H., Brown,L.G., Pyntikova,T.,
            Cho,T.J., Koutseva,N., Zaghlul,S., Graves,T., Rock,S.,
            Kremitzki,C., Fulton,R.S., Dugan,S., Ding,Y., Morton,D., Khan,Z.,
            Lewis,L., Buhay,C., Wang,Q., Watt,J., Holder,M., Lee,S.,
            Nazareth,L., Alfoldi,J., Rozen,S., Muzny,D.M., Warren,W.C.,
            Gibbs,R.A., Wilson,R.K. and Page,D.C.
  TITLE     Mammalian Y chromosomes retain widely expressed dosage-sensitive
            regulators
  JOURNAL   Nature 508 (7497), 494-499 (2014)
   PUBMED   24759411
  REMARK    Erratum:[Nature. 2014 Oct 2;514(7520):126. Alfoldi, Jessica
            [added]]
REFERENCE   2  (residues 1 to 2552)
  AUTHORS   Cortez,D., Marin,R., Toledo-Flores,D., Froidevaux,L., Liechti,A.,
            Waters,P.D., Grutzner,F. and Kaessmann,H.
  TITLE     Origins and functional evolution of Y chromosomes across mammals
  JOURNAL   Nature 508 (7497), 488-493 (2014)
   PUBMED   24759410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from JF827152.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JF827152.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2552
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="Y"
                     /map="Yq11"
     Protein         1..2552
                     /product="ubiquitin specific peptidase 9, Y-linked"
                     /note="probable ubiquitin carboxyl-terminal hydrolase
                     FAF-X"
                     /calculated_mol_wt=291724
     Region          881..964
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          1554..1957
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(1560,1565,1878,1901)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          2094..2476
                     /region_name="DUF3517"
                     /note="Domain of unknown function (DUF3517); pfam12030"
                     /db_xref="CDD:463438"
     CDS             1..2552
                     /gene="Usp9y"
                     /coded_by="NM_001329902.1:417..8075"
                     /db_xref="GeneID:103694559"
                     /db_xref="RGD:9087771"
ORIGIN      
        1 mtvttrgspv genesqgqap dgqsqpsfqq nqisssdssn enspatppde qgqgdappqh
       61 eeedptfpha dlakledmin rprwvvpvlp kgelevllea sidltkkgid akseacqrff
      121 rdvltvsftk iltdeavsgw kfeihrciin nthrlmelcv aklsqdwfpf lellaialnp
      181 hckfhvynga rpcesvsssv qfpedelfac spdlrspkgw lvdlintfgt lngfqilhdr
      241 fisgsalnvq tiaalikpfg qcceyltqht lkkyfipvie vvpqllqklt neelkkeakt
      301 evkndaismi ikflknlasr ipgqeetvkn leifrlkmil rllqissfng kmnalneink
      361 vlssvsyyth rhgnseeewl taermaewiq qnnilsivlq dslhqpqyve klekilrfvi
      421 kekaltlqdl nniwaaqagk heaivknvhd llaklawdfs peqldhlfdc fkaswtnask
      481 kqreklleli rrlaeddkdg vmaqkvlnll wnlahsddvp vdimdlalsa hikildyscs
      541 qdrdtqkiqw idcfieefrt nnkwvipalk qikeicslfg eapqnlsqth rsphvfyrhd
      601 lisqlqhnha lvtlvaenla tymnsirlya rdhedydpqt irlgsryshv qevqerlnfl
      661 rfllkdgqlw lcasqakqiw hclaenavyf sdreacfmwy sklmgdepdl dpdinkeffe
      721 snvlqldpsl ltengikcfe rffktvncre gklmikrkvy mmddldligl dylwkvviqs
      781 nddisnraid llkeiytslg prlqanqvvi hedfiqscfd rmkssydtlh vldsdkdnif
      841 scarqeairi vriltvlrey isecdsdyhe ermilpmsra frgkhlsltv rfpnqskevd
      901 dldilshtna tigsvrrcil nrinanvtht kielfiggel idseddrklv eqlnlkdksl
      961 itakflqins nmpsspdsss dssagspgnh chnnyrdvpn semenclpgv imslqpryis
     1021 flwqvadlgs mltmptlrdg arilmklmpp dnttienlra vcsdhlnlge rrlgqslhsl
     1081 ffgssaskvl yltevvyill mpagahladi ssdfqyhflk ngglplvlsm liqnnflpnt
     1141 dvetrrdayf salkiaklll ttigyghvqa iaeacqpvad gtdpktpinq athdqavvlq
     1201 nalqsipnps secmlrnvsi rlahqisgla sryipdicvi raiqkiiwts gcgslelvfs
     1261 pheditktyk mttstrsnpe vkdeqvccea levmtlcfal iptaldslsk ekawqsfvid
     1321 lllycpskti rqlaqeqffl ictrccmghr pllffitllf tilgsaatek gkhsdvyfpl
     1381 lrrlltyayn snihipnvdv llndeinwlk rvrdyikntg etsvedpile ghlgvtkell
     1441 sfqtpdkkyh igckagganl vkeliddfif paskaylqys rsgempnkqt ipvcgspatv
     1501 nagfellval afgcvrnlkq ivncltemfy igtpvntlae weylppvgpr ppkgfvglkn
     1561 agatcymnsv iqqlymipsi rnsilaieni wndtdddtfk derqdsenni dprddvfgyp
     1621 hqfedkptln kaedrkdyni gvlkhlqitf ghlaasqlqy yvprgfwqqf rlwgepvnlr
     1681 eqhdaleffn slvdsldeaf kalghptlls kvlggsfadq kicqgcphry eceesfttln
     1741 vdirnhqnll dsleqyikgd lleganayhc ekcdkkvdtv krllikklps vlaiqlkrfd
     1801 ydwerecaik fndyfefpre ldmepytvag atklegdgvh pqtqlikqne qsenvvpgst
     1861 kyrlvgvlvh sgqangghyy syiiqrngkd nnrgrwfkfd dgdvteckmd ddeemknqcf
     1921 ggeymgevfd hmmkrmsyrr qkrwwnayil fyermditde dnemitylse ltitrphqim
     1981 spaiersvwk qnvqflhnqm qfsleyfqfi kklltcnavy lnpapgqdhl ppeaeditmi
     2041 siqlaarflf ttgfhtkkiv rgpandwyda lcillrhskn vrfwfahnvl fnvsnrfsey
     2101 llecpsaevr gtfaklivfi ahfslqdgss ssfaspfatp gpysqiydnl slsdhllkav
     2161 lsllrrevse hgrhlqqyfn lfimyaslgl aektqllkln vpttfmlvsl degpgppiky
     2221 qyaelgklhs vvsqlirccs vssrmqssin gnpplpnpfg dpnlsqpimp iqqnvadilf
     2281 mrttyvkkii edcsnseetv kllrfccwen pqfscsvlse llwqgaysya yelqpyldll
     2341 lqiilledsw qahrihnalk gipsdrdglf dtiqhfknhh qkrayqcikw mvtlfnscpv
     2401 ayqilqgngd lkkkwtwave wlgdelerkp ysgnphytys nwsppiqsne tangyflers
     2461 hsarmtlaka cdlcpeedtd dqdapdehes papqertfyl yshrsqyqqs yvpeqpysgl
     2521 tehhlnepqk ndepqethes seeessslik dq
//
LOCUS       NP_001388214             531 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 18 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001388214
VERSION     NP_001388214.1
DBSOURCE    REFSEQ: accession NM_001401285.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Yang,H., Zhang,Z., Ding,X., Jiang,X., Tan,L., Lin,C., Xu,L., Li,G.,
            Lu,L., Qin,Z., Feng,X. and Li,M.
  TITLE     RP58 knockdown contributes to hypoxia-ischemia-induced pineal
            dysfunction and circadian rhythm disruption in neonatal rats
  JOURNAL   J Pineal Res 75 (1), e12885 (2023)
   PUBMED   37183291
  REMARK    GeneRIF: RP58 knockdown contributes to hypoxia-ischemia-induced
            pineal dysfunction and circadian rhythm disruption in neonatal
            rats.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Enzo,E., Santinon,G., Pocaterra,A., Aragona,M., Bresolin,S.,
            Forcato,M., Grifoni,D., Pession,A., Zanconato,F., Guzzo,G.,
            Bicciato,S. and Dupont,S.
  TITLE     Aerobic glycolysis tunes YAP/TAZ transcriptional activity
  JOURNAL   EMBO J 34 (10), 1349-1370 (2015)
   PUBMED   25796446
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Okado,H., Ohtaka-Maruyama,C., Sugitani,Y., Fukuda,Y., Ishida,R.,
            Hirai,S., Miwa,A., Takahashi,A., Aoki,K., Mochida,K., Suzuki,O.,
            Honda,T., Nakajima,K., Ogawa,M., Terashima,T., Matsuda,J.,
            Kawano,H. and Kasai,M.
  TITLE     The transcriptional repressor RP58 is crucial for cell-division
            patterning and neuronal survival in the developing cortex
  JOURNAL   Dev Biol 331 (2), 140-151 (2009)
   PUBMED   19409883
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Takahashi,A., Hirai,S., Ohtaka-Maruyama,C., Miwa,A., Hata,Y.,
            Okabe,S. and Okado,H.
  TITLE     Co-localization of a novel transcriptional repressor simiRP58 with
            RP58
  JOURNAL   Biochem Biophys Res Commun 368 (3), 637-642 (2008)
   PUBMED   18262495
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Kang,J.S., Yang,Y.C., Liu,H.L., Li,Y.H., Du,Y.C. and Li,R.X.
  TITLE     Cloning and Distribution of rRP58, A Novel Neuronal Gene
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 33 (5),
            563-568 (2001)
   PUBMED   12040400
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Meng,G., Inazawa,J., Ishida,R., Tokura,K., Nakahara,K., Aoki,K. and
            Kasai,M.
  TITLE     Structural analysis of the gene encoding RP58, a sequence-specific
            transrepressor associated with heterochromatin
  JOURNAL   Gene 242 (1-2), 59-64 (2000)
   PUBMED   10721697
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Aoki,K., Meng,G., Suzuki,K., Takashi,T., Kameoka,Y., Nakahara,K.,
            Ishida,R. and Kasai,M.
  TITLE     RP58 associates with condensed chromatin and mediates a
            sequence-specific transcriptional repression
  JOURNAL   J Biol Chem 273 (41), 26698-26704 (1998)
   PUBMED   9756912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1105680.1, BG376882.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q25"
     Protein         1..531
                     /product="zinc finger and BTB domain-containing protein 18
                     isoform 2"
                     /note="rRP58; 58 kDa repressor protein; zinc finger
                     protein 238; transcriptional repressor RP58; zinc finger
                     and BTB domain-containing protein 18"
                     /calculated_mol_wt=59193
     Region          10..156
                     /region_name="BTB_POZ_ZBTB18_RP58"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 18 (ZBTB18); cd18324"
                     /db_xref="CDD:349633"
     Region          <360..>490
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(381,384,397,401)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(421,424,437,441)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(426,428,430,432..433,436..437,440,454,456,460..461,
                     464..465,468,482,484,486,488..489,492..493)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          434..456
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..495
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..531
                     /gene="Zbtb18"
                     /gene_synonym="Rp58; Zfp238; Znf238"
                     /coded_by="NM_001401285.1:150..1745"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64619"
                     /db_xref="RGD:621548"
ORIGIN      
        1 mcpkgyedsm efpdhsrhll qclseqrhqg flcdctvlvg daqfrahrav lascsmyfhl
       61 fykdqldkrd ivhlnsdivt apafalllef myegklqfkd lpiedvlaaa sylhmydivk
      121 vckkklkeka tteadstkke edasscsdkv eslsdgsshm agdlpsdede geddklnilp
      181 skrdlaaepg nmwmrlpsda agipqaggea ephataagkt vaspcsstes lsqrsvtsvr
      241 dsadvdcvld lsvksslsgv enlnssyfss qdvlrsnlvq vkvekeascd esdvgtndyd
      301 mehstvkesv sannrvqyep ahlaplreds vlreldredk asddemmtpe servqveggm
      361 essllpyvsn ilspagqifm cplcnkvfps philqihlst hfreqdgirs kpaadvnvpt
      421 cslcgktfsc mytlkrhert hsgekpytct qcgksfqysh nlsrhavvht rekphackwc
      481 errftqsgdl yrhirkfhce lvnslsvkse alslptvrdw tledssqelw k
//
LOCUS       NP_001421483             531 aa            linear   ROD 28-APR-2025
DEFINITION  heat shock factor protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001421483 XP_006256567
VERSION     NP_001421483.1
DBSOURCE    REFSEQ: accession NM_001434554.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Kanugovi Vijayavittal,A., Kumar,P., Sugunan,S., Joseph,C.,
            Devaki,B., Paithankar,K. and Amere Subbarao,S.
  TITLE     Heat shock transcription factor HSF2 modulates the autophagy
            response through the BTG2-SOD2 axis
  JOURNAL   Biochem Biophys Res Commun 600, 44-50 (2022)
   PUBMED   35182974
  REMARK    GeneRIF: Heat shock transcription factor HSF2 modulates the
            autophagy response through the BTG2-SOD2 axis.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Huang,C.Y., Chen,J.Y., Kuo,C.H., Pai,P.Y., Ho,T.J., Chen,T.S.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     Mitochondrial ROS-induced ERK1/2 activation and HSF2-mediated AT1 R
            upregulation are required for doxorubicin-induced cardiotoxicity
  JOURNAL   J Cell Physiol 233 (1), 463-475 (2018)
   PUBMED   28295305
  REMARK    GeneRIF: DOX induced mitochondrial ROS release to activate
            ERK1/2-mediated HSF2 nuclear translocation and AT1 R upregulation
            causing DOX-damaged heart failure in vitro and in vivo.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Huang,C.Y., Pai,P.Y., Kuo,C.H., Ho,T.J., Lin,J.Y., Lin,D.Y.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     p53-mediated miR-18 repression activates HSF2 for IGF-IIR-dependent
            myocyte hypertrophy in hypertension-induced heart failure
  JOURNAL   Cell Death Dis 8 (8), e2990 (2017)
   PUBMED   28796250
  REMARK    GeneRIF: p53-mediated miR-18 repression activates HSF2 for
            IGF-IIR-dependent myocyte hypertrophy in hypertension-induced heart
            failure
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Liu,F., Xu,Z.L., Qian,X.J., Qiu,W.Y. and Huang,H.
  TITLE     Expression of Hsf1, Hsf2, and Phlda1 in cells undergoing
            cryptorchid-induced apoptosis in rat testes
  JOURNAL   Mol Reprod Dev 78 (4), 283-291 (2011)
   PUBMED   21480429
  REMARK    GeneRIF: The Hsf2 is mainly expressed in round spermatids in
            control testis. Hsf2 expression is significantly increased in both
            nuclei and cytoplasm of spermatocytes in 7-day cryptorchid testis.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Fujimoto,M., Oshima,K., Shinkawa,T., Wang,B.B., Inouye,S.,
            Hayashida,N., Takii,R. and Nakai,A.
  TITLE     Analysis of HSF4 binding regions reveals its necessity for gene
            regulation during development and heat shock response in mouse
            lenses
  JOURNAL   J Biol Chem 283 (44), 29961-29970 (2008)
   PUBMED   18755693
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Kwong,J.M., Lalezary,M., Nguyen,J.K., Yang,C., Khattar,A., Piri,N.,
            Mareninov,S., Gordon,L.K. and Caprioli,J.
  TITLE     Co-expression of heat shock transcription factors 1 and 2 in rat
            retinal ganglion cells
  JOURNAL   Neurosci Lett 405 (3), 191-195 (2006)
   PUBMED   16889897
  REMARK    GeneRIF: both heat shock transcription 2 is linked to the heat
            shock response in retinal ganglion cells.
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Wang,G., Ying,Z., Jin,X., Tu,N., Zhang,Y., Phillips,M.,
            Moskophidis,D. and Mivechi,N.F.
  TITLE     Essential requirement for both hsf1 and hsf2 transcriptional
            activity in spermatogenesis and male fertility
  JOURNAL   Genesis 38 (2), 66-80 (2004)
   PUBMED   14994269
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Min,J.N., Han,M.Y., Lee,S.S., Kim,K.J. and Park,Y.M.
  TITLE     Regulation of rat heat shock factor 2 expression during the early
            organogenic phase of embryogenesis
  JOURNAL   Biochim Biophys Acta 1494 (3), 256-262 (2000)
   PUBMED   11121583
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Eriksson,M., Jokinen,E., Sistonen,L. and Leppa,S.
  TITLE     Heat shock factor 2 is activated during mouse heart development
  JOURNAL   Int J Dev Biol 44 (5), 471-477 (2000)
   PUBMED   11032181
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Kubota,H., Matsumoto,S., Yokota,S., Yanagi,H. and Yura,T.
  TITLE     Transcriptional activation of mouse cytosolic chaperonin CCT
            subunit genes by heat shock factors HSF1 and HSF2
  JOURNAL   FEBS Lett 461 (1-2), 125-129 (1999)
   PUBMED   10561509
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Nov 13, 2024 this sequence version replaced XP_006256567.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.67022.1,
                                           SRR26643297.53474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..531
                     /product="heat shock factor protein 2 isoform 2"
                     /note="heat shock factor 2; heat shock factor protein 2;
                     heat shock transcription factor hsf2"
                     /calculated_mol_wt=59668
     Region          6..110
                     /region_name="HSF"
                     /note="heat shock factor; smart00415"
                     /db_xref="CDD:214654"
     Region          230..496
                     /region_name="Vert_HS_TF"
                     /note="Vertebrate heat shock transcription factor;
                     pfam06546"
                     /db_xref="CDD:461944"
     CDS             1..531
                     /gene="Hsf2"
                     /coded_by="NM_001434554.1:95..1690"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64441"
                     /db_xref="RGD:68395"
ORIGIN      
        1 mkqssnvpaf lsklwtlvee thtnefitws qngqsflvld eqrfakeilp kyfkhnnmas
       61 fvrqlnmygf rkvvhiesgi vkqerdgpve fqhphfkqgq ddllenikrk vssskpeenk
      121 irqedltkii ssaqkvqikq etiesrlsel kseneslwke vselrakhaq qqqvirkivq
      181 fivtlvqnnq lvslkrkrpl llntngapkk nlfqhivkep tdnhhhkvph srteglksre
      241 risddiiiyd vtednvdeen ipvipetned vvvdpssqyp diviveddne deyapviqsg
      301 eqseparvgs assssplmss avqlngssnl tsedpvtmmd silndninll gkvelldyld
      361 sidcsledfq amlsgrqfsi dpdllvdlft ssvqmnptdy inntksenkg leatknsvvq
      421 qvseegrksk skpdkqliqy tafpllafld gnpasaveqg tttassevvp svdkpievde
      481 lldsnldqep tqsklvrlep lteaeaseat lfylcelapa pldsdmplld s
//
LOCUS       NP_001402762             603 aa            linear   ROD 28-APR-2025
DEFINITION  grainyhead-like protein 3 homolog isoform 1 [Rattus norvegicus].
ACCESSION   NP_001402762 XP_008762438
VERSION     NP_001402762.1
DBSOURCE    REFSEQ: accession NM_001415833.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Gordon,W.M., Zeller,M.D., Klein,R.H., Swindell,W.R., Ho,H.,
            Espetia,F., Gudjonsson,J.E., Baldi,P.F. and Andersen,B.
  TITLE     A GRHL3-regulated repair pathway suppresses immune-mediated
            epidermal hyperplasia
  JOURNAL   J Clin Invest 124 (12), 5205-5218 (2014)
   PUBMED   25347468
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Haendeler,J., Mlynek,A., Buchner,N., Lukosz,M., Graf,M.,
            Guettler,C., Jakob,S., Farrokh,S., Kunze,K., Goy,C.,
            Guardiola-Serrano,F., Schaal,H., Cortese-Krott,M., Deenen,R.,
            Kohrer,K., Winkler,C. and Altschmied,J.
  TITLE     Two isoforms of Sister-Of-Mammalian Grainyhead have opposing
            functions in endothelial cells and in vivo
  JOURNAL   Arterioscler Thromb Vasc Biol 33 (7), 1639-1646 (2013)
   PUBMED   23685552
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Brouns,M.R., De Castro,S.C., Terwindt-Rouwenhorst,E.A., Massa,V.,
            Hekking,J.W., Hirst,C.S., Savery,D., Munts,C., Partridge,D.,
            Lamers,W., Kohler,E., van Straaten,H.W., Copp,A.J. and Greene,N.D.
  TITLE     Over-expression of Grhl2 causes spina bifida in the Axial defects
            mutant mouse
  JOURNAL   Hum Mol Genet 20 (8), 1536-1546 (2011)
   PUBMED   21262862
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Boglev,Y., Wilanowski,T., Caddy,J., Parekh,V., Auden,A., Darido,C.,
            Hislop,N.R., Cangkrama,M., Ting,S.B. and Jane,S.M.
  TITLE     The unique and cooperative roles of the Grainy head-like
            transcription factors in epidermal development reflect unexpected
            target gene specificity
  JOURNAL   Dev Biol 349 (2), 512-522 (2011)
   PUBMED   21081122
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Rifat,Y., Parekh,V., Wilanowski,T., Hislop,N.R., Auden,A.,
            Ting,S.B., Cunningham,J.M. and Jane,S.M.
  TITLE     Regional neural tube closure defined by the Grainy head-like
            transcription factors
  JOURNAL   Dev Biol 345 (2), 237-245 (2010)
   PUBMED   20654612
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Yu,Z., Lin,K.K., Bhandari,A., Spencer,J.A., Xu,X., Wang,N., Lu,Z.,
            Gill,G.N., Roop,D.R., Wertz,P. and Andersen,B.
  TITLE     The Grainyhead-like epithelial transactivator Get-1/Grhl3 regulates
            epidermal terminal differentiation and interacts functionally with
            LMO4
  JOURNAL   Dev Biol 299 (1), 122-136 (2006)
   PUBMED   16949565
REFERENCE   7  (residues 1 to 603)
  AUTHORS   Ting,S.B., Caddy,J., Hislop,N., Wilanowski,T., Auden,A., Zhao,L.L.,
            Ellis,S., Kaur,P., Uchida,Y., Holleran,W.M., Elias,P.M.,
            Cunningham,J.M. and Jane,S.M.
  TITLE     A homolog of Drosophila grainy head is essential for epidermal
            integrity in mice
  JOURNAL   Science 308 (5720), 411-413 (2005)
   PUBMED   15831758
REFERENCE   8  (residues 1 to 603)
  AUTHORS   Ting,S.B., Wilanowski,T., Auden,A., Hall,M., Voss,A.K., Thomas,T.,
            Parekh,V., Cunningham,J.M. and Jane,S.M.
  TITLE     Inositol- and folate-resistant neural tube defects in mice lacking
            the epithelial-specific factor Grhl-3
  JOURNAL   Nat Med 9 (12), 1513-1519 (2003)
   PUBMED   14608380
REFERENCE   9  (residues 1 to 603)
  AUTHORS   Kudryavtseva,E.I., Sugihara,T.M., Wang,N., Lasso,R.J.,
            Gudnason,J.F., Lipkin,S.M. and Andersen,B.
  TITLE     Identification and characterization of Grainyhead-like epithelial
            transactivator (GET-1), a novel mammalian Grainyhead-like factor
  JOURNAL   Dev Dyn 226 (4), 604-617 (2003)
   PUBMED   12666198
REFERENCE   10 (residues 1 to 603)
  AUTHORS   Hall,M., Gofflot,F., Iseki,S. and Morriss-Kay,G.M.
  TITLE     Effects of the curly tail genotype on neuroepithelial integrity and
            cell proliferation during late stages of primary neurulation
  JOURNAL   J Anat 199 (Pt 6), 645-655 (2001)
   PUBMED   11787818
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 3, 2023 this sequence version replaced XP_008762438.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.14625.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418971 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..603
                     /product="grainyhead-like protein 3 homolog isoform 1"
                     /note="transcription factor CP2-like 4; grainyhead-like
                     protein 3 homolog; grainyhead-like 3"
                     /calculated_mol_wt=67755
     Region          219..421
                     /region_name="CP2"
                     /note="CP2 transcription factor; pfam04516"
                     /db_xref="CDD:461338"
     CDS             1..603
                     /gene="Grhl3"
                     /gene_synonym="Tfcp2l4"
                     /coded_by="NM_001415833.1:208..2019"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298555"
                     /db_xref="RGD:1308320"
ORIGIN      
        1 msneldfrsv rllkndpvsf qkfpynnede awktylenpl taatkaimrv ngddesvaal
       61 sflydyymgp kekrilssst ggrndqgkky yhsmdyepdl aplespthlm kfltenvsgs
      121 pdytdqlkkn nllglegalp tpgktstlpp gpskleagsm dsyllptsdm ydnsslnslf
      181 esihgvpptq rwqpdstfkd dpqesllfpd ilktspeapc pedypslksd feytlgspka
      241 ihikagespm aylnkgqfyp vtlrtpaggk glslssskvk svvmivfdnd kvpveqlrfw
      301 rhwhsrqpta kqrvidvadc kenfntvqhi eevaynalsf vwnvneeakv figvnclstd
      361 fssqkgvkgv plnlqidtyd cgagterlvh ravcqikifc dkgaerkmrd derkqfrrkv
      421 kcpdssnnag ikgcllsgfr gnettylrpe adletqpvlf ipnlhfsslq rpggvvpsag
      481 hsssdrlplk rtcspfaeef eplpskqake ddlqrvllyv rreteevfda lmlktpdlkg
      541 lrnaisekyg fpeenickvy kkckrgilvn mdnniiqhys nhvaflldmg eldgkiqiil
      601 kel
//
LOCUS       NP_001420978             408 aa            linear   ROD 28-APR-2025
DEFINITION  Golgi-associated RAB2 interactor protein 2 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001420978 XP_038968567
VERSION     NP_001420978.1
DBSOURCE    REFSEQ: accession NM_001434049.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 18, 2024 this sequence version replaced XP_038968567.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1412896.1,
                                           SRR26643293.35898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..408
                     /product="Golgi-associated RAB2 interactor protein 2
                     isoform 4"
                     /note="family with sequence similarity 71, member D;
                     Golgi-associated RAB2 interactor protein 2"
                     /calculated_mol_wt=46254
     Region          115..185
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     CDS             1..408
                     /gene="Garin2"
                     /gene_synonym="Fam71d"
                     /coded_by="NM_001434049.1:233..1459"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:366671"
                     /db_xref="RGD:1564393"
ORIGIN      
        1 mkknkskskk lvnkqdalci phyyrlghlk nildggeyap yvsppilesn fiqvnrrges
       61 iylhnranwv tvgicssnhv fktpnmmlla hlttearkeq eplfktilks sspgnlvltr
      121 fiplqfvtis vhsaknmrlk vklingrsyy lqlcapmykq diifsqwvdl ipllnqekak
      181 ttqvseissl seitnstdit gslditdita lpelqtmcsk tqrcpcnime sedfseytda
      241 tdvtdvtdvl enevtdvqdi kivtevtevs evqistnvsg vkivfenddi iknkqeekdn
      301 nlkhrslrdt ktkndyrdsp khvsisnrtl aledeetfqt tltpvksked ickeiydets
      361 eekmislqnt hlkatesrst rtdsdtsgly sfavfplisi sfpfftll
//
LOCUS       NP_001417165             328 aa            linear   ROD 28-APR-2025
DEFINITION  musashi RNA-binding protein 2 isoform e [Rattus norvegicus].
ACCESSION   NP_001417165 XP_038943595
VERSION     NP_001417165.1
DBSOURCE    REFSEQ: accession NM_001430236.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Sengupta,U., Montalbano,M., McAllen,S., Minuesa,G., Kharas,M. and
            Kayed,R.
  TITLE     Formation of Toxic Oligomeric Assemblies of RNA-binding Protein:
            Musashi in Alzheimer's disease
  JOURNAL   Acta Neuropathol Commun 6 (1), 113 (2018)
   PUBMED   30367664
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Sakakibara,S., Nakamura,Y., Yoshida,T., Shibata,S., Koike,M.,
            Takano,H., Ueda,S., Uchiyama,Y., Noda,T. and Okano,H.
  TITLE     RNA-binding protein Musashi family: roles for CNS stem cells and a
            subpopulation of ependymal cells revealed by targeted disruption
            and antisense ablation
  JOURNAL   Proc Natl Acad Sci U S A 99 (23), 15194-15199 (2002)
   PUBMED   12407178
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Sakakibara,S., Nakamura,Y., Satoh,H. and Okano,H.
  TITLE     Rna-binding protein Musashi2: developmentally regulated expression
            in neural precursor cells and subpopulations of neurons in
            mammalian CNS
  JOURNAL   J Neurosci 21 (20), 8091-8107 (2001)
   PUBMED   11588182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 7, 2024 this sequence version replaced XP_038943595.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.25302.1,
                                           SRR26643296.28148.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..328
                     /product="musashi RNA-binding protein 2 isoform e"
                     /note="Musashi homolog 2; RNA-binding protein Musashi
                     homolog 2"
                     /calculated_mol_wt=34980
     Region          17..109
                     /region_name="RRM1_MSI2"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein Musashi homolog 2 (Musashi-2) and similar
                     proteins; cd12760"
                     /db_xref="CDD:410153"
     Site            order(24,26..30,51,53,62..64,66,89,92,94..97)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410153"
     Region          111..184
                     /region_name="RRM2_MSI"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein Musashi homologs Musashi-1, Musashi-2 and similar
                     proteins; cd12323"
                     /db_xref="CDD:240769"
     CDS             1..328
                     /gene="Msi2"
                     /gene_synonym="RGD1560397"
                     /coded_by="NM_001430236.1:188..1174"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:360596"
                     /db_xref="RGD:1560397"
ORIGIN      
        1 meangspgts gsandsqhdp gkmfigglsw qtspdslrdy fskfgeirec mvmrdpttkr
       61 srgfgfvtfa dpasvdkvlg qphheldskt idpkvafprr aqpkmvtrtk kifvgglsan
      121 tvvedvkqyf eqfgkvedam lmfdkttnrh rgfgfvtfen edvvekvcei hfheinnkmv
      181 eckkaqpkev mfppgtrgra rglpytmdaf mlgmgmlgyp nfvatygrgy pgfapsygyq
      241 fpgfpaaayg pvaaaavaaa rgsgsnparp ggfpganspg pvadlygpas qdsgvgnyis
      301 aaspqpgsgf ghgiasipgc pgktgrsf
//
LOCUS       NP_001013925             323 aa            linear   ROD 28-APR-2025
DEFINITION  transmembrane protein 171 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001013925 XP_215130
VERSION     NP_001013925.2
DBSOURCE    REFSEQ: accession NM_001013903.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Feb 25, 2022 this sequence version replaced NP_001013925.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY185507.1, SRR26360172.756581.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..323
                     /product="transmembrane protein 171 isoform 1"
                     /note="parturition-related protein 2; proline-rich protein
                     PRP2"
                     /calculated_mol_wt=34613
     Region          2..318
                     /region_name="TMEM171"
                     /note="Transmembrane protein family 171; pfam15471"
                     /db_xref="CDD:464734"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     Region          251..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6K0P5.1)"
     CDS             1..323
                     /gene="Tmem171"
                     /gene_synonym="Prp2"
                     /coded_by="NM_001013903.2:115..1086"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293634"
                     /db_xref="RGD:1359492"
ORIGIN      
        1 mssvgtaepd gdqrdrqvsk lifflfvfga vllcvgilis ifgyqacqyk plshcsmvlk
       61 iagpscavmg lgtvilarsr arlqlrerqr qghqdpdqsf fcgesrqfaq clifgflflt
      121 sgmlisilgi wvpgcgsdwa qeplnetnsg egepqicsfl slqimgpliv lvglcffvva
      181 hvkkksnlss srdtseiegg hthstepvhi tvgdsviifp pppppyfaes saaapspgan
      241 slhrienpps ysslfnlsrt ptpenqgaas erdreviyti sgpgsssess htghlpldlp
      301 pryeeketap atplgapses spp
//
LOCUS       NP_001418673             185 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC681385 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001418673 XP_001061529
VERSION     NP_001418673.1
DBSOURCE    REFSEQ: accession NM_001431744.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jul 22, 2024 this sequence version replaced XP_001061529.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.674804.1,
                                           SRR22582416.1196004.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..185
                     /product="uncharacterized protein LOC681385 isoform 1
                     precursor"
                     /note="vomeronasal secretory protein 2; rCG64269-like"
                     /calculated_mol_wt=19531
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2134
     Region          28..173
                     /region_name="lipocalin_1_3_4_13-like"
                     /note="lipocalin-1, -3, -4, -13 and similar proteins;
                     cd19414"
                     /db_xref="CDD:381189"
     Site            order(32,36,47,58,60,68,70,72,83,85,87,96,98,102..103,105,
                     107,116,118,120,129,131,133,135)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381189"
     Site            order(47,83,102..103,129,131)
                     /site_type="other"
                     /note="citrate-binding site [ion binding]"
                     /db_xref="CDD:381189"
     CDS             1..185
                     /gene="Lcn4l2"
                     /coded_by="NM_001431744.1:56..613"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:681385"
                     /db_xref="RGD:1596705"
ORIGIN      
        1 mkyllltvll fgllailqaq ddlpflsdek klsgiwflka tvsqrrqtge qtvvafphsl
       61 tcpeegilei rntfmsggqc ikillrmqkt eepgqysnff rhnlfyiyel pvkdhyifym
      121 esipfekkfq eghligkcpk enlealeefk efiqrkgllq eniivpeqre rcvpihdgah
      181 knhkc
//
LOCUS       NP_598236                865 aa            linear   ROD 28-APR-2025
DEFINITION  carbohydrate-responsive element-binding protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_598236
VERSION     NP_598236.2
DBSOURCE    REFSEQ: accession NM_133552.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Hu,A., Lan,H., Yao,Z. and Kong,X.
  TITLE     Carbohydrate response element-binding protein (ChREBP) mediates
            decreased SNAP25 expression in islets from diabetic Goto-Kakizaki
            (GK) rats
  JOURNAL   FEBS Open Bio 14 (11), 1864-1872 (2024)
   PUBMED   39300600
  REMARK    GeneRIF: Carbohydrate response element-binding protein (ChREBP)
            mediates decreased SNAP25 expression in islets from diabetic
            Goto-Kakizaki (GK) rats.
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Katz,L.S., Brill,G., Wang,P., Lambertini,L., Zhang,P.,
            Haldeman,J.M., Liu,H., Newgard,C.B., Stewart,A.F., Garcia-Ocana,A.
            and Scott,D.K.
  TITLE     Transcriptional activation of the Myc gene by glucose in beta-cells
            requires a ChREBP-dependent 3-D chromatin interaction between the
            Myc and Pvt1 genes
  JOURNAL   Mol Metab 79, 101848 (2024)
   PUBMED   38042369
  REMARK    GeneRIF: Transcriptional activation of the Myc gene by glucose in
            beta-cells requires a ChREBP-dependent 3-D chromatin interaction
            between the Myc and Pvt1 genes.
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Zhan,H., Wang,Y., Yu,S., Cai,G., Zeng,Y., Ma,J., Liu,W. and Wu,W.
  TITLE     Upregulation of Mlxipl induced by cJun in the spinal dorsal horn
            after peripheral nerve injury counteracts mechanical allodynia by
            inhibiting neuroinflammation
  JOURNAL   Aging (Albany NY) 12 (11), 11004-11024 (2020)
   PUBMED   32518215
  REMARK    GeneRIF: Upregulation of Mlxipl induced by cJun in the spinal
            dorsal horn after peripheral nerve injury counteracts mechanical
            allodynia by inhibiting neuroinflammation.
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Han,J.H., Kim,S., Kim,S., Lee,H., Park,S.Y. and Woo,C.H.
  TITLE     FMK, an Inhibitor of p90RSK, Inhibits High Glucose-Induced TXNIP
            Expression via Regulation of ChREBP in Pancreatic beta Cells
  JOURNAL   Int J Mol Sci 20 (18), 4424 (2019)
   PUBMED   31505737
  REMARK    GeneRIF: these findings suggest FMK may protect against HG-induced
            beta-cell dysfunction and TXNIP expression by ChREBP regulation in
            pancreatic beta-cells, and that FMK is a potential therapeutic
            reagent for the drug development of diabetes and its complications.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Van der Werf,R., Walter,C., Bietiger,W., Seyfritz,E., Mura,C.,
            Peronet,C., Legrandois,J., Werner,D., Ennahar,S., Digel,F.,
            Maillard-Pedracini,E., Pinget,M., Jeandidier,N., Marchioni,E.,
            Sigrist,S. and Dal,S.
  TITLE     Beneficial effects of cherry consumption as a dietary intervention
            for metabolic, hepatic and vascular complications in type 2
            diabetic rats
  JOURNAL   Cardiovasc Diabetol 17 (1), 104 (2018)
   PUBMED   30029691
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 865)
  AUTHORS   Kawaguchi,T., Osatomi,K., Yamashita,H., Kabashima,T. and Uyeda,K.
  TITLE     Mechanism for fatty acid 'sparing' effect on glucose-induced
            transcription: regulation of carbohydrate-responsive
            element-binding protein by AMP-activated protein kinase
  JOURNAL   J Biol Chem 277 (6), 3829-3835 (2002)
   PUBMED   11724780
REFERENCE   7  (residues 1 to 865)
  AUTHORS   Yamashita,H., Takenoshita,M., Sakurai,M., Bruick,R.K., Henzel,W.J.,
            Shillinglaw,W., Arnot,D. and Uyeda,K.
  TITLE     A glucose-responsive transcription factor that regulates
            carbohydrate metabolism in the liver
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 9116-9121 (2001)
   PUBMED   11470916
REFERENCE   8  (residues 1 to 865)
  AUTHORS   Cairo,S., Merla,G., Urbinati,F., Ballabio,A. and Reymond,A.
  TITLE     WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted
            region, is a new member of the Mlx transcription factor network
  JOURNAL   Hum Mol Genet 10 (6), 617-627 (2001)
   PUBMED   11230181
REFERENCE   9  (residues 1 to 865)
  AUTHORS   de Luis,O., Valero,M.C. and Jurado,L.A.
  TITLE     WBSCR14, a putative transcription factor gene deleted in
            Williams-Beuren syndrome: complete characterisation of the human
            gene and the mouse ortholog
  JOURNAL   Eur J Hum Genet 8 (3), 215-222 (2000)
   PUBMED   10780788
REFERENCE   10 (residues 1 to 865)
  AUTHORS   Volpe,C.M., Koo,J., Miloro,S.M., Driscoll,D.L., Nava,H.R. and
            Douglass,H.O. Jr.
  TITLE     The effect of extended lymphadenectomy on survival in patients with
            gastric adenocarcinoma
  JOURNAL   J Am Coll Surg 181 (1), 56-64 (1995)
   PUBMED   7599772
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 5, 2021 this sequence version replaced NP_598236.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB074517.1, SRR26643287.27958.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..865
                     /product="carbohydrate-responsive element-binding protein
                     isoform 2"
                     /note="Williams-Beuren syndrome chromosome region 14
                     homolog; carbohydrate-responsive element-binding protein;
                     MLX interactor; class D basic helix-loop-helix protein 14;
                     WS basic-helix-loop-helix leucine zipper protein;
                     Williams-Beuren syndrome chromosomal region 14 protein"
                     /calculated_mol_wt=94849
     Region          15..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          53..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          81..196
                     /region_name="NES2-NLS_ChREBP"
                     /note="nuclear export signal 2 (NES2) and nuclear import
                     signal (NLS) domains found in carbohydrate-responsive
                     element-binding protein (ChREBP), and similar proteins;
                     cd21771"
                     /db_xref="CDD:439287"
     Site            order(117,121,124,127..131,134)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:439287"
     Site            order(124,127..128)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:439287"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          <262..655
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          334..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          500..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:11724780; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            615
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          659..734
                     /region_name="bHLHzip_MLXIPL"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in MLX-interacting protein-like (MLXIPL) and similar
                     proteins; cd19689"
                     /db_xref="CDD:381532"
     Site            order(664,666..668,670..672,674..675,679,701..702)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381532"
     Site            order(678,681..682,684..685,688..690,703,706..707,710,
                     712..714,716..717,719..720,723,726..727,730..731,733..734)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381532"
     Region          716..737
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     CDS             1..865
                     /gene="Mlxipl"
                     /gene_synonym="bHLHd14; ChREBP; Wbscr14; WS-bHLH"
                     /coded_by="NM_133552.2:33..2630"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171078"
                     /db_xref="RGD:620400"
ORIGIN      
        1 maraladlsv nlqvprvvps pdsdsdtdle dpsprrsagg lhrsqvihsg hfmvssphsd
       61 sltrrrdqeg pvgladfgpr sidptltrlf eclslaysgk lvspkwknfk glkllcrdki
      121 rlnnaiwraw yiqyvqrrks pvcgfvtplq gseadehrkp eavvlegnyw krrievvmre
      181 yhkwriyykk rlrkssregd flapkqvegg wppperwceq lfssvvpvll ggseeepggr
      241 qlldldcfls disdtlftmt qpspsslqlp sedayvgnad miqpdltplq pslddfmeis
      301 dfftnyrppq tptssnfpep psfgpmadsl fsggilgpem pspasassss gmtplsgntr
      361 lqarnscsgp ldpstfpsse fllpedpktk mppapvptpl lpypgpvkvh glepctpspf
      421 ptmapppall seeplfsarf pfttvppapg vstlpapttf vptpqpgpvp gpvpfpvdhl
      481 phgylepvfg phftvpqgvq prckpcsppp ggrkaspptl tsatasptat atardnnpcl
      541 tqllraakpe qvlepstvps tllrppespd avpeiprvra fyppipaptp prpppgpatl
      601 apprslvvpk aerlsppass gserrlsgdl nsiqppgals vhlsppqtvl srgrvdnnkm
      661 enrrithisa eqkrrfnikl gfdtlhglvs tlsaqpslkv skattlqkta eyilmlqqer
      721 aamqeeaqql rdeieelnaa inlcqqqlpa tgvpithqrf dqmrdmfddy vrtrtlhnwk
      781 fwvfsilirp lfesfngmvs taslhslrqt slawldqycs lpalrptvln slrqlststs
      841 iltdpslvpe qatravtegp lgrpl
//
LOCUS       NP_001419239             434 aa            linear   ROD 28-APR-2025
DEFINITION  BEN domain-containing protein 7 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419239 XP_038952409
VERSION     NP_001419239.1
DBSOURCE    REFSEQ: accession NM_001432310.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Jul 30, 2024 this sequence version replaced XP_038952409.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.55111.1,
                                           SRR26643288.58182.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..434
                     /product="BEN domain-containing protein 7 isoform 2"
                     /note="BEN domain-containing protein 7"
                     /calculated_mol_wt=48023
     Region          312..391
                     /region_name="BEN"
                     /note="BEN domain; pfam10523"
                     /db_xref="CDD:463133"
     CDS             1..434
                     /gene="Bend7"
                     /gene_synonym="RGD1305898"
                     /coded_by="NM_001432310.1:398..1702"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361275"
                     /db_xref="RGD:1305898"
ORIGIN      
        1 mefserkrsr ksqsfklvsr dyhhevykis efsndvnget ketqpmflgd gsmeikkqit
       61 gmrrllndrt griyqrvgke geklkeepqd vdlvwpqrln ssteapqglh ppsrgawnel
      121 paqsgqfsgq pgprsrtfqs qphisassng elpgvnstag sncctcncqs tlqailqelk
      181 tmrklmhfqa vgtqnrqqpp islvcsqrta isrkrnkkkk vlpkavepmt tvkpkpspse
      241 tekkpaavaa rppglqaaec asaeenhilg fgivlkspss dpevqlaegf dvfmpksqld
      301 silsnytrsg sllfrklvca ffddktlans lpngkrkrgl ndnrkgldqn ivgaikvfte
      361 nyctanhvdk lpgprdwvqi lqdqiklarr rlkrgsaeva dgderldgis lpptghafvs
      421 rretpedpep gsia
//
LOCUS       NP_001005889             583 aa            linear   ROD 28-APR-2025
DEFINITION  radixin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001005889 XP_236234
VERSION     NP_001005889.2
DBSOURCE    REFSEQ: accession NM_001005889.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Kawase,A., Nakasaka,M., Bando,H., Yasuda,S., Shimada,H. and
            Iwaki,M.
  TITLE     Changes in Radixin Expression and Interaction with Efflux
            Transporters in the Liver of Adjuvant-Induced Arthritic Rats
  JOURNAL   Inflammation 43 (1), 85-94 (2020)
   PUBMED   31654296
  REMARK    GeneRIF: Changes in Radixin Expression and Interaction with Efflux
            Transporters in the Liver of Adjuvant-Induced Arthritic Rats.
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Wu,Y., Zhang,S., Zhang,C., Xuan,Z., Li,S., Gao,Y. and Hu,Y.
  TITLE     [The transfection of lentiviral siRNA vectors targeting ezrin,
            radixin and moesin facilitates influenza virus replication in
            primary pulmonary microvascular endothelial cells]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 31 (4), 456-461 (2015)
   PUBMED   25854562
  REMARK    GeneRIF: Overexpression ezrin, radixin and moesin facilitates
            influenza virus H1N1 replication in primary pulmonary microvascular
            endothelial cells.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Baeyens,N., Latrache,I., Yerna,X., Noppe,G., Horman,S. and Morel,N.
  TITLE     Redundant control of migration and adhesion by ERM proteins in
            vascular smooth muscle cells
  JOURNAL   Biochem Biophys Res Commun 441 (3), 579-585 (2013)
   PUBMED   24184478
  REMARK    GeneRIF: These results indicate that ezrin, radixin, and moesin
            exert a redundant control on platelet derived growth factor-induced
            vascular smooth muscle cells migration by regulating focal adhesion
            turn-over and cell adhesion to substrate.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Aranda,J.F., Reglero-Real,N., Marcos-Ramiro,B., Ruiz-Saenz,A.,
            Fernandez-Martin,L., Bernabe-Rubio,M., Kremer,L., Ridley,A.J.,
            Correas,I., Alonso,M.A. and Millan,J.
  TITLE     MYADM controls endothelial barrier function through ERM-dependent
            regulation of ICAM-1 expression
  JOURNAL   Mol Biol Cell 24 (4), 483-494 (2013)
   PUBMED   23264465
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Hugo,C., Hugo,C., Pichler,R., Gordon,K., Schmidt,R., Amieva,M.,
            Couser,W.G., Furthmayr,H. and Johnson,R.J.
  TITLE     The cytoskeletal linking proteins, moesin and radixin, are
            upregulated by platelet-derived growth factor, but not basic
            fibroblast growth factor in experimental mesangial proliferative
            glomerulonephritis
  JOURNAL   J Clin Invest 97 (11), 2499-2508 (1996)
   PUBMED   8647942
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Andreoli,C., Martin,M., Le Borgne,R., Reggio,H. and Mangeat,P.
  TITLE     Ezrin has properties to self-associate at the plasma membrane
  JOURNAL   J Cell Sci 107 (Pt 9), 2509-2521 (1994)
   PUBMED   7844168
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Funayama,N., Nagafuchi,A., Sato,N., Tsukita,S. and Tsukita,S.
  TITLE     Radixin is a novel member of the band 4.1 family
  JOURNAL   J Cell Biol 115 (4), 1039-1048 (1991)
   PUBMED   1955455
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Sato,N., Yonemura,S., Obinata,T., Tsukita,S. and Tsukita,S.
  TITLE     Radixin, a barbed end-capping actin-modulating protein, is
            concentrated at the cleavage furrow during cytokinesis
  JOURNAL   J Cell Biol 113 (2), 321-330 (1991)
   PUBMED   1707055
  REMARK    Erratum:[J Cell Biol 1991 Sep;114(5):1101-3]
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Tsukita,S., Hieda,Y. and Tsukita,S.
  TITLE     A new 82-kD barbed end-capping protein (radixin) localized in the
            cell-to-cell adherens junction: purification and characterization
  JOURNAL   J Cell Biol 108 (6), 2369-2382 (1989)
   PUBMED   2500445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 26, 2004 this sequence version replaced NP_001005889.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087147.1, SRR26643429.30151.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..583
                     /product="radixin isoform 2"
                     /calculated_mol_wt=68413
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..583
                     /gene="Rdx"
                     /coded_by="NM_001005889.3:223..1974"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:315655"
                     /db_xref="RGD:1359472"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lrqieeqtmk
      361 aqkeleeqtr kaleleqerq rakeeaerld rerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmcap ppppppavvp
      481 ptenehdeqd ehsaeasael ssegvtnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eam
//
LOCUS       NP_001103065             305 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC690478 [Rattus norvegicus].
ACCESSION   NP_001103065 XP_001074560
VERSION     NP_001103065.1
DBSOURCE    REFSEQ: accession NM_001109595.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473988.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001074560.1.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..305
                     /product="uncharacterized protein LOC690478"
                     /calculated_mol_wt=30750
     Region          27..182
                     /region_name="Keratin_B2"
                     /note="Keratin, high sulfur B2 protein; pfam01500"
                     /db_xref="CDD:366678"
     Region          42..85
                     /region_name="Keratin_B2_2"
                     /note="Keratin, high sulfur B2 protein; pfam13885"
                     /db_xref="CDD:464017"
     Region          258..298
                     /region_name="Keratin_B2_2"
                     /note="Keratin, high sulfur B2 protein; pfam13885"
                     /db_xref="CDD:464017"
     CDS             1..305
                     /gene="Krtap10-9"
                     /coded_by="NM_001109595.1:1..918"
                     /db_xref="GeneID:690478"
                     /db_xref="RGD:1596032"
ORIGIN      
        1 manstmsics sdlsynsrvc lpgscdsctd sswqvddspe sccepcgcap sccqpsccvp
       61 ccapsccvps ccqasccaps cctptpcllc tpvscvsspc cqsscctpsc cqqsscqsac
      121 stcspcqqpc gvtlcckpvc cvpvccgass sccqqsscep scctsspcqq pcgvtlcckp
      181 vcctpicsgs ccqqsscqss ccqpsccvpv ccrpvcctpi csassssccq psccapvcck
      241 pvcckpcssl sllcrpvcrp accvptsscc asscqpsccr pascvsllcr pacsrqacsg
      301 qkstc
//
LOCUS       NP_775175                602 aa            linear   ROD 28-APR-2025
DEFINITION  PEX5-related protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_775175
VERSION     NP_775175.2
DBSOURCE    REFSEQ: accession NM_173152.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Foote,K.M., Lyman,K.A., Han,Y., Michailidis,I.E., Heuermann,R.J.,
            Mandikian,D., Trimmer,J.S., Swanson,G.T. and Chetkovich,D.M.
  TITLE     Phosphorylation of the HCN channel auxiliary subunit TRIP8b is
            altered in an animal model of temporal lobe epilepsy and modulates
            channel function
  JOURNAL   J Biol Chem 294 (43), 15743-15758 (2019)
   PUBMED   31492750
  REMARK    GeneRIF: loss of TRIP8b phosphorylation may affect HCN channel
            properties during epileptogenesis.
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Wilkars,W., Wollberg,J., Mohr,E., Han,M., Chetkovich,D.M.,
            Bahring,R. and Bender,R.A.
  TITLE     Nedd4-2 regulates surface expression and may affect N-glycosylation
            of hyperpolarization-activated cyclic nucleotide-gated (HCN)-1
            channels
  JOURNAL   FASEB J 28 (5), 2177-2190 (2014)
   PUBMED   24451387
  REMARK    GeneRIF: Nedd4-2 plays an important role in the regulation of HCN1
            trafficking and may compete with TRIP8b(1a-4) in this process
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Wilkars,W., Liu,Z., Lewis,A.S., Stoub,T.R., Ramos,E.M., Brandt,N.,
            Nicholson,D.A., Chetkovich,D.M. and Bender,R.A.
  TITLE     Regulation of axonal HCN1 trafficking in perforant path involves
            expression of specific TRIP8b isoforms
  JOURNAL   PLoS One 7 (2), e32181 (2012)
   PUBMED   22363812
  REMARK    GeneRIF: TRIP8b isoforms are important regulators of HCN1
            trafficking in entorhinal neurons.
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Sheets,P.L., Suter,B.A., Kiritani,T., Chan,C.S., Surmeier,D.J. and
            Shepherd,G.M.
  TITLE     Corticospinal-specific HCN expression in mouse motor cortex:
            I(h)-dependent synaptic integration as a candidate microcircuit
            mechanism involved in motor control
  JOURNAL   J Neurophysiol 106 (5), 2216-2231 (2011)
   PUBMED   21795621
  REMARK    GeneRIF: Hyperpolarization current expression was high in
            corticospinal neurons and low in corticostriatal and
            corticocortical neurons, a pattern mirrored by mRNA levels for HCN1
            and Trip8b subunits.
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Popova,N.V., Plotnikov,A.N., Ziganshin,R.Kh., Deyev,I.E. and
            Petrenko,A.G.
  TITLE     Analysis of proteins interacting with TRIP8b adapter
  JOURNAL   Biochemistry (Mosc) 73 (6), 644-651 (2008)
   PUBMED   18620529
  REMARK    GeneRIF: A role of TRIP8b in receptor-mediated endocytosis.
REFERENCE   7  (residues 1 to 602)
  AUTHORS   Fransen,M., Amery,L., Hartig,A., Brees,C., Rabijns,A.,
            Mannaerts,G.P. and Van Veldhoven,P.P.
  TITLE     Comparison of the PTS1- and Rab8b-binding properties of Pex5p and
            Pex5Rp/TRIP8b
  JOURNAL   Biochim Biophys Acta 1783 (5), 864-873 (2008)
   PUBMED   18346465
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Santoro,B., Wainger,B.J. and Siegelbaum,S.A.
  TITLE     Regulation of HCN channel surface expression by a novel C-terminal
            protein-protein interaction
  JOURNAL   J Neurosci 24 (47), 10750-10762 (2004)
   PUBMED   15564593
REFERENCE   9  (residues 1 to 602)
  AUTHORS   Amery,L., Sano,H., Mannaerts,G.P., Snider,J., Van Looy,J.,
            Fransen,M. and Van Veldhoven,P.P.
  TITLE     Identification of PEX5p-related novel peroxisome-targeting signal 1
            (PTS1)-binding proteins in mammals
  JOURNAL   Biochem J 357 (Pt 3), 635-646 (2001)
   PUBMED   11463335
REFERENCE   10 (residues 1 to 602)
  AUTHORS   Chen,S., Liang,M.C., Chia,J.N., Ngsee,J.K. and Ting,A.E.
  TITLE     Rab8b and its interacting partner TRIP8b are involved in regulated
            secretion in AtT20 cells
  JOURNAL   J Biol Chem 276 (16), 13209-13216 (2001)
   PUBMED   11278749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Nov 26, 2020 this sequence version replaced NP_775175.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.10649.1,
                                           SRR26360176.284892.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..602
                     /product="PEX5-related protein isoform 1"
                     /note="PEX5-related protein; pex5Rp; PEX5-like protein;
                     peroxin-5-related protein; peroxin 2; TPR-containing
                     Rab8b-interacting protein; tetratricopeptide
                     repeat-containing Rab8b-interacting protein"
                     /calculated_mol_wt=66742
     Region          94..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          167..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          208..>403
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          302..335
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            order(306..307,310..311,313,337,340..341,344..345,
                     347..348,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          306..330
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          332..601
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          335..365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          336..369
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          370..398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          371..403
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C437; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          450..483
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          450..478
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(451,454..455,458..459,461,485,488..489,492..493,
                     495..496,519,522..523,526..527,530)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          483..513
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          485..517
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     Region          518..546
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          519..551
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N3.1)"
     CDS             1..602
                     /gene="Pex5l"
                     /gene_synonym="Pex2; TRIP8b; Trjip8b"
                     /coded_by="NM_173152.4:384..2192"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:286937"
                     /db_xref="RGD:708407"
ORIGIN      
        1 myqghmqgkg sraadkavam vmkeiprees aeekplltmt sqlvneqqes rpllspsidd
       61 flcetkseai akpvtsntav lttgldlldl sepvsqtqtk akksesssks sslkkkadgs
      121 dlisadaeqr aqalrgpets sldldiqtql ekwddvkfhg drtskghlma erkscssrag
      181 skellwsseh rsqpelstgk salnsesase lelvapaqar ltkehrwgsa llsrnhslee
      241 eferakaave sdtefwdkmq aeweemarrn wisenqeaqn qvtvsasekg yyfhtenpfk
      301 dwpgafeegl krlkegdlpv tilfmeaail qdpgdaeawq flgitqaene neqaaivalq
      361 rclelqpnnl kalmalavsy tntshqqdac ealknwikqn pkykylvknk kgspgltrrm
      421 skspvdssvl egvkdlylea ahqngdmidp dlqtglgvlf hlsgefnrai dafnaaltvr
      481 pedyslwnrl gatlangdrs eeaveaytra leiqpgfirs rynlgiscin lgayreavsn
      541 fltalslqrk srnqqqvphp aisgniwaal rialslmdqp elfqaanlgd ldvllrafnl
      601 dp
//
LOCUS       NP_001385815             277 aa            linear   ROD 28-APR-2025
DEFINITION  developmental pluripotency-associated protein 4 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001385815 XP_006248356
VERSION     NP_001385815.1
DBSOURCE    REFSEQ: accession NM_001398886.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Nakamura,T., Nakagawa,M., Ichisaka,T., Shiota,A. and Yamanaka,S.
  TITLE     Essential roles of ECAT15-2/Dppa2 in functional lung development
  JOURNAL   Mol Cell Biol 31 (21), 4366-4378 (2011)
   PUBMED   21896782
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Dec 27, 2021 this sequence version replaced XP_006248356.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.31326.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..277
                     /product="developmental pluripotency-associated protein 4
                     isoform 3"
                     /note="developmental pluripotency-associated protein 4"
                     /calculated_mol_wt=30250
     Region          23..>131
                     /region_name="PLN03188"
                     /note="kinesin-12 family protein; Provisional"
                     /db_xref="CDD:215621"
     Region          107..194
                     /region_name="Dppa2_A"
                     /note="Dppa2/4 conserved region in higher vertebrates;
                     pfam14049"
                     /db_xref="CDD:433674"
     Region          202..268
                     /region_name="DCR"
                     /note="Dppa2/4 conserved region; pfam14047"
                     /db_xref="CDD:464071"
     CDS             1..277
                     /gene="Dppa4"
                     /coded_by="NM_001398886.1:70..903"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:685378"
                     /db_xref="RGD:1595070"
ORIGIN      
        1 mepsgskkgr aeepreevec qmssqpstss aktkatgkkq rksekddgck peeksaqdpe
       61 tpgharrkvp vppfpqhlpp vnlihrdvlr awcqemklss kgqpelknvp dsakearlkm
      121 prkkmktepg eesqvtvple ivtvpeeqip alvdppvlye evsttvvtts aseavlaswa
      181 riaanakkle avpsnatset ygemwcvvhg tslpatssgw vrlqfhagqa wvpdkkgkai
      241 alfllpactf ppphlednml cpkcvhknki ltksleg
//
LOCUS       NP_001127970             375 aa            linear   ROD 28-APR-2025
DEFINITION  RNA binding protein fox-1 homolog 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001127970 XP_001081777 XP_038941608 XP_213535
VERSION     NP_001127970.1
DBSOURCE    REFSEQ: accession NM_001134498.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Anderson,M.B., Das,S. and Miller,K.E.
  TITLE     Subcellular localization of neuronal nuclei (NeuN) antigen in size
            and calcitonin gene-related peptide (CGRP) populations of dorsal
            root ganglion (DRG) neurons during acute peripheral inflammation
  JOURNAL   Neurosci Lett 760, 135974 (2021)
   PUBMED   34146639
  REMARK    GeneRIF: Subcellular localization of neuronal nuclei (NeuN) antigen
            in size and calcitonin gene-related peptide (CGRP) populations of
            dorsal root ganglion (DRG) neurons during acute peripheral
            inflammation.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Du,Z., Zhang,H., Chen,Q., Gao,Y. and Sun,B.
  TITLE     Intranasal Calcitonin Gene-Related Peptide Protects Against Focal
            Cerebral Ischemic Injury in Rats Through the Wnt/beta-Catenin
            Pathway
  JOURNAL   Med Sci Monit 24, 8860-8869 (2018)
   PUBMED   30531687
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Zimatkin,S.M. and Karniushko,O.A.
  TITLE     [EXPRESSION OF DOUBLECORTIN AND NeuN IN THE DEVELOPING CEREBELLAR
            NEURONS IN RAT]
  JOURNAL   Morfologiia 149 (1), 38-42 (2016)
   PUBMED   27487661
  REMARK    GeneRIF: EXPRESSION OF DOUBLECORTIN AND NeuN IN THE DEVELOPING
            CEREBELLAR NEURONS IN RAT
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Jakovcevski,M., Ruan,H., Shen,E.Y., Dincer,A., Javidfar,B., Ma,Q.,
            Peter,C.J., Cheung,I., Mitchell,A.C., Jiang,Y., Lin,C.L.,
            Pothula,V., Stewart,A.F., Ernst,P., Yao,W.D. and Akbarian,S.
  TITLE     Neuronal Kmt2a/Mll1 histone methyltransferase is essential for
            prefrontal synaptic plasticity and working memory
  JOURNAL   J Neurosci 35 (13), 5097-5108 (2015)
   PUBMED   25834037
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Korzhevskiy,D.E., Beznin,G.V., Kolos,Y.A. and Kirik,V.
  TITLE     [CYTOPLASMIC LOCALIZATION OF NEUN/Fox-3 NUCLEAR PROTEIN IN THE
            PANCREATIC CELLS]
  JOURNAL   Morfologiia 148 (5), 88-90 (2015)
   PUBMED   26987225
  REMARK    GeneRIF: the presence of NeuN protein in the secretory epithelial
            cells of the exocrine part of this organ. The protein was located
            in the apical part of the cytoplasm slightly below the zone of
            zymogen granules.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Marcal,N., Patel,H., Dong,Z., Belanger-Jasmin,S., Hoffman,B.,
            Helgason,C.D., Dang,J. and Stifani,S.
  TITLE     Antagonistic effects of Grg6 and Groucho/TLE on the transcription
            repression activity of brain factor 1/FoxG1 and cortical neuron
            differentiation
  JOURNAL   Mol Cell Biol 25 (24), 10916-10929 (2005)
   PUBMED   16314515
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Franke,H., Klimke,K., Brinckmann,U., Grosche,J., Francke,M.,
            Sperlagh,B., Reichenbach,A., Liebert,U.G. and Illes,P.
  TITLE     P2X(7) receptor-mRNA and -protein in the mouse retina; changes
            during retinal degeneration in BALBCrds mice
  JOURNAL   Neurochem Int 47 (4), 235-242 (2005)
   PUBMED   15964665
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Feng,R., Wang,H., Wang,J., Shrom,D., Zeng,X. and Tsien,J.Z.
  TITLE     Forebrain degeneration and ventricle enlargement caused by double
            knockout of Alzheimer's presenilin-1 and presenilin-2
  JOURNAL   Proc Natl Acad Sci U S A 101 (21), 8162-8167 (2004)
   PUBMED   15148382
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Arvidsson,A., Collin,T., Kirik,D., Kokaia,Z. and Lindvall,O.
  TITLE     Neuronal replacement from endogenous precursors in the adult brain
            after stroke
  JOURNAL   Nat Med 8 (9), 963-970 (2002)
   PUBMED   12161747
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Mullen,R.J., Buck,C.R. and Smith,A.M.
  TITLE     NeuN, a neuronal specific nuclear protein in vertebrates
  JOURNAL   Development 116 (1), 201-211 (1992)
   PUBMED   1483388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Oct 27, 2022 this sequence version replaced
            XP_038941608.1, XP_213535.4, XP_001081777.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.65414.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..375
                     /product="RNA binding protein fox-1 homolog 3 isoform 2"
                     /note="fox-1 homolog C; neuronal nuclei;
                     hexaribonucleotide binding protein 3; RNA binding protein,
                     fox-1 homolog 3"
                     /calculated_mol_wt=40463
     Region          <25..170
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Region          99..174
                     /region_name="RRM_FOX1_like"
                     /note="RNA recognition motif (RRM) found in vertebrate RNA
                     binding protein fox-1 homologs and similar proteins;
                     cd12407"
                     /db_xref="CDD:409841"
     Site            order(100,102,104..109,129..133,135..140,142,166,171..174)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409841"
     Region          208..346
                     /region_name="Fox-1_C"
                     /note="Calcitonin gene-related peptide regulator C
                     terminal; pfam12414"
                     /db_xref="CDD:463568"
     CDS             1..375
                     /gene="Rbfox3"
                     /gene_synonym="Hrnbp3; Neun; RGD1560070"
                     /coded_by="NM_001134498.4:582..1709"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:287847"
                     /db_xref="RGD:1560070"
ORIGIN      
        1 maqpyppaqy ppppqngipa eyapppphpt qdysgqtpvp pehgmtlytp aqthpeqpgt
       61 eastqpiagt qtvpqadeaa qtdsqqlhps dptekqqpkr lhvsnipfrf rdpdlrqmfg
      121 qfgkildvei ifnergskgf gfvtfetssd adrareklng tivegrkiev nnatarvmtn
      181 kkpgnpyang wklnpvvgav ygpefyavts fpypttgtav ayrgahlrgr gravyntfra
      241 apppppipty gaaleqtlvk mpvpwaglap cplppqqtpe payptspafp plscpfasrv
      301 vyqdgfygae iyggyaayry aqpaaaaaaa aysdsygrvy aaadpyhhti gptatysigt
      361 maslcrggys rftpy
//
LOCUS       NP_001013946             406 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial ribosome-associated GTPase 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001013946 XP_215964
VERSION     NP_001013946.2
DBSOURCE    REFSEQ: accession NM_001013924.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kotani,T., Akabane,S., Takeyasu,K., Ueda,T. and Takeuchi,N.
  TITLE     Human G-proteins, ObgH1 and Mtg1, associate with the large
            mitochondrial ribosome subunit and are involved in translation and
            assembly of respiratory complexes
  JOURNAL   Nucleic Acids Res 41 (6), 3713-3722 (2013)
   PUBMED   23396448
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On May 10, 2024 this sequence version replaced NP_001013946.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1654547.1,
                                           SRR26360181.2973311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..406
                     /product="mitochondrial ribosome-associated GTPase 2
                     isoform 1"
                     /note="GTP-binding protein 5"
                     /calculated_mol_wt=44123
     Region          113..385
                     /region_name="Obg_CgtA"
                     /note="Obg family GTPase CgtA; TIGR02729"
                     /db_xref="CDD:274271"
     CDS             1..406
                     /gene="Mtg2"
                     /gene_synonym="Gtpbp5"
                     /coded_by="NM_001013924.2:250..1470"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="GeneID:296462"
                     /db_xref="RGD:1359243"
ORIGIN      
        1 mvptrlvlar tctvfdsvlk wapstcavlk psqllplqas crllsvgivd hakhrepsgk
       61 kllsekklkr hfvdhrrvlf rggsggsgms cfhseprkef ggpdggdggn gghiilrvdq
      121 qvkslssvls qyqgfsgedg gskncfgrgg atlyiqvpvg tlvkegdeiv adlshlgdey
      181 vaalggaggk gnrfflandn rapvtctpgq pgqervlyle lktmahagmv gfpnagkssl
      241 lraisnakpa vasypfttln phvgivhyeg hqqvavadip giirgahqnk glglsflrhi
      301 ercrfflyvv dlslpepwtq vddlkyelek yeeglsersh viiankidlp qarahllqlq
      361 drlgqevial saltgenleq lllhlkvlhd ahieaeleqg rqplrw
//
LOCUS       NP_001420796             405 aa            linear   ROD 28-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 15 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001420796 XP_006248197
VERSION     NP_001420796.1
DBSOURCE    REFSEQ: accession NM_001433867.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Okamoto,K., Iwasaki,N., Doi,K., Noiri,E., Iwamoto,Y., Uchigata,Y.,
            Fujita,T. and Tokunaga,K.
  TITLE     Inhibition of glucose-stimulated insulin secretion by KCNJ15, a
            newly identified susceptibility gene for type 2 diabetes
  JOURNAL   Diabetes 61 (7), 1734-1741 (2012)
   PUBMED   22566534
  REMARK    GeneRIF: It was shown that downregulation of Kcnj15 leads to
            increased insulin secretion in vitro and in vivo. The mechanism for
            regulating insulin secretion inolved a calcium-sensiong receptor.
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Earley,S. and Resta,T.C.
  TITLE     Estradiol attenuates hypoxia-induced pulmonary endothelin-1 gene
            expression
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 283 (1), L86-L93 (2002)
   PUBMED   12060564
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Hill,C.E., Briggs,M.M., Liu,J. and Magtanong,L.
  TITLE     Cloning, expression, and localization of a rat hepatocyte inwardly
            rectifying potassium channel
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 282 (2), G233-G240 (2002)
   PUBMED   11804844
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Pearson,W.L., Dourado,M., Schreiber,M., Salkoff,L. and Nichols,C.G.
  TITLE     Expression of a functional Kir4 family inward rectifier K+ channel
            from a gene cloned from mouse liver
  JOURNAL   J Physiol 514 (Pt 3) (Pt 3), 639-653 (1999)
   PUBMED   9882736
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Oct 10, 2024 this sequence version replaced XP_006248197.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2296926.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..405
                     /product="ATP-sensitive inward rectifier potassium channel
                     15 isoform 1"
                     /note="ATP-sensitive inward rectifier potassium channel
                     15; inward rectifier K(+) channel Kir4.2; potassium
                     channel, inwardly rectifying subfamily J member 15;
                     potassium voltage-gated channel subfamily J member 15"
                     /calculated_mol_wt=45777
     Region          60..201
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            91..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZF1.1)"
     Region          157..162
                     /region_name="Selectivity filter. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZF1.1)"
     Site            170..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZF1.1)"
     Site            187
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q91ZF1.1)"
     Region          208..379
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..405
                     /gene="Kcnj15"
                     /gene_synonym="Kir4.2"
                     /coded_by="NM_001433867.1:1302..2519"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:170847"
                     /db_xref="RGD:621662"
ORIGIN      
        1 mvarwvkgse daplalqkip dlqsgprslr meaihigmss aplvkhsngv glkahrprvm
       61 sksghsnvri dkvdgiylly lqdlwttvid mkwrykltlf aatfvmtwfl fgvvyyaiaf
      121 ihgdlelges nsnhtpcimk vdsltgaflf slesqttigy gvrsiteecp haifllvaql
      181 vittlieifi tgtflakiar pkkraetikf shcaviskqn gklclviqva nmrkslliqc
      241 qlsgkllqth vtkegerill nqatvkfhvd sssespflil pmtfyhvlde tsplrdltpq
      301 nlkekefelv vllnatvest savcqsrtsy ipeeiywgfe fvpvvslskn gkyvadfsqf
      361 eqirkspdct fycadsekqk leeqyrqedq rerelrslll qqsnv
//
LOCUS       NP_001402669            1212 aa            linear   ROD 28-APR-2025
DEFINITION  nonsense-mediated mRNA decay factor SMG7 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001402669 XP_006250067
VERSION     NP_001402669.1
DBSOURCE    REFSEQ: accession NM_001415740.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1212)
  AUTHORS   Azzalin,C.M., Reichenbach,P., Khoriauli,L., Giulotto,E. and
            Lingner,J.
  TITLE     Telomeric repeat containing RNA and RNA surveillance factors at
            mammalian chromosome ends
  JOURNAL   Science 318 (5851), 798-801 (2007)
   PUBMED   17916692
REFERENCE   2  (residues 1 to 1212)
  AUTHORS   Ohnishi,T., Yamashita,A., Kashima,I., Schell,T., Anders,K.R.,
            Grimson,A., Hachiya,T., Hentze,M.W., Anderson,P. and Ohno,S.
  TITLE     Phosphorylation of hUPF1 induces formation of mRNA surveillance
            complexes containing hSMG-5 and hSMG-7
  JOURNAL   Mol Cell 12 (5), 1187-1200 (2003)
   PUBMED   14636577
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Dec 28, 2022 this sequence version replaced XP_006250067.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1212
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..1212
                     /product="nonsense-mediated mRNA decay factor SMG7 isoform
                     3"
                     /EC_number="2.7.11.1"
                     /note="protein SMG7; Smg-7 homolog, nonsense mediated mRNA
                     decay factor; nonsense-mediated mRNA decay factor SMG7"
                     /calculated_mol_wt=134931
     Region          80..192
                     /region_name="EST1"
                     /note="Telomerase activating protein Est1; pfam10374"
                     /db_xref="CDD:463062"
     Region          179..205
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(181..182,185..186,188,212,215..216,219..220,
                     222..223,246,249..250,253..254,257)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          196..455
                     /region_name="EST1_DNA_bind"
                     /note="Est1 DNA/RNA binding domain; pfam10373"
                     /db_xref="CDD:431239"
     Region          210..240
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1212
                     /gene="Smg7"
                     /gene_synonym="RGD1310761"
                     /coded_by="NM_001415740.2:173..3811"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:360855"
                     /db_xref="RGD:1310761"
ORIGIN      
        1 mllqivivge nvsfksqmrt enlkseehlk ssnirqaevl kaemtdsklg paevwtsrqa
       61 lqdlyqkmlv tdleyaldkk veqdlwnhaf knqittlqgq aknranpnrs evqanlslfl
      121 eaasgfytql lqelctvfnv dlpcrvkssq lgiisnkqth tsaivkpqss scsyicqhcl
      181 vhlgdiaryr nqtsqaesyy rhaaqlvpsn gqpynqlail asskgdhltt ifyycrsiav
      241 kfpfpaastn lqkalskale srdelktkwg vsdfikafik fhghvylsks leklsplrek
      301 leeqfkrllf qkafnsqqlv hvtvinlfql hhlrdfsnet eqhsysqdeq lcwtqllalf
      361 msflgilckc plqndsqesy nayplpavkv smdwlrlrpr vfqeavvder qyiwpwlisl
      421 lnsfhpredd lsstnatplp eefelqgfla lrpsfrnldf skghqgitgd kegqqrrirq
      481 qrlisigkwi adnqprliqc enevgkllfi teipeliled pseakenlil qetsaiesha
      541 sdgspglksv lstgrspsts cdsgekpvvt fkenikprev nrdqgrsfpp kevrrdcskg
      601 vtvtqddgqk dsskrraetk rctlgklqet gkqsvavqvk sqtelrktpv searktpvtq
      661 tpsqtnnsqf ipihhpgafp plpsrpgfpp ptyvipppva fsmgsgytfp agvsvpgtfl
      721 qstahspagn qvqagkqshi pysqqrpsgp gpmnqgpqqs qppsqpplts lpaqptaqst
      781 sqlqvqalaq qqqsptkvip algkspphhs gfqqyqqada skqlwnppqv qsplgkimpv
      841 kqpyylqtqd piklfepslq ppviqqqple kkmkpfpmep ynhnpsevkv pefywdssys
      901 madnravmaq qpnmdrrskr spgvfrpeqd pvprmpfedp ksspllppdl lkslaaleee
      961 eelifsnppd lypallgpla slpgrslfks llekpselms hsssflsltg fsvnqerypn
     1021 ssvfnevygk nltasskael spsvassqet slyslfegtp wspslpassd hstpasqsph
     1081 ssnpsslpss ppthnhnsap fsnfgpigtp dnrdrrpadr wktdkpamgg fgvdylsats
     1141 ssenswhqas tpsgtwtghg psmedssavl meslksiwss smmhpgpsal eqllmqqkqk
     1201 qqrgqgamnp ph
//
LOCUS       NP_001100950             759 aa            linear   ROD 28-APR-2025
DEFINITION  striatin-4 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100950 XP_001074709 XP_218432
VERSION     NP_001100950.2
DBSOURCE    REFSEQ: accession NM_001107480.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Lin,L., Lo,L.H., Lyu,Q. and Lai,K.O.
  TITLE     Determination of dendritic spine morphology by the striatin
            scaffold protein STRN4 through interaction with the phosphatase
            PP2A
  JOURNAL   J Biol Chem 292 (23), 9451-9464 (2017)
   PUBMED   28442576
  REMARK    GeneRIF: STRN4 is preferentially expressed in mushroom spines, and
            STRN4 specifically maintains mushroom spines but not thin spines
            and filopodia through interaction with the phosphatase PP2A
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Benoist,M., Baude,A., Tasmadjian,A., Dargent,B., Kessler,J.P. and
            Castets,F.
  TITLE     Distribution of zinedin in the rat brain
  JOURNAL   J Neurochem 106 (2), 969-977 (2008)
   PUBMED   18466332
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Gaillard,S., Bailly,Y., Benoist,M., Rakitina,T., Kessler,J.P.,
            Fronzaroli-Molinieres,L., Dargent,B. and Castets,F.
  TITLE     Targeting of proteins of the striatin family to dendritic spines:
            role of the coiled-coil domain
  JOURNAL   Traffic 7 (1), 74-84 (2006)
   PUBMED   16445688
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Baillat,G., Moqrich,A., Castets,F., Baude,A., Bailly,Y.,
            Benmerah,A. and Monneron,A.
  TITLE     Molecular cloning and characterization of phocein, a protein found
            from the Golgi complex to dendritic spines
  JOURNAL   Mol Biol Cell 12 (3), 663-673 (2001)
   PUBMED   11251078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BQ198897.1.
            
            On Jun 18, 2009 this sequence version replaced NP_001100950.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.1184.1,
                                           SRR26643299.1335.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 18466332
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..759
                     /product="striatin-4 isoform 1"
                     /note="zinedin; striatin, calmodulin binding protein 4"
                     /calculated_mol_wt=81306
     Region          64..188
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          436..758
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(443,461,465,471..472,495..496,514,518,524..525,
                     548..549,566,571,577..578,595,614,619,624..625,639..640,
                     660,664,670..671,683..684,701,706,712..713,725,730,748,
                     752,758)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          449..495
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          501..548
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          553..591
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          600..636
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          646..682
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          688..727
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          734..758
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..759
                     /gene="Strn4"
                     /coded_by="NM_001107480.2:455..2734"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308392"
                     /db_xref="RGD:1307030"
ORIGIN      
        1 mmeeraaaav asaascrplg sgtapnptaa apasspapgp gpvgkggggg gspgptagpe
       61 plslpgilhf iqhewarfea ekarweaera elqaqvaflq gerkgqenlk tdlvrrikml
      121 eyalkqerak yhklkfgtdl nqgekkadls eqvsngpves vtldnsplvw kegrqllrqy
      181 leevgytdti ldmrskrvrs llgrslelng agepvegapr aspgpgglsg gesllvkqie
      241 eqikrnaagk dgkerlggsv leqipflqnc ededsdedde ldsvqhkkqr vrlpskalvp
      301 emededeedd sedainefdf lgsgedgegs pdprrcaseg nphelesrrv klqgiladlr
      361 dvdglppkvt vpppgtpqpr phegsfgfss dvfimdtigg gevslgdlad ltvtndndls
      421 cdlsdskdaf kktwnpkftl rshydgirsl afhhsqsall tasedgtlkl wnlqkavtak
      481 knaaldvepi hafrahrgpv lavtmgsnse ycysggadar ihswkipdln mdpydgydps
      541 vlscvleghg davwglafsp tsqrlascsa dgtiriwdps ssgssclctf pmagehgipt
      601 svaftstepa hvvasfrsgd tvlydleagg alltlesrgs sgptqinqvv shpnqpltit
      661 ahddrgirfl dnrtgksvhs mvahldavtc lavdpngvfl msgshdcslr lwsldnktcv
      721 qeitahrkkh eeaihavach pskaliasag adalakvfv
//
LOCUS       NP_001415653            1132 aa            linear   ROD 28-APR-2025
DEFINITION  CRACD like isoform 1 [Rattus norvegicus].
ACCESSION   NP_001415653
VERSION     NP_001415653.1
DBSOURCE    REFSEQ: accession NM_001428724.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.31338.1,
                                           SRR26643298.48509.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..1132
                     /product="CRACD like isoform 1"
                     /calculated_mol_wt=120980
     Region          144..242
                     /region_name="DUF4592"
                     /note="Domain of unknown function (DUF4592); pfam15262"
                     /db_xref="CDD:464602"
     Region          <445..579
                     /region_name="PTZ00436"
                     /note="60S ribosomal protein L19-like protein;
                     Provisional"
                     /db_xref="CDD:185616"
     Region          <501..1018
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1132
                     /gene="Cracdl"
                     /gene_synonym="RGD1310819"
                     /coded_by="NM_001428724.1:261..3659"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:301351"
                     /db_xref="RGD:1310819"
ORIGIN      
        1 mistrvmdik lreaaeglge dstgkkkskf ktfkklfgkk krketaptgn sawkqnpaks
       61 evitieesgp vydsedelee srgtmgsral shdsiffpes gqdparpvrv fsqenvcdri
      121 kalqlkiqcn vklgppppgg lpikraeetg msseddglpr sppemsllhd vgpgpaikil
      181 vsssrpqspd hmsdasvssr tldgslapvv dfshppefss cldnsaakhk llvkprnqrs
      241 sklrrlssra qseclsdlsw tleeedyeek slfhvsmees pdvrqrdlmp grrsefggpa
      301 tllspggaca rrarlqhsta vsasmeeggs lgnepsslpa tpevsepmav svpgleslsl
      361 lesspyhipr veikkeelst gglcplvest skeapcgsgd vetplstdip erdvvpskeg
      421 sappegdqaf pegdttlpgg dtlppegntt ppkgvmappe rdispskdnm sppkrimapp
      481 erdkspsegd vappkrimap perdkspseg dvappkrima pperdkspse gdvappkrim
      541 apperdksps egdvtppkri mapperdksp segdvappkg imappeidks psegdvappk
      601 gimepperdm llpkgdippa ktitdtnlet psdterqdqs vqeeeltlvv prperatgte
      661 sstipapspp apksclkhkt lvpsgsaaes plkepslsvq dkaavpparh rptqaatsgg
      721 peraapgrks drsaepqrss vkrfsvtssr ararasssrl peysahvpag grapllrsgl
      781 awrseaaldd lqvppkppdr kttggdpqns gdvgagqagp gkslqdaesc aatlqepaag
      841 edqslfpvkl rstslslkyr dssaheakai krysaevrle kgglallpkd eqshvgaapa
      901 lrgsrspngq gkgktrspeq pgtkpplprk pllqsltlpy paagpdtspg eserlipvnq
      961 ppeprkeksp hqgaekgqpp aatgpgadgq ptppwitmar qkrrgapdlp vnqeekpgsr
     1021 lqktetgkqa kvaervqesv kqgdfvrsks flmtpakppv tqrqgsklsl keglqrgisl
     1081 shqnlaaqaa attekelhql krasyassdq pswmelarkk sqawsdmpqi ik
//
LOCUS       NP_001424036            1219 aa            linear   ROD 28-APR-2025
DEFINITION  AF4/FMR2 family member 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424036 XP_006250695
VERSION     NP_001424036.1
DBSOURCE    REFSEQ: accession NM_001437107.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1219)
  AUTHORS   Luo,Z., Lin,C. and Shilatifard,A.
  TITLE     The super elongation complex (SEC) family in transcriptional
            control
  JOURNAL   Nat Rev Mol Cell Biol 13 (9), 543-547 (2012)
   PUBMED   22895430
  REMARK    Review article
REFERENCE   2  (residues 1 to 1219)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   3  (residues 1 to 1219)
  AUTHORS   Baskaran,K., Erfurth,F., Taborn,G., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A., Iannaccone,P.M. and Domer,P.H.
  TITLE     Cloning and developmental expression of the murine homolog of the
            acute leukemia proto-oncogene AF4
  JOURNAL   Oncogene 15 (16), 1967-1978 (1997)
   PUBMED   9365243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006250695.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.50988.1,
                                           SRR26643296.32702.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760476,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1219
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..1219
                     /product="AF4/FMR2 family member 1 isoform 2"
                     /note="myeloid/lymphoid or mixed-lineage leukemia
                     (trithorax homolog, Drosophila); translocated to, 2;
                     AF4/FMR2 family, member 1"
                     /calculated_mol_wt=131538
     Region          8..506
                     /region_name="AF-4"
                     /note="AF-4 proto-oncoprotein N-terminal region;
                     pfam05110"
                     /db_xref="CDD:461550"
     Region          767..781
                     /region_name="AF4_int"
                     /note="AF4 interaction motif; pfam18875"
                     /db_xref="CDD:436798"
     Region          956..1217
                     /region_name="AF-4_C"
                     /note="AF-4 proto-oncoprotein C-terminal region;
                     pfam18876"
                     /db_xref="CDD:465894"
     CDS             1..1219
                     /gene="Aff1"
                     /gene_synonym="Mllt2"
                     /coded_by="NM_001437107.1:150..3809"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305152"
                     /db_xref="RGD:1307940"
ORIGIN      
        1 maahsslyne drnllrirek errnqeahqe keafpekapl faepyktakg delssriqtm
       61 lgdyeemkef lsskshphrl dgsedrpgkp rypschdrgs gasgsfrthv yhqpthtsap
      121 gslsvsnvsq spkmaqprme pvpslhakiy gapdgprpaq drlsqghcsr kcdrraegds
      181 erklspfiss lpspvpplsp ahsrpqatsk ahgsgtgtqs cyaskpskdp vvtaqeketp
      241 ldslvavtsl gaappqppcq tfpppplpsk siamqqkpta yvrpmdgqdq apsespelkp
      301 pledfgqqsf ekpdlkvpak akltrlrmps qtveqpysne vhcveeilke mthswpsplt
      361 aihtpstaep srfpfptkdp lhissatqsq kqydapskth pnpqqgtsml eddlqlsdse
      421 esdveqavek ppsppappsa pqtipepvas ahsssaeses sesdsssdse sessssdsee
      481 nepletqape peppttnkwq ldnwltkvnq psvplesrgs tesprcrqes kgggeggsdq
      541 qhpdskdppl kssskalrgp segpqpgkrn cpkspaqqet ppprqtvgsk qprkptkgst
      601 qaeqpqassr vegeagpvay gskeqtskdk pkvktkgrpr avgsrepkse vpvpvpqaav
      661 pkpqppaptp iekrkhksst apskalsgpq ptkdsagdrn qehpalvslt qsqgqpnsgr
      721 gsgggrtsgc rqavitqeds crdklllplr dtkllsplrd sppptslvvk itldlltrvp
      781 qppgkggrpr ksehkqlpag kkqdleargc dsssrvtkkr kaepekehsh krlrldksqt
      841 sssssshaes sksktprpss ecsrkemlpp ppvvpsssss ssssqkpskp ahkrprpdad
      901 igsqdpprss gstkssctds svpkhrkvqa rdsehkgssg daanpfpvps lpngnskpgk
      961 pqvksdrqqa dfhmkeakkl kckaeamvdk agkafkylea vlsfiecgma tesessaksa
     1021 ytvysetvdl ikfvmslksf sdntvpaqek ifavlclrcq sllnmamfrc kkdtvmkysr
     1081 tlsehfrsts kvaqapspcv arstgvpspv spmpspassa gsqtsagssm gamgatatvs
     1141 tpvtiqnmts syvtitshvl kaftlweqae altrknkeff aqlstkvrvl alnsslvdlv
     1201 hytrqglqrl rqapqtplm
//
LOCUS       NP_001100915             675 aa            linear   ROD 28-APR-2025
DEFINITION  heat shock 70 kDa protein 12A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100915 XP_001065021 XP_217648
VERSION     NP_001100915.1
DBSOURCE    REFSEQ: accession NM_001107445.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001065021.1, XP_217648.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.7036.1,
                                           SRR26643288.7722.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..675
                     /product="heat shock 70 kDa protein 12A isoform 2"
                     /note="heat shock 70kDa protein 12A; heat shock protein
                     12A"
                     /calculated_mol_wt=74700
     Region          57..523
                     /region_name="ASKHA_NBD_HSP70_HSPA12A"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 12A (HSPA12A) and similar proteins; cd11735"
                     /db_xref="CDD:466841"
     CDS             1..675
                     /gene="Hspa12a"
                     /coded_by="NM_001107445.2:66..2093"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:307997"
                     /db_xref="RGD:1305531"
ORIGIN      
        1 madkeagggd agpretapts ayssparslg dtgitplsps hilndadpvs eqqtflvvva
       61 idfgttssgy aysftkepec ihvmrrwegg dpgvsnqktp ttilltperk fhsfgyaard
      121 fyhdldpnea kqwlylekfk mklhttgdlt mdtdltaang kkvkaleift yalqyfkeqa
      181 lkelsdqags dfensdvrwv itvpaiwkqp akqfmreaay qaglaspens eqliialepe
      241 aasiycrklr lhqmielssk avvngysasd tvgagfaqak ehvrrnrqsr tflvenvige
      301 iwseleegdk yvvvdsgggt vdltvhqirl peghlkelyk atggpygslg vdyefekllc
      361 kifgedfieq fkikrpaawv dlmiafesrk raaapdrtnp lnitlpfsfi dyykkfrghs
      421 vehalrksnv dfvkwssqgm lrmspdamna lfkptidsii ehlrdlfqkp evstvkflfl
      481 vggfaeapll qqavqaafgd kcriiipqdv gltilkgavl fgldpavikv rrspltygvg
      541 vlnryvegkh ppekllvkdg trwctdvfdk fisadqsval gelvkrsytp akpsqlviii
      601 niyssenddv sfitdpgvkk cgtlrldltg tsgaavparr eiqtlmqfgd teikatavdi
      661 atsksvkvgi dflny
//
LOCUS       NP_001421143             525 aa            linear   ROD 28-APR-2025
DEFINITION  male-specific lethal 3 homolog isoform 4 [Rattus norvegicus].
ACCESSION   NP_001421143 XP_006256901
VERSION     NP_001421143.1
DBSOURCE    REFSEQ: accession NM_001434214.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Basilicata,M.F., Bruel,A.L., Semplicio,G., Valsecchi,C.I.K.,
            Aktas,T., Duffourd,Y., Rumpf,T., Morton,J., Bache,I.,
            Szymanski,W.G., Gilissen,C., Vanakker,O., Ounap,K., Mittler,G., van
            der Burgt,I., El Chehadeh,S., Cho,M.T., Pfundt,R., Tan,T.Y.,
            Kirchhoff,M., Menten,B., Vergult,S., Lindstrom,K., Reis,A.,
            Johnson,D.S., Fryer,A., McKay,V., Fisher,R.B., Thauvin-Robinet,C.,
            Francis,D., Roscioli,T., Pajusalu,S., Radtke,K., Ganesh,J.,
            Brunner,H.G., Wilson,M., Faivre,L., Kalscheuer,V.M., Thevenon,J.
            and Akhtar,A.
  CONSRTM   DDD Study
  TITLE     De novo mutations in MSL3 cause an X-linked syndrome marked by
            impaired histone H4 lysine 16 acetylation
  JOURNAL   Nat Genet 50 (10), 1442-1451 (2018)
   PUBMED   30224647
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Kim,D., Blus,B.J., Chandra,V., Huang,P., Rastinejad,F. and
            Khorasanizadeh,S.
  TITLE     Corecognition of DNA and a methylated histone tail by the MSL3
            chromodomain
  JOURNAL   Nat Struct Mol Biol 17 (8), 1027-1029 (2010)
   PUBMED   20657587
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Oct 24, 2024 this sequence version replaced XP_006256901.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.60742.1,
                                           SRR26643298.31501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13"
     Protein         1..525
                     /product="male-specific lethal 3 homolog isoform 4"
                     /note="male-specific lethal-3 homolog 1"
                     /calculated_mol_wt=60139
     Region          15..81
                     /region_name="CBD_MSL3_like"
                     /note="chromo barrel domain of human male-specific lethal
                     complex subunit 3, and similar proteins; cd18983"
                     /db_xref="CDD:350846"
     Site            order(26..27,31..34,54,56..59,63,65..68,70..72,75..76)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350846"
     Site            order(31,56,59,63)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350846"
     Site            order(53,55..60,62..66)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Site            order(53,56,60,62,66)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350846"
     Region          166..510
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..525
                     /gene="Msl3"
                     /gene_synonym="Msl31; Msl3l1"
                     /coded_by="NM_001434214.1:33..1610"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:317464"
                     /db_xref="RGD:1549763"
ORIGIN      
        1 msaskgmkfq fhsgekvlcf epdptkarvl ydakiidvii gkdekgrkip eylihfngwn
       61 sswdrwaaed hvlhdtdenr rlqrklakka iarlrgtgkk krrcrlpgvd svlksvpvke
      121 ktkndensis stchescgek nggikehrqr rikvktkgkk kvlslrsrkd mdertitiei
      181 pevlkkqled dcyyinrrkr lvklpcqtni itilesyvkh fainaafsan erprhhhamm
      241 hahmnvhyvp aeknvdlcke mvdglritfd ytlplvllyp yeqtqykrvt sskfflpike
      301 sttttnrsqe elspspplln pstpqstesq pptgepatpk rrkaepealq slrrstrhst
      361 ncdrlsesss spqpkrrqqd tstsmpklfl hlekktpvhs rssspipltp skdgsavfag
      421 fegrrtnein evlswklvpd nyppgdqppp psyiygaqhl lrlfvklpei lgkmsfsekn
      481 lkallkhfdl flrflaeyhd dffpesayva aceahystkn praiy
//
LOCUS       NP_001388552             970 aa            linear   ROD 28-APR-2025
DEFINITION  metal transporter CNNM1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001388552 XP_006231545
VERSION     NP_001388552.1
DBSOURCE    REFSEQ: accession NM_001401623.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Guo,D., Ling,J., Wang,M.H., She,J.X., Gu,J. and Wang,C.Y.
  TITLE     Physical interaction and functional coupling between ACDP4 and the
            intracellular ion chaperone COX11, an implication of the role of
            ACDP4 in essential metal ion transport and homeostasis
  JOURNAL   Mol Pain 1, 15 (2005)
   PUBMED   15840172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Wang,C.Y., Yang,P., Shi,J.D., Purohit,S., Guo,D., An,H., Gu,J.G.,
            Ling,J., Dong,Z. and She,J.X.
  TITLE     Molecular cloning and characterization of the mouse Acdp gene
            family
  JOURNAL   BMC Genomics 5 (1), 7 (2004)
   PUBMED   14723793
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 16, 2022 this sequence version replaced XP_006231545.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.8079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..970
                     /product="metal transporter CNNM1 isoform 2"
                     /note="metal transporter CNNM1; cyclin M1"
                     /calculated_mol_wt=105673
     Region          250..>554
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
     Region          428..553
                     /region_name="CBS_pair_CorC_HlyC_assoc"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains the majority of which are
                     associated with the CorC_HlyC domain; cd04590"
                     /db_xref="CDD:341366"
     Region          436..503
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Site            order(463,478,482..483,486,507,529..531)
                     /site_type="other"
                     /note="putative ligand binding site I [chemical binding]"
                     /db_xref="CDD:341366"
     Region          507..552
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     CDS             1..970
                     /gene="Cnnm1"
                     /coded_by="NM_001401623.1:140..3052"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:309387"
                     /db_xref="RGD:1308728"
ORIGIN      
        1 maaaaaaaaa lgvrlrdccs rgavlllffs lsprppaaaa wllglrpedt aggrvslegg
       61 tlraaegtsf llrvyfqpgp avpaapvpap slapgengtg dwaprlvfie eppgagsaap
      121 savptrppgp qrcreqsdwa sdvevlgplr pggvagsalv qvrvrelrkg eaerggaggg
      181 gklfslcawd grawhhhgaa ggfllrvrpr lygpggdllp pawlralgal lllalsalfs
      241 glrlsllsld pvelrvlrns gsaaeqeqar rvqavrgrgt hllctlllgq aganaalagw
      301 lyaslppgvg dpgedsgeag vhfpwlpalv ctgavflgae icpysvcsrh glaiashsvc
      361 ltrllmaaaf pvcyplgrll dwalrqeist fytrekllet lraadpysdl vkeelniiqg
      421 alelrtkvve evltplgdcf mlrsdavldf atvseilrsg ytripvyegd qrhnivdilf
      481 vkdlafvdpd dctplltvtr fynrplhcvf ndtrldtvle efkkgkshla ivqrvnnege
      541 gdpfyevmgi vtlediieei ikseildetd lytdnrkkqr vphrerrrhd fslfklsdse
      601 irvkispqll lathrfmate vepfkslyls ekillrllkh pnviqelkfd ernkkapehy
      661 lyqrsrpvdy fvlllqgkve vevgkeglrf engaftyygv paimtsacsd ndvrkvgsla
      721 gssvflpvsv srtfafsrgd slagspvnrs psrcsglnrs espnrersdf ggsntqlcsn
      781 nlytpdysvh ilsdvqfvki trqqyqnalt achmdsspqs pdmeaftdgd stkapttrgt
      841 pqtpkddpvl tllsnrtslp csrsdglrsp gevvylrmee mafpqeempn feehkaqqvs
      901 lspvtvptaa aseteccnih ldpeaspcss dseetmgkkl lrtlsgrkrk ksadgerase
      961 ensnltplit
//
LOCUS       NP_001420683             604 aa            linear   ROD 28-APR-2025
DEFINITION  radixin isoform 1 [Rattus norvegicus].
ACCESSION   NP_001420683 XP_038937381
VERSION     NP_001420683.1
DBSOURCE    REFSEQ: accession NM_001433754.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Kawase,A., Nakasaka,M., Bando,H., Yasuda,S., Shimada,H. and
            Iwaki,M.
  TITLE     Changes in Radixin Expression and Interaction with Efflux
            Transporters in the Liver of Adjuvant-Induced Arthritic Rats
  JOURNAL   Inflammation 43 (1), 85-94 (2020)
   PUBMED   31654296
  REMARK    GeneRIF: Changes in Radixin Expression and Interaction with Efflux
            Transporters in the Liver of Adjuvant-Induced Arthritic Rats.
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Wu,Y., Zhang,S., Zhang,C., Xuan,Z., Li,S., Gao,Y. and Hu,Y.
  TITLE     [The transfection of lentiviral siRNA vectors targeting ezrin,
            radixin and moesin facilitates influenza virus replication in
            primary pulmonary microvascular endothelial cells]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 31 (4), 456-461 (2015)
   PUBMED   25854562
  REMARK    GeneRIF: Overexpression ezrin, radixin and moesin facilitates
            influenza virus H1N1 replication in primary pulmonary microvascular
            endothelial cells.
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Baeyens,N., Latrache,I., Yerna,X., Noppe,G., Horman,S. and Morel,N.
  TITLE     Redundant control of migration and adhesion by ERM proteins in
            vascular smooth muscle cells
  JOURNAL   Biochem Biophys Res Commun 441 (3), 579-585 (2013)
   PUBMED   24184478
  REMARK    GeneRIF: These results indicate that ezrin, radixin, and moesin
            exert a redundant control on platelet derived growth factor-induced
            vascular smooth muscle cells migration by regulating focal adhesion
            turn-over and cell adhesion to substrate.
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Aranda,J.F., Reglero-Real,N., Marcos-Ramiro,B., Ruiz-Saenz,A.,
            Fernandez-Martin,L., Bernabe-Rubio,M., Kremer,L., Ridley,A.J.,
            Correas,I., Alonso,M.A. and Millan,J.
  TITLE     MYADM controls endothelial barrier function through ERM-dependent
            regulation of ICAM-1 expression
  JOURNAL   Mol Biol Cell 24 (4), 483-494 (2013)
   PUBMED   23264465
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Hugo,C., Hugo,C., Pichler,R., Gordon,K., Schmidt,R., Amieva,M.,
            Couser,W.G., Furthmayr,H. and Johnson,R.J.
  TITLE     The cytoskeletal linking proteins, moesin and radixin, are
            upregulated by platelet-derived growth factor, but not basic
            fibroblast growth factor in experimental mesangial proliferative
            glomerulonephritis
  JOURNAL   J Clin Invest 97 (11), 2499-2508 (1996)
   PUBMED   8647942
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Andreoli,C., Martin,M., Le Borgne,R., Reggio,H. and Mangeat,P.
  TITLE     Ezrin has properties to self-associate at the plasma membrane
  JOURNAL   J Cell Sci 107 (Pt 9), 2509-2521 (1994)
   PUBMED   7844168
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Funayama,N., Nagafuchi,A., Sato,N., Tsukita,S. and Tsukita,S.
  TITLE     Radixin is a novel member of the band 4.1 family
  JOURNAL   J Cell Biol 115 (4), 1039-1048 (1991)
   PUBMED   1955455
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Sato,N., Yonemura,S., Obinata,T., Tsukita,S. and Tsukita,S.
  TITLE     Radixin, a barbed end-capping actin-modulating protein, is
            concentrated at the cleavage furrow during cytokinesis
  JOURNAL   J Cell Biol 113 (2), 321-330 (1991)
   PUBMED   1707055
  REMARK    Erratum:[J Cell Biol 1991 Sep;114(5):1101-3]
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Tsukita,S., Hieda,Y. and Tsukita,S.
  TITLE     A new 82-kD barbed end-capping protein (radixin) localized in the
            cell-to-cell adherens junction: purification and characterization
  JOURNAL   J Cell Biol 108 (6), 2369-2382 (1989)
   PUBMED   2500445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 7, 2024 this sequence version replaced XP_038937381.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.44199.1,
                                           SRR26643289.22881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..604
                     /product="radixin isoform 1"
                     /calculated_mol_wt=70898
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..604
                     /gene="Rdx"
                     /coded_by="NM_001433754.1:223..2037"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:315655"
                     /db_xref="RGD:1359472"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lrqieeqtmk
      361 aqkeleeqtr kaleleqerq rakeeaerld rerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmcap ppppppavvp
      481 ptenehdeqd ehsaeasael ssegvtnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eamwgpklya lfqmrscqss
      601 ikqm
//
LOCUS       NP_001418973             981 aa            linear   ROD 28-APR-2025
DEFINITION  similar to WD repeat domain 59 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001418973 XP_063134730
VERSION     NP_001418973.1
DBSOURCE    REFSEQ: accession NM_001432044.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Bar-Peled,L. and Sabatini,D.M.
  TITLE     Regulation of mTORC1 by amino acids
  JOURNAL   Trends Cell Biol 24 (7), 400-406 (2014)
   PUBMED   24698685
  REMARK    Review article
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 25, 2024 this sequence version replaced XP_063134730.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.80072.1,
                                           SRR26643296.38940.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..981
                     /product="similar to WD repeat domain 59 isoform 2"
                     /note="WD repeat-containing protein 59; GATOR complex
                     protein WDR59; GATOR2 complex protein WDR59"
                     /calculated_mol_wt=110478
     Region          <46..137
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          62..103
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          100..>343
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          109..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          154..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..229
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          237..279
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..316
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          401..501
                     /region_name="RWD"
                     /note="domain in RING finger and WD repeat containing
                     proteins and DEXDc-like helicases subfamily related to the
                     UBCc domain; smart00591"
                     /db_xref="CDD:214735"
     Region          929..975
                     /region_name="mRING-H2-C3H3C2_WDR59"
                     /note="Modified RING finger, H2 subclass (C3H3C2-type),
                     found in WD repeat-containing protein 59 (WDR59) and
                     similar proteins; cd16692"
                     /db_xref="CDD:438353"
     CDS             1..981
                     /gene="Wdr59"
                     /coded_by="NM_001432044.1:96..3041"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:690751"
                     /db_xref="RGD:1592213"
ORIGIN      
        1 maarwssenv vvefrdsqat amsvdcvgqh avlsgrrfly ivnldapfeg hrkisrqskw
       61 digavqwnph dsfahyfaas snqrvdlykw kdgsgevgtt lqghtrvisd ldwavfepdl
      121 lvtssvdtyi yiwdikdtrk pavalsavag asqvkwnkkn anylatshdg dvriwdkrkp
      181 staveylaah lskihgldwh pdsehifats sqdnsvkfwd yrqprkylni lpcqvpvwka
      241 rytpfsnglv tvmvpqlrre nslllwnvfd lntpvhtfvg hddvvlefqw rrqkegskdy
      301 qlvtwsrdqt lrmwrvdyqm qrlcandild gvdefiesis llpepektlh pqdtdhqpsl
      361 shgeedgnvt dvlaikedpp sslleerrsd qlglpqtlqq efslinvqir nvnvemdaad
      421 rsctvsvhcs nhrvkmlvtf paqypnnaap sfqfinptti tsavkakllk ilkdtslqkv
      481 krnqsclepc lrqlvscles fvnqedsass npfalpnsvt pplptfarvt taygsyqdan
      541 ipfprtsgar fcgagylvyf trpmtmhrav spteptprsl salsayhtgl iapmkirtea
      601 pgnlrlysgs ptrsekeqvs issfyykerk srrwkskreg sdsgnrpika agkviiqdvs
      661 cllpvhkslg elyilnvndt qetcqknats amlvgrkdlv qvwslatvat dlclgpksdp
      721 dletpwarhp fgrqllesll ahycrlrdvq tlamlcsvfe aqsrpqglpn pfgpfpnrss
      781 nfvvshsryp sftssgscss msdpgfntgg wsiagreteh isspwgessp eelrfgslty
      841 sdprererdq hdknkrlldp antqqfddfk kcygeilyrw glrekraevl kfvscppdph
      901 kgiefgvycs hcrsevrgtq caickgftfq caichvavrg ssnfcltcgh gghtshmmew
      961 frtqevcptg cgchcllest f
//
LOCUS       NP_001400566             365 aa            linear   ROD 28-APR-2025
DEFINITION  N-lysine methyltransferase KMT5A isoform 2 [Rattus norvegicus].
ACCESSION   NP_001400566 XP_038945698
VERSION     NP_001400566.1
DBSOURCE    REFSEQ: accession NM_001413637.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Li,Y., Cheng,M., Jin,J., Zhang,D., Zhang,S., Bai,Y. and Xu,J.
  TITLE     Interaction of Sp1 and Setd8 promotes vascular smooth muscle cells
            apoptosis by activating Mark4 in vascular calcification
  JOURNAL   Aging (Albany NY) 16 (3), 2438-2456 (2024)
   PUBMED   38301049
  REMARK    GeneRIF: Interaction of Sp1 and Setd8 promotes vascular smooth
            muscle cells apoptosis by activating Mark4 in vascular
            calcification.
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Li,J., Song,H., Chen,T., Zhang,S., Zhang,C., Ma,C., Zhang,L.,
            Wang,T., Qian,Y. and Deng,X.
  TITLE     Lysine Methyltransferase 5A Promotes the Progression of Growth
            Hormone Pituitary Neuroendocrine Tumors through the
            Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Neuroendocrinology 114 (6), 589-601 (2024)
   PUBMED   38565081
  REMARK    GeneRIF: Lysine Methyltransferase 5A Promotes the Progression of
            Growth Hormone Pituitary Neuroendocrine Tumors through the
            Wnt/beta-Catenin Signaling Pathway.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Li,X., Qian,Y., Shen,W., Zhang,S., Han,H., Zhang,Y., Liu,S., Lv,S.
            and Zhang,X.
  TITLE     Mechanism of SET8 Activates the Nrf2-KEAP1-ARE Signaling Pathway to
            Promote the Recovery of Motor Function after Spinal Cord Injury
  JOURNAL   Mediators Inflamm 2023, 4420592 (2023)
   PUBMED   36936537
  REMARK    GeneRIF: Mechanism of SET8 Activates the Nrf2-KEAP1-ARE Signaling
            Pathway to Promote the Recovery of Motor Function after Spinal Cord
            Injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Barrett,E., Loverin,A., Wang,H., Carlson,M., Larsen,T.D.,
            Almeida,M.M., Whitman,J., Baack,M.L. and Joss-Moore,L.A.
  TITLE     Uteroplacental Insufficiency with Hypoxia Upregulates Placental
            PPARgamma-KMT5A Axis in the Rat
  JOURNAL   Reprod Sci 28 (5), 1476-1488 (2021)
   PUBMED   33398850
  REMARK    GeneRIF: Uteroplacental Insufficiency with Hypoxia Upregulates
            Placental PPARgamma-KMT5A Axis in the Rat.
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Pan,C., Chen,H., Wang,L., Yang,S., Fu,H., Zheng,Y., Miao,M. and
            Jiao,B.
  TITLE     Down-regulation of MiR-127 facilitates hepatocyte proliferation
            during rat liver regeneration
  JOURNAL   PLoS One 7 (6), e39151 (2012)
   PUBMED   22720056
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Kalakonda,N., Fischle,W., Boccuni,P., Gurvich,N., Hoya-Arias,R.,
            Zhao,X., Miyata,Y., Macgrogan,D., Zhang,J., Sims,J.K., Rice,J.C.
            and Nimer,S.D.
  TITLE     Histone H4 lysine 20 monomethylation promotes transcriptional
            repression by L3MBTL1
  JOURNAL   Oncogene 27 (31), 4293-4304 (2008)
   PUBMED   18408754
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Sims,J.K. and Rice,J.C.
  TITLE     PR-Set7 establishes a repressive trans-tail histone code that
            regulates differentiation
  JOURNAL   Mol Cell Biol 28 (14), 4459-4468 (2008)
   PUBMED   18474616
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Shi,X., Kachirskaia,I., Yamaguchi,H., West,L.E., Wen,H., Wang,E.W.,
            Dutta,S., Appella,E. and Gozani,O.
  TITLE     Modulation of p53 function by SET8-mediated methylation at lysine
            382
  JOURNAL   Mol Cell 27 (4), 636-646 (2007)
   PUBMED   17707234
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Nov 4, 2022 this sequence version replaced XP_038945698.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.105086.1,
                                           SRR26643299.50406.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..365
                     /product="N-lysine methyltransferase KMT5A isoform 2"
                     /EC_number="2.1.1.354"
                     /note="SET domain-containing 8; histone-lysine
                     N-methyltransferase SETD8; histone methyltransferase
                     Pr-set7/Set8; N-lysine methyltransferase SETD8; SET domain
                     containing (lysine methyltransferase) 8; lysine
                     (K)-specific methyltransferase 5A; N-lysine
                     methyltransferase KMT5A"
                     /calculated_mol_wt=41126
     Region          213..352
                     /region_name="SET_SETD8"
                     /note="SET domain found in SET domain-containing protein 8
                     (SETD8) and similar proteins; cd10528"
                     /db_xref="CDD:380926"
     Site            order(240..242,258,283..287,308..312,349)
                     /site_type="active"
                     /db_xref="CDD:380926"
     Site            order(240..242,283..284,308..312,349)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380926"
     Site            order(258,272,275..276,282..283,285..288,320,331,347,
                     349..352)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380926"
     CDS             1..365
                     /gene="Kmt5a"
                     /gene_synonym="Pr-set7; RGD1305893; Setd8"
                     /coded_by="NM_001413637.1:63..1160"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:689820"
                     /db_xref="RGD:1587560"
ORIGIN      
        1 mgeagavgrr rpfpgaprrr wwrrqqqqqq rrrqrwwpgr gegegagraa mglaglqenv
       61 fagqskiyay mspnkcsgmr splqeensva hhevkcpgkp lagiyrkree krnagnvirs
      121 avkseeqksk dtrrgplapf pnqkpeatep pktpppscds tsvavakqal kkplkgkqap
      181 rkksqgktqq nrkltdfypv rrssrkskae lqseerkkid eliesgkeeg mkidlidgkg
      241 rgviatkrfs rgdfvveyhg dlieitdakk realyaqdps tgcymyyfqy lsktycvdat
      301 qetnrlgrli nhskcgncqt klhdidgvph liliasrdia ageellydyg drskasieay
      361 pwlkh
//
LOCUS       NP_001034109             464 aa            linear   ROD 28-APR-2025
DEFINITION  BUB3-interacting and GLEBS motif-containing protein ZNF207 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001034109 XP_221231
VERSION     NP_001034109.1
DBSOURCE    REFSEQ: accession NM_001039020.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Jiang,H., Wang,S., Huang,Y., He,X., Cui,H., Zhu,X. and Zheng,Y.
  TITLE     Phase transition of spindle-associated protein regulate spindle
            apparatus assembly
  JOURNAL   Cell 163 (1), 108-122 (2015)
   PUBMED   26388440
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Toledo,C.M., Herman,J.A., Olsen,J.B., Ding,Y., Corrin,P.,
            Girard,E.J., Olson,J.M., Emili,A., DeLuca,J.G. and Paddison,P.J.
  TITLE     BuGZ is required for Bub3 stability, Bub1 kinetochore function, and
            chromosome alignment
  JOURNAL   Dev Cell 28 (3), 282-294 (2014)
   PUBMED   24462187
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Jiang,H., He,X., Wang,S., Jia,J., Wan,Y., Wang,Y., Zeng,R.,
            Yates,J. 3rd, Zhu,X. and Zheng,Y.
  TITLE     A microtubule-associated zinc finger protein, BuGZ, regulates
            mitotic chromosome alignment by ensuring Bub3 stability and
            kinetochore targeting
  JOURNAL   Dev Cell 28 (3), 268-281 (2014)
   PUBMED   24462186
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Misawa,K., Nosaka,T., Morita,S., Kaneko,A., Nakahata,T., Asano,S.
            and Kitamura,T.
  TITLE     A method to identify cDNAs based on localization of green
            fluorescent protein fusion products
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3062-3066 (2000)
   PUBMED   10716735
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Taguchi,E., Muramatsu,H., Fan,Q.W., Kurosawa,N., Sobue,G. and
            Muramatsu,T.
  TITLE     Zep: A novel zinc finger protein containing a large proline-rich
            domain
  JOURNAL   J Biochem 124 (6), 1220-1228 (1998)
   PUBMED   9832628
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jan 12, 2006 this sequence version replaced XP_221231.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100269.1, SRR26643298.62579.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..464
                     /product="BUB3-interacting and GLEBS motif-containing
                     protein ZNF207 isoform 1"
                     /note="BUB3-interacting and GLEBS motif-containing protein
                     ZNF207"
                     /calculated_mol_wt=49647
     Region          10..90
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          13..34
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          13..34
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(18,24,31,33,36,43)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          37..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          <406..441
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     CDS             1..464
                     /gene="Zfp207"
                     /coded_by="NM_001039020.3:138..1532"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303763"
                     /db_xref="RGD:1308121"
ORIGIN      
        1 mgrkkkkqlk pwcwycnrdf ddekiliqhq kakhfkchic hkklytgpgl aihcmqvhke
       61 tidavpnaip grtdieleiy gmegipekdm derrrlleqk tqesqkkkqq ddsdeyddde
      121 saastsfqpq pvqpqqgyip pmaqpglppv pgapgmppgi pplmpgvppl mpgmppvmpg
      181 mppglhhqrk ytqsfcgeni mmpmggmmpp gpgipplmpg mppgmpppvp rpgippmtqa
      241 qavsapgiln rppaptaavp apqppvtkpl fpsagqaqaa vqgpvgtdfk plnstpaatt
      301 teppkptfpa ytqstastts ttnstaakpa asitskpatl tttsatskli hpdedislee
      361 rraqlpkyqr nlprpgqtpi gnppvgpigg mmppqpgipq qqgmrppmpp hgqygghhqg
      421 mpgylpgamp pygqgppmvp pyqggpprpp mgmrppvmsq ggry
//
LOCUS       NP_110487                507 aa            linear   ROD 28-APR-2025
DEFINITION  myocyte-specific enhancer factor 2D [Rattus norvegicus].
ACCESSION   NP_110487 XP_001069089 XP_001069142
VERSION     NP_110487.2
DBSOURCE    REFSEQ: accession NM_030860.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Cao,J., Guo,B., Li,S., Zhang,X., Zhang,X., Zhang,G., Sun,Y.,
            Wang,Y., Song,X. and Zhang,Z.
  TITLE     Neuroprotection against 1-Methyl-4-phenylpyridinium-induced
            cytotoxicity by naturally occurring polydatin through activation of
            transcription factor MEF2D
  JOURNAL   Neuroreport 32 (12), 1065-1072 (2021)
   PUBMED   34232128
  REMARK    GeneRIF: Neuroprotection against
            1-Methyl-4-phenylpyridinium-induced cytotoxicity by naturally
            occurring polydatin through activation of transcription factor
            MEF2D.
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Li,J., Aponte Paris,S., Thakur,H., Kapiloff,M.S. and
            Dodge-Kafka,K.L.
  TITLE     Muscle A-kinase-anchoring protein-beta-bound calcineurin toggles
            active and repressive transcriptional complexes of myocyte enhancer
            factor 2D
  JOURNAL   J Biol Chem 294 (7), 2543-2554 (2019)
   PUBMED   30523159
  REMARK    GeneRIF: these results highlight the importance of mAKAPbeta
            signalosomes for regulating MEF2D activity in striated muscle,
            affirming mAKAPbeta as a nodal regulator in the myocyte
            intracellular signaling network.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Guo,B., Hu,S., Zheng,C., Wang,H., Luo,F., Li,H., Cui,W., Yang,X.,
            Cui,G., Mak,S., Choi,T.C., Ma,E.D., Wang,Y., Lee,S.M.Y., Zhang,Z.
            and Han,Y.
  TITLE     Substantial protection against MPTP-associated Parkinson's
            neurotoxicity in vitro and in vivo by anti-cancer agent SU4312 via
            activation of MEF2D and inhibition of MAO-B
  JOURNAL   Neuropharmacology 126, 12-24 (2017)
   PUBMED   28807675
  REMARK    GeneRIF: Study suggests that SU4312 provides therapeutic benefits
            in cellular and animal models of Parkinson's disease, possibly
            through multiple mechanisms including enhancement of myocyte
            enhancer factor 2D through the activation of PI3-K/Akt pathway.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Li,K., Pan,J., Wang,J., Liu,F. and Wang,L.
  TITLE     MiR-665 regulates VSMCs proliferation via targeting FGF9 and MEF2D
            and modulating activities of Wnt/beta-catenin signaling
  JOURNAL   Am J Transl Res 9 (10), 4402-4414 (2017)
   PUBMED   29118903
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Desjardins,C.A. and Naya,F.J.
  TITLE     Antagonistic regulation of cell-cycle and differentiation gene
            programs in neonatal cardiomyocytes by homologous MEF2
            transcription factors
  JOURNAL   J Biol Chem 292 (25), 10613-10629 (2017)
   PUBMED   28473466
  REMARK    GeneRIF: MEF2A and MEF2D were absolutely required for cardiomyocyte
            survival, whereas MEF2C, despite its major role in cardiac
            morphogenesis and direct reprogramming, was dispensable for this
            process.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Yang,C.C., Ornatsky,O.I., McDermott,J.C., Cruz,T.F. and Prody,C.A.
  TITLE     Interaction of myocyte enhancer factor 2 (MEF2) with a
            mitogen-activated protein kinase, ERK5/BMK1
  JOURNAL   Nucleic Acids Res 26 (20), 4771-4777 (1998)
   PUBMED   9753748
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Di Lisi,R., Millino,C., Calabria,E., Altruda,F., Schiaffino,S. and
            Ausoni,S.
  TITLE     Combinatorial cis-acting elements control tissue-specific
            activation of the cardiac troponin I gene in vitro and in vivo
  JOURNAL   J Biol Chem 273 (39), 25371-25380 (1998)
   PUBMED   9738004
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Black,B.L., Ligon,K.L., Zhang,Y. and Olson,E.N.
  TITLE     Cooperative transcriptional activation by the neurogenic basic
            helix-loop-helix protein MASH1 and members of the myocyte enhancer
            factor-2 (MEF2) family
  JOURNAL   J Biol Chem 271 (43), 26659-26663 (1996)
   PUBMED   8900141
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Han,T.H. and Prywes,R.
  TITLE     Regulatory role of MEF2D in serum induction of the c-jun promoter
  JOURNAL   Mol Cell Biol 15 (6), 2907-2915 (1995)
   PUBMED   7760790
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081790.1.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001069142.1, XP_001069089.1, NP_110487.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..507
                     /product="myocyte-specific enhancer factor 2D"
                     /calculated_mol_wt=54111
     Region          1..346
                     /region_name="ARG80"
                     /note="Regulator of arginine metabolism and related MADS
                     box-containing transcription factors [Transcription];
                     COG5068"
                     /db_xref="CDD:227400"
     Region          2..78
                     /region_name="MADS_MEF2_like"
                     /note="MEF2 (myocyte enhancer factor 2)-like/Type II
                     subfamily of MADS (MCM1, Agamous, Deficiens, and SRF
                     (serum response factor) box family of eukaryotic
                     transcriptional regulators. Binds DNA and exists as hetero
                     and homo-dimers. Differs from SRF-like/Type I...; cd00265"
                     /db_xref="CDD:238165"
     Site            order(2..4,6,8,13,15,19..20,23..24,26..27,30..31,33..34,
                     38)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238165"
     Site            order(21,28..29,32..33,35..36,39,44,46,48,54,56,62,65..66,
                     69,72..73)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238165"
     Site            59
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:238165"
     Region          97..154
                     /region_name="HJURP_C"
                     /note="Holliday junction regulator protein family
                     C-terminal repeat; pfam12347"
                     /db_xref="CDD:463543"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63943; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Region          174..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89038.1)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q63943; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Region          244..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89038.1)"
     Site            245
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14814; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Region          357..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89038.1)"
     Region          423..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O89038.1)"
     Site            425
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q14814; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14814; propagated from
                     UniProtKB/Swiss-Prot (O89038.1)"
     CDS             1..507
                     /gene="Mef2d"
                     /coded_by="NM_030860.2:455..1978"
                     /db_xref="GeneID:81518"
                     /db_xref="RGD:621489"
ORIGIN      
        1 mgrkkiqiqr itdernrqvt ftkrkfglmk kayelsvlcd ceialiifnh snklfqyast
       61 dmdkvllkyt eynephesrt nadiietlrk kgfngcdspe pdgedsleqs plledkyrra
      121 seeldglfrr ygssvpapnf ampvtvpvsn qssmqfsnps sslvtpslvt ssltdprlls
      181 pqqpalqrns vspglpqrpa sagamlggdl nsangacpsp vgngyvsara spgllpvang
      241 nglnkvipak sppppthntq lgapsrkpdl rvitsqggkg lmhhlnnaqr lgvsqsthsl
      301 ttpvvsvatp sllsqglpfs smptayntdy qlpsaelssl pafsspagla lgnvtawqqp
      361 qqpqqpqppq ppqsqpqppq pqpqqppqqq phlvpvslsn lipgsplphv gaaltvtthp
      421 hisiksepvs psrerspapp ppavfpaarp epgeglsspa ggsyetgdrd dgrgdfgptl
      481 gllrpapepe aegsavkrmr ldtwtlk
//
LOCUS       NP_620812                155 aa            linear   ROD 28-APR-2025
DEFINITION  LIM domain only protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_620812 XP_346552
VERSION     NP_620812.2
DBSOURCE    REFSEQ: accession NM_139112.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Susa,T., Ishikawa,A., Cai,L.Y., Kato,T., Matsumoto,K., Kitahara,K.,
            Kurokawa,R., Ono,T. and Kato,Y.
  TITLE     The highly related LIM factors, LMO1, LMO3 and LMO4, play different
            roles in the regulation of the pituitary glycoprotein hormone
            alpha-subunit (alpha GSU) gene
  JOURNAL   Biosci Rep 30 (1), 51-58 (2009)
   PUBMED   19228115
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Chervinsky,D.S., Zhao,X.F., Lam,D.H., Ellsworth,M., Gross,K.W. and
            Aplan,P.D.
  TITLE     Disordered T-cell development and T-cell malignancies in SCL LMO1
            double-transgenic mice: parallels with E2A-deficient mice
  JOURNAL   Mol Cell Biol 19 (7), 5025-5035 (1999)
   PUBMED   10373552
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Ono,Y., Fukuhara,N. and Yoshie,O.
  TITLE     TAL1 and LIM-only proteins synergistically induce retinaldehyde
            dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia
            by acting as cofactors for GATA3
  JOURNAL   Mol Cell Biol 18 (12), 6939-6950 (1998)
   PUBMED   9819382
REFERENCE   5  (residues 1 to 155)
  AUTHORS   McGuire,E.A., Rintoul,C.E., Sclar,G.M. and Korsmeyer,S.J.
  TITLE     Thymic overexpression of Ttg-1 in transgenic mice results in T-cell
            acute lymphoblastic leukemia/lymphoma
  JOURNAL   Mol Cell Biol 12 (9), 4186-4196 (1992)
   PUBMED   1508213
REFERENCE   6  (residues 1 to 155)
  AUTHORS   McGuire,E.A., Davis,A.R. and Korsmeyer,S.J.
  TITLE     T-cell translocation gene 1 (Ttg-1) encodes a nuclear protein
            normally expressed in neural lineage cells
  JOURNAL   Blood 77 (3), 599-606 (1991)
   PUBMED   1703797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 24, 2007 this sequence version replaced NP_620812.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM033186.1, BF419154.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..155
                     /product="LIM domain only protein 3 isoform 2"
                     /note="neuronal-specific transcription factor DAT1;
                     dopamine-inducible LIM-domain transcription factor DAT1;
                     LIM domain only protein 1; LIM domain only protein 3"
                     /calculated_mol_wt=17575
     Region          23..77
                     /region_name="LIM1_LMO1_LMO3"
                     /note="The first LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09388"
                     /db_xref="CDD:188774"
     Site            order(23,26,44,47,50,53,73,76)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188774"
     Region          87..141
                     /region_name="LIM2_LMO1_LMO3"
                     /note="The second LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09389"
                     /db_xref="CDD:188775"
     Site            order(87,90,109,112,115,118,137,140)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188775"
     CDS             1..155
                     /gene="Lmo1"
                     /gene_synonym="Dat1"
                     /coded_by="NM_139112.3:191..658"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:245979"
                     /db_xref="RGD:621166"
ORIGIN      
        1 mvldqedgvp mlsvqpkgkq kgcagcnrki kdryllkald kywhedclkc accdcrlgev
       61 gstlytkanl ilcrrdylrl fgttgncaac sklipafemv mrardnvyhl dcfacqlcnq
      121 rfcvgdkffl knnmilcqmd yeeghlngtf esqvq
//
LOCUS       NP_001178692             369 aa            linear   ROD 28-APR-2025
DEFINITION  protein L-Myc isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178692 XP_233490
VERSION     NP_001178692.1
DBSOURCE    REFSEQ: accession NM_001191763.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kopecky,B.J., Decook,R. and Fritzsch,B.
  TITLE     N-Myc and L-Myc are essential for hair cell formation but not
            maintenance
  JOURNAL   Brain Res 1484, 1-14 (2012)
   PUBMED   23022312
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 17, 2010 this sequence version replaced XP_233490.5.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20674.1,
                                           SRR26643288.23575.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..369
                     /product="protein L-Myc isoform 1"
                     /note="Avian myelocytomatosis viral (v-myc) related
                     oncogene homolog 1, lung carcinoma derived (Lmyc); protein
                     L-Myc-1; v-myc myelocytomatosis viral oncogene homolog 1,
                     lung carcinoma derived; v-myc avian myelocytomatosis viral
                     oncogene lung carcinoma derived homolog"
                     /calculated_mol_wt=40937
     Region          2..220
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          281..369
                     /region_name="bHLHzip_L-Myc"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in L-Myc and similar proteins; cd11457"
                     /db_xref="CDD:381463"
     Site            order(283,287..288,291..292,294..296,298..299,303,
                     323..324)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381463"
     Site            order(302,305..306,308..309,312,325,328..329,332,334..336,
                     338..339,341..342,345,348..349,352..353,355..357,359..360,
                     362..369)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     Site            order(302,305..306,308..309,312,325,328..329,332,334..336,
                     338..339,341..342,345,348..349,352..353,355..356,359,
                     362..363,366..367,369)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     CDS             1..369
                     /gene="Mycl"
                     /gene_synonym="Lmyc1; Mycl1"
                     /coded_by="NM_001191763.3:571..1680"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298506"
                     /db_xref="RGD:1588591"
ORIGIN      
        1 mdfdsyqhyf ydydcgedfy rstapsediw kkfelvpspp tsppwgsgpg avdpasgisp
       61 gepwpgggag deaesrghsk awgrnyasii rrdcmwsgfs arerlervvs drlapgvprg
      121 nppkapatpd gtpsleasnp apatqcqlge pktqacsgse spsdsegeei dvvtvekrrs
      181 ldirkpvtit vradpldpcm khfhisihqq qhnyaarfpp escsqegdpe pgaqeealei
      241 eapkekeeee eeeeeeeeiv spppveneap qschpkpvss dtedvtkrkn hnflerkrrn
      301 dlrsrflalr dqvptlascs kapkvvilsk aleylqalvg aekkmatekr qlrcrqqqlq
      361 kriaylsgy
//
LOCUS       NP_001020893             370 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-dependent kinase 10 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001020893 XP_341713
VERSION     NP_001020893.2
DBSOURCE    REFSEQ: accession NM_001025722.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Guen,V.J., Gamble,C., Perez,D.E., Bourassa,S., Zappel,H.,
            Gartner,J., Lees,J.A. and Colas,P.
  TITLE     STAR syndrome-associated CDK10/Cyclin M regulates actin network
            architecture and ciliogenesis
  JOURNAL   Cell Cycle 15 (5), 678-688 (2016)
   PUBMED   27104747
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Guen,V.J., Gamble,C., Flajolet,M., Unger,S., Thollet,A.,
            Ferandin,Y., Superti-Furga,A., Cohen,P.A., Meijer,L. and Colas,P.
  TITLE     CDK10/cyclin M is a protein kinase that controls ETS2 degradation
            and is deficient in STAR syndrome
  JOURNAL   Proc Natl Acad Sci U S A 110 (48), 19525-19530 (2013)
   PUBMED   24218572
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Sergere,J.C., Thuret,J.Y., Le Roux,G., Carosella,E.D. and
            Leteurtre,F.
  TITLE     Human CDK10 gene isoforms
  JOURNAL   Biochem Biophys Res Commun 276 (1), 271-277 (2000)
   PUBMED   11006117
  REMARK    Erratum:[Biochem Biophys Res Commun 2000 Dec 20;279(2):738-9]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC098804.1 and AI071224.1.
            
            On Oct 12, 2007 this sequence version replaced NP_001020893.1.
            
            Summary: The protein encoded by this gene belongs to the CDK
            subfamily of the Ser/Thr protein kinase family. The CDK subfamily
            members are highly similar to the gene products of S. cerevisiae
            cdc28, and S. pombe cdc2, and are known to be essential for cell
            cycle progression. The human ortholog has been shown to play a role
            in cellular proliferation. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This minor variant (3) contains an alternate 5'
            end exon compared to transcript variant 1, and encodes a longer
            isoform (3) with a distinct N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..370
                     /product="cyclin-dependent kinase 10 isoform 3"
                     /EC_number="2.7.11.22"
                     /note="cell division protein kinase 10; cyclin-dependent
                     kinase (CDC2-like) 10"
                     /calculated_mol_wt=41840
     Region          41..349
                     /region_name="STKc_CDK10"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 10; cd07845"
                     /db_xref="CDD:173742"
     Site            order(55..58,63,76,78,95,109,127..130,133,135..136,173,
                     175,177..178,180,191,194,206,208..211,213,251..252)
                     /site_type="active"
                     /db_xref="CDD:173742"
     Site            order(55..58,63,76,78,109,127..130,133,136,177..178,180,
                     191)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173742"
     Site            order(87..89,91,94..95,97..98,101..102,114,116,123,162,
                     165..168,196,198..201,205..206,319,323..325)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:173742"
     Site            order(95,135,173,175,194,206,208..211,213,251..252)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173742"
     Site            order(190..201,203..213)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173742"
     CDS             1..370
                     /gene="Cdk10"
                     /coded_by="NM_001025722.2:430..1542"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361434"
                     /db_xref="RGD:1304851"
ORIGIN      
        1 mvafclvskm qvmsqcqiwv rhhlccsfqi ptlaaslfql grcrsvkefe klnrigegty
       61 givyrardtq tdeivalkkv rmdkekdgip isslreitll lrlrhpnive lkevvvgnhl
      121 esiflvmgyc eqdlasllen mptpfseaqv kcillqvlrg lqylhrsfii hrdlkvsnll
      181 mtdkgcvkta dfglaraygv pvkpmtpkvv tlwyrapell lgtttqttsi dmwavgcila
      241 ellahkpllp gtseihqidl ivqllgtpse niwpgfsklp lagqyslrkq pynnlkhkfp
      301 wlseaglrll nflfmydpkk ratagdcles syfkekplpc epelmptfph hrnkraapaa
      361 tegqskrcrp
//
LOCUS       NP_001388492            1538 aa            linear   ROD 28-APR-2025
DEFINITION  LIM and calponin homology domains-containing protein 1 isoform d
            [Rattus norvegicus].
ACCESSION   NP_001388492 XP_038947825
VERSION     NP_001388492.1
DBSOURCE    REFSEQ: accession NM_001401563.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1538)
  AUTHORS   Lin,Y.H., Zhen,Y.Y., Chien,K.Y., Lee,I.C., Lin,W.C., Chen,M.Y. and
            Pai,L.M.
  TITLE     LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell
            migration
  JOURNAL   Mol Biol Cell 28 (8), 1054-1065 (2017)
   PUBMED   28228547
REFERENCE   2  (residues 1 to 1538)
  AUTHORS   Mella,C., Martinez,F., de Los Angeles Garcia,M., Nualart,F.,
            Castro,V., Bustos,P., Carvajal,N. and Uribe,E.
  TITLE     Expression and localization of an agmatinase-like protein in the
            rat brain
  JOURNAL   Histochem Cell Biol 134 (2), 137-144 (2010)
   PUBMED   20607275
  REMARK    GeneRIF: An agmatinase-like protein was detected in the
            hypothalamus in glial cells and arcuate nucleus neurons, and in
            hippocampus astrocytes and neurons, but not in brain cortex
REFERENCE   3  (residues 1 to 1538)
  AUTHORS   Uribe,E., Salas,M., Enriquez,S., Orellana,M.S. and Carvajal,N.
  TITLE     Cloning and functional expression of a rodent brain cDNA encoding a
            novel protein with agmatinase activity, but not belonging to the
            arginase family
  JOURNAL   Arch Biochem Biophys 461 (1), 146-150 (2007)
   PUBMED   17291445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 16, 2022 this sequence version replaced XP_038947825.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1538
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..1538
                     /product="LIM and calponin homology domains-containing
                     protein 1 isoform d"
                     /note="LIM and calponin homology domains-containing
                     protein 1"
                     /calculated_mol_wt=171935
     Region          23..140
                     /region_name="CH_LIMCH1"
                     /note="calponin homology (CH) domain found in LIM and
                     calponin homology domains-containing protein 1; cd21278"
                     /db_xref="CDD:409127"
     Site            order(23,27,77,79..80,83..84,86,96..104,122,124..125,
                     127..128,131..132,135)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409127"
     Region          250..>311
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          <276..>412
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <736..868
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          <1222..1259
                     /region_name="GBP_C"
                     /note="Guanylate-binding protein, C-terminal domain;
                     cd16269"
                     /db_xref="CDD:293879"
     Region          1468..1525
                     /region_name="LIM"
                     /note="Zinc-binding domain present in Lin-11, Isl-1,
                     Mec-3; smart00132"
                     /db_xref="CDD:214528"
     Site            order(1468,1471,1491,1494,1497,1500,1522,1525)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..1538
                     /gene="Limch1"
                     /gene_synonym="RGD1305269"
                     /coded_by="NM_001401563.1:22..4638"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:305332"
                     /db_xref="RGD:1305269"
ORIGIN      
        1 macpalglev lqplqpeppp epafaeaqkw ieqvtgrsfg dkdfrtglen gillcellna
       61 ikpglvkkin rlptpiagld ntilflrgck elglkesqlf dpsdlqdtsn rvtvknfdys
      121 rklknvlvti ywlgkaansc tsysgttlnl kefegllaqm rketddiesp krsirdsgyi
      181 dcwdsersds lspprhgrdd sfdsldsfgs rsrqtpspdv vlrgssdgrg sdsesdlphr
      241 klpdvkkddm sarrtshgep ksavpfnqyl pnksnqtayv paplrkkkae reeyrkswst
      301 atsplggerp fsypetieee gseagspted dpssqmdpdg kpecgleapp sngkaqsped
      361 aaavpaaipe dreaverqkr rrleqagikv mpaaqrfasq kqsseekeai rdiilrkenp
      421 flahqhgkds esedeaacll pdlekddfaa rrarmnqrkp mvplnqllyg pyrkndeaka
      481 gssqhlskgp sdkknlgykr dqghredvnr vvacvmqtqe seplemsfrk apdlqkddla
      541 qrriqgrlsq hreapsfikl sgiteadlet werlkvsget rdgdaqntca pepspeidae
      601 tairddfasr karaykkapg prqkfvhfgp vteidqqtwq rlsigkagpr dnvevlshss
      661 esrtssrspp stttfdlkee qmlspqsdyr tvpsgtdgrl kkapwlapvl esqeeqvcvq
      721 snnpkteevt ptclpqekee vikkepemlp rvqrpegssg plygprtpvs ddaestsmfd
      781 mrceeeaavl phsrarqeql qlinnqlree ddkwqddlar wksrrrsasq dlikkeeerk
      841 kmeklmsged gtserrksik tyreivqeke rrerelheay knarsqeeae gilqqyierf
      901 tiseavlerl empkilersh stepnvssfp ndpspmkylr qqslpppkft atvettiart
      961 svpessvaag tgspsktstp ntvpmltprp ysqpknsqev lktfkvdgkv smngetargd
     1021 vegkekedpt avapgpsltk sqmfegvatv hgspvqvkqg snsieinikk pnsppqelta
     1081 aseetesngr ddengeessg ardveldsae pqhftttvtr csptvalvef ssspqlrnev
     1141 peeqdqkkpe nemsgkvelv lsqkvakpks pepeatltfp fldkmpetdq lhlpnlnsqa
     1201 dspssekspa stpfkfwawd peeerrrqek wqqeqerllq eryqkeqdkl keewekaqke
     1261 veeeerryye eerkiiedtv vpftissssa dqlstsssvt egsgtrnkmd lencqdrdke
     1321 rrqntplqen dsdsslkare sglpeehssl tqspsansen svskgisqdq qpeteaeash
     1381 cgtnpqsaqd ppwnqqisnp ptsksedvkp ktlaleksin hqiespgerr kksprenfra
     1441 gplspcsptp pgqspnrykr sisgkklcss cglalgkgaa miietlnlyf hiqcfrcgic
     1501 kgqlgdavsg tdvrirngll nctdcymrsr sagqpttl
//
LOCUS       NP_113701                166 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin-3 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_113701
VERSION     NP_113701.2
DBSOURCE    REFSEQ: accession NM_031513.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Piprode,V., Singh,K., Kumar,A., Josh,S.R. and Wani,M.R.
  TITLE     IL-3 inhibits rat osteoclast differentiation induced by TNF-alpha
            and other pro-osteoclastogenic cytokines
  JOURNAL   J Biosci 46 (2021)
   PUBMED   34183475
  REMARK    GeneRIF: IL-3 inhibits rat osteoclast differentiation induced by
            TNF-alpha and other pro-osteoclastogenic cytokines.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Lee,J., Lim,S., Song,B.W., Cha,M.J., Ham,O., Lee,S.Y., Lee,C.,
            Park,J.H., Bae,Y., Seo,H.H., Seung,M., Choi,E. and Hwang,K.C.
  TITLE     MicroRNA-29b inhibits migration and proliferation of vascular
            smooth muscle cells in neointimal formation
  JOURNAL   J Cell Biochem 116 (4), 598-608 (2015)
   PUBMED   25389122
  REMARK    GeneRIF: Findings demonstrated that miR-29b successfully suppressed
            the proliferation and migration of smooth muscle cells induced by
            IL-3 stimulation, probably through targeting of Mcl-1 and MMP2.
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Miyake,Y., Tanaka,K. and Arakawa,M.
  TITLE     IL3 rs40401 polymorphism and interaction with smoking in risk of
            asthma in Japanese women: the Kyushu Okinawa Maternal and Child
            Health study
  JOURNAL   Scand J Immunol 79 (6), 410-414 (2014)
   PUBMED   24684517
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Miyake,Y., Tanaka,K. and Arakawa,M.
  TITLE     IL3 SNP rs40401 variant is a risk factor for rhinoconjunctivitis in
            Japanese women: the Kyushu Okinawa maternal and child health study
  JOURNAL   Cytokine 64 (1), 86-89 (2013)
   PUBMED   23953855
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Dougan,M., Li,D., Neuberg,D., Mihm,M., Googe,P., Wong,K.K. and
            Dranoff,G.
  TITLE     A dual role for the immune response in a mouse model of
            inflammation-associated lung cancer
  JOURNAL   J Clin Invest 121 (6), 2436-2446 (2011)
   PUBMED   21537082
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Ito,T., Jagus,R. and May,W.S.
  TITLE     Interleukin 3 stimulates protein synthesis by regulating
            double-stranded RNA-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7455-7459 (1994)
   PUBMED   7519779
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Tsuji,K., Lyman,S.D., Sudo,T., Clark,S.C. and Ogawa,M.
  TITLE     Enhancement of murine hematopoiesis by synergistic interactions
            between steel factor (ligand for c-kit), interleukin-11, and other
            early acting factors in culture
  JOURNAL   Blood 79 (11), 2855-2860 (1992)
   PUBMED   1375116
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Okada,S., Nakauchi,H., Nagayoshi,K., Nakamura,M., Miura,Y. and
            Suda,T.
  TITLE     Synergistic effect of IL-3 and IL-6 on highly enriched murine
            hemopoietic progenitors
  JOURNAL   Exp Hematol 20 (5), 546-551 (1992)
   PUBMED   1350248
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Haig,D.M., McMenamin,C., Redmond,J., Brown,D., Young,I.G.,
            Cohen,S.D. and Hapel,A.J.
  TITLE     Rat IL-3 stimulates the growth of rat mucosal mast cells in culture
  JOURNAL   Immunology 65 (2), 205-211 (1988)
   PUBMED   3263940
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Cohen,D.R., Hapel,A.J. and Young,I.G.
  TITLE     Cloning and expression of the rat interleukin-3 gene
  JOURNAL   Nucleic Acids Res 14 (9), 3641-3658 (1986)
   PUBMED   3086845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Dec 3, 2020 this sequence version replaced NP_113701.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U81492.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN09345331
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..166
                     /product="interleukin-3 isoform 1 precursor"
                     /note="IL-3; MCGF; mast cell growth factor;
                     P-cell-stimulating factor; hematopoietic growth factor;
                     multipotential colony-stimulating factor"
                     /calculated_mol_wt=15638
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3096
     Region          34..140
                     /region_name="IL3"
                     /note="Interleukin-3; pfam02059"
                     /db_xref="CDD:460431"
     CDS             1..166
                     /gene="Il3"
                     /coded_by="NM_031513.3:29..529"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:24495"
                     /db_xref="RGD:2897"
ORIGIN      
        1 mvlassttsi lcmllpllml fhqglqfsgs ahrllrtldc rtialeilvk lpypqvsgln
       61 nsddkanlrn stlrrvnlde flksqeefds qdtmdikskl qklkccipaa asdsvlpgvy
      121 nkdlddfkkk lrfyvihlkd lqpvsvsrpp qptsssdnfr pmtvec
//
LOCUS       NP_001417262             178 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC690326 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001417262 XP_038964315
VERSION     NP_001417262.1
DBSOURCE    REFSEQ: accession NM_001430333.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On May 10, 2024 this sequence version replaced XP_038964315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.20003.1, CV111224.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..178
                     /product="uncharacterized protein LOC690326 isoform 2
                     precursor"
                     /note="lipoprotein(a) like 2, pseudogene"
                     /calculated_mol_wt=17032
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2157
     CDS             1..178
                     /gene="Lpal2"
                     /coded_by="NM_001430333.1:210..746"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:690326"
                     /db_xref="RGD:1597362"
ORIGIN      
        1 maasrillvl lsisllalts aqranedden spqdqealee gdanqqnggi hkglneiknh
       61 lqdqlnqhge esiklrrgkn gqgrnrrsad dslegqdlqs enqrggdgqg drgrrgqkgq
      121 kgkggqkgqk gkggqkgqkg kggqkgqkgk ggrrnqqgqy nsssknqrkg epakdvlq
//
LOCUS       NP_001388005             109 aa            linear   ROD 28-APR-2025
DEFINITION  U6 snRNA-associated Sm-like protein LSm7 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001388005 XP_006241020
VERSION     NP_001388005.1
DBSOURCE    REFSEQ: accession NM_001401076.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Bertram,K., Agafonov,D.E., Dybkov,O., Haselbach,D., Leelaram,M.N.,
            Will,C.L., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
            Activation
  JOURNAL   Cell 170 (4), 701-713 (2017)
   PUBMED   28781166
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Agafonov,D.E., Kastner,B., Dybkov,O., Hofele,R.V., Liu,W.T.,
            Urlaub,H., Luhrmann,R. and Stark,H.
  TITLE     Molecular architecture of the human U4/U6.U5 tri-snRNP
  JOURNAL   Science 351 (6280), 1416-1420 (2016)
   PUBMED   26912367
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Wahl,M.C., Will,C.L. and Luhrmann,R.
  TITLE     The spliceosome: design principles of a dynamic RNP machine
  JOURNAL   Cell 136 (4), 701-718 (2009)
   PUBMED   19239890
  REMARK    Review article
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Chen,Y.I., Moore,R.E., Ge,H.Y., Young,M.K., Lee,T.D. and
            Stevens,S.W.
  TITLE     Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes
            expands the catalog of participating factors
  JOURNAL   Nucleic Acids Res 35 (12), 3928-3944 (2007)
   PUBMED   17537823
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Achsel,T., Brahms,H., Kastner,B., Bachi,A., Wilm,M. and Luhrmann,R.
  TITLE     A doughnut-shaped heteromer of human Sm-like proteins binds to the
            3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in
            vitro
  JOURNAL   EMBO J 18 (20), 5789-5802 (1999)
   PUBMED   10523320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Feb 1, 2022 this sequence version replaced XP_006241020.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1370492.1,
                                           SRR26360172.417660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..109
                     /product="U6 snRNA-associated Sm-like protein LSm7 isoform
                     3"
                     /note="U6 snRNA-associated Sm-like protein LSm7; LSM7
                     homolog, U6 small nuclear RNA associated; LSM7 U6 small
                     nuclear RNA and mRNA degradation associated"
                     /calculated_mol_wt=12245
     Region          17..103
                     /region_name="LSm7"
                     /note="Like-Sm protein 7; cd01729"
                     /db_xref="CDD:212476"
     Site            order(19,21,24..25,30,32..34,37,39,44..51,53,75,77,79..92)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:212476"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212476"
     Site            order(47,49,83)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212476"
     Site            79..90
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212476"
     CDS             1..109
                     /gene="Lsm7"
                     /coded_by="NM_001401076.1:24..353"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362829"
                     /db_xref="RGD:1305354"
ORIGIN      
        1 marptfqqdk ekkkkesild lskyidktir vkfqggreas gilkgfdpll nlvldgtiey
       61 mrdpddqykl tedtrqlglv vcrgtsvvli cpqdgmeaip npfvqqqdt
//
LOCUS       NP_001401905             560 aa            linear   ROD 28-APR-2025
DEFINITION  SH3 domain-binding protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001401905 XP_006251313
VERSION     NP_001401905.1
DBSOURCE    REFSEQ: accession NM_001414976.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Zeng,L., Ye,F., Jin,Y., Luo,Y. and Zhu,H.
  TITLE     Overexpression of DEL-1 Downregulates SH3BP2 Expression and
            Inhibits Porphyromonas gingivalis-induced Gingival Inflammation In
            Vivo and In Vitro
  JOURNAL   Oral Health Prev Dent 20, 199-206 (2022)
   PUBMED   35481344
  REMARK    GeneRIF: Overexpression of DEL-1 Downregulates SH3BP2 Expression
            and Inhibits Porphyromonas gingivalis-induced Gingival Inflammation
            In Vivo and In Vitro.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Mehlitz,A., Banhart,S., Maurer,A.P., Kaushansky,A., Gordus,A.G.,
            Zielecki,J., Macbeath,G. and Meyer,T.F.
  TITLE     Tarp regulates early Chlamydia-induced host cell survival through
            interactions with the human adaptor protein SHC1
  JOURNAL   J Cell Biol 190 (1), 143-157 (2010)
   PUBMED   20624904
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Ueki,Y., Tiziani,V., Santanna,C., Fukai,N., Maulik,C.,
            Garfinkle,J., Ninomiya,C., doAmaral,C., Peters,H., Habal,M.,
            Rhee-Morris,L., Doss,J.B., Kreiborg,S., Olsen,B.R. and
            Reichenberger,E.
  TITLE     Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause
            cherubism
  JOURNAL   Nat Genet 28 (2), 125-126 (2001)
   PUBMED   11381256
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Ren,R., Mayer,B.J., Cicchetti,P. and Baltimore,D.
  TITLE     Identification of a ten-amino acid proline-rich SH3 binding site
  JOURNAL   Science 259 (5098), 1157-1161 (1993)
   PUBMED   8438166
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Dec 16, 2022 this sequence version replaced XP_006251313.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ218289.1, SRR26360176.837805.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..560
                     /product="SH3 domain-binding protein 2 isoform 2"
                     /calculated_mol_wt=62253
     Region          19..133
                     /region_name="PH_3BP2"
                     /note="SH3 domain-binding protein 2 Pleckstrin homology
                     (PH) domain; cd13308"
                     /db_xref="CDD:270118"
     Region          455..555
                     /region_name="SH2_SH3BP2"
                     /note="Src homology 2 domain found in c-Abl SH3
                     domain-binding protein-2 (SH3BP2); cd10359"
                     /db_xref="CDD:198222"
     Site            order(463,487,509,511)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198222"
     Site            order(510,537)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198222"
     CDS             1..560
                     /gene="Sh3bp2"
                     /coded_by="NM_001414976.1:88..1770"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305450"
                     /db_xref="RGD:1310588"
ORIGIN      
        1 meaeemhwpv pmkaigaqnl ltmpggvaka gylhkkggtq lqllkwplrf viihqrciyy
       61 fksstsaspq gafslsgynr vmraaeetts nnvfpfkiih iskkhrtwff sassederks
      121 wmamlrreig hfhekkelpl dtsdsssdtd sfygaverpi dislssyptd nedyehedee
      181 dsylepdspg pmkledalty ppayppppvp vprkptfsdl prahsftsks pspllppppp
      241 krglmdtgpa pedakkdplg lrrvepslrv patprrmsdp pvsnvptvpn lrkhpcfrds
      301 anpgpepwtp ghgtssvsss ttmaittsrn cdklksfhls srgppasepp pvpankpkfl
      361 kiveeaspre aaksapvppv aprppvqkms mpevtvrpav lprpektplp hlqrsppdgq
      421 sfrgfsfeka rqpsqadtge edsdedyekv plpnsvfvnt tesceverlf katnplgepq
      481 dglycirnss tksgkvlvvw dessnkvrny rifekdskfy legevlfasv gsmvehyhth
      541 vlpshqslll rhpygyagpr
//
LOCUS       NP_001418618             305 aa            linear   ROD 28-APR-2025
DEFINITION  neuronal membrane glycoprotein M6-b isoform 7 [Rattus norvegicus].
ACCESSION   NP_001418618 XP_006256912
VERSION     NP_001418618.1
DBSOURCE    REFSEQ: accession NM_001431689.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Bang,M.L., Vainshtein,A., Yang,H.J., Eshed-Eisenbach,Y., Devaux,J.,
            Werner,H.B. and Peles,E.
  TITLE     Glial M6B stabilizes the axonal membrane at peripheral nodes of
            Ranvier
  JOURNAL   Glia 66 (4), 801-812 (2018)
   PUBMED   29282769
  REMARK    GeneRIF: Study identified glycoprotein M6B as a Schwann cell
            microvilli component of peripheral nodes of Ranvier. Study detected
            Na(+) channel clusters at heminodes without any associated M6B,
            indicating that it is not required for initial channel clustering;
            showed that absence of M6B results in progressive appearance of
            nodal protrusions of the nodal axolemma, that are often accompanied
            by the presence of enlarged mitochondria.
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Drabek,K., van de Peppel,J., Eijken,M. and van Leeuwen,J.P.
  TITLE     GPM6B regulates osteoblast function and induction of mineralization
            by controlling cytoskeleton and matrix vesicle release
  JOURNAL   J Bone Miner Res 26 (9), 2045-2051 (2011)
   PUBMED   21638316
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Fjorback,A.W., Muller,H.K. and Wiborg,O.
  TITLE     Membrane glycoprotein M6B interacts with the human serotonin
            transporter
  JOURNAL   J Mol Neurosci 37 (3), 191-200 (2009)
   PUBMED   18581270
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Shimokawa,N. and Miura,M.
  TITLE     Rhombex-29, a novel gene of the PLP/DM20-M6 family cloned from rat
            medulla oblongata by differential display
  JOURNAL   J Neurosci Res 62 (1), 1-8 (2000)
   PUBMED   11002282
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Yan,Y., Lagenaur,C. and Narayanan,V.
  TITLE     Molecular cloning of M6: identification of a PLP/DM20 gene family
  JOURNAL   Neuron 11 (3), 423-431 (1993)
   PUBMED   8398137
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 19, 2024 this sequence version replaced XP_006256912.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.31566.1,
                                           SRR26360176.767614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840108, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13-q14"
     Protein         1..305
                     /product="neuronal membrane glycoprotein M6-b isoform 7"
                     /note="neuronal membrane glycoprotein M6-b; Rhombex-29;
                     rhombencephalic expression protein-29 kDa"
                     /calculated_mol_wt=33384
     Region          63..298
                     /region_name="Myelin_PLP"
                     /note="Myelin proteolipid protein (PLP or lipophilin);
                     pfam01275"
                     /db_xref="CDD:460144"
     CDS             1..305
                     /gene="Gpm6b"
                     /gene_synonym="M6b"
                     /coded_by="NM_001431689.1:243..1160"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:192179"
                     /db_xref="RGD:620580"
ORIGIN      
        1 mkpametaae enteqsqerk vnsraemeig ryhwmypgsk nhqyrpvptl gdragplssp
       61 gcfeccikcl ggvpyaslva tilcfsgval fcgcghvala gtvaileqhf stntsdhall
      121 seviqlmqyv iygiasfffl ygiillaegf yttsavkelh gefkttacgr cisgmfvflt
      181 yvlgvawlgv fgfsavpvfm fyniwstcev ikspqsngts gveqicvdvr qygiipwnaf
      241 pgkicgsale nicntnefym syhlfivaca gagatviall iymmattyny avlkfksred
      301 cctkf
//
LOCUS       NP_001128249             293 aa            linear   ROD 28-APR-2025
DEFINITION  peroxisomal biogenesis factor 19 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001128249 XP_213930
VERSION     NP_001128249.1
DBSOURCE    REFSEQ: accession NM_001134777.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Kinoshita,N., Matsuura,A. and Fujiki,Y.
  TITLE     Peroxisome biogenesis: a novel inducible PEX19 splicing variant is
            involved in early stages of peroxisome proliferation
  JOURNAL   J Biochem 161 (3), 297-308 (2017)
   PUBMED   28391327
  REMARK    GeneRIF: The PEX19i most likely plays important roles involving the
            membrane formation at early stages, in prompt response to
            peroxisome proliferation. Similar types of PEX19 mRNA variants were
            also elevated in mouse regenerating liver.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Pinto,M.P., Grou,C.P., Fransen,M., Sa-Miranda,C. and Azevedo,J.E.
  TITLE     The cytosolic domain of PEX3, a protein involved in the biogenesis
            of peroxisomes, binds membrane lipids
  JOURNAL   Biochim Biophys Acta 1793 (11), 1669-1675 (2009)
   PUBMED   19715730
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Neufeld,C., Filipp,F.V., Simon,B., Neuhaus,A., Schuller,N.,
            David,C., Kooshapur,H., Madl,T., Erdmann,R., Schliebs,W.,
            Wilmanns,M. and Sattler,M.
  TITLE     Structural basis for competitive interactions of Pex14 with the
            import receptors Pex5 and Pex19
  JOURNAL   EMBO J 28 (6), 745-754 (2009)
   PUBMED   19197237
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Matsuzaki,T. and Fujiki,Y.
  TITLE     The peroxisomal membrane protein import receptor Pex3p is directly
            transported to peroxisomes by a novel Pex19p- and Pex16p-dependent
            pathway
  JOURNAL   J Cell Biol 183 (7), 1275-1286 (2008)
   PUBMED   19114594
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Biermanns,M. and Gartner,J.
  TITLE     Targeting elements in the amino-terminal part direct the human
            70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes
  JOURNAL   Biochem Biophys Res Commun 285 (3), 649-655 (2001)
   PUBMED   11453642
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Jones,J.M., Morrell,J.C. and Gould,S.J.
  TITLE     Multiple distinct targeting signals in integral peroxisomal
            membrane proteins
  JOURNAL   J Cell Biol 153 (6), 1141-1150 (2001)
   PUBMED   11402059
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Sacksteder,K.A., Jones,J.M., South,S.T., Li,X., Liu,Y. and
            Gould,S.J.
  TITLE     PEX19 binds multiple peroxisomal membrane proteins, is
            predominantly cytoplasmic, and is required for peroxisome membrane
            synthesis
  JOURNAL   J Cell Biol 148 (5), 931-944 (2000)
   PUBMED   10704444
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Matsuzono,Y., Kinoshita,N., Tamura,S., Shimozawa,N., Hamasaki,M.,
            Ghaedi,K., Wanders,R.J., Suzuki,Y., Kondo,N. and Fujiki,Y.
  TITLE     Human PEX19: cDNA cloning by functional complementation, mutation
            analysis in a patient with Zellweger syndrome, and potential role
            in peroxisomal membrane assembly
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2116-2121 (1999)
   PUBMED   10051604
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Kammerer,S., Arnold,N., Gutensohn,W., Mewes,H.W., Kunau,W.H.,
            Hofler,G., Roscher,A.A. and Braun,A.
  TITLE     Genomic organization and molecular characterization of a gene
            encoding HsPXF, a human peroxisomal farnesylated protein
  JOURNAL   Genomics 45 (1), 200-210 (1997)
   PUBMED   9339377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB718412.1, CK600534.1, BQ782704.1 and BE108398.1.
            
            On Sep 6, 2008 this sequence version replaced XP_213930.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..293
                     /product="peroxisomal biogenesis factor 19 isoform 2"
                     /note="peroxin-19; peroxisomal farnesylated protein;
                     peroxisome biogenesis factor 19"
                     /calculated_mol_wt=31730
     Region          2..91
                     /region_name="Necessary for PEX19 function on peroxisome
                     biogenesis. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          2..56
                     /region_name="Docking to the peroxisome membrane and
                     binding to PEX3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P40855; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          25..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40855; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          74..278
                     /region_name="Pex19"
                     /note="Pex19 protein family; pfam04614"
                     /db_xref="CDD:461367"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCI5; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     CDS             1..293
                     /gene="Pex19"
                     /gene_synonym="PxF"
                     /coded_by="NM_001134777.1:27..908"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289233"
                     /db_xref="RGD:1306913"
ORIGIN      
        1 maaaeggcga gveadrelee llesalddfd kakpspapsp tisapdasgp qkrspgdtak
       61 dalfasqekf fqelfdsela sqataefeka mkelaeeeph lveqfqklse aagrvgsdas
      121 sqqeftsclk etlsglakna tdlqnagmse eeltkamegl gmdegdgegn ilpimqslmq
      181 nllskdvlyp slkeitekyp ewlqshqesi ppeqfekyqq qhsvmgkice qfeaetptds
      241 eathrarfea vldlmqqlqd lghppkelag emytgpsgsl lillagtlfp sar
//
LOCUS       NP_001424895             902 aa            linear   ROD 28-APR-2025
DEFINITION  tight junction protein ZO-3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424895 XP_006240995
VERSION     NP_001424895.1
DBSOURCE    REFSEQ: accession NM_001437966.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Qiao,X., Roth,I., Feraille,E. and Hasler,U.
  TITLE     Different effects of ZO-1, ZO-2 and ZO-3 silencing on kidney
            collecting duct principal cell proliferation and adhesion
  JOURNAL   Cell Cycle 13 (19), 3059-3075 (2014)
   PUBMED   25486565
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Capaldo,C.T., Koch,S., Kwon,M., Laur,O., Parkos,C.A. and Nusrat,A.
  TITLE     Tight function zonula occludens-3 regulates cyclin D1-dependent
            cell proliferation
  JOURNAL   Mol Biol Cell 22 (10), 1677-1685 (2011)
   PUBMED   21411630
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Aho,S., Lupo,J., Coly,P.A., Sabine,A., Castellazzi,M., Morand,P.,
            Sergeant,A., Manet,E., Boyer,V. and Gruffat,H.
  TITLE     Characterization of the ubinuclein protein as a new member of the
            nuclear and adhesion complex components (NACos)
  JOURNAL   Biol Cell 101 (6), 319-334 (2009)
   PUBMED   18823282
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Adachi,M., Inoko,A., Hata,M., Furuse,K., Umeda,K., Itoh,M. and
            Tsukita,S.
  TITLE     Normal establishment of epithelial tight junctions in mice and
            cultured cells lacking expression of ZO-3, a tight-junction MAGUK
            protein
  JOURNAL   Mol Cell Biol 26 (23), 9003-9015 (2006)
   PUBMED   17000770
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Inoko,A., Itoh,M., Tamura,A., Matsuda,M., Furuse,M. and Tsukita,S.
  TITLE     Expression and distribution of ZO-3, a tight junction MAGUK
            protein, in mouse tissues
  JOURNAL   Genes Cells 8 (11), 837-845 (2003)
   PUBMED   14622136
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Unda,F.J., Perez-Nanclares,G., Le Morvan,V., Hernandez,C.,
            Vilaxa,A., De-la-Fuente,M. and Gorry,P.
  TITLE     Dynamic assembly of tight junction-associated proteins ZO-1, ZO-2,
            ZO-3 and occludin during mouse tooth development
  JOURNAL   Histol Histopathol 18 (1), 27-38 (2003)
   PUBMED   12507281
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_006240995.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.27059.1,
                                           SRR26643291.19419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..902
                     /product="tight junction protein ZO-3 isoform 2"
                     /note="tight junction protein ZO-3"
                     /calculated_mol_wt=99070
     Region          10..91
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(21..27,40,43,71,75,78..79)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          185..263
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(185..191,196..212,215..217,220,222..223,230,
                     238..239,241..242,254..260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(197..203,209,212,242,246,249..250)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          368..449
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(379..385,395,398,427,431,434..435)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          464..537
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(472,474,477,481,502..503,531,533..534)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          580..756
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..902
                     /gene="Tjp3"
                     /coded_by="NM_001437966.1:205..2913"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314640"
                     /db_xref="RGD:1309247"
ORIGIN      
        1 meeltiweqh tatlykdprr gfgiavsggh draggpvvvs dvvpggpaeg rlqtgdhivm
       61 vngvsvenvt safaiqilkt ctktanitvk rprrvqlpat kaspasghql sdqeeadhgr
      121 gyegdsssgs grswgersrr sragrrvrmg shgrrsscgg seangldlvs gykrlpkqdv
      181 lmrplksvlv krrnseefgv klgsqifikh itesglaarn rglqegdlil qingvssanl
      241 slsdtrrlie ksegqltllv lrdsgqflvn ippavsdsds slmedisdlt selsqappsh
      301 ipppplksrr spedsqtdsp vetpqpqrre rsvdsraiae pespgesryd iyrvpsrqsl
      361 edrgyspdtr vvrfpkgvsi glrlaggndv gifvsgvqag spadgqgiqe gdeilqvndm
      421 pfrnltreea vqfllglpag edvelviqsk qdifrkmvqs rvgdsfyirt hfelepsppy
      481 glgftrgdvf hvvdtlyrgs gsghghsshg glwlaarmgr dlreqergvi pnqsraeqla
      541 sleaaqraag lgpgastgsn praefwrlrg lrrgakktmt qrsredlsal trqghyppye
      601 rvvlreasfk rpvvilgpva diamkrltte vpeqfeiaes vsrtdspski ikldtvrvia
      661 erdkhalldv tpsaierlny vqyypvvifc apesrsalka lrewlapasr rssrrlyaqa
      721 qklqkhsghl ftatiplngt sdswyqevka viqqqqarpi wtaedqlngs sedldlpghg
      781 laassgdlsc dsransdyed tdgegtytdr egepqdfdee apptalarss epvwvddhqg
      841 lmghgriaaa evqadshytp dqrrqdsmrt ykhealrkkf trardiessd eegydwgpat
      901 dl
//
LOCUS       NP_001178655             660 aa            linear   ROD 28-APR-2025
DEFINITION  heparan-sulfate 6-O-sulfotransferase 2 [Rattus norvegicus].
ACCESSION   NP_001178655 XP_228681
VERSION     NP_001178655.1
DBSOURCE    REFSEQ: accession NM_001191726.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Habuchi,H., Tanaka,M., Habuchi,O., Yoshida,K., Suzuki,H., Ban,K.
            and Kimata,K.
  TITLE     The occurrence of three isoforms of heparan sulfate
            6-O-sulfotransferase having different specificities for hexuronic
            acid adjacent to the targeted N-sulfoglucosamine
  JOURNAL   J Biol Chem 275 (4), 2859-2868 (2000)
   PUBMED   10644753
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 17, 2010 this sequence version replaced XP_228681.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.33139.1,
                                           SRR26360194.1583346.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..660
                     /product="heparan-sulfate 6-O-sulfotransferase 2"
                     /EC_number="2.8.2.-"
                     /calculated_mol_wt=74383
     Region          225..531
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     CDS             1..660
                     /gene="Hs6st2"
                     /gene_synonym="RGD1563872; RGD1564397"
                     /coded_by="NM_001191726.1:1..1983"
                     /db_xref="GeneID:302489"
                     /db_xref="RGD:1564397"
ORIGIN      
        1 malpafaara lgpplqpeqg aparttcprr hsrveaelaa srpgsvaasv ragpprgvsl
       61 gfnspplqdk ppktfsslag alraplfall prgrrrrmhd lrrrwdlgsl cralltrgla
      121 avghslkhvl saifskifgp lasvgnmdek snklllalvm lflfavivlq yvcpgtecql
      181 lrlqafsspv pdpyrsedes sarfvprynf srgdllrkvd fdikgddliv flhiqktggt
      241 tfgrhlvrni qleqpcecrv gqkkctchrp gkretwlfsr fstgwscglh adwteltscv
      301 pavvdgkrda rlrpsrwrif qildaaskdr wgssnfnsga nspsstkprs ttksgknfhy
      361 itilrdpvsr ylsewrhvqr gatwkaslhv cdgrpptsee lpscytgddw sgcplkefmd
      421 cpynlannrq vrmlsdltlv gcynlsvmpe kqrnkvlles aksnlkhmaf fgltefqrkt
      481 qylfektfnm nfispftqyn ttrassvein eeiqkriegl nfldmelysy akdlflqryq
      541 fmrqkehqda rrkrqeqrkf lkgrflqthf qsqsqsqgqs qgqsqgqsqg pgqnlsqnpn
      601 pnpnqnltqn lsqnltqssn pnltqrenhg sqkqgsgqeq sdsstsngtn dyigsvetwr
//
LOCUS       NP_001424032             581 aa            linear   ROD 28-APR-2025
DEFINITION  SLAIN motif-containing protein 2 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001424032 XP_006250961
VERSION     NP_001424032.1
DBSOURCE    REFSEQ: accession NM_001437103.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   van der Vaart,B., Manatschal,C., Grigoriev,I., Olieric,V.,
            Gouveia,S.M., Bjelic,S., Demmers,J., Vorobjev,I., Hoogenraad,C.C.,
            Steinmetz,M.O. and Akhmanova,A.
  TITLE     SLAIN2 links microtubule plus end-tracking proteins and controls
            microtubule growth in interphase
  JOURNAL   J Cell Biol 193 (6), 1083-1099 (2011)
   PUBMED   21646404
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006250961.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.46651.1,
                                           SRR26643292.51611.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..581
                     /product="SLAIN motif-containing protein 2 isoform 3"
                     /note="SLAIN motif-containing protein 2"
                     /calculated_mol_wt=62342
     Region          130..581
                     /region_name="SLAIN"
                     /note="SLAIN motif-containing family; pfam15301"
                     /db_xref="CDD:464627"
     CDS             1..581
                     /gene="Slain2"
                     /gene_synonym="RGD1311593"
                     /coded_by="NM_001437103.1:197..1942"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:305310"
                     /db_xref="RGD:1311593"
ORIGIN      
        1 medvnsnvna dqevrklqel vkklekqneq lrsrsgavqs agllgpgspa ragvstpssg
       61 aasprgfplg lgakasggag sgprrtssed lrdatsllaa gegglldeve plrpdelerl
      121 sgweeeeesw lysspkkklt pmqksvsplv wcrqvldyps pdvecakksl ihkldqtmsa
      181 lkrqnlynnp fnsmsysspy spnasspyss gfnspsstpv rppivkqlil pgnsgnfkss
      241 sdrnpplspq ssidselsas eldedsigsn yklndvtdvq ilarmqeesl rqeyaattsr
      301 rssgsscnst rrgtfsdqel daqslddedd smhhavypav nrfspsprns prpspkqspr
      361 nsprsrspar gieysraspq pmisrlqqpr lslqghptdl qtsnvkneek lrrslpnlsr
      421 tsntqvdsvk ssrsdsnfqv pnggiprmqp qasaipspgk frspaapspl alrqpvkafs
      481 nhgsgsgsqe ttqftqttss pgppvvqnta panpssnins atltrpagta amrsglprps
      541 apsaggipvp rsklvqpvrr slpapktygs mkddswkdgc y
//
LOCUS       NP_064464                238 aa            linear   ROD 28-APR-2025
DEFINITION  prolactin family 8, subfamily A, member 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_064464 XP_002728522
VERSION     NP_064464.1
DBSOURCE    REFSEQ: accession NM_020079.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wiemers,D.O., Shao,L.J., Ain,R., Dai,G. and Soares,M.J.
  TITLE     The mouse prolactin gene family locus
  JOURNAL   Endocrinology 144 (1), 313-325 (2003)
   PUBMED   12488360
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Dai,G., Liu,B., Szpirer,C., Levan,G., Kwok,S.C. and Soares,M.J.
  TITLE     Prolactin-like protein-C variant: complementary deoxyribonucleic
            acid, unique six exon gene structure, and trophoblast cell-specific
            expression
  JOURNAL   Endocrinology 137 (11), 5009-5019 (1996)
   PUBMED   8895375
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U93351.1.
            
            On May 10, 2012 this sequence version replaced XP_002728522.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U93351.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Rattus norvegicus"
                     /strain="WKY"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..238
                     /product="prolactin family 8, subfamily A, member 3
                     precursor"
                     /note="prolactin-like protein C 1"
                     /calculated_mol_wt=23903
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3334
     Region          31..238
                     /region_name="prolactin_like"
                     /note="Prolactin (PRL or PRL1), chorionic
                     somatomammotropin, and related pituitary gland hormones;
                     cd10288"
                     /db_xref="CDD:198438"
     Site            order(31..33,41..43,48,51..52,57,60..61,98..99,108,
                     112..113,162,165,168..169,216..217,220..221,223..225,
                     227..228,231,238)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198438"
     CDS             1..238
                     /gene="Prl8a3"
                     /gene_synonym="Plp-Cv; Plpc; Plpcv; Prlpc; Prlpc1"
                     /coded_by="NM_020079.1:44..760"
                     /db_xref="GeneID:100361884"
                     /db_xref="RGD:3406"
ORIGIN      
        1 melaltqppf fgtllmlvvs nlllwekaas ipacmvedgg cwdpleetvn saiqkaenlr
       61 nlahhlyvef yqnqfssrqf adlnsqlmrw detvvktgty chstlarpqn kginieievy
      121 lqtlinfvgs wispllhlvi elsamegvpe tilskakdle ennrqllddl rwiltkvspt
      181 aemkeefpsw gylsflksss knhkflavfn lsncleddtk ftlyhlrilk clitgkdc
//
LOCUS       NP_001402667            1187 aa            linear   ROD 28-APR-2025
DEFINITION  nonsense-mediated mRNA decay factor SMG7 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001402667 XP_006250068
VERSION     NP_001402667.1
DBSOURCE    REFSEQ: accession NM_001415738.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1187)
  AUTHORS   Azzalin,C.M., Reichenbach,P., Khoriauli,L., Giulotto,E. and
            Lingner,J.
  TITLE     Telomeric repeat containing RNA and RNA surveillance factors at
            mammalian chromosome ends
  JOURNAL   Science 318 (5851), 798-801 (2007)
   PUBMED   17916692
REFERENCE   2  (residues 1 to 1187)
  AUTHORS   Ohnishi,T., Yamashita,A., Kashima,I., Schell,T., Anders,K.R.,
            Grimson,A., Hachiya,T., Hentze,M.W., Anderson,P. and Ohno,S.
  TITLE     Phosphorylation of hUPF1 induces formation of mRNA surveillance
            complexes containing hSMG-5 and hSMG-7
  JOURNAL   Mol Cell 12 (5), 1187-1200 (2003)
   PUBMED   14636577
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Dec 28, 2022 this sequence version replaced XP_006250068.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q21"
     Protein         1..1187
                     /product="nonsense-mediated mRNA decay factor SMG7 isoform
                     2"
                     /EC_number="2.7.11.1"
                     /note="protein SMG7; Smg-7 homolog, nonsense mediated mRNA
                     decay factor; nonsense-mediated mRNA decay factor SMG7"
                     /calculated_mol_wt=132068
     Region          55..167
                     /region_name="EST1"
                     /note="Telomerase activating protein Est1; pfam10374"
                     /db_xref="CDD:463062"
     Region          154..180
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(156..157,160..161,163,187,190..191,194..195,
                     197..198,221,224..225,228..229,232)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          171..430
                     /region_name="EST1_DNA_bind"
                     /note="Est1 DNA/RNA binding domain; pfam10373"
                     /db_xref="CDD:431239"
     Region          185..215
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1187
                     /gene="Smg7"
                     /gene_synonym="RGD1310761"
                     /coded_by="NM_001415738.2:109..3672"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360855"
                     /db_xref="RGD:1310761"
ORIGIN      
        1 mslqsaqylr qaevlkaemt dsklgpaevw tsrqalqdly qkmlvtdley aldkkveqdl
       61 wnhafknqit tlqgqaknra npnrsevqan lslfleaasg fytqllqelc tvfnvdlpcr
      121 vkssqlgiis nkqthtsaiv kpqssscsyi cqhclvhlgd iaryrnqtsq aesyyrhaaq
      181 lvpsngqpyn qlailasskg dhlttifyyc rsiavkfpfp aastnlqkal skalesrdel
      241 ktkwgvsdfi kafikfhghv ylskslekls plrekleeqf krllfqkafn sqqlvhvtvi
      301 nlfqlhhlrd fsneteqhsy sqdeqlcwtq llalfmsflg ilckcplqnd sqesynaypl
      361 pavkvsmdwl rlrprvfqea vvderqyiwp wlisllnsfh preddlsstn atplpeefel
      421 qgflalrpsf rnldfskghq gitgdkegqq rrirqqrlis igkwiadnqp rliqcenevg
      481 kllfiteipe liledpseak enlilqetsa ieshasdgsp glksvlstgr spstscdsge
      541 kpvvtfkeni kprevnrdqg rsfppkevrr dcskgvtvtq ddgqkdsskr raetkrctlg
      601 klqetgkqsv avqvksqtel rktpvseark tpvtqtpsqt nnsqfipihh pgafpplpsr
      661 pgfppptyvi pppvafsmgs gytfpagvsv pgtflqstah spagnqvqag kqshipysqq
      721 rpsgpgpmnq gpqqsqppsq ppltslpaqp taqstsqlqv qalaqqqqsp tkvipalgks
      781 pphhsgfqqy qqadaskqlw nppqvqsplg kimpvkqpyy lqtqdpiklf epslqppviq
      841 qqplekkmkp fpmepynhnp sevkvpefyw dssysmadnr avmaqqpnmd rrskrspgvf
      901 rpeqdpvprm pfedpksspl lppdllksla aleeeeelif snppdlypal lgplaslpgr
      961 slfksllekp selmshsssf lsltgfsvnq erypnssvfn evygknltas skaelspsva
     1021 ssqetslysl fegtpwspsl passdhstpa sqsphssnps slpssppthn hnsapfsnfg
     1081 pigtpdnrdr rpadrwktdk pamggfgvdy lsatsssens whqastpsgt wtghgpsmed
     1141 ssavlmeslk siwsssmmhp gpsaleqllm qqkqkqqrgq gamnpph
//
LOCUS       NP_001257703             958 aa            linear   ROD 28-APR-2025
DEFINITION  sodium/calcium exchanger 1 isoform 4 precursor [Rattus norvegicus].
ACCESSION   NP_001257703
VERSION     NP_001257703.1
DBSOURCE    REFSEQ: accession NM_001270774.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Yijian,L., Weihan,S., Lin,Y., Heng,Z., Yu,W., Lin,S., Shuo,M.,
            Mengyang,L. and Jianxun,W.
  TITLE     CircNCX1 modulates cardiomyocyte proliferation through promoting
            ubiquitination of BRG1
  JOURNAL   Cell Signal 120, 111193 (2024)
   PUBMED   38679350
  REMARK    GeneRIF: CircNCX1 modulates cardiomyocyte proliferation through
            promoting ubiquitination of BRG1.
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Kang,Q., Zhang,J., Xie,C., Fang,S. and Chai,W.
  TITLE     Circular RNA SLC8A1 triggers hippocampal neuronal ferroptosis by
            regulating FUS-mediated ATF3 mRNA stability in epilepsy
  JOURNAL   Exp Cell Res 434 (1), 113848 (2024)
   PUBMED   37918704
  REMARK    GeneRIF: Circular RNA SLC8A1 triggers hippocampal neuronal
            ferroptosis by regulating FUS-mediated ATF3 mRNA stability in
            epilepsy.
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Yang,L., Zhang,L., Zhu,J., Wang,Y., Zou,N., Liu,Z. and Wang,Y.
  TITLE     Abnormal expression and role of MicroRNA-214-3p/SLC8A1 in neonatal
            Hypoxic-Ischaemic encephalopathy
  JOURNAL   Int J Exp Pathol 104 (4), 199-208 (2023)
   PUBMED   37032493
  REMARK    GeneRIF: Abnormal expression and role of MicroRNA-214-3p/SLC8A1 in
            neonatal Hypoxic-Ischaemic encephalopathy.
REFERENCE   4  (residues 1 to 958)
  AUTHORS   Petrozziello,T., Boscia,F., Tedeschi,V., Pannaccione,A., de
            Rosa,V., Corvino,A., Severino,B., Annunziato,L. and Secondo,A.
  TITLE     Na+/Ca2+ exchanger isoform 1 takes part to the Ca2+-related
            prosurvival pathway of SOD1 in primary motor neurons exposed to
            beta-methylamino-L-alanine
  JOURNAL   Cell Commun Signal 20 (1), 8 (2022)
   PUBMED   35022040
  REMARK    GeneRIF: Na(+)/Ca(2+) exchanger isoform 1 takes part to the
            Ca(2+)-related prosurvival pathway of SOD1 in primary motor neurons
            exposed to beta-methylamino-L-alanine.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 958)
  AUTHORS   Tedeschi,V., Sisalli,M.J., Pannaccione,A., Piccialli,I.,
            Molinaro,P., Annunziato,L. and Secondo,A.
  TITLE     Na+/Ca2+ exchanger isoform 1 (NCX1) and canonical transient
            receptor potential channel 6 (TRPC6) are recruited by STIM1 to
            mediate Store-Operated Calcium Entry in primary cortical neurons
  JOURNAL   Cell Calcium 101, 102525 (2022)
   PUBMED   34995919
  REMARK    GeneRIF: Na(+)/Ca(2+) exchanger isoform 1 (NCX1) and canonical
            transient receptor potential channel 6 (TRPC6) are recruited by
            STIM1 to mediate Store-Operated Calcium Entry in primary cortical
            neurons.
REFERENCE   6  (residues 1 to 958)
  AUTHORS   Furman,I., Cook,O., Kasir,J., Low,W. and Rahamimoff,H.
  TITLE     The putative amino-terminal signal peptide of the cloned rat brain
            Na(+)-Ca2+ exchanger gene (RBE-1) is not mandatory for functional
            expression
  JOURNAL   J Biol Chem 270 (32), 19120-19127 (1995)
   PUBMED   7642578
REFERENCE   7  (residues 1 to 958)
  AUTHORS   Lee,S.L., Yu,A.S. and Lytton,J.
  TITLE     Tissue-specific expression of Na(+)-Ca2+ exchanger isoforms
  JOURNAL   J Biol Chem 269 (21), 14849-14852 (1994)
   PUBMED   8195112
REFERENCE   8  (residues 1 to 958)
  AUTHORS   Kieval,R.S., Bloch,R.J., Lindenmayer,G.E., Ambesi,A. and
            Lederer,W.J.
  TITLE     Immunofluorescence localization of the Na-Ca exchanger in heart
            cells
  JOURNAL   Am J Physiol 263 (2 Pt 1), C545-C550 (1992)
   PUBMED   1514597
REFERENCE   9  (residues 1 to 958)
  AUTHORS   Komuro,I., Wenninger,K.E., Philipson,K.D. and Izumo,S.
  TITLE     Molecular cloning and characterization of the human cardiac
            Na+/Ca2+ exchanger cDNA
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4769-4773 (1992)
   PUBMED   1374913
REFERENCE   10 (residues 1 to 958)
  AUTHORS   Nicoll,D.A., Longoni,S. and Philipson,K.D.
  TITLE     Molecular cloning and functional expression of the cardiac
            sarcolemmal Na(+)-Ca2+ exchanger
  JOURNAL   Science 250 (4980), 562-565 (1990)
   PUBMED   1700476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.825537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..958
                     /product="sodium/calcium exchanger 1 isoform 4 precursor"
                     /note="sodium/calcium exchanger 1; Na-Ca exchanger;
                     Na(+)/Ca(2+)-exchange protein 1; solute carrier family 8
                     (sodium/calcium exchanger), member 1; solute carrier
                     family 8 member 1"
                     /calculated_mol_wt=103136
     Region          1..958
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3563
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            134..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          138..178
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          251..270
                     /region_name="Putative calmodulin-binding region.
                     /evidence=ECO:0000250|UniProtKB:P23685"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70414; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70414; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            786..806
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            810..830
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          827..863
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            860..880
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            892..912
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            930..950
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     CDS             1..958
                     /gene="Slc8a1"
                     /gene_synonym="Ncx; Ncx1"
                     /coded_by="NM_001270774.2:35..2911"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:29715"
                     /db_xref="RGD:3717"
ORIGIN      
        1 mlrlslppnv smgfrlvtlv allfthvdhi tadteaetgg nettectgsy yckkgvilpi
       61 wepqdpsfgd kiaratvyfv amvymflgvs iiadrfmssi evitsqekei tikkpngett
      121 kttvriwnet vsnltlmalg ssapeillsv ievcghnfta gdlgpstivg saafnmfiii
      181 alcvyvvpdg etrkikhlrv ffvtaawsif aytwlyiils vsspgvvevw eglltffffp
      241 icvvfawvad rrllfykyvy kryragkqrg miiehegdrp askteiemdg kvvnshvdnf
      301 ldgalvlevd erdqddeear remarilkel kqkhpdkeie qlielanyqv lsqqqksraf
      361 yriqatrlmt gagnilkrha adqarkavsm hevnmdvven dpvskvffeq gtyqclencg
      421 tvaltiirrg gdltntvfvd frtedgtana gsdyeftegt vifkpgetqk eirvgiiddd
      481 ifeedenflv hlsnvrvsse vsedgildsn hvsaiaclgs pntatitifd ddhagiftfe
      541 epvthvsesi gimevkvlrt sgargnviip yktiegtarg ggedfedtcg elefqndeiv
      601 ktisvkvidd eeyeknktff ieigeprlve msekkggftl tgqpvfrkvh ardhpipstv
      661 isiseeyddk qpltskeeee rriaemgrpi lgehtklevi ieesyefkst vdklikktnl
      721 alvvgtnswr eqfieaitvs agedddddec geeklpscfd yvmhfltvfw kvlfafvppt
      781 eywngwacfi vsilmigllt afigdlashf gctiglkdsv tavvfvalgt svpdtfaskv
      841 aatqdqyada signvtgsna vnvflgigva wsiaaiyhaa ngeqfkvspg tlafsvtlft
      901 ifafinvgvl lyrrrpeigg elggprtakl ltsslfvllw llyiffssle aychikgf
//
LOCUS       NP_001419888             524 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain containing 149 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419888 XP_006251096
VERSION     NP_001419888.1
DBSOURCE    REFSEQ: accession NM_001432959.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Aug 5, 2024 this sequence version replaced XP_006251096.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.34996.1,
                                           SRR26643297.43500.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q11"
     Protein         1..524
                     /product="coiled-coil domain containing 149 isoform 2"
                     /note="coiled-coil domain-containing protein 149"
                     /calculated_mol_wt=58875
     Region          21..333
                     /region_name="CC149"
                     /note="Coiled-coil domain-containing protein 149-A;
                     pfam09789"
                     /db_xref="CDD:462902"
     CDS             1..524
                     /gene="Ccdc149"
                     /coded_by="NM_001432959.1:146..1720"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:688939"
                     /db_xref="RGD:1582968"
ORIGIN      
        1 mdgdrtesdw qglvseylvc krkleskkea llilskeldt cqqerdqykl manqlrerhq
       61 slkkkyreli dgdpslppek rkqanlaqll resqdrnkhl geeikelrqr lgevqgdnkl
      121 lrmtiakqrl gdeeigvrhf aaheredlve qlerakeqie slehdlqasv delqdvkeer
      181 asyqdkvdrl nqelnhilgg henriidvda lcmenrylqe rlkqlheevs llksniakyk
      241 nalerrknsk tqgksnssal tgvlsakqvq dllsedhgcs lpatpqsiad lkslatalle
      301 tiheknmviq hqrqtnrilg nrvaelekkl rtlevsglws lpggkdtill sdqtlptiqk
      361 skspllkfve qpteskesar dgeiqtqerd esraaaealt vpedagrpav sspappsnan
      421 qhsdfhhppv pqplseevnt vggreitqlt dgqeatdlee vpreapteeq rcepqpspss
      481 lsqeecivtl qdhlpsmqpe vkatstggdr giseggdtrs tvqt
//
LOCUS       NP_001178900            1018 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein kinase 31 [Rattus norvegicus].
ACCESSION   NP_001178900 XP_575472
VERSION     NP_001178900.1
DBSOURCE    REFSEQ: accession NM_001191971.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Zhou,J., Stein,P., Leu,N.A., Chmatal,L., Xue,J., Ma,J., Huang,X.,
            Lampson,M.A., Schultz,R.M. and Wang,P.J.
  TITLE     Accelerated reproductive aging in females lacking a novel
            centromere protein SYCP2L
  JOURNAL   Hum Mol Genet 24 (22), 6505-6514 (2015)
   PUBMED   26362258
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Bao,J., Wang,L., Lei,J., Hu,Y., Liu,Y., Shen,H., Yan,W. and Xu,C.
  TITLE     STK31(TDRD8) is dynamically regulated throughout mouse
            spermatogenesis and interacts with MIWI protein
  JOURNAL   Histochem Cell Biol 137 (3), 377-389 (2012)
   PUBMED   22205278
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 17, 2010 this sequence version replaced XP_575472.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.22849.1,
                                           SRR26360181.660357.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..1018
                     /product="serine/threonine-protein kinase 31"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=115022
     Region          61..135
                     /region_name="Tudor_TDRD8"
                     /note="Tudor domain found in Tudor domain-containing
                     protein 8 (TDRD8) and similar proteins; cd20430"
                     /db_xref="CDD:410501"
     Site            order(89,96,113,116,118)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410501"
     Region          <297..>698
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          803..>922
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     CDS             1..1018
                     /gene="Stk31"
                     /gene_synonym="RGD1564384"
                     /coded_by="NM_001191971.1:23..3079"
                     /db_xref="GeneID:500120"
                     /db_xref="RGD:1564384"
ORIGIN      
        1 mwgqrlfagt avaesvsfpg lvqmdedthy nkvedvvgsh vedavtfwaq nvsrnkdimk
       61 igcslsevcp hansvfgnld pkkiygglfs edkcwyrckv lktisddkcl vryidygnte
      121 ilnrsdivei ppelqfssia kkyrlwglqi psgqevtqfd qgrtflgsli fekeikmrik
      181 atyqdgtvia qaeygtvdig eevakkgfae kcrltsgida seakkpdpnq lalrslknpi
      241 plwgrrsnqs tfsrpkghfn grltldvkye tnagnhvtfp keslaagdfn lgsnvslaki
      301 kqdqklieen eklktekevl lenykalelk veqtaqelqq ektatmdltk hlestlktcv
      361 gtrlknlaak vellkeirhi nisirfgndl sdamqvldeg sfttlaslse lekiwaeynv
      421 aqekiqtcpn enegniliae rnevqqklfv avdvfilevd elpldkrlkt lqdlatsles
      481 vygkakegtn seeilrkfyd wqctkreefa sirseteasl qhlvawfqns qkvfdlslde
      541 pltsedmign ideilektes cvckelelsl ieqgvvdkei ilstysqvlq rihseekfia
      601 tmlskykdsv efkkqiidcl nkspsvdyll sikktlkglk aqlrwklvek snleesddhd
      661 gteiekikqe itqlrssvfq eiyhereeye klnsltqkwf pelpllypei gllkymnsgg
      721 lltmslerdl ldtepmkels skrplvcsev ngqpvllkgy svdvdtegrv iqraasyhra
      781 cgyakeeesg llpliflfmc ksdpvaylmv pyypkanlsa vqasmpltse ealkvmkgva
      841 rglhtlhsan iihgslhqnn vfalnreqgi vgdfdftkse sqrasvnmmv gglsllspel
      901 kigkppsass dlyaygclll wlsvpnqefe tnedgipkvd qfhlddnvks llcsliyfrs
      961 smtaeqvlna ecfllpkgkt ipntekeiey tqhnkedesk iesldrykek arngeanp
//
LOCUS       NP_001103362             840 aa            linear   ROD 28-APR-2025
DEFINITION  fibroblast growth factor receptor 2 isoform b precursor [Rattus
            norvegicus].
ACCESSION   NP_001103362 XP_001077699 XP_001077810 XP_001079420 XP_001079450
            XP_001079458 XP_001079467 XP_001079477 XP_001079488 XP_001079498
            XP_001079510 XP_001079521 XP_001079530 XP_341941
VERSION     NP_001103362.1
DBSOURCE    REFSEQ: accession NM_001109892.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Tian,M., Yang,J., Yan,X., Cao,Y., Liu,Y., Lei,Y. and Lv,H.
  TITLE     Knockdown of lncRNA TUG1 alleviates diabetic retinal vascular
            dysfunction through regulating miR-524-5p/FGFR2
  JOURNAL   Bioengineered 13 (5), 12661-12672 (2022)
   PUBMED   35599572
  REMARK    GeneRIF: Knockdown of lncRNA TUG1 alleviates diabetic retinal
            vascular dysfunction through regulating miR-524-5p/FGFR2.
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Kilcoyne,S., Potter,K.R., Gordon,Z., Overton,S., Brockbank,S.,
            Jayamohan,J., Magdum,S., Smith,M., Johnson,D., Wall,S. and
            Wilkie,A.O.M.
  TITLE     Feeding, Communication, Hydrocephalus, and Intracranial
            Hypertension in Patients With Severe FGFR2-Associated Pfeiffer
            Syndrome
  JOURNAL   J Craniofac Surg 32 (1), 134-140 (2021)
   PUBMED   33074973
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Zhu,M., Chen,G., Yang,Y., Yang,J., Qin,B. and Gu,L.
  TITLE     miR-217-5p regulates myogenesis in skeletal muscle stem cells by
            targeting FGFR2
  JOURNAL   Mol Med Rep 22 (2), 850-858 (2020)
   PUBMED   32626929
  REMARK    GeneRIF: miR2175p regulates myogenesis in skeletal muscle stem
            cells by targeting FGFR2.
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Xu,Z., Zhu,X., Wang,M., Lu,Y. and Dai,C.
  TITLE     FGF/FGFR2 Protects against Tubular Cell Death and Acute Kidney
            Injury Involving Erk1/2 Signaling Activation
  JOURNAL   Kidney Dis (Basel) 6 (3), 181-194 (2020)
   PUBMED   32523960
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Chen,P., Xu,B., Feng,Y., Li,K.X., Liu,Z., Sun,X., Lu,X.L.,
            Wang,L.Q., Chen,Y.W., Fan,X.X., Yang,X.L., Wang,N., Qiao,G.F. and
            Li,B.Y.
  TITLE     FGF-21 ameliorates essential hypertension of SHR via baroreflex
            afferent function
  JOURNAL   Brain Res Bull 154, 9-20 (2020)
   PUBMED   31626954
REFERENCE   6  (residues 1 to 840)
  AUTHORS   Park,W.J., Theda,C., Maestri,N.E., Meyers,G.A., Fryburg,J.S.,
            Dufresne,C., Cohen,M.M. Jr. and Jabs,E.W.
  TITLE     Analysis of phenotypic features and FGFR2 mutations in Apert
            syndrome
  JOURNAL   Am J Hum Genet 57 (2), 321-328 (1995)
   PUBMED   7668257
REFERENCE   7  (residues 1 to 840)
  AUTHORS   Schell,U., Hehr,A., Feldman,G.J., Robin,N.H., Zackai,E.H., de
            Die-Smulders,C., Viskochil,D.H., Stewart,J.M., Wolff,G., Ohashi,H.
            et al.
  TITLE     Mutations in FGFR1 and FGFR2 cause familial and sporadic Pfeiffer
            syndrome
  JOURNAL   Hum Mol Genet 4 (3), 323-328 (1995)
   PUBMED   7795583
REFERENCE   8  (residues 1 to 840)
  AUTHORS   Jabs,E.W., Li,X., Scott,A.F., Meyers,G., Chen,W., Eccles,M.,
            Mao,J.I., Charnas,L.R., Jackson,C.E. and Jaye,M.
  TITLE     Jackson-Weiss and Crouzon syndromes are allelic with mutations in
            fibroblast growth factor receptor 2
  JOURNAL   Nat Genet 8 (3), 275-279 (1994)
   PUBMED   7874170
  REMARK    Erratum:[Nat Genet 1995 Apr;9(4):451]
REFERENCE   9  (residues 1 to 840)
  AUTHORS   Reardon,W., Winter,R.M., Rutland,P., Pulleyn,L.J., Jones,B.M. and
            Malcolm,S.
  TITLE     Mutations in the fibroblast growth factor receptor 2 gene cause
            Crouzon syndrome
  JOURNAL   Nat Genet 8 (1), 98-103 (1994)
   PUBMED   7987400
REFERENCE   10 (residues 1 to 840)
  AUTHORS   Savagner,P., Valles,A.M., Jouanneau,J., Yamada,K.M. and Thiery,J.P.
  TITLE     Alternative splicing in fibroblast growth factor receptor 2 is
            associated with induced epithelial-mesenchymal transition in rat
            bladder carcinoma cells
  JOURNAL   Mol Biol Cell 5 (8), 851-862 (1994)
   PUBMED   7803853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW531062.1, BF420170.1, L19105.1, L19104.1, CB777398.1, L19110.1,
            CB780941.1, CB716134.1, CO397781.1, CF109832.1, DV718561.1 and
            CB769194.1.
            
            On or before Oct 12, 2007 this sequence version replaced
            XP_001079521.1, XP_001079530.1, XP_001079420.1, XP_001079450.1,
            XP_001079488.1, XP_001079510.1, XP_001079477.1, XP_001079498.1,
            XP_001079458.1, XP_001079467.1, XP_341941.3, XP_001077699.1,
            XP_001077810.1.
            
            Transcript Variant: This variant (b) lacks an alternate internal
            exon and contains an alternate internal exon compared to variant a.
            The resulting isoform (b) has the same N- and C-termini but differs
            in an internal segment compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00155311, SAMD00155315
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..840
                     /product="fibroblast growth factor receptor 2 isoform b
                     precursor"
                     /EC_number="2.7.10.1"
                     /calculated_mol_wt=89792
     sig_peptide     1..40
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4245
     Region          50..143
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          77..81
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          88..92
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          123..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          136..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          173..267
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          173..176
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          184..189
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(185,187,189)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(186,193..195,197)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          193..201
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          207..212
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          215..217
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          226..229
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          233..238
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          247..254
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          257..267
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          275..379
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          275..278
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          282..286
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          294..301
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(299,304..306,335..336,340,344,365)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          305..312
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          327..332
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          344..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          475..787
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(506..507,509,514,534,536,553,583..586,590,645,
                     649..650,652,663,681..685,694,728)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(506..507,509,514,534,536,553,583..586,590,649..650,
                     652,663)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(645,649,681..685,694,728)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            662..687
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..840
                     /gene="Fgfr2"
                     /gene_synonym="KGFR"
                     /coded_by="NM_001109892.1:590..3112"
                     /note="isoform b precursor is encoded by transcript
                     variant b"
                     /db_xref="GeneID:25022"
                     /db_xref="RGD:2611"
ORIGIN      
        1 mglpstwryg tgpgigtvtm vswgrficlv lvtmatlsla rpsfslvedt tlepeepptk
       61 yqisqpeacv vapgeslelr cmlkdaavis wtkdgvhlgp nnrtvligey lqikgatprd
      121 sglyacaaar tvdsetlyfm vnvtdaissg ddeddtdsse dfvsenrsnq rapywtntek
      181 mekrlhavpa antvkfrcpa ggnptptmrw lkngkefkqe hriggykvrn qhwslimesv
      241 vpsdkgnytc lveneygsin htyhldvver sphrpilqag lpanastvvg gdvefvckvy
      301 sdaqphiqwi khvekngsky gpdglpylkv lkaagvnttd keievlyirn vtfedageyt
      361 clagnsigis fhsawltvlp apvrekeita spdyleiaiy cigvfliacm vvtvifcrmk
      421 tttkkpdfss qpavhkltkr iplrrqvtvs aessssmnsn tplvrittrl sstadtpmla
      481 gvseyelped pkwefprdkl tlgkplgegc fgqvvmaeav gidkdrpkea vtvavkmlkd
      541 datekdlsdl vsememmkmi gkhkniinll gactqdgply viveyaskgn lreylrarrp
      601 pgmeysydin rvpeeqmtfk dlvsctyqla rgmeylasqk cihrdlaarn vlvtennvmk
      661 iadfglardi nnidyykktt ngrlpvkwma pealfdrvyt hqsdvwsfgv lmweiftlgg
      721 spypgipvee lfkllkeghr mdkptnctne lymmmrdcwh avpsqrptfk qlvedldril
      781 tlttneeyld ltqpleqysp sypdtrsscs sgddsvfspd pmpydpclpq yphingsvkt
//
LOCUS       NP_001399832             182 aa            linear   ROD 28-APR-2025
DEFINITION  transmembrane protein 40 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001399832
VERSION     NP_001399832.1
DBSOURCE    REFSEQ: accession NM_001412903.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.2079199.1,
                                           SRR26643299.20700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680412, SAMN06680413
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..182
                     /product="transmembrane protein 40 isoform 1"
                     /calculated_mol_wt=20142
     Region          62..181
                     /region_name="TMEM40"
                     /note="Transmembrane protein 40 family; pfam15817"
                     /db_xref="CDD:464892"
     CDS             1..182
                     /gene="Tmem40"
                     /gene_synonym="RGD1306976"
                     /coded_by="NM_001412903.1:45..593"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:680858"
                     /db_xref="RGD:1587025"
ORIGIN      
        1 measgsssqs pnssavhret edlnhssded khsrgprkhr rkshrdsspg adhgelevlk
       61 delqlyggaa gemvlagesg lrrrgsgsae geveasqlnr lnikkddeff hfvllcfaig
      121 allvcyhyys dwfmslgvgl ltfasletig iyfglvyrih svlqgfipll qkfrlpgfrr
      181 tn
//
LOCUS       NP_001416370             964 aa            linear   ROD 28-APR-2025
DEFINITION  angiomotin-like protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416370 XP_038938161
VERSION     NP_001416370.1
DBSOURCE    REFSEQ: accession NM_001429441.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Zheng,Y., Vertuani,S., Nystrom,S., Audebert,S., Meijer,I.,
            Tegnebratt,T., Borg,J.P., Uhlen,P., Majumdar,A. and Holmgren,L.
  TITLE     Angiomotin-like protein 1 controls endothelial polarity and
            junction stability during sprouting angiogenesis
  JOURNAL   Circ Res 105 (3), 260-270 (2009)
   PUBMED   19590046
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
REFERENCE   3  (residues 1 to 964)
  AUTHORS   Sugihara-Mizuno,Y., Adachi,M., Kobayashi,Y., Hamazaki,Y.,
            Nishimura,M., Imai,T., Furuse,M. and Tsukita,S.
  TITLE     Molecular characterization of angiomotin/JEAP family proteins:
            interaction with MUPP1/Patj and their endogenous properties
  JOURNAL   Genes Cells 12 (4), 473-486 (2007)
   PUBMED   17397395
REFERENCE   4  (residues 1 to 964)
  AUTHORS   Patrie,K.M.
  TITLE     Identification and characterization of a novel tight
            junction-associated family of proteins that interacts with a WW
            domain of MAGI-1
  JOURNAL   Biochim Biophys Acta 1745 (1), 131-144 (2005)
   PUBMED   16019084
REFERENCE   5  (residues 1 to 964)
  AUTHORS   Nishimura,M., Kakizaki,M., Ono,Y., Morimoto,K., Takeuchi,M.,
            Inoue,Y., Imai,T. and Takai,Y.
  TITLE     JEAP, a novel component of tight junctions in exocrine cells
  JOURNAL   J Biol Chem 277 (7), 5583-5587 (2002)
   PUBMED   11733531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038938161.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.21207.1,
                                           SRR26643290.28318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..964
                     /product="angiomotin-like protein 1 isoform 2"
                     /note="angiomotin-like protein 1"
                     /calculated_mol_wt=107459
     Region          <444..>702
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          613..819
                     /region_name="Angiomotin_C"
                     /note="Angiomotin C terminal; pfam12240"
                     /db_xref="CDD:463503"
     CDS             1..964
                     /gene="Amotl1"
                     /coded_by="NM_001429441.1:220..3114"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315430"
                     /db_xref="RGD:1305268"
ORIGIN      
        1 mrraksrrgp cepvlrappp icyspgspaq iledhayfyp dlqlysgrhe aptltveang
       61 glrgksvedp lssfhspnfl rtpevemrgs edvasgrvlq rliqeqlryg tptenmnlla
      121 iqhqatgsag pahstnnfss tetltqedpq mvyqsarqep qgqehqgdnt vmekqvrstq
      181 pqqnneelpt yeeakaqsqf frgqqqqqqq qqqqqqqqgq gplghtyyma ggtsqksrte
      241 grptvnrans gqahkdealk elkqghvrsl serimqlsle rngtkqhlps sgngksfkag
      301 gepspaqpvc kaldprgppp eypfktkpmk spvsknqdhg lyysdqhpgv lhemvkpypa
      361 pqpartevav lryqpppeyg vtsrpcqlpf pstvqqhspm ssqtssisgp lhsvslplpl
      421 pmslaapqpp paspsqqlgp dafaiveraq qmveilteen rvlhqelqgc ydnadklhkf
      481 ekelqsisea yeslvksttk resldkamrn klegeirrlh dfnrdlrdrl etanrqlssr
      541 eyeghedkaa eshhmsqnke flkekeklem elaavrtase dhrrhieild qalsnaqarv
      601 ikleeelrek qayvekvekl qqaltqlqsa cekrgqmerr lrtwlereld alrtqqkhgn
      661 gqpvnlpeyn apalmelvre keerilalea dmtkweqkyl eestirhfam saaaaataer
      721 dttisnhsrn gsygesslea hiwpeeeevv qanrrcqdme ytiknlhaki iekdamikvl
      781 qqrsrkdagk tdssslrpar svpsiaaatg thsrqtslts gqlaedkkee ktwkgsigfl
      841 lgkehqgqas apllpatpas alspptstts assthaktgs kdsstqtdki telfwpsmas
      901 lpsrgrlsta psnspvlkhp aakgtvekqe nspghgksse hrgrvssllq kpefpdgeim
      961 evli
//
LOCUS       NP_001420798             375 aa            linear   ROD 28-APR-2025
DEFINITION  ATP-sensitive inward rectifier potassium channel 15 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001420798 XP_006248201
VERSION     NP_001420798.1
DBSOURCE    REFSEQ: accession NM_001433869.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Okamoto,K., Iwasaki,N., Doi,K., Noiri,E., Iwamoto,Y., Uchigata,Y.,
            Fujita,T. and Tokunaga,K.
  TITLE     Inhibition of glucose-stimulated insulin secretion by KCNJ15, a
            newly identified susceptibility gene for type 2 diabetes
  JOURNAL   Diabetes 61 (7), 1734-1741 (2012)
   PUBMED   22566534
  REMARK    GeneRIF: It was shown that downregulation of Kcnj15 leads to
            increased insulin secretion in vitro and in vivo. The mechanism for
            regulating insulin secretion inolved a calcium-sensiong receptor.
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Earley,S. and Resta,T.C.
  TITLE     Estradiol attenuates hypoxia-induced pulmonary endothelin-1 gene
            expression
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 283 (1), L86-L93 (2002)
   PUBMED   12060564
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Hill,C.E., Briggs,M.M., Liu,J. and Magtanong,L.
  TITLE     Cloning, expression, and localization of a rat hepatocyte inwardly
            rectifying potassium channel
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 282 (2), G233-G240 (2002)
   PUBMED   11804844
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Pearson,W.L., Dourado,M., Schreiber,M., Salkoff,L. and Nichols,C.G.
  TITLE     Expression of a functional Kir4 family inward rectifier K+ channel
            from a gene cloned from mouse liver
  JOURNAL   J Physiol 514 (Pt 3) (Pt 3), 639-653 (1999)
   PUBMED   9882736
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Oct 10, 2024 this sequence version replaced XP_006248201.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.1603892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071, SAMN16676784
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..375
                     /product="ATP-sensitive inward rectifier potassium channel
                     15 isoform 2"
                     /note="ATP-sensitive inward rectifier potassium channel
                     15; inward rectifier K(+) channel Kir4.2; potassium
                     channel, inwardly rectifying subfamily J member 15;
                     potassium voltage-gated channel subfamily J member 15"
                     /calculated_mol_wt=42475
     Region          30..171
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Region          178..349
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     CDS             1..375
                     /gene="Kcnj15"
                     /gene_synonym="Kir4.2"
                     /coded_by="NM_001433869.1:436..1563"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:170847"
                     /db_xref="RGD:621662"
ORIGIN      
        1 meaihigmss aplvkhsngv glkahrprvm sksghsnvri dkvdgiylly lqdlwttvid
       61 mkwrykltlf aatfvmtwfl fgvvyyaiaf ihgdlelges nsnhtpcimk vdsltgaflf
      121 slesqttigy gvrsiteecp haifllvaql vittlieifi tgtflakiar pkkraetikf
      181 shcaviskqn gklclviqva nmrkslliqc qlsgkllqth vtkegerill nqatvkfhvd
      241 sssespflil pmtfyhvlde tsplrdltpq nlkekefelv vllnatvest savcqsrtsy
      301 ipeeiywgfe fvpvvslskn gkyvadfsqf eqirkspdct fycadsekqk leeqyrqedq
      361 rerelrslll qqsnv
//
LOCUS       NP_001382635            1207 aa            linear   ROD 28-APR-2025
DEFINITION  PAN2-PAN3 deadenylation complex catalytic subunit Pan2 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001382635 XP_006240845
VERSION     NP_001382635.1
DBSOURCE    REFSEQ: accession NM_001395706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Wahle,E. and Winkler,G.S.
  TITLE     RNA decay machines: deadenylation by the Ccr4-not and Pan2-Pan3
            complexes
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 561-570 (2013)
   PUBMED   23337855
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Zheng,D., Ezzeddine,N., Chen,C.Y., Zhu,W., He,X. and Shyu,A.B.
  TITLE     Deadenylation is prerequisite for P-body formation and mRNA decay
            in mammalian cells
  JOURNAL   J Cell Biol 182 (1), 89-101 (2008)
   PUBMED   18625844
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Uchida,N., Hoshino,S. and Katada,T.
  TITLE     Identification of a human cytoplasmic poly(A) nuclease complex
            stimulated by poly(A)-binding protein
  JOURNAL   J Biol Chem 279 (2), 1383-1391 (2004)
   PUBMED   14583602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Jul 30, 2021 this sequence version replaced XP_006240845.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760400 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..1207
                     /product="PAN2-PAN3 deadenylation complex catalytic
                     subunit Pan2 isoform 2"
                     /EC_number="3.1.13.4"
                     /note="PAB-dependent poly(A)-specific ribonuclease subunit
                     2; ubiquitin specific peptidase 52; ubiquitin specific
                     protease 52; PAN2 polyA specific ribonuclease subunit
                     homolog; PAN deadenylation complex subunit 2; PAN2 poly(A)
                     specific ribonuclease subunit; PAB1P-dependent
                     poly(A)-specific ribonuclease; poly(A)-nuclease
                     deadenylation complex subunit 2; PAN2-PAN3 deadenylation
                     complex catalytic subunit Pan2; inactive ubiquitin
                     carboxyl-terminal hydrolase 52; PAB-dependent
                     poly(A)-specific ribonuclease subunit PAN2;
                     PAB1P-dependent poly(A)-nuclease; PAN deadenylation
                     complex catalytic subunit 2"
                     /calculated_mol_wt=135703
     Region          75..357
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(90,94,99,114..115,142,148..149,153..154,171,176,182,
                     195,210,215,221..222,234..235,251,264,270..271,283..284,
                     303,319,325,347,351,357)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          153..193
                     /region_name="WD 1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          195..231
                     /region_name="WD 2.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          244..280
                     /region_name="WD 3.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          328..367
                     /region_name="WD 4.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          368..484
                     /region_name="Linker.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03182"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          516..903
                     /region_name="UCH_1"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam13423"
                     /db_xref="CDD:463872"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q504Q3; propagated from
                     UniProtKB/Swiss-Prot (Q6IE70.1)"
     Region          980..1153
                     /region_name="PAN2_exo"
                     /note="DEDDh 3'-5' exonuclease domain of the eukaryotic
                     exoribonuclease PAN2; cd06143"
                     /db_xref="CDD:99846"
     Site            order(983..986,988,1044,1048,1087..1088,1090..1092,1139,
                     1144)
                     /site_type="active"
                     /db_xref="CDD:99846"
     Site            order(983..986,988,1044,1048,1087..1088,1090..1091,1139,
                     1144)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99846"
     Site            order(983,985,1092,1139,1144)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99846"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q504Q3; propagated from
                     UniProtKB/Swiss-Prot (Q6IE70.1)"
     CDS             1..1207
                     /gene="Pan2"
                     /gene_synonym="Usp52"
                     /coded_by="NM_001395706.1:256..3879"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:408200"
                     /db_xref="RGD:1303301"
ORIGIN      
        1 mnfegldpgl aefspamhst ldpvldahln psllqnveld pegvalealp vqesvhimeg
       61 vyselhsvva evgvpvsvsh fdlqeemlwv gshgghatsf fgpaleryss fqvngsddir
      121 qiqslengil fltknnlkym arggliifdy lldesedmhs llladnntll vgglqnhvle
      181 idlntvqetq kyavetpgvt imrqtnrfff cghtsgkvsl rdlrsfkveh efdafsgsls
      241 dfdvhgnlla acgfssrltg lacdrflkvy dlrmmraitp lqvhvdpafl rfiptytsrl
      301 aiisqsgqcq fceptglanp adifhvnpvg pllmtfdvsa skqalafgds egcvhlwtds
      361 pepsfnpysr etefalpclv dslpaldwsq dllplslipv plttdallsd wpaansapap
      421 rrappvdaei lrtmkkvgfi gyapnprtrl rnqipyrlke sdhefdnfsq vtesptgree
      481 eplhtvskky rkvtikyskl gledfdfkhy nktlfaglep hipnaycncm iqvlyflepv
      541 rcliqnhlcq kefclacelg flfhmldlsr gdpcqgsnfl rafrtipeas algliladsd
      601 easgkgslar liqrwnrfil tqlhqdmqel evpqayrgag gssfcssgds iigqlfscem
      661 encslcrcgs etvrasstll ftlsypegsi cdktgknydf aqvlkrsicl eqntqawcds
      721 cekyqptiqt rnirhlpdil vincevnssk eadfwrlqae vafkiavkkf ggevkskefa
      781 ladrkelrsp egflccssme elknvwlpfs irmkmtknkg ldvcnwadeh elsslgtpsq
      841 wgparaeeeh gvyvydlmat vvhildsrtg gslvahikvg etyhqrkegv thqqwylfnd
      901 fliepidkye avqfdmnwkv pailyyvkrn lnsrynlnik npieasvlla easlarkqrk
      961 thttfiplml nempqvgdlv gldaefvtln eeeaelrsdg tkstikpsqm svaritcvrg
     1021 qgpnegipfi ddyistqeqv vdyltqysgi kpgdldakis skhlttlkst ylklrflidi
     1081 gvkfvghglq kdfrvinlmv pkdqvldtvy lfhmprkrmi slrflawyfl dlkiqgethd
     1141 siedartalq lyrkylelsk ngaepesfhk vlkglyekgr kmdwkvpepe sqsspknaav
     1201 fpsvlal
//
LOCUS       NP_001101279             875 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 512B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001101279 XP_001057229 XP_230967
VERSION     NP_001101279.1
DBSOURCE    REFSEQ: accession NM_001107809.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Balestri,F., Barsotti,C., Lutzemberger,L., Camici,M. and Ipata,P.L.
  TITLE     Key role of uridine kinase and uridine phosphorylase in the
            homeostatic regulation of purine and pyrimidine salvage in brain
  JOURNAL   Neurochem Int 51 (8), 517-523 (2007)
   PUBMED   17643556
  REMARK    GeneRIF: At relatively high UTP and CTP levels the inhibition of
            uridine kinase channels uridine towards phosphorolysis. The
            ribose-1-phosphate is then transformed into PRPP, which is used for
            purine salvage synthesis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_230967.4, XP_001057229.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.14823.1,
                                           SRR26643429.15007.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..875
                     /product="zinc finger protein 512B isoform 2"
                     /note="uridine kinase-like 1"
                     /calculated_mol_wt=96024
     Region          <170..474
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          579..600
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          615..636
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..875
                     /gene="Zfp512b"
                     /gene_synonym="Urkl1; Znf512b"
                     /coded_by="NM_001107809.2:356..2983"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:311721"
                     /db_xref="RGD:1305284"
ORIGIN      
        1 mtesfcvggg rrlqgssksg pgkggsrkev qlpllqdppk lgmpvvhsgh tvpsqaplcf
       61 dpgnsasdkt egkkkgrpka enqalrdipl slmnqwkdef kahsrvkcpn sgcwlefpsi
      121 yglkyhyqrc qggaisdrla fpcpfceaaf tsktqlekhr iwnhmdhplp apkpgpvsrp
      181 vtinrpvgvs kpigvskpvt vgkpvgvskp igiskpvtvs rpipvtkpvt vsrpmqvsrp
      241 vpvtkpipit kpvpltkhmp vtklvtvskp vpltkpvpvs rpivvskpvp vsrpiaisrh
      301 tppckmvlls ksenktlrat gknsnkkraa dsldtcpilp kqarqengey gpstvdqsvt
      361 fqlstdpsns sllpgsrplm gkealrpigp vsqpeedper tkhrrkqktp kkftgeqpsi
      421 sgtfglkgla kaedkarvhr skkqegsgse evrkkvlatp vtvskeaptp vahpapggpe
      481 eqwqraiher geavcptcnv vtrktlvglk khmevchklq ealkcqhcrk qfkskaglny
      541 htmaehsakp tdaeasegge qeererlrkv lkqmgrlrcp qegcgaafss lmgyqyhqrr
      601 cgkppcevds psfpcthcgk tyrskaghdy hvrsehtapp peeptdkipe aedllgvert
      661 psgrirrtsa qvavfhlqei aedelardwt krrmkddlvp etarlnytrp glptlnpqll
      721 eawknevkek ghvncpndcc eaiyssvsgl kahfascskg dhlvgkyrcl lcpkefsses
      781 gvkyhilkth genwfrtsad ppskhksqds lmprkekkks lsggkkrgrk pkersseepa
      841 sklppnrddw ppggrdrgar sstgkkagag kapek
//
LOCUS       NP_001419343             934 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear receptor coactivator 7 isoform b [Rattus norvegicus].
ACCESSION   NP_001419343 XP_063132627
VERSION     NP_001419343.1
DBSOURCE    REFSEQ: accession NM_001432414.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Finelli,M.J., Sanchez-Pulido,L., Liu,K.X., Davies,K.E. and
            Oliver,P.L.
  TITLE     The Evolutionarily Conserved Tre2/Bub2/Cdc16 (TBC), Lysin Motif
            (LysM), Domain Catalytic (TLDc) Domain Is Neuroprotective against
            Oxidative Stress
  JOURNAL   J Biol Chem 291 (6), 2751-2763 (2016)
   PUBMED   26668325
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Shao,W., Halachmi,S. and Brown,M.
  TITLE     ERAP140, a conserved tissue-specific nuclear receptor coactivator
  JOURNAL   Mol Cell Biol 22 (10), 3358-3372 (2002)
   PUBMED   11971969
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_063132627.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.393.1, SRR26643287.202.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..934
                     /product="nuclear receptor coactivator 7 isoform b"
                     /calculated_mol_wt=104965
     Region          <101..159
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          772..934
                     /region_name="TLDc"
                     /note="domain in TBC and LysM domain containing proteins;
                     smart00584"
                     /db_xref="CDD:214733"
     CDS             1..934
                     /gene="Ncoa7"
                     /gene_synonym="RGD1566426"
                     /coded_by="NM_001432414.1:603..3407"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:498995"
                     /db_xref="RGD:1566426"
ORIGIN      
        1 mdtkeekkep kerkqsyfar lkkkkqakqn aeivsaarsh sgkddshsvi leqdksniaa
       61 egdqstdekk krknnqlkei rrmelkryyn addnqskshd kkekkmvvqk pqgtleytag
      121 sqdtlnsval kfnvtpnrlv elnklfthti vpgqvlfvpd anipsstlrl ssstpgatvs
      181 psssdaeydk lpdadlarka lkpiervlss tseedepgvv kflkmncryf tdgkgvvggv
      241 mivtpnnimf dphksdplvi engceeygli cpmeevvsia lyndishmki kdalpspgew
      301 edlasekdin pfskfksink ekrqqngert laldvksvgs peestermrt rteppddses
      361 wklknleysr gtasefpsvt qlskgpssvc aaleptaken rllgdedfvd leelssqpgs
      421 gmdkgdarke clpydqkkda pqtimsakkg eeqsapdvtg tesdaelkga ldsetgekqd
      481 eapevdkqsg spenwrestl sihedldkvk liefylnknk egsqlsenvl kselserksi
      541 epdgiditls sslpqagdsp peshkepgtl cvkgggtppp klhpsaeetv tnnkealdsl
      601 essldklcqg aqmdnrseiq lwllkriqvp iedilpskee ksktppmflc ikvgkpmrks
      661 fashsttmvq qygkrrkqpe ywfavprerv dhlytffvqw spdvygkdak eqgfvvveke
      721 eltmidnffs epttksweii tveeakrrks tcsyyeeeee eeeglpilqs hsallenmhi
      781 eqlarrlpar vqgypwrlay stlehgtslk tlyrksasld spvllvikdm dnqifgayat
      841 hpfrfsdhyy gtgetflytf spnfkvfkws gensyfingd isslelgggg grfglwldad
      901 lyhgrsnscs tfnndilskk edfivqdlev wtfe
//
LOCUS       NP_001419375            1291 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology domain-containing family A member 7 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001419375 XP_063135562
VERSION     NP_001419375.1
DBSOURCE    REFSEQ: accession NM_001432446.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1291)
  AUTHORS   Shah,J., Rouaud,F., Guerrera,D., Vasileva,E., Popov,L.M.,
            Kelley,W.L., Rubinstein,E., Carette,J.E., Amieva,M.R. and Citi,S.
  TITLE     A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
            Promote alpha-Toxin Cytotoxicity
  JOURNAL   Cell Rep 25 (8), 2132-2147 (2018)
   PUBMED   30463011
REFERENCE   2  (residues 1 to 1291)
  AUTHORS   Endres,B.T., Priestley,J.R., Palygin,O., Flister,M.J.,
            Hoffman,M.J., Weinberg,B.D., Grzybowski,M., Lombard,J.H.,
            Staruschenko,A., Moreno,C., Jacob,H.J. and Geurts,A.M.
  TITLE     Mutation of Plekha7 attenuates salt-sensitive hypertension in the
            rat
  JOURNAL   Proc Natl Acad Sci U S A 111 (35), 12817-12822 (2014)
   PUBMED   25136115
REFERENCE   3  (residues 1 to 1291)
  AUTHORS   Kurita,S., Yamada,T., Rikitsu,E., Ikeda,W. and Takai,Y.
  TITLE     Binding between the junctional proteins afadin and PLEKHA7 and
            implication in the formation of adherens junction in epithelial
            cells
  JOURNAL   J Biol Chem 288 (41), 29356-29368 (2013)
   PUBMED   23990464
REFERENCE   4  (residues 1 to 1291)
  AUTHORS   Pulimeno,P., Paschoud,S. and Citi,S.
  TITLE     A role for ZO-1 and PLEKHA7 in recruiting paracingulin to tight and
            adherens junctions of epithelial cells
  JOURNAL   J Biol Chem 286 (19), 16743-16750 (2011)
   PUBMED   21454477
  REMARK    GeneRIF: ZO-1 and PLEKHA7 are paracingulin-interacting proteins
            that are involved in its recruitment to epithelial tight and
            adherens junctions, respectively
REFERENCE   5  (residues 1 to 1291)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 1291)
  AUTHORS   Meng,W., Mushika,Y., Ichii,T. and Takeichi,M.
  TITLE     Anchorage of microtubule minus ends to adherens junctions regulates
            epithelial cell-cell contacts
  JOURNAL   Cell 135 (5), 948-959 (2008)
   PUBMED   19041755
REFERENCE   7  (residues 1 to 1291)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_063135562.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1536005.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1291
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..1291
                     /product="pleckstrin homology domain-containing family A
                     member 7 isoform 1"
                     /note="pleckstrin homology domain containing, family A
                     member 7"
                     /calculated_mol_wt=146648
     Region          55..84
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          158..280
                     /region_name="PH_PEPP1_2_3"
                     /note="Phosphoinositol 3-phosphate binding proteins 1, 2,
                     and 3 pleckstrin homology (PH) domain; cd13248"
                     /db_xref="CDD:270068"
     Site            order(172,174..175,182,184,195,257)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270068"
     Region          734..>834
                     /region_name="CCDC90-like"
                     /note="Coiled-coil domain-containing protein 90-like;
                     pfam07798"
                     /db_xref="CDD:462268"
     Region          <861..967
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1291
                     /gene="Plekha7"
                     /gene_synonym="RGD1304650"
                     /coded_by="NM_001432446.1:16..3891"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:499249"
                     /db_xref="RGD:1598216"
ORIGIN      
        1 maaavgrdtl pehwsygvcr dgrvffindq lrcttwlhpr tgepvnsghm irsdlprgwe
       61 egfteegasf fidhnqqttt frhpvtgqfs senseyvlre ephphmskqe rnqrpssmvs
      121 etstagttst leakpgpkii kssskvhsfg krdqairrnl nvpvvvrgwl hkqdssgmrl
      181 wkrrwfvlad yclfyykdsr eeavlgsipl psyvispvap edrisrkysf kavhtgmral
      241 iystttagsq aehsgmrtyy fsadtledmn awvramnqaa qvlsrsslkr dkverqampq
      301 anhtdacqec ghvgpghsrd cprrgyedai vfdrreqeee rfrsqrdtle grrdrskars
      361 pylpaeedal fvdlpggprg qqaqpqraer nglppyglge qngtsgysrt appranlekh
      421 sqrktnlaqt ehwakaqkgd grslpldqtl prqgpsqpps flenyqtlpr ntrypsgsss
      481 ppprnlpsdy kyaqdrashl kmsseerrah rdgtvwqlye wqqrqqfrhg sptapigags
      541 pefteqgrsr sllevprsis vppspsdipp pgpprpfppr rphtpaervt vkppdqrrsv
      601 dislggsprk arghavknss hvdrrsmpsm gymthtvsap slhgksaddt ylqlkkdley
      661 ldlkiknnep linvlykvlk ksargcrpgr smtgrdllkd rslkpmkiae sdtdvklsif
      721 ceqdrilqdl edkiralken kdqlesvlev lhrqteqyrd qpqhlekitc qqrllqedlv
      781 hiraelcres temenawney lklekdveql kqtlqeqhrr afffqeksqi qkdlwriedv
      841 maglsvnken yrvlvgsvkn perktvplfp hpsvpslspt eskpalqpsp ptspvrtple
      901 vrlfpqlqty vpyrphppql rkvvsplqsp tkatpqaede apprpplpel yspedqppav
      961 pplpreatii rhtsvrglkr qsderkrdre qgqcvngdlk velrsyvsep elasfsgdvp
     1021 rpslglvgse sryqtlpgrg lsgstsrlqq sstiapyvtl rrglnaenss vtfsrpksal
     1081 erlysgdhqr gkmsaeeqle rmkrhqkalv rerkrtlsqg ertgllsary lsqplpgdlg
     1141 swkreqefdl qlleraaqgd rkdkeegwlk vqatpvmeld lepqdydldi nrelskpekv
     1201 siperyvevd peeppsveel qaryqkaeki rnilarssmc nlqppgqdrn sladldtqmq
     1261 eqeriinisy alaseasqrs kqvaaqavtd p
//
LOCUS       NP_001100426             413 aa            linear   ROD 28-APR-2025
DEFINITION  histone-lysine N-methyltransferase SUV39H1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001100426 XP_001063363 XP_217594
VERSION     NP_001100426.1
DBSOURCE    REFSEQ: accession NM_001106956.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Yang,G., Weng,X., Zhao,Y., Zhang,X., Hu,Y., Dai,X., Liang,P.,
            Wang,P., Ma,L., Sun,X., Hou,L., Xu,H., Fang,M., Li,Y., Jenuwein,T.,
            Xu,Y. and Sun,A.
  TITLE     The histone H3K9 methyltransferase SUV39H links SIRT1 repression to
            myocardial infarction
  JOURNAL   Nat Commun 8, 14941 (2017)
   PUBMED   28361889
  REMARK    GeneRIF: SUV39H augments intracellular reactive oxygen species
            levels in a SIRT1-dependent manner.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,J., Liang,L., Miao,X., Wu,S., Cao,J., Tao,B., Mao,Q., Mo,K.,
            Xiong,M., Lutz,B.M., Bekker,A. and Tao,Y.X.
  TITLE     Contribution of the Suppressor of Variegation 3-9 Homolog 1 in
            Dorsal Root Ganglia and Spinal Cord Dorsal Horn to Nerve
            Injury-induced Nociceptive Hypersensitivity
  JOURNAL   Anesthesiology 125 (4), 765-778 (2016)
   PUBMED   27483126
  REMARK    GeneRIF: SUV39H1 plays a critical role in chromosome dynamics and
            development, neurite outgrowth, and ethanol-induced neuroadaptation
            through gene-specific silencing.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yang,B., Yang,J., Bai,J., Pu,P., Liu,J., Wang,F. and Ruan,B.
  TITLE     Suv39h1 protects from myocardial ischemia-reperfusion injury in
            diabetic rats
  JOURNAL   Cell Physiol Biochem 33 (4), 1176-1185 (2014)
   PUBMED   24752040
  REMARK    GeneRIF: Overexpression of Suv39h1 results in the de-activation of
            proinflammatory pathways and reduced apoptosis and myocardial
            injury.
REFERENCE   4  (residues 1 to 413)
  AUTHORS   He,Y., Korboukh,I., Jin,J. and Huang,J.
  TITLE     Targeting protein lysine methylation and demethylation in cancers
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 44 (1), 70-79 (2012)
   PUBMED   22194015
  REMARK    Review article
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Bosch-Presegue,L., Raurell-Vila,H., Marazuela-Duque,A.,
            Kane-Goldsmith,N., Valle,A., Oliver,J., Serrano,L. and Vaquero,A.
  TITLE     Stabilization of Suv39H1 by SirT1 is part of oxidative stress
            response and ensures genome protection
  JOURNAL   Mol Cell 42 (2), 210-223 (2011)
   PUBMED   21504832
  REMARK    GeneRIF: SirT1 preserves heterochromatin structure: it modulates
            Suv39h1 protein levels in stress conditions by preventing
            MDM2-mediated polyubiquitination at K87.
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Davison,J.M., Mellott,T.J., Kovacheva,V.P. and Blusztajn,J.K.
  TITLE     Gestational choline supply regulates methylation of histone H3,
            expression of histone methyltransferases G9a (Kmt1c) and Suv39h1
            (Kmt1a), and DNA methylation of their genes in rat fetal liver and
            brain
  JOURNAL   J Biol Chem 284 (4), 1982-1989 (2009)
   PUBMED   19001366
  REMARK    GeneRIF: mRNA and protein expression of histone methyltransferases
            G9a and Suv39h1 were directly related to the availability of
            choline
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Renthal,W., Carle,T.L., Maze,I., Covington,H.E. 3rd, Truong,H.T.,
            Alibhai,I., Kumar,A., Montgomery,R.L., Olson,E.N. and Nestler,E.J.
  TITLE     Delta FosB mediates epigenetic desensitization of the c-fos gene
            after chronic amphetamine exposure
  JOURNAL   J Neurosci 28 (29), 7344-7349 (2008)
   PUBMED   18632938
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Pogribny,I.P., Ross,S.A., Tryndyak,V.P., Pogribna,M., Poirier,L.A.
            and Karpinets,T.V.
  TITLE     Histone H3 lysine 9 and H4 lysine 20 trimethylation and the
            expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in
            hepatocarcinogenesis induced by methyl deficiency in rats
  JOURNAL   Carcinogenesis 27 (6), 1180-1186 (2006)
   PUBMED   16497704
  REMARK    GeneRIF: Suv4-20h2 and Suv-39h1 histone methyltransferases are
            expressed and Histone H3 lysine 9 and H4 lysine 20 are
            trimethylated in hepatocarcinogenesis induced by methyl deficiency
            in rats [Suv4-20h2 and Suv-39h1]
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Liu,D.X., Nath,N., Chellappan,S.P. and Greene,L.A.
  TITLE     Regulation of neuron survival and death by p130 and associated
            chromatin modifiers
  JOURNAL   Genes Dev 19 (6), 719-732 (2005)
   PUBMED   15769944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_217594.3, XP_001063363.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.60585.1,
                                           SRR26643292.64989.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..413
                     /product="histone-lysine N-methyltransferase SUV39H1
                     isoform 1"
                     /EC_number="2.1.1.354"
                     /note="histone-lysine N-methyltransferase SUV39H1;
                     suppressor of variegation 3-9 homolog 1-like 1"
                     /calculated_mol_wt=47636
     Region          44..92
                     /region_name="CD_SUV39H1_like"
                     /note="chromodomain of histone methyltransferase SUV39H1,
                     and similar proteins; cd18639"
                     /db_xref="CDD:349289"
     Site            order(44..48,63,65..68,72,74..77,79..80,86,89..90)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349289"
     Region          159..413
                     /region_name="SET_SUV39H1"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in suppressor of variegation 3-9 homolog 1 (SUV39H1)
                     and similar proteins; cd10525"
                     /db_xref="CDD:380923"
     Site            order(255..257,297..298,321..325,366,400..403,412)
                     /site_type="other"
                     /note="putative SAM binding site"
                     /db_xref="CDD:380923"
     Site            order(255..257,274,281,284..285,287,296..301,304,310,
                     321..325,333,335,348,364,366,399..403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380923"
     Site            order(299..301,310,333,348,366)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380923"
     Site            order(327,401,403,408)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380923"
     CDS             1..413
                     /gene="Suv39h1"
                     /gene_synonym="RGD1565028; Suv39h1l1"
                     /coded_by="NM_001106956.2:472..1713"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:302553"
                     /db_xref="RGD:1565028"
ORIGIN      
        1 mgepatlgcs vccksswnql qdlcrlakls cpalgvskkn lydfeveylc dykkireqey
       61 ylvkwrgypd sentweprqn lkcvrilkqf hkdlerelvr rhrrskpprh ldpnlanylv
      121 qkakqrralq rweqelnakr shlgritven evdldgpprs fvyineyrvg egitlnqvav
      181 gcecqdclla ptggccpgas lhkfayndqg qvrlkagqpi yecnsrcccg ydcpnrvvqk
      241 girynlcifr tddgrgwgvr tlekirknsf vmeyvgeiit seeaerrgqi ydrqgatylf
      301 dldyvedvyt vdaayygnis hfvnhscdpn lqvynvfidn lderlpriaf fatrtiwage
      361 eltfdynmqv dpvdmestrm dsnfglaglp gspkkrvrie ckcgttacrk ylf
//
LOCUS       NP_001419341             945 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear receptor coactivator 7 isoform a [Rattus norvegicus].
ACCESSION   NP_001419341 XP_006227820
VERSION     NP_001419341.1
DBSOURCE    REFSEQ: accession NM_001432412.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Finelli,M.J., Sanchez-Pulido,L., Liu,K.X., Davies,K.E. and
            Oliver,P.L.
  TITLE     The Evolutionarily Conserved Tre2/Bub2/Cdc16 (TBC), Lysin Motif
            (LysM), Domain Catalytic (TLDc) Domain Is Neuroprotective against
            Oxidative Stress
  JOURNAL   J Biol Chem 291 (6), 2751-2763 (2016)
   PUBMED   26668325
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Shao,W., Halachmi,S. and Brown,M.
  TITLE     ERAP140, a conserved tissue-specific nuclear receptor coactivator
  JOURNAL   Mol Cell Biol 22 (10), 3358-3372 (2002)
   PUBMED   11971969
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_006227820.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.201.1, SRR26643284.109.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..945
                     /product="nuclear receptor coactivator 7 isoform a"
                     /calculated_mol_wt=106294
     Region          <101..159
                     /region_name="LysM"
                     /note="LysM repeat [Cell wall/membrane/envelope
                     biogenesis]; COG1388"
                     /db_xref="CDD:440998"
     Region          783..945
                     /region_name="TLDc"
                     /note="domain in TBC and LysM domain containing proteins;
                     smart00584"
                     /db_xref="CDD:214733"
     CDS             1..945
                     /gene="Ncoa7"
                     /gene_synonym="RGD1566426"
                     /coded_by="NM_001432412.1:603..3440"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:498995"
                     /db_xref="RGD:1566426"
ORIGIN      
        1 mdtkeekkep kerkqsyfar lkkkkqakqn aeivsaarsh sgkddshsvi leqdksniaa
       61 egdqstdekk krknnqlkei rrmelkryyn addnqskshd kkekkmvvqk pqgtleytag
      121 sqdtlnsval kfnvtpnrlv elnklfthti vpgqvlfvpd anipsstlrl ssstpgatvs
      181 psssdaeydk lpdadlarka lkpiervlss tseedepgvv kflkmncryf tdgkgvvggv
      241 mivtpnnimf dphksdplvi engceeygli cpmeevvsia lyndishmki kdalpsdlpr
      301 dvcplyrpge wedlasekdi npfskfksin kekrqqnger tlaldvksvg speestermr
      361 trteppddse swklknleys rgtasefpsv tqlskgpssv caaleptake nrllgdedfv
      421 dleelssqpg sgmdkgdark eclpydqkkd apqtimsakk geeqsapdvt gtesdaelkg
      481 aldsetgekq deapevdkqs gspenwrest lsihedldkv kliefylnkn kegsqlsenv
      541 lkselserks iepdgiditl ssslpqagds ppeshkepgt lcvkgggtpp pklhpsaeet
      601 vtnnkealds lessldklcq gaqmdnrsei qlwllkriqv piedilpske eksktppmfl
      661 cikvgkpmrk sfashsttmv qqygkrrkqp eywfavprer vdhlytffvq wspdvygkda
      721 keqgfvvvek eeltmidnff septtkswei itveeakrrk stcsyyeeee eeeeglpilq
      781 shsallenmh ieqlarrlpa rvqgypwrla ystlehgtsl ktlyrksasl dspvllvikd
      841 mdnqifgaya thpfrfsdhy ygtgetflyt fspnfkvfkw sgensyfing disslelggg
      901 ggrfglwlda dlyhgrsnsc stfnndilsk kedfivqdle vwtfe
//
LOCUS       NP_001416086             301 aa            linear   ROD 28-APR-2025
DEFINITION  receptor expression-enhancing protein 1 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001416086 XP_038963742
VERSION     NP_001416086.1
DBSOURCE    REFSEQ: accession NM_001429157.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Hashimoto,Y., Shirane,M., Matsuzaki,F., Saita,S., Ohnishi,T. and
            Nakayama,K.I.
  TITLE     Protrudin regulates endoplasmic reticulum morphology and function
            associated with the pathogenesis of hereditary spastic paraplegia
  JOURNAL   J Biol Chem 289 (19), 12946-12961 (2014)
   PUBMED   24668814
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Bjork,S., Hurt,C.M., Ho,V.K. and Angelotti,T.
  TITLE     REEPs are membrane shaping adapter proteins that modulate specific
            g protein-coupled receptor trafficking by affecting ER cargo
            capacity
  JOURNAL   PLoS One 8 (10), e76366 (2013)
   PUBMED   24098485
  REMARK    Erratum:[PLoS One. 2013;8(12).
            doi:10.1371/annotation/6f86410c-63c3-4fcd-b1cb-9fd8d2ea95d0]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Park,S.H., Zhu,P.P., Parker,R.L. and Blackstone,C.
  TITLE     Hereditary spastic paraplegia proteins REEP1, spastin, and
            atlastin-1 coordinate microtubule interactions with the tubular ER
            network
  JOURNAL   J Clin Invest 120 (4), 1097-1110 (2010)
   PUBMED   20200447
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Saito,H., Kubota,M., Roberts,R.W., Chi,Q. and Matsunami,H.
  TITLE     RTP family members induce functional expression of mammalian
            odorant receptors
  JOURNAL   Cell 119 (5), 679-691 (2004)
   PUBMED   15550249
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Apr 10, 2024 this sequence version replaced XP_038963742.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.13388.1,
                                           SRR26643289.13215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q32"
     Protein         1..301
                     /product="receptor expression-enhancing protein 1 isoform
                     3"
                     /note="receptor expression-enhancing protein 1"
                     /calculated_mol_wt=33648
     Region          19..94
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     CDS             1..301
                     /gene="Reep1"
                     /gene_synonym="RGD1305230"
                     /coded_by="NM_001429157.1:102..1007"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362384"
                     /db_xref="RGD:1305230"
ORIGIN      
        1 mvswiisrlv vlifgtlypa yysykavksk dikeyvkwmm ywiifalftt aetftdiflc
       61 wfpfyyelki afvawllspy tkgssllyrk fvhptlsske keiddclvqa kdrsydalvh
      121 fgkrglnvaa taavmaaskv arifhfvssl dlregqgqga lserlrsfsm qdlttirgdg
      181 apapsgpppp gsgrssgkhg qpkmsrsase sagssvctcc stcrtrkvve gdvseggvks
      241 wephqvqnpl afsdeeeedl lefiykykap rrtefpleap prtlrsrfrk kstsssatet
      301 t
//
LOCUS       NP_001388489            1561 aa            linear   ROD 28-APR-2025
DEFINITION  LIM and calponin homology domains-containing protein 1 isoform a
            [Rattus norvegicus].
ACCESSION   NP_001388489 XP_038947830
VERSION     NP_001388489.1
DBSOURCE    REFSEQ: accession NM_001401560.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1561)
  AUTHORS   Lin,Y.H., Zhen,Y.Y., Chien,K.Y., Lee,I.C., Lin,W.C., Chen,M.Y. and
            Pai,L.M.
  TITLE     LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell
            migration
  JOURNAL   Mol Biol Cell 28 (8), 1054-1065 (2017)
   PUBMED   28228547
REFERENCE   2  (residues 1 to 1561)
  AUTHORS   Mella,C., Martinez,F., de Los Angeles Garcia,M., Nualart,F.,
            Castro,V., Bustos,P., Carvajal,N. and Uribe,E.
  TITLE     Expression and localization of an agmatinase-like protein in the
            rat brain
  JOURNAL   Histochem Cell Biol 134 (2), 137-144 (2010)
   PUBMED   20607275
  REMARK    GeneRIF: An agmatinase-like protein was detected in the
            hypothalamus in glial cells and arcuate nucleus neurons, and in
            hippocampus astrocytes and neurons, but not in brain cortex
REFERENCE   3  (residues 1 to 1561)
  AUTHORS   Uribe,E., Salas,M., Enriquez,S., Orellana,M.S. and Carvajal,N.
  TITLE     Cloning and functional expression of a rodent brain cDNA encoding a
            novel protein with agmatinase activity, but not belonging to the
            arginase family
  JOURNAL   Arch Biochem Biophys 461 (1), 146-150 (2007)
   PUBMED   17291445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 16, 2022 this sequence version replaced XP_038947830.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1561
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..1561
                     /product="LIM and calponin homology domains-containing
                     protein 1 isoform a"
                     /note="LIM and calponin homology domains-containing
                     protein 1"
                     /calculated_mol_wt=174595
     Region          23..140
                     /region_name="CH_LIMCH1"
                     /note="calponin homology (CH) domain found in LIM and
                     calponin homology domains-containing protein 1; cd21278"
                     /db_xref="CDD:409127"
     Site            order(23,27,77,79..80,83..84,86,96..104,122,124..125,
                     127..128,131..132,135)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409127"
     Region          250..>311
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          <276..>412
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          <736..868
                     /region_name="DUF4757"
                     /note="Domain of unknown function (DUF4757); pfam15949"
                     /db_xref="CDD:464950"
     Region          <1245..1282
                     /region_name="GBP_C"
                     /note="Guanylate-binding protein, C-terminal domain;
                     cd16269"
                     /db_xref="CDD:293879"
     Region          1491..1548
                     /region_name="LIM"
                     /note="Zinc-binding domain present in Lin-11, Isl-1,
                     Mec-3; smart00132"
                     /db_xref="CDD:214528"
     Site            order(1491,1494,1514,1517,1520,1523,1545,1548)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..1561
                     /gene="Limch1"
                     /gene_synonym="RGD1305269"
                     /coded_by="NM_001401560.1:22..4707"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:305332"
                     /db_xref="RGD:1305269"
ORIGIN      
        1 macpalglev lqplqpeppp epafaeaqkw ieqvtgrsfg dkdfrtglen gillcellna
       61 ikpglvkkin rlptpiagld ntilflrgck elglkesqlf dpsdlqdtsn rvtvknfdys
      121 rklknvlvti ywlgkaansc tsysgttlnl kefegllaqm rketddiesp krsirdsgyi
      181 dcwdsersds lspprhgrdd sfdsldsfgs rsrqtpspdv vlrgssdgrg sdsesdlphr
      241 klpdvkkddm sarrtshgep ksavpfnqyl pnksnqtayv paplrkkkae reeyrkswst
      301 atsplggerp fsypetieee gseagspted dpssqmdpdg kpecgleapp sngkaqsped
      361 aaavpaaipe dreaverqkr rrleqagikv mpaaqrfasq kqsseekeai rdiilrkenp
      421 flahqhgkds esedeaacll pdlekddfaa rrarmnqrkp mvplnqllyg pyrkndeaka
      481 gssqhlskgp sdkknlgykr dqghredvnr vvacvmqtqe seplemsfrk apdlqkddla
      541 qrriqgrlsq hreapsfikl sgiteadlet werlkvsget rdgdaqntca pepspeidae
      601 tairddfasr karaykkapg prqkfvhfgp vteidqqtwq rlsigkagpr dnvevlshss
      661 esrtssrspp stttfdlkee qmlspqsdyr tvpsgtdgrl kkapwlapvl esqeeqvcvq
      721 snnpkteevt ptclpqekee vikkepemlp rvqrpegssg plygprtpvs ddaestsmfd
      781 mrceeeaavl phsrarqeql qlinnqlree ddkwqddlar wksrrrsasq dlikkeeerk
      841 kmeklmsged gtserrksik tyreivqeke rrerelheay knarsqeeae gilqqyierf
      901 tiseavlerl empkilersh stepnvssfp ndpspmkylr qqslpppkft atvettiart
      961 svpessvaag tgspsktstp ntvpmltprp ysqpknsqev lktfkvdgkv smngetargd
     1021 vegkekedpt avapgpsltk sqmfegvatv hgspvqvkqg snsieinikk pnsppqelta
     1081 aseetesngr ddengeessg ardveldsae pqhftttvtr csptvalvef ssspqlrnev
     1141 peeqdqkkpe nemsgkvelv lsqkvakpks pepeatltfp fldkmpetdq lhlpnlnsqe
     1201 lpgsaplrvq nswrrsqffs qsadspssek spastpfkfw awdpeeerrr qekwqqeqer
     1261 llqeryqkeq dklkeeweka qkeveeeerr yyeeerkiie dtvvpftiss ssadqlstss
     1321 svtegsgtrn kmdlencqdr dkerrqntpl qendsdsslk aresglpeeh ssltqspsan
     1381 sensvskgis qdqqpeteae ashcgtnpqs aqdppwnqqi snpptsksed vkpktlalek
     1441 sinhqiespg errkkspren fragplspcs ptppgqspnr ykrsisgkkl csscglalgk
     1501 gaamiietln lyfhiqcfrc gickgqlgda vsgtdvrirn gllnctdcym rsrsagqptt
     1561 l
//
LOCUS       NP_001419586             488 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC691551 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419586 XP_063137071
VERSION     NP_001419586.1
DBSOURCE    REFSEQ: accession NM_001432657.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 1, 2024 this sequence version replaced XP_063137071.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.24743.1,
                                           SRR26360181.1967579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..488
                     /product="uncharacterized protein LOC691551 isoform 2"
                     /note="transmembrane protein 180"
                     /calculated_mol_wt=55577
     Region          71..455
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(79..80,83..84,87,120,183..184,186..188,191,212,
                     215..216,219,309,312..313,316..318,321,349,353,405..406,
                     410,414,438,441..442,445..446,449)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     CDS             1..488
                     /gene="Mfsd13b"
                     /coded_by="NM_001432657.1:275..1741"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:691551"
                     /db_xref="RGD:1582763"
ORIGIN      
        1 mseplasqeh grellkgnhq phlilgvwgw pvkaaspeks yhsfksiefl kgtkisawkm
       61 tllnikseaw ayslitlgte mlssffsfyy mklflevyki selafyqsqv ilmiwniltd
      121 lsgyfhmssq ndcclsyrcs llgallhava fllpwfpwkh yresdwltgl qlvvslcafd
      181 sthtwvqqaq crlfaetspr hesrlqltri nqvaslvgst silfcglish nmeilpnfqa
      241 iavliaflal isfysgmfhm rrfefqripe enflseseqe lagtsvillm rqilpqrnly
      301 lflimnffqv fhltffsnfm mifvdnlipn kalsssvrsi mygagficpq clvllgqswl
      361 ktygyykvil lsfclegaaa lvmlllgqeh yfclavyltv imvivhtsfc lfnlpvadmv
      421 dadllkckrq sslslmvsvi nalftrsaqs lapililskl sqhgyrelts ragdrtqgla
      481 larqalyh
//
LOCUS       NP_001013969             555 aa            linear   ROD 28-APR-2025
DEFINITION  solute carrier family 22 member 22 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001013969 XP_235317
VERSION     NP_001013969.1
DBSOURCE    REFSEQ: accession NM_001013947.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Hatano,R., Onoe,K., Obara,M., Matsubara,M., Kanai,Y., Muto,S. and
            Asano,S.
  TITLE     Sex hormones induce a gender-related difference in renal expression
            of a novel prostaglandin transporter, OAT-PG, influencing basal
            PGE2 concentration
  JOURNAL   Am J Physiol Renal Physiol 302 (3), F342-F349 (2012)
   PUBMED   22031854
  REMARK    GeneRIF: OAT-PG is involved in local PGE(2) clearance in the renal
            cortex.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 20, 2005 this sequence version replaced XP_235317.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081982.1, AB559554.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..555
                     /product="solute carrier family 22 member 22 isoform 1"
                     /note="prostaglandin transporter OAT-PG; solute carrier
                     family 22 (organic cation transporter), member 22"
                     /calculated_mol_wt=62155
     Region          109..516
                     /region_name="MFS_OAT"
                     /note="Organic anion transporters of the Major Facilitator
                     Superfamily of transporters; cd17374"
                     /db_xref="CDD:340932"
     Site            order(126..127,130..131,134,160,210..211,213..215,218,234,
                     237..238,241,357,360..361,364..366,369,389,393,444..445,
                     449,453,469,472..473,476..477,480)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340932"
     CDS             1..555
                     /gene="Slc22a22"
                     /gene_synonym="oat-pg; RGD1304605"
                     /coded_by="NM_001013947.2:70..1737"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:299944"
                     /db_xref="RGD:1304605"
ORIGIN      
        1 mafdeilhhv gdrgrfqiwm ivvlnilsmv sslhdvienf taaipahhcs vnlldtsrse
       61 ismamnltte ammkvsipmg pnqkpeqcrr frhpqwqfid snistsnste letepcldgw
      121 tydhsvftst ivtewdlvcd fqsfkyyaqa tslaghfvaa pfcgiisdrf grkpllmycs
      181 laygilgtcc afvpnfslyc vlrflssasa stvgmnclil vleetsvqwh atvivlsglf
      241 sstglaglgg layvlsdwhl iqltsalpyf iffilfcwvp esarwlmitg ktdqalkelq
      301 riasingkkd iaqnlttedl rskvkedvcs tvkhfsikdi iinpmirkiv lcyssvlfae
      361 lfsifgllld vhmlgknifv tqillgvidi psksltyfil rnvrrrplia fllfatggci
      421 titmflsedm yvlrlaifil gkgcfaafis intaycnels pvplrstlng iyisvarlas
      481 vlsaltlvtr kyfvllpmif cgvlpivati niyflpetfn hpitdtikdm ekrnrlmskn
      541 isekegqdfl ettnc
//
LOCUS       NP_445888                495 aa            linear   ROD 28-APR-2025
DEFINITION  double-stranded RNA-binding protein Staufen homolog 1 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_445888
VERSION     NP_445888.1
DBSOURCE    REFSEQ: accession NM_053436.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Lee,K., Yoo,K.S., Park,Y.S. and Kim,H.K.
  TITLE     Activity of Arhgef4 is modulated through Staufen1 in neurons
  JOURNAL   Neurosci Lett 756, 135962 (2021)
   PUBMED   34022264
  REMARK    GeneRIF: Activity of Arhgef4 is modulated through Staufen1 in
            neurons.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Xue,Y., Guo,Y., Luo,S., Zhou,W., Xiang,J., Zhu,Y., Xiang,Z. and
            Shen,J.
  TITLE     Aberrantly Methylated-Differentially Expressed Genes Identify Novel
            Atherosclerosis Risk Subtypes
  JOURNAL   Front Genet 11, 569572 (2020)
   PUBMED   33381146
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Blackham,S.L. and McGarvey,M.J.
  TITLE     A host cell RNA-binding protein, Staufen1, has a role in hepatitis
            C virus replication before virus assembly
  JOURNAL   J Gen Virol 94 (Pt 11), 2429-2436 (2013)
   PUBMED   23907398
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Ghoujal,B., Milev,M.P., Ajamian,L., Abel,K. and Mouland,A.J.
  TITLE     ESCRT-II's involvement in HIV-1 genomic RNA trafficking and
            assembly
  JOURNAL   Biol Cell 104 (12), 706-721 (2012)
   PUBMED   22978549
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Villace,P., Marion,R.M. and Ortin,J.
  TITLE     The composition of Staufen-containing RNA granules from human cells
            indicates their role in the regulated transport and translation of
            messenger RNAs
  JOURNAL   Nucleic Acids Res 32 (8), 2411-2420 (2004)
   PUBMED   15121898
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Macchi,P., Kroening,S., Palacios,I.M., Baldassa,S., Grunewald,B.,
            Ambrosino,C., Goetze,B., Lupas,A., St Johnston,D. and Kiebler,M.
  TITLE     Barentsz, a new component of the Staufen-containing
            ribonucleoprotein particles in mammalian cells, interacts with
            Staufen in an RNA-dependent manner
  JOURNAL   J Neurosci 23 (13), 5778-5788 (2003)
   PUBMED   12843282
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Monshausen,M., Rehbein,M., Richter,D. and Kindler,S.
  TITLE     The RNA-binding protein Staufen from rat brain interacts with
            protein phosphatase-1
  JOURNAL   J Neurochem 81 (3), 557-564 (2002)
   PUBMED   12065664
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Monshausen,M., Putz,U., Rehbein,M., Schweizer,M.,
            DesGroseillers,L., Kuhl,D., Richter,D. and Kindler,S.
  TITLE     Two rat brain staufen isoforms differentially bind RNA
  JOURNAL   J Neurochem 76 (1), 155-165 (2001)
   PUBMED   11145988
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Kiebler,M.A., Hemraj,I., Verkade,P., Kohrmann,M., Fortes,P.,
            Marion,R.M., Ortin,J. and Dotti,C.G.
  TITLE     The mammalian staufen protein localizes to the somatodendritic
            domain of cultured hippocampal neurons: implications for its
            involvement in mRNA transport
  JOURNAL   J Neurosci 19 (1), 288-297 (1999)
   PUBMED   9870958
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN932990.1, AF227200.1 and BC081755.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF227200.1, SRR8487227.63913.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..495
                     /product="double-stranded RNA-binding protein Staufen
                     homolog 1 isoform 1"
                     /note="staufen RNA binding protein homolog 1;
                     double-stranded RNA-binding protein Staufen homolog 1"
                     /calculated_mol_wt=54671
     Region          1..70
                     /region_name="DSRM_SF"
                     /note="double-stranded RNA binding motif (DSRM)
                     superfamily; cl00054"
                     /db_xref="CDD:444671"
     Site            order(16..17,19,39,56..58,61)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380710"
     Region          95..167
                     /region_name="DSRM_SF"
                     /note="double-stranded RNA binding motif (DSRM)
                     superfamily; cl00054"
                     /db_xref="CDD:444671"
     Site            order(102..103,105,134,151..153,156)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380712"
     Region          194..279
                     /region_name="DSRM_STAU1_rpt4"
                     /note="fourth double-stranded RNA binding motif of
                     double-stranded RNA-binding protein Staufen homolog 1
                     (Staufen 1) and similar proteins; cd19885"
                     /db_xref="CDD:380714"
     Site            order(208,211..212,214..215,230..235,255,259)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380714"
     Region          366..475
                     /region_name="Staufen_C"
                     /note="Staufen C-terminal domain; pfam16482"
                     /db_xref="CDD:465131"
     CDS             1..495
                     /gene="Stau1"
                     /gene_synonym="Stau"
                     /coded_by="NM_053436.2:240..1727"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:84496"
                     /db_xref="RGD:621778"
ORIGIN      
        1 mykpvdphsr mqstysygmr ggayppryfy pfpvppllyq velsvggqqf ngkgkmrppv
       61 khdataralr tlqseplper levngresee enlnkseisq vfeialkrnl pvnfesfplt
      121 qvaresgpph mknfvtrvsv gefvgegegk skkiskknaa ravleqlrrl pplpavervk
      181 prikkksqpt cklqtapdyg qgmnpisrla qiqqakkeke peymllterg lprrrefvmq
      241 vkvghhtaeg agtnkkvakr naaenmleil gfkvpqaqpa kpalkseekt pvkkpgdgrk
      301 vtffepspgd engtsnkede frmpylshqq lpagilpmvp evaqavgvsq ghhtkdfara
      361 apnpakatvt amiarellyg gtsptaetil ksnissghvp hgprtrpseq lyylsraqgf
      421 qveykdfpkn nknecvslin cssqpplvsh gigkdvesch dmaalnilkl lseldqqste
      481 mprtgngpvs acgrc
//
LOCUS       NP_001419589             455 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC691551 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001419589 XP_017445709
VERSION     NP_001419589.1
DBSOURCE    REFSEQ: accession NM_001432660.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 1, 2024 this sequence version replaced XP_017445709.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.5553.1,
                                           SRR26360181.3375591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..455
                     /product="uncharacterized protein LOC691551 isoform 5"
                     /note="transmembrane protein 180"
                     /calculated_mol_wt=51787
     Region          12..449
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(20..21,24..25,28,61,124..125,127..129,132,153,
                     156..157,160,250,253..254,257..259,262,290,294,346..347,
                     351,355,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     CDS             1..455
                     /gene="Mfsd13b"
                     /coded_by="NM_001432660.1:511..1878"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:691551"
                     /db_xref="RGD:1582763"
ORIGIN      
        1 mtllniksea wayslitlgt emlssffsfy ymklflevyk iselafyqsq vilmiwnilt
       61 dlsgyfhmss qndcclsyrc sllgallhav afllpwfpwk hyresdwltg lqlvvslcaf
      121 dsthtwvqqa qcrlfaetsp rhesrlqltr inqvaslvgs tsilfcglis hnmeilpnfq
      181 aiavliafla lisfysgmfh mrrfefqrip eenflseseq elagtsvill mrqilpqrnl
      241 ylflimnffq vfhltffsnf mmifvdnlip nkalsssvrs imygagficp qclvllgqsw
      301 lktygyykvi llsfclegaa alvmlllgqe hyfclavylt vimvivhtsf clfnlpvadm
      361 vdadllkckr qsslslmvsv inalftrsaq slapililsk lsqhgyrelt srtlldlqds
      421 mfglvcvisl giatvqiltw ssfsiskrrd cpgmv
//
LOCUS       NP_113882                513 aa            linear   ROD 28-APR-2025
DEFINITION  heat shock factor protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_113882
VERSION     NP_113882.1
DBSOURCE    REFSEQ: accession NM_031694.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Kanugovi Vijayavittal,A., Kumar,P., Sugunan,S., Joseph,C.,
            Devaki,B., Paithankar,K. and Amere Subbarao,S.
  TITLE     Heat shock transcription factor HSF2 modulates the autophagy
            response through the BTG2-SOD2 axis
  JOURNAL   Biochem Biophys Res Commun 600, 44-50 (2022)
   PUBMED   35182974
  REMARK    GeneRIF: Heat shock transcription factor HSF2 modulates the
            autophagy response through the BTG2-SOD2 axis.
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Huang,C.Y., Chen,J.Y., Kuo,C.H., Pai,P.Y., Ho,T.J., Chen,T.S.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     Mitochondrial ROS-induced ERK1/2 activation and HSF2-mediated AT1 R
            upregulation are required for doxorubicin-induced cardiotoxicity
  JOURNAL   J Cell Physiol 233 (1), 463-475 (2018)
   PUBMED   28295305
  REMARK    GeneRIF: DOX induced mitochondrial ROS release to activate
            ERK1/2-mediated HSF2 nuclear translocation and AT1 R upregulation
            causing DOX-damaged heart failure in vitro and in vivo.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Huang,C.Y., Pai,P.Y., Kuo,C.H., Ho,T.J., Lin,J.Y., Lin,D.Y.,
            Tsai,F.J., Padma,V.V., Kuo,W.W. and Huang,C.Y.
  TITLE     p53-mediated miR-18 repression activates HSF2 for IGF-IIR-dependent
            myocyte hypertrophy in hypertension-induced heart failure
  JOURNAL   Cell Death Dis 8 (8), e2990 (2017)
   PUBMED   28796250
  REMARK    GeneRIF: p53-mediated miR-18 repression activates HSF2 for
            IGF-IIR-dependent myocyte hypertrophy in hypertension-induced heart
            failure
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Liu,F., Xu,Z.L., Qian,X.J., Qiu,W.Y. and Huang,H.
  TITLE     Expression of Hsf1, Hsf2, and Phlda1 in cells undergoing
            cryptorchid-induced apoptosis in rat testes
  JOURNAL   Mol Reprod Dev 78 (4), 283-291 (2011)
   PUBMED   21480429
  REMARK    GeneRIF: The Hsf2 is mainly expressed in round spermatids in
            control testis. Hsf2 expression is significantly increased in both
            nuclei and cytoplasm of spermatocytes in 7-day cryptorchid testis.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Fujimoto,M., Oshima,K., Shinkawa,T., Wang,B.B., Inouye,S.,
            Hayashida,N., Takii,R. and Nakai,A.
  TITLE     Analysis of HSF4 binding regions reveals its necessity for gene
            regulation during development and heat shock response in mouse
            lenses
  JOURNAL   J Biol Chem 283 (44), 29961-29970 (2008)
   PUBMED   18755693
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Kwong,J.M., Lalezary,M., Nguyen,J.K., Yang,C., Khattar,A., Piri,N.,
            Mareninov,S., Gordon,L.K. and Caprioli,J.
  TITLE     Co-expression of heat shock transcription factors 1 and 2 in rat
            retinal ganglion cells
  JOURNAL   Neurosci Lett 405 (3), 191-195 (2006)
   PUBMED   16889897
  REMARK    GeneRIF: both heat shock transcription 2 is linked to the heat
            shock response in retinal ganglion cells.
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Wang,G., Ying,Z., Jin,X., Tu,N., Zhang,Y., Phillips,M.,
            Moskophidis,D. and Mivechi,N.F.
  TITLE     Essential requirement for both hsf1 and hsf2 transcriptional
            activity in spermatogenesis and male fertility
  JOURNAL   Genesis 38 (2), 66-80 (2004)
   PUBMED   14994269
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Min,J.N., Han,M.Y., Lee,S.S., Kim,K.J. and Park,Y.M.
  TITLE     Regulation of rat heat shock factor 2 expression during the early
            organogenic phase of embryogenesis
  JOURNAL   Biochim Biophys Acta 1494 (3), 256-262 (2000)
   PUBMED   11121583
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Eriksson,M., Jokinen,E., Sistonen,L. and Leppa,S.
  TITLE     Heat shock factor 2 is activated during mouse heart development
  JOURNAL   Int J Dev Biol 44 (5), 471-477 (2000)
   PUBMED   11032181
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Kubota,H., Matsumoto,S., Yokota,S., Yanagi,H. and Yura,T.
  TITLE     Transcriptional activation of mouse cytosolic chaperonin CCT
            subunit genes by heat shock factors HSF1 and HSF2
  JOURNAL   FEBS Lett 461 (1-2), 125-129 (1999)
   PUBMED   10561509
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086554.1, AF172640.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..513
                     /product="heat shock factor protein 2 isoform 1"
                     /note="heat shock factor 2; heat shock factor protein 2;
                     heat shock transcription factor hsf2"
                     /calculated_mol_wt=57613
     Region          6..110
                     /region_name="HSF"
                     /note="heat shock factor; smart00415"
                     /db_xref="CDD:214654"
     Region          230..478
                     /region_name="Vert_HS_TF"
                     /note="Vertebrate heat shock transcription factor;
                     pfam06546"
                     /db_xref="CDD:461944"
     CDS             1..513
                     /gene="Hsf2"
                     /coded_by="NM_031694.3:95..1636"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64441"
                     /db_xref="RGD:68395"
ORIGIN      
        1 mkqssnvpaf lsklwtlvee thtnefitws qngqsflvld eqrfakeilp kyfkhnnmas
       61 fvrqlnmygf rkvvhiesgi vkqerdgpve fqhphfkqgq ddllenikrk vssskpeenk
      121 irqedltkii ssaqkvqikq etiesrlsel kseneslwke vselrakhaq qqqvirkivq
      181 fivtlvqnnq lvslkrkrpl llntngapkk nlfqhivkep tdnhhhkvph srteglksre
      241 risddiiiyd vtednvdeen ipvipetned vvvdpssqyp diviveddne deyapviqsg
      301 eqseparvgs assssplmss avqlngssnl tsedpvtmmd silndninll gkvelldyld
      361 sidcsledfq amlsgrqfsi dpdllvdsen kgleatknsv vqqvseegrk skskpdkqli
      421 qytafpllaf ldgnpasave qgtttassev vpsvdkpiev delldsnldq eptqsklvrl
      481 eplteaease atlfylcela papldsdmpl lds
//
LOCUS       NP_001424114             766 aa            linear   ROD 28-APR-2025
DEFINITION  alpha-adducin isoform 4 [Rattus norvegicus].
ACCESSION   NP_001424114 XP_006251222
VERSION     NP_001424114.1
DBSOURCE    REFSEQ: accession NM_001437185.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Kugelmann,D., Waschke,J. and Radeva,M.Y.
  TITLE     Adducin is involved in endothelial barrier stabilization
  JOURNAL   PLoS One 10 (5), e0126213 (2015)
   PUBMED   25978380
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Procino,G., Romano,F., Torielli,L., Ferrari,P., Bianchi,G.,
            Svelto,M. and Valenti,G.
  TITLE     Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension
  JOURNAL   Am J Hypertens 24 (7), 822-828 (2011)
   PUBMED   21451595
  REMARK    GeneRIF: Altered expression of renal aquaporins and alpha-adducin
            polymorphisms may contribute to the establishment of salt-sensitive
            hypertension.
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Tripodi,G., Casari,G., Tisminetzky,S., Bianchi,G., Devescovi,G.,
            Muro,A., Tuteja,R. and Baralle,F.E.
  TITLE     Characterisation and chromosomal localisation of the rat alpha- and
            beta-adducin-encoding genes
  JOURNAL   Gene 166 (2), 307-311 (1995)
   PUBMED   8543181
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Seidel,B., Zuschratter,W., Wex,H., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Spatial and sub-cellular localization of the membrane
            cytoskeleton-associated protein alpha-adducin in the rat brain
  JOURNAL   Brain Res 700 (1-2), 13-24 (1995)
   PUBMED   8624703
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Dong,L., Chapline,C., Mousseau,B., Fowler,L., Ramsay,K.,
            Stevens,J.L. and Jaken,S.
  TITLE     35H, a sequence isolated as a protein kinase C binding protein, is
            a novel member of the adducin family
  JOURNAL   J Biol Chem 270 (43), 25534-25540 (1995)
   PUBMED   7592723
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 28, 2025 this sequence version replaced XP_006251222.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.54976.1,
                                           SRR26643296.33289.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..766
                     /product="alpha-adducin isoform 4"
                     /note="alpha-adducin; erythrocyte adducin subunit alpha;
                     alpha-ADD; adducin 1 (alpha)"
                     /calculated_mol_wt=83556
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Region          588..>737
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     CDS             1..766
                     /gene="Add1"
                     /coded_by="NM_001437185.1:181..2481"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:24170"
                     /db_xref="RGD:2041"
ORIGIN      
        1 mngdtraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmta svpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvkv nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdakcivhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekiliqknl gpkskvlilr
      301 nhglvsvges veeaffyihn lvvaceiqvr tlasaggpdn lvlldpgkyk aksrspgtpa
      361 gegsgsppkw qigeqefeal mrmldnlgyr tgypyrypal rerskkysdv evpasvtghs
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgddaseeg qngsspkskt kvwtnithdh
      481 vkpllqslss gvcvpscitn clwtkedghr tstsavpnlf vplntnpkev qemrnkireq
      541 nlqdiktagp qsqvlcgvmm drslvqgelv taskaiieke yqphvivstt gpnpfntltd
      601 releeyrrev erkqkgseen ldetreqkek sppdqsavpn tppstpvkle gglpqeptsr
      661 dgsdattskp tppdlspdep sealafptva eeahaspdtt qplaeadpep asasapgaee
      721 vaspateegs pmdpgsdgsp gkspskkkkk frtpsflkks kkksds
//
LOCUS       NP_001416596             306 aa            linear   ROD 28-APR-2025
DEFINITION  forkhead box protein R1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416596 XP_006243030
VERSION     NP_001416596.1
DBSOURCE    REFSEQ: accession NM_001429667.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 25, 2024 this sequence version replaced XP_006243030.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.492649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..306
                     /product="forkhead box protein R1 isoform 2"
                     /note="forkhead box protein R1"
                     /calculated_mol_wt=34621
     Region          173..261
                     /region_name="FH_FOXR"
                     /note="Forkhead (FH) domain found in the Forkhead box
                     protein R (FOXR) subfamily; cd20036"
                     /db_xref="CDD:410810"
     Site            order(180,198..199,202,221..222,224..225,228,235,249..251,
                     253)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410810"
     CDS             1..306
                     /gene="Foxr1"
                     /coded_by="NM_001429667.1:433..1353"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315601"
                     /db_xref="RGD:1309739"
ORIGIN      
        1 mgnecflsft tshlseaeqk lalyrlrive ppklplekip npdkdgpdik pnlwmwvnpn
       61 ivyppgklev avkkedsssa ppasqsalke edscseasei paqqpppprk qkrkqkekhi
      121 asspsiweep teeeeakdrd dsfsvalpsl ptraplqnrw rlrqaispeg rlwsrpplhy
      181 fhlialalrn sppcglsvqq iynftrehfp ffrtapeawk ntvrhnlcfr dsfekvpvsk
      241 qgeastrprs clwklteegh rrfseeartl astrlqsiqq cmsqpgvkpc qvheprgggp
      301 eaqtlg
//
LOCUS       NP_001424528             887 aa            linear   ROD 28-APR-2025
DEFINITION  transportin-2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424528 XP_017456753
VERSION     NP_001424528.1
DBSOURCE    REFSEQ: accession NM_001437599.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   van der Giessen,K. and Gallouzi,I.E.
  TITLE     Involvement of transportin 2-mediated HuR import in muscle cell
            differentiation
  JOURNAL   Mol Biol Cell 18 (7), 2619-2629 (2007)
   PUBMED   17475777
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Apr 4, 2025 this sequence version replaced XP_017456753.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.64053.1,
                                           SRR26643298.75672.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..887
                     /product="transportin-2 isoform 2"
                     /note="transportin 2 (importin 3, karyopherin beta 2b)"
                     /calculated_mol_wt=100268
     Region          22..756
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Region          93..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(106..107,110,113..114,144..145,148,151..152,155,
                     190..191,194,197..198,201,231..232,235,238..239,272..273,
                     276,279..280)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          127..155
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          165..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          213..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          252..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(412..413,416,419..420,453..454,457,460..461,464,
                     495..496,499,502..503,506,536..537,540,543..544,579..580,
                     585,588..589)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          436..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          518..544
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          559..590
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          659..693
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          705..735
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          746..774
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..887
                     /gene="Tnpo2"
                     /coded_by="NM_001437599.1:155..2818"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:304670"
                     /db_xref="RGD:1310356"
ORIGIN      
        1 mdwqpdeqgl qqvlqllkds qspntatqri vqdklkqlnq fpdfnnylif vltrlksede
       61 ptrslsglil knnvkahyqs fpppvadfik qeclnnigda ssliratigi littiaskge
      121 lqmwpellpq lcnllnsedy ntcegafgal qkicedssel ldsdalnrpl nimipkflqf
      181 fkhcspkirs haiacvnqfi mdraqalmdn idtfiehlfa lavdddpevr knvcralvml
      241 levridrlip hmhsiiqyml qrtqdhdenv aleacefwlt laeqpickev lashlvqlip
      301 ilvngmkyse idiillkgdv eedeavpdse qdikprfhks rtvtltheae rpdgsedaed
      361 dddddalsdw nlrkcsaaal dvlanvfree llphllpllk gllfhpewvv kesgilvlga
      421 iaegcmqgmv pylpeliphl iqclsdkkal vrsiacwtls ryahwvvsqp pdmhlkplmt
      481 ellkrildgn krvqeaacsa fatleeeact elvpylsyil dtlvfafgky qhknllilyd
      541 aigtladsvg hhlnqpeyiq klmppliqkw nelkdedkdl fplleclssv atalqsgflp
      601 ycepvyqrcv tlvqktlaqa mmytqhpeqy eapdkdfmiv aldllsglae glgghveqlv
      661 arsnimtllf qcmqdsmpev rqssfallgd ltkacfihvk pciaefmpil gtnlnpefis
      721 vcnnatwaig eicmqmgaem qpyvqmvlsn lveiinrpnt pktllentai tigrlgyvcp
      781 qevapmlqqf irpwctslrn irdneekdsa frgicmmigv npggvvqdfi ffcdavaswv
      841 spkddlrdmf ykilhgfkdq vgeenwqqfs eqfppllker laafygv
//
LOCUS       NP_001417059             215 aa            linear   ROD 28-APR-2025
DEFINITION  disks large homolog 5-like isoform 1 [Rattus norvegicus].
ACCESSION   NP_001417059 XP_063122394
VERSION     NP_001417059.1
DBSOURCE    REFSEQ: accession NM_001430130.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On May 7, 2024 this sequence version replaced XP_063122394.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1273782.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8"
     Protein         1..215
                     /product="disks large homolog 5-like isoform 1"
                     /calculated_mol_wt=25508
     Region          48..134
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..215
                     /gene="LOC134480032"
                     /coded_by="NM_001430130.1:38..685"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:134480032"
                     /db_xref="RGD:402237256"
ORIGIN      
        1 mfsrlrknfg rvnadfgqtg vresrlsski ndgqrklawg mlkdgrltss pgpvvinkea
       61 ntenteeqrl irqlqsatee rnelrdllty vteryrnnra sryirsnpfy eklkikerev
      121 msllhnlemr niehcekfqe iqkeinfyrn lpirihmdki cmqkklfpfr keskaeqlds
      181 apllqkflfd lnkkdkdeqe ktsnlqtkqh ldntt
//
LOCUS       NP_001101357            1120 aa            linear   ROD 28-APR-2025
DEFINITION  scavenger receptor cysteine-rich type 1 protein M130 precursor
            [Rattus norvegicus].
ACCESSION   NP_001101357 XP_001061914 XP_232342
VERSION     NP_001101357.1
DBSOURCE    REFSEQ: accession NM_001107887.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Yip,J.L.K., Xavier,S., Balasuriya,G.K., Hill-Yardin,E.L. and
            Spencer,S.J.
  TITLE     Macrophage regulation of the 'second brain': CD163 intestinal
            macrophages interact with inhibitory interneurons to regulate
            colonic motility - evidence from the Cx3cr1-Dtr rat model
  JOURNAL   Front Immunol 14, 1269890 (2023)
   PUBMED   37868978
  REMARK    GeneRIF: Macrophage regulation of the 'second brain': CD163
            intestinal macrophages interact with inhibitory interneurons to
            regulate colonic motility - evidence from the Cx3cr1-Dtr rat model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Fischer-Riepe,L., Daber,N., Schulte-Schrepping,J., Veras De
            Carvalho,B.C., Russo,A., Pohlen,M., Fischer,J., Chasan,A.I.,
            Wolf,M., Ulas,T., Glander,S., Schulz,C., Skryabin,B., Wollbrink
            Dipl-Ing,A., Steingraeber,N., Stremmel,C., Koehle,M., Gartner,F.,
            Vettorazzi,S., Holzinger,D., Gross,J., Rosenbauer,F., Stoll,M.,
            Niemann,S., Tuckermann,J., Schultze,J.L., Roth,J. and
            Barczyk-Kahlert,K.
  TITLE     CD163 expression defines specific, IRF8-dependent,
            immune-modulatory macrophages in the bone marrow
  JOURNAL   J Allergy Clin Immunol 146 (5), 1137-1151 (2020)
   PUBMED   32199911
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Etzerodt,A., Moulin,M., Doktor,T.K., Delfini,M.,
            Mossadegh-Keller,N., Bajenoff,M., Sieweke,M.H., Moestrup,S.K.,
            Auphan-Anezin,N. and Lawrence,T.
  TITLE     Tissue-resident macrophages in omentum promote metastatic spread of
            ovarian cancer
  JOURNAL   J Exp Med 217 (4) (2020)
   PUBMED   31951251
REFERENCE   4  (residues 1 to 1120)
  AUTHORS   Dighal,A., Mukhopadhyay,D., Sengupta,R., Moulik,S., Mukherjee,S.,
            Roy,S., Chaudhuri,S.J., Das,N.K. and Chatterjee,M.
  TITLE     Iron trafficking in patients with Indian Post kala-azar dermal
            leishmaniasis
  JOURNAL   PLoS Negl Trop Dis 14 (2), e0007991 (2020)
   PUBMED   32023254
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1120)
  AUTHORS   Sun,H., Jiang,R., Han,B., Du,X., Ma,C., Xu,Y., Chen,Z., Wang,L.,
            Yang,S., Lv,X., Zhao,H. and Li,X.
  TITLE     Serum levels of soluble CD163 and soluble CD14 following antibiotic
            therapy of patients with acute brucellosis
  JOURNAL   J Infect Dev Ctries 13 (8), 714-719 (2019)
   PUBMED   32069255
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1120)
  AUTHORS   Kusi,K.A., Gyan,B.A., Goka,B.Q., Dodoo,D., Obeng-Adjei,G.,
            Troye-Blomberg,M., Akanmori,B.D. and Adjimani,J.P.
  TITLE     Levels of soluble CD163 and severity of malaria in children in
            Ghana
  JOURNAL   Clin Vaccine Immunol 15 (9), 1456-1460 (2008)
   PUBMED   18632918
REFERENCE   7  (residues 1 to 1120)
  AUTHORS   Fabriek,B.O., Polfliet,M.M., Vloet,R.P., van der Schors,R.C.,
            Ligtenberg,A.J., Weaver,L.K., Geest,C., Matsuno,K., Moestrup,S.K.,
            Dijkstra,C.D. and van den Berg,T.K.
  TITLE     The macrophage CD163 surface glycoprotein is an erythroblast
            adhesion receptor
  JOURNAL   Blood 109 (12), 5223-5229 (2007)
   PUBMED   17353345
  REMARK    GeneRIF: identify CD163 on macrophages as an adhesion receptor for
            erythroblasts in erythroblastic islands, and suggest a regulatory
            role for CD163 during erythropoiesis
REFERENCE   8  (residues 1 to 1120)
  AUTHORS   Nielsen,M.J., Madsen,M., Moller,H.J. and Moestrup,S.K.
  TITLE     The macrophage scavenger receptor CD163: endocytic properties of
            cytoplasmic tail variants
  JOURNAL   J Leukoc Biol 79 (4), 837-845 (2006)
   PUBMED   16434690
REFERENCE   9  (residues 1 to 1120)
  AUTHORS   Polfliet,M.M., Fabriek,B.O., Daniels,W.P., Dijkstra,C.D. and van
            den Berg,T.K.
  TITLE     The rat macrophage scavenger receptor CD163: expression, regulation
            and role in inflammatory mediator production
  JOURNAL   Immunobiology 211 (6-8), 419-425 (2006)
   PUBMED   16920481
  REMARK    GeneRIF: A broadly expressed macrophage scavenger receptor that may
            play a role in the activation of macrophages during hemolytic
            and/or inflammatory conditions.
REFERENCE   10 (residues 1 to 1120)
  AUTHORS   Schaer,D.J., Schleiffenbaum,B., Kurrer,M., Imhof,A., Bachli,E.,
            Fehr,J., Moller,H.J., Moestrup,S.K. and Schaffner,A.
  TITLE     Soluble hemoglobin-haptoglobin scavenger receptor CD163 as a
            lineage-specific marker in the reactive hemophagocytic syndrome
  JOURNAL   Eur J Haematol 74 (1), 6-10 (2005)
   PUBMED   15613100
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473964.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_232342.4, XP_001061914.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5756307,
                              SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..1120
                     /product="scavenger receptor cysteine-rich type 1 protein
                     M130 precursor"
                     /note="scavenger receptor cysteine-rich type 1 protein
                     M130; CD163 antigen; cluster of differentiation 163"
                     /calculated_mol_wt=116886
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3855
     Region          50..149
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          157..258
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          265..365
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          372..474
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          480..579
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          584..684
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          721..821
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          931..1031
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     CDS             1..1120
                     /gene="Cd163"
                     /gene_synonym="ED2"
                     /coded_by="NM_001107887.1:98..3460"
                     /db_xref="GeneID:312701"
                     /db_xref="RGD:1310382"
ORIGIN      
        1 mgknrmvllg gagspgykgf vhlgffvvav ssllsvsavt qapegrkkel rlaggenncs
       61 grvelkihek wgtvcgngws mnevsvvcqq lgcptlikap gwanasagsg diwmdkvsct
      121 gnesalwdck hegwgkhnct heqdagvtca dgsnlemrlv nsgdnrcsgr veikfqgkwg
      181 tvcddnfskd hasvickqlg cgsaisfsgs aklgagsgqi wlddlacngn esaiwdckhr
      241 gwgrhncdha edvgvicldg adlslrlvdg vskcsgrlev rfqgewgtvc ddswdrrdas
      301 vvckqlgcpt aitaigrvna segsgpiwld sisceghepa lweckhqewg khycnhkeda
      361 gvtcsdgadl elrlvgggsr cagmveveiq kltgkvcsrg wtltdadvvc rqlgcgsalq
      421 tqskiysktk teatntwlfp gscsgnetsl wqcknwqwgg lscdhfeeaq vtcsghrkpr
      481 lvggeipcsg rvevkhgdtw gsvcdfdlsl eaagvvcrel qcgtvvsilg gahfgegsgq
      541 iwgeefqcsg deshlslcsv appldrtcsh srdvsivcsr yidirladgk sscegrvelk
      601 tlgawgplcs shwdiedahv lcqqlkcgva lstpggahfg kgagqvwrhk fhctgteehi
      661 gdcpmtalgt pmcsdgqvas vicsgnqsht llpcsssssv qttsstiakd sdvpciasgq
      721 lrlvggggrc agrvevyheg swgticddsw dltdanvvck qldcgvaina tgsayfgegt
      781 gdiwldeidc sgkeshiwqc hshgwgrhnc rhkedagvvc sefmslrltn eahrvnctgr
      841 levfyngtwg sigssnmspt tvgvvcrqlg cadngtvkpt ssdktptrpm wtdsvqcpkg
      901 vdtlwqcpss pwkqrqasps qeswivcddk irlqeghtdc sgrveiwhrg swgtvcddsw
      961 dlndaevack qlgcgqavea lkeaafgpgt gpiwlnemkc rgnesslwdc parpwshsdc
     1021 ghkedasvkc lprmtlesqh gtghstltal lvcgaillvl liafllwtlk rrqtqrltvs
     1081 srgevlihqv qyqemdsktd dldllkssgw hlrnldmtas
//
LOCUS       NP_001419845             490 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 420 isoform a [Rattus norvegicus].
ACCESSION   NP_001419845 XP_038949674
VERSION     NP_001419845.1
DBSOURCE    REFSEQ: accession NM_001432916.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Beckerman,R. and Prives,C.
  TITLE     Transcriptional regulation by p53
  JOURNAL   Cold Spring Harb Perspect Biol 2 (8), a000935 (2010)
   PUBMED   20679336
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 5, 2024 this sequence version replaced XP_038949674.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1484104.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMEA5760475
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..490
                     /product="zinc finger protein 420 isoform a"
                     /note="zinc finger protein 383; Zinc finger protein
                     420-like"
                     /calculated_mol_wt=55965
     Region          27..88
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          202..224
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          215..235
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          227..252
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          243..263
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <246..490
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(332,334,336,338..339,342..343,346,360,362,366..367,
                     370..371,374,388,390,392,394..395,398..399,402)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..490
                     /gene="Zfp420"
                     /coded_by="NM_001432916.1:144..1616"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:103690163"
                     /db_xref="RGD:2323829"
ORIGIN      
        1 msalplqryp verggmaadh akhkkqvafs dvsldfsqee waclgpaqra lykdvmleny
       61 shllsvaglh ipkpqvisll eqgkepwmvg keltrglcsa lesmceskll slkkevyele
      121 scqrefmrlt kqgldypgfr dvlecgsqlq nghgsqepla reymptfvqq tfltlhqiin
      181 dekpyeckkc rkvftqnsqf iqhqrihige ksyeckecgk ffscgshvtr hlkihtgekp
      241 feckdcgkaf scssylsqhq rihtgkkpye ckdcgkafsy csnlidhqri htgekpyack
      301 vcgkaftkss qlfqhvrvht gekpyeckec gkaftqsskl vqhqrihtge kpyeckecgk
      361 afssgsaltn hqrihtgekp yeckdcgkaf tqssqlrqhq rihagekpfe clecgkaftq
      421 nsqlfqhqrv hsdekpyecn kcgkafnkcs nltrhlrthr ddkpcscnec gktfsnesel
      481 irhqevhsne
//
LOCUS       NP_001419015             497 aa            linear   ROD 28-APR-2025
DEFINITION  IQ motif containing M like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001419015 XP_063134586
VERSION     NP_001419015.1
DBSOURCE    REFSEQ: accession NM_001432086.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 25, 2024 this sequence version replaced XP_063134586.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.78657.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..497
                     /product="IQ motif containing M like 1 isoform 1"
                     /note="IQ domain-containing protein M-like"
                     /calculated_mol_wt=58065
     Region          283..305
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     CDS             1..497
                     /gene="Iqcml1"
                     /coded_by="NM_001432086.1:453..1946"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:102554391"
                     /db_xref="RGD:7680597"
ORIGIN      
        1 mataeaipev vegpllettq rdflqeaksl iaqhykrvne nkahgtsidv fknkhqkpkt
       61 gqfipfeikk seilnvveeh rlvlrsissp kdtakcsnlt easqqtslke qhvpniknky
      121 qpvdllkkek vklgkimddi esvskrmeke kemnlrkyrm sepfhsqigl slhnatshlg
      181 llkeladrtl ydqrsaalmr sshlphesaq tlsgasiifk dyyirplkkk eiqpikkelk
      241 plnkrsqiiv kpdkinnkvk rigphieifq lfqgrkrlif tkrivkliii iqafirgwle
      301 rkrlqrlksk alyhgpnlka vikmyrslih rvrhrlglwr trqiiyfgel eewmdrkkfy
      361 etmfakredw qglersellk yfndcghfpt qkqidelwdl fhrysegkys evirkssaie
      421 llftlyppqg arvnagtrlr stwlrplvdg eegykyiapf lpslsvleas kgvvrlphlm
      481 nqyqekkgkk nvltvld
//
LOCUS       NP_001100880             523 aa            linear   ROD 28-APR-2025
DEFINITION  adhesion G-protein coupled receptor G5 precursor [Rattus
            norvegicus].
ACCESSION   NP_001100880 XP_001061414 XP_240979
VERSION     NP_001100880.1
DBSOURCE    REFSEQ: accession NM_001107410.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474006.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001061414.1, XP_240979.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN06680442
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..523
                     /product="adhesion G-protein coupled receptor G5
                     precursor"
                     /note="probable G-protein coupled receptor 114; G
                     protein-coupled receptor 114-like"
                     /calculated_mol_wt=56179
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2593
     Region          183..228
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          242..513
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          243..267
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          276..297
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          310..332
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          352..368
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          404..427
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          451..473
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          477..502
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..523
                     /gene="Adgrg5"
                     /gene_synonym="Gpr114"
                     /coded_by="NM_001107410.1:82..1653"
                     /db_xref="GeneID:307645"
                     /db_xref="RGD:1305559"
ORIGIN      
        1 mdqhqalffc lcllaaqvvl vetlpeilnl mkrlerpigr alssrvrfih hleqmllnas
       61 fhghnltlqt nsiqslvfkl scgfpglsls satltnvsqa waphamqfpa eltknacvts
      121 rpaelrlicv yfftahlfqd drnssllnny vlgaqldhrp vnnlqrpvni sfwhnrsleg
      181 ytvtcvfwke gagkhswgaw spkgcyteqp sptqvlchcn hltyfavlml sgdpvptelq
      241 tpleyislvg csisivasll tillnahsrk lsdsttrihl nlngsvllln itfllssqmv
      301 pptvprsvct vlaatlhyal lssltwmgve gfnlylllgr vynvyirryl lklcvlgwgf
      361 pallvllllm ikssvygpcv isfsksqeng tgfqnvsmcw vrspmvhsil vmgyggltsl
      421 fnlvvlawal wilcrlrkre kalspwacrd ivmvlgltvl lgttwslaff sfsvfllpqv
      481 flftifnsly gfflflwfcs qkrysdaeak avmeavsfsq mth
//
LOCUS       NP_001101063             949 aa            linear   ROD 28-APR-2025
DEFINITION  metal transporter CNNM1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001101063 XP_001055974 XP_219879
VERSION     NP_001101063.2
DBSOURCE    REFSEQ: accession NM_001107593.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Guo,D., Ling,J., Wang,M.H., She,J.X., Gu,J. and Wang,C.Y.
  TITLE     Physical interaction and functional coupling between ACDP4 and the
            intracellular ion chaperone COX11, an implication of the role of
            ACDP4 in essential metal ion transport and homeostasis
  JOURNAL   Mol Pain 1, 15 (2005)
   PUBMED   15840172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Wang,C.Y., Yang,P., Shi,J.D., Purohit,S., Guo,D., An,H., Gu,J.G.,
            Ling,J., Dong,Z. and She,J.X.
  TITLE     Molecular cloning and characterization of the mouse Acdp gene
            family
  JOURNAL   BMC Genomics 5 (1), 7 (2004)
   PUBMED   14723793
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Feb 16, 2022 this sequence version replaced NP_001101063.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.8080.1,
                                           SRR26360194.2043226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..949
                     /product="metal transporter CNNM1 isoform 1"
                     /note="metal transporter CNNM1; cyclin M1"
                     /calculated_mol_wt=103554
     Region          250..>554
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
     Region          428..553
                     /region_name="CBS_pair_CorC_HlyC_assoc"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains the majority of which are
                     associated with the CorC_HlyC domain; cd04590"
                     /db_xref="CDD:341366"
     Region          436..503
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Site            order(463,478,482..483,486,507,529..531)
                     /site_type="other"
                     /note="putative ligand binding site I [chemical binding]"
                     /db_xref="CDD:341366"
     Region          507..552
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     CDS             1..949
                     /gene="Cnnm1"
                     /coded_by="NM_001107593.2:140..2989"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:309387"
                     /db_xref="RGD:1308728"
ORIGIN      
        1 maaaaaaaaa lgvrlrdccs rgavlllffs lsprppaaaa wllglrpedt aggrvslegg
       61 tlraaegtsf llrvyfqpgp avpaapvpap slapgengtg dwaprlvfie eppgagsaap
      121 savptrppgp qrcreqsdwa sdvevlgplr pggvagsalv qvrvrelrkg eaerggaggg
      181 gklfslcawd grawhhhgaa ggfllrvrpr lygpggdllp pawlralgal lllalsalfs
      241 glrlsllsld pvelrvlrns gsaaeqeqar rvqavrgrgt hllctlllgq aganaalagw
      301 lyaslppgvg dpgedsgeag vhfpwlpalv ctgavflgae icpysvcsrh glaiashsvc
      361 ltrllmaaaf pvcyplgrll dwalrqeist fytrekllet lraadpysdl vkeelniiqg
      421 alelrtkvve evltplgdcf mlrsdavldf atvseilrsg ytripvyegd qrhnivdilf
      481 vkdlafvdpd dctplltvtr fynrplhcvf ndtrldtvle efkkgkshla ivqrvnnege
      541 gdpfyevmgi vtlediieei ikseildetd lytdnrkkqr vphrerrrhd fslfklsdse
      601 irvkispqll lathrfmate vepfkslyls ekillrllkh pnviqelkfd ernkkapehy
      661 lyqrsrpvdy fvlllqgkve vevgkeglrf engaftyygv paimtsacsd ndvrkvgsla
      721 gssvflnrsp srcsglnrse spnrersdfg gsntqlcsnn lytpdysvhi lsdvqfvkit
      781 rqqyqnalta chmdsspqsp dmeaftdgds tkapttrgtp qtpkddpvlt llsnrtslpc
      841 srsdglrspg evvylrmeem afpqeempnf eehkaqqvsl spvtvptaaa seteccnihl
      901 dpeaspcssd seetmgkkll rtlsgrkrkk sadgerasee nsnltplit
//
LOCUS       NP_001420880            2647 aa            linear   ROD 28-APR-2025
DEFINITION  filamin-A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001420880 XP_006229631
VERSION     NP_001420880.1
DBSOURCE    REFSEQ: accession NM_001433951.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2647)
  AUTHORS   Shi,Y., Qiu,T., Wu,C., Yuan,W., Yao,X., Jiang,L., Wang,N., Wang,L.,
            Han,Q., Yang,G., Liu,X. and Sun,X.
  TITLE     Filamin A facilitates NLRP3 inflammasome activation during
            arsenic-induced nonalcoholic steatohepatitis
  JOURNAL   Environ Sci Pollut Res Int 30 (49), 107703-107715 (2023)
   PUBMED   37740811
  REMARK    GeneRIF: Filamin A facilitates NLRP3 inflammasome activation during
            arsenic-induced nonalcoholic steatohepatitis.
REFERENCE   2  (residues 1 to 2647)
  AUTHORS   Zou,M., Huang,C., Li,X., He,X., Chen,Y., Liao,W., Liao,Y., Sun,J.,
            Liu,Z., Zhong,L. and Bin,J.
  TITLE     Circular RNA expression profile and potential function of
            hsa_circRNA_101238 in human thoracic aortic dissection
  JOURNAL   Oncotarget 8 (47), 81825-81837 (2017)
   PUBMED   29137225
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2647)
  AUTHORS   Segura,I., Lange,C., Knevels,E., Moskalyuk,A., Pulizzi,R.,
            Eelen,G., Chaze,T., Tudor,C., Boulegue,C., Holt,M., Daelemans,D.,
            Matondo,M., Ghesquiere,B., Giugliano,M., Ruiz de Almodovar,C.,
            Dewerchin,M. and Carmeliet,P.
  TITLE     The Oxygen Sensor PHD2 Controls Dendritic Spines and Synapses via
            Modification of Filamin A
  JOURNAL   Cell Rep 14 (11), 2653-2667 (2016)
   PUBMED   26972007
REFERENCE   4  (residues 1 to 2647)
  AUTHORS   Tirupula,K.C., Ithychanda,S.S., Mohan,M.L., Naga Prasad,S.V.,
            Qin,J. and Karnik,S.S.
  TITLE     G protein-coupled receptors directly bind filamin A with high
            affinity and promote filamin phosphorylation
  JOURNAL   Biochemistry 54 (44), 6673-6683 (2015)
   PUBMED   26460884
REFERENCE   5  (residues 1 to 2647)
  AUTHORS   Cho,Y., Park,D. and Cavalli,V.
  TITLE     Filamin A is required in injured axons for HDAC5 activity and axon
            regeneration
  JOURNAL   J Biol Chem 290 (37), 22759-22770 (2015)
   PUBMED   26157139
REFERENCE   6  (residues 1 to 2647)
  AUTHORS   Liu,G., Thomas,L., Warren,R.A., Enns,C.A., Cunningham,C.C.,
            Hartwig,J.H. and Thomas,G.
  TITLE     Cytoskeletal protein ABP-280 directs the intracellular trafficking
            of furin and modulates proprotein processing in the endocytic
            pathway
  JOURNAL   J Cell Biol 139 (7), 1719-1733 (1997)
   PUBMED   9412467
REFERENCE   7  (residues 1 to 2647)
  AUTHORS   Ohta,Y., Stossel,T.P. and Hartwig,J.H.
  TITLE     Ligand-sensitive binding of actin-binding protein to immunoglobulin
            G Fc receptor I (Fc gamma RI)
  JOURNAL   Cell 67 (2), 275-282 (1991)
   PUBMED   1833070
REFERENCE   8  (residues 1 to 2647)
  AUTHORS   Gorlin,J.B., Yamin,R., Egan,S., Stewart,M., Stossel,T.P.,
            Kwiatkowski,D.J. and Hartwig,J.H.
  TITLE     Human endothelial actin-binding protein (ABP-280, nonmuscle
            filamin): a molecular leaf spring
  JOURNAL   J Cell Biol 111 (3), 1089-1105 (1990)
   PUBMED   2391361
REFERENCE   9  (residues 1 to 2647)
  AUTHORS   Ezzell,R.M., Kenney,D.M., Egan,S., Stossel,T.P. and Hartwig,J.H.
  TITLE     Localization of the domain of actin-binding protein that binds to
            membrane glycoprotein Ib and actin in human platelets
  JOURNAL   J Biol Chem 263 (26), 13303-13309 (1988)
   PUBMED   3138234
REFERENCE   10 (residues 1 to 2647)
  AUTHORS   Fox,J.E.
  TITLE     Identification of actin-binding protein as the protein linking the
            membrane skeleton to glycoproteins on platelet plasma membranes
  JOURNAL   J Biol Chem 260 (22), 11970-11977 (1985)
   PUBMED   4044584
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Oct 16, 2024 this sequence version replaced XP_006229631.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.66016.1,
                                           SRR26643299.69084.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2647
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..2647
                     /product="filamin-A isoform 1"
                     /note="actin binding protein 280; filamin, alpha;
                     Endothelial actin-binding protein 280); filamin A, alpha"
                     /calculated_mol_wt=281086
     Region          25..153
                     /region_name="CH_FLNA_rpt1"
                     /note="first calponin homology (CH) domain found in
                     filamin-A (FLN-A) and similar proteins; cd21308"
                     /db_xref="CDD:409157"
     Site            order(30..35,41..42,45,49,91..94,99..102,104..105,
                     108..109,111,120..128,133,135..136,138..139,142..143,146)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409157"
     Site            order(51,54..55,58..59,61,63,65..66,68..70,73,76,97..98)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409157"
     Region          156..269
                     /region_name="CH_FLNA_rpt2"
                     /note="second calponin homology (CH) domain found in
                     filamin-A (FLN-A) and similar proteins; cd21312"
                     /db_xref="CDD:409161"
     Site            order(168,172,220,222..223,226..227,229,238..246,253,
                     255..256,258..259,262..263,266)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409161"
     Site            order(226,230,233..235,240,244)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409161"
     Region          281..375
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          381..477
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          480..571
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          577..659
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          672..766
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          769..869
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          872..968
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          972..1064
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1067..1156
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1160..1252
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1256..1352
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1355..1442
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1448..1542
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1545..1639
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1665..1743
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          <1797..1861
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          1868..1954
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2047..2136
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2238..2328
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2332..2423
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2429..2519
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2558..2646
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     CDS             1..2647
                     /gene="Flna"
                     /gene_synonym="RGD1560614"
                     /coded_by="NM_001433951.1:221..8164"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:293860"
                     /db_xref="RGD:1560614"
ORIGIN      
        1 mssshsrsgq saagaspagg idtrdaempa tekdlaedap wkkiqqntft rwcnehlkcv
       61 skrianlqtd lsdglrlial levlsqkkmh rkhnqrptfr qmqlenvsva lefldresik
      121 lvsidskaiv dgnlklilgl iwtlilhysi smpmwdeeed eeakkqtpkq rllgwiqnkl
      181 pqlpitnfsr dwqsgralga lvdscapglc pdwdswdask pvnnareamq qaddwlgipq
      241 vitpeeivdp nvdehsvmty lsqfpkaklk pgaplrpkln pkkaraygpg ieptgnmvkk
      301 raeftvetrs agqgevlvyv edpaghqeea kvtanndknr tfsvwyvpev tgthkvtvlf
      361 agqhiakspf evyvdksqgd askvtaqgpg lepsgniank ttyfeiftag agigevevvi
      421 qdptgqkgtv epqleargds tyrcsyqptm egvhtvhvtf agvpiprspy tvtvgqacnp
      481 tacravgrgl qpkgvrvket adfkvytkga gsgelkvtvk gpkgeervkq kdlgdgvygf
      541 eyyptipgty tvtitwggqn igrspfevkv gtecgnqkvr awgpgleggi vgksadfvve
      601 aigddvgtlg fsvegpsqak iecddkgdgs cdvrywpqea geyavhvlcn sedirlspfm
      661 adireapqdf hpdrvkargp glektgvain kpaeftvdak hagkaplrvq vqdneghsve
      721 ttvkdngngt yscsyvprkp vkhtamvswg gvsipnspfr vnvgagshpn kvkvygpgva
      781 ktglkahept yftvdcteag qgdvsigikc apgvvgptea didfdiirnd ndtftvkytp
      841 cgagsytimv lfadqatpts pirvkvepsh daskvkaegp glnrtgvelg kpthftvnak
      901 tagkgkldvq fsglakgdav rdvdiidhhd ntytvkytpv qqgpvgvsvt yggdhipksp
      961 fsvgvspsld lskikvsglv dkvdvgkdqe ftvkskgagg qgkvaskivs psgaavpckv
     1021 epglgadnsv vrfvpreegp yevevtydgv pvpgspfpve avaptkpskv kafgpglqgg
     1081 nagsparfti dtkgagtggl gltvegpcea qlecldngdg tcsvsyvpte pgdyninilf
     1141 adthipgspf kahvvpcfda skvkcsgpgl eratagevgq fqvdcssags aeltieicse
     1201 aglpaevyiq dhgdgthtit yiplcpgayt vtikyggqpv pnfpsklqve pavdtsgvqc
     1261 ygpgiegqgv freattefsv daraltqtgg phvkarvanp sgnltdtyvq dcgdgtykve
     1321 ytpyeegvhs vdvtydgspv psspfqvpvt egcdpsrvrv hgpgiqsgtt nkpnkftvet
     1381 rgagtgglgl avegpseakm scmdnkdgsc sveyipyeag tyslnvtygg hqvpgspfkv
     1441 pvhdvtdask vkcsgpglsp gmvranlpqs fqvdtskagv aplqvkvqgp kglvepvdvv
     1501 dnadgtqtvn yvpsregsys isvlygeeev prspfkvkvl pthdaskvka sgpglnttgv
     1561 paslpvefti dakdagegll avqitdpegk pkkthiqdnh dgtytvayvp dvtgrytili
     1621 kyggdeipfs pyrvravptg daskctvtvs igghglgagi gptiqigeet vitvdtkaag
     1681 kgkvtctvct pdgsevdvdv venedgtfdi fytapqpgky vicvrfggeh vpnspfqvta
     1741 lagdqptvqt plrpqqlpsq ytypqgsqqt wiperpmvgv ngldvtslrp fdlvipftik
     1801 kgeitgevrm psgkvaqpsi tdnkdgtvtv ryspseaglh emdirydnmh ipgsplqfyv
     1861 dyvncghita ygpglthgvv nkpatftvnt kdagegglsl aiegpskaei sctdnqdgtc
     1921 svsylpvlpg dysilvkynd qhipgspfta rvtgddsmrm shlkvgsaad ipinisetdl
     1981 slltatvvpp sgreepcllk rlrnghvgis fvpketgehl vhvkkngqhv asspipvvis
     2041 qseigdasrv rvsgqglheg htfepaefii dtrdagyggl slsiegpskv dintedledg
     2101 tcrvtycpte pgnyiinikf adqhvpgspf svkvtgegrv kesitrrrra psvanvgshc
     2161 dlslkipeis iqdmtaqvts psgktheaei vegenhtyci rfvpaemgmh tvsvkykgqh
     2221 vpgspfqftv gplgeggahk vraggpgler aeagvpaefg iwtreagagg laiavegpsk
     2281 aeisfedrkd gscgvayvvq epgdyevsvk fneehipdsp fvvpvaspsg darrltvssl
     2341 qesglkvnqp asfavslnga kgaidakvhs psgaleecyv teidqdkyav rfiprengvy
     2401 lidvkfngth ipgspfkirv gepghggdpg lvsaygagle ggvtgspaef ivntsnagag
     2461 alsvtidgps kvkmdcqecp egyrvtytpm apgsylisik yggpyhiggs pfkakvtgpr
     2521 lvsnhslhet ssvfvdsltk vatvpqhats gpgpadvskv vakglglska yvgqksnftv
     2581 dcskagnnml lvgvhgprtp ceeilvkhmg srlysvsyll kdkgeytlvv kwgdehipgs
     2641 pyrimvp
//
LOCUS       NP_596920                581 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 384 isoform 1 [Rattus norvegicus].
ACCESSION   NP_596920
VERSION     NP_596920.2
DBSOURCE    REFSEQ: accession NM_133429.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Hayata,T., Nakamoto,T., Ezura,Y. and Noda,M.
  TITLE     Ciz, a transcription factor with a nucleocytoplasmic shuttling
            activity, interacts with C-propeptides of type I collagen
  JOURNAL   Biochem Biophys Res Commun 368 (2), 205-210 (2008)
   PUBMED   18211825
  REMARK    GeneRIF: These results revealed that Ciz interacts with
            C-propeptides of type I collagen and this association takes place
            in nuclei.
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Shah,R., Alvarez,M., Jones,D.R., Torrungruang,K., Watt,A.J.,
            Selvamurugan,N., Partridge,N.C., Quinn,C.O., Pavalko,F.M.,
            Rhodes,S.J. and Bidwell,J.P.
  TITLE     Nmp4/CIZ regulation of matrix metalloproteinase 13 (MMP-13)
            response to parathyroid hormone in osteoblasts
  JOURNAL   Am J Physiol Endocrinol Metab 287 (2), E289-E296 (2004)
   PUBMED   15026307
  REMARK    GeneRIF: Nmp4/CIZ is a component of a multiprotein assemblage or
            enhanceosome within the MMP-13 parathyroid hormone response region
            and that, within this context, Nmp4/CIZ promotes both basal
            expression and hormonal synergy.
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Torrungruang,K., Shah,R., Alvarez,M., Bowen,D.K., Gerard,R.,
            Pavalko,F.M., Elmendorf,J.S., Charoonpatrapong,K., Hock,J.,
            Rhodes,S.J. and Bidwell,J.P.
  TITLE     Osteoblast intracellular localization of Nmp4 proteins
  JOURNAL   Bone 30 (6), 931-936 (2002)
   PUBMED   12052465
  REMARK    GeneRIF: localization in the cytoplasm of osteoblasts[Nmp4 -
            nuclear matrix protein 4]
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Thunyakitpisal,P., Alvarez,M., Tokunaga,K., Onyia,J.E., Hock,J.,
            Ohashi,N., Feister,H., Rhodes,S.J. and Bidwell,J.P.
  TITLE     Cloning and functional analysis of a family of nuclear matrix
            transcription factors (NP/NMP4) that regulate type I collagen
            expression in osteoblasts
  JOURNAL   J Bone Miner Res 16 (1), 10-23 (2001)
   PUBMED   11149472
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Nakamoto,T., Yamagata,T., Sakai,R., Ogawa,S., Honda,H., Ueno,H.,
            Hirano,N., Yazaki,Y. and Hirai,H.
  TITLE     CIZ, a zinc finger protein that interacts with p130(cas) and
            activates the expression of matrix metalloproteinases
  JOURNAL   Mol Cell Biol 20 (5), 1649-1658 (2000)
   PUBMED   10669742
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 18, 2005 this sequence version replaced NP_596920.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF216804.1, SRR26643292.19943.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..581
                     /product="zinc finger protein 384 isoform 1"
                     /note="nuclear matrix transcription factor 4; nuclear
                     matrix protein 4; Cas-associated zinc finger protein"
                     /calculated_mol_wt=63207
     Region          171..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQJ4.1)"
     Region          <209..409
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          320..340
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(325,327,329,331..332,335..336,339,353,355,359..360,
                     363..364,367,383,385,387,389..390,393..394,397)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          348..368
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          376..398
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          406..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          502..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EQJ4.1)"
     CDS             1..581
                     /gene="Zfp384"
                     /gene_synonym="Ciz; Nmp4; Znf384"
                     /coded_by="NM_133429.3:288..2033"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171018"
                     /db_xref="RGD:708346"
ORIGIN      
        1 meeshfnsnp yfwpsiptvs gqientmfin kmkdqllpek gcglapphyp tlltvpasvs
       61 lssgismdte skseqltphs qasvtqnitv vpvpstglmt agvscsqrwr regsqsrgpg
      121 lvitspsgsl vttassaqtf pistpmivsa lppgsqalqv vpdlskkvas tlteeggggg
      181 ggggtvappk pprgrkkkrm lesglpemnd pyvlapgddd dhqkdgktyr crmcsltfys
      241 ksemqihsks htetkphkcp hcsktfanss ylaqhirihs gakpyscnfc eksfrqlshl
      301 qqhtrihskm htetikphkc phcsktfant sylaqhlrih sgakpyncsy cqkafrqlsh
      361 lqqhtrihtg drpykcahpg cekaftqlsn lqshrrqhnk dkpfkchnch raytdaasle
      421 ahlsthtvkh akvytctics raytsetylm khmrkhnppd lqqqvqaaaa aaavaqaqaq
      481 aqaqaqaqaq aqaqaqaqaq aqaqasqasq qqqqqqpppp qpphfqspga apqgggggds
      541 nqnpppqcsf dltpykpaeh hkdicltvtt stiqvehlas s
//
LOCUS       NP_001416825             163 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin-3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416825 XP_006246288
VERSION     NP_001416825.1
DBSOURCE    REFSEQ: accession NM_001429896.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Piprode,V., Singh,K., Kumar,A., Josh,S.R. and Wani,M.R.
  TITLE     IL-3 inhibits rat osteoclast differentiation induced by TNF-alpha
            and other pro-osteoclastogenic cytokines
  JOURNAL   J Biosci 46 (2021)
   PUBMED   34183475
  REMARK    GeneRIF: IL-3 inhibits rat osteoclast differentiation induced by
            TNF-alpha and other pro-osteoclastogenic cytokines.
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Lee,J., Lim,S., Song,B.W., Cha,M.J., Ham,O., Lee,S.Y., Lee,C.,
            Park,J.H., Bae,Y., Seo,H.H., Seung,M., Choi,E. and Hwang,K.C.
  TITLE     MicroRNA-29b inhibits migration and proliferation of vascular
            smooth muscle cells in neointimal formation
  JOURNAL   J Cell Biochem 116 (4), 598-608 (2015)
   PUBMED   25389122
  REMARK    GeneRIF: Findings demonstrated that miR-29b successfully suppressed
            the proliferation and migration of smooth muscle cells induced by
            IL-3 stimulation, probably through targeting of Mcl-1 and MMP2.
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Miyake,Y., Tanaka,K. and Arakawa,M.
  TITLE     IL3 rs40401 polymorphism and interaction with smoking in risk of
            asthma in Japanese women: the Kyushu Okinawa Maternal and Child
            Health study
  JOURNAL   Scand J Immunol 79 (6), 410-414 (2014)
   PUBMED   24684517
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Miyake,Y., Tanaka,K. and Arakawa,M.
  TITLE     IL3 SNP rs40401 variant is a risk factor for rhinoconjunctivitis in
            Japanese women: the Kyushu Okinawa maternal and child health study
  JOURNAL   Cytokine 64 (1), 86-89 (2013)
   PUBMED   23953855
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Dougan,M., Li,D., Neuberg,D., Mihm,M., Googe,P., Wong,K.K. and
            Dranoff,G.
  TITLE     A dual role for the immune response in a mouse model of
            inflammation-associated lung cancer
  JOURNAL   J Clin Invest 121 (6), 2436-2446 (2011)
   PUBMED   21537082
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Ito,T., Jagus,R. and May,W.S.
  TITLE     Interleukin 3 stimulates protein synthesis by regulating
            double-stranded RNA-dependent protein kinase
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7455-7459 (1994)
   PUBMED   7519779
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Tsuji,K., Lyman,S.D., Sudo,T., Clark,S.C. and Ogawa,M.
  TITLE     Enhancement of murine hematopoiesis by synergistic interactions
            between steel factor (ligand for c-kit), interleukin-11, and other
            early acting factors in culture
  JOURNAL   Blood 79 (11), 2855-2860 (1992)
   PUBMED   1375116
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Okada,S., Nakauchi,H., Nagayoshi,K., Nakamura,M., Miura,Y. and
            Suda,T.
  TITLE     Synergistic effect of IL-3 and IL-6 on highly enriched murine
            hemopoietic progenitors
  JOURNAL   Exp Hematol 20 (5), 546-551 (1992)
   PUBMED   1350248
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Haig,D.M., McMenamin,C., Redmond,J., Brown,D., Young,I.G.,
            Cohen,S.D. and Hapel,A.J.
  TITLE     Rat IL-3 stimulates the growth of rat mucosal mast cells in culture
  JOURNAL   Immunology 65 (2), 205-211 (1988)
   PUBMED   3263940
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Cohen,D.R., Hapel,A.J. and Young,I.G.
  TITLE     Cloning and expression of the rat interleukin-3 gene
  JOURNAL   Nucleic Acids Res 14 (9), 3641-3658 (1986)
   PUBMED   3086845
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 2, 2024 this sequence version replaced XP_006246288.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U81493.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN09345331
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..163
                     /product="interleukin-3 isoform 2"
                     /note="IL-3; MCGF; mast cell growth factor;
                     P-cell-stimulating factor; hematopoietic growth factor;
                     multipotential colony-stimulating factor"
                     /calculated_mol_wt=18196
     Region          34..137
                     /region_name="IL3"
                     /note="Interleukin-3; pfam02059"
                     /db_xref="CDD:460431"
     CDS             1..163
                     /gene="Il3"
                     /coded_by="NM_001429896.1:29..520"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24495"
                     /db_xref="RGD:2897"
ORIGIN      
        1 mvlassttsi lcmllpllml fhqglqfsgs ahrllrtldc rtialeilvk lpvsglnnsd
       61 dkanlrnstl rrvnldeflk sqeefdsqdt mdiksklqkl kccipaaasd svlpgvynkd
      121 lddfkkklrf yvihlkdlqp vsvsrppqpt sssdnfrpmt vec
//
LOCUS       NP_001103048             166 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC690326 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001103048 XP_001074099
VERSION     NP_001103048.1
DBSOURCE    REFSEQ: accession NM_001109578.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001074099.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI289662.1, SRR22582416.1299000.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..166
                     /product="uncharacterized protein LOC690326 isoform 1
                     precursor"
                     /note="lipoprotein(a) like 2, pseudogene"
                     /calculated_mol_wt=15822
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2157
     CDS             1..166
                     /gene="Lpal2"
                     /coded_by="NM_001109578.2:210..710"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:690326"
                     /db_xref="RGD:1597362"
ORIGIN      
        1 maasrillvl lsisllalts aqranedden spqdqealee gdanqqnggi hkglneiknh
       61 lqdqlnqhge esiklrrgkn gqgrnrrsad dslegqdlqs enqrggdgqg drgrrgqkgq
      121 kgkggqkgqk gkggqkgqkg kggqkgqkgk ggrrnqqend qqfsqe
//
LOCUS       NP_001386536             110 aa            linear   ROD 28-APR-2025
DEFINITION  anaphase-promoting complex subunit 16 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001386536 XP_008771177
VERSION     NP_001386536.1
DBSOURCE    REFSEQ: accession NM_001399607.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Jan 12, 2022 this sequence version replaced XP_008771177.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210195.1, FQ100981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676807 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..110
                     /product="anaphase-promoting complex subunit 16 isoform 1"
                     /note="rCG22080-like"
                     /calculated_mol_wt=11514
     Region          27..106
                     /region_name="ANAPC16"
                     /note="Anaphase-promoting complex, subunit 16; pfam17256"
                     /db_xref="CDD:435817"
     CDS             1..110
                     /gene="Anapc16"
                     /coded_by="NM_001399607.1:147..479"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100360936"
                     /db_xref="RGD:2321124"
ORIGIN      
        1 maassssssa ggvsgssvpg sgfsvsdlap prkalftypk gageiledgs erflcesvfs
       61 yqvastlkqv khdqqvarme klaglveele adewrfkpie qllgftpssg
//
LOCUS       NP_001099240             902 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 598 [Rattus norvegicus].
ACCESSION   NP_001099240 XP_001056388 XP_213230
VERSION     NP_001099240.1
DBSOURCE    REFSEQ: accession NM_001105770.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Sundaramoorthy,E., Leonard,M., Mak,R., Liao,J., Fulzele,A. and
            Bennett,E.J.
  TITLE     ZNF598 and RACK1 Regulate Mammalian Ribosome-Associated Quality
            Control Function by Mediating Regulatory 40S Ribosomal
            Ubiquitylation
  JOURNAL   Mol Cell 65 (4), 751-760 (2017)
   PUBMED   28132843
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Juszkiewicz,S. and Hegde,R.S.
  TITLE     Initiation of Quality Control during Poly(A) Translation Requires
            Site-Specific Ribosome Ubiquitination
  JOURNAL   Mol Cell 65 (4), 743-750 (2017)
   PUBMED   28065601
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Fu,X., Zang,K., Zhou,Z., Reichardt,L.F. and Xu,B.
  TITLE     Retrograde neurotrophic signaling requires a protein interacting
            with receptor tyrosine kinases via C2H2 zinc fingers
  JOURNAL   Mol Biol Cell 21 (1), 36-49 (2010)
   PUBMED   19864463
  REMARK    GeneRIF: NTRAP regulates retrograde neurotrophic signaling by
            controlling the formation of signaling endosomes.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001056388.1, XP_213230.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..902
                     /product="zinc finger protein 598"
                     /calculated_mol_wt=98723
     Region          26..>335
                     /region_name="COG5236"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227561"
     Region          <390..612
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     CDS             1..902
                     /gene="Zfp598"
                     /gene_synonym="Ntrap; Znf598"
                     /coded_by="NM_001105770.1:13..2721"
                     /db_xref="GeneID:287119"
                     /db_xref="RGD:1304900"
ORIGIN      
        1 maaagaegrr aaleavaape rgggscvlcc gdleatalgr cdhpvcyrcs tkmrvlceqr
       61 ycavcreelr qvvfgkklpa famipihqlq hekkydiyfa dgkvfalyrq llqhecprcp
      121 hlppfslfgd leqhmrkqhe lfccklclkh lkiftherkw ysrkdlarhr mqgdpddtsh
      181 rghplckfcd eryldndell khlrrdhyfc hfcdadgaqd yysdyaylre hfrekhflce
      241 egrcsteqft hafrteidlk ahktachsrs raearqnrqi dlqfsfaprh srrsegvvsg
      301 edyeevdryn rqgragrasg rgaqqnrrgs wreeedreva aairasvaaq qqeetqrved
      361 reegsrpkke eaavrvpees rghrrlpraq gegtgskets tngpvsqeaf satgpgpvva
      421 psntlpppnp klkdedfpsl cvstscctav tpssvglala ypapprgknt fqeedfpalv
      481 ssapkpssap sslisawnss cskkgnpptp gaqavvgssq psrkagkgsr ggrkggpapv
      541 dedsggltvq elrsvpttva vssllapvan qnsakvgkkk kmgsekpgat sspllppdht
      601 pkpsgaeqvp eaplskaevp vtivvnghse gsalawsipk eppglprplg plpcpipqed
      661 fpalggpcpp rmppppgfst vvllkgtppp pppppglvpp iskpppgfss flpsshstcv
      721 pstttitttt tnmkaprlap tagaylvpen frernlqliq sikdflqsde acfskfkshs
      781 gefrqgmisa aqyykscrdl lgenfqkifs ellallpdta kqqellsaht dfcsrerpps
      841 skskknkknv wqtstqqlgl dccvcptcqq vlahgdvssh qalhaarddd fpslqaiari
      901 it
//
LOCUS       NP_001258149             521 aa            linear   ROD 28-APR-2025
DEFINITION  brain-specific angiogenesis inhibitor 1-associated protein 2-like
            protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001258149 XP_001063469 XP_003754364
VERSION     NP_001258149.1
DBSOURCE    REFSEQ: accession NM_001271220.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Pykalainen,A., Boczkowska,M., Zhao,H., Saarikangas,J., Rebowski,G.,
            Jansen,M., Hakanen,J., Koskela,E.V., Peranen,J., Vihinen,H.,
            Jokitalo,E., Salminen,M., Ikonen,E., Dominguez,R. and
            Lappalainen,P.
  TITLE     Pinkbar is an epithelial-specific BAR domain protein that generates
            planar membrane structures
  JOURNAL   Nat Struct Mol Biol 18 (8), 902-907 (2011)
   PUBMED   21743456
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Veltman,D.M., Auciello,G., Spence,H.J., Machesky,L.M.,
            Rappoport,J.Z. and Insall,R.H.
  TITLE     Functional analysis of Dictyostelium IBARa reveals a conserved role
            of the I-BAR domain in endocytosis
  JOURNAL   Biochem J 436 (1), 45-52 (2011)
   PUBMED   21401524
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473950.2.
            
            On or before Sep 9, 2012 this sequence version replaced
            XP_003754364.1, XP_001063469.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132263
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..521
                     /product="brain-specific angiogenesis inhibitor
                     1-associated protein 2-like protein 2 isoform 2"
                     /note="brain-specific angiogenesis inhibitor 1-associated
                     protein 2-like protein 2; rCG60233-like; BAI1-associated
                     protein 2-like 2"
                     /calculated_mol_wt=58274
     Region          6..220
                     /region_name="I-BAR_IMD_BAIAP2L2"
                     /note="Inverse (I)-BAR, also known as the IRSp53/MIM
                     homology Domain (IMD), of Brain-specific Angiogenesis
                     Inhibitor 1-Associated Protein 2-Like 2; cd07644"
                     /db_xref="CDD:153328"
     Site            order(14..15,23,26..27,30,33..34,37,40..41,43..44,48,
                     50..51,54..55,57..58,61..62,71,75,82,85,174,177..178,
                     180..181,184..185,187..188,191..192,195,198..199,202,206,
                     209,216..217,219..220)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153328"
     Region          327..385
                     /region_name="SH3_BAIAP2L2"
                     /note="Src Homology 3 domain of Brain-specific
                     Angiogenesis Inhibitor 1-Associated Protein 2-Like 2;
                     cd11914"
                     /db_xref="CDD:212847"
     Site            order(332..333,335,342..343,355..356,361..363,365,
                     375..376,378..381)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212847"
     CDS             1..521
                     /gene="Baiap2l2"
                     /gene_synonym="RGD1308786"
                     /coded_by="NM_001271220.1:151..1716"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:685357"
                     /db_xref="RGD:1595091"
ORIGIN      
        1 mapemdqfyr stmaiyksim eqfnpalenl vylgnnylra fhalseaaev yfsaiqkige
       61 qalqsstsqi lgeilvqmsd tqrhlnsdle vvvqtfhgdl lqhmekntkl dmqfikdscq
      121 hyeieyrhra anlekcmsel wrmerkrdkn aremkesvnr lhaqmqafvs eskraaelee
      181 krryrflaek hlllsntflq flgrargmlq nrvllwkeqs easrspsrah spgllgpalg
      241 ppypsgrltp trldmpprpl geygsprsrh gsgsygpeps earsasqlep drrslprtps
      301 asslyasntq rsrsnsfger lggggarrvr alvshsegan htllrfsagd vvevlvpeaq
      361 ngwlygkleg ssasgwfpea yvkpleempm npmnpvapmn smapmspmne lpsrsyplrg
      421 shslddlldr pgnpaassdy wdsqsrsrtp srvpsrapsp appplpnrrs svgsmgaatd
      481 vkklmsweqn ppelfprgtn pfatvklrpt vtndrsapli r
//
LOCUS       NP_001178508             334 aa            linear   ROD 28-APR-2025
DEFINITION  ELMO domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178508 XP_002729969
VERSION     NP_001178508.1
DBSOURCE    REFSEQ: accession NM_001191579.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jul 17, 2010 this sequence version replaced XP_002729969.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1706814.1,
                                           SRR26360172.2461073.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..334
                     /product="ELMO domain-containing protein 1 isoform 1"
                     /note="ELMO domain-containing protein 1; ELMO/CED-12
                     domain containing 1"
                     /calculated_mol_wt=38941
     Region          119..303
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..334
                     /gene="Elmod1"
                     /gene_synonym="RGD1564186"
                     /coded_by="NM_001191579.2:373..1377"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315670"
                     /db_xref="RGD:1564186"
ORIGIN      
        1 mkhflrmliq vclyfyckfl wrcmkfvmrk ltgrcelqri cygtkpgasr tmkietslrd
       61 skskllqtsv svhpdaiekt iddimelkki npdinpqlgi slqacllqiv gyrnliadve
      121 klrrepydsd npqheemllk lweflkpntp lesriskqwc eigfqgddpk tdfrgmgllg
      181 lynlqyfaer datvaqqvlc dsvhpkcrdi tkeeiskfsk tewekkkmdk aigysfaivg
      241 initdlaynl lvsgalkthf yniapeaptl shfqqtfcyl mhefhkfwie edpmdimefn
      301 rvrekfrkri ikqlqnpdma lcphfaaseg linm
//
LOCUS       NP_001420154             707 aa            linear   ROD 28-APR-2025
DEFINITION  phospholipid transfer protein C2CD2L isoform 2 [Rattus norvegicus].
ACCESSION   NP_001420154 XP_006242980
VERSION     NP_001420154.1
DBSOURCE    REFSEQ: accession NM_001433225.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Lees,J.A., Messa,M., Sun,E.W., Wheeler,H., Torta,F., Wenk,M.R., De
            Camilli,P. and Reinisch,K.M.
  TITLE     Lipid transport by TMEM24 at ER-plasma membrane contacts regulates
            pulsatile insulin secretion
  JOURNAL   Science 355 (6326) (2017)
   PUBMED   28209843
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Pottekat,A., Becker,S., Spencer,K.R., Yates,J.R. 3rd, Manning,G.,
            Itkin-Ansari,P. and Balch,W.E.
  TITLE     Insulin biosynthetic interaction network component, TMEM24,
            facilitates insulin reserve pool release
  JOURNAL   Cell Rep 4 (5), 921-930 (2013)
   PUBMED   24012759
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Aug 7, 2024 this sequence version replaced XP_006242980.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643285.30818.1,
                                           SRR26643297.28060.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..707
                     /product="phospholipid transfer protein C2CD2L isoform 2"
                     /note="transmembrane protein 24; C2 domain-containing
                     protein 2-like; C2 calcium-dependent domain containing
                     2-like; phospholipid transfer protein C2CD2L"
                     /calculated_mol_wt=76001
     Region          84..260
                     /region_name="SMP_C2CD2L"
                     /note="synaptotagmin-like mitochondrial-lipid-binding
                     protein (SMP) domain found in C2 domain-containing protein
                     2-like (C2CD2L); cd21683"
                     /db_xref="CDD:439239"
     Site            order(98,101..102,106,110,130,135,156,161,163,165,185,187,
                     191,193,205,207,209,219,242,245..246,251,253..256)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:439239"
     Region          288..412
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     CDS             1..707
                     /gene="C2cd2l"
                     /gene_synonym="Tmem24"
                     /coded_by="NM_001433225.1:395..2518"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300666"
                     /db_xref="RGD:1310281"
ORIGIN      
        1 mdpdwgqrdv gwaallvlfa aslltvlgwl lqyarglwls ragggrdsrp asaaepggsl
       61 relgvwrsll rlratrssap eeagvrglla slfafksfre nwqrawvral neqacrdgss
      121 iqiafeeipq lpprasishv tcvdqsertm vlhcqlaaee vrfpisvtqq spaavsmety
      181 hvtltlpptq levsleeipd egllvswaft drpdlslkvl pksqtrerde eqpelstvee
      241 likdaivstq pammvnlrac sapgglvpse kpptmsqaqp siprptrlfl rqlrashlgs
      301 elggteelcc aaeldnpmqq kwtkptrags evewaedlal dlgpqsrelt lkvlrssscg
      361 daellgqatl pvgspskpls rrqvcpltpg pgkslspaai vtvelhyeqg sprnlgtpts
      421 stprpsitpt kkieldrtim pdgtivttvt tvqsrprvdg kladspsrsp skvevtekmt
      481 tvlsessgps nashsssres hlsngldpva etairqltep sgraakktpt krstliisgv
      541 skvpiaqdel alslgyaasl easmqddaga sggpssppsd psatspgpvd alssptsvqe
      601 adettrsdis erpsvddves etgstgalet rslkdhkvsf lrsgtklifr rrprqkeagl
      661 sqshddlsnt tatpsvrkka gsfsrrlikr fsfkskpkan gnpspql
//
LOCUS       NP_001416931            1786 aa            linear   ROD 28-APR-2025
DEFINITION  tuberin isoform b [Rattus norvegicus].
ACCESSION   NP_001416931 XP_063124507
VERSION     NP_001416931.1
DBSOURCE    REFSEQ: accession NM_001430002.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1786)
  AUTHORS   Kazami,M., Sakamoto,T., Suzuki,T., Inoue,H., Kato,H.,
            Kobayashi,K.I., Tadokoro,T. and Yamamoto,Y.
  TITLE     Ca2+/Calmodulin induces translocation of membrane-associated TSC2
            to the nucleus where it suppresses CYP24A1 expression
  JOURNAL   Biosci Biotechnol Biochem 87 (1), 45-53 (2022)
   PUBMED   36331254
  REMARK    GeneRIF: Ca2+/Calmodulin induces translocation of
            membrane-associated TSC2 to the nucleus where it suppresses CYP24A1
            expression.
REFERENCE   2  (residues 1 to 1786)
  AUTHORS   Joly,F., Jeckel,P., Kriebel,M., Raut,S., El Massioui,N.,
            Vaillend,C., Johnson,L.R., Volkmer,H. and Doyere,V.
  TITLE     Disruption of amygdala Tsc2 in adolescence leads to changed
            prelimbic cellular activity and generalized fear responses at
            adulthood in rats
  JOURNAL   Cereb Cortex 32 (20), 4619-4639 (2022)
   PUBMED   35149865
  REMARK    GeneRIF: Disruption of amygdala Tsc2 in adolescence leads to
            changed prelimbic cellular activity and generalized fear responses
            at adulthood in rats.
REFERENCE   3  (residues 1 to 1786)
  AUTHORS   Petrasek,T., Vojtechova,I., Klovrza,O., Tuckova,K., Vejmola,C.,
            Rak,J., Sulakova,A., Kaping,D., Bernhardt,N., de Vries,P.J.,
            Otahal,J. and Waltereit,R.
  TITLE     mTOR inhibitor improves autistic-like behaviors related to Tsc2
            haploinsufficiency but not following developmental status
            epilepticus
  JOURNAL   J Neurodev Disord 13 (1), 14 (2021)
   PUBMED   33863288
  REMARK    GeneRIF: mTOR inhibitor improves autistic-like behaviors related to
            Tsc2 haploinsufficiency but not following developmental status
            epilepticus.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1786)
  AUTHORS   Inoue,T., Kokubo,T., Daino,K., Yanagihara,H., Watanabe,F.,
            Tsuruoka,C., Amasaki,Y., Morioka,T., Homma-Takeda,S., Kobayashi,T.,
            Hino,O., Shimada,Y. and Kakinuma,S.
  TITLE     Interstitial chromosomal deletion of the tuberous sclerosis complex
            2 locus is a signature for radiation-associated renal tumors in
            Eker rats
  JOURNAL   Cancer Sci 111 (3), 840-848 (2020)
   PUBMED   31925975
  REMARK    GeneRIF: Reduced expression of Tsc2 was also observed in the
            majority of the LOH-negative carcinomas.
REFERENCE   5  (residues 1 to 1786)
  AUTHORS   Yan,Z., Grenert,J.P., Joseph,N.M., Ren,C., Chen,X., Shafizadeh,N.
            and Kakar,S.
  TITLE     Hepatic angiomyolipoma: mutation analysis and immunohistochemical
            pitfalls in diagnosis
  JOURNAL   Histopathology 73 (1), 101-108 (2018)
   PUBMED   29512829
REFERENCE   6  (residues 1 to 1786)
  AUTHORS   Mizuguchi,M., Kato,M., Yamanouchi,H., Ikeda,K. and Takashima,S.
  TITLE     Loss of tuberin from cerebral tissues with tuberous sclerosis and
            astrocytoma
  JOURNAL   Ann Neurol 40 (6), 941-944 (1996)
   PUBMED   9007104
REFERENCE   7  (residues 1 to 1786)
  AUTHORS   Wienecke,R., Maize,J.C. Jr., Shoarinejad,F., Vass,W.C., Reed,J.,
            Bonifacino,J.S., Resau,J.H., de Gunzburg,J., Yeung,R.S. and
            DeClue,J.E.
  TITLE     Co-localization of the TSC2 product tuberin with its target Rap1 in
            the Golgi apparatus
  JOURNAL   Oncogene 13 (5), 913-923 (1996)
   PUBMED   8806680
REFERENCE   8  (residues 1 to 1786)
  AUTHORS   Xiao,G.H., Jin,F. and Yeung,R.S.
  TITLE     Identification of tuberous sclerosis 2 messenger RNA splice
            variants that are conserved and differentially expressed in rat and
            human tissues
  JOURNAL   Cell Growth Differ 6 (9), 1185-1191 (1995)
   PUBMED   8519695
REFERENCE   9  (residues 1 to 1786)
  AUTHORS   Kobayashi,T., Nishizawa,M., Hirayama,Y., Kobayashi,E. and Hino,O.
  TITLE     cDNA structure, alternative splicing and exon-intron organization
            of the predisposing tuberous sclerosis (Tsc2) gene of the Eker rat
            model
  JOURNAL   Nucleic Acids Res 23 (14), 2608-2613 (1995)
   PUBMED   7651821
REFERENCE   10 (residues 1 to 1786)
  AUTHORS   Kobayashi,T., Hirayama,Y., Kobayashi,E., Kubo,Y. and Hino,O.
  TITLE     A germline insertion in the tuberous sclerosis (Tsc2) gene gives
            rise to the Eker rat model of dominantly inherited cancer
  JOURNAL   Nat Genet 9 (1), 70-74 (1995)
   PUBMED   7704028
  REMARK    Erratum:[Nat Genet 1995 Feb;9(2):218]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 2, 2024 this sequence version replaced XP_063124507.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.37218.1,
                                           SRR26643297.33273.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1786
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..1786
                     /product="tuberin isoform b"
                     /note="tuberin; tuberous sclerosis 2 homolog protein;
                     tuberous sclerosis 2 protein homolog; renal carcinoma"
                     /calculated_mol_wt=198561
     Region          54..419
                     /region_name="DUF3384"
                     /note="Domain of unknown function (DUF3384); pfam11864"
                     /db_xref="CDD:463376"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          555..903
                     /region_name="Tuberin"
                     /note="pfam03542"
                     /db_xref="CDD:460965"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1078..1136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1130
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1307..1336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1350..1369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1382..1469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1443
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1541..1727
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          1741..1770
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1743
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61037; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1777
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     CDS             1..1786
                     /gene="Tsc2"
                     /gene_synonym="Rc"
                     /coded_by="NM_001430002.1:113..5473"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:24855"
                     /db_xref="RGD:3908"
ORIGIN      
        1 makptskdsg lkekfkillg lgtsrpnprc aegkqtefii taeilrelsg ecglnnrirm
       61 igqicdvakt kkleehavea lwkavsdllq perppearha vlallkaivq gqgdrlgvlr
      121 alffkvikdy psnedlherl evfkaltdng rhityleeel aefvlqwmdv glssefllvl
      181 vnlvkfnscy ldeyiapmvh micllcirtv ssvdievslq vldavvcync lpaeslplfi
      241 itlcrtvnvk elcepcwklm rnllgthlgh saiynmcrim enrsymedap llrgavffvg
      301 malwgahrly slknsptsvl psfyeamtcp nevvsyeivl sitrlikkyr kelqavtwdi
      361 lldiierllq qlqnldspel rtivhdlltt veelcdqnef hgsqeryyel vesyadqrpe
      421 ssllnlityr aqsihpakdg wiqnlqllme rffrnecrsa vrikvldvls fvllinrqfy
      481 eeelinsvvi sqlshipedk dhqvrklatq llvdlaegch thhfnslldi iekvmarsls
      541 ppleleerdl avysasledv ktavlgllvi lqtklytlpa shatrvyetl ishiqlhykh
      601 gyslpiassi rlqafdflll lradslhrlg lpnkdgvvrf spyclcdcae ldrasekkas
      661 gplspptgpp spvptgpavr lghlpysllf rvllqclkqe tdwkvlklvl sklpeslryk
      721 vliftspcsv dqlssalcsm lsapktlerl rgtpegfsrt dlhlavvpvl talisyhnyl
      781 dktrqremvy cleqgliyrc asqcvvalai csvempdiii kalpvlvvkl thisatasma
      841 iplleflstl arlphlyrnf aaeqyasvfa islpytnpsk fnqyivclah hviamwfirc
      901 rlpfrkdfvp yitkglrsnv llsfddtpek dsfrarstsl nerpkslria rapkqglnns
      961 ppvkefkesc aaeafrcrsi svsehvvrsr iqtsltsasl gsadensmaq addnlknlhl
     1021 eltetcldmm aryvfsnfta vpkrspvgef llaggrtktw lvgnklvtvt tsvgtgtrsl
     1081 lgldsgdlqg gsasssdpgt hvrqtkeapa klesqagqqv srgardrvrs msgghglrvg
     1141 vldtsapytp ggpaslgaqa apaarpekpc agaqlpaaek anlaayvpll tqgwaeilvr
     1201 rptgntswlm slenplspfs sdinnmplqe lsnalmaaer fkehrdtaly kslsvpaagt
     1261 akpptlprsn tdsavvleeg spgeahvpve ppeledfeaa lgtdrhcqrp daysrsssas
     1321 sqeekshlee laaggipier aissegarpt vdlsfqpsqp lsksssspel qtlqdilgdl
     1381 gdktdigrls peakvrsqsg ildgeaatws apgeesritv ppegplpsss prspsglrpr
     1441 gytisdsaps rrgkrverdn fksrtaassa ekvpginpsf vflqlyhspf fgdesnkpil
     1501 lpnesfersv qlldqipsyd thkiavlyvg egqssselai lsnehgsyry tefltglgrl
     1561 ielkdcqpdk vylggldvcg edgqftycwh ddimqavfhi atlmptkdvd khrcdkkrhl
     1621 gndfvsiiyn dsgedfklgt ikgqfnfvhv iitpldykcn lltlqcrkdm eglvdtsvak
     1681 ivsdrnlsfv arqmalhanm asqvhhsrsn ptdiypskwi arlrhikrlr qrireevhys
     1741 npslplmhpp ahtkvpaqap teatptyetg qrkrlissvd dftefv
//
LOCUS       NP_001094178             534 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear respiratory factor 1 [Rattus norvegicus].
ACCESSION   NP_001094178 XP_001062755 XP_231566
VERSION     NP_001094178.1
DBSOURCE    REFSEQ: accession NM_001100708.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Niu,N., Li,H., Du,X., Wang,C., Li,J., Yang,J., Liu,C., Yang,S.,
            Zhu,Y. and Zhao,W.
  TITLE     Effects of NRF-1 and PGC-1alpha cooperation on HIF-1alpha and rat
            cardiomyocyte apoptosis under hypoxia
  JOURNAL   Gene 834, 146565 (2022)
   PUBMED   35569770
  REMARK    GeneRIF: Effects of NRF-1 and PGC-1alpha cooperation on HIF-1alpha
            and rat cardiomyocyte apoptosis under hypoxia.
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Pejon,T.M.M., Faria,V.S., Gobatto,C.A., Manchado-Gobatto,F.B.,
            Scariot,P.P.M., Cornachione,A.S. and Beck,W.R.
  TITLE     Effect of 12-wk Training in Ovariectomised Rats on PGC-1alpha,
            NRF-1 and Energy Substrates
  JOURNAL   Int J Sports Med 43 (7), 632-641 (2022)
   PUBMED   35180801
  REMARK    GeneRIF: Effect of 12-wk Training in Ovariectomised Rats on
            PGC-1alpha, NRF-1 and Energy Substrates.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Li,H., Niu,N., Yang,J., Dong,F., Zhang,T., Li,S. and Zhao,W.
  TITLE     Nuclear respiratory factor 1 protects H9C2 cells against
            hypoxia-induced apoptosis via the death receptor pathway and
            mitochondrial pathway
  JOURNAL   Cell Biol Int 45 (8), 1784-1796 (2021)
   PUBMED   33913583
  REMARK    GeneRIF: Nuclear respiratory factor 1 protects H9C2 cells against
            hypoxia-induced apoptosis via the death receptor pathway and
            mitochondrial pathway.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Li,Y., Yu,X.J., Xiao,T., Chi,H.L., Zhu,G.Q. and Kang,Y.M.
  TITLE     Nrf1 Knock-Down in the Hypothalamic Paraventricular Nucleus
            Alleviates Hypertension Through Intervention of Superoxide
            Production-Removal Balance and Mitochondrial Function
  JOURNAL   Cardiovasc Toxicol 21 (6), 472-489 (2021)
   PUBMED   33582931
  REMARK    GeneRIF: Nrf1 Knock-Down in the Hypothalamic Paraventricular
            Nucleus Alleviates Hypertension Through Intervention of Superoxide
            Production-Removal Balance and Mitochondrial Function.
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Wang,X., Huang,L., Jiang,S., Cheng,K., Wang,D., Luo,Q., Wu,X. and
            Zhu,L.
  TITLE     Testosterone attenuates pulmonary epithelial inflammation in male
            rats of COPD model through preventing NRF1-derived NF-kappaB
            signaling
  JOURNAL   J Mol Cell Biol 13 (2), 128-140 (2021)
   PUBMED   33475136
  REMARK    GeneRIF: Testosterone attenuates pulmonary epithelial inflammation
            in male rats of COPD model through preventing NRF1-derived
            NF-kappaB signaling.
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Suliman,H.B., Carraway,M.S., Welty-Wolf,K.E., Whorton,A.R. and
            Piantadosi,C.A.
  TITLE     Lipopolysaccharide stimulates mitochondrial biogenesis via
            activation of nuclear respiratory factor-1
  JOURNAL   J Biol Chem 278 (42), 41510-41518 (2003)
   PUBMED   12902348
  REMARK    GeneRIF: oxidative stress stimulates mitochondrial biogenesis in
            part via nuclear respiratory factor 1 (NRF-1) activation and
            corresponding to recovery events after LPS-induced liver damage.
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Maraia,R.J. and Intine,R.V.
  TITLE     Recognition of nascent RNA by the human La antigen: conserved and
            divergent features of structure and function
  JOURNAL   Mol Cell Biol 21 (2), 367-379 (2001)
   PUBMED   11134326
  REMARK    Review article
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Xia,Y., Buja,L.M. and McMillin,J.B.
  TITLE     Activation of the cytochrome c gene by electrical stimulation in
            neonatal rat cardiac myocytes. Role of NRF-1 and c-Jun
  JOURNAL   J Biol Chem 273 (20), 12593-12598 (1998)
   PUBMED   9575220
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Koyama,H., Kurokawa,T., Nonami,T., Nakao,A., Sugiyama,S.,
            Murakami,T., Shimomura,Y. and Takagi,H.
  TITLE     Increases in the mitochondrial DNA replication and transcription in
            the remnant liver of rats
  JOURNAL   Biochem Biophys Res Commun 243 (3), 858-861 (1998)
   PUBMED   9501001
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Gopalakrishnan,L. and Scarpulla,R.C.
  TITLE     Structure, expression, and chromosomal assignment of the human gene
            encoding nuclear respiratory factor 1
  JOURNAL   J Biol Chem 270 (30), 18019-18025 (1995)
   PUBMED   7629110
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161956.1.
            
            On or before Sep 7, 2008 this sequence version replaced
            XP_231566.4, XP_001062755.1.
            
            Summary: This gene encodes a protein that homodimerizes and
            functions as a transcription factor which activates the expression
            of some key metabolic genes regulating cellular growth and nuclear
            genes required for respiration, heme biosynthesis, and
            mitochondrial DNA transcription and replication. Confusion has
            occurred in bibliographic databases for genes in the 'nuclear
            respiratory factor' and 'nuclear factor (erythroid-derived 2)-like'
            families due to a shared symbol or alias of Nrf1. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161956.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132275
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..534
                     /product="nuclear respiratory factor 1"
                     /note="NRF-1; alpha-pal; alpha palindromic-binding
                     protein"
                     /calculated_mol_wt=57149
     Region          87..283
                     /region_name="Nrf1_DNA-bind"
                     /note="NLS-binding and DNA-binding and dimerization
                     domains of Nrf1; pfam10491"
                     /db_xref="CDD:463112"
     Region          450..525
                     /region_name="TGS_YchF_OLA1"
                     /note="TGS (ThrRS, GTPase and SpoT) domain found in the
                     YchF/OLA1 family proteins; cd04867"
                     /db_xref="CDD:340516"
     CDS             1..534
                     /gene="Nrf1"
                     /gene_synonym="Nfe2l1_retired"
                     /coded_by="NM_001100708.1:246..1850"
                     /db_xref="GeneID:312195"
                     /db_xref="RGD:1304603"
ORIGIN      
        1 meehgvtqte hmatieahav aqqvqqvhva tytehsmlsa dedspssped tsyddsdiln
       61 staadevtah laaagpvgma aaaavatgkk rkrphvfesn psirkrqqtr llrklratld
      121 eyttrvgqqa ivlcispskp npvfkvfgaa plenvvrkyk smiledlesa laehapapqe
      181 vnselpplti dgipvsvdkm tqaqlrafip emlkystgrg kpgwgkesck piwwpedipw
      241 anvrsdvrte eqkqrvswtq alrtivkncy kqhgredlly afedqqtqtq attthsiahl
      301 vpsqtvvqtf snpdgtvsli qvgtgatvat ladaselptt vtvaqvnysa vadgeveqnw
      361 atlqggemti qttqaseatq avaslaeaav aasqemqqga tvtmalnsea aahavatlae
      421 atlqgggqiv lsgetaaavg altgvqdang pdgvhawtis kavtapqaag kihtdfgkgf
      481 imaevmkded lkeessenaa kaagkykqpg rayvvedgdi iffkfnspqq lkrk
//
LOCUS       NP_001257584             839 aa            linear   ROD 28-APR-2025
DEFINITION  NT-3 growth factor receptor isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001257584
VERSION     NP_001257584.1
DBSOURCE    REFSEQ: accession NM_001270655.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Chen,Z., Huang,Z., Luo,Y., Zou,Q., Bai,L., Tang,G., Wang,X.,
            Cao,G., Huang,M., Xiang,J. and Yu,H.
  TITLE     Genome-wide analysis identifies critical DNA methylations within
            NTRKs genes in colorectal cancer
  JOURNAL   J Transl Med 19 (1), 73 (2021)
   PUBMED   33593392
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Tan,W., Dong,L., Shi,X., Tang,Q. and Jiang,D.
  TITLE     P75NTR Exacerbates SCI-induced Mitochondrial Damage and Neuronal
            Apoptosis Depending on NTRK3
  JOURNAL   Curr Neurovasc Res 18 (5), 552-564 (2021)
   PUBMED   34970951
  REMARK    GeneRIF: P75NTR Exacerbates SCI-induced Mitochondrial Damage and
            Neuronal Apoptosis Depending on NTRK3.
REFERENCE   3  (residues 1 to 839)
  AUTHORS   Qiao,X., Yin,F., Ji,Y., Li,Y., Yan,P. and Lai,J.
  TITLE     5-Aza-2'-deoxycytidine in the medial prefrontal cortex regulates
            alcohol-related behavior and Ntf3-TrkC expression in rats
  JOURNAL   PLoS One 12 (6), e0179469 (2017)
   PUBMED   28614398
  REMARK    GeneRIF: Data show that 5-Aza-dc reversed the alcohol-induced
            downregulation of neurotrophin-3 (Ntf3), correspondingly the
            expression of its receptor-neurotrophic receptor tyrosine kinase 3
            (TrkC) was reduced.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 839)
  AUTHORS   Behrouz Sharif,S., Hashemzadeh,S., Mousavi Ardehaie,R.,
            Eftekharsadat,A., Ghojazadeh,M., Mehrtash,A.H., Estiar,M.A.,
            Teimoori-Toolabi,L. and Sakhinia,E.
  TITLE     Detection of aberrant methylated SEPT9 and NTRK3 genes in sporadic
            colorectal cancer patients as a potential diagnostic biomarker
  JOURNAL   Oncol Lett 12 (6), 5335-5343 (2016)
   PUBMED   28105243
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Dmitrieva,V.G., Stavchansky,V.V., Povarova,O.V., Skvortsova,V.I.,
            Limborska,S.A. and Dergunova,L.V.
  TITLE     [Effects of ischemia on the expression of neurotrophins and their
            receptors in rat brain structures outside the lesion site,
            including on the opposite hemisphere]
  JOURNAL   Mol Biol (Mosk) 50 (5), 775-784 (2016)
   PUBMED   27830679
  REMARK    GeneRIF: It has been shown that ischemia influenced the expression
            of neurotrophins (Bdnf, Ngf, Nt-3) and their receptors (TrkB, TrkA,
            TrkC, p75) in brain structures outside the lesion focus, including
            the contralateral hemisphere.
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Qian,X., Riccio,A., Zhang,Y. and Ginty,D.D.
  TITLE     Identification and characterization of novel substrates of Trk
            receptors in developing neurons
  JOURNAL   Neuron 21 (5), 1017-1029 (1998)
   PUBMED   9856458
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Fernyhough,P., Diemel,L.T. and Tomlinson,D.R.
  TITLE     Target tissue production and axonal transport of neurotrophin-3 are
            reduced in streptozotocin-diabetic rats
  JOURNAL   Diabetologia 41 (3), 300-306 (1998)
   PUBMED   9541170
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Tsoulfas,P., Soppet,D., Escandon,E., Tessarollo,L.,
            Mendoza-Ramirez,J.L., Rosenthal,A., Nikolics,K. and Parada,L.F.
  TITLE     The rat trkC locus encodes multiple neurogenic receptors that
            exhibit differential response to neurotrophin-3 in PC12 cells
  JOURNAL   Neuron 10 (5), 975-990 (1993)
   PUBMED   8494648
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Valenzuela,D.M., Maisonpierre,P.C., Glass,D.J., Rojas,E., Nunez,L.,
            Kong,Y., Gies,D.R., Stitt,T.N., Ip,N.Y. and Yancopoulos,G.D.
  TITLE     Alternative forms of rat TrkC with different functional
            capabilities
  JOURNAL   Neuron 10 (5), 963-974 (1993)
   PUBMED   8494647
REFERENCE   10 (residues 1 to 839)
  AUTHORS   Merlio,J.P., Ernfors,P., Jaber,M. and Persson,H.
  TITLE     Molecular cloning of rat trkC and distribution of cells expressing
            messenger RNAs for members of the trk family in the rat central
            nervous system
  JOURNAL   Neuroscience 51 (3), 513-532 (1992)
   PUBMED   1488112
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L03813.1 and L14446.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L14446.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..839
                     /product="NT-3 growth factor receptor isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="NT-3 growth factor receptor; trk-C; GP145-TrkC;
                     trkC tyrosine kinase; neurotrophic tyrosine kinase,
                     receptor, type 3; neural receptor protein-tyrosine kinase
                     (trkC)"
                     /calculated_mol_wt=90928
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3477
     Region          103..160
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          105..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          152..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          163..208
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Region          214..299
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          227..231
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          240..244
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          266..270
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          281..286
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..396
                     /region_name="IgI_TrKABC_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptors
                     TrkA, TrkB, and TrkC; member of the I-set of Ig
                     superfamily (IgSF) domains; cd04971"
                     /db_xref="CDD:409360"
     Region          305..311
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409360"
     Region          313..316
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409360"
     Region          319..327
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409360"
     Site            328
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          330..337
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409360"
     Region          340..343
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409360"
     Region          348..354
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409360"
     Site            order(353,366..367,370)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          358..366
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409360"
     Region          374..382
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409360"
     Region          385..393
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409360"
     Region          532..832
                     /region_name="PTKc_TrkC"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tropomyosin Related Kinase C; cd05094"
                     /db_xref="CDD:270676"
     Site            order(544..548,552,570,572,617..620,623..624,679,683..684,
                     686,697,729..733,742,776)
                     /site_type="active"
                     /db_xref="CDD:270676"
     Site            order(544..545,547..548,552,570,572,617..620,623..624,
                     683..684,686,697)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270676"
     Site            order(679,683,729..733,742,776)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270676"
     Site            order(696..711,726..735)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270676"
     CDS             1..839
                     /gene="Ntrk3"
                     /gene_synonym="trkC"
                     /coded_by="NM_001270655.1:52..2571"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:29613"
                     /db_xref="RGD:3214"
ORIGIN      
        1 mdvslcpakc sfwrifllgs vwldyvgsvl acpancvcsk teincrrpdd gnlfpllegq
       61 dsgnsngnas initdisrni tsihienwrg lhtlnavdme lytglqklti knsglrniqp
      121 rafaknphlr yinlssnrlt tlswqlfqtl slrelrleqn ffncscdirw mqlwqeqgea
      181 rldsqslyci sadgsqlplf rmnisqcdlp eisvshvnlt vregdnavit cngsgsplpd
      241 vdwivtglqs inthqtnlnw tnvhainltl vnvtsedngf tltciaenvv gmsnasvalt
      301 vyypprvvsl vepevrlehc iefvvrgnpt ptlhwlyngq plreskiihm dyyqegevse
      361 gcllfnkpth ynngnytlia knalgtanqt inghflkepf pestdffdfe sdasptppit
      421 vthkpeedtf gvsiavglaa facvllvvlf iminkygrrs kfgmkgpvav isgeedsasp
      481 lhhinhgitt pssldagpdt vvigmtripv ienpqyfrqg hnchkpdtyv qhikrrdivl
      541 krelgegafg kvflaecynl sptkdkmlva vkalkdptla arkdfqreae lltnlqhehi
      601 vkfygvcgdg dplimvfeym khgdlnkflr ahgpdamilv dgqprqakge lglsqmlhia
      661 sqiasgmvyl asqhfvhrdl atrnclvgan llvkigdfgm srdvystdyy rlfnpsgndf
      721 ciwcevgght mlpirwmppe simyrkftte sdvwsfgvil weiftygkqp wfqlsntevi
      781 ecitqgrvle rprvcpkevy dvmlgcwqre pqqrlnikei ykilhalgka tpiyldilg
//
LOCUS       NP_036812               1809 aa            linear   ROD 28-APR-2025
DEFINITION  tuberin isoform a [Rattus norvegicus].
ACCESSION   NP_036812
VERSION     NP_036812.3
DBSOURCE    REFSEQ: accession NM_012680.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1809)
  AUTHORS   Kazami,M., Sakamoto,T., Suzuki,T., Inoue,H., Kato,H.,
            Kobayashi,K.I., Tadokoro,T. and Yamamoto,Y.
  TITLE     Ca2+/Calmodulin induces translocation of membrane-associated TSC2
            to the nucleus where it suppresses CYP24A1 expression
  JOURNAL   Biosci Biotechnol Biochem 87 (1), 45-53 (2022)
   PUBMED   36331254
  REMARK    GeneRIF: Ca2+/Calmodulin induces translocation of
            membrane-associated TSC2 to the nucleus where it suppresses CYP24A1
            expression.
REFERENCE   2  (residues 1 to 1809)
  AUTHORS   Joly,F., Jeckel,P., Kriebel,M., Raut,S., El Massioui,N.,
            Vaillend,C., Johnson,L.R., Volkmer,H. and Doyere,V.
  TITLE     Disruption of amygdala Tsc2 in adolescence leads to changed
            prelimbic cellular activity and generalized fear responses at
            adulthood in rats
  JOURNAL   Cereb Cortex 32 (20), 4619-4639 (2022)
   PUBMED   35149865
  REMARK    GeneRIF: Disruption of amygdala Tsc2 in adolescence leads to
            changed prelimbic cellular activity and generalized fear responses
            at adulthood in rats.
REFERENCE   3  (residues 1 to 1809)
  AUTHORS   Petrasek,T., Vojtechova,I., Klovrza,O., Tuckova,K., Vejmola,C.,
            Rak,J., Sulakova,A., Kaping,D., Bernhardt,N., de Vries,P.J.,
            Otahal,J. and Waltereit,R.
  TITLE     mTOR inhibitor improves autistic-like behaviors related to Tsc2
            haploinsufficiency but not following developmental status
            epilepticus
  JOURNAL   J Neurodev Disord 13 (1), 14 (2021)
   PUBMED   33863288
  REMARK    GeneRIF: mTOR inhibitor improves autistic-like behaviors related to
            Tsc2 haploinsufficiency but not following developmental status
            epilepticus.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1809)
  AUTHORS   Inoue,T., Kokubo,T., Daino,K., Yanagihara,H., Watanabe,F.,
            Tsuruoka,C., Amasaki,Y., Morioka,T., Homma-Takeda,S., Kobayashi,T.,
            Hino,O., Shimada,Y. and Kakinuma,S.
  TITLE     Interstitial chromosomal deletion of the tuberous sclerosis complex
            2 locus is a signature for radiation-associated renal tumors in
            Eker rats
  JOURNAL   Cancer Sci 111 (3), 840-848 (2020)
   PUBMED   31925975
  REMARK    GeneRIF: Reduced expression of Tsc2 was also observed in the
            majority of the LOH-negative carcinomas.
REFERENCE   5  (residues 1 to 1809)
  AUTHORS   Yan,Z., Grenert,J.P., Joseph,N.M., Ren,C., Chen,X., Shafizadeh,N.
            and Kakar,S.
  TITLE     Hepatic angiomyolipoma: mutation analysis and immunohistochemical
            pitfalls in diagnosis
  JOURNAL   Histopathology 73 (1), 101-108 (2018)
   PUBMED   29512829
REFERENCE   6  (residues 1 to 1809)
  AUTHORS   Mizuguchi,M., Kato,M., Yamanouchi,H., Ikeda,K. and Takashima,S.
  TITLE     Loss of tuberin from cerebral tissues with tuberous sclerosis and
            astrocytoma
  JOURNAL   Ann Neurol 40 (6), 941-944 (1996)
   PUBMED   9007104
REFERENCE   7  (residues 1 to 1809)
  AUTHORS   Wienecke,R., Maize,J.C. Jr., Shoarinejad,F., Vass,W.C., Reed,J.,
            Bonifacino,J.S., Resau,J.H., de Gunzburg,J., Yeung,R.S. and
            DeClue,J.E.
  TITLE     Co-localization of the TSC2 product tuberin with its target Rap1 in
            the Golgi apparatus
  JOURNAL   Oncogene 13 (5), 913-923 (1996)
   PUBMED   8806680
REFERENCE   8  (residues 1 to 1809)
  AUTHORS   Xiao,G.H., Jin,F. and Yeung,R.S.
  TITLE     Identification of tuberous sclerosis 2 messenger RNA splice
            variants that are conserved and differentially expressed in rat and
            human tissues
  JOURNAL   Cell Growth Differ 6 (9), 1185-1191 (1995)
   PUBMED   8519695
REFERENCE   9  (residues 1 to 1809)
  AUTHORS   Kobayashi,T., Nishizawa,M., Hirayama,Y., Kobayashi,E. and Hino,O.
  TITLE     cDNA structure, alternative splicing and exon-intron organization
            of the predisposing tuberous sclerosis (Tsc2) gene of the Eker rat
            model
  JOURNAL   Nucleic Acids Res 23 (14), 2608-2613 (1995)
   PUBMED   7651821
REFERENCE   10 (residues 1 to 1809)
  AUTHORS   Kobayashi,T., Hirayama,Y., Kobayashi,E., Kubo,Y. and Hino,O.
  TITLE     A germline insertion in the tuberous sclerosis (Tsc2) gene gives
            rise to the Eker rat model of dominantly inherited cancer
  JOURNAL   Nat Genet 9 (1), 70-74 (1995)
   PUBMED   7704028
  REMARK    Erratum:[Nat Genet 1995 Feb;9(2):218]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 2, 2024 this sequence version replaced NP_036812.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U24150.1, SRR26643296.25478.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1809
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..1809
                     /product="tuberin isoform a"
                     /note="tuberin; tuberous sclerosis 2 homolog protein;
                     tuberous sclerosis 2 protein homolog; renal carcinoma"
                     /calculated_mol_wt=201082
     Region          54..419
                     /region_name="DUF3384"
                     /note="Domain of unknown function (DUF3384); pfam11864"
                     /db_xref="CDD:463376"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          555..903
                     /region_name="Tuberin"
                     /note="pfam03542"
                     /db_xref="CDD:460965"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1078..1136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1130
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1330..1359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1373..1392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1405..1492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1466
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:12172553; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Region          1564..1750
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          1764..1793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49816.1)"
     Site            1766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61037; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1800
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     Site            1801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49815; propagated from
                     UniProtKB/Swiss-Prot (P49816.1)"
     CDS             1..1809
                     /gene="Tsc2"
                     /gene_synonym="Rc"
                     /coded_by="NM_012680.4:113..5542"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:24855"
                     /db_xref="RGD:3908"
ORIGIN      
        1 makptskdsg lkekfkillg lgtsrpnprc aegkqtefii taeilrelsg ecglnnrirm
       61 igqicdvakt kkleehavea lwkavsdllq perppearha vlallkaivq gqgdrlgvlr
      121 alffkvikdy psnedlherl evfkaltdng rhityleeel aefvlqwmdv glssefllvl
      181 vnlvkfnscy ldeyiapmvh micllcirtv ssvdievslq vldavvcync lpaeslplfi
      241 itlcrtvnvk elcepcwklm rnllgthlgh saiynmcrim enrsymedap llrgavffvg
      301 malwgahrly slknsptsvl psfyeamtcp nevvsyeivl sitrlikkyr kelqavtwdi
      361 lldiierllq qlqnldspel rtivhdlltt veelcdqnef hgsqeryyel vesyadqrpe
      421 ssllnlityr aqsihpakdg wiqnlqllme rffrnecrsa vrikvldvls fvllinrqfy
      481 eeelinsvvi sqlshipedk dhqvrklatq llvdlaegch thhfnslldi iekvmarsls
      541 ppleleerdl avysasledv ktavlgllvi lqtklytlpa shatrvyetl ishiqlhykh
      601 gyslpiassi rlqafdflll lradslhrlg lpnkdgvvrf spyclcdcae ldrasekkas
      661 gplspptgpp spvptgpavr lghlpysllf rvllqclkqe tdwkvlklvl sklpeslryk
      721 vliftspcsv dqlssalcsm lsapktlerl rgtpegfsrt dlhlavvpvl talisyhnyl
      781 dktrqremvy cleqgliyrc asqcvvalai csvempdiii kalpvlvvkl thisatasma
      841 iplleflstl arlphlyrnf aaeqyasvfa islpytnpsk fnqyivclah hviamwfirc
      901 rlpfrkdfvp yitkglrsnv llsfddtpek dsfrarstsl nerpkslria rapkqglnns
      961 ppvkefkesc aaeafrcrsi svsehvvrsr iqtsltsasl gsadensmaq addnlknlhl
     1021 eltetcldmm aryvfsnfta vpkrspvgef llaggrtktw lvgnklvtvt tsvgtgtrsl
     1081 lgldsgdlqg gsasssdpgt hvrqtkeapa klesqagqqv srgardrvrs msgghglrvg
     1141 vldtsapytp ggpaslgaqa apaarpekpc agaqlpaaek anlaayvpll tqgwaeilvr
     1201 rptgntswlm slenplspfs sdinnmplqe lsnalmaaer fkehrdtaly kslsvpaagt
     1261 akpptlprsn tvasfsslyq pscqgqlhrs vswadsavvl eegspgeahv pveppeledf
     1321 eaalgtdrhc qrpdaysrss sassqeeksh leelaaggip ieraissega rptvdlsfqp
     1381 sqplskssss pelqtlqdil gdlgdktdig rlspeakvrs qsgildgeaa twsapgeesr
     1441 itvppegplp sssprspsgl rprgytisds apsrrgkrve rdnfksrtaa ssaekvpgin
     1501 psfvflqlyh spffgdesnk pillpnesfe rsvqlldqip sydthkiavl yvgegqssse
     1561 lailsnehgs yrytefltgl grlielkdcq pdkvylggld vcgedgqfty cwhddimqav
     1621 fhiatlmptk dvdkhrcdkk rhlgndfvsi iyndsgedfk lgtikgqfnf vhviitpldy
     1681 kcnlltlqcr kdmeglvdts vakivsdrnl sfvarqmalh anmasqvhhs rsnptdiyps
     1741 kwiarlrhik rlrqrireev hysnpslplm hppahtkvpa qapteatpty etgqrkrlis
     1801 svddftefv
//
LOCUS       NP_037051               1091 aa            linear   ROD 28-APR-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-1 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_037051
VERSION     NP_037051.2
DBSOURCE    REFSEQ: accession NM_012919.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Lu,Y., Wang,J., Li,L. and Zhang,X.
  TITLE     The role of voltage-gated calcium channel alpha2delta-1 in the
            occurrence and development in myofascial orofacial pain
  JOURNAL   BMC Oral Health 24 (1), 552 (2024)
   PUBMED   38735923
  REMARK    GeneRIF: The role of voltage-gated calcium channel alpha2delta-1 in
            the occurrence and development in myofascial orofacial pain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Al Katat,A., Zhao,J., Calderone,A. and Parent,L.
  TITLE     Sympathetic Stimulation Upregulates the Ca2+ Channel Subunit,
            CaValpha2delta1, via the beta1 and ERK 1/2 Pathway in Neonatal
            Ventricular Cardiomyocytes
  JOURNAL   Cells 11 (2), 188 (2022)
   PUBMED   35053304
  REMARK    GeneRIF: Sympathetic Stimulation Upregulates the Ca(2+) Channel
            Subunit, CaValpha2delta1, via the beta1 and ERK 1/2 Pathway in
            Neonatal Ventricular Cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Fu,M., Liu,F., Zhang,Y.Y., Lin,J., Huang,C.L., Li,Y.L., Wang,H.,
            Zhou,C., Li,C.J. and Shen,J.F.
  TITLE     The alpha2delta-1-NMDAR1 interaction in the trigeminal ganglion
            contributes to orofacial ectopic pain following inferior alveolar
            nerve injury
  JOURNAL   Brain Res Bull 171, 162-171 (2021)
   PUBMED   33811955
  REMARK    GeneRIF: The alpha2delta-1-NMDAR1 interaction in the trigeminal
            ganglion contributes to orofacial ectopic pain following inferior
            alveolar nerve injury.
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Meyer,J.O. and Dolphin,A.C.
  TITLE     Rab11-dependent recycling of calcium channels is mediated by
            auxiliary subunit alpha2delta-1 but not alpha2delta-3
  JOURNAL   Sci Rep 11 (1), 10256 (2021)
   PUBMED   33986433
  REMARK    GeneRIF: Rab11-dependent recycling of calcium channels is mediated
            by auxiliary subunit alpha2delta-1 but not alpha2delta-3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Martinez San Segundo,P., Terni,B., Burgueno,J., Monroy,X.,
            Dordal,A., Merlos,M. and Llobet,A.
  TITLE     Outside-in regulation of the readily releasable pool of synaptic
            vesicles by alpha2delta-1
  JOURNAL   FASEB J 34 (1), 1362-1377 (2020)
   PUBMED   31914622
  REMARK    GeneRIF: These observations prompt to consider alpha2delta-1 as an
            outside-in signaling platform that binds exogenous and endogenous
            cues for regulating the coupling of voltage-gated calcium channels
            to synaptic vesicles.
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Chu,P.J. and Best,P.M.
  TITLE     Molecular cloning of calcium channel alpha(2)delta-subunits from
            rat atria and the differential regulation of their expression by
            IGF-1
  JOURNAL   J Mol Cell Cardiol 35 (2), 207-215 (2003)
   PUBMED   12606261
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Yamada,Y., Nagashima,M., Tsutsuura,M., Kobayashi,T., Seki,S.,
            Makita,N., Horio,Y. and Tohse,N.
  TITLE     Cloning of a functional splice variant of L-type calcium channel
            beta 2 subunit from rat heart
  JOURNAL   J Biol Chem 276 (50), 47163-47170 (2001)
   PUBMED   11604404
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Bell,D.C., Butcher,A.J., Berrow,N.S., Page,K.M., Brust,P.F.,
            Nesterova,A., Stauderman,K.A., Seabrook,G.R., Nurnberg,B. and
            Dolphin,A.C.
  TITLE     Biophysical properties, pharmacology, and modulation of human,
            neuronal L-type (alpha(1D), Ca(V)1.3) voltage-dependent calcium
            currents
  JOURNAL   J Neurophysiol 85 (2), 816-827 (2001)
   PUBMED   11160515
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Kim,H.L., Kim,H., Lee,P., King,R.G. and Chin,H.
  TITLE     Rat brain expresses an alternatively spliced form of the
            dihydropyridine-sensitive L-type calcium channel alpha 2 subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (8), 3251-3255 (1992)
   PUBMED   1314383
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Jun 15;89(12):5699]
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF286488.1.
            
            On Jun 9, 2003 this sequence version replaced NP_037051.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF286488.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..1091
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-1 isoform 1 precursor"
                     /note="voltage-dependent calcium channel subunit
                     alpha-2/delta-1; voltage-gated calcium channel subunit
                     alpha-2/delta-1; Calcium channel subunit alpha 2 delta
                     (dihydropyridine - sensitive L-type); calcium channel,
                     voltage-dependent, alpha2/delta subunit 1"
                     /calculated_mol_wt=120963
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2523
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Region          104..223
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Region          239..417
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(259,261,263,331,363)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          259..263
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P54290.1)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Region          509..606
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Region          632..1060
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            876
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            973
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P54290.1)"
     Site            1062..1082
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54290.1)"
     CDS             1..1091
                     /gene="Cacna2d1"
                     /gene_synonym="Cacna2; CCHLA2; DHSCCA"
                     /coded_by="NM_012919.3:286..3561"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25399"
                     /db_xref="RGD:2247"
ORIGIN      
        1 maagcllalt ltlfqswlig psseepfpsp vtikswvdkm qedlvtlakt asgvtqladi
       61 yekyqdlytv epnnarqlve iaardiekll snrskalvrl ameaekvqaa hqwredfasn
      121 evvyynakdd ldperneses gsqrikpvfi edanfgrqis yqhaavhipt diyegstivl
      181 nelnwtsald evfkrnrded ptllwqvfgs atglaryypa spwvdnsrtp nkidlydvrr
      241 rpwyiqgaas pkdmlilvdv sgsvsgltlk lirtsvseml etlsdddfvn vasfnsnaqd
      301 vscfqhlvqa nvrnkkvlkd avnnitakgi tdykkgfsfa feqllnynvs rancnkiiml
      361 ftdggeeraq eifakynkdk kvrvftfsvg qhnydrgpiq wmacenkgyy yeipsigair
      421 intqeyldvl grpmvlagdk akqvqwtnvy ldalelglvi tgtlpvfnvt gqsenktnlk
      481 nqlilgvmgv dvsledikrl tprftlcpng yyfaidpngy vllhpnlqpk npksqepvtl
      541 dfldaelend ikveirnkmi dgesgektfr tlvksqdery idkgnrtytw tpvngtdysl
      601 alvlptysfy yikakieeti tqarskkgkm kdsetlkpdn feesgytfia preycndlkp
      661 sdnnteflln fnefidrktp nnpscntdli nrilldagft nelvqnywsk qknikgvkar
      721 fvvtdggitr vypkeagenw qenpetyeds fykrsldndn yvftapyfnk sgpgayesgi
      781 mvskavelyi qgkllkpavv gikidvnswi enftktsird pcagpvcdck rnsdvmdcvi
      841 lddggfllma nhddytnqig rffgeidpsm mrhlvnisly afnksydyqs vcdpgaapkq
      901 gaghrsayvp sitdilqigw wataaawsil qqlllsltfp rlleavemee ddftaslskq
      961 sciteqtqyf fkndtksfsg lldcgncsri fhveklmntn lvfimveskg tcpcdtrllm
     1021 qaeqtsdgpd pcdmvkqpry rkgpdvcfdn nvledytdcg gvsglnpslw sifglqfill
     1081 wlvsgsrhyl w
//
LOCUS       NP_036804                497 aa            linear   ROD 28-APR-2025
DEFINITION  thyroid hormone receptor beta isoform 1 [Rattus norvegicus].
ACCESSION   NP_036804
VERSION     NP_036804.2
DBSOURCE    REFSEQ: accession NM_012672.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Mukherjee,S., Dasgupta,S., Adhikari,U. and Panja,S.S.
  TITLE     Molecular modeling and molecular dynamics simulation studies on
            thyroid hormone receptor from Rattus norvegicus: role of conserved
            water molecules
  JOURNAL   J Mol Model 27 (5), 126 (2021)
   PUBMED   33834296
  REMARK    GeneRIF: Molecular modeling and molecular dynamics simulation
            studies on thyroid hormone receptor from Rattus norvegicus: role of
            conserved water molecules.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Fernandez,M., Pannella,M., Baldassarro,V.A., Flagelli,A.,
            Alastra,G., Giardino,L. and Calza,L.
  TITLE     Thyroid Hormone Signaling in Embryonic Stem Cells: Crosstalk with
            the Retinoic Acid Pathway
  JOURNAL   Int J Mol Sci 21 (23), 8945 (2020)
   PUBMED   33255695
  REMARK    GeneRIF: Thyroid Hormone Signaling in Embryonic Stem Cells:
            Crosstalk with the Retinoic Acid Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Leach,P.T., Kenney,J.W., Connor,D.A. and Gould,T.J.
  TITLE     Thyroid receptor beta involvement in the effects of acute nicotine
            on hippocampus-dependent memory
  JOURNAL   Neuropharmacology 93, 155-163 (2015)
   PUBMED   25666034
  REMARK    GeneRIF: This study demonstrated that Thyroid receptor beta
            involvement in the effects of acute nicotine on
            hippocampus-dependent memory
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Frau,C., Loi,R., Petrelli,A., Perra,A., Menegon,S., Kowalik,M.A.,
            Pinna,S., Leoni,V.P., Fornari,F., Gramantieri,L.,
            Ledda-Columbano,G.M., Giordano,S. and Columbano,A.
  TITLE     Local hypothyroidism favors the progression of preneoplastic
            lesions to hepatocellular carcinoma in rats
  JOURNAL   Hepatology 61 (1), 249-259 (2015)
   PUBMED   25156012
  REMARK    GeneRIF: down-regulated in hepatocellular carcinoma
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Sharma,P., Thakran,S., Deng,X., Elam,M.B. and Park,E.A.
  TITLE     Nuclear corepressors mediate the repression of phospholipase A2
            group IIa gene transcription by thyroid hormone
  JOURNAL   J Biol Chem 288 (23), 16321-16333 (2013)
   PUBMED   23629656
  REMARK    GeneRIF: a novel inverse recruitment mechanism in which liganded
            TRbeta recruits corepressors to inhibit PLA2g2a expression.
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Horlein,A.J., Naar,A.M., Heinzel,T., Torchia,J., Gloss,B.,
            Kurokawa,R., Ryan,A., Kamei,Y., Soderstrom,M., Glass,C.K. et al.
  TITLE     Ligand-independent repression by the thyroid hormone receptor
            mediated by a nuclear receptor co-repressor
  JOURNAL   Nature 377 (6548), 397-404 (1995)
   PUBMED   7566114
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Ali,I.U., Lidereau,R. and Callahan,R.
  TITLE     Presence of two members of c-erbA receptor gene family (c-erbA beta
            and c-erbA2) in smallest region of somatic homozygosity on
            chromosome 3p21-p25 in human breast carcinoma
  JOURNAL   J Natl Cancer Inst 81 (23), 1815-1820 (1989)
   PUBMED   2573734
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Hodin,R.A., Lazar,M.A., Wintman,B.I., Darling,D.S., Koenig,R.J.,
            Larsen,P.R., Moore,D.D. and Chin,W.W.
  TITLE     Identification of a thyroid hormone receptor that is
            pituitary-specific
  JOURNAL   Science 244 (4900), 76-79 (1989)
   PUBMED   2539642
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Murray,M.B., Zilz,N.D., McCreary,N.L., MacDonald,M.J. and
            Towle,H.C.
  TITLE     Isolation and characterization of rat cDNA clones for two distinct
            thyroid hormone receptors
  JOURNAL   J Biol Chem 263 (25), 12770-12777 (1988)
   PUBMED   2457590
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Koenig,R.J., Warne,R.L., Brent,G.A., Harney,J.W., Larsen,P.R. and
            Moore,D.D.
  TITLE     Isolation of a cDNA clone encoding a biologically active thyroid
            hormone receptor
  JOURNAL   Proc Natl Acad Sci U S A 85 (14), 5031-5035 (1988)
   PUBMED   2899322
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Apr 19, 2007 this sequence version replaced NP_036804.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..497
                     /product="thyroid hormone receptor beta isoform 1"
                     /note="thyroid hormone receptor, beta (avian
                     erythroblastic leukemia viral (v-erb-a) oncogene homolog
                     2); TRbeta2Delta; thyroid hormone receptor beta2delta;
                     nuclear receptor subfamily 1 group A member 2; thyroid
                     hormone receptor beta 3"
                     /calculated_mol_wt=56651
     Region          106..228
                     /region_name="NR_DBD_TR"
                     /note="DNA-binding domain of thyroid hormone receptors
                     (TRs) is composed of two C4-type zinc fingers; cd06961"
                     /db_xref="CDD:143519"
     Site            order(107,110,124,127,181,187,197,200)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143519"
     Site            order(117..119,125..126,128,166,168..169,172,194..195,198,
                     201,214..216,221,224..225,227..228)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143519"
     Site            order(117,120,211,213..214)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:143519"
     Region          252..494
                     /region_name="NR_LBD_TR"
                     /note="The ligand binding domain of thyroid hormone
                     receptor, a members of a superfamily of nuclear receptors;
                     cd06935"
                     /db_xref="CDD:132733"
     Site            order(305,308..309,311..312,315,318,346,349,353,365..367,
                     377,380,382,389,471,478,491)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132733"
     Site            order(317,320,324,334,338,341,489..490,493)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132733"
     Site            order(384,429,459,462..463,466,469..470,472..473)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132733"
     CDS             1..497
                     /gene="Thrb"
                     /gene_synonym="c-erbA-2; C-erba-beta; ERBA2; Nr1a2;
                     RATT3REC; T3rec; TRbeta"
                     /coded_by="NM_012672.3:254..1747"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24831"
                     /db_xref="RGD:3858"
ORIGIN      
        1 mtpnsmteng lpawdkqkph pdrgqdwklv gmseaclhrk shverrgalk neqtsshliq
       61 atwassifhl dpddvndqsv ssaqtfqtee kkckgyipsy ldkdelcvvc gdkatgyhyr
      121 citcegckps htrdektgiw fhtdtsstsl hsvwmlssrq wdpegffrrt iqkslhpsys
      181 ckyegkciid kvtrnqcqec rfkkciyvgm atdlvlddsk rlakrkliee nrekrrreel
      241 qksighkpep tdeewelikt vteahvatna qgshwkqkrk flpedigqap ivnapeggkv
      301 dleafshftk iitpaitrvv dfakklpmfc elpcedqiil lkgccmeims lraavrydpd
      361 setltlngem avtrgqlkng glgvvsdaif dlgmslssfn lddtevallq avllmssdrp
      421 glacveriek yqdsfllafe hyinyrkhhv thfwpkllmk vtdlrmigac hasrflhmkv
      481 ecptelfppl flevfed
//
LOCUS       NP_001420020            1508 aa            linear   ROD 28-APR-2025
DEFINITION  glutamate-rich 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001420020 XP_017446849
VERSION     NP_001420020.1
DBSOURCE    REFSEQ: accession NM_001433091.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Aug 6, 2024 this sequence version replaced XP_017446849.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.10551.1,
                                           SRR26360176.1161933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1508
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1508
                     /product="glutamate-rich 3 isoform 2"
                     /note="glutamate-rich protein 3"
                     /calculated_mol_wt=166274
     Region          299..414
                     /region_name="DUF4590"
                     /note="Domain of unknown function (DUF4590); pfam15257"
                     /db_xref="CDD:464597"
     Region          <963..1239
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <1201..1491
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     CDS             1..1508
                     /gene="Erich3"
                     /coded_by="NM_001433091.1:481..5007"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:295528"
                     /db_xref="RGD:1593279"
ORIGIN      
        1 mshshpagll atynsltdkh lagyfnntri rrhllrsgli trsgrilsek eykvnnmkqd
       61 hqkyirecla raifhkvldm eryrqleikr klddlarrer iqrlkgehtr rfiednmpil
      121 tphppagpkt nrghsvlaee grsspltlta prpytapgnm qppvrlqpll snrqirngsk
      181 itsgskpktl lleseapfpl agkkammkfr nymdnsqked lyqlphinsy qipvppspqp
      241 qaksfrenrl eawrrkrlrp itaphglepl ftkdpgriyk taphsnavit mvyfgknvhv
      301 syddidfrde ikiyqqhcgg enlcvykgkl lekdtfqfis krhhgypfsl tfylngiqvn
      361 rissccefkh rrssrlggkr gyfgfvcvek aspcyrciia mgldrkpssm kpkkdkiaek
      421 keeslkknqg klrkdrenap skrnemerke ssvsaafsae eiklgvkevr taieemewkg
      481 righsvweed qdnavkydye edfeidelkq dekedgedqd ddqmsrgtks ptegekdnln
      541 pekeletsse kaldardsen fedtgcsdse eddrqdlktt ssissrshpy ssesedeste
      601 vggeadsvns egesskssss qdlrensdpg klhfpaeeyl gteieeqeit kldgdngpwl
      661 telsgthvte ekptkgsqal lesepkesrq vassevraks ellkeaglpw veevgqitge
      721 aqkpghgrst ppgpsptddg vtpmrkpevn ldrvveekav lssneqpvqa aqemrtlkee
      781 amekdepsqs edtdasvglr ekaemgedgt crpqdadmdg gprekagmle dgtchpqdad
      841 tdgglrekag iskvplgers ptgeqqasae qvtetgqypl riaseveagt egsrrhgeeq
      901 lisiekvaag asvflsveqg vdrqrdedpd rqaslqtgme egrtvsqgeq elekaaftds
      961 tglssetlge aailkeagts evkeaeremg spkpdgdqgk egalaelevm gpvvdtgper
     1021 edgseeaalg geraargrke fleaetpfss stgepqaspw edfpgnheel skedtaregi
     1081 itdtesteer dvravfpgel aaaggmekae rptpplretg sdreeetgae vlktedlleh
     1141 kvkgeeegtv revgfeeeac assheteadt enaeptgate sgevtklpee lpeertitlf
     1201 eatpqfeksp eesaatnteh qggeelpgqe seapwpqerg lshdgegllg apgpepadka
     1261 qgpegiftar geewaaeepd shveperlee ngplqvqggd imrrtqgnlp kerltravvc
     1321 reaevekpqg egdgdkecsp gtetvglivq nwitggstve aqedpqegei edsaewrevs
     1381 eesksadgip masssadaqq etwdrageal getaneertl tedmtpraek vavveevtsa
     1441 gamaetqqeq apevqysrpg edreggeaka sqhpgmagee tgatrkdeeh qtgaagefrg
     1501 svsqseta
//
LOCUS       NP_599235               1487 aa            linear   ROD 28-APR-2025
DEFINITION  adhesion G protein-coupled receptor L2 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_599235
VERSION     NP_599235.3
DBSOURCE    REFSEQ: accession NM_134408.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1487)
  AUTHORS   Vezain,M., Lecuyer,M., Rubio,M., Dupe,V., Ratie,L., David,V.,
            Pasquier,L., Odent,S., Coutant,S., Tournier,I., Trestard,L.,
            Adle-Biassette,H., Vivien,D., Frebourg,T., Gonzalez,B.J.,
            Laquerriere,A. and Saugier-Veber,P.
  TITLE     A de novo variant in ADGRL2 suggests a novel mechanism underlying
            the previously undescribed association of extreme microcephaly with
            severely reduced sulcation and rhombencephalosynapsis
  JOURNAL   Acta Neuropathol Commun 6 (1), 109 (2018)
   PUBMED   30340542
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1487)
  AUTHORS   Anderson,G.R., Maxeiner,S., Sando,R., Tsetsenis,T., Malenka,R.C.
            and Sudhof,T.C.
  TITLE     Postsynaptic adhesion GPCR latrophilin-2 mediates target
            recognition in entorhinal-hippocampal synapse assembly
  JOURNAL   J Cell Biol 216 (11), 3831-3846 (2017)
   PUBMED   28972101
REFERENCE   3  (residues 1 to 1487)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 1487)
  AUTHORS   Archambaud,C., Nahori,M.A., Soubigou,G., Becavin,C., Laval,L.,
            Lechat,P., Smokvina,T., Langella,P., Lecuit,M. and Cossart,P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   5  (residues 1 to 1487)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   6  (residues 1 to 1487)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 1487)
  AUTHORS   Kreienkamp,H.J., Zitzer,H., Gundelfinger,E.D., Richter,D. and
            Bockers,T.M.
  TITLE     The calcium-independent receptor for alpha-latrotoxin from human
            and rodent brains interacts with members of the ProSAP/SSTRIP/Shank
            family of multidomain proteins
  JOURNAL   J Biol Chem 275 (42), 32387-32390 (2000)
   PUBMED   10964907
REFERENCE   8  (residues 1 to 1487)
  AUTHORS   Ichtchenko,K., Bittner,M.A., Krasnoperov,V., Little,A.R.,
            Chepurny,O., Holz,R.W. and Petrenko,A.G.
  TITLE     A novel ubiquitously expressed alpha-latrotoxin receptor is a
            member of the CIRL family of G-protein-coupled receptors
  JOURNAL   J Biol Chem 274 (9), 5491-5498 (1999)
   PUBMED   10026162
REFERENCE   9  (residues 1 to 1487)
  AUTHORS   Sugita,S., Ichtchenko,K., Khvotchev,M. and Sudhof,T.C.
  TITLE     alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an
            unusual family of ubiquitous G-protein-linked receptors. G-protein
            coupling not required for triggering exocytosis
  JOURNAL   J Biol Chem 273 (49), 32715-32724 (1998)
   PUBMED   9830014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF063102.1, FM039554.1, AF081148.1, CB579130.1, AF081151.1,
            CO556290.1, FM099106.1, FM068641.1 and AA899882.1.
            
            On Oct 7, 2014 this sequence version replaced NP_599235.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF063102.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1487
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q45"
     Protein         1..1487
                     /product="adhesion G protein-coupled receptor L2 isoform 1
                     precursor"
                     /note="latrophilin-2; calcium-independent alpha-latrotoxin
                     receptor 2; calcium-independent alpha-latrotoxin receptor
                     homolog 2"
                     /calculated_mol_wt=163973
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2850
     mat_peptide     26..1487
                     /product="Adhesion G protein-coupled receptor L2.
                     /id=PRO_0000012911"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
                     /calculated_mol_wt=163973
     Region          36..132
                     /region_name="Gal_Rha_Lectin_LPHN2"
                     /note="galactose/rhamnose binding lectin domain found in
                     latrophilin-2 and similar proteins; cd22845"
                     /db_xref="CDD:438702"
     Site            order(37..40,42,45,52..54,68,70..73,122,124)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438702"
     Site            order(43,64,78,114,116..121)
                     /site_type="other"
                     /note="putative rhamnose binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            order(95,98..99)
                     /site_type="other"
                     /note="putative NAG binding site [chemical binding]"
                     /db_xref="CDD:438702"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          142..398
                     /region_name="OLF"
                     /note="Olfactomedin-like domain; cl02549"
                     /db_xref="CDD:470611"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          422..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          469..533
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            524
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          542..764
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            735
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          788..840
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Site            791
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Region          792..841
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            828..829
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098; propagated
                     from UniProtKB/Swiss-Prot (O88923.2)"
     Region          848..1129
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          851..875
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            856..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          884..905
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            885..905
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            912..932
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          915..937
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          956..972
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            957..977
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          991..1014
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            995..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1065..1087
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1066..1086
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1091..1116
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            1091..1111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1128..1487
                     /region_name="Latrophilin"
                     /note="Latrophilin Cytoplasmic C-terminal region;
                     pfam02354"
                     /db_xref="CDD:460538"
     Region          1139..1160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Region          1386..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88923.2)"
     Site            1402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZZ7; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88923.2)"
     CDS             1..1487
                     /gene="Adgrl2"
                     /gene_synonym="Cirl-2; Cirl2; Cl2ac; Lphn2"
                     /coded_by="NM_134408.3:24..4487"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:171447"
                     /db_xref="RGD:620835"
ORIGIN      
        1 mvssgcrmrs lwfimiisfs pntegfsraa lpfglvrrel scegysidlr cpgsdvimie
       61 sanygrtddk icdadpfqme ntdcylpdaf kimtqrcnnr tqcvvvtgsd vfpdpcpgty
      121 kylevqyecv pymeqkvfvc pgtlkaivds psiyeaeqka gawckdplqa adkiyfmpwt
      181 pyrtdtliey asledfqnsr qtttyklpnr vdgtgfvvyd gavffnkert rnivkfdlrt
      241 riksgeaiin yanyhdtspy rwggktdidl avdenglwvi yateqnngmi visqlnpytl
      301 rfeatwetty dkraasnafm icgvlyvvrs vyqdneseag knvidyiynt rlsrgehvdv
      361 pfpnqyqyia avdynprdnq lyvwnnnfil ryslefgppd paqvpttavt itssaelfkt
      421 tvsttsstsq rgpvsstvag pqegsrgtkp ppavsttkip pvtnifplpe rfcealemkg
      481 ikwpqtqrgm mverpcpkgt rgtasylcma stgtwnpkgp dlsnctshwv nqlaqkirsg
      541 enaaslanel akhtkgtvfa gdvsssvrlm eqlvdildaq lqelkpsekd sagrsynklq
      601 krektcrayl kaivdtvdnl lraetldcwk hmnsseqaht atmlldtlee gafvladnll
      661 eptrvsmptd nivlevavls tegqvqdftf hlgfkgafss iqlsantvkq nsrnglakvv
      721 fiiyrslgpf lstenatvkl gadllgrnst iavnshvlsv sinkessrvy ltdpvlfsmp
      781 hidsdnyfna ncsfwnyser tmmgywstqg cklvdtnktr ttcacshltn failmahrei
      841 vykdgvhkll ltvitwvgiv vslvclaici ftfcffrglq sdrntihknl cinlfiaefi
      901 fligidktqy tiacpvfagl lhffflaafs wmclegvqly lmlvevfese ysrkkyyyva
      961 gylfpatvvg vsaaidyksy gtleacwlhv dnyfiwsfig pvtfiillni iflvitlckm
     1021 vkhsntlkpd ssrleninny rvcdgyyntd lpgyednkpf ikswvlgafa llcllgltws
     1081 fgllfvneet vvmaylftaf nafqglfifi fhcalqkkvr keyakcfrhw yccgglptes
     1141 phssvkasts rtsaryssgt qsrirrmwnd tvrkqsessf isgdinstst lnqgmtgnyl
     1201 ltnpllrphg tnnpyntlla etvvcnapsa pvfnspghsl nntrdtsamd tlplngnfnn
     1261 syslrkadyh dgvqvvdcgl slndtafekm iiselvhnnl rgsnkthnle lklpvkpvig
     1321 gssseddaiv adasslmhgd npglefrhke leaplipqrt hsllyqpqkk vkpeatdsyv
     1381 sqltaeadeh lqspnrdsly tsmpnlrdsp ypesspdmae dlspsrrsen ediyyksmpn
     1441 lgagrqlqmc yqisrgnsdg yiipinkegc ipegdvregq mqlvtsl
//
LOCUS       NP_001417060             165 aa            linear   ROD 28-APR-2025
DEFINITION  disks large homolog 5-like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001417060 XP_063122395
VERSION     NP_001417060.1
DBSOURCE    REFSEQ: accession NM_001430131.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On May 7, 2024 this sequence version replaced XP_063122395.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.430175.1,
                                           SRR26360181.216956.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8"
     Protein         1..165
                     /product="disks large homolog 5-like isoform 2"
                     /calculated_mol_wt=19223
     Region          48..>99
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..165
                     /gene="LOC134480032"
                     /coded_by="NM_001430131.1:38..535"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:134480032"
                     /db_xref="RGD:402237256"
ORIGIN      
        1 mfsrlrknfg rvnadfgqtg vresrlsski ndgqrklawg mlkdgrltss pgpvvinkea
       61 ntenteeqrl irqlqsatee rnelrdllty vteryrnnrn lpirihmdki cmqkklfpfr
      121 keskaeqlds apllqkflfd lnkkdkdeqe ktsnlqtkqh ldntt
//
LOCUS       NP_001100444             416 aa            linear   ROD 28-APR-2025
DEFINITION  RNA binding protein fox-1 homolog 1 [Rattus norvegicus].
ACCESSION   NP_001100444 XP_001076609 XP_220155
VERSION     NP_001100444.2
DBSOURCE    REFSEQ: accession NM_001106974.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Shen,F., Xu,X., Yu,Z., Li,H., Shen,H., Li,X., Shen,M. and Chen,G.
  TITLE     Rbfox-1 contributes to CaMKIIalpha expression and intracerebral
            hemorrhage-induced secondary brain injury via blocking
            micro-RNA-124
  JOURNAL   J Cereb Blood Flow Metab 41 (3), 530-545 (2021)
   PUBMED   32248729
  REMARK    GeneRIF: Rbfox-1 contributes to CaMKIIalpha expression and
            intracerebral hemorrhage-induced secondary brain injury via
            blocking micro-RNA-124.
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Vaht,M., Laas,K., Fernandez-Castillo,N., Kurrikoff,T., Kanarik,M.,
            Faraone,S.V., Tooding,L.M., Veidebaum,T., Franke,B., Reif,A.,
            Cormand,B. and Harro,J.
  TITLE     Variants of the Aggression-Related RBFOX1 Gene in a Population
            Representative Birth Cohort Study: Aggressiveness, Personality, and
            Alcohol Use Disorder
  JOURNAL   Front Psychiatry 11, 501847 (2020)
   PUBMED   33329073
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Kucherenko,M.M. and Shcherbata,H.R.
  TITLE     Stress-dependent miR-980 regulation of Rbfox1/A2bp1 promotes
            ribonucleoprotein granule formation and cell survival
  JOURNAL   Nat Commun 9 (1), 312 (2018)
   PUBMED   29358748
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Wang,J., Li,G., Yu,D., Wong,Y.P., Yong,T.F., Liang,M.C., Liao,P.,
            Foo,R., Hoppe,U.C. and Soong,T.W.
  TITLE     Characterization of CaV1.2 exon 33 heterozygous knockout mice and
            negative correlation between Rbfox1 and CaV1.2 exon 33 expressions
            in human heart failure
  JOURNAL   Channels (Austin) 12 (1), 51-57 (2018)
   PUBMED   28949795
  REMARK    Correction to:[Addendum to: Li G, Wang J, Liao P, Bartels P, Zhang
            H, Yu D, Liang MC, Poh KK, Yu CY, Jiang F, et al. Exclusion of
            alternative exon 33 of CaV1.2 calcium channels in heart is
            proarrhythmogenic. Proc Natl Acad Sci U S A. 2017;114:E4288-E4295.
            http://doi: 10.1073/pnas.1617205114.]
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Kapeli,K., Pratt,G.A., Vu,A.Q., Hutt,K.R., Martinez,F.J.,
            Sundararaman,B., Batra,R., Freese,P., Lambert,N.J., Huelga,S.C.,
            Chun,S.J., Liang,T.Y., Chang,J., Donohue,J.P., Shiue,L., Zhang,J.,
            Zhu,H., Cambi,F., Kasarskis,E., Hoon,S., Ares,M. Jr., Burge,C.B.,
            Ravits,J., Rigo,F. and Yeo,G.W.
  TITLE     Distinct and shared functions of ALS-associated proteins TDP-43,
            FUS and TAF15 revealed by multisystem analyses
  JOURNAL   Nat Commun 7, 12143 (2016)
   PUBMED   27378374
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Pistoni,M., Shiue,L., Cline,M.S., Bortolanza,S., Neguembor,M.V.,
            Xynos,A., Ares,M. Jr. and Gabellini,D.
  TITLE     Rbfox1 downregulation and altered calpain 3 splicing by FRG1 in a
            mouse model of Facioscapulohumeral muscular dystrophy (FSHD)
  JOURNAL   PLoS Genet 9 (1), e1003186 (2013)
   PUBMED   23300487
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Gehman,L.T., Meera,P., Stoilov,P., Shiue,L., O'Brien,J.E.,
            Meisler,M.H., Ares,M. Jr., Otis,T.S. and Black,D.L.
  TITLE     The splicing regulator Rbfox2 is required for both cerebellar
            development and mature motor function
  JOURNAL   Genes Dev 26 (5), 445-460 (2012)
   PUBMED   22357600
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Kim,K.K., Kim,Y.C., Adelstein,R.S. and Kawamoto,S.
  TITLE     Fox-3 and PSF interact to activate neural cell-specific alternative
            splicing
  JOURNAL   Nucleic Acids Res 39 (8), 3064-3078 (2011)
   PUBMED   21177649
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Ma,L., Hanson,R.L., Traurig,M.T., Muller,Y.L., Kaur,B.P.,
            Perez,J.M., Meyre,D., Fu,M., Korner,A., Franks,P.W., Kiess,W.,
            Kobes,S., Knowler,W.C., Kovacs,P., Froguel,P., Shuldiner,A.R.,
            Bogardus,C. and Baier,L.J.
  TITLE     Evaluation of A2BP1 as an obesity gene
  JOURNAL   Diabetes 59 (11), 2837-2845 (2010)
   PUBMED   20724578
  REMARK    GeneRIF: Association analysis suggests that variation in A2BP1
            influences obesity.
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Shibata,H., Huynh,D.P. and Pulst,S.M.
  TITLE     A novel protein with RNA-binding motifs interacts with ataxin-2
  JOURNAL   Hum Mol Genet 9 (9), 1303-1313 (2000)
   PUBMED   10814712
  REMARK    Erratum:[Hum Mol Genet 2000 Jul 22;9(12):1903]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jan 10, 2008 this sequence version replaced NP_001100444.1.
            
            Summary: The Fox-1 family of RNA-binding proteins is evolutionarily
            conserved, and regulates tissue-specific alternative splicing in
            metazoa. Fox-1 recognizes a (U)GCAUG stretch in regulated exons or
            in flanking introns. [provided by RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..416
                     /product="RNA binding protein fox-1 homolog 1"
                     /note="fox-1 homolog A; ataxin 2 binding protein 1; RNA
                     binding protein, fox-1 homolog 1"
                     /calculated_mol_wt=44425
     Region          31..>220
                     /region_name="Agg_substance"
                     /note="LPXTG-anchored aggregation substance; NF033875"
                     /db_xref="CDD:411439"
     Region          136..211
                     /region_name="RRM_FOX1_like"
                     /note="RNA recognition motif (RRM) found in vertebrate RNA
                     binding protein fox-1 homologs and similar proteins;
                     cd12407"
                     /db_xref="CDD:409841"
     Site            order(137,139,141..146,166..170,172..177,179,203,208..211)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409841"
     Region          272..361
                     /region_name="Fox-1_C"
                     /note="Calcitonin gene-related peptide regulator C
                     terminal; pfam12414"
                     /db_xref="CDD:463568"
     CDS             1..416
                     /gene="Rbfox1"
                     /gene_synonym="A2bp1"
                     /coded_by="NM_001106974.2:230..1480"
                     /db_xref="GeneID:302920"
                     /db_xref="RGD:1311210"
ORIGIN      
        1 mlasqgvllh sygvpmvvpa apffpglmqg nqeaaaapdt maqpyasaqf appqngipae
       61 ytaphphpap eytgqttvpd htlnlypptq thseqsadts aqtvsgtatq tddaaptdgq
      121 pqtqpsente nksqpkrlhv snipfrfrdp dlrqmfgqfg kildveiifn ergskgfgfv
      181 tfensadadr areklhgtvv egrkievnna tarvmtnkka vnpytngwkl npvvgavysp
      241 dfyagtvllc qanqegssmy sgpsslvyts ampgfpypaa taaaayrgah lrgrgrtvyn
      301 tfraaapppp ipayggvvyq dgfygadiyg gyaayryaqp tpataaaysd sygrvyaadp
      361 yhhtlapapt ygvgamnafa pltdaktrsh addvglvlss lqasiyrggy nrfapy
//
LOCUS       NP_001380696             495 aa            linear   ROD 28-APR-2025
DEFINITION  BUB3-interacting and GLEBS motif-containing protein ZNF207 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001380696
VERSION     NP_001380696.1
DBSOURCE    REFSEQ: accession NM_001393767.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Jiang,H., Wang,S., Huang,Y., He,X., Cui,H., Zhu,X. and Zheng,Y.
  TITLE     Phase transition of spindle-associated protein regulate spindle
            apparatus assembly
  JOURNAL   Cell 163 (1), 108-122 (2015)
   PUBMED   26388440
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Toledo,C.M., Herman,J.A., Olsen,J.B., Ding,Y., Corrin,P.,
            Girard,E.J., Olson,J.M., Emili,A., DeLuca,J.G. and Paddison,P.J.
  TITLE     BuGZ is required for Bub3 stability, Bub1 kinetochore function, and
            chromosome alignment
  JOURNAL   Dev Cell 28 (3), 282-294 (2014)
   PUBMED   24462187
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Jiang,H., He,X., Wang,S., Jia,J., Wan,Y., Wang,Y., Zeng,R.,
            Yates,J. 3rd, Zhu,X. and Zheng,Y.
  TITLE     A microtubule-associated zinc finger protein, BuGZ, regulates
            mitotic chromosome alignment by ensuring Bub3 stability and
            kinetochore targeting
  JOURNAL   Dev Cell 28 (3), 268-281 (2014)
   PUBMED   24462186
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Misawa,K., Nosaka,T., Morita,S., Kaneko,A., Nakahata,T., Asano,S.
            and Kitamura,T.
  TITLE     A method to identify cDNAs based on localization of green
            fluorescent protein fusion products
  JOURNAL   Proc Natl Acad Sci U S A 97 (7), 3062-3066 (2000)
   PUBMED   10716735
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Taguchi,E., Muramatsu,H., Fan,Q.W., Kurosawa,N., Sobue,G. and
            Muramatsu,T.
  TITLE     Zep: A novel zinc finger protein containing a large proline-rich
            domain
  JOURNAL   J Biochem 124 (6), 1220-1228 (1998)
   PUBMED   9832628
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.42172.1,
                                           SRR26643288.42159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..495
                     /product="BUB3-interacting and GLEBS motif-containing
                     protein ZNF207 isoform 2"
                     /note="BUB3-interacting and GLEBS motif-containing protein
                     ZNF207"
                     /calculated_mol_wt=52648
     Region          10..90
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          13..34
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          13..34
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(18,24,31,33,36,43)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          37..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          <437..472
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     CDS             1..495
                     /gene="Zfp207"
                     /coded_by="NM_001393767.2:138..1625"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:303763"
                     /db_xref="RGD:1308121"
ORIGIN      
        1 mgrkkkkqlk pwcwycnrdf ddekiliqhq kakhfkchic hkklytgpgl aihcmqvhke
       61 tidavpnaip grtdieleiy gmegipekdm derrrlleqk tqesqkkkqq ddsdeyddde
      121 saastsfqpq pvqpqqgyip pmaqpglppv pgapgmppgi pplmpgvppl mpgmppvmpg
      181 mppglhhqrk ytqsfcgeni mmpmggmmpp gpgipplmpg mppgmpppvp rpgippmtqa
      241 qavsapgiln rppaptaavp apqppvtkpl fpsagqmgtp vtssstassn seslsasska
      301 lfpstaqaqa avqgpvgtdf kplnstpaat tteppkptfp aytqstastt sttnstaakp
      361 aasitskpat ltttsatskl ihpdedisle erraqlpkyq rnlprpgqtp ignppvgpig
      421 gmmppqpgip qqqgmrppmp phgqygghhq gmpgylpgam ppygqgppmv ppyqggpprp
      481 pmgmrppvms qggry
//
LOCUS       NP_001420976            2086 aa            linear   ROD 28-APR-2025
DEFINITION  dedicator of cytokinesis protein 11 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001420976 XP_006257515
VERSION     NP_001420976.1
DBSOURCE    REFSEQ: accession NM_001434047.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2086)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2086)
  AUTHORS   Matsuda,T., Yanase,S., Takaoka,A. and Maruyama,M.
  TITLE     The immunosenescence-related gene Zizimin2 is associated with early
            bone marrow B cell development and marginal zone B cell formation
  JOURNAL   Immun Ageing 12, 1 (2015)
   PUBMED   25729399
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2086)
  AUTHORS   Sakabe,I., Asai,A., Iijima,J. and Maruyama,M.
  TITLE     Age-related guanine nucleotide exchange factor, mouse Zizimin2,
            induces filopodia in bone marrow-derived dendritic cells
  JOURNAL   Immun Ageing 9, 2 (2012)
   PUBMED   22494997
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2086)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Oct 18, 2024 this sequence version replaced XP_006257515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.56433.1,
                                           SRR26643284.21590.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2086
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq34"
     Protein         1..2086
                     /product="dedicator of cytokinesis protein 11 isoform 2"
                     /note="dedicator of cytokinesis protein 11"
                     /calculated_mol_wt=239168
     Region          38..147
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          161..284
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          639..828
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1628..2040
                     /region_name="DHR2_DOCK11"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 11; cd11700"
                     /db_xref="CDD:212573"
     Site            order(1733,1743,1745..1746,1748..1749,1752..1753,
                     1755..1756,1759..1760)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212573"
     Site            order(1767..1770,1801..1802,1804..1807,1809..1810,
                     1829..1831,1848,1850,1879,1881,1888..1889,1895,1897,
                     1934..1935,1938,1952,1954,1958,1961..1963,1966..1972,1975,
                     2003,2021..2022,2024..2025,2028)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212573"
     Site            1966..1971
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212573"
     CDS             1..2086
                     /gene="Dock11"
                     /coded_by="NM_001434047.1:110..6370"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:313438"
                     /db_xref="RGD:1564707"
ORIGIN      
        1 maevrkftkr lskpgtaael rqsvseavrg svvlekaklv epldyenvit qrktqiysdp
       61 lrdllmfpme dislsvigrq lrtvqstvpe daekraqslf vkeciktyst dwhvvnykye
      121 dfsgdfrmlp ckslrpekip nhvfeidedc ekdedssslc sqkggvikqg wlhkanvnst
      181 itvtmkvfkr ryfyltqlpd gsyilnsykd eknskeskgc iyldacidvv qcpkmrrhaf
      241 elkmldkysh ylaaeteqem eewlitlkki iqintdslvq ekketveaiq eeetssqgka
      301 enimaslers mhpelmkygr eteqlnklsr gdgrqnlfsf dsevqrldfs giepdvkpfe
      361 ekcnkrflvn chdltfnilg higdnakgpp tnvepffitl alfdvknnck isadfhvdln
      421 ppsvremlwg mstqlandgn tkgsspesli hgiaesrlcy irqgifsvtn phpeiflvvr
      481 iekvlqgnit hcaepyikns dpiktaqkvh rtakqvcsrl gqyrmpfawa arpifkdlqg
      541 sldldgkfsp lykqdsskls nedilkllse ykkpektklq iipgqlnitv ecvpvdlpnc
      601 itssyvplkp fekncqnitv eveefvpemt kycypftiyk nhlyvyplql kydsqksfak
      661 arniavcvef rdsdesdtsa lkciygkpag svfttnayav vshhnqnpef ydeikielpi
      721 hlhqkhhllf tfyhvscein tkgttkkqdt vetpvgfawv pllkdgrvtt leqqlpvsan
      781 lppgylnvnd aesrrqsnad ikwvdgakpl lkikthlest iytqdlhvhk ffhhcqliqs
      841 gskevpgeli kylkclhame iqvmiqflpv ilmqlfrvlt nmtheddvpi nctmvllhiv
      901 skcheegles ylrsfikysf rpekpstlqa qlihetlatt miailkqsad flainkllky
      961 swfffeiiak smatylleen kiklprgqrf peayhhilhs lllaiiphvt iryaeipdes
     1021 rnvnyslasf lkrcltlmdr gfvfnlindy isgfspkdpk vlaeykfefl qticnhehyi
     1081 plnlpmafak pklqrvqdff sfavdrltsv dsnleyslsd eyckhhflvg lllretsial
     1141 qdnyeiryta isviknllik hafdtryqhk nqqakiaqly lpfvglllen iqrlagrdtl
     1201 yscaampnsa srdefpcgfv sptsrgslat dkepaygsfq nghgikreds rgslipegat
     1261 gfpdpgstge ntrqsssrts vsqynrldqy eirnllmcyl yivkmisedt lltywnkvsp
     1321 qelinilvll evclfhfrym gkrniarvhd awlskhfgid rksqtmpalr nrsgvmqarl
     1381 qhlsslessf tlnhssatte adifhqalle gntatevslt vldtisfftq cfksqllnnd
     1441 ghnplmkkvf dihlaflkng qsevslkhvf aslrsfiskf psaffkgrvn mcaafcyevl
     1501 kcctskisst rneasallyl lmrnnfeytk rktflrthlq iiiavsqlia dvalsggsrf
     1561 qeslfiinnf ansdrpmkat afptevkdlt krirtvlmat aqmkehekdp emlidlqysl
     1621 aksyastpel rktwldsmak ihikngdfse aamcyvhvaa lvaeflhrkk lfpsgcsafk
     1681 kitpnideeg amkedagmmd vhyseevlle lleqcvdglw kaeryevise iskliipiye
     1741 krrefekltq vyrtlhgayt kilevmhtkk rllgtffrva fygqsffeee dgkeyiykep
     1801 kltglseisf rlvklygekf gtenikiiqd sdkvnakeld pkfahiqvty vkpyfddkel
     1861 terktefern hninrfvfea pytlsgkkqg cieeqckrrt ilttsnsfpy vkkripitce
     1921 qqvnlkpidv atdeikdkta elhklcssad vdmiqlqlkl qgcvsvqvna gplayarafl
     1981 nesqankypp kkvnelkdmf rkfiqacsia lelnerlike dqieyheglk snfrdmvkel
     2041 sdiiheqilq edtmhspwmn ntlhvfcais gtssnrgygs prysev
//
LOCUS       NP_059041               1255 aa            linear   ROD 28-APR-2025
DEFINITION  neural cell adhesion molecule L1 isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_059041 XP_017457629 XP_346880
VERSION     NP_059041.2
DBSOURCE    REFSEQ: accession NM_017345.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1255)
  AUTHORS   Gallo,P.N., Mihelc,E., Eisert,R., Bradshaw,G.A., Dimek,F.,
            Leffler,A., Kalocsay,M. and Moiseenkova-Bell,V.
  TITLE     The dynamic TRPV2 ion channel proximity proteome reveals functional
            links of calcium flux with cellular adhesion factors NCAM and L1CAM
            in neurite outgrowth
  JOURNAL   Cell Calcium 121, 102894 (2024)
   PUBMED   38728789
  REMARK    GeneRIF: The dynamic TRPV2 ion channel proximity proteome reveals
            functional links of calcium flux with cellular adhesion factors
            NCAM and L1CAM in neurite outgrowth.
REFERENCE   2  (residues 1 to 1255)
  AUTHORS   Platek,R., Grycz,K., Wieckowska,A., Czarkowska-Bauch,J. and Skup,M.
  TITLE     L1 Cell Adhesion Molecule Overexpression Down Regulates Phosphacan
            and Up Regulates Structural Plasticity-Related Genes Rostral and
            Caudal to the Complete Spinal Cord Transection
  JOURNAL   J Neurotrauma 37 (3), 534-554 (2020)
   PUBMED   31426714
  REMARK    GeneRIF: L1 Cell Adhesion Molecule Overexpression Down Regulates
            Phosphacan and Up Regulates Structural Plasticity-Related Genes
            Rostral and Caudal to the Complete Spinal Cord Transection.
REFERENCE   3  (residues 1 to 1255)
  AUTHORS   Emmert,A.S., Vuong,S.M., Shula,C., Lindquist,D., Yuan,W., Hu,Y.C.,
            Mangano,F.T. and Goto,J.
  TITLE     Characterization of a novel rat model of X-linked hydrocephalus by
            CRISPR-mediated mutation in L1cam
  JOURNAL   J Neurosurg 132 (3), 945-958 (2019)
   PUBMED   30738385
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1255)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   5  (residues 1 to 1255)
  AUTHORS   White,K.M., Sabatino,J.A., He,M., Davis,N., Tang,N. and Bearer,C.F.
  TITLE     Toluene disruption of the functions of L1 cell adhesion molecule at
            concentrations associated with occupational exposures
  JOURNAL   Pediatr Res 80 (1), 145-150 (2016)
   PUBMED   27027721
  REMARK    GeneRIF: toluene inhibits L1-lipid raft interactions at
            occupationally relevant concentrations and may lead to a fetal
            solvent spectrum disorder similar to fetal alcohol spectrum
            disorder
REFERENCE   6  (residues 1 to 1255)
  AUTHORS   Shults,C.W., Alberti,L., Kimber,T.A. and Stallcup,W.B.
  TITLE     Mesostriatal dopaminergic axons transiently express high levels of
            NILE during development
  JOURNAL   Exp Neurol 116 (3), 275-285 (1992)
   PUBMED   1350253
REFERENCE   7  (residues 1 to 1255)
  AUTHORS   Tocco,M.D., Fujita,K. and Guroff,G.
  TITLE     Effect of dexamethasone on the nerve growth factor-induced increase
            in the NILE glycoprotein in PC12 cells
  JOURNAL   J Neurosci Res 31 (1), 28-32 (1992)
   PUBMED   1377284
REFERENCE   8  (residues 1 to 1255)
  AUTHORS   Miura,M., Kobayashi,M., Asou,H. and Uyemura,K.
  TITLE     Molecular cloning of cDNA encoding the rat neural cell adhesion
            molecule L1. Two L1 isoforms in the cytoplasmic region are produced
            by differential splicing
  JOURNAL   FEBS Lett 289 (1), 91-95 (1991)
   PUBMED   1894011
REFERENCE   9  (residues 1 to 1255)
  AUTHORS   Prince,J.T., Milona,N. and Stallcup,W.B.
  TITLE     Characterization of a partial cDNA clone for the NILE glycoprotein
            and identification of the encoded polypeptide domain
  JOURNAL   J Neurosci 9 (5), 1825-1834 (1989)
   PUBMED   2723751
REFERENCE   10 (residues 1 to 1255)
  AUTHORS   Prince,J.T., Milona,N. and Stallcup,W.B.
  TITLE     Characterization of a partial cDNA clone for the NILE glycoprotein
            and identification of the encoded polypeptide domain
  JOURNAL   J Neurosci 9 (3), 876-883 (1989)
   PUBMED   2466966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On or before Jul 18, 2024 this sequence version replaced
            XP_017457629.1, NP_059041.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: X59149.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA5760383,
                                    SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1255
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..1255
                     /product="neural cell adhesion molecule L1 isoform 1
                     precursor"
                     /note="NILE; nerve-growth factor-inducible large external
                     glycoprotein; NCAM-L1; N-CAM-L1; neuron-glia cell adhesion
                     molecule; neural cell adhesion molecule L1"
                     /calculated_mol_wt=138173
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2239
     Region          35..130
                     /region_name="IgI_L1-CAM_like"
                     /note="Immunoglobulin (Ig)-like domain of the L1 cell
                     adhesion molecule (CAM) and similar proteins; member of
                     the I-set of Ig superfamily (IgSF) domains; cd05733"
                     /db_xref="CDD:409396"
     Region          35..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409396"
     Region          44..48
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409396"
     Region          53..60
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409396"
     Region          66..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409396"
     Region          74..76
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409396"
     Region          83..86
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409396"
     Region          93..97
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409396"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          109..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409396"
     Region          120..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409396"
     Region          139..229
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          153..157
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          167..171
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          190..194
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          205..210
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          221..224
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          247..329
                     /region_name="Ig3_L1-CAM"
                     /note="Third immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05876"
                     /db_xref="CDD:409460"
     Region          259..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409460"
     Region          272..276
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409460"
     Site            293
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409460"
     Region          308..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409460"
     Region          321..324
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409460"
     Region          333..421
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          349..353
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..366
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          386..390
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          400..405
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          413..416
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          427..513
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          443..447
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          456..460
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          479..483
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          493..498
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          506..509
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          515..611
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          534..538
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          549..553
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          553..555
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          562..564
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          573..577
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          587..592
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          600..603
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          611..708
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(611,680,695)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            670
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            order(696..697,699..700)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          697..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          717..798
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            725
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            776
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          824..906
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            824
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            848
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            875
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            order(902..903,905..906)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            order(917,984,999)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          920..1002
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            968
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            978
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1021
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1029
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1072
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1123..1145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Region          1146..1231
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32004; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Region          1224..1255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     Site            1246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32004; propagated from
                     UniProtKB/Swiss-Prot (Q05695.3)"
     CDS             1..1255
                     /gene="L1cam"
                     /gene_synonym="Hsas; Hyd; N-CAM L1; NCAML1; NgCAM"
                     /coded_by="NM_017345.3:255..4022"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:50687"
                     /db_xref="RGD:619777"
ORIGIN      
        1 mvmmlwyvlp lllcspclli qipdeykghh vleppviteq sprrlvvfpt ddislkcear
       61 grpqvefrwt kdgihfkpke elgvvvheap ysgsftiegn nsfaqrfqgi yrcyasnnlg
      121 tamsheiqlv aegapkwpke tvkpveveeg esvvlpcnpp psaaplriyw mnskilhikq
      181 dervsmgqng dlyfanvlts dnhsdyicna hfpgtrtiiq kepidlrvkp tnsmidrkpr
      241 llfptnsssh lvalqgqsli leciaegfpt ptikwlhpsd pmptdrviyq nhnktlqlln
      301 vgeeddgeyt claenslgsa rhayyvtvea apywlqkpqs hlygpgetar ldcqvqgrpq
      361 pevtwringm siekvnkdqk yrieqgslil snvqpsdtmv tqcearnqhg lllanayiyv
      421 vqlpariltk dnqtymaveg stayllckaf gapvpsvqwl deegttvlqd erffpyangt
      481 lgirdlqand tgryfcqaan dqnnvtilan lqvkeatqit qgprstiekk garvtftcqa
      541 sfdpslqasi twrgdgrdlq ergdsdkyfi edgqlviqsl dysdqgnysc vasteldeve
      601 sraqllvvgs pgpvphlels drhllkqsqv hlswspaedh nspiekydie fedkemapek
      661 wfslgkvpgn qtsttlklsp yvhytfrvta inkygsgeps pvsetvvtpe aapeknpvdv
      721 rgegnetnnm vitwkplrwm dwnapqiqyr vqwrplgkqe twkeqtvsdp flvvsntstf
      781 vpyeikvqav nnqgkgpepq vtigysgedy pqvspeledi tifnsstvlv rwrpvdlaqv
      841 kghlrgynvt ywwkgsqrkh skrhvhkshm vvpanttsai lsglrpyssy hvevqafngr
      901 glgpasewtf stpegvpghp ealhlecqsd tslllhwqpp lshngvltgy llsyhpldge
      961 skeqlffnls dpelrthnlt nlnpdlqyrf qlqattqqgp geaivreggt malfgkpdfg
     1021 nisvtageny svvswvpreg qcnfrfhilf kalpegkvsp dhqpqpqyvs ynqssytqwd
     1081 lqpdtkyeih lmrekvllhh lavktngtgp vrvsttgsfa segwfiafvs aiillllill
     1141 ilcfikrskg gkysvkdked tqvdsearpm kdetfgeysd neekafgssq pslngdikpl
     1201 gsddsladyg gsvdvqfned gsfigqysgk kekeaaggnd ssgatspinp avale
//
LOCUS       NP_001178689            2073 aa            linear   ROD 28-APR-2025
DEFINITION  dedicator of cytokinesis protein 11 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001178689 XP_233283
VERSION     NP_001178689.1
DBSOURCE    REFSEQ: accession NM_001191760.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2073)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   2  (residues 1 to 2073)
  AUTHORS   Matsuda,T., Yanase,S., Takaoka,A. and Maruyama,M.
  TITLE     The immunosenescence-related gene Zizimin2 is associated with early
            bone marrow B cell development and marginal zone B cell formation
  JOURNAL   Immun Ageing 12, 1 (2015)
   PUBMED   25729399
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2073)
  AUTHORS   Sakabe,I., Asai,A., Iijima,J. and Maruyama,M.
  TITLE     Age-related guanine nucleotide exchange factor, mouse Zizimin2,
            induces filopodia in bone marrow-derived dendritic cells
  JOURNAL   Immun Ageing 9, 2 (2012)
   PUBMED   22494997
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2073)
  AUTHORS   Nishikimi,A., Meller,N., Uekawa,N., Isobe,K., Schwartz,M.A. and
            Maruyama,M.
  TITLE     Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide
            exchange factor expressed predominantly in lymphocytes
  JOURNAL   FEBS Lett 579 (5), 1039-1046 (2005)
   PUBMED   15710388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 17, 2010 this sequence version replaced XP_233283.3.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.65998.1,
                                           SRR26643284.21588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2073
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq34"
     Protein         1..2073
                     /product="dedicator of cytokinesis protein 11 isoform 1"
                     /note="dedicator of cytokinesis protein 11"
                     /calculated_mol_wt=237682
     Region          38..147
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          161..284
                     /region_name="PH_DOCK-D"
                     /note="Dedicator of cytokinesis-D subfamily Pleckstrin
                     homology (PH) domain; cd13267"
                     /db_xref="CDD:270087"
     Region          639..828
                     /region_name="C2_Dock-D"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08697"
                     /db_xref="CDD:176079"
     Region          1615..2027
                     /region_name="DHR2_DOCK11"
                     /note="Dock Homology Region 2, a GEF domain, of Class D
                     Dedicator of Cytokinesis 11; cd11700"
                     /db_xref="CDD:212573"
     Site            order(1720,1730,1732..1733,1735..1736,1739..1740,
                     1742..1743,1746..1747)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212573"
     Site            order(1754..1757,1788..1789,1791..1794,1796..1797,
                     1816..1818,1835,1837,1866,1868,1875..1876,1882,1884,
                     1921..1922,1925,1939,1941,1945,1948..1950,1953..1959,1962,
                     1990,2008..2009,2011..2012,2015)
                     /site_type="other"
                     /note="Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212573"
     Site            1953..1958
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212573"
     CDS             1..2073
                     /gene="Dock11"
                     /coded_by="NM_001191760.2:110..6331"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:313438"
                     /db_xref="RGD:1564707"
ORIGIN      
        1 maevrkftkr lskpgtaael rqsvseavrg svvlekaklv epldyenvit qrktqiysdp
       61 lrdllmfpme dislsvigrq lrtvqstvpe daekraqslf vkeciktyst dwhvvnykye
      121 dfsgdfrmlp ckslrpekip nhvfeidedc ekdedssslc sqkggvikqg wlhkanvnst
      181 itvtmkvfkr ryfyltqlpd gsyilnsykd eknskeskgc iyldacidvv qcpkmrrhaf
      241 elkmldkysh ylaaeteqem eewlitlkki iqintdslvq ekketveaiq eeetssqgka
      301 enimaslers mhpelmkygr eteqlnklsr gdgrqnlfsf dsevqrldfs giepdvkpfe
      361 ekcnkrflvn chdltfnilg higdnakgpp tnvepffitl alfdvknnck isadfhvdln
      421 ppsvremlwg mstqlandgn tkgsspesli hgiaesrlcy irqgifsvtn phpeiflvvr
      481 iekvlqgnit hcaepyikns dpiktaqkvh rtakqvcsrl gqyrmpfawa arpifkdlqg
      541 sldldgkfsp lykqdsskls nedilkllse ykkpektklq iipgqlnitv ecvpvdlpnc
      601 itssyvplkp fekncqnitv eveefvpemt kycypftiyk nhlyvyplql kydsqksfak
      661 arniavcvef rdsdesdtsa lkciygkpag svfttnayav vshhnqnpef ydeikielpi
      721 hlhqkhhllf tfyhvscein tkgttkkqdt vetpvgfawv pllkdgrvtt leqqlpvsan
      781 lppgylnvnd aesrrqsnad ikwvdgakpl lkikthlest iytqdlhvhk ffhhcqliqs
      841 gskevpgeli kylkclhame iqvmiqflpv ilmqlfrvlt nmtheddvpi nctmvllhiv
      901 skcheegles ylrsfikysf rpekpstlqa qlihetlatt miailkqsad flainkllky
      961 swfffeiiak smatylleen kiklprgqrf peayhhilhs lllaiiphvt iryaeipdes
     1021 rnvnyslasf lkrcltlmdr gfvfnlindy isgfspkdpk vlaeykfefl qticnhehyi
     1081 plnlpmafak pklqrvqdsn leyslsdeyc khhflvglll retsialqdn yeirytaisv
     1141 iknllikhaf dtryqhknqq akiaqlylpf vgllleniqr lagrdtlysc aampnsasrd
     1201 efpcgfvspt srgslatdke paygsfqngh gikredsrgs lipegatgfp dpgstgentr
     1261 qsssrtsvsq ynrldqyeir nllmcylyiv kmisedtllt ywnkvspqel inilvllevc
     1321 lfhfrymgkr niarvhdawl skhfgidrks qtmpalrnrs gvmqarlqhl sslessftln
     1381 hssatteadi fhqallegnt atevsltvld tisfftqcfk sqllnndghn plmkkvfdih
     1441 laflkngqse vslkhvfasl rsfiskfpsa ffkgrvnmca afcyevlkcc tskisstrne
     1501 asallyllmr nnfeytkrkt flrthlqiii avsqliadva lsggsrfqes lfiinnfans
     1561 drpmkatafp tevkdltkri rtvlmataqm kehekdpeml idlqyslaks yastpelrkt
     1621 wldsmakihi kngdfseaam cyvhvaalva eflhrkklfp sgcsafkkit pnideegamk
     1681 edagmmdvhy seevllelle qcvdglwkae ryeviseisk liipiyekrr efekltqvyr
     1741 tlhgaytkil evmhtkkrll gtffrvafyg qsffeeedgk eyiykepklt glseisfrlv
     1801 klygekfgte nikiiqdsdk vnakeldpkf ahiqvtyvkp yfddkelter ktefernhni
     1861 nrfvfeapyt lsgkkqgcie eqckrrtilt tsnsfpyvkk ripitceqqv nlkpidvatd
     1921 eikdktaelh klcssadvdm iqlqlklqgc vsvqvnagpl ayaraflnes qankyppkkv
     1981 nelkdmfrkf iqacsialel nerlikedqi eyheglksnf rdmvkelsdi iheqilqedt
     2041 mhspwmnntl hvfcaisgts snrgygspry sev
//
LOCUS       NP_001034426             569 aa            linear   ROD 28-APR-2025
DEFINITION  far upstream element-binding protein 3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001034426
VERSION     NP_001034426.2
DBSOURCE    REFSEQ: accession NM_001039337.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Zivraj,K.H., Rehbein,M., Olschlager-Schutt,J., Schob,C., Falley,K.,
            Buck,F., Schweizer,M., Schepis,A., Kremmer,E., Richter,D.,
            Kreienkamp,H.J. and Kindler,S.
  TITLE     The RNA-binding protein MARTA2 regulates dendritic targeting of
            MAP2 mRNAs in rat neurons
  JOURNAL   J Neurochem 124 (5), 670-684 (2013)
   PUBMED   23121659
  REMARK    GeneRIF: in neurons MARTA2 appears to represent a key trans-acting
            factor involved in dendritic targeting of MAP2 mRNAs.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Weber,A., Kristiansen,I., Johannsen,M., Oelrich,B., Scholmann,K.,
            Gunia,S., May,M., Meyer,H.A., Behnke,S., Moch,H. and Kristiansen,G.
  TITLE     The FUSE binding proteins FBP1 and FBP3 are potential c-myc
            regulators in renal, but not in prostate and bladder cancer
  JOURNAL   BMC Cancer 8, 369 (2008)
   PUBMED   19087307
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Davis-Smyth,T., Duncan,R.C., Zheng,T., Michelotti,G. and Levens,D.
  TITLE     The far upstream element-binding proteins comprise an ancient
            family of single-strand DNA-binding transactivators
  JOURNAL   J Biol Chem 271 (49), 31679-31687 (1996)
   PUBMED   8940189
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Wu,C., Narayan,P. and Puett,D.
  TITLE     Protein engineering of a novel constitutively active
            hormone-receptor complex
  JOURNAL   J Biol Chem 271 (49), 31638-31642 (1996)
   PUBMED   8940183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 26, 2024 this sequence version replaced NP_001034426.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ212354.1, SRR26643291.8636.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..569
                     /product="far upstream element-binding protein 3 isoform
                     b"
                     /note="MAP2 RNA trans-acting protein 2; far upstream
                     element (FUSE) binding protein 3"
                     /calculated_mol_wt=61306
     Region          78..148
                     /region_name="KH-I_FUBP3_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22480"
                     /db_xref="CDD:411908"
     Site            order(87,89..91,93..97,100..101,104..105,110..113)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411908"
     Region          159..241
                     /region_name="KH-I_FUBP3_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22483"
                     /db_xref="CDD:411911"
     Site            order(172,174..176,178..182,185..186,189..190,195..198)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411911"
     Region          252..321
                     /region_name="KH-I_FUBP3_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22486"
                     /db_xref="CDD:411914"
     Site            order(262..267,269..273,276..277,286,288..289,299)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411914"
     Region          356..424
                     /region_name="KH-I_FUBP3_rpt4"
                     /note="fourth type I K homology (KH) RNA-binding domain
                     found in far upstream element-binding protein 3 (FUBP3)
                     and similar proteins; cd22489"
                     /db_xref="CDD:411917"
     Site            order(363..364,366..368,370..371,373..374,377..378,382,
                     387,389..390,392,403)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411917"
     CDS             1..569
                     /gene="Fubp3"
                     /gene_synonym="Marta2"
                     /coded_by="NM_001039337.2:81..1790"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:362106"
                     /db_xref="RGD:1307004"
ORIGIN      
        1 maelvqgqsa pvglkaedfv dalhrvrqia akidsiphln nstplvdpsv ygygvqkrpl
       61 ddgvgnqlga lvhqravite efkvpdkmvg fiigrggeqi sriqaesgck iqiasessgi
      121 perpcvltgt pesieqakrl lgqivdrcrn gpgfhndidg nstiqellip askvglvigk
      181 ggetikqlqe rtgvkmvmiq dgplptgadk plritgdpfk vqqaremvle iirekdqadf
      241 rgvrsdftsr agggsievsv prfvvgivig rngemikkiq ndagvriqfk pddgispera
      301 aqvmgppdrc qhaariinel iltaqereil ggltgtrgrg rgrgdwsvgt pggiqeityt
      361 vpadkcglvi gkggeniksi nqqsgahvel qrnpppntdp nlriftirga pqqievarhl
      421 idekvggasl gaptafgqsp fsqppaaphq ntfpprafpn iaakvngnph stpvsgppaf
      481 ltqgwgstyq awqqptqqvp sqqsqpqnsq pdyskawedy ykkqghttsa apqassppdy
      541 tmawaeyyrq qaafygqtlg qaqahsqeq
//
LOCUS       NP_001424035            1223 aa            linear   ROD 28-APR-2025
DEFINITION  AF4/FMR2 family member 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424035 XP_006250694
VERSION     NP_001424035.1
DBSOURCE    REFSEQ: accession NM_001437106.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1223)
  AUTHORS   Luo,Z., Lin,C. and Shilatifard,A.
  TITLE     The super elongation complex (SEC) family in transcriptional
            control
  JOURNAL   Nat Rev Mol Cell Biol 13 (9), 543-547 (2012)
   PUBMED   22895430
  REMARK    Review article
REFERENCE   2  (residues 1 to 1223)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   3  (residues 1 to 1223)
  AUTHORS   Baskaran,K., Erfurth,F., Taborn,G., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A., Iannaccone,P.M. and Domer,P.H.
  TITLE     Cloning and developmental expression of the murine homolog of the
            acute leukemia proto-oncogene AF4
  JOURNAL   Oncogene 15 (16), 1967-1978 (1997)
   PUBMED   9365243
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Mar 27, 2025 this sequence version replaced XP_006250694.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1062085.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1223
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..1223
                     /product="AF4/FMR2 family member 1 isoform 1"
                     /note="myeloid/lymphoid or mixed-lineage leukemia
                     (trithorax homolog, Drosophila); translocated to, 2;
                     AF4/FMR2 family, member 1"
                     /calculated_mol_wt=131981
     Region          12..510
                     /region_name="AF-4"
                     /note="AF-4 proto-oncoprotein N-terminal region;
                     pfam05110"
                     /db_xref="CDD:461550"
     Region          771..785
                     /region_name="AF4_int"
                     /note="AF4 interaction motif; pfam18875"
                     /db_xref="CDD:436798"
     Region          960..1221
                     /region_name="AF-4_C"
                     /note="AF-4 proto-oncoprotein C-terminal region;
                     pfam18876"
                     /db_xref="CDD:465894"
     CDS             1..1223
                     /gene="Aff1"
                     /gene_synonym="Mllt2"
                     /coded_by="NM_001437106.1:228..3899"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305152"
                     /db_xref="RGD:1307940"
ORIGIN      
        1 mafkdsssss lynedrnllr irekerrnqe ahqekeafpe kaplfaepyk takgdelssr
       61 iqtmlgdyee mkeflssksh phrldgsedr pgkprypsch drgsgasgsf rthvyhqpth
      121 tsapgslsvs nvsqspkmaq prmepvpslh akiygapdgp rpaqdrlsqg hcsrkcdrra
      181 egdserklsp fisslpspvp plspahsrpq atskahgsgt gtqscyaskp skdpvvtaqe
      241 ketpldslva vtslgaappq ppcqtfpppp lpsksiamqq kptayvrpmd gqdqapsesp
      301 elkppledfg qqsfekpdlk vpakakltrl rmpsqtveqp ysnevhcvee ilkemthswp
      361 spltaihtps taepsrfpfp tkdplhissa tqsqkqydap skthpnpqqg tsmleddlql
      421 sdseesdveq avekppsppa ppsapqtipe pvasahsssa esessesdss sdsesessss
      481 dseeneplet qapepepptt nkwqldnwlt kvnqpsvple srgstesprc rqeskgggeg
      541 gsdqqhpdsk dpplkssska lrgpsegpqp gkrncpkspa qqetppprqt vgskqprkpt
      601 kgstqaeqpq assrvegeag pvaygskeqt skdkpkvktk grpravgsre pksevpvpvp
      661 qaavpkpqpp aptpiekrkh ksstapskal sgpqptkdsa gdrnqehpal vsltqsqgqp
      721 nsgrgsgggr tsgcrqavit qedscrdkll lplrdtklls plrdspppts lvvkitldll
      781 trvpqppgkg grprksehkq lpagkkqdle argcdsssrv tkkrkaepek ehshkrlrld
      841 ksqtssssss haessksktp rpssecsrke mlppppvvps ssssssssqk pskpahkrpr
      901 pdadigsqdp prssgstkss ctdssvpkhr kvqardsehk gssgdaanpf pvpslpngns
      961 kpgkpqvksd rqqadfhmke akklkckaea mvdkagkafk yleavlsfie cgmatesess
     1021 aksaytvyse tvdlikfvms lksfsdntvp aqekifavlc lrcqsllnma mfrckkdtvm
     1081 kysrtlsehf rstskvaqap spcvarstgv pspvspmpsp assagsqtsa gssmgamgat
     1141 atvstpvtiq nmtssyvtit shvlkaftlw eqaealtrkn keffaqlstk vrvlalnssl
     1201 vdlvhytrqg lqrlrqapqt plm
//
LOCUS       NP_001416378             776 aa            linear   ROD 28-APR-2025
DEFINITION  junctional cadherin complex regulator isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001416378 XP_038938253
VERSION     NP_001416378.1
DBSOURCE    REFSEQ: accession NM_001429449.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Appelbe,O.K., Bollman,B., Attarwala,A., Triebes,L.A.,
            Muniz-Talavera,H., Curry,D.J. and Schmidt,J.V.
  TITLE     Disruption of the mouse Jhy gene causes abnormal ciliary
            microtubule patterning and juvenile hydrocephalus
  JOURNAL   Dev Biol 382 (1), 172-185 (2013)
   PUBMED   23906841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038938253.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.29824.1,
                                           SRR26360186.1874073.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..776
                     /product="junctional cadherin complex regulator isoform 1"
                     /note="juvenile hydrocephalus; uncharacterized protein
                     C11orf63 homolog; jhy protein homolog"
                     /calculated_mol_wt=88432
     Region          654..773
                     /region_name="JHY"
                     /note="Jhy protein; pfam15261"
                     /db_xref="CDD:464601"
     CDS             1..776
                     /gene="Jhy"
                     /gene_synonym="RGD1309108"
                     /coded_by="NM_001429449.1:66..2396"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315578"
                     /db_xref="RGD:1309108"
ORIGIN      
        1 mplwmnkykp vpkrssrspv hhtnlrtpps grafkeedfn liskdslesd seslpreakf
       61 wsdikdqiqd kdmepdslee dssseteeaa hgtnreglga qgaganhshh qvedkysdlr
      121 ydpnwknkke egqllaveal pesadsssdn lpgaplypsr epsmrlsvgk gkekrspqse
      181 asllgsefls pkyecgtrqn effselsdsd qedqeekssd lspylkssss hnevflpgsr
      241 gprrrksrqy fveknkltlg lpapktdsyl qlhnkkrget rleqisypir dagkmtvqdd
      301 kgventfmdp edkwhqrakq lknyqehlsq cedtksgnvp rgqssnaanv qqpsrrtaka
      361 rvqkqkkyqn glkslgtkeq vvsqnnqnns lqqpqtqrlp mdtsskhepa aqmtasnpnl
      421 qdprtlthnp kvtsdpffpp ketfdrvvyk nsvlglntnk rrghrykeek rilyqqqpiy
      481 ifsdgdlqdf nelshrhesl sqrgpqsdyr mnthrsrstk tkkpskepea etkyknieml
      541 wklhsssdme pvsaspdsrl aqimeqhqqa llqlaevqps egslsstvfp pilsrveses
      601 qldsershkh qmrmarsnse gyllqlekgk rhrkrsqsrt kssklkgyqk rdvklgglgp
      661 dfasirdkmq tllqqkeyak qvkeynmktl svlskpqtsk tdskstisrk kaldyaktip
      721 kpkppnlpyq tmkktnnskh sekegslpei slleilqsrh erekqavaaf kvlhiv
//
LOCUS       NP_073169                522 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger and BTB domain-containing protein 18 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_073169 XP_008768022
VERSION     NP_073169.2
DBSOURCE    REFSEQ: accession NM_022678.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Yang,H., Zhang,Z., Ding,X., Jiang,X., Tan,L., Lin,C., Xu,L., Li,G.,
            Lu,L., Qin,Z., Feng,X. and Li,M.
  TITLE     RP58 knockdown contributes to hypoxia-ischemia-induced pineal
            dysfunction and circadian rhythm disruption in neonatal rats
  JOURNAL   J Pineal Res 75 (1), e12885 (2023)
   PUBMED   37183291
  REMARK    GeneRIF: RP58 knockdown contributes to hypoxia-ischemia-induced
            pineal dysfunction and circadian rhythm disruption in neonatal
            rats.
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Enzo,E., Santinon,G., Pocaterra,A., Aragona,M., Bresolin,S.,
            Forcato,M., Grifoni,D., Pession,A., Zanconato,F., Guzzo,G.,
            Bicciato,S. and Dupont,S.
  TITLE     Aerobic glycolysis tunes YAP/TAZ transcriptional activity
  JOURNAL   EMBO J 34 (10), 1349-1370 (2015)
   PUBMED   25796446
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Yokoyama,S., Ito,Y., Ueno-Kudoh,H., Shimizu,H., Uchibe,K.,
            Albini,S., Mitsuoka,K., Miyaki,S., Kiso,M., Nagai,A., Hikata,T.,
            Osada,T., Fukuda,N., Yamashita,S., Harada,D., Mezzano,V., Kasai,M.,
            Puri,P.L., Hayashizaki,Y., Okado,H., Hashimoto,M. and Asahara,H.
  TITLE     A systems approach reveals that the myogenesis genome network is
            regulated by the transcriptional repressor RP58
  JOURNAL   Dev Cell 17 (6), 836-848 (2009)
   PUBMED   20059953
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Okado,H., Ohtaka-Maruyama,C., Sugitani,Y., Fukuda,Y., Ishida,R.,
            Hirai,S., Miwa,A., Takahashi,A., Aoki,K., Mochida,K., Suzuki,O.,
            Honda,T., Nakajima,K., Ogawa,M., Terashima,T., Matsuda,J.,
            Kawano,H. and Kasai,M.
  TITLE     The transcriptional repressor RP58 is crucial for cell-division
            patterning and neuronal survival in the developing cortex
  JOURNAL   Dev Biol 331 (2), 140-151 (2009)
   PUBMED   19409883
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Takahashi,A., Hirai,S., Ohtaka-Maruyama,C., Miwa,A., Hata,Y.,
            Okabe,S. and Okado,H.
  TITLE     Co-localization of a novel transcriptional repressor simiRP58 with
            RP58
  JOURNAL   Biochem Biophys Res Commun 368 (3), 637-642 (2008)
   PUBMED   18262495
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Kang,J.S., Yang,Y.C., Liu,H.L., Li,Y.H., Du,Y.C. and Li,R.X.
  TITLE     Cloning and Distribution of rRP58, A Novel Neuronal Gene
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 33 (5),
            563-568 (2001)
   PUBMED   12040400
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Meng,G., Inazawa,J., Ishida,R., Tokura,K., Nakahara,K., Aoki,K. and
            Kasai,M.
  TITLE     Structural analysis of the gene encoding RP58, a sequence-specific
            transrepressor associated with heterochromatin
  JOURNAL   Gene 242 (1-2), 59-64 (2000)
   PUBMED   10721697
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Aoki,K., Meng,G., Suzuki,K., Takashi,T., Kameoka,Y., Nakahara,K.,
            Ishida,R. and Kasai,M.
  TITLE     RP58 associates with condensed chromatin and mediates a
            sequence-specific transcriptional repression
  JOURNAL   J Biol Chem 273 (41), 26698-26704 (1998)
   PUBMED   9756912
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Feb 7, 2022 this sequence version replaced
            XP_008768022.1, NP_073169.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.867097.1,
                                           SRR26360194.2358628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q25"
     Protein         1..522
                     /product="zinc finger and BTB domain-containing protein 18
                     isoform 1"
                     /note="rRP58; 58 kDa repressor protein; zinc finger
                     protein 238; transcriptional repressor RP58; zinc finger
                     and BTB domain-containing protein 18"
                     /calculated_mol_wt=58182
     Region          1..147
                     /region_name="BTB_POZ_ZBTB18_RP58"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 18 (ZBTB18); cd18324"
                     /db_xref="CDD:349633"
     Region          121..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKY3.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JKY3.1)"
     Region          310..427
                     /region_name="Interaction with DNMT3A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKY3.1)"
     Region          <351..>481
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(372,375,388,392)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(412,415,428,432)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(417,419,421,423..424,427..428,431,445,447,451..452,
                     455..456,459,473,475,477,479..480,483..484)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          425..447
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          440..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          468..486
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99592; propagated from
                     UniProtKB/Swiss-Prot (Q9JKY3.1)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99592; propagated from
                     UniProtKB/Swiss-Prot (Q9JKY3.1)"
     CDS             1..522
                     /gene="Zbtb18"
                     /gene_synonym="Rp58; Zfp238; Znf238"
                     /coded_by="NM_022678.2:285..1853"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64619"
                     /db_xref="RGD:621548"
ORIGIN      
        1 mefpdhsrhl lqclseqrhq gflcdctvlv gdaqfrahra vlascsmyfh lfykdqldkr
       61 divhlnsdiv tapafallle fmyegklqfk dlpiedvlaa asylhmydiv kvckkklkek
      121 atteadstkk eedasscsdk veslsdgssh magdlpsded egeddklnil pskrdlaaep
      181 gnmwmrlpsd aagipqagge aephataagk tvaspcsste slsqrsvtsv rdsadvdcvl
      241 dlsvksslsg venlnssyfs sqdvlrsnlv qvkvekeasc desdvgtndy dmehstvkes
      301 vsannrvqye pahlaplred svlreldred kasddemmtp eservqvegg messllpyvs
      361 nilspagqif mcplcnkvfp sphilqihls thfreqdgir skpaadvnvp tcslcgktfs
      421 cmytlkrher thsgekpytc tqcgksfqys hnlsrhavvh trekphackw cerrftqsgd
      481 lyrhirkfhc elvnslsvks ealslptvrd wtledssqel wk
//
LOCUS       NP_001418972             984 aa            linear   ROD 28-APR-2025
DEFINITION  similar to WD repeat domain 59 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001418972 XP_038954183
VERSION     NP_001418972.1
DBSOURCE    REFSEQ: accession NM_001432043.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 984)
  AUTHORS   Wolfson,R.L., Chantranupong,L., Wyant,G.A., Gu,X., Orozco,J.M.,
            Shen,K., Condon,K.J., Petri,S., Kedir,J., Scaria,S.M.,
            Abu-Remaileh,M., Frankel,W.N. and Sabatini,D.M.
  TITLE     KICSTOR recruits GATOR1 to the lysosome and is necessary for
            nutrients to regulate mTORC1
  JOURNAL   Nature 543 (7645), 438-442 (2017)
   PUBMED   28199306
REFERENCE   2  (residues 1 to 984)
  AUTHORS   Bar-Peled,L. and Sabatini,D.M.
  TITLE     Regulation of mTORC1 by amino acids
  JOURNAL   Trends Cell Biol 24 (7), 400-406 (2014)
   PUBMED   24698685
  REMARK    Review article
REFERENCE   3  (residues 1 to 984)
  AUTHORS   Bar-Peled,L., Chantranupong,L., Cherniack,A.D., Chen,W.W.,
            Ottina,K.A., Grabiner,B.C., Spear,E.D., Carter,S.L., Meyerson,M.
            and Sabatini,D.M.
  TITLE     A Tumor suppressor complex with GAP activity for the Rag GTPases
            that signal amino acid sufficiency to mTORC1
  JOURNAL   Science 340 (6136), 1100-1106 (2013)
   PUBMED   23723238
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On Jul 27, 2024 this sequence version replaced XP_038954183.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.42788.1,
                                           SRR26643290.53076.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..984
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..984
                     /product="similar to WD repeat domain 59 isoform 1"
                     /note="WD repeat-containing protein 59; GATOR complex
                     protein WDR59; GATOR2 complex protein WDR59"
                     /calculated_mol_wt=110778
     Region          <46..137
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          62..103
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          100..>343
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          109..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          154..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..229
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          237..279
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..316
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          401..501
                     /region_name="RWD"
                     /note="domain in RING finger and WD repeat containing
                     proteins and DEXDc-like helicases subfamily related to the
                     UBCc domain; smart00591"
                     /db_xref="CDD:214735"
     Region          932..978
                     /region_name="mRING-H2-C3H3C2_WDR59"
                     /note="Modified RING finger, H2 subclass (C3H3C2-type),
                     found in WD repeat-containing protein 59 (WDR59) and
                     similar proteins; cd16692"
                     /db_xref="CDD:438353"
     CDS             1..984
                     /gene="Wdr59"
                     /coded_by="NM_001432043.1:96..3050"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:690751"
                     /db_xref="RGD:1592213"
ORIGIN      
        1 maarwssenv vvefrdsqat amsvdcvgqh avlsgrrfly ivnldapfeg hrkisrqskw
       61 digavqwnph dsfahyfaas snqrvdlykw kdgsgevgtt lqghtrvisd ldwavfepdl
      121 lvtssvdtyi yiwdikdtrk pavalsavag asqvkwnkkn anylatshdg dvriwdkrkp
      181 staveylaah lskihgldwh pdsehifats sqdnsvkfwd yrqprkylni lpcqvpvwka
      241 rytpfsnglv tvmvpqlrre nslllwnvfd lntpvhtfvg hddvvlefqw rrqkegskdy
      301 qlvtwsrdqt lrmwrvdyqm qrlcandild gvdefiesis llpepektlh pqdtdhqpsl
      361 shgeedgnvt dvlaikedpp sslleerrsd qlglpqtlqq efslinvqir nvnvemdaad
      421 rsctvsvhcs nhrvkmlvtf paqypnnaap sfqfinptti tsavkakllk ilkdtslqkv
      481 krnqsclepc lrqlvscles fvnqedsass npfalpnsvt pplptfarvt taygsyqdan
      541 ipfprtsgar fcgagylvyf trpmtmhrav spteptprsl salsayhtgl iapmkirtea
      601 pgnlrlysgs ptrsekeqvs issfyykerk srrwkskreg sdsgnrpika agkviiqdvs
      661 cllpvhkslg elyilnvndt qetcqknats amlvgrkdlv qvwslatvat dlclgpksdp
      721 dletpwarhp fgrqllesll ahycrlrdvq tlamlcsvfe aqsrpqglpn pfgpfpnrss
      781 nfvvshsryp sftssgscss msdpgfntgg wsivslagre tehisspwge sspeelrfgs
      841 ltysdprere rdqhdknkrl ldpantqqfd dfkkcygeil yrwglrekra evlkfvscpp
      901 dphkgiefgv ycshcrsevr gtqcaickgf tfqcaichva vrgssnfclt cghgghtshm
      961 mewfrtqevc ptgcgchcll estf
//
LOCUS       NP_001416981             504 aa            linear   ROD 28-APR-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 3
            isoform 3 [Rattus norvegicus].
ACCESSION   NP_001416981 XP_038946622
VERSION     NP_001416981.1
DBSOURCE    REFSEQ: accession NM_001430052.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Rai,A.K., Chen,J.X., Selbach,M. and Pelkmans,L.
  TITLE     Kinase-controlled phase transition of membraneless organelles in
            mitosis
  JOURNAL   Nature 559 (7713), 211-216 (2018)
   PUBMED   29973724
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kim,K., Cha,J.S., Cho,Y.S., Kim,H., Chang,N., Kim,H.J. and Cho,H.S.
  TITLE     Crystal Structure of Human Dual-Specificity Tyrosine-Regulated
            Kinase 3 Reveals New Structural Features and Insights into its
            Auto-phosphorylation
  JOURNAL   J Mol Biol 430 (10), 1521-1530 (2018)
   PUBMED   29634919
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Wippich,F., Bodenmiller,B., Trajkovska,M.G., Wanka,S., Aebersold,R.
            and Pelkmans,L.
  TITLE     Dual specificity kinase DYRK3 couples stress granule
            condensation/dissolution to mTORC1 signaling
  JOURNAL   Cell 152 (4), 791-805 (2013)
   PUBMED   23415227
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Guo,X., Williams,J.G., Schug,T.T. and Li,X.
  TITLE     DYRK1A and DYRK3 promote cell survival through phosphorylation and
            activation of SIRT1
  JOURNAL   J Biol Chem 285 (17), 13223-13232 (2010)
   PUBMED   20167603
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Wojchowski,D.M., Menon,M.P., Sathyanarayana,P., Fang,J., Karur,V.,
            Houde,E., Kapelle,W. and Bogachev,O.
  TITLE     Erythropoietin-dependent erythropoiesis: New insights and questions
  JOURNAL   Blood Cells Mol Dis 36 (2), 232-238 (2006)
   PUBMED   16524748
  REMARK    Review article
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Li,K., Zhao,S., Karur,V. and Wojchowski,D.M.
  TITLE     DYRK3 activation, engagement of protein kinase A/cAMP response
            element-binding protein, and modulation of progenitor cell survival
  JOURNAL   J Biol Chem 277 (49), 47052-47060 (2002)
   PUBMED   12356771
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Lord,K.A., Creasy,C.L., King,A.G., King,C., Burns,B.M., Lee,J.C.
            and Dillon,S.B.
  TITLE     REDK, a novel human regulatory erythroid kinase
  JOURNAL   Blood 95 (9), 2838-2846 (2000)
   PUBMED   10779429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On May 3, 2024 this sequence version replaced XP_038946622.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.3326465.1,
                                           SRR26643293.53131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..504
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 3 isoform 3"
                     /EC_number="2.7.12.1"
                     /note="dual-specificity tyrosine-(Y)-phosphorylation
                     regulated kinase 3"
                     /calculated_mol_wt=56496
     Region          60..439
                     /region_name="PKc_DYRK2_3"
                     /note="Catalytic domain of the protein kinases,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinases 2 and 3; cd14224"
                     /db_xref="CDD:271126"
     Site            order(132..136,140,153,155,169,189,205..208,211,213..214,
                     252,254,256..257,259,272,275,284,286..289,291,328)
                     /site_type="active"
                     /db_xref="CDD:271126"
     Site            order(132..136,140,153,155,189,205..208,211,252,254,
                     256..257,259,272)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271126"
     Site            order(169,213,252,254,275,284,286..289,291,328)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271126"
     Site            271..291
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271126"
     CDS             1..504
                     /gene="Dyrk3"
                     /coded_by="NM_001430052.1:327..1841"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:304775"
                     /db_xref="RGD:1310924"
ORIGIN      
        1 mkveqlfqef gsrrtstlqs dgvsnsekss pasqgkssds lgtvkcslss rpskvlpltp
       61 eqalkqykhh ltayekleii sypeiyfvgp nakkrqgvig gpnnggydda dgayihvprd
      121 hlayryevlk iigkgsfgqv arvydhklrq yvalkmvrne krfhrqaaee irilehlkkq
      181 dktgsmnvih mlesftfrnh vcmafellsi dlyelikknk fqgfsvqlvr kfaqsilqsl
      241 dalhknkiih cdlkpenill khhgrsatkv idfgsscfey qklytyiqsr fyrapeiilg
      301 crystpidiw sfgcilaell tgqplfpged egdqlacmme llgmppqkll eqskrakyfi
      361 nskglprycs vttqtdgrvv llggrsrrgk krgppgskdw aaalkgcddy lfieflkrcl
      421 qwdpsarltp aqalrhpwis ksaprplttd kvsgkrvvnp tnafqglgsk lppvvgiask
      481 lkanlmsets gsiplcsvlp klis
//
LOCUS       NP_001420836            1015 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-like GTPase OPA1, mitochondrial isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001420836 XP_006248559
VERSION     NP_001420836.1
DBSOURCE    REFSEQ: accession NM_001433907.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Kaur,H., Carrillo,O., Garcia,I., Ramos,I., St Vallier,S., De La
            Torre,P., Lopez,A., Keniry,M., Bazan,D., Elizondo,J., Grishma,K.C.,
            Ann MacMillan-Crow,L. and Gilkerson,R.
  TITLE     Differentiation activates mitochondrial OPA1 processing in myoblast
            cell lines
  JOURNAL   Mitochondrion 78, 101933 (2024)
   PUBMED   38986925
  REMARK    GeneRIF: Differentiation activates mitochondrial OPA1 processing in
            myoblast cell lines.
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Chen,W., DU,H., Sha,Y., Zhou,Y., Liang,J., Chen,Y., Ma,Q., Wu,X.
            and Qian,G.
  TITLE     [Long noncoding RNA H19 promotes vascular calcification by
            repressing the Bax inhibitor 1/optic atrophy 1 pathway]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 43 (9), 1469-1475 (2023)
   PUBMED   37814860
  REMARK    GeneRIF: [Long noncoding RNA H19 promotes vascular calcification by
            repressing the Bax inhibitor 1/optic atrophy 1 pathway].
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Garcia,I., Calderon,F., la Torre,P., Vallier,S.S., Rodriguez,C.,
            Agarwala,D., Keniry,M., Innis-Whitehouse,W. and Gilkerson,R.
  TITLE     Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts
  JOURNAL   Mitochondrion 57, 88-96 (2021)
   PUBMED   33383158
  REMARK    GeneRIF: Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts.
REFERENCE   4  (residues 1 to 1015)
  AUTHORS   Pang,Y., Qin,M., Hu,P., Ji,K., Xiao,R., Sun,N., Pan,X. and Zhang,X.
  TITLE     Resveratrol protects retinal ganglion cells against ischemia
            induced damage by increasing Opa1 expression
  JOURNAL   Int J Mol Med 46 (5), 1707-1720 (2020)
   PUBMED   32901846
  REMARK    GeneRIF: Resveratrol protects retinal ganglion cells against
            ischemia induced damage by increasing Opa1 expression.
REFERENCE   5  (residues 1 to 1015)
  AUTHORS   Rodriguez-Graciani,K.M., Chapa-Dubocq,X.R., MacMillan-Crow,L.A. and
            Javadov,S.
  TITLE     Association Between L-OPA1 Cleavage and Cardiac Dysfunction During
            Ischemia-Reperfusion Injury in Rats
  JOURNAL   Cell Physiol Biochem 54 (6), 1101-1114 (2020)
   PUBMED   33119220
  REMARK    GeneRIF: Association Between L-OPA1 Cleavage and Cardiac
            Dysfunction During Ischemia-Reperfusion Injury in Rats.
REFERENCE   6  (residues 1 to 1015)
  AUTHORS   Satoh,M., Hamamoto,T., Seo,N., Kagawa,Y. and Endo,H.
  TITLE     Differential sublocalization of the dynamin-related protein OPA1
            isoforms in mitochondria
  JOURNAL   Biochem Biophys Res Commun 300 (2), 482-493 (2003)
   PUBMED   12504110
REFERENCE   7  (residues 1 to 1015)
  AUTHORS   Misaka,T., Miyashita,T. and Kubo,Y.
  TITLE     Primary structure of a dynamin-related mouse mitochondrial GTPase
            and its distribution in brain, subcellular localization, and effect
            on mitochondrial morphology
  JOURNAL   J Biol Chem 277 (18), 15834-15842 (2002)
   PUBMED   11847212
REFERENCE   8  (residues 1 to 1015)
  AUTHORS   Aung,T., Ocaka,L., Ebenezer,N.D., Morris,A.G., Brice,G.,
            Child,A.H., Hitchings,R.A., Lehmann,O.J. and Bhattacharya,S.S.
  TITLE     Investigating the association between OPA1 polymorphisms and
            glaucoma: comparison between normal tension and high tension
            primary open angle glaucoma
  JOURNAL   Hum Genet 110 (5), 513-514 (2002)
   PUBMED   12073024
REFERENCE   9  (residues 1 to 1015)
  AUTHORS   Aung,T., Ocaka,L., Ebenezer,N.D., Morris,A.G., Krawczak,M.,
            Thiselton,D.L., Alexander,C., Votruba,M., Brice,G., Child,A.H.,
            Francis,P.J., Hitchings,R.A., Lehmann,O.J. and Bhattacharya,S.S.
  TITLE     A major marker for normal tension glaucoma: association with
            polymorphisms in the OPA1 gene
  JOURNAL   Hum Genet 110 (1), 52-56 (2002)
   PUBMED   11810296
REFERENCE   10 (residues 1 to 1015)
  AUTHORS   Alexander,C., Votruba,M., Pesch,U.E., Thiselton,D.L., Mayer,S.,
            Moore,A., Rodriguez,M., Kellner,U., Leo-Kottler,B., Auburger,G.,
            Bhattacharya,S.S. and Wissinger,B.
  TITLE     OPA1, encoding a dynamin-related GTPase, is mutated in autosomal
            dominant optic atrophy linked to chromosome 3q28
  JOURNAL   Nat Genet 26 (2), 211-215 (2000)
   PUBMED   11017080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Oct 10, 2024 this sequence version replaced XP_006248559.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.31224.1,
                                           SRR26643290.39660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..1015
                     /product="dynamin-like GTPase OPA1, mitochondrial isoform
                     1"
                     /EC_number="3.6.5.5"
                     /note="optic atrophy 1 (autosomal dominant); dynamin-like
                     120 kDa protein, mitochondrial; optic atrophy 1-like
                     protein; optic atrophy 1 homolog; mitochondrial OPA1;
                     optic atrophy protein 1 homolog; RN protein; dynamin-like
                     GTPase OPA1, mitochondrial"
                     /calculated_mol_wt=117319
     Region          342..616
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            350..357
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(351,353..358,371..372,378,453,523,525..526,557..561)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(352..353,457,470,495,497,499..502,504..505,526,
                     528..531,560..561)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            378
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            382..384
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            453..456
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(455..456,486..487)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            522..525
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Site            557..559
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          672..1015
                     /region_name="OPA1_C"
                     /note="Dynamin-like GTPase OPA1 C-terminal; pfam19434"
                     /db_xref="CDD:466080"
     CDS             1..1015
                     /gene="Opa1"
                     /coded_by="NM_001433907.1:148..3195"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171116"
                     /db_xref="RGD:708423"
ORIGIN      
        1 mwragraala cevcqslvkh ssgvqrnvpl qklhlvsrsi yrshhpalkl qrpqlrtsfq
       61 qfssltnlsl hklklsptky gyqprrnfwp arlaarllkl ryiilgsavg ggytakktfd
      121 ewkdmipdls dykwivpdfi weideyidle kirkalpsse dlanfapdld kiaeslsllk
      181 dfftagpklv sevieasepl lllgtpgeta fratdhgses dkhyrkgllg elillqqqiq
      241 eheeearraa gqystsyaqq krkvsdkeki dqlqeellht qlkyqriler lekenkelrk
      301 lvlqkddkgi hhrklkksli dmysevldvl sdydasyntq dhlprvvvvg dqsagktsvl
      361 emiaqarifp rgsgemmtrs pvkvtlsegp hhvalfkdss refdltkeed laalrheiel
      421 rmrknvkegc tvspetisln vkgpglqrmv lvdlpgvint vtsgmapdtk etifsiskay
      481 mqnpnaiilc iqdgsvdaer sivtdlvsqm dphgrrtifv ltkvdlaekn vaspsriqqi
      541 iegklfpmka lgyfavvtgk gnssesieai reyeeeffqn skllktsmlk ahqvttrnls
      601 lavsdcfwkm vresveqqad sfkatrfnle tewknnyprl reldrnelfe kakneildev
      661 islsqvtpkh weeilqqslw ervsthvien iylpaaqtmn sgtfnttvdi klkqwtdkql
      721 pnkavevawe tlqdefsrfm tepkgkehdd ifdklkeavk eesikrhkwn dfaedslrvi
      781 qhnaledrsi sdkqqwdaai yfmeealqgr lkdtenaien migpdwkkrw iywknrtqeq
      841 cvhnetknel ekmlkvndeh paylasdeit tvrknlesrg vevdpslikd twhqvyrrhf
      901 lktalnhcnl crrgfyyyqr hfidselecn dvvlfwriqr mlaitantlr qqltntevrr
      961 leknvkevle dfaedgekkv klltgkrvql aedlkkvrei qekldafiea lhqek
//
LOCUS       NP_001296289             334 aa            linear   ROD 28-APR-2025
DEFINITION  prostatic spermine-binding protein isoform 2 [Rattus norvegicus].
ACCESSION   NP_001296289 XP_008765769
VERSION     NP_001296289.1
DBSOURCE    REFSEQ: accession NM_001309360.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Anderegg,R.J., Carr,S.A., Huang,I.Y., Hiipakka,R.A., Chang,C.S. and
            Liao,S.T.
  TITLE     Correction of the cDNA-derived protein sequence of prostatic
            spermine binding protein: pivotal role of tandem mass spectrometry
            in sequence analysis
  JOURNAL   Biochemistry 27 (12), 4214-4221 (1988)
   PUBMED   3166977
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Chang,C.S., Saltzman,A.G., Hiipakka,R.A., Huang,I.Y. and Liao,S.S.
  TITLE     Prostatic spermine-binding protein. Cloning and nucleotide sequence
            of cDNA, amino acid sequence, and androgenic control of mRNA level
  JOURNAL   J Biol Chem 262 (6), 2826-2831 (1987)
   PUBMED   3818623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 29, 2015 this sequence version replaced XP_008765769.1.
            
            Transcript Variant: This variant (2) contains an alternate exon in
            the 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is longer than
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02675.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..334
                     /product="prostatic spermine-binding protein isoform 2"
                     /note="prostatic spermine-binding protein; zymogen granule
                     protein 16B"
                     /calculated_mol_wt=37072
     Region          <110..205
                     /region_name="Jacalin_ZG16_like"
                     /note="Jacalin-like lectin domain of the zymogen granule
                     protein 16 and related proteins; cd09611"
                     /db_xref="CDD:187707"
     CDS             1..334
                     /gene="Sbp"
                     /gene_synonym="Zg16b"
                     /coded_by="NM_001309360.1:40..1044"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25540"
                     /db_xref="RGD:3623"
ORIGIN      
        1 mvqvfwsylw rvsapqmtps saeggrkmea ggcvcgkhnv erysdwdsls llapkailtv
       61 svcllwrasq kshhlpaask cqivphtlrs haavgdpgsp crshlqspdi qlrfggnwsd
      121 vygsrslkyk eflledgehv tqvsgtrklc ltslsfttnk grvvtfgvrr glsfnesggs
      181 dkylvtvngl yapglclngm gfkwknihdd fddndddked dddehdddne edhgdkdndk
      241 dhdddhdddd ddkeddneed vdderddkdd deeeddndke ndkddgegsg ddddnddedd
      301 dkdddggsgn ddddgddded ddggdddngd eeee
//
LOCUS       NP_001376196             909 aa            linear   ROD 28-APR-2025
DEFINITION  whirlin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001376196
VERSION     NP_001376196.1
DBSOURCE    REFSEQ: accession NM_001389267.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Ebrahim,S., Ingham,N.J., Lewis,M.A., Rogers,M.J.C., Cui,R.,
            Kachar,B., Pass,J.C. and Steel,K.P.
  TITLE     Alternative Splice Forms Influence Functions of Whirlin in
            Mechanosensory Hair Cell Stereocilia
  JOURNAL   Cell Rep 15 (5), 935-943 (2016)
   PUBMED   27117407
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Ciardo,M.G., Andres-Borderia,A., Cuesta,N., Valente,P.,
            Camprubi-Robles,M., Yang,J., Planells-Cases,R. and
            Ferrer-Montiel,A.
  TITLE     Whirlin increases TRPV1 channel expression and cellular stability
  JOURNAL   Biochim Biophys Acta 1863 (1), 115-127 (2016)
   PUBMED   26516054
  REMARK    GeneRIF: findings indicate that Whirlin and TRPV1 are associated in
            a subset of nociceptors and that TRPV1 protein stability is
            increased through the interaction with the cytoskeletal scaffold
            protein.
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Chen,Q., Zou,J., Shen,Z., Zhang,W. and Yang,J.
  TITLE     Whirlin and PDZ domain-containing 7 (PDZD7) proteins are both
            required to form the quaternary protein complex associated with
            Usher syndrome type 2
  JOURNAL   J Biol Chem 289 (52), 36070-36088 (2014)
   PUBMED   25406310
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Zou,J., Zheng,T., Ren,C., Askew,C., Liu,X.P., Pan,B., Holt,J.R.,
            Wang,Y. and Yang,J.
  TITLE     Deletion of PDZD7 disrupts the Usher syndrome type 2 protein
            complex in cochlear hair cells and causes hearing loss in mice
  JOURNAL   Hum Mol Genet 23 (9), 2374-2390 (2014)
   PUBMED   24334608
REFERENCE   5  (residues 1 to 909)
  AUTHORS   Green,J.A., Yang,J., Grati,M., Kachar,B. and Bhat,M.A.
  TITLE     Whirlin, a cytoskeletal scaffolding protein, stabilizes the
            paranodal region and axonal cytoskeleton in myelinated axons
  JOURNAL   BMC Neurosci 14, 96 (2013)
   PUBMED   24011083
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 909)
  AUTHORS   Kikkawa,Y., Mburu,P., Morse,S., Kominami,R., Townsend,S. and
            Brown,S.D.
  TITLE     Mutant analysis reveals whirlin as a dynamic organizer in the
            growing hair cell stereocilium
  JOURNAL   Hum Mol Genet 14 (3), 391-400 (2005)
   PUBMED   15590699
REFERENCE   7  (residues 1 to 909)
  AUTHORS   Delprat,B., Michel,V., Goodyear,R., Yamasaki,Y., Michalski,N.,
            El-Amraoui,A., Perfettini,I., Legrain,P., Richardson,G.,
            Hardelin,J.P. and Petit,C.
  TITLE     Myosin XVa and whirlin, two deafness gene products required for
            hair bundle growth, are located at the stereocilia tips and
            interact directly
  JOURNAL   Hum Mol Genet 14 (3), 401-410 (2005)
   PUBMED   15590698
REFERENCE   8  (residues 1 to 909)
  AUTHORS   Mburu,P., Mustapha,M., Varela,A., Weil,D., El-Amraoui,A.,
            Holme,R.H., Rump,A., Hardisty,R.E., Blanchard,S., Coimbra,R.S.,
            Perfettini,I., Parkinson,N., Mallon,A.M., Glenister,P.,
            Rogers,M.J., Paige,A.J., Moir,L., Clay,J., Rosenthal,A., Liu,X.Z.,
            Blanco,G., Steel,K.P., Petit,C. and Brown,S.D.
  TITLE     Defects in whirlin, a PDZ domain molecule involved in stereocilia
            elongation, cause deafness in the whirler mouse and families with
            DFNB31
  JOURNAL   Nat Genet 34 (4), 421-428 (2003)
   PUBMED   12833159
REFERENCE   9  (residues 1 to 909)
  AUTHORS   Yap,C.C., Liang,F., Yamazaki,Y., Muto,Y., Kishida,H., Hayashida,T.,
            Hashikawa,T. and Yano,R.
  TITLE     CIP98, a novel PDZ domain protein, is expressed in the central
            nervous system and interacts with calmodulin-dependent serine
            kinase
  JOURNAL   J Neurochem 85 (1), 123-134 (2003)
   PUBMED   12641734
  REMARK    GeneRIF: CIP98, a novel protein (98 kDa) consisting of three PDZ
            domains and a proline-rich region, is widely expressed in the
            central nervous system and interacts with CASK
            (calmodulin-dependent serine kinase)
REFERENCE   10 (residues 1 to 909)
  AUTHORS   Holme,R.H., Kiernan,B.W., Brown,S.D. and Steel,K.P.
  TITLE     Elongation of hair cell stereocilia is defective in the mouse
            mutant whirler
  JOURNAL   J Comp Neurol 450 (1), 94-102 (2002)
   PUBMED   12124769
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.28215.1,
                                           SRR26643298.27558.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..909
                     /product="whirlin isoform 2"
                     /note="CASK-interacting protein CIP98; deafness, autosomal
                     recessive 31"
                     /calculated_mol_wt=96677
     Region          38..113
                     /region_name="HN_L-whirlin_R1_like"
                     /note="first harmonin_N_like domain (repeat 1) of the long
                     isoform of whirlin, and related domains; cd07356"
                     /db_xref="CDD:259822"
     Site            order(40,44,57,60,63..64,67)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259822"
     Region          139..220
                     /region_name="PDZ1_FL-whirlin"
                     /note="PDZ domain 1 of the full-length isoform of whirlin
                     and related domains; cd06740"
                     /db_xref="CDD:467222"
     Site            order(152..158,170,173,202,206,209..210)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467222"
     Region          241..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          276..359
                     /region_name="PDZ2_FL-whirlin"
                     /note="PDZ domain 2 of the full-length isoform of whirlin
                     and related domains; cd06741"
                     /db_xref="CDD:467223"
     Site            order(288..294,306,309,338,342,345..346)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467223"
     Region          418..498
                     /region_name="HN_L-whirlin_R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of the
                     long isoform of whirlin, and related domains; cd07357"
                     /db_xref="CDD:259823"
     Site            order(419,422,426,439,442,445..446,449)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259823"
     Region          502..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          550..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          619..719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P202; propagated from
                     UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          741..817
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810W9.1)"
     Region          816..906
                     /region_name="PDZ3_FL-whirlin-like"
                     /note="PDZ domain 3 of the full-length isoform of whirlin,
                     PDZ domain 1 of the short isoform of whirlin, and related
                     domains; cd06742"
                     /db_xref="CDD:467224"
     Site            order(827..833,846,849,879,883,886..887)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467224"
     CDS             1..909
                     /gene="Whrn"
                     /gene_synonym="Cip98; Dfnb31"
                     /coded_by="NM_001389267.1:752..3481"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:313255"
                     /db_xref="RGD:631330"
ORIGIN      
        1 mnaqldglsv sssstgslgs aaaaaggggg aglrllsanv rqlhqaltal lsepereqft
       61 hclnayharr nvfdlvrtlr vlldspvkrr llpmlrlvip rsdqllfdqy taeglylpat
      121 tpyrqpawaa pdgagpgevr lvslrrakah eglgfsirgg sehgvgiyvs lvepgslaek
      181 eglrvgdqil rvndkslarv thaeavkalk gskklvlsvy sagripggyv tnhiytwvdp
      241 qgrstsppss lphgstlrqh eddrrsalhl lqsgdekkvn lvlgdgrslg ltirggaeyg
      301 lgiyitgvdp gseaessglk vgdqilevng rsflsilhde avkllkssrh liltvkdvgr
      361 lpharttvdq tkwiassrig esitnsagfp gdlteegtnk pgfykgpags qvtlsslgnq
      421 trallddqar hllteqerat mmyyldqyrg gtisvealvm alfellntha kfsllsevrg
      481 iispqdldrf dhlvlrreie smkarqppgp gvgdtysmvs ysdtgsstgs hgtsttvssa
      541 rntldlegtg ettqgstnal pdvsvddvrs psedlpgikp pppppplaqg hdrllgqtrk
      601 pvredsapls saahsgivfs aprnrspppp pgiaptptpg pssardspss piyasishan
      661 pssrkpldth lalvnqhpig pfprvqspph lksppaeapg agaglpppsp sehadavgan
      721 qhfvlvevhr pdsepdvnev ralpqtrtas tlsqlsdsgq tlsedsgvda geteastsgr
      781 grqtantknk ngkelpqter ttegankppg lleptstlir vrksaatlgi aieggantrq
      841 plprivtiqr ggsahncgql kvghvilevn gqtlrgkehr eaarviaeaf ktkerdyidf
      901 lvtefnvml
//
LOCUS       NP_001387989             831 aa            linear   ROD 28-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 1 isoform 4
            [Rattus norvegicus].
ACCESSION   NP_001387989 XP_017454692
VERSION     NP_001387989.1
DBSOURCE    REFSEQ: accession NM_001401060.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Berg,J.M., Lee,C., Chen,L., Galvan,L., Cepeda,C., Chen,J.Y.,
            Penagarikano,O., Stein,J.L., Li,A., Oguro-Ando,A., Miller,J.A.,
            Vashisht,A.A., Starks,M.E., Kite,E.P., Tam,E., Gdalyahu,A.,
            Al-Sharif,N.B., Burkett,Z.D., White,S.A., Fears,S.C., Levine,M.S.,
            Wohlschlegel,J.A. and Geschwind,D.H.
  TITLE     JAKMIP1, a Novel Regulator of Neuronal Translation, Modulates
            Synaptic Function and Autistic-like Behaviors in Mouse
  JOURNAL   Neuron 88 (6), 1173-1191 (2015)
   PUBMED   26627310
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Vidal,R.L., Fuentes,P., Valenzuela,J.I., Alvarado-Diaz,C.P.,
            Ramirez,O.A., Kukuljan,M. and Couve,A.
  TITLE     RNA interference of Marlin-1/Jakmip1 results in abnormal
            morphogenesis and migration of cortical pyramidal neurons
  JOURNAL   Mol Cell Neurosci 51 (1-2), 1-11 (2012)
   PUBMED   22828129
  REMARK    GeneRIF: RNA interference of Marlin-1 in vivo results in abnormal
            migration and abnormal morphology of newborn pyramidal neurons
            during the formation of the cortex.
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Vidal,R.L., Valenzuela,J.I., Lujan,R. and Couve,A.
  TITLE     Cellular and subcellular localization of Marlin-1 in the brain
  JOURNAL   BMC Neurosci 10, 37 (2009)
   PUBMED   19386132
  REMARK    GeneRIF: Marlin-1 is enriched in restricted areas of the brain
            including olfactory bulb, cerebral cortex, hippocampus and
            cerebellum; it is abundant in dendrites and axons of hippocampal
            neurons, associated with microtubules at the ultrastructural level.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 831)
  AUTHORS   Vidal,R.L., Ramirez,A., Castro,M., Concha,I.I. and Couve,A.
  TITLE     Marlin-1 is expressed in testis and associates to the cytoskeleton
            and GABAB receptors
  JOURNAL   J Cell Biochem 103 (3), 886-895 (2008)
   PUBMED   17668444
  REMARK    GeneRIF: Our findings demonstrate that Marlin-1 associates with a
            microtubule fraction and with GABA(B) receptors in testis
            suggesting that the set of protein interactions of Marlin-1 are
            conserved in different tissues.
REFERENCE   5  (residues 1 to 831)
  AUTHORS   Nishimura,Y., Martin,C.L., Vazquez-Lopez,A., Spence,S.J.,
            Alvarez-Retuerto,A.I., Sigman,M., Steindler,C., Pellegrini,S.,
            Schanen,N.C., Warren,S.T. and Geschwind,D.H.
  TITLE     Genome-wide expression profiling of lymphoblastoid cell lines
            distinguishes different forms of autism and reveals shared pathways
  JOURNAL   Hum Mol Genet 16 (14), 1682-1698 (2007)
   PUBMED   17519220
REFERENCE   6  (residues 1 to 831)
  AUTHORS   Vidal,R.L., Ramirez,O.A., Sandoval,L., Koenig-Robert,R., Hartel,S.
            and Couve,A.
  TITLE     Marlin-1 and conventional kinesin link GABAB receptors to the
            cytoskeleton and regulate receptor transport
  JOURNAL   Mol Cell Neurosci 35 (3), 501-512 (2007)
   PUBMED   17532644
REFERENCE   7  (residues 1 to 831)
  AUTHORS   Couve,A., Restituito,S., Brandon,J.M., Charles,K.J., Bawagan,H.,
            Freeman,K.B., Pangalos,M.N., Calver,A.R. and Moss,S.J.
  TITLE     Marlin-1, a novel RNA-binding protein associates with GABA
            receptors
  JOURNAL   J Biol Chem 279 (14), 13934-13943 (2004)
   PUBMED   14718537
  REMARK    GeneRIF: Marlin-1 functions to regulate the cellular levels of
            GABA(B) R2 subunits, which may have significant effects on the
            production of functional GABA(B) receptor heterodimers.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 1, 2022 this sequence version replaced XP_017454692.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..831
                     /product="janus kinase and microtubule-interacting protein
                     1 isoform 4"
                     /note="multiple alpha helices and RNA-linker protein 1;
                     multiple coiled-coil GABABR1-binding protein"
                     /calculated_mol_wt=97120
     Region          1..365
                     /region_name="Mediates association with microtubules.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          <24..>607
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          415..612
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          452..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     CDS             1..831
                     /gene="Jakmip1"
                     /gene_synonym="Marlin-1; Marlin1"
                     /coded_by="NM_001401060.1:383..2878"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:305434"
                     /db_xref="RGD:1562401"
ORIGIN      
        1 mskkgrskge kpetetdsvq maneelrakl tniqiefqqe kskvgklrer lqeaklereq
       61 eqrrhtayis elkaklheek tkelqalrea lirqheqeaa rtakikegel qrlqatlnvl
      121 rdgaadkvkt alladareea rrtfdgerqr lqqeilelka arkqaeeals ncmqadkaka
      181 adlraayqah qdevhrikre cerdirrlmd eikgkervil alekelgvqa gqtqrlllqk
      241 ealdeqlvqv keaerhhssp krelppgigd maelmggqdq hmderdvrrf qlkiaelnsv
      301 irkledrntl ladernellk rsretevqlk plveknkrmn kknedllhsi qrmeeklksl
      361 trenvemkek lsaqaslkrh tslndlsltr deqeieflrl qvleqqhvid dlslererll
      421 rskrhrgksl kppkkhvvet ffgfdeesvd setlsetsyn tdrtdrtpat peedldettt
      481 reeadlrfcq ltreyqalqr ayallqeqvg gtldaerear treqlqadll rcqakiedle
      541 kllvekgqda awveekqvlm rtnqdlleki yrlemeenql ksemqdakdq nellefrvle
      601 leererrspa fnlqittfpe nnssalqlfc hqegvkgvni selmknldil gdngnlrnee
      661 qvaviqagtv lalcekwlkq iegteaaltq kmmdlekekd qfsrqkgyle qeldyrkeal
      721 dqaylkiqdl eatlynalqq epgrrasesl sasqredlqa avekvrrqll rqsrefdsqi
      781 lrermellqq aqqkiremeg klelqrrqlk eleekflflf lffslafilw p
//
LOCUS       NP_001041510             348 aa            linear   ROD 28-APR-2025
DEFINITION  RT1 class Ib, locus M5 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001041510 XP_001075560 XP_574715
VERSION     NP_001041510.2
DBSOURCE    REFSEQ: accession NM_001048045.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Acar,M., Cora,T., Tunc,R. and Acar,H.
  TITLE     HLA-B27 subtypes in Turkish patients with ankylosing spondylitis
            and healthy controls
  JOURNAL   Rheumatol Int 32 (10), 3103-3105 (2012)
   PUBMED   21927904
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Lambracht-Washington,D., Moore,Y.F., Wonigeit,K. and Lindahl,K.F.
  TITLE     Structure and expression of MHC class Ib genes of the central M
            region in rat and mouse: M4, M5, and M6
  JOURNAL   Immunogenetics 60 (3-4), 131-145 (2008)
   PUBMED   18324395
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Shankarkumar,U., Ghosh,K. and Mohanty,D.
  TITLE     Novel HLA B*2714 and B*2708 allele associations in seronegative
            spondarthritis patients and haemophilia patients with chronic
            synovitis in India
  JOURNAL   Tissue Antigens 62 (2), 175-178 (2003)
   PUBMED   12889998
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Gunther,E. and Walter,L.
  TITLE     The major histocompatibility complex of the rat (Rattus norvegicus)
  JOURNAL   Immunogenetics 53 (7), 520-542 (2001)
   PUBMED   11685465
  REMARK    Review article
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Gul,A., Uyar,F.A., Inanc,M., Ocal,L., Tugal-Tutkun,I., Aral,O.,
            Konice,M. and Saruhan-Direskeneli,G.
  TITLE     Lack of association of HLA-B*51 with a severe disease course in
            Behcet's disease
  JOURNAL   Rheumatology (Oxford) 40 (6), 668-672 (2001)
   PUBMED   11426025
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Orchard,T.R., Thiyagaraja,S., Welsh,K.I., Wordsworth,B.P., Hill
            Gaston,J.S. and Jewell,D.P.
  TITLE     Clinical phenotype is related to HLA genotype in the peripheral
            arthropathies of inflammatory bowel disease
  JOURNAL   Gastroenterology 118 (2), 274-278 (2000)
   PUBMED   10648455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883052.1.
            
            On Dec 3, 2009 this sequence version replaced NP_001041510.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region compared to variant 1. The resulting
            protein (isoform 2) is shorter but has the same N- and C-termini
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..348
                     /product="RT1 class Ib, locus M5 isoform 2 precursor"
                     /note="major histocompatibility complex, class I, F; MHC
                     class Ib antigen RT1.M5 long isoform; MHC class Ib antigen
                     RT1.M5 short isoform"
                     /calculated_mol_wt=37027
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2047
     Region          26..204
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Region          208..299
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          209..216
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          224..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(227,229,256..257,259..261,267,269)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(234..236,264,289)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          238..243
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          246..249
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          253..261
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          264..274
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          281..288
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          295..298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..348
                     /gene="RT1-M5"
                     /gene_synonym="Hla-f; RGD1560260; RT1.M5"
                     /coded_by="NM_001048045.2:1..1047"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:499400"
                     /db_xref="RGD:1595816"
ORIGIN      
        1 mgssvfsvll plllsrawal nqvgagihsl qffatavtqp ssrehsfifv gfvddtqflc
       61 ynnqgesqrm epralwvknm gpgywerqtr mvkdisknsl vnlreamsvy nhsedgthvf
      121 qcvsgcdvgp dglflrgheq haydgrdyla lnkdlhswta gdtaaqitrr kweeagvaeq
      181 rrtylkgecv eslrtyleig ketllgadpp kahvthhpsp egdntlrcwa lgfypsditl
      241 twqrdgedlt qdmelvetrp ggdgtfqkwa avvvpsgeeh rytccveheg lteplllkwd
      301 pskhtipimg itaglvflgv aftgavvaia mrkqrahler sdkyltwt
//
LOCUS       NP_001424616             742 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-1-like protein isoform 7 [Rattus norvegicus].
ACCESSION   NP_001424616 XP_038943821
VERSION     NP_001424616.1
DBSOURCE    REFSEQ: accession NM_001437687.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 742)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 742)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 742)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 742)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 742)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943821.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.67899.1,
                                           SRR26643299.49190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..742
                     /product="dynamin-1-like protein isoform 7"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=82256
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          23..302
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Region          32..39
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,146,216,218..219,245..249,252)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,150,163,188,190,192..195,197..198,219,
                     221..224,248..250)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          58..60
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          146..149
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            146..149
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(148..149,179..180)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          215..218
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            215..218
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          225..510
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          245..248
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            245..247
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          344..489
                     /region_name="Middle domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          448..691
                     /region_name="Interaction with GSK3B.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          502..569
                     /region_name="B domain.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Region          523..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            591
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            592
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:22745122; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            603
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K1M6; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00429; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:17301055,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK1 and PKA.
                     /evidence=ECO:0000269|PubMed:28463107; propagated from
                     UniProtKB/Swiss-Prot (O35303.1)"
     Region          646..736
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          660..674
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000250|UniProtKB:O00429"
                     /note="propagated from UniProtKB/Swiss-Prot (O35303.1)"
     CDS             1..742
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437687.1:135..2363"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengveaeew gkflhtknkl ytdfdeirqe ieneterisg
      121 nnkgvspepi hlkvfspnvv nltlvdlpgm tkvpvgdqpk dielqireli lrfisnpnsi
      181 ilavtaantd matsealkis revdpdgrrt lavitkldlm dagtdamdvl mgrvipvklg
      241 iigvvnrsql dinnkksvtd sirdeyaflq kkypslanrn gtkylartln rllmhhirdc
      301 lpelktrinv laaqyqslln sygepvddks atllqlitkf ateycntieg takyietsel
      361 cggaricyif hetfgrtles vdplgglnti diltairnat gprpalfvpe vsfellvkrq
      421 ikrleepslr cvelvheemq riiqhcsnys tqellrfpkl hdaivevvtc llrkrlpvtn
      481 emvhnlvaie layintkhpd fadacglmnn nieeqrrnrl arelpsavsr dksskvpsal
      541 apasqepspa asaeadgkli qdnrretknv asagggigdg grigdggqep ttgnwrgmlk
      601 tskaeellae ekskpipimp aspqkghavn lldvpvpvar klsareqrdc evierliksy
      661 flivrkniqd svpkavmhfl vnhvkdtlqs elvgqlykss llddlltese dmaqrrkeaa
      721 dmlkalqgas qiiaeireth lw
//
LOCUS       NP_660185                952 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 15 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_660185
VERSION     NP_660185.2
DBSOURCE    REFSEQ: accession NM_145184.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Zhang,T., Wang,L. and Chen,L.
  TITLE     Alleviative effect of microRNA-497 on diabetic neuropathic pain in
            rats in relation to decreased USP15
  JOURNAL   Cell Biol Toxicol 39 (5), 1-16 (2023)
   PUBMED   35478295
  REMARK    GeneRIF: Alleviative effect of microRNA-497 on diabetic neuropathic
            pain in rats in relation to decreased USP15.
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Wu,Z., Zhu,L., Nie,X., Wei,L. and Qi,Y.
  TITLE     USP15 promotes pulmonary vascular remodeling in pulmonary
            hypertension in a YAP1/TAZ-dependent manner
  JOURNAL   Exp Mol Med 55 (1), 183-195 (2023)
   PUBMED   36635430
  REMARK    GeneRIF: USP15 promotes pulmonary vascular remodeling in pulmonary
            hypertension in a YAP1/TAZ-dependent manner.
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Zhang,L., Gao,X., Qin,Z., Shi,X., Xu,K., Wang,S., Tang,M., Wang,W.,
            Gao,S., Zuo,L., Zhang,L. and Zhang,W.
  TITLE     USP15 participates in DBP-induced testicular oxidative stress
            injury through regulating the Keap1/Nrf2 signaling pathway
  JOURNAL   Sci Total Environ 783, 146898 (2021)
   PUBMED   34088152
  REMARK    GeneRIF: USP15 participates in DBP-induced testicular oxidative
            stress injury through regulating the Keap1/Nrf2 signaling pathway.
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Chen,X., Bao,G. and Liu,F.
  TITLE     Inhibition of USP15 Prevent Glutamate-Induced Oxidative Damage by
            Activating Nrf2/HO-1 Signaling Pathway in HT22 Cells
  JOURNAL   Cell Mol Neurobiol 40 (6), 999-1010 (2020)
   PUBMED   31933062
  REMARK    GeneRIF: Inhibition of USP15 Prevent Glutamate-Induced Oxidative
            Damage by Activating Nrf2/HO-1 Signaling Pathway in HT22 Cells.
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Nie,Z.Y., Yao,M., Yang,Z., Yang,L., Liu,X.J., Yu,J., Ma,Y.,
            Zhang,N., Zhang,X.Y., Liu,M.H., Jiang,L.L. and Luo,J.M.
  TITLE     De-regulated STAT5A/miR-202-5p/USP15/Caspase-6 regulatory axis
            suppresses CML cell apoptosis and contributes to Imatinib
            resistance
  JOURNAL   J Exp Clin Cancer Res 39 (1), 17 (2020)
   PUBMED   31952546
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Elliott,P.R., Liu,H., Pastok,M.W., Grossmann,G.J., Rigden,D.J.,
            Clague,M.J., Urbe,S. and Barsukov,I.L.
  TITLE     Structural variability of the ubiquitin specific protease DUSP-UBL
            double domains
  JOURNAL   FEBS Lett 585 (21), 3385-3390 (2011)
   PUBMED   22001210
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Inui,M., Manfrin,A., Mamidi,A., Martello,G., Morsut,L., Soligo,S.,
            Enzo,E., Moro,S., Polo,S., Dupont,S., Cordenonsi,M. and Piccolo,S.
  TITLE     USP15 is a deubiquitylating enzyme for receptor-activated SMADs
  JOURNAL   Nat Cell Biol 13 (11), 1368-1375 (2011)
   PUBMED   21947082
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Hetfeld,B.K., Helfrich,A., Kapelari,B., Scheel,H., Hofmann,K.,
            Guterman,A., Glickman,M., Schade,R., Kloetzel,P.M. and Dubiel,W.
  TITLE     The zinc finger of the CSN-associated deubiquitinating enzyme USP15
            is essential to rescue the E3 ligase Rbx1
  JOURNAL   Curr Biol 15 (13), 1217-1221 (2005)
   PUBMED   16005295
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Angelats,C., Wang,X.W., Jermiin,L.S., Copeland,N.G., Jenkins,N.A.
            and Baker,R.T.
  TITLE     Isolation and characterization of the mouse ubiquitin-specific
            protease Usp15
  JOURNAL   Mamm Genome 14 (1), 31-46 (2003)
   PUBMED   12532266
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Park,K.C., Choi,E.J., Min,S.W., Chung,S.S., Kim,H., Suzuki,T.,
            Tanaka,K. and Chung,C.H.
  TITLE     Tissue-specificity, functional characterization and subcellular
            localization of a rat ubiquitin-specific processing protease,
            UBP109, whose mRNA expression is developmentally regulated
  JOURNAL   Biochem J 349 (Pt 2), 443-453 (2000)
   PUBMED   10880343
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Oct 10, 2024 this sequence version replaced NP_660185.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.25338.1, AF106657.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..952
                     /product="ubiquitin carboxyl-terminal hydrolase 15 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 15; ubiquitin
                     specific protease 15; deubiquitinating enzyme Ubp109;
                     ubiquitin thioesterase 15; deubiquitinating enzyme 15;
                     ubiquitin-specific-processing protease 15; ubiquitin
                     carboxyl-terminal hydrolase of 109 kDa"
                     /calculated_mol_wt=109110
     Region          2..223
                     /region_name="Mediates interaction with SART3.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R085.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E8; propagated from
                     UniProtKB/Swiss-Prot (Q9R085.1)"
     Region          12..903
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5H1; propagated from
                     UniProtKB/Swiss-Prot (Q9R085.1)"
     Region          597..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R085.1)"
     Region          923..952
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R085.1)"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E8; propagated from
                     UniProtKB/Swiss-Prot (Q9R085.1)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y4E8; propagated from
                     UniProtKB/Swiss-Prot (Q9R085.1)"
     CDS             1..952
                     /gene="Usp15"
                     /gene_synonym="Ubp109"
                     /coded_by="NM_145184.2:68..2926"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171329"
                     /db_xref="RGD:628795"
ORIGIN      
        1 maeggaadld tqrsdiatll ktslrkgdtw ylvdsrwfkq wkkyvgfdsw dkyqmgdqnv
       61 ypgpidnsgl lkdgdaqslk ehlideldyi llptegwnkl vswytlmegq epiarkvveq
      121 gmfvkhckve vyltelklce ngnmnnvvtr rfskadtidt iekeirkifn ipdekearlw
      181 nkymsntfep lnkpdstiqd aglyqgqvlv ieqknedgtw prgpsapnvk nsnyclpsyt
      241 ayknydysep grnneqpglc glsnlgntcf mnsaiqclsn tpplteyfln dkyqeelnfd
      301 nplgmrgeia ksyaelikqm wsgkfsyvtp rafktqvgrf apqfsgyqqq dcqellafll
      361 dglhedlnri rkkpyiqlkd adgrpdkvva eeawenhlkr ndsiivdifh glfkstlvcp
      421 ecakisvtfd pfcyltlplp mkkerslevy lvrmdplakp mqykvivpki gnildlctal
      481 salsgvpadk mivtdiynhr fhrifamden lssimerddi yvfeininrt edtehvvipv
      541 clrekfrhss ythhtgsslf gqpflmavpr nntedklynl lllrmcryvk msteteetdg
      601 plrccedqni ngngpngihe egspsemetd epddessqdq elpsenensq sedsvggdnd
      661 senglcteet ckgqltghkk rlftfqfnnl gntdinyikd dtrhirfddr qlrldersfl
      721 aldwdpdlkk ryfdenaaed fekhesveyk ppkrpfvklk dcielfttke klgaedpwyc
      781 pnckehqqat kkldlwslpp vlvvhlkrfs ysrymrdkld tlvdfpisdl dmseflinpn
      841 agpcrynlia vsnhyggmgg ghytafaknk ddgkwyyfdd ssvstasedq ivskaayvlf
      901 yqrqdtfsgt gffpldretk gasaatgvpl esdedsndnd ndlenencmh tn
//
LOCUS       NP_775123                392 aa            linear   ROD 28-APR-2025
DEFINITION  B2 bradykinin receptor isoform 2 [Rattus norvegicus].
ACCESSION   NP_775123
VERSION     NP_775123.2
DBSOURCE    REFSEQ: accession NM_173100.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Shen,M., Yu,M., Qiu,C., Zhang,G., Li,J., Fang,W. and Wang,Q.
  TITLE     Myocardial angiogenesis induced by exercise training involves a
            regulatory mechanism mediated by kinin receptors
  JOURNAL   Clin Exp Hypertens 43 (5), 408-415 (2021)
   PUBMED   33687297
  REMARK    GeneRIF: Myocardial angiogenesis induced by exercise training
            involves a regulatory mechanism mediated by kinin receptors.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Dagher,O.K., Jaffa,M.A., Habib,A., Ziyadeh,F.N. and Jaffa,A.A.
  TITLE     Heteromerization fingerprints between bradykinin B2 and thromboxane
            TP receptors in native cells
  JOURNAL   PLoS One 14 (5), e0216908 (2019)
   PUBMED   31086419
  REMARK    GeneRIF: This is the first study that provides evidence supporting
            the existence of bradykinin receptor B2 - thromboxane TP receptors
            heteromerization fingerprints in primary cultured vascular smooth
            muscle cell.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Ma,Z., Dong,Q., Lyu,B., Wang,J., Quan,Y. and Gong,S.
  TITLE     The expression of bradykinin and its receptors in spinal cord
            ischemia-reperfusion injury rat model
  JOURNAL   Life Sci 218, 340-345 (2019)
   PUBMED   30580020
  REMARK    GeneRIF: High bradykinin receptor B2 expression is associated with
            spinal cord ischemia-reperfusion injury.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Sanguesa,G., Shaligram,S., Akther,F., Roglans,N., Laguna,J.C.,
            Rahimian,R. and Alegret,M.
  TITLE     Type of supplemented simple sugar, not merely calorie intake,
            determines adverse effects on metabolism and aortic function in
            female rats
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (2), H289-H304 (2017)
   PUBMED   27923787
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Siltari,A., Korpela,R. and Vapaatalo,H.
  TITLE     Bradykinin -induced vasodilatation: Role of age, ACE1-inhibitory
            peptide, mas- and bradykinin receptors
  JOURNAL   Peptides 85, 46-55 (2016)
   PUBMED   27628189
  REMARK    GeneRIF: Mas receptor antagonist abolished relaxation while
            bradykinin receptor antagonist only slightly reduced it, suggesting
            that bradykinin-induced vasorelaxation is regulated also by other
            mechanisms than the classical BR1/BR2 pathway.
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Feletou,M., Lonchampt,M., Robineau,P., Jamonneau,I., Thurieau,C.,
            Fauchere,J.L., Villa,P., Ghezzi,P., Prost,J.F. and Canet,E.
  TITLE     Effects of the bradykinin B2 receptor antagonist S 16118
            (p-guanidobenzoyl-[Hyp3,Thi5,D-Tic7,Oic8]bradykinin) in different
            in vivo animal models of inflammation
  JOURNAL   J Pharmacol Exp Ther 273 (3), 1078-1084 (1995)
   PUBMED   7791078
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Pesquero,J.B., Lindsey,C.J., Zeh,K., Paiva,A.C., Ganten,D. and
            Bader,M.
  TITLE     Molecular structure and expression of rat bradykinin B2 receptor
            gene. Evidence for alternative splicing
  JOURNAL   J Biol Chem 269 (43), 26920-26925 (1994)
   PUBMED   7929432
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Wang,D.Z., Ma,J.X., Chao,L. and Chao,J.
  TITLE     Molecular cloning and sequence analysis of rat bradykinin B2
            receptor gene
  JOURNAL   Biochim Biophys Acta 1219 (1), 171-174 (1994)
   PUBMED   8086459
REFERENCE   9  (residues 1 to 392)
  AUTHORS   McEachern,A.E., Shelton,E.R., Bhakta,S., Obernolte,R., Bach,C.,
            Zuppan,P., Fujisaki,J., Aldrich,R.W. and Jarnagin,K.
  TITLE     Expression cloning of a rat B2 bradykinin receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7724-7728 (1991)
   PUBMED   1715575
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Rajakulasingam,K., Polosa,R., Holgate,S.T. and Howarth,P.H.
  TITLE     Comparative nasal effects of bradykinin, kallidin and
            [Des-Arg9]-bradykinin in atopic rhinitic and normal volunteers
  JOURNAL   J Physiol 437, 577-587 (1991)
   PUBMED   1890650
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Jul 27, 2012 this sequence version replaced NP_775123.1.
            
            Transcript Variant: This variant (2) lacks an internal exon in the
            5' region, compared to variant 1. The resulting isoform (2) is
            shorter and has a distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.23971.1, X69681.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..392
                     /product="B2 bradykinin receptor isoform 2"
                     /note="B2 bradykinin receptor; B2R; BK-2 receptor;
                     bradykinin receptor, beta 2"
                     /calculated_mol_wt=44482
     Region          60..344
                     /region_name="7tmA_BK-2"
                     /note="bradykinin receptor B2, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15381"
                     /db_xref="CDD:320503"
     Region          60..86
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320503"
     Site            order(65,114,117..118,122,135,138..139,142,193,197,214,
                     284,287,319,323)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320503"
     Region          93..118
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320503"
     Region          131..161
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320503"
     Region          174..195
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320503"
     Region          222..251
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320503"
     Region          264..294
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320503"
     Region          312..337
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320503"
     CDS             1..392
                     /gene="Bdkrb2"
                     /gene_synonym="B2BKR; B2BRA"
                     /coded_by="NM_173100.3:133..1311"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25245"
                     /db_xref="RGD:2201"
ORIGIN      
        1 mhcswkrpvl lsvhepmptt aslgiemfni ttqalgsahn gtfsevncpd tewwswlnai
       61 qapflwvlfl laalenifvl svfclhktnc tvaeiylgnl aaadlilacg lpfwaitian
      121 nfdwlfgevl crvvntmiym nlyssicflm lvsidrylal vktmsmgrmr gvrwaklysl
      181 viwsctllls spmlvfrtmk dyreeghnvt acvivypsrs wevftnmlln lvgfllplsi
      241 itfctvrimq vlrnnemkkf kevqtekkat vlvlavlglf vlcwfpfqis tfldtllrlg
      301 vlsgcwnera vdivtqissy vaysnsclnp lvyvivgkrf rkksrevyqa icrkggcmge
      361 svqmensmgt lrtsisvdrq ihklqdwagn kq
//
LOCUS       NP_001417095            1161 aa            linear   ROD 28-APR-2025
DEFINITION  Fas binding factor 1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001417095 XP_063126246
VERSION     NP_001417095.1
DBSOURCE    REFSEQ: accession NM_001430166.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Ye,X., Zeng,H., Ning,G., Reiter,J.F. and Liu,A.
  TITLE     C2cd3 is critical for centriolar distal appendage assembly and
            ciliary vesicle docking in mammals
  JOURNAL   Proc Natl Acad Sci U S A 111 (6), 2164-2169 (2014)
   PUBMED   24469809
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Tanos,B.E., Yang,H.J., Soni,R., Wang,W.J., Macaluso,F.P.,
            Asara,J.M. and Tsou,M.F.
  TITLE     Centriole distal appendages promote membrane docking, leading to
            cilia initiation
  JOURNAL   Genes Dev 27 (2), 163-168 (2013)
   PUBMED   23348840
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 1161)
  AUTHORS   Sugimoto,M., Inoko,A., Shiromizu,T., Nakayama,M., Zou,P.,
            Yonemura,S., Hayashi,Y., Izawa,I., Sasoh,M., Uji,Y., Kaibuchi,K.,
            Kiyono,T. and Inagaki,M.
  TITLE     The keratin-binding protein Albatross regulates polarization of
            epithelial cells
  JOURNAL   J Cell Biol 183 (1), 19-28 (2008)
   PUBMED   18838552
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 7, 2024 this sequence version replaced XP_063126246.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.39825.1,
                                           SRR26643296.29077.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..1161
                     /product="Fas binding factor 1 isoform 3"
                     /note="Fas (TNFRSF6) binding factor 1"
                     /calculated_mol_wt=128835
     Region          <115..565
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <592..>1077
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1161
                     /gene="Fbf1"
                     /coded_by="NM_001430166.1:580..4065"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:287836"
                     /db_xref="RGD:1310662"
ORIGIN      
        1 msaaaaflpr hvkalkakkg lkgsiddvlg dllgddille kpvetashak dtssspqwls
       61 skakflpkds agglaaadae vssdsdadpq vflqnmkdld smdddlfgrm kshppsgkgt
      121 akasgkevps kpkpagtlta dekgdaiptk kpppassrfg lqykkfsfed fedplaglls
      181 deeeetakkp patesklapk spstaagqgp svpltpgdtp irkkeplfde gddimttlgf
      241 edspkaerkk agdqegplpa rskldellgr gtaakllprp gtgerrefkl dkkyqkpedk
      301 edswddeilt fgayqptvas segrqsrrqs vrflgeggpd lkgetlsfkq spppasspih
      361 prkggadwlg lkdddldlls pspvqkaqqe dsamtpsllp ptnqpsapep hsvptglpsa
      421 akppakgarp svkasqvssp kaseekeddw lshvisqkks qnlareertg pskdlnspgs
      481 rsqipasslp iastqvleqa sageasrptt qgiaavrpav tgapvswsqa ttvvpvddpk
      541 rgtasasgdf ssrepavyip hsqeptglsv piqtllpesm mqsllpgsgf qkqllaaqgq
      601 lqsstaqlqv ellqsqtkls eleaqvrkle lersqhrmll eslqqrhqad leliedahrs
      661 hvkvletsyq qreeqlrrek evlsaqhasy cqeaerarte lvaqhqrqma maeqekdqev
      721 arlrelqqas ilemrkdheh qlqrlkmlkd qeidavtsat shtrslngii eqmekfsssl
      781 ntlssrveas hvttsqerel girqqdeqlr alqerlgrqq rdmeeersrl qevigkmevr
      841 lseqsrlleq erwrvaaeks kaesaqrtle eqrkimvqqv amereelera ksalleeqks
      901 vmnkcgeerr rlaaewaeff tqqklskera ereaeramha dtqrestiis ltkeqaeltv
      961 racelrakee kliaereale rerqelrlek drlhkaslrl qaraqevehm skvaskkyee
     1021 geqalqearq mqteqqgrlq vvqrqqewlr qqeqrvhqeh lslaqqrlql drvrqeapss
     1081 lpglppraqg paassldavq apastapqrs qtaavqmpth llakllllkh taeedhdfle
     1141 neqffletlk kapynmayhs a
//
LOCUS       NP_001417265             424 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial ribosome-associated GTPase 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001417265 XP_006235880
VERSION     NP_001417265.1
DBSOURCE    REFSEQ: accession NM_001430336.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kotani,T., Akabane,S., Takeyasu,K., Ueda,T. and Takeuchi,N.
  TITLE     Human G-proteins, ObgH1 and Mtg1, associate with the large
            mitochondrial ribosome subunit and are involved in translation and
            assembly of respiratory complexes
  JOURNAL   Nucleic Acids Res 41 (6), 3713-3722 (2013)
   PUBMED   23396448
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On May 10, 2024 this sequence version replaced XP_006235880.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2091967.1,
                                           SRR26360176.2214630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q43"
     Protein         1..424
                     /product="mitochondrial ribosome-associated GTPase 2
                     isoform 2"
                     /note="GTP-binding protein 5"
                     /calculated_mol_wt=45983
     Region          131..403
                     /region_name="Obg_CgtA"
                     /note="Obg family GTPase CgtA; TIGR02729"
                     /db_xref="CDD:274271"
     CDS             1..424
                     /gene="Mtg2"
                     /gene_synonym="Gtpbp5"
                     /coded_by="NM_001430336.1:91..1365"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:296462"
                     /db_xref="RGD:1359243"
ORIGIN      
        1 mtliipsshl qplsaaqamv ptrlvlartc tvfdsvlkwa pstcavlkps qllplqascr
       61 llsvgivdha khrepsgkkl lsekklkrhf vdhrrvlfrg gsggsgmscf hseprkefgg
      121 pdggdggngg hiilrvdqqv kslssvlsqy qgfsgedggs kncfgrggat lyiqvpvgtl
      181 vkegdeivad lshlgdeyva alggaggkgn rfflandnra pvtctpgqpg qervlylelk
      241 tmahagmvgf pnagkssllr aisnakpava sypfttlnph vgivhyeghq qvavadipgi
      301 irgahqnkgl glsflrhier crfflyvvdl slpepwtqvd dlkyelekye eglsershvi
      361 iankidlpqa rahllqlqdr lgqevialsa ltgenleqll lhlkvlhdah ieaeleqgrq
      421 plrw
//
LOCUS       NP_001102204             217 aa            linear   ROD 28-APR-2025
DEFINITION  MOB kinase activator 3A [Rattus norvegicus].
ACCESSION   NP_001102204 XP_001071737 XP_343162
VERSION     NP_001102204.1
DBSOURCE    REFSEQ: accession NM_001108734.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168845.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001071737.1, XP_343162.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168845.1, CV104448.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..217
                     /product="MOB kinase activator 3A"
                     /note="MOB1, Mps One Binder kinase activator-like 2B; mps
                     one binder kinase activator-like 2A; MOB1, Mps One Binder
                     kinase activator-like 2A"
                     /calculated_mol_wt=25396
     Region          36..208
                     /region_name="Mob1_phocein"
                     /note="Mob1/phocein family; pfam03637"
                     /db_xref="CDD:461000"
     CDS             1..217
                     /gene="Mob3a"
                     /gene_synonym="Mobkl2a; Mobkl2b"
                     /coded_by="NM_001108734.2:72..725"
                     /db_xref="GeneID:362833"
                     /db_xref="RGD:1308187"
ORIGIN      
        1 msnpflkqvf nkdktfrpkr kfepgtqrfe lhkraqasln agldlrlavq lppgedlndw
       61 vavhvvdffn rvnliygtis dgcteqscpv msggpkyeyr wqdeqryrkp talsaprymd
      121 llmdwievqi nnedlfptnv gtpfpktflq avrkilsrlf rvfvhvyihh fdriaqmgse
      181 ahvntcykhf yyfvtefsli dpkeleplke mtsrmch
//
LOCUS       NP_001386647             191 aa            linear   ROD 28-APR-2025
DEFINITION  chromatin complexes subunit BAP18 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001386647 XP_006246714
VERSION     NP_001386647.1
DBSOURCE    REFSEQ: accession NM_001399718.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jan 13, 2022 this sequence version replaced XP_006246714.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.587583.1,
                                           SRR26360176.2101728.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840105,
                                           SAMN12840106 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..191
                     /product="chromatin complexes subunit BAP18 isoform 2"
                     /note="chromatin complexes subunit BAP18"
                     /calculated_mol_wt=19814
     Region          41..77
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     CDS             1..191
                     /gene="Bacc1"
                     /gene_synonym="C10h17orf49; RGD1308134"
                     /coded_by="NM_001399718.1:66..641"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:287452"
                     /db_xref="RGD:1308134"
ORIGIN      
        1 mtsastkvge ifsaagaaft klgeltmqlh pvsdsspaga kwteteieml raavkrfgdd
       61 lnhiscvike rtvaqikttv krkvyedsgi plpaespkkg pkkmtsgvls ppnapppsss
      121 svpeaggppi kkqkadvtls alndsdansd lvdveglget ppakklnfdq dsltldsgll
      181 stsadaplls c
//
LOCUS       NP_001396205             799 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 431-like isoform 1 [Rattus norvegicus].
ACCESSION   NP_001396205 XP_038940831
VERSION     NP_001396205.1
DBSOURCE    REFSEQ: accession NM_001409276.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jul 12, 2022 this sequence version replaced XP_038940831.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.38877.1,
                                           SRR26643288.39282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q38"
     Protein         1..799
                     /product="zinc finger protein 431-like isoform 1"
                     /calculated_mol_wt=91730
     Region          4..44
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          64..478
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          78..97
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          105..125
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          133..153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          162..181
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          189..209
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(194,196,198,200..201,204..205,208,222,224,228..229,
                     232..233,236,250,252,254,256..257,260..261,264)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          217..237
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          245..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          273..293
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          297..711
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          301..321
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(306,308,310,312..313,316..317,320,334,336,340..341,
                     344..345,348,362,364,366,368..369,372..373,376)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          329..349
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(558,560,562,564..565,568..569,572,586,588,592..593,
                     596..597,600,614,616,618,620..621,624..625,628)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          637..657
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          665..685
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          693..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          705..730
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          721..741
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(726,728,730,732..733,736..737,740,754,756,760..761,
                     764..765,768,782,784,786,788..789,792..793,796)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          745..>799
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          749..769
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          761..786
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          777..797
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..799
                     /gene="LOC120094815"
                     /coded_by="NM_001409276.1:97..2496"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:120094815"
                     /db_xref="RGD:41247165"
ORIGIN      
        1 mdaltyddvh vnftreewal ldpsqkslyk dvmletyrnl taigynwedh tidehcqsfr
       61 rhgrherchp gekpsentqc gkafaqqshl qrhksthtge klyeckphdk aftydsqlqt
      121 lerihtgekp ykcnqcgkaf errcnlgrhk lihtgrksyk ynqcgkdfag lshlkthgit
      181 htggkpykcd qcgkafayhs slqvhkriht gekpyvcdqc gkafaqlghl qvhgithtge
      241 kpykcdqcgk afahhsylqv hkrihtgekl cecdqcgkaf lshsylqvhk rihtgenlye
      301 cdqcgkafts hsylqvhkri htgeklyecd qcgkaftshs ylqvhkriht gekpyvcdqc
      361 gkafarlsyl kthgithtge kpykcdqcgk afehrcnlgs hklihtgekp ykcdqcgkaf
      421 sshsylqvhk rihtgeklce cdqcgkafss hsylqvhkri htgqnlyecd qcgkafashs
      481 ylqvhkriht geklcecdqc gkafsshsyl qvhkrihtge klyecdqcgk afashsylqv
      541 hkrihtgenl yecdqcskaf ashsylqvhk rihtgekpyv cdwcnkafay hsylqvhkri
      601 htgekpyvcd qcgkdfvvps elkrhkriht gekpykcnec gkafvgqndl kkhrrthtge
      661 kpykcnecgk afvfnfnlra hkvihtgekp ykcsecgkaf acntslrthk aihtgvkpfe
      721 ckqcgkafac ntslqthrai htgvkpfeck qcgkafvgqn dlkrheriht gekpyecnec
      781 gkafsqssql qlhkrthty
//
LOCUS       NP_037156                279 aa            linear   ROD 28-APR-2025
DEFINITION  prostatic spermine-binding protein isoform 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_037156
VERSION     NP_037156.3
DBSOURCE    REFSEQ: accession NM_013024.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Anderegg,R.J., Carr,S.A., Huang,I.Y., Hiipakka,R.A., Chang,C.S. and
            Liao,S.T.
  TITLE     Correction of the cDNA-derived protein sequence of prostatic
            spermine binding protein: pivotal role of tandem mass spectrometry
            in sequence analysis
  JOURNAL   Biochemistry 27 (12), 4214-4221 (1988)
   PUBMED   3166977
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Chang,C.S., Saltzman,A.G., Hiipakka,R.A., Huang,I.Y. and Liao,S.S.
  TITLE     Prostatic spermine-binding protein. Cloning and nucleotide sequence
            of cDNA, amino acid sequence, and androgenic control of mRNA level
  JOURNAL   J Biol Chem 262 (6), 2826-2831 (1987)
   PUBMED   3818623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 29, 2015 this sequence version replaced NP_037156.2.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA338445.1, CA339207.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..279
                     /product="prostatic spermine-binding protein isoform 1
                     precursor"
                     /note="prostatic spermine-binding protein; zymogen granule
                     protein 16B"
                     /calculated_mol_wt=29427
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1756
     mat_peptide     18..279
                     /product="Prostatic spermine-binding protein.
                     /id=PRO_0000022390"
                     /note="propagated from UniProtKB/Swiss-Prot (P08723.1)"
                     /calculated_mol_wt=29427
     Site            18
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:3166977; propagated from
                     UniProtKB/Swiss-Prot (P08723.1)"
     Region          22..150
                     /region_name="Jacalin_ZG16_like"
                     /note="Jacalin-like lectin domain of the zymogen granule
                     protein 16 and related proteins; cd09611"
                     /db_xref="CDD:187707"
     Site            order(25..26,47..48,51,53,71..72,93..95,97,115,137,141,
                     143)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:187707"
     Site            62
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P08723.1)"
     Region          160..279
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08723.1)"
     CDS             1..279
                     /gene="Sbp"
                     /gene_synonym="Zg16b"
                     /coded_by="NM_013024.4:161..1000"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25540"
                     /db_xref="RGD:3623"
ORIGIN      
        1 mlllvtlall agptcraqni lgnnvgtyfy vageehgqlr glrifltvid likgiqlrfg
       61 gnwsdvygsr slkykeflle dgehvtqvsg trklcltsls fttnkgrvvt fgvrrglsfn
      121 esggsdkylv tvnglyapgl clngmgfkwk nihddfddnd ddkeddddeh dddneedhgd
      181 kdndkdhddd hddddddked dneedvdder ddkdddeeed dndkendkdd gegsgddddn
      241 ddedddkddd ggsgnddddg dddedddggd ddngdeeee
//
LOCUS       NP_001419633             648 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin 4 induced 1 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001419633 XP_063134247
VERSION     NP_001419633.1
DBSOURCE    REFSEQ: accession NM_001432704.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Boulland,M.L., Marquet,J., Molinier-Frenkel,V., Moller,P.,
            Guiter,C., Lasoudris,F., Copie-Bergman,C., Baia,M., Gaulard,P.,
            Leroy,K. and Castellano,F.
  TITLE     Human IL4I1 is a secreted L-phenylalanine oxidase expressed by
            mature dendritic cells that inhibits T-lymphocyte proliferation
  JOURNAL   Blood 110 (1), 220-227 (2007)
   PUBMED   17356132
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 1, 2024 this sequence version replaced XP_063134247.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2976432.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..648
                     /product="interleukin 4 induced 1 isoform 1 precursor"
                     /note="rCG53598-like; L-amino-acid oxidase"
                     /calculated_mol_wt=69140
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2916
     Region          75..512
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
     CDS             1..648
                     /gene="Il4i1"
                     /coded_by="NM_001432704.1:330..2276"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:100360621"
                     /db_xref="RGD:1304831"
ORIGIN      
        1 mgarrapqrp actlhlvlva tllglavslq wraasnlnli ekcmvdhdye qllkvvtlgl
       61 nrtskpqkvv vvgagvaglv aakvlsdagh kvtileagnr iggriftfrd ektgwigelg
      121 amrmpsshri lhqlcrslgl nltqftqyde nawtevkgvk lrnyvvekmp eklgydlnhr
      181 erghspediy qmalnkaikd vkvlgckkam nmfsehtlle yllkegnlsq pavqllgdvm
      241 skegffylsl aeafrahacl sdrlrysriv ggwdllpral lsslsgtvll napvvsisqg
      301 rhevhvhftt slqshslevm tadvvlltas gpalqrisfs ppltrkrqea lralhyvaas
      361 kvflsfhrpf wheehimggh sntdrpsrli fypapgegsl llasytwsda aapfaglste
      421 qtlhlvlkdl aalhgpvvyr lwdgrgvvkr waedpysqgg fvvqpplfgq gtedydwsvp
      481 ygriyfageh talphgwvet avksglraal rinsnygygm vdletlehal aeasfaeqyl
      541 egdqpeeqqa qeevnpdrqd lsqkhllvet gpdgqqhvfv enipeplehv fmktnpqekg
      601 hkhqiiypse hghvhgevip egpghvhrkh ghvgsgtlqh mhgevdhs
//
LOCUS       NP_001128235            1069 aa            linear   ROD 28-APR-2025
DEFINITION  huntingtin-interacting protein 1-related protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001128235
VERSION     NP_001128235.1
DBSOURCE    REFSEQ: accession NM_001134763.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Peng,L., Yang,Q., Xu,X., Du,Y., Wu,Y., Shi,X., Xu,J., Zhu,L. and
            Luo,J.
  TITLE     Huntingtin-Interacting Protein 1-Related Protein Plays a Critical
            Role in Dendritic Development and Excitatory Synapse Formation in
            Hippocampal Neurons
  JOURNAL   Front Mol Neurosci 10, 186 (2017)
   PUBMED   28663723
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Kim,J.H., Yoon,S., Won,M., Sim,S.H., Ko,J.J., Han,S., Lee,K.A.,
            Lee,K. and Bae,J.
  TITLE     HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces
            BAK-dependent cell death
  JOURNAL   Cell Physiol Biochem 23 (1-3), 43-52 (2009)
   PUBMED   19255499
REFERENCE   4  (residues 1 to 1069)
  AUTHORS   Wilbur,J.D., Chen,C.Y., Manalo,V., Hwang,P.K., Fletterick,R.J. and
            Brodsky,F.M.
  TITLE     Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R
            (Hip1-related protein) is regulated by clathrin light chain
  JOURNAL   J Biol Chem 283 (47), 32870-32879 (2008)
   PUBMED   18790740
REFERENCE   5  (residues 1 to 1069)
  AUTHORS   Jain,R.N., Al-Menhali,A.A., Keeley,T.M., Ren,J., El-Zaatari,M.,
            Chen,X., Merchant,J.L., Ross,T.S., Chew,C.S. and Samuelson,L.C.
  TITLE     Hip1r is expressed in gastric parietal cells and is required for
            tubulovesicle formation and cell survival in mice
  JOURNAL   J Clin Invest 118 (7), 2459-2470 (2008)
   PUBMED   18535670
REFERENCE   6  (residues 1 to 1069)
  AUTHORS   Hyun,T.S., Rao,D.S., Saint-Dic,D., Michael,L.E., Kumar,P.D.,
            Bradley,S.V., Mizukami,I.F., Oravecz-Wilson,K.I. and Ross,T.S.
  TITLE     HIP1 and HIP1r stabilize receptor tyrosine kinases and bind
            3-phosphoinositides via epsin N-terminal homology domains
  JOURNAL   J Biol Chem 279 (14), 14294-14306 (2004)
   PUBMED   14732715
REFERENCE   7  (residues 1 to 1069)
  AUTHORS   Okano,A., Usuda,N., Furihata,K., Nakayama,K., Bao Tian,Q.,
            Okamoto,T. and Suzuki,T.
  TITLE     Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is
            localized in the postsynaptic regions
  JOURNAL   Brain Res 967 (1-2), 210-225 (2003)
   PUBMED   12650982
  REMARK    GeneRIF: Localization of HIP1r at postsynaptic spines in rat brain
            suggests a role of HIP1r for vesicle trafficking through
            interaction with F-actin and working together with huntingtin and
            HIP1 at the synaptic sites.
REFERENCE   8  (residues 1 to 1069)
  AUTHORS   Legendre-Guillemin,V., Metzler,M., Charbonneau,M., Gan,L.,
            Chopra,V., Philie,J., Hayden,M.R. and McPherson,P.S.
  TITLE     HIP1 and HIP12 display differential binding to F-actin, AP2, and
            clathrin. Identification of a novel interaction with clathrin light
            chain
  JOURNAL   J Biol Chem 277 (22), 19897-19904 (2002)
   PUBMED   11889126
REFERENCE   9  (residues 1 to 1069)
  AUTHORS   Engqvist-Goldstein,A.E., Warren,R.A., Kessels,M.M., Keen,J.H.,
            Heuser,J. and Drubin,D.G.
  TITLE     The actin-binding protein Hip1R associates with clathrin during
            early stages of endocytosis and promotes clathrin assembly in vitro
  JOURNAL   J Cell Biol 154 (6), 1209-1223 (2001)
   PUBMED   11564758
REFERENCE   10 (residues 1 to 1069)
  AUTHORS   Engqvist-Goldstein,A.E., Kessels,M.M., Chopra,V.S., Hayden,M.R. and
            Drubin,D.G.
  TITLE     An actin-binding protein of the Sla2/Huntingtin interacting protein
            1 family is a novel component of clathrin-coated pits and vesicles
  JOURNAL   J Cell Biol 147 (7), 1503-1518 (1999)
   PUBMED   10613908
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB005052.1 and BC169096.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB005052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..1069
                     /product="huntingtin-interacting protein 1-related protein
                     isoform 1"
                     /calculated_mol_wt=119422
     Region          30..299
                     /region_name="ANTH"
                     /note="ANTH domain; pfam07651"
                     /db_xref="CDD:400137"
     Site            order(37,47,49..50)
                     /site_type="other"
                     /note="PtdIns(4,5)P2-binding site [chemical binding]"
                     /db_xref="CDD:340811"
     Region          <356..>639
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          462..560
                     /region_name="HIP1_clath_bdg"
                     /note="Clathrin-binding domain of Huntingtin-interacting
                     protein 1; pfam16515"
                     /db_xref="CDD:465154"
     Region          815..1013
                     /region_name="ILWEQ"
                     /note="I/LWEQ domain; smart00307"
                     /db_xref="CDD:214607"
     CDS             1..1069
                     /gene="Hip1r"
                     /coded_by="NM_001134763.1:37..3246"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:81917"
                     /db_xref="RGD:621615"
ORIGIN      
        1 mnsiknvpar vlsrrpghsl eaereqfdkt qaisiskain sqeapvkekh arriilgthh
       61 ekgaftfwsy aiglplpsss ilswkfchvl hkvlrdghpn vlhdcqryrs nireigdlwg
      121 hlrdqyghlv niytkllltk isfhlkhpqf paglevtdev lekaagtdvn nifqltvemf
      181 dymdcelkls esvfrqlnta iavsqmssgq crlapliqvi qdcshlyhyt vklmfklhsc
      241 lpadtlqghr drfheqfhsl rnffrrasdm lyfkrliqip rlpegppnfl rasalaehik
      301 pvvvipeeap eeeepenlie issgppagep vqvvadlfdq tfgppngsmk ddrdlqienl
      361 krevetlrae lekikmeaqr yisqlkgqvn sleaeleeqr kqkqkalvdn eqlrhelaql
      421 kalqlegarn qglreeaerk asatearysk lkekhnelin thaellrkna dtakqltvtq
      481 qsqeevarvk eqlafqmeqv kresemkmee qsdqleklkr elvakagela haqealsrte
      541 qsgselssrl dtlnaekeal sgairqreae llaaqslvre keealsqeqq rsaqekgelq
      601 grlaekesqe qglqqkllde qfavlrgaaa eaeailqdav sklddplhlr ctsspdylvs
      661 raqaaldsvs glekghtqyl assedasalv aaltrfshla adtivnggat shlaptdpad
      721 rlidtcrecg aralelmgql qdqtklpraq pslmraplqg ilqlgqdlkp ksldvrqeel
      781 gamvdkemaa tsaaiedavr riedmmnqar hessgvklev nerilnsctd lmkairllvm
      841 tstslqkeiv esgrgaatqq efyaknsrwt eglisaskav gwgatqlves adkvvlhmgk
      901 yeelivcshe iaastaqlva askvkankns phlsrlqecs rtvneraanv vastksgqeq
      961 iedrdtmdfs glsliklkkq emetqvrvle lektleaerv rlgelrkqhy vlaggmgtpg
     1021 eeepsrpspa prsgatkkpp laqkpsiapr pdnqldkkdg vypaqlvny
//
LOCUS       NP_001420122             175 aa            linear   ROD 28-APR-2025
DEFINITION  DPY30 domain-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001420122 XP_017455820
VERSION     NP_001420122.1
DBSOURCE    REFSEQ: accession NM_001433193.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Aug 7, 2024 this sequence version replaced XP_017455820.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1270824.1,
                                           SRR26360181.2174198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..175
                     /product="DPY30 domain-containing protein 1 isoform 2"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20295
     Region          2..44
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     Region          <44..>168
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
     CDS             1..175
                     /gene="Dydc1"
                     /coded_by="NM_001433193.1:132..659"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:688433"
                     /db_xref="RGD:1588855"
ORIGIN      
        1 mesrylqqcl gtcltqglae varvrpldpi eylalwiyky kenesmeqlr qkelialehe
       61 relammeqem mdrlkaeell fqqqlafqle lemqekekqk tedfkteqek stkdtmstes
      121 iskgeeamps eesmmdsgkt laeisdryga pnlsrveeld epmlsdialn idqdl
//
LOCUS       NP_001418096            1845 aa            linear   ROD 28-APR-2025
DEFINITION  Ecm29 proteasome adaptor and scaffold isoform a [Rattus
            norvegicus].
ACCESSION   NP_001418096 XP_056841526
VERSION     NP_001418096.1
DBSOURCE    REFSEQ: accession NM_001431167.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1845)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   2  (residues 1 to 1845)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 1845)
  AUTHORS   Gorbea,C., Goellner,G.M., Teter,K., Holmes,R.K. and Rechsteiner,M.
  TITLE     Characterization of mammalian Ecm29, a 26 S proteasome-associated
            protein that localizes to the nucleus and membrane vesicles
  JOURNAL   J Biol Chem 279 (52), 54849-54861 (2004)
   PUBMED   15496406
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jul 9, 2024 this sequence version replaced XP_056841526.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.19099.1,
                                           SRR26643295.21439.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1845
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..1845
                     /product="Ecm29 proteasome adaptor and scaffold isoform a"
                     /note="proteasome adapter and scaffold protein ECM29"
                     /calculated_mol_wt=204088
     Region          16..522
                     /region_name="Ecm29"
                     /note="Proteasome stabilizer; pfam13001"
                     /db_xref="CDD:463769"
     Region          396..428
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          440..466
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          475..506
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          515..541
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1084..1107
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(1099..1100,1103,1106..1107,1140,1143,1146..1147,
                     1152,1180..1181,1184,1187..1188,1191,1222..1223,1226,
                     1229..1230,1272..1273,1276,1279..1280)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          1119..1152
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1162..1192
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1201..1230
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1251..1281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1398..1427
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..1845
                     /gene="Ecpas"
                     /gene_synonym="RGD1306148"
                     /coded_by="NM_001431167.1:296..5833"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:313196"
                     /db_xref="RGD:1306148"
ORIGIN      
        1 maaaaasasq delnqlervf lrlghaetde qlqniiskfl ppvllklsst qegvrkkvme
       61 llvhlnkrik srpkiqlpve tllvqyqdpa avsfvtnfti iyvkmgyprl pvekqcelap
      121 tlltamegkp qpqqdslmhl liptlfhmky paessksasp fnlaekpktv qllldfmldv
      181 llmpygyvln esqsrqnsss sqgsssnsgg ssgipqpppg msfyaakrvi gdnpwtpeql
      241 eqcklgivkf ieaeqvpele avlhlviass dtrhsvataa dlelkskqsl idwnnpaiin
      301 kmykvylgdi plktkegavl kpelkrdpvs trvklkivph llrsrqaaet fpaniqvvyd
      361 glfgtntnsk lrtlslqfvh hicitcpeik ikplgpmlln gltklineyk edpkllsmay
      421 savgklssrm phlftkdial vqqlfealck eepetrlaiq ealsmmvgay stlegaqrtl
      481 mealvasyli kpevqvrqva vkfastvfps dhipsrylll laagdpreev hgeaqrvlrc
      541 lpgrnkkesa skqmpsfpem vyyiqekash rmktpvkymt gttvlpfnpa afgeivlylr
      601 mclahsagvv ptsqsladmq dhapaigryi rtlmsssqat asscnksget npvqiyigll
      661 qqllagvggl pvmyclleav svypeklatk fvdktewiks lmssskeemr elaalfysvv
      721 vstvsgkelk smveqlikat kdnhspevqh gsllalgftv grylakkrvr maeqhdletd
      781 ddllpeqeev irsatetigs fldstsplla iaactalgei grngplpips egsgftklhl
      841 vesllnrips sketnkmker aiqtlgyfpv gdgdfphqkl llqglmdsve akqielqfti
      901 geaitsaaig tssvaardaw lvteeeyipp agakvndvvp wvldvilnkh iispnphvrq
      961 aaciwllslv rklsthvevk shlkeiqsaf vsvlsendel sqdvaskglg lvydlgseqd
     1021 qqelvstlvd tlrtgkrvkh evsgetvvfq ggglgktpdg qglstykelc slasdlsqpd
     1081 lvykfmnlan hhamwnsrkg aafgfnviat rageqlapfl pqlvprlyry qfdpnlgirq
     1141 amtsiwnalv tdksmvdkyl keilqdlikn ltsnmwrvre ssclalndll rgrplddvid
     1201 klpemwetlf rvqddikesv rkaaelalkt lskvcvkmcd pakgaagqrt iavllpclld
     1261 kgmmspvtev ralsintlvk isksagamlk phapklipal leslsvlepq vlnylslrat
     1321 eqekdamdsa rlsaaksspm metinmclqy ldvsvlgelv prlcelirsg vglgtkggca
     1381 svivslttqc pqdltpysgk lmsallsglt drnsviqksc afamghlvrt srdsstekll
     1441 qkltawymek eepiyktsca ltihaigrys pdvlknhake vlplaflgmh eiadeeksek
     1501 eecnmwtevw qenvpgsfgg irlylqelit itqkalqsqs wkmkaqgaia masiakqtss
     1561 lvppylgmil salvqglagr twagkeellk aiacvvtass teleksvpnq pttneilqav
     1621 lkecckenlk ykivaiscaa dvlkatkedr fqefsdivmp likknslesm gvrttkaede
     1681 nekerelqle sllgafeslg kawprnpdtq rcyrqemckl mcerlrlstw kvqlgvlqsm
     1741 naffqglmll eeehadpeal aeilletcqs ityslenkty ssvrtealsv ielllkklee
     1801 gkqwesltae crrlliesla tmetdnrpel qekasvlkkt lesle
//
LOCUS       NP_001420187            1147 aa            linear   ROD 28-APR-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-2 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001420187 XP_006243799
VERSION     NP_001420187.1
DBSOURCE    REFSEQ: accession NM_001433258.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Zhang,J., Wu,L., Li,Z. and Fu,G.
  TITLE     miR-1231 exacerbates arrhythmia by targeting calciumchannel gene
            CACNA2D2 in myocardial infarction
  JOURNAL   Am J Transl Res 9 (4), 1822-1833 (2017)
   PUBMED   28469787
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Li,B., Zhao,Q., Wang,L.X., Deng,C.Y., Zeng,F., Wu,T.G., Jiang,Z.F.
            and Xu,D.L.
  TITLE     Effect of beta3-adrenergic receptor on atrial L-type Ca(2+) current
            in rats with chronic heart failure
  JOURNAL   Heart Lung Circ 23 (4), 369-377 (2014)
   PUBMED   24055266
  REMARK    GeneRIF: There was no difference in the mRNA expression of
            alpha2delta-2 (Cacna2d2) between the BRL group and CHF control
            group (0.264 +/- 0.005 vs. 0.243 +/- 0.017, P>0.05), which was also
            higher than in the normal control group (0.137 +/- 0.013, P<0.01).
REFERENCE   3  (residues 1 to 1147)
  AUTHORS   Eroglu,C., Allen,N.J., Susman,M.W., O'Rourke,N.A., Park,C.Y.,
            Ozkan,E., Chakraborty,C., Mulinyawe,S.B., Annis,D.S.,
            Huberman,A.D., Green,E.M., Lawler,J., Dolmetsch,R., Garcia,K.C.,
            Smith,S.J., Luo,Z.D., Rosenthal,A., Mosher,D.F. and Barres,B.A.
  TITLE     Gabapentin receptor alpha2delta-1 is a neuronal thrombospondin
            receptor responsible for excitatory CNS synaptogenesis
  JOURNAL   Cell 139 (2), 380-392 (2009)
   PUBMED   19818485
REFERENCE   4  (residues 1 to 1147)
  AUTHORS   Kaja,S., Todorov,B., van de Ven,R.C., Ferrari,M.D., Frants,R.R.,
            van den Maagdenberg,A.M. and Plomp,J.J.
  TITLE     Redundancy of Cav2.1 channel accessory subunits in transmitter
            release at the mouse neuromuscular junction
  JOURNAL   Brain Res 1143, 92-101 (2007)
   PUBMED   17320843
REFERENCE   5  (residues 1 to 1147)
  AUTHORS   Hatano,S., Yamashita,T., Sekiguchi,A., Iwasaki,Y., Nakazawa,K.,
            Sagara,K., Iinuma,H., Aizawa,T. and Fu,L.T.
  TITLE     Molecular and electrophysiological differences in the L-type Ca2+
            channel of the atrium and ventricle of rat hearts
  JOURNAL   Circ J 70 (5), 610-614 (2006)
   PUBMED   16636499
  REMARK    GeneRIF: The level of the alpha1C (Cacna1c) (Cav1.2) protein was
            decreased (approximately 0.5-fold) and that of alpha2 delta-1
            (Cacna2d1) was increased (approximately 2-fold) in the atrium
            compared with the ventricle
REFERENCE   6  (residues 1 to 1147)
  AUTHORS   Walter,J.T., Alvina,K., Womack,M.D., Chevez,C. and Khodakhah,K.
  TITLE     Decreases in the precision of Purkinje cell pacemaking cause
            cerebellar dysfunction and ataxia
  JOURNAL   Nat Neurosci 9 (3), 389-397 (2006)
   PUBMED   16474392
REFERENCE   7  (residues 1 to 1147)
  AUTHORS   Cole,R.L., Lechner,S.M., Williams,M.E., Prodanovich,P.,
            Bleicher,L., Varney,M.A. and Gu,G.
  TITLE     Differential distribution of voltage-gated calcium channel alpha-2
            delta (alpha2delta) subunit mRNA-containing cells in the rat
            central nervous system and the dorsal root ganglia
  JOURNAL   J Comp Neurol 491 (3), 246-269 (2005)
   PUBMED   16134135
  REMARK    GeneRIF: The alpha2delta-2 subunit is also found in brain regions
            known to be involved in olfaction, somatic motor control, fluid
            homeostasis, ingestive and defensive behaviors, neuroendocrine
            functions, and circadian rhythm.
REFERENCE   8  (residues 1 to 1147)
  AUTHORS   Chu,P.J. and Best,P.M.
  TITLE     Molecular cloning of calcium channel alpha(2)delta-subunits from
            rat atria and the differential regulation of their expression by
            IGF-1
  JOURNAL   J Mol Cell Cardiol 35 (2), 207-215 (2003)
   PUBMED   12606261
REFERENCE   9  (residues 1 to 1147)
  AUTHORS   Barclay,J., Balaguero,N., Mione,M., Ackerman,S.L., Letts,V.A.,
            Brodbeck,J., Canti,C., Meir,A., Page,K.M., Kusumi,K.,
            Perez-Reyes,E., Lander,E.S., Frankel,W.N., Gardiner,R.M.,
            Dolphin,A.C. and Rees,M.
  TITLE     Ducky mouse phenotype of epilepsy and ataxia is associated with
            mutations in the Cacna2d2 gene and decreased calcium channel
            current in cerebellar Purkinje cells
  JOURNAL   J Neurosci 21 (16), 6095-6104 (2001)
   PUBMED   11487633
REFERENCE   10 (residues 1 to 1147)
  AUTHORS   Holz,A., Frank,M., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and
            Schwab,M.E.
  TITLE     Chromosomal localization of the myelin-associated oligodendrocytic
            basic protein and expression in the genetically linked neurological
            mouse mutants ducky and tippy
  JOURNAL   J Neurochem 69 (5), 1801-1809 (1997)
   PUBMED   9349522
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Aug 8, 2024 this sequence version replaced XP_006243799.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760433 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1147
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform 2 precursor"
                     /note="voltage-dependent calcium channel subunit
                     alpha-2/delta-2; voltage-gated calcium channel subunit
                     alpha-2/delta-2; calcium channel, voltage dependent,
                     alpha2/delta subunit 2; calcium channel,
                     voltage-dependent, alpha 2/delta subunit 2"
                     /calculated_mol_wt=127895
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
                     /calculated_mol_wt=1857
     Region          144..268
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          280..459
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(300,302,304,372,404)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          300..304
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          536..645
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          665..1107
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            857
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            1110..1130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     CDS             1..1147
                     /gene="Cacna2d2"
                     /coded_by="NM_001433258.1:215..3658"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:300992"
                     /db_xref="RGD:631360"
ORIGIN      
        1 mavpartcga swpgpvrtar pwpgrgprpc pdprgpasgp arplllllpp llllplltap
       61 gasaysfpqq htmqhwarrl eqeidgvmri fggvqqlrei ykdnrnlfdv qenepqklve
      121 kvagdiesll drkvqalkrl adaaenfqka hrwqdnikee dimyydakad aelddpesed
      181 mergsktsal rldfieepnf knkvnysyta vqiptdiykg stvilnelnw tealenvfie
      241 nrrqdptllw qvfgsatgvt ryypatpwra pkkidlydvr rrpwyiqgas spkdmviivd
      301 vsgsvsgltl klmktsvcem ldtlsdddyv nvasfnekaq pvscfthlvq anvrnkkvfk
      361 eavqgmvakg ttgykagfey afdqlqnsni trancnkmim mftdggedrv qdvfekynwp
      421 nrtvrvftfs vgqhnydvtp lqwmactnkg yyfeipsiga irintqeyld vlgrpmvlag
      481 kdakqvqwtn vyedalglgl vvtgtlpvfn ltqdgpgekk nqlilgvmgi dvalndikrl
      541 tpnytlgang yvfaidlngy vllhpnlkpq ttnfrepvtl dfldaelede nkeeirrsmi
      601 dgdkghkqir tlvksldery idevirnytw vpirstnysl glvlppysty ylqanlsdqi
      661 lqvkyfefll pssfeseghv fiapreyckd lnasdnntef lknfielmek vtpdskqcnn
      721 fllhnlildt gitqqlverv wrdqdlntys llavfaatdg gitrvfpnka aedwtenpep
      781 fnasfyrrsl dnrgyifkpp hqdsllrple lendtvgvlv stavelslgr rtlrpavvgv
      841 kldleawaek fkvlasnrth qdqpqkcgps shcemdcevn nedllcvlid dggflvlsnq
      901 nhqwdqvgrf fsevdanlml alynnsfytr kesydyqaac apqppgnlga aprgvfvpti
      961 adflnlawwt saaawslfqq llygliyhsw fqadpaeaeg spetresscv mkqtqyyfgs
     1021 vnasynaiid cgncsrlfha qrltntnllf vvaekplcsq cevgrllqke thsdgpeqce
     1081 lvqrpryrrg phicfdynat edtsdcgrga sfppslgvlv slqlllllgl pprpqpqihs
     1141 faasrrl
//
LOCUS       NP_058893                532 aa            linear   ROD 28-APR-2025
DEFINITION  CUGBP Elav-like family member 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_058893
VERSION     NP_058893.2
DBSOURCE    REFSEQ: accession NM_017197.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Liu,Y., Wang,H., Wang,J., Wei,B., Zhang,X., Zhang,M., Cao,D.,
            Dai,J., Wang,Z., Nyirimigabo,E. and Ji,G.
  TITLE     A positive feedback regulation of Heme oxygenase 1 by CELF1 in
            cardiac myoblast cells
  JOURNAL   Biochim Biophys Acta Gene Regul Mech 1862 (2), 209-218 (2019)
   PUBMED   30508596
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bai,Z., Chai,X.R., Yoon,M.J., Kim,H.J., Lo,K.A., Zhang,Z.C., Xu,D.,
            Siang,D.T.C., Walet,A.C.E., Xu,S.H., Chia,S.Y., Chen,P., Yang,H.,
            Ghosh,S. and Sun,L.
  TITLE     Dynamic transcriptome changes during adipose tissue energy
            expenditure reveal critical roles for long noncoding RNA regulators
  JOURNAL   PLoS Biol 15 (8), e2002176 (2017)
   PUBMED   28763438
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Del Pino Sans,J., Krishnan,S., Aggison,L.K., Adams,H.L.,
            Shrikant,M.M., Lopez-Giraldez,F. and Petersen,S.L.
  TITLE     Microarray analysis of neonatal rat anteroventral periventricular
            transcriptomes identifies the proapoptotic Cugbp2 gene as
            sex-specific and regulated by estradiol
  JOURNAL   Neuroscience 303, 312-322 (2015)
   PUBMED   26166732
  REMARK    GeneRIF: This study demonstrated that Cugbp2 regulates splicing and
            translation of mRNAs linked to sexual differentiation in rats.
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Moraes,K.C., Monteiro,C.J. and Pacheco-Soares,C.
  TITLE     A novel function for CUGBP2 in controlling the pro-inflammatory
            stimulus in H9c2 cells: subcellular trafficking of messenger
            molecules
  JOURNAL   Cell Biol Int 37 (10), 1129-1138 (2013)
   PUBMED   23661609
  REMARK    GeneRIF: a regulatory connection between COX-2 and CUGBP2 in the
            cardiac cells, was demonstrated.
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Mukhopadhyay,D., Houchen,C.W., Kennedy,S., Dieckgraefe,B.K. and
            Anant,S.
  TITLE     Coupled mRNA stabilization and translational silencing of
            cyclooxygenase-2 by a novel RNA binding protein, CUGBP2
  JOURNAL   Mol Cell 11 (1), 113-126 (2003)
   PUBMED   12535526
  REMARK    GeneRIF: These findings identify a novel paradigm for RNA binding
            proteins such as CUGBP2 in facilitating opposing functions of mRNA
            stability and translation inhibition and reveal a mechanism for
            inhibiting cyclooxygenase-2 expression in cancer cells.
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Zhang,W., Liu,H., Han,K. and Grabowski,P.J.
  TITLE     Region-specific alternative splicing in the nervous system:
            implications for regulation by the RNA-binding protein NAPOR
  JOURNAL   RNA 8 (5), 671-685 (2002)
   PUBMED   12022233
  REMARK    GeneRIF: tissue-specific distribution of NAPOR, CUG-BP, and other
            highly related proteins within the nervous system
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Levers,T.E., Tait,S., Birling,M.C., Brophy,P.J. and Price,D.J.
  TITLE     Etr-r3/mNapor, encoding an ELAV-type RNA binding protein, is
            expressed in differentiating cells in the developing rodent
            forebrain
  JOURNAL   Mech Dev 112 (1-2), 191-193 (2002)
   PUBMED   11850193
  REMARK    GeneRIF: Etr-r3/mNapor, encoding an ELAV-type RNA binding protein,
            is expressed in differentiating cells in the developing rodent
            forebrain
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Ladd,A.N., Charlet,N. and Cooper,T.A.
  TITLE     The CELF family of RNA binding proteins is implicated in
            cell-specific and developmentally regulated alternative splicing
  JOURNAL   Mol Cell Biol 21 (4), 1285-1296 (2001)
   PUBMED   11158314
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Choi,D.K., Ito,T., Tsukahara,F., Hirai,M. and Sakaki,Y.
  TITLE     Developmentally-regulated expression of mNapor encoding an
            apoptosis-induced ELAV-type RNA binding protein
  JOURNAL   Gene 237 (1), 135-142 (1999)
   PUBMED   10524244
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Mar 28, 2007 this sequence version replaced NP_058893.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ010386.1, SRR26643298.69796.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..532
                     /product="CUGBP Elav-like family member 2 isoform 1"
                     /note="RNA-binding protein Brunol3; Cugbp- and Etr3-like
                     factor 2; CUG-BP- and ETR-3-like factor 2; bruno-like
                     protein 3; neuroblastoma apoptosis-related RNA-binding
                     protein; RNA-binding protein BRUNOL-3; elav-type
                     RNA-binding protein 3; CUG triplet repeat, RNA binding
                     protein 2"
                     /calculated_mol_wt=56827
     Region          57..140
                     /region_name="RRM1_CELF1_2_Bruno"
                     /note="RNA recognition motif 1 (RRM1) found in CUGBP
                     Elav-like family member CELF-1, CELF-2, Drosophila
                     melanogaster Bruno protein and similar proteins; cd12631"
                     /db_xref="CDD:410040"
     Site            order(61,63..64,67,88..91,93..94,101..103,105,135,137,
                     139..140)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410040"
     Region          149..229
                     /region_name="RRM2_CELF1_2"
                     /note="RNA recognition motif 2 (RRM2) found in CUGBP
                     Elav-like family member CELF-1, CELF-2 and similar
                     proteins; cd12634"
                     /db_xref="CDD:410042"
     Site            order(151,153,155..156,159,178,180,182,190..192,194,
                     220..221,224,226,228..229)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410042"
     Region          440..531
                     /region_name="RRM3_CELF1_2"
                     /note="RNA recognition motif 3 (RRM3) found in CUGBP
                     Elav-like family member CELF-1, CELF-2 and similar
                     proteins; cd12638"
                     /db_xref="CDD:241082"
     CDS             1..532
                     /gene="Celf2"
                     /gene_synonym="Brunol3; Cugbp2; Etr3; Napor"
                     /coded_by="NM_017197.4:180..1778"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29428"
                     /db_xref="RGD:68347"
ORIGIN      
        1 mfertselaf vetisvesmr cpksavtmrn eelllsngta nkmngaldhs dqpdpdaikm
       61 fvgqiprsws ekelkelfep ygavyqinvl rdrsqnppqs kgccfvtfyt rkaaleaqna
      121 lhniktlpgm hhpiqmkpad seksnavedr klfigmvskk cnendirvmf spfgqieecr
      181 ilrgpdglsr gcafvtfstr amaqnaikam hqsqtmegcs spivvkfadt qkdkeqrrlq
      241 qqlaqqmqql ntatwgnltg lggltpqyla llqqatsssn lgafsgiqqm agmnalqlqn
      301 latlaaaaaa aqtsatstna nplsstssal galtspvaas tpnstagaam nsltslgtlq
      361 glagatvgln ninalavaqm lsgmaalngg lgatgltngt agtmdaltqa ysgiqqyaaa
      421 alptlysqsl lqqqsaagsq kegpeganlf iyhlpqefgd qdilqmfmpf gnvisakvfi
      481 dkqtnlskcf gfvsydnpvs aqaaiqamng fqigmkrlkv qlkrskndsk py
//
LOCUS       NP_001386658             524 aa            linear   ROD 28-APR-2025
DEFINITION  apoptosis inhibitor 5 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001386658 XP_006234648
VERSION     NP_001386658.1
DBSOURCE    REFSEQ: accession NM_001399729.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Van den Berghe,L., Laurell,H., Huez,I., Zanibellato,C., Prats,H.
            and Bugler,B.
  TITLE     FIF [fibroblast growth factor-2 (FGF-2)-interacting-factor], a
            nuclear putatively antiapoptotic factor, interacts specifically
            with FGF-2
  JOURNAL   Mol Endocrinol 14 (11), 1709-1724 (2000)
   PUBMED   11075807
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Kim,J.W., Cho,H.S., Kim,J.H., Hur,S.Y., Kim,T.E., Lee,J.M.,
            Kim,I.K. and Namkoong,S.E.
  TITLE     AAC-11 overexpression induces invasion and protects cervical cancer
            cells from apoptosis
  JOURNAL   Lab Invest 80 (4), 587-594 (2000)
   PUBMED   10780674
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Tewari,M., Yu,M., Ross,B., Dean,C., Giordano,A. and Rubin,R.
  TITLE     AAC-11, a novel cDNA that inhibits apoptosis after growth factor
            withdrawal
  JOURNAL   Cancer Res 57 (18), 4063-4069 (1997)
   PUBMED   9307294
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 13, 2022 this sequence version replaced XP_006234648.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.391083.1,
                                           SRR26360194.1087354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q31"
     Protein         1..524
                     /product="apoptosis inhibitor 5 isoform 1"
                     /calculated_mol_wt=58889
     Region          4..497
                     /region_name="API5"
                     /note="Apoptosis inhibitory protein 5 (API5); pfam05918"
                     /db_xref="CDD:428672"
     Region          63..91
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          97..139
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..524
                     /gene="Api5"
                     /coded_by="NM_001399729.1:154..1728"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:362170"
                     /db_xref="RGD:1309772"
ORIGIN      
        1 mptveelyrn ygiladateq vgqhkdayqv ildgvkggtk ekrlaaqfip kffkhfpela
       61 dsainaqldl cededvsirr qaikelpqfa tgenlprvad iltqllqtdd saefnlvnna
      121 llsifkmdak gtlgglfsqi lqgedivrer aikflstklk tlpdevltke veeliltesk
      181 kvledvtgee fvlfmkilsg lkslqtvsgr qqlvelvaeq adleqtfsps dpdcvdrllq
      241 ctrqavplfs knvhstrfvt yfceqvlpnl stlttpvegl diqlevlkll aemssfcgdm
      301 ekletnlrkl fdklleympl ppeeaengen agneepklqf syvecllysf hqlgrklpdf
      361 ltaklnaekl kdfkirlqyf arglqvyirq lrlalqgktg ealkteenki kvvalkitnn
      421 invlikdlfh ippsykstvt lswkpvqkve igqkrtsedt ssgsppkksp ggpkrdarqi
      481 ynppsgkyss nlgnfnyeqr gafrgsrggr gwgtrgnrsr grly
//
LOCUS       NP_001423954             521 aa            linear   ROD 28-APR-2025
DEFINITION  biotinidase isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001423954 XP_006252674
VERSION     NP_001423954.1
DBSOURCE    REFSEQ: accession NM_001437025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Pindolia,K., Jordan,M., Guo,C., Matthews,N., Mock,D.M., Strovel,E.,
            Blitzer,M. and Wolf,B.
  TITLE     Development and characterization of a mouse with profound
            biotinidase deficiency: a biotin-responsive neurocutaneous disorder
  JOURNAL   Mol Genet Metab 102 (2), 161-169 (2011)
   PUBMED   21051254
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Brumwell,C.L., Hossain,W.A., Morest,D.K. and Wolf,B.
  TITLE     Biotinidase reveals the morphogenetic sequence in cochlea and
            cochlear nucleus of mice
  JOURNAL   Hear Res 209 (1-2), 104-121 (2005)
   PUBMED   16107307
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 26, 2025 this sequence version replaced XP_006252674.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.58182.1,
                                           SRR26360194.26191.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..521
                     /product="biotinidase isoform 2 precursor"
                     /EC_number="3.5.1.12"
                     /note="biotinase"
                     /calculated_mol_wt=55591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=2449
     mat_peptide     26..521
                     /product="Biotinidase. /evidence=ECO:0000255.
                     /id=PRO_0000292882"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVF9.1)"
                     /calculated_mol_wt=55591
     Region          36..339
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Site            order(90,190,194,196,223..224,226..227,249)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(90,190,223)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     Site            order(191..195,202..204,224,226..230,233..234,255..256,
                     258..260,262..263,287..288,335..339)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          371..520
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVF9.1)"
     CDS             1..521
                     /gene="Btd"
                     /coded_by="NM_001437025.1:627..2192"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:306262"
                     /db_xref="RGD:1305316"
ORIGIN      
        1 msgartahal vfllgcsala lgvcsasleh geaeyyvaav yehrsvlspn plelssrqqa
       61 lelmkqnldv yeqqvmaaaq kgahiivfpe dgihgfnftr tsiypfldlm psprlvswnp
      121 clepfrfndt evlqrlscma ikgkmflvan lgtkqpclgs dpgcpqdgry qfntnvafsd
      181 ngtlvgryrk hnlyfeeafd spadvdlttf dtpfagkfgm ftcfdilffd pavrllrdfe
      241 vkhiayptaw mnqlpllaai eiqkafataf gvtvlaanih hptlgmtgsg ihtplksfwy
      301 hnmddpeghl iiarvatnpq glvgtentts emdpshrkfl kvlsgdpyce kdaqevrcde
      361 aakwnlnapp tfhsemmydn ftlvpvwgke ghlqvcsnsl cchllferpa lskelyalgv
      421 fdglhtvhgt yyvqacalvk cggagfetcg qeiseaeglf dfhlwgnfst lyvfplflts
      481 gmtldtpdql gwesdhyflr krglssglvt aalygrlyer n
//
LOCUS       NP_001402636            1253 aa            linear   ROD 28-APR-2025
DEFINITION  immunoglobulin superfamily DCC subclass member 4 isoform 2
            precursor [Rattus norvegicus].
ACCESSION   NP_001402636 XP_038937675
VERSION     NP_001402636.1
DBSOURCE    REFSEQ: accession NM_001415707.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1253)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 1253)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   3  (residues 1 to 1253)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 23, 2022 this sequence version replaced XP_038937675.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.30815.1,
                                           SRR26643299.35768.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1253
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1253
                     /product="immunoglobulin superfamily DCC subclass member 4
                     isoform 2 precursor"
                     /note="neighbor of Punc E11"
                     /calculated_mol_wt=132427
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2294
     Region          38..130
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          51..55
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..122
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          144..215
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          249..330
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          260..264
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          273..278
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          308..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          323..326
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          349..421
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          351..355
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          364..368
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          385..391
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          <401..>603
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          401..406
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          414..417
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            order(630,709,724)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          632..726
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          750..842
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(750,815,830)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(831..832,834..835)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          850..942
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(931..932,934..935)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..1253
                     /gene="Igdcc4"
                     /gene_synonym="Nope"
                     /coded_by="NM_001415707.2:77..3838"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:363081"
                     /db_xref="RGD:1310919"
ORIGIN      
        1 maradtgrgl laltfcllsa rgelplpqet tvqlscdegp lrvvlgpeqa vvldctlgaa
       61 aagppttvtw skdgdvvler dnlhllpngs lrlssplepe dsddeealsv wkviegsysc
      121 lahgplgvva sqvavvklat ledfslhpes qtveengtar fechteglpa piitwekdqv
      181 tvteeprlit lpngvlqild vqdsdagsyr cvatnsarqr fsqeallsva lrgsleatrg
      241 qdvvivaape nttvvsgqsv vlecvasadp tpfvswvrqd gkpistdviv lgrtnllias
      301 aqprhsgvyv crankprtrd fataaaelrv laapaisqap ealsrtrast arfvcrasge
      361 prptlhwlhd gaplrpngrv kvqggggslv itqiglqdsg yyqcvaensa gtacaaapla
      421 vvvreglpsa ptrvkatpls ssavlvawer pelhseqiig fslhyqkarg vdnveyqfav
      481 nndttelqvr dlepntdyef yvvaysqlga srtsspalvh tlddvpsaap qlslsspnps
      541 dirvawlplp sslsngqvvk ykieygsgke edqvfstevp gnetqltlns lqpnkvyrvr
      601 isagtgagyg vpsqwmqhrt pgahnqshvp fapaelkvra kmeslvvswq ppphptqisg
      661 yklywrevgt eeeadgdrpp ggrgdqawdv gpvrlkkkvk qyeltqlvpg rlyevklvaf
      721 nkhedgyaav wkgktekapt pdlpiqrgpp lppahvhaes nsstsiwlrw kkpdfttvki
      781 vnytvrfgpw glrnaslvty ytssgedili gglkpftkye favqshgvdm dgpfgsvver
      841 stlpdrpstp psdlrlsplt pstvrlhwcp ptepngeive ylilysnnht qpehqwtllt
      901 tegnifsaev hglesdtryf fkmgartevg pgpfsrlqdv itlqetfsds ldvhsvtgii
      961 vgvclgllcl lacmcaglrr sshrealpgl sstatagnpa lysrarlgpp svpaaheles
     1021 lvhprpqdws pppsdvedka kvhslmggsv sdcrghskrk iswaqaggpn wagswagcel
     1081 pqgsgprpal trallppagt gqtlllqalv ydaiksngrk kpspacrnqv eaevivhsdf
     1141 saskgcpdlh lqdlepeeal paevlpptag vvdlsqgadw lgreleecqp attgperltc
     1201 lpeaasascs csdlqpssav eeapgkgcqp kalcpleisp slprapvssa qvp
//
LOCUS       NP_620191                342 aa            linear   ROD 28-APR-2025
DEFINITION  prostasin precursor [Rattus norvegicus].
ACCESSION   NP_620191
VERSION     NP_620191.1
DBSOURCE    REFSEQ: accession NM_138836.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Frateschi,S., Keppner,A., Malsure,S., Iwaszkiewicz,J., Sergi,C.,
            Merillat,A.M., Fowler-Jaeger,N., Randrianarison,N., Planes,C. and
            Hummler,E.
  TITLE     Mutations of the serine protease CAP1/Prss8 lead to reduced
            embryonic viability, skin defects, and decreased ENaC activity
  JOURNAL   Am J Pathol 181 (2), 605-615 (2012)
   PUBMED   22705055
  REMARK    GeneRIF: Mutations of the serine protease CAP1/Prss8 lead to
            reduced embryonic viability, skin defects, and decreased ENaC
            activity.
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Steensgaard,M., Svenningsen,P., Tinning,A.R., Nielsen,T.D.,
            Jorgensen,F., Kjaersgaard,G., Madsen,K. and Jensen,B.L.
  TITLE     Apical serine protease activity is necessary for assembly of a
            high-resistance renal collecting duct epithelium
  JOURNAL   Acta Physiol (Oxf) 200 (4), 347-359 (2010)
   PUBMED   20645929
  REMARK    GeneRIF: Data show that apical, GPI-anchored, lipid raft-associated
            serine protease activity, compatible with prostasin, is necessary
            for the development of a high-resistance collecting duct
            epithelium.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Spacek,D.V., Perez,A.F., Ferranti,K.M., Wu,L.K., Moy,D.M.,
            Magnan,D.R. and King,T.R.
  TITLE     The mouse frizzy (fr) and rat 'hairless' (frCR) mutations are
            natural variants of protease serine S1 family member 8 (Prss8)
  JOURNAL   Exp Dermatol 19 (6), 527-532 (2010)
   PUBMED   20201958
  REMARK    GeneRIF: A 12-bp deletion in the third exon of the Prss8 gene is
            responsible for the mutant 'hairless', frizzy-Charles River (frCR)
            phenotype. No alterations to Prss8 coding sequences were detected
            in the allelic 'fuzzy' rat variant.
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Chen,M., Chen,L.M., Lin,C.Y. and Chai,K.X.
  TITLE     Hepsin activates prostasin and cleaves the extracellular domain of
            the epidermal growth factor receptor
  JOURNAL   Mol Cell Biochem 337 (1-2), 259-266 (2010)
   PUBMED   19911255
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Narikiyo,T., Kitamura,K., Adachi,M., Miyoshi,T., Iwashita,K.,
            Shiraishi,N., Nonoguchi,H., Chen,L.M., Chai,K.X., Chao,J. and
            Tomita,K.
  TITLE     Regulation of prostasin by aldosterone in the kidney
  JOURNAL   J Clin Invest 109 (3), 401-408 (2002)
   PUBMED   11828000
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Chen,L.M. and Chai,K.X.
  TITLE     Prostasin serine protease inhibits breast cancer invasiveness and
            is transcriptionally regulated by promoter DNA methylation
  JOURNAL   Int J Cancer 97 (3), 323-329 (2002)
   PUBMED   11774283
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Mok,S.C., Chao,J., Skates,S., Wong,K., Yiu,G.K., Muto,M.G.,
            Berkowitz,R.S. and Cramer,D.W.
  TITLE     Prostasin, a potential serum marker for ovarian cancer:
            identification through microarray technology
  JOURNAL   J Natl Cancer Inst 93 (19), 1458-1464 (2001)
   PUBMED   11584061
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Adachi,M., Kitamura,K., Miyoshi,T., Narikiyo,T., Iwashita,K.,
            Shiraishi,N., Nonoguchi,H. and Tomita,K.
  TITLE     Activation of epithelial sodium channels by prostasin in Xenopus
            oocytes
  JOURNAL   J Am Soc Nephrol 12 (6), 1114-1121 (2001)
   PUBMED   11373334
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Laribi,A., Berteau,P., Gala,J., Eschwege,P., Benoit,G., Tombal,B.,
            Schmitt,F. and Loric,S.
  TITLE     Blood-borne RT-PCR assay for prostasin- specific transcripts to
            identify circulating prostate cells in cancer patients
  JOURNAL   Eur Urol 39 (1), 65-71 (2001)
   PUBMED   11173941
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB017638.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB017638.1, BC061800.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132262,
                                           SAMD00132266 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..342
                     /product="prostasin precursor"
                     /function="serine protease"
                     /note="prostasin; channel-activating protease 1; protease,
                     serine, 8"
                     /calculated_mol_wt=33782
     sig_peptide     1..29
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ES87.3)"
                     /calculated_mol_wt=3079
     mat_peptide     33..322
                     /product="Prostasin. /id=PRO_0000240513"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES87.3)"
                     /calculated_mol_wt=31247
     Region          45..284
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            45
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(85,134,238)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ES87.3)"
     Site            order(232,257,259)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES87.3)"
     CDS             1..342
                     /gene="Prss8"
                     /gene_synonym="CAP1"
                     /coded_by="NM_138836.1:224..1252"
                     /db_xref="GeneID:192107"
                     /db_xref="RGD:619973"
ORIGIN      
        1 malrvglglg qlealfilll igllqsriga dgteascgav iqpritgggs akpgqwpwqv
       61 sityngvhvc ggslvsnqwv vsaahcfpre hskeeyevkl gahqldsfsn divvhtvaqi
      121 ishssyreeg sqgdialirl sspvtfsryi rpiclpaana sfpnglhctv tgwghvapsv
      181 slqtprplqq levplisret csclyninav peephtiqqd mlcagyvkgg kdacqgdsgg
      241 plscpidglw ylagivswgd acgapnrpgv ytltstyasw ihhhvaelqp ravpqtqesq
      301 pdghlcnhhp vfnlaaaqkl srpilflpls ltlglfslwl eh
//
LOCUS       NP_062141                970 aa            linear   ROD 28-APR-2025
DEFINITION  sodium/calcium exchanger 1 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_062141
VERSION     NP_062141.3
DBSOURCE    REFSEQ: accession NM_019268.4
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Yijian,L., Weihan,S., Lin,Y., Heng,Z., Yu,W., Lin,S., Shuo,M.,
            Mengyang,L. and Jianxun,W.
  TITLE     CircNCX1 modulates cardiomyocyte proliferation through promoting
            ubiquitination of BRG1
  JOURNAL   Cell Signal 120, 111193 (2024)
   PUBMED   38679350
  REMARK    GeneRIF: CircNCX1 modulates cardiomyocyte proliferation through
            promoting ubiquitination of BRG1.
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Kang,Q., Zhang,J., Xie,C., Fang,S. and Chai,W.
  TITLE     Circular RNA SLC8A1 triggers hippocampal neuronal ferroptosis by
            regulating FUS-mediated ATF3 mRNA stability in epilepsy
  JOURNAL   Exp Cell Res 434 (1), 113848 (2024)
   PUBMED   37918704
  REMARK    GeneRIF: Circular RNA SLC8A1 triggers hippocampal neuronal
            ferroptosis by regulating FUS-mediated ATF3 mRNA stability in
            epilepsy.
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Yang,L., Zhang,L., Zhu,J., Wang,Y., Zou,N., Liu,Z. and Wang,Y.
  TITLE     Abnormal expression and role of MicroRNA-214-3p/SLC8A1 in neonatal
            Hypoxic-Ischaemic encephalopathy
  JOURNAL   Int J Exp Pathol 104 (4), 199-208 (2023)
   PUBMED   37032493
  REMARK    GeneRIF: Abnormal expression and role of MicroRNA-214-3p/SLC8A1 in
            neonatal Hypoxic-Ischaemic encephalopathy.
REFERENCE   4  (residues 1 to 970)
  AUTHORS   Petrozziello,T., Boscia,F., Tedeschi,V., Pannaccione,A., de
            Rosa,V., Corvino,A., Severino,B., Annunziato,L. and Secondo,A.
  TITLE     Na+/Ca2+ exchanger isoform 1 takes part to the Ca2+-related
            prosurvival pathway of SOD1 in primary motor neurons exposed to
            beta-methylamino-L-alanine
  JOURNAL   Cell Commun Signal 20 (1), 8 (2022)
   PUBMED   35022040
  REMARK    GeneRIF: Na(+)/Ca(2+) exchanger isoform 1 takes part to the
            Ca(2+)-related prosurvival pathway of SOD1 in primary motor neurons
            exposed to beta-methylamino-L-alanine.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 970)
  AUTHORS   Tedeschi,V., Sisalli,M.J., Pannaccione,A., Piccialli,I.,
            Molinaro,P., Annunziato,L. and Secondo,A.
  TITLE     Na+/Ca2+ exchanger isoform 1 (NCX1) and canonical transient
            receptor potential channel 6 (TRPC6) are recruited by STIM1 to
            mediate Store-Operated Calcium Entry in primary cortical neurons
  JOURNAL   Cell Calcium 101, 102525 (2022)
   PUBMED   34995919
  REMARK    GeneRIF: Na(+)/Ca(2+) exchanger isoform 1 (NCX1) and canonical
            transient receptor potential channel 6 (TRPC6) are recruited by
            STIM1 to mediate Store-Operated Calcium Entry in primary cortical
            neurons.
REFERENCE   6  (residues 1 to 970)
  AUTHORS   Furman,I., Cook,O., Kasir,J., Low,W. and Rahamimoff,H.
  TITLE     The putative amino-terminal signal peptide of the cloned rat brain
            Na(+)-Ca2+ exchanger gene (RBE-1) is not mandatory for functional
            expression
  JOURNAL   J Biol Chem 270 (32), 19120-19127 (1995)
   PUBMED   7642578
REFERENCE   7  (residues 1 to 970)
  AUTHORS   Lee,S.L., Yu,A.S. and Lytton,J.
  TITLE     Tissue-specific expression of Na(+)-Ca2+ exchanger isoforms
  JOURNAL   J Biol Chem 269 (21), 14849-14852 (1994)
   PUBMED   8195112
REFERENCE   8  (residues 1 to 970)
  AUTHORS   Kieval,R.S., Bloch,R.J., Lindenmayer,G.E., Ambesi,A. and
            Lederer,W.J.
  TITLE     Immunofluorescence localization of the Na-Ca exchanger in heart
            cells
  JOURNAL   Am J Physiol 263 (2 Pt 1), C545-C550 (1992)
   PUBMED   1514597
REFERENCE   9  (residues 1 to 970)
  AUTHORS   Komuro,I., Wenninger,K.E., Philipson,K.D. and Izumo,S.
  TITLE     Molecular cloning and characterization of the human cardiac
            Na+/Ca2+ exchanger cDNA
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4769-4773 (1992)
   PUBMED   1374913
REFERENCE   10 (residues 1 to 970)
  AUTHORS   Nicoll,D.A., Longoni,S. and Philipson,K.D.
  TITLE     Molecular cloning and functional expression of the cardiac
            sarcolemmal Na(+)-Ca2+ exchanger
  JOURNAL   Science 250 (4980), 562-565 (1990)
   PUBMED   1700476
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Jul 31, 2012 this sequence version replaced NP_062141.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..970
                     /product="sodium/calcium exchanger 1 isoform 1 precursor"
                     /note="sodium/calcium exchanger 1; Na-Ca exchanger;
                     Na(+)/Ca(2+)-exchange protein 1; solute carrier family 8
                     (sodium/calcium exchanger), member 1; solute carrier
                     family 8 member 1"
                     /calculated_mol_wt=104511
     Region          1..970
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3563
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            72..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            134..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          138..178
                     /region_name="Alpha-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            168..188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          251..270
                     /region_name="Putative calmodulin-binding region.
                     /evidence=ECO:0000250|UniProtKB:P23685"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70414; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70414; propagated from
                     UniProtKB/Swiss-Prot (Q01728.3)"
     Site            798..818
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            822..842
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Region          839..875
                     /region_name="Alpha-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            872..892
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            904..924
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     Site            942..962
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01728.3)"
     CDS             1..970
                     /gene="Slc8a1"
                     /gene_synonym="Ncx; Ncx1"
                     /coded_by="NM_019268.4:35..2947"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:29715"
                     /db_xref="RGD:3717"
ORIGIN      
        1 mlrlslppnv smgfrlvtlv allfthvdhi tadteaetgg nettectgsy yckkgvilpi
       61 wepqdpsfgd kiaratvyfv amvymflgvs iiadrfmssi evitsqekei tikkpngett
      121 kttvriwnet vsnltlmalg ssapeillsv ievcghnfta gdlgpstivg saafnmfiii
      181 alcvyvvpdg etrkikhlrv ffvtaawsif aytwlyiils vsspgvvevw eglltffffp
      241 icvvfawvad rrllfykyvy kryragkqrg miiehegdrp askteiemdg kvvnshvdnf
      301 ldgalvlevd erdqddeear remarilkel kqkhpdkeie qlielanyqv lsqqqksraf
      361 yriqatrlmt gagnilkrha adqarkavsm hevnmdvven dpvskvffeq gtyqclencg
      421 tvaltiirrg gdltntvfvd frtedgtana gsdyeftegt vifkpgetqk eirvgiiddd
      481 ifeedenflv hlsnvrvsse vsedgildsn hvsaiaclgs pntatitifd ddhagiftfe
      541 epvthvsesi gimevkvlrt sgargnviip yktiegtarg ggedfedtcg elefqndeiv
      601 ktisvkvidd eeyeknktff ieigeprlve msekkallln elggftltgk kmygqpvfrk
      661 vhardhpips tvisiseeyd dkqpltskee eerriaemgr pilgehtkle viieesyefk
      721 stvdklikkt nlalvvgtns wreqfieait vsageddddd ecgeeklpsc fdyvmhfltv
      781 fwkvlfafvp pteywngwac fivsilmigl ltafigdlas hfgctiglkd svtavvfval
      841 gtsvpdtfas kvaatqdqya dasignvtgs navnvflgig vawsiaaiyh aangeqfkvs
      901 pgtlafsvtl ftifafinvg vllyrrrpei ggelggprta klltsslfvl lwllyiffss
      961 leaychikgf
//
LOCUS       NP_071777               2325 aa            linear   ROD 28-APR-2025
DEFINITION  myomegalin isoform 1 [Rattus norvegicus].
ACCESSION   NP_071777 XP_346635
VERSION     NP_071777.2
DBSOURCE    REFSEQ: accession NM_022382.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2325)
  AUTHORS   Bouguenina,H., Salaun,D., Mangon,A., Muller,L., Baudelet,E.,
            Camoin,L., Tachibana,T., Cianferani,S., Audebert,S.,
            Verdier-Pinard,P. and Badache,A.
  TITLE     EB1-binding-myomegalin protein complex promotes centrosomal
            microtubules functions
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10687-E10696 (2017)
   PUBMED   29162697
REFERENCE   2  (residues 1 to 2325)
  AUTHORS   Wu,J., de Heus,C., Liu,Q., Bouchet,B.P., Noordstra,I., Jiang,K.,
            Hua,S., Martin,M., Yang,C., Grigoriev,I., Katrukha,E.A.,
            Altelaar,A.F.M., Hoogenraad,C.C., Qi,R.Z., Klumperman,J. and
            Akhmanova,A.
  TITLE     Molecular Pathway of Microtubule Organization at the Golgi
            Apparatus
  JOURNAL   Dev Cell 39 (1), 44-60 (2016)
   PUBMED   27666745
REFERENCE   3  (residues 1 to 2325)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    GeneRIF: MMGL isoform 4 is involved in the phosphorylation of
            Cardiac Myosin Binding Protein-C as well as cardiac troponin I.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2325)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   5  (residues 1 to 2325)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   6  (residues 1 to 2325)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Dec 1, 2020 this sequence version replaced NP_071777.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF139185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2325
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2325
                     /product="myomegalin isoform 1"
                     /note="phosphodiesterase-binding protein clone 46;
                     myomegalin"
                     /calculated_mol_wt=262130
     Region          6..73
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          58..>524
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          314..1040
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1556..1621
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1876..>2055
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..2325
                     /gene="Pde4dip"
                     /coded_by="NM_022382.2:187..7164"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64183"
                     /db_xref="RGD:708410"
ORIGIN      
        1 msngyrtlsq hlndlkkenf slklriyfle ermqqkyevs redvykrnie lkveveslkr
       61 elqdrkqhlh ktwadeedln sqneaelrrq veepqqeteh vyelldnniq llqeesrfak
      121 deatqmetlv eaekgcnlel serwkdatkn redapgdqvk ldqysaalaq rdrrieelrq
      181 slaaqeglve qlsrekqqll hlleepggme vqpmpkglpt qqkpdlnetp ttqpsvsdsh
      241 laelqdkiqq tevtnkilqe klndmscelr saqessqkqd ttiqslkeml ksreseteel
      301 yqviegqndt maklremlhq sqlgqlqsse giapaqqqva lldlqsalfc sqleiqklqr
      361 llrqkerqla dgkrcmqfve aaaqereqqk eaawkhnqel rkalqhlqge lhsksqqlhv
      421 leaekyneir tqgqniqhls hslshkeqli qelqellqyr dttdktldtn evfleklrqr
      481 iqdravaler videkfsale ekdkelrqlr lavrdrdhdl erlrcvlsan eatmqsmesl
      541 lrargleveq ltatcqnlqw lkeeletkfg hwqkeqesii qqlqtslhdr nkevedlsat
      601 llhklgpgqs evaeelcqrl qrkervlqdl lsdrnkqame hemevqgllq smgtreqerq
      661 avaekmvqaf mernselqal rqylggkelm aasqafisnq pagatsvgph hgeqtdqgst
      721 qmpsrddsts ltareeasip rstlgdsdtv aglekelsna keelelmakk eresqielsa
      781 lqsmmavqee elqvqaadle sltrniqike dlikdlqmql vdpedmpame rltqevlllr
      841 ekvasvepqg qegsenrrqq lllmleglvd ersrlnealq aerqlysslv kfhaqpetse
      901 rdrtlqvele gaqvlrsrle evlgrslerl srletlaaig gatagdeted tstqftdsie
      961 eeaahnshqq likvsleksl ttmetqntcl qppspvgedg nrhlqeemlh lraeihqhle
     1021 ekrkaeaelk elkaqieeag fssvshirnt mlslclenae lkeqmgeams dgweveedke
     1081 kgevmvetvv akgglsedsl qaefrkvqgr lksayniinl lkeqlvlrss egntkempef
     1141 lvrlarevdr mnmglpssek hqhqeqenmt arpgprpqsl klgtalsvdg yqlenksqaq
     1201 dsghqpqfsl pgstkhlrsq laqcrqryqd lqekllisea tvfaqanqle kyrailsesl
     1261 vkqdskqiqv dlqdlgyetc grseneaere ettspeceeh gnlrpvvlve glcseqgyld
     1321 pvlvsspvkk plenkpgkre efqaqgtsdd ssllrkdird lkaqlqnayk viqnlrsrvr
     1381 slsatsdyss slerprklra vatlegasph svtdedegwl sdgtgafypp glqakknlen
     1441 liqrvsqlea qlpktglegk laeelrsasw pgkydsliqd qarelsylrq kiregrgicy
     1501 lltqhskdtv ksfedllrsn didyylgqsf reqlaqggql tdrltsklst kdhksekeea
     1561 gleplalrls relqekekvi evlqakldtr slsppsshaa sdshrsasst sflsddieac
     1621 sdmdvaseyt hyeekkpsps nsaasasqgl kgeprsssis lptpqnppke asqaqpgfhf
     1681 nsipkpasls qapmhftvps fmpfgpsgpp llgccetpvv slaeaqqelq mlqkqlgesv
     1741 siapptstst llsnhteass prysnpaqph spargtielg rilepgylgs gqwdmmrpqk
     1801 gsisgelssg ssmyqlnskp tgadlleehl geirnlrqrl eesicvndrl reqlqhrlss
     1861 tarengstsh fysqglesmp qlynenralr eenqslqtrl shasrghsqe vdhlrealls
     1921 sssqlqelek eleqqkaerr qlledlqekq deivhfreer lslqennsrl qhklallqqq
     1981 ceekqqlsls lqselqiyes lyenpkkglk afsldscyqv pgelsclvae iralrvqleq
     2041 siqvnnrlrl qleqqmdhga gkaslsscpv nqsfsakael anqqppfqgs aasppvrdvg
     2101 lnspavvlps nscsvpgsds aiisrtnngs desaatktpp kmevdaadgp fasghgrhvi
     2161 ghvddydtlq qqigegklli qkilsltrpa rsvpaldaqg teapgtksvh elrssaraln
     2221 hsleesasll tmfwraalpn shgsvlvgee gklmekelld lraqvsqqqq llqstavrlk
     2281 tanqrkksme qfivshltrt hdvlkkartn lemksfralm ctpal
//
LOCUS       NP_001417175             368 aa            linear   ROD 28-APR-2025
DEFINITION  T-cell immunoglobulin and mucin domain containing 4 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_001417175 XP_038943082
VERSION     NP_001417175.1
DBSOURCE    REFSEQ: accession NM_001430246.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Kawano,M. and Nagata,S.
  TITLE     Lupus-like autoimmune disease caused by a lack of Xkr8, a
            caspase-dependent phospholipid scramblase
  JOURNAL   Proc Natl Acad Sci U S A 115 (9), 2132-2137 (2018)
   PUBMED   29440417
REFERENCE   2  (residues 1 to 368)
  AUTHORS   DICKIES,M.M.
  TITLE     A new viable yellow mutation in the house mouse
  JOURNAL   J Hered 53, 84-86 (1962)
   PUBMED   13886198
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 8, 2024 this sequence version replaced XP_038943082.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.34533.1,
                                           SRR26643299.42208.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q21"
     Protein         1..368
                     /product="T-cell immunoglobulin and mucin domain
                     containing 4 isoform 1 precursor"
                     /note="T-cell immunoglobulin and mucin domain-containing
                     protein 4"
                     /calculated_mol_wt=37820
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2702
     Region          29..129
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          51..55
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          95..99
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..114
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          124..127
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..368
                     /gene="Timd4"
                     /gene_synonym="AABR07072096.1; RGD1564516"
                     /coded_by="NM_001430246.1:14..1120"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:497891"
                     /db_xref="RGD:1564516"
ORIGIN      
        1 mskgllllwl vmelwllclt paasedtiig flgqsvtlpc qysswsqsrn smcwgrgscp
       61 gskcngellr tdgtrtisrk sgkytlwgsi rlgdvsltis ntnqddsgvy ccrievpgwf
      121 ndvkktvrle lrratttkrp ttttrlttrp ttqpttrptt tpyltttpep lpttvmttpd
      181 ptttaqpqtl attavgtavt mypstmpgsf sqkttsfstt eiftkgsait aesetlsafn
      241 nsqrsgmtis tdtalvrptg skawilssts qlmtqkttlt attrresskk tgelykiedr
      301 qtniliiacc vgfvlmvllf lafllrgkva eanclrrhrr pdntedtplr gnrdcemdql
      361 engtccqt
//
LOCUS       NP_001419277             640 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 431 like 14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419277 XP_038952237
VERSION     NP_001419277.1
DBSOURCE    REFSEQ: accession NM_001432348.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Jul 30, 2024 this sequence version replaced XP_038952237.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.36138.1,
                                           SRR26360194.1618711.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..640
                     /product="zinc finger protein 431 like 14 isoform 2"
                     /note="zinc finger protein 431-like"
                     /calculated_mol_wt=75409
     Region          28..68
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          165..185
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          197..213
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          217..624
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          221..241
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(226,228,230,232..233,236..237,240,254,256,260..261,
                     264..265,268,282,284,286,288..289,292..293,296)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          249..269
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          277..297
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          305..325
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(310,312,314,316..317,320..321,324,338,340,344..345,
                     348..349,352,366,368,370,372..373,376..377,380)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          333..353
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          361..381
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          389..409
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(394,396,398,400..401,404..405,408,422,424,428..429,
                     432..433,436,450,452,454,456..457,460..461,464)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          417..437
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          445..465
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          473..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          501..521
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(506,508,510,512..513,516..517,520,534,536,540..541,
                     544..545,548,562,564,566,568..569,572..573,576)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          529..549
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..577
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          585..605
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          613..633
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..640
                     /gene="Znf431l14"
                     /coded_by="NM_001432348.1:43..1965"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:120097793"
                     /db_xref="RGD:40939685"
ORIGIN      
        1 miglmcfdvc crmsygragn llirnmtvtf edvhvnftqe ewalldpfqk klykdvmlet
       61 yrnlnaigfn weeqnieehc qrsrrqkryf lyarhersqs aeipseythc gkpfashahs
      121 hpqknerihs ekkpseviqc veayapytil qihkrtqarq kpyecsqrgk vfanhiklkk
      181 herlhterep ykynefdkay srpsslqkhk rvhtgekpyk cnecdkafsr pssfqkhkrv
      241 htgekpykcn ecdkafsqps rlqqhkniht gekpfkcnec dkafsrpsrl kqhkyihtge
      301 kpykcnecdk afsehsslqm hkrvhtgekp ykcnecdraf svrsnlqkhk rvhtgekpyk
      361 cnecdkafsr psrlkqhkyi htgekpykcn ecdkafsrps slqthksvht gekpykcnec
      421 dkafsghsnl qkhkrvhtge kpykcnecdk afsetsslqk hkrlhtgekp ykcnecdkaf
      481 svhsilwkhk rvhtgekpye cnecdkafsd hsslqshkrv htgekpykcn ecdkafsrss
      541 slqkhkrvht gekpykcnec dkafsrpssl qkhkrvhtge kpykcneydk afsvhcslwm
      601 hkrvhtgekp ykcnecdkaf srpsrlqqhk sshwtetlev
//
LOCUS       NP_001382570             349 aa            linear   ROD 28-APR-2025
DEFINITION  ETS translocation variant 3-like protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001382570
VERSION     NP_001382570.1
DBSOURCE    REFSEQ: accession NM_001395641.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.12708.1,
                                           SRR26360181.2425487.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..349
                     /product="ETS translocation variant 3-like protein isoform
                     1"
                     /note="ets variant gene 3-like; ETS translocation variant
                     3-like protein; ets variant 3-like"
                     /calculated_mol_wt=39458
     Region          70..156
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..349
                     /gene="Etv3l"
                     /gene_synonym="RGD1562620"
                     /coded_by="NM_001395641.1:378..1427"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:499651"
                     /db_xref="RGD:1562620"
ORIGIN      
        1 mdlqrphrel rrkhrkqpsl qsklnpllpp tmycncfseg iraapvnywi sglafpdway
       61 kaesspgsrq iqlwhfilel lqkeefrhvi awqqgeygef vikdpdevar lwgrrkckpq
      121 mnydklsral ryyynkrilh ktkgkrftyk fnfsklivad cppwkvwtps tpclllrppa
      181 lcqtalvpva eqseplrsml ctratgtqpa rertppqppe asgdkdsssf ssfgsvlgpg
      241 wqnpcccfwn hqgdlpsfas fapvpclccn wahlsgpilp plsseqplle slkpgprlpg
      301 pmwmpgawhf pglhllarlr qgteapevpq apgiggkswp rakqapgfq
//
LOCUS       NP_001418980             774 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 606 isoform b [Rattus norvegicus].
ACCESSION   NP_001418980 XP_038956598
VERSION     NP_001418980.1
DBSOURCE    REFSEQ: accession NM_001432051.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Gebelein,B., Mesa,K. and Urrutia,R.
  TITLE     A novel profile of expressed sequence tags for zinc finger encoding
            genes from the poorly differentiated exocrine pancreatic cell line
            AR4IP
  JOURNAL   Cancer Lett 105 (2), 225-231 (1996)
   PUBMED   8697448
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 25, 2024 this sequence version replaced XP_038956598.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.1200.1,
                                           SRR26643296.674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..774
                     /product="zinc finger protein 606 isoform b"
                     /calculated_mol_wt=89627
     Region          44..103
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          373..772
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          386..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          441..461
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(446,448,450,452..453,456..457,460,474,476,480..481,
                     484..485,488,502,504,506,508..509,512..513,516)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          525..545
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          553..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          581..601
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          609..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(614,616,618,620..621,624..625,628,642,644,648..649,
                     652..653,656,670,672,674,676..677,680..681,684)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          637..657
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          665..685
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          693..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          721..741
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          749..769
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..774
                     /gene="Zfp606"
                     /gene_synonym="Znf606"
                     /coded_by="NM_001432051.1:146..2470"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:292610"
                     /db_xref="RGD:1309810"
ORIGIN      
        1 mdqsdpsvsw alcpqdpawh iegspeesrr qadglqtaqd qepvtfkdva vaftqeeweq
       61 ldlvqrtlyr dvmletyghl lsvgnqiakp evislleqee pwsleqgypk sscpewmrnv
      121 eskalipaqs vfeeeqssng mvleryiwdn pwlsrlgvlg ygdqiemyhm nqnagmremv
      181 fmqkqvlsqr gsefcklgte ysqslnlipp qrvsqlehfy ksdthletwr cnsaimyadk
      241 vtcenidyek afcqsvqpvy paklqtrdnm fkctdavksf nhiiqfgdhk avhtgeklyg
      301 ykeyhqifnq spsliehprf qiggnqyeky keygnifyfs sfmehqnigg vekaykynew
      361 ekvfgydsll aqhtstytae kpyefnkcgt sfiwssyliq hkkthpgdkp yecdkcrkvf
      421 rnrsaltkhe rthtgikpye cnkcgkafsw nshlivhtri htgekpyvcn ecgksfnwns
      481 hlighqrtht gekpfectec gksfswsshl iahmrmhtge kpfkcdecek afrdysalsk
      541 herthsgakp ykctecgksf swsshliahq rthtgekpyn cqecgkafre rsaltkheii
      601 hsgikpyecn kcgkscsqma hlvrhqrtht gekpyecnkc gksfsqschl vahrrihtge
      661 kpykcnqcer sfncsshlia hrrthtgekp yrcnecgkaf nessslivhl rnhtgekpyk
      721 cihcekafck nssliihqrm hsgekrficn qcgrafsghs allqhqknhs eekl
//
LOCUS       NP_001102389             927 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein kinase/endoribonuclease IRE2 precursor
            [Rattus norvegicus].
ACCESSION   NP_001102389 XP_001079523 XP_344960
VERSION     NP_001102389.1
DBSOURCE    REFSEQ: accession NM_001108919.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Niu,J., Wu,Z., Xue,H., Zhang,Y., Gao,Q., Li,C. and Zhao,P.
  TITLE     Sevoflurane post-conditioning alleviated hypoxic-ischemic brain
            injury in neonatal rats by inhibiting endoplasmic reticulum
            stress-mediated autophagy via IRE1 signalings
  JOURNAL   Neurochem Int 150, 105198 (2021)
   PUBMED   34601014
  REMARK    GeneRIF: Sevoflurane post-conditioning alleviated hypoxic-ischemic
            brain injury in neonatal rats by inhibiting endoplasmic reticulum
            stress-mediated autophagy via IRE1 signalings.
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Nishitoh,H., Matsuzawa,A., Tobiume,K., Saegusa,K., Takeda,K.,
            Inoue,K., Hori,S., Kakizuka,A. and Ichijo,H.
  TITLE     ASK1 is essential for endoplasmic reticulum stress-induced neuronal
            cell death triggered by expanded polyglutamine repeats
  JOURNAL   Genes Dev 16 (11), 1345-1355 (2002)
   PUBMED   12050113
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Bertolotti,A., Wang,X., Novoa,I., Jungreis,R., Schlessinger,K.,
            Cho,J.H., West,A.B. and Ron,D.
  TITLE     Increased sensitivity to dextran sodium sulfate colitis in
            IRE1beta-deficient mice
  JOURNAL   J Clin Invest 107 (5), 585-593 (2001)
   PUBMED   11238559
REFERENCE   4  (residues 1 to 927)
  AUTHORS   Iwawaki,T., Hosoda,A., Okuda,T., Kamigori,Y., Nomura-Furuwatari,C.,
            Kimata,Y., Tsuru,A. and Kohno,K.
  TITLE     Translational control by the ER transmembrane kinase/ribonuclease
            IRE1 under ER stress
  JOURNAL   Nat Cell Biol 3 (2), 158-164 (2001)
   PUBMED   11175748
REFERENCE   5  (residues 1 to 927)
  AUTHORS   Urano,F., Wang,X., Bertolotti,A., Zhang,Y., Chung,P., Harding,H.P.
            and Ron,D.
  TITLE     Coupling of stress in the ER to activation of JNK protein kinases
            by transmembrane protein kinase IRE1
  JOURNAL   Science 287 (5453), 664-666 (2000)
   PUBMED   10650002
REFERENCE   6  (residues 1 to 927)
  AUTHORS   Wang,X.Z., Harding,H.P., Zhang,Y., Jolicoeur,E.M., Kuroda,M. and
            Ron,D.
  TITLE     Cloning of mammalian Ire1 reveals diversity in the ER stress
            responses
  JOURNAL   EMBO J 17 (19), 5708-5717 (1998)
   PUBMED   9755171
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473956.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001079523.1, XP_344960.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5756307, SAMEA5760383
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..927
                     /product="serine/threonine-protein kinase/endoribonuclease
                     IRE2 precursor"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase/endoribonuclease
                     IRE2; endoplasmic reticulum (ER) to nucleus signalling 2"
                     /calculated_mol_wt=99452
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3645
     Region          37..365
                     /region_name="Luminal_IRE1"
                     /note="The Luminal domain, a dimerization domain, of the
                     Serine/Threonine protein kinase, Inositol-requiring
                     protein 1; cd09769"
                     /db_xref="CDD:188875"
     Site            order(113..117,123,125..128,130..132,144,146..148,151,
                     159..160,168,170,185,187..189)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:188875"
     Region          507..771
                     /region_name="STKc_IRE1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inositol-requiring protein 1; cd13982"
                     /db_xref="CDD:270884"
     Site            order(507,530..531,533,556..557,559,561,566..570,582,613,
                     616..617,620..621,645,762,765)
                     /site_type="other"
                     /note="dimer interface (back-to-back) [polypeptide
                     binding]"
                     /db_xref="CDD:270884"
     Site            order(513,527,662..663,691,735..737,760)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:270884"
     Site            order(516..520,525,536,538,565,581..584,587,589,627,629,
                     631..632,634,650,653,672..675)
                     /site_type="active"
                     /db_xref="CDD:270884"
     Site            order(516..520,523,525,536,538,565,581..582,584,587,
                     631..632,634,650)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270884"
     Site            order(518,521..522,524,539,541,573,575..576,717..718,
                     720..721,724)
                     /site_type="other"
                     /note="dimer interface (face-to-face) [polypeptide
                     binding]"
                     /db_xref="CDD:270884"
     Site            order(520,587,589,627,629,631,653,672..675)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270884"
     Site            order(649..664,668..675)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270884"
     Region          774..899
                     /region_name="RNase_Ire1"
                     /note="RNase domain (also known as the kinase extension
                     nuclease domain) of Ire1; cd10422"
                     /db_xref="CDD:199217"
     Site            order(774..775,778,782,846,864,894,897..898)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:199217"
     Site            order(776,872,876,879..880,884)
                     /site_type="other"
                     /note="kinase interface [polypeptide binding]"
                     /db_xref="CDD:199217"
     Site            order(778,782,785..786,843,846..847,850,863..865,893..894,
                     897)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:199217"
     CDS             1..927
                     /gene="Ern2"
                     /coded_by="NM_001108919.1:26..2809"
                     /db_xref="GeneID:365363"
                     /db_xref="RGD:1308743"
ORIGIN      
        1 marpvqsfql wsalgfllql aiflgklgpq vqsvrpesll fvstldgslh alnkqtgdlk
       61 wtvkddpiiq gpmyvtemaf lsdpadgsly ilgtqkqqgl mklpftipel vhaspcrssd
      121 gvfytgrkqd awfvvdpesg etqmtltteg fstpqlyigr tqytvsmhdp rtptlrwntt
      181 yrrysappvd gspgkymshl tscgmglllt vdpgsgtvlw tqdlgvpvtg iytwhqdglr
      241 qlphltlard tlhflvlrwg hirlpasssq dtvtqfssld tellmtlyvg keeagfyvsk
      301 alvhagvalv prgltlapmd gpttdevtvq vsgeregsps tavrypsgsv alpsqwllig
      361 yhepppvlht tmlrvqrtpg kgsadtrdsd dlhapalsfe flnlkreepw dpelhpeeka
      421 dtypglgsqd llaasftail lgawvlylmr qqqqspsapa gpsdlpqdtq vqlsrdtlqn
      481 qrrfqsppep vqpahdpeae qptvvgkisf npkdvlgrga ggtfvfrgqf egravavkrl
      541 lrecfslvqr evqllqesdr hpnvlryfct eqgpqfhyia lelcqaslqe yvespdldrw
      601 glgptmvlqq mmsglahlhs lhivhrdlkp gnilmagpds qgqgrvvisd fglckklpag
      661 rcsfslhsgi pgtegwmape llqlppdspt savdifsagc vfyyvlsggs hpfgeslyrq
      721 anilsgdhcl aqlqeethdk vvaldlvkam lsllpqdrps agwvlahplf wsrakelqff
      781 qdvsdwleke peqgplvtal eagsykvvre nwykhisapl qedlkrfrsy kgtsvrdllr
      841 amrnkkhhyr elptevrqtl gqlpagfaqy ftqrfprlll hthramrtca seslflpyyp
      901 aaleargscq vpqraetprg pkgrprs
//
LOCUS       NP_001101769             486 aa            linear   ROD 28-APR-2025
DEFINITION  ETS translocation variant 4 [Rattus norvegicus].
ACCESSION   NP_001101769 XP_001081496 XP_340911
VERSION     NP_001101769.1
DBSOURCE    REFSEQ: accession NM_001108299.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Kandemir,B., Davis,S., Yigit,E.N., Ozturk,G., Yilmaz,B., Laroche,S.
            and Kurnaz,I.A.
  TITLE     Expression of Pea3 protein subfamily members in hippocampus and
            potential regulation following neuronal stimulation
  JOURNAL   Neurosci Lett 738, 135348 (2020)
   PUBMED   32891673
  REMARK    GeneRIF: Expression of Pea3 protein subfamily members in
            hippocampus and potential regulation following neuronal
            stimulation.
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Fontanet,P.A., Rios,A.S., Alsina,F.C., Paratcha,G. and Ledda,F.
  TITLE     Pea3 Transcription Factors, Etv4 and Etv5, Are Required for Proper
            Hippocampal Dendrite Development and Plasticity
  JOURNAL   Cereb Cortex 28 (1), 236-249 (2018)
   PUBMED   27909004
  REMARK    GeneRIF: This study demonstrates that Etv4 and Etv5 transcription
            factors are expressed in hippocampal pyramidal neurons during the
            main period of dendritogenesis; reveals a novel role for Etv4 and
            Etv5 transcription factors for hippocampal circuit development and
            the coordination of synaptic maturation; and indicates that both
            factors are essential in the transcriptional program linking BDNF
            signaling to dendrite development.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Xu,B., Washington,A.M. and Hinton,B.T.
  TITLE     PTEN signaling through RAF1 proto-oncogene serine/threonine kinase
            (RAF1)/ERK in the epididymis is essential for male fertility
  JOURNAL   Proc Natl Acad Sci U S A 111 (52), 18643-18648 (2014)
   PUBMED   25512490
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Park,S.W., Do,H.J., Ha,W.T., Han,M.H., Park,K.H., Song,H., Kim,N.H.
            and Kim,J.H.
  TITLE     Transcriptional activation of OCT4 by the ETS transcription factor
            PEA3 in NCCIT human embryonic carcinoma cells
  JOURNAL   FEBS Lett 588 (17), 3129-3136 (2014)
   PUBMED   24983502
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Fontanet,P., Irala,D., Alsina,F.C., Paratcha,G. and Ledda,F.
  TITLE     Pea3 transcription factor family members Etv4 and Etv5 mediate
            retrograde signaling and axonal growth of DRG sensory neurons in
            response to NGF
  JOURNAL   J Neurosci 33 (40), 15940-15951 (2013)
   PUBMED   24089499
  REMARK    GeneRIF: these data establish Etv4 and Etv5 as essential molecules
            of the transcriptional program linking neurotrophin signaling to
            sensory neuronal differentiation
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Perez,A., Barco,R., Fernandez,I., Price-Schiavi,S.A. and
            Carraway,K.L.
  TITLE     PEA3 transactivates the Muc4/sialomucin complex promoter in mammary
            epithelial and tumor cells
  JOURNAL   J Biol Chem 278 (38), 36942-36952 (2003)
   PUBMED   12855694
  REMARK    GeneRIF: expression of PEA3 in mammary tumors leads to
            up-regulation of Muc4/SMC transcription, the gene product of which
            may contribute to the metastatic potential of mammary tumors.
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Chotteau-Lelievre,A., Montesano,R., Soriano,J., Soulie,P.,
            Desbiens,X. and de Launoit,Y.
  TITLE     PEA3 transcription factors are expressed in tissues undergoing
            branching morphogenesis and promote formation of duct-like
            structures by mammary epithelial cells in vitro
  JOURNAL   Dev Biol 259 (2), 241-257 (2003)
   PUBMED   12871699
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Shou,Z., Yamada,K., Inazu,T., Kawata,H., Hirano,S., Mizutani,T.,
            Yazawa,T., Sekiguchi,T., Yoshino,M., Kajitani,T., Okada,K. and
            Miyamoto,K.
  TITLE     Genomic structure and analysis of transcriptional regulation of the
            mouse zinc-fingers and homeoboxes 1 (ZHX1) gene
  JOURNAL   Gene 302 (1-2), 83-94 (2003)
   PUBMED   12527199
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Livet,J., Sigrist,M., Stroebel,S., De Paola,V., Price,S.R.,
            Henderson,C.E., Jessell,T.M. and Arber,S.
  TITLE     ETS gene Pea3 controls the central position and terminal
            arborization of specific motor neuron pools
  JOURNAL   Neuron 35 (5), 877-892 (2002)
   PUBMED   12372283
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Arber,S., Han,B., Mendelsohn,M., Smith,M., Jessell,T.M. and
            Sockanathan,S.
  TITLE     Requirement for the homeobox gene Hb9 in the consolidation of motor
            neuron identity
  JOURNAL   Neuron 23 (4), 659-674 (1999)
   PUBMED   10482234
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_340911.3, XP_001081496.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..486
                     /product="ETS translocation variant 4"
                     /note="polyomavirus enhancer activator-3; ets variant gene
                     4 (E1A enhancer binding protein, E1AF)"
                     /calculated_mol_wt=53846
     Region          6..341
                     /region_name="ETS_PEA3_N"
                     /note="PEA3 subfamily ETS-domain transcription factor N
                     terminal domain; pfam04621"
                     /db_xref="CDD:461371"
     Region          343..426
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..486
                     /gene="Etv4"
                     /gene_synonym="Pea3"
                     /coded_by="NM_001108299.1:269..1729"
                     /db_xref="GeneID:360635"
                     /db_xref="RGD:1306524"
ORIGIN      
        1 merrmkggyl dqrvpytfcs kspgngslge almvpqgklm dpgslppsds edlfqdlshf
       61 qetwlaeaqv pdsdeqfvpd fhsenlafhs pttrikkepq sprtdpalsc srkpplsyhh
      121 geqclyssay dsprqiaiks papgapgqsp lqpfsraepq qsllrassss qshpghgylg
      181 ehssvfqqpv dmchaftspq gggreplpap yqhqlsepcp pypqqsfkqe yhdplyeqag
      241 qpaasqggvs ghrypgagvv ikqertdfay dsdvpgcasm ylhpegfsap ssgdgvmgyg
      301 yekslrpfpd dvcivpekfe gdikqegvga fregppyqrr galqlwqflv allddptnah
      361 fiawtgrgme fkliepeeva rlwgiqknrp amnydklsrs lryyyekgim qkvageryvy
      421 kfvcepealf slafpdnhrp alkaefdrpv seedtvplsh ldespaylpe lagpaqpfgh
      481 kggysy
//
LOCUS       NP_001385714             944 aa            linear   ROD 28-APR-2025
DEFINITION  neutral alpha-glucosidase AB isoform 2 [Rattus norvegicus].
ACCESSION   NP_001385714 XP_006231039
VERSION     NP_001385714.1
DBSOURCE    REFSEQ: accession NM_001398785.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Tian,W., Jiang,X., Sung,Y.K., Shuffle,E., Wu,T.H., Kao,P.N.,
            Tu,A.B., Dorfmuller,P., Cao,A., Wang,L., Peng,G., Kim,Y., Zhang,P.,
            Chappell,J., Pasupneti,S., Dahms,P., Maguire,P., Chaib,H.,
            Zamanian,R., Peters-Golden,M., Snyder,M.P., Voelkel,N.F.,
            Humbert,M., Rabinovitch,M. and Nicolls,M.R.
  TITLE     Phenotypically Silent Bone Morphogenetic Protein Receptor 2
            Mutations Predispose Rats to Inflammation-Induced Pulmonary
            Arterial Hypertension by Enhancing the Risk for Neointimal
            Transformation
  JOURNAL   Circulation 140 (17), 1409-1425 (2019)
   PUBMED   31462075
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Besse,W., Dong,K., Choi,J., Punia,S., Fedeles,S.V., Choi,M.,
            Gallagher,A.R., Huang,E.B., Gulati,A., Knight,J., Mane,S.,
            Tahvanainen,E., Tahvanainen,P., Sanna-Cherchi,S., Lifton,R.P.,
            Watnick,T., Pei,Y.P., Torres,V.E. and Somlo,S.
  TITLE     Isolated polycystic liver disease genes define effectors of
            polycystin-1 function
  JOURNAL   J Clin Invest 127 (5), 1772-1785 (2017)
   PUBMED   28375157
  REMARK    Erratum:[J Clin Invest. 2017 Sep 1;127(9):3558. doi:
            10.1172/JCI96729. PMID: 28862642]
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Caputo,A.T., Alonzi,D.S., Marti,L., Reca,I.B., Kiappes,J.L.,
            Struwe,W.B., Cross,A., Basu,S., Lowe,E.D., Darlot,B., Santino,A.,
            Roversi,P. and Zitzmann,N.
  TITLE     Structures of mammalian ER alpha-glucosidase II capture the binding
            modes of broad-spectrum iminosugar antivirals
  JOURNAL   Proc Natl Acad Sci U S A 113 (32), E4630-E4638 (2016)
   PUBMED   27462106
REFERENCE   4  (residues 1 to 944)
  AUTHORS   Porath,B., Gainullin,V.G., Cornec-Le Gall,E., Dillinger,E.K.,
            Heyer,C.M., Hopp,K., Edwards,M.E., Madsen,C.D., Mauritz,S.R.,
            Banks,C.J., Baheti,S., Reddy,B., Herrero,J.I., Banales,J.M.,
            Hogan,M.C., Tasic,V., Watnick,T.J., Chapman,A.B., Vigneau,C.,
            Lavainne,F., Audrezet,M.P., Ferec,C., Le Meur,Y., Torres,V.E. and
            Harris,P.C.
  CONSRTM   Genkyst Study Group, HALT Progression of Polycystic Kidney Disease
            Group; Consortium for Radiologic Imaging Studies of Polycystic
            Kidney Disease
  TITLE     Mutations in GANAB, Encoding the Glucosidase IIalpha Subunit, Cause
            Autosomal-Dominant Polycystic Kidney and Liver Disease
  JOURNAL   Am J Hum Genet 98 (6), 1193-1207 (2016)
   PUBMED   27259053
REFERENCE   5  (residues 1 to 944)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   6  (residues 1 to 944)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 944)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   8  (residues 1 to 944)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 944)
  AUTHORS   Pelletier,M.F., Marcil,A., Sevigny,G., Jakob,C.A., Tessier,D.C.,
            Chevet,E., Menard,R., Bergeron,J.J. and Thomas,D.Y.
  TITLE     The heterodimeric structure of glucosidase II is required for its
            activity, solubility, and localization in vivo
  JOURNAL   Glycobiology 10 (8), 815-827 (2000)
   PUBMED   10929008
REFERENCE   10 (residues 1 to 944)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 23, 2021 this sequence version replaced XP_006231039.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.5143.1,
                                           SRR26643294.5779.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..944
                     /product="neutral alpha-glucosidase AB isoform 2"
                     /EC_number="3.2.1.84"
                     /note="neutral alpha-glucosidase AB; alpha glucosidase 2
                     alpha neutral subunit; neutral AB; glucosidase, alpha;
                     neutral AB"
                     /calculated_mol_wt=106773
     Region          242..384
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            283
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          384..851
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(429,542,602,615,618,651,676)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     CDS             1..944
                     /gene="Ganab"
                     /gene_synonym="G2an"
                     /coded_by="NM_001398785.2:15..2849"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:293721"
                     /db_xref="RGD:1309775"
ORIGIN      
        1 maaiaavaar rrrswlslvl aylgvclgit lavdrsnfkt ceessfckrq rsirpglspy
       61 ralldtlqlg pdaltvhlth evtkvllvle lqglqknmtr irideleprr pryrvpdvlv
      121 adpatarlsi sgrddnsvel tvaegpykii ltakpfrldl ledrslllsv narglmafeh
      181 qraprvpqep kdaaegngae pearpgdgdk peetqekaek depgaweetf kthsdskpyg
      241 ptsvgldfsl pgmehvygip ehadslrlkv teggepyrly nldvfqyeln npmalygsvp
      301 vllahsfhrd lgifwlnaae twvdissnta gktlfgkmld ylqgsgetpq tdirwmsesg
      361 ivdvflmlgp svldvfrqha sltgtqalpp lfslgyhqsr wnyrdeadvl evdqgfddhn
      421 mpcdviwldi ehadgkryft wdptrfpqpl nmlehlaskr rklvaivdph ikvdsgyrvh
      481 eelrnhglyv ktrdgsdyeg wcwpgsasyp dftnpqmraw wanmfnfhny egsapnlfvw
      541 ndmnepsvfn gpevtmlkda vhyggwehrd ihniyglyvh matadgliqr sggierpfvl
      601 sraffsgsqr fgavwtgdnt aewdhlkisi pmclslalvg lsfcgadvgg ffknpepell
      661 vrwyqmgayq pffrahahld tgrrepwlla sqyqdairda lfqrysllpf wytlfyqahq
      721 egfpvmrplw vqypedmstf smedqfmlgd allihpvsda gahgvqvylp geeevwydiq
      781 syqkhhgpqt lylpvtlssi pvfqrggtiv prwmrvrrss dcmkedpitl fvalsaqgta
      841 qgelflddgh tfnyqnrhef llrrfsfsgn tlvsssadpk ghletpvwie rvvimgagkp
      901 aavvlqtkgs pesrlsfqhd petsvltlrk pgvnvasdws ihlr
//
LOCUS       NP_062121                825 aa            linear   ROD 28-APR-2025
DEFINITION  NT-3 growth factor receptor isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_062121
VERSION     NP_062121.1
DBSOURCE    REFSEQ: accession NM_019248.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Chen,Z., Huang,Z., Luo,Y., Zou,Q., Bai,L., Tang,G., Wang,X.,
            Cao,G., Huang,M., Xiang,J. and Yu,H.
  TITLE     Genome-wide analysis identifies critical DNA methylations within
            NTRKs genes in colorectal cancer
  JOURNAL   J Transl Med 19 (1), 73 (2021)
   PUBMED   33593392
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Tan,W., Dong,L., Shi,X., Tang,Q. and Jiang,D.
  TITLE     P75NTR Exacerbates SCI-induced Mitochondrial Damage and Neuronal
            Apoptosis Depending on NTRK3
  JOURNAL   Curr Neurovasc Res 18 (5), 552-564 (2021)
   PUBMED   34970951
  REMARK    GeneRIF: P75NTR Exacerbates SCI-induced Mitochondrial Damage and
            Neuronal Apoptosis Depending on NTRK3.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Qiao,X., Yin,F., Ji,Y., Li,Y., Yan,P. and Lai,J.
  TITLE     5-Aza-2'-deoxycytidine in the medial prefrontal cortex regulates
            alcohol-related behavior and Ntf3-TrkC expression in rats
  JOURNAL   PLoS One 12 (6), e0179469 (2017)
   PUBMED   28614398
  REMARK    GeneRIF: Data show that 5-Aza-dc reversed the alcohol-induced
            downregulation of neurotrophin-3 (Ntf3), correspondingly the
            expression of its receptor-neurotrophic receptor tyrosine kinase 3
            (TrkC) was reduced.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Behrouz Sharif,S., Hashemzadeh,S., Mousavi Ardehaie,R.,
            Eftekharsadat,A., Ghojazadeh,M., Mehrtash,A.H., Estiar,M.A.,
            Teimoori-Toolabi,L. and Sakhinia,E.
  TITLE     Detection of aberrant methylated SEPT9 and NTRK3 genes in sporadic
            colorectal cancer patients as a potential diagnostic biomarker
  JOURNAL   Oncol Lett 12 (6), 5335-5343 (2016)
   PUBMED   28105243
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Dmitrieva,V.G., Stavchansky,V.V., Povarova,O.V., Skvortsova,V.I.,
            Limborska,S.A. and Dergunova,L.V.
  TITLE     [Effects of ischemia on the expression of neurotrophins and their
            receptors in rat brain structures outside the lesion site,
            including on the opposite hemisphere]
  JOURNAL   Mol Biol (Mosk) 50 (5), 775-784 (2016)
   PUBMED   27830679
  REMARK    GeneRIF: It has been shown that ischemia influenced the expression
            of neurotrophins (Bdnf, Ngf, Nt-3) and their receptors (TrkB, TrkA,
            TrkC, p75) in brain structures outside the lesion focus, including
            the contralateral hemisphere.
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Qian,X., Riccio,A., Zhang,Y. and Ginty,D.D.
  TITLE     Identification and characterization of novel substrates of Trk
            receptors in developing neurons
  JOURNAL   Neuron 21 (5), 1017-1029 (1998)
   PUBMED   9856458
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Fernyhough,P., Diemel,L.T. and Tomlinson,D.R.
  TITLE     Target tissue production and axonal transport of neurotrophin-3 are
            reduced in streptozotocin-diabetic rats
  JOURNAL   Diabetologia 41 (3), 300-306 (1998)
   PUBMED   9541170
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Tsoulfas,P., Soppet,D., Escandon,E., Tessarollo,L.,
            Mendoza-Ramirez,J.L., Rosenthal,A., Nikolics,K. and Parada,L.F.
  TITLE     The rat trkC locus encodes multiple neurogenic receptors that
            exhibit differential response to neurotrophin-3 in PC12 cells
  JOURNAL   Neuron 10 (5), 975-990 (1993)
   PUBMED   8494648
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Valenzuela,D.M., Maisonpierre,P.C., Glass,D.J., Rojas,E., Nunez,L.,
            Kong,Y., Gies,D.R., Stitt,T.N., Ip,N.Y. and Yancopoulos,G.D.
  TITLE     Alternative forms of rat TrkC with different functional
            capabilities
  JOURNAL   Neuron 10 (5), 963-974 (1993)
   PUBMED   8494647
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Merlio,J.P., Ernfors,P., Jaber,M. and Persson,H.
  TITLE     Molecular cloning of rat trkC and distribution of cells expressing
            messenger RNAs for members of the trk family in the rat central
            nervous system
  JOURNAL   Neuroscience 51 (3), 513-532 (1992)
   PUBMED   1488112
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L03813.1 and L14445.2.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L03813.1, L14445.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..825
                     /product="NT-3 growth factor receptor isoform 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="NT-3 growth factor receptor; trk-C; GP145-TrkC;
                     trkC tyrosine kinase; neurotrophic tyrosine kinase,
                     receptor, type 3; neural receptor protein-tyrosine kinase
                     (trkC)"
                     /calculated_mol_wt=89302
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3477
     Region          103..160
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          105..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          152..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          163..208
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Region          214..299
                     /region_name="ig"
                     /note="Immunoglobulin domain; pfam00047"
                     /db_xref="CDD:395002"
     Region          227..231
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          240..244
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          266..270
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          281..286
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..297
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..396
                     /region_name="IgI_TrKABC_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptors
                     TrkA, TrkB, and TrkC; member of the I-set of Ig
                     superfamily (IgSF) domains; cd04971"
                     /db_xref="CDD:409360"
     Region          305..311
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409360"
     Region          313..316
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409360"
     Region          319..327
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409360"
     Site            328
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          330..337
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409360"
     Region          340..343
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409360"
     Region          348..354
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409360"
     Site            order(353,366..367,370)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          358..366
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409360"
     Region          374..382
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409360"
     Region          385..393
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409360"
     Region          532..818
                     /region_name="PTKc_TrkC"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tropomyosin Related Kinase C; cd05094"
                     /db_xref="CDD:270676"
     Site            order(544..548,552,570,572,617..620,623..624,679,683..684,
                     686,697,715..719,728,762)
                     /site_type="active"
                     /db_xref="CDD:270676"
     Site            order(544..545,547..548,552,570,572,617..620,623..624,
                     683..684,686,697)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270676"
     Site            order(679,683,715..719,728,762)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270676"
     Site            696..721
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270676"
     CDS             1..825
                     /gene="Ntrk3"
                     /gene_synonym="trkC"
                     /coded_by="NM_019248.2:52..2529"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:29613"
                     /db_xref="RGD:3214"
ORIGIN      
        1 mdvslcpakc sfwrifllgs vwldyvgsvl acpancvcsk teincrrpdd gnlfpllegq
       61 dsgnsngnas initdisrni tsihienwrg lhtlnavdme lytglqklti knsglrniqp
      121 rafaknphlr yinlssnrlt tlswqlfqtl slrelrleqn ffncscdirw mqlwqeqgea
      181 rldsqslyci sadgsqlplf rmnisqcdlp eisvshvnlt vregdnavit cngsgsplpd
      241 vdwivtglqs inthqtnlnw tnvhainltl vnvtsedngf tltciaenvv gmsnasvalt
      301 vyypprvvsl vepevrlehc iefvvrgnpt ptlhwlyngq plreskiihm dyyqegevse
      361 gcllfnkpth ynngnytlia knalgtanqt inghflkepf pestdffdfe sdasptppit
      421 vthkpeedtf gvsiavglaa facvllvvlf iminkygrrs kfgmkgpvav isgeedsasp
      481 lhhinhgitt pssldagpdt vvigmtripv ienpqyfrqg hnchkpdtyv qhikrrdivl
      541 krelgegafg kvflaecynl sptkdkmlva vkalkdptla arkdfqreae lltnlqhehi
      601 vkfygvcgdg dplimvfeym khgdlnkflr ahgpdamilv dgqprqakge lglsqmlhia
      661 sqiasgmvyl asqhfvhrdl atrnclvgan llvkigdfgm srdvystdyy rvgghtmlpi
      721 rwmppesimy rkfttesdvw sfgvilweif tygkqpwfql snteviecit qgrvlerprv
      781 cpkevydvml gcwqrepqqr lnikeiykil halgkatpiy ldilg
//
LOCUS       NP_001029193             694 aa            linear   ROD 28-APR-2025
DEFINITION  TBC1 domain family member 14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001029193 XP_573632
VERSION     NP_001029193.2
DBSOURCE    REFSEQ: accession NM_001034021.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Longatti,A., Lamb,C.A., Razi,M., Yoshimura,S., Barr,F.A. and
            Tooze,S.A.
  TITLE     TBC1D14 regulates autophagosome formation via Rab11- and
            ULK1-positive recycling endosomes
  JOURNAL   J Cell Biol 197 (5), 659-675 (2012)
   PUBMED   22613832
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Fuchs,E., Haas,A.K., Spooner,R.A., Yoshimura,S., Lord,J.M. and
            Barr,F.A.
  TITLE     Specific Rab GTPase-activating proteins define the Shiga toxin and
            epidermal growth factor uptake pathways
  JOURNAL   J Cell Biol 177 (6), 1133-1143 (2007)
   PUBMED   17562788
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Yamano,Y., Ohyama,K., Ohta,M., Sano,T., Ritani,A., Shimada,J.,
            Ashida,N., Yoshida,E., Ikehara,K. and Morishima,I.
  TITLE     A novel spermatogenesis related factor-2 (SRF-2) gene expression
            affected by TCDD treatment
  JOURNAL   Endocr J 52 (1), 75-81 (2005)
   PUBMED   15758561
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Horiba,N., Masuda,S., Takeuchi,A., Saito,H., Okuda,M. and Inui,K.
  TITLE     Gene expression variance based on random sequencing in rat remnant
            kidney
  JOURNAL   Kidney Int 66 (1), 29-45 (2004)
   PUBMED   15200410
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB746983.1 and BC099760.1.
            
            On Jan 10, 2008 this sequence version replaced NP_001029193.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC099760.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..694
                     /product="TBC1 domain family member 14 isoform 2"
                     /note="Up-regulated in nephrectomized rat kidney #2;
                     spermatogenesis-related factor 2"
                     /calculated_mol_wt=78113
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2M4; propagated from
                     UniProtKB/Swiss-Prot (Q5CD77.2)"
     Region          108..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5CD77.2)"
     Region          272..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5CD77.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2M4; propagated from
                     UniProtKB/Swiss-Prot (Q5CD77.2)"
     Region          330..>369
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          399..631
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..694
                     /gene="Tbc1d14"
                     /gene_synonym="SRF-2; UR-NR#2"
                     /coded_by="NM_001034021.2:151..2235"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:360956"
                     /db_xref="RGD:1309993"
ORIGIN      
        1 mtdgnlstsm ngvalmgild grpgdslqel qhlsikavpr slsvpdygpt lklgaledrh
       61 slqsvdsgip tleignpepv pcsvvhvkrk qseseiiper afqsacplps ctpsaptgse
      121 reqavrksst fprtgydsvk lysptskals rsddvsvcsv sslgtelstt lsvsnedild
      181 lmvtsnssai vtlendddpq ftdvtlssik etsdlhqqdc vaeteegrkl rllqpfshff
      241 trnllarkqn arldrqrdlg wklfgkvplr etaqkdskkt qkeyedkagr psrppspkqn
      301 vrknldfepl sttaliledr panlpakpae eaqkhrqqye emvvqakkre lkeaqrrkkq
      361 leerckvees ignavltwnn eilpnwetmw cskkvrdlww qgippsvrgk vwslaignel
      421 nithelfdic larakerwrs lstggseven edagfsaadr easlelikld isrtfpnlci
      481 fqqggpyhdm lhsilgaytc yrpdvgyvqg msfiaavlil nldtadafia fsnllnkpcq
      541 maffrvdhgl mltyfaafev ffeenlpklf ahfkknnlta diylidwift lyskslpldl
      601 acriwdvfcr dgeeflfrta lgilklfedi ltrmdfihsa qfltrlpedl paddvfaais
      661 tvqmqsrnkk waqvlsalqk dsremekgsp slrh
//
LOCUS       NP_001423684             265 aa            linear   ROD 28-APR-2025
DEFINITION  occludin/ELL domain-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001423684 XP_006252918
VERSION     NP_001423684.1
DBSOURCE    REFSEQ: accession NM_001436755.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 20, 2025 this sequence version replaced XP_006252918.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169113.1, CV795590.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..265
                     /product="occludin/ELL domain-containing protein 1 isoform
                     2"
                     /note="occludin/ELL domain-containing protein 1"
                     /calculated_mol_wt=29636
     Region          113..253
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..265
                     /gene="Ocel1"
                     /gene_synonym="RGD1563236; RGD1565407"
                     /coded_by="NM_001436755.1:347..1144"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:290628"
                     /db_xref="RGD:1565407"
ORIGIN      
        1 mqipagpssr rrsrgplacg sqsrrsgpda tcnsrpaagg rqsatapcmp arerpqprag
       61 rphcqprpse lrtrprkivf adelqprapl hpekhprdlg prpnpvpdye lkyppvtsrr
      121 drsryaavfq dqyeeflelq rqvgamqakl qqlealllsl ppprsqvspg ppvpqppcgc
      181 aastgwnavt amvallspfp tlpfqkevrm aahvrrefek krvdpgfldk qarcdylkgk
      241 lrhlkaqirk fddqrdsnse nsvyf
//
LOCUS       NP_001402665             784 aa            linear   ROD 28-APR-2025
DEFINITION  protein enabled homolog isoform 3 [Rattus norvegicus].
ACCESSION   NP_001402665 XP_038946857
VERSION     NP_001402665.1
DBSOURCE    REFSEQ: accession NM_001415736.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Deng,G., Luo,Y., Zhang,Y., Zhang,J. and He,Z.
  TITLE     Enabled homolog (ENAH) regulated by RNA binding protein splicing
            factor 3b subunit 4 (SF3B4) exacerbates the proliferation, invasion
            and migration of hepatocellular carcinoma cells via Notch signaling
            pathway
  JOURNAL   Bioengineered 13 (2), 2194-2206 (2022)
   PUBMED   35030977
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Wang,D.D., Chen,Y.B., Zhao,J.J., Zhang,X.F., Zhu,G.C., Weng,D.S.,
            Pan,K., Lv,L., Pan,Q.Z., Jiang,S.S., Wang,L.L. and Xia,J.C.
  TITLE     TES functions as a Mena-dependent tumor suppressor in gastric
            cancer carcinogenesis and metastasis
  JOURNAL   Cancer Commun (Lond) 39 (1), 3 (2019)
   PUBMED   30728082
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Riquelme,D.N., Meyer,A.S., Barzik,M., Keating,A. and Gertler,F.B.
  TITLE     Selectivity in subunit composition of Ena/VASP tetramers
  JOURNAL   Biosci Rep 35 (5), e00246 (2015)
   PUBMED   26221026
  REMARK    GeneRIF: The tetramerization domain (TD) at the C-termini of
            enabled/VASP proteins conferred the observed selectivity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Ram,R., Wescott,A.P., Varandas,K., Dirksen,R.T. and Blaxall,B.C.
  TITLE     Mena associates with Rac1 and modulates connexin 43 remodeling in
            cardiomyocytes
  JOURNAL   Am J Physiol Heart Circ Physiol 306 (1), H154-H159 (2014)
   PUBMED   24186093
  REMARK    GeneRIF: Mena is associated with active Rac1 in cardiomyocytes.
            Knockdown of Mena increased Rac1 activity, connexin43 expression
            and localization.
REFERENCE   5  (residues 1 to 784)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 784)
  AUTHORS   Giesemann,T., Schwarz,G., Nawrotzki,R., Berhorster,K.,
            Rothkegel,M., Schluter,K., Schrader,N., Schindelin,H., Mendel,R.R.,
            Kirsch,J. and Jockusch,B.M.
  TITLE     Complex formation between the postsynaptic scaffolding protein
            gephyrin, profilin, and Mena: a possible link to the microfilament
            system
  JOURNAL   J Neurosci 23 (23), 8330-8339 (2003)
   PUBMED   12967995
REFERENCE   7  (residues 1 to 784)
  AUTHORS   Tani,K., Sato,S., Sukezane,T., Kojima,H., Hirose,H., Hanafusa,H.
            and Shishido,T.
  TITLE     Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
            enabled (Mena) by c-Abl kinase
  JOURNAL   J Biol Chem 278 (24), 21685-21692 (2003)
   PUBMED   12672821
REFERENCE   8  (residues 1 to 784)
  AUTHORS   Lanier,L.M., Gates,M.A., Witke,W., Menzies,A.S., Wehman,A.M.,
            Macklis,J.D., Kwiatkowski,D., Soriano,P. and Gertler,F.B.
  TITLE     Mena is required for neurulation and commissure formation
  JOURNAL   Neuron 22 (2), 313-325 (1999)
   PUBMED   10069337
REFERENCE   9  (residues 1 to 784)
  AUTHORS   Yamabhai,M. and Kay,B.K.
  TITLE     Examining the specificity of Src homology 3 domain--ligand
            interactions with alkaline phosphatase fusion proteins
  JOURNAL   Anal Biochem 247 (1), 143-151 (1997)
   PUBMED   9126384
REFERENCE   10 (residues 1 to 784)
  AUTHORS   Gertler,F.B., Niebuhr,K., Reinhard,M., Wehland,J. and Soriano,P.
  TITLE     Mena, a relative of VASP and Drosophila Enabled, is implicated in
            the control of microfilament dynamics
  JOURNAL   Cell 87 (2), 227-239 (1996)
   PUBMED   8861907
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On Dec 28, 2022 this sequence version replaced XP_038946857.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q26"
     Protein         1..784
                     /product="protein enabled homolog isoform 3"
                     /note="protein enabled homolog"
                     /calculated_mol_wt=84084
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          <341..517
                     /region_name="PLN03209"
                     /note="translocon at the inner envelope of chloroplast
                     subunit 62; Provisional"
                     /db_xref="CDD:178748"
     Region          599..625
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(606..607,609..610,613,615..619)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          615..618
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          746..780
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..784
                     /gene="Enah"
                     /coded_by="NM_001415736.1:397..2751"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:360891"
                     /db_xref="RGD:1307666"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqeagptl
      121 prqnsqlpaq vqngpsqeem eiqrrqlqeq qrqkelerer mererlerer lererlerer
      181 leqeqlerqr qerehverle rerlerlere rqdrererer leqlereqve wererrmsna
      241 apssdsslys aplpeysscq ppsapppsya kvisapvsda apdyavvtal pptstpptpp
      301 lrhsatrfat slgsafhpvl phyatvprpl nrnsrpsspv ntpssqppaa kscawptsnf
      361 splppsppim issppgkatg prpvlpvcvs spvpqmppsp tapngsldsv typvspppts
      421 gpaapppppp pppppppppp ppplpplasl shcgsqaspp pgtplastps skpsvlpsps
      481 aaapasvetp lnpelgdssa sepglqaasq paetpapqgh vlgppapppp pplpsgpaya
      541 salppppgpp pppplpsagp pppppppppl pnqvpppppp ppapplpasg ifsgsmsedn
      601 rpltglaaai agaklrkvsr vedgsfpsgg ntvsvnlass ktdsgrgngp lplggsglme
      661 emsallarrr riaekgstie teqkedrsed aepvtskaas tstpeptrkp wertntmngs
      721 kspvisrpks tpssqpsang vqtegldydr lkqdildemr kelaklkeel idairqelsk
      781 snta
//
LOCUS       NP_001418338             883 aa            linear   ROD 28-APR-2025
DEFINITION  phospholipase DDHD1 isoform 5 [Rattus norvegicus].
ACCESSION   NP_001418338 XP_006251835
VERSION     NP_001418338.1
DBSOURCE    REFSEQ: accession NM_001431409.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Baba,T., Kashiwagi,Y., Arimitsu,N., Kogure,T., Edo,A., Maruyama,T.,
            Nakao,K., Nakanishi,H., Kinoshita,M., Frohman,M.A., Yamamoto,A. and
            Tani,K.
  TITLE     Phosphatidic acid (PA)-preferring phospholipase A1 regulates
            mitochondrial dynamics
  JOURNAL   J Biol Chem 289 (16), 11497-11511 (2014)
   PUBMED   24599962
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Jul 16, 2024 this sequence version replaced XP_006251835.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.53448.1,
                                           SRR26360181.1399883.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..883
                     /product="phospholipase DDHD1 isoform 5"
                     /note="phospholipase DDHD1"
                     /calculated_mol_wt=98467
     Region          594..868
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     CDS             1..883
                     /gene="Ddhd1"
                     /coded_by="NM_001431409.1:34..2685"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:305816"
                     /db_xref="RGD:1308576"
ORIGIN      
        1 mnypgrgapr sperngrggg awelgsdaag vfggggccfe hqpgdgvpls llraeplhla
       61 pgaddlshla ldpclsdeny dfssaesgss lryysegesa gggssssppp plvapnsggg
      121 gaagggpgdr krsrpggcaa rhryevvtel gpeevrwfyk edkktwkpfi gydslriela
      181 frsllqttgs rarsadrdgd rvcgptssfr eddedracgf cpravgpepe meelvtiepv
      241 cvrgglyevd vtqgecypvy wnqadkipvm rgqwfidgtw qpleeeesnl ieqehlscfr
      301 gqqmqenfdi emsksidgkd avhsfklsrn hvdwhsmdev ylysdattsk iartvtqklg
      361 fskasssgtr lhrgyveeat ledkpsqtsh ivfvvhgigq kmdqgriikn tammreaark
      421 ieekhfanha thveflpvew rskltldgdt vdsitpdkvr glrdmlnssa mdimyytspl
      481 yrdelvkglq qelnrlyslf csrnpdfeek ggkvsivshs lgcvitydim mgwnpvrlye
      541 qllqkeeelp derwmsyeer hlldelyitk rrlreiedrl hglkapsgsq tpalkfkven
      601 ffcmgsplav flalrgirpg ntgsqdhilp reicnrllni fhptdpvayr leplilkhys
      661 nispvqihwy ntsnplpyeh mkpnflnpak eptsasesen iaaipspvts pvlsrrhyge
      721 sitnigkasi lgaasigkgl ggmlfsrfgr sstpqpseps kdsaeeekkp vsspstttva
      781 tqtlphsssg fldsayfrlq esffylpqll fpenvmqskd dslvelehri dfelreglve
      841 srywsavtsh taywssldva lflltfmykh ehdseaktsl dsi
//
LOCUS       NP_001420766             981 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 15 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001420766 XP_006241493
VERSION     NP_001420766.1
DBSOURCE    REFSEQ: accession NM_001433837.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Zhang,T., Wang,L. and Chen,L.
  TITLE     Alleviative effect of microRNA-497 on diabetic neuropathic pain in
            rats in relation to decreased USP15
  JOURNAL   Cell Biol Toxicol 39 (5), 1-16 (2023)
   PUBMED   35478295
  REMARK    GeneRIF: Alleviative effect of microRNA-497 on diabetic neuropathic
            pain in rats in relation to decreased USP15.
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Wu,Z., Zhu,L., Nie,X., Wei,L. and Qi,Y.
  TITLE     USP15 promotes pulmonary vascular remodeling in pulmonary
            hypertension in a YAP1/TAZ-dependent manner
  JOURNAL   Exp Mol Med 55 (1), 183-195 (2023)
   PUBMED   36635430
  REMARK    GeneRIF: USP15 promotes pulmonary vascular remodeling in pulmonary
            hypertension in a YAP1/TAZ-dependent manner.
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Zhang,L., Gao,X., Qin,Z., Shi,X., Xu,K., Wang,S., Tang,M., Wang,W.,
            Gao,S., Zuo,L., Zhang,L. and Zhang,W.
  TITLE     USP15 participates in DBP-induced testicular oxidative stress
            injury through regulating the Keap1/Nrf2 signaling pathway
  JOURNAL   Sci Total Environ 783, 146898 (2021)
   PUBMED   34088152
  REMARK    GeneRIF: USP15 participates in DBP-induced testicular oxidative
            stress injury through regulating the Keap1/Nrf2 signaling pathway.
REFERENCE   4  (residues 1 to 981)
  AUTHORS   Chen,X., Bao,G. and Liu,F.
  TITLE     Inhibition of USP15 Prevent Glutamate-Induced Oxidative Damage by
            Activating Nrf2/HO-1 Signaling Pathway in HT22 Cells
  JOURNAL   Cell Mol Neurobiol 40 (6), 999-1010 (2020)
   PUBMED   31933062
  REMARK    GeneRIF: Inhibition of USP15 Prevent Glutamate-Induced Oxidative
            Damage by Activating Nrf2/HO-1 Signaling Pathway in HT22 Cells.
REFERENCE   5  (residues 1 to 981)
  AUTHORS   Nie,Z.Y., Yao,M., Yang,Z., Yang,L., Liu,X.J., Yu,J., Ma,Y.,
            Zhang,N., Zhang,X.Y., Liu,M.H., Jiang,L.L. and Luo,J.M.
  TITLE     De-regulated STAT5A/miR-202-5p/USP15/Caspase-6 regulatory axis
            suppresses CML cell apoptosis and contributes to Imatinib
            resistance
  JOURNAL   J Exp Clin Cancer Res 39 (1), 17 (2020)
   PUBMED   31952546
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 981)
  AUTHORS   Elliott,P.R., Liu,H., Pastok,M.W., Grossmann,G.J., Rigden,D.J.,
            Clague,M.J., Urbe,S. and Barsukov,I.L.
  TITLE     Structural variability of the ubiquitin specific protease DUSP-UBL
            double domains
  JOURNAL   FEBS Lett 585 (21), 3385-3390 (2011)
   PUBMED   22001210
REFERENCE   7  (residues 1 to 981)
  AUTHORS   Inui,M., Manfrin,A., Mamidi,A., Martello,G., Morsut,L., Soligo,S.,
            Enzo,E., Moro,S., Polo,S., Dupont,S., Cordenonsi,M. and Piccolo,S.
  TITLE     USP15 is a deubiquitylating enzyme for receptor-activated SMADs
  JOURNAL   Nat Cell Biol 13 (11), 1368-1375 (2011)
   PUBMED   21947082
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 981)
  AUTHORS   Hetfeld,B.K., Helfrich,A., Kapelari,B., Scheel,H., Hofmann,K.,
            Guterman,A., Glickman,M., Schade,R., Kloetzel,P.M. and Dubiel,W.
  TITLE     The zinc finger of the CSN-associated deubiquitinating enzyme USP15
            is essential to rescue the E3 ligase Rbx1
  JOURNAL   Curr Biol 15 (13), 1217-1221 (2005)
   PUBMED   16005295
REFERENCE   9  (residues 1 to 981)
  AUTHORS   Angelats,C., Wang,X.W., Jermiin,L.S., Copeland,N.G., Jenkins,N.A.
            and Baker,R.T.
  TITLE     Isolation and characterization of the mouse ubiquitin-specific
            protease Usp15
  JOURNAL   Mamm Genome 14 (1), 31-46 (2003)
   PUBMED   12532266
REFERENCE   10 (residues 1 to 981)
  AUTHORS   Park,K.C., Choi,E.J., Min,S.W., Chung,S.S., Kim,H., Suzuki,T.,
            Tanaka,K. and Chung,C.H.
  TITLE     Tissue-specificity, functional characterization and subcellular
            localization of a rat ubiquitin-specific processing protease,
            UBP109, whose mRNA expression is developmentally regulated
  JOURNAL   Biochem J 349 (Pt 2), 443-453 (2000)
   PUBMED   10880343
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Oct 10, 2024 this sequence version replaced XP_006241493.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.19700.1,
                                           SRR26360194.657143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..981
                     /product="ubiquitin carboxyl-terminal hydrolase 15 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 15; ubiquitin
                     specific protease 15; deubiquitinating enzyme Ubp109;
                     ubiquitin thioesterase 15; deubiquitinating enzyme 15;
                     ubiquitin-specific-processing protease 15; ubiquitin
                     carboxyl-terminal hydrolase of 109 kDa"
                     /calculated_mol_wt=112214
     Region          12..932
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     CDS             1..981
                     /gene="Usp15"
                     /gene_synonym="Ubp109"
                     /coded_by="NM_001433837.1:68..3013"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171329"
                     /db_xref="RGD:628795"
ORIGIN      
        1 maeggaadld tqrsdiatll ktslrkgdtw ylvdsrwfkq wkkyvgfdsw dkyqmgdqnv
       61 ypgpidnsgl lkdgdaqslk ehlideldyi llptegwnkl vswytlmegq epiarkvveq
      121 gmfvkhckve vyltelklce ngnmnnvvtr rfskadtidt iekeirkifn ipdekearlw
      181 nkymsntfep lnkpdstiqd aglyqgqvlv ieqknedgtw prgpsapksp gasnfstlpk
      241 ispsslsnny nninnrnvkn snyclpsyta yknydysepg rnneqpglcg lsnlgntcfm
      301 nsaiqclsnt pplteyflnd kyqeelnfdn plgmrgeiak syaelikqmw sgkfsyvtpr
      361 afktqvgrfa pqfsgyqqqd cqellaflld glhedlnrir kkpyiqlkda dgrpdkvvae
      421 eawenhlkrn dsiivdifhg lfkstlvcpe cakisvtfdp fcyltlplpm kkerslevyl
      481 vrmdplakpm qykvivpkig nildlctals alsgvpadkm ivtdiynhrf hrifamdenl
      541 ssimerddiy vfeininrte dtehvvipvc lrekfrhssy thhtgsslfg qpflmavprn
      601 ntedklynll llrmcryvkm steteetdgp lrccedqnin gngpngihee gspsemetde
      661 pddessqdqe lpsenensqs edsvggdnds englcteetc kgqltghkkr lftfqfnnlg
      721 ntdinyikdd trhirfddrq lrldersfla ldwdpdlkkr yfdenaaedf ekhesveykp
      781 pkrpfvklkd cielfttkek lgaedpwycp nckehqqatk kldlwslppv lvvhlkrfsy
      841 srymrdkldt lvdfpisdld mseflinpna gpcrynliav snhyggmggg hytafaknkd
      901 dgkwyyfdds svstasedqi vskaayvlfy qrqdtfsgtg ffpldretkg asaatgvple
      961 sdedsndndn dlenencmht n
//
LOCUS       NP_001376164            2462 aa            linear   ROD 28-APR-2025
DEFINITION  myomegalin isoform 4 [Rattus norvegicus].
ACCESSION   NP_001376164 XP_017446565
VERSION     NP_001376164.1
DBSOURCE    REFSEQ: accession NM_001389235.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2462)
  AUTHORS   Bouguenina,H., Salaun,D., Mangon,A., Muller,L., Baudelet,E.,
            Camoin,L., Tachibana,T., Cianferani,S., Audebert,S.,
            Verdier-Pinard,P. and Badache,A.
  TITLE     EB1-binding-myomegalin protein complex promotes centrosomal
            microtubules functions
  JOURNAL   Proc Natl Acad Sci U S A 114 (50), E10687-E10696 (2017)
   PUBMED   29162697
REFERENCE   2  (residues 1 to 2462)
  AUTHORS   Wu,J., de Heus,C., Liu,Q., Bouchet,B.P., Noordstra,I., Jiang,K.,
            Hua,S., Martin,M., Yang,C., Grigoriev,I., Katrukha,E.A.,
            Altelaar,A.F.M., Hoogenraad,C.C., Qi,R.Z., Klumperman,J. and
            Akhmanova,A.
  TITLE     Molecular Pathway of Microtubule Organization at the Golgi
            Apparatus
  JOURNAL   Dev Cell 39 (1), 44-60 (2016)
   PUBMED   27666745
REFERENCE   3  (residues 1 to 2462)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    GeneRIF: MMGL isoform 4 is involved in the phosphorylation of
            Cardiac Myosin Binding Protein-C as well as cardiac troponin I.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2462)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   5  (residues 1 to 2462)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   6  (residues 1 to 2462)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Dec 1, 2020 this sequence version replaced XP_017446565.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2462
                     /product="myomegalin isoform 4"
                     /note="phosphodiesterase-binding protein clone 46;
                     myomegalin"
                     /calculated_mol_wt=277372
     Region          126..193
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          178..>644
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          434..1160
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1676..1741
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1961..>2200
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2462
                     /gene="Pde4dip"
                     /coded_by="NM_001389235.1:38..7426"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64183"
                     /db_xref="RGD:708410"
ORIGIN      
        1 mkrtdsgsic hhapppcwah haprqsprqp ssrerrpper agswavaaee eeavssapwm
       61 rhyfgeedge mvprtsnaaa flsdtkdrgp pvqsqvwrsa ekvpfgqahs lrafekpplv
      121 qtqalrdfek hlndlkkenf slklriyfle ermqqkyevs redvykrnie lkveveslkr
      181 elqdrkqhlh ktwadeedln sqneaelrrq veepqqeteh vyelldnniq llqeesrfak
      241 deatqmetlv eaekgcnlel serwkdatkn redapgdqvk ldqysaalaq rdrrieelrq
      301 slaaqeglve qlsrekqqll hlleepggme vqpmpkglpt qqkpdlnetp ttqpsvsdsh
      361 laelqdkiqq tevtnkilqe klndmscelr saqessqkqd ttiqslkeml ksreseteel
      421 yqviegqndt maklremlhq sqlgqlqsse giapaqqqva lldlqsalfc sqleiqklqr
      481 llrqkerqla dgkrcmqfve aaaqereqqk eaawkhnqel rkalqhlqge lhsksqqlhv
      541 leaekyneir tqgqniqhls hslshkeqli qelqellqyr dttdktldtn evfleklrqr
      601 iqdravaler videkfsale ekdkelrqlr lavrdrdhdl erlrcvlsan eatmqsmesl
      661 lrargleveq ltatcqnlqw lkeeletkfg hwqkeqesii qqlqtslhdr nkevedlsat
      721 llhklgpgqs evaeelcqrl qrkervlqdl lsdrnkqame hemevqgllq smgtreqerq
      781 avaekmvqaf mernselqal rqylggkelm aasqafisnq pagatsvgph hgeqtdqgst
      841 qmpsrddsts ltareeasip rstlgdsdtv aglekelsna keelelmakk eresqielsa
      901 lqsmmavqee elqvqaadle sltrniqike dlikdlqmql vdpedmpame rltqevlllr
      961 ekvasvepqg qegsenrrqq lllmleglvd ersrlnealq aerqlysslv kfhaqpetse
     1021 rdrtlqvele gaqvlrsrle evlgrslerl srletlaaig gatagdeted tstqftdsie
     1081 eeaahnshqq likvsleksl ttmetqntcl qppspvgedg nrhlqeemlh lraeihqhle
     1141 ekrkaeaelk elkaqieeag fssvshirnt mlslclenae lkeqmgeams dgweveedke
     1201 kgevmvetvv akgglsedsl qaefrkvqgr lksayniinl lkeqlvlrss egntkempef
     1261 lvrlarevdr mnmglpssek hqhqeqenmt arpgprpqsl klgtalsvdg yqlenksqaq
     1321 dsghqpqfsl pgstkhlrsq laqcrqryqd lqekllisea tvfaqanqle kyrailsesl
     1381 vkqdskqiqv dlqdlgyetc grseneaere ettspeceeh gnlrpvvlve glcseqgyld
     1441 pvlvsspvkk plenkpgkre efqaqgtsdd ssllrkdird lkaqlqnayk viqnlrsrvr
     1501 slsatsdyss slerprklra vatlegasph svtdedegwl sdgtgafypp glqakknlen
     1561 liqrvsqlea qlpktglegk laeelrsasw pgkydsliqd qarelsylrq kiregrgicy
     1621 lltqhskdtv ksfedllrsn didyylgqsf reqlaqggql tdrltsklst kdhksekeea
     1681 gleplalrls relqekekvi evlqakldtr slsppsshaa sdshrsasst sflsddieac
     1741 sdmdvaseyt hyeekkpsps nsdsihhssh stvlssnpsa asasqglkge prsssislpt
     1801 pqnppkeasq aqpgfhfnsi pkpaslsqap mhftvpsfmp fgpsgppllg ccetpvvsla
     1861 eaqqelqmlq kqlgesvsia pptststlls nhteasspry snpaqphspa rgtielgril
     1921 epgylgsgqw dmmrpqkgsi sgelssgssm yqlnskptga dlleehlgei rnlrqrlees
     1981 icvndrlreq lqhrlsstar engstshfys qglesmpqly nenralreen qslqtrlsha
     2041 srghsqevdh lreallssss qlqelekele qqkaerrqll edlqekqdei vhfreerlsl
     2101 qennsrlqhk lallqqqcee kqqlslslqs elqiyeslye npkkglkafs ldscyqvpge
     2161 lsclvaeira lrvqleqsiq vnnrlrlqle qqmdhgagka slsscpvnqs fsakaelanq
     2221 qppfqgsaas ppvrdvglns pavvlpsnsc svpgsdsaii srtnngsdes aatktppkme
     2281 vdaadgpfas ghgrhvighv ddydtlqqqi gegklliqki lsltrparsv paldaqgtea
     2341 pgtksvhelr ssaralnhsl eesaslltmf wraalpnshg svlvgeegkl mekelldlra
     2401 qvsqqqqllq stavrlktan qrkksmeqfi vshltrthdv lkkartnlem ksfralmctp
     2461 al
//
LOCUS       NP_001129344             824 aa            linear   ROD 28-APR-2025
DEFINITION  lysine-specific demethylase RSBN1L [Rattus norvegicus].
ACCESSION   NP_001129344 XP_231305
VERSION     NP_001129344.1
DBSOURCE    REFSEQ: accession NM_001135872.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Oct 16, 2008 this sequence version replaced XP_231305.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.16404.1,
                                           SRR26643293.21476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..824
                     /product="lysine-specific demethylase RSBN1L"
                     /note="round spermatid basic protein 1-like protein"
                     /calculated_mol_wt=92181
     CDS             1..824
                     /gene="Rsbn1l"
                     /gene_synonym="RGD1308748"
                     /coded_by="NM_001135872.1:453..2927"
                     /db_xref="GeneID:311987"
                     /db_xref="RGD:1308748"
ORIGIN      
        1 maeppnparg pvavlsekea fgklqpssre spgsmsakkv rteekkgprr vngegdsggn
       61 ggqlqppaap spqsygspaa wsfaarpaas sqatprgcya fsaspsvssa sasssqpvpr
      121 kllvassllh aqphrvllpp vtppaaakpr rpkekrekek rrhglggadr dengeakplp
      181 rdkikdkike kdkekererk khkvmseikk engdvkiflk sgkekpktni edlqikkvkk
      241 kkkkkhkene krkrpkmysk siqticsgll saedqeakgi lndnvkdcig khldtkncds
      301 kvpdnsdfpf vslkeprvqn dlkrldtlef kqlihvehqp nggasvihay cselsclspv
      361 emrrfaeefv glafseness aafyvmgvvh gaatylpdfl dyfsynfpns pvkmeilgkk
      421 dietttmsnf haqvkrtysh gtyragpmrq islvgavdee vgdyfpefld mleespflkc
      481 tlpwgtlssl klesrkdsdd gpimwvrpge qmipvadmpk spfkrkrttn eiknlqylpr
      541 tsepremlfe drtrahadhi gqgferqtta avgvlkavhc gqrpdqprvt kdvicfhaed
      601 flevvqrmql dlhepplsqc vqwvddakln qlrregirya riqlydndiy fiprnvvhqf
      661 ktvsavcsla whvrlklyha edtchstvth eqgipsgpts svlgthtenq sssdpvlsdr
      721 lhskyespqv kqepvvslni keepvtvtvs aktrtpnnte gksskaksdh vqfsdfhidm
      781 dskfentnkd lkedlcpgsv qevdtrqhsc ipsnqdrsde nnvc
//
LOCUS       NP_001419636             640 aa            linear   ROD 28-APR-2025
DEFINITION  interleukin 4 induced 1 isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_001419636 XP_038949956
VERSION     NP_001419636.1
DBSOURCE    REFSEQ: accession NM_001432707.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Boulland,M.L., Marquet,J., Molinier-Frenkel,V., Moller,P.,
            Guiter,C., Lasoudris,F., Copie-Bergman,C., Baia,M., Gaulard,P.,
            Leroy,K. and Castellano,F.
  TITLE     Human IL4I1 is a secreted L-phenylalanine oxidase expressed by
            mature dendritic cells that inhibits T-lymphocyte proliferation
  JOURNAL   Blood 110 (1), 220-227 (2007)
   PUBMED   17356132
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 1, 2024 this sequence version replaced XP_038949956.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1294526.1,
                                           SRR26643293.2906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..640
                     /product="interleukin 4 induced 1 isoform 2 precursor"
                     /note="rCG53598-like; L-amino-acid oxidase"
                     /calculated_mol_wt=69140
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1962
     Region          67..504
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
     CDS             1..640
                     /gene="Il4i1"
                     /coded_by="NM_001432707.1:330..2252"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:100360621"
                     /db_xref="RGD:1304831"
ORIGIN      
        1 maglalhlvl vatllglavs lqwraasnln liekcmvdhd yeqllkvvtl glnrtskpqk
       61 vvvvgagvag lvaakvlsda ghkvtileag nriggriftf rdektgwige lgamrmpssh
      121 rilhqlcrsl glnltqftqy denawtevkg vklrnyvvek mpeklgydln hrerghsped
      181 iyqmalnkai kdvkvlgckk amnmfsehtl leyllkegnl sqpavqllgd vmskegffyl
      241 slaeafraha clsdrlrysr ivggwdllpr allsslsgtv llnapvvsis qgrhevhvhf
      301 ttslqshsle vmtadvvllt asgpalqris fsppltrkrq ealralhyva askvflsfhr
      361 pfwheehimg ghsntdrpsr lifypapgeg slllasytws daaapfagls teqtlhlvlk
      421 dlaalhgpvv yrlwdgrgvv krwaedpysq ggfvvqpplf gqgtedydws vpygriyfag
      481 ehtalphgwv etavksglra alrinsnygy gmvdletleh alaeasfaeq ylegdqpeeq
      541 qaqeevnpdr qdlsqkhllv etgpdgqqhv fvenipeple hvfmktnpqe kghkhqiiyp
      601 sehghvhgev ipegpghvhr khghvgsgtl qhmhgevdhs
//
LOCUS       NP_001401281            1376 aa            linear   ROD 28-APR-2025
DEFINITION  misshapen-like kinase 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001401281 XP_006246780
VERSION     NP_001401281.1
DBSOURCE    REFSEQ: accession NM_001414352.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1376)
  AUTHORS   Gloerich,M., ten Klooster,J.P., Vliem,M.J., Koorman,T.,
            Zwartkruis,F.J., Clevers,H. and Bos,J.L.
  TITLE     Rap2A links intestinal cell polarity to brush border formation
  JOURNAL   Nat Cell Biol 14 (8), 793-801 (2012)
   PUBMED   22797597
REFERENCE   2  (residues 1 to 1376)
  AUTHORS   Kaneko,S., Chen,X., Lu,P., Yao,X., Wright,T.G., Rajurkar,M.,
            Kariya,K., Mao,J., Ip,Y.T. and Xu,L.
  TITLE     Smad inhibition by the Ste20 kinase Misshapen
  JOURNAL   Proc Natl Acad Sci U S A 108 (27), 11127-11132 (2011)
   PUBMED   21690388
REFERENCE   3  (residues 1 to 1376)
  AUTHORS   Hussain,N.K., Hsin,H., Huganir,R.L. and Sheng,M.
  TITLE     MINK and TNIK differentially act on Rap2-mediated signal
            transduction to regulate neuronal structure and AMPA receptor
            function
  JOURNAL   J Neurosci 30 (44), 14786-14794 (2010)
   PUBMED   21048137
REFERENCE   4  (residues 1 to 1376)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 1376)
  AUTHORS   Nonaka,H., Takei,K., Umikawa,M., Oshiro,M., Kuninaka,K.,
            Bayarjargal,M., Asato,T., Yamashiro,Y., Uechi,Y., Endo,S.,
            Suzuki,T. and Kariya,K.I.
  TITLE     MINK is a Rap2 effector for phosphorylation of the postsynaptic
            scaffold protein TANC1
  JOURNAL   Biochem Biophys Res Commun 377 (2), 573-578 (2008)
   PUBMED   18930710
REFERENCE   6  (residues 1 to 1376)
  AUTHORS   McCarty,N., Paust,S., Ikizawa,K., Dan,I., Li,X. and Cantor,H.
  TITLE     Signaling by the kinase MINK is essential in the negative selection
            of autoreactive thymocytes
  JOURNAL   Nat Immunol 6 (1), 65-72 (2005)
   PUBMED   15608642
  REMARK    Erratum:[Nat Immunol. 2005 Feb;6(2):219]
REFERENCE   7  (residues 1 to 1376)
  AUTHORS   Hu,Y., Leo,C., Yu,S., Huang,B.C., Wang,H., Shen,M., Luo,Y.,
            Daniel-Issakani,S., Payan,D.G. and Xu,X.
  TITLE     Identification and functional characterization of a novel human
            misshapen/Nck interacting kinase-related kinase, hMINK beta
  JOURNAL   J Biol Chem 279 (52), 54387-54397 (2004)
   PUBMED   15469942
  REMARK    Erratum:[J Biol Chem. 2005 Feb 11;280(6):5128]
REFERENCE   8  (residues 1 to 1376)
  AUTHORS   Dan,I., Watanabe,N.M., Kobayashi,T., Yamashita-Suzuki,K.,
            Fukagaya,Y., Kajikawa,E., Kimura,W.K., Nakashima,T.M.,
            Matsumoto,K., Ninomiya-Tsuji,J. and Kusumi,A.
  TITLE     Molecular cloning of MINK, a novel member of mammalian GCK family
            kinases, which is up-regulated during postnatal mouse cerebral
            development
  JOURNAL   FEBS Lett 469 (1), 19-23 (2000)
   PUBMED   10708748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Nov 18, 2022 this sequence version replaced XP_006246780.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1376
                     /product="misshapen-like kinase 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="MEK kinase kinase 6; GCK family kinase MiNK;
                     misshapen/NIK-related kinase; MAPK/ERK kinase kinase
                     kinase 6; mitogen-activated protein kinase kinase kinase
                     kinase 6"
                     /calculated_mol_wt=155197
     Region          8..289
                     /region_name="STKc_MAP4K4_6_N"
                     /note="N-terminal Catalytic domain of the Serine/Threonine
                     Kinases, Mitogen-Activated Protein Kinase Kinase Kinase
                     Kinase 4 and 6; cd06636"
                     /db_xref="CDD:270806"
     Site            order(31..35,39,52,54,83,105..108,111..112,115,153,
                     155..158,160,170..171,174,188..191,193,225,234)
                     /site_type="active"
                     /db_xref="CDD:270806"
     Site            order(31..35,39,52,54,83,105..108,111..112,115,157..158,
                     160,171)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270806"
     Site            order(34..35,153,155..157,174,188..191,193,225,234)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270806"
     Site            170..193
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270806"
     Region          549..>864
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1058..1356
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..1376
                     /gene="Mink1"
                     /gene_synonym="MEKKK 6"
                     /coded_by="NM_001414352.1:203..4333"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:303259"
                     /db_xref="RGD:1359135"
ORIGIN      
        1 mgdpaparsl ddidlsalrd pagifelvev vgngtygqvy kgrhvktgql aaikvmdvte
       61 deeeeikqei nmlkkyshhr niatyygafi kksppgnddq lwlvmefcga gsvtdlvknt
      121 kgnalkedci ayicreilrg lahlhahkvi hrdikgqnvl ltenaevklv dfgvsaqldr
      181 tvgrrntfig tpywmapevi acdenpdaty dyrsdiwslg itaiemaega pplcdmhpmr
      241 alfliprnpp prlkskkwsk kftdfidtcl iktylsrppt eqllkfpfir dqpterqvri
      301 qlkdhidrsr kkrgekeete yeysgseeed dshgeegeps simnvpgest lrreflrlqq
      361 enksnsealk qqqqlqqqqq rdpeahikhl lhqrqrriee qkeerrrvee qqrrereqrk
      421 lqekeqqrrl edmqalrree errqaereqe yirhrleeeq rqleilqqql lqeqallley
      481 krkqleeqrq serlqrqlqq ehaylkslqq qqqqqqqlqk qqqqqqqqqq qqqqqqilpg
      541 drkplyhygr ginpadkpaw areveerarm nkqqnsplak tkpssagpep pipqaspspp
      601 gplsqtppmq rpvepqegph kslvahrvpl kpyaapvprs qslqdqptrn laafpashdp
      661 dpaavptpta tpsargavir qnsdptsegp gpspnppswv rpdneappkv pqrtssiata
      721 lntsgaggsr paqavrarpr snsawqiylq rraergtpkp pgppaqppgp pntssnpdlr
      781 rsdpgwersd svlpashghl pqagslernr nrvgastkld sspvlspgnk akpedhrsrp
      841 grpadfvllk ertldeapkp pkkamdysss seevessede eeegdgepse gsrdtpggrs
      901 dgdtdsvstm vvhdveevsg tqpsygggtm vvqrtpeeer sllladsngy tnlpdvvqps
      961 hsptensqgq spptkdgggd yqsrglvkap gkssftmfvd lgiyqpggsg dtipitalvg
     1021 geggrldqlq fdvrkgsvvn vnptntrahs etpeirkykk rfnseilcaa lwgvnllvgt
     1081 englmlldrs gqgkvyglig rrrfqqmdvl eglnllitis gkrnklrvyy lswlrnkilh
     1141 ndpevekkqg wttvgdmegc ghyrvvkyer ikflvialkn svevyawapk pyhkfmafks
     1201 fadlphrpll vdltveegqr lkviygssag fhavdvdsgn sydiyipvhi qsqitphaiv
     1261 flpntdgmem llcyedegvy vntygriikd vvlqwgempt svayicsnqi mgwgekaiei
     1321 rsvetghldg vfmhkraqrl kflcerndkv ffasvrsggs sqvyfmtlnr ncimnw
//
LOCUS       NP_001100462             721 aa            linear   ROD 28-APR-2025
DEFINITION  cytoplasmic polyadenylation element-binding protein 4 [Rattus
            norvegicus].
ACCESSION   NP_001100462 XP_001064017 XP_220269
VERSION     NP_001100462.1
DBSOURCE    REFSEQ: accession NM_001106992.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Calderone,V., Gallego,J., Fernandez-Miranda,G., Garcia-Pras,E.,
            Maillo,C., Berzigotti,A., Mejias,M., Bava,F.A., Angulo-Urarte,A.,
            Graupera,M., Navarro,P., Bosch,J., Fernandez,M. and Mendez,R.
  TITLE     Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic
            Expression of Vascular Endothelial Growth Factor and Angiogenesis
            in Chronic Liver Disease
  JOURNAL   Gastroenterology 150 (4), 982-97 (2016)
   PUBMED   26627607
  REMARK    GeneRIF: Identify a mechanism of VEGF overexpression in liver and
            mesentery that promotes pathologic, but not physiologic,
            angiogenesis, via sequential and nonredundant functions of CPEB1
            and CPEB4.
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Kan,M.C., Oruganty-Das,A., Cooper-Morgan,A., Jin,G., Swanger,S.A.,
            Bassell,G.J., Florman,H., van Leyen,K. and Richter,J.D.
  TITLE     CPEB4 is a cell survival protein retained in the nucleus upon
            ischemia or endoplasmic reticulum calcium depletion
  JOURNAL   Mol Cell Biol 30 (24), 5658-5671 (2010)
   PUBMED   20937770
  REMARK    GeneRIF: Data show that treatment of neurons with ionotropic
            glutamate receptor agonists causes CPEB4 to accumulate in the
            nucleus.
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Peng,S.C., Lai,Y.T., Huang,H.Y., Huang,H.D. and Huang,Y.S.
  TITLE     A novel role of CPEB3 in regulating EGFR gene transcription via
            association with Stat5b in neurons
  JOURNAL   Nucleic Acids Res 38 (21), 7446-7457 (2010)
   PUBMED   20639532
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Huang,Y.S., Kan,M.C., Lin,C.L. and Richter,J.D.
  TITLE     CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and
            translational control of AMPA receptor GluR2 mRNA
  JOURNAL   EMBO J 25 (20), 4865-4876 (2006)
   PUBMED   17024188
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001064017.1, XP_220269.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..721
                     /product="cytoplasmic polyadenylation element-binding
                     protein 4"
                     /calculated_mol_wt=79014
     Region          464..555
                     /region_name="RRM1_CPEB2_like"
                     /note="RNA recognition motif 1 (RRM1) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12724"
                     /db_xref="CDD:410123"
     Region          572..652
                     /region_name="RRM2_CPEB2_like"
                     /note="RNA recognition motif 2 (RRM2) found in cytoplasmic
                     polyadenylation element-binding protein CPEB-2, CPEB-3,
                     CPEB-4 and similar protiens; cd12726"
                     /db_xref="CDD:410125"
     Region          647..708
                     /region_name="CEBP_ZZ"
                     /note="Cytoplasmic polyadenylation element-binding protein
                     ZZ domain; pfam16366"
                     /db_xref="CDD:465105"
     CDS             1..721
                     /gene="Cpeb4"
                     /coded_by="NM_001106992.1:1..2166"
                     /db_xref="GeneID:303010"
                     /db_xref="RGD:1311931"
ORIGIN      
        1 mgdygfgvlv qsntgnksaf pvrfhphlqp phhhqnatpn paafinnnta angssagsaw
       61 lfpapathni qdeilgseka ksqqqeqqdp lekqqlspsp gqeagilpet ekakaeenpg
      121 dnssensngk ekiriespvl tgfdyqeatg lgtstqplts sassltgfsn wsaaiapsss
      181 tiinedasff hqggvpgasa nngallfqnf phhvspgfgg sfspqigpls qhhphhphfq
      241 hhhsqhqqqr rspasphppp fthrnaafnq lphlannlnk ppspwssyqs psptpsssws
      301 pggggyggwg asqgrdhrrg lnggitplns isplkknfas nhiqlqkyar pssafapksw
      361 medslnradn ifpfpdrprt fdmhslessl idimraends ikgrlnysyp gsdsslling
      421 qsslfpmedg flddgrgdqp lhsglgsphc fthqngerve rysrkvfvgg lppdidedei
      481 tasfrrfgpl ivdwphkaes ksyfppkgya fllfqdessv qalidaciee dgklylcvss
      541 ptikdkpvqi rpwnlsdsdf vmdgsqpldp rktifvggvp rplravelam imdrlyggvc
      601 yagidtdpel kypkgagrva fsnqqsyiaa isarfvqlqh geidkrvevk pyvlddqlcd
      661 ecqgarcggk fapffcanvt clqyyceycw aaihsragre fhkplvkegg drprhisfrw
      721 n
//
LOCUS       NP_001387987             864 aa            linear   ROD 28-APR-2025
DEFINITION  janus kinase and microtubule-interacting protein 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001387987 XP_006251156
VERSION     NP_001387987.1
DBSOURCE    REFSEQ: accession NM_001401058.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Berg,J.M., Lee,C., Chen,L., Galvan,L., Cepeda,C., Chen,J.Y.,
            Penagarikano,O., Stein,J.L., Li,A., Oguro-Ando,A., Miller,J.A.,
            Vashisht,A.A., Starks,M.E., Kite,E.P., Tam,E., Gdalyahu,A.,
            Al-Sharif,N.B., Burkett,Z.D., White,S.A., Fears,S.C., Levine,M.S.,
            Wohlschlegel,J.A. and Geschwind,D.H.
  TITLE     JAKMIP1, a Novel Regulator of Neuronal Translation, Modulates
            Synaptic Function and Autistic-like Behaviors in Mouse
  JOURNAL   Neuron 88 (6), 1173-1191 (2015)
   PUBMED   26627310
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Vidal,R.L., Fuentes,P., Valenzuela,J.I., Alvarado-Diaz,C.P.,
            Ramirez,O.A., Kukuljan,M. and Couve,A.
  TITLE     RNA interference of Marlin-1/Jakmip1 results in abnormal
            morphogenesis and migration of cortical pyramidal neurons
  JOURNAL   Mol Cell Neurosci 51 (1-2), 1-11 (2012)
   PUBMED   22828129
  REMARK    GeneRIF: RNA interference of Marlin-1 in vivo results in abnormal
            migration and abnormal morphology of newborn pyramidal neurons
            during the formation of the cortex.
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Vidal,R.L., Valenzuela,J.I., Lujan,R. and Couve,A.
  TITLE     Cellular and subcellular localization of Marlin-1 in the brain
  JOURNAL   BMC Neurosci 10, 37 (2009)
   PUBMED   19386132
  REMARK    GeneRIF: Marlin-1 is enriched in restricted areas of the brain
            including olfactory bulb, cerebral cortex, hippocampus and
            cerebellum; it is abundant in dendrites and axons of hippocampal
            neurons, associated with microtubules at the ultrastructural level.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Vidal,R.L., Ramirez,A., Castro,M., Concha,I.I. and Couve,A.
  TITLE     Marlin-1 is expressed in testis and associates to the cytoskeleton
            and GABAB receptors
  JOURNAL   J Cell Biochem 103 (3), 886-895 (2008)
   PUBMED   17668444
  REMARK    GeneRIF: Our findings demonstrate that Marlin-1 associates with a
            microtubule fraction and with GABA(B) receptors in testis
            suggesting that the set of protein interactions of Marlin-1 are
            conserved in different tissues.
REFERENCE   5  (residues 1 to 864)
  AUTHORS   Nishimura,Y., Martin,C.L., Vazquez-Lopez,A., Spence,S.J.,
            Alvarez-Retuerto,A.I., Sigman,M., Steindler,C., Pellegrini,S.,
            Schanen,N.C., Warren,S.T. and Geschwind,D.H.
  TITLE     Genome-wide expression profiling of lymphoblastoid cell lines
            distinguishes different forms of autism and reveals shared pathways
  JOURNAL   Hum Mol Genet 16 (14), 1682-1698 (2007)
   PUBMED   17519220
REFERENCE   6  (residues 1 to 864)
  AUTHORS   Vidal,R.L., Ramirez,O.A., Sandoval,L., Koenig-Robert,R., Hartel,S.
            and Couve,A.
  TITLE     Marlin-1 and conventional kinesin link GABAB receptors to the
            cytoskeleton and regulate receptor transport
  JOURNAL   Mol Cell Neurosci 35 (3), 501-512 (2007)
   PUBMED   17532644
REFERENCE   7  (residues 1 to 864)
  AUTHORS   Couve,A., Restituito,S., Brandon,J.M., Charles,K.J., Bawagan,H.,
            Freeman,K.B., Pangalos,M.N., Calver,A.R. and Moss,S.J.
  TITLE     Marlin-1, a novel RNA-binding protein associates with GABA
            receptors
  JOURNAL   J Biol Chem 279 (14), 13934-13943 (2004)
   PUBMED   14718537
  REMARK    GeneRIF: Marlin-1 functions to regulate the cellular levels of
            GABA(B) R2 subunits, which may have significant effects on the
            production of functional GABA(B) receptor heterodimers.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 1, 2022 this sequence version replaced XP_006251156.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..864
                     /product="janus kinase and microtubule-interacting protein
                     1 isoform 2"
                     /note="multiple alpha helices and RNA-linker protein 1;
                     multiple coiled-coil GABABR1-binding protein"
                     /calculated_mol_wt=100492
     Region          1..365
                     /region_name="Mediates association with microtubules.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          <24..>607
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          415..612
                     /region_name="JAKMIP_CC3"
                     /note="JAKMIP CC3 domain; pfam16034"
                     /db_xref="CDD:464986"
     Region          452..481
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96N16; propagated from
                     UniProtKB/Swiss-Prot (Q3SWS9.1)"
     Region          <678..>814
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..864
                     /gene="Jakmip1"
                     /gene_synonym="Marlin-1; Marlin1"
                     /coded_by="NM_001401058.1:383..2977"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:305434"
                     /db_xref="RGD:1562401"
ORIGIN      
        1 mskkgrskge kpetetdsvq maneelrakl tniqiefqqe kskvgklrer lqeaklereq
       61 eqrrhtayis elkaklheek tkelqalrea lirqheqeaa rtakikegel qrlqatlnvl
      121 rdgaadkvkt alladareea rrtfdgerqr lqqeilelka arkqaeeals ncmqadkaka
      181 adlraayqah qdevhrikre cerdirrlmd eikgkervil alekelgvqa gqtqrlllqk
      241 ealdeqlvqv keaerhhssp krelppgigd maelmggqdq hmderdvrrf qlkiaelnsv
      301 irkledrntl ladernellk rsretevqlk plveknkrmn kknedllhsi qrmeeklksl
      361 trenvemkek lsaqaslkrh tslndlsltr deqeieflrl qvleqqhvid dlslererll
      421 rskrhrgksl kppkkhvvet ffgfdeesvd setlsetsyn tdrtdrtpat peedldettt
      481 reeadlrfcq ltreyqalqr ayallqeqvg gtldaerear treqlqadll rcqakiedle
      541 kllvekgqda awveekqvlm rtnqdlleki yrlemeenql ksemqdakdq nellefrvle
      601 leererrspa fnlqittfpe nnssalqlfc hqegvkgvni selmknldil gdngnlrnee
      661 qvaviqagtv lalcekwlkq iegteaaltq kmmdlekekd qfsrqkgyle qeldyrkeal
      721 dqaylkiqdl eatlynalqq epgrrasesl sasqredlqa avekvrrqll rqsrefdsqi
      781 lrermellqq aqqkiremeg klelqrrqlk eleekhsfcg ledshaprtr arqrisgitr
      841 vpvvphphsn qnptvqqsys ksga
//
LOCUS       NP_001385494             439 aa            linear   ROD 28-APR-2025
DEFINITION  growth hormone-releasing hormone receptor isoform 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_001385494 XP_017447971
VERSION     NP_001385494.1
DBSOURCE    REFSEQ: accession NM_001398565.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Florea,V., Majid,S.S., Kanashiro-Takeuchi,R.M., Cai,R.Z.,
            Block,N.L., Schally,A.V., Hare,J.M. and Rodrigues,C.O.
  TITLE     Agonists of growth hormone-releasing hormone stimulate self-renewal
            of cardiac stem cells and promote their survival
  JOURNAL   Proc Natl Acad Sci U S A 111 (48), 17260-17265 (2014)
   PUBMED   25404316
  REMARK    GeneRIF: Data show that cardiac stem cells (CSCs) isolated from
            mouse, rat and pig myocardium express growth hormone-releasing
            hormone receptor (GHRH-R) and agonists of GHRH-R stimulate their
            proliferation and survival.
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Epitacio-Pereira,C.C., Silva,G.M., Salvatori,R., Santana,J.A.,
            Pereira,F.A., Gois-Junior,M.B., Britto,A.V., Oliveira,C.R.,
            Souza,A.H., Santos,E.G., Campos,V.C., Pereira,R.M., Valenca,E.H.,
            Barbosa,R.A., Farias,M.I., de Paula,F.J., Ribeiro,T.V.,
            Oliveira,M.C. and Aguiar-Oliveira,M.H.
  TITLE     Isolated GH deficiency due to a GHRH receptor mutation causes hip
            joint problems and genu valgum, and reduces size but not density of
            trabecular and mixed bone
  JOURNAL   J Clin Endocrinol Metab 98 (11), E1710-E1715 (2013)
   PUBMED   24057284
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Leggett,J., Harper,E., Waite,E., Marks,P., Martinez,A. and
            Lightman,S.
  TITLE     GHRH receptor-targeted botulinum neurotoxin selectively inhibits
            pulsatile GH secretion in male rats
  JOURNAL   Endocrinology 154 (9), 3305-3318 (2013)
   PUBMED   23825127
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Weigent,D.A.
  TITLE     Expression of lymphocyte-derived growth hormone (GH) and
            GH-releasing hormone receptors in aging rats
  JOURNAL   Cell Immunol 282 (2), 71-78 (2013)
   PUBMED   23770714
  REMARK    GeneRIF: Data show alterations in growth hormone (GH) synthesis and
            expression of GH-releasing hormone receptor (GHRH receptor) on
            cells of the immune system that may play a role in the immune
            response in aging.
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Penna,C., Settanni,F., Tullio,F., Trovato,L., Pagliaro,P.,
            Alloatti,G., Ghigo,E. and Granata,R.
  TITLE     GH-releasing hormone induces cardioprotection in isolated male rat
            heart via activation of RISK and SAFE pathways
  JOURNAL   Endocrinology 154 (4), 1624-1635 (2013)
   PUBMED   23417421
  REMARK    GeneRIF: GHRH protects the heart from I/R injury through
            GHRHR-mediated mechanisms, leading to activation of RISK and SAFE
            pathways, which converge on mitochondria and possibly on
            AMP-activated protein kinase.
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Lin,C., Lin,S.C., Chang,C.P. and Rosenfeld,M.G.
  TITLE     Pit-1-dependent expression of the receptor for growth hormone
            releasing factor mediates pituitary cell growth
  JOURNAL   Nature 360 (6406), 765-768 (1992)
   PUBMED   1334535
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Mayo,K.E.
  TITLE     Molecular cloning and expression of a pituitary-specific receptor
            for growth hormone-releasing hormone
  JOURNAL   Mol Endocrinol 6 (10), 1734-1744 (1992)
   PUBMED   1333056
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Wilson,D.B. and Wyatt,D.P.
  TITLE     Adrenocorticotropic cell distribution in adult and embryonic
            pituitaries of the little (lit) mutant mouse
  JOURNAL   Anat Embryol (Berl) 186 (4), 347-353 (1992)
   PUBMED   1329576
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Beamer,W.H. and Eicher,E.M.
  TITLE     Stimulation of growth in the little mouse
  JOURNAL   J Endocrinol 71 (1), 37-45 (1976)
   PUBMED   978118
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Eicher,E.M. and Beamer,W.G.
  TITLE     Inherited ateliotic dwarfism in mice. Characteristics of the
            mutation, little, on chromosome 6
  JOURNAL   J Hered 67 (2), 87-91 (1976)
   PUBMED   1270792
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Dec 20, 2021 this sequence version replaced XP_017447971.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF122055.1, SRR26360172.463744.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..439
                     /product="growth hormone-releasing hormone receptor
                     isoform 3 precursor"
                     /note="GRFR; GRF receptor; GHRH receptor; growth
                     hormone-releasing factor receptor; Growth hormone -
                     releasing receptor"
                     /calculated_mol_wt=46307
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2475
     Region          54..112
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          126..393
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          129..153
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Region          162..183
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          203..225
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Region          244..260
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          278..301
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          328..350
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          355..380
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..439
                     /gene="Ghrhr"
                     /gene_synonym="GHRHREC"
                     /coded_by="NM_001398565.1:86..1405"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:25321"
                     /db_xref="RGD:2688"
ORIGIN      
        1 mdsllwatwv lcllnlwgva lghlhlecdf itqlrddela clqaaegtnn ssmgcpgtwd
       61 gllcwpptgs gqwvslpcpe ffshfgsdpg avkrdctitg wsdpfppypv acpvplellt
      121 eeksyfstvk iiyttghsis ivalcvaiai lvalrrlhcp rnyihtqlfa tfilkasavf
      181 lkdaavfqgd stdhcsmsti lckvsvavsh fatmtnfswl laeavylscl lastsprskp
      241 afwwlvlagw glpvlctgtw vgcklafedt acwdlddssp ywwiikgpiv lsvgvnfglf
      301 lniicillrk lgpaqgglht raqywrlsks tllliplfgi hyiifnflpd saglgirlpl
      361 elglgsfqgf vvavlycfln qevrteisrk wyghdpellp arrtctewtt pprsrvkvpv
      421 yqpptfsvpv cphlfflpi
//
LOCUS       NP_001418674             189 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC681385 isoform 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001418674 XP_063140906
VERSION     NP_001418674.1
DBSOURCE    REFSEQ: accession NM_001431745.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jul 22, 2024 this sequence version replaced XP_063140906.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.2553000.1,
                                           SRR22582416.367511.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..189
                     /product="uncharacterized protein LOC681385 isoform 2
                     precursor"
                     /note="vomeronasal secretory protein 2; rCG64269-like"
                     /calculated_mol_wt=20043
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2134
     Region          28..169
                     /region_name="lipocalin_1_3_4_13-like"
                     /note="lipocalin-1, -3, -4, -13 and similar proteins;
                     cd19414"
                     /db_xref="CDD:381189"
     Site            order(32,36,47,58,60,68,70,72,83,85,87,96,98,102..103,105,
                     107,116,118,120,129,131,133,135)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381189"
     Site            order(47,83,102..103,129,131)
                     /site_type="other"
                     /note="citrate-binding site [ion binding]"
                     /db_xref="CDD:381189"
     CDS             1..189
                     /gene="Lcn4l2"
                     /coded_by="NM_001431745.1:56..625"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:681385"
                     /db_xref="RGD:1596705"
ORIGIN      
        1 mkyllltvll fgllailqaq ddlpflsdek klsgiwflka tvsqrrqtge qtvvafphsl
       61 tcpeegilei rntfmsggqc ikillrmqkt eepgqysnff rhnlfyiyel pvkdhyifym
      121 esipfekkfq eghligkcpk enlealeefk efiqrkgllq eniivpeqrv vyflshstqe
      181 pqmlshlch
//
LOCUS       NP_001100636             913 aa            linear   ROD 28-APR-2025
DEFINITION  transportin-2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100636 XP_001070750 XP_222478
VERSION     NP_001100636.1
DBSOURCE    REFSEQ: accession NM_001107166.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   van der Giessen,K. and Gallouzi,I.E.
  TITLE     Involvement of transportin 2-mediated HuR import in muscle cell
            differentiation
  JOURNAL   Mol Biol Cell 18 (7), 2619-2629 (2007)
   PUBMED   17475777
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_222478.4, XP_001070750.1.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..913
                     /product="transportin-2 isoform 1"
                     /note="transportin 2 (importin 3, karyopherin beta 2b)"
                     /calculated_mol_wt=102746
     Region          22..756
                     /region_name="KAP95"
                     /note="Karyopherin (importin) beta [Intracellular
                     trafficking and secretion]; COG5215"
                     /db_xref="CDD:227540"
     Region          93..114
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(106..107,110,113..114,144..145,148,151..152,155,
                     190..191,194,197..198,201,231..232,235,238..239,272..273,
                     276,279..280)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          127..155
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          165..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          213..239
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          252..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(412..413,416,419..420,453..454,457,460..461,464,
                     495..496,499,502..503,506,536..537,540,543..544,579..580,
                     585,588..589)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          436..464
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          477..507
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          518..544
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          559..590
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          659..693
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          705..735
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          746..774
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..913
                     /gene="Tnpo2"
                     /coded_by="NM_001107166.2:112..2853"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304670"
                     /db_xref="RGD:1310356"
ORIGIN      
        1 mdwqpdeqgl qqvlqllkds qspntatqri vqdklkqlnq fpdfnnylif vltrlksede
       61 ptrslsglil knnvkahyqs fpppvadfik qeclnnigda ssliratigi littiaskge
      121 lqmwpellpq lcnllnsedy ntcegafgal qkicedssel ldsdalnrpl nimipkflqf
      181 fkhcspkirs haiacvnqfi mdraqalmdn idtfiehlfa lavdddpevr knvcralvml
      241 levridrlip hmhsiiqyml qrtqdhdenv aleacefwlt laeqpickev lashlvqlip
      301 ilvngmkyse idiillkgdv eedeavpdse qdikprfhks rtvtltheae rpdgsedaed
      361 dddddalsdw nlrkcsaaal dvlanvfree llphllpllk gllfhpewvv kesgilvlga
      421 iaegcmqgmv pylpeliphl iqclsdkkal vrsiacwtls ryahwvvsqp pdmhlkplmt
      481 ellkrildgn krvqeaacsa fatleeeact elvpylsyil dtlvfafgky qhknllilyd
      541 aigtladsvg hhlnqpeyiq klmppliqkw nelkdedkdl fplleclssv atalqsgflp
      601 ycepvyqrcv tlvqktlaqa mmytqhpeqy eapdkdfmiv aldllsglae glgghveqlv
      661 arsnimtllf qcmqdsmpev rqssfallgd ltkacfihvk pciaefmpil gtnlnpefis
      721 vcnnatwaig eicmqmgaem qpyvqmvlsn lveiinrpnt pktllentai tigrlgyvcp
      781 qevapmlqqf irpwctslrn irdneekdsa frgicmmigv npggvvqdfi ffcdavaswv
      841 spkddlrdmf ykilhgfkdq vgeenwqqfs eqfppllker laafygvfvc vivggcagec
      901 aasrshcalv egg
//
LOCUS       NP_001182128            2354 aa            linear   ROD 28-APR-2025
DEFINITION  voltage-dependent N-type calcium channel subunit alpha-1B isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001182128
VERSION     NP_001182128.1
DBSOURCE    REFSEQ: accession NM_001195199.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2354)
  AUTHORS   Cai,Z., Quan,L., Chang,X., Qiu,Z. and Zhou,H.
  TITLE     High-voltage long-duration pulsed radiofrequency attenuates
            neuropathic pain in CCI rats by inhibiting Cav2.2 in spinal dorsal
            horn and dorsal root ganglion
  JOURNAL   Brain Res 1785, 147892 (2022)
   PUBMED   35341732
  REMARK    GeneRIF: High-voltage long-duration pulsed radiofrequency
            attenuates neuropathic pain in CCI rats by inhibiting Cav2.2 in
            spinal dorsal horn and dorsal root ganglion.
REFERENCE   2  (residues 1 to 2354)
  AUTHORS   Silveirinha,V.C., Lin,H., Tanifuji,S., Mochida,S., Cottrell,G.S.,
            Cimarosti,H. and Stephens,G.J.
  TITLE     CaV2.2 (N-type) voltage-gated calcium channels are activated by
            SUMOylation pathways
  JOURNAL   Cell Calcium 93, 102326 (2021)
   PUBMED   33360835
  REMARK    GeneRIF: CaV2.2 (N-type) voltage-gated calcium channels are
            activated by SUMOylation pathways.
REFERENCE   3  (residues 1 to 2354)
  AUTHORS   Castro,H., Bermeo,K., Arenas,I. and Garcia,D.E.
  TITLE     Maintenance of CaV2.2 channel-current by PIP2 unveiled by neomycin
            in sympathetic neurons of the rat
  JOURNAL   Arch Biochem Biophys 682, 108261 (2020)
   PUBMED   31923392
  REMARK    GeneRIF: interacting PIP2 charges not only underly the maintenance
            of the channel-current but also that charge screening of PIP2 by
            itself unveils the voltage-independent features of CaV2.2 channels
            in SCG neurons
REFERENCE   4  (residues 1 to 2354)
  AUTHORS   Buchta,W.C., Moutal,A., Hines,B., Garcia-Keller,C., Smith,A.C.W.,
            Kalivas,P., Khanna,R. and Riegel,A.C.
  TITLE     Dynamic CRMP2 Regulation of CaV2.2 in the Prefrontal Cortex
            Contributes to the Reinstatement of Cocaine Seeking
  JOURNAL   Mol Neurobiol 57 (1), 346-357 (2020)
   PUBMED   31359322
  REMARK    GeneRIF: Dynamic CRMP2 Regulation of CaV2.2 in the Prefrontal
            Cortex Contributes to the Reinstatement of Cocaine Seeking.
REFERENCE   5  (residues 1 to 2354)
  AUTHORS   Gandini,M.A., Souza,I.A., Raval,D., Xu,J., Pan,Y.X. and
            Zamponi,G.W.
  TITLE     Differential regulation of Cav2.2 channel exon 37 variants by
            alternatively spliced mu-opioid receptors
  JOURNAL   Mol Brain 12 (1), 98 (2019)
   PUBMED   31775826
  REMARK    GeneRIF: This study provides new insights into the roles of the MOR
            full-length C-terminal variants in modulating Cav2.2 channel
            isoform activities.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2354)
  AUTHORS   Wheeler,D.B., Randall,A. and Tsien,R.W.
  TITLE     Roles of N-type and Q-type Ca2+ channels in supporting hippocampal
            synaptic transmission
  JOURNAL   Science 264 (5155), 107-111 (1994)
   PUBMED   7832825
REFERENCE   7  (residues 1 to 2354)
  AUTHORS   Hell,J.W., Appleyard,S.M., Yokoyama,C.T., Warner,C. and
            Catterall,W.A.
  TITLE     Differential phosphorylation of two size forms of the N-type
            calcium channel alpha 1 subunit which have different COOH termini
  JOURNAL   J Biol Chem 269 (10), 7390-7396 (1994)
   PUBMED   8125957
REFERENCE   8  (residues 1 to 2354)
  AUTHORS   Pragnell,M., De Waard,M., Mori,Y., Tanabe,T., Snutch,T.P. and
            Campbell,K.P.
  TITLE     Calcium channel beta-subunit binds to a conserved motif in the I-II
            cytoplasmic linker of the alpha 1-subunit
  JOURNAL   Nature 368 (6466), 67-70 (1994)
   PUBMED   7509046
REFERENCE   9  (residues 1 to 2354)
  AUTHORS   Dubel,S.J., Starr,T.V., Hell,J., Ahlijanian,M.K., Enyeart,J.J.,
            Catterall,W.A. and Snutch,T.P.
  TITLE     Molecular cloning of the alpha-1 subunit of an
            omega-conotoxin-sensitive calcium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (11), 5058-5062 (1992)
   PUBMED   1317580
REFERENCE   10 (residues 1 to 2354)
  AUTHORS   Snutch,T.P., Leonard,J.P., Gilbert,M.M., Lester,H.A. and
            Davidson,N.
  TITLE     Rat brain expresses a heterogeneous family of calcium channels
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3391-3395 (1990)
   PUBMED   1692134
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HQ008360.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2354
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..2354
                     /product="voltage-dependent N-type calcium channel subunit
                     alpha-1B isoform 1"
                     /note="voltage-dependent N-type calcium channel subunit
                     alpha-1B; voltage-dependent N-type calcium channel subunit
                     alpha-1B-like; voltage gated N-type calcium channel
                     Ca(v)2.2; brain calcium channel III; voltage-gated calcium
                     channel subunit alpha Cav2.2; calcium channel, L type,
                     alpha-1 polypeptide; calcium channel, voltage-dependent, N
                     type, alpha 1B subunit"
                     /calculated_mol_wt=263908
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            22
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          82..359
                     /region_name="I"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            91..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          94..367
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            132..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            164..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            188..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            222..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q00975; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            314
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            332..356
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          379..396
                     /region_name="Binding to the beta subunit"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          469..713
                     /region_name="II"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          482..721
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            484..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            513..535
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            546..567
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            575..587
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            606..631
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            664
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            684..710
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          820..1041
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1071..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1168..1398
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1170..1188
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1197..1221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1263..1283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1302..1321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1383
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1409..1434
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1488..1737
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1490..1508
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1517..1541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1552..1573
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1581
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1582..1600
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1620..1639
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1673
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1693
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1702..1725
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1746..1799
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1810..1887
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1971..>2273
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1999..2220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     CDS             1..2354
                     /gene="Cacna1b"
                     /gene_synonym="BIII"
                     /coded_by="NM_001195199.2:125..7189"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:257648"
                     /db_xref="RGD:628852"
ORIGIN      
        1 mvrfgdelgg ryggtggger argggaggag gpgqgglppg qrvlykqsia qrartmalyn
       61 pipvkqncft vnrslfvfse dnvvrkyakr itewppfeym ilatiianci vlaleqhlpd
      121 gdktpmserl ddtepyfigi fcfeagikii algfvfhkgs ylrngwnvmd fvvvltgila
      181 tagtdfdlrt lravrvlrpl klvsgipslq vvlksimkam vpllqiglll ffailmfaii
      241 glefymgkfh kacfpnstda epvgdfpcgk eaparlcdsd tecreywpgp nfgitnfdni
      301 lfailtvfqc itmegwtdil yntndaagnt wnwlyfipli iigsffmlnl vlgvlsgefa
      361 kerervenrr aflklrrqqq ierelngyle wifkaeevml aeedknaeek spldavlkra
      421 atkksrndli haeegedrfv dlcaagspfa raslksgkte sssyfrrkek mfrflirrmv
      481 kaqsfywvvl cvvalntlcv amvhynqpqr lttalyfaef vflglfltem slkmyglgpr
      541 syfrssfncf dfgvivgsif evvwaaikpg tsfgisvlra lrllrifkvt kywnslrnlv
      601 vsllnsmksi isllfllflf ivvfallgmq lfggqfnfqd etpttnfdtf paailtvfqi
      661 ltgedwnavm yhgiesqggv skgmfssfyf ivltlfgnyt llnvflaiav dnlanaqelt
      721 kdeeemeeaa nqklalqkak evaevspmsa anisiaafvk qtrgtvsrss svssvnspqq
      781 nsakarsvwe qrasqlrlqn lrascealys emdpeerlry astrhvrpdm kthmdrplvv
      841 epgrdglrgp agnkskpegt eategadppr rhhrhrdrdk tsastpagge qdrtdcpkae
      901 stetgareer arprrshske apgadtqvrc ersrrhhrrg speeaterep rrhrahrhaq
      961 dsskegkegt apvlvpkger rarhrgprtg pretenseep trrhrakhkv pptleppere
     1021 vaekesnvve gdketrnhqp keprcdleai avtgvgslhm lpstclqkvd eqpedadnqr
     1081 nvtrmgsqps dpsttvhvpv tltgppgeat vvpsantdle gqaegkkeae addvlrrgpr
     1141 pivpyssmfc lsptnllrrf chyivtmryf emvilvvial ssialaaedp vrtdsfrnna
     1201 lkymdyiftg vftfemvikm idlglllhpg ayfrdlwnil dfivvsgalv afafsgskgk
     1261 dintikslrv lrvlrplkti krlpklkavf dcvvnslknv lnilivymlf mfifaviavq
     1321 lfkgkffyct deskelerdc rgqyldyeke eveaqprqwk kydfhydnvl walltlftvs
     1381 tgegwpmvlk hsvdatyeeq gpspgfrmel sifyvvyfvv fpfffvnifv aliiitfqeq
     1441 gdkvmsecsl ekneracidf aisakpltry mpqnkqsfqy ktwtfvvspp feyfimamia
     1501 lntvvlmmkf ydapyeyelm lkclnivfts mfslecilki iafgvlnyfr dawnvfdfvt
     1561 vlgsitdilv teiaetnnfi nlsflrlfra arlikllrqg ytirillwtf vqsfkalpyv
     1621 clliamlffi yaiigmqvfg nialddgtsi nrhnnfrtfl qalmllfrsa tgeawheiml
     1681 sclgnracdp hanasecgsd fayfyfvsfi flcsflmlnl fvavimdnfe yltrdssilg
     1741 phhldefirv waeydpaacg risyndmfem lkhmspplgl gkkcparvay krlvrmnmpi
     1801 snedmtvhft stlmalirta leiklapagt kqhqcdaelr keissvwanl pqktldllvp
     1861 phkpdemtvg kvyaalmifd fykqnkttrd qthqapggls qmgpvslfhp lkatleqtqp
     1921 avlrgarvfl rqksatslsn ggaiqtqesg ikeslswgtq rtqdvlyear aplerghsae
     1981 ipvgqpgala vdvqmqnmtl rgpdgepqpg lesqgraasm prlaaetqpa pnaspmkrsi
     2041 stlaprphgt qlcntvldrp ppsqvshhhh hrchrrrdkk qrslekgpsl svdtegapst
     2101 aagsglphge gstgcrrerk qergrsqerr qpsssssekq rfyscdrfgs reppqpkpsl
     2161 sshpisptaa lepgphpqgs gsvngsplms tsgastpgrg grrqlpqtpl tprpsitykt
     2221 ansspvhfae gqsglpafsp grlsrglseh nallqkepls qplasgsrig sdpylgqrld
     2281 seasahnlpe dtltfeeava tnsgrssrts yvssltsqsh plrrvpngyh ctlglstgvr
     2341 arhsyhhpdq dhwc
//
LOCUS       NP_001416369            1001 aa            linear   ROD 28-APR-2025
DEFINITION  angiomotin-like protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001416369 XP_038938160
VERSION     NP_001416369.1
DBSOURCE    REFSEQ: accession NM_001429440.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Zheng,Y., Vertuani,S., Nystrom,S., Audebert,S., Meijer,I.,
            Tegnebratt,T., Borg,J.P., Uhlen,P., Majumdar,A. and Holmgren,L.
  TITLE     Angiomotin-like protein 1 controls endothelial polarity and
            junction stability during sprouting angiogenesis
  JOURNAL   Circ Res 105 (3), 260-270 (2009)
   PUBMED   19590046
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Fang,L., Wang,X., Yamoah,K., Chen,P.L., Pan,Z.Q. and Huang,L.
  TITLE     Characterization of the human COP9 signalosome complex using
            affinity purification and mass spectrometry
  JOURNAL   J Proteome Res 7 (11), 4914-4925 (2008)
   PUBMED   18850735
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Sugihara-Mizuno,Y., Adachi,M., Kobayashi,Y., Hamazaki,Y.,
            Nishimura,M., Imai,T., Furuse,M. and Tsukita,S.
  TITLE     Molecular characterization of angiomotin/JEAP family proteins:
            interaction with MUPP1/Patj and their endogenous properties
  JOURNAL   Genes Cells 12 (4), 473-486 (2007)
   PUBMED   17397395
REFERENCE   4  (residues 1 to 1001)
  AUTHORS   Patrie,K.M.
  TITLE     Identification and characterization of a novel tight
            junction-associated family of proteins that interacts with a WW
            domain of MAGI-1
  JOURNAL   Biochim Biophys Acta 1745 (1), 131-144 (2005)
   PUBMED   16019084
REFERENCE   5  (residues 1 to 1001)
  AUTHORS   Nishimura,M., Kakizaki,M., Ono,Y., Morimoto,K., Takeuchi,M.,
            Inoue,Y., Imai,T. and Takai,Y.
  TITLE     JEAP, a novel component of tight junctions in exocrine cells
  JOURNAL   J Biol Chem 277 (7), 5583-5587 (2002)
   PUBMED   11733531
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038938160.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.21205.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..1001
                     /product="angiomotin-like protein 1 isoform 1"
                     /note="angiomotin-like protein 1"
                     /calculated_mol_wt=111272
     Region          <481..>739
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          650..856
                     /region_name="Angiomotin_C"
                     /note="Angiomotin C terminal; pfam12240"
                     /db_xref="CDD:463503"
     CDS             1..1001
                     /gene="Amotl1"
                     /coded_by="NM_001429440.1:267..3272"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315430"
                     /db_xref="RGD:1305268"
ORIGIN      
        1 mheglggsmd lsgnwtledg swlsptgdrh fpngrgesdf vdttpasfsp eelapppicy
       61 spgspaqile dhayfypdlq lysgrheapt ltveangglr gksvedplss fhspnflrtp
      121 evemrgsedv asgrvlqrli qeqlrygtpt enmnllaiqh qatgsagpah stnnfsstet
      181 ltqedpqmvy qsarqepqgq ehqgdntvme kqvrstqpqq nneelptyee akaqsqffrg
      241 qqqqqqqqqq qqqqqgqgpl ghtyymaggt sqksrtegrp tvnransgqa hkdealkelk
      301 qghvrslser imqlslerng tkqhlpssgn gksfkaggep spaqpvckal dprgpppeyp
      361 fktkpmkspv sknqdhglyy sdqhpgvlhe mvkpypapqp artevavlry qpppeygvts
      421 rpcqlpfpst vqqhspmssq tssisgplhs vslplplpms laapqpppas psqqlgpdaf
      481 aiveraqqmv eilteenrvl hqelqgcydn adklhkfeke lqsiseayes lvksttkres
      541 ldkamrnkle geirrlhdfn rdlrdrleta nrqlssreye ghedkaaesh hmsqnkeflk
      601 ekeklemela avrtasedhr rhieildqal snaqarvikl eeelrekqay vekveklqqa
      661 ltqlqsacek rgqmerrlrt wlereldalr tqqkhgngqp vnlpeynapa lmelvrekee
      721 rilaleadmt kweqkylees tirhfamsaa aaataerdtt isnhsrngsy gessleahiw
      781 peeeevvqan rrcqdmeyti knlhakiiek damikvlqqr srkdagktds sslrparsvp
      841 siaaatgths rqtsltsgql aedkkeektw kgsigfllgk ehqgqasapl lpatpasals
      901 pptsttsass thaktgskds stqtdkitel fwpsmaslps rgrlstapsn spvlkhpaak
      961 gtvekqensp ghgkssehrg rvssllqkpe fpdgeimevl i
//
LOCUS       NP_001387847             702 aa            linear   ROD 28-APR-2025
DEFINITION  putative methyltransferase NSUN7 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001387847 XP_006251010
VERSION     NP_001387847.1
DBSOURCE    REFSEQ: accession NM_001400918.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Harris,T., Marquez,B., Suarez,S. and Schimenti,J.
  TITLE     Sperm motility defects and infertility in male mice with a mutation
            in Nsun7, a member of the Sun domain-containing family of putative
            RNA methyltransferases
  JOURNAL   Biol Reprod 77 (2), 376-382 (2007)
   PUBMED   17442852
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jan 28, 2022 this sequence version replaced XP_006251010.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.235887.1,
                                           SRR26643293.56898.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..702
                     /product="putative methyltransferase NSUN7 isoform 3"
                     /note="Williams-Beuren syndrome critical region protein
                     20; NOL1/NOP2/Sun domain family, member 7; putative
                     methyltransferase NSUN7"
                     /calculated_mol_wt=78922
     CDS             1..702
                     /gene="Nsun7"
                     /gene_synonym="RGD1310137"
                     /coded_by="NM_001400918.1:525..2633"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:305339"
                     /db_xref="RGD:1310137"
ORIGIN      
        1 mldpnsamdf fdqenmeels qlaslemsgd lvskrkpsaa lekssypdsv yvtaanifqg
       61 iriqrpadkv iinygdellp sswtqaeeds fqrlsyelaf stlkyqdile silidtdifs
      121 sttipdqlns liivmlydfq drkfqprvlp ndavtipevq evenllnsfk tklaaalarc
      181 rikhdalsiy hilpetvrkq eqrastlply awinigkvsl eevyddlrkk gfdkvksiay
      241 lndkvfavdq hcfnvlifps hfkrellnid likdyklifq dksrslavhs vkalinmddd
      301 ilmvntgswy tvahmsilts gntskifvcg ieseekdsda kklftkmgce nieilhetfl
      361 siepkdqrlq nvkvilllpr csslgvsnpv efilnehedt sllqdlsqgg lpkdklqifa
      421 qqqfeqltha mkfakaqaiv yctcsvseee neevvkkale fqspalklqp yrlsppvlpl
      481 cslkeielsm drffrlepsd itngcflsil trerdpsetv svkdvlaraa akglldgvev
      541 gktlkrdkkr kkakaplpka ppqadlahdh ssvtgadnsi qmkiteflhr eskasavktp
      601 lpakpvpqva assqirkpsk plstplvrtt rpsekagsfg rprpegkgip lkpveiilpp
      661 vtfpfsspqg prfqmpgthf yyrfigskds sredrinnfl ik
//
LOCUS       NP_001402778             627 aa            linear   ROD 28-APR-2025
DEFINITION  myotonin-protein kinase isoform 4 [Rattus norvegicus].
ACCESSION   NP_001402778 XP_008757268
VERSION     NP_001402778.1
DBSOURCE    REFSEQ: accession NM_001415849.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Damanafshan,A., Elzenaar,I., Samson-Couterie,B., van der Made,I.,
            Bourajjaj,M., van den Hoogenhof,M.M., van Veen,H.A., Picavet,D.I.,
            Beqqali,A., Ehler,E., De Windt,L.J., Pinto,Y.M. and van Oort,R.J.
  TITLE     The MEF2 transcriptional target DMPK induces loss of sarcomere
            structure and cardiomyopathy
  JOURNAL   Cardiovasc Res 114 (11), 1474-1486 (2018)
   PUBMED   29648621
  REMARK    GeneRIF: MEF2-induced loss of sarcomeres is mediated by DMPK via a
            decrease in sarcomeric gene expression by interfering with SRF
            transcriptional activity, leading to adverse cardiomyocyte
            remodelling and heart failure.
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Harmon,E.B., Harmon,M.L., Larsen,T.D., Yang,J., Glasford,J.W. and
            Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase is critical for nuclear envelope
            integrity
  JOURNAL   J Biol Chem 286 (46), 40296-40306 (2011)
   PUBMED   21949239
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Forner,F., Furlan,S. and Salvatori,S.
  TITLE     Mass spectrometry analysis of complexes formed by myotonic
            dystrophy protein kinase (DMPK)
  JOURNAL   Biochim Biophys Acta 1804 (6), 1334-1341 (2010)
   PUBMED   20188867
  REMARK    GeneRIF: DMPK peptides were identified by high-resolution mass
            spectrometry together with several putative DMPK-binding proteins,
            including several heat shock proteins such as HSP20/HSPB6,
            HSP60/CPN60, HSP70 and HSP90.
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Harmon,E.B., Harmon,M.L., Larsen,T.D., Paulson,A.F. and
            Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase is expressed in embryonic
            myocytes and is required for myotube formation
  JOURNAL   Dev Dyn 237 (9), 2353-2366 (2008)
   PUBMED   18729234
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Andrade,A., de Leon,M.B., Hernandez-Hernandez,O., Cisneros,B. and
            Felix,R.
  TITLE     Myotonic dystrophy CTG repeat expansion alters Ca2+ channel
            functional expression in PC12 cells
  JOURNAL   FEBS Lett 581 (23), 4430-4438 (2007)
   PUBMED   17719582
  REMARK    GeneRIF: Data suggest modifications in the processing of N-type
            Ca(2+) channels in PC12 cells expressing the DM1 mutation.
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Mistry,D.J., Moorman,J.R., Reddy,S. and Mounsey,J.P.
  TITLE     Skeletal muscle Na currents in mice heterozygous for Six5
            deficiency
  JOURNAL   Physiol Genomics 6 (3), 153-158 (2001)
   PUBMED   11526199
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Muranyi,A., Zhang,R., Liu,F., Hirano,K., Ito,M., Epstein,H.F. and
            Hartshorne,D.J.
  TITLE     Myotonic dystrophy protein kinase phosphorylates the myosin
            phosphatase targeting subunit and inhibits myosin phosphatase
            activity
  JOURNAL   FEBS Lett 493 (2-3), 80-84 (2001)
   PUBMED   11287000
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Bush,E.W., Helmke,S.M., Birnbaum,R.A. and Perryman,M.B.
  TITLE     Myotonic dystrophy protein kinase domains mediate localization,
            oligomerization, novel catalytic activity, and autoinhibition
  JOURNAL   Biochemistry 39 (29), 8480-8490 (2000)
   PUBMED   10913253
REFERENCE   9  (residues 1 to 627)
  AUTHORS   Benders,A.A., Groenen,P.J., Oerlemans,F.T., Veerkamp,J.H. and
            Wieringa,B.
  TITLE     Myotonic dystrophy protein kinase is involved in the modulation of
            the Ca2+ homeostasis in skeletal muscle cells
  JOURNAL   J Clin Invest 100 (6), 1440-1447 (1997)
   PUBMED   9294109
REFERENCE   10 (residues 1 to 627)
  AUTHORS   Boucher,C.A., King,S.K., Carey,N., Krahe,R., Winchester,C.L.,
            Rahman,S., Creavin,T., Meghji,P., Bailey,M.E., Chartier,F.L. et al.
  TITLE     A novel homeodomain-encoding gene is associated with a large CpG
            island interrupted by the myotonic dystrophy unstable (CTG)n repeat
  JOURNAL   Hum Mol Genet 4 (10), 1919-1925 (1995)
   PUBMED   8595416
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 4, 2023 this sequence version replaced XP_008757268.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.2765389.1,
                                           SRR21887623.2765398.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..627
                     /product="myotonin-protein kinase isoform 4"
                     /EC_number="2.7.11.1"
                     /note="dystrophia myotonica kinase, B15; dystrophia
                     myotonica-protein kinase; myotonin-protein kinase"
                     /calculated_mol_wt=69737
     Region          69..401
                     /region_name="STKc_DMPK_like"
                     /note="Catalytic domain of Myotonic Dystrophy protein
                     kinase (DMPK)-like Serine/Threonine Kinases; cd05597"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,148..149,151,155,157,195,197,
                     199..200,202,212..213,216,231..236,270,276,279)
                     /site_type="active"
                     /db_xref="CDD:270748"
     Site            order(77..81,85,98,100,132,149..151,155,195,197,199..200,
                     202,212..213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270748"
     Site            order(81,155,157,195,197,199,216,231..236,270,276,279)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270748"
     Site            order(212..222,225..236)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270748"
     Site            395..400
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270748"
     Region          467..527
                     /region_name="DMPK_coil"
                     /note="DMPK coiled coil domain like; pfam08826"
                     /db_xref="CDD:117396"
     CDS             1..627
                     /gene="Dmpk"
                     /gene_synonym="Dm15"
                     /coded_by="NM_001415849.1:138..2021"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:308405"
                     /db_xref="RGD:1309825"
ORIGIN      
        1 msaevrlrql qqlvldpgfl gleplldlll gvhqelgash laqdkyvadf lqwvepiaar
       61 lkevrlqrdd feilkvigrg afsevavvkm kqtgqvyamk imnkwdmlkr gevscfreer
      121 dvlvkgdrrw itqlhfafqd enylylvmey yvggdlltll skfgeripae marfylaeiv
      181 maidsvhrlg yvhrdikpdn illdrcghir ladfgsclkl qpdgtvrslv avgtpdylsp
      241 eilqavgggp gagsygpecd wwalgvfaye mfygqtpfya dstaetyaki vhyrehlslp
      301 radmgvpeea qdlirgllcp aeirlgrgga gdfqkhpfff gldweglrds vppftpdfeg
      361 atdtcnfdvv edrltametl sdmqedmalg vhlpfvgysy scmasrdnqv tdptpmelea
      421 lqlpvsdlqg ldlpppvspp dqaaeeadpa avpvppaete tmvtlrelqe aleeevltrq
      481 slsreleair tanqnfssql qeaevrnrdl eahvrqlqer memlqapgaa avtgvpspra
      541 tdppshmapr pwlwasarww gqapctavtc cslpgslgla yprriacscs pllwllpphw
      601 aalgwwpipa vspqsgvsre ppsppep
//
LOCUS       NP_001386460             416 aa            linear   ROD 28-APR-2025
DEFINITION  nucleolar and spindle-associated protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001386460 XP_006234830
VERSION     NP_001386460.1
DBSOURCE    REFSEQ: accession NM_001399531.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Raemaekers,T., Ribbeck,K., Beaudouin,J., Annaert,W., Van Camp,M.,
            Stockmans,I., Smets,N., Bouillon,R., Ellenberg,J. and Carmeliet,G.
  TITLE     NuSAP, a novel microtubule-associated protein involved in mitotic
            spindle organization
  JOURNAL   J Cell Biol 162 (6), 1017-1029 (2003)
   PUBMED   12963707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 10, 2022 this sequence version replaced XP_006234830.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161947.1, SRR26643285.12788.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..416
                     /product="nucleolar and spindle-associated protein 1
                     isoform 1"
                     /calculated_mol_wt=47282
     Region          157..410
                     /region_name="NUSAP"
                     /note="Nucleolar and spindle-associated protein;
                     pfam16006"
                     /db_xref="CDD:464970"
     CDS             1..416
                     /gene="Nusap1"
                     /coded_by="NM_001399531.1:75..1325"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:311336"
                     /db_xref="RGD:1305764"
ORIGIN      
        1 mtvpsaeeld sfkysdlqnl akrlglranl radkllralk ahlnpetrre nknqdenqss
       61 afsydetetq vtseeqaete sgshvtrtrr rkrktihgip tsqdhmemkr rdsttfqnqe
      121 nqdlratekv pslpeqrped gnaasseegk indkkgplek rslctdgfsk lgnskrisat
      181 tpnfkrlhea hfkkmeside ymvrkkkhfk ehdslnelkq ldkkvtpvpp rgrlsvlctp
      241 arqrcsqghs atkmnvrfsa atkdnehkcs ltktparksp hvtapgsask gqavlktpkl
      301 ktternstav itpfklmtea tqtpgsskkp ifdlkaslsr plnykphkgk lkpwgqaken
      361 nslnecvsrv tlhrktykqp plqtreeqrk rhvqerkerk ekllearrnl gvtkaq
//
LOCUS       NP_001424797            2000 aa            linear   ROD 28-APR-2025
DEFINITION  myosin-14 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424797 XP_006229118
VERSION     NP_001424797.1
DBSOURCE    REFSEQ: accession NM_001437868.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2000)
  AUTHORS   Billington,N., Wang,A., Mao,J., Adelstein,R.S. and Sellers,J.R.
  TITLE     Characterization of three full-length human nonmuscle myosin II
            paralogs
  JOURNAL   J Biol Chem 288 (46), 33398-33410 (2013)
   PUBMED   24072716
REFERENCE   2  (residues 1 to 2000)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   3  (residues 1 to 2000)
  AUTHORS   Choi,B.O., Kang,S.H., Hyun,Y.S., Kanwal,S., Park,S.W., Koo,H.,
            Kim,S.B., Choi,Y.C., Yoo,J.H., Kim,J.W., Park,K.D., Choi,K.G.,
            Kim,S.J., Zuchner,S. and Chung,K.W.
  TITLE     A complex phenotype of peripheral neuropathy, myopathy, hoarseness,
            and hearing loss is linked to an autosomal dominant mutation in
            MYH14
  JOURNAL   Hum Mutat 32 (6), 669-677 (2011)
   PUBMED   21480433
REFERENCE   4  (residues 1 to 2000)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 2000)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 2000)
  AUTHORS   Kim,K.Y., Kovacs,M., Kawamoto,S., Sellers,J.R. and Adelstein,R.S.
  TITLE     Disease-associated mutations and alternative splicing alter the
            enzymatic and motile activity of nonmuscle myosins II-B and II-C
  JOURNAL   J Biol Chem 280 (24), 22769-22775 (2005)
   PUBMED   15845534
REFERENCE   7  (residues 1 to 2000)
  AUTHORS   Turney,S.G. and Bridgman,P.C.
  TITLE     Laminin stimulates and guides axonal outgrowth via growth cone
            myosin II activity
  JOURNAL   Nat Neurosci 8 (6), 717-719 (2005)
   PUBMED   15880105
REFERENCE   8  (residues 1 to 2000)
  AUTHORS   Bao,J., Jana,S.S. and Adelstein,R.S.
  TITLE     Vertebrate nonmuscle myosin II isoforms rescue small interfering
            RNA-induced defects in COS-7 cell cytokinesis
  JOURNAL   J Biol Chem 280 (20), 19594-19599 (2005)
   PUBMED   15774463
  REMARK    Erratum:[J Biol Chem. 2006 Apr 14;281(15):10652]
REFERENCE   9  (residues 1 to 2000)
  AUTHORS   Donaudy,F., Snoeckx,R., Pfister,M., Zenner,H.P., Blin,N., Di
            Stazio,M., Ferrara,A., Lanzara,C., Ficarella,R., Declau,F.,
            Pusch,C.M., Nurnberg,P., Melchionda,S., Zelante,L., Ballana,E.,
            Estivill,X., Van Camp,G., Gasparini,P. and Savoia,A.
  TITLE     Nonmuscle myosin heavy-chain gene MYH14 is expressed in cochlea and
            mutated in patients affected by autosomal dominant hearing
            impairment (DFNA4)
  JOURNAL   Am J Hum Genet 74 (4), 770-776 (2004)
   PUBMED   15015131
REFERENCE   10 (residues 1 to 2000)
  AUTHORS   Golomb,E., Ma,X., Jana,S.S., Preston,Y.A., Kawamoto,S.,
            Shoham,N.G., Goldin,E., Conti,M.A., Sellers,J.R. and Adelstein,R.S.
  TITLE     Identification and characterization of nonmuscle myosin II-C, a new
            member of the myosin II family
  JOURNAL   J Biol Chem 279 (4), 2800-2808 (2004)
   PUBMED   14594953
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006229118.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.2271.1,
                                           SRR26643288.2234.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2000
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..2000
                     /product="myosin-14 isoform 1"
                     /EC_number="5.6.1.8"
                     /note="myosin, heavy polypeptide 14; myosin-14; myosin,
                     heavy chain 14, non-muscle"
                     /calculated_mol_wt=228784
     Region          115..792
                     /region_name="MYSc_Myh14_mammals"
                     /note="class II myosin heavy chain 14 motor domain;
                     cd14930"
                     /db_xref="CDD:276893"
     Site            order(142..150,194..201,255..265,482..487)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276893"
     Site            142..150
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276893"
     Site            194..201
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276893"
     Site            255..265
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276893"
     Site            482..487
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276893"
     Site            order(511..522,525..534)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276893"
     Site            724..733
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276893"
     Site            order(736..752,777..792)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276893"
     Region          869..1949
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     CDS             1..2000
                     /gene="Myh14"
                     /coded_by="NM_001437868.1:236..6238"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="GeneID:308572"
                     /db_xref="RGD:1306821"
ORIGIN      
        1 matvtlsvpg rkvasrpgpv peaaqpflfa prtpnvggpg gpqvewtarr mvwvpselhg
       61 feaaalrdeg eeeaevelae sgrrlrlprd qiqrmnppkf skaedmaelt clneasvlhn
      121 lreryysgli ytysglfcvv inpykqlpiy teaivemyrg kkrhevpphi yavtegayrs
      181 mlqdredqsi lctgesgagk tentkkviqy lahvasspkg rkepgvpasv stmsygeler
      241 qllqanpile afgnaktvkn dnssrfgkfi rinfdiagyi vganietyll eksrairqak
      301 decsfhifyq llggageqlk adlllepysh yrfltngpss spgqerelfq etleslrvlg
      361 llpeeitaml rtvsavlqfg nivlkkernt dqatmpdnta aqklcrllgl gvtdfsrall
      421 tprikvgrdy vqkaqtkeqa dfalealaka tyerlfrwlv lrlnraldrs prqgasflgi
      481 ldiagfeifq lnsfeqlcin ytneklqqlf nhtmfvleqe eyqregipwt fldfgldlqp
      541 cidlierpan ppgllallde ecwfpkatdk sfvekvaqeq gshpkfqrpr nlrdqadfsv
      601 lhyagkvdyk anewlmknmd plndnvaall hqstdrltae iwkdvegivg leqvsslgdg
      661 ppggrprrgm frtvgqlyke slsrlmatls ntnpsfvrci vpnhekragk leprlvldql
      721 rcngvlegir icrqgfpnri lfqefrqrye iltpnaipkg fmdgkqacek miqaleldpn
      781 lyrvgqskif fragvlaqle eerdlkvtdi ivsfqaaarg ylarrafqrr qqqqsalrvm
      841 qrncaaylkl rnwqwwrlfi kvkpllqvtr qdevlqaraq elqkvqelqq qsarevgelq
      901 grvaqleeer arlaeqlrae aelcseaeet rarlaarkqe lelvvtelea rvgeeeecsr
      961 qlqsekkrlq qhiqelethl eaeegarqkl qlekvtteak mkkfeedlll ledqnsklsk
     1021 errlleerla efssqaaeee ekvkslnklr vkyeatiadm edrlkkeekg rqeleklkrr
     1081 ldgesselqe qmmeqkqrae elliqlgrke eelqsalvra eeeggaraql lkslreaqag
     1141 laeaqedlea ervarakaek qrrdlgeele alrgeledtl dstnaqqelr skreqevtel
     1201 kktleeeart hevamqelrq rhsqalvelt eqleqarrgk svwektrlsl eaevselkte
     1261 lsslqtsrqe geqkrrrles qlqevqgrss dseraraeaa eklqraqvel esvstalsea
     1321 eskairlske lssaesqlhd tqellqeetr aklalgsrvr aleaeaaglr eqmeeevvar
     1381 eragrelqtt qaqlsewrrr qeeeaavlea geearrraar eaetlaqrla ekteaverle
     1441 rarrrlqqel ddatvdlgqq kqllstlekk qrkfdqllae ekaavlrave drerveaegr
     1501 erearalslt raleeeqear eelerqnral raeleallss kddvgknvhe lerarrvaeq
     1561 aasdlrtqvt eledeltaae daklrlevtv qalkaqherd lqgrddagee rrrqlakqlr
     1621 daeverdeer kqralamaar kkleleleel kaqtsaagqg keeavkqlkk mqaqmkelwr
     1681 eveetrssre emftlsrese krlkgleaev lrlqeelaas drarrqaqqd rdemaeevas
     1741 gnlskaatle ekrqlegrlg qleeeleeeq nnsellkdhy rklvlqvetl ttelsaersf
     1801 sakaesgrqq lerqiqelra rlgeedagar arqkmliaal esklaqaeeq leqesreril
     1861 sgklvrraek rlkevvlqvd eerrvadqlr dqleksnlrl kqlkrqleea eeeasraqag
     1921 rrrlqreled vtesaesmnr evttlrnrlr rgpltfttrt vrqvfrleeg vasdeeeaeg
     1981 aepgsaptqe peapppaapq
//
LOCUS       NP_001102189             843 aa            linear   ROD 28-APR-2025
DEFINITION  tetratricopeptide repeat protein 7B isoform 3 [Rattus norvegicus].
ACCESSION   NP_001102189 XP_001064941 XP_038968457 XP_343095
VERSION     NP_001102189.2
DBSOURCE    REFSEQ: accession NM_001108719.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Baskin,J.M., Wu,X., Christiano,R., Oh,M.S., Schauder,C.M.,
            Gazzerro,E., Messa,M., Baldassari,S., Assereto,S., Biancheri,R.,
            Zara,F., Minetti,C., Raimondi,A., Simons,M., Walther,T.C.,
            Reinisch,K.M. and De Camilli,P.
  TITLE     The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P
            synthesis at the plasma membrane
  JOURNAL   Nat Cell Biol 18 (1), 132-138 (2016)
   PUBMED   26571211
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Nakatsu,F., Baskin,J.M., Chung,J., Tanner,L.B., Shui,G., Lee,S.Y.,
            Pirruccello,M., Hao,M., Ingolia,N.T., Wenk,M.R. and De Camilli,P.
  TITLE     PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its
            impact on plasma membrane identity
  JOURNAL   J Cell Biol 199 (6), 1003-1016 (2012)
   PUBMED   23229899
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Feb 9, 2022 this sequence version replaced
            XP_038968457.1, NP_001102189.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2069507.1,
                                           SRR22582416.651441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..843
                     /product="tetratricopeptide repeat protein 7B isoform 3"
                     /note="tetratricopeptide repeat protein 7B"
                     /calculated_mol_wt=94053
     Region          1..386
                     /region_name="TTC7_N"
                     /note="Tetratricopeptide repeat protein 7 N-terminal;
                     pfam19440"
                     /db_xref="CDD:466084"
     Region          365..391
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          371..611
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          431..459
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
     Region          549..577
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          695..>828
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          696..724
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          730..758
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(731,734..735,738..739,741,765,768..769,772..773,
                     775..776,799,802..803,806..807,810)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          763..793
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          798..826
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..843
                     /gene="Ttc7b"
                     /coded_by="NM_001108719.3:147..2678"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:362768"
                     /db_xref="RGD:1305920"
ORIGIN      
        1 matrkagsrl eteiercrse cqweripelv kqlsaklian ddmaelllge skleqhlkek
       61 plrqgasprg prpqltevrk hltaaldrgn lkseflqesn lvmaklnyve gdykealniy
      121 arvglddlpl mavppyrlrm iaeayatkgl cleklpvsss tsnlhvdreq dvitcyekag
      181 diallylqei erviltniqn rspkpgpaph dqelgfflet glqrahvlyf kngnltrgvg
      241 rfrellrave trttqnlrmt iarqlaeill rgmceqsywn pleeppcqsp lddplrkgan
      301 tktytlprra rvysgenifc pqenteeall lllisesman rdavlsripe hksdrlislq
      361 sasvvydllt ialgrrgqye mlsecleram kfafeefhlw yqfalslmaa gksaravkvl
      421 kecirlkpdd atipllaakl cvgslhwlee aekfaktvvd vgektsefka kgylalglty
      481 slqatdaslr gmqevlqrka llalqrahsl sptdhqaafy lalqlaisrq ipealgyvrq
      541 alqlqgddan slhllallls aqkhhhdaln iidmalseyp enfillfskv kleslcrgpd
      601 ealltckhml qiwkscynlt npsdsgrgss lldrtiadrr qlntitlpdf sdpetgsvha
      661 tsvaasrveq alsevasslq ssapkqgplh pwmtlaqiwl haaevyigig kpaeatactq
      721 eaanlfpmsh nvlymrgqva elrgnfdear rwyeealsis pthvksmqrl alvlhqlgry
      781 slaekilrda vqvnstahev wnglgevlqa qgndaaatec fltaleleas spavpftvip
      841 rvl
//
LOCUS       NP_001416380             772 aa            linear   ROD 28-APR-2025
DEFINITION  junctional cadherin complex regulator isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001416380 XP_038938254
VERSION     NP_001416380.1
DBSOURCE    REFSEQ: accession NM_001429451.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Appelbe,O.K., Bollman,B., Attarwala,A., Triebes,L.A.,
            Muniz-Talavera,H., Curry,D.J. and Schmidt,J.V.
  TITLE     Disruption of the mouse Jhy gene causes abnormal ciliary
            microtubule patterning and juvenile hydrocephalus
  JOURNAL   Dev Biol 382 (1), 172-185 (2013)
   PUBMED   23906841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038938254.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.2448806.1,
                                           SRR26360186.779038.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..772
                     /product="junctional cadherin complex regulator isoform 2"
                     /note="juvenile hydrocephalus; uncharacterized protein
                     C11orf63 homolog; jhy protein homolog"
                     /calculated_mol_wt=87904
     Region          650..769
                     /region_name="JHY"
                     /note="Jhy protein; pfam15261"
                     /db_xref="CDD:464601"
     CDS             1..772
                     /gene="Jhy"
                     /gene_synonym="RGD1309108"
                     /coded_by="NM_001429451.1:1216..3534"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:315578"
                     /db_xref="RGD:1309108"
ORIGIN      
        1 mnkykpvpkr ssrspvhhtn lrtppsgraf keedfnlisk dslesdsesl preakfwsdi
       61 kdqiqdkdme pdsleedsss eteeaahgtn reglgaqgag anhshhqved kysdlrydpn
      121 wknkkeegql lavealpesa dsssdnlpga plypsrepsm rlsvgkgkek rspqseasll
      181 gseflspkye cgtrqneffs elsdsdqedq eekssdlspy lksssshnev flpgsrgprr
      241 rksrqyfvek nkltlglpap ktdsylqlhn kkrgetrleq isypirdagk mtvqddkgve
      301 ntfmdpedkw hqrakqlkny qehlsqcedt ksgnvprgqs snaanvqqps rrtakarvqk
      361 qkkyqnglks lgtkeqvvsq nnqnnslqqp qtqrlpmdts skhepaaqmt asnpnlqdpr
      421 tlthnpkvts dpffppketf drvvyknsvl glntnkrrgh rykeekrily qqqpiyifsd
      481 gdlqdfnels hrheslsqrg pqsdyrmnth rsrstktkkp skepeaetky kniemlwklh
      541 sssdmepvsa spdsrlaqim eqhqqallql aevqpsegsl sstvfppils rvesesqlds
      601 ershkhqmrm arsnsegyll qlekgkrhrk rsqsrtkssk lkgyqkrdvk lgglgpdfas
      661 irdkmqtllq qkeyakqvke ynmktlsvls kpqtsktdsk stisrkkald yaktipkpkp
      721 pnlpyqtmkk tnnskhseke gslpeislle ilqsrherek qavaafkvlh iv
//
LOCUS       NP_001424826             949 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Rattus norvegicus].
ACCESSION   NP_001424826 XP_038934784
VERSION     NP_001424826.1
DBSOURCE    REFSEQ: accession NM_001437897.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934784.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.41661.1,
                                           SRR26643292.31375.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..949
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=103214
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          645..>940
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..949
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437897.1:643..3492"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlvsth
      541 hlhssseded iegtfpnels lqqafseyqi qqmtanfvdq fgfndeefad qddninapfd
      601 riaeinfnie adedspsaal feaccsdriq pfdddeediw edeetrctar vmararfgap
      661 htsenyskka vghggqgrkt gsptarnvpg latpssptqk egprsesdsa gttwtavfde
      721 pvnplsaasg aardvgssaw aagpsvaeek gwakftdfqp fccsetgprc sspvdmdhsn
      781 aeggqspgpe kafgptspca wnvcvtrkap lvasdssssg gsdseddeka agavealcag
      841 htgkaspppr taeaaagrae cpdstvlapa cpapsevtis pavatiapsk agsptativv
      901 sssvatavpp gpimavttta paivatlgtm tkdrktdalp dgaalngpv
//
LOCUS       NP_001233594             344 aa            linear   ROD 28-APR-2025
DEFINITION  N-lysine methyltransferase KMT5A isoform 1 [Rattus norvegicus].
ACCESSION   NP_001233594 XP_001072149 XP_002724864 XP_038945700
VERSION     NP_001233594.2
DBSOURCE    REFSEQ: accession NM_001246665.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Li,Y., Cheng,M., Jin,J., Zhang,D., Zhang,S., Bai,Y. and Xu,J.
  TITLE     Interaction of Sp1 and Setd8 promotes vascular smooth muscle cells
            apoptosis by activating Mark4 in vascular calcification
  JOURNAL   Aging (Albany NY) 16 (3), 2438-2456 (2024)
   PUBMED   38301049
  REMARK    GeneRIF: Interaction of Sp1 and Setd8 promotes vascular smooth
            muscle cells apoptosis by activating Mark4 in vascular
            calcification.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Li,J., Song,H., Chen,T., Zhang,S., Zhang,C., Ma,C., Zhang,L.,
            Wang,T., Qian,Y. and Deng,X.
  TITLE     Lysine Methyltransferase 5A Promotes the Progression of Growth
            Hormone Pituitary Neuroendocrine Tumors through the
            Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Neuroendocrinology 114 (6), 589-601 (2024)
   PUBMED   38565081
  REMARK    GeneRIF: Lysine Methyltransferase 5A Promotes the Progression of
            Growth Hormone Pituitary Neuroendocrine Tumors through the
            Wnt/beta-Catenin Signaling Pathway.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Li,X., Qian,Y., Shen,W., Zhang,S., Han,H., Zhang,Y., Liu,S., Lv,S.
            and Zhang,X.
  TITLE     Mechanism of SET8 Activates the Nrf2-KEAP1-ARE Signaling Pathway to
            Promote the Recovery of Motor Function after Spinal Cord Injury
  JOURNAL   Mediators Inflamm 2023, 4420592 (2023)
   PUBMED   36936537
  REMARK    GeneRIF: Mechanism of SET8 Activates the Nrf2-KEAP1-ARE Signaling
            Pathway to Promote the Recovery of Motor Function after Spinal Cord
            Injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Barrett,E., Loverin,A., Wang,H., Carlson,M., Larsen,T.D.,
            Almeida,M.M., Whitman,J., Baack,M.L. and Joss-Moore,L.A.
  TITLE     Uteroplacental Insufficiency with Hypoxia Upregulates Placental
            PPARgamma-KMT5A Axis in the Rat
  JOURNAL   Reprod Sci 28 (5), 1476-1488 (2021)
   PUBMED   33398850
  REMARK    GeneRIF: Uteroplacental Insufficiency with Hypoxia Upregulates
            Placental PPARgamma-KMT5A Axis in the Rat.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Pan,C., Chen,H., Wang,L., Yang,S., Fu,H., Zheng,Y., Miao,M. and
            Jiao,B.
  TITLE     Down-regulation of MiR-127 facilitates hepatocyte proliferation
            during rat liver regeneration
  JOURNAL   PLoS One 7 (6), e39151 (2012)
   PUBMED   22720056
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Kalakonda,N., Fischle,W., Boccuni,P., Gurvich,N., Hoya-Arias,R.,
            Zhao,X., Miyata,Y., Macgrogan,D., Zhang,J., Sims,J.K., Rice,J.C.
            and Nimer,S.D.
  TITLE     Histone H4 lysine 20 monomethylation promotes transcriptional
            repression by L3MBTL1
  JOURNAL   Oncogene 27 (31), 4293-4304 (2008)
   PUBMED   18408754
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Sims,J.K. and Rice,J.C.
  TITLE     PR-Set7 establishes a repressive trans-tail histone code that
            regulates differentiation
  JOURNAL   Mol Cell Biol 28 (14), 4459-4468 (2008)
   PUBMED   18474616
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Shi,X., Kachirskaia,I., Yamaguchi,H., West,L.E., Wen,H., Wang,E.W.,
            Dutta,S., Appella,E. and Gozani,O.
  TITLE     Modulation of p53 function by SET8-mediated methylation at lysine
            382
  JOURNAL   Mol Cell 27 (4), 636-646 (2007)
   PUBMED   17707234
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Ahmed,F., Torrado,M., Zinovieva,R.D., Senatorov,V.V., Wistow,G. and
            Tomarev,S.I.
  TITLE     Gene expression profile of the rat eye iridocorneal angle: NEIBank
            expressed sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 45 (9), 3081-3090 (2004)
   PUBMED   15326124
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On or before Nov 4, 2022 this sequence version replaced
            XP_038945700.1, NP_001233594.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.3696011.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760433,
                                           SAMEA5760494 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..344
                     /product="N-lysine methyltransferase KMT5A isoform 1"
                     /EC_number="2.1.1.354"
                     /note="SET domain-containing 8; histone-lysine
                     N-methyltransferase SETD8; histone methyltransferase
                     Pr-set7/Set8; N-lysine methyltransferase SETD8; SET domain
                     containing (lysine methyltransferase) 8; lysine
                     (K)-specific methyltransferase 5A; N-lysine
                     methyltransferase KMT5A"
                     /calculated_mol_wt=38150
     Region          192..331
                     /region_name="SET_SETD8"
                     /note="SET domain found in SET domain-containing protein 8
                     (SETD8) and similar proteins; cd10528"
                     /db_xref="CDD:380926"
     Site            order(219..221,237,262..266,287..291,328)
                     /site_type="active"
                     /db_xref="CDD:380926"
     Site            order(219..221,262..263,287..291,328)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380926"
     Site            order(237,251,254..255,261..262,264..267,299,310,326,
                     328..331)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380926"
     CDS             1..344
                     /gene="Kmt5a"
                     /gene_synonym="Pr-set7; RGD1305893; Setd8"
                     /coded_by="NM_001246665.2:242..1276"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:689820"
                     /db_xref="RGD:1587560"
ORIGIN      
        1 mckpraveaa aaavaatapg pemverrgpg rprsdgenvf agqskiyaym spnkcsgmrs
       61 plqeensvah hevkcpgkpl agiyrkreek rnagnvirsa vkseeqkskd trrgplapfp
      121 nqkpeatepp ktpppscdst svavakqalk kplkgkqapr kksqgktqqn rkltdfypvr
      181 rssrkskael qseerkkide liesgkeegm kidlidgkgr gviatkrfsr gdfvveyhgd
      241 lieitdakkr ealyaqdpst gcymyyfqyl sktycvdatq etnrlgrlin hskcgncqtk
      301 lhdidgvphl iliasrdiaa geellydygd rskasieayp wlkh
//
LOCUS       NP_001424798            1992 aa            linear   ROD 28-APR-2025
DEFINITION  myosin-14 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001424798 XP_006229119
VERSION     NP_001424798.1
DBSOURCE    REFSEQ: accession NM_001437869.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1992)
  AUTHORS   Billington,N., Wang,A., Mao,J., Adelstein,R.S. and Sellers,J.R.
  TITLE     Characterization of three full-length human nonmuscle myosin II
            paralogs
  JOURNAL   J Biol Chem 288 (46), 33398-33410 (2013)
   PUBMED   24072716
REFERENCE   2  (residues 1 to 1992)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   3  (residues 1 to 1992)
  AUTHORS   Choi,B.O., Kang,S.H., Hyun,Y.S., Kanwal,S., Park,S.W., Koo,H.,
            Kim,S.B., Choi,Y.C., Yoo,J.H., Kim,J.W., Park,K.D., Choi,K.G.,
            Kim,S.J., Zuchner,S. and Chung,K.W.
  TITLE     A complex phenotype of peripheral neuropathy, myopathy, hoarseness,
            and hearing loss is linked to an autosomal dominant mutation in
            MYH14
  JOURNAL   Hum Mutat 32 (6), 669-677 (2011)
   PUBMED   21480433
REFERENCE   4  (residues 1 to 1992)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 1992)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 1992)
  AUTHORS   Kim,K.Y., Kovacs,M., Kawamoto,S., Sellers,J.R. and Adelstein,R.S.
  TITLE     Disease-associated mutations and alternative splicing alter the
            enzymatic and motile activity of nonmuscle myosins II-B and II-C
  JOURNAL   J Biol Chem 280 (24), 22769-22775 (2005)
   PUBMED   15845534
REFERENCE   7  (residues 1 to 1992)
  AUTHORS   Turney,S.G. and Bridgman,P.C.
  TITLE     Laminin stimulates and guides axonal outgrowth via growth cone
            myosin II activity
  JOURNAL   Nat Neurosci 8 (6), 717-719 (2005)
   PUBMED   15880105
REFERENCE   8  (residues 1 to 1992)
  AUTHORS   Bao,J., Jana,S.S. and Adelstein,R.S.
  TITLE     Vertebrate nonmuscle myosin II isoforms rescue small interfering
            RNA-induced defects in COS-7 cell cytokinesis
  JOURNAL   J Biol Chem 280 (20), 19594-19599 (2005)
   PUBMED   15774463
  REMARK    Erratum:[J Biol Chem. 2006 Apr 14;281(15):10652]
REFERENCE   9  (residues 1 to 1992)
  AUTHORS   Donaudy,F., Snoeckx,R., Pfister,M., Zenner,H.P., Blin,N., Di
            Stazio,M., Ferrara,A., Lanzara,C., Ficarella,R., Declau,F.,
            Pusch,C.M., Nurnberg,P., Melchionda,S., Zelante,L., Ballana,E.,
            Estivill,X., Van Camp,G., Gasparini,P. and Savoia,A.
  TITLE     Nonmuscle myosin heavy-chain gene MYH14 is expressed in cochlea and
            mutated in patients affected by autosomal dominant hearing
            impairment (DFNA4)
  JOURNAL   Am J Hum Genet 74 (4), 770-776 (2004)
   PUBMED   15015131
REFERENCE   10 (residues 1 to 1992)
  AUTHORS   Golomb,E., Ma,X., Jana,S.S., Preston,Y.A., Kawamoto,S.,
            Shoham,N.G., Goldin,E., Conti,M.A., Sellers,J.R. and Adelstein,R.S.
  TITLE     Identification and characterization of nonmuscle myosin II-C, a new
            member of the myosin II family
  JOURNAL   J Biol Chem 279 (4), 2800-2808 (2004)
   PUBMED   14594953
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 10, 2025 this sequence version replaced XP_006229119.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.1556.1,
                                           SRR26643296.1372.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1992
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..1992
                     /product="myosin-14 isoform 2"
                     /EC_number="5.6.1.8"
                     /note="myosin, heavy polypeptide 14; myosin-14; myosin,
                     heavy chain 14, non-muscle"
                     /calculated_mol_wt=227957
     Region          115..784
                     /region_name="MYSc_Myh14_mammals"
                     /note="class II myosin heavy chain 14 motor domain;
                     cd14930"
                     /db_xref="CDD:276893"
     Site            order(142..150,194..201,247..257,474..479)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276893"
     Site            142..150
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276893"
     Site            194..201
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276893"
     Site            247..257
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276893"
     Site            474..479
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276893"
     Site            order(503..514,517..526)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276893"
     Site            716..725
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276893"
     Site            order(728..744,769..784)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276893"
     Region          861..1941
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     CDS             1..1992
                     /gene="Myh14"
                     /coded_by="NM_001437869.1:236..6214"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:308572"
                     /db_xref="RGD:1306821"
ORIGIN      
        1 matvtlsvpg rkvasrpgpv peaaqpflfa prtpnvggpg gpqvewtarr mvwvpselhg
       61 feaaalrdeg eeeaevelae sgrrlrlprd qiqrmnppkf skaedmaelt clneasvlhn
      121 lreryysgli ytysglfcvv inpykqlpiy teaivemyrg kkrhevpphi yavtegayrs
      181 mlqdredqsi lctgesgagk tentkkviqy lahvasspkg rkepgvpgel erqllqanpi
      241 leafgnaktv kndnssrfgk firinfdiag yivganiety lleksrairq akdecsfhif
      301 yqllggageq lkadlllepy shyrfltngp ssspgqerel fqetleslrv lgllpeeita
      361 mlrtvsavlq fgnivlkker ntdqatmpdn taaqklcrll glgvtdfsra lltprikvgr
      421 dyvqkaqtke qadfaleala katyerlfrw lvlrlnrald rsprqgasfl gildiagfei
      481 fqlnsfeqlc inytneklqq lfnhtmfvle qeeyqregip wtfldfgldl qpcidlierp
      541 anppgllall deecwfpkat dksfvekvaq eqgshpkfqr prnlrdqadf svlhyagkvd
      601 ykanewlmkn mdplndnvaa llhqstdrlt aeiwkdvegi vgleqvsslg dgppggrprr
      661 gmfrtvgqly keslsrlmat lsntnpsfvr civpnhekra gkleprlvld qlrcngvleg
      721 iricrqgfpn rilfqefrqr yeiltpnaip kgfmdgkqac ekmiqaleld pnlyrvgqsk
      781 iffragvlaq leeerdlkvt diivsfqaaa rgylarrafq rrqqqqsalr vmqrncaayl
      841 klrnwqwwrl fikvkpllqv trqdevlqar aqelqkvqel qqqsarevge lqgrvaqlee
      901 erarlaeqlr aeaelcseae etrarlaark qelelvvtel earvgeeeec srqlqsekkr
      961 lqqhiqelet hleaeegarq klqlekvtte akmkkfeedl llledqnskl skerrlleer
     1021 laefssqaae eeekvkslnk lrvkyeatia dmedrlkkee kgrqeleklk rrldgessel
     1081 qeqmmeqkqr aeelliqlgr keeelqsalv raeeeggara qllkslreaq aglaeaqedl
     1141 eaervaraka ekqrrdlgee lealrgeled tldstnaqqe lrskreqevt elkktleeea
     1201 rthevamqel rqrhsqalve lteqleqarr gksvwektrl sleaevselk telsslqtsr
     1261 qegeqkrrrl esqlqevqgr ssdserarae aaeklqraqv elesvstals eaeskairls
     1321 kelssaesql hdtqellqee traklalgsr vraleaeaag lreqmeeevv areragrelq
     1381 ttqaqlsewr rrqeeeaavl eageearrra areaetlaqr laekteaver lerarrrlqq
     1441 elddatvdlg qqkqllstle kkqrkfdqll aeekaavlra vedrerveae grerearals
     1501 ltraleeeqe areelerqnr alraeleall sskddvgknv helerarrva eqaasdlrtq
     1561 vteledelta aedaklrlev tvqalkaqhe rdlqgrddag eerrrqlakq lrdaeverde
     1621 erkqralama arkklelele elkaqtsaag qgkeeavkql kkmqaqmkel wreveetrss
     1681 reemftlsre sekrlkglea evlrlqeela asdrarrqaq qdrdemaeev asgnlskaat
     1741 leekrqlegr lgqleeelee eqnnsellkd hyrklvlqve tlttelsaer sfsakaesgr
     1801 qqlerqiqel rarlgeedag ararqkmlia alesklaqae eqleqesrer ilsgklvrra
     1861 ekrlkevvlq vdeerrvadq lrdqleksnl rlkqlkrqle eaeeeasraq agrrrlqrel
     1921 edvtesaesm nrevttlrnr lrrgpltftt rtvrqvfrle egvasdeeea egaepgsapt
     1981 qepeapppaa pq
//
LOCUS       NP_001402763             602 aa            linear   ROD 28-APR-2025
DEFINITION  grainyhead-like protein 3 homolog isoform 2 [Rattus norvegicus].
ACCESSION   NP_001402763 XP_006239211
VERSION     NP_001402763.1
DBSOURCE    REFSEQ: accession NM_001415834.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Gordon,W.M., Zeller,M.D., Klein,R.H., Swindell,W.R., Ho,H.,
            Espetia,F., Gudjonsson,J.E., Baldi,P.F. and Andersen,B.
  TITLE     A GRHL3-regulated repair pathway suppresses immune-mediated
            epidermal hyperplasia
  JOURNAL   J Clin Invest 124 (12), 5205-5218 (2014)
   PUBMED   25347468
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Haendeler,J., Mlynek,A., Buchner,N., Lukosz,M., Graf,M.,
            Guettler,C., Jakob,S., Farrokh,S., Kunze,K., Goy,C.,
            Guardiola-Serrano,F., Schaal,H., Cortese-Krott,M., Deenen,R.,
            Kohrer,K., Winkler,C. and Altschmied,J.
  TITLE     Two isoforms of Sister-Of-Mammalian Grainyhead have opposing
            functions in endothelial cells and in vivo
  JOURNAL   Arterioscler Thromb Vasc Biol 33 (7), 1639-1646 (2013)
   PUBMED   23685552
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Brouns,M.R., De Castro,S.C., Terwindt-Rouwenhorst,E.A., Massa,V.,
            Hekking,J.W., Hirst,C.S., Savery,D., Munts,C., Partridge,D.,
            Lamers,W., Kohler,E., van Straaten,H.W., Copp,A.J. and Greene,N.D.
  TITLE     Over-expression of Grhl2 causes spina bifida in the Axial defects
            mutant mouse
  JOURNAL   Hum Mol Genet 20 (8), 1536-1546 (2011)
   PUBMED   21262862
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Boglev,Y., Wilanowski,T., Caddy,J., Parekh,V., Auden,A., Darido,C.,
            Hislop,N.R., Cangkrama,M., Ting,S.B. and Jane,S.M.
  TITLE     The unique and cooperative roles of the Grainy head-like
            transcription factors in epidermal development reflect unexpected
            target gene specificity
  JOURNAL   Dev Biol 349 (2), 512-522 (2011)
   PUBMED   21081122
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Rifat,Y., Parekh,V., Wilanowski,T., Hislop,N.R., Auden,A.,
            Ting,S.B., Cunningham,J.M. and Jane,S.M.
  TITLE     Regional neural tube closure defined by the Grainy head-like
            transcription factors
  JOURNAL   Dev Biol 345 (2), 237-245 (2010)
   PUBMED   20654612
REFERENCE   6  (residues 1 to 602)
  AUTHORS   Yu,Z., Lin,K.K., Bhandari,A., Spencer,J.A., Xu,X., Wang,N., Lu,Z.,
            Gill,G.N., Roop,D.R., Wertz,P. and Andersen,B.
  TITLE     The Grainyhead-like epithelial transactivator Get-1/Grhl3 regulates
            epidermal terminal differentiation and interacts functionally with
            LMO4
  JOURNAL   Dev Biol 299 (1), 122-136 (2006)
   PUBMED   16949565
REFERENCE   7  (residues 1 to 602)
  AUTHORS   Ting,S.B., Caddy,J., Hislop,N., Wilanowski,T., Auden,A., Zhao,L.L.,
            Ellis,S., Kaur,P., Uchida,Y., Holleran,W.M., Elias,P.M.,
            Cunningham,J.M. and Jane,S.M.
  TITLE     A homolog of Drosophila grainy head is essential for epidermal
            integrity in mice
  JOURNAL   Science 308 (5720), 411-413 (2005)
   PUBMED   15831758
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Ting,S.B., Wilanowski,T., Auden,A., Hall,M., Voss,A.K., Thomas,T.,
            Parekh,V., Cunningham,J.M. and Jane,S.M.
  TITLE     Inositol- and folate-resistant neural tube defects in mice lacking
            the epithelial-specific factor Grhl-3
  JOURNAL   Nat Med 9 (12), 1513-1519 (2003)
   PUBMED   14608380
REFERENCE   9  (residues 1 to 602)
  AUTHORS   Kudryavtseva,E.I., Sugihara,T.M., Wang,N., Lasso,R.J.,
            Gudnason,J.F., Lipkin,S.M. and Andersen,B.
  TITLE     Identification and characterization of Grainyhead-like epithelial
            transactivator (GET-1), a novel mammalian Grainyhead-like factor
  JOURNAL   Dev Dyn 226 (4), 604-617 (2003)
   PUBMED   12666198
REFERENCE   10 (residues 1 to 602)
  AUTHORS   Hall,M., Gofflot,F., Iseki,S. and Morriss-Kay,G.M.
  TITLE     Effects of the curly tail genotype on neuroepithelial integrity and
            cell proliferation during late stages of primary neurulation
  JOURNAL   J Anat 199 (Pt 6), 645-655 (2001)
   PUBMED   11787818
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jan 3, 2023 this sequence version replaced XP_006239211.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.23182.1,
                                           SRR26643299.24903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16418971 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..602
                     /product="grainyhead-like protein 3 homolog isoform 2"
                     /note="transcription factor CP2-like 4; grainyhead-like
                     protein 3 homolog; grainyhead-like 3"
                     /calculated_mol_wt=67684
     Region          219..421
                     /region_name="CP2"
                     /note="CP2 transcription factor; pfam04516"
                     /db_xref="CDD:461338"
     CDS             1..602
                     /gene="Grhl3"
                     /gene_synonym="Tfcp2l4"
                     /coded_by="NM_001415834.1:208..2016"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298555"
                     /db_xref="RGD:1308320"
ORIGIN      
        1 msneldfrsv rllkndpvsf qkfpynnede awktylenpl taatkaimrv ngddesvaal
       61 sflydyymgp kekrilssst ggrndqgkky yhsmdyepdl aplespthlm kfltenvsgs
      121 pdytdqlkkn nllglegalp tpgktstlpp gpskleagsm dsyllptsdm ydnsslnslf
      181 esihgvpptq rwqpdstfkd dpqesllfpd ilktspeapc pedypslksd feytlgspka
      241 ihikagespm aylnkgqfyp vtlrtpaggk glslssskvk svvmivfdnd kvpveqlrfw
      301 rhwhsrqpta kqrvidvadc kenfntvqhi eevaynalsf vwnvneeakv figvnclstd
      361 fssqkgvkgv plnlqidtyd cgagterlvh ravcqikifc dkgaerkmrd derkqfrrkv
      421 kcpdssnngi kgcllsgfrg nettylrpea dletqpvlfi pnlhfsslqr pggvvpsagh
      481 sssdrlplkr tcspfaeefe plpskqaked dlqrvllyvr reteevfdal mlktpdlkgl
      541 rnaisekygf peenickvyk kckrgilvnm dnniiqhysn hvaflldmge ldgkiqiilk
      601 el
//
LOCUS       NP_001092937             849 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor 30 precursor [Rattus norvegicus].
ACCESSION   NP_001092937 XP_222983
VERSION     NP_001092937.1
DBSOURCE    REFSEQ: accession NM_001099467.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000001.1.
            
            On Jul 26, 2007 this sequence version replaced XP_222983.2.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..849
                     /product="vomeronasal 2 receptor 30 precursor"
                     /calculated_mol_wt=95540
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2184
     Region          41..500
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(70,167..168,391)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(108,111,151,241)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          509..562
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          582..833
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          582..607
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(585,588..589,592..593,595..596,630,634,637..638,646,
                     650)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          619..640
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(639,651..652,655..656,659,739,744,747..748,751,785,
                     788..789,792,796,804..805,808,811,815)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          649..673
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          697..713
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          740..766
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          774..797
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          802..827
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..849
                     /gene="Vom2r30"
                     /gene_synonym="RGD1561133"
                     /coded_by="NM_001099467.1:1..2550"
                     /db_xref="GeneID:289295"
                     /db_xref="RGD:1561133"
ORIGIN      
        1 mfilmvvfff lnlphlmanf tdprcfwrin ldedqnkdlg iscsfilgav qlpmekdyfn
       61 qtlnvlkttk tnkyalvlaf smneinrnpd llpnmslvik htlsycdgkt vhhivkekfy
      121 nplpnyicne etmcsflltg lnwissiklf reldvflfpr flqisygpfh sifsdneqfp
      181 yvyqmtpkdt llplamvsii hyfnwnwvgl visdndegnq flselkketq tkeicfafvt
      241 mmtindlssy hktemyynei vmsstnviii ygetdsiiel sfrmwkspvi qriwitksel
      301 dfptsngdls hdifygtltf lhhhgeisgf knfvetryhl ksrdlnllip ewnyfnyeas
      361 asnckilrny ssnsslewlt eqkfqmafnd esnsiynavy amahalhekn lqevdnqeik
      421 ngkrtsthcl klnsflrkth ftnplgdkvi mkqrervqed ydivhiqnfs qrlrikvkig
      481 kfspyfphgg rfhlyeemie latgsrkmps svcsadcspg frkiwkegma accficspcp
      541 eneisnetnm dqcvncpeyq yankeknkci qkgviflsye dplgmvlali afclsvftav
      601 vfcvfvknhd tpivkannri lsyllvmslm fcflcsfffi ghpnnatcil qqitfgitft
      661 vavstvlakt itvvlafkit dpgrmlrnfl vlgapnyiip icsllqcilc aiwlavsppf
      721 vdidkhsehg hiiivcnkgs vmafycvlgy laclalgsft maflaknlpd tfneakyltf
      781 silvffsvwv tflpvyhstk grvmvaveif silsssagml gciftpkiyi ilvkpernsi
      841 qrireksyf
//
LOCUS       NP_112323                868 aa            linear   ROD 28-APR-2025
DEFINITION  muscle, skeletal receptor tyrosine protein kinase precursor [Rattus
            norvegicus].
ACCESSION   NP_112323
VERSION     NP_112323.2
DBSOURCE    REFSEQ: accession NM_031061.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Bahreinipour,M.A., Joukar,S., Hovanloo,F., Najafipour,H.,
            Naderi,V., Rajiamirhasani,A. and Esmaeili-Mahani,S.
  TITLE     Mild aerobic training with blood flow restriction increases the
            hypertrophy index and MuSK in both slow and fast muscles of old
            rats: Role of PGC-1alpha
  JOURNAL   Life Sci 202, 103-109 (2018)
   PUBMED   29604268
  REMARK    GeneRIF: Low endurance exercise plus blood flow restriction
            improves the MuSK and hypertrophy index of both slow and fast
            muscles of elderly rats probably through the rise of PGC-1alpha
            expression
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Tan-Sindhunata,M.B., Mathijssen,I.B., Smit,M., Baas,F., de
            Vries,J.I., van der Voorn,J.P., Kluijt,I., Hagen,M.A., Blom,E.W.,
            Sistermans,E., Meijers-Heijboer,H., Waisfisz,Q., Weiss,M.M. and
            Groffen,A.J.
  TITLE     Identification of a Dutch founder mutation in MUSK causing fetal
            akinesia deformation sequence
  JOURNAL   Eur J Hum Genet 23 (9), 1151-1157 (2015)
   PUBMED   25537362
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Tsonis,A.I., Zisimopoulou,P., Lazaridis,K., Tzartos,J.,
            Matsigkou,E., Zouvelou,V., Mantegazza,R., Antozzi,C., Andreetta,F.,
            Evoli,A., Deymeer,F., Saruhan-Direskeneli,G., Durmus,H.,
            Brenner,T., Vaknin,A., Berrih-Aknin,S., Behin,A., Sharshar,T., De
            Baets,M., Losen,M., Martinez-Martinez,P., Kleopa,K.A.,
            Zamba-Papanicolaou,E., Kyriakides,T., Kostera-Pruszczyk,A.,
            Szczudlik,P., Szyluk,B., Lavrnic,D., Basta,I., Peric,S.,
            Tallaksen,C., Maniaol,A., Casasnovas Pons,C., Pitha,J.,
            Jakubikova,M., Hanisch,F. and Tzartos,S.J.
  TITLE     MuSK autoantibodies in myasthenia gravis detected by cell based
            assay--A multinational study
  JOURNAL   J Neuroimmunol 284, 10-17 (2015)
   PUBMED   26025053
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Witzemann,V., Chevessier,F., Pacifici,P.G. and Yampolsky,P.
  TITLE     The neuromuscular junction: selective remodeling of synaptic
            regulators at the nerve/muscle interface
  JOURNAL   Mech Dev 130 (6-8), 402-411 (2013)
   PUBMED   23032192
  REMARK    Review article
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Terrado,J., Burgess,R.W., DeChiara,T., Yancopoulos,G., Sanes,J.R.
            and Kato,A.C.
  TITLE     Motoneuron survival is enhanced in the absence of neuromuscular
            junction formation in embryos
  JOURNAL   J Neurosci 21 (9), 3144-3150 (2001)
   PUBMED   11312299
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Gautam,M., DeChiara,T.M., Glass,D.J., Yancopoulos,G.D. and
            Sanes,J.R.
  TITLE     Distinct phenotypes of mutant mice lacking agrin, MuSK, or rapsyn
  JOURNAL   Brain Res Dev Brain Res 114 (2), 171-178 (1999)
   PUBMED   10320756
REFERENCE   8  (residues 1 to 868)
  AUTHORS   Bowen,D.C., Park,J.S., Bodine,S., Stark,J.L., Valenzuela,D.M.,
            Stitt,T.N., Yancopoulos,G.D., Lindsay,R.M., Glass,D.J. and
            DiStefano,P.S.
  TITLE     Localization and regulation of MuSK at the neuromuscular junction
  JOURNAL   Dev Biol 199 (2), 309-319 (1998)
   PUBMED   9698449
REFERENCE   9  (residues 1 to 868)
  AUTHORS   DeChiara,T.M., Bowen,D.C., Valenzuela,D.M., Simmons,M.V.,
            Poueymirou,W.T., Thomas,S., Kinetz,E., Compton,D.L., Rojas,E.,
            Park,J.S., Smith,C., DiStefano,P.S., Glass,D.J., Burden,S.J. and
            Yancopoulos,G.D.
  TITLE     The receptor tyrosine kinase MuSK is required for neuromuscular
            junction formation in vivo
  JOURNAL   Cell 85 (4), 501-512 (1996)
   PUBMED   8653786
REFERENCE   10 (residues 1 to 868)
  AUTHORS   Valenzuela,D.M., Stitt,T.N., DiStefano,P.S., Rojas,E., Mattsson,K.,
            Compton,D.L., Nunez,L., Park,J.S., Stark,J.L., Gies,D.R. et al.
  TITLE     Receptor tyrosine kinase specific for the skeletal muscle lineage:
            expression in embryonic muscle, at the neuromuscular junction, and
            after injury
  JOURNAL   Neuron 15 (3), 573-584 (1995)
   PUBMED   7546737
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Nov 27, 2020 this sequence version replaced NP_112323.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U34985.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760386,
                                           SAMEA5760475 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..868
                     /product="muscle, skeletal receptor tyrosine protein
                     kinase precursor"
                     /EC_number="2.7.10.1"
                     /note="muscle-specific tyrosine kinase receptor MuSK;
                     muscle, skeletal receptor tyrosine protein kinase;
                     muscle-specific kinase receptor; muscle-specific tyrosine
                     protein kinase receptor; muscle specific kinase (neural
                     fold/somite kinase 1); muscle, skeletal, receptor tyrosine
                     kinase"
                     /calculated_mol_wt=94484
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
                     /calculated_mol_wt=2347
     mat_peptide     22..868
                     /product="Muscle, skeletal receptor tyrosine protein
                     kinase. /id=PRO_0000024448"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62838.1)"
                     /calculated_mol_wt=94484
     Region          28..117
                     /region_name="IgI_1_MuSK"
                     /note="agrin-responsive first immunoglobulin-like domains
                     (Ig1) of the MuSK ectodomain; a member of the I-set of
                     IgSF domains; cd20970"
                     /db_xref="CDD:409562"
     Region          28..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409562"
     Region          35..39
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409562"
     Region          45..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409562"
     Region          58..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409562"
     Region          65..67
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409562"
     Region          75..78
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409562"
     Region          82..88
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409562"
     Region          95..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409562"
     Region          109..117
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409562"
     Region          122..209
                     /region_name="IgI_2_MuSK"
                     /note="agrin-responsive second immunoglobulin-like domains
                     (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a
                     member of the I-set of Ig superfamily domains; cd20968"
                     /db_xref="CDD:409560"
     Region          122..125
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409560"
     Region          129..131
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409560"
     Region          137..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409560"
     Region          151..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409560"
     Region          158..161
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409560"
     Region          166..170
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409560"
     Region          173..179
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409560"
     Region          186..194
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409560"
     Region          197..202
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409560"
     Region          204..209
                     /region_name="Ig strand G'"
                     /note="Ig strand G' [structural motif]"
                     /db_xref="CDD:409560"
     Region          213..296
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Region          229..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          242..246
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          268..272
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..284
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          292..295
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          313..457
                     /region_name="CRD_TK_ROR_related"
                     /note="Cysteine-rich domain of proteins similar to
                     tyrosine kinase-like orphan receptors; cd07469"
                     /db_xref="CDD:143578"
     Site            order(324,326..328,337..339)
                     /site_type="other"
                     /note="putative Wnt binding site [polypeptide binding]"
                     /db_xref="CDD:143578"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19664639; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Site            459
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Site            495..515
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62838.1)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Region          568..857
                     /region_name="PTKc_Musk"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Muscle-specific kinase; cd05050"
                     /db_xref="CDD:133181"
     Site            order(580..584,588,606,608,654..657,660..661,724,728..729,
                     731,742,760..764,773,807)
                     /site_type="active"
                     /db_xref="CDD:133181"
     Site            order(580..581,583..584,588,606,608,654..657,660..661,
                     728..729,731,742)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133181"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:Q61006; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     Site            order(724,728,760..764,773,807)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133181"
     Site            741..766
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133181"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20603078; propagated from
                     UniProtKB/Swiss-Prot (Q62838.1)"
     CDS             1..868
                     /gene="Musk"
                     /gene_synonym="Nsk1"
                     /coded_by="NM_031061.2:120..2726"
                     /db_xref="GeneID:81725"
                     /db_xref="RGD:3211"
ORIGIN      
        1 mrelvnipll qmltlvafsg teklpkapvi ttpletvdal veevatfmca vesypqpeis
       61 wtrnkilikl fdtrysiren gqlltilsve dsddgiycct anngvggave scgalqvkmk
      121 pkitrppinv kiieglkavl pcttmgnpkp svswikgdsa lrensriavl esgslrihnv
      181 qkedagqyrc vaknslgtay sklvklevev farilrapes hnvtfgsfvt lrctaigmpv
      241 ptiswiengn avssgsiqen vkdrvidsrl qlfitkpgly tciatnkhge kfstakaaat
      301 vsiaewsksq keskgycaqy rgevcdavlv kdslvffnts ypdpeeaqel lihtawnelk
      361 avsplcrpaa eallcnhlfq ecssgvlptp mpicreycla vkelfcakew lamegkthrg
      421 lyrsgmhflp vpecsklpsm hqdptactrl pyldykkeni ttfpsitssk psvdipnlpa
      481 stssfavspa ysmtviisim scfavfallt ittlyccrrr rewknkkres aavtlttlps
      541 ellldrlhpn pmyqrmplll npkllsleyp rnnieyvrdi gegafgrvfq arapgllpye
      601 pftmvavkml keeasadmqa dfqreaalma efdnpnivkl lgvcavgkpm cllfeymayg
      661 dlneflrsms phtvcslshs dlstrarvss pgppplscae qlciarqvaa gmaylserkf
      721 vhrdlatrnc lvgenmvvki adfglsrniy sadyykadgn daipirwmpp esifynrytt
      781 esdvwaygvv lweifsyglq pyygmaheev iyyvrdgnil acpencplel ynlmrlcwsk
      841 lpadrpsfcs ihrilqrmce raegtvgv
//
LOCUS       NP_001103406             360 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-dependent kinase 10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001103406
VERSION     NP_001103406.1
DBSOURCE    REFSEQ: accession NM_001109936.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Guen,V.J., Gamble,C., Perez,D.E., Bourassa,S., Zappel,H.,
            Gartner,J., Lees,J.A. and Colas,P.
  TITLE     STAR syndrome-associated CDK10/Cyclin M regulates actin network
            architecture and ciliogenesis
  JOURNAL   Cell Cycle 15 (5), 678-688 (2016)
   PUBMED   27104747
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Guen,V.J., Gamble,C., Flajolet,M., Unger,S., Thollet,A.,
            Ferandin,Y., Superti-Furga,A., Cohen,P.A., Meijer,L. and Colas,P.
  TITLE     CDK10/cyclin M is a protein kinase that controls ETS2 degradation
            and is deficient in STAR syndrome
  JOURNAL   Proc Natl Acad Sci U S A 110 (48), 19525-19530 (2013)
   PUBMED   24218572
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Sergere,J.C., Thuret,J.Y., Le Roux,G., Carosella,E.D. and
            Leteurtre,F.
  TITLE     Human CDK10 gene isoforms
  JOURNAL   Biochem Biophys Res Commun 276 (1), 271-277 (2000)
   PUBMED   11006117
  REMARK    Erratum:[Biochem Biophys Res Commun 2000 Dec 20;279(2):738-9]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DY320517.1, DN935585.1,
            BC098804.1 and AI071224.1.
            
            Summary: The protein encoded by this gene belongs to the CDK
            subfamily of the Ser/Thr protein kinase family. The CDK subfamily
            members are highly similar to the gene products of S. cerevisiae
            cdc28, and S. pombe cdc2, and are known to be essential for cell
            cycle progression. The human ortholog has been shown to play a role
            in cellular proliferation. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the most
            predominant transcript and encodes isoform 1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..360
                     /product="cyclin-dependent kinase 10 isoform 1"
                     /EC_number="2.7.11.22"
                     /note="cell division protein kinase 10; cyclin-dependent
                     kinase (CDC2-like) 10"
                     /calculated_mol_wt=40799
     Region          31..339
                     /region_name="STKc_CDK10"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 10; cd07845"
                     /db_xref="CDD:173742"
     Site            order(45..48,53,66,68,85,99,117..120,123,125..126,163,165,
                     167..168,170,181,184,196,198..201,203,241..242)
                     /site_type="active"
                     /db_xref="CDD:173742"
     Site            order(45..48,53,66,68,99,117..120,123,126,167..168,170,
                     181)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173742"
     Site            order(77..79,81,84..85,87..88,91..92,104,106,113,152,
                     155..158,186,188..191,195..196,309,313..315)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:173742"
     Site            order(85,125,163,165,184,196,198..201,203,241..242)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173742"
     Site            order(180..191,193..203)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173742"
     CDS             1..360
                     /gene="Cdk10"
                     /coded_by="NM_001109936.1:9..1091"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361434"
                     /db_xref="RGD:1304851"
ORIGIN      
        1 maevdlesdq irlkcirkeg fftvppehrl grcrsvkefe klnrigegty givyrardtq
       61 tdeivalkkv rmdkekdgip isslreitll lrlrhpnive lkevvvgnhl esiflvmgyc
      121 eqdlasllen mptpfseaqv kcillqvlrg lqylhrsfii hrdlkvsnll mtdkgcvkta
      181 dfglaraygv pvkpmtpkvv tlwyrapell lgtttqttsi dmwavgcila ellahkpllp
      241 gtseihqidl ivqllgtpse niwpgfsklp lagqyslrkq pynnlkhkfp wlseaglrll
      301 nflfmydpkk ratagdcles syfkekplpc epelmptfph hrnkraapaa tegqskrcrp
//
LOCUS       NP_001401664            2190 aa            linear   ROD 28-APR-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 12 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001401664 XP_006257166
VERSION     NP_001401664.1
DBSOURCE    REFSEQ: accession NM_001414735.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2190)
  AUTHORS   Makinen,N., Aavikko,M., Heikkinen,T., Taipale,M., Taipale,J.,
            Koivisto-Korander,R., Butzow,R. and Vahteristo,P.
  TITLE     Exome Sequencing of Uterine Leiomyosarcomas Identifies Frequent
            Mutations in TP53, ATRX, and MED12
  JOURNAL   PLoS Genet 12 (2), e1005850 (2016)
   PUBMED   26891131
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2190)
  AUTHORS   Lesca,G., Moizard,M.P., Bussy,G., Boggio,D., Hu,H., Haas,S.A.,
            Ropers,H.H., Kalscheuer,V.M., Des Portes,V., Labalme,A.,
            Sanlaville,D., Edery,P., Raynaud,M. and Lespinasse,J.
  TITLE     Clinical and neurocognitive characterization of a family with a
            novel MED12 gene frameshift mutation
  JOURNAL   Am J Med Genet A 161A (12), 3063-3071 (2013)
   PUBMED   24039113
REFERENCE   3  (residues 1 to 2190)
  AUTHORS   Poss,Z.C., Ebmeier,C.C. and Taatjes,D.J.
  TITLE     The Mediator complex and transcription regulation
  JOURNAL   Crit Rev Biochem Mol Biol 48 (6), 575-608 (2013)
   PUBMED   24088064
  REMARK    Review article
REFERENCE   4  (residues 1 to 2190)
  AUTHORS   Vogl,M.R., Reiprich,S., Kuspert,M., Kosian,T., Schrewe,H.,
            Nave,K.A. and Wegner,M.
  TITLE     Sox10 cooperates with the mediator subunit 12 during terminal
            differentiation of myelinating glia
  JOURNAL   J Neurosci 33 (15), 6679-6690 (2013)
   PUBMED   23575864
REFERENCE   5  (residues 1 to 2190)
  AUTHORS   Vulto-van Silfhout,A.T., de Vries,B.B., van Bon,B.W., Hoischen,A.,
            Ruiterkamp-Versteeg,M., Gilissen,C., Gao,F., van Zwam,M.,
            Harteveld,C.L., van Essen,A.J., Hamel,B.C., Kleefstra,T.,
            Willemsen,M.A., Yntema,H.G., van Bokhoven,H., Brunner,H.G.,
            Boyer,T.G. and de Brouwer,A.P.
  TITLE     Mutations in MED12 cause X-linked Ohdo syndrome
  JOURNAL   Am J Hum Genet 92 (3), 401-406 (2013)
   PUBMED   23395478
REFERENCE   6  (residues 1 to 2190)
  AUTHORS   Ge,K., Guermah,M., Yuan,C.X., Ito,M., Wallberg,A.E.,
            Spiegelman,B.M. and Roeder,R.G.
  TITLE     Transcription coactivator TRAP220 is required for PPAR gamma
            2-stimulated adipogenesis
  JOURNAL   Nature 417 (6888), 563-567 (2002)
   PUBMED   12037571
REFERENCE   7  (residues 1 to 2190)
  AUTHORS   Kang,Y.K., Guermah,M., Yuan,C.X. and Roeder,R.G.
  TITLE     The TRAP/Mediator coactivator complex interacts directly with
            estrogen receptors alpha and beta through the TRAP220 subunit and
            directly enhances estrogen receptor function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2642-2647 (2002)
   PUBMED   11867769
REFERENCE   8  (residues 1 to 2190)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   9  (residues 1 to 2190)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 2190)
  AUTHORS   Ito,M., Yuan,C.X., Malik,S., Gu,W., Fondell,J.D., Yamamura,S.,
            Fu,Z.Y., Zhang,X., Qin,J. and Roeder,R.G.
  TITLE     Identity between TRAP and SMCC complexes indicates novel pathways
            for the function of nuclear receptors and diverse mammalian
            activators
  JOURNAL   Mol Cell 3 (3), 361-370 (1999)
   PUBMED   10198638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Dec 9, 2022 this sequence version replaced XP_006257166.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.56101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2190
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..2190
                     /product="mediator of RNA polymerase II transcription
                     subunit 12 isoform 1"
                     /note="mediator of RNA polymerase II transcription subunit
                     12"
                     /calculated_mol_wt=244408
     Region          106..161
                     /region_name="Med12"
                     /note="Transcription mediator complex subunit Med12;
                     pfam09497"
                     /db_xref="CDD:462818"
     Region          287..758
                     /region_name="Med12-LCEWAV"
                     /note="Eukaryotic Mediator 12 subunit domain; pfam12145"
                     /db_xref="CDD:463472"
     Region          1821..2027
                     /region_name="Med12-PQL"
                     /note="Eukaryotic Mediator 12 catenin-binding domain;
                     pfam12144"
                     /db_xref="CDD:463471"
     CDS             1..2190
                     /gene="Med12"
                     /coded_by="NM_001414735.1:22..6594"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:679693"
                     /db_xref="RGD:1585896"
ORIGIN      
        1 maafgilsye hrplkrlrlg ppdvypqdpk qkedeltaln vkqgfnnqpa vsgdehgsak
       61 nvnfnpakis snfssiiaek lrcntlsdtg rrkslmnqkd nfwlvtarsq saintwftdl
      121 agtkplthla kkvpifskke evfgylakyt vpvmraawli kmtcayyaam setkvkkknt
      181 adpftewtqi itkylweqlq kmaeyyrpgp agsgvcgsai gplphdvema irqwdynekl
      241 alfmfqdgml drhefltwvl ecfekirpge dellklllpl llrysgefvq saylsrrlay
      301 fctrrlalql dgvnshsshv isaqstsslp ttpapqppts ntpstpfsdl lmcpqhrplv
      361 fglscilqti llccpsalvw hysltdsrik tgspldhlpi apsnlpmpeg nsaftqqvra
      421 klreieqqik ergqavevrw sfdkcqeata gftigrvlht levldshsfe rsdfsnslds
      481 lcnrifglgp skdgheissd ddavvsllce wavsckrsgr hramvvakll ekrqaeieae
      541 rcgeseaade kgsvasgsls apsapifqdv llqfldtqap mltdprsese rveffnlvll
      601 fcelirhdvf shnmytctli srgdlafgtp gprppspfdd paddperkea egsssskled
      661 pglsesmdid psssvlfedm ekpdfslfsp tmpcegkgsp spekpdvekd vkpppkekie
      721 gtlgilydqp rhvqyathfp ipqeescshe cnqrlvvlfg vgkqrddarh aikkitkdil
      781 kvlnrkgtae tdqlapivpl npgdltflgg edgqkrrrnr peafptaedi fakfqhlshy
      841 dqhqvtaqvs rnvleqitsf algmsyhlpl vqhvqfvfdl meyslsisgl idfaiqllne
      901 lsvveaelll kssdlvgsyt tslclcivav lrhyhaclil nqdqmaqvfe glcgvvkhgm
      961 nrsdgssaer cilaylydly tscshlkskf gelfsdfcsk vkntiycnve psesnmrwap
     1021 efmidtlenp aahtftytgl gkslsenpan rysfvcnalm hvcvghhdpd rvndiailca
     1081 eltgycksls aewlgvlkal ccssnngtcg fndllcnvdv sdlsfhdsla tfvailiarq
     1141 cllledlirc aaipsllnaa cseqdsepga rltcrillhl fktpqlnpcq sdgnkptvgi
     1201 rsscdrhlla asqnrivdga vfavlkavfv lgdaelkgsg ftvpggteel peeeggggss
     1261 grrqggrnis vetasldvya kyvlrsicqq ewvgerclks lcedsndlqd pvlssaqaqr
     1321 lmqlicyphr lldsedgenp qrqrikrilk nldqwtmrqs slelqlmikq tpntemnsll
     1381 eniakatiev fqqsaetgss sgstasnmps sskakpvlss lersgvwlva pliaklptsv
     1441 qghvlkaage elekgqhlgs ssrkerdrqk qksmsllsqq pflslvltcl kgqdeqregl
     1501 laslhsqvhq ivinwrenqy lddckpkqlm healklrlnl vggmfdtvqr stqqttewaq
     1561 llleiiisgt vdmqsnnelf ttvldmlsvl ingtlaadms sisqgsmeen kraymnlvkk
     1621 lqkdlgerqs dslekvhqll plpkqnrdvi tcepqgslid tkgnkiagfd sifkkeglqv
     1681 stkqkispwe lfeglkpsta plswawfgtv rvdrrvarge eqqrlllyht hlrprprayy
     1741 leplplpped eeppapalle pekkapeppk tdkpgtapps teerkkkstk gkkrsqpatk
     1801 sedygmgpgr sgpygvtvpp dllhhanpgs ishlsyrqss mglytqnqpl paggprvdpy
     1861 rpvrlpmqkl ptrptypgvl pttmttvmgl epssyktsvy rqqqptvpqg qrlrqqlqak
     1921 iqsqgmlgqs svhqmtpsss yglqssqgyt syvshvglqq htgpagtmvp psyssqpyqs
     1981 thpstnptlv dptrhlqqrp sgyvhqqapt yghgltstqr fshqtlqqtp mmgtmtplsa
     2041 qgvqagvrst silpeqqqqq qqqqqqqqqq qqqqqqqqqq qqqqqqqyhi rqqqqqqqil
     2101 rqqqqqqqqq qqqqqqqqqq qqqqpqqqqp hqqqqqaapp qpqpqsqpqf qrqglqqtqq
     2161 qqqtaalvrq lqqqlsntqp qpstnifgry
//
LOCUS       NP_064473               2765 aa            linear   ROD 28-APR-2025
DEFINITION  teneurin-2 [Rattus norvegicus].
ACCESSION   NP_064473 XP_346398
VERSION     NP_064473.1
DBSOURCE    REFSEQ: accession NM_020088.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2765)
  AUTHORS   Silva,J.P., Lelianova,V.G., Ermolyuk,Y.S., Vysokov,N.,
            Hitchen,P.G., Berninghausen,O., Rahman,M.A., Zangrandi,A.,
            Fidalgo,S., Tonevitsky,A.G., Dell,A., Volynski,K.E. and
            Ushkaryov,Y.A.
  TITLE     Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a
            high-affinity transsynaptic receptor pair with signaling
            capabilities
  JOURNAL   Proc Natl Acad Sci U S A 108 (29), 12113-12118 (2011)
   PUBMED   21724987
  REMARK    GeneRIF: Latrophilin 1 and its endogenous ligand Lasso/teneurin-2
            form a high-affinity transsynaptic receptor pair with signaling
            capabilities.
REFERENCE   2  (residues 1 to 2765)
  AUTHORS   Feng,K., Zhou,X.H., Oohashi,T., Morgelin,M., Lustig,A.,
            Hirakawa,S., Ninomiya,Y., Engel,J., Rauch,U. and Fassler,R.
  TITLE     All four members of the Ten-m/Odz family of transmembrane proteins
            form dimers
  JOURNAL   J Biol Chem 277 (29), 26128-26135 (2002)
   PUBMED   12000766
REFERENCE   3  (residues 1 to 2765)
  AUTHORS   Otaki,J.M. and Firestein,S.
  TITLE     Neurestin: putative transmembrane molecule implicated in neuronal
            development
  JOURNAL   Dev Biol 212 (1), 165-181 (1999)
   PUBMED   10419693
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF086607.1.
            
            On Jan 12, 2005 this sequence version replaced XP_346398.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF086607.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2765
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..2765
                     /product="teneurin-2"
                     /note="ten-2; ten-m2; teneurin-2-like; tenascin-M2; odz,
                     odd Oz/ten-m homolog 2; protein Odd Oz/ten-m homolog 2;
                     neurestin"
                     /calculated_mol_wt=306443
     Region          10..374
                     /region_name="Ten_N"
                     /note="Teneurin Intracellular Region; pfam06484"
                     /db_xref="CDD:461932"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTS5; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          111..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHK6; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            380..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            443
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            528..529
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          580..602
                     /region_name="EGF_2"
                     /note="EGF-like domain; pfam07974"
                     /db_xref="CDD:400365"
     Region          644..790
                     /region_name="C_rich_MXAN6577"
                     /note="MXAN_6577-like cysteine-rich domain; NF041328"
                     /db_xref="CDD:469225"
     Region          798..831
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          834..864
                     /region_name="acid_disulf_rpt"
                     /note="acidic double-disulfide repeat; NF033662"
                     /db_xref="CDD:411265"
     Site            916
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1231..1561
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          1231..1270
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Site            1258
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1263..1307
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1282..1325
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1333..1377
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1349..1387
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1392..1443
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1403..1444
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1465..1492
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1467..1500
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1521..1564
                     /region_name="NHL 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1522..2459
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          1535..1561
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1574..1593
                     /region_name="YD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1610..1630
                     /region_name="YD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1673..1692
                     /region_name="YD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1693..1715
                     /region_name="YD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1703
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1740
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1798
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1883
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1886..1905
                     /region_name="YD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1927..1945
                     /region_name="YD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1946..1966
                     /region_name="YD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1973..1990
                     /region_name="YD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            1984
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          1991..2012
                     /region_name="YD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2013..2030
                     /region_name="YD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2033..2053
                     /region_name="YD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2056..2076
                     /region_name="YD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2084..2104
                     /region_name="YD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2110..2127
                     /region_name="YD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2128..2154
                     /region_name="YD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2156..2169
                     /region_name="YD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2170..2193
                     /region_name="YD 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            2188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2196..2216
                     /region_name="YD 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2217..2237
                     /region_name="YD 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2239..2259
                     /region_name="YD 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2271..2291
                     /region_name="YD 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2293..2313
                     /region_name="YD 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            2328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2339..2380
                     /region_name="YD 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Site            2639
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1K2.2)"
     Region          2681..2758
                     /region_name="Tox-GHH"
                     /note="GHH signature containing HNH/Endo VII superfamily
                     nuclease toxin; pfam15636"
                     /db_xref="CDD:464783"
     CDS             1..2765
                     /gene="Tenm2"
                     /gene_synonym="Lasso; Odz2"
                     /coded_by="NM_020088.1:133..8430"
                     /db_xref="GeneID:117242"
                     /db_xref="RGD:727907"
ORIGIN      
        1 mdvkdrrhrs ltrgrcgkec rytsssldse dcrvptqksy sssetlkayd hdsrmhygnr
       61 vtdlvhresd efsrqganft laelgiceps phrsgycsdm gilhqgysls tgsdadsdte
      121 ggmspehair lwgrgiksrr ssglssrens altltdsdne nksdddngrp ipptssssll
      181 psaqlpsshn pppvscqmpl ldsntshqim dtnpdeefsp nsyllracsg pqqasssgpp
      241 nhhsqstlrp plppphnhtl shhhssansl nrnsltnrrs qihapapapn dlattpesvq
      301 lqdswvlnsn vpletrhflf ktssgstplf sssspgyplt sgtvytpppr llprntfsrk
      361 afklkkpsky cswkcaalsa iaaalllail layfiamhll glnwqlqpad ghtfnngvrt
      421 glpgnddvat vpsggkvpws lknssidsge aevgrrvtqe vppgvfwrsq ihisqpqflk
      481 fnislgkdal fgvyirrglp pshaqydfme rldgkekwsv vesprerrsi qtlvqneavf
      541 vqyldvglwh lafyndgkdk emvsfntvvl dsvqdcprnc hgngecvsgl chcfpgflga
      601 dcakaacpvl csgngqyskg tcqcysgwkg aecdvpmnqc idpscgghgs cidgncvcaa
      661 gykgehceev dcldptcssh gvcvngeclc spgwgglnce larvqcpdqc sghgtylpds
      721 glcncdpnwm gpdcsvevcs vdcgthgvci ggacrceegw tgaacdqrvc hprciehgtc
      781 kdgkcecreg wngehctidg cpdlcngngr ctlgqnswqc vcqtgwrgpg cnvametsca
      841 dnkdnegdgl vdcldpdccl qsacqnsllc rgsrdpldii qqgqtdwpav ksfydrikll
      901 agkdsthiip gdnpfnsslv slirgqvvtt dgtplvgvnv sfvkypkygy titrqdgtfd
      961 lianggsalt lhferapfms rertvwppwn sfyamdtlvm kteensipsc dlsgfvrpdp
     1021 iiissplstf fsaspaanpi vpetqvlhee ielpgtnvkl rylssrtagy ksllkitmtq
     1081 stvplnlirv hlmvaveghl fqksfqaspn laytfiwdkt daygqrvygl sdavvsvgfe
     1141 yetcpslilw ekrtallqgf eldpsnlggw sldkhhtlnv ksgillkgtg enqfltqqpa
     1201 iitsimgngr rrsiscpscn glaegnklla pvalavgidg slfvgdfnyi rrifpsrnvt
     1261 silelrnkef khsnspghky ylavdpvtgs lyvsdtnsrr iyrvkslsga kdlagnsevv
     1321 agtgeqclpf dearcgdggk avdatlmspr giavdknglm yfvdatmirk vdqngiistl
     1381 lgsndltavr plscdssmdv aqvrlewptd lavnpmdnsl yvlennvilr itenhqvsii
     1441 agrpmhcqvp gidyslskla ihsalesasa iaishtgvly itetdekkin rlrqvttnge
     1501 icllagaasd cdckndvnci cysgddayat dailnspssl avapdgtiyi adlgnirira
     1561 vsknkpvlna fnqyeaaspg eqelyvfnad gihqytvslv tgeylynfty sadndvteli
     1621 dnngnslkir rdssgmprhl lmpdnqiitl tvgtngglka vstqnlelgl mtydgntgll
     1681 atksdetgwt tfydydhegr ltnvtrptgv vtslhremek sitvdiensn rdndvtvitn
     1741 lssveasytv vqdqvrnsyq lcsngtlrvm yangmgvsfh sephvlagtl tptigrcnis
     1801 lpmenglnsi ewrlrkeqik gkvtifgrkl rvhgrnllsi dydrnirtek iyddhrkftl
     1861 riiydqvgrp flwlpssgla avnvsyffng rlaglqrgam sertdidkqg rivsrmfadg
     1921 kvwsysyldk smvlllqsqr qyifeydssd rlhavtmpsv arhsmsthts igyirniynp
     1981 pesnasvifd ysddgrilkt sflgtgrqvf ykygklskls eivydstavt fgydettgvl
     2041 kmvnlqsggf sctiryrkvg plvdkqiyrf seegminarf dytyhdnsfr iasikpvise
     2101 tplpvdlyry deisgkvehf gkfgviyydi nqiittavmt lskhfdthgr ikevqyemfr
     2161 slmywmtvqy dsmgrvikre lklgpyantt kytydydgdg qlqsvavndr ptwrysydln
     2221 gnlhllnpgn sarlmplryd lrdritrlgd vqykidddgy lcqrgsdife ynskglltra
     2281 ynkasgwsvq yrydgvsrra syktnlghhl qyfysdlhhp trithvynhs nseitslyyd
     2341 lqghlfames ssgeeyyvas dntgtplavf singlmikql qytaygeiyy dsnpdfqmvi
     2401 gfhgglydpl tklvhftqrd ydvlagrwts pdytmwrnvg kepapfnlym fknnnplsne
     2461 ldlknyvtdv kswlvmfgfq lsniipgfpr akmyfvpppy elsesqasen gqlitgvqqt
     2521 terhnqafla legqviskkl hagirekagh wfatttpiig kgimfaikeg rvttgvssia
     2581 sedsrkvasv lnnayyldkm hysiegkdth yfvkigaadg dlvtlgttig rkvlesgvnv
     2641 tvsqptllvn grtrrftnie fqystlllsi rygltpdtld eekarvldqa rqralgtawa
     2701 keqqkardgr egsrlwtege kqqllstgrv qgyegyyvlp veqypelads ssniqflrqn
     2761 emgkr
//
LOCUS       NP_001155281             752 aa            linear   ROD 28-APR-2025
DEFINITION  striatin-4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001155281
VERSION     NP_001155281.1
DBSOURCE    REFSEQ: accession NM_001161809.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Lin,L., Lo,L.H., Lyu,Q. and Lai,K.O.
  TITLE     Determination of dendritic spine morphology by the striatin
            scaffold protein STRN4 through interaction with the phosphatase
            PP2A
  JOURNAL   J Biol Chem 292 (23), 9451-9464 (2017)
   PUBMED   28442576
  REMARK    GeneRIF: STRN4 is preferentially expressed in mushroom spines, and
            STRN4 specifically maintains mushroom spines but not thin spines
            and filopodia through interaction with the phosphatase PP2A
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Benoist,M., Baude,A., Tasmadjian,A., Dargent,B., Kessler,J.P. and
            Castets,F.
  TITLE     Distribution of zinedin in the rat brain
  JOURNAL   J Neurochem 106 (2), 969-977 (2008)
   PUBMED   18466332
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Gaillard,S., Bailly,Y., Benoist,M., Rakitina,T., Kessler,J.P.,
            Fronzaroli-Molinieres,L., Dargent,B. and Castets,F.
  TITLE     Targeting of proteins of the striatin family to dendritic spines:
            role of the coiled-coil domain
  JOURNAL   Traffic 7 (1), 74-84 (2006)
   PUBMED   16445688
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Baillat,G., Moqrich,A., Castets,F., Baude,A., Bailly,Y.,
            Benmerah,A. and Monneron,A.
  TITLE     Molecular cloning and characterization of phocein, a protein found
            from the Golgi complex to dendritic spines
  JOURNAL   Mol Biol Cell 12 (3), 663-673 (2001)
   PUBMED   11251078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1, BF408712.1, BC168948.1 and BQ198897.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the central coding region, compared to variant 1. The resulting
            isoform (2) lacks an internal 7-aa segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.1688954.1,
                                           SRR26643291.782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: PMID: 18466332
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..752
                     /product="striatin-4 isoform 2"
                     /note="zinedin; striatin, calmodulin binding protein 4"
                     /calculated_mol_wt=80636
     Region          64..188
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          429..751
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(436,454,458,464..465,488..489,507,511,517..518,
                     541..542,559,564,570..571,588,607,612,617..618,632..633,
                     653,657,663..664,676..677,694,699,705..706,718,723,741,
                     745,751)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          442..488
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          494..541
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          546..584
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          593..629
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          639..675
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          681..720
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          727..751
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..752
                     /gene="Strn4"
                     /coded_by="NM_001161809.1:455..2713"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308392"
                     /db_xref="RGD:1307030"
ORIGIN      
        1 mmeeraaaav asaascrplg sgtapnptaa apasspapgp gpvgkggggg gspgptagpe
       61 plslpgilhf iqhewarfea ekarweaera elqaqvaflq gerkgqenlk tdlvrrikml
      121 eyalkqerak yhklkfgtdl nqgekkadls eqvsngpves vtldnsplvw kegrqllrqy
      181 leevgytdti ldmrskrvrs llgrslelng agepvegapr aspgpgglsg gesllvkqie
      241 eqikrnaagk dgkerlggsv leqipflqnc ededsdedde ldsvqhkkqr vrlpskalvp
      301 emededeedd sedainefdf lgsgedgegs pdprrcaseg nphelesrrv klqgiladlr
      361 dvdglppkvt vpppgtpqpr phedvfimdt igggevslgd ladltvtndn dlscdlsdsk
      421 dafkktwnpk ftlrshydgi rslafhhsqs alltasedgt lklwnlqkav takknaaldv
      481 epihafrahr gpvlavtmgs nseycysgga darihswkip dlnmdpydgy dpsvlscvle
      541 ghgdavwgla fsptsqrlas csadgtiriw dpsssgsscl ctfpmagehg iptsvaftst
      601 epahvvasfr sgdtvlydle aggalltles rgssgptqin qvvshpnqpl titahddrgi
      661 rfldnrtgks vhsmvahlda vtclavdpng vflmsgshdc slrlwsldnk tcvqeitahr
      721 kkheeaihav achpskalia sagadalakv fv
//
LOCUS       NP_001333231             997 aa            linear   ROD 28-APR-2025
DEFINITION  similar to Est1p-like protein B isoform 1 [Rattus norvegicus].
ACCESSION   NP_001333231
VERSION     NP_001333231.1
DBSOURCE    REFSEQ: accession NM_001346302.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ074030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840116
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..997
                     /product="similar to Est1p-like protein B isoform 1"
                     /calculated_mol_wt=113747
     Region          92..204
                     /region_name="EST1"
                     /note="Telomerase activating protein Est1; pfam10374"
                     /db_xref="CDD:463062"
     Region          188..222
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(189,192..193,196..197,199,229,232..233,236,238..239,
                     264,267,270..271,274)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          213..>414
                     /region_name="EST1_DNA_bind"
                     /note="Est1 DNA/RNA binding domain; pfam10373"
                     /db_xref="CDD:431239"
     Region          227..257
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          263..286
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          841..997
                     /region_name="PIN_Smg5-like"
                     /note="VapC-like PIN domain of human nonsense-mediated
                     decay factor Smg5, and other similar eukaryotic homologs;
                     cd09884"
                     /db_xref="CDD:350232"
     Site            846
                     /site_type="other"
                     /note="conserved Asp residue"
                     /db_xref="CDD:350232"
     CDS             1..997
                     /gene="Smg5l1"
                     /gene_synonym="RGD1309489"
                     /coded_by="NM_001346302.1:271..3264"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314915"
                     /db_xref="RGD:1309489"
ORIGIN      
        1 mgigcsslht vgntvsiaqk esglmeknqe etlratflyq evclaaqrld iflqkenahk
       61 evfkphvlal remlqqacik lmflhpvvyg rkaeellwrk iysdivmllm ktnkkqmdtf
      121 qhwgeplqah lkaglkfyeh lflflqghye lrlqsyidwp hnaihligck kvgptsveea
      181 swarmachrc llylgdlfry qhefldlatk nlaercyyra lsvapnmgmp fnqlgalmgs
      241 kyydleatyy yqrclhaevp fkgaawnlkr lydhagkrys clkryqgrkl shsqrqcwdn
      301 krllvsflyl qsllqpkrkf kaarlialcq lvlddfrlcl syrpyqsglc qasiedkppk
      361 gylflpdfli fhmvvlclmn vhslrksgsk qqkpaviftl tlfsylvqhv ntriqaelqk
      421 rkltpeeaal rdgcwdkepg kehqdfpspg lqnnhsqksh kwsgicrese asfhsccdsd
      481 eteedenssl ssqaqsdtgs etshsdttde egsgslgsde iqksggspkp krahsrnklk
      541 ayvppdslld llkttisssl paplsqklqg khasplapvf shnvltpptd ptptvalsss
      601 lgtegeissf petefymgss weqrsfitqn nlqttqwkld ilsaegllpt ikvilswlrs
      661 nhslllshwr svcslwdhls vllnllpsvg dlqhpglcls hhlqdllqsc qwpntpkylq
      721 lpedialfqq sspqvsqdre glgqdppqlt nqeevivric ffrsfghfat rlpgqflrfd
      781 sklgifvsst lersesapqq fprttprirl skdivqlwlq revallektl rspqtrsvlt
      841 pylfpdpral cehlsviqkl atsakfflii pkivvdtlyi lkwedrrala aitfledelk
      901 rrnqyilcqs fvskrlvrpr mtkpdsdawd lynilefcks lldssrpgil dpssmvmiit
      961 gvclehprnf syplqlvlgm ateagveikn ilsfhke
//
LOCUS       NP_001400159             328 aa            linear   ROD 28-APR-2025
DEFINITION  RNA binding protein fox-1 homolog 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001400159
VERSION     NP_001400159.1
DBSOURCE    REFSEQ: accession NM_001413230.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Anderson,M.B., Das,S. and Miller,K.E.
  TITLE     Subcellular localization of neuronal nuclei (NeuN) antigen in size
            and calcitonin gene-related peptide (CGRP) populations of dorsal
            root ganglion (DRG) neurons during acute peripheral inflammation
  JOURNAL   Neurosci Lett 760, 135974 (2021)
   PUBMED   34146639
  REMARK    GeneRIF: Subcellular localization of neuronal nuclei (NeuN) antigen
            in size and calcitonin gene-related peptide (CGRP) populations of
            dorsal root ganglion (DRG) neurons during acute peripheral
            inflammation.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Du,Z., Zhang,H., Chen,Q., Gao,Y. and Sun,B.
  TITLE     Intranasal Calcitonin Gene-Related Peptide Protects Against Focal
            Cerebral Ischemic Injury in Rats Through the Wnt/beta-Catenin
            Pathway
  JOURNAL   Med Sci Monit 24, 8860-8869 (2018)
   PUBMED   30531687
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Zimatkin,S.M. and Karniushko,O.A.
  TITLE     [EXPRESSION OF DOUBLECORTIN AND NeuN IN THE DEVELOPING CEREBELLAR
            NEURONS IN RAT]
  JOURNAL   Morfologiia 149 (1), 38-42 (2016)
   PUBMED   27487661
  REMARK    GeneRIF: EXPRESSION OF DOUBLECORTIN AND NeuN IN THE DEVELOPING
            CEREBELLAR NEURONS IN RAT
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Jakovcevski,M., Ruan,H., Shen,E.Y., Dincer,A., Javidfar,B., Ma,Q.,
            Peter,C.J., Cheung,I., Mitchell,A.C., Jiang,Y., Lin,C.L.,
            Pothula,V., Stewart,A.F., Ernst,P., Yao,W.D. and Akbarian,S.
  TITLE     Neuronal Kmt2a/Mll1 histone methyltransferase is essential for
            prefrontal synaptic plasticity and working memory
  JOURNAL   J Neurosci 35 (13), 5097-5108 (2015)
   PUBMED   25834037
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Korzhevskiy,D.E., Beznin,G.V., Kolos,Y.A. and Kirik,V.
  TITLE     [CYTOPLASMIC LOCALIZATION OF NEUN/Fox-3 NUCLEAR PROTEIN IN THE
            PANCREATIC CELLS]
  JOURNAL   Morfologiia 148 (5), 88-90 (2015)
   PUBMED   26987225
  REMARK    GeneRIF: the presence of NeuN protein in the secretory epithelial
            cells of the exocrine part of this organ. The protein was located
            in the apical part of the cytoplasm slightly below the zone of
            zymogen granules.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Marcal,N., Patel,H., Dong,Z., Belanger-Jasmin,S., Hoffman,B.,
            Helgason,C.D., Dang,J. and Stifani,S.
  TITLE     Antagonistic effects of Grg6 and Groucho/TLE on the transcription
            repression activity of brain factor 1/FoxG1 and cortical neuron
            differentiation
  JOURNAL   Mol Cell Biol 25 (24), 10916-10929 (2005)
   PUBMED   16314515
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Franke,H., Klimke,K., Brinckmann,U., Grosche,J., Francke,M.,
            Sperlagh,B., Reichenbach,A., Liebert,U.G. and Illes,P.
  TITLE     P2X(7) receptor-mRNA and -protein in the mouse retina; changes
            during retinal degeneration in BALBCrds mice
  JOURNAL   Neurochem Int 47 (4), 235-242 (2005)
   PUBMED   15964665
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Feng,R., Wang,H., Wang,J., Shrom,D., Zeng,X. and Tsien,J.Z.
  TITLE     Forebrain degeneration and ventricle enlargement caused by double
            knockout of Alzheimer's presenilin-1 and presenilin-2
  JOURNAL   Proc Natl Acad Sci U S A 101 (21), 8162-8167 (2004)
   PUBMED   15148382
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Arvidsson,A., Collin,T., Kirik,D., Kokaia,Z. and Lindvall,O.
  TITLE     Neuronal replacement from endogenous precursors in the adult brain
            after stroke
  JOURNAL   Nat Med 8 (9), 963-970 (2002)
   PUBMED   12161747
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Mullen,R.J., Buck,C.R. and Smith,A.M.
  TITLE     NeuN, a neuronal specific nuclear protein in vertebrates
  JOURNAL   Development 116 (1), 201-211 (1992)
   PUBMED   1483388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.65413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..328
                     /product="RNA binding protein fox-1 homolog 3 isoform 1"
                     /note="fox-1 homolog C; neuronal nuclei;
                     hexaribonucleotide binding protein 3; RNA binding protein,
                     fox-1 homolog 3"
                     /calculated_mol_wt=35481
     Region          <25..170
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Region          99..174
                     /region_name="RRM_FOX1_like"
                     /note="RNA recognition motif (RRM) found in vertebrate RNA
                     binding protein fox-1 homologs and similar proteins;
                     cd12407"
                     /db_xref="CDD:409841"
     Site            order(100,102,104..109,129..133,135..140,142,166,171..174)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409841"
     Region          208..299
                     /region_name="Fox-1_C"
                     /note="Calcitonin gene-related peptide regulator C
                     terminal; pfam12414"
                     /db_xref="CDD:463568"
     CDS             1..328
                     /gene="Rbfox3"
                     /gene_synonym="Hrnbp3; Neun; RGD1560070"
                     /coded_by="NM_001413230.2:582..1568"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:287847"
                     /db_xref="RGD:1560070"
ORIGIN      
        1 maqpyppaqy ppppqngipa eyapppphpt qdysgqtpvp pehgmtlytp aqthpeqpgt
       61 eastqpiagt qtvpqadeaa qtdsqqlhps dptekqqpkr lhvsnipfrf rdpdlrqmfg
      121 qfgkildvei ifnergskgf gfvtfetssd adrareklng tivegrkiev nnatarvmtn
      181 kkpgnpyang wklnpvvgav ygpefyavts fpypttgtav ayrgahlrgr gravyntfra
      241 apppppipty gavvyqdgfy gaeiyggyaa yryaqpaaaa aaaaysdsyg rvyaaadpyh
      301 htigptatys igtmaslcrg gysrftpy
//
LOCUS       NP_001257783             461 aa            linear   ROD 28-APR-2025
DEFINITION  thyroid hormone receptor beta isoform 2 [Rattus norvegicus].
ACCESSION   NP_001257783
VERSION     NP_001257783.1
DBSOURCE    REFSEQ: accession NM_001270854.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Mukherjee,S., Dasgupta,S., Adhikari,U. and Panja,S.S.
  TITLE     Molecular modeling and molecular dynamics simulation studies on
            thyroid hormone receptor from Rattus norvegicus: role of conserved
            water molecules
  JOURNAL   J Mol Model 27 (5), 126 (2021)
   PUBMED   33834296
  REMARK    GeneRIF: Molecular modeling and molecular dynamics simulation
            studies on thyroid hormone receptor from Rattus norvegicus: role of
            conserved water molecules.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Fernandez,M., Pannella,M., Baldassarro,V.A., Flagelli,A.,
            Alastra,G., Giardino,L. and Calza,L.
  TITLE     Thyroid Hormone Signaling in Embryonic Stem Cells: Crosstalk with
            the Retinoic Acid Pathway
  JOURNAL   Int J Mol Sci 21 (23), 8945 (2020)
   PUBMED   33255695
  REMARK    GeneRIF: Thyroid Hormone Signaling in Embryonic Stem Cells:
            Crosstalk with the Retinoic Acid Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Leach,P.T., Kenney,J.W., Connor,D.A. and Gould,T.J.
  TITLE     Thyroid receptor beta involvement in the effects of acute nicotine
            on hippocampus-dependent memory
  JOURNAL   Neuropharmacology 93, 155-163 (2015)
   PUBMED   25666034
  REMARK    GeneRIF: This study demonstrated that Thyroid receptor beta
            involvement in the effects of acute nicotine on
            hippocampus-dependent memory
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Frau,C., Loi,R., Petrelli,A., Perra,A., Menegon,S., Kowalik,M.A.,
            Pinna,S., Leoni,V.P., Fornari,F., Gramantieri,L.,
            Ledda-Columbano,G.M., Giordano,S. and Columbano,A.
  TITLE     Local hypothyroidism favors the progression of preneoplastic
            lesions to hepatocellular carcinoma in rats
  JOURNAL   Hepatology 61 (1), 249-259 (2015)
   PUBMED   25156012
  REMARK    GeneRIF: down-regulated in hepatocellular carcinoma
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Sharma,P., Thakran,S., Deng,X., Elam,M.B. and Park,E.A.
  TITLE     Nuclear corepressors mediate the repression of phospholipase A2
            group IIa gene transcription by thyroid hormone
  JOURNAL   J Biol Chem 288 (23), 16321-16333 (2013)
   PUBMED   23629656
  REMARK    GeneRIF: a novel inverse recruitment mechanism in which liganded
            TRbeta recruits corepressors to inhibit PLA2g2a expression.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Horlein,A.J., Naar,A.M., Heinzel,T., Torchia,J., Gloss,B.,
            Kurokawa,R., Ryan,A., Kamei,Y., Soderstrom,M., Glass,C.K. et al.
  TITLE     Ligand-independent repression by the thyroid hormone receptor
            mediated by a nuclear receptor co-repressor
  JOURNAL   Nature 377 (6548), 397-404 (1995)
   PUBMED   7566114
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Ali,I.U., Lidereau,R. and Callahan,R.
  TITLE     Presence of two members of c-erbA receptor gene family (c-erbA beta
            and c-erbA2) in smallest region of somatic homozygosity on
            chromosome 3p21-p25 in human breast carcinoma
  JOURNAL   J Natl Cancer Inst 81 (23), 1815-1820 (1989)
   PUBMED   2573734
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Hodin,R.A., Lazar,M.A., Wintman,B.I., Darling,D.S., Koenig,R.J.,
            Larsen,P.R., Moore,D.D. and Chin,W.W.
  TITLE     Identification of a thyroid hormone receptor that is
            pituitary-specific
  JOURNAL   Science 244 (4900), 76-79 (1989)
   PUBMED   2539642
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Murray,M.B., Zilz,N.D., McCreary,N.L., MacDonald,M.J. and
            Towle,H.C.
  TITLE     Isolation and characterization of rat cDNA clones for two distinct
            thyroid hormone receptors
  JOURNAL   J Biol Chem 263 (25), 12770-12777 (1988)
   PUBMED   2457590
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Koenig,R.J., Warne,R.L., Brent,G.A., Harney,J.W., Larsen,P.R. and
            Moore,D.D.
  TITLE     Isolation of a cDNA clone encoding a biologically active thyroid
            hormone receptor
  JOURNAL   Proc Natl Acad Sci U S A 85 (14), 5031-5035 (1988)
   PUBMED   2899322
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J03933.1, J03819.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p16"
     Protein         1..461
                     /product="thyroid hormone receptor beta isoform 2"
                     /note="thyroid hormone receptor, beta (avian
                     erythroblastic leukemia viral (v-erb-a) oncogene homolog
                     2); TRbeta2Delta; thyroid hormone receptor beta2delta;
                     nuclear receptor subfamily 1 group A member 2; thyroid
                     hormone receptor beta 3"
                     /calculated_mol_wt=52426
     Region          1..106
                     /region_name="Modulating"
                     /note="propagated from UniProtKB/Swiss-Prot (P18113.2)"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18113.2)"
     Region          106..192
                     /region_name="NR_DBD_TR"
                     /note="DNA-binding domain of thyroid hormone receptors
                     (TRs) is composed of two C4-type zinc fingers; cd06961"
                     /db_xref="CDD:143519"
     Site            order(107,110,124,127,145,151,161,164)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143519"
     Site            order(117..119,125..126,128,130,132..133,136,158..159,162,
                     165,178..180,185,188..189,191..192)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143519"
     Site            order(117,120,175,177..178)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:143519"
     Region          216..458
                     /region_name="NR_LBD_TR"
                     /note="The ligand binding domain of thyroid hormone
                     receptor, a members of a superfamily of nuclear receptors;
                     cd06935"
                     /db_xref="CDD:132733"
     Region          244..461
                     /region_name="Interaction with NR2F6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P18113.2)"
     Site            order(269,272..273,275..276,279,282,310,313,317,329..331,
                     341,344,346,353,435,442,455)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132733"
     Site            order(281,284,288,298,302,305,453..454,457)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132733"
     Site            order(348,393,423,426..427,430,433..434,436..437)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132733"
     CDS             1..461
                     /gene="Thrb"
                     /gene_synonym="c-erbA-2; C-erba-beta; ERBA2; Nr1a2;
                     RATT3REC; T3rec; TRbeta"
                     /coded_by="NM_001270854.1:254..1639"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24831"
                     /db_xref="RGD:3858"
ORIGIN      
        1 mtpnsmteng lpawdkqkph pdrgqdwklv gmseaclhrk shverrgalk neqtsshliq
       61 atwassifhl dpddvndqsv ssaqtfqtee kkckgyipsy ldkdelcvvc gdkatgyhyr
      121 citcegckgf frrtiqkslh psysckyegk ciidkvtrnq cqecrfkkci yvgmatdlvl
      181 ddskrlakrk lieenrekrr reelqksigh kpeptdeewe liktvteahv atnaqgshwk
      241 qkrkflpedi gqapivnape ggkvdleafs hftkiitpai trvvdfakkl pmfcelpced
      301 qiillkgccm eimslraavr ydpdsetltl ngemavtrgq lkngglgvvs daifdlgmsl
      361 ssfnlddtev allqavllms sdrpglacve riekyqdsfl lafehyinyr khhvthfwpk
      421 llmkvtdlrm igachasrfl hmkvecptel fpplflevfe d
//
LOCUS       NP_001387558             290 aa            linear   ROD 28-APR-2025
DEFINITION  insulin-like growth factor-binding protein 3 receptor isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001387558 XP_038957133
VERSION     NP_001387558.1
DBSOURCE    REFSEQ: accession NM_001400629.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 26, 2022 this sequence version replaced XP_038957133.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1451660.1,
                                           SRR26360176.165554.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36-q37"
     Protein         1..290
                     /product="insulin-like growth factor-binding protein 3
                     receptor isoform 2"
                     /note="insulin-like growth factor-binding protein 3
                     receptor"
                     /calculated_mol_wt=30895
     Region          99..219
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     CDS             1..290
                     /gene="Tmem219"
                     /gene_synonym="RGD1560566"
                     /coded_by="NM_001400629.1:30..902"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:308986"
                     /db_xref="RGD:1560566"
ORIGIN      
        1 mrvwtdwgga vagararagp aprraahdvt grrsppgckr hsteaqtpll pmgscqaghn
       61 lhlclahhpp lvcatlilll lglsglglgg fllthttglr spdipqdwvt flrsfgqlsl
      121 cpmnetvtgk wqgphvvgll ttlnfggdpd rnktqtfqam ipgsqigfke iagesvlvta
      181 rvasgrtpgt clyfsgipki lpssqppisc seegagnatl spmmgeecvi vwsherfvlt
      241 klltseelal cgsrllvlgs flvllcgflc cataacfhpr pefhwsrarl
//
LOCUS       NP_001014810             303 aa            linear   ROD 28-APR-2025
DEFINITION  protein YIF1B isoform b [Rattus norvegicus].
ACCESSION   NP_001014810
VERSION     NP_001014810.1
DBSOURCE    REFSEQ: accession NM_001014810.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Alterio,J., Masson,J., Diaz,J., Chachlaki,K., Salman,H., Areias,J.,
            Al Awabdh,S., Emerit,M.B. and Darmon,M.
  TITLE     Yif1B Is Involved in the Anterograde Traffic Pathway and the Golgi
            Architecture
  JOURNAL   Traffic 16 (9), 978-993 (2015)
   PUBMED   26077767
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Al Awabdh,S., Miserey-Lenkei,S., Bouceba,T., Masson,J., Kano,F.,
            Marinach-Patrice,C., Hamon,M., Emerit,M.B. and Darmon,M.
  TITLE     A new vesicular scaffolding complex mediates the G-protein-coupled
            5-HT1A receptor targeting to neuronal dendrites
  JOURNAL   J Neurosci 32 (41), 14227-14241 (2012)
   PUBMED   23055492
  REMARK    GeneRIF: A new protein trafficking pathway model is proposed in
            which Yif1B is the scaffold protein recruiting the 5-HT1A receptor
            complex.
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Carrel,D., Masson,J., Al Awabdh,S., Capra,C.B., Lenkei,Z.,
            Hamon,M., Emerit,M.B. and Darmon,M.
  TITLE     Targeting of the 5-HT1A serotonin receptor to neuronal dendrites is
            mediated by Yif1B
  JOURNAL   J Neurosci 28 (32), 8063-8073 (2008)
   PUBMED   18685031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.975611.1,
                                           SRR22399489.44302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..303
                     /product="protein YIF1B isoform b"
                     /note="protein YIF1B; YIP1-interacting factor homolog B"
                     /calculated_mol_wt=33022
     Region          65..298
                     /region_name="YIF1"
                     /note="pfam03878"
                     /db_xref="CDD:461081"
     CDS             1..303
                     /gene="Yif1b"
                     /gene_synonym="Yip1b"
                     /coded_by="NM_001014810.2:123..1034"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:292768"
                     /db_xref="RGD:735199"
ORIGIN      
        1 mprpgrgria askrrvpvsq pgmadphqff ddtssapsrg yggqpspgsl gyptssseaa
       61 flaapmsnma maygsslaaq gkelvdknid rfipvsklky yfavdtvyvg kklgllvfpy
      121 lhqdwevqyq qdtpvaprfd inapdlyipa mafityilva glalgtqdrf spdllglqas
      181 salawltlev vaillslylv tvntdlttid lvaflgykyv gmiggvltgl lfgkigyylv
      241 lawccvsifv fmirtlrlki laqaaaegvp vrgarnqlrm yltmavaaaq pvlmywltfh
      301 lvr
//
LOCUS       NP_001424894             911 aa            linear   ROD 28-APR-2025
DEFINITION  tight junction protein ZO-3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424894 XP_038934945
VERSION     NP_001424894.1
DBSOURCE    REFSEQ: accession NM_001437965.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Qiao,X., Roth,I., Feraille,E. and Hasler,U.
  TITLE     Different effects of ZO-1, ZO-2 and ZO-3 silencing on kidney
            collecting duct principal cell proliferation and adhesion
  JOURNAL   Cell Cycle 13 (19), 3059-3075 (2014)
   PUBMED   25486565
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Capaldo,C.T., Koch,S., Kwon,M., Laur,O., Parkos,C.A. and Nusrat,A.
  TITLE     Tight function zonula occludens-3 regulates cyclin D1-dependent
            cell proliferation
  JOURNAL   Mol Biol Cell 22 (10), 1677-1685 (2011)
   PUBMED   21411630
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Aho,S., Lupo,J., Coly,P.A., Sabine,A., Castellazzi,M., Morand,P.,
            Sergeant,A., Manet,E., Boyer,V. and Gruffat,H.
  TITLE     Characterization of the ubinuclein protein as a new member of the
            nuclear and adhesion complex components (NACos)
  JOURNAL   Biol Cell 101 (6), 319-334 (2009)
   PUBMED   18823282
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Adachi,M., Inoko,A., Hata,M., Furuse,K., Umeda,K., Itoh,M. and
            Tsukita,S.
  TITLE     Normal establishment of epithelial tight junctions in mice and
            cultured cells lacking expression of ZO-3, a tight-junction MAGUK
            protein
  JOURNAL   Mol Cell Biol 26 (23), 9003-9015 (2006)
   PUBMED   17000770
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Inoko,A., Itoh,M., Tamura,A., Matsuda,M., Furuse,M. and Tsukita,S.
  TITLE     Expression and distribution of ZO-3, a tight junction MAGUK
            protein, in mouse tissues
  JOURNAL   Genes Cells 8 (11), 837-845 (2003)
   PUBMED   14622136
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Unda,F.J., Perez-Nanclares,G., Le Morvan,V., Hernandez,C.,
            Vilaxa,A., De-la-Fuente,M. and Gorry,P.
  TITLE     Dynamic assembly of tight junction-associated proteins ZO-1, ZO-2,
            ZO-3 and occludin during mouse tooth development
  JOURNAL   Histol Histopathol 18 (1), 27-38 (2003)
   PUBMED   12507281
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Haskins,J., Gu,L., Wittchen,E.S., Hibbard,J. and Stevenson,B.R.
  TITLE     ZO-3, a novel member of the MAGUK protein family found at the tight
            junction, interacts with ZO-1 and occludin
  JOURNAL   J Cell Biol 141 (1), 199-208 (1998)
   PUBMED   9531559
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934945.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.29568.1,
                                           SRR26643291.19422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..911
                     /product="tight junction protein ZO-3 isoform 1"
                     /note="tight junction protein ZO-3"
                     /calculated_mol_wt=100088
     Region          19..100
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(30..36,49,52,80,84,87..88)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          194..272
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(194..200,205..221,224..226,229,231..232,239,
                     247..248,250..251,263..269)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(206..212,218,221,251,255,258..259)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          377..458
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(388..394,404,407,436,440,443..444)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          473..546
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(481,483,486,490,511..512,540,542..543)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          589..765
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..911
                     /gene="Tjp3"
                     /coded_by="NM_001437965.1:169..2904"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314640"
                     /db_xref="RGD:1309247"
ORIGIN      
        1 mavrfqvadm eeltiweqht atlykdprrg fgiavsgghd raggpvvvsd vvpggpaegr
       61 lqtgdhivmv ngvsvenvts afaiqilktc tktanitvkr prrvqlpatk aspasghqls
      121 dqeeadhgrg yegdsssgsg rswgersrrs ragrrvrmgs hgrrsscggs eangldlvsg
      181 ykrlpkqdvl mrplksvlvk rrnseefgvk lgsqifikhi tesglaarnr glqegdlilq
      241 ingvssanls lsdtrrliek segqltllvl rdsgqflvni ppavsdsdss lmedisdlts
      301 elsqappshi pppplksrrs pedsqtdspv etpqpqrrer svdsraiaep espgesrydi
      361 yrvpsrqsle drgyspdtrv vrfpkgvsig lrlaggndvg ifvsgvqags padgqgiqeg
      421 deilqvndmp frnltreeav qfllglpage dvelviqskq difrkmvqsr vgdsfyirth
      481 felepsppyg lgftrgdvfh vvdtlyrgsg sghghsshgg lwlaarmgrd lreqergvip
      541 nqsraeqlas leaaqraagl gpgastgsnp raefwrlrgl rrgakktmtq rsredlsalt
      601 rqghyppyer vvlreasfkr pvvilgpvad iamkrlttev peqfeiaesv srtdspskii
      661 kldtvrviae rdkhalldvt psaierlnyv qyypvvifca pesrsalkal rewlapasrr
      721 ssrrlyaqaq klqkhsghlf tatiplngts dswyqevkav iqqqqarpiw taedqlngss
      781 edldlpghgl aassgdlscd sransdyedt dgegtytdre gepqdfdeea pptalarsse
      841 pvwvddhqgl mghgriaaae vqadshytpd qrrqdsmrty khealrkkft rardiessde
      901 egydwgpatd l
//
LOCUS       NP_001101495             310 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein C14orf28 homolog [Rattus norvegicus].
ACCESSION   NP_001101495 XP_001080064 XP_234234
VERSION     NP_001101495.1
DBSOURCE    REFSEQ: accession NM_001108025.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473947.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234234.2, XP_001080064.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132266 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..310
                     /product="uncharacterized protein C14orf28 homolog"
                     /calculated_mol_wt=36267
     CDS             1..310
                     /gene="Dorip1"
                     /gene_synonym="C6h14orf28; RGD1307621"
                     /coded_by="NM_001108025.1:85..1017"
                     /db_xref="GeneID:314168"
                     /db_xref="RGD:1307621"
ORIGIN      
        1 mktlfeeika siknnynqdr sfwrpvlpwg gvftikagrk avsctplyve irlkntctid
       61 gflmllyvil nendnfprel slhfgrefvd cflylmdtys fttvkllwiw dkmekqqyks
      121 evhkaslvid lfgnehdnft knlenlmsti qesycsnwrc ptrvqedqqr tisinppqei
      181 phgnlirlav delfcskiel ceergcgglr efsqrvfchg appfvvlnmq hwksedlayv
      241 pyyldlsdhk yllegatlfn keehhysaaf qidghwmhyd glrnvnlill nkppefllls
      301 slvyiratek
//
LOCUS       NP_001425362             449 aa            linear   ROD 28-APR-2025
DEFINITION  activating transcription factor 7-interacting protein 2 isoform 4
            [Rattus norvegicus].
ACCESSION   NP_001425362 XP_006245794
VERSION     NP_001425362.1
DBSOURCE    REFSEQ: accession NM_001438433.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Apr 18, 2025 this sequence version replaced XP_006245794.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1415041.1,
                                           SRR26643293.61370.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q11"
     Protein         1..449
                     /product="activating transcription factor 7-interacting
                     protein 2 isoform 4"
                     /calculated_mol_wt=50342
     Region          59..267
                     /region_name="ATF7IP_BD"
                     /note="ATF-interacting protein binding domain; pfam16788"
                     /db_xref="CDD:465271"
     Region          342..439
                     /region_name="fn3_4"
                     /note="Fibronectin-III type domain; pfam16794"
                     /db_xref="CDD:465273"
     CDS             1..449
                     /gene="Atf7ip2"
                     /coded_by="NM_001438433.1:78..1427"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:497859"
                     /db_xref="RGD:1583744"
ORIGIN      
        1 mespdrkrrk vlkakktmpt scrkqmeiln qsknveapkt tvvtnipngh nqkmfsenke
       61 nvkvmktseq inenaceale rhtalleqvk hwirqeicti ncnlfdkkln elnerigktq
      121 crskheaiag elfikirrlq kriktvlssq gnclepntlp sntvckvtds vnlsvtqrsv
      181 ksqskrmssv nhtpfnssek asrkinlpsa cvefvsesnd dvmlisvenp nlttpiasdp
      241 teirkntsrn vssspnarse vvpvekkfdf vidltregls sysiespsft lkstskavlr
      301 skeiipvaen gnegfgsfeh lpplpeppap lpemadkiqd tlppqkpelk vkqvlrpssi
      361 altwnipkvn pkcapvesyh lflyyegsnh ltwkkvaeik alplpmactl sqmlastkyy
      421 favqskdifg rygpfcnikc ipgfsenlt
//
LOCUS       NP_001424624             705 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-1-like protein isoform 15 [Rattus norvegicus].
ACCESSION   NP_001424624 XP_038943828
VERSION     NP_001424624.1
DBSOURCE    REFSEQ: accession NM_001437695.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Chen,T., Yang,J., Zheng,Y., Zhou,X., Huang,H., Zhang,H. and Xu,Z.
  TITLE     ERK1/2 Regulates Epileptic Seizures by Modulating the DRP1-Mediated
            Mitochondrial Dynamic
  JOURNAL   Synapse 78 (5), e22309 (2024)
   PUBMED   39285628
  REMARK    GeneRIF: ERK1/2 Regulates Epileptic Seizures by Modulating the
            DRP1-Mediated Mitochondrial Dynamic.
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Sun,J., Shao,Y., Pei,L., Zhu,Q., Yu,X. and Yao,W.
  TITLE     AKAP1 alleviates VSMC phenotypic modulation and neointima formation
            by inhibiting Drp1-dependent mitochondrial fission
  JOURNAL   Biomed Pharmacother 176, 116858 (2024)
   PUBMED   38850669
  REMARK    GeneRIF: AKAP1 alleviates VSMC phenotypic modulation and neointima
            formation by inhibiting Drp1-dependent mitochondrial fission.
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Zhang,H., Chen,L., Li,J., Sun,J., Zhao,Q., Wang,S. and Li,G.
  TITLE     STAT3 phosphorylation at Tyr705 affects DRP1 (dynamin-related
            protein 1) controlled-mitochondrial fission during the development
            of apoptotic-resistance in pulmonary arterial endothelial cells
  JOURNAL   Genes Genomics 46 (7), 751-762 (2024)
   PUBMED   38733520
  REMARK    GeneRIF: STAT3 phosphorylation at Tyr705 affects DRP1
            (dynamin-related protein 1) controlled-mitochondrial fission during
            the development of apoptotic-resistance in pulmonary arterial
            endothelial cells.
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Dubois,M., Boulghobra,D., Rochebloine,G., Pallot,F., Yehya,M.,
            Bornard,I., Gayrard,S., Coste,F., Walther,G., Meyer,G.,
            Gaillard,J.C., Armengaud,J., Alpha-Bazin,B. and Reboul,C.
  TITLE     Hyperglycemia triggers RyR2-dependent alterations of mitochondrial
            calcium homeostasis in response to cardiac ischemia-reperfusion:
            Key role of DRP1 activation
  JOURNAL   Redox Biol 70, 103044 (2024)
   PUBMED   38266577
  REMARK    GeneRIF: Hyperglycemia triggers RyR2-dependent alterations of
            mitochondrial calcium homeostasis in response to cardiac
            ischemia-reperfusion: Key role of DRP1 activation.
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Fan,R.Z., Sportelli,C., Lai,Y., Salehe,S.S., Pinnell,J.R.,
            Brown,H.J., Richardson,J.R., Luo,S. and Tieu,K.
  TITLE     A partial Drp1 knockout improves autophagy flux independent of
            mitochondrial function
  JOURNAL   Mol Neurodegener 19 (1), 26 (2024)
   PUBMED   38504290
  REMARK    GeneRIF: A partial Drp1 knockout improves autophagy flux
            independent of mitochondrial function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Smirnova,E., Griparic,L., Shurland,D.L. and van der Bliek,A.M.
  TITLE     Dynamin-related protein Drp1 is required for mitochondrial division
            in mammalian cells
  JOURNAL   Mol Biol Cell 12 (8), 2245-2256 (2001)
   PUBMED   11514614
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Chen,C.H., Hwang,S.L., Howng,S.L., Chou,C.K. and Hong,Y.R.
  TITLE     Three rat brain alternative splicing dynamin-like protein variants:
            interaction with the glycogen synthase kinase 3beta and action as a
            substrate
  JOURNAL   Biochem Biophys Res Commun 268 (3), 893-898 (2000)
   PUBMED   10679301
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Pitts,K.R., Yoon,Y., Krueger,E.W. and McNiven,M.A.
  TITLE     The dynamin-like protein DLP1 is essential for normal distribution
            and morphology of the endoplasmic reticulum and mitochondria in
            mammalian cells
  JOURNAL   Mol Biol Cell 10 (12), 4403-4417 (1999)
   PUBMED   10588666
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Imoto,M., Tachibana,I. and Urrutia,R.
  TITLE     Identification and functional characterization of a novel human
            protein highly related to the yeast dynamin-like GTPase Vps1p
  JOURNAL   J Cell Sci 111 (Pt 10), 1341-1349 (1998)
   PUBMED   9570752
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Yoon,Y., Pitts,K.R., Dahan,S. and McNiven,M.A.
  TITLE     A novel dynamin-like protein associates with cytoplasmic vesicles
            and tubules of the endoplasmic reticulum in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 779-793 (1998)
   PUBMED   9472031
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Apr 9, 2025 this sequence version replaced XP_038943828.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.30246.1,
                                           SRR26643289.31606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..705
                     /product="dynamin-1-like protein isoform 15"
                     /EC_number="3.6.5.5"
                     /note="dynamin-1-like protein; N-terminal region;
                     dynamin-like protein 1; C-terminal region; dynamin-related
                     protein 1"
                     /calculated_mol_wt=78452
     Region          23..302
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(33,35..40,53..54,59,146,216,218..219,245..249,252)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(34..35,150,163,188,190,192..195,197..198,219,
                     221..224,248..250)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            59
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            63..65
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            146..149
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(148..149,179..180)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            215..218
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          225..510
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            245..247
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          609..699
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     CDS             1..705
                     /gene="Dnm1l"
                     /gene_synonym="DLP1; Dnml1; Drp1"
                     /coded_by="NM_001437695.1:135..2252"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:114114"
                     /db_xref="RGD:620416"
ORIGIN      
        1 mealipvink lqdvfntvga diiqlpqivv vgtqssgkss vleslvgrdl lprgtgvvtr
       61 rplilqlvhv spedkrkttg eengveaeew gkflhtknkl ytdfdeirqe ieneterisg
      121 nnkgvspepi hlkvfspnvv nltlvdlpgm tkvpvgdqpk dielqireli lrfisnpnsi
      181 ilavtaantd matsealkis revdpdgrrt lavitkldlm dagtdamdvl mgrvipvklg
      241 iigvvnrsql dinnkksvtd sirdeyaflq kkypslanrn gtkylartln rllmhhirdc
      301 lpelktrinv laaqyqslln sygepvddks atllqlitkf ateycntieg takyietsel
      361 cggaricyif hetfgrtles vdplgglnti diltairnat gprpalfvpe vsfellvkrq
      421 ikrleepslr cvelvheemq riiqhcsnys tqellrfpkl hdaivevvtc llrkrlpvtn
      481 emvhnlvaie layintkhpd fadacglmnn nieeqrrnrl arelpsavsr dkvasagggi
      541 gdggrigdgg qepttgnwrg mlktskaeel laeekskpip impaspqkgh avnlldvpvp
      601 varklsareq rdcevierli ksyflivrkn iqdsvpkavm hflvnhvkdt lqselvgqly
      661 kssllddllt esedmaqrrk eaadmlkalq gasqiiaeir ethlw
//
LOCUS       NP_001257642             398 aa            linear   ROD 28-APR-2025
DEFINITION  B2 bradykinin receptor isoform 1 [Rattus norvegicus].
ACCESSION   NP_001257642
VERSION     NP_001257642.1
DBSOURCE    REFSEQ: accession NM_001270713.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Shen,M., Yu,M., Qiu,C., Zhang,G., Li,J., Fang,W. and Wang,Q.
  TITLE     Myocardial angiogenesis induced by exercise training involves a
            regulatory mechanism mediated by kinin receptors
  JOURNAL   Clin Exp Hypertens 43 (5), 408-415 (2021)
   PUBMED   33687297
  REMARK    GeneRIF: Myocardial angiogenesis induced by exercise training
            involves a regulatory mechanism mediated by kinin receptors.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Dagher,O.K., Jaffa,M.A., Habib,A., Ziyadeh,F.N. and Jaffa,A.A.
  TITLE     Heteromerization fingerprints between bradykinin B2 and thromboxane
            TP receptors in native cells
  JOURNAL   PLoS One 14 (5), e0216908 (2019)
   PUBMED   31086419
  REMARK    GeneRIF: This is the first study that provides evidence supporting
            the existence of bradykinin receptor B2 - thromboxane TP receptors
            heteromerization fingerprints in primary cultured vascular smooth
            muscle cell.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Ma,Z., Dong,Q., Lyu,B., Wang,J., Quan,Y. and Gong,S.
  TITLE     The expression of bradykinin and its receptors in spinal cord
            ischemia-reperfusion injury rat model
  JOURNAL   Life Sci 218, 340-345 (2019)
   PUBMED   30580020
  REMARK    GeneRIF: High bradykinin receptor B2 expression is associated with
            spinal cord ischemia-reperfusion injury.
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Sanguesa,G., Shaligram,S., Akther,F., Roglans,N., Laguna,J.C.,
            Rahimian,R. and Alegret,M.
  TITLE     Type of supplemented simple sugar, not merely calorie intake,
            determines adverse effects on metabolism and aortic function in
            female rats
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (2), H289-H304 (2017)
   PUBMED   27923787
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Siltari,A., Korpela,R. and Vapaatalo,H.
  TITLE     Bradykinin -induced vasodilatation: Role of age, ACE1-inhibitory
            peptide, mas- and bradykinin receptors
  JOURNAL   Peptides 85, 46-55 (2016)
   PUBMED   27628189
  REMARK    GeneRIF: Mas receptor antagonist abolished relaxation while
            bradykinin receptor antagonist only slightly reduced it, suggesting
            that bradykinin-induced vasorelaxation is regulated also by other
            mechanisms than the classical BR1/BR2 pathway.
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Feletou,M., Lonchampt,M., Robineau,P., Jamonneau,I., Thurieau,C.,
            Fauchere,J.L., Villa,P., Ghezzi,P., Prost,J.F. and Canet,E.
  TITLE     Effects of the bradykinin B2 receptor antagonist S 16118
            (p-guanidobenzoyl-[Hyp3,Thi5,D-Tic7,Oic8]bradykinin) in different
            in vivo animal models of inflammation
  JOURNAL   J Pharmacol Exp Ther 273 (3), 1078-1084 (1995)
   PUBMED   7791078
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Pesquero,J.B., Lindsey,C.J., Zeh,K., Paiva,A.C., Ganten,D. and
            Bader,M.
  TITLE     Molecular structure and expression of rat bradykinin B2 receptor
            gene. Evidence for alternative splicing
  JOURNAL   J Biol Chem 269 (43), 26920-26925 (1994)
   PUBMED   7929432
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Wang,D.Z., Ma,J.X., Chao,L. and Chao,J.
  TITLE     Molecular cloning and sequence analysis of rat bradykinin B2
            receptor gene
  JOURNAL   Biochim Biophys Acta 1219 (1), 171-174 (1994)
   PUBMED   8086459
REFERENCE   9  (residues 1 to 398)
  AUTHORS   McEachern,A.E., Shelton,E.R., Bhakta,S., Obernolte,R., Bach,C.,
            Zuppan,P., Fujisaki,J., Aldrich,R.W. and Jarnagin,K.
  TITLE     Expression cloning of a rat B2 bradykinin receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7724-7728 (1991)
   PUBMED   1715575
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Rajakulasingam,K., Polosa,R., Holgate,S.T. and Howarth,P.H.
  TITLE     Comparative nasal effects of bradykinin, kallidin and
            [Des-Arg9]-bradykinin in atopic rhinitic and normal volunteers
  JOURNAL   J Physiol 437, 577-587 (1991)
   PUBMED   1890650
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M59967.2 and JAXUCZ010000006.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M59967.2, SRR26643298.36952.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMN09345238
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..398
                     /product="B2 bradykinin receptor isoform 1"
                     /note="B2 bradykinin receptor; B2R; BK-2 receptor;
                     bradykinin receptor, beta 2"
                     /calculated_mol_wt=45060
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Region          66..350
                     /region_name="7tmA_BK-2"
                     /note="bradykinin receptor B2, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15381"
                     /db_xref="CDD:320503"
     Region          66..92
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320503"
     Site            68..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Site            order(71,120,123..124,128,141,144..145,148,199,203,220,
                     290,293,325,329)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320503"
     Region          99..124
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320503"
     Site            101..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Region          137..167
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320503"
     Site            139..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Region          180..201
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320503"
     Site            183..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Region          228..257
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320503"
     Site            229..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Region          270..300
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320503"
     Site            275..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Region          318..343
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320503"
     Site            319..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25023.4)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GRK6.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GRK6.
                     /evidence=ECO:0000269|PubMed:10085087; propagated from
                     UniProtKB/Swiss-Prot (P25023.4)"
     CDS             1..398
                     /gene="Bdkrb2"
                     /gene_synonym="B2BKR; B2BRA"
                     /coded_by="NM_001270713.2:267..1463"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25245"
                     /db_xref="RGD:2201"
ORIGIN      
        1 mdtrsslcpk tqavvevamf wgpgchlstc iemfnittqa lgsahngtfs evncpdteww
       61 swlnaiqapf lwvlfllaal enifvlsvfc lhktnctvae iylgnlaaad lilacglpfw
      121 aitiannfdw lfgevlcrvv ntmiymnlys sicflmlvsi drylalvktm smgrmrgvrw
      181 aklyslviws ctlllsspml vfrtmkdyre eghnvtacvi vypsrswevf tnmllnlvgf
      241 llplsiitfc tvrimqvlrn nemkkfkevq tekkatvlvl avlglfvlcw fpfqistfld
      301 tllrlgvlsg cwneravdiv tqissyvays nsclnplvyv ivgkrfrkks revyqaicrk
      361 ggcmgesvqm ensmgtlrts isvdrqihkl qdwagnkq
//
LOCUS       NP_001418611             328 aa            linear   ROD 28-APR-2025
DEFINITION  neuronal membrane glycoprotein M6-b isoform 1 [Rattus norvegicus].
ACCESSION   NP_001418611 XP_006256911
VERSION     NP_001418611.1
DBSOURCE    REFSEQ: accession NM_001431682.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Bang,M.L., Vainshtein,A., Yang,H.J., Eshed-Eisenbach,Y., Devaux,J.,
            Werner,H.B. and Peles,E.
  TITLE     Glial M6B stabilizes the axonal membrane at peripheral nodes of
            Ranvier
  JOURNAL   Glia 66 (4), 801-812 (2018)
   PUBMED   29282769
  REMARK    GeneRIF: Study identified glycoprotein M6B as a Schwann cell
            microvilli component of peripheral nodes of Ranvier. Study detected
            Na(+) channel clusters at heminodes without any associated M6B,
            indicating that it is not required for initial channel clustering;
            showed that absence of M6B results in progressive appearance of
            nodal protrusions of the nodal axolemma, that are often accompanied
            by the presence of enlarged mitochondria.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Drabek,K., van de Peppel,J., Eijken,M. and van Leeuwen,J.P.
  TITLE     GPM6B regulates osteoblast function and induction of mineralization
            by controlling cytoskeleton and matrix vesicle release
  JOURNAL   J Bone Miner Res 26 (9), 2045-2051 (2011)
   PUBMED   21638316
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Fjorback,A.W., Muller,H.K. and Wiborg,O.
  TITLE     Membrane glycoprotein M6B interacts with the human serotonin
            transporter
  JOURNAL   J Mol Neurosci 37 (3), 191-200 (2009)
   PUBMED   18581270
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Shimokawa,N. and Miura,M.
  TITLE     Rhombex-29, a novel gene of the PLP/DM20-M6 family cloned from rat
            medulla oblongata by differential display
  JOURNAL   J Neurosci Res 62 (1), 1-8 (2000)
   PUBMED   11002282
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Yan,Y., Lagenaur,C. and Narayanan,V.
  TITLE     Molecular cloning of M6: identification of a PLP/DM20 gene family
  JOURNAL   Neuron 11 (3), 423-431 (1993)
   PUBMED   8398137
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 19, 2024 this sequence version replaced XP_006256911.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.31541.1,
                                           SRR26360194.2531519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840108, SAMN12840110
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq13-q14"
     Protein         1..328
                     /product="neuronal membrane glycoprotein M6-b isoform 1"
                     /note="neuronal membrane glycoprotein M6-b; Rhombex-29;
                     rhombencephalic expression protein-29 kDa"
                     /calculated_mol_wt=36066
     Region          63..298
                     /region_name="Myelin_PLP"
                     /note="Myelin proteolipid protein (PLP or lipophilin);
                     pfam01275"
                     /db_xref="CDD:460144"
     CDS             1..328
                     /gene="Gpm6b"
                     /gene_synonym="M6b"
                     /coded_by="NM_001431682.1:243..1229"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:192179"
                     /db_xref="RGD:620580"
ORIGIN      
        1 mkpametaae enteqsqerk vnsraemeig ryhwmypgsk nhqyrpvptl gdragplssp
       61 gcfeccikcl ggvpyaslva tilcfsgval fcgcghvala gtvaileqhf stntsdhall
      121 seviqlmqyv iygiasfffl ygiillaegf yttsavkelh gefkttacgr cisgmfvflt
      181 yvlgvawlgv fgfsavpvfm fyniwstcev ikspqsngts gveqicvdvr qygiipwnaf
      241 pgkicgsale nicntnefym syhlfivaca gagatviali hflmilssnw aylkdaskmq
      301 ayqdikakee qelqdiqsrs keqlnsyt
//
LOCUS       NP_001102954             151 aa            linear   ROD 28-APR-2025
DEFINITION  myosin light polypeptide 6 [Rattus norvegicus].
ACCESSION   NP_001102954 NP_001094453 XP_001065562
VERSION     NP_001102954.1
DBSOURCE    REFSEQ: accession NM_001109484.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Revenu,C., Ubelmann,F., Hurbain,I., El-Marjou,F., Dingli,F.,
            Loew,D., Delacour,D., Gilet,J., Brot-Laroche,E., Rivero,F.,
            Louvard,D. and Robine,S.
  TITLE     A new role for the architecture of microvillar actin bundles in
            apical retention of membrane proteins
  JOURNAL   Mol Biol Cell 23 (2), 324-336 (2012)
   PUBMED   22114352
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Kesimer,M., Scull,M., Brighton,B., DeMaria,G., Burns,K., O'Neal,W.,
            Pickles,R.J. and Sheehan,J.K.
  TITLE     Characterization of exosome-like vesicles released from human
            tracheobronchial ciliated epithelium: a possible role in innate
            defense
  JOURNAL   FASEB J 23 (6), 1858-1868 (2009)
   PUBMED   19190083
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Fu,Z.Y., Xie,B.T., Ma,Y.T. and Gong,Z.X.
  TITLE     Preparation of monoclonal antibodies against human ventricular
            myosin light chain 1 (HVMLC1) for functional studies
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 38 (9), 625-632 (2006)
   PUBMED   16953301
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Iwai,N., Shimoike,H. and Kinoshita,M.
  TITLE     Genes up-regulated in hypertrophied ventricle
  JOURNAL   Biochem Biophys Res Commun 209 (2), 527-534 (1995)
   PUBMED   7733921
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Hailstones,D.L. and Gunning,P.W.
  TITLE     Characterization of human myosin light chains 1sa and 3nm:
            implications for isoform evolution and function
  JOURNAL   Mol Cell Biol 10 (3), 1095-1104 (1990)
   PUBMED   2304459
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474104.2.
            
            On or before Aug 31, 2021 this sequence version replaced
            NP_001094453.2, XP_001065562.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5756307,
                              SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..151
                     /product="myosin light polypeptide 6"
                     /note="myosin, light chain 6, alkali, smooth muscle and
                     non-muscle; myosin, light polypeptide 6, alkali, smooth
                     muscle and non-muscle-like; non-muscle myosin alkali light
                     chain; myosin light chain 3; myosin light chain alkali 3;
                     smooth muscle and nonmuscle myosin light chain alkali 6;
                     myosin light chain A3; 17 kDa myosin light chain"
                     /calculated_mol_wt=16830
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine.
                     /evidence=ECO:0000250|UniProtKB:P60660; propagated from
                     UniProtKB/Swiss-Prot (Q64119.3)"
     Region          5..149
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60660; propagated from
                     UniProtKB/Swiss-Prot (Q64119.3)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60660; propagated from
                     UniProtKB/Swiss-Prot (Q64119.3)"
     CDS             1..151
                     /gene="Myl6"
                     /gene_synonym="LC17; MLC-3; Myl6l"
                     /coded_by="NM_001109484.1:69..524"
                     /db_xref="GeneID:685867"
                     /db_xref="RGD:1589019"
ORIGIN      
        1 mcdftedqta efkeafqlfd rtgdgkilys qcgdvmralg qnptnaevlk vlgnpksdem
       61 nvkvldfehf lpmlqtvakn kdqgtyedyv eglrvfdkeg ngtvmgaeir hvlvtlgekm
      121 teeevemlva ghedsngcin yeelvrmvln g
//
LOCUS       NP_001120851             504 aa            linear   ROD 28-APR-2025
DEFINITION  apoptosis inhibitor 5 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001120851 XP_001071044 XP_342471
VERSION     NP_001120851.1
DBSOURCE    REFSEQ: accession NM_001127379.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Van den Berghe,L., Laurell,H., Huez,I., Zanibellato,C., Prats,H.
            and Bugler,B.
  TITLE     FIF [fibroblast growth factor-2 (FGF-2)-interacting-factor], a
            nuclear putatively antiapoptotic factor, interacts specifically
            with FGF-2
  JOURNAL   Mol Endocrinol 14 (11), 1709-1724 (2000)
   PUBMED   11075807
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Kim,J.W., Cho,H.S., Kim,J.H., Hur,S.Y., Kim,T.E., Lee,J.M.,
            Kim,I.K. and Namkoong,S.E.
  TITLE     AAC-11 overexpression induces invasion and protects cervical cancer
            cells from apoptosis
  JOURNAL   Lab Invest 80 (4), 587-594 (2000)
   PUBMED   10780674
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Tewari,M., Yu,M., Ross,B., Dean,C., Giordano,A. and Rubin,R.
  TITLE     AAC-11, a novel cDNA that inhibits apoptosis after growth factor
            withdrawal
  JOURNAL   Cancer Res 57 (18), 4063-4069 (1997)
   PUBMED   9307294
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before May 17, 2008 this sequence version replaced
            XP_342471.3, XP_001071044.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC162003.1, SRR22582416.1261102.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q31"
     Protein         1..504
                     /product="apoptosis inhibitor 5 isoform 2"
                     /calculated_mol_wt=56654
     Region          4..503
                     /region_name="API5"
                     /note="Apoptosis inhibitory protein 5 (API5); pfam05918"
                     /db_xref="CDD:428672"
     Region          63..91
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          97..139
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..504
                     /gene="Api5"
                     /coded_by="NM_001127379.2:154..1668"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:362170"
                     /db_xref="RGD:1309772"
ORIGIN      
        1 mptveelyrn ygiladateq vgqhkdayqv ildgvkggtk ekrlaaqfip kffkhfpela
       61 dsainaqldl cededvsirr qaikelpqfa tgenlprvad iltqllqtdd saefnlvnna
      121 llsifkmdak gtlgglfsqi lqgedivrer aikflstklk tlpdevltke veeliltesk
      181 kvledvtgee fvlfmkilsg lkslqtvsgr qqlvelvaeq adleqtfsps dpdcvdrllq
      241 ctrqavplfs knvhstrfvt yfceqvlpnl stlttpvegl diqlevlkll aemssfcgdm
      301 ekletnlrkl fdklleympl ppeeaengen agneepklqf syvecllysf hqlgrklpdf
      361 ltaklnaekl kdfkirlqyf arglqvyirq lrlalqgktg ealkteenki kvvalkitnn
      421 invlikdlfh ippsykstvt lswkpvqkve igqkrtsedt ssgsppkksp ggpkrdarqi
      481 ynppsgkyss nlgnfnyers lqgk
//
LOCUS       NP_001400182            2336 aa            linear   ROD 28-APR-2025
DEFINITION  voltage-dependent N-type calcium channel subunit alpha-1B isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001400182 XP_006233639
VERSION     NP_001400182.1
DBSOURCE    REFSEQ: accession NM_001413253.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2336)
  AUTHORS   Cai,Z., Quan,L., Chang,X., Qiu,Z. and Zhou,H.
  TITLE     High-voltage long-duration pulsed radiofrequency attenuates
            neuropathic pain in CCI rats by inhibiting Cav2.2 in spinal dorsal
            horn and dorsal root ganglion
  JOURNAL   Brain Res 1785, 147892 (2022)
   PUBMED   35341732
  REMARK    GeneRIF: High-voltage long-duration pulsed radiofrequency
            attenuates neuropathic pain in CCI rats by inhibiting Cav2.2 in
            spinal dorsal horn and dorsal root ganglion.
REFERENCE   2  (residues 1 to 2336)
  AUTHORS   Silveirinha,V.C., Lin,H., Tanifuji,S., Mochida,S., Cottrell,G.S.,
            Cimarosti,H. and Stephens,G.J.
  TITLE     CaV2.2 (N-type) voltage-gated calcium channels are activated by
            SUMOylation pathways
  JOURNAL   Cell Calcium 93, 102326 (2021)
   PUBMED   33360835
  REMARK    GeneRIF: CaV2.2 (N-type) voltage-gated calcium channels are
            activated by SUMOylation pathways.
REFERENCE   3  (residues 1 to 2336)
  AUTHORS   Castro,H., Bermeo,K., Arenas,I. and Garcia,D.E.
  TITLE     Maintenance of CaV2.2 channel-current by PIP2 unveiled by neomycin
            in sympathetic neurons of the rat
  JOURNAL   Arch Biochem Biophys 682, 108261 (2020)
   PUBMED   31923392
  REMARK    GeneRIF: interacting PIP2 charges not only underly the maintenance
            of the channel-current but also that charge screening of PIP2 by
            itself unveils the voltage-independent features of CaV2.2 channels
            in SCG neurons
REFERENCE   4  (residues 1 to 2336)
  AUTHORS   Buchta,W.C., Moutal,A., Hines,B., Garcia-Keller,C., Smith,A.C.W.,
            Kalivas,P., Khanna,R. and Riegel,A.C.
  TITLE     Dynamic CRMP2 Regulation of CaV2.2 in the Prefrontal Cortex
            Contributes to the Reinstatement of Cocaine Seeking
  JOURNAL   Mol Neurobiol 57 (1), 346-357 (2020)
   PUBMED   31359322
  REMARK    GeneRIF: Dynamic CRMP2 Regulation of CaV2.2 in the Prefrontal
            Cortex Contributes to the Reinstatement of Cocaine Seeking.
REFERENCE   5  (residues 1 to 2336)
  AUTHORS   Gandini,M.A., Souza,I.A., Raval,D., Xu,J., Pan,Y.X. and
            Zamponi,G.W.
  TITLE     Differential regulation of Cav2.2 channel exon 37 variants by
            alternatively spliced mu-opioid receptors
  JOURNAL   Mol Brain 12 (1), 98 (2019)
   PUBMED   31775826
  REMARK    GeneRIF: This study provides new insights into the roles of the MOR
            full-length C-terminal variants in modulating Cav2.2 channel
            isoform activities.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2336)
  AUTHORS   Wheeler,D.B., Randall,A. and Tsien,R.W.
  TITLE     Roles of N-type and Q-type Ca2+ channels in supporting hippocampal
            synaptic transmission
  JOURNAL   Science 264 (5155), 107-111 (1994)
   PUBMED   7832825
REFERENCE   7  (residues 1 to 2336)
  AUTHORS   Hell,J.W., Appleyard,S.M., Yokoyama,C.T., Warner,C. and
            Catterall,W.A.
  TITLE     Differential phosphorylation of two size forms of the N-type
            calcium channel alpha 1 subunit which have different COOH termini
  JOURNAL   J Biol Chem 269 (10), 7390-7396 (1994)
   PUBMED   8125957
REFERENCE   8  (residues 1 to 2336)
  AUTHORS   Pragnell,M., De Waard,M., Mori,Y., Tanabe,T., Snutch,T.P. and
            Campbell,K.P.
  TITLE     Calcium channel beta-subunit binds to a conserved motif in the I-II
            cytoplasmic linker of the alpha 1-subunit
  JOURNAL   Nature 368 (6466), 67-70 (1994)
   PUBMED   7509046
REFERENCE   9  (residues 1 to 2336)
  AUTHORS   Dubel,S.J., Starr,T.V., Hell,J., Ahlijanian,M.K., Enyeart,J.J.,
            Catterall,W.A. and Snutch,T.P.
  TITLE     Molecular cloning of the alpha-1 subunit of an
            omega-conotoxin-sensitive calcium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (11), 5058-5062 (1992)
   PUBMED   1317580
REFERENCE   10 (residues 1 to 2336)
  AUTHORS   Snutch,T.P., Leonard,J.P., Gilbert,M.M., Lester,H.A. and
            Davidson,N.
  TITLE     Rat brain expresses a heterogeneous family of calcium channels
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3391-3395 (1990)
   PUBMED   1692134
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Oct 27, 2022 this sequence version replaced XP_006233639.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M92905.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2336
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..2336
                     /product="voltage-dependent N-type calcium channel subunit
                     alpha-1B isoform 3"
                     /note="voltage-dependent N-type calcium channel subunit
                     alpha-1B; voltage-dependent N-type calcium channel subunit
                     alpha-1B-like; voltage gated N-type calcium channel
                     Ca(v)2.2; brain calcium channel III; voltage-gated calcium
                     channel subunit alpha Cav2.2; calcium channel, L type,
                     alpha-1 polypeptide; calcium channel, voltage-dependent, N
                     type, alpha 1B subunit"
                     /calculated_mol_wt=262064
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            22
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          82..359
                     /region_name="I"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            91..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          94..367
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            132..152
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            164..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            188..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            222..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q00975; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            314
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            332..356
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          379..396
                     /region_name="Binding to the beta subunit"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          469..713
                     /region_name="II"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          482..721
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            484..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            513..535
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            546..567
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            575..587
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            606..631
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            664
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            684..710
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          800..1021
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1051..1076
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1135..1421
                     /region_name="III"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1148..1382
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1150..1168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1177..1201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1216..1240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1247..1267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1286..1305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1367
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1393..1418
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1458..1711
                     /region_name="IV"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1472..1719
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1474..1492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1501..1525
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1536..1557
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1564..1582
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1602..1621
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1655
                     /site_type="other"
                     /note="Calcium ion selectivity and permeability.
                     /evidence=ECO:0000250|UniProtKB:P15381; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            1684..1707
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Region          1728..1781
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1792..1869
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1953..>2255
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1981..2202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55017; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     Site            2253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q02294.1)"
     CDS             1..2336
                     /gene="Cacna1b"
                     /gene_synonym="BIII"
                     /coded_by="NM_001413253.1:125..7135"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:257648"
                     /db_xref="RGD:628852"
ORIGIN      
        1 mvrfgdelgg ryggtggger argggaggag gpgqgglppg qrvlykqsia qrartmalyn
       61 pipvkqncft vnrslfvfse dnvvrkyakr itewppfeym ilatiianci vlaleqhlpd
      121 gdktpmserl ddtepyfigi fcfeagikii algfvfhkgs ylrngwnvmd fvvvltgila
      181 tagtdfdlrt lravrvlrpl klvsgipslq vvlksimkam vpllqiglll ffailmfaii
      241 glefymgkfh kacfpnstda epvgdfpcgk eaparlcdsd tecreywpgp nfgitnfdni
      301 lfailtvfqc itmegwtdil yntndaagnt wnwlyfipli iigsffmlnl vlgvlsgefa
      361 kerervenrr aflklrrqqq ierelngyle wifkaeevml aeedknaeek spldavlkra
      421 atkksrndli haeegedrfv dlcaagspfa raslksgkte sssyfrrkek mfrflirrmv
      481 kaqsfywvvl cvvalntlcv amvhynqpqr lttalyfaef vflglfltem slkmyglgpr
      541 syfrssfncf dfgvivgsif evvwaaikpg tsfgisvlra lrllrifkvt kywnslrnlv
      601 vsllnsmksi isllfllflf ivvfallgmq lfggqfnfqd etpttnfdtf paailtvfqi
      661 ltgedwnavm yhgiesqggv skgmfssfyf ivltlfgnyt llnvflaiav dnlanaqelt
      721 kdeeemeeaa nqklalqkak evaevspmsa anisiaarqq nsakarsvwe qrasqlrlqn
      781 lrascealys emdpeerlry astrhvrpdm kthmdrplvv epgrdglrgp agnkskpegt
      841 eategadppr rhhrhrdrdk tsastpagge qdrtdcpkae stetgareer arprrshske
      901 apgadtqvrc ersrrhhrrg speeaterep rrhrahrhaq dsskegkegt apvlvpkger
      961 rarhrgprtg pretenseep trrhrakhkv pptleppere vaekesnvve gdketrnhqp
     1021 keprcdleai avtgvgslhm lpstclqkvd eqpedadnqr nvtrmgsqps dpsttvhvpv
     1081 tltgppgeat vvpsantdle gqaegkkeae addvlrrgpr pivpyssmfc lsptnllrrf
     1141 chyivtmryf emvilvvial ssialaaedp vrtdsfrnna lkymdyiftg vftfemvikm
     1201 idlglllhpg ayfrdlwnil dfivvsgalv afafssfmgg skgkdintik slrvlrvlrp
     1261 lktikrlpkl kavfdcvvns lknvlniliv ymlfmfifav iavqlfkgkf fyctdeskel
     1321 erdcrgqyld yekeeveaqp rqwkkydfhy dnvlwalltl ftvstgegwp mvlkhsvdat
     1381 yeeqgpspgf rmelsifyvv yfvvfpfffv nifvaliiit fqeqgdkvms ecsleknera
     1441 cidfaisakp ltrympqnkq sfqyktwtfv vsppfeyfim amialntvvl mmkfydapye
     1501 yelmlkclni vftsmfslec ilkiiafgvl nyfrdawnvf dfvtvlgsit dilvteiann
     1561 finlsflrlf raarlikllr qgytirillw tfvqsfkalp yvclliamlf fiyaiigmqv
     1621 fgnialddgt sinrhnnfrt flqalmllfr satgeawhei mlsclgnrac dphanasecg
     1681 sdfayfyfvs fiflcsflml nlfvavimdn feyltrdssi lgphhldefi rvwaeydpaa
     1741 cgrisyndmf emlkhmsppl glgkkcparv aykrlvrmnm pisnedmtvh ftstlmalir
     1801 taleiklapa gtkqhqcdae lrkeissvwa nlpqktldll vpphkpdemt vgkvyaalmi
     1861 fdfykqnktt rdqthqapgg lsqmgpvslf hplkatleqt qpavlrgarv flrqksatsl
     1921 snggaiqtqe sgikeslswg tqrtqdvlye araplerghs aeipvgqpga lavdvqmqnm
     1981 tlrgpdgepq pglesqgraa smprlaaetq papnaspmkr sistlaprph gtqlcntvld
     2041 rpppsqvshh hhhrchrrrd kkqrslekgp slsvdtegap staagsglph gegstgcrre
     2101 rkqergrsqe rrqpssssse kqrfyscdrf gsreppqpkp slsshpispt aalepgphpq
     2161 gsgsvngspl mstsgastpg rggrrqlpqt pltprpsity ktansspvhf aegqsglpaf
     2221 spgrlsrgls ehnallqkep lsqplasgsr igsdpylgqr ldseasahnl pedtltfeea
     2281 vatnsgrssr tsyvssltsq shplrrvpng yhctlglstg vrarhsyhhp dqdhwc
//
LOCUS       NP_001121021            1026 aa            linear   ROD 28-APR-2025
DEFINITION  LLGL scribble cell polarity complex component 2 [Rattus
            norvegicus].
ACCESSION   NP_001121021 XP_001073376 XP_001081717 XP_001081718 XP_573224
VERSION     NP_001121021.1
DBSOURCE    REFSEQ: accession NM_001127549.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Saito,Y., Li,L., Coyaud,E., Luna,A., Sander,C., Raught,B.,
            Asara,J.M., Brown,M. and Muthuswamy,S.K.
  TITLE     LLGL2 rescues nutrient stress by promoting leucine uptake in ER+
            breast cancer
  JOURNAL   Nature 569 (7755), 275-279 (2019)
   PUBMED   30996345
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Sripathy,S., Lee,M. and Vasioukhin,V.
  TITLE     Mammalian Llgl2 is necessary for proper branching morphogenesis
            during placental development
  JOURNAL   Mol Cell Biol 31 (14), 2920-2933 (2011)
   PUBMED   21606200
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Yasumi,M., Sakisaka,T., Hoshino,T., Kimura,T., Sakamoto,Y.,
            Yamanaka,T., Ohno,S. and Takai,Y.
  TITLE     Direct binding of Lgl2 to LGN during mitosis and its requirement
            for normal cell division
  JOURNAL   J Biol Chem 280 (8), 6761-6765 (2005)
   PUBMED   15632202
REFERENCE   4  (residues 1 to 1026)
  AUTHORS   Yamanaka,T., Horikoshi,Y., Sugiyama,Y., Ishiyama,C., Suzuki,A.,
            Hirose,T., Iwamatsu,A., Shinohara,A. and Ohno,S.
  TITLE     Mammalian Lgl forms a protein complex with PAR-6 and aPKC
            independently of PAR-3 to regulate epithelial cell polarity
  JOURNAL   Curr Biol 13 (9), 734-743 (2003)
   PUBMED   12725730
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166481.1.
            
            On or before May 23, 2008 this sequence version replaced
            XP_001073376.1, XP_573224.2, XP_001081717.1, XP_001081718.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..1026
                     /product="LLGL scribble cell polarity complex component 2"
                     /note="lethal(2) giant larvae protein homolog 2; lethal
                     giant larvae homolog 2, scribble cell polarity complex
                     component; LLGL2, scribble cell polarity complex
                     component"
                     /calculated_mol_wt=113893
     Region          <36..261
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          36..72
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          77..121
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..189
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          192..228
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          271..372
                     /region_name="LLGL"
                     /note="LLGL2; pfam08366"
                     /db_xref="CDD:462446"
     CDS             1..1026
                     /gene="Llgl2"
                     /gene_synonym="RGD1560307"
                     /coded_by="NM_001127549.1:171..3251"
                     /db_xref="GeneID:360661"
                     /db_xref="RGD:1560307"
ORIGIN      
        1 mrrflrtghd parerlkrdl fqfnktvehg fphqpsalgy spslrilaig trsgavklyg
       61 apgvefmglh kennavlqih flpgqcqlvt llddnslhlw slkvkggvse lqeeesftlr
      121 gppgaapsat qiteilphss gellylgtes gsvfvvrlpg fcalhdrtis sdevlqwlpe
      181 earhrrvfem vealqehprd pnqiligysr glvviwdlra srvlshflsh qqlenvswqr
      241 dgclivtchs dgshcqwsvp sdtqspeplr ssvpygpfpc kaitkifwlt trqglpftif
      301 qggmprasyg drhcisvvhn gqqtafdfts rvidftvlme adpvaafddp yalvvlaeee
      361 lvvidlqtpg wppvqlpyla slhcsaitcs hhvsniplkl weriiaagsr qnshfstmew
      421 pidggtslap pppqrdlllt ghedgtvrfw dasgvclrll yklstvrvfl tdtdlsenls
      481 aqgedewppl rkvgsfdpys ddprlgiqki flckysgyla vagtagqvlv lelndeaaeh
      541 aveqveadll qdqegyrwkg herlaarpgp vrfeagfqpf vlvqcqppav vtslalhsew
      601 rlvafgtshg fglfdhqqrr qvfvkctlhp sdqlalegpl srvkslkksl rqsfrrmrrs
      661 rasshkrrpg gptgeaqaqa vntkaertgl qnmelapvqr kiearsaeds ftgfvrtlyf
      721 adtylrdssr hcpslwagtn ggtvyafslr vppaerrade pvraeqakei qlmhrapvvg
      781 ilvldghnvp lpeplevahd lskspdmqgs hqllvvseeq fkvftlpkvs aklklkltal
      841 egsrvrrvgv ahfgscraed ygehhlavlt nlgdiqvvsv pllkpqvrys cirredvsgi
      901 ascvftkygq gfylispsef erfslstkwl veprclvdsa karnhnrpsn gnstgpkrts
      961 gqvrnsrsqs dgaetkpgpv mehallsdaw vlkevqstle gdqgscgnwr shrvavgcrl
     1021 sngeae
//
LOCUS       NP_001424825             922 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Rattus norvegicus].
ACCESSION   NP_001424825 XP_038934794
VERSION     NP_001424825.1
DBSOURCE    REFSEQ: accession NM_001437896.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schmid,E.M., Ford,M.G., Burtey,A., Praefcke,G.J., Peak-Chew,S.Y.,
            Mills,I.G., Benmerah,A. and McMahon,H.T.
  TITLE     Role of the AP2 beta-appendage hub in recruiting partners for
            clathrin-coated vesicle assembly
  JOURNAL   PLoS Biol 4 (9), e262 (2006)
   PUBMED   16903783
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_038934794.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.26757.1,
                                           SRR26643292.31376.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..922
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     subunit 2; SAPS domain family, member 2"
                     /calculated_mol_wt=100195
     Region          128..534
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          618..>913
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..922
                     /gene="Ppp6r2"
                     /gene_synonym="RGD1563990; Saps2"
                     /coded_by="NM_001437896.1:643..3411"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:300146"
                     /db_xref="RGD:1563990"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvnl
       61 itqdppqdme ekvrfkypnt acelltcdvp qisdrlgede sllnllydfl dqepplnpll
      121 asffsktign liarkteqvi mflkkkdkfi slilkhigts almdlllrlv scvepvvlrq
      181 evlhwlneek viqrlvelih phqdedrqsn asqalcdiir lgrdqgsqlq etvepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgmq vllalleprr vgteglvdsf sqglersysv
      301 sssilhgiep wlknfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhlq velciaails hagreeqaea grsdgkvepv
      421 qgsgdgggkp ettpsitspp entmvthlfq kcclvqrile aweandntqa aggmrrgnmg
      481 hltrianavv qnleqgpvqt hisevirglp aecrgrwesf veetlmetnr rntvdlafse
      541 yqiqqmtanf vdqfgfndee fadqddnina pfdriaeinf nieadedsps aalfeaccsd
      601 riqpfdddee diwedeetrc tarvmararf gaphtsenys kkavghggqg rktgsptarn
      661 vpglatpssp tqkegprses dsagttwtav fdepvnplsa asgaardvgs sawaagpsva
      721 eekgwakftd fqpfccsetg prcsspvdmd hsnaeggqsp gpekafgpts pcawnvcvtr
      781 kaplvasdss ssggsdsedd ekaagaveal caghtgkasp pprtaeaaag raecpdstvl
      841 apacpapsev tispavatia pskagsptat ivvsssvata vppgpimavt ttapaivatl
      901 gtmtkdrktd alpdgaalng pv
//
LOCUS       NP_001385814             294 aa            linear   ROD 28-APR-2025
DEFINITION  developmental pluripotency-associated protein 4 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001385814 XP_001063552
VERSION     NP_001385814.1
DBSOURCE    REFSEQ: accession NM_001398885.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Nakamura,T., Nakagawa,M., Ichisaka,T., Shiota,A. and Yamanaka,S.
  TITLE     Essential roles of ECAT15-2/Dppa2 in functional lung development
  JOURNAL   Mol Cell Biol 31 (21), 4366-4378 (2011)
   PUBMED   21896782
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Dec 27, 2021 this sequence version replaced XP_001063552.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.69001.1,
                                           SRR26643295.43190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..294
                     /product="developmental pluripotency-associated protein 4
                     isoform 2"
                     /note="developmental pluripotency-associated protein 4"
                     /calculated_mol_wt=32268
     Region          124..211
                     /region_name="Dppa2_A"
                     /note="Dppa2/4 conserved region in higher vertebrates;
                     pfam14049"
                     /db_xref="CDD:433674"
     Region          219..285
                     /region_name="DCR"
                     /note="Dppa2/4 conserved region; pfam14047"
                     /db_xref="CDD:464071"
     CDS             1..294
                     /gene="Dppa4"
                     /coded_by="NM_001398885.1:70..954"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:685378"
                     /db_xref="RGD:1595070"
ORIGIN      
        1 mepsgskkgr aeepreevec qmssqpstss aktkatgkkq rksekddgck peeksaqdpe
       61 tpgharrkvp vppfpqhlpp vnlihrdvlr awcqemklss kgqkldaykr llarafpdqm
      121 pelknvpdsa kearlkmprk kmktepgees qvtvpleivt vpeeqipalv dppvlyeevs
      181 ttvvttsase avlaswaria anakkleavp snatsetyge mwcvvhgtsl patssgwvrl
      241 qfhagqawvp dkkgkaialf llpactfppp hlednmlcpk cvhknkiltk sleg
//
LOCUS       NP_001417162             346 aa            linear   ROD 28-APR-2025
DEFINITION  musashi RNA-binding protein 2 isoform b [Rattus norvegicus].
ACCESSION   NP_001417162 XP_038943591
VERSION     NP_001417162.1
DBSOURCE    REFSEQ: accession NM_001430233.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Sengupta,U., Montalbano,M., McAllen,S., Minuesa,G., Kharas,M. and
            Kayed,R.
  TITLE     Formation of Toxic Oligomeric Assemblies of RNA-binding Protein:
            Musashi in Alzheimer's disease
  JOURNAL   Acta Neuropathol Commun 6 (1), 113 (2018)
   PUBMED   30367664
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Sakakibara,S., Nakamura,Y., Yoshida,T., Shibata,S., Koike,M.,
            Takano,H., Ueda,S., Uchiyama,Y., Noda,T. and Okano,H.
  TITLE     RNA-binding protein Musashi family: roles for CNS stem cells and a
            subpopulation of ependymal cells revealed by targeted disruption
            and antisense ablation
  JOURNAL   Proc Natl Acad Sci U S A 99 (23), 15194-15199 (2002)
   PUBMED   12407178
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Sakakibara,S., Nakamura,Y., Satoh,H. and Okano,H.
  TITLE     Rna-binding protein Musashi2: developmentally regulated expression
            in neural precursor cells and subpopulations of neurons in
            mammalian CNS
  JOURNAL   J Neurosci 21 (20), 8091-8107 (2001)
   PUBMED   11588182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On May 7, 2024 this sequence version replaced XP_038943591.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643289.28985.1,
                                           SRR26643296.28150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..346
                     /product="musashi RNA-binding protein 2 isoform b"
                     /note="Musashi homolog 2; RNA-binding protein Musashi
                     homolog 2"
                     /calculated_mol_wt=36783
     Region          17..109
                     /region_name="RRM1_MSI2"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein Musashi homolog 2 (Musashi-2) and similar
                     proteins; cd12760"
                     /db_xref="CDD:410153"
     Site            order(24,26..30,51,53,62..64,66,89,92,94..97)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410153"
     Region          111..184
                     /region_name="RRM2_MSI"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein Musashi homologs Musashi-1, Musashi-2 and similar
                     proteins; cd12323"
                     /db_xref="CDD:240769"
     CDS             1..346
                     /gene="Msi2"
                     /gene_synonym="RGD1560397"
                     /coded_by="NM_001430233.1:188..1228"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:360596"
                     /db_xref="RGD:1560397"
ORIGIN      
        1 meangspgts gsandsqhdp gkmfigglsw qtspdslrdy fskfgeirec mvmrdpttkr
       61 srgfgfvtfa dpasvdkvlg qphheldskt idpkvafprr aqpkmvtrtk kifvgglsan
      121 tvvedvkqyf eqfgkvedam lmfdkttnrh rgfgfvtfen edvvekvcei hfheinnkmv
      181 eckkaqpkev mfppgtrgra rglpytmdaf mlgmgmlgyp nfvatygrgy pgfapsygyq
      241 fpgfpaaayg pvaaaavaaa rgsvlnsysa qpnfgaptsp agsnparpgg fpganspgpv
      301 adlygpasqd sgvgnyisaa spqpgsgfgh giasipgcpg ktgrsf
//
LOCUS       NP_001388337             683 aa            linear   ROD 28-APR-2025
DEFINITION  THO complex subunit 5 homolog isoform 3 [Rattus norvegicus].
ACCESSION   NP_001388337 XP_006251401
VERSION     NP_001388337.1
DBSOURCE    REFSEQ: accession NM_001401408.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Wang,L., Miao,Y.L., Zheng,X., Lackford,B., Zhou,B., Han,L., Yao,C.,
            Ward,J.M., Burkholder,A., Lipchina,I., Fargo,D.C., Hochedlinger,K.,
            Shi,Y., Williams,C.J. and Hu,G.
  TITLE     The THO complex regulates pluripotency gene mRNA export and
            controls embryonic stem cell self-renewal and somatic cell
            reprogramming
  JOURNAL   Cell Stem Cell 13 (6), 676-690 (2013)
   PUBMED   24315442
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Katahira,J.
  TITLE     mRNA export and the TREX complex
  JOURNAL   Biochim Biophys Acta 1819 (6), 507-513 (2012)
   PUBMED   22178508
  REMARK    Review article
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Dominguez-Sanchez,M.S., Barroso,S., Gomez-Gonzalez,B., Luna,R. and
            Aguilera,A.
  TITLE     Genome instability and transcription elongation impairment in human
            cells depleted of THO/TREX
  JOURNAL   PLoS Genet 7 (12), e1002386 (2011)
   PUBMED   22144908
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Mancini,A., Niemann-Seyde,S.C., Pankow,R., El Bounkari,O.,
            Klebba-Farber,S., Koch,A., Jaworska,E., Spooncer,E., Gruber,A.D.,
            Whetton,A.D. and Tamura,T.
  TITLE     THOC5/FMIP, an mRNA export TREX complex protein, is essential for
            hematopoietic primitive cell survival in vivo
  JOURNAL   BMC Biol 8, 1 (2010)
   PUBMED   20051105
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Sjoblom,T., Jones,S., Wood,L.D., Parsons,D.W., Lin,J., Barber,T.D.,
            Mandelker,D., Leary,R.J., Ptak,J., Silliman,N., Szabo,S.,
            Buckhaults,P., Farrell,C., Meeh,P., Markowitz,S.D., Willis,J.,
            Dawson,D., Willson,J.K., Gazdar,A.F., Hartigan,J., Wu,L., Liu,C.,
            Parmigiani,G., Park,B.H., Bachman,K.E., Papadopoulos,N.,
            Vogelstein,B., Kinzler,K.W. and Velculescu,V.E.
  TITLE     The consensus coding sequences of human breast and colorectal
            cancers
  JOURNAL   Science 314 (5797), 268-274 (2006)
   PUBMED   16959974
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Masuda,S., Das,R., Cheng,H., Hurt,E., Dorman,N. and Reed,R.
  TITLE     Recruitment of the human TREX complex to mRNA during splicing
  JOURNAL   Genes Dev 19 (13), 1512-1517 (2005)
   PUBMED   15998806
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Guo,S., Hakimi,M.A., Baillat,D., Chen,X., Farber,M.J.,
            Klein-Szanto,A.J., Cooch,N.S., Godwin,A.K. and Shiekhattar,R.
  TITLE     Linking transcriptional elongation and messenger RNA export to
            metastatic breast cancers
  JOURNAL   Cancer Res 65 (8), 3011-3016 (2005)
   PUBMED   15833825
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Mancini,A., Koch,A., Whetton,A.D. and Tamura,T.
  TITLE     The M-CSF receptor substrate and interacting protein FMIP is
            governed in its subcellular localization by protein kinase
            C-mediated phosphorylation, and thereby potentiates M-CSF-mediated
            differentiation
  JOURNAL   Oncogene 23 (39), 6581-6589 (2004)
   PUBMED   15221008
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Tamura,T., Mancini,A., Joos,H., Koch,A., Hakim,C., Dumanski,J.,
            Weidner,K.M. and Niemann,H.
  TITLE     FMIP, a novel Fms-interacting protein, affects
            granulocyte/macrophage differentiation
  JOURNAL   Oncogene 18 (47), 6488-6495 (1999)
   PUBMED   10597251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 11, 2022 this sequence version replaced XP_006251401.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.1798631.1,
                                           SRR26360176.1829125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..683
                     /product="THO complex subunit 5 homolog isoform 3"
                     /note="THO complex subunit 5 homolog; fms-interacting
                     protein; Fms interacting protein; THO complex 5"
                     /calculated_mol_wt=78657
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          2..199
                     /region_name="Interaction with THOC7.
                     /evidence=ECO:0000250|UniProtKB:Q13769"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          2..144
                     /region_name="Interaction with CSF1R.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          7..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX7.1)"
     Region          103..452
                     /region_name="FmiP_Thoc5"
                     /note="Fms-interacting protein/Thoc5; pfam09766"
                     /db_xref="CDD:462889"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13769; propagated from
                     UniProtKB/Swiss-Prot (Q68FX7.1)"
     CDS             1..683
                     /gene="Thoc5"
                     /gene_synonym="Fmip"
                     /coded_by="NM_001401408.1:61..2112"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:360972"
                     /db_xref="RGD:1304991"
ORIGIN      
        1 mssesskkrk pkvirsdgtp tegkrnrsdt eqegryysee aevdlrdpgr dyelykytcq
       61 elqrlmaeiq dlkskgskdv aieieerriq scvhfmtlkk lnrlahirlk kgrdqtheak
      121 qkvdayhlql qnllyevmhl qkeitkclef kskheeidlv sleefyseap pniskaeitm
      181 gdphqqtlar ldweleqrkr laekyrecls nkekilkeie vkkeylsslq prlnsimqas
      241 lpvqeylfmp fdqahkqyet arhlppplyv lfvqataygq acdktlsvai egsvdeakal
      301 fkppedsqdd esdsdaeeeq ttkrrrptlg vqlddkrkem lkrhplsvll dlkckdnsvl
      361 hltffylmnl nimtvkakvt tamelitpis agdllspdsv lsclypgdhg kktpnpanqy
      421 qfdkvgiltl rdyvlelghp ylwvqklggl hfpkeqpqht vmadhsqsas hmettmkllk
      481 trvqsrlalh kqfaslehgi vpvtsecqyl fpakvvsrlv kwmimahedy melhftkdiv
      541 eaglagdtnl yylaliergt aklqaavvln pgyssippvf rlclnwkgek tnsnddnira
      601 mesevnvcyr elcgprpshq lltnqlqrlc vlldvylete shddsvegpk efpqekmclr
      661 lfrgpsrmkp fkynhpqgff shr
//
LOCUS       NP_001014106             460 aa            linear   ROD 28-APR-2025
DEFINITION  gasdermin D like 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001014106 XP_235286
VERSION     NP_001014106.1
DBSOURCE    REFSEQ: accession NM_001014084.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 20, 2005 this sequence version replaced XP_235286.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.41283.1,
                                           SRR26360181.994678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..460
                     /product="gasdermin D like 1 isoform 2"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=50819
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..>380
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..460
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001014084.2:255..1637"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelaqel cksicdmltr vlllyggkvr pqgevalqgn tgqavlpcvs
      421 cigllrsich mtkqnkllrf qpivpmtiqc qsmgssqlnk
//
LOCUS       NP_001387872            1370 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology-like domain family B member 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001387872 XP_038936702
VERSION     NP_001387872.1
DBSOURCE    REFSEQ: accession NM_001400943.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1370)
  AUTHORS   Nakaya,Y., Sukowati,E.W. and Sheng,G.
  TITLE     Epiblast integrity requires CLASP and Dystroglycan-mediated
            microtubule anchoring to the basal cortex
  JOURNAL   J Cell Biol 202 (4), 637-651 (2013)
   PUBMED   23940118
REFERENCE   2  (residues 1 to 1370)
  AUTHORS   Levi,L., Hanukoglu,I., Raikhinstein,M., Kohen,F. and Koch,Y.
  TITLE     Cloning of LL5, a novel protein encoding cDNA from a rat pituitary
            library
  JOURNAL   Biochim Biophys Acta 1216 (2), 342-344 (1993)
   PUBMED   8241284
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Jan 31, 2022 this sequence version replaced XP_038936702.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760386
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1370
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..1370
                     /product="pleckstrin homology-like domain family B member
                     1 isoform 2"
                     /note="protein LL5-alpha"
                     /calculated_mol_wt=149878
     Region          24..142
                     /region_name="FHA_PHLB1"
                     /note="forkhead associated (FHA) domain found in
                     pleckstrin homology-like domain family B member 1 (PHLDB1)
                     and similar proteins; cd22713"
                     /db_xref="CDD:438765"
     Region          143..>547
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <681..>1240
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          <684..>897
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1259..1363
                     /region_name="PH_PHLDB1_2"
                     /note="Pleckstrin homology-like domain-containing family B
                     member 2 pleckstrin homology (PH) domain; cd14673"
                     /db_xref="CDD:270192"
     CDS             1..1370
                     /gene="Phldb1"
                     /gene_synonym="Ll5"
                     /coded_by="NM_001400943.2:99..4211"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171434"
                     /db_xref="RGD:620878"
ORIGIN      
        1 matlnrnqlg pgcktqavvq kgpldlietg qglkvqtdkp hlvslgsgrl staitllple
       61 egrtvigsaa rdislqgpgl apehcyienl rgtltlypcg nactidglpv rqptrltqgc
      121 mlclgqstfl rfnhpaeakw mksmipaggr apgstyspgs aeseslvngn htaqpatrap
      181 pacashsslv ssiekdlqei mdslvleepg aagkkpaats plspvanggr yllspptspg
      241 amsvgssyen tspafsplss passgscash spsgqepgps vpplvparss syhlalqppq
      301 srpsgsrsse sprlgrkggh erppspglrg lltdspaatv laearrttes prlggqlpvv
      361 aislseypss garsqptsip gspkfqspvp aprnkigtlq drppspfrep pgtervltts
      421 psrqlvgrtf sdgsatrtlq ppesprlgrr gldsmrelpp lspslsrral splpartapd
      481 pklsrevaes prprrwaahg tspedfsltl gargrrtrsp sptlgeslap rkgsfsgrls
      541 payslgsltg asprqsphaq rklssgdlrv piprerknsi teisdneddl leyhrrqrqe
      601 rlreqemerl erqrletiln lcaeysradg gpetgelpsi geataalala grrpsrglag
      661 aivvsgrsge esggasqrlw esmersdeen lkeecsstes tqqehedaps tklqgevlav
      721 eeeraqvlgr veqlkvrvke leqqlqeaar eaemerallq gereaerall qkeqramdql
      781 qeklvaletg iqkerdkead aletetklfe dlefqqlere srveeerela gqgllrskae
      841 llrsvskrke rlavldsqag qiraqavqes erlareknav lqllqkekek ltvlerryhs
      901 ltggrsfpkt tstlkemekl llpavdleqw yqelmaglgt glaaasprss ppplpakasr
      961 qlqvyrskmn gdmasplprt rsgplpsssg ssssssqlsv atlgrspspk sallaqngts
     1021 slprnlaatl qdietkrqla lqqkghqvie eqrrrlaelk qkaaaeaqcq wdalhgaaaf
     1081 pagpsgfptl mhhsilhhlp agrergeege haydtlsles sdsmetsist ggnsacspdn
     1141 mssasgldmg kieemekmlk eahaeksrlm esreremelr rqaleeerrr reqverrlqs
     1201 esarrqqlve kevklrekqf sqarpltryl pnrkedfdlk thiessghgv dtclhvvlss
     1261 kvcrgylikm ggkikswkkr wfvfdrlkrt lsyyvdkhet klkgviyfqa ieevyydhlr
     1321 saakspnpal tfcvkthdrl yymvapsaea mriwmdvivt gaegytqfmn
//
LOCUS       NP_001386684             292 aa            linear   ROD 28-APR-2025
DEFINITION  homeobox protein Hox-D8 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001386684 XP_038962310
VERSION     NP_001386684.1
DBSOURCE    REFSEQ: accession NM_001399755.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   van den Akker,E., Fromental-Ramain,C., de Graaff,W., Le
            Mouellic,H., Brulet,P., Chambon,P. and Deschamps,J.
  TITLE     Axial skeletal patterning in mice lacking all paralogous group 8
            Hox genes
  JOURNAL   Development 128 (10), 1911-1921 (2001)
   PUBMED   11311170
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Zappavigna,V., Renucci,A., Izpisua-Belmonte,J.C., Urier,G.,
            Peschle,C. and Duboule,D.
  TITLE     HOX4 genes encode transcription factors with potential auto- and
            cross-regulatory capacities
  JOURNAL   EMBO J 10 (13), 4177-4187 (1991)
   PUBMED   1756725
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 13, 2022 this sequence version replaced XP_038962310.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.11964.1,
                                           SRR26643285.11936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..292
                     /product="homeobox protein Hox-D8 isoform 1"
                     /note="homeobox protein Hox-D8-like"
                     /calculated_mol_wt=31455
     Region          143..276
                     /region_name="COG5576"
                     /note="Homeodomain-containing transcription factor
                     [Transcription]"
                     /db_xref="CDD:227863"
     Region          200..256
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..292
                     /gene="Hoxd8"
                     /coded_by="NM_001399755.1:204..1082"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100912936"
                     /db_xref="RGD:6489440"
ORIGIN      
        1 mssyfvnply skykaaaaaa aaaaaaaaag eainptyydc hfapevsgrh aaalqlygns
       61 aagfphappq ahahphpspp pgcgggggpg pgqnyfhaga gspvaayqaa ppppphpppp
      121 pppppcggia chgepakfyg ydnlqrqpif ttqqeaelvq ypdcksssgn igedpdhlnq
      181 ssspsqmfpw mrpqaapgrr rgrqtysrfq tlelekeflf npyltrkrri evshtlalte
      241 rqvkiwfqnr rmkwkkennr dkfpasrpea kdgdpkkevs gleedgaegp tn
//
LOCUS       NP_001420283             497 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 385B isoform a [Rattus norvegicus].
ACCESSION   NP_001420283 XP_017447189
VERSION     NP_001420283.1
DBSOURCE    REFSEQ: accession NM_001433354.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Iijima,K., Yamada,H., Miharu,M., Imadome,K., Miyagawa,Y.,
            Akimoto,S., Kobayashi,K., Okita,H., Nakazawa,A., Fujiwara,S.,
            Fujimoto,J. and Kiyokawa,N.
  TITLE     ZNF385B is characteristically expressed in germinal center B cells
            and involved in B-cell apoptosis
  JOURNAL   Eur J Immunol 42 (12), 3405-3415 (2012)
   PUBMED   22945289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Aug 9, 2024 this sequence version replaced XP_017447189.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.16564.1,
                                           SRR26643293.17291.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..497
                     /product="zinc finger protein 385B isoform a"
                     /note="zinc finger protein 533"
                     /calculated_mol_wt=52903
     Region          35..65
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          36..58
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          186..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          186..208
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          312..336
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          314..376
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(321..323,325..326,330,375,382,385..389,391..392)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          375..399
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          377..399
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..497
                     /gene="Zfp385b"
                     /gene_synonym="Zfp533"
                     /coded_by="NM_001433354.1:445..1938"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:311137"
                     /db_xref="RGD:1311181"
ORIGIN      
        1 mnmasflrgf eekglkndrp gdqfskekkk ilfsfcdvcn iqlnsaaqaq vhydgkshrk
       61 rvkqlsdgqp pppaqgsvpl laspcpgpgp gpgtntstgs achtttlpal vrtptlmmqp
      121 sldikpfmsf pvdsssavgl fpnfntkrrg lfgtnkffqm dpvqkavinh tfgvsippkk
      181 kqviscnvcq lrfnsdsqae ahytgskhak kvkaleatkn kpkmvpskds akanpscsvr
      241 pgtgdssdks edkgkikats ssqpsgsegg sfflksgttp ltlgaiasps kstngapgsv
      301 aeseeekakk llycslckva vnslsqleah ntgskhktmv earngagpik syprpgsrlk
      361 vqngskgsgl qnktfhceic dvhvnseiql kqhissrrhk drvagkplkp kyspynklqr
      421 spsilaakla fqkdlmkpla ptflssplaa aavstalslp prpsaslfqa aaippallrp
      481 ghgpiratpt silfapy
//
LOCUS       NP_001100845             299 aa            linear   ROD 28-APR-2025
DEFINITION  peroxisomal biogenesis factor 19 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001100845 XP_001057306 XP_001057359 XP_001057414 XP_225711
VERSION     NP_001100845.1
DBSOURCE    REFSEQ: accession NM_001107375.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Kinoshita,N., Matsuura,A. and Fujiki,Y.
  TITLE     Peroxisome biogenesis: a novel inducible PEX19 splicing variant is
            involved in early stages of peroxisome proliferation
  JOURNAL   J Biochem 161 (3), 297-308 (2017)
   PUBMED   28391327
  REMARK    GeneRIF: The PEX19i most likely plays important roles involving the
            membrane formation at early stages, in prompt response to
            peroxisome proliferation. Similar types of PEX19 mRNA variants were
            also elevated in mouse regenerating liver.
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Bharti,P., Schliebs,W., Schievelbusch,T., Neuhaus,A., David,C.,
            Kock,K., Herrmann,C., Meyer,H.E., Wiese,S., Warscheid,B., Theiss,C.
            and Erdmann,R.
  TITLE     PEX14 is required for microtubule-based peroxisome motility in
            human cells
  JOURNAL   J Cell Sci 124 (Pt 10), 1759-1768 (2011)
   PUBMED   21525035
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Pinto,M.P., Grou,C.P., Fransen,M., Sa-Miranda,C. and Azevedo,J.E.
  TITLE     The cytosolic domain of PEX3, a protein involved in the biogenesis
            of peroxisomes, binds membrane lipids
  JOURNAL   Biochim Biophys Acta 1793 (11), 1669-1675 (2009)
   PUBMED   19715730
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Neufeld,C., Filipp,F.V., Simon,B., Neuhaus,A., Schuller,N.,
            David,C., Kooshapur,H., Madl,T., Erdmann,R., Schliebs,W.,
            Wilmanns,M. and Sattler,M.
  TITLE     Structural basis for competitive interactions of Pex14 with the
            import receptors Pex5 and Pex19
  JOURNAL   EMBO J 28 (6), 745-754 (2009)
   PUBMED   19197237
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Matsuzaki,T. and Fujiki,Y.
  TITLE     The peroxisomal membrane protein import receptor Pex3p is directly
            transported to peroxisomes by a novel Pex19p- and Pex16p-dependent
            pathway
  JOURNAL   J Cell Biol 183 (7), 1275-1286 (2008)
   PUBMED   19114594
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Biermanns,M. and Gartner,J.
  TITLE     Targeting elements in the amino-terminal part direct the human
            70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes
  JOURNAL   Biochem Biophys Res Commun 285 (3), 649-655 (2001)
   PUBMED   11453642
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Jones,J.M., Morrell,J.C. and Gould,S.J.
  TITLE     Multiple distinct targeting signals in integral peroxisomal
            membrane proteins
  JOURNAL   J Cell Biol 153 (6), 1141-1150 (2001)
   PUBMED   11402059
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Sacksteder,K.A., Jones,J.M., South,S.T., Li,X., Liu,Y. and
            Gould,S.J.
  TITLE     PEX19 binds multiple peroxisomal membrane proteins, is
            predominantly cytoplasmic, and is required for peroxisome membrane
            synthesis
  JOURNAL   J Cell Biol 148 (5), 931-944 (2000)
   PUBMED   10704444
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Matsuzono,Y., Kinoshita,N., Tamura,S., Shimozawa,N., Hamasaki,M.,
            Ghaedi,K., Wanders,R.J., Suzuki,Y., Kondo,N. and Fujiki,Y.
  TITLE     Human PEX19: cDNA cloning by functional complementation, mutation
            analysis in a patient with Zellweger syndrome, and potential role
            in peroxisomal membrane assembly
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2116-2121 (1999)
   PUBMED   10051604
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Kammerer,S., Arnold,N., Gutensohn,W., Mewes,H.W., Kunau,W.H.,
            Hofler,G., Roscher,A.A. and Braun,A.
  TITLE     Genomic organization and molecular characterization of a gene
            encoding HsPXF, a human peroxisomal farnesylated protein
  JOURNAL   Genomics 45 (1), 200-210 (1997)
   PUBMED   9339377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB718412.1, CK600534.1, CO573662.1, BF543157.1, AI712677.1 and
            CK838542.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225711.4, XP_001057359.1, XP_001057414.1, XP_001057306.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FN802327.1, SRR8487231.156072.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..299
                     /product="peroxisomal biogenesis factor 19 isoform 1"
                     /note="peroxin-19; peroxisomal farnesylated protein;
                     peroxisome biogenesis factor 19"
                     /calculated_mol_wt=32350
     mat_peptide     2..296
                     /product="Peroxisomal biogenesis factor 19.
                     /id=PRO_0000218761"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
                     /calculated_mol_wt=31993
     Region          2..91
                     /region_name="Necessary for PEX19 function on peroxisome
                     biogenesis. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          2..56
                     /region_name="Docking to the peroxisome membrane and
                     binding to PEX3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P40855; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          25..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P40855; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Region          74..299
                     /region_name="Pex19"
                     /note="Pex19 protein family; pfam04614"
                     /db_xref="CDD:461367"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCI5; propagated from
                     UniProtKB/Swiss-Prot (Q9QYU1.1)"
     Site            296
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q9QYU1.1)"
     CDS             1..299
                     /gene="Pex19"
                     /gene_synonym="PxF"
                     /coded_by="NM_001107375.2:27..926"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289233"
                     /db_xref="RGD:1306913"
ORIGIN      
        1 maaaeggcga gveadrelee llesalddfd kakpspapsp tisapdasgp qkrspgdtak
       61 dalfasqekf fqelfdsela sqataefeka mkelaeeeph lveqfqklse aagrvgsdas
      121 sqqeftsclk etlsglakna tdlqnagmse eeltkamegl gmdegdgegn ilpimqslmq
      181 nllskdvlyp slkeitekyp ewlqshqesi ppeqfekyqq qhsvmgkice qfeaetptds
      241 eathrarfea vldlmqqlqd lghppkelag emppglnfdl dalnlsgppg angeqclim
//
LOCUS       NP_001092935             866 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor, 9 [Rattus norvegicus].
ACCESSION   NP_001092935 XP_001064753
VERSION     NP_001092935.1
DBSOURCE    REFSEQ: accession NM_001099465.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Aug 15, 2007 this sequence version replaced XP_001064753.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..866
                     /product="vomeronasal 2 receptor, 9"
                     /calculated_mol_wt=99700
     Region          44..512
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(79,181..182,406)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(117,120,163,255)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          520..573
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          594..844
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          594..618
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(596,599..600,603..604,606..607,641,645,648..649,657,
                     661)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          630..651
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(650,662..663,666..667,670,750,755,758..759,762,796,
                     799..800,803,807,815..816,819,822,826)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          660..684
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          708..724
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          751..777
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          785..808
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          813..838
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..866
                     /gene="Vom2r9"
                     /gene_synonym="RGD1564755"
                     /coded_by="NM_001099465.1:1..2601"
                     /db_xref="GeneID:685666"
                     /db_xref="RGD:1591347"
ORIGIN      
        1 myvnrmfcvf ipwsmqiptf ecafqysecy frfkenfhce gnvvigaffp lhtfytankt
       61 aygnvmnyyk dfylkykfnn yqfvlalvfa ieeinknphl lsnislgfhv ynvpyteknt
      121 lmstliwltg qrnfmpnync rmnrmsaaal tgtswatsaq igtllqlykf pqvreiiltf
      181 gpsdpilsdr gqfsslyqma pndttlslam vslmlhfnws wvgllliddh kgthilshlr
      241 eemdrskicl alvemipvtw tsfsynfwkn lkkiqeslan vfiiygdids lqglmdnlgq
      301 qlitwkvwim nsqwdstkqa dyflldsfhg slifshhhee sfefsnfirk vnpykypedp
      361 ylpklwyalf ncsfskfdcq llencqpnas lelfpttiid msmseesyni ytsvyavaht
      421 lqemslqqcq mqshlkgekm vffpwqlhhf lrkihegdhm slewkwrfie eydilnfwnf
      481 pkglglkvkv gtfsldapqg eqlslsehmi qwptkftqip qsacytscwp gfrkatqkgr
      541 avccydcipc ldneisnetd vdqcvkcpet hfpnteknnc lqksmsfley ndnlgmvlit
      601 ialcfsaltl avlgvfvkyr dtpivkannr tlsyillmtl vvcflcsllf ighpntatcl
      661 mqqttfgivf tvalstvlak vitvvmafkf tipgritrwl mvsrapnyvi pictliqivl
      721 cgiylgtspp fldqdpyseh dhilivcnkg sdvvfhcilg ylcflalgsc vmaflsrnlp
      781 dtfnesklls fsmqvflcvw vtflpvyhst kgkvmvamqv ssilassagi lgfifapkcy
      841 iillrpdqns lhhirntayt rrnkpl
//
LOCUS       NP_001389371             156 aa            linear   ROD 28-APR-2025
DEFINITION  LIM domain only protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001389371
VERSION     NP_001389371.1
DBSOURCE    REFSEQ: accession NM_001402442.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Kusy,S., Gerby,B., Goardon,N., Gault,N., Ferri,F., Gerard,D.,
            Armstrong,F., Ballerini,P., Cayuela,J.M., Baruchel,A., Pflumio,F.
            and Romeo,P.H.
  TITLE     NKX3.1 is a direct TAL1 target gene that mediates proliferation of
            TAL1-expressing human T cell acute lymphoblastic leukemia
  JOURNAL   J Exp Med 207 (10), 2141-2156 (2010)
   PUBMED   20855495
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Susa,T., Ishikawa,A., Cai,L.Y., Kato,T., Matsumoto,K., Kitahara,K.,
            Kurokawa,R., Ono,T. and Kato,Y.
  TITLE     The highly related LIM factors, LMO1, LMO3 and LMO4, play different
            roles in the regulation of the pituitary glycoprotein hormone
            alpha-subunit (alpha GSU) gene
  JOURNAL   Biosci Rep 30 (1), 51-58 (2009)
   PUBMED   19228115
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Chervinsky,D.S., Zhao,X.F., Lam,D.H., Ellsworth,M., Gross,K.W. and
            Aplan,P.D.
  TITLE     Disordered T-cell development and T-cell malignancies in SCL LMO1
            double-transgenic mice: parallels with E2A-deficient mice
  JOURNAL   Mol Cell Biol 19 (7), 5025-5035 (1999)
   PUBMED   10373552
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Ono,Y., Fukuhara,N. and Yoshie,O.
  TITLE     TAL1 and LIM-only proteins synergistically induce retinaldehyde
            dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia
            by acting as cofactors for GATA3
  JOURNAL   Mol Cell Biol 18 (12), 6939-6950 (1998)
   PUBMED   9819382
REFERENCE   5  (residues 1 to 156)
  AUTHORS   McGuire,E.A., Rintoul,C.E., Sclar,G.M. and Korsmeyer,S.J.
  TITLE     Thymic overexpression of Ttg-1 in transgenic mice results in T-cell
            acute lymphoblastic leukemia/lymphoma
  JOURNAL   Mol Cell Biol 12 (9), 4186-4196 (1992)
   PUBMED   1508213
REFERENCE   6  (residues 1 to 156)
  AUTHORS   McGuire,E.A., Davis,A.R. and Korsmeyer,S.J.
  TITLE     T-cell translocation gene 1 (Ttg-1) encodes a nuclear protein
            normally expressed in neural lineage cells
  JOURNAL   Blood 77 (3), 599-606 (1991)
   PUBMED   1703797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.662257.1,
                                           SRR22399489.3956773.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q33"
     Protein         1..156
                     /product="LIM domain only protein 3 isoform 1"
                     /note="neuronal-specific transcription factor DAT1;
                     dopamine-inducible LIM-domain transcription factor DAT1;
                     LIM domain only protein 1; LIM domain only protein 3"
                     /calculated_mol_wt=17706
     Region          24..78
                     /region_name="LIM1_LMO1_LMO3"
                     /note="The first LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09388"
                     /db_xref="CDD:188774"
     Site            order(24,27,45,48,51,54,74,77)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188774"
     Region          88..142
                     /region_name="LIM2_LMO1_LMO3"
                     /note="The second LIM domain of LMO1 and LMO3 (LIM domain
                     only protein 1 and 3); cd09389"
                     /db_xref="CDD:188775"
     Site            order(88,91,110,113,116,119,138,141)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188775"
     CDS             1..156
                     /gene="Lmo1"
                     /gene_synonym="Dat1"
                     /coded_by="NM_001402442.1:526..996"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:245979"
                     /db_xref="RGD:621166"
ORIGIN      
        1 mmvldkedgv pmlsvqpkgk qkgcagcnrk ikdryllkal dkywhedclk caccdcrlge
       61 vgstlytkan lilcrrdylr lfgttgncaa csklipafem vmrardnvyh ldcfacqlcn
      121 qrfcvgdkff lknnmilcqm dyeeghlngt fesqvq
//
LOCUS       NP_001120993             171 aa            linear   ROD 28-APR-2025
DEFINITION  chromatin complexes subunit BAP18 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001120993 XP_001079776 XP_213357
VERSION     NP_001120993.1
DBSOURCE    REFSEQ: accession NM_001127521.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Vermeulen,M., Eberl,H.C., Matarese,F., Marks,H., Denissov,S.,
            Butter,F., Lee,K.K., Olsen,J.V., Hyman,A.A., Stunnenberg,H.G. and
            Mann,M.
  TITLE     Quantitative interaction proteomics and genome-wide profiling of
            epigenetic histone marks and their readers
  JOURNAL   Cell 142 (6), 967-980 (2010)
   PUBMED   20850016
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before May 23, 2008 this sequence version replaced
            XP_213357.2, XP_001079776.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158879.1, SRR26360186.1856709.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760434,
                                           SAMN12840105 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..171
                     /product="chromatin complexes subunit BAP18 isoform 1"
                     /note="chromatin complexes subunit BAP18"
                     /calculated_mol_wt=17823
     Region          41..77
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     CDS             1..171
                     /gene="Bacc1"
                     /gene_synonym="C10h17orf49; RGD1308134"
                     /coded_by="NM_001127521.3:66..581"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:287452"
                     /db_xref="RGD:1308134"
ORIGIN      
        1 mtsastkvge ifsaagaaft klgeltmqlh pvsdsspaga kwteteieml raavkrfgdd
       61 lnhiscvike rtvaqikttv krkvyedsgi plpaespkkg pkkmtsgvls ppnapppsss
      121 svpeaggppi kkqkadvtls alndsdansd lvdveglget ppakklnfdq a
//
LOCUS       NP_001380784             567 aa            linear   ROD 28-APR-2025
DEFINITION  SLAIN motif-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001380784 XP_038949462
VERSION     NP_001380784.1
DBSOURCE    REFSEQ: accession NM_001393855.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Mar 18, 2021 this sequence version replaced XP_038949462.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.197970.1,
                                           SRR22399484.789151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..567
                     /product="SLAIN motif-containing protein 1 isoform 2"
                     /note="SLAIN motif-containing protein 1"
                     /calculated_mol_wt=60548
     Region          185..567
                     /region_name="SLAIN"
                     /note="SLAIN motif-containing family; pfam15301"
                     /db_xref="CDD:464627"
     CDS             1..567
                     /gene="Slain1"
                     /gene_synonym="RGD1308626"
                     /coded_by="NM_001393855.1:187..1890"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361087"
                     /db_xref="RGD:1308626"
ORIGIN      
        1 mmaeqvkcas pvagsgagpg pvvnaelevk klqelvrkle kqneqlrsra asaaaaphll
       61 llqppppsap ppagacsplt thrapastts pgpgalgpaf pgtyclpspa psllcslqpa
      121 dapfvyskpa agffagggsp epwtagtppg eaatpplppp tlldevepld leslaawsed
      181 ddytwlyigs sktftlseks lsplqwcrhv ldnptpemea arrslrfrle qgytsrgspl
      241 spqssidsel stseleddsi smgyklqdlt dvqimarlqe eslrqdcast sgsvsrnsst
      301 islssgkkgt csdqeydrys ledeeefdhl pppqprlprc spfqrgiphs qtfssirdcr
      361 rspssqyfps nnfqqpqyys pqaqtpdqqp nrtngdklrr smpnlarmps ttavssnlss
      421 pvtvrssqsf dsslhgagsg vsrvpscips pgqiqhrvhs vghfpvpirq plkatayvsp
      481 tvqgssssmp lsngtqlysn tgiptpnkaa asgimgrsal prpslaings nlprskiaqp
      541 vrsflqppkp lsslstlrdg nwrdgcy
//
LOCUS       NP_001387557             291 aa            linear   ROD 28-APR-2025
DEFINITION  insulin-like growth factor-binding protein 3 receptor isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001387557 XP_038957132
VERSION     NP_001387557.1
DBSOURCE    REFSEQ: accession NM_001400628.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 26, 2022 this sequence version replaced XP_038957132.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.371513.1,
                                           SRR26360176.683755.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36-q37"
     Protein         1..291
                     /product="insulin-like growth factor-binding protein 3
                     receptor isoform 1"
                     /note="insulin-like growth factor-binding protein 3
                     receptor"
                     /calculated_mol_wt=31051
     Region          100..220
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     CDS             1..291
                     /gene="Tmem219"
                     /gene_synonym="RGD1560566"
                     /coded_by="NM_001400628.1:30..905"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:308986"
                     /db_xref="RGD:1560566"
ORIGIN      
        1 mrvwtdwgga vagararagp aprraahdvt grrsppgckr rhsteaqtpl lpmgscqagh
       61 nlhlclahhp plvcatlill llglsglglg gfllthttgl rspdipqdwv tflrsfgqls
      121 lcpmnetvtg kwqgphvvgl lttlnfggdp drnktqtfqa mipgsqigfk eiagesvlvt
      181 arvasgrtpg tclyfsgipk ilpssqppis cseegagnat lspmmgeecv ivwsherfvl
      241 tklltseela lcgsrllvlg sflvllcgfl ccataacfhp rpefhwsrar l
//
LOCUS       NP_001421159            1067 aa            linear   ROD 28-APR-2025
DEFINITION  pumilio homolog 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001421159 XP_006239941
VERSION     NP_001421159.1
DBSOURCE    REFSEQ: accession NM_001434230.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Yu,S., Wang,M., Xie,Y., Wang,B. and Xu,Y.
  TITLE     MiR-495-3p promotes cardiac hypertrophy by targeting Pum2
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (8), 116-120 (2024)
   PUBMED   39262254
  REMARK    GeneRIF: MiR-495-3p promotes cardiac hypertrophy by targeting Pum2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Yoon,D.S., Choi,Y., Lee,K.M., Ko,E.A., Kim,E.J., Park,K.H. and
            Lee,J.W.
  TITLE     Downregulation of the RNA-binding protein PUM2 facilitates
            MSC-driven bone regeneration and prevents OVX-induced bone loss
  JOURNAL   J Biomed Sci 30 (1), 26 (2023)
   PUBMED   37088847
  REMARK    GeneRIF: Downregulation of the RNA-binding protein PUM2 facilitates
            MSC-driven bone regeneration and prevents OVX-induced bone loss.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Cao,Y., Liu,C., Wang,Q., Wang,W., Tao,E. and Wan,L.
  TITLE     Pum2 mediates Sirt1 mRNA decay and exacerbates
            hypoxia/reoxygenation-induced cardiomyocyte apoptosis
  JOURNAL   Exp Cell Res 393 (1), 112058 (2020)
   PUBMED   32437714
  REMARK    GeneRIF: Pum2 mediates Sirt1 mRNA decay and exacerbates
            hypoxia/reoxygenation-induced cardiomyocyte apoptosis.
REFERENCE   4  (residues 1 to 1067)
  AUTHORS   Martinez,J.C., Randolph,L.K., Iascone,D.M., Pernice,H.F.,
            Polleux,F. and Hengst,U.
  TITLE     Pum2 Shapes the Transcriptome in Developing Axons through Retention
            of Target mRNAs in the Cell Body
  JOURNAL   Neuron 104 (5), 931-946 (2019)
   PUBMED   31606248
  REMARK    GeneRIF: These results reveal that Pum2 shapes axonal
            transcriptomes by preventing the transport of Pumilio-binding
            elements -containing mRNAs into axons
REFERENCE   5  (residues 1 to 1067)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   6  (residues 1 to 1067)
  AUTHORS   Fiore,R., Khudayberdiev,S., Christensen,M., Siegel,G.,
            Flavell,S.W., Kim,T.K., Greenberg,M.E. and Schratt,G.
  TITLE     Mef2-mediated transcription of the miR379-410 cluster regulates
            activity-dependent dendritogenesis by fine-tuning Pumilio2 protein
            levels
  JOURNAL   EMBO J 28 (6), 697-710 (2009)
   PUBMED   19197241
  REMARK    GeneRIF: Mef2-induced expression of at least three individual
            miRNAs of the miR379-410 cluster is required for activity-dependent
            dendritic outgrowth of hippocampal neurons.
REFERENCE   7  (residues 1 to 1067)
  AUTHORS   Ginter-Matuszewska,B., Spik,A., Rembiszewska,A., Koyias,C.,
            Kupryjanczyk,J. and Jaruzelska,J.
  TITLE     The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1
            proteins in human male germ cells
  JOURNAL   Mol Hum Reprod 15 (3), 173-179 (2009)
   PUBMED   19168546
REFERENCE   8  (residues 1 to 1067)
  AUTHORS   Galgano,A., Forrer,M., Jaskiewicz,L., Kanitz,A., Zavolan,M. and
            Gerber,A.P.
  TITLE     Comparative analysis of mRNA targets for human PUF-family proteins
            suggests extensive interaction with the miRNA regulatory system
  JOURNAL   PLoS One 3 (9), e3164 (2008)
   PUBMED   18776931
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1067)
  AUTHORS   Vessey,J.P., Vaccani,A., Xie,Y., Dahm,R., Karra,D., Kiebler,M.A.
            and Macchi,P.
  TITLE     Dendritic localization of the translational repressor Pumilio 2 and
            its contribution to dendritic stress granules
  JOURNAL   J Neurosci 26 (24), 6496-6508 (2006)
   PUBMED   16775137
REFERENCE   10 (residues 1 to 1067)
  AUTHORS   White,E.K., Moore-Jarrett,T. and Ruley,H.E.
  TITLE     PUM2, a novel murine puf protein, and its consensus RNA-binding
            site
  JOURNAL   RNA 7 (12), 1855-1866 (2001)
   PUBMED   11780640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Oct 24, 2024 this sequence version replaced XP_006239941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.24875.1,
                                           SRR22582424.1231399.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..1067
                     /product="pumilio homolog 2 isoform 1"
                     /note="pumilio 2"
                     /calculated_mol_wt=114229
     Region          722..1045
                     /region_name="Pumilio"
                     /note="Pumilio-family RNA binding domain; cd07920"
                     /db_xref="CDD:153420"
     Site            order(778..779,782,814..815,818,853,856,888..889,892,
                     921..922,924..925,928,957..958,960..961,964,1000..1001,
                     1003..1004,1007,1037,1040)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153420"
     CDS             1..1067
                     /gene="Pum2"
                     /coded_by="NM_001434230.1:238..3441"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298874"
                     /db_xref="RGD:1311024"
ORIGIN      
        1 mnhdfqalal esrgmgellp tkkfwepdds tkdgqkgifl gddewretaw gtshhsmsqp
       61 imvqrrsgqs fhgnsevnai lsprsesggl gvsmveyvls sspadkldsr frkgtfgtrd
      121 aetdgpekgd qkgkaspfee dqnrdlkqdd edskingrgl pngmdadckd fnrtpgsrqa
      181 sptevverlg pstnppeglg plpnptankp lveefsnpet qnldamdqvg ldslqfdypg
      241 nqvpmdssga tvglfdynsq qqlfqrtnal tvqqltaaqq qqyalaaaqq phiagvfsag
      301 lapaafvpnp yiisaappgt dpytaaglaa aatlagpavv ppqyygvpwg vypanlfqqq
      361 aaaaasntan qqaasqaqpg qqqvlrpgag qrpitpsqgq qgqqaeslaa aaaanptlaf
      421 gqslaagmpg yqvlaptayy dqtgalvvgp gartglgapv rlmaptpvli ssaaaqaaaa
      481 aaaaggtans ltgstnglfr pigtqppqqq qqqqpstnlq snsfygsssl tnssqssslf
      541 shgpgqpgsa slgfgsgssl gaaigsalsg fgssvgssas ssatrresls tssdlykrss
      601 sslapigqpf ynslgfsssp spigmplpsq tpghsltppp slsshgssss lhlggltngs
      661 gryisaapga eakyrsasst sslfssssql fppsrlrynr sdimpsgrsr lledfrnnrf
      721 pnlqlrdlmg hivefsqdqh gsrfiqqkle ratpaerqmv fneivqaayq lmtdvfgnyv
      781 iqkffefgsl dqklalanri rghvlplalq mygcrviqka lesissdqqv isemvkeldg
      841 hvlkcvkdqn gnhvvqkcie cvqpqslqfi idafkgqvfv lsthpygcrv iqrilehcta
      901 eqtlpileel hqhteqlvqd qygnyviqhv lehgrpedks kivseirgkv lalsqhkfas
      961 nvvekcvtha sraerallid evccqndgph salytmmkdq yanyvvqkmi dmaepaqrki
     1021 imhkirphit tlrkytygkh ilaklekyyl knspdlgpig gppngml
//
LOCUS       NP_001161472             521 aa            linear   ROD 28-APR-2025
DEFINITION  mesoderm induction early response protein 3 [Rattus norvegicus].
ACCESSION   NP_001161472 XP_001074643 XP_226757
VERSION     NP_001161472.1
DBSOURCE    REFSEQ: accession NM_001168000.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Huang,W., Chen,J., Liu,X., Liu,X., Duan,S., Chen,L., Liu,X.,
            Lan,J., Zou,Y., Guo,D. and Zhou,J.
  TITLE     MIER3 induces epithelial-mesenchymal transition and promotes breast
            cancer cell aggressiveness via forming a co-repressor complex with
            HDAC1/HDAC2/Snail
  JOURNAL   Exp Cell Res 406 (1), 112722 (2021)
   PUBMED   34242623
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Zhang,H., Wang,L., Bai,J., Jiao,W. and Wang,M.
  TITLE     MIER3 suppresses the progression of non-small cell lung cancer by
            inhibiting Wnt/beta-Catenin pathway and histone acetyltransferase
            activity
  JOURNAL   Transl Cancer Res 9 (1), 346-357 (2020)
   PUBMED   35117188
  REMARK    Erratum:[Transl Cancer Res. 2020 Nov;9(11):7379-7380. doi:
            10.21037/tcr-2020-005. PMID: 35129549]
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Derwish,R., Paterno,G.D. and Gillespie,L.L.
  TITLE     Differential HDAC1 and 2 Recruitment by Members of the MIER Family
  JOURNAL   PLoS One 12 (1), e0169338 (2017)
   PUBMED   28046085
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 521)
  AUTHORS   denDekker,A.D., Xu,X., Vaughn,M.D., Puckett,A.H., Gardner,L.L.,
            Lambring,C.J., Deschenes,L. and Samuelson,D.J.
  TITLE     Rat Mcs1b is concordant to the genome-wide association-identified
            breast cancer risk locus at human 5q11.2 and MIER3 is a candidate
            cancer susceptibility gene
  JOURNAL   Cancer Res 72 (22), 6002-6012 (2012)
   PUBMED   22993404
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On or before Nov 23, 2009 this sequence version replaced
            XP_226757.3, XP_001074643.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ013732.1, SRR26643288.8446.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..521
                     /product="mesoderm induction early response protein 3"
                     /note="mesoderm induction early response 1, family member
                     3"
                     /calculated_mol_wt=58230
     Region          149..197
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          255..299
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(255,285..286,288..289,291..293,295..297)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          309..521
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..521
                     /gene="Mier3"
                     /gene_synonym="RGD1311241"
                     /coded_by="NM_001168000.2:48..1613"
                     /db_xref="GeneID:310086"
                     /db_xref="RGD:1311241"
ORIGIN      
        1 mlvhdydder tleeeelmgd gknfsseied lekegnmple dllafygyes tiptvanssa
       61 nsspselade lpdmtldkee iakdllsgdd eetqssaddl tpsvtshets dffprplrsn
      121 ttcdgdkese iedvetdsgn spedlrkeim iglqyqaeip pylgeysgde kayenedqll
      181 wrpdvvlesk vkeylietsl rtgnekvldr issgthtrdn eqalyellkc nhnvteaier
      241 yccngkasqe gmtawteeec rsfehalmly gkdfhliqkn kvrsrtvaec vafyymwkks
      301 erydyfaqqt kfgkkrynhh pgvtdymdrl vdeteslgdt vsssaltsnr pepipdqpln
      361 ilssftasdl taltnsvatv cnptdvscld dsfsplgnap rgqvnhvpvv teelltlpsn
      421 gesdcfnlfe tgfyhselnp mcseeserpa krlkmgiavp esfmnevsvn nlgvdfenht
      481 hhitsakmav svadfgslsa setngfinah tlhqhaalhs e
//
LOCUS       NP_001418889            1296 aa            linear   ROD 28-APR-2025
DEFINITION  DENN domain containing 5B isoform 1 [Rattus norvegicus].
ACCESSION   NP_001418889 XP_038964851
VERSION     NP_001418889.1
DBSOURCE    REFSEQ: accession NM_001431960.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1296)
  AUTHORS   Gordon,S.M., Neufeld,E.B., Yang,Z., Pryor,M., Freeman,L.A., Fan,X.,
            Kullo,I.J., Biesecker,L.G. and Remaley,A.T.
  TITLE     DENND5B Regulates Intestinal Triglyceride Absorption and Body Mass
  JOURNAL   Sci Rep 9 (1), 3597 (2019)
   PUBMED   30837651
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1296)
  AUTHORS   Yoshimura,S., Gerondopoulos,A., Linford,A., Rigden,D.J. and
            Barr,F.A.
  TITLE     Family-wide characterization of the DENN domain Rab GDP-GTP
            exchange factors
  JOURNAL   J Cell Biol 191 (2), 367-381 (2010)
   PUBMED   20937701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 24, 2024 this sequence version replaced XP_038964851.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.17940.1,
                                           SRR26643287.12520.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q44"
     Protein         1..1296
                     /product="DENN domain containing 5B isoform 1"
                     /note="DENN/MADD domain containing 5B; DENN
                     domain-containing protein 5B"
                     /calculated_mol_wt=146989
     Region          19..142
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Region          209..397
                     /region_name="DENN"
                     /note="DENN (AEX-3) domain; pfam02141"
                     /db_xref="CDD:460461"
     Region          521..596
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     Region          749..954
                     /region_name="RUN1_DENND5B"
                     /note="RUN1 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17691"
                     /db_xref="CDD:439053"
     Site            order(766,770,773,777,780,929,933,936..937,939,943..944)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439053"
     Region          958..1066
                     /region_name="PLAT_RAB6IP1"
                     /note="PLAT/LH2 domain present in RAB6 interacting protein
                     1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an
                     eight stranded beta-barrel. In RabIP1 this domain may
                     participate in lipid-mediated modulation of Rab6IP1's
                     function via it's generally proposed...; cd01757"
                     /db_xref="CDD:238855"
     Region          1113..1291
                     /region_name="RUN2_DENND5B"
                     /note="RUN2 domain found in DENN domain-containing protein
                     5B (DENND5B) and similar proteins; cd17693"
                     /db_xref="CDD:439055"
     CDS             1..1296
                     /gene="Dennd5b"
                     /coded_by="NM_001431960.1:257..4147"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100365679"
                     /db_xref="RGD:2318606"
ORIGIN      
        1 msgsgaapgp gsgsspaacr fahyfvlcgi dadsglepde lavlyqwlea drhgksqdaa
       61 nttsgenfdq splrrtfksk vlahypqnie wnpfdqdavn mlcmpkglsf rtqadnkdpq
      121 fhsfiitred gsrtygfvlt fyeevtskqi ctamqtlyqm hnaeqyssvy assscsmdsl
      181 assidegdat sllklqryns ydinrdtlyv sksiclitpl pfmqacrkfl lqlhkavtsq
      241 qppplplesy ihnilyevpl pppgrslkfy gvyepvicqr pgpnelplsd yplreacell
      301 glenlvqvft cvllemqill ysqdyqrlmt vaegittllf pfqwqhvyvp ilpasllhfl
      361 dapvpylmgl qskegtdrsk lelpqeanlc fvdidnhfie lpeefpqfpn kvdfiqelse
      421 vllqfgippe gslhcsesat klknmvlkdl andkkngnvp tnnvsvyell kgsetiarlq
      481 alakrtgvtv gkidfpasls ekekdlklqc eeadlrdsql nvqlrevfan rftqmfadye
      541 afviqtaqdm eswltsreqm qnfdkasfls dqpepylpfl srfietqmfa tfidnkimsq
      601 weekdpllrv fdsriekmrl ynvraptlrt siyqkcsslk eaaqsieqrl mkmdhtaihp
      661 hlldmkigqg kyeqgffpkl qsdvlatgpa nnnrwvsrst taqrrkerlr qnaehiglds
      721 dlrekymqea rslgknlrqp klsdlspavi aqtnwkfveg llkecrmktk rmlvekmghe
      781 avelghgean itgleentli aslcdlleri wshgllvkqg ksalwshliq fqdreekqeh
      841 ltdspvalgp errksdsgvm lptlrvsliq dmrhvqnmte iktdvgrara wirlslekkl
      901 lsqhlkqlls nqpltkklyk ryaflrceee reqflyhlls lnavdyfcft svfttimipy
      961 rsviipikkl snaiitsnpw icvsgelgdt gvmqipknll emtfecqnlg klttvqighd
     1021 nsgllakwlv dcvmvrneit ghtyrfpcgr wlgkgvddgs leriligelm tsasdedlgk
     1081 qcrtppqqks ptttrrlsit sltgkpakpn agqiqegige avnnivkhfh kpekergslt
     1141 vllcgenglv aaleqvfhhg fksarifhkn vfiwdfveka vayfestdqi ldneddmliq
     1201 kpscktfchy vnavntaprn igkdgkfqil vclgtrdhll pqwipllaec paitrmyeen
     1261 allrdhmtvn slirilqtiq dftivlegsl ikgvdv
//
LOCUS       NP_001099535             226 aa            linear   ROD 28-APR-2025
DEFINITION  occludin/ELL domain-containing protein 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001099535 XP_001065228 XP_214288
VERSION     NP_001099535.1
DBSOURCE    REFSEQ: accession NM_001106065.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001065228.1, XP_214288.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM389499.1, BP499055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..226
                     /product="occludin/ELL domain-containing protein 1 isoform
                     1"
                     /note="occludin/ELL domain-containing protein 1"
                     /calculated_mol_wt=25746
     Region          113..214
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..226
                     /gene="Ocel1"
                     /gene_synonym="RGD1563236; RGD1565407"
                     /coded_by="NM_001106065.2:347..1027"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:290628"
                     /db_xref="RGD:1565407"
ORIGIN      
        1 mqipagpssr rrsrgplacg sqsrrsgpda tcnsrpaagg rqsatapcmp arerpqprag
       61 rphcqprpse lrtrprkivf adelqprapl hpekhprdlg prpnpvpdye lkyppvtsrr
      121 drsryaavfq dqyeeflelq rqvgamqakl qqlealllsl ppprsqkevr maahvrrefe
      181 kkrvdpgfld kqarcdylkg klrhlkaqir kfddqrdsns ensvyf
//
LOCUS       NP_001103060             239 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein LOC690415 [Rattus norvegicus].
ACCESSION   NP_001103060 XP_001074400
VERSION     NP_001103060.1
DBSOURCE    REFSEQ: accession NM_001109590.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PREDICTED REFSEQ: This record has not been reviewed and the
            function is unknown. The reference sequence was derived from
            CH473988.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001074400.1.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..239
                     /product="uncharacterized protein LOC690415"
                     /calculated_mol_wt=24017
     Region          23..160
                     /region_name="Keratin_B2"
                     /note="Keratin, high sulfur B2 protein; pfam01500"
                     /db_xref="CDD:366678"
     Region          23..63
                     /region_name="Keratin_B2_2"
                     /note="Keratin, high sulfur B2 protein; pfam13885"
                     /db_xref="CDD:464017"
     Region          199..239
                     /region_name="Keratin_B2_2"
                     /note="Keratin, high sulfur B2 protein; pfam13885"
                     /db_xref="CDD:464017"
     CDS             1..239
                     /gene="Krtap10-10l2"
                     /coded_by="NM_001109590.1:1..720"
                     /db_xref="GeneID:690415"
                     /db_xref="RGD:1596091"
ORIGIN      
        1 maastmsvcs dartnsswqv ddcpesccep cgcapsccqp sccvpsccqs sccapsccap
       61 tpcllctpvs cvsspccqss cctpsccqqs scqpacctss pcqqpcgvtl cckpvcctpi
      121 csgsssccqq sscqssccqp sccvtlccrp vcckpvcctp icsasssscc qpsccapvcc
      181 kpvcckpcss lsllcspvcr paccvptssc casscqpscc rpascvsllc rpacscttc
//
LOCUS       NP_001092954             861 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal 2 receptor 56 precursor [Rattus norvegicus].
ACCESSION   NP_001092954 XP_001079237 XP_578648
VERSION     NP_001092954.1
DBSOURCE    REFSEQ: accession NM_001099484.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Young,J.M. and Trask,B.J.
  TITLE     V2R gene families degenerated in primates, dog and cow, but
            expanded in opossum
  JOURNAL   Trends Genet 23 (5), 212-215 (2007)
   PUBMED   17382427
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000007.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_578648.2, XP_001079237.1.
            
            Sequence Note: This record was generated from sequence identified
            by Janet Young (Fred Hutchinson Cancer Research Center).
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..861
                     /product="vomeronasal 2 receptor 56 precursor"
                     /calculated_mol_wt=94536
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3587
     Region          48..511
                     /region_name="PBP1_pheromone_receptor"
                     /note="Ligand-binding domain of the V2R pheromone
                     receptor, a member of the family C receptors within the
                     G-protein coupled receptor superfamily; cd06365"
                     /db_xref="CDD:380588"
     Site            order(76,176..177,401)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:380588"
     Site            order(115,118,159,250)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:380588"
     Region          520..572
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          592..843
                     /region_name="7tmC_V2R_pheromone"
                     /note="vomeronasal type-2 pheromone receptors, member of
                     the class C family of seven-transmembrane G
                     protein-coupled receptors; cd15283"
                     /db_xref="CDD:320410"
     Region          592..617
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(595,598..599,602..603,605..606,640,644,647..648,656,
                     660)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:320410"
     Region          629..650
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320410"
     Site            order(649,661..662,665..666,669,749,754,757..758,761,795,
                     798..799,802,806,814..815,818,821,825)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320410"
     Region          659..683
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320410"
     Region          707..723
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320410"
     Region          750..776
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320410"
     Region          784..807
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320410"
     Region          812..837
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320410"
     CDS             1..861
                     /gene="Vom2r56"
                     /gene_synonym="RGD1559561"
                     /coded_by="NM_001099484.1:1..2586"
                     /db_xref="GeneID:503127"
                     /db_xref="RGD:1559561"
ORIGIN      
        1 madmekaytl ivfflllrls filcsfpeat cfwrinhnen lesnmrkdcg filftipvhl
       61 vedhfrvlld fplpvntypy vlvmlfaiee inknpnllpn stlgftflgd qcditstdln
      121 nlnmlsksge mnpnyiceys fcdvaltgpt wtvsarvgtl lqlfkipqvm lsvtygpfhd
      181 slsdrdlfph lyqiapkdts lvlamvslmi hflwkwvglv ildddqgvqf lsdmkeevkt
      241 neiclafvnm ipanmqlyie raetyyfqim tssanvviiy gnvnstlevs frrwemlgiw
      301 rlwittsqwd visrsrdfti dsfhgtlsls hhyqeistfk hfiqktnfsa ypeavslvrl
      361 gwiylncsvs vcecktlnhc lsntilellp whsfdmamnd eryniynavy avahafhnmr
      421 lqqvdikvle swegliprcm qvndflknvr linpigdpvn inqgrnldam ydifnvlnfp
      481 qgyvlkvkvg qfspyfahdq qlflsedmie watgsrqfst svcsmpchpg fkkshqegka
      541 dccfdcsrcp aneisnttds eecvkcpedw yadteqthcl pkavtflaye dplgmalvcl
      601 alcfsvltal vlgvflkhre tpivkannrt lsyilltali fcflcsllfv gnpntttcil
      661 qqttfgilft vsvstvlakt ltvvlafrit lpgrrmrglm vsripkyiip ictvvqiily
      721 giwlwtsppf vdidthsehg cititcskgs vmafycvlgy lgslalvsft vaflarnlpd
      781 tfneakfltf smlvfcsvwi tflpvyhssk gkvmvavevf silassmgll gcifipkcyi
      841 illrpdrnsi qkfrdktqmn q
//
LOCUS       NP_001257511             467 aa            linear   ROD 28-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform d precursor [Rattus norvegicus].
ACCESSION   NP_001257511
VERSION     NP_001257511.1
DBSOURCE    REFSEQ: accession NM_001270582.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1, Z23279.1 and CR475040.1.
            
            Transcript Variant: This variant (5) lacks two alternate in-frame
            exons compared to variant (1). The resulting isoform (d) has the
            same N- and C-termini but is shorter compared to isoform a.
            Variants 4 and 5 both encode the same isoform (d).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.23141.1, Z23279.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..467
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform d precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=51258
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          149..416
                     /region_name="7tmB1_PACAP-R1"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type 1 receptor, member of the class B family of
                     seven-transmembrane G protein-coupled receptors; cd15987"
                     /db_xref="CDD:320653"
     Region          151..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320653"
     Site            order(156,160,202,205..206,209,226,233,304..305,307,309,
                     365,368,381,385)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320653"
     Region          185..207
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320653"
     Region          226..253
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320653"
     Region          265..285
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320653"
     Region          301..330
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320653"
     Region          346..373
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320653"
     Region          378..403
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320653"
     CDS             1..467
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_001270582.1:338..1741"
                     /note="isoform d precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiylrl arstlllipl
      361 fgihytvfaf spenvskrer lvfelglgsf qgfvvavlyc flngevqaei krkwrswkvn
      421 ryftmdfkhr hpslassgvn ggtqlsilsk sssqlrmssl padnlat
//
LOCUS       NP_112513               1068 aa            linear   ROD 28-APR-2025
DEFINITION  huntingtin-interacting protein 1-related protein isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_112513 XP_001072438 XP_001079139
VERSION     NP_112513.1
DBSOURCE    REFSEQ: accession NM_031234.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Catsburg,L.A., Westra,M., van Schaik,A.M. and MacGillavry,H.D.
  TITLE     Dynamics and nanoscale organization of the postsynaptic endocytic
            zone at excitatory synapses
  JOURNAL   Elife 11, e74387 (2022)
   PUBMED   35072626
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1068)
  AUTHORS   Peng,L., Yang,Q., Xu,X., Du,Y., Wu,Y., Shi,X., Xu,J., Zhu,L. and
            Luo,J.
  TITLE     Huntingtin-Interacting Protein 1-Related Protein Plays a Critical
            Role in Dendritic Development and Excitatory Synapse Formation in
            Hippocampal Neurons
  JOURNAL   Front Mol Neurosci 10, 186 (2017)
   PUBMED   28663723
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1068)
  AUTHORS   Kim,J.H., Yoon,S., Won,M., Sim,S.H., Ko,J.J., Han,S., Lee,K.A.,
            Lee,K. and Bae,J.
  TITLE     HIP1R interacts with a member of Bcl-2 family, BCL2L10, and induces
            BAK-dependent cell death
  JOURNAL   Cell Physiol Biochem 23 (1-3), 43-52 (2009)
   PUBMED   19255499
REFERENCE   4  (residues 1 to 1068)
  AUTHORS   Wilbur,J.D., Chen,C.Y., Manalo,V., Hwang,P.K., Fletterick,R.J. and
            Brodsky,F.M.
  TITLE     Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R
            (Hip1-related protein) is regulated by clathrin light chain
  JOURNAL   J Biol Chem 283 (47), 32870-32879 (2008)
   PUBMED   18790740
REFERENCE   5  (residues 1 to 1068)
  AUTHORS   Jain,R.N., Al-Menhali,A.A., Keeley,T.M., Ren,J., El-Zaatari,M.,
            Chen,X., Merchant,J.L., Ross,T.S., Chew,C.S. and Samuelson,L.C.
  TITLE     Hip1r is expressed in gastric parietal cells and is required for
            tubulovesicle formation and cell survival in mice
  JOURNAL   J Clin Invest 118 (7), 2459-2470 (2008)
   PUBMED   18535670
REFERENCE   6  (residues 1 to 1068)
  AUTHORS   Hyun,T.S., Rao,D.S., Saint-Dic,D., Michael,L.E., Kumar,P.D.,
            Bradley,S.V., Mizukami,I.F., Oravecz-Wilson,K.I. and Ross,T.S.
  TITLE     HIP1 and HIP1r stabilize receptor tyrosine kinases and bind
            3-phosphoinositides via epsin N-terminal homology domains
  JOURNAL   J Biol Chem 279 (14), 14294-14306 (2004)
   PUBMED   14732715
REFERENCE   7  (residues 1 to 1068)
  AUTHORS   Okano,A., Usuda,N., Furihata,K., Nakayama,K., Bao Tian,Q.,
            Okamoto,T. and Suzuki,T.
  TITLE     Huntingtin-interacting protein-1-related protein of rat (rHIP1R) is
            localized in the postsynaptic regions
  JOURNAL   Brain Res 967 (1-2), 210-225 (2003)
   PUBMED   12650982
  REMARK    GeneRIF: Localization of HIP1r at postsynaptic spines in rat brain
            suggests a role of HIP1r for vesicle trafficking through
            interaction with F-actin and working together with huntingtin and
            HIP1 at the synaptic sites.
REFERENCE   8  (residues 1 to 1068)
  AUTHORS   Legendre-Guillemin,V., Metzler,M., Charbonneau,M., Gan,L.,
            Chopra,V., Philie,J., Hayden,M.R. and McPherson,P.S.
  TITLE     HIP1 and HIP12 display differential binding to F-actin, AP2, and
            clathrin. Identification of a novel interaction with clathrin light
            chain
  JOURNAL   J Biol Chem 277 (22), 19897-19904 (2002)
   PUBMED   11889126
REFERENCE   9  (residues 1 to 1068)
  AUTHORS   Engqvist-Goldstein,A.E., Warren,R.A., Kessels,M.M., Keen,J.H.,
            Heuser,J. and Drubin,D.G.
  TITLE     The actin-binding protein Hip1R associates with clathrin during
            early stages of endocytosis and promotes clathrin assembly in vitro
  JOURNAL   J Cell Biol 154 (6), 1209-1223 (2001)
   PUBMED   11564758
REFERENCE   10 (residues 1 to 1068)
  AUTHORS   Engqvist-Goldstein,A.E., Kessels,M.M., Chopra,V.S., Hayden,M.R. and
            Drubin,D.G.
  TITLE     An actin-binding protein of the Sla2/Huntingtin interacting protein
            1 family is a novel component of clathrin-coated pits and vesicles
  JOURNAL   J Cell Biol 147 (7), 1503-1518 (1999)
   PUBMED   10613908
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB005052.1 and BC169096.1.
            
            On or before Sep 6, 2008 this sequence version replaced
            XP_001072438.1, XP_001079139.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..1068
                     /product="huntingtin-interacting protein 1-related protein
                     isoform 2"
                     /calculated_mol_wt=119294
     Region          30..299
                     /region_name="ANTH"
                     /note="ANTH domain; pfam07651"
                     /db_xref="CDD:400137"
     Site            order(37,47,49..50)
                     /site_type="other"
                     /note="PtdIns(4,5)P2-binding site [chemical binding]"
                     /db_xref="CDD:340811"
     Region          <355..>638
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          461..559
                     /region_name="HIP1_clath_bdg"
                     /note="Clathrin-binding domain of Huntingtin-interacting
                     protein 1; pfam16515"
                     /db_xref="CDD:465154"
     Region          814..1012
                     /region_name="ILWEQ"
                     /note="I/LWEQ domain; smart00307"
                     /db_xref="CDD:214607"
     CDS             1..1068
                     /gene="Hip1r"
                     /coded_by="NM_031234.1:37..3243"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:81917"
                     /db_xref="RGD:621615"
ORIGIN      
        1 mnsiknvpar vlsrrpghsl eaereqfdkt qaisiskain sqeapvkekh arriilgthh
       61 ekgaftfwsy aiglplpsss ilswkfchvl hkvlrdghpn vlhdcqryrs nireigdlwg
      121 hlrdqyghlv niytkllltk isfhlkhpqf paglevtdev lekaagtdvn nifqltvemf
      181 dymdcelkls esvfrqlnta iavsqmssgq crlapliqvi qdcshlyhyt vklmfklhsc
      241 lpadtlqghr drfheqfhsl rnffrrasdm lyfkrliqip rlpegppnfl rasalaehik
      301 pvvvipeeap eeeepenlie issgppagep vvvadlfdqt fgppngsmkd drdlqienlk
      361 revetlrael ekikmeaqry isqlkgqvns leaeleeqrk qkqkalvdne qlrhelaqlk
      421 alqlegarnq glreeaerka satearyskl kekhnelint haellrknad takqltvtqq
      481 sqeevarvke qlafqmeqvk resemkmeeq sdqleklkre lvakagelah aqealsrteq
      541 sgselssrld tlnaekeals gairqreael laaqslvrek eealsqeqqr saqekgelqg
      601 rlaekesqeq glqqklldeq favlrgaaae aeailqdavs klddplhlrc tsspdylvsr
      661 aqaaldsvsg lekghtqyla ssedasalva altrfshlaa dtivnggats hlaptdpadr
      721 lidtcrecga ralelmgqlq dqtklpraqp slmraplqgi lqlgqdlkpk sldvrqeelg
      781 amvdkemaat saaiedavrr iedmmnqarh essgvklevn erilnsctdl mkairllvmt
      841 stslqkeive sgrgaatqqe fyaknsrwte glisaskavg wgatqlvesa dkvvlhmgky
      901 eelivcshei aastaqlvaa skvkanknsp hlsrlqecsr tvneraanvv astksgqeqi
      961 edrdtmdfsg lsliklkkqe metqvrvlel ektleaervr lgelrkqhyv laggmgtpge
     1021 eepsrpspap rsgatkkppl aqkpsiaprp dnqldkkdgv ypaqlvny
//
LOCUS       NP_001380622            1770 aa            linear   ROD 28-APR-2025
DEFINITION  sodium leak channel NALCN isoform 1 [Rattus norvegicus].
ACCESSION   NP_001380622
VERSION     NP_001380622.1
DBSOURCE    REFSEQ: accession NM_001393693.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Kang,Y., Wu,J.X. and Chen,L.
  TITLE     Structure of voltage-modulated sodium-selective NALCN-FAM155A
            channel complex
  JOURNAL   Nat Commun 11 (1), 6199 (2020)
   PUBMED   33273469
  REMARK    GeneRIF: Structure of voltage-modulated sodium-selective
            NALCN-FAM155A channel complex.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Al-Sayed,M.D., Al-Zaidan,H., Albakheet,A., Hakami,H., Kenana,R.,
            Al-Yafee,Y., Al-Dosary,M., Qari,A., Al-Sheddi,T., Al-Muheiza,M.,
            Al-Qubbaj,W., Lakmache,Y., Al-Hindi,H., Ghaziuddin,M., Colak,D. and
            Kaya,N.
  TITLE     Mutations in NALCN cause an autosomal-recessive syndrome with
            severe hypotonia, speech impairment, and cognitive delay
  JOURNAL   Am J Hum Genet 93 (4), 721-726 (2013)
   PUBMED   24075186
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Koroglu,C., Seven,M. and Tolun,A.
  TITLE     Recessive truncating NALCN mutation in infantile neuroaxonal
            dystrophy with facial dysmorphism
  JOURNAL   J Med Genet 50 (8), 515-520 (2013)
   PUBMED   23749988
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Lu,B., Su,Y., Das,S., Liu,J., Xia,J. and Ren,D.
  TITLE     The neuronal channel NALCN contributes resting sodium permeability
            and is required for normal respiratory rhythm
  JOURNAL   Cell 129 (2), 371-383 (2007)
   PUBMED   17448995
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Nash,H.A., Scott,R.L., Lear,B.C. and Allada,R.
  TITLE     An unusual cation channel mediates photic control of locomotion in
            Drosophila
  JOURNAL   Curr Biol 12 (24), 2152-2158 (2002)
   PUBMED   12498692
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Lee,J.H., Cribbs,L.L. and Perez-Reyes,E.
  TITLE     Cloning of a novel four repeat protein related to voltage-gated
            sodium and calcium channels
  JOURNAL   FEBS Lett 445 (2-3), 231-236 (1999)
   PUBMED   10094463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2232786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q25"
     Protein         1..1770
                     /product="sodium leak channel NALCN isoform 1"
                     /note="sodium leak channel non-selective protein; sodium
                     leak channel NALCN; brain voltage-gated cation channel;
                     voltage gated channel-like protein 1; four domain-type
                     voltage-gated ion channel alpha-1 subunit; voltage gated
                     channel like 1; rb21-channel"
                     /calculated_mol_wt=203844
     Region          36..331
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            66..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            107..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            174..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            295..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          383..603
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            417..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            448..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            473..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            503..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            570..599
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          762..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          887..1161
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            887..906
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            916..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            948..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            981..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1016..1039
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            1130..1159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          1209..1458
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1211..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1237..1260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1272..1293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1297..1318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1332..1357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1421..1447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     CDS             1..1770
                     /gene="Nalcn"
                     /gene_synonym="Vgcnl1"
                     /coded_by="NM_001393693.1:317..5629"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:266760"
                     /db_xref="RGD:628710"
ORIGIN      
        1 mlkrkqssrv eaqpvtdfgp deslsdnadi lwinkpwvhs llricaiisv isvcmntpmt
       61 fehypplqyv tftldtllmf lytaemiakm hirgivkgds syvkdrwcvf dgfmvfclwv
      121 slvlqvfeia divdqmspwg mlriprplim irafriyfrf elprtritni lkrsgeqiws
      181 vsifllffll lygilgvqmf gtftyhcvvn dtkpgnvtwn slaipdthcs peleegyqcp
      241 pgfkcmdled lglsrqelgy sgfneigtsi ftvyeassqe gwvflmyrai dsfprwrsyf
      301 yfitliffla wlvknvfiav iietfaeirv qfqqmwgtrs sttstattqm fhedaaggwq
      361 lvavdvnkpq grapaclqkm mrssvfhmfi lsmvtvdviv aasnyykgen frrqydefyl
      421 aevaftvlfd leallkiwcl gftgyisssl hkfelllvig ttlhvypdly hsqftyfqvl
      481 rvvrlikisp aledfvykif gpgkklgslv vftasllivm saislqmfcf veeldrfttf
      541 prafmsmfqi ltqegwvdvm dqtlnavghm waplvaiyfi lyhlfatlil lslfvavild
      601 nleldedlkk lkqlkqsean adtkeklplr lrifekfpnr pqmvkisklp sdftvpkire
      661 sfmkqfidrq qqdtcclfri lpstsssscd npkrptvedn kyidqklrks vfsirarnll
      721 eketavtkil ractrqrmls gsfegqpake rsilsvqhhi rqerrslrhg snsqrisrgk
      781 sletltqdhs ntvryrnaqr edseikmiqe kkeqaemkrk vqeeelrenh pyfdkplfiv
      841 grehrfrnfc rvvvrarfna sktdpvtgav kntkyhqlyd llglvtyldw vmitvticsc
      901 ismmfespfr rvmhaptlqi aeyvfvifms ielnlkimad glfftptavi rdfggvmdif
      961 iylvsliflc wmpqnvpaes gaqllmvlrc lrplrifklv pqmrkvvrel fsgfkeiflv
     1021 sillltlmlv fasfgvqlfa gklakcndpn iirredcngi frinvsvskn lnlklrpgek
     1081 kpgfwvprvw anprnfnfdn vgnamlalfe vlslkgwvev rdviihrvgp ihgiyihvfv
     1141 flgcmigltl fvgvvianfn enkgtalltv dqrrwedlks rlkiaqplhl pprpdndgfr
     1201 akmyditqhp ffkrtiallv laqsvllsvk wdvedpvtvp latmsvvftf ifvlevtmki
     1261 iamspagfwq srrnrydllv tslgvvwvvl hfallnayty mmgacvivfr ffsicgkhvt
     1321 lkmllltvvv smyksffiiv gmfllllcya fagvvlfgtv kygeninrha nfssagkait
     1381 vlfrivtged wnkimhdcmv qppfctpdef tywatdcgny agalmyfcsf yviiayimln
     1441 llvaiivenf slfysteedq llsyndlrhf qiiwnmvddk regviptfrv kfllrllrgr
     1501 levdldkdkl lfkhmcyeme rlhnggdvtf hdvlsmlsyr svdirkslql eellareqle
     1561 ytieeevakq tirmwlkkcl krirakqqqs csiihslres qqqelsrfln ppsiettqps
     1621 edtnansqdh ntqpesssqq qllsptlsdr ggsrqdaadt gkpqrkigqw rlpsaaiaek
     1681 tapvnkmssy sqdpereeee vskgflapkp ishsvssvnl rfggrttmks vvckmnpmpd
     1741 tascgsevkk wwtrqltves desgddlldi
//
LOCUS       NP_001402708            1031 aa            linear   ROD 28-APR-2025
DEFINITION  delphilin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001402708 XP_006248927
VERSION     NP_001402708.1
DBSOURCE    REFSEQ: accession NM_001415779.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Takeuchi,T., Ohtsuki,G., Yoshida,T., Fukaya,M., Wainai,T.,
            Yamashita,M., Yamazaki,Y., Mori,H., Sakimura,K., Kawamoto,S.,
            Watanabe,M., Hirano,T. and Mishina,M.
  TITLE     Enhancement of both long-term depression induction and optokinetic
            response adaptation in mice lacking delphilin
  JOURNAL   PLoS One 3 (5), e2297 (2008)
   PUBMED   18509461
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Chaki,S., Yoshikawa,R. and Okuyama,S.
  TITLE     Group II metabotropic glutamate receptor-mediated regulation of
            dopamine release from slices of rat nucleus accumbens
  JOURNAL   Neurosci Lett 404 (1-2), 182-186 (2006)
   PUBMED   16781059
  REMARK    GeneRIF: Group II mGluRs may play a significant role in regulating
            dopamine release in the nucleus accumbens.
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Yamashita,T., Miyagi,Y., Ono,M., Ito,H., Watanabe,K., Sonoda,T.,
            Tsuzuki,K., Ozawa,S., Aoki,I., Okuda,K., Mishina,M. and Kawamoto,S.
  TITLE     Identification and characterization of a novel Delphilin variant
            with an alternative N-terminus
  JOURNAL   Brain Res Mol Brain Res 141 (1), 83-94 (2005)
   PUBMED   16168524
REFERENCE   4  (residues 1 to 1031)
  AUTHORS   Miyagi,Y., Yamashita,T., Fukaya,M., Sonoda,T., Okuno,T., Yamada,K.,
            Watanabe,M., Nagashima,Y., Aoki,I., Okuda,K., Mishina,M. and
            Kawamoto,S.
  TITLE     Delphilin: a novel PDZ and formin homology domain-containing
            protein that synaptically colocalizes and interacts with glutamate
            receptor delta 2 subunit
  JOURNAL   J Neurosci 22 (3), 803-814 (2002)
   PUBMED   11826110
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Dec 29, 2022 this sequence version replaced XP_006248927.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.79646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..1031
                     /product="delphilin isoform 2"
                     /note="delphilin; glutamate receptor, ionotropic, delta 2
                     (Grid2) interacting protein 1"
                     /calculated_mol_wt=113255
     Region          <12..29
                     /region_name="harmonin_N_like"
                     /note="N-terminal protein-binding module of harmonin and
                     similar domains, also known as HHD (harmonin homology
                     domain); cl11968"
                     /db_xref="CDD:448372"
     Region          97..170
                     /region_name="PDZ2_L-delphilin-like"
                     /note="PDZ domain 2 of delphilin (L-delphilin isoform),
                     and related domains; cd06744"
                     /db_xref="CDD:467226"
     Site            order(105..111,119,122,151,155,158..159)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467226"
     Region          206..285
                     /region_name="HN_L-delphilin-R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of
                     L-delphilin, and related domains; cd07355"
                     /db_xref="CDD:259821"
     Site            order(207,210,214,227,230,233..234,237)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259821"
     Region          640..1008
                     /region_name="FH2"
                     /note="Formin Homology 2 Domain; pfam02181"
                     /db_xref="CDD:396655"
     CDS             1..1031
                     /gene="Grid2ip"
                     /coded_by="NM_001415779.1:92..3187"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:288484"
                     /db_xref="RGD:1310492"
ORIGIN      
        1 mgkdqgfsrh frifipkkhr arfdevvsqg llgklcrarr aqgaqrlrrs rseerperll
       61 vstrasaapr rpdeppprka asllggrtgp ggprrtvrvy kgnksfgftl rghgpvwies
      121 vlpgspaena slksgdrilf lngldmrncs hdkvvsmlqg sgamptlvve egpvpfasds
      181 dsldsptras altslqwvad ilpssirvqg rtfsqqldhl ltpperygvc ralesffqhr
      241 sidtlivdvy pvldtpakqv lwqflyqllt yeeqelcqek iacflgytai tepessldle
      301 pestpeptpe pqprsslras smcrrslrsq gleaslscgp gdcsemplpl ipgerqagdg
      361 tslpetpnpk mmsavyaele srlnsgfkgk igtvsksras ppvpslvgts gprtlsgvsw
      421 pgdrllpspc ydplcsggla spssseshpy asldssraps pqpglgsihp dsppspdpir
      481 ppsrrklfaf srpvrsrdtd rfldvlseql gprvtivddf ltpendyeem sfhddqgsfv
      541 tnerssasec vssseegssl tyssisdhip ppplsppppp plpfhdpkps srtsdgprgp
      601 pqsltkpltq ishpvppppp pplpppvpca ppmisrgvgh rrsetshmsv krlrweqven
      661 segtiwgqlg edsdydklsd mvkyldlelh fgtqkppkpv pgpepfrkke vveilshkka
      721 yntsillahl kltpgelrqv lmsmeprrle pahlaqlllf apdadeeqry qafreapgrl
      781 sepdqfvlqm lsvpeyktrl rslhfqatlq ekteeirgsl eclrqaslel knsrklakil
      841 efvlamgnyl ndgqpktnkt tgfkinflte lnstktvdgk stflhilaks lsqhfpellg
      901 faqdlptvpl aakvnqralt vdladlhdtv seiqvacqsm vpssedrfav vmtsfletaq
      961 palraldglq reameelgka laffgedska ttseaffgif sefmskfera lsdlqagdgp
     1021 rssgmvspla w
//
LOCUS       NP_001418517             653 aa            linear   ROD 28-APR-2025
DEFINITION  sciellin isoform 2 [Rattus norvegicus].
ACCESSION   NP_001418517 XP_038949459
VERSION     NP_001418517.1
DBSOURCE    REFSEQ: accession NM_001431588.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Chou,C.K., Fan,C.C., Lin,P.S., Liao,P.Y., Tung,J.C., Hsieh,C.H.,
            Hung,M.C., Chen,C.H. and Chang,W.C.
  TITLE     Sciellin mediates mesenchymal-to-epithelial transition in
            colorectal cancer hepatic metastasis
  JOURNAL   Oncotarget 7 (18), 25742-25754 (2016)
   PUBMED   27013588
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Pyle,A.L., Li,B., Maupin,A.B., Guzman,R.J., Crimmins,D.L.,
            Olson,S., Atkinson,J.B. and Young,P.P.
  TITLE     Biomechanical stress induces novel arterial intima-enriched genes:
            implications for vascular adaptation to stress
  JOURNAL   Cardiovasc Pathol 19 (2), e13-e20 (2010)
   PUBMED   19211270
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Champliaud,M.F., Viel,A. and Baden,H.P.
  TITLE     The expression of vitamin D-upregulated protein 1 in skin and its
            interaction with sciellin in cultured keratinocytes
  JOURNAL   J Invest Dermatol 121 (4), 781-785 (2003)
   PUBMED   14632196
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Champliaud,M.F., Baden,H.P., Koch,M., Jin,W., Burgeson,R.E. and
            Viel,A.
  TITLE     Gene characterization of sciellin (SCEL) and protein localization
            in vertebrate epithelia displaying barrier properties
  JOURNAL   Genomics 70 (2), 264-268 (2000)
   PUBMED   11112355
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Champliaud,M.F., Burgeson,R.E., Jin,W., Baden,H.P. and Olson,P.F.
  TITLE     cDNA cloning and characterization of sciellin, a LIM domain protein
            of the keratinocyte cornified envelope
  JOURNAL   J Biol Chem 273 (47), 31547-31554 (1998)
   PUBMED   9813070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            On Jul 19, 2024 this sequence version replaced XP_038949459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.54945.1,
                                           SRR26643290.46954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q21"
     Protein         1..653
                     /product="sciellin isoform 2"
                     /calculated_mol_wt=72742
     Region          585..643
                     /region_name="LIM"
                     /note="Zinc-binding domain present in Lin-11, Isl-1,
                     Mec-3; smart00132"
                     /db_xref="CDD:214528"
     Site            order(586,589,609,612,615,618,640,643)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..653
                     /gene="Scel"
                     /coded_by="NM_001431588.1:148..2109"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361086"
                     /db_xref="RGD:1305102"
ORIGIN      
        1 msnfssrkks pvgndpkstq gaalrqqgfh dvnkrraflq dnswikklpe eekdenygrv
       61 vlsrhnshda ldrkiterde pkatisryrs edmldrslst frtpestktp agssfsantt
      121 apstpattpv kkkrqswfpp pppghnapps tgasrrdppl hpplppkpcs piaspkqlrq
      181 shrqmhmata gacgeadrha arnirtedld diirvaaalq ktdkgeeldn lirmnkslnr
      241 nqgldglfra nlkaqqldkr aqslesliym ntqmdrdgkg nqafgsfkki nqradtergs
      301 qdqrsiirtn amaerssrrg kdldsvmkis pkghesatgk qdlgglinvn petnksmkrg
      361 qslenlikvt levnrsskgg qsldnfikav patdranqgs qgldslmkvt psanksnqhs
      421 ldelvntspk avkttaghqd ldkfikvnad vltnnqrnhd ldnsirgnpt vnrcdqrdqd
      481 lkgltevnsr vsedknervd gqangvtnsl rkesprtsvy shetktslss nsgtrnagpk
      541 dtvvytrtyv enskspkdgy qenisgkyiq tvystsdrsv ierdmctycr kplgvetkmi
      601 ldelqicchs tcfkceickr plenlqagds iwiyrqtihc epcyskvmak wiq
//
LOCUS       NP_001333232             973 aa            linear   ROD 28-APR-2025
DEFINITION  similar to Est1p-like protein B isoform 2 [Rattus norvegicus].
ACCESSION   NP_001333232
VERSION     NP_001333232.1
DBSOURCE    REFSEQ: accession NM_001346303.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start site compared to variant 1. The encoded isoform
            (2) has a shorter N-terminus than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.2170939.1,
                                           SRR26360194.1044639.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840106
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q31"
     Protein         1..973
                     /product="similar to Est1p-like protein B isoform 2"
                     /calculated_mol_wt=111375
     Region          68..180
                     /region_name="EST1"
                     /note="Telomerase activating protein Est1; pfam10374"
                     /db_xref="CDD:463062"
     Region          164..198
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(165,168..169,172..173,175,205,208..209,212,214..215,
                     240,243,246..247,250)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          189..>390
                     /region_name="EST1_DNA_bind"
                     /note="Est1 DNA/RNA binding domain; pfam10373"
                     /db_xref="CDD:431239"
     Region          203..233
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          239..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          817..973
                     /region_name="PIN_Smg5-like"
                     /note="VapC-like PIN domain of human nonsense-mediated
                     decay factor Smg5, and other similar eukaryotic homologs;
                     cd09884"
                     /db_xref="CDD:350232"
     Site            822
                     /site_type="other"
                     /note="conserved Asp residue"
                     /db_xref="CDD:350232"
     CDS             1..973
                     /gene="Smg5l1"
                     /gene_synonym="RGD1309489"
                     /coded_by="NM_001346303.1:364..3285"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:314915"
                     /db_xref="RGD:1309489"
ORIGIN      
        1 meknqeetlr atflyqevcl aaqrldiflq kenahkevfk phvlalreml qqaciklmfl
       61 hpvvygrkae ellwrkiysd ivmllmktnk kqmdtfqhwg eplqahlkag lkfyehlflf
      121 lqghyelrlq syidwphnai hligckkvgp tsveeaswar machrcllyl gdlfryqhef
      181 ldlatknlae rcyyralsva pnmgmpfnql galmgskyyd leatyyyqrc lhaevpfkga
      241 awnlkrlydh agkrysclkr yqgrklshsq rqcwdnkrll vsflylqsll qpkrkfkaar
      301 lialcqlvld dfrlclsyrp yqsglcqasi edkppkgylf lpdflifhmv vlclmnvhsl
      361 rksgskqqkp aviftltlfs ylvqhvntri qaelqkrklt peeaalrdgc wdkepgkehq
      421 dfpspglqnn hsqkshkwsg icreseasfh sccdsdetee densslssqa qsdtgsetsh
      481 sdttdeegsg slgsdeiqks ggspkpkrah srnklkayvp pdslldllkt tissslpapl
      541 sqklqgkhas plapvfshnv ltpptdptpt valssslgte geissfpete fymgssweqr
      601 sfitqnnlqt tqwkldilsa egllptikvi lswlrsnhsl llshwrsvcs lwdhlsvlln
      661 llpsvgdlqh pglclshhlq dllqscqwpn tpkylqlped ialfqqsspq vsqdreglgq
      721 dppqltnqee vivricffrs fghfatrlpg qflrfdsklg ifvsstlers esapqqfprt
      781 tprirlskdi vqlwlqreva llektlrspq trsvltpylf pdpralcehl sviqklatsa
      841 kffliipkiv vdtlyilkwe drralaaitf ledelkrrnq yilcqsfvsk rlvrprmtkp
      901 dsdawdlyni lefcksllds srpgildpss mvmiitgvcl ehprnfsypl qlvlgmatea
      961 gveiknilsf hke
//
LOCUS       NP_001030003             520 aa            linear   ROD 28-APR-2025
DEFINITION  zinc finger protein 384 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001030003
VERSION     NP_001030003.1
DBSOURCE    REFSEQ: accession NM_001034831.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Hayata,T., Nakamoto,T., Ezura,Y. and Noda,M.
  TITLE     Ciz, a transcription factor with a nucleocytoplasmic shuttling
            activity, interacts with C-propeptides of type I collagen
  JOURNAL   Biochem Biophys Res Commun 368 (2), 205-210 (2008)
   PUBMED   18211825
  REMARK    GeneRIF: These results revealed that Ciz interacts with
            C-propeptides of type I collagen and this association takes place
            in nuclei.
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Shah,R., Alvarez,M., Jones,D.R., Torrungruang,K., Watt,A.J.,
            Selvamurugan,N., Partridge,N.C., Quinn,C.O., Pavalko,F.M.,
            Rhodes,S.J. and Bidwell,J.P.
  TITLE     Nmp4/CIZ regulation of matrix metalloproteinase 13 (MMP-13)
            response to parathyroid hormone in osteoblasts
  JOURNAL   Am J Physiol Endocrinol Metab 287 (2), E289-E296 (2004)
   PUBMED   15026307
  REMARK    GeneRIF: Nmp4/CIZ is a component of a multiprotein assemblage or
            enhanceosome within the MMP-13 parathyroid hormone response region
            and that, within this context, Nmp4/CIZ promotes both basal
            expression and hormonal synergy.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Torrungruang,K., Shah,R., Alvarez,M., Bowen,D.K., Gerard,R.,
            Pavalko,F.M., Elmendorf,J.S., Charoonpatrapong,K., Hock,J.,
            Rhodes,S.J. and Bidwell,J.P.
  TITLE     Osteoblast intracellular localization of Nmp4 proteins
  JOURNAL   Bone 30 (6), 931-936 (2002)
   PUBMED   12052465
  REMARK    GeneRIF: localization in the cytoplasm of osteoblasts[Nmp4 -
            nuclear matrix protein 4]
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Thunyakitpisal,P., Alvarez,M., Tokunaga,K., Onyia,J.E., Hock,J.,
            Ohashi,N., Feister,H., Rhodes,S.J. and Bidwell,J.P.
  TITLE     Cloning and functional analysis of a family of nuclear matrix
            transcription factors (NP/NMP4) that regulate type I collagen
            expression in osteoblasts
  JOURNAL   J Bone Miner Res 16 (1), 10-23 (2001)
   PUBMED   11149472
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Nakamoto,T., Yamagata,T., Sakai,R., Ogawa,S., Honda,H., Ueno,H.,
            Hirano,N., Yazaki,Y. and Hirai,H.
  TITLE     CIZ, a zinc finger protein that interacts with p130(cas) and
            activates the expression of matrix metalloproteinases
  JOURNAL   Mol Cell Biol 20 (5), 1649-1658 (2000)
   PUBMED   10669742
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF216806.1, SRR26643292.19947.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..520
                     /product="zinc finger protein 384 isoform 2"
                     /note="nuclear matrix transcription factor 4; nuclear
                     matrix protein 4; Cas-associated zinc finger protein"
                     /calculated_mol_wt=56094
     Region          <209..395
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          231..251
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(264,266,268,270..271,274..275,278,292,294,298..299,
                     302..303,306,322,324,326,328..329,332..333,336)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          271..296
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          299..326
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          315..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          375..395
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..520
                     /gene="Zfp384"
                     /gene_synonym="Ciz; Nmp4; Znf384"
                     /coded_by="NM_001034831.2:204..1766"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:171018"
                     /db_xref="RGD:708346"
ORIGIN      
        1 meeshfnsnp yfwpsiptvs gqientmfin kmkdqllpek gcglapphyp tlltvpasvs
       61 lssgismdte skseqltphs qasvtqnitv vpvpstglmt agvscsqrwr regsqsrgpg
      121 lvitspsgsl vttassaqtf pistpmivsa lppgsqalqv vpdlskkvas tlteeggggg
      181 ggggtvappk pprgrkkkrm lesglpemnd pyvlapgddd dhqkdgktyr crmcsltfys
      241 ksemqihsks htetkphkcp hcsktfanss ylaqhirihs gakpyscnfc eksfrqlshl
      301 qqhtrihtgd rpykcahpgc ekaftqlsnl qshrrqhnkd kpfkchnchr aytdaaslea
      361 hlsthtvkha kvytcticsr aytsetylmk hmrkhnppdl qqqvqaaaaa aavaqaqaqa
      421 qaqaqaqaqa qaqaqaqaqa qaqasqasqq qqqqqppppq pphfqspgaa pqgggggdsn
      481 qnpppqcsfd ltpykpaehh kdicltvtts tiqvehlass
//
LOCUS       NP_598195                495 aa            linear   ROD 28-APR-2025
DEFINITION  pituitary adenylate cyclase-activating polypeptide type I receptor
            isoform b precursor [Rattus norvegicus].
ACCESSION   NP_598195
VERSION     NP_598195.1
DBSOURCE    REFSEQ: accession NM_133511.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Feher,M., Marton,Z., Szabo,A., Kocsa,J., Kormos,V., Hunyady,A.,
            Kovacs,L.A., Ujvari,B., Berta,G., Farkas,J., Furedi,N., Gaszner,T.,
            Pytel,B., Reglodi,D. and Gaszner,B.
  TITLE     Downregulation of PACAP and the PAC1 Receptor in the Basal Ganglia,
            Substantia Nigra and Centrally Projecting Edinger-Westphal Nucleus
            in the Rotenone model of Parkinson's Disease
  JOURNAL   Int J Mol Sci 24 (14), 11843 (2023)
   PUBMED   37511603
  REMARK    GeneRIF: Downregulation of PACAP and the PAC1 Receptor in the Basal
            Ganglia, Substantia Nigra and Centrally Projecting Edinger-Westphal
            Nucleus in the Rotenone model of Parkinson's Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Minnig,M.A., Blasio,A., Ferragud,A., Sami,Y.N., Erhard,E.E.,
            Clark,R.H., DiLeo,A., Giuliano,C., Everitt,B.J., Cottone,P. and
            Sabino,V.
  TITLE     Pituitary adenylate cyclase-activating polypeptide type 1 receptor
            within the nucleus accumbens core mediates excessive alcohol
            drinking in alcohol-preferring rats
  JOURNAL   Neuropharmacology 212, 109063 (2022)
   PUBMED   35460713
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide type 1
            receptor within the nucleus accumbens core mediates excessive
            alcohol drinking in alcohol-preferring rats.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Maunze,B., Bruckner,K.W., Desai,N.N., Chen,C., Chen,F., Baker,D.
            and Choi,S.
  TITLE     Pituitary adenylate cyclase-activating polypeptide receptor
            activation in the hypothalamus recruits unique signaling pathways
            involved in energy homeostasis
  JOURNAL   Am J Physiol Endocrinol Metab 322 (3), E199-E210 (2022)
   PUBMED   35001657
  REMARK    GeneRIF: Pituitary adenylate cyclase-activating polypeptide
            receptor activation in the hypothalamus recruits unique signaling
            pathways involved in energy homeostasis.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Johnson,G.C., Parsons,R.L., May,V. and Hammack,S.E.
  TITLE     Pituitary adenylate cyclase-activating polypeptide-induced PAC1
            receptor internalization and recruitment of MEK/ERK signaling
            enhance excitability of dentate gyrus granule cells
  JOURNAL   Am J Physiol Cell Physiol 318 (5), C870-C878 (2020)
   PUBMED   32186931
  REMARK    GeneRIF: we examined the direct effects of PACAP on dentate gyrus
            (DG) granule cells in brain slices using whole cell patch
            recordings in current clamp mode. PACAP significantly increased the
            intrinsic excitability of DG granule cells via PAC1 receptor
            activation.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Spengler,D., Waeber,C., Pantaloni,C., Holsboer,F., Bockaert,J.,
            Seeburg,P.H. and Journot,L.
  TITLE     Differential signal transduction by five splice variants of the
            PACAP receptor
  JOURNAL   Nature 365 (6442), 170-175 (1993)
   PUBMED   8396727
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Morrow,J.A., Lutz,E.M., West,K.M., Fink,G. and Harmar,A.J.
  TITLE     Molecular cloning and expression of a cDNA encoding a receptor for
            pituitary adenylate cyclase activating polypeptide (PACAP)
  JOURNAL   FEBS Lett 329 (1-2), 99-105 (1993)
   PUBMED   8394834
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Hashimoto,H., Ishihara,T., Shigemoto,R., Mori,K. and Nagata,S.
  TITLE     Molecular cloning and tissue distribution of a receptor for
            pituitary adenylate cyclase-activating polypeptide
  JOURNAL   Neuron 11 (2), 333-342 (1993)
   PUBMED   8394723
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Hosoya,M., Onda,H., Ogi,K., Masuda,Y., Miyamoto,Y., Ohtaki,T.,
            Okazaki,H., Arimura,A. and Fujino,M.
  TITLE     Molecular cloning and functional expression of rat cDNAs encoding
            the receptor for pituitary adenylate cyclase activating polypeptide
            (PACAP)
  JOURNAL   Biochem Biophys Res Commun 194 (1), 133-143 (1993)
   PUBMED   7687425
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Pisegna,J.R. and Wank,S.A.
  TITLE     Molecular cloning and functional expression of the pituitary
            adenylate cyclase-activating polypeptide type I receptor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6345-6349 (1993)
   PUBMED   8392197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D16465.1, JAXUCZ010000004.1 and CR475040.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant (1). The resulting isoform (b) has the
            same N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D16465.1, SRR26643298.23139.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..495
                     /product="pituitary adenylate cyclase-activating
                     polypeptide type I receptor isoform b precursor"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type IA receptor; PACAP type IA receptor; adenylate
                     cyclase activating polypeptide 1 (pituitary) receptor type
                     I; adenylate cyclase activating polypeptide 1 type 1
                     receptor; ADCYAP receptor type 1; adenylate cyclase
                     activating polypeptide 1 receptor type 1; pituitary
                     adenylate cyclase activating polypeptide 1 receptor (1);
                     pituitary adenylate cyclase activating polypeptide
                     receptor; PACAP-R-1A; adenylate cyclase activating
                     polypeptide 1 receptor 1; PACAP type I receptor; pituitary
                     adenylate cyclase-activating polypeptide type I receptor"
                     /calculated_mol_wt=54475
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1994
     Region          51..136
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          149..444
                     /region_name="7tmB1_PACAP-R1"
                     /note="pituitary adenylate cyclase-activating polypeptide
                     type 1 receptor, member of the class B family of
                     seven-transmembrane G protein-coupled receptors; cd15987"
                     /db_xref="CDD:320653"
     Region          151..176
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320653"
     Site            order(156,160,202,205..206,209,226,233,304..305,307,309,
                     393,396,409,413)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320653"
     Region          185..207
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320653"
     Region          226..253
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320653"
     Region          265..285
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320653"
     Region          301..330
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320653"
     Region          346..401
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320653"
     Region          406..431
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320653"
     CDS             1..495
                     /gene="Adcyap1r1"
                     /gene_synonym="PAC1-R; PACAP-R1; PACAP-R1A; PACAPR1;
                     PACAPR1A"
                     /coded_by="NM_133511.2:338..1825"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:24167"
                     /db_xref="RGD:2038"
ORIGIN      
        1 marvlqlslt alllpvaiam hsdcifkkeq amcleriqra ndlmglness pgcpgmwdni
       61 tcwkpaqvge mvlvscpevf rifnpdqvwm tetigdsgfa dsnsleitdm gvvgrncted
      121 gwsepfphyf dacgfddyep esgdqdyyyl svkalytvgy stslatltta mvilcrfrkl
      181 hctrnfihmn lfvsfmlrai svfikdwily aeqdsshcfv stveckavmv ffhycvvsny
      241 fwlfieglyl ftllvetffp erryfywyti igwgtptvcv tvwavlrlyf ddagcwdmnd
      301 stalwwvikg pvvgsimvnf vlfigiiiil vqklqspdmg gnessiyfsc vqkcyckpqr
      361 aqqhsckmse lstitlrlar stllliplfg ihytvfafsp envskrerlv felglgsfqg
      421 fvvavlycfl ngevqaeikr kwrswkvnry ftmdfkhrhp slassgvngg tqlsilskss
      481 sqlrmsslpa dnlat
//
LOCUS       NP_001014011             449 aa            linear   ROD 28-APR-2025
DEFINITION  ras GTPase-activating protein-binding protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001014011 XP_223243
VERSION     NP_001014011.1
DBSOURCE    REFSEQ: accession NM_001013989.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Xiao,X., He,Z., Tong,S., Dai,L., Xiao,Q., Qin,Z. and Lin,T.
  TITLE     lncRNA XIST knockdown suppresses hypoxia/reoxygenation
            (H/R)-induced apoptosis of H9C2 cells by regulating
            miR-545-3p/G3BP2
  JOURNAL   IUBMB Life 73 (9), 1103-1114 (2021)
   PUBMED   34060227
  REMARK    GeneRIF: lncRNA XIST knockdown suppresses hypoxia/reoxygenation
            (H/R)-induced apoptosis of H9C2 cells by regulating
            miR-545-3p/G3BP2.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hong,H.Q., Lu,J., Fang,X.L., Zhang,Y.H., Cai,Y., Yuan,J., Liu,P.Q.
            and Ye,J.T.
  TITLE     G3BP2 is involved in isoproterenol-induced cardiac hypertrophy
            through activating the NF-kappaB signaling pathway
  JOURNAL   Acta Pharmacol Sin 39 (2), 184-194 (2018)
   PUBMED   28816235
  REMARK    GeneRIF: new insight into the functions of G3BP2
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Matsuki,H., Takahashi,M., Higuchi,M., Makokha,G.N., Oie,M. and
            Fujii,M.
  TITLE     Both G3BP1 and G3BP2 contribute to stress granule formation
  JOURNAL   Genes Cells 18 (2), 135-146 (2013)
   PUBMED   23279204
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Cristea,I.M., Rozjabek,H., Molloy,K.R., Karki,S., White,L.L.,
            Rice,C.M., Rout,M.P., Chait,B.T. and MacDonald,M.R.
  TITLE     Host factors associated with the Sindbis virus RNA-dependent RNA
            polymerase: role for G3BP1 and G3BP2 in virus replication
  JOURNAL   J Virol 84 (13), 6720-6732 (2010)
   PUBMED   20392851
  REMARK    GeneRIF: Two related proteins found in association with nsP4 at
            both times of infection, GTPase-activating protein (SH3 domain)
            binding protein 1 (G3BP1) and G3BP2 were also previously identified
            as associated with sindbis virus nsP2 and nsP3.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Apr 20, 2005 this sequence version replaced XP_223243.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.16953.1,
                                           SRR22582416.1557093.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..449
                     /product="ras GTPase-activating protein-binding protein 2
                     isoform 2"
                     /note="ras GTPase-activating protein-binding protein 2;
                     GTPase activating protein (SH3 domain) binding protein 2"
                     /calculated_mol_wt=50639
     Region          7..135
                     /region_name="NTF2"
                     /note="Nuclear transport factor 2 (NTF2) domain plays an
                     important role in the trafficking of macromolecules, ions
                     and small molecules between the cytoplasm and nucleus.
                     This bi-directional transport of macromolecules across the
                     nuclear envelope requires many...; cd00780"
                     /db_xref="CDD:238403"
     Site            order(35,41,56,81,83..84,93,115,128..130,132,134)
                     /site_type="active"
                     /note="TAP/p15 interaction [active]"
                     /db_xref="CDD:238403"
     Site            order(39,41..42,78..79,81,83..84,91,95..97,101,103..106,
                     109,115,128..130,132..135)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238403"
     Site            order(42..43,68,73,96,98,100..101,103,106,131,133,135)
                     /site_type="active"
                     /note="RanGDP-NTF2 interaction [active]"
                     /db_xref="CDD:238403"
     Region          293..375
                     /region_name="RRM_G3BP2"
                     /note="RNA recognition motif (RRM) found in ras
                     GTPase-activating protein-binding protein 2 (G3BP2) and
                     similar proteins; cd12464"
                     /db_xref="CDD:409897"
     CDS             1..449
                     /gene="G3bp2"
                     /gene_synonym="RGD1309571"
                     /coded_by="NM_001013989.2:215..1564"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:305240"
                     /db_xref="RGD:1309571"
ORIGIN      
        1 mvmekpspll vgrefvrqyy tllnkapeyl hrfygrnssy vhggvdasgk pqeavygqnd
       61 ihhkvlslnf sechtkirhv dahatlsdgv vvqvmgllsn sgqperkfmq tfvlapegsv
      121 pnkfyvhndm fryedevfgd sepeldeese deveeeqedr qpspepvqen ansayyeahp
      181 vtngieeple esshepepep esetkteelk pqaeekhlee leeksatppp tepaslpqep
      241 pkprvdakpe vqsqpprvre qrprerpgfp prgprpgrgd teqndsdnrr iirypdshql
      301 fvgnlphdid enelkeffms fgnvvelrin tkgvggklpn fgfvvfddse pvqriliakp
      361 imfrgevrln veekktraar eretrgggdd rrdirrndrg pggprgivgg gmmrdrdgrg
      421 ppprggmtqk lgsgrgtgqm egrftgqrr
//
LOCUS       NP_001425064             562 aa            linear   ROD 28-APR-2025
DEFINITION  tubby-related protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001425064 XP_063122812
VERSION     NP_001425064.1
DBSOURCE    REFSEQ: accession NM_001438135.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Apr 16, 2025 this sequence version replaced XP_063122812.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.3154.1,
                                           SRR26360181.2039021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..562
                     /product="tubby-related protein 2 isoform 2"
                     /note="tubby-related protein 2; tubby-like protein 2"
                     /calculated_mol_wt=62826
     Region          39..>212
                     /region_name="Tub_N"
                     /note="Tubby N-terminal; pfam16322"
                     /db_xref="CDD:465092"
     Region          308..557
                     /region_name="Tub"
                     /note="Tub family; pfam01167"
                     /db_xref="CDD:460094"
     CDS             1..562
                     /gene="Tulp2"
                     /coded_by="NM_001438135.1:16..1704"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361576"
                     /db_xref="RGD:1310551"
ORIGIN      
        1 mdregprgpr rgtsqeneqw kketledefs gvrlqkleqq rqlfekkqrr krqeplmvqa
       61 npdaslrhrr prrgeerfqs dsswglgvgs pflqenvpqa hlpsgahsal vtmsyvgdgs
      121 gerapllspr gavytrgngp avrhlcwlpd ssdsdveevt medipvisrp pkthlanrrr
      181 gwlaspgpgi seeeevepkd arvedktpsp dpdptensdr vhgdsascnm eentakknie
      241 tasgigdedp ekkeateste tnnalvaskv lqgdgdtsnh sawnmtcpmp rtpgprlged
      301 meayvllpap rehmvqcriv rnkhgvdkgm fpsyylylea edgvavrssp lghfllagrk
      361 rkrsktsnyl isldpkdmsr ngnnfvgkvr snvlgtkfti fdngvnpern ywipdsarir
      421 eelgvvcyet nvlgfrgprk mtvilpgmds rkqrmkvqpq ndqdsilsrv qkgarhglll
      481 lqnkapswsd esgayvlnfh grvtrasvkn fqivhpdepd hlvlqfgrva pniftmdfry
      541 plcplqafai clssfdgkla ce
//
LOCUS       NP_037205                285 aa            linear   ROD 28-APR-2025
DEFINITION  protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform b
            [Rattus norvegicus].
ACCESSION   NP_037205
VERSION     NP_037205.3
DBSOURCE    REFSEQ: accession NM_013073.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Dung,T.T., Yi,Y.S., Heo,J., Yang,W.S., Kim,J.H., Kim,H.G.,
            Park,J.G., Yoo,B.C., Cho,J.Y. and Hong,S.
  TITLE     Critical role of protein L-isoaspartyl methyltransferase in basic
            fibroblast growth factor-mediated neuronal cell differentiation
  JOURNAL   BMB Rep 49 (8), 437-442 (2016)
   PUBMED   26973341
  REMARK    GeneRIF: PIMT was critical for bFGF-mediated neuronal
            differentiation of PC12 cells and regulated the MAPK and Akt
            signaling pathways.
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Kapadia,B., Viswakarma,N., Parsa,K.V., Kain,V., Behera,S.,
            Suraj,S.K., Babu,P.P., Kar,A., Panda,S., Zhu,Y.J., Jia,Y.,
            Thimmapaya,B., Reddy,J.K. and Misra,P.
  TITLE     ERK2-mediated phosphorylation of transcriptional coactivator
            binding protein PIMT/NCoA6IP at Ser298 augments hepatic
            gluconeogenesis
  JOURNAL   PLoS One 8 (12), e83787 (2013)
   PUBMED   24358311
  REMARK    GeneRIF: ERK2-mediated phosphorylation of transcriptional
            coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic
            gluconeogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Yan,G., Qin,Q., Yi,B., Chuprun,K., Sun,H., Huang,S. and Sun,J.
  TITLE     Protein-L-isoaspartate (D-aspartate) O-methyltransferase protects
            cardiomyocytes against hypoxia induced apoptosis through inhibiting
            proapoptotic kinase Mst1
  JOURNAL   Int J Cardiol 168 (4), 3291-3299 (2013)
   PUBMED   23647599
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Boivin,D., Bilodeau,D. and Beliveau,R.
  TITLE     Immunochemical characterization of L-isoaspartyl-protein carboxyl
            methyltransferase from mammalian tissues
  JOURNAL   Biochem J 309 (Pt 3) (Pt 3), 993-998 (1995)
   PUBMED   7639720
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Shirasawa,T., Endoh,R., Zeng,Y.X., Sakamoto,K. and Mori,H.
  TITLE     Protein L-isoaspartyl methyltransferase: developmentally regulated
            gene expression and protein localization in the central nervous
            system of aged rat
  JOURNAL   Neurosci Lett 188 (1), 37-40 (1995)
   PUBMED   7783974
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Mizobuchi,M., Murao,K., Takeda,R. and Kakimoto,Y.
  TITLE     Tissue-specific expression of isoaspartyl protein carboxyl
            methyltransferase gene in rat brain and testis
  JOURNAL   J Neurochem 62 (1), 322-328 (1994)
   PUBMED   8263531
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Cassidy,E.M., Wakim,B.T., Ferguson,A.G. and Samarel,A.M.
  TITLE     Asparaginyl deamidation-methylation of rat ventricular myosin light
            chains
  JOURNAL   J Mol Cell Cardiol 23 (5), 589-601 (1991)
   PUBMED   1886138
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Sato,M., Yoshida,T. and Tuboi,S.
  TITLE     Primary structure of rat brain protein carboxyl methyltransferase
            deduced from cDNA sequence
  JOURNAL   Biochem Biophys Res Commun 161 (1), 342-347 (1989)
   PUBMED   2730663
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 20, 2021 this sequence version replaced NP_037205.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088417.1, SRR26360172.1640875.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..285
                     /product="protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase isoform b"
                     /EC_number="2.1.1.77"
                     /note="protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase; PIMT; protein-beta-aspartate
                     methyltransferase; L-isoaspartyl protein carboxyl
                     methyltransferase; protein L-isoaspartyl/D-aspartyl
                     methyltransferase"
                     /calculated_mol_wt=30248
     Region          66..274
                     /region_name="PCMT"
                     /note="Protein-L-isoaspartate(D-aspartate)
                     O-methyltransferase (PCMT); pfam01135"
                     /db_xref="CDD:395902"
     CDS             1..285
                     /gene="Pcmt1"
                     /gene_synonym="PCM"
                     /coded_by="NM_013073.4:294..1151"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:25604"
                     /db_xref="RGD:3268"
ORIGIN      
        1 mpgarsggsg sdgsnsgrss gdtsgavtvw evvsllgkll gtvaalkvvl yllrvcfama
       61 wksggashse lihnlrkngi iktdkvfevm latdrshyak snpymdspqs igfqatisap
      121 hmhayalell fdqlhegaka ldvgsgsgil tacfarmvgh sgkvigidhi kelvddsitn
      181 vkkddpmlls sgrvrlvvgd grmgfaeeap ydaihvgaaa pvvpqalidq lkpggrlilp
      241 vgpaggnqml eqydklqdgs vkmkplmgvi yvpltdkekq wsrwk
//
LOCUS       NP_001380757             625 aa            linear   ROD 28-APR-2025
DEFINITION  PEX5-related protein isoform 7 [Rattus norvegicus].
ACCESSION   NP_001380757
VERSION     NP_001380757.1
DBSOURCE    REFSEQ: accession NM_001393828.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Foote,K.M., Lyman,K.A., Han,Y., Michailidis,I.E., Heuermann,R.J.,
            Mandikian,D., Trimmer,J.S., Swanson,G.T. and Chetkovich,D.M.
  TITLE     Phosphorylation of the HCN channel auxiliary subunit TRIP8b is
            altered in an animal model of temporal lobe epilepsy and modulates
            channel function
  JOURNAL   J Biol Chem 294 (43), 15743-15758 (2019)
   PUBMED   31492750
  REMARK    GeneRIF: loss of TRIP8b phosphorylation may affect HCN channel
            properties during epileptogenesis.
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Wilkars,W., Wollberg,J., Mohr,E., Han,M., Chetkovich,D.M.,
            Bahring,R. and Bender,R.A.
  TITLE     Nedd4-2 regulates surface expression and may affect N-glycosylation
            of hyperpolarization-activated cyclic nucleotide-gated (HCN)-1
            channels
  JOURNAL   FASEB J 28 (5), 2177-2190 (2014)
   PUBMED   24451387
  REMARK    GeneRIF: Nedd4-2 plays an important role in the regulation of HCN1
            trafficking and may compete with TRIP8b(1a-4) in this process
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Wilkars,W., Liu,Z., Lewis,A.S., Stoub,T.R., Ramos,E.M., Brandt,N.,
            Nicholson,D.A., Chetkovich,D.M. and Bender,R.A.
  TITLE     Regulation of axonal HCN1 trafficking in perforant path involves
            expression of specific TRIP8b isoforms
  JOURNAL   PLoS One 7 (2), e32181 (2012)
   PUBMED   22363812
  REMARK    GeneRIF: TRIP8b isoforms are important regulators of HCN1
            trafficking in entorhinal neurons.
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Sheets,P.L., Suter,B.A., Kiritani,T., Chan,C.S., Surmeier,D.J. and
            Shepherd,G.M.
  TITLE     Corticospinal-specific HCN expression in mouse motor cortex:
            I(h)-dependent synaptic integration as a candidate microcircuit
            mechanism involved in motor control
  JOURNAL   J Neurophysiol 106 (5), 2216-2231 (2011)
   PUBMED   21795621
  REMARK    GeneRIF: Hyperpolarization current expression was high in
            corticospinal neurons and low in corticostriatal and
            corticocortical neurons, a pattern mirrored by mRNA levels for HCN1
            and Trip8b subunits.
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Popova,N.V., Plotnikov,A.N., Ziganshin,R.Kh., Deyev,I.E. and
            Petrenko,A.G.
  TITLE     Analysis of proteins interacting with TRIP8b adapter
  JOURNAL   Biochemistry (Mosc) 73 (6), 644-651 (2008)
   PUBMED   18620529
  REMARK    GeneRIF: A role of TRIP8b in receptor-mediated endocytosis.
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Fransen,M., Amery,L., Hartig,A., Brees,C., Rabijns,A.,
            Mannaerts,G.P. and Van Veldhoven,P.P.
  TITLE     Comparison of the PTS1- and Rab8b-binding properties of Pex5p and
            Pex5Rp/TRIP8b
  JOURNAL   Biochim Biophys Acta 1783 (5), 864-873 (2008)
   PUBMED   18346465
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Santoro,B., Wainger,B.J. and Siegelbaum,S.A.
  TITLE     Regulation of HCN channel surface expression by a novel C-terminal
            protein-protein interaction
  JOURNAL   J Neurosci 24 (47), 10750-10762 (2004)
   PUBMED   15564593
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Amery,L., Sano,H., Mannaerts,G.P., Snider,J., Van Looy,J.,
            Fransen,M. and Van Veldhoven,P.P.
  TITLE     Identification of PEX5p-related novel peroxisome-targeting signal 1
            (PTS1)-binding proteins in mammals
  JOURNAL   Biochem J 357 (Pt 3), 635-646 (2001)
   PUBMED   11463335
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Chen,S., Liang,M.C., Chia,J.N., Ngsee,J.K. and Ting,A.E.
  TITLE     Rab8b and its interacting partner TRIP8b are involved in regulated
            secretion in AtT20 cells
  JOURNAL   J Biol Chem 276 (16), 13209-13216 (2001)
   PUBMED   11278749
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.514018.1,
                                           SRR26360176.2186780.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..625
                     /product="PEX5-related protein isoform 7"
                     /note="PEX5-related protein; pex5Rp; PEX5-like protein;
                     peroxin-5-related protein; peroxin 2; TPR-containing
                     Rab8b-interacting protein; tetratricopeptide
                     repeat-containing Rab8b-interacting protein"
                     /calculated_mol_wt=69367
     Region          231..>426
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(329..330,333..334,336,360,363..364,367..368,
                     370..371,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          329..353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          355..624
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          358..388
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          393..421
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          473..501
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(474,477..478,481..482,484,508,511..512,515..516,
                     518..519,542,545..546,549..550,553)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          506..536
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          541..569
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..625
                     /gene="Pex5l"
                     /gene_synonym="Pex2; TRIP8b; Trjip8b"
                     /coded_by="NM_001393828.2:209..2086"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:286937"
                     /db_xref="RGD:708407"
ORIGIN      
        1 mqmnylkske qgygklssde dleiivdqkq gkgsraadka vamvmkeipr eesaeekpll
       61 tmtsqlvneq qesrpllsps iddflcetks eaiakpvtsn tavlttgldl ldlsepvsqt
      121 qtkakksess skssslkkka dgsdlisada eqraqalrgp etssldldiq tqlekwddvk
      181 fhgdrtskgh lmaerkscss ragskellws sehrsqpels tgksalnses aselelvapa
      241 qarltkehrw gsallsrnhs leeeferaka avesdtefwd kmqaeweema rrnwisenqe
      301 aqnqvtvsas ekgyyfhten pfkdwpgafe eglkrlkegd lpvtilfmea ailqdpgdae
      361 awqflgitqa eneneqaaiv alqrclelqp nnlkalmala vsytntshqq dacealknwi
      421 kqnpkykylv knkkgspglt rrmskspvds svlegvkdly leaahqngdm idpdlqtglg
      481 vlfhlsgefn raidafnaal tvrpedyslw nrlgatlang drseeaveay traleiqpgf
      541 irsrynlgis cinlgayrea vsnfltalsl qrksrnqqqv phpaisgniw aalrialslm
      601 dqpelfqaan lgdldvllra fnldp
//
LOCUS       NP_001100374            1233 aa            linear   ROD 28-APR-2025
DEFINITION  mitogen-activated protein kinase kinase kinase kinase 4 isoform 1
            [Rattus norvegicus].
ACCESSION   NP_001100374 XP_001058422 XP_001058485 XP_001058541 XP_001058590
            XP_001058649 XP_001058712 XP_217381
VERSION     NP_001100374.2
DBSOURCE    REFSEQ: accession NM_001106904.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1233)
  AUTHORS   Yang,J., Zheng,X.G., Wu,Y.L., Wang,A.P., Wang,C.H., Chen,W.X.,
            Zhong,S. and Yang,H.
  TITLE     Intestinal epithelial cell-derived exosomes package microRNA-23a-3p
            alleviate gut damage after ischemia/reperfusion via targeting
            MAP4K4
  JOURNAL   Biomed Pharmacother 149, 112810 (2022)
   PUBMED   35303564
  REMARK    GeneRIF: Intestinal epithelial cell-derived exosomes package
            microRNA-23a-3p alleviate gut damage after ischemia/reperfusion via
            targeting MAP4K4.
REFERENCE   2  (residues 1 to 1233)
  AUTHORS   Li,W., Liu,S., Su,S., Chen,Y. and Sun,G.
  TITLE     Construction and validation of a novel prognostic signature of
            microRNAs in lung adenocarcinoma
  JOURNAL   PeerJ 9, e10470 (2021)
   PUBMED   33510968
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1233)
  AUTHORS   Chen,S., Tang,Y., Yang,C., Li,K., Huang,X. and Cao,J.
  TITLE     Silencing CDC25A inhibits the proliferation of liver cancer cells
            by downregulating IL-6 in vitro and in vivo
  JOURNAL   Int J Mol Med 45 (3), 743-752 (2020)
   PUBMED   31922225
REFERENCE   4  (residues 1 to 1233)
  AUTHORS   Lin,J.C., Lee,Y.C., Tan,T.H., Liang,Y.C., Chuang,H.C., Fann,Y.C.,
            Johnson,K.R. and Lin,Y.J.
  TITLE     RBM4-SRSF3-MAP4K4 splicing cascade modulates the metastatic
            signature of colorectal cancer cell
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (2), 259-272 (2018)
   PUBMED   29138007
REFERENCE   5  (residues 1 to 1233)
  AUTHORS   Gao,X., Chen,G., Gao,C., Zhang,D.H., Kuan,S.F., Stabile,L.P.,
            Liu,G. and Hu,J.
  TITLE     MAP4K4 is a novel MAPK/ERK pathway regulator required for lung
            adenocarcinoma maintenance
  JOURNAL   Mol Oncol 11 (6), 628-639 (2017)
   PUBMED   28306189
REFERENCE   6  (residues 1 to 1233)
  AUTHORS   Bouzakri,K., Ribaux,P. and Halban,P.A.
  TITLE     Silencing mitogen-activated protein 4 kinase 4 (MAP4K4) protects
            beta cells from tumor necrosis factor-alpha-induced decrease of
            IRS-2 and inhibition of glucose-stimulated insulin secretion
  JOURNAL   J Biol Chem 284 (41), 27892-27898 (2009)
   PUBMED   19690174
  REMARK    GeneRIF: Results identify MAP4K4 as a key upstream mediator of
            TNF-alpha action on the beta cell, preventing tumor necrosis
            factor-alpha-induced decrease of IRS-2 and inhibition of
            glucose-stimulated insulin secretion.
REFERENCE   7  (residues 1 to 1233)
  AUTHORS   Loh,S.H., Francescut,L., Lingor,P., Bahr,M. and Nicotera,P.
  TITLE     Identification of new kinase clusters required for neurite
            outgrowth and retraction by a loss-of-function RNA interference
            screen
  JOURNAL   Cell Death Differ 15 (2), 283-298 (2008)
   PUBMED   18007665
REFERENCE   8  (residues 1 to 1233)
  AUTHORS   Machida,N., Umikawa,M., Takei,K., Sakima,N., Myagmar,B.E.,
            Taira,K., Uezato,H., Ogawa,Y. and Kariya,K.
  TITLE     Mitogen-activated protein kinase kinase kinase kinase 4 as a
            putative effector of Rap2 to activate the c-Jun N-terminal kinase
  JOURNAL   J Biol Chem 279 (16), 15711-15714 (2004)
   PUBMED   14966141
REFERENCE   9  (residues 1 to 1233)
  AUTHORS   Yao,Z., Zhou,G., Wang,X.S., Brown,A., Diener,K., Gan,H. and
            Tan,T.H.
  TITLE     A novel human STE20-related protein kinase, HGK, that specifically
            activates the c-Jun N-terminal kinase signaling pathway
  JOURNAL   J Biol Chem 274 (4), 2118-2125 (1999)
   PUBMED   9890973
REFERENCE   10 (residues 1 to 1233)
  AUTHORS   Su,Y.C., Han,J., Xu,S., Cobb,M. and Skolnik,E.Y.
  TITLE     NIK is a new Ste20-related kinase that binds NCK and MEKK1 and
            activates the SAPK/JNK cascade via a conserved regulatory domain
  JOURNAL   EMBO J 16 (6), 1279-1290 (1997)
   PUBMED   9135144
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Mar 3, 2022 this sequence version replaced NP_001100374.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1233
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..1233
                     /product="mitogen-activated protein kinase kinase kinase
                     kinase 4 isoform 1"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=140737
     Region          8..289
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(31..34,37,39,52,54,83,105..108,153,157..158,160,
                     170..171)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          915..1213
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..1233
                     /gene="Map4k4"
                     /coded_by="NM_001106904.2:314..4015"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:301363"
                     /db_xref="RGD:1305322"
ORIGIN      
        1 mandspaksl vdidlsslrd pagifelvev vgngtygqvy kgrhvktgql aaikvmdvte
       61 deeeeiklei nmlkkyshhr niatyygafi kksppghddq lwlvmefcga gsitdlvknt
      121 kgntlkedwi ayisreilrg lahlhihhvi hrdikgqnvl ltenaevklv dfgvsaqldr
      181 tvgrrntfig tpywmapevi acdenpdaty dyrsdlwscg itaiemaega pplcdmhpmr
      241 alfliprnpp prlkskkwsk kffsfiegcl vknymqrpst eqllkhpfir dqpnerqvri
      301 qlkdhidrtr kkrgekdete yeysgseeee eevpeqegep ssivnvpges tlrrdflrlq
      361 qenkerseal rrqqllqeqq lreqeeykrq llaerqkrie qqkeqrrrle eqqrrerear
      421 rqqereqrrr eqeekrrlee lerrrkeeee rrraedekrr vereqeyirr qleeeqrhle
      481 ilqqqllqeq amllhdhrrp haqqppppqq qdrskpsyha pepkphydpa drarevqwsh
      541 laslknnvsp vsrshsfsdp spkfahhhlr sqdpcppsrs eglsqssdsk sevpeptqka
      601 wsrsdsdevp prvpvrttsr spvlsrrdsp lqgsgqqnsq agqrnstssi eprllwerve
      661 klvprpgsgs ssgssnsgsq pgshpgsqsg sgerfrvrss sksegspsqr lenaakkped
      721 kkevfrplkp avridltala kelravedvr pphkvtdyss sseesgttde eeedveqega
      781 ddstsgpedt raasslnlsn getesvktmi vhddvesepa mtpskegtli vrqtqsasst
      841 lqkhkssssf tpfidprllq ispssgttvt svvgfscdgl rpeairqdpt rkgsvvnvnp
      901 tntrpqsdtp eirkykkrfn seilcaalwg vnllvgtesg lmlldrsgqg kvyplisrrr
      961 fqqmdvlegl nvlvtisgkk dklrvyylsw lrnkilhndp evekkqgwtt vgdlegcvhy
     1021 kvvkyerikf lvialkssve vyawapkpyh kfmafksfge lvhkpllvdl tveegqrlkv
     1081 iygscagfha vdvdsgsvyd iylpthiqct ikphaiiilp ntdgmellvc yedegvyvnt
     1141 ygritkdvvl qwgemptsva yirsnqtmgw gekaieirsv etghldgvfm hkraqrlkfl
     1201 cerndkvffa svrsggssqv yfmtlgrtsl lsw
//
LOCUS       NP_001423804             909 aa            linear   ROD 28-APR-2025
DEFINITION  epidermal growth factor receptor substrate 15-like 1 isoform 3
            [Rattus norvegicus].
ACCESSION   NP_001423804 XP_006252866
VERSION     NP_001423804.1
DBSOURCE    REFSEQ: accession NM_001436875.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Mar 24, 2025 this sequence version replaced XP_006252866.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.46658.1,
                                           SRR26643296.35272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..909
                     /product="epidermal growth factor receptor substrate
                     15-like 1 isoform 3"
                     /note="epidermal growth factor receptor substrate 15-like
                     1"
                     /calculated_mol_wt=99356
     Region          19..85
                     /region_name="EH"
                     /note="Eps15 homology domain; found in proteins implicated
                     in endocytosis, vesicle transport, and signal
                     transduction. The alignment contains a pair of EF-hand
                     motifs, typically one of them is canonical and binds to
                     Ca2+, while the other may not bind to Ca2+. A...; cd00052"
                     /db_xref="CDD:238009"
     Site            order(25..27,34..38)
                     /site_type="active"
                     /note="pseudo EF-hand loop [active]"
                     /db_xref="CDD:238009"
     Site            order(43,53,57)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:238009"
     Site            order(61,63,65,72)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238009"
     Region          121..214
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          268..364
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          381..>545
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     CDS             1..909
                     /gene="Eps15l1"
                     /coded_by="NM_001436875.1:35..2764"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:361120"
                     /db_xref="RGD:1565708"
ORIGIN      
        1 maapllplsq qipsgnplye syykqvdpay tgrvgaseaa lflkksglsd ivlgkiwdla
       61 dpegkgfldk qgfyvalrlv acaqsghevt lsnlgltmpp pkfhdtsspl matqssaeah
      121 wavrveekak fdgifesllp vngllsgdkv kpvlmnsklp ldvlgrvwdl sdidkdghld
      181 rdefavamhl vyralekepv psvlppplip pskrkktvfa gavpvlpasp ppkdslrstp
      241 shgsvsslns tgslspkhsv kqtqppvawv vpvadkmrfd eiflktdldl dgyvsgqevk
      301 eifmhsgltq nllahiwala dtrqtgklsk eqfalamyfi qqkvskgidp pqvlspdmvp
      361 psergtpipd sssalgsgef tgvkelddis qeiaqlqrek ysleqdirek eeairqkase
      421 vqelqndldr etsslqelea qkqdaqdrld emdqqkaklr dmlsdvrqkc qdetqtissl
      481 ktqiqsqesd lksqeddlnr akselnrlqq eetqleqsiq agraqletil rslkctqddi
      541 nqarsklsql qeshleahrs leqydqvpdg vsgtslpdla tlnegillae rggfgamddp
      601 fknkallfsn nsqelhpdpf qaedpfksdp fkgadpfkgd pfqsdpfseq qtavtdpfgg
      661 dpfkesdpfh sstsddffkk qtkndpftsd pftknpslps kldpfessdp fssssisskg
      721 sdpfgtldpf gsssfssaeg fadfsqmskp ppsgpfsssl ggtgfsddpf kskqdtpalp
      781 pkkpapprpk ppsgqstpvs qlgssafpes pdpfqplead sgdpfqnkkg fgdpfsgkdp
      841 fapsssakpp kasssgfadf tsfgneeqql awakreseka eqerlarlrr qeqedlelai
      901 alskadmpa
//
LOCUS       NP_001424903             472 aa            linear   ROD 28-APR-2025
DEFINITION  gasdermin D like 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001424903 XP_063119591
VERSION     NP_001424903.1
DBSOURCE    REFSEQ: accession NM_001437974.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Apr 11, 2025 this sequence version replaced XP_063119591.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.847200.1,
                                           SRR26643293.41285.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..472
                     /product="gasdermin D like 1 isoform 1"
                     /note="gasdermin domain containing protein RGD1359449"
                     /calculated_mol_wt=51874
     Region          4..238
                     /region_name="Gasdermin"
                     /note="Gasdermin pore forming domain; pfam04598"
                     /db_xref="CDD:398339"
     Region          258..428
                     /region_name="Gasdermin_C"
                     /note="Gasdermin PUB domain; pfam17708"
                     /db_xref="CDD:407590"
     CDS             1..472
                     /gene="Gsdmdl1"
                     /gene_synonym="RGD1359449"
                     /coded_by="NM_001437974.1:299..1717"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:314959"
                     /db_xref="RGD:1359449"
ORIGIN      
        1 msslflrstk slvrelgrkg elvpvdslns sqrlrpfclv rkkhkhslwp wdtpliptdf
       61 slldvlepgc pdpevnhskp iyswekeaeg ltgavsvsag lqsqvtgsgt ttclsalavq
      121 tlwvspftwe mllekrklrs prpsflqelq srkereslyv vteavetlqd tilqshdqmr
      181 gagqlsllql ghvqvqgqsh vdtekmvsip qgsvlayrvl qlvveedgwa vlyfperklc
      241 rnarvaiafs qesgeesnfy slrdqadsql qdlvtlsser ratllgalqe llrdqqalqe
      301 ledtleqald tgllaqlegp ggcvlcilqd stsnlscskg railyilgal aalsepqhcl
      361 laqsierqil seelelvasi lehncnqtee ttsplptgvl calksedevl ilnlvqgcgl
      421 eleksgcqlp wdptvvpqls alyacltglq lltdpspgls rtvpeeetli cp
//
LOCUS       NP_783182               1157 aa            linear   ROD 28-APR-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-2 isoform 1
            precursor [Rattus norvegicus].
ACCESSION   NP_783182
VERSION     NP_783182.2
DBSOURCE    REFSEQ: accession NM_175592.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1157)
  AUTHORS   Zhang,J., Wu,L., Li,Z. and Fu,G.
  TITLE     miR-1231 exacerbates arrhythmia by targeting calciumchannel gene
            CACNA2D2 in myocardial infarction
  JOURNAL   Am J Transl Res 9 (4), 1822-1833 (2017)
   PUBMED   28469787
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1157)
  AUTHORS   Li,B., Zhao,Q., Wang,L.X., Deng,C.Y., Zeng,F., Wu,T.G., Jiang,Z.F.
            and Xu,D.L.
  TITLE     Effect of beta3-adrenergic receptor on atrial L-type Ca(2+) current
            in rats with chronic heart failure
  JOURNAL   Heart Lung Circ 23 (4), 369-377 (2014)
   PUBMED   24055266
  REMARK    GeneRIF: There was no difference in the mRNA expression of
            alpha2delta-2 (Cacna2d2) between the BRL group and CHF control
            group (0.264 +/- 0.005 vs. 0.243 +/- 0.017, P>0.05), which was also
            higher than in the normal control group (0.137 +/- 0.013, P<0.01).
REFERENCE   3  (residues 1 to 1157)
  AUTHORS   Eroglu,C., Allen,N.J., Susman,M.W., O'Rourke,N.A., Park,C.Y.,
            Ozkan,E., Chakraborty,C., Mulinyawe,S.B., Annis,D.S.,
            Huberman,A.D., Green,E.M., Lawler,J., Dolmetsch,R., Garcia,K.C.,
            Smith,S.J., Luo,Z.D., Rosenthal,A., Mosher,D.F. and Barres,B.A.
  TITLE     Gabapentin receptor alpha2delta-1 is a neuronal thrombospondin
            receptor responsible for excitatory CNS synaptogenesis
  JOURNAL   Cell 139 (2), 380-392 (2009)
   PUBMED   19818485
REFERENCE   4  (residues 1 to 1157)
  AUTHORS   Kaja,S., Todorov,B., van de Ven,R.C., Ferrari,M.D., Frants,R.R.,
            van den Maagdenberg,A.M. and Plomp,J.J.
  TITLE     Redundancy of Cav2.1 channel accessory subunits in transmitter
            release at the mouse neuromuscular junction
  JOURNAL   Brain Res 1143, 92-101 (2007)
   PUBMED   17320843
REFERENCE   5  (residues 1 to 1157)
  AUTHORS   Hatano,S., Yamashita,T., Sekiguchi,A., Iwasaki,Y., Nakazawa,K.,
            Sagara,K., Iinuma,H., Aizawa,T. and Fu,L.T.
  TITLE     Molecular and electrophysiological differences in the L-type Ca2+
            channel of the atrium and ventricle of rat hearts
  JOURNAL   Circ J 70 (5), 610-614 (2006)
   PUBMED   16636499
  REMARK    GeneRIF: The level of the alpha1C (Cacna1c) (Cav1.2) protein was
            decreased (approximately 0.5-fold) and that of alpha2 delta-1
            (Cacna2d1) was increased (approximately 2-fold) in the atrium
            compared with the ventricle
REFERENCE   6  (residues 1 to 1157)
  AUTHORS   Walter,J.T., Alvina,K., Womack,M.D., Chevez,C. and Khodakhah,K.
  TITLE     Decreases in the precision of Purkinje cell pacemaking cause
            cerebellar dysfunction and ataxia
  JOURNAL   Nat Neurosci 9 (3), 389-397 (2006)
   PUBMED   16474392
REFERENCE   7  (residues 1 to 1157)
  AUTHORS   Cole,R.L., Lechner,S.M., Williams,M.E., Prodanovich,P.,
            Bleicher,L., Varney,M.A. and Gu,G.
  TITLE     Differential distribution of voltage-gated calcium channel alpha-2
            delta (alpha2delta) subunit mRNA-containing cells in the rat
            central nervous system and the dorsal root ganglia
  JOURNAL   J Comp Neurol 491 (3), 246-269 (2005)
   PUBMED   16134135
  REMARK    GeneRIF: The alpha2delta-2 subunit is also found in brain regions
            known to be involved in olfaction, somatic motor control, fluid
            homeostasis, ingestive and defensive behaviors, neuroendocrine
            functions, and circadian rhythm.
REFERENCE   8  (residues 1 to 1157)
  AUTHORS   Chu,P.J. and Best,P.M.
  TITLE     Molecular cloning of calcium channel alpha(2)delta-subunits from
            rat atria and the differential regulation of their expression by
            IGF-1
  JOURNAL   J Mol Cell Cardiol 35 (2), 207-215 (2003)
   PUBMED   12606261
REFERENCE   9  (residues 1 to 1157)
  AUTHORS   Barclay,J., Balaguero,N., Mione,M., Ackerman,S.L., Letts,V.A.,
            Brodbeck,J., Canti,C., Meir,A., Page,K.M., Kusumi,K.,
            Perez-Reyes,E., Lander,E.S., Frankel,W.N., Gardiner,R.M.,
            Dolphin,A.C. and Rees,M.
  TITLE     Ducky mouse phenotype of epilepsy and ataxia is associated with
            mutations in the Cacna2d2 gene and decreased calcium channel
            current in cerebellar Purkinje cells
  JOURNAL   J Neurosci 21 (16), 6095-6104 (2001)
   PUBMED   11487633
REFERENCE   10 (residues 1 to 1157)
  AUTHORS   Holz,A., Frank,M., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and
            Schwab,M.E.
  TITLE     Chromosomal localization of the myelin-associated oligodendrocytic
            basic protein and expression in the genetically linked neurological
            mouse mutants ducky and tippy
  JOURNAL   J Neurochem 69 (5), 1801-1809 (1997)
   PUBMED   9349522
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Aug 8, 2024 this sequence version replaced NP_783182.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF486277.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1157
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1157
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform 1 precursor"
                     /note="voltage-dependent calcium channel subunit
                     alpha-2/delta-2; voltage-gated calcium channel subunit
                     alpha-2/delta-2; calcium channel, voltage dependent,
                     alpha2/delta subunit 2; calcium channel,
                     voltage-dependent, alpha 2/delta subunit 2"
                     /calculated_mol_wt=128939
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
                     /calculated_mol_wt=1857
     mat_peptide     19..1157
                     /product="Voltage-dependent calcium channel subunit
                     alpha-2/delta-2. /id=PRO_0000304643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
                     /calculated_mol_wt=128939
     Region          144..268
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          280..459
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(300,302,304,372,404)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          300..304
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          536..645
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            627
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Region          672..1117
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            864
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8CFG6.1)"
     Site            1120..1140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CFG6.1)"
     CDS             1..1157
                     /gene="Cacna2d2"
                     /coded_by="NM_175592.3:215..3688"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:300992"
                     /db_xref="RGD:631360"
ORIGIN      
        1 mavpartcga swpgpvrtar pwpgrgprpc pdprgpasgp arplllllpp llllplltap
       61 gasaysfpqq htmqhwarrl eqeidgvmri fggvqqlrei ykdnrnlfdv qenepqklve
      121 kvagdiesll drkvqalkrl adaaenfqka hrwqdnikee dimyydakad aelddpesed
      181 mergsktsal rldfieepnf knkvnysyta vqiptdiykg stvilnelnw tealenvfie
      241 nrrqdptllw qvfgsatgvt ryypatpwra pkkidlydvr rrpwyiqgas spkdmviivd
      301 vsgsvsgltl klmktsvcem ldtlsdddyv nvasfnekaq pvscfthlvq anvrnkkvfk
      361 eavqgmvakg ttgykagfey afdqlqnsni trancnkmim mftdggedrv qdvfekynwp
      421 nrtvrvftfs vgqhnydvtp lqwmactnkg yyfeipsiga irintqeyld vlgrpmvlag
      481 kdakqvqwtn vyedalglgl vvtgtlpvfn ltqdgpgekk nqlilgvmgi dvalndikrl
      541 tpnytlgang yvfaidlngy vllhpnlkpq ttnfrepvtl dfldaelede nkeeirrsmi
      601 dgdkghkqir tlvksldery idevirnytw vpirstnysl glvlppysty ylqanlsdqi
      661 lqvklpiskl kdfefllpss feseghvfia preyckdlna sdnnteflkn fielmekvtp
      721 dskqcnnfll hnlildtgit qqlvervwrd qdlntyslla vfaatdggit rvfpnkaaed
      781 wtenpepfna sfyrrsldnr gyifkpphqd sllrplelen dtvgvlvsta velslgrrtl
      841 rpavvgvkld leawaekfkv lasnrthqdq pqkqcgpssh cemdcevnne dllcvliddg
      901 gflvlsnqnh qwdqvgrffs evdanlmlal ynnsfytrke sydyqaacap qppgnlgaap
      961 rgvfvptiad flnlawwtsa aawslfqqll ygliyhswfq adpaeaegsp etresscvmk
     1021 qtqyyfgsvn asynaiidcg ncsrlfhaqr ltntnllfvv aekplcsqce vgrllqketh
     1081 cpadgpeqce lvqrpryrrg phicfdynat edtsdcgrga sfppslgvlv slqlllllgl
     1141 pprpqpqihs faasrrl
//
LOCUS       NP_001401152            2428 aa            linear   ROD 28-APR-2025
DEFINITION  myosin phosphatase Rho-interacting protein isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001401152 XP_006246484
VERSION     NP_001401152.1
DBSOURCE    REFSEQ: accession NM_001414223.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2428)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 2428)
  AUTHORS   He,N., Qu,Y.J., Li,D.Y. and Yue,S.W.
  TITLE     RIP3 Inhibition ameliorates chronic constriction injury-induced
            neuropathic pain by suppressing JNK signaling
  JOURNAL   Aging (Albany NY) 13 (21), 24417-24431 (2021)
   PUBMED   34772825
  REMARK    GeneRIF: RIP3 Inhibition ameliorates chronic constriction
            injury-induced neuropathic pain by suppressing JNK signaling.
REFERENCE   3  (residues 1 to 2428)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2428)
  AUTHORS   Huang,J.F., Shang,L., Zhang,M.Q., Wang,H., Chen,D., Tong,J.B.,
            Huang,H., Yan,X.X., Zeng,L.P. and Xiong,K.
  TITLE     Differential neuronal expression of receptor interacting protein 3
            in rat retina: involvement in ischemic stress response
  JOURNAL   BMC Neurosci 14, 16 (2013)
   PUBMED   23374330
  REMARK    GeneRIF: The results indicated that RIP3 is expressed
            differentially in retinal neurons in adult rats, including subsets
            of ganglion cells, amacrine and horizontal cells. RIP3 protein
            levels are elevated rapidly following aHIOP
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2428)
  AUTHORS   Murakami,Y., Matsumoto,H., Roh,M., Suzuki,J., Hisatomi,T.,
            Ikeda,Y., Miller,J.W. and Vavvas,D.G.
  TITLE     Receptor interacting protein kinase mediates necrotic cone but not
            rod cell death in a mouse model of inherited degeneration
  JOURNAL   Proc Natl Acad Sci U S A 109 (36), 14598-14603 (2012)
   PUBMED   22908283
REFERENCE   6  (residues 1 to 2428)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   7  (residues 1 to 2428)
  AUTHORS   Riddick,N., Ohtani,K. and Surks,H.K.
  TITLE     Targeting by myosin phosphatase-RhoA interacting protein mediates
            RhoA/ROCK regulation of myosin phosphatase
  JOURNAL   J Cell Biochem 103 (4), 1158-1170 (2008)
   PUBMED   17661354
  REMARK    GeneRIF: myosin phosphatase-rho interacting protein is a scaffold
            linking RhoA to regulate myosin phosphatase at the stress fiber.
REFERENCE   8  (residues 1 to 2428)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   9  (residues 1 to 2428)
  AUTHORS   Mulder,J., Ariaens,A., van Horck,F.P. and Moolenaar,W.H.
  TITLE     Inhibition of RhoA-mediated SRF activation by p116Rip
  JOURNAL   FEBS Lett 579 (27), 6121-6127 (2005)
   PUBMED   16243315
REFERENCE   10 (residues 1 to 2428)
  AUTHORS   Mulder,J., Poland,M., Gebbink,M.F., Calafat,J., Moolenaar,W.H. and
            Kranenburg,O.
  TITLE     p116Rip is a novel filamentous actin-binding protein
  JOURNAL   J Biol Chem 278 (29), 27216-27223 (2003)
   PUBMED   12732640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Nov 16, 2022 this sequence version replaced XP_006246484.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2428
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..2428
                     /product="myosin phosphatase Rho-interacting protein
                     isoform 4"
                     /note="RIP3; rho-interacting protein 3; Rho interacting
                     protein 3"
                     /calculated_mol_wt=274627
     Region          16..151
                     /region_name="PH_RIP"
                     /note="Rho-Interacting Protein Pleckstrin homology (PH)
                     domain; cd01236"
                     /db_xref="CDD:269942"
     Region          152..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97434; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Region          512..613
                     /region_name="PH_M-RIP"
                     /note="Myosin phosphatase-RhoA Interacting Protein
                     Pleckstrin homology (PH) domain; cd13275"
                     /db_xref="CDD:270094"
     Region          855..>1183
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <1670..>2365
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <2058..>2320
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2428
                     /gene="Mprip"
                     /gene_synonym="M-rip; Mrip; p116Rip; Rhoip3"
                     /coded_by="NM_001414223.1:315..7601"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:116504"
                     /db_xref="RGD:619947"
ORIGIN      
        1 msaakenpcr kfqanifnks kcqncfkpre shllndedlt qakpiyggwl llapdgtdfd
       61 npvhrsrkwq rrffilyehg llryaldemp ttlpqgtinm nqctdvvdge artgqkfslc
      121 iltpdkehfi raetkeiisg wlemlmvypr tnkqnqkkkr kvepptpqep gpakmavtss
      181 sggssgssss sssssipsae kvpttkstlw qeemrakdqp dgtslspvqs psqsqppaac
      241 tpretgldsk edenilsgdr vdggrkvrve sgyfslekak qdlraeeqlp pllsppspst
      301 phsrygcpgs psqelshplh spglpapsrm vysicpdslg easrppnhmd sssaggwgte
      361 ilgstfafka srqyaaladv pkairishre afqverrrle hrtrarspgr eevarlfgne
      421 rrrsqviekf ealdiekaeh metnmliltt pssdtrqgrs erraiprkrd fasetptapl
      481 sdacplsphr raksldrrst essmtpdlln fkkgwltkqy edgqwkkhwf vladqslryy
      541 rdsvaeeaad ldgeinlstc ydvteypvqr nygfqihtke geftlsamts girrnwiqti
      601 mkhvlptsap dvtsslpegk nkstsfdtcl rpsekqeaep gepdpeqkks rarerrregr
      661 sktfdwaefr piqqalaqer astvgssdsg dpgcleaepg elererarrr eerrkrfgml
      721 dtndgpgmed talrmdidrs pgllgtpdlk tqnvhveieq rwhqvettpl reekqvpiap
      781 lhlsledrse rlstheltsl lekeleqsqk easdlleqnr llqdqlrval greqsaregy
      841 vlqtevatsp sgawqrlhrv nqdlqselea qcrrqelitq qiqtlkhsyg eakdairhhe
      901 aeiqtlqtrl gdaaaelaik eqalaklkge lkleqgkvre qleewqhska vlrgqlrase
      961 qklqsteall lektqelrdl etkqalqrdr qkevqrlqec iaelsqqlgt seqaqrlmek
     1021 klkrnytlll esceqekqal lqnlkevedk asayedqlqg hvqqvealqk eklsetckgt
     1081 ervhklqeel eareasirql aqhvqslhde rdlikhqfqe lmervatsdg dvaelqeklk
     1141 greadyqnle hshhrvsiql qsvrtllrek eeelklikea hervlekkdq dlnealvkmi
     1201 algssleete iklqekeecl rrfvsdspkd akepqsttdp teedsgiltl gsvtrvfpgf
     1261 phsqpededp saslgeegss gslsreenii ppksadmpdr egqlqstvks dqgapvkrpr
     1321 irfstiqcqr yihpegcaka wtsstssdts qdqspsedsv sseatpstlp aaadaetyis
     1381 iihsletkly vteeklkdvt vrlesqqgqs qeallalhqq wagteaqlre qlrvsllqas
     1441 tlasqleqer qqkvtniehh sgeledfqak nsqaltclen cweklrslpq anqeegqdac
     1501 aaslaniesm lvsaikalqp waspaesrmq aekekghpme sgiaapmqqp cqpilneqeh
     1561 rkllsaqivl easlinqiad slksttsnvy gvlceltqsg ewplkkesaa psagapmeiw
     1621 akkvlvngef wsqveslskh lgtlgeetac tsadkqqhvp qsladatwir aelsyatqsv
     1681 relfhhrlqs iqetlqgtqa alqqhkcmlg eilgayqtpd ferviqqile tlrhptdred
     1741 hvqtswdqsp lgevlrpgtd gsqeplqafh qspevlaaiq delaqqlrek asileeisaa
     1801 lpvlpptepl ggcqrllqms qhlsydacle glgqyssllv qdaiiqaqvc yaacrirley
     1861 ekelqfykka cqeargascq krtqavgalk eeyeellhkq kseyqkvitl iekentelka
     1921 kvsqldhqqr clqeaeskhs esmfalqgry eeeircmveq lshtentlqa ersrvlsqld
     1981 asvkdrqame qhhvqqmkml edrfqlkvre lqavhqeelr alqehyiwsm rgalslcqps
     2041 hpdsplapgp sepravpaak deaesmtglr eriqeleaqm gvmreelghk elegdvaalq
     2101 ekyqrdfesl katcergfaa meethqkkie dlqrqhqrel eklreekdrl laeetaatis
     2161 aieamknahr eemereleks qrsqissins diealrrqyl eelqsvqrel evlseqysqk
     2221 clenahlaqa leaerqalrq cqrenqelna hnqelnnrla aeitrlrtll tgegggestg
     2281 lpltqgkday elevllrvke seiqylkqei sslkdelqta lrdkkyasdk ykdiytelsi
     2341 akakadcdis rlkeqlkaat ealgekspeg ttvsgydimk sksnpdflkk drscvtrqlr
     2401 nirskslkeg ltvqerlklf esrdlkkd
//
LOCUS       NP_001420209             542 aa            linear   ROD 28-APR-2025
DEFINITION  ankyrin repeat and ubiquitin domain containing 1 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001420209 XP_002729082
VERSION     NP_001420209.1
DBSOURCE    REFSEQ: accession NM_001433280.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Aug 8, 2024 this sequence version replaced XP_002729082.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582424.1551789.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN09345238, SAMN09345329
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..542
                     /product="ankyrin repeat and ubiquitin domain containing 1
                     isoform 1"
                     /note="no mechanoreceptor potential C-like"
                     /calculated_mol_wt=61084
     Region          1..78
                     /region_name="Ubl1_ANKUB1"
                     /note="ubiquitin-like (Ubl) domain 1 found in Ankyrin
                     repeat and ubiquitin domain-containing 1 (ANKUB1) and
                     similar proteins; cd17050"
                     /db_xref="CDD:340570"
     Region          80..162
                     /region_name="Ubl2_ANKUB1"
                     /note="ubiquitin-like (Ubl) domain 2 found in Ankyrin
                     repeat and ubiquitin domain-containing 1 (ANKUB1) and
                     similar proteins; cd17051"
                     /db_xref="CDD:340571"
     Region          195..232
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          196..296
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Site            order(197..198,201..203,205..206,210,213,232,234,236,
                     245..246,249..251,253..254,258,261,271,273,275,279..280,
                     283..285,287..288,292,295)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          234..271
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..542
                     /gene="Ankub1"
                     /coded_by="NM_001433280.1:197..1825"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100361272"
                     /db_xref="RGD:2320491"
ORIGIN      
        1 mrifiafegs feafdvaaht svgaikqmvk dyfhiplsed kqgrwylelt yagaalknnw
       61 slsdvgisfc stlkcfvkke dkptlyvfna vtqetmaike nmsildrkvs dlrmlvtlsc
      121 gfpvsvyclr tpaglemydc ntlkdyqtdi gttlrldvwd gwkeflmgcl lgqkpkvqry
      181 lskegpvlky qkrvalyiaa fhghteltew alkqgaqphe avgvhpcraw chealhtdvs
      241 ncpihaaaea gqllilkafv nfsvlcleck naagqsplai askhqhkdcv lyllskiwst
      301 vsflklsvpm riyikikqwi lraqtrrchk sqpsrarvsg akvgdtvmvd gftkpkmtsk
      361 swykaedksw htaqsklppc kqqpsrkpig slpmsqhdtk kqiftfpslv daknfsevqs
      421 yqqenqkkia aparkeknik npylpqvplp pvsrvhyahp qfyctppsgd cllrslfksf
      481 sehsgrtpre naiyclavas afkekrwlqq leiarvlakr sisnltvkgg pakcenypes
      541 vl
//
LOCUS       NP_001421335             656 aa            linear   ROD 28-APR-2025
DEFINITION  RNA-binding protein EWS isoform 1 [Rattus norvegicus].
ACCESSION   NP_001421335 XP_006251265
VERSION     NP_001421335.1
DBSOURCE    REFSEQ: accession NM_001434406.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Parvanov,E.D., Tian,H., Billings,T., Saxl,R.L., Spruce,C.,
            Aithal,R., Krejci,L., Paigen,K. and Petkov,P.M.
  TITLE     PRDM9 interactions with other proteins provide a link between
            recombination hotspots and the chromosomal axis in meiosis
  JOURNAL   Mol Biol Cell 28 (3), 488-499 (2017)
   PUBMED   27932493
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Thomsen,C., Grundevik,P., Elias,P., Stahlberg,A. and Aman,P.
  TITLE     A conserved N-terminal motif is required for complex formation
            between FUS, EWSR1, TAF15 and their oncogenic fusion proteins
  JOURNAL   FASEB J 27 (12), 4965-4974 (2013)
   PUBMED   23975937
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Young,P.J., Francis,J.W., Lince,D., Coon,K., Androphy,E.J. and
            Lorson,C.L.
  TITLE     The Ewing's sarcoma protein interacts with the Tudor domain of the
            survival motor neuron protein
  JOURNAL   Brain Res Mol Brain Res 119 (1), 37-49 (2003)
   PUBMED   14597228
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Delattre,O., Zucman,J., Plougastel,B., Desmaze,C., Melot,T.,
            Peter,M., Kovar,H., Joubert,I., de Jong,P., Rouleau,G. et al.
  TITLE     Gene fusion with an ETS DNA-binding domain caused by chromosome
            translocation in human tumours
  JOURNAL   Nature 359 (6391), 162-165 (1992)
   PUBMED   1522903
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Oct 26, 2024 this sequence version replaced XP_006251265.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1099942.1,
                                           SRR26643291.35935.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..656
                     /product="RNA-binding protein EWS isoform 1"
                     /note="RNA-binding protein EWS; Ewing sarcoma breakpoint
                     region 1; RNA-binding protein EWS-like"
                     /calculated_mol_wt=68287
     Region          361..444
                     /region_name="RRM_EWS"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     Ewing Sarcoma Protein (EWS); cd12533"
                     /db_xref="CDD:409950"
     Region          518..547
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          522..543
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     CDS             1..656
                     /gene="Ewsr1"
                     /coded_by="NM_001434406.1:47..2017"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:289752"
                     /db_xref="RGD:1307258"
ORIGIN      
        1 mastdystys qaaaqqgysa ytaqptqgya qttqaygqqs ygtygqptdv sytqaqstat
       61 ygqtayatsy gqpptgyttp tapqaysqpv qgygtgaydt ttatvtttqa syaaqsaygt
      121 qpaypaygqq paataptrpq dgnkpaetsq pqsstggynq pslgygqsny sypqvpgsyp
      181 mqpvtappsy pptsysssqp tsydqssysq qntygqpssy gqqssygqqs sygqqpptsy
      241 ppqtgsysqa psqysqqsss ygqqssfrqd hpssmgvygq esggfsgpge nrslsgpdnr
      301 grgrggfdrg gmsrggrggg rggmgsager ggfnkpggpm degpdldlgl pidpdedsdn
      361 savyvqglnd svtlddladf fkqcgvvkmn krtgqpmihi yldketgkpk gdatvsyedp
      421 ptakaavewf dgkdfqgskl kvslarkkpp lnsmrggmpp regrgmpppl rggpggpggp
      481 ggpmgrmggr ggdrggfppr gprgsrgnps gggnvqhrag dwqcpnpgcg nqnfawrtec
      541 nqckapkpeg flpppfpppg gdrgrggpgg mrggrgglmd rggpggmfrg grggdrggfr
      601 ggrgmdrggf gggrrggpgg ppgplmeqmg grrggrggpg kmdkgehrqe rrdrpy
//
LOCUS       NP_001386538             129 aa            linear   ROD 28-APR-2025
DEFINITION  anaphase-promoting complex subunit 16 isoform 3 [Rattus
            norvegicus].
ACCESSION   NP_001386538 XP_006256496
VERSION     NP_001386538.1
DBSOURCE    REFSEQ: accession NM_001399609.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000020.1.
            
            On Jan 12, 2022 this sequence version replaced XP_006256496.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ209472.1, FQ216099.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..129
                     /product="anaphase-promoting complex subunit 16 isoform 3"
                     /note="rCG22080-like"
                     /calculated_mol_wt=13652
     Region          46..125
                     /region_name="ANAPC16"
                     /note="Anaphase-promoting complex, subunit 16; pfam17256"
                     /db_xref="CDD:435817"
     CDS             1..129
                     /gene="Anapc16"
                     /coded_by="NM_001399609.1:144..533"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:100360936"
                     /db_xref="RGD:2321124"
ORIGIN      
        1 msarsslsyt neerlllegm aassssssag gvsgssvpgs gfsvsdlapp rkalftypkg
       61 ageiledgse rflcesvfsy qvastlkqvk hdqqvarmek laglveelea dewrfkpieq
      121 llgftpssg
//
LOCUS       NP_001417382             770 aa            linear   ROD 28-APR-2025
DEFINITION  tripartite motif-containing protein 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001417382 XP_063138188
VERSION     NP_001417382.1
DBSOURCE    REFSEQ: accession NM_001430453.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Xu,K., Li,S., Yang,Q., Zhou,Z., Fu,M., Yang,X., Hao,K., Liu,Y. and
            Ji,H.
  TITLE     MicroRNA-145-5p targeting of TRIM2 mediates the apoptosis of
            retinal ganglion cells via the PI3K/AKT signaling pathway in
            glaucoma
  JOURNAL   J Gene Med 23 (11), e3378 (2021)
   PUBMED   34291866
  REMARK    GeneRIF: MicroRNA-145-5p targeting of TRIM2 mediates the apoptosis
            of retinal ganglion cells via the PI3K/AKT signaling pathway in
            glaucoma.
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Thompson,S., Pearson,A.N., Ashley,M.D., Jessick,V., Murphy,B.M.,
            Gafken,P., Henshall,D.C., Morris,K.T., Simon,R.P. and Meller,R.
  TITLE     Identification of a novel Bcl-2-interacting mediator of cell death
            (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and
            its role in rapid ischemic tolerance-induced neuroprotection
  JOURNAL   J Biol Chem 286 (22), 19331-19339 (2011)
   PUBMED   21478148
  REMARK    GeneRIF: a role for TRIM2 in mediating the p42/p44 MAPK-dependent
            ubiquitination of Bim in rapid ischemic tolerance.
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Balastik,M., Ferraguti,F., Pires-da Silva,A., Lee,T.H.,
            Alvarez-Bolado,G., Lu,K.P. and Gruss,P.
  TITLE     Deficiency in ubiquitin ligase TRIM2 causes accumulation of
            neurofilament light chain and neurodegeneration
  JOURNAL   Proc Natl Acad Sci U S A 105 (33), 12016-12021 (2008)
   PUBMED   18687884
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On May 14, 2024 this sequence version replaced XP_063138188.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.1300916.1,
                                           SRR26643297.8021.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..770
                     /product="tripartite motif-containing protein 2 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="tripartite motif protein 2; E3 ubiquitin-protein
                     ligase TRIM2; tripartite motif-containing protein 2;
                     RING-type E3 ubiquitin transferase TRIM2"
                     /calculated_mol_wt=84105
     Region          33..>135
                     /region_name="RAD18"
                     /note="RING-finger-containing E3 ubiquitin ligase [Signal
                     transduction mechanisms]; COG5432"
                     /db_xref="CDD:227719"
     Region          41..91
                     /region_name="RING-HC_TRIM2"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 2 (TRIM2); cd16767"
                     /db_xref="CDD:438423"
     Region          141..182
                     /region_name="Bbox2_TRIM2_C-VII"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing protein 2 (TRIM2) and similar proteins;
                     cd19824"
                     /db_xref="CDD:380882"
     Region          187..313
                     /region_name="BBC"
                     /note="B-Box C-terminal domain; smart00502"
                     /db_xref="CDD:128778"
     Site            order(191,194..195,197..199,202,205,219..220,223,226..227,
                     230..231,234,241..242,245,248..249,252..253,256,266..267,
                     270,274,277..278,281..282,284..285,293,296..297,300,
                     303..304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467844"
     Region          351..447
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          497..770
                     /region_name="NHL_TRIM2_like"
                     /note="NHL repeat domain of the tripartite
                     motif-containing protein 2 (TRIM2) and related proteins;
                     cd14960"
                     /db_xref="CDD:271330"
     Region          515..554
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          562..601
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          604..641
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          648..689
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          695..737
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     Region          740..766
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271330"
     CDS             1..770
                     /gene="Trim2"
                     /coded_by="NM_001430453.1:74..2386"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:361970"
                     /db_xref="RGD:1310981"
ORIGIN      
        1 mpssgrygtq qragsrtagp tcqwsrmase gasipspvvr qidkqflics icleryknpk
       61 vlpclhtfce rclqnyipah sltlscpvcr qtsilpekgv aalqnnffit nlmdvlqrtp
      121 gsngedpsil qtvtavaagk plscpnhdgn vmefycqsce tamcrecteg ehaehptvpl
      181 kdvveqhkas lqvqldavnk rlpeidsalq fiseiihqlt nqkasivddi hstfdelqkt
      241 lnvrksvllm elevnyglkh kvlqsqldtl lqgqesiksc snftaqalnh gtetevllvk
      301 kqmseklnel adqdfplhpr endqldfive teglkksihn lgtilttnav asetvatgeg
      361 lrqtiigqpm svtittkdkd gelcktgnay ltaelstpdg svadgeildn kngtyeflyt
      421 vqkegdftls lrlydqhirg spfklkvirs advspttegv krrvkspgsg hvkqkavkrp
      481 asmystgkrk enpieddlif rvgtkgrnkg eftnlqgvaa stsgkiliad snnqcvqifs
      541 ndgqfksrfg irgrspgqlq rptgvavhps gdiiiadydn kwvsifsndg kfktkigsgk
      601 lmgpkgvsvd rnghiivvdn kaccvfifqp ngkivtrfgs rgngdrqfag phfaavnssn
      661 eiiitdfhnh svkvfnqege fmlkfgsnge gngqfnaptg vavdsngnii vadwgnsriq
      721 vfdgsgsfls yintsadply gpqglaltsd ghvvvadsgn hcfkvyrylq
//
LOCUS       NP_001423420            1309 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear factor related to kappa-B-binding protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001423420 XP_006242815
VERSION     NP_001423420.1
DBSOURCE    REFSEQ: accession NM_001436491.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1309)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   2  (residues 1 to 1309)
  AUTHORS   Watanabe,S. and Peterson,C.L.
  TITLE     The INO80 family of chromatin-remodeling enzymes: regulators of
            histone variant dynamics
  JOURNAL   Cold Spring Harb Symp Quant Biol 75, 35-42 (2010)
   PUBMED   21502417
  REMARK    Review article
REFERENCE   3  (residues 1 to 1309)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Mar 13, 2025 this sequence version replaced XP_006242815.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.11056.1,
                                           SRR26643293.44541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1309
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..1309
                     /product="nuclear factor related to kappa-B-binding
                     protein isoform 1"
                     /calculated_mol_wt=140093
     Region          42..153
                     /region_name="DEUBAD_NFRKB"
                     /note="DEUBAD domain found in nuclear factor related to
                     kappa-B-binding protein (NFRKB) and similar proteins;
                     cd21865"
                     /db_xref="CDD:439381"
     Site            order(49,57,61,65,69,73..75,77,84,88,92,97..100,103..104,
                     107,111,124,128,131..132,135,139,142..143,149..150,153)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439381"
     Region          404..490
                     /region_name="NFRKB_winged"
                     /note="NFRKB Winged Helix-like; pfam14465"
                     /db_xref="CDD:433973"
     Region          <695..899
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <1007..>1185
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..1309
                     /gene="Nfrkb"
                     /coded_by="NM_001436491.1:108..4037"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:315523"
                     /db_xref="RGD:1310558"
ORIGIN      
        1 mdsldhmltd plelgpcgdg hstgimedcl lggtrvslpe dlledpeiff dvvslstwqe
       61 vlsdsqrehl qqflpqfptd tveqqnelil alfsgenfrf gnplhiaqkl frdghfnpev
      121 vkyrqlcfks qykrylssqq qyfhrllrqi lasrsdllem artsgpalpf rhkhhspsrs
      181 peerewrtqq rylkvlrevk eecgdtalss deeatldlqe kfsfedlssw lpssparsps
      241 pavplrvvpt lsttdmktad kielgdsdlk lmlkkhhekr khqpdhpdll tgdltlsdim
      301 trvnagrkgs laalydlavl kkkvkekeek kkkkikliks eaedlaepls ntegvptlsq
      361 apsplaissi keepledikp clgineisss ffsllleill lesqaslpml edrvldwqss
      421 passlnswfs aapnwaelvl palqylages ravpssfspf vefkektqqw kllgqsqdne
      481 kelaalfhlw letkdqafck qenedssdam tpvprvrtdy vvrpstgeek rvfqeqeryr
      541 ysqphkaftf rmhgfesvvg pvkgvfdket slnkarehsl lrsdrpayvt ilslvrdaaa
      601 rlpngegtra eicellkdsq flapdvtstq vntvvsgald rlhyekdpcv kydigrklwi
      661 ylhrdrseee ferihqaqaa aakarkalqq kpkppskvks snkegsvkgl sgpsepsqms
      721 lsdssmpptp vtpvtpttpa lptpispppv savsrsgstt vsepaksssg vllvssptmp
      781 qlgtmlspas iqtppssqtt arvvshsssa glpqvrvvaq pslpavsqqs vgpaqplpqm
      841 pagpqirvpv tatqtkvvpq avvatvpvkg qttaasvqrp gpaqtgltvt slpaavspgs
      901 ktamsspgss apsasttavi qnvtgqniik qvsitgqlgv kpqtgnsipl tatnfriqgk
      961 dvlrlppssi ttdakgqtvl ritpdmmatl aksqvttvkl tqdlfgagsg tagkgisatl
     1021 hvtsnpvhaa dspakapsas vpssapagtt vvkvtpdlkp tetsssafrl mpalgvsvad
     1081 qkgkntvass eakpaatiri vqglgvmppk agqtitvaah akqgasvagg sgtvhsstvs
     1141 lpsinatvsk tvavasgats tpisigtgap tvrqvpvntt vvstsqsgkl ptritvplsv
     1201 isqpmkgksv vtapiikgnl ganlsglgrn iilttmpaga kliagnkpvs fltaqqlqql
     1261 qqqgqatqvr iqtvpashlq qgtasgsska vstvvvttap spkqapeqq
//
LOCUS       NP_001416399             210 aa            linear   ROD 28-APR-2025
DEFINITION  synaptosomal-associated protein 23 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001416399 XP_038961741
VERSION     NP_001416399.1
DBSOURCE    REFSEQ: accession NM_001429470.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Dolai,S., Takahashi,T., Qin,T., Liang,T., Xie,L., Kang,F.,
            Miao,Y.F., Xie,H., Kang,Y., Manuel,J., Winter,E., Roche,P.A.,
            Cattral,M.S. and Gaisano,H.Y.
  TITLE     Pancreas-specific SNAP23 depletion prevents pancreatitis by
            attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes
  JOURNAL   Autophagy 17 (10), 3068-3081 (2021)
   PUBMED   33213278
  REMARK    GeneRIF: Pancreas-specific SNAP23 depletion prevents pancreatitis
            by attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes.
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Serrano-Lopez,E.M., Lopez-Martinez,D., Gomez-Fernandez,J.C.,
            Egea-Jimenez,A.L. and Corbalan-Garcia,S.
  TITLE     PKCepsilon controls the fusion of secretory vesicles in mast cells
            in a phosphatidic acid-dependent mode
  JOURNAL   Int J Biol Macromol 185, 377-389 (2021)
   PUBMED   34147527
  REMARK    GeneRIF: PKCepsilon controls the fusion of secretory vesicles in
            mast cells in a phosphatidic acid-dependent mode.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Naskar,P., Naqvi,N. and Puri,N.
  TITLE     Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23
            leads to massive inhibition in exocytosis from mast cells
  JOURNAL   J Biosci 43 (1), 127-138 (2018)
   PUBMED   29485121
  REMARK    GeneRIF: Blocking dephosphorylation at serine 120 residue in
            SNAP-23 leads to massive inhibition in exocytosis from mast cells.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Weber,P., Batoulis,H., Rink,K.M., Dahlhoff,S., Pinkwart,K.,
            Sollner,T.H. and Lang,T.
  TITLE     Electrostatic anchoring precedes stable membrane attachment of
            SNAP25/SNAP23 to the plasma membrane
  JOURNAL   Elife 6, e19394 (2017)
   PUBMED   28240595
  REMARK    GeneRIF: Electrostatic anchoring precedes stable membrane
            attachment of SNAP25 and SNAP23 to the plasma membrane.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Rao,S.K., Huynh,C., Proux-Gillardeaux,V., Galli,T. and Andrews,N.W.
  TITLE     Identification of SNAREs involved in synaptotagmin VII-regulated
            lysosomal exocytosis
  JOURNAL   J Biol Chem 279 (19), 20471-20479 (2004)
   PUBMED   14993220
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Abonyo,B.O., Gou,D., Wang,P., Narasaraju,T., Wang,Z. and Liu,L.
  TITLE     Syntaxin 2 and SNAP-23 are required for regulated surfactant
            secretion
  JOURNAL   Biochemistry 43 (12), 3499-3506 (2004)
   PUBMED   15035620
  REMARK    GeneRIF: SNAP-23 is expressed in alveolar type II cells of the
            lung; evidence supports its functional role in exocytosis of lung
            surfactant by alveolar type II cells.
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Banerjee,A., Li,G., Alexander,E.A. and Schwartz,J.H.
  TITLE     Role of SNAP-23 in trafficking of H+-ATPase in cultured inner
            medullary collecting duct cells
  JOURNAL   Am J Physiol Cell Physiol 280 (4), C775-C781 (2001)
   PUBMED   11245593
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Okamoto,M., Schoch,S. and Sudhof,T.C.
  TITLE     EHSH1/intersectin, a protein that contains EH and SH3 domains and
            binds to dynamin and SNAP-25. A protein connection between
            exocytosis and endocytosis?
  JOURNAL   J Biol Chem 274 (26), 18446-18454 (1999)
   PUBMED   10373452
REFERENCE   10 (residues 1 to 210)
  AUTHORS   St-Denis,J.F., Cabaniols,J.P., Cushman,S.W. and Roche,P.A.
  TITLE     SNAP-23 participates in SNARE complex assembly in rat adipose cells
  JOURNAL   Biochem J 338 (Pt 3) (Pt 3), 709-715 (1999)
   PUBMED   10051443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038961741.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.2123615.1,
                                           SRR26360181.1541011.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..210
                     /product="synaptosomal-associated protein 23 isoform 1"
                     /note="SNAP-23; vesicle-membrane fusion protein SNAP-23;
                     synaptosomal-associated protein, 23 kD;
                     synaptosomal-associated protein 23"
                     /calculated_mol_wt=23104
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09044; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          86..147
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          104..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70377.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          148..206
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(148,150..151,154..159,161..162,165..166,168..170,
                     172..173,176..177,179..180,182..187,189..190,193,196,200,
                     203,206)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            179
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..210
                     /gene="Snap23"
                     /coded_by="NM_001429470.1:117..749"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:64630"
                     /db_xref="RGD:620221"
ORIGIN      
        1 mddlspeeiq lrahqvtdes lestrrilgl aiesqdagik titmldeqge qlnrieegmd
       61 qinkdmreae ktltelnkcc glcvcpcnrt knfesgknyk atwgdggdss psnvvskqps
      121 ritngqpqqt tgaasggyik ritndarede meenltqvgs ilgnlknmal dmgneidaqn
      181 qqiqkiteka dtnknridia ntrakklids
//
LOCUS       NP_001419389             747 aa            linear   ROD 28-APR-2025
DEFINITION  anoctamin 9 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419389 XP_006230651
VERSION     NP_001419389.1
DBSOURCE    REFSEQ: accession NM_001432460.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Suzuki,J., Fujii,T., Imao,T., Ishihara,K., Kuba,H. and Nagata,S.
  TITLE     Calcium-dependent phospholipid scramblase activity of TMEM16
            protein family members
  JOURNAL   J Biol Chem 288 (19), 13305-13316 (2013)
   PUBMED   23532839
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Tian,Y., Schreiber,R. and Kunzelmann,K.
  TITLE     Anoctamins are a family of Ca2+-activated Cl- channels
  JOURNAL   J Cell Sci 125 (Pt 21), 4991-4998 (2012)
   PUBMED   22946059
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Scudieri,P., Sondo,E., Ferrera,L. and Galietta,L.J.
  TITLE     The anoctamin family: TMEM16A and TMEM16B as calcium-activated
            chloride channels
  JOURNAL   Exp Physiol 97 (2), 177-183 (2012)
   PUBMED   21984732
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Ousingsawat,J., Kongsuphol,P., Schreiber,R. and Kunzelmann,K.
  TITLE     CFTR and TMEM16A are separate but functionally related Cl- channels
  JOURNAL   Cell Physiol Biochem 28 (4), 715-724 (2011)
   PUBMED   22178883
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Schreiber,R., Uliyakina,I., Kongsuphol,P., Warth,R., Mirza,M.,
            Martins,J.R. and Kunzelmann,K.
  TITLE     Expression and function of epithelial anoctamins
  JOURNAL   J Biol Chem 285 (10), 7838-7845 (2010)
   PUBMED   20056604
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 30, 2024 this sequence version replaced XP_006230651.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.4970.1,
                                           SRR26643297.3915.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..747
                     /product="anoctamin 9 isoform 2"
                     /calculated_mol_wt=86950
     Region          <106..171
                     /region_name="Anoct_dimer"
                     /note="dimerization domain of Ca+-activated
                     chloride-channel, anoctamin; pfam16178"
                     /db_xref="CDD:465044"
     Region          174..729
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     CDS             1..747
                     /gene="Ano9"
                     /gene_synonym="RGD1560565"
                     /coded_by="NM_001432460.1:68..2311"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:499287"
                     /db_xref="RGD:1560565"
ORIGIN      
        1 mqvdeslqil vgsegdhlpl memgsckpea sdqwdcvlva dlqtqksqkh vqrqqqflek
       61 lerngfhfkv lkdqkkvffg iradsavidm yrtllmkped prsrakqnfn iattririvn
      121 fvvnskkrls dtfedlvkdg vfetmfllhk geedlsrewa qwrnvfqpqp idkireyfge
      181 kvalyftwlg wytymlvpaa vvglivflsg falfdssqis keicsaddif mcplgdnsrr
      241 yqrlsemctf aklthlfdne gtvifaifma lwatvfleiw krkrarevqs welyewdeee
      301 eemalelins phyelkkhhh sylsstiili lslfmiclmi gmahllvvyr vlaaalfssf
      361 leqqvttavv vtgavvhyvi ivimtkvnkc valklckfee prtfseqesk ftvkffilqf
      421 fahfssliyi afilgringh pgkstrlagl wkleechlsg cmmdlfiqma iimglkqtls
      481 ncieylypll ahkcrsvqay rhgrkskdpe laewqrnyhm npvntfslfd efmemmiqyg
      541 fttifvaafp lapllalfsn lveirldaik mvrlqrrlvp rkakdigtwl qvletigvla
      601 viangmviaf tsefiprvvy kyhygpcrkn qtftddclkd yvnhslsvfy tkdfqdhgrm
      661 egqenvtvcr yrdyrndhdy nlseqfwfil airlafvilf ehvalcikli aawfvpdvpq
      721 svknevleek yqrirgrmcf ssrstdv
//
LOCUS       NP_001389376             412 aa            linear   ROD 28-APR-2025
DEFINITION  histone-lysine N-methyltransferase SUV39H1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001389376 XP_006256767
VERSION     NP_001389376.1
DBSOURCE    REFSEQ: accession NM_001402447.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Yang,G., Weng,X., Zhao,Y., Zhang,X., Hu,Y., Dai,X., Liang,P.,
            Wang,P., Ma,L., Sun,X., Hou,L., Xu,H., Fang,M., Li,Y., Jenuwein,T.,
            Xu,Y. and Sun,A.
  TITLE     The histone H3K9 methyltransferase SUV39H links SIRT1 repression to
            myocardial infarction
  JOURNAL   Nat Commun 8, 14941 (2017)
   PUBMED   28361889
  REMARK    GeneRIF: SUV39H augments intracellular reactive oxygen species
            levels in a SIRT1-dependent manner.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,J., Liang,L., Miao,X., Wu,S., Cao,J., Tao,B., Mao,Q., Mo,K.,
            Xiong,M., Lutz,B.M., Bekker,A. and Tao,Y.X.
  TITLE     Contribution of the Suppressor of Variegation 3-9 Homolog 1 in
            Dorsal Root Ganglia and Spinal Cord Dorsal Horn to Nerve
            Injury-induced Nociceptive Hypersensitivity
  JOURNAL   Anesthesiology 125 (4), 765-778 (2016)
   PUBMED   27483126
  REMARK    GeneRIF: SUV39H1 plays a critical role in chromosome dynamics and
            development, neurite outgrowth, and ethanol-induced neuroadaptation
            through gene-specific silencing.
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yang,B., Yang,J., Bai,J., Pu,P., Liu,J., Wang,F. and Ruan,B.
  TITLE     Suv39h1 protects from myocardial ischemia-reperfusion injury in
            diabetic rats
  JOURNAL   Cell Physiol Biochem 33 (4), 1176-1185 (2014)
   PUBMED   24752040
  REMARK    GeneRIF: Overexpression of Suv39h1 results in the de-activation of
            proinflammatory pathways and reduced apoptosis and myocardial
            injury.
REFERENCE   4  (residues 1 to 412)
  AUTHORS   He,Y., Korboukh,I., Jin,J. and Huang,J.
  TITLE     Targeting protein lysine methylation and demethylation in cancers
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 44 (1), 70-79 (2012)
   PUBMED   22194015
  REMARK    Review article
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Bosch-Presegue,L., Raurell-Vila,H., Marazuela-Duque,A.,
            Kane-Goldsmith,N., Valle,A., Oliver,J., Serrano,L. and Vaquero,A.
  TITLE     Stabilization of Suv39H1 by SirT1 is part of oxidative stress
            response and ensures genome protection
  JOURNAL   Mol Cell 42 (2), 210-223 (2011)
   PUBMED   21504832
  REMARK    GeneRIF: SirT1 preserves heterochromatin structure: it modulates
            Suv39h1 protein levels in stress conditions by preventing
            MDM2-mediated polyubiquitination at K87.
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Davison,J.M., Mellott,T.J., Kovacheva,V.P. and Blusztajn,J.K.
  TITLE     Gestational choline supply regulates methylation of histone H3,
            expression of histone methyltransferases G9a (Kmt1c) and Suv39h1
            (Kmt1a), and DNA methylation of their genes in rat fetal liver and
            brain
  JOURNAL   J Biol Chem 284 (4), 1982-1989 (2009)
   PUBMED   19001366
  REMARK    GeneRIF: mRNA and protein expression of histone methyltransferases
            G9a and Suv39h1 were directly related to the availability of
            choline
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Renthal,W., Carle,T.L., Maze,I., Covington,H.E. 3rd, Truong,H.T.,
            Alibhai,I., Kumar,A., Montgomery,R.L., Olson,E.N. and Nestler,E.J.
  TITLE     Delta FosB mediates epigenetic desensitization of the c-fos gene
            after chronic amphetamine exposure
  JOURNAL   J Neurosci 28 (29), 7344-7349 (2008)
   PUBMED   18632938
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Pogribny,I.P., Ross,S.A., Tryndyak,V.P., Pogribna,M., Poirier,L.A.
            and Karpinets,T.V.
  TITLE     Histone H3 lysine 9 and H4 lysine 20 trimethylation and the
            expression of Suv4-20h2 and Suv-39h1 histone methyltransferases in
            hepatocarcinogenesis induced by methyl deficiency in rats
  JOURNAL   Carcinogenesis 27 (6), 1180-1186 (2006)
   PUBMED   16497704
  REMARK    GeneRIF: Suv4-20h2 and Suv-39h1 histone methyltransferases are
            expressed and Histone H3 lysine 9 and H4 lysine 20 are
            trimethylated in hepatocarcinogenesis induced by methyl deficiency
            in rats [Suv4-20h2 and Suv-39h1]
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Liu,D.X., Nath,N., Chellappan,S.P. and Greene,L.A.
  TITLE     Regulation of neuron survival and death by p130 and associated
            chromatin modifiers
  JOURNAL   Genes Dev 19 (6), 719-732 (2005)
   PUBMED   15769944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Nov 25, 2022 this sequence version replaced XP_006256767.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160871.1, SRR26643290.55555.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..412
                     /product="histone-lysine N-methyltransferase SUV39H1
                     isoform 2"
                     /EC_number="2.1.1.354"
                     /note="histone-lysine N-methyltransferase SUV39H1;
                     suppressor of variegation 3-9 homolog 1-like 1"
                     /calculated_mol_wt=47623
     Region          43..91
                     /region_name="CD_SUV39H1_like"
                     /note="chromodomain of histone methyltransferase SUV39H1,
                     and similar proteins; cd18639"
                     /db_xref="CDD:349289"
     Site            order(43..47,62,64..67,71,73..76,78..79,85,88..89)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349289"
     Region          158..412
                     /region_name="SET_SUV39H1"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in suppressor of variegation 3-9 homolog 1 (SUV39H1)
                     and similar proteins; cd10525"
                     /db_xref="CDD:380923"
     Site            order(254..256,296..297,320..324,365,399..402,411)
                     /site_type="other"
                     /note="putative SAM binding site"
                     /db_xref="CDD:380923"
     Site            order(254..256,273,280,283..284,286,295..300,303,309,
                     320..324,332,334,347,363,365,398..402)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380923"
     Site            order(298..300,309,332,347,365)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380923"
     Site            order(326,400,402,407)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380923"
     CDS             1..412
                     /gene="Suv39h1"
                     /gene_synonym="RGD1565028; Suv39h1l1"
                     /coded_by="NM_001402447.1:168..1406"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:302553"
                     /db_xref="RGD:1565028"
ORIGIN      
        1 maenlkgcsv ccksswnqlq dlcrlaklsc palgvskknl ydfeveylcd ykkireqeyy
       61 lvkwrgypds entweprqnl kcvrilkqfh kdlerelvrr hrrskpprhl dpnlanylvq
      121 kakqrralqr weqelnakrs hlgritvene vdldgpprsf vyineyrvge gitlnqvavg
      181 cecqdcllap tggccpgasl hkfayndqgq vrlkagqpiy ecnsrcccgy dcpnrvvqkg
      241 irynlcifrt ddgrgwgvrt lekirknsfv meyvgeiits eeaerrgqiy drqgatylfd
      301 ldyvedvytv daayygnish fvnhscdpnl qvynvfidnl derlpriaff atrtiwagee
      361 ltfdynmqvd pvdmestrmd snfglaglpg spkkrvriec kcgttacrky lf
//
LOCUS       NP_001102654             214 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain-containing protein 169 [Rattus norvegicus].
ACCESSION   NP_001102654 XP_001059085 XP_574944
VERSION     NP_001102654.1
DBSOURCE    REFSEQ: accession NM_001109184.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474003.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_574944.2, XP_001059085.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..214
                     /product="coiled-coil domain-containing protein 169"
                     /calculated_mol_wt=24531
     Region          55..181
                     /region_name="DUF4600"
                     /note="Domain of unknown function (DUF4600); pfam15372"
                     /db_xref="CDD:434673"
     CDS             1..214
                     /gene="Ccdc169"
                     /coded_by="NM_001109184.1:49..693"
                     /db_xref="GeneID:499618"
                     /db_xref="RGD:1593170"
ORIGIN      
        1 mgeghgdtfe gvstdrlkle lleeihmkdv vqlstleirh kiaeleanln tdlagsewkt
       61 ryetqlelnd qlekqivslk ekmekvrgnp sdrlssirvy ekmpveslnl llkqlekekr
      121 slenqvkdya lkleqeskvf hrtnserrsy isemsqvsgl tqvskrqqmd plprmkespv
      181 ktgrhssvnq kttnakkgpv kkvsrsnhlp klnp
//
LOCUS       NP_001402637            1252 aa            linear   ROD 28-APR-2025
DEFINITION  immunoglobulin superfamily DCC subclass member 4 isoform 3
            precursor [Rattus norvegicus].
ACCESSION   NP_001402637 XP_038937676
VERSION     NP_001402637.1
DBSOURCE    REFSEQ: accession NM_001415708.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1252)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 1252)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   3  (residues 1 to 1252)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Dec 23, 2022 this sequence version replaced XP_038937676.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.22113.1,
                                           SRR26643289.23248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1252
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..1252
                     /product="immunoglobulin superfamily DCC subclass member 4
                     isoform 3 precursor"
                     /note="neighbor of Punc E11"
                     /calculated_mol_wt=132298
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2294
     Region          38..130
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          51..55
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..122
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          144..215
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          249..330
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          260..264
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          273..278
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          294..298
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          308..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          323..326
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          349..421
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          351..355
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          364..368
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          385..391
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          <401..>602
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          401..406
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          414..417
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            order(629,708,723)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          631..725
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          749..841
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(749,814,829)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(830..831,833..834)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          849..941
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(930..931,933..934)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..1252
                     /gene="Igdcc4"
                     /gene_synonym="Nope"
                     /coded_by="NM_001415708.2:77..3835"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:363081"
                     /db_xref="RGD:1310919"
ORIGIN      
        1 maradtgrgl laltfcllsa rgelplpqet tvqlscdegp lrvvlgpeqa vvldctlgaa
       61 aagppttvtw skdgdvvler dnlhllpngs lrlssplepe dsddeealsv wkviegsysc
      121 lahgplgvva sqvavvklat ledfslhpes qtveengtar fechteglpa piitwekdqv
      181 tvteeprlit lpngvlqild vqdsdagsyr cvatnsarqr fsqeallsva lrgsleatrg
      241 qdvvivaape nttvvsgqsv vlecvasadp tpfvswvrqd gkpistdviv lgrtnllias
      301 aqprhsgvyv crankprtrd fataaaelrv laapaisqap ealsrtrast arfvcrasge
      361 prptlhwlhd gaplrpngrv kvqggggslv itqiglqdsg yyqcvaensa gtacaaapla
      421 vvvreglpsa ptrvkatpls ssavlvawer pelhseqiig fslhyqkarg vdnveyqfav
      481 nndttelqvr dlepntdyef yvvaysqlga srtsspalvh tlddvpsaap qlslsspnps
      541 dirvawlplp sslsngqvvk ykieygsgke dqvfstevpg netqltlnsl qpnkvyrvri
      601 sagtgagygv psqwmqhrtp gahnqshvpf apaelkvrak meslvvswqp pphptqisgy
      661 klywrevgte eeadgdrppg grgdqawdvg pvrlkkkvkq yeltqlvpgr lyevklvafn
      721 khedgyaavw kgktekaptp dlpiqrgppl ppahvhaesn sstsiwlrwk kpdfttvkiv
      781 nytvrfgpwg lrnaslvtyy tssgedilig glkpftkyef avqshgvdmd gpfgsvvers
      841 tlpdrpstpp sdlrlspltp stvrlhwcpp tepngeivey lilysnnhtq pehqwtlltt
      901 egnifsaevh glesdtryff kmgartevgp gpfsrlqdvi tlqetfsdsl dvhsvtgiiv
      961 gvclgllcll acmcaglrrs shrealpgls statagnpal ysrarlgpps vpaahelesl
     1021 vhprpqdwsp ppsdvedkak vhslmggsvs dcrghskrki swaqaggpnw agswagcelp
     1081 qgsgprpalt rallppagtg qtlllqalvy daiksngrkk pspacrnqve aevivhsdfs
     1141 askgcpdlhl qdlepeealp aevlpptagv vdlsqgadwl greleecqpa ttgperltcl
     1201 peaasascsc sdlqpssave eapgkgcqpk alcpleisps lprapvssaq vp
//
LOCUS       NP_001380635             866 aa            linear   ROD 28-APR-2025
DEFINITION  carbohydrate-responsive element-binding protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001380635 XP_038944970
VERSION     NP_001380635.1
DBSOURCE    REFSEQ: accession NM_001393706.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Hu,A., Lan,H., Yao,Z. and Kong,X.
  TITLE     Carbohydrate response element-binding protein (ChREBP) mediates
            decreased SNAP25 expression in islets from diabetic Goto-Kakizaki
            (GK) rats
  JOURNAL   FEBS Open Bio 14 (11), 1864-1872 (2024)
   PUBMED   39300600
  REMARK    GeneRIF: Carbohydrate response element-binding protein (ChREBP)
            mediates decreased SNAP25 expression in islets from diabetic
            Goto-Kakizaki (GK) rats.
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Katz,L.S., Brill,G., Wang,P., Lambertini,L., Zhang,P.,
            Haldeman,J.M., Liu,H., Newgard,C.B., Stewart,A.F., Garcia-Ocana,A.
            and Scott,D.K.
  TITLE     Transcriptional activation of the Myc gene by glucose in beta-cells
            requires a ChREBP-dependent 3-D chromatin interaction between the
            Myc and Pvt1 genes
  JOURNAL   Mol Metab 79, 101848 (2024)
   PUBMED   38042369
  REMARK    GeneRIF: Transcriptional activation of the Myc gene by glucose in
            beta-cells requires a ChREBP-dependent 3-D chromatin interaction
            between the Myc and Pvt1 genes.
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Zhan,H., Wang,Y., Yu,S., Cai,G., Zeng,Y., Ma,J., Liu,W. and Wu,W.
  TITLE     Upregulation of Mlxipl induced by cJun in the spinal dorsal horn
            after peripheral nerve injury counteracts mechanical allodynia by
            inhibiting neuroinflammation
  JOURNAL   Aging (Albany NY) 12 (11), 11004-11024 (2020)
   PUBMED   32518215
  REMARK    GeneRIF: Upregulation of Mlxipl induced by cJun in the spinal
            dorsal horn after peripheral nerve injury counteracts mechanical
            allodynia by inhibiting neuroinflammation.
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Han,J.H., Kim,S., Kim,S., Lee,H., Park,S.Y. and Woo,C.H.
  TITLE     FMK, an Inhibitor of p90RSK, Inhibits High Glucose-Induced TXNIP
            Expression via Regulation of ChREBP in Pancreatic beta Cells
  JOURNAL   Int J Mol Sci 20 (18), 4424 (2019)
   PUBMED   31505737
  REMARK    GeneRIF: these findings suggest FMK may protect against HG-induced
            beta-cell dysfunction and TXNIP expression by ChREBP regulation in
            pancreatic beta-cells, and that FMK is a potential therapeutic
            reagent for the drug development of diabetes and its complications.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Van der Werf,R., Walter,C., Bietiger,W., Seyfritz,E., Mura,C.,
            Peronet,C., Legrandois,J., Werner,D., Ennahar,S., Digel,F.,
            Maillard-Pedracini,E., Pinget,M., Jeandidier,N., Marchioni,E.,
            Sigrist,S. and Dal,S.
  TITLE     Beneficial effects of cherry consumption as a dietary intervention
            for metabolic, hepatic and vascular complications in type 2
            diabetic rats
  JOURNAL   Cardiovasc Diabetol 17 (1), 104 (2018)
   PUBMED   30029691
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Kawaguchi,T., Osatomi,K., Yamashita,H., Kabashima,T. and Uyeda,K.
  TITLE     Mechanism for fatty acid 'sparing' effect on glucose-induced
            transcription: regulation of carbohydrate-responsive
            element-binding protein by AMP-activated protein kinase
  JOURNAL   J Biol Chem 277 (6), 3829-3835 (2002)
   PUBMED   11724780
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Yamashita,H., Takenoshita,M., Sakurai,M., Bruick,R.K., Henzel,W.J.,
            Shillinglaw,W., Arnot,D. and Uyeda,K.
  TITLE     A glucose-responsive transcription factor that regulates
            carbohydrate metabolism in the liver
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 9116-9121 (2001)
   PUBMED   11470916
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Cairo,S., Merla,G., Urbinati,F., Ballabio,A. and Reymond,A.
  TITLE     WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted
            region, is a new member of the Mlx transcription factor network
  JOURNAL   Hum Mol Genet 10 (6), 617-627 (2001)
   PUBMED   11230181
REFERENCE   9  (residues 1 to 866)
  AUTHORS   de Luis,O., Valero,M.C. and Jurado,L.A.
  TITLE     WBSCR14, a putative transcription factor gene deleted in
            Williams-Beuren syndrome: complete characterisation of the human
            gene and the mouse ortholog
  JOURNAL   Eur J Hum Genet 8 (3), 215-222 (2000)
   PUBMED   10780788
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Volpe,C.M., Koo,J., Miloro,S.M., Driscoll,D.L., Nava,H.R. and
            Douglass,H.O. Jr.
  TITLE     The effect of extended lymphadenectomy on survival in patients with
            gastric adenocarcinoma
  JOURNAL   J Am Coll Surg 181 (1), 56-64 (1995)
   PUBMED   7599772
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Mar 5, 2021 this sequence version replaced XP_038944970.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FN432819.1, SRR26360181.46554.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..866
                     /product="carbohydrate-responsive element-binding protein
                     isoform 1"
                     /note="Williams-Beuren syndrome chromosome region 14
                     homolog; carbohydrate-responsive element-binding protein;
                     MLX interactor; class D basic helix-loop-helix protein 14;
                     WS basic-helix-loop-helix leucine zipper protein;
                     Williams-Beuren syndrome chromosomal region 14 protein"
                     /calculated_mol_wt=94977
     Region          15..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          53..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          81..196
                     /region_name="NES2-NLS_ChREBP"
                     /note="nuclear export signal 2 (NES2) and nuclear import
                     signal (NLS) domains found in carbohydrate-responsive
                     element-binding protein (ChREBP), and similar proteins;
                     cd21771"
                     /db_xref="CDD:439287"
     Site            order(117,121,124,127..131,134)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:439287"
     Site            order(124,127..128)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:439287"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          <262..656
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          334..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:11724780; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NP71; propagated from
                     UniProtKB/Swiss-Prot (Q8VIP2.1)"
     Region          660..735
                     /region_name="bHLHzip_MLXIPL"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in MLX-interacting protein-like (MLXIPL) and similar
                     proteins; cd19689"
                     /db_xref="CDD:381532"
     Site            order(665,667..669,671..673,675..676,680,702..703)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381532"
     Site            order(679,682..683,685..686,689..691,704,707..708,711,
                     713..715,717..718,720..721,724,727..728,731..732,734..735)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381532"
     Region          717..738
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VIP2.1)"
     CDS             1..866
                     /gene="Mlxipl"
                     /gene_synonym="bHLHd14; ChREBP; Wbscr14; WS-bHLH"
                     /coded_by="NM_001393706.1:37..2637"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:171078"
                     /db_xref="RGD:620400"
ORIGIN      
        1 maraladlsv nlqvprvvps pdsdsdtdle dpsprrsagg lhrsqvihsg hfmvssphsd
       61 sltrrrdqeg pvgladfgpr sidptltrlf eclslaysgk lvspkwknfk glkllcrdki
      121 rlnnaiwraw yiqyvqrrks pvcgfvtplq gseadehrkp eavvlegnyw krrievvmre
      181 yhkwriyykk rlrkssregd flapkqvegg wppperwceq lfssvvpvll ggseeepggr
      241 qlldldcfls disdtlftmt qpspsslqlp sedayvgnad miqpdltplq pslddfmeis
      301 dfftnyrppq tptssnfpep psfgpmadsl fsggilgpem pspasassss gmtplsgntr
      361 lqarnscsgp ldpstfpsse fllpedpktk mppapvptpl lpypgpvkvh glepctpspf
      421 ptmapppall seeplfsarf pfttvppapg vstlpapttf vptpqpgpvp gpvpfpvdhl
      481 phgylepvfg phftvpqgvq prckpcsppp ggrkaspptl tsatasptat atardnnpcl
      541 tqllraakpe qvlepstvps tllrppespq davpeiprvr afyppipapt pprpppgpat
      601 lapprslvvp kaerlsppas sgserrlsgd lnsiqppgal svhlsppqtv lsrgrvdnnk
      661 menrrithis aeqkrrfnik lgfdtlhglv stlsaqpslk vskattlqkt aeyilmlqqe
      721 raamqeeaqq lrdeieelna ainlcqqqlp atgvpithqr fdqmrdmfdd yvrtrtlhnw
      781 kfwvfsilir plfesfngmv staslhslrq tslawldqyc slpalrptvl nslrqlstst
      841 siltdpslvp eqatravteg plgrpl
//
LOCUS       NP_001419452             189 aa            linear   ROD 28-APR-2025
DEFINITION  spermatogenesis-associated protein 3 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001419452 XP_006245474
VERSION     NP_001419452.1
DBSOURCE    REFSEQ: accession NM_001432523.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Jul 31, 2024 this sequence version replaced XP_006245474.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.51697.1,
                                           SRR26360181.3348826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..189
                     /product="spermatogenesis-associated protein 3 isoform 2"
                     /note="spermatogenesis-associated protein 3"
                     /calculated_mol_wt=20679
     Region          9..188
                     /region_name="SPATA3"
                     /note="Spermatogenesis-associated protein 3 family;
                     pfam15662"
                     /db_xref="CDD:434837"
     CDS             1..189
                     /gene="Spata3"
                     /coded_by="NM_001432523.1:106..675"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:363270"
                     /db_xref="RGD:1308164"
ORIGIN      
        1 mkkvkkkksd srrrrnsisp qtssdcshrp ssetqrscpd pcsppqtqsl qesipphqis
       61 pepklqqpss qpllpseerv sspclvstep kppcrkavpl tyaaprscsc vvcpgssacw
      121 rrlglchsri fdvllprdws smpgrgfpnl ltfyrkpsrk yctsrnsras sprncccgsg
      181 gpgscllhg
//
LOCUS       NP_001416139             326 aa            linear   ROD 28-APR-2025
DEFINITION  ELMO domain-containing protein 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416139 XP_006243145
VERSION     NP_001416139.1
DBSOURCE    REFSEQ: accession NM_001429210.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Apr 12, 2024 this sequence version replaced XP_006243145.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.63582.1,
                                           SRR26360176.227430.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..326
                     /product="ELMO domain-containing protein 1 isoform 2"
                     /note="ELMO domain-containing protein 1; ELMO/CED-12
                     domain containing 1"
                     /calculated_mol_wt=37956
     Region          119..295
                     /region_name="ELMO_CED12"
                     /note="ELMO/CED-12 family; pfam04727"
                     /db_xref="CDD:461411"
     CDS             1..326
                     /gene="Elmod1"
                     /gene_synonym="RGD1564186"
                     /coded_by="NM_001429210.1:373..1353"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:315670"
                     /db_xref="RGD:1564186"
ORIGIN      
        1 mkhflrmliq vclyfyckfl wrcmkfvmrk ltgrcelqri cygtkpgasr tmkietslrd
       61 skskllqtsv svhpdaiekt iddimelkki npdinpqlgi slqacllqiv gyrnliadve
      121 klrrepydsd npqheemllk lweflkpntp lesriskqwc eigfqgddpk tdfrgmgllg
      181 lynlqyfaer datvaqqvlc dsvhpkcskf sktewekkkm dkaigysfai vginitdlay
      241 nllvsgalkt hfyniapeap tlshfqqtfc ylmhefhkfw ieedpmdime fnrvrekfrk
      301 riikqlqnpd malcphfaas eglinm
//
LOCUS       NP_001388365             482 aa            linear   ROD 28-APR-2025
DEFINITION  ras GTPase-activating protein-binding protein 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001388365 XP_006250795
VERSION     NP_001388365.1
DBSOURCE    REFSEQ: accession NM_001401436.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Xiao,X., He,Z., Tong,S., Dai,L., Xiao,Q., Qin,Z. and Lin,T.
  TITLE     lncRNA XIST knockdown suppresses hypoxia/reoxygenation
            (H/R)-induced apoptosis of H9C2 cells by regulating
            miR-545-3p/G3BP2
  JOURNAL   IUBMB Life 73 (9), 1103-1114 (2021)
   PUBMED   34060227
  REMARK    GeneRIF: lncRNA XIST knockdown suppresses hypoxia/reoxygenation
            (H/R)-induced apoptosis of H9C2 cells by regulating
            miR-545-3p/G3BP2.
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hong,H.Q., Lu,J., Fang,X.L., Zhang,Y.H., Cai,Y., Yuan,J., Liu,P.Q.
            and Ye,J.T.
  TITLE     G3BP2 is involved in isoproterenol-induced cardiac hypertrophy
            through activating the NF-kappaB signaling pathway
  JOURNAL   Acta Pharmacol Sin 39 (2), 184-194 (2018)
   PUBMED   28816235
  REMARK    GeneRIF: new insight into the functions of G3BP2
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Matsuki,H., Takahashi,M., Higuchi,M., Makokha,G.N., Oie,M. and
            Fujii,M.
  TITLE     Both G3BP1 and G3BP2 contribute to stress granule formation
  JOURNAL   Genes Cells 18 (2), 135-146 (2013)
   PUBMED   23279204
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Cristea,I.M., Rozjabek,H., Molloy,K.R., Karki,S., White,L.L.,
            Rice,C.M., Rout,M.P., Chait,B.T. and MacDonald,M.R.
  TITLE     Host factors associated with the Sindbis virus RNA-dependent RNA
            polymerase: role for G3BP1 and G3BP2 in virus replication
  JOURNAL   J Virol 84 (13), 6720-6732 (2010)
   PUBMED   20392851
  REMARK    GeneRIF: Two related proteins found in association with nsP4 at
            both times of infection, GTPase-activating protein (SH3 domain)
            binding protein 1 (G3BP1) and G3BP2 were also previously identified
            as associated with sindbis virus nsP2 and nsP3.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Feb 11, 2022 this sequence version replaced XP_006250795.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.2224042.1,
                                           SRR26360186.2776238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..482
                     /product="ras GTPase-activating protein-binding protein 2
                     isoform 1"
                     /note="ras GTPase-activating protein-binding protein 2;
                     GTPase activating protein (SH3 domain) binding protein 2"
                     /calculated_mol_wt=53943
     Region          7..135
                     /region_name="NTF2"
                     /note="Nuclear transport factor 2 (NTF2) domain plays an
                     important role in the trafficking of macromolecules, ions
                     and small molecules between the cytoplasm and nucleus.
                     This bi-directional transport of macromolecules across the
                     nuclear envelope requires many...; cd00780"
                     /db_xref="CDD:238403"
     Site            order(35,41,56,81,83..84,93,115,128..130,132,134)
                     /site_type="active"
                     /note="TAP/p15 interaction [active]"
                     /db_xref="CDD:238403"
     Site            order(39,41..42,78..79,81,83..84,91,95..97,101,103..106,
                     109,115,128..130,132..135)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238403"
     Site            order(42..43,68,73,96,98,100..101,103,106,131,133,135)
                     /site_type="active"
                     /note="RanGDP-NTF2 interaction [active]"
                     /db_xref="CDD:238403"
     Region          326..408
                     /region_name="RRM_G3BP2"
                     /note="RNA recognition motif (RRM) found in ras
                     GTPase-activating protein-binding protein 2 (G3BP2) and
                     similar proteins; cd12464"
                     /db_xref="CDD:409897"
     CDS             1..482
                     /gene="G3bp2"
                     /gene_synonym="RGD1309571"
                     /coded_by="NM_001401436.1:215..1663"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305240"
                     /db_xref="RGD:1309571"
ORIGIN      
        1 mvmekpspll vgrefvrqyy tllnkapeyl hrfygrnssy vhggvdasgk pqeavygqnd
       61 ihhkvlslnf sechtkirhv dahatlsdgv vvqvmgllsn sgqperkfmq tfvlapegsv
      121 pnkfyvhndm fryedevfgd sepeldeese deveeeqedr qpspepvqen ansayyeahp
      181 vtngieeple esshepepep esetkteelk pqaeekhlee leeksatppp tepaslpqep
      241 pkafswasvt sknlppsgtv sssgipphvk apvsqprvda kpevqsqppr vreqrprerp
      301 gfpprgprpg rgdteqndsd nrriirypds hqlfvgnlph didenelkef fmsfgnvvel
      361 rintkgvggk lpnfgfvvfd dsepvqrili akpimfrgev rlnveekktr aareretrgg
      421 gddrrdirrn drgpggprgi vgggmmrdrd grgppprggm tqklgsgrgt gqmegrftgq
      481 rr
//
LOCUS       NP_001094154             591 aa            linear   ROD 28-APR-2025
DEFINITION  SH3 domain-binding protein 2 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001094154 XP_001059805 XP_223534
VERSION     NP_001094154.1
DBSOURCE    REFSEQ: accession NM_001100684.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Zeng,L., Ye,F., Jin,Y., Luo,Y. and Zhu,H.
  TITLE     Overexpression of DEL-1 Downregulates SH3BP2 Expression and
            Inhibits Porphyromonas gingivalis-induced Gingival Inflammation In
            Vivo and In Vitro
  JOURNAL   Oral Health Prev Dent 20, 199-206 (2022)
   PUBMED   35481344
  REMARK    GeneRIF: Overexpression of DEL-1 Downregulates SH3BP2 Expression
            and Inhibits Porphyromonas gingivalis-induced Gingival Inflammation
            In Vivo and In Vitro.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Mehlitz,A., Banhart,S., Maurer,A.P., Kaushansky,A., Gordus,A.G.,
            Zielecki,J., Macbeath,G. and Meyer,T.F.
  TITLE     Tarp regulates early Chlamydia-induced host cell survival through
            interactions with the human adaptor protein SHC1
  JOURNAL   J Cell Biol 190 (1), 143-157 (2010)
   PUBMED   20624904
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Ueki,Y., Tiziani,V., Santanna,C., Fukai,N., Maulik,C.,
            Garfinkle,J., Ninomiya,C., doAmaral,C., Peters,H., Habal,M.,
            Rhee-Morris,L., Doss,J.B., Kreiborg,S., Olsen,B.R. and
            Reichenberger,E.
  TITLE     Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause
            cherubism
  JOURNAL   Nat Genet 28 (2), 125-126 (2001)
   PUBMED   11381256
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Ren,R., Mayer,B.J., Cicchetti,P. and Baltimore,D.
  TITLE     Identification of a ten-amino acid proline-rich SH3 binding site
  JOURNAL   Science 259 (5098), 1157-1161 (1993)
   PUBMED   8438166
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB762696.1, EX490894.1, JAXUCZ010000014.1, DY320365.1, CO557208.1
            and BM384145.1.
            
            On or before Dec 20, 2009 this sequence version replaced
            XP_001059805.1, XP_223534.4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760400, SAMN06680416
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..591
                     /product="SH3 domain-binding protein 2 isoform 1"
                     /calculated_mol_wt=65566
     Region          50..164
                     /region_name="PH_3BP2"
                     /note="SH3 domain-binding protein 2 Pleckstrin homology
                     (PH) domain; cd13308"
                     /db_xref="CDD:270118"
     Region          486..586
                     /region_name="SH2_SH3BP2"
                     /note="Src homology 2 domain found in c-Abl SH3
                     domain-binding protein-2 (SH3BP2); cd10359"
                     /db_xref="CDD:198222"
     Site            order(494,518,540,542)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198222"
     Site            order(541,568)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198222"
     CDS             1..591
                     /gene="Sh3bp2"
                     /coded_by="NM_001100684.1:47..1822"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:305450"
                     /db_xref="RGD:1310588"
ORIGIN      
        1 mgfgtgrgha rhsrvsetcl gpwnlcpavs fmeaeemhwp vpmkaigaqn lltmpggvak
       61 agylhkkggt qlqllkwplr fviihqrciy yfksstsasp qgafslsgyn rvmraaeett
      121 snnvfpfkii hiskkhrtwf fsassederk swmamlrrei ghfhekkelp ldtsdsssdt
      181 dsfygaverp idislssypt dnedyehede edsylepdsp gpmkledalt yppayppppv
      241 pvprkptfsd lprahsftsk spspllpppp pkrglmdtgp apedakkdpl glrrvepslr
      301 vpatprrmsd ppvsnvptvp nlrkhpcfrd sanpgpepwt pghgtssvss sttmaittsr
      361 ncdklksfhl ssrgppasep ppvpankpkf lkiveeaspr eaaksapvpp vaprppvqkm
      421 smpevtvrpa vlprpektpl phlqrsppdg qsfrgfsfek arqpsqadtg eedsdedyek
      481 vplpnsvfvn ttesceverl fkatnplgep qdglycirns stksgkvlvv wdessnkvrn
      541 yrifekdskf ylegevlfas vgsmvehyht hvlpshqsll lrhpygyagp r
//
LOCUS       NP_001102894              95 aa            linear   ROD 28-APR-2025
DEFINITION  keratin-associated protein 19-1 [Rattus norvegicus].
ACCESSION   NP_001102894 XP_001056757 XP_001056822 XP_001056890 XP_001056956
VERSION     NP_001102894.1
DBSOURCE    REFSEQ: accession NM_001109424.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473989.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001056956.1, XP_001056822.1, XP_001056890.1, XP_001056757.1.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..95
                     /product="keratin-associated protein 19-1"
                     /calculated_mol_wt=9604
     CDS             1..95
                     /gene="Krtap16-5"
                     /coded_by="NM_001109424.1:50..337"
                     /db_xref="GeneID:680703"
                     /db_xref="RGD:1588263"
ORIGIN      
        1 msyygsyygg lgygyggfgg lncgcssirr lgygsgfggf gygsgfggyg ygsgfggygy
       61 gsgfrgygyg sgfggygygc rrpshyggyg fssfy
//
LOCUS       NP_001357980            2415 aa            linear   ROD 28-APR-2025
DEFINITION  myosin phosphatase Rho-interacting protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001357980 XP_006246485
VERSION     NP_001357980.1
DBSOURCE    REFSEQ: accession NM_001371051.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2415)
  AUTHORS   Zhang,J., Li,X., Zhang,Z., Zhang,J., Ma,L., Wang,S., Guo,X., Li,H.,
            Pan,B. and Niu,Q.
  TITLE     Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced PC12 cells
            necroptosis
  JOURNAL   Ecotoxicol Environ Saf 270, 115860 (2024)
   PUBMED   38142589
  REMARK    GeneRIF: Role of the RIP3-PGAM5-Drp1 pathway in aluminum-induced
            PC12 cells necroptosis.
REFERENCE   2  (residues 1 to 2415)
  AUTHORS   He,N., Qu,Y.J., Li,D.Y. and Yue,S.W.
  TITLE     RIP3 Inhibition ameliorates chronic constriction injury-induced
            neuropathic pain by suppressing JNK signaling
  JOURNAL   Aging (Albany NY) 13 (21), 24417-24431 (2021)
   PUBMED   34772825
  REMARK    GeneRIF: RIP3 Inhibition ameliorates chronic constriction
            injury-induced neuropathic pain by suppressing JNK signaling.
REFERENCE   3  (residues 1 to 2415)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2415)
  AUTHORS   Huang,J.F., Shang,L., Zhang,M.Q., Wang,H., Chen,D., Tong,J.B.,
            Huang,H., Yan,X.X., Zeng,L.P. and Xiong,K.
  TITLE     Differential neuronal expression of receptor interacting protein 3
            in rat retina: involvement in ischemic stress response
  JOURNAL   BMC Neurosci 14, 16 (2013)
   PUBMED   23374330
  REMARK    GeneRIF: The results indicated that RIP3 is expressed
            differentially in retinal neurons in adult rats, including subsets
            of ganglion cells, amacrine and horizontal cells. RIP3 protein
            levels are elevated rapidly following aHIOP
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2415)
  AUTHORS   Murakami,Y., Matsumoto,H., Roh,M., Suzuki,J., Hisatomi,T.,
            Ikeda,Y., Miller,J.W. and Vavvas,D.G.
  TITLE     Receptor interacting protein kinase mediates necrotic cone but not
            rod cell death in a mouse model of inherited degeneration
  JOURNAL   Proc Natl Acad Sci U S A 109 (36), 14598-14603 (2012)
   PUBMED   22908283
REFERENCE   6  (residues 1 to 2415)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   7  (residues 1 to 2415)
  AUTHORS   Riddick,N., Ohtani,K. and Surks,H.K.
  TITLE     Targeting by myosin phosphatase-RhoA interacting protein mediates
            RhoA/ROCK regulation of myosin phosphatase
  JOURNAL   J Cell Biochem 103 (4), 1158-1170 (2008)
   PUBMED   17661354
  REMARK    GeneRIF: myosin phosphatase-rho interacting protein is a scaffold
            linking RhoA to regulate myosin phosphatase at the stress fiber.
REFERENCE   8  (residues 1 to 2415)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   9  (residues 1 to 2415)
  AUTHORS   Mulder,J., Ariaens,A., van Horck,F.P. and Moolenaar,W.H.
  TITLE     Inhibition of RhoA-mediated SRF activation by p116Rip
  JOURNAL   FEBS Lett 579 (27), 6121-6127 (2005)
   PUBMED   16243315
REFERENCE   10 (residues 1 to 2415)
  AUTHORS   Mulder,J., Poland,M., Gebbink,M.F., Calafat,J., Moolenaar,W.H. and
            Kranenburg,O.
  TITLE     p116Rip is a novel filamentous actin-binding protein
  JOURNAL   J Biol Chem 278 (29), 27216-27223 (2003)
   PUBMED   12732640
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Jun 26, 2019 this sequence version replaced XP_006246485.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2415
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..2415
                     /product="myosin phosphatase Rho-interacting protein
                     isoform 1"
                     /note="RIP3; rho-interacting protein 3; Rho interacting
                     protein 3"
                     /calculated_mol_wt=273070
     Region          16..151
                     /region_name="PH_RIP"
                     /note="Rho-Interacting Protein Pleckstrin homology (PH)
                     domain; cd01236"
                     /db_xref="CDD:269942"
     Region          152..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97434; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6WCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9ERE6.1)"
     Region          512..613
                     /region_name="PH_M-RIP"
                     /note="Myosin phosphatase-RhoA Interacting Protein
                     Pleckstrin homology (PH) domain; cd13275"
                     /db_xref="CDD:270094"
     Region          855..>1183
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <1670..>2365
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <2058..>2320
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2415
                     /gene="Mprip"
                     /gene_synonym="M-rip; Mrip; p116Rip; Rhoip3"
                     /coded_by="NM_001371051.2:315..7562"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:116504"
                     /db_xref="RGD:619947"
ORIGIN      
        1 msaakenpcr kfqanifnks kcqncfkpre shllndedlt qakpiyggwl llapdgtdfd
       61 npvhrsrkwq rrffilyehg llryaldemp ttlpqgtinm nqctdvvdge artgqkfslc
      121 iltpdkehfi raetkeiisg wlemlmvypr tnkqnqkkkr kvepptpqep gpakmavtss
      181 sggssgssss sssssipsae kvpttkstlw qeemrakdqp dgtslspvqs psqsqppaac
      241 tpretgldsk edenilsgdr vdggrkvrve sgyfslekak qdlraeeqlp pllsppspst
      301 phsrygcpgs psqelshplh spglpapsrm vysicpdslg easrppnhmd sssaggwgte
      361 ilgstfafka srqyaaladv pkairishre afqverrrle hrtrarspgr eevarlfgne
      421 rrrsqviekf ealdiekaeh metnmliltt pssdtrqgrs erraiprkrd fasetptapl
      481 sdacplsphr raksldrrst essmtpdlln fkkgwltkqy edgqwkkhwf vladqslryy
      541 rdsvaeeaad ldgeinlstc ydvteypvqr nygfqihtke geftlsamts girrnwiqti
      601 mkhvlptsap dvtsslpegk nkstsfdtcl rpsekqeaep gepdpeqkks rarerrregr
      661 sktfdwaefr piqqalaqer astvgssdsg dpgcleaepg elererarrr eerrkrfgml
      721 dtndgpgmed talrmdidrs pgllgtpdlk tqnvhveieq rwhqvettpl reekqvpiap
      781 lhlsledrse rlstheltsl lekeleqsqk easdlleqnr llqdqlrval greqsaregy
      841 vlqtevatsp sgawqrlhrv nqdlqselea qcrrqelitq qiqtlkhsyg eakdairhhe
      901 aeiqtlqtrl gdaaaelaik eqalaklkge lkleqgkvre qleewqhska vlrgqlrase
      961 qklqsteall lektqelrdl etkqalqrdr qkevqrlqec iaelsqqlgt seqaqrlmek
     1021 klkrnytlll esceqekqal lqnlkevedk asayedqlqg hvqqvealqk eklsetckgt
     1081 ervhklqeel eareasirql aqhvqslhde rdlikhqfqe lmervatsdg dvaelqeklk
     1141 greadyqnle hshhrvsiql qsvrtllrek eeelklikea hervlekkdq dlnealvkmi
     1201 algssleete iklqekeecl rrfvsdspkd akepqsttdp teedsgiltl gsvtrvfpgf
     1261 phsqpededp saslgeegss gslsreenii ppksadmpdr egqlqstvks dqgapvkrpr
     1321 irfstiqcqr yihpegcaka wtsstssdts qdqspsedsv sseatpstlp aaadaetyis
     1381 iihsletkly vteeklkdvt vrlesqqgqs qeallalhqq wagteaqlre qlrvsllqas
     1441 tlasqleqer qqkvtniehh sgeledfqak nsqaltclen cweklrslpq anqeegqdac
     1501 aaslaniesm lvsaikalqp waspaesrmq aekekghpme sgiaapmqqp cqpilneqeh
     1561 rkllsaqivl easlinqiad slksttsnvy gvlceltqsg ewplkkesaa psagapmeiw
     1621 akkvlvngef wsqveslskh lgtlgeetac tsadkqqhvp qsladatwir aelsyatqsv
     1681 relfhhrlqs iqetlqgtqa alqqhkcmlg eilgayqtpd ferviqqile tlrhptdred
     1741 hvqtswdqsp lgevlrpgtd gsqeplqafh qspevlaaiq delaqqlrek asileeisaa
     1801 lpvlpptepl ggcqrllqms qhlsydacle glgqyssllv qdaiiqaqvc yaacrirley
     1861 ekelqfykka cqeargascq krtqavgalk eeyeellhkq kseyqkvitl iekentelka
     1921 kvsqldhqqr clqeaeskhs esmfalqgry eeeircmveq lshtentlqa ersrvlsqld
     1981 asvkdrqame qhhvqqmkml edrfqlkvre lqavhqeelr alqehyiwsm rgalslcqps
     2041 hpdsplapgp sepravpaak deaesmtglr eriqeleaqm gvmreelghk elegdvaalq
     2101 ekyqrdfesl katcergfaa meethqkkie dlqrqhqrel eklreekdrl laeetaatis
     2161 aieamknahr eemereleks qrsqissins diealrrqyl eelqsvqrel evlseqysqk
     2221 clenahlaqa leaerqalrq cqrenqelna hnqelnnrla aeitrlrtll tgegggestg
     2281 lpltqgkday elevllrvke seiqylkqei sslkdelqta lrdkkyasdk ykdiytelsi
     2341 akakadcdis rlkeqlkaat ealgekspeg ttvsgydimk sksnpdflkk drscvtrqlr
     2401 nirsksvieq vswdn
//
LOCUS       NP_001398532             399 aa            linear   ROD 28-APR-2025
DEFINITION  protein L-Myc isoform 2 [Rattus norvegicus].
ACCESSION   NP_001398532 XP_006238855
VERSION     NP_001398532.1
DBSOURCE    REFSEQ: accession NM_001411603.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Kopecky,B.J., Decook,R. and Fritzsch,B.
  TITLE     N-Myc and L-Myc are essential for hair cell formation but not
            maintenance
  JOURNAL   Brain Res 1484, 1-14 (2012)
   PUBMED   23022312
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Aug 29, 2022 this sequence version replaced XP_006238855.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.20673.1,
                                           SRR26643292.22843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..399
                     /product="protein L-Myc isoform 2"
                     /note="Avian myelocytomatosis viral (v-myc) related
                     oncogene homolog 1, lung carcinoma derived (Lmyc); protein
                     L-Myc-1; v-myc myelocytomatosis viral oncogene homolog 1,
                     lung carcinoma derived; v-myc avian myelocytomatosis viral
                     oncogene lung carcinoma derived homolog"
                     /calculated_mol_wt=43754
     Region          26..250
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          311..399
                     /region_name="bHLHzip_L-Myc"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in L-Myc and similar proteins; cd11457"
                     /db_xref="CDD:381463"
     Site            order(313,317..318,321..322,324..326,328..329,333,
                     353..354)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381463"
     Site            order(332,335..336,338..339,342,355,358..359,362,364..366,
                     368..369,371..372,375,378..379,382..383,385..387,389..390,
                     392..399)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     Site            order(332,335..336,338..339,342,355,358..359,362,364..366,
                     368..369,371..372,375,378..379,382..383,385..386,389,
                     392..393,396..397,399)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381463"
     CDS             1..399
                     /gene="Mycl"
                     /gene_synonym="Lmyc1; Mycl1"
                     /coded_by="NM_001411603.2:118..1317"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298506"
                     /db_xref="RGD:1588591"
ORIGIN      
        1 mcvcagcras psrrgaaplq vagggsegad mdfdsyqhyf ydydcgedfy rstapsediw
       61 kkfelvpspp tsppwgsgpg avdpasgisp gepwpgggag deaesrghsk awgrnyasii
      121 rrdcmwsgfs arerlervvs drlapgvprg nppkapatpd gtpsleasnp apatqcqlge
      181 pktqacsgse spsdsegeei dvvtvekrrs ldirkpvtit vradpldpcm khfhisihqq
      241 qhnyaarfpp escsqegdpe pgaqeealei eapkekeeee eeeeeeeeiv spppveneap
      301 qschpkpvss dtedvtkrkn hnflerkrrn dlrsrflalr dqvptlascs kapkvvilsk
      361 aleylqalvg aekkmatekr qlrcrqqqlq kriaylsgy
//
LOCUS       NP_073164                492 aa            linear   ROD 28-APR-2025
DEFINITION  methyl-CpG-binding protein 2 isoform 2 [Rattus norvegicus].
ACCESSION   NP_073164
VERSION     NP_073164.2
DBSOURCE    REFSEQ: accession NM_022673.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Lee,C.C., Park,K.B., Kim,M.S. and Jeon,Y.D.
  TITLE     CBP Expression Contributes to Neuropathic Pain via CREB and MeCP2
            Regulation in the Spared Nerve Injury Rat Model
  JOURNAL   Medicina (Kaunas) 60 (6), 989 (2024)
   PUBMED   38929606
  REMARK    GeneRIF: CBP Expression Contributes to Neuropathic Pain via CREB
            and MeCP2 Regulation in the Spared Nerve Injury Rat Model.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Zuo,C., Fan,P., Yang,Y. and Hu,C.
  TITLE     MiR-488-3p facilitates wound healing through CYP1B1-mediated
            Wnt/beta-catenin signaling pathway by targeting MeCP2
  JOURNAL   J Diabetes Investig 15 (2), 145-158 (2024)
   PUBMED   37961023
  REMARK    GeneRIF: MiR-488-3p facilitates wound healing through
            CYP1B1-mediated Wnt/beta-catenin signaling pathway by targeting
            MeCP2.
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Xu,M., Qi,S., Calhoun,V., Dai,J., Yu,B., Zhang,K., Pei,M., Li,C.,
            Wei,Y., Jiang,R., Zhi,D., Huang,Z., Qiu,Z., Liang,Z. and Sui,J.
  TITLE     Aberrant brain functional and structural developments in MECP2
            duplication rats
  JOURNAL   Neurobiol Dis 173, 105838 (2022)
   PUBMED   35985556
  REMARK    GeneRIF: Aberrant brain functional and structural developments in
            MECP2 duplication rats.
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Choi,M., Ko,S.Y., Seo,J.Y., Kim,D.G., Lee,H., Chung,H. and Son,H.
  TITLE     Autistic-like social deficits in hippocampal MeCP2 knockdown rat
            models are rescued by ketamine
  JOURNAL   BMB Rep 55 (5), 238-243 (2022)
   PUBMED   35410641
  REMARK    GeneRIF: Autistic-like social deficits in hippocampal MeCP2
            knockdown rat models are rescued by ketamine.
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Mao,X. and Yin,Z.
  TITLE     Inhibition of miR-205 promotes proliferation, migration and
            fibrosis of tenocytes through targeting MECP2: Implications for
            rotator cuff injury
  JOURNAL   Adv Clin Exp Med 31 (4), 437-443 (2022)
   PUBMED   35166074
  REMARK    GeneRIF: Inhibition of miR-205 promotes proliferation, migration
            and fibrosis of tenocytes through targeting MECP2: Implications for
            rotator cuff injury.
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Rountree,M.R., Bachman,K.E. and Baylin,S.B.
  TITLE     DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex
            at replication foci
  JOURNAL   Nat Genet 25 (3), 269-277 (2000)
   PUBMED   10888872
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Coy,J.F., Sedlacek,Z., Bachner,D., Delius,H. and Poustka,A.
  TITLE     A complex pattern of evolutionary conservation and alternative
            polyadenylation within the long 3'-untranslated region of the
            methyl-CpG-binding protein 2 gene (MeCP2) suggests a regulatory
            role in gene expression
  JOURNAL   Hum Mol Genet 8 (7), 1253-1262 (1999)
   PUBMED   10369871
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Nan,X., Campoy,F.J. and Bird,A.
  TITLE     MeCP2 is a transcriptional repressor with abundant binding sites in
            genomic chromatin
  JOURNAL   Cell 88 (4), 471-481 (1997)
   PUBMED   9038338
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Tate,P., Skarnes,W. and Bird,A.
  TITLE     The methyl-CpG binding protein MeCP2 is essential for embryonic
            development in the mouse
  JOURNAL   Nat Genet 12 (2), 205-208 (1996)
   PUBMED   8563762
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Lewis,J.D., Meehan,R.R., Henzel,W.J., Maurer-Fogy,I., Jeppesen,P.,
            Klein,F. and Bird,A.
  TITLE     Purification, sequence, and cellular localization of a novel
            chromosomal protein that binds to methylated DNA
  JOURNAL   Cell 69 (6), 905-914 (1992)
   PUBMED   1606614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Sep 24, 2006 this sequence version replaced NP_073164.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ897369.1, SRR26643298.33716.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMN12840115 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..492
                     /product="methyl-CpG-binding protein 2 isoform 2"
                     /note="meCP-2 protein"
                     /calculated_mol_wt=52917
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17046689,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Region          92..169
                     /region_name="MBD"
                     /note="Methyl-CpG binding domain; smart00391"
                     /db_xref="CDD:128673"
     Site            order(107,109,111,119,121,130,133,137)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51608; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Region          147..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Site            162
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2D6; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51608; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17046689,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Region          250..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Region          269..309
                     /region_name="Interaction with NCOR2.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2D6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Region          285..309
                     /region_name="Interaction with TBL1XR1.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2D6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2D6; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Region          325..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00566.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000269|PubMed:17046689; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51608; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     Site            455
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51608; propagated from
                     UniProtKB/Swiss-Prot (Q00566.1)"
     CDS             1..492
                     /gene="Mecp2"
                     /gene_synonym="MECP2_e1"
                     /coded_by="NM_022673.3:218..1696"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:29386"
                     /db_xref="RGD:3075"
ORIGIN      
        1 mvagmlglre eksedqdlqg lkekplkfkk vkkdkkedke gkheplqpsa hhsaepaeag
       61 kaetsessgs apavpeasas pkqrrsiird rgpmyddptl pegwtrklkq rksgrsagky
      121 dvylinpqgk afrskvelia yfekvgdtsl dpndfdftvt grgspsrreq kppkkpkspk
      181 apgtgrgrgr pkgsgtgrpk aaasegvqvk rvlekspgkl lvkmpfqasp ggkgegggat
      241 tsaqvmvikr pgrkrkaead pqaipkkrgr kpgsvvaaaa aeakkkavke ssirsvqetv
      301 lpikkrktre tvsievkevv kpllvstlge ksgkglktck spgrkskess pkgrsssass
      361 ppkkehhhhh hhaespkapm pllppppppe pqssedpisp pepqdlsssi ckeekmprag
      421 slesdgcpke paktqpmvaa aatttttttt tvaekykhrg egerkdivss smprpnreep
      481 vdsrtpvter vs
//
LOCUS       NP_001395889            1099 aa            linear   ROD 28-APR-2025
DEFINITION  IQ motif and SEC7 domain-containing protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001395889 XP_038964685
VERSION     NP_001395889.1
DBSOURCE    REFSEQ: accession NM_001408960.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Elagabani,M.N., Brisevac,D., Kintscher,M., Pohle,J., Kohr,G.,
            Schmitz,D. and Kornau,H.C.
  TITLE     Subunit-selective N-Methyl-d-aspartate (NMDA) Receptor Signaling
            through Brefeldin A-resistant Arf Guanine Nucleotide Exchange
            Factors BRAG1 and BRAG2 during Synapse Maturation
  JOURNAL   J Biol Chem 291 (17), 9105-9118 (2016)
   PUBMED   26884337
  REMARK    GeneRIF: both Arf6 activation through GluN2B-BRAG1 during early
            development and the transition from BRAG1- to BRAG2-dependent Arf6
            signaling induced by the GluN2 subunit switch are critical for the
            development of mature glutamatergic synapses.
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Yue,J., Xie,M., Gou,X., Lee,P., Schneider,M.D. and Wu,X.
  TITLE     Microtubules regulate focal adhesion dynamics through MAP4K4
  JOURNAL   Dev Cell 31 (5), 572-585 (2014)
   PUBMED   25490267
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Oka,S., Uramoto,H., Shimokawa,H., Yamada,S. and Tanaka,F.
  TITLE     Epidermal growth factor receptor-GEP100-Arf6 axis affects the
            prognosis of lung adenocarcinoma
  JOURNAL   Oncology 86 (5-6), 263-270 (2014)
   PUBMED   24902879
REFERENCE   4  (residues 1 to 1099)
  AUTHORS   Sakagami,H., Katsumata,O., Hara,Y., Tamaki,H., Watanabe,M.,
            Harvey,R.J. and Fukaya,M.
  TITLE     Distinct synaptic localization patterns of brefeldin A-resistant
            guanine nucleotide exchange factors BRAG2 and BRAG3 in the mouse
            retina
  JOURNAL   J Comp Neurol 521 (4), 860-876 (2013)
   PUBMED   22886754
REFERENCE   5  (residues 1 to 1099)
  AUTHORS   Dmitriev,A.A., Kashuba,V.I., Haraldson,K., Senchenko,V.N.,
            Pavlova,T.V., Kudryavtseva,A.V., Anedchenko,E.A., Krasnov,G.S.,
            Pronina,I.V., Loginov,V.I., Kondratieva,T.T., Kazubskaya,T.P.,
            Braga,E.A., Yenamandra,S.P., Ignatjev,I., Ernberg,I., Klein,G.,
            Lerman,M.I. and Zabarovsky,E.R.
  TITLE     Genetic and epigenetic analysis of non-small cell lung cancer with
            NotI-microarrays
  JOURNAL   Epigenetics 7 (5), 502-513 (2012)
   PUBMED   22491060
REFERENCE   6  (residues 1 to 1099)
  AUTHORS   Xie,C.G., Wei,S.M., Chen,J.M., Xu,X.F., Cai,J.T., Chen,Q.Y. and
            Jia,L.T.
  TITLE     Down-regulation of GEP100 causes increase in E-cadherin levels and
            inhibits pancreatic cancer cell invasion
  JOURNAL   PLoS One 7 (5), e37854 (2012)
   PUBMED   22662237
REFERENCE   7  (residues 1 to 1099)
  AUTHORS   Menju,T., Hashimoto,S., Hashimoto,A., Otsuka,Y., Handa,H.,
            Ogawa,E., Toda,Y., Wada,H., Date,H. and Sabe,H.
  TITLE     Engagement of overexpressed Her2 with GEP100 induces autonomous
            invasive activities and provides a biomarker for metastases of lung
            adenocarcinoma
  JOURNAL   PLoS One 6 (9), e25301 (2011)
   PUBMED   21966491
REFERENCE   8  (residues 1 to 1099)
  AUTHORS   Scholz,R., Berberich,S., Rathgeber,L., Kolleker,A., Kohr,G. and
            Kornau,H.C.
  TITLE     AMPA receptor signaling through BRAG2 and Arf6 critical for
            long-term synaptic depression
  JOURNAL   Neuron 66 (5), 768-780 (2010)
   PUBMED   20547133
REFERENCE   9  (residues 1 to 1099)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 1099)
  AUTHORS   Morishige,M., Hashimoto,S., Ogawa,E., Toda,Y., Kotani,H.,
            Hirose,M., Wei,S., Hashimoto,A., Yamada,A., Yano,H., Mazaki,Y.,
            Kodama,H., Nio,Y., Manabe,T., Wada,H., Kobayashi,H. and Sabe,H.
  TITLE     GEP100 links epidermal growth factor receptor signalling to Arf6
            activation to induce breast cancer invasion
  JOURNAL   Nat Cell Biol 10 (1), 85-92 (2008)
   PUBMED   18084281
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jul 5, 2022 this sequence version replaced XP_038964685.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.24121.1,
                                           SRR26360176.561874.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..1099
                     /product="IQ motif and SEC7 domain-containing protein 1
                     isoform 2"
                     /note="IQ motif and SEC7 domain-containing protein 1; IQ
                     motif and Sec7 domain 1"
                     /calculated_mol_wt=122555
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DN90; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Region          249..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2JUG7.1)"
     Region          296..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2JUG7.1)"
     Region          333..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A0G2JUG7.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Region          508..696
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          728..857
                     /region_name="IQ_SEC7_PH"
                     /note="PH domain; pfam16453"
                     /db_xref="CDD:465120"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DN90; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6DN90; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DN90; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S2; propagated from
                     UniProtKB/Swiss-Prot (A0A0G2JUG7.1)"
     CDS             1..1099
                     /gene="Iqsec1"
                     /coded_by="NM_001408960.1:363..3662"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:686590"
                     /db_xref="RGD:1596313"
ORIGIN      
        1 macrrryfve geapssetgt sldspsayhq gplvpgssls pdhyehtsvg ayglyagpgp
       61 qqrtrrprlq hstsvlrkqa eeeaikrsrs lsesyelssd lqdkqvemle rkyggrlvtr
      121 haartiqtaf rqyqmnknfe rlrssmsenr msrrivlsnm rmqfsfegpe kvhssyfegk
      181 qvsvtndgsq lgalvpsecg dlsdpalksp apssdfadai teledafsrq vkslaesidd
      241 alncrslhse evpasdtara rdtepkpglh gmdhrkldem tasysdvtly ideeelsppl
      301 plsqagdrps stesdlrlrs ggaaqdywal ahkedkadtd tscrstpsle rpeprlrveh
      361 lplltiepps dssvelsdrs drsslkrqsa yerslggqqg spkhgphggp pkglpreepe
      421 lrprpprple shlaingsan rqsksesdys dgdndsinst snsndtincs sesssrdslr
      481 eqtlskqtyh ketrnswdsp afsndvirkr hyriglnlfn kkpekgiqyl iergfvpdtp
      541 vgvahfllqr kglsrqmige flgnrqkqfn rdvldcvvde mdfsamelde alrkfqahir
      601 vqgeaqkver lieafsqryc vcnpgvvrqf rnpdtifila faiillntdm yspnvkperk
      661 mkledfvknl rgvddgedip retligiyer irkrelktne dhvsqvqkve klivgkkpig
      721 slhhglgcvl slphrrlvcy crlfevpdpn kpqklglhqr eiflfndllv vtkifqkkkn
      781 svtysfrqsf slygmqvllf enqyypngir ltsavpgadi kvlinfnapn pqdrkkftdd
      841 lresvaevqe mekhriesel ekqkgvvrps msqcsslkke sgngtlsrac lddsyasgeg
      901 lkrsalsssl rdlseagkrg rrssagsles nvegsiissp hmrrratstr ecpsrppqpv
      961 pnsssllgsl fgsrrgkppp qahppsappp apphahhpgp segplhghha qychaqqnpp
     1021 pyhhhhhyhp pphlqhthqy hhgphsghpp ygahahshpp lptahpghag hsahhhgqpp
     1081 apppptsska kpsgistvv
//
LOCUS       NP_059056                569 aa            linear   ROD 28-APR-2025
DEFINITION  coilin [Rattus norvegicus].
ACCESSION   NP_059056
VERSION     NP_059056.2
DBSOURCE    REFSEQ: accession NM_017360.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Krejci,J., Legartova,S. and Bartova,E.
  TITLE     Neural Differentiation in HDAC1-Depleted Cells Is Accompanied by
            Coilin Downregulation and the Accumulation of Cajal Bodies in
            Nucleoli
  JOURNAL   Stem Cells Int 2017, 1021240 (2017)
   PUBMED   28337219
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Stern,J.L., Zyner,K.G., Pickett,H.A., Cohen,S.B. and Bryan,T.M.
  TITLE     Telomerase recruitment requires both TCAB1 and Cajal bodies
            independently
  JOURNAL   Mol Cell Biol 32 (13), 2384-2395 (2012)
   PUBMED   22547674
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Richter,K., Brar,S., Ray,M., Pisitkun,P., Bolland,S., Verkoczy,L.
            and Diaz,M.
  TITLE     Speckled-like pattern in the germinal center (SLIP-GC), a nuclear
            GTPase expressed in activation-induced deaminase-expressing
            lymphomas and germinal center B cells
  JOURNAL   J Biol Chem 284 (44), 30652-30661 (2009)
   PUBMED   19734146
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Lemm,I., Girard,C., Kuhn,A.N., Watkins,N.J., Schneider,M.,
            Bordonne,R. and Luhrmann,R.
  TITLE     Ongoing U snRNP biogenesis is required for the integrity of Cajal
            bodies
  JOURNAL   Mol Biol Cell 17 (7), 3221-3231 (2006)
   PUBMED   16687569
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Hong,S., Ka,S., Kim,S., Park,Y. and Kang,S.
  TITLE     p80 coilin, a coiled body-specific protein, interacts with
            ataxin-1, the SCA1 gene product
  JOURNAL   Biochim Biophys Acta 1638 (1), 35-42 (2003)
   PUBMED   12757932
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Tucker,K.E., Berciano,M.T., Jacobs,E.Y., LePage,D.F.,
            Shpargel,K.B., Rossire,J.J., Chan,E.K., Lafarga,M., Conlon,R.A. and
            Matera,A.G.
  TITLE     Residual Cajal bodies in coilin knockout mice fail to recruit Sm
            snRNPs and SMN, the spinal muscular atrophy gene product
  JOURNAL   J Cell Biol 154 (2), 293-307 (2001)
   PUBMED   11470819
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Ferreira,J. and Carmo-Fonseca,M.
  TITLE     The biogenesis of the coiled body during early mouse development
  JOURNAL   Development 121 (2), 601-612 (1995)
   PUBMED   7768196
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Carmo-Fonseca,M., Ferreira,J. and Lamond,A.I.
  TITLE     Assembly of snRNP-containing coiled bodies is regulated in
            interphase and mitosis--evidence that the coiled body is a kinetic
            nuclear structure
  JOURNAL   J Cell Biol 120 (4), 841-852 (1993)
   PUBMED   7679389
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On Nov 27, 2020 this sequence version replaced NP_059056.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF399643.1, SRR26360172.1799348.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..569
                     /product="coilin"
                     /calculated_mol_wt=62287
     Region          7..138
                     /region_name="Coilin_N"
                     /note="Coilin N-terminus; pfam15862"
                     /db_xref="CDD:464910"
     CDS             1..569
                     /gene="Coil"
                     /coded_by="NM_017360.2:1..1710"
                     /db_xref="GeneID:50998"
                     /db_xref="RGD:62031"
ORIGIN      
        1 maasetvrvr lqfdypppat phctvfwllv dlnrcrvvtd lislirqrfg fssgallgly
       61 leggllppse sarlvrdndc lrvkledqgl pealivsngg dsnfpcrksk krafklvede
      121 etdqgykypd kywkrqedsg pnekasdlet klfpdevrrt knkrkskvag ipaeedeeet
      181 kkksskrkek ceqkkqtras kspkqqthke ggsqncsfpr asyrsslaka rrrsstgakg
      241 spsylseses cpdsvsdghc svttmqgvtl seklsaellk dgatktaaan rqsskpsftf
      301 ssgkgkasra sssssdssse sedqflvskn mlegasdflk ttglfagqgc sspglsletp
      361 gimgwkpsds nrgrqapgpn vpvptslgrg wgrgedflfg kglrgrgirg rgrgrgqtvs
      421 cilnrssesq kqkqlndilt nsstviqnpv etskkdysll pllaaapqvg ekiafkllel
      481 tsdyspdvsd ykegkilshd petqqvdiev lsslpalkep gkfdlvyhne ngtevveyav
      541 tqekritvfw kelidprlii dssssissk
//
LOCUS       NP_001037736             227 aa            linear   ROD 28-APR-2025
DEFINITION  prolactin family 2, subfamily C, member 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001037736 XP_001068854 XP_577570
VERSION     NP_001037736.1
DBSOURCE    REFSEQ: accession NM_001044271.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Premzl,M.
  TITLE     Curated eutherian third party data gene data sets
  JOURNAL   Data Brief 6, 208-213 (2015)
   PUBMED   26862561
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Premzl,M.
  TITLE     Third party data gene data set of eutherian growth hormone genes
  JOURNAL   Genom Data 6, 166-169 (2015)
   PUBMED   26697363
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Alam,S.M., Ain,R., Konno,T., Ho-Chen,J.K. and Soares,M.J.
  TITLE     The rat prolactin gene family locus: species-specific gene family
            expansion
  JOURNAL   Mamm Genome 17 (8), 858-877 (2006)
   PUBMED   16897344
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ329281.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_577570.2, XP_001068854.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ329281.1, LM644197.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Rattus norvegicus"
                     /strain="Holtzman Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..227
                     /product="prolactin family 2, subfamily C, member 1
                     precursor"
                     /note="growth hormone d4"
                     /calculated_mol_wt=22730
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3217
     Region          23..227
                     /region_name="Hormone_1"
                     /note="Somatotropin hormone family; pfam00103"
                     /db_xref="CDD:306585"
     Site            order(29..31,39..41,46,49..50,55,58..59,83..84,94,
                     100..101,150,153,156..157,204..205,208..209,211..213,
                     215..216,219,227)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198438"
     CDS             1..227
                     /gene="Prl2c1"
                     /gene_synonym="Ghd4; RGD1562878"
                     /coded_by="NM_001044271.1:61..744"
                     /db_xref="GeneID:502122"
                     /db_xref="RGD:1562878"
ORIGIN      
        1 mqlsltqpss willllvtnl flwknvasvp fcamrnvrcf mfledmfdla gsmshnisie
       61 vsemftefek hyakvpglkd ksltrchtts lpipenkeqa khthygallk sahmvlkawk
      121 splndlvrqi stlknipdti iskatdiklk insveqgvns iinrmlqngd eernypawss
      181 lpifksnded asirsfygmi scldndckkv diylnvlkcy vlqmdnc
//
LOCUS       NP_001161825             357 aa            linear   ROD 28-APR-2025
DEFINITION  RT1 class Ib, locus M5 isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001161825
VERSION     NP_001161825.1
DBSOURCE    REFSEQ: accession NM_001168353.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Acar,M., Cora,T., Tunc,R. and Acar,H.
  TITLE     HLA-B27 subtypes in Turkish patients with ankylosing spondylitis
            and healthy controls
  JOURNAL   Rheumatol Int 32 (10), 3103-3105 (2012)
   PUBMED   21927904
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Lambracht-Washington,D., Moore,Y.F., Wonigeit,K. and Lindahl,K.F.
  TITLE     Structure and expression of MHC class Ib genes of the central M
            region in rat and mouse: M4, M5, and M6
  JOURNAL   Immunogenetics 60 (3-4), 131-145 (2008)
   PUBMED   18324395
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Shankarkumar,U., Ghosh,K. and Mohanty,D.
  TITLE     Novel HLA B*2714 and B*2708 allele associations in seronegative
            spondarthritis patients and haemophilia patients with chronic
            synovitis in India
  JOURNAL   Tissue Antigens 62 (2), 175-178 (2003)
   PUBMED   12889998
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Gunther,E. and Walter,L.
  TITLE     The major histocompatibility complex of the rat (Rattus norvegicus)
  JOURNAL   Immunogenetics 53 (7), 520-542 (2001)
   PUBMED   11685465
  REMARK    Review article
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Gul,A., Uyar,F.A., Inanc,M., Ocal,L., Tugal-Tutkun,I., Aral,O.,
            Konice,M. and Saruhan-Direskeneli,G.
  TITLE     Lack of association of HLA-B*51 with a severe disease course in
            Behcet's disease
  JOURNAL   Rheumatology (Oxford) 40 (6), 668-672 (2001)
   PUBMED   11426025
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Orchard,T.R., Thiyagaraja,S., Welsh,K.I., Wordsworth,B.P., Hill
            Gaston,J.S. and Jewell,D.P.
  TITLE     Clinical phenotype is related to HLA genotype in the peripheral
            arthropathies of inflammatory bowel disease
  JOURNAL   Gastroenterology 118 (2), 274-278 (2000)
   PUBMED   10648455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883052.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760434
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..357
                     /product="RT1 class Ib, locus M5 isoform 1 precursor"
                     /note="major histocompatibility complex, class I, F; MHC
                     class Ib antigen RT1.M5 long isoform; MHC class Ib antigen
                     RT1.M5 short isoform"
                     /calculated_mol_wt=37969
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2047
     Region          26..204
                     /region_name="MHC_I"
                     /note="Class I Histocompatibility antigen, domains alpha 1
                     and 2; pfam00129"
                     /db_xref="CDD:395078"
     Region          208..299
                     /region_name="IgC1_MHC_I_alpha3"
                     /note="Class I major histocompatibility complex (MHC)
                     alpha chain, alpha3 immunoglobulin domain; member of the
                     C1-set of Ig superfamily (IgSF) domains; cd07698"
                     /db_xref="CDD:409495"
     Region          209..216
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409495"
     Region          224..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409495"
     Site            order(227,229,256..257,259..261,267,269)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Site            order(234..236,264,289)
                     /site_type="other"
                     /note="MHC binding domain interface [polypeptide binding]"
                     /db_xref="CDD:409495"
     Region          238..243
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409495"
     Region          246..249
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409495"
     Region          253..261
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409495"
     Region          264..274
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409495"
     Region          281..288
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409495"
     Region          295..298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409495"
     CDS             1..357
                     /gene="RT1-M5"
                     /gene_synonym="Hla-f; RGD1560260; RT1.M5"
                     /coded_by="NM_001168353.1:1..1074"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:499400"
                     /db_xref="RGD:1595816"
ORIGIN      
        1 mgssvfsvll plllsrawal nqvgagihsl qffatavtqp ssrehsfifv gfvddtqflc
       61 ynnqgesqrm epralwvknm gpgywerqtr mvkdisknsl vnlreamsvy nhsedgthvf
      121 qcvsgcdvgp dglflrgheq haydgrdyla lnkdlhswta gdtaaqitrr kweeagvaeq
      181 rrtylkgecv eslrtyleig ketllgadpp kahvthhpsp egdntlrcwa lgfypsditl
      241 twqrdgedlt qdmelvetrp ggdgtfqkwa avvvpsgeeh rytccveheg lteplllkwd
      301 pskhtipimg itaglvflgv aftgavvaia mrkqrgcrvl tpskahlers dkyltwt
//
LOCUS       NP_001417074             215 aa            linear   ROD 28-APR-2025
DEFINITION  disks large homolog 5-like isoform 1 [Rattus norvegicus].
ACCESSION   NP_001417074 XP_063122370
VERSION     NP_001417074.1
DBSOURCE    REFSEQ: accession NM_001430145.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On May 7, 2024 this sequence version replaced XP_063122370.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.944429.1,
                                           SRR26360181.2314387.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN06621351
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8"
     Protein         1..215
                     /product="disks large homolog 5-like isoform 1"
                     /calculated_mol_wt=25468
     Region          48..134
                     /region_name="Takusan"
                     /note="pfam04822"
                     /db_xref="CDD:461445"
     CDS             1..215
                     /gene="LOC134480019"
                     /coded_by="NM_001430145.1:73..720"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:134480019"
                     /db_xref="RGD:402460855"
ORIGIN      
        1 mfsrlrknfg rvnadfgqtg vresrlsski ndgqrklawg mlndgrltss pgpvvinkea
       61 ntenteeqrl irqlqsatee rnelrdllty vteryrnnra sryirsnpfy eklkikerev
      121 msllhnlemr niehcekfqe lqkeinfyrn lpsrihmdki cmqkklfpfr kegkteqlds
      181 apllqkflfd lnkkdkdeqe ktsnlqtkqh ldntt
//
LOCUS       NP_001415655            1131 aa            linear   ROD 28-APR-2025
DEFINITION  CRACD like isoform 2 [Rattus norvegicus].
ACCESSION   NP_001415655
VERSION     NP_001415655.1
DBSOURCE    REFSEQ: accession NM_001428726.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.35000.1,
                                           SRR26643294.36027.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1131
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..1131
                     /product="CRACD like isoform 2"
                     /calculated_mol_wt=120908
     Region          144..242
                     /region_name="DUF4592"
                     /note="Domain of unknown function (DUF4592); pfam15262"
                     /db_xref="CDD:464602"
     Region          <445..579
                     /region_name="PTZ00436"
                     /note="60S ribosomal protein L19-like protein;
                     Provisional"
                     /db_xref="CDD:185616"
     Region          <501..1018
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1131
                     /gene="Cracdl"
                     /gene_synonym="RGD1310819"
                     /coded_by="NM_001428726.1:261..3656"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:301351"
                     /db_xref="RGD:1310819"
ORIGIN      
        1 mistrvmdik lreaaeglge dstgkkkskf ktfkklfgkk krketaptgn sawkqnpaks
       61 evitieesgp vydsedelee srgtmgsral shdsiffpes gqdparpvrv fsqenvcdri
      121 kalqlkiqcn vklgppppgg lpikraeetg msseddglpr sppemsllhd vgpgpaikil
      181 vsssrpqspd hmsdasvssr tldgslapvv dfshppefss cldnsaakhk llvkprnqrs
      241 sklrrlssra qseclsdlsw tleeedyeek slfhvsmees pdvrqrdlmp grrsefggpa
      301 tllspggaca rrarlqhsta vsasmeeggs lgnepsslpa tpevsepmav svpgleslsl
      361 lesspyhipr veikkeelst gglcplvest skeapcgsgd vetplstdip erdvvpskeg
      421 sappegdqaf pegdttlpgg dtlppegntt ppkgvmappe rdispskdnm sppkrimapp
      481 erdkspsegd vappkrimap perdkspseg dvappkrima pperdkspse gdvappkrim
      541 apperdksps egdvtppkri mapperdksp segdvappkg imappeidks psegdvappk
      601 gimepperdm llpkgdippa ktitdtnlet psdterqdqs vqeeeltlvv prperatgte
      661 sstipapspp apksclkhkt lvpsgsaaes plkepslsvq dkaavpparh rptqaatsgg
      721 peraapgrks drsaepqrss vkrfsvtssr ararasssrl peysahvpag grapllrsgl
      781 awrseaaldd lqvppkppdr kttggdpqns gdvgagqagp gkslqdaesc aatlqepaag
      841 edqslfpvkl rstslslkyr dssaheakai krysaevrle kgglallpkd eqshvgaapa
      901 lrgsrspngq gkgktrspeq pgtkpplprk pllqsltlpy paagpdtspg eserlipvnq
      961 ppeprkeksp hqgaekgqpp aatgpgadgq ptppwitmar qkrrgapdlp vnqeekpgsr
     1021 lqktetgkqa kvaervqesv kqgdfvrsks flmtpakppv tqrqgsklsl keglqrgisl
     1081 shqnlaqaaa ttekelhqlk rasyassdqp swmelarkks qawsdmpqii k
//
LOCUS       NP_001419238             433 aa            linear   ROD 28-APR-2025
DEFINITION  BEN domain-containing protein 7 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001419238 XP_038952410
VERSION     NP_001419238.1
DBSOURCE    REFSEQ: accession NM_001432309.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000017.1.
            
            On Jul 30, 2024 this sequence version replaced XP_038952410.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582419.738338.1,
                                           SRR26643288.58186.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840106,
                                           SAMN12840108 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..433
                     /product="BEN domain-containing protein 7 isoform 1"
                     /note="BEN domain-containing protein 7"
                     /calculated_mol_wt=47952
     Region          312..391
                     /region_name="BEN"
                     /note="BEN domain; pfam10523"
                     /db_xref="CDD:463133"
     CDS             1..433
                     /gene="Bend7"
                     /gene_synonym="RGD1305898"
                     /coded_by="NM_001432309.1:398..1699"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:361275"
                     /db_xref="RGD:1305898"
ORIGIN      
        1 mefserkrsr ksqsfklvsr dyhhevykis efsndvnget ketqpmflgd gsmeikkqit
       61 gmrrllndrt griyqrvgke geklkeepqd vdlvwpqrln ssteapqglh ppsrgawnel
      121 paqsgqfsgq pgprsrtfqs qphisassng elpgvnstag sncctcncqs tlqailqelk
      181 tmrklmhfqa vgtqnrqqpp islvcsqrta isrkrnkkkk vlpkavepmt tvkpkpspse
      241 tekkpaavaa rppglqaaec asaeenhilg fgivlkspss dpevqlaegf dvfmpksqld
      301 silsnytrsg sllfrklvca ffddktlans lpngkrkrgl ndnrkgldqn ivgaikvfte
      361 nyctanhvdk lpgprdwvqi lqdqiklarr rlkrgsevad gderldgisl pptghafvsr
      421 retpedpepg sia
//
LOCUS       NP_058798                493 aa            linear   ROD 28-APR-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 3
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_058798
VERSION     NP_058798.2
DBSOURCE    REFSEQ: accession NM_017102.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Dakic,T., Lakic,I., Zec,M., Takic,M., Stojiljkovic,M. and
            Jevdjovic,T.
  TITLE     Fructose-rich diet and walnut supplementation differently regulate
            rat hypothalamic and hippocampal glucose transporters expression
  JOURNAL   J Sci Food Agric 101 (14), 5984-5991 (2021)
   PUBMED   33856052
  REMARK    GeneRIF: Fructose-rich diet and walnut supplementation differently
            regulate rat hypothalamic and hippocampal glucose transporters
            expression.
REFERENCE   2  (residues 1 to 493)
  AUTHORS   von Leden,R.E., Moritz,K.E., Bermudez,S., Jaiswal,S., Wilson,C.M.,
            Dardzinski,B.J. and Byrnes,K.R.
  TITLE     Aging alters glucose uptake in the naive and injured rodent spinal
            cord
  JOURNAL   Neurosci Lett 690, 23-28 (2019)
   PUBMED   30296507
  REMARK    GeneRIF: findings show that age alters glucose uptake and GLUT3/4
            expression profiles before and after Spinal Cord Injury.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Solis-Maldonado,M., Miro,M.P., Acuna,A.I., Covarrubias-Pinto,A.,
            Loaiza,A., Mayorga,G., Beltran,F.A., Cepeda,C., Levine,M.S.,
            Concha,I.I., Batiz,L.F., Carrasco,M.A. and Castro,M.A.
  TITLE     Altered lactate metabolism in Huntington's disease is dependent on
            GLUT3 expression
  JOURNAL   CNS Neurosci Ther 24 (4), 343-352 (2018)
   PUBMED   29582588
  REMARK    GeneRIF: Study found no differences in mRNA or protein levels of
            neuronal monocarboxylate transporters (MCTs). Functional analyses
            revealed that neuronal MCT2 had high catalytic efficiency in
            Huntington's disease (HD) cells. Ascorbic acid did not stimulate
            lactate uptake in HD cells; and was unable to inhibit glucose
            transport in HD cells because they exhibit decreased expression of
            the neuronal glucose transporter GLUT3.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Pearson-Leary,J. and McNay,E.C.
  TITLE     Novel Roles for the Insulin-Regulated Glucose Transporter-4 in
            Hippocampally Dependent Memory
  JOURNAL   J Neurosci 36 (47), 11851-11864 (2016)
   PUBMED   27881773
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Deng,D., Sun,P., Yan,C., Ke,M., Jiang,X., Xiong,L., Ren,W.,
            Hirata,K., Yamamoto,M., Fan,S. and Yan,N.
  TITLE     Molecular basis of ligand recognition and transport by glucose
            transporters
  JOURNAL   Nature 526 (7573), 391-396 (2015)
   PUBMED   26176916
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Campbell,I.W., Dominiczak,A.F., Livingstone,C. and Gould,G.W.
  TITLE     Analysis of the glucose transporter compliment of metabolically
            important tissues from the Milan hypertensive rat
  JOURNAL   Biochem Biophys Res Commun 211 (3), 780-791 (1995)
   PUBMED   7598707
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Krishnan,S.N. and Haddad,G.G.
  TITLE     Cloning of glucose transporter-3 (GLUT3) cDNA from rat brain
  JOURNAL   Life Sci 56 (14), 1193-1197 (1995)
   PUBMED   7475896
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Simpson,I.A., Chundu,K.R., Davies-Hill,T., Honer,W.G. and Davies,P.
  TITLE     Decreased concentrations of GLUT1 and GLUT3 glucose transporters in
            the brains of patients with Alzheimer's disease
  JOURNAL   Ann Neurol 35 (5), 546-551 (1994)
   PUBMED   8179300
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Nagamatsu,S., Sawa,H., Kamada,K., Nakamichi,Y., Yoshimoto,K. and
            Hoshino,T.
  TITLE     Neuron-specific glucose transporter (NSGT): CNS distribution of
            GLUT3 rat glucose transporter (RGT3) in rat central neurons
  JOURNAL   FEBS Lett 334 (3), 289-295 (1993)
   PUBMED   8243635
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Colville,C.A., Seatter,M.J., Jess,T.J., Gould,G.W. and Thomas,H.M.
  TITLE     Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3)
            glucose transporters in Xenopus oocytes: substrate specificities
            and effects of transport inhibitors
  JOURNAL   Biochem J 290 (Pt 3) (Pt 3), 701-706 (1993)
   PUBMED   8457197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jun 10, 2007 this sequence version replaced NP_058798.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643295.19679.1,
                                           SRR26643292.19637.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..493
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 3 isoform 1"
                     /note="GLUT-3; glucose transporter type 3, brain; solute
                     carrier family 2, facilitated glucose transporter member
                     3-like; solute carrier family 2 (facilitated glucose
                     transporter), member 3; solute carrier family 2, member 2;
                     Solute carrier family 2 A3 (neuron glucose transporter)"
                     /calculated_mol_wt=53432
     Site            11..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Region          12..456
                     /region_name="MFS_GLUT_Class1"
                     /note="Class 1 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17431"
                     /db_xref="CDD:340989"
     Site            order(24,28,159,162..163,166,280..281,285..286,289,315,
                     377..378,382,386,409,413)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340989"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            119..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            154..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P32037; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     Site            270..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Region          277..279
                     /region_name="Important for selectivity against fructose.
                     /evidence=ECO:0000250|UniProtKB:P11169"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            332..352
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            364..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            400..420
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            430..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07647.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P32037; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q07647.1)"
     CDS             1..493
                     /gene="Slc2a3"
                     /gene_synonym="GLUT3"
                     /coded_by="NM_017102.3:124..1605"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:25551"
                     /db_xref="RGD:3706"
ORIGIN      
        1 mgtakvtpsl vfavtvatig sfqfgyntgv inapetiikd flnytleerl edlpsegllt
       61 tlwslcvaif svggmigsfs vglfvnrfgr rnsmllvnli ailggclmgf akiaesveml
      121 ilgrliigif cglctgfvpm yigevsptal rgafgtlnql givvgilvaq vfgldfilgs
      181 eelwpgllgl tiipailqsa alpfcpespr fllinrkeed qateilqrlw gtpdviqeiq
      241 emkdesirms qekqvtvlel fkspsyfqpl lisvvlqlsq qfsginavfy ystgifqdag
      301 vqepiyatig agvvntiftv vslflverag rrtlhmiglg gmavcsvfmt islllkdeye
      361 amsfvcivai lvyvaffeig pgpipwfiva elfsqgprpa amavagcsnw tsnflvgmff
      421 psaaaylgay vfiifaaflv ffliftffkv petkgrtfed itrafegqaq sgkgsagvel
      481 nsmqpvketp gna
//
LOCUS       NP_001180221            2187 aa            linear   ROD 28-APR-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 12 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001180221 XP_002727624
VERSION     NP_001180221.1
DBSOURCE    REFSEQ: accession NM_001193292.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2187)
  AUTHORS   Makinen,N., Aavikko,M., Heikkinen,T., Taipale,M., Taipale,J.,
            Koivisto-Korander,R., Butzow,R. and Vahteristo,P.
  TITLE     Exome Sequencing of Uterine Leiomyosarcomas Identifies Frequent
            Mutations in TP53, ATRX, and MED12
  JOURNAL   PLoS Genet 12 (2), e1005850 (2016)
   PUBMED   26891131
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2187)
  AUTHORS   Lesca,G., Moizard,M.P., Bussy,G., Boggio,D., Hu,H., Haas,S.A.,
            Ropers,H.H., Kalscheuer,V.M., Des Portes,V., Labalme,A.,
            Sanlaville,D., Edery,P., Raynaud,M. and Lespinasse,J.
  TITLE     Clinical and neurocognitive characterization of a family with a
            novel MED12 gene frameshift mutation
  JOURNAL   Am J Med Genet A 161A (12), 3063-3071 (2013)
   PUBMED   24039113
REFERENCE   3  (residues 1 to 2187)
  AUTHORS   Poss,Z.C., Ebmeier,C.C. and Taatjes,D.J.
  TITLE     The Mediator complex and transcription regulation
  JOURNAL   Crit Rev Biochem Mol Biol 48 (6), 575-608 (2013)
   PUBMED   24088064
  REMARK    Review article
REFERENCE   4  (residues 1 to 2187)
  AUTHORS   Vogl,M.R., Reiprich,S., Kuspert,M., Kosian,T., Schrewe,H.,
            Nave,K.A. and Wegner,M.
  TITLE     Sox10 cooperates with the mediator subunit 12 during terminal
            differentiation of myelinating glia
  JOURNAL   J Neurosci 33 (15), 6679-6690 (2013)
   PUBMED   23575864
REFERENCE   5  (residues 1 to 2187)
  AUTHORS   Vulto-van Silfhout,A.T., de Vries,B.B., van Bon,B.W., Hoischen,A.,
            Ruiterkamp-Versteeg,M., Gilissen,C., Gao,F., van Zwam,M.,
            Harteveld,C.L., van Essen,A.J., Hamel,B.C., Kleefstra,T.,
            Willemsen,M.A., Yntema,H.G., van Bokhoven,H., Brunner,H.G.,
            Boyer,T.G. and de Brouwer,A.P.
  TITLE     Mutations in MED12 cause X-linked Ohdo syndrome
  JOURNAL   Am J Hum Genet 92 (3), 401-406 (2013)
   PUBMED   23395478
REFERENCE   6  (residues 1 to 2187)
  AUTHORS   Ge,K., Guermah,M., Yuan,C.X., Ito,M., Wallberg,A.E.,
            Spiegelman,B.M. and Roeder,R.G.
  TITLE     Transcription coactivator TRAP220 is required for PPAR gamma
            2-stimulated adipogenesis
  JOURNAL   Nature 417 (6888), 563-567 (2002)
   PUBMED   12037571
REFERENCE   7  (residues 1 to 2187)
  AUTHORS   Kang,Y.K., Guermah,M., Yuan,C.X. and Roeder,R.G.
  TITLE     The TRAP/Mediator coactivator complex interacts directly with
            estrogen receptors alpha and beta through the TRAP220 subunit and
            directly enhances estrogen receptor function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2642-2647 (2002)
   PUBMED   11867769
REFERENCE   8  (residues 1 to 2187)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   9  (residues 1 to 2187)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 2187)
  AUTHORS   Ito,M., Yuan,C.X., Malik,S., Gu,W., Fondell,J.D., Yamamura,S.,
            Fu,Z.Y., Zhang,X., Qin,J. and Roeder,R.G.
  TITLE     Identity between TRAP and SMCC complexes indicates novel pathways
            for the function of nuclear receptors and diverse mammalian
            activators
  JOURNAL   Mol Cell 3 (3), 361-370 (1999)
   PUBMED   10198638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Jul 18, 2010 this sequence version replaced XP_002727624.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.68160.1,
                                           SRR26643298.32178.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2187
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq22"
     Protein         1..2187
                     /product="mediator of RNA polymerase II transcription
                     subunit 12 isoform 2"
                     /note="mediator of RNA polymerase II transcription subunit
                     12"
                     /calculated_mol_wt=244096
     Region          106..161
                     /region_name="Med12"
                     /note="Transcription mediator complex subunit Med12;
                     pfam09497"
                     /db_xref="CDD:462818"
     Region          287..758
                     /region_name="Med12-LCEWAV"
                     /note="Eukaryotic Mediator 12 subunit domain; pfam12145"
                     /db_xref="CDD:463472"
     Region          1821..2024
                     /region_name="Med12-PQL"
                     /note="Eukaryotic Mediator 12 catenin-binding domain;
                     pfam12144"
                     /db_xref="CDD:463471"
     CDS             1..2187
                     /gene="Med12"
                     /coded_by="NM_001193292.2:22..6585"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:679693"
                     /db_xref="RGD:1585896"
ORIGIN      
        1 maafgilsye hrplkrlrlg ppdvypqdpk qkedeltaln vkqgfnnqpa vsgdehgsak
       61 nvnfnpakis snfssiiaek lrcntlsdtg rrkslmnqkd nfwlvtarsq saintwftdl
      121 agtkplthla kkvpifskke evfgylakyt vpvmraawli kmtcayyaam setkvkkknt
      181 adpftewtqi itkylweqlq kmaeyyrpgp agsgvcgsai gplphdvema irqwdynekl
      241 alfmfqdgml drhefltwvl ecfekirpge dellklllpl llrysgefvq saylsrrlay
      301 fctrrlalql dgvnshsshv isaqstsslp ttpapqppts ntpstpfsdl lmcpqhrplv
      361 fglscilqti llccpsalvw hysltdsrik tgspldhlpi apsnlpmpeg nsaftqqvra
      421 klreieqqik ergqavevrw sfdkcqeata gftigrvlht levldshsfe rsdfsnslds
      481 lcnrifglgp skdgheissd ddavvsllce wavsckrsgr hramvvakll ekrqaeieae
      541 rcgeseaade kgsvasgsls apsapifqdv llqfldtqap mltdprsese rveffnlvll
      601 fcelirhdvf shnmytctli srgdlafgtp gprppspfdd paddperkea egsssskled
      661 pglsesmdid psssvlfedm ekpdfslfsp tmpcegkgsp spekpdvekd vkpppkekie
      721 gtlgilydqp rhvqyathfp ipqeescshe cnqrlvvlfg vgkqrddarh aikkitkdil
      781 kvlnrkgtae tdqlapivpl npgdltflgg edgqkrrrnr peafptaedi fakfqhlshy
      841 dqhqvtaqvs rnvleqitsf algmsyhlpl vqhvqfvfdl meyslsisgl idfaiqllne
      901 lsvveaelll kssdlvgsyt tslclcivav lrhyhaclil nqdqmaqvfe glcgvvkhgm
      961 nrsdgssaer cilaylydly tscshlkskf gelfsdfcsk vkntiycnve psesnmrwap
     1021 efmidtlenp aahtftytgl gkslsenpan rysfvcnalm hvcvghhdpd rvndiailca
     1081 eltgycksls aewlgvlkal ccssnngtcg fndllcnvdv sdlsfhdsla tfvailiarq
     1141 cllledlirc aaipsllnaa cseqdsepga rltcrillhl fktpqlnpcq sdgnkptvgi
     1201 rsscdrhlla asqnrivdga vfavlkavfv lgdaelkgsg ftvpggteel peeeggggss
     1261 grrqggrnis vetasldvya kyvlrsicqq ewvgerclks lcedsndlqd pvlssaqaqr
     1321 lmqlicyphr lldsedgenp qrqrikrilk nldqwtmrqs slelqlmikq tpntemnsll
     1381 eniakatiev fqqsaetgss sgstasnmps sskakpvlss lersgvwlva pliaklptsv
     1441 qghvlkaage elekgqhlgs ssrkerdrqk qksmsllsqq pflslvltcl kgqdeqregl
     1501 laslhsqvhq ivinwrenqy lddckpkqlm healklrlnl vggmfdtvqr stqqttewaq
     1561 llleiiisgt vdmqsnnelf ttvldmlsvl ingtlaadms sisqgsmeen kraymnlvkk
     1621 lqkdlgerqs dslekvhqll plpkqnrdvi tcepqgslid tkgnkiagfd sifkkeglqv
     1681 stkqkispwe lfeglkpsta plswawfgtv rvdrrvarge eqqrlllyht hlrprprayy
     1741 leplplpped eeppapalle pekkapeppk tdkpgtapps teerkkkstk gkkrsqpatk
     1801 sedygmgpgr sgpygvtvpp dllhhanpgs ishlsyrqss mglytqnqpl paggprvdpy
     1861 rpvrlpmqkl ptrptypgvl pttmttvmgl epssyktsvy rqqqptvpqg qrlrqqlqqs
     1921 qgmlgqssvh qmtpsssygl qssqgytsyv shvglqqhtg pagtmvppsy ssqpyqsthp
     1981 stnptlvdpt rhlqqrpsgy vhqqaptygh gltstqrfsh qtlqqtpmmg tmtplsaqgv
     2041 qagvrstsil peqqqqqqqq qqqqqqqqqq qqqqqqqqqq qqqqyhirqq qqqqqilrqq
     2101 qqqqqqqqqq qqqqqqqqqq qpqqqqphqq qqqaappqpq pqsqpqfqrq glqqtqqqqq
     2161 taalvrqlqq qlsntqpqps tnifgry
//
LOCUS       NP_001420121             176 aa            linear   ROD 28-APR-2025
DEFINITION  DPY30 domain-containing protein 1 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001420121 XP_006252879
VERSION     NP_001420121.1
DBSOURCE    REFSEQ: accession NM_001433192.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Aug 7, 2024 this sequence version replaced XP_006252879.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.73935.1,
                                           SRR26360181.162627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..176
                     /product="DPY30 domain-containing protein 1 isoform 1"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20423
     Region          2..44
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..176
                     /gene="Dydc1"
                     /coded_by="NM_001433192.1:132..662"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:688433"
                     /db_xref="RGD:1588855"
ORIGIN      
        1 mesrylqqcl gtcltqglae varvrpldpi eylalwiyky kenesmeqlr qkelialehe
       61 relammeqem mdrlkaeell fqqqqlafql elemqekekq ktedfkteqe kstkdtmste
      121 siskgeeamp seesmmdsgk tlaeisdryg apnlsrveel depmlsdial nidqdl
//
LOCUS       NP_001388925            1287 aa            linear   ROD 28-APR-2025
DEFINITION  mitogen-activated protein kinase kinase kinase kinase 4 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001388925
VERSION     NP_001388925.1
DBSOURCE    REFSEQ: accession NM_001401996.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1287)
  AUTHORS   Yang,J., Zheng,X.G., Wu,Y.L., Wang,A.P., Wang,C.H., Chen,W.X.,
            Zhong,S. and Yang,H.
  TITLE     Intestinal epithelial cell-derived exosomes package microRNA-23a-3p
            alleviate gut damage after ischemia/reperfusion via targeting
            MAP4K4
  JOURNAL   Biomed Pharmacother 149, 112810 (2022)
   PUBMED   35303564
  REMARK    GeneRIF: Intestinal epithelial cell-derived exosomes package
            microRNA-23a-3p alleviate gut damage after ischemia/reperfusion via
            targeting MAP4K4.
REFERENCE   2  (residues 1 to 1287)
  AUTHORS   Li,W., Liu,S., Su,S., Chen,Y. and Sun,G.
  TITLE     Construction and validation of a novel prognostic signature of
            microRNAs in lung adenocarcinoma
  JOURNAL   PeerJ 9, e10470 (2021)
   PUBMED   33510968
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1287)
  AUTHORS   Chen,S., Tang,Y., Yang,C., Li,K., Huang,X. and Cao,J.
  TITLE     Silencing CDC25A inhibits the proliferation of liver cancer cells
            by downregulating IL-6 in vitro and in vivo
  JOURNAL   Int J Mol Med 45 (3), 743-752 (2020)
   PUBMED   31922225
REFERENCE   4  (residues 1 to 1287)
  AUTHORS   Lin,J.C., Lee,Y.C., Tan,T.H., Liang,Y.C., Chuang,H.C., Fann,Y.C.,
            Johnson,K.R. and Lin,Y.J.
  TITLE     RBM4-SRSF3-MAP4K4 splicing cascade modulates the metastatic
            signature of colorectal cancer cell
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1865 (2), 259-272 (2018)
   PUBMED   29138007
REFERENCE   5  (residues 1 to 1287)
  AUTHORS   Gao,X., Chen,G., Gao,C., Zhang,D.H., Kuan,S.F., Stabile,L.P.,
            Liu,G. and Hu,J.
  TITLE     MAP4K4 is a novel MAPK/ERK pathway regulator required for lung
            adenocarcinoma maintenance
  JOURNAL   Mol Oncol 11 (6), 628-639 (2017)
   PUBMED   28306189
REFERENCE   6  (residues 1 to 1287)
  AUTHORS   Bouzakri,K., Ribaux,P. and Halban,P.A.
  TITLE     Silencing mitogen-activated protein 4 kinase 4 (MAP4K4) protects
            beta cells from tumor necrosis factor-alpha-induced decrease of
            IRS-2 and inhibition of glucose-stimulated insulin secretion
  JOURNAL   J Biol Chem 284 (41), 27892-27898 (2009)
   PUBMED   19690174
  REMARK    GeneRIF: Results identify MAP4K4 as a key upstream mediator of
            TNF-alpha action on the beta cell, preventing tumor necrosis
            factor-alpha-induced decrease of IRS-2 and inhibition of
            glucose-stimulated insulin secretion.
REFERENCE   7  (residues 1 to 1287)
  AUTHORS   Loh,S.H., Francescut,L., Lingor,P., Bahr,M. and Nicotera,P.
  TITLE     Identification of new kinase clusters required for neurite
            outgrowth and retraction by a loss-of-function RNA interference
            screen
  JOURNAL   Cell Death Differ 15 (2), 283-298 (2008)
   PUBMED   18007665
REFERENCE   8  (residues 1 to 1287)
  AUTHORS   Machida,N., Umikawa,M., Takei,K., Sakima,N., Myagmar,B.E.,
            Taira,K., Uezato,H., Ogawa,Y. and Kariya,K.
  TITLE     Mitogen-activated protein kinase kinase kinase kinase 4 as a
            putative effector of Rap2 to activate the c-Jun N-terminal kinase
  JOURNAL   J Biol Chem 279 (16), 15711-15714 (2004)
   PUBMED   14966141
REFERENCE   9  (residues 1 to 1287)
  AUTHORS   Yao,Z., Zhou,G., Wang,X.S., Brown,A., Diener,K., Gan,H. and
            Tan,T.H.
  TITLE     A novel human STE20-related protein kinase, HGK, that specifically
            activates the c-Jun N-terminal kinase signaling pathway
  JOURNAL   J Biol Chem 274 (4), 2118-2125 (1999)
   PUBMED   9890973
REFERENCE   10 (residues 1 to 1287)
  AUTHORS   Su,Y.C., Han,J., Xu,S., Cobb,M. and Skolnik,E.Y.
  TITLE     NIK is a new Ste20-related kinase that binds NCK and MEKK1 and
            activates the SAPK/JNK cascade via a conserved regulatory domain
  JOURNAL   EMBO J 16 (6), 1279-1290 (1997)
   PUBMED   9135144
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMN12840105 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1287
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..1287
                     /product="mitogen-activated protein kinase kinase kinase
                     kinase 4 isoform 2"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=146562
     Region          8..289
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(31..34,37,39,52,54,83,105..108,153,157..158,160,
                     170..171)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270806"
     Region          969..1267
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..1287
                     /gene="Map4k4"
                     /coded_by="NM_001401996.1:314..4177"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:301363"
                     /db_xref="RGD:1305322"
ORIGIN      
        1 mandspaksl vdidlsslrd pagifelvev vgngtygqvy kgrhvktgql aaikvmdvte
       61 deeeeiklei nmlkkyshhr niatyygafi kksppghddq lwlvmefcga gsitdlvknt
      121 kgntlkedwi ayisreilrg lahlhihhvi hrdikgqnvl ltenaevklv dfgvsaqldr
      181 tvgrrntfig tpywmapevi acdenpdaty dyrsdlwscg itaiemaega pplcdmhpmr
      241 alfliprnpp prlkskkwsk kffsfiegcl vknymqrpst eqllkhpfir dqpnerqvri
      301 qlkdhidrtr kkrgekdete yeysgseeee eevpeqegep ssivnvpges tlrrdflrlq
      361 qenkerseal rrqqllqeqq lreqeeykrq llaerqkrie qqkeqrrrle eqqrrerear
      421 rqqereqrrr eqeekrrlee lerrrkeeee rrraedekrr vereqeyirr qleeeqrhle
      481 ilqqqllqeq amllhdhrrp haqqppppqq qdrskpsyha pepkphydpa drarevedrf
      541 rktnhsspea qakqtgrgle ppvpsrsesf sngnsesvhp alqrpaepqv qwshlaslkn
      601 nvspvsrshs fsdpspkfah hhlrsqdpcp psrseglsqs sdsksevpep tqkawsrsds
      661 devpprvpvr ttsrspvlsr rdsplqgsgq qnsqagqrns tssieprllw erveklvprp
      721 gsgsssgssn sgsqpgshpg sqsgsgerfr vrsssksegs psqrlenaak kpedkkevfr
      781 plkpagevdl talakelrav edvrpphkvt dysssseesg ttdeeeedve qegaddstsg
      841 pedtraassl nlsngetesv ktmivhddve sepamtpske gtlivrqtqs asstlqkhks
      901 sssftpfidp rllqispssg ttvtsvvgfs cdglrpeair qdptrkgsvv nvnptntrpq
      961 sdtpeirkyk krfnseilca alwgvnllvg tesglmlldr sgqgkvypli srrrfqqmdv
     1021 leglnvlvti sgkkdklrvy ylswlrnkil hndpevekkq gwttvgdleg cvhykvvkye
     1081 rikflvialk ssvevyawap kpyhkfmafk sfgelvhkpl lvdltveegq rlkviygsca
     1141 gfhavdvdsg svydiylpth iqctikphai iilpntdgme llvcyedegv yvntygritk
     1201 dvvlqwgemp tsvayirsnq tmgwgekaie irsvetghld gvfmhkraqr lkflcerndk
     1261 vffasvrsgg ssqvyfmtlg rtsllsw
//
LOCUS       NP_036844                841 aa            linear   ROD 28-APR-2025
DEFINITION  fibroblast growth factor receptor 2 isoform a precursor [Rattus
            norvegicus].
ACCESSION   NP_036844
VERSION     NP_036844.1
DBSOURCE    REFSEQ: accession NM_012712.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Tian,M., Yang,J., Yan,X., Cao,Y., Liu,Y., Lei,Y. and Lv,H.
  TITLE     Knockdown of lncRNA TUG1 alleviates diabetic retinal vascular
            dysfunction through regulating miR-524-5p/FGFR2
  JOURNAL   Bioengineered 13 (5), 12661-12672 (2022)
   PUBMED   35599572
  REMARK    GeneRIF: Knockdown of lncRNA TUG1 alleviates diabetic retinal
            vascular dysfunction through regulating miR-524-5p/FGFR2.
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Kilcoyne,S., Potter,K.R., Gordon,Z., Overton,S., Brockbank,S.,
            Jayamohan,J., Magdum,S., Smith,M., Johnson,D., Wall,S. and
            Wilkie,A.O.M.
  TITLE     Feeding, Communication, Hydrocephalus, and Intracranial
            Hypertension in Patients With Severe FGFR2-Associated Pfeiffer
            Syndrome
  JOURNAL   J Craniofac Surg 32 (1), 134-140 (2021)
   PUBMED   33074973
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Zhu,M., Chen,G., Yang,Y., Yang,J., Qin,B. and Gu,L.
  TITLE     miR-217-5p regulates myogenesis in skeletal muscle stem cells by
            targeting FGFR2
  JOURNAL   Mol Med Rep 22 (2), 850-858 (2020)
   PUBMED   32626929
  REMARK    GeneRIF: miR2175p regulates myogenesis in skeletal muscle stem
            cells by targeting FGFR2.
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Xu,Z., Zhu,X., Wang,M., Lu,Y. and Dai,C.
  TITLE     FGF/FGFR2 Protects against Tubular Cell Death and Acute Kidney
            Injury Involving Erk1/2 Signaling Activation
  JOURNAL   Kidney Dis (Basel) 6 (3), 181-194 (2020)
   PUBMED   32523960
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Chen,P., Xu,B., Feng,Y., Li,K.X., Liu,Z., Sun,X., Lu,X.L.,
            Wang,L.Q., Chen,Y.W., Fan,X.X., Yang,X.L., Wang,N., Qiao,G.F. and
            Li,B.Y.
  TITLE     FGF-21 ameliorates essential hypertension of SHR via baroreflex
            afferent function
  JOURNAL   Brain Res Bull 154, 9-20 (2020)
   PUBMED   31626954
REFERENCE   6  (residues 1 to 841)
  AUTHORS   Park,W.J., Theda,C., Maestri,N.E., Meyers,G.A., Fryburg,J.S.,
            Dufresne,C., Cohen,M.M. Jr. and Jabs,E.W.
  TITLE     Analysis of phenotypic features and FGFR2 mutations in Apert
            syndrome
  JOURNAL   Am J Hum Genet 57 (2), 321-328 (1995)
   PUBMED   7668257
REFERENCE   7  (residues 1 to 841)
  AUTHORS   Schell,U., Hehr,A., Feldman,G.J., Robin,N.H., Zackai,E.H., de
            Die-Smulders,C., Viskochil,D.H., Stewart,J.M., Wolff,G., Ohashi,H.
            et al.
  TITLE     Mutations in FGFR1 and FGFR2 cause familial and sporadic Pfeiffer
            syndrome
  JOURNAL   Hum Mol Genet 4 (3), 323-328 (1995)
   PUBMED   7795583
REFERENCE   8  (residues 1 to 841)
  AUTHORS   Jabs,E.W., Li,X., Scott,A.F., Meyers,G., Chen,W., Eccles,M.,
            Mao,J.I., Charnas,L.R., Jackson,C.E. and Jaye,M.
  TITLE     Jackson-Weiss and Crouzon syndromes are allelic with mutations in
            fibroblast growth factor receptor 2
  JOURNAL   Nat Genet 8 (3), 275-279 (1994)
   PUBMED   7874170
  REMARK    Erratum:[Nat Genet 1995 Apr;9(4):451]
REFERENCE   9  (residues 1 to 841)
  AUTHORS   Reardon,W., Winter,R.M., Rutland,P., Pulleyn,L.J., Jones,B.M. and
            Malcolm,S.
  TITLE     Mutations in the fibroblast growth factor receptor 2 gene cause
            Crouzon syndrome
  JOURNAL   Nat Genet 8 (1), 98-103 (1994)
   PUBMED   7987400
REFERENCE   10 (residues 1 to 841)
  AUTHORS   Savagner,P., Valles,A.M., Jouanneau,J., Yamada,K.M. and Thiery,J.P.
  TITLE     Alternative splicing in fibroblast growth factor receptor 2 is
            associated with induced epithelial-mesenchymal transition in rat
            bladder carcinoma cells
  JOURNAL   Mol Biol Cell 5 (8), 851-862 (1994)
   PUBMED   7803853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW531062.1, BF420170.1, L19104.1, CB777398.1, L19110.1, CB780941.1,
            CB716134.1, CO397781.1, CF109832.1, DV718561.1 and CB769194.1.
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00155311, SAMD00155315
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..841
                     /product="fibroblast growth factor receptor 2 isoform a
                     precursor"
                     /EC_number="2.7.10.1"
                     /calculated_mol_wt=89945
     sig_peptide     1..40
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4245
     Region          50..143
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          77..81
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409362"
     Region          88..92
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409362"
     Region          109..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409362"
     Region          123..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409362"
     Region          136..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409362"
     Region          173..267
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          173..176
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          184..189
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(185,187,189)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(186,193..195,197)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          193..201
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          207..212
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          215..217
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          226..229
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          233..238
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          247..254
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          257..267
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          275..377
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          293..297
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          306..310
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..346
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..361
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          369..372
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          476..788
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(507..508,510,515,535,537,554,584..587,591,646,
                     650..651,653,664,682..686,695,729)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(507..508,510,515,535,537,554,584..587,591,650..651,
                     653,664)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(646,650,682..686,695,729)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            663..688
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..841
                     /gene="Fgfr2"
                     /gene_synonym="KGFR"
                     /coded_by="NM_012712.1:590..3115"
                     /note="isoform a precursor is encoded by transcript
                     variant a"
                     /db_xref="GeneID:25022"
                     /db_xref="RGD:2611"
ORIGIN      
        1 mglpstwryg tgpgigtvtm vswgrficlv lvtmatlsla rpsfslvedt tlepeepptk
       61 yqisqpeacv vapgeslelr cmlkdaavis wtkdgvhlgp nnrtvligey lqikgatprd
      121 sglyacaaar tvdsetlyfm vnvtdaissg ddeddtdsse dfvsenrsnq rapywtntek
      181 mekrlhavpa antvkfrcpa ggnptptmrw lkngkefkqe hriggykvrn qhwslimesv
      241 vpsdkgnytc lveneygsin htyhldvver sphrpilqag lpanastvvg gdvefvckvy
      301 sdaqphiqwi khvekngsky gpdglpylkv lkhsginssn aevlalfnvt emdageyick
      361 vsnyigqanq sawltvlpkq qapvrekeit aspdyleiai ycigvfliac mvvtvifcrm
      421 ktttkkpdfs sqpavhkltk riplrrqvtv saessssmns ntplvrittr lsstadtpml
      481 agvseyelpe dpkwefprdk ltlgkplgeg cfgqvvmaea vgidkdrpke avtvavkmlk
      541 ddatekdlsd lvsememmkm igkhkniinl lgactqdgpl yviveyaskg nlreylrarr
      601 ppgmeysydi nrvpeeqmtf kdlvsctyql argmeylasq kcihrdlaar nvlvtennvm
      661 kiadfglard innidyykkt tngrlpvkwm apealfdrvy thqsdvwsfg vlmweiftlg
      721 gspypgipve elfkllkegh rmdkptnctn elymmmrdcw havpsqrptf kqlvedldri
      781 ltlttneeyl dltqpleqys psypdtrssc ssgddsvfsp dpmpydpclp qyphingsvk
      841 t
//
LOCUS       NP_001178889             768 aa            linear   ROD 28-APR-2025
DEFINITION  TSC22 domain family protein 2 [Rattus norvegicus].
ACCESSION   NP_001178889 XP_574948
VERSION     NP_001178889.1
DBSOURCE    REFSEQ: accession NM_001191960.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Fiol,D.F., Mak,S.K. and Kultz,D.
  TITLE     Specific TSC22 domain transcripts are hypertonically induced and
            alternatively spliced to protect mouse kidney cells during osmotic
            stress
  JOURNAL   FEBS J 274 (1), 109-124 (2007)
   PUBMED   17147695
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_574948.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.6137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..768
                     /product="TSC22 domain family protein 2"
                     /calculated_mol_wt=78287
     Region          <232..630
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          681..743
                     /region_name="ZIP_TSC22D2"
                     /note="leucine zipper domain found in TSC22 domain family
                     protein 2; cd21939"
                     /db_xref="CDD:409279"
     Site            order(695..697,700,703..704,707..708,710..711,714..715,
                     717..718,721..722,725,729)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:409279"
     CDS             1..768
                     /gene="Tsc22d2"
                     /coded_by="NM_001191960.1:1..2307"
                     /db_xref="GeneID:499624"
                     /db_xref="RGD:1593169"
ORIGIN      
        1 mskmpakkks cfqitsvtta qvatsitedt eslddpdesr tedvsseifd vsratdygpe
       61 evcersssee tlnnvgdaet pgtvspnlil dgqlaaasav panggggvpa rsvagalsqt
      121 laavatsvsa pgpssatpsq ppatcssrfr vikldhgsge pyrrgrwtcm eyyerdsdss
      181 vlsrsgdcir hsntleqtae rdsglgatgg svvvvvasmq gahgldsgtd ssltavsqlp
      241 psekmsqptl aqpqsfsvgq pqppppvgga vapssvslpl fpgaatgsqp mtaatqptql
      301 qgavaggalp gpvgqglppp pnvnlaqpva ltaqpgpavg sslsqqfayp qppippghll
      361 pvqpsgqsey lpphvalqpp spaqplstsa satsasaasf plgsgqsvss lgaqmmgasa
      421 qpsevvapgp vpvgqaapcq pagvapaaig gvvqpgsglt gvgqpqsvqp pphmggsvql
      481 savpggphtv vpgvpnvpaa vpvpsvpvvp ttsvtmpnvp aplgqsqqls ghtpvsrsss
      541 viqqvgppla qgthsaptsl pqsdlsqfqt qtqslvrqid dtrrkseplp qaplsliaen
      601 kpvvkppvad alanplqltp mnslatsvfs iaipvdgded rnpstafyqa fhlntfqesk
      661 slwdsasggg vvaidnkieq amdlvkshlm yavreevevl keqikelver nsllerenal
      721 lkslsnndql sqlpaqqanp gstsqqqami aqppqptqpp qqpnvssa
//
LOCUS       NP_001416398             221 aa            linear   ROD 28-APR-2025
DEFINITION  synaptosomal-associated protein 23 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001416398 XP_038961739
VERSION     NP_001416398.1
DBSOURCE    REFSEQ: accession NM_001429469.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Dolai,S., Takahashi,T., Qin,T., Liang,T., Xie,L., Kang,F.,
            Miao,Y.F., Xie,H., Kang,Y., Manuel,J., Winter,E., Roche,P.A.,
            Cattral,M.S. and Gaisano,H.Y.
  TITLE     Pancreas-specific SNAP23 depletion prevents pancreatitis by
            attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes
  JOURNAL   Autophagy 17 (10), 3068-3081 (2021)
   PUBMED   33213278
  REMARK    GeneRIF: Pancreas-specific SNAP23 depletion prevents pancreatitis
            by attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes.
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Serrano-Lopez,E.M., Lopez-Martinez,D., Gomez-Fernandez,J.C.,
            Egea-Jimenez,A.L. and Corbalan-Garcia,S.
  TITLE     PKCepsilon controls the fusion of secretory vesicles in mast cells
            in a phosphatidic acid-dependent mode
  JOURNAL   Int J Biol Macromol 185, 377-389 (2021)
   PUBMED   34147527
  REMARK    GeneRIF: PKCepsilon controls the fusion of secretory vesicles in
            mast cells in a phosphatidic acid-dependent mode.
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Naskar,P., Naqvi,N. and Puri,N.
  TITLE     Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23
            leads to massive inhibition in exocytosis from mast cells
  JOURNAL   J Biosci 43 (1), 127-138 (2018)
   PUBMED   29485121
  REMARK    GeneRIF: Blocking dephosphorylation at serine 120 residue in
            SNAP-23 leads to massive inhibition in exocytosis from mast cells.
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Weber,P., Batoulis,H., Rink,K.M., Dahlhoff,S., Pinkwart,K.,
            Sollner,T.H. and Lang,T.
  TITLE     Electrostatic anchoring precedes stable membrane attachment of
            SNAP25/SNAP23 to the plasma membrane
  JOURNAL   Elife 6, e19394 (2017)
   PUBMED   28240595
  REMARK    GeneRIF: Electrostatic anchoring precedes stable membrane
            attachment of SNAP25 and SNAP23 to the plasma membrane.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Rao,S.K., Huynh,C., Proux-Gillardeaux,V., Galli,T. and Andrews,N.W.
  TITLE     Identification of SNAREs involved in synaptotagmin VII-regulated
            lysosomal exocytosis
  JOURNAL   J Biol Chem 279 (19), 20471-20479 (2004)
   PUBMED   14993220
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Abonyo,B.O., Gou,D., Wang,P., Narasaraju,T., Wang,Z. and Liu,L.
  TITLE     Syntaxin 2 and SNAP-23 are required for regulated surfactant
            secretion
  JOURNAL   Biochemistry 43 (12), 3499-3506 (2004)
   PUBMED   15035620
  REMARK    GeneRIF: SNAP-23 is expressed in alveolar type II cells of the
            lung; evidence supports its functional role in exocytosis of lung
            surfactant by alveolar type II cells.
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Banerjee,A., Li,G., Alexander,E.A. and Schwartz,J.H.
  TITLE     Role of SNAP-23 in trafficking of H+-ATPase in cultured inner
            medullary collecting duct cells
  JOURNAL   Am J Physiol Cell Physiol 280 (4), C775-C781 (2001)
   PUBMED   11245593
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Okamoto,M., Schoch,S. and Sudhof,T.C.
  TITLE     EHSH1/intersectin, a protein that contains EH and SH3 domains and
            binds to dynamin and SNAP-25. A protein connection between
            exocytosis and endocytosis?
  JOURNAL   J Biol Chem 274 (26), 18446-18454 (1999)
   PUBMED   10373452
REFERENCE   10 (residues 1 to 221)
  AUTHORS   St-Denis,J.F., Cabaniols,J.P., Cushman,S.W. and Roche,P.A.
  TITLE     SNAP-23 participates in SNARE complex assembly in rat adipose cells
  JOURNAL   Biochem J 338 (Pt 3) (Pt 3), 709-715 (1999)
   PUBMED   10051443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 23, 2024 this sequence version replaced XP_038961739.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643296.11195.1,
                                           SRR26643289.10557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..221
                     /product="synaptosomal-associated protein 23 isoform 2"
                     /note="SNAP-23; vesicle-membrane fusion protein SNAP-23;
                     synaptosomal-associated protein, 23 kD;
                     synaptosomal-associated protein 23"
                     /calculated_mol_wt=24335
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          100..158
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          159..217
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(159,161..162,165..170,172..173,176..177,179..181,
                     183..184,187..188,190..191,193..198,200..201,204,207,211,
                     214,217)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            190
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..221
                     /gene="Snap23"
                     /coded_by="NM_001429469.1:149..814"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64630"
                     /db_xref="RGD:620221"
ORIGIN      
        1 mddlspeeiq lrahqvtdes lestrrilgl aiesqdagik titmldeqge qlnrieegmd
       61 qinkdmreae ktltelnkcc glcvcpcnrf svggcffetr tknfesgkny katwgdggds
      121 spsnvvskqp sritngqpqq ttgaasggyi kritndared emeenltqvg silgnlknma
      181 ldmgneidaq nqqiqkitek adtnknridi antrakklid s
//
LOCUS       NP_001100295             259 aa            linear   ROD 28-APR-2025
DEFINITION  meiotic recombination protein REC114 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001100295 XP_001072768 XP_217167
VERSION     NP_001100295.1
DBSOURCE    REFSEQ: accession NM_001106825.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001072768.1, XP_217167.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360186.2133808.1,
                                           SRR26643291.23207.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..259
                     /product="meiotic recombination protein REC114 isoform 2"
                     /note="meiotic recombination protein REC114"
                     /calculated_mol_wt=28166
     Region          20..254
                     /region_name="REC114-like"
                     /note="Meiotic recombination protein REC114-like;
                     pfam15165"
                     /db_xref="CDD:464541"
     CDS             1..259
                     /gene="Rec114"
                     /gene_synonym="RGD1311874"
                     /coded_by="NM_001106825.2:36..815"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:300751"
                     /db_xref="RGD:1311874"
ORIGIN      
        1 maeagnvasg lglpgevsqw plrrygrfml ldngespgps saaaaapspt wkvfessees
       61 gclvltivvs ghffisqgqt llegfsligs knwlkivrrm dcllfgttik dksrmfrvqf
      121 sgesqeeale hccgcvqtlt qyvtvqepdr itqelqqspg preagesqgk dplqqgssli
      181 leqhvcmaag tglleertsv thlaqsilap ekltlayegs swgaeelgpf lrlclmdqnf
      241 pafveeveke lkkitglrn
//
LOCUS       NP_001020803             655 aa            linear   ROD 28-APR-2025
DEFINITION  RNA-binding protein EWS isoform 2 [Rattus norvegicus].
ACCESSION   NP_001020803 XP_237930
VERSION     NP_001020803.2
DBSOURCE    REFSEQ: accession NM_001025632.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Parvanov,E.D., Tian,H., Billings,T., Saxl,R.L., Spruce,C.,
            Aithal,R., Krejci,L., Paigen,K. and Petkov,P.M.
  TITLE     PRDM9 interactions with other proteins provide a link between
            recombination hotspots and the chromosomal axis in meiosis
  JOURNAL   Mol Biol Cell 28 (3), 488-499 (2017)
   PUBMED   27932493
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Thomsen,C., Grundevik,P., Elias,P., Stahlberg,A. and Aman,P.
  TITLE     A conserved N-terminal motif is required for complex formation
            between FUS, EWSR1, TAF15 and their oncogenic fusion proteins
  JOURNAL   FASEB J 27 (12), 4965-4974 (2013)
   PUBMED   23975937
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Young,P.J., Francis,J.W., Lince,D., Coon,K., Androphy,E.J. and
            Lorson,C.L.
  TITLE     The Ewing's sarcoma protein interacts with the Tudor domain of the
            survival motor neuron protein
  JOURNAL   Brain Res Mol Brain Res 119 (1), 37-49 (2003)
   PUBMED   14597228
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Delattre,O., Zucman,J., Plougastel,B., Desmaze,C., Melot,T.,
            Peter,M., Kovar,H., Joubert,I., de Jong,P., Rouleau,G. et al.
  TITLE     Gene fusion with an ETS DNA-binding domain caused by chromosome
            translocation in human tumours
  JOURNAL   Nature 359 (6391), 162-165 (1992)
   PUBMED   1522903
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1.
            
            On Jun 3, 2008 this sequence version replaced NP_001020803.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC162004.1, SRR26360194.155858.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..655
                     /product="RNA-binding protein EWS isoform 2"
                     /note="RNA-binding protein EWS; Ewing sarcoma breakpoint
                     region 1; RNA-binding protein EWS-like"
                     /calculated_mol_wt=68200
     Region          360..443
                     /region_name="RRM_EWS"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     Ewing Sarcoma Protein (EWS); cd12533"
                     /db_xref="CDD:409950"
     Region          517..546
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          521..542
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275375"
     CDS             1..655
                     /gene="Ewsr1"
                     /coded_by="NM_001025632.3:47..2014"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:289752"
                     /db_xref="RGD:1307258"
ORIGIN      
        1 mastdystys qaaaqqgysa ytaqptqgya qttqaygqqs ygtygqptdv sytqaqstat
       61 ygqtayatsy gqpptgyttp tapqaysqpv qgygtgaydt ttatvtttqa syaaqsaygt
      121 qpaypaygqq paataptrpq dgnkpaetsq pqsstggynq pslgygqsny sypqvpgsyp
      181 mqpvtappsy pptsysssqp tsydqssysq qntygqpssy gqqssygqqs sygqqpptsy
      241 ppqtgsysqa psqysqqsss ygqqssfrqd hpssmgvygq esggfsgpge nrslsgpdnr
      301 grgrggfdrg gmsrggrggg rggmgagerg gfnkpggpmd egpdldlglp idpdedsdns
      361 avyvqglnds vtlddladff kqcgvvkmnk rtgqpmihiy ldketgkpkg datvsyedpp
      421 takaavewfd gkdfqgsklk vslarkkppl nsmrggmppr egrgmppplr ggpggpggpg
      481 gpmgrmggrg gdrggfpprg prgsrgnpsg ggnvqhragd wqcpnpgcgn qnfawrtecn
      541 qckapkpegf lpppfpppgg drgrggpggm rggrgglmdr ggpggmfrgg rggdrggfrg
      601 grgmdrggfg ggrrggpggp pgplmeqmgg rrggrggpgk mdkgehrqer rdrpy
//
LOCUS       NP_001420249             758 aa            linear   ROD 28-APR-2025
DEFINITION  POTE ankyrin domain family member M like 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001420249 XP_063132003
VERSION     NP_001420249.1
DBSOURCE    REFSEQ: accession NM_001433320.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Aug 9, 2024 this sequence version replaced XP_063132003.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360181.139071.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..758
                     /product="POTE ankyrin domain family member M like 2
                     isoform 1"
                     /note="chromatin structure-remodeling complex protein
                     SYD-like; POTE ankyrin domain family member M like 1;
                     ankyrin repeat domain-containing protein 36C-like;
                     mucin-5AC-like"
                     /calculated_mol_wt=81872
     Region          <50..223
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          50..78
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(80,82,86..87,90..92,94..95,99,102,111,113,115,
                     119..120,123..125,127..128,132,135,144,146,148,152..153,
                     156..158,160..161,165,168)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          80..111
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          113..144
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          146..176
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          179..209
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <342..524
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     CDS             1..758
                     /gene="Poteml2"
                     /gene_synonym="Poteml1"
                     /coded_by="NM_001433320.1:149..2425"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100911353"
                     /db_xref="RGD:6493549"
ORIGIN      
        1 mdedsmtfnf prrrrwytrl whscrrlgcl chqrsrqfhr yqigydpvgp lqraasvgdl
       61 vttesmiysr ehhvdeydrr grtslhyacv hnhpdvvtll leynsniniq ddegctplik
      121 avqcqntdcv yillrhnanp nltdfhgnta fhhaasrgni kivklllkyn vdfeaktkyg
      181 ltplqlatye nhtemikfle sksadaqavq vsssarrpah kkkvkhvrfn kevfvfnner
      241 plsrrvrspr qlksilktsi qhnseagmql tgrspwcvnv dnvsstssvk gesgrkihik
      301 pkksqnsfrk sgvyvssrva pilevweent satdektkme nfhsvpseaa advgpststa
      361 dsldaaepaq tkstkeaasl tavepeptks tiaadsltav epaqtkstia tdsltavepa
      421 ltkstkdaas ltaaepaptk stnaadslta vepvptkstn aadsltavep vptkstiaad
      481 sliaaepapt ksttaadslt avepmptkst taadsltave paptksttaa asltaaepap
      541 tksttaadgl tadepaptks ttaadgltad epelsltyaa dstvsgdsgp ashigldyvv
      601 dlplykestr ykphadpept pgsctcysld siqmtnltll isfseeeify tassdeessf
      661 ipdieeglpa tqapvdnfda sasaepinhs mnplrvggyl rapaiahipf lpfiwlvssl
      721 fsvitwmkiq iqhawheeng qgaptdkkvg svaaapdp
//
LOCUS       NP_001420837             997 aa            linear   ROD 28-APR-2025
DEFINITION  dynamin-like GTPase OPA1, mitochondrial isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001420837 XP_006248560
VERSION     NP_001420837.1
DBSOURCE    REFSEQ: accession NM_001433908.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 997)
  AUTHORS   Kaur,H., Carrillo,O., Garcia,I., Ramos,I., St Vallier,S., De La
            Torre,P., Lopez,A., Keniry,M., Bazan,D., Elizondo,J., Grishma,K.C.,
            Ann MacMillan-Crow,L. and Gilkerson,R.
  TITLE     Differentiation activates mitochondrial OPA1 processing in myoblast
            cell lines
  JOURNAL   Mitochondrion 78, 101933 (2024)
   PUBMED   38986925
  REMARK    GeneRIF: Differentiation activates mitochondrial OPA1 processing in
            myoblast cell lines.
REFERENCE   2  (residues 1 to 997)
  AUTHORS   Chen,W., DU,H., Sha,Y., Zhou,Y., Liang,J., Chen,Y., Ma,Q., Wu,X.
            and Qian,G.
  TITLE     [Long noncoding RNA H19 promotes vascular calcification by
            repressing the Bax inhibitor 1/optic atrophy 1 pathway]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 43 (9), 1469-1475 (2023)
   PUBMED   37814860
  REMARK    GeneRIF: [Long noncoding RNA H19 promotes vascular calcification by
            repressing the Bax inhibitor 1/optic atrophy 1 pathway].
REFERENCE   3  (residues 1 to 997)
  AUTHORS   Garcia,I., Calderon,F., la Torre,P., Vallier,S.S., Rodriguez,C.,
            Agarwala,D., Keniry,M., Innis-Whitehouse,W. and Gilkerson,R.
  TITLE     Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts
  JOURNAL   Mitochondrion 57, 88-96 (2021)
   PUBMED   33383158
  REMARK    GeneRIF: Mitochondrial OPA1 cleavage is reversibly activated by
            differentiation of H9c2 cardiomyoblasts.
REFERENCE   4  (residues 1 to 997)
  AUTHORS   Pang,Y., Qin,M., Hu,P., Ji,K., Xiao,R., Sun,N., Pan,X. and Zhang,X.
  TITLE     Resveratrol protects retinal ganglion cells against ischemia
            induced damage by increasing Opa1 expression
  JOURNAL   Int J Mol Med 46 (5), 1707-1720 (2020)
   PUBMED   32901846
  REMARK    GeneRIF: Resveratrol protects retinal ganglion cells against
            ischemia induced damage by increasing Opa1 expression.
REFERENCE   5  (residues 1 to 997)
  AUTHORS   Rodriguez-Graciani,K.M., Chapa-Dubocq,X.R., MacMillan-Crow,L.A. and
            Javadov,S.
  TITLE     Association Between L-OPA1 Cleavage and Cardiac Dysfunction During
            Ischemia-Reperfusion Injury in Rats
  JOURNAL   Cell Physiol Biochem 54 (6), 1101-1114 (2020)
   PUBMED   33119220
  REMARK    GeneRIF: Association Between L-OPA1 Cleavage and Cardiac
            Dysfunction During Ischemia-Reperfusion Injury in Rats.
REFERENCE   6  (residues 1 to 997)
  AUTHORS   Satoh,M., Hamamoto,T., Seo,N., Kagawa,Y. and Endo,H.
  TITLE     Differential sublocalization of the dynamin-related protein OPA1
            isoforms in mitochondria
  JOURNAL   Biochem Biophys Res Commun 300 (2), 482-493 (2003)
   PUBMED   12504110
REFERENCE   7  (residues 1 to 997)
  AUTHORS   Misaka,T., Miyashita,T. and Kubo,Y.
  TITLE     Primary structure of a dynamin-related mouse mitochondrial GTPase
            and its distribution in brain, subcellular localization, and effect
            on mitochondrial morphology
  JOURNAL   J Biol Chem 277 (18), 15834-15842 (2002)
   PUBMED   11847212
REFERENCE   8  (residues 1 to 997)
  AUTHORS   Aung,T., Ocaka,L., Ebenezer,N.D., Morris,A.G., Brice,G.,
            Child,A.H., Hitchings,R.A., Lehmann,O.J. and Bhattacharya,S.S.
  TITLE     Investigating the association between OPA1 polymorphisms and
            glaucoma: comparison between normal tension and high tension
            primary open angle glaucoma
  JOURNAL   Hum Genet 110 (5), 513-514 (2002)
   PUBMED   12073024
REFERENCE   9  (residues 1 to 997)
  AUTHORS   Aung,T., Ocaka,L., Ebenezer,N.D., Morris,A.G., Krawczak,M.,
            Thiselton,D.L., Alexander,C., Votruba,M., Brice,G., Child,A.H.,
            Francis,P.J., Hitchings,R.A., Lehmann,O.J. and Bhattacharya,S.S.
  TITLE     A major marker for normal tension glaucoma: association with
            polymorphisms in the OPA1 gene
  JOURNAL   Hum Genet 110 (1), 52-56 (2002)
   PUBMED   11810296
REFERENCE   10 (residues 1 to 997)
  AUTHORS   Alexander,C., Votruba,M., Pesch,U.E., Thiselton,D.L., Mayer,S.,
            Moore,A., Rodriguez,M., Kellner,U., Leo-Kottler,B., Auburger,G.,
            Bhattacharya,S.S. and Wissinger,B.
  TITLE     OPA1, encoding a dynamin-related GTPase, is mutated in autosomal
            dominant optic atrophy linked to chromosome 3q28
  JOURNAL   Nat Genet 26 (2), 211-215 (2000)
   PUBMED   11017080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000011.1.
            
            On Oct 10, 2024 this sequence version replaced XP_006248560.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643292.46107.1,
                                           SRR26643299.48621.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..997
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..997
                     /product="dynamin-like GTPase OPA1, mitochondrial isoform
                     2"
                     /EC_number="3.6.5.5"
                     /note="optic atrophy 1 (autosomal dominant); dynamin-like
                     120 kDa protein, mitochondrial; optic atrophy 1-like
                     protein; optic atrophy 1 homolog; mitochondrial OPA1;
                     optic atrophy protein 1 homolog; RN protein; dynamin-like
                     GTPase OPA1, mitochondrial"
                     /calculated_mol_wt=115430
     Region          324..598
                     /region_name="DLP_1"
                     /note="Dynamin_like protein family includes dynamins and
                     Mx proteins; cd08771"
                     /db_xref="CDD:206738"
     Site            332..339
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(333,335..340,353..354,360,435,505,507..508,539..543)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(334..335,439,452,477,479,481..484,486..487,508,
                     510..513,542..543)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Site            360
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            364..366
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            435..438
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(437..438,468..469)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Site            504..507
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Site            539..541
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Region          654..997
                     /region_name="OPA1_C"
                     /note="Dynamin-like GTPase OPA1 C-terminal; pfam19434"
                     /db_xref="CDD:466080"
     CDS             1..997
                     /gene="Opa1"
                     /coded_by="NM_001433908.1:148..3141"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:171116"
                     /db_xref="RGD:708423"
ORIGIN      
        1 mwragraala cevcqslvkh ssgvqrnvpl qklhlvsrsi yrshhpalkl qrpqlrtsfq
       61 qfssltnlsl hklklsptky gyqprrnfwp arlaarllkl ryiilgsavg ggytakktfd
      121 ewkdmipdls dykwivpdfi weideyidle kirkalpsse dlanfapdld kiaeslsllk
      181 dfftagtpge tafratdhgs esdkhyrkgl lgelillqqq iqeheeearr aagqystsya
      241 qqkrkvsdke kidqlqeell htqlkyqril erlekenkel rklvlqkddk gihhrklkks
      301 lidmysevld vlsdydasyn tqdhlprvvv vgdqsagkts vlemiaqari fprgsgemmt
      361 rspvkvtlse gphhvalfkd ssrefdltke edlaalrhei elrmrknvke gctvspetis
      421 lnvkgpglqr mvlvdlpgvi ntvtsgmapd tketifsisk aymqnpnaii lciqdgsvda
      481 ersivtdlvs qmdphgrrti fvltkvdlae knvaspsriq qiiegklfpm kalgyfavvt
      541 gkgnssesie aireyeeeff qnskllktsm lkahqvttrn lslavsdcfw kmvresveqq
      601 adsfkatrfn letewknnyp rlreldrnel fekakneild evislsqvtp khweeilqqs
      661 lwervsthvi eniylpaaqt mnsgtfnttv diklkqwtdk qlpnkaveva wetlqdefsr
      721 fmtepkgkeh ddifdklkea vkeesikrhk wndfaedslr viqhnaledr sisdkqqwda
      781 aiyfmeealq grlkdtenai enmigpdwkk rwiywknrtq eqcvhnetkn elekmlkvnd
      841 ehpaylasde ittvrknles rgvevdpsli kdtwhqvyrr hflktalnhc nlcrrgfyyy
      901 qrhfidsele cndvvlfwri qrmlaitant lrqqltntev rrleknvkev ledfaedgek
      961 kvklltgkrv qlaedlkkvr eiqekldafi ealhqek
//
LOCUS       NP_001386462             415 aa            linear   ROD 28-APR-2025
DEFINITION  nucleolar and spindle-associated protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001386462 XP_006234831
VERSION     NP_001386462.1
DBSOURCE    REFSEQ: accession NM_001399533.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Raemaekers,T., Ribbeck,K., Beaudouin,J., Annaert,W., Van Camp,M.,
            Stockmans,I., Smets,N., Bouillon,R., Ellenberg,J. and Carmeliet,G.
  TITLE     NuSAP, a novel microtubule-associated protein involved in mitotic
            spindle organization
  JOURNAL   J Cell Biol 162 (6), 1017-1029 (2003)
   PUBMED   12963707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Jan 10, 2022 this sequence version replaced XP_006234831.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643297.12551.1,
                                           SRR26643292.13957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..415
                     /product="nucleolar and spindle-associated protein 1
                     isoform 2"
                     /calculated_mol_wt=47154
     Region          157..409
                     /region_name="NUSAP"
                     /note="Nucleolar and spindle-associated protein;
                     pfam16006"
                     /db_xref="CDD:464970"
     CDS             1..415
                     /gene="Nusap1"
                     /coded_by="NM_001399533.1:75..1322"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:311336"
                     /db_xref="RGD:1305764"
ORIGIN      
        1 mtvpsaeeld sfkysdlqnl akrlglranl radkllralk ahlnpetrre nknqdenqss
       61 afsydetetq vtseeqaete sgshvtrtrr rkrktihgip tsqdhmemkr rdsttfqnqe
      121 nqdlratekv pslpeqrped gnaasseegk indkkgplek rslctdgfsk lgnskrisat
      181 tpnfkrlhea hfkkmeside ymvrkkkhfk ehdslnelkl dkkvtpvppr grlsvlctpa
      241 rqrcsqghsa tkmnvrfsaa tkdnehkcsl tktparksph vtapgsaskg qavlktpklk
      301 tternstavi tpfklmteat qtpgsskkpi fdlkaslsrp lnykphkgkl kpwgqakenn
      361 slnecvsrvt lhrktykqpp lqtreeqrkr hvqerkerke kllearrnlg vtkaq
//
LOCUS       NP_001102275             190 aa            linear   ROD 28-APR-2025
DEFINITION  spermatogenesis-associated protein 3 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001102275 XP_001063654 XP_006245473 XP_343613
VERSION     NP_001102275.1
DBSOURCE    REFSEQ: accession NM_001108805.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On or before Jul 31, 2024 this sequence version replaced
            XP_006245473.1, XP_001063654.1, XP_343613.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.51696.1,
                                           SRR26360181.3362305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..190
                     /product="spermatogenesis-associated protein 3 isoform 1"
                     /note="spermatogenesis-associated protein 3"
                     /calculated_mol_wt=20750
     Region          9..189
                     /region_name="SPATA3"
                     /note="Spermatogenesis-associated protein 3 family;
                     pfam15662"
                     /db_xref="CDD:434837"
     CDS             1..190
                     /gene="Spata3"
                     /coded_by="NM_001108805.2:106..678"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:363270"
                     /db_xref="RGD:1308164"
ORIGIN      
        1 mkkvkkkksd srrrrnsisp qtssdcshrp ssetqrscpd pcsppqtqsl qesipphqis
       61 pepklqqpss qpllpseerv sspclvstep kppcrkaavp ltyaaprscs cvvcpgssac
      121 wrrlglchsr ifdvllprdw ssmpgrgfpn lltfyrkpsr kyctsrnsra ssprncccgs
      181 ggpgscllhg
//
LOCUS       NP_037222                118 aa            linear   ROD 28-APR-2025
DEFINITION  vesicle-associated membrane protein 1 [Rattus norvegicus].
ACCESSION   NP_037222
VERSION     NP_037222.2
DBSOURCE    REFSEQ: accession NM_013090.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Rodepeter,F.R., Wiegand,S., Luers,H.G., Bonaterra,G.A., Lowe,A.W.,
            Bette,M., Jacob,R. and Mandic,R.
  TITLE     Indication for differential sorting of the rat v-SNARE splice
            isoforms VAMP-1a and -1b
  JOURNAL   Biochem Cell Biol 95 (4), 500-509 (2017)
   PUBMED   28314111
  REMARK    GeneRIF: differential sorting of the rat v-SNARE splice isoforms
            VAMP-1a and -1b
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Sitarska,E., Xu,J., Park,S., Liu,X., Quade,B., Stepien,K.,
            Sugita,K., Brautigam,C.A., Sugita,S. and Rizo,J.
  TITLE     Autoinhibition of Munc18-1 modulates synaptobrevin binding and
            helps to enable Munc13-dependent regulation of membrane fusion
  JOURNAL   Elife 6, e24278 (2017)
   PUBMED   28477408
  REMARK    GeneRIF: Together with previous studies, these data support a model
            whereby Munc18-1 acts as a template for SNARE complex assembly, and
            autoinhibition of synaptobrevin binding contributes to enabling
            regulation of neurotransmitter release by Munc13-1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Gu,Y. and Huganir,R.L.
  TITLE     Identification of the SNARE complex mediating the exocytosis of
            NMDA receptors
  JOURNAL   Proc Natl Acad Sci U S A 113 (43), 12280-12285 (2016)
   PUBMED   27791016
  REMARK    GeneRIF: Our study uncovers the postsynaptic function of the
            SNAP25-VAMP1-syntaxin4 complex in mediating the constitutive
            exocytosis of NMDA receptors, suggesting that this SNARE complex is
            involved in excitatory synaptic transmission
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Meng,J., Wang,J., Steinhoff,M. and Dolly,J.O.
  TITLE     TNFalpha induces co-trafficking of TRPV1/TRPA1 in VAMP1-containing
            vesicles to the plasmalemma via Munc18-1/syntaxin1/SNAP-25 mediated
            fusion
  JOURNAL   Sci Rep 6, 21226 (2016)
   PUBMED   26888187
  REMARK    GeneRIF: TNFalpha induces co-trafficking of TRPV1/TRPA1 in
            VAMP1-containing vesicles to the plasmalemma via
            Munc18-1/syntaxin1/SNAP-25 mediated fusion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Peng,L., Adler,M., Demogines,A., Borrell,A., Liu,H., Tao,L.,
            Tepp,W.H., Zhang,S.C., Johnson,E.A., Sawyer,S.L. and Dong,M.
  TITLE     Widespread sequence variations in VAMP1 across vertebrates suggest
            a potential selective pressure from botulinum neurotoxins
  JOURNAL   PLoS Pathog 10 (7), e1004177 (2014)
   PUBMED   25010769
  REMARK    GeneRIF: residue 48 of VAMP1 varies frequently between M and I
            across seventeen closely related primate species, suggesting a
            potential selective pressure from members of BoNTs for resistance
            in vertebrates.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Nabokina,S.M.
  TITLE     Intracellular localization of VAMP-1 protein in human neutrophils
  JOURNAL   Bull Exp Biol Med 131 (2), 130-131 (2001)
   PUBMED   11391393
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Martincic,I., Peralta,M.E. and Ngsee,J.K.
  TITLE     Isolation and characterization of a dual prenylated Rab and VAMP2
            receptor
  JOURNAL   J Biol Chem 272 (43), 26991-26998 (1997)
   PUBMED   9341137
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Mandic,R., Trimble,W.S. and Lowe,A.W.
  TITLE     Tissue-specific alternative RNA splicing of rat vesicle-associated
            membrane protein-1 (VAMP-1)
  JOURNAL   Gene 199 (1-2), 173-179 (1997)
   PUBMED   9358054
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Elferink,L.A., Trimble,W.S. and Scheller,R.H.
  TITLE     Two vesicle-associated membrane protein genes are differentially
            expressed in the rat central nervous system
  JOURNAL   J Biol Chem 264 (19), 11061-11064 (1989)
   PUBMED   2472388
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Trimble,W.S., Cowan,D.M. and Scheller,R.H.
  TITLE     VAMP-1: a synaptic vesicle-associated integral membrane protein
  JOURNAL   Proc Natl Acad Sci U S A 85 (12), 4538-4542 (1988)
   PUBMED   3380805
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB582258.1, CO567426.1, BC092206.1 and AI059682.1.
            
            On Sep 28, 2005 this sequence version replaced NP_037222.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM030153.1, BC092206.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..118
                     /product="vesicle-associated membrane protein 1"
                     /note="VAMP-1; synaptobrevin-1"
                     /calculated_mol_wt=12666
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63666.2)"
     Region          32..94
                     /region_name="R-SNARE_VAMP2"
                     /note="SNARE motif of VAMP2; cd15870"
                     /db_xref="CDD:277223"
     Site            order(33..35,37..38,40..45,47..49,51,54..55,57..59,61..66,
                     68..73,75..80,82..87,89..91,94)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277223"
     Site            58
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277223"
     Site            60..61
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type F (BoNT/F, botF).
                     /evidence=ECO:0000269|PubMed:1331807,
                     ECO:0000269|PubMed:8505288; propagated from
                     UniProtKB/Swiss-Prot (Q63666.2)"
     Site            61..62
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type D (BoNT/D, botD).
                     /evidence=ECO:0000269|PubMed:8175689; propagated from
                     UniProtKB/Swiss-Prot (Q63666.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62442; propagated from
                     UniProtKB/Swiss-Prot (Q63666.2)"
     Site            97..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63666.2)"
     CDS             1..118
                     /gene="Vamp1"
                     /gene_synonym="Syb1"
                     /coded_by="NM_013090.2:135..491"
                     /db_xref="GeneID:25624"
                     /db_xref="RGD:3948"
ORIGIN      
        1 msapaqppae gtegaapggg ppgpppntts nrrlqqtqaq veevvdimrv nvdkvlerdq
       61 klselddrad alqagasvfe ssaaklkrky wwknckmmim lgaicaiivv viviyift
//
LOCUS       NP_113915                647 aa            linear   ROD 28-APR-2025
DEFINITION  LIM domain kinase 1 [Rattus norvegicus].
ACCESSION   NP_113915 XP_346434 XP_347353
VERSION     NP_113915.2
DBSOURCE    REFSEQ: accession NM_031727.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Chen,Y., Song,D., Gao,J., Zhang,X. and Chen,X.
  TITLE     Circ-Zfp644 acts as a pro-hypertrophic mediator in an Ang-II
            induced in vitro myocardial hypertrophy model
  JOURNAL   Cell Biol Int 45 (6), 1260-1268 (2021)
   PUBMED   33559936
  REMARK    GeneRIF: Circ-Zfp644 acts as a pro-hypertrophic mediator in an
            Ang-II induced in vitro myocardial hypertrophy model.
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Chen,B., Lin,W., Qi,W., Li,S., Hong,Z. and Zhao,H.
  TITLE     Cofilin Inhibition by Limk1 Reduces Rod Formation and Cell
            Apoptosis after Ischemic Stroke
  JOURNAL   Neuroscience 444, 64-75 (2020)
   PUBMED   32697981
  REMARK    GeneRIF: Cofilin Inhibition by Limk1 Reduces Rod Formation and Cell
            Apoptosis after Ischemic Stroke.
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Liu,W., Wu,J., Huang,J., Zhuo,P., Lin,Y., Wang,L., Lin,R., Chen,L.
            and Tao,J.
  TITLE     Electroacupuncture Regulates Hippocampal Synaptic Plasticity via
            miR-134-Mediated LIMK1 Function in Rats with Ischemic Stroke
  JOURNAL   Neural Plast 2017, 9545646 (2017)
   PUBMED   28116173
  REMARK    GeneRIF: MiR-134-mediated LIM domain kinase was involved in
            Regulates Hippocampal Synaptic Plasticity via miR-134-mediated
            LIMK1 function in rats with ischemic stroke induced hippocampal
            synaptic plasticity, which served as a contributor to improving
            learning and memory during the recovery stage of ischemic stroke.
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Yu,Y., Zhang,P., Yan,J., Sun,Y., Wu,X., Xi,S., Zhang,L., Sun,Y.,
            Hu,R. and Jiang,H.
  TITLE     Sevoflurane induces cognitive impairments via the
            MiR-27b/LIMK1-signaling pathway in developing rats
  JOURNAL   Inhal Toxicol 28 (14), 731-738 (2016)
   PUBMED   27973945
  REMARK    GeneRIF: We demonstrated that LIMK1, as one target of miR-27b,
            might mediate sevoflurane-induced synapse deficits in the
            hippocampus. These results emphasize the potential role of LIMK1 in
            cognitive dysfunction in rats.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   George,J., Soares,C., Montersino,A., Beique,J.C. and Thomas,G.M.
  TITLE     Palmitoylation of LIM Kinase-1 ensures spine-specific actin
            polymerization and morphological plasticity
  JOURNAL   Elife 4, e06327 (2015)
   PUBMED   25884247
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Rosso,S., Bollati,F., Bisbal,M., Peretti,D., Sumi,T., Nakamura,T.,
            Quiroga,S., Ferreira,A. and Caceres,A.
  TITLE     LIMK1 regulates Golgi dynamics, traffic of Golgi-derived vesicles,
            and process extension in primary cultured neurons
  JOURNAL   Mol Biol Cell 15 (7), 3433-3449 (2004)
   PUBMED   15090620
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Foletta,V.C., Moussi,N., Sarmiere,P.D., Bamburg,J.R. and Bernard,O.
  TITLE     LIM kinase 1, a key regulator of actin dynamics, is widely
            expressed in embryonic and adult tissues
  JOURNAL   Exp Cell Res 294 (2), 392-405 (2004)
   PUBMED   15023529
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Yang,E., Kim,H., Lee,J., Shin,J.S., Yoon,H., Kim,S.J. and Choi,I.H.
  TITLE     Overexpression of LIM kinase 1 renders resistance to apoptosis in
            PC12 cells by inhibition of caspase activation
  JOURNAL   Cell Mol Neurobiol 24 (2), 181-192 (2004)
   PUBMED   15176434
  REMARK    GeneRIF: PC12 cells overexpressing the wild-type LIMK1 were more
            resistant to cell death and the level of caspase 3 activation in
            these cells was lower than in the control PC12 cells or than in the
            PC12 cells expressing a mutant LIMK1 lacking the kinase domain.
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Geneste,O., Copeland,J.W. and Treisman,R.
  TITLE     LIM kinase and Diaphanous cooperate to regulate serum response
            factor and actin dynamics
  JOURNAL   J Cell Biol 157 (5), 831-838 (2002)
   PUBMED   12034774
  REMARK    GeneRIF: LIM kinase and Diaphanous cooperate to regulate serum
            response factor and actin dynamics.
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Nunoue,K., Ohashi,K., Okano,I. and Mizuno,K.
  TITLE     LIMK-1 and LIMK-2, two members of a LIM motif-containing protein
            kinase family
  JOURNAL   Oncogene 11 (4), 701-710 (1995)
   PUBMED   7651734
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB726578.1, BF565872.1, CB702103.1, AW529884.1, CB691076.1,
            AC091000.2 and CV112377.1.
            
            On Oct 12, 2007 this sequence version replaced NP_113915.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..647
                     /product="LIM domain kinase 1"
                     /EC_number="2.7.11.1"
                     /note="LIM-domain containing, protein kinase 1; LIMK-1;
                     LIM motif-containing protein kinase 1"
                     /calculated_mol_wt=72477
     Region          5..77
                     /region_name="LIM1_LIMK1"
                     /note="The first LIM domain of LIMK1 (LIM domain Kinase
                     1); cd09462"
                     /db_xref="CDD:188846"
     Site            order(25,28,46,49,52,55,72,75)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188846"
     Region          84..138
                     /region_name="LIM2_LIMK1"
                     /note="The second LIM domain of LIMK1 (LIM domain Kinase
                     1); cd09464"
                     /db_xref="CDD:188848"
     Site            order(84,87,105,108,111,114,134,137)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188848"
     Region          160..258
                     /region_name="PDZ_LIMK-like"
                     /note="PDZ domain of LIM Kinase (LIMK) family, and related
                     domains; cd06754"
                     /db_xref="CDD:467236"
     Site            order(175..181,202,205,236,240,243..244)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467236"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Region          256..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53669.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     Region          345..611
                     /region_name="STKc_LIMK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     LIM domain kinase 1; cd14221"
                     /db_xref="CDD:271123"
     Site            order(345..349,353,366,368,384,397,413..416,419..420,422,
                     460,462,464..465,467,478,481,511..514)
                     /site_type="active"
                     /db_xref="CDD:271123"
     Site            order(345..349,353,366,368,384,397,413..416,419..420,460,
                     462,464..465,467,478)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271123"
     Site            order(349,420,422,460,462,464,481,511..514)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271123"
     Site            order(477..489,497..514)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271123"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK1 and PAK1.
                     /evidence=ECO:0000250|UniProtKB:P53667; propagated from
                     UniProtKB/Swiss-Prot (P53669.1)"
     CDS             1..647
                     /gene="Limk1"
                     /coded_by="NM_031727.2:184..2127"
                     /db_xref="GeneID:65172"
                     /db_xref="RGD:62055"
ORIGIN      
        1 mrltllcctw reermgeegs elpvcascsq siydgqylqa lnadwhadcf rccecstsls
       61 hqyyekdgql fckkdywary geschgcseh itkglvmvag elkyhpecfi clacgnfigd
      121 gdtytlvehs klycgqcyyq tvvtpvieqi lpdspgshlp htvtlvsipa sahgkrglsv
      181 sidpphgppg cgtehshtvr vqgvdpgcms pdvknsihig drileingtp irnvpldeid
      241 lliqetsrll qltlehdphd slghgpvsdp splaspvhtp sgqagssarq kpvlrscsid
      301 tspgagslvs pasqrkdlgr seslrvvcrp hrifrpsdli hgevlgkgcf gqaikvthre
      361 tgevmvmkel irfdeetqrt flkevkvmrc lehpnvlkfi gvlykdkrln fiteyikggt
      421 lrgiiksmds qypwsqrvsf akdiasgmay lhsmniihrd lnshnclvre nrnvvvadfg
      481 larlmidekg qsedlrslkk pdrkkrytvv gnpywmapem ingrsydekv dvfsfgivlc
      541 eiigrvnadp dylprtmdfg lnvrgfldry cppncppsff pitvrccdld pekrpsfvkl
      601 eqwletlrmh laghlplgpq leqlergfwe tyrrgesslp ahpevpd
//
LOCUS       NP_001008948             314 aa            linear   ROD 28-APR-2025
DEFINITION  vomeronasal type-1 receptor 98 [Rattus norvegicus].
ACCESSION   NP_001008948 XP_038964663
VERSION     NP_001008948.1
DBSOURCE    REFSEQ: accession NM_001008948.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Young,J.M., Massa,H.F., Hsu,L. and Trask,B.J.
  TITLE     Extreme variability among mammalian V1R gene families
  JOURNAL   Genome Res 20 (1), 10-18 (2010)
   PUBMED   19952141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000004.1.
            
            On Jun 27, 2022 this sequence version replaced XP_038964663.1.
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on single protein-coding
                                         transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..314
                     /product="vomeronasal type-1 receptor 98"
                     /note="vomeronasal type-1 receptor A8; vomeronasal
                     V1r-type receptor V1ra8; vomernasal 1 receptor Vom1r98;
                     vomeronasal 1 receptor, A8"
                     /calculated_mol_wt=35762
     Region          12..304
                     /region_name="7tm_V1R_pheromone"
                     /note="vomeronasal organ pheromone receptor type-1 family,
                     member of the seven-transmembrane G protein-coupled
                     receptor superfamily; cd13949"
                     /db_xref="CDD:320087"
     Region          12..37
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320087"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          49..71
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320087"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          85..107
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320087"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          133..149
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320087"
     Site            134..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          184..207
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320087"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          233..258
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320087"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     Region          268..293
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320087"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5J3E5.1)"
     CDS             1..314
                     /gene="Vom1r98"
                     /gene_synonym="V1ra8"
                     /coded_by="NM_001008948.1:1..945"
                     /db_xref="GeneID:494294"
                     /db_xref="RGD:1549694"
ORIGIN      
        1 mnkdttmycs ayirdvffce igvgisansc lllfhifmfi rghrprltdl piglmalihl
       61 lmlllaayia kdffmssgwd ditcklfifl hrffrslsvc atcmlsvfqt iilcpqsshl
      121 akfkpnspyh lscffifmsi fytsisshil iaaiatqnlt svnliyitks csflpmsssm
      181 qrtfstllaf rnafliglmg lstcymatll crhktrsqrl qnsklspkat peqraiwtll
      241 mfmsfflvms tfdsiisysr tifqgnpsly caqilvahsy avvspmlvls nenrltnpli
      301 smyerivrld flcw
//
LOCUS       NP_001007602             104 aa            linear   ROD 28-APR-2025
DEFINITION  pterin-4-alpha-carbinolamine dehydratase [Rattus norvegicus].
ACCESSION   NP_001007602 XP_342136
VERSION     NP_001007602.1
DBSOURCE    REFSEQ: accession NM_001007601.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Rho,H., Jones,C.N. and Rose,R.B.
  TITLE     Kinetic stability may determine the interaction dynamics of the
            bifunctional protein DCoH1, the dimerization cofactor of the
            transcription factor HNF-1alpha
  JOURNAL   Biochemistry 49 (47), 10187-10197 (2010)
   PUBMED   21047120
  REMARK    GeneRIF: a point mutation at the DCoH1 tetramer interface, Thr 51
            Ser, overcomes the dissociation barrier of the homotetramer and
            increases the interaction with HNF-1alpha.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Rose,R.B., Pullen,K.E., Bayle,J.H., Crabtree,G.R. and Alber,T.
  TITLE     Biochemical and structural basis for partially redundant enzymatic
            and transcriptional functions of DCoH and DCoH2
  JOURNAL   Biochemistry 43 (23), 7345-7355 (2004)
   PUBMED   15182178
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Bossow,S., Riepl,S. and Igo-Kemenes,T.
  TITLE     Characterization of the chicken and rat DCoH gene domains using an
            improved ligation-mediated PCR method
  JOURNAL   Biol Chem 379 (11), 1359-1365 (1998)
   PUBMED   9865610
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Johnen,G., Kowlessur,D., Citron,B.A. and Kaufman,S.
  TITLE     Characterization of the wild-type form of 4a-carbinolamine
            dehydratase and two naturally occurring mutants associated with
            hyperphenylalaninemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (26), 12384-12388 (1995)
   PUBMED   8618906
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1996 Apr 30;93(9):4519]
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Ficner,R., Sauer,U.H., Stier,G. and Suck,D.
  TITLE     Three-dimensional structure of the bifunctional protein PCD/DCoH, a
            cytoplasmic enzyme interacting with transcription factor HNF1
  JOURNAL   EMBO J 14 (9), 2034-2042 (1995)
   PUBMED   7744010
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Hauer,C.R., Rebrin,I., Thony,B., Neuheiser,F., Curtius,H.C.,
            Hunziker,P., Blau,N., Ghisla,S. and Heizmann,C.W.
  TITLE     Phenylalanine hydroxylase-stimulating protein/pterin-4
            alpha-carbinolamine dehydratase from rat and human liver.
            Purification, characterization, and complete amino acid sequence
  JOURNAL   J Biol Chem 268 (7), 4828-4831 (1993)
   PUBMED   8444860
REFERENCE   9  (residues 1 to 104)
  AUTHORS   Citron,B.A., Davis,M.D., Milstien,S., Gutierrez,J., Mendel,D.B.,
            Crabtree,G.R. and Kaufman,S.
  TITLE     Identity of 4a-carbinolamine dehydratase, a component of the
            phenylalanine hydroxylation system, and DCoH, a transregulator of
            homeodomain proteins
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 11891-11894 (1992)
   PUBMED   1465414
  REMARK    GeneRIF: Rat Pcbd1 is a moonlighting protein that has dehydratase
            activity in addition to functioning as a cofactor which regulates
            HNF1alpha.
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Mendel,D.B., Khavari,P.A., Conley,P.B., Graves,M.K., Hansen,L.P.,
            Admon,A. and Crabtree,G.R.
  TITLE     Characterization of a cofactor that regulates dimerization of a
            mammalian homeodomain protein
  JOURNAL   Science 254 (5039), 1762-1767 (1991)
   PUBMED   1763325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM060466.1, FM067129.1 and DV724713.1.
            
            On Nov 29, 2004 this sequence version replaced XP_342136.1.
            
            Summary: This gene encodes a member of the
            pterin-4-alpha-carbinolamine dehydratase family. The encoded
            protein has been identified as a moonlighting protein based on its
            ability to perform mechanistically distinct functions. The encoded
            protein functions as both a dehydratase involved in
            tetrahydrobiopterin biosynthesis, and as a cofactor for
            HNF1A-dependent transcription. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM060466.1, FM067129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 1465414
            RefSeq Select criteria          :: based on conservation,
                                               expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..104
                     /product="pterin-4-alpha-carbinolamine dehydratase"
                     /EC_number="4.2.1.96"
                     /note="dimerization cofactor of HNF1; pterin carbinolamine
                     dehydratase; 4-alpha-hydroxy-tetrahydropterin dehydratase;
                     phenylalanine hydroxylase-stimulating protein;
                     6-pyruvoyl-tetrahydropterin synthase/dimerization cofactor
                     of hepatocyte nuclear factor 1 alpha (TCF1); pterin-4
                     alpha-carbinolamine dehydratase/dimerization cofactor of
                     hepatocyte nuclear factor 1 alpha"
                     /calculated_mol_wt=11868
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:8444860; propagated from
                     UniProtKB/Swiss-Prot (P61459.2)"
     Region          24..99
                     /region_name="PCD_DCoH_subfamily_b"
                     /note="PCD_DCoH: The bifunctional protein
                     pterin-4alpha-carbinolamine dehydratase (PCD), also known
                     as DCoH (dimerization cofactor of hepatocyte nuclear
                     factor-1), is both a transcription activator and a
                     metabolic enzyme. DCoH stimulates gene expression by...;
                     cd00914"
                     /db_xref="CDD:238456"
     Site            order(43,47,63,66,80)
                     /site_type="other"
                     /note="aromatic arch"
                     /db_xref="CDD:238456"
     Site            order(43,58,63..70)
                     /site_type="other"
                     /note="DCoH dimer interaction site [polypeptide binding]"
                     /db_xref="CDD:238456"
     Site            order(44..45,51..52,55,58..59)
                     /site_type="other"
                     /note="DCoH /HNF-1 dimer interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:238456"
     Site            order(44,51..52,55,59)
                     /site_type="other"
                     /note="DCoH tetramer interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:238456"
     Site            order(61..63,78,80..81)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238456"
     CDS             1..104
                     /gene="Pcbd1"
                     /gene_synonym="DCoH; Pcbd; Pcd; Phs; TCF1"
                     /coded_by="NM_001007601.2:39..353"
                     /db_xref="GeneID:29700"
                     /db_xref="RGD:3263"
ORIGIN      
        1 magkahrlsa eerdqllpnl ravgwneleg rdaifkqfhf kdfnrafgfm trvalqaekl
       61 dhhpewfnvy nkvhitlsth ecaglserdi nlasfieqva vsmt
//
LOCUS       NP_001274039             146 aa            linear   ROD 28-APR-2025
DEFINITION  vascular endothelial growth factor A isoform 8 precursor [Rattus
            norvegicus].
ACCESSION   NP_001274039
VERSION     NP_001274039.1
DBSOURCE    REFSEQ: accession NM_001287110.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Fu,W., Ye,Y. and Hu,F.
  TITLE     LncRNA XIST promotes neovascularization in diabetic retinopathy by
            regulating miR-101-3p/VEGFA
  JOURNAL   Arch Endocrinol Metab 68, e230097 (2024)
   PUBMED   38739522
  REMARK    GeneRIF: LncRNA XIST promotes neovascularization in diabetic
            retinopathy by regulating miR-101-3p/VEGFA.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Li,Z., Xie,L., Zou,L., Xiao,S. and Tao,J.
  TITLE     Overexpression of RAD54L attenuates osteoarthritis by suppressing
            the HIF-1alpha/VEGF signaling pathway: Bioinformatics analysis and
            experimental validation
  JOURNAL   PLoS One 19 (4), e0298575 (2024)
   PUBMED   38593124
  REMARK    GeneRIF: Overexpression of RAD54L attenuates osteoarthritis by
            suppressing the HIF-1alpha/VEGF signaling pathway: Bioinformatics
            analysis and experimental validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Bastide,A., Karaa,Z., Bornes,S., Hieblot,C., Lacazette,E., Prats,H.
            and Touriol,C.
  TITLE     An upstream open reading frame within an IRES controls expression
            of a specific VEGF-A isoform
  JOURNAL   Nucleic Acids Res 36 (7), 2434-2445 (2008)
   PUBMED   18304943
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Meiron,M., Anunu,R., Scheinman,E.J., Hashmueli,S. and Levi,B.Z.
  TITLE     New isoforms of VEGF are translated from alternative initiation CUG
            codons located in its 5'UTR
  JOURNAL   Biochem Biophys Res Commun 282 (4), 1053-1060 (2001)
   PUBMED   11352659
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Terman,B.I., Dougher-Vermazen,M., Carrion,M.E., Dimitrov,D.,
            Armellino,D.C., Gospodarowicz,D. and Bohlen,P.
  TITLE     Identification of the KDR tyrosine kinase as a receptor for
            vascular endothelial cell growth factor
  JOURNAL   Biochem Biophys Res Commun 187 (3), 1579-1586 (1992)
   PUBMED   1417831
REFERENCE   9  (residues 1 to 146)
  AUTHORS   de Vries,C., Escobedo,J.A., Ueno,H., Houck,K., Ferrara,N. and
            Williams,L.T.
  TITLE     The fms-like tyrosine kinase, a receptor for vascular endothelial
            growth factor
  JOURNAL   Science 255 (5047), 989-991 (1992)
   PUBMED   1312256
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Breier,G., Albrecht,U., Sterrer,S. and Risau,W.
  TITLE     Expression of vascular endothelial growth factor during embryonic
            angiogenesis and endothelial cell differentiation
  JOURNAL   Development 114 (2), 521-532 (1992)
   PUBMED   1592003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO565920.1, BC168708.1,
            AF215726.1 and JAXUCZ010000009.1.
            
            Summary: This gene is a member of the PDGF/VEGF growth factor
            family. It encodes a heparin-binding protein, which exists as a
            disulfide-linked homodimer. This growth factor induces
            proliferation and migration of vascular endothelial cells, and is
            essential for both physiological and pathological angiogenesis.
            Disruption of this gene in mice resulted in abnormal embryonic
            blood vessel formation. This gene is upregulated in many known
            tumors and its expression is correlated with tumor stage and
            progression. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. There is also
            evidence for alternative translation initiation from upstream
            non-AUG (CUG) codons resulting in additional isoforms. A recent
            study showed that a C-terminally extended isoform is produced by
            use of an alternative in-frame translation termination codon via a
            stop codon readthrough mechanism, and that this isoform is
            antiangiogenic. Expression of some isoforms derived from the AUG
            start codon is regulated by a small upstream open reading frame,
            which is located within an internal ribosome entry site. [provided
            by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (3) lacks two consecutive in-frame
            exons in the 3' coding region, compared to variant 1. This variant
            can initiate translation from non-AUG (CUG) site, and also from a
            downstream, in-frame AUG site. The isoform (8) represented in this
            RefSeq is derived from the AUG start codon and it is shorter at the
            N-terminus and lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887623.2678531.1,
                                           SRR21887620.628547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 18304943
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..146
                     /product="vascular endothelial growth factor A isoform 8
                     precursor"
                     /note="vascular permeability factor"
                     /calculated_mol_wt=14027
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3180
     mat_peptide     27..146
                     /product="vascular endothelial growth factor A isoform 8"
                     /calculated_mol_wt=14027
     Region          49..131
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(49..52,86,88..91,106..109)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(51,82,86,93,127,129)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(76,85)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P16612.2)"
     CDS             1..146
                     /gene="Vegfa"
                     /gene_synonym="Vegf; VEGF-A; VEGF111; VEGF164; VPF"
                     /coded_by="NM_001287110.1:1015..1455"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:83785"
                     /db_xref="RGD:619991"
ORIGIN      
        1 mnfllswvhw tlalllylhh akwsqaaptt egeqkahevv kfmdvyqrsy crpietlvdi
       61 fqeypdeiey ifkpscvplm rcagccndea lecvptsesn vtmqimrikp hqsqhigems
      121 flqhsrcecr pkkdrtkpek cdkprr
//
LOCUS       NP_001030170             586 aa            linear   ROD 28-APR-2025
DEFINITION  CTP synthase 2 [Rattus norvegicus].
ACCESSION   NP_001030170
VERSION     NP_001030170.1
DBSOURCE    REFSEQ: accession NM_001034998.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Lynch,E.M. and Kollman,J.M.
  TITLE     Coupled structural transitions enable highly cooperative regulation
            of human CTPS2 filaments
  JOURNAL   Nat Struct Mol Biol 27 (1), 42-48 (2020)
   PUBMED   31873303
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Tan,W.L., Bhattacharya,B., Loh,M., Balasubramanian,I., Akram,M.,
            Dong,D., Wong,L., Thakkar,B., Salto-Tellez,M., Soo,R.A.,
            Fichtner,I., Iacopetta,B. and Soong,R.
  TITLE     Low cytosine triphosphate synthase 2 expression renders resistance
            to 5-fluorouracil in colorectal cancer
  JOURNAL   Cancer Biol Ther 11 (6), 599-608 (2011)
   PUBMED   21378502
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Kassel,K.M., Au da,R., Higgins,M.J., Hines,M. and Graves,L.M.
  TITLE     Regulation of human cytidine triphosphate synthetase 2 by
            phosphorylation
  JOURNAL   J Biol Chem 285 (44), 33727-33736 (2010)
   PUBMED   20739275
REFERENCE   6  (residues 1 to 586)
  AUTHORS   van Kuilenburg,A.B., Meinsma,R., Vreken,P., Waterham,H.R. and van
            Gennip,A.H.
  TITLE     Identification of a cDNA encoding an isoform of human CTP
            synthetase
  JOURNAL   Biochim Biophys Acta 1492 (2-3), 548-552 (2000)
   PUBMED   10899599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC085949.1, DV724473.1 and JAXUCZ010000021.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085949.1, SRR26643293.32492.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation, longest
                                                protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq14"
     Protein         1..586
                     /product="CTP synthase 2"
                     /EC_number="6.3.4.2"
                     /note="CTP synthetase 2; UTP--ammonia ligase 2; cytidine
                     5'-triphosphate synthase 2; cytidine triphosphate synthase
                     II; CTP synthase II"
                     /calculated_mol_wt=65543
     Region          1..557
                     /region_name="PLN02327"
                     /note="CTP synthase"
                     /db_xref="CDD:215186"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N0.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N0.1)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N0.1)"
     CDS             1..586
                     /gene="Ctps2"
                     /coded_by="NM_001034998.2:91..1851"
                     /db_xref="GeneID:619580"
                     /db_xref="RGD:1563369"
ORIGIN      
        1 mkyilvtggv isgigkgiia ssigtilksc glrvtaikid pyinidagtf spyehgevfv
       61 lndggevdld lgnyerfldi nlykdnnitt gkiyqhvink errgdylgkt vqvvphitda
      121 iqdwvmnqak vsvdgnkedp qicvielggt igdiegmafv eafrqfqfka krenfynihv
      181 slvpqpsatg eqktkptqns vralrglgls pdlivcrsst piemavkeki smfchvnpeq
      241 vicihdvssi yrvpllleeq gvvkyfqerl dlpindcsnn llfkwktmad ryerlqkics
      301 ialvgkytkl rdcyasvfka lehsalainh klnlmyidsi dlepvtkaed pvkfheawqk
      361 lcladgilvp ggfgirgtlg klqaiswart kkipflgicl gmqlaviefa rnclnlkdan
      421 stefdpntpv plvidmpehn pgdlggtmrl glrrtvftte nsilkklygd vpyieerhrh
      481 ryevnpnlin qfenkdlcfv gedvdgkrme iieltghpyf igvqfhpefs srpmkpsppy
      541 lglllaatgt lnthlqqmsk lsysdiysda sddsfseakf aeldin
//
LOCUS       NP_001004442             445 aa            linear   ROD 28-APR-2025
DEFINITION  protein disulfide-isomerase A6 precursor [Rattus norvegicus].
ACCESSION   NP_001004442 XP_343129
VERSION     NP_001004442.1
DBSOURCE    REFSEQ: accession NM_001004442.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Milochau,A., Lagree,V., Benassy,M.N., Chaignepain,S., Papin,J.,
            Garcia-Arcos,I., Lajoix,A., Monterrat,C., Coudert,L.,
            Schmitter,J.M., Ochoa,B. and Lang,J.
  TITLE     Synaptotagmin 11 interacts with components of the RNA-induced
            silencing complex RISC in clonal pancreatic beta-cells
  JOURNAL   FEBS Lett 588 (14), 2217-2222 (2014)
   PUBMED   24882364
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Eletto,D., Eletto,D., Dersh,D., Gidalevitz,T. and Argon,Y.
  TITLE     Protein disulfide isomerase A6 controls the decay of IRE1alpha
            signaling via disulfide-dependent association
  JOURNAL   Mol Cell 53 (4), 562-576 (2014)
   PUBMED   24508390
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Jansen,G., Maattanen,P., Denisov,A.Y., Scarffe,L., Schade,B.,
            Balghi,H., Dejgaard,K., Chen,L.Y., Muller,W.J., Gehring,K. and
            Thomas,D.Y.
  TITLE     An interaction map of endoplasmic reticulum chaperones and foldases
  JOURNAL   Mol Cell Proteomics 11 (9), 710-723 (2012)
   PUBMED   22665516
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Holbrook,L.M., Watkins,N.A., Simmonds,A.D., Jones,C.I.,
            Ouwehand,W.H. and Gibbins,J.M.
  TITLE     Platelets release novel thiol isomerase enzymes which are recruited
            to the cell surface following activation
  JOURNAL   Br J Haematol 148 (4), 627-637 (2010)
   PUBMED   19995400
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Alanen,H.I., Salo,K.E., Pirneskoski,A. and Ruddock,L.W.
  TITLE     pH dependence of the peptide thiol-disulfide oxidase activity of
            six members of the human protein disulfide isomerase family
  JOURNAL   Antioxid Redox Signal 8 (3-4), 283-291 (2006)
   PUBMED   16677074
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Breuza,L., Halbeisen,R., Jeno,P., Otte,S., Barlowe,C., Hong,W. and
            Hauri,H.P.
  TITLE     Proteomics of endoplasmic reticulum-Golgi intermediate compartment
            (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
            ERGIC-32, a new cycling protein that interacts with human Erv46
  JOURNAL   J Biol Chem 279 (45), 47242-47253 (2004)
   PUBMED   15308636
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Meunier,L., Usherwood,Y.K., Chung,K.T. and Hendershot,L.M.
  TITLE     A subset of chaperones and folding enzymes form multiprotein
            complexes in endoplasmic reticulum to bind nascent proteins
  JOURNAL   Mol Biol Cell 13 (12), 4456-4469 (2002)
   PUBMED   12475965
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Fullekrug,J., Sonnichsen,B., Wunsch,U., Arseven,K., Nguyen Van,P.,
            Soling,H.D. and Mieskes,G.
  TITLE     CaBP1, a calcium binding protein of the thioredoxin family, is a
            resident KDEL protein of the ER and not of the intermediate
            compartment
  JOURNAL   J Cell Sci 107 (Pt 10), 2719-2727 (1994)
   PUBMED   7876340
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082063.1.
            
            On Sep 20, 2004 this sequence version replaced XP_343129.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082063.1, SRR8487226.117249.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..445
                     /product="protein disulfide-isomerase A6 precursor"
                     /EC_number="5.3.4.1"
                     /note="protein disulfide-isomerase A6; calcium-binding
                     protein 1; protein disulfide isomerase P5; thioredoxin
                     domain-containing protein 7; protein disulfide isomerase
                     associated 6; thioredoxin domain containing 7; protein
                     disulfide isomerase-related protein"
                     /calculated_mol_wt=46193
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2585
     Region          31..133
                     /region_name="PDI_a_P5"
                     /note="PDIa family, P5 subfamily; composed of eukaryotic
                     proteins similar to human P5, a PDI-related protein with a
                     domain structure of aa'b (where a and a' are redox active
                     TRX domains and b is a redox inactive TRX-like domain).
                     Like PDI, P5 is located in the...; cd03001"
                     /db_xref="CDD:239299"
     Site            order(60,63,123)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239299"
     Region          166..271
                     /region_name="PDI_a_P5"
                     /note="PDIa family, P5 subfamily; composed of eukaryotic
                     proteins similar to human P5, a PDI-related protein with a
                     domain structure of aa'b (where a and a' are redox active
                     TRX domains and b is a redox inactive TRX-like domain).
                     Like PDI, P5 is located in the...; cd03001"
                     /db_xref="CDD:239299"
     Site            order(195,198,261)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239299"
     Region          280..409
                     /region_name="P5_C"
                     /note="P5 family, C-terminal redox inactive TRX-like
                     domain; P5 is a protein disulfide isomerase (PDI)-related
                     protein with a domain structure of aa'b (where a and a'
                     are redox active TRX domains and b is a redox inactive
                     TRX-like domain). Like PDI, P5 is...; cd02983"
                     /db_xref="CDD:239281"
     CDS             1..445
                     /gene="Pdia6"
                     /gene_synonym="CaBP1; P5; Txndc7"
                     /coded_by="NM_001004442.1:19..1356"
                     /db_xref="GeneID:286906"
                     /db_xref="RGD:628688"
ORIGIN      
        1 mrvismarlv lglvsctffl avsalysssd dvieltpsnf nreviqsdsl wlvefyapwc
       61 ghcqrltpew kkaasalkdv vkvgavnadk hqslggqygv qgfptikifg anknkpedyq
      121 ggrtgeaivd aalsalrqlv kdrlggrsgg yssgkqgrgd ssskkdvvel tddtfdknvl
      181 dsedvwmvef yapwcghckn lepewaaaat evkeqtkgkv klaavdatvn qvlasrygik
      241 gfptikifqk gespvdydgg rtrsdivsra ldlfsdnapp pelleiined iakktceehq
      301 lcvvavlphi ldtgatgrns ylevllklad kykkkmwgwl wteagaqyel enalgiggfg
      361 ypamaainar kmkfallkgs fseqginefl relsfgrgst apvgggsfpn itprepwdgk
      421 dgelpveddi dlsdvelddl ekdel
//
LOCUS       NP_112347                683 aa            linear   ROD 28-APR-2025
DEFINITION  protein kinase C eta type [Rattus norvegicus].
ACCESSION   NP_112347
VERSION     NP_112347.1
DBSOURCE    REFSEQ: accession NM_031085.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Wang,H., Li,Y., Jiang,S., Liu,N., Zhou,Q., Li,Q., Chen,Z., Lin,Y.,
            Chen,C. and Deng,Y.
  TITLE     LncRNA xist regulates sepsis associated neuroinflammation in the
            periventricular white matter of CLP rats by miR-122-5p/PKCeta Axis
  JOURNAL   Front Immunol 14, 1225482 (2023)
   PUBMED   38115999
  REMARK    GeneRIF: LncRNA xist regulates sepsis associated neuroinflammation
            in the periventricular white matter of CLP rats by
            miR-122-5p/PKCeta Axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Li,X., Xu,L., Hou,X., Geng,J., Tian,J., Liu,X. and Bai,X.
  TITLE     Advanced Oxidation Protein Products Aggravate Tubulointerstitial
            Fibrosis Through Protein Kinase C-Dependent Mitochondrial Injury in
            Early Diabetic Nephropathy
  JOURNAL   Antioxid Redox Signal 30 (9), 1162-1185 (2019)
   PUBMED   29482336
  REMARK    GeneRIF: Study provides mechanistic evidence that inhibition of
            PKCeta isoform alleviated mitochondrial injuries and function,
            attenuated apoptosis, and renal fibrosis in high glucose
            (HG)-cultured advanced oxidation protein products (AOPPs)-induced
            HK-2 cells. Thus, AOPPs-induced mitochondrial dysfunction and
            oxidative stress cause tubulointerstitial fibrosis in diabetic
            nephropathy via activation of the PKCeta isoform.
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Liang,Y., Cucchetti,M., Roncagalli,R., Yokosuka,T., Malzac,A.,
            Bertosio,E., Imbert,J., Nijman,I.J., Suchanek,M., Saito,T.,
            Wulfing,C., Malissen,B. and Malissen,M.
  TITLE     The lymphoid lineage-specific actin-uncapping protein Rltpr is
            essential for costimulation via CD28 and the development of
            regulatory T cells
  JOURNAL   Nat Immunol 14 (8), 858-866 (2013)
   PUBMED   23793062
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Lau,E., Kluger,H., Varsano,T., Lee,K., Scheffler,I., Rimm,D.L.,
            Ideker,T. and Ronai,Z.A.
  TITLE     PKCepsilon promotes oncogenic functions of ATF2 in the nucleus
            while blocking its apoptotic function at mitochondria
  JOURNAL   Cell 148 (3), 543-555 (2012)
   PUBMED   22304920
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Raveh-Amit,H., Hai,N., Rotem-Dai,N., Shahaf,G., Gopas,J. and
            Livneh,E.
  TITLE     Protein kinase Ceta activates NF-kappaB in response to
            camptothecin-induced DNA damage
  JOURNAL   Biochem Biophys Res Commun 412 (2), 313-317 (2011)
   PUBMED   21820409
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Hussaini,I.M., Karns,L.R., Vinton,G., Carpenter,J.E., Redpath,G.T.,
            Sando,J.J. and VandenBerg,S.R.
  TITLE     Phorbol 12-myristate 13-acetate induces protein kinase
            ceta-specific proliferative response in astrocytic tumor cells
  JOURNAL   J Biol Chem 275 (29), 22348-22354 (2000)
   PUBMED   10806212
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Albert,C.J. and Ford,D.A.
  TITLE     Protein kinase C translocation and PKC-dependent protein
            phosphorylation during myocardial ischemia
  JOURNAL   Am J Physiol 276 (2), H642-H650 (1999)
   PUBMED   9950866
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Mahadev,K. and Vemuri,M.C.
  TITLE     Selective changes in protein kinase C isoforms and phosphorylation
            of endogenous substrate proteins in rat cerebral cortex during pre-
            and postnatal ethanol exposure
  JOURNAL   Arch Biochem Biophys 356 (2), 249-257 (1998)
   PUBMED   9705215
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Chen,C.C., Wang,J.K., Chen,W.C. and Lin,S.B.
  TITLE     Protein kinase C eta mediates lipopolysaccharide-induced
            nitric-oxide synthase expression in primary astrocytes
  JOURNAL   J Biol Chem 273 (31), 19424-19430 (1998)
   PUBMED   9677361
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Dekker,L.V., Parker,P.J. and McIntyre,P.
  TITLE     Biochemical properties of rat protein kinase C-eta expressed in COS
            cells
  JOURNAL   FEBS Lett 312 (2-3), 195-199 (1992)
   PUBMED   1426252
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081782.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081782.1, X68400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..683
                     /product="protein kinase C eta type"
                     /EC_number="2.7.11.13"
                     /note="PKC-L; nPKC-eta"
                     /calculated_mol_wt=77816
     Region          8..140
                     /region_name="C2_PKC_epsilon"
                     /note="C2 domain in Protein Kinase C (PKC) epsilon;
                     cd04014"
                     /db_xref="CDD:175981"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P24723; propagated from
                     UniProtKB/Swiss-Prot (Q64617.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P24723; propagated from
                     UniProtKB/Swiss-Prot (Q64617.1)"
     Site            order(42,89,95)
                     /site_type="metal-binding"
                     /note="metal binding pocket [ion binding]"
                     /db_xref="CDD:175981"
     Region          166..226
                     /region_name="C1_nPKC_epsilon-like_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in novel protein kinase C (nPKC) epsilon,
                     eta, and similar proteins; cd20835"
                     /db_xref="CDD:410385"
     Site            order(177..183,191..195,199)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410385"
     Region          244..298
                     /region_name="C1_nPKC_epsilon-like_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in novel protein kinase C (nPKC) epsilon,
                     eta, and similar proteins; cd20838"
                     /db_xref="CDD:410388"
     Site            order(251..257,265..269,272)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410388"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23298; propagated from
                     UniProtKB/Swiss-Prot (Q64617.1)"
     Region          359..681
                     /region_name="STKc_nPKC_eta"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Novel Protein Kinase C eta; cd05590"
                     /db_xref="CDD:270742"
     Site            order(361..365,369,382,384,417,433..434,436,440,442,479,
                     481,483..484,486,496..497,500,514..519,546,552,555)
                     /site_type="active"
                     /db_xref="CDD:270742"
     Site            order(361..365,369,382,384,417,434..436,440,479,481,
                     483..484,486,496..497)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270742"
     Site            order(365,440,442,479,481,483,500,514..519,546,552,555)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270742"
     Site            496..519
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270742"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q64617.1)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64617.1)"
     Site            656
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270742"
     Site            671..676
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270742"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q64617.1)"
     CDS             1..683
                     /gene="Prkch"
                     /coded_by="NM_031085.2:188..2239"
                     /db_xref="GeneID:81749"
                     /db_xref="RGD:621888"
ORIGIN      
        1 mssgtmkfng ylrvrigeav glqptrwslr hslfkkghql ldpyltvsvd qvrvgqtstk
       61 qktnkptyne efctnvsdgg hlelavfhet plgydhfvan ctlqfqellr tagtsdtfeg
      121 wvdlepegkv fvvitltgsf teatlqrdri fkhftrkrqr amrrrvhqvn ghkfmatylr
      181 qptycshcre fiwgvfgkqg yqcqvctcvv hkrchhlivt actcqnnink vdakiaeqrf
      241 giniphkfnv hnykvptfcd hcgsllwgim rqglqckick mnvhircqan vapncgvnav
      301 elaktlagmg lqpgnispts klisrstlrr qgkegskegn gigvnsssrf gidnfefirv
      361 lgkgsfgkvm lariketgel yavkvlkkdv ilqdddvect mtekrilsla rnhpfltqlf
      421 ccfqtpdrlf fvmefvnggd lmfhiqksrr fdeararfya aeiisalmfl hekgiiyrdl
      481 kldnvlldhe ghckladfgm ckegicngvt tatfcgtpdy iapeilqeml ygpavdwwam
      541 gvllyemlcg hapfeaened dlfeailnde vvyptwlhed atgilksfmt knptmrlgsl
      601 tqggeheilr hpffkeidwv qlnhrqlepp frpriksred vsnfdpdfik eepvltpide
      661 ghlpminqde frnfsyvspe lqp
//
LOCUS       NP_001013172             351 aa            linear   ROD 28-APR-2025
DEFINITION  polycomb group RING finger protein 6 [Rattus norvegicus].
ACCESSION   NP_001013172 XP_219963
VERSION     NP_001013172.1
DBSOURCE    REFSEQ: accession NM_001013154.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Almeida,M., Pintacuda,G., Masui,O., Koseki,Y., Gdula,M., Cerase,A.,
            Brown,D., Mould,A., Innocent,C., Nakayama,M., Schermelleh,L.,
            Nesterova,T.B., Koseki,H. and Brockdorff,N.
  TITLE     PCGF3/5-PRC1 initiates Polycomb recruitment in X chromosome
            inactivation
  JOURNAL   Science 356 (6342), 1081-1084 (2017)
   PUBMED   28596365
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Taherbhoy,A.M., Huang,O.W. and Cochran,A.G.
  TITLE     BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase
  JOURNAL   Nat Commun 6, 7621 (2015)
   PUBMED   26151332
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Gil,J. and O'Loghlen,A.
  TITLE     PRC1 complex diversity: where is it taking us?
  JOURNAL   Trends Cell Biol 24 (11), 632-641 (2014)
   PUBMED   25065329
  REMARK    Review article
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Simon,J.A. and Kingston,R.E.
  TITLE     Occupying chromatin: Polycomb mechanisms for getting to genomic
            targets, stopping transcriptional traffic, and staying put
  JOURNAL   Mol Cell 49 (5), 808-824 (2013)
   PUBMED   23473600
  REMARK    Review article
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Maertens,G.N., El Messaoudi-Aubert,S., Racek,T., Stock,J.K.,
            Nicholls,J., Rodriguez-Niedenfuhr,M., Gil,J. and Peters,G.
  TITLE     Several distinct polycomb complexes regulate and co-localize on the
            INK4a tumor suppressor locus
  JOURNAL   PLoS One 4 (7), e6380 (2009)
   PUBMED   19636380
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Akasaka,T., Takahashi,N., Suzuki,M., Koseki,H., Bodmer,R. and
            Koga,H.
  TITLE     MBLR, a new RING finger protein resembling mammalian Polycomb gene
            products, is regulated by cell cycle-dependent phosphorylation
  JOURNAL   Genes Cells 7 (8), 835-850 (2002)
   PUBMED   12167161
REFERENCE   8  (residues 1 to 351)
  AUTHORS   Kanno,M., Hasegawa,M., Ishida,A., Isono,K. and Taniguchi,M.
  TITLE     mel-18, a Polycomb group-related mammalian gene, encodes a
            transcriptional negative regulator with tumor suppressive activity
  JOURNAL   EMBO J 14 (22), 5672-5678 (1995)
   PUBMED   8521824
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083820.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219963.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..351
                     /product="polycomb group RING finger protein 6"
                     /note="ring finger protein 134"
                     /calculated_mol_wt=39575
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI70.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BYE7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI70.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BYE7; propagated from
                     UniProtKB/Swiss-Prot (Q5XI70.1)"
     Region          126..184
                     /region_name="RING-HC_PCGF6"
                     /note="RING finger found in polycomb group RING finger
                     protein 6 (PCGF6) and similar proteins; cd16738"
                     /db_xref="CDD:438396"
     Site            order(134,138,140..141,144,146..147,149..153,156..159,
                     161..162)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:438396"
     Site            order(135,138,151,153,156,159,170,173)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438396"
     Region          253..342
                     /region_name="RAWUL_PCGF6"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     6 (PCGF6) and similar proteins; cd17085"
                     /db_xref="CDD:340605"
     CDS             1..351
                     /gene="Pcgf6"
                     /gene_synonym="Rnf134"
                     /coded_by="NM_001013154.1:55..1110"
                     /db_xref="GeneID:309457"
                     /db_xref="RGD:1306904"
ORIGIN      
        1 meeaetdate nkraseakra samlpppppp isppalipap aageegpasl aqagapgcsr
       61 srppeleper slgrlrgrfe dydeeleede emeeeeeeee emshfslrle sgradsedee
      121 erlinlvelt pyilcsickg ylidattite clhtfcksci vrhfyysnrc pkcnivvhqt
      181 qplynirldr qlqdivyklv vnleerekkq mhdfykergl evpkpavpqp vpaskgrtkk
      241 alesvfripp eldvslllef iganedtghf kplekkfvrv sgeatighve kflrrkmgld
      301 pacqvdiicg dhlleryqtl reirraigdt amqdgllvlh yglvvsplki t
//
LOCUS       NP_075244               1574 aa            linear   ROD 28-APR-2025
DEFINITION  multiple epidermal growth factor-like domains protein 6 precursor
            [Rattus norvegicus].
ACCESSION   NP_075244 XP_346756
VERSION     NP_075244.1
DBSOURCE    REFSEQ: accession NM_022955.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1574)
  AUTHORS   Nakayama,M., Nakajima,D., Nagase,T., Nomura,N., Seki,N. and
            Ohara,O.
  TITLE     Identification of high-molecular-weight proteins with multiple
            EGF-like motifs by motif-trap screening
  JOURNAL   Genomics 51 (1), 27-34 (1998)
   PUBMED   9693030
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB011532.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346756.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMN11044071
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1574
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1574
                     /product="multiple epidermal growth factor-like domains
                     protein 6 precursor"
                     /note="multiple epidermal growth factor-like domains
                     protein 6; EGF-like domain-containing protein 3; multiple
                     EGF-like domains protein 6; multiple epidermal growth
                     factor-like domains protein 6-like; EGF-like-domain,
                     multiple 3; multiple EGF-like domain protein 3; multiple
                     epidermal growth factor-like domains 6; epidermal growth
                     factor-like protein 3"
                     /calculated_mol_wt=162608
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2859
     mat_peptide     28..1574
                     /product="Multiple epidermal growth factor-like domains
                     protein 6. /id=PRO_0000007525"
                     /note="propagated from UniProtKB/Swiss-Prot (O88281.1)"
                     /calculated_mol_wt=162608
     Region          41..113
                     /region_name="EMI"
                     /note="EMI domain; pfam07546"
                     /db_xref="CDD:462204"
     Region          127..162
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <154..202
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          209..245
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <237..285
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          <284..325
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          338..373
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <371..410
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          <413..452
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          1555..1574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88281.1)"
     CDS             1..1574
                     /gene="Megf6"
                     /gene_synonym="Egfl3"
                     /coded_by="NM_022955.1:235..4959"
                     /db_xref="GeneID:65049"
                     /db_xref="RGD:621188"
ORIGIN      
        1 mpvraearaa wrvvalalll lpampaaspp ltprplqpsm phvcaeqklt lvghrqpcvq
       61 afsrivpvwr rtgcaqqawc igqerrtvyy msyrqvyate artvfrccpg wsqkpgqegc
      121 lsdvdecasa nggcegpccn tvggfycrcp pgyqlqgdgk tcqdvdecra hnggcqhrcv
      181 ntpgsylcec kpgfrlhtdg rtclaissct lgnggcqhqc vqltvtqhrc qcrpqyqlqe
      241 dgrrcvrrsp caegnggcmh icqelrglah cgchpgyqla adrktcedvd ecalglaqca
      301 hgclntqgsf kcvchagyel gadgrqcyri emeivnscea gnggcshgcs htstgplctc
      361 prgyeldedq ktcididdca nspccqqaca ntpggyecsc fagyrlntdg cgcedvdeca
      421 sghggcehhc snlagsfqcf ceagyrlded rrgctslees vvdldgrlpf vrplphiavl
      481 rdelprlfqd dygaeeeaaa aelrgehtlt ekfvcldhsf ghdcsltcdd crnggtcfpg
      541 qdgcdcpegw tgiicnetcp pdtfgkncss pctcqnggtc dpvlgacrcp pgvsgahced
      601 gcpkgfygkh crkkchcanr grchrlygac lcdpglygrf chlacppwaf gpgcsedclc
      661 eqshtrscnp kdgscsckag fqgercqaec esgffgpgcr hrctcqpgva cdpvsgecrt
      721 qcppgyqged cgqecpvgtf gvncsgscsc vgapchrvtg eclcppgktg edcgadcpeg
      781 rwglgcqeic pacehgascn petgtclclp gfvgsrcqdt csagwygtgc qircacandg
      841 hcdpttgrcs capgwtglsc qracdsghwg pdcihpcncs aghgncdavs glclceagye
      901 gprceqscrq gyygpsceqk crcehgaacd hvsgactcpa gwrgsfceha cpagffgldc
      961 dsacncsaga pcdavtgsci cpagrwgprc aqscppltfg lncsqictcf ngascdsvtg
     1021 qchcapgwmg ptclqacppg lygkncqhsc lcrnggrcdp ilgqctcpeg wtglacenec
     1081 lpghyaagcq lncsclhggi cdrltghclc pagwtgdkcq sscvsgtfgv hceehcacrk
     1141 gaschhvtga cfcppgwrgp hceqacprgw fgeacaqrcl cptnaschhv tgecrcppgf
     1201 tglsceqacq pgtfgkdceh lcqcpgetwa cdpasgvctc aagyhgtgcl qrcpsgrygp
     1261 gcehickcln ggtcdpatga cycpagflga dcslacpqgr fgpscahvca crqgaacdpv
     1321 sgacicspgk tgvrcehgcp qdrfgkgcel kcacrngglc hatngscscp lgwmgphceh
     1381 acpagrygaa cllecfcqnn gscepttgac lcgpgfygqa cehscpsgfh gpgcqrvcec
     1441 qqgapcdpvs gqclcpagfh gqfcekgces gsfgdgclqq cnchtgvpcd pisglclcpp
     1501 grtgaacdld crrgrfgpgc alrcdcggga dcdpisgqch cvdsymgptc revptqisss
     1561 rpapqhpssr amkh
//
LOCUS       NP_001153704             133 aa            linear   ROD 28-APR-2025
DEFINITION  40S ribosomal protein S30 precursor [Rattus norvegicus].
ACCESSION   NP_001153704
VERSION     NP_001153704.1
DBSOURCE    REFSEQ: accession NM_001160232.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 133)
  AUTHORS   O'Donohue,M.F., Choesmel,V., Faubladier,M., Fichant,G. and
            Gleizes,P.E.
  TITLE     Functional dichotomy of ribosomal proteins during the synthesis of
            mammalian 40S ribosomal subunits
  JOURNAL   J Cell Biol 190 (5), 853-866 (2010)
   PUBMED   20819938
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Yu,Y., Ji,H., Doudna,J.A. and Leary,J.A.
  TITLE     Mass spectrometric analysis of the human 40S ribosomal subunit:
            native and HCV IRES-bound complexes
  JOURNAL   Protein Sci 14 (6), 1438-1446 (2005)
   PUBMED   15883184
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Tollin,M., Bergman,P., Svenberg,T., Jornvall,H., Gudmundsson,G.H.
            and Agerberth,B.
  TITLE     Antimicrobial peptides in the first line defence of human colon
            mucosa
  JOURNAL   Peptides 24 (4), 523-530 (2003)
   PUBMED   12860195
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Hiemstra,P.S., van den Barselaar,M.T., Roest,M., Nibbering,P.H. and
            van Furth,R.
  TITLE     Ubiquicidin, a novel murine microbicidal protein present in the
            cytosolic fraction of macrophages
  JOURNAL   J Leukoc Biol 66 (3), 423-428 (1999)
   PUBMED   10496312
REFERENCE   7  (residues 1 to 133)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   8  (residues 1 to 133)
  AUTHORS   Olvera,J. and Wool,I.G.
  TITLE     The carboxyl extension of a ubiquitin-like protein is rat ribosomal
            protein S30
  JOURNAL   J Biol Chem 268 (24), 17967-17974 (1993)
   PUBMED   8394356
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091402.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DV213562.1, FM061813.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..133
                     /product="40S ribosomal protein S30 precursor"
                     /note="40S ribosomal protein S30; ubiquitin-like protein
                     FUBI; Finkel-Biskis-Reilly murine sarcoma
                     virusubiquitously expressed; Finkel-Biskis-Reilly murine
                     sarcoma virus (FBR-MuSV) ubiquitously expressed (fox
                     derived) protein"
                     /calculated_mol_wt=14241
     mat_peptide     1..74
                     /product="ubiquitin-like protein fubi"
                     /calculated_mol_wt=7742
     Region          1..74
                     /region_name="Ubl_FUBI"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin-like
                     protein FUBI and similar proteins; cd01793"
                     /db_xref="CDD:340491"
     mat_peptide     75..133
                     /product="ribosomal protein S30"
                     /calculated_mol_wt=6648
     Region          75..132
                     /region_name="Ribosomal_S30"
                     /note="Ribosomal protein S30; pfam04758"
                     /db_xref="CDD:398432"
     CDS             1..133
                     /gene="Fau"
                     /coded_by="NM_001160232.1:66..467"
                     /db_xref="GeneID:29752"
                     /db_xref="RGD:61938"
ORIGIN      
        1 mqlfvraqel htlevtgqet vaqikahvas legiapedqv vllagspled eatlgqcgve
       61 alttlevagr mlggkvhgsl aragkvrgqt pkvakqekkk kktgrakrrm qynrrfvnvv
      121 ptfgkkkgpn ans
//
LOCUS       NP_112400                152 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin-conjugating enzyme E2 B [Rattus norvegicus].
ACCESSION   NP_112400
VERSION     NP_112400.1
DBSOURCE    REFSEQ: accession NM_031138.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Peng,Y., Zhang,Q., Cheng,H., Yan,G. and Xing,C.
  TITLE     Upregulation of ubiquitin conjugating enzyme E2B (Ube2b)
            ameliorates neuropathic pain by regulating Kcna2 (potassium
            voltage-gated channel subfamily A member 2) in primary afferent
            neurons
  JOURNAL   Bioengineered 12 (1), 7470-7480 (2021)
   PUBMED   34632937
  REMARK    GeneRIF: Upregulation of ubiquitin conjugating enzyme E2B (Ube2b)
            ameliorates neuropathic pain by regulating Kcna2 (potassium
            voltage-gated channel subfamily A member 2) in primary afferent
            neurons.
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Chen,Z.G., Wang,Y.J., Chen,R.S., Geng,F., Gan,C.L., Wang,W.S.,
            Liu,X., Zhou,H., He,L., Hu,G. and Liu,J.G.
  TITLE     Ube2b-dependent degradation of DNMT3a relieves a transcriptional
            brake on opiate-induced synaptic and behavioral plasticity
  JOURNAL   Mol Psychiatry 26 (4), 1162-1177 (2021)
   PUBMED   31576007
  REMARK    GeneRIF: Ube2b-dependent degradation of DNMT3a relieves a
            transcriptional brake on opiate-induced synaptic and behavioral
            plasticity.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   David,Y., Ziv,T., Admon,A. and Navon,A.
  TITLE     The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
            preferred lysines
  JOURNAL   J Biol Chem 285 (12), 8595-8604 (2010)
   PUBMED   20061386
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Kim,J., Guermah,M., McGinty,R.K., Lee,J.S., Tang,Z., Milne,T.A.,
            Shilatifard,A., Muir,T.W. and Roeder,R.G.
  TITLE     RAD6-Mediated transcription-coupled H2B ubiquitylation directly
            stimulates H3K4 methylation in human cells
  JOURNAL   Cell 137 (3), 459-471 (2009)
   PUBMED   19410543
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Ryu,K.S., Choi,Y.S., Ko,J., Kim,S.O., Kim,H.J., Cheong,H.K.,
            Jeon,Y.H., Choi,B.S. and Cheong,C.
  TITLE     Direct characterization of E2-dependent target specificity and
            processivity using an artificial p27-linker-E2 ubiquitination
            system
  JOURNAL   BMB Rep 41 (12), 852-857 (2008)
   PUBMED   19123975
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Grootegoed,J.A., Baarends,W.M., Roest,H.P. and Hoeijmakers,J.H.
  TITLE     Knockout mouse model and gametogenic failure
  JOURNAL   Mol Cell Endocrinol 145 (1-2), 161-166 (1998)
   PUBMED   9922113
  REMARK    Review article
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Gantla,S., Bakker,C.T., Deocharan,B., Thummala,N.R., Zweiner,J.,
            Sinaasappel,M., Roy Chowdhury,J., Bosma,P.J. and Roy Chowdhury,N.
  TITLE     Splice-site mutations: a novel genetic mechanism of Crigler-Najjar
            syndrome type 1
  JOURNAL   Am J Hum Genet 62 (3), 585-592 (1998)
   PUBMED   9497253
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Wing,S.S. and Banville,D.
  TITLE     14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and
            regulation upon fasting and by insulin
  JOURNAL   Am J Physiol 267 (1 Pt 1), E39-E48 (1994)
   PUBMED   8048511
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Wing,S.S., Dumas,F. and Banville,D.
  TITLE     A rabbit reticulocyte ubiquitin carrier protein that supports
            ubiquitin-dependent proteolysis (E214k) is homologous to the yeast
            DNA repair gene RAD6
  JOURNAL   J Biol Chem 267 (10), 6495-6501 (1992)
   PUBMED   1313008
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Koken,M.H., Reynolds,P., Jaspers-Dekker,I., Prakash,L., Prakash,S.,
            Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Structural and functional conservation of two human homologs of the
            yeast DNA repair gene RAD6
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 8865-8869 (1991)
   PUBMED   1717990
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN931313.1, BC070946.1 and BE111816.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DN931313.1, BC070946.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..152
                     /product="ubiquitin-conjugating enzyme E2 B"
                     /EC_number="2.3.2.23"
                     /note="E2(14k); ubiquitin-protein ligase B; ubiquitin
                     carrier protein B; RAD6 homolog B; ubiquitin-conjugating
                     enzyme E2(14k); ubiquitin-conjugating enzyme E2B, RAD6
                     homology; ubiquitin conjugating enzyme;
                     ubiquitin-conjugating enzyme E2B (RAD6 homolog, S.
                     cerevisiae); E2 ubiquitin-conjugating enzyme B"
                     /calculated_mol_wt=17181
     Region          3..145
                     /region_name="UBCc_UBE2A_2B"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin-conjugating enzymes E2A, E2B and
                     related proteins; cd23790"
                     /db_xref="CDD:467410"
     CDS             1..152
                     /gene="Ube2b"
                     /gene_synonym="HR6B"
                     /coded_by="NM_031138.2:102..560"
                     /db_xref="GeneID:81816"
                     /db_xref="RGD:708345"
ORIGIN      
        1 mstparrrlm rdfkrlqedp pvgvsgapse nnimqwnavi fgpegtpfed gtfklviefs
       61 eeypnkpptv rflskmfhpn vyadgsicld ilqnrwspty dvssiltsiq slldepnpns
      121 pansqaaqly qenkreyekr vsaiveqswn ds
//
LOCUS       NP_001099699             512 aa            linear   ROD 28-APR-2025
DEFINITION  centrosomal protein CCDC61 [Rattus norvegicus].
ACCESSION   NP_001099699
VERSION     NP_001099699.1
DBSOURCE    REFSEQ: accession NM_001106229.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127532.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..512
                     /product="centrosomal protein CCDC61"
                     /note="coiled-coil domain-containing protein 61; VFL3
                     homolog"
                     /calculated_mol_wt=57599
     Region          1..142
                     /region_name="Head domain.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Region          7..139
                     /region_name="HD_CCDC61_N"
                     /note="N-terminal head domain found in coiled-coil
                     domain-containing protein 61 and similar proteins;
                     cd22284"
                     /db_xref="CDD:409001"
     Site            order(8,19,34,36,39,41)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409001"
     Region          <147..>319
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          282..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Region          430..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6R9; propagated from
                     UniProtKB/Swiss-Prot (A0JPP8.1)"
     CDS             1..512
                     /gene="Ccdc61"
                     /gene_synonym="RGD1307390"
                     /coded_by="NM_001106229.1:344..1882"
                     /db_xref="GeneID:292680"
                     /db_xref="RGD:1307390"
ORIGIN      
        1 meqpaglqvd ymfrgvehav rvvvsgqvle levedrmtad qwrgefdanf iedlthktgn
       61 fkqfsifcnm lesaltqsse svtldlltyt dleslrsrkl ggrpgpcprs aqlnskryli
      121 liysvefdri hyplplpyqg kpdpvvlqgi irslkeelgh lrgmnggqda reteiwhlre
      181 qvtrlasekr eleaqlgrsr eealagraar qeaeslrglv rglelelrqe rglggraagr
      241 rsqdcrrlak eleevkaser nlrarlktln celamyrrgr rtlpagared ralssrerst
      301 srgrtatrss sresnrgars hgrpahpsps ptgsrvprfd ptafvkakek kqreirmkrq
      361 qqqqqqrnrm gsggsgdgps vswshqtrpp aavtgrgdaa nrsrnrsssv dsfrsrcssv
      421 sscseledfs qsvsksrrcr grgkppspip wsgsktkstt rernnhqrhl assgawvpik
      481 eyssdyqgad maeidarlka lqeymnrldt rs
//
LOCUS       NP_001017459             719 aa            linear   ROD 28-APR-2025
DEFINITION  nuclear protein MDM1 [Rattus norvegicus].
ACCESSION   NP_001017459 XP_235172
VERSION     NP_001017459.2
DBSOURCE    REFSEQ: accession NM_001017459.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Hoh,R.A., Stowe,T.R., Turk,E. and Stearns,T.
  TITLE     Transcriptional program of ciliated epithelial cells reveals new
            cilium and centrosome components and links to human disease
  JOURNAL   PLoS One 7 (12), e52166 (2012)
   PUBMED   23300604
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Won,J., Shi,L.Y., Hicks,W., Wang,J., Hurd,R., Naggert,J.K.,
            Chang,B. and Nishina,P.M.
  TITLE     Mouse model resources for vision research
  JOURNAL   J Ophthalmol 2011, 391384 (2011)
   PUBMED   21052544
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB544747.1, CV126474.1 and BC087101.1.
            
            On Oct 1, 2011 this sequence version replaced NP_001017459.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..719
                     /product="nuclear protein MDM1"
                     /note="transformed mouse 3T3 cell double minute 1; Mdm1
                     nuclear protein homolog"
                     /calculated_mol_wt=80567
     Region          9..554
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     Region          9..15
                     /region_name="ST]-E-Y-X(3)-F motif 1, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q8TC05"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Region          78..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Region          192..198
                     /region_name="ST]-E-Y-X(3)-F motif 2, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q8TC05"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Region          235..241
                     /region_name="ST]-E-Y-X(3)-F motif 3, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q8TC05"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Region          306..312
                     /region_name="ST]-E-Y-X(3)-F motif 4, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000250|UniProtKB:Q8TC05"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Region          453..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TC05; propagated from
                     UniProtKB/Swiss-Prot (Q5PQN4.2)"
     CDS             1..719
                     /gene="Mdm1"
                     /coded_by="NM_001017459.2:124..2283"
                     /db_xref="GeneID:314859"
                     /db_xref="RGD:1561092"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsesynpsv gqkytwaglr sdqlgitkep sfiskrrvpy
       61 ydpqiskyle wngtvrenda lappepqiir tpkpqeaeqr edanhetvlp qeasrvpkrt
      121 rshsadsrae gasdgvekhq dvtknhslvn advelrpstk plpesieprl drhlrkkagl
      181 avvplnnalr nseyqrqfvw ktcketapvc aanqvfrnks qvipqfqgnt fiheseykrn
      241 fkgltpvkep klreylkgns sfeilspekk adepldlevd masedsdqpi kkpapwrhqr
      301 lgkvnseyra kflspaqyly kagawtrvke slshqgslna mwyaevkelr ekaesyrkrv
      361 qgthfsrdhl nqimsdsncc wdvssvasse gtissniqal dlagdltshr tlqkhpptkl
      421 eekkvalaeq plentirsle lpeaptmarr klawdaaegt qkedtqeeps geedgrearg
      481 kdkqvcagel qkvdmqtska dgptegsets svssgkggrl ptprlrelgi qrthhdlttp
      541 avggavlvsp akakpsaleq rrrpssqdgl etlkkgitkk gkhrplsllt sptagmktvd
      601 plplrqdcda nvlrvaegtl pvlknldhqt ntpgqpspct lpychpssri qgrlrdpefq
      661 hnigkprmnn tqllphgafn dedadrlsei sarsavsslq afqtlaraqk rkenfwgkp
//
LOCUS       NP_001257618             178 aa            linear   ROD 28-APR-2025
DEFINITION  FXYD domain-containing ion transport regulator 5 precursor [Rattus
            norvegicus].
ACCESSION   NP_001257618
VERSION     NP_001257618.1
DBSOURCE    REFSEQ: accession NM_001270689.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Ding,L. and Li,J.
  TITLE     FXYD domain containing ion transport regulator 5 (FXYD5) silencing
            promotes cell viability and alleviates inflammatory response in
            cerulein-induced AR42J cells by blocking JAK2/STAT3 signaling
            pathway
  JOURNAL   Bioengineered 13 (2), 2639-2647 (2022)
   PUBMED   35042436
  REMARK    GeneRIF: FXYD domain containing ion transport regulator 5 (FXYD5)
            silencing promotes cell viability and alleviates inflammatory
            response in cerulein-induced AR42J cells by blocking JAK2/STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Huang,X., Wang,B., Yang,D., Shi,X., Hong,J., Wang,S., Dai,X.,
            Zhou,X. and Geng,Y.J.
  TITLE     Reduced expression of FXYD domain containing ion transport
            regulator 5 in association with hypertension
  JOURNAL   Int J Mol Med 29 (2), 231-238 (2012)
   PUBMED   22085977
  REMARK    GeneRIF: FXYD5 may have profound impact on the regulation of blood
            pressure.
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Ino,Y., Gotoh,M., Sakamoto,M., Tsukagoshi,K. and Hirohashi,S.
  TITLE     Dysadherin, a cancer-associated cell membrane glycoprotein,
            down-regulates E-cadherin and promotes metastasis
  JOURNAL   Proc Natl Acad Sci U S A 99 (1), 365-370 (2002)
   PUBMED   11756660
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Sweadner,K.J. and Rael,E.
  TITLE     The FXYD gene family of small ion transport regulators or channels:
            cDNA sequence, protein signature sequence, and expression
  JOURNAL   Genomics 68 (1), 41-56 (2000)
   PUBMED   10950925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000001.1, FM122563.1
            and DV726876.1.
            
            Summary: This reference sequence was derived from multiple
            replicate ESTs and validated by similar mouse cDNA sequence and
            human genomic sequence. This gene encodes a member of a family of
            small membrane proteins that share a 35-amino acid signature
            sequence domain, beginning with the sequence PFXYD and containing 7
            invariant and 6 highly conserved amino acids. The approved human
            gene nomenclature for the family is FXYD-domain containing ion
            transport regulator. Mouse FXYD5 has been termed RIC (Related to
            Ion Channel). FXYD2, also known as the gamma subunit of the
            Na,K-ATPase, regulates the properties of that enzyme. FXYD1
            (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and
            FXYD5 (RIC) have been shown to induce channel activity in
            experimental expression systems. Transmembrane topology has been
            established for two family members (FXYD1 and FXYD2), with the
            N-terminus extracellular and the C-terminus on the cytoplasmic side
            of the membrane. Three transcript variants encoding the same
            protein have been found for this gene. [RefSeq curation by Kathleen
            J. Sweadner, Ph.D., sweadner@helix.mgh.harvard.edu., Dec 2000].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ220058.1, SRR21887623.2039243.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676806 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..178
                     /product="FXYD domain-containing ion transport regulator 5
                     precursor"
                     /note="oncoprotein induced transcript 2"
                     /calculated_mol_wt=16963
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          21..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P59647.2)"
     mat_peptide     22..178
                     /product="FXYD domain-containing ion transport regulator
                     5. /id=PRO_0000010371"
                     /note="propagated from UniProtKB/Swiss-Prot (P59647.2)"
                     /calculated_mol_wt=16963
     Region          128..175
                     /region_name="FXYD_FXYD5"
                     /note="FXYD domain of FXYD domain-containing ion transport
                     regulator 5; cd20323"
                     /db_xref="CDD:410559"
     Site            order(135,137,139,142..143,146..147,149..150,153,156..158,
                     160..161,163)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410559"
     Site            147..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P59647.2)"
     CDS             1..178
                     /gene="Fxyd5"
                     /gene_synonym="RIC"
                     /coded_by="NM_001270689.1:70..606"
                     /db_xref="GeneID:60338"
                     /db_xref="RGD:620827"
ORIGIN      
        1 msppsqlcll tivalilpse gqtpekprss ftahqssvtt hvpvpdqtsp gvqttppiwt
       61 seageatgsq taaktktqql tematanpvt dpgpltssek gtpalsriks psppkgympp
      121 syienpldpn enspfyydnt tlrkrgllva avlfitgiii ltsgkcrqfs qlclnrhr
//
LOCUS       NP_001005884             739 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial proton/calcium exchanger protein precursor [Rattus
            norvegicus].
ACCESSION   NP_001005884 XP_223541
VERSION     NP_001005884.1
DBSOURCE    REFSEQ: accession NM_001005884.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Shao,J., Fu,Z., Ji,Y., Guan,X., Guo,S., Ding,Z., Yang,X., Cong,Y.
            and Shen,Y.
  TITLE     Leucine zipper-EF-hand containing transmembrane protein 1 (LETM1)
            forms a Ca2+/H+ antiporter
  JOURNAL   Sci Rep 6, 34174 (2016)
   PUBMED   27669901
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Hou,T., Jian,C., Xu,J., Huang,A.Y., Xi,J., Hu,K., Wei,L., Cheng,H.
            and Wang,X.
  TITLE     Identification of EFHD1 as a novel Ca(2+) sensor for mitoflash
            activation
  JOURNAL   Cell Calcium 59 (5), 262-270 (2016)
   PUBMED   26975899
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Doonan,P.J., Chandramoorthy,H.C., Hoffman,N.E., Zhang,X.,
            Cardenas,C., Shanmughapriya,S., Rajan,S., Vallem,S., Chen,X.,
            Foskett,J.K., Cheung,J.Y., Houser,S.R. and Madesh,M.
  TITLE     LETM1-dependent mitochondrial Ca2+ flux modulates cellular
            bioenergetics and proliferation
  JOURNAL   FASEB J 28 (11), 4936-4949 (2014)
   PUBMED   25077561
  REMARK    GeneRIF: Reconstitution of LETM1 or antioxidant overexpression
            rescued mitochondrial Ca(2+) transport and bioenergetics
            Erratum:[FASEB J. 2015 Aug;29(8):3593. doi:
            10.1096/fj.14-256453ERR. PMID: 26232296]
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Zhang,X., Chen,G., Lu,Y., Liu,J., Fang,M., Luo,J., Cao,Q. and
            Wang,X.
  TITLE     Association of mitochondrial letm1 with epileptic seizures
  JOURNAL   Cereb Cortex 24 (10), 2533-2540 (2014)
   PUBMED   23645710
  REMARK    GeneRIF: Letm1 expression is decreased in patients with intractable
            TLE and a rat model of epilepsy. Down-regulation of Letm1 leads to
            increases mitochondrial swelling and decreased MT-CYB expression,
            which is associated with susceptibility to seizures.
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Jiang,D., Zhao,L. and Clapham,D.E.
  TITLE     Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+
            antiporter
  JOURNAL   Science 326 (5949), 144-147 (2009)
   PUBMED   19797662
REFERENCE   6  (residues 1 to 739)
  AUTHORS   Tamai,S., Iida,H., Yokota,S., Sayano,T., Kiguchiya,S., Ishihara,N.,
            Hayashi,J., Mihara,K. and Oka,T.
  TITLE     Characterization of the mitochondrial protein LETM1, which
            maintains the mitochondrial tubular shapes and interacts with the
            AAA-ATPase BCS1L
  JOURNAL   J Cell Sci 121 (Pt 15), 2588-2600 (2008)
   PUBMED   18628306
REFERENCE   7  (residues 1 to 739)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 739)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   9  (residues 1 to 739)
  AUTHORS   Endele,S., Fuhry,M., Pak,S.J., Zabel,B.U. and Winterpacht,A.
  TITLE     LETM1, a novel gene encoding a putative EF-hand Ca(2+)-binding
            protein, flanks the Wolf-Hirschhorn syndrome (WHS) critical region
            and is deleted in most WHS patients
  JOURNAL   Genomics 60 (2), 218-225 (1999)
   PUBMED   10486213
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083642.1.
            
            On Oct 23, 2004 this sequence version replaced XP_223541.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083642.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..739
                     /product="mitochondrial proton/calcium exchanger protein
                     precursor"
                     /note="LETM1 and EF-hand domain-containing protein 1,
                     mitochondrial; leucine zipper-EF-hand-containing
                     transmembrane protein 1; mitochondrial proton/calcium
                     exchanger protein; electroneutral mitochondrial
                     K(+)/H(+)exchanger"
                     /calculated_mol_wt=70764
     transit_peptide 1..114
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5XIN6.1)"
                     /calculated_mol_wt=12314
     mat_peptide     115..739
                     /product="Mitochondrial proton/calcium exchanger protein.
                     /id=PRO_0000017696"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIN6.1)"
                     /calculated_mol_wt=70764
     Region          190..421
                     /region_name="LETM1_RBD"
                     /note="LETM1-like, RBD; pfam07766"
                     /db_xref="CDD:462258"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PINK1.
                     /evidence=ECO:0000250|UniProtKB:O95202; propagated from
                     UniProtKB/Swiss-Prot (Q5XIN6.1)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIN6.1)"
     Site            596
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O95202; propagated from
                     UniProtKB/Swiss-Prot (Q5XIN6.1)"
     Region          717..739
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIN6.1)"
     CDS             1..739
                     /gene="Letm1"
                     /gene_synonym="KHE"
                     /coded_by="NM_001005884.1:200..2419"
                     /db_xref="GeneID:305457"
                     /db_xref="RGD:1359678"
ORIGIN      
        1 masillrscr grgparlasp raasprgslr draclsctrt vgltshesvl srcctpanpv
       61 ylyfksepls cwtqrpecqg tvaraawtpa sarlvvtgpq ylpvrgwhss splgedsmie
      121 kslkslkdkn kkleeggpvy sppaqvvvkk slgqkildel khyyhgfrll widtkiaarm
      181 lwrilnghtl trrerrqflr icadlfrlvp flvfvvvpfm efllpvvvkl fpnmlpstfe
      241 tqsikeerlk kelrvklela kflqdtieem alknkaakgn atkdfsaffq kiretgerps
      301 neeimrfskl fedeltldnl trpqlvalck llelqsigtn nflrfqltmr lrsikaddkl
      361 iseegvdslt vkelqaacra rgmralgvte drlkgqlkqw ldlhlyheip tsllilsram
      421 ylpdtlspad qlkstlqtlp eivakeaqvk aaevegeqvd nkakleatlq eeaaiqqehl
      481 eelkraaeta kdiqpevaea tvpgrpgael qpkmvdvipp seilkdtapv leglkgeeit
      541 keeidilsda csklkeqkks ltkekeelel lkedvqdyse dlqeikkels ktgdekyiee
      601 staskrlskr vqqmigqidg litqlettqq ngkldpaaas sptgesvisv delisamkqi
      661 khipehklis ltsaldenkd gniniddlvk vidlvnkedv qisttqvaei vatlekeekv
      721 eekekakeka ekeaaevkn
//
LOCUS       NP_112263                147 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D2B [Rattus norvegicus].
ACCESSION   NP_112263
VERSION     NP_112263.1
DBSOURCE    REFSEQ: accession NM_031001.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Tokumoto,M., Lee,J.Y., Fujiwara,Y., Uchiyama,M. and Satoh,M.
  TITLE     Inorganic arsenic induces apoptosis through downregulation of Ube2d
            genes and p53 accumulation in rat proximal tubular cells
  JOURNAL   J Toxicol Sci 38 (6), 815-820 (2013)
   PUBMED   24212999
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Zhang,L., Fairall,L., Goult,B.T., Calkin,A.C., Hong,C.,
            Millard,C.J., Tontonoz,P. and Schwabe,J.W.
  TITLE     The IDOL-UBE2D complex mediates sterol-dependent degradation of the
            LDL receptor
  JOURNAL   Genes Dev 25 (12), 1262-1274 (2011)
   PUBMED   21685362
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Tokumoto,M., Fujiwara,Y., Shimada,A., Hasegawa,T., Seko,Y.,
            Nagase,H. and Satoh,M.
  TITLE     Cadmium toxicity is caused by accumulation of p53 through the
            down-regulation of Ube2d family genes in vitro and in vivo
  JOURNAL   J Toxicol Sci 36 (2), 191-200 (2011)
   PUBMED   21467746
REFERENCE   4  (residues 1 to 147)
  AUTHORS   David,Y., Ziv,T., Admon,A. and Navon,A.
  TITLE     The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
            preferred lysines
  JOURNAL   J Biol Chem 285 (12), 8595-8604 (2010)
   PUBMED   20061386
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Lopez Salon,M., Morelli,L., Castano,E.M., Soto,E.F. and
            Pasquini,J.M.
  TITLE     Defective ubiquitination of cerebral proteins in Alzheimer's
            disease
  JOURNAL   J Neurosci Res 62 (2), 302-310 (2000)
   PUBMED   11020223
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Wing,S.S., Bedard,N., Morales,C., Hingamp,P. and Trasler,J.
  TITLE     A novel rat homolog of the Saccharomyces cerevisiae
            ubiquitin-conjugating enzymes UBC4 and UBC5 with distinct
            biochemical features is induced during spermatogenesis
  JOURNAL   Mol Cell Biol 16 (8), 4064-4072 (1996)
   PUBMED   8754804
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Wing,S.S. and Jain,P.
  TITLE     Molecular cloning, expression and characterization of a ubiquitin
            conjugation enzyme (E2(17)kB) highly expressed in rat testis
  JOURNAL   Biochem J 305 (Pt 1) (Pt 1), 125-132 (1995)
   PUBMED   7826319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078808.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC078808.1, U56407.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D2B"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-conjugating enzyme E2D 2; E2(17)KB 2B;
                     ubiquitin-protein ligase D2B; ubiquitin carrier protein
                     D2B; ubiquitin-conjugating enzyme E2-17 kDa 2B;
                     ubiquitin-conjugating enzyme E2(17)KB 2B; E2
                     ubiquitin-conjugating enzyme D2B; ubiquitin-conjugating
                     enzyme E2D 4 (putative)"
                     /calculated_mol_wt=16528
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="Ube2d2b"
                     /gene_synonym="RGD69425; Ube2d2; Ube2d4"
                     /coded_by="NM_031001.2:186..629"
                     /db_xref="GeneID:79435"
                     /db_xref="RGD:69425"
ORIGIN      
        1 malkrihkel ndlaqdppaq csagpvgedm fhwqatimgp ndspyqggaf fltidfptey
       61 pfkppkveft triyhpnvns ngsicldilr sqwspaltis kvllsissll cdpnpddplv
      121 peiaqiyktd rdkynrtare wtqkyam
//
LOCUS       NP_852048                561 aa            linear   ROD 28-APR-2025
DEFINITION  lengsin [Rattus norvegicus].
ACCESSION   NP_852048
VERSION     NP_852048.1
DBSOURCE    REFSEQ: accession NM_181383.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wyatt,K., Gao,C., Tsai,J.Y., Fariss,R.N., Ray,S. and Wistow,G.
  TITLE     A role for lengsin, a recruited enzyme, in terminal differentiation
            in the vertebrate lens
  JOURNAL   J Biol Chem 283 (10), 6607-6615 (2008)
   PUBMED   18178558
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY280501.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY280501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..561
                     /product="lengsin"
                     /note="glutamate-ammonia ligase domain-containing protein
                     1; glutamate-ammonia ligase (glutamine synthase) domain
                     containing 1; glutamate-ammonia ligase (glutamine
                     synthetase) domain containing 1"
                     /calculated_mol_wt=62138
     Region          1..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TT51.1)"
     Region          91..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TT51.1)"
     Region          138..223
                     /region_name="Gln-synt_N"
                     /note="Glutamine synthetase, beta-Grasp domain; pfam03951"
                     /db_xref="CDD:427610"
     Region          235..559
                     /region_name="Gln-synt_C"
                     /note="Glutamine synthetase, catalytic domain; pfam00120"
                     /db_xref="CDD:425473"
     CDS             1..561
                     /gene="Lgsn"
                     /gene_synonym="Gluld1; Lgs"
                     /coded_by="NM_181383.2:37..1722"
                     /db_xref="GeneID:316304"
                     /db_xref="RGD:727925"
ORIGIN      
        1 mndegdlaqe dttkdeanst egsrvnklkr trrkvtkphl csadgdeitm ansremsrnq
       61 tadlskpgsa eswswhnakd aqdqipvvks slpsagapda efnpntdhtr dnaqslilpq
      121 lssrmkhikq emaknhlqfv rfeatdlhgv srsksipaqf fqekvihgvf mprgylelmp
      181 npkdnevnhi ratcfnsdiv lmpelstfrv lpwaertarv icdtftvtge plltspryia
      241 krqlrqlqda gfsllsafiy dfcifgvpev insktisfpa stllsnhdqp fmqelvdgly
      301 htganvesfs sstrpgqmei cflpefgiss adnaftlrtg vqevarryny iaslvietgf
      361 cnsgilshsi wdvsgktnmf ysgsgverlt ltgkkwlagl lkhsaalscl mapavncrkr
      421 yckdsrdlkd svpttwgynd nscalnvkch gekgtqienk lgsatanpyl vlaatvaagl
      481 dglqssdgaa aesdesqdly qpepseiplk medalaaleq declkqalge tfiryfvamk
      541 kyeleneetd aegnkfleyf i
//
LOCUS       NP_001100220             660 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat transmembrane protein FLRT2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001100220 XP_001064239 XP_234361
VERSION     NP_001100220.1
DBSOURCE    REFSEQ: accession NM_001106750.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Hwang,H.J., Kang,D., Kim,J.R., Choi,J.H., Ryu,J.K., Herman,A.B.,
            Ko,Y.G., Park,H.J., Gorospe,M. and Lee,J.S.
  TITLE     FLRT2 prevents endothelial cell senescence and vascular aging by
            regulating the ITGB4/mTORC2/p53 signaling pathway
  JOURNAL   JCI Insight 9 (7), e172678 (2024)
   PUBMED   38587072
  REMARK    GeneRIF: FLRT2 prevents endothelial cell senescence and vascular
            aging by regulating the ITGB4/mTORC2/p53 signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Schroeder,A., Vanderlinden,J., Vints,K., Ribeiro,L.F.,
            Vennekens,K.M., Gounko,N.V., Wierda,K.D. and de Wit,J.
  TITLE     A Modular Organization of LRR Protein-Mediated Synaptic Adhesion
            Defines Synapse Identity
  JOURNAL   Neuron 99 (2), 329-344 (2018)
   PUBMED   29983322
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Yamagishi,S., Hampel,F., Hata,K., Del Toro,D., Schwark,M.,
            Kvachnina,E., Bastmeyer,M., Yamashita,T., Tarabykin,V., Klein,R.
            and Egea,J.
  TITLE     FLRT2 and FLRT3 act as repulsive guidance cues for Unc5-positive
            neurons
  JOURNAL   EMBO J 30 (14), 2920-2933 (2011)
   PUBMED   21673655
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Muller,P.S., Schulz,R., Maretto,S., Costello,I., Srinivas,S.,
            Bikoff,E. and Robertson,E.
  TITLE     The fibronectin leucine-rich repeat transmembrane protein Flrt2 is
            required in the epicardium to promote heart morphogenesis
  JOURNAL   Development 138 (7), 1297-1308 (2011)
   PUBMED   21350012
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Haines,B.P., Wheldon,L.M., Summerbell,D., Heath,J.K. and Rigby,P.W.
  TITLE     Regulated expression of FLRT genes implies a functional role in the
            regulation of FGF signalling during mouse development
  JOURNAL   Dev Biol 297 (1), 14-25 (2006)
   PUBMED   16872596
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473982.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234361.4, XP_001064239.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM117735.1, CB732320.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..660
                     /product="leucine-rich repeat transmembrane protein FLRT2
                     precursor"
                     /note="leucine-rich repeat transmembrane protein FLRT2;
                     fibronectin-like domain-containing leucine-rich
                     transmembrane protein 2"
                     /calculated_mol_wt=69930
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3962
     Region          35..62
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; pfam01462"
                     /db_xref="CDD:396168"
     mat_peptide     36..660
                     /product="Leucine-rich repeat transmembrane protein FLRT2.
                     /id=PRO_0000434524"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
                     /calculated_mol_wt=69930
     Region          50..>310
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          62..87
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          65..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          88..108
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          90..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          109..131
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          111..134
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          132..157
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          135..160
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          159..181
                     /region_name="LRR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          161..181
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..205
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          183..202
                     /region_name="LRR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          203..228
                     /region_name="LRR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          206..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          229..251
                     /region_name="LRR 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          232..253
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          252..274
                     /region_name="LRR 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          254..277
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          275..298
                     /region_name="LRR 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          278..301
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          282..>359
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          372..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     Region          426..494
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZTV3.1)"
     CDS             1..660
                     /gene="Flrt2"
                     /coded_by="NM_001106750.1:765..2747"
                     /db_xref="GeneID:299236"
                     /db_xref="RGD:1308574"
ORIGIN      
        1 mglqtakwps hgtfvlkfwl imslglyshv skllacpsvc rcdrnfvycn ersltsvplg
       61 ipegvtvlyl hnnqinnagf paelhnvqsv htvylygnql defpmnlpkn vrvlhlqenn
      121 iqtisraala qllkleelhl ddnsistvgv edgafreais lkllflsknh lssvpvglpv
      181 dlqelrvden riavisdmaf qnltslerli vdgnlltnkg iadgtfshlt klkefsivrn
      241 slshpppdlp gthlirlylq dnqinhiplt afanlrkler ldisnnqlrm ltqgvfdhls
      301 nlkqltarnn pwfcdcsikw vtewlkyips slnvrgfmcq gpeqvrgmav relnmnllsc
      361 ptttpglpvf tpapstvspt tqsptvsvps psrgsvppap apsklptipd wdgreratpp
      421 iseriqlsih fvndtsiqvs wlslftvmay kltwvkmghs lvggivqeri vsgekqhlsl
      481 vnleprstyr iclvpldafn yrtvedtics eatthasyln ngsntasshe qttshtmgsp
      541 fllagligga vifvlvvlls vfcwhmhkkg rytsqkwkyn rgrrkddyce agtkkdnsil
      601 emtetsfqiv slnndqllkg dfrlqpiytp ngginytdch ipnnmrycns svpdlehcht
//
LOCUS       NP_001164076            1312 aa            linear   ROD 28-APR-2025
DEFINITION  tetratricopeptide repeat protein 41 [Rattus norvegicus].
ACCESSION   NP_001164076 XP_001079794 XP_001080111
VERSION     NP_001164076.1
DBSOURCE    REFSEQ: accession NM_001170605.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1312)
  AUTHORS   van den Akker,E., Vankan-Berkhoudt,Y., Valk,P.J., Lowenberg,B. and
            Delwel,R.
  TITLE     The common viral insertion site Evi12 is located in the
            5'-noncoding region of Gnn, a novel gene with enhanced expression
            in two subclasses of human acute myeloid leukemia
  JOURNAL   J Virol 79 (9), 5249-5258 (2005)
   PUBMED   15827139
REFERENCE   2  (residues 1 to 1312)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before May 22, 2010 this sequence version replaced
            XP_001079794.1, XP_001080111.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643293.39230.1,
                                           SRR26643293.39226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1312
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..1312
                     /product="tetratricopeptide repeat protein 41"
                     /note="tetratricopeptide repeat protein GNN; Grp94
                     neighboring nucleotidase; TPR repeat protein GNN;
                     grp94-neighboring nucleotidase; TPR repeat protein 41;
                     first gene upstream of Nt5dc3"
                     /calculated_mol_wt=150679
     Region          334..>441
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     CDS             1..1312
                     /gene="Ttc41"
                     /gene_synonym="Gnn"
                     /coded_by="NM_001170605.1:1..3939"
                     /db_xref="GeneID:362863"
                     /db_xref="RGD:1302940"
ORIGIN      
        1 mieeaietaq rynsqpilkr qkpirpyics tidfqderdf laktifpqln dfcssrgtyf
       61 kavdlrwsal kahksftnnq frqysclhsq hlklcldyvn rcfpfficll gqtygdflpd
      121 ytpfllskvk dleslskgeq nlyvaakngy pwvlktpncs ltefeiiqaa frkksqfqff
      181 yfrtsnsllr tfseeeeeee eklssgyqvd rqgkvkvgkl kakiigkglp vrfyrdldel
      241 gdmvlkdwsa vveelypvtm imenidykhs fenlyheefv enckqvfvis kesnrtfeml
      301 erfaikdlel nsdstvagag ldsilrinsl ptcksilllc gergcgkstl ianwvddfks
      361 rhpgvlmvpy fvgstcescd imsvmhyfim elqhrangpq lemdflneds nvlvfsllie
      421 vfmaaislkp cilvldgiee lvgiygisgq kakdfswlpr slpphckfil ssvssslsck
      481 slcarpdvkt velnslgded tkfsifrqhl sapdqerfgq skpilrkkpn lnplkltlia
      541 selqecriyr nefqclreyl evasvqelwe lilkrwvedy swplkhkett vdnvisglsg
      601 wvvdvlcllc ishcglaede llqildmmgy rdhhkvtavh waafrnatkn wiqekpngll
      661 yfqhqslrna vehkmlgvti svresnpnvs qnstnhkkvh fhqvlmkyfq rqtifwrvyq
      721 elpwhmkmsg yweglcgfit spiitdfisk iqnpslwtrl hlvhywdvll eagsdvleaf
      781 llsaakieae dsqklkkrtt lsvlecslfe itaadkgrmi lfigsflklm gkineaeklf
      841 lsvedmllqs psmtemllka qnaigelyld igmmqkglty fqkawsnllr ftlsdlkisq
      901 elmkqkvkvm nnlaksasee flkenhvley atevskyvmd nprdqatmry tegvlmlasg
      961 naalaklkfq eclnirrrlf gnknilvgei mefladllff llgeneksqr kqaieyykqv
     1021 ikikekadsv atcklvrkql nislsdtlck lagqllsgdf chhatmeavs ylyrsldlra
     1081 ahlgpshasi egilhllrei qrsrgrrswp qgmnqlypeg sscgfslwen lpklnfhsaq
     1141 ssdtvntamc mnihrfqrak stepslvsdk akyfpgrgkk tltpilsmsa eekaqnsqir
     1201 nslrkqpprk kgvyplktys lidkngsvrl srqrvfsael gsgrslinsi yrqplrapls
     1261 adnpwksise lvsekwlfht phycftpqks vfprrsqiet kmlktshdfd ke
//
LOCUS       NP_001014164             461 aa            linear   ROD 28-APR-2025
DEFINITION  ufm1-specific protease 2 [Rattus norvegicus].
ACCESSION   NP_001014164 XP_341437
VERSION     NP_001014164.1
DBSOURCE    REFSEQ: accession NM_001014142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Yoo,H.M., Kang,S.H., Kim,J.Y., Lee,J.E., Seong,M.W., Lee,S.W.,
            Ka,S.H., Sou,Y.S., Komatsu,M., Tanaka,K., Lee,S.T., Noh,D.Y.,
            Baek,S.H., Jeon,Y.J. and Chung,C.H.
  TITLE     Modification of ASC1 by UFM1 is crucial for ERalpha transactivation
            and breast cancer development
  JOURNAL   Mol Cell 56 (2), 261-274 (2014)
   PUBMED   25219498
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Ha,B.H., Jeon,Y.J., Shin,S.C., Tatsumi,K., Komatsu,M., Tanaka,K.,
            Watson,C.M., Wallis,G., Chung,C.H. and Kim,E.E.
  TITLE     Structure of ubiquitin-fold modifier 1-specific protease UfSP2
  JOURNAL   J Biol Chem 286 (12), 10248-10257 (2011)
   PUBMED   21228277
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Kang,S.H., Kim,G.R., Seong,M., Baek,S.H., Seol,J.H., Bang,O.S.,
            Ovaa,H., Tatsumi,K., Komatsu,M., Tanaka,K. and Chung,C.H.
  TITLE     Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases,
            UfSP1 and UfSP2
  JOURNAL   J Biol Chem 282 (8), 5256-5262 (2007)
   PUBMED   17182609
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083771.1.
            
            On Apr 20, 2005 this sequence version replaced XP_341437.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083771.1, SRR8487226.17675.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..461
                     /product="ufm1-specific protease 2"
                     /EC_number="3.4.22.-"
                     /calculated_mol_wt=52176
     Region          272..453
                     /region_name="Peptidase_C78"
                     /note="Peptidase family C78; pfam07910"
                     /db_xref="CDD:400318"
     CDS             1..461
                     /gene="Ufsp2"
                     /gene_synonym="RGD1311161"
                     /coded_by="NM_001014142.1:63..1448"
                     /db_xref="GeneID:361151"
                     /db_xref="RGD:1311161"
ORIGIN      
        1 mdilfrirgg fdlafqlapp kemfiknalr qvlndlttkl ssdalvfric nssvylwpns
       61 dantgeltds sacksvvdli qfdqeedtkr kfmkkkdkkl tdmqqivnid lmleistplg
      121 avtpiieren eehhyinmsl pidavvsvap eetwgkvrkl lvdailnqlv dvekcilrym
      181 kgtsivvpep lhfllpggkn lvtvlypsgi pddqlqayrk elhdlfklph drpylkrina
      241 yhfpdelykd gyirnphayl sppniegsmi cmvqgtyayh hymqnrvddn gwgcayrslq
      301 tvcswfrhqg yteraipthr eiqqalvdag dkpatfvgsr qwigsievql vlnqligvts
      361 kilfvnqgse masqgrelan hfqnvgtpvm igggvlahti lgvawnettg qikflildph
      421 ytgaedlqvi lekgwcgwkg pdfwnkdayy nlclpqrpna l
//
LOCUS       NP_001094339             542 aa            linear   ROD 28-APR-2025
DEFINITION  cilia- and flagella-associated protein 157 [Rattus norvegicus].
ACCESSION   NP_001094339 XP_002726139 XP_575114
VERSION     NP_001094339.1
DBSOURCE    REFSEQ: accession NM_001100869.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Weidemann,M., Schuster-Gossler,K., Stauber,M., Wrede,C.,
            Hegermann,J., Ott,T., Boldt,K., Beyer,T., Serth,K., Kremmer,E.,
            Blum,M., Ueffing,M. and Gossler,A.
  TITLE     CFAP157 is a murine downstream effector of FOXJ1 that is
            specifically required for flagellum morphogenesis and sperm
            motility
  JOURNAL   Development 143 (24), 4736-4748 (2016)
   PUBMED   27965440
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098043.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_002726139.1, XP_575114.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..542
                     /product="cilia- and flagella-associated protein 157"
                     /note="uncharacterized protein C9orf117 homolog"
                     /calculated_mol_wt=62660
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7B0.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4V7B0.2)"
     Region          51..>361
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..542
                     /gene="Cfap157"
                     /coded_by="NM_001100869.1:23..1651"
                     /db_xref="GeneID:499781"
                     /db_xref="RGD:1560002"
ORIGIN      
        1 mapkkksnkg gkeiqskkki ggrkdtsgsk tpelamveel kefyhkqiqd ledrlaryqr
       61 kwdelavqek lfrqefeqla nnkkeivafl krtlnqrvde itdlndqlqs lqvakemekd
      121 afeaqlaqvr hefqetkdql ttenialgik lssleefrlq keeltekyma leeqlrrqeg
      181 eykdyvynle kksvldkdrl rkeiiqrvnl vatefrkvat nqmwettrra ilennnvtlq
      241 lskvskqgvq llqeneqlkg aqgklcqqle llentqeima kknignqkvi lmltekcrqq
      301 rkgteeaeql rlqlfqleqn ietlekanqt lrsekdqlde qlkeqraean rlqeeltkeq
      361 kirtnlktvl tqatsllrdi lqmrpetedg dfdvvfqlqr kellqqllvl lssavvskpq
      421 qdmgshqdkq paglskdsrl iaqtskqgaa sllqqlstit tyqpgdlglv prrlqvhipp
      481 kpqdlrplsc vtrmgicklq ntteiypsga lkrfkkftlp rpflhtgrps rcrkpdvapv
      541 pp
//
LOCUS       NP_001102946             154 aa            linear   ROD 28-APR-2025
DEFINITION  prefoldin subunit 2 [Rattus norvegicus].
ACCESSION   NP_001102946 XP_001061711 XP_001061762
VERSION     NP_001102946.1
DBSOURCE    REFSEQ: accession NM_001109476.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Djouder,N., Metzler,S.C., Schmidt,A., Wirbelauer,C., Gstaiger,M.,
            Aebersold,R., Hess,D. and Krek,W.
  TITLE     S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
            activates a negative feedback program that counters S6K1 survival
            signaling
  JOURNAL   Mol Cell 28 (1), 28-40 (2007)
   PUBMED   17936702
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Tsao,M.L., Chao,C.H. and Yeh,C.T.
  TITLE     Interaction of hepatitis C virus F protein with prefoldin 2
            perturbs tubulin cytoskeleton organization
  JOURNAL   Biochem Biophys Res Commun 348 (1), 271-277 (2006)
   PUBMED   16876117
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473985.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001061762.1, XP_001061711.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158649.1, CK366527.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..154
                     /product="prefoldin subunit 2"
                     /note="prefoldin 2"
                     /calculated_mol_wt=16449
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN18.1)"
     Region          25..124
                     /region_name="Prefoldin_2"
                     /note="prefoldin subunit 2; cd23163"
                     /db_xref="CDD:467479"
     Region          25..64
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467479"
     Site            order(26,30,33..34,37..38,40..41,44..45,48,102,105,109,
                     113,116..117,120..121,124)
                     /site_type="other"
                     /note="prefoldin beta subunit /TRiC interface [polypeptide
                     binding]"
                     /db_xref="CDD:467479"
     Site            order(57,60,64..65,68..74,76..81,85..86,90)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467479"
     Region          84..124
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467479"
     Region          126..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN18.1)"
     CDS             1..154
                     /gene="Pfdn2"
                     /coded_by="NM_001109476.1:11..475"
                     /db_xref="GeneID:685607"
                     /db_xref="RGD:1591406"
ORIGIN      
        1 madssgrvgk sggsgtgkga vsaeqviagf nrlrqeqrgl askaaeleme lnehslvidt
       61 lkevdetrkc yrmvggvlve rtvkevlpal egnkeqiqki ietlsqqlqa kgkelnefre
      121 khnirlmged ekpaakense gagaksssag vlvs
//
LOCUS       NP_036826                619 aa            linear   ROD 28-APR-2025
DEFINITION  sodium-dependent dopamine transporter [Rattus norvegicus].
ACCESSION   NP_036826
VERSION     NP_036826.1
DBSOURCE    REFSEQ: accession NM_012694.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Hynes,T., Fouyssac,M., Puaud,M., Joshi,D., Chernoff,C.,
            Stiebahl,S., Michaud,L. and Belin,D.
  TITLE     Pan-striatal reduction in the expression of the astrocytic dopamine
            transporter precedes the development of dorsolateral striatum
            dopamine-dependent incentive heroin seeking habits
  JOURNAL   Eur J Neurosci 59 (10), 2502-2521 (2024)
   PUBMED   38650303
  REMARK    GeneRIF: Pan-striatal reduction in the expression of the astrocytic
            dopamine transporter precedes the development of dorsolateral
            striatum dopamine-dependent incentive heroin seeking habits.
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Puzzo,C., D'Angio,R., Albanese,S., Orlando,D., Mangili,I.,
            Capobianco,M., Liberati,A.S. and Adriani,W.
  TITLE     Inheritance of wild and truncated DAT alleles from grand-parents:
            Opposite transgenerational consequences on the behavioral phenotype
            in adolescent DAT heterozygous rats
  JOURNAL   Neurosci Lett 810, 137352 (2023)
   PUBMED   37321389
  REMARK    GeneRIF: Inheritance of wild and truncated DAT alleles from
            grand-parents: Opposite transgenerational consequences on the
            behavioral phenotype in adolescent DAT heterozygous rats.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Vilca,S., Wahlestedt,C., Izenwasser,S., Gainetdinov,R.R. and
            Pardo,M.
  TITLE     Dopamine Transporter Knockout Rats Display Epigenetic Alterations
            in Response to Cocaine Exposure
  JOURNAL   Biomolecules 13 (7), 1107 (2023)
   PUBMED   37509143
  REMARK    GeneRIF: Dopamine Transporter Knockout Rats Display Epigenetic
            Alterations in Response to Cocaine Exposure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Hamamah,S., Hajnal,A. and Covasa,M.
  TITLE     Reduced Striatal Dopamine Transporter Availability and Heightened
            Response to Natural and Pharmacological Stimulation in
            CCK-1R-Deficient Obese Rats
  JOURNAL   Int J Mol Sci 24 (11), 9773 (2023)
   PUBMED   37298724
  REMARK    GeneRIF: Reduced Striatal Dopamine Transporter Availability and
            Heightened Response to Natural and Pharmacological Stimulation in
            CCK-1R-Deficient Obese Rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Shao,D., Jiang,D., Huang,Q., Ren,S., Li,J., Xiao,J., Guan,Y.,
            Lai,B., Zhao,J., Xie,F. and Hua,F.
  TITLE     Brain glucose metabolism and dopamine transporter changes in rats
            with morphine-induced conditioned place preference
  JOURNAL   Addict Biol 28 (5), e13277 (2023)
   PUBMED   37186440
  REMARK    GeneRIF: Brain glucose metabolism and dopamine transporter changes
            in rats with morphine-induced conditioned place preference.
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Gu,H., Wall,S.C. and Rudnick,G.
  TITLE     Stable expression of biogenic amine transporters reveals
            differences in inhibitor sensitivity, kinetics, and ion dependence
  JOURNAL   J Biol Chem 269 (10), 7124-7130 (1994)
   PUBMED   8125921
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Kitayama,S., Shimada,S., Xu,H., Markham,L., Donovan,D.M. and
            Uhl,G.R.
  TITLE     Dopamine transporter site-directed mutations differentially alter
            substrate transport and cocaine binding
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7782-7785 (1992)
   PUBMED   1502198
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Giros,B., el Mestikawy,S., Bertrand,L. and Caron,M.G.
  TITLE     Cloning and functional characterization of a cocaine-sensitive
            dopamine transporter
  JOURNAL   FEBS Lett 295 (1-3), 149-154 (1991)
   PUBMED   1765147
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Kilty,J.E., Lorang,D. and Amara,S.G.
  TITLE     Cloning and expression of a cocaine-sensitive rat dopamine
            transporter
  JOURNAL   Science 254 (5031), 578-579 (1991)
   PUBMED   1948035
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Shimada,S., Kitayama,S., Lin,C.L., Patel,A., Nanthakumar,E.,
            Gregor,P., Kuhar,M. and Uhl,G.
  TITLE     Cloning and expression of a cocaine-sensitive dopamine transporter
            complementary DNA
  JOURNAL   Science 254 (5031), 576-578 (1991)
   PUBMED   1948034
  REMARK    Erratum:[Science 1992 Mar 6;255(5049):1195]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M80233.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M80233.1, M80570.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760396 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..619
                     /product="sodium-dependent dopamine transporter"
                     /note="DAT; DA transporter; solute carrier family 6
                     (neurotransmitter transporter, dopamine), member 3; solute
                     carrier family 6 (neurotransmitter transporter), member 3"
                     /calculated_mol_wt=68615
     Site            57..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Region          60..613
                     /region_name="SLC6sbd_DAT1"
                     /note="Na(+)- and Cl(-)-dependent dopamine transporter 1;
                     solute-binding domain; cd11514"
                     /db_xref="CDD:212083"
     Site            order(75,78,417,420..421)
                     /site_type="other"
                     /note="Na binding site 2 [ion binding]"
                     /db_xref="CDD:212083"
     Site            order(76..77,79..82,156,319..320,325,327,421,424..425)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:212083"
     Site            order(77,82,320,352)
                     /site_type="other"
                     /note="Na binding site 1 [ion binding]"
                     /db_xref="CDD:212083"
     Site            order(84..85,155,159,162,386,390)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:212083"
     Site            96..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            105
                     /site_type="other"
                     /note="Contributes to high-affinity binding to cocaine.
                     /evidence=ECO:0000250|UniProtKB:Q61327; propagated from
                     UniProtKB/Swiss-Prot (P23977.1)"
     Site            128..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q01959; propagated from
                     UniProtKB/Swiss-Prot (P23977.1)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:Q01959; propagated from
                     UniProtKB/Swiss-Prot (P23977.1)"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23977.1)"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23977.1)"
     Site            236..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            256..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            306..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            335..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            400..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            442..465
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            466..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            516..541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Site            553..582
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     Region          560..589
                     /region_name="Interaction with TGFB1I1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P23977.1)"
     CDS             1..619
                     /gene="Slc6a3"
                     /gene_synonym="Dat1"
                     /coded_by="NM_012694.2:89..1948"
                     /db_xref="GeneID:24898"
                     /db_xref="RGD:3715"
ORIGIN      
        1 mskskcsvgp mssvvapake snavgpreve lilvkeqngv qltnstlinp pqtpveaqer
       61 etwskkidfl lsvigfavdl anvwrfpylc ykngggaflv pyllfmviag mplfymelal
      121 gqfnregaag vwkicpvlkg vgftvilisf yvgffynvii awalhyffss ftmdlpwihc
      181 nntwnspncs dahasnssdg lglndtfgtt paaeyfergv lhlhqsrgid dlgpprwqlt
      241 aclvlvivll yfslwkgvkt sgkvvwitat mpyvvltall lrgvtlpgam dgiraylsvd
      301 fyrlceasvw idaatqvcfs lgvgfgvlia fssynkftnn cyrdaiitts insltsfssg
      361 fvvfsflgym aqkhnvpird vatdgpglif iiypeaiatl plssawaavf flmlltlgid
      421 samggmesvi tglvdefqll hrhrelftlg ivlatfllsl fcvtnggiyv ftlldhfaag
      481 tsilfgvlie aigvawfygv qqfsddikqm tgqrpnlywr lcwklvspcf llyvvvvsiv
      541 tfrpphygay ifpdwanalg wiiatssmam vpiyatykfc slpgsfrekl ayaitpekdh
      601 qlvdrgevrq ftlrhwlll
//
LOCUS       NP_001037755             571 aa            linear   ROD 28-APR-2025
DEFINITION  la-related protein 7 [Rattus norvegicus].
ACCESSION   NP_001037755 XP_001076161
VERSION     NP_001037755.2
DBSOURCE    REFSEQ: accession NM_001044290.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Hasler,D., Meduri,R., Bak,M., Lehmann,G., Heizinger,L., Wang,X.,
            Li,Z.T., Sement,F.M., Bruckmann,A., Dock-Bregeon,A.C., Merkl,R.,
            Kalb,R., Grauer,E., Kunstmann,E., Zavolan,M., Liu,M.F., Fischer,U.
            and Meister,G.
  TITLE     The Alazami Syndrome-Associated Protein LARP7 Guides U6 Small
            Nuclear RNA Modification and Contributes to Splicing Robustness
  JOURNAL   Mol Cell 77 (5), 1014-1031 (2020)
   PUBMED   32017898
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Eichhorn,C.D., Yang,Y., Repeta,L. and Feigon,J.
  TITLE     Structural basis for recognition of human 7SK long noncoding RNA by
            the La-related protein Larp7
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6457-E6466 (2018)
   PUBMED   29946027
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Egloff,S., Vitali,P., Tellier,M., Raffel,R., Murphy,S. and Kiss,T.
  TITLE     The 7SK snRNP associates with the little elongation complex to
            promote snRNA gene expression
  JOURNAL   EMBO J 36 (7), 934-948 (2017)
   PUBMED   28254838
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Eichhorn,C.D., Chug,R. and Feigon,J.
  TITLE     hLARP7 C-terminal domain contains an xRRM that binds the 3' hairpin
            of 7SK RNA
  JOURNAL   Nucleic Acids Res 44 (20), 9977-9989 (2016)
   PUBMED   27679474
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Okamura,D., Maeda,I., Taniguchi,H., Tokitake,Y., Ikeda,M.,
            Ozato,K., Mise,N., Abe,K., Noce,T., Izpisua Belmonte,J.C. and
            Matsui,Y.
  TITLE     Cell cycle gene-specific control of transcription has a critical
            role in proliferation of primordial germ cells
  JOURNAL   Genes Dev 26 (22), 2477-2482 (2012)
   PUBMED   23154982
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Xue,Y., Yang,Z., Chen,R. and Zhou,Q.
  TITLE     A capping-independent function of MePCE in stabilizing 7SK snRNA
            and facilitating the assembly of 7SK snRNP
  JOURNAL   Nucleic Acids Res 38 (2), 360-369 (2010)
   PUBMED   19906723
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM031800.1 and BC083898.1.
            
            On Sep 30, 2011 this sequence version replaced NP_001037755.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083898.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..571
                     /product="la-related protein 7"
                     /note="La ribonucleoprotein domain family, member 7"
                     /calculated_mol_wt=64818
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Region          26..106
                     /region_name="LARP_7"
                     /note="La RNA-binding domain of La-related protein 7;
                     cd08032"
                     /db_xref="CDD:153401"
     Site            order(36,39..40,45,48..49,51,72..74)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153401"
     Region          121..200
                     /region_name="RRM1_LARP7"
                     /note="RNA recognition motif 1 (RRM1) found in La-related
                     protein 7 (LARP7) and similar proteins; cd12290"
                     /db_xref="CDD:409732"
     Region          181..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q05CL8; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q05CL8; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G0J3; propagated from
                     UniProtKB/Swiss-Prot (Q5XI01.2)"
     Region          411..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI01.2)"
     Region          443..524
                     /region_name="RRM2_LARP7"
                     /note="RNA recognition motif 2 in La-related protein 7
                     (LARP7) and similar proteins; cd12542"
                     /db_xref="CDD:409958"
     CDS             1..571
                     /gene="Larp7"
                     /coded_by="NM_001044290.2:112..1827"
                     /db_xref="GeneID:686883"
                     /db_xref="RGD:1592474"
ORIGIN      
        1 metenqktme estekrkeek kkrsrvkqvl adiakqvdfw fgdanlhkdr flreqieksr
       61 dgyvdisllv sfnkmkkltt dgkliaralk sssvveldle gtrirrkkpl gerpkdeeer
      121 tvyvellpkn vthswiervf gkcgnvvyis iphykstgdp kgfafvefet keqaakaief
      181 lnnppeeapr kpgifpktvk nkpipslrva eekkkkkkkk grikkeesvq akelvvdsss
      241 sgvskatkrp rtasegseae tpeapkqpak kkkkrdkvet gglpeskagk rerssaeded
      301 clpprpklkk raqkdgggpa asevskehrd lefcsteeek epgdrkgdsl skgkrkhkkk
      361 hkerhkmgee viplrvlskt ewmdlkkeyl alqkasmasl kktisqikle semeteskap
      421 pgsgqqcstq ekvsaqgpqf vtgvivkils edplpgrkqv kdilatisev vyidllegdt
      481 echarfktpe daqavmnaqt eikkkhswnl eilsgdheqr ywqkilvdrq aklnqprekk
      541 rgteklitka ekirlaktqq asqhirfsey d
//
LOCUS       NP_203501               1236 aa            linear   ROD 28-APR-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
            [Rattus norvegicus].
ACCESSION   NP_203501 XP_342006
VERSION     NP_203501.1
DBSOURCE    REFSEQ: accession NM_033350.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Wu,J., Zhang,C., Liu,C., Zhang,A., Li,A., Zhang,J. and Zhang,Y.
  TITLE     Aortic constriction induces hypertension and cardiac hypertrophy
            via (pro)renin receptor activation and the PLC-beta3 signaling
            pathway
  JOURNAL   Mol Med Rep 19 (1), 573-580 (2019)
   PUBMED   30431106
  REMARK    GeneRIF: High phospholipase C beta 3 expression is associated with
            hypertension and cardiac hypertrophy.
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Friedrich,B., Euler,P., Ziegler,R., Kuhn,A., Landwehrmeyer,B.G.,
            Luthi-Carter,R., Weiller,C., Hellwig,S. and Zucker,B.
  TITLE     Comparative analyses of Purkinje cell gene expression profiles
            reveal shared molecular abnormalities in models of different
            polyglutamine diseases
  JOURNAL   Brain Res 1481, 37-48 (2012)
   PUBMED   22917585
REFERENCE   4  (residues 1 to 1236)
  AUTHORS   Singal,T., Dhalla,N.S. and Tappia,P.S.
  TITLE     Reciprocal regulation of transcription factors and PLC isozyme gene
            expression in adult cardiomyocytes
  JOURNAL   J Cell Mol Med 14 (6B), 1824-1835 (2010)
   PUBMED   19538471
  REMARK    GeneRIF: Silencing of either c-Fos or c-Jun also depressed the
            norepinephrine-mediated increases in PLC beta(1), beta(3) and
            gamma(1) protein content and activity in an isozyme specific
            manner.
REFERENCE   5  (residues 1 to 1236)
  AUTHORS   Lyssand,J.S., DeFino,M.C., Tang,X.B., Hertz,A.L., Feller,D.B.,
            Wacker,J.L., Adams,M.E. and Hague,C.
  TITLE     Blood pressure is regulated by an alpha1D-adrenergic
            receptor/dystrophin signalosome
  JOURNAL   J Biol Chem 283 (27), 18792-18800 (2008)
   PUBMED   18468998
REFERENCE   6  (residues 1 to 1236)
  AUTHORS   Wang,S., Gebre-Medhin,S., Betsholtz,C., Stalberg,P., Zhou,Y.,
            Larsson,C., Weber,G., Feinstein,R., Oberg,K., Gobl,A. and
            Skogseid,B.
  TITLE     Targeted disruption of the mouse phospholipase C beta3 gene results
            in early embryonic lethality
  JOURNAL   FEBS Lett 441 (2), 261-265 (1998)
   PUBMED   9883896
REFERENCE   7  (residues 1 to 1236)
  AUTHORS   Ju,H., Zhao,S., Tappia,P.S., Panagia,V. and Dixon,I.M.
  TITLE     Expression of Gq alpha and PLC-beta in scar and border tissue in
            heart failure due to myocardial infarction
  JOURNAL   Circulation 97 (9), 892-899 (1998)
   PUBMED   9521338
REFERENCE   8  (residues 1 to 1236)
  AUTHORS   Kang,J.S., Lee,H.B., Rhee,S.G., Park,K. and Yoo,O.J.
  TITLE     The 5'-upstream region of the rat phospholipase C-beta 3 gene
            contains two critical Sp1 sites and an HIV Inr-like element
  JOURNAL   Gene 197 (1-2), 19-28 (1997)
   PUBMED   9332346
REFERENCE   9  (residues 1 to 1236)
  AUTHORS   Smrcka,A.V. and Sternweis,P.C.
  TITLE     Regulation of purified subtypes of phosphatidylinositol-specific
            phospholipase C beta by G protein alpha and beta gamma subunits
  JOURNAL   J Biol Chem 268 (13), 9667-9674 (1993)
   PUBMED   8387502
REFERENCE   10 (residues 1 to 1236)
  AUTHORS   Jhon,D.Y., Lee,H.H., Park,D., Lee,C.W., Lee,K.H., Yoo,O.J. and
            Rhee,S.G.
  TITLE     Cloning, sequencing, purification, and Gq-dependent activation of
            phospholipase C-beta 3
  JOURNAL   J Biol Chem 268 (9), 6654-6661 (1993)
   PUBMED   8454637
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ120508.1.
            
            On Aug 8, 2005 this sequence version replaced XP_342006.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ120507.1, DQ120508.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Rattus norvegicus"
                     /strain="SHR"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1236
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-3"
                     /EC_number="3.1.4.11"
                     /note="PLC-beta-3; phosphoinositide phospholipase
                     C-beta-3; phospholipase C, beta 3
                     (phosphatidylinositol-specific)"
                     /calculated_mol_wt=139538
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q01970; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Region          22..149
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(27,29,40,57,123)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(30,32,37,39,41,56..57)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          154..304
                     /region_name="EFh_PI-PLCbeta3"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 3 (PI-PLC-beta3); cd16210"
                     /db_xref="CDD:320040"
     Region          154..183
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320040"
     Region          187..216
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320040"
     Region          225..254
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320040"
     Site            257..263
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:320040"
     Region          271..304
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320040"
     Region          316..694
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Region          <318..834
                     /region_name="PLN02952"
                     /note="phosphoinositide phospholipase C"
                     /db_xref="CDD:178538"
     Site            order(332..333,362,364,379,413,466,468,620,647,649)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(332,379)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(333,362,364,413)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Region          467..588
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JE6.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01970; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01970; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01970; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Region          888..938
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JE6.2)"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01970; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Region          1032..1204
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q99JE6.2)"
     Region          1198..1236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JE6.2)"
     Region          1233..1236
                     /region_name="Interaction with SHANK2.
                     /evidence=ECO:0000269|PubMed:15632121"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99JE6.2)"
     CDS             1..1236
                     /gene="Plcb3"
                     /coded_by="NM_033350.1:13..3723"
                     /db_xref="GeneID:29322"
                     /db_xref="RGD:61993"
ORIGIN      
        1 magarpgvha lqlepptvve tlrrgskfik wdeeassrnl vtlrvdpngf flywtgpnme
       61 vdtldissir dtrtgryarl pkdpkirevl gfggpdtrle eklmtvvagp dpvnttflnf
      121 mavqddtvkv wseelfklam nilaqnasrn tflrkaytkl klqvnqdgri pvknilkmfs
      181 adkkrvetal escglnfnrs esirpdefsl eiferflnkl clrpdidkil leigakgkpy
      241 ltleqlmdfi nqkqrdprln evlypplrss qarlliekye pnkqflerdq msmegfsryl
      301 ggeengilpl ealdlsmdmt qplsayfins shntyltagq lagtssvemy rqallwgcrc
      361 veldvwkgrp peeepfithg ftmttevplr dvleaiaeta fktspypvil sfenhvdsak
      421 qqakmaeycr sifgeallid pldkyplsag tplpspqdlm grilvknkkr hrpstgvpds
      481 svrkrpleqs nsalsessaa tepsspqlgs pssdscpgls ngeevglekt slepqkslge
      541 eglnrgpnvl mpdrdredee edeeeeettd pkkpttdegt assevnatee mstlvnyvep
      601 vkfksfeaar krnkcfemss fvetkameql tkspmefvey nkqqlsriyp kgtrvdssny
      661 mpqlfwnvgc qlvalnfqtl dlpmqlnagv feyngrsgyl lkpefmrrpd ksfdpftevi
      721 vdgivanalr vkvisgqfls drkvgiyvev dmfglpvdtr rkyrtrtsqg nsfnpvwdee
      781 pfdfpkvvlp tlaslriaaf eeggrfvghr ilpvsairsg yhyvclrnea nqplclpall
      841 iyteasdyip ddhqdyaeal inpikhvslm dqrakqlaal igeseaqast emcqetpsqq
      901 qgsqlssnpa pnpldasprw ppgpttspts tslsspgqrd dliasilsev tptpleelrs
      961 hkamvklrsr qdrdlrelhk khqrkavalt rrlldglaqa raegkcrpss salsratnve
     1021 dvkeeekeaa rqyrefqnrq vqsllelrea qadaeterrl ehlkqaqqrl revvldahtt
     1081 qfkrlkelne rekkelqkil drkrnnsise aktrekhkke velteinrrh itesvnsirr
     1141 leeaqkqrhe rllagqqqvl qqlveeepkl vaqltqecqe qrerlpqeir rcllgetseg
     1201 lgdgplvaca snghaagsgg hqsgadsesq eentql
//
LOCUS       NP_037133                422 aa            linear   ROD 28-APR-2025
DEFINITION  paired box protein Pax-6 [Rattus norvegicus].
ACCESSION   NP_037133
VERSION     NP_037133.1
DBSOURCE    REFSEQ: accession NM_013001.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ma,R., Li,Y., Dong,X., Zhang,Y., Chen,X., Zhang,Y., Zou,H. and
            Wang,Y.
  TITLE     PAX6/CXCL14 regulatory axis promotes the repair of corneal injury
            by enhancing corneal epithelial cell proliferation
  JOURNAL   J Transl Med 22 (1), 458 (2024)
   PUBMED   38750454
  REMARK    GeneRIF: PAX6/CXCL14 regulatory axis promotes the repair of corneal
            injury by enhancing corneal epithelial cell proliferation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Ikeda,K., Onimaru,H., Inada,H., Tien Lin,S., Arata,S. and Osumi,N.
  TITLE     Structural and functional defects of the respiratory neural system
            in the medulla and spinal cord of Pax6 mutant rats
  JOURNAL   Brain Res Bull 152, 107-116 (2019)
   PUBMED   31301380
  REMARK    GeneRIF: Structural and functional defects of the respiratory
            neural system in the medulla and spinal cord of Pax6 mutant rats.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Mo,J.L., Liu,Q., Kou,Z.W., Wu,K.W., Yang,P., Chen,X.H. and Sun,F.Y.
  TITLE     MicroRNA-365 modulates astrocyte conversion into neuron in adult
            rat brain after stroke by targeting Pax6
  JOURNAL   Glia 66 (7), 1346-1362 (2018)
   PUBMED   29451327
  REMARK    GeneRIF: Results demonstrate that the miR-365-PAX6 system regulates
            the conversion of astrocytes into neurons in the ischemic brain.
            Both exogenous expression of PAX6 and administration of miR-365
            antagomir are likely to promote brain repair by enhancing
            neurogenesis in adult mammalian brain following ischemic injury.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Lipponen,A., El-Osta,A., Kaspi,A., Ziemann,M., Khurana,I., Kn,H.,
            Navarro-Ferrandis,V., Puhakka,N., Paananen,J. and Pitkanen,A.
  TITLE     Transcription factors Tp73, Cebpd, Pax6, and Spi1 rather than DNA
            methylation regulate chronic transcriptomics changes after
            experimental traumatic brain injury
  JOURNAL   Acta Neuropathol Commun 6 (1), 17 (2018)
   PUBMED   29482641
  REMARK    GeneRIF: Four upregulated transcription factors Pax6, Tp73, Cebpd,
            and Spi1, appeared as potent regulators of chronic post-traumatic
            brain injury (TBI) gene expression. They regulate molecular
            networks contributing to post-injury secondary damage, including
            apoptosis and inflammation, strengthening the feasibility of
            therapeutically targeting these molecular networks even after the
            acute post-TBI period.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   So,K., Chung,Y., Yu,S.K. and Jun,Y.
  TITLE     Regional Immunoreactivity of Pax6 in the Neurogenic Zone After
            Chronic Prenatal Hypoxia
  JOURNAL   In Vivo 31 (6), 1125-1129 (2017)
   PUBMED   29102934
  REMARK    GeneRIF: These results suggest that Pax6 immunoreactivity showed
            diverse patterns in the neurogenic zone after prenatal hypoxia and
            Pax6 has important effects on neurogenesis
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Osumi-Yamashita,N., Kuratani,S., Ninomiya,Y., Aoki,K., Iseki,S.,
            Chareonvit,S., Doi,H., Fujiwara,M., Watanabe,T. and Eto,K.
  TITLE     Cranial anomaly of homozygous rSey rat is associated with a defect
            in the migration pathway of midbrain crest cells
  JOURNAL   Dev Growth Differ 39 (1), 53-67 (1997)
   PUBMED   9079035
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Mirzayans,F., Pearce,W.G., MacDonald,I.M. and Walter,M.A.
  TITLE     Mutation of the PAX6 gene in patients with autosomal dominant
            keratitis
  JOURNAL   Am J Hum Genet 57 (3), 539-548 (1995)
   PUBMED   7668281
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Martha,A., Strong,L.C., Ferrell,R.E. and Saunders,G.F.
  TITLE     Three novel aniridia mutations in the human PAX6 gene
  JOURNAL   Hum Mutat 6 (1), 44-49 (1995)
   PUBMED   7550230
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Matsuo,T., Osumi-Yamashita,N., Noji,S., Ohuchi,H., Koyama,E.,
            Myokai,F., Matsuo,N., Taniguchi,S., Doi,H., Iseki,S. et al.
  TITLE     A mutation in the Pax-6 gene in rat small eye is associated with
            impaired migration of midbrain crest cells
  JOURNAL   Nat Genet 3 (4), 299-304 (1993)
   PUBMED   7981749
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Favor,J.
  TITLE     A comparison of the dominant cataract and recessive specific-locus
            mutation rates induced by treatment of male mice with
            ethylnitrosourea
  JOURNAL   Mutat Res 110 (2), 367-382 (1983)
   PUBMED   6877261
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128741.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128741.1, U69644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q33"
     Protein         1..422
                     /product="paired box protein Pax-6"
                     /note="paired box homeotic gene 6; oculorhombin; paired
                     box gene 6"
                     /calculated_mol_wt=46624
     Region          4..128
                     /region_name="PAX"
                     /note="Paired Box domain; smart00351"
                     /db_xref="CDD:128645"
     Region          7..63
                     /region_name="PAI subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00381"
                     /note="propagated from UniProtKB/Swiss-Prot (P63016.1)"
     Site            order(9..10,15,17..19,21,26,38,40,49,52,54..55,59,68..74,
                     76..79,98..100,119,121..122,125,128)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238076"
     Region          82..130
                     /region_name="RED subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00381"
                     /note="propagated from UniProtKB/Swiss-Prot (P63016.1)"
     Region          157..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63016.1)"
     Region          212..267
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          269..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63016.1)"
     Region          345..422
                     /region_name="Required for suppression of NFATC1-mediated
                     transcription. /evidence=ECO:0000250|UniProtKB:P63015"
                     /note="propagated from UniProtKB/Swiss-Prot (P63016.1)"
     CDS             1..422
                     /gene="Pax6"
                     /coded_by="NM_013001.2:161..1429"
                     /db_xref="GeneID:25509"
                     /db_xref="RGD:3258"
ORIGIN      
        1 mqnshsgvnq lggvfvngrp lpdstrqkiv elahsgarpc disrilqvsn gcvskilgry
       61 yetgsirpra iggskprvat pevvskiaqy krecpsifaw eirdrllseg vctndnipsv
      121 ssinrvlrnl asekqqmgad gmydklrmln gqtgswgtrp gwypgtsvpg qptqdgcqqq
      181 egqgentnsi ssngedsdea qmrlqlkrkl qrnrtsftqe qiealekefe rthypdvfar
      241 erlaakidlp eariqvwfsn rrakwrreek lrnqrrqasn tpshipisss fstsvyqpip
      301 qpttpvssft sgsmlgrtdt altntysalp pmpsftmann lpmqppvpsq tssyscmlpt
      361 spsvngrsyd tytpphmqth mnsqpmgtsg ttstglispg vsvpvqvpgs epdmsqywpr
      421 lq
//
LOCUS       NP_062090               2461 aa            linear   ROD 28-APR-2025
DEFINITION  microtubule-associated protein 1B [Rattus norvegicus].
ACCESSION   NP_062090 XP_001061557 XP_215469
VERSION     NP_062090.1
DBSOURCE    REFSEQ: accession NM_019217.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2461)
  AUTHORS   Sole,L., Wagnon,J.L., Akin,E.J., Meisler,M.H. and Tamkun,M.M.
  TITLE     The MAP1B Binding Domain of Nav1.6 Is Required for Stable
            Expression at the Axon Initial Segment
  JOURNAL   J Neurosci 39 (22), 4238-4251 (2019)
   PUBMED   30914445
  REMARK    GeneRIF: This work confirms a new biological role of MAP1B in the
            regulation of sodium channel localization
REFERENCE   2  (residues 1 to 2461)
  AUTHORS   Palenzuela,R., Gutierrez,Y., Draffin,J.E., Lario,A., Benoist,M. and
            Esteban,J.A.
  TITLE     MAP1B Light Chain Modulates Synaptic Transmission via AMPA Receptor
            Intracellular Trapping
  JOURNAL   J Neurosci 37 (41), 9945-9963 (2017)
   PUBMED   28904092
  REMARK    GeneRIF: MAP1B restricts the access of AMPARs to dendritic spines
            and the postsynaptic membrane, contributing to downregulating
            synaptic transmission
REFERENCE   3  (residues 1 to 2461)
  AUTHORS   Tortosa,E., Adolfs,Y., Fukata,M., Pasterkamp,R.J., Kapitein,L.C.
            and Hoogenraad,C.C.
  TITLE     Dynamic Palmitoylation Targets MAP6 to the Axon to Promote
            Microtubule Stabilization during Neuronal Polarization
  JOURNAL   Neuron 94 (4), 809-825 (2017)
   PUBMED   28521134
REFERENCE   4  (residues 1 to 2461)
  AUTHORS   Gumy,L.F., Katrukha,E.A., Grigoriev,I., Jaarsma,D., Kapitein,L.C.,
            Akhmanova,A. and Hoogenraad,C.C.
  TITLE     MAP2 Defines a Pre-axonal Filtering Zone to Regulate KIF1- versus
            KIF5-Dependent Cargo Transport in Sensory Neurons
  JOURNAL   Neuron 94 (2), 347-362 (2017)
   PUBMED   28426968
REFERENCE   5  (residues 1 to 2461)
  AUTHORS   Liu,Y., Lee,J.W. and Ackerman,S.L.
  TITLE     Mutations in the microtubule-associated protein 1A (Map1a) gene
            cause Purkinje cell degeneration
  JOURNAL   J Neurosci 35 (11), 4587-4598 (2015)
   PUBMED   25788676
REFERENCE   6  (residues 1 to 2461)
  AUTHORS   Fawcett,J.W., Mathews,G., Housden,E., Goedert,M. and Matus,A.
  TITLE     Regenerating sciatic nerve axons contain the adult rather than the
            embryonic pattern of microtubule associated proteins
  JOURNAL   Neuroscience 61 (4), 789-804 (1994)
   PUBMED   7838378
REFERENCE   7  (residues 1 to 2461)
  AUTHORS   Zauner,W., Kratz,J., Staunton,J., Feick,P. and Wiche,G.
  TITLE     Identification of two distinct microtubule binding domains on
            recombinant rat MAP 1B
  JOURNAL   Eur J Cell Biol 57 (1), 66-74 (1992)
   PUBMED   1639092
REFERENCE   8  (residues 1 to 2461)
  AUTHORS   Rienitz,A., Grenningloh,G., Hermans-Borgmeyer,I., Kirsch,J.,
            Littauer,U.Z., Prior,P., Gundelfinger,E.D., Schmitt,B. and Betz,H.
  TITLE     Neuraxin, a novel putative structural protein of the rat central
            nervous system that is immunologically related to
            microtubule-associated protein 5
  JOURNAL   EMBO J 8 (10), 2879-2888 (1989)
   PUBMED   2555150
REFERENCE   9  (residues 1 to 2461)
  AUTHORS   Schoenfeld,T.A., McKerracher,L., Obar,R. and Vallee,R.B.
  TITLE     MAP 1A and MAP 1B are structurally related microtubule associated
            proteins with distinct developmental patterns in the CNS
  JOURNAL   J Neurosci 9 (5), 1712-1730 (1989)
   PUBMED   2470876
REFERENCE   10 (residues 1 to 2461)
  AUTHORS   Benjamin,S., Cambray-Deakin,M.A. and Burgoyne,R.D.
  TITLE     Effect of hypothyroidism on the expression of three
            microtubule-associated proteins (1A, 1B and 2) in developing rat
            cerebellum
  JOURNAL   Neuroscience 27 (3), 931-939 (1988)
   PUBMED   3252178
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CB610210.1,
            X60370.1, BF286433.1, CF977184.1, BG665276.1, CB579120.1,
            CB583564.1, BG378086.1, CB810012.1, CB584802.1, CA510735.1,
            CB580055.1, CA510940.1, CO393350.1, CB576609.1, AA925503.1 and
            CA503854.1.
            
            On or before Oct 28, 2007 this sequence version replaced
            XP_215469.2, XP_001061557.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN14984024
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..2461
                     /product="microtubule-associated protein 1B"
                     /note="MAP-1B; neuraxin"
                     /calculated_mol_wt=269545
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          522..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          <531..1158
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          856..1154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            941
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            956
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            963
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1009
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1175..1277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1274
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1299..1749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1518
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          <1543..1875
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            1611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1646
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1762..1819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1781
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1789
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1843..1884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1871..1887
                     /region_name="MAP1B 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1874
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1888..1904
                     /region_name="MAP1B 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          1905..1921
                     /region_name="MAP1B 3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1921..1969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            1925
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            1942
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          1956..1972
                     /region_name="MAP1B 6. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          1990..2006
                     /region_name="MAP1B 7. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          2007..2023
                     /region_name="MAP1B 8. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          2009..2029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          2024..2040
                     /region_name="MAP1B 9. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            2027
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          2041..2057
                     /region_name="MAP1B 10. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          2045..2071
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            2057
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          2087..2343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Region          <2095..2348
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            2264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            2282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Region          2287..2459
                     /region_name="Mediates interaction with TMEM185A.
                     /evidence=ECO:0000250|UniProtKB:P46821"
                     /note="propagated from UniProtKB/Swiss-Prot (P15205.3)"
     Site            2298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P46821; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     Site            2407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14873; propagated from
                     UniProtKB/Swiss-Prot (P15205.3)"
     CDS             1..2461
                     /gene="Map1b"
                     /gene_synonym="Mtap1b"
                     /coded_by="NM_019217.1:165..7550"
                     /db_xref="GeneID:29456"
                     /db_xref="RGD:3043"
ORIGIN      
        1 matvvveate pepsgsignp aattspslsh rfldskfyll vvvgetvtee hlrraignie
       61 lgirswdtnl iecnldqelk lfvsrhsarf spevpgqkil hhrsdvletv vlinpsdeav
      121 stevrlmitd aarhkllvlt gqcfentgel ilqsgsfsfq nfieiftdqe igellstthp
      181 ankasltlfc peegdwknsn ldrhnlqdfi niklnsasil pemeglseft eylsesvevp
      241 spfdileppt sggflklskp ccyifpggrg dsalfavngf nmlinggser kscfwklirh
      301 ldrvdsillt higddnlpgi nsmlqrkiae leeersqgst snsdwmknli spdlgvvfln
      361 vpenlknpep nikmkrstee acftlqylnk lsmkpeplfr svgnaiepvi lfqkmgvgkl
      421 emyvlnpvks skemqyfmqq wtgtnkdkae lilpngqevd ipisyltsvs slivwhpanp
      481 aekiirvlfp gnstqynile gleklkhldf lkqplatqkd ltgqvstppv kqvklkqrad
      541 sreslkpatk plssksvrke skeeapeatk asqvektpkv eskekvivkk dkpgkveskp
      601 svtekevpsk eeqspvkaev aekaateskp kvtkdkvvkk eiktkpeekk eekpkkevak
      661 kedktplkkd ekpkkeeakk eikkeikkee kkelkkevkk etplkdakke vkkdekkevk
      721 keekepkkei kkiskdikks tplsdtkkpa alkpkvakke eptkkepiaa gklkdkgkvk
      781 vikkegktte aaatavgtaa vaaaagvaas gpakeleaer slmsspedlt kdfeelkaee
      841 idvakdikpq leliedeekl ketepgeayv iqketevskg saespdegit ttegegeceq
      901 tpeelepvek qgvddiekfe degagfeess eagdyeekae teeaeepeed gednvsgsas
      961 khsptedeei akaeadvhik ekresvasgd draeedmdea lekgeaeqse eegeeeedka
     1021 edareedhep dkteaedyvm avvdkaaeag vtedqydflg tpakqpgvqs psrepassih
     1081 detlpggses eatasdeenr edqpeeftat sgytqstiei sseptpmdem stprdvmtde
     1141 tnneetesps qefvnitkye sslysqeysk pvvasfngls dgsktdatdg rdynasasti
     1201 sppssmeedk fsksalrday rpeetdvktg aeldikdvsd erlspaksps lspsppspie
     1261 ktplgersvn fsltpneika saegeatavv spgvtqavve ehcaspeekt levvspsqsv
     1321 tgsaghtpyy qsptdekssh lptevtenaq avpvsfefte akdenerssi spmdepvpds
     1381 espiekvlsp lrsppligse sayedflsad dkalgrrses pfegkngkqg fsdkespvsd
     1441 ltsdlyqdkq eeksagfipi kedfspekka sdaeimssqs alalderklg gdgsptqvdv
     1501 sqfgsfkedt kmsisegtvs dksatpvdeg vaedtyshme gvasvstasv atssfpeptt
     1561 ddvspslhae vgsphstevd dslsvsvvqt pttfqetems pskeecprpm sisppdfspk
     1621 taksrtpvqd hrseqssmsi efgqespehs lamdfsrqsp dhptvgagml hitengptev
     1681 dyspsdiqds slshkippte epsytqdndl selisvsqve aspstssaht psqiasplqe
     1741 dtlsdvvppr dmslyaslas ekvqslegek lspksdispl tpressptys pgfsdstsga
     1801 kestaayqts ssppidaaaa epygfrssml fdtmqhhlal srdlttssve kdnggktpgd
     1861 fnyayqkpes ttespdeedy dyeshektiq ahdvggyyye ktertikspc dsgysyetie
     1921 kttktpedgg ysceitektt rtpeeggysy eisekttrtp evsgytyekt ersrrllddi
     1981 sngyddtedg ghtlgdcsys yettekitsf pesesysyet ttkttrspdt saycyetmek
     2041 itktpqasty syetsdrcyt perkspsear qdvdlclvss cefkhpktel spsfinpnpl
     2101 ewfageepte esekpltqsg gapppsggkq qgrqcdetpp tsvsesapsq tdsdvppete
     2161 ecpsitadan idsedeseti ptdktvtykh mdpppapmqd rspsprhpdv smvdpealai
     2221 eqnlgkalkk dlkekaktkk pgtktksssp vkkgdgkskp saaspkpgal kessdkvsrv
     2281 aspkkkesve kamkttttpe vkatrgeekd ketknaanas asksvktata gpgttktaks
     2341 stvppglpvy ldlcyipnhs nsknvdveff krvrssyyvv sgndpaaeep sravldalle
     2401 gkaqwgsnmq vtlipthdse vmrewyqeth ekqqdlnimv lassstvvmq desfpackie
     2461 l
//
LOCUS       NP_067710                 79 aa            linear   ROD 28-APR-2025
DEFINITION  calcium/calmodulin-dependent protein kinase II inhibitor 2 [Rattus
            norvegicus].
ACCESSION   NP_067710
VERSION     NP_067710.1
DBSOURCE    REFSEQ: accession NM_021678.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Jain,S.S., Paglialunga,S., Vigna,C., Ludzki,A., Herbst,E.A.,
            Lally,J.S., Schrauwen,P., Hoeks,J., Tupling,A.R., Bonen,A. and
            Holloway,G.P.
  TITLE     High-fat diet-induced mitochondrial biogenesis is regulated by
            mitochondrial-derived reactive oxygen species activation of CaMKII
  JOURNAL   Diabetes 63 (6), 1907-1913 (2014)
   PUBMED   24520120
  REMARK    GeneRIF: High-fat diet-induced mitochondrial biogenesis is
            regulated by mitochondrial-derived reactive oxygen species
            activation of CaMKII
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Joiner,M.L., Koval,O.M., Li,J., He,B.J., Allamargot,C., Gao,Z.,
            Luczak,E.D., Hall,D.D., Fink,B.D., Chen,B., Yang,J., Moore,S.A.,
            Scholz,T.D., Strack,S., Mohler,P.J., Sivitz,W.I., Song,L.S. and
            Anderson,M.E.
  TITLE     CaMKII determines mitochondrial stress responses in heart
  JOURNAL   Nature 491 (7423), 269-273 (2012)
   PUBMED   23051746
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Lucchesi,W., Mizuno,K. and Giese,K.P.
  TITLE     Novel insights into CaMKII function and regulation during memory
            formation
  JOURNAL   Brain Res Bull 85 (1-2), 2-8 (2011)
   PUBMED   21070840
  REMARK    Review article
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Skelding,K.A., Rostas,J.A. and Verrills,N.M.
  TITLE     Controlling the cell cycle: the role of
            calcium/calmodulin-stimulated protein kinases I and II
  JOURNAL   Cell Cycle 10 (4), 631-639 (2011)
   PUBMED   21301225
  REMARK    Review article
REFERENCE   5  (residues 1 to 79)
  AUTHORS   Chang,B.H., Mukherji,S. and Soderling,T.R.
  TITLE     Characterization of a calmodulin kinase II inhibitor protein in
            brain
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10890-10895 (1998)
   PUBMED   9724800
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF041854.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF041854.1, BP482874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..79
                     /product="calcium/calmodulin-dependent protein kinase II
                     inhibitor 2"
                     /note="caM-KIIN; caM-KIINbeta; CaM-KII inhibitory protein"
                     /calculated_mol_wt=8497
     Region          1..79
                     /region_name="CaM-KIIN"
                     /note="Calcium/calmodulin-dependent protein kinase II
                     inhibitor; pfam15170"
                     /db_xref="CDD:373618"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2N6.1)"
     Region          43..69
                     /region_name="Inhibitory domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z2N6.1)"
     CDS             1..79
                     /gene="Camk2n2"
                     /coded_by="NM_021678.1:86..325"
                     /db_xref="GeneID:59314"
                     /db_xref="RGD:708411"
ORIGIN      
        1 mseilpyged kmgrfgadpe gsdlsfscrl qdtnsffagn qakrppklgq igrakrvvie
       61 ddriddvlkg mgekppsgv
//
LOCUS       NP_001101051            1872 aa            linear   ROD 28-APR-2025
DEFINITION  plexin-A3 precursor [Rattus norvegicus].
ACCESSION   NP_001101051 XP_001055498 XP_219723
VERSION     NP_001101051.2
DBSOURCE    REFSEQ: accession NM_001107581.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1872)
  AUTHORS   Xiang,X., Zhang,X. and Huang,Q.L.
  TITLE     Plexin A3 is involved in semaphorin 3F-mediated oligodendrocyte
            precursor cell migration
  JOURNAL   Neurosci Lett 530 (2), 127-132 (2012)
   PUBMED   23063687
  REMARK    GeneRIF: These results suggest that plexin A3 is expressed in OPCs
            and immature oligodendrocytes and is involved in OPC migration.
REFERENCE   2  (residues 1 to 1872)
  AUTHORS   Matsuoka,R.L., Chivatakarn,O., Badea,T.C., Samuels,I.S., Cahill,H.,
            Katayama,K., Kumar,S.R., Suto,F., Chedotal,A., Peachey,N.S.,
            Nathans,J., Yoshida,Y., Giger,R.J. and Kolodkin,A.L.
  TITLE     Class 5 transmembrane semaphorins control selective Mammalian
            retinal lamination and function
  JOURNAL   Neuron 71 (3), 460-473 (2011)
   PUBMED   21835343
REFERENCE   3  (residues 1 to 1872)
  AUTHORS   He,H., Yang,T., Terman,J.R. and Zhang,X.
  TITLE     Crystal structure of the plexin A3 intracellular region reveals an
            autoinhibited conformation through active site sequestration
  JOURNAL   Proc Natl Acad Sci U S A 106 (37), 15610-15615 (2009)
   PUBMED   19717441
REFERENCE   4  (residues 1 to 1872)
  AUTHORS   Schwarz,Q., Waimey,K.E., Golding,M., Takamatsu,H., Kumanogoh,A.,
            Fujisawa,H., Cheng,H.J. and Ruhrberg,C.
  TITLE     Plexin A3 and plexin A4 convey semaphorin signals during facial
            nerve development
  JOURNAL   Dev Biol 324 (1), 1-9 (2008)
   PUBMED   18804103
REFERENCE   5  (residues 1 to 1872)
  AUTHORS   Cheng,H.J., Bagri,A., Yaron,A., Stein,E., Pleasure,S.J. and
            Tessier-Lavigne,M.
  TITLE     Plexin-A3 mediates semaphorin signaling and regulates the
            development of hippocampal axonal projections
  JOURNAL   Neuron 32 (2), 249-263 (2001)
   PUBMED   11683995
REFERENCE   6  (residues 1 to 1872)
  AUTHORS   Strolin Benedetti,M., Goldaniga,G., Montesanti,L., Battaglia,R. and
            Vicario,G.
  TITLE     Disposition of 14C-labelled FCE 22101 in animals
  JOURNAL   J Antimicrob Chemother 23 Suppl C, 165-171 (1989)
   PUBMED   2732138
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AC094668.10.
            
            On Jan 9, 2008 this sequence version replaced NP_001101051.1.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data because no single transcript was available for the full length
            of the gene. The extent of this transcript is supported by
            orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132270 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1872
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..1872
                     /product="plexin-A3 precursor"
                     /note="Plexin 4, SEX, homolog to the cMet/HGF receptors"
                     /calculated_mol_wt=205966
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZPX4.1)"
                     /calculated_mol_wt=2036
     mat_peptide     20..1872
                     /product="Plexin-A3. /id=PRO_0000411105"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZPX4.1)"
                     /calculated_mol_wt=205966
     Region          22..490
                     /region_name="Sema_plexin_A3"
                     /note="The Sema domain, a protein interacting module, of
                     Plexin A3; cd11273"
                     /db_xref="CDD:200534"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZPX4.1)"
     Site            order(77,79..80,139,176..178,204..206,213..215,369,372,
                     374,377..381,391..392,394)
                     /site_type="other"
                     /note="putative Semaphorin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:200534"
     Region          491..>528
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          547..637
                     /region_name="TIG_plexin"
                     /note="TIG domain; pfam17960"
                     /db_xref="CDD:465588"
     Site            549
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZPX4.1)"
     Region          638..685
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          691..785
                     /region_name="TIG_2"
                     /note="TIG domain found in plexin; pfam18020"
                     /db_xref="CDD:465619"
     Region          789..838
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          841..935
                     /region_name="IPT_plexin_repeat1"
                     /note="First repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01180"
                     /db_xref="CDD:238585"
     Region          936..1022
                     /region_name="IPT_plexin_repeat2"
                     /note="Second repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01179"
                     /db_xref="CDD:238584"
     Region          1024..1124
                     /region_name="IPT_plexin_repeat3"
                     /note="Third repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01181"
                     /db_xref="CDD:238586"
     Region          1126..1209
                     /region_name="IPT_PCSR"
                     /note="IPT domain of Plexins and Cell Surface Receptors
                     (PCSR) and related proteins . This subgroup contains IPT
                     domains of plexins, receptors, like the
                     plasminogen-related growth factor receptors, the
                     hepatocyte growth factor-scatter factors, and the...;
                     cd00603"
                     /db_xref="CDD:238337"
     Site            1163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZPX4.1)"
     Site            1221..1241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZPX4.1)"
     Region          1294..1837
                     /region_name="Plexin_cytopl"
                     /note="Plexin cytoplasmic RasGAP domain; pfam08337"
                     /db_xref="CDD:462434"
     Site            1597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51805; propagated from
                     UniProtKB/Swiss-Prot (D3ZPX4.1)"
     CDS             1..1872
                     /gene="Plxna3"
                     /gene_synonym="Plxn4; SEX"
                     /coded_by="NM_001107581.2:174..5792"
                     /db_xref="GeneID:309280"
                     /db_xref="RGD:1584973"
ORIGIN      
        1 mhtvcllpll fftiggclgs srpfrtfvvt dttlthlavh rvtgevfvga vnrvfklasn
       61 ltelrahvtg piednarcyp ppsmrvcshr lvpvdnvnkl llidyaarrl vacgsiwqgi
      121 cqflrlddlf klgephhrke hylsgaqepd smagviveqg qgpsklfvgt avdgkseyfp
      181 tlssrklidd edsgdmfslv yqdefvssqi kipsdtlsly pafdiyyiyg fvsasfvyfl
      241 tlqldtqqtl ldtagekfft skivrmcagd sefysyvefp igcswrgvey rlvqsahlak
      301 pglllaqalg vpadedvlft ifsqgqknra npprqtilcl ftlssinahi rrriqscyrg
      361 egtlalpwll nkelpcintp mqingnfcgl vlnqplgglh vieglpllad stdgmasvaa
      421 ytyhqhsvvf igtrsgnlkk vrvdgsqdaq lyetvsvvqg tpilrdllfs pdhrhiylls
      481 ekqvsqlpve tceqylscaa clgsgdphcg wcvlqhrccr egacpgasap hgfaeelnkc
      541 iqvrvrpnnv svtssgvqlt vamrnvpdls lgvscsfeev teseaillps gelrcpspsl
      601 qelqtltrgh gathtvrlql lsmetgvrfa gvdfvfyncs alqscmscvg spypchwcky
      661 rhvctshphe csfqegrvhs pegcpeilpr gdllipvgvm qpltlraknl pqpqsgqkny
      721 ecvvrvqgrq hrvpavrfns ssvqcqnasy fyegdefgdt eldfsvvwdg dfpidkppsf
      781 rallykcwaq rpscglclka dprfncgwci sehrcqlrvh cpapksnwmh psqkgarcsh
      841 pritqihplt gpkeggtrvt ivgenlglts revglrvagv rcnsipteyv saerivceme
      901 eslvpspppg paelcvgdcs adfrtqsqql ysfvtptldr vsptrgpasg gtrltisgts
      961 ldagsrvtvi irdgecqfvr rdaeaivcis pistlgpsqa piilaidhan isstgviyty
     1021 tqdptvthle ptwsiingst sitvsgthll tvqeprvrak yrgiettntc qvindtamlc
     1081 kapgiflghp qpraqgehpd efgflldhvq aarslnrssf tyypdpsfep lgpsgvldvk
     1141 pgshvvlkgk nlipaaagss rlnytvligg qpcaltvsdt qllcdspsqt grqpvmvlvg
     1201 glefwlgtlh itadraltlp amvglaaggg llllaitvvl vaykrktqda drtlkrlqlq
     1261 mdnlesrval eckeafaelq tdineltnhm dgvqipfldy rtyavrvlfp gieahpvlke
     1321 ldtppnveka lrlfgqllhs raflltfiht leaqssfsmr drgtvasltm valqsrldya
     1381 tgllkqllad lieknleskn hpklllrrte svaekmltnw ftfllhkflk ecageplfll
     1441 ycaikqqmek gpidaitgea ryslsedkli rqqidyktlt lhcvcpeseg saqvpvkvln
     1501 cdsitqakdk lldtvykgip ysqrpkaedm dlewrqgrma riilqdedit tkiecdwkri
     1561 nslahyqvtd gslvalvpkq vsaynmansf tftrslsrye sllraasspd slrsrapmlt
     1621 pdqeagtklw hlvknhdhad hregdrgskm vseiyltrll atkgtlqkfv ddlfetvfst
     1681 ahrgsalpla ikymfdflde qadqrqisdp dvrhtwksnc lplrfwvnvi knpqfvfdih
     1741 knsitdacls vvaqtfmdsc stsehrlgkd spsnkllyak dipnykswve ryyrdiakma
     1801 sisdqdmday lveqsrlhan dfnvlsalse lyfyvtkyrq eiltsldrda scrkhklrqk
     1861 leqiitlvss ss
//
LOCUS       NP_001034095             589 aa            linear   ROD 28-APR-2025
DEFINITION  kelch-like protein 25 [Rattus norvegicus].
ACCESSION   NP_001034095 XP_218809
VERSION     NP_001034095.1
DBSOURCE    REFSEQ: accession NM_001039006.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Yanagiya,A., Suyama,E., Adachi,H., Svitkin,Y.V., Aza-Blanc,P.,
            Imataka,H., Mikami,S., Martineau,Y., Ronai,Z.A. and Sonenberg,N.
  TITLE     Translational homeostasis via the mRNA cap-binding protein, eIF4E
  JOURNAL   Mol Cell 46 (6), 847-858 (2012)
   PUBMED   22578813
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099111.1.
            
            On Jan 12, 2006 this sequence version replaced XP_218809.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099111.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q31"
     Protein         1..589
                     /product="kelch-like protein 25"
                     /note="ectoderm-neural cortex protein 2; ENC-2; kelch-like
                     25"
                     /calculated_mol_wt=65709
     Region          24..151
                     /region_name="BTB_POZ_KLHL25"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 25 (KLHL25); cd18254"
                     /db_xref="CDD:349563"
     Region          39..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          296..340
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     Region          330..374
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          341..388
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     Region          378..431
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          389..444
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     Region          434..480
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          446..492
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     Region          482..525
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          493..538
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     Region          528..573
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          539..585
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLM4.1)"
     CDS             1..589
                     /gene="Klhl25"
                     /gene_synonym="RGD1310815"
                     /coded_by="NM_001039006.1:103..1872"
                     /db_xref="GeneID:293023"
                     /db_xref="RGD:1310815"
ORIGIN      
        1 msvsvhetrk srsstgsmni svfhkashpd cvlahlntlr khcmftdvtl wagdrafpch
       61 ravlaassry feamfshglr esrddtvnfq dnlhpevlel lldfayssri vineenaesl
      121 leagdmlqfh dvrdaaaefl eknlspsncl gmmvlsdahq crrlyefscr mslvhfetvr
      181 qsedfnslsr dtlldlisrd eletedervv feailqwvkh dleqrkvhlp lllrnvrlal
      241 lpsdclkkav sgeallmade ctkliideaf rcktkillnd gvvtspfarp rkaghtllil
      301 ggqtfmcdki yqvdhkakei ipkadlpspr kefsasaigc kvyvtggrgs engvskdvwv
      361 ydtvheewsk aapmliarfg hgsaelencl yvvgghtsla gifpaspsvs lkqvekydpg
      421 dnkwtmvapm rdgvsnaavv saklklfvfg gtsihrdmvs kvqcfdpsdn rwtikaecpq
      481 pwrytaaavl gsqifimggd teytaasayr fdcetnqwtr igdmtakrms chavasgnkl
      541 yvvggyfgtq rcktldcydp tsdtwncits vpysliptaf vstwkhlpa
//
LOCUS       NP_446345                442 aa            linear   ROD 28-APR-2025
DEFINITION  syndecan-3 precursor [Rattus norvegicus].
ACCESSION   NP_446345
VERSION     NP_446345.3
DBSOURCE    REFSEQ: accession NM_053893.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Liu,C.H., Kuo,Y.C., Wang,C.Y., Hsu,C.C., Ho,Y.J., Chiang,Y.C.,
            Mai,F.D., Lin,W.J. and Liao,W.C.
  TITLE     Syndecan-3 contributes to the regulation of the microenvironment at
            the node of Ranvier following end-to-side neurorrhaphy: sodium
            image analysis
  JOURNAL   Histochem Cell Biol 155 (3), 355-367 (2021)
   PUBMED   33170350
  REMARK    GeneRIF: Syndecan-3 contributes to the regulation of the
            microenvironment at the node of Ranvier following end-toside
            neurorrhaphy: sodium image analysis.
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Kwon,M.J., Park,J., Jang,S., Eom,C.Y. and Oh,E.S.
  TITLE     The Conserved Phenylalanine in the Transmembrane Domain Enhances
            Heteromeric Interactions of Syndecans
  JOURNAL   J Biol Chem 291 (2), 872-881 (2016)
   PUBMED   26601939
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Landgraf,P., Mikhaylova,M., Macharadze,T., Borutzki,C.,
            Zenclussen,A.C., Wahle,P. and Kreutz,M.R.
  TITLE     Binding of Y-P30 to syndecan 2/3 regulates the nuclear localization
            of CASK
  JOURNAL   PLoS One 9 (2), e85924 (2014)
   PUBMED   24498267
  REMARK    GeneRIF: Data suggest that Y-P30 can control the nuclear
            localization of Calcium/calmodulin-dependent serine kinase (CASK)
            in a syndecan (SDC) -2 and -3 -dependent manner.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 442)
  AUTHORS   De Rossi,G. and Whiteford,J.R.
  TITLE     A novel role for syndecan-3 in angiogenesis
  JOURNAL   F1000Res 2, 270 (2013)
   PUBMED   24555114
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Imai,S., Kaksonen,M., Raulo,E., Kinnunen,T., Fages,C., Meng,X.,
            Lakso,M. and Rauvala,H.
  TITLE     Osteoblast recruitment and bone formation enhanced by cell
            matrix-associated heparin-binding growth-associated molecule
            (HB-GAM)
  JOURNAL   J Cell Biol 143 (4), 1113-1128 (1998)
   PUBMED   9817766
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Nakanishi,T., Kadomatsu,K., Okamoto,T., Ichihara-Tanaka,K.,
            Kojima,T., Saito,H., Tomoda,Y. and Muramatsu,T.
  TITLE     Expression of syndecan-1 and -3 during embryogenesis of the central
            nervous system in relation to binding with midkine
  JOURNAL   J Biochem 121 (2), 197-205 (1997)
   PUBMED   9089390
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Carey,D.J., Conner,K., Asundi,V.K., O'Mahony,D.J., Stahl,R.C.,
            Showalter,L., Cizmeci-Smith,G., Hartman,J. and Rothblum,L.I.
  TITLE     cDNA cloning, genomic organization, and in vivo expression of rat
            N-syndecan
  JOURNAL   J Biol Chem 272 (5), 2873-2879 (1997)
   PUBMED   9006931
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Raulo,E., Chernousov,M.A., Carey,D.J., Nolo,R. and Rauvala,H.
  TITLE     Isolation of a neuronal cell surface receptor of heparin binding
            growth-associated molecule (HB-GAM). Identification as N-syndecan
            (syndecan-3)
  JOURNAL   J Biol Chem 269 (17), 12999-13004 (1994)
   PUBMED   8175719
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Carey,D.J., Evans,D.M., Stahl,R.C., Asundi,V.K., Conner,K.J.,
            Garbes,P. and Cizmeci-Smith,G.
  TITLE     Molecular cloning and characterization of N-syndecan, a novel
            transmembrane heparan sulfate proteoglycan
  JOURNAL   J Cell Biol 117 (1), 191-201 (1992)
   PUBMED   1556152
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U73184.1, U52825.1 and JAXUCZ010000005.1.
            
            On Oct 11, 2007 this sequence version replaced NP_446345.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U52825.1, SRR26643297.20306.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..442
                     /product="syndecan-3 precursor"
                     /note="SYND3; N-syndecan; neuroglycan"
                     /calculated_mol_wt=41454
     sig_peptide     1..44
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4453
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     mat_peptide     45..442
                     /product="Syndecan-3. /id=PRO_0000033509"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
                     /calculated_mol_wt=41454
     Region          55..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            78
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            80
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            82
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            89
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            107
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Region          151..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            161
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) serine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            162
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            170
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            172
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Region          180..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Region          225..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Region          252..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            315
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Region          339..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            367
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (glycosaminoglycan) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Region          378..440
                     /region_name="Syndecan"
                     /note="Syndecan domain; pfam01034"
                     /db_xref="CDD:460035"
     Site            383..384
                     /site_type="cleavage"
                     /note="Cleavage of ectodomain. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Region          419..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33671.3)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75056; propagated from
                     UniProtKB/Swiss-Prot (P33671.3)"
     CDS             1..442
                     /gene="Sdc3"
                     /coded_by="NM_053893.3:47..1375"
                     /db_xref="GeneID:116673"
                     /db_xref="RGD:621486"
ORIGIN      
        1 mkpgpprrgt aqgqrvdtat hgpgarglll ppllllllag raagaqrwrn enferpvdle
       61 gsgdddsfpd delddlysgs gsgyfeqesg letamrfipd ialaaptapa mlpttviqpv
      121 dtpfeellse hpgpepvtsp plvtevtevv eepsqratti stttsttaat ttgaptmata
      181 pataattaps tpaappatat tadirttgiq gllplpltta atakattpav psppttvatl
      241 dteaptprlv ntatsrpral prpvttqepe vaerstlplg ttapgpteva qtptpesllt
      301 ttqdepevpv sggpsgdfel qeettqpdta nevvavegaa akpspplgtl pkgarpglgl
      361 hdnaidsgss aaqlpqksil erkevlvavi vggvvgalfa aflvtlliyr mkkkdegsyt
      421 leepkqasvt yqkpdkqeef ya
//
LOCUS       NP_997707                127 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase PPP1R11 [Rattus norvegicus].
ACCESSION   NP_997707 XP_215296
VERSION     NP_997707.2
DBSOURCE    REFSEQ: accession NM_212542.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   McKelvey,A.C., Lear,T.B., Dunn,S.R., Evankovich,J., Londino,J.D.,
            Bednash,J.S., Zhang,Y., McVerry,B.J., Liu,Y. and Chen,B.B.
  TITLE     RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate
            immunity
  JOURNAL   Elife 5, e18496 (2016)
   PUBMED   27805901
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Cheng,L., Pilder,S., Nairn,A.C., Ramdas,S. and Vijayaraghavan,S.
  TITLE     PP1gamma2 and PPP1R11 are parts of a multimeric complex in
            developing testicular germ cells in which their steady state levels
            are reciprocally related
  JOURNAL   PLoS One 4 (3), e4861 (2009)
   PUBMED   19300506
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Coriton,O., Lepourcelet,M., Hampe,A., Galibert,F. and Mosser,J.
  TITLE     Transcriptional analysis of the 69-kb sequence centromeric to
            HLA-J: a dense and complex structure of five genes
  JOURNAL   Mamm Genome 11 (12), 1127-1131 (2000)
   PUBMED   11130983
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Zhang,J., Zhang,L., Zhao,S. and Lee,E.Y.
  TITLE     Identification and characterization of the human HCG V gene product
            as a novel inhibitor of protein phosphatase-1
  JOURNAL   Biochemistry 37 (47), 16728-16734 (1998)
   PUBMED   9843442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM088354.1, EX488885.1, BC079252.1 and CX571132.1.
            
            On Dec 20, 2007 this sequence version replaced NP_997707.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM133232.1, BC079252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..127
                     /product="E3 ubiquitin-protein ligase PPP1R11"
                     /EC_number="2.3.2.27"
                     /note="protein phosphatase 1 regulatory subunit 11;
                     t-complex testis expressed-5"
                     /calculated_mol_wt=13805
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Region          30..72
                     /region_name="PPI_Ypi1"
                     /note="Protein phosphatase inhibitor; pfam07491"
                     /db_xref="CDD:429489"
     Region          53..63
                     /region_name="Atypical RING finger domain 1.
                     /evidence=ECO:0000250|UniProtKB:O60927"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Region          70..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Region          86..95
                     /region_name="Atypical RING finger domain 2.
                     /evidence=ECO:0000250|UniProtKB:O60927"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFY6.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O60927; propagated from
                     UniProtKB/Swiss-Prot (Q6MFY6.2)"
     CDS             1..127
                     /gene="Ppp1r11"
                     /gene_synonym="HCGV; Tctex5"
                     /coded_by="NM_212542.3:202..585"
                     /db_xref="GeneID:294207"
                     /db_xref="RGD:1303163"
ORIGIN      
        1 maeagaggls etvtettvtv ttepenrslt iklrkrkpek kvewssdtvd nehmgrrssk
       61 ccciyekpra fgesstesde deeegcghth cvrghrkgrr pttpgptptt ppqppdpsqp
      121 ppgpmqh
//
LOCUS       NP_067687                465 aa            linear   ROD 28-APR-2025
DEFINITION  chromogranin-A precursor [Rattus norvegicus].
ACCESSION   NP_067687 XP_346782
VERSION     NP_067687.2
DBSOURCE    REFSEQ: accession NM_021655.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Bharat,V., Siebrecht,M., Burk,K., Ahmed,S., Reissner,C.,
            Kohansal-Nodehi,M., Steubler,V., Zweckstetter,M., Ting,J.T. and
            Dean,C.
  TITLE     Capture of Dense Core Vesicles at Synapses by JNK-Dependent
            Phosphorylation of Synaptotagmin-4
  JOURNAL   Cell Rep 21 (8), 2118-2133 (2017)
   PUBMED   29166604
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Friese,R.S., Altshuler,A.E., Zhang,K., Miramontes-Gonzalez,J.P.,
            Hightower,C.M., Jirout,M.L., Salem,R.M., Gayen,J.R.,
            Mahapatra,N.R., Biswas,N., Cale,M., Vaingankar,S.M., Kim,H.S.,
            Courel,M., Taupenot,L., Ziegler,M.G., Schork,N.J., Pravenec,M.,
            Mahata,S.K., Schmid-Schonbein,G.W. and O'Connor,D.T.
  TITLE     MicroRNA-22 and promoter motif polymorphisms at the Chga locus in
            genetic hypertension: functional and therapeutic implications for
            gene expression and the pathogenesis of hypertension
  JOURNAL   Hum Mol Genet 22 (18), 3624-3640 (2013)
   PUBMED   23674521
  REMARK    GeneRIF: hypothesized that the 3'-UTR and promoter mutations lead
            to dysregulation (diminution) of Chga in brainstem cardiovascular
            control nuclei, ultimately contributing to the pathogenesis of
            hypertension in spontaneously hypertensive rats
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Pasqua,T., Corti,A., Gentile,S., Pochini,L., Bianco,M.,
            Metz-Boutigue,M.H., Cerra,M.C., Tota,B. and Angelone,T.
  TITLE     Full-length human chromogranin-A cardioactivity: myocardial,
            coronary, and stimulus-induced processing evidence in normotensive
            and hypertensive male rat hearts
  JOURNAL   Endocrinology 154 (9), 3353-3365 (2013)
   PUBMED   23751870
  REMARK    GeneRIF: Data suggest that Chga plays role in cardiocirculatory
            homeostasis and allostasis in hypertension; in hypertension,
            negative inotropic effect elicited by full-length Chga in heart may
            represent compensatory mechanism for increased blood pressure.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Tota,B., Gentile,S., Pasqua,T., Bassino,E., Koshimizu,H.,
            Cawley,N.X., Cerra,M.C., Loh,Y.P. and Angelone,T.
  TITLE     The novel chromogranin A-derived serpinin and pyroglutaminated
            serpinin peptides are positive cardiac beta-adrenergic-like
            inotropes
  JOURNAL   FASEB J 26 (7), 2888-2898 (2012)
   PUBMED   22459152
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Koshimizu,H., Cawley,N.X., Yergy,A.L. and Loh,Y.P.
  TITLE     Role of pGlu-serpinin, a novel chromogranin A-derived peptide in
            inhibition of cell death
  JOURNAL   J Mol Neurosci 45 (2), 294-303 (2011)
   PUBMED   21537909
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Hsiao,R.J., Neumann,H.P., Parmer,R.J., Barbosa,J.A. and
            O'Connor,D.T.
  TITLE     Chromogranin A in familial pheochromocytoma: diagnostic screening
            value, prediction of tumor mass, and post-resection kinetics
            indicating two-compartment distribution
  JOURNAL   Am J Med 88 (6), 607-613 (1990)
   PUBMED   2189303
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Parmer,R.J., Koop,A.H., Handa,M.T. and O'Connor,D.T.
  TITLE     Molecular cloning of chromogranin A from rat pheochromocytoma cells
  JOURNAL   Hypertension 14 (4), 435-444 (1989)
   PUBMED   2793216
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Hutton,J.C., Nielsen,E. and Kastern,W.
  TITLE     The molecular cloning of the chromogranin A-like precursor of
            beta-granin and pancreastatin from the endocrine pancreas
  JOURNAL   FEBS Lett 236 (2), 269-274 (1988)
   PUBMED   3044825
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Iacangelo,A., Okayama,H. and Eiden,L.E.
  TITLE     Primary structure of rat chromogranin A and distribution of its
            mRNA
  JOURNAL   FEBS Lett 227 (2), 115-121 (1988)
   PUBMED   2828116
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Hutton,J.C., Hansen,F. and Peshavaria,M.
  TITLE     beta-Granins: 21 kDa co-secreted peptides of the insulin granule
            closely related to adrenal medullary chromogranin A
  JOURNAL   FEBS Lett 188 (2), 336-340 (1985)
   PUBMED   3896848
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB743841.1 and BC087703.1.
            
            On Mar 9, 2007 this sequence version replaced NP_067687.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..465
                     /product="chromogranin-A precursor"
                     /note="cgA; chromogranin A (parathyroid secretory protein
                     1)"
                     /calculated_mol_wt=50092
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1822
     Region          25..465
                     /region_name="Granin"
                     /note="Granin (chromogranin or secretogranin); pfam01271"
                     /db_xref="CDD:279595"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05059; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10645; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26339; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            331
                     /site_type="amidation"
                     /note="Glycine amide.
                     /evidence=ECO:0000250|UniProtKB:P05059; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05059; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            432
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P10645; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            440
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P26339,
                     ECO:0000303|PubMed:22459152; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10354.1)"
     CDS             1..465
                     /gene="Chga"
                     /coded_by="NM_021655.2:152..1549"
                     /db_xref="GeneID:24258"
                     /db_xref="RGD:2338"
ORIGIN      
        1 mrssaalall lcagqvfalp vnspmtkgdt kvmkcvlevi sdslskpspm pvspecletl
       61 qgdervlsil rhqnllkelq dlalqgaker aqqqqqqqqq qqqqqqqqqq hssfedelse
      121 vfenqspaak hgdaaseaps kdtvekreds dkgqqdafeg ttegprpqaf pepkqessmm
      181 gnsqspgedt anntqsptsl psqehgipqt tegsergpsa qqqarkakqe ekeeeeeeke
      241 eeeeekeeka iarekagpke vptaassshf ysgykkiqkd ddgqsesqav ngktgaseav
      301 psegkgeleh sqqeedgeea magppqglfp ggkgqelerk qqeeeeeeer lsrewedkrw
      361 srmdqlakel taekrleged dpdrsmklsf raraygfrdp gpqlrrgwrp ssredsvear
      421 gdfeekkeee gsanrraedq eleslsaiea elekvahqlq alrrg
//
LOCUS       NP_001274042             148 aa            linear   ROD 28-APR-2025
DEFINITION  vascular endothelial growth factor A isoform 11 [Rattus
            norvegicus].
ACCESSION   NP_001274042
VERSION     NP_001274042.1
DBSOURCE    REFSEQ: accession NM_001287113.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Fu,W., Ye,Y. and Hu,F.
  TITLE     LncRNA XIST promotes neovascularization in diabetic retinopathy by
            regulating miR-101-3p/VEGFA
  JOURNAL   Arch Endocrinol Metab 68, e230097 (2024)
   PUBMED   38739522
  REMARK    GeneRIF: LncRNA XIST promotes neovascularization in diabetic
            retinopathy by regulating miR-101-3p/VEGFA.
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Li,Z., Xie,L., Zou,L., Xiao,S. and Tao,J.
  TITLE     Overexpression of RAD54L attenuates osteoarthritis by suppressing
            the HIF-1alpha/VEGF signaling pathway: Bioinformatics analysis and
            experimental validation
  JOURNAL   PLoS One 19 (4), e0298575 (2024)
   PUBMED   38593124
  REMARK    GeneRIF: Overexpression of RAD54L attenuates osteoarthritis by
            suppressing the HIF-1alpha/VEGF signaling pathway: Bioinformatics
            analysis and experimental validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Bastide,A., Karaa,Z., Bornes,S., Hieblot,C., Lacazette,E., Prats,H.
            and Touriol,C.
  TITLE     An upstream open reading frame within an IRES controls expression
            of a specific VEGF-A isoform
  JOURNAL   Nucleic Acids Res 36 (7), 2434-2445 (2008)
   PUBMED   18304943
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Meiron,M., Anunu,R., Scheinman,E.J., Hashmueli,S. and Levi,B.Z.
  TITLE     New isoforms of VEGF are translated from alternative initiation CUG
            codons located in its 5'UTR
  JOURNAL   Biochem Biophys Res Commun 282 (4), 1053-1060 (2001)
   PUBMED   11352659
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Terman,B.I., Dougher-Vermazen,M., Carrion,M.E., Dimitrov,D.,
            Armellino,D.C., Gospodarowicz,D. and Bohlen,P.
  TITLE     Identification of the KDR tyrosine kinase as a receptor for
            vascular endothelial cell growth factor
  JOURNAL   Biochem Biophys Res Commun 187 (3), 1579-1586 (1992)
   PUBMED   1417831
REFERENCE   9  (residues 1 to 148)
  AUTHORS   de Vries,C., Escobedo,J.A., Ueno,H., Houck,K., Ferrara,N. and
            Williams,L.T.
  TITLE     The fms-like tyrosine kinase, a receptor for vascular endothelial
            growth factor
  JOURNAL   Science 255 (5047), 989-991 (1992)
   PUBMED   1312256
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Breier,G., Albrecht,U., Sterrer,S. and Risau,W.
  TITLE     Expression of vascular endothelial growth factor during embryonic
            angiogenesis and endothelial cell differentiation
  JOURNAL   Development 114 (2), 521-532 (1992)
   PUBMED   1592003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO565920.1, BC168708.1,
            AY378102.1 and JAXUCZ010000009.1.
            
            Summary: This gene is a member of the PDGF/VEGF growth factor
            family. It encodes a heparin-binding protein, which exists as a
            disulfide-linked homodimer. This growth factor induces
            proliferation and migration of vascular endothelial cells, and is
            essential for both physiological and pathological angiogenesis.
            Disruption of this gene in mice resulted in abnormal embryonic
            blood vessel formation. This gene is upregulated in many known
            tumors and its expression is correlated with tumor stage and
            progression. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. There is also
            evidence for alternative translation initiation from upstream
            non-AUG (CUG) codons resulting in additional isoforms. A recent
            study showed that a C-terminally extended isoform is produced by
            use of an alternative in-frame translation termination codon via a
            stop codon readthrough mechanism, and that this isoform is
            antiangiogenic. Expression of some isoforms derived from the AUG
            start codon is regulated by a small upstream open reading frame,
            which is located within an internal ribosome entry site. [provided
            by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (7) lacks an internal exon in the
            5' region, which results in translation initiation at a downstream
            AUG site, and an in-frame, internal coding exon, compared to
            variant 1. The resulting isoform (11) is shorter at the N-terminus
            and lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY033504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..148
                     /product="vascular endothelial growth factor A isoform 11"
                     /note="vascular permeability factor"
                     /calculated_mol_wt=17350
     Region          7..89
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(7..10,44,46..49,64..67)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(9,40,44,51,85,87)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(34,43)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Region          100..148
                     /region_name="VEGF_C"
                     /note="VEGF heparin-binding domain; pfam14554"
                     /db_xref="CDD:405273"
     CDS             1..148
                     /gene="Vegfa"
                     /gene_synonym="Vegf; VEGF-A; VEGF111; VEGF164; VPF"
                     /coded_by="NM_001287113.1:1092..1538"
                     /note="isoform 11 is encoded by transcript variant 7"
                     /db_xref="GeneID:83785"
                     /db_xref="RGD:619991"
ORIGIN      
        1 mdvyqrsycr pietlvdifq eypdeieyif kpscvplmrc agccndeale cvptsesnvt
       61 mqimrikphq sqhigemsfl qhsrcecrpk kdrtkpenhc epcserrkhl fvqdpqtckc
      121 sckntdsrck arqlelnert crcdkprr
//
LOCUS       NP_671485                699 aa            linear   ROD 28-APR-2025
DEFINITION  protein CASC3 [Rattus norvegicus].
ACCESSION   NP_671485
VERSION     NP_671485.1
DBSOURCE    REFSEQ: accession NM_147144.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Zhan,X., Yan,C., Zhang,X., Lei,J. and Shi,Y.
  TITLE     Structure of a human catalytic step I spliceosome
  JOURNAL   Science 359 (6375), 537-545 (2018)
   PUBMED   29301961
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   5  (residues 1 to 699)
  AUTHORS   Kunz,J.B., Neu-Yilik,G., Hentze,M.W., Kulozik,A.E. and Gehring,N.H.
  TITLE     Functions of hUpf3a and hUpf3b in nonsense-mediated mRNA decay and
            translation
  JOURNAL   RNA 12 (6), 1015-1022 (2006)
   PUBMED   16601204
REFERENCE   6  (residues 1 to 699)
  AUTHORS   Macchi,P., Kroening,S., Palacios,I.M., Baldassa,S., Grunewald,B.,
            Ambrosino,C., Goetze,B., Lupas,A., St Johnston,D. and Kiebler,M.
  TITLE     Barentsz, a new component of the Staufen-containing
            ribonucleoprotein particles in mammalian cells, interacts with
            Staufen in an RNA-dependent manner
  JOURNAL   J Neurosci 23 (13), 5778-5788 (2003)
   PUBMED   12843282
  REMARK    GeneRIF: data suggest that the mRNA transport machinery is
            conserved during evolution, and that mammalian Btz is an additional
            component of the dendritic ribonucleoprotein particles in
            hippocampal neurons
REFERENCE   7  (residues 1 to 699)
  AUTHORS   Degot,S., Regnier,C.H., Wendling,C., Chenard,M.P., Rio,M.C. and
            Tomasetto,C.
  TITLE     Metastatic Lymph Node 51, a novel nucleo-cytoplasmic protein
            overexpressed in breast cancer
  JOURNAL   Oncogene 21 (28), 4422-4434 (2002)
   PUBMED   12080473
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF525467.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF525467.1, SRR8487230.133965.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..699
                     /product="protein CASC3"
                     /note="barentsz protein; cancer susceptibility candidate
                     3; cancer susceptibility candidate gene 3 protein homolog;
                     protein barentsz; metastatic lymph node 51; cancer
                     susceptibility 3; metastatic lymph node gene 51 protein
                     homolog"
                     /calculated_mol_wt=75774
     Region          1..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K3W3; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15234; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          134..280
                     /region_name="Necessary for RNA-binding, interaction with
                     MAGOH and localization in nucleus speckles.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          134..280
                     /region_name="Sufficient to form the EJC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          143..245
                     /region_name="Btz"
                     /note="CASC3/Barentsz eIF4AIII binding; smart01044"
                     /db_xref="CDD:214991"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          201..207
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          251..259
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          <273..699
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O15234; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          374..699
                     /region_name="Necessary for localization in cytoplasmic
                     stress granules. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          458..467
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15234; propagated from
                     UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          577..596
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     Region          629..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3X0.1)"
     CDS             1..699
                     /gene="Casc3"
                     /gene_synonym="Btz; Mln51"
                     /coded_by="NM_147144.1:1..2100"
                     /db_xref="GeneID:259170"
                     /db_xref="RGD:628766"
ORIGIN      
        1 madrrrqras qdtedeesga sgsdsgspar gggscsgsag gggsgslpsq rggrggglhl
       61 rrvesggaks aeesecesed gmegdavlsd yesaedsege eeyseeensk velkseanda
      121 adssakekge ekpeskgtvt gerqsgdgqe stepvenkvg kkgpkhlddd edrknpayip
      181 rkglffehdl rgqtqeeevr pkgrqrklwk degrwehdkf redeqapksr qelialygyd
      241 irsahnpddi kprrirkprf gsppqrdpnw igdrsskshr hqgpggnlpp rtfinrnaag
      301 tgrmstsrny srsggfkegr tsfrpvevgg qhgarsgetl kheanyrsrr leqtpmrdps
      361 pepdapllgs pekeevaset paavpditpp apdrpiekks ysrarrtrtk vgdavkaaee
      421 vpppseglts aatvpestpp aaktgnweap vdsttggleq dvaqlniaeq nwspgqpsfl
      481 qprelrgmpn hihmgagppp qfnrmeemgv qsgrakryss qrqrpvpepp appvhisime
      541 ghyydplqfq gpiythgdsp aplppqgmiv qpemhlphpg lhphqspapl pnpglypppv
      601 smspgqpppq qllaptyfsa pgvmnfgnps ypyapgalpp pppphlypnt qapsqvyggv
      661 tyynpaqqqv qpkpspprrt pqpvsikppp sevvsrgss
//
LOCUS       NP_446028                224 aa            linear   ROD 28-APR-2025
DEFINITION  peroxiredoxin-6 [Rattus norvegicus].
ACCESSION   NP_446028
VERSION     NP_446028.1
DBSOURCE    REFSEQ: accession NM_053576.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Xiong,J., Zhou,R. and Deng,X.
  TITLE     PRDX6 alleviated heart failure by inhibiting doxorubicin-induced
            ferroptosis through the JAK2/STAT1 pathway inactivation
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 354-364 (2024)
   PUBMED   38530594
  REMARK    GeneRIF: PRDX6 alleviated heart failure by inhibiting
            doxorubicin-induced ferroptosis through the JAK2/STAT1 pathway
            inactivation.
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Shen,W., Yang,L., Yang,Y., Wang,P., Tao,X., Shen,Y., Wang,S. and
            Shen,Y.
  TITLE     PRDX6 Promotes Fatty Acid Oxidation via PLA2-Dependent PPARalpha
            Activation in Rats Fed High-Fat Diet
  JOURNAL   Antioxid Redox Signal 38 (16-18), 1184-1200 (2023)
   PUBMED   36401357
  REMARK    GeneRIF: PRDX6 Promotes Fatty Acid Oxidation via PLA2-Dependent
            PPARalpha Activation in Rats Fed High-Fat Diet.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Li,H., Wu,Z., Zhong,R., Zhang,Q., Chen,Q. and Shen,Y.
  TITLE     PRDX6 knockout restrains the malignant progression of intrahepatic
            cholangiocarcinoma
  JOURNAL   Med Oncol 39 (12), 250 (2022)
   PUBMED   36209344
  REMARK    GeneRIF: PRDX6 knockout restrains the malignant progression of
            intrahepatic cholangiocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Hong,T., Zhou,Y., Peng,L., Wu,X., Li,Y., Li,Y. and Zhao,Y.
  TITLE     Knocking Down Peroxiredoxin 6 Aggravates Cerebral
            Ischemia-Reperfusion Injury by Enhancing Mitophagy
  JOURNAL   Neuroscience 482, 30-42 (2022)
   PUBMED   34863856
  REMARK    GeneRIF: Knocking Down Peroxiredoxin 6 Aggravates Cerebral
            Ischemia-Reperfusion Injury by Enhancing Mitophagy.
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Tang,B., Ni,W., Zhou,J., Ling,Y., Niu,D., Lu,X., Chen,T.,
            Ramalingam,M. and Hu,J.
  TITLE     Peroxiredoxin 6 secreted by Schwann-like cells protects neuron
            against ischemic stroke in rats via PTEN/PI3K/AKT pathway
  JOURNAL   Tissue Cell 73, 101635 (2021)
   PUBMED   34482185
  REMARK    GeneRIF: Peroxiredoxin 6 secreted by Schwann-like cells protects
            neuron against ischemic stroke in rats via PTEN/PI3K/AKT pathway.
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Chen,J.W., Dodia,C., Feinstein,S.I., Jain,M.K. and Fisher,A.B.
  TITLE     1-Cys peroxiredoxin, a bifunctional enzyme with glutathione
            peroxidase and phospholipase A2 activities
  JOURNAL   J Biol Chem 275 (37), 28421-28427 (2000)
   PUBMED   10893423
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Andreeva,S.G., Merkulova,M.I., Shuvaeva,T.M., Novoselov,V.I.,
            Peshenko,I.V., Novoselov,S.V., Fesenko,E.E. and Lipkin,V.M.
  TITLE     [Study of structure of secretory 28 kDa protein from the rat
            olfactory epithelium]
  JOURNAL   Bioorg Khim 24 (11), 816-821 (1998)
   PUBMED   10079938
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Choi,H.J., Kang,S.W., Yang,C.H., Rhee,S.G. and Ryu,S.E.
  TITLE     Crystal structure of a novel human peroxidase enzyme at 2.0 A
            resolution
  JOURNAL   Nat Struct Biol 5 (5), 400-406 (1998)
   PUBMED   9587003
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Kim,T.S., Sundaresh,C.S., Feinstein,S.I., Dodia,C., Skach,W.R.,
            Jain,M.K., Nagase,T., Seki,N., Ishikawa,K., Nomura,N. and
            Fisher,A.B.
  TITLE     Identification of a human cDNA clone for lysosomal type
            Ca2+-independent phospholipase A2 and properties of the expressed
            protein
  JOURNAL   J Biol Chem 272 (4), 2542-2550 (1997)
   PUBMED   8999971
  REMARK    Erratum:[J Biol Chem 1997 Apr 18;272(16):10981]
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Peshenko,I.V., Novoselov,V.I., Evdokimov,V.A., Nikolaev,Yu.V.,
            Shuvaeva,T.M., Lipkin,V.M. and Fesenko,E.E.
  TITLE     Novel 28-kDa secretory protein from rat olfactory epithelium
  JOURNAL   FEBS Lett 381 (1-2), 12-14 (1996)
   PUBMED   8641418
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF014009.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF014009.1, Y17295.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q22"
     Protein         1..224
                     /product="peroxiredoxin-6"
                     /EC_number="3.1.1.4"
                     /EC_number="2.3.1.23"
                     /EC_number="1.11.1.27"
                     /note="NSGPx; aiPLA2; 1-Cys PRX; antioxidant protein 2;
                     non-selenium glutathione peroxidase; acidic
                     calcium-independent phospholipase A2; 1-Cys peroxiredoxin;
                     thiol-specific antioxidant protein; glutathione-dependent
                     peroxiredoxin; LPC acyltransferase 5; lyso-PC
                     acyltransferase 5; lysophosphatidylcholine acyltransferase
                     5"
                     /calculated_mol_wt=24688
     Region          7..222
                     /region_name="PRX_1cys"
                     /note="Peroxiredoxin (PRX) family, 1-cys PRX subfamily;
                     composed of PRXs containing only one conserved cysteine,
                     which serves as the peroxidatic cysteine. They are
                     homodimeric thiol-specific antioxidant (TSA) proteins that
                     confer a protective role in cells by...; cd03016"
                     /db_xref="CDD:239314"
     Site            order(7,45,48..50,53,85,88,115,130,144..146,148..150,
                     152..157,159,162,166..167,176..177,179..180,217,220)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239314"
     Site            order(19,73..75,77..78,80..81,83..84,97,106..107,117,
                     128..129,192,210)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239314"
     Region          31..40
                     /region_name="Required and sufficient for targeting to
                     lysosomes and lamellar bodies.
                     /evidence=ECO:0000269|PubMed:19700648"
                     /note="propagated from UniProtKB/Swiss-Prot (O35244.3)"
     Site            32
                     /site_type="other"
                     /note="Important for phospholipase activity.
                     /evidence=ECO:0000305|PubMed:17652308; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     Site            order(44,47,132)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239314"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30041; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P30041; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P30041; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000269|PubMed:19140803; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     Site            209
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P30041; propagated from
                     UniProtKB/Swiss-Prot (O35244.3)"
     CDS             1..224
                     /gene="Prdx6"
                     /gene_synonym="LPCAT-5"
                     /coded_by="NM_053576.2:21..695"
                     /db_xref="GeneID:94167"
                     /db_xref="RGD:71005"
ORIGIN      
        1 mpgglllgde apnfeantti ghirfhdflg dswgilfshp rdftpvctte lgraaklape
       61 fakrnvklia lsidsvedhf awskdinayn gaapteklpf piiddkdrdl aillgmldpa
      121 ekdekgmpvt arvvfifgpd kklklsilyp attgrnfdei lrvvdslqlt asnpvatpvd
      181 wkkgesvmvl ptlpeeeakq lfpkgvftke lpsgkkylry tpqp
//
LOCUS       NP_113728                462 aa            linear   ROD 28-APR-2025
DEFINITION  coagulation factor IX precursor [Rattus norvegicus].
ACCESSION   NP_113728
VERSION     NP_113728.1
DBSOURCE    REFSEQ: accession NM_031540.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Metzger,J.M., Tadin-Strapps,M., Thankappan,A., Strapps,W.R.,
            DiPietro,M., Leander,K., Zhang,Z., Shin,M.K., Levorse,J., Desai,K.,
            Xu,Y., Lai,K., Wu,W., Chen,Z., Cai,T.Q., Jochnowitz,N., Bentley,R.,
            Hoos,L., Zhou,Y., Sepp-Lorenzino,L., Seiffert,D. and Andre,P.
  TITLE     Titrating haemophilia B phenotypes using siRNA strategy: evidence
            that antithrombotic activity is separated from bleeding liability
  JOURNAL   Thromb Haemost 113 (6), 1300-1311 (2015)
   PUBMED   25790442
  REMARK    GeneRIF: Data provide substantial evidence of a participation of
            fIX in the mechanisms regulating thrombosis prior to those
            regulating primary haemostasis.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Smith,S.A., Travers,R.J. and Morrissey,J.H.
  TITLE     How it all starts: Initiation of the clotting cascade
  JOURNAL   Crit Rev Biochem Mol Biol 50 (4), 326-336 (2015)
   PUBMED   26018600
  REMARK    Review article
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Mizurini,D.M., Francischetti,I.M., Andersen,J.F. and Monteiro,R.Q.
  TITLE     Nitrophorin 2, a factor IX(a)-directed anticoagulant, inhibits
            arterial thrombosis without impairing haemostasis
  JOURNAL   Thromb Haemost 104 (6), 1116-1123 (2010)
   PUBMED   20838739
  REMARK    GeneRIF: Nitrophorin 2, a factor IX(a)-directed anticoagulant, is a
            potent and long-lasting inhibitor of arterial thrombosis with minor
            effects on haemostasis.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Zhang,L., Gu,D.S., DU,W.T., Liu,P.X., Lu,S.H. and Yang,R.C.
  TITLE     [Human coagulation factor IX gene therapy in murine hemophilia B by
            hydrodynamic delivery and site-specific genomic integration]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 31 (5), 294-299 (2010)
   PUBMED   21122306
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Verma,D., Moghimi,B., LoDuca,P.A., Singh,H.D., Hoffman,B.E.,
            Herzog,R.W. and Daniell,H.
  TITLE     Oral delivery of bioencapsulated coagulation factor IX prevents
            inhibitor formation and fatal anaphylaxis in hemophilia B mice
  JOURNAL   Proc Natl Acad Sci U S A 107 (15), 7101-7106 (2010)
   PUBMED   20351275
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Reijnen,M.J., Sladek,F.M., Bertina,R.M. and Reitsma,P.H.
  TITLE     Disruption of a binding site for hepatocyte nuclear factor 4
            results in hemophilia B Leyden
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6300-6303 (1992)
   PUBMED   1631121
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Giannelli,F., Green,P.M., High,K.A., Sommer,S., Lillicrap,D.P.,
            Ludwig,M., Olek,K., Reitsma,P.H., Goossens,M., Yoshioka,A. et al.
  TITLE     Haemophilia B: database of point mutations and short additions and
            deletions--second edition
  JOURNAL   Nucleic Acids Res 19 Suppl (Suppl), 2193-2219 (1991)
   PUBMED   2041805
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Sarkar,G., Koeberl,D.D. and Sommer,S.S.
  TITLE     Direct sequencing of the activation peptide and the catalytic
            domain of the factor IX gene in six species
  JOURNAL   Genomics 6 (1), 133-143 (1990)
   PUBMED   2303254
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Suehiro,K., Kawabata,S., Miyata,T., Takeya,H., Takamatsu,J.,
            Ogata,K., Kamiya,T., Saito,H., Niho,Y. and Iwanaga,S.
  TITLE     Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by
            tryptophan and its activation by alpha-chymotrypsin and rat mast
            cell chymase
  JOURNAL   J Biol Chem 264 (35), 21257-21265 (1989)
   PUBMED   2592373
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Chen,S.H., Thompson,A.R., Zhang,M. and Scott,C.R.
  TITLE     Three point mutations in the factor IX genes of five hemophilia B
            patients. Identification strategy using localization by altered
            epitopes in their hemophilic proteins
  JOURNAL   J Clin Invest 84 (1), 113-118 (1989)
   PUBMED   2472424
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1, FM036569.1 and M26247.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643286.48408.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..462
                     /product="coagulation factor IX precursor"
                     /EC_number="3.4.21.22"
                     /note="christmas factor; Coagulation factor IX (plasma
                     thromboplastic component, Christmas disease, hemophilia
                     B); coagulation factor 9"
                     /calculated_mol_wt=49589
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2238
     Region          21..85
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     mat_peptide     40..462
                     /product="Coagulation factor IX. /id=PRO_0000088685"
                     /note="propagated from UniProtKB/Swiss-Prot (P16296.2)"
                     /calculated_mol_wt=47479
     Site            46
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            47
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            54
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            56
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            59
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            60
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            65
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            66
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            69
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            72
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            75
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            78
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            79
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P00741,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Region          86..122
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(86,89,103)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            92
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) serine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            103
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyaspartate.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Region          127..163
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            185..186
                     /site_type="cleavage"
                     /note="Cleavage, by factor XIa.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            195
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            199
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            216
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            226
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            227..228
                     /site_type="cleavage"
                     /note="Cleavage, by factor XIa.
                     /evidence=ECO:0000250|UniProtKB:P00740; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Region          228..458
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            228
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(268,316,412)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16296.2)"
     Site            order(406,431,433)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..462
                     /gene="F9"
                     /coded_by="NM_031540.1:1..1389"
                     /db_xref="GeneID:24946"
                     /db_xref="RGD:2589"
ORIGIN      
        1 madapglipi fllgyllste cavfldrena tkiltrpkry nsgkleefvq gnlereciee
       61 rcsfeearev fentekttef wkqyvdgdqc esnpclnggi ckddinsyec wcqagfegrn
      121 celdatcsik ngrckqfckn spdnkiicsc tegyqlaedq kscepavpfp cgrvsvayns
      181 kkitraetvf sntdygnste lildditnst ildnltense pindftrvvg genakpgqip
      241 wqvilngeie afcggaiine kwivtaahcl kpgdkievva gehnideked teqrrnvirt
      301 iphhqynati nkyshdiall eldkplilns yvtpicvank eytniflkfg sgyvsgwgkv
      361 fnkgrqasil qylrvplvdr atclrstkfs iynnmfcagy reggkdsceg dsggphvtev
      421 egtsfltgii swgeecamkg kygiytkvsr yvnwikektk lt
//
LOCUS       NP_001007711             480 aa            linear   ROD 28-APR-2025
DEFINITION  2-phosphoxylose phosphatase 1 [Rattus norvegicus].
ACCESSION   NP_001007711 XP_236554
VERSION     NP_001007711.1
DBSOURCE    REFSEQ: accession NM_001007710.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Koike,T., Izumikawa,T., Sato,B. and Kitagawa,H.
  TITLE     Identification of phosphatase that dephosphorylates xylose in the
            glycosaminoglycan-protein linkage region of proteoglycans
  JOURNAL   J Biol Chem 289 (10), 6695-6708 (2014)
   PUBMED   24425863
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081981.1.
            
            On Nov 29, 2004 this sequence version replaced XP_236554.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081981.1, CV110731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q31"
     Protein         1..480
                     /product="2-phosphoxylose phosphatase 1"
                     /EC_number="3.1.3.2"
                     /note="acid phosphatase-like protein 2; acid
                     phosphatase-like 2"
                     /calculated_mol_wt=54828
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H78.1)"
     Region          87..424
                     /region_name="HP"
                     /note="Histidine phosphatase domain found in a
                     functionally diverse set of proteins, mostly phosphatases;
                     contains a His residue which is phosphorylated during the
                     reaction; cl11399"
                     /db_xref="CDD:472174"
     Site            order(96..97,100,209,378..379)
                     /site_type="active"
                     /note="catalytic core [active]"
                     /db_xref="CDD:132717"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q66H78.1)"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H78.1)"
     Site            354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q66H78.1)"
     CDS             1..480
                     /gene="Pxylp1"
                     /gene_synonym="Acpl2"
                     /coded_by="NM_001007710.1:97..1539"
                     /db_xref="GeneID:315939"
                     /db_xref="RGD:1359617"
ORIGIN      
        1 mlyrnrflvl lalagllafl slslqffhli pvsttknggs sksrkrimpd pvtepptvdp
       61 vyeallycni psvaehsmeg haphhyklvs vhvfirhgdr yplyaipktk rpeidctlva
      121 srkpyhpkle afvghmlkgs gasfesplgs lplypnhplc emgeltqtgv vqhlqngqll
      181 rdiylrkhkl lpnnwssdql ylettgksrt lqsglallyg flpefdwkkv yfkhqpsalf
      241 csgscycplr nqylekeqrr qyllrlknsd lertygemak ivdiptkqlr aanpidsmlc
      301 hfchnvsfpc srsgclgmeh fkvikthqie dererhekll yfgysllgah pilnqtvnrm
      361 qraalgwrde lftlysahdv tlspilsalg llearfprfa arlvfelwqd rqkpsehsvr
      421 ilyngadvtf htsfchdfhk hspkpmcple nlvrfvkrdm fvaldgsstn yydachgega
//
LOCUS       NP_001007676             281 aa            linear   ROD 28-APR-2025
DEFINITION  complement C1q tumor necrosis factor-related protein 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_001007676 XP_221139
VERSION     NP_001007676.1
DBSOURCE    REFSEQ: accession NM_001007675.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Jeon,J.H., Kim,K.Y., Kim,J.H., Baek,A., Cho,H., Lee,Y.H., Kim,J.W.,
            Kim,D., Han,S.H., Lim,J.S., Kim,K.I., Yoon,D.Y., Kim,S.H., Oh,G.T.,
            Kim,E. and Yang,Y.
  TITLE     A novel adipokine CTRP1 stimulates aldosterone production
  JOURNAL   FASEB J 22 (5), 1502-1511 (2008)
   PUBMED   18171693
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Kim,K.Y., Kim,H.Y., Kim,J.H., Lee,C.H., Kim,D.H., Lee,Y.H.,
            Han,S.H., Lim,J.S., Cho,D.H., Lee,M.S., Yoon,S., Kim,K.I.,
            Yoon,D.Y. and Yang,Y.
  TITLE     Tumor necrosis factor-alpha and interleukin-1beta increases CTRP1
            expression in adipose tissue
  JOURNAL   FEBS Lett 580 (16), 3953-3960 (2006)
   PUBMED   16806199
  REMARK    GeneRIF: These findings indicate that CTRP1 expression may be
            associated with a low-grade chronic inflammation status in adipose
            tissues.[Ctrp1]
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Lasser,G., Guchhait,P., Ellsworth,J.L., Sheppard,P., Lewis,K.,
            Bishop,P., Cruz,M.A., Lopez,J.A. and Fruebis,J.
  TITLE     C1qTNF-related protein-1 (CTRP-1): a vascular wall protein that
            inhibits collagen-induced platelet aggregation by blocking VWF
            binding to collagen
  JOURNAL   Blood 107 (2), 423-430 (2006)
   PUBMED   16195328
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Wong,G.W., Wang,J., Hug,C., Tsao,T.S. and Lodish,H.F.
  TITLE     A family of Acrp30/adiponectin structural and functional paralogs
  JOURNAL   Proc Natl Acad Sci U S A 101 (28), 10302-10307 (2004)
   PUBMED   15231994
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Innamorati,G., Whang,M.I., Molteni,R., Le Gouill,C. and
            Birnbaumer,M.
  TITLE     GIP, a G-protein-coupled receptor interacting protein
  JOURNAL   Regul Pept 109 (1-3), 173-179 (2002)
   PUBMED   12409230
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083720.1.
            
            On Nov 29, 2004 this sequence version replaced XP_221139.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083720.1, FQ209955.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.3"
     Protein         1..281
                     /product="complement C1q tumor necrosis factor-related
                     protein 1 precursor"
                     /note="complement C1q tumor necrosis factor-related
                     protein 1; C1q and tumor necrosis factor related protein
                     1"
                     /calculated_mol_wt=29463
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2597
     mat_peptide     26..281
                     /product="Complement C1q tumor necrosis factor-related
                     protein 1. /id=PRO_0000320082"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIG2.1)"
                     /calculated_mol_wt=29463
     Region          36..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIG2.1)"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5XIG2.1)"
     Region          98..>138
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          107..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIG2.1)"
     Region          147..275
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..281
                     /gene="C1qtnf1"
                     /gene_synonym="Ctrp1"
                     /coded_by="NM_001007675.1:266..1111"
                     /db_xref="GeneID:303701"
                     /db_xref="RGD:1359204"
ORIGIN      
        1 mgsrgqgfml gcclllavtw gpvlslvprv qeeqqeweet eeltspldhv trpeethkry
       61 spslreglpt srcyrccdsn ppvyqtippp qinitilkge kgdrgdrglq gkygkigstg
      121 prghigpkgq kgsmgapgdh cksqyaafsv grkkalhsnd yfqpvvfdte fvnlynhfnm
      181 ftgkfycyvp giyffslnvh twnqketylh imkneeevvi lyaqvsdrsi mqsqslmlel
      241 reqdevwvrl fkgerenaif sdefdtyitf sgylvkpase p
//
LOCUS       NP_001104765             357 aa            linear   ROD 28-APR-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein A3 isoform b [Rattus
            norvegicus].
ACCESSION   NP_001104765
VERSION     NP_001104765.1
DBSOURCE    REFSEQ: accession NM_001111295.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Mori,K., Nihei,Y., Arzberger,T., Zhou,Q., Mackenzie,I.R.,
            Hermann,A., Hanisch,F., Kamp,F., Nuscher,B., Orozco,D., Edbauer,D.
            and Haass,C.
  CONSRTM   German Consortium for Frontotemporal Lobar Degeneration; Bavarian
            Brain Banking Alliance
  TITLE     Reduced hnRNPA3 increases C9orf72 repeat RNA levels and
            dipeptide-repeat protein deposition
  JOURNAL   EMBO Rep 17 (9), 1314-1325 (2016)
   PUBMED   27461252
  REMARK    GeneRIF: Neurons in the hippocampus of C9orf72 patients are
            frequently devoid of hnRNPA3. Reduced nuclear hnRNPA3 in the
            hippocampus of patients with extended C9orf72 repeats correlates
            with increased DPR deposition.
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Todd,M.A. and Picketts,D.J.
  TITLE     PHF6 interacts with the nucleosome remodeling and deacetylation
            (NuRD) complex
  JOURNAL   J Proteome Res 11 (8), 4326-4337 (2012)
   PUBMED   22720776
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Chen,J.J., Jiang,H.Y., Liu,P., Liu,W., Wei,M.T., Wang,S.X. and
            Weng,Y.G.
  TITLE     [Differential analysis of two-dimensional gel electrophoresis
            profiles in lung tissue of rats exposed to silica early]
  JOURNAL   Zhonghua Yu Fang Yi Xue Za Zhi 43 (5), 418-422 (2009)
   PUBMED   19534998
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Shultz,M.A., Zhang,L., Gu,Y.Z., Baker,G.L., Fannuchi,M.V.,
            Padua,A.M., Gurske,W.A., Morin,D., Penn,S.G., Jovanovich,S.B.,
            Plopper,C.G. and Buckpitt,A.R.
  TITLE     Gene expression analysis in response to lung toxicants: I.
            Sequencing and microarray development
  JOURNAL   Am J Respir Cell Mol Biol 30 (3), 296-310 (2004)
   PUBMED   12947022
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Ma,A.S., Moran-Jones,K., Shan,J., Munro,T.P., Snee,M.J., Hoek,K.S.
            and Smith,R.
  TITLE     Heterogeneous nuclear ribonucleoprotein A3, a novel RNA trafficking
            response element-binding protein
  JOURNAL   J Biol Chem 277 (20), 18010-18020 (2002)
   PUBMED   11886857
  REMARK    GeneRIF: has a role in cytoplasmic trafficking of RNA (heterogenous
            nuclear ribonucleoprotein A3)
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Percipalle,P., Jonsson,A., Nashchekin,D., Karlsson,C., Bergman,T.,
            Guialis,A. and Daneholt,B.
  TITLE     Nuclear actin is associated with a specific subset of hnRNP
            A/B-type proteins
  JOURNAL   Nucleic Acids Res 30 (8), 1725-1734 (2002)
   PUBMED   11937625
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Plomaritoglou,A., Choli-Papadopoulou,T. and Guialis,A.
  TITLE     Molecular characterization of a murine, major A/B type hnRNP
            protein: mBx
  JOURNAL   Biochim Biophys Acta 1490 (1-2), 54-62 (2000)
   PUBMED   10786617
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB585714.1, CB725005.1 and BC081878.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ214617.1, SRR8487231.108729.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..357
                     /product="heterogeneous nuclear ribonucleoprotein A3
                     isoform b"
                     /note="hnRNP A3"
                     /calculated_mol_wt=36955
     Region          11..91
                     /region_name="RRM1_hnRNPA3"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) and
                     similar proteins; cd12763"
                     /db_xref="CDD:410156"
     Site            order(14,16,18..19,41,43,45,54..56,58,81,84,86..91)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410156"
     Region          104..183
                     /region_name="RRM2_hnRNPA3"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A3 (hnRNP A3) and
                     similar proteins; cd12582"
                     /db_xref="CDD:409996"
     Region          310..>326
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..357
                     /gene="Hnrnpa3"
                     /gene_synonym="Hnrpa3; mBx"
                     /coded_by="NM_001111295.1:81..1154"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:362152"
                     /db_xref="RGD:727807"
ORIGIN      
        1 meghdpkepe qlrklfiggl sfettddslr ehfekwgtlt dcvvmrdpqt krsrgfgfvt
       61 yscveevdaa mcarphkvdg rvvepkravs redsvkpgah ltvkkifvgg ikedteeynl
      121 rdyfekygki etievmedrq sgkkrgfafv tfddhdtvdk ivvqkyhtin ghncevkkal
      181 skqemqsags qrgrgggsgn fmgrggnfgg gggnfgrggn fggrggyggg gggsrgsygg
      241 gdggyngfgg dggnygggpg yssrggyggg gpgygnqggg yggggggydg yneggnfggg
      301 nyggggnynd fgnysgqqqs nygpmkggsf ggrssgspyg ggygsgggsg gygsrrf
//
LOCUS       NP_001013932             340 aa            linear   ROD 28-APR-2025
DEFINITION  guanine nucleotide-binding protein subunit beta-4 [Rattus
            norvegicus].
ACCESSION   NP_001013932 XP_227042
VERSION     NP_001013932.1
DBSOURCE    REFSEQ: accession NM_001013910.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Ahmed,S.M., Theriault,B.L., Uppalapati,M., Chiu,C.W., Gallie,B.L.,
            Sidhu,S.S. and Angers,S.
  TITLE     KIF14 negatively regulates Rap1a-Radil signaling during breast
            cancer progression
  JOURNAL   J Cell Biol 199 (6), 951-967 (2012)
   PUBMED   23209302
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Mahmoud,S., Yun,J.K. and Ruiz-Velasco,V.
  TITLE     Gbeta2 and Gbeta4 participate in the opioid and adrenergic
            receptor-mediated Ca2+ channel modulation in rat sympathetic
            neurons
  JOURNAL   J Physiol 590 (19), 4673-4689 (2012)
   PUBMED   22711958
  REMARK    GeneRIF: Gnb2 and Gnb4 participate in the opioid and adrenergic
            receptor-mediated Ca2+ channel modulation in rat sympathetic
            neurons
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Liang,J.J., Cockett,M. and Khawaja,X.Z.
  TITLE     Immunohistochemical localization of G protein beta1, beta2, beta3,
            beta4, beta5, and gamma3 subunits in the adult rat brain
  JOURNAL   J Neurochem 71 (1), 345-355 (1998)
   PUBMED   9648884
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Betty,M., Harnish,S.W., Rhodes,K.J. and Cockett,M.I.
  TITLE     Distribution of heterotrimeric G-protein beta and gamma subunits in
            the rat brain
  JOURNAL   Neuroscience 85 (2), 475-486 (1998)
   PUBMED   9622245
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097370.1.
            
            On Apr 20, 2005 this sequence version replaced XP_227042.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097370.1, AY552804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q24"
     Protein         1..340
                     /product="guanine nucleotide-binding protein subunit
                     beta-4"
                     /note="G-protein beta 4 subunit; guanine
                     nucleotide-binding protein subunit beta-4-like; guanine
                     nucleotide binding protein (G protein), beta polypeptide
                     4; transducin beta chain 4; guanine nucleotide binding
                     protein beta 4 subunit; guanine nucleotide binding
                     protein, beta 4; guanine nucleotide binding protein (G
                     protein), beta 4"
                     /calculated_mol_wt=37232
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HAV0; propagated from
                     UniProtKB/Swiss-Prot (O35353.4)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62873; propagated from
                     UniProtKB/Swiss-Prot (O35353.4)"
     Region          48..340
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          53..92
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Site            order(54,72,76,82..83,95..96,114,118,124..125,141..142,
                     159,163,169..170,183,201,205,211..212,224..225,243,247,
                     253..254,265..266,286,291,297..298,310..311,329,333,
                     339..340)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          58..95
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          95..134
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          101..141
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          141..179
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          146..181
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..221
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          188..223
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          224..263
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          229..265
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphohistidine.
                     /evidence=ECO:0000250|UniProtKB:P62871; propagated from
                     UniProtKB/Swiss-Prot (O35353.4)"
     Region          268..307
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          273..309
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          310..339
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O35353.4)"
     Region          315..339
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..340
                     /gene="Gnb4"
                     /coded_by="NM_001013910.2:74..1096"
                     /db_xref="GeneID:294962"
                     /db_xref="RGD:1359321"
ORIGIN      
        1 mseleqlrqe aeqlrnqiqd arkacndatl vqitsnmdsv griqmrtrrt lrghlakiya
       61 mhwgydsrll vsasqdgkli iwdsyttnkm haiplrsswv mtcayapsgn yvacggldni
      121 csiynlktre gnvrvsrelp ghtgylsccr flddgqiits sgdttcalwd ietgqqtttf
      181 tghsgdvmsl slspdlktfv sgacdasskl wdirdgmcrq sftghisdin avsffpsgya
      241 fatgsddatc rlfdlradqe lllyshdnii cgitsvafsk sgrlllagyd dfncsvwdal
      301 kggragvlag hdnrvsclgv tddgmavatg swdsflriwn
//
LOCUS       NP_001004094             255 aa            linear   ROD 28-APR-2025
DEFINITION  proteasome subunit alpha type-3 [Rattus norvegicus].
ACCESSION   NP_001004094
VERSION     NP_001004094.1
DBSOURCE    REFSEQ: accession NM_001004094.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Bingol,B. and Schuman,E.M.
  TITLE     Activity-dependent dynamics and sequestration of proteasomes in
            dendritic spines
  JOURNAL   Nature 441 (7097), 1144-1148 (2006)
   PUBMED   16810255
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Tanaka,K., Kanayama,H., Tamura,T., Lee,D.H., Kumatori,A.,
            Fujiwara,T., Ichihara,A., Tokunaga,F., Aruga,R. and Iwanaga,S.
  TITLE     cDNA cloning and sequencing of component C8 of proteasomes from rat
            hepatoma cells
  JOURNAL   Biochem Biophys Res Commun 171 (2), 676-683 (1990)
   PUBMED   2403356
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M58593.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: M58593.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q25"
     Protein         1..255
                     /product="proteasome subunit alpha type-3"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit C8; proteasome subunit K;
                     proteasome component C8; multicatalytic endopeptidase
                     complex subunit C8; alpha-7; proteasome subunit alpha-7"
                     /calculated_mol_wt=28288
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:2335242; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     Region          5..217
                     /region_name="proteasome_alpha_type_3"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03751"
                     /db_xref="CDD:239720"
     Site            order(10..13,15..16,18..19,23,26,29..30,33,41,56,58..59,
                     82..84,86..87,118,121,124..125,128..132,150,155..156,158,
                     160..161,163)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239720"
     Site            order(35,51,53,66,168)
                     /site_type="active"
                     /db_xref="CDD:239720"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P25788; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     Site            206
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P25788; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     Site            230
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P25788; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P18422.3)"
     CDS             1..255
                     /gene="Psma3l"
                     /coded_by="NM_001004094.1:28..795"
                     /db_xref="GeneID:408248"
                     /db_xref="RGD:1598236"
ORIGIN      
        1 mssigtgydl sastfspdgr vfqveyamka vensstaigi rckdgvvfgv eklvlsklye
       61 egsnkrlfnv drhvgmavag lladarslad iareeasnfr snfgyniplk hladrvamyv
      121 haytlysavr pfgcsfmlgs ysvndgaqly midpsgvsyg ywgcaigkar qaakteiekl
      181 qmkemtcrdv vkevakiiyi vhdevkdkaf elelswvgel tkgrheivpk dvreeaekya
      241 keslkeedes dddnm
//
LOCUS       NP_001032884             113 aa            linear   ROD 28-APR-2025
DEFINITION  protein FMC1 homolog [Rattus norvegicus].
ACCESSION   NP_001032884 XP_575438
VERSION     NP_001032884.1
DBSOURCE    REFSEQ: accession NM_001037795.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Li,Y., Jourdain,A.A., Calvo,S.E., Liu,J.S. and Mootha,V.K.
  TITLE     CLIC, a tool for expanding biological pathways based on
            co-expression across thousands of datasets
  JOURNAL   PLoS Comput Biol 13 (7), e1005653 (2017)
   PUBMED   28719601
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Higashi,S., Katagi,K., Shintani,N., Ikeda,K., Sugimoto,Y.,
            Tsuchiya,S., Inoue,N., Tanaka,S., Koumoto,M., Kasai,A.,
            Nakazawa,T., Hayata-Takano,A., Hamagami,K., Tomimoto,S.,
            Yoshida,T., Ohkubo,T., Nagayasu,K., Ago,Y., Onaka,Y., Hashimoto,R.,
            Ichikawa,A., Baba,A. and Hashimoto,H.
  TITLE     p13 overexpression in pancreatic beta-cells ameliorates type 2
            diabetes in high-fat-fed mice
  JOURNAL   Biochem Biophys Res Commun 461 (4), 612-617 (2015)
   PUBMED   25912136
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098843.1.
            
            On Dec 16, 2005 this sequence version replaced XP_575438.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098843.1, AW921139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..113
                     /product="protein FMC1 homolog"
                     /note="UPF0562 protein C7orf55 homolog; formation of
                     mitochondrial complexes 1 homolog; formation of
                     mitochondrial complex V assembly factor 1 homolog"
                     /calculated_mol_wt=12613
     Region          7..103
                     /region_name="Complex1_LYR_FMC1"
                     /note="LYR (leucine-tyrosine-arginine) motif found in
                     formation of mitochondrial complex V assembly factor 1
                     (FMC1) and similar proteins; cd20271"
                     /db_xref="CDD:380766"
     Region          94..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G012.1)"
     CDS             1..113
                     /gene="Fmc1"
                     /coded_by="NM_001037795.1:50..391"
                     /db_xref="GeneID:500087"
                     /db_xref="RGD:1559476"
ORIGIN      
        1 maalgspart lrgllrelry lnaatgrpyr dtaayrylvk afrahrvtse klcraqhelh
       61 fqaatylcll rsirqhvalh qefhgkgers veesaglvgl qlphqpggkg wep
//
LOCUS       NP_114190                261 aa            linear   ROD 28-APR-2025
DEFINITION  calbindin [Rattus norvegicus].
ACCESSION   NP_114190
VERSION     NP_114190.1
DBSOURCE    REFSEQ: accession NM_031984.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Varshney,S., Adela,R., Kachhawa,G., Dada,R., Kulshreshtha,V.,
            Kumari,R., Agarwal,R. and Khadgawat,R.
  TITLE     Disrupted placental vitamin D metabolism and calcium signaling in
            gestational diabetes and pre-eclampsia patients
  JOURNAL   Endocrine 80 (1), 191-200 (2023)
   PUBMED   36477942
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Vishnyakova,P.A., Moiseev,K.Y., Spirichev,A.A., Emanuilov,A.I.,
            Nozdrachev,A.D. and Masliukov,P.M.
  TITLE     Expression of calbindin and calretinin in the dorsomedial and
            ventromedial hypothalamic nuclei during aging
  JOURNAL   Anat Rec (Hoboken) 304 (5), 1094-1104 (2021)
   PUBMED   33040447
  REMARK    GeneRIF: Expression of calbindin and calretinin in the dorsomedial
            and ventromedial hypothalamic nuclei during aging.
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Silva-Pena,D., Garcia-Marchena,N., Alen,F., Araos,P., Rivera,P.,
            Vargas,A., Garcia-Fernandez,M.I., Martin-Velasco,A.I.,
            Villanua,M.A., Castilla-Ortega,E., Santin,L., Pavon,F.J.,
            Serrano,A., Rubio,G., Rodriguez de Fonseca,F. and Suarez,J.
  TITLE     Alcohol-induced cognitive deficits are associated with decreased
            circulating levels of the neurotrophin BDNF in humans and rats
  JOURNAL   Addict Biol 24 (5), 1019-1033 (2019)
   PUBMED   30277635
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Noble,J.W., Almalki,R., Roe,S.M., Wagner,A., Duman,R. and
            Atack,J.R.
  TITLE     The X-ray structure of human calbindin-D28K: an improved model
  JOURNAL   Acta Crystallogr D Struct Biol 74 (Pt 10), 1008-1014 (2018)
   PUBMED   30289411
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Stebbing,M.J., Balasubramanyan,S. and Smith,P.A.
  TITLE     Calbindin-D-28K like immunoreactivity in superficial dorsal horn
            neurons and effects of sciatic chronic constriction injury
  JOURNAL   Neuroscience 324, 330-343 (2016)
   PUBMED   26975894
  REMARK    GeneRIF: Calbindin D-28K does not appear to associate with any
            particular neuronal phenotype in the spinal dorsal horn, which may
            reflect that fact that most morphological types can be excitatory
            or inhibitory Its expression and distribution is unaffected by
            chronic constriction injury and increased excitatory synaptic drive
            to Cal+ neurons is unlikely to play a role in chronic constriction
            injury-induced central sensitization
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Gabrielides,C., McCormack,A.L., Hunt,D.F. and Christakos,S.
  TITLE     Brain calbindin-D28k and an Mr 29,000 calcium binding protein in
            cerebellum are different but related proteins: evidence obtained
            from sequence analysis by tandem mass spectrometry
  JOURNAL   Biochemistry 30 (3), 656-662 (1991)
   PUBMED   1988053
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Lomri,N., Perret,C., Gouhier,N. and Thomasset,M.
  TITLE     Cloning and analysis of calbindin-D28K cDNA and its expression in
            the central nervous system
  JOURNAL   Gene 80 (1), 87-98 (1989)
   PUBMED   2792772
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Gross,M.D., Kumar,R. and Hunziker,W.
  TITLE     Expression in Escherichia coli of full-length and mutant rat brain
            calbindin D28. Comparison with the purified native protein
  JOURNAL   J Biol Chem 263 (28), 14426-14432 (1988)
   PUBMED   3049577
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Hunziker,W. and Schrickel,S.
  TITLE     Rat brain calbindin D28: six domain structure and extensive amino
            acid homology with chicken calbindin D28
  JOURNAL   Mol Endocrinol 2 (5), 465-473 (1988)
   PUBMED   2843757
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Yamakuni,T., Kuwano,R., Odani,S., Miki,N., Yamaguchi,K. and
            Takahashi,Y.
  TITLE     Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein
  JOURNAL   J Neurochem 48 (5), 1590-1596 (1987)
   PUBMED   3031218
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK479935.1 and BC081764.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081764.1, X04280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..261
                     /product="calbindin"
                     /note="calbindin 1, 28 kD; cerebellar Ca-binding protein,
                     spot 35 protein; vitamin D-dependent calcium-binding
                     protein, avian-type; D-28K; calbindin D28"
                     /calculated_mol_wt=29863
     Region          2..7
                     /region_name="Interaction with RANBP9.
                     /evidence=ECO:0000250|UniProtKB:P05937"
                     /note="propagated from UniProtKB/Swiss-Prot (P07171.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1988053; propagated from
                     UniProtKB/Swiss-Prot (P07171.2)"
     Region          16..259
                     /region_name="EFh_HEF_CB"
                     /note="EF-hand, calcium binding motif, found in calbindin
                     (CB); cd16176"
                     /db_xref="CDD:320076"
     Region          16..44
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     Site            order(24,26,28,35,111,113,115,122,155,157,159,166,199,201,
                     203,210)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320076"
     Region          57..86
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     Region          102..131
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     Region          146..175
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     Region          190..219
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     Region          231..259
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320076"
     CDS             1..261
                     /gene="Calb1"
                     /gene_synonym="CaBP28K"
                     /coded_by="NM_031984.2:116..901"
                     /db_xref="GeneID:83839"
                     /db_xref="RGD:69340"
ORIGIN      
        1 maeshlqssl itasqffeiw lhfdadgsgy legkelqnli qellqarkka glelspemkt
       61 fvdqygqrdd gkigivelah vlpteenfll lfrcqqlksc eefmktwrky dtdhsgfiet
      121 eelknflkdl lekanktvdd tklaeytdlm lklfdsnndg kleltemarl lpvqenfllk
      181 fqgikmcgke fnkafelydq dgngyidene ldallkdlce knkqeldinn istykknima
      241 lsdggklyrt dlalilsagd n
//
LOCUS       NP_001012761             539 aa            linear   ROD 28-APR-2025
DEFINITION  phosphatidylinositol 4-phosphate 5-kinase type-1 beta [Rattus
            norvegicus].
ACCESSION   NP_001012761 XP_219913
VERSION     NP_001012761.1
DBSOURCE    REFSEQ: accession NM_001012743.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Liu,T. and Lee,S.Y.
  TITLE     Phosphatidylinositol 4-phosphate 5-kinase alpha negatively
            regulates nerve growth factor-induced neurite outgrowth in PC12
            cells
  JOURNAL   Exp Mol Med 45 (3), e16 (2013)
   PUBMED   23538529
  REMARK    GeneRIF: PIP5Kalpha acts as a negative regulator of nerve growth
            factor-induced neurite outgrowth by inhibiting PI3K/Akt signaling
            pathway in PC12 cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Lee,S.Y., Kim,B., Yoon,S., Kim,Y.J., Liu,T., Woo,J.H., Chwae,Y.J.,
            Joe,E.H. and Jou,I.
  TITLE     Phosphatidylinositol 4-phosphate 5-kinase alpha is induced in
            ganglioside-stimulated brain astrocytes and contributes to
            inflammatory responses
  JOURNAL   Exp Mol Med 42 (9), 662-673 (2010)
   PUBMED   20720456
  REMARK    GeneRIF: Ganglioside treatment of primary astrocytes enhances
            PIP5Kalpha expression. PIP5Kalpha knockdown attenuates
            ganglioside-induced inflammatory responses.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Volpicelli-Daley,L.A., Lucast,L., Gong,L.W., Liu,L., Sasaki,J.,
            Sasaki,T., Abrams,C.S., Kanaho,Y. and De Camilli,P.
  TITLE     Phosphatidylinositol-4-phosphate 5-kinases and phosphatidylinositol
            4,5-bisphosphate synthesis in the brain
  JOURNAL   J Biol Chem 285 (37), 28708-28714 (2010)
   PUBMED   20622009
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Manes,S., Fuentes,G., Peregil,R.M., Rojas,A.M. and Lacalle,R.A.
  TITLE     An isoform-specific PDZ-binding motif targets type I PIP5 kinase
            beta to the uropod and controls polarization of neutrophil-like
            HL60 cells
  JOURNAL   FASEB J 24 (9), 3381-3392 (2010)
   PUBMED   20442317
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Vasudevan,L., Jeromin,A., Volpicelli-Daley,L., De Camilli,P.,
            Holowka,D. and Baird,B.
  TITLE     The beta- and gamma-isoforms of type I PIP5K regulate distinct
            stages of Ca2+ signaling in mast cells
  JOURNAL   J Cell Sci 122 (Pt 14), 2567-2574 (2009)
   PUBMED   19549683
  REMARK    GeneRIF: The beta- and gamma-isoforms of type I PIP5K regulate
            distinct stages of Ca2+ signaling in mast cells.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Ishihara,H., Shibasaki,Y., Kizuki,N., Katagiri,H., Yazaki,Y.,
            Asano,T. and Oka,Y.
  TITLE     Cloning of cDNAs encoding two isoforms of 68-kDa type I
            phosphatidylinositol-4-phosphate 5-kinase
  JOURNAL   J Biol Chem 271 (39), 23611-23614 (1996)
   PUBMED   8798574
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090349.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219913.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090349.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q51"
     Protein         1..539
                     /product="phosphatidylinositol 4-phosphate 5-kinase type-1
                     beta"
                     /EC_number="2.7.1.68"
                     /note="PIP5KIbeta; PIP5KIalpha; ptdIns(4)P-5-kinase beta;
                     PIP5K1-beta; ptdIns(4)P-5-kinase 1 beta;
                     phosphatidylinositol-4-phosphate 5-kinase, type 1 alpha;
                     phosphatidylinositol 4-phosphate 5-kinase type I beta;
                     phosphatidylinositol 4-phosphate 5-kinase type I alpha"
                     /calculated_mol_wt=60602
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5CZZ9.1)"
     Region          27..400
                     /region_name="PIPKc_PIP5K1B"
                     /note="Phosphatidylinositol phosphate kinase (PIPK)
                     catalytic domain found in phosphatidylinositol 4-phosphate
                     5-kinase type-1 beta (PIP5K1beta) and similar proteins;
                     cd17307"
                     /db_xref="CDD:340444"
     Site            order(50..55,57,93,153,156..157,161..162,254,257,261)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:340444"
     Site            order(120..123,125,127,136,138,188..191,203,224,270,
                     349..350)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340444"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5CZZ9.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70181; propagated from
                     UniProtKB/Swiss-Prot (Q5CZZ9.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5CZZ9.1)"
     CDS             1..539
                     /gene="Pip5k1b"
                     /gene_synonym="Pip5k1a"
                     /coded_by="NM_001012743.1:528..2147"
                     /db_xref="GeneID:309419"
                     /db_xref="RGD:1310914"
ORIGIN      
        1 msstaengda vpgkqneekt ykktassaik gaiqlgigyt vgnltskper dvlmqdfyvv
       61 esvflpsegs nltpahhypd frfktyapla fryfrelfgi kpddylysic seplielsnp
      121 gasgslfflt sddefiiktv qhkeaeflqk llpgyymnln qnprtllpkf yglycmqsgg
      181 inirivvmnn vlpramrmhl tydlkgstyk rrasrkerek pnptfkdldf lqdmheglyf
      241 dtetynalmk tlqrdcrvle sfkimdysll lgihildhsl kdkeeeplqn apdakrpgmq
      301 kvlystames iqgpgksadg iiaenpdtmg gipakshkge klllfmgiid ilqsyrlmkk
      361 lehswkalvy dgdtvsvhrp sfyadrflkf mnsrvfkkiq alkaspskkr cnsiaalkat
      421 sqeilssisq ewkdekqdll tegqsfssld eealgsrhrp dlvpstpslf eaaslattis
      481 ssslyvgehy phdrttlysn skglpssstf tleegtiylt aepnaletqd dasvldvyl
//
LOCUS       NP_062053                274 aa            linear   ROD 28-APR-2025
DEFINITION  tryptase beta-2 precursor [Rattus norvegicus].
ACCESSION   NP_062053
VERSION     NP_062053.2
DBSOURCE    REFSEQ: accession NM_019180.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Taketomi,Y., Ueno,N., Kojima,T., Sato,H., Murase,R., Yamamoto,K.,
            Tanaka,S., Sakanaka,M., Nakamura,M., Nishito,Y., Kawana,M.,
            Kambe,N., Ikeda,K., Taguchi,R., Nakamizo,S., Kabashima,K.,
            Gelb,M.H., Arita,M., Yokomizo,T., Nakamura,M., Watanabe,K.,
            Hirai,H., Nakamura,M., Okayama,Y., Ra,C., Aritake,K., Urade,Y.,
            Morimoto,K., Sugimoto,Y., Shimizu,T., Narumiya,S., Hara,S. and
            Murakami,M.
  TITLE     Mast cell maturation is driven via a group III phospholipase
            A2-prostaglandin D2-DP1 receptor paracrine axis
  JOURNAL   Nat Immunol 14 (6), 554-563 (2013)
   PUBMED   23624557
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Hallgren,J., Spillmann,D. and Pejler,G.
  TITLE     Structural requirements and mechanism for heparin-induced
            activation of a recombinant mouse mast cell tryptase, mouse mast
            cell protease-6: formation of active tryptase monomers in the
            presence of low molecular weight heparin
  JOURNAL   J Biol Chem 276 (46), 42774-42781 (2001)
   PUBMED   11533057
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Lutzelschwab,C., Pejler,G., Aveskogh,M. and Hellman,L.
  TITLE     Secretory granule proteases in rat mast cells. Cloning of 10
            different serine proteases and a carboxypeptidase A from various
            rat mast cell populations
  JOURNAL   J Exp Med 185 (1), 13-29 (1997)
   PUBMED   8996238
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Ide,H., Itoh,H., Tomita,M., Murakumo,Y., Kobayashi,T., Maruyama,H.,
            Osada,Y. and Nawa,Y.
  TITLE     cDNA sequencing and expression of rat mast cell tryptase
  JOURNAL   J Biochem 118 (1), 210-215 (1995)
   PUBMED   8537314
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U67909.1.
            
            On Jun 3, 2010 this sequence version replaced NP_062053.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U67909.1, D38455.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..274
                     /product="tryptase beta-2 precursor"
                     /EC_number="3.4.21.59"
                     /note="mast cell protease 6; rMCP-6; tryptase-2"
                     /calculated_mol_wt=28499
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2017
     mat_peptide     30..274
                     /product="Tryptase beta-2. /id=PRO_0000027493"
                     /note="propagated from UniProtKB/Swiss-Prot (P50343.1)"
                     /calculated_mol_wt=27462
     Region          30..268
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            30
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(73,120,223)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P21845; propagated from
                     UniProtKB/Swiss-Prot (P50343.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50343.1)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P50343.1)"
     Site            order(217,242,244)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..274
                     /gene="Tpsb2"
                     /gene_synonym="Mcpt6"
                     /coded_by="NM_019180.2:16..840"
                     /db_xref="GeneID:29268"
                     /db_xref="RGD:3065"
ORIGIN      
        1 mlklllllal splaslvhaa pcpvkqrvgi vggreasesk wpwqvslrfk fsfwmhfcgg
       61 slihpqwvlt aahcvglhik spelfrvqlr eqylyyadql ltvnrtvvhp hyytvedgad
      121 iallelenpv nvsthihpts lppasetfps gtscwvtgwg didsdepllp pyplkqvkvp
      181 ivenslcdrk yhtglytgdd vpivqdgmlc agntrsdscq gdsggplvck vkgtwlqagv
      241 vswgegcaea nrpgiytrvt yyldwihryv pqrs
//
LOCUS       NP_113953                463 aa            linear   ROD 28-APR-2025
DEFINITION  retinoic acid receptor RXR-gamma [Rattus norvegicus].
ACCESSION   NP_113953 XP_341152
VERSION     NP_113953.1
DBSOURCE    REFSEQ: accession NM_031765.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Huang,W., Li,K., Liu,A., Yang,Z., Hu,C., Chen,D. and Wang,H.
  TITLE     miR-330-5p inhibits H2O2-induced adipogenic differentiation of MSCs
            by regulating RXRgamma
  JOURNAL   Int J Mol Med 42 (4), 2042-2052 (2018)
   PUBMED   30015907
  REMARK    GeneRIF: the results of the present study revealed that miR3305p
            acts as a critical regulator of RXRgamma, and is able to
            determinate the fate of MSCs to differentiate into adipocytes. This
            suggests that miR3305p and RXRgamma may be target molecules for
            controlling metabolic diseases.
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Dong,T., Zhang,Z., Zhou,W., Zhou,X., Geng,C., Chang,L.K., Tian,X.
            and Liu,S.
  TITLE     WNT10A/beta-catenin pathway in tumorigenesis of papillary thyroid
            carcinoma
  JOURNAL   Oncol Rep 38 (2), 1287-1294 (2017)
   PUBMED   28677753
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Arfaoui,A., Lobo,M.V., Boulbaroud,S., Ouichou,A., Mesfioui,A. and
            Arenas,M.I.
  TITLE     Expression of retinoic acid receptors and retinoid X receptors in
            normal and vitamin A deficient adult rat brain
  JOURNAL   Ann Anat 195 (2), 111-121 (2013)
   PUBMED   23017197
  REMARK    GeneRIF: RXRgamma was absent in the female rat brain, while it was
            observed in some regions in the male.
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Latasa,M.J., Ituero,M., Moran-Gonzalez,A., Aranda,A. and
            Cosgaya,J.M.
  TITLE     Retinoic acid regulates myelin formation in the peripheral nervous
            system
  JOURNAL   Glia 58 (12), 1451-1464 (2010)
   PUBMED   20648638
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Lee,S.M., Lee,J.Y., Choi,J.E., Lee,S.Y., Park,J.Y. and Kim,D.S.
  TITLE     Epigenetic inactivation of retinoid X receptor genes in non-small
            cell lung cancer and the relationship with clinicopathologic
            features
  JOURNAL   Cancer Genet Cytogenet 197 (1), 39-45 (2010)
   PUBMED   20113835
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Georgiades,P. and Brickell,P.M.
  TITLE     Differential expression of the rat retinoid X receptor gamma gene
            during skeletal muscle differentiation suggests a role in
            myogenesis
  JOURNAL   Dev Dyn 210 (3), 227-235 (1997)
   PUBMED   9389449
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Ben-Shushan,E., Sharir,H., Pikarsky,E. and Bergman,Y.
  TITLE     A dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and
            retinoic acid receptor:retinoid X receptor heterodimers regulates
            Oct-3/4 expression in embryonal carcinoma cells
  JOURNAL   Mol Cell Biol 15 (2), 1034-1048 (1995)
   PUBMED   7823919
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Chen,H. and Privalsky,M.L.
  TITLE     Cooperative formation of high-order oligomers by retinoid X
            receptors: an unexpected mode of DNA recognition
  JOURNAL   Proc Natl Acad Sci U S A 92 (2), 422-426 (1995)
   PUBMED   7831303
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Liu,Q. and Linney,E.
  TITLE     The mouse retinoid-X receptor-gamma gene: genomic organization and
            evidence for functional isoforms
  JOURNAL   Mol Endocrinol 7 (5), 651-658 (1993)
   PUBMED   8391126
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Mangelsdorf,D.J., Borgmeyer,U., Heyman,R.A., Zhou,J.Y., Ong,E.S.,
            Oro,A.E., Kakizuka,A. and Evans,R.M.
  TITLE     Characterization of three RXR genes that mediate the action of
            9-cis retinoic acid
  JOURNAL   Genes Dev 6 (3), 329-344 (1992)
   PUBMED   1312497
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091363.1.
            
            On Apr 19, 2005 this sequence version replaced XP_341152.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..463
                     /product="retinoic acid receptor RXR-gamma"
                     /note="RXR gamma-1; retinoic X receptor gamma-1; nuclear
                     receptor subfamily 2 group B member 3; retinoic acid
                     receptor RXR-gamma-like"
                     /calculated_mol_wt=50762
     Region          1..138
                     /region_name="Modulating. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJR8.1)"
     Region          16..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJR8.1)"
     Region          25..134
                     /region_name="Nuc_recep-AF1"
                     /note="Nuclear/hormone receptor activator site AF-1;
                     pfam11825"
                     /db_xref="CDD:463363"
     Region          137..213
                     /region_name="NR_DBD_RXR"
                     /note="DNA-binding domain of retinoid X receptor (RXR) is
                     composed of two C4-type zinc fingers; cd06956"
                     /db_xref="CDD:143514"
     Site            order(139,142,156,159,175,181,191,194)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143514"
     Site            order(144,185..186,188,190)
                     /site_type="other"
                     /note="RXR/ECR heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:143514"
     Site            order(148..151,157..158,160,162,164..165,168,176,188..189,
                     192,195,208..210,212..213)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143514"
     Site            order(170,193,196..197,200..201,205..207,211..213)
                     /site_type="other"
                     /note="RXR/PPAR heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:143514"
     Site            order(186..187,190)
                     /site_type="other"
                     /note="RXR/RXR homodimer interface DR1 [polypeptide
                     binding]"
                     /db_xref="CDD:143514"
     Region          205..230
                     /region_name="Hinge"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJR8.1)"
     Site            207..212
                     /site_type="other"
                     /note="RXR/RXR homodimer interface DR2 [polypeptide
                     binding]"
                     /db_xref="CDD:143514"
     Site            order(211,213)
                     /site_type="other"
                     /note="RXR/RAR heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:143514"
     Region          233..441
                     /region_name="NR_LBD_RXR_like"
                     /note="The ligand binding domain of the retinoid X
                     receptor and Ultraspiracle, members of nuclear receptor
                     superfamily; cd06943"
                     /db_xref="CDD:132741"
     Site            order(269..270,272..273,276,310,314,317,327..328,343,433,
                     436..437)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132741"
     Site            order(278,281,285,290,295..296,298..299,303)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132741"
     Site            order(349,353,357,374,380,394..395,398..399,402,416..417,
                     420..421,423..425,427..428,431,435)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:132741"
     Site            order(349,353,357,380,382,391,398,402,414,417..418,
                     421..424,427..428,431,435)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:132741"
     CDS             1..463
                     /gene="Rxrg"
                     /coded_by="NM_031765.1:231..1622"
                     /db_xref="GeneID:83574"
                     /db_xref="RGD:620046"
ORIGIN      
        1 mygnyshfmk fptgfggspg htgstsmsps valptgkpmd shpsytdtpv saprtlsavg
       61 tplnalgspy rvitsamgpp sgalaappgi nlvvppssql nvvnsvssse dikplpglpg
      121 ignmnypsts pgslvkhica icgdrssgkh ygvyscegck gffkrtirkd liytcrdnkd
      181 clidkrqrnr cqycryqkcl vmgmkreavq eerqrsrera eseaecastg hedmpveril
      241 eaelavepkt esygdmsves stndpvtnic haadkqlftl vewakriphf sdltledqvi
      301 llragwnell iasfshrsvs vqdgillatg lhvhrssahs agvgsifdrv ltelvskmkd
      361 mrmdkselgc lraivlfnpd akglsnpsev etlrekvyat leaytkqkyp eqpgrfakll
      421 lrlpalrsig lkclehlfff kligdtpidt flmemletpl qit
//
LOCUS       NP_001012121             387 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich protein 5 [Rattus norvegicus].
ACCESSION   NP_001012121 XP_235544
VERSION     NP_001012121.1
DBSOURCE    REFSEQ: accession NM_001012121.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Gan,X., Wang,J., Wang,C., Sommer,E., Kozasa,T., Srinivasula,S.,
            Alessi,D., Offermanns,S., Simon,M.I. and Wu,D.
  TITLE     PRR5L degradation promotes mTORC2-mediated PKC-delta
            phosphorylation and cell migration downstream of Galpha12
  JOURNAL   Nat Cell Biol 14 (7), 686-696 (2012)
   PUBMED   22609986
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Laplante,M. and Sabatini,D.M.
  TITLE     mTOR signaling in growth control and disease
  JOURNAL   Cell 149 (2), 274-293 (2012)
   PUBMED   22500797
  REMARK    Review article
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Pearce,L.R., Sommer,E.M., Sakamoto,K., Wullschleger,S. and
            Alessi,D.R.
  TITLE     Protor-1 is required for efficient mTORC2-mediated activation of
            SGK1 in the kidney
  JOURNAL   Biochem J 436 (1), 169-179 (2011)
   PUBMED   21413931
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC090007.1.
            
            On Feb 11, 2005 this sequence version replaced XP_235544.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090007.1, CK653260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132268
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..387
                     /product="proline-rich protein 5"
                     /note="protor-1; protein observed with Rictor-1; proline
                     rich 5 (renal)"
                     /calculated_mol_wt=42409
     Region          10..96
                     /region_name="Interaction with RICTOR.
                     /evidence=ECO:0000250|UniProtKB:P85299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Region          11..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Region          40..159
                     /region_name="HbrB"
                     /note="HbrB-like; pfam08539"
                     /db_xref="CDD:430059"
     Region          189..219
                     /region_name="Interaction with RICTOR.
                     /evidence=ECO:0000250|UniProtKB:P85299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Region          <224..326
                     /region_name="PHA03326"
                     /note="nuclear egress membrane protein; Provisional"
                     /db_xref="CDD:223045"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q812A5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Region          262..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Region          365..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVG6.1)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q812A5; propagated from
                     UniProtKB/Swiss-Prot (Q5FVG6.1)"
     CDS             1..387
                     /gene="Prr5"
                     /gene_synonym="Protor1"
                     /coded_by="NM_001012121.1:179..1342"
                     /db_xref="GeneID:315189"
                     /db_xref="RGD:1307954"
ORIGIN      
        1 mrtlrrlkfm sspslsdlgk repgaagade rgtqqrraca natwnsihng viavfqrkgl
       61 pdqelfilne gvrqllktel gsffteylqn qlltkgmvil rdkirfyegq klldslaetw
      121 dfffsdvlpt lqaifypvqg kepsvrqlal lhfrntitls vkledalars hacvppaiaq
      181 mllvlqgvhe srgvtedylr letliqkvvs pylgtyglys negpcthsci lekrflrrsr
      241 sgdilaknpv vrsksyntpl lnpvaeheae gtasggtsir rhsvsemtsc pepqgfvdtp
      301 dqgpsgtfrs spsphsgpcp srlyppahsp eqgpdhgspp tsspetlvdq ilesvdsdse
      361 gifidfgrgs rssvsdfeaa ggrpsvv
//
LOCUS       NP_036697                465 aa            linear   ROD 28-APR-2025
DEFINITION  hexokinase-4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_036697
VERSION     NP_036697.1
DBSOURCE    REFSEQ: accession NM_012565.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Samario-Roman,J., Velasco,M., Larque,C., Cardenas-Vazquez,R.,
            Ortiz-Huidobro,R.I. and Hiriart,M.
  TITLE     NGF effects promote the maturation of rat pancreatic beta cells by
            regulating GLUT2 levels and distribution, and glucokinase activity
  JOURNAL   PLoS One 19 (6), e0303934 (2024)
   PUBMED   38875221
  REMARK    GeneRIF: NGF effects promote the maturation of rat pancreatic beta
            cells by regulating GLUT2 levels and distribution, and glucokinase
            activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Llanos,P., Ordenes,P., Rhoads,D.B., Santibanez,J.F.,
            Garcia-Robles,M. and Millan,C.
  TITLE     BMAL1 Regulates Glucokinase Expression Through E-Box Elements In
            Vitro
  JOURNAL   Adv Exp Med Biol 1408, 235-249 (2023)
   PUBMED   37093431
  REMARK    GeneRIF: BMAL1 Regulates Glucokinase Expression Through E-Box
            Elements In Vitro.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Nozaki,Y., Petersen,M.C., Zhang,D., Vatner,D.F., Perry,R.J.,
            Abulizi,A., Haedersdal,S., Zhang,X.M., Butrico,G.M., Samuel,V.T.,
            Mason,G.F., Cline,G.W., Petersen,K.F., Rothman,D.L. and
            Shulman,G.I.
  TITLE     Metabolic control analysis of hepatic glycogen synthesis in vivo
  JOURNAL   Proc Natl Acad Sci U S A 117 (14), 8166-8176 (2020)
   PUBMED   32188779
  REMARK    GeneRIF: Study in different rat models demonstrated that
            glucokinase (GCK)-mediated glucose phosphorylation is the
            rate-controlling step in insulin-stimulated hepatic glycogen
            synthesis in vivo under both normal and pathophysiological
            conditions of fatty liver-associated hepatic insulin resistance and
            it is controlled chiefly through GCK translocation.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Hao,C.L., Lin,H.L., Ke,L.Y., Yen,H.W. and Shen,K.P.
  TITLE     Pre-germinated brown rice extract ameliorates high-fat diet-induced
            metabolic syndrome
  JOURNAL   J Food Biochem 43 (3), e12769 (2019)
   PUBMED   31353547
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Chakera,A.J., Hurst,P.S., Spyer,G., Ogunnowo-Bada,E.O., Marsh,W.J.,
            Riches,C.H., Yueh,C.Y., Markkula,S.P., Dalley,J.W., Cox,R.D.,
            Macdonald,I.A., Amiel,S.A., MacLeod,K.M., Heisler,L.K.,
            Hattersley,A.T. and Evans,M.L.
  TITLE     Molecular reductions in glucokinase activity increase
            counter-regulatory responses to hypoglycemia in mice and humans
            with diabetes
  JOURNAL   Mol Metab 17, 17-27 (2018)
   PUBMED   30146176
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Vionnet,N., Stoffel,M., Takeda,J., Yasuda,K., Bell,G.I., Zouali,H.,
            Lesage,S., Velho,G., Iris,F., Passa,P. et al.
  TITLE     Nonsense mutation in the glucokinase gene causes early-onset
            non-insulin-dependent diabetes mellitus
  JOURNAL   Nature 356 (6371), 721-722 (1992)
   PUBMED   1570017
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Hughes,S.D., Quaade,C., Milburn,J.L., Cassidy,L. and Newgard,C.B.
  TITLE     Expression of normal and novel glucokinase mRNAs in anterior
            pituitary and islet cells
  JOURNAL   J Biol Chem 266 (7), 4521-4530 (1991)
   PUBMED   1999433
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Hayzer,D.J. and Iynedjian,P.B.
  TITLE     Alternative splicing of glucokinase mRNA in rat liver
  JOURNAL   Biochem J 270 (1), 261-263 (1990)
   PUBMED   2396986
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Zahner,D. and Malaisse,W.J.
  TITLE     Kinetic behaviour of liver glucokinase in diabetes. I. Alteration
            in streptozotocin-diabetic rats
  JOURNAL   Diabetes Res 14 (3), 101-108 (1990)
   PUBMED   2132180
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Coleman,D.L.
  TITLE     Genetic control of glucokinase activity in mice
  JOURNAL   Biochem Genet 15 (3-4), 297-305 (1977)
   PUBMED   141272
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X53589.1 and X53588.1.
            
            Transcript Variant: This variant (2) lacks an alternate coding exon
            and uses an alternate splice junction at the 3' end of another
            coding exon compared to variant 1. The resulting isoform (2) has
            the same N-and C-termini but differs in an internal segment
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X53588.1, J04218.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132270,
                                           SAMEA5756307 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..465
                     /product="hexokinase-4 isoform 2"
                     /EC_number="2.7.1.1"
                     /note="HK4; HK IV; hexokinase-4; hexokinase-D; hexokinase
                     type IV"
                     /calculated_mol_wt=51788
     Region          16..458
                     /region_name="ASKHA_NBD_HK4_meta"
                     /note="nucleotide-binding domain (NBD) of type IV
                     hexokinase from metazoan hexokinase (HK) domain family;
                     cd24092"
                     /db_xref="CDD:466942"
     CDS             1..465
                     /gene="Gck"
                     /gene_synonym="GLK; GLUKA; RNGK2"
                     /coded_by="NM_012565.2:109..1506"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:24385"
                     /db_xref="RGD:2670"
ORIGIN      
        1 mamdttrcga qlltlveqil aefqlqeedl kkvmsrmqke mdrglrleth eeasvkmlpt
       61 yvrstpegse vgdflsldlg gtnfrvmlvk vgegeagqws vktkhqmysi pedamtgtae
      121 mlfdyiseci sdfldkhqmk hkklplgftf sfpvrhedld kgillnwtkg fkasgaegnn
      181 ivgllrdaik rrgdfemdvv amvndtvatm iscyyedrqc evgmivgtgc nacymeemqn
      241 velvegdegr mcvntewgaf gdsgeldefl leydrmvdes sanpgqqlye kiiggkymge
      301 lvrlvllklv denllfhgea seqlrtrgaf etrfvsqves dsgdrkqihn ilstlglrps
      361 vtdcdivrra cesvstraah mcsaglagvi nrmresrsed vmritvgvdg svyklhpsfk
      421 erfhasvrrl tpnceitfie seegsgrgaa lvsavackka cmlaq
//
LOCUS       NP_076454                432 aa            linear   ROD 28-APR-2025
DEFINITION  glyceraldehyde-3-phosphate dehydrogenase, testis-specific [Rattus
            norvegicus].
ACCESSION   NP_076454
VERSION     NP_076454.1
DBSOURCE    REFSEQ: accession NM_023964.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Liu,J., Sun,C.M., Zhang,C.L., Wang,X. and Li,J.Y.
  TITLE     Location and characterization of GAPDS in male reproduction
  JOURNAL   Urol Int 90 (4), 449-454 (2013)
   PUBMED   23306140
  REMARK    GeneRIF: GAPDS protein was expressed in both Sertoli cells and
            elongated sperms. The expression of GAPDS gradually increased with
            age in the epididymis.
REFERENCE   2  (residues 1 to 432)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Danshina,P.V., Geyer,C.B., Dai,Q., Goulding,E.H., Willis,W.D.,
            Kitto,G.B., McCarrey,J.R., Eddy,E.M. and O'Brien,D.A.
  TITLE     Phosphoglycerate kinase 2 (PGK2) is essential for sperm function
            and male fertility in mice
  JOURNAL   Biol Reprod 82 (1), 136-145 (2010)
   PUBMED   19759366
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Tanii,I., Yagura,T., Inagaki,N., Nakayama,T., Imaizumi,K. and
            Yoshinaga,K.
  TITLE     Preferential localization of rat GAPDS on the ribs of fibrous
            sheath of sperm flagellum and its expression during flagellar
            formation
  JOURNAL   Acta Histochem Cytochem 40 (1), 19-26 (2007)
   PUBMED   17375205
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Welch,J.E., Barbee,R.R., Magyar,P.L., Bunch,D.O. and O'Brien,D.A.
  TITLE     Expression of the spermatogenic cell-specific glyceraldehyde
            3-phosphate dehydrogenase (GAPDS) in rat testis
  JOURNAL   Mol Reprod Dev 73 (8), 1052-1060 (2006)
   PUBMED   16700075
  REMARK    GeneRIF: results describe the expression of the spermatogenic
            cell-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) in
            rat testis.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Eddy,E.M., Toshimori,K. and O'Brien,D.A.
  TITLE     Fibrous sheath of mammalian spermatozoa
  JOURNAL   Microsc Res Tech 61 (1), 103-115 (2003)
   PUBMED   12672126
  REMARK    Review article
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Welch,J.E., Brown,P.L., O'Brien,D.A., Magyar,P.L., Bunch,D.O.,
            Mori,C. and Eddy,E.M.
  TITLE     Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed
            specifically in spermatogenic cells
  JOURNAL   J Androl 21 (2), 328-338 (2000)
   PUBMED   10714828
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Bunch,D.O., Welch,J.E., Magyar,P.L., Eddy,E.M. and O'Brien,D.A.
  TITLE     Glyceraldehyde 3-phosphate dehydrogenase-S protein distribution
            during mouse spermatogenesis
  JOURNAL   Biol Reprod 58 (3), 834-841 (1998)
   PUBMED   9510974
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Ercolani,L., Florence,B., Denaro,M. and Alexander,M.
  TITLE     Isolation and complete sequence of a functional human
            glyceraldehyde-3-phosphate dehydrogenase gene
  JOURNAL   J Biol Chem 263 (30), 15335-15341 (1988)
   PUBMED   3170585
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Heinz,F. and Freimuller,B.
  TITLE     Glyceraldehyde-3-phosphate dehydrogenase from human tissues
  JOURNAL   Methods Enzymol 89 Pt D, 301-305 (1982)
   PUBMED   7144574
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ297631.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ297631.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..432
                     /product="glyceraldehyde-3-phosphate dehydrogenase,
                     testis-specific"
                     /EC_number="1.2.1.12"
                     /function="glycolytic enzyme"
                     /note="spermatogenic glyceraldehyde-3-phosphate
                     dehydrogenase; spermatogenic cell-specific glyceraldehyde
                     3-phosphate dehydrogenase 2; glyceraldehyde-3-phosphate
                     dehydrogenase type 2"
                     /calculated_mol_wt=46577
     Region          1..97
                     /region_name="Testis-specific N-terminal extension.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV6.1)"
     Region          40..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESV6.1)"
     Region          <102..427
                     /region_name="PLN02272"
                     /note="glyceraldehyde-3-phosphate dehydrogenase"
                     /db_xref="CDD:177912"
     Site            275
                     /site_type="other"
                     /note="Activates thiol group during catalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV6.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ESV6.1)"
     CDS             1..432
                     /gene="Gapdhs"
                     /gene_synonym="gapdh-2; Gapds"
                     /coded_by="NM_023964.1:4..1302"
                     /db_xref="GeneID:66020"
                     /db_xref="RGD:620150"
ORIGIN      
        1 msrrdvvltn vtvvqlrrdp cpcpcpcpcp cpcpvirppp pppkveeppp pkeepppppp
       61 pppppqiepe epkeappppp pppppppppp ppppkpakel tvgingfgri grlvlrvcme
      121 kgvrvvavnd pfidpeymvy mfkydsthgr ykgtvehkng rlvvdnlein vfqckepkei
      181 pwssvgnpyv veatgvylsi eaasghissg arrvivtaps pdapmlvmgv nekdynpgsm
      241 tvvsnasctt nclaplakvi herfgivegl mttvhaytat qktvdgpskk dwrggrgahq
      301 niipsstgaa kavgkvipel ngkltgmafr vptpnvsvvd ltcrlaqpas ytaikeavka
      361 aakgpmagil aytedqvvst dfngdshssi fdakagialn dnfvklvswy dneygyshrv
      421 vdllrymfsr ek
//
LOCUS       NP_001101990             770 aa            linear   ROD 28-APR-2025
DEFINITION  protein PAT1 homolog 1 [Rattus norvegicus].
ACCESSION   NP_001101990 XP_001079118 XP_342030
VERSION     NP_001101990.1
DBSOURCE    REFSEQ: accession NM_001108520.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Jonas,S. and Izaurralde,E.
  TITLE     The role of disordered protein regions in the assembly of decapping
            complexes and RNP granules
  JOURNAL   Genes Dev 27 (24), 2628-2641 (2013)
   PUBMED   24352420
  REMARK    Review article
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Totaro,A., Renzi,F., La Fata,G., Mattioli,C., Raabe,M., Urlaub,H.
            and Achsel,T.
  TITLE     The human Pat1b protein: a novel mRNA deadenylation factor
            identified by a new immunoprecipitation technique
  JOURNAL   Nucleic Acids Res 39 (2), 635-647 (2011)
   PUBMED   20852261
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Marnef,A., Maldonado,M., Bugaut,A., Balasubramanian,S., Kress,M.,
            Weil,D. and Standart,N.
  TITLE     Distinct functions of maternal and somatic Pat1 protein paralogs
  JOURNAL   RNA 16 (11), 2094-2107 (2010)
   PUBMED   20826699
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Ozgur,S., Chekulaeva,M. and Stoecklin,G.
  TITLE     Human Pat1b connects deadenylation with mRNA decapping and controls
            the assembly of processing bodies
  JOURNAL   Mol Cell Biol 30 (17), 4308-4323 (2010)
   PUBMED   20584987
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Braun,J.E., Tritschler,F., Haas,G., Igreja,C., Truffault,V.,
            Weichenrieder,O. and Izaurralde,E.
  TITLE     The C-terminal alpha-alpha superhelix of Pat is required for mRNA
            decapping in metazoa
  JOURNAL   EMBO J 29 (14), 2368-2380 (2010)
   PUBMED   20543818
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168974.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001079118.1, XP_342030.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168974.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132271, SAMD00132275
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..770
                     /product="protein PAT1 homolog 1"
                     /note="PAT1-like protein 1; protein PAT1 homolog b;
                     protein associated with topoisomerase II homolog 1"
                     /calculated_mol_wt=86738
     Region          1..397
                     /region_name="Involved in nuclear foci localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          1..84
                     /region_name="Region A, interaction with DDX6/RCK.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          85..388
                     /region_name="Region N, interaction with decapping
                     machinery. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          86..95
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            217
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          223..397
                     /region_name="Involved in RNA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            223
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          <231..>613
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Site            263
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86TB9; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            284
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          320..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          369..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Site            385
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          389..448
                     /region_name="Region H. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          398..770
                     /region_name="Involved in nuclear speckle localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     Region          449..770
                     /region_name="Region C. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DF93.1)"
     CDS             1..770
                     /gene="Patl1"
                     /gene_synonym="Pat1b; RGD1305514"
                     /coded_by="NM_001108520.2:106..2418"
                     /db_xref="GeneID:361736"
                     /db_xref="RGD:1305514"
ORIGIN      
        1 mfryesledc pldededafq glgeedeeid qfnddtfgsg avdddwqeah erlaeleekl
       61 pvaadeqtgn gerdemdllg dheenlaerl skmvienele dpavmravqt rpvlqpqpgs
      121 lnssiwdgse vlrrirgpll aqemptvsvl eyalpqrppq gpeddrdlse ralprrstsp
      181 iigsppvrav pigtppkqma vpsfnqqilc pkpvhvrppm pprypapyge rmspnqlcsv
      241 pnssllghpf ppsvppvlsp lqraqllgga qlqpgrmsps qfarvpgfvg splaamnpkl
      301 lqgrvgqmlp papgfraffs apppatpppq qhppgpgphl qnlrpqapmf rpdtthlhpq
      361 hrrllhqrql qsrnqhrnln gtgdrgghrv shqdhlrkdp yanlmlqrek dwvskiqmmq
      421 lqstdpyldd fyyqnyfekl ekssaaeemq gdgpkkertk litpqvarle haykpvqfeg
      481 slgkltvssv nnprkmidav vtsrseddet kekqvrdkrr ktlviiekty sllldvedye
      541 rryllsleee rpaltderkh kiwsmydnlr gklpgqerps ddhfvqimci rkgkrmvari
      601 lpflsteqaa dilmatarnl pflikkdaqd evlpcllspf slllyhlpsv tvtsllqqlm
      661 nlpqsatapa psnshltavl qnkfglslll illsrgedlh ssdptvestq nnqwtevmfm
      721 atqellripq aalakpisip tnlvslfsry vdrqklnlle tklqlvqgmr
//
LOCUS       NP_942072                162 aa            linear   ROD 28-APR-2025
DEFINITION  transmembrane protein 138 [Rattus norvegicus].
ACCESSION   NP_942072 XP_342022
VERSION     NP_942072.2
DBSOURCE    REFSEQ: accession NM_198777.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Lee,J.H., Silhavy,J.L., Lee,J.E., Al-Gazali,L., Thomas,S.,
            Davis,E.E., Bielas,S.L., Hill,K.J., Iannicelli,M., Brancati,F.,
            Gabriel,S.B., Russ,C., Logan,C.V., Sharif,S.M., Bennett,C.P.,
            Abe,M., Hildebrandt,F., Diplas,B.H., Attie-Bitach,T., Katsanis,N.,
            Rajab,A., Koul,R., Sztriha,L., Waters,E.R., Ferro-Novick,S.,
            Woods,C.G., Johnson,C.A., Valente,E.M., Zaki,M.S. and Gleeson,J.G.
  TITLE     Evolutionarily assembled cis-regulatory module at a human
            ciliopathy locus
  JOURNAL   Science 335 (6071), 966-969 (2012)
   PUBMED   22282472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC061578.1 and BF282432.1.
            
            On Jan 13, 2007 this sequence version replaced NP_942072.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161808.1, FQ220672.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..162
                     /product="transmembrane protein 138"
                     /calculated_mol_wt=19135
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B1WBM3.1)"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBM3.1)"
     Region          38..156
                     /region_name="TMEM138"
                     /note="Transmembrane protein 138; pfam14935"
                     /db_xref="CDD:434328"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBM3.1)"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBM3.1)"
     Site            115..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1WBM3.1)"
     CDS             1..162
                     /gene="Tmem138"
                     /coded_by="NM_198777.2:161..649"
                     /db_xref="GeneID:361728"
                     /db_xref="RGD:735168"
ORIGIN      
        1 mlqtsnyslv lslqflllcy dlfvnsfsel lrmapviqlv lfiiqdiail fniiiiflmf
       61 fntfvfqagl vnllfhkfkg tiiltsvyla lsislhvwvm nvrwkdsssf rwtnglqtlf
      121 vfqrlaavly cyfykrtavr lgdprfyqds lwlrkefmqv rr
//
LOCUS       NP_001020839             362 aa            linear   ROD 28-APR-2025
DEFINITION  histidine protein methyltransferase 1 homolog [Rattus norvegicus].
ACCESSION   NP_001020839 XP_222828
VERSION     NP_001020839.1
DBSOURCE    REFSEQ: accession NM_001025668.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Cloutier,P., Lavallee-Adam,M., Faubert,D., Blanchette,M. and
            Coulombe,B.
  TITLE     A newly uncovered group of distantly related lysine
            methyltransferases preferentially interact with molecular
            chaperones to regulate their activity
  JOURNAL   PLoS Genet 9 (1), e1003210 (2013)
   PUBMED   23349634
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098702.1.
            
            On Jul 22, 2005 this sequence version replaced XP_222828.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098702.1, FQ148754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..362
                     /product="histidine protein methyltransferase 1 homolog"
                     /EC_number="2.1.1.85"
                     /note="methyltransferase-like protein 18;
                     methyltransferase like 18; methyltransferase 18, RPL3
                     N3-histidine"
                     /calculated_mol_wt=39878
     Region          28..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM84.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95568; propagated from
                     UniProtKB/Swiss-Prot (Q4KM84.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95568; propagated from
                     UniProtKB/Swiss-Prot (Q4KM84.1)"
     Site            144
                     /site_type="methylation"
                     /note="Tele-methylhistidine.
                     /evidence=ECO:0000250|UniProtKB:O95568; propagated from
                     UniProtKB/Swiss-Prot (Q4KM84.1)"
     Region          149..>201
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          <176..>312
                     /region_name="Nnt1"
                     /note="Protein N-terminal and lysine N-methylase,
                     NNT1/EFM7 family [Posttranslational modification, protein
                     turnover, chaperones]; COG3897"
                     /db_xref="CDD:443104"
     Region          237..243
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O95568"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM84.1)"
     CDS             1..362
                     /gene="Mettl18"
                     /gene_synonym="RGD1306783"
                     /coded_by="NM_001025668.1:369..1457"
                     /db_xref="GeneID:304928"
                     /db_xref="RGD:1306783"
ORIGIN      
        1 mafqfnfsie edlenkltsl ddgtcvlksq kgkedknqst elpglpqdrl wkcsslgsaa
       61 ssedtdspps tadrsgvpea cekqpslkpa kehvipkdcd qvlenkvlem lpgsqhvsta
      121 vvktislkek fpgenivsqs fsshsdlipg vyegglkiwe ctfdlmtyft kakvkfagqk
      181 vldlgcgsgl lgitaskgga revhfqdyng lvidevtlpn vvanvplqgd snginepagk
      241 rqrksevaqe tckcrlfsge waefcklvls eklfvkydli ltsetiynpd yystlhetll
      301 rllsrngrvl laskahyfgv gggvhlfqkf veekgvfetr tlevideglk rflmemtfkc
      361 ps
//
LOCUS       NP_001008379             210 aa            linear   ROD 28-APR-2025
DEFINITION  tetraspanin-31 [Rattus norvegicus].
ACCESSION   NP_001008379 XP_343218
VERSION     NP_001008379.1
DBSOURCE    REFSEQ: accession NM_001008378.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC086452.1.
            
            On Dec 16, 2004 this sequence version replaced XP_343218.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086452.1, FQ215742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..210
                     /product="tetraspanin-31"
                     /note="tspan-31; sarcoma-amplified sequence homolog;
                     sarcoma amplified sequence"
                     /calculated_mol_wt=22529
     Region          9..196
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U1V9.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U1V9.1)"
     CDS             1..210
                     /gene="Tspan31"
                     /gene_synonym="Sas"
                     /coded_by="NM_001008378.1:94..726"
                     /db_xref="GeneID:362890"
                     /db_xref="RGD:1309876"
ORIGIN      
        1 macggfacsk nalcalnvvy mlvgllligv aawgkglgvv ssihiiggvi avgvflllia
       61 vaglvgavnh hqvllffymi ilglvfifqf giscsclain rntqadvina swwvlsnstr
      121 helersfdcc glfnlttvhl hddascsalc ktrsspcqmc getflkhsdk alkilggvgl
      181 ffsfteilgv wlamrfrnqk dpranpsafl
//
LOCUS       NP_001128167              80 aa            linear   ROD 28-APR-2025
DEFINITION  protein FAM229B [Rattus norvegicus].
ACCESSION   NP_001128167
VERSION     NP_001128167.1
DBSOURCE    REFSEQ: accession NM_001134695.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC158777.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158777.1, CK596292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..80
                     /product="protein FAM229B"
                     /note="UPF0731 protein C6orf225 homolog"
                     /calculated_mol_wt=8666
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BND4.1)"
     Region          3..80
                     /region_name="UPF0731"
                     /note="UPF0731 family; pfam14982"
                     /db_xref="CDD:291643"
     CDS             1..80
                     /gene="Fam229b"
                     /coded_by="NM_001134695.1:332..574"
                     /db_xref="GeneID:100188933"
                     /db_xref="RGD:2300149"
ORIGIN      
        1 mpfrfgtqpr rfpveggdss ielesglsss ascngketsp nrqlrrcpgs hcltitdvpi
       61 tvyatmrkpp aqsskemrpk
//
LOCUS       NP_113984                930 aa            linear   ROD 28-APR-2025
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 5 [Rattus
            norvegicus].
ACCESSION   NP_113984
VERSION     NP_113984.1
DBSOURCE    REFSEQ: accession NM_031796.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Simmons,A.D., Musy,M.M., Lopes,C.S., Hwang,L.Y., Yang,Y.P. and
            Lovett,M.
  TITLE     A direct interaction between EXT proteins and glycosyltransferases
            is defective in hereditary multiple exostoses
  JOURNAL   Hum Mol Genet 8 (12), 2155-2164 (1999)
   PUBMED   10545594
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Ten Hagen,K.G., Hagen,F.K., Balys,M.M., Beres,T.M., Van
            Wuyckhuyse,B. and Tabak,L.A.
  TITLE     Cloning and expression of a novel, tissue specifically expressed
            member of the UDP-GalNAc:polypeptide
            N-acetylgalactosaminyltransferase family
  JOURNAL   J Biol Chem 273 (42), 27749-27754 (1998)
   PUBMED   9765313
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF049344.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF049344.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..930
                     /product="polypeptide N-acetylgalactosaminyltransferase 5"
                     /EC_number="2.4.1.41"
                     /note="galNAc-T5; pp-GaNTase 5; polypeptide GalNAc
                     transferase 5; protein-UDP acetylgalactosaminyltransferase
                     5; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 5;
                     UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
                     T5; UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 5 (GalNAc-T5)"
                     /calculated_mol_wt=104989
     Site            13..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Region          163..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z7M9; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          344..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          485..594
                     /region_name="Catalytic subdomain A"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Region          489..790
                     /region_name="pp-GalNAc-T"
                     /note="pp-GalNAc-T initiates the formation of mucin-type
                     O-linked glycans; cd02510"
                     /db_xref="CDD:133004"
     Site            order(493..495,497,526,555,558,562,578..580,662..663,
                     685..686,688,713,716,721)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:133004"
     Site            568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            order(578,580,713)
                     /site_type="active"
                     /note="Mn binding site [active]"
                     /db_xref="CDD:133004"
     Region          654..716
                     /region_name="Catalytic subdomain B"
                     /note="propagated from UniProtKB/Swiss-Prot (O88422.1)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Region          796..928
                     /region_name="beta-trefoil_Ricin-like"
                     /note="ricin B-type lectin domain, beta-trefoil fold;
                     cl49609"
                     /db_xref="CDD:483949"
     Site            order(814..816,821,823,831..832)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            817
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            835
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     Site            order(850..851,859,861,869..870)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            order(900..902,909,911,919..920)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:467293"
     Site            902
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88422.1)"
     CDS             1..930
                     /gene="Galnt5"
                     /coded_by="NM_031796.1:113..2905"
                     /db_xref="GeneID:83627"
                     /db_xref="RGD:620361"
ORIGIN      
        1 mnkirkffrg sgrvlafifv asviwllfdm aalrlsfsei ntgilkedim rreqtgfrve
       61 adqmtilsps srgmrpprng aggkesfrka enrvlkveen vdqvqrkgkm qfllgrgkav
      121 slwhrthvqt lpvtlpmqkt qgrdskpevs slhmmskqtt vlgsekdsft vsrgvplnkt
      181 aehtetldkk qeapenynls sdtskqasqr alnvtisvrt drskqqsqtv tkssiqfasl
      241 pilkpeevtv tkkteaqgkd lkyeahkarp llkftadvgh lkkqstnetg lgvlpeadga
      301 kvapgkklnf sesqiviitk eegqktdtke vpnskiqtvf pkllgesqgk hiprsqsqtl
      361 ssplapkrav sqskptlaee lhtarsnlta kattvghqqs hanisenpgk hhvlridvtl
      421 sprdlnapgq fgrpvvvppg kkkeaeqrwk egnfnvylsd lipvdraied trpagcaeql
      481 vhndlpttsi imcfvdevws allrsvhsvl nrspphlike illvddfstk dylkanldky
      541 msqfpkvril rlkerhglir arlagaqnat gdvltfldsh vecnvgwlep llervylnrk
      601 kvacpvievi ndkdmsymtv dnfqrgvftw pmnfgwrtip pdviakngik etdiircpvm
      661 agglfsidks yfyelgtydp gldvwggenm elsfkvwmcg geieiipcsr vghifrndnp
      721 ysfpkdrmkt vernlvrvae vwldeykelf yghgdhlidq gldvgnltqq relrkklkcq
      781 sfkwyldnvf pdlkapvvra sgvfinlalg kcvsiknitv vledcdgsse lqqfnytwvr
      841 likhgewcva pipdkgsltl ypcdnrnnrl kwlhrsasaf hpelvdhivf esyqqllcme
      901 gnfsqktlkl aacnptepqq kwkfekyydv
//
LOCUS       NP_001128218             590 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat transmembrane neuronal protein 4 precursor
            [Rattus norvegicus].
ACCESSION   NP_001128218 XP_001065407 XP_575570
VERSION     NP_001128218.1
DBSOURCE    REFSEQ: accession NM_001134746.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Um,J.W., Pramanik,G., Ko,J.S., Song,M.Y., Lee,D., Kim,H.,
            Park,K.S., Sudhof,T.C., Tabuchi,K. and Ko,J.
  TITLE     Calsyntenins function as synaptogenic adhesion molecules in concert
            with neurexins
  JOURNAL   Cell Rep 6 (6), 1096-1109 (2014)
   PUBMED   24613359
  REMARK    Erratum:[Cell Rep. 2024 Aug 27;43(8):114646. doi:
            10.1016/j.celrep.2024.114646. PMID: 39110596]
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Siddiqui,T.J., Tari,P.K., Connor,S.A., Zhang,P., Dobie,F.A.,
            She,K., Kawabe,H., Wang,Y.T., Brose,N. and Craig,A.M.
  TITLE     An LRRTM4-HSPG complex mediates excitatory synapse development on
            dentate gyrus granule cells
  JOURNAL   Neuron 79 (4), 680-695 (2013)
   PUBMED   23911104
REFERENCE   3  (residues 1 to 590)
  AUTHORS   de Wit,J., O'Sullivan,M.L., Savas,J.N., Condomitti,G.,
            Caccese,M.C., Vennekens,K.M., Yates,J.R. 3rd and Ghosh,A.
  TITLE     Unbiased discovery of glypican as a receptor for LRRTM4 in
            regulating excitatory synapse development
  JOURNAL   Neuron 79 (4), 696-711 (2013)
   PUBMED   23911103
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Schwenk,J., Harmel,N., Brechet,A., Zolles,G., Berkefeld,H.,
            Muller,C.S., Bildl,W., Baehrens,D., Huber,B., Kulik,A., Klocker,N.,
            Schulte,U. and Fakler,B.
  TITLE     High-resolution proteomics unravel architecture and molecular
            diversity of native AMPA receptor complexes
  JOURNAL   Neuron 74 (4), 621-633 (2012)
   PUBMED   22632720
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Linhoff,M.W., Lauren,J., Cassidy,R.M., Dobie,F.A., Takahashi,H.,
            Nygaard,H.B., Airaksinen,M.S., Strittmatter,S.M. and Craig,A.M.
  TITLE     An unbiased expression screen for synaptogenic proteins identifies
            the LRRTM protein family as synaptic organizers
  JOURNAL   Neuron 61 (5), 734-749 (2009)
   PUBMED   19285470
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC168219.1.
            
            On or before Sep 5, 2008 this sequence version replaced
            XP_001065407.1, XP_575570.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC168219.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..590
                     /product="leucine-rich repeat transmembrane neuronal
                     protein 4 precursor"
                     /note="leucine-rich repeat transmembrane neuronal protein
                     4"
                     /calculated_mol_wt=63911
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3277
     mat_peptide     31..590
                     /product="Leucine-rich repeat transmembrane neuronal
                     protein 4. /id=PRO_0000420526"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
                     /calculated_mol_wt=63911
     Region          43..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          60..83
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          64..86
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          66..>311
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..107
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          87..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          108..131
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          111..134
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          132..155
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          135..158
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          157..179
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          159..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          180..203
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          183..206
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..227
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          207..230
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          228..251
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          231..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          252..275
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          255..278
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          276..299
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (B4F7C5.1)"
     Region          303..315
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            425..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B4F7C5.1)"
     CDS             1..590
                     /gene="Lrrtm4"
                     /gene_synonym="RGD1560707"
                     /coded_by="NM_001134746.1:7..1779"
                     /db_xref="GeneID:500219"
                     /db_xref="RGD:1560707"
ORIGIN      
        1 mgfrlitqlk gmsvllvlfp tlllvmltga qracpkncrc dgkivycesh afadipenis
       61 ggsqglslrf nsiqklksnq faglnqliwl yldhnyissv dedafqgirr lkelilssnk
      121 itylhnktfh pvpnlrnldl synklqtlqs eqfkglrkli ilhlrsnslk tvpirvfqdc
      181 rnldfldlgy nrlrslsrna fagllklkel hlehnqfski nfahfprlfn lrsiylqwnr
      241 irsvsqgltw twsslhtldl sgndiqaiep gtfkclpnlq klnldsnklt nvsqetvnaw
      301 islisitlsg nmwecsrsic plfywlknfk gnkestmica gpkhiqgekv sdavetynic
      361 sdvqvvnter shlapqtpqk ppffpkptif ksdaipatle avspspgfqi pgtdheyehv
      421 sfhkiiagsv alflsvamil lviyvswkry pasmkqlqqh slmkrrrkka reserqmnsp
      481 lqeyyvdykp tnsetmdisv ngsgpctyti sgsrecemph hvkplpyysy dqpvigycqa
      541 hqplhinkay eavsieqdds pslelgrdhs fiatiarsaa paiyleritn
//
LOCUS       NP_001014215             300 aa            linear   ROD 28-APR-2025
DEFINITION  arginine/serine-rich protein 1 [Rattus norvegicus].
ACCESSION   NP_001014215 XP_342945
VERSION     NP_001014215.2
DBSOURCE    REFSEQ: accession NM_001014193.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB811984.1, CO405856.1, BF282923.1 and BP475626.1.
            
            On Jun 22, 2007 this sequence version replaced NP_001014215.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ214327.1, FQ230600.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..300
                     /product="arginine/serine-rich protein 1"
                     /note="UPF0471 protein C1orf63 homolog"
                     /calculated_mol_wt=34385
     Region          1..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Region          6..300
                     /region_name="RSRP"
                     /note="Arginine/Serine-Rich protein 1; pfam17069"
                     /db_xref="CDD:293674"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUV0; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BUV0; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Site            147
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3UC65; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Region          222..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2S0.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2S0.2)"
     CDS             1..300
                     /gene="Rsrp1"
                     /gene_synonym="RGD1359529"
                     /coded_by="NM_001014193.2:211..1113"
                     /db_xref="GeneID:362626"
                     /db_xref="RGD:1359529"
ORIGIN      
        1 mssaavskyv ndmwpgspqe kaspstsgsg rssrlssrsr srsssrssrp hsrsssrsss
       61 rshsrprrsr rsrsrsrsrr rhqrkyrrys rsysrsrsrs rghryyrdsr yeqprryyqs
      121 pspyrsrsrs rsrgrshhrr syyaitrgrr yygfgrtvyp edrprwrers rtrsrsrsrt
      181 pfrlsekdrm elleiakana akalgtanfd lpaslrakea sqgavscsgp ktehsekqte
      241 vgtknaseks aaaqrniafs snnsvakple kttkaaveet ssgspkidkk kspyglwipv
//
LOCUS       NP_001093944             780 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-F [Rattus norvegicus].
ACCESSION   NP_001093944 XP_001054372 XP_340764
VERSION     NP_001093944.1
DBSOURCE    REFSEQ: accession NM_001100474.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   D'Angiolella,V., Donato,V., Vijayakumar,S., Saraf,A., Florens,L.,
            Washburn,M.P., Dynlacht,B. and Pagano,M.
  TITLE     SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity
            through CP110 degradation
  JOURNAL   Nature 466 (7302), 138-142 (2010)
   PUBMED   20596027
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Tetzlaff,M.T., Bai,C., Finegold,M., Wilson,J., Harper,J.W.,
            Mahon,K.A. and Elledge,S.J.
  TITLE     Cyclin F disruption compromises placental development and affects
            normal cell cycle execution
  JOURNAL   Mol Cell Biol 24 (6), 2487-2498 (2004)
   PUBMED   14993286
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            On or before Oct 14, 2007 this sequence version replaced
            XP_001054372.1, XP_340764.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF410816.1, SRR26643292.39421.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..780
                     /product="cyclin-F"
                     /calculated_mol_wt=86659
     Region          20..28
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          31..82
                     /region_name="F-box_FBXO1"
                     /note="F-box domain found in F-box only protein 1 (FBXO1)
                     and similar proteins; cd22082"
                     /db_xref="CDD:438854"
     Site            order(35,39,42..43,46..47,51,53..54,58..60,62)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438854"
     Region          <88..138
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          307..401
                     /region_name="CYCLIN_CCNF_rpt1"
                     /note="first cyclin box found in G2/mitotic-specific
                     cyclin-F (CCNF) and similar proteins; cd20521"
                     /db_xref="CDD:410225"
     Region          310..313
                     /region_name="D box 1.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          343..346
                     /region_name="D box 2.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          349..352
                     /region_name="D box 3.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          429..540
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          544..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          568..574
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          582..761
                     /region_name="PEST"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          651..733
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          745..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     Region          762..765
                     /region_name="D box 4.
                     /evidence=ECO:0000250|UniProtKB:P41002"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K4F8.2)"
     CDS             1..780
                     /gene="Ccnf"
                     /coded_by="NM_001100474.1:32..2374"
                     /db_xref="GeneID:117524"
                     /db_xref="RGD:67401"
ORIGIN      
        1 mgsggvihcr cakcfcyptk rrikrrprnl tilslpedvl fhilkwlsvg dilavravhs
       61 hlkylvdnha svwasasfqe lwpspqnlkl feraaekgnf eaavklgiay lyneglsvsd
      121 eacaevnglk asrffsmaer lntgsdpfiw lfirppwsvs gscckavvhd slraecqlqr
      181 shkasilhcl grvlnlfede ekrkqahnlf eesahqgcla ssyllwesdr kvdmsdpgrc
      241 lhsfrklrdy aakgcweaql alakacaggs qlglegkacs esvcqlfqas qavnkqqifs
      301 vqkglsdtmr yilidwlvev atmkdftslc lhltvecvdr ylrrrlvpry klqllgiacm
      361 victrfiske iltireavwl tdntykyedl vrvmgeiisa legkiriptv vdykevlltl
      421 vpvaprtqhl csflceltll htslsvyapa rlasaallla rlmhghtqpw ttqlwdltgf
      481 sysdltpcvl slhkkcfhdd apkdyrqvsl tavkqrfedk cyeeisqeev lsyaelcsal
      541 gvkqespepp sfpssgeiht flsspsgrrs krkrenslqe drgsfvttpt aelsnqeetl
      601 lgslldwsld ccsgyegdqe segekegdvt apsglldvtv vylnpeehcc qessdeevwp
      661 edkshptpgt qappasapwp lpcnrgdpgk dvttsgyssv sssspissld ggmvgsprst
      721 svlsvgshss tkpcyhqakk sclqcrppnp pesgahqqpv krqnlsvhsd edtnlgflkl
//
LOCUS       NP_112516                147 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D3 [Rattus norvegicus].
ACCESSION   NP_112516
VERSION     NP_112516.1
DBSOURCE    REFSEQ: accession NM_031237.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Wang,X., Yang,P., Jiang,Y., Xu,Y., Wang,N., Rao,P., Yang,L., Sun,L.
            and Lu,D.
  TITLE     UBE2D3 contributes to myocardial ischemia-reperfusion injury by
            regulating autophagy in dependence of p62/SQSTM1
  JOURNAL   Cell Signal 87, 110118 (2021)
   PUBMED   34391873
  REMARK    GeneRIF: UBE2D3 contributes to myocardial ischemia-reperfusion
            injury by regulating autophagy in dependence of p62/SQSTM1.
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Hasson,S.A., Kane,L.A., Yamano,K., Huang,C.H., Sliter,D.A.,
            Buehler,E., Wang,C., Heman-Ackah,S.M., Hessa,T., Guha,R.,
            Martin,S.E. and Youle,R.J.
  TITLE     High-content genome-wide RNAi screens identify regulators of parkin
            upstream of mitophagy
  JOURNAL   Nature 504 (7479), 291-295 (2013)
   PUBMED   24270810
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Tokumoto,M., Lee,J.Y., Fujiwara,Y., Uchiyama,M. and Satoh,M.
  TITLE     Inorganic arsenic induces apoptosis through downregulation of Ube2d
            genes and p53 accumulation in rat proximal tubular cells
  JOURNAL   J Toxicol Sci 38 (6), 815-820 (2013)
   PUBMED   24212999
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Zhang,L., Fairall,L., Goult,B.T., Calkin,A.C., Hong,C.,
            Millard,C.J., Tontonoz,P. and Schwabe,J.W.
  TITLE     The IDOL-UBE2D complex mediates sterol-dependent degradation of the
            LDL receptor
  JOURNAL   Genes Dev 25 (12), 1262-1274 (2011)
   PUBMED   21685362
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Wenzel,D.M., Lissounov,A., Brzovic,P.S. and Klevit,R.E.
  TITLE     UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
            hybrids
  JOURNAL   Nature 474 (7349), 105-108 (2011)
   PUBMED   21532592
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Qiu,X.B., Markant,S.L., Yuan,J. and Goldberg,A.L.
  TITLE     Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel
            pathway for triggering apoptosis
  JOURNAL   EMBO J 23 (4), 800-810 (2004)
   PUBMED   14765125
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Lopez Salon,M., Morelli,L., Castano,E.M., Soto,E.F. and
            Pasquini,J.M.
  TITLE     Defective ubiquitination of cerebral proteins in Alzheimer's
            disease
  JOURNAL   J Neurosci Res 62 (2), 302-310 (2000)
   PUBMED   11020223
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Wing,S.S. and Jain,P.
  TITLE     Molecular cloning, expression and characterization of a ubiquitin
            conjugation enzyme (E2(17)kB) highly expressed in rat testis
  JOURNAL   Biochem J 305 (Pt 1) (Pt 1), 125-132 (1995)
   PUBMED   7826319
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB006852.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB006852.1, CF110851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q43"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D3"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="PAPase; E2(17)KB 3; phosphoarginine phosphatase;
                     ubiquitin-protein ligase D3; ubiquitin carrier protein D3;
                     ubiquitin-conjugating enzyme E2-17 kDa 3;
                     ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog,
                     yeast); ubiquitin-conjugating enzyme E2(17)KB 3;
                     ubiquitin-conjugating enzyme E2D 3 (homologous to yeast
                     UBC4/5); E2 ubiquitin-conjugating enzyme D3;
                     (E3-independent) E2 ubiquitin-conjugating enzyme D3"
                     /calculated_mol_wt=16556
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="Ube2d3"
                     /coded_by="NM_031237.1:274..717"
                     /db_xref="GeneID:81920"
                     /db_xref="RGD:619912"
ORIGIN      
        1 malkrinkel sdlardppaq csagpvgddm fhwqatimgp ndspyqggvf fltihfptdy
       61 pfkppkvaft triyhpnins ngsicldilr sqwspaltis kvllsicsll cdpnpddplv
      121 peiariyktd rdkynrisre wtqkyam
//
LOCUS       NP_001029034             458 aa            linear   ROD 28-APR-2025
DEFINITION  cell adhesion molecule CEACAM1 isoform 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_001029034
VERSION     NP_001029034.1
DBSOURCE    REFSEQ: accession NM_001033862.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Huff,L.P., Kikuchi,D.S., Faidley,E., Forrester,S.J., Tsai,M.Z.,
            Lassegue,B. and Griendling,K.K.
  TITLE     Polymerase-delta-interacting protein 2 activates the RhoGEF
            epithelial cell transforming sequence 2 in vascular smooth muscle
            cells
  JOURNAL   Am J Physiol Cell Physiol 316 (5), C621-C631 (2019)
   PUBMED   30726115
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Bonsor,D.A., Gunther,S., Beadenkopf,R., Beckett,D. and
            Sundberg,E.J.
  TITLE     Diverse oligomeric states of CEACAM IgV domains
  JOURNAL   Proc Natl Acad Sci U S A 112 (44), 13561-13566 (2015)
   PUBMED   26483485
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Huang,Y.H., Zhu,C., Kondo,Y., Anderson,A.C., Gandhi,A., Russell,A.,
            Dougan,S.K., Petersen,B.S., Melum,E., Pertel,T., Clayton,K.L.,
            Raab,M., Chen,Q., Beauchemin,N., Yazaki,P.J., Pyzik,M.,
            Ostrowski,M.A., Glickman,J.N., Rudd,C.E., Ploegh,H.L., Franke,A.,
            Petsko,G.A., Kuchroo,V.K. and Blumberg,R.S.
  TITLE     CEACAM1 regulates TIM-3-mediated tolerance and exhaustion
  JOURNAL   Nature 517 (7534), 386-390 (2015)
   PUBMED   25363763
  REMARK    Erratum:[Nature. 2016 Aug 18;536(7616):359. doi:
            10.1038/nature17421. PMID: 26982724]
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Heckt,T., Bickert,T., Jeschke,A., Seitz,S., Schulze,J., Ito,W.D.,
            Zimmermann,W., Amling,M., Schinke,T., Horst,A.K. and Keller,J.
  TITLE     Increased osteoclastogenesis in mice lacking the carcinoembryonic
            antigen-related cell adhesion molecule 1
  JOURNAL   PLoS One 9 (12), e114360 (2014)
   PUBMED   25490771
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Singer,B.B., Opp,L., Heinrich,A., Schreiber,F.,
            Binding-Liermann,R., Berrocal-Almanza,L.C., Heyl,K.A., Muller,M.M.,
            Weimann,A., Zweigner,J. and Slevogt,H.
  TITLE     Soluble CEACAM8 interacts with CEACAM1 inhibiting TLR2-triggered
            immune responses
  JOURNAL   PLoS One 9 (4), e94106 (2014)
   PUBMED   24743304
  REMARK    GeneRIF: CEACAM8 interacts with CEACAM1 inhibiting TLR2-triggered
            immune responses
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Culic,O., Huang,Q.H., Flanagan,D., Hixson,D. and Lin,S.H.
  TITLE     Molecular cloning and expression of a new rat liver cell-CAM105
            isoform. Differential phosphorylation of isoforms
  JOURNAL   Biochem J 285 (Pt 1) (Pt 1), 47-53 (1992)
   PUBMED   1637321
REFERENCE   7  (residues 1 to 458)
  AUTHORS   McCuaig,K., Turbide,C. and Beauchemin,N.
  TITLE     mmCGM1a: a mouse carcinoembryonic antigen gene family member,
            generated by alternative splicing, functions as an adhesion
            molecule
  JOURNAL   Cell Growth Differ 3 (3), 165-174 (1992)
   PUBMED   1633107
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Dveksler,G.S., Pensiero,M.N., Cardellichio,C.B., Williams,R.K.,
            Jiang,G.S., Holmes,K.V. and Dieffenbach,C.W.
  TITLE     Cloning of the mouse hepatitis virus (MHV) receptor: expression in
            human and hamster cell lines confers susceptibility to MHV
  JOURNAL   J Virol 65 (12), 6881-6891 (1991)
   PUBMED   1719235
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Lin,S.H., Culic,O., Flanagan,D. and Hixson,D.C.
  TITLE     Immunochemical characterization of two isoforms of rat liver
            ecto-ATPase that show an immunological and structural identity with
            a glycoprotein cell-adhesion molecule with Mr 105,000
  JOURNAL   Biochem J 278 (Pt 1) (Pt 1), 155-161 (1991)
   PUBMED   1831973
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Williams,R.K., Jiang,G.S. and Holmes,K.V.
  TITLE     Receptor for mouse hepatitis virus is a member of the
            carcinoembryonic antigen family of glycoproteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (13), 5533-5536 (1991)
   PUBMED   1648219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M92848.1, X91137.1, BC061740.1, J04963.1 and JAXUCZ010000001.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X91137.1, Z12019.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..458
                     /product="cell adhesion molecule CEACAM1 isoform 3
                     precursor"
                     /note="GP110; pp120; C-CAM 105; ecto-ATPase; cell-CAM 105;
                     ATP-dependent taurocolate-carrier protein; bone
                     gamma-carboxyglutamic acid (Gla) protein; osteocalcin;
                     CEA-related cell adhesion molecule 1 (bone
                     gamma-carboxyglutamic acid (Gla) protein) (osteocalcin);
                     carcinoembryonic antigen-related cell adhesion molecule 1
                     (biliary glycoprotein); pp120/ecto-ATPase;
                     carcinoembryonic antigen related cell adhesion molecule 1;
                     cell adhesion molecule CEACAM1"
                     /calculated_mol_wt=46978
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3801
     Site            35
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P13688; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     Region          36..140
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          39..142
                     /region_name="Required for homophilic binding.
                     /evidence=ECO:0000269|PubMed:8831574"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..140
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          146..234
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          146..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          153..158
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          163..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          176..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          183..186
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          190..194
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          197..202
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          212..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          224..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          243..318
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          243..249
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          254..261
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          267..273
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          276..281
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          284..290
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          293..304
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          307..318
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          324..411
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          324..328
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          331..335
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P16573.4)"
     Region          340..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          353..358
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          360..363
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          367..371
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          374..379
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical.
                     /evidence=ECO:0000250|UniProtKB:P31809,
                     ECO:0000255|PROSITE-ProRule:PRU00498; propagated from
                     UniProtKB/Swiss-Prot (P16573.4)"
     Region          389..397
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          401..410
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            426..446
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16573.4)"
     CDS             1..458
                     /gene="Ceacam1"
                     /gene_synonym="Bgp; BGPR; Ccam1; CD66a"
                     /coded_by="NM_001033862.1:58..1434"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:81613"
                     /db_xref="RGD:67396"
ORIGIN      
        1 melasarllr gqipwrglll taslltywsp lttaqvtvda vppnvveeks vlllahnlpq
       61 efqvfywykg ttlnpdseia ryirsdnmsk tgpaysgret iysngslffq nvnktderay
      121 tlsvfdqqfn piqtsvqfrv ypalqkpnvt gnnsnpmege pfvslmcepy tnntsylwsr
      181 ngeslsegdr vtfsegnrtl tllnvrrtdk gyyecearnp atfnrsdpfn ldviygpdap
      241 visppdiylh qgsnlnlsch adsnppaqyf wlineklqts sqelfisnit tnnsgtyacf
      301 vnntvtglsr ttvknitvfe pvtqpsiqit nttvkelgsv tltcfskdtg vsvrwlfnsq
      361 slqltdrmtl sqdnstlrid pikredagdy qceisnpvsf rishpikldv ipdptqgnsg
      421 lsegaiagiv igsvagvali aalayflysr ktggsgsf
//
LOCUS       NP_001005899             240 aa            linear   ROD 28-APR-2025
DEFINITION  C-type lectin domain family 4 member A [Rattus norvegicus].
ACCESSION   NP_001005899 XP_579154
VERSION     NP_001005899.2
DBSOURCE    REFSEQ: accession NM_001005899.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Flornes,L.M., Bryceson,Y.T., Spurkland,A., Lorentzen,J.C.,
            Dissen,E. and Fossum,S.
  TITLE     Identification of lectin-like receptors expressed by antigen
            presenting cells and neutrophils and their mapping to a novel gene
            complex
  JOURNAL   Immunogenetics 56 (7), 506-517 (2004)
   PUBMED   15368084
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY581051.1.
            
            On May 23, 2007 this sequence version replaced NP_001005899.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY581051.1, AY494060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..240
                     /product="C-type lectin domain family 4 member A"
                     /note="dendritic cell inhibitory receptor 1; C-type lectin
                     superfamily member 6; C-type (calcium dependent,
                     carbohydrate recognition domain) lectin, superfamily
                     member 6"
                     /calculated_mol_wt=27300
     Region          5..10
                     /region_name="ITIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67EQ0.1)"
     Region          18..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67EQ0.1)"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q67EQ0.1)"
     Region          107..235
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(168,200,202,206,212..213,221..224)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(175,178,203,206..207)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(178,207)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q67EQ0.1)"
     CDS             1..240
                     /gene="Clec4a"
                     /gene_synonym="Clecsf6; Dcir1"
                     /coded_by="NM_001005899.2:15..737"
                     /db_xref="GeneID:474143"
                     /db_xref="RGD:1359662"
ORIGIN      
        1 maseityaev riknesnssv tysgspaapr ekptrhlskp gsllvpftsl mvlllllait
       61 flvafiiyfq kysqfleekk aikgithkel nciknvllme ekswsccpkn wkpfgshcyw
      121 vtkhtstysk aswneseknc fsmgahllvi hskeeqdfit gilnrdaayf iglwdsghrq
      181 wqwvsqtpyn asatfwhkge pssddekcvi inhlnsgwgw ndipcsgkqq svcqmkkiql
//
LOCUS       NP_001007741             327 aa            linear   ROD 28-APR-2025
DEFINITION  vacuolar protein sorting-associated protein 26A [Rattus
            norvegicus].
ACCESSION   NP_001007741 XP_342141
VERSION     NP_001007741.1
DBSOURCE    REFSEQ: accession NM_001007740.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   McNally,K.E., Faulkner,R., Steinberg,F., Gallon,M., Ghai,R.,
            Pim,D., Langton,P., Pearson,N., Danson,C.M., Nagele,H.,
            Morris,L.L., Singla,A., Overlee,B.L., Heesom,K.J., Sessions,R.,
            Banks,L., Collins,B.M., Berger,I., Billadeau,D.D., Burstein,E. and
            Cullen,P.J.
  TITLE     Retriever is a multiprotein complex for retromer-independent
            endosomal cargo recycling
  JOURNAL   Nat Cell Biol 19 (10), 1214-1225 (2017)
   PUBMED   28892079
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Peng,D., Wang,J., Zhang,R., Jiang,F., Tam,C.H.T., Jiang,G.,
            Wang,T., Chen,M., Yan,J., Wang,S., Yan,D., He,Z., Ma,R.C.W.,
            Bao,Y., Hu,C. and Jia,W.
  TITLE     CDKAL1 rs7756992 is associated with diabetic retinopathy in a
            Chinese population with type 2 diabetes
  JOURNAL   Sci Rep 7 (1), 8812 (2017)
   PUBMED   28821857
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Eze,I.C., Imboden,M., Kumar,A., von Eckardstein,A., Stolz,D.,
            Gerbase,M.W., Kunzli,N., Pons,M., Kronenberg,F., Schindler,C. and
            Probst-Hensch,N.
  TITLE     Air pollution and diabetes association: Modification by type 2
            diabetes genetic risk score
  JOURNAL   Environ Int 94, 263-271 (2016)
   PUBMED   27281273
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Follett,J., Bugarcic,A., Yang,Z., Ariotti,N., Norwood,S.J.,
            Collins,B.M., Parton,R.G. and Teasdale,R.D.
  TITLE     Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal
            Association of Retromer and Induces alpha-Synuclein Aggregation
  JOURNAL   J Biol Chem 291 (35), 18283-18298 (2016)
   PUBMED   27385586
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Lin,T.B., Lai,C.Y., Hsieh,M.C., Wang,H.H., Cheng,J.K., Chau,Y.P.,
            Chen,G.D. and Peng,H.Y.
  TITLE     VPS26A-SNX27 Interaction-Dependent mGluR5 Recycling in Dorsal Horn
            Neurons Mediates Neuropathic Pain in Rats
  JOURNAL   J Neurosci 35 (44), 14943-14955 (2015)
   PUBMED   26538661
  REMARK    GeneRIF: VPS26A-SNX27 interaction plays a role in the development
            of neuropathic pain.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Gorbea,C., Pratt,G., Ustrell,V., Bell,R., Sahasrabudhe,S.,
            Hughes,R.E. and Rechsteiner,M.
  TITLE     A protein interaction network for Ecm29 links the 26 S proteasome
            to molecular motors and endosomal components
  JOURNAL   J Biol Chem 285 (41), 31616-31633 (2010)
   PUBMED   20682791
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Collins,B.M., Skinner,C.F., Watson,P.J., Seaman,M.N. and Owen,D.J.
  TITLE     Vps29 has a phosphoesterase fold that acts as a protein interaction
            scaffold for retromer assembly
  JOURNAL   Nat Struct Mol Biol 12 (7), 594-602 (2005)
   PUBMED   15965486
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Arighi,C.N., Hartnell,L.M., Aguilar,R.C., Haft,C.R. and
            Bonifacino,J.S.
  TITLE     Role of the mammalian retromer in sorting of the cation-independent
            mannose 6-phosphate receptor
  JOURNAL   J Cell Biol 165 (1), 123-133 (2004)
   PUBMED   15078903
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Seaman,M.N.
  TITLE     Cargo-selective endosomal sorting for retrieval to the Golgi
            requires retromer
  JOURNAL   J Cell Biol 165 (1), 111-122 (2004)
   PUBMED   15078902
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079150.1.
            
            On Nov 29, 2004 this sequence version replaced XP_342141.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079150.1, FQ211877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..327
                     /product="vacuolar protein sorting-associated protein 26A"
                     /note="vesicle protein sorting 26A; vacuole protein
                     sorting 26; H beta 58; vacuolar protein sorting 26 homolog
                     A; VPS26 retromer complex comonent A"
                     /calculated_mol_wt=37984
     Region          8..283
                     /region_name="Vps26"
                     /note="Vacuolar protein sorting-associated protein 26;
                     pfam03643"
                     /db_xref="CDD:397622"
     Region          306..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY86.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY86.1)"
     CDS             1..327
                     /gene="Vps26a"
                     /gene_synonym="Vps26"
                     /coded_by="NM_001007740.1:82..1065"
                     /db_xref="GeneID:361846"
                     /db_xref="RGD:1359254"
ORIGIN      
        1 msflggffgp iceidvalsd getrkmaemk tedgkvekhy lfydgesvsg kvnlafkqpg
       61 krlehqgiri efvgqielfn dksnthefvn lvkelalpge ltqsrsydfe fmqvekpyes
      121 yiganvrlry flkvtivrrl tdlvkeydli vhqlatypev nnsikmevgi edclhiefey
      181 nkskyhlkdv ivgkiyfllv rikiqhmelq likkeitgig psttteteti akyeimdgap
      241 vkgesipirl flagydptpt mrdvnkkfsv ryflnlvlvd eedrryfkqq eiilwrkape
      301 klrkqrtnfh qrfespesqa saeqpem
//
LOCUS       NP_001032257             403 aa            linear   ROD 28-APR-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase FKBP8 [Rattus norvegicus].
ACCESSION   NP_001032257 XP_214316
VERSION     NP_001032257.1
DBSOURCE    REFSEQ: accession NM_001037180.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Mali,G.R., Yeyati,P.L., Mizuno,S., Dodd,D.O., Tennant,P.A.,
            Keighren,M.A., Zur Lage,P., Shoemark,A., Garcia-Munoz,A.,
            Shimada,A., Takeda,H., Edlich,F., Takahashi,S., von Kreigsheim,A.,
            Jarman,A.P. and Mill,P.
  TITLE     ZMYND10 functions in a chaperone relay during axonemal dynein
            assembly
  JOURNAL   Elife 7, e34389 (2018)
   PUBMED   29916806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Li,H., Zhang,C., Cui,H., Guo,K., Wang,F., Zhao,T., Liang,W., Lv,Q.
            and Zhang,Y.
  TITLE     FKBP8 interact with classical swine fever virus NS5A protein and
            promote virus RNA replication
  JOURNAL   Virus Genes 52 (1), 99-106 (2016)
   PUBMED   26748656
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Cho,A., Ko,H.W. and Eggenschwiler,J.T.
  TITLE     FKBP8 cell-autonomously controls neural tube patterning through a
            Gli2- and Kif3a-dependent mechanism
  JOURNAL   Dev Biol 321 (1), 27-39 (2008)
   PUBMED   18590716
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Wong,R.L., Wlodarczyk,B.J., Min,K.S., Scott,M.L., Kartiko,S.,
            Yu,W., Merriweather,M.Y., Vogel,P., Zambrowicz,B.P. and
            Finnell,R.H.
  TITLE     Mouse Fkbp8 activity is required to inhibit cell death and
            establish dorso-ventral patterning in the posterior neural tube
  JOURNAL   Hum Mol Genet 17 (4), 587-601 (2008)
   PUBMED   18003640
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Okamoto,T., Nishimura,Y., Ichimura,T., Suzuki,K., Miyamura,T.,
            Suzuki,T., Moriishi,K. and Matsuura,Y.
  TITLE     Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90
  JOURNAL   EMBO J 25 (20), 5015-5025 (2006)
   PUBMED   17024179
  REMARK    Erratum:[EMBO J. 2006 Nov 29;25(23):5634]
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Kang,C.B., Tai,J., Chia,J. and Yoon,H.S.
  TITLE     The flexible loop of Bcl-2 is required for molecular interaction
            with immunosuppressant FK-506 binding protein 38 (FKBP38)
  JOURNAL   FEBS Lett 579 (6), 1469-1476 (2005)
   PUBMED   15733859
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Bulgakov,O.V., Eggenschwiler,J.T., Hong,D.H., Anderson,K.V. and
            Li,T.
  TITLE     FKBP8 is a negative regulator of mouse sonic hedgehog signaling in
            neural tissues
  JOURNAL   Development 131 (9), 2149-2159 (2004)
   PUBMED   15105374
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107454.1.
            
            On Nov 18, 2005 this sequence version replaced XP_214316.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107454.1, SRR8487227.303595.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..403
                     /product="peptidyl-prolyl cis-trans isomerase FKBP8"
                     /EC_number="5.2.1.8"
                     /note="rotamase; PPIase FKBP8; FK506-binding protein 8;
                     FK506 binding protein 8, 38kDa"
                     /calculated_mol_wt=43425
     Region          26..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U9.1)"
     Region          103..192
                     /region_name="FKBP_C"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase;
                     pfam00254"
                     /db_xref="CDD:459735"
     Region          210..>337
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          212..245
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U9.1)"
     Site            order(220..221,223,247,267..268,271..272,274..275,298,
                     301..302,305..306,309)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          245..292
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          263..296
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U9.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14318; propagated from
                     UniProtKB/Swiss-Prot (Q3B7U9.1)"
     Region          297..330
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U9.1)"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7U9.1)"
     CDS             1..403
                     /gene="Fkbp8"
                     /gene_synonym="FKBP-8"
                     /coded_by="NM_001037180.1:78..1289"
                     /db_xref="GeneID:290652"
                     /db_xref="RGD:1308670"
ORIGIN      
        1 maswaepsep aaqllcgapl legfevldgv ddaeeeddls glppledmgq ptveeaeqpg
       61 alareflaat epepapapap eewldilgng llrkktlvpg ptgssrplkg qvvtvhlqms
      121 lengtrvqee pelaftlgdc dviqaldlsv plmhvgetam vtadskycyg pqgsrspyip
      181 phaalclevt lktaedgpdl emlsgqerva lanrkrecgn ahyqradfvl aansydlaik
      241 aitsnakvdm tceeeeellq lkvkclnnla asqlkldhyr aalrscsqvl ehqpdnikal
      301 frkgkvlaqq geyseaipil raalklepsn ktihaelskl vkkraaqrst etalyrkmlg
      361 npsrlpakcp gkgawsipwk wlfgataval ggvalsvvia arn
//
LOCUS       NP_001100254             907 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing G-protein coupled receptor 5
            precursor [Rattus norvegicus].
ACCESSION   NP_001100254 XP_235149
VERSION     NP_001100254.1
DBSOURCE    REFSEQ: accession NM_001106784.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Lee,C., Minich,A., Li,B., Miyake,H., Seo,S. and Pierro,A.
  TITLE     Influence of stress factors on intestinal epithelial injury and
            regeneration
  JOURNAL   Pediatr Surg Int 34 (2), 155-160 (2018)
   PUBMED   29018960
  REMARK    GeneRIF: IL-6 expression increased in all groups compared to
            control. Lgr5 expression was up-regulated in cells exposed to a
            single stressor, but down-regulated when multiple stressors were
            administered.
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Chen,X., Hao,J., Fu,T., Liu,J., Yu,M., He,S., Qian,R. and Zhang,F.
  TITLE     Temporal and Spatial Expression of LGR5 After Acute Spinal Cord
            Injury in Adult Rats
  JOURNAL   Neurochem Res 41 (10), 2645-2654 (2016)
   PUBMED   27339869
  REMARK    GeneRIF: that Leucine-rich repeat-containing G-protein coupled
            receptor 5might be of great significance in CNS pathophysiology
            after spinal cord injury
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Junttila,M.R., Mao,W., Wang,X., Wang,B.E., Pham,T., Flygare,J.,
            Yu,S.F., Yee,S., Goldenberg,D., Fields,C., Eastham-Anderson,J.,
            Singh,M., Vij,R., Hongo,J.A., Firestein,R., Schutten,M.,
            Flagella,K., Polakis,P. and Polson,A.G.
  TITLE     Targeting LGR5+ cells with an antibody-drug conjugate for the
            treatment of colon cancer
  JOURNAL   Sci Transl Med 7 (314), 314ra186 (2015)
   PUBMED   26582901
  REMARK    GeneRIF: Report targeting LGR5+ tumor stem cells with an
            antibody-drug conjugate as effective treatment for colon cancer.
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Li,W., Wu,J., Yang,J., Sun,S., Chai,R., Chen,Z.Y. and Li,H.
  TITLE     Notch inhibition induces mitotically generated hair cells in
            mammalian cochleae via activating the Wnt pathway
  JOURNAL   Proc Natl Acad Sci U S A 112 (1), 166-171 (2015)
   PUBMED   25535395
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Rastetter,R.H., Bernard,P., Palmer,J.S., Chassot,A.A., Chen,H.,
            Western,P.S., Ramsay,R.G., Chaboissier,M.C. and Wilhelm,D.
  TITLE     Marker genes identify three somatic cell types in the fetal mouse
            ovary
  JOURNAL   Dev Biol 394 (2), 242-252 (2014)
   PUBMED   25158167
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Cruciat,C.M. and Niehrs,C.
  TITLE     Secreted and transmembrane wnt inhibitors and activators
  JOURNAL   Cold Spring Harb Perspect Biol 5 (3), a015081 (2013)
   PUBMED   23085770
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Ruffner,H., Sprunger,J., Charlat,O., Leighton-Davies,J.,
            Grosshans,B., Salathe,A., Zietzling,S., Beck,V., Therier,M.,
            Isken,A., Xie,Y., Zhang,Y., Hao,H., Shi,X., Liu,D., Song,Q.,
            Clay,I., Hintzen,G., Tchorz,J., Bouchez,L.C., Michaud,G., Finan,P.,
            Myer,V.E., Bouwmeester,T., Porter,J., Hild,M., Bassilana,F.,
            Parker,C.N. and Cong,F.
  TITLE     R-Spondin potentiates Wnt/beta-catenin signaling through orphan
            receptors LGR4 and LGR5
  JOURNAL   PLoS One 7 (7), e40976 (2012)
   PUBMED   22815884
REFERENCE   8  (residues 1 to 907)
  AUTHORS   Lu,C.C., Appler,J.M., Houseman,E.A. and Goodrich,L.V.
  TITLE     Developmental profiling of spiral ganglion neurons reveals insights
            into auditory circuit assembly
  JOURNAL   J Neurosci 31 (30), 10903-10918 (2011)
   PUBMED   21795542
REFERENCE   9  (residues 1 to 907)
  AUTHORS   Carmon,K.S., Gong,X., Lin,Q., Thomas,A. and Liu,Q.
  TITLE     R-spondins function as ligands of the orphan receptors LGR4 and
            LGR5 to regulate Wnt/beta-catenin signaling
  JOURNAL   Proc Natl Acad Sci U S A 108 (28), 11452-11457 (2011)
   PUBMED   21693646
REFERENCE   10 (residues 1 to 907)
  AUTHORS   de Lau,W., Barker,N., Low,T.Y., Koo,B.K., Li,V.S., Teunissen,H.,
            Kujala,P., Haegebarth,A., Peters,P.J., van de Wetering,M.,
            Stange,D.E., van Es,J.E., Guardavaccaro,D., Schasfoort,R.B.,
            Mohri,Y., Nishimori,K., Mohammed,S., Heck,A.J. and Clevers,H.
  TITLE     Lgr5 homologues associate with Wnt receptors and mediate R-spondin
            signalling
  JOURNAL   Nature 476 (7360), 293-297 (2011)
   PUBMED   21727895
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473960.2.
            
            On Oct 4, 2007 this sequence version replaced XP_235149.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..907
                     /product="leucine-rich repeat-containing G-protein coupled
                     receptor 5 precursor"
                     /note="G protein-coupled receptor 49"
                     /calculated_mol_wt=97662
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2315
     mat_peptide     22..907
                     /product="Leucine-rich repeat-containing G-protein coupled
                     receptor 5. /id=PRO_0000422818"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
                     /calculated_mol_wt=97662
     Region          44..64
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          <48..107
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          65..88
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          68..91
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          89..112
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          92..>456
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          92..115
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          114..136
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          116..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          137..160
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          140..163
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          162..184
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          164..187
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..208
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          188..211
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          209..232
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          212..235
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          233..256
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          236..258
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          257..279
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          259..282
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          281..303
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          283..304
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          304..327
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          307..353
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          328..350
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          351..375
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          354..375
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          376..399
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          377..396
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          397..420
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          400..423
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          422..444
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          445..467
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          558..831
                     /region_name="7tmA_LGR5"
                     /note="leucine-rich repeats-containing G protein-coupled
                     receptor 5, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15363"
                     /db_xref="CDD:320485"
     Region          559..585
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320485"
     Site            562..582
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          564..585
                     /region_name="LRR 18"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          592..617
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320485"
     Site            596..616
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Site            order(613,616..617,637..642,644..645,648,693,695..699,721,
                     724..726,728..730,732..733,779,782..783,785..786,789,
                     798..799,801..803,806,809..810)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320485"
     Region          637..667
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320485"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          679..701
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320485"
     Site            683..703
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          721..750
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320485"
     Site            724..744
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          759..789
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320485"
     Site            776..796
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     Region          799..824
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320485"
     Site            803..823
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AC13.1)"
     CDS             1..907
                     /gene="Lgr5"
                     /gene_synonym="Gpr49"
                     /coded_by="NM_001106784.1:1..2724"
                     /db_xref="GeneID:299802"
                     /db_xref="RGD:1307733"
ORIGIN      
        1 mdtsrvrmll sllallqlva agspprpdtm prgcpsychc eldgrmllrv dcsdlglsel
       61 psnlsvftsy ldlsmnnisq lpasllhrlr fleelrlagn althipkgaf aglhslkvlm
      121 lqnnqlrqvp eealqnlrsl qslrldanhi syvppscfsg lhslrhlwld dnaltdvpvq
      181 afrslsalqa mtlalnkihh iadhafgnls slvvlhlhnn rihslgkkcf dglhsletld
      241 lnynnldefp taiktlsnlk elgfhsnnir siperafvgn pslitihfyd npiqfvgisa
      301 fqhlpelrtl tlngasqite fpdltgtatl esltltgaki sslpqtvcdq lpnlqvldls
      361 ynlledlpsl sgcqklqkid lrhneiyeik ggtfqqlfnl rslnlarnki aiihpnafst
      421 lpslikldls snllssfpvt glhglthlkl tgnralqsli psanfpelki iempyayqcc
      481 afggcenvyk ipnqwnkdds ssvddlrkkd aglfqvqder dledflldfe edlkvlhsvq
      541 cspppgpfkp cehlfgswli rigvwttavl alscnalvaf tvfrtplyis siklligvia
      601 vvdilmgvss ailavvdtft fgsfaqhgaw weggigcqiv gflsifases svflltlaal
      661 ergfsvkcss kfemkaplss lkaiillcvl laltiatvpl lggseynasp lclplpfgep
      721 sttgymvalv llnslcflim tiaytrlycs lekgelenlw dcsmvkhtal llftncilyc
      781 pvaflsfssl lnltfispev ikfillvivp lpaclnplly ivfnphfked mgslgkqtrf
      841 wtrakhpsll sinsddvekr scdstqalvs fthasiaydl psdsgsspay pmteschlss
      901 vafvpcl
//
LOCUS       NP_001094109             768 aa            linear   ROD 28-APR-2025
DEFINITION  POU domain, class 2, transcription factor 1 [Rattus norvegicus].
ACCESSION   NP_001094109 XP_001075635 XP_341149
VERSION     NP_001094109.1
DBSOURCE    REFSEQ: accession NM_001100639.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Gu,Y.H., Wang,J., Lu,W.C., Cheng,Y., Tao,R., Zhang,S.J., Xu,T.,
            Zhai,K.W., Luo,S.X. and Xin,W.J.
  TITLE     POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment
  JOURNAL   Neurochem Res 48 (12), 3652-3664 (2023)
   PUBMED   37592110
  REMARK    GeneRIF: POU2F1/DNMT3a Pathway Participates in Neuropathic Pain by
            Hypermethylation-Mediated LRFN4 Downregulation Following
            Oxaliplatin Treatment.
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Zhang,W.F., Zhu,T.T., Xiong,Y.W., Xiong,A.Z., Ge,X.Y., Hu,C.P. and
            Zhang,Z.
  TITLE     Negative feedback regulation between microRNA let-7g and LOX-1
            mediated hypoxia-induced PASMCs proliferation
  JOURNAL   Biochem Biophys Res Commun 488 (4), 655-663 (2017)
   PUBMED   28108289
  REMARK    Erratum:[Biochem Biophys Res Commun. 2017 Oct 21;492(3):529. doi:
            10.1016/j.bbrc.2017.08.080. PMID: 28851539]
REFERENCE   3  (residues 1 to 768)
  AUTHORS   Gahete,M.D., Duran-Prado,M., Delgado-Niebla,E., Garrido,J.J.,
            Rhodes,S.J., Garcia-Navarro,S., Gracia-Navarro,F., Malagon,M.M.,
            Luque,R.M. and Castano,J.P.
  TITLE     Porcine sst1 can physically interact with other somatostatin
            receptors, and its expression is regulated by
            metabolic/inflammatory sensors
  JOURNAL   Am J Physiol Endocrinol Metab 306 (5), E483-E493 (2014)
   PUBMED   24368669
REFERENCE   4  (residues 1 to 768)
  AUTHORS   Dumay-Odelot,H., Durrieu-Gaillard,S., Da Silva,D., Roeder,R.G. and
            Teichmann,M.
  TITLE     Cell growth- and differentiation-dependent regulation of RNA
            polymerase III transcription
  JOURNAL   Cell Cycle 9 (18), 3687-3699 (2010)
   PUBMED   20890107
  REMARK    Review article
REFERENCE   5  (residues 1 to 768)
  AUTHORS   Wang,P., Wang,Q., Sun,J., Wu,J., Li,H., Zhang,N., Huang,Y., Su,B.,
            Li,R.K., Liu,L., Zhang,Y., Elsholtz,H.P., Hu,J., Gaisano,H.Y. and
            Jin,T.
  TITLE     POU homeodomain protein Oct-1 functions as a sensor for cyclic AMP
  JOURNAL   J Biol Chem 284 (39), 26456-26465 (2009)
   PUBMED   19617623
  REMARK    GeneRIF: Data show that cAMP elevation reduces nuclear Oct-1
            content in primary pancreatic islet cells.
REFERENCE   6  (residues 1 to 768)
  AUTHORS   Dailey,L., Yuan,H. and Basilico,C.
  TITLE     Interaction between a novel F9-specific factor and octamer-binding
            proteins is required for cell-type-restricted activity of the
            fibroblast growth factor 4 enhancer
  JOURNAL   Mol Cell Biol 14 (12), 7758-7769 (1994)
   PUBMED   7969117
REFERENCE   7  (residues 1 to 768)
  AUTHORS   Rosfjord,E. and Rizzino,A.
  TITLE     The octamer motif present in the Rex-1 promoter binds Oct-1 and
            Oct-3 expressed by EC cells and ES cells
  JOURNAL   Biochem Biophys Res Commun 203 (3), 1795-1802 (1994)
   PUBMED   7945330
REFERENCE   8  (residues 1 to 768)
  AUTHORS   Lillycrop,K.A. and Latchman,D.S.
  TITLE     Cloning and sequencing of the rat Oct-1 POU box
  JOURNAL   Nucleic Acids Res 19 (13), 3744 (1991)
   PUBMED   1677182
REFERENCE   9  (residues 1 to 768)
  AUTHORS   Timchenko,N.A., Zhuchenko,O.P., Timchenko,L.T., Iguchi-Ariga,S.M.,
            Ariga,H., Bozhkov,V.M. and Tomilin,N.V.
  TITLE     Rat DNA sequence associated with a complex form of DNA polymerase
            alpha in nonregenerating liver interacts with a ubiquitous
            transcription/replication factor Oct-1
  JOURNAL   Biomed Sci 2 (6), 595-600 (1991)
   PUBMED   1841628
REFERENCE   10 (residues 1 to 768)
  AUTHORS   Scholer,H.R., Ruppert,S., Suzuki,N., Chowdhury,K. and Gruss,P.
  TITLE     New type of POU domain in germ line-specific protein Oct-4
  JOURNAL   Nature 344 (6265), 435-439 (1990)
   PUBMED   1690859
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DV214198.1 and U17013.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_341149.3, XP_001075635.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q23"
     Protein         1..768
                     /product="POU domain, class 2, transcription factor 1"
                     /note="NF-A1; OTF-1; oct-1; octamer-binding transcription
                     factor 1; octamer-binding protein 1"
                     /calculated_mol_wt=78640
     Region          303..377
                     /region_name="POU"
                     /note="Found in Pit-Oct-Unc transcription factors;
                     smart00352"
                     /db_xref="CDD:197673"
     Region          405..461
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          475..754
                     /region_name="POU2F1_C"
                     /note="POU domain, class 2, transcription factor 1
                     C-terminal; pfam19536"
                     /db_xref="CDD:437368"
     CDS             1..768
                     /gene="Pou2f1"
                     /coded_by="NM_001100639.1:3..2309"
                     /db_xref="GeneID:171068"
                     /db_xref="RGD:621689"
ORIGIN      
        1 madggaasqd essaaaaaaa dsrmnnpset nkssmesgda stgtqtngld fekqpvpvgg
       61 aistaqaqaf lghlhqvqla gtslqaaaqs lnvqskssee sgdsqqssqp sqqpsvqsai
      121 pqtqlmlagg qitgltltpa qqqlllqqaq aqaqllaaav qqhsasqqhs aagatisasa
      181 atpmtqipls qpiqiaqdlq qlqqlqqqnl nlqqfvlvhp ttnlqpaqfi isqtpqgqqg
      241 llqaqnlltq lpqqsqanll qpqpsitlts qpttptrtia atpiqtlpqs qttpkridtp
      301 sleepsdlee leqfaktfkq rriklgftqg dvglamgkly gndfsqttis rfealnlsfk
      361 nmcklkplle kwlndaenls sdstasspsa lnspglgaeg lnrrrkkrts ietnirvale
      421 ksfmenqkpt seditliaeq lnmekevirv wfcnrrqkek rinppssggt ssspikaifp
      481 sptslvattp slvtsstatt ltvnpvlplt saamtnlslt gttdstsnnt atvistappa
      541 ssavtspsls pspsasasts eassasetst tqttstplps plgasqvmvt asglqtaaaa
      601 alqgaaqlpa naslaamaaa aglnpglmap sqfaaggall slnpgtlgga lspalmsnst
      661 latiqalass gslpitslda tgnlvfanag gapnivtapl flnpqnlsll tsnpvslvsa
      721 aaastgnsap taslhassts tesiqnslft vasasgaast ttaaskaq
//
LOCUS       NP_001034123             334 aa            linear   ROD 28-APR-2025
DEFINITION  WD repeat-containing protein 5 [Rattus norvegicus].
ACCESSION   NP_001034123 XP_342398
VERSION     NP_001034123.1
DBSOURCE    REFSEQ: accession NM_001039034.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Topalidou,I., Cattin-Ortola,J., Pappas,A.L., Cooper,K.,
            Merrihew,G.E., MacCoss,M.J. and Ailion,M.
  TITLE     The EARP Complex and Its Interactor EIPR-1 Are Required for Cargo
            Sorting to Dense-Core Vesicles
  JOURNAL   PLoS Genet 12 (5), e1006074 (2016)
   PUBMED   27191843
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Shinsky,S.A. and Cosgrove,M.S.
  TITLE     Unique Role of the WD-40 Repeat Protein 5 (WDR5) Subunit within the
            Mixed Lineage Leukemia 3 (MLL3) Histone Methyltransferase Complex
  JOURNAL   J Biol Chem 290 (43), 25819-25833 (2015)
   PUBMED   26324722
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Ravnskjaer,K., Hogan,M.F., Lackey,D., Tora,L., Dent,S.Y.,
            Olefsky,J. and Montminy,M.
  TITLE     Glucagon regulates gluconeogenesis through KAT2B- and WDR5-mediated
            epigenetic effects
  JOURNAL   J Clin Invest 123 (10), 4318-4328 (2013)
   PUBMED   24051374
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Patel,D.J. and Wang,Z.
  TITLE     Readout of epigenetic modifications
  JOURNAL   Annu Rev Biochem 82, 81-118 (2013)
   PUBMED   23642229
  REMARK    Review article
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Shilatifard,A.
  TITLE     The COMPASS family of histone H3K4 methylases: mechanisms of
            regulation in development and disease pathogenesis
  JOURNAL   Annu Rev Biochem 81, 65-95 (2012)
   PUBMED   22663077
  REMARK    Review article
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Han,Z., Guo,L., Wang,H., Shen,Y., Deng,X.W. and Chai,J.
  TITLE     Structural basis for the specific recognition of methylated histone
            H3 lysine 4 by the WD-40 protein WDR5
  JOURNAL   Mol Cell 22 (1), 137-144 (2006)
   PUBMED   16600877
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Brown,S.A., Ripperger,J., Kadener,S., Fleury-Olela,F., Vilbois,F.,
            Rosbash,M. and Schibler,U.
  TITLE     PERIOD1-associated proteins modulate the negative limb of the
            mammalian circadian oscillator
  JOURNAL   Science 308 (5722), 693-696 (2005)
   PUBMED   15860628
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Gori,F., Divieti,P. and Demay,M.B.
  TITLE     Cloning and characterization of a novel WD-40 repeat protein that
            dramatically accelerates osteoblastic differentiation
  JOURNAL   J Biol Chem 276 (49), 46515-46522 (2001)
   PUBMED   11551928
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100156.1.
            
            On Jan 12, 2006 this sequence version replaced XP_342398.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100156.1, SRR8487226.110483.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..334
                     /product="WD repeat-containing protein 5"
                     /note="WD repeat-containing protein 5-like"
                     /calculated_mol_wt=36457
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P61964; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          <36..330
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          43..82
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          48..85
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..126
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          91..127
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            107
                     /site_type="other"
                     /note="Important for interaction with histone H3.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P61964; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          128..168
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          132..168
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            133
                     /site_type="other"
                     /note="Important for interaction with histone H3.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          169..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          175..210
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          212..253
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          217..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          256..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          261..298
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            263
                     /site_type="other"
                     /note="Important for interaction with histone H3.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          299..333
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q498M4.1)"
     Region          304..330
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            322
                     /site_type="other"
                     /note="Important for interaction with histone H3.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q498M4.1)"
     CDS             1..334
                     /gene="Wdr5"
                     /coded_by="NM_001039034.1:365..1369"
                     /db_xref="GeneID:362093"
                     /db_xref="RGD:1305159"
ORIGIN      
        1 mateekkpet eaaraqptps ssatqskptp vkpnyalkft laghtkavss vkfspngewl
       61 asssadklik iwgaydgkfe ktisghklgi sdvawssdsn llvsasddkt lkiwdvssgk
      121 clktlkghsn yvfccnfnpq snlivsgsfd esvriwdvkt gkclktlpah sdpvsavhfn
      181 rdgslivsss ydglcriwdt asgqclktli dddnppvsfv kfspngkyil aatldntlkl
      241 wdyskgkclk tytghkneky cifanfsvtg gkwivsgsed nlvyiwnlqt keivqklqgh
      301 tdvvistach pteniiasaa lendktiklw ksdc
//
LOCUS       NP_001103107             334 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing protein 39 [Rattus norvegicus].
ACCESSION   NP_001103107 XP_001077333
VERSION     NP_001103107.1
DBSOURCE    REFSEQ: accession NM_001109637.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Will,R.D., Eden,M., Just,S., Hansen,A., Eder,A., Frank,D., Kuhn,C.,
            Seeger,T.S., Oehl,U., Wiemann,S., Korn,B., Koegl,M., Rottbauer,W.,
            Eschenhagen,T., Katus,H.A. and Frey,N.
  TITLE     Myomasp/LRRC39, a heart- and muscle-specific protein, is a novel
            component of the sarcomeric M-band and is involved in stretch
            sensing
  JOURNAL   Circ Res 107 (10), 1253-1264 (2010)
   PUBMED   20847312
  REMARK    GeneRIF: Reveal myomasp/LRRC39 as a previously unrecognized
            component of an M-band-associated signaling pathway that regulates
            cardiomyocyte gene expression in response to biomechanical stress.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473952.1.
            
            On Oct 4, 2007 this sequence version replaced XP_001077333.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ215425.1, BC158606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..334
                     /product="leucine-rich repeat-containing protein 39"
                     /note="myomasp; myosin-interacting M-band-associated
                     stress-responsive protein"
                     /calculated_mol_wt=38585
     Region          59..82
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          61..>280
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          83..105
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          85..107
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..128
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          108..127
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..151
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          131..153
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="LRR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          154..177
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..198
                     /region_name="LRR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          178..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          199..221
                     /region_name="LRR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          201..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          223..244
                     /region_name="LRR 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          224..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          245..269
                     /region_name="LRR 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     Region          247..269
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          272..295
                     /region_name="LRR 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZXS4.1)"
     CDS             1..334
                     /gene="Lrrc39"
                     /coded_by="NM_001109637.1:232..1236"
                     /db_xref="GeneID:691307"
                     /db_xref="RGD:1585106"
ORIGIN      
        1 mtesvvctga vstvkevwee rikkhhedvk rekefqqklv riwedrvslt klkekvtred
       61 griilrieke ewktlpssll klnqlqewql hrtgllkipe figrfqhliv ldlsrntise
      121 iprgiglltr lqelilsynk iktvpkelsn casleklela vnrdisdlpt elskllklth
      181 ldlsmnqftt iplavldmpa lewldmgsns lqqlpdtldr mqslhtlwlq rneitclpet
      241 irnmknlgtl vlsnnklqdi pgcmeemtsl rfvnfrdnpl rlevtlppsd dvdgeeeqel
      301 fglqfmhayi qesrrtedqv nclthtpsst rsdg
//
LOCUS       NP_001100922             191 aa            linear   ROD 28-APR-2025
DEFINITION  programmed cell death protein 6 [Rattus norvegicus].
ACCESSION   NP_001100922 XP_001056202 XP_217732
VERSION     NP_001100922.1
DBSOURCE    REFSEQ: accession NM_001107452.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Sargeant,J., Seiler,D.K., Costain,T., Madreiter-Sokolowski,C.T.,
            Gordon,D.E., Peden,A.A., Malli,R., Graier,W.F. and Hay,J.C.
  TITLE     ALG-2 and peflin regulate COPII targeting and secretion in response
            to calcium signaling
  JOURNAL   J Biol Chem 297 (6), 101393 (2021)
   PUBMED   34762908
  REMARK    GeneRIF: ALG-2 and peflin regulate COPII targeting and secretion in
            response to calcium signaling.
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Kanadome,T., Shibata,H., Kuwata,K., Takahara,T. and Maki,M.
  TITLE     The calcium-binding protein ALG-2 promotes endoplasmic reticulum
            exit site localization and polymerization of Trk-fused gene (TFG)
            protein
  JOURNAL   FEBS J 284 (1), 56-76 (2017)
   PUBMED   27813252
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Ma,J., Zhang,X., Feng,Y., Zhang,H., Wang,X., Zheng,Y., Qiao,W. and
            Liu,X.
  TITLE     Structural and Functional Study of Apoptosis-linked
            Gene-2.Heme-binding Protein 2 Interactions in HIV-1 Production
  JOURNAL   J Biol Chem 291 (52), 26670-26685 (2016)
   PUBMED   27784779
REFERENCE   4  (residues 1 to 191)
  AUTHORS   McGourty,C.A., Akopian,D., Walsh,C., Gorur,A., Werner,A.,
            Schekman,R., Bautista,D. and Rape,M.
  TITLE     Regulation of the CUL3 Ubiquitin Ligase by a Calcium-Dependent
            Co-adaptor
  JOURNAL   Cell 167 (2), 525-538 (2016)
   PUBMED   27716508
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Tanner,J.J., Frey,B.B., Pemberton,T. and Henzl,M.T.
  TITLE     EF5 Is the High-Affinity Mg(2+) Site in ALG-2
  JOURNAL   Biochemistry 55 (36), 5128-5141 (2016)
   PUBMED   27541325
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Lee,J.H., Rho,S.B. and Chun,T.
  TITLE     Programmed cell death 6 (PDCD6) protein interacts with
            death-associated protein kinase 1 (DAPk1): additive effect on
            apoptosis via caspase-3 dependent pathway
  JOURNAL   Biotechnol Lett 27 (14), 1011-1015 (2005)
   PUBMED   16132846
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Rao,R.V., Poksay,K.S., Castro-Obregon,S., Schilling,B., Row,R.H.,
            del Rio,G., Gibson,B.W., Ellerby,H.M. and Bredesen,D.E.
  TITLE     Molecular components of a cell death pathway activated by
            endoplasmic reticulum stress
  JOURNAL   J Biol Chem 279 (1), 177-187 (2004)
   PUBMED   14561754
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Kitaura,Y., Satoh,H., Takahashi,H., Shibata,H. and Maki,M.
  TITLE     Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
            by dimerization through their fifth EF-hand regions
  JOURNAL   Arch Biochem Biophys 399 (1), 12-18 (2002)
   PUBMED   11883899
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Missotten,M., Nichols,A., Rieger,K. and Sadoul,R.
  TITLE     Alix, a novel mouse protein undergoing calcium-dependent
            interaction with the apoptosis-linked-gene 2 (ALG-2) protein
  JOURNAL   Cell Death Differ 6 (2), 124-129 (1999)
   PUBMED   10200558
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Vito,P., Lacana,E. and D'Adamio,L.
  TITLE     Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and
            Alzheimer's disease gene ALG-3
  JOURNAL   Science 271 (5248), 521-525 (1996)
   PUBMED   8560270
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474002.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001056202.1, XP_217732.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213638.1, FQ234686.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..191
                     /product="programmed cell death protein 6"
                     /note="apoptosis-linked gene 2 protein homolog"
                     /calculated_mol_wt=21773
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:O75340; propagated from
                     UniProtKB/Swiss-Prot (G3V7W1.1)"
     Region          27..191
                     /region_name="EFh_PEF_ALG-2"
                     /note="EF-hand, calcium binding motif, found in
                     apoptosis-linked gene 2 protein (ALG-2) and similar
                     proteins; cd16183"
                     /db_xref="CDD:320058"
     Region          27..56
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320058"
     Site            order(36,38,40,47,103,105,107,114,169,171,173)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320058"
     Region          64..93
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320058"
     Site            order(71..72,74,91,94..95,122..123,159,162,165..166,169,
                     172,174)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320058"
     Region          94..124
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320058"
     Site            order(124,130,133..134,137,158,161..162,164..165,174..181,
                     183..184,187..188,191)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320058"
     Region          130..159
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320058"
     Region          160..191
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320058"
     CDS             1..191
                     /gene="Pdcd6"
                     /gene_synonym="ALG-2"
                     /coded_by="NM_001107452.1:123..698"
                     /db_xref="GeneID:308061"
                     /db_xref="RGD:1311239"
ORIGIN      
        1 maaysyrpgp gagpgpaaga alpdqsflwn vfqrvdkdrs gvisdnelqq alsngtwtpf
       61 npvtvrsiis mfdrenkagv nfseftgvwk yitdwqnvfr tydrdnsgmi dkhelkqals
      121 gfgyrlsdqf hdilirkfdr qgrgqiafdd fiqgcivlqr ltdifrrydt dqdgwiqvsy
      181 eqylsmvfsi v
//
LOCUS       NP_001102191             153 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich membrane anchor 1 precursor [Rattus norvegicus].
ACCESSION   NP_001102191 XP_001066450 XP_001073629
VERSION     NP_001102191.2
DBSOURCE    REFSEQ: accession NM_001108721.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Xie,H.Q., Liang,D., Leung,K.W., Chen,V.P., Zhu,K.Y., Chan,W.K.,
            Choi,R.C., Massoulie,J. and Tsim,K.W.
  TITLE     Targeting acetylcholinesterase to membrane rafts: a function
            mediated by the proline-rich membrane anchor (PRiMA) in neurons
  JOURNAL   J Biol Chem 285 (15), 11537-11546 (2010)
   PUBMED   20147288
  REMARK    GeneRIF: PRiMA in neurons has a role in targeting
            acetylcholinesterase to membrane rafts
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Tsim,K.W., Leung,K.W., Mok,K.W., Chen,V.P., Zhu,K.Y., Zhu,J.T.,
            Guo,A.J., Bi,C.W., Zheng,K.Y., Lau,D.T., Xie,H.Q. and Choi,R.C.
  TITLE     Expression and Localization of PRiMA-linked globular form
            acetylcholinesterase in vertebrate neuromuscular junctions
  JOURNAL   J Mol Neurosci 40 (1-2), 40-46 (2010)
   PUBMED   19680821
  REMARK    GeneRIF: These findings suggest that the restricted localization of
            PRiMA-linked G4 AChE at the nmjs could be contributed by the
            pre-synaptic motor neuron and/or the post-synaptic muscle fiber.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Leung,K.W., Xie,H.Q., Chen,V.P., Mok,M.K., Chu,G.K., Choi,R.C. and
            Tsim,K.W.
  TITLE     Restricted localization of proline-rich membrane anchor (PRiMA) of
            globular form acetylcholinesterase at the neuromuscular
            junctions--contribution and expression from motor neurons
  JOURNAL   FEBS J 276 (11), 3031-3042 (2009)
   PUBMED   19490106
  REMARK    GeneRIF: Data show that after denervation, the expression of PRiMA,
            AChE(T) and G(4) AChE decreased markedly in the spinal cord, and in
            fast- and slow-twitch muscles.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Xie,H.Q., Choi,R.C., Leung,K.W., Chen,V.P., Chu,G.K. and Tsim,K.W.
  TITLE     Transcriptional regulation of proline-rich membrane anchor (PRiMA)
            of globular form acetylcholinesterase in neuron: an inductive
            effect of neuron differentiation
  JOURNAL   Brain Res 1265, 13-23 (2009)
   PUBMED   19368807
  REMARK    GeneRIF: These results suggested that a MAP kinase signaling
            pathway served as one of the transcriptional regulators in
            controlling PRiMA gene expression during the neuronal
            differentiation process.
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Noureddine,H., Carvalho,S., Schmitt,C., Massoulie,J. and Bon,S.
  TITLE     Acetylcholinesterase associates differently with its anchoring
            proteins ColQ and PRiMA
  JOURNAL   J Biol Chem 283 (30), 20722-20732 (2008)
   PUBMED   18511416
  REMARK    GeneRIF: Acetylcholinesterase associates differently with its
            anchoring proteins ColQ and PRiMA
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Perrier,A.L., Massoulie,J. and Krejci,E.
  TITLE     PRiMA: the membrane anchor of acetylcholinesterase in the brain
  JOURNAL   Neuron 33 (2), 275-285 (2002)
   PUBMED   11804574
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On or before Sep 25, 2008 this sequence version replaced
            XP_001073629.1, XP_001066450.1, NP_001102191.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2407620.1,
                                           SRR26360176.1188233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..153
                     /product="proline-rich membrane anchor 1 precursor"
                     /calculated_mol_wt=12511
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4003
     mat_peptide     36..153
                     /product="Proline-rich membrane anchor 1.
                     /id=PRO_0000410722"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZP4.1)"
                     /calculated_mol_wt=12511
     Region          37..153
                     /region_name="PRIMA1"
                     /note="Proline-rich membrane anchor 1; pfam16101"
                     /db_xref="CDD:406495"
     Region          59..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZP4.1)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZZP4.1)"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZP4.1)"
     Region          133..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZP4.1)"
     CDS             1..153
                     /gene="Prima1"
                     /gene_synonym="PRiMA; Prima1l"
                     /coded_by="NM_001108721.2:103..564"
                     /db_xref="GeneID:690195"
                     /db_xref="RGD:1583978"
ORIGIN      
        1 mllrdlvlrh gccwpslllh calhplwglv qvthaepqks cskvtdscqh icqcrppppl
       61 pppppppppp rllsapapns tscpaedsww sglviivavv caslvfltvl viicykaikr
      121 kplrkdenga svaeypmsss psnkgvdvna avv
//
LOCUS       NP_446293               1929 aa            linear   ROD 28-APR-2025
DEFINITION  lactase/phlorizin hydrolase preproprotein [Rattus norvegicus].
ACCESSION   NP_446293 XP_001055600 XP_001055660 XP_341116
VERSION     NP_446293.1
DBSOURCE    REFSEQ: accession NM_053841.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1929)
  AUTHORS   Chaudhry,K.K., Mahmood,S. and Mahmood,A.
  TITLE     Hormone induced changes in lactase glycosylation in developing rat
            intestine
  JOURNAL   Mol Cell Biochem 318 (1-2), 183-190 (2008)
   PUBMED   18712286
  REMARK    GeneRIF: These findings suggest the role of these hormones in
            inducing changes in lactase glycosylation during postnatal
            development of intestine, which may contribute to adult-type
            hypolactasia in rats.
REFERENCE   2  (residues 1 to 1929)
  AUTHORS   Chaudhry,K.K., Mahmood,S. and Mahmood,A.
  TITLE     Hormone induced expression of brush border lactase in suckling rat
            intestine
  JOURNAL   Mol Cell Biochem 312 (1-2), 11-16 (2008)
   PUBMED   18273561
  REMARK    GeneRIF: Thyroxine, insulin or cortisone induced changes in lactase
            expression in suckling rat intestine.
REFERENCE   3  (residues 1 to 1929)
  AUTHORS   Akiyama,K., Morita,H., Suetsugu,S., Kuraba,S., Numata,Y.,
            Yamamoto,Y., Inui,K., Ideura,T., Wakisaka,N., Nakano,K., Oniki,H.,
            Takenawa,T., Matsuyama,M. and Yoshimura,A.
  TITLE     Actin -related protein 3 (Arp3) is mutated in proteinuric BUF/Mna
            rats
  JOURNAL   Mamm Genome 19 (1), 41-50 (2008)
   PUBMED   18064521
REFERENCE   4  (residues 1 to 1929)
  AUTHORS   Jurjus,A., Barada,K., Khoury,N., Assef,M.D., Foltzer,C.J.,
            Reimund,J.M. and Kedinger,M.
  TITLE     Morphological and biochemical alterations in the jejunum following
            iodoacetamide-induced colitis in rats
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1191-1203 (2006)
   PUBMED   17218984
REFERENCE   5  (residues 1 to 1929)
  AUTHORS   Kuranuki,S., Mochizuki,K. and Goda,T.
  TITLE     Dietary sucrose enhances intestinal lactase gene expression in
            euthyroid rats
  JOURNAL   J Nutr Sci Vitaminol (Tokyo) 52 (5), 347-351 (2006)
   PUBMED   17190105
REFERENCE   6  (residues 1 to 1929)
  AUTHORS   Scherer,W., Penugonda,B., Allen,K., Ruiz,M. and Poveda,C.
  TITLE     Bonding amalgam to tooth structure: a scanning electron microscope
            study
  JOURNAL   J Esthet Dent 4 (6), 199-201 (1992)
   PUBMED   1299293
REFERENCE   7  (residues 1 to 1929)
  AUTHORS   Boukamel,R. and Freund,J.N.
  TITLE     The rat LPH gene 5' region: comparative structure with the human
            gene
  JOURNAL   DNA Seq 3 (2), 119-121 (1992)
   PUBMED   1339333
REFERENCE   8  (residues 1 to 1929)
  AUTHORS   Duluc,I., Boukamel,R., Mantei,N., Semenza,G., Raul,F. and
            Freund,J.N.
  TITLE     Sequence of the precursor of intestinal lactase-phlorizin hydrolase
            from fetal rat
  JOURNAL   Gene 103 (2), 275-276 (1991)
   PUBMED   1909681
REFERENCE   9  (residues 1 to 1929)
  AUTHORS   Buller,H.A., Kothe,M.J., Goldman,D.A., Grubman,S.A., Sasak,W.V.,
            Matsudaira,P.T., Montgomery,R.K. and Grand,R.J.
  TITLE     Coordinate expression of lactase-phlorizin hydrolase mRNA and
            enzyme levels in rat intestine during development
  JOURNAL   J Biol Chem 265 (12), 6978-6983 (1990)
   PUBMED   1691182
  REMARK    Erratum:[J Biol Chem 1990 Aug 5;265(22):13410]
REFERENCE   10 (residues 1 to 1929)
  AUTHORS   Leese,H.J. and Semenza,G.
  TITLE     On the identity between the small intestinal enzymes phlorizin
            hydrolase and glycosylceramidase
  JOURNAL   J Biol Chem 248 (23), 8170-8173 (1973)
   PUBMED   4752949
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_001055660.1, XP_001055600.1, XP_341116.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. The extent of this transcript is supported
            by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760434
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1929
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..1929
                     /product="lactase/phlorizin hydrolase preproprotein"
                     /EC_number="3.2.1.108"
                     /EC_number="3.2.1.62"
                     /note="lactase-phlorizin hydrolase;
                     lactase-glycosylceramidase"
                     /calculated_mol_wt=215349
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2280
     Region          46..289
                     /region_name="Glycosyl hydrolase-1 1, Region I.
                     /evidence=ECO:0000250|UniProtKB:P09849, ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02401.2)"
     Region          86..>224
                     /region_name="Glycosyl hydrolases"
                     /note="A functionally diverse superfamily containing
                     glycosyl hydrolase families 1,5,10,17,44,72, and others;
                     cl23725"
                     /db_xref="CDD:474034"
     Site            370
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Region          380..849
                     /region_name="Glycosyl hydrolases"
                     /note="A functionally diverse superfamily containing
                     glycosyl hydrolase families 1,5,10,17,44,72, and others;
                     cl23725"
                     /db_xref="CDD:474034"
     Site            514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            825
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     mat_peptide     869..1929
                     /product="Lactase/phlorizin hydrolase.
                     /evidence=ECO:0000250|UniProtKB:P09849.
                     /id=PRO_0000011772"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02401.2)"
                     /calculated_mol_wt=120732
     Region          902..1366
                     /region_name="Glyco_hydro_1"
                     /note="Glycosyl hydrolase family 1; pfam00232"
                     /db_xref="CDD:395176"
     Region          905..1368
                     /region_name="Glycosyl hydrolase-1 3, Region III.
                     Phlorizin hydrolase/Glycosylceramidase activity.
                     /evidence=ECO:0000250|UniProtKB:P09849, ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02401.2)"
     Site            937
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            992
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1038
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1282
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Region          1375..1848
                     /region_name="Glycosyl hydrolase-1 4, Region IV. Lactase
                     activity. /evidence=ECO:0000250|UniProtKB:P09849,
                     ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02401.2)"
     Region          1375..1842
                     /region_name="Glyco_hydro_1"
                     /note="Glycosyl hydrolase family 1; pfam00232"
                     /db_xref="CDD:395176"
     Site            1510
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1658
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1763
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1816
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02401.2)"
     Site            1885..1903
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02401.2)"
     CDS             1..1929
                     /gene="Lct"
                     /gene_synonym="Lph"
                     /coded_by="NM_053841.1:2..5791"
                     /db_xref="GeneID:116569"
                     /db_xref="RGD:620823"
ORIGIN      
        1 melpwtalfl stvllglscq gsdwesdrnf isaagpltnd lvlnlnyppg kqgsdvvsgn
       61 tdiyicqqpl psflsqyfss lrasqvthyk vllswaqllp tgssknpdqe avqcyrqllq
      121 slkdaqlepm vvlchqtppt ssaiqregaf adlfadyatl afqsfgdlve iwftfsdlek
      181 vimdlphkdl kasalqtlsn ahrrafdiyh rkfssqggkl svvlkaedip ellpdpalaa
      241 lvqgsvdfls ldlsyecqsv atlpqklsel qnlepkvkvf iytlkledcp atgtspssll
      301 islleainkd qiqtvgfdvn aflsctsnse espscsltds lalqteqqqe tavpsspgsa
      361 yqrvwaafan qsreerdafl qdvfpegflw gistgafnve ggwaeggrgp siwdhygnln
      421 aaegqatakv asdsyhkpas dvallrgira qvykfsisws rlfptgqkst pnrqgvayyn
      481 klidrlldsh iepmatlfhw dlpqalqeqg gwqnesvvea fldyaafcfs tfgdrvklwv
      541 tfhepwvmsy agygtgqhap aisdpgmasf kvahlilkah artwhlydlh hrlqqqgrvg
      601 ivlnsdwaep ldrkspqdla aaerflhfml gwfahpifvd gdypttlraq iqhinqqcgh
      661 plaqlpefte aekrllkgsa dflglshyts rliskagrqt ctssydnigg fsqhvdpewp
      721 qtaspwirvv pwgirrllrf asmeytkgkl piflagngmp vgeeadlfdd svrvnyfnly
      781 inevlkavke dlvdvrsyiv rslidgyegp lgfsqrfgly hvnfndssrp rtprksayff
      841 tsiiekngfs akkvkrnplp vradftsrar vtdslpsevp skakivwekf skqprferdl
      901 fyhgtfrddf lwgvsssayq ieggwnadgk gpsiwdnfth tpgngvkdna tgdvacdsyh
      961 qldadlnilr tlkvksyrfs iswsrifptg rnstinkqgv dyynrlidsl vdnnifpmvt
     1021 lfhwdlpqal qdiggwenps lielfdsyad fcfktfgdrv kfwmtfnepw chvvlgyssg
     1081 ifppsvqepg wlpykvshiv ikaharvyht ydekyrseqk gvislslnth waepkdpglq
     1141 rdveaadrml qftmgwfahp ifkngdypdv mkwtvgnrse lqhlassrlp tfteeeknyv
     1201 rgtadvfcin tytsvfvqhs tprlnppsyd ddmelkliem nsstgvmhpd vpwgtrrlln
     1261 wikeeygnip iyitengqgl enptlddter ifyhktyine alkaykldgv dlrgysawtl
     1321 mddfewllgy tmrfglyhvd fnhvsrprta rasaryyaev ianngmplar edeflygefp
     1381 kgfiwsaasa syqvegawra dgkglsiwdt fshtplrign ddngdvacds yhkiaedvva
     1441 lqnlgvshyr fsiawsrilp dgttkfinea glsyyvrfid allaagitpq vtiyhwdlpq
     1501 alqdvggwen etivqrfkey advlfqrlgd rvkfwitlne pfviaaqgyg tgvsapgisf
     1561 rpgtapyiag hnlikahaea whlyndvyra rqggtisiti ssdwaeprdp tnqgdveaar
     1621 ryvqfmggwf ahpifkngdy pevmktrird rslaaglnks rlpeftesek srikgtfdff
     1681 gfnhyttvla ynldypaafs sfdadrgvas iadsswpvsg sfwlkvtpfg frrilnwlke
     1741 eynnppiyvt engvsrrgep elndtdriyy lrsyinealk avqdkvdlrg ytvwsimdnf
     1801 ewatgfaerf gvhfvnrsdp slpripkasa kfyativrcn gfpdpaqgph pclqqpedaa
     1861 ptaspvqsev pflglmlgia eaqtalyvlf allllgacsl afltykycrr skqgnaqpsq
     1921 hqlspissf
//
LOCUS       NP_001101549             352 aa            linear   ROD 28-APR-2025
DEFINITION  carbohydrate sulfotransferase 11 [Rattus norvegicus].
ACCESSION   NP_001101549 XP_001079715 XP_235007
VERSION     NP_001101549.1
DBSOURCE    REFSEQ: accession NM_001108079.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Izumikawa,T., Okuura,Y., Koike,T., Sakoda,N. and Kitagawa,H.
  TITLE     Chondroitin 4-O-sulfotransferase-1 regulates the chain length of
            chondroitin sulfate in co-operation with chondroitin
            N-acetylgalactosaminyltransferase-2
  JOURNAL   Biochem J 434 (2), 321-331 (2011)
   PUBMED   21138417
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Kluppel,M., Wight,T.N., Chan,C., Hinek,A. and Wrana,J.L.
  TITLE     Maintenance of chondroitin sulfation balance by
            chondroitin-4-sulfotransferase 1 is required for chondrocyte
            development and growth factor signaling during cartilage
            morphogenesis
  JOURNAL   Development 132 (17), 3989-4003 (2005)
   PUBMED   16079159
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Okuda,T., Mita,S., Yamauchi,S., Matsubara,T., Yagi,F., Yamamori,D.,
            Fukuta,M., Kuroiwa,A., Matsuda,Y. and Habuchi,O.
  TITLE     Molecular cloning, expression, and chromosomal mapping of human
            chondroitin 4-sulfotransferase, whose expression pattern in human
            tissues is different from that of chondroitin 6-sulfotransferase
  JOURNAL   J Biochem 128 (5), 763-770 (2000)
   PUBMED   11056388
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Yamauchi,S., Mita,S., Matsubara,T., Fukuta,M., Habuchi,H.,
            Kimata,K. and Habuchi,O.
  TITLE     Molecular cloning and expression of chondroitin 4-sulfotransferase
  JOURNAL   J Biol Chem 275 (12), 8975-8981 (2000)
   PUBMED   10722746
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473960.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001079715.1, XP_235007.3.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN06680432, SAMN12840116
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q13"
     Protein         1..352
                     /product="carbohydrate sulfotransferase 11"
                     /EC_number="2.8.2.5"
                     /note="C4ST; C4S-1; C4ST-1; chondroitin 4-sulfotransferase
                     1; chondroitin 4-O-sulfotransferase 1; carbohydrate
                     (chondroitin 4) sulfotransferase 11"
                     /calculated_mol_wt=41495
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P69478.1)"
     Region          113..344
                     /region_name="Sulfotransfer_2"
                     /note="Sulfotransferase family; pfam03567"
                     /db_xref="CDD:427369"
     Site            205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69478.1)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69478.1)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P69478.1)"
     Site            342
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P69478.1)"
     CDS             1..352
                     /gene="Chst11"
                     /gene_synonym="C4ST1"
                     /coded_by="NM_001108079.1:368..1426"
                     /db_xref="GeneID:314694"
                     /db_xref="RGD:1308400"
ORIGIN      
        1 mkpallevmr mnricrmvla tclgsfilvi fyfqsmlhpv mrrnpfgvdi ccrkgsrspl
       61 qelynpiqle lsntailhqm rrdqvtdtcr ansamsrkrr vltpndlkhl vvdedheliy
      121 cyvpkvactn wkrlmmvlsg rgkysdpmei paneahvsan lktlnqysip einhrlksym
      181 kflfvrepfe rlvsayrnkf tqkyntsfhk rygtkiirrq rknatqealr kgddvkfeef
      241 vaylidphtq reepfnehwq tvyslchpch ihydlvgkye tleedsnyvl rlagvsgylk
      301 fptyakstrt tdemtteffq nisaehqtql yevykldflm fnysvpnylk ld
//
LOCUS       NP_058919                656 aa            linear   ROD 28-APR-2025
DEFINITION  sodium-dependent phosphate transporter 2 [Rattus norvegicus].
ACCESSION   NP_058919
VERSION     NP_058919.1
DBSOURCE    REFSEQ: accession NM_017223.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Prie,D., Torres,P.U. and Friedlander,G.
  TITLE     Phosphate handling: new genes, new molecules
  JOURNAL   Horm Res Paediatr 76 Suppl 1, 71-75 (2011)
   PUBMED   21778753
  REMARK    Review article
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Picard,N., Capuano,P., Stange,G., Mihailova,M., Kaissling,B.,
            Murer,H., Biber,J. and Wagner,C.A.
  TITLE     Acute parathyroid hormone differentially regulates renal brush
            border membrane phosphate cotransporters
  JOURNAL   Pflugers Arch 460 (3), 677-687 (2010)
   PUBMED   20526720
  REMARK    GeneRIF: expression in renal brush border reduced by parathyroid
            hormone
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Villa-Bellosta,R. and Sorribas,V.
  TITLE     Compensatory regulation of the sodium/phosphate cotransporters
            NaPi-IIc (SCL34A3) and Pit-2 (SLC20A2) during Pi deprivation and
            acidosis
  JOURNAL   Pflugers Arch 459 (3), 499-508 (2010)
   PUBMED   19841935
  REMARK    GeneRIF: Results describe the regulation of the sodium/phosphate
            cotransporters SCL34A3 and SLC20A2 during phosphate deprivation and
            acidosis in rat kidney.
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Breusegem,S.Y., Takahashi,H., Giral-Arnal,H., Wang,X., Jiang,T.,
            Verlander,J.W., Wilson,P., Miyazaki-Anzai,S., Sutherland,E.,
            Caldas,Y., Blaine,J.T., Segawa,H., Miyamoto,K., Barry,N.P. and
            Levi,M.
  TITLE     Differential regulation of the renal sodium-phosphate
            cotransporters NaPi-IIa, NaPi-IIc, and PiT-2 in dietary potassium
            deficiency
  JOURNAL   Am J Physiol Renal Physiol 297 (2), F350-F361 (2009)
   PUBMED   19493963
  REMARK    GeneRIF: Differential regulation of the renal sodium-phosphate
            cotransporters NaPi-IIa, NaPi-IIc, and PiT-2 in dietary potassium
            deficiency.
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Villa-Bellosta,R., Bogaert,Y.E., Levi,M. and Sorribas,V.
  TITLE     Characterization of phosphate transport in rat vascular smooth
            muscle cells: implications for vascular calcification
  JOURNAL   Arterioscler Thromb Vasc Biol 27 (5), 1030-1036 (2007)
   PUBMED   17322102
  REMARK    GeneRIF: We have used RNA interference to demonstrate that Pit1 and
            Pit2 are the transporters responsible for Na-dependent Pi transport
            in VSMCs.
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Frei,P., Gao,B., Hagenbuch,B., Mate,A., Biber,J., Murer,H.,
            Meier,P.J. and Stieger,B.
  TITLE     Identification and localization of sodium-phosphate cotransporters
            in hepatocytes and cholangiocytes of rat liver
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 288 (4), G771-G778 (2005)
   PUBMED   15564340
  REMARK    GeneRIF: PiT-1 (Slc20a1) and PiT-2 (Slc20a2) were detected at the
            basolateral membrane of hepatocytes.
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Wada,K., Mizuno,M., Komori,T. and Tamura,M.
  TITLE     Extracellular inorganic phosphate regulates gibbon ape leukemia
            virus receptor-2/phosphate transporter mRNA expression in rat bone
            marrow stromal cells
  JOURNAL   J Cell Physiol 198 (1), 40-47 (2004)
   PUBMED   14584042
  REMARK    GeneRIF: mRNA expression level of Glvr-2 was increased by the
            addition of inorganic phosphate (Pi) in bone marrow stromal cells
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Miller,D.G. and Miller,A.D.
  TITLE     A family of retroviruses that utilize related phosphate
            transporters for cell entry
  JOURNAL   J Virol 68 (12), 8270-8276 (1994)
   PUBMED   7966619
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Kavanaugh,M.P., Miller,D.G., Zhang,W., Law,W., Kozak,S.L., Kabat,D.
            and Miller,A.D.
  TITLE     Cell-surface receptors for gibbon ape leukemia virus and
            amphotropic murine retrovirus are inducible sodium-dependent
            phosphate symporters
  JOURNAL   Proc Natl Acad Sci U S A 91 (15), 7071-7075 (1994)
   PUBMED   8041748
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Miller,D.G., Edwards,R.H. and Miller,A.D.
  TITLE     Cloning of the cellular receptor for amphotropic murine
            retroviruses reveals homology to that for gibbon ape leukemia virus
  JOURNAL   Proc Natl Acad Sci U S A 91 (1), 78-82 (1994)
   PUBMED   8278411
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070908.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070908.1, SRR8487227.268257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..656
                     /product="sodium-dependent phosphate transporter 2"
                     /note="gibbon ape leukemia virus receptor 2; phosphate
                     transporter 2; receptor for amphitropic viruses 1;
                     receptor for amphotropic viruses 1; solute carrier family
                     20 (phosphate transporter), member 2"
                     /calculated_mol_wt=70617
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Region          25..>224
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            143..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08357; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08357; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q08357; propagated from
                     UniProtKB/Swiss-Prot (Q63488.1)"
     Region          <478..638
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
     Site            484..504
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            532..552
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            573..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            595..610
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     Site            623..643
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63488.1)"
     CDS             1..656
                     /gene="Slc20a2"
                     /gene_synonym="Ab1-188; Glvr2; Pit-2; RAM-1; Ram1"
                     /coded_by="NM_017223.2:415..2385"
                     /db_xref="GeneID:29502"
                     /db_xref="RGD:3699"
ORIGIN      
        1 mamdgylwmv ilgfiiafil afsvgandva nsfgtavgsg vvtlrqacil asifettgsv
       61 llgakvgeti rkgiidvnly netvetlmag evsamvgsav wqliasflrl pisgthcivg
      121 stigfslvai gpkgvqwmel vkivaswfis pllsgfmsgv lfilirmfil tkedpvpngl
      181 qalplfyaat iainvfsimy tgapvlglsl piwaialisf gvallfaffv wlfvcpwmkr
      241 kiagrlekes alsrasdesl rkvqeaespv fkelpgakas ddsavpltsl ageaagaseg
      301 tsagnhpras ygralsmthg sakspisngt fgfeghmrnd ghvyhtvhkd sglykdllhk
      361 ihvdkgpeek paqennyrll rrnnsytcyt aaicgmpvha tfrasdtssa pedseklvgd
      421 tvsyskkrlr ydsyssycna vaeaeieaee ggvemrlase ltdpdqphed paedekeekd
      481 saevhllfhf lqvltacfgs fahggndvsn aigplvalwl iykqggvtqe aatpvwllfy
      541 ggvgictglw vwgrrviqtm gkdltpitps sgftielasa ftvviasnig lpvstthckv
      601 gsvvavgwir srkavdwrlf rnifiawfvt vpvaglfsaa imallmyicg fvsssr
//
LOCUS       NP_001019427             270 aa            linear   ROD 28-APR-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 4 [Rattus
            norvegicus].
ACCESSION   NP_001019427 XP_224355
VERSION     NP_001019427.1
DBSOURCE    REFSEQ: accession NM_001024256.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Poss,Z.C., Ebmeier,C.C. and Taatjes,D.J.
  TITLE     The Mediator complex and transcription regulation
  JOURNAL   Crit Rev Biochem Mol Biol 48 (6), 575-608 (2013)
   PUBMED   24088064
  REMARK    Review article
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Krebs,A.R., Demmers,J., Karmodiya,K., Chang,N.C., Chang,A.C. and
            Tora,L.
  TITLE     ATAC and Mediator coactivators form a stable complex and regulate a
            set of non-coding RNA genes
  JOURNAL   EMBO Rep 11 (7), 541-547 (2010)
   PUBMED   20508642
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Lando,M., Holden,M., Bergersen,L.C., Svendsrud,D.H., Stokke,T.,
            Sundfor,K., Glad,I.K., Kristensen,G.B. and Lyng,H.
  TITLE     Gene dosage, expression, and ontology analysis identifies driver
            genes in the carcinogenesis and chemoradioresistance of cervical
            cancer
  JOURNAL   PLoS Genet 5 (11), e1000719 (2009)
   PUBMED   19911042
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Malik,S., Guermah,M., Yuan,C.X., Wu,W., Yamamura,S. and Roeder,R.G.
  TITLE     Structural and functional organization of TRAP220, the
            TRAP/mediator subunit that is targeted by nuclear receptors
  JOURNAL   Mol Cell Biol 24 (18), 8244-8254 (2004)
   PUBMED   15340084
  REMARK    Erratum:[Mol Cell Biol. 2022 Nov 17;42(11):e0035922. doi:
            10.1128/mcb.00359-22. PMID: 36255214]
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Wang,Q., Sharma,D., Ren,Y. and Fondell,J.D.
  TITLE     A coregulatory role for the TRAP-mediator complex in androgen
            receptor-mediated gene expression
  JOURNAL   J Biol Chem 277 (45), 42852-42858 (2002)
   PUBMED   12218053
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Kang,Y.K., Guermah,M., Yuan,C.X. and Roeder,R.G.
  TITLE     The TRAP/Mediator coactivator complex interacts directly with
            estrogen receptors alpha and beta through the TRAP220 subunit and
            directly enhances estrogen receptor function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2642-2647 (2002)
   PUBMED   11867769
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Malik,S., Gu,W., Wu,W., Qin,J. and Roeder,R.G.
  TITLE     The USA-derived transcriptional coactivator PC2 is a submodule of
            TRAP/SMCC and acts synergistically with other PCs
  JOURNAL   Mol Cell 5 (4), 753-760 (2000)
   PUBMED   10882111
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Ito,M., Yuan,C.X., Malik,S., Gu,W., Fondell,J.D., Yamamura,S.,
            Fu,Z.Y., Zhang,X., Qin,J. and Roeder,R.G.
  TITLE     Identity between TRAP and SMCC complexes indicates novel pathways
            for the function of nuclear receptors and diverse mammalian
            activators
  JOURNAL   Mol Cell 3 (3), 361-370 (1999)
   PUBMED   10198638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC093402.1.
            
            On May 27, 2005 this sequence version replaced XP_224355.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093402.1, EV763024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..270
                     /product="mediator of RNA polymerase II transcription
                     subunit 4"
                     /note="mediator of RNA polymerase II transcription,
                     subunit 4 homolog; vitamin D receptor interacting protein"
                     /calculated_mol_wt=29694
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561Q8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPJ6; propagated from
                     UniProtKB/Swiss-Prot (Q561Q8.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPJ6; propagated from
                     UniProtKB/Swiss-Prot (Q561Q8.1)"
     Region          64..>189
                     /region_name="Med4"
                     /note="Vitamin-D-receptor interacting Mediator subunit 4;
                     pfam10018"
                     /db_xref="CDD:401849"
     Region          227..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561Q8.1)"
     CDS             1..270
                     /gene="Med4"
                     /gene_synonym="Vdrip"
                     /coded_by="NM_001024256.1:13..825"
                     /db_xref="GeneID:306030"
                     /db_xref="RGD:1306671"
ORIGIN      
        1 maasssgeke kermggvsgm tglgstrerl lsaledlevl sreliemlai srnqkllqle
       61 eenqvlelli hrdgdfqelm klalnqgkvh hemqalekev ekrdsdiqql qkqlkeaeqi
      121 latavyqake klksiekark gaisseeiik yahrisasna vcapltwvpg dprrpyptdl
      181 emrsgllgqm nnpstsgvng hlpgdalaag rlpdvlapqy pwqsndmsvn mlppnhstdf
      241 lleppghnke neddvevmst dssssssdsd
//
LOCUS       NP_001103835             501 aa            linear   ROD 28-APR-2025
DEFINITION  actin nucleation-promoting factor WASL [Rattus norvegicus].
ACCESSION   NP_001103835 XP_001061794
VERSION     NP_001103835.1
DBSOURCE    REFSEQ: accession NM_001110365.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Bouslama,R., Dumont,V., Lindfors,S., Paavolainen,L., Tienari,J.,
            Nisen,H., Mirtti,T., Saleem,M.A., Gordin,D., Groop,P.H.,
            Suetsugu,S. and Lehtonen,S.
  TITLE     Phosphorylation of PACSIN2 at S313 Regulates Podocyte Architecture
            in Coordination with N-WASP
  JOURNAL   Cells 12 (11), 1487 (2023)
   PUBMED   37296607
  REMARK    GeneRIF: Phosphorylation of PACSIN2 at S313 Regulates Podocyte
            Architecture in Coordination with N-WASP.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Houy,S., Nicolas,G., Momboisse,F., Malacombe,M., Bader,M.F.,
            Vitale,N., Lecomte,M.C., Ory,S. and Gasman,S.
  TITLE     alphaII-spectrin controls calcium-regulated exocytosis in
            neuroendocrine chromaffin cells through neuronal Wiskott-Aldrich
            Syndrome protein interaction
  JOURNAL   IUBMB Life 72 (4), 544-552 (2020)
   PUBMED   31859439
  REMARK    GeneRIF: alphaII-spectrin controls calcium-regulated exocytosis in
            neuroendocrine chromaffin cells through neuronal Wiskott-Aldrich
            Syndrome protein interaction.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Okrut,J., Prakash,S., Wu,Q., Kelly,M.J. and Taunton,J.
  TITLE     Allosteric N-WASP activation by an inter-SH3 domain linker in Nck
  JOURNAL   Proc Natl Acad Sci U S A 112 (47), E6436-E6445 (2015)
   PUBMED   26554011
  REMARK    GeneRIF: Nck was the most potent activator of N-WASP-driven actin
            assembly.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Jaudon,F., Raynaud,F., Wehrle,R., Bellanger,J.M., Doulazmi,M.,
            Vodjdani,G., Gasman,S., Fagni,L., Dusart,I., Debant,A. and
            Schmidt,S.
  TITLE     The RhoGEF DOCK10 is essential for dendritic spine morphogenesis
  JOURNAL   Mol Biol Cell 26 (11), 2112-2127 (2015)
   PUBMED   25851601
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Banjade,S. and Rosen,M.K.
  TITLE     Phase transitions of multivalent proteins can promote clustering of
            membrane receptors
  JOURNAL   Elife 3, e04123 (2014)
   PUBMED   25321392
  REMARK    GeneRIF: biochemical reconstitution on supported lipid bilayers of
            protein clusters containing the adhesion receptor Nephrin and its
            cytoplasmic partners, Nck and N-WASP, is reported.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Qualmann,B. and Kelly,R.B.
  TITLE     Syndapin isoforms participate in receptor-mediated endocytosis and
            actin organization
  JOURNAL   J Cell Biol 148 (5), 1047-1062 (2000)
   PUBMED   10704453
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Qualmann,B., Roos,J., DiGregorio,P.J. and Kelly,R.B.
  TITLE     Syndapin I, a synaptic dynamin-binding protein that associates with
            the neural Wiskott-Aldrich syndrome protein
  JOURNAL   Mol Biol Cell 10 (2), 501-513 (1999)
   PUBMED   9950691
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Suetsugu,S., Miki,H. and Takenawa,T.
  TITLE     The essential role of profilin in the assembly of actin for
            microspike formation
  JOURNAL   EMBO J 17 (22), 6516-6526 (1998)
   PUBMED   9822597
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Miki,H., Sasaki,T., Takai,Y. and Takenawa,T.
  TITLE     Induction of filopodium formation by a WASP-related
            actin-depolymerizing protein N-WASP
  JOURNAL   Nature 391 (6662), 93-96 (1998)
   PUBMED   9422512
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Fukuoka,M., Miki,H. and Takenawa,T.
  TITLE     Identification of N-WASP homologs in human and rat brain
  JOURNAL   Gene 196 (1-2), 43-48 (1997)
   PUBMED   9322739
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473959.1.
            
            On Nov 16, 2007 this sequence version replaced XP_001061794.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..501
                     /product="actin nucleation-promoting factor WASL"
                     /note="neural Wiskott-Aldrich syndrome protein;
                     Wiskott-Aldrich syndrome-like"
                     /calculated_mol_wt=54165
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O00401; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     Region          28..135
                     /region_name="WH1"
                     /note="WH1 domain; pfam00568"
                     /db_xref="CDD:395450"
     Site            order(37,39,44,48,63,65,72,74,76,89,101,109,115)
                     /site_type="other"
                     /note="WAS mutation hotspots"
                     /db_xref="CDD:269916"
     Site            order(46,48,54,104,106)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269916"
     Region          135..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08816.2)"
     Region          180..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08816.2)"
     Region          199..256
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(200,203,206,208,211,229,233)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238077"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TNK2.
                     /evidence=ECO:0000250|UniProtKB:O00401; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FAK1 and TNK2.
                     /evidence=ECO:0000269|PubMed:14676198,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     Region          263..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08816.2)"
     Site            304
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O00401; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     Region          398..424
                     /region_name="WH2_N-WASP_r1"
                     /note="first tandem Wiskott Aldrich syndrome homology
                     region 2 (WH2 motif) repeat found in human Neural
                     Wiskott-Aldrich syndrome protein (N-WASP) and related
                     domains; cd22074"
                     /db_xref="CDD:409217"
     Site            order(401..402,404..406,408..410,415..418)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409217"
     Region          415..418
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409217"
     Region          425..449
                     /region_name="WH2_hN-WASP_r2_like"
                     /note="second tandem Wiskott Aldrich syndrome homology
                     region 2 (WH2 motif) repeat found in human Neural
                     Wiskott-Aldrich syndrome protein (N-WASP) and related
                     domains; cd22075"
                     /db_xref="CDD:409218"
     Site            order(430,432..434,436..438,441,443..445)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409218"
     Region          442..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08816.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00401; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00401; propagated from
                     UniProtKB/Swiss-Prot (O08816.2)"
     CDS             1..501
                     /gene="Wasl"
                     /gene_synonym="N-WASP; TRS4"
                     /coded_by="NM_001110365.1:366..1871"
                     /db_xref="GeneID:682507"
                     /db_xref="RGD:735144"
ORIGIN      
        1 mssgqqpprr vtnvgslllt pqeneslfsf lgkkcvtmss avvqlyaadr ncmwskkcsg
       61 vaclvkdnpq rsyflrifdi kdgkllweqe lynnfvynsp rgyfhtfagd tcqvalnfan
      121 eeeakkfrka vtdllgrrqr ksekrrdapn gpnlpmatvd iknpeittnr fygsqvnnis
      181 htkekkkgka kkkrltkadi gtpsnfqhig hvgwdpntgf dlnnldpelk nlfdmcgise
      241 aqlkdretsk viydfiektg gveavknelr rqapppppps rggppppppp phssgppppp
      301 argrgapppp psraptaapp ppppsrpgvv vpppppnrmy pppppalpss apsgpppppp
      361 lsmagstapp pppppppppg pppppglpsd gdhqvpassg nkaalldqir egaqlkkveq
      421 nsrpvscsgr dalldqirqg iqlksvsdgq estpptpapt sgivgalmev mqkrskaihs
      481 sdededddde edfedddewe d
//
LOCUS       NP_001121162             764 aa            linear   ROD 28-APR-2025
DEFINITION  nucleolar transcription factor 1 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001121162
VERSION     NP_001121162.1
DBSOURCE    REFSEQ: accession NM_001127690.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Edvardson,S., Nicolae,C.M., Agrawal,P.B., Mignot,C., Payne,K.,
            Prasad,A.N., Prasad,C., Sadler,L., Nava,C., Mullen,T.E.,
            Begtrup,A., Baskin,B., Powis,Z., Shaag,A., Keren,B., Moldovan,G.L.
            and Elpeleg,O.
  TITLE     Heterozygous De Novo UBTF Gain-of-Function Variant Is Associated
            with Neurodegeneration in Childhood
  JOURNAL   Am J Hum Genet 101 (2), 267-273 (2017)
   PUBMED   28777933
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Sun,X., Chen,H., Deng,Z., Hu,B., Luo,H., Zeng,X., Han,L., Cai,G.
            and Ma,L.
  TITLE     The Warsaw breakage syndrome-related protein DDX11 is required for
            ribosomal RNA synthesis and embryonic development
  JOURNAL   Hum Mol Genet 24 (17), 4901-4915 (2015)
   PUBMED   26089203
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Nonnekens,J., Perez-Fernandez,J., Theil,A.F., Gadal,O., Bonnart,C.
            and Giglia-Mari,G.
  TITLE     Mutations in TFIIH causing trichothiodystrophy are responsible for
            defects in ribosomal RNA production and processing
  JOURNAL   Hum Mol Genet 22 (14), 2881-2893 (2013)
   PUBMED   23562818
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     TFIIB-related factors in RNA polymerase I transcription
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 265-273 (2013)
   PUBMED   22960599
  REMARK    Review article
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Brehm,M.A., Wundenberg,T., Williams,J., Mayr,G.W. and Shears,S.B.
  TITLE     A non-catalytic role for inositol 1,3,4,5,6-pentakisphosphate
            2-kinase in the synthesis of ribosomal RNA
  JOURNAL   J Cell Sci 126 (Pt 2), 437-444 (2013)
   PUBMED   23203802
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Lin,C.Y., Tuan,J., Scalia,P., Bui,T. and Comai,L.
  TITLE     The cell cycle regulatory factor TAF1 stimulates ribosomal DNA
            transcription by binding to the activator UBF
  JOURNAL   Curr Biol 12 (24), 2142-2146 (2002)
   PUBMED   12498690
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Sutherland,H.G., Mumford,G.K., Newton,K., Ford,L.V., Farrall,R.,
            Dellaire,G., Caceres,J.F. and Bickmore,W.A.
  TITLE     Large-scale identification of mammalian proteins localized to
            nuclear sub-compartments
  JOURNAL   Hum Mol Genet 10 (18), 1995-2011 (2001)
   PUBMED   11555636
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Pelletier,G., Stefanovsky,V.Y., Faubladier,M.,
            Hirschler-Laszkiewicz,I., Savard,J., Rothblum,L.I., Cote,J. and
            Moss,T.
  TITLE     Competitive recruitment of CBP and Rb-HDAC regulates UBF
            acetylation and ribosomal transcription
  JOURNAL   Mol Cell 6 (5), 1059-1066 (2000)
   PUBMED   11106745
  REMARK    GeneRIF: competitive recruitment of CBP and Rb-HDAC regulates UBF
            acetylation and ribosomal transcription
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Ridsdale,R.A., Semotok,J.L., Larson,D.E., Rothblum,L.I. and
            Harauz,G.
  TITLE     Topology of recombinant rat upstream binding factor
  JOURNAL   Biochem Cell Biol 76 (4), 649-655 (1998)
   PUBMED   10099786
REFERENCE   10 (residues 1 to 764)
  AUTHORS   O'Mahony,D.J. and Rothblum,L.I.
  TITLE     Identification of two forms of the RNA polymerase I transcription
            factor UBF
  JOURNAL   Proc Natl Acad Sci U S A 88 (8), 3180-3184 (1991)
   PUBMED   2014238
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Transcript Variant: This variant (2) includes an alternate exon in
            the coding region compared to variant 1. The resulting protein
            (isoform 2) is longer but has the same N- and C-termini compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643287.25773.1,
                                           SRR26643429.39244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760386,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..764
                     /product="nucleolar transcription factor 1 isoform 2"
                     /note="nucleolar transcription factor 1; UBF-1;
                     upstream-binding factor 1; transcription factor UBF;
                     upstream binding transcription factor, RNA polymerase I"
                     /calculated_mol_wt=89306
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25977.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          109..185
                     /region_name="HMG-box_UBF1_rpt1-like"
                     /note="first high mobility group (HMG)-box found in
                     upstream-binding factor 1 (UBF1) and similar proteins;
                     cd21998"
                     /db_xref="CDD:438814"
     Site            order(113..114,116..120,123..124,131,143..144,147,
                     150..151,158,162,165,169,172)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438814"
     Region          196..270
                     /region_name="HMG-box_UBF1_rpt2"
                     /note="second high mobility group (HMG)-box found in
                     upstream-binding factor 1 (UBF1) and similar proteins;
                     cd21999"
                     /db_xref="CDD:438815"
     Site            order(197..198,200..204,207..208,215,227..228,231,
                     234..235,242,246,249,253,256)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438815"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          297..379
                     /region_name="HMG-box_UBF1_rpt3"
                     /note="third high mobility group (HMG)-box found in
                     upstream-binding factor 1 (UBF1) and similar proteins;
                     cd22000"
                     /db_xref="CDD:438816"
     Site            order(299..300,302..306,309..310,317,325..326,329,
                     332..333,340,344,347,351,354)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438816"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25976; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          370..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25977.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25976; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          405..470
                     /region_name="HMG-box_UBF1_rpt4"
                     /note="fourth high mobility group (HMG)-box found in
                     upstream-binding factor 1 (UBF1) and similar proteins;
                     cd22001"
                     /db_xref="CDD:438817"
     Site            order(408..409,411..415,418..419,426,438..439,442,
                     445..446,453,457,460,464,467)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438817"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25976; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          456..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25977.1)"
     Region          479..562
                     /region_name="HMG_box_5"
                     /note="HMG (high mobility group) box 5; pfam14887"
                     /db_xref="CDD:434287"
     Site            order(483..484,486..490,493..494,501,512..513,516,
                     519..520,527,531,534,538,541)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438818"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          546..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25977.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25976; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          565..650
                     /region_name="HMG-box_UBF1_rpt6-like"
                     /note="sixth high mobility group (HMG)-box found in
                     upstream-binding factor 1 (UBF1) and similar proteins;
                     cd22003"
                     /db_xref="CDD:438819"
     Site            order(569..570,572..576,579..580,587,597..598,601,
                     604..605,612,616,619,623,626)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438819"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25976; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17480; propagated from
                     UniProtKB/Swiss-Prot (P25977.1)"
     Region          648..764
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25977.1)"
     CDS             1..764
                     /gene="Ubtf"
                     /gene_synonym="Tcfubf"
                     /coded_by="NM_001127690.2:211..2505"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25574"
                     /db_xref="RGD:3927"
ORIGIN      
        1 mngeadcptd lemaapkgqd rwsqedmltl lecmknnlps ndsskfktte shmdwekvaf
       61 kdfsgdmckl kwveisnevr kfrtltelil daqehvknpy kgkklkkhpd fpkkpltpyf
      121 rffmekraky aklhpemsnl dltkilskky kelpekkkmk yiqdfqrekq efernlarfr
      181 edhpdliqna kksdipekpk tpqqlwythe kkvylkvrpd attkevkdsl gkqwsqlsdk
      241 krlkwihkal eqrkeyeeim rdyiqkhpel niseegitks tltkaerqlk dkfdgrptkp
      301 ppnsyslyca elmanmkdvp stermvlcsq qwkllsqkek dayhkkcdqk kkdyevellr
      361 fleslpeeeq qrvlgeekml ninkkqttsp askkpsqegg kggsekpkrp vsamfifsee
      421 krrqlqeerp elseseltrl larmwndlse kkkakykare aalkaqserk pggeredrgk
      481 lpespkraee iwqqsvigdy larfkndrvk alkamemtwn nmekkeklmw ikkaaedqkr
      541 yerelsemra ppaatnsskk mkfqgepkkp pmngyqkfsq ellsngelnh lplkermvei
      601 gsrwqrisqs qkehykklae eqqrqykvhl dlwvkslspq draaykeyis nkrknmtklr
      661 gpnpkssrtt lqskseseed ddeedddddd eeeeeddeng dssedggdss esssedesed
      721 gdeneddddd edddeddded ednesegsss sssssgdssd sdsn
//
LOCUS       NP_058766                255 aa            linear   ROD 28-APR-2025
DEFINITION  3-oxo-5-alpha-steroid 4-dehydrogenase 1 [Rattus norvegicus].
ACCESSION   NP_058766
VERSION     NP_058766.2
DBSOURCE    REFSEQ: accession NM_017070.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Su,Y., Li,H., Chen,X., Wang,Y., Li,X., Sun,J. and Ge,R.S.
  TITLE     Ziram inhibits rat neurosteroidogenic 5alpha-reductase 1 and
            3alpha-hydroxysteroid dehydrogenase
  JOURNAL   Toxicol Mech Methods 28 (1), 38-44 (2018)
   PUBMED   28707553
  REMARK    GeneRIF: Ziram inhibited SRD5A1 and AKR1C14 activities, thus
            possibly interfering with neurosteroid production in rats.
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Wang,Y., Sun,J., Chen,L., Zhou,S., Lin,H., Wang,Y., Lin,N. and
            Ge,R.S.
  TITLE     Effects of resveratrol on rat neurosteroid synthetic enzymes
  JOURNAL   Fitoterapia 122, 61-66 (2017)
   PUBMED   28823883
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Rossetti,M.F., Varayoud,J., Moreno-Piovano,G.S., Luque,E.H. and
            Ramos,J.G.
  TITLE     Environmental enrichment attenuates the age-related decline in the
            mRNA expression of steroidogenic enzymes and reduces the
            methylation state of the steroid 5alpha-reductase type 1 gene in
            the rat hippocampus
  JOURNAL   Mol Cell Endocrinol 412, 330-338 (2015)
   PUBMED   26021641
  REMARK    GeneRIF: Exposure of middle-aged rats to environmental enrichment
            increased mRNA levels of 5al;pha-reductase-1, 3alpha-HSD and
            cytochrome P450 17alpha-hydroxylase/c17,20-lyase and decreased the
            methylation state of the 5alpha-reductase-1 gene
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Livingstone,D.E., Barat,P., Di Rollo,E.M., Rees,G.A., Weldin,B.A.,
            Rog-Zielinska,E.A., MacFarlane,D.P., Walker,B.R. and Andrew,R.
  TITLE     5alpha-Reductase type 1 deficiency or inhibition predisposes to
            insulin resistance, hepatic steatosis, and liver fibrosis in
            rodents
  JOURNAL   Diabetes 64 (2), 447-458 (2015)
   PUBMED   25239636
  REMARK    GeneRIF: The effects of deficiency or inhibition of S5AR1 on the
            risk of liver disease and insulin resistance in male rats and mice
            are reported.
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Castro,B., Sanchez,P., Torres,J.M., Preda,O., del Moral,R.G. and
            Ortega,E.
  TITLE     Bisphenol A exposure during adulthood alters expression of
            aromatase and 5alpha-reductase isozymes in rat prostate
  JOURNAL   PLoS One 8 (2), e55905 (2013)
   PUBMED   23405234
  REMARK    GeneRIF: Low Srd5a1 expression is associated with benign prostatic
            hypertrophy.
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Taylor,M.F., Bhattacharyya,A.K. and Collins,D.C.
  TITLE     Inhibition of rat steroid 5 alpha-reductase (isozyme 1) by suramin
  JOURNAL   Steroids 60 (7), 452-456 (1995)
   PUBMED   7482629
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Eicheler,W., Seitz,J., Steinhoff,M., Forssmann,W.G., Adermann,K.
            and Aumuller,G.
  TITLE     Distribution of rat hepatic steroid 5 alpha-reductase 1 as shown by
            immunohistochemistry
  JOURNAL   Exp Clin Endocrinol Diabetes 103 (2), 105-112 (1995)
   PUBMED   7553073
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Thigpen,A.E. and Russell,D.W.
  TITLE     Four-amino acid segment in steroid 5 alpha-reductase 1 confers
            sensitivity to finasteride, a competitive inhibitor
  JOURNAL   J Biol Chem 267 (12), 8577-8583 (1992)
   PUBMED   1314830
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Andersson,S. and Russell,D.W.
  TITLE     Structural and biochemical properties of cloned and expressed human
            and rat steroid 5 alpha-reductases
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3640-3644 (1990)
   PUBMED   2339109
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Andersson,S., Bishop,R.W. and Russell,D.W.
  TITLE     Expression cloning and regulation of steroid 5 alpha-reductase, an
            enzyme essential for male sexual differentiation
  JOURNAL   J Biol Chem 264 (27), 16249-16255 (1989)
   PUBMED   2476440
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CO394005.1, J05035.1, CV112588.1 and BC088303.1.
            
            On Oct 9, 2005 this sequence version replaced NP_058766.1.
            
            Sequence Note: This sequence has been modified as follows: removed
            22 bp suspected to be vector contamination from the 3' end.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J05035.1, BC127454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..255
                     /product="3-oxo-5-alpha-steroid 4-dehydrogenase 1"
                     /EC_number="1.3.1.22"
                     /note="SR type 1; steroid-5-alpha-reductase, alpha
                     polypeptide 1 (3-oxo-5 alpha-steroid delta 4-dehydrogenase
                     alpha 1); steroid 5-alpha-reductase"
                     /calculated_mol_wt=29208
     Region          106..255
                     /region_name="Steroid_dh"
                     /note="3-oxo-5-alpha-steroid 4-dehydrogenase; pfam02544"
                     /db_xref="CDD:460585"
     CDS             1..255
                     /gene="Srd5a1"
                     /gene_synonym="S5AR 1"
                     /coded_by="NM_017070.3:157..924"
                     /db_xref="GeneID:24950"
                     /db_xref="RGD:3757"
ORIGIN      
        1 meldelclld mlvylegfma fvsivglrsv gspygryspq wpgirvparp awfiqelpsm
       61 awplyeyirp aaarlgnlpn rvllamflih yvqrtlvfpv lirggkptll vtfvlaflfc
      121 tfngyvqsry lsqfavyaed wvthpcfltg falwlvgmvi nihsdhilrn lrkpgetgyk
      181 iprgglfeyv saanyfgelv ewcgfalasw slqgvvfalf tlstlltrak qhhqwyhekf
      241 edypksrkil ipfvl
//
LOCUS       NP_001013258              85 aa            linear   ROD 28-APR-2025
DEFINITION  anaphase-promoting complex subunit CDC26 [Rattus norvegicus].
ACCESSION   NP_001013258 XP_345541
VERSION     NP_001013258.1
DBSOURCE    REFSEQ: accession NM_001013240.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Jin,L., Williamson,A., Banerjee,S., Philipp,I. and Rape,M.
  TITLE     Mechanism of ubiquitin-chain formation by the human
            anaphase-promoting complex
  JOURNAL   Cell 133 (4), 653-665 (2008)
   PUBMED   18485873
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Dube,P., Herzog,F., Gieffers,C., Sander,B., Riedel,D., Muller,S.A.,
            Engel,A., Peters,J.M. and Stark,H.
  TITLE     Localization of the coactivator Cdh1 and the cullin subunit Apc2 in
            a cryo-electron microscopy model of vertebrate APC/C
  JOURNAL   Mol Cell 20 (6), 867-879 (2005)
   PUBMED   16364912
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Gmachl,M., Gieffers,C., Podtelejnikov,A.V., Mann,M. and Peters,J.M.
  TITLE     The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are
            sufficient to ubiquitinate substrates of the anaphase-promoting
            complex
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8973-8978 (2000)
   PUBMED   10922056
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM103539.1 and BC086343.1.
            
            On Apr 20, 2005 this sequence version replaced XP_345541.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC086343.1, EV774948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840105, SAMN12840109
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..85
                     /product="anaphase-promoting complex subunit CDC26"
                     /calculated_mol_wt=9671
     Region          1..64
                     /region_name="ANAPC_CDC26"
                     /note="Anaphase-promoting complex APC subunit CDC26;
                     pfam10471"
                     /db_xref="CDD:402205"
     Region          26..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YDN7.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6YDN7.1)"
     CDS             1..85
                     /gene="Cdc26"
                     /gene_synonym="BWK-2"
                     /coded_by="NM_001013240.2:267..524"
                     /db_xref="GeneID:366381"
                     /db_xref="RGD:1311342"
ORIGIN      
        1 mlrrkptrle lklddieefe nirkdleark kqkedvegvg tsdgegaagl ssdpksreqm
       61 indrigykpq lktnnrtsqf gnfef
//
LOCUS       NP_001019526             229 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain-containing protein 134 precursor [Rattus
            norvegicus].
ACCESSION   NP_001019526 XP_576315
VERSION     NP_001019526.1
DBSOURCE    REFSEQ: accession NM_001024355.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Yu,B., Zhang,T., Xia,P., Gong,X., Qiu,X. and Huang,J.
  TITLE     CCDC134 serves a crucial role in embryonic development
  JOURNAL   Int J Mol Med 41 (1), 381-390 (2018)
   PUBMED   29115376
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088206.1.
            
            On May 27, 2005 this sequence version replaced XP_576315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088206.1, SRR8487227.101274.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..229
                     /product="coiled-coil domain-containing protein 134
                     precursor"
                     /note="coiled-coil domain-containing protein 134"
                     /calculated_mol_wt=24091
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2364
     mat_peptide     23..229
                     /product="Coiled-coil domain-containing protein 134.
                     /id=PRO_0000254111"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M862.1)"
                     /calculated_mol_wt=24091
     Region          23..198
                     /region_name="ERK-JNK_inhib"
                     /note="ERK and JNK pathways, inhibitor; pfam15002"
                     /db_xref="CDD:464435"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5M862.1)"
     Region          191..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M862.1)"
     Region          226..229
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000250|UniProtKB:Q9H6E4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M862.1)"
     CDS             1..229
                     /gene="Ccdc134"
                     /coded_by="NM_001024355.1:209..898"
                     /db_xref="GeneID:500909"
                     /db_xref="RGD:1559657"
ORIGIN      
        1 mdllqslavf fvlllpgtev tgtlkstldp slkiykkmfe vkrreqllal knlaqlndih
       61 qqykildvml kglfkvleds rtvliaadvl pdgplpqdek lkdafshvve ntaffgdvvl
      121 rfpkivhhyf dhnsnwnlli rwgisfcnqt gvfdqgphsp vlslmaqelg itekdsdfqn
      181 pftidrtefi pstdpfqkal reeekrrkke ekrkeirkgp risrsqsel
//
LOCUS       NP_058899                405 aa            linear   ROD 28-APR-2025
DEFINITION  growth/differentiation factor 11 precursor [Rattus norvegicus].
ACCESSION   NP_058899 XP_001071574 XP_343149
VERSION     NP_058899.1
DBSOURCE    REFSEQ: accession NM_017203.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wang,B., Chen,S.M., Yang,S.Q., Jiang,J.M., Zhang,P., Zou,W. and
            Tang,X.Q.
  TITLE     GDF11 mediates H2S to prevent chronic stress-induced cognitive
            impairment by reducing hippocampal NLRP3/caspase-1-dependent
            pyroptosis
  JOURNAL   J Affect Disord 344, 600-611 (2024)
   PUBMED   37827256
  REMARK    GeneRIF: GDF11 mediates H2S to prevent chronic stress-induced
            cognitive impairment by reducing hippocampal
            NLRP3/caspase-1-dependent pyroptosis.
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,Y., Bai,P., Lu,J., Lui,K.H.W., Zhao,T., Wen,D., He,B. and
            Zhu,Z.
  TITLE     Effect of growth differentiation factor 11 expression after
            peripheral nerve injury in Sprague-Dawley rats
  JOURNAL   Neurol Res 45 (9), 835-842 (2023)
   PUBMED   37220327
  REMARK    GeneRIF: Effect of growth differentiation factor 11 expression
            after peripheral nerve injury in Sprague-Dawley rats.
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Wang,H., Zhang,Y., Liu,H. and Li,S.
  TITLE     GDF11, a target of miR-32-5p, suppresses high-glucose-induced
            mitochondrial dysfunction and apoptosis in HK-2 cells through
            PI3K/AKT signaling activation
  JOURNAL   Int Urol Nephrol 55 (7), 1767-1778 (2023)
   PUBMED   36749472
  REMARK    GeneRIF: GDF11, a target of miR-32-5p, suppresses
            high-glucose-induced mitochondrial dysfunction and apoptosis in
            HK-2 cells through PI3K/AKT signaling activation.
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Wang,Z., Jiang,P., Liu,F., Du,X., Ma,L., Ye,S., Cao,H., Sun,P.,
            Su,N., Lin,F., Zhang,R. and Li,C.
  TITLE     GDF11 Regulates PC12 Neural Stem Cells via ALK5-Dependent PI3K-Akt
            Signaling Pathway
  JOURNAL   Int J Mol Sci 23 (20), 12279 (2022)
   PUBMED   36293138
  REMARK    GeneRIF: GDF11 Regulates PC12 Neural Stem Cells via ALK5-Dependent
            PI3K-Akt Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Duan,F., Wang,X., Wang,H., Wang,Y., Zhang,Y., Chen,J., Zhu,X. and
            Chen,B.
  TITLE     GDF11 ameliorates severe acute pancreatitis through modulating
            macrophage M1 and M2 polarization by targeting the TGFbetaR1/SMAD-2
            pathway
  JOURNAL   Int Immunopharmacol 108, 108777 (2022)
   PUBMED   35461108
  REMARK    GeneRIF: GDF11 ameliorates severe acute pancreatitis through
            modulating macrophage M1 and M2 polarization by targeting the
            TGFbetaR1/SMAD-2 pathway.
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Kim,J., Wu,H.H., Lander,A.D., Lyons,K.M., Matzuk,M.M. and
            Calof,A.L.
  TITLE     GDF11 controls the timing of progenitor cell competence in
            developing retina
  JOURNAL   Science 308 (5730), 1927-1930 (2005)
   PUBMED   15976303
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Harmon,E.B., Apelqvist,A.A., Smart,N.G., Gu,X., Osborne,D.H. and
            Kim,S.K.
  TITLE     GDF11 modulates NGN3+ islet progenitor cell number and promotes
            beta-cell differentiation in pancreas development
  JOURNAL   Development 131 (24), 6163-6174 (2004)
   PUBMED   15548585
REFERENCE   8  (residues 1 to 405)
  AUTHORS   Esquela,A.F. and Lee,S.J.
  TITLE     Regulation of metanephric kidney development by
            growth/differentiation factor 11
  JOURNAL   Dev Biol 257 (2), 356-370 (2003)
   PUBMED   12729564
REFERENCE   9  (residues 1 to 405)
  AUTHORS   McPherron,A.C., Lawler,A.M. and Lee,S.J.
  TITLE     Regulation of anterior/posterior patterning of the axial skeleton
            by growth/differentiation factor 11
  JOURNAL   Nat Genet 22 (3), 260-264 (1999)
   PUBMED   10391213
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Nakashima,M., Toyono,T., Akamine,A. and Joyner,A.
  TITLE     Expression of growth/differentiation factor 11, a new member of the
            BMP/TGFbeta superfamily during mouse embryogenesis
  JOURNAL   Mech Dev 80 (2), 185-189 (1999)
   PUBMED   10072786
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_001071574.1, XP_343149.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.37699.1,
                                           SRR22582416.1634475.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840110 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q11"
     Protein         1..405
                     /product="growth/differentiation factor 11 precursor"
                     /note="GDF-11; bone morphogenetic protein 11"
                     /calculated_mol_wt=42362
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2577
     Region          59..283
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9Z217.2)"
     Site            119..120
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q9Z1W4;
                     propagated from UniProtKB/Swiss-Prot (Q9Z217.2)"
     Site            296
                     /site_type="cleavage"
                     /note="Cleavage, by FURIN.
                     /evidence=ECO:0000250|UniProtKB:O95390; propagated from
                     UniProtKB/Swiss-Prot (Q9Z217.2)"
     mat_peptide     297..405
                     /product="Growth/differentiation factor 11.
                     /id=PRO_0000033991"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z217.2)"
                     /calculated_mol_wt=12457
     Region          299..405
                     /region_name="TGF_beta_GDF8"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in growth/differentiation factor 8 (GDF8) and
                     similar proteins; cd19388"
                     /db_xref="CDD:381658"
     Site            order(299..300,308,310,316,323..327,329,332,334..338,340,
                     345..348,351..353,355..357,359..360,362..364,369,371,375,
                     379..391,394..397,399,405)
                     /site_type="other"
                     /note="polypeptide substrate binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:381658"
     Site            order(316,318,320,323,325,327,334,336..340,348..349,
                     351..353,355..357,360..361,363..367,369..372,375,380,382,
                     394..397,399,405)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381658"
     Site            order(321,326..327,329..332,379,381,383,387..391)
                     /site_type="other"
                     /note="polypeptide substrate binding site 1 [polypeptide
                     binding]"
                     /db_xref="CDD:381658"
     CDS             1..405
                     /gene="Gdf11"
                     /gene_synonym="BMP-11"
                     /coded_by="NM_017203.1:34..1251"
                     /db_xref="GeneID:29454"
                     /db_xref="RGD:2673"
ORIGIN      
        1 mvlaaplllg flllalelrp rgeaaegpaa aaaaaaaaag vggerssrpa psaapepdgc
       61 pvcvwrqhsr elrlesiksq ilsklrlkea pnisrevvkq llpkapplqq ildlhdfqgd
      121 alqpedflee deyhattetv ismaqetdpa vqtdgsplcc hfhfspkvmf tkvlkaqlwv
      181 ylrpvprpat vylqilrlkp ltgegtaggg gggrrhirir slkielhsrs ghwqsidfkq
      241 vlhswfrqpq snwgieinaf dpsgtdlavt slgpgaeglh pfmelrvlen tkrsrrnlgl
      301 dcdehssesr ccrypltvdf eafgwdwiia pkrykanycs gqceymfmqk yphthlvqqa
      361 nprgsagpcc tptkmspinm lyfndkqqii ygkipgmvvd rcgcs
//
LOCUS       NP_037213               1055 aa            linear   ROD 28-APR-2025
DEFINITION  focal adhesion kinase 1 [Rattus norvegicus].
ACCESSION   NP_037213
VERSION     NP_037213.1
DBSOURCE    REFSEQ: accession NM_013081.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   de Oliveira Neves,V.G., Blascke de Mello,M.M., Rodrigues,D.,
            Pernomian,L., de Oliveira,I.S., Parente,J.M., Arantes,E.C.,
            Tostes,R.C. and Castro,M.M.
  TITLE     Type I collagen proteolysis by matrix metalloproteinase-2
            contributes to focal adhesion kinase activation and vascular smooth
            muscle cell proliferation in the aorta in early hypertension
  JOURNAL   Vascul Pharmacol 152, 107211 (2023)
   PUBMED   37607602
  REMARK    GeneRIF: Type I collagen proteolysis by matrix metalloproteinase-2
            contributes to focal adhesion kinase activation and vascular smooth
            muscle cell proliferation in the aorta in early hypertension.
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Chen,B., Wu,P., Liang,L., Zhao,C., Wang,Z., He,L., Zhang,R. and
            Xu,N.
  TITLE     Inhibited effect of an RGD peptide hydrogel on the expression of
            beta1-integrin, FAK, and Akt in Tenon's capsule fibroblasts
  JOURNAL   J Biomed Mater Res B Appl Biomater 109 (11), 1857-1865 (2021)
   PUBMED   33847460
  REMARK    GeneRIF: Inhibited effect of an RGD peptide hydrogel on the
            expression of beta1-integrin, FAK, and Akt in Tenon's capsule
            fibroblasts.
REFERENCE   3  (residues 1 to 1055)
  AUTHORS   Shangguan,Y., Wu,Z., Xie,X., Zhou,S., He,H., Xiao,H., Liu,L.,
            Zhu,J., Chen,H., Han,H., Wang,H. and Chen,L.
  TITLE     Low-activity programming of the PDGFRbeta/FAK pathway mediates
            H-type vessel dysplasia and high susceptibility to osteoporosis in
            female offspring rats after prenatal dexamethasone exposure
  JOURNAL   Biochem Pharmacol 185, 114414 (2021)
   PUBMED   33434537
  REMARK    GeneRIF: Low-activity programming of the PDGFRbeta/FAK pathway
            mediates H-type vessel dysplasia and high susceptibility to
            osteoporosis in female offspring rats after prenatal dexamethasone
            exposure.
REFERENCE   4  (residues 1 to 1055)
  AUTHORS   Garcia-Keller,C., Scofield,M.D., Neuhofer,D., Varanasi,S.,
            Reeves,M.T., Hughes,B., Anderson,E., Richie,C.T., Mejias-Aponte,C.,
            Pickel,J., Hope,B.T., Harvey,B.K., Cowan,C.W. and Kalivas,P.W.
  TITLE     Relapse-Associated Transient Synaptic Potentiation Requires
            Integrin-Mediated Activation of Focal Adhesion Kinase and Cofilin
            in D1-Expressing Neurons
  JOURNAL   J Neurosci 40 (44), 8463-8477 (2020)
   PUBMED   33051346
  REMARK    GeneRIF: Relapse-Associated Transient Synaptic Potentiation
            Requires Integrin-Mediated Activation of Focal Adhesion Kinase and
            Cofilin in D1-Expressing Neurons.
REFERENCE   5  (residues 1 to 1055)
  AUTHORS   Ramaniuk,O., Klimova,Z., Grousl,T. and Vomastek,T.
  TITLE     Quantitative Phase Imaging of Spreading Fibroblasts Identifies the
            Role of Focal Adhesion Kinase in the Stabilization of the Cell Rear
  JOURNAL   Biomolecules 10 (8), 1089 (2020)
   PUBMED   32707896
  REMARK    GeneRIF: Quantitative Phase Imaging of Spreading Fibroblasts
            Identifies the Role of Focal Adhesion Kinase in the Stabilization
            of the Cell Rear.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1055)
  AUTHORS   Judson,P.L., He,X., Cance,W.G. and Van Le,L.
  TITLE     Overexpression of focal adhesion kinase, a protein tyrosine kinase,
            in ovarian carcinoma
  JOURNAL   Cancer 86 (8), 1551-1556 (1999)
   PUBMED   10526262
REFERENCE   7  (residues 1 to 1055)
  AUTHORS   Derkinderen,P., Toutant,M., Burgaya,F., Le Bert,M., Siciliano,J.C.,
            de Franciscis,V., Gelman,M. and Girault,J.A.
  TITLE     Regulation of a neuronal form of focal adhesion kinase by
            anandamide
  JOURNAL   Science 273 (5282), 1719-1722 (1996)
   PUBMED   8781236
REFERENCE   8  (residues 1 to 1055)
  AUTHORS   Burgaya,F. and Girault,J.A.
  TITLE     Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals
            multiple transcripts with different patterns of expression
  JOURNAL   Brain Res Mol Brain Res 37 (1-2), 63-73 (1996)
   PUBMED   8738136
REFERENCE   9  (residues 1 to 1055)
  AUTHORS   Calalb,M.B., Polte,T.R. and Hanks,S.K.
  TITLE     Tyrosine phosphorylation of focal adhesion kinase at sites in the
            catalytic domain regulates kinase activity: a role for Src family
            kinases
  JOURNAL   Mol Cell Biol 15 (2), 954-963 (1995)
   PUBMED   7529876
REFERENCE   10 (residues 1 to 1055)
  AUTHORS   Russell,J.C., Koeslag,D.G., Manickavel,V., Amy,R.M. and
            Dolphin,P.J.
  TITLE     Effects of advancing age and severe food restriction on
            pathological processes in the insulin resistant JCR:LA-corpulent
            rat
  JOURNAL   Diabetes Res 15 (2), 53-62 (1990)
   PUBMED   2132399
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1, AF020777.1, EV773243.1, U43942.1, CB713440.1,
            CA511845.1, CA508631.1 and AI717382.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF020777.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..1055
                     /product="focal adhesion kinase 1"
                     /EC_number="2.7.10.2"
                     /note="FADK 1; pp125FAK; focal adhesion kinase-related
                     nonkinase; PTK2 protein tyrosine kinase 2"
                     /calculated_mol_wt=119586
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35346.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          35..130
                     /region_name="FERM_N_2"
                     /note="FERM N-terminal domain; pfam18038"
                     /db_xref="CDD:436229"
     Region          36..258
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P34152; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          254..364
                     /region_name="FERM_C_FAK1"
                     /note="FERM domain C-lobe of Focal Adhesion Kinase 1 and
                     2; cd13190"
                     /db_xref="CDD:270011"
     Site            order(262,282,284,291)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270011"
     Site            order(296,301..304,341,345,348..349)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270011"
     Site            341..352
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270011"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14500712; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          415..684
                     /region_name="PTKc_FAK"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Focal Adhesion Kinase; cd05056"
                     /db_xref="CDD:133187"
     Site            order(428..432,436,452,454,471,484,499..502,505..506,546,
                     550..551,553,564,581..585,594,628)
                     /site_type="active"
                     /db_xref="CDD:133187"
     Site            order(428..432,436,452,454,471,484,499..502,505..506,
                     550..551,553,564)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133187"
     Site            order(546,550,581..585,594,628)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133187"
     Site            563..587
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133187"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            577
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by RET and SRC.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            order(594..598,632,636,661)
                     /site_type="other"
                     /note="FERM domain interface [polypeptide binding]"
                     /db_xref="CDD:133187"
     Region          685..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35346.1)"
     Region          707..1055
                     /region_name="Interaction with TGFB1I1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35346.1)"
     Site            722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12732587; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:P34152; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          837..923
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35346.1)"
     Site            843
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12732587,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          915..1055
                     /region_name="Interaction with ARHGEF28.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35346.1)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q05397; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     Region          919..1048
                     /region_name="Focal_AT"
                     /note="Focal adhesion targeting region; pfam03623"
                     /db_xref="CDD:460992"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35346.1)"
     CDS             1..1055
                     /gene="Ptk2"
                     /gene_synonym="FAK; FRNK; p125FAK"
                     /coded_by="NM_013081.2:433..3600"
                     /db_xref="GeneID:25614"
                     /db_xref="RGD:3443"
ORIGIN      
        1 maaayldpnl nhtpssstkt hlgtgtersp gamervlkvf hyfessnept twasiirhgd
       61 atdvrgiiqk ivdshkvkhv acygfrlshl rseevhwlhv dmgvssvrek yelahppeew
      121 kyelrirylp kgflnqfted kptlnffyqq vksdymleia dqvdqdialk lgcleirrsy
      181 wemrgnalek ksnyevlekd vglkrffpks lldsvkaktl rkliqqtfrq fanlnreesi
      241 lkffeilspv yrfdkecfkc algsswiisv elaigpeegi syltdkgcnp thladfnqvq
      301 tiqysnsedk drkgmlqlki agapepltvt apsltiaenm adlidgycrl vngatqsfii
      361 rpqkegeral psipklanne kqgmrthavs vsetddyaei ideedtytmp strdyeiqre
      421 rielgrcige gqfgdvhqgv ylspenpala vaiktcknct sdsvrekflq ealtmrqfdh
      481 phivkligvi tenpvwiime lctlgelrsf lqvrkysldl aslilyayql stalaylesk
      541 rfvhrdiaar nvlvssndcv klgdfglsry medstyykas kgklpikwma pesinfrrft
      601 sasdvwmfgv cmweilmhgv kpfqgvknnd vigrienger lpmppncppt lyslmtkcwa
      661 ydpsrrprft elkaqlstil eeekvqqeer mrmesrrqat vswdsggsde appkpsrpgy
      721 psprssegfy pspqhmvqtn hyqisgypgs hgipamagsi ypgqaslldq telwnhrpqe
      781 msmwqpsved saaldlrgmg qvlpphlmee rlirqqqeme edqrwlekee rflkpdvrls
      841 rgsidredgs fqgptgnqhi yqpvgkpdpa appkkpprpg apghlsnlss isspaesyne
      901 gvkpwrlqpq eisppptanl drsndkvyen vtglvkavie msskiqpapp eeyvpmvkev
      961 glalrtllat vdetipilpa sthreiemaq kllnsdlgel iskmklaqqy vmtslqqeyk
     1021 kqmltaahal avdaknlldv idqarlkmlg qtrph
//
LOCUS       NP_001094280             515 aa            linear   ROD 28-APR-2025
DEFINITION  RNA-binding region-containing protein 3 [Rattus norvegicus].
ACCESSION   NP_001094280 XP_001073167
VERSION     NP_001094280.1
DBSOURCE    REFSEQ: accession NM_001100810.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Pessa,H.K., Will,C.L., Meng,X., Schneider,C., Watkins,N.J.,
            Perala,N., Nymark,M., Turunen,J.J., Luhrmann,R. and Frilander,M.J.
  TITLE     Minor spliceosome components are predominantly localized in the
            nucleus
  JOURNAL   Proc Natl Acad Sci U S A 105 (25), 8655-8660 (2008)
   PUBMED   18559850
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166571.1.
            
            On Jun 4, 2008 this sequence version replaced XP_001073167.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166571.1, SRR8487231.186011.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..515
                     /product="RNA-binding region-containing protein 3"
                     /note="RNA-binding protein 40; RNA-binding motif protein
                     40"
                     /calculated_mol_wt=57906
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G055.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G055.2)"
     Region          28..100
                     /region_name="RRM1_RBM40_like"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein 40 (RBM40) and similar proteins; cd12238"
                     /db_xref="CDD:409684"
     Region          107..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G055.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96LT9; propagated from
                     UniProtKB/Swiss-Prot (Q4G055.2)"
     Region          215..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G055.2)"
     Region          337..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G055.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4G055.2)"
     Region          418..500
                     /region_name="RRM2_RBM40_like"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein 40 (RBM40) and similar proteins; cd12239"
                     /db_xref="CDD:409685"
     CDS             1..515
                     /gene="Rnpc3"
                     /coded_by="NM_001100810.1:47..1594"
                     /db_xref="GeneID:691538"
                     /db_xref="RGD:1582776"
ORIGIN      
        1 mavpepsmpl srggpgsasl spprgdrtll vrhlpaelta eekedllkyf gaqsvrvlsd
       61 kgrlkhtafa tfpnekaaik altrlhqlkl lghtlvvefa keqdrvhssc pasnaekkkr
      121 lddtvendke kkepdvltve ngiapnhglt fplnsclkym ypppsstila nivnalasvp
      181 kfyvqvlhlm nkmnlptpfg pitarppmye dyvqlhaplp ptspqppeep plpdededls
      241 skeseyessd eedrqrmnkl melanfqpkr pktvkprhvr kkrkikdmlt vpspasqslh
      301 pvllpsdvfd qpqpvgnkki efnistnvpa alnkdleteq nneeknsdsp dtglddsntg
      361 fgklfpkpnv niteeikeds dempsqfisr relekgrisr eemetlsvfr syepgepncr
      421 iyvknlarhv qekdlkfifg ryvdfssetq rimfdirlmk egrmkgqafv glpnekaaak
      481 alkeangyvl fgkpmvvqfa rsarpkhdsk egkrk
//
LOCUS       NP_446114                527 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-L1 [Rattus norvegicus].
ACCESSION   NP_446114
VERSION     NP_446114.1
DBSOURCE    REFSEQ: accession NM_053662.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Herrmann,A., Fleischer,K., Czajkowska,H., Muller-Newen,G. and
            Becker,W.
  TITLE     Characterization of cyclin L1 as an immobile component of the
            splicing factor compartment
  JOURNAL   FASEB J 21 (12), 3142-3152 (2007)
   PUBMED   17494991
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Chen,H.H., Wang,Y.C. and Fann,M.J.
  TITLE     Identification and characterization of the CDK12/cyclin L1 complex
            involved in alternative splicing regulation
  JOURNAL   Mol Cell Biol 26 (7), 2736-2745 (2006)
   PUBMED   16537916
  REMARK    GeneRIF: CDK12 and cyclin L1/L2 are cyclin-dependent kinase and
            cyclin partners and regulate alternative splicing.
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Sgambato,V., Minassian,R., Nairn,A.C. and Hyman,S.E.
  TITLE     Regulation of ania-6 splice variants by distinct signaling pathways
            in striatal neurons
  JOURNAL   J Neurochem 86 (1), 153-164 (2003)
   PUBMED   12807435
  REMARK    GeneRIF: Ania-6 transcription is mostly regulated via cAMP response
            element binding protein (CREB), but that signaling pathways that
            converge on CREB at the transcriptional level produce different
            effects on splicing and neuronal gene expression
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Berke,J.D., Sgambato,V., Zhu,P.P., Lavoie,B., Vincent,M., Krause,M.
            and Hyman,S.E.
  TITLE     Dopamine and glutamate induce distinct striatal splice forms of
            Ania-6, an RNA polymerase II-associated cyclin
  JOURNAL   Neuron 32 (2), 277-287 (2001)
   PUBMED   11683997
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Berke,J.D., Paletzki,R.F., Aronson,G.J., Hyman,S.E. and Gerfen,C.R.
  TITLE     A complex program of striatal gene expression induced by
            dopaminergic stimulation
  JOURNAL   J Neurosci 18 (14), 5301-5310 (1998)
   PUBMED   9651213
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF030091.3 and CB608234.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF030091.3, BC161817.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760494 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..527
                     /product="cyclin-L1"
                     /note="cyclin-L; cyclin Ania-6a; cyclin-L1-like"
                     /calculated_mol_wt=59660
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Region          41..196
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          89..191
                     /region_name="Cyclin-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Region          200..322
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          204..288
                     /region_name="Cyclin-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK58; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Region          327..527
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK58; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK58; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Region          391..433
                     /region_name="RS"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UK58; propagated from
                     UniProtKB/Swiss-Prot (Q9R1Q2.1)"
     CDS             1..527
                     /gene="Ccnl1"
                     /gene_synonym="Ania-6a; Ccnl"
                     /coded_by="NM_053662.3:90..1673"
                     /db_xref="GeneID:114121"
                     /db_xref="RGD:620864"
ORIGIN      
        1 masgphptst aaaasassaa psaggsssgt ttttttttgg iligdrlyse vsltidhsvi
       61 peerlsptps mqdgldlpse tdlrilgcel iqaagillrl pqvamatgqv lfhrffysks
      121 fvkhsfeiva macinlaski eeaprrirdv invfhhlrql rgkrtpspli ldqnyintkn
      181 qvikaerrvl kelgfcvhvk hphkiivmyl qvlecernqt lvqtawnymn dslrtnvfvr
      241 fqpetiacac iylaaralqi plptrphwfl lfgtteeeiq eicietlrly trkkpnyell
      301 ekevekrkva lqeaklkakg lnldgtpals tlggfspask pssprevkae ekspvsinvk
      361 tvkkepedrq qaskspyngv rkdskrsrns rsasrsrsrt rsrsrshtpr rhynnrrsrs
      421 gtyssrsrsr srshsesprr hhnhgsphlk akhtredlks snrhghkrkk srsrsqsktr
      481 dhsdvtkkhr herghhrdrr ersrsfersh kgkhhggsrs ghgrhrr
//
LOCUS       NP_543183                951 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 1 [Rattus
            norvegicus].
ACCESSION   NP_543183
VERSION     NP_543183.1
DBSOURCE    REFSEQ: accession NM_080907.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Wada,T., Miyata,T., Inagi,R., Nangaku,M., Wagatsuma,M., Suzuki,D.,
            Wadzinski,B.E., Okubo,K. and Kurokawa,K.
  TITLE     Cloning and characterization of a novel subunit of protein
            serine/threonine phosphatase 4 from mesangial cells
  JOURNAL   J Am Soc Nephrol 12 (12), 2601-2608 (2001)
   PUBMED   11729228
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061726.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061726.1, AF332004.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q37"
     Protein         1..951
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 1"
                     /calculated_mol_wt=105485
     Region          26..63
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          48..76
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          82..119
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          87..115
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          127..164
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          133..157
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(149..150,153,156..157,191..192,195,198..199,202,
                     231..232,235,238..239,242,270..271,274,277..278,309..310,
                     313,316)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          168..206
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          173..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..246
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          212..243
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          248..285
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          252..278
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          287..324
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          289..316
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          326..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          <358..532
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          407..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          450..>475
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     Region          502..539
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          539..569
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          592..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Site            order(644..645,648,651..652,682..683,686,689..690,693,
                     720..721,724,727..728,731,761..762,765,768..769,800..801,
                     804,807..808)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          665..693
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          699..735
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          703..732
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          741..769
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          777..815
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          780..809
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          820..858
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Region          862..899
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8VI02.1)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TF05; propagated from
                     UniProtKB/Swiss-Prot (Q8VI02.1)"
     CDS             1..951
                     /gene="Ppp4r1"
                     /gene_synonym="Pp4r1"
                     /coded_by="NM_080907.2:89..2944"
                     /db_xref="GeneID:140943"
                     /db_xref="RGD:619798"
ORIGIN      
        1 madlsllqed lpedadglgv ddyssesdvi iipsaldfvs qdemltplgr ldkyaasenv
       61 fnrqmvarsl ldtlrevcge erdciavler isrladdsep tvraelmeqv phialfcqen
      121 rpsipyafsk yllpivvryl adqnnqvrkt sqaallalle qelierldve tkvcpvlidl
      181 tapdsnddvk teavaimckm apmvgkdite rlilprfcem ccdcrmfhvr kvcaanfgdi
      241 csvvgqqate emllprffql csdnvwgvrk acaecfmavs catcqeirrt klsalfinli
      301 sdpsrwvrqa afqslgpfis tfanpsssgq cfkdesksse dkdrirddgv vqeeqsrped
      361 apsdlsaphs sarldgtleg caaetpgdsa gdmrvpadss llctlssesp qeaasdaesg
      421 kkhdnnsksa srpdvgtssp eptpldqemf nsfhfwrtpl pqidldkelq qdpgerpspe
      481 rtgdapaapv pgspsitmat rkeleemien lephmddpdv kaqvevlsaa lrastldahd
      541 eaggaeqrse lqddavgagg elpncsised tseplviaae enmeatpdyi hggadvgpgg
      601 gggfspdeer rpkvqdvvpq alldqylsmt dpsraqtvdt eiakhcaysl pgvaltlgrq
      661 nwhclretye tlasdmqwkv rrtlafsihe lavilgdqlt aadlvpifng flkdldevri
      721 gvlkhlhdfl kllhidkrre ylyqlqeflv tdnsrnwrfr aelaeqlill lelysprdvy
      781 dylrpialnl cadkvssvrw isyklvsemv kklhmatppt fgvelinelv enfgrcpkws
      841 grqafvfvcq tvieddclpm dqfavhlmph lltlandrvp nvrvllaktl rqtllekeyf
      901 lasaschqea veqtimalqm drdsdvkyfa sihpsstkls edamstasst y
//
LOCUS       NP_599182                412 aa            linear   ROD 28-APR-2025
DEFINITION  POU domain, class 4, transcription factor 2 [Rattus norvegicus].
ACCESSION   NP_599182 XP_001074669 XP_344757
VERSION     NP_599182.1
DBSOURCE    REFSEQ: accession NM_134355.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Mele,L., Maskell,L.J., Stuckey,D.J., Clark,J.E., Heads,R.J. and
            Budhram-Mahadeo,V.S.
  TITLE     The POU4F2/Brn-3b transcription factor is required for the
            hypertrophic response to angiotensin II in the heart
  JOURNAL   Cell Death Dis 10 (8), 621 (2019)
   PUBMED   31413277
  REMARK    GeneRIF: hearts from male Brn-3b KO mutant mice display contractile
            dysfunction at baseline but also attenuated hypertrophic responses
            to AngII treatment. Hearts from AngII-treated male Brn-3b KO mice
            develop further contractile dysfunction linked to extensive
            fibrosis/remodelling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Maskell,L.J., Qamar,K., Babakr,A.A., Hawkins,T.A., Heads,R.J. and
            Budhram-Mahadeo,V.S.
  TITLE     Essential but partially redundant roles for POU4F1/Brn-3a and
            POU4F2/Brn-3b transcription factors in the developing heart
  JOURNAL   Cell Death Dis 8 (6), e2861 (2017)
   PUBMED   28594399
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Bitsi,S., Ali,H., Maskell,L., Ounzain,S., Mohamed-Ali,V. and
            Budhram-Mahadeo,V.S.
  TITLE     Profound hyperglycemia in knockout mutant mice identifies novel
            function for POU4F2/Brn-3b in regulating metabolic processes
  JOURNAL   Am J Physiol Endocrinol Metab 310 (5), E303-E312 (2016)
   PUBMED   26670484
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Phatak,N.R., Stankowska,D.L. and Krishnamoorthy,R.R.
  TITLE     Transcription Factor Brn-3b Overexpression Enhances Neurite
            Outgrowth in PC12 Cells Under Condition of Hypoxia
  JOURNAL   Cell Mol Neurobiol 35 (6), 769-783 (2015)
   PUBMED   25786379
  REMARK    GeneRIF: A potential role for Brn-3b in neurodegenerative diseases
            in which hypoxia/ischemia contribute to pathophysiology of the
            disease.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Wu,F., Kaczynski,T.J., Sethuramanujam,S., Li,R., Jain,V.,
            Slaughter,M. and Mu,X.
  TITLE     Two transcription factors, Pou4f2 and Isl1, are sufficient to
            specify the retinal ganglion cell fate
  JOURNAL   Proc Natl Acad Sci U S A 112 (13), E1559-E1568 (2015)
   PUBMED   25775587
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Xiang,M., Zhou,L., Macke,J.P., Yoshioka,T., Hendry,S.H., Eddy,R.L.,
            Shows,T.B. and Nathans,J.
  TITLE     The Brn-3 family of POU-domain factors: primary structure, binding
            specificity, and expression in subsets of retinal ganglion cells
            and somatosensory neurons
  JOURNAL   J Neurosci 15 (7 Pt 1), 4762-4785 (1995)
   PUBMED   7623109
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Morris,P.J., Theil,T., Ring,C.J., Lillycrop,K.A., Moroy,T. and
            Latchman,D.S.
  TITLE     The opposite and antagonistic effects of the closely related POU
            family transcription factors Brn-3a and Brn-3b on the activity of a
            target promoter are dependent on differences in the POU domain
  JOURNAL   Mol Cell Biol 14 (10), 6907-6914 (1994)
   PUBMED   7935408
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Turner,E.E., Jenne,K.J. and Rosenfeld,M.G.
  TITLE     Brn-3.2: a Brn-3-related transcription factor with distinctive
            central nervous system expression and regulation by retinoic acid
  JOURNAL   Neuron 12 (1), 205-218 (1994)
   PUBMED   7904822
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Theil,T., McLean-Hunter,S., Zornig,M. and Moroy,T.
  TITLE     Mouse Brn-3 family of POU transcription factors: a new
            aminoterminal domain is crucial for the oncogenic activity of
            Brn-3a
  JOURNAL   Nucleic Acids Res 21 (25), 5921-5929 (1993)
   PUBMED   8290353
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Xiang,M., Zhou,L., Peng,Y.W., Eddy,R.L., Shows,T.B. and Nathans,J.
  TITLE     Brn-3b: a POU domain gene expressed in a subset of retinal ganglion
            cells
  JOURNAL   Neuron 11 (4), 689-701 (1993)
   PUBMED   7691107
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On or before Dec 20, 2009 this sequence version replaced
            XP_001074669.1, XP_344757.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN12840115,
                              SAMN13663594 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..412
                     /product="POU domain, class 4, transcription factor 2"
                     /note="brain-3B; brain-specific homeobox/POU domain
                     protein 3B"
                     /calculated_mol_wt=43099
     Region          29..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          94..240
                     /region_name="Required for transcriptional activation.
                     /evidence=ECO:0000250|UniProtKB:Q63934"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          113..122
                     /region_name="POU-IV box"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          123..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          174..188
                     /region_name="Nuclear speckle targeting signal.
                     /evidence=ECO:0000250|UniProtKB:Q12837"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          <201..>289
                     /region_name="ACR_tran"
                     /note="AcrB/AcrD/AcrF family; cl47191"
                     /db_xref="CDD:481531"
     Region          241..412
                     /region_name="Required for DNA-binding and transcriptional
                     repression. /evidence=ECO:0000250|UniProtKB:Q63934"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V7L5.1)"
     Region          253..330
                     /region_name="POU"
                     /note="Found in Pit-Oct-Unc transcription factors;
                     smart00352"
                     /db_xref="CDD:197673"
     Region          349..405
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..412
                     /gene="Pou4f2"
                     /gene_synonym="Brn-3.2; Brn-3B; Brn3b"
                     /coded_by="NM_134355.1:241..1479"
                     /db_xref="GeneID:171355"
                     /db_xref="RGD:620075"
ORIGIN      
        1 mmmmslnskq afsmphagsl hvepkysalh saspgssapa apsasspsss snagsggggg
       61 gggggggggr sssssssgsg ggggggseam rraclptpps nifggldesl laraealaav
      121 divsqskshh hhpphhspfk pdatyhtmnt ipctsaasss svpishpsal agthhhhhhh
      181 hhhhhqphqa legellehls pglalgamag pdgtvvstpa haphmatmnp mhqaalsmah
      241 ahglpshmgc msdvdadprd leafaerfkq rriklgvtqa dvgsalanlk ipgvgslsqs
      301 ticrfesltl shnnmialkp ilqawleeae kshrekltkp elfngaekkr krtsiaapek
      361 rsleayfaiq prpssekiaa iaekldlkkn vvrvwfcnqr qkqkrmkysa gi
//
LOCUS       NP_001253983              85 aa            linear   ROD 28-APR-2025
DEFINITION  anaphase-promoting complex subunit CDC26 [Rattus norvegicus].
ACCESSION   NP_001253983
VERSION     NP_001253983.1
DBSOURCE    REFSEQ: accession NM_001267054.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Jin,L., Williamson,A., Banerjee,S., Philipp,I. and Rape,M.
  TITLE     Mechanism of ubiquitin-chain formation by the human
            anaphase-promoting complex
  JOURNAL   Cell 133 (4), 653-665 (2008)
   PUBMED   18485873
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Dube,P., Herzog,F., Gieffers,C., Sander,B., Riedel,D., Muller,S.A.,
            Engel,A., Peters,J.M. and Stark,H.
  TITLE     Localization of the coactivator Cdh1 and the cullin subunit Apc2 in
            a cryo-electron microscopy model of vertebrate APC/C
  JOURNAL   Mol Cell 20 (6), 867-879 (2005)
   PUBMED   16364912
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Gmachl,M., Gieffers,C., Podtelejnikov,A.V., Mann,M. and Peters,J.M.
  TITLE     The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are
            sufficient to ubiquitinate substrates of the anaphase-promoting
            complex
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8973-8978 (2000)
   PUBMED   10922056
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.1608234.1,
                                           SRR22399484.365186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840109, SAMN12840111
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..85
                     /product="anaphase-promoting complex subunit CDC26"
                     /calculated_mol_wt=9671
     Region          1..64
                     /region_name="ANAPC_CDC26"
                     /note="Anaphase-promoting complex APC subunit CDC26;
                     pfam10471"
                     /db_xref="CDD:402205"
     Region          26..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YDN7.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6YDN7.1)"
     CDS             1..85
                     /gene="Cdc26"
                     /gene_synonym="BWK-2"
                     /coded_by="NM_001267054.1:195..452"
                     /db_xref="GeneID:366381"
                     /db_xref="RGD:1311342"
ORIGIN      
        1 mlrrkptrle lklddieefe nirkdleark kqkedvegvg tsdgegaagl ssdpksreqm
       61 indrigykpq lktnnrtsqf gnfef
//
LOCUS       NP_001013906             726 aa            linear   ROD 28-APR-2025
DEFINITION  BRCA1-A complex subunit RAP80 [Rattus norvegicus].
ACCESSION   NP_001013906 XP_214427
VERSION     NP_001013906.1
DBSOURCE    REFSEQ: accession NM_001013884.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Panier,S., Ichijima,Y., Fradet-Turcotte,A., Leung,C.C., Kaustov,L.,
            Arrowsmith,C.H. and Durocher,D.
  TITLE     Tandem protein interaction modules organize the ubiquitin-dependent
            response to DNA double-strand breaks
  JOURNAL   Mol Cell 47 (3), 383-395 (2012)
   PUBMED   22742833
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Wang,B., Hurov,K., Hofmann,K. and Elledge,S.J.
  TITLE     NBA1, a new player in the Brca1 A complex, is required for DNA
            damage resistance and checkpoint control
  JOURNAL   Genes Dev 23 (6), 729-739 (2009)
   PUBMED   19261749
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Feng,L., Huang,J. and Chen,J.
  TITLE     MERIT40 facilitates BRCA1 localization and DNA damage repair
  JOURNAL   Genes Dev 23 (6), 719-728 (2009)
   PUBMED   19261748
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Shao,G., Patterson-Fortin,J., Messick,T.E., Feng,D., Shanbhag,N.,
            Wang,Y. and Greenberg,R.A.
  TITLE     MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to
            DNA double-strand breaks
  JOURNAL   Genes Dev 23 (6), 740-754 (2009)
   PUBMED   19261746
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Shao,G., Lilli,D.R., Patterson-Fortin,J., Coleman,K.A.,
            Morrissey,D.E. and Greenberg,R.A.
  TITLE     The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes
            RNF8-Ubc13-dependent ubiquitination events at DNA double strand
            breaks
  JOURNAL   Proc Natl Acad Sci U S A 106 (9), 3166-3171 (2009)
   PUBMED   19202061
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Kim,H., Chen,J. and Yu,X.
  TITLE     Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage
            response
  JOURNAL   Science 316 (5828), 1202-1205 (2007)
   PUBMED   17525342
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Sobhian,B., Shao,G., Lilli,D.R., Culhane,A.C., Moreau,L.A., Xia,B.,
            Livingston,D.M. and Greenberg,R.A.
  TITLE     RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage
            sites
  JOURNAL   Science 316 (5828), 1198-1202 (2007)
   PUBMED   17525341
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Wang,B., Matsuoka,S., Ballif,B.A., Zhang,D., Smogorzewska,A.,
            Gygi,S.P. and Elledge,S.J.
  TITLE     Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
            damage response
  JOURNAL   Science 316 (5828), 1194-1198 (2007)
   PUBMED   17525340
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Yan,Z., Kim,Y.S. and Jetten,A.M.
  TITLE     RAP80, a novel nuclear protein that interacts with the
            retinoid-related testis-associated receptor
  JOURNAL   J Biol Chem 277 (35), 32379-32388 (2002)
   PUBMED   12080054
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Seol,W., Choi,H.S. and Moore,D.D.
  TITLE     Isolation of proteins that interact specifically with the retinoid
            X receptor: two novel orphan receptors
  JOURNAL   Mol Endocrinol 9 (1), 72-85 (1995)
   PUBMED   7760852
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087149.1.
            
            On Apr 20, 2005 this sequence version replaced XP_214427.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087149.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..726
                     /product="BRCA1-A complex subunit RAP80"
                     /note="receptor-associated protein 80; ubiquitin
                     interaction motif-containing protein 1"
                     /calculated_mol_wt=80250
     Region          1..101
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          47..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5U5Q9; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          60..78
                     /region_name="LR motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          72..128
                     /region_name="RAP80_UIM"
                     /note="RAP80 N-terminal ubiquitin interaction motif;
                     pfam18282"
                     /db_xref="CDD:436382"
     Region          93..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          97..103
                     /region_name="UIM-linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          100..200
                     /region_name="Necessary for interaction with NR6A1
                     N-terminus. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          119..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          270..400
                     /region_name="AIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          272..330
                     /region_name="AIR_RAP80-like"
                     /note="ABRAXAS Interacting Region (AIR) of
                     Receptor-Associated Protein 80 (RAP80), and related
                     domains; cd20912"
                     /db_xref="CDD:411022"
     Site            order(272..278,281..282,299..300,303,306..307,310..311,
                     314)
                     /site_type="other"
                     /note="MERIT40 binding site [polypeptide binding]"
                     /db_xref="CDD:411022"
     Site            order(272..280,282,284..285,287,291..292,294..295,
                     297..299,301..302,305..306,309)
                     /site_type="other"
                     /note="ABRAXAS binding site [polypeptide binding]"
                     /db_xref="CDD:411022"
     Site            order(281..283,289..290,292..293,296..297,300..301,
                     304..305,307..308,311..327)
                     /site_type="other"
                     /note="BRE binding site [polypeptide binding]"
                     /db_xref="CDD:411022"
     Region          356..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          400..507
                     /region_name="Necessary for interaction with NR6A1
                     C-terminus. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          512..589
                     /region_name="Zinc-finger-like region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Region          611..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96RL1; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQK4.1)"
     CDS             1..726
                     /gene="Uimc1"
                     /gene_synonym="RGD1307009"
                     /coded_by="NM_001013884.1:64..2244"
                     /db_xref="GeneID:290997"
                     /db_xref="RGD:1307009"
ORIGIN      
        1 mprrkkkike asegqnlekk dlettssvsi kkkrrledlf ivisdsdgee tkeenglqkm
       61 ktkqsnrskc lakrkiaqms eeeqfalalk mseqeakevn nqeekeeell rkaiaeslns
      121 rwssdasaar prplstgpss hphqdstkds gttegiwqla ppslckgsqi sqgneaeegk
      181 epwdhsenpe eeplsgssgs qdqssrpvfe nekvkcfdrc tghlaehtqc gkpqestgsg
      241 cafpkavqgr gdtsrqclpt padtkglqdi ggtvhyywgv pfcpagvdpd qytsvilcql
      301 evyqkslkma qrqlvkkrgf gepvlprppf liqnecgqee qtsekhegls edvragaree
      361 rqgsgasvwh setkdsqksp itslkqrlll eeepttgrgq ssqglfveet seevlksseg
      421 ddavpasqsi avltskrdlv lmpeasteev tvcpetqlss fepldlnged svdgreipte
      481 lgmtvsnrqv dnreagkdsr ppavsasarv scplcnqdfp ptkieqhamy ctglmepetv
      541 ltrrrreakk ksdgrtaaqp aldisrkekc ylckslvplg eyqchvetcl qlanvdreng
      601 tegmrrprvc apvegkpkqr lrkskekghs qgrllslleq sehrttgver tpkcseagaf
      661 rmpspdveea gcsrerqssl sklnlnespi ksfvpvseat nclvdfkgqf afrsqtksgr
      721 grrrks
//
LOCUS       NP_446076                315 aa            linear   ROD 28-APR-2025
DEFINITION  pituitary homeobox 1 [Rattus norvegicus].
ACCESSION   NP_446076
VERSION     NP_446076.1
DBSOURCE    REFSEQ: accession NM_053624.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Zhao,X. and Yang,X.
  TITLE     Retinoic Acid Promotes Retinoic Acid Signaling by Suppression of
            Pitx1 In Tendon Cells: A Possible Mechanism of a Clubfoot-Like
            Phenotype Induced by Retinoic Acid
  JOURNAL   Med Sci Monit 25, 6980-6989 (2019)
   PUBMED   31527569
  REMARK    GeneRIF: Pitx1 binds to the promoter region of SIRT1 and promotes
            the transcription of SIRT1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Sobrier,M.L., Tsai,Y.C., Perez,C., Leheup,B., Bouceba,T.,
            Duquesnoy,P., Copin,B., Sizova,D., Penzo,A., Stanger,B.Z.,
            Cooke,N.E., Liebhaber,S.A. and Amselem,S.
  TITLE     Functional characterization of a human POU1F1 mutation associated
            with isolated growth hormone deficiency: a novel etiology for IGHD
  JOURNAL   Hum Mol Genet 25 (3), 472-483 (2016)
   PUBMED   26612202
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Simpson,M.T., Venkatesh,I., Callif,B.L., Thiel,L.K., Coley,D.M.,
            Winsor,K.N., Wang,Z., Kramer,A.A., Lerch,J.K. and Blackmore,M.G.
  TITLE     The tumor suppressor HHEX inhibits axon growth when prematurely
            expressed in developing central nervous system neurons
  JOURNAL   Mol Cell Neurosci 68, 272-283 (2015)
   PUBMED   26306672
  REMARK    GeneRIF: This study idnetifed that the PITX1 as inhibitors of
            neurite outgrowth.
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Gajewska,A., Herman,A.P., Wolinska-Witort,E., Kochman,K. and
            Zwierzchowski,L.
  TITLE     In vivo oestrogenic modulation of Egr1 and Pitx1 gene expression in
            female rat pituitary gland
  JOURNAL   J Mol Endocrinol 53 (3), 355-366 (2014)
   PUBMED   25258388
  REMARK    GeneRIF: Orchestrated Egr1 and Pitx1 activities depending on
            specific central and peripheral regulatory inputs could be
            responsible for physiologically variable Lhb gene promoter
            activation in vivo.
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Duboc,V. and Logan,M.P.
  TITLE     Pitx1 is necessary for normal initiation of hindlimb outgrowth
            through regulation of Tbx4 expression and shapes hindlimb
            morphologies via targeted growth control
  JOURNAL   Development 138 (24), 5301-5309 (2011)
   PUBMED   22071103
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Lanctot,C., Moreau,A., Chamberland,M., Tremblay,M.L. and Drouin,J.
  TITLE     Hindlimb patterning and mandible development require the Ptx1 gene
  JOURNAL   Development 126 (9), 1805-1810 (1999)
   PUBMED   10101115
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Szeto,D.P., Rodriguez-Esteban,C., Ryan,A.K., O'Connell,S.M.,
            Liu,F., Kioussi,C., Gleiberman,A.S., Izpisua-Belmonte,J.C. and
            Rosenfeld,M.G.
  TITLE     Role of the Bicoid-related homeodomain factor Pitx1 in specifying
            hindlimb morphogenesis and pituitary development
  JOURNAL   Genes Dev 13 (4), 484-494 (1999)
   PUBMED   10049363
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Potter,M., Wax,J. and Jones,G.M.
  TITLE     Indomethacin is a potent inhibitor of pristane and plastic disc
            induced plasmacytomagenesis in a hypersusceptible BALB/c congenic
            strain
  JOURNAL   Blood 90 (1), 260-269 (1997)
   PUBMED   9207461
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Bach,I., Carriere,C., Ostendorff,H.P., Andersen,B. and
            Rosenfeld,M.G.
  TITLE     A family of LIM domain-associated cofactors confer transcriptional
            synergism between LIM and Otx homeodomain proteins
  JOURNAL   Genes Dev 11 (11), 1370-1380 (1997)
   PUBMED   9192866
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Lamonerie,T., Tremblay,J.J., Lanctot,C., Therrien,M., Gauthier,Y.
            and Drouin,J.
  TITLE     Ptx1, a bicoid-related homeo box transcription factor involved in
            transcription of the pro-opiomelanocortin gene
  JOURNAL   Genes Dev 10 (10), 1284-1295 (1996)
   PUBMED   8675014
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061966.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061966.1, AB047298.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..315
                     /product="pituitary homeobox 1"
                     /note="homeobox protein PITX1; paired-like homeodomain
                     transcription factor 1"
                     /calculated_mol_wt=34076
     Region          1..103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99NA7.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P78337; propagated from
                     UniProtKB/Swiss-Prot (Q99NA7.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P78337; propagated from
                     UniProtKB/Swiss-Prot (Q99NA7.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P78337; propagated from
                     UniProtKB/Swiss-Prot (Q99NA7.1)"
     Region          90..146
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          149..280
                     /region_name="Interaction with PIT-1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99NA7.1)"
     Region          277..294
                     /region_name="OAR"
                     /note="OAR motif; pfam03826"
                     /db_xref="CDD:461067"
     Region          281..294
                     /region_name="OAR.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99NA7.1)"
     Region          287..291
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99NA7.1)"
     CDS             1..315
                     /gene="Pitx1"
                     /gene_synonym="Bft"
                     /coded_by="NM_053624.2:292..1239"
                     /db_xref="GeneID:113983"
                     /db_xref="RGD:69253"
ORIGIN      
        1 mdafkggmsl erlpeglrpp pppphdmgps fhlartadpr eplensases sdadlpdker
       61 ggeakvpedg gagsagcgsa edpakkkkqr rqrthftsqq lqeleatfqr nrypdmsmre
      121 eiavwtnlte prvrvwfknr rakwrkrern qqldlckggy vpqfsglvqp yedvyaaagy
      181 synnwaaksl apaplstksf tffnsmspls sqsmfsapss issmtmpssm gpgsvpgmpn
      241 sglnninnlt gsslnsamsp gacpygtpas pysvyrdtcn sslaslrlks kqhssfgygg
      301 lqgpasglna cqyns
//
LOCUS       NP_062022                845 aa            linear   ROD 28-APR-2025
DEFINITION  matrin-3 [Rattus norvegicus].
ACCESSION   NP_062022 XP_212889
VERSION     NP_062022.2
DBSOURCE    REFSEQ: accession NM_019149.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Ishibashi,O., Hayashi,M., Horikawa,A., Owada,H., Miyamoto,R.,
            Mizukami,N. and Inui,T.
  TITLE     The Role of miR-217-5p in the Puromycin Aminonucleoside-Induced
            Morphological Change of Podocytes
  JOURNAL   Noncoding RNA 8 (3), 43 (2022)
   PUBMED   35736640
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Horikawa,A., Yoneda,T., Yaoita,E., Yamaguchi,K., Shigenobu,S.,
            Kuramochi,M., Yamate,J., Inui,T. and Ishibashi,O.
  TITLE     A novel splicing variant of small nucleolar RNA host gene 4 is a
            podocyte-selective non-coding RNA upregulated in response to
            puromycin aminonucleoside-induced podocyte injury
  JOURNAL   J Biochem 165 (5), 447-454 (2019)
   PUBMED   30597036
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Morchikh,M., Cribier,A., Raffel,R., Amraoui,S., Cau,J., Severac,D.,
            Dubois,E., Schwartz,O., Bennasser,Y. and Benkirane,M.
  TITLE     HEXIM1 and NEAT1 Long Non-coding RNA Form a Multi-subunit Complex
            that Regulates DNA-Mediated Innate Immune Response
  JOURNAL   Mol Cell 67 (3), 387-399 (2017)
   PUBMED   28712728
REFERENCE   4  (residues 1 to 845)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   5  (residues 1 to 845)
  AUTHORS   Cui,W., Dai,X., Marcho,C., Han,Z., Zhang,K., Tremblay,K.D. and
            Mager,J.
  TITLE     Towards Functional Annotation of the Preimplantation Transcriptome:
            An RNAi Screen in Mammalian Embryos
  JOURNAL   Sci Rep 6, 37396 (2016)
   PUBMED   27869233
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 845)
  AUTHORS   Hibino,Y., Tsukada,S. and Sugano,N.
  TITLE     Purification and characterization of a DNA binding protein in a
            nuclear scaffold fraction from rat ascites hepatoma cells
  JOURNAL   Carcinogenesis 18 (4), 707-713 (1997)
   PUBMED   9111204
REFERENCE   7  (residues 1 to 845)
  AUTHORS   Hibino,Y., Tsukada,S. and Sugano,N.
  TITLE     Properties of a DNA-binding protein from rat nuclear scaffold
            fraction
  JOURNAL   Biochem Biophys Res Commun 197 (1), 336-342 (1993)
   PUBMED   8250943
REFERENCE   8  (residues 1 to 845)
  AUTHORS   Hibino,Y., Nakamura,K., Tsukada,S. and Sugano,N.
  TITLE     Purification and characterization of nuclear scaffold proteins
            which bind to a highly repetitive bent DNA from rat liver
  JOURNAL   Biochim Biophys Acta 1174 (2), 162-170 (1993)
   PUBMED   8357833
REFERENCE   9  (residues 1 to 845)
  AUTHORS   Hibino,Y., Nakamura,K., Asano,S. and Sugano,N.
  TITLE     Affinity of a highly repetitive bent DNA for nuclear scaffold
            proteins from rat liver
  JOURNAL   Biochem Biophys Res Commun 184 (2), 853-858 (1992)
   PUBMED   1575753
REFERENCE   10 (residues 1 to 845)
  AUTHORS   Belgrader,P., Dey,R. and Berezney,R.
  TITLE     Molecular cloning of matrin 3. A 125-kilodalton protein of the
            nuclear matrix contains an extensive acidic domain
  JOURNAL   J Biol Chem 266 (15), 9893-9899 (1991)
   PUBMED   2033075
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000018.1.
            
            On Mar 27, 2005 this sequence version replaced NP_062022.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M63485.1, SRR26643429.53788.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p11"
     Protein         1..845
                     /product="matrin-3"
                     /note="nuclear scaffold protein P130/MAT3"
                     /calculated_mol_wt=94371
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          147..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43244.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          187..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43244.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          288..322
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          342..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43244.2)"
     Region          398..473
                     /region_name="RRM1_MATR3"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     matrin-3; cd12714"
                     /db_xref="CDD:410113"
     Region          496..575
                     /region_name="RRM2_MATR3"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     matrin-3; cd12715"
                     /db_xref="CDD:410114"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            522
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            571
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          588..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43244.2)"
     Region          <590..>776
                     /region_name="MDN1"
                     /note="Midasin, AAA ATPase with vWA domain, involved in
                     ribosome maturation [Translation, ribosomal structure and
                     biogenesis]; COG5271"
                     /db_xref="CDD:444083"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            654
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          708..716
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P43244.2)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     Region          796..831
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Site            834
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P43243; propagated from
                     UniProtKB/Swiss-Prot (P43244.2)"
     CDS             1..845
                     /gene="Matr3"
                     /gene_synonym="P130/MAT3; snhg4"
                     /coded_by="NM_019149.3:241..2778"
                     /db_xref="GeneID:29150"
                     /db_xref="RGD:3052"
ORIGIN      
        1 msksfqqssl grdsqghgrd lsaagiglla aatqslsmpa slgrmnqgta rlaslmnlgm
       61 ssslnqqgah salssastss hnlqsifnig srgplplssq hrgdtdqasn ilasfglsar
      121 dldelsrype dkitpenlpq illqlkrrrt eegptlsygr dgrsatrepp yrvprddwee
      181 krhfrrdsfd drgpslnpvl dydhgsrsqe sgyydrmdye ddrlrdgerc rddsffgets
      241 hnyhkfdsey ermgrgpgpl qerslfekkr gappssnied fhgllpkgyp hlcsicdlpv
      301 hsnkewsqhi ngashsrrcq llleiypewn pdndtghtmg dpfmlqqstn papgilgppp
      361 psfhlggpav gprgnlgagn gnlqgprhmq kgrvetsrvv himdfqrgkn lryqllqlve
      421 pfgvisnhli lnkineafie mattedaqaa vdyytttpal vfgkpvrvhl sqkykrikkp
      481 egkpdqkfdq kqelgrvihl snlphsgysd savlklaepy gkiknyilmr mksqafieme
      541 tredamamvd hclkkalwfq grcvkvdlse kykklvlrip nrgidllkkd ksrkrsyspd
      601 gkespsdkks ktdgaqkten paegkeqeek sgedgekdtk ddqteqepsm llesedellv
      661 deeeaaalle sgssvgdetd lanlgdvssd gkkepsdkav kkdasatskk klkkvdkiee
      721 ldqeneaale ngikneente pgaesaenad dpnkdasdns dgqndenked ytipdeyrig
      781 pyqpnvpvgi dyvipktgfy cklcslfytn eevaknthcs slphyqklkk flnklaeerr
      841 qkket
//
LOCUS       NP_001100549             634 aa            linear   ROD 28-APR-2025
DEFINITION  kelch-like protein 22 [Rattus norvegicus].
ACCESSION   NP_001100549 XP_001063385 XP_221268
VERSION     NP_001100549.1
DBSOURCE    REFSEQ: accession NM_001107079.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Chen,J., Ou,Y., Yang,Y., Li,W., Xu,Y., Xie,Y. and Liu,Y.
  TITLE     KLHL22 activates amino-acid-dependent mTORC1 signalling to promote
            tumorigenesis and ageing
  JOURNAL   Nature 557 (7706), 585-589 (2018)
   PUBMED   29769719
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Beck,J., Maerki,S., Posch,M., Metzger,T., Persaud,A., Scheel,H.,
            Hofmann,K., Rotin,D., Pedrioli,P., Swedlow,J.R., Peter,M. and
            Sumara,I.
  TITLE     Ubiquitylation-dependent localization of PLK1 in mitosis
  JOURNAL   Nat Cell Biol 15 (4), 430-439 (2013)
   PUBMED   23455478
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Maerki,S., Olma,M.H., Staubli,T., Steigemann,P., Gerlich,D.W.,
            Quadroni,M., Sumara,I. and Peter,M.
  TITLE     The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
            microtubules in anaphase and is required for cytokinesis
  JOURNAL   J Cell Biol 187 (6), 791-800 (2009)
   PUBMED   19995937
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473999.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_221268.4, XP_001063385.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..634
                     /product="kelch-like protein 22"
                     /note="kelch-like 22"
                     /calculated_mol_wt=71643
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q53GT1; propagated from
                     UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          27..151
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          52..592
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          147..250
                     /region_name="BACK_KLHL22"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 22 (KLHL22); cd18461"
                     /db_xref="CDD:350536"
     Region          294..335
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          299..349
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          340..385
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          350..399
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          389..433
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          400..446
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          436..481
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..493
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          483..531
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          494..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          534..580
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..593
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Region          600..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZC3.1)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q53GT1; propagated from
                     UniProtKB/Swiss-Prot (D3ZZC3.1)"
     CDS             1..634
                     /gene="Klhl22"
                     /gene_synonym="RGD1306288"
                     /coded_by="NM_001107079.1:68..1972"
                     /db_xref="GeneID:303792"
                     /db_xref="RGD:1306288"
ORIGIN      
        1 maeeqdfaql cklstqpshs hcvnntyrst qhsqallrgl lalrdsgilf dvvlvvegrh
       61 ieahrillaa scdyfrgmfa gglkemeqee vlihgvsyna mcqilhfiyt selelslsnv
      121 qetlvaacql qipeiihfcc dflmswvdee nildvyrlae lfdlnrltqq ldtyilknfv
      181 afsrtdkyrq lplekvysll ssnrlevsce tevyegally hysmeqvqad qislheppkl
      241 letvrfplme aevlqrlhdk lgpsplrdtv asalmyhrne slqpslqgph telrsdfqcv
      301 vgfggihstp stilsdqaky lnpllgewkh ftaslaprms nqgiavlnnf vyliggdnnv
      361 qgfraesrcw rydprhnrwf qiqslqqeha dlcvcvvgky iyavagrdyh nnlsaveryd
      421 patnsweyva plkkevyaha gttlqgkmyi tcgrrgedyl kethcydpgs ntwhtladgp
      481 vrrawhgmaa lldklfvigg snndagyrrd vhqvacysct srqwssvcpl paghgepgia
      541 vldnriyvlg grshnrgsrt gyvhiydmek dcweegpqln nsisglaacv ltlprsllhe
      601 qprgtpnrsq adadfasevm svsdweefdn ssed
//
LOCUS       NP_062017                335 aa            linear   ROD 28-APR-2025
DEFINITION  tartrate-resistant acid phosphatase type 5 isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_062017
VERSION     NP_062017.2
DBSOURCE    REFSEQ: accession NM_019144.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Brito,V.G.B., Patrocinio,M.S., de Sousa,M.C.L., Barreto,A.E.A.,
            Frasnelli,S.C.T., Lara,V.S., Santos,C.F. and Oliveira,S.H.P.
  TITLE     Telmisartan Prevents Alveolar Bone Loss by Decreasing the
            Expression of Osteoclasts Markers in Hypertensive Rats With
            Periodontal Disease
  JOURNAL   Front Pharmacol 11, 579926 (2020)
   PUBMED   33364953
  REMARK    Erratum:[Front Pharmacol. 2021 Feb 19;11:635927. doi:
            10.3389/fphar.2020.635927. PMID: 33679393]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Solberg,L.B., Brorson,S.H., Stordalen,G.A., Baekkevold,E.S.,
            Andersson,G. and Reinholt,F.P.
  TITLE     Increased tartrate-resistant Acid phosphatase expression in
            osteoblasts and osteocytes in experimental osteoporosis in rats
  JOURNAL   Calcif Tissue Int 94 (5), 510-521 (2014)
   PUBMED   24395179
  REMARK    GeneRIF: increased osteoclast activity does not affect TRAP
            expression in osteoblasts and osteocytes
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Fernandes Mda,S., Yanai,M.M., Martins,G.M., Iano,F.G., Leite,A.L.,
            Cestari,T.M., Taga,R., Buzalaf,M.A. and de Oliveira,R.C.
  TITLE     Effects of fluoride in bone repair: an evaluation of RANKL, OPG and
            TRAP expression
  JOURNAL   Odontology 102 (1), 22-30 (2014)
   PUBMED   22878484
  REMARK    GeneRIF: RANKL and OPG expressions were not changed by chronic
            exposure to fluoride in the drinking water during the studied
            periods; on the other hand, TRAP expression was changed (at 7 days)
            by chronic exposure to fluoride
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Harada,K., Itoh,H., Kawazoe,Y., Miyazaki,S., Doi,K., Kubo,T.,
            Akagawa,Y. and Shiba,T.
  TITLE     Polyphosphate-mediated inhibition of tartrate-resistant acid
            phosphatase and suppression of bone resorption of osteoclasts
  JOURNAL   PLoS One 8 (11), e78612 (2013)
   PUBMED   24223830
  REMARK    GeneRIF: Polyphosphate may play an important regulatory role in
            osteoclastic bone resorption by inhibiting TRAP activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Chen,X., Qin,B., Li,X., Jin,T., Zhu,G., Zhou,W. and Wang,Z.
  TITLE     Effects of fluoride and cadmium co-exposure on bone in male rats
  JOURNAL   Biol Trace Elem Res 154 (3), 396-402 (2013)
   PUBMED   23868496
  REMARK    GeneRIF: Data indicate that tartrate-resistant acid phosphatase 5b
            levels treated with cadmium and fluoride or in combination were
            1-2.5 folds higher than the control.
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Wisner-Lynch,L.A., Shalhoub,V. and Marks,S.C. Jr.
  TITLE     Administration of colony stimulating factor-1 to toothless
            osteopetrotic rats normalizes osteoblast, but not osteoclast, gene
            expression
  JOURNAL   Bone 16 (6), 611-618 (1995)
   PUBMED   7669437
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Ek-Rylander,B., Bill,P., Norgard,M., Nilsson,S. and Andersson,G.
  TITLE     Cloning, sequence, and developmental expression of a type 5,
            tartrate-resistant, acid phosphatase of rat bone
  JOURNAL   J Biol Chem 266 (36), 24684-24689 (1991)
   PUBMED   1722212
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Ek-Rylander,B., Bergman,T. and Andersson,G.
  TITLE     Characterization of a tartrate-resistant acid phosphatase (ATPase)
            from rat bone: hydrodynamic properties and N-terminal amino acid
            sequence
  JOURNAL   J Bone Miner Res 6 (4), 365-373 (1991)
   PUBMED   1830446
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Roiko,K., Janne,O.A. and Vihko,P.
  TITLE     Primary structure of rat secretory acid phosphatase and comparison
            to other acid phosphatases
  JOURNAL   Gene 89 (2), 223-229 (1990)
   PUBMED   2373368
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Plakhotin,M.V., Loktionova,L.Ia., Luk'ianovskii,V.A.,
            Filippov,Iu.I. and Ochirov,N.I.
  TITLE     [Osteosynthesis of the tubular bones using a polymeric pin]
  JOURNAL   Veterinariia (12), 89-90 (1978)
   PUBMED   734913
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CV074238.1, BC078847.1 and BM386942.1.
            
            On Aug 8, 2012 this sequence version replaced NP_062017.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN16676789
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..335
                     /product="tartrate-resistant acid phosphatase type 5
                     isoform 1 precursor"
                     /EC_number="3.1.3.2"
                     /note="tartrate-resistant acid phosphatase type 5; acid
                     phosphatase type V; TR-AP; trATPase; tartrate-resistant
                     acid ATPase; type 5 acid phosphatase"
                     /calculated_mol_wt=34350
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3163
     Region          36..321
                     /region_name="MPP_ACP5"
                     /note="Homo sapiens acid phosphatase 5 and related
                     proteins, metallophosphatase domain; cd07378"
                     /db_xref="CDD:277324"
     Site            order(43,81,84,120,215,224,250,252)
                     /site_type="active"
                     /db_xref="CDD:277324"
     Site            order(43,81,84,120,215,250,252)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277324"
     Site            126
                     /site_type="other"
                     /note="N-glycosylation site [posttranslational
                     modification]"
                     /db_xref="CDD:277324"
     CDS             1..335
                     /gene="Acp5"
                     /gene_synonym="Trap; TTRRAP"
                     /coded_by="NM_019144.2:71..1078"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25732"
                     /db_xref="RGD:2022"
ORIGIN      
        1 mttcasssmd twmvllglqi lllpllahct apastlrfva vgdwggvpna pfhtareman
       61 akeiartvqi mgadfimslg dnfyftgvhd andkrfqetf edvfsdralr nipwyvlagn
      121 hdhlgnvsaq iayskiskrw nfpspyyrlr fkvprsnitv aifmldtvml cgnsddfvsq
      181 qpemprdlgv artqlswlkk qlaaakedyv lvaghypiws iaehgptrcl vknlrpllaa
      241 ygvtaylcgh dhnlqylqde ngvgyvlsga gnfmdpsvrh qrkvpngylr fhygsedslg
      301 gftyveigsk emsityveas gkslfktslp rrprp
//
LOCUS       NP_001020181             973 aa            linear   ROD 28-APR-2025
DEFINITION  NLR family member X1 precursor [Rattus norvegicus].
ACCESSION   NP_001020181
VERSION     NP_001020181.1
DBSOURCE    REFSEQ: accession NM_001025010.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 973)
  AUTHORS   Zhang,Y., Chen,D., Wang,Y., Wang,X., Zhang,Z. and Xin,Y.
  TITLE     Neuroprotective effects of melatonin-mediated mitophagy through
            nucleotide-binding oligomerization domain and leucine-rich
            repeat-containing protein X1 in neonatal hypoxic-ischemic brain
            damage
  JOURNAL   FASEB J 37 (2), e22784 (2023)
   PUBMED   36692416
  REMARK    GeneRIF: Neuroprotective effects of melatonin-mediated mitophagy
            through nucleotide-binding oligomerization domain and leucine-rich
            repeat-containing protein X1 in neonatal hypoxic-ischemic brain
            damage.
REFERENCE   2  (residues 1 to 973)
  AUTHORS   Guan,X., Zhou,W., Li,L. and Peng,Q.
  TITLE     Dexmedetomidine Alleviates Hypoxic-Ischemic Brain Damage in
            Neonatal Rats Through Reducing MicroRNA-134-5p-Mediated NLRX1
            Downregulation
  JOURNAL   J Stroke Cerebrovasc Dis 31 (5), 106411 (2022)
   PUBMED   35259612
  REMARK    GeneRIF: Dexmedetomidine Alleviates Hypoxic-Ischemic Brain Damage
            in Neonatal Rats Through Reducing MicroRNA-134-5p-Mediated NLRX1
            Downregulation.
REFERENCE   3  (residues 1 to 973)
  AUTHORS   Tong,R., Jia,T., Shi,R. and Yan,F.
  TITLE     Inhibition of microRNA-15 protects H9c2 cells against CVB3-induced
            myocardial injury by targeting NLRX1 to regulate the NLRP3
            inflammasome
  JOURNAL   Cell Mol Biol Lett 25, 6 (2020)
   PUBMED   32099552
  REMARK    GeneRIF: Inhibition of microRNA-15 protects H9c2 cells against
            CVB3-induced myocardial injury by targeting NLRX1 to regulate the
            NLRP3 inflammasome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 973)
  AUTHORS   Allen,I.C., Moore,C.B., Schneider,M., Lei,Y., Davis,B.K.,
            Scull,M.A., Gris,D., Roney,K.E., Zimmermann,A.G., Bowzard,J.B.,
            Ranjan,P., Monroe,K.M., Pickles,R.J., Sambhara,S. and Ting,J.P.
  TITLE     NLRX1 protein attenuates inflammatory responses to infection by
            interfering with the RIG-I-MAVS and TRAF6-NF-kappaB signaling
            pathways
  JOURNAL   Immunity 34 (6), 854-865 (2011)
   PUBMED   21703540
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089834.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089834.1, SRR8487230.137780.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..973
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..973
                     /product="NLR family member X1 precursor"
                     /calculated_mol_wt=98067
     transit_peptide 1..84
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q5FVQ8.1)"
                     /calculated_mol_wt=9542
     Region          41..965
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          73..554
                     /region_name="Required for interaction with MAVS.
                     /evidence=ECO:0000250|UniProtKB:Q86UT6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ8.1)"
     mat_peptide     85..973
                     /product="NLR family member X1. /evidence=ECO:0000250.
                     /id=PRO_0000296192"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ8.1)"
                     /calculated_mol_wt=98067
     Region          158..318
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          554..972
                     /region_name="Required for the repression of MAVS-induced
                     interferon signaling.
                     /evidence=ECO:0000250|UniProtKB:Q86UT6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ8.1)"
     Region          696..724
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          725..746
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          747..770
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <751..881
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          771..806
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          807..834
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          863..884
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..973
                     /gene="Nlrx1"
                     /gene_synonym="RGD1311293"
                     /coded_by="NM_001025010.1:89..3010"
                     /db_xref="GeneID:315599"
                     /db_xref="RGD:1311293"
ORIGIN      
        1 mrwgchlprt swgsglgrtv plpdelriqs swpfkgvhhp lrpprafirh hgnsadsapp
       61 pgrhgqlfrs isateaiqrh rrnltewfsr lpreerqfgp tfaldtvhvd pvirestpdd
      121 llrpstelat ghqrtqaelp plalsqlfdp dacgrrvqtv vlygtvgtgk stlvrkmvld
      181 wcygrlpafe llipfscedl sslgstpasl cqlvtqrytp lkevlplmna agsrllfvlh
      241 glerlnldfr lagtglcsdp eepgapaaim vnllrkymlp easilvttrp saigripsky
      301 vgrygeicgf sdtnlqklyf qlrlnqpdcg ygaggtgvsv tpaqrdnliq mlsrnleghh
      361 qiaaacflps ycwlvcatlh flhaptsagq tltsiytsfl rlnfngetld stdpsnlslm
      421 syaartmgkl ayegvssrkt yfseedvrgc leagikteee fqllqifrrd alrfflapcv
      481 epghlgtfvf tvpamqeyla alyivlglrk talqrvgkev fefvgrvged vslvlgivak
      541 llplrilpll fnllkvvprv fgrmvsksre avaqamvlem freedyyndd vldqmgasil
      601 gvegprrhpd eppedevfel fpmfmsglls ahnravlaql gcpiknldal enaqaikkkl
      661 gkmgrqvlpp selldhlffh yefqnqrfsa evlgslrqln lagvrmtplk ctvvasvlgs
      721 grhpldevnl ascqldpagl htlmpvllra rklglqlnnl gpeacrdlrd lllhdqcqit
      781 tlrlsnnplt aagvgvlmdg lagntsvthl sllhtdlgde glellaaqld rnkqlqelnv
      841 ayngagdtva lalakaarkh pslellhlyf nelssegrqv lrdlggsgeg garvvaslte
      901 gtavseywsv ilsevqrnln swdpvrvqrh lklllrdled srgatlnpwr kaqllrvese
      961 vktlleqlgg sgh
//
LOCUS       NP_852032                388 aa            linear   ROD 28-APR-2025
DEFINITION  LIM/homeobox protein Lhx9 [Rattus norvegicus].
ACCESSION   NP_852032 XP_001066548
VERSION     NP_852032.1
DBSOURCE    REFSEQ: accession NM_181367.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Molle,B., Pere,S., Failli,V., Bach,I. and Retaux,S.
  TITLE     Lhx9 and lhx9alpha: differential biochemical properties and effects
            on neuronal differentiation
  JOURNAL   DNA Cell Biol 23 (11), 761-768 (2004)
   PUBMED   15585134
  REMARK    GeneRIF: Lhx9 and Lhx9alpha isoforms could be implicated in
            regulating various aspects of neuronal differentiation
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Mazaud,S., Oreal,E., Guigon,C.J., Carre-Eusebe,D. and Magre,S.
  TITLE     Lhx9 expression during gonadal morphogenesis as related to the
            state of cell differentiation
  JOURNAL   Gene Expr Patterns 2 (3-4), 373-377 (2002)
   PUBMED   12617828
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Birk,O.S., Casiano,D.E., Wassif,C.A., Cogliati,T., Zhao,L.,
            Zhao,Y., Grinberg,A., Huang,S., Kreidberg,J.A., Parker,K.L.,
            Porter,F.D. and Westphal,H.
  TITLE     The LIM homeobox gene Lhx9 is essential for mouse gonad formation
  JOURNAL   Nature 403 (6772), 909-913 (2000)
   PUBMED   10706291
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY273890.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001066548.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY273890.1, AY724502.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984036, SAMN14984043
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..388
                     /product="LIM/homeobox protein Lhx9"
                     /note="LIM homeobox protein 9; LIM-homeodomain type
                     transcription factor 9"
                     /calculated_mol_wt=42803
     Region          52..115
                     /region_name="LIM1_Lhx2"
                     /note="The first LIM domain of Lhx2; cd09469"
                     /db_xref="CDD:188853"
     Site            order(62,65,83,86,89,92,111,114)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188853"
     Region          120..178
                     /region_name="LIM2_Lhx2_Lhx9"
                     /note="The second LIM domain of Lhx2 and Lhx9 family;
                     cd09377"
                     /db_xref="CDD:188763"
     Site            order(124,127,146,149,152,155,174,177)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188763"
     Region          239..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W90.1)"
     Region          259..315
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          321..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W90.1)"
     Region          369..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80W90.1)"
     CDS             1..388
                     /gene="Lhx9"
                     /coded_by="NM_181367.2:127..1293"
                     /db_xref="GeneID:289048"
                     /db_xref="RGD:727956"
ORIGIN      
        1 mlngttleaa mlfhgisggh iqgimeemer rsktearlak gtqlngrdag mpplspekpa
       61 lcagcggkis dryyllavdk qwhlrclkcc ecklalesel tcfakdgsiy ckedyyrrfs
      121 vqrcarchlg isasemvmra rdsvyhlscf tcstcnktlt tgdhfgmkds lvycrahfet
      181 llqgeyppql sytelaaksg glalpyfngt gtvqkgrprk rkspalgvdi vnynsgcnen
      241 eadhldrdqq pyppsqktkr mrtsfkhhql rtmksyfain hnpdakdlkq laqktgltkr
      301 vlqvwfqnar akfrrnllrq enggvdkadg tslpappsad sgaltppgta ttltdltnpt
      361 vtvvttvtsn mdshesgsps qttltnlf
//
LOCUS       NP_001037745             320 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial glutamate carrier 2 [Rattus norvegicus].
ACCESSION   NP_001037745 XP_001058858
VERSION     NP_001037745.2
DBSOURCE    REFSEQ: accession NM_001044280.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Casimir,M., Lasorsa,F.M., Rubi,B., Caille,D., Palmieri,F., Meda,P.
            and Maechler,P.
  TITLE     Mitochondrial glutamate carrier GC1 as a newly identified player in
            the control of glucose-stimulated insulin secretion
  JOURNAL   J Biol Chem 284 (37), 25004-25014 (2009)
   PUBMED   19584051
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB726923.1, BC094517.1 and BG380364.1.
            
            On Aug 31, 2012 this sequence version replaced NP_001037745.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094517.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..320
                     /product="mitochondrial glutamate carrier 2"
                     /note="glutamate carrier 2, mitochondrial; GC-2;
                     glutamate/H(+) symporter 2; solute carrier family 25
                     (mitochondrial carrier), member 18; solute carrier family
                     25 (glutamate carrier), member 18"
                     /calculated_mol_wt=34039
     Region          9..102
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          11..97
                     /region_name="Solcar 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            66..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Region          105..215
                     /region_name="Solcar 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Region          111..209
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H1K4; propagated from
                     UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Region          222..307
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          224..313
                     /region_name="Solcar 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q505J6.2)"
     CDS             1..320
                     /gene="Slc25a18"
                     /coded_by="NM_001044280.2:274..1236"
                     /db_xref="GeneID:681896"
                     /db_xref="RGD:1590470"
ORIGIN      
        1 miacrmssqd lsitakling giaglvgvtc vfpidlaktr lqnqqgkdvy kgmtdclvkt
       61 araegflgmy rgaavnltlv tpekaiklaa ndflrqllmq dgtqrnlkme mlagcgagic
      121 qvvitcpmem lkiqlqdagr lavcqqasas atptsrpyst gststhrrps atliawellr
      181 tqglsglyrg lgatllrdip fsiiyfplfa nlnqlgvsel tgkasfthsf vagcaagsvs
      241 avavtpldvl ktriqtlkkg lgedtyrgvt dcarklwtqe gaaafmkgag cralviaplf
      301 giaqgvyfig igerilkcfe
//
LOCUS       NP_001102733             239 aa            linear   ROD 28-APR-2025
DEFINITION  leucine rich adaptor protein 1 [Rattus norvegicus].
ACCESSION   NP_001102733 XP_575888
VERSION     NP_001102733.1
DBSOURCE    REFSEQ: accession NM_001109263.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Jing,Z., Yuan,X., Zhang,J., Huang,X., Zhang,Z., Liu,J., Zhang,M.,
            Oyang,J., Zhang,Y., Zhang,Z. and Yang,R.
  TITLE     Chromosome 1 open reading frame 190 promotes activation of
            NF-kappaB canonical pathway and resistance of dendritic cells to
            tumor-associated inhibition in vitro
  JOURNAL   J Immunol 185 (11), 6719-6727 (2010)
   PUBMED   21048106
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Tan,I., Yong,J., Dong,J.M., Lim,L. and Leung,T.
  TITLE     A tripartite complex containing MRCK modulates lamellar actomyosin
            retrograde flow
  JOURNAL   Cell 135 (1), 123-136 (2008)
   PUBMED   18854160
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474008.2.
            
            On Oct 4, 2007 this sequence version replaced XP_575888.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132271 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q35"
     Protein         1..239
                     /product="leucine rich adaptor protein 1"
                     /note="adaptor protein LRAP35a; NF-kappa-B activator
                     C1orf190 homolog; leucine repeat adapter protein 35A"
                     /calculated_mol_wt=25760
     Region          39..159
                     /region_name="LURAP"
                     /note="Leucine rich adaptor protein; pfam14854"
                     /db_xref="CDD:434270"
     Region          55..83
                     /region_name="LRR 1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G3.1)"
     Region          93..114
                     /region_name="LRR 2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G3.1)"
     Region          107..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A8G3.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D6I9; propagated from
                     UniProtKB/Swiss-Prot (D4A8G3.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A8G3.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D4A8G3.1)"
     CDS             1..239
                     /gene="Lurap1"
                     /gene_synonym="LRAP35a; Lrp35a; RGD1566001"
                     /coded_by="NM_001109263.1:107..826"
                     /db_xref="GeneID:500527"
                     /db_xref="RGD:1566001"
ORIGIN      
        1 megtaesqtp dlrdvegkvg rktpegllrg lrgecdlgts gdvllpgass tghglgdkim
       61 alrmelaylr aidvkilqql vtlnegieav rwlleergtl tshcssltss qysltggspe
      121 rsrrgswdsl pdtsstdrld svsigsfldt vapreldeqg hpgpscpeid wakvipsedr
      181 artevdmtst klgsltatwk lpgdglqcgp pepseddsak qgfeahwywg qcqddvtfl
//
LOCUS       NP_714962                688 aa            linear   ROD 28-APR-2025
DEFINITION  sodium channel and clathrin linker 1 [Rattus norvegicus].
ACCESSION   NP_714962
VERSION     NP_714962.1
DBSOURCE    REFSEQ: accession NM_153740.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Ye,X., Zeng,H., Ning,G., Reiter,J.F. and Liu,A.
  TITLE     C2cd3 is critical for centriolar distal appendage assembly and
            ciliary vesicle docking in mammals
  JOURNAL   Proc Natl Acad Sci U S A 111 (6), 2164-2169 (2014)
   PUBMED   24469809
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Tanos,B.E., Yang,H.J., Soni,R., Wang,W.J., Macaluso,F.P.,
            Asara,J.M. and Tsou,M.F.
  TITLE     Centriole distal appendages promote membrane docking, leading to
            cilia initiation
  JOURNAL   Genes Dev 27 (2), 163-168 (2013)
   PUBMED   23348840
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Wilson,M.J., Zhang,M.M., Azam,L., Olivera,B.M., Bulaj,G. and
            Yoshikami,D.
  TITLE     Navbeta subunits modulate the inhibition of Nav1.8 by the analgesic
            gating modifier muO-conotoxin MrVIB
  JOURNAL   J Pharmacol Exp Ther 338 (2), 687-693 (2011)
   PUBMED   21586605
  REMARK    GeneRIF: Coexpression of beta-subunits of NaV1.8 strongly
            influences the affinity of the muO-conotoxin MrVIB conopeptide for
            the channel.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Liu,C., Cummins,T.R., Tyrrell,L., Black,J.A., Waxman,S.G. and
            Dib-Hajj,S.D.
  TITLE     CAP-1A is a novel linker that binds clathrin and the voltage-gated
            sodium channel Na(v)1.8
  JOURNAL   Mol Cell Neurosci 28 (4), 636-649 (2005)
   PUBMED   15797711
  REMARK    GeneRIF: SAP-1 is the first example of an adapter protein that
            links clathrin and a sodium channel and may regulate Na(v)1.8
            channel density at the cell surface.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF421190.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF421190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q26"
     Protein         1..688
                     /product="sodium channel and clathrin linker 1"
                     /note="clathrin-associated protein 1A; sodium
                     channel-associated protein 1; sodium channel
                     Nav1.8-binding protein"
                     /calculated_mol_wt=80198
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96NL6; propagated from
                     UniProtKB/Swiss-Prot (Q8CJ99.1)"
     Region          <212..>688
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:G5E861; propagated from
                     UniProtKB/Swiss-Prot (Q8CJ99.1)"
     CDS             1..688
                     /gene="Sclt1"
                     /gene_synonym="CAP-1A; Sap1"
                     /coded_by="NM_153740.1:1..2067"
                     /db_xref="GeneID:266809"
                     /db_xref="RGD:628721"
ORIGIN      
        1 mateidllrd qnvklndilr qhqiehifrd pamqnsmskg grgdtltnsv ndqsalppli
       61 aeyekhleel nrqltyyqkh mgemklqlet vitenerlhs klkdavekql ealpfgtgig
      121 ndicaddetv rnlqeqlqia nqeknwavql wqtasqeles vqklyqehmt eaqihvfenr
      181 kqkdqlnnfq qltkklhvan eniemtnhhf lktvteqnme ieklrkqlrq akldlrvavt
      241 kveeltkvte glqeqmlkke edimsaqgke easdrrvqql qssikqlesr lciaiqeanv
      301 lktgktqlek qikelqakcs esenekyeai srardsmqll eeanikqnqi lleekqkeve
      361 rekmkktish liqdaaikar kevestkkqy evlilqlkee lsalqmdcde kqgqidrair
      421 gkraveeele kiyregkqde gdyrkleemh qrclaaersk ddlqlrlkta enrikqlein
      481 sseeisrshe miqklqtvle serencgfvs eqrlklqqen eqlqketedl rkvaleaqkk
      541 aklkvstmeh qfsikehgfe vqlremedsn rnsivelrhl laaqqktanr wkeetkklte
      601 saemrisslk selsrqklht qellsqlema nekvaenekl ilehqekanr lqrrlsqaee
      661 raasasqqls vitvqrrkaa smmnleni
//
LOCUS       NP_001034638             531 aa            linear   ROD 28-APR-2025
DEFINITION  UDP-glucuronosyltransferase 1A5 precursor [Rattus norvegicus].
ACCESSION   NP_001034638
VERSION     NP_001034638.1
DBSOURCE    REFSEQ: accession NM_001039549.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Gagez,A.L., Rouguieg-Malki,K., Sauvage,F.L., Marquet,P. and
            Picard,N.
  TITLE     Simultaneous evaluation of six human glucuronidation activities in
            liver microsomes using liquid chromatography-tandem mass
            spectrometry
  JOURNAL   Anal Biochem 427 (1), 52-59 (2012)
   PUBMED   22579593
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Bellemare,J., Rouleau,M., Girard,H., Harvey,M. and Guillemette,C.
  TITLE     Alternatively spliced products of the UGT1A gene interact with the
            enzymatically active proteins to inhibit glucuronosyltransferase
            activity in vitro
  JOURNAL   Drug Metab Dispos 38 (10), 1785-1789 (2010)
   PUBMED   20610558
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Rowbotham,S.E., Illingworth,N.A., Daly,A.K., Veal,G.J. and
            Boddy,A.V.
  TITLE     Role of UDP-glucuronosyltransferase isoforms in 13-cis retinoic
            acid metabolism in humans
  JOURNAL   Drug Metab Dispos 38 (7), 1211-1217 (2010)
   PUBMED   20308471
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Kishi,M., Emi,Y., Sakaguchi,M., Ikushiro,S. and Iyanagi,T.
  TITLE     Ontogenic isoform switching of UDP-glucuronosyltransferase family 1
            in rat liver
  JOURNAL   Biochem Biophys Res Commun 377 (3), 815-819 (2008)
   PUBMED   18938141
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Operana,T.N. and Tukey,R.H.
  TITLE     Oligomerization of the UDP-glucuronosyltransferase 1A proteins:
            homo- and heterodimerization analysis by fluorescence resonance
            energy transfer and co-immunoprecipitation
  JOURNAL   J Biol Chem 282 (7), 4821-4829 (2007)
   PUBMED   17179145
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Li,Y.Q., Prentice,D.A., Howard,M.L., Mashford,M.L. and Desmond,P.V.
  TITLE     The effect of hormones on the expression of five isoforms of
            UDP-glucuronosyltransferase in primary cultures of rat hepatocytes
  JOURNAL   Pharm Res 16 (2), 191-197 (1999)
   PUBMED   10100302
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Emi,Y., Ikushiro,S. and Iyanagi,T.
  TITLE     Drug-responsive and tissue-specific alternative expression of
            multiple first exons in rat UDP-glucuronosyltransferase family 1
            (UGT1) gene complex
  JOURNAL   J Biochem 117 (2), 392-399 (1995)
   PUBMED   7608130
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Iyanagi,T.
  TITLE     Molecular basis of multiple UDP-glucuronosyltransferase isoenzyme
            deficiencies in the hyperbilirubinemic rat (Gunn rat)
  JOURNAL   J Biol Chem 266 (35), 24048-24052 (1991)
   PUBMED   1748678
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Ritter,J.K., Crawford,J.M. and Owens,I.S.
  TITLE     Cloning of two human liver bilirubin UDP-glucuronosyltransferase
            cDNAs with expression in COS-1 cells
  JOURNAL   J Biol Chem 266 (2), 1043-1047 (1991)
   PUBMED   1898728
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Sato,H., Koiwai,O., Tanabe,K. and Kashiwamata,S.
  TITLE     Isolation and sequencing of rat liver bilirubin
            UDP-glucuronosyltransferase cDNA: possible alternate splicing of a
            common primary transcript
  JOURNAL   Biochem Biophys Res Commun 169 (1), 260-264 (1990)
   PUBMED   2112380
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092531.16, AY435132.1 and AC120922.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF461734.1, AY435132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..531
                     /product="UDP-glucuronosyltransferase 1A5 precursor"
                     /EC_number="2.4.1.17"
                     /note="UDP-glucuronosyltransferase 1-5;
                     UDP-glucuronosyltransferase 1A5; B5; UDPGT; UGT1*5;
                     UGT1.5; UGT1-05; UDP glycosyltransferase 1 family,
                     polypeptide A5; UDP glucuronosyltransferase 1 family,
                     polypeptide A5"
                     /calculated_mol_wt=57290
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2650
     mat_peptide     26..531
                     /product="UDP-glucuronosyltransferase 1A5.
                     /id=PRO_0000036016"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64638.1)"
                     /calculated_mol_wt=57290
     Region          26..522
                     /region_name="UDPGT"
                     /note="UDP-glucoronosyl and UDP-glucosyl transferase;
                     pfam00201"
                     /db_xref="CDD:278624"
     Site            order(36..37,39,200,203..204,208,249,307,370,372,374..375,
                     378)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(36,307,370,372,374..375)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            37
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64638.1)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64638.1)"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64638.1)"
     Site            293
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64638.1)"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64638.1)"
     Site            489..505
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64638.1)"
     CDS             1..531
                     /gene="Ugt1a5"
                     /gene_synonym="UDPGT 1-5; Ugt1; Ugt1a6"
                     /coded_by="NM_001039549.1:36..1631"
                     /db_xref="GeneID:574523"
                     /db_xref="RGD:1583689"
ORIGIN      
        1 mglhvtlqgl aglllllyal pwaeggkvlv fpmegshwls mrdvvrelha rghqavvlap
       61 evtvhikeed fftlqtypvp ytrqgfrqqm mrnikvvfet gnyvktflet seilknistv
      121 llrscmnllh ngsllqhlns ssfdmvltdp vipcgavlak ylgiptvffl ryipcgidse
      181 atqcpkpssy ipnlltmlsd hmtflqrvkn mlyplalkyi chfsftryes lasellqrev
      241 slvevlshas vwlfrgdfvf dyprpvmpnm vfiggincvi kkplsqefea yvnasgehgi
      301 vvfslgsmvs eipekkamei aealgripqt vlwrytgtrp snlakntilv kwlpqndllg
      361 hpkarafith sgshgiyegi cngvpmvmmp lfgdqmdnak rmetrgagvt lnvlemtadd
      421 lenalktvin nksykenimr lsslhkdrpi epldlavfwv eyvmrhkgap hlrpaahdlt
      481 wyqyhsldvi gfllaivltv vfivykscay gcrkcfggkg rvkkshkskt h
//
LOCUS       NP_113860                740 aa            linear   ROD 28-APR-2025
DEFINITION  solute carrier family 15 member 2 [Rattus norvegicus].
ACCESSION   NP_113860
VERSION     NP_113860.2
DBSOURCE    REFSEQ: accession NM_031672.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Parker,J.L., Deme,J.C., Wu,Z., Kuteyi,G., Huo,J., Owens,R.J.,
            Biggin,P.C., Lea,S.M. and Newstead,S.
  TITLE     Cryo-EM structure of PepT2 reveals structural basis for
            proton-coupled peptide and prodrug transport in mammals
  JOURNAL   Sci Adv 7 (35) (2021)
   PUBMED   34433568
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Alghamdi,O., King,N., Jones,G.L. and Moens,P.D.J.
  TITLE     Effect of ageing and hypertension on the expression and activity of
            PEPT2 in normal and hypertrophic hearts
  JOURNAL   Amino Acids 53 (2), 183-193 (2021)
   PUBMED   33404911
  REMARK    GeneRIF: Effect of ageing and hypertension on the expression and
            activity of PEPT2 in normal and hypertrophic hearts.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Minocha,E., Chaturvedi,C.P. and Nityanand,S.
  TITLE     Renogenic characterization and in vitro differentiation of rat
            amniotic fluid stem cells into renal proximal tubular- and
            juxtaglomerular-like cells
  JOURNAL   In Vitro Cell Dev Biol Anim 55 (2), 138-147 (2019)
   PUBMED   30645697
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Gukasyan,H.J., Uchiyama,T., Kim,K.J., Ehrhardt,C., Wu,S.K.,
            Borok,Z., Crandall,E.D. and Lee,V.H.L.
  TITLE     Oligopeptide Transport in Rat Lung Alveolar Epithelial Cells is
            Mediated by Pept2
  JOURNAL   Pharm Res 34 (12), 2488-2497 (2017)
   PUBMED   28831683
  REMARK    GeneRIF: This study confirms the absence of Pept1 from rat lung
            alveolar epithelium in vitro. Functional Slc15a2/PEPT2 expression
            in type II-like cell monolayers suggests its involvement in
            oligopeptide lung disposition, and offers rationale for therapeutic
            development of di/tripeptides, peptidomimetics employing pulmonary
            drug delivery.
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Beale,J.H., Parker,J.L., Samsudin,F., Barrett,A.L., Senan,A.,
            Bird,L.E., Scott,D., Owens,R.J., Sansom,M.S.P., Tucker,S.J.,
            Meredith,D., Fowler,P.W. and Newstead,S.
  TITLE     Crystal Structures of the Extracellular Domain from PepT1 and PepT2
            Provide Novel Insights into Mammalian Peptide Transport
  JOURNAL   Structure 23 (10), 1889-1899 (2015)
   PUBMED   26320580
  REMARK    GeneRIF: Crystal structures of the extracellular domain from PepT1
            and PepT2 provide novel insights into mammalian peptide transport.
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Rubio-Aliaga,I., Boll,M. and Daniel,H.
  TITLE     Cloning and characterization of the gene encoding the mouse peptide
            transporter PEPT2
  JOURNAL   Biochem Biophys Res Commun 276 (2), 734-741 (2000)
   PUBMED   11027540
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Ganapathy,M.E., Huang,W., Rajan,D.P., Carter,A.L., Sugawara,M.,
            Iseki,K., Leibach,F.H. and Ganapathy,V.
  TITLE     beta-lactam antibiotics as substrates for OCTN2, an organic
            cation/carnitine transporter
  JOURNAL   J Biol Chem 275 (3), 1699-1707 (2000)
   PUBMED   10636865
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Chen,X.Z., Zhu,T., Smith,D.E. and Hediger,M.A.
  TITLE     Stoichiometry and kinetics of the high-affinity H+-coupled peptide
            transporter PepT2
  JOURNAL   J Biol Chem 274 (5), 2773-2779 (1999)
   PUBMED   9915809
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Saito,H., Terada,T., Okuda,M., Sasaki,S. and Inui,K.
  TITLE     Molecular cloning and tissue distribution of rat peptide
            transporter PEPT2
  JOURNAL   Biochim Biophys Acta 1280 (2), 173-177 (1996)
   PUBMED   8639691
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Liu,W., Liang,R., Ramamoorthy,S., Fei,Y.J., Ganapathy,M.E.,
            Hediger,M.A., Ganapathy,V. and Leibach,F.H.
  TITLE     Molecular cloning of PEPT 2, a new member of the H+/peptide
            cotransporter family, from human kidney
  JOURNAL   Biochim Biophys Acta 1235 (2), 461-466 (1995)
   PUBMED   7756356
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC085327.1.
            
            On Sep 12, 2012 this sequence version replaced NP_113860.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085327.1, D63149.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..740
                     /product="solute carrier family 15 member 2"
                     /note="peptide transporter 2; kidney H(+)/peptide
                     cotransporter; solute carrier family 15 (H+/peptide
                     transporter), member 2; solute carrier family 15
                     (oligopeptide transporter), member 2"
                     /calculated_mol_wt=82490
     Region          69..707
                     /region_name="2A1704"
                     /note="Peptide:H+ symporter (also transports b-lactam
                     antibiotics, the antitumor agent, bestatin, and various
                     protease inhibitors); TIGR00926"
                     /db_xref="CDD:273343"
     CDS             1..740
                     /gene="Slc15a2"
                     /coded_by="NM_031672.2:140..2362"
                     /db_xref="GeneID:60577"
                     /db_xref="RGD:61972"
ORIGIN      
        1 mleereskep amnpfqknes ketlfspvst eemlprppsp pkksppkifg ssypvsiafi
       61 vvnefcerfs yygmkavltl yflyflhwne dtstsvyhaf sslcyftpil gaaiadswlg
      121 kfktiiylsl vyvlghvfks lgaipilggk mlhtilslvg lslialgtgg ikpcvaafgg
      181 dqfeeehaea rtryfsvfyl ainagslist fitpmlrgdv kcfgqdcyal afgvpgllmv
      241 lalvvfamgs kmyrkpppeg nivaqvikci wfalcnrfrn rsgdlpkrqh wldwaaekyp
      301 khliadvkal trvlflyipl pmfwalldqq gsrwtlqank mngdlgffvl qpdqmqvlnp
      361 flvlifiplf dlviyrlisk crinfsslrk mavgmilacl afavaalvet kingmihpqp
      421 asqeiflqvl nladgdvkvt vlgsrnnsll vesvssfqnt thysklhlea ksqdlhfhlk
      481 ynslsvhndh sveekncyql lihqdgesis smlvkdtgik pangmaairf intlhkdlni
      541 sldtdaplsv gkdygvsayr tvlrgkypav hcetedkvfs ldlgqldfgt tylfvitnit
      601 sqglqawkae dipvnklsia wqlpqyvlvt aaevmfsvtg lefsysqaps smksvlqaaw
      661 lltvavgnii vlvvaqfsgl aqwaefvlfs clllvvclif svmayyyvpl ksedtreatd
      721 kqipavqgnm inletkntrl
//
LOCUS       NP_001257975             185 aa            linear   ROD 28-APR-2025
DEFINITION  sodium channel regulatory subunit beta-1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001257975
VERSION     NP_001257975.1
DBSOURCE    REFSEQ: accession NM_001271046.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Al-Ward,H., Liu,N., Omorou,M., Huang,Y., Chen,W., Liu,C.Y., Lv,S.,
            Murshed,A., Shaher,F., Li,Y., Zhang,Y., Lu,L., Gao,W., Sun,Y.E. and
            Xu,H.
  TITLE     The relationship between miRNA-210 and SCN1B in fetal rats with
            hypoxic-ischemic brain injury
  JOURNAL   Biosci Rep 43 (1) (2023)
   PUBMED   36541246
  REMARK    GeneRIF: The relationship between miRNA-210 and SCN1B in fetal rats
            with hypoxic-ischemic brain injury.
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Pan,X., Li,Z., Zhou,Q., Shen,H., Wu,K., Huang,X., Chen,J.,
            Zhang,J., Zhu,X., Lei,J., Xiong,W., Gong,H., Xiao,B. and Yan,N.
  TITLE     Structure of the human voltage-gated sodium channel Nav1.4 in
            complex with beta1
  JOURNAL   Science 362 (6412) (2018)
   PUBMED   30190309
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Johnson,K.W., Herold,K.F., Milner,T.A., Hemmings,H.C. Jr. and
            Platholi,J.
  TITLE     Sodium channel subtypes are differentially localized to pre- and
            post-synaptic sites in rat hippocampus
  JOURNAL   J Comp Neurol 525 (16), 3563-3578 (2017)
   PUBMED   28758202
  REMARK    GeneRIF: Nav1.1 and Nav1.2 are highly expressed in axon terminals
            in central hilus compared to stratum radiatum and in dendrites and
            spines in stratum radiatum compared to central hilus
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Sanchez-Solano,A., Islas,A.A., Scior,T., Paiz-Candia,B.,
            Millan-PerezPena,L. and Salinas-Stefanon,E.M.
  TITLE     Characterization of specific allosteric effects of the Na+ channel
            beta1 subunit on the Nav1.4 isoform
  JOURNAL   Eur Biophys J 46 (5), 485-494 (2017)
   PUBMED   28012039
  REMARK    GeneRIF: the role of the intracellular IFM motif of rNav1.4
            (skeletal muscle isoform of the rat Na(+) channel) on the
            alpha-beta1 functional interaction
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Huang,X., Du,Y., Yang,P., Lin,S., Xi,Y., Yang,Z. and Ma,A.
  TITLE     Age-dependent alterations of voltage-gated Na(+) channel isoforms
            in rat sinoatrial node
  JOURNAL   Mech Ageing Dev 152, 80-90 (2015)
   PUBMED   26528804
  REMARK    GeneRIF: the presences of Nav1.1, Nav1.6, Navbeta1 and Navbeta3
            mRNA and their reduced levels in rat SAN during aging.
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Kazen-Gillespie,K.A., Ragsdale,D.S., D'Andrea,M.R., Mattei,L.N.,
            Rogers,K.E. and Isom,L.L.
  TITLE     Cloning, localization, and functional expression of sodium channel
            beta1A subunits
  JOURNAL   J Biol Chem 275 (2), 1079-1088 (2000)
   PUBMED   10625649
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Dib-Hajj,S.D. and Waxman,S.G.
  TITLE     Genes encoding the beta 1 subunit of voltage-dependent Na+ channel
            in rat, mouse and human contain conserved introns
  JOURNAL   FEBS Lett 377 (3), 485-488 (1995)
   PUBMED   8549781
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Oh,Y. and Waxman,S.G.
  TITLE     The beta 1 subunit mRNA of the rat brain Na+ channel is expressed
            in glial cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9985-9989 (1994)
   PUBMED   7937931
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Makita,N., Bennett,P.B. Jr. and George,A.L. Jr.
  TITLE     Voltage-gated Na+ channel beta 1 subunit mRNA expressed in adult
            human skeletal muscle, heart, and brain is encoded by a single gene
  JOURNAL   J Biol Chem 269 (10), 7571-7578 (1994)
   PUBMED   8125980
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Isom,L.L., De Jongh,K.S., Patton,D.E., Reber,B.F., Offord,J.,
            Charbonneau,H., Walsh,K., Goldin,A.L. and Catterall,W.A.
  TITLE     Primary structure and functional expression of the beta 1 subunit
            of the rat brain sodium channel
  JOURNAL   Science 256 (5058), 839-842 (1992)
   PUBMED   1375395
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (3) contains an alternate exon in
            the 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at a downstream start codon, compared to variant 1. The
            encoded isoform (2) has a shorter N-terminus, compared to isoform
            1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ216374.1, SRR22399481.601673.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..185
                     /product="sodium channel regulatory subunit beta-1 isoform
                     2"
                     /note="sodium channel subunit beta-1; sodium channel,
                     voltage-gated, type 1, beta polypeptide; sodium channel,
                     voltage-gated, type I, beta polypeptide; sodium channel,
                     voltage-gated, type I, beta subunit; sodium channel
                     regulatory subunit beta-1"
                     /calculated_mol_wt=21295
     Region          8..114
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     CDS             1..185
                     /gene="Scn1b"
                     /coded_by="NM_001271046.2:106..663"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:29686"
                     /db_xref="RGD:3631"
ORIGIN      
        1 mtfkilcisc krrsettaet ftewtfrqkg teefvkilry enevlqleed erfegrvvwn
       61 gsrgtkdlqd lsifitnvty nhsgdyechv yrllffdnye hntsvvkkih levvdkanrd
      121 masivseimm yvlivvltiw lvaemvycyk kiaaateaaa qenaseylai tseskenctg
      181 vqvae
//
LOCUS       NP_665729                425 aa            linear   ROD 28-APR-2025
DEFINITION  stabilizer of axonemal microtubules 4 [Rattus norvegicus].
ACCESSION   NP_665729
VERSION     NP_665729.1
DBSOURCE    REFSEQ: accession NM_145786.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Baeza,V., Cifuentes,M., Martinez,F., Ramirez,E., Nualart,F.,
            Ferrada,L., Oviedo,M.J., De Lima,I., Troncoso,N., Saldivia,N. and
            Salazar,K.
  TITLE     IIIG9 inhibition in adult ependymal cells changes adherens
            junctions structure and induces cellular detachment
  JOURNAL   Sci Rep 11 (1), 18537 (2021)
   PUBMED   34535732
  REMARK    GeneRIF: IIIG9 inhibition in adult ependymal cells changes adherens
            junctions structure and induces cellular detachment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Cifuentes,M., Baeza,V., Arrabal,P.M., Visser,R., Grondona,J.M.,
            Saldivia,N., Martinez,F., Nualart,F. and Salazar,K.
  TITLE     Expression of a Novel Ciliary Protein, IIIG9, During the
            Differentiation and Maturation of Ependymal Cells
  JOURNAL   Mol Neurobiol 55 (2), 1652-1664 (2018)
   PUBMED   28194645
  REMARK    GeneRIF: IIIG9 is localized in the cilia of adult ependymal cells
            and that its expression is correlated with the process of ependymal
            differentiation and with the maturation of radial glia.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Danielson,P.E., Sautkulis,L.N., Foye,P.E., Hedlund,P.B. and
            Carson,M.J.
  TITLE     A novel mRNA expressed along brain ventricles
  JOURNAL   Brain Res Gene Expr Patterns 1 (2), 83-88 (2002)
   PUBMED   15018803
  REMARK    GeneRIF: IIIG9 mRNA is expressed along brain ventricles
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY032665.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY032665.1, BC081718.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..425
                     /product="stabilizer of axonemal microtubules 4"
                     /note="uncharacterized protein C11orf66 homolog; protein
                     phosphatase 1, regulatory subunit 32"
                     /calculated_mol_wt=47482
     Region          2..416
                     /region_name="PPP1R32"
                     /note="Protein phosphatase 1 regulatory subunit 32;
                     pfam15691"
                     /db_xref="CDD:464804"
     Region          259..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HR9.1)"
     Region          315..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HR9.1)"
     CDS             1..425
                     /gene="Saxo4"
                     /gene_synonym="Iiig9; Ppp1r32"
                     /coded_by="NM_145786.1:117..1394"
                     /db_xref="GeneID:252958"
                     /db_xref="RGD:708532"
ORIGIN      
        1 mmgklplgvv spyvkmssgg csdplkfyat cyctaygree fkprmgshvg tgyksnyrpl
       61 vsyqphldtl dnpavgeqih dtsksvasqs yaplevpdgk qplpwnlhqt tsgygrekvn
      121 igplskevrk vhfdtqdhgp qtitglepke vplihqqqgk gstewensry gprfmtseyn
      181 skylkespnh pdlllkktig skeetgftee stknpivfqp psqaypgdpv lhpgrsitks
      241 dylpishpqg neflpvlarg sdrdtgysrv serslnprmp tpssqptsms hrsyqppqrm
      301 qqsnvallgr esvgnkeptg ftlnnpsyvr ssyeqdrdqr ylttynqgyf enipkgldre
      361 gwtrggiqpq kagayalsep vthmdttpnp tetlrhlhph vgrtltsvdp fyrdvphsnr
      421 yptss
//
LOCUS       NP_062132                279 aa            linear   ROD 28-APR-2025
DEFINITION  complement component 1 Q subcomponent-binding protein,
            mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_062132 XP_346399
VERSION     NP_062132.2
DBSOURCE    REFSEQ: accession NM_019259.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Udvari,E.B., Volgyi,K., Gulyassy,P., Dimen,D., Kis,V., Barna,J.,
            Szabo,E.R., Lubec,G., Juhasz,G., Kekesi,K.A. and Dobolyi,A.
  TITLE     Synaptic proteome changes in the hypothalamus of mother rats
  JOURNAL   J Proteomics 159, 54-66 (2017)
   PUBMED   28286321
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Arif,M., Thakur,S.C. and Datta,K.
  TITLE     Disrupted hyaluronan binding protein 1 (HABP1) expression: one of
            the key mediator for ovarian dysfunction in polycystic ovary rat
  JOURNAL   Mol Cell Biochem 398 (1-2), 233-244 (2015)
   PUBMED   25300617
  REMARK    GeneRIF: Data indicate that disrupted ovarian hyaluronan binding
            protein 1 (HABP1) along with concurrent altered expression and
            hyperactivation of related MMPs can lead to abnormal follicular
            maturation resulting into ovarian dysfunction in polycystic ovary
            (PCO).
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Boyken,J., Gronborg,M., Riedel,D., Urlaub,H., Jahn,R. and Chua,J.J.
  TITLE     Molecular profiling of synaptic vesicle docking sites reveals novel
            proteins but few differences between glutamatergic and GABAergic
            synapses
  JOURNAL   Neuron 78 (2), 285-297 (2013)
   PUBMED   23622064
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Yagi,M., Uchiumi,T., Takazaki,S., Okuno,B., Nomura,M., Yoshida,S.,
            Kanki,T. and Kang,D.
  TITLE     p32/gC1qR is indispensable for fetal development and mitochondrial
            translation: importance of its RNA-binding ability
  JOURNAL   Nucleic Acids Res 40 (19), 9717-9737 (2012)
   PUBMED   22904065
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Yoshikawa,H., Komatsu,W., Hayano,T., Miura,Y., Homma,K.,
            Izumikawa,K., Ishikawa,H., Miyazawa,N., Tachikawa,H., Yamauchi,Y.,
            Isobe,T. and Takahashi,N.
  TITLE     Splicing factor 2-associated protein p32 participates in ribosome
            biogenesis by regulating the binding of Nop52 and fibrillarin to
            preribosome particles
  JOURNAL   Mol Cell Proteomics 10 (8), M110.006148 (2011)
   PUBMED   21536856
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Lynch,N.J., Reid,K.B., van den Berg,R.H., Daha,M.R., Leigh,L.A.,
            Ghebrehiwet,B., Lim,W.B. and Schwaeble,W.J.
  TITLE     Characterisation of the rat and mouse homologues of gC1qBP, a 33
            kDa glycoprotein that binds to the globular 'heads' of C1q
  JOURNAL   FEBS Lett 418 (1-2), 111-114 (1997)
   PUBMED   9414106
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Muta,T., Kang,D., Kitajima,S., Fujiwara,T. and Hamasaki,N.
  TITLE     p32 protein, a splicing factor 2-associated protein, is localized
            in mitochondrial matrix and is functionally important in
            maintaining oxidative phosphorylation
  JOURNAL   J Biol Chem 272 (39), 24363-24370 (1997)
   PUBMED   9305894
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Herwald,H., Dedio,J., Kellner,R., Loos,M. and Muller-Esterl,W.
  TITLE     Isolation and characterization of the kininogen-binding protein p33
            from endothelial cells. Identity with the gC1q receptor
  JOURNAL   J Biol Chem 271 (22), 13040-13047 (1996)
   PUBMED   8662673
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Deb,T.B. and Datta,K.
  TITLE     Molecular cloning of human fibroblast hyaluronic acid-binding
            protein confirms its identity with P-32, a protein co-purified with
            splicing factor SF2. Hyaluronic acid-binding protein as P-32
            protein, co-purified with splicing factor SF2
  JOURNAL   J Biol Chem 271 (4), 2206-2212 (1996)
   PUBMED   8567680
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Ghebrehiwet,B., Lim,B.L., Peerschke,E.I., Willis,A.C. and Reid,K.B.
  TITLE     Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
            glycoprotein that binds to the globular 'heads' of C1q
  JOURNAL   J Exp Med 179 (6), 1809-1821 (1994)
   PUBMED   8195709
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070510.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_346399.1, NP_062132.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070510.1, FQ214480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..279
                     /product="complement component 1 Q subcomponent-binding
                     protein, mitochondrial precursor"
                     /note="complement component 1 Q subcomponent-binding
                     protein, mitochondrial; GC1q-R protein; glycoprotein
                     gC1qBP; complement component 1, q subcomponent binding
                     protein"
                     /calculated_mol_wt=23726
     transit_peptide 1..71
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (O35796.2)"
                     /calculated_mol_wt=7289
     mat_peptide     72..279
                     /product="Complement component 1 Q subcomponent-binding
                     protein, mitochondrial. /id=PRO_0000018592"
                     /note="propagated from UniProtKB/Swiss-Prot (O35796.2)"
                     /calculated_mol_wt=23726
     Region          74..91
                     /region_name="C1q binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35796.2)"
     Region          84..276
                     /region_name="MAM33"
                     /note="Mitochondrial glycoprotein; pfam02330"
                     /db_xref="CDD:460534"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q07021; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O35658; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     Region          134..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35796.2)"
     Region          166..210
                     /region_name="Interaction with MAVS.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O35796.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q07021; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07021; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07021; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q07021; propagated from
                     UniProtKB/Swiss-Prot (O35796.2)"
     CDS             1..279
                     /gene="C1qbp"
                     /gene_synonym="gC1qR; Habp1"
                     /coded_by="NM_019259.2:2..841"
                     /db_xref="GeneID:29681"
                     /db_xref="RGD:2230"
ORIGIN      
        1 mlpllrcvpr algaaatglr asipapplrh llqpaprpcl rpfgllsvra gsarrsgllq
       61 ppvpcacgcg alhtegdkaf vefltdeike ekkiqkhksl pkmsgdwele vngteakllr
      121 kvagekitvt fninnsippt fdgeeepsqg qkaeeqepel tstpnfvvev tktdgkktlv
      181 ldchypedei ghedeaesdi fsikevsfqt tgdsewrdtn ytlntdsldw alydhlmdfl
      241 adrgvdntfa delvelstal ehqeyitfle dlksfvksq
//
LOCUS       NP_001008861             921 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 11 [Rattus norvegicus].
ACCESSION   NP_001008861 XP_579253
VERSION     NP_001008861.2
DBSOURCE    REFSEQ: accession NM_001008861.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Fang,Y., Zhao,T., Ni,H., Li,Y., Zhu,Y., Gao,R., Zhang,L., Jia,Z.
            and Chen,G.
  TITLE     USP11 exacerbates neuronal apoptosis after traumatic brain injury
            via PKM2-mediated PI3K/AKT signaling pathway
  JOURNAL   Brain Res 1807, 148321 (2023)
   PUBMED   36898475
  REMARK    GeneRIF: USP11 exacerbates neuronal apoptosis after traumatic brain
            injury via PKM2-mediated PI3K/AKT signaling pathway.
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Zhang,Y., Hailati,J., Ma,X., Midilibieke,H. and Liu,Z.
  TITLE     Ubiquitin-specific protease 11 Aggravates
            Ischemia-reperfusion-induced Cardiomyocyte Pyroptosis and Injury by
            Promoting TRAF3 Deubiquitination
  JOURNAL   Balkan Med J 40 (3), 205-214 (2023)
   PUBMED   37000116
  REMARK    GeneRIF: Ubiquitin-specific protease 11 Aggravates
            Ischemia-reperfusion-induced Cardiomyocyte Pyroptosis and Injury by
            Promoting TRAF3 Deubiquitination.
REFERENCE   3  (residues 1 to 921)
  AUTHORS   Xu,Z., Li,X., Chen,J., Zhao,J., Wang,J., Ji,Y., Shen,Y., Han,L.,
            Shi,J. and Zhang,D.
  TITLE     USP11, Deubiquitinating Enzyme, Associated with Neuronal Apoptosis
            Following Intracerebral Hemorrhage
  JOURNAL   J Mol Neurosci 58 (1), 16-27 (2016)
   PUBMED   26334325
  REMARK    GeneRIF: USP11 is upregulated in neurons adjacent to the hematoma
            following ICH.
REFERENCE   4  (residues 1 to 921)
  AUTHORS   Schoenfeld,A.R., Apgar,S., Dolios,G., Wang,R. and Aaronson,S.A.
  TITLE     BRCA2 is ubiquitinated in vivo and interacts with USP11, a
            deubiquitinating enzyme that exhibits prosurvival function in the
            cellular response to DNA damage
  JOURNAL   Mol Cell Biol 24 (17), 7444-7455 (2004)
   PUBMED   15314155
REFERENCE   5  (residues 1 to 921)
  AUTHORS   Puente,X.S. and Lopez-Otin,C.
  TITLE     A genomic analysis of rat proteases and protease inhibitors
  JOURNAL   Genome Res 14 (4), 609-622 (2004)
   PUBMED   15060002
REFERENCE   6  (residues 1 to 921)
  AUTHORS   Ideguchi,H., Ueda,A., Tanaka,M., Yang,J., Tsuji,T., Ohno,S.,
            Hagiwara,E., Aoki,A. and Ishigatsubo,Y.
  TITLE     Structural and functional characterization of the USP11
            deubiquitinating enzyme, which interacts with the RanGTP-associated
            protein RanBPM
  JOURNAL   Biochem J 367 (Pt 1), 87-95 (2002)
   PUBMED   12084015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC090333.1.
            
            On Sep 28, 2005 this sequence version replaced NP_001008861.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090333.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..921
                     /product="ubiquitin carboxyl-terminal hydrolase 11"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 11; ubiquitin
                     thioesterase 11; deubiquitinating enzyme 11;
                     ubiquitin-specific-processing protease 11"
                     /calculated_mol_wt=105108
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5D006.1)"
     Region          23..888
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Site            194
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51784; propagated from
                     UniProtKB/Swiss-Prot (Q5D006.1)"
     Region          592..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5D006.1)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51784; propagated from
                     UniProtKB/Swiss-Prot (Q5D006.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5D006.1)"
     Region          893..921
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5D006.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51784; propagated from
                     UniProtKB/Swiss-Prot (Q5D006.1)"
     CDS             1..921
                     /gene="Usp11"
                     /gene_synonym="Uhx1"
                     /coded_by="NM_001008861.2:10..2775"
                     /db_xref="GeneID:408217"
                     /db_xref="RGD:1303052"
ORIGIN      
        1 maavaadpaa aavpasaedr etqpeampdl dqqwrqigng rerplrages wflvekhwyk
       61 qweayvkggd qdastfpgsi nnsglfedqi swhlrerlve gddyvllpap awnylvswyg
      121 lkddqppier kvielpgirk vevypielll vqhsdmetal tiqfsysdsv dlvlqtareq
      181 flvepqedtr lwtknsegsl drlcntqitl ldacletgql vimetrnkdg twpsaqlcgm
      241 nnmpdededf qgqpgicglt nlgntcfmns alqclsnvpq lteyflnnry leelnfrnpl
      301 gmkgelaeay adlvkqtwsg yhrsivpnvf knkvghfasq flgyqqhdsq ellsflldgl
      361 hedlnrvkkk eyvelcngag rpdlevaqea wqnhkrrnds vivdtfhglf kstlvcpdcg
      421 nvsvtfdpfc ylsvplpvcs rrvlevffvp mdprrkpeqh rvvvpkkgni sdlcvalsth
      481 tsvapdkmiv advfshrfyk lyqledplsg ildrddifvy evtgriepve gsrddivvpv
      541 ylrertpsrd ynnsyyglil fghpllvsvp rdrfswegly nilmyrlsry vtkptsdddd
      601 gdekgdened edveddssse eekeemsgpt dndgtqeseq eqagtssgvt grcpslldns
      661 lhtsqwpprr rrkqlftlqt vnsngtsdrt tspeeaqtqp yiamdwepem krryydevea
      721 egyvkhdcvg ymlkknpvql keciklfttv etlekenpwy cssckqhqla tkkldlwmlp
      781 evliihlkrf sfskfsrekl dtlvqfpird ldfsefvikp knesapdlyk ydliavsnhy
      841 ggmrdghytt facnkdsgqw hyfddnsvsp vnenqieska ayvlfyqrqd vgrrqsqtas
      901 setptspass stpnsdimdv n
//
LOCUS       NP_671706                456 aa            linear   ROD 28-APR-2025
DEFINITION  ruvB-like 1 [Rattus norvegicus].
ACCESSION   NP_671706
VERSION     NP_671706.1
DBSOURCE    REFSEQ: accession NM_147177.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Mir,R.A., Bele,A., Mirza,S., Srivastava,S., Olou,A.A., Ammons,S.A.,
            Kim,J.H., Gurumurthy,C.B., Qiu,F., Band,H. and Band,V.
  TITLE     A Novel Interaction of Ecdysoneless (ECD) Protein with R2TP Complex
            Component RUVBL1 Is Required for the Functional Role of ECD in Cell
            Cycle Progression
  JOURNAL   Mol Cell Biol 36 (6), 886-899 (2015)
   PUBMED   26711270
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Freund,A., Zhong,F.L., Venteicher,A.S., Meng,Z., Veenstra,T.D.,
            Frydman,J. and Artandi,S.E.
  TITLE     Proteostatic control of telomerase function through TRiC-mediated
            folding of TCAB1
  JOURNAL   Cell 159 (6), 1389-1403 (2014)
   PUBMED   25467444
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Obri,A., Ouararhni,K., Papin,C., Diebold,M.L., Padmanabhan,K.,
            Marek,M., Stoll,I., Roy,L., Reilly,P.T., Mak,T.W., Dimitrov,S.,
            Romier,C. and Hamiche,A.
  TITLE     ANP32E is a histone chaperone that removes H2A.Z from chromatin
  JOURNAL   Nature 505 (7485), 648-653 (2014)
   PUBMED   24463511
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Makino,Y., Kanemaki,M., Kurokawa,Y., Koji,T. and Tamura,Ta.
  TITLE     A rat RuvB-like protein, TIP49a, is a germ cell-enriched novel DNA
            helicase
  JOURNAL   J Biol Chem 274 (22), 15329-15335 (1999)
   PUBMED   10336418
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Kikuchi,N., Gohshi,T., Kawahire,S., Tachibana,T., Yoneda,Y.,
            Isobe,T., Lim,C.R., Kohno,K., Ichimura,T., Omata,S. and Horigome,T.
  TITLE     Molecular shape and ATP binding activity of rat p50, a putative
            mammalian homologue of RuvB DNA helicase
  JOURNAL   J Biochem 125 (3), 487-494 (1999)
   PUBMED   10050036
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Kurokawa,Y., Kanemaki,M., Makino,Y. and Tamura,T.A.
  TITLE     A notable example of an evolutionary conserved gene: studies on a
            putative DNA helicase TIP49
  JOURNAL   DNA Seq 10 (1), 37-42 (1999)
   PUBMED   10565543
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Bauer,A., Huber,O. and Kemler,R.
  TITLE     Pontin52, an interaction partner of beta-catenin, binds to the TATA
            box binding protein
  JOURNAL   Proc Natl Acad Sci U S A 95 (25), 14787-14792 (1998)
   PUBMED   9843967
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Kanemaki,M., Makino,Y., Yoshida,T., Kishimoto,T., Koga,A.,
            Yamamoto,K., Yamamoto,M., Moncollin,V., Egly,J.M., Muramatsu,M. and
            Tamura,T.
  TITLE     Molecular cloning of a rat 49-kDa TBP-interacting protein (TIP49)
            that is highly homologous to the bacterial RuvB
  JOURNAL   Biochem Biophys Res Commun 235 (1), 64-68 (1997)
   PUBMED   9196036
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB002406.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002406.1, BC086531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..456
                     /product="ruvB-like 1"
                     /EC_number="3.6.4.12"
                     /note="RuvB-like protein 1; pontin 52; DNA helicase p50;
                     49 kDa TBP-interacting protein; 49 kDa TATA box-binding
                     protein-interacting protein"
                     /calculated_mol_wt=50083
     Region          14..369
                     /region_name="TIP49"
                     /note="TIP49 P-loop domain; pfam06068"
                     /db_xref="CDD:399217"
     Region          374..439
                     /region_name="TIP49_C"
                     /note="TIP49 AAA-lid domain; pfam17856"
                     /db_xref="CDD:436097"
     Site            453
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y265; propagated from
                     UniProtKB/Swiss-Prot (P60123.1)"
     CDS             1..456
                     /gene="Ruvbl1"
                     /gene_synonym="NMP238; Pontin52; Tip49a"
                     /coded_by="NM_147177.1:31..1401"
                     /db_xref="GeneID:65137"
                     /db_xref="RGD:68373"
ORIGIN      
        1 mkieevkstt ktqriashsh vkglgldesg lakqaasglv gqenareacg vivelikskk
       61 magravllag ppgtgktala laiaqelgsk vpfcpmvgse vysteikkte vlmenfrrai
      121 glriketkev yegevteltp cetenpmggy gktishviig lktakgtkql kldpsifesl
      181 qkerveagdv iyieansgav krqgrcdtya tefdleaeey vplpkgdvhk kkeiiqdvtl
      241 hdldvanarp qggqdilsmm gqlmkpkkte itdklrgein kvvnkyidqg vaelvpgvlf
      301 vdevhmldie cftylhrale ssiapivifa snrgncvirg teditsphgi pldlldrvmi
      361 irtmlytpqe mkqiikiraq teginiseea lnhlgeigtk ttlrysvqll tpanllakin
      421 gkdsiekehv eeiselfyda kssakiladq qdkymk
//
LOCUS       NP_001012154             629 aa            linear   ROD 28-APR-2025
DEFINITION  FAST kinase domain-containing protein 4 [Rattus norvegicus].
ACCESSION   NP_001012154 XP_341254
VERSION     NP_001012154.1
DBSOURCE    REFSEQ: accession NM_001012154.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Boehm,E., Zaganelli,S., Maundrell,K., Jourdain,A.A., Thore,S. and
            Martinou,J.C.
  TITLE     FASTKD1 and FASTKD4 have opposite effects on expression of specific
            mitochondrial RNAs, depending upon their endonuclease-like RAP
            domain
  JOURNAL   Nucleic Acids Res 45 (10), 6135-6146 (2017)
   PUBMED   28335001
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Simarro,M., Gimenez-Cassina,A., Kedersha,N., Lazaro,J.B.,
            Adelmant,G.O., Marto,J.A., Rhee,K., Tisdale,S., Danial,N.,
            Benarafa,C., Orduna,A. and Anderson,P.
  TITLE     Fast kinase domain-containing protein 3 is a mitochondrial protein
            essential for cellular respiration
  JOURNAL   Biochem Biophys Res Commun 401 (3), 440-446 (2010)
   PUBMED   20869947
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087073.1.
            
            On Feb 11, 2005 this sequence version replaced XP_341254.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087073.1, FQ217643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..629
                     /product="FAST kinase domain-containing protein 4"
                     /note="protein TBRG4; transforming growth factor beta
                     regulated gene 4"
                     /calculated_mol_wt=71050
     Region          94..342
                     /region_name="TBRG4-like_N"
                     /note="transforming growth factor beta (TGFbeta) regulator
                     4 (TBRG4) and similar proteins; predicted alpha-helical
                     domain N-terminal to FAST kinase-like protein, subdomain 1
                     (FAST_1); cd23739"
                     /db_xref="CDD:467932"
     Region          367..438
                     /region_name="FAST_1"
                     /note="FAST kinase-like protein, subdomain 1; pfam06743"
                     /db_xref="CDD:461999"
     Region          449..534
                     /region_name="FAST_2"
                     /note="FAST kinase-like protein, subdomain 2; pfam08368"
                     /db_xref="CDD:462448"
     Region          561..618
                     /region_name="RAP"
                     /note="This domain is found in various eukaryotic species,
                     particularly in apicomplexans; smart00952"
                     /db_xref="CDD:214932"
     CDS             1..629
                     /gene="Tbrg4"
                     /coded_by="NM_001012154.1:49..1938"
                     /db_xref="GeneID:360977"
                     /db_xref="RGD:1309737"
ORIGIN      
        1 mavrlmkqct cllreatrlv ptvapvgrlr lagvacktlt ssvsspssgs ltellgkeqv
       61 ftpypehqev dyliekatrp eellellggd hslhhnhaal ilirlsylls ekpkekallv
      121 edarfqqlvr lvdsqitsvw hgtlvkllrs lytlvlpqgs kelrsveqev rwrlrrlkyk
      181 hlvflaesca pfmkeqhske llaellrhle rrwteisdsr tlvsmmtmag hlseslmnrl
      241 edkclelveq fgpdelrkvl mtlaaqsrrs vpllraisyh lvqkpfpmtk gmlldlayay
      301 gklsfhqtqv aqrlaadllp fipsmtpgev arcaksfafl kwlnlplfea ftqhllnsaq
      361 dvslshlcsv llafarlnfh peqedqffnl vhekldsvlg slepalqvdl vwalcvlqqv
      421 qvaelqtvlh pglhtrfles kspkdqstfq klvhinstal leypeykgpf lpasavapsp
      481 spsnkkmtpl qkelqdalka llgnndtgsl evatqygwvl daevlldaeg hflplrdfva
      541 phlaqpvgnq plppgakria flrwefpnfn srskdllgrf vlarrhvlaa gflvvdvpyy
      601 ewldlksewq ktaylkdkmr kavaeelak
//
LOCUS       NP_001008305             416 aa            linear   ROD 28-APR-2025
DEFINITION  prostate tumor-overexpressed gene 1 protein homolog [Rattus
            norvegicus].
ACCESSION   NP_001008305 XP_214944
VERSION     NP_001008305.1
DBSOURCE    REFSEQ: accession NM_001008304.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085836.1.
            
            On Dec 16, 2004 this sequence version replaced XP_214944.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..416
                     /product="prostate tumor-overexpressed gene 1 protein
                     homolog"
                     /note="prostate tumor over expressed gene 1; prostate
                     tumor overexpressed 1"
                     /calculated_mol_wt=46718
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2W6.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91VU8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2W6.1)"
     Region          89..238
                     /region_name="Med25"
                     /note="Mediator complex subunit 25 PTOV activation and
                     synapsin 2; pfam11232"
                     /db_xref="CDD:463243"
     Region          184..416
                     /region_name="Interaction with FLOT1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2W6.1)"
     Region          254..399
                     /region_name="Med25"
                     /note="Mediator complex subunit 25 PTOV activation and
                     synapsin 2; pfam11232"
                     /db_xref="CDD:463243"
     CDS             1..416
                     /gene="Ptov1"
                     /coded_by="NM_001008304.1:109..1359"
                     /db_xref="GeneID:292888"
                     /db_xref="RGD:1306977"
ORIGIN      
        1 mvrprraphr sgaggplggr grpprplvvr avrsrswpag prgpqpprir arsappmega
       61 rvfgalgpig psspgltlgg lavnehrlsn kllawsgvle wqekrrpfsd saaklkrtlp
      121 cqayvnqgen letdqwpqkl imqlipqqll ttlgplfrns qlaqfhftnr dcdslkglcr
      181 imgngfagcm lfphispcev rvlmllyssk kkifmglipy dqsgfvnair qvittrkqav
      241 gpggvhsgpv qivnnkflaw sgvmewqepr pepnsrskrw lpshvyvnqg eilrtdqwpr
      301 rlfmqlipqq llttlvplfr nsrlvqfhft kdmetlkslc rimdngfagc vhfsykasce
      361 vrvlmllyss ekkifiglip hdqsnfvngi rrvianqqqv lqrsleqeqq qrgmgg
//
LOCUS       NP_001178039            2919 aa            linear   ROD 28-APR-2025
DEFINITION  cadherin EGF LAG seven-pass G-type receptor 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_001178039 XP_001076220
VERSION     NP_001178039.1
DBSOURCE    REFSEQ: accession NM_001191110.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2919)
  AUTHORS   Zhou,X., Zhan,Z., Tang,C., Li,J., Zheng,X., Zhu,S. and Qi,J.
  TITLE     Silencing Celsr2 inhibits the proliferation and migration of
            Schwann cells through suppressing the Wnt/beta-catenin signaling
            pathway
  JOURNAL   Biochem Biophys Res Commun 533 (4), 623-630 (2020)
   PUBMED   32988580
  REMARK    GeneRIF: Silencing Celsr2 inhibits the proliferation and migration
            of Schwann cells through suppressing the Wnt/beta-catenin signaling
            pathway.
REFERENCE   2  (residues 1 to 2919)
  AUTHORS   Vogel,P., Read,R.W., Hansen,G.M., Payne,B.J., Small,D., Sands,A.T.
            and Zambrowicz,B.P.
  TITLE     Congenital hydrocephalus in genetically engineered mice
  JOURNAL   Vet Pathol 49 (1), 166-181 (2012)
   PUBMED   21746835
REFERENCE   3  (residues 1 to 2919)
  AUTHORS   Qu,Y., Glasco,D.M., Zhou,L., Sawant,A., Ravni,A., Fritzsch,B.,
            Damrau,C., Murdoch,J.N., Evans,S., Pfaff,S.L., Formstone,C.,
            Goffinet,A.M., Chandrasekhar,A. and Tissir,F.
  TITLE     Atypical cadherins Celsr1-3 differentially regulate migration of
            facial branchiomotor neurons in mice
  JOURNAL   J Neurosci 30 (28), 9392-9401 (2010)
   PUBMED   20631168
REFERENCE   4  (residues 1 to 2919)
  AUTHORS   Tissir,F., Qu,Y., Montcouquiol,M., Zhou,L., Komatsu,K., Shi,D.,
            Fujimori,T., Labeau,J., Tyteca,D., Courtoy,P., Poumay,Y., Uemura,T.
            and Goffinet,A.M.
  TITLE     Lack of cadherins Celsr2 and Celsr3 impairs ependymal ciliogenesis,
            leading to fatal hydrocephalus
  JOURNAL   Nat Neurosci 13 (6), 700-707 (2010)
   PUBMED   20473291
REFERENCE   5  (residues 1 to 2919)
  AUTHORS   Shima,Y., Kawaguchi,S.Y., Kosaka,K., Nakayama,M., Hoshino,M.,
            Nabeshima,Y., Hirano,T. and Uemura,T.
  TITLE     Opposing roles in neurite growth control by two seven-pass
            transmembrane cadherins
  JOURNAL   Nat Neurosci 10 (8), 963-969 (2007)
   PUBMED   17618280
  REMARK    GeneRIF: The Celsr2 enhanced neurite growth of neuron in
            hippocampus of rat.
REFERENCE   6  (residues 1 to 2919)
  AUTHORS   Shima,Y., Kengaku,M., Hirano,T., Takeichi,M. and Uemura,T.
  TITLE     Regulation of dendritic maintenance and growth by a mammalian
            7-pass transmembrane cadherin
  JOURNAL   Dev Cell 7 (2), 205-216 (2004)
   PUBMED   15296717
REFERENCE   7  (residues 1 to 2919)
  AUTHORS   Morgan,R., El-Kadi,A.M. and Theokli,C.
  TITLE     Flamingo, a cadherin-type receptor involved in the Drosophila
            planar polarity pathway, can block signaling via the canonical wnt
            pathway in Xenopus laevis
  JOURNAL   Int J Dev Biol 47 (4), 245-252 (2003)
   PUBMED   12755329
REFERENCE   8  (residues 1 to 2919)
  AUTHORS   Vincent,J.B., Skaug,J. and Scherer,S.W.
  TITLE     The human homologue of flamingo, EGFL2, encodes a brain-expressed
            large cadherin-like protein with epidermal growth factor-like
            domains, and maps to chromosome 1p13.3-p21.1
  JOURNAL   DNA Res 7 (3), 233-235 (2000)
   PUBMED   10907856
REFERENCE   9  (residues 1 to 2919)
  AUTHORS   Johnson,K.J., Patel,S.R. and Boekelheide,K.
  TITLE     Multiple cadherin superfamily members with unique expression
            profiles are produced in rat testis
  JOURNAL   Endocrinology 141 (2), 675-683 (2000)
   PUBMED   10650949
REFERENCE   10 (residues 1 to 2919)
  AUTHORS   Nakayama,M., Nakajima,D., Nagase,T., Nomura,N., Seki,N. and
            Ohara,O.
  TITLE     Identification of high-molecular-weight proteins with multiple
            EGF-like motifs by motif-trap screening
  JOURNAL   Genomics 51 (1), 27-34 (1998)
   PUBMED   9693030
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000002.1.
            
            On Jul 17, 2010 this sequence version replaced XP_001076220.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011529.1, SRR26360194.2129060.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2919
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2919
                     /product="cadherin EGF LAG seven-pass G-type receptor 2
                     precursor"
                     /note="flamingo-like protein celsr2; seven-pass
                     transmembrane cadherin; multiple epidermal growth
                     factor-like domains 3; multiple EGF-like domains protein
                     3; multiple epidermal growth factor-like domains protein
                     3; cadherin EGF LAG seven-pas G-type receptor 2;
                     Flamingo1; cadherin, EGF LAG seven-pass G-type receptor 2
                     (flamingo homolog, Drosophila)"
                     /calculated_mol_wt=313897
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3245
     Region          185..285
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(192..193,248,250,281,283..284)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          293..395
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(300..301,356,358,391,393..394)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          404..501
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(410..411,463,465,497,499..500)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          509..606
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(516..517,569,571,602,604..605)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          614..708
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(621..622,674,676,704,706..707)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          716..811
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(723..724,774,776,807,809..810)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          819..917
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(826..827,880,882,913,915..916)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          925..1019
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(932..933,985,987,1015,1017..1018)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1042..1120
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          1289..1324
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1333..1366
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1369..1552
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          1578..1609
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1644..1770
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1795..1829
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1819..1868
                     /region_name="DSL"
                     /note="Delta serrate ligand; cl19567"
                     /db_xref="CDD:473190"
     Region          1924..1969
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domai;
                     smart00180"
                     /db_xref="CDD:214543"
     Site            order(1924,1926,1936,1943,1945,1954)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1972..2034
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Region          2051..2289
                     /region_name="GAIN"
                     /note="GPCR-Autoproteolysis INducing (GAIN) domain;
                     pfam16489"
                     /db_xref="CDD:465137"
     Region          2315..2368
                     /region_name="GPS"
                     /note="G-protein-coupled receptor proteolytic site domain;
                     smart00303"
                     /db_xref="CDD:197639"
     Region          2373..2626
                     /region_name="7tmB2_CELSR2"
                     /note="Cadherin EGF LAG seven-pass G-type receptor 2,
                     member of the class B2 family of seven-transmembrane G
                     protein-coupled receptors; cd15992"
                     /db_xref="CDD:320658"
     Region          2375..2400
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320658"
     Site            order(2380,2384,2426,2429..2430,2433,2440,2447,2519..2520,
                     2522,2524,2576,2579,2591,2595)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320658"
     Region          2409..2431
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320658"
     Region          2440..2467
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320658"
     Region          2479..2499
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320658"
     Region          2516..2545
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320658"
     Region          2557..2584
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320658"
     Region          2588..2613
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320658"
     CDS             1..2919
                     /gene="Celsr2"
                     /gene_synonym="Megf3"
                     /coded_by="NM_001191110.1:1..8760"
                     /db_xref="GeneID:83465"
                     /db_xref="RGD:69237"
ORIGIN      
        1 mrsraasapl ptpllpllll llllppspll gdqvgpcrsl gsggrgssga capvgwlcpa
       61 sasnlwlyts rcrdsgielt ghlvphhdgl rvwcpesgah iplppssegc pwscrllgig
      121 ghlspqgtlt lpqehpclka prlrcqsckl aqapglrage gsreesmggr rkrnvntapq
      181 fqppsyqatv penqpagtsv aslraidpde geagrleytm dalfdsrsnh ffsldpitga
      241 vttaeeldre tksthvfrvt aqdhgmprrs alatltilvt dtndhdpvfe qqeykeslre
      301 nlevgyevlt vratdgdapp nanilyrlle gpggspsevf eidprsgvir trgpvdreev
      361 esykliveas dqgrdpgprs stavvflsve ddndnapqfs ekryvvqvre dvtpgapvlr
      421 vtasdrdkgs nalvhysims gnargqfyld aqtgaldvvs pldyettkey tlriraqdgg
      481 rpplsnvsgl vtvqvldind napifvstpf qatvlesvpl gylvlhvqai dadagenarl
      541 eyslagvghd fpftinngtg wisvaaeldr eevdfysfgv eardhgtpal tasasvsvti
      601 ldvndnnptf tqpeytvrln edaavgtsvv tvsavdrdah svityqitsg ntrnrfsits
      661 qsggglvsla lpldyklerq yvlavtasdg trqdtaqivv nvtdanthrp vfqsshytvn
      721 vnedrpagtt vvlisatded tgenarityf medsipqfri dadtgavttq aeldyedqvs
      781 ytlaitardn gipqksdtty leilvndvnd napqflrdsy qgsvyedvpp ftsvlqisat
      841 drdsglngrv fytfqggddg dgdfivests givrtlrrld renvaqyilr ayavdkgmpp
      901 artpmevtvt vldvndnppv feqdefdvfv eenspiglav arvtatdpde gtnaqimyqi
      961 vegnipevfq ldifsgelta lvdldyedrp eyilviqats aplvsratvh vrlldrndnp
     1021 pvlgnfeilf nnyvtnrsss fpggaigrvp ahdpdisdsl tysfergnel slvllnastg
     1081 elrlsraldn nrpleaimsv lvsdgvhsvt aqcslrvtii tdemlthsit lrledmsper
     1141 flspllglfi qavaatlatp pdhvvvfnvq rdtdapgghi lnvslsvgqp pgpgggppfl
     1201 psedlqerly lnrslltais aqrvlpfddn iclrepceny mrcvsvlrfd ssapfiasss
     1261 vlfrpihpvg glrcrcppgf tgdycetevd lcysrpcgph ghcrsreggy tclcrdgytg
     1321 ehcevsarsg rctpgvckng gtcvnllvgg fkcdcpsgdf ekpfcqvttr sfparsfitf
     1381 rglrqrfhft lalsfatker dglllyngrf nekhdfvale viqeqvqltf sagestttvs
     1441 pfvpggvsdg qwhtvqlkyy nkpllgqtgl pqgpseqkva vvsvdgcdtg valrfgamlg
     1501 nyscaaqgtq ggskksldlt gplllggvpd lpesfpvrmr hfvgcmknlq vdsrhvdmad
     1561 fianngtvpg cptkknvcds ntchnggtcv nqwdafscec plgfggksca qemanpqrfl
     1621 gsslvawhgl slpisqpwhl slmfrtrqad gvllqavtrg rstitlqlra ghvvlsvegt
     1681 glqasslrle pgrandgdwh haqlslgasg gpghailsfd ygqqkaegnl gprlhglhls
     1741 nmtvggvpgp assvargfrg clqgvrvset pegvssldps rgesinvepg cswpdpcdsn
     1801 pcptnsycsn dwdsyscscd pgyygdnctn vcdlnpcehq svctrkpsap hgyiceclpn
     1861 ylgpycetri dqpcprgwwg hptcgpcncd vskgfdpdcn ktsgechcke nhyrppsspt
     1921 cllcdcyptg slsrvcdped gqcpckpgvi grqcdrcdnp faevttngce vnydscprai
     1981 eagiwwprtr fglpaaapcp kgsfgtavrh cdehrgwlpp nlfnctsvtf selkgfaerl
     2041 qrnesgldsg rsqrlalllr natqhtsgyf gsdvkvayql atrllahesa qrgfglsatq
     2101 dvhftenllr vgsalldaan krhweliqqt eggtawllqh yeayasalaq nmrhtylspf
     2161 tivtpnivis vvrldkgnfa gtklpryeal rgerppdlet tvilpesvfr emppmvrsag
     2221 pgeaqeteel arrqrrhpel sqgeavasvi iyhtlagllp hnydpdkrsl rvpkrpvint
     2281 pvvsisvhdd eellpraldk pvtvqfrlle teertkpicv fwnhsilvsg tggwsargce
     2341 vvfrneshvs cqcnhmtsfa vlmdvsrren geilplktlt yvalgvtlaa lmitflfltl
     2401 lralrsnqhg irrnltaalg laqlvfllgi nqadlpfact viaillhfly lctfswalle
     2461 alhlyralte vrdvnaspmr fyymlgwgvp afitglavgl dpegygnpdf cwlsiydtli
     2521 wsfagpvafa vsmsvflyil sarascaaqr qgfekkgpvs glrssftvll llsatwllal
     2581 lsvnsdtllf hylfaacncv qgpfiflsyv vlskevrkal kfacsrkpsp dpalttkstl
     2641 tssyncpspy adgrlyqpyg dsagslhsas rsgksqpsyi pfllreestl npgqvppglg
     2701 dpsglfmegq aqqhdpdtds dsdlsleddq sgsyasthss dseeeeeeaa fpgeqgwdsl
     2761 lgpgaerlpl hstpkdggpg sgkvpwpgdf gtttkensgs gpleerpren gdaltregsl
     2821 gplpgpstqp hkgilkkkcl ptisekssll rlpleqgtgs srgstasegs rngppprppp
     2881 rqslqeqlng vmpiamsika gtvdedssgs eflffnflh
//
LOCUS       NP_112402                466 aa            linear   ROD 28-APR-2025
DEFINITION  vimentin [Rattus norvegicus].
ACCESSION   NP_112402
VERSION     NP_112402.1
DBSOURCE    REFSEQ: accession NM_031140.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Zholudeva,A.O., Potapov,N.S., Kozlova,E.A., Lomakina,M.E. and
            Alexandrova,A.Y.
  TITLE     Impairment of Assembly of the Vimentin Intermediate Filaments Leads
            to Suppression of Formation and Maturation of Focal Contacts and
            Alteration of the Type of Cellular Protrusions
  JOURNAL   Biochemistry (Mosc) 89 (1), 184-195 (2024)
   PUBMED   38467554
  REMARK    GeneRIF: Impairment of Assembly of the Vimentin Intermediate
            Filaments Leads to Suppression of Formation and Maturation of Focal
            Contacts and Alteration of the Type of Cellular Protrusions.
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Coelho,N.R., Tomkiewicz,C., Correia,M.J., Goncalves-Dias,C.,
            Barouki,R., Pereira,S.A., Coumoul,X. and Monteiro,E.C.
  TITLE     First evidence of aryl hydrocarbon receptor as a druggable target
            in hypertension induced by chronic intermittent hypoxia
  JOURNAL   Pharmacol Res 159, 104869 (2020)
   PUBMED   32416216
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Liang,J.R. and Yang,H.
  TITLE     Ginkgolic acid (GA) suppresses gastric cancer growth by inducing
            apoptosis and suppressing STAT3/JAK2 signaling regulated by ROS
  JOURNAL   Biomed Pharmacother 125, 109585 (2020)
   PUBMED   32106377
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Vakhrusheva,A., Endzhievskaya,S., Zhuikov,V., Nekrasova,T.,
            Parshina,E., Ovsiannikova,N., Popov,V., Bagrov,D., Minin
            Acapital,A. Cyrillic and Sokolova,O.S.
  TITLE     The role of vimentin in directional migration of rat fibroblasts
  JOURNAL   Cytoskeleton (Hoboken) 76 (9-10), 467-476 (2019)
   PUBMED   31626376
  REMARK    GeneRIF: The role of vimentin in directional migration of rat
            fibroblasts.
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Zhu,W.B., Zhao,Z.F. and Zhou,X.
  TITLE     AMD3100 inhibits epithelial-mesenchymal transition, cell invasion,
            and metastasis in the liver and the lung through blocking the
            SDF-1alpha/CXCR4 signaling pathway in prostate cancer
  JOURNAL   J Cell Physiol 234 (7), 11746-11759 (2019)
   PUBMED   30537000
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Bussemakers,M.J., Verhaegh,G.W., van Bokhoven,A., Debruyne,F.M. and
            Schalken,J.A.
  TITLE     Differential expression of vimentin in rat prostatic tumors
  JOURNAL   Biochem Biophys Res Commun 182 (3), 1254-1259 (1992)
   PUBMED   1540169
REFERENCE   7  (residues 1 to 466)
  AUTHORS   Bussemakers,M.J., van Bokhoven,A., van Groningen,J.J.,
            Debruyne,F.M. and Schalken,J.A.
  TITLE     Increased expression of retroviral sequences in progressionally
            advanced rat prostatic tumors
  JOURNAL   Biochem Biophys Res Commun 182 (1), 318-324 (1992)
   PUBMED   1370615
REFERENCE   8  (residues 1 to 466)
  AUTHORS   Monteiro,M.J. and Cleveland,D.W.
  TITLE     Expression of NF-L and NF-M in fibroblasts reveals coassembly of
            neurofilament and vimentin subunits
  JOURNAL   J Cell Biol 108 (2), 579-593 (1989)
   PUBMED   2493000
REFERENCE   9  (residues 1 to 466)
  AUTHORS   Akoglu,T., Kozakoglu,H. and Akoglu,E.
  TITLE     Antibody to intermediate filaments of the cytoskeleton in patients
            with Behcet's disease
  JOURNAL   Clin Immunol Immunopathol 41 (3), 427-432 (1986)
   PUBMED   3780056
REFERENCE   10 (residues 1 to 466)
  AUTHORS   Kurki,P., Helve,T. and Virtanen,I.
  TITLE     Antibodies to cytoplasmic intermediate filaments in rheumatic
            diseases
  JOURNAL   J Rheumatol 10 (4), 558-562 (1983)
   PUBMED   6352937
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X62952.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X62952.1, BC061847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Rattus norvegicus"
                     /strain="Fischer Copenhagen"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17q12.3"
     Protein         1..466
                     /product="vimentin"
                     /calculated_mol_wt=53602
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Region          2..95
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            7
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKC, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          14..101
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            33
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            34
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine, alternate.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2, PKA, PKC and ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12686602; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKC.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          96..131
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Region          102..410
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            129
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          132..153
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          154..245
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            188
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            223
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          246..268
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Region          269..407
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            294
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P20152; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          326..329
                     /region_name="[IL]-x-C-x-x-[DE] motif.
                     /evidence=ECO:0000250|UniProtKB:P08670"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            351
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            373
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Region          408..466
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P31000.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            445
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08670; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31000.2)"
     CDS             1..466
                     /gene="Vim"
                     /coded_by="NM_031140.1:81..1481"
                     /db_xref="GeneID:81818"
                     /db_xref="RGD:621646"
ORIGIN      
        1 mstrsvssss yrrmfggsgt ssrpssnrsy vttstrtysl gsalrpstsr slyssspgga
       61 yvtrssavrl rssmpgvrll qdsvdfslad aintefkntr tnekvelqel ndrfanyidk
      121 vrfleqqnki llaeleqlkg qgksrlgdly eeemrelrrq vdqltndkar veverdnlae
      181 dimrlreklq eemlqreeae stlqsfrqdv dnaslarldl erkveslqee iaflkklhde
      241 eiqelqaqiq eqhvqidvdv skpdltaalr dvrqqyesva aknlqeaeew ykskfadlse
      301 aanrnndalr qakqesneyr rqvqsltcev dalkgtnesl erqmremeen faleaanyqd
      361 tigrlqdeiq nmkeemarhl reyqdllnvk maldieiaty rkllegeesr islplpnfss
      421 lnlretnles lplvdthskr tlliktvetr dgqvinetsq hhddle
//
LOCUS       NP_001025088             297 aa            linear   ROD 28-APR-2025
DEFINITION  protein MEMO1 [Rattus norvegicus].
ACCESSION   NP_001025088 XP_216638
VERSION     NP_001025088.1
DBSOURCE    REFSEQ: accession NM_001029917.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Zaoui,K., Benseddik,K., Daou,P., Salaun,D. and Badache,A.
  TITLE     ErbB2 receptor controls microtubule capture by recruiting ACF7 to
            the plasma membrane of migrating cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (43), 18517-18522 (2010)
   PUBMED   20937854
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098061.1.
            
            On Jul 29, 2005 this sequence version replaced XP_216638.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098061.1, SRR8487226.149576.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..297
                     /product="protein MEMO1"
                     /note="protein memo; mediator of ErbB2-driven cell
                     motility 1; memo-1"
                     /calculated_mol_wt=33548
     Region          9..294
                     /region_name="MEMO_like"
                     /note="Memo (mediator of ErbB2-driven cell motility) is
                     co-precipitated with the C terminus of ErbB2, a protein
                     involved in cell motility; cd07361"
                     /db_xref="CDD:153373"
     Site            order(16,49,81,131,189,192,244)
                     /site_type="active"
                     /note="putative ligand binding pocket/active site
                     [active]"
                     /db_xref="CDD:153373"
     Site            order(49,81)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:153373"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q91VH6; propagated from
                     UniProtKB/Swiss-Prot (Q4QQR9.1)"
     CDS             1..297
                     /gene="Memo1"
                     /gene_synonym="RGD1309929"
                     /coded_by="NM_001029917.1:27..920"
                     /db_xref="GeneID:298787"
                     /db_xref="RGD:1309929"
ORIGIN      
        1 msnrvvcrea shagswytas gpqlnaqleg wlsqvqstkr paraiiapha gytycgscaa
       61 haykqvdpsi trrifilgps hhvplsrcal ssvdiyrtpl ydlridqkiy gelwktgmfe
      121 rmslqtdede hsiemhlpyt akameshkde ftiipvlvga lseskeqefg klfskyladp
      181 snlfvvssdf chwgqrfrys yydesqgeiy rsiehldkmg msiieqldpv sfsnylkkyh
      241 nticgrhpig vllnaitelq ksgmnmsfsf lnyaqssqcr swqdssvsya agaltvh
//
LOCUS       NP_445870                307 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin recognition factor in ER-associated degradation protein 1
            [Rattus norvegicus].
ACCESSION   NP_445870
VERSION     NP_445870.1
DBSOURCE    REFSEQ: accession NM_053418.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Hao,Q., Jiao,S., Shi,Z., Li,C., Meng,X., Zhang,Z., Wang,Y.,
            Song,X., Wang,W., Zhang,R., Zhao,Y., Wong,C.C. and Zhou,Z.
  TITLE     A non-canonical role of the p97 complex in RIG-I antiviral
            signaling
  JOURNAL   EMBO J 34 (23), 2903-2920 (2015)
   PUBMED   26471729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Zhong,Y., Shen,H., Wang,Y., Yang,Y., Yang,P. and Fang,S.
  TITLE     Identification of ERAD components essential for dislocation of the
            null Hong Kong variant of alpha-1-antitrypsin (NHK)
  JOURNAL   Biochem Biophys Res Commun 458 (2), 424-428 (2015)
   PUBMED   25660456
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Chen,S.F., Wu,C.H., Lee,Y.M., Tam,K., Tsai,Y.C., Liou,J.Y. and
            Shyue,S.K.
  TITLE     Caveolin-1 interacts with Derlin-1 and promotes ubiquitination and
            degradation of cyclooxygenase-2 via collaboration with p97 complex
  JOURNAL   J Biol Chem 288 (46), 33462-33469 (2013)
   PUBMED   24089527
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Bebeacua,C., Forster,A., McKeown,C., Meyer,H.H., Zhang,X. and
            Freemont,P.S.
  TITLE     Distinct conformations of the protein complex p97-Ufd1-Npl4
            revealed by electron cryomicroscopy
  JOURNAL   Proc Natl Acad Sci U S A 109 (4), 1098-1103 (2012)
   PUBMED   22232657
REFERENCE   5  (residues 1 to 307)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   7  (residues 1 to 307)
  AUTHORS   De Luca,A., Pasini,A., Amati,F., Botta,A., Spalletta,G.,
            Alimenti,S., Caccamo,F., Conti,E., Trakalo,J., Macciardi,F.,
            Dallapiccola,B. and Novelli,G.
  TITLE     Association study of a promoter polymorphism of UFD1L gene with
            schizophrenia
  JOURNAL   Am J Med Genet 105 (6), 529-533 (2001)
   PUBMED   11496370
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Chung,M.Y., Lu,J.H., Weng,Y.Y. and Hwang,B.
  TITLE     Absence of mutations in human ubiquitin fusion-degradation protein
            gene in tetralogy of Fallot
  JOURNAL   J Mol Med (Berl) 79 (5-6), 338-342 (2001)
   PUBMED   11485030
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Yamagishi,H., Garg,V., Matsuoka,R., Thomas,T. and Srivastava,D.
  TITLE     A molecular pathway revealing a genetic basis for human cardiac and
            craniofacial defects
  JOURNAL   Science 283 (5405), 1158-1161 (1999)
   PUBMED   10024240
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK599711.1, AF234601.1 and BC061998.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161818.1, CF110642.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q23"
     Protein         1..307
                     /product="ubiquitin recognition factor in ER-associated
                     degradation protein 1"
                     /note="UB fusion protein 1; ubiquitin fusion degradation
                     protein 1 homolog; ubiquitin fusion degradation 1 like"
                     /calculated_mol_wt=34354
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q92890; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     Region          19..192
                     /region_name="UFD1"
                     /note="Ubiquitin fusion degradation protein UFD1;
                     pfam03152"
                     /db_xref="CDD:460828"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92890; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     Region          230..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES53.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92890; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92890; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92890; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     Region          282..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ES53.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9ES53.1)"
     CDS             1..307
                     /gene="Ufd1"
                     /coded_by="NM_053418.2:96..1019"
                     /db_xref="GeneID:84478"
                     /db_xref="RGD:619822"
ORIGIN      
        1 mfsfnmfdhp iprvfqnrfs tqyrcfsvsm lagpndrsdv ekggkiimpp saldqlsrln
       61 itypmlfklt nknsdrmthc gvlefvadeg icylphwmmq nllleegglv qvesvnlqva
      121 tyskfqpqsp dflditnpka vlenalrnfa clttgdviai nynekiyelr vmetkpdkav
      181 siiecdmnvd fdaplgykep erpvqheesi egeadhsgya gevgfrafsg sgnrldgkkk
      241 gvepspspik pgdikrgipn yefklgkitf irnsrpmvkk veedeaggrf vafsgegqsl
      301 rkkgrkp
//
LOCUS       NP_001100976            1038 aa            linear   ROD 28-APR-2025
DEFINITION  teashirt homolog 3 [Rattus norvegicus].
ACCESSION   NP_001100976 XP_001079868 XP_218516
VERSION     NP_001100976.1
DBSOURCE    REFSEQ: accession NM_001107506.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Caubit,X., Gubellini,P., Andrieux,J., Roubertoux,P.L., Metwaly,M.,
            Jacq,B., Fatmi,A., Had-Aissouni,L., Kwan,K.Y., Salin,P.,
            Carlier,M., Lieden,A., Rudd,E., Shinawi,M., Vincent-Delorme,C.,
            Cuisset,J.M., Lemaitre,M.P., Abderrehamane,F., Duban,B.,
            Lemaitre,J.F., Woolf,A.S., Bockenhauer,D., Severac,D., Dubois,E.,
            Zhu,Y., Sestan,N., Garratt,A.N., Lydia Kerkerian-Le,Goff. and
            Fasano,L.
  TITLE     TSHZ3 deletion causes an autism syndrome and defects in cortical
            projection neurons
  JOURNAL   Nat Genet 48 (11), 1359-1369 (2016)
   PUBMED   27668656
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Caubit,X., Thoby-Brisson,M., Voituron,N., Filippi,P., Bevengut,M.,
            Faralli,H., Zanella,S., Fortin,G., Hilaire,G. and Fasano,L.
  TITLE     Teashirt 3 regulates development of neurons involved in both
            respiratory rhythm and airflow control
  JOURNAL   J Neurosci 30 (28), 9465-9476 (2010)
   PUBMED   20631175
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Kajiwara,Y., Akram,A., Katsel,P., Haroutunian,V., Schmeidler,J.,
            Beecham,G., Haines,J.L., Pericak-Vance,M.A. and Buxbaum,J.D.
  TITLE     FE65 binds Teashirt, inhibiting expression of the primate-specific
            caspase-4
  JOURNAL   PLoS One 4 (4), e5071 (2009)
   PUBMED   19343227
REFERENCE   4  (residues 1 to 1038)
  AUTHORS   Caubit,X., Lye,C.M., Martin,E., Core,N., Long,D.A., Vola,C.,
            Jenkins,D., Garratt,A.N., Skaer,H., Woolf,A.S. and Fasano,L.
  TITLE     Teashirt 3 is necessary for ureteral smooth muscle differentiation
            downstream of SHH and BMP4
  JOURNAL   Development 135 (19), 3301-3310 (2008)
   PUBMED   18776146
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001079868.1, XP_218516.3.
            
            ##Evidence-Data-START##
            CDS exon combination :: BF567083.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5756307, SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..1038
                     /product="teashirt homolog 3"
                     /note="zinc finger protein 537; teashirt zinc finger
                     family member 3"
                     /calculated_mol_wt=113695
     Region          172..194
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(179..181,183..184,188,193,238,241..245,247..248)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          233..255
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          849..917
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(849..853,855,879,889,902,904..905,908..909,911..913,
                     915..916)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(851,854,905,908..909,912)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     CDS             1..1038
                     /gene="Tshz3"
                     /gene_synonym="Zfp537"
                     /coded_by="NM_001107506.1:130..3246"
                     /db_xref="GeneID:308523"
                     /db_xref="RGD:1306322"
ORIGIN      
        1 mcpekelska cpsyqnspaa efsshemdse shisetsdrm adfesssikn eeetkevqvp
       61 ledttvsdsl eqmkavynnf lsnsywsnln lnlhqpssen ngggssssss ssssscgsgs
      121 fdwhqsamak tlqqvsqnrm lpepslfstv qlyrqsskly gsiftgaskf rckdcsaayd
      181 tlveltvhmn etghyrddnh etdnnnpkrw skprkrslle megkedaqkv lkcmycghsf
      241 eslqdlsvhm iktkhyqkvp lkepvtpvaa kiipaarkkp slelelpssp dstggtpkat
      301 lsdasdalqk nsnpyitpnn ryghqngasy awhfearksq ilkcmecgss hdtlqeltah
      361 mmvtghfikv tnsamkkgkp imetpvtpti ttlldekvqs vplaattfts psntpasvsp
      421 kltveikkev dkekavldek pkekekasee eekydissky hyltendlee spkggldilk
      481 slentvtsai nkaqngtpsw ggypsihaay qlpnmmklsl gssgkstplk pmfgnseivs
      541 ptktqtlvsp pssqtspmpk tnfhameelv kkvtekvakv eekmkepdsk lsppkratps
      601 pcsseqsepi kmeassgsgf ksqenspspp rdvckeasps aepvengkel vkplsggsls
      661 gstaiitdhp peqpfvnpls alqsvmnihl gkaakpslpa ldpmsmlfkm snslaekaav
      721 atppplqakk aehldryfyh vnndqpidlt kgksdkgcsl gsgllsptst spatssstvt
      781 taktsavvsf msnsplrena lsdisdmlkn lteshtskss tpssiseksd idgatleeae
      841 estpaqkrkg rqsnwnpqhl lilqaqfaas lrqtsegkyi msdlspqerm hisrftglsm
      901 ttishwlanv kyqlrrtggt kflknldtgh pvffcndcas qirtpstyis hleshlgfrl
      961 rdlsklsteq innqiaqtks psekmvtssp eedlgttyqc klcnrtfask havklhlskt
     1021 hgkspedhll fvselekq
//
LOCUS       NP_037187                888 aa            linear   ROD 28-APR-2025
DEFINITION  mitogen-activated protein kinase kinase kinase 12 [Rattus
            norvegicus].
ACCESSION   NP_037187
VERSION     NP_037187.1
DBSOURCE    REFSEQ: accession NM_013055.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Tenenbaum,M., Plaisance,V., Boutry,R., Pawlowski,V., Jacovetti,C.,
            Sanchez-Parra,C., Ezanno,H., Bourry,J., Beeler,N., Pasquetti,G.,
            Gmyr,V., Dalle,S., Kerr-Conte,J., Pattou,F., Hirai,S.I.,
            Regazzi,R., Bonnefond,A., Froguel,P. and Abderrahmani,A.
  TITLE     The Map3k12 (Dlk)/JNK3 signaling pathway is required for pancreatic
            beta-cell proliferation during postnatal development
  JOURNAL   Cell Mol Life Sci 78 (1), 287-298 (2021)
   PUBMED   32189007
  REMARK    GeneRIF: The Map3k12 (Dlk)/JNK3 signaling pathway is required for
            pancreatic beta-cell proliferation during postnatal development.
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Huang,Y.A., Zhou,B., Wernig,M. and Sudhof,T.C.
  TITLE     ApoE2, ApoE3, and ApoE4 Differentially Stimulate APP Transcription
            and Abeta Secretion
  JOURNAL   Cell 168 (3), 427-441 (2017)
   PUBMED   28111074
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Chen,M., Geoffroy,C.G., Wong,H.N., Tress,O., Nguyen,M.T.,
            Holzman,L.B., Jin,Y. and Zheng,B.
  TITLE     Leucine Zipper-bearing Kinase promotes axon growth in mammalian
            central nervous system neurons
  JOURNAL   Sci Rep 6, 31482 (2016)
   PUBMED   27511108
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Holland,S.M., Collura,K.M., Ketschek,A., Noma,K., Ferguson,T.A.,
            Jin,Y., Gallo,G. and Thomas,G.M.
  TITLE     Palmitoylation controls DLK localization, interactions and activity
            to ensure effective axonal injury signaling
  JOURNAL   Proc Natl Acad Sci U S A 113 (3), 763-768 (2016)
   PUBMED   26719418
  REMARK    GeneRIF: These findings explain how DLK specifically mediates nerve
            injury responses and reveal a novel cellular mechanism that ensures
            the specificity of neuronal kinase signaling.
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Itoh,T., Horiuchi,M., Ikeda,R.H. Jr., Xu,J., Bannerman,P.,
            Pleasure,D., Penninger,J.M., Tournier,C. and Itoh,A.
  TITLE     ZPK/DLK and MKK4 form the critical gateway to axotomy-induced
            motoneuron death in neonates
  JOURNAL   J Neurosci 34 (32), 10729-10742 (2014)
   PUBMED   25100604
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Ganguly,A., Oo,T.F., Rzhetskaya,M., Pratt,R., Yarygina,O.,
            Momoi,T., Kholodilov,N. and Burke,R.E.
  TITLE     CEP11004, a novel inhibitor of the mixed lineage kinases,
            suppresses apoptotic death in dopamine neurons of the substantia
            nigra induced by 6-hydroxydopamine
  JOURNAL   J Neurochem 88 (2), 469-480 (2004)
   PUBMED   14690535
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Hirai,S., Kawaguchi,A., Hirasawa,R., Baba,M., Ohnishi,T. and
            Ohno,S.
  TITLE     MAPK-upstream protein kinase (MUK) regulates the radial migration
            of immature neurons in telencephalon of mouse embryo
  JOURNAL   Development 129 (19), 4483-4495 (2002)
   PUBMED   12223406
  REMARK    GeneRIF: MUK/DLK/ZPK, and JNK activity increase potently and
            temporally in newly generated neurons in developing mouse
            telencephalon during radial migration
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Mata,M., Merritt,S.E., Fan,G., Yu,G.G. and Holzman,L.B.
  TITLE     Characterization of dual leucine zipper-bearing kinase, a mixed
            lineage kinase present in synaptic terminals whose phosphorylation
            state is regulated by membrane depolarization via calcineurin
  JOURNAL   J Biol Chem 271 (28), 16888-16896 (1996)
   PUBMED   8663324
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Hirai,S., Izawa,M., Osada,S., Spyrou,G. and Ohno,S.
  TITLE     Activation of the JNK pathway by distantly related protein kinases,
            MEKK and MUK
  JOURNAL   Oncogene 12 (3), 641-650 (1996)
   PUBMED   8637721
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Holzman,L.B., Merritt,S.E. and Fan,G.
  TITLE     Identification, molecular cloning, and characterization of dual
            leucine zipper bearing kinase. A novel serine/threonine protein
            kinase that defines a second subfamily of mixed lineage kinases
  JOURNAL   J Biol Chem 269 (49), 30808-30817 (1994)
   PUBMED   7983011
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D49785.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D49785.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..888
                     /product="mitogen-activated protein kinase kinase kinase
                     12"
                     /EC_number="2.7.11.25"
                     /note="dual leucine zipper kinase; MAPK-upstream kinase;
                     mixed lineage kinase; leucine-zipper protein kinase; dual
                     leucine zipper bearing kinase; Zipper (leucine) protein
                     kinase; Mitogen activated protein kinase 12 (Zipper
                     (leucine) protein kinase)"
                     /calculated_mol_wt=96177
     Region          26..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60700; propagated from
                     UniProtKB/Swiss-Prot (Q63796.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60700; propagated from
                     UniProtKB/Swiss-Prot (Q63796.1)"
     Region          164..400
                     /region_name="STKc_MAP3K12_13"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13;
                     cd14059"
                     /db_xref="CDD:270961"
     Site            order(164..168,172,183,185,207,223..226,230,232,269,271,
                     273..274,276,287,290,305..308)
                     /site_type="active"
                     /db_xref="CDD:270961"
     Site            order(164..168,172,183,185,207,223..226,230,269,271,
                     273..274,276,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270961"
     Site            order(168,230,232,269,271,273,290,305..308)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270961"
     Site            286..308
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270961"
     Region          423..444
                     /region_name="Leucine-zipper 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     Region          476..497
                     /region_name="Leucine-zipper 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     Region          557..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60700; propagated from
                     UniProtKB/Swiss-Prot (Q63796.1)"
     Region          654..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     Region          743..888
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63796.1)"
     CDS             1..888
                     /gene="Map3k12"
                     /gene_synonym="DLK; MUK; PK; Zpk"
                     /coded_by="NM_013055.1:451..3117"
                     /db_xref="GeneID:25579"
                     /db_xref="RGD:3988"
ORIGIN      
        1 maclhetrtp spsfggfvst lseasmrkld pdtsdctpek dltptqcvlr dvvplggqgg
       61 ggpspspgge pppepfansv lqlheqdtgg pggatgspes rasrvradev rlqcqsgsgf
      121 leglfgclrp vwtmigkays tehkqqqedl wevpfeeild lqwvgsgaqg avflgrfhge
      181 evavkkvrdl ketdikhlrk lkhpniitfk gvctqapcyc ilmefcaqgq lyevlragrp
      241 vtpsllvdws mgiaggmnyl hlhkiihrdl kspnmlityd dvvkisdfgt skelsdkstk
      301 msfagtvawm apevirnepv sekvdiwsfg vvlwelltge ipykdvdssa iiwgvgsnsl
      361 hlpvpsscpd gfkillrqcw nrkprnrpsf rqillhldia sadvlstpqe tyfksqaewr
      421 eevklhfeki ksegtclhrl eeelvmrrre elrhaldire hyerkleran nlymelnalm
      481 lqlelkerel lrreqalerr cpgllkshts rsllhgntme klikkrnvpq klsphskrpd
      541 ilktesllpk ldaalsgvgl pgcpkappsp grsrrgktrh rkasakgscg dlpglraalp
      601 phepgglgsp gglgvgptaw dasppalrgl hhdlllrkms ssspdllsaa lgargrgatg
      661 gardpgsppp pqgdtppseg sapgstspds pggakgeppp pvgpgegvgl lgtgregttg
      721 rggsragyqh ltpaallyra avtrsqkrgi sseeeegevd sevelppsqr wpqgpnmrqs
      781 lstfssenps dveegtasep spsgtpevgs tntderpder sddmcsqgse ipldlptsev
      841 vperetsslp mqhqddqgpn pedsdcdste ldnsnsidal pppaslpp
//
LOCUS       NP_075589                217 aa            linear   ROD 28-APR-2025
DEFINITION  vesicle transport through interaction with t-SNAREs homolog 1A
            [Rattus norvegicus].
ACCESSION   NP_075589 XP_346592
VERSION     NP_075589.1
DBSOURCE    REFSEQ: accession NM_023101.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Milochau,A., Lagree,V., Benassy,M.N., Chaignepain,S., Papin,J.,
            Garcia-Arcos,I., Lajoix,A., Monterrat,C., Coudert,L.,
            Schmitter,J.M., Ochoa,B. and Lang,J.
  TITLE     Synaptotagmin 11 interacts with components of the RNA-induced
            silencing complex RISC in clonal pancreatic beta-cells
  JOURNAL   FEBS Lett 588 (14), 2217-2222 (2014)
   PUBMED   24882364
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Wilhelm,B.G., Mandad,S., Truckenbrodt,S., Krohnert,K., Schafer,C.,
            Rammner,B., Koo,S.J., Classen,G.A., Krauss,M., Haucke,V., Urlaub,H.
            and Rizzoli,S.O.
  TITLE     Composition of isolated synaptic boutons reveals the amounts of
            vesicle trafficking proteins
  JOURNAL   Science 344 (6187), 1023-1028 (2014)
   PUBMED   24876496
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Lu,Y., Zhang,Z., Sun,D., Sweeney,S.T. and Gao,F.B.
  TITLE     Syntaxin 13, a genetic modifier of mutant CHMP2B in frontotemporal
            dementia, is required for autophagosome maturation
  JOURNAL   Mol Cell 52 (2), 264-271 (2013)
   PUBMED   24095276
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Shitara,A., Shibui,T., Okayama,M., Arakawa,T., Mizoguchi,I.,
            Sakakura,Y. and Takuma,T.
  TITLE     VAMP4 is required to maintain the ribbon structure of the Golgi
            apparatus
  JOURNAL   Mol Cell Biochem 380 (1-2), 11-21 (2013)
   PUBMED   23677696
  REMARK    Erratum:[Mol Cell Biochem. 2013 Aug;380(1-2):301. Shakakura,
            Yasunori [corrected to Sakakura, Yasunori]]
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Bourassa,C.V., Meijer,I.A., Merner,N.D., Grewal,K.K.,
            Stefanelli,M.G., Hodgkinson,K., Ives,E.J., Pryse-Phillips,W.,
            Jog,M., Boycott,K., Grimes,D.A., Goobie,S., Leckey,R., Dion,P.A.
            and Rouleau,G.A.
  TITLE     VAMP1 mutation causes dominant hereditary spastic ataxia in
            Newfoundland families
  JOURNAL   Am J Hum Genet 91 (3), 548-552 (2012)
   PUBMED   22958904
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Tai,G., Lu,L., Wang,T.L., Tang,B.L., Goud,B., Johannes,L. and
            Hong,W.
  TITLE     Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in
            transport from the early/recycling endosome to the trans-Golgi
            network
  JOURNAL   Mol Biol Cell 15 (9), 4011-4022 (2004)
   PUBMED   15215310
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Kreykenbohm,V., Wenzel,D., Antonin,W., Atlachkine,V. and von
            Mollard,G.F.
  TITLE     The SNAREs vti1a and vti1b have distinct localization and SNARE
            complex partners
  JOURNAL   Eur J Cell Biol 81 (5), 273-280 (2002)
   PUBMED   12067063
  REMARK    GeneRIF: Data describe a novel SNARE complex containing vti1a and
            vti1b, found on small synaptic vesicles and clathrin-coated
            vesicles isolated from nerve terminals.
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Antonin,W., Fasshauer,D., Becker,S., Jahn,R. and Schneider,T.R.
  TITLE     Crystal structure of the endosomal SNARE complex reveals common
            structural principles of all SNAREs
  JOURNAL   Nat Struct Biol 9 (2), 107-111 (2002)
   PUBMED   11786915
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Antonin,W., Holroyd,C., Fasshauer,D., Pabst,S., Von Mollard,G.F.
            and Jahn,R.
  TITLE     A SNARE complex mediating fusion of late endosomes defines
            conserved properties of SNARE structure and function
  JOURNAL   EMBO J 19 (23), 6453-6464 (2000)
   PUBMED   11101518
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Antonin,W., Riedel,D. and von Mollard,G.F.
  TITLE     The SNARE Vti1a-beta is localized to small synaptic vesicles and
            participates in a novel SNARE complex
  JOURNAL   J Neurosci 20 (15), 5724-5732 (2000)
   PUBMED   10908612
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF262221.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346592.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF262221.1, SRR8487231.156339.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q55"
     Protein         1..217
                     /product="vesicle transport through interaction with
                     t-SNAREs homolog 1A"
                     /note="vti1-rp2; vesicle transport v-SNARE protein
                     Vti1-like 2; SNARE Vti1a-beta protein"
                     /calculated_mol_wt=25030
     Region          12..90
                     /region_name="V-SNARE"
                     /note="Vesicle transport v-SNARE protein N-terminus;
                     pfam05008"
                     /db_xref="CDD:461516"
     Region          122..183
                     /region_name="SNARE_Vti1a"
                     /note="SNARE motif of Vti1b-like; cd15891"
                     /db_xref="CDD:277244"
     Site            order(127..128,131..132,134..136,138..143,145..147,
                     149..150,152..153,156..157,159..164,166..168,170..171,
                     173..178,180..181)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277244"
     Site            156
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277244"
     CDS             1..217
                     /gene="Vti1a"
                     /gene_synonym="DD6A4-2(1); Vti1"
                     /coded_by="NM_023101.1:26..679"
                     /db_xref="GeneID:65277"
                     /db_xref="RGD:621490"
ORIGIN      
        1 msadfegyeq dfavltaeit skisrvprlp pdekkqmvan vekqleeare lleqmdlevr
       61 eippqsrgmy snrmrsykqe mgkletdfkr sriaysdevr nellgdagns senqrahlld
      121 nterlerssr rleagyqiav eteqigqeml enlshdreri qrarerlret danlgkssri
      181 ltgmlrriiq nrillvilgi ivvitiltai tffvrgh
//
LOCUS       NP_001009689             214 aa            linear   ROD 28-APR-2025
DEFINITION  cdc42 effector protein 2 [Rattus norvegicus].
ACCESSION   NP_001009689 XP_219523
VERSION     NP_001009689.1
DBSOURCE    REFSEQ: accession NM_001009689.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Trost,M., English,L., Lemieux,S., Courcelles,M., Desjardins,M. and
            Thibault,P.
  TITLE     The phagosomal proteome in interferon-gamma-activated macrophages
  JOURNAL   Immunity 30 (1), 143-154 (2009)
   PUBMED   19144319
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Joberty,G., Perlungher,R.R. and Macara,I.G.
  TITLE     The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
            proteins
  JOURNAL   Mol Cell Biol 19 (10), 6585-6597 (1999)
   PUBMED   10490598
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Burbelo,P.D., Snow,D.M., Bahou,W. and Spiegel,S.
  TITLE     MSE55, a Cdc42 effector protein, induces long cellular extensions
            in fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 96 (16), 9083-9088 (1999)
   PUBMED   10430899
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087091.1.
            
            On Jan 13, 2005 this sequence version replaced XP_219523.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087091.1, CK601352.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN11044071 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..214
                     /product="cdc42 effector protein 2"
                     /note="binder of Rho GTPases 1; CDC42 effector protein
                     (Rho GTPase binding) 2"
                     /calculated_mol_wt=22917
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O14613; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Region          29..87
                     /region_name="CRIB"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cl00113"
                     /db_xref="CDD:412170"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14613; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Region          103..206
                     /region_name="BORG_CEP"
                     /note="Cdc42 effector; pfam14957"
                     /db_xref="CDD:464403"
     Region          118..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZX9; propagated from
                     UniProtKB/Swiss-Prot (Q5PQP4.1)"
     CDS             1..214
                     /gene="Cdc42ep2"
                     /coded_by="NM_001009689.1:237..881"
                     /db_xref="GeneID:309175"
                     /db_xref="RGD:1310253"
ORIGIN      
        1 mstkvpiylk rgsrkgkkek lrdllssdmi spplgdfrht ihigsgggdd mfgdisflqg
       61 kfhllpgtav eeaeedgsfd lpfqftrttt vcgrelpggl spllknaisl pviggpqalt
      121 lpttqappkp prlhlespqp spksspqeag nvdiwrvpea glphngmspe peaeepflsh
      181 assllslhvd lgpsilddvl qimdqdlgrv qipt
//
LOCUS       NP_599223                431 aa            linear   ROD 28-APR-2025
DEFINITION  calcium uptake protein 2, mitochondrial [Rattus norvegicus].
ACCESSION   NP_599223
VERSION     NP_599223.2
DBSOURCE    REFSEQ: accession NM_134396.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Vishnu,N., Hamilton,A., Bagge,A., Wernersson,A., Cowan,E.,
            Barnard,H., Sancak,Y., Kamer,K.J., Spegel,P., Fex,M., Tengholm,A.,
            Mootha,V.K., Nicholls,D.G. and Mulder,H.
  TITLE     Mitochondrial clearance of calcium facilitated by MICU2 controls
            insulin secretion
  JOURNAL   Mol Metab 51, 101239 (2021)
   PUBMED   33932586
  REMARK    GeneRIF: Mitochondrial clearance of calcium facilitated by MICU2
            controls insulin secretion.
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Matesanz-Isabel,J., Arias-del-Val,J., Alvarez-Illera,P.,
            Fonteriz,R.I., Montero,M. and Alvarez,J.
  TITLE     Functional roles of MICU1 and MICU2 in mitochondrial Ca(2+) uptake
  JOURNAL   Biochim Biophys Acta 1858 (6), 1110-1117 (2016)
   PUBMED   26903221
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Tsai,M.F., Phillips,C.B., Ranaghan,M., Tsai,C.W., Wu,Y.,
            Willliams,C. and Miller,C.
  TITLE     Dual functions of a small regulatory subunit in the mitochondrial
            calcium uniporter complex
  JOURNAL   Elife 5, e15545 (2016)
   PUBMED   27099988
  REMARK    Erratum:[Elife. 2017 Mar 02;6:e26228. doi: 10.7554/eLife.26228.
            PMID: 28253172]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Petrungaro,C., Zimmermann,K.M., Kuttner,V., Fischer,M., Dengjel,J.,
            Bogeski,I. and Riemer,J.
  TITLE     The Ca(2+)-Dependent Release of the Mia40-Induced MICU1-MICU2 Dimer
            from MCU Regulates Mitochondrial Ca(2+) Uptake
  JOURNAL   Cell Metab 22 (4), 721-733 (2015)
   PUBMED   26387864
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Patron,M., Checchetto,V., Raffaello,A., Teardo,E., Vecellio
            Reane,D., Mantoan,M., Granatiero,V., Szabo,I., De Stefani,D. and
            Rizzuto,R.
  TITLE     MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by
            exerting opposite effects on MCU activity
  JOURNAL   Mol Cell 53 (5), 726-737 (2014)
   PUBMED   24560927
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Sancak,Y., Markhard,A.L., Kitami,T., Kovacs-Bogdan,E., Kamer,K.J.,
            Udeshi,N.D., Carr,S.A., Chaudhuri,D., Clapham,D.E., Li,A.A.,
            Calvo,S.E., Goldberger,O. and Mootha,V.K.
  TITLE     EMRE is an essential component of the mitochondrial calcium
            uniporter complex
  JOURNAL   Science 342 (6164), 1379-1382 (2013)
   PUBMED   24231807
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Plovanich,M., Bogorad,R.L., Sancak,Y., Kamer,K.J., Strittmatter,L.,
            Li,A.A., Girgis,H.S., Kuchimanchi,S., De Groot,J., Speciner,L.,
            Taneja,N., Oshea,J., Koteliansky,V. and Mootha,V.K.
  TITLE     MICU2, a paralog of MICU1, resides within the mitochondrial
            uniporter complex to regulate calcium handling
  JOURNAL   PLoS One 8 (2), e55785 (2013)
   PUBMED   23409044
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Tsai,L.C., Chan,G.C., Nangle,S.N., Shimizu-Albergine,M.,
            Jones,G.L., Storm,D.R., Beavo,J.A. and Zweifel,L.S.
  TITLE     Inactivation of Pde8b enhances memory, motor performance, and
            protects against age-induced motor coordination decay
  JOURNAL   Genes Brain Behav 11 (7), 837-847 (2012)
   PUBMED   22925203
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Cros,N., Tkatchenko,A.V., Pisani,D.F., Leclerc,L., Leger,J.J.,
            Marini,J.F. and Dechesne,C.A.
  TITLE     Analysis of altered gene expression in rat soleus muscle atrophied
            by disuse
  JOURNAL   J Cell Biochem 83 (3), 508-519 (2001)
   PUBMED   11596118
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF327513.1, EV765275.1, BQ207114.1, DY317464.1, EX491796.1 and
            CV797964.1.
            
            On Oct 26, 2007 this sequence version replaced NP_599223.1.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF327513.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMD00132261,
                                    SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..431
                     /product="calcium uptake protein 2, mitochondrial"
                     /note="EF-hand domain-containing family member A1; EF hand
                     domain family A1; EF-hand domain family, member A1"
                     /calculated_mol_wt=49084
     Region          81..199
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          173..392
                     /region_name="EFh_MICU2"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 2, mitochondrial (MICU2) and similar
                     proteins; cd16174"
                     /db_xref="CDD:320082"
     Region          173..202
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320082"
     Site            order(182,184,186,193,372,374,376,383)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320082"
     Region          230..260
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320082"
     Region          326..355
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320082"
     Region          363..392
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320082"
     CDS             1..431
                     /gene="Micu2"
                     /gene_synonym="Efha1; RGD1309934; Smhs2"
                     /coded_by="NM_134396.2:12..1307"
                     /db_xref="GeneID:171433"
                     /db_xref="RGD:619739"
ORIGIN      
        1 maaaagrsar laawgerlrr glaaggravp srgplaaava gvalagagaa whhgrvkaaa
       61 restltglvq kndlgpiekl slrkqrfmqf sslehdgeyy mtprdflfsv mfermdrktl
      121 vkklakkdie dvlsgiqtar cgstffrdlg dkgvisytey lflltiltkp hsgfhvafkm
      181 ldadgnemie rkefvklqki iskqdgfktv ktneieyqep tvnepglntt lqvrffgkrg
      241 ekklhykefr rfmenlqtev qemeflqfsk glnfmrkedf aewllfftns enkdiywknv
      301 reklsvgesi sldefksfch ftthledfai amqmfslahr pvrlaefkra vkvatgqels
      361 nnlldtvfki fdldgdecls hgeflgvlkn rmhrglwvsq qqsvqeywkc vkkesikgvk
      421 eawkqagkgp f
//
LOCUS       NP_446434                130 aa            linear   ROD 28-APR-2025
DEFINITION  small ribosomal subunit protein uS8 [Rattus norvegicus].
ACCESSION   NP_446434 XP_212877
VERSION     NP_446434.1
DBSOURCE    REFSEQ: accession NM_053982.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Chen,R., He,J., Wang,C., Xu,M., An,N. and Bai,Y.
  TITLE     RPS15A Mediates PI3K/AKT Signaling-Induced Parathyroid Cell
            Proliferation in Rats with Secondary Hyperparathyroidism
  JOURNAL   Ann Clin Lab Sci 53 (2), 313-321 (2023)
   PUBMED   37094854
  REMARK    GeneRIF: RPS15A Mediates PI3K/AKT Signaling-Induced Parathyroid
            Cell Proliferation in Rats with Secondary Hyperparathyroidism.
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Yu,Y., Ji,H., Doudna,J.A. and Leary,J.A.
  TITLE     Mass spectrometric analysis of the human 40S ribosomal subunit:
            native and HCV IRES-bound complexes
  JOURNAL   Protein Sci 14 (6), 1438-1446 (2005)
   PUBMED   15883184
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Lian,Z., Liu,J., Li,L., Li,X., Tufan,N.L., Wu,M.C., Wang,H.Y.,
            Arbuthnot,P., Kew,M. and Feitelson,M.A.
  TITLE     Human S15a expression is upregulated by hepatitis B virus X protein
  JOURNAL   Mol Carcinog 40 (1), 34-46 (2004)
   PUBMED   15108328
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Chan,Y.L., Olvera,J., Paz,V. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein S15a
  JOURNAL   Biochem Biophys Res Commun 200 (3), 1498-1504 (1994)
   PUBMED   8185605
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Collatz,E., Ulbrich,N., Tsurugi,K., Lightfoot,H.N., MacKinlay,W.,
            Lin,A. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 40 S ribosomal subunit proteins Sa, Sc,
            S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18,
            S19, S20, S21, S26, S27', and S29
  JOURNAL   J Biol Chem 252 (24), 9071-9080 (1977)
   PUBMED   925037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X77953.1.
            
            On Dec 17, 2003 this sequence version replaced XP_212877.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X77953.1, FQ223930.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q35"
     Protein         1..130
                     /product="small ribosomal subunit protein uS8"
                     /EC_number="3.6.5.3"
                     /note="40S ribosomal protein S15a"
                     /calculated_mol_wt=14708
     Region          1..130
                     /region_name="PTZ00158"
                     /note="40S ribosomal protein S15A; Provisional"
                     /db_xref="CDD:185487"
     CDS             1..130
                     /gene="Rps15a"
                     /coded_by="NM_053982.1:10..402"
                     /db_xref="GeneID:117053"
                     /db_xref="RGD:619939"
ORIGIN      
        1 mvrmnvlada lksinnaekr gkrqvlirpc skvivrfltv mmkhgyigef eiiddhragk
       61 ivvnltgrln kcgvisprfd vqlkdlekwq nnllpsrqfg fivlttsagi mdheearrkh
      121 tggkilgfff
//
LOCUS       NP_037158                313 aa            linear   ROD 28-APR-2025
DEFINITION  syndecan-1 precursor [Rattus norvegicus].
ACCESSION   NP_037158
VERSION     NP_037158.1
DBSOURCE    REFSEQ: accession NM_013026.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Qin,L.L., Xue,F., Yin,F., Zhao,J. and Zhang,K.Y.
  TITLE     Expression of syndecan-1, PKC and VEGF in rats with acute kidney
            injury and correlation between syndecan-1 and renal function
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (24), 12794-12801 (2020)
   PUBMED   33378064
  REMARK    GeneRIF: Expression of syndecan-1, PKC and VEGF in rats with acute
            kidney injury and correlation between syndecan-1 and renal
            function.
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Jing,Z., Wei-Jie,Y., Yi-Feng,Z.G. and Jing,H.
  TITLE     Downregulation of Syndecan-1 induce glomerular endothelial cell
            dysfunction through modulating internalization of VEGFR-2
  JOURNAL   Cell Signal 28 (8), 826-837 (2016)
   PUBMED   27075925
  REMARK    GeneRIF: down-regulation of Syndecan-1 could inhibit VEGF-VEGFR-2
            signaling through regulating internalization of VEGFR-2.
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Torres Filho,I.P., Torres,L.N., Salgado,C. and Dubick,M.A.
  TITLE     Plasma syndecan-1 and heparan sulfate correlate with microvascular
            glycocalyx degradation in hemorrhaged rats after different
            resuscitation fluids
  JOURNAL   Am J Physiol Heart Circ Physiol 310 (11), H1468-H1478 (2016)
   PUBMED   27037369
  REMARK    GeneRIF: Plasma syndecan-1 and heparan sulfate correlate with
            microvascular glycocalyx degradation in hemorrhaged rats after
            different resuscitation fluids.
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Kwon,M.J., Park,J., Jang,S., Eom,C.Y. and Oh,E.S.
  TITLE     The Conserved Phenylalanine in the Transmembrane Domain Enhances
            Heteromeric Interactions of Syndecans
  JOURNAL   J Biol Chem 291 (2), 872-881 (2016)
   PUBMED   26601939
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Adepu,S., Rosman,C.W., Dam,W., van Dijk,M.C., Navis,G., van
            Goor,H., Bakker,S.J. and van den Born,J.
  TITLE     Incipient renal transplant dysfunction associates with tubular
            syndecan-1 expression and shedding
  JOURNAL   Am J Physiol Renal Physiol 309 (2), F137-F145 (2015)
   PUBMED   25972509
  REMARK    GeneRIF: expression upregulated two months after renal
            transplantation
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Larrain,J., Cizmeci-Smith,G., Troncoso,V., Stahl,R.C., Carey,D.J.
            and Brandan,E.
  TITLE     Syndecan-1 expression is down-regulated during myoblast terminal
            differentiation. Modulation by growth factors and retinoic acid
  JOURNAL   J Biol Chem 272 (29), 18418-18424 (1997)
   PUBMED   9218485
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Nakanishi,T., Kadomatsu,K., Okamoto,T., Ichihara-Tanaka,K.,
            Kojima,T., Saito,H., Tomoda,Y. and Muramatsu,T.
  TITLE     Expression of syndecan-1 and -3 during embryogenesis of the central
            nervous system in relation to binding with midkine
  JOURNAL   J Biochem 121 (2), 197-205 (1997)
   PUBMED   9089390
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Shworak,N.W., Kojima,T. and Rosenberg,R.D.
  TITLE     Isolation and characterization of ryudocan and syndecan heparan
            sulfate proteoglycans, core proteins, and cDNAs from a rat
            endothelial cell line
  JOURNAL   Haemostasis 23 Suppl 1, 161-176 (1993)
   PUBMED   8495865
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Cizmeci-Smith,G., Asundi,V., Stahl,R.C., Teichman,L.J.,
            Chernousov,M., Cowan,K. and Carey,D.J.
  TITLE     Regulated expression of syndecan in vascular smooth muscle cells
            and cloning of rat syndecan core protein cDNA
  JOURNAL   J Biol Chem 267 (22), 15729-15736 (1992)
   PUBMED   1639809
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Kojima,T., Shworak,N.W. and Rosenberg,R.D.
  TITLE     Molecular cloning and expression of two distinct cDNA-encoding
            heparan sulfate proteoglycan core proteins from a rat endothelial
            cell line
  JOURNAL   J Biol Chem 267 (7), 4870-4877 (1992)
   PUBMED   1537865
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061834.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061834.1, M81785.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..313
                     /product="syndecan-1 precursor"
                     /calculated_mol_wt=30669
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2563
     mat_peptide     23..313
                     /product="Syndecan-1. /id=PRO_0000033502"
                     /note="propagated from UniProtKB/Swiss-Prot (P26260.2)"
                     /calculated_mol_wt=30669
     Region          27..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26260.2)"
     Site            37
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P18828; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Site            45
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (heparan sulfate) serine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Site            47
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (heparan sulfate) serine.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Region          95..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26260.2)"
     Site            209
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P18827; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Site            219
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:P18828; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     Region          248..309
                     /region_name="Syndecan"
                     /note="Syndecan domain; pfam01034"
                     /db_xref="CDD:460035"
     Site            253..254
                     /site_type="cleavage"
                     /note="Cleavage of ectodomain. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P26260.2)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P26260.2)"
     Region          286..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26260.2)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18827; propagated from
                     UniProtKB/Swiss-Prot (P26260.2)"
     CDS             1..313
                     /gene="Sdc1"
                     /gene_synonym="HSPG; Synd1; SYNDECA; Syndecan"
                     /coded_by="NM_013026.2:209..1150"
                     /db_xref="GeneID:25216"
                     /db_xref="RGD:3648"
ORIGIN      
        1 mrraalwlwl calalrlqpa lpqivtanvp pedqdgsgdd sdnfsgsgtg alpdmtlsrq
       61 tpstwkdvwl ltatptapep tsrdteatlt silpagekpe egepvahvea epdftardke
      121 keattrpret tqlpvtqqas taarattaqa svtshphgdv qpglhetlap tapgqpdhqp
      181 psvedggtsv ikevvedett nqlpagegsg eqdftfetsg entavagvep dlrnqspvde
      241 gatgasqgll drkevlggvi agglvglifa vclvafmlyr mkkkdegsys leepkqangg
      301 ayqkptkqee fya
//
LOCUS       NP_071611                395 aa            linear   ROD 28-APR-2025
DEFINITION  neuromedin-U receptor 2 [Rattus norvegicus].
ACCESSION   NP_071611
VERSION     NP_071611.3
DBSOURCE    REFSEQ: accession NM_022275.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Vallof,D., Kalafateli,A.L. and Jerlhag,E.
  TITLE     Brain region-specific neuromedin U signalling regulates
            alcohol-related behaviours and food intake in rodents
  JOURNAL   Addict Biol 25 (3), e12764 (2020)
   PUBMED   31069918
  REMARK    GeneRIF: Brain region-specific neuromedin U signalling regulates
            alcohol-related behaviours and food intake in rodents.
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Peng,S., Lu,Y., Li,P., Liu,P., Shi,X., Liu,C., Zhang,Y., Liu,S. and
            Wang,J.
  TITLE     The short interference RNA (siRNA) targeting NMUR2 relieves
            nociception in a bone cancer pain model of rat through PKC-ERK and
            PI3K-AKT pathways
  JOURNAL   Biochem Biophys Res Commun 512 (3), 616-622 (2019)
   PUBMED   30914203
  REMARK    GeneRIF: NMUR2 is upregulated in bone cancer pain rat model. Short
            interference RNA NMUR2 alleviates nociception in bone cancer pain
            rat model.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   McCue,D.L., Kasper,J.M., A and Hommel,J.D.
  TITLE     Incubation of feeding behavior is regulated by neuromedin U
            receptor 2 in the paraventricular nucleus of the hypothalamus
  JOURNAL   Behav Brain Res 359, 763-770 (2019)
   PUBMED   30227148
  REMARK    GeneRIF: This study shown that modulation of neuromedin U receptor
            2 (NMUR2) in the paraventricular nucleus of the hypothalamus (PVN)
            results in increased food intake and motivation for energy-dense
            foods.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Benzon,C.R., Johnson,S.B., McCue,D.L., Li,D., Green,T.A. and
            Hommel,J.D.
  TITLE     Neuromedin U receptor 2 knockdown in the paraventricular nucleus
            modifies behavioral responses to obesogenic high-fat food and leads
            to increased body weight
  JOURNAL   Neuroscience 258, 270-279 (2014)
   PUBMED   24269937
  REMARK    GeneRIF: Results demonstrate that NMUR2 signaling in the
            paraventricular nucleus of the hypothalamus regulates consumption
            and preference for high-fat foods without disrupting feeding
            behavior associated with non-obesogenic standard chow
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Lin,T.Y., Wu,F.J., Lee,W.Y., Hsiao,C.L. and Luo,C.W.
  TITLE     Ovarian regulation of neuromedin U and its local actions in the
            ovary, mediated through neuromedin U receptor 2
  JOURNAL   Am J Physiol Endocrinol Metab 304 (8), E800-E809 (2013)
   PUBMED   23423171
  REMARK    GeneRIF: NMU and NMU receptor 2 compose a novel autocrine system in
            theca/interstitial cells in which the intensity of signaling is
            tightly controlled by gonadotropins.
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Qiu,D.L., Chu,C.P., Tsukino,H., Shirasaka,T., Nakao,H., Kato,K.,
            Kunitake,T., Katoh,T. and Kannan,H.
  TITLE     Neuromedin U receptor-2 mRNA and HCN channels mRNA expression in
            NMU-sensitive neurons in rat hypothalamic paraventricular nucleus
  JOURNAL   Neurosci Lett 374 (1), 69-72 (2005)
   PUBMED   15631899
  REMARK    GeneRIF: These results suggest that NMU modulates the function of
            the PVN putative parvocellular neurons and is involved in the
            regulation of OTergic and VPergic neurons by enhanced HCN ion
            channels activity via NMU-receptor 2.
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Yu,X.H., Cao,C.Q., Mennicken,F., Puma,C., Dray,A., O'Donnell,D.,
            Ahmad,S. and Perkins,M.
  TITLE     Pro-nociceptive effects of neuromedin U in rat
  JOURNAL   Neuroscience 120 (2), 467-474 (2003)
   PUBMED   12890516
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Raddatz,R., Wilson,A.E., Artymyshyn,R., Bonini,J.A., Borowsky,B.,
            Boteju,L.W., Zhou,S., Kouranova,E.V., Nagorny,R., Guevarra,M.S.,
            Dai,M., Lerman,G.S., Vaysse,P.J., Branchek,T.A., Gerald,C.,
            Forray,C. and Adham,N.
  TITLE     Identification and characterization of two neuromedin U receptors
            differentially expressed in peripheral tissues and the central
            nervous system
  JOURNAL   J Biol Chem 275 (42), 32452-32459 (2000)
   PUBMED   10899166
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Hosoya,M., Moriya,T., Kawamata,Y., Ohkubo,S., Fujii,R., Matsui,H.,
            Shintani,Y., Fukusumi,S., Habata,Y., Hinuma,S., Onda,H.,
            Nishimura,O. and Fujino,M.
  TITLE     Identification and functional characterization of a novel subtype
            of neuromedin U receptor
  JOURNAL   J Biol Chem 275 (38), 29528-29532 (2000)
   PUBMED   10887190
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Howard,A.D., Wang,R., Pong,S.S., Mellin,T.N., Strack,A., Guan,X.M.,
            Zeng,Z., Williams,D.L. Jr., Feighner,S.D., Nunes,C.N., Murphy,B.,
            Stair,J.N., Yu,H., Jiang,Q., Clements,M.K., Tan,C.P., McKee,K.K.,
            Hreniuk,D.L., McDonald,T.P., Lynch,K.R., Evans,J.F., Austin,C.P.,
            Caskey,C.T., Van der Ploeg,L.H. and Liu,Q.
  TITLE     Identification of receptors for neuromedin U and its role in
            feeding
  JOURNAL   Nature 406 (6791), 70-74 (2000)
   PUBMED   10894543
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1, AB041229.1, AF242875.1, CB556410.1 and
            BM384513.1.
            
            On Aug 2, 2012 this sequence version replaced NP_071611.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643429.36724.1, AB041229.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN17050745 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation, longest
                                                protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..395
                     /product="neuromedin-U receptor 2"
                     /note="NMU-R2; G-protein-coupled receptor FM-4; G-protein
                     coupled receptor TGR-1"
                     /calculated_mol_wt=44592
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          38..330
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          40..64
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          73..95
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Site            75..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          112..134
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            116..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          157..173
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          206..229
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          259..281
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     Region          298..323
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Region          323..389
                     /region_name="NmU-R2_C_term"
                     /note="Neuromedin-U receptor 2, C-terminal; pfam19285"
                     /db_xref="CDD:466027"
     Region          374..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ESQ4.2)"
     CDS             1..395
                     /gene="Nmur2"
                     /gene_synonym="FM-4; Nmu2r"
                     /coded_by="NM_022275.3:127..1314"
                     /db_xref="GeneID:64042"
                     /db_xref="RGD:621155"
ORIGIN      
        1 mgklenaswi hdplmkylns teeylahlcg pkrsdlslpv svayaliflv gvmgnllvcm
       61 vivrhqtlkt ptnyylfsla vsdllvlllg mpleiyemwh nypflfgpvg cyfktalfet
      121 vcfasilsvt tvsveryvai vhpfrakles trrralrils lvwsfsvvfs lpntsihgik
      181 fqhfpngssv pgsatctvtk pmwvynliiq atsflfyilp mtlisvlyyl mglrlkrdes
      241 leankvavni hrpsrksvtk mlfvlvlvfa icwtpfhvdr lffsfveewt eslaavfnli
      301 hvvsgvffyl ssavnpiiyn llsrrfraaf rnvvsptckw chprhrpqgp paqkiiflte
      361 chlvelteda gpqfpgqssi hntnlttapc agevp
//
LOCUS       NP_113715                330 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase PP1-alpha catalytic subunit
            [Rattus norvegicus].
ACCESSION   NP_113715
VERSION     NP_113715.1
DBSOURCE    REFSEQ: accession NM_031527.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Gao,J., Hu,X.D., Yang,H. and Xia,H.
  TITLE     Distinct Roles of Protein Phosphatase 1 Bound on Neurabin and
            Spinophilin and Its Regulation in AMPA Receptor Trafficking and LTD
            Induction
  JOURNAL   Mol Neurobiol 55 (9), 7179-7186 (2018)
   PUBMED   29383693
  REMARK    GeneRIF: PP1 bound on spinophilin, a close homolog of neurabin and
            another major synaptic PP1 anchoring protein, does not play a role
            in long term depression [LTD] induction, which suggests that
            neurabin plays a privileged role in nanodomain targeting of PP1 in
            LTD induction.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Santos,M., Rebelo,S., Van Kleeff,P.J., Kim,C.E., Dauer,W.T.,
            Fardilha,M., da Cruz E Silva,O.A. and da Cruz E Silva,E.F.
  TITLE     The nuclear envelope protein, LAP1B, is a novel protein phosphatase
            1 substrate
  JOURNAL   PLoS One 8 (10), e76788 (2013)
   PUBMED   24116158
  REMARK    GeneRIF: Data indicate that the protein phosphatase 1 (PP1) and
            nuclear membrane protein lamina associated polypeptide 1B (LAP1B)
            LAP1B:PP1 complex can be immunoprecipitated from cerebral cortex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Wurzenberger,C., Held,M., Lampson,M.A., Poser,I., Hyman,A.A. and
            Gerlich,D.W.
  TITLE     Sds22 and Repo-Man stabilize chromosome segregation by
            counteracting Aurora B on anaphase kinetochores
  JOURNAL   J Cell Biol 198 (2), 173-183 (2012)
   PUBMED   22801782
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Ouimet,C.C., da Cruz e Silva,E.F. and Greengard,P.
  TITLE     The alpha and gamma 1 isoforms of protein phosphatase 1 are highly
            and specifically concentrated in dendritic spines
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3396-3400 (1995)
   PUBMED   7724573
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Moorhead,G., MacKintosh,C., Morrice,N. and Cohen,P.
  TITLE     Purification of the hepatic glycogen-associated form of protein
            phosphatase-1 by microcystin-Sepharose affinity chromatography
  JOURNAL   FEBS Lett 362 (2), 101-105 (1995)
   PUBMED   7720853
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Kitamura,K., Mizuno,Y., Sasaki,A., Yasui,A., Tsuiki,S. and
            Kikuchi,K.
  TITLE     Molecular cloning and sequence analysis of cDNA for the catalytic
            subunit 1 alpha of rat kidney type 1 protein phosphatase, and
            detection of the gene expression at high levels in hepatoma cells
            and regenerating livers as compared to rat livers
  JOURNAL   J Biochem 109 (2), 307-310 (1991)
   PUBMED   1650776
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Wadzinski,B.E., Heasley,L.E. and Johnson,G.L.
  TITLE     Multiplicity of protein serine-threonine phosphatases in PC12
            pheochromocytoma and FTO-2B hepatoma cells
  JOURNAL   J Biol Chem 265 (35), 21504-21508 (1990)
   PUBMED   2174876
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Sasaki,K., Shima,H., Kitagawa,Y., Irino,S., Sugimura,T. and
            Nagao,M.
  TITLE     Identification of members of the protein phosphatase 1 gene family
            in the rat and enhanced expression of protein phosphatase 1 alpha
            gene in rat hepatocellular carcinomas
  JOURNAL   Jpn J Cancer Res 81 (12), 1272-1280 (1990)
   PUBMED   2177460
  REMARK    Erratum:[Jpn J Cancer Res. 1991 Jul;82(7):873. PMID: 1653777]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D00859.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D00859.1, FQ233040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..330
                     /product="serine/threonine-protein phosphatase PP1-alpha
                     catalytic subunit"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase-1d; PP-1A; Protein phosphatase
                     type 1 alpha, catalytic subunit; protein phosphatase 1,
                     catalytic subunit, alpha isozyme"
                     /calculated_mol_wt=37381
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Region          8..298
                     /region_name="MPP_PP1_PPKL"
                     /note="PP1, PPKL (PP1 and kelch-like) enzymes, and related
                     proteins, metallophosphatase domain; cd07414"
                     /db_xref="CDD:277359"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Site            order(64,66,92,96,124..125,129..130,134,173,195..197,206,
                     220..222,248,272..276)
                     /site_type="active"
                     /db_xref="CDD:277359"
     Site            order(64,66,92,124,173,248)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277359"
     Site            order(96,129..130,134,195..197,206,220..222,272..276)
                     /site_type="other"
                     /note="natural toxin binding site [chemical binding]"
                     /db_xref="CDD:277359"
     Site            order(179,181,198,203,216,225,233..234,236..238,240..242,
                     257,261,288..289,291,293,295)
                     /site_type="other"
                     /note="MYPT1 binding site [polypeptide binding]"
                     /db_xref="CDD:277359"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62137; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Region          306..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62138.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62137; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62138.1)"
     CDS             1..330
                     /gene="Ppp1ca"
                     /gene_synonym="PP1alpha"
                     /coded_by="NM_031527.1:69..1061"
                     /db_xref="GeneID:24668"
                     /db_xref="RGD:3375"
ORIGIN      
        1 msdseklnld siigrllevq gsrpgknvql teneirglcl ksreiflsqp illeleaplk
       61 icgdihgqyy dllrlfeygg fppesnylfl gdyvdrgkqs leticlllay kikypenffl
      121 lrgnhecasi nriygfydec krryniklwk tftdcfnclp iaaivdekif cchgglspdl
      181 qsmeqirrim rptdvpdqgl lcdllwsdpd kdvqgwgend rgvsftfgae vvakflhkhd
      241 ldlicrahqv vedgyeffak rqlvtlfsap nycgefdnag ammsvdetlm csfqilkpad
      301 knkgkygqfs glnpggrpit pprnsakakk
//
LOCUS       NP_001178767             386 aa            linear   ROD 28-APR-2025
DEFINITION  protein phosphatase methylesterase 1 [Rattus norvegicus].
ACCESSION   NP_001178767 XP_341892
VERSION     NP_001178767.1
DBSOURCE    REFSEQ: accession NM_001191838.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Lipina,C. and Hundal,H.S.
  TITLE     Carnosic acid stimulates glucose uptake in skeletal muscle cells
            via a PME-1/PP2A/PKB signalling axis
  JOURNAL   Cell Signal 26 (11), 2343-2349 (2014)
   PUBMED   25038454
  REMARK    GeneRIF: findings provide new insight into how CA may improve
            glucose homeostasis through enhancing peripheral glucose clearance
            in tissues such as skeletal muscle through a PME-1/PP2A/PKB
            signalling axis
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Sjostrom,M., Stenstrom,K., Eneling,K., Zwiller,J., Katz,A.I.,
            Takemori,H. and Bertorello,A.M.
  TITLE     SIK1 is part of a cell sodium-sensing network that regulates active
            sodium transport through a calcium-dependent process
  JOURNAL   Proc Natl Acad Sci U S A 104 (43), 16922-16927 (2007)
   PUBMED   17939993
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Ogris,E., Du,X., Nelson,K.C., Mak,E.K., Yu,X.X., Lane,W.S. and
            Pallas,D.C.
  TITLE     A protein phosphatase methylesterase (PME-1) is one of several
            novel proteins stably associating with two inactive mutants of
            protein phosphatase 2A
  JOURNAL   J Biol Chem 274 (20), 14382-14391 (1999)
   PUBMED   10318862
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jul 17, 2010 this sequence version replaced XP_341892.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..386
                     /product="protein phosphatase methylesterase 1"
                     /EC_number="3.1.1.89"
                     /calculated_mol_wt=42185
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZT2.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y570; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT2.2)"
     Site            16
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BVQ5;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9Y570; propagated from
                     UniProtKB/Swiss-Prot (Q4FZT2.2)"
     Region          66..>229
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          255..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4FZT2.2)"
     CDS             1..386
                     /gene="Ppme1"
                     /gene_synonym="PME-1; RGD1309683"
                     /coded_by="NM_001191838.1:146..1306"
                     /db_xref="GeneID:361613"
                     /db_xref="RGD:1309683"
ORIGIN      
        1 msaleksmhl grlpsrpplp gsggsqsgak mrmgpgrkrd ftpvpwsqyf esmedveven
       61 etgkdtfrvy ksgsegpvll llhggghsal swavftaaii srvqcrival dlrshgetkv
      121 knsedlsaet makdvgnvve amygdlpppv mlighsmgga iavhtaaanl vpsllglcmi
      181 dvvegtamda lnsmqnflrg rpktfkslen aiewsvksgq irnlesarvs mvgqvkqceg
      241 itspessksi vegiieeeee deegsesvnk rkkeddmetk kdhpytwrie laktekywdg
      301 wfrglsnlfl scpipkllll agvdrldkdl tigqmqgkfq mqvlpqcgha vhedapdkva
      361 eavatflirh rfaepiggfq cvfpgc
//
LOCUS       NP_110478                337 aa            linear   ROD 28-APR-2025
DEFINITION  B1 bradykinin receptor [Rattus norvegicus].
ACCESSION   NP_110478
VERSION     NP_110478.1
DBSOURCE    REFSEQ: accession NM_030851.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Punapart,M., Seppa,K., Jagomae,T., Liiv,M., Reimets,R.,
            Kirillov,S., Kaasik,A., Moons,L., De Groef,L., Terasmaa,A.,
            Vasar,E. and Plaas,M.
  TITLE     The Expression of RAAS Key Receptors, Agtr2 and Bdkrb1, Is
            Downregulated at an Early Stage in a Rat Model of Wolfram Syndrome
  JOURNAL   Genes (Basel) 12 (11), 1717 (2021)
   PUBMED   34828323
  REMARK    GeneRIF: The Expression of RAAS Key Receptors, Agtr2 and Bdkrb1, Is
            Downregulated at an Early Stage in a Rat Model of Wolfram Syndrome.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Shen,M., Yu,M., Qiu,C., Zhang,G., Li,J., Fang,W. and Wang,Q.
  TITLE     Myocardial angiogenesis induced by exercise training involves a
            regulatory mechanism mediated by kinin receptors
  JOURNAL   Clin Exp Hypertens 43 (5), 408-415 (2021)
   PUBMED   33687297
  REMARK    GeneRIF: Myocardial angiogenesis induced by exercise training
            involves a regulatory mechanism mediated by kinin receptors.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Catalan,M., Aranguiz,P., Boza,P., Olmedo,I., Humeres,C., Vivar,R.,
            Anfossi,R., Ayala,P., Espinoza,C., Lavandero,S. and Diaz-Araya,G.
  TITLE     TGF-beta1 induced up-regulation of B1 kinin receptor promotes
            antifibrotic activity in rat cardiac myofibroblasts
  JOURNAL   Mol Biol Rep 46 (5), 5197-5207 (2019)
   PUBMED   31309451
  REMARK    GeneRIF: Findings show that B1R negatively regulates collagen
            synthesis in cardiac myofibroblasts involving differents signaling
            pathways.
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Ma,Z., Dong,Q., Lyu,B., Wang,J., Quan,Y. and Gong,S.
  TITLE     The expression of bradykinin and its receptors in spinal cord
            ischemia-reperfusion injury rat model
  JOURNAL   Life Sci 218, 340-345 (2019)
   PUBMED   30580020
  REMARK    GeneRIF: High bradykinin receptor B1 expression is associated with
            spinal cord ischemia-reperfusion injury.
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Hachana,S., Bhat,M., Senecal,J., Huppe-Gourgues,F., Couture,R. and
            Vaucher,E.
  TITLE     Expression, distribution and function of kinin B1 receptor in the
            rat diabetic retina
  JOURNAL   Br J Pharmacol 175 (6), 968-983 (2018)
   PUBMED   29285756
  REMARK    GeneRIF: Our results support the detrimental role of B1 receptors
            on endothelial and glial cells in acute and advanced phases of
            diabetes retinopathy
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Naicker,S., Naidoo,S., Ramsaroop,R., Moodley,D. and Bhoola,K.
  TITLE     Tissue kallikrein and kinins in renal disease
  JOURNAL   Immunopharmacology 44 (1-2), 183-192 (1999)
   PUBMED   10604543
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Jones,C., Phillips,E., Davis,C., Arbuckle,J., Yaqoob,M.,
            Burgess,G.M., Docherty,R.J., Webb,M., Bevan,S.J. and McIntyre,P.
  TITLE     Molecular characterisation of cloned bradykinin B1 receptors from
            rat and human
  JOURNAL   Eur J Pharmacol 374 (3), 423-433 (1999)
   PUBMED   10422787
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Ni,A., Chai,K.X., Chao,L. and Chao,J.
  TITLE     Molecular cloning and expression of rat bradykinin B1 receptor
  JOURNAL   Biochim Biophys Acta 1442 (2-3), 177-185 (1998)
   PUBMED   9804950
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Bachvarov,D.R., Landry,M., Pelletier,I., Chevrette,M., Betard,C.,
            Houde,I., Bergeron,J., Lebel,M. and Marceau,F.
  TITLE     Characterization of two polymorphic sites in the human kinin B1
            receptor gene: altered frequency of an allele in patients with a
            history of end-stage renal failure
  JOURNAL   J Am Soc Nephrol 9 (4), 598-604 (1998)
   PUBMED   9555662
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Pesquero,J.B., Pesquero,J.L., Oliveira,S.M., Roscher,A.A.,
            Metzger,R., Ganten,D. and Bader,M.
  TITLE     Molecular cloning and functional characterization of a mouse
            bradykinin B1 receptor gene
  JOURNAL   Biochem Biophys Res Commun 220 (1), 219-225 (1996)
   PUBMED   8602848
  REMARK    Erratum:[Biochem Biophys Res Commun. 1996 Jul 5;224(1):281. doi:
            10.1006/bbrc.1996.1020. PMID: 8694827]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ132230.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ132230.2, U66107.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680435, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     Protein         1..337
                     /product="B1 bradykinin receptor"
                     /note="B1R; KB1; BK-1 receptor; kinin B1 receptor;
                     bradykinin receptor, beta 1; bradykinin B1 receptor"
                     /calculated_mol_wt=38247
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97583.2)"
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97583.2)"
     Region          37..333
                     /region_name="7tmA_BK-1"
                     /note="bradykinin receptor B1, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15380"
                     /db_xref="CDD:320502"
     Region          38..64
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320502"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Site            order(43,103,106..107,111,124,127..128,131,182,186,201,
                     273,276,308,312)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320502"
     Region          82..107
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320502"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Region          120..150
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320502"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Region          163..184
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320502"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97583.2)"
     Region          209..238
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320502"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Region          253..283
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320502"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     Region          301..326
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320502"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97583.2)"
     CDS             1..337
                     /gene="Bdkrb1"
                     /gene_synonym="b1bkr; Bdkrb; BKR"
                     /coded_by="NM_030851.1:140..1153"
                     /db_xref="GeneID:81509"
                     /db_xref="RGD:620401"
ORIGIN      
        1 masevllelq psnrslqapa nitscesale dwdllyrvlp gfviticffg llgnllvlsf
       61 fllpwrqwww qqrqrqqrlt iaeiylanla asdlvfvlgl pfwaenignr fnwpfgtdlc
      121 rvvsgvikan lfvsiflvva isqdryrllv ypmtswgyrr rrqaqatcll iwvaggllsi
      181 ptfllrsvkv vpdlnvsaci llfpheawhf armvelnvlg fllpvtaiif fnyhilaslr
      241 gqkeasrtrc ggpkgskttg liltlvasfl vcwcpyhffa fldflvqvrv iqdcswkeit
      301 dlglqlanff afvnsclnpl iyvfagrllk trvlgtl
//
LOCUS       NP_076490                504 aa            linear   ROD 28-APR-2025
DEFINITION  caM kinase-like vesicle-associated protein [Rattus norvegicus].
ACCESSION   NP_076490
VERSION     NP_076490.1
DBSOURCE    REFSEQ: accession NM_024000.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Liang,Z., Zhan,Y., Shen,Y., Wong,C.C., Yates,J.R. 3rd, Plattner,F.,
            Lai,K.O. and Ip,N.Y.
  TITLE     The pseudokinase CaMKv is required for the activity-dependent
            maintenance of dendritic spines
  JOURNAL   Nat Commun 7, 13282 (2016)
   PUBMED   27796283
  REMARK    GeneRIF: Camkv has a role in activity-dependent maintenance of
            dendritic spines
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Godbout,M., Erlander,M.G., Hasel,K.W., Danielson,P.E., Wong,K.K.,
            Battenberg,E.L., Foye,P.E., Bloom,F.E. and Sutcliffe,J.G.
  TITLE     1G5: a calmodulin-binding, vesicle-associated, protein kinase-like
            protein enriched in forebrain neurites
  JOURNAL   J Neurosci 14 (1), 1-13 (1994)
   PUBMED   8283228
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L22557.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L22557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..504
                     /product="caM kinase-like vesicle-associated protein"
                     /function="unknown"
                     /note="vesicle-associated calmodulin-binding protein"
                     /calculated_mol_wt=53975
     Region          22..286
                     /region_name="STKc_CaMK_like"
                     /note="Catalytic domain of an Uncharacterized group of
                     Serine/Threonine kinases with similarity to
                     Calcium/calmodulin-dependent protein kinases; cd14088"
                     /db_xref="CDD:270990"
     Site            order(30..34,38,51,53,83,99..102,106,108,144..145,147,
                     149..150,152,165..166,169,181..185,187)
                     /site_type="active"
                     /db_xref="CDD:270990"
     Site            order(30..33,38,51,53,83,99..102,106,149..150,152,
                     165..166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270990"
     Site            order(34,106,108,144..145,147,149,169,181..185,187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270990"
     Site            165..185
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270990"
     Region          370..>485
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          378..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63092.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHL1; propagated from
                     UniProtKB/Swiss-Prot (Q63092.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q63092.1)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHL1; propagated from
                     UniProtKB/Swiss-Prot (Q63092.1)"
     CDS             1..504
                     /gene="Camkv"
                     /gene_synonym="1G5"
                     /coded_by="NM_024000.1:133..1647"
                     /db_xref="GeneID:79011"
                     /db_xref="RGD:621488"
ORIGIN      
        1 mpfgcvtlgd kknynqpsev tdrydlgqvv kteefceifr akdkttgklh tckkfqkrdg
       61 rkvrkaakne igilkmvkhp nilqlvdvfv trkeyfifle latgrevfdw ildqgyyser
      121 dtsnvvrqvl eavaylhslk ivhrnlklen lvyynrlkns kivisdfhla klenglikep
      181 cgtpeylape vvgrqrygrp vdcwaigvim yillsgnppf yeeveeddye nhdknlfrki
      241 lagdyefdsp ywddisqaak dlvtrlmeve qdqritaeea ishewisgna asdknikdgv
      301 caqieknfar akwkkavrvt tlmkrlrape qsgtaatsda atpgaaggav aaaaggaapa
      361 sgasatvgtg gdagcaaksd dmasadrsat patdgsatpa tdgsvtpatd gsitpatdgs
      421 vtpatdrsat patdgratpa teestvpaaq ssaapaakaa atpepavaqp dstalegatg
      481 qappsskgee atgcaqesqr vets
//
LOCUS       NP_001106837            1032 aa            linear   ROD 28-APR-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001106837
VERSION     NP_001106837.1
DBSOURCE    REFSEQ: accession NM_001113366.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Zieger,H.L., Kunde,S.A., Rademacher,N., Schmerl,B. and
            Shoichet,S.A.
  TITLE     Disease-associated synaptic scaffold protein CNK2 modulates PSD
            size and influences localisation of the regulatory kinase TNIK
  JOURNAL   Sci Rep 10 (1), 5709 (2020)
   PUBMED   32235845
  REMARK    GeneRIF: Disease-associated synaptic scaffold protein CNK2
            modulates PSD size and influences localisation of the regulatory
            kinase TNIK.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Lim,J., Ritt,D.A., Zhou,M. and Morrison,D.K.
  TITLE     The CNK2 scaffold interacts with vilse and modulates Rac cycling
            during spine morphogenesis in hippocampal neurons
  JOURNAL   Curr Biol 24 (7), 786-792 (2014)
   PUBMED   24656827
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Iida,J., Nishimura,W., Yao,I. and Hata,Y.
  TITLE     Synaptic localization of membrane-associated guanylate
            kinase-interacting protein mediated by the pleckstrin homology
            domain
  JOURNAL   Eur J Neurosci 15 (9), 1493-1498 (2002)
   PUBMED   12028359
  REMARK    GeneRIF: MAGUIN-1 and -2 are recruited to synapses by the
            pleckstrin homology domain and that MAGUIN-1 subsequently interacts
            with PSD-95 at synapses.
REFERENCE   8  (residues 1 to 1032)
  AUTHORS   Yao,I., Hata,Y., Ide,N., Hirao,K., Deguchi,M., Nishioka,H.,
            Mizoguchi,A. and Takai,Y.
  TITLE     MAGUIN, a novel neuronal membrane-associated guanylate
            kinase-interacting protein
  JOURNAL   J Biol Chem 274 (17), 11889-11896 (1999)
   PUBMED   10207009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF102854.1, JAXUCZ010000021.1 and AF102853.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF102853.1, SRR26643298.31879.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..1032
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 1"
                     /note="maguin-1; maguin-2; CNK2; CNK homolog protein 2;
                     connector enhancer of KSR 2; membrane-associated guanylate
                     kinase-interacting protein"
                     /calculated_mol_wt=117260
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          324..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          339..>487
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          480..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          559..672
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     Region          682..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          866..900
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     CDS             1..1032
                     /gene="Cnksr2"
                     /coded_by="NM_001113366.1:174..3272"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:59322"
                     /db_xref="RGD:708454"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv vgwqlknlvn alredpsgvi ltlkkrpqsm
      301 ltsapallkn mrwkplalqp liprsptssv atpsstistp tkrdssalqd lyippppaep
      361 yiprdekgnl pcedlrghmv gkpvhkgses pnsfldqeyr krfniveedt vlycyeyekg
      421 rsssqgrres tptygklrpi smpveynwvg dyedpnkmkr dsrrensllr ymsnekiaqe
      481 eymfqrnskk dtgkkskkkg dkstspthys llpslqmdal rqdimgtpvp ettlyhtfqq
      541 sslqhkskkk nkgaiagksk rrisckdlgr gdcegwlwkk kdaksyfsqk wkkywfvlkd
      601 aslywyinee dekaegfisl pefkidrase crkkyafkac hpkiksfyfa aehlddmnrw
      661 lnrinmltag yaererikqe qdywsesdke eadtpstpkq dsppppydty prppsmscas
      721 pyveakhsrl sstetsqsqs sheefrqevt gssavspirk tasqrrswqd lietpltssg
      781 lhylqtlple dsvfsdsaai spehrrqstl ptqkchlqdh ygpyplaese rmqvlngngg
      841 kprsftlprd sgfnhcclna pvsacdpqdd iqppeveeee eeeeeeaage nigeknenre
      901 eklgdslqdl yraleeasls plgehristk ieyklsfikr cndpvmnekl hrlrilkstl
      961 karegevaii dkvldnpdlt skefqqwkqm yldlfldicq nttsndplsi ssevdvitss
     1021 lththsyiet hv
//
LOCUS       NP_001019428             518 aa            linear   ROD 28-APR-2025
DEFINITION  centromere protein T [Rattus norvegicus].
ACCESSION   NP_001019428 XP_226416
VERSION     NP_001019428.1
DBSOURCE    REFSEQ: accession NM_001024257.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Prendergast,L., van Vuuren,C., Kaczmarczyk,A., Doering,V.,
            Hellwig,D., Quinn,N., Hoischen,C., Diekmann,S. and Sullivan,K.F.
  TITLE     Premitotic assembly of human CENPs -T and -W switches centromeric
            chromatin to a mitotic state
  JOURNAL   PLoS Biol 9 (6), e1001082 (2011)
   PUBMED   21695110
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Gascoigne,K.E., Takeuchi,K., Suzuki,A., Hori,T., Fukagawa,T. and
            Cheeseman,I.M.
  TITLE     Induced ectopic kinetochore assembly bypasses the requirement for
            CENP-A nucleosomes
  JOURNAL   Cell 145 (3), 410-422 (2011)
   PUBMED   21529714
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC093396.1.
            
            On May 27, 2005 this sequence version replaced XP_226416.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093396.1, SRR8487230.61727.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..518
                     /product="centromere protein T"
                     /note="CENP-T"
                     /calculated_mol_wt=56730
     Region          1..375
                     /region_name="CENP-T_N"
                     /note="Centromere kinetochore component CENP-T N-terminus;
                     pfam16171"
                     /db_xref="CDD:465039"
     Region          1..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96BT3; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Region          94..381
                     /region_name="Flexible stalk domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561R1.1)"
     Region          102..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561R1.1)"
     Region          271..362
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BT3; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96BT3; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Region          375..412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q561R1.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q561R1.1)"
     Region          407..510
                     /region_name="CENP-T_C"
                     /note="Centromere kinetochore component CENP-T histone
                     fold; pfam15511"
                     /db_xref="CDD:434768"
     Site            order(419..420,423..424,427..433,435..436,439..440,
                     443..449,451..452,454,456,458,466..469,472,475..476,
                     478..481,491..492,495..496,500,503..504)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467045"
     Site            order(450,453..454,457..458,461..462,464,470..471,474,
                     477..478,484)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467045"
     CDS             1..518
                     /gene="Cenpt"
                     /gene_synonym="RGD1309383"
                     /coded_by="NM_001024257.1:8..1564"
                     /db_xref="GeneID:307805"
                     /db_xref="RGD:1309383"
ORIGIN      
        1 madlsspdgd ptirtllrhv ldtadshtpr rrqstqtnpq rrrsqtpysk rqgsqrktst
       61 rkhshgtgsv grlarvqghg hleeqtprtl lqnilltape sstvmpnpvv kpaqvpevar
      121 psrrgssrgs lelqlpeldp pstlapglka pgkrkqklrl svfqqevnqq lplpqeqrga
      181 adgsslassf nlsfvpsvqp qtvdrpglar rrpvrrpvni gaflqnlenk sltsalpgds
      241 hrtpvaalpt dvvfedtqpf sqplagcsls vhhslpnpsq tevedaervv gprtpstgtr
      301 pqsqmsragf gasplpfsep qpqspelrea vgskeaeepk dlegssgdee tsgmpasrel
      361 sssaqdllla eephqlfepp pspgvaavss esvpaklpsr trtaqprhhq dpykaglshy
      421 vklfsfhtkm pvekaalemv ekcldeyfqr lcndlevfaa hagrktvkpk dlellmrrqg
      481 lvtdqvslhv lverylpley rqqlipcafr gnsvfpaq
//
LOCUS       NP_001014201             476 aa            linear   ROD 28-APR-2025
DEFINITION  WD repeat, SAM and U-box domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001014201 XP_342438
VERSION     NP_001014201.1
DBSOURCE    REFSEQ: accession NM_001014179.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089856.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342438.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089856.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..476
                     /product="WD repeat, SAM and U-box domain-containing
                     protein 1"
                     /note="WD repeat, SAM and U-box domain containing 1"
                     /calculated_mol_wt=52114
     Region          <3..311
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          10..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          16..52
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          52..91
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          57..93
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          95..134
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          101..136
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          137..176
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          143..177
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          178..228
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          183..236
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          237..276
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          242..266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          279..318
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVN8.1)"
     Region          284..308
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          328..399
                     /region_name="SAM_WDSUB1"
                     /note="SAM domain of WDSUB1 proteins; cd09505"
                     /db_xref="CDD:188904"
     Region          404..476
                     /region_name="U-box"
                     /note="U-box domain; pfam04564"
                     /db_xref="CDD:398320"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8N9V3; propagated from
                     UniProtKB/Swiss-Prot (Q5FVN8.1)"
     CDS             1..476
                     /gene="Wdsub1"
                     /coded_by="NM_001014179.1:205..1635"
                     /db_xref="GeneID:362137"
                     /db_xref="RGD:1359296"
ORIGIN      
        1 mvklihtlad hgddvsccaf sstllatcsl dktirlysls dfaelphspl kfhtyavhcc
       61 sfspsghvla scstdgttvl wsahsghtlt vleqpggspv rvccfspdst ylasgaadgs
      121 vvlwnahsyk lyrcgsvkds slvacafspd ggllvtgssg gdltvwddrm rclhsekahd
      181 lgitccsfss qplsggehgl qlyrlascgq dceiklwvvs ftrvlgfelk yrstlsghca
      241 pvlacafshd gqmlasgsvd ksviiydigt qsvlhtltqh tryvttcafa pntlllatgs
      301 mdktvniwqf dletpcqags vsdqlkhfie dwseedvskw lraqgledlv difrtnnidg
      361 kellhltkes lagdmkiesl glrskvlrsi delrtrmesl ssgipdefic pitrelmkdp
      421 viasdgysye reameswihk kkrtspmtnl alpslvltpn rtlkmainrw lethqk
//
LOCUS       NP_001094258             604 aa            linear   ROD 28-APR-2025
DEFINITION  specifically androgen-regulated gene protein isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001094258 XP_001058496 XP_573444
VERSION     NP_001094258.1
DBSOURCE    REFSEQ: accession NM_001100788.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Steketee,K., Ziel-van der Made,A.C., van der Korput,H.A.,
            Houtsmuller,A.B. and Trapman,J.
  TITLE     A bioinformatics-based functional analysis shows that the
            specifically androgen-regulated gene SARG contains an active direct
            repeat androgen response element in the first intron
  JOURNAL   J Mol Endocrinol 33 (2), 477-491 (2004)
   PUBMED   15525603
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1.
            
            On or before Dec 17, 2009 this sequence version replaced
            XP_001058496.1, XP_573444.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. The extent of this transcript is supported
            by orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.51485.1,
                                           SRR26643288.48670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN16676784
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..604
                     /product="specifically androgen-regulated gene protein
                     isoform 1"
                     /note="specifically androgen-regulated gene protein"
                     /calculated_mol_wt=64481
     Region          20..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V8.2)"
     Region          40..604
                     /region_name="SARG"
                     /note="Specifically androgen-regulated gene protein;
                     pfam15385"
                     /db_xref="CDD:464692"
     Region          64..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW04; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW04; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI29; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI29; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Region          424..484
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V8.2)"
     Region          497..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V8.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9BW04; propagated from
                     UniProtKB/Swiss-Prot (Q499V8.2)"
     Region          553..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q499V8.2)"
     CDS             1..604
                     /gene="C13h1orf116"
                     /gene_synonym="Sarg"
                     /coded_by="NM_001100788.1:325..2139"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:498222"
                     /db_xref="RGD:1565034"
ORIGIN      
        1 mpkrelwpag scsepvthig scgsmmstts thsgssdssy dflsaeekec llflektigs
       61 leaeadsgls tdesepatsp qsfralpttt qrapqgkpea rdtqqvpvpv pkraaqssgp
      121 pespspglrs gsyslprnlh lgrsqnlrks atqtnsvsea pevfleepkk gqtrqgakti
      181 qppapsqegt pdlntvlipp peafqditsk kaegesppkk pgeqthrpqg hilersphsq
      241 kkadmssetm thkatekgwt egpqrpqqpp tqpsqntqae epslpsgvkp niqqslltat
      301 kprrlppniv lkssrssfhs hpqnwlsnht eatdsgpvss lqeqrkarre aleklglpqd
      361 qddpslpvnk htgsfkvkea qaqtssqara paqpaspalv rgtasvaeka ssvkaitpld
      421 slskgwipaq etppgkvgaa ksmpipipka skenssltqs kpdprltlqe ssipglrqmn
      481 fksntlersg vglssylsaa ekdpggqtst slgkspfldk vsssvfrnsr prpaslgmgk
      541 dfagiqggkl vgleqgqcsq qpsfkgqshd klprppcvsv kispkgipdg hrrealkklg
      601 llke
//
LOCUS       NP_997627               2161 aa            linear   ROD 28-APR-2025
DEFINITION  protein PRRC2A [Rattus norvegicus].
ACCESSION   NP_997627 XP_238193
VERSION     NP_997627.1
DBSOURCE    REFSEQ: accession NM_212462.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2161)
  AUTHORS   Piras,I.S., Angius,A., Andreani,M., Testi,M., Lucarelli,G.,
            Floris,M., Marktel,S., Ciceri,F., La Nasa,G., Fleischhauer,K.,
            Roncarolo,M.G., Bulfone,A., Gregori,S. and Bacchetta,R.
  TITLE     BAT2 and BAT3 polymorphisms as novel genetic risk factors for
            rejection after HLA-related SCT
  JOURNAL   Bone Marrow Transplant 49 (11), 1400-1404 (2014)
   PUBMED   25111513
  REMARK    Erratum:[Bone Marrow Transplant. 2014 Nov;49(11):1452. Nasa, G La
            [corrected to La Nasa, G]]
REFERENCE   2  (residues 1 to 2161)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 2161)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 2161)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 2161)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 2161)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   7  (residues 1 to 2161)
  AUTHORS   Urcelay,E., Santiago,J.L., de la Calle,H., Martinez,A., Mendez,J.,
            Ibarra,J.M., Maluenda,C., Fernandez-Arquero,M. and de la
            Concha,E.G.
  TITLE     Type 1 diabetes in the Spanish population: additional factors to
            class II HLA-DR3 and -DR4
  JOURNAL   BMC Genomics 6, 56 (2005)
   PUBMED   15842729
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2161)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   9  (residues 1 to 2161)
  AUTHORS   Matsuzaka,Y., Makino,S., Nakajima,K., Tomizawa,M., Oka,A.,
            Bahram,S., Kulski,J.K., Tamiya,G. and Inoko,H.
  TITLE     New polymorphic microsatellite markers in the human MHC class III
            region
  JOURNAL   Tissue Antigens 57 (5), 397-404 (2001)
   PUBMED   11556964
REFERENCE   10 (residues 1 to 2161)
  AUTHORS   Hashimoto,M., Nakamura,N., Obayashi,H., Kimura,F., Moriwaki,A.,
            Hasegawa,G., Shigeta,H., Kitagawa,Y., Nakano,K., Kondo,M., Ohta,M.
            and Nishimura,M.
  TITLE     Genetic contribution of the BAT2 gene microsatellite polymorphism
            to the age-at-onset of insulin-dependent diabetes mellitus
  JOURNAL   Hum Genet 105 (3), 197-199 (1999)
   PUBMED   10987645
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883046.1.
            
            On Aug 30, 2004 this sequence version replaced XP_238193.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2161
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..2161
                     /product="protein PRRC2A"
                     /note="large proline-rich protein BAT2; HLA-B-associated
                     transcript 2; proline-rich and coiled-coil-containing
                     protein 2A"
                     /calculated_mol_wt=228917
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          2..189
                     /region_name="BAT2_N"
                     /note="BAT2 N-terminus; pfam07001"
                     /db_xref="CDD:462063"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            27
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          41..1815
                     /region_name="4 X 57 AA type A repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          49..716
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            272
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            296
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          337..560
                     /region_name="2 X type B repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          738..1774
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            908
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1000
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1069
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1088
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1095
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1097
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1199
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSC1; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            1761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          1806..1886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          1920..2110
                     /region_name="3 X 50 AA type C repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          1948..1978
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          2024..2049
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            2040
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Region          2065..2161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            2086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48634; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     Site            2117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG48.1)"
     CDS             1..2161
                     /gene="Prrc2a"
                     /gene_synonym="Bat2"
                     /coded_by="NM_212462.2:1..6486"
                     /db_xref="GeneID:294250"
                     /db_xref="RGD:1303025"
ORIGIN      
        1 msdrsgptak gkdgkkyssl nlfdtykgks leiqkpavap rhglqslgkv aiarrmpppa
       61 nlpslkaenk gndpnvslvp kdgtgwaskq eqsdpkssda staqppesqp lpasqtpasn
      121 qpkrpptape ntpsvpsgvk swaqasvthg ahgdggrass llsrfsreef ptlqaagdqd
      181 kaakeresae qssgpgpslr pqnsttwrdg ggrgpdeleg pdsklhhghd prgglqpsgp
      241 pqfppyrgmm ppfmyppylp fpppygpqgp yryptpdgps rfprvagprg sgppmrlvep
      301 vgrpsilked nlkefdqldq enddgwagah eevdyteklk fsdeedgrds deegaeghkd
      361 sqsaageepe tdgkkgtspg selpppktaw tensrpsete paappipkpp pppphrgpvg
      421 nwgppgdypd rggppckppa pededeawrq rrkqssseis laverarrrr eeeerrmqee
      481 rraacaeklk rldekfgapd krlkaepaap pvtppapalp pvvpketptp palpptptpt
      541 pekdpeepah appvqsaptq agppaptpvs gggtasstss gsfeaspaep qlpskegpep
      601 peevpapttp papkvepkgd gvgptrqpps qglgypkyqk slpprfqrqq qeqllkqqqq
      661 qqwqqqqqqq gtappapvpp sppqpvtlga vpapqapppp pkalypgalg rpppmppmnf
      721 dprwmmippy vdprllqgrp pldfyppgvh psglvprers dsggsssepf erhappllre
      781 rgtppvdpkl awvgdvfttt ptdprpltsp lrqaadeeek slrsetppvp ppppylanyp
      841 gfpengtpgp pisrfplees appgprplpw ppgndeaakm qapppkkepp keepaqlsgp
      901 eagrkpargv ggggqgpppp rrenrtetrw gprpgscrrg ippedpgvpp rragpikkpp
      961 ppvkadelpp kslepgdetp kapkpdalkt akgkvgpket paggnlspap rlrrdysyer
     1021 vgptscrgrg rgeyfargrg frgtyggrgr garsrefrsy refrgddgrg ggsggtnhps
     1081 aprgrtaset rsegseyeei pkrrrqrgse tgsethesdl apsdkeappp kegvlaqvpl
     1141 appqpgapps paparfstar ggrvftprgv psrrgrgggr pppvcsgwsp pakslvpkkp
     1201 ptgplppnke plkeklisgp lspmsragnm gvgmedgerp rrrrhgraqq qdkpprfrrl
     1261 kqdrenaarg tdgkpppltl pastpaptet latvaapppp rrtaakspdl snqnsdqane
     1321 ewetasessd faserrgdke tppaalitsk avgtpggnsg gagpgistms rgdlsqrakd
     1381 lskrsfssqr pgmdrqnrrp gaggktgggg ssggggagpg grtgpgrgdk rswpspknrs
     1441 rppeerppgl plpppppsss avfrldqvih snpagiqqal aqlssrqgnv tapgghprpk
     1501 pgppqapqgs sprppthydp prasnaissd phfeepgpmv rgvggtprds agvnpfppkr
     1561 rerpprkpel lqeetvpash ssgflgskpe vpgpqeesrd sgtealtphi wnrlhtatsr
     1621 ksyqpgsiep wmeplspfed vagtemsqsd sgvdlsggsq vssgpcsqrs spdgglkgsa
     1681 egpprrpggp splkavpges ssasepseph rrrppasheg erkelpreqp lppgpigter
     1741 sqrtdrgpep gplrpahrag sqvefgttnk dsdlclvvgd tlkgekelaa sateavpvsr
     1801 dwellpsasa saepqakslg sgqcgpepsp sgqrlypevf ygspgppnsq vsggapidsq
     1861 lhpssggfrp gtpsvhqyrs qplylppgpa ppsallsgva lkgqfldfsa lqatelgklp
     1921 aggvlyppps flysaafcps plpdppllqv rqdlpspsdf ystplqpggq sgflpsgapa
     1981 qqmllpvvds qlpvvnfgsl ppapppappp lsllpvgpal qppnlavrpp papaarvlps
     2041 parpfpaslg raelhpvelk pfqdyrklss nlggpgssra ppsgrsfsgl nsrlkappst
     2101 ysgvfrtqri dlyqqasppd alrwmpkpwe rtgppsregp prraeepgpr gekepglppp
     2161 r
//
LOCUS       NP_001019933             484 aa            linear   ROD 28-APR-2025
DEFINITION  DNA primase large subunit isoform 2 [Rattus norvegicus].
ACCESSION   NP_001019933 XP_217375
VERSION     NP_001019933.1
DBSOURCE    REFSEQ: accession NM_001024762.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Popanda,O., Flohr,C., Dai,J.C., Hunzicker,A. and Thielmann,H.W.
  TITLE     A mutation in subunit B of the DNA polymerase alpha-primase complex
            from Novikoff hepatoma cells concomitant with a conformational
            change and abnormal catalytic properties of the DNA polymerase
            alpha-primase complex
  JOURNAL   Mol Carcinog 31 (4), 171-183 (2001)
   PUBMED   11536367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097454.1.
            
            On Jun 10, 2005 this sequence version replaced XP_217375.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097454.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..484
                     /product="DNA primase large subunit isoform 2"
                     /note="DNA primase large subunit; p58; DNA primase 58 kDa
                     subunit; DNA primase, p58 subunit; DNA polymerase alpha
                     subunit III (primase); primase, DNA, polypeptide 2;
                     primase (DNA) subunit 2"
                     /calculated_mol_wt=55738
     Region          28..428
                     /region_name="PriL_PriS_Eukaryotic"
                     /note="Eukaryotic core primase: Large subunit, PriL;
                     cd07322"
                     /db_xref="CDD:143474"
     Site            order(188..189,192,196,201..206)
                     /site_type="other"
                     /note="PriL_PriS interface [polypeptide binding]"
                     /db_xref="CDD:143474"
     CDS             1..484
                     /gene="Prim2"
                     /gene_synonym="Pola3"
                     /coded_by="NM_001024762.1:323..1777"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:301323"
                     /db_xref="RGD:631433"
ORIGIN      
        1 mqfsgrtrkk lrlagdqrna cyphslqfyl qpptenislt efeslafdrv kllkaienlg
       61 vsyvkgteqy qskleaeirk lkfsyrenle deyeprrrdh ishfilrlay cqsedlrrwf
      121 iqqemdllrf rfsilpkdkv qsflkdthlh feaisdeekt lreqdimass pslsgvrwes
      181 esvykvpfad aldlfrgrkv yledgfayvp lkdivaiiln efratlskal altarslpav
      241 qsderlqpll shlshsytgq dystqkstgk isldqidsls tksfppcmrq lhkalrenhh
      301 lrhggrmqyg lflkgigltl eqalqfwkqe fikgkmdpdk fdkgysynir hsfgkegkrt
      361 dytpfscmki iltnppsqgd fhgcpfrhsd aellkqkmqt ykipasgisq vddcgfslnh
      421 pnqfffesqr iltggkdikk eashpetpqh kpstqktkda tsalasldss lemdlegled
      481 yfsk
//
LOCUS       NP_001019974             607 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing protein 63 [Rattus norvegicus].
ACCESSION   NP_001019974 XP_344437
VERSION     NP_001019974.1
DBSOURCE    REFSEQ: accession NM_001024803.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097406.1.
            
            On Jun 10, 2005 this sequence version replaced XP_344437.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..607
                     /product="leucine-rich repeat-containing protein 63"
                     /calculated_mol_wt=69086
     Region          322..353
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <357..>480
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          357..378
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          358..380
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          380..401
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          381..403
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          403..424
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          404..426
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          426..447
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          427..449
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          449..470
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          450..469
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          471..497
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     Region          475..497
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          498..524
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G0.1)"
     CDS             1..607
                     /gene="Lrrc63"
                     /coded_by="NM_001024803.1:207..2030"
                     /db_xref="GeneID:364427"
                     /db_xref="RGD:1559507"
ORIGIN      
        1 mrkriyhsfk tqqhplllrr plppklpklp lvkkkvrivq tgsarepqea rrkfdteesa
       61 lvkidqsvsq pqkpasvqnv cldyehdepe rvvnifphph gvrrlhwkvp ksaagsmfip
      121 rclsassrvf rktlsqikra rkslkskqde dltkkpfsnt lviseelskp lppsysrlia
      181 srfkhsgtkf rpapkishyi qelpllkdvk etvlspissa ssaipepews erplpkttig
      241 kviqlntgsl ppahslptpa lprkpprqim ienavmtrkt etqkpveitl rptrrldpda
      301 hvlrgdgfka vgatrsetil alttlaiinc qiygrnalnf kgfflaqcpd ltsvafqlvy
      361 lnlsyndlhq fpgevlylqn lqvlklrnnp ireipseiqq lkylrkftia fnfitslpag
      421 lfclnyleel dvsyneieni pneiqklrsl ekltvdgtni tafppgilkl nlvklefent
      481 ftippfwlen scnnpprlth icslfivknn lhkildydpv vvqkylists dcdwchgpkf
      541 gegfgiirsc nifglshvpi kfhvcslscy leiressfvl egfpsrrial nmdwvkerkv
      601 snvsfyl
//
LOCUS       NP_036817                459 aa            linear   ROD 28-APR-2025
DEFINITION  vasoactive intestinal polypeptide receptor 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_036817
VERSION     NP_036817.1
DBSOURCE    REFSEQ: accession NM_012685.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Tasma,Z., Siow,A., Harris,P.W.R., Brimble,M.A., O'Carroll,S.J.,
            Hay,D.L. and Walker,C.S.
  TITLE     PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and Human
            Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor
            Antibodies
  JOURNAL   Int J Mol Sci 23 (22), 13797 (2022)
   PUBMED   36430275
  REMARK    GeneRIF: PAC1, VPAC1, and VPAC2 Receptor Expression in Rat and
            Human Trigeminal Ganglia: Characterization of PACAP-Responsive
            Receptor Antibodies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zverev Acapital,A. Cyrillic, Leonov,N.V., capital A, Cyrillicnikina
            capital TE, Cyrilliccapital,A. Cyrillic and Zefirov capital,T.E.
            CyrillicL.
  TITLE     Vasoactive Intestinal Peptide Changes the Frequency and Force of
            Myocardial Contraction in Rats
  JOURNAL   Bull Exp Biol Med 169 (6), 787-790 (2020)
   PUBMED   33098516
  REMARK    GeneRIF: Vasoactive Intestinal Peptide Changes the Frequency and
            Force of Myocardial Contraction in Rats.
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Han,X., Ran,Y., Su,M., Liu,Y., Tang,W., Dong,Z. and Yu,S.
  TITLE     Chronic changes in pituitary adenylate cyclase-activating
            polypeptide and related receptors in response to repeated chemical
            dural stimulation in rats
  JOURNAL   Mol Pain 13, 1744806917720361 (2017)
   PUBMED   28776455
  REMARK    GeneRIF: the protein and mRNA expression of pituitary adenylate
            cyclase-activating polypeptide-related receptors (PAC1, VPAC1, and
            VPAC2) in the trigeminal ganglia and trigeminal nucleus caudalis to
            identify changes associated with repetitive applications of
            chemical dural stimulations.
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Nunan,R., Sivasathiaseelan,H., Khan,D., Zaben,M. and Gray,W.
  TITLE     Microglial VPAC1R mediates a novel mechanism of
            neuroimmune-modulation of hippocampal precursor cells via IL-4
            release
  JOURNAL   Glia 62 (8), 1313-1327 (2014)
   PUBMED   24801739
  REMARK    GeneRIF: Stimulating hippocampal microglia with the peptide
            neurotransmitter VIP via VPAC1 receptors increases production of
            IL-4 which promotes their trophic and proliferative effects on
            neural stem/progenitor cells
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Li,D., Jiao,J., Shatos,M.A., Hodges,R.R. and Dartt,D.A.
  TITLE     Effect of VIP on intracellular [Ca2+], extracellular regulated
            kinase 1/2, and secretion in cultured rat conjunctival goblet cells
  JOURNAL   Invest Ophthalmol Vis Sci 54 (4), 2872-2884 (2013)
   PUBMED   23518767
  REMARK    GeneRIF: In cultured rat conjunctival goblet cells, VPAC1 and 2
            receptors are functional; VIP stimulates a cAMP-dependent increase
            in [Ca(2+)]i and glycoconjugate secretion, but not ERK1/2
            activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Guidone,G., Muller,D., Vogt,K. and Mukhopadhyay,A.K.
  TITLE     Characterization of VIP and PACAP receptors in cultured rat penis
            corpus cavernosum smooth muscle cells and their interaction with
            guanylate cyclase-B receptors
  JOURNAL   Regul Pept 108 (2-3), 63-72 (2002)
   PUBMED   12220728
  REMARK    GeneRIF: characterization of this receptor in cultured rat penis
            corpus cavernosum smooth muscle cells and its interaction with
            guanylate cyclase-B receptors
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Dorsam,G. and Goetzl,E.J.
  TITLE     Vasoactive intestinal peptide receptor-1 (VPAC-1) is a novel gene
            target of the hemolymphopoietic transcription factor Ikaros
  JOURNAL   J Biol Chem 277 (16), 13488-13493 (2002)
   PUBMED   11812772
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Pei,L. and Melmed,S.
  TITLE     Characterization of the rat vasoactive intestinal polypeptide
            receptor gene 5' region
  JOURNAL   Biochem J 308 (Pt 3) (Pt 3), 719-723 (1995)
   PUBMED   8948424
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Sreedharan,S.P., Patel,D.R., Huang,J.X. and Goetzl,E.J.
  TITLE     Cloning and functional expression of a human neuroendocrine
            vasoactive intestinal peptide receptor
  JOURNAL   Biochem Biophys Res Commun 193 (2), 546-553 (1993)
   PUBMED   8390245
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Ishihara,T., Shigemoto,R., Mori,K., Takahashi,K. and Nagata,S.
  TITLE     Functional expression and tissue distribution of a novel receptor
            for vasoactive intestinal polypeptide
  JOURNAL   Neuron 8 (4), 811-819 (1992)
   PUBMED   1314625
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087136.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087136.1, M86835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..459
                     /product="vasoactive intestinal polypeptide receptor 1
                     precursor"
                     /note="vasoactive intestinal polypeptide receptor 1; PACAP
                     type II receptor; pituitary adenylate cyclase-activating
                     polypeptide type II receptor"
                     /calculated_mol_wt=48949
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3127
     mat_peptide     31..459
                     /product="Vasoactive intestinal polypeptide receptor 1.
                     /id=PRO_0000012858"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
                     /calculated_mol_wt=48949
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30083.1)"
     Region          59..130
                     /region_name="HormR"
                     /note="Domain present in hormone receptors; smart00008"
                     /db_xref="CDD:214468"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30083.1)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30083.1)"
     Region          140..407
                     /region_name="7tmB1_VIP-R1"
                     /note="vasoactive intestinal polypeptide (VIP) receptor 1,
                     member of the class B family of seven-transmembrane G
                     protein-coupled receptors; cd15269"
                     /db_xref="CDD:320397"
     Region          142..167
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320397"
     Site            143..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Site            order(147,151,193,196..197,200,217,224,295..296,298,300,
                     356,359,372,376)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320397"
     Region          176..198
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320397"
     Site            176..197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Region          217..244
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320397"
     Site            218..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Site            256..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Region          256..276
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320397"
     Region          292..321
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320397"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30083.1)"
     Site            294..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Region          337..364
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320397"
     Site            341..361
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     Region          369..394
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320397"
     Site            370..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30083.1)"
     CDS             1..459
                     /gene="Vipr1"
                     /gene_synonym="PACAP-R-2; PACAP-R2; RATVASREC; RGD1564352;
                     VASREC; VIP-R-1"
                     /coded_by="NM_012685.2:90..1469"
                     /db_xref="GeneID:24875"
                     /db_xref="RGD:3961"
ORIGIN      
        1 mrppspphvr wlcvlagala calrpagsqa aspqheceyl qlieiqrqqc leeaqlenet
       61 tgcskmwdnl tcwpttprgq avvldcplif qlfapihgyn isrscteegw sqlepgpyhi
      121 acglndrass ldeqqqtkfy ntvktgytig yslslasllv amailslfrk lhctrnyihm
      181 hlfmsfilra tavfikdmal fnsgeidhcs easvgckaav vffqycvman ffwllvegly
      241 lytllavsff serkyfwgyi ligwgvpsvf itiwtvvriy fedfgcwdti insslwwiik
      301 apillsilvn fvlficiiri lvqklrppdi gkndsspysr lakstlllip lfgihyvmfa
      361 ffpdnfkaqv kmvfelvvgs fqgfvvaily cflngevqae lrrkwrrwhl qgvlgwssks
      421 qhpwggsnga tcstqvsmlt rvspsarrss sfqaevslv
//
LOCUS       NP_001020234             414 aa            linear   ROD 28-APR-2025
DEFINITION  secernin-1 [Rattus norvegicus].
ACCESSION   NP_001020234 XP_578274
VERSION     NP_001020234.1
DBSOURCE    REFSEQ: accession NM_001025063.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Lindhout,F.W., Cao,Y., Kevenaar,J.T., Bodzeta,A., Stucchi,R.,
            Boumpoutsari,M.M., Katrukha,E.A., Altelaar,M., MacGillavry,H.D. and
            Hoogenraad,C.C.
  TITLE     VAP-SCRN1 interaction regulates dynamic endoplasmic reticulum
            remodeling and presynaptic function
  JOURNAL   EMBO J 38 (20), e101345 (2019)
   PUBMED   31441084
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079152.1.
            
            On Jun 25, 2005 this sequence version replaced XP_578274.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079152.1, SRR8487227.329367.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMN12840109
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..414
                     /product="secernin-1"
                     /calculated_mol_wt=46265
     Region          18..>231
                     /region_name="PepD"
                     /note="Dipeptidase [Amino acid transport and metabolism];
                     cl41909"
                     /db_xref="CDD:477862"
     CDS             1..414
                     /gene="Scrn1"
                     /coded_by="NM_001025063.1:175..1419"
                     /db_xref="GeneID:502776"
                     /db_xref="RGD:1560999"
ORIGIN      
        1 msgappsysf valpprakdg lvvfgknsar prdevqevvy fpavdheaes kvectyisid
       61 qvprthaivi srpawlwgae mganehgvci aneainarep aaeteallgm dlvrlglerg
      121 ttakealdii vslldehgqg gnyyedahsc hsfqsayllv drdeawvlet vgkywaaeri
      181 tegvrcicnh lslttkmdee hpelrtyaqs qgwwtgedef nfaqvfspad dhldccagkd
      241 slekqeesit vqtminilrd kasgvcidse sflttasivs vlpqnrsspc ihyftgtpdp
      301 srsifkpfif vddvklvpka qspcfgdddp akkeprfqek pdrrhelyka hewaravies
      361 dqeqgrtlrk tmlelekqgl eameeilssp eppdpaevgd lfydcvdtem kffk
//
LOCUS       NP_446027               2182 aa            linear   ROD 28-APR-2025
DEFINITION  calcineurin-binding protein cabin-1 [Rattus norvegicus].
ACCESSION   NP_446027 XP_003753505 XP_003753506
VERSION     NP_446027.2
DBSOURCE    REFSEQ: accession NM_053575.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2182)
  AUTHORS   Wen,Y., Chen,J., Liu,L., Guo,G., Zeng,Y., Zhang,Y., Zeng,Z.,
            Wang,Z., Peng,X. and Liang,J.
  TITLE     Cabin1 involves in renal tubular epithelial cells mitochondrial
            dysfunction through SIRT1/p53 pathway
  JOURNAL   J Recept Signal Transduct Res 40 (2), 141-147 (2020)
   PUBMED   32000560
  REMARK    GeneRIF: Cabin1 involves in renal tubular epithelial cells
            mitochondrial dysfunction through SIRT1/p53 pathway.
REFERENCE   2  (residues 1 to 2182)
  AUTHORS   Wen,Y., Liu,L., Xu,Q., Zhou,P., Li,H., Wang,Z. and Liang,J.
  TITLE     Knocking down Cabin1 induces glomerular podocyte injury
  JOURNAL   Int Urol Nephrol 50 (5), 983-991 (2018)
   PUBMED   29368245
  REMARK    GeneRIF: Knocking down Cabin1 induces the disruption of
            cytoskeleton and mitochondrial dysfunction in podocyte. Cabin1
            could be a crucial factor in podocyte damage.
REFERENCE   3  (residues 1 to 2182)
  AUTHORS   Wen,Y., Li,H., Zhou,P., Liu,L., Wang,Z. and Liang,J.
  TITLE     Upregulation of Cabin1 During Injury to Renal Tubular Epithelial
            Cells in Rats
  JOURNAL   Iran J Kidney Dis 11 (6), 430-437 (2017)
   PUBMED   29190603
  REMARK    GeneRIF: Injury to renal tubular epithelial cells results in
            up-regulation of cabin1 expression.
REFERENCE   4  (residues 1 to 2182)
  AUTHORS   Wen,Y., Zhou,P., Liu,L., Wang,Z., Zhang,Y. and Liang,J.
  TITLE     Effect of the knockdown of Cabin1 on p53 in glomerular podocyte
  JOURNAL   J Recept Signal Transduct Res 36 (2), 173-180 (2016)
   PUBMED   26400065
  REMARK    GeneRIF: In conclusion, Cabin1 expression significantly increases
            during podocyte injury. Knockdown of Cabin1 induces p53 expression
            decrease in cultured podocyte. Cabin1 may provide a new target to
            investigate podocyte injury.
REFERENCE   5  (residues 1 to 2182)
  AUTHORS   Yi,J.K., Kim,H.J., Yu,D.H., Park,S.J., Shin,M.J., Yuh,H.S.,
            Bae,K.B., Ji,Y.R., Kim,N.R., Park,S.J., Kim,J.Y., Lee,H.S.,
            Lee,S.G., Yoon du,H., Hyun,B.H., Kim,W.U. and Ryoo,Z.Y.
  TITLE     Regulation of inflammatory responses and fibroblast-like
            synoviocyte apoptosis by calcineurin-binding protein 1 in mice with
            collagen-induced arthritis
  JOURNAL   Arthritis Rheum 64 (7), 2191-2200 (2012)
   PUBMED   22275266
REFERENCE   6  (residues 1 to 2182)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   7  (residues 1 to 2182)
  AUTHORS   Kim,M.J., Jo,D.G., Hong,G.S., Kim,B.J., Lai,M., Cho,D.H., Kim,K.W.,
            Bandyopadhyay,A., Hong,Y.M., Kim,D.H., Cho,C., Liu,J.O.,
            Snyder,S.H. and Jung,Y.K.
  TITLE     Calpain-dependent cleavage of cain/cabin1 activates calcineurin to
            mediate calcium-triggered cell death
  JOURNAL   Proc Natl Acad Sci U S A 99 (15), 9870-9875 (2002)
   PUBMED   12114545
REFERENCE   8  (residues 1 to 2182)
  AUTHORS   Lai,M.M., Luo,H.R., Burnett,P.E., Hong,J.J. and Snyder,S.H.
  TITLE     The calcineurin-binding protein cain is a negative regulator of
            synaptic vesicle endocytosis
  JOURNAL   J Biol Chem 275 (44), 34017-34020 (2000)
   PUBMED   10931822
REFERENCE   9  (residues 1 to 2182)
  AUTHORS   Lai,M.M., Burnett,P.E., Wolosker,H., Blackshaw,S. and Snyder,S.H.
  TITLE     Cain, a novel physiologic protein inhibitor of calcineurin
  JOURNAL   J Biol Chem 273 (29), 18325-18331 (1998)
   PUBMED   9660798
REFERENCE   10 (residues 1 to 2182)
  AUTHORS   van Deursen,J., Boer,J., Kasper,L. and Grosveld,G.
  TITLE     G2 arrest and impaired nucleocytoplasmic transport in mouse embryos
            lacking the proto-oncogene CAN/Nup214
  JOURNAL   EMBO J 15 (20), 5574-5583 (1996)
   PUBMED   8896451
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF061947.1, JAXUCZ010000020.1 and DV716961.1.
            
            On or before Jul 7, 2012 this sequence version replaced
            XP_003753505.1, XP_003753506.1, NP_446027.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF061947.1, SRR26643429.57528.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2182
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..2182
                     /product="calcineurin-binding protein cabin-1"
                     /note="calcineurin inhibitor; calcineurin-binding protein
                     cabin-1-like"
                     /calculated_mol_wt=242669
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Region          30..>205
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          36..69
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          90..123
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,125,128..129,132..133,135..136,
                     159,162..163,166..167,170)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          123..153
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          125..157
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          158..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          356..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          615..648
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Region          1055..1088
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Site            order(1056,1059..1060,1063..1064,1066,1090,1093..1094,
                     1097..1098,1100,1106,1141,1144..1145,1148..1149,1152)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1056..1083
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1088..1135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1106..1139
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          1299..1496
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Site            1439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Region          1671..1848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          <1914..2156
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1917..2035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Site            2003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Region          2054..2126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Region          2078..2115
                     /region_name="Required for interaction with calcineurin"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     Site            2113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Site            2116
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y6J0; propagated from
                     UniProtKB/Swiss-Prot (O88480.1)"
     Region          2118..2152
                     /region_name="MEF2_binding"
                     /note="MEF2 binding; pfam09047"
                     /db_xref="CDD:370261"
     Region          2160..2182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88480.1)"
     CDS             1..2182
                     /gene="Cabin1"
                     /gene_synonym="Cain"
                     /coded_by="NM_053575.2:326..6874"
                     /db_xref="GeneID:94165"
                     /db_xref="RGD:620263"
ORIGIN      
        1 miriaalnas stieddhegs fkshkiqtke aqeaeafaly hkaldlqkhd rfeesakayh
       61 ellearllre avssgdekeg lkhpglilky styknlaqla aqredletam efyleavmld
      121 stdvnlwyki ghvalrlirl plarhafeeg lrcnpdhwpc ldnlitvlyt lsdyttclyf
      181 ickalekdcr yskglvlkek ifeeqpclrk dslrmflkcd msvhevsvna aetqaivdea
      241 lglrkkrqal ivrekepdlk lvqpipfftw kclgesllam ynhlttcepp rpslgkridl
      301 sdyqdpsqll apsvvvtpvs vvqpspvctn ptvavaepvl sytsvtttsf plhspglldt
      361 gtpmgdvsgg dkskkgvkrk ktleesgeta krrsarvrnt kckkeekvdf qgllvkflps
      421 rlrkldpeee ddpfnnyevq seaklesfsn vgphrlsfds atfmesekqd vhaflmenlt
      481 nggvlelmmr ylksmghkfl lkwppglaev vlsvyhswrr hstslpnpll rdcsnkhikd
      541 mmlmslscme lqldqwlltk grsstvsprn cpagvvtgrf gpdfpgthcl gdllqlsfas
      601 sqrdlfedgw lefvvrvywl karflalqgd meqalenydi cteilqssta lqaqagaeqr
      661 divirlpnlh ndsivsleei dknlkslerc qsleeiqrlf eagdykavvq llrptlctsg
      721 fdrakhlefm tsiperpaql lllqdsllrl eehrqcfecs dvalneavqq mlnssdsaak
      781 eewaatvtql llgmeqalss dsrgsilkes ssptglvrlt nnliqvidcs mavqeepkep
      841 yvssvlpwii lhriiwqeed tfrslchqqq lqnpteegis empmlpsslm llntaheylg
      901 rrswccnsdg allrfyvhvl qkelaasase dthpykeele taleqcfycl ysfpskkska
      961 ryleehsaqq vdltwedalf mfeyfkpktl pefdsyktst vsadlanllk riativprte
     1021 kpalsmdkvs ayiegtsaev pclpdgadpa ppvlnelyyl ladyhfknke qskaikfymh
     1081 dicicpnrfd swagmalara sriqdklnsn elksdgpiwr hatpvlncfr raleidssnl
     1141 slwieygtms yalhsfasrq lkqwraelpp evvqqmedrr dsmletarhc ftsaahcegd
     1201 gdeeewlihy mlgkvaekqq qpptvyllhy rqaghylhee aarypkkihy hnppelamea
     1261 levyfrlhas ilkllgkpds gvsaevlvsf mkeaaegpfa rgeekntpka sekekaclvd
     1321 edshssagtl pgpgaslpss sgpgltsppy tatpidhdyv kckkprqqat pddrsqdsta
     1381 valsdssstq dffneptsll dgsrkllpek risglsaqag psgkdlpgpt eergkteesl
     1441 esteafrvve psvqkpvads sasayipskp avstpppwdg kkrsdplgep vafpqglpag
     1501 aeeqrqflte qciasfclcl srfpqhyksl yrlaflytys kthrnlqwar dvllgssipw
     1561 qqlqhmpaqg lfcernktnf fngiwripvd eidrpgsfaw hmnrsivlll kvlaqlrdhs
     1621 tllkvssmlq rtpdqgkkyl rdadrqvlaq rafiltvkvl edtlselaeg lehpgskacg
     1681 lsgarmttdv shkaspedgq eslphpkklp ladgsgpgpe pggkvgplhq lpvatdtrdn
     1741 teqggepkdk erppvgptep mdtgetaarh pdleptprll pgrpprdrgp esrsaelsle
     1801 elsistrqqp aplvpspvtp ttaapttmga raaghpeeap prpnrkrkll qdtesgktll
     1861 ldayrvwqqg qkamaydlsr iekimsetym likqvdeeta leqavkfcqv hlgaaaqrqa
     1921 sgdapttpkh pkdsrenffp atvapsapdt tapdalqrps dshlkpglaa aitcppsasa
     1981 stpdpgipqp hrpeavpsra plspdgeevs gvtegpsfls qeprhshqmk maatgplaeq
     2041 hcwpveaacq tgaeptfsqa tstkvpssgs tqtpeshqgk tessraksrl lpnmpklvip
     2101 sattkfppei tvtpptptll spkgsiseet kqklksails aqsaanvrke slcqpalevl
     2161 etssqessle setdedddfm dv
//
LOCUS       NP_998732                123 aa            linear   ROD 28-APR-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA12 [Rattus norvegicus].
ACCESSION   NP_998732 XP_342081
VERSION     NP_998732.1
DBSOURCE    REFSEQ: accession NM_213567.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Vannini,A. and Cramer,P.
  TITLE     Conservation between the RNA polymerase I, II, and III
            transcription initiation machineries
  JOURNAL   Mol Cell 45 (4), 439-446 (2012)
   PUBMED   22365827
  REMARK    Review article
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Schneider,D.A.
  TITLE     RNA polymerase I activity is regulated at multiple steps in the
            transcription cycle: recent insights into factors that influence
            transcription elongation
  JOURNAL   Gene 493 (2), 176-184 (2012)
   PUBMED   21893173
  REMARK    Review article
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Hong,L., Zhang,Y., Liu,N., Liu,C., Zhi,M., Pan,Y., Lan,M., Sun,L.
            and Fan,D.
  TITLE     Suppression of the cell proliferation in stomach cancer cells by
            the ZNRD1 gene
  JOURNAL   Biochem Biophys Res Commun 321 (3), 611-616 (2004)
   PUBMED   15358150
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI232728.1, FM113828.1 and BX883052.1.
            
            On Aug 30, 2004 this sequence version replaced XP_342081.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            CDS exon combination :: FM058208.1, FM113828.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..123
                     /product="DNA-directed RNA polymerase I subunit RPA12"
                     /EC_number="2.7.7.6"
                     /note="nuclear RNA polymerase I small specific subunit
                     Rpa12 like; zinc ribbon domain-containing protein 1; zinc
                     ribbon domain containing 1; DNA-directed RNA polymerase I
                     subunit H"
                     /calculated_mol_wt=13455
     Region          16..115
                     /region_name="RPB9"
                     /note="DNA-directed RNA polymerase, subunit
                     M/Transcription elongation factor TFIIS [Transcription];
                     COG1594"
                     /db_xref="CDD:441202"
     Region          76..122
                     /region_name="Zn-ribbon_RPA12"
                     /note="C-terminal zinc ribbon domain of RPA12 subunit of
                     RNA polymerase I; cd10507"
                     /db_xref="CDD:259792"
     Site            order(84,87,112,115)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259792"
     Region          103..104
                     /region_name="Hairpin.
                     /evidence=ECO:0000250|UniProtKB:Q9P1U0,
                     ECO:0000250|UniProtKB:Q9Y2Y1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MFY5.1)"
     CDS             1..123
                     /gene="Polr1h"
                     /gene_synonym="HTEX-6; Tctex6; Znrd1"
                     /coded_by="NM_213567.2:32..403"
                     /db_xref="GeneID:361784"
                     /db_xref="RGD:1303114"
ORIGIN      
        1 melarpcsnf qsdldfcpdc gsvlplpgvq dtvicprcgf sidvrdfggk vvktsvvfnk
       61 lgtvipmsvd egpesqgpvv drrcsrcghe gmayytrqmr sadegqtvfy tcinckfqek
      121 eds
//
LOCUS       NP_001101494             719 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat and fibronectin type-III domain-containing
            protein 5 precursor [Rattus norvegicus].
ACCESSION   NP_001101494 XP_001076173 XP_234219
VERSION     NP_001101494.1
DBSOURCE    REFSEQ: accession NM_001108024.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Choi,Y., Nam,J., Whitcomb,D.J., Song,Y.S., Kim,D., Jeon,S.,
            Um,J.W., Lee,S.G., Woo,J., Kwon,S.K., Li,Y., Mah,W., Kim,H.M.,
            Ko,J., Cho,K. and Kim,E.
  TITLE     SALM5 trans-synaptically interacts with LAR-RPTPs in a
            splicing-dependent manner to regulate synapse development
  JOURNAL   Sci Rep 6, 26676 (2016)
   PUBMED   27225731
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Zhu,Y., Yao,S., Augustine,M.M., Xu,H., Wang,J., Sun,J.,
            Broadwater,M., Ruff,W., Luo,L., Zhu,G., Tamada,K. and Chen,L.
  TITLE     Neuron-specific SALM5 limits inflammation in the CNS via its
            interaction with HVEM
  JOURNAL   Sci Adv 2 (4), e1500637 (2016)
   PUBMED   27152329
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Mah,W., Ko,J., Nam,J., Han,K., Chung,W.S. and Kim,E.
  TITLE     Selected SALM (synaptic adhesion-like molecule) family proteins
            regulate synapse formation
  JOURNAL   J Neurosci 30 (16), 5559-5568 (2010)
   PUBMED   20410109
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Morimura,N., Inoue,T., Katayama,K. and Aruga,J.
  TITLE     Comparative analysis of structure, expression and PSD95-binding
            capacity of Lrfn, a novel family of neuronal transmembrane proteins
  JOURNAL   Gene 380 (2), 72-83 (2006)
   PUBMED   16828986
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473947.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_234219.3, XP_001076173.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760393,
                              SAMEA5760396 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q23"
     Protein         1..719
                     /product="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 5 precursor"
                     /note="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 5"
                     /calculated_mol_wt=77326
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2032
     mat_peptide     18..719
                     /product="Leucine-rich repeat and fibronectin type-III
                     domain-containing protein 5. /id=PRO_0000394523"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
                     /calculated_mol_wt=77326
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          53..76
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <69..>211
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          76..97
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          100..121
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..169
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..193
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          173..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          196..217
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          197..215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          240..>272
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          287..374
                     /region_name="IgI_SALM5_like"
                     /note="Immunoglobulin domain of human Synaptic
                     Adhesion-Like Molecule 5 (SALM5) and similar proteins;
                     member of the I-set of IgSF domains; cd05764"
                     /db_xref="CDD:409421"
     Region          287..290
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409421"
     Region          294..297
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409421"
     Region          303..311
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409421"
     Site            order(309,311,319,326,361..363,365)
                     /site_type="other"
                     /note="PTPdelta binding site [polypeptide binding]"
                     /db_xref="CDD:409421"
     Region          317..322
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409421"
     Region          325..327
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409421"
     Region          333..337
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409421"
     Site            339
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          340..344
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409421"
     Region          354..361
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409421"
     Region          364..374
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409421"
     Region          383..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          421..494
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Site            452
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4A1J9.1)"
     Site            530..550
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          614..719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A1J9.1)"
     Region          <631..714
                     /region_name="Metaviral_G"
                     /note="Metaviral_G glycoprotein; pfam09595"
                     /db_xref="CDD:462833"
     CDS             1..719
                     /gene="Lrfn5"
                     /coded_by="NM_001108024.1:484..2643"
                     /db_xref="GeneID:314164"
                     /db_xref="RGD:1309357"
ORIGIN      
        1 mekflfylfl igiavraqic pkrcvcqils pnlatlcakk gllfvppnid rrtvelrlad
       61 nfvtnikrkd fanmtslvdl tlsrntisfi tphafadlrn lralhlnsnr ltkitndmfs
      121 glsnlhhlil nnnqltliss tafddvfale eldlsynnle tipwdavekm vslhtlsldh
      181 nmidnipkgt fshlhkmtrl dvtsnklqkl ppdplfqraq vlatsgiisp stfalsfggn
      241 plhcncellw lrrlsreddl etcaspallt gryfwsipee eflcepplit rhthemrvle
      301 gqratlrcka rgdpepaihw ispegklisn atrslvydng tldilittvk dtgaftcias
      361 npageatqtm dlhiiklphl lnstnnihep dpgssdists tksgsnasss ngdtkmsqdk
      421 ivvaeassst allkfnfqrn ipgirmfqiq yngtyddtlv yrmipptskt flvnnlasgt
      481 mydlcvlaiy ddgitsltat rvvgciqftt eqdyvrchfm qsqflggtmi iiiggiivas
      541 vlvfiiilmi rykvcnnngq hkvtkvsnvy sqtngaqmqg csvtlpqsms kqamgheena
      601 qcckvasdsa iqssetcssq dsstttsalp ptwtssapvs qkqkrktgtk psaepqseav
      661 tnvesqntnr nnstalqlas cppdsvtegp tsqrahtkpn alltnvdqnv qetqrlesi
//
LOCUS       NP_058701                507 aa            linear   ROD 28-APR-2025
DEFINITION  fumarate hydratase, mitochondrial precursor [Rattus norvegicus].
ACCESSION   NP_058701
VERSION     NP_058701.2
DBSOURCE    REFSEQ: accession NM_017005.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Rodriguez-Rivera,C., Gonzalez-Martin,C., Fernandez-Millan,E.,
            Alvarez,C., Escriva,F. and Alguacil,L.F.
  TITLE     Perinatal undernourishment provokes long-lasting alterations of
            clusterin and fumarate hydratase expression in the rat nucleus
            accumbens
  JOURNAL   Nutr Neurosci 25 (9), 1796-1800 (2022)
   PUBMED   33755527
  REMARK    GeneRIF: Perinatal undernourishment provokes long-lasting
            alterations of clusterin and fumarate hydratase expression in the
            rat nucleus accumbens.
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Zheng,X., Chen,M., Li,X., Yang,P., Zhao,X., Ouyang,Y., Yang,Z.,
            Liang,M., Hou,E. and Tian,Z.
  TITLE     Insufficient fumarase contributes to hypertension by an imbalance
            of redox metabolism in Dahl salt-sensitive rats
  JOURNAL   Hypertens Res 42 (11), 1672-1682 (2019)
   PUBMED   31235845
  REMARK    GeneRIF: Insufficient fumarase contributes to hypertension by an
            imbalance of redox metabolism in Dahl salt-sensitive rats.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Ajalla Aleixo,M.A., Rangel,V.L., Rustiguel,J.K., de Padua,R.A.P.
            and Nonato,M.C.
  TITLE     Structural, biochemical and biophysical characterization of
            recombinant human fumarate hydratase
  JOURNAL   FEBS J 286 (10), 1925-1940 (2019)
   PUBMED   30761759
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Kulkarni,R.A., Bak,D.W., Wei,D., Bergholtz,S.E., Briney,C.A.,
            Shrimp,J.H., Alpsoy,A., Thorpe,A.L., Bavari,A.E., Crooks,D.R.,
            Levy,M., Florens,L., Washburn,M.P., Frizzell,N., Dykhuizen,E.C.,
            Weerapana,E., Linehan,W.M. and Meier,J.L.
  TITLE     A chemoproteomic portrait of the oncometabolite fumarate
  JOURNAL   Nat Chem Biol 15 (4), 391-400 (2019)
   PUBMED   30718813
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Bulku,A., Weaver,T.M. and Berkmen,M.B.
  TITLE     Biochemical Characterization of Two Clinically-Relevant Human
            Fumarase Variants Defective for Oligomerization
  JOURNAL   Open Biochem J 12, 1-15 (2018)
   PUBMED   29456767
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Wei,M.H., Toure,O., Glenn,G.M., Pithukpakorn,M., Neckers,L.,
            Stolle,C., Choyke,P., Grubb,R., Middelton,L., Turner,M.L.,
            Walther,M.M., Merino,M.J., Zbar,B., Linehan,W.M. and Toro,J.R.
  TITLE     Novel mutations in FH and expansion of the spectrum of phenotypes
            expressed in families with hereditary leiomyomatosis and renal cell
            cancer
  JOURNAL   J Med Genet 43 (1), 18-27 (2006)
   PUBMED   15937070
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Bourgeron,T., Chretien,D., Poggi-Bach,J., Doonan,S., Rabier,D.,
            Letouze,P., Munnich,A., Rotig,A., Landrieu,P. and Rustin,P.
  TITLE     Mutation of the fumarase gene in two siblings with progressive
            encephalopathy and fumarase deficiency
  JOURNAL   J Clin Invest 93 (6), 2514-2518 (1994)
   PUBMED   8200987
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Suzuki,T., Sato,M., Yoshida,T. and Tuboi,S.
  TITLE     Rat liver mitochondrial and cytosolic fumarases with identical
            amino acid sequences are encoded from a single gene
  JOURNAL   J Biol Chem 264 (5), 2581-2586 (1989)
   PUBMED   2914923
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Lai,J.C. and Clark,J.B.
  TITLE     Preparation and properties of mitochondria derived from
            synaptosomes
  JOURNAL   Biochem J 154 (2), 423-432 (1976)
   PUBMED   938457
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087598.1.
            
            On Oct 12, 2007 this sequence version replaced NP_058701.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087598.1, J04473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..507
                     /product="fumarate hydratase, mitochondrial precursor"
                     /EC_number="4.2.1.2"
                     /note="fumarate hydratase, mitochondrial; fumarase;
                     fumarate hydratase 1"
                     /calculated_mol_wt=50040
     transit_peptide 1..41
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:2914923; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
                     /calculated_mol_wt=4443
     mat_peptide     42..507
                     /product="Fumarate hydratase, mitochondrial.
                     /id=PRO_0000010325"
                     /note="propagated from UniProtKB/Swiss-Prot (P14408.2)"
                     /calculated_mol_wt=50040
     Region          46..505
                     /region_name="FumC"
                     /note="Fumarate hydratase class II [Energy production and
                     conversion]; COG0114"
                     /db_xref="CDD:439884"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            289
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07954; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            375
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P05042; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     Site            499
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97807; propagated from
                     UniProtKB/Swiss-Prot (P14408.2)"
     CDS             1..507
                     /gene="Fh"
                     /gene_synonym="Fh1"
                     /coded_by="NM_017005.2:15..1538"
                     /db_xref="GeneID:24368"
                     /db_xref="RGD:2614"
ORIGIN      
        1 mnrafcllar srrfprvpsa gavlsgeaat lprcapnvvr masqnsfrie ydtfgelkvp
       61 tdkyygaqtv rstmnfkigg atermpipvi kafgilkraa aevnqeygld pkiasaimka
      121 adevaegkln dhfplvvwqt gsgtqtnmnv nevisnraie mlggelgskk pvhpndhvnk
      181 sqssndtfpt amhiaaalev hqvllpglqk lhdalsaksk efaqvikigr thtqdavplt
      241 lgqefsgyvq qvqyamerik aampriyela aggtavgtgl ntrigfaekv aakvaaltgl
      301 pfvtapnkfe alaahdalve lsgamnttac slmkiandir flgsgprsgl gelilpenep
      361 gssimpgkvn ptqceamtmv aaqvmgnhva vtvggsnghf elnvfkpmmi knvlhsarll
      421 gdasvsften cvvgiqante rinklmnesl mlvtalnphi gydkaakiak tahkngstlk
      481 etaielgylt aeqfdewvkp kdmlgpk
//
LOCUS       NP_113963                277 aa            linear   ROD 28-APR-2025
DEFINITION  caspase-6 [Rattus norvegicus].
ACCESSION   NP_113963
VERSION     NP_113963.2
DBSOURCE    REFSEQ: accession NM_031775.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wang,C., Li,Q., Jia,Z., Zhang,H., Li,Y., Zhao,Q., Su,L., Yu,Y. and
            Xu,R.
  TITLE     Spinal caspase-6 contributes to remifentanil-induced hyperalgesia
            via regulating CCL21/CXCR3 pathway in rats
  JOURNAL   Neurosci Lett 721, 134802 (2020)
   PUBMED   32014515
  REMARK    GeneRIF: Spinal caspase-6 contributes to remifentanil-induced
            hyperalgesia via regulating CCL21/CXCR3 pathway in rats.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Nie,Z.Y., Yao,M., Yang,Z., Yang,L., Liu,X.J., Yu,J., Ma,Y.,
            Zhang,N., Zhang,X.Y., Liu,M.H., Jiang,L.L. and Luo,J.M.
  TITLE     De-regulated STAT5A/miR-202-5p/USP15/Caspase-6 regulatory axis
            suppresses CML cell apoptosis and contributes to Imatinib
            resistance
  JOURNAL   J Exp Clin Cancer Res 39 (1), 17 (2020)
   PUBMED   31952546
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Woo,V., Cheng,C., Duraikannu,A., Chandrasekhar,A., Purdy,K.,
            Martinez,J.A. and Zochodne,D.W.
  TITLE     Caspase-6 is a Dispensable Enabler of Adult Mammalian Axonal
            Degeneration
  JOURNAL   Neuroscience 371, 242-253 (2018)
   PUBMED   29229552
  REMARK    GeneRIF: To evaluate an axon autonomous role of Casp6, study
            examined axon integrity following transection ex vivo, and analyzed
            the serial morphological fragmentation of neurofilament expression
            as a structural index of axonal degeneration. Adding a specific
            Casp6 inhibitor to the preparation delayed neurofilament
            fragmentation.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Wei,Y., Zheng,D., Guo,X., Zhao,M., Gao,L. and Bai,L.
  TITLE     Transient Receptor Potential Channel, Vanilloid 5, Induces
            Chondrocyte Apoptosis in a Rat Osteoarthritis Model Through the
            Mediation of Ca2+ Influx
  JOURNAL   Cell Physiol Biochem 46 (2), 687-698 (2018)
   PUBMED   29621761
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Harrison,D.C., Davis,R.P., Bond,B.C., Campbell,C.A., James,M.F.,
            Parsons,A.A. and Philpott,K.L.
  TITLE     Caspase mRNA expression in a rat model of focal cerebral ischemia
  JOURNAL   Brain Res Mol Brain Res 89 (1-2), 133-146 (2001)
   PUBMED   11311984
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Guo,R.F., Huber-Lang,M., Wang,X., Sarma,V., Padgaonkar,V.A.,
            Craig,R.A., Riedemann,N.C., McClintock,S.D., Hlaing,T., Shi,M.M.
            and Ward,P.A.
  TITLE     Protective effects of anti-C5a in sepsis-induced thymocyte
            apoptosis
  JOURNAL   J Clin Invest 106 (10), 1271-1280 (2000)
   PUBMED   11086028
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Ferrer,I.
  TITLE     Role of caspases in ionizing radiation-induced apoptosis in the
            developing cerebellum
  JOURNAL   J Neurobiol 41 (4), 549-558 (1999)
   PUBMED   10590178
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Vakkala,M., Paakko,P. and Soini,Y.
  TITLE     Expression of caspases 3, 6 and 8 is increased in parallel with
            apoptosis and histological aggressiveness of the breast lesion
  JOURNAL   Br J Cancer 81 (4), 592-599 (1999)
   PUBMED   10574243
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Kaushal,G.P., Singh,A.B. and Shah,S.V.
  TITLE     Identification of gene family of caspases in rat kidney and altered
            expression in ischemia-reperfusion injury
  JOURNAL   Am J Physiol 274 (3), F587-F595 (1998)
   PUBMED   9530276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM068086.1 and BC078785.1.
            
            On Aug 23, 2004 this sequence version replaced NP_113963.1.
            
            Transcript Variant: This variant (1) is the longer transcript.
            Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078785.1, AF025670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132294
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q43"
     Protein         1..277
                     /product="caspase-6"
                     /EC_number="3.4.22.59"
                     /note="CASP-6; apoptotic protease Mch-2"
                     /calculated_mol_wt=31443
     Region          20..273
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; smart00115"
                     /db_xref="CDD:214521"
     Region          25..27
                     /region_name="Tri-arginine exosite.
                     /evidence=ECO:0000250|UniProtKB:P55212"
                     /note="propagated from UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(47,105,144,151,200..205,209..210)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08738; propagated from
                     UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(104,146)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Region          108..125
                     /region_name="130's region.
                     /evidence=ECO:0000250|UniProtKB:P55212"
                     /note="propagated from UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(152,185..186,193,196,199,222,230,236,256,261..262,
                     264,267..268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(153,184)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55212; propagated from
                     UniProtKB/Swiss-Prot (O35397.2)"
     CDS             1..277
                     /gene="Casp6"
                     /gene_synonym="Mch2"
                     /coded_by="NM_031775.3:222..1055"
                     /db_xref="GeneID:83584"
                     /db_xref="RGD:70967"
ORIGIN      
        1 mtetdgfyrs revldpaeqy kmdhkrrgta lifnherffw hlalperrgt nadrdnltrr
       61 fselgfevkc fndlraeell lkihevstss hvdadcflcv flshgegnhi yaydakieiq
      121 tltglfkgdk cqslvgkpki fiiqacrgsq hdvpvvpldv vdhqtdkldd nvtqvdaasv
      181 ytlpagadfl mcysvaegyy shretvngsw yiqdlcemla rhgsslefte lltlvnrkvs
      241 qrrvdfckdp gaigkkqvpc fasmltkklh fcpkpsk
//
LOCUS       NP_001019929             558 aa            linear   ROD 28-APR-2025
DEFINITION  protein polyglycylase TTLL10 isoform 2 [Rattus norvegicus].
ACCESSION   NP_001019929 XP_233723
VERSION     NP_001019929.1
DBSOURCE    REFSEQ: accession NM_001024758.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Rogowski,K., Juge,F., van Dijk,J., Wloga,D., Strub,J.M.,
            Levilliers,N., Thomas,D., Bre,M.H., Van Dorsselaer,A., Gaertig,J.
            and Janke,C.
  TITLE     Evolutionary divergence of enzymatic mechanisms for
            posttranslational polyglycylation
  JOURNAL   Cell 137 (6), 1076-1087 (2009)
   PUBMED   19524510
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097417.1 and CK653520.1.
            
            On Jun 13, 2005 this sequence version replaced XP_233723.3.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The resulting
            isoform (2) lacks an internal segment, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097417.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..558
                     /product="protein polyglycylase TTLL10 isoform 2"
                     /EC_number="6.-.-.-"
                     /note="protein polyglycylase TTLL10; tubulin--tyrosine
                     ligase-like protein 10; tubulin tyrosine ligase-like
                     family, member 10"
                     /calculated_mol_wt=63323
     Region          154..407
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     CDS             1..558
                     /gene="Ttll10"
                     /coded_by="NM_001024758.2:184..1860"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:298692"
                     /db_xref="RGD:1560839"
ORIGIN      
        1 mgssveeglr pelsqleqda dnlgeeeaar lpvtslngll megdrhpnpg qgpffyiggt
       61 ngasiisnyc eskgwqrtqd srcedyklkw ceikcrdnyc sfregqqllf qlpnnklltt
      121 kigllsalre hartlskarl mpstqakvlk mdeffpetyr ldirderqaf ftlfdetqmw
      181 ickptasnqg kgiflirsqe eaaalqaktq sieddpiyrk mpfrapqarv vqryvqnpll
      241 ldgkkfdvrs ymliacampy mvffghgyar ltlslynphs sdlsghltnq fmqkksplym
      301 llkdstvwsm ehlnryindk frkskglprd wvfttftkrm qqimshcfla vksklecklg
      361 yfdligcdfl idenfkvwll emnsnpalht ncevlkevip gvvmetldla letcqkslhs
      421 qkmlplqsqr rfvllynget tdlwprlgss rppirlpyan snharstcei ssssltstrv
      481 tiadrpaark smssrtapic asrksrlsds ggvsieeset svcsglpegs rdaarepslg
      541 pteeereeeq rstshrgs
//
LOCUS       NP_001011941             335 aa            linear   ROD 28-APR-2025
DEFINITION  hsp90 co-chaperone Cdc37-like 1 [Rattus norvegicus].
ACCESSION   NP_001011941 XP_215233
VERSION     NP_001011941.1
DBSOURCE    REFSEQ: accession NM_001011941.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Scholz,G.M., Cartledge,K. and Hall,N.E.
  TITLE     Identification and characterization of Harc, a novel
            Hsp90-associating relative of Cdc37
  JOURNAL   J Biol Chem 276 (33), 30971-30979 (2001)
   PUBMED   11413142
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083761.1.
            
            On Feb 11, 2005 this sequence version replaced XP_215233.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083761.1, SRR8487226.162359.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q52"
     Protein         1..335
                     /product="hsp90 co-chaperone Cdc37-like 1"
                     /note="cell division cycle 37 homolog-like 1"
                     /calculated_mol_wt=38184
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Region          2..170
                     /region_name="Self-association. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L3B6; propagated from
                     UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Region          <71..139
                     /region_name="CDC37_N"
                     /note="Cdc37 N terminal kinase binding; cl03951"
                     /db_xref="CDD:446243"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7L3B6; propagated from
                     UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Region          145..277
                     /region_name="CDC37_M"
                     /note="Cdc37 Hsp90 binding domain; smart01070"
                     /db_xref="CDD:215010"
     Region          147..276
                     /region_name="Self-association and interaction with Hsp90.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Region          266..335
                     /region_name="Interaction with Hsp70.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC3.1)"
     Region          277..335
                     /region_name="Required for interaction with STIP1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIC3.1)"
     CDS             1..335
                     /gene="Cdc37l1"
                     /gene_synonym="Cdc37l"
                     /coded_by="NM_001011941.1:97..1104"
                     /db_xref="GeneID:293886"
                     /db_xref="RGD:1309295"
ORIGIN      
        1 meqpwpppgp wsfprtgget eeesdldvsp ssshyspvpd ggaqmyshgi elacqrqkef
       61 vkssvackwn laeaqqklgs lalhnsesld qehakaqtav selrqreeew rqkeealvqr
      121 ertclwnvda iskdvfnksf inqdkrkted edksqsfmqk yeqkirhfgm lsrwddsqrf
      181 lsdhpylvce etakylilwc fhleaeqkga lmeqiahqav vmqfimemak ncnvdprgcf
      241 rlffqkakae eegyfeafkn eleafkarvr lyaqsqsfap vtvenhaphs gvgcigsaep
      301 lpqnpdslqc cppaplcsvd svvhkedddr mmdtv
//
LOCUS       NP_001014176             633 aa            linear   ROD 28-APR-2025
DEFINITION  dynein axonemal assembly factor 1 [Rattus norvegicus].
ACCESSION   NP_001014176 XP_341698
VERSION     NP_001014176.1
DBSOURCE    REFSEQ: accession NM_001014154.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Duquesnoy,P., Escudier,E., Vincensini,L., Freshour,J.,
            Bridoux,A.M., Coste,A., Deschildre,A., de Blic,J., Legendre,M.,
            Montantin,G., Tenreiro,H., Vojtek,A.M., Loussert,C., Clement,A.,
            Escalier,D., Bastin,P., Mitchell,D.R. and Amselem,S.
  TITLE     Loss-of-function mutations in the human ortholog of Chlamydomonas
            reinhardtii ODA7 disrupt dynein arm assembly and cause primary
            ciliary dyskinesia
  JOURNAL   Am J Hum Genet 85 (6), 890-896 (2009)
   PUBMED   19944405
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Loges,N.T., Olbrich,H., Becker-Heck,A., Haffner,K., Heer,A.,
            Reinhard,C., Schmidts,M., Kispert,A., Zariwala,M.A., Leigh,M.W.,
            Knowles,M.R., Zentgraf,H., Seithe,H., Nurnberg,G., Nurnberg,P.,
            Reinhardt,R. and Omran,H.
  TITLE     Deletions and point mutations of LRRC50 cause primary ciliary
            dyskinesia due to dynein arm defects
  JOURNAL   Am J Hum Genet 85 (6), 883-889 (2009)
   PUBMED   19944400
REFERENCE   3  (residues 1 to 633)
  AUTHORS   van Rooijen,E., Giles,R.H., Voest,E.E., van Rooijen,C.,
            Schulte-Merker,S. and van Eeden,F.J.
  TITLE     LRRC50, a conserved ciliary protein implicated in polycystic kidney
            disease
  JOURNAL   J Am Soc Nephrol 19 (6), 1128-1138 (2008)
   PUBMED   18385425
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079038.1.
            
            On Apr 20, 2005 this sequence version replaced XP_341698.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..633
                     /product="dynein axonemal assembly factor 1"
                     /note="leucine-rich repeat-containing protein 50; dynein
                     assembly factor 1, axonemal; leucine rich repeat
                     containing 50"
                     /calculated_mol_wt=69825
     Region          1..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          101..123
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          105..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..290
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          124..145
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          146..167
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          147..168
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          168..189
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          169..190
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          190..211
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          191..215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          215..236
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          216..240
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          241..268
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <294..>379
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          326..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          404..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYH9.1)"
     Region          538..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYH9.1)"
     CDS             1..633
                     /gene="Dnaaf1"
                     /gene_synonym="Lrrc50; RGD1310542"
                     /coded_by="NM_001014154.1:64..1965"
                     /db_xref="GeneID:361419"
                     /db_xref="RGD:1310542"
ORIGIN      
        1 mhpeaseppv dsaaepslee sagdhgdagp gvrkeeinet ketcvgpctt scqsqqqpsg
       61 dngsdglfth srddrddrgp rmtkqflqkl ckqhklyvtp alndtlylhf kgfdrienle
      121 eytglrclwl ecngiqrien lqaqselrcl flqvnllhki enleplqkld alnlsnnyik
      181 tienlsclpv lntlqmahnr letvadiehl reclqlcvld lshnslsdpe ilsvletmpc
      241 lrvlnlmgnp vtkhipnyrr tvtvrlkhlt ylddrpvfpk dracaeawar ggyaaekeer
      301 hqwesrehkk itdslealam ikrraeerkk ardrgetplp eseksiptsp eaqekppkge
      361 tqqkmesfvk esfeakdelf pekpgegeel svvvgnrave dadlsgnlah tqtpvvvtpe
      421 evtspveatd gartedteai aletkeklfi ddlpdledvd gtdvsvedqt kdtgirkiqa
      481 isslsddsdl eleelplsvf egtpisptga lshifavskd pseaarvpfa dicmptattd
      541 letqsqdpst asshpliqel gedelteges nqplppqsca sdptlaqsse ggdsqlpaat
      601 plgdgaenea qsslypeeps trigledief gld
//
LOCUS       NP_001102264             504 aa            linear   ROD 28-APR-2025
DEFINITION  CCR4-NOT transcription complex subunit 11 [Rattus norvegicus].
ACCESSION   NP_001102264 XP_001058746 XP_343561
VERSION     NP_001102264.1
DBSOURCE    REFSEQ: accession NM_001108794.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Bawankar,P., Loh,B., Wohlbold,L., Schmidt,S. and Izaurralde,E.
  TITLE     NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT
            complex that docks onto the NOT1 N-terminal domain
  JOURNAL   RNA Biol 10 (2), 228-244 (2013)
   PUBMED   23303381
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Mauxion,F., Preve,B. and Seraphin,B.
  TITLE     C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex
  JOURNAL   RNA Biol 10 (2), 267-276 (2013)
   PUBMED   23232451
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Lau,N.C., Kolkman,A., van Schaik,F.M., Mulder,K.W., Pijnappel,W.W.,
            Heck,A.J. and Timmers,H.T.
  TITLE     Human Ccr4-Not complexes contain variable deadenylase subunits
  JOURNAL   Biochem J 422 (3), 443-453 (2009)
   PUBMED   19558367
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC158750.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_343561.3, XP_001058746.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158750.1, FQ233266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..504
                     /product="CCR4-NOT transcription complex subunit 11"
                     /note="UPF0760 protein C2orf29 homolog"
                     /calculated_mol_wt=54705
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA9.1)"
     Site            38
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9UKZ1; propagated from
                     UniProtKB/Swiss-Prot (B0BNA9.1)"
     Region          226..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BNA9.1)"
     Region          365..488
                     /region_name="CNOT11"
                     /note="CCR4-NOT transcription complex subunit 11;
                     pfam10155"
                     /db_xref="CDD:401964"
     CDS             1..504
                     /gene="Cnot11"
                     /gene_synonym="RGD1560909"
                     /coded_by="NM_001108794.2:73..1587"
                     /db_xref="GeneID:363221"
                     /db_xref="RGD:1560909"
ORIGIN      
        1 mpgggastas grllsadprg areaaafrsg pagssggrgg aggpgsgsgg pagrmsltpk
       61 elssllsiis eeagggstfe glstafhhyf skadhfrlgs vlvmllqqpd llpsaaqrlt
      121 alyllwemyr teplaanpfa asfahllnpa pparggqepd rpplsgflpp itppekffls
      181 qlmlapprel fkktprqial mdvgnmgqsv disglqlala erqselptqs kasfpsilsd
      241 pdpdssnsaf dssvasrite slvsgpkppi eshfrpefir pppplhiced elawlnptep
      301 ehaiqwdrsm cvknstgvei krimakafks plsspqqtql lgelekdpkl vyhigltpak
      361 lpdlvennpl vaiemllklm qssqiteyfs vlvnmdmslh smevvnrltt avdlppefih
      421 lyisncistc eqikdkymqn rlvrlvcvfl qslirnkiin vqdlfievqa fciefsrire
      481 aaglfrllkt ldtgetpset kvsk
//
LOCUS       NP_001030092             497 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-C [Rattus norvegicus].
ACCESSION   NP_001030092 XP_214861
VERSION     NP_001030092.1
DBSOURCE    REFSEQ: accession NM_001034920.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Kim,M., Tezuka,T., Tanaka,K. and Yamamoto,T.
  TITLE     Cbl-c suppresses v-Src-induced transformation through
            ubiquitin-dependent protein degradation
  JOURNAL   Oncogene 23 (9), 1645-1655 (2004)
   PUBMED   14661060
  REMARK    Erratum:[Oncogene. 2004 Oct 14;23(47):7903-4]
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Keane,M.M., Ettenberg,S.A., Nau,M.M., Banerjee,P., Cuello,M.,
            Penninger,J. and Lipkowitz,S.
  TITLE     cbl-3: a new mammalian cbl family protein
  JOURNAL   Oncogene 18 (22), 3365-3375 (1999)
   PUBMED   10362357
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN934498.1 and BC105776.1.
            
            On Oct 21, 2005 this sequence version replaced XP_214861.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105776.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..497
                     /product="E3 ubiquitin-protein ligase CBL-C"
                     /EC_number="2.3.2.27"
                     /note="Casitas B-lineage lymphoma c; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence c; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase C; Cbl
                     proto-oncogene C, E3 ubiquitin protein ligase; RING-type
                     E3 ubiquitin transferase CBL-C"
                     /calculated_mol_wt=55675
     Region          7..145
                     /region_name="4H"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8H4.1)"
     Region          13..145
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          146..218
                     /region_name="EF-hand-like"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8H4.1)"
     Region          149..232
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          219..321
                     /region_name="SH2-like"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8H4.1)"
     Region          226..322
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(244,264,266..269,274,286,288)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(289..292,305..307)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          322..350
                     /region_name="Linker. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8H4.1)"
     Region          336..400
                     /region_name="RING-HC_Cbl-c"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-c and similar proteins;
                     cd16710"
                     /db_xref="CDD:438370"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:Q9ULV8; propagated from
                     UniProtKB/Swiss-Prot (G3V8H4.1)"
     Region          351..497
                     /region_name="Interaction with RET. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (G3V8H4.1)"
     CDS             1..497
                     /gene="Cblc"
                     /coded_by="NM_001034920.2:23..1516"
                     /db_xref="GeneID:292699"
                     /db_xref="RGD:1307651"
ORIGIN      
        1 maaatapqgw qwgepralgr avkllqrlee qcrdlrlfvg ppslrdllpr taqllrevak
       61 arsdktrgdp egpggagdfl viyltnleak grqvaellph rgkkdanqdv fpegsrfrrq
      121 laklalifsh mhaelsalfp egkycghlyq itkgsantfw rencgvrcvl pwaefqsllc
      181 schpvepgpi mqalrstldl tcsghvsvfe fdiftrlfqp wptllknwql lavnhpgyma
      241 fltydevqtr lqayrdkpgs yifrpsctrl gqwaigyvss ngsilqtipl nkpllqvllk
      301 gqkdgiflyp dgknhnpdlt elcraelnqc iqvsqeqlql yqamnstfel ckicterdkd
      361 vriepcghll cscclaawqh sdsqtcpfcr ceikgreavs icqaqersme vrttagdsgd
      421 nchqeaaewk lesvtpsapp lppevpcpqr pqdkgwltla pftlprlrpp lplpkmasvl
      481 wevtsrpqvr egatess
//
LOCUS       NP_001095298             398 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF11 [Rattus norvegicus].
ACCESSION   NP_001095298 XP_001064047 XP_574883
VERSION     NP_001095298.1
DBSOURCE    REFSEQ: accession NM_001101828.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Morokuma,Y., Nakamura,N., Kato,A., Notoya,M., Yamamoto,Y.,
            Sakai,Y., Fukuda,H., Yamashina,S., Hirata,Y. and Hirose,S.
  TITLE     MARCH-XI, a novel transmembrane ubiquitin ligase implicated in
            ubiquitin-dependent protein sorting in developing spermatids
  JOURNAL   J Biol Chem 282 (34), 24806-24815 (2007)
   PUBMED   17604280
  REMARK    GeneRIF: MARCH-XI acts as a ubiquitin ligase with a role in
            ubiquitin-mediated protein sorting in the TGN-MVB transport
            pathway, which may be involved in mammalian spermiogenesis
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK596283.1, AB048841.1 and AW528861.1.
            
            On or before Dec 7, 2007 this sequence version replaced
            XP_001064047.1, XP_574883.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB048841.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q22"
     Protein         1..398
                     /product="E3 ubiquitin-protein ligase MARCHF11"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase MARCH11;
                     membrane-associated RING finger protein 11;
                     membrane-associated RING-CH protein XI;
                     membrane-associated ring finger (C3HC4) 11; RING-type E3
                     ubiquitin transferase MARCH11; RING-type E3 ubiquitin
                     transferase MARCHF11"
                     /calculated_mol_wt=43795
     Region          1..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6P320.1)"
     Region          164..223
                     /region_name="RING_CH-C4HC3_MARCH11"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH11 (MARCH11); cd16810"
                     /db_xref="CDD:438460"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6P320.1)"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (A6P320.1)"
     Region          367..370
                     /region_name="YXXL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (A6P320.1)"
     Region          395..398
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (A6P320.1)"
     CDS             1..398
                     /gene="Marchf11"
                     /gene_synonym="MARCH-XI; March11; RGD1559945"
                     /coded_by="NM_001101828.1:205..1401"
                     /db_xref="GeneID:499558"
                     /db_xref="RGD:1559945"
ORIGIN      
        1 msdegskrgs radsleaepp lppppppppp gesslvptsp ryrpplpapl erivgsgepp
       61 velaprrkge plpplppsrl pgdqevsaag dscegprrlp evklpeaaag kgspaepeag
      121 acgegerrgt gdqpetrsvc ssrssssggs gdqrsghqhq hhqpickicf qgaeqgelln
      181 pcrcdgsvry thqlcllkwi sergswtcel ccyryhvtai kmkqpcqwqs isitlvekvq
      241 miavilgslf liasvtwllw safspyavwq rkdilfqicy gmygfmdlvc iglivhegaa
      301 vyrvfkrwra vnlhwdvlny dkatdieess rgesstsrtl wlplsalrnr nlvhptqlts
      361 prfqcgyvll hlfnrmrahe dvsedngsge vvmrvtsv
//
LOCUS       NP_001096830             134 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich nuclear receptor coactivator 2 [Rattus norvegicus].
ACCESSION   NP_001096830
VERSION     NP_001096830.1
DBSOURCE    REFSEQ: accession NM_001103360.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Cho,H., Kim,K.M. and Kim,Y.K.
  TITLE     Human proline-rich nuclear receptor coregulatory protein 2 mediates
            an interaction between mRNA surveillance machinery and decapping
            complex
  JOURNAL   Mol Cell 33 (1), 75-86 (2009)
   PUBMED   19150429
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081903.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081903.1, EV763414.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00155329, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..134
                     /product="proline-rich nuclear receptor coactivator 2"
                     /calculated_mol_wt=14750
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE1.1)"
     Region          88..106
                     /region_name="PNRC"
                     /note="Proline-rich nuclear receptor coactivator motif;
                     pfam15365"
                     /db_xref="CDD:464675"
     Region          94..100
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HE1.1)"
     CDS             1..134
                     /gene="Pnrc2"
                     /coded_by="NM_001103360.1:372..776"
                     /db_xref="GeneID:100125373"
                     /db_xref="RGD:1642418"
ORIGIN      
        1 mgggerynip dpqsrnaskn qqqhnrqktk dqnsqmkivh kkkerghgyn psavqnggkt
       61 kslsnnsnwn aslsspsllf ksqasqnyag akfseppsps vlpkppshwv hvslnpsdke
      121 tmtfqlktll kvqv
//
LOCUS       NP_001032855            2136 aa            linear   ROD 28-APR-2025
DEFINITION  U5 small nuclear ribonucleoprotein 200 kDa helicase [Rattus
            norvegicus].
ACCESSION   NP_001032855 XP_215831
VERSION     NP_001032855.2
DBSOURCE    REFSEQ: accession NM_001037766.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2136)
  AUTHORS   Zhan,X., Yan,C., Zhang,X., Lei,J. and Shi,Y.
  TITLE     Structure of a human catalytic step I spliceosome
  JOURNAL   Science 359 (6375), 537-545 (2018)
   PUBMED   29301961
REFERENCE   2  (residues 1 to 2136)
  AUTHORS   Haselbach,D., Komarov,I., Agafonov,D.E., Hartmuth,K., Graf,B.,
            Dybkov,O., Urlaub,H., Kastner,B., Luhrmann,R. and Stark,H.
  TITLE     Structure and Conformational Dynamics of the Human Spliceosomal
            Bact Complex
  JOURNAL   Cell 172 (3), 454-464 (2018)
   PUBMED   29361316
REFERENCE   3  (residues 1 to 2136)
  AUTHORS   Pabis,M., Neufeld,N., Steiner,M.C., Bojic,T., Shav-Tal,Y. and
            Neugebauer,K.M.
  TITLE     The nuclear cap-binding complex interacts with the U4/U6.U5
            tri-snRNP and promotes spliceosome assembly in mammalian cells
  JOURNAL   RNA 19 (8), 1054-1063 (2013)
   PUBMED   23793891
REFERENCE   4  (residues 1 to 2136)
  AUTHORS   Chang,T.H., Tung,L., Yeh,F.L., Chen,J.H. and Chang,S.L.
  TITLE     Functions of the DExD/H-box proteins in nuclear pre-mRNA splicing
  JOURNAL   Biochim Biophys Acta 1829 (8), 764-774 (2013)
   PUBMED   23454554
  REMARK    Review article
REFERENCE   5  (residues 1 to 2136)
  AUTHORS   Zhang,L., Li,X. and Zhao,R.
  TITLE     Structural analyses of the pre-mRNA splicing machinery
  JOURNAL   Protein Sci 22 (6), 677-692 (2013)
   PUBMED   23592432
  REMARK    Review article
REFERENCE   6  (residues 1 to 2136)
  AUTHORS   Li,N., Mei,H., MacDonald,I.M., Jiao,X. and Hejtmancik,J.F.
  TITLE     Mutations in ASCC3L1 on 2q11.2 are associated with autosomal
            dominant retinitis pigmentosa in a Chinese family
  JOURNAL   Invest Ophthalmol Vis Sci 51 (2), 1036-1043 (2010)
   PUBMED   19710410
REFERENCE   7  (residues 1 to 2136)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   8  (residues 1 to 2136)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 2136)
  AUTHORS   Laggerbauer,B., Achsel,T. and Luhrmann,R.
  TITLE     The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in
            vitro
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4188-4192 (1998)
   PUBMED   9539711
REFERENCE   10 (residues 1 to 2136)
  AUTHORS   Lauber,J., Fabrizio,P., Teigelkamp,S., Lane,W.S., Hartmann,E. and
            Luhrmann,R.
  TITLE     The HeLa 200 kDa U5 snRNP-specific protein and its homologue in
            Saccharomyces cerevisiae are members of the DEXH-box protein family
            of putative RNA helicases
  JOURNAL   EMBO J 15 (15), 4001-4015 (1996)
   PUBMED   8670905
COMMENT     INFERRED REFSEQ: This record is predicted by genome sequence
            analysis and is not yet supported by experimental evidence. The
            reference sequence was derived from JAXUCZ010000003.1.
            
            On Dec 18, 2009 this sequence version replaced NP_001032855.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2429982.1,
                                           SRR26360194.2390531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2136
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..2136
                     /product="U5 small nuclear ribonucleoprotein 200 kDa
                     helicase"
                     /EC_number="3.6.4.13"
                     /note="activating signal cointegrator 1 complex subunit
                     3-like 1; BRR2 homolog; U5 snRNP-specific 200 kDa protein;
                     small nuclear ribonucleoprotein 200 (U5)"
                     /calculated_mol_wt=244405
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          39..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          254..363
                     /region_name="Helicase_PWI"
                     /note="N-terminal helicase PWI domain; pfam18149"
                     /db_xref="CDD:436309"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          462..1017
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
     Region          464..677
                     /region_name="DEXHc_Brr2_1"
                     /note="N-terminal DEXH-box helicase domain of spliceosomal
                     Brr2 RNA helicase; cd18019"
                     /db_xref="CDD:350777"
     Site            order(480,482,485,506..510,615..616)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350777"
     Site            order(544..546,572..576,578..579,589,591..592,595,599,624)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350777"
     Region          615..618
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:16641100; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            971
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          982..1285
                     /region_name="Sec63"
                     /note="Sec63 Brl domain; pfam02889"
                     /db_xref="CDD:460740"
     Region          1282..2136
                     /region_name="Interaction with TSSC4.
                     /evidence=ECO:0000250|UniProtKB:O75643"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          1309..1849
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
     Region          1325..1515
                     /region_name="DEXHc_Brr2_2"
                     /note="C-terminal D[D/E]X[H/Q]-box helicase domain of
                     spliceosomal Brr2 RNA helicase; cd18021"
                     /db_xref="CDD:350779"
     Site            order(1325,1327..1329,1332,1351..1357)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350779"
     Site            1428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          1454..1457
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            1765
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T2; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Region          1809..2125
                     /region_name="SEC63"
                     /note="Domain of unknown function in Sec63p, Brr2p and
                     other proteins; smart00611"
                     /db_xref="CDD:214744"
     Site            2002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            2131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            2133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     Site            2135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O75643; propagated from
                     UniProtKB/Swiss-Prot (F1LNJ2.1)"
     CDS             1..2136
                     /gene="Snrnp200"
                     /gene_synonym="Ascc3l1; U5-200KD"
                     /coded_by="NM_001037766.2:111..6521"
                     /db_xref="GeneID:296126"
                     /db_xref="RGD:1561120"
ORIGIN      
        1 madvtarslq yeykansnlv lqadrslidr trrdeptgev lslvgklegt rmgdkaqrtk
       61 pqmqeerrak rrkrdedrhd inkmkgytll segidemvgi iykpktketr etyevllsfi
      121 qaalgdqprd ilcgaadevl avlkneklrd kerrreidll lgqtddtryh vlvnlgkkit
      181 dyggdkeiqn mddnidetyg vnvqfesdee egdedvygev reeasdddme gdeavvrctl
      241 sanlvasgel msskkkdlhp rdidafwlqr qlsrfyddai vsqkkadevl eilktasddr
      301 ecenqlvlll gfntfdfikv lrqhrmmily ctllasaqse aekerimgkm eadpelskfl
      361 yqlheteked lireersrre rvrqsrmdtd letmdldqgg ealaprqvld ledlvftqgs
      421 hfmankrcql pdgsfrrqrk gyeevhvpal kpkpfgseeq llpveklpky aqagfegfkt
      481 lnriqsklyr aaletdenll lcaptgagkt nvalmcmlre igkhinmdgt invddfkiiy
      541 iapmrslvqe mvgsfgkrla tygitvaelt gdhqlckeei satqiivctp ekwdiitrkg
      601 gertytqlvr livldeihll hddrgpvlea lvarairnie mtqedvrlig lsatlpnyed
      661 vatflrvdpa kglfyfdnsf rpvpleqtyv gitekkaikr fqimneivye kimehagknq
      721 vlvfvhsrke tgktaraird mclekdtlgl flregsaste vlrteaeqck nlelkdllpy
      781 gfaihhagmt rvdrtlvedl fadkhiqvlv statlawgvn lpahtviikg tqvyspekgr
      841 wtelgaldil qmlgragrpq ydtkgegili tshgelqyyl sllnqqlpie sqmvsklpdm
      901 lnaeivlgnv qnakdavnwl gyaylyirml rsptlygish ddlkgdplld qrrldlvhta
      961 almldknnlv kydkktgnfq vtelgriash yyitndtvqt ynqllkptls eielfrvfsl
     1021 ssefknitvr eeeklelqkl lervpipvke sieepsakin vllqafisql klegfalmad
     1081 mvyvtqsagr lmraifeivl nrgwaqltdk tlnlckmidk rmwqsmcplr qfrklpeevv
     1141 kkiekknfpf erlydlnhne igelirmpkm gktihkyvhl fpklelsvhl qpitrstlkv
     1201 eltitpdfqw dekvhgssea fwilvedvds evilhheyfl lkakyaqdeh litffvpvfe
     1261 plppqyfirv vsdrwlscet qlpvsfrhli lpekypppte lldlqplpvs alrnsafesl
     1321 yqdkfpffnp iqtqvfntvy nsddnvfvga ptgsgktica efailrmllq nsegrcvyit
     1381 pmealaeqvy mdwyekfqdr lnkkvvlltg etstdlkllg kgniiistpe kwdilsrrwk
     1441 qrknvqninl fvvdevhlig gengpvlevi csrmryissq ierpirival ssslsnakdv
     1501 ahwlgcsats tfnfhpnvrp vplelhiqgf nishtqtrll smakpvyhai tkhspkkpvi
     1561 vfvpsrkqtr ltaidilttc aadiqrqrfl hctekdlipy leklsdstlk etllngvgyl
     1621 heglspmerr lveqlfssga iqvvvasrsl cwgmnvaahl viimdtqyyn gkihayvdyp
     1681 iydvlqmvgh anrplqddeg rcvimcqgsk kdffkkflye plpveshldh cmhdhfnaei
     1741 vtktienkqd avdyltwtfl yrrmtqnpny ynlqgishrh lsdhlselve qtlsdleqsk
     1801 cisiedemdv aplnlgmiaa yyyinyttie lfsmslnakt kvrglieiis naaeyenipi
     1861 rhhednllrq laqkvphkln npkfndphvk tnlllqahls rmqlsaelqs dteeilskai
     1921 rliqacvdvl ssngwlspal aamelaqmvt qamwskdsyl kqlphftseh ikrctdkgve
     1981 svfdimemed eernallqlt dsqiadvarf cnrypniels yevvdkdsir sggpvvvlvq
     2041 lereeevtgp viaplfpqkr eegwwvvigd aksnslisik rltlqqkakv kldfvapatg
     2101 ghnytlyfms daymgcdqey kfsvdvkeae tdsdsd
//
LOCUS       NP_001013880             247 aa            linear   ROD 28-APR-2025
DEFINITION  TLC domain-containing protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_001013880 XP_213376
VERSION     NP_001013880.1
DBSOURCE    REFSEQ: accession NM_001013858.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Ruiz,M., Bodhicharla,R., Svensk,E., Devkota,R., Busayavalasa,K.,
            Palmgren,H., Stahlman,M., Boren,J. and Pilon,M.
  TITLE     Membrane fluidity is regulated by the C. elegans transmembrane
            protein FLD-1 and its human homologs TLCD1/2
  JOURNAL   Elife 7, e40686 (2018)
   PUBMED   30509349
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085876.1.
            
            On Apr 20, 2005 this sequence version replaced XP_213376.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085876.1, CO405247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q25"
     Protein         1..247
                     /product="TLC domain-containing protein 1 precursor"
                     /note="TLC domain-containing protein 1; calfacilitin"
                     /calculated_mol_wt=25675
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U2T1.1)"
                     /calculated_mol_wt=3073
     mat_peptide     28..247
                     /product="TLC domain-containing protein 1.
                     /id=PRO_0000285679"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T1.1)"
                     /calculated_mol_wt=25675
     Region          41..234
                     /region_name="TLC"
                     /note="TRAM, LAG1 and CLN8 homology domains; smart00724"
                     /db_xref="CDD:214789"
     Site            47..67
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T1.1)"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T1.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T1.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T1.1)"
     CDS             1..247
                     /gene="Tlcd1"
                     /coded_by="NM_001013858.1:132..875"
                     /db_xref="GeneID:287472"
                     /db_xref="RGD:1359195"
ORIGIN      
        1 mplllhpawp lllgatltfr alrrvlcrlp lpahvqtdpl rtwrwhnllv sfthsivsgi
       61 wallciwqtp emlveietaw svcgyllvcf sagyfihdtv divvsrqtra sweylvhhvm
      121 amgaffsgif wkrfvgggvl tllvevsnif ltlrmmmkin naqdillykv nkyvnlvmyf
      181 lfrlapqayl tkfflqyagq rtlgtfllsi llmldvmili yfsrllrsdf cperapsrqq
      241 kdkflte
//
LOCUS       NP_001012113             473 aa            linear   ROD 28-APR-2025
DEFINITION  phosphatidylserine synthase 1 [Rattus norvegicus].
ACCESSION   NP_001012113 XP_234787
VERSION     NP_001012113.1
DBSOURCE    REFSEQ: accession NM_001012113.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Stone,S.J. and Vance,J.E.
  TITLE     Phosphatidylserine synthase-1 and -2 are localized to
            mitochondria-associated membranes
  JOURNAL   J Biol Chem 275 (44), 34534-34540 (2000)
   PUBMED   10938271
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087129.1.
            
            On Feb 11, 2005 this sequence version replaced XP_234787.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087129.1, SRR8487231.140665.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..473
                     /product="phosphatidylserine synthase 1"
                     /EC_number="2.7.8.29"
                     /note="ptdSer synthase 1; serine-exchange enzyme I"
                     /calculated_mol_wt=55533
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P48651; propagated from
                     UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            73..93
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Region          96..372
                     /region_name="PSS"
                     /note="Phosphatidyl serine synthase; pfam03034"
                     /db_xref="CDD:460783"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            320..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            356..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48651; propagated from
                     UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48651; propagated from
                     UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Region          430..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48651; propagated from
                     UniProtKB/Swiss-Prot (Q5PQL5.1)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48651; propagated from
                     UniProtKB/Swiss-Prot (Q5PQL5.1)"
     CDS             1..473
                     /gene="Ptdss1"
                     /gene_synonym="PSS-1"
                     /coded_by="NM_001012113.1:108..1529"
                     /db_xref="GeneID:314553"
                     /db_xref="RGD:1308949"
ORIGIN      
        1 mascvgsrtl skddvnyrmh frmineqqve ditidffyrp htitllsfti islmyfaftr
       61 ddcvpedniw rgilsvifff liisvlafpn gpftrphpal wrmvfglsvl yflflvfllf
      121 lnfeqvkslm ywldpnlrya treadimeya vnchvitwer ivshfdifaf ghfwgwamka
      181 llirsyglcw tisitwelte lffmhllpnf aecwwdqvil dillcngggi wlgmvvcrfl
      241 emrtyhwasf kdihtttgki kravlqftpa swtyvrwfdp kssfqrvagi ylfmiiwqlt
      301 elntfflkhi fvfqashpls wcrilfigci taptvrqyya yltdtqckrv gtqcwvfgvi
      361 gfleaivcik fgqdlfsktq ilyvvlwllc vafttflcly gmvwyaehyg hrektysece
      421 dgtyspeisw yhgkgskgse dsppkhsnnn eshssrrrnr hskskvtngv gkk
//
LOCUS       NP_001258063             194 aa            linear   ROD 28-APR-2025
DEFINITION  myelin-associated neurite-outgrowth inhibitor [Rattus norvegicus].
ACCESSION   NP_001258063 XP_001073605
VERSION     NP_001258063.1
DBSOURCE    REFSEQ: accession NM_001271134.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Mishra,M., Lee,S., Lin,M.K., Yamashita,T. and Heese,K.
  TITLE     Characterizing the neurite outgrowth inhibitory effect of Mani
  JOURNAL   FEBS Lett 586 (19), 3018-3023 (2012)
   PUBMED   22771904
  REMARK    GeneRIF: Considering the protein structure of Mani obtained via a
            series of bio-computational studies, we propose a
            Cdc27-Mani-APC-related signalling pathway may be involved in CNS
            axon regeneration.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            On Sep 1, 2012 this sequence version replaced XP_001073605.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643291.25184.1,
                                           SRR26643288.37082.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760393,
                                           SAMEA5760433 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q21"
     Protein         1..194
                     /product="myelin-associated neurite-outgrowth inhibitor"
                     /note="protein FAM168B; mani"
                     /calculated_mol_wt=20063
     Region          1..194
                     /region_name="TCRP1"
                     /note="Tongue Cancer Chemotherapy Resistant Protein 1;
                     pfam14944"
                     /db_xref="CDD:434335"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:A1KXE4; propagated from
                     UniProtKB/Swiss-Prot (D4AEP3.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A1KXE4; propagated from
                     UniProtKB/Swiss-Prot (D4AEP3.1)"
     Site            19..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AEP3.1)"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D4AEP3.1)"
     Site            142..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D4AEP3.1)"
     CDS             1..194
                     /gene="Fam168b"
                     /coded_by="NM_001271134.1:183..767"
                     /db_xref="GeneID:690188"
                     /db_xref="RGD:1583985"
ORIGIN      
        1 mnpvyspgss gvpyanakgi gypagfpvgy aaapayspnm ypganptfqt gytpgtpykv
       61 scsptsgavp pyssspnpyq tavypvrsay pqqspyaqqg tyytqplyaa pphvihhttv
      121 vqpngmpatv ypapippprg sgvtmgmvag ttmamsagtl ltahsptpva phpvtvptyr
      181 apgtptysyv ppqw
//
LOCUS       NP_001007728             141 aa            linear   ROD 28-APR-2025
DEFINITION  ly6/PLAUR domain-containing protein 1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001007728 XP_341114
VERSION     NP_001007728.1
DBSOURCE    REFSEQ: accession NM_001007727.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Wu,M., Puddifoot,C.A., Taylor,P. and Joiner,W.J.
  TITLE     Mechanisms of inhibition and potentiation of alpha4beta2 nicotinic
            acetylcholine receptors by members of the Ly6 protein family
  JOURNAL   J Biol Chem 290 (40), 24509-24518 (2015)
   PUBMED   26276394
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Tekinay,A.B., Nong,Y., Miwa,J.M., Lieberam,I., Ibanez-Tallon,I.,
            Greengard,P. and Heintz,N.
  TITLE     A role for LYNX2 in anxiety-related behavior
  JOURNAL   Proc Natl Acad Sci U S A 106 (11), 4477-4482 (2009)
   PUBMED   19246390
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Egerod,K.L., Holst,B., Petersen,P.S., Hansen,J.B., Mulder,J.,
            Hokfelt,T. and Schwartz,T.W.
  TITLE     GPR39 splice variants versus antisense gene LYPD1: expression and
            regulation in gastrointestinal tract, endocrine pancreas, liver,
            and white adipose tissue
  JOURNAL   Mol Endocrinol 21 (7), 1685-1698 (2007)
   PUBMED   17488974
  REMARK    GeneRIF: The 3' exon of the GPR39 gene overlaps with antisense gene
            LYPD1.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082032.1.
            
            On Nov 29, 2004 this sequence version replaced XP_341114.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082032.1, CK474993.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q12"
     Protein         1..141
                     /product="ly6/PLAUR domain-containing protein 1 precursor"
                     /note="ly6/PLAUR domain-containing protein 1"
                     /calculated_mol_wt=13181
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2167
     mat_peptide     21..115
                     /product="Ly6/PLAUR domain-containing protein 1.
                     /id=PRO_0000226745"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H42.1)"
                     /calculated_mol_wt=10374
     Region          22..107
                     /region_name="TFP_LU_ECD_LYPD1"
                     /note="extracellular domain (ECD) found in Ly6/PLAUR
                     domain-containing protein 1 (LYPD1) and similar proteins;
                     cd23559"
                     /db_xref="CDD:467089"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q66H42.1)"
     CDS             1..141
                     /gene="Lypd1"
                     /gene_synonym="Lypdc1"
                     /coded_by="NM_001007727.1:303..728"
                     /db_xref="GeneID:360838"
                     /db_xref="RGD:1549754"
ORIGIN      
        1 mwvlgiaatf cglfwlpgla lqiqcyqcee fqlnndcssp efivnctvnv qdmcqkevme
       61 qsagimyrks cassaaclia sagyqsfcsp gklnsvcisc cntplcngpr pkkrgssasa
      121 irpelfttvl ffnlalclah c
//
LOCUS       NP_446403               1172 aa            linear   ROD 28-APR-2025
DEFINITION  guanine nucleotide exchange factor DBS isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_446403
VERSION     NP_446403.2
DBSOURCE    REFSEQ: accession NM_053951.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1172)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   2  (residues 1 to 1172)
  AUTHORS   Kostenko,E.V., Olabisi,O.O., Sahay,S., Rodriguez,P.L. and
            Whitehead,I.P.
  TITLE     Ccpg1, a novel scaffold protein that regulates the activity of the
            Rho guanine nucleotide exchange factor Dbs
  JOURNAL   Mol Cell Biol 26 (23), 8964-8975 (2006)
   PUBMED   17000758
REFERENCE   3  (residues 1 to 1172)
  AUTHORS   Ueda,S., Kataoka,T. and Satoh,T.
  TITLE     Role of the Sec14-like domain of Dbl family exchange factors in the
            regulation of Rho family GTPases in different subcellular sites
  JOURNAL   Cell Signal 16 (8), 899-906 (2004)
   PUBMED   15157669
REFERENCE   4  (residues 1 to 1172)
  AUTHORS   Rossman,K.L., Cheng,L., Mahon,G.M., Rojas,R.J., Snyder,J.T.,
            Whitehead,I.P. and Sondek,J.
  TITLE     Multifunctional roles for the PH domain of Dbs in regulating Rho
            GTPase activation
  JOURNAL   J Biol Chem 278 (20), 18393-18400 (2003)
   PUBMED   12637522
REFERENCE   5  (residues 1 to 1172)
  AUTHORS   Horii,Y., Beeler,J.F., Sakaguchi,K., Tachibana,M. and Miki,T.
  TITLE     A novel oncogene, ost, encodes a guanine nucleotide exchange factor
            that potentially links Rho and Rac signaling pathways
  JOURNAL   EMBO J 13 (20), 4776-4786 (1994)
   PUBMED   7957046
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CH473970.2.
            
            On Jan 11, 2008 this sequence version replaced NP_446403.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1172
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..1172
                     /product="guanine nucleotide exchange factor DBS isoform
                     1"
                     /note="guanine nucleotide exchange factor DBS; OST
                     oncogene; DBL's big sister; MCF2-transforming
                     sequence-like protein; mcf.2 transforming sequence-like"
                     /calculated_mol_wt=131968
     Region          46..191
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     Region          322..524
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            427..432
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          603..780
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(609,613,710,732..733,736..737,739..740,743..744,
                     747..748,751,776,780)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          787..918
                     /region_name="PH_Dbs"
                     /note="DBL's big sister protein pleckstrin homology (PH)
                     domain; cd01227"
                     /db_xref="CDD:269934"
     Site            order(857,859)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269934"
     Region          1082..1134
                     /region_name="SH3_DBS"
                     /note="Src homology 3 domain of DBL's Big Sister (DBS), a
                     guanine nucleotide exchange factor; cd11857"
                     /db_xref="CDD:212791"
     Site            order(1087,1089,1092,1096,1114..1115,1130,1132..1133)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212791"
     CDS             1..1172
                     /gene="Mcf2l"
                     /gene_synonym="mcf 2l; Ost"
                     /coded_by="NM_053951.2:19..3537"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:117020"
                     /db_xref="RGD:619782"
ORIGIN      
        1 mrfwlrneem aleemvqrln avskntdeim hqdivplcaa diqeqlkkrf aylsggrgqd
       61 gspvitfpdy pafseipdke fqnvmtylts ipslqdagig filvidrrqd kwtsvkasvl
      121 riaasfpanl qlvlvlrptg ffqrtlsdia fkfnrdefkm kvpvmmlssv pelhgyidks
      181 qltedlggtl dychsrwlch rtaiesfalm vkqtaqmlqa fgtelaetel pndvqstslv
      241 lsahtekkak vkedlqlalt egnsileslr eplaesivhs vnqdqldnqa tvkrlltqln
      301 eteaafdefw akhqqkleqc lqlrhfeqgf revktaldsm sqkiaaftdv gnslahvqhl
      361 lkdlttfeek ssvavdkara lslegqqlie nrhyavdsih pkceelqhlc dhfasevtrr
      421 rdllskslel hslletsmkw sdegifllas qpvdkcqsqd gaeaalqeie kfletgaenk
      481 iqelnkiyke yecilnqdll ehvqkvfqkq esteemfhrr qaslkklaak qtrpvqpvap
      541 rpealtksps pspgswrsse nsssegnalr rgpyrrakse mseprqgrts stgeeeesla
      601 ilrrhvmnel ldterayvee llcvlegyaa emdnplmahl istglqnkkn ilfgnmeeiy
      661 hfhnriflre lescidcpel vgrcflerme efqiyekycq nkprseslwr qcsdcpffqe
      721 cqkkldhkls ldsyllkpvq ritkyqlllk emlkyskhce gaedlqeals silgilkavn
      781 dsmhliaitg ydgnlgdlgk llmqgsfsvw tdhkkghtkv kelarfkpmq rhlflhekav
      841 lfckkreeng egyekapsys ykqslnmtav gitenvkgdt kkfeiwynar eevyiiqapt
      901 peikaawvne irkvltsqlq acreasqhra leqshslplp tpastsptkg strnvkkled
      961 rktdplcleg cvssslpkpp ekgkddavps stsessalsr krftlqglan lkasptspdk
     1021 kakrhevksd ptpfglrgws ktshsleape edggwssaee linssdaeed ggvgprklvp
     1081 gkytvlmdge kggsdtlamr sgdmvevvee gteglwyvrd ltsskegwvp asslatllgk
     1141 sssaqclsss gkthcarqlc pepakilspe pv
//
LOCUS       NP_077346                467 aa            linear   ROD 28-APR-2025
DEFINITION  gamma-aminobutyric acid receptor subunit gamma-3 precursor [Rattus
            norvegicus].
ACCESSION   NP_077346
VERSION     NP_077346.3
DBSOURCE    REFSEQ: accession NM_024370.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Baer,K., Essrich,C., Benson,J.A., Benke,D., Bluethmann,H.,
            Fritschy,J.M. and Luscher,B.
  TITLE     Postsynaptic clustering of gamma-aminobutyric acid type A receptors
            by the gamma3 subunit in vivo
  JOURNAL   Proc Natl Acad Sci U S A 96 (22), 12860-12865 (1999)
   PUBMED   10536013
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Neelands,T.R. and Macdonald,R.L.
  TITLE     Incorporation of the pi subunit into functional gamma-aminobutyric
            Acid(A) receptors
  JOURNAL   Mol Pharmacol 56 (3), 598-610 (1999)
   PUBMED   10462548
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Herb,A., Wisden,W., Luddens,H., Puia,G., Vicini,S. and Seeburg,P.H.
  TITLE     The third gamma subunit of the gamma-aminobutyric acid type A
            receptor family
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1433-1437 (1992)
   PUBMED   1311098
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Knoflach,F., Rhyner,T., Villa,M., Kellenberger,S., Drescher,U.,
            Malherbe,P., Sigel,E. and Mohler,H.
  TITLE     The gamma 3-subunit of the GABAA-receptor confers sensitivity to
            benzodiazepine receptor ligands
  JOURNAL   FEBS Lett 293 (1-2), 191-194 (1991)
   PUBMED   1660002
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Sulpizio,A., Fowler,P.J. and Macko,E.
  TITLE     Antagonism of fenfluramine-induced hyperthermia: a measure of
            central serotonin inhibition
  JOURNAL   Life Sci 22 (16), 1439-1446 (1978)
   PUBMED   27681
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X63324.1 and M81142.1.
            
            On Dec 22, 2003 this sequence version replaced NP_077346.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X63324.1, M81142.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760384 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..467
                     /product="gamma-aminobutyric acid receptor subunit gamma-3
                     precursor"
                     /note="gamma-aminobutyric acid A receptor, gamma 3;
                     gamma-aminobutyric acid receptor subunit gamma-3; GABA(A)
                     receptor subunit gamma-3; GABAAR subunit gamma-3;
                     gamma-aminobutyric acid (GABA) A receptor, gamma 3;
                     GABA-alpha receptor gamma-3 subunit; gamma-aminobutyric
                     acid (GABA) A receptor, subunit gamma 3;
                     gamma-aminobutyric acid type A receptor gamma 3 subunit"
                     /calculated_mol_wt=52497
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1814
     mat_peptide     18..467
                     /product="Gamma-aminobutyric acid receptor subunit
                     gamma-3. /id=PRO_0000000483"
                     /note="propagated from UniProtKB/Swiss-Prot (P28473.1)"
                     /calculated_mol_wt=52497
     Region          50..464
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          71..252
                     /region_name="LGIC_ECD_GABAAR_G"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit gamma; cd19000"
                     /db_xref="CDD:349801"
     Site            order(78,97)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349801"
     Site            order(81,83..84,89..90,97,99..100,117,119..120,129..134,
                     137,139,141..142,148..150,152,162..164,192,252)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349801"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28473.1)"
     Region          171..185
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349801"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28473.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28473.1)"
     Site            284..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28473.1)"
     Site            312..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28473.1)"
     Site            447..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28473.1)"
     CDS             1..467
                     /gene="Gabrg3"
                     /coded_by="NM_024370.3:121..1524"
                     /db_xref="GeneID:79211"
                     /db_xref="RGD:621735"
ORIGIN      
        1 maaklllllc lfsglharsr rveeddseds psnqkwvlap ksqdtdvtli lnkllreydk
       61 klrpdigikp tvidvdiyvn sigpvssinm eyqidiffaq twtdsrlrfn stmkiltlns
      121 nmvgliwipd tifrnsktae ahwittpnql lriwndgkil ytlrltinae cqlqlhnfpm
      181 dahacpltfs sygypkeemi yrwrknsvea adqkswrlyq fdfmglrntt eivttsagdy
      241 vvmtiyfels rrmgyftiqt yipciltvvl swvsfwikkd atparttlgi ttvltmttls
      301 tiarkslprv syvtamdlfv tvcflfvfaa lmeyatlnyy sscrkptirk kktsllhpds
      361 trwipdrisl qapsnyslld mrppppvmit lnnsmywqef edtcvyecld gkdcqsffcc
      421 yeecksgswr rgrihidvse ldsysrvffp tsfllfnlvy wvgylyl
//
LOCUS       NP_620271               1258 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-dependent kinase 12 isoform 2 [Rattus norvegicus].
ACCESSION   NP_620271
VERSION     NP_620271.1
DBSOURCE    REFSEQ: accession NM_138916.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1258)
  AUTHORS   Liu,M., Fan,H., Li,T., Sihong,L., Qiao,S. and Bi,J.
  TITLE     Low expression of CDK12 in gastric cancer is correlated with
            advanced stage and poor outcome
  JOURNAL   Pathol Res Pract 216 (7), 152962 (2020)
   PUBMED   32534699
REFERENCE   2  (residues 1 to 1258)
  AUTHORS   Wang,C., Wang,H., Lieftink,C., du Chatinier,A., Gao,D., Jin,G.,
            Jin,H., Beijersbergen,R.L., Qin,W. and Bernards,R.
  TITLE     CDK12 inhibition mediates DNA damage and is synergistic with
            sorafenib treatment in hepatocellular carcinoma
  JOURNAL   Gut 69 (4), 727-736 (2020)
   PUBMED   31519701
REFERENCE   3  (residues 1 to 1258)
  AUTHORS   Ji,J., Zhou,C., Wu,J., Cai,Q., Shi,M., Zhang,H., Yu,Y., Zhu,Z. and
            Zhang,J.
  TITLE     Expression pattern of CDK12 protein in gastric cancer and its
            positive correlation with CD8+ cell density and CCL12 expression
  JOURNAL   Int J Med Sci 16 (8), 1142-1148 (2019)
   PUBMED   31523177
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1258)
  AUTHORS   Jeronimo,C., Bataille,A.R. and Robert,F.
  TITLE     The writers, readers, and functions of the RNA polymerase II
            C-terminal domain code
  JOURNAL   Chem Rev 113 (11), 8491-8522 (2013)
   PUBMED   23837720
  REMARK    Review article
REFERENCE   5  (residues 1 to 1258)
  AUTHORS   Egloff,S., Dienstbier,M. and Murphy,S.
  TITLE     Updating the RNA polymerase CTD code: adding gene-specific layers
  JOURNAL   Trends Genet 28 (7), 333-341 (2012)
   PUBMED   22622228
  REMARK    Review article
REFERENCE   6  (residues 1 to 1258)
  AUTHORS   Iorns,E., Martens-de Kemp,S.R., Lord,C.J. and Ashworth,A.
  TITLE     CRK7 modifies the MAPK pathway and influences the response to
            endocrine therapy
  JOURNAL   Carcinogenesis 30 (10), 1696-1701 (2009)
   PUBMED   19651820
REFERENCE   7  (residues 1 to 1258)
  AUTHORS   Chen,H.H., Wang,Y.C. and Fann,M.J.
  TITLE     Identification and characterization of the CDK12/cyclin L1 complex
            involved in alternative splicing regulation
  JOURNAL   Mol Cell Biol 26 (7), 2736-2745 (2006)
   PUBMED   16537916
  REMARK    GeneRIF: CDK12 and cyclin L1/L2 are cyclin-dependent kinase and
            cyclin partners and regulate alternative splicing.
REFERENCE   8  (residues 1 to 1258)
  AUTHORS   Zhang,X.H., Zhang,H., Tu,Y., Gao,X., Zhou,C., Jin,M., Zhao,G.,
            Jing,N., Li,B.M. and Yu,L.
  TITLE     Identification of a novel protein for memory regulation in the
            hippocampus
  JOURNAL   Biochem Biophys Res Commun 334 (2), 418-424 (2005)
   PUBMED   16009348
REFERENCE   9  (residues 1 to 1258)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
REFERENCE   10 (residues 1 to 1258)
  AUTHORS   Ko,T.K., Kelly,E. and Pines,J.
  TITLE     CrkRS: a novel conserved Cdc2-related protein kinase that
            colocalises with SC35 speckles
  JOURNAL   J Cell Sci 114 (Pt 14), 2591-2603 (2001)
   PUBMED   11683387
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY072294.1 and BE117540.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY072294.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132268
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1258
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1258
                     /product="cyclin-dependent kinase 12 isoform 2"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="cell division cycle 2-related protein kinase 7;
                     cell division protein kinase 12; CDC2-related protein
                     kinase 7; CDC2-related kinase 7; protein kinase for
                     splicing component; Cdc2-related kinase,
                     arginine/serine-rich; hippyragranin"
                     /calculated_mol_wt=139854
     Region          1..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Region          485..603
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Region          616..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Region          715..1016
                     /region_name="STKc_CDK12"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 12; cd07864"
                     /db_xref="CDD:270847"
     Site            order(729..732,737,750,752,769,783,809..812,815,817..818,
                     855,857,859..860,862,873,876,889,891..894,896,934..935)
                     /site_type="active"
                     /db_xref="CDD:270847"
     Site            order(729..732,737,750,752,783,809..812,815,818,859..860,
                     862,873)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270847"
     Site            order(761..763,765,768,772,775,785..788,790,805)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270847"
     Site            order(769,817,855,857,876,889,891..894,896,934..935)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270847"
     Site            order(872..884,886..896)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270847"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            889
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Region          1046..1101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            1049
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Region          1156..1199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            1240
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NYV4; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q14AX6; propagated from
                     UniProtKB/Swiss-Prot (Q3MJK5.1)"
     CDS             1..1258
                     /gene="Cdk12"
                     /gene_synonym="Crk7; Crkrs; Hgn; Pksc"
                     /coded_by="NM_138916.2:66..3842"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:192350"
                     /db_xref="RGD:621111"
ORIGIN      
        1 mpnserhggk kdgsggasgt sqpssgggss nsrerhrlvs khkrhkskhs kdmglvtpea
       61 aslgtiikpl veyddissds dtfsddmafk sdrrenderr gtdrsdrlhr hrhhqhrrsr
      121 dllktkqtek eknqevsksg smkdrlsgss krsvegnddy gkaqlsksss kesrsskmhk
      181 ektrkerelk sghkdrsksh rkretpksyk tvdspkrrsr sphrkwsdss kqddspsgas
      241 ygqdydlspp rshtssnyds ykkspgstsr rqsisppyke psayqsstrs pspysrrqrs
      301 vspysrrrss syersgsysg rspspygrrr ssspflskrs lsrspissrk smksrsrspa
      361 ysrhssshsk kkrsgsrsrh ssispvrlpl nsslgaelsr kkkeraaaaa aakldgkesk
      421 gspiilpkke kfevkesgle skklprgiks ekstpdtelv nvahsntevk ncldtgkvkl
      481 denlqkhpvk dlkaqgtkdt kpvalkeviv tsketetsek ealpplptit sppplpsttp
      541 ppqtpplppl pplpavplqp plpppqppfs qvpvsntstl pssphprtst lssqtnsqpl
      601 vqvsmktqls vtaaiphlkt stlpplplpp llpgdddmds pkemlpskpa kkekeqrtrh
      661 lltdlplppe lpggdpsppd spepkaitpp qqpykkrpki ccprygerrq tesdwgkrcv
      721 dkfdiigiig egtygqvyka kdkdtgelva lkkvrldnek egfpitaire ikilrqlvhq
      781 svvnmkeivt dkqdaldfkk dkgafylvfe ymdhdlmgll esglvhfsed hiksfmkqlm
      841 egldychkkn flhrdikcsn illnnsgqik ladfglarly nseesrpytn kvitlwyrpp
      901 elllgeeryt paidvwscgc ilgelftkkp ifqanlelaq lelisrlcgs pcpavwpdvi
      961 klpyfntmkp kkqyrrrlre efsfipsaal dlldhmltld pskrctaeqt lqsdflkdve
     1021 lskmappdlp hwqdchelws kkrrrqrqsg ivieeqppsk asrkettsgt aaepvknssp
     1081 appqpapvka epgpgdavgl gditqqlnqs elavllnllq sqtdlsipqm aqllnihsnp
     1141 emqqqlealn qsisalteas sqqqdsesia peeslkevps vsvvlppaeq ttpeasntpa
     1201 dmqnmlavll sqlmktqepa gnleentsdk nsgpqgprrt ptmpqeeaag kqtghesq
//
LOCUS       NP_001257779             448 aa            linear   ROD 28-APR-2025
DEFINITION  hexokinase-4 isoform 3 [Rattus norvegicus].
ACCESSION   NP_001257779
VERSION     NP_001257779.1
DBSOURCE    REFSEQ: accession NM_001270850.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Samario-Roman,J., Velasco,M., Larque,C., Cardenas-Vazquez,R.,
            Ortiz-Huidobro,R.I. and Hiriart,M.
  TITLE     NGF effects promote the maturation of rat pancreatic beta cells by
            regulating GLUT2 levels and distribution, and glucokinase activity
  JOURNAL   PLoS One 19 (6), e0303934 (2024)
   PUBMED   38875221
  REMARK    GeneRIF: NGF effects promote the maturation of rat pancreatic beta
            cells by regulating GLUT2 levels and distribution, and glucokinase
            activity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Llanos,P., Ordenes,P., Rhoads,D.B., Santibanez,J.F.,
            Garcia-Robles,M. and Millan,C.
  TITLE     BMAL1 Regulates Glucokinase Expression Through E-Box Elements In
            Vitro
  JOURNAL   Adv Exp Med Biol 1408, 235-249 (2023)
   PUBMED   37093431
  REMARK    GeneRIF: BMAL1 Regulates Glucokinase Expression Through E-Box
            Elements In Vitro.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Nozaki,Y., Petersen,M.C., Zhang,D., Vatner,D.F., Perry,R.J.,
            Abulizi,A., Haedersdal,S., Zhang,X.M., Butrico,G.M., Samuel,V.T.,
            Mason,G.F., Cline,G.W., Petersen,K.F., Rothman,D.L. and
            Shulman,G.I.
  TITLE     Metabolic control analysis of hepatic glycogen synthesis in vivo
  JOURNAL   Proc Natl Acad Sci U S A 117 (14), 8166-8176 (2020)
   PUBMED   32188779
  REMARK    GeneRIF: Study in different rat models demonstrated that
            glucokinase (GCK)-mediated glucose phosphorylation is the
            rate-controlling step in insulin-stimulated hepatic glycogen
            synthesis in vivo under both normal and pathophysiological
            conditions of fatty liver-associated hepatic insulin resistance and
            it is controlled chiefly through GCK translocation.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Hao,C.L., Lin,H.L., Ke,L.Y., Yen,H.W. and Shen,K.P.
  TITLE     Pre-germinated brown rice extract ameliorates high-fat diet-induced
            metabolic syndrome
  JOURNAL   J Food Biochem 43 (3), e12769 (2019)
   PUBMED   31353547
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Chakera,A.J., Hurst,P.S., Spyer,G., Ogunnowo-Bada,E.O., Marsh,W.J.,
            Riches,C.H., Yueh,C.Y., Markkula,S.P., Dalley,J.W., Cox,R.D.,
            Macdonald,I.A., Amiel,S.A., MacLeod,K.M., Heisler,L.K.,
            Hattersley,A.T. and Evans,M.L.
  TITLE     Molecular reductions in glucokinase activity increase
            counter-regulatory responses to hypoglycemia in mice and humans
            with diabetes
  JOURNAL   Mol Metab 17, 17-27 (2018)
   PUBMED   30146176
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Vionnet,N., Stoffel,M., Takeda,J., Yasuda,K., Bell,G.I., Zouali,H.,
            Lesage,S., Velho,G., Iris,F., Passa,P. et al.
  TITLE     Nonsense mutation in the glucokinase gene causes early-onset
            non-insulin-dependent diabetes mellitus
  JOURNAL   Nature 356 (6371), 721-722 (1992)
   PUBMED   1570017
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Hughes,S.D., Quaade,C., Milburn,J.L., Cassidy,L. and Newgard,C.B.
  TITLE     Expression of normal and novel glucokinase mRNAs in anterior
            pituitary and islet cells
  JOURNAL   J Biol Chem 266 (7), 4521-4530 (1991)
   PUBMED   1999433
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Hayzer,D.J. and Iynedjian,P.B.
  TITLE     Alternative splicing of glucokinase mRNA in rat liver
  JOURNAL   Biochem J 270 (1), 261-263 (1990)
   PUBMED   2396986
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Zahner,D. and Malaisse,W.J.
  TITLE     Kinetic behaviour of liver glucokinase in diabetes. I. Alteration
            in streptozotocin-diabetic rats
  JOURNAL   Diabetes Res 14 (3), 101-108 (1990)
   PUBMED   2132180
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Coleman,D.L.
  TITLE     Genetic control of glucokinase activity in mice
  JOURNAL   Biochem Genet 15 (3-4), 297-305 (1977)
   PUBMED   141272
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000014.1 and X53588.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region and uses two alternate splice junctions compared to
            variant 1. The resulting isoform (3) has a shorter and distinct
            N-terminus and contains two alternate internal segments compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M25807.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..448
                     /product="hexokinase-4 isoform 3"
                     /EC_number="2.7.1.1"
                     /note="HK4; HK IV; hexokinase-4; hexokinase-D; hexokinase
                     type IV"
                     /calculated_mol_wt=49930
     Region          15..441
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     CDS             1..448
                     /gene="Gck"
                     /gene_synonym="GLK; GLUKA; RNGK2"
                     /coded_by="NM_001270850.1:37..1383"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:24385"
                     /db_xref="RGD:2670"
ORIGIN      
        1 mlddrarmea tkkekveqil aefqlqeedl kkvmsrmqke mdrglrleth eeasvkmlpt
       61 yvrstpegse vgdflsldlg gtnfrvmlvk vgegeagqws vktkhqmysi pedamtgtae
      121 mmkhkklplg ftfsfpvrhe dldkgillnw tkgfkasgae gnnivgllrd aikrrgdfem
      181 dvvamvndtv atmiscyyed rqcevgmivg tgcnacymee mqnvelvegd egrmcvntew
      241 gafgdsgeld eflleydrmv dessanpgqq lyekiiggky mgelvrlvll klvdenllfh
      301 geaseqlrtr gafetrfvsq vesdsgdrkq ihnilstlgl rpsvtdcdiv rracesvstr
      361 aahmcsagla gvinrmresr sedvmritvg vdgsvyklhp sfkerfhasv rrltpnceit
      421 fieseegsgr gaalvsavac kkacmlaq
//
LOCUS       NP_598273                305 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase 6 catalytic subunit [Rattus
            norvegicus].
ACCESSION   NP_598273 XP_346652
VERSION     NP_598273.2
DBSOURCE    REFSEQ: accession NM_133589.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Panier,S. and Durocher,D.
  TITLE     Push back to respond better: regulatory inhibition of the DNA
            double-strand break response
  JOURNAL   Nat Rev Mol Cell Biol 14 (10), 661-672 (2013)
   PUBMED   24002223
  REMARK    Review article
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Nasu-Nishimura,Y., Hayashi,T., Ohishi,T., Okabe,T., Ohwada,S.,
            Hasegawa,Y., Senda,T., Toyoshima,C., Nakamura,T. and Akiyama,T.
  TITLE     Role of the Rho GTPase-activating protein RICS in neurite outgrowth
  JOURNAL   Genes Cells 11 (6), 607-614 (2006)
   PUBMED   16716191
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Becker,W., Kentrup,H., Klumpp,S., Schultz,J.E. and Joost,H.G.
  TITLE     Molecular cloning of a protein serine/threonine phosphatase
            containing a putative regulatory tetratricopeptide repeat domain
  JOURNAL   J Biol Chem 269 (36), 22586-22592 (1994)
   PUBMED   8077208
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078747.1.
            
            On or before Jan 12, 2005 this sequence version replaced
            XP_346652.1, NP_598273.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078747.1, BC063151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840129, SAMN16676810
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..305
                     /product="serine/threonine-protein phosphatase 6 catalytic
                     subunit"
                     /EC_number="3.1.3.16"
                     /note="PP-V; PP6C; protein phosphatase V"
                     /calculated_mol_wt=35028
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00743; propagated from
                     UniProtKB/Swiss-Prot (Q64620.2)"
     Region          5..289
                     /region_name="MPP_PP2A_PP4_PP6"
                     /note="PP2A, PP4, and PP6 phosphoprotein phosphatases,
                     metallophosphatase domain; cd07415"
                     /db_xref="CDD:277360"
     Site            order(47,63,66..67,69..70,72,74..75,87,102..106,117..118,
                     121..122,126..127,130..131,139,264,273,283,289)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:277360"
     Site            order(53,55,81,85,113..114,118..119,123,163,185..187,196,
                     209..211,237,239,263..265)
                     /site_type="active"
                     /db_xref="CDD:277360"
     Site            order(53,55,81,113,163,237)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277360"
     CDS             1..305
                     /gene="Ppp6c"
                     /coded_by="NM_133589.2:99..1016"
                     /db_xref="GeneID:171121"
                     /db_xref="RGD:708460"
ORIGIN      
        1 mapldldkyv eiarqckylp endlkrlcdy vcdllleesn vqpvstpvtv cgdihgqfyd
       61 lcelfrtggq vpdtnyifmg dfvdrgyysl etftyllalk akwpdritll rgnhesrqit
      121 qvygfydecq tkygnanawr yctkvfdmlt vaalideqil cvhgglspdi ktldqirtie
      181 rnqeiphkga fcdlvwsdpe dvdtwaispr gagwlfgakv tnefvhinnl klicrahqlv
      241 hegykfmfde klvtvwsapn ycyrcgnias imvfkdvntr epklfravpd servipprtt
      301 tpyfl
//
LOCUS       NP_001007743             409 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin-associated domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001007743 XP_342389
VERSION     NP_001007743.1
DBSOURCE    REFSEQ: accession NM_001007742.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Kamura,T., Hara,T., Matsumoto,M., Ishida,N., Okumura,F.,
            Hatakeyama,S., Yoshida,M., Nakayama,K. and Nakayama,K.I.
  TITLE     Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
            at G1 phase
  JOURNAL   Nat Cell Biol 6 (12), 1229-1235 (2004)
   PUBMED   15531880
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083603.1.
            
            On Nov 29, 2004 this sequence version replaced XP_342389.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083603.1, FQ210767.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..409
                     /product="ubiquitin-associated domain-containing protein
                     1"
                     /note="UBA domain-containing protein 1; E3
                     ubiquitin-protein ligase subunit KPC2; kip1
                     ubiquitination-promoting complex protein 2; ubiquitin
                     associated domain containing 1"
                     /calculated_mol_wt=45416
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BSL1; propagated from
                     UniProtKB/Swiss-Prot (Q5XIR9.1)"
     Region          9..95
                     /region_name="Ubl_KPC2"
                     /note="ubiquitin-like (Ubl) domain found in Kip1
                     ubiquitination-promoting complex protein 2 (KPC2) and
                     similar proteins; cd17066"
                     /db_xref="CDD:340586"
     Region          195..232
                     /region_name="UBA1_KPC2"
                     /note="UBA1 domain found in Kip1 ubiquitination-promoting
                     complex protein 2 (KPC2) and similar proteins; cd14303"
                     /db_xref="CDD:270488"
     Region          235..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIR9.1)"
     Region          294..331
                     /region_name="UBA2_KPC2"
                     /note="UBA2 domain found in Kip1 ubiquitination-promoting
                     complex protein 2 (KPC2) and similar proteins; cd14304"
                     /db_xref="CDD:270489"
     Region          357..396
                     /region_name="STI1"
                     /note="Heat shock chaperonin-binding motif; smart00727"
                     /db_xref="CDD:128966"
     CDS             1..409
                     /gene="Ubac1"
                     /gene_synonym="Ubadc1"
                     /coded_by="NM_001007742.1:169..1398"
                     /db_xref="GeneID:362087"
                     /db_xref="RGD:1359542"
ORIGIN      
        1 mfvqeekifa gkvlrlhica adgsewleea tedtsveklk esclkhgahg sledpknvth
       61 hklihaaser vlsdsktile eniqdqdvll likkrapspi pkmadvsaee kkkqeqkapd
      121 kdailratan lpacstdrta vqttmrdfqt elrkilvsli evaqkllaln pdavelfkka
      181 namldedede rvdetalrql temgfpesra skalrlnhms vpqamewlie hsedpaidtp
      241 lpghaaqaea saaaatssss seaavgtsve deesrdelte ifkkirrkke fradaravis
      301 lmemgfdeke vidalrvnnn qqnaacewll gdrkpspeel dqgidpnspl fqaildnpvv
      361 qlgltnpktl lafedmlenp lnstqwmndp etgpvmlqis rifqtlnrt
//
LOCUS       NP_853659                391 aa            linear   ROD 28-APR-2025
DEFINITION  tumor susceptibility gene 101 protein [Rattus norvegicus].
ACCESSION   NP_853659
VERSION     NP_853659.2
DBSOURCE    REFSEQ: accession NM_181628.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Sunohara,M., Kriz,W., Kranzlin,B., Kretzler,M., Gretz,N.,
            Endlich,K. and Endlich,N.
  TITLE     Upregulation of Tumor Susceptibility Gene 101 (TSG101) by
            mechanical stress in podocytes
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 65 (1), 84-88 (2019)
   PUBMED   30782301
  REMARK    GeneRIF: mechanical stress upregulates TSG101 in podocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Tsunemi,T., Hamada,K. and Krainc,D.
  TITLE     ATP13A2/PARK9 regulates secretion of exosomes and alpha-synuclein
  JOURNAL   J Neurosci 34 (46), 15281-15287 (2014)
   PUBMED   25392495
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Colombo,M., Moita,C., van Niel,G., Kowal,J., Vigneron,J.,
            Benaroch,P., Manel,N., Moita,L.F., Thery,C. and Raposo,G.
  TITLE     Analysis of ESCRT functions in exosome biogenesis, composition and
            secretion highlights the heterogeneity of extracellular vesicles
  JOURNAL   J Cell Sci 126 (Pt 24), 5553-5565 (2013)
   PUBMED   24105262
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Wu,S.C., Yang,J.C., Rau,C.S., Chen,Y.C., Lu,T.H., Lin,M.W.,
            Tzeng,S.L., Wu,Y.C., Wu,C.J. and Hsieh,C.H.
  TITLE     Profiling circulating microRNA expression in experimental sepsis
            using cecal ligation and puncture
  JOURNAL   PLoS One 8 (10), e77936 (2013)
   PUBMED   24205035
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Zheng,Y., Campbell,E.C., Lucocq,J., Riches,A. and Powis,S.J.
  TITLE     Monitoring the Rab27 associated exosome pathway using nanoparticle
            tracking analysis
  JOURNAL   Exp Cell Res 319 (12), 1706-1713 (2013)
   PUBMED   23092844
REFERENCE   6  (residues 1 to 391)
  AUTHORS   O'Boyle,J.D., Proctor,M.L., Fong,K.M., Lin,W.M., Miller,D.S. and
            Muller,C.Y.
  TITLE     Role of TSG101 in uterine cervix cancer
  JOURNAL   Gynecol Oncol 75 (3), 401-405 (1999)
   PUBMED   10600297
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Klaes,R., Kloor,M., Willeke,F., Melsheimer,P., von Knebel
            Doeberitz,M. and Ridder,R.
  TITLE     Significant increase of a specific variant TSG101 transcript during
            the progression of cervical neoplasia
  JOURNAL   Eur J Cancer 35 (5), 733-737 (1999)
   PUBMED   10505033
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Chang,J.G., Su,T.H., Wei,H.J., Wang,J.C., Chen,Y.J., Chang,C.P. and
            Jeng,C.J.
  TITLE     Analysis of TSG101 tumour susceptibility gene transcripts in
            cervical and endometrial cancers
  JOURNAL   Br J Cancer 79 (3-4), 445-450 (1999)
   PUBMED   10027311
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Sun,Z., Pan,J., Bubley,G. and Balk,S.P.
  TITLE     Frequent abnormalities of TSG101 transcripts in human prostate
            cancer
  JOURNAL   Oncogene 15 (25), 3121-3125 (1997)
   PUBMED   9444960
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Torres,G., Bitran,M. and Huidobro-Toro,J.P.
  TITLE     Co-release of neuropeptide Y (NPY) and noradrenaline from the
            sympathetic nerve terminals supplying the rat vas deferens;
            influence of calcium and the stimulation intensity
  JOURNAL   Neurosci Lett 148 (1-2), 39-42 (1992)
   PUBMED   1300501
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC070951.1.
            
            On Jun 6, 2004 this sequence version replaced NP_853659.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070951.1, AY293306.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..391
                     /product="tumor susceptibility gene 101 protein"
                     /note="Tumor supressor; ESCRT-I complex subunit TSG101"
                     /calculated_mol_wt=43947
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q99816; propagated from
                     UniProtKB/Swiss-Prot (Q6IRE4.1)"
     Region          21..139
                     /region_name="UEV"
                     /note="UEV domain; pfam05743"
                     /db_xref="CDD:399041"
     Region          159..163
                     /region_name="Interaction with CEP55.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IRE4.1)"
     Region          195..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IRE4.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99816; propagated from
                     UniProtKB/Swiss-Prot (Q6IRE4.1)"
     Region          229..>350
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Region          317..376
                     /region_name="Vps23_core"
                     /note="Vps23 core domain; pfam09454"
                     /db_xref="CDD:462803"
     Region          321..324
                     /region_name="PTAP motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IRE4.1)"
     CDS             1..391
                     /gene="Tsg101"
                     /gene_synonym="Rw"
                     /coded_by="NM_181628.2:42..1217"
                     /db_xref="GeneID:292925"
                     /db_xref="RGD:3909"
ORIGIN      
        1 mavsesqlkk mmskykyrdl tvrqtvnvia mykdlkpvld syvfndgssr elvnltgtip
       61 vryrgniyni piclwlldty pynppicfvk ptssmtiktg khvdangkiy lpylhdwkhp
      121 rselleliqi mivifgeepp vfsrptvsas yppytaagpp ntsylpsmps gisaypsgyp
      181 pnpsgypgcp yppagpypat tssqypsqpp vttagpsrdg tisedtiras lisavsdklr
      241 wrmkeemdga qaelnalkrt eedlkkghqk leemvtrldq evaevdknie llkkkdeels
      301 salekmenqs enndidevii ptaplykqil nlyaeenaie dtifylgeal rrgvidldvf
      361 lkhvrllsrk qfqlralmqk arktaglsdl y
//
LOCUS       NP_001093976             451 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-dependent kinase 18 [Rattus norvegicus].
ACCESSION   NP_001093976 XP_001059896 XP_213886
VERSION     NP_001093976.1
DBSOURCE    REFSEQ: accession NM_001100506.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Hirose,T., Tamaru,T., Okumura,N., Nagai,K. and Okada,M.
  TITLE     PCTAIRE 2, a Cdc2-related serine/threonine kinase, is predominantly
            expressed in terminally differentiated neurons
  JOURNAL   Eur J Biochem 249 (2), 481-488 (1997)
   PUBMED   9370357
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082045.1.
            
            On or before Aug 4, 2007 this sequence version replaced
            XP_213886.4, XP_001059896.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082045.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..451
                     /product="cyclin-dependent kinase 18"
                     /EC_number="2.7.11.22"
                     /note="serine/threonine-protein kinase PCTAIRE-3; PCTAIRE
                     protein kinase 3; cell division protein kinase 18;
                     PCTAIRE-motif protein kinase 3"
                     /calculated_mol_wt=51751
     Region          39..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35832.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35832.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35832.1)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q04899; propagated from
                     UniProtKB/Swiss-Prot (O35832.1)"
     Region          115..402
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(127..130,133,135,148,150,180,196..199,242,246..247,
                     249,259..260)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35832.1)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O35832.1)"
     CDS             1..451
                     /gene="Cdk18"
                     /gene_synonym="PCTAIRE3; Pctk3"
                     /coded_by="NM_001100506.1:10..1365"
                     /db_xref="GeneID:289019"
                     /db_xref="RGD:1309523"
ORIGIN      
        1 mnkmknfkrr lslsvprpet ieesltefte qfnqlhtqrn edgrdepgql spgvqyqqrq
       61 nqrrfsmedl nkrlslpmdi rlpqeflqkl qlenpglpkp ltrmsrrasl sdigfgklet
      121 yvkldklgeg tyatvfkgrs kltenlvalk eirleheega pctairevsl lkdlkhaniv
      181 tlhdlihtdr sltlvfeyld sdlkqyldhc gnlmnmhnvk ifmfqllrgl aychrrkilh
      241 rdlkpqnlli nergelklad fglaraksvp tktysnevvt lwyrppdvll gsteystpid
      301 mwgvgcilye matgkplfpg stvkeelhli frllgtptee swpgvtsise fraynfpryl
      361 pqpllshapr ldteginllt slllyesksr msaeaalshp yfqslgervh qlddtasifs
      421 lkeiqlqkdp gyrglafqhp grgksrrqsi f
//
LOCUS       NP_064458                591 aa            linear   ROD 28-APR-2025
DEFINITION  parathyroid hormone/parathyroid hormone-related peptide receptor
            precursor [Rattus norvegicus].
ACCESSION   NP_064458
VERSION     NP_064458.1
DBSOURCE    REFSEQ: accession NM_020073.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Chen,H.M., Dai,J.J., Zhu,R., Peng,F.F., Wu,S.Z., Yu,H.,
            Krepinsky,J.C. and Zhang,B.F.
  TITLE     Parathyroid hormone-related protein induces fibronectin
            up-regulation in rat mesangial cells through reactive oxygen
            species/Src/EGFR signaling
  JOURNAL   Biosci Rep 39 (4) (2019)
   PUBMED   30926678
  REMARK    GeneRIF: Our study thus demonstrates the new role of PTHrP in
            fibronectin up-regulation for the first time in glomerular
            mesangial cells. These data also provided new insights to guide
            development of therapy for glomerular sclerosis
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Liu,C., Shao,G., Lu,Y., Xue,M., Liang,F., Zhang,Z. and Bai,L.
  TITLE     Parathyroid Hormone-Related Protein (1-40) Enhances Calcium Uptake
            in Rat Enterocytes Through PTHR1 Receptor and Protein Kinase
            Calpha/beta Signaling
  JOURNAL   Cell Physiol Biochem 51 (4), 1695-1709 (2018)
   PUBMED   30504697
  REMARK    GeneRIF: PTHrP (1-40) stimulates calcium uptake via PTHR1 receptor
            and PKC alpha/beta signaling pathway in rat enterocytes, and
            calcium transporters TRPV6 and CaBP-D9k are necessary for this
            stimulatory effect.
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Shimomura-Kuroki,J., Farooq,M., Sekimoto,T., Amizuka,N. and
            Shimomura,Y.
  TITLE     Characterization of a PTH1R missense mutation responsible for
            Jansen type metaphyseal chondrodysplasia
  JOURNAL   Odontology 105 (2), 150-154 (2017)
   PUBMED   27160269
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Wilson,R., Geyer,S.H., Reissig,L., Rose,J., Szumska,D., Hardman,E.,
            Prin,F., McGuire,C., Ramirez-Solis,R., White,J., Galli,A.,
            Tudor,C., Tuck,E., Mazzeo,C.I., Smith,J.C., Robertson,E.,
            Adams,D.J., Mohun,T. and Weninger,W.J.
  TITLE     Highly variable penetrance of abnormal phenotypes in embryonic
            lethal knockout mice
  JOURNAL   Wellcome Open Res 1, 1 (2017)
   PUBMED   27996060
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Filipovic,N., Vrdoljak,M., Vuica,A., Jeric,M., Jelicic Kadic,A.,
            Utrobicic,T., Masek,T. and Grkovic,I.
  TITLE     Expression of PTHrP and PTH/PTHrP receptor 1 in the superior
            cervical ganglia of rats
  JOURNAL   Neuropeptides 48 (6), 353-359 (2014)
   PUBMED   25278090
  REMARK    GeneRIF: Results show the expression of PTHrP and its receptor,
            PTHR1, in the majority of neurons and glial cells in the SCG of
            rats. Expression of PTHrP, but not PTHR1 in the cytoplasm of SCG
            neurons is influenced by ovarian activity.
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Lanske,B., Karaplis,A.C., Lee,K., Luz,A., Vortkamp,A., Pirro,A.,
            Karperien,M., Defize,L.H., Ho,C., Mulligan,R.C., Abou-Samra,A.B.,
            Juppner,H., Segre,G.V. and Kronenberg,H.M.
  TITLE     PTH/PTHrP receptor in early development and Indian
            hedgehog-regulated bone growth
  JOURNAL   Science 273 (5275), 663-666 (1996)
   PUBMED   8662561
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Kong,X.F., Schipani,E., Lanske,B., Joun,H., Karperien,M.,
            Defize,L.H., Juppner,H., Potts,J.T. Jr., Segre,G.V.,
            Kronenberg,H.M. et al.
  TITLE     The rat, mouse and human genes encoding the receptor for
            parathyroid hormone and parathyroid hormone-related peptide are
            highly homologous
  JOURNAL   Biochem Biophys Res Commun 200 (3), 1290-1299 (1994)
   PUBMED   8185578
  REMARK    Erratum:[Biochem Biophys Res Commun. 1994 Jun 15;201(2):1058. doi:
            10.1006/bbrc.1994.1811. PMID: 8002976]
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Pausova,Z., Bourdon,J., Clayton,D., Mattei,M.G., Seldin,M.F.,
            Janicic,N., Riviere,M., Szpirer,J., Levan,G., Szpirer,C. et al.
  TITLE     Cloning of a parathyroid hormone/parathyroid hormone-related
            peptide receptor (PTHR) cDNA from a rat osteosarcoma (UMR 106) cell
            line: chromosomal assignment of the gene in the human, mouse, and
            rat genomes
  JOURNAL   Genomics 20 (1), 20-26 (1994)
   PUBMED   8020952
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Schneider,H., Feyen,J.H., Seuwen,K. and Movva,N.R.
  TITLE     Cloning and functional expression of a human parathyroid hormone
            receptor
  JOURNAL   Eur J Pharmacol 246 (2), 149-155 (1993)
   PUBMED   8397094
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Abou-Samra,A.B., Juppner,H., Force,T., Freeman,M.W., Kong,X.F.,
            Schipani,E., Urena,P., Richards,J., Bonventre,J.V., Potts,J.T. Jr.
            et al.
  TITLE     Expression cloning of a common receptor for parathyroid hormone and
            parathyroid hormone-related peptide from rat osteoblast-like cells:
            a single receptor stimulates intracellular accumulation of both
            cAMP and inositol trisphosphates and increases intracellular free
            calcium
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2732-2736 (1992)
   PUBMED   1313566
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L19475.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L19475.1, M77184.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..591
                     /product="parathyroid hormone/parathyroid hormone-related
                     peptide receptor precursor"
                     /note="parathyroid hormone receptor 1; parathyroid
                     hormone/parathyroid hormone-related peptide receptor; PTH1
                     receptor; PTH/PTHr receptor; PTH/PTHrP type I receptor"
                     /calculated_mol_wt=63887
     sig_peptide     1..24
                     /calculated_mol_wt=2392
     mat_peptide     25..591
                     /product="parathyroid hormone/parathyroid hormone-related
                     peptide receptor"
                     /calculated_mol_wt=63887
     Region          67..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          105..170
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25961.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25961.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25961.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25961.1)"
     Region          184..476
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          187..211
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320650"
     Site            189..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          220..241
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320650"
     Site            220..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          282..304
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320650"
     Site            283..306
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Site            321..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          323..339
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320650"
     Region          356..379
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320650"
     Site            362..382
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          407..429
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320650"
     Site            410..428
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          438..463
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320650"
     Site            441..463
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          474..477
                     /region_name="Important for interaction with G proteins.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     Region          516..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25961.1)"
     CDS             1..591
                     /gene="Pth1r"
                     /gene_synonym="Pthr; Pthr1; PTHrel"
                     /coded_by="NM_020073.2:46..1821"
                     /db_xref="GeneID:56813"
                     /db_xref="RGD:3442"
ORIGIN      
        1 mgaariapsl alllccpvls sayalvdadd vftkeeqifl lhraqaqcdk llkevlhtaa
       61 nimesdkgwt pastsgkprk ekasgkfype skenkdvptg srrrgrpclp ewdnivcwpl
      121 gapgevvavp cpdyiydfnh kghayrrcdr ngswevvpgh nrtwanysec lkfmtnetre
      181 revfdrlgmi ytvgysmsla sltvavlila yfrrlhctrn yihmhmflsf mlraasifvk
      241 davlysgftl deaerlteee lhiiaqvppp paaaavgyag crvavtffly flatnyywil
      301 veglylhsli fmaffsekky lwgftifgwg lpavfvavwv gvratlantg cwdlssghkk
      361 wiiqvpilas vvlnfilfin iirvlatklr etnagrcdtr qqyrkllrst lvlvplfgvh
      421 ytvfmalpyt evsgtlwqiq mhyemlfnsf qgffvaiiyc fcngevqaei rkswsrwtla
      481 ldfkrkarsg sssysygpmv shtsvtnvgp raglslplsp rlppattngh sqlpghakpg
      541 apatetetlp vtmavpkddg flngscsgld eeasgsarpp pllqeewetv m
//
LOCUS       NP_001093974             228 aa            linear   ROD 28-APR-2025
DEFINITION  large ribosomal subunit protein mL64 [Rattus norvegicus].
ACCESSION   NP_001093974 XP_001071308 XP_213842
VERSION     NP_001093974.1
DBSOURCE    REFSEQ: accession NM_001100504.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Hayes,J.D. and Dinkova-Kostova,A.T.
  TITLE     The Nrf2 regulatory network provides an interface between redox and
            intermediary metabolism
  JOURNAL   Trends Biochem Sci 39 (4), 199-218 (2014)
   PUBMED   24647116
  REMARK    Review article
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Ran,Q., Hao,P., Xiao,Y., Xiang,L., Ye,X., Deng,X., Zhao,J. and
            Li,Z.
  TITLE     CRIF1 interacting with CDK2 regulates bone marrow
            microenvironment-induced G0/G1 arrest of leukemia cells
  JOURNAL   PLoS One 9 (2), e85328 (2014)
   PUBMED   24520316
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 228)
  AUTHORS   .
  TITLE     SOX9 and the switch hitting genes
  JOURNAL   Nat Genet 9 (1), 1-2 (1995)
   PUBMED   7704013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000019.1.
            
            On or before Nov 22, 2008 this sequence version replaced
            XP_001071308.1, XP_213842.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083178.1, FQ217511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN12840107
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..228
                     /product="large ribosomal subunit protein mL64"
                     /note="growth arrest and DNA damage-inducible
                     proteins-interacting protein 1; 39S ribosomal protein L59,
                     mitochondrial; growth arrest and DNA-damage-inducible,
                     gamma interacting protein 1"
                     /calculated_mol_wt=26336
     Region          1..211
                     /region_name="CR6_interact"
                     /note="Growth arrest and DNA-damage-inducible
                     proteins-interacting protein 1; pfam10147"
                     /db_xref="CDD:431088"
     Region          20..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XJW2.2)"
     Region          184..200
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XJW2.2)"
     Region          186..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XJW2.2)"
     CDS             1..228
                     /gene="Gadd45gip1"
                     /gene_synonym="MRP-L59"
                     /coded_by="NM_001100504.1:1..687"
                     /db_xref="GeneID:288916"
                     /db_xref="RGD:1309249"
ORIGIN      
        1 maapatrsry llrltvtlgp rsrsyhappp prrrpaphwp drenlmtprw qltpryaakq
       61 fgrhgaisgv ppaslwpsse qlceleaeer ewypslatmq eslrvqqqaa earrqareqh
      121 iaecmakmpq mienwrkqkr erwekiqadk errarlqaea qeqlgyhvdp rsarfqellq
      181 dldkqqrkrl keerqrqkke ariaamasae gqdsaeaqds aasgkpss
//
LOCUS       NP_001020844             410 aa            linear   ROD 28-APR-2025
DEFINITION  centromere protein U [Rattus norvegicus].
ACCESSION   NP_001020844 XP_224859
VERSION     NP_001020844.1
DBSOURCE    REFSEQ: accession NM_001025673.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Wang,X., Marcinkiewicz,M., Gatain,Y., Bouchard,M., Mao,J.,
            Tremblay,M., Uetani,N., Hanissian,S., Qi,S., Wu,J. and Luo,H.
  TITLE     Investigation of tissue-specific expression and functions of
            MLF1-IP during development and in the immune system
  JOURNAL   PLoS One 8 (5), e63783 (2013)
   PUBMED   23724000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Hanissian,S.H., Teng,B., Akbar,U., Janjetovic,Z., Zhou,Q.,
            Duntsch,C. and Robertson,J.H.
  TITLE     Regulation of myeloid leukemia factor-1 interacting protein
            (MLF1IP) expression in glioblastoma
  JOURNAL   Brain Res 1047 (1), 56-64 (2005)
   PUBMED   15893739
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097399.1.
            
            On Jul 22, 2005 this sequence version replaced XP_224859.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097399.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q11"
     Protein         1..410
                     /product="centromere protein U"
                     /note="CENP-U; MLF1-interacting protein; myeloid leukemia
                     factor 1 interacting protein"
                     /calculated_mol_wt=46670
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Region          4..21
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PLK1.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Region          87..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C4M7; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C4M7; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Region          137..312
                     /region_name="CENP-U"
                     /note="CENP-A nucleosome associated complex (NAC) subunit;
                     pfam13097"
                     /db_xref="CDD:463785"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8C4M7; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q71F23; propagated from
                     UniProtKB/Swiss-Prot (Q4V8G7.1)"
     Region          276..>355
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          295..312
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8G7.1)"
     CDS             1..410
                     /gene="Cenpu"
                     /gene_synonym="Mlf1ip"
                     /coded_by="NM_001025673.1:228..1460"
                     /db_xref="GeneID:306464"
                     /db_xref="RGD:1562566"
ORIGIN      
        1 maarrslrys gdpgakrsrn tlgstnsrkq kagqkpkrkd vfdfpntsdv ssmlreleee
       61 epyetfdppl hstaiytdde lykhcvssts pathrgkesr nlnpseneas gndsiklsak
      121 kprrklepis desdssednv rrsvsierpr arkppaapaa assssspser paeqvtprkt
      181 sfpqpsavee tpaaqsqlkt qkkvrpspgr rkrprrgsth sdasesmhil clegkrqsdv
      241 meldvvlsaf ertfldykqr vesescnqai skfyfkikge lirmlkevqm lkalkrkntk
      301 iisnmekkrq rlidvqdeli rlepqlkqlq tkyddlkkrk salknskhfl snlkqlyqdy
      361 snvreeepke kekydssslp allfkarsil gaekhlktin yhlgkllkqd
//
LOCUS       NP_037157                 92 aa            linear   ROD 28-APR-2025
DEFINITION  C-C motif chemokine 3 precursor [Rattus norvegicus].
ACCESSION   NP_037157
VERSION     NP_037157.2
DBSOURCE    REFSEQ: accession NM_013025.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Yang,Y., Shen,C., Li,J., Yuan,J., Wei,J., Huang,F., Wang,F., Li,G.,
            Li,Y., Xing,L., Peng,L., Yang,M., Cao,M., Zheng,H., Wu,W., Zou,R.,
            Li,D., Xu,Z., Wang,H., Zhang,M., Zhang,Z., Gao,G.F., Jiang,C.,
            Liu,L. and Liu,Y.
  TITLE     Plasma IP-10 and MCP-3 levels are highly associated with disease
            severity and predict the progression of COVID-19
  JOURNAL   J Allergy Clin Immunol 146 (1), 119-127 (2020)
   PUBMED   32360286
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Liu,J., Zhang,S., Huang,Y. and Sun,L.
  TITLE     miR-21 protects neonatal rats from hypoxic-ischemic brain damage by
            targeting CCL3
  JOURNAL   Apoptosis 25 (3-4), 275-289 (2020)
   PUBMED   32306124
  REMARK    GeneRIF: miR-21 protects neonatal rats from hypoxic-ischemic brain
            damage by targeting CCL3.
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Huang,C., Wang,Y., Li,X., Ren,L., Zhao,J., Hu,Y., Zhang,L., Fan,G.,
            Xu,J., Gu,X., Cheng,Z., Yu,T., Xia,J., Wei,Y., Wu,W., Xie,X.,
            Yin,W., Li,H., Liu,M., Xiao,Y., Gao,H., Guo,L., Xie,J., Wang,G.,
            Jiang,R., Gao,Z., Jin,Q., Wang,J. and Cao,B.
  TITLE     Clinical features of patients infected with 2019 novel coronavirus
            in Wuhan, China
  JOURNAL   Lancet 395 (10223), 497-506 (2020)
   PUBMED   31986264
  REMARK    Erratum:[Lancet. 2020 Feb 15;395(10223):496. doi:
            10.1016/S0140-6736(20)30252-X. PMID: 32007144]
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Iwata-Yoshikawa,N., Okamura,T., Shimizu,Y., Kotani,O., Sato,H.,
            Sekimukai,H., Fukushi,S., Suzuki,T., Sato,Y., Takeda,M.,
            Tashiro,M., Hasegawa,H. and Nagata,N.
  TITLE     Acute Respiratory Infection in Human Dipeptidyl Peptidase
            4-Transgenic Mice Infected with Middle East Respiratory Syndrome
            Coronavirus
  JOURNAL   J Virol 93 (6), e01818-18 (2019)
   PUBMED   30626685
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Zhang,H., Wu,J., Wu,J., Fan,Q., Zhou,J., Wu,J., Liu,S., Zang,J.,
            Ye,J., Xiao,M., Tian,T. and Gao,J.
  TITLE     Exosome-mediated targeted delivery of miR-210 for angiogenic
            therapy after cerebral ischemia in mice
  JOURNAL   J Nanobiotechnology 17 (1), 29 (2019)
   PUBMED   30782171
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Post,T.W., Bozic,C.R., Rothenberg,M.E., Luster,A.D., Gerard,N. and
            Gerard,C.
  TITLE     Molecular characterization of two murine eosinophil beta chemokine
            receptors
  JOURNAL   J Immunol 155 (11), 5299-5305 (1995)
   PUBMED   7594543
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Ben-Baruch,A., Xu,L., Young,P.R., Bengali,K., Oppenheim,J.J. and
            Wang,J.M.
  TITLE     Monocyte chemotactic protein-3 (MCP3) interacts with multiple
            leukocyte receptors. C-C CKR1, a receptor for macrophage
            inflammatory protein-1 alpha/Rantes, is also a functional receptor
            for MCP3
  JOURNAL   J Biol Chem 270 (38), 22123-22128 (1995)
   PUBMED   7545673
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Shi,M.M., Godleski,J.J. and Paulauskis,J.D.
  TITLE     Molecular cloning and posttranscriptional regulation of macrophage
            inflammatory protein-1 alpha in alveolar macrophages
  JOURNAL   Biochem Biophys Res Commun 211 (1), 289-295 (1995)
   PUBMED   7779098
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Shanley,T.P., Schmal,H., Friedl,H.P., Jones,M.L. and Ward,P.A.
  TITLE     Role of macrophage inflammatory protein-1 alpha (MIP-1 alpha) in
            acute lung injury in rats
  JOURNAL   J Immunol 154 (9), 4793-4802 (1995)
   PUBMED   7722328
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Santolini,B.M., Nai Fovino,P.L. and Rossoni,L.
  TITLE     [The behavior of intra-leukocyte peroxidase after irradiation with
            radar microwaves in intra-articular exudates]
  JOURNAL   Minerva Ortop 22 (12), 459-462 (1971)
   PUBMED   5135051
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U22414.1.
            
            On Dec 20, 2003 this sequence version replaced NP_037157.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U22414.1, DV728694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN13663625 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Rattus norvegicus"
                     /strain="CD"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..92
                     /product="C-C motif chemokine 3 precursor"
                     /note="C-C motif chemokine 3; MIP-1-alpha; small-inducible
                     cytokine A3; macrophage inflammatory protein 1-alpha;
                     Macrophage inflammatory protein 1 alpha (Small inducible
                     cytokine A3); chemokine (C-C motif) ligand 3"
                     /calculated_mol_wt=7854
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2499
     mat_peptide     24..92
                     /product="C-C motif chemokine 3. /id=PRO_0000005160"
                     /note="propagated from UniProtKB/Swiss-Prot (P50229.1)"
                     /calculated_mol_wt=7854
     Region          31..85
                     /region_name="SCY"
                     /note="Intercrine alpha family (small cytokine C-X-C)
                     (chemokine CXC); smart00199"
                     /db_xref="CDD:197570"
     Site            order(34..38,40..41,42..46,56..57,79..89)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:238170"
     Site            order(36,38,50,52,57,62..64,72..74,80..81,84..85,88..89)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238170"
     Site            order(36,38,54,56..57,63,71,73)
                     /site_type="other"
                     /note="dimer interface (P form) [polypeptide binding]"
                     /db_xref="CDD:238170"
     Site            order(36,63,72)
                     /site_type="active"
                     /note="putative receptor binding cleft [active]"
                     /db_xref="CDD:238170"
     Site            order(36..38,40..41,42..46)
                     /site_type="active"
                     /note="N-loop [active]"
                     /db_xref="CDD:238170"
     Site            order(38,50,52,62,64,72,74,80..81,84..85,88..89)
                     /site_type="other"
                     /note="dimer interface (I form) [polypeptide binding]"
                     /db_xref="CDD:238170"
     Site            order(40..41,44..46,68,70)
                     /site_type="other"
                     /note="putative glycosaminoglycan (GAG) binding site
                     [chemical binding]"
                     /db_xref="CDD:238170"
     Site            order(52,59,77,79,82..83,86)
                     /site_type="other"
                     /note="putative glycosaminoglycan (GAG) binding site
                     [chemical binding]"
                     /db_xref="CDD:238170"
     Site            56..57
                     /site_type="other"
                     /note="30s-loop"
                     /db_xref="CDD:238170"
     Site            order(66,68)
                     /site_type="other"
                     /note="40s-loop"
                     /db_xref="CDD:238170"
     CDS             1..92
                     /gene="Ccl3"
                     /gene_synonym="MIP-1a; Scya3"
                     /coded_by="NM_013025.2:70..348"
                     /db_xref="GeneID:25542"
                     /db_xref="RGD:3647"
ORIGIN      
        1 mkvstaalav llctmalwne vfsapygadt ptaccfsygr qiprkfiady fetsslcsqp
       61 gvifltkrnr qicadpketw vqeyitelel na
//
LOCUS       NP_001102759             149 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein C11orf97 homolog [Rattus norvegicus].
ACCESSION   NP_001102759 XP_001074200 XP_576356
VERSION     NP_001102759.1
DBSOURCE    REFSEQ: accession NM_001109289.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Stauber,M., Boldt,K., Wrede,C., Weidemann,M., Kellner,M.,
            Schuster-Gossler,K., Kuhnel,M.P., Hegermann,J., Ueffing,M. and
            Gossler,A.
  TITLE     1700012B09Rik, a FOXJ1 effector gene active in ciliated tissues of
            the mouse but not essential for motile ciliogenesis
  JOURNAL   Dev Biol 429 (1), 186-199 (2017)
   PUBMED   28666954
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Stauber,M., Weidemann,M., Dittrich-Breiholz,O., Lobschat,K.,
            Alten,L., Mai,M., Beckers,A., Kracht,M. and Gossler,A.
  TITLE     Identification of FOXJ1 effectors during ciliogenesis in the foetal
            respiratory epithelium and embryonic left-right organiser of the
            mouse
  JOURNAL   Dev Biol 423 (2), 170-188 (2017)
   PUBMED   27914912
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473993.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_576356.1, XP_001074200.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF113898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..149
                     /product="uncharacterized protein C11orf97 homolog"
                     /calculated_mol_wt=16337
     CDS             1..149
                     /gene="C8h11orf97"
                     /gene_synonym="RGD1561795"
                     /coded_by="NM_001109289.1:4..453"
                     /db_xref="GeneID:500945"
                     /db_xref="RGD:1561795"
ORIGIN      
        1 mpcvpeqpva elrglvavgr gdpggmrrqe alvvtagtas easrdgeqpr paglvcrarv
       61 epggpqesrq qwktflycep hkrikevlee elsikrdech vksptavald giwsirrnlp
      121 vggmipgqqs rncslpqtky ysrhgglrr
//
LOCUS       NP_001096826             185 aa            linear   ROD 28-APR-2025
DEFINITION  UPF0669 protein C6orf120 homolog precursor [Rattus norvegicus].
ACCESSION   NP_001096826
VERSION     NP_001096826.1
DBSOURCE    REFSEQ: accession NM_001103356.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Wang,X., Liu,H., Wang,Y., Wang,P., Yi,Y., Lin,Y. and Li,X.
  TITLE     Novel protein C6ORF120 promotes liver fibrosis by activating
            hepatic stellate cells through the PI3K/Akt/mTOR pathway
  JOURNAL   J Gastroenterol Hepatol 39 (7), 1422-1430 (2024)
   PUBMED   38523410
  REMARK    GeneRIF: Novel protein C6ORF120 promotes liver fibrosis by
            activating hepatic stellate cells through the PI3K/Akt/mTOR
            pathway.
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Wu,Y.N., Zhang,R., Song,X.C., Han,X.X., Zhang,J. and Li,X.
  TITLE     C6orf120 gene knockout in rats mitigates concanavalin A-induced
            autoimmune hepatitis via regulating NKT cells
  JOURNAL   Cell Immunol 371, 104467 (2022)
   PUBMED   34896761
  REMARK    GeneRIF: C6orf120 gene knockout in rats mitigates concanavalin
            Ainduced autoimmune hepatitis via regulating NKT cells.
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Zhang,M.K., Ma,H.M., Zhang,J., Song,X.C., Ye,X.H., Li,Y.F.,
            Zhang,Y.F., He,L.L., Wei,H.S. and Li,X.
  TITLE     Deletion of the C6orf120 gene with unknown function ameliorates
            autoimmune hepatitis induced by concanavalin A
  JOURNAL   Cell Immunol 331, 9-15 (2018)
   PUBMED   29748000
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079175.1, JAXUCZ010000001.1 and BG373545.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079175.1, SRR26643298.990.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..185
                     /product="UPF0669 protein C6orf120 homolog precursor"
                     /note="UPF0669 protein C6orf120 homolog"
                     /calculated_mol_wt=18360
     Region          1..185
                     /region_name="UPF0669"
                     /note="Putative cytokine, C6ORF120; pfam17065"
                     /db_xref="CDD:293670"
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2560
     mat_peptide     24..185
                     /product="UPF0669 protein C6orf120 homolog.
                     /id=PRO_0000297665"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY64.1)"
                     /calculated_mol_wt=18360
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6AY64.1)"
     CDS             1..185
                     /gene="C1h6orf120"
                     /gene_synonym="C6orf120"
                     /coded_by="NM_001103356.2:213..770"
                     /db_xref="GeneID:100125364"
                     /db_xref="RGD:1642424"
ORIGIN      
        1 matpwrcall milasqvvil vkcledddvp eewlllhvvq gqigagnysy lrlnhegkii
       61 lrmqslrgda dlyvsdstph psfdeyelqs vtcgqdvvsi pahfqrpvgi giyghpshhe
      121 sdfemrvyyd rtvdqypfge aayaadqtgt sqkqaytpee aaqeeesvlw tilisilklv
      181 leilf
//
LOCUS       NP_001020221             288 aa            linear   ROD 28-APR-2025
DEFINITION  borealin [Rattus norvegicus].
ACCESSION   NP_001020221 XP_575906
VERSION     NP_001020221.1
DBSOURCE    REFSEQ: accession NM_001025050.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wang,T., Dai,L., Shen,S., Yang,Y., Yang,M., Yang,X., Qiu,Y. and
            Wang,W.
  TITLE     Comprehensive Molecular Analyses of a Macrophage-Related Gene
            Signature With Regard to Prognosis, Immune Features, and Biomarkers
            for Immunotherapy in Hepatocellular Carcinoma Based on WGCNA and
            the LASSO Algorithm
  JOURNAL   Front Immunol 13, 843408 (2022)
   PUBMED   35693827
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Capalbo,L., Montembault,E., Takeda,T., Bassi,Z.I., Glover,D.M. and
            D'Avino,P.P.
  TITLE     The chromosomal passenger complex controls the function of
            endosomal sorting complex required for transport-III Snf7 proteins
            during cytokinesis
  JOURNAL   Open Biol 2 (5), 120070 (2012)
   PUBMED   22724069
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Parra,M.T., Gomez,R., Viera,A., Llano,E., Pendas,A.M., Rufas,J.S.
            and Suja,J.A.
  TITLE     Sequential assembly of centromeric proteins in male mouse meiosis
  JOURNAL   PLoS Genet 5 (3), e1000417 (2009)
   PUBMED   19283064
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Xia,F., Canovas,P.M., Guadagno,T.M. and Altieri,D.C.
  TITLE     A survivin-ran complex regulates spindle formation in tumor cells
  JOURNAL   Mol Cell Biol 28 (17), 5299-5311 (2008)
   PUBMED   18591255
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Vader,G., Kauw,J.J., Medema,R.H. and Lens,S.M.
  TITLE     Survivin mediates targeting of the chromosomal passenger complex to
            the centromere and midbody
  JOURNAL   EMBO Rep 7 (1), 85-92 (2006)
   PUBMED   16239925
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Sampath,S.C., Ohi,R., Leismann,O., Salic,A., Pozniakovski,A. and
            Funabiki,H.
  TITLE     The chromosomal passenger complex is required for chromatin-induced
            microtubule stabilization and spindle assembly
  JOURNAL   Cell 118 (2), 187-202 (2004)
   PUBMED   15260989
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079274.1.
            
            On Jun 25, 2005 this sequence version replaced XP_575906.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079274.1, SRR8487231.17980.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..288
                     /product="borealin"
                     /note="cell division cycle-associated protein 8"
                     /calculated_mol_wt=31968
     Region          1..149
                     /region_name="Required for interaction with SENP3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          1..88
                     /region_name="Required for centromere localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          1..58
                     /region_name="Required for interaction with INCENP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          10..109
                     /region_name="Required to form a minimal CPC core complex
                     that localizes to the central spindle and midbody and
                     properly executes the role of the CPC during cytokinesis.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          20..78
                     /region_name="Required for interaction with INCENP and
                     BIRC5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          20..76
                     /region_name="Nbl1_Borealin_N"
                     /note="Nbl1 / Borealin N terminal; pfam10444"
                     /db_xref="CDD:463095"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TTK.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TTK.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          124..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Region          168..283
                     /region_name="Borealin"
                     /note="Cell division cycle-associated protein 8;
                     pfam10512"
                     /db_xref="CDD:463127"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q53HL2; propagated from
                     UniProtKB/Swiss-Prot (Q6AXW0.1)"
     CDS             1..288
                     /gene="Cdca8"
                     /coded_by="NM_001025050.1:129..995"
                     /db_xref="GeneID:500545"
                     /db_xref="RGD:1566306"
ORIGIN      
        1 mapkkrssrg trtntlrsrk lasflkdfdr evqvrtkqie sdrqtllkev enlynievlr
       61 lpkalqvmkw ldyfalggnr qaleeaatad rditeinnlt aeaiqtplks vkkrkvievd
      121 eaikeeeede eeeggggggr kshknlrsar vkrcppskkr tqsiqgrsrs krlshdfvtp
      181 amsrlepslv kptpgmtprf dsrvfktpgl rtpaakeqvy nisingspla dskeislsvp
      241 igggaslrll asdlqrvdia qlnpealgni kklssrlaqi cssirtgr
//
LOCUS       NP_446268                533 aa            linear   ROD 28-APR-2025
DEFINITION  calcitonin receptor isoform 1b precursor [Rattus norvegicus].
ACCESSION   NP_446268
VERSION     NP_446268.2
DBSOURCE    REFSEQ: accession NM_053816.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Andreassen,K.V., Feigh,M., Hjuler,S.T., Gydesen,S., Henriksen,J.E.,
            Beck-Nielsen,H., Christiansen,C., Karsdal,M.A. and Henriksen,K.
  TITLE     A novel oral dual amylin and calcitonin receptor agonist (KBP-042)
            exerts antiobesity and antidiabetic effects in rats
  JOURNAL   Am J Physiol Endocrinol Metab 307 (1), E24-E33 (2014)
   PUBMED   24801386
  REMARK    GeneRIF: In conclusion, oral KBP-042 is a novel DACRA, which exerts
            antiobesity and antidiabetic efficacy by dual modulation of insulin
            sensitivity and directly decelerating stress on the pancreatic
            alpha- and beta-cells.
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Gooi,J.H., Chia,L.Y., Walsh,N.C., Karsdal,M.A., Quinn,J.M.,
            Martin,T.J. and Sims,N.A.
  TITLE     Decline in calcitonin receptor expression in osteocytes with age
  JOURNAL   J Endocrinol 221 (2), 181-191 (2014)
   PUBMED   24516262
  REMARK    GeneRIF: Calcitonin receptor mRNA expression declines with age on
            osteocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Tural,S., Kara,N., Alayli,G. and Tomak,L.
  TITLE     Association between osteoporosis and polymorphisms of the bone Gla
            protein, estrogen receptor 1, collagen 1-A1 and calcitonin receptor
            genes in Turkish postmenopausal women
  JOURNAL   Gene 515 (1), 167-172 (2013)
   PUBMED   23137636
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Matsubara,R., Kukita,T., Ichigi,Y., Takigawa,I., Qu,P.F.,
            Funakubo,N., Miyamoto,H., Nonaka,K. and Kukita,A.
  TITLE     Characterization and identification of subpopulations of
            mononuclear preosteoclasts induced by TNF-alpha in combination with
            TGF-beta in rats
  JOURNAL   PLoS One 7 (10), e47930 (2012)
   PUBMED   23110133
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Abdelmagid,N., Bereczky-Veress,B., Guerreiro-Cacais,A.O.,
            Bergman,P., Luhr,K.M., Bergstrom,T., Skoldenberg,B., Piehl,F.,
            Olsson,T. and Diez,M.
  TITLE     The calcitonin receptor gene is a candidate for regulation of
            susceptibility to herpes simplex type 1 neuronal infection leading
            to encephalitis in rat
  JOURNAL   PLoS Pathog 8 (6), e1002753 (2012)
   PUBMED   22761571
  REMARK    GeneRIF: variability in Calcr was identified as potentially
            critical for infection and viral spread to the CNS and subsequent
            Herpes simplex encephalitis development.
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Albrandt,K., Brady,E.M., Moore,C.X., Mull,E., Sierzega,M.E. and
            Beaumont,K.
  TITLE     Molecular cloning and functional expression of a third isoform of
            the human calcitonin receptor and partial characterization of the
            calcitonin receptor gene
  JOURNAL   Endocrinology 136 (12), 5377-5384 (1995)
   PUBMED   7588285
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Lee,S.K., Goldring,S.R. and Lorenzo,J.A.
  TITLE     Expression of the calcitonin receptor in bone marrow cell cultures
            and in bone: a specific marker of the differentiated osteoclast
            that is regulated by calcitonin
  JOURNAL   Endocrinology 136 (10), 4572-4581 (1995)
   PUBMED   7664679
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Egerton,M., Needham,M., Evans,S., Millest,A., Cerillo,G.,
            McPheat,J., Popplewell,M., Johnstone,D. and Hollis,M.
  TITLE     Identification of multiple human calcitonin receptor isoforms:
            heterologous expression and pharmacological characterization
  JOURNAL   J Mol Endocrinol 14 (2), 179-189 (1995)
   PUBMED   7619207
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Pandya,S.
  TITLE     Obituary. Dr. Wilder Penfield, 1891-1976
  JOURNAL   Neurol India 24 (2), V-VI (1976)
   PUBMED   796748
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Blattner,R.J.
  TITLE     Hemolytic anemia associated with Wilson's disease
  JOURNAL   J Pediatr 71 (2), 284-287 (1967)
   PUBMED   4961748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB791100.1, L14618.1 and L14617.1.
            
            On Oct 9, 2005 this sequence version replaced NP_446268.1.
            
            Transcript Variant: This variant (1b), previously called 1,
            represents the longer variant and encodes the longer isoform (1b,
            previously called a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760384, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q13"
     Protein         1..533
                     /product="calcitonin receptor isoform 1b precursor"
                     /note="CT-R; C1A/C1B"
                     /calculated_mol_wt=57499
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5005
     Region          86..154
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          162..472
                     /region_name="7tmB1_calcitonin_R"
                     /note="calcitonin receptor, member of the class B family
                     of seven-transmembrane G protein-coupled receptors;
                     cd15274"
                     /db_xref="CDD:341343"
     Region          164..189
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341343"
     Site            order(169,173,215,218..219,222,274,281,351..352,354,356,
                     410,413,427,431)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:341343"
     Site            order(197,297..298,301..303,306..308,377,380..381,
                     384..385,399,402,448,458,462,469,472)
                     /site_type="other"
                     /note="G protein interaction site [polypeptide binding]"
                     /db_xref="CDD:341343"
     Region          198..220
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341343"
     Region          274..301
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341343"
     Region          313..333
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341343"
     Region          348..377
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341343"
     Region          391..418
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341343"
     Region          424..449
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341343"
     CDS             1..533
                     /gene="Calcr"
                     /coded_by="NM_053816.2:242..1843"
                     /note="isoform 1b precursor is encoded by transcript
                     variant 1b"
                     /db_xref="GeneID:116506"
                     /db_xref="RGD:621001"
ORIGIN      
        1 mtprrsrmkr rnlrkpkmrf lllnrftlll lllvsptpvl qaptnltdsg ldqepflylv
       61 grkklldaqy kcydriqqlp pyegegpycn rtwdgwmcwd dtpagvmsyq hcpdyfpdfd
      121 ptekvskycd engewfrhpd snrtwsnytl cnaftpdklh nayvlyylal vghsmsiaal
      181 iasmgiflff knlscqrvtl hknmfltyil nsiiiiihlv evvpngdlvr rdpmhifhhn
      241 tymwtmqwel spplplsahe gkmdphdsev isckilhffh qymmacnyfw mlcegiylht
      301 livmavfted qrlrwyyllg wgfpivptii haitravyyn dncwlsteth llyiihgpvm
      361 aalvvnfffl lnivrvlvtk mrqtheaeay mylkavkatm vlvpllgiqf vvfpwrpsnk
      421 vlgkiydylm hslihfqgff vatiycfcnh evqvtlkrqw aqfkiqwshr wgrrrrptnr
      481 vvsapravaf aepgglpiyi chqeprnppv snnegeegte mipmnviqqd ssa
//
LOCUS       NP_001019437             299 aa            linear   ROD 28-APR-2025
DEFINITION  leucine zipper transcription factor-like protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001019437 XP_236735
VERSION     NP_001019437.1
DBSOURCE    REFSEQ: accession NM_001024266.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Chamling,X., Seo,S., Searby,C.C., Kim,G., Slusarski,D.C. and
            Sheffield,V.C.
  TITLE     The centriolar satellite protein AZI1 interacts with BBS4 and
            regulates ciliary trafficking of the BBSome
  JOURNAL   PLoS Genet 10 (2), e1004083 (2014)
   PUBMED   24550735
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Seo,S., Zhang,Q., Bugge,K., Breslow,D.K., Searby,C.C., Nachury,M.V.
            and Sheffield,V.C.
  TITLE     A novel protein LZTFL1 regulates ciliary trafficking of the BBSome
            and Smoothened
  JOURNAL   PLoS Genet 7 (11), e1002358 (2011)
   PUBMED   22072986
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC092585.1.
            
            On May 27, 2005 this sequence version replaced XP_236735.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092585.1, FQ219473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..299
                     /product="leucine zipper transcription factor-like protein
                     1"
                     /calculated_mol_wt=34507
     Region          20..294
                     /region_name="Leu_zip"
                     /note="Leucine zipper; pfam15294"
                     /db_xref="CDD:464620"
     Region          145..299
                     /region_name="Interaction with BSS9.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q562C6.1)"
     CDS             1..299
                     /gene="Lztfl1"
                     /coded_by="NM_001024266.1:44..943"
                     /db_xref="GeneID:316102"
                     /db_xref="RGD:1306628"
ORIGIN      
        1 maelglnehh qnevinymrf arskrglrlk tvdscfqdlk esrlveetft idevsevlng
       61 lqavvhseve selintahtn vlllrqlfsq aekwylklqt dvselenrel leqvaefeka
      121 efassnkkpi iditkpklvp ineggttell nkeilrlqqe neklksrlkt ietqavnald
      181 eksklervlq dlqldqgnqq dfikaqdldd lentvaalks efqktlndkt enqksleenl
      241 aaakhdllrv qeqlsmaeke lekkfqqtaa yrnmkeiltk kndqikdlrk rlakyesed
//
LOCUS       NP_001073168             388 aa            linear   ROD 28-APR-2025
DEFINITION  cdc42 effector protein 1 [Rattus norvegicus].
ACCESSION   NP_001073168 XP_001076184 XP_235488
VERSION     NP_001073168.1
DBSOURCE    REFSEQ: accession NM_001079700.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Hirsch,D.S., Pirone,D.M. and Burbelo,P.D.
  TITLE     A new family of Cdc42 effector proteins, CEPs, function in
            fibroblast and epithelial cell shape changes
  JOURNAL   J Biol Chem 276 (2), 875-883 (2001)
   PUBMED   11035016
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Joberty,G., Perlungher,R.R. and Macara,I.G.
  TITLE     The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
            proteins
  JOURNAL   Mol Cell Biol 19 (10), 6585-6597 (1999)
   PUBMED   10490598
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128744.1.
            
            On or before Dec 10, 2006 this sequence version replaced
            XP_235488.4, XP_001076184.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128744.1, EX491595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132266, SAMD00132295
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..388
                     /product="cdc42 effector protein 1"
                     /note="binder of Rho GTPases 5; CDC42 effector protein
                     (Rho GTPase binding) 1"
                     /calculated_mol_wt=40898
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91W92; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Region          37..>64
                     /region_name="CRIB"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cl00113"
                     /db_xref="CDD:412170"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91W92; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            53
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Region          117..234
                     /region_name="BORG_CEP"
                     /note="Cdc42 effector; pfam14957"
                     /db_xref="CDD:464403"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91W92; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Region          165..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00587; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Region          237..270
                     /region_name="2 X 7 AA tandem repeats of
                     [PT]-[AT]-A-[ENT]-[PT]-[PTS]-[AG]. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5P0.1)"
     Region          237..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A1A5P0.1)"
     CDS             1..388
                     /gene="Cdc42ep1"
                     /coded_by="NM_001079700.1:103..1269"
                     /db_xref="GeneID:315121"
                     /db_xref="RGD:1311131"
ORIGIN      
        1 mpgpqggtga psmslgklsp vgwvpsshgk rrltadmisp plgdfrhtmh vgrggdvfgd
       61 tsflsnhggr sgnthrsprs flarklqqvr rvgvpprrma spaatspapp pispiiknai
      121 slpqlnqaty dslvvsklsf dstpasstdg rsgyglesgf ctisrlprve khssrdrdhd
      181 rdpdhsqdre qssspsepnp npelrrsdsl lsfrfdldlg psllsellgv mslseapaan
      241 ppapaanpap takppadavt tldtvtslpa ptasspssgr fpngvtavlg pvaevkaspv
      301 gegpqvpskm afdrrgaswg airasrhyte mdarrelagv lpqvhgswes lneewsappa
      361 ssrapvpstv qanafefada deddevkv
//
LOCUS       NP_001004243             659 aa            linear   ROD 28-APR-2025
DEFINITION  RNA polymerase II-associated protein 3 [Rattus norvegicus].
ACCESSION   NP_001004243 XP_217045
VERSION     NP_001004243.1
DBSOURCE    REFSEQ: accession NM_001004243.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Mir,R.A., Bele,A., Mirza,S., Srivastava,S., Olou,A.A., Ammons,S.A.,
            Kim,J.H., Gurumurthy,C.B., Qiu,F., Band,H. and Band,V.
  TITLE     A Novel Interaction of Ecdysoneless (ECD) Protein with R2TP Complex
            Component RUVBL1 Is Required for the Functional Role of ECD in Cell
            Cycle Progression
  JOURNAL   Mol Cell Biol 36 (6), 886-899 (2015)
   PUBMED   26711270
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079414.1.
            
            On Sep 10, 2004 this sequence version replaced XP_217045.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079414.1, SRR8487231.169441.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..659
                     /product="RNA polymerase II-associated protein 3"
                     /calculated_mol_wt=74514
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T3; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          8..41
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          39..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T3; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          107..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T3; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T3; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          126..>352
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          133..166
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          133..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(134,137..138,141..142,144,168,171..172,175..176,
                     178..179,202,205..206,209..210,213)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          166..196
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..200
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          201..234
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          201..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          272..>405
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          282..315
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          282..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(283,286..287,290..291,293,317,320..321,324..325,
                     327..328,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          315..345
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          317..349
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          350..383
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          350..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          447..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T3; propagated from
                     UniProtKB/Swiss-Prot (Q68FQ7.1)"
     Region          539..629
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..659
                     /gene="Rpap3"
                     /coded_by="NM_001004243.1:20..1999"
                     /db_xref="GeneID:300189"
                     /db_xref="RGD:1303036"
ORIGIN      
        1 mtstskavel qlqvkhnaee lqdfmrdleh wektmrqkdl elrrqsgvpe enlppirngs
       61 frkkkkrktk dsskktkeen tknriksfdy dawakldvds ildeldkeds thdsvsqese
      121 sdedgvrvds qkalvlkekg nkyfkqgkyd eaiecytkgm dadpynpvlp tnrasayfrl
      181 kkfavaesdc nlaialsrsy tkayarrgaa rfalqkleda rkdyvkvlel epdnfeatne
      241 lrkidqalts kenshpkdia avikpaeger kanedqrgrq kaiaekdlgn gffkegkyeq
      301 aiecytrgia adstnallpa nramaylkvq kyeeaerdct qailldgsys kafarrgtar
      361 tflgkineak qdfetvllle pgnkqavtel srikkeliek grwddvflds tqrhnvvkpv
      421 dsphrgspka lkkvfieetg nliesvdape ssatvpesdr aavavdtgrk kdfsqgdsvs
      481 sgetprakvl kieavgdssa pqaqvdvkqg vrqsvsekts vrvaqtpgql aavvlppvpa
      541 nsfqlesdfr qlrsspemly qyvkkiepsl ypklfqknld pdvfnqiiki lhdfyverek
      601 palifevler lsqlrrfdma vmfmsgtere ltkvlfnhle kselkedsve elkkryggg
//
LOCUS       NP_001008300             461 aa            linear   ROD 28-APR-2025
DEFINITION  mRNA cap guanine-N(7) methyltransferase [Rattus norvegicus].
ACCESSION   NP_001008300 XP_214547
VERSION     NP_001008300.1
DBSOURCE    REFSEQ: accession NM_001008299.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Varshney,D., Petit,A.P., Bueren-Calabuig,J.A., Jansen,C.,
            Fletcher,D.A., Peggie,M., Weidlich,S., Scullion,P., Pisliakov,A.V.
            and Cowling,V.H.
  TITLE     Molecular basis of RNA guanine-7 methyltransferase (RNMT)
            activation by RAM
  JOURNAL   Nucleic Acids Res 44 (21), 10423-10436 (2016)
   PUBMED   27422871
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Gonatopoulos-Pournatzis,T. and Cowling,V.H.
  TITLE     Cap-binding complex (CBC)
  JOURNAL   Biochem J 457 (2), 231-242 (2014)
   PUBMED   24354960
  REMARK    Review article
            Erratum:[Biochem J. 2014 Feb 15;458(1):185]
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Gonatopoulos-Pournatzis,T., Dunn,S., Bounds,R. and Cowling,V.H.
  TITLE     RAM/Fam103a1 is required for mRNA cap methylation
  JOURNAL   Mol Cell 44 (4), 585-596 (2011)
   PUBMED   22099306
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Bujnicki,J.M., Feder,M., Radlinska,M. and Rychlewski,L.
  TITLE     mRNA:guanine-N7 cap methyltransferases: identification of novel
            members of the family, evolutionary analysis, homology modeling,
            and analysis of sequence-structure-function relationships
  JOURNAL   BMC Bioinformatics 2, 2 (2001)
   PUBMED   11472630
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Niikura,Y. and Mizumoto,K.
  TITLE     Cloning and characterization of three human cDNAs encoding mRNA
            (guanine-7-)-methyltransferase, an mRNA cap methylase
  JOURNAL   Biochem Biophys Res Commun 251 (1), 27-34 (1998)
   PUBMED   9790902
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC085858.1 and CN543861.1.
            
            On Dec 16, 2004 this sequence version replaced XP_214547.2.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC085858.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132261, SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..461
                     /product="mRNA cap guanine-N(7) methyltransferase"
                     /EC_number="2.1.1.56"
                     /note="mRNA cap guanine-N7 methyltransferase; RG7MT1; mRNA
                     cap methyltransferase; mRNA
                     (guanine-N(7)-)-methyltransferase"
                     /calculated_mol_wt=52686
     Region          1..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0L8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0L8; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Region          107..109
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Region          124..460
                     /region_name="Pox_MCEL"
                     /note="mRNA capping enzyme; pfam03291"
                     /db_xref="CDD:281307"
     Site            order(189..195,212..213,245..247,269)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     Site            193
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            199
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            224
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            273
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            355
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     Site            452
                     /site_type="other"
                     /note="mRNA cap binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00895; propagated
                     from UniProtKB/Swiss-Prot (Q5U2U7.1)"
     CDS             1..461
                     /gene="Rnmt"
                     /coded_by="NM_001008299.2:95..1480"
                     /db_xref="GeneID:291534"
                     /db_xref="RGD:1309242"
ORIGIN      
        1 messvkasvd setesspgvn etaaasgqrl sektrqqadq pktqddlveq nssyvqdsps
       61 kkrkldveii ldekhseddg gaskrskler gggsedepsp gglterkrkl qpqdaletqt
      121 rkfqkleegh ssavaahyne lqevglvkrs qsrifylrnf nnwiksilig eilekvrqrk
      181 nrditvldlg cgkggdllkw rkgrisrlvc adiadismkq cqqryedmkc rrdneyifsa
      241 efitadcske llvekfhdpe myfdicscqf achysfesle qadmmlrnac grlnpggyfi
      301 gttpnsfeli rrleasetes fgneiytvkf qkkgnyplfg ckydfnlegv vdvpeflvyf
      361 plltemakky nmkliykktf lefyeekikn nenkmllkrm qalesypane nsklasekag
      421 dyahaaeymk nsqvrlplgt lskseweats iylvfafekq q
//
LOCUS       NP_058876                406 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology-like domain family A member 1 [Rattus
            norvegicus].
ACCESSION   NP_058876
VERSION     NP_058876.2
DBSOURCE    REFSEQ: accession NM_017180.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Sun,L., Gao,G., Wang,X., Zhang,X. and Li,Y.
  TITLE     Protective effect of basic helix-loop-helix family member e40 on
            cerebral ischemia/reperfusion injury: Inhibition of apoptosis via
            repressing the transcription of pleckstrin homology-like domain
            family A, member 1
  JOURNAL   Adv Clin Exp Med 32 (6), 655-666 (2023)
   PUBMED   36881362
  REMARK    GeneRIF: Protective effect of basic helix-loop-helix family member
            e40 on cerebral ischemia/reperfusion injury: Inhibition of
            apoptosis via repressing the transcription of pleckstrin
            homology-like domain family A, member 1.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Guo,Y., Jia,P., Chen,Y., Yu,H., Xin,X., Bao,Y., Yang,H., Wu,N.,
            Sun,Y. and Jia,D.
  TITLE     PHLDA1 is a new therapeutic target of oxidative stress and ischemia
            reperfusion-induced myocardial injury
  JOURNAL   Life Sci 245, 117347 (2020)
   PUBMED   31981628
  REMARK    GeneRIF: role in oxidative stress and ischemia reperfusion-induced
            myocardial injury
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Ono,A., Hirooka,K., Nakano,Y., Nitta,E., Nishiyama,A. and
            Tsujikawa,A.
  TITLE     Gene expression changes in the retina after systemic administration
            of aldosterone
  JOURNAL   Jpn J Ophthalmol 62 (4), 499-507 (2018)
   PUBMED   29713904
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Wang,J., Wang,F., Zhu,J., Song,M., An,J. and Li,W.
  TITLE     Transcriptome Profiling Reveals PHLDA1 as a Novel Molecular Marker
            for Ischemic Cardiomyopathy
  JOURNAL   J Mol Neurosci 65 (1), 102-109 (2018)
   PUBMED   29736818
  REMARK    GeneRIF: Expression of PHLDA1 was elevated in ischemic
            cardiomyopathy.  Overexpression of PHLDA1 promotes apoptosis of
            cardiac muscle cell.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Liu,F., Xu,Z.L., Qian,X.J., Qiu,W.Y. and Huang,H.
  TITLE     Expression of Hsf1, Hsf2, and Phlda1 in cells undergoing
            cryptorchid-induced apoptosis in rat testes
  JOURNAL   Mol Reprod Dev 78 (4), 283-291 (2011)
   PUBMED   21480429
  REMARK    GeneRIF: The expression of Phlda1 mRNA is significantly elevated 3
            days after induction of cryptorchidism.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Gomes,I., Xiong,W., Miki,T. and Rosner,M.R.
  TITLE     A proline- and glutamine-rich protein promotes apoptosis in
            neuronal cells
  JOURNAL   J Neurochem 73 (2), 612-622 (1999)
   PUBMED   10428057
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Park,C.G., Lee,S.Y., Kandala,G., Lee,S.Y. and Choi,Y.
  TITLE     A novel gene product that couples TCR signaling to Fas(CD95)
            expression in activation-induced cell death
  JOURNAL   Immunity 4 (6), 583-591 (1996)
   PUBMED   8673705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            On Sep 1, 2009 this sequence version replaced NP_058876.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF192802.1, CK479569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..406
                     /product="pleckstrin homology-like domain family A member
                     1"
                     /note="PQR protein; proline- and glutamine-rich protein;
                     PQ-rich protein; T-cell death associated"
                     /calculated_mol_wt=45487
     Region          1..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA1.2)"
     Region          188..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA1.2)"
     Region          253..>277
                     /region_name="DUF3622"
                     /note="Protein of unknown function (DUF3622); pfam12286"
                     /db_xref="CDD:432455"
     Region          353..380
                     /region_name="11 X 2 AA repeats of P-H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA1.2)"
     CDS             1..406
                     /gene="Phlda1"
                     /gene_synonym="Tdag"
                     /coded_by="NM_017180.2:2..1222"
                     /db_xref="GeneID:29380"
                     /db_xref="RGD:3836"
ORIGIN      
        1 mrrtpaaerl selgfpprrg sqeppfplgv trgwggwpie krcegprpvp fsersaedgr
       61 eqpahgsgil wrvrtrlslc rdpepppppp plcllrvsll calraggrgs rwsedsarll
      121 llppagasgs lkaerssstp yagrmlessg ckalkegvle krsdgllqlw kkkcciltee
      181 glllippkqv qhqqqqqqqq qpgqgtaeps qpsgpavtsl eppaklkelh fsnmktvdcv
      241 erkgkymyft vvmaegkeid frcpqdqgwn aeitlqmvqy knrqailavk strqkqqhlv
      301 qqqppqtqqi qpqpqpqiqp qpqpqiqpqp qpqpqpqpqp qqqpqpqqlh syphphphly
      361 phphphahsh phphphphph qlqhahqplh sqpqghrllr stsnsa
//
LOCUS       NP_114024                393 aa            linear   ROD 28-APR-2025
DEFINITION  vascular endothelial growth factor A isoform 1 [Rattus norvegicus].
ACCESSION   NP_114024
VERSION     NP_114024.2
DBSOURCE    REFSEQ: accession NM_031836.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Fu,W., Ye,Y. and Hu,F.
  TITLE     LncRNA XIST promotes neovascularization in diabetic retinopathy by
            regulating miR-101-3p/VEGFA
  JOURNAL   Arch Endocrinol Metab 68, e230097 (2024)
   PUBMED   38739522
  REMARK    GeneRIF: LncRNA XIST promotes neovascularization in diabetic
            retinopathy by regulating miR-101-3p/VEGFA.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Li,Z., Xie,L., Zou,L., Xiao,S. and Tao,J.
  TITLE     Overexpression of RAD54L attenuates osteoarthritis by suppressing
            the HIF-1alpha/VEGF signaling pathway: Bioinformatics analysis and
            experimental validation
  JOURNAL   PLoS One 19 (4), e0298575 (2024)
   PUBMED   38593124
  REMARK    GeneRIF: Overexpression of RAD54L attenuates osteoarthritis by
            suppressing the HIF-1alpha/VEGF signaling pathway: Bioinformatics
            analysis and experimental validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Bastide,A., Karaa,Z., Bornes,S., Hieblot,C., Lacazette,E., Prats,H.
            and Touriol,C.
  TITLE     An upstream open reading frame within an IRES controls expression
            of a specific VEGF-A isoform
  JOURNAL   Nucleic Acids Res 36 (7), 2434-2445 (2008)
   PUBMED   18304943
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Meiron,M., Anunu,R., Scheinman,E.J., Hashmueli,S. and Levi,B.Z.
  TITLE     New isoforms of VEGF are translated from alternative initiation CUG
            codons located in its 5'UTR
  JOURNAL   Biochem Biophys Res Commun 282 (4), 1053-1060 (2001)
   PUBMED   11352659
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Terman,B.I., Dougher-Vermazen,M., Carrion,M.E., Dimitrov,D.,
            Armellino,D.C., Gospodarowicz,D. and Bohlen,P.
  TITLE     Identification of the KDR tyrosine kinase as a receptor for
            vascular endothelial cell growth factor
  JOURNAL   Biochem Biophys Res Commun 187 (3), 1579-1586 (1992)
   PUBMED   1417831
REFERENCE   9  (residues 1 to 393)
  AUTHORS   de Vries,C., Escobedo,J.A., Ueno,H., Houck,K., Ferrara,N. and
            Williams,L.T.
  TITLE     The fms-like tyrosine kinase, a receptor for vascular endothelial
            growth factor
  JOURNAL   Science 255 (5047), 989-991 (1992)
   PUBMED   1312256
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Breier,G., Albrecht,U., Sterrer,S. and Risau,W.
  TITLE     Expression of vascular endothelial growth factor during embryonic
            angiogenesis and endothelial cell differentiation
  JOURNAL   Development 114 (2), 521-532 (1992)
   PUBMED   1592003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO565920.1, BC168708.1,
            AF215725.1 and JAXUCZ010000009.1.
            
            On Nov 16, 2007 this sequence version replaced NP_114024.1.
            
            Summary: This gene is a member of the PDGF/VEGF growth factor
            family. It encodes a heparin-binding protein, which exists as a
            disulfide-linked homodimer. This growth factor induces
            proliferation and migration of vascular endothelial cells, and is
            essential for both physiological and pathological angiogenesis.
            Disruption of this gene in mice resulted in abnormal embryonic
            blood vessel formation. This gene is upregulated in many known
            tumors and its expression is correlated with tumor stage and
            progression. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. There is also
            evidence for alternative translation initiation from upstream
            non-AUG (CUG) codons resulting in additional isoforms. A recent
            study showed that a C-terminally extended isoform is produced by
            use of an alternative in-frame translation termination codon via a
            stop codon readthrough mechanism, and that this isoform is
            antiangiogenic. Expression of some isoforms derived from the AUG
            start codon is regulated by a small upstream open reading frame,
            which is located within an internal ribosome entry site. [provided
            by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. This variant can initiate translation from non-AUG
            (CUG) site, and also from a downstream, in-frame AUG site. The
            isoform (1) represented in this RefSeq is derived from the CUG
            start codon and it is the longest isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.1281030.1,
                                           SRR26360194.1524171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 11352659, 11563986
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..393
                     /product="vascular endothelial growth factor A isoform 1"
                     /note="vascular permeability factor"
                     /calculated_mol_wt=42953
     Region          180
                     /region_name="alternative AUG start codon"
     Region          228..310
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(228..231,265,267..270,285..288)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(230,261,265,272,306,308)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(255,264)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Region          345..393
                     /region_name="VEGF_C"
                     /note="VEGF heparin-binding domain; pfam14554"
                     /db_xref="CDD:405273"
     CDS             1..393
                     /gene="Vegfa"
                     /gene_synonym="Vegf; VEGF-A; VEGF111; VEGF164; VPF"
                     /coded_by="NM_031836.3:478..1659"
                     /note="isoform 1 is encoded by transcript variant 1;
                     non-AUG (CUG) translation initiation codon"
                     /db_xref="GeneID:83785"
                     /db_xref="RGD:619991"
ORIGIN      
        1 mtdrqtdtap spsahllagg qptvdaaasr eqepkpapgg gvegvgargi arklfvqllg
       61 sslsgvavvc aaggkpigag rsassglekp gpekrgekek eeergpqwal gsrepgswtg
      121 eaavcadsap aarapqapar asvpegrgar qgaqesglpr spsrrgsasr agpgrasetm
      181 nfllswvhwt lalllylhha kwsqaaptte geqkahevvk fmdvyqrsyc rpietlvdif
      241 qeypdeieyi fkpscvplmr cagccndeal ecvptsesnv tmqimrikph qsqhigemsf
      301 lqhsrcecrp kkdrtkpekk svrgkgkgqk rkrkksrfks wsvhcepcse rrkhlfvqdp
      361 qtckcscknt dsrckarqle lnertcrcdk prr
//
LOCUS       NP_001034104             218 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial fission factor isoform 2 [Rattus norvegicus].
ACCESSION   NP_001034104 XP_217448
VERSION     NP_001034104.1
DBSOURCE    REFSEQ: accession NM_001039015.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Lee,J., Pappalardo,Z., Chopra,D.G., Hennings,T.G., Vaughn,I.,
            Lan,C., Choe,J.J., Ang,K., Chen,S., Arkin,M., McManus,M.T.,
            German,M.S. and Ku,G.M.
  TITLE     A Genetic Interaction Map of Insulin Production Identifies Mfi as
            an Inhibitor of Mitochondrial Fission
  JOURNAL   Endocrinology 159 (9), 3321-3330 (2018)
   PUBMED   30059978
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Zhang,X.M., Zhang,L., Wang,G., Niu,W., He,Z., Ding,L. and Jia,J.
  TITLE     Suppression of mitochondrial fission in experimental cerebral
            ischemia: The potential neuroprotective target of p38 MAPK
            inhibition
  JOURNAL   Neurochem Int 90, 1-8 (2015)
   PUBMED   26116440
REFERENCE   3  (residues 1 to 218)
  AUTHORS   da Silva,A.F., Mariotti,F.R., Maximo,V. and Campello,S.
  TITLE     Mitochondria dynamism: of shape, transport and cell migration
  JOURNAL   Cell Mol Life Sci 71 (12), 2313-2324 (2014)
   PUBMED   24442478
  REMARK    Review article
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Long,B., Wang,K., Li,N., Murtaza,I., Xiao,J.Y., Fan,Y.Y., Liu,C.Y.,
            Li,W.H., Cheng,Z. and Li,P.
  TITLE     miR-761 regulates the mitochondrial network by targeting
            mitochondrial fission factor
  JOURNAL   Free Radic Biol Med 65, 371-379 (2013)
   PUBMED   23867156
  REMARK    GeneRIF: This study reveals a novel model of mitochondrial fission
            regulation, which is composed of miR-761 and mitochondrial fission
            factor
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Palmer,C.S., Elgass,K.D., Parton,R.G., Osellame,L.D.,
            Stojanovski,D. and Ryan,M.T.
  TITLE     Adaptor proteins MiD49 and MiD51 can act independently of Mff and
            Fis1 in Drp1 recruitment and are specific for mitochondrial fission
  JOURNAL   J Biol Chem 288 (38), 27584-27593 (2013)
   PUBMED   23921378
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Loson,O.C., Song,Z., Chen,H. and Chan,D.C.
  TITLE     Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in
            mitochondrial fission
  JOURNAL   Mol Biol Cell 24 (5), 659-667 (2013)
   PUBMED   23283981
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Palmer,C.S., Osellame,L.D., Stojanovski,D. and Ryan,M.T.
  TITLE     The regulation of mitochondrial morphology: intricate mechanisms
            and dynamic machinery
  JOURNAL   Cell Signal 23 (10), 1534-1545 (2011)
   PUBMED   21683788
  REMARK    Review article
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Otera,H., Wang,C., Cleland,M.M., Setoguchi,K., Yokota,S.,
            Youle,R.J. and Mihara,K.
  TITLE     Mff is an essential factor for mitochondrial recruitment of Drp1
            during mitochondrial fission in mammalian cells
  JOURNAL   J Cell Biol 191 (6), 1141-1158 (2010)
   PUBMED   21149567
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Dixit,E., Boulant,S., Zhang,Y., Lee,A.S., Odendall,C., Shum,B.,
            Hacohen,N., Chen,Z.J., Whelan,S.P., Fransen,M., Nibert,M.L.,
            Superti-Furga,G. and Kagan,J.C.
  TITLE     Peroxisomes are signaling platforms for antiviral innate immunity
  JOURNAL   Cell 141 (4), 668-681 (2010)
   PUBMED   20451243
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Gandre-Babbe,S. and van der Bliek,A.M.
  TITLE     The novel tail-anchored membrane protein Mff controls mitochondrial
            and peroxisomal fission in mammalian cells
  JOURNAL   Mol Biol Cell 19 (6), 2402-2412 (2008)
   PUBMED   18353969
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1, FN804971.1 and BC098682.1.
            
            On Jan 12, 2006 this sequence version replaced XP_217448.3.
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons, compared to variant 1. The encoded isoform (2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360172.2500758.1,
                                           SRR26643289.26208.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q34"
     Protein         1..218
                     /product="mitochondrial fission factor isoform 2"
                     /calculated_mol_wt=24840
     Region          1..218
                     /region_name="Miff"
                     /note="Mitochondrial and peroxisomal fission factor Mff;
                     pfam05644"
                     /db_xref="CDD:461701"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZY8; propagated from
                     UniProtKB/Swiss-Prot (Q4KM98.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9GZY8; propagated from
                     UniProtKB/Swiss-Prot (Q4KM98.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM98.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PCP5; propagated from
                     UniProtKB/Swiss-Prot (Q4KM98.1)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PCP5; propagated from
                     UniProtKB/Swiss-Prot (Q4KM98.1)"
     Site            199..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM98.1)"
     CDS             1..218
                     /gene="Mff"
                     /gene_synonym="RGD1310230"
                     /coded_by="NM_001039015.2:342..998"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:301563"
                     /db_xref="RGD:1310230"
ORIGIN      
        1 maeisriqye meytegisqr mrvpeklkva ppnadleqgf qdgvpnasvi mqvperivvt
       61 gnnedisfsr padldliqst pfkplalktp prvltlserp ldfldlerpp ptpqseeira
      121 vgrlkrersm senavrqngq lvrndsmygi ssldaavega sedmsvvdaa slrrqiikln
      181 rrlqlleeen kerakremvm ysitvafwll nswlwfrr
//
LOCUS       NP_783638                161 aa            linear   ROD 28-APR-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase-like 3 [Rattus norvegicus].
ACCESSION   NP_783638
VERSION     NP_783638.1
DBSOURCE    REFSEQ: accession NM_175707.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Mesa,A., Somarelli,J.A. and Herrera,R.J.
  TITLE     Spliceosomal immunophilins
  JOURNAL   FEBS Lett 582 (16), 2345-2351 (2008)
   PUBMED   18544344
  REMARK    Review article
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087645.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087645.1, FQ214147.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q31"
     Protein         1..161
                     /product="peptidyl-prolyl cis-trans isomerase-like 3"
                     /EC_number="5.2.1.8"
                     /note="PPIase; cyclophilin-like protein PPIL3; rotamase
                     PPIL3; peptidylprolyl cis-trans isomerase-like protein 3;
                     cyclophilin-like protein 3; peptidylprolyl isomerase
                     (cyclophilin)-like 3"
                     /calculated_mol_wt=17982
     Region          1..154
                     /region_name="Cyclophilin_PPIL3_like"
                     /note="Proteins similar to Human cyclophilin-like
                     peptidylprolyl cis- trans isomerase (PPIL3). Members of
                     this family lack a key residue important for cyclosporin
                     binding: the tryptophan residue corresponding to W121 in
                     human hCyP-18a; most members have a...; cd01928"
                     /db_xref="CDD:238909"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H2H8; propagated from
                     UniProtKB/Swiss-Prot (Q812D3.1)"
     Site            order(43..44,49,100,102,110)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238909"
     Site            61
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9D6L8; propagated from
                     UniProtKB/Swiss-Prot (Q812D3.1)"
     CDS             1..161
                     /gene="Ppil3"
                     /gene_synonym="Cyp10l"
                     /coded_by="NM_175707.3:319..804"
                     /db_xref="GeneID:301432"
                     /db_xref="RGD:631415"
ORIGIN      
        1 msvtlhtdvg dikievfcer tpktcenfla lcasnyyngc vfhrnikgfm vqtgdptgtg
       61 rggssiwgkk fedeyseylk hnvrgvvsma nngpntngsq ffitygkqph ldmkytvfgk
      121 vidgletlde leklpvnekt yrplndvhik ditihanpfa q
//
LOCUS       NP_036934               1088 aa            linear   ROD 28-APR-2025
DEFINITION  platelet-derived growth factor receptor alpha precursor [Rattus
            norvegicus].
ACCESSION   NP_036934 XP_001067574 XP_001067631 XP_001067681 XP_214030
VERSION     NP_036934.1
DBSOURCE    REFSEQ: accession NM_012802.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1088)
  AUTHORS   Zhou,H., Yang,Z., Mu,L. and Shi,Y.
  TITLE     Integrated Analysis of Multiple Microarray Studies to Identify Core
            Gene-Expression Signatures Involved in Tubulointerstitial Injury in
            Diabetic Nephropathy
  JOURNAL   Biomed Res Int 2022, 9554658 (2022)
   PUBMED   35592524
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1088)
  AUTHORS   Zhu,Y., Li,F., Shi,W., Zhai,C., Wang,J., Yan,X., Wang,Q., Zhang,Q.,
            Yang,L., Gao,L. and Li,M.
  TITLE     COP9 signalosome subunit 6 mediates PDGF -induced pulmonary
            arterial smooth muscle cells proliferation
  JOURNAL   Exp Cell Res 371 (2), 379-388 (2018)
   PUBMED   30180991
  REMARK    GeneRIF: CSN6 mediates PDGF-induced pulmonary arterial smooth
            muscle cells proliferation.
REFERENCE   3  (residues 1 to 1088)
  AUTHORS   Zhang,X., Zhao,F., Zhao,J.F., Fu,H.Y., Huang,X.J. and Lv,B.D.
  TITLE     PDGF-mediated PI3K/AKT/beta-catenin signaling regulates gap
            junctions in corpus cavernosum smooth muscle cells
  JOURNAL   Exp Cell Res 362 (2), 252-259 (2018)
   PUBMED   29174980
  REMARK    GeneRIF: Treatment with different concentrations of PDGF increased
            the levels of phosphorylated protein kinase B (AKT), beta-catenin,
            and Cx43, whereas inhibition of PDGFR or activation of
            phosphatidylinositol 3 kinase (PI3K)/AKT signaling altered
            b-catenin and Cx43 expression.
REFERENCE   4  (residues 1 to 1088)
  AUTHORS   Schmid,F.M., Schou,K.B., Vilhelm,M.J., Holm,M.S., Breslin,L.,
            Farinelli,P., Larsen,L.A., Andersen,J.S., Pedersen,L.B. and
            Christensen,S.T.
  TITLE     IFT20 modulates ciliary PDGFRalpha signaling by regulating the
            stability of Cbl E3 ubiquitin ligases
  JOURNAL   J Cell Biol 217 (1), 151-161 (2018)
   PUBMED   29237719
REFERENCE   5  (residues 1 to 1088)
  AUTHORS   Yan,J.F., Huang,W.J., Zhao,J.F., Fu,H.Y., Zhang,G.Y., Huang,X.J.
            and Lv,B.D.
  TITLE     The platelet-derived growth factor receptor/STAT3 signaling pathway
            regulates the phenotypic transition of corpus cavernosum smooth
            muscle in rats
  JOURNAL   PLoS One 12 (2), e0172191 (2017)
   PUBMED   28245285
  REMARK    GeneRIF: STAT3 overexpression in corpus cavernosum smooth muscle in
            rats weakened the suppressive effect of PDGFR inhibition on the
            morphology and phenotypic transformation induced by PDGF-BB
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1088)
  AUTHORS   Sarzani,R., Arnaldi,G., Takasaki,I., Brecher,P. and Chobanian,A.V.
  TITLE     Effects of hypertension and aging on platelet-derived growth factor
            and platelet-derived growth factor receptor expression in rat aorta
            and heart
  JOURNAL   Hypertension 18 (5 Suppl), III93-III99 (1991)
   PUBMED   1657776
REFERENCE   7  (residues 1 to 1088)
  AUTHORS   Yu,J.C., Heidaran,M.A., Pierce,J.H., Gutkind,J.S., Lombardi,D.,
            Ruggiero,M. and Aaronson,S.A.
  TITLE     Tyrosine mutations within the alpha platelet-derived growth factor
            receptor kinase insert domain abrogate receptor-associated
            phosphatidylinositol-3 kinase activity without affecting mitogenic
            or chemotactic signal transduction
  JOURNAL   Mol Cell Biol 11 (7), 3780-3785 (1991)
   PUBMED   1646396
REFERENCE   8  (residues 1 to 1088)
  AUTHORS   Lee,K.H., Bowen-Pope,D.F. and Reed,R.R.
  TITLE     Isolation and characterization of the alpha platelet-derived growth
            factor receptor from rat olfactory epithelium
  JOURNAL   Mol Cell Biol 10 (5), 2237-2246 (1990)
   PUBMED   2157969
REFERENCE   9  (residues 1 to 1088)
  AUTHORS   Seifert,R.A., Hart,C.E., Phillips,P.E., Forstrom,J.W., Ross,R.,
            Murray,M.J. and Bowen-Pope,D.F.
  TITLE     Two different subunits associate to create isoform-specific
            platelet-derived growth factor receptors
  JOURNAL   J Biol Chem 264 (15), 8771-8778 (1989)
   PUBMED   2542288
REFERENCE   10 (residues 1 to 1088)
  AUTHORS   Matsui,T., Heidaran,M., Miki,T., Popescu,N., La Rochelle,W.,
            Kraus,M., Pierce,J. and Aaronson,S.
  TITLE     Isolation of a novel receptor cDNA establishes the existence of two
            PDGF receptor genes
  JOURNAL   Science 243 (4892), 800-804 (1989)
   PUBMED   2536956
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M63837.1, Z14118.1, CK477487.1, CB801421.1, CK475330.1, CK475090.1,
            CA512174.1, CB738013.1, CK478629.1, DV719360.1 and CA505634.1.
            
            On or before Oct 13, 2007 this sequence version replaced
            XP_001067631.1, XP_001067574.1, XP_001067681.1, XP_214030.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M63837.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1088
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..1088
                     /product="platelet-derived growth factor receptor alpha
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="alpha-type platelet-derived growth factor receptor;
                     PDGF-R-alpha; CD140 antigen-like family member A;
                     PDGFR-alpha; alpha platelet-derived growth factor
                     receptor; platelet-derived growth factor alpha receptor;
                     platelet-derived growth factor receptor alpha-like;
                     platelet derived growth factor receptor, alpha
                     polypeptide"
                     /calculated_mol_wt=120336
     sig_peptide     1..23
                     /note="propagated from UniProtKB/Swiss-Prot (P20786.2)"
                     /calculated_mol_wt=2382
     mat_peptide     24..1088
                     /product="Platelet-derived growth factor receptor alpha.
                     /id=PRO_0000016762"
                     /note="propagated from UniProtKB/Swiss-Prot (P20786.2)"
                     /calculated_mol_wt=120336
     Region          27..99
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Region          211..309
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          230..234
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          243..247
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          272..276
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          286..291
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..304
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          312..412
                     /region_name="Ig4_PDGFR"
                     /note="Fourth immunoglobulin (Ig)-like domain of
                     platelet-derived growth factor receptor (PDGFR); cd05859"
                     /db_xref="CDD:409445"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            528..548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20786.2)"
     Region          554..955
                     /region_name="PTKc_PDGFR_alpha"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Platelet Derived Growth Factor Receptor alpha; cd05105"
                     /db_xref="CDD:173653"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            order(598..599,601..604,606,624,626,674,676,680,817,
                     821..822,824,835,853..857,866,901)
                     /site_type="active"
                     /db_xref="CDD:173653"
     Site            order(598..599,601..604,606,624,626,674,676,680,821..822,
                     824,835)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173653"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            order(817,821,853..857,866,901)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173653"
     Site            834..859
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173653"
     Site            848
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     Region          1017..1088
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20786.2)"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P16234; propagated from
                     UniProtKB/Swiss-Prot (P20786.2)"
     CDS             1..1088
                     /gene="Pdgfra"
                     /gene_synonym="APDGFR; PDGFACE"
                     /coded_by="NM_012802.1:134..3400"
                     /db_xref="GeneID:25267"
                     /db_xref="RGD:3284"
ORIGIN      
        1 mgtsqaflvl sclltgpsli vcqlllpsil pnenekivpl sssfslrcfg esevswqhpm
       61 seeedpnvei rteennsslf vtvlevvnas aahtgwytcy ynhtqteese iegrhiyiyv
      121 pdpdmafvpl gmtdslvive eddsaiipcr ttdpdtevtl hnngrlvpas ydsrqgfngt
      181 fsvgpyicea tvrgrtfkts efnvyalkat selnlemdtr qtvykageti vvtcavfnne
      241 vvdlqwtypg evrnkgitml eeiklpsikl vytltvpkat vkdsgdyeca arqatkevke
      301 mktvtisvhe kgfvqirptf ghletvnlhq vrefvvevqa yptpriswlk dnltlienlt
      361 eittdvqrsq etryqsklkl irakeedsgh ytiivqnddd mksytfelst lvpasilelv
      421 ddhhgsgggq tvrctaegtp lpniewmick dikkcnndts wtvlasnvsn iitefhqrgr
      481 stvegrvsfa kveetiavrc lakndlgign relklvaptl rseltvaaav lvllvivivs
      541 livlvviwkq kpryeirwrv iesispdghe yiyvdpmqlp ydsrwefprd glvlgrilgs
      601 gafgkvvegt ayglsrsqpv mkvavkmlkp tarssekqal mselkimthl gphlnivnll
      661 gactksgpiy iiteycfygd lvnylhknrd sfmsrhpekp kkdldifgln padestrsyv
      721 ilsfenngdy vdmkqadttq yvpmlerkev skysdiqrsl ydrpasykkk smldseaknl
      781 lsdddseglt lldllsftyq vargmeflas kncvhrdlaa rnvllaqgki vkicdfglar
      841 dimhdsnyvs kgstflpvkw mapesifdnl yttlsdvwsy gvllweifsl ggtpypgmmv
      901 dstfynkiks gyrmakpdha tsevyeimvq cwnsepekrp sfyhlseive nllpgqykks
      961 yekihldflk sdhpavarmr vdsdnayigv tykneedklk eweggldeqr lsadsgyiip
     1021 lpdidpvpee edlgkrnrhs sqtseesaie tgsssstfik redetiedid mmddigidss
     1081 dlvedsfl
//
LOCUS       NP_036767                246 aa            linear   ROD 28-APR-2025
DEFINITION  serine protease 1 precursor [Rattus norvegicus].
ACCESSION   NP_036767
VERSION     NP_036767.1
DBSOURCE    REFSEQ: accession NM_012635.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Yang,H., Zhang,H., Chen,Z., Wang,Y. and Gao,B.
  TITLE     Effects of tRNA-derived fragments and microRNAs regulatory network
            on pancreatic acinar intracellular trypsinogen activation
  JOURNAL   Bioengineered 13 (2), 3207-3220 (2022)
   PUBMED   35045793
  REMARK    GeneRIF: Effects of tRNA-derived fragments and microRNAs regulatory
            network on pancreatic acinar intracellular trypsinogen activation.
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Chang,M., Alsaigh,T., Kistler,E.B. and Schmid-Schonbein,G.W.
  TITLE     Breakdown of mucin as barrier to digestive enzymes in the ischemic
            rat small intestine
  JOURNAL   PLoS One 7 (6), e40087 (2012)
   PUBMED   22768227
  REMARK    GeneRIF: These results indicate that mucin plays an important role
            in the preservation of the mucosal barrier and that ischemia but
            not digestive enzymes disturbs mucin integrity, while digestive
            enzymes actively mediate epithelial cell disruption.
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Lauhio,A., Sorsa,T., Srinivas,R., Stenman,M., Tervahartiala,T.,
            Stenman,U.H., Gronhagen-Riska,C. and Honkanen,E.
  TITLE     Urinary matrix metalloproteinase -8, -9, -14 and their regulators
            (TRY-1, TRY-2, TATI) in patients with diabetic nephropathy
  JOURNAL   Ann Med 40 (4), 312-320 (2008)
   PUBMED   18428024
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Towatari,T., Ide,M., Ohba,K., Chiba,Y., Murakami,M., Shiota,M.,
            Kawachi,M., Yamada,H. and Kido,H.
  TITLE     Identification of ectopic anionic trypsin I in rat lungs
            potentiating pneumotropic virus infectivity and increased enzyme
            level after virus infection
  JOURNAL   Eur J Biochem 269 (10), 2613-2621 (2002)
   PUBMED   12027901
  REMARK    GeneRIF: ectopic anionic trypsin I in rat lungs induced by virus
            infection may trigger virus spread in rat lungs
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Dakka,N., Puigserver,A. and Wicker,C.
  TITLE     Regulation by a protein-free carbohydrate-rich diet of rat
            pancreatic mRNAs encoding trypsin and elastase isoenzymes
  JOURNAL   Biochem J 268 (2), 471-474 (1990)
   PUBMED   2363685
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Dubick,M.A. and Majumdar,A.P.
  TITLE     Biochemical changes in the exocrine pancreas of rats fed caffeine
  JOURNAL   Proc Soc Exp Biol Med 191 (2), 153-158 (1989)
   PUBMED   2726780
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Dubick,M.A., Palmer,R., Lau,P.P., Morrill,P.R. and Geokas,M.C.
  TITLE     Altered exocrine pancreatic function in rats treated with nicotine
  JOURNAL   Toxicol Appl Pharmacol 96 (1), 132-139 (1988)
   PUBMED   2460970
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Fletcher,T.S., Tsukamoto,H. and Largman,C.
  TITLE     Immunoenzymometric determination of trypsin/alpha 1-protease
            inhibitor complex in plasma of rats with experimental pancreatitis
  JOURNAL   Clin Chem 32 (9), 1738-1741 (1986)
   PUBMED   3527480
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Majumdar,A.P., Vesenka,G.D., Dubick,M.A., Yu,G.S., DeMorrow,J.M.
            and Geokas,M.C.
  TITLE     Morphological and biochemical changes of the pancreas in rats
            treated with acetaldehyde
  JOURNAL   Am J Physiol 250 (5 Pt 1), G598-G606 (1986)
   PUBMED   2422952
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from V01273.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: V01273.1, FQ211333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..246
                     /product="serine protease 1 precursor"
                     /EC_number="3.4.21.4"
                     /note="protease, serine, 2; anionic trypsin-1;
                     pretrypsinogen I; anionic trypsin I; pancreatic trypsin 1;
                     protease, serine, 1 (trypsin 1); protease, serine 1;
                     beta-trypsin; cationic trypsinogen"
                     /calculated_mol_wt=24565
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1413
     mat_peptide     24..246
                     /product="Serine protease 1. /id=PRO_0000028208"
                     /note="propagated from UniProtKB/Swiss-Prot (P00762.1)"
                     /calculated_mol_wt=23605
     Region          24..242
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            24
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(63,107,200)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(194,215,217)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            194
                     /site_type="other"
                     /note="Required for specificity; propagated from
                     UniProtKB/Swiss-Prot (P00762.1)"
     CDS             1..246
                     /gene="Prss1"
                     /gene_synonym="PTRYI; RATPTRYI; Try1"
                     /coded_by="NM_012635.1:13..753"
                     /db_xref="GeneID:24691"
                     /db_xref="RGD:3417"
ORIGIN      
        1 msallilalv gaavafpled ddkivggytc pehsvpyqvs lnsgyhfcgg slindqwvvs
       61 aahcyksriq vrlgehninv legdeqfina akiikhpnys swtlnndiml iklsspvkln
      121 arvapvalps acapagtqcl isgwgntlsn gvnnpdllqc vdapvlsqad ceaaypgeit
      181 ssmicvgfle ggkdscqgds ggpvvcngql qgivswgygc alpdnpgvyt kvcnfvgwiq
      241 dtiaan
//
LOCUS       NP_001013876             237 aa            linear   ROD 28-APR-2025
DEFINITION  biorientation of chromosomes in cell division protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001013876 XP_213257
VERSION     NP_001013876.2
DBSOURCE    REFSEQ: accession NM_001013854.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Porter,I.M., Schleicher,K., Porter,M. and Swedlow,J.R.
  TITLE     Bod1 regulates protein phosphatase 2A at mitotic kinetochores
  JOURNAL   Nat Commun 4, 2677 (2013)
   PUBMED   24157919
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Porter,I.M., McClelland,S.E., Khoudoli,G.A., Hunter,C.J.,
            Andersen,J.S., McAinsh,A.D., Blow,J.J. and Swedlow,J.R.
  TITLE     Bod1, a novel kinetochore protein required for chromosome
            biorientation
  JOURNAL   J Cell Biol 179 (2), 187-197 (2007)
   PUBMED   17938248
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079025.1.
            
            On Sep 13, 2012 this sequence version replaced NP_001013876.1.
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079025.1, CK355577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q12"
     Protein         1..237
                     /product="biorientation of chromosomes in cell division
                     protein 1"
                     /note="biorientation defective protein 1; family with
                     sequence similarity 44, member B"
                     /calculated_mol_wt=25105
     Region          107..200
                     /region_name="COMPASS-Shg1"
                     /note="COMPASS (Complex proteins associated with Set1p)
                     component shg1; pfam05205"
                     /db_xref="CDD:461586"
     CDS             1..237
                     /gene="Bod1"
                     /gene_synonym="Fam44b; RGD1305622"
                     /coded_by="NM_001013854.1:56..769"
                     /db_xref="GeneID:287173"
                     /db_xref="RGD:1305622"
ORIGIN      
        1 mqrslvtlld erqqrgqrga pwssppptlp ppsppppwgp pclrsaahgs rrssrargra
       61 rgaamadsag agaagqasgp aggssgaggt vnpaslppgd pqlialiveq lksrglfdsf
      121 rrdcladvdt kpayqnlrqk vdnfvsthld kqewnpamnk nqlrnglrqs vvqsgmleag
      181 vdriisqvvd pklnhifrpq ieraihefla aqkkeavpap ppepegqdpp apsqdas
//
LOCUS       NP_058797                164 aa            linear   ROD 28-APR-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase A [Rattus norvegicus].
ACCESSION   NP_058797
VERSION     NP_058797.1
DBSOURCE    REFSEQ: accession NM_017101.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Kalinina,A., Tilova,L., Kirsanov,K., Lesovaya,E., Zhidkova,E.,
            Fetisov,T., Ilyinskaya,G., Yakubovskaya,M., Kazansky,D. and
            Khromykh,L.
  TITLE     Secreted cyclophilin A is non-genotoxic but acts as a tumor
            promoter
  JOURNAL   Toxicology 500, 153675 (2023)
   PUBMED   37993081
  REMARK    GeneRIF: Secreted cyclophilin A is non-genotoxic but acts as a
            tumor promoter.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Demir,B., Kersin,B., Gojayeva,F., Arman,A. and Binnetoglu,A.
  TITLE     Concentrations of Serum Cyclophilin A in Patients With Bell Palsy
  JOURNAL   J Craniofac Surg 31 (4), e368-e370 (2020)
   PUBMED   32149981
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Bouybayoune,I., Comerio,L., Pasetto,L., Bertani,I., Bonetto,V. and
            Chiesa,R.
  TITLE     Cyclophillin A deficiency accelerates RML-induced prion disease
  JOURNAL   Neurobiol Dis 130, 104498 (2019)
   PUBMED   31181281
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Liu,L., Zuo,L., Yang,J., Xin,S., Zhang,J., Zhou,J., Li,G., Tang,J.
            and Lu,J.
  TITLE     Exosomal cyclophilin A as a novel noninvasive biomarker for
            Epstein-Barr virus associated nasopharyngeal carcinoma
  JOURNAL   Cancer Med 8 (6), 3142-3151 (2019)
   PUBMED   31063269
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Tian,H., Yu,D., Hu,Y., Zhang,P., Yang,Y., Hu,Q. and Li,M.
  TITLE     Angiotensin II upregulates cyclophilin A by enhancing ROS
            production in rat cardiomyocytes
  JOURNAL   Mol Med Rep 18 (5), 4349-4355 (2018)
   PUBMED   30221707
  REMARK    GeneRIF: the action of Ang II was primarily dependent on the
            angiotensin type 2 receptor (AT2R), not the type 1 receptor. These
            results provided an insight into the role of the AT2R signaling
            pathway in Ang IIinduced myocardial hypertrophy
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Braaten,D. and Luban,J.
  TITLE     Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene
            targeting in human T cells
  JOURNAL   EMBO J 20 (6), 1300-1309 (2001)
   PUBMED   11250896
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Connern,C.P. and Halestrap,A.P.
  TITLE     Purification and N-terminal sequencing of peptidyl-prolyl
            cis-trans-isomerase from rat liver mitochondrial matrix reveals the
            existence of a distinct mitochondrial cyclophilin
  JOURNAL   Biochem J 284 (Pt 2) (Pt 2), 381-385 (1992)
   PUBMED   1599421
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Lad,R.P., Smith,M.A. and Hilt,D.C.
  TITLE     Molecular cloning and regional distribution of rat brain
            cyclophilin
  JOURNAL   Brain Res Mol Brain Res 9 (3), 239-244 (1991)
   PUBMED   1851525
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Danielson,P.E., Forss-Petter,S., Brow,M.A., Calavetta,L.,
            Douglass,J., Milner,R.J. and Sutcliffe,J.G.
  TITLE     p1B15: a cDNA clone of the rat mRNA encoding cyclophilin
  JOURNAL   DNA 7 (4), 261-267 (1988)
   PUBMED   3293952
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Theodor,L., Peleg,D. and Meyuhas,O.
  TITLE     P31, a mammalian housekeeping protein encoded by a multigene family
            containing a high proportion of pseudogenes
  JOURNAL   Biochim Biophys Acta 826 (2-3), 137-146 (1985)
   PUBMED   2996604
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M19533.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M19533.1, FQ241390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..164
                     /product="peptidyl-prolyl cis-trans isomerase A"
                     /EC_number="5.2.1.8"
                     /note="PPIase A; rotamase A; cyclophilin A; cyclosporin
                     A-binding protein"
                     /calculated_mol_wt=17743
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline, in Peptidyl-prolyl cis-trans
                     isomerase A, N-terminally processed.
                     /evidence=ECO:0000269|Ref.7; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Region          4..162
                     /region_name="cyclophilin_ABH_like"
                     /note="Cyclophilin A, B and H-like cyclophilin-type
                     peptidylprolyl cis- trans isomerase (PPIase) domain. This
                     family represents the archetypal cystolic cyclophilin
                     similar to human cyclophilins A, B and H. PPIase is an
                     enzyme which accelerates protein folding...; cd01926"
                     /db_xref="CDD:238907"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            order(54..55,60,111,113,121)
                     /site_type="active"
                     /db_xref="CDD:238907"
     Site            76
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62937; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     Site            133
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17742; propagated from
                     UniProtKB/Swiss-Prot (P10111.2)"
     CDS             1..164
                     /gene="Ppia"
                     /gene_synonym="CYCA; CyP-A; p1B15; p31"
                     /coded_by="NM_017101.1:43..537"
                     /db_xref="GeneID:25518"
                     /db_xref="RGD:3372"
ORIGIN      
        1 mvnptvffdi tadgeplgrv cfelfadkvp ktaenfrals tgekgfgykg ssfhriipgf
       61 mcqggdftrh ngtggksiyg ekfedenfil khtgpgilsm anagpntngs qffictakte
      121 wldgkhvvfg kvkegmsive amerfgsrng ktskkitisd cgql
//
LOCUS       NP_001007652             283 aa            linear   ROD 28-APR-2025
DEFINITION  peflin [Rattus norvegicus].
ACCESSION   NP_001007652 XP_238392
VERSION     NP_001007652.1
DBSOURCE    REFSEQ: accession NM_001007651.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Sargeant,J., Seiler,D.K., Costain,T., Madreiter-Sokolowski,C.T.,
            Gordon,D.E., Peden,A.A., Malli,R., Graier,W.F. and Hay,J.C.
  TITLE     ALG-2 and peflin regulate COPII targeting and secretion in response
            to calcium signaling
  JOURNAL   J Biol Chem 297 (6), 101393 (2021)
   PUBMED   34762908
  REMARK    GeneRIF: ALG-2 and peflin regulate COPII targeting and secretion in
            response to calcium signaling.
REFERENCE   2  (residues 1 to 283)
  AUTHORS   McGourty,C.A., Akopian,D., Walsh,C., Gorur,A., Werner,A.,
            Schekman,R., Bautista,D. and Rape,M.
  TITLE     Regulation of the CUL3 Ubiquitin Ligase by a Calcium-Dependent
            Co-adaptor
  JOURNAL   Cell 167 (2), 525-538 (2016)
   PUBMED   27716508
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Rayl,M., Truitt,M., Held,A., Sargeant,J., Thorsen,K. and Hay,J.C.
  TITLE     Penta-EF-Hand Protein Peflin Is a Negative Regulator of ER-To-Golgi
            Transport
  JOURNAL   PLoS One 11 (6), e0157227 (2016)
   PUBMED   27276012
  REMARK    GeneRIF: This work identifies for the first time a clear steady
            state role for a PEF protein in ER-to-Golgi transport-peflin is a
            negative regulator of transport.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Kitaura,Y., Satoh,H., Takahashi,H., Shibata,H. and Maki,M.
  TITLE     Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
            by dimerization through their fifth EF-hand regions
  JOURNAL   Arch Biochem Biophys 399 (1), 12-18 (2002)
   PUBMED   11883899
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Kitaura,Y., Matsumoto,S., Satoh,H., Hitomi,K. and Maki,M.
  TITLE     Peflin and ALG-2, members of the penta-EF-hand protein family, form
            a heterodimer that dissociates in a Ca2+-dependent manner
  JOURNAL   J Biol Chem 276 (17), 14053-14058 (2001)
   PUBMED   11278427
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082028.1.
            
            On Nov 29, 2004 this sequence version replaced XP_238392.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082028.1, FQ219120.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..283
                     /product="peflin"
                     /note="penta-EF hand domain-containing protein 1; PEF
                     protein with a long N-terminal hydrophobic domain"
                     /calculated_mol_wt=29881
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z8.1)"
     Region          21..108
                     /region_name="9 X 9 AA approximate tandem repeat of
                     [AP]-P-G-G-P-Y-G-G-P-P"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z8.1)"
     Region          56..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z8.1)"
     Region          117..282
                     /region_name="EFh_PEF_peflin"
                     /note="EF-hand, calcium binding motif, found in peflin and
                     similar proteins; cd16184"
                     /db_xref="CDD:320059"
     Region          117..146
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Site            order(126,128,130,137,193,195,197,204)
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:320059"
     Region          154..183
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          184..214
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          203..283
                     /region_name="Required for interaction with PDCD6.
                     /evidence=ECO:0000250|UniProtKB:Q9UBV8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z8.1)"
     Region          220..250
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          251..282
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     CDS             1..283
                     /gene="Pef1"
                     /gene_synonym="Peflin"
                     /coded_by="NM_001007651.1:13..864"
                     /db_xref="GeneID:297900"
                     /db_xref="RGD:1359536"
ORIGIN      
        1 masypdgqsy pgaagqvpgp hpggyypgpp hgggqygsgf ppggygapap ggpygypsag
       61 gtpsgtpggp ygggppggpy gggppggpyg qahpspygtq ppgpygqggv ppnvdpeays
      121 wfqsvdadhs gyislkelkq alvnsnwssf ndetclmmin mfdktktgri dvvgfsalwk
      181 flqqwknlfq qydrdhsgsi sstelqqals qmgynlspqf tqllvsryct rsaipamqld
      241 cfikvctqlq vlteafrekd tavqgnirls fedfvtmtas rml
//
LOCUS       NP_001099694             223 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin-conjugating enzyme E2 S [Rattus norvegicus].
ACCESSION   NP_001099694 XP_001071810 XP_214806
VERSION     NP_001099694.1
DBSOURCE    REFSEQ: accession NM_001106224.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wang,W. and Kirschner,M.W.
  TITLE     Emi1 preferentially inhibits ubiquitin chain elongation by the
            anaphase-promoting complex
  JOURNAL   Nat Cell Biol 15 (7), 797-806 (2013)
   PUBMED   23708001
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Wickliffe,K.E., Lorenz,S., Wemmer,D.E., Kuriyan,J. and Rape,M.
  TITLE     The mechanism of linkage-specific ubiquitin chain elongation by a
            single-subunit E2
  JOURNAL   Cell 144 (5), 769-781 (2011)
   PUBMED   21376237
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Bremm,A., Freund,S.M. and Komander,D.
  TITLE     Lys11-linked ubiquitin chains adopt compact conformations and are
            preferentially hydrolyzed by the deubiquitinase Cezanne
  JOURNAL   Nat Struct Mol Biol 17 (8), 939-947 (2010)
   PUBMED   20622874
REFERENCE   4  (residues 1 to 223)
  AUTHORS   David,Y., Ziv,T., Admon,A. and Navon,A.
  TITLE     The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
            preferred lysines
  JOURNAL   J Biol Chem 285 (12), 8595-8604 (2010)
   PUBMED   20061386
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Garnett,M.J., Mansfeld,J., Godwin,C., Matsusaka,T., Wu,J.,
            Russell,P., Pines,J. and Venkitaraman,A.R.
  TITLE     UBE2S elongates ubiquitin chains on APC/C substrates to promote
            mitotic exit
  JOURNAL   Nat Cell Biol 11 (11), 1363-1369 (2009)
   PUBMED   19820702
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Williamson,A., Wickliffe,K.E., Mellone,B.G., Song,L., Karpen,G.H.
            and Rape,M.
  TITLE     Identification of a physiological E2 module for the human
            anaphase-promoting complex
  JOURNAL   Proc Natl Acad Sci U S A 106 (43), 18213-18218 (2009)
   PUBMED   19822757
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC169077.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_214806.1, XP_001071810.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC169077.1, EV772705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..223
                     /product="ubiquitin-conjugating enzyme E2 S"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-protein ligase S; ubiquitin carrier
                     protein S; E2 ubiquitin-conjugating enzyme S"
                     /calculated_mol_wt=24084
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q16763; propagated from
                     UniProtKB/Swiss-Prot (B5DFI8.1)"
     Region          10..155
                     /region_name="UBCc_UBE2S"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 S and related
                     domains; cd23804"
                     /db_xref="CDD:467424"
     Region          159..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B5DFI8.1)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q16763; propagated from
                     UniProtKB/Swiss-Prot (B5DFI8.1)"
     CDS             1..223
                     /gene="Ube2s"
                     /gene_synonym="RGD1564746"
                     /coded_by="NM_001106224.2:133..804"
                     /db_xref="GeneID:292588"
                     /db_xref="RGD:1564746"
ORIGIN      
        1 mnsnvenlpp hiirlvykev ttltadppdg ikvfpneedl tdlqvtiegp egtpyagglf
       61 rmklllgkdf pasppkgyfl tkifhpnvgp ngeicvnvlk rdwtaelgir hvlltikcll
      121 ihpnpesaln eeagrlllen yeeyaararl lteihggacs tssgraeasr dlasgasass
      181 tdpmtpgvlg gaegpmakkh agerdkklaa kkkldkkral rrl
//
LOCUS       NP_062178                154 aa            linear   ROD 28-APR-2025
DEFINITION  fibroblast growth factor 2 [Rattus norvegicus].
ACCESSION   NP_062178
VERSION     NP_062178.1
DBSOURCE    REFSEQ: accession NM_019305.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Zhou,C., Sun,J., Wu,L., Liu,C., Cheng,Q., Xie,S. and Zhang,J.
  TITLE     LTBP2 down-regulated FGF2 to repress vascular smooth muscle cell
            proliferation and vascular remodeling in a rat model of
            intracranial aneurysm
  JOURNAL   Neurosci Lett 842, 137988 (2024)
   PUBMED   39288883
  REMARK    GeneRIF: LTBP2 down-regulated FGF2 to repress vascular smooth
            muscle cell proliferation and vascular remodeling in a rat model of
            intracranial aneurysm.
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Li,Z., Liu,Y., Li,X., Yang,S., Feng,S., Li,G., Jin,F. and Nie,S.
  TITLE     Knockdown the moyamoya disease susceptibility gene, RNF213,
            upregulates the expression of basic fibroblast growth factor and
            matrix metalloproteinase-9 in bone marrow derived mesenchymal stem
            cells
  JOURNAL   Neurosurg Rev 47 (1), 246 (2024)
   PUBMED   38811382
  REMARK    GeneRIF: Knockdown the moyamoya disease susceptibility gene,
            RNF213, upregulates the expression of basic fibroblast growth
            factor and matrix metalloproteinase-9 in bone marrow derived
            mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Uzay,B., Bahadir-Varol,A., Hokelekli,F.O., Yilmaz,M., Esen,E.C.,
            Basar,K., Ayhan,Y., Dalkara,T. and Eren-Kocak,E.
  TITLE     FGF2 gene's antisense protein, NUDT6, plays a depressogenic role by
            promoting inflammation and suppressing neurogenesis without
            altering FGF2 signalling
  JOURNAL   J Physiol 602 (7), 1427-1442 (2024)
   PUBMED   38468384
  REMARK    GeneRIF: FGF2 gene's antisense protein, NUDT6, plays a
            depressogenic role by promoting inflammation and suppressing
            neurogenesis without altering FGF2 signalling.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Xie,X., Zhang,X., Li,S. and Du,W.
  TITLE     Involvement of Fgf2-mediated tau protein phosphorylation in
            cognitive deficits induced by sevoflurane in aged rats
  JOURNAL   Mol Med 30 (1), 39 (2024)
   PUBMED   38493090
  REMARK    GeneRIF: Involvement of Fgf2-mediated tau protein phosphorylation
            in cognitive deficits induced by sevoflurane in aged rats.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Grinchii,D., Levin-Greenwald,M., Lezmy,N., Gordon,T., Paliokha,R.,
            Khoury,T., Racicky,M., Herburg,L., Grothe,C., Dremencov,E. and
            Barak,S.
  TITLE     FGF2 activity regulates operant alcohol self-administration and
            mesolimbic dopamine transmission
  JOURNAL   Drug Alcohol Depend 248, 109920 (2023)
   PUBMED   37224676
  REMARK    GeneRIF: FGF2 activity regulates operant alcohol
            self-administration and mesolimbic dopamine transmission.
REFERENCE   6  (residues 1 to 154)
  AUTHORS   el-Husseini,A.E., Paterson,J.A., Myal,Y. and Shiu,R.P.
  TITLE     PCR detection of the rat brain basic fibroblast growth factor
            (bFGF) mRNA containing a unique 3' untranslated region
  JOURNAL   Biochim Biophys Acta 1131 (3), 314-316 (1992)
   PUBMED   1378302
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Venesio,T., Taverna,D., Hynes,N.E., Deed,R., MacAllan,D.,
            Ciardiello,F., Valverius,E.M., Salomon,D.S., Callahan,R. and
            Merlo,G.
  TITLE     The int-2 gene product acts as a growth factor and substitutes for
            basic fibroblast growth factor in promoting the differentiation of
            a normal mouse mammary epithelial cell line
  JOURNAL   Cell Growth Differ 3 (1), 63-71 (1992)
   PUBMED   1376141
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Fujimoto,K., Ichimori,Y., Kakizoe,T., Okajima,E., Sakamoto,H.,
            Sugimura,T. and Terada,M.
  TITLE     Increased serum levels of basic fibroblast growth factor in
            patients with renal cell carcinoma
  JOURNAL   Biochem Biophys Res Commun 180 (1), 386-392 (1991)
   PUBMED   1718278
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Mansukhani,A., Moscatelli,D., Talarico,D., Levytska,V. and
            Basilico,C.
  TITLE     A murine fibroblast growth factor (FGF) receptor expressed in CHO
            cells is activated by basic FGF and Kaposi FGF
  JOURNAL   Proc Natl Acad Sci U S A 87 (11), 4378-4382 (1990)
   PUBMED   2161540
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Shimasaki,S., Emoto,N., Koba,A., Mercado,M., Shibata,F.,
            Cooksey,K., Baird,A. and Ling,N.
  TITLE     Complementary DNA cloning and sequencing of rat ovarian basic
            fibroblast growth factor and tissue distribution study of its mRNA
  JOURNAL   Biochem Biophys Res Commun 157 (1), 256-263 (1988)
   PUBMED   3196337
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M22427.1 and JAXUCZ010000002.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M22427.1, SRR26643294.8636.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q25"
     Protein         1..154
                     /product="fibroblast growth factor 2"
                     /note="heparin-binding growth factor 2; HBGF-2; basic
                     fibroblast growth factor; angiogenesis promoting growth
                     factor; heparin binding growth factor; fibroblast growth
                     factor 2a"
                     /calculated_mol_wt=17008
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13109.1)"
     mat_peptide     10..154
                     /product="Fibroblast growth factor 2. /id=PRO_0000008939"
                     /note="propagated from UniProtKB/Swiss-Prot (P13109.1)"
                     /calculated_mol_wt=16307
     Region          27..151
                     /region_name="beta-trefoil_FGF2"
                     /note="FGF domain, beta-trefoil fold, found in fibroblast
                     growth factor 2 (FGF2) and similar proteins; cd23314"
                     /db_xref="CDD:467000"
     Site            order(35,127..128,133,142..144)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:467000"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by TEC.
                     /evidence=ECO:0000250|UniProtKB:P09038; propagated from
                     UniProtKB/Swiss-Prot (P13109.1)"
     Region          127..143
                     /region_name="Heparin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P13109.1)"
     Site            127
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P09038; propagated from
                     UniProtKB/Swiss-Prot (P13109.1)"
     Site            128
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P09038; propagated from
                     UniProtKB/Swiss-Prot (P13109.1)"
     Site            133
                     /site_type="other"
                     /note="Important for interaction with integrin.
                     /evidence=ECO:0000250|UniProtKB:P09038; propagated from
                     UniProtKB/Swiss-Prot (P13109.1)"
     CDS             1..154
                     /gene="Fgf2"
                     /gene_synonym="bFGF; Fgf-2; Fgf2a"
                     /coded_by="NM_019305.2:533..997"
                     /db_xref="GeneID:54250"
                     /db_xref="RGD:2609"
ORIGIN      
        1 maagsitslp alpedgggaf ppghfkdpkr lycknggffl rihpdgrvdg vreksdphvk
       61 lqlqaeergv vsikgvcanr ylamkedgrl laskcvteec ffferlesnn yntyrsrkys
      121 swyvalkrtg qyklgsktgp gqkailflpm saks
//
LOCUS       NP_113951                410 aa            linear   ROD 28-APR-2025
DEFINITION  platelet-activating factor acetylhydrolase IB subunit alpha [Rattus
            norvegicus].
ACCESSION   NP_113951 XP_346402
VERSION     NP_113951.1
DBSOURCE    REFSEQ: accession NM_031763.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Gutierrez,P.A., Ackermann,B.E., Vershinin,M. and McKenney,R.J.
  TITLE     Differential effects of the dynein-regulatory factor
            Lissencephaly-1 on processive dynein-dynactin motility
  JOURNAL   J Biol Chem 292 (29), 12245-12255 (2017)
   PUBMED   28576829
  REMARK    GeneRIF: Data suggest that binding of Lis1 to DDB complex does not
            strongly disrupt processive motility along microtubules; motile DDB
            complex binds up to two Lis1 dimers; mutational analysis suggested
            that Lis1 binds directly to the dynein motor domains during DDB
            complex movement. (Lis1 = lissencephaly 1 protein; DDB complex =
            dynein-dynactin-BicD2 complex; BicD2 = bicaudal D homolog 2
            protein)
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Villarin,J.M., McCurdy,E.P., Martinez,J.C. and Hengst,U.
  TITLE     Local synthesis of dynein cofactors matches retrograde transport to
            acutely changing demands
  JOURNAL   Nat Commun 7, 13865 (2016)
   PUBMED   28000671
  REMARK    GeneRIF: Data show that axonal synthesis of Lis1 and p150Glued is
            required for the adjustment of retrograde transport to acutely
            changing neurotrophin signalling in the periphery of neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Shao,C.Y., Zhu,J., Xie,Y.J., Wang,Z., Wang,Y.N., Wang,Y., Su,L.D.,
            Zhou,L., Zhou,T.H. and Shen,Y.
  TITLE     Distinct functions of nuclear distribution proteins LIS1, Ndel1 and
            NudCL in regulating axonal mitochondrial transport
  JOURNAL   Traffic 14 (7), 785-797 (2013)
   PUBMED   23551859
  REMARK    GeneRIF: LIS1 interacts with KIF5b and regulates mitochondrial
            axonal transport in both anterograde and retrograde directions.
            Erratum:[Traffic. 2013 Oct;14(10):1105-8]
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Sipe,C.W., Liu,L., Lee,J., Grimsley-Myers,C. and Lu,X.
  TITLE     Lis1 mediates planar polarity of auditory hair cells through
            regulation of microtubule organization
  JOURNAL   Development 140 (8), 1785-1795 (2013)
   PUBMED   23533177
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Sudarov,A., Gooden,F., Tseng,D., Gan,W.B. and Ross,M.E.
  TITLE     Lis1 controls dynamics of neuronal filopodia and spines to impact
            synaptogenesis and social behaviour
  JOURNAL   EMBO Mol Med 5 (4), 591-607 (2013)
   PUBMED   23483716
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Manya,H., Aoki,J., Watanabe,M., Adachi,T., Asou,H., Inoue,Y.,
            Arai,H. and Inoue,K.
  TITLE     Switching of platelet-activating factor acetylhydrolase catalytic
            subunits in developing rat brain
  JOURNAL   J Biol Chem 273 (29), 18567-18572 (1998)
   PUBMED   9660828
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Morris,S.M., Albrecht,U., Reiner,O., Eichele,G. and Yu-Lee,L.Y.
  TITLE     The lissencephaly gene product Lis1, a protein involved in neuronal
            migration, interacts with a nuclear movement protein, NudC
  JOURNAL   Curr Biol 8 (10), 603-606 (1998)
   PUBMED   9601647
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Watanabe,M., Aoki,J., Manya,H., Arai,H. and Inoue,K.
  TITLE     Molecular cloning of cDNAs encoding alpha1, alpha2, and beta
            subunits of rat brain platelet-activating factor acetylhydrolase
  JOURNAL   Biochim Biophys Acta 1401 (1), 73-79 (1998)
   PUBMED   9459487
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Lo Nigro,C., Chong,C.S., Smith,A.C., Dobyns,W.B., Carrozzo,R. and
            Ledbetter,D.H.
  TITLE     Point mutations and an intragenic deletion in LIS1, the
            lissencephaly causative gene in isolated lissencephaly sequence and
            Miller-Dieker syndrome
  JOURNAL   Hum Mol Genet 6 (2), 157-164 (1997)
   PUBMED   9063735
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Guarda,P.G. and Vitale,M.
  TITLE     [A rare case of ileo-ileal intussusception secondary to
            adenocarcinoma of the small intestine in a 21-year-old adult]
  JOURNAL   Minerva Chir 46 (18), 985-987 (1991)
   PUBMED   1754098
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072510.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346402.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072510.1, AF016049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..410
                     /product="platelet-activating factor acetylhydrolase IB
                     subunit alpha"
                     /EC_number="3.1.1.47"
                     /note="PAF-AH beta; LIS-1; platelet-activating factor
                     acetylhydrolase beta subunit (PAF-AH beta); PAFAH alpha;
                     PAF-AH alpha; PAF-AH 45 kDa subunit; lissencephaly-1
                     protein; PAF acetylhydrolase 45 kDa subunit"
                     /calculated_mol_wt=46539
     Region          1..102
                     /region_name="Interaction with NDEL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     Region          1..66
                     /region_name="Interaction with NDE1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     Region          1..38
                     /region_name="Required for self-association and
                     interaction with PAFAH1B2 and PAFAH1B3.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     Region          10..34
                     /region_name="LisH"
                     /note="pfam08513"
                     /db_xref="CDD:462501"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P43034; propagated from
                     UniProtKB/Swiss-Prot (P63004.2)"
     Region          83..410
                     /region_name="Interaction with dynein and dynactin.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     Region          104..408
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(107,125,129,135..136,148..149,167,171,177..178,
                     190..191,208,213,219..220,233,250,255,261..262,274..275,
                     313,317,323..324,336..337,354,359,365..366,378..379,397,
                     401,407..408)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P43034; propagated from
                     UniProtKB/Swiss-Prot (P63004.2)"
     Region          111..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          154..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..231
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          238..273
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          279..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          341..377
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          367..409
                     /region_name="Interaction with DCX.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     Region          383..407
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          388..410
                     /region_name="Interaction with NDEL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P63004.2)"
     CDS             1..410
                     /gene="Pafah1b1"
                     /gene_synonym="LIS1"
                     /coded_by="NM_031763.3:498..1730"
                     /db_xref="GeneID:83572"
                     /db_xref="RGD:620331"
ORIGIN      
        1 mvlsqrqrde lnraiadylr sngyeeaysv fkkeaeldmn eeldkkyagl lekkwtsvir
       61 lqkkvmeles klneakeeft sggplgqkrd pkewiprppe kyalsghrsp vtrvifhpvf
      121 svmvsaseda tikvwdyetg dfertlkght dsvqdisfdh sgkllascsa dmtiklwdfq
      181 gfecirtmhg hdhnvssvai mpngdhivsa srdktikmwe vqtgycvktf tghrewvrmv
      241 rpnqdgtlia scsndqtvrv wvvatkecka elrehehvve ciswapessy ssiseatgse
      301 tkksgkpgpf llsgsrdkti kmwdvstgmc lmtlvghdnw vrgvlfhsgg kfilscaddk
      361 tlrvwdyknk rcmktlnahe hfvtsldfhk tapyvvtgsv dqtvkvwecr
//
LOCUS       NP_783169               1222 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein kinase WNK4 [Rattus norvegicus].
ACCESSION   NP_783169
VERSION     NP_783169.2
DBSOURCE    REFSEQ: accession NM_175579.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1222)
  AUTHORS   Bhuiyan,M.I.H., Song,S., Yuan,H., Begum,G., Kofler,J., Kahle,K.T.,
            Yang,S.S., Lin,S.H., Alper,S.L., Subramanya,A.R. and Sun,D.
  TITLE     WNK-Cab39-NKCC1 signaling increases the susceptibility to ischemic
            brain damage in hypertensive rats
  JOURNAL   J Cereb Blood Flow Metab 37 (8), 2780-2794 (2017)
   PUBMED   27798271
REFERENCE   2  (residues 1 to 1222)
  AUTHORS   Vorontsova,I., Lam,L., Delpire,E., Lim,J. and Donaldson,P.
  TITLE     Identification of the WNK-SPAK/OSR1 signaling pathway in rodent and
            human lenses
  JOURNAL   Invest Ophthalmol Vis Sci 56 (1), 310-321 (2014)
   PUBMED   25515571
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1222)
  AUTHORS   Ponce-Coria,J., Markadieu,N., Austin,T.M., Flammang,L., Rios,K.,
            Welling,P.A. and Delpire,E.
  TITLE     A novel Ste20-related proline/alanine-rich kinase
            (SPAK)-independent pathway involving calcium-binding protein 39
            (Cab39) and serine threonine kinase with no lysine member 4 (WNK4)
            in the activation of Na-K-Cl cotransporters
  JOURNAL   J Biol Chem 289 (25), 17680-17688 (2014)
   PUBMED   24811174
  REMARK    GeneRIF: in addition to SPAK and OSR1, WNK4 is able to anchor
            itself to the N-terminal domain of NKCC1 and to promote
            cotransporter activation.
REFERENCE   4  (residues 1 to 1222)
  AUTHORS   Shibata,S., Zhang,J., Puthumana,J., Stone,K.L. and Lifton,R.P.
  TITLE     Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via
            ubiquitination and degradation of WNK4
  JOURNAL   Proc Natl Acad Sci U S A 110 (19), 7838-7843 (2013)
   PUBMED   23576762
REFERENCE   5  (residues 1 to 1222)
  AUTHORS   Wakabayashi,M., Mori,T., Isobe,K., Sohara,E., Susa,K., Araki,Y.,
            Chiga,M., Kikuchi,E., Nomura,N., Mori,Y., Matsuo,H., Murata,T.,
            Nomura,S., Asano,T., Kawaguchi,H., Nonoyama,S., Rai,T., Sasaki,S.
            and Uchida,S.
  TITLE     Impaired KLHL3-mediated ubiquitination of WNK4 causes human
            hypertension
  JOURNAL   Cell Rep 3 (3), 858-868 (2013)
   PUBMED   23453970
REFERENCE   6  (residues 1 to 1222)
  AUTHORS   Kahle,K.T., Wilson,F.H., Leng,Q., Lalioti,M.D., O'Connell,A.D.,
            Dong,K., Rapson,A.K., MacGregor,G.G., Giebisch,G., Hebert,S.C. and
            Lifton,R.P.
  TITLE     WNK4 regulates the balance between renal NaCl reabsorption and K+
            secretion
  JOURNAL   Nat Genet 35 (4), 372-376 (2003)
   PUBMED   14608358
REFERENCE   7  (residues 1 to 1222)
  AUTHORS   Yang,C.L., Angell,J., Mitchell,R. and Ellison,D.H.
  TITLE     WNK kinases regulate thiazide-sensitive Na-Cl cotransport
  JOURNAL   J Clin Invest 111 (7), 1039-1045 (2003)
   PUBMED   12671053
REFERENCE   8  (residues 1 to 1222)
  AUTHORS   Monti,J., Zimdahl,H., Schulz,H., Plehm,R., Ganten,D. and Hubner,N.
  TITLE     The role of Wnk4 in polygenic hypertension: a candidate gene
            analysis on rat chromosome 10
  JOURNAL   Hypertension 41 (4), 938-942 (2003)
   PUBMED   12642508
  REMARK    GeneRIF: Gene analysis of rat chromosome 10 suggest that Wnk4 does
            not have a role in polygenic hypertension.
REFERENCE   9  (residues 1 to 1222)
  AUTHORS   Wilson,F.H., Kahle,K.T., Sabath,E., Lalioti,M.D., Rapson,A.K.,
            Hoover,R.S., Hebert,S.C., Gamba,G. and Lifton,R.P.
  TITLE     Molecular pathogenesis of inherited hypertension with hyperkalemia:
            the Na-Cl cotransporter is inhibited by wild-type but not mutant
            WNK4
  JOURNAL   Proc Natl Acad Sci U S A 100 (2), 680-684 (2003)
   PUBMED   12515852
REFERENCE   10 (residues 1 to 1222)
  AUTHORS   Wilson,F.H., Disse-Nicodeme,S., Choate,K.A., Ishikawa,K.,
            Nelson-Williams,C., Desitter,I., Gunel,M., Milford,D.V.,
            Lipkin,G.W., Achard,J.M., Feely,M.P., Dussol,B., Berland,Y.,
            Unwin,R.J., Mayan,H., Simon,D.B., Farfel,Z., Jeunemaitre,X. and
            Lifton,R.P.
  TITLE     Human hypertension caused by mutations in WNK kinases
  JOURNAL   Science 293 (5532), 1107-1112 (2001)
   PUBMED   11498583
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY192567.1, AY187039.1 and BQ211864.1.
            
            On Oct 1, 2009 this sequence version replaced NP_783169.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY192567.1, AY187039.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1222
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1222
                     /product="serine/threonine-protein kinase WNK4"
                     /EC_number="2.7.11.1"
                     /note="WNK4 Ser/Thr kinase; protein kinase with no lysine
                     4; protein kinase lysine-deficient 4"
                     /calculated_mol_wt=132677
     Region          1..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96J92; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          169..429
                     /region_name="STKc_WNK4"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 4; cd14033"
                     /db_xref="CDD:270935"
     Site            order(177..181,183,185,198,200,231,251..254,258,260,299,
                     301,303..304,306,318,321,335..338)
                     /site_type="active"
                     /db_xref="CDD:270935"
     Site            order(177..181,183,185,198,200,231,251..254,258,299,301,
                     303..304,306,318)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270935"
     Site            order(181,258,260,299,301,303,321,335..338)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270935"
     Site            317..338
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270935"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15883153; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          450..512
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          527..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          554..564
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96J92; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          591..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          626..679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          747..809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          836..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          927..1087
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          996..999
                     /region_name="RFXV motif.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Region          1169..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7TPK6.3)"
     Site            1196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80UE6; propagated from
                     UniProtKB/Swiss-Prot (Q7TPK6.3)"
     CDS             1..1222
                     /gene="Wnk4"
                     /gene_synonym="Ac2-059; Prkwnk4"
                     /coded_by="NM_175579.3:27..3695"
                     /db_xref="GeneID:287715"
                     /db_xref="RGD:631401"
ORIGIN      
        1 mlaprntetg vhmsqteadl alrpspslts mgptrlgppp rrvrrfsgka eprprssrps
       61 rrssvdlgll sswsqpasll peppdppdsa gpmrsppsns kehpegtwtg aapvkaadsa
      121 cpeltvssgg pgsrepprvp daaarerrre qeekedtetq avatspdgry lkfdieigrg
      181 sfktvyrgld tdttvevawc elqarklsra erqrfseeve mlkglqhpni vrfydswksv
      241 lrgqvcivlv telmtsgtlk tylrrfremk prvlqrwsrq ilrglhflhs rvppilhrdl
      301 kcdnvfitgp sgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd eavdvyafgm
      361 cmlematsey pysecqnaaq iyrkvtsgtk pnsfykvkmp evkeiiegci rtdknerfti
      421 qdllthaffr eergvhvela eeddgekpgl klwlrmedar rggrprdnqa ieflfqlgrd
      481 aaeevaqemv alglvceady qpvaravrer vaaiqrkrek lrkarelevl ppdsgpppat
      541 vsmtpgppsa fppepeepea dqhqsflfrh asyssttsdc etdgylsssg fldasdpalq
      601 ppggmpsspa ephlclpsgf alsiprsgpg sdfspgdsya sdaasglsdm geggqmrknp
      661 vktlrrrprs rlrvtsvsdq sdrvvecqlq thnskmvtfr fdldgdspee iaaamvynef
      721 ilpserdgfl srireiiqrv etllkrdagp seatedalsp qeeaaampal pgpsdeelqr
      781 sispeqrswa afstspsspg tplspgtpfs pgtppvfpcp ifpitspsch pypfsqvssn
      841 pcpqapssll psssgasqvp fpspslptss plpfspsypq vplhpaslpt cpsppplpst
      901 taapllslas afslavmtva qsllspspgl lsqsppappg plpsmplpla scdqeslsaq
      961 taeteneasr npaqpllgda rlapiseegk pqlvgrfqvt sskepaeppl qpasptlsrs
     1021 lklptpqlts essdtedsaa ggpetreala esdraaeglg vaideekdeg kepqiggssp
     1081 ilsqpspvwm nysysslcls seesessged eefwaelqnl rqkhlsevea lqtlqkkeie
     1141 dlysrlgkqp ppgivapaam lscrqrrlsk gsfptsrrns lqrsdlpgpg imrknslsgs
     1201 stgsqeqras kgvtfagdvg rm
//
LOCUS       NP_001020073             548 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing protein 56 [Rattus norvegicus].
ACCESSION   NP_001020073 XP_344978
VERSION     NP_001020073.1
DBSOURCE    REFSEQ: accession NM_001024902.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097444.1.
            
            On Jun 17, 2005 this sequence version replaced XP_344978.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097444.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..548
                     /product="leucine-rich repeat-containing protein 56"
                     /calculated_mol_wt=60357
     Region          <92..292
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          94..115
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     Region          95..117
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          117..138
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     Region          118..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          139..160
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     Region          140..161
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          161..182
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     Region          162..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          186..206
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     Region          405..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8C9.1)"
     CDS             1..548
                     /gene="Lrrc56"
                     /gene_synonym="RGD1311654"
                     /coded_by="NM_001024902.1:166..1812"
                     /db_xref="GeneID:365389"
                     /db_xref="RGD:1311654"
ORIGIN      
        1 mdpawdgsqg srpgtasirv relswqglnn pqpqnkrlgs hgdiyrerrv eehlsparlq
       61 alaqvddlql vrvlemcvdt rknslgnfgm hlpnliqlkl nhsclgslrd lgtslgqlqv
      121 lwlarcgltd ldgigsflal kelyvsynni sdlsplclle qlevldlegn nvedlgqmry
      181 lqlcprlttl tlegnlvclk pdpgpsnkap qdynyraevk klipqlhild evpttctnlp
      241 apqklsqdwl mvkeaikegn vldillprle cshgatirkf dptlpvpetq pwalsllvpe
      301 gplpegllse npaaedhasn lthgpgqvlc gnptkglrer rnqyqewapl eqlpphrpdl
      361 airpstlrpd paescdlsmt glrawrepgl rpllqrqlef qqerlthvqa qdpqkapieq
      421 edqtgpktsl tplrlasels rtsgfhlips ppkypmppes gisslgrsad lpfrgrrlrv
      481 lgslgpslge gsvlgerlal ralevssdps hraqgcpdpk pslgpatcpl glhclhhlnp
      541 ippahpfp
//
LOCUS       NP_001013082             278 aa            linear   ROD 28-APR-2025
DEFINITION  F-box only protein 17 [Rattus norvegicus].
ACCESSION   NP_001013082 XP_214880
VERSION     NP_001013082.2
DBSOURCE    REFSEQ: accession NM_001013064.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Glenn,K.A., Nelson,R.F., Wen,H.M., Mallinger,A.J. and Paulson,H.L.
  TITLE     Diversity in tissue expression, substrate binding, and SCF complex
            formation for a lectin family of ubiquitin ligases
  JOURNAL   J Biol Chem 283 (19), 12717-12729 (2008)
   PUBMED   18203720
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079218.1 and BE120593.1.
            
            On Apr 1, 2008 this sequence version replaced NP_001013082.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..278
                     /product="F-box only protein 17"
                     /calculated_mol_wt=31539
     Region          <28..65
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Site            order(28..29,32..33,37,39..40,45..47,49)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438852"
     Region          100..273
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     CDS             1..278
                     /gene="Fbxo17"
                     /gene_synonym="Fbg4; Fbx17; Fbxo26"
                     /coded_by="NM_001013064.2:297..1133"
                     /db_xref="GeneID:292757"
                     /db_xref="RGD:1308308"
ORIGIN      
        1 mgaqpsrrrm teaqhmalae lppelllqvl shvppralvt rcrpvcrawr dlvdgpsvwl
       61 lqlardrsae gralyalaqs cpadrnghdd fplcalarfc llaplgrnli ynscgeqgfr
      121 gwevehggng waveknltmv pgapsqtcfv tsfewcfkrq lvdlvkegvw qelldsaqie
      181 iyiadwwgar encgciyrlr vrlldehene vvkfsaspnp vlqwterscr qvshvftdfg
      241 kgiryvsfeq ygrdtrswvg hygalvthst vrvrirls
//
LOCUS       NP_001012087             692 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF7 [Rattus norvegicus].
ACCESSION   NP_001012087 XP_229946
VERSION     NP_001012087.1
DBSOURCE    REFSEQ: accession NM_001012087.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Zhao,K., Yang,Y., Zhang,G., Wang,C., Wang,D., Wu,M. and Mei,Y.
  TITLE     Regulation of the Mdm2-p53 pathway by the ubiquitin E3 ligase
            MARCH7
  JOURNAL   EMBO Rep 19 (2), 305-319 (2018)
   PUBMED   29295817
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Flach,K., Ramminger,E., Hilbrich,I., Arsalan-Werner,A.,
            Albrecht,F., Herrmann,L., Goedert,M., Arendt,T. and Holzer,M.
  TITLE     Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates
            tau protein in vitro impairing microtubule binding
  JOURNAL   Biochim Biophys Acta 1842 (9), 1527-1538 (2014)
   PUBMED   24905733
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Zhao,B., Ito,K., Iyengar,P.V., Hirose,S. and Nakamura,N.
  TITLE     MARCH7 E3 ubiquitin ligase is highly expressed in developing
            spermatids of rats and its possible involvement in head and tail
            formation
  JOURNAL   Histochem Cell Biol 139 (3), 447-460 (2013)
   PUBMED   23104140
  REMARK    GeneRIF: The results suggest that MARCH7 is involved in
            spermiogenesis by regulating the structural and functional
            integrity of the head and tail of developing spermatids.
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Nathan,J.A., Sengupta,S., Wood,S.A., Admon,A., Markson,G.,
            Sanderson,C. and Lehner,P.J.
  TITLE     The ubiquitin E3 ligase MARCH7 is differentially regulated by the
            deubiquitylating enzymes USP7 and USP9X
  JOURNAL   Traffic 9 (7), 1130-1145 (2008)
   PUBMED   18410486
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Metcalfe,S.M., Muthukumarana,P.A., Thompson,H.L., Haendel,M.A. and
            Lyons,G.E.
  TITLE     Leukaemia inhibitory factor (LIF) is functionally linked to
            axotrophin and both LIF and axotrophin are linked to regulatory
            immune tolerance
  JOURNAL   FEBS Lett 579 (3), 609-614 (2005)
   PUBMED   15670816
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083842.1.
            
            On Feb 11, 2005 this sequence version replaced XP_229946.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMD00132280
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..692
                     /product="E3 ubiquitin-protein ligase MARCHF7"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase MARCH7; MARCH-VII;
                     RING-type E3 ubiquitin transferase MARCHF7;
                     membrane-associated RING-CH protein VII;
                     membrane-associated RING finger protein 7; RING-type E3
                     ubiquitin transferase MARCH7; axotrophin;
                     membrane-associated ring finger (C3HC4) 7, E3 ubiquitin
                     protein ligase"
                     /calculated_mol_wt=76221
     Region          1..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          201..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          296..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          360..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          440..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          512..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          550..611
                     /region_name="RING_CH-C4HC3_MARCH7"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH7 (MARCH7); cd16812"
                     /db_xref="CDD:438461"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     CDS             1..692
                     /gene="Marchf7"
                     /gene_synonym="Axot; March7"
                     /coded_by="NM_001012087.1:190..2268"
                     /db_xref="GeneID:311059"
                     /db_xref="RGD:1308993"
ORIGIN      
        1 meskpsripr risvqpsgsl sarmvsgnrg tslndsyhsr dssfrldsey qsasasasas
       61 pyqstwyses eitqgarsrs qnqqrdhdsk rpklsctnct stsagrnigs glntlsdssw
      121 rpgqvprsss mvlgsfgtdl mrerrdlerr rdssisslmd yshrsgdfta payvqervps
      181 sysqgarpke naantlqlns stnhqlpseh qtvpssrdss rssfrshfsp rqsesfrnss
      241 hpafsylssr netptissse ragssqrpfq essdnegrrt trrllsrias smsstffsrr
      301 ssqdslntrs lssenyispr tltsqsrnng asssevndgr aseasqgfrf lrrrwglssl
      361 sqnhssepda enfnqesegr ntgpwlsssl rnrctplfsr rrregrdess rispsdvppr
      421 shlfrresne vvhleaqgds lgaaasrpqa sgasgnasas gstpdlpqgg rntgiagilp
      481 gslfrfavpp algsnltdnv titvdiipsg wssadgksek aksapsrdpe klqkikesll
      541 ledsdeeeeg dlcricqmaa asssnlliep ckctgslqyv hqecmkkwlq akinsgssle
      601 avttcelcke klqlnledfd ihelhrahan eqaeyefiss glylvvllhl ceqsfsdmmg
      661 ntiepstrvr finlartlqa hmedletsed ef
//
LOCUS       NP_113992                257 aa            linear   ROD 28-APR-2025
DEFINITION  cytokine-inducible SH2-containing protein [Rattus norvegicus].
ACCESSION   NP_113992 XP_001074104 XP_343473
VERSION     NP_113992.1
DBSOURCE    REFSEQ: accession NM_031804.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Anderson,S.T., Barclay,J.L., Fanning,K.J., Kusters,D.H.,
            Waters,M.J. and Curlewis,J.D.
  TITLE     Mechanisms underlying the diminished sensitivity to prolactin
            negative feedback during lactation: reduced STAT5 signaling and
            up-regulation of cytokine-inducible SH2 domain-containing protein
            (CIS) expression in tuberoinfundibular dopaminergic neurons
  JOURNAL   Endocrinology 147 (3), 1195-1202 (2006)
   PUBMED   16357045
  REMARK    GeneRIF: during lactation, STAT5 signaling is reduced and CIS is
            upregulated in tuberoinfundibular dopaminergic neurons
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Landsman,T. and Waxman,D.J.
  TITLE     Role of the cytokine-induced SH2 domain-containing protein CIS in
            growth hormone receptor internalization
  JOURNAL   J Biol Chem 280 (45), 37471-37480 (2005)
   PUBMED   16154995
  REMARK    GeneRIF: The growth hormone(GH)-responsive rat liver cell line
            CWSV-1 was used to investigate the role of CIS and the proteasome
            in GH-induced GHR internalization.
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Ji,K.A., Yang,M.S., Jou,I., Shong,M.H. and Joe,E.H.
  TITLE     Thrombin induces expression of cytokine-induced SH2 protein (CIS)
            in rat brain astrocytes: involvement of phospholipase A2,
            cyclooxygenase, and lipoxygenase
  JOURNAL   Glia 48 (2), 102-111 (2004)
   PUBMED   15378659
  REMARK    GeneRIF: Thrombin-stimulation of reactive oxygen species,
            prostaglandin and leukotriene production in astrocytes results in
            cytokine-induced SH2 protein [CIS] expression which may be a
            feedback mechanism preventing prolonged inflammatory responses
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Kasagi,Y., Tokita,R., Nakata,T., Imaki,T. and Minami,S.
  TITLE     Human growth hormone induces SOCS3 and CIS mRNA increase in the
            hypothalamic neurons of hypophysectomized rats
  JOURNAL   Endocr J 51 (2), 145-154 (2004)
   PUBMED   15118263
  REMARK    GeneRIF: HGH acts directly on the neurons in the hypothalamus, and
            increases SOCS3 and CIS mRNAs, suggesting that these negative
            regulators may be involved in the mechanism that turns off the hGH
            action in the hypothalamic neurons.
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Chen,S., Anderson,P.O., Li,L., Sjogren,H.O., Wang,P. and Li,S.L.
  TITLE     Functional association of cytokine-induced SH2 protein and protein
            kinase C in activated T cells
  JOURNAL   Int Immunol 15 (3), 403-409 (2003)
   PUBMED   12618484
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Morales,O., Faulds,M.H., Lindgren,U.J. and Haldosen,L.A.
  TITLE     1Alpha,25-dihydroxyvitamin D3 inhibits GH-induced expression of
            SOCS-3 and CIS and prolongs growth hormone signaling via the Janus
            kinase (JAK2)/signal transducers and activators of transcription
            (STAT5) system in osteoblast-like cells
  JOURNAL   J Biol Chem 277 (38), 34879-34884 (2002)
   PUBMED   12107179
  REMARK    GeneRIF: inhibition of GH-induced expression in osteoblast-like
            cells
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Mao,Y., Ling,P.R., Fitzgibbons,T.P., McCowen,K.C., Frick,G.P.,
            Bistrian,B.R. and Smith,R.J.
  TITLE     Endotoxin-induced inhibition of growth hormone receptor signaling
            in rat liver in vivo
  JOURNAL   Endocrinology 140 (12), 5505-5515 (1999)
   PUBMED   10579313
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC161930.1.
            
            On or before Sep 7, 2008 this sequence version replaced
            XP_001074104.1, XP_343473.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161930.1, AF065161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132275, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..257
                     /product="cytokine-inducible SH2-containing protein"
                     /note="SOCS; CIS-1; suppressor of cytokine signaling;
                     cytokine inducible SH2-containing protein 1"
                     /calculated_mol_wt=28409
     Region          77..164
                     /region_name="SH2_CIS"
                     /note="Src homology 2 (SH2) domain found in
                     cytokine-inducible SH2-containing protein (CIS); cd10718"
                     /db_xref="CDD:198285"
     Site            order(89,107,109,117,130)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198285"
     Site            order(140,142,163)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198285"
     Region          217..257
                     /region_name="SOCS_CIS1"
                     /note="SOCS (suppressors of cytokine signaling) box of CIS
                     (cytokine-inducible SH2 protein) 1-like proteins. Together
                     with the SOCS proteins, the CIS/SOCS family of proteins is
                     characterized by the presence of a C-terminal SOCS box and
                     a central SH2 domain; cd03734"
                     /db_xref="CDD:239703"
     Site            order(218..223,229,234,240,245)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239703"
     CDS             1..257
                     /gene="Cish"
                     /gene_synonym="Cis"
                     /coded_by="NM_031804.1:116..889"
                     /db_xref="GeneID:83681"
                     /db_xref="RGD:69261"
ORIGIN      
        1 mvlcvqgscp llvveqigqr plwaqslelp gpamqplptg afpeevteet pvqsenepkv
       61 ldpegdllci aktfsylres gwywgsitas earqhlqkmp egtflvrdst hpsylftlsv
      121 kttrgptnvr ieyadssfrl dsnclsrpri lafpdvvslv qhyvasctad trsdspdpap
      181 tpalpvpkpd apgdpvlpip vatavhlklv qpfvrrssar slqhlcrlvi nrlvtdvdcl
      241 plprrmadyl rqypfql
//
LOCUS       NP_001034120             578 aa            linear   ROD 28-APR-2025
DEFINITION  triokinase/FMN cyclase [Rattus norvegicus].
ACCESSION   NP_001034120
VERSION     NP_001034120.1
DBSOURCE    REFSEQ: accession NM_001039031.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Rodrigues,J.R., Couto,A., Cabezas,A., Pinto,R.M., Ribeiro,J.M.,
            Canales,J., Costas,M.J. and Cameselle,J.C.
  TITLE     Bifunctional homodimeric triokinase/FMN cyclase: contribution of
            protein domains to the activities of the human enzyme and molecular
            dynamics simulation of domain movements
  JOURNAL   J Biol Chem 289 (15), 10620-10636 (2014)
   PUBMED   24569995
REFERENCE   2  (residues 1 to 578)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Diao,F., Li,S., Tian,Y., Zhang,M., Xu,L.G., Zhang,Y., Wang,R.P.,
            Chen,D., Zhai,Z., Zhong,B., Tien,P. and Shu,H.B.
  TITLE     Negative regulation of MDA5- but not RIG-I-mediated innate
            antiviral signaling by the dihydroxyacetone kinase
  JOURNAL   Proc Natl Acad Sci U S A 104 (28), 11706-11711 (2007)
   PUBMED   17600090
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Cabezas,A., Costas,M.J., Pinto,R.M., Couto,A. and Cameselle,J.C.
  TITLE     Identification of human and rat FAD-AMP lyase (cyclic FMN forming)
            as ATP-dependent dihydroxyacetone kinases
  JOURNAL   Biochem Biophys Res Commun 338 (4), 1682-1689 (2005)
   PUBMED   16289032
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Hagopian,K., Ramsey,J.J. and Weindruch,R.
  TITLE     Fructose metabolizing enzymes from mouse liver: influence of age
            and caloric restriction
  JOURNAL   Biochim Biophys Acta 1721 (1-3), 37-43 (2005)
   PUBMED   15652177
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Massillon,D., Stalmans,W., van de Werve,G. and Bollen,M.
  TITLE     Identification of the glycogenic compound 5-iodotubercidin as a
            general protein kinase inhibitor
  JOURNAL   Biochem J 299 (Pt 1) (Pt 1), 123-128 (1994)
   PUBMED   8166629
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Beutler,E. and Guinto,E.
  TITLE     Dihydroxyacetone metabolism by human erythrocytes: demonstration of
            triokinase activity and its characterization
  JOURNAL   Blood 41 (4), 559-568 (1973)
   PUBMED   4688871
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098925.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..578
                     /product="triokinase/FMN cyclase"
                     /EC_number="2.7.1.29"
                     /EC_number="4.6.1.15"
                     /EC_number="2.7.1.28"
                     /note="bifunctional ATP-dependent dihydroxyacetone
                     kinase/FAD-AMP lyase (cyclizing); dihydroxyacetone kinase
                     2 homolog"
                     /calculated_mol_wt=59313
     Region          4..570
                     /region_name="PRK14479"
                     /note="dihydroxyacetone kinase; Provisional; cl29418"
                     /db_xref="CDD:475197"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KLZ6.1)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KLZ6.1)"
     CDS             1..578
                     /gene="Tkfc"
                     /gene_synonym="Dak; RGD1311026"
                     /coded_by="NM_001039031.1:280..2016"
                     /db_xref="GeneID:361730"
                     /db_xref="RGD:1311026"
ORIGIN      
        1 msskkmvnsv egcagdalag fvacnpdlql lqgyrvalrs dldslkgrva llsgggsghe
       61 pahagfigkg mltgviagav faspavgsil aairavaqag tagtllivkn ytgdrlnfgl
      121 ameqakaegi svemvviedd saftvlkkag rrglcgtili hkvagalaee gmgleeitkk
      181 vsviakaigt lgvslspcsv pgtkptfela ademelglgi hgeagvrrik lvpvdqivtl
      241 mldhmtdtsn ishvpvksgs svvlmvnnlg glsflelgii adaairlleg rgvkvaralv
      301 gtfmsalemr gvsltlmlvd epllklidae tnakawphms kvsvtgrnri raaptepaea
      361 peataaggva skqmtlvldr isttliglee hlnaldraag dgdcgsthsr aakaiqgwlk
      421 egptpaspaq vlsklsvlll ekmggssgal yglfltaaaq plkantdlpa wsaamdaglk
      481 amqkygkaap gdrtmldslw aaaqelqawk spgasllpvl tkavksaeaa aeatknmeag
      541 agrasyissa qldqpdpgav aaaaifrail evlqtkaa
//
LOCUS       NP_001014221             425 aa            linear   ROD 28-APR-2025
DEFINITION  V-type proton ATPase subunit C 2 [Rattus norvegicus].
ACCESSION   NP_001014221 XP_343130
VERSION     NP_001014221.1
DBSOURCE    REFSEQ: accession NM_001014199.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Rahman,S., Ishizuka-Katsura,Y., Arai,S., Saijo,S., Yamato,I.,
            Toyama,M., Ohsawa,N., Inoue,M., Honda,K., Terada,T., Shirouzu,M.,
            Yokoyama,S., Iwata,S. and Murata,T.
  TITLE     Expression, purification and characterization of isoforms of
            peripheral stalk subunits of human V-ATPase
  JOURNAL   Protein Expr Purif 78 (2), 181-188 (2011)
   PUBMED   21356312
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Cruciat,C.M., Ohkawara,B., Acebron,S.P., Karaulanov,E.,
            Reinhard,C., Ingelfinger,D., Boutros,M. and Niehrs,C.
  TITLE     Requirement of prorenin receptor and vacuolar H+-ATPase-mediated
            acidification for Wnt signaling
  JOURNAL   Science 327 (5964), 459-463 (2010)
   PUBMED   20093472
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Feng,N.H., Lin,H.I., Wang,J.S., Chou,S.T., Ma,H.K., Rooney,S.A. and
            Lu,J.F.
  TITLE     Differential expression of a V-type ATPase C subunit gene,
            Atp6v1c2, during culture of rat lung type II pneumocytes
  JOURNAL   J Biomed Sci 12 (6), 899-911 (2005)
   PUBMED   16283434
  REMARK    GeneRIF: analysis of V-type ATPase C subunit gene, Atp6v1c2, during
            culture of rat lung type II pneumocytes
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Sun-Wada,G.H., Murata,Y., Namba,M., Yamamoto,A., Wada,Y. and
            Futai,M.
  TITLE     Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b)
            specifically expressed in kidney and lung
  JOURNAL   J Biol Chem 278 (45), 44843-44851 (2003)
   PUBMED   12947086
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Sun-Wada,G.H., Yoshimizu,T., Imai-Senga,Y., Wada,Y. and Futai,M.
  TITLE     Diversity of mouse proton-translocating ATPase: presence of
            multiple isoforms of the C, d and G subunits
  JOURNAL   Gene 302 (1-2), 147-153 (2003)
   PUBMED   12527205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079083.1.
            
            On Apr 20, 2005 this sequence version replaced XP_343130.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079083.1, AY594319.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q16"
     Protein         1..425
                     /product="V-type proton ATPase subunit C 2"
                     /EC_number="7.1.2.2"
                     /note="V-ATPase subunit C 2; vacuolar proton pump subunit
                     C 2; vacuolar H+ ATPase C2; ATPase, H+ transporting, V1
                     subunit C; ATPase, H+ transporting, lysosomal V1 subunit
                     C2"
                     /calculated_mol_wt=48112
     Region          4..415
                     /region_name="V-ATPase_C"
                     /note="V-ATPase subunit C; pfam03223"
                     /db_xref="CDD:460851"
     Region          55..75
                     /region_name="3-helical coiled coil"
                     /note="3-helical coiled coil [structural motif]"
                     /db_xref="CDD:270211"
     Region          120..146
                     /region_name="3-helical coiled coil"
                     /note="3-helical coiled coil [structural motif]"
                     /db_xref="CDD:270211"
     Region          274..349
                     /region_name="3-helical coiled coil"
                     /note="3-helical coiled coil [structural motif]"
                     /db_xref="CDD:270211"
     Region          295..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYE4.1)"
     CDS             1..425
                     /gene="Atp6v1c2"
                     /coded_by="NM_001014199.1:132..1409"
                     /db_xref="GeneID:362802"
                     /db_xref="RGD:1359430"
ORIGIN      
        1 msefwlisap gdkenlqale rmnsvtsksn lshntkfaip dfkvgtldsl vglsdelgkl
       61 dtfaeslikr maqsvvevme dskgkvhenl langvdltsf vthfewdmak ypakqplvsv
      121 vdtlakqlaq ietdlksrta aysvlkanle nlekkstgnl ftrtlsdivs kedfvldsey
      181 litllvivpk ssyvqwqkty eslsdmvvpr stkliaedne gglftvtlfr kviedfkvka
      241 kenkfivref yydekeikre reemtrllsd kkqqyqtscv alkkgsatyr dhkvkvtplg
      301 nptrptagqn dresegegeg pllrwlkvnf seafiawihi kalrvfvesv lryglpvnfq
      361 avllqphkks atkrlrevln svfrhldeva aasildasve ipglqlsnqd yfpyvyfhid
      421 lslld
//
LOCUS       NP_036895                796 aa            linear   ROD 28-APR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase alpha precursor [Rattus
            norvegicus].
ACCESSION   NP_036895
VERSION     NP_036895.2
DBSOURCE    REFSEQ: accession NM_012763.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Ghai,R., Bugarcic,A., Liu,H., Norwood,S.J., Skeldal,S.,
            Coulson,E.J., Li,S.S., Teasdale,R.D. and Collins,B.M.
  TITLE     Structural basis for endosomal trafficking of diverse transmembrane
            cargos by PX-FERM proteins
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), E643-E652 (2013)
   PUBMED   23382219
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Wang,P.S., Wang,J., Xiao,Z.C. and Pallen,C.J.
  TITLE     Protein-tyrosine phosphatase alpha acts as an upstream regulator of
            Fyn signaling to promote oligodendrocyte differentiation and
            myelination
  JOURNAL   J Biol Chem 284 (48), 33692-33702 (2009)
   PUBMED   19812040
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Huang,J., Huang,A., Zhang,Q., Lin,Y.C. and Yu,H.G.
  TITLE     Novel mechanism for suppression of hyperpolarization-activated
            cyclic nucleotide-gated pacemaker channels by receptor-like
            tyrosine phosphatase-alpha
  JOURNAL   J Biol Chem 283 (44), 29912-29919 (2008)
   PUBMED   18768480
  REMARK    GeneRIF: RPTPalpha plays a critical role in HCN channel function
            via tyrosine dephosphorylation
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Lin,D., Kamsteeg,E.J., Zhang,Y., Jin,Y., Sterling,H., Yue,P.,
            Roos,M., Duffield,A., Spencer,J., Caplan,M. and Wang,W.H.
  TITLE     Expression of tetraspan protein CD63 activates protein-tyrosine
            kinase (PTK) and enhances the PTK-induced inhibition of ROMK
            channels
  JOURNAL   J Biol Chem 283 (12), 7674-7681 (2008)
   PUBMED   18211905
  REMARK    GeneRIF: CD63 plays a role in the regulation of ROMK channels
            through its association with RPTPalpha, which in turn interacts
            with and activates Src family PTK, thus reducing ROMK activity.
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Lei,G., Xue,S., Chery,N., Liu,Q., Xu,J., Kwan,C.L., Fu,Y.P.,
            Lu,Y.M., Liu,M., Harder,K.W. and Yu,X.M.
  TITLE     Gain control of N-methyl-D-aspartate receptor activity by
            receptor-like protein tyrosine phosphatase alpha
  JOURNAL   EMBO J 21 (12), 2977-2989 (2002)
   PUBMED   12065411
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Calera,M.R., Vallega,G. and Pilch,P.F.
  TITLE     Dynamics of protein-tyrosine phosphatases in rat adipocytes
  JOURNAL   J Biol Chem 275 (9), 6308-6312 (2000)
   PUBMED   10692429
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Helmke,S., Lohse,K., Mikule,K., Wood,M.R. and Pfenninger,K.H.
  TITLE     SRC binding to the cytoskeleton, triggered by growth cone
            attachment to laminin, is protein tyrosine phosphatase-dependent
  JOURNAL   J Cell Sci 111 (Pt 16), 2465-2475 (1998)
   PUBMED   9683640
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Su,J., Batzer,A. and Sap,J.
  TITLE     Receptor tyrosine phosphatase R-PTP-alpha is
            tyrosine-phosphorylated and associated with the adaptor protein
            Grb2
  JOURNAL   J Biol Chem 269 (29), 18731-18734 (1994)
   PUBMED   7518443
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Moriyama,T., Fujiwara,Y., Imai,E., Takenaka,M., Kawanishi,S.,
            Inoue,T., Noguchi,T., Tanaka,T., Kamada,T. and Ueda,N.
  TITLE     cDNA cloning of rat LRP, a receptor like protein tyrosine
            phosphatase, and evidence for its gene regulation in cultured rat
            mesangial cells
  JOURNAL   Biochem Biophys Res Commun 188 (1), 34-39 (1992)
   PUBMED   1417854
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081828.1.
            
            On Dec 8, 2007 this sequence version replaced NP_036895.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081828.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..796
                     /product="receptor-type tyrosine-protein phosphatase alpha
                     precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase alpha;
                     R-PTP-alpha; protein tyrosine phosphatase alpha"
                     /calculated_mol_wt=88096
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2121
     Region          <18..169
                     /region_name="PHA03255"
                     /note="BDLF3; Provisional"
                     /db_xref="CDD:165513"
     mat_peptide     20..796
                     /product="Receptor-type tyrosine-protein phosphatase
                     alpha. /id=PRO_0000025435"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03348.1)"
                     /calculated_mol_wt=88096
     Site            20
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Region          78..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03348.1)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            146..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03348.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     Region          208..503
                     /region_name="R-PTPc-A-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 1; cd14621"
                     /db_xref="CDD:350469"
     Region          557..784
                     /region_name="R-PTPc-A-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 2; cd14623"
                     /db_xref="CDD:350471"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q03348.1)"
     CDS             1..796
                     /gene="Ptpra"
                     /gene_synonym="LRP"
                     /coded_by="NM_012763.2:266..2656"
                     /db_xref="GeneID:25167"
                     /db_xref="RGD:3450"
ORIGIN      
        1 mdswfililf gsglihisan ntttvspslg ttrliktstt esakeenkts nstssvisls
       61 vtptfspnlt leptyvttvn sshsdngtkr aastesggtt ispngtygtw ltdnqftdar
      121 tepwegnsst aattpetfpp adetpiiavm valssllviv fiiivlymlr fkkykqagsh
      181 snsfrlsngr tedvepqsvp llarspstnr kfpplpvdkl eeeinrrmad dnklfreefn
      241 alpacpiqat ceaaskeenk eknryvnilp ydhsrvhltp vegvpdsdyi nasfingyqe
      301 knkfiaaqgp keetvndfwr miweqntati vmvtnlkerk eckcaqywpd qgcwtygnvr
      361 vsvedvtvlv dytvrkfciq qvgdvtnrkp qrlitqfhft swpdfgvpft pigmlkflkk
      421 vkacnpqyag aivvhcsagv grtgtfvvid amldmmhser kvdvygfvsr iraqrcqmvq
      481 tdmqyvfiyq allehylygd televtsldt hlqkiynkip gtsnngleee fkkltsikiq
      541 ndkmrtgnlp anmkknrvlq iipyefnrvi ipvkrgeent dyvnasfidg yrqkdsyias
      601 qgpllhtied fwrmiwewks csivmltele ergqekcaqy wpsdglvsyg ditvelkkee
      661 ecesytvrdl lvtntrenks rqirqfhfhg wpevgipsdg kgminiiaav qkqqqqsgnh
      721 pitvhcsaga grtgtfcals tvlervkaeg ildvfqtvks lrlqrphmvq tleqyefcyk
      781 vvqeyidafs dyanfk
//
LOCUS       NP_037166                630 aa            linear   ROD 28-APR-2025
DEFINITION  sodium-dependent serotonin transporter [Rattus norvegicus].
ACCESSION   NP_037166 XP_001080660 XP_001080667
VERSION     NP_037166.2
DBSOURCE    REFSEQ: accession NM_013034.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Boillot,M., Ter Horst,J., Lopez,J.R., Di Fazio,I., Steens,I.L.M.,
            Cohen,M.X. and Homberg,J.R.
  TITLE     Serotonin transporter knockout in rats reduces beta- and gamma-band
            functional connectivity between the orbitofrontal cortex and
            amygdala during auditory discrimination
  JOURNAL   Cereb Cortex 34 (8) (2024)
   PUBMED   39128940
  REMARK    GeneRIF: Serotonin transporter knockout in rats reduces beta- and
            gamma-band functional connectivity between the orbitofrontal cortex
            and amygdala during auditory discrimination.
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Sun,M., Brivio,P., Shan,L., Docq,S., Heltzel,L.C.M.W.,
            Smits,C.A.J., Middelman,A., Vrooman,R., Spoelder,M.,
            Verheij,M.M.M., Buitelaar,J.K., Boillot,M., Calabrese,F.,
            Homberg,J.R. and Hanswijk,S.I.
  TITLE     Offspring's own serotonin transporter genotype, independently from
            the maternal one, increases anxiety- and depression-like behavior
            and alters neuroplasticity markers in rats
  JOURNAL   J Affect Disord 350, 89-101 (2024)
   PUBMED   38220097
  REMARK    GeneRIF: Offspring's own serotonin transporter genotype,
            independently from the maternal one, increases anxiety- and
            depression-like behavior and alters neuroplasticity markers in
            rats.
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Ngoupaye,G.T., Mokgokong,M., Madlala,T. and Mabandla,M.V.
  TITLE     Alteration of the alpha5 GABA receptor and 5HTT lead to cognitive
            deficits associated with major depressive-like behaviors in a
            14-day combined stress rat model
  JOURNAL   Int J Neurosci 133 (9), 959-976 (2023)
   PUBMED   34937496
  REMARK    GeneRIF: Alteration of the alpha5 GABA receptor and 5HTT lead to
            cognitive deficits associated with major depressive-like behaviors
            in a 14-day combined stress rat model.
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Yildirim,H., Efe Daskan,B., Aksoz,E., Sen,F. and Celebi,M.
  TITLE     Regional expression differences of SERT and TSPAN8 in hippocampus,
            cerebellum and cortex of wild-type young, adult and middle-aged
            rats
  JOURNAL   Gene 885, 147706 (2023)
   PUBMED   37572802
  REMARK    GeneRIF: Regional expression differences of SERT and TSPAN8 in
            hippocampus, cerebellum and cortex of wild-type young, adult and
            middle-aged rats.
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Thorne,B.N., Ellenbroek,B.A. and Day,D.J.
  TITLE     The serotonin reuptake transporter modulates mitochondrial copy
            number and mitochondrial respiratory complex gene expression in the
            frontal cortex and cerebellum in a sexually dimorphic manner
  JOURNAL   J Neurosci Res 100 (3), 869-879 (2022)
   PUBMED   35043462
  REMARK    GeneRIF: The serotonin reuptake transporter modulates mitochondrial
            copy number and mitochondrial respiratory complex gene expression
            in the frontal cortex and cerebellum in a sexually dimorphic
            manner.
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Ramamoorthy,J.D., Ramamoorthy,S., Papapetropoulos,A.,
            Catravas,J.D., Leibach,F.H. and Ganapathy,V.
  TITLE     Cyclic AMP-independent up-regulation of the human serotonin
            transporter by staurosporine in choriocarcinoma cells
  JOURNAL   J Biol Chem 270 (29), 17189-17195 (1995)
   PUBMED   7615516
REFERENCE   7  (residues 1 to 630)
  AUTHORS   Ramamoorthy,S., Bauman,A.L., Moore,K.R., Han,H., Yang-Feng,T.,
            Chang,A.S., Ganapathy,V. and Blakely,R.D.
  TITLE     Antidepressant- and cocaine-sensitive human serotonin transporter:
            molecular cloning, expression, and chromosomal localization
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2542-2546 (1993)
   PUBMED   7681602
REFERENCE   8  (residues 1 to 630)
  AUTHORS   Mayser,W., Betz,H. and Schloss,P.
  TITLE     Isolation of cDNAs encoding a novel member of the neurotransmitter
            transporter gene family
  JOURNAL   FEBS Lett 295 (1-3), 203-206 (1991)
   PUBMED   1765155
REFERENCE   9  (residues 1 to 630)
  AUTHORS   Blakely,R.D., Berson,H.E., Fremeau,R.T. Jr., Caron,M.G., Peek,M.M.,
            Prince,H.K. and Bradley,C.C.
  TITLE     Cloning and expression of a functional serotonin transporter from
            rat brain
  JOURNAL   Nature 354 (6348), 66-70 (1991)
   PUBMED   1944572
REFERENCE   10 (residues 1 to 630)
  AUTHORS   Hoffman,B.J., Mezey,E. and Brownstein,M.J.
  TITLE     Cloning of a serotonin transporter affected by antidepressants
  JOURNAL   Science 254 (5031), 579-580 (1991)
   PUBMED   1948036
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M79450.1, CB736426.1, JAXUCZ010000010.1, BF548147.1 and AI547408.1.
            
            On or before Jun 25, 2006 this sequence version replaced
            XP_001080667.1, XP_001080660.1, NP_037166.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y11024.1, X63995.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..630
                     /product="sodium-dependent serotonin transporter"
                     /note="Solute carrier family 6 (neurotransmitter
                     transporter serotonin) member 4 (5-hydroxytryptamine
                     (serotonin) transporter); serotonin transporter; 5HTT; 5HT
                     transporter; solute carrier family 6 (neurotransmitter
                     transporter), member 4; solute carrier family 6
                     (neurotransmitter transporter, serotonin), member 4"
                     /calculated_mol_wt=70041
     Region          23..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Region          24..64
                     /region_name="5HT_transport_N"
                     /note="Serotonin (5-HT) neurotransmitter transporter,
                     N-terminus; pfam03491"
                     /db_xref="CDD:397524"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31645; propagated from
                     UniProtKB/Swiss-Prot (P31652.1)"
     Region          79..615
                     /region_name="SLC6sbd_SERT"
                     /note="Na(+)- and Cl(-)-dependent serotonin transporter
                     SERT; solute-binding domain; cd11513"
                     /db_xref="CDD:271399"
     Site            88..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            order(94,97,434,437..438)
                     /site_type="other"
                     /note="Na binding site 2 [ion binding]"
                     /db_xref="CDD:271399"
     Site            order(95..96,98..101,176,335..336,341,343,438,441..442)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:271399"
     Site            order(96,101,336,368)
                     /site_type="other"
                     /note="Na binding site 1 [ion binding]"
                     /db_xref="CDD:271399"
     Site            order(103..104,175,179,182,403,407)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:271399"
     Site            116..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P31645; propagated from
                     UniProtKB/Swiss-Prot (P31652.1)"
     Site            161..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            208
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P31645; propagated from
                     UniProtKB/Swiss-Prot (P31652.1)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P31645; propagated from
                     UniProtKB/Swiss-Prot (P31652.1)"
     Site            253..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17310063; propagated from
                     UniProtKB/Swiss-Prot (P31652.1)"
     Site            278..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            325..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            361..380
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            422..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            464..483
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            495..516
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            539..558
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Site            575..595
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     Region          616..624
                     /region_name="Interaction with RAB4A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P31652.1)"
     CDS             1..630
                     /gene="Slc6a4"
                     /gene_synonym="SERT"
                     /coded_by="NM_013034.4:108..2000"
                     /db_xref="GeneID:25553"
                     /db_xref="RGD:3714"
ORIGIN      
        1 mettplnsqk vlseckdred cqengvlqkg vpttadraep sqisngysav pstsagdeas
       61 hsipaatttl vaeirqgere twgkkmdfll svigyavdlg niwrfpyicy qngggafllp
      121 ytimaifggi plfymelalg qyhrngcisi wrkicpifkg igyaiciiaf yiasyyntii
      181 awalyyliss ltdrlpwtsc tnswntgnct nyfaqdnitw tlhstspaee fylrhvlqih
      241 qskglqdlgt iswqltlciv liftviyfsi wkgvktsgkv vwvtatfpyi vlsvllvrga
      301 tlpgawrgvv fylkpnwqkl letgvwvdaa aqiffslgpg fgvllafasy nkfnnncyqd
      361 alvtsvvncm tsfvsgfvif tvlgymaemr nedvsevakd agpsllfity aeaianmpas
      421 tffaiifflm litlgldstf aglegvitav ldefphiwak rrewfvlivv itcvlgsllt
      481 ltsggayvvt lleeyatgpa vltvalieav avswfygitq fcsdvkemlg fspgwfwric
      541 wvaisplfll fiicsflmsp pqlrlfqyny phwsivlgyc igmssvicip tyiiyrlist
      601 pgtlkeriik sitpetptei pcgdirmnav
//
LOCUS       NP_001020886             128 aa            linear   ROD 28-APR-2025
DEFINITION  LIM domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001020886 XP_340924
VERSION     NP_001020886.1
DBSOURCE    REFSEQ: accession NM_001025715.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098855.1.
            
            On Jul 22, 2005 this sequence version replaced XP_340924.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098855.1, CO572150.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..128
                     /product="LIM domain-containing protein 2"
                     /calculated_mol_wt=14105
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM31.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9BT23; propagated from
                     UniProtKB/Swiss-Prot (Q4KM31.1)"
     Region          41..93
                     /region_name="LIM_Eplin_like_1"
                     /note="a LIM domain subfamily on a group of proteins with
                     unknown function; cd09486"
                     /db_xref="CDD:188870"
     Site            order(41,44,62,65,68,71,89,92)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188870"
     CDS             1..128
                     /gene="Limd2"
                     /gene_synonym="RGD1309967"
                     /coded_by="NM_001025715.1:134..520"
                     /db_xref="GeneID:360646"
                     /db_xref="RGD:1309967"
ORIGIN      
        1 mfqaagaaqa tpsheakgss gnstvqrsks fslraqvket caacqktvyp merlvadkli
       61 fhnscfcckh chtklslgsy aamhgefyck phfqqlfksk gnydegfgrk qhkelwahke
      121 vdsgtkta
//
LOCUS       NP_112292               1305 aa            linear   ROD 28-APR-2025
DEFINITION  cyclin-G-associated kinase [Rattus norvegicus].
ACCESSION   NP_112292
VERSION     NP_112292.1
DBSOURCE    REFSEQ: accession NM_031030.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1305)
  AUTHORS   Beilina,A., Rudenko,I.N., Kaganovich,A., Civiero,L., Chau,H.,
            Kalia,S.K., Kalia,L.V., Lobbestael,E., Chia,R., Ndukwe,K., Ding,J.,
            Nalls,M.A., Olszewski,M., Hauser,D.N., Kumaran,R., Lozano,A.M.,
            Baekelandt,V., Greene,L.E., Taymans,J.M., Greggio,E. and
            Cookson,M.R.
  CONSRTM   International Parkinson's Disease Genomics Consortium; North
            American Brain Expression Consortium
  TITLE     Unbiased screen for interactors of leucine-rich repeat kinase 2
            supports a common pathway for sporadic and familial Parkinson
            disease
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2626-2631 (2014)
   PUBMED   24510904
REFERENCE   2  (residues 1 to 1305)
  AUTHORS   Yim,Y.I., Sun,T., Wu,L.G., Raimondi,A., De Camilli,P., Eisenberg,E.
            and Greene,L.E.
  TITLE     Endocytosis and clathrin-uncoating defects at synapses of auxilin
            knockout mice
  JOURNAL   Proc Natl Acad Sci U S A 107 (9), 4412-4417 (2010)
   PUBMED   20160091
REFERENCE   3  (residues 1 to 1305)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 1305)
  AUTHORS   Lee,D.W., Zhao,X., Yim,Y.I., Eisenberg,E. and Greene,L.E.
  TITLE     Essential role of cyclin-G-associated kinase (Auxilin-2) in
            developing and mature mice
  JOURNAL   Mol Biol Cell 19 (7), 2766-2776 (2008)
   PUBMED   18434600
REFERENCE   5  (residues 1 to 1305)
  AUTHORS   Zhang,C.X., Engqvist-Goldstein,A.E., Carreno,S., Owen,D.J.,
            Smythe,E. and Drubin,D.G.
  TITLE     Multiple roles for cyclin G-associated kinase in clathrin-mediated
            sorting events
  JOURNAL   Traffic 6 (12), 1103-1113 (2005)
   PUBMED   16262722
  REMARK    GeneRIF: Early stages of clathrin-mediated endocytosis (CME) were
            partially inhibited when GAK expression was knocked down; GAK plays
            a role in clathrin-dependent trafficking from the trans Golgi
            network.
REFERENCE   6  (residues 1 to 1305)
  AUTHORS   Lee,D.W., Zhao,X., Zhang,F., Eisenberg,E. and Greene,L.E.
  TITLE     Depletion of GAK/auxilin 2 inhibits receptor-mediated endocytosis
            and recruitment of both clathrin and clathrin adaptors
  JOURNAL   J Cell Sci 118 (Pt 18), 4311-4321 (2005)
   PUBMED   16155256
REFERENCE   7  (residues 1 to 1305)
  AUTHORS   Kanaoka,Y., Kimura,S.H., Okazaki,I., Ikeda,M. and Nojima,H.
  TITLE     GAK: a cyclin G associated kinase contains a tensin/auxilin-like
            domain
  JOURNAL   FEBS Lett 402 (1), 73-80 (1997)
   PUBMED   9013862
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D38560.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D38560.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..1305
                     /product="cyclin-G-associated kinase"
                     /EC_number="2.7.11.1"
                     /note="dnaJ homolog subfamily C member 26"
                     /calculated_mol_wt=143573
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Region          39..320
                     /region_name="STKc_GAK"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, cyclin G-Associated Kinase; cd14036"
                     /db_xref="CDD:270938"
     Site            order(46..50,54,67,69,99,123..126,129,131,173,175,
                     177..178,180,191,194,222..225)
                     /site_type="active"
                     /db_xref="CDD:270938"
     Site            order(46..50,54,67,69,99,123..126,129,173,175,177..178,
                     180,191)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270938"
     Site            order(50,129,131,173,175,177,194,222..225)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270938"
     Site            order(190..220,222..225)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270938"
     Region          332..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97874.1)"
     Region          398..560
                     /region_name="PTP_GAK"
                     /note="protein tyrosine phosphatase-like domain of
                     cyclin-G-associated kinase; cd14564"
                     /db_xref="CDD:350412"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Region          568..706
                     /region_name="PTEN_C2"
                     /note="C2 domain of PTEN tumour-suppressor protein;
                     pfam10409"
                     /db_xref="CDD:463081"
     Region          747..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97874.1)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Region          819..>1138
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Region          1044..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97874.1)"
     Site            1122
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99KY4; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Site            1171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14976; propagated from
                     UniProtKB/Swiss-Prot (P97874.1)"
     Region          <1253..1298
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(1269..1271,1283,1286..1287,1290..1291)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     CDS             1..1305
                     /gene="Gak"
                     /coded_by="NM_031030.2:105..4022"
                     /db_xref="GeneID:81659"
                     /db_xref="RGD:621589"
ORIGIN      
        1 msllqsaldf lagpgslgga agrdqsdfvg qtvelgelrl rvrrvlaegg fafvyeaqdl
       61 gsgreyalkr llsneeeknr aiiqevcflk klsghpnivq fcsaasigke esdtgqaefl
      121 lltelckgql veflrrveck gplscdsilk ifyqtcravq hmhrqkppii hrdlkvenll
      181 lsnqgtiklc dfgsattish ypdyswsaqk ramveeeitr nttpmyrtpe ivdlysnfpi
      241 gekqdiwalg cilyllcfrq hpfedgaklr ivngkysipv ndtrytvfhd lirgmlkvnp
      301 eerlsiaevv rqlqeiaaar nvnpkapite lleqnggygn sgpsraqpps ggpvnssgvl
      361 alaeydqpyg gfldilrggt erlftnlkdt sskviqsvan yakgdldisy itsriavmsf
      421 paegvesaik nniedvrlfl dakhpghyav ynlspriyra skfhnrvtec gwavrraphl
      481 hslytlcrsm hawlredhrn vcvvhcmdgr aasavavcaf lcfcrlfsta eaavymfsmk
      541 rcppgiwpsh kryieyvcdm vaeepitphs kpmlvksvvm tpvplfskqr ngcrpfcevy
      601 vgeervttts qeydrmkefk iedgkavipl gitvqgdvlt iiyharstlg grlqakmasm
      661 kmfqiqfhtg fvprnattvk fakydldacd iqekypdlfq vnlevevepr drpsrdvppw
      721 entslrglnp kilfsnreeq qdilskfgkp elprqpgsta qydaeagspe aeitesdspq
      781 ssstdtnhfl htldwqeekd petgvdntsp kesqsnliad gdgsevsdee eascpseerk
      841 pgagedtprl aagtrqqdli fdvgmlaapq epvqpeegvd llglhsegdl rpaaplqasg
      901 vqssntdlls sllepsdasq vgppgdllgg etplllaspv sllgvqsnlq gkvpdtvdpf
      961 dqfllpsssd tqpcskpdlf geflnsdsva sstafpsths apppscstaf lhlgdlpaep
     1021 nkviassshp dllggwdtwa etalpgpasm pvpegtlfss aghpappgpn psqtksqnpd
     1081 pfadlsdlss slqglpaglp agsfvgtsat thksnsswqt trptapgtsw ppqakpapra
     1141 seqlrshfsv igareergvr apsfaqkpkv sendfedllp nqgfsksdkk gpktmaemrk
     1201 qelardtdpf klklldwieg kerniralls tlhtvlwdge srwtpvsmad lvtpeqvkkq
     1261 yrravlvvhp dkatgqpyeq sakmifmeln dawsefenqg srplf
//
LOCUS       NP_001017491             406 aa            linear   ROD 28-APR-2025
DEFINITION  lymphocyte transmembrane adapter 1 [Rattus norvegicus].
ACCESSION   NP_001017491 XP_573453
VERSION     NP_001017491.1
DBSOURCE    REFSEQ: accession NM_001017491.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhu,M., Granillo,O., Wen,R., Yang,K., Dai,X., Wang,D. and Zhang,W.
  TITLE     Negative regulation of lymphocyte activation by the adaptor protein
            LAX
  JOURNAL   J Immunol 174 (9), 5612-5619 (2005)
   PUBMED   15843560
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Zhu,M., Janssen,E., Leung,K. and Zhang,W.
  TITLE     Molecular cloning of a novel gene encoding a membrane-associated
            adaptor protein (LAX) in lymphocyte signaling
  JOURNAL   J Biol Chem 277 (48), 46151-46158 (2002)
   PUBMED   12359715
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089837.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573453.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389, SAMN06680412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..406
                     /product="lymphocyte transmembrane adapter 1"
                     /note="membrane-associated adapter protein LAX"
                     /calculated_mol_wt=43805
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Region          28..355
                     /region_name="LAX"
                     /note="Lymphocyte activation family X; pfam15681"
                     /db_xref="CDD:464799"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Region          109..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWV1; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Region          219..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWV1; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWV1; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8IWV1; propagated from
                     UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     Region          358..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVQ5.1)"
     CDS             1..406
                     /gene="Lax1"
                     /coded_by="NM_001017491.1:350..1570"
                     /db_xref="GeneID:498232"
                     /db_xref="RGD:1563522"
ORIGIN      
        1 myttpappei trrssepstq qgtlgslege kghllfpgfv vlvtiflvvi vtcilwsrkk
       61 qkkrrvpylq vtpslalppp rqrakniydf lprqqtelgr hqlsgfstes llsrasdspe
      121 pevpqasgsl qkhrasvhav eytvgvydng tvaqmcgpla ssahrvcdgt srnnsisske
      181 sndyvnipta edtsetltct kstpeshlgl psgqrlefae gghagcgkat drtgvwapgl
      241 qgsnslsegd dssqssndyv nmtgldledi qesrprvafq ccrdyenvpp vvangsqlqt
      301 veevtssttd rgepaqrtlp svyhmafrps awsedgamip geeasngdss dyenvlvpel
      361 egkdwkqgpg twhpsdertp sdqagkfcea vypagslate tsgeev
//
LOCUS       NP_659550                924 aa            linear   ROD 28-APR-2025
DEFINITION  centrosomal protein of 104 kDa [Rattus norvegicus].
ACCESSION   NP_659550 XP_001076921 XP_575968
VERSION     NP_659550.2
DBSOURCE    REFSEQ: accession NM_145082.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Babcock,K.K., Chen,X., Eggeman,K.T., Kumar,K.N., Decedue,C.J. and
            Michaelis,E.K.
  TITLE     A synaptic membrane glycine-, glutamate- and
            thienylcyclohexylpiperidine-binding protein: isolation and
            immunochemical characterization
  JOURNAL   Neurochem Int 29 (5), 507-519 (1996)
   PUBMED   8939461
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Kumar,K.N., Babcock,K.K., Johnson,P.S., Chen,X., Ahmad,M. and
            Michaelis,E.K.
  TITLE     Cloning of the cDNA for a brain glycine-, glutamate- and
            thienylcyclohexylpiperidine-binding protein
  JOURNAL   Biochem Biophys Res Commun 216 (1), 390-398 (1995)
   PUBMED   7488117
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AA924538.1, BI289406.1, CB544954.1, JAXUCZ010000005.1, U53513.1,
            CV797293.1, CB792008.1, CO390283.1, FM108776.1, DV722335.1 and
            CK843167.1.
            
            On or before May 22, 2010 this sequence version replaced
            XP_575968.3, XP_001076921.2, NP_659550.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data from several strains because no single
            transcript was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments and
            orthologous data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.1321335.1,
                                           SRR26360186.630141.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..924
                     /product="centrosomal protein of 104 kDa"
                     /note="glycine-, glutamate-,
                     thienylcyclohexylpiperidine-binding protein; gly-, L-Glu
                     and TCP-binding protein; glycine-, glutamate- and
                     thienylcyclohexylpiperidine-binding protein"
                     /calculated_mol_wt=103889
     Region          <300..418
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          309..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     Region          350..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     Region          431..468
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(451..452,455,467..468,497..498,501,504..505,508,
                     545..546,549,552..553,556,576..577,580,583..584,626..627,
                     630,633..634)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          480..508
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          527..557
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          528..566
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     Region          563..584
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          603..639
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     Region          606..635
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          675..743
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     Region          882..924
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8X7.3)"
     CDS             1..924
                     /gene="Cep104"
                     /gene_synonym="GlyBP"
                     /coded_by="NM_145082.2:247..3021"
                     /db_xref="GeneID:246295"
                     /db_xref="RGD:708505"
ORIGIN      
        1 mphkigfvvv sssghedgfs arelmihapt vsgwrspkfc qfpqeivlqm vercrirklq
       61 llahqymiss kvefyisesl peylvpyqae rfrrlgyvsl cdnektgcka relksvyvda
      121 vgqflklifh qnhankynvy nqvalvaini igdpadlgde snttcrekli dhylghsphn
      181 pedpaldgtf agrsdyispl ddlafdmyqd pevaqiirrl derkreaakk erydhakklk
      241 qaiadlqkvg erlgryevek rravekedyd lakekkqqma ryraqvyeql elhgllqgep
      301 emqrpfalpl qplaspsspq hwkavsslpr teelaaedtc agpilqekpl assprhsavd
      361 rsppaagpap rshvealpyd erplpvtrkq leepsaepev readsdvrrr gvsaepeplt
      421 ekalreassa idtlgealva gayskmwscr edallalykr lmempvgtqk gfvknmlras
      481 vflirraikd ivtsvfqasl kllkmiitqy ipkhklgkld ttycveraip lllartgdss
      541 arlrvmalnf iqemalfkev rslqlipsyl vqplktnasv hlamsqvdll arllrdlgte
      601 gsgftvdnvm kfavsalehr vyevretavr iildmyrqhp altlehlppd dsttrrnlly
      661 kaifegfaki dgrpteaegk tqkrvvtkea ekqkkeetka lqglsaapre tqagvqeken
      721 eavklknqdp qgrkaappdt peipdnhyld nlcifcgern esfteegldl hywkhclmlt
      781 rcdhcrqvve issltehllt ecdkrdgfgk cprcseavpk eelprhiktk ecnpaksekv
      841 anrcplchen fapgeeawkv hlmgsagctm nlrkthilck apapqqgkgp masksgtsap
      901 kvgskiptpk gglsksssrt htrr
//
LOCUS       NP_444178                424 aa            linear   ROD 28-APR-2025
DEFINITION  vasopressin V1a receptor [Rattus norvegicus].
ACCESSION   NP_444178
VERSION     NP_444178.2
DBSOURCE    REFSEQ: accession NM_053019.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Das,S., Komnenov,D., Newhouse,L., Rishi,A.K. and Rossi,N.F.
  TITLE     Paraventricular Nucleus V1a Receptor Knockdown Blunts
            Neurocardiovascular Responses to Acute Stress in Male Rats after
            Chronic Mild Unpredictable Stress
  JOURNAL   Physiol Behav 253, 113867 (2022)
   PUBMED   35661787
  REMARK    GeneRIF: Paraventricular Nucleus V1a Receptor Knockdown Blunts
            Neurocardiovascular Responses to Acute Stress in Male Rats after
            Chronic Mild Unpredictable Stress.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Salehi,M.S., Neumann,I.D., Jurek,B. and Pandamooz,S.
  TITLE     Co-Stimulation of Oxytocin and Arginine-Vasopressin Receptors
            Affect Hypothalamic Neurospheroid Size
  JOURNAL   Int J Mol Sci 22 (16), 8464 (2021)
   PUBMED   34445168
  REMARK    GeneRIF: Co-Stimulation of Oxytocin and Arginine-Vasopressin
            Receptors Affect Hypothalamic Neurospheroid Size.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Komnenov,D., Quaal,H. and Rossi,N.F.
  TITLE     V1a and V1b vasopressin receptors within the paraventricular
            nucleus contribute to hypertension in male rats exposed to chronic
            mild unpredictable stress
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 320 (3), R213-R225 (2021)
   PUBMED   33264070
  REMARK    GeneRIF: V1a and V1b vasopressin receptors within the
            paraventricular nucleus contribute to hypertension in male rats
            exposed to chronic mild unpredictable stress.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Savic,B., Martin,A., Mecawi,A.S., Bukumiric,Z.,
            Antunes-Rodrigues,J., Murphy,D., Sarenac,O. and Japundzic-Zigon,N.
  TITLE     Vasopressin and v1br gene expression is increased in the
            hypothalamic pvn of borderline hypertensive rats
  JOURNAL   Hypertens Res 43 (11), 1165-1174 (2020)
   PUBMED   32415179
  REMARK    GeneRIF: Vasopressin and v1br gene expression is increased in the
            hypothalamic pvn of borderline hypertensive rats.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Freeman,S.M., Ngo,J., Singh,B., Masnaghetti,M., Bales,K.L. and
            Blevins,J.E.
  TITLE     Effects of Chronic Oxytocin Administration and Diet Composition on
            Oxytocin and Vasopressin 1a Receptor Binding in the Rat Brain
  JOURNAL   Neuroscience 392, 241-251 (2018)
   PUBMED   30071278
  REMARK    GeneRIF: Findings suggest that forebrain oxytocin receptor and
            vasopressin 1a are down-regulated in response to chronic oxytocin
            treatment.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Murasawa,S., Matsubara,H., Kijima,K., Maruyama,K., Mori,Y. and
            Inada,M.
  TITLE     Structure of the rat V1a vasopressin receptor gene and
            characterization of its promoter region and complete cDNA sequence
            of the 3'-end
  JOURNAL   J Biol Chem 270 (34), 20042-20050 (1995)
   PUBMED   7650021
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Chini,B., Mouillac,B., Ala,Y., Balestre,M.N., Trumpp-Kallmeyer,S.,
            Hoflack,J., Elands,J., Hibert,M., Manning,M., Jard,S. et al.
  TITLE     Tyr115 is the key residue for determining agonist selectivity in
            the V1a vasopressin receptor
  JOURNAL   EMBO J 14 (10), 2176-2182 (1995)
   PUBMED   7774575
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Wheatley,M., Howl,J., Morel,A. and Davies,A.R.
  TITLE     Homology between neurohypophyseal hormone receptors
  JOURNAL   Biochem J 296 (Pt 2) (Pt 2), 519 (1993)
   PUBMED   8257445
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Morel,A., Lolait,S.J. and Brownstein,M.J.
  TITLE     Molecular cloning and expression of rat V1a and V2 arginine
            vasopressin receptors
  JOURNAL   Regul Pept 45 (1-2), 53-59 (1993)
   PUBMED   8511367
  REMARK    Review article
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Morel,A., O'Carroll,A.M., Brownstein,M.J. and Lolait,S.J.
  TITLE     Molecular cloning and expression of a rat V1a arginine vasopressin
            receptor
  JOURNAL   Nature 356 (6369), 523-526 (1992)
   PUBMED   1560825
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U39450.1.
            
            On Jul 23, 2003 this sequence version replaced NP_444178.1.
            
            Summary: This gene encodes a receptor for arginine vasopressin, a
            neurohypophyseal hormone involved in diuresis inhibition, smooth
            muscle contraction, liver glycogenolysis stimulation and regulation
            of adrenocorticotropic hormone release from the pituitary. This
            receptor represents one of three G protein-coupled arginine
            vasopressin receptors which functions through a
            phosphotidylinositol-calcium second messenger system in vascular
            and hepatic tissues. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z11690.1, BC088095.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..424
                     /product="vasopressin V1a receptor"
                     /note="arginine vasopressin receptor V1a;
                     vascular/hepatic-type arginine vasopressin receptor;
                     antidiuretic hormone receptor 1a"
                     /calculated_mol_wt=47524
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Site            27
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30560.4)"
     Region          52..365
                     /region_name="7tmA_V1aR"
                     /note="vasopressin receptor subtype 1A, member of the
                     class A family of seven-transmembrane G protein-coupled
                     receptors; cd15385"
                     /db_xref="CDD:320507"
     Region          53..79
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320507"
     Site            53..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          86..113
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320507"
     Site            89..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Site            order(109,112..113,124..129,131..132,135,179,181..185,215,
                     218..220,222..224,226..227,310,313..314,316..317,320,
                     332..333,335..337,340,343..344)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320507"
     Region          124..154
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320507"
     Site            126..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          166..187
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320507"
     Site            169..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          215..244
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320507"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          290..320
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320507"
     Site            300..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          333..358
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320507"
     Site            338..357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Region          378..424
                     /region_name="V1R_C"
                     /note="Vasopressin V1 receptor, C-terminal; pfam08983"
                     /db_xref="CDD:430355"
     Region          383..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30560.4)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62463; propagated from
                     UniProtKB/Swiss-Prot (P30560.4)"
     CDS             1..424
                     /gene="Avpr1a"
                     /gene_synonym="AVPR; V1a; V1aR"
                     /coded_by="NM_053019.2:242..1516"
                     /db_xref="GeneID:25107"
                     /db_xref="RGD:2185"
ORIGIN      
        1 msfprgsqdr svgnsspwwp lttegsngsq eaarlgegds plgdvrneel akleiavlav
       61 ifvvavlgns svllalhrtp rktsrmhlfi rhlsladlav affqvlpqlc wdityrfrgp
      121 dwlcrvvkhl qvfamfasay mlvvmtadry iavchplktl qqparrsrlm iatswvlsfi
      181 lstpqyfifs vieievnngt ktqdcwatfi qpwgtrayvt wmtsgvfvap vvvlgtcygf
      241 icyhiwrnir gktassrhsk gdkgsgeavg pfhkgllvtp cvssvksisr akirtvkmtf
      301 vivsayilcw apffivqmws vwdenfiwtd senpsitita llaslnsccn pwiymffsgh
      361 llqdcvqsfp cchsmaqkfa kddsdsmsrr qtsysnnrsp tnstgmwkds pkssksirfi
      421 pvst
//
LOCUS       NP_112397                480 aa            linear   ROD 28-APR-2025
DEFINITION  Krueppel-like factor 10 [Rattus norvegicus].
ACCESSION   NP_112397
VERSION     NP_112397.1
DBSOURCE    REFSEQ: accession NM_031135.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Li,Q., Shen,P., Zeng,S. and Liu,P.
  TITLE     TIEG1 Inhibits Angiotensin II-induced Cardiomyocyte Hypertrophy by
            Inhibiting Transcription Factor GATA4
  JOURNAL   J Cardiovasc Pharmacol 66 (2), 196-203 (2015)
   PUBMED   26252173
  REMARK    GeneRIF: A novel role for TIEG1 was determined as an inhibitor in
            angiotensin II-induced cardiomyocyte hypertrophy.
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Martinez-Armenta,M., Diaz de Leon-Guerrero,S., Catalan,A.,
            Alvarez-Arellano,L., Uribe,R.M., Subramaniam,M., Charli,J.L. and
            Perez-Martinez,L.
  TITLE     TGFbeta2 regulates hypothalamic Trh expression through the TGFbeta
            inducible early gene-1 (TIEG1) during fetal development
  JOURNAL   Mol Cell Endocrinol 400, 129-139 (2015)
   PUBMED   25448845
  REMARK    GeneRIF: TGFbeta2 regulates hypothalamic TRH expression through
            TIEG1 during fetal development.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Iizuka,K., Takeda,J. and Horikawa,Y.
  TITLE     Kruppel-like factor-10 is directly regulated by carbohydrate
            response element-binding protein in rat primary hepatocytes
  JOURNAL   Biochem Biophys Res Commun 412 (4), 638-643 (2011)
   PUBMED   21856285
  REMARK    GeneRIF: these data suggest that crosstalk between ChREBP and
            KLF-10 is involved in the regulation of the lipogenic pathway.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Spittau,G., Happel,N., Behrendt,M., Chao,T.I., Krieglstein,K. and
            Spittau,B.
  TITLE     Tieg1/Klf10 is upregulated by NGF and attenuates cell cycle
            progression in the pheochromocytoma cell line PC12
  JOURNAL   J Neurosci Res 88 (9), 2017-2025 (2010)
   PUBMED   20155803
  REMARK    GeneRIF: our results identify Tieg1/Klf10 as a new NGF target gene
            and substantiate its anti-proliferative function in the NGF
            signaling pathway in PC12 cells
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Hirota,T., Kon,N., Itagaki,T., Hoshina,N., Okano,T. and Fukada,Y.
  TITLE     Transcriptional repressor TIEG1 regulates Bmal1 gene through GC box
            and controls circadian clockwork
  JOURNAL   Genes Cells 15 (2), 111-121 (2010)
   PUBMED   20070857
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Subramaniam,M., Gorny,G., Johnsen,S.A., Monroe,D.G., Evans,G.L.,
            Fraser,D.G., Rickard,D.J., Rasmussen,K., van Deursen,J.M.,
            Turner,R.T., Oursler,M.J. and Spelsberg,T.C.
  TITLE     TIEG1 null mouse-derived osteoblasts are defective in
            mineralization and in support of osteoclast differentiation in
            vitro
  JOURNAL   Mol Cell Biol 25 (3), 1191-1199 (2005)
   PUBMED   15657444
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Noti,J.D., Johnson,A.K. and Dillon,J.D.
  TITLE     The zinc finger transcription factor transforming growth factor
            beta-inducible early gene-1 confers myeloid-specific activation of
            the leukocyte integrin CD11d promoter
  JOURNAL   J Biol Chem 279 (26), 26948-26958 (2004)
   PUBMED   15087465
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Hevroni,D., Rattner,A., Bundman,M., Lederfein,D., Gabarah,A.,
            Mangelus,M., Silverman,M.A., Kedar,H., Naor,C., Kornuc,M.,
            Hanoch,T., Seger,R., Theill,L.E., Nedivi,E., Richter-Levin,G. and
            Citri,Y.
  TITLE     Hippocampal plasticity involves extensive gene induction and
            multiple cellular mechanisms
  JOURNAL   J Mol Neurosci 10 (2), 75-98 (1998)
   PUBMED   9699150
  REMARK    Review article
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Tachibana,I., Imoto,M., Adjei,P.N., Gores,G.J., Subramaniam,M.,
            Spelsberg,T.C. and Urrutia,R.
  TITLE     Overexpression of the TGFbeta-regulated zinc finger encoding gene,
            TIEG, induces apoptosis in pancreatic epithelial cells
  JOURNAL   J Clin Invest 99 (10), 2365-2374 (1997)
   PUBMED   9153278
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097309.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097309.1, U78875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132297, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..480
                     /product="Krueppel-like factor 10"
                     /note="TIEG-1; TGFB-inducible early growth response
                     protein 1; zinc finger transcription factor homolog CPG20;
                     transforming growth factor-beta-inducible early growth
                     response protein 1; TGFB inducible early growth response;
                     Kruppel-like factor 10"
                     /calculated_mol_wt=51698
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08876.1)"
     Region          33..369
                     /region_name="KLF10_N"
                     /note="N-terminal domain of Kruppel-like factor 10;
                     cd21572"
                     /db_xref="CDD:409241"
     Region          64..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08876.1)"
     Region          97..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08876.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13118; propagated from
                     UniProtKB/Swiss-Prot (O08876.1)"
     Region          202..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O08876.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13118; propagated from
                     UniProtKB/Swiss-Prot (O08876.1)"
     Region          369..393
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          374..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(378,380,382,384..385,388..389,392,408,410,414..415,
                     418..419,422,436,438,440,442..443,446..447,450)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          385..412
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          401..423
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..451
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          431..451
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..480
                     /gene="Klf10"
                     /gene_synonym="Tieg"
                     /coded_by="NM_031135.2:47..1489"
                     /db_xref="GeneID:81813"
                     /db_xref="RGD:621652"
ORIGIN      
        1 mlnfgaslqq asegkmelis ekskegahpw dkaeqsdfea vealmsmscd wkshfkkyle
       61 nrpvtpvsdt seedsllpgt pdlqtvpafc ltppyspsdf epsqgsnlta papptghfrs
      121 lsdaakppsi apfkeeeksp laapplpkaq atsvirhtad aqlcnhqscp vkaasilnyq
      181 dnsfrrrthi nveatrknip caavspnrpk pepstaanga ekagtapydf avpssetvic
      241 rssqpaptsp vqksvlmssp tvstggvppl pvicqmvplp annslvttvv pssppsqppa
      301 vcspvlfmgt qvpkgtvmfv vpqpvvqspk ppvvspngtr lspiapapgf spsaarvtpq
      361 idssrvrshi cshpgcgkty fksshlkahv rthtgekpfs cswkgcerrf arsdelsrhr
      421 rthtgekkfa cpmcdrrfmr sdhltkharr hlsakklpnw qmevsklndi alppatasaq
//
LOCUS       NP_001029187             496 aa            linear   ROD 28-APR-2025
DEFINITION  calcitonin receptor isoform 1a precursor [Rattus norvegicus].
ACCESSION   NP_001029187
VERSION     NP_001029187.1
DBSOURCE    REFSEQ: accession NM_001034015.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Andreassen,K.V., Feigh,M., Hjuler,S.T., Gydesen,S., Henriksen,J.E.,
            Beck-Nielsen,H., Christiansen,C., Karsdal,M.A. and Henriksen,K.
  TITLE     A novel oral dual amylin and calcitonin receptor agonist (KBP-042)
            exerts antiobesity and antidiabetic effects in rats
  JOURNAL   Am J Physiol Endocrinol Metab 307 (1), E24-E33 (2014)
   PUBMED   24801386
  REMARK    GeneRIF: In conclusion, oral KBP-042 is a novel DACRA, which exerts
            antiobesity and antidiabetic efficacy by dual modulation of insulin
            sensitivity and directly decelerating stress on the pancreatic
            alpha- and beta-cells.
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Gooi,J.H., Chia,L.Y., Walsh,N.C., Karsdal,M.A., Quinn,J.M.,
            Martin,T.J. and Sims,N.A.
  TITLE     Decline in calcitonin receptor expression in osteocytes with age
  JOURNAL   J Endocrinol 221 (2), 181-191 (2014)
   PUBMED   24516262
  REMARK    GeneRIF: Calcitonin receptor mRNA expression declines with age on
            osteocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Tural,S., Kara,N., Alayli,G. and Tomak,L.
  TITLE     Association between osteoporosis and polymorphisms of the bone Gla
            protein, estrogen receptor 1, collagen 1-A1 and calcitonin receptor
            genes in Turkish postmenopausal women
  JOURNAL   Gene 515 (1), 167-172 (2013)
   PUBMED   23137636
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Matsubara,R., Kukita,T., Ichigi,Y., Takigawa,I., Qu,P.F.,
            Funakubo,N., Miyamoto,H., Nonaka,K. and Kukita,A.
  TITLE     Characterization and identification of subpopulations of
            mononuclear preosteoclasts induced by TNF-alpha in combination with
            TGF-beta in rats
  JOURNAL   PLoS One 7 (10), e47930 (2012)
   PUBMED   23110133
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Abdelmagid,N., Bereczky-Veress,B., Guerreiro-Cacais,A.O.,
            Bergman,P., Luhr,K.M., Bergstrom,T., Skoldenberg,B., Piehl,F.,
            Olsson,T. and Diez,M.
  TITLE     The calcitonin receptor gene is a candidate for regulation of
            susceptibility to herpes simplex type 1 neuronal infection leading
            to encephalitis in rat
  JOURNAL   PLoS Pathog 8 (6), e1002753 (2012)
   PUBMED   22761571
  REMARK    GeneRIF: variability in Calcr was identified as potentially
            critical for infection and viral spread to the CNS and subsequent
            Herpes simplex encephalitis development.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Albrandt,K., Brady,E.M., Moore,C.X., Mull,E., Sierzega,M.E. and
            Beaumont,K.
  TITLE     Molecular cloning and functional expression of a third isoform of
            the human calcitonin receptor and partial characterization of the
            calcitonin receptor gene
  JOURNAL   Endocrinology 136 (12), 5377-5384 (1995)
   PUBMED   7588285
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Lee,S.K., Goldring,S.R. and Lorenzo,J.A.
  TITLE     Expression of the calcitonin receptor in bone marrow cell cultures
            and in bone: a specific marker of the differentiated osteoclast
            that is regulated by calcitonin
  JOURNAL   Endocrinology 136 (10), 4572-4581 (1995)
   PUBMED   7664679
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Egerton,M., Needham,M., Evans,S., Millest,A., Cerillo,G.,
            McPheat,J., Popplewell,M., Johnstone,D. and Hollis,M.
  TITLE     Identification of multiple human calcitonin receptor isoforms:
            heterologous expression and pharmacological characterization
  JOURNAL   J Mol Endocrinol 14 (2), 179-189 (1995)
   PUBMED   7619207
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Pandya,S.
  TITLE     Obituary. Dr. Wilder Penfield, 1891-1976
  JOURNAL   Neurol India 24 (2), V-VI (1976)
   PUBMED   796748
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Blattner,R.J.
  TITLE     Hemolytic anemia associated with Wilson's disease
  JOURNAL   J Pediatr 71 (2), 284-287 (1967)
   PUBMED   4961748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB791100.1 and L14617.1.
            
            Transcript Variant: This variant (1a, previously called 2), lacks
            an alternate in-frame exon compared to variant 1b. The resulting
            isoform (1a, previously called b), has the same N- and C-termini
            but is shorter compared to isoform 1b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L13041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN14984027, SAMN14984033
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q13"
     Protein         1..496
                     /product="calcitonin receptor isoform 1a precursor"
                     /note="CT-R; C1A/C1B"
                     /calculated_mol_wt=53086
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5005
     Region          86..154
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Region          162..435
                     /region_name="7tmB1_calcitonin_R"
                     /note="calcitonin receptor, member of the class B family
                     of seven-transmembrane G protein-coupled receptors;
                     cd15274"
                     /db_xref="CDD:341343"
     Region          164..189
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341343"
     Site            order(169,173,215,218..219,222,237,244,314..315,317,319,
                     373,376,390,394)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:341343"
     Site            order(197,260..261,264..266,269..271,340,343..344,
                     347..348,362,365,411,421,425,432,435)
                     /site_type="other"
                     /note="G protein interaction site [polypeptide binding]"
                     /db_xref="CDD:341343"
     Region          198..220
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341343"
     Region          237..264
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341343"
     Region          276..296
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341343"
     Region          311..340
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341343"
     Region          354..381
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341343"
     Region          387..412
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341343"
     CDS             1..496
                     /gene="Calcr"
                     /coded_by="NM_001034015.1:242..1732"
                     /note="isoform 1a precursor is encoded by transcript
                     variant 1a"
                     /db_xref="GeneID:116506"
                     /db_xref="RGD:621001"
ORIGIN      
        1 mtprrsrmkr rnlrkpkmrf lllnrftlll lllvsptpvl qaptnltdsg ldqepflylv
       61 grkklldaqy kcydriqqlp pyegegpycn rtwdgwmcwd dtpagvmsyq hcpdyfpdfd
      121 ptekvskycd engewfrhpd snrtwsnytl cnaftpdklh nayvlyylal vghsmsiaal
      181 iasmgiflff knlscqrvtl hknmfltyil nsiiiiihlv evvpngdlvr rdpisckilh
      241 ffhqymmacn yfwmlcegiy lhtlivmavf tedqrlrwyy llgwgfpivp tiihaitrav
      301 yyndncwlst ethllyiihg pvmaalvvnf ffllnivrvl vtkmrqthea eaymylkavk
      361 atmvlvpllg iqfvvfpwrp snkvlgkiyd ylmhslihfq gffvatiycf cnhevqvtlk
      421 rqwaqfkiqw shrwgrrrrp tnrvvsapra vafaepgglp iyichqeprn ppvsnnegee
      481 gtemipmnvi qqdssa
//
LOCUS       NP_037106               1801 aa            linear   ROD 28-APR-2025
DEFINITION  laminin subunit beta-2 precursor [Rattus norvegicus].
ACCESSION   NP_037106
VERSION     NP_037106.1
DBSOURCE    REFSEQ: accession NM_012974.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1801)
  AUTHORS   Wirtz,M.K., Sykes,R., Samples,J., Edmunds,B., Choi,D., Keene,D.R.,
            Tufa,S.F., Sun,Y.Y. and Keller,K.E.
  TITLE     Identification of Missense Extracellular Matrix Gene Variants in a
            Large Glaucoma Pedigree and Investigation of the N700S
            Thrombospondin-1 Variant in Normal and Glaucomatous Trabecular
            Meshwork Cells
  JOURNAL   Curr Eye Res 47 (1), 79-90 (2022)
   PUBMED   34143713
REFERENCE   2  (residues 1 to 1801)
  AUTHORS   Pulido,D., Briggs,D.C., Hua,J. and Hohenester,E.
  TITLE     Crystallographic analysis of the laminin beta2 short arm reveals
            how the LF domain is inserted into a regular array of LE domains
  JOURNAL   Matrix Biol 57-58, 204-212 (2017)
   PUBMED   27425256
  REMARK    GeneRIF: Crystallographic analysis of the LAMB2 short arm reveals
            how the LF domain is inserted into a regular array of LE domains.
REFERENCE   3  (residues 1 to 1801)
  AUTHORS   Barallobre-Barreiro,J., Gupta,S.K., Zoccarato,A.,
            Kitazume-Taneike,R., Fava,M., Yin,X., Werner,T., Hirt,M.N.,
            Zampetaki,A., Viviano,A., Chong,M., Bern,M., Kourliouros,A.,
            Domenech,N., Willeit,P., Shah,A.M., Jahangiri,M., Schaefer,L.,
            Fischer,J.W., Iozzo,R.V., Viner,R., Thum,T., Heineke,J.,
            Kichler,A., Otsu,K. and Mayr,M.
  TITLE     Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin
            Activity in Human Atrial Fibrillation
  JOURNAL   Circulation 134 (11), 817-832 (2016)
   PUBMED   27559042
REFERENCE   4  (residues 1 to 1801)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   5  (residues 1 to 1801)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   6  (residues 1 to 1801)
  AUTHORS   Noakes,P.G., Miner,J.H., Gautam,M., Cunningham,J.M., Sanes,J.R. and
            Merlie,J.P.
  TITLE     The renal glomerulus of mice lacking s-laminin/laminin beta 2:
            nephrosis despite molecular compensation by laminin beta 1
  JOURNAL   Nat Genet 10 (4), 400-406 (1995)
   PUBMED   7670489
REFERENCE   7  (residues 1 to 1801)
  AUTHORS   Noakes,P.G., Gautam,M., Mudd,J., Sanes,J.R. and Merlie,J.P.
  TITLE     Aberrant differentiation of neuromuscular junctions in mice lacking
            s-laminin/laminin beta 2
  JOURNAL   Nature 374 (6519), 258-262 (1995)
   PUBMED   7885444
REFERENCE   8  (residues 1 to 1801)
  AUTHORS   Utani,A., Nomizu,M., Timpl,R., Roller,P.P. and Yamada,Y.
  TITLE     Laminin chain assembly. Specific sequences at the C terminus of the
            long arm are required for the formation of specific double- and
            triple-stranded coiled-coil structures
  JOURNAL   J Biol Chem 269 (29), 19167-19175 (1994)
   PUBMED   8034675
REFERENCE   9  (residues 1 to 1801)
  AUTHORS   Engvall,E., Earwicker,D., Haaparanta,T., Ruoslahti,E. and
            Sanes,J.R.
  TITLE     Distribution and isolation of four laminin variants; tissue
            restricted distribution of heterotrimers assembled from five
            different subunits
  JOURNAL   Cell Regul 1 (10), 731-740 (1990)
   PUBMED   2099832
REFERENCE   10 (residues 1 to 1801)
  AUTHORS   Hunter,D.D., Shah,V., Merlie,J.P. and Sanes,J.R.
  TITLE     A laminin-like adhesive protein concentrated in the synaptic cleft
            of the neuromuscular junction
  JOURNAL   Nature 338 (6212), 229-234 (1989)
   PUBMED   2922051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X16563.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X16563.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132293
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1801
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1801
                     /product="laminin subunit beta-2 precursor"
                     /note="laminin chain beta 2; laminin, beta 2; laminin
                     chain B3; S-LAM beta; S-laminin subunit beta; laminin-3
                     subunit beta; laminin-4 subunit beta; laminin-7 subunit
                     beta; laminin-9 subunit beta; laminin-11 subunit beta;
                     laminin-14 subunit beta; laminin-15 subunit beta"
                     /calculated_mol_wt=192734
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3759
     mat_peptide     36..1801
                     /product="laminin subunit beta-2"
                     /calculated_mol_wt=192734
     Region          50..284
                     /region_name="Laminin_N"
                     /note="Laminin N-terminal (Domain VI); pfam00055"
                     /db_xref="CDD:459653"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Region          286..338
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(286,288,295,313,315,324)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          350..402
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(350,352,359,377,380,389)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            371
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Region          413..470
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(413,415,426,441,443,452)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          472..523
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(473,475,487,494,496,505)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          524..565
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(525,527,537,544,546,555)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          786..831
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domai;
                     smart00180"
                     /db_xref="CDD:214543"
     Site            order(786,788,798,805,807,816)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          834..882
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(834,836,846,853,855,864)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          880..927
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(880,882,889,896,899,908)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          929..987
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(930,932,946,957,959,968)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          989..>1031
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(989,991,1003,1010,1013,1022)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1041..1095
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1041,1043,1053,1068,1070,1079)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            1088
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Region          1098..1146
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1098,1100,1110,1117,1119,1128)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1146..1193
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1146,1148,1158,1165,1167,1176)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1193..1412
                     /region_name="Domain II"
                     /note="propagated from UniProtKB/Swiss-Prot (P15800.1)"
     Site            1252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Site            1311
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Site            1351
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Region          1413..1445
                     /region_name="Domain alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (P15800.1)"
     Region          1446..1801
                     /region_name="Domain I"
                     /note="propagated from UniProtKB/Swiss-Prot (P15800.1)"
     Region          <1448..>1793
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            1502
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Site            1535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55268; propagated from
                     UniProtKB/Swiss-Prot (P15800.1)"
     Region          1684..1703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15800.1)"
     Region          1730..1801
                     /region_name="cc_LAMB2_C"
                     /note="C-terminal coiled-coil domain found in laminin
                     subunit beta-2 (LAMB2); cd22299"
                     /db_xref="CDD:411970"
     Site            order(1733..1734,1737..1738,1740..1741,1744,1751..1752,
                     1754..1755,1758,1761..1762,1765..1766,1768..1770,
                     1772..1773,1776,1779..1780,1782..1784,1786..1787,
                     1789..1791,1793..1795,1797..1800)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:411970"
     CDS             1..1801
                     /gene="Lamb2"
                     /gene_synonym="SLAM"
                     /coded_by="NM_012974.1:69..5474"
                     /db_xref="GeneID:25473"
                     /db_xref="RGD:2988"
ORIGIN      
        1 mewasgkpgr grqgqpvpwe lrlglllsvl aatlaqvpsl dvpgcsrgsc ypatgdllvg
       61 radrltasst cglhspqpyc ivshlqdekk cflcdsrrpf sardnpnshr iqnvvtsfap
      121 qrrtawwqse ngvpmvtiql dleaefhfth limtfktfrp aamlversad fgrtwrvyry
      181 fsydcgadfp giplapprrw ddvvcesrys eiepstegev iyrvldpaip ipdpyssriq
      241 nllkitnlrv nltrlhtlgd nlldprreir ekyyyalyel virgncfcyg hasqcapapg
      301 apahaegmvh gacickhntr glnceqcqdf yqdlpwhpae dghthacrkc ecnghshsch
      361 fdmavylasg nvsggvcdgc qhntagrhce lcrpffyrdp tkdmrdpaac rpcdcdpmgs
      421 qdggrcdshd dpvlglvsgq crckehvvgt rcqqcrdgff glsasnprgc qrcqcnsrgt
      481 vpggtpcdss sgtcfckrlv tgdgcdrclp ghwglshdll gcrpcdcdvg galdpqcdea
      541 tgqcpcrphm igrrceqvqp gyfrpfldhl tweaegahgq vlevverlvt nretpswtgv
      601 gfvrlregqe veflvtslpr amdydlllrw epqvpeqwae lelvvqrpgp vsahspcghv
      661 lprddriqgm lhpntrvlvf prpvclepgl syklklkltg tggrahpetp ysgsgilids
      721 lvlqphvlml emfsggdaaa lerrttfery rcheeglmps ktplseacvp llisasslvy
      781 ngalpcqcdp qgslssecnp hggqcrckpg vvgrrcdaca tgyygfgpag cqacqcspdg
      841 alsalcegts gqclcrtgaf glrcdhcqrg qwgfpncrpc vcngradecd ahtgaclgcr
      901 dytggehcer ciagfhgdpr lpyggqcrpc pcpegpgsqr hfatschrdg ysqqivchcr
      961 agytglrcea capghfgdps kpggrcqlce csgnidptdp gacdphtgqc lrclhhtegp
     1021 hcghckpgfh gqaarqschr ctcnllgtdp qrcpstdlch cdpstgqcpc lphvqglscd
     1081 rcapnfwnft sgrgcqpcac hpsrargptc neftgqchch agfggrtcse cqelhwgdpg
     1141 lqcracdcdp rgidkpqchr stghcscrpg vsgvrcdqca rgfsgvfpac hpchacfgdw
     1201 drvvqdlaar trrleqwaqe lqqtgvlgaf essflnlqgk lgmvqaivaa rntsaastak
     1261 lveateglrh eigktterlt qleaeltdvq denfnanhal sglerdglal nltlrqldqh
     1321 ldilkhsnfl gaydsirhah sqsteaerra nastfaipsp vsnsadtrrr aevlmgaqre
     1381 nfnrqhlanq qalgrlstht htlsltgvne lvcgapgdap catspcggag crdedgqprc
     1441 gglgcsgaaa tadlalgrar htqaelqral vegggilsrv setrrqaeea qqraqaaldk
     1501 anasrgqveq anqelreliq nvkdflsqeg adpdsiemva trvldisipa speqiqrlas
     1561 eiaervrsla dvdtilahtm gdvrraeqll qdaqrarsra egerqkaetv qaaleeaqra
     1621 qgaaqgairg avvdtknteq tlqqvqerma gteqslnsas erarqlhall ealklkragn
     1681 slaastaeet agsaqsrare aekqlreqvg dqyqtvrala erkaegvlaa qaraeqlrde
     1741 argllqaaqd klqrlqeleg tyeenerele vkaaqldgle armrsvlqai nlqvqiyntc
     1801 q
//
LOCUS       NP_036938                426 aa            linear   ROD 28-APR-2025
DEFINITION  mitogen-activated protein kinase 10 isoform 2 [Rattus norvegicus].
ACCESSION   NP_036938
VERSION     NP_036938.2
DBSOURCE    REFSEQ: accession NM_012806.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Gonzalez-Vazquez,A., Raftery,R.M., Gunbay,S., Chen,G., Murray,D.J.
            and O'Brien,F.J.
  TITLE     Accelerating bone healing in vivo by harnessing the age-altered
            activation of c-Jun N-terminal kinase 3
  JOURNAL   Biomaterials 268, 120540 (2021)
   PUBMED   33307368
  REMARK    GeneRIF: Accelerating bone healing in vivo by harnessing the
            age-altered activation of c-Jun N-terminal kinase 3.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Tenenbaum,M., Plaisance,V., Boutry,R., Pawlowski,V., Jacovetti,C.,
            Sanchez-Parra,C., Ezanno,H., Bourry,J., Beeler,N., Pasquetti,G.,
            Gmyr,V., Dalle,S., Kerr-Conte,J., Pattou,F., Hirai,S.I.,
            Regazzi,R., Bonnefond,A., Froguel,P. and Abderrahmani,A.
  TITLE     The Map3k12 (Dlk)/JNK3 signaling pathway is required for pancreatic
            beta-cell proliferation during postnatal development
  JOURNAL   Cell Mol Life Sci 78 (1), 287-298 (2021)
   PUBMED   32189007
  REMARK    GeneRIF: The Map3k12 (Dlk)/JNK3 signaling pathway is required for
            pancreatic beta-cell proliferation during postnatal development.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Wei,X., Gong,J., Ma,J., Zhang,T., Li,Y., Lan,T., Guo,P. and Qi,S.
  TITLE     Targeting the Dvl-1/beta-arrestin2/JNK3 interaction disrupts
            Wnt5a-JNK3 signaling and protects hippocampal CA1 neurons during
            cerebral ischemia reperfusion
  JOURNAL   Neuropharmacology 135, 11-21 (2018)
   PUBMED   29510185
  REMARK    GeneRIF: results indicate that Wnt5a-mediated JNK3 activation
            participates in Ischemia/Reperfusion brain injury by targeting the
            Dvl-1-beta-arrestin2/JNK3 interaction
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Tonges,L., Planchamp,V., Koch,J.C., Herdegen,T., Bahr,M. and
            Lingor,P.
  TITLE     JNK isoforms differentially regulate neurite growth and
            regeneration in dopaminergic neurons in vitro
  JOURNAL   J Mol Neurosci 45 (2), 284-293 (2011)
   PUBMED   21468718
  REMARK    GeneRIF: Data suggest that JNK isoforms are involved in
            differential regulation of neuronal death and regeneration, and
            that JNK3 appears to be required for regeneration and survival in
            the case of an environment permissive for regeneration.
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Kieran,M.W., Katz,S., Vail,B., Zon,L.I. and Mayer,B.J.
  TITLE     Concentration-dependent positive and negative regulation of a MAP
            kinase by a MAP kinase kinase
  JOURNAL   Oncogene 18 (48), 6647-6657 (1999)
   PUBMED   10597270
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Butterfield,L., Zentrich,E., Beekman,A. and Heasley,L.E.
  TITLE     Stress- and cell type-dependent regulation of transfected c-Jun
            N-terminal kinase and mitogen-activated protein kinase kinase
            isoforms
  JOURNAL   Biochem J 338 (Pt 3) (Pt 3), 681-686 (1999)
   PUBMED   10051439
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Yang,D.D., Kuan,C.Y., Whitmarsh,A.J., Rincon,M., Zheng,T.S.,
            Davis,R.J., Rakic,P. and Flavell,R.A.
  TITLE     Absence of excitotoxicity-induced apoptosis in the hippocampus of
            mice lacking the Jnk3 gene
  JOURNAL   Nature 389 (6653), 865-870 (1997)
   PUBMED   9349820
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Kyriakis,J.M., Banerjee,P., Nikolakaki,E., Dai,T., Rubie,E.A.,
            Ahmad,M.F., Avruch,J. and Woodgett,J.R.
  TITLE     The stress-activated protein kinase subfamily of c-Jun kinases
  JOURNAL   Nature 369 (6476), 156-160 (1994)
   PUBMED   8177321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FQ084081.1, L27128.1,
            FQ211777.1 and FQ083521.1.
            
            On Jul 18, 2012 this sequence version replaced NP_036938.1.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as integration points for multiple
            biochemical signals, and thus are involved in a wide variety of
            cellular processes, such as proliferation, differentiation,
            transcription regulation and development. This kinase is
            specifically expressed in a subset of neurons in the nervous system
            and is activated by threonine and tyrosine phosphorylation.
            Targeted deletion of this gene in mice suggests that it may have a
            role in stress-induced neuronal apoptosis. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. A recent study provided evidence for translational
            readthrough in this gene, and expression of an additional
            C-terminally extended isoform via the use of an alternative
            in-frame translation termination codon. [provided by RefSeq, Dec
            2017].
            
            Transcript Variant: This variant (2) uses an alternate acceptor
            splice site in the 5' region, which results in translation
            initiation from an in-frame, downstream start codon compared to
            variant 1. The encoded isoform (2, also known as SAPK beta) has a
            shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: FQ211777.1, L27128.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA5760383, SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..426
                     /product="mitogen-activated protein kinase 10 isoform 2"
                     /EC_number="2.7.11.24"
                     /note="p54-beta; SAPK-beta; c-Jun N-terminal kinase 3;
                     stress-activated protein kinase JNK3; MAPK 10; MAP kinase
                     10; Stress activated protein kinase beta"
                     /calculated_mol_wt=47997
     Region          25..360
                     /region_name="STKc_JNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     c-Jun N-terminal Kinase; cd07850"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,72,86,108..114,116..117,151,153,
                     155..156,158,168..169,172,183,185..188,190,227)
                     /site_type="active"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,86,108..114,158,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270840"
     Site            order(72,116,151,153,172,183,185..188,190,227)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270840"
     Site            order(112,118,127,130,159..163,323..324,326,329)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:270840"
     Site            order(168..178,182..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270840"
     CDS             1..426
                     /gene="Mapk10"
                     /gene_synonym="Jnk3; SAPb; SAPKC; Serk2"
                     /coded_by="NM_012806.2:654..1934"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25272"
                     /db_xref="RGD:3663"
ORIGIN      
        1 mskskvdnqf ysvevgdstf tvlkryqnlk pigsgaqgiv caaydavldr nvaikklsrp
       61 fqnqthakra yrelvlmkcv nhkniislln vftpqktlee fqdvylvmel mdanlcqviq
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartagtsf
      181 mmtpyvvtry yrapevilgm gykenvdiws vgcimgemvr hkilfpgrdy idqwnkvieq
      241 lgtpcpefmk klqptvrnyv enrpkyaglt fpklfpdslf padsehnklk asqardllsk
      301 mlvidpakri svddalqhpy invwydpaev eapppqiydk qlderehtie ewkeliykev
      361 mnseektkng vvkgqpspsg aavnsseslp psssvndiss mstdqtlasd tdssleasag
      421 plgccr
//
LOCUS       NP_001073169             622 aa            linear   ROD 28-APR-2025
DEFINITION  cilia- and flagella-associated protein 206 [Rattus norvegicus].
ACCESSION   NP_001073169 XP_001062641 XP_001065205 XP_345516
VERSION     NP_001073169.1
DBSOURCE    REFSEQ: accession NM_001079701.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Gibbs,R.A., Weinstock,G.M., Metzker,M.L., Muzny,D.M.,
            Sodergren,E.J., Scherer,S., Scott,G., Steffen,D., Worley,K.C.,
            Burch,P.E., Okwuonu,G., Hines,S., Lewis,L., DeRamo,C., Delgado,O.,
            Dugan-Rocha,S., Miner,G., Morgan,M., Hawes,A., Gill,R., Celera,
            Holt,R.A., Adams,M.D., Amanatides,P.G., Baden-Tillson,H.,
            Barnstead,M., Chin,S., Evans,C.A., Ferriera,S., Fosler,C.,
            Glodek,A., Gu,Z., Jennings,D., Kraft,C.L., Nguyen,T.,
            Pfannkoch,C.M., Sitter,C., Sutton,G.G., Venter,J.C., Woodage,T.,
            Smith,D., Lee,H.M., Gustafson,E., Cahill,P., Kana,A.,
            Doucette-Stamm,L., Weinstock,K., Fechtel,K., Weiss,R.B., Dunn,D.M.,
            Green,E.D., Blakesley,R.W., Bouffard,G.G., De Jong,P.J.,
            Osoegawa,K., Zhu,B., Marra,M., Schein,J., Bosdet,I., Fjell,C.,
            Jones,S., Krzywinski,M., Mathewson,C., Siddiqui,A., Wye,N.,
            McPherson,J., Zhao,S., Fraser,C.M., Shetty,J., Shatsman,S.,
            Geer,K., Chen,Y., Abramzon,S., Nierman,W.C., Havlak,P.H., Chen,R.,
            Durbin,K.J., Simons,R., Ren,Y., Song,X.Z., Li,B., Liu,Y., Qin,X.,
            Cawley,S., Worley,K.C., Cooney,A.J., D'Souza,L.M., Martin,K.,
            Wu,J.Q., Gonzalez-Garay,M.L., Jackson,A.R., Kalafus,K.J.,
            McLeod,M.P., Milosavljevic,A., Virk,D., Volkov,A., Wheeler,D.A.,
            Zhang,Z., Bailey,J.A., Eichler,E.E., Tuzun,E., Birney,E.,
            Mongin,E., Ureta-Vidal,A., Woodwark,C., Zdobnov,E., Bork,P.,
            Suyama,M., Torrents,D., Alexandersson,M., Trask,B.J., Young,J.M.,
            Huang,H., Wang,H., Xing,H., Daniels,S., Gietzen,D., Schmidt,J.,
            Stevens,K., Vitt,U., Wingrove,J., Camara,F., Mar Alba,M.,
            Abril,J.F., Guigo,R., Smit,A., Dubchak,I., Rubin,E.M., Couronne,O.,
            Poliakov,A., Hubner,N., Ganten,D., Goesele,C., Hummel,O.,
            Kreitler,T., Lee,Y.A., Monti,J., Schulz,H., Zimdahl,H.,
            Himmelbauer,H., Lehrach,H., Jacob,H.J., Bromberg,S.,
            Gullings-Handley,J., Jensen-Seaman,M.I., Kwitek,A.E., Lazar,J.,
            Pasko,D., Tonellato,P.J., Twigger,S., Ponting,C.P., Duarte,J.M.,
            Rice,S., Goodstadt,L., Beatson,S.A., Emes,R.D., Winter,E.E.,
            Webber,C., Brandt,P., Nyakatura,G., Adetobi,M., Chiaromonte,F.,
            Elnitski,L., Eswara,P., Hardison,R.C., Hou,M., Kolbe,D., Makova,K.,
            Miller,W., Nekrutenko,A., Riemer,C., Schwartz,S., Taylor,J.,
            Yang,S., Zhang,Y., Lindpaintner,K., Andrews,T.D., Caccamo,M.,
            Clamp,M., Clarke,L., Curwen,V., Durbin,R., Eyras,E., Searle,S.M.,
            Cooper,G.M., Batzoglou,S., Brudno,M., Sidow,A., Stone,E.A.,
            Venter,J.C., Payseur,B.A., Bourque,G., Lopez-Otin,C., Puente,X.S.,
            Chakrabarti,K., Chatterji,S., Dewey,C., Pachter,L., Bray,N.,
            Yap,V.B., Caspi,A., Tesler,G., Pevzner,P.A., Haussler,D.,
            Roskin,K.M., Baertsch,R., Clawson,H., Furey,T.S., Hinrichs,A.S.,
            Karolchik,D., Kent,W.J., Rosenbloom,K.R., Trumbower,H.,
            Weirauch,M., Cooper,D.N., Stenson,P.D., Ma,B., Brent,M.,
            Arumugam,M., Shteynberg,D., Copley,R.R., Taylor,M.S., Riethman,H.,
            Mudunuri,U., Peterson,J., Guyer,M., Felsenfeld,A., Old,S.,
            Mockrin,S. and Collins,F.
  CONSRTM   Rat Genome Sequencing Project Consortium
  TITLE     Genome sequence of the Brown Norway rat yields insights into
            mammalian evolution
  JOURNAL   Nature 428 (6982), 493-521 (2004)
   PUBMED   15057822
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC128759.1.
            
            On or before Dec 10, 2006 this sequence version replaced
            XP_345516.1, XP_001062641.1, XP_001065205.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC128759.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q21"
     Protein         1..622
                     /product="cilia- and flagella-associated protein 206"
                     /note="UPF0704 protein C6orf165 homolog"
                     /calculated_mol_wt=70704
     Region          214..491
                     /region_name="FAP206"
                     /note="Domain of unknown function; pfam12018"
                     /db_xref="CDD:463432"
     CDS             1..622
                     /gene="Cfap206"
                     /gene_synonym="RGD1310641"
                     /coded_by="NM_001079701.1:128..1996"
                     /db_xref="GeneID:366347"
                     /db_xref="RGD:1310641"
ORIGIN      
        1 mpptqaesvi kniireigqe caahgeitse tvvafmvkav vldpsngfnm drtlvktdvq
       61 klvklcvarl ldnknpsldt ikmqvyfdmn ytsredflee hhrvlesrlg ivsreitdtr
      121 acakeelenl yrkivsyvll rsglgsptdi kivreataal qsvfpqaelc tfltlskkdk
      181 erqlkeltmi vtgirlfnrd cgkggegidd lpailleaip atthhidsql qiaqeqafry
      241 taiiekvtnn plmakelqpy mlkealynvr qyeiflqtvl sdiitcaeev elmtkqlaaq
      301 leqlkmtvks ktavptsqvf pifialaslw tsfqdetvli svlsnlttnl elflgthdll
      361 fpekvmqgll dgvivktdmt rieehleekv qladfrvlew lfpettanfn klliqyrgfc
      421 gytfavtdgl llpgnptigi lkykekyytf nsrdaaysfa enpdhyinli kekakknael
      481 iqllelhqqf etlipysqmk dvdkhfikpi tkcengtqtd thilpptivr syewnewelr
      541 rkaiqlanlr qkmthsvqtd lshmrrdnas qvyplkevgt qskregstrv prpqifiagl
      601 rggqsktthg vkinltravd et
//
LOCUS       NP_001094446             722 aa            linear   ROD 28-APR-2025
DEFINITION  pre-B-cell leukemia transcription factor-interacting protein 1
            [Rattus norvegicus].
ACCESSION   NP_001094446 XP_001073314 XP_227420
VERSION     NP_001094446.1
DBSOURCE    REFSEQ: accession NM_001100976.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC129100.1.
            
            On or before Aug 12, 2007 this sequence version replaced
            XP_227420.4, XP_001073314.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129100.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..722
                     /product="pre-B-cell leukemia transcription
                     factor-interacting protein 1"
                     /note="hematopoietic PBX-interacting protein; pre-B-cell
                     leukemia homeobox interacting protein 1"
                     /calculated_mol_wt=80145
     Region          1..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96AQ6; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96AQ6; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96AQ6; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96AQ6; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TVI8; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Region          <268..>442
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          442..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VD12.1)"
     Region          472..>592
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          482..502
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VD12.1)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A2VD12.1)"
     Region          686..711
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VD12.1)"
     Region          691..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A2VD12.1)"
     CDS             1..722
                     /gene="Pbxip1"
                     /coded_by="NM_001100976.1:36..2204"
                     /db_xref="GeneID:310644"
                     /db_xref="RGD:1305180"
ORIGIN      
        1 mascpdsdns wvlagsetlp vetlgpesrv dpeseeapqa lqdsskadgk esagtlngee
       61 mlfqtessqg egaalpeese akgalggddg hgtkrpgdta vqedlqetpm vtslgpdtqd
      121 lernihpqnl psspravwke hgcsssdddt dvdveglrrr rgrepsppqp taavdgedqa
      181 kgegigelgi slnmcflgal vllglgillf sgallepete pveeaelqvf petelvqtvg
      241 nrqdeveqlq asvppdsvps lqsmgllldk lakenqdirl lqaqlqaqke elqsllhqpk
      301 gleeenarlr ealqqgktsh qaleselqql rarlqglean cvrgvdgvcl nwggspqggk
      361 atteqghkgq epdtslleqh kqleaeakal rqelqkqwql lgsvhrnlqr glqdagqgap
      421 ahaglaelgh mlaqtlqgle sqgintgrss ndseawhqkk prfqhprews grekwrggqr
      481 dqkaehwklk keesgqdrkk swrdegreft ghwkenrpra eesgsrkdsk rqdpkvhprk
      541 sgnshsgerq khswgkdnsp dsvsweellr rkyrppqgcs gvadcarqeg lalfgvelap
      601 vrqqelasvl reylarlpwa gqltkelpls payfgedgif rhdrlrfrdf vdaledslee
      661 valkqtgddd evddfedfif shffgdkalk rrskkkekqp wnhravgpre ehsrhphhyh
      721 qg
//
LOCUS       NP_997660                798 aa            linear   ROD 28-APR-2025
DEFINITION  bromodomain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_997660 XP_238186
VERSION     NP_997660.1
DBSOURCE    REFSEQ: accession NM_212495.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Sanchez,R., Meslamani,J. and Zhou,M.M.
  TITLE     The bromodomain: from epigenome reader to druggable target
  JOURNAL   Biochim Biophys Acta 1839 (8), 676-685 (2014)
   PUBMED   24686119
  REMARK    Review article
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Segura,M.F., Fontanals-Cirera,B., Gaziel-Sovran,A., Guijarro,M.V.,
            Hanniford,D., Zhang,G., Gonzalez-Gomez,P., Morante,M., Jubierre,L.,
            Zhang,W., Darvishian,F., Ohlmeyer,M., Osman,I., Zhou,M.M. and
            Hernando,E.
  TITLE     BRD4 sustains melanoma proliferation and represents a new target
            for epigenetic therapy
  JOURNAL   Cancer Res 73 (20), 6264-6276 (2013)
   PUBMED   23950209
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Wang,F., Liu,H., Blanton,W.P., Belkina,A., Lebrasseur,N.K. and
            Denis,G.V.
  TITLE     Brd2 disruption in mice causes severe obesity without Type 2
            diabetes
  JOURNAL   Biochem J 425 (1), 71-83 (2009)
   PUBMED   19883376
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 798)
  AUTHORS   LeRoy,G., Rickards,B. and Flint,S.J.
  TITLE     The double bromodomain proteins Brd2 and Brd3 couple histone
            acetylation to transcription
  JOURNAL   Mol Cell 30 (1), 51-60 (2008)
   PUBMED   18406326
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Lorenz,S., Taylor,K.P., Gehrmann,A., Becker,T., Muhle,H.,
            Gresch,M., Tauer,U., Sander,T. and Stephani,U.
  TITLE     Association of BRD2 polymorphisms with photoparoxysmal response
  JOURNAL   Neurosci Lett 400 (1-2), 135-139 (2006)
   PUBMED   16516380
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Crowley,T., Brunori,M., Rhee,K., Wang,X. and Wolgemuth,D.J.
  TITLE     Change in nuclear-cytoplasmic localization of a double-bromodomain
            protein during proliferation and differentiation of mouse spinal
            cord and dorsal root ganglia
  JOURNAL   Brain Res Dev Brain Res 149 (2), 93-101 (2004)
   PUBMED   15063089
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Greenwald,R.J., Tumang,J.R., Sinha,A., Currier,N., Cardiff,R.D.,
            Rothstein,T.L., Faller,D.V. and Denis,G.V.
  TITLE     E mu-BRD2 transgenic mice develop B-cell lymphoma and leukemia
  JOURNAL   Blood 103 (4), 1475-1484 (2004)
   PUBMED   14563639
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Pal,D.K., Evgrafov,O.V., Tabares,P., Zhang,F., Durner,M. and
            Greenberg,D.A.
  TITLE     BRD2 (RING3) is a probable major susceptibility gene for common
            juvenile myoclonic epilepsy
  JOURNAL   Am J Hum Genet 73 (2), 261-270 (2003)
   PUBMED   12830434
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Crowley,T.E., Kaine,E.M., Yoshida,M., Nandi,A. and Wolgemuth,D.J.
  TITLE     Reproductive cycle regulation of nuclear import, euchromatic
            localization, and association with components of Pol II mediator of
            a mammalian double-bromodomain protein
  JOURNAL   Mol Endocrinol 16 (8), 1727-1737 (2002)
   PUBMED   12145330
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883042.1.
            
            On Aug 30, 2004 this sequence version replaced XP_238186.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..798
                     /product="bromodomain-containing protein 2"
                     /calculated_mol_wt=87920
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P25440; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25440; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25440; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Region          53..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Region          73..179
                     /region_name="Bromo_Brdt_I_like"
                     /note="Bromodomain, Brdt_like subfamily, repeat I. Human
                     Brdt is a testis-specific member of the BET subfamily of
                     bromodomain proteins; the first bromodomain in Brdt has
                     been shown to be essential for male germ cell
                     differentiation. Bromodomains are 110 amino...; cd05497"
                     /db_xref="CDD:99929"
     Site            order(102,109,112,151,155,161)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99929"
     Region          <215..332
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          267..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25440; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25440; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Region          348..449
                     /region_name="Bromo_Brdt_II_like"
                     /note="Bromodomain, Brdt_like subfamily, repeat II. Human
                     Brdt is a testis-specific member of the BET subfamily of
                     bromodomain proteins; the first bromodomain in Brdt has
                     been shown to be essential for male germ cell
                     differentiation. Bromodomains are 110 amino...; cd05498"
                     /db_xref="CDD:99930"
     Site            order(375,382,385,424,428,434)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99930"
     Region          455..648
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Region          553..557
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MGA9.1)"
     Region          639..701
                     /region_name="BET"
                     /note="Bromodomain extra-terminal - transcription
                     regulation; pfam17035"
                     /db_xref="CDD:435704"
     Region          735..798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MGA9.1)"
     CDS             1..798
                     /gene="Brd2"
                     /gene_synonym="Ring3"
                     /coded_by="NM_212495.1:683..3079"
                     /db_xref="GeneID:294276"
                     /db_xref="RGD:1303324"
ORIGIN      
        1 mlqnvtphkl pgegnagllg lgpeaaapgk rirkpsllye gfesptmasv palqlapanp
       61 pppevsnpkk pgrvtnqlqy lhkvvmkalw khqfawpfrq pvdavklglp dyhkiikqpm
      121 dmgtikrrle nnyywaasec mqdfntmftn cyiynkptdd ivlmaqtlek iflqkvasmp
      181 qeeqelvvti pknshkkgak laalqgsits ahqvpavssv shtalytppp eipttvlnip
      241 hpsvisspll kslhsagppl lavsaappaq plakkkgvkr kadtttptpt ailapgspas
      301 ppgslepkaa rlppmrresg rpikpprkdl pdsqqqhqss kkgklseqlk hcngilkell
      361 skkhaayawp fykpvdasal glhdyhdiik hpmdlstvkr kmenrdyrda qefaadvrlm
      421 fsncykynpp dhdvvamark lqdvfefrya kmpdeplepg plpvstalpp glaksssess
      481 seesssesss eeeeeedeed eeeesessds eeerahrlae lqeqlravhe qlaalsqgpi
      541 skpkrkrekk ekkkkrkaek hrgrigided dkgpraprpl qpkkskkagg ggsnattlsh
      601 pgfgtsagss nklpkkaqkt appvlptgyd seeeeesrpm sydekrqlsl dinklpgekl
      661 grvvhiiqar epslrdsnpe eieidfetlk pstlrelery vlsclrkkpr kpytirkpvg
      721 ktkeelalek krelekrlqd vsgqlnstkk ppkkasekte ssaqqvavsr lsasssssds
      781 ssssssssss dtsdsdsg
//
LOCUS       NP_001077093            1333 aa            linear   ROD 28-APR-2025
DEFINITION  sister chromatid cohesion protein PDS5 homolog A [Rattus
            norvegicus].
ACCESSION   NP_001077093 XP_001070956 XP_223406
VERSION     NP_001077093.1
DBSOURCE    REFSEQ: accession NM_001083624.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1333)
  AUTHORS   Hagemann,C., Weigelin,B., Schommer,S., Schulze,M., Al-Jomah,N.,
            Anacker,J., Gerngras,S., Kuhnel,S., Kessler,A.F., Polat,B.,
            Ernestus,R.I., Patel,R. and Vince,G.H.
  TITLE     The cohesin-interacting protein, precocious dissociation of sisters
            5A/sister chromatid cohesion protein 112, is up-regulated in human
            astrocytic tumors
  JOURNAL   Int J Mol Med 27 (1), 39-51 (2011)
   PUBMED   21069257
  REMARK    GeneRIF: Data show that the siRNA-mediated knockdown of Pds5A
            affects sister chromatid cohesion but does not influence mitotic
            checkpoint function or the proliferation and survival of
            glioblastoma multiforme cells.
REFERENCE   2  (residues 1 to 1333)
  AUTHORS   Nishiyama,T., Ladurner,R., Schmitz,J., Kreidl,E., Schleiffer,A.,
            Bhaskara,V., Bando,M., Shirahige,K., Hyman,A.A., Mechtler,K. and
            Peters,J.M.
  TITLE     Sororin mediates sister chromatid cohesion by antagonizing Wapl
  JOURNAL   Cell 143 (5), 737-749 (2010)
   PUBMED   21111234
REFERENCE   3  (residues 1 to 1333)
  AUTHORS   Terret,M.E., Sherwood,R., Rahman,S., Qin,J. and Jallepalli,P.V.
  TITLE     Cohesin acetylation speeds the replication fork
  JOURNAL   Nature 462 (7270), 231-234 (2009)
   PUBMED   19907496
REFERENCE   4  (residues 1 to 1333)
  AUTHORS   Zhang,B., Chang,J., Fu,M., Huang,J., Kashyap,R., Salavaggione,E.,
            Jain,S., Kulkarni,S., Deardorff,M.A., Uzielli,M.L., Dorsett,D.,
            Beebe,D.C., Jay,P.Y., Heuckeroth,R.O., Krantz,I. and Milbrandt,J.
  TITLE     Dosage effects of cohesin regulatory factor PDS5 on mammalian
            development: implications for cohesinopathies
  JOURNAL   PLoS One 4 (5), e5232 (2009)
   PUBMED   19412548
  REMARK    Erratum:[PLoS One. 2009;4(5). doi:
            10.1371/annotation/ea5b7eb5-5087-448a-8325-c8efff1f54d9.
            Shashikant, Kulkarni [corrected to Kulkarni, Shashikant]]
REFERENCE   5  (residues 1 to 1333)
  AUTHORS   Watrin,E., Schleiffer,A., Tanaka,K., Eisenhaber,F., Nasmyth,K. and
            Peters,J.M.
  TITLE     Human Scc4 is required for cohesin binding to chromatin,
            sister-chromatid cohesion, and mitotic progression
  JOURNAL   Curr Biol 16 (9), 863-874 (2006)
   PUBMED   16682347
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EF460313.1.
            
            On or before Apr 1, 2007 this sequence version replaced
            XP_223406.4, XP_001070956.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF460313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p11"
     Protein         1..1333
                     /product="sister chromatid cohesion protein PDS5 homolog
                     A"
                     /note="PDS5, regulator of cohesion maintenance, homolog A"
                     /calculated_mol_wt=150156
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Region          38..1108
                     /region_name="PDS5"
                     /note="Sister chromatid cohesion protein PDS5 protein;
                     pfam20168"
                     /db_xref="CDD:466319"
     Site            order(262..263,266,269..270,299..300,303,306..307,312,
                     340..341,344,347,377..378,381,384..385,415..416)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          282..312
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          322..348
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          359..385
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          392..428
                     /region_name="HEAT. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1096
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Region          1133..1333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1145
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1207
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1210
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1289
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     Site            1304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q29RF7; propagated from
                     UniProtKB/Swiss-Prot (A4L9P7.1)"
     CDS             1..1333
                     /gene="Pds5a"
                     /gene_synonym="RGD1307094; Scc-112"
                     /coded_by="NM_001083624.1:7..4008"
                     /db_xref="GeneID:305343"
                     /db_xref="RGD:1307094"
ORIGIN      
        1 mdftqpkpat alcgvvsadg kiayppgvke itdkittdem ikrlkmvvkt fmdmdqdsed
       61 ekqqylplal hlasefflrn pnkdvrllva ccladifriy apeapytshd klkdiflfit
      121 rqlkgledtk spqfnryfyl lenlawvksy nicfeledcn eifiqlfrtl fsvinnshnk
      181 kvqmhmldlm ssiimegdgv tqelldsili nlipahknln kqsfdlakvl lkrtvqtiea
      241 cianffnqvl vlgrssvsdl sehvfdliqe lfaidphlll svmpqlefkl ksndgeerla
      301 vvrllaklfg skdsdlatqn rplwqcflgr fndihvpvrl esvkfashcl mnhpdlakdl
      361 teylkvrshd peeairhdvi vtiitaakrd lalvndqllg fvrertldkr wrvrkeammg
      421 laqlykkycl hgeagkeaae kvswikdkll hiyyqnsidd kllvekifaq ylvphnlete
      481 ermkclyyly asldpnavka lnemwkcqnm lrshvrelld lhkqptsean csamfgklmt
      541 iaknlpdpgk aqdfvkkfnq vlgddeklrs qlellisptc sckqadicvr eiarklanpk
      601 qptnpflemv kflleriapv hidseaisal vklmnksieg taddeeegvs pdsairsgle
      661 llkvlsfthp tsfhsaetye sllqclrmed dkvaeaaiqi frntghkiet dlpqirstli
      721 pilhqkakrg tphqakqavh cihaifsnke vqlaqifepl srslnadvpe qlitplvslg
      781 hismlapdqf aspmksvvan fivkdllmnd rstgekngkl wspdeevspe vlakvqaikl
      841 lvrwllgmkn nqsksanstl rllsamlvse gdlteqkris ksdmsrlrla agsaimklaq
      901 epcyheiitp eqfqlcalvi ndecyqvrqi faqklhkalv klllpleyma ifalcakdpv
      961 kerraharqc llknisirre yikqnpmate kllsllpeyv vpymihllah dpdftrsqdv
     1021 dqlrdikecl wfmlevlmtk nennshafmk kmaenikltr daqspdeakt neklytvcdv
     1081 alcvinsksa lcnadspkdp vlpmkfftqp ekdfsndksy iseetrvlll tgkpkptgvl
     1141 gtvnkplsat grkpyvrsag tetgsninas selspsagnr sreqssease tgvseneenp
     1201 vriisvtpvk sidtvknkei nsdqstqgni ssdrgkkriv taagaeniqq kpdekadesg
     1261 ppapskprrg rrpksesqgn atknddlskp vskgrkraag sqesleagna kapklqdgak
     1321 kavpaerqid lqr
//
LOCUS       NP_996833                183 aa            linear   ROD 28-APR-2025
DEFINITION  mid1-interacting protein 1 [Rattus norvegicus].
ACCESSION   NP_996833
VERSION     NP_996833.1
DBSOURCE    REFSEQ: accession NM_206950.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Kim,C.W., Moon,Y.A., Park,S.W., Cheng,D., Kwon,H.J. and Horton,J.D.
  TITLE     Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12
            provides a tertiary level of regulation of fatty acid synthesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (21), 9626-9631 (2010)
   PUBMED   20457939
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Aipoalani,D.L., O'Callaghan,B.L., Mashek,D.G., Mariash,C.N. and
            Towle,H.C.
  TITLE     Overlapping roles of the glucose-responsive genes, S14 and S14R, in
            hepatic lipogenesis
  JOURNAL   Endocrinology 151 (5), 2071-2077 (2010)
   PUBMED   20233797
  REMARK    GeneRIF: Data support the hypothesis that both S14 and S14R are
            directly involved in supporting hepatic lipogenesis and that the
            two proteins play overlapping roles in this process.
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Nishi,N., Shoji,H., Miyanaka,H. and Nakamura,T.
  TITLE     Transient up-regulation of a novel member of Spot 14 family in
            androgen-stimulated rat prostate
  JOURNAL   Biochim Biophys Acta 1780 (7-8), 1004-1009 (2008)
   PUBMED   18505691
  REMARK    GeneRIF: Transient up-regulation of slap protein in
            androgen-stimulated prostate is reported.
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Berti,C., Fontanella,B., Ferrentino,R. and Meroni,G.
  TITLE     Mig12, a novel Opitz syndrome gene product partner, is expressed in
            the embryonic ventral midline and co-operates with Mid1 to bundle
            and stabilize microtubules
  JOURNAL   BMC Cell Biol 5, 9 (2004)
   PUBMED   15070402
  REMARK    Publication Status: Online-Only
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061715.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061715.1, EV775988.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132300, SAMD00132308
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq12"
     Protein         1..183
                     /product="mid1-interacting protein 1"
                     /note="MID1 interacting G12-like protein; spot 14-like
                     androgen-inducible protein; protein STRAIT11499 homolog;
                     mid1-interacting G12-like protein; gastrulation-specific
                     G12-like protein; spot 14-R; spot 14-related protein; MID1
                     interacting protein 1 (gastrulation specific G12 homolog)"
                     /calculated_mol_wt=20283
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPA3; propagated from
                     UniProtKB/Swiss-Prot (Q6P7D5.1)"
     Region          3..179
                     /region_name="Spot_14"
                     /note="Thyroid hormone-inducible hepatic protein Spot 14;
                     pfam07084"
                     /db_xref="CDD:462085"
     Region          51..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P7D5.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P7D5.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6P7D5.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NPA3; propagated from
                     UniProtKB/Swiss-Prot (Q6P7D5.1)"
     CDS             1..183
                     /gene="Mid1ip1"
                     /gene_synonym="Mig12; S14R; slap"
                     /coded_by="NM_206950.1:438..989"
                     /db_xref="GeneID:404280"
                     /db_xref="RGD:1303258"
ORIGIN      
        1 mmqicdtynq khslfnamnr figavnnmdq tvmvpsllrd vplsepdldn evsvevggsg
       61 scleerttpa pspgsangsf fapsrdmysh yvllksirnd iewgvlhqps sppagseegt
      121 wkpkdilvgl shlestdage edleqqfhyh lrglhtvlsk ltrkaniltn rykqeigfsn
      181 wgh
//
LOCUS       NP_037322                780 aa            linear   ROD 28-APR-2025
DEFINITION  ATP-dependent 6-phosphofructokinase, liver type [Rattus
            norvegicus].
ACCESSION   NP_037322 XP_001079376
VERSION     NP_037322.1
DBSOURCE    REFSEQ: accession NM_013190.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Yi,W., Clark,P.M., Mason,D.E., Keenan,M.C., Hill,C., Goddard,W.A.
            3rd, Peters,E.C., Driggers,E.M. and Hsieh-Wilson,L.C.
  TITLE     Phosphofructokinase 1 glycosylation regulates cell growth and
            metabolism
  JOURNAL   Science 337 (6097), 975-980 (2012)
   PUBMED   22923583
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Hotta,K., Nakajima,H., Yamasaki,T., Hamaguchi,T., Kuwajima,M.,
            Noguchi,T., Tanaka,T., Kono,N. and Tarui,S.
  TITLE     Rat-liver-type phosphofructokinase mRNA. Structure, tissue
            distribution and regulation
  JOURNAL   Eur J Biochem 202 (2), 293-298 (1991)
   PUBMED   1836995
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Brand,I.A. and Heinickel,A.
  TITLE     Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa
            Zn(2+)-binding protein (parathymosin)
  JOURNAL   J Biol Chem 266 (31), 20984-20989 (1991)
   PUBMED   1834654
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Gekakis,N., Gehnrich,S.C. and Sul,H.S.
  TITLE     Phosphofructokinase isozyme expression during myoblast
            differentiation
  JOURNAL   J Biol Chem 264 (7), 3658-3661 (1989)
   PUBMED   2521854
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Vora,S., Oskam,R. and Staal,G.E.
  TITLE     Isoenzymes of phosphofructokinase in the rat. Demonstration of the
            three non-identical subunits by biochemical, immunochemical and
            kinetic studies
  JOURNAL   Biochem J 229 (2), 333-341 (1985)
   PUBMED   2931076
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Castano,J.G., Nieto,A. and Feliu,J.E.
  TITLE     Inactivation of phosphofructokinase by glucagon in rat hepatocytes
  JOURNAL   J Biol Chem 254 (13), 5576-5579 (1979)
   PUBMED   156182
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X58865.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001079376.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X58865.1, BC061791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..780
                     /product="ATP-dependent 6-phosphofructokinase, liver type"
                     /EC_number="2.7.1.11"
                     /note="phosphofructokinase, liver, B-type;
                     6-phosphofructokinase type B; phosphohexokinase;
                     6-phosphofructokinase, liver type; PFK-B;
                     phosphofructokinase 1; phosphofructo-1-kinase isozyme B"
                     /calculated_mol_wt=85208
     Region          2..390
                     /region_name="N-terminal catalytic PFK domain 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30835.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P17858; propagated from
                     UniProtKB/Swiss-Prot (P30835.3)"
     Region          13..773
                     /region_name="Eukaryotic_PFK"
                     /note="Phosphofructokinase, a key regulatory enzyme in
                     glycolysis, catalyzes the phosphorylation of
                     fructose-6-phosphate to fructose-1,6-biphosphate. The
                     members belong to a subfamily of the PFKA family (cd00363)
                     and include eukaryotic ATP-dependent...; cd00764"
                     /db_xref="CDD:238389"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47857; propagated from
                     UniProtKB/Swiss-Prot (P30835.3)"
     Region          391..400
                     /region_name="Interdomain linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P30835.3)"
     Region          401..780
                     /region_name="C-terminal regulatory PFK domain 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30835.3)"
     Site            529
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P30835.3)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P12382; propagated from
                     UniProtKB/Swiss-Prot (P30835.3)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P30835.3)"
     CDS             1..780
                     /gene="Pfkl"
                     /gene_synonym="ATP-PFK; PFK-L"
                     /coded_by="NM_013190.4:67..2409"
                     /db_xref="GeneID:25741"
                     /db_xref="RGD:3311"
ORIGIN      
        1 matvdleklr msgagkaigv ltsggdaqgm naavravtrm giyvgakvfl iyegyeglve
       61 ggenikpanw lsvsniiqlg gtiigsarck afttregrla aaynllqhgi tnlcviggdg
      121 sltganifrn ewgslleelv kegkisesta qnyahlsiag lvgsidndfc gtdmtigtds
      181 alhrimevid aitttaqshq rtfvlevmgr hcgylalvsa lasgadwlfi peappedgwe
      241 nfmcerlget rsrgsrlnii iiaegaidrh gkpisssyvk dlvvqrlgfd trvtvlghvq
      301 rggtpsafdr vlsskmgmea vmalleatpd tpacvvslsg nqsvrlplme cvqvtkdvqk
      361 amdekrfdea iqlrgrsfen nwkiykllah qkvskeksnf slailnvgap aagmnaavrs
      421 avrtgisegh tvyvvhdgfe glakgqvqev gwhdvagwlg rggsmlgtkr tlpkphleai
      481 venlrtynih allviggfea yegvlqlvea rgryeelciv mcvipatisn nvpgtdfslg
      541 sdtavnaame scdrikqsas gtkrrvfive tmggycgyla tvtgiavgad aayvfedpfn
      601 ihdlkanveh mtekmktdiq rglvlrnekc hehyttefly nlyssegrgv fdcrtnvlgh
      661 lqqggaptpf drnygtklgv kamlwmsekl rdvyrkgrvf anapdsacvi glrkkvvafs
      721 svtelkketd fehrmpreqw wlnlrlmlkm lahyrismad yvsgelehvt rrtlsidkgf
//
LOCUS       NP_001099379            1325 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 42 [Rattus norvegicus].
ACCESSION   NP_001099379 XP_001072044 XP_237865
VERSION     NP_001099379.1
DBSOURCE    REFSEQ: accession NM_001105909.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1325)
  AUTHORS   Kim,Y.K., Kim,Y.S., Yoo,K.J., Lee,H.J., Lee,D.R., Yeo,C.Y. and
            Baek,K.H.
  TITLE     The expression of Usp42 during embryogenesis and spermatogenesis in
            mouse
  JOURNAL   Gene Expr Patterns 7 (1-2), 143-148 (2007)
   PUBMED   16904385
REFERENCE   2  (residues 1 to 1325)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474012.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_001072044.1, XP_237865.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132263,
                              SAMD00132272 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1325
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..1325
                     /product="ubiquitin carboxyl-terminal hydrolase 42"
                     /EC_number="3.4.19.12"
                     /note="deubiquitinating enzyme 42; ubiquitin thiolesterase
                     42; ubiquitin-specific-processing protease 42; ubiquitin
                     specific protease 42; ubiquitin thioesterase 42"
                     /calculated_mol_wt=146227
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          64..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H9J4; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          109..409
                     /region_name="Peptidase_C19E"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02661"
                     /db_xref="CDD:239126"
     Site            order(114,119,370,387)
                     /site_type="active"
                     /db_xref="CDD:239126"
     Region          416..502
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H9J4; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          539..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          567..952
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          602..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          718..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          802..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            858
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H9J4; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          879..1032
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          1146..1259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            1190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H9J4; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            1228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            1231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            1235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H9J4; propagated from
                     UniProtKB/Swiss-Prot (D3ZU96.1)"
     Region          1290..1325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZU96.1)"
     CDS             1..1325
                     /gene="Usp42"
                     /coded_by="NM_001105909.1:1..3978"
                     /db_xref="GeneID:288482"
                     /db_xref="RGD:1305231"
ORIGIN      
        1 mtivdkteps dpstcqnqpg sseavspedm dtgsaswgav ssisdvsnht lslgpvpgav
       61 vynnssvpek skpsppkdqv lgdgiappqk vlfpsekicl kwqqshrvga glqnlgntcf
      121 anaalqclty tpplanymls hehsktchae gfcmmctmqt hitqalsnpg dvikpmfvin
      181 emrriarhfr fgnqedahef lqytvdamqk aclngsnkld rhtqattlvc qifggylrsr
      241 vkclnckgvs dtfdpyldit leikaaqsvt kaleqfvkpe qldgensykc skckkmvpas
      301 krftihrssn vltislkrfa nftggkiakd vkypeyldir pymsqpngep iiyvlyavlv
      361 htgfnchagh yfcyikasng lwyqmndsiv stsdirsvln qqayvlfyir shdvkngget
      421 thpahspgqs sprpgisqrv vnskqaapgf igpqlpphvm kntphlngtt pvkdtpsssv
      481 sspngntsvn raspatasts vqnwsvnrps vipehpkkqk itisihnklp vrqgqaqlnn
      541 nlhgpcleap skaapsstit npsaiqstsn apttsvspse scpkpmvngk akvgssvlvp
      601 ygaesseesd eeskglaken gvdmmtstqs srpetadedg easphelqes vmlngansad
      661 sdsresslaf dsascqvqpd lhtenlfnkl nglpgkvtpa plqsvpedki letfkltnqa
      721 kgpaveeswt ttggsspras vsqpepitde tspleipeav tngsmktpst tspleptisc
      781 tkedssvvvv saepmevlps vpalcnstgt tlgdapvpes cdpgdltanp sqpsqavkgd
      841 paensenstl aevverlspa psvltgdgce qklflylste gseeaedssr ssavsadtvp
      901 pqpdrttssc agaaeqaagd rgdggsvgpk aqepspakek mnslrkvdrg hyrsrrdrss
      961 sgehvrdsra rpedhhhkkr rcysrerpkq erhpantycn ggqhlghgdr asperrslsr
     1021 yshhhsrvrs gleqdwsryh hsenepawar erfypdkmrw dkcryyhdry tttlytarea
     1081 arewrplhgr eherlvqsgr phkdsywgrk gwdlqsrgke rphfhsprea pglavplerh
     1141 lqekaalsvq dsshslperf hehesvklrk rryetldnnd dhpekkvhks lekdaleepr
     1201 akkhkkskkk kkskdkhrar dsrhqqesdf sgaysdadlh rhrkkkkkkk rhsrksedfi
     1261 kdvemhlpkl ssyeavghfr rtegtfllad glpvedsgpf rektkhlrme srpdrchlse
     1321 ygqgn
//
LOCUS       NP_001100041             406 aa            linear   ROD 28-APR-2025
DEFINITION  LIM/homeobox protein Lhx2 [Rattus norvegicus].
ACCESSION   NP_001100041 XP_001054855 XP_216050
VERSION     NP_001100041.1
DBSOURCE    REFSEQ: accession NM_001106571.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Cao,M., Zhao,J., Du,L., Chen,Z., Zhang,L., Liu,X., Cheng,J.,
            Yan,Y., Zhang,C. and Li,H.
  TITLE     The combination of hair follicle-specific marker LHX2 and
            co-expressed marker can distinguish between sweat gland placodes
            and hair placodes in rat
  JOURNAL   J Mol Histol 52 (6), 1225-1232 (2021)
   PUBMED   34581932
  REMARK    GeneRIF: The combination of hair follicle-specific marker LHX2 and
            co-expressed marker can distinguish between sweat gland placodes
            and hair placodes in rat.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Muralidharan,B., Khatri,Z., Maheshwari,U., Gupta,R., Roy,B.,
            Pradhan,S.J., Karmodiya,K., Padmanabhan,H., Shetty,A.S., Balaji,C.,
            Kolthur-Seetharam,U., Macklis,J.D., Galande,S. and Tole,S.
  TITLE     LHX2 Interacts with the NuRD Complex and Regulates Cortical Neuron
            Subtype Determinants Fezf2 and Sox11
  JOURNAL   J Neurosci 37 (1), 194-203 (2017)
   PUBMED   28053041
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hsu,L.C., Nam,S., Cui,Y., Chang,C.P., Wang,C.F., Kuo,H.C.,
            Touboul,J.D. and Chou,S.J.
  TITLE     Lhx2 regulates the timing of beta-catenin-dependent cortical
            neurogenesis
  JOURNAL   Proc Natl Acad Sci U S A 112 (39), 12199-12204 (2015)
   PUBMED   26371318
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Folgueras,A.R., Guo,X., Pasolli,H.A., Stokes,N., Polak,L., Zheng,D.
            and Fuchs,E.
  TITLE     Architectural niche organization by LHX2 is linked to hair follicle
            stem cell function
  JOURNAL   Cell Stem Cell 13 (3), 314-327 (2013)
   PUBMED   24012369
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Honda,S., Kozako,T., Shimeno,H., Soeda,S. and Harada,N.
  TITLE     LIM-homeodomain transcription factor, Lhx2, is involved in
            transcriptional control of brain-specific promoter/exon 1f of the
            mouse aromatase gene
  JOURNAL   J Neuroendocrinol 24 (11), 1367-1374 (2012)
   PUBMED   22734700
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Bach,I., Rodriguez-Esteban,C., Carriere,C., Bhushan,A., Krones,A.,
            Rose,D.W., Glass,C.K., Andersen,B., Izpisua Belmonte,J.C. and
            Rosenfeld,M.G.
  TITLE     RLIM inhibits functional activity of LIM homeodomain transcription
            factors via recruitment of the histone deacetylase complex
  JOURNAL   Nat Genet 22 (4), 394-399 (1999)
   PUBMED   10431247
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Bendall,A.J., Rincon-Limas,D.E., Botas,J. and Abate-Shen,C.
  TITLE     Protein complex formation between Msx1 and Lhx2 homeoproteins is
            incompatible with DNA binding activity
  JOURNAL   Differentiation 63 (3), 151-157 (1998)
   PUBMED   9697309
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Porter,F.D., Drago,J., Xu,Y., Cheema,S.S., Wassif,C., Huang,S.P.,
            Lee,E., Grinberg,A., Massalas,J.S., Bodine,D., Alt,F. and
            Westphal,H.
  TITLE     Lhx2, a LIM homeobox gene, is required for eye, forebrain, and
            definitive erythrocyte development
  JOURNAL   Development 124 (15), 2935-2944 (1997)
   PUBMED   9247336
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Roberson,M.S., Schoderbek,W.E., Tremml,G. and Maurer,R.A.
  TITLE     Activation of the glycoprotein hormone alpha-subunit promoter by a
            LIM-homeodomain transcription factor
  JOURNAL   Mol Cell Biol 14 (5), 2985-2993 (1994)
   PUBMED   7513049
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Xu,Y., Baldassare,M., Fisher,P., Rathbun,G., Oltz,E.M.,
            Yancopoulos,G.D., Jessell,T.M. and Alt,F.W.
  TITLE     LH-2: a LIM/homeodomain gene expressed in developing lymphocytes
            and neural cells
  JOURNAL   Proc Natl Acad Sci U S A 90 (1), 227-231 (1993)
   PUBMED   7678338
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473983.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001054855.1, XP_216050.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132265 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..406
                     /product="LIM/homeobox protein Lhx2"
                     /note="LIM homeobox protein 2; homeobox protein LH-2"
                     /calculated_mol_wt=44288
     Region          43..106
                     /region_name="LIM1_Lhx2"
                     /note="The first LIM domain of Lhx2; cd09469"
                     /db_xref="CDD:188853"
     Site            order(53,56,74,77,80,83,102,105)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188853"
     Region          111..169
                     /region_name="LIM2_Lhx2_Lhx9"
                     /note="The second LIM domain of Lhx2 and Lhx9 family;
                     cd09377"
                     /db_xref="CDD:188763"
     Site            order(115,118,137,140,143,146,165,168)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188763"
     Region          <247..378
                     /region_name="COG5576"
                     /note="Homeodomain-containing transcription factor
                     [Transcription]"
                     /db_xref="CDD:227863"
     Region          267..323
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..406
                     /gene="Lhx2"
                     /gene_synonym="Lh-2; LH2A"
                     /coded_by="NM_001106571.1:60..1280"
                     /db_xref="GeneID:296706"
                     /db_xref="RGD:71076"
ORIGIN      
        1 mlfhslsgpe vhgvidemdr rakseapais saidrgdtet tmpsissdra alcagcggki
       61 sdryyllavd kqwhmrclkc cecklnlese ltcfskdgsi yckedyyrrf svqrcarchl
      121 gisasemvmr ardlvyhlnc ftcttcnkml ttgdhfgmkd slvycrlhfe allqgeypah
      181 fnhadvaaaa aaaaaaksag lgsaganplg lpyyngvgtv qkgrprkrks pgpgadlaay
      241 naalscnend aehldrdqpy pssqktkrmr tsfkhhqlrt mksyfainhn pdakdlkqla
      301 qktgltkrvl qvwfqnarak frrnllrqen tgvdktsdat lqtgtpsgpa selsnaslsp
      361 sstpttltdl tsptlptvts vltsvpgnle ghephspsqt tltnlf
//
LOCUS       NP_001119844             832 aa            linear   ROD 28-APR-2025
DEFINITION  cytosolic carboxypeptidase-like protein 5 [Rattus norvegicus].
ACCESSION   NP_001119844 XP_001064958 XP_001065011 XP_001065062 XP_001065119
            XP_001065177
VERSION     NP_001119844.1
DBSOURCE    REFSEQ: accession NM_001126372.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Xia,P., Ye,B., Wang,S., Zhu,X., Du,Y., Xiong,Z., Tian,Y. and Fan,Z.
  TITLE     Glutamylation of the DNA sensor cGAS regulates its binding and
            synthase activity in antiviral immunity
  JOURNAL   Nat Immunol 17 (4), 369-378 (2016)
   PUBMED   26829768
  REMARK    Erratum:[Nat Immunol. 2016 Apr;17(4):469. doi: 10.1038/ni0416-469e.
            PMID: 27002845]
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Tort,O., Tanco,S., Rocha,C., Bieche,I., Seixas,C., Bosc,C.,
            Andrieux,A., Moutin,M.J., Aviles,F.X., Lorenzo,J. and Janke,C.
  TITLE     The cytosolic carboxypeptidases CCP2 and CCP3 catalyze
            posttranslational removal of acidic amino acids
  JOURNAL   Mol Biol Cell 25 (19), 3017-3027 (2014)
   PUBMED   25103237
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Rodriguez de la Vega Otazo,M., Lorenzo,J., Tort,O., Aviles,F.X. and
            Bautista,J.M.
  TITLE     Functional segregation and emerging role of cilia-related cytosolic
            carboxypeptidases (CCPs)
  JOURNAL   FASEB J 27 (2), 424-431 (2013)
   PUBMED   23085998
REFERENCE   4  (residues 1 to 832)
  AUTHORS   Rogowski,K., van Dijk,J., Magiera,M.M., Bosc,C., Deloulme,J.C.,
            Bosson,A., Peris,L., Gold,N.D., Lacroix,B., Bosch Grau,M., Bec,N.,
            Larroque,C., Desagher,S., Holzer,M., Andrieux,A., Moutin,M.J. and
            Janke,C.
  TITLE     A family of protein-deglutamylating enzymes associated with
            neurodegeneration
  JOURNAL   Cell 143 (4), 564-578 (2010)
   PUBMED   21074048
REFERENCE   5  (residues 1 to 832)
  AUTHORS   Kimura,Y., Kurabe,N., Ikegami,K., Tsutsumi,K., Konishi,Y.,
            Kaplan,O.I., Kunitomo,H., Iino,Y., Blacque,O.E. and Setou,M.
  TITLE     Identification of tubulin deglutamylase among Caenorhabditis
            elegans and mammalian cytosolic carboxypeptidases (CCPs)
  JOURNAL   J Biol Chem 285 (30), 22936-22941 (2010)
   PUBMED   20519502
REFERENCE   6  (residues 1 to 832)
  AUTHORS   Kalinina,E., Biswas,R., Berezniuk,I., Hermoso,A., Aviles,F.X. and
            Fricker,L.D.
  TITLE     A novel subfamily of mouse cytosolic carboxypeptidases
  JOURNAL   FASEB J 21 (3), 836-850 (2007)
   PUBMED   17244818
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC166490.1.
            
            On or before May 8, 2008 this sequence version replaced
            XP_001065062.1, XP_001065177.1, XP_001064958.1, XP_001065119.1,
            XP_001065011.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC166490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q14"
     Protein         1..832
                     /product="cytosolic carboxypeptidase-like protein 5"
                     /EC_number="3.4.17.24"
                     /note="ATP/GTP binding protein-like 5; protein
                     deglutamylase CCP5"
                     /calculated_mol_wt=92423
     Region          10..155
                     /region_name="Pepdidase_M14_N"
                     /note="Cytosolic carboxypeptidase N-terminal domain;
                     pfam18027"
                     /db_xref="CDD:407865"
     Region          27..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV17.1)"
     Region          183..575
                     /region_name="M14_AGBL5_like"
                     /note="Peptidase M14-like domain of ATP/GTP binding
                     protein (AGBL)-5 and related proteins; cd06236"
                     /db_xref="CDD:349455"
     Site            order(252,255,303,312..313,435..436,445,517)
                     /site_type="active"
                     /db_xref="CDD:349455"
     Region          343..362
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV17.1)"
     Region          376..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV17.1)"
     Region          606..752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2GV17.1)"
     CDS             1..832
                     /gene="Agbl5"
                     /coded_by="NM_001126372.1:571..3069"
                     /db_xref="GeneID:362710"
                     /db_xref="RGD:1598311"
ORIGIN      
        1 melrcggllf ssrfdsgnla hvekvetvps dgegvggaat aptsgsassp dyefnvwtrp
       61 dcaeteyeng nrswfyfsvr ggtpgkliki nimnmnkqsk lysqgmapfv rtlpsrprwe
      121 rirerptfem tetqfvlsfv hrfvegrgat tffafcypfs ysdcqdllsq ldqrfpenys
      181 ahsspldsiy yhrellcysl dglrvdllti tschglrddr eprleqlfpd vgtprpfrft
      241 gkrifflssr vhpgetpssf vfngfldfil rpddpraqtl rrlfvfklip mlnpdgvvrg
      301 hyrtdsrgvn lnrqylkpda vlhpaiygak avllyhhvhs rlnsknpsnq qpsslhlppe
      361 vplsdlekan nlhnelhlgq spdgenhdrw tetepteekt dpvwimpqpi peleepapda
      421 ippkesgvay yvdlhghask rgcfmygnsf sdestqvenm lypklislns ahfdfqgcnf
      481 seknmyardr rdgqskegsg rvaiykasgi ihsytlecny ntgrsvnsip aachdngras
      541 ppppptfpsr ytvelfeqvg ralaiaaldm aecnpwpriv lsehssltnl rawmlkhvrn
      601 srgltstanv glnkkrgsrt ppksnnglpv scsenalsra rsfstgtstg gsssqqnspq
      661 mknspsfpfh gsrpaglpgl gsstqkvshr vlgpvreprc pdrrrrqqqq qqqqqqqqqq
      721 qqqplnqrst tsslapsptl asasptssrn mgscllpnsl slsgsscpfs ssgdkpeavm
      781 vigksllgag aripcirtrl qtcqrrvsar rgpgfprlgp gwagahrrla eg
//
LOCUS       NP_001014255             284 aa            linear   ROD 28-APR-2025
DEFINITION  type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase [Rattus
            norvegicus].
ACCESSION   NP_001014255 XP_344325
VERSION     NP_001014255.1
DBSOURCE    REFSEQ: accession NM_001014233.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Hashimoto,Y., Shirane,M. and Nakayama,K.I.
  TITLE     TMEM55B contributes to lysosomal homeostasis and amino acid-induced
            mTORC1 activation
  JOURNAL   Genes Cells 23 (6), 418-434 (2018)
   PUBMED   29644770
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Morioka,S., Nigorikawa,K., Okada,E., Tanaka,Y., Kasuu,Y.,
            Yamada,M., Kofuji,S., Takasuga,S., Nakanishi,H., Sasaki,T. and
            Hazeki,K.
  TITLE     TMEM55a localizes to macrophage phagosomes to downregulate
            phagocytosis
  JOURNAL   J Cell Sci 131 (5) (2018)
   PUBMED   29378918
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Willett,R., Martina,J.A., Zewe,J.P., Wills,R., Hammond,G.R.V. and
            Puertollano,R.
  TITLE     TFEB regulates lysosomal positioning by modulating TMEM55B
            expression and JIP4 recruitment to lysosomes
  JOURNAL   Nat Commun 8 (1), 1580 (2017)
   PUBMED   29146937
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Medina,M.W., Bauzon,F., Naidoo,D., Theusch,E., Stevens,K.,
            Schilde,J., Schubert,C., Mangravite,L.M., Rudel,L.L., Temel,R.E.,
            Runz,H. and Krauss,R.M.
  TITLE     Transmembrane protein 55B is a novel regulator of cellular
            cholesterol metabolism
  JOURNAL   Arterioscler Thromb Vasc Biol 34 (9), 1917-1923 (2014)
   PUBMED   25035345
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Ungewickell,A., Hugge,C., Kisseleva,M., Chang,S.C., Zou,J.,
            Feng,Y., Galyov,E.E., Wilson,M. and Majerus,P.W.
  TITLE     The identification and characterization of two
            phosphatidylinositol-4,5-bisphosphate 4-phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 102 (52), 18854-18859 (2005)
   PUBMED   16365287
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087604.1.
            
            On Apr 20, 2005 this sequence version replaced XP_344325.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087604.1, EX492614.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p14"
     Protein         1..284
                     /product="type 1 phosphatidylinositol 4,5-bisphosphate
                     4-phosphatase"
                     /EC_number="3.1.3.78"
                     /note="PtdIns-4,5-P(2) 4-phosphatase type I; ptdIns-4,5-P2
                     4-Ptase I; type I phosphatidylinositol 4,5-bisphosphate
                     4-phosphatase; transmembrane protein 55B; transmembrane
                     protein 55B-like; type 1 PtdIns-4,5-P2 4-Ptase"
                     /calculated_mol_wt=29862
     Region          1..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPM8.1)"
     Region          4..277
                     /region_name="Tmemb_55A"
                     /note="Transmembrane protein 55A; pfam09788"
                     /db_xref="CDD:462901"
     Region          140..146
                     /region_name="CX5R motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPM8.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5PPM8.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPM8.1)"
     Site            246..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PPM8.1)"
     CDS             1..284
                     /gene="Pip4p1"
                     /gene_synonym="RGD1307475; Tmem55b"
                     /coded_by="NM_001014233.2:103..957"
                     /db_xref="GeneID:364298"
                     /db_xref="RGD:1307475"
ORIGIN      
        1 maadgerspl lseagdggag gnglagpggs atgpgggltp sappygagkh appqafppfp
       61 eghpavlpge dpppysplts pdsgsapmit crvcqspinv egkmhqhvvk cgvcneatpi
      121 knappgkkyv rcpcncllic kvtsqriacp rpyckriinl gpvhpgplsp epqpmgvrvi
      181 cghckntflw teftdrtlar cphcrkvssi grryprkrci ccfllgllla vtatglafgt
      241 wkpaqqyggi yaawafvill avlclgraly wgcmkvshpv qnfs
//
LOCUS       NP_001029297            1293 aa            linear   ROD 28-APR-2025
DEFINITION  period circadian protein homolog 1 [Rattus norvegicus].
ACCESSION   NP_001029297 XP_340823
VERSION     NP_001029297.1
DBSOURCE    REFSEQ: accession NM_001034125.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1293)
  AUTHORS   Wei,J., Wang,Y., Tu,S., Zhang,S., Feng,Y., Hou,Y., Ai,H. and
            Chen,Z.
  TITLE     Circadian rhythm disruption upregulating Per1 in mandibular
            condylar chondrocytes mediating temporomandibular joint
            osteoarthritis via GSK3beta/beta-CATENIN pathway
  JOURNAL   J Transl Med 22 (1), 662 (2024)
   PUBMED   39010104
  REMARK    GeneRIF: Circadian rhythm disruption upregulating Per1 in
            mandibular condylar chondrocytes mediating temporomandibular joint
            osteoarthritis via GSK3beta/beta-CATENIN pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1293)
  AUTHORS   Wei,J.M., Tu,S.Q., Wang,Y.X., Zhang,S., Feng,Y., Ai,H. and Chen,Z.
  TITLE     Clock gene Per1 regulates rat temporomandibular osteoarthritis
            through NF-kappaB pathway: an in vitro and in vivo study
  JOURNAL   J Orthop Surg Res 18 (1), 817 (2023)
   PUBMED   37907921
  REMARK    GeneRIF: Clock gene Per1 regulates rat temporomandibular
            osteoarthritis through NF-kappaB pathway: an in vitro and in vivo
            study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1293)
  AUTHORS   Jin,W., Tian,Y., Ding,Y., Zhou,D., Li,L., Yuan,M., Wu,Y., Ye,M.,
            Luan,J. and Yang,K.
  TITLE     Pers reverse angiotensin II -induced vascular smooth muscle cell
            proliferation by targeting cyclin E expression via inhibition of
            the MAPK signaling pathway
  JOURNAL   Chronobiol Int 40 (7), 903-917 (2023)
   PUBMED   37338051
  REMARK    GeneRIF: Pers reverse angiotensin II -induced vascular smooth
            muscle cell proliferation by targeting cyclin E expression via
            inhibition of the MAPK signaling pathway.
REFERENCE   4  (residues 1 to 1293)
  AUTHORS   Costello,H.M., Juffre,A., Cheng,K.Y., Bratanatawira,P.,
            Crislip,G.R., Zietara,A., Spires,D.R., Staruschenko,A., Douma,L.G.
            and Gumz,M.L.
  TITLE     The circadian clock protein PER1 is important in maintaining
            endothelin axis regulation in Dahl salt-sensitive rats
  JOURNAL   Can J Physiol Pharmacol 101 (3), 136-146 (2023)
   PUBMED   36450128
  REMARK    GeneRIF: The circadian clock protein PER1 is important in
            maintaining endothelin axis regulation in Dahl salt-sensitive rats.
REFERENCE   5  (residues 1 to 1293)
  AUTHORS   Zietara,A., Spires,D.R., Juffre,A., Costello,H.M., Crislip,G.R.,
            Douma,L.G., Levchenko,V., Dissanayake,L.V., Klemens,C.A.,
            Nikolaienko,O., Geurts,A.M., Gumz,M.L. and Staruschenko,A.
  TITLE     Knockout of the Circadian Clock Protein PER1 (Period1) Exacerbates
            Hypertension and Increases Kidney Injury in Dahl Salt-Sensitive
            Rats
  JOURNAL   Hypertension 79 (11), 2519-2529 (2022)
   PUBMED   36093781
  REMARK    GeneRIF: Knockout of the Circadian Clock Protein PER1 (Period1)
            Exacerbates Hypertension and Increases Kidney Injury in Dahl
            Salt-Sensitive Rats.
REFERENCE   6  (residues 1 to 1293)
  AUTHORS   Takekida,S., Yan,L., Maywood,E.S., Hastings,M.H. and Okamura,H.
  TITLE     Differential adrenergic regulation of the circadian expression of
            the clock genes Period1 and Period2 in the rat pineal gland
  JOURNAL   Eur J Neurosci 12 (12), 4557-4561 (2000)
   PUBMED   11122368
REFERENCE   7  (residues 1 to 1293)
  AUTHORS   Masubuchi,S., Honma,S., Abe,H., Ishizaki,K., Namihira,M., Ikeda,M.
            and Honma,K.
  TITLE     Clock genes outside the suprachiasmatic nucleus involved in
            manifestation of locomotor activity rhythm in rats
  JOURNAL   Eur J Neurosci 12 (12), 4206-4214 (2000)
   PUBMED   11122332
REFERENCE   8  (residues 1 to 1293)
  AUTHORS   Jin,X., Shearman,L.P., Weaver,D.R., Zylka,M.J., de Vries,G.J. and
            Reppert,S.M.
  TITLE     A molecular mechanism regulating rhythmic output from the
            suprachiasmatic circadian clock
  JOURNAL   Cell 96 (1), 57-68 (1999)
   PUBMED   9989497
REFERENCE   9  (residues 1 to 1293)
  AUTHORS   Sangoram,A.M., Saez,L., Antoch,M.P., Gekakis,N., Staknis,D.,
            Whiteley,A., Fruechte,E.M., Vitaterna,M.H., Shimomura,K.,
            King,D.P., Young,M.W., Weitz,C.J. and Takahashi,J.S.
  TITLE     Mammalian circadian autoregulatory loop: a timeless ortholog and
            mPer1 interact and negatively regulate CLOCK-BMAL1-induced
            transcription
  JOURNAL   Neuron 21 (5), 1101-1113 (1998)
   PUBMED   9856465
REFERENCE   10 (residues 1 to 1293)
  AUTHORS   Balsalobre,A., Damiola,F. and Schibler,U.
  TITLE     A serum shock induces circadian gene expression in mammalian tissue
            culture cells
  JOURNAL   Cell 93 (6), 929-937 (1998)
   PUBMED   9635423
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY903229.1.
            
            On Feb 6, 2006 this sequence version replaced XP_340823.2.
            
            Summary: This gene is a member of the Period family of genes and is
            expressed in a circadian pattern in the suprachiasmatic nucleus,
            the primary circadian pacemaker in the mammalian brain. Genes in
            this family encode components of the circadian rhythms of locomotor
            activity, metabolism, and behavior. This gene is upregulated by
            Clock/Arntl heterodimers but then represses this upregulation in a
            feedback loop using Per/Cry heterodimers to interact with
            Clock/Arntl. Polymorphisms in this gene may increase the risk of
            getting certain cancers. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY903229.1, AY903230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1293
                     /organism="Rattus norvegicus"
                     /strain="SHR/OlaIpcv"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1293
                     /product="period circadian protein homolog 1"
                     /note="circadian clock protein PERIOD 1; period 1; period
                     homolog 1; period circadian clock 1"
                     /calculated_mol_wt=136033
     Region          1..151
                     /region_name="Interaction with BTRC.
                     /evidence=ECO:0000250|UniProtKB:O15534"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          1..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CSNK1E. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CSNK1E. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CSNK1E. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          138..147
                     /region_name="Nuclear export signal 1.
                     /evidence=ECO:0000250|UniProtKB:O54943"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          373..457
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(373,377,383,396..399,427,432)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(393,397,405,408..409,439,441)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          489..498
                     /region_name="Nuclear export signal 2.
                     /evidence=ECO:0000250|UniProtKB:O35973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          509..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          596..814
                     /region_name="Required for phosphorylation by CSNK1E.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          647..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35973; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35973; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15534; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          748..771
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          808..870
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15534; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          823..839
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O35973"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          935..1094
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            975
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15534; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O15534; propagated from
                     UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          978..985
                     /region_name="Nuclear export signal 3.
                     /evidence=ECO:0000250|UniProtKB:O54943"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          1039..1043
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          <1079..1198
                     /region_name="Period_C"
                     /note="Period protein 2/3C-terminal region; pfam12114"
                     /db_xref="CDD:463464"
     Region          1145..1293
                     /region_name="CRY binding domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     Region          1204..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CHI5.2)"
     CDS             1..1293
                     /gene="Per1"
                     /gene_synonym="rper1"
                     /coded_by="NM_001034125.1:58..3939"
                     /db_xref="GeneID:287422"
                     /db_xref="RGD:727863"
ORIGIN      
        1 msgplegadg ggdprpgepf cpggvpspga pqhrpcpgps laddtdansn gssgnesngh
       61 esrgasqrss hssssgngkd sallettess kstnsqspsp psssiaysll sasseqdnps
      121 tsgcsseqsa rartqkelmt alrelklrlp perrgkgrsg tlatlqyala cvkqvqanqe
      181 yyqqwsleeg epcamdmsty tleelehits eytlrnqdtf svavsfltgr ivyiseqagv
      241 llrckrdvfr garfsellap qdvgvfygst tpsrlptwgt gtsagsglkd ftqeksvfcr
      301 irggpdrdpg pryqpfrltp yvtkirvsdg apaqpcclli aerihsgyea prippdkrif
      361 ttrhtpsclf qdvderaapl lgylpqdllg apvllflhpe drplmlaihk kilqlagqpf
      421 dhspirfcar ngeyvtmdts wagfvhpwsr kvafvlgrhk vrtaplnedv ftppvpspap
      481 sldsdiqels eqihrlllqp vhsssttglc gvgplmspgp lhspgsssds nggdaegpgp
      541 papvtfqqic kdvhlvkhqg qqlfiesrak ppprprllat gtfkakvlpc qspnpeleva
      601 papdqaslal apeeperkes sgcsyqqinc ldsilryles cnipnttkrk casssctass
      661 asdddkqrag pvpvgakkdt ssavlsgega tprkepvvgg tlsplalank aesvvsvtsq
      721 csfsstivhv gdkkppesdi immedlpgla pgpapspaps ptvapdpapd ayrpvgltka
      781 vlslhtqkee qaflsrfrdl grlrgldtss vapsapgchh gpipsgrrhh crskakrsrh
      841 hqtprpetpc yvshpspvps sgpwppppat tpfpavvqpy plpvfsprgg pqplppapts
      901 vspatfpspl vtpmvalvlp nylfpsptsy pygvsqapve gpptpashsp spslppppps
      961 pphrpdsplf nsrcssplql nllqleespr teggaaaggp gssagplpps eesaepeprl
     1021 vevtessnqd alsgssdlle lllqedsrsg tgsaasgslg sglgsgsgsg sheggstsas
     1081 itrssqssht skyfgsidss eaeagaaqar tepgdqviky vlqdpiwllm anadqhvmmt
     1141 yqvpsrdaas vlkqdrerlr amqkqqprfs edqrrelgav hswvrkgqlp qaldvtacvd
     1201 cgssvqdpgh sddplfseld glglepmeeg ggegggvggg gggvgggggd ggeeaqtqig
     1261 tkgsssqdsa meeeeqggss sspalpaeen gts
//
LOCUS       NP_001029289             448 aa            linear   ROD 28-APR-2025
DEFINITION  beclin-1 [Rattus norvegicus].
ACCESSION   NP_001029289
VERSION     NP_001029289.1
DBSOURCE    REFSEQ: accession NM_001034117.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Zhan,Y., Li,L., Guo,C., Zhang,Y., Zhao,L., Tao,Z., Zhang,H. and
            Chen,S.
  TITLE     MicroRNA-141-3p reduces pulmonary hypoxia/reoxygenation injury
            through suppression of Beclin-1-dependent autophagy
  JOURNAL   Aging (Albany NY) 16 (2), 1352-1373 (2024)
   PUBMED   38261732
  REMARK    GeneRIF: MicroRNA-141-3p reduces pulmonary hypoxia/reoxygenation
            injury through suppression of Beclin-1-dependent autophagy.
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Luo,H., Huang,D., Tang,X., Liu,Y., Luo,Q., Liu,C., Huang,H.,
            Chen,W. and Qi,Z.
  TITLE     Beclin-1 exerts protective effects against cerebral
            ischemia-reperfusion injury by promoting DNA damage repair through
            a non-autophagy-dependent regulatory mechanism
  JOURNAL   Int J Mol Med 49 (5) (2022)
   PUBMED   35266018
  REMARK    GeneRIF: Beclin1 exerts protective effects against cerebral
            ischemiareperfusion injury by promoting DNA damage repair through a
            nonautophagydependent regulatory mechanism.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Kang,H., Chen,J. and Cao,S.
  TITLE     Propofol Regulates the Expression of BecliN-1 through miR-30b and
            Protects against Lung Ischemia-Reperfusion Injury
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 67 (5), 348-355 (2022)
   PUBMED   35818233
  REMARK    GeneRIF: Propofol Regulates the Expression of BecliN-1 through
            miR-30b and Protects against Lung Ischemia-Reperfusion Injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Chen,Y.H., Chiu,W.C., Xiao,Q., Chen,Y.L., Shirakawa,H. and
            Yang,S.C.
  TITLE     Synbiotics Alleviate Hepatic Damage, Intestinal Injury and Muscular
            Beclin-1 Elevation in Rats after Chronic Ethanol Administration
  JOURNAL   Int J Mol Sci 22 (22), 12547 (2021)
   PUBMED   34830430
  REMARK    GeneRIF: Synbiotics Alleviate Hepatic Damage, Intestinal Injury and
            Muscular Beclin-1 Elevation in Rats after Chronic Ethanol
            Administration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Shi,G., Zhang,Z., Ma,S., Li,Y., Du,S., Chu,Y., Li,Y., Tang,X.,
            Yang,Y., Chen,Z., Wang,Z. and Wu,H.
  TITLE     Hepatic interferon regulatory factor 8 expression mediates liver
            ischemia/reperfusion injury in mice
  JOURNAL   Biochem Pharmacol 192, 114728 (2021)
   PUBMED   34400126
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Tanida,I., Ueno,T. and Kominami,E.
  TITLE     LC3 conjugation system in mammalian autophagy
  JOURNAL   Int J Biochem Cell Biol 36 (12), 2503-2518 (2004)
   PUBMED   15325588
  REMARK    Review article
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Yue,Z., Jin,S., Yang,C., Levine,A.J. and Heintz,N.
  TITLE     Beclin 1, an autophagy gene essential for early embryonic
            development, is a haploinsufficient tumor suppressor
  JOURNAL   Proc Natl Acad Sci U S A 100 (25), 15077-15082 (2003)
   PUBMED   14657337
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Yue,Z., Horton,A., Bravin,M., DeJager,P.L., Selimi,F. and Heintz,N.
  TITLE     A novel protein complex linking the delta 2 glutamate receptor and
            autophagy: implications for neurodegeneration in lurcher mice
  JOURNAL   Neuron 35 (5), 921-933 (2002)
   PUBMED   12372286
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Kihara,A., Kabeya,Y., Ohsumi,Y. and Yoshimori,T.
  TITLE     Beclin-phosphatidylinositol 3-kinase complex functions at the
            trans-Golgi network
  JOURNAL   EMBO Rep 2 (4), 330-335 (2001)
   PUBMED   11306555
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Liang,X.H., Kleeman,L.K., Jiang,H.H., Gordon,G., Goldman,J.E.,
            Berry,G., Herman,B. and Levine,B.
  TITLE     Protection against fatal Sindbis virus encephalitis by beclin, a
            novel Bcl-2-interacting protein
  JOURNAL   J Virol 72 (11), 8586-8596 (1998)
   PUBMED   9765397
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK600131.1 and BC074011.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC074011.1, SRR8487227.17539.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..448
                     /product="beclin-1"
                     /note="coiled-coil myosin-like BCL2-interacting protein;
                     beclin 1 (coiled-coil, myosin-like BCL2-interacting
                     protein); beclin 1, autophagy related"
                     /calculated_mol_wt=51426
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Region          47..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O88597; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Region          103..127
                     /region_name="BH3"
                     /note="Beclin-1 BH3 domain, Bcl-2-interacting; pfam15285"
                     /db_xref="CDD:464614"
     Region          106..125
                     /region_name="BH3. /evidence=ECO:0000250|UniProtKB:Q14457"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Region          110..157
                     /region_name="Interaction with BCL2 and BCL2L1 isoform
                     Bcl-X(L). /evidence=ECO:0000250|UniProtKB:Q14457"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q14457; propagated from
                     UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Region          133..259
                     /region_name="APG6_N"
                     /note="Apg6 coiled-coil region; pfam17675"
                     /db_xref="CDD:465452"
     Region          243..448
                     /region_name="Evolutionary conserved domain (ECD).
                     /evidence=ECO:0000250|UniProtKB:Q14457"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XJ1.1)"
     Region          265..443
                     /region_name="APG6"
                     /note="Apg6 BARA domain; pfam04111"
                     /db_xref="CDD:461178"
     Region          423..448
                     /region_name="Required for membrane-association.
                     /evidence=ECO:0000250|UniProtKB:Q14457"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91XJ1.1)"
     CDS             1..448
                     /gene="Becn1"
                     /gene_synonym="Beclin1"
                     /coded_by="NM_001034117.1:203..1549"
                     /db_xref="GeneID:114558"
                     /db_xref="RGD:620190"
ORIGIN      
        1 megskassst mqvsfvcqrc sqplkldtsf kildrvtiqe ltapllttaq akpgesqeee
       61 ansgeepfie trqdgvsrrf ipparmmste sansftlige asdggtmenl srrlkvtgdl
      121 fdimsgqtdv dhplceectd tlldqldtql nvtenecqny krclemleqm negdseqlqr
      181 elkelaleee rliqeledve knrkvvaenl ekvqaeaerl dqeeaqyqre ysefkrqqle
      241 lddelksven qmryaqmqld klkktnvfna tfhiwhsgqf gtinnfrlgr lpsapvewne
      301 inaawgqtvl llhalankmg lkfqryrlvp ygnhsylesl tdkskelply csgglrffwd
      361 nkfdhamvaf ldcvqqfkee vekgetrfcl pyrmdvekgk iedtggsggs ysiktqfnse
      421 eqwtkalkfm ltnlkwglaw vssqfynk
//
LOCUS       NP_997694                259 aa            linear   ROD 28-APR-2025
DEFINITION  (3R)-3-hydroxyacyl-CoA dehydrogenase [Rattus norvegicus].
ACCESSION   NP_997694 XP_342097
VERSION     NP_997694.1
DBSOURCE    REFSEQ: accession NM_212529.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Venkatesan,R., Sah-Teli,S.K., Awoniyi,L.O., Jiang,G., Prus,P.,
            Kastaniotis,A.J., Hiltunen,J.K., Wierenga,R.K. and Chen,Z.
  TITLE     Insights into mitochondrial fatty acid synthesis from the structure
            of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA
            dehydrogenase
  JOURNAL   Nat Commun 5, 4805 (2014)
   PUBMED   25203508
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Chen,Z., Kastaniotis,A.J., Miinalainen,I.J., Rajaram,V.,
            Wierenga,R.K. and Hiltunen,J.K.
  TITLE     17beta-hydroxysteroid dehydrogenase type 8 and carbonyl reductase
            type 4 assemble as a ketoacyl reductase of human mitochondrial FAS
  JOURNAL   FASEB J 23 (11), 3682-3691 (2009)
   PUBMED   19571038
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ohno,S., Nishikawa,K., Honda,Y. and Nakajin,S.
  TITLE     Expression in E. coli and tissue distribution of the human
            homologue of the mouse Ke 6 gene, 17beta-hydroxysteroid
            dehydrogenase type 8
  JOURNAL   Mol Cell Biochem 309 (1-2), 209-215 (2008)
   PUBMED   17978863
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Fomitcheva,J., Baker,M.E., Anderson,E., Lee,G.Y. and Aziz,N.
  TITLE     Characterization of Ke 6, a new 17beta-hydroxysteroid
            dehydrogenase, and its expression in gonadal tissues
  JOURNAL   J Biol Chem 273 (35), 22664-22671 (1998)
   PUBMED   9712896
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Aziz,N., Brown,D., Lee,W.S. and Naray-Fejes-Toth,A.
  TITLE     Aberrant 11beta-hydroxysteroid dehydrogenase-1 activity in the cpk
            mouse: implications for regulation by the Ke 6 gene
  JOURNAL   Endocrinology 137 (12), 5581-5588 (1996)
   PUBMED   8940387
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Walter,L., Fischer,K. and Gunther,E.
  TITLE     Physical mapping of the Ring1, Ring2, Ke6, Ke4, Rxrb, Col11a2, and
            RT1.Hb genes in the rat major histocompatibility complex
  JOURNAL   Immunogenetics 44 (3), 218-221 (1996)
   PUBMED   8662089
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883042.1.
            
            On Aug 30, 2004 this sequence version replaced XP_342097.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..259
                     /product="(3R)-3-hydroxyacyl-CoA dehydrogenase"
                     /EC_number="1.1.1.62"
                     /EC_number="1.1.1.239"
                     /EC_number="1.1.1.n12"
                     /note="estradiol 17-beta-dehydrogenase 8; 17-beta-HSD 8;
                     testosterone 17-beta-dehydrogenase 8;
                     17-beta-hydroxysteroid dehydrogenase 8;
                     3-oxoacyl-[acyl-carrier-protein] reductase; KAR alpha
                     subunit; 3-ketoacyl-[acyl-carrier-protein] reductase alpha
                     subunit"
                     /calculated_mol_wt=26660
     Region          11..258
                     /region_name="BKR_SDR_c"
                     /note="beta-Keto acyl carrier protein reductase (BKR),
                     involved in Type II FAS, classical (c) SDRs; cd05333"
                     /db_xref="CDD:187594"
     Site            order(16,18..21,40..41,72..74,101..104,124,152..154,167,
                     171,197..198,200,202..204)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187594"
     Site            order(28,32,81,108..111,113..115,118..119,122,126..127,
                     130..131,133..134,137..138,141,158..165,168..169,172..173,
                     176..177,179..184,186..187,199,220..222,224..227,230,
                     233..234,236..237,241,244..256,258)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187594"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB5.1)"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P50171; propagated from
                     UniProtKB/Swiss-Prot (Q6MGB5.1)"
     Site            order(109..111,113,115,118..119,122,126..127,130..131,134,
                     137..138,141,157..165,168..169,172..173,176..177,179..181,
                     183..184)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187594"
     Site            order(125,154,167,171)
                     /site_type="active"
                     /db_xref="CDD:187594"
     CDS             1..259
                     /gene="Hsd17b8"
                     /gene_synonym="Fabgl; Ke6; RING2"
                     /coded_by="NM_212529.1:17..796"
                     /db_xref="GeneID:361802"
                     /db_xref="RGD:1303158"
ORIGIN      
        1 masqlrlrsa lalvtgagsg igraisvrla aegaavaacd ldgaaaqdtv rllgnpgsed
       61 reprgkhaaf qadvsegpaa krlleqvqac ffrppsvvvs cagitrdefl lhmseedwdr
      121 viavnlkgtf lvtqaaaqal vssggrgsii nissivgkvg nigqtnyass kagvigltqt
      181 aarelgrhgi rcnsvlpgfi atpmtqkmpe kvkdkvtami plghmgdped vadvvaflas
      241 edsgyitgas vevsgglfm
//
LOCUS       NP_076468               1115 aa            linear   ROD 28-APR-2025
DEFINITION  period circadian protein homolog 3 [Rattus norvegicus].
ACCESSION   NP_076468
VERSION     NP_076468.2
DBSOURCE    REFSEQ: accession NM_023978.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Banach,E., Pawlak,J., Kapelski,P., Szczepankiewicz,A.,
            Rajewska-Rager,A., Skibinska,M., Czerski,P., Twarowska-Hauser,J.
            and Dmitrzak-Weglarz,M.
  TITLE     Clock genes polymorphisms in male bipolar patients with comorbid
            alcohol abuse
  JOURNAL   J Affect Disord 241, 142-146 (2018)
   PUBMED   30121446
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Zhang,L., Hirano,A., Hsu,P.K., Jones,C.R., Sakai,N., Okuro,M.,
            McMahon,T., Yamazaki,M., Xu,Y., Saigoh,N., Saigoh,K., Lin,S.T.,
            Kaasik,K., Nishino,S., Ptacek,L.J. and Fu,Y.H.
  TITLE     A PERIOD3 variant causes a circadian phenotype and is associated
            with a seasonal mood trait
  JOURNAL   Proc Natl Acad Sci U S A 113 (11), E1536-E1544 (2016)
   PUBMED   26903630
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Hasan,S., van der Veen,D.R., Winsky-Sommerer,R., Hogben,A.,
            Laing,E.E., Koentgen,F., Dijk,D.J. and Archer,S.N.
  TITLE     A human sleep homeostasis phenotype in mice expressing a
            primate-specific PER3 variable-number tandem-repeat coding-region
            polymorphism
  JOURNAL   FASEB J 28 (6), 2441-2454 (2014)
   PUBMED   24577121
REFERENCE   4  (residues 1 to 1115)
  AUTHORS   Maire,M., Reichert,C.F., Gabel,V., Viola,A.U., Strobel,W.,
            Krebs,J., Landolt,H.P., Bachmann,V., Cajochen,C. and Schmidt,C.
  TITLE     Sleep ability mediates individual differences in the vulnerability
            to sleep loss: evidence from a PER3 polymorphism
  JOURNAL   Cortex 52, 47-59 (2014)
   PUBMED   24439663
REFERENCE   5  (residues 1 to 1115)
  AUTHORS   Hasan,S., van der Veen,D.R., Winsky-Sommerer,R., Dijk,D.J. and
            Archer,S.N.
  TITLE     Altered sleep and behavioral activity phenotypes in PER3-deficient
            mice
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 301 (6), R1821-R1830 (2011)
   PUBMED   21957163
REFERENCE   6  (residues 1 to 1115)
  AUTHORS   Barnes,J.W., Tischkau,S.A., Barnes,J.A., Mitchell,J.W.,
            Burgoon,P.W., Hickok,J.R. and Gillette,M.U.
  TITLE     Requirement of mammalian Timeless for circadian rhythmicity
  JOURNAL   Science 302 (5644), 439-442 (2003)
   PUBMED   14564007
  REMARK    Erratum:[Science. 2003 Nov 14;302(5648):1153]
REFERENCE   7  (residues 1 to 1115)
  AUTHORS   Dudley,C.A., Erbel-Sieler,C., Estill,S.J., Reick,M., Franken,P.,
            Pitts,S. and McKnight,S.L.
  TITLE     Altered patterns of sleep and behavioral adaptability in
            NPAS2-deficient mice
  JOURNAL   Science 301 (5631), 379-383 (2003)
   PUBMED   12843397
REFERENCE   8  (residues 1 to 1115)
  AUTHORS   Kita,Y., Shiozawa,M., Jin,W., Majewski,R.R., Besharse,J.C.,
            Greene,A.S. and Jacob,H.J.
  TITLE     Implications of circadian gene expression in kidney, liver and the
            effects of fasting on pharmacogenomic studies
  JOURNAL   Pharmacogenetics 12 (1), 55-65 (2002)
   PUBMED   11773865
REFERENCE   9  (residues 1 to 1115)
  AUTHORS   Ebisawa,T., Uchiyama,M., Kajimura,N., Mishima,K., Kamei,Y.,
            Katoh,M., Watanabe,T., Sekimoto,M., Shibui,K., Kim,K., Kudo,Y.,
            Ozeki,Y., Sugishita,M., Toyoshima,R., Inoue,Y., Yamada,N.,
            Nagase,T., Ozaki,N., Ohara,O., Ishida,N., Okawa,M., Takahashi,K.
            and Yamauchi,T.
  TITLE     Association of structural polymorphisms in the human period3 gene
            with delayed sleep phase syndrome
  JOURNAL   EMBO Rep 2 (4), 342-346 (2001)
   PUBMED   11306557
REFERENCE   10 (residues 1 to 1115)
  AUTHORS   Jin,X., Shearman,L.P., Weaver,D.R., Zylka,M.J., de Vries,G.J. and
            Reppert,S.M.
  TITLE     A molecular mechanism regulating rhythmic output from the
            suprachiasmatic circadian clock
  JOURNAL   Cell 96 (1), 57-68 (1999)
   PUBMED   9989497
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB092512.1 and JAXUCZ010000005.1.
            
            On Jan 29, 2008 this sequence version replaced NP_076468.1.
            
            Summary: This gene is a member of the Period family of genes and is
            expressed in a circadian pattern in the suprachiasmatic nucleus,
            the primary circadian pacemaker in the mammalian brain. Genes in
            this family encode components of the circadian rhythms of locomotor
            activity, metabolism, and behavior. This gene is upregulated by
            Clock/Arntl heterodimers but then represses this upregulation in a
            feedback loop using Per/Cry heterodimers to interact with
            Clock/Arntl. Polymorphisms in this gene have been linked to sleep
            disorders. [provided by RefSeq, Feb 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643299.25679.1,
                                           SRR26360190.789438.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1115
                     /product="period circadian protein homolog 3"
                     /note="circadian clock protein PERIOD 3; period homolog 3;
                     period circadian clock 3"
                     /calculated_mol_wt=121787
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          54..63
                     /region_name="Nuclear export signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          281..369
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(284,288,294,307..310,339,344)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(304,308,316,319..320,351,353)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          400..409
                     /region_name="Nuclear export signal 3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          419..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          483..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          551..750
                     /region_name="CSNK1E binding domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          718..744
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          720..739
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          878..910
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56645; propagated from
                     UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          913..920
                     /region_name="Nuclear export signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     Region          <946..1089
                     /region_name="Period_C"
                     /note="Period protein 2/3C-terminal region; pfam12114"
                     /db_xref="CDD:463464"
     Region          947..1011
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8CJE2.1)"
     CDS             1..1115
                     /gene="Per3"
                     /gene_synonym="period3; rper3"
                     /coded_by="NM_023978.2:1..3348"
                     /db_xref="GeneID:78962"
                     /db_xref="RGD:621581"
ORIGIN      
        1 mdpcgnpavp ggdcpqtrgp glqgssgqeg plqgicvdss hsehedrnrm seelimvvqe
       61 mkkyfpaerh tkpstldaln yalrcvhsvq anseffqsls prgarqaeat vynleeltsl
      121 asehtskntd tfvavfsfls grlvhiseqa awilnskkgf lkslhfvdll aprdvrvfya
      181 htaptqlpfw ntwtqrasqy ecapvkpffc ricgggdreq krhyspfril pylvhvhspa
      241 qpepepcclt lvekihsgye apripvdkrv fttthtpgcv flevderavp llgflpqdli
      301 gtsiltylhp edrplmvavh qkvlkyvghp pfehspirfc tqngdyvild sswssfvnpw
      361 srkvsfiigr hkvrtsplne dvfatrikka tshdeditel qeqihrlllq pvhasassgy
      421 gslgssgsqe qhisvtssse ssghcveeaq qeqmtlqqvy asvnkiknvg qqlyiesmar
      481 ssvkpvmetc tepqgsdeqk dfsssqtlkn kstdtgsggd lrpeqhsssy qqmncidsvi
      541 ryltsysfpa lkrkcisctn tsssseeakp npeadgslrd teqlldipeq ettapsadae
      601 ggvartlsta alsmasgvsq cscssttdhv pplqsesvag acepwalrtk ahvtaegfkp
      661 vgltaavlsa htqkeeqnyv drfrekilts pygcylqqeg rnhakyacvv gagatpkhsr
      721 cagserrkhk rkklptpvds ssssahlcph vrgllpdvqh wsasvtspca tglalpsalv
      781 vpsqtpylls sfplqdmapq gvgdsaawga aaecpplsag pqpvstfpsa ymgtfmtvll
      841 hnsplfplwp asfspypflg atgpsqmapl vpamapdlep tpsdhgprrv eenwethsee
      901 ehpfissrss splqlnllqe empapseyad avrrgacpda kqlcvtgnsg srsppcatge
      961 latasvqqes ssaaasgssa ssvhgsgsdy tsevsengqr sqdrqrdraf sgaaeesiwr
     1021 miertpecvl mtyqvpergr dtvlredlek lhsmerqqpq fssaqkeela kvrswihsrp
     1081 apeerqlqsy vtcenrgsvg dtaeaceqcp aedts
//
LOCUS       NP_037212               2316 aa            linear   ROD 28-APR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase zeta isoform 1 precursor
            [Rattus norvegicus].
ACCESSION   NP_037212 XP_346696
VERSION     NP_037212.2
DBSOURCE    REFSEQ: accession NM_013080.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2316)
  AUTHORS   Tanga,N., Kuboyama,K., Kishimoto,A., Kiyonari,H., Shiraishi,A.,
            Suzuki,R., Watanabe,T., Fujikawa,A. and Noda,M.
  TITLE     The PTN-PTPRZ signal activates the AFAP1L2-dependent PI3K-AKT
            pathway for oligodendrocyte differentiation: Targeted inactivation
            of PTPRZ activity in mice
  JOURNAL   Glia 67 (5), 967-984 (2019)
   PUBMED   30667096
REFERENCE   2  (residues 1 to 2316)
  AUTHORS   Fujikawa,A., Sugawara,H., Tanaka,T., Matsumoto,M., Kuboyama,K.,
            Suzuki,R., Tanga,N., Ogata,A., Masumura,M. and Noda,M.
  TITLE     Targeting PTPRZ inhibits stem cell-like properties and
            tumorigenicity in glioblastoma cells
  JOURNAL   Sci Rep 7 (1), 5609 (2017)
   PUBMED   28717188
  REMARK    GeneRIF: High PTPRZ1 expression is associated with glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2316)
  AUTHORS   Reinehr,S., Reinhard,J., Wiemann,S., Stute,G., Kuehn,S.,
            Woestmann,J., Dick,H.B., Faissner,A. and Joachim,S.C.
  TITLE     Early remodelling of the extracellular matrix proteins tenascin-C
            and phosphacan in retina and optic nerve of an experimental
            autoimmune glaucoma model
  JOURNAL   J Cell Mol Med 20 (11), 2122-2137 (2016)
   PUBMED   27374750
  REMARK    GeneRIF: tenascin-C and phosphacan represent early indicators of
            neurodegeneration.
REFERENCE   4  (residues 1 to 2316)
  AUTHORS   Kuboyama,K., Fujikawa,A., Suzuki,R., Tanga,N. and Noda,M.
  TITLE     Role of Chondroitin Sulfate (CS) Modification in the Regulation of
            Protein-tyrosine Phosphatase Receptor Type Z (PTPRZ) Activity:
            PLEIOTROPHIN-PTPRZ-A SIGNALING IS INVOLVED IN OLIGODENDROCYTE
            DIFFERENTIATION
  JOURNAL   J Biol Chem 291 (35), 18117-18128 (2016)
   PUBMED   27445335
REFERENCE   5  (residues 1 to 2316)
  AUTHORS   Fujikawa,A., Nagahira,A., Sugawara,H., Ishii,K., Imajo,S.,
            Matsumoto,M., Kuboyama,K., Suzuki,R., Tanga,N., Noda,M.,
            Uchiyama,S., Tomoo,T., Ogata,A., Masumura,M. and Noda,M.
  TITLE     Small-molecule inhibition of PTPRZ reduces tumor growth in a rat
            model of glioblastoma
  JOURNAL   Sci Rep 6, 20473 (2016)
   PUBMED   26857455
  REMARK    GeneRIF: The intracellular delivery of SCB4380 by liposome carriers
            inhibited PTPRZ activity in C6 glioblastoma cells, and thereby
            suppressed their migration and proliferation in vitro and tumor
            growth in a rat allograft model.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2316)
  AUTHORS   Milev,P., Meyer-Puttlitz,B., Margolis,R.K. and Margolis,R.U.
  TITLE     Complex-type asparagine-linked oligosaccharides on phosphacan and
            protein-tyrosine phosphatase-zeta/beta mediate their binding to
            neural cell adhesion molecules and tenascin
  JOURNAL   J Biol Chem 270 (42), 24650-24653 (1995)
   PUBMED   7559574
REFERENCE   7  (residues 1 to 2316)
  AUTHORS   Maurel,P., Meyer-Puttlitz,B., Flad,M., Margolis,R.U. and
            Margolis,R.K.
  TITLE     Nucleotide sequence and molecular variants of rat receptor-type
            protein tyrosine phosphatase-zeta/beta
  JOURNAL   DNA Seq 5 (5), 323-328 (1995)
   PUBMED   7579589
REFERENCE   8  (residues 1 to 2316)
  AUTHORS   Milev,P., Friedlander,D.R., Sakurai,T., Karthikeyan,L., Flad,M.,
            Margolis,R.K., Grumet,M. and Margolis,R.U.
  TITLE     Interactions of the chondroitin sulfate proteoglycan phosphacan,
            the extracellular domain of a receptor-type protein tyrosine
            phosphatase, with neurons, glia, and neural cell adhesion molecules
  JOURNAL   J Cell Biol 127 (6 Pt 1), 1703-1715 (1994)
   PUBMED   7528221
REFERENCE   9  (residues 1 to 2316)
  AUTHORS   Grumet,M., Milev,P., Sakurai,T., Karthikeyan,L., Bourdon,M.,
            Margolis,R.K. and Margolis,R.U.
  TITLE     Interactions with tenascin and differential effects on cell
            adhesion of neurocan and phosphacan, two major chondroitin sulfate
            proteoglycans of nervous tissue
  JOURNAL   J Biol Chem 269 (16), 12142-12146 (1994)
   PUBMED   7512960
REFERENCE   10 (residues 1 to 2316)
  AUTHORS   Maurel,P., Rauch,U., Flad,M., Margolis,R.K. and Margolis,R.U.
  TITLE     Phosphacan, a chondroitin sulfate proteoglycan of brain that
            interacts with neurons and neural cell-adhesion molecules, is an
            extracellular variant of a receptor-type protein tyrosine
            phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 91 (7), 2512-2516 (1994)
   PUBMED   7511813
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U09357.1, JAXUCZ010000004.1 and BE104455.1.
            
            On Jan 5, 2010 this sequence version replaced NP_037212.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09357.1, SRR26360194.1381186.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2316
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..2316
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 1 precursor"
                     /EC_number="3.1.3.48"
                     /note="receptor-type tyrosine-protein phosphatase zeta;
                     3H1 keratan sulfate proteoglycan; 3F8 chondroitin sulfate
                     proteoglycan; PTP zeta; R-PTP-zeta; 6B4 proteoglycan;
                     protein tyrosine phosphatase, receptor-type, Z polypeptide
                     1"
                     /calculated_mol_wt=252588
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2802
     mat_peptide     25..2316
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 1"
                     /calculated_mol_wt=252588
     Region          45..298
                     /region_name="alpha_CARP_receptor_like"
                     /note="Carbonic anhydrase alpha related protein,
                     receptor_like subfamily. Carbonic anhydrase related
                     proteins (CARPs) are sequence similar to carbonic
                     anhydrases. Carbonic anhydrases are zinc-containing
                     enzymes that catalyze the reversible hydration of
                     carbon...; cd03122"
                     /db_xref="CDD:239396"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          313..401
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            order(397..398,400..401)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          433..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          518..537
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          586..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            595
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            610
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          636..720
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            645
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine,
                     alternate. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            685
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            786
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1005
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1025
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1058
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          1141..1172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Region          1204..1228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Region          1401..1521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1463
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          1545..1622
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1550
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1552
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1611
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1638..1663
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1685
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:B9EKR1; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Site            1688
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          1718..1995
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Site            2056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P23471; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     Region          2078..2281
                     /region_name="R-PTP-Z-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase Z, repeat 2; cd17669"
                     /db_xref="CDD:350507"
     Site            2224
                     /site_type="other"
                     /note="Ancestral active site; propagated from
                     UniProtKB/Swiss-Prot (Q62656.1)"
     CDS             1..2316
                     /gene="Ptprz1"
                     /gene_synonym="Ptpz; PTPzeta-A; PTPzeta-B; PTPzeta-S;
                     RPTPbeta"
                     /coded_by="NM_013080.2:106..7056"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25613"
                     /db_xref="RGD:3455"
ORIGIN      
        1 mrilqsflac vqllcvcrld waygyyrqqr klveeigwsy tgalnqknwg kkypicnspk
       61 qspinidedl tqvnvnlkkl kfqgwekpsl entfihntgk tveinltndy ylsgglsekv
      121 fkaskmtfhw gkcnvssegs ehslegqkfp lemqiycfda drfssfeetv kgkgrlrals
      181 ilfeigveen ldykaiidgt esvsrfgkqa aldpfilqnl lpnstdkyyi yngsltsppc
      241 tdtvewivfk dtvsisesql avfcevltmq qsgyvmlmdy lqnnfreqqy kfsrqvfssy
      301 tgkeeiheav cssepenvqa dpenytslli twerprvvyd tmiekfavly qplegndqtk
      361 hefltdgyqd lgailnnlip nmsyvlqiva icsnglygky sdqlivdmpt edaeldlfpe
      421 ligteeiike edygkgneed tglnpgrdsa tnqirkkepq vsttthynhm gtkyneaktn
      481 rsptkgsefs gksdvlntsl nptsqqvaef nperemslps qigtnlpphs vegtsaslns
      541 gsktllvfpq mnlsgtaesl nmvsiteyke vsadlseeen lltdfkldsg addssgsspa
      601 sstvpfstdn lshgytsssd tpeavtydvl rpestrnale dsapsgsees lkdpslegsv
      661 wfpgstdltt qsetgsgreg flqvnstdfq vdesrettet fspdatasrg psvtdmemph
      721 ystfayppte vtphaftpss rpldlaptsn ilhsqttqpv yngetplqps yssevfplvt
      781 pllldnqtln ttpaasssds alhatpvfps vgvsfdsils syddapllpf ssasfssdlf
      841 hhlhtvsqtl pqvtsaaerd elslhasllv aggdllleps lvqysdvmsh qvtihaasdt
      901 lefgsesavl yktsmvsqie spssdvvmha yssgpetsya iegshhvltv ssssaipvhd
      961 sigvadqgsl linpshislp essfitptas llqlppalsg dgewsgassd selllpdtdg
     1021 lrtlnmsspv svadftytts vsgddikpls kgemmygnet elkmssfsdm aypskstvvp
     1081 kmsdivnkws eslketsvsv ssinsvftes lvypitkvfd qeisrvpeii fpvkpthtas
     1141 qasgdtwlkp glstnsepal sdtassevlh pstqpllyea aspfnteall qpsfpasdvd
     1201 tllktalpsg prdpvltetp mveqssssms lplasesass kstlhftsvp vlnmspsdvh
     1261 ptslqrltvp hsreeyfeqg llkskspqqv lpslhshdef fqtahldisq ayppkgrhaf
     1321 atpilsidep qntlisrlvy sedifmhpei sitdkaltgl pttvsdvlia tdhsvplgsg
     1381 pismttvspn rddsvtttkl llpskatskp thsarsdadl vgggedgddy ddddyddids
     1441 drfpvnkcms cspyresqek vmndsdtqes slvdqsdpis hllsenteee nggtgvtrvd
     1501 kspdksppps mlpqkhndgr edrdiqmgsa vlphtpgska wavltsdees gsgqgtsdsl
     1561 ndnetstdfs fpdvnekdad gvleaddtgi apgsprsstp svtsghsgvs nsseaeasns
     1621 shesriglae glesekkavi plvivsaltf iclvvlvgil iywrkcfqta hfyledntsp
     1681 rvistpptpi fpisddigai pikhfpkhva dlhasngfte efetlkefyq evqsctvdlg
     1741 itadssnhpd nkhknryvni vaydhsrvkl tqlaekdgkl tdyinanyvd gynrpkayia
     1801 aqgplkstae dfwrmiwehn vevivmitnl vekgrrkcdq ywptdgseey gsflvnqknv
     1861 qvlayytvrn ftlrntkikk gsqkgrssgr lvtqyhytqw pdmgvpeysl pvlafvrkta
     1921 qakrhavgpv vvhcsagvgr tgtyivldsm lqqiqhegtv nifgflkhir sqrnylvqte
     1981 eqyvfihdtl veailskete vpdshihsyv ntllipgpsg ktklekqfql lsqsnilqsd
     2041 ystalkqcnr eknrtssiip versrvgiss lsgegtdyin asyimgyyqs nefiitqhpl
     2101 lhtikdfwrm iwdhnaqlvv mipdgqnmae defvywpnkd epincesfkv tlmseehkcl
     2161 sneeklivqd fileatqddy vlevrhfqcp kwpnpdspis ktfelisiik eeaanrdgpm
     2221 ivhdehggvt agtfcalttl mhqlekensm dvyqvakmin lmrpgvftdi eqyqflykvv
     2281 lslvstrqee npstsldsng aalpdgniae sleslv
//
LOCUS       NP_446140                 83 aa            linear   ROD 28-APR-2025
DEFINITION  retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic
            phosphodiesterase subunit gamma [Rattus norvegicus].
ACCESSION   NP_446140
VERSION     NP_446140.1
DBSOURCE    REFSEQ: accession NM_053688.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Wang,H., Lee,Y. and Malbon,C.C.
  TITLE     PDE6 is an effector for the Wnt/Ca2+/cGMP-signalling pathway in
            development
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 792-796 (2004)
   PUBMED   15494017
  REMARK    GeneRIF: PDE6 is an effector for the Wnt/Ca2+/cGMP-signalling
            pathway in development [review]
            Review article
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Cote,R.H.
  TITLE     Characteristics of photoreceptor PDE (PDE6): similarities and
            differences to PDE5
  JOURNAL   Int J Impot Res 16 Suppl 1, S28-S33 (2004)
   PUBMED   15224133
  REMARK    Review article
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Morin,F., Vannier,B., Houdart,F., Regnacq,M., Berges,T. and
            Voisin,P.
  TITLE     A proline-rich domain in the gamma subunit of phosphodiesterase 6
            mediates interaction with SH3-containing proteins
  JOURNAL   Mol Vis 9, 449-459 (2003)
   PUBMED   14502124
  REMARK    Erratum:[Mol Vis. 2003 Sep 18;9:449]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Tate,R.J., Arshavsky,V.Y. and Pyne,N.J.
  TITLE     The identification of the inhibitory gamma-subunits of the type 6
            retinal cyclic guanosine monophosphate phosphodiesterase in
            non-retinal tissues: differential processing of mRNA transcripts
  JOURNAL   Genomics 79 (4), 582-586 (2002)
   PUBMED   11944991
  REMARK    Erratum:[Genomics. 2004 Feb;83(2):346]
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Wan,K.F., Sambi,B.S., Frame,M., Tate,R. and Pyne,N.J.
  TITLE     The inhibitory gamma subunit of the type 6 retinal cyclic guanosine
            monophosphate phosphodiesterase is a novel intermediate regulating
            p42/p44 mitogen-activated protein kinase signaling in human
            embryonic kidney 293 cells
  JOURNAL   J Biol Chem 276 (41), 37802-37808 (2001)
   PUBMED   11502744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AI070066.1 and AF169390.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI070066.1, CB725406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q43"
     Protein         1..83
                     /product="retinal cone rhodopsin-sensitive cGMP
                     3',5'-cyclic phosphodiesterase subunit gamma"
                     /EC_number="3.1.4.35"
                     /note="GMP-PDE gamma; phosphodiesterase 6G, cGMP-specific,
                     rod, gamma; phosphodiesterase 6H, cGMP-specific, cone,
                     gamma"
                     /calculated_mol_wt=8913
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61250.1)"
     Region          2..83
                     /region_name="PDE6_gamma"
                     /note="Retinal cGMP phosphodiesterase, gamma subunit;
                     pfam04868"
                     /db_xref="CDD:428163"
     CDS             1..83
                     /gene="Pde6h"
                     /gene_synonym="Pde6g"
                     /coded_by="NM_053688.2:11..262"
                     /db_xref="GeneID:114248"
                     /db_xref="RGD:70933"
ORIGIN      
        1 msdspclspp apsqgpttpr kgppkfkqrq trqfkskppk kgvkgfgddi pgmeglgtdi
       61 tvicpweafs hlelhelaqf gii
//
LOCUS       NP_036961                115 aa            linear   ROD 28-APR-2025
DEFINITION  cholecystokinin preproprotein [Rattus norvegicus].
ACCESSION   NP_036961
VERSION     NP_036961.1
DBSOURCE    REFSEQ: accession NM_012829.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Cawthon,C.R. and de La Serre,C.B.
  TITLE     The critical role of CCK in the regulation of food intake and
            diet-induced obesity
  JOURNAL   Peptides 138, 170492 (2021)
   PUBMED   33422646
  REMARK    GeneRIF: The critical role of CCK in the regulation of food intake
            and diet-induced obesity.
            Review article
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Plaza,A., Merino,B., Del Olmo,N. and Ruiz-Gayo,M.
  TITLE     The cholecystokinin receptor agonist, CCK-8, induces adiponectin
            production in rat white adipose tissue
  JOURNAL   Br J Pharmacol 176 (15), 2678-2690 (2019)
   PUBMED   31012948
  REMARK    GeneRIF: The cholecystokinin receptor agonist, CCK-8, induces
            adiponectin production in rat white adipose tissue.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Plaza,A., Merino,B., Cano,V., Dominguez,G., Perez-Castells,J.,
            Fernandez-Alfonso,M.S., Sengenes,C., Chowen,J.A. and Ruiz-Gayo,M.
  TITLE     Cholecystokinin is involved in triglyceride fatty acid uptake by
            rat adipose tissue
  JOURNAL   J Endocrinol 236 (3), 137-150 (2018)
   PUBMED   29339381
  REMARK    GeneRIF: results show that cholecystokinin promotes lipid storage
            in white adipose tissue by acting on adipocyte cholecystokinin-2
            receptor
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Booker,S.A., Althof,D., Degro,C.E., Watanabe,M., Kulik,A. and
            Vida,I.
  TITLE     Differential surface density and modulatory effects of presynaptic
            GABAB receptors in hippocampal cholecystokinin and parvalbumin
            basket cells
  JOURNAL   Brain Struct Funct 222 (8), 3677-3690 (2017)
   PUBMED   28466358
  REMARK    GeneRIF: Study provides the first direct comparative and
            quantitative data showing that presynaptic GABAB receptors exert
            differential inhibition at cholecystokinin (CCK) and parvalbumin
            (PV) basket cell (BC) synapses, resulting from a higher surface
            expression of the receptor at all CCK BC terminals and a lower
            protein density present in a subpopulation of boutons of PV BCs.
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Roman,C.W., Sloat,S.R. and Palmiter,R.D.
  TITLE     A tale of two circuits: CCKNTS neuron stimulation controls appetite
            and induces opposing motivational states by projections to distinct
            brain regions
  JOURNAL   Neuroscience 358, 316-324 (2017)
   PUBMED   28684275
  REMARK    GeneRIF: The two projections from CCK(NTS) neurons reduce food
            intake through opposite motivational states; one pathway signals
            positive valence (CCK(NTS)-->paraventricular nucleus of the
            hypothalamus ) and the other signals negative valence
            (CCK(NTS)-->parabrachial nucleus).
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Deschenes,R.J., Haun,R.S., Funckes,C.L. and Dixon,J.E.
  TITLE     A gene encoding rat cholecystokinin. Isolation, nucleotide
            sequence, and promoter activity
  JOURNAL   J Biol Chem 260 (2), 1280-1286 (1985)
   PUBMED   2981840
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Deschenes,R.J., Haun,R.S., Sunkel,D., Roos,B.A. and Dixon,J.E.
  TITLE     Modulation of cholecystokinin gene expression
  JOURNAL   Ann N Y Acad Sci 448, 53-60 (1985)
   PUBMED   3861130
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Conrath-Verrier,M., Dietl,M. and Tramu,G.
  TITLE     Cholecystokinin-like immunoreactivity in the dorsal horn of the
            spinal cord of the rat: a light and electron microscopic study
  JOURNAL   Neuroscience 13 (3), 871-885 (1984)
   PUBMED   6084830
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Deschenes,R.J., Lorenz,L.J., Haun,R.S., Roos,B.A., Collier,K.J. and
            Dixon,J.E.
  TITLE     Cloning and sequence analysis of a cDNA encoding rat
            preprocholecystokinin
  JOURNAL   Proc Natl Acad Sci U S A 81 (3), 726-730 (1984)
   PUBMED   6199787
REFERENCE   10 (residues 1 to 115)
  AUTHORS   McLaughlin,C.L., Baile,C.A. and Peikin,S.R.
  TITLE     Hyperphagia during lactation: satiety response to CCK and growth of
            the pancreas
  JOURNAL   Am J Physiol 244 (1), E61-E65 (1983)
   PUBMED   6185005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X01032.1, FQ144519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840110, SAMN12840115
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..115
                     /product="cholecystokinin preproprotein"
                     /calculated_mol_wt=10935
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1924
     Region          4..115
                     /region_name="Gastrin"
                     /note="Gastrin/cholecystokinin family; pfam00918"
                     /db_xref="CDD:459996"
     proprotein      21..115
                     /product="cholecystokinin proprotein"
                     /calculated_mol_wt=10935
     mat_peptide     46..103
                     /product="cholecystokinin"
                     /calculated_mol_wt=6641
     mat_peptide     65..103
                     /product="cholecystokinin-39"
                     /exception="alternative processing"
                     /calculated_mol_wt=4597
     mat_peptide     71..103
                     /product="cholecystokinin-33"
                     /exception="alternative processing"
                     /calculated_mol_wt=3809
     mat_peptide     82..103
                     /product="cholecystokinin-22"
                     /exception="alternative processing"
                     /calculated_mol_wt=2654
     mat_peptide     92..103
                     /product="cholecystokinin-12"
                     /exception="alternative processing"
                     /calculated_mol_wt=1536
     mat_peptide     96..103
                     /product="cholecystokinin-8"
                     /exception="alternative processing"
                     /calculated_mol_wt=1064
     Site            97
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:8208365; propagated from
                     UniProtKB/Swiss-Prot (P01355.1)"
     Site            103
                     /site_type="amidation"
                     /note="Phenylalanine amide.
                     /evidence=ECO:0000250|UniProtKB:P06307; propagated from
                     UniProtKB/Swiss-Prot (P01355.1)"
     Site            106..107
                     /site_type="cleavage"
                     /note="Cleavage; propagated from UniProtKB/Swiss-Prot
                     (P01355.1)"
     Site            111
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000269|Ref.5;
                     propagated from UniProtKB/Swiss-Prot (P01355.1)"
     Site            113
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000269|Ref.5;
                     propagated from UniProtKB/Swiss-Prot (P01355.1)"
     CDS             1..115
                     /gene="Cck"
                     /coded_by="NM_012829.2:111..458"
                     /db_xref="GeneID:25298"
                     /db_xref="RGD:2288"
ORIGIN      
        1 mkcgvclcvv mavlaagala qpvvpveavd pmeqraeeap rrqlravlrp dseprarlga
       61 llaryiqqvr kapsgrmsvl knlqgldpsh risdrdymgw mdfgrrsaed yeyps
//
LOCUS       NP_877402                196 aa            linear   ROD 28-APR-2025
DEFINITION  calcineurin B homologous protein 2 [Rattus norvegicus].
ACCESSION   NP_877402
VERSION     NP_877402.1
DBSOURCE    REFSEQ: accession NM_182738.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Knaapen,M., Koch,A.H., Koch,C., Koch,K.T., Li,X., van Rooij,P.C.,
            Tijssen,J.G., Peters,R.J., van der Wal,A.C., Damman,P. and de
            Winter,R.J.
  TITLE     Prevalence of left and balanced coronary arterial dominance
            decreases with increasing age of patients at autopsy. A postmortem
            coronary angiograms study
  JOURNAL   Cardiovasc Pathol 22 (1), 49-53 (2013)
   PUBMED   22463919
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Li,Q.H., Wang,L.H., Lin,Y.N., Chang,G.Q., Li,H.W., Jin,W.N.,
            Hu,R.H. and Pang,T.X.
  TITLE     Nuclear accumulation of calcineurin B homologous protein 2 (CHP2)
            results in enhanced proliferation of tumor cells
  JOURNAL   Genes Cells 16 (4), 416-426 (2011)
   PUBMED   21392185
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Bales,J.W., Ma,X., Yan,H.Q., Jenkins,L.W. and Dixon,C.E.
  TITLE     Regional calcineurin subunit B isoform expression in rat
            hippocampus following a traumatic brain injury
  JOURNAL   Brain Res 1358, 211-220 (2010)
   PUBMED   20713027
  REMARK    GeneRIF: Calcineurin B isoforms showed increased expression
            throughout the CA1 and CA2 while there was a decrease in expression
            within the ipsilateral dentate gyrus.
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Li,G.D., Zhang,X., Li,R., Wang,Y.D., Wang,Y.L., Han,K.J.,
            Qian,X.P., Yang,C.G., Liu,P., Wei,Q., Chen,W.F., Zhang,J. and
            Zhang,Y.
  TITLE     CHP2 activates the calcineurin/nuclear factor of activated T cells
            signaling pathway and enhances the oncogenic potential of HEK293
            cells
  JOURNAL   J Biol Chem 283 (47), 32660-32668 (2008)
   PUBMED   18815128
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Inoue,H., Nakamura,Y., Nagita,M., Takai,T., Masuda,M., Nakamura,N.
            and Kanazawa,H.
  TITLE     Calcineurin homologous protein isoform 2 (CHP2), Na+/H+
            exchangers-binding protein, is expressed in intestinal epithelium
  JOURNAL   Biol Pharm Bull 26 (2), 148-155 (2003)
   PUBMED   12576672
  REMARK    GeneRIF: CHP2 is predominantly expressed in epithelial cells of the
            small and large intestine where it may regulate epithelial Na+/H+
            exchanger(NHE)isoforms NHE2-4.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB086189.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB086189.1, FM101005.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q36"
     Protein         1..196
                     /product="calcineurin B homologous protein 2"
                     /calculated_mol_wt=22354
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q810D1.1)"
     Region          30..184
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          137..148
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q810D1.1)"
     CDS             1..196
                     /gene="Chp2"
                     /gene_synonym="chp-2"
                     /coded_by="NM_182738.1:39..629"
                     /db_xref="GeneID:308965"
                     /db_xref="RGD:727796"
ORIGIN      
        1 mgsrsshval ipdvdqirre tgfsqasllr lyhrfqaldr eekgflsrld lqqigalavn
       61 plgdriidsf fpngsqrvyf agfarvlayf rpideddatl rdpkqpepln srmnklrfaf
      121 qlydldrdgk isrnemlqvl rlmvgvqvtd eqlesitdrt vqeadedgdg avsflefaks
      181 lekmnieqkm sirilk
//
LOCUS       NP_071567                496 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase XIAP [Rattus norvegicus].
ACCESSION   NP_071567 XP_003754888 XP_003754889
VERSION     NP_071567.1
DBSOURCE    REFSEQ: accession NM_022231.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Xu,L.J., Yang,Y., Yuan,L.F., Liu,H., Xu,N.P., Yang,Y. and Huang,L.
  TITLE     SP1-stimulated miR-208a-5p aggravates sepsis-induced myocardial
            injury via targeting XIAP
  JOURNAL   Exp Cell Res 435 (1), 113905 (2024)
   PUBMED   38163563
  REMARK    GeneRIF: SP1-stimulated miR-208a-5p aggravates sepsis-induced
            myocardial injury via targeting XIAP.
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Xiang,R.P., Zhou,M.J., Cui,R., Yu,H.Y., Chen,Q., Huang,Y.J., Li,Z.
            and Yu,C.
  TITLE     Effects of Different Degrees of Carotid Artery Stenosis on the
            Expression of XIAP and Smac in the Ischemic Penumbra of Rats with
            Cerebral Ischemia-Reperfusion
  JOURNAL   J Stroke Cerebrovasc Dis 30 (2), 105516 (2021)
   PUBMED   33310074
  REMARK    GeneRIF: Effects of Different Degrees of Carotid Artery Stenosis on
            the Expression of XIAP and Smac in the Ischemic Penumbra of Rats
            with Cerebral Ischemia-Reperfusion.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Deng,W., Fan,C., Zhao,Y., Mao,Y., Li,J., Zhang,Y. and Teng,J.
  TITLE     MicroRNA-130a regulates neurological deficit and angiogenesis in
            rats with ischaemic stroke by targeting XIAP
  JOURNAL   J Cell Mol Med 24 (18), 10987-11000 (2020)
   PUBMED   32790238
  REMARK    GeneRIF: MicroRNA-130a regulates neurological deficit and
            angiogenesis in rats with ischaemic stroke by targeting XIAP.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Jiang,L. and Xiao,J.
  TITLE     2-phenylethynesulfonamide inhibits growth of oral squamous cell
            carcinoma cells by blocking the function of heat shock protein 70
  JOURNAL   Biosci Rep 40 (3) (2020)
   PUBMED   32110810
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Li,S., Zhao,Y., He,X., Kim,T.H., Kuharsky,D.K., Rabinowich,H.,
            Chen,J., Du,C. and Yin,X.M.
  TITLE     Relief of extrinsic pathway inhibition by the Bid-dependent
            mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis
  JOURNAL   J Biol Chem 277 (30), 26912-26920 (2002)
   PUBMED   12011074
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Perrelet,D., Ferri,A., Liston,P., Muzzin,P., Korneluk,R.G. and
            Kato,A.C.
  TITLE     IAPs are essential for GDNF-mediated neuroprotective effects in
            injured motor neurons in vivo
  JOURNAL   Nat Cell Biol 4 (2), 175-179 (2002)
   PUBMED   11813002
  REMARK    GeneRIF: Results show that inhibition of XIAP or NAIP activity
            prevents GDNF-mediated neuroprotective effects, suggesting that
            XIAP and NAIP are essential for intracellular signalling of GDNF in
            motor neuron survival (Birc4 protein).
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Holcik,M., Lefebvre,C.A., Hicks,K. and Korneluk,R.G.
  TITLE     Cloning and characterization of the rat homologues of the Inhibitor
            of Apoptosis protein 1, 2, and 3 genes
  JOURNAL   BMC Genomics 3, 5 (2002)
   PUBMED   11860601
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Suzuki,Y., Imai,Y., Nakayama,H., Takahashi,K., Takio,K. and
            Takahashi,R.
  TITLE     A serine protease, HtrA2, is released from the mitochondria and
            interacts with XIAP, inducing cell death
  JOURNAL   Mol Cell 8 (3), 613-621 (2001)
   PUBMED   11583623
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Deveraux,Q.L., Takahashi,R., Salvesen,G.S. and Reed,J.C.
  TITLE     X-linked IAP is a direct inhibitor of cell-death proteases
  JOURNAL   Nature 388 (6639), 300-304 (1997)
   PUBMED   9230442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC111718.10 and AB033366.1.
            
            On or before Jun 26, 2012 this sequence version replaced
            XP_003754888.1, XP_003754889.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB033366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMD00132289
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq35"
     Protein         1..496
                     /product="E3 ubiquitin-protein ligase XIAP"
                     /EC_number="2.3.2.27"
                     /note="baculoviral IAP repeat-containing protein 4;
                     RIAP-3; X-linked IAP; IAP homolog A; inhibitor of
                     apoptosis protein 3; X-linked inhibitor of apoptosis
                     protein; IAP-3; apoptosis inhibitor protein 3; baculoviral
                     IAP repeat-containing 4; X-linked inhibitor of apoptosis,
                     E3 ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase XIAP"
                     /calculated_mol_wt=55942
     Region          26..93
                     /region_name="BIR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R0I6.1)"
     Region          28..95
                     /region_name="BIR"
                     /note="Baculoviral inhibition of apoptosis protein repeat
                     domain; Found in inhibitors of apoptosis proteins (IAPs)
                     and other proteins. In higher eukaryotes, BIR domains
                     inhibit apoptosis by acting as direct inhibitors of the
                     caspase family of protease enzymes; cd00022"
                     /db_xref="CDD:237989"
     Site            order(55,60,62,69..71,73,77,82,86..87)
                     /site_type="active"
                     /note="peptide binding groove [active]"
                     /db_xref="CDD:237989"
     Site            order(63,66,83,90)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:237989"
     Region          162..232
                     /region_name="BIR"
                     /note="Baculoviral inhibition of apoptosis protein repeat;
                     smart00238"
                     /db_xref="CDD:197595"
     Region          163..230
                     /region_name="BIR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R0I6.1)"
     Site            order(192,197,199,206..208,210,214,219,223..224)
                     /site_type="active"
                     /note="peptide binding groove [active]"
                     /db_xref="CDD:237989"
     Site            order(200,203,220,227)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:237989"
     Region          264..330
                     /region_name="BIR"
                     /note="Baculoviral inhibition of apoptosis protein repeat;
                     smart00238"
                     /db_xref="CDD:197595"
     Region          264..329
                     /region_name="BIR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R0I6.1)"
     Site            order(291,296,298,305..307,309,313,318,322..323)
                     /site_type="active"
                     /note="peptide binding groove [active]"
                     /db_xref="CDD:237989"
     Site            order(299,302,319,326)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:237989"
     Region          369..418
                     /region_name="UBA_BIRC4_8"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8)
                     and similar proteins; cd14395"
                     /db_xref="CDD:270578"
     Region          433..496
                     /region_name="RING-HC_BIRC4_8"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase XIAP, baculoviral IAP
                     repeat-containing protein 8 (BIRC8) and similar proteins;
                     cd16714"
                     /db_xref="CDD:438374"
     Site            order(436..437,439..440,443..444,446..447,460,462..463,
                     465,467,491..495)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438374"
     Site            order(462..464,471,485,488..489,491..492,494)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438374"
     CDS             1..496
                     /gene="Xiap"
                     /gene_synonym="Api3; Birc4; riap3"
                     /coded_by="NM_022231.2:331..1821"
                     /db_xref="GeneID:63879"
                     /db_xref="RGD:620692"
ORIGIN      
        1 mtfnsfegsr tvvpadtnkd eefveefnrl ktfanfpsss pvsastlara gflytgegdt
       61 vqcfschaav drwqygdsav grhrrispnc rfingfyfen gatqstspgi qngqyksenc
      121 vgnrnhfald rpsethadyl lrtgqvvdis dtiyprnpam cseearlktf qnwpdyahls
      181 prelasagly ytgiddqvqc fccggklknw epcdrawseh rrhfpncffv lgrnvnvrse
      241 sgvssdrnfp nstnsprnpa maeydarivt fgtwlysvnk eqlaragfya lgegdkvkcf
      301 hcgggltdwk psedpweqha kwypgckyll dekgqeyinn ihlthslges vvrtaektps
      361 vtkkiddtif qnpmvqeair mgfnfkdikk tmeeklqtsg snylslevli adlvsaqkdn
      421 sqdessqtsl qkdisteeql rrlqeeklck icmdrniaiv fvpcghlvtc kqcaeavdkc
      481 pmcctvitfk qkifms
//
LOCUS       NP_077351                476 aa            linear   ROD 28-APR-2025
DEFINITION  growth/differentiation factor 10 precursor [Rattus norvegicus].
ACCESSION   NP_077351 XP_346484
VERSION     NP_077351.1
DBSOURCE    REFSEQ: accession NM_024375.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Zhao,Q., Xu,J., Han,X., Zhang,Z., Qu,J. and Cheng,Z.
  TITLE     Growth differentiation factor 10 induces angiogenesis to promote
            wound healing in rats with diabetic foot ulcers by activating
            TGF-beta1/Smad3 signaling pathway
  JOURNAL   Front Endocrinol (Lausanne) 13, 1013018 (2023)
   PUBMED   36714584
  REMARK    GeneRIF: Growth differentiation factor 10 induces angiogenesis to
            promote wound healing in rats with diabetic foot ulcers by
            activating TGF-beta1/Smad3 signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Jiang,L., Tan,B., Li,S., Wang,L., Zheng,L., Liu,Y., Long,Z. and
            Wu,Y.
  TITLE     Decrease of growth and differentiation factor 10 contributes to
            neuropathic pain through N-methyl-D-aspartate receptor activation
  JOURNAL   Neuroreport 28 (8), 444-450 (2017)
   PUBMED   28394782
  REMARK    GeneRIF: Results suggest that the decreasing growth and
            differentiation factor 10 may contribute toward neuropathic pain by
            facilitating N-methyl-D-aspartate receptor activation. Findings
            shed new light on the understanding of the molecular mechanisms
            underlying neuropathic pain.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Barallobre-Barreiro,J., Oklu,R., Lynch,M., Fava,M., Baig,F.,
            Yin,X., Barwari,T., Potier,D.N., Albadawi,H., Jahangiri,M.,
            Porter,K.E., Watkins,M.T., Misra,S., Stoughton,J. and Mayr,M.
  TITLE     Extracellular matrix remodelling in response to venous
            hypertension: proteomics of human varicose veins
  JOURNAL   Cardiovasc Res 110 (3), 419-430 (2016)
   PUBMED   27068509
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Zhao,L., Isayama,K., Chen,H., Yamauchi,N., Shigeyoshi,Y.,
            Hashimoto,S. and Hattori,M.A.
  TITLE     The nuclear receptor REV-ERBalpha represses the transcription of
            growth/differentiation factor 10 and 15 genes in rat endometrium
            stromal cells
  JOURNAL   Physiol Rep 4 (2) (2016)
   PUBMED   26811051
  REMARK    GeneRIF: findings indicate that the attenuation of REV-ERBalpha
            leads to an upregulation of Gdf10 and Gdf15 in decidual cells
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Bubenek,S., Nastase,A., Niculescu,A.M., Baila,S., Herlea,V.,
            Lazar,V., Paslaru,L., Botezatu,A., Tomescu,D., Popescu,I. and
            Dima,S.
  TITLE     Assessment of gene expression profiles in peripheral occlusive
            arterial disease
  JOURNAL   Can J Cardiol 28 (6), 712-720 (2012)
   PUBMED   22721676
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Kaihara,S., Bessho,K., Okubo,Y., Sonobe,J., Komatsu,Y., Miura,M.,
            Miyatake,S., Nakao,K. and Iizuka,T.
  TITLE     Over expression of bone morphogenetic protein-3b (BMP-3b) using an
            adenoviral vector promote the osteoblastic differentiation in C2C12
            cells and augment the bone formation induced by bone morphogenetic
            protein-2 (BMP-2) in rats
  JOURNAL   Life Sci 72 (15), 1683-1693 (2003)
   PUBMED   12559390
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Erickson,G.F. and Shimasaki,S.
  TITLE     The spatiotemporal expression pattern of the bone morphogenetic
            protein family in rat ovary cell types during the estrous cycle
  JOURNAL   Reprod Biol Endocrinol 1, 9 (2003)
   PUBMED   12741959
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Nakamura,K., Kadotani,Y., Ushigome,H., Akioka,K., Okamoto,M.,
            Ohmori,Y., Yaoi,T., Fushiki,S., Yoshimura,R. and Yoshimura,N.
  TITLE     Antisense oligonucleotide for tissue factor inhibits hepatic
            ischemic reperfusion injury
  JOURNAL   Biochem Biophys Res Commun 297 (3), 433-441 (2002)
   PUBMED   12270110
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Hino,J., Matsuo,H. and Kangawa,K.
  TITLE     Bone morphogenetic protein-3b (BMP-3b) gene expression is
            correlated with differentiation in rat calvarial osteoblasts
  JOURNAL   Biochem Biophys Res Commun 256 (2), 419-424 (1999)
   PUBMED   10079200
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Takao,M., Hino,J., Takeshita,N., Konno,Y., Nishizawa,T., Matsuo,H.
            and Kangawa,K.
  TITLE     Identification of rat bone morphogenetic protein-3b (BMP-3b), a new
            member of BMP-3
  JOURNAL   Biochem Biophys Res Commun 219 (2), 656-662 (1996)
   PUBMED   8605043
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D49494.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346484.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D49494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p16"
     Protein         1..476
                     /product="growth/differentiation factor 10 precursor"
                     /note="bone morphogenetic protein 3b; BIP; BMP-3b; GDF-10;
                     bone-inducing protein; prepro bone inducing protein"
                     /calculated_mol_wt=49936
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3043
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55108.1)"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55108.1)"
     Region          268..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55108.1)"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55108.1)"
     Region          330..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55108.1)"
     Region          365..476
                     /region_name="TGF_beta_GDF10"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in growth/differentiation factor 10 (GDF10)
                     and similar proteins; cd19394"
                     /db_xref="CDD:381664"
     mat_peptide     367..476
                     /product="Growth/differentiation factor 10.
                     /id=PRO_0000033849"
                     /note="propagated from UniProtKB/Swiss-Prot (P55108.1)"
                     /calculated_mol_wt=12438
     Site            order(379,381,385..386,388,398,400..402,419..420,423..424,
                     426..427,430,435..437,440,442..443,446,466..468,470,476)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381664"
     Site            467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55108.1)"
     CDS             1..476
                     /gene="Gdf10"
                     /coded_by="NM_024375.1:240..1670"
                     /db_xref="GeneID:79216"
                     /db_xref="RGD:621512"
ORIGIN      
        1 mapglarisl rsqllplvpl llllrgagcg hrvpswsslp saadsvqrdr dlqqspgdaa
       61 aalgpgaqdi vavhmlrlye kynrrgappg ggntvrsfra rldvidqkpv yffnltsmqd
      121 semiltatfh fysepprwpr arevfckpra knascrlltp glparlhlif rslsqntatq
      181 gllrgamalt ppprglwqak dissiikaar rdgelllsaq ldsgekdlgv prpsshmpyi
      241 lvyandlais epnsvavtlq rydpfpagdf epgaapnssa dprvrraaqv skplqdnelp
      301 glderpapal haqhfhkhef wsspfralkp rtgrkdrkkk dqdtftpsss qvldfdektm
      361 qkarrrqwde prvcsrrylk vdfadigwne wiispksfda yycagacefp mpkivrpsnh
      421 atiqsivrav givpgipepc cvpdkmnslg vlfldenrnv vlkvypnmsv etcacr
//
LOCUS       NP_001094205             534 aa            linear   ROD 28-APR-2025
DEFINITION  lysophosphatidylcholine acyltransferase 1 [Rattus norvegicus].
ACCESSION   NP_001094205 XP_001057012 XP_001057066 XP_341748
VERSION     NP_001094205.1
DBSOURCE    REFSEQ: accession NM_001100735.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Okubo,M., Yamanaka,H., Kobayashi,K., Kanda,H., Dai,Y. and
            Noguchi,K.
  TITLE     Up-regulation of platelet-activating factor synthases and its
            receptor in spinal cord contribute to development of neuropathic
            pain following peripheral nerve injury
  JOURNAL   Mol Pain 8, 8 (2012)
   PUBMED   22296727
  REMARK    GeneRIF: These data show the histological localization of PAF
            synthases and its receptor in the spinal cord following peripheral
            nerve injury.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Moessinger,C., Kuerschner,L., Spandl,J., Shevchenko,A. and
            Thiele,C.
  TITLE     Human lysophosphatidylcholine acyltransferases 1 and 2 are located
            in lipid droplets where they catalyze the formation of
            phosphatidylcholine
  JOURNAL   J Biol Chem 286 (24), 21330-21339 (2011)
   PUBMED   21498505
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Won,J., Shi,L.Y., Hicks,W., Wang,J., Hurd,R., Naggert,J.K.,
            Chang,B. and Nishina,P.M.
  TITLE     Mouse model resources for vision research
  JOURNAL   J Ophthalmol 2011, 391384 (2011)
   PUBMED   21052544
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Butler,P.L. and Mallampalli,R.K.
  TITLE     Cross-talk between remodeling and de novo pathways maintains
            phospholipid balance through ubiquitination
  JOURNAL   J Biol Chem 285 (9), 6246-6258 (2010)
   PUBMED   20018880
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Harayama,T., Shindou,H., Ogasawara,R., Suwabe,A. and Shimizu,T.
  TITLE     Identification of a novel noninflammatory biosynthetic pathway of
            platelet-activating factor
  JOURNAL   J Biol Chem 283 (17), 11097-11106 (2008)
   PUBMED   18285344
  REMARK    GeneRIF: LPCAT1 transfers acetate from acetyl-CoA to lyso-PAF; its
            activity and expression are independent of inflammatory signals
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Soupene,E., Fyrst,H. and Kuypers,F.A.
  TITLE     Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes
  JOURNAL   Proc Natl Acad Sci U S A 105 (1), 88-93 (2008)
   PUBMED   18156367
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Chen,X., Hyatt,B.A., Mucenski,M.L., Mason,R.J. and Shannon,J.M.
  TITLE     Identification and characterization of a lysophosphatidylcholine
            acyltransferase in alveolar type II cells
  JOURNAL   Proc Natl Acad Sci U S A 103 (31), 11724-11729 (2006)
   PUBMED   16864775
  REMARK    GeneRIF: Results suggest that lysophosphatidylcholine
            acyltransferase (LPCAT) plays a critical role in regulating
            surfactant phospholipid biosynthesis [LPCAT].
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Nakanishi,H., Shindou,H., Hishikawa,D., Harayama,T., Ogasawara,R.,
            Suwabe,A., Taguchi,R. and Shimizu,T.
  TITLE     Cloning and characterization of mouse lung-type
            acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1).
            Expression in alveolar type II cells and possible involvement in
            surfactant production
  JOURNAL   J Biol Chem 281 (29), 20140-20147 (2006)
   PUBMED   16704971
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF406111.1, CB718601.1, AB244983.2, CK365681.1, EB482109.1,
            CN544249.1 and AW533114.1.
            
            On or before Nov 22, 2008 this sequence version replaced
            XP_001057066.1, XP_001057012.1, XP_341748.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..534
                     /product="lysophosphatidylcholine acyltransferase 1"
                     /EC_number="2.3.1.51"
                     /EC_number="2.3.1.23"
                     /EC_number="2.3.1.67"
                     /EC_number="2.3.1.25"
                     /note="LPCAT-1; lysoPAFAT; LPC acyltransferase 1;
                     acyltransferase-like 2; lysoPC acyltransferase 1; lyso-PAF
                     acetyltransferase; acetyl-CoA:lyso-PAF acetyltransferase;
                     1-acylglycerophosphocholine O-acyltransferase;
                     1-alkylglycerophosphocholine O-acetyltransferase;
                     acetyl-CoA:lyso-platelet-activating factor
                     acetyltransferase; 1-acylglycerol-3-phosphate
                     O-acyltransferase; 1-alkenylglycerophosphocholine
                     O-acyltransferase"
                     /calculated_mol_wt=59631
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HAQ0.2)"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HAQ0.2)"
     Region          103..314
                     /region_name="LPLAT_LPCAT1-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: LPCAT1-like; cd07991"
                     /db_xref="CDD:153253"
     Site            order(135,138,140,153..156,209..211)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153253"
     Region          135..140
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q3TFD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HAQ0.2)"
     Region          <350..412
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Site            order(353,357..358,392,394,396,398,400,403)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     Region          384..446
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Site            order(392,394,396,403,429,431,433,440)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Region          421..480
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          531..534
                     /region_name="Di-lysine motif.
                     /evidence=ECO:0000250|UniProtKB:Q3TFD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HAQ0.2)"
     CDS             1..534
                     /gene="Lpcat1"
                     /gene_synonym="Aytl2; RGD1311599"
                     /coded_by="NM_001100735.1:138..1742"
                     /db_xref="GeneID:361467"
                     /db_xref="RGD:1311599"
ORIGIN      
        1 mrlrgrgpra apssssgagd arrlappgrn pfvhelrlsa lqkaqvafmt ltlfpirllf
       61 aafmmllawp falvaslgpp dkepeqplal wrkvvdfllk aimrtmwfag gfhrvavkgr
      121 qalpteaail tlaphssyfd aipvtmtmss ivmkaesrdi piwgtliryi rpvfvsrsdq
      181 dsrrktveei krraqsngkw pqimifpegt ctnrtclitf kpgafipgvp vqpvvlrypn
      241 kldtitwtwq gpgalkilwl tlcqfqnqve ieflpvycps eeekrnpaly asnvrrvmak
      301 algvsvtdyt fedcqlalae gqlrlpadtc llefarlvrg lglkpenlek dldkysesar
      361 mkrgekirlp efaaylevpv sdaledmfsl fdesgggeid lreyvvalsv vcrpsqtlat
      421 iqlafkmygs pedgsidead lscilktalg iseltvtdlf qaidqeergr itfddfcgfa
      481 emypdfaedy lypdqthsds caqtppaptp ngfcidfspe hsdfgrknsc kkvd
//
LOCUS       NP_001037746             305 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein C10orf62 homolog [Rattus norvegicus].
ACCESSION   NP_001037746 XP_001058281
VERSION     NP_001037746.1
DBSOURCE    REFSEQ: accession NM_001044281.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078978.1.
            
            On Aug 24, 2006 this sequence version replaced XP_001058281.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC078978.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..305
                     /product="uncharacterized protein C10orf62 homolog"
                     /calculated_mol_wt=33893
     Region          1..208
                     /region_name="DUF5569"
                     /note="Family of unknown function (DUF5569); pfam17729"
                     /db_xref="CDD:465472"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYN3.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYN3.1)"
     Region          92..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYN3.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYN3.1)"
     Region          <165..>302
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          197..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYN3.1)"
     CDS             1..305
                     /gene="C1h10orf62"
                     /coded_by="NM_001044281.1:151..1068"
                     /db_xref="GeneID:682010"
                     /db_xref="RGD:1588156"
ORIGIN      
        1 mlwaqrkkrk attettedkp aeshrpndsw ikshfsrlse eklpayrrvs scgyspegkh
       61 geanttlhvd tvttkhgegg valhrdsfas kqkisgtsvs kemqresgks psmendtwaa
      121 vaactkeida kghhvansvl qrspeyhrtg haesrnispe dlkaleevel klkgnflthr
      181 etvvaganqa htvynqshhg nqshqnhnty pchqnnqsrs vhyqghhpsh lshqgypsys
      241 shqnhpghps qqghsshsnq qghlglssqq ghpsqsshqs hqgqpghpnh qshslvnrrn
      301 qiyds
//
LOCUS       NP_976080                161 aa            linear   ROD 28-APR-2025
DEFINITION  vitamin K epoxide reductase complex subunit 1 [Rattus norvegicus].
ACCESSION   NP_976080 XP_219366
VERSION     NP_976080.1
DBSOURCE    REFSEQ: accession NM_203335.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Yigit,N., Duman,M.T., Cetinturk,D., Saygili-Yigit,F., Colak,E. and
            Colak,R.
  TITLE     Vkorc1 gene polymorphisms confer resistance to anticoagulant
            rodenticide in Turkish rats
  JOURNAL   PeerJ 11, e15055 (2023)
   PUBMED   37151288
  REMARK    GeneRIF: Vkorc1 gene polymorphisms confer resistance to
            anticoagulant rodenticide in Turkish rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Krijger,I.M., Strating,M., van Gent-Pelzer,M., van der Lee,T.A.J.,
            Burt,S.A., Schroeten,F.H., de Vries,R., de Cock,M., Maas,M. and
            Meerburg,B.G.
  TITLE     Large-scale identification of rodenticide resistance in Rattus
            norvegicus and Mus musculus in the Netherlands based on Vkorc1
            codon 139 mutations
  JOURNAL   Pest Manag Sci 79 (3), 989-995 (2023)
   PUBMED   36309944
  REMARK    GeneRIF: Large-scale identification of rodenticide resistance in
            Rattus norvegicus and Mus musculus in the Netherlands based on
            Vkorc1 codon 139 mutations.
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Bermejo-Nogales,A., Rodriguez Martin,J.A., Coll,J. and Navas,J.M.
  TITLE     VKORC1 single nucleotide polymorphisms in rodents in Spain
  JOURNAL   Chemosphere 308 (Pt 1), 136021 (2022)
   PUBMED   35970209
  REMARK    GeneRIF: VKORC1 single nucleotide polymorphisms in rodents in
            Spain.
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Damin-Pernik,M., Hammed,A., Giraud,L., Goulois,J., Benoit,E. and
            Lattard,V.
  TITLE     Distribution of non-synonymous Vkorc1 mutations in roof rats
            (Rattus rattus) in France and in Spain - consequences for
            management
  JOURNAL   Pestic Biochem Physiol 183, 105052 (2022)
   PUBMED   35430058
  REMARK    GeneRIF: Distribution of non-synonymous Vkorc1 mutations in roof
            rats (Rattus rattus) in France and in Spain - consequences for
            management.
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Chua,C., Humaidi,M., Neves,E.S., Mailepessov,D., Ng,L.C. and Aik,J.
  TITLE     VKORC1 mutations in rodent populations of a tropical city-state as
            an indicator of anticoagulant rodenticide resistance
  JOURNAL   Sci Rep 12 (1), 4553 (2022)
   PUBMED   35296766
  REMARK    GeneRIF: VKORC1 mutations in rodent populations of a tropical
            city-state as an indicator of anticoagulant rodenticide resistance.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Rost,S., Fregin,A., Ivaskevicius,V., Conzelmann,E., Hortnagel,K.,
            Pelz,H.J., Lappegard,K., Seifried,E., Scharrer,I., Tuddenham,E.G.,
            Muller,C.R., Strom,T.M. and Oldenburg,J.
  TITLE     Mutations in VKORC1 cause warfarin resistance and multiple
            coagulation factor deficiency type 2
  JOURNAL   Nature 427 (6974), 537-541 (2004)
   PUBMED   14765194
  REMARK    GeneRIF: identified, by using linkage information from three
            species the gene VKORC1 which encodes a small transmembrane protein
            of the endoplasmic reticulum; VKORC1 contains missense mutations in
            both human disorders and in a warfarin-resistant rat strain
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Wilson,C.R., Sauer,J.M., Carlson,G.P., Wallin,R., Ward,M.P. and
            Hooser,S.B.
  TITLE     Species comparison of vitamin K1 2,3-epoxide reductase activity in
            vitro: kinetics and warfarin inhibition
  JOURNAL   Toxicology 189 (3), 191-198 (2003)
   PUBMED   12832152
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Begent,L.A., Hill,A.P., Steventon,G.B., Hutt,A.J., Pallister,C.J.
            and Cowell,D.C.
  TITLE     Characterization and purification of the vitamin K1 2,3 epoxide
            reductases system from rat liver
  JOURNAL   J Pharm Pharmacol 53 (4), 481-486 (2001)
   PUBMED   11341364
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Silverman,R.B. and Nandi,D.L.
  TITLE     Effect of N-ethylmaleimide on beef and rat liver vitamin K1 epoxide
            reductase
  JOURNAL   J Enzyme Inhib 3 (4), 289-294 (1990)
   PUBMED   2319331
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Matsubara,T., Touchi,A., Harauchi,T., Takano,K. and Yoshizaki,T.
  TITLE     Depression of liver microsomal vitamin K epoxide reductase activity
            associated with antibiotic-induced coagulopathy
  JOURNAL   Biochem Pharmacol 38 (16), 2693-2701 (1989)
   PUBMED   2764989
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB314647.1, AY423047.1 and
            AW253787.1.
            
            On Mar 30, 2004 this sequence version replaced XP_219366.1.
            
            Summary: Vitamin K is essential for blood clotting but must be
            enzymatically activated. This enzymatically activated form of
            vitamin K is a reduced form required for the carboxylation of
            glutamic acid residues in some blood-clotting proteins. The product
            of this gene encodes the enzyme that is responsible for reducing
            vitamin K 2,3-epoxide to the enzymatically activated form. Fatal
            bleeding can be caused by vitamin K deficiency and by the vitamin K
            antagonist warfarin, and it is the product of this gene that is
            sensitive to warfarin. In humans, mutations in this gene can be
            associated with deficiencies in vitamin-K-dependent clotting
            factors and, in humans and rats, with warfarin resistance.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ210919.1, EV779143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..161
                     /product="vitamin K epoxide reductase complex subunit 1"
                     /EC_number="1.17.4.4"
                     /note="vitamin K1 epoxide reductase (warfarin-sensitive);
                     phylloquinone epoxide reductase; vitamin K1 2,3-epoxide
                     reductase subunit 1; Warfarin resistance"
                     /calculated_mol_wt=17652
     Site            10..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TEK4.1)"
     Region          25..149
                     /region_name="VKOR_euk"
                     /note="Vitamin K epoxide reductase family in eukaryotes,
                     excluding plants; cd12917"
                     /db_xref="CDD:240600"
     Site            order(43,51,57,132,135)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:240600"
     Site            81..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TEK4.1)"
     Site            101..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TEK4.1)"
     Site            132..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TEK4.1)"
     Site            132..135
                     /site_type="active"
                     /note="redox center [active]"
                     /db_xref="CDD:240600"
     CDS             1..161
                     /gene="Vkorc1"
                     /coded_by="NM_203335.2:23..508"
                     /db_xref="GeneID:309004"
                     /db_xref="RGD:1303107"
ORIGIN      
        1 mgttwrspgr lrlalclagl alslyalhvk aararnedyr alcdvgtais csrvfssrwg
       61 rgfglvehvl gadsilnqsn sifgcmfyti qlllgclrgr wasillilss lvsvagslyl
      121 awilffvlyd fcivcittya inaglmllsf qkvpehkvkk p
//
LOCUS       NP_001164004             727 aa            linear   ROD 28-APR-2025
DEFINITION  protein polyglycylase TTLL10 isoform 1 [Rattus norvegicus].
ACCESSION   NP_001164004
VERSION     NP_001164004.1
DBSOURCE    REFSEQ: accession NM_001170533.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Rogowski,K., Juge,F., van Dijk,J., Wloga,D., Strub,J.M.,
            Levilliers,N., Thomas,D., Bre,M.H., Van Dorsselaer,A., Gaertig,J.
            and Janke,C.
  TITLE     Evolutionary divergence of enzymatic mechanisms for
            posttranslational polyglycylation
  JOURNAL   Cell 137 (6), 1076-1087 (2009)
   PUBMED   19524510
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC097417.1, CK653520.1 and BC083833.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..727
                     /product="protein polyglycylase TTLL10 isoform 1"
                     /EC_number="6.-.-.-"
                     /note="protein polyglycylase TTLL10; tubulin--tyrosine
                     ligase-like protein 10; tubulin tyrosine ligase-like
                     family, member 10"
                     /calculated_mol_wt=82650
     Region          <53..125
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          323..576
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     CDS             1..727
                     /gene="Ttll10"
                     /coded_by="NM_001170533.1:99..2282"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:298692"
                     /db_xref="RGD:1560839"
ORIGIN      
        1 mfkriscsyr gviscqslyl nsrhrghthr gqdslgrrkl trqrrdakmp lhpparrphg
       61 hrrngseaqt eattqdtgrl scprrvgaav cpiqglghra arrprrgvgt tsasraprpg
      121 almpatrnrp rfihyrvqpp rthvsfkrpk rsrthqshtk vpgwthekrm gssveeglrp
      181 elsqleqdad nlgeeeaarl pvtslngllm egdrhpnpgq gpffyiggtn gasiisnyce
      241 skgwqrtqds rcedyklkwc eikcrdnycs fregqqllfq lpnnkllttk igllsalreh
      301 artlskarlm pstqakvlkm deffpetyrl dirderqaff tlfdetqmwi ckptasnqgk
      361 giflirsqee aaalqaktqs ieddpiyrkm pfrapqarvv qryvqnplll dgkkfdvrsy
      421 mliacampym vffghgyarl tlslynphss dlsghltnqf mqkksplyml lkdstvwsme
      481 hlnryindkf rkskglprdw vfttftkrmq qimshcflav ksklecklgy fdligcdfli
      541 denfkvwlle mnsnpalhtn cevlkevipg vvmetldlal etcqkslhsq kmlplqsqrr
      601 fvllyngett dlwprlgssr ppirlpyans nharstceis sssltstrvt iadrpaarks
      661 mssrtapica srksrlsdsg gvsieesets vcsglpegsr daarepslgp teeereeeqr
      721 stshrgs
//
LOCUS       NP_112372                158 aa            linear   ROD 28-APR-2025
DEFINITION  small ribosomal subunit protein uS17 [Rattus norvegicus].
ACCESSION   NP_112372
VERSION     NP_112372.1
DBSOURCE    REFSEQ: accession NM_031110.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   5  (residues 1 to 158)
  AUTHORS   O'Donohue,M.F., Choesmel,V., Faubladier,M., Fichant,G. and
            Gleizes,P.E.
  TITLE     Functional dichotomy of ribosomal proteins during the synthesis of
            mammalian 40S ribosomal subunits
  JOURNAL   J Cell Biol 190 (5), 853-866 (2010)
   PUBMED   20819938
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Yu,Y., Ji,H., Doudna,J.A. and Leary,J.A.
  TITLE     Mass spectrometric analysis of the human 40S ribosomal subunit:
            native and HCV IRES-bound complexes
  JOURNAL   Protein Sci 14 (6), 1438-1446 (2005)
   PUBMED   15883184
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Tanaka,T., Kuwano,Y., Ishikawa,K. and Ogata,K.
  TITLE     Nucleotide sequence of cloned cDNA specific for rat ribosomal
            protein S11
  JOURNAL   J Biol Chem 260 (10), 6329-6333 (1985)
   PUBMED   3838984
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Collatz,E., Ulbrich,N., Tsurugi,K., Lightfoot,H.N., MacKinlay,W.,
            Lin,A. and Wool,I.G.
  TITLE     Isolation of eukaryotic ribosomal proteins. Purification and
            characterization of the 40 S ribosomal subunit proteins Sa, Sc,
            S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18,
            S19, S20, S21, S26, S27', and S29
  JOURNAL   J Biol Chem 252 (24), 9071-9080 (1977)
   PUBMED   925037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from K03250.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: K03250.1, FQ221188.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132276, SAMD00132291
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..158
                     /product="small ribosomal subunit protein uS17"
                     /note="40S ribosomal protein S11"
                     /calculated_mol_wt=18300
     Region          1..158
                     /region_name="PTZ00241"
                     /note="40S ribosomal protein S11; Provisional"
                     /db_xref="CDD:240326"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.2;
                     propagated from UniProtKB/Swiss-Prot (P62282.3)"
     Site            38
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62280; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     Site            45
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62280; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62281; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62280; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     Site            69
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P62281; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62280; propagated from
                     UniProtKB/Swiss-Prot (P62282.3)"
     CDS             1..158
                     /gene="Rps11"
                     /coded_by="NM_031110.1:3..479"
                     /db_xref="GeneID:81774"
                     /db_xref="RGD:621026"
ORIGIN      
        1 madiqteray qkqptifqnk krvllgetgk eklpryykni glgfktpkea iegtyidkkc
       61 pftgnvsirg rilsgvvtkm kmqrtivirr dylhyirkyn rfekrhknms vhlspcfrdv
      121 qigdivtvge crplsktvrf nvlkvtkaag tkkqfqkf
//
LOCUS       NP_001013921             612 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquilin-like protein [Rattus norvegicus].
ACCESSION   NP_001013921 XP_219040
VERSION     NP_001013921.1
DBSOURCE    REFSEQ: accession NM_001013899.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083634.1.
            
            On Apr 20, 2005 this sequence version replaced XP_219040.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC083634.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..612
                     /product="ubiquilin-like protein"
                     /calculated_mol_wt=67664
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIP4.1)"
     Region          31..101
                     /region_name="Ubl_PLICs"
                     /note="ubiquitin-like (Ubl) domain found in eukaryotic
                     protein linking integrin-associated protein (IAP, also
                     known as CD47) with cytoskeleton (PLIC) proteins; cd01808"
                     /db_xref="CDD:340506"
     Site            order(36,73..78,94..97,99,101)
                     /site_type="other"
                     /note="Pru interaction site [polypeptide binding]"
                     /db_xref="CDD:340506"
     Site            order(66,69,73,75..78,80,97,99..101)
                     /site_type="other"
                     /note="putative S5a binding site"
                     /db_xref="CDD:340506"
     Region          569..606
                     /region_name="UBA_PLICs"
                     /note="UBA domain of eukaryotic protein linking
                     integrin-associated protein (IAP, also known as CD47) with
                     cytoskeleton (PLIC) proteins; cd14399"
                     /db_xref="CDD:270582"
     Site            order(579..584,600,603..605)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270582"
     CDS             1..612
                     /gene="Ubqlnl"
                     /gene_synonym="RGD1307202"
                     /coded_by="NM_001013899.1:212..2050"
                     /db_xref="GeneID:293287"
                     /db_xref="RGD:1307202"
ORIGIN      
        1 mphiisrspr mpqsrhpagv padgnippgv irvivktpgn qnvftvaedt svrqfkeqls
       61 shfkcqmeql vlvsmgrllk dhdtlsqrgi tdghtihvvi kskhgsrslt hsfrnlltnn
      121 pchqdrnpkg nsstvcqsag msetkvessi lmepdaskvc tqdpevgspe qieqmletlc
      181 vqrllsnmff mhqlppehpd mqdliqqnpe vshlldnsei lcqtlelarh laiiqeimqi
      241 qqpaqnpeht lnpqpylgle tipngnivlg qgydnfndhm lngvhvhdll eddsftalla
      301 eqvleqvqtp slcqpppqeq wgqlsssqvi fanscgfltt pteanlnttn nasrenpaia
      361 atqgqsnvca vqqpteipsl ctipviqepr egdkdttipq gssaqwleed lqqseeqsss
      421 qitrsmiqll rthphmaaem llllnppqln eqwrqqtatp lqssqlsdll lalanpktsq
      481 allqiehglq llateapall pyiepylwgl gwlipsscdy ldtvpwtwnv qdtvepqcpe
      541 schksgtvlq reqplsgdss hslqapevrf skemeclqam gfvnynanlq aliatdgdtn
      601 aaihklkasq gf
//
LOCUS       NP_955429                426 aa            linear   ROD 28-APR-2025
DEFINITION  pannexin-1 isoform a [Rattus norvegicus].
ACCESSION   NP_955429 XP_235835
VERSION     NP_955429.1
DBSOURCE    REFSEQ: accession NM_199397.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Fukuyama,K., Motomura,E. and Okada,M.
  TITLE     Age-Dependent Activation of Pannexin1 Function Contributes to the
            Development of Epileptogenesis in Autosomal Dominant Sleep-related
            Hypermotor Epilepsy Model Rats
  JOURNAL   Int J Mol Sci 25 (3), 1619 (2024)
   PUBMED   38338895
  REMARK    GeneRIF: Age-Dependent Activation of Pannexin1 Function Contributes
            to the Development of Epileptogenesis in Autosomal Dominant
            Sleep-related Hypermotor Epilepsy Model Rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Kurisu,R., Saigusa,T., Aono,Y., Hayashi,Y., Hitomi,S., Shimada,M.,
            Iwata,K. and Shinoda,M.
  TITLE     Pannexin 1 role in the trigeminal ganglion in infraorbital nerve
            injury-induced mechanical allodynia
  JOURNAL   Oral Dis 29 (4), 1770-1781 (2023)
   PUBMED   35029007
  REMARK    GeneRIF: Pannexin 1 role in the trigeminal ganglion in infraorbital
            nerve injury-induced mechanical allodynia.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Liu,Y., Qu,H.Q., Chang,X., Qu,J., Mentch,F.D., Nguyen,K., Tian,L.,
            Glessner,J., Sleiman,P.M.A. and Hakonarson,H.
  TITLE     Mutation burden analysis of six common mental disorders in African
            Americans by whole genome sequencing
  JOURNAL   Hum Mol Genet 31 (22), 3769-3776 (2022)
   PUBMED   35642741
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Luetic,M., Kretzschmar,G., Grobe,M., Jercic,L., Bota,I., Ivic,V.,
            Balog,M., Zjalic,M., Vitlov Uljevic,M., Heffer,M., Gaspar,R.,
            Tabi,T., Vukojevic,K., Vari,S.G. and Filipovic,N.
  TITLE     Sex-specific effects of metformin and liraglutide on renal
            pathology and expression of connexin 45 and pannexin 1 following
            long-term high-fat high-sugar diet
  JOURNAL   Acta Histochem 123 (8), 151817 (2021)
   PUBMED   34808525
  REMARK    GeneRIF: Sex-specific effects of metformin and liraglutide on renal
            pathology and expression of connexin 45 and pannexin 1 following
            long-term high-fat high-sugar diet.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Koyama,R., Iwata,K., Hayashi,Y., Hitomi,S., Shibuta,I.,
            Furukawa,A., Asano,S., Kaneko,T., Yonehara,Y. and Shinoda,M.
  TITLE     Pannexin 1-Mediated ATP Signaling in the Trigeminal Spinal
            Subnucleus Caudalis Is Involved in Tongue Cancer Pain
  JOURNAL   Int J Mol Sci 22 (21), 11404 (2021)
   PUBMED   34768835
  REMARK    GeneRIF: Pannexin 1-Mediated ATP Signaling in the Trigeminal Spinal
            Subnucleus Caudalis Is Involved in Tongue Cancer Pain.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Boassa,D., Ambrosi,C., Qiu,F., Dahl,G., Gaietta,G. and Sosinsky,G.
  TITLE     Pannexin1 channels contain a glycosylation site that targets the
            hexamer to the plasma membrane
  JOURNAL   J Biol Chem 282 (43), 31733-31743 (2007)
   PUBMED   17715132
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Pelegrin,P. and Surprenant,A.
  TITLE     Pannexin-1 mediates large pore formation and interleukin-1beta
            release by the ATP-gated P2X7 receptor
  JOURNAL   EMBO J 25 (21), 5071-5082 (2006)
   PUBMED   17036048
  REMARK    GeneRIF: pannexin-1 is required for processing of caspase-1 and
            release of mature IL-1beta induced by P2X(7) receptor activation.
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Vanden Abeele,F., Bidaux,G., Gordienko,D., Beck,B., Panchin,Y.V.,
            Baranova,A.V., Ivanov,D.V., Skryma,R. and Prevarskaya,N.
  TITLE     Functional implications of calcium permeability of the channel
            formed by pannexin 1
  JOURNAL   J Cell Biol 174 (4), 535-546 (2006)
   PUBMED   16908669
  REMARK    Erratum:[J Cell Biol. 2013 May 27;201(5):777]
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Dvoriantchikova,G., Ivanov,D., Panchin,Y. and Shestopalov,V.I.
  TITLE     Expression of pannexin family of proteins in the retina
  JOURNAL   FEBS Lett 580 (9), 2178-2182 (2006)
   PUBMED   16616526
  REMARK    GeneRIF: Panx1 and Panx2 are abundantly expressed in the retina,
            and may therefore contribute to the electrical and metabolic
            coupling, or to signaling between retinal neurons
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Bruzzone,R., Hormuzdi,S.G., Barbe,M.T., Herb,A. and Monyer,H.
  TITLE     Pannexins, a family of gap junction proteins expressed in brain
  JOURNAL   Proc Natl Acad Sci U S A 100 (23), 13644-13649 (2003)
   PUBMED   14597722
  REMARK    GeneRIF: the different expression patterns of pannexin 1 (Panx1)
            and pannexin 2 (Panx2) in the brain indicate that pannexins form
            cell type-specific gap junctions with distinct properties that may
            subserve different functions.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000008.1 and
            BM385439.1.
            
            On Jan 12, 2004 this sequence version replaced XP_235835.2.
            
            Summary: The protein encoded by this gene is a plasma membrane
            protein that is a structural component of gap junctions. The
            encoded protein acts as a homodimer or as a heterodimer with other
            isoforms or proteins. Two additional variants have been found, and
            the isoforms expressed from them are found in the cytoplasm. It is
            thought that these two isoforms could attenuate the actions of the
            membrane-bound protein. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ557015.1, SRR26643288.32796.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN12840110,
                                           SAMN12840111 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q12"
     Protein         1..426
                     /product="pannexin-1 isoform a"
                     /note="pannexin-1"
                     /calculated_mol_wt=47942
     mat_peptide     1..378
                     /product="Caspase-activated pannexin-1.
                     /evidence=ECO:0000250|UniProtKB:Q96RD7.
                     /id=PRO_0000460044"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
                     /calculated_mol_wt=42819
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIP4; propagated from
                     UniProtKB/Swiss-Prot (P60570.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
     Site            254
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P60570.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
     Site            375..378
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3 or CASP7.
                     /evidence=ECO:0000250|UniProtKB:Q96RD7; propagated from
                     UniProtKB/Swiss-Prot (P60570.1)"
     Region          407..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60570.1)"
     CDS             1..426
                     /gene="Panx1"
                     /gene_synonym="px1"
                     /coded_by="NM_199397.2:435..1715"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:315435"
                     /db_xref="RGD:735204"
ORIGIN      
        1 maiahlatey vfsdfllkep tepkfkglrl elavdkmvtc iavglpllli slafaqeisi
       61 gtqiscfsps sfswrqaafv dsycwaavqq knslqsesgn lplwlhkffp yilllfaill
      121 ylpalfwrfa aaphlcsdlk fimeeldkvy nraikaaksa rdldlrdgpg ppgvtenvgq
      181 slweiseshf kypiveqylk tkknsshlim kyiscrlvtf avvllaciyl syyfslssls
      241 deflcsiksg vlrndstipd sfqckliavg ifqllslinl lvyallvpvv iytlfvpfrq
      301 ktdvlkvyei lptfdvlhfk segyndlsly nlfleenise lksykclkvl eniksngqgi
      361 dpmllltnlg mikmdvidgk vpmslqtkge dqgsqrmdfk dldlssetaa nngeknsrqr
      421 llnssc
//
LOCUS       NP_001076043             656 aa            linear   ROD 28-APR-2025
DEFINITION  FAST kinase domain-containing protein 3, mitochondrial precursor
            [Rattus norvegicus].
ACCESSION   NP_001076043 XP_001058032 XP_214418
VERSION     NP_001076043.1
DBSOURCE    REFSEQ: accession NM_001082574.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Boehm,E., Zornoza,M., Jourdain,A.A., Delmiro Magdalena,A.,
            Garcia-Consuegra,I., Torres Merino,R., Orduna,A., Martin,M.A.,
            Martinou,J.C., De la Fuente,M.A. and Simarro,M.
  TITLE     Role of FAST Kinase Domains 3 (FASTKD3) in Post-transcriptional
            Regulation of Mitochondrial Gene Expression
  JOURNAL   J Biol Chem 291 (50), 25877-25887 (2016)
   PUBMED   27789713
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Simarro,M., Gimenez-Cassina,A., Kedersha,N., Lazaro,J.B.,
            Adelmant,G.O., Marto,J.A., Rhee,K., Tisdale,S., Danial,N.,
            Benarafa,C., Orduna,A. and Anderson,P.
  TITLE     Fast kinase domain-containing protein 3 is a mitochondrial protein
            essential for cellular respiration
  JOURNAL   Biochem Biophys Res Commun 401 (3), 440-446 (2010)
   PUBMED   20869947
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CK359441.1 and
            BC079475.1.
            
            On or before Mar 11, 2007 this sequence version replaced
            XP_001058032.1, XP_214418.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760400,
                              SAMN16676786 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..656
                     /product="FAST kinase domain-containing protein 3,
                     mitochondrial precursor"
                     /note="FAST kinase domain-containing protein 3,
                     mitochondrial"
                     /calculated_mol_wt=75117
     Region          122..416
                     /region_name="RESC6-like"
                     /note="RNA-editing substrate-binding complex subunit 6
                     (RESC6) and related proteins; cl46254"
                     /db_xref="CDD:480594"
     Region          404..475
                     /region_name="FAST_1"
                     /note="FAST kinase-like protein, subdomain 1; pfam06743"
                     /db_xref="CDD:461999"
     Region          486..576
                     /region_name="FAST_2"
                     /note="FAST kinase-like protein, subdomain 2; pfam08368"
                     /db_xref="CDD:462448"
     Region          589..646
                     /region_name="RAP"
                     /note="This domain is found in various eukaryotic species,
                     particularly in apicomplexans; smart00952"
                     /db_xref="CDD:214932"
     CDS             1..656
                     /gene="Fastkd3"
                     /gene_synonym="RGD1309729"
                     /coded_by="NM_001082574.1:49..2019"
                     /db_xref="GeneID:290946"
                     /db_xref="RGD:1309729"
ORIGIN      
        1 maftlrrafc hmsvfwmpga vvalkihpan nvqkavrdcl rvwfcslqpd lfrvrfyhay
       61 cksfhsengn dlhpvgepwf sqaqvwnqpe qtlknedeem lsrrlnsfas feevlsfiht
      121 ldtlpvtlas aallriceig krddeqrlpk evlenrvfqa lclrcerdps hltnavlvtv
      181 lqslvidpqs slvlslvaec qrrlrrgsle vhhlcvlges larlqgasce ilklvicqlq
      241 senletfape divsvyrilq acpeevdkhq tflntvnnfs lsivsylspk sishvltalv
      301 aldqtharpl liklgksvvr yiprftneel rqvleafvyf ghsdrfftea leqhvaaqcf
      361 sldpavassv meycsrkril skpifdvvae ifvcqsekfs psqiseliep fgklnylppn
      421 apalfrkven vlfahlrhfp pkmllrllhs cslierhpvn fmskifspff lqrlqgkesy
      481 ldrlslaqmt qlfltsvlec pfykgpkllp kyqvksfltp ccsletpmdl hlyksvvigl
      541 idllgsrlyf askvltpyyy tidveiklde dgfvlpftvd edvhtrvalc idgpqrfclg
      601 skhllgkeai kqrhlrllgy qvvqvpyhel elltsrlelv dylqrklfsq sstvhw
//
LOCUS       NP_036901                619 aa            linear   ROD 28-APR-2025
DEFINITION  guanylate cyclase soluble subunit beta-1 [Rattus norvegicus].
ACCESSION   NP_036901
VERSION     NP_036901.2
DBSOURCE    REFSEQ: accession NM_012769.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Galley,J.C., Miller,M.P., Sanker,S., Liu,M., Sharina,I., Martin,E.,
            Gomez,D. and Straub,A.C.
  TITLE     FoxO4 controls sGCbeta transcription in vascular smooth muscle
  JOURNAL   Am J Physiol Heart Circ Physiol 322 (3), H417-H426 (2022)
   PUBMED   35089807
  REMARK    GeneRIF: FoxO4 controls sGCbeta transcription in vascular smooth
            muscle.
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Wang,X., Du,W., Li,M., Zhang,Y., Li,H., Sun,K., Liu,J., Dong,P.,
            Meng,X., Yi,W., Yang,L., Zhao,R. and Hu,J.
  TITLE     The beta subunit of soluble guanylyl cyclase GUCY1B3 exerts
            cardioprotective effects against ischemic injury via the
            PKCepsilon/Akt pathway
  JOURNAL   J Cell Biochem 120 (3), 3071-3081 (2019)
   PUBMED   30485489
  REMARK    GeneRIF: GUCY1B3 was upregulated in neonatal rat ventricular
            myocytes in response to ischemia and reperfusion (IR) injury, and
            restored IR-induced cell death and apoptosis. Other results suggest
            that GUCY1B3 has an antiapoptotic effect and this effect is
            mediated by the activation of PKCepsilon and Akt.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Sagi,Y., Heiman,M., Peterson,J.D., Musatov,S., Scarduzio,M.,
            Logan,S.M., Kaplitt,M.G., Surmeier,D.J., Heintz,N. and Greengard,P.
  TITLE     Nitric oxide regulates synaptic transmission between spiny
            projection neurons
  JOURNAL   Proc Natl Acad Sci U S A 111 (49), 17636-17641 (2014)
   PUBMED   25413364
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Apr 7;112(14):E1811. doi:
            10.1073/pnas.1504794112. PMID: 25787251]
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Allerston,C.K., von Delft,F. and Gileadi,O.
  TITLE     Crystal structures of the catalytic domain of human soluble
            guanylate cyclase
  JOURNAL   PLoS One 8 (3), e57644 (2013)
   PUBMED   23505436
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Peregud,D.I., Yakovlev,A.A., Stepanichev,M.Y., Onufriev,M.V.,
            Panchenko,L.F. and Gulyaeva,N.V.
  TITLE     Content of mRNA for NMDA glutamate receptor subunits in the frontal
            cortex and striatum of rats after morphine withdrawal is related to
            the degree of abstinence
  JOURNAL   Bull Exp Biol Med 153 (6), 835-838 (2012)
   PUBMED   23113297
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Russwurm,M., Wittau,N. and Koesling,D.
  TITLE     Guanylyl cyclase/PSD-95 interaction: targeting of the nitric
            oxide-sensitive alpha2beta1 guanylyl cyclase to synaptic membranes
  JOURNAL   J Biol Chem 276 (48), 44647-44652 (2001)
   PUBMED   11572861
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Koike,G., Chiche,J.D., Shiozawa,M., Simon,J.S., Szpirer,J.,
            Jacob,H.J., Szpirer,C. and Bloch,K.D.
  TITLE     Localization of rat genes in the nitric oxide signaling pathway:
            candidates for the pathogenesis of complex diseases
  JOURNAL   Mamm Genome 10 (1), 71-73 (1999)
   PUBMED   9892738
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Guala,A., Mittino,D., Ghini,T. and Quazza,G.
  TITLE     [Are metoclopramide dystonias familial?]
  JOURNAL   Pediatr Med Chir 14 (6), 617-618 (1992)
   PUBMED   1298936
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Nakane,M., Saheki,S., Kuno,T., Ishii,K. and Murad,F.
  TITLE     Molecular cloning of a cDNA coding for 70 kilodalton subunit of
            soluble guanylate cyclase from rat lung
  JOURNAL   Biochem Biophys Res Commun 157 (3), 1139-1147 (1988)
   PUBMED   2905128
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Arnold,W.P., Mittal,C.K., Katsuki,S. and Murad,F.
  TITLE     Nitric oxide activates guanylate cyclase and increases guanosine
            3':5'-cyclic monophosphate levels in various tissue preparations
  JOURNAL   Proc Natl Acad Sci U S A 74 (8), 3203-3207 (1977)
   PUBMED   20623
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081840.1.
            
            On Sep 16, 2004 this sequence version replaced NP_036901.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081840.1, M22562.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..619
                     /product="guanylate cyclase soluble subunit beta-1"
                     /EC_number="4.6.1.2"
                     /note="guanylate cyclase 1, soluble, beta 3; soluble
                     guanylyl cyclase beta 1 subunit; GCS-beta-1; soluble
                     guanylate cyclase small subunit; GCS-beta-3; guanylate
                     cyclase soluble subunit beta-3; guanylate cyclase 1
                     soluble subunit beta 3; guanylate cyclase, soluble, beta
                     1"
                     /calculated_mol_wt=70326
     Region          2..166
                     /region_name="HNOB"
                     /note="Haem-NO-binding; pfam07700"
                     /db_xref="CDD:462233"
     Region          207..406
                     /region_name="HNOBA"
                     /note="Heme NO binding associated; pfam07701"
                     /db_xref="CDD:462234"
     Region          412..605
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(424,426..431,473,475..477,480,541..543,547..548,
                     551..552,593)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(426,477)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(431,447,450..451,454,458,473..474,529,532,542..545,
                     548,593)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..619
                     /gene="Gucy1b1"
                     /gene_synonym="Gucy1b3; SGC"
                     /coded_by="NM_012769.2:89..1948"
                     /db_xref="GeneID:25202"
                     /db_xref="RGD:2769"
ORIGIN      
        1 mygfvnhale llvirnygpe vwedikkeaq ldeegqflvr iiyddsktyd lvaaaskvln
       61 lnageilqmf gkmffvfcqe sgydtilrvl gsnvreflqn ldalhdhlat iypgmrapsf
      121 rctdaekgkg lilhyysere glqdivigii ktvaqqihgt eidmkviqqr seecdhtqfl
      181 ieekeskeed fyedldrfee ngtqdsrisp ytfckafpfh iifdrdlvvt qcgnaiyrvl
      241 pqlqpgkcsl lsvfslvrph idisfhgils hintvfvlrs keglldvekl ecedeltgae
      301 isclrlkgqm iylpeadsil flcspsvmnl ddltrrglyl sdiplhdatr dlvllgeqfr
      361 eeykltqele iltdrlqltl raledekkkt dtllysvlpp svanelrhkr pvpakrydnv
      421 tilfsgivgf nafcskhasg egamkivnll ndlytrfdtl tdsrknpfvy kvetvgdkym
      481 tvsglpepci hharsichla ldmmeiagqv qvdgesvqit igihtgevvt gvigqrmpry
      541 clfgntvnlt srtettgekg kinvseytyr clmspensdp qfhlehrgpv smkgkkepmq
      601 vwflsrkntg teetnqden
//
LOCUS       NP_072120                177 aa            linear   ROD 28-APR-2025
DEFINITION  CCHC-type zinc finger nucleic acid binding protein [Rattus
            norvegicus].
ACCESSION   NP_072120
VERSION     NP_072120.1
DBSOURCE    REFSEQ: accession NM_022598.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Chen,S., Su,L., Qiu,J., Xiao,N., Lin,J., Tan,J.H., Ou,T.M.,
            Gu,L.Q., Huang,Z.S. and Li,D.
  TITLE     Mechanistic studies for the role of cellular nucleic-acid-binding
            protein (CNBP) in regulation of c-myc transcription
  JOURNAL   Biochim Biophys Acta 1830 (10), 4769-4777 (2013)
   PUBMED   23774591
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Massa,R., Panico,M.B., Caldarola,S., Fusco,F.R., Sabatelli,P.,
            Terracciano,C., Botta,A., Novelli,G., Bernardi,G. and Loreni,F.
  TITLE     The myotonic dystrophy type 2 (DM2) gene product zinc finger
            protein 9 (ZNF9) is associated with sarcomeres and normally
            localized in DM2 patients' muscles
  JOURNAL   Neuropathol Appl Neurobiol 36 (4), 275-284 (2010)
   PUBMED   20102514
  REMARK    GeneRIF: findings showed that ZNF9 is ubiquitously expressed in
            mammalian tissues, and that its signal is not substantially
            modified in myotonic dystrophy type 2 muscles
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Chen,W., Wang,Y., Abe,Y., Cheney,L., Udd,B. and Li,Y.P.
  TITLE     Haploinsuffciency for Znf9 in Znf9+/- mice is associated with
            multiorgan abnormalities resembling myotonic dystrophy
  JOURNAL   J Mol Biol 368 (1), 8-17 (2007)
   PUBMED   17335846
  REMARK    GeneRIF: Znf9 haploinsufficiency contributes to the myotonic
            dystrophy phenotype in Znf9+/- mice.
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Tsuji,A.B., Sugyo,A., Ogiu,T., Sagara,M., Kimura,T., Ishikawa,A.,
            Sudo,H., Ohtsuki,M., Aburatani,H., Imai,T. and Harada,Y.N.
  TITLE     Fine mapping of radiation susceptibility and gene expression
            analysis of LEC congenic rat lines
  JOURNAL   Genomics 86 (3), 271-279 (2005)
   PUBMED   15978772
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Shimizu,K., Chen,W., Ashique,A.M., Moroi,R. and Li,Y.P.
  TITLE     Molecular cloning, developmental expression, promoter analysis and
            functional characterization of the mouse CNBP gene
  JOURNAL   Gene 307, 51-62 (2003)
   PUBMED   12706888
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Yasuda,J., Mashiyama,S., Makino,R., Ohyama,S., Sekiya,T. and
            Hayashi,K.
  TITLE     Cloning and characterization of rat cellular nucleic acid binding
            protein (CNBP) cDNA
  JOURNAL   DNA Res 2 (1), 45-49 (1995)
   PUBMED   7788528
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Warden,C.H., Krisans,S.K., Purcell-Huynh,D., Leete,L.M.,
            Daluiski,A., Diep,A., Taylor,B.A. and Lusis,A.J.
  TITLE     Mouse cellular nucleic acid binding proteins: a highly conserved
            family identified by genetic mapping and sequencing
  JOURNAL   Genomics 24 (1), 14-19 (1994)
   PUBMED   7896269
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D45254.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D45254.1, BC062225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..177
                     /product="CCHC-type zinc finger nucleic acid binding
                     protein"
                     /note="zinc finger protein 9 (a cellular retroviral
                     nucleic acid binding protein); cellular nucleic
                     acid-binding protein; cellular nucleic acid binding
                     protein 1"
                     /calculated_mol_wt=19332
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62633; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53996; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     Region          25..38
                     /region_name="RNA-binding Arg/Gly-rich region (RGG-box).
                     /evidence=ECO:0000250|UniProtKB:P62633"
                     /note="propagated from UniProtKB/Swiss-Prot (P62634.1)"
     Site            25
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:P62633; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     Site            27
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000250|UniProtKB:P62633; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53996; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     Region          54..171
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Site            79
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P62633; propagated from
                     UniProtKB/Swiss-Prot (P62634.1)"
     CDS             1..177
                     /gene="Cnbp"
                     /gene_synonym="Cnbp1; Znf9"
                     /coded_by="NM_022598.1:166..699"
                     /db_xref="GeneID:64530"
                     /db_xref="RGD:621807"
ORIGIN      
        1 mssnecfkcg rsghwarecp tgggrgrgmr srgrggftsd rgfqfvsssl pdicyrcges
       61 ghlakdcdlq edacyncgrg ghiakdckep krereqccyn cgkpghlard cdhadeqkcy
      121 scgefghiqk dctkvkcyrc getghvainc sktsevncyr cgesghlare ctieata
//
LOCUS       NP_955422                579 aa            linear   ROD 28-APR-2025
DEFINITION  folliculin [Rattus norvegicus].
ACCESSION   NP_955422 XP_220518 XP_340809
VERSION     NP_955422.1
DBSOURCE    REFSEQ: accession NM_199390.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Shen,K., Rogala,K.B., Chou,H.T., Huang,R.K., Yu,Z. and
            Sabatini,D.M.
  TITLE     Cryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex
  JOURNAL   Cell 179 (6), 1319-1329 (2019)
   PUBMED   31704029
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Lawrence,R.E., Fromm,S.A., Fu,Y., Yokom,A.L., Kim,D.J.,
            Thelen,A.M., Young,L.N., Lim,C.Y., Samelson,A.J., Hurley,J.H. and
            Zoncu,R.
  TITLE     Structural mechanism of a Rag GTPase activation checkpoint by the
            lysosomal folliculin complex
  JOURNAL   Science 366 (6468), 971-977 (2019)
   PUBMED   31672913
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Meng,J. and Ferguson,S.M.
  TITLE     GATOR1-dependent recruitment of FLCN-FNIP to lysosomes coordinates
            Rag GTPase heterodimer nucleotide status in response to amino acids
  JOURNAL   J Cell Biol 217 (8), 2765-2776 (2018)
   PUBMED   29848618
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Wada,S., Neinast,M., Jang,C., Ibrahim,Y.H., Lee,G., Babu,A., Li,J.,
            Hoshino,A., Rowe,G.C., Rhee,J., Martina,J.A., Puertollano,R.,
            Blenis,J., Morley,M., Baur,J.A., Seale,P. and Arany,Z.
  TITLE     The tumor suppressor FLCN mediates an alternate mTOR pathway to
            regulate browning of adipose tissue
  JOURNAL   Genes Dev 30 (22), 2551-2564 (2016)
   PUBMED   27913603
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Yan,M., Audet-Walsh,E., Manteghi,S., Dufour,C.R., Walker,B.,
            Baba,M., St-Pierre,J., Giguere,V. and Pause,A.
  TITLE     Chronic AMPK activation via loss of FLCN induces functional beige
            adipose tissue through PGC-1alpha/ERRalpha
  JOURNAL   Genes Dev 30 (9), 1034-1046 (2016)
   PUBMED   27151976
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Baba,M., Hong,S.B., Sharma,N., Warren,M.B., Nickerson,M.L.,
            Iwamatsu,A., Esposito,D., Gillette,W.K., Hopkins,R.F. 3rd,
            Hartley,J.L., Furihata,M., Oishi,S., Zhen,W., Burke,T.R. Jr.,
            Linehan,W.M., Schmidt,L.S. and Zbar,B.
  TITLE     Folliculin encoded by the BHD gene interacts with a binding
            protein, FNIP1, and AMPK, and is involved in AMPK and mTOR
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15552-15557 (2006)
   PUBMED   17028174
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Togashi,Y., Kobayashi,T., Momose,S., Ueda,M., Okimoto,K. and
            Hino,O.
  TITLE     Transgenic rescue from embryonic lethality and renal carcinogenesis
            in the Nihon rat model by introduction of a wild-type Bhd gene
  JOURNAL   Oncogene 25 (20), 2885-2889 (2006)
   PUBMED   16369488
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Kouchi,M., Okimoto,K., Matsumoto,I., Tanaka,K., Yasuba,M. and
            Hino,O.
  TITLE     Natural history of the Nihon (Bhd gene mutant) rat, a novel model
            for human Birt-Hogg-Dube syndrome
  JOURNAL   Virchows Arch 448 (4), 463-471 (2006)
   PUBMED   16447066
  REMARK    GeneRIF: The Nihon rat is a useful tool for analyzing the events
            leading to renal tumorigenesis and for studying BHD gene functions.
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Okimoto,K., Sakurai,J., Kobayashi,T., Mitani,H., Hirayama,Y.,
            Nickerson,M.L., Warren,M.B., Zbar,B., Schmidt,L.S. and Hino,O.
  TITLE     A germ-line insertion in the Birt-Hogg-Dube (BHD) gene gives rise
            to the Nihon rat model of inherited renal cancer
  JOURNAL   Proc Natl Acad Sci U S A 101 (7), 2023-2027 (2004)
   PUBMED   14769940
  REMARK    GeneRIF: a germ-line mutation in the BHD gene caused by the
            insertion of a single nucleotide in the Nihon rat, results in a
            frameshift and produces a stop codon 26 aa downstream; the
            homozygous mutant condition was lethal at an early stage of fetal
            life
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Nickerson,M.L., Warren,M.B., Toro,J.R., Matrosova,V., Glenn,G.,
            Turner,M.L., Duray,P., Merino,M., Choyke,P., Pavlovich,C.P.,
            Sharma,N., Walther,M., Munroe,D., Hill,R., Maher,E., Greenberg,C.,
            Lerman,M.I., Linehan,W.M., Zbar,B. and Schmidt,L.S.
  TITLE     Mutations in a novel gene lead to kidney tumors, lung wall defects,
            and benign tumors of the hair follicle in patients with the
            Birt-Hogg-Dube syndrome
  JOURNAL   Cancer Cell 2 (2), 157-164 (2002)
   PUBMED   12204536
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085848.1.
            
            On or before Jan 12, 2004 this sequence version replaced
            XP_220518.2, XP_340809.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085848.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q22"
     Protein         1..579
                     /product="folliculin"
                     /EC_number="2.7.1.21"
                     /note="birt-Hogg-Dube syndrome protein homolog"
                     /calculated_mol_wt=63991
     Region          32..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Region          106..265
                     /region_name="Folliculin"
                     /note="Vesicle coat protein involved in Golgi to plasma
                     membrane transport; pfam11704"
                     /db_xref="CDD:463323"
     Site            164
                     /site_type="other"
                     /note="Essential for GTPase activation (GAP) activity.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Region          294..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Region          345..566
                     /region_name="Folliculin_C"
                     /note="Folliculin C-terminal domain; pfam16692"
                     /db_xref="CDD:465236"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NFG4; propagated from
                     UniProtKB/Swiss-Prot (Q76JQ2.1)"
     CDS             1..579
                     /gene="Flcn"
                     /gene_synonym="Bhd"
                     /coded_by="NM_199390.2:419..2158"
                     /db_xref="GeneID:303185"
                     /db_xref="RGD:735088"
ORIGIN      
        1 mnaivalchf celhgprtlf ctevlhaplp qgagsgdspg qveqaeeeeg giqmssrvra
       61 hspaegastd ssspgpkksd mcegcrslav ghpgyishdk etsikyvshq hpnhpqlfsi
      121 vrqacvrsls cevcpgregp iffgdeqhgf vfshtffikd slargfqrwy siiaimmdri
      181 ylinswpfll gkirgiisel qgkalkvfea eqfgcpqraq rmntaftpfl hqrngnaars
      241 ltsltsddnl waclhtsfaw llkacgsrlt ekllegapte dtlvqmekla dleeeseswd
      301 nseaeeeeka pataegaegr elascptess flsacgswqp pklsvfkslr hmrqvlgaps
      361 frmlawhvlm gnqviwksrd vnlvhsafev lrtmlpvgcv riipyssqye eayrcnflgl
      421 sppvpipahv lasefvvvve vhtatrsnph pagceddqsl skyefvvtsg spvaadrvgp
      481 tilnkmeaal tnqnlsvdvv dqclvclkee wmnkvkvlfk ftkvdsrpke dtqkllsvlg
      541 aseednvkll kfwmtglskt ykshlmstvr sptaaesrn
//
LOCUS       NP_997483                485 aa            linear   ROD 28-APR-2025
DEFINITION  carbohydrate sulfotransferase 7 precursor [Rattus norvegicus].
ACCESSION   NP_997483 XP_228417
VERSION     NP_997483.1
DBSOURCE    REFSEQ: accession NM_207600.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Thiselton,D.L., McDowall,J., Brandau,O., Ramser,J., d'Esposito,F.,
            Bhattacharya,S.S., Ross,M.T., Hardcastle,A.J. and Meindl,A.
  TITLE     An integrated, functionally annotated gene map of the DXS8026-ELK1
            interval on human Xp11.3-Xp11.23: potential hotspot for
            neurogenetic disorders
  JOURNAL   Genomics 79 (4), 560-572 (2002)
   PUBMED   11944989
  REMARK    Erratum:[Genomics 2002 Jun;79(6):891]
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Uchimura,K., Fasakhany,F., Kadomatsu,K., Matsukawa,T., Yamakawa,T.,
            Kurosawa,N. and Muramatsu,T.
  TITLE     Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular
            cloning of a novel enzyme with different distribution and
            specificities
  JOURNAL   Biochem Biophys Res Commun 274 (2), 291-296 (2000)
   PUBMED   10913333
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Kitagawa,H., Fujita,M., Ito,N. and Sugahara,K.
  TITLE     Molecular cloning and expression of a novel chondroitin
            6-O-sulfotransferase
  JOURNAL   J Biol Chem 275 (28), 21075-21080 (2000)
   PUBMED   10781596
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC111079.1.
            
            On Aug 30, 2004 this sequence version replaced XP_228417.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC111079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq11"
     Protein         1..485
                     /product="carbohydrate sulfotransferase 7 precursor"
                     /EC_number="2.8.2.17"
                     /note="chondroitin 6-sulfotransferase 7; GST-5; C6ST-2;
                     glcNAc6ST-4; chondroitin 6-sulfotransferase 2;
                     N-acetylglucosamine 6-O-sulfotransferase 1; carbohydrate
                     (N-acetylglucosamine 6-O) sulfotransferase 7;
                     galactose/N-acetylglucosamine/N-acetylglucosamine
                     6-O-sulfotransferase 5; N-acetylglucosamine
                     6-O-sulfotransferase 4"
                     /calculated_mol_wt=51102
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4008
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Region          66..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NS84; propagated from
                     UniProtKB/Swiss-Prot (Q6XQG8.1)"
     Region          465..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XQG8.1)"
     CDS             1..485
                     /gene="Chst7"
                     /gene_synonym="Gn6st-4"
                     /coded_by="NM_207600.2:112..1569"
                     /db_xref="GeneID:302302"
                     /db_xref="RGD:1303028"
ORIGIN      
        1 mkgrrrrrre yckftlllal ytlllllvps vldsgseqdk ggrdcpglqr slgvwsleaa
       61 aagereqgae vrfqaegnpd rsprpqgnls airesvtqek qhiyvhatwr tgssflgelf
      121 nqhpdvfyly epmwhlwqal ypgnaeslqg alrdmlrslf rcdfsvlrly aqpgdpaera
      181 pdsanlttam lfrwrtnkvi cspplcpaap raradvglve dkacestcpp vplraleaec
      241 rkypvvvikd vrlldlgvlv pllrdpglnl kvvqlfrdpr avhnsrlksr hgllresiqv
      301 lrtrqrgdrf qrvllahgvg arpggqsral psapradffl tsalevicea wlrdllftrg
      361 aptwlrrryl rlryedlvwq pqvqlrrllr fsglrtlaal dafafnmtrg saygadrpfh
      421 lsardareav hawrerlsqe qvrqveaacd pamrllaypr sgderdvktv rkgetpletn
      481 anwat
//
LOCUS       NP_036963                150 aa            linear   ROD 28-APR-2025
DEFINITION  CCAAT/enhancer-binding protein gamma [Rattus norvegicus].
ACCESSION   NP_036963 XP_001079636 XP_341843
VERSION     NP_036963.1
DBSOURCE    REFSEQ: accession NM_012831.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Sato,Y., Miyake,K., Kaneoka,H. and Iijima,S.
  TITLE     Sumoylation of CCAAT/enhancer-binding protein alpha and its
            functional roles in hepatocyte differentiation
  JOURNAL   J Biol Chem 281 (31), 21629-21639 (2006)
   PUBMED   16735515
  REMARK    GeneRIF: sumoylation of C/EBPalpha blocked its inhibitory effect on
            cell proliferation by leading to the disruption of a
            proliferation-inhibitory complex because of a failure of the
            sumoylated C/EBPalpha to interact with BRG1.
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Mullins,D.N., Crawford,E.L., Khuder,S.A., Hernandez,D.A., Yoon,Y.
            and Willey,J.C.
  TITLE     CEBPG transcription factor correlates with antioxidant and DNA
            repair genes in normal bronchial epithelial cells but not in
            individuals with bronchogenic carcinoma
  JOURNAL   BMC Cancer 5, 141 (2005)
   PUBMED   16255782
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Gordon,C.T., Fox,V.J., Najdovska,S. and Perkins,A.C.
  TITLE     C/EBPdelta and C/EBPgamma bind the CCAAT-box in the human
            beta-globin promoter and modulate the activity of the CACC-box
            binding protein, EKLF
  JOURNAL   Biochim Biophys Acta 1729 (1), 74-80 (2005)
   PUBMED   15833715
REFERENCE   4  (residues 1 to 150)
  AUTHORS   He,L., Ronis,M.J. and Badger,T.M.
  TITLE     Ethanol induction of class I alcohol dehydrogenase expression in
            the rat occurs through alterations in CCAAT/enhancer binding
            proteins beta and gamma
  JOURNAL   J Biol Chem 277 (46), 43572-43577 (2002)
   PUBMED   12213809
  REMARK    GeneRIF: the C/EBP site and the enhancer binding proteins beta and
            gamma are involved in rat hepatic Class I ADH gene expression in
            vivo by ethanol
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Milosavljevic,T.S., Petrovic,M.V., Cvetkovic,I.D. and Grigorov,I.I.
  TITLE     DNA binding activity of C/EBPbeta and C/EBPdelta for the rat
            alpha2-macroglobulin gene promoter is regulated in an acute-phase
            dependent manner
  JOURNAL   Biochemistry (Mosc) 67 (8), 918-926 (2002)
   PUBMED   12223092
  REMARK    GeneRIF: DNA binding activity of C/EBPbeta and C/EBPdelta for the
            rat alpha2-macroglobulin gene promoter is regulated in an
            acute-phase dependent manner
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Cooper,C., Henderson,A., Artandi,S., Avitahl,N. and Calame,K.
  TITLE     Ig/EBP (C/EBP gamma) is a transdominant negative inhibitor of C/EBP
            family transcriptional activators
  JOURNAL   Nucleic Acids Res 23 (21), 4371-4377 (1995)
   PUBMED   7501458
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Davydov,I.V., Bohmann,D., Krammer,P.H. and Li-Weber,M.
  TITLE     Cloning of the cDNA encoding human C/EBP gamma, a protein binding
            to the PRE-I enhancer element of the human interleukin-4 promoter
  JOURNAL   Gene 161 (2), 271-275 (1995)
   PUBMED   7665092
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Cooper,C., Johnson,D., Roman,C., Avitahl,N., Tucker,P. and
            Calame,K.
  TITLE     The C/EBP family of transcriptional activators is functionally
            important for Ig VH promoter activity in vivo and in vitro
  JOURNAL   J Immunol 149 (10), 3225-3231 (1992)
   PUBMED   1431100
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Thomassin,H., Hamel,D., Bernier,D., Guertin,M. and Belanger,L.
  TITLE     Molecular cloning of two C/EBP-related proteins that bind to the
            promoter and the enhancer of the alpha 1-fetoprotein gene. Further
            analysis of C/EBP beta and C/EBP gamma
  JOURNAL   Nucleic Acids Res 20 (12), 3091-3098 (1992)
   PUBMED   1377818
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Nishizawa,M. and Nagata,S.
  TITLE     cDNA clones encoding leucine-zipper proteins which interact with
            G-CSF gene promoter element 1-binding protein
  JOURNAL   FEBS Lett 299 (1), 36-38 (1992)
   PUBMED   1371974
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X64403.1.
            
            On or before May 24, 2007 this sequence version replaced
            XP_341843.3, XP_001079636.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X64403.1, BC166589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..150
                     /product="CCAAT/enhancer-binding protein gamma"
                     /note="c/EBP gamma; homolog to a human CCAAT/enhancer
                     binding protein - gamma; CCAAT/enhancer binding protein
                     (C/EBP), gamma"
                     /calculated_mol_wt=16257
     Region          27..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26801.2)"
     Region          60..120
                     /region_name="bZIP_CEBPG"
                     /note="Basic leucine zipper (bZIP) domain of
                     CCAAT/enhancer-binding protein gamma (CEBPG): a
                     DNA-binding and dimerization domain; cd14713"
                     /db_xref="CDD:269861"
     Region          62..120
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269861"
     Site            order(65..66,68..69,71..73,75..80,82,86)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269861"
     Region          66..93
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P26801.2)"
     Site            order(87,90,93..94,97..98,100..101,103..105,107..108,
                     111..112,114..115,118..119)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269861"
     Region          97..118
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P26801.2)"
     CDS             1..150
                     /gene="Cebpg"
                     /gene_synonym="C/EBP; CEBPRNA"
                     /coded_by="NM_012831.1:256..708"
                     /db_xref="GeneID:25301"
                     /db_xref="RGD:2330"
ORIGIN      
        1 msklsqpast agvngisvih tqahasglqq vpqlvpagpg gggkavppsk qskksspmdr
       61 nsdeyrqrre rnnmavkksr lkskqkaqdt lqrvnqlkee nerleakikl ltkelsvlkd
      121 lflehahnla dnvqpistet tvansdntgq
//
LOCUS       NP_001037757             468 aa            linear   ROD 28-APR-2025
DEFINITION  microtubule-associated tyrosine carboxypeptidase 1 [Rattus
            norvegicus].
ACCESSION   NP_001037757 XP_001067108 XP_001067155 XP_001067199 XP_001067251
VERSION     NP_001037757.1
DBSOURCE    REFSEQ: accession NM_001044292.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098942.1.
            
            On or before Aug 24, 2006 this sequence version replaced
            XP_001067108.1, XP_001067155.1, XP_001067251.1, XP_001067199.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132268
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..468
                     /product="microtubule-associated tyrosine carboxypeptidase
                     1"
                     /EC_number="3.4.17.17"
                     /note="microtubule-associated tyrosine carboxypeptidase"
                     /calculated_mol_wt=53372
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A9.1)"
     Region          77..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7A9.1)"
     Region          136..442
                     /region_name="DUF1704"
                     /note="Domain of unknown function (DUF1704); cl06858"
                     /db_xref="CDD:471526"
     CDS             1..468
                     /gene="Matcap1"
                     /gene_synonym="Kiaa0895l; Matcap"
                     /coded_by="NM_001044292.1:501..1907"
                     /db_xref="GeneID:688736"
                     /db_xref="RGD:1585272"
ORIGIN      
        1 mvldsgtqvy eqappsppas spsqhhklkp snrngpplyp wpqslampla lavpsalqhq
       61 tmwqtfsklh leqrshmkrs estysvnstg rrgrgkaplg rgcdpgggtl rpaaslphia
      121 kirkdvvsgs nkspcmlval rptnmdqere kffqshyayn pqfeyqepmp msvlekyqea
      181 sgqfmhqavg iikavlekfg tyenfeaatg gqlltkcqiw sivrrymqke gcvgevvvql
      241 sedllsqavm mvensrptla inltgarqyw legmlrheig thylrgvnns rqpwhstegr
      301 qqyglrpanp teeglaslhs vlfrkqpflw raallyytih qaahmsfrql fqdleqyvqd
      361 edvrweycvr akrgqtdtsl pgcfskdqvy ldgilrilrh rqtidfqllt slgkvsyedv
      421 eqlrphgvld ktrvphfmkd ldryrqqleh imttnrldea elgrllpd
//
LOCUS       NP_001013219             497 aa            linear   ROD 28-APR-2025
DEFINITION  ganglioside-induced differentiation-associated-protein 2 [Rattus
            norvegicus].
ACCESSION   NP_001013219 XP_342304
VERSION     NP_001013219.1
DBSOURCE    REFSEQ: accession NM_001013201.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Liu,H., Nakagawa,T., Kanematsu,T., Uchida,T. and Tsuji,S.
  TITLE     Isolation of 10 differentially expressed cDNAs in differentiated
            Neuro2a cells induced through controlled expression of the GD3
            synthase gene
  JOURNAL   J Neurochem 72 (5), 1781-1790 (1999)
   PUBMED   10217254
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082000.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342304.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..497
                     /product="ganglioside-induced
                     differentiation-associated-protein 2"
                     /calculated_mol_wt=56000
     Region          55..222
                     /region_name="Macro_GDAP2-like"
                     /note="macrodomain, GDAP2-like family; cd02905"
                     /db_xref="CDD:394876"
     Site            order(74,86,88,130,167..174)
                     /site_type="other"
                     /note="putative ADP-ribose binding site [chemical
                     binding]"
                     /db_xref="CDD:394876"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NXN4; propagated from
                     UniProtKB/Swiss-Prot (Q66H63.1)"
     Region          349..480
                     /region_name="CRAL_TRIO_2"
                     /note="Divergent CRAL/TRIO domain; pfam13716"
                     /db_xref="CDD:463965"
     CDS             1..497
                     /gene="Gdap2"
                     /coded_by="NM_001013201.1:214..1707"
                     /db_xref="GeneID:362004"
                     /db_xref="RGD:1306050"
ORIGIN      
        1 mdplgapsqf vdvdtlvswg dsyedevnss dstaeafqed snrspflynr dingkvvlwk
       61 gdvallncta ivntsneslt dknpvsesif mlagpdlked lqklkgcrtg eakltkgfnl
      121 aarfiihtvg pkyksryrta aesslyscyr nvlqlakeqs mssvgfcvin sakrgypled
      181 athialrtvr rfleihgeti ekvvfaisel eeatyqkllp lyfprslkee sqslpslpad
      241 ignaegepvv perqirisek pgasedheed edeglgvdls figshafarm egdidkqrkl
      301 ilqgqlseaa lqkqhqrnyn rwlcqarsed lsdiaslkal yqtgvdncgr tvmvvvgrni
      361 pvtlidmdka llyfihvmdh iavkeyvlvy fhtltseynh ldsdflkkly dvvdikykrn
      421 lkavyfvhpt frskvstwff ttfsvsglkd kihhvdslqq lfsaispeqi dfppfvleyd
      481 arengpyfas yppspdl
//
LOCUS       NP_036687                441 aa            linear   ROD 28-APR-2025
DEFINITION  protein C-ets-1 [Rattus norvegicus].
ACCESSION   NP_036687
VERSION     NP_036687.1
DBSOURCE    REFSEQ: accession NM_012555.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Gu,M., Li,X., Wu,R., Cheng,X., Zhou,S. and Gu,X.
  TITLE     The Transcription Factor Ets1 Influences Axonal Growth via
            Regulation of Lcn2
  JOURNAL   Mol Neurobiol 61 (2), 971-981 (2024)
   PUBMED   37672148
  REMARK    GeneRIF: The Transcription Factor Ets1 Influences Axonal Growth via
            Regulation of Lcn2.
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Guo,X., Zhang,B.F., Zhang,J., Liu,G., Hu,Q. and Chen,J.
  TITLE     The histone demthylase KDM3A protects the myocardium from
            ischemia/reperfusion injury via promotion of ETS1 expression
  JOURNAL   Commun Biol 5 (1), 270 (2022)
   PUBMED   35338235
  REMARK    GeneRIF: The histone demthylase KDM3A protects the myocardium from
            ischemia/reperfusion injury via promotion of ETS1 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Feng,W., Guan,Z., Xing,D., Li,X., Ying,W.Z., Remedies,C.E.,
            Inscho,E.W. and Sanders,P.W.
  TITLE     Avian erythroblastosis virus E26 oncogene homolog-1 (ETS-1) plays a
            role in renal microvascular pathophysiology in the Dahl
            salt-sensitive rat
  JOURNAL   Kidney Int 97 (3), 528-537 (2020)
   PUBMED   31932071
  REMARK    GeneRIF: Avian erythroblastosis virus E26 oncogene homolog-1
            (ETS-1) plays a role in renal microvascular pathophysiology in the
            Dahl salt-sensitive rat.
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Surles-Zeigler,M.C., Li,Y., Distel,T.J., Omotayo,H., Ge,S. and
            Ford,B.D.
  TITLE     Transcriptomic analysis of neuregulin-1 regulated genes following
            ischemic stroke by computational identification of promoter binding
            sites: A role for the ETS-1 transcription factor
  JOURNAL   PLoS One 13 (6), e0197092 (2018)
   PUBMED   29856744
  REMARK    GeneRIF: Transcriptomic analysis of neuregulin-1 regulated genes
            following ischemic stroke by computational identification of
            promoter binding sites: A role for the ETS-1 transcription factor.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Feng,W., Chen,B., Xing,D., Li,X., Fatima,H., Jaimes,E.A. and
            Sanders,P.W.
  TITLE     Haploinsufficiency of the Transcription Factor Ets-1 Is
            Renoprotective in Dahl Salt-Sensitive Rats
  JOURNAL   J Am Soc Nephrol 28 (11), 3239-3250 (2017)
   PUBMED   28696249
  REMARK    GeneRIF: Reduced renal expression of ETS-1 prevented
            hypertension-associated kidney injury in SS rats
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Suzuki,H., Romano-Spica,V., Papas,T.S. and Bhat,N.K.
  TITLE     ETS1 suppresses tumorigenicity of human colon cancer cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (10), 4442-4446 (1995)
   PUBMED   7753825
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hagman,J. and Grosschedl,R.
  TITLE     An inhibitory carboxyl-terminal domain in Ets-1 and Ets-2 mediates
            differential binding of ETS family factors to promoter sequences of
            the mb-1 gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 8889-8893 (1992)
   PUBMED   1409581
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Kakaar,D.N., Samuel,S.A., Sharma,S. and Chopra,S.
  TITLE     Nurses' use of fertility regulating methods--a study
  JOURNAL   Nurs J India 83 (5), 111-113 (1992)
   PUBMED   1298911
REFERENCE   9  (residues 1 to 441)
  AUTHORS   Aparicio,J.M.
  TITLE     HLA and non-HLA genetic factors in Japanese IDDM
  JOURNAL   Hokkaido Igaku Zasshi 66 (6), 780-793 (1991)
   PUBMED   1686010
REFERENCE   10 (residues 1 to 441)
  AUTHORS   Aparicio,J.M., Wakisaka,A., Takada,A., Matsuura,N. and Yoshiki,T.
  TITLE     Non-HLA genetic factors and insulin dependent diabetes mellitus in
            the Japanese: TCRA, TCRB and TCRG, INS, THY1, CD3D and ETS1
  JOURNAL   Dis Markers 8 (5), 283-294 (1990)
   PUBMED   1982251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC101927.1, L20681.1 and JAXUCZ010000008.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.28749.1,
                                           SRR26360172.208863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q21"
     Protein         1..441
                     /product="protein C-ets-1"
                     /note="p54; Ets avian erythroblastosis virus E2 oncogene
                     homolog 1 (tumor progression locus 1); v-ets
                     erythroblastosis virus E26 oncogene homolog 1; v-ets avian
                     erythroblastosis virus E26 oncogene homolog 1"
                     /calculated_mol_wt=50292
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000250|UniProtKB:P27577; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Region          51..138
                     /region_name="SAM_PNT-ETS-1"
                     /note="Sterile alpha motif (SAM)/Pointed domain of ETS-1;
                     cd08542"
                     /db_xref="CDD:176092"
     Site            order(114,116,120)
                     /site_type="other"
                     /note="ERK2 MAP kinase docking site [polypeptide binding]"
                     /db_xref="CDD:176092"
     Region          130..243
                     /region_name="Activation domain, required for
                     transcription activation.
                     /evidence=ECO:0000250|UniProtKB:P14921"
                     /note="propagated from UniProtKB/Swiss-Prot (P41156.1)"
     Region          147..334
                     /region_name="Ets1_N_flank"
                     /note="Ets1 N-terminal flanking region of Ets domain;
                     pfam19525"
                     /db_xref="CDD:466113"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27577; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Region          304..312
                     /region_name="Helix HI-1.
                     /evidence=ECO:0000250|UniProtKB:P27577"
                     /note="propagated from UniProtKB/Swiss-Prot (P41156.1)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P14921; propagated from
                     UniProtKB/Swiss-Prot (P41156.1)"
     Region          323..330
                     /region_name="Helix HI-2.
                     /evidence=ECO:0000250|UniProtKB:P27577"
                     /note="propagated from UniProtKB/Swiss-Prot (P41156.1)"
     Region          334..418
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     Region          418..422
                     /region_name="Helix H4.
                     /evidence=ECO:0000250|UniProtKB:P27577"
                     /note="propagated from UniProtKB/Swiss-Prot (P41156.1)"
     Region          426..432
                     /region_name="Helix H5.
                     /evidence=ECO:0000250|UniProtKB:P27577"
                     /note="propagated from UniProtKB/Swiss-Prot (P41156.1)"
     CDS             1..441
                     /gene="Ets1"
                     /gene_synonym="Ets-1; Etsoncb; Tpl1"
                     /coded_by="NM_012555.2:280..1605"
                     /db_xref="GeneID:24356"
                     /db_xref="RGD:2583"
ORIGIN      
        1 mkaavdlkpt ltiiktekvd lelfpspdme cadvplltps skemmsqalk atfsgftkeq
       61 qrlgipkdpr qwtethvrdw vmwavnefsl kgvdfqkfcm ngaalcalgk ecflelapdf
      121 vgdilwehle ilqkedvkpy qvngvnptyp esrytsdyfi sygiehaqcv ppsefsepsf
      181 itesyqtlhp isseellslk yendypsvil rdplqtdtlq tdyfaikqev ltpdnmcmgr
      241 asrgklggqd sfesiesyds cdrltqswss qssfnslqrv psydsfdsed ypaalpnhkp
      301 kgtfkdyvrd radlnkdkpv ipaaalagyt gsgpiqlwqf llelltdksc qsfiswtgdg
      361 wefklsdpde varrwgkrkn kpkmnyekls rglryyydkn iihktagkry vyrfvcdlqs
      421 llgytpeelh amldvkpdad e
//
LOCUS       NP_001099569             331 aa            linear   ROD 28-APR-2025
DEFINITION  cathepsin 7 precursor [Rattus norvegicus].
ACCESSION   NP_001099569 XP_001065193 XP_225126
VERSION     NP_001099569.1
DBSOURCE    REFSEQ: accession NM_001106099.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474032.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_225126.1, XP_001065193.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p14"
     Protein         1..331
                     /product="cathepsin 7 precursor"
                     /calculated_mol_wt=36110
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1776
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Region          33..50
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q91ZF2"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZ07.1)"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (D3ZZ07.1)"
     mat_peptide     112..331
                     /product="Cathepsin 7.
                     /evidence=ECO:0000250|UniProtKB:O60911.
                     /id=PRO_0000415398"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZZ07.1)"
                     /calculated_mol_wt=24775
     Region          113..329
                     /region_name="Peptidase_C1A"
                     /note="Peptidase C1A subfamily (MEROPS database
                     nomenclature); composed of cysteine peptidases (CPs)
                     similar to papain, including the mammalian CPs (cathepsins
                     B, C, F, H, L, K, O, S, V, X and W). Papain is an
                     endopeptidase with specific substrate preferences;
                     cd02248"
                     /db_xref="CDD:239068"
     Site            order(130,136,274,298)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            order(180..181,246,272,275,325)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     CDS             1..331
                     /gene="Cts7"
                     /coded_by="NM_001106099.1:244..1239"
                     /db_xref="GeneID:290970"
                     /db_xref="RGD:1309226"
ORIGIN      
        1 mtvavflail clraalaapr pdysldaewe ewkrnnakty speeekqrra vweenvkmik
       61 whtmqnglwm nnftiemnef gdmtgeemrm mtdssaltlr ngkhiqkrnv kipktldwrd
      121 tgcvapvrsq ggcgacwafs vaasiesqlf kktgklipls vqnlidctvt ygnndcsggk
      181 pytafqyvkn nggleaeaty pyeaklrhcr yrpersvvki arffvvprne ealmqalvty
      241 gpiavaidgs hasfkryrgg iyhepkcrrd tldhglllvg ygyeghesen rkywllknsh
      301 geqwgergym klprdqnnyc giasyamypl l
//
LOCUS       NP_001020213             217 aa            linear   ROD 28-APR-2025
DEFINITION  fin bud initiation factor homolog precursor [Rattus norvegicus].
ACCESSION   NP_001020213 XP_575197
VERSION     NP_001020213.1
DBSOURCE    REFSEQ: accession NM_001025042.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Lakner,J., Seyer,C., Hermsdorf,T. and Schoneberg,T.
  TITLE     Characterization of the expression, promoter activity and molecular
            architecture of fibin
  JOURNAL   BMC Biochem 12, 26 (2011)
   PUBMED   21615908
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK364593.1 and BC085873.1.
            
            On Jun 25, 2005 this sequence version replaced XP_575197.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q34"
     Protein         1..217
                     /product="fin bud initiation factor homolog precursor"
                     /calculated_mol_wt=22550
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2222
     Region          16..209
                     /region_name="Fibin"
                     /note="Fin bud initiation factor homolog; pfam15819"
                     /db_xref="CDD:406297"
     mat_peptide     19..217
                     /product="Fin bud initiation factor homolog.
                     /id=PRO_0000349213"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2T4.1)"
                     /calculated_mol_wt=22550
     Site            30
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5U2T4.1)"
     CDS             1..217
                     /gene="Fibin"
                     /coded_by="NM_001025042.2:355..1008"
                     /db_xref="GeneID:499856"
                     /db_xref="RGD:1563711"
ORIGIN      
        1 mmftkliwmg ffchlcrgyf dgplypemsn gtlhhyfvpd gdyeenddpe kcqllfrvsd
       61 rrrcsqgegg qassllsltl reeftvlgrq vedagrvleg isksisydld geesygkylr
      121 reshqigday snsdksltel eskfkqgqeq dsrqesrlne dflgmlvhtr sllketlgis
      181 vglrdkyell ahtirshgtr lgrlksdyle gggqkmg
//
LOCUS       NP_001017464             506 aa            linear   ROD 28-APR-2025
DEFINITION  BTB/POZ domain-containing protein 16 [Rattus norvegicus].
ACCESSION   NP_001017464 XP_341942
VERSION     NP_001017464.1
DBSOURCE    REFSEQ: accession NM_001017464.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079317.1.
            
            On Apr 29, 2005 this sequence version replaced XP_341942.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37-q41"
     Protein         1..506
                     /product="BTB/POZ domain-containing protein 16"
                     /note="BTB (POZ) domain containing 16"
                     /calculated_mol_wt=58328
     Region          74..214
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          206..302
                     /region_name="BACK_BTBD16"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     BTB/POZ domain-containing protein 16 (BTBD16); cd18492"
                     /db_xref="CDD:350567"
     CDS             1..506
                     /gene="Btbd16"
                     /gene_synonym="RGD1311454"
                     /coded_by="NM_001017464.2:243..1763"
                     /db_xref="GeneID:361658"
                     /db_xref="RGD:1311454"
ORIGIN      
        1 mkmlnsrkir merrivgatn rwrfpqdhfc gdllalsqmc nvlnvdldda lknpdklcis
       61 kfqklftesi mdsgtqsgea dvildclgfk welhhpqifq setlaklylt aliqntkssq
      121 rdlekilkvh stermkkrsp vkkiiislri ndpavtrvaf alalknlymn evemtvdnvl
      181 gvlasahilq fnrlfrkcvs tmlnrltpct iknfylagck ykeeqltnac ekwlamnlvp
      241 lvgtqihlrh ipepllykvl ksprlftfse fhllktllmw vylqmngkvq tlpihetmla
      301 ffssfpkksc fleqdpghsw mplflclrlh gitsgkdlee ikhinffpes wlvrvtanhy
      361 halesggnmv hlkdlstqam rfgllfrqey ttysetisiy gyffeikgik hdttsysfsm
      421 qrirhtdlec pssvcehsti slrserlvky eiraqtlvdg rwqefgtnqi mqkfgfikpg
      481 ckshalkiqt vgipiyasfa fifpas
//
LOCUS       NP_001012092             580 aa            linear   ROD 28-APR-2025
DEFINITION  XK-related protein 7 [Rattus norvegicus].
ACCESSION   NP_001012092 XP_230742
VERSION     NP_001012092.1
DBSOURCE    REFSEQ: accession NM_001012092.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY534261.1.
            
            On Feb 11, 2005 this sequence version replaced XP_230742.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY534261.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..580
                     /product="XK-related protein 7"
                     /note="X Kell blood group precursor related family member
                     7 homolog; XK, Kell blood group complex subunit-related
                     family, member 7; X-linked Kx blood group related 7"
                     /calculated_mol_wt=64207
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Region          59..441
                     /region_name="XK-related"
                     /note="XK-related protein; pfam09815"
                     /db_xref="CDD:462912"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            326..346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     Region          <439..>535
                     /region_name="PHA02682"
                     /note="ORF080 virion core protein; Provisional"
                     /db_xref="CDD:177464"
     Region          470..516
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH56.1)"
     CDS             1..580
                     /gene="Xkr7"
                     /coded_by="NM_001012092.1:164..1906"
                     /db_xref="GeneID:311549"
                     /db_xref="RGD:1359224"
ORIGIN      
        1 maaksdgaaa vagpgpegpa gadrggaggr gevaagiagp gpveagcpgp ryelrdccwv
       61 lcallvffsd gatdlwlaas yylqgqstyf gltllfvllp slvvqllsfr wfvydysept
      121 gtpgpavstk dsdivgaais tkdsavafrt kegspelvpr papssagayr rrccrlcvwl
      181 lqtlvhllql gqvwrylral ylglqsrwrg erlrrhfywr mlfesadvsm lrlletflrs
      241 apqlvlqlsl lvhrgrepel ltalsisasl vslawtlasy qkvlrdsrdd krplsykgav
      301 vqvlwhlfti aartlafalf asvyrlyfgi fivahwcimt fwviqgetdf cmskweeiiy
      361 nmvvgiiyif cwfnvkegrs rrrvtlyyci vllenaaltg fwyssrnfst dfyslilvcv
      421 vassfalgif fmcvyycllh pngpmlgpqa pgcifpeapg pcgppadait spprslprtt
      481 gaerdgaavg geragtptpp vfqvrpglpp tpvarplrte gpviridlpr kkypawdahf
      541 idrrlrktil aleysspatp rlqyrsmgts qelleyettv
//
LOCUS       NP_001012177             563 aa            linear   ROD 28-APR-2025
DEFINITION  methylcrotonoyl-CoA carboxylase beta chain, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001012177 XP_342182
VERSION     NP_001012177.1
DBSOURCE    REFSEQ: accession NM_001012177.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Chu,C.H. and Cheng,D.
  TITLE     Expression, purification, characterization of human
            3-methylcrotonyl-CoA carboxylase (MCCC)
  JOURNAL   Protein Expr Purif 53 (2), 421-427 (2007)
   PUBMED   17360195
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Stadler,S.C., Polanetz,R., Meier,S., Mayerhofer,P.U.,
            Herrmann,J.M., Anslinger,K., Roscher,A.A., Roschinger,W. and
            Holzinger,A.
  TITLE     Mitochondrial targeting signals and mature peptides of
            3-methylcrotonyl-CoA carboxylase
  JOURNAL   Biochem Biophys Res Commun 334 (3), 939-946 (2005)
   PUBMED   16023992
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Gallardo,M.E., Desviat,L.R., Rodriguez,J.M., Esparza-Gordillo,J.,
            Perez-Cerda,C., Perez,B., Rodriguez-Pombo,P., Criado,O., Sanz,R.,
            Morton,D.H., Gibson,K.M., Le,T.P., Ribes,A., de Cordoba,S.R.,
            Ugarte,M. and Penalva,M.A.
  TITLE     The molecular basis of 3-methylcrotonylglycinuria, a disorder of
            leucine catabolism
  JOURNAL   Am J Hum Genet 68 (2), 334-346 (2001)
   PUBMED   11170888
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Oei,J. and Robinson,B.H.
  TITLE     Simultaneous preparation of the three biotin-containing
            mitochondrial carboxylases from rat liver
  JOURNAL   Biochim Biophys Acta 840 (1), 1-5 (1985)
   PUBMED   3995077
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083581.1.
            
            On Feb 11, 2005 this sequence version replaced XP_342182.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083581.1, SRR8487231.54669.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..563
                     /product="methylcrotonoyl-CoA carboxylase beta chain,
                     mitochondrial"
                     /EC_number="6.4.1.4"
                     /note="MCCase subunit beta; 3-methylcrotonyl-CoA
                     carboxylase 2; 3-methylcrotonyl-CoA:carbon dioxide ligase
                     subunit beta; 3-methylcrotonyl-CoA carboxylase
                     non-biotin-containing subunit; methylcrotonoyl-Coenzyme A
                     carboxylase 2 (beta); methylcrotonoyl-CoA carboxylase 2
                     (beta)"
                     /calculated_mol_wt=59038
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q5XIT9.1)"
                     /calculated_mol_wt=2498
     mat_peptide     23..563
                     /product="Methylcrotonoyl-CoA carboxylase beta chain,
                     mitochondrial. /id=PRO_0000284069"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIT9.1)"
                     /calculated_mol_wt=59038
     Region          36..563
                     /region_name="Carboxyl_trans"
                     /note="Carboxyl transferase domain; cl47203"
                     /db_xref="CDD:481543"
     Region          49..555
                     /region_name="Carboxyltransferase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01138"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIT9.1)"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3ULD5; propagated from
                     UniProtKB/Swiss-Prot (Q5XIT9.1)"
     Region          343..372
                     /region_name="Acyl-CoA binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XIT9.1)"
     Site            495
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q3ULD5; propagated from
                     UniProtKB/Swiss-Prot (Q5XIT9.1)"
     Site            511
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3ULD5; propagated from
                     UniProtKB/Swiss-Prot (Q5XIT9.1)"
     CDS             1..563
                     /gene="Mccc2"
                     /coded_by="NM_001012177.1:139..1830"
                     /db_xref="GeneID:361884"
                     /db_xref="RGD:1310279"
ORIGIN      
        1 mwgalrsvlr pcsrasvprq rayhgdavar lgtqpdsgss tyqenyeqmk alvnqlhera
       61 qyvrlggsek ararhtsrgk llprdridnl idpgspflef sqfagyklyg eeevpaggii
      121 tgigrvsgve cmivandatv kggtyypvtv kkhvraqeia lqnrlpciyl vdsgganlpr
      181 qadtfpdrdh fgrifynqai mssknitqia vvmgsctagg ayvpamaden iivqrqgtif
      241 lagpplvkaa tgeevsaedl ggadlhcrrs gvtdhyaldd hhalhltrkv vrslnyqkkl
      301 dvtvepseep lfpadelygi vganlkrsfd vreviarivd gsrfnefkal ygdtlvtgfa
      361 rifgypvgii gnngvlfses akkgahfvql ccqrnipllf lqnitgfmvg kdyeaegiak
      421 dgakmvaavs cakvpkitvi iggsygagny gmcgrayspr flymwpnari svmggeqaat
      481 vlatvardqr aregkqfssa eeaalkepii krfeeegnpy yssarlwddg iidpvdtrlv
      541 lglsisaaln apiqrtdfgi frm
//
LOCUS       NP_653357                316 aa            linear   ROD 28-APR-2025
DEFINITION  protein lifeguard 2 [Rattus norvegicus].
ACCESSION   NP_653357
VERSION     NP_653357.1
DBSOURCE    REFSEQ: accession NM_144756.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Shen,W., Liu,J., Fan,M., Wang,S., Zhang,Y., Wen,L., Wang,R.,
            Wei,W., Li,N., Zhang,Y. and Zhao,G.
  TITLE     MiR-3202 protects smokers from chronic obstructive pulmonary
            disease through inhibiting FAIM2: An in vivo and in vitro study
  JOURNAL   Exp Cell Res 362 (2), 370-377 (2018)
   PUBMED   29208459
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Urresti,J., Ruiz-Meana,M., Coccia,E., Arevalo,J.C., Castellano,J.,
            Fernandez-Sanz,C., Galenkamp,K.M., Planells-Ferrer,L.,
            Moubarak,R.S., Llecha-Cano,N., Reix,S., Garcia-Dorado,D.,
            Barneda-Zahonero,B. and Comella,J.X.
  TITLE     Lifeguard Inhibits Fas Ligand-mediated Endoplasmic
            Reticulum-Calcium Release Mandatory for Apoptosis in Type II
            Apoptotic Cells
  JOURNAL   J Biol Chem 291 (3), 1221-1234 (2016)
   PUBMED   26582200
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Merianda,T.T., Vuppalanchi,D., Yoo,S., Blesch,A. and Twiss,J.L.
  TITLE     Axonal transport of neural membrane protein 35 mRNA increases axon
            growth
  JOURNAL   J Cell Sci 126 (Pt 1), 90-102 (2013)
   PUBMED   23097042
  REMARK    GeneRIF: Data show that NMP35 supports axonal growth, and
            overexpression of an axonally targeted NMP35 mRNA is sufficient to
            increase axonal outgrowth.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Boender,A.J., van Rozen,A.J. and Adan,R.A.
  TITLE     Nutritional state affects the expression of the obesity-associated
            genes Etv5, Faim2, Fto, and Negr1
  JOURNAL   Obesity (Silver Spring) 20 (12), 2420-2425 (2012)
   PUBMED   22627920
  REMARK    GeneRIF: expression of Etv5, Faim2, Fto, Negr1 but not Sh2b1 is
            affected by nutritional state in these two areas, and the
            relationship between nutritional state and expression levels of
            obesity-associated genes in two brain areas relevant to feeding.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Hurtado de Mendoza,T., Perez-Garcia,C.G., Kroll,T.T., Hoong,N.H.,
            O'Leary,D.D. and Verma,I.M.
  TITLE     Antiapoptotic protein Lifeguard is required for survival and
            maintenance of Purkinje and granular cells
  JOURNAL   Proc Natl Acad Sci U S A 108 (41), 17189-17194 (2011)
   PUBMED   21957071
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2014 Aug 12;111(32):11906]
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Reich,A., Spering,C., Gertz,K., Harms,C., Gerhardt,E.,
            Kronenberg,G., Nave,K.A., Schwab,M., Tauber,S.C., Drinkut,A.,
            Harms,K., Beier,C.P., Voigt,A., Gobbels,S., Endres,M. and
            Schulz,J.B.
  TITLE     Fas/CD95 regulatory protein Faim2 is neuroprotective after
            transient brain ischemia
  JOURNAL   J Neurosci 31 (1), 225-233 (2011)
   PUBMED   21209208
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Fernandez,M., Segura,M.F., Sole,C., Colino,A., Comella,J.X. and
            Cena,V.
  TITLE     Lifeguard/neuronal membrane protein 35 regulates Fas
            ligand-mediated apoptosis in neurons via microdomain recruitment
  JOURNAL   J Neurochem 103 (1), 190-203 (2007)
   PUBMED   17635665
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Beier,C.P., Wischhusen,J., Gleichmann,M., Gerhardt,E.,
            Pekanovic,A., Krueger,A., Taylor,V., Suter,U., Krammer,P.H.,
            Endres,M., Weller,M. and Schulz,J.B.
  TITLE     FasL (CD95L/APO-1L) resistance of neurons mediated by
            phosphatidylinositol 3-kinase-Akt/protein kinase B-dependent
            expression of lifeguard/neuronal membrane protein 35
  JOURNAL   J Neurosci 25 (29), 6765-6774 (2005)
   PUBMED   16033886
  REMARK    GeneRIF: LFG mediated the FasL resistance of cerebellar granular
            cells to apoptosis
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Schweitzer,B., Suter,U. and Taylor,V.
  TITLE     Neural membrane protein 35/Lifeguard is localized at postsynaptic
            sites and in dendrites
  JOURNAL   Brain Res Mol Brain Res 107 (1), 47-56 (2002)
   PUBMED   12414123
  REMARK    GeneRIF: NMP35 protein occurs throughout the brain and spinal cord,
            especially in dendrites of several neuronal cell types and in the
            surrounding neuropil. NMP35 co-localizes with the glutamate
            receptor GluR2 and the presynaptic vesicle protein synaptophysin.
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Schweitzer,B., Taylor,V., Welcher,A.A., McClelland,M. and Suter,U.
  TITLE     Neural membrane protein 35 (NMP35): a novel member of a gene family
            which is highly expressed in the adult nervous system
  JOURNAL   Mol Cell Neurosci 11 (5-6), 260-273 (1998)
   PUBMED   9698393
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087606.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087606.1, AF044201.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132292,
                                           SAMD00132295 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..316
                     /product="protein lifeguard 2"
                     /note="lifeguard; neural membrane protein 35; protein
                     lifeguard 2-like"
                     /calculated_mol_wt=34905
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Region          92..312
                     /region_name="LFG_like"
                     /note="Proteins similar to and including lifeguard (LFG),
                     a putative regulator of apoptosis; cd10428"
                     /db_xref="CDD:198410"
     Site            106..126
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O88407.1)"
     Site            194..214
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O88407.1)"
     CDS             1..316
                     /gene="Faim2"
                     /gene_synonym="Lfg; NMP35"
                     /coded_by="NM_144756.2:75..1025"
                     /db_xref="GeneID:246274"
                     /db_xref="RGD:628744"
ORIGIN      
        1 mtqgklsvan kapgtegqqq angekkdapa vpsappsyee atsgeglkag afpqgptavp
       61 lhpswayvdp ssssgyeggf paghhelfst fswddqkvrq lfirkvytil lvqllvtlav
      121 valftfcdvv kdyvqanpgw ywasyavffa tyltlaccsg prrhfpwnli lltiftlsma
      181 yltgmlssyy nttsvllclg italvclsvt ifsfqtkfdf tschgvlfvl lmtlffsgll
      241 laillpfqyv pwlhavyavl gagvftlfla fdtqllmgnr rhslspeeyi fgalniyldi
      301 iyiftfflql fgtnre
//
LOCUS       NP_001163818            2343 aa            linear   ROD 28-APR-2025
DEFINITION  pecanex-like protein 1 [Rattus norvegicus].
ACCESSION   NP_001163818 XP_234385
VERSION     NP_001163818.1
DBSOURCE    REFSEQ: accession NM_001170347.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2343)
  AUTHORS   Geisinger,A., Alsheimer,M., Baier,A., Benavente,R. and Wettstein,R.
  TITLE     The mammalian gene pecanex 1 is differentially expressed during
            spermatogenesis
  JOURNAL   Biochim Biophys Acta 1728 (1-2), 34-43 (2005)
   PUBMED   15777640
  REMARK    GeneRIF: pecanex 1 could play an important role in the testis,
            related to spermatogenesis.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000006.1.
            
            On Dec 17, 2009 this sequence version replaced XP_234385.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2343
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..2343
                     /product="pecanex-like protein 1"
                     /note="pecanex homolog protein 1; pecanex homolog 1"
                     /calculated_mol_wt=257813
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Region          98..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Region          271..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Region          306..691
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Region          323..>615
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          749..826
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            978..998
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1009..1029
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1034..1054
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1068..1088
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1118..1138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1162..1182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1195..1215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1268..1288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1296..1316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1406..1426
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1434..1454
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1458..1478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Site            1493..1513
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     Region          1784..2010
                     /region_name="Pecanex_C"
                     /note="Pecanex protein (C-terminus); pfam05041"
                     /db_xref="CDD:461533"
     Region          2050..2120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PSU6.1)"
     CDS             1..2343
                     /gene="Pcnx1"
                     /gene_synonym="Pcnx"
                     /coded_by="NM_001170347.1:9..7040"
                     /db_xref="GeneID:314288"
                     /db_xref="RGD:1306115"
ORIGIN      
        1 mgsqtlqilr qgvwaalsgg wyydphqatf vnalhlylwl fllglpftly malpssmiiv
       61 avycpvvaav fivlkmvnyr lhraldagev vdrsaneftd qrakaeqgnc strrkdsngp
      121 sdpgggiems efireatppv gcssrnsyag ldpsnqigsg ssrlgtaati kgdtdtakts
      181 ddislslgqs sslckegsee qdlatdrklf rlvsndsfvs iqpslsscgq dlprdfsdkv
      241 slpshsqhhr vdqslcsacd tevaslvplh shsyrkehrp rgvprtsssa vafpdaslsg
      301 lplyqqqqrr gldpvtelds skphsgtres lvgqscplaq sqpaadrrks ysqpptkcgk
      361 sralnaeksv dslrslstrs sgstesycsg tdrdtnstls sykseqtsst hiesilsehd
      421 espkvgdksa rkegcaesae erchgatdrr tssdktaleg stpagppeap daqaseekpd
      481 qvapsssase danknphane ftvpgdrppe qsaeskeeqg ekpslstdsk vckddggkqk
      541 egdvrpksss lihrttsahk pgrrrtgkkr assfdssrhr dyvsfrgvsg tkphsaifch
      601 dedssdqsdl srapsvhsah hfssdssssa tshscqspeg kysalktkhg hkdrgtdsdh
      661 thrahpgpeg takkrasrrt ssthsaktra rvlsldsgtv aclndsnrll apdsikpltt
      721 sksdleakeg evldelsllg rasqletvtr srnslpsqva fpegeeqdaa tgaaqaseea
      781 vafrrerstf rrqavrrrhn agsnptpptl ligpplslqd gqqgqqstaq vkvqsrppsq
      841 aavlsasasl lvrkgsvhld ashdhasavg gsslhdelgk fsstlyetgg cdmslvnfep
      901 aarrasnicd tdshvsssts vrfyphdmls lpqirlnrll tidtdlleqq didlspdlaa
      961 tygpteeaaq kvkhyyrfwi lpqlwiginf drltllalfd rnreilenil avvlailvaf
     1021 lgsilliqgf frdiwvfqfc lviascqysl lksvqpdsss prhghnriia ysrpvyfclc
     1081 cgliwlldyg srnlstskfk lygitftnpl vllsardlvi vftlcfpivf figllpqvnt
     1141 fvmylceqld ihifggnatt sllaalysfl csvvavally glcygalrds wdgqhipvlf
     1201 svfcgllvav syhlsrqssd psvlfsliqs kifpktdekn pedplsevkd plpeklsnsv
     1261 serlqsdlvv cvvigvlyfa ihvstvftal qpalkyvlya lvgfvglvth yvlpqvrkql
     1321 pwhcfsrpll ktaehnqyev rnaatmmwfe klhvwllfve knviyplivl nelsssadti
     1381 aspkkldtel galmitvagl kllrssfssp tyqyitvift vlffkfdyea fsetmlldlf
     1441 fmsilfsklw ellyklqfvy tyvapwqitw gsafhafaqp favphsamlf vqavvsalfs
     1501 tplnpflgsa ifitsyvrpv kfwerdyntk rvdhsntrla sqldrnpgsd dnnlnsifye
     1561 hltrslqhsl cgdlllgrwg nystgdcfil asdylnalvh lietgnglvt fqlrglefrg
     1621 tycqqrevea itegveedeg fcccepghvp hvlsfnaafg qrwlawevvv tkyilegysi
     1681 tdnsaasmlq vfdlrrvltt yyvkgiiyyv ttsskleewl anetmqeglr lcadrnyvdv
     1741 dptfnpnide dydhrlagis resfcviyln wieycssrra kpldvdkdss lvtlcyglcv
     1801 lgrralgtas hhmssnlesf lyglhalfkg dfrissvrde wifadmellr kvvvpgirms
     1861 iklhqdhfts pdeyddptvl yeaivshekn lviahegdpa wrsavlansp sllalrhvmd
     1921 dgtneykiim lnrrylsfrv ikvnkecvrg lwagqqqelv flrnrnperg siqnakqalr
     1981 nminsscdqp igypifvspl ttsysdshdq lkeilggpis lgnirdfivs twhrlrkgcg
     2041 agcnsggnie dsdtgggtsc pansattasd phnsvpqgst ghpgqgagsg lhppttsypp
     2101 tlgtshsahs vqsslvrqsp arasmasqss ycygsrhssl rmsttgfvpc rrsstsqisl
     2161 rnlpssiqsr lsmvnqmeaa sqggmgcvqh glpssssssq sipackhhtl vaflgaegsq
     2221 sgateaqpgn tsspatisha rkgevvyrvq ivdlsqileg invskrkelq wpdegirlka
     2281 grnswkdwsp qegmeghvvh rwvpcsrdps trshidktvl lvqiddkyvt vietgvlelg
     2341 aev
//
LOCUS       NP_001102919             523 aa            linear   ROD 28-APR-2025
DEFINITION  glycerate kinase [Rattus norvegicus].
ACCESSION   NP_001102919 XP_001070289 XP_001070333 XP_001070374 XP_001070415
VERSION     NP_001102919.1
DBSOURCE    REFSEQ: accession NM_001109449.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Guo,J.H., Hexige,S., Chen,L., Zhou,G.J., Wang,X., Jiang,J.M.,
            Kong,Y.H., Ji,G.Q., Wu,C.Q., Zhao,S.Y. and Yu,L.
  TITLE     Isolation and characterization of the human D-glyceric acidemia
            related glycerate kinase gene GLYCTK1 and its alternatively
            splicing variant GLYCTK2
  JOURNAL   DNA Seq 17 (1), 1-7 (2006)
   PUBMED   16753811
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Katayama,H., Kitagawa,Y. and Sugimoto,E.
  TITLE     Purification of rat liver glycerate kinase and studies of its
            enzymatic and immunological properties
  JOURNAL   J Biochem 88 (3), 765-773 (1980)
   PUBMED   6252205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105621.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001070289.1, XP_001070333.1, XP_001070374.1, XP_001070415.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105621.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..523
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /calculated_mol_wt=55057
     Region          33..515
                     /region_name="GckA"
                     /note="Glycerate-2-kinase [Carbohydrate transport and
                     metabolism]; COG2379"
                     /db_xref="CDD:441946"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q0VGK3.1)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8QZY2; propagated from
                     UniProtKB/Swiss-Prot (Q0VGK3.1)"
     CDS             1..523
                     /gene="Glyctk"
                     /coded_by="NM_001109449.2:86..1657"
                     /db_xref="GeneID:684314"
                     /db_xref="RGD:1591498"
ORIGIN      
        1 maaalqvlpc llrapsrpfl wgppvarmts gmalaeqarq lfdsavgavq pgpmlqrtls
       61 ldpsgkqlkv rdrtfqlqen lylvgfgkav lgmaaaadel lgqhlvqgvi svpkgiraav
      121 elagkqemll kphshiqvfe gaednlpdrd alraaqaiqq laerltaddl llvlisgggs
      181 allpapippv tleekqtltk llaargatiq elntirkals qlkggglaqa aypaqvvsli
      241 lsdvigdple viasgptvas thsvqdclhi lnhyglraal prsvktvlsr adsdphgpht
      301 cghvlnviig snslalaeaq rqaevlgyha mvlstamqgd vrrvaqfygl larvaaaclt
      361 sstaerplee eaklhqlaae lqlpdlqlee aleavakakg pvcllaggep tvqlqgsgkg
      421 grnqelalrv gaelgkqplg pvdvlflsgg tdgqdgptkv agawvmsdlv sqasaenldf
      481 atfldnndsy tffcsfqggt hllhtgltgt nvmdvhllvf hpq
//
LOCUS       NP_037215                654 aa            linear   ROD 28-APR-2025
DEFINITION  endoplasmic reticulum chaperone BiP precursor [Rattus norvegicus].
ACCESSION   NP_037215
VERSION     NP_037215.1
DBSOURCE    REFSEQ: accession NM_013083.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Mou,L., Sun,D., Qu,J., Tan,X., Wang,S., Zeng,Q. and Liu,C.
  TITLE     GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline
  JOURNAL   J Hazard Mater 476, 135101 (2024)
   PUBMED   39002476
  REMARK    GeneRIF: GRP78/IRE1 and cGAS/STING pathway crosstalk through CHOP
            facilitates iodoacetic acid-mediated testosterone decline.
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Yan,Z., Liu,Y., Yang,B., Zhao,W., Wang,Y., Wang,D., Li,J., Jiao,X.
            and Cao,J.
  TITLE     Endoplasmic reticulum stress caused by traumatic injury promotes
            cardiomyocyte apoptosis through acetylation modification of GRP78
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (1), 96-105 (2024)
   PUBMED   38105649
  REMARK    GeneRIF: Endoplasmic reticulum stress caused by traumatic injury
            promotes cardiomyocyte apoptosis through acetylation modification
            of GRP78.
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Han,J., Jia,D., Yao,H., Xu,C., Huan,Z., Jin,H. and Ge,X.
  TITLE     GRP78 improves the therapeutic effect of mesenchymal stem cells on
            hemorrhagic shock-induced liver injury: Involvement of the NF-small
            ka, CyrillicB and HO-1/Nrf-2 pathways
  JOURNAL   FASEB J 38 (1), e23334 (2024)
   PUBMED   38050647
  REMARK    GeneRIF: GRP78 improves the therapeutic effect of mesenchymal stem
            cells on hemorrhagic shock-induced liver injury: Involvement of the
            NF-small ka, CyrillicB and HO-1/Nrf-2 pathways.
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Ishteyaque,S., Yadav,K.S., Verma,S., Washimkar,K.R. and Mugale,M.N.
  TITLE     CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit apoptosis
            and promotes progression of hepatocellular carcinoma
  JOURNAL   Arch Biochem Biophys 745, 109701 (2023)
   PUBMED   37499993
  REMARK    GeneRIF: CYP2E1 triggered GRP78/ATF6/CHOP signaling axis inhibit
            apoptosis and promotes progression of hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Wang,S., Duan,J., Liao,J., Wang,Y., Xiao,X., Li,L., Liu,Y., Gu,H.,
            Yang,P., Fu,D., Du,J., Li,X. and Shao,M.
  TITLE     LncRNA H19 inhibits ER stress induced apoptosis and improves
            diabetic cardiomyopathy by regulating PI3K/AKT/mTOR axis
  JOURNAL   Aging (Albany NY) 14 (16), 6809-6828 (2022)
   PUBMED   36044268
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Kuznetsov,G., Chen,L.B. and Nigam,S.K.
  TITLE     Several endoplasmic reticulum stress proteins, including ERp72,
            interact with thyroglobulin during its maturation
  JOURNAL   J Biol Chem 269 (37), 22990-22995 (1994)
   PUBMED   7916014
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Viville,S., Neefjes,J., Lotteau,V., Dierich,A., Lemeur,M.,
            Ploegh,H., Benoist,C. and Mathis,D.
  TITLE     Mice lacking the MHC class II-associated invariant chain
  JOURNAL   Cell 72 (4), 635-648 (1993)
   PUBMED   7679955
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Pedersen,R.C. and Brownie,A.C.
  TITLE     Steroidogenesis-activator polypeptide isolated from a rat Leydig
            cell tumor
  JOURNAL   Science 236 (4798), 188-190 (1987)
   PUBMED   3563495
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Chang,S.C., Wooden,S.K., Nakaki,T., Kim,Y.K., Lin,A.Y., Kung,L.,
            Attenello,J.W. and Lee,A.S.
  TITLE     Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its
            regulatory sequences and the effect of protein glycosylation on its
            expression
  JOURNAL   Proc Natl Acad Sci U S A 84 (3), 680-684 (1987)
   PUBMED   3468506
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Munro,S. and Pelham,H.R.
  TITLE     An Hsp70-like protein in the ER: identity with the 78 kd
            glucose-regulated protein and immunoglobulin heavy chain binding
            protein
  JOURNAL   Cell 46 (2), 291-300 (1986)
   PUBMED   3087629
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB578015.1, BC062017.1, M14050.1 and CB327067.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062017.1, CF111168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p11"
     Protein         1..654
                     /product="endoplasmic reticulum chaperone BiP precursor"
                     /EC_number="3.6.4.10"
                     /note="78 kDa glucose-regulated protein; heat shock 70 kDa
                     protein 5; steroidogenesis-activator polypeptide;
                     immunoglobulin heavy chain-binding protein; GRP-78; heat
                     shock 70kDa protein 5 (glucose-regulated protein); heat
                     shock 70kD protein 5; heat shock protein 5; HSP70 family
                     protein 5; binding-immunoglobulin protein; heat shock
                     protein 70 family protein 5; endoplasmic reticulum
                     chaperone BiP; heat shock protein family A member 5"
                     /calculated_mol_wt=70475
     Region          1..80
                     /region_name="Required for interaction with ELAPOR1.
                     /evidence=ECO:0000250|UniProtKB:P11021"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1890
     mat_peptide     19..654
                     /product="endoplasmic reticulum chaperone BiP"
                     /calculated_mol_wt=70475
     Region          30..635
                     /region_name="HSP70"
                     /note="Hsp70 protein; pfam00012"
                     /db_xref="CDD:394970"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Region          125..280
                     /region_name="Nucleotide-binding (NBD).
                     /evidence=ECO:0000250|UniProtKB:P11021"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20029; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            213
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20029; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            271
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P0DMV8; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20029; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P20029; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Region          409..419
                     /region_name="Interdomain linker.
                     /evidence=ECO:0000250|UniProtKB:G3I8R9"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     Region          420..500
                     /region_name="Substrate-binding (SBD).
                     /evidence=ECO:0000250|UniProtKB:P11021"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     Site            492
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P0DMV8; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11021; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            585
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, in vitro.
                     /evidence=ECO:0000250|UniProtKB:P0DMV8;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11021; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:P11021;
                     propagated from UniProtKB/Swiss-Prot (P06761.1)"
     Site            591
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P11021; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Region          631..654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P20029; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06761.1)"
     Region          651..654
                     /region_name="Prevents secretion from ER"
                     /note="propagated from UniProtKB/Swiss-Prot (P06761.1)"
     CDS             1..654
                     /gene="Hspa5"
                     /gene_synonym="BIP; GRP 78; GRP78"
                     /coded_by="NM_013083.2:182..2146"
                     /db_xref="GeneID:25617"
                     /db_xref="RGD:2843"
ORIGIN      
        1 mkftvvaaal lllcavraee edkkedvgtv vgidlgttys cvgvfkngrv eiiandqgnr
       61 itpsyvaftp egerligdaa knqltsnpen tvfdakrlig rtwndpsvqq dikflpfkvv
      121 ekktkpyiqv digggqtktf apeeisamvl tkmketaeay lgkkvthavv tvpayfndaq
      181 rqatkdagti aglnvmriin eptaaaiayg ldkregekni lvfdlgggtf dvslltidng
      241 vfevvatngd thlggedfdq rvmehfikly kkktgkdvrk dnravqklrr evekakrals
      301 sqhqarieie sffegedfse tltrakfeel nmdlfrstmk pvqkvledsd lkksdideiv
      361 lvggstripk iqqlvkeffn gkepsrginp deavaygaav qagvlsgdqd tgdlvlldvc
      421 pltlgietvg gvmtkliprn tvvptkksqi fstasdnqpt vtikvyeger pltkdnhllg
      481 tfdltgippa prgvpqievt feidvngilr vtaedkgtgn knkititndq nrltpeeier
      541 mvndaekfae edkklkerid trnelesyay slknqigdke klggklsped ketmekavee
      601 kiewleshqd adiedfkakk keleeivqpi isklygsggp pptgeedtse kdel
//
LOCUS       NP_001020901             569 aa            linear   ROD 28-APR-2025
DEFINITION  F-box/WD repeat-containing protein 5 [Rattus norvegicus].
ACCESSION   NP_001020901 XP_342383
VERSION     NP_001020901.1
DBSOURCE    REFSEQ: accession NM_001025730.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Hui,X., Hu,F., Liu,J., Li,C., Yang,Y., Shu,S., Liu,P., Wang,F. and
            Li,S.
  TITLE     FBXW5 acts as a negative regulator of pathological cardiac
            hypertrophy by decreasing the TAK1 signaling to pro-hypertrophic
            members of the MAPK signaling pathway
  JOURNAL   J Mol Cell Cardiol 151, 31-43 (2021)
   PUBMED   32971071
  REMARK    GeneRIF: FBXW5 acts as a negative regulator of pathological cardiac
            hypertrophy by decreasing the TAK1 signaling to pro-hypertrophic
            members of the MAPK signaling pathway.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Zhao,P., Chao,W. and Li,W.
  TITLE     FBXW5 reduction alleviates spinal cord injury (SCI) by blocking
            microglia activity: A mechanism involving p38 and JNK
  JOURNAL   Biochem Biophys Res Commun 514 (2), 558-564 (2019)
   PUBMED   31060780
  REMARK    GeneRIF: FBXW5 reduction alleviates spinal cord injury by blocking
            microglia activity and down-regulating p38 and JNK.
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Ha,J.Y., Kim,J.S., Kang,Y.H., Bok,E., Kim,Y.S. and Son,J.H.
  TITLE     Tnfaip8 l1/Oxi-beta binds to FBXW5, increasing autophagy through
            activation of TSC2 in a Parkinson's disease model
  JOURNAL   J Neurochem 129 (3), 527-538 (2014)
   PUBMED   24444419
  REMARK    GeneRIF: oxidative stress induces Tnfaip8 l1/Oxi-beta, which
            results in increased autophagy by its exclusive binding with FBXW5
            to stabilize TSC2
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Werner,A., Disanza,A., Reifenberger,N., Habeck,G., Becker,J.,
            Calabrese,M., Urlaub,H., Lorenz,H., Schulman,B., Scita,G. and
            Melchior,F.
  TITLE     SCFFbxw5 mediates transient degradation of actin remodeller Eps8 to
            allow proper mitotic progression
  JOURNAL   Nat Cell Biol 15 (2), 179-188 (2013)
   PUBMED   23314863
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Puklowski,A., Homsi,Y., Keller,D., May,M., Chauhan,S., Kossatz,U.,
            Grunwald,V., Kubicka,S., Pich,A., Manns,M.P., Hoffmann,I.,
            Gonczy,P. and Malek,N.P.
  TITLE     The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets
            HsSAS-6 to control centrosome duplication
  JOURNAL   Nat Cell Biol 13 (8), 1004-1009 (2011)
   PUBMED   21725316
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Hu,J., Zacharek,S., He,Y.J., Lee,H., Shumway,S., Duronio,R.J. and
            Xiong,Y.
  TITLE     WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2
            by DDB1-CUL4-ROC1 ligase
  JOURNAL   Genes Dev 22 (7), 866-871 (2008)
   PUBMED   18381890
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC099179.1.
            
            On Jul 22, 2005 this sequence version replaced XP_342383.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099179.1, SRR8487227.58696.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..569
                     /product="F-box/WD repeat-containing protein 5"
                     /note="F-box and WD-40 domain-containing protein 5; F-box
                     and WD-40 domain protein 5"
                     /calculated_mol_wt=63903
     Region          7..51
                     /region_name="F-box_FBXW5"
                     /note="F-box domain found in F-box/WD repeat-containing
                     protein 5 (FBXW5) and similar proteins; cd22132"
                     /db_xref="CDD:438904"
     Site            order(9,13,16..17,20..21,25,27..28,32..34,36)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438904"
     Region          <75..191
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          85..120
                     /region_name="WD40"
                     /note="WD40 repeats; smart00320"
                     /db_xref="CDD:197651"
     Region          90..129
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI9.1)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK4.
                     /evidence=ECO:0000250|UniProtKB:Q969U6; propagated from
                     UniProtKB/Swiss-Prot (Q4KLI9.1)"
     Region          308..316
                     /region_name="D-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI9.1)"
     Region          <450..542
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          470..509
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI9.1)"
     Region          475..501
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          511..551
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KLI9.1)"
     Region          516..541
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..569
                     /gene="Fbxw5"
                     /coded_by="NM_001025730.2:129..1838"
                     /db_xref="GeneID:362081"
                     /db_xref="RGD:1305661"
ORIGIN      
        1 mdeggmpllp dslvyqifls lgpadvlaag lvcrqwqavs rdeflwreqf yryyqvardv
       61 prhpaatswy eefrrlydmv pcvevqtlke htdqvlhlsf shsgyqfasc skdctvkiwn
      121 ndltisllhs admrpynwsy tqfsqfnqdd slllasgvfl gphnsssgei avisldsfal
      181 lsrvrnkpyd vfgcwltets lisgnlhrig dvtscsvlwl nnafqdvese nvnvvkrlfk
      241 iqnlnastir tvmvadcsrf dspdllldag dqaglpcrvf dlggdteeea tdpglhtsgs
      301 ghvkeglrrv fdsvldghgq lsdcaletkv aellaqghtk ppecpdadsr nkylifttgc
      361 ltysphqigi kqilphqmtt agpvlgegrg sdaffdaldh vidvhghiig mglspdnryl
      421 yvnsrawppg svvadpmqpp piaeeidllv fdlktmrevk ralrahrayt pndecffifl
      481 dvsrdfvasg aedrhgyiwd rhyniclakl rhedvvnsva fspqeqelll tasddatika
      541 wrsprivrvl qaphprprpf fswfashrr
//
LOCUS       NP_068616                245 aa            linear   ROD 28-APR-2025
DEFINITION  kit ligand isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_068616
VERSION     NP_068616.1
DBSOURCE    REFSEQ: accession NM_021844.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Zheng,H., Liu,Y.J., Chen,Z.C. and Fan,G.Q.
  TITLE     miR-222 regulates cell growth, apoptosis, and autophagy of
            interstitial cells of Cajal isolated from slow transit constipation
            rats by targeting c-kit
  JOURNAL   Indian J Gastroenterol 40 (2), 198-208 (2021)
   PUBMED   33792838
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Sudo,H.
  TITLE     Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation
            under a Tau Deficiency in Mammary Epithelial Cells
  JOURNAL   Int J Mol Sci 19 (9), 2488 (2018)
   PUBMED   30142893
  REMARK    GeneRIF: The data suggest that microtubule acetylation upregulates
            KL1 and induces more aneuploidy if tau is deficient.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Zhang,W., Wu,T., Zhang,C., Luo,L., Xie,M. and Huang,H.
  TITLE     Cadmium exposure in newborn rats ovary induces developmental
            disorders of primordial follicles and the differential expression
            of SCF/c-kit gene
  JOURNAL   Toxicol Lett 280, 20-28 (2017)
   PUBMED   28801138
  REMARK    GeneRIF: It was concluded that the exposure of cadimium on newborn
            rats ovaries could inhibit follicle development. SCF/c-kit system
            might mediate follicle development damage caused by cadmium, which
            is associated with DNA hypomethylation of SCF/c-kit promoter region
            may be worthy of further study.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Qin,Q., Liu,J., Ma,Y., Wang,Y., Zhang,F., Gao,S. and Dong,L.
  TITLE     Aberrant expressions of stem cell factor/c-KIT in rat testis with
            varicocele
  JOURNAL   J Formos Med Assoc 116 (7), 542-548 (2017)
   PUBMED   27707610
  REMARK    GeneRIF: the SCF/c-KIT system is aberrantly expressed in
            varicocele(VC) testis, which could be involved in male infertility
            caused by VC.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Lee,J.H., Lee,M., Ahn,C., Kang,H.Y., Tran,D.N. and Jeung,E.B.
  TITLE     Parabens Accelerate Ovarian Dysfunction in a 4-Vinylcyclohexene
            Diepoxide-Induced Ovarian Failure Model
  JOURNAL   Int J Environ Res Public Health 14 (2), 161 (2017)
   PUBMED   28208728
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Ploemacher,R.E., van Soest,P.L., Boudewijn,A. and Neben,S.
  TITLE     Interleukin-12 enhances interleukin-3 dependent multilineage
            hematopoietic colony formation stimulated by interleukin-11 or
            steel factor
  JOURNAL   Leukemia 7 (9), 1374-1380 (1993)
   PUBMED   7690439
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Tsuji,K., Lyman,S.D., Sudo,T., Clark,S.C. and Ogawa,M.
  TITLE     Enhancement of murine hematopoiesis by synergistic interactions
            between steel factor (ligand for c-kit), interleukin-11, and other
            early acting factors in culture
  JOURNAL   Blood 79 (11), 2855-2860 (1992)
   PUBMED   1375116
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Lu,H.S., Clogston,C.L., Wypych,J., Fausset,P.R., Lauren,S.,
            Mendiaz,E.A., Zsebo,K.M. and Langley,K.E.
  TITLE     Amino acid sequence and post-translational modification of stem
            cell factor isolated from buffalo rat liver cell-conditioned medium
  JOURNAL   J Biol Chem 266 (13), 8102-8107 (1991)
   PUBMED   1708771
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Martin,F.H., Suggs,S.V., Langley,K.E., Lu,H.S., Ting,J.,
            Okino,K.H., Morris,C.F., McNiece,I.K., Jacobsen,F.W., Mendiaz,E.A.
            et al.
  TITLE     Primary structure and functional expression of rat and human stem
            cell factor DNAs
  JOURNAL   Cell 63 (1), 203-211 (1990)
   PUBMED   2208279
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Zsebo,K.M., Wypych,J., McNiece,I.K., Lu,H.S., Smith,K.A.,
            Karkare,S.B., Sachdev,R.K., Yuschenkoff,V.N., Birkett,N.C.,
            Williams,L.R. et al.
  TITLE     Identification, purification, and biological characterization of
            hematopoietic stem cell factor from buffalo rat liver--conditioned
            medium
  JOURNAL   Cell 63 (1), 195-201 (1990)
   PUBMED   2208278
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment in the 3' coding region, compared to variant 1. The
            resulting protein (isoform 2) is shorter when it is compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB105879.1, SRR26643429.26573.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..245
                     /product="kit ligand isoform 2 precursor"
                     /EC_number="3.2.1.31"
                     /note="mast cell growth factor; C-kit ligand;
                     hematopoietic growth factor KL; stem cell factor KL-1;
                     steel factor/kit ligand"
                     /calculated_mol_wt=24689
     Region          1..245
                     /region_name="SCF"
                     /note="Stem cell factor; pfam02404"
                     /db_xref="CDD:396808"
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3010
     CDS             1..245
                     /gene="Kitlg"
                     /gene_synonym="Kitl; Mgf; SCF"
                     /coded_by="NM_021844.2:175..912"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:60427"
                     /db_xref="RGD:3086"
ORIGIN      
        1 mkktqtwiit ciylqlllfn plvktqeicr npvtdnvkdi tklvanlpnd ymitlnyvag
       61 mdvlpshcwl rdmvthlsvs lttlldkfsn iseglsnysi idklgkivdd lvacmeenap
      121 knvkeslkkp etrnftpeef fsifnrsida fkdfmvasdt sdcvlsstlg pekgkaaksp
      181 edpglqwtam alpalislvi gfafgalywk kkqssltrav eniqineedn eismlqqker
      241 efqev
//
LOCUS       NP_001025081             868 aa            linear   ROD 28-APR-2025
DEFINITION  programmed cell death 6-interacting protein [Rattus norvegicus].
ACCESSION   NP_001025081 XP_576494
VERSION     NP_001025081.2
DBSOURCE    REFSEQ: accession NM_001029910.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Salim,S., Nasir,J. and Chen,P.E.
  TITLE     Overexpression of the dopamine receptor-interacting protein
            Alix/AIP1 modulates NMDA receptor-triggered cell death
  JOURNAL   FEBS Lett 593 (12), 1381-1391 (2019)
   PUBMED   31077357
  REMARK    GeneRIF: demonstrate a previously unreported role for Alix as a
            potential modulator of NMDAR function
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Campos,Y., Qiu,X., Gomero,E., Wakefield,R., Horner,L.,
            Brutkowski,W., Han,Y.G., Solecki,D., Frase,S., Bongiovanni,A. and
            d'Azzo,A.
  TITLE     Alix-mediated assembly of the actomyosin-tight junction polarity
            complex preserves epithelial polarity and epithelial barrier
  JOURNAL   Nat Commun 7, 11876 (2016)
   PUBMED   27336173
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Chiasserini,D., van Weering,J.R., Piersma,S.R., Pham,T.V.,
            Malekzadeh,A., Teunissen,C.E., de Wit,H. and Jimenez,C.R.
  TITLE     Proteomic analysis of cerebrospinal fluid extracellular vesicles: a
            comprehensive dataset
  JOURNAL   J Proteomics 106, 191-204 (2014)
   PUBMED   24769233
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Colombo,M., Moita,C., van Niel,G., Kowal,J., Vigneron,J.,
            Benaroch,P., Manel,N., Moita,L.F., Thery,C. and Raposo,G.
  TITLE     Analysis of ESCRT functions in exosome biogenesis, composition and
            secretion highlights the heterogeneity of extracellular vesicles
  JOURNAL   J Cell Sci 126 (Pt 24), 5553-5565 (2013)
   PUBMED   24105262
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Sandrin,V. and Sundquist,W.I.
  TITLE     ESCRT requirements for EIAV budding
  JOURNAL   Retrovirology 10, 104 (2013)
   PUBMED   24107264
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 868)
  AUTHORS   von Schwedler,U.K., Stuchell,M., Muller,B., Ward,D.M., Chung,H.Y.,
            Morita,E., Wang,H.E., Davis,T., He,G.P., Cimbora,D.M., Scott,A.,
            Krausslich,H.G., Kaplan,J., Morham,S.G. and Sundquist,W.I.
  TITLE     The protein network of HIV budding
  JOURNAL   Cell 114 (6), 701-713 (2003)
   PUBMED   14505570
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Schmidt,M.H.H., Chen,B., Randazzo,L.M. and Bogler,O.
  TITLE     SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse
            cytoskeletal elements, including FAKs, and modulate cell adhesion
  JOURNAL   J Cell Sci 116 (Pt 14), 2845-2855 (2003)
   PUBMED   12771190
  REMARK    GeneRIF: adaptor protein SETA (CIN85) and its binding partner AIP1
            are involved with the cytoskeleton and in the regulation of cell
            adhesion
REFERENCE   8  (residues 1 to 868)
  AUTHORS   Chen,B., Borinstein,S.C., Gillis,J., Sykes,V.W. and Bogler,O.
  TITLE     The glioma-associated protein SETA interacts with AIP1/Alix and
            ALG-2 and modulates apoptosis in astrocytes
  JOURNAL   J Biol Chem 275 (25), 19275-19281 (2000)
   PUBMED   10858458
REFERENCE   9  (residues 1 to 868)
  AUTHORS   Missotten,M., Nichols,A., Rieger,K. and Sadoul,R.
  TITLE     Alix, a novel mouse protein undergoing calcium-dependent
            interaction with the apoptosis-linked-gene 2 (ALG-2) protein
  JOURNAL   Cell Death Differ 6 (2), 124-129 (1999)
   PUBMED   10200558
REFERENCE   10 (residues 1 to 868)
  AUTHORS   Vito,P., Pellegrini,L., Guiet,C. and D'Adamio,L.
  TITLE     Cloning of AIP1, a novel protein that associates with the
            apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction
  JOURNAL   J Biol Chem 274 (3), 1533-1540 (1999)
   PUBMED   9880530
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 29, 2008 this sequence version replaced NP_001025081.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.34892.1,
                                           SRR26643293.47923.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..868
                     /product="programmed cell death 6-interacting protein"
                     /note="ALG-2 interacting protein 1; ALG-2 interacting
                     protein X"
                     /calculated_mol_wt=95751
     Region          2..345
                     /region_name="BRO1_Alix"
                     /note="Protein-interacting, N-terminal, Bro1-like domain
                     of mammalian Alix and related domains; cd09240"
                     /db_xref="CDD:185763"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            order(131,134,147,150..151,199,202..203,212,215..216,335,
                     337,339,341)
                     /site_type="other"
                     /note="putative ESCRT-III binding site"
                     /db_xref="CDD:185763"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Region          360..698
                     /region_name="V_Alix"
                     /note="Middle V-domain of mammalian Alix and related
                     domains are dimerization and protein interaction modules;
                     cd09235"
                     /db_xref="CDD:185748"
     Region          418..868
                     /region_name="Interaction with SDCBP.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            order(440,498,502,505..506,669,672..673,676,679)
                     /site_type="other"
                     /note="YPXnL-motif binding site"
                     /db_xref="CDD:185748"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Region          503..868
                     /region_name="Self-association.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            638..644
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:185748"
     Region          714..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Region          717..720
                     /region_name="Interaction with TSG101.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Site            744
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4; propagated from
                     UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Region          797..806
                     /region_name="Interaction with CEP55.
                     /evidence=ECO:0000250|UniProtKB:Q8WUM4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     Region          <814..>868
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     Region          832..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QZA2.2)"
     CDS             1..868
                     /gene="Pdcd6ip"
                     /gene_synonym="AIP1; Alix; RGD1561176"
                     /coded_by="NM_001029910.3:133..2739"
                     /db_xref="GeneID:501083"
                     /db_xref="RGD:68357"
ORIGIN      
        1 masfiwvqlk ktsevdlakp lvkfiqqtyp sggeeqaqyc raaeelsklr rsalgrpldk
       61 hegaletllr yydqicsiep kfpfsenqic ltftwkdafd kgslfggsvk lalaslgyek
      121 scvlfncaal asqiaaeqnl dndeglktaa kqyqfasgaf lhikdtvlsa lsreptvdis
      181 pdtvgtlsli mlaqaqevff lkatrdkmkd aiiaklanqa adyfgdafkq cqykdalpke
      241 vfptlaakqc imqanaeyhq silakqqkkf geeiarlqha aeliknvasr ydeyvnvkdf
      301 sdkinralaa akkdndfiyh drvpdlkdld pigkatlvkp tpvnvpisqk ftdlfekmvp
      361 vsvqqslavf sqrkadlvnr siaqmreatt langvlasln lpaaiedvsg dtvpqsiltk
      421 stavveqggi qtvdqlikel pellqrnrei leeslrllde eeatdndlra kfkdrwqrtp
      481 sndlykplra egakfravld kavqadgqvk eryqshrdti allckpepel naaipsanpa
      541 ktmqgsevvn vlksllsnld eikkeregle ndlksvnfdm tskfltalaq dgvineeals
      601 vteldriygg lttkvqeslk kqegllkniq vshqefskmk qsnseaslre evlknlatay
      661 dnfvelvanl kegtkfynel teilvrfqnk csdivfarkt erdellkdlq qsiarepsap
      721 sipppayqss pagghatapt paprtmppak pqpparpppp vlpanrvppa aaatapagvg
      781 tasaappqtp gsapppqaqg ppyptypgyp gycqmpmpmg ynpytygqyn mpyppvyhqs
      841 pgqapypgpq qptypfpqpp qqsyypqq
//
LOCUS       NP_062247                248 aa            linear   ROD 28-APR-2025
DEFINITION  proenkephalin-B preproprotein [Rattus norvegicus].
ACCESSION   NP_062247
VERSION     NP_062247.2
DBSOURCE    REFSEQ: accession NM_019374.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Phillips,R.A., Wan,E., Tuscher,J.J., Reid,D., Drake,O.R., Ianov,L.
            and Day,J.J.
  TITLE     Temporally specific gene expression and chromatin remodeling
            programs regulate a conserved Pdyn enhancer
  JOURNAL   Elife 12, 89993 (2023)
   PUBMED   37938195
  REMARK    GeneRIF: Temporally specific gene expression and chromatin
            remodeling programs regulate a conserved Pdyn enhancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Ozkan-Kotiloglu,S., Kaya-Akyuzlu,D., Yurdakul,R., Yildirim,M.A. and
            Ozgur-Ilhan,I.
  TITLE     Effect of PDYN and OPRK1 polymorphisms on the risk of alcohol use
            disorder and the intensity of depressive symptoms
  JOURNAL   Alcohol Alcohol 58 (4), 404-414 (2023)
   PUBMED   37177778
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Wang,Y., Zhou,B., Fang,S., Zhu,S., Xu,T., Dilikumaer,M. and Li,G.
  TITLE     Dynorphin participates in interaction between depression and
            non-erosive reflux disease
  JOURNAL   Esophagus 20 (1), 158-169 (2023)
   PUBMED   36244036
  REMARK    GeneRIF: Dynorphin participates in interaction between depression
            and non-erosive reflux disease.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Legaki,E., Tsaklakidou,D., Hatzimanolis,A., Segredou,E.,
            Petalotis,M., Moularogiorgou,G., Mouchtouri,V., Lykouras,L.,
            Stefanis,N.C. and Gazouli,M.
  TITLE     Association of Alcohol Use Disorder Risk With ADH1B, DRD2, FAAH,
            SLC39A8, GCKR, and PDYN Genetic Polymorphisms
  JOURNAL   In Vivo 36 (5), 2092-2104 (2022)
   PUBMED   36099111
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Kaya-Akyuzlu,D., Ozkan-Kotiloglu,S., Yalcin-Sahiner,S.,
            Agtas-Ertan,E. and Ozgur-Ilhan,I.
  TITLE     Association of PDYN 68-bp VNTR polymorphism with sublingual
            buprenorphine/naloxone treatment and with opioid or alcohol use
            disorder: Effect on craving, depression, anxiety and age onset of
            first use
  JOURNAL   Eur J Pharmacol 921, 174862 (2022)
   PUBMED   35271823
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Spangler,R., Unterwald,E.M. and Kreek,M.J.
  TITLE     'Binge' cocaine administration induces a sustained increase of
            prodynorphin mRNA in rat caudate-putamen
  JOURNAL   Brain Res Mol Brain Res 19 (4), 323-327 (1993)
   PUBMED   7694032
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Przewlocka,B., Lason,W. and Przewlocki,R.
  TITLE     Repeated ethanol administration decreases prodynorphin biosynthesis
            in the rat hippocampus
  JOURNAL   Neurosci Lett 134 (2), 195-198 (1992)
   PUBMED   1589146
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Douglass,J., McMurray,C.T., Garrett,J.E., Adelman,J.P. and
            Calavetta,L.
  TITLE     Characterization of the rat prodynorphin gene
  JOURNAL   Mol Endocrinol 3 (12), 2070-2078 (1989)
   PUBMED   2628741
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Knepel,W., Schwaninger,M. and Dohler,K.D.
  TITLE     Corelease of dynorphin-like immunoreactivity, luteinizing hormone,
            and follicle-stimulating hormone from rat adenohypophysis in vitro
  JOURNAL   Endocrinology 117 (2), 481-487 (1985)
   PUBMED   2862008
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Civelli,O., Douglass,J., Goldstein,A. and Herbert,E.
  TITLE     Sequence and expression of the rat prodynorphin gene
  JOURNAL   Proc Natl Acad Sci U S A 82 (12), 4291-4295 (1985)
   PUBMED   3858883
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On Apr 25, 2008 this sequence version replaced NP_062247.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.18514.1,
                                           SRR26643291.10267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..248
                     /product="proenkephalin-B preproprotein"
                     /note="proenkephalin-B; preprodynorphin;
                     beta-neoendorphin-dynorphin"
                     /calculated_mol_wt=25879
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2276
     Region          22..66
                     /region_name="Opiods_neuropep"
                     /note="Vertebrate endogenous opioids neuropeptide;
                     pfam01160"
                     /db_xref="CDD:426090"
     Region          174..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06300.2)"
     CDS             1..248
                     /gene="Pdyn"
                     /coded_by="NM_019374.3:236..982"
                     /db_xref="GeneID:29190"
                     /db_xref="RGD:62054"
ORIGIN      
        1 mawsrlmlaa cllvipsevt adclslcslc avrtqdgphp inplicslec qdlvppseew
       61 etcrgfwsfl tltasglhgk ddlenevale egyteltkll epllkelekg qlltsvseek
      121 lrglssrfgn gresellgtd lmndeaaqag tlhfneedlr kqakryggfl rkypkrssem
      181 agdedrgqdg dqvghedlyk ryggflrrir pklkwdnqkr yggflrrqfk vvtrsqenpn
      241 tysedldv
//
LOCUS       NP_068543                400 aa            linear   ROD 28-APR-2025
DEFINITION  sphingosine 1-phosphate receptor 5 [Rattus norvegicus].
ACCESSION   NP_068543
VERSION     NP_068543.2
DBSOURCE    REFSEQ: accession NM_021775.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Kihara,Y., Maceyka,M., Spiegel,S. and Chun,J.
  TITLE     Lysophospholipid receptor nomenclature review: IUPHAR Review 8
  JOURNAL   Br J Pharmacol 171 (15), 3575-3594 (2014)
   PUBMED   24602016
  REMARK    Review article
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Khalid,A.M., Asano,A., Hosaka,Y.Z., Ohyama,K., Ohta,M. and
            Yamano,Y.
  TITLE     Expression of a novel sphingosine 1-phosphate receptor motif
            protein gene in maturing rat testes
  JOURNAL   Biosci Biotechnol Biochem 76 (9), 1769-1773 (2012)
   PUBMED   22972346
  REMARK    GeneRIF: The LOC290876-encoded gene product (EDG-8) has distinct
            roles in the nucleus during the processes of spermatocyte
            maturation and spermatid production in meiosis.
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Chiyo,M., Iwata,T., Webb,T.J., Vasko,M.R., Thompson,E.L.,
            Heidler,K.M., Cummings,O.W., Yoshida,S., Fujisawa,T., Brand,D.D.
            and Wilkes,D.S.
  TITLE     Silencing S1P1 receptors regulates collagen-V reactive
            lymphocyte-mediated immunobiology in the transplanted lung
  JOURNAL   Am J Transplant 8 (3), 537-546 (2008)
   PUBMED   18294150
  REMARK    GeneRIF: These data demonstrate novel roles of S1P(1R,) which
            include regulating emigration and modulating lymphocyte activation.
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Jolly,P.S., Bektas,M., Watterson,K.R., Sankala,H., Payne,S.G.,
            Milstien,S. and Spiegel,S.
  TITLE     Expression of SphK1 impairs degranulation and motility of RBL-2H3
            mast cells by desensitizing S1P receptors
  JOURNAL   Blood 105 (12), 4736-4742 (2005)
   PUBMED   15741218
  REMARK    GeneRIF: SphK1 has a role in regulating degranulation and motility
            of rat mast cells by desensitizing S1P receptors
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Jaillard,C., Harrison,S., Stankoff,B., Aigrot,M.S., Calver,A.R.,
            Duddy,G., Walsh,F.S., Pangalos,M.N., Arimura,N., Kaibuchi,K.,
            Zalc,B. and Lubetzki,C.
  TITLE     Edg8/S1P5: an oligodendroglial receptor with dual function on
            process retraction and cell survival
  JOURNAL   J Neurosci 25 (6), 1459-1469 (2005)
   PUBMED   15703400
  REMARK    GeneRIF: Edg8/S1P5 activation on oligodendroglial cells modulates
            two distinct functional pathways mediating either process
            retraction or cell survival and that these effects depend on the
            developmental stage of the cell.
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Niedernberg,A., Scherer,C.R., Busch,A.E. and Kostenis,E.
  TITLE     Comparative analysis of human and rat S1P(5) (edg8): differential
            expression profiles and sensitivities to antagonists
  JOURNAL   Biochem Pharmacol 64 (8), 1243-1250 (2002)
   PUBMED   12234605
  REMARK    GeneRIF: differences between hS1P(5) and rS1P(5) will be an
            important point to be considered in the development of selective
            receptor antagonists.
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Brinkmann,V., Davis,M.D., Heise,C.E., Albert,R., Cottens,S.,
            Hof,R., Bruns,C., Prieschl,E., Baumruker,T., Hiestand,P.,
            Foster,C.A., Zollinger,M. and Lynch,K.R.
  TITLE     The immune modulator FTY720 targets sphingosine 1-phosphate
            receptors
  JOURNAL   J Biol Chem 277 (24), 21453-21457 (2002)
   PUBMED   11967257
  REMARK    GeneRIF: The immune modulator FTY720 targets sphingosine
            1-phosphate receptors.
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Malek,R.L., Toman,R.E., Edsall,L.C., Wong,S., Chiu,J.,
            Letterle,C.A., Van Brocklyn,J.R., Milstien,S., Spiegel,S. and
            Lee,N.H.
  TITLE     Nrg-1 belongs to the endothelial differentiation gene family of G
            protein-coupled sphingosine-1-phosphate receptors
  JOURNAL   J Biol Chem 276 (8), 5692-5699 (2001)
   PUBMED   11069896
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Im,D.S., Heise,C.E., Ancellin,N., O'Dowd,B.F., Shei,G.J.,
            Heavens,R.P., Rigby,M.R., Hla,T., Mandala,S., McAllister,G.,
            George,S.R. and Lynch,K.R.
  TITLE     Characterization of a novel sphingosine 1-phosphate receptor, Edg-8
  JOURNAL   J Biol Chem 275 (19), 14281-14286 (2000)
   PUBMED   10799507
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Glickman,M., Malek,R.L., Kwitek-Black,A.E., Jacob,H.J. and Lee,N.H.
  TITLE     Molecular cloning, tissue-specific expression, and chromosomal
            localization of a novel nerve growth factor-regulated G-protein-
            coupled receptor, nrg-1
  JOURNAL   Mol Cell Neurosci 14 (2), 141-152 (1999)
   PUBMED   10532805
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF115249.1.
            
            On Jun 4, 2003 this sequence version replaced NP_068543.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF115249.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q13"
     Protein         1..400
                     /product="sphingosine 1-phosphate receptor 5"
                     /note="S1P5; NRG-1; S1P receptor 5; S1P receptor Edg-8;
                     sphingosine 1-phosphate receptor Edg-8; endothelial
                     differentiation G-protein-coupled receptor 8; nerve growth
                     factor-regulated G-protein-coupled receptor 1; endothelial
                     differentiation, sphingolipid G-protein-coupled receptor,
                     8"
                     /calculated_mol_wt=42238
     Site            20
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          37..318
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          39..63
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:410628"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          72..93
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:410628"
     Region          109..131
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:410628"
     Site            112..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          153..169
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          190..213
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          251..273
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          286..311
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Region          330..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JKM5.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JKM5.1)"
     CDS             1..400
                     /gene="S1pr5"
                     /gene_synonym="Edg-8; Edg8"
                     /coded_by="NM_021775.2:258..1460"
                     /db_xref="GeneID:60399"
                     /db_xref="RGD:620566"
ORIGIN      
        1 mesgllrpap vsevivlhyn ytgklrgary qpgaglrada avclavcafi vlenlavllv
       61 lgrhprfhap mflllgsltl sdllagaaya tnillsgplt lrlspalwfa reggvfvala
      121 asvlsllaia ierhltmarr gpapaasrar tlamavaawg llltlgllpa lgwnclgrle
      181 acstvlpvya kayvlfcvla flgilaaica lyariycqvr anarrlragp gsrratsssr
      241 srhtprslal lrtlsvvlla fvacwgplfl lllldvacpa racpvllqad pflglamans
      301 llnpiiytft nrdlrhallr llccgrgpcn qdssnslqrs psavgpsggg lrrclpptld
      361 rssspsehsc pqrdgmdtsc stgspgaata nrtlvpdatd
//
LOCUS       NP_001253984              85 aa            linear   ROD 28-APR-2025
DEFINITION  anaphase-promoting complex subunit CDC26 [Rattus norvegicus].
ACCESSION   NP_001253984
VERSION     NP_001253984.1
DBSOURCE    REFSEQ: accession NM_001267055.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Jin,L., Williamson,A., Banerjee,S., Philipp,I. and Rape,M.
  TITLE     Mechanism of ubiquitin-chain formation by the human
            anaphase-promoting complex
  JOURNAL   Cell 133 (4), 653-665 (2008)
   PUBMED   18485873
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Dube,P., Herzog,F., Gieffers,C., Sander,B., Riedel,D., Muller,S.A.,
            Engel,A., Peters,J.M. and Stark,H.
  TITLE     Localization of the coactivator Cdh1 and the cullin subunit Apc2 in
            a cryo-electron microscopy model of vertebrate APC/C
  JOURNAL   Mol Cell 20 (6), 867-879 (2005)
   PUBMED   16364912
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Gmachl,M., Gieffers,C., Podtelejnikov,A.V., Mann,M. and Peters,J.M.
  TITLE     The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are
            sufficient to ubiquitinate substrates of the anaphase-promoting
            complex
  JOURNAL   Proc Natl Acad Sci U S A 97 (16), 8973-8978 (2000)
   PUBMED   10922056
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM103539.1, DY317988.1 and BC086343.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213015.1, FQ217142.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q24"
     Protein         1..85
                     /product="anaphase-promoting complex subunit CDC26"
                     /calculated_mol_wt=9671
     Region          1..64
                     /region_name="ANAPC_CDC26"
                     /note="Anaphase-promoting complex APC subunit CDC26;
                     pfam10471"
                     /db_xref="CDD:402205"
     Region          26..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6YDN7.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6YDN7.1)"
     CDS             1..85
                     /gene="Cdc26"
                     /gene_synonym="BWK-2"
                     /coded_by="NM_001267055.1:159..416"
                     /db_xref="GeneID:366381"
                     /db_xref="RGD:1311342"
ORIGIN      
        1 mlrrkptrle lklddieefe nirkdleark kqkedvegvg tsdgegaagl ssdpksreqm
       61 indrigykpq lktnnrtsqf gnfef
//
LOCUS       NP_001102373             796 aa            linear   ROD 28-APR-2025
DEFINITION  histone-lysine N-methyltransferase PRDM9 [Rattus norvegicus].
ACCESSION   NP_001102373 XP_001056338 XP_344848
VERSION     NP_001102373.2
DBSOURCE    REFSEQ: accession NM_001108903.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Gasic,S., Mihola,O. and Trachtulec,Z.
  TITLE     Prdm9 deficiency of rat oocytes causes synapsis among
            non-homologous chromosomes and aneuploidy
  JOURNAL   Mamm Genome 33 (4), 590-605 (2022)
   PUBMED   35596034
  REMARK    GeneRIF: Prdm9 deficiency of rat oocytes causes synapsis among
            non-homologous chromosomes and aneuploidy.
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Diagouraga,B., Clement,J.A.J., Duret,L., Kadlec,J., de Massy,B. and
            Baudat,F.
  TITLE     PRDM9 Methyltransferase Activity Is Essential for Meiotic DNA
            Double-Strand Break Formation at Its Binding Sites
  JOURNAL   Mol Cell 69 (5), 853-865 (2018)
   PUBMED   29478809
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Altemose,N., Noor,N., Bitoun,E., Tumian,A., Imbeault,M.,
            Chapman,J.R., Aricescu,A.R. and Myers,S.R.
  TITLE     A map of human PRDM9 binding provides evidence for novel behaviors
            of PRDM9 and other zinc-finger proteins in meiosis
  JOURNAL   Elife 6, e28383 (2017)
   PUBMED   29072575
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Parvanov,E.D., Tian,H., Billings,T., Saxl,R.L., Spruce,C.,
            Aithal,R., Krejci,L., Paigen,K. and Petkov,P.M.
  TITLE     PRDM9 interactions with other proteins provide a link between
            recombination hotspots and the chromosomal axis in meiosis
  JOURNAL   Mol Biol Cell 28 (3), 488-499 (2017)
   PUBMED   27932493
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Li,X., Li,C., Li,X., Cui,P., Li,Q., Guo,Q., Han,H., Liu,S. and
            Sun,G.
  TITLE     Involvement of Histone Lysine Methylation in p21 Gene Expression in
            Rat Kidney In Vivo and Rat Mesangial Cells In Vitro under Diabetic
            Conditions
  JOURNAL   J Diabetes Res 2016, 3853242 (2016)
   PUBMED   27652271
  REMARK    GeneRIF: SET7/9 Recruitment to p21 Gene Promoter Was Increased
            under Diabetic Conditions
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Berg,I.L., Neumann,R., Sarbajna,S., Odenthal-Hesse,L., Butler,N.J.
            and Jeffreys,A.J.
  TITLE     Variants of the protein PRDM9 differentially regulate a set of
            human meiotic recombination hotspots highly active in African
            populations
  JOURNAL   Proc Natl Acad Sci U S A 108 (30), 12378-12383 (2011)
   PUBMED   21750151
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Baudat,F., Buard,J., Grey,C., Fledel-Alon,A., Ober,C.,
            Przeworski,M., Coop,G. and de Massy,B.
  TITLE     PRDM9 is a major determinant of meiotic recombination hotspots in
            humans and mice
  JOURNAL   Science 327 (5967), 836-840 (2010)
   PUBMED   20044539
  REMARK    Erratum:[Science. 2010 May 7;328(5979):690]
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Parvanov,E.D., Petkov,P.M. and Paigen,K.
  TITLE     Prdm9 controls activation of mammalian recombination hotspots
  JOURNAL   Science 327 (5967), 835 (2010)
   PUBMED   20044538
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Mihola,O., Trachtulec,Z., Vlcek,C., Schimenti,J.C. and Forejt,J.
  TITLE     A mouse speciation gene encodes a meiotic histone H3
            methyltransferase
  JOURNAL   Science 323 (5912), 373-375 (2009)
   PUBMED   19074312
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Hayashi,K., Yoshida,K. and Matsui,Y.
  TITLE     A histone H3 methyltransferase controls epigenetic events required
            for meiotic prophase
  JOURNAL   Nature 438 (7066), 374-378 (2005)
   PUBMED   16292313
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Dec 23, 2009 this sequence version replaced NP_001102373.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. The extent of this transcript is supported
            by orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643290.727.1,
                                           SRR26643293.1116.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q12"
     Protein         1..796
                     /product="histone-lysine N-methyltransferase PRDM9"
                     /EC_number="2.1.1.354"
                     /EC_number="2.1.1.355"
                     /EC_number="2.1.1.361"
                     /EC_number="2.1.1.362"
                     /EC_number="2.1.1.359"
                     /note="PR domain-containing protein 9; PR domain zinc
                     finger protein 9; PR domain containing 7; PR domain
                     containing 9; PR domain 9; protein-lysine
                     N-methyltransferase PRDM9; [histone H4]-lysine20
                     N-methyltransferase PRDM9; [histone H3]-lysine4
                     N-trimethyltransferase PRDM9; [histone H3]-lysine9
                     N-trimethyltransferase PRDM9; [histone H3]-lysine36
                     N-trimethyltransferase PRDM9; [histone
                     H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9"
                     /calculated_mol_wt=92448
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Region          32..89
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          149..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Region          175..205
                     /region_name="SSXRD"
                     /note="SSXRD motif; pfam09514"
                     /db_xref="CDD:430657"
     Region          244..372
                     /region_name="PR-SET_PRDM7_9"
                     /note="PR-SET domain found in PR domain zinc finger
                     protein 7 (PRDM7) and 9 (PRDM9) and similar proteins;
                     cd19193"
                     /db_xref="CDD:380970"
     Site            order(257,260..262,280,291..292,294..298,308,321..325,327,
                     336..337,361..362,364..365,368..369)
                     /site_type="active"
                     /db_xref="CDD:380970"
     Site            order(257,260..262,294..295,321..325,327,361,365,369)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380970"
     Site            372
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ9; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:Q96EQ9;
                     propagated from UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Site            376
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ9; propagated from
                     UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Site            378
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q96EQ9; propagated from
                     UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Region          402..748
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          443..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C6Y7.1)"
     Region          521..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(581,583,585,587..588,591..592,595,609,611,615..616,
                     619..620,623,637,639,641,643..644,647..648,651)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          604..624
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          632..652
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          660..680
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          688..708
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          716..736
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          744..764
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          756..780
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          772..792
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..796
                     /gene="Prdm9"
                     /gene_synonym="Prdm7"
                     /coded_by="NM_001108903.2:136..2526"
                     /db_xref="GeneID:365155"
                     /db_xref="RGD:1305247"
ORIGIN      
        1 msrtmntnkp eenstegdag klewkpkvkd efkdisiyfs keewaemgew ekiryrnvkr
       61 nykmlisigl raprpafmcy qrqaikpqin dnedsdeewt pkqqvsspwv pfrvkhskqq
      121 ketprmplsd kssvkevfgi enllntsgse haqkpvcspe egntsgqhfg kklklrrknv
      181 evnryrlrer kdlayeevse pqdddylyce kcqnffidsc pnhgppvfvk dsvvdrghpn
      241 hsvlslppgl rigpsgipea glgvwneasd lpvglhfgpy kgqitedeea ansgyswlit
      301 kgrncyeyvd gqdesqanwm ryvncardde eqnlvafqyh rkifyrtcrv irpgrellvw
      361 ygdeygqelg ikwgskmkkg ftagrelrte ihpcflcsla fssqkfltqh vewnhrteif
      421 pgasarinpk pgdpcpdqlq ehfdsqnknd kasnevkrks kprhkwtrqr istafsstlk
      481 eqmrseeskr tveeelrtgq ttniedtaks fiasetsrie rqcgqcfsdk snvsehqrth
      541 tgekpyicre cgrgfsqksd likhqrthte ekpyicrecg rgftqksdli khqrthteek
      601 pyicrecgrg ftqksdlikh qrthtgekpy icrecgrgft qksdlikhqr thteekpyic
      661 recgrgftqk sslirhqrth tgekpyicre cglgftqksn lirhlrthtg ekpyicrecg
      721 lgftrksnli qhqrthtgek pyicrecgqg ltwkssliqh qrthtgekpy icrecgrgft
      781 wkssliqhqr thtvek
//
LOCUS       NP_598230                578 aa            linear   ROD 28-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 15A [Rattus norvegicus].
ACCESSION   NP_598230
VERSION     NP_598230.2
DBSOURCE    REFSEQ: accession NM_133546.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Yang,T., He,R., Li,G., Liang,J., Zhao,L., Zhao,X., Li,L. and
            Wang,P.
  TITLE     Growth arrest and DNA damage-inducible protein 34 (GADD34)
            contributes to cerebral ischemic injury and can be detected in
            plasma exosomes
  JOURNAL   Neurosci Lett 758, 136004 (2021)
   PUBMED   34098025
  REMARK    GeneRIF: Growth arrest and DNA damage-inducible protein 34 (GADD34)
            contributes to cerebral ischemic injury and can be detected in
            plasma exosomes.
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Tan,Z., Zhang,W., Sun,J., Fu,Z., Ke,X., Zheng,C., Zhang,Y., Li,P.,
            Liu,Y., Hu,Q., Wang,H. and Zheng,Z.
  TITLE     ZIKV infection activates the IRE1-XBP1 and ATF6 pathways of
            unfolded protein response in neural cells
  JOURNAL   J Neuroinflammation 15 (1), 275 (2018)
   PUBMED   30241539
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Ren,F., Shi,H., Zhang,L., Zhang,X., Wen,T., Xie,B., Zheng,S.,
            Chen,Y., Li,L., Chen,D. and Duan,Z.
  TITLE     The dysregulation of endoplasmic reticulum stress response in
            acute-on-chronic liver failure patients caused by acute
            exacerbation of chronic hepatitis B
  JOURNAL   J Viral Hepat 23 (1), 23-31 (2016)
   PUBMED   26234401
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Mohammad-Gharibani,P., Modi,J., Menzie,J., Genova,R., Ma,Z.,
            Tao,R., Prentice,H. and Wu,J.Y.
  TITLE     Mode of action of S-methyl-N, N-diethylthiocarbamate sulfoxide
            (DETC-MeSO) as a novel therapy for stroke in a rat model
  JOURNAL   Mol Neurobiol 50 (2), 655-672 (2014)
   PUBMED   24573692
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Lin,M.H., Yen,J.H., Weng,C.Y., Wang,L., Ha,C.L. and Wu,M.J.
  TITLE     Lipid peroxidation end product 4-hydroxy-trans-2-nonenal triggers
            unfolded protein response and heme oxygenase-1 expression in PC12
            cells: Roles of ROS and MAPK pathways
  JOURNAL   Toxicology 315, 24-37 (2014)
   PUBMED   24291486
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Lee,Y.Y., Cevallos,R.C. and Jan,E.
  TITLE     An upstream open reading frame regulates translation of GADD34
            during cellular stresses that induce eIF2alpha phosphorylation
  JOURNAL   J Biol Chem 284 (11), 6661-6673 (2009)
   PUBMED   19131336
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Su,Z.Z., Goldstein,N.I., Jiang,H., Wang,M.N., Duigou,G.J.,
            Young,C.S. and Fisher,P.B.
  TITLE     PEG-3, a nontransforming cancer progression gene, is a positive
            regulator of cancer aggressiveness and angiogenesis
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15115-15120 (1999)
   PUBMED   10611347
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Doutheil,J., Althausen,S., Gissel,C. and Paschen,W.
  TITLE     Activation of MYD116 (gadd34) expression following transient
            forebrain ischemia of rat: implications for a role of disturbances
            of endoplasmic reticulum calcium homeostasis
  JOURNAL   Brain Res Mol Brain Res 63 (2), 225-232 (1999)
   PUBMED   9878749
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Amundson,S.A., Zhan,Q., Penn,L.Z. and Fornace,A.J. Jr.
  TITLE     Myc suppresses induction of the growth arrest genes gadd34, gadd45,
            and gadd153 by DNA-damaging agents
  JOURNAL   Oncogene 17 (17), 2149-2154 (1998)
   PUBMED   9811446
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Su,Z.Z., Shi,Y. and Fisher,P.B.
  TITLE     Subtraction hybridization identifies a transformation
            progression-associated gene PEG-3 with sequence homology to a
            growth arrest and DNA damage-inducible gene
  JOURNAL   Proc Natl Acad Sci U S A 94 (17), 9125-9130 (1997)
   PUBMED   9256446
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1997 Oct 28;94(22):12241]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1 and BC072513.1.
            
            On Nov 1, 2005 this sequence version replaced NP_598230.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072513.1, SRR22399484.1288634.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN12840115, SAMN16676789
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            regulatory uORF        :: PMID: 19131336
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..578
                     /product="protein phosphatase 1 regulatory subunit 15A"
                     /note="progression elevated gene 3 protein; growth arrest
                     and DNA damage-inducible protein GADD34; myeloid
                     differentiation primary response protein MyD116 homolog;
                     myeloid differentiation primary response gene 116; protein
                     phosphatase 1, regulatory (inhibitor) subunit 15A"
                     /calculated_mol_wt=63453
     Region          1..165
                     /region_name="Required for localization in the endoplasmic
                     reticulum. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          101..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          158..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75807; propagated from
                     UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          279..375
                     /region_name="3 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          319..417
                     /region_name="Interaction with SMAD7.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          330..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          363..462
                     /region_name="Interaction with KMT2A/MLL1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75807; propagated from
                     UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          368..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O75807; propagated from
                     UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          443..490
                     /region_name="Interaction with SMARCB1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     Region          <459..526
                     /region_name="PP1c_bdg"
                     /note="Phosphatase-1 catalytic subunit binding region;
                     pfam10488"
                     /db_xref="CDD:431311"
     Region          532..578
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IN02.2)"
     CDS             1..578
                     /gene="Ppp1r15a"
                     /gene_synonym="Gadd34; Myd116; Peg-3; RGD1624209"
                     /coded_by="NM_133546.3:226..1962"
                     /db_xref="GeneID:171071"
                     /db_xref="RGD:621526"
ORIGIN      
        1 mapsprpqhv lhwkeahsfy llsplmgfls rawsrlrgpe vseawlaetv aganqieada
       61 lltpppvsen hlplretegn gtpewskaaq rlcldveaqs sppktwglsd idehngkpgq
      121 dglreqeveh taglptlqpl hlqgadkkvg evvareegvs elayptshwe ggpaedeedt
      181 etvkkahqas aasiapgykp stsvycpgea ehrateekgt dnkaepsgsh srvweyhtre
      241 rpkqegetkp eqhragqshp cqnaeaeegg petsvcsgsa flkawvyrpg edteeeedsd
      301 ldsaeedtah tcttphtsaf lkawvyrpge dteeeddgdw dsaeedtaqs cttphtsafl
      361 kawvyrpged teeeddsenv apvdsetvds cqstqhclpv ektkgcgeae pppfqvafyl
      421 pgqkpappwa apklplrlqk rlrsfkapar nqdpeiplkg rkvhfsekvt vhflavwagp
      481 aqaarrgpwe qfardrsrfa rriaqaeeql gpyltpafra rawtrlrnlp lplsssslpl
      541 pepcssteat plsqdvttps plpseippps ldlggrrg
//
LOCUS       NP_001008888             274 aa            linear   ROD 28-APR-2025
DEFINITION  cytochrome b-c1 complex subunit Rieske, mitochondrial [Rattus
            norvegicus].
ACCESSION   NP_001008888 XP_214457
VERSION     NP_001008888.1
DBSOURCE    REFSEQ: accession NM_001008888.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Guo,R., Zong,S., Wu,M., Gu,J. and Yang,M.
  TITLE     Architecture of Human Mitochondrial Respiratory Megacomplex
            I2III2IV2
  JOURNAL   Cell 170 (6), 1247-1257 (2017)
   PUBMED   28844695
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Sanchez,E., Lobo,T., Fox,J.L., Zeviani,M., Winge,D.R. and
            Fernandez-Vizarra,E.
  TITLE     LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of
            mitochondrial Complex III assembly in human cells
  JOURNAL   Biochim Biophys Acta 1827 (3), 285-293 (2013)
   PUBMED   23168492
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Munusamy,S., Saba,H., Mitchell,T., Megyesi,J.K., Brock,R.W. and
            Macmillan-Crow,L.A.
  TITLE     Alteration of renal respiratory Complex-III during experimental
            type-1 diabetes
  JOURNAL   BMC Endocr Disord 9, 2 (2009)
   PUBMED   19166612
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Werner,H.B., Kuhlmann,K., Shen,S., Uecker,M., Schardt,A.,
            Dimova,K., Orfaniotou,F., Dhaunchak,A., Brinkmann,B.G., Mobius,W.,
            Guarente,L., Casaccia-Bonnefil,P., Jahn,O. and Nave,K.A.
  TITLE     Proteolipid protein is required for transport of sirtuin 2 into CNS
            myelin
  JOURNAL   J Neurosci 27 (29), 7717-7730 (2007)
   PUBMED   17634366
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Sun,G., Kinter,M.T. and Anderson,V.E.
  TITLE     Mass spectrometric characterization of mitochondrial electron
            transport complexes: subunits of the rat heart ubiquinol-cytochrome
            c reductase
  JOURNAL   J Mass Spectrom 38 (5), 531-539 (2003)
   PUBMED   12794875
  REMARK    GeneRIF: Mass spectrometric characterization of
            ubiquinol-cytochrome c reductase; ten of the 11 polypeptides
            present in this complex were detected directly by MALDI-TOFMS
            following electroelution of the active complex
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Jeyaseelan,R., Poizat,C., Wu,H.Y. and Kedes,L.
  TITLE     Molecular mechanisms of doxorubicin-induced cardiomyopathy.
            Selective suppression of Reiske iron-sulfur protein, ADP/ATP
            translocase, and phosphofructokinase genes is associated with ATP
            depletion in rat cardiomyocytes
  JOURNAL   J Biol Chem 272 (9), 5828-5832 (1997)
   PUBMED   9038198
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Joste,V., Goitom,Z. and Nelson,B.D.
  TITLE     Thyroid hormone regulation of nuclear-encoded mitochondrial inner
            membrane polypeptides of the liver
  JOURNAL   Eur J Biochem 184 (1), 255-260 (1989)
   PUBMED   2776768
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Nishikimi,M., Hosokawa,Y., Toda,H., Suzuki,H. and Ozawa,T.
  TITLE     Cloning and sequence analysis of a cDNA encoding the Rieske
            iron-sulfur protein of rat mitochondrial cytochrome bc1 complex
  JOURNAL   Biochem Biophys Res Commun 159 (1), 19-25 (1989)
   PUBMED   2538119
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085339.1.
            
            On Jan 6, 2005 this sequence version replaced XP_214457.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085339.1, FQ213498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..274
                     /product="cytochrome b-c1 complex subunit Rieske,
                     mitochondrial"
                     /EC_number="7.1.1.8"
                     /note="RISP; complex III subunit 5; rieske iron-sulfur
                     protein; cytochrome b-c1 complex subunit 5; Rieske protein
                     UQCRFS1; liver regeneration-related protein LRRGT00195;
                     ubiquinol-cytochrome c reductase iron-sulfur subunit"
                     /calculated_mol_wt=29315
     Region          2..77
                     /region_name="Ubiq-Cytc-red_N"
                     /note="Ubiquinol-cytochrome c reductase 8 kDa, N-terminal;
                     pfam09165"
                     /db_xref="CDD:462698"
     mat_peptide     79..274
                     /product="Cytochrome b-c1 complex subunit Rieske,
                     mitochondrial. /id=PRO_0000030671"
                     /note="propagated from UniProtKB/Swiss-Prot (P20788.2)"
                     /calculated_mol_wt=21465
     Region          80..145
                     /region_name="UCR_TM"
                     /note="Ubiquinol cytochrome reductase transmembrane
                     region; pfam02921"
                     /db_xref="CDD:460747"
     Site            104..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20788.2)"
     Region          151..274
                     /region_name="Rieske_cytochrome_bc1"
                     /note="Iron-sulfur protein (ISP) component of the bc(1)
                     complex family, Rieske domain; The Rieske domain is a
                     [2Fe-2S] cluster binding domain involved in electron
                     transfer. The bc(1) complex is a multisubunit enzyme found
                     in many different organisms including...; cd03470"
                     /db_xref="CDD:239552"
     Site            order(217,219..220,236,239,241)
                     /site_type="other"
                     /note="[2Fe-2S] cluster binding site [ion binding]"
                     /db_xref="CDD:239552"
     CDS             1..274
                     /gene="Uqcrfs1"
                     /gene_synonym="LRRGT00195"
                     /coded_by="NM_001008888.1:56..880"
                     /db_xref="GeneID:291103"
                     /db_xref="RGD:628838"
ORIGIN      
        1 mlsvaarsgp fapvlsatsr gvagalrpll qsavpatsep pvldvkrpfl creslsgqaa
       61 trplvatvgl nvpasvrysh tdikvpdfsd yrraevldst ksskessear kgfsylvtat
      121 ttvgvayaak navsqfvssm sasadvlams kieiklsdip egknmafkwr gkplfvrhrt
      181 kkeidqeaav evsqlrdpqh dlervkkpew viligvcthl gcvpianagd fggyycpchg
      241 shydasgrir kgpaplnlev ptyeftsgdv vvvg
//
LOCUS       NP_620435                308 aa            linear   ROD 28-APR-2025
DEFINITION  barttin [Rattus norvegicus].
ACCESSION   NP_620435
VERSION     NP_620435.1
DBSOURCE    REFSEQ: accession NM_138979.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Uetsuka,S., Ogata,G., Nagamori,S., Isozumi,N., Nin,F., Yoshida,T.,
            Komune,S., Kitahara,T., Kikkawa,Y., Inohara,H., Kanai,Y. and
            Hibino,H.
  TITLE     Molecular architecture of the stria vascularis membrane transport
            system, which is essential for physiological functions of the
            mammalian cochlea
  JOURNAL   Eur J Neurosci 42 (3), 1984-2002 (2015)
   PUBMED   26060893
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Wolf,K., Meier-Meitinger,M., Bergler,T., Castrop,H., Vitzthum,H.,
            Riegger,G.A., Kurtz,A. and Kramer,B.K.
  TITLE     Parallel down-regulation of chloride channel CLC-K1 and barttin
            mRNA in the thin ascending limb of the rat nephron by furosemide
  JOURNAL   Pflugers Arch 446 (6), 665-671 (2003)
   PUBMED   12759757
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Waldegger,S., Jeck,N., Barth,P., Peters,M., Vitzthum,H., Wolf,K.,
            Kurtz,A., Konrad,M. and Seyberth,H.W.
  TITLE     Barttin increases surface expression and changes current properties
            of ClC-K channels
  JOURNAL   Pflugers Arch 444 (3), 411-418 (2002)
   PUBMED   12111250
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Estevez,R., Boettger,T., Stein,V., Birkenhager,R., Otto,E.,
            Hildebrandt,F. and Jentsch,T.J.
  TITLE     Barttin is a Cl- channel beta-subunit crucial for renal Cl-
            reabsorption and inner ear K+ secretion
  JOURNAL   Nature 414 (6863), 558-561 (2001)
   PUBMED   11734858
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Birkenhager,R., Otto,E., Schurmann,M.J., Vollmer,M., Ruf,E.M.,
            Maier-Lutz,I., Beekmann,F., Fekete,A., Omran,H., Feldmann,D.,
            Milford,D.V., Jeck,N., Konrad,M., Landau,D., Knoers,N.V.,
            Antignac,C., Sudbrak,R., Kispert,A. and Hildebrandt,F.
  TITLE     Mutation of BSND causes Bartter syndrome with sensorineural
            deafness and kidney failure
  JOURNAL   Nat Genet 29 (3), 310-314 (2001)
   PUBMED   11687798
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081725.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081725.1, AJ421029.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA5760389
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..308
                     /product="barttin"
                     /note="Bartter syndrome, infantile, with sensorineural
                     deafness (Barttin); barttin CLCNK-type chloride channel
                     accessory beta subunit; barttin CLCNK type accessory beta
                     subunit"
                     /calculated_mol_wt=33764
     Region          1..72
                     /region_name="Regulates channel membrane trafficking and
                     anion conductance. /evidence=ECO:0000250|UniProtKB:Q8WZ55"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Site            6..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Region          27..242
                     /region_name="Barttin"
                     /note="Bartter syndrome, infantile, with sensorineural
                     deafness (Barttin); pfam15462"
                     /db_xref="CDD:464731"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIM4; propagated from
                     UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIM4; propagated from
                     UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Region          127..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Region          162..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R2H3.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q8R2H3.1)"
     CDS             1..308
                     /gene="Bsnd"
                     /coded_by="NM_138979.2:200..1126"
                     /db_xref="GeneID:192675"
                     /db_xref="RGD:621139"
ORIGIN      
        1 madektfrig fivlglflls lgtflmshdr pqvygtfyam gsimviggvl wsmcqcypki
       61 tfvpadsdfq gmlspkalsl letglsevks pqppyvrlwe eaaydqslpd fthiqmkvmg
      121 ysedprplla pelktgtssa kegephsaqt wmeaavvvhr eldekegeks rsqssppacs
      181 qgsaplasfh ddldvgsseg rspqpsppdr deahlqvpwa srgpldrfgd faliddtpis
      241 edmglegqaq eealpskqpw slrmkeetvq agaeepeqee edlyyglpds pgdplpdkel
      301 gfepdvqg
//
LOCUS       NP_071533                380 aa            linear   ROD 28-APR-2025
DEFINITION  protein c-Fos [Rattus norvegicus].
ACCESSION   NP_071533 XP_234422
VERSION     NP_071533.1
DBSOURCE    REFSEQ: accession NM_022197.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Glaeser,B., Panariello,V., Banerjee,A. and Olsen,C.M.
  TITLE     Environmental Enrichment during Abstinence Reduces Oxycodone
            Seeking and c-Fos Expression in a Subpopulation of Medial
            Prefrontal Cortex Neurons
  JOURNAL   Drug Alcohol Depend 255, 111077 (2024)
   PUBMED   38228055
  REMARK    GeneRIF: Environmental Enrichment during Abstinence Reduces
            Oxycodone Seeking and c-Fos Expression in a Subpopulation of Medial
            Prefrontal Cortex Neurons.
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Vega-Rivera,N.M., Estrada-Camarena,E., Azpilcueta-Morales,G.,
            Cervantes-Anaya,N., Trevino,S., Becerril-Villanueva,E. and
            Lopez-Rubalcava,C.
  TITLE     Chronic Variable Stress and Cafeteria Diet Combination Exacerbate
            Microglia and c-fos Activation but Not Experimental Anxiety or
            Depression in a Menopause Model
  JOURNAL   Int J Mol Sci 25 (3), 1455 (2024)
   PUBMED   38338735
  REMARK    GeneRIF: Chronic Variable Stress and Cafeteria Diet Combination
            Exacerbate Microglia and c-fos Activation but Not Experimental
            Anxiety or Depression in a Menopause Model.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Byun,Y. and Noh,J.
  TITLE     Social play exclusion model in adolescent rats: Monitoring
            locomotor and emotional behavior associated with social play and
            examining c-Fos expression in the brain
  JOURNAL   Physiol Behav 273, 114379 (2024)
   PUBMED   37858915
  REMARK    GeneRIF: Social play exclusion model in adolescent rats: Monitoring
            locomotor and emotional behavior associated with social play and
            examining c-Fos expression in the brain.
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Feng,L., A,L., Bao,T., Mu,X., Ta,N., Duan,Q., Ta,L., Chen,Y.,
            Bai,L. and Fu,M.
  TITLE     An integrated network analysis, RNA-seq and in vivo validation
            approaches to explore the protective mechanism of Mongolian
            medicine formulae Ruda-6 against indomethacin-induced gastric ulcer
            in rats
  JOURNAL   Front Pharmacol 14, 1181133 (2023)
   PUBMED   37637418
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Akdag,M.Z., Ogras,E., Doganyigit,Z., Akyuz,E., Akdag,M.B., Okan,A.,
            Akpolat,V. and Kullu,I.R.
  TITLE     The increase in c-fos expression in epileptic seizures is inhibited
            by magnetic field application, but not KCa1.1 channel expression
  JOURNAL   Electromagn Biol Med 42 (2), 81-97 (2023)
   PUBMED   37598353
  REMARK    GeneRIF: The increase in c-fos expression in epileptic seizures is
            inhibited by magnetic field application, but not KCa1.1 channel
            expression.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Reghunath,R.
  TITLE     Eye injuries and foreign bodies
  JOURNAL   Nurs J India 83 (6), 157-160 (1992)
   PUBMED   1298921
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Stopera,S.A., Davie,J.R. and Bird,R.P.
  TITLE     Colonic aberrant crypt foci are associated with increased
            expression of c-fos: the possible role of modified c-fos expression
            in preneoplastic lesions in colon cancer
  JOURNAL   Carcinogenesis 13 (4), 573-578 (1992)
   PUBMED   1576709
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Abate,C., Luk,D., Gentz,R., Rauscher,F.J. 3rd and Curran,T.
  TITLE     Expression and purification of the leucine zipper and DNA-binding
            domains of Fos and Jun: both Fos and Jun contact DNA directly
  JOURNAL   Proc Natl Acad Sci U S A 87 (3), 1032-1036 (1990)
   PUBMED   2105492
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1990 Jun;87(11):4411]
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Claycomb,W.C. and Lanson,N.A. Jr.
  TITLE     Proto-oncogene expression in proliferating and differentiating
            cardiac and skeletal muscle
  JOURNAL   Biochem J 247 (3), 701-706 (1987)
   PUBMED   2447874
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Leibovitch,S.A., Leibovitch,M.P., Guillier,M., Hillion,J. and
            Harel,J.
  TITLE     Differential expression of protooncogenes related to transformation
            and cancer progression in rat myoblasts
  JOURNAL   Cancer Res 46 (8), 4097-4103 (1986)
   PUBMED   2425941
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from DQ089699.1.
            
            On May 12, 2005 this sequence version replaced XP_234422.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ149169.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132264
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q31"
     Protein         1..380
                     /product="protein c-Fos"
                     /note="c-fos oncogene; v-fos FBJ murine osteosarcoma viral
                     oncogene homolog; proto-oncogene c-FOS; proto-oncogene
                     cFOS; FBJ osteosarcoma oncogene"
                     /calculated_mol_wt=40796
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P01100; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P01100; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Region          139..159
                     /region_name="Basic motif, required for the activation of
                     phospholipid synthesis, but not for CDS1-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P12841.1)"
     Region          147..200
                     /region_name="bZIP_Fos"
                     /note="Basic leucine zipper (bZIP) domain of the oncogene
                     Fos (Fos): a DNA-binding and dimerization domain; cd14721"
                     /db_xref="CDD:269869"
     Region          147..199
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269869"
     Site            order(158,161..162,165..166,168..169,172..173,175..176,
                     179..180,182..183,186..187,189..190,193..194,196..197)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269869"
     Region          165..193
                     /region_name="leucine zipper"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:7816602; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:17223854; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:17223854; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Region          354..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12841.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1, MAPK3 and RPS6KA3.
                     /evidence=ECO:0000269|PubMed:17223854; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1 and MAPK3.
                     /evidence=ECO:0000269|PubMed:17223854; propagated from
                     UniProtKB/Swiss-Prot (P12841.1)"
     CDS             1..380
                     /gene="Fos"
                     /gene_synonym="c-fos"
                     /coded_by="NM_022197.2:153..1295"
                     /db_xref="GeneID:314322"
                     /db_xref="RGD:2626"
ORIGIN      
        1 mmfsgfnady easssrcssa spagdslsyy hspadsfssm gspvntqdfc adlsvssanf
       61 iptvtaists pdlqwlvqpt lvssvapsqt raphpyglpt pstgayarag vvktmsggra
      121 qsigrrgkve qlspeeeekr rirrernkma aakcrnrrre ltdtlqaetd qledeksalq
      181 teianllkek eklefilaah rpackipndl gfpeemsvts ldltgglpea ttpeseeaft
      241 lpllndpepk pslepvknis nmelkaepfd dflfpassrp sgsetarsvp dvdlsgsfya
      301 adweplhsss lgmgpmvtel eplctpvvtc tpscttytss fvftypeads fpscaaahrk
      361 gsssnepssd slssptllal
//
LOCUS       NP_001012123             243 aa            linear   ROD 28-APR-2025
DEFINITION  complement C1q tumor necrosis factor-related protein 5 precursor
            [Rattus norvegicus].
ACCESSION   NP_001012123 XP_236180
VERSION     NP_001012123.1
DBSOURCE    REFSEQ: accession NM_001012123.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Yang,W.M. and Lee,W.
  TITLE     CTRP5 ameliorates palmitate-induced apoptosis and insulin
            resistance through activation of AMPK and fatty acid oxidation
  JOURNAL   Biochem Biophys Res Commun 452 (3), 715-721 (2014)
   PUBMED   25195818
  REMARK    GeneRIF: CTRP5 ameliorates palmitate-induced apoptosis and insulin
            resistance through activation of AMPK and fatty acid oxidation.
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Lu,C.C., Appler,J.M., Houseman,E.A. and Goodrich,L.V.
  TITLE     Developmental profiling of spiral ganglion neurons reveals insights
            into auditory circuit assembly
  JOURNAL   J Neurosci 31 (30), 10903-10918 (2011)
   PUBMED   21795542
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Park,S.Y., Choi,J.H., Ryu,H.S., Pak,Y.K., Park,K.S., Lee,H.K. and
            Lee,W.
  TITLE     C1q tumor necrosis factor alpha-related protein isoform 5 is
            increased in mitochondrial DNA-depleted myocytes and activates
            AMP-activated protein kinase
  JOURNAL   J Biol Chem 284 (41), 27780-27789 (2009)
   PUBMED   19651784
  REMARK    GeneRIF: These results highlight C1QTNF5 as a putative biomarker
            for mitochondrial dysfunction and a potent activator of AMPK.
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wong,G.W., Krawczyk,S.A., Kitidis-Mitrokostas,C., Revett,T.,
            Gimeno,R. and Lodish,H.F.
  TITLE     Molecular, biochemical and functional characterizations of C1q/TNF
            family members: adipose-tissue-selective expression patterns,
            regulation by PPAR-gamma agonist, cysteine-mediated
            oligomerizations, combinatorial associations and metabolic
            functions
  JOURNAL   Biochem J 416 (2), 161-177 (2008)
   PUBMED   18783346
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Mandal,M.N., Vasireddy,V., Reddy,G.B., Wang,X., Moroi,S.E.,
            Pattnaik,B.R., Hughes,B.A., Heckenlively,J.R., Hitchcock,P.F.,
            Jablonski,M.M. and Ayyagari,R.
  TITLE     CTRP5 is a membrane-associated and secretory protein in the RPE and
            ciliary body and the S163R mutation of CTRP5 impairs its secretion
  JOURNAL   Invest Ophthalmol Vis Sci 47 (12), 5505-5513 (2006)
   PUBMED   17122142
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089992.1.
            
            On Feb 11, 2005 this sequence version replaced XP_236180.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089992.1, CO404596.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..243
                     /product="complement C1q tumor necrosis factor-related
                     protein 5 precursor"
                     /note="complement C1q tumor necrosis factor-related
                     protein 5; C1q and tumor necrosis factor related protein
                     5; adiponectin e"
                     /calculated_mol_wt=23815
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1538
     Region          15..124
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH0.1)"
     mat_peptide     16..243
                     /product="Complement C1q tumor necrosis factor-related
                     protein 5. /id=PRO_0000003537"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVH0.1)"
                     /calculated_mol_wt=23815
     Region          29..95
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          105..232
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..243
                     /gene="C1qtnf5"
                     /gene_synonym="Adie"
                     /coded_by="NM_001012123.1:232..963"
                     /db_xref="GeneID:315598"
                     /db_xref="RGD:1308802"
ORIGIN      
        1 mrpllallll glasgsppld dnkipslcpg qpglpgtpgh hgsqglpgrd grdgrdgapg
       61 apgekgeggr pglpgprgep gprgeagpvg aigpagecsv pprsafsakr sesrvpppad
      121 tplpfdrvll neqghydatt gkftcqvpgv yyfavhatvy raslqfdlvk ngqsiasffq
      181 ffggwpkpas lsggamvrle pedqvwvqvg vgdyigiyas iktdstfsgf lvysdwhssp
      241 vfa
//
LOCUS       NP_001029305             406 aa            linear   ROD 28-APR-2025
DEFINITION  kelch domain-containing protein 2 [Rattus norvegicus].
ACCESSION   NP_001029305 XP_216721
VERSION     NP_001029305.1
DBSOURCE    REFSEQ: accession NM_001034133.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105756.1.
            
            On Oct 14, 2005 this sequence version replaced XP_216721.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105756.1, CF110746.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..406
                     /product="kelch domain-containing protein 2"
                     /calculated_mol_wt=45795
     Region          31..85
                     /region_name="Kelch 1.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     Region          32..91
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          32..89
                     /region_name="Kelch_4"
                     /note="Galactose oxidase, central domain; pfam13418"
                     /db_xref="CDD:433191"
     Region          78..341
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          92..138
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          92..136
                     /region_name="Kelch 2.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     Region          148..207
                     /region_name="Kelch 3.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     Region          218..265
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          221..259
                     /region_name="Kelch 4.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     Region          271..311
                     /region_name="Kelch 5.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     Region          322..359
                     /region_name="Kelch 6.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2U9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRE6.1)"
     CDS             1..406
                     /gene="Klhdc2"
                     /coded_by="NM_001034133.1:177..1397"
                     /db_xref="GeneID:299113"
                     /db_xref="RGD:1306504"
ORIGIN      
        1 madgnedara edmpgpafeg yeamelacpa ersghvavsd grhmfvwggy ksnqvrglyd
       61 fylpreelwi ynmetgrwkk integdvpps msgscavcvd rvlylfgghh srgntnkfym
      121 ldsrsadrvl qweridcqgi ppsskdklgv wvyknkliff ggygylpedk vlgtfefdet
      181 sfwnsshprg wndhvhildt etfawsqpit tgkapspraa hacatvgnkg fvfggryrda
      241 rmndlhylnl dtwewnelip qgicpvgrsw hsltpvssdh lflfggftte kqplsdawty
      301 cisknewiqf nhpyvekprl whtacasdeg evivfggcan nllvhhraah snevlifsvq
      361 pkslvrlsle avicfkemla nswsclpkhl lhsvnqrfgs nntsgs
//
LOCUS       NP_058765                493 aa            linear   ROD 28-APR-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-3 precursor [Rattus
            norvegicus].
ACCESSION   NP_058765
VERSION     NP_058765.3
DBSOURCE    REFSEQ: accession NM_017069.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Montoya-Gress,L., Juarez-Rojas,L., Almanza-Perez,J.,
            Farfan-Garcia,E., Gomez-Quiroz,L., Ommati,M.M., Heidari,R.,
            Querejeta-Villagomez,E., Alatorre-Perez,A. and Retana-Marquez,S.
  TITLE     Changes in D4 and GABAA subunit alpha3 receptors in the thalamic
            reticular nucleus caused by unilateral lesion of the globus
            pallidus
  JOURNAL   Acta Neurobiol Exp (Wars) 84 (3), 275-287 (2024)
   PUBMED   39392023
  REMARK    GeneRIF: Changes in D4 and GABAA subunit alpha3 receptors in the
            thalamic reticular nucleus caused by unilateral lesion of the
            globus pallidus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Ordaz,R.P., Garay,E., Limon,A., Perez-Samartin,A.,
            Sanchez-Gomez,M.V., Robles-Martinez,L., Cisneros-Mejorado,A.,
            Matute,C. and Arellano,R.O.
  TITLE     GABAA Receptors Expressed in Oligodendrocytes Cultured from the
            Neonatal Rat Contain alpha3 and gamma1 Subunits and Present
            Differential Functional and Pharmacological Properties
  JOURNAL   Mol Pharmacol 99 (2), 133-146 (2021)
   PUBMED   33288547
  REMARK    GeneRIF: GABAA Receptors Expressed in Oligodendrocytes Cultured
            from the Neonatal Rat Contain alpha3 and gamma1 Subunits and
            Present Differential Functional and Pharmacological Properties.
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Liu,X., Wei,F., Cheng,Y., Zhang,Y., Jia,G., Zhou,J., Zhu,M.,
            Shan,Y., Sun,X., Yu,L., Merzenich,M.M., Lurie,D.I., Zheng,Q. and
            Zhou,X.
  TITLE     Auditory Training Reverses Lead (Pb)-Toxicity-Induced Changes in
            Sound-Azimuth Selectivity of Cortical Neurons
  JOURNAL   Cereb Cortex 29 (8), 3294-3304 (2019)
   PUBMED   30137254
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Nair,B., Johar,K., Priya,A. and Wong-Riley,M.T.
  TITLE     Specificity protein 4 (Sp4) transcriptionally regulates inhibitory
            GABAergic receptors in neurons
  JOURNAL   Biochim Biophys Acta 1863 (1), 1-9 (2016)
   PUBMED   26469128
  REMARK    GeneRIF: Sp4 functionally regulates the transcription of Gabra1
            (GABAA alpha1) and Gabra2 (GABAA alpha2), but not Gabra3 (GABAA
            alpha3) subunit genes.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Sarkar,S. and Chang,S.L.
  TITLE     Ethanol concentration-dependent alterations in gene expression
            during acute binge drinking in the HIV-1 transgenic rat
  JOURNAL   Alcohol Clin Exp Res 37 (7), 1082-1090 (2013)
   PUBMED   23413777
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Sigamoni,M.
  TITLE     Planning nursing education for 2000 AD: in pursuit of reality
  JOURNAL   Nurs J India 83 (7), 163-168 (1992)
   PUBMED   1298923
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Wisden,W. and Seeburg,P.H.
  TITLE     GABAA receptor channels: from subunits to functional entities
  JOURNAL   Curr Opin Neurobiol 2 (3), 263-269 (1992)
   PUBMED   1379501
  REMARK    Review article
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Laurie,D.J., Seeburg,P.H. and Wisden,W.
  TITLE     The distribution of 13 GABAA receptor subunit mRNAs in the rat
            brain. II. Olfactory bulb and cerebellum
  JOURNAL   J Neurosci 12 (3), 1063-1076 (1992)
   PUBMED   1312132
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Wisden,W., Laurie,D.J., Monyer,H. and Seeburg,P.H.
  TITLE     The distribution of 13 GABAA receptor subunit mRNAs in the rat
            brain. I. Telencephalon, diencephalon, mesencephalon
  JOURNAL   J Neurosci 12 (3), 1040-1062 (1992)
   PUBMED   1312131
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Seeburg,P.H., Wisden,W., Verdoorn,T.A., Pritchett,D.B., Werner,P.,
            Herb,A., Luddens,H., Sprengel,R. and Sakmann,B.
  TITLE     The GABAA receptor family: molecular and functional diversity
  JOURNAL   Cold Spring Harb Symp Quant Biol 55, 29-40 (1990)
   PUBMED   1966765
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            On Aug 30, 2012 this sequence version replaced NP_058765.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X51991.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            RefSeq Select criteria           :: based on conservation, longest
                                                protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq37"
     Protein         1..493
                     /product="gamma-aminobutyric acid receptor subunit alpha-3
                     precursor"
                     /note="gamma-aminobutyric acid receptor subunit alpha-3;
                     GABA(A) receptor subunit alpha-3; Gamma-animobutyric acid
                     (GABA) A receptor, alpha 3; gamma-aminobutyric acid
                     (GABA-A) receptor, subunit alpha 3; gamma-aminobutyric
                     acid type A receptor alpha3 subunit; GABA-A receptor
                     alpha-3 subunit; gamma-aminobutyric acid (GABA) A
                     receptor, alpha 3; GABAAR subunit alpha-3"
                     /calculated_mol_wt=52285
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3163
     Region          27..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
     mat_peptide     29..493
                     /product="Gamma-aminobutyric acid receptor subunit
                     alpha-3. /id=PRO_0000000439"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
                     /calculated_mol_wt=52285
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Region          69..479
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          75..274
                     /region_name="LGIC_ECD_GABAAR_A3"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-3 (GABAAR-A3 or GABRA3); cd19036"
                     /db_xref="CDD:349837"
     Site            order(89,117)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349837"
     Site            order(101,103..104,109..110,117,119..120,137,139..140,
                     149..154,157,159,161..162,168..170,172,182..184,212,274)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349837"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Region          191..205
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349837"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            277..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
     Site            304..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
     Site            338..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26049; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P26049; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26049; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26049; propagated from
                     UniProtKB/Swiss-Prot (P20236.2)"
     Site            459..480
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20236.2)"
     CDS             1..493
                     /gene="Gabra3"
                     /coded_by="NM_017069.3:238..1719"
                     /db_xref="GeneID:24947"
                     /db_xref="RGD:2648"
ORIGIN      
        1 mittqmwhfy vtrvglllli silpgttgqg esrrqepgdf vkqdigglsp khapdipdds
       61 tdnitiftri ldrlldgydn rlrpglgdav tevktdiyvt sfgpvsdtdm eytidvffrq
      121 twhderlkfd gpmkilplnn llaskiwtpd tffhngkksv ahnmttpnkl lrlvdngtll
      181 ytmrltihae cpmhledfpm dvhacplkfg syaytkaevi yswtlgknks vevaqdgsrl
      241 nqydllghvv gteiirsstg eyvvmtthfh lkrkigyfvi qtylpcimtv ilsqvsfwln
      301 resvpartvf gvttvltmtt lsisarnslp kvayatamdw fiavcyafvf saliefatvn
      361 yftkrswawe gkkvpealem kkktpaaptk ktsttfnivg ttypinlakd tefstiskaa
      421 aapsasstpt viaspkttyv qdspaetkty nsvskvdkis riifpvlfai fnlvywatyv
      481 nresaikgmi rkq
//
LOCUS       NP_068527                352 aa            linear   ROD 28-APR-2025
DEFINITION  ly6/PLAUR domain-containing protein 3 precursor [Rattus
            norvegicus].
ACCESSION   NP_068527
VERSION     NP_068527.1
DBSOURCE    REFSEQ: accession NM_021759.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Ngora,H., Galli,U.M., Miyazaki,K. and Zoller,M.
  TITLE     Membrane-bound and exosomal metastasis-associated C4.4A promotes
            migration by associating with the alpha(6)beta(4) integrin and
            MT1-MMP
  JOURNAL   Neoplasia 14 (2), 95-107 (2012)
   PUBMED   22431918
  REMARK    GeneRIF: the first explanation for the C4.4A contribution to wound
            healing and metastasis.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Kriegbaum,M.C., Jacobsen,B., Hald,A. and Ploug,M.
  TITLE     Expression of C4.4A, a structural uPAR homolog, reflects squamous
            epithelial differentiation in the adult mouse and during
            embryogenesis
  JOURNAL   J Histochem Cytochem 59 (2), 188-201 (2011)
   PUBMED   21339181
  REMARK    GeneRIF: a possible functional role of C4.4A in early
            differentiation of stratified squamous epithelia
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Paret,C., Bourouba,M., Beer,A., Miyazaki,K., Schnolzer,M.,
            Fiedler,S. and Zoller,M.
  TITLE     Ly6 family member C4.4A binds laminins 1 and 5, associates with
            galectin-3 and supports cell migration
  JOURNAL   Int J Cancer 115 (5), 724-733 (2005)
   PUBMED   15729693
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Wurfel,J., Seiter,S., Stassar,M., Claas,A., Klas,R., Rosel,M.,
            Marhaba,R., Savelyeva,L., Schwab,M., Matzku,S. and Zoller,M.
  TITLE     Cloning of the human homologue of the metastasis-associated rat
            C4.4A
  JOURNAL   Gene 262 (1-2), 35-41 (2001)
   PUBMED   11179665
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Rosel,M., Claas,C., Seiter,S., Herlevsen,M. and Zoller,M.
  TITLE     Cloning and functional characterization of a new
            phosphatidyl-inositol anchored molecule of a metastasizing rat
            pancreatic tumor
  JOURNAL   Oncogene 17 (15), 1989-2002 (1998)
   PUBMED   9788443
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ001043.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ001043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132302, SAMN16676810
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Rattus norvegicus"
                     /strain="BDIX"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..352
                     /product="ly6/PLAUR domain-containing protein 3 precursor"
                     /note="ly6/PLAUR domain-containing protein 3; GPI-anchored
                     metastasis-associated protein C4.4A; metastasis-associated
                     GPI-anchored protein; metastasis-associated molecule;
                     GPI-anchored metastasis-associated protein homolog"
                     /calculated_mol_wt=33352
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3627
     mat_peptide     33..330
                     /product="Ly6/PLAUR domain-containing protein 3.
                     /id=PRO_0000226755"
                     /note="propagated from UniProtKB/Swiss-Prot (O55162.1)"
                     /calculated_mol_wt=31224
     Region          33..119
                     /region_name="TFP_LU_ECD_LYPD3_rpt1"
                     /note="first extracellular domain (ECD) found in Ly6/PLAUR
                     domain-containing protein 3 (LYPD3) and similar proteins;
                     cd23562"
                     /db_xref="CDD:467092"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O55162.1)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O55162.1)"
     Region          138..228
                     /region_name="TFP_LU_ECD_LYPD3_rpt2"
                     /note="second extracellular domain (ECD) found in
                     Ly6/PLAUR domain-containing protein 3 (LYPD3) and similar
                     proteins; cd23563"
                     /db_xref="CDD:467093"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O55162.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O55162.1)"
     Region          236..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O55162.1)"
     CDS             1..352
                     /gene="Lypd3"
                     /gene_synonym="C4.4a"
                     /coded_by="NM_021759.1:81..1139"
                     /db_xref="GeneID:60378"
                     /db_xref="RGD:69053"
ORIGIN      
        1 mdaarrgdtq pvmwttrwll llplllcega qalecyscvq kaddgcsphk mktvkcgpgv
       61 dvcteavgav esihgqfsva vrgcgsgipg kndrgldlhg llafiqlqqc tedrcnakln
      121 ltlrglnpag nesayehnga ecyscmglsr ekcqgamppv vncynasgrv ykgcfdgnvt
      181 ltaanvtvsl pvrgcvqdea ctrdgvtgpg ftlsgsccqg prcnsdlrnk tyfsprippl
      241 vllpppttpa pstrtqnsss ttsttaptta tttikpttvq ashtssthet eheviqeegs
      301 hlsggatghq drsnmgkfpe kggaqipskg gsdalgswls ailltvvaga ml
//
LOCUS       NP_001101200             955 aa            linear   ROD 28-APR-2025
DEFINITION  kinesin heavy chain isoform 5C [Rattus norvegicus].
ACCESSION   NP_001101200 XP_001064328 XP_241981
VERSION     NP_001101200.1
DBSOURCE    REFSEQ: accession NM_001107730.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Mingardi,J., Paoli,C., La Via,L., Carini,G., Misztak,P., Cifani,C.,
            Popoli,M., Barbon,A. and Musazzi,L.
  TITLE     Involvement of miR-135a-5p Downregulation in Acute and Chronic
            Stress Response in the Prefrontal Cortex of Rats
  JOURNAL   Int J Mol Sci 24 (2), 1552 (2023)
   PUBMED   36675068
  REMARK    GeneRIF: Involvement of miR-135a-5p Downregulation in Acute and
            Chronic Stress Response in the Prefrontal Cortex of Rats.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Brachet,A., Lario,A., Fernandez-Rodrigo,A., Heisler,F.F.,
            Gutierrez,Y., Lobo,C., Kneussel,M. and Esteban,J.A.
  TITLE     A kinesin 1-protrudin complex mediates AMPA receptor synaptic
            removal during long-term depression
  JOURNAL   Cell Rep 36 (5), 109499 (2021)
   PUBMED   34348158
  REMARK    GeneRIF: A kinesin 1-protrudin complex mediates AMPA receptor
            synaptic removal during long-term depression.
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Budaitis,B.G., Jariwala,S., Reinemann,D.N., Schimert,K.I.,
            Scarabelli,G., Grant,B.J., Sept,D., Lang,M.J. and Verhey,K.J.
  TITLE     Neck linker docking is critical for Kinesin-1 force generation in
            cells but at a cost to motor speed and processivity
  JOURNAL   Elife 8, e44146 (2019)
   PUBMED   31084716
  REMARK    GeneRIF: These results demonstrate that the neck linker serves as a
            mechanical element for kinesin-1 transport under physiological
            conditions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 955)
  AUTHORS   Oksdath,M., Guil,A.F.N., Grassi,D., Sosa,L.J. and Quiroga,S.
  TITLE     The Motor KIF5C Links the Requirements of Stable Microtubules and
            IGF-1 Receptor Membrane Insertion for Neuronal Polarization
  JOURNAL   Mol Neurobiol 54 (8), 6085-6096 (2017)
   PUBMED   27699600
  REMARK    GeneRIF: We conclude that the enrichment of stable microtubules in
            the future axon enhances KIF5C-mediated vesicular transport of
            syntaxin 6 and VAMP4, which in turn mediates the polarized
            insertion of IGF-1r in the plasmalemma, a key step for neuronal
            polarization
REFERENCE   5  (residues 1 to 955)
  AUTHORS   Sanger,A., Yip,Y.Y., Randall,T.S., Pernigo,S., Steiner,R.A. and
            Dodding,M.P.
  TITLE     SKIP controls lysosome positioning using a composite kinesin-1
            heavy and light chain-binding domain
  JOURNAL   J Cell Sci 130 (9), 1637-1651 (2017)
   PUBMED   28302907
  REMARK    GeneRIF: cargo recognition and concurrent activation of kinesin-1
            proceed in hierarchical stepwise fashion driven by a dynamic
            network of inter- and intra-molecular interactions.
REFERENCE   6  (residues 1 to 955)
  AUTHORS   Verhey,K.J., Meyer,D., Deehan,R., Blenis,J., Schnapp,B.J.,
            Rapoport,T.A. and Margolis,B.
  TITLE     Cargo of kinesin identified as JIP scaffolding proteins and
            associated signaling molecules
  JOURNAL   J Cell Biol 152 (5), 959-970 (2001)
   PUBMED   11238452
REFERENCE   7  (residues 1 to 955)
  AUTHORS   Kanai,Y., Okada,Y., Tanaka,Y., Harada,A., Terada,S. and Hirokawa,N.
  TITLE     KIF5C, a novel neuronal kinesin enriched in motor neurons
  JOURNAL   J Neurosci 20 (17), 6374-6384 (2000)
   PUBMED   10964943
REFERENCE   8  (residues 1 to 955)
  AUTHORS   Kozielski,F., Sack,S., Marx,A., Thormahlen,M., Schonbrunn,E.,
            Biou,V., Thompson,A., Mandelkow,E.M. and Mandelkow,E.
  TITLE     The crystal structure of dimeric kinesin and implications for
            microtubule-dependent motility
  JOURNAL   Cell 91 (7), 985-994 (1997)
   PUBMED   9428521
REFERENCE   9  (residues 1 to 955)
  AUTHORS   Sack,S., Muller,J., Marx,A., Thormahlen,M., Mandelkow,E.M.,
            Brady,S.T. and Mandelkow,E.
  TITLE     X-ray structure of motor and neck domains from rat brain kinesin
  JOURNAL   Biochemistry 36 (51), 16155-16165 (1997)
   PUBMED   9405049
REFERENCE   10 (residues 1 to 955)
  AUTHORS   Lockhart,A., Crevel,I.M. and Cross,R.A.
  TITLE     Kinesin and ncd bind through a single head to microtubules and
            compete for a shared MT binding site
  JOURNAL   J Mol Biol 249 (4), 763-771 (1995)
   PUBMED   7602588
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473983.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_241981.3, XP_001064328.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q12"
     Protein         1..955
                     /product="kinesin heavy chain isoform 5C"
                     /note="kinesin heavy chain neuron-specific 2; kinesin-1"
                     /calculated_mol_wt=109052
     Region          6..327
                     /region_name="KISc_KHC_KIF5"
                     /note="Kinesin motor domain, kinesin heavy chain (KHC) or
                     KIF5-like subgroup; cd01369"
                     /db_xref="CDD:276820"
     Site            order(16,86,89,91..94,232)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276820"
     Site            order(157..159,162,276,280..281)
                     /site_type="other"
                     /note="beta tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Site            order(158..160,162,238..240,249,253,257,276,281)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276820"
     Region          174..315
                     /region_name="Microtubule-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P56536.3)"
     Site            order(236,238..239,253,256..257,260)
                     /site_type="other"
                     /note="alpha tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P28738; propagated from
                     UniProtKB/Swiss-Prot (P56536.3)"
     Region          407..>751
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          616..>923
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          835..904
                     /region_name="Khc_CBD_cc"
                     /note="cargo binding coiled-coil domain found in kinesin
                     heavy chains; cd23649"
                     /db_xref="CDD:467880"
     Region          859..955
                     /region_name="Globular"
                     /note="propagated from UniProtKB/Swiss-Prot (P56536.3)"
     Region          909..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56536.3)"
     CDS             1..955
                     /gene="Kif5c"
                     /coded_by="NM_001107730.1:352..3219"
                     /db_xref="GeneID:311024"
                     /db_xref="RGD:1308539"
ORIGIN      
        1 madpaecsik vmcrfrplne aeilrgdkfi pkfkgeetvv igqgkpyvfd rvlppnttqe
       61 qvynacakqi vkdvlegyng tifaygqtss gkthtmegkl hdpqlmgiip riahdifdhi
      121 ysmdenlefh ikvsyfeiyl dkirdlldvs ktnlavhedk nrvpyvkgct erfvsspeev
      181 mdvidegkan rhvavtnmne hssrshsifl inikqenvet ekklsgklyl vdlagsekvs
      241 ktgaegavld eakninksls algnvisala egtkthvpyr dskmtrilqd slggncrtti
      301 viccspsvfn eaetkstlmf gqraktiknt vsvnleltae ewkkkyekek eknkalksvi
      361 qhlevelnrw rngeavpede qisakdqknl epcdntpiid nitpvvdgis aekekydeei
      421 tslyrqlddk ddeinqqsql aeklkqqmld qdellastrr dyekiqeelt rlqieneaak
      481 devkevlqal eelavnydqk sqevedktra neqltdelaq ktttltttqr elsqlqelsn
      541 hqkkrateil nlllkdlgei ggiigtndvk tladvngvie eeftmarlyi skmksevksl
      601 vnrskqlesa qtdsnrkmna serelaacql lisqheakik sltdymqnme qkrrqleesq
      661 dslseelakl raqekmhevs fqdkekehlt rlqdaeevkk aleqqmeshr eahqkqlsrl
      721 rdeieekqri ideirdlnqk lqleqerlss dynklkiedq erevklekll llndkreqar
      781 edlkgleetv srelqtlhnl rklfvqdltt rvkksvelds ddgggsaaqk qkisflennl
      841 eqltkvhkql vrdnadlrce lpklekrlra taervkales alkeakenam rdrkryqqev
      901 drikeavrak nmarrahsaq iakpirpghy passptavha vrggggssns thyqk
//
LOCUS       NP_058886                626 aa            linear   ROD 28-APR-2025
DEFINITION  myelin-associated glycoprotein precursor [Rattus norvegicus].
ACCESSION   NP_058886
VERSION     NP_058886.1
DBSOURCE    REFSEQ: accession NM_017190.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Nikulina,E., Gkioka,V., Siddiq,M.M., Mellado,W., Hilaire,M.,
            Cain,C.R., Hannila,S.S. and Filbin,M.T.
  TITLE     Myelin-associated glycoprotein inhibits neurite outgrowth through
            inactivation of the small GTPase Rap1
  JOURNAL   FEBS Lett 594 (9), 1389-1402 (2020)
   PUBMED   31985825
  REMARK    GeneRIF: Myelin-associated glycoprotein inhibits neurite outgrowth
            through inactivation of the small GTPase Rap1.
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Pronker,M.F., Lemstra,S., Snijder,J., Heck,A.J., Thies-Weesie,D.M.,
            Pasterkamp,R.J. and Janssen,B.J.
  TITLE     Structural basis of myelin-associated glycoprotein adhesion and
            signalling
  JOURNAL   Nat Commun 7, 13584 (2016)
   PUBMED   27922006
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Hu,B., Arpag,S., Zhang,X., Mobius,W., Werner,H., Sosinsky,G.,
            Ellisman,M., Zhang,Y., Hamilton,A., Chernoff,J. and Li,J.
  TITLE     Tuning PAK Activity to Rescue Abnormal Myelin Permeability in HNPP
  JOURNAL   PLoS Genet 12 (9), e1006290 (2016)
   PUBMED   27583434
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Palandri,A., Salvador,V.R., Wojnacki,J., Vivinetto,A.L.,
            Schnaar,R.L. and Lopez,P.H.
  TITLE     Myelin-associated glycoprotein modulates apoptosis of motoneurons
            during early postnatal development via NgR/p75(NTR)
            receptor-mediated activation of RhoA signaling pathways
  JOURNAL   Cell Death Dis 6 (9), e1876 (2015)
   PUBMED   26335717
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Lossos,A., Elazar,N., Lerer,I., Schueler-Furman,O., Fellig,Y.,
            Glick,B., Zimmerman,B.E., Azulay,H., Dotan,S., Goldberg,S.,
            Gomori,J.M., Ponger,P., Newman,J.P., Marreed,H., Steck,A.J.,
            Schaeren-Wiemers,N., Mor,N., Harel,M., Geiger,T.,
            Eshed-Eisenbach,Y., Meiner,V. and Peles,E.
  TITLE     Myelin-associated glycoprotein gene mutation causes
            Pelizaeus-Merzbacher disease-like disorder
  JOURNAL   Brain 138 (Pt 9), 2521-2536 (2015)
   PUBMED   26179919
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Pedraza,L., Owens,G.C., Green,L.A. and Salzer,J.L.
  TITLE     The myelin-associated glycoproteins: membrane disposition, evidence
            of a novel disulfide linkage between immunoglobulin-like domains,
            and posttranslational palmitylation
  JOURNAL   J Cell Biol 111 (6 Pt 1), 2651-2661 (1990)
   PUBMED   1703542
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Owens,G.C., Boyd,C.J., Bunge,R.P. and Salzer,J.L.
  TITLE     Expression of recombinant myelin-associated glycoprotein in primary
            Schwann cells promotes the initial investment of axons by
            myelinating Schwann cells
  JOURNAL   J Cell Biol 111 (3), 1171-1182 (1990)
   PUBMED   1697293
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Arquint,M., Roder,J., Chia,L.S., Down,J., Wilkinson,D., Bayley,H.,
            Braun,P. and Dunn,R.
  TITLE     Molecular cloning and primary structure of myelin-associated
            glycoprotein
  JOURNAL   Proc Natl Acad Sci U S A 84 (2), 600-604 (1987)
   PUBMED   2432614
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Johnson,D., Sato,S., Quarles,R.H., Inuzuka,T., Brady,R.O. and
            Tourtellotte,W.W.
  TITLE     Quantitation of the myelin-associated glycoprotein in human nervous
            tissue from controls and multiple sclerosis patients
  JOURNAL   J Neurochem 46 (4), 1086-1093 (1986)
   PUBMED   2419505
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Sternberger,N.H., Quarles,R.H., Itoyama,Y. and Webster,H.D.
  TITLE     Myelin-associated glycoprotein demonstrated immunocytochemically in
            myelin and myelin-forming cells of developing rat
  JOURNAL   Proc Natl Acad Sci U S A 76 (3), 1510-1514 (1979)
   PUBMED   375239
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M16800.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M16800.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760389,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..626
                     /product="myelin-associated glycoprotein precursor"
                     /note="S-MAG (C-term.); siglec-4a; brain neuron
                     cytoplasmic protein 3; sialic acid-binding Ig-like lectin
                     4a"
                     /calculated_mol_wt=67474
     sig_peptide     1..16
                     /note="myelin-associated glycoprotein signal peptide
                     (put.); putative"
                     /calculated_mol_wt=1897
     mat_peptide     17..626
                     /product="myelin-associated glycoprotein"
                     /calculated_mol_wt=67474
     Region          20..325
                     /region_name="Interaction with RTN4R and RTN4RL2.
                     /evidence=ECO:0000269|PubMed:19420245"
                     /note="propagated from UniProtKB/Swiss-Prot (P07722.1)"
     Region          22..138
                     /region_name="IgV_CD33"
                     /note="Immunoglobulin Variable (IgV) domain at the
                     N-terminus of CD33 and related Siglecs (sialic
                     acid-binding Ig-like lectins); cd05712"
                     /db_xref="CDD:409377"
     Region          22..46
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          22..26
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409377"
     Region          29..33
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409377"
     Region          35..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409377"
     Region          47..54
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          55..62
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          55..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409377"
     Region          63..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          73..76
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409377"
     Region          87..120
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          88..92
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409377"
     Region          98..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409377"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Region          113..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409377"
     Site            order(118,127..128)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409377"
     Region          121..125
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          126..138
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409377"
     Region          126..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409377"
     Region          141..235
                     /region_name="IgC2_CD33_d2_like"
                     /note="Second immunoglobulin domain of Cluster of
                     Differentiation (CD) 33 and related Siglecs; member of the
                     C2-set of IgSF domains; cd20987"
                     /db_xref="CDD:409579"
     Region          141..145
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409579"
     Region          154..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409579"
     Region          171..176
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409579"
     Region          200..206
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409579"
     Region          213..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409579"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Region          227..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409579"
     Region          239..309
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Region          333..409
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          343..347
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..360
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          375..379
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          389..394
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            450
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            454
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            517..536
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07722.1)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P07722.1)"
     Region          577..626
                     /region_name="Required for normal axon myelination in the
                     central nervous system.
                     /evidence=ECO:0000250|UniProtKB:P20917"
                     /note="propagated from UniProtKB/Swiss-Prot (P07722.1)"
     Region          581..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07722.1)"
     CDS             1..626
                     /gene="Mag"
                     /gene_synonym="1B236"
                     /coded_by="NM_017190.4:163..2043"
                     /db_xref="GeneID:29409"
                     /db_xref="RGD:3035"
ORIGIN      
        1 miflttlplf wimisasrgg hwgawmpssi safegtcvsi pcrfdfpdel rpavvhgvwy
       61 fnspypknyp pvvfksrtqv vhesfqgrsr llgdlglrnc tlllstlspe lggkyyfrgd
      121 lggynqytfs ehsvldiint pnivvppevv agtevevscm vpdncpelrp elswlghegl
      181 geptvlgrlr edegtwvqvs llhfvptrea nghrlgcqaa fpnttlqfeg yasldvkypp
      241 vivemnssve aiegshvsll cgadsnpppl ltwmrdgmvl reavaeslyl dleevtpaed
      301 giyaclaena ygqdnrtvel svmyapwkpt vngtvvaveg etvsilcstq snpdpiltif
      361 kekqilatvi yesqlqlelp avtpeddgey wcvaenqygq ratafnlsve fapiillesh
      421 caaardtvqc lcvvksnpep svafelpsrn vtvneteref vysersglll tsiltlrgqa
      481 qapprvicts rnlygtqsle lpfqgahrlm wakigpvgav vafailiaiv cyitqtrrkk
      541 nvtespsfsa gdnphvlysp efrisgapdk yesekrlgse rrllglrgep peldlsyshs
      601 dlgkrptkds ytlteelaey aeirvk
//
LOCUS       NP_001001510             608 aa            linear   ROD 28-APR-2025
DEFINITION  kelch-like protein 10 [Rattus norvegicus].
ACCESSION   NP_001001510 XP_220973
VERSION     NP_001001510.1
DBSOURCE    REFSEQ: accession NM_001001510.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Yan,W., Ma,L., Burns,K.H. and Matzuk,M.M.
  TITLE     Haploinsufficiency of kelch-like protein homolog 10 causes
            infertility in male mice
  JOURNAL   Proc Natl Acad Sci U S A 101 (20), 7793-7798 (2004)
   PUBMED   15136734
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY495338.1.
            
            On Aug 30, 2004 this sequence version replaced XP_220973.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY495338.1, BC085842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..608
                     /product="kelch-like protein 10"
                     /calculated_mol_wt=68832
     Region          36..572
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          292..339
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Region          329..372
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          340..386
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Region          376..420
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          388..433
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Region          423..466
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          434..480
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Region          470..513
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          481..527
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6JEL3.1)"
     Region          517..560
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          529..574
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL3.1)"
     CDS             1..608
                     /gene="Klhl10"
                     /coded_by="NM_001001510.1:108..1934"
                     /db_xref="GeneID:303533"
                     /db_xref="RGD:1303290"
ORIGIN      
        1 memessaast rfhqphmerk msamtceifn elrlegklcd vvikvngfef nahknilcsc
       61 ssyfralfts gwnntekkvy nipgispdmm kliieyaytr tvpitpdnve kllaaadqfn
      121 imgivrgcce flkselcldn cigickftdy yycpelrqka ymfilhnfee mvkvsaefle
      181 lsvtelkdii ekdelnvkqe davfeailkw ishdpqnrkq hisvllpkvr lalmhaeyfm
      241 nnvkmndyvk dseeckpvii nalkamydln mngpsnsdft npltrprlpy ailfaiggws
      301 ggsptnaiea ydaradrwvn vtceeespra yhgaaylkgy vyiiggfdsv dyfnsvkrfd
      361 pvkktwhqva pmhsrrcyvs vtvlsnfiya mggfdgyvrl ntaeryepet nqwtliapmh
      421 eqrsdasatt lygkvyicgg fngneclfta evyntesnqw tviapmrsrr sgigviayge
      481 hvyavggfdg anrlrsaeay spvantwrti ptmfnprsnf gievvddllf vvggfngftt
      541 tfnvecydek tdewydahdm siyrsalscc vvpglanvge yaarrdnftg lalrdevkys
      601 aststlpv
//
LOCUS       NP_062081                610 aa            linear   ROD 28-APR-2025
DEFINITION  menin [Rattus norvegicus].
ACCESSION   NP_062081
VERSION     NP_062081.1
DBSOURCE    REFSEQ: accession NM_019208.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Jiang,Z., Wan,S. and Xing,B.
  TITLE     Wild-type menin is rapidly degraded via the ubiquitin-proteasome
            pathway in a rat insulinoma cell line
  JOURNAL   Biosci Rep 39 (10) (2019)
   PUBMED   31652443
  REMARK    GeneRIF: Wild-type menin is rapidly degraded via the
            ubiquitin-proteasome pathway in a rat insulinoma cell line.
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Xing,B., Ma,J., Jiang,Z., Feng,Z., Ling,S., Szigety,K., Su,W.,
            Zhang,L., Jia,R., Sun,Y., Zhang,L., Kong,X., Ma,X. and Hua,X.
  TITLE     GLP-1 signaling suppresses menin's transcriptional block by
            phosphorylation in beta cells
  JOURNAL   J Cell Biol 218 (3), 855-870 (2019)
   PUBMED   30792230
  REMARK    GeneRIF: results have uncovered a previously unappreciated
            physiological link in which GLP-1 signaling suppresses menin
            function through phosphorylation-triggered and actin/myosin
            cytoskeletal protein-mediated derepression of gene transcription.
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Gillam,M.P., Nimbalkar,D., Sun,L., Christov,K., Ray,D., Kaldis,P.,
            Liu,X. and Kiyokawa,H.
  TITLE     MEN1 tumorigenesis in the pituitary and pancreatic islet requires
            Cdk4 but not Cdk2
  JOURNAL   Oncogene 34 (7), 932-938 (2015)
   PUBMED   24531709
  REMARK    GeneRIF: CDK4 is a critical downstream target of MEN1-dependent
            tumor suppression and is required for tumorigenic proliferation in
            the pituitary and pancreatic islet, whereas CDK2 is dispensable for
            tumorigenesis in these neuroendocrine cell types.
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Ouyang,M., Su,W., Xiao,L., Rao,J.N., Jiang,L., Li,Y., Turner,D.J.,
            Gorospe,M. and Wang,J.Y.
  TITLE     Modulation by miR-29b of intestinal epithelium homoeostasis through
            the repression of menin translation
  JOURNAL   Biochem J 465 (2), 315-323 (2015)
   PUBMED   25317587
  REMARK    GeneRIF: These findings indicate that miR-29b represses translation
            of Men1 mRNA, in turn affecting intestinal epithelial homoeostasis
            by altering IEC apoptosis.
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Vijayaraghavan,J., Maggi,E.C. and Crabtree,J.S.
  TITLE     miR-24 regulates menin in the endocrine pancreas
  JOURNAL   Am J Physiol Endocrinol Metab 307 (1), E84-E92 (2014)
   PUBMED   24824656
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Karges,W., Maier,S., Wissmann,A., Dralle,H., Dosch,H.M. and
            Boehm,B.O.
  TITLE     Primary structure, gene expression and chromosomal mapping of
            rodent homologs of the MEN1 tumor suppressor gene
  JOURNAL   Biochim Biophys Acta 1446 (3), 286-294 (1999)
   PUBMED   10524203
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Agarwal,S.K., Guru,S.C., Heppner,C., Erdos,M.R., Collins,R.M.,
            Park,S.Y., Saggar,S., Chandrasekharappa,S.C., Collins,F.S.,
            Spiegel,A.M., Marx,S.J. and Burns,A.L.
  TITLE     Menin interacts with the AP1 transcription factor JunD and
            represses JunD-activated transcription
  JOURNAL   Cell 96 (1), 143-152 (1999)
   PUBMED   9989505
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Stewart,C., Parente,F., Piehl,F., Farnebo,F., Quincey,D.,
            Silins,G., Bergman,L., Carle,G.F., Lemmens,I., Grimmond,S.,
            Xian,C.Z., Khodei,S., Teh,B.T., Lagercrantz,J., Siggers,P.,
            Calender,A., Van de Vem,V., Kas,K., Weber,G., Hayward,N.,
            Gaudray,P. and Larsson,C.
  TITLE     Characterization of the mouse Men1 gene and its expression during
            development
  JOURNAL   Oncogene 17 (19), 2485-2493 (1998)
   PUBMED   9824159
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Guru,S.C., Goldsmith,P.K., Burns,A.L., Marx,S.J., Spiegel,A.M.,
            Collins,F.S. and Chandrasekharappa,S.C.
  TITLE     Menin, the product of the MEN1 gene, is a nuclear protein
  JOURNAL   Proc Natl Acad Sci U S A 95 (4), 1630-1634 (1998)
   PUBMED   9465067
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Lemmens,I., Van de Ven,W.J., Kas,K., Zhang,C.X., Giraud,S.,
            Wautot,V., Buisson,N., De Witte,K., Salandre,J., Lenoir,G.,
            Pugeat,M., Calender,A., Parente,F., Quincey,D., Gaudray,P., De
            Wit,M.J., Lips,C.J., Hoppener,J.W., Khodaei,S., Grant,A.L.,
            Weber,G., Kytola,S., Teh,B.T., Farnebo,F., Thakker,R.V. et al.
  TITLE     Identification of the multiple endocrine neoplasia type 1 (MEN1)
            gene. The European Consortium on MEN1
  JOURNAL   Hum Mol Genet 6 (7), 1177-1183 (1997)
   PUBMED   9215690
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB773186.1, CB814296.1, AF130370.1, CV079282.1 and BQ193347.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023400.1, AF130369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..610
                     /product="menin"
                     /note="multiple endocrine neoplasia 1; multiple endocrine
                     neoplasia I; multiple endocrine neoplasia type I"
                     /calculated_mol_wt=67205
     Region          2..608
                     /region_name="Menin"
                     /note="pfam05053"
                     /db_xref="CDD:398642"
     Site            order(92,95..96,98..99,101..105)
                     /site_type="other"
                     /note="LEDGF interaction interface [polypeptide binding]"
                     /db_xref="CDD:271218"
     Site            order(136..138,153..155,178..181,238,241,244,246,278,282,
                     319,323,359,363)
                     /site_type="other"
                     /note="MLL1 binding site [polypeptide binding]"
                     /db_xref="CDD:271218"
     Region          214..390
                     /region_name="Interaction with FANCD2.
                     /evidence=ECO:0000250|UniProtKB:O00255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR8.1)"
     Region          460..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9WVR8.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR8.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR8.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O00255; propagated from
                     UniProtKB/Swiss-Prot (Q9WVR8.1)"
     CDS             1..610
                     /gene="Men1"
                     /gene_synonym="menin"
                     /coded_by="NM_019208.3:403..2235"
                     /db_xref="GeneID:29417"
                     /db_xref="RGD:3078"
ORIGIN      
        1 mglkaaqktl fplrsiddvv rlfaaelgre epdlvllslv lgfvehflav nrviptnvpe
       61 ltfqpspapd ppggltyfpv adlsiiaaly arftaqirga vdlslypreg gvssrelvkk
      121 vsdviwnsls rsyfkdrahi qslfsfitgt kldssgvafa vvgacqalgl rdvhlalsed
      181 hawvvfgsng eqtaevtwhg kgnedrrgqt vnagvaersw lylkgsymrc drkmevafmv
      241 cainpsidlh tdslellqlq qkllwllydl ghlerypmal gnladleele ptpgrpdplt
      301 lyhkgiasak tyyqdehiyp ymylagyhcr nrnvrealqa wadtatviqd ynycredeei
      361 ykeffevand vipnllkeaa slleageerp geqaqgtqgq gsalqdpecf ahllrfydgi
      421 ckweegsptp vlhvgwatfl vqslgrfegq vrqkvhivsr eaeaaeaeep wgdearegrr
      481 rgprreskpe eppppkkpal dkgpgsgqsa gsgpprktsg tvsgtargte vssaaqapap
      541 aaspppegpv ltfqsekmkg mkellvatki nssaiklqlt aqsqvqmkkq kvstpsdytl
      601 sflkrqrkgl
//
LOCUS       NP_036837                457 aa            linear   ROD 28-APR-2025
DEFINITION  T-cell surface glycoprotein CD4 precursor [Rattus norvegicus].
ACCESSION   NP_036837
VERSION     NP_036837.1
DBSOURCE    REFSEQ: accession NM_012705.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Reuter,S., Kentrup,D., Grabner,A., Kohler,G., Buscher,K. and
            Edemir,B.
  TITLE     C4d Deposition after Allogeneic Renal Transplantation in Rats Is
            Involved in Initial Apoptotic Cell Clearance
  JOURNAL   Cells 10 (12), 3499 (2021)
   PUBMED   34944007
  REMARK    GeneRIF: C4d Deposition after Allogeneic Renal Transplantation in
            Rats Is Involved in Initial Apoptotic Cell Clearance.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Li,S., Jiang,L., Li,X., Lin,F., Wang,Y., Li,B., Jiang,T., An,W.,
            Liu,S., Liu,H., Xu,P., Zhao,L., Zhang,L., Mu,J., Wang,H., Kang,J.,
            Li,Y., Huang,L., Zhu,C., Zhao,S., Lu,J., Ji,J. and Zhao,J.
  TITLE     Clinical and pathological investigation of patients with severe
            COVID-19
  JOURNAL   JCI Insight 5 (12), 138070 (2020)
   PUBMED   32427582
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yao,Z., Zheng,Z., Wu,K. and Junhua,Z.
  TITLE     Immune environment modulation in pneumonia patients caused by
            coronavirus: SARS-CoV, MERS-CoV and SARS-CoV-2
  JOURNAL   Aging (Albany NY) 12 (9), 7639-7651 (2020)
   PUBMED   32364527
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Wang,F.J., Cui,D. and Qian,W.D.
  TITLE     Therapeutic Effect of CD4+CD25+ Regulatory T Cells Amplified In
            Vitro on Experimental Autoimmune Neuritis in Rats
  JOURNAL   Cell Physiol Biochem 47 (1), 390-402 (2018)
   PUBMED   29772575
  REMARK    GeneRIF: Adoptive transfusion of CD4+CD25+ Regulatory T Cells into
            Experimental Autoimmune Neuritis model rats has significant
            therapeutic effects.
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Vuohelainen,V., Paavonen,T., Hamalainen,M., Moilanen,E. and
            Mennander,A.A.
  TITLE     C4d Deposition Reveals Myocardial Infarction After Cardiac
            Arrest--Experimental Study
  JOURNAL   Adv Clin Exp Med 24 (3), 393-399 (2015)
   PUBMED   26467126
  REMARK    GeneRIF: Increased C4d deposition may be amenable to identify early
            myocardial infarction after cardiac arrest.
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Ayliffe,W., Alam,Y., Bell,E.B., McLeod,D. and Hutchinson,I.V.
  TITLE     Prolongation of rat corneal graft survival by treatment with
            anti-CD4 monoclonal antibody
  JOURNAL   Br J Ophthalmol 76 (10), 602-606 (1992)
   PUBMED   1358194
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Seong,R.H., Chamberlain,J.W. and Parnes,J.R.
  TITLE     Signal for T-cell differentiation to a CD4 cell lineage is
            delivered by CD4 transmembrane region and/or cytoplasmic tail
  JOURNAL   Nature 356 (6371), 718-720 (1992)
   PUBMED   1533274
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Beyers,A.D., Spruyt,L.L. and Williams,A.F.
  TITLE     Molecular associations between the T-lymphocyte antigen receptor
            complex and the surface antigens CD2, CD4, or CD8 and CD5
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2945-2949 (1992)
   PUBMED   1372996
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Nabozny,G.H., Cobbold,S.P., Waldmann,H. and Kong,Y.C.
  TITLE     Suppression in murine experimental autoimmune thyroiditis: in vivo
            inhibition of CD4+ T cell-mediated resistance by a nondepleting rat
            CD4 monoclonal antibody
  JOURNAL   Cell Immunol 138 (1), 185-196 (1991)
   PUBMED   1680568
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Sayegh,M.H., Sablinski,T., Tanaka,K., Kut,J.P., Kwok,C.A.,
            Tilney,N.L., Kupiec-Weglinski,J.W. and Milford,E.L.
  TITLE     Effects of BWH-4 anti-CD4 monoclonal antibody on rat vascularized
            cardiac allografts before and after engraftment
  JOURNAL   Transplantation 51 (2), 296-299 (1991)
   PUBMED   1704648
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M15768.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M15768.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..457
                     /product="T-cell surface glycoprotein CD4 precursor"
                     /note="T-cell surface glycoprotein CD4; W3/25 antigen;
                     T-cell surface antigen T4/Leu-3; CD4 antigen"
                     /calculated_mol_wt=48372
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3084
     mat_peptide     28..457
                     /product="T-cell surface glycoprotein CD4"
                     /calculated_mol_wt=48372
     Region          28..124
                     /region_name="IgV_1_CD4"
                     /note="First immunoglobulin (Ig) domain of Cluster of
                     Differentiation (CD) 4; member of the V-set of IgSF
                     domains; cd07690"
                     /db_xref="CDD:409487"
     Region          28..44
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409487"
     Region          28..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409487"
     Site            order(30,32,34,103,106,123)
                     /site_type="other"
                     /note="interchain domain interface [polypeptide binding]"
                     /db_xref="CDD:409487"
     Region          37..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409487"
     Region          45..52
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409487"
     Region          52..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409487"
     Region          53..58
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409487"
     Region          60..74
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409487"
     Region          60..66
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409487"
     Site            order(70..73,75,87)
                     /site_type="other"
                     /note="MHC interface [polypeptide binding]"
                     /db_xref="CDD:409487"
     Region          70..74
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409487"
     Region          75..112
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409487"
     Region          81..85
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409487"
     Region          92..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409487"
     Region          106..113
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409487"
     Region          113..116
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409487"
     Region          116..124
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409487"
     Region          117..124
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409487"
     Region          127..206
                     /region_name="C2-set"
                     /note="Immunoglobulin C2-set domain; pfam05790"
                     /db_xref="CDD:399065"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409491"
     Region          155..159
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409491"
     Region          170..174
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409491"
     Region          184..189
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409491"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2113054; propagated from
                     UniProtKB/Swiss-Prot (P05540.1)"
     Region          197..200
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409491"
     Region          210..315
                     /region_name="CD4-extracel"
                     /note="CD4, extracellular; pfam09191"
                     /db_xref="CDD:462712"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2113054; propagated from
                     UniProtKB/Swiss-Prot (P05540.1)"
     Region          316..387
                     /region_name="C2-set"
                     /note="Immunoglobulin C2-set domain; pfam05790"
                     /db_xref="CDD:399065"
     Site            392
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05540.1)"
     Site            395..417
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05540.1)"
     Region          400..443
                     /region_name="CD4_CD"
                     /note="cytoplasmic domain of T-cell surface glycoprotein
                     CD4 and similar proteins; cd22570"
                     /db_xref="CDD:439337"
     Site            430..443
                     /site_type="other"
                     /note="NEF binding site [polypeptide binding]"
                     /db_xref="CDD:439337"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01730; propagated from
                     UniProtKB/Swiss-Prot (P05540.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01730; propagated from
                     UniProtKB/Swiss-Prot (P05540.1)"
     CDS             1..457
                     /gene="Cd4"
                     /gene_synonym="p55; W3/25"
                     /coded_by="NM_012705.1:54..1427"
                     /db_xref="GeneID:24932"
                     /db_xref="RGD:2306"
ORIGIN      
        1 mcrgfsfrhl lpllllqlsk llvvtqgktv vlgkeggsae lpcestsrrs asfawkssdq
       61 ktilgyknkl likgslelys rfdsrknawe rgsfpliink lrmedsqtyv celenkkeev
      121 elwvfrvtfn pgtrllqgqs ltlildsnpk vsdppieckh kssnivkdsk afsthslriq
      181 dsgiwnctvt lnqkkhsfdm klsvlgfast sitayksege saefsfplnl geeslqgelr
      241 wkaekapssq switfslknq kvsvqkstsn pkfqlsetlp ltlqipqvsl qfagsgnltl
      301 tldrgilyqe vnlvvmkvtq pdsntltcev mgptspkmrl ilkqenqear vsrqekviqv
      361 qapeagvwqc llsegeevkm dskiqvlskg lnqtmflavv lgsafsflvf tglcilfcvr
      421 crhqqrqaar msqikrllse kktcqcshrm qkshnli
//
LOCUS       NP_001003975             293 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein C6orf47 homolog [Rattus norvegicus].
ACCESSION   NP_001003975 XP_579112
VERSION     NP_001003975.1
DBSOURCE    REFSEQ: accession NM_001003975.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX883045.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579112.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM066921.1, BC101859.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06621351, SAMN16676806
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..293
                     /product="uncharacterized protein C6orf47 homolog"
                     /calculated_mol_wt=31694
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG51.1)"
     Region          16..264
                     /region_name="DUF4661"
                     /note="Domain of unknown function (DUF4661); pfam15576"
                     /db_xref="CDD:464770"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG51.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6MG51.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95873; propagated from
                     UniProtKB/Swiss-Prot (Q6MG51.1)"
     Region          268..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG51.1)"
     CDS             1..293
                     /gene="G4"
                     /coded_by="NM_001003975.3:427..1308"
                     /db_xref="GeneID:406868"
                     /db_xref="RGD:1303038"
ORIGIN      
        1 mflrrlggwl prpwgrkkst ktdlpapepr wvdsspensg sdwdsapetm gdvgplktkd
       61 sgtrrppqaa pessrdtrvy qlgskrmdsl kkdkaasaiq esarletgga vpkldldpvd
      121 sggmknlgvs pqgrlgttgp eallekpgrr qkllrwlrge pgapshylqd peeylqistn
      181 ltlhllella sallalcsrp lraildalgl rgpvglwlhg llcflaalhg lhavlsllta
      241 hplhfaclfg llqalvlavs lrepvedeet adwesegqgk eakeqtegpg ral
//
LOCUS       NP_001013938             228 aa            linear   ROD 28-APR-2025
DEFINITION  CD302 antigen precursor [Rattus norvegicus].
ACCESSION   NP_001013938 XP_215741
VERSION     NP_001013938.1
DBSOURCE    REFSEQ: accession NM_001013916.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Kato,M., Khan,S., d'Aniello,E., McDonald,K.J. and Hart,D.N.
  TITLE     The novel endocytic and phagocytic C-Type lectin receptor
            DCL-1/CD302 on macrophages is colocalized with F-actin, suggesting
            a role in cell adhesion and migration
  JOURNAL   J Immunol 179 (9), 6052-6063 (2007)
   PUBMED   17947679
  REMARK    GeneRIF: hDCL-1 is an unconventional lectin receptor that plays
            roles not only in endocytosis/phagocytosis but also in cell
            adhesion and migration
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC089829.1.
            
            On Apr 20, 2005 this sequence version replaced XP_215741.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089829.1, FQ218624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..228
                     /product="CD302 antigen precursor"
                     /note="type I transmembrane C-type lectin receptor DCL-1;
                     C-type lectin domain family 13 member A; CD302 antigen"
                     /calculated_mol_wt=23443
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2026
     mat_peptide     21..228
                     /product="CD302 antigen. /id=PRO_0000252334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVR3.1)"
                     /calculated_mol_wt=23443
     Region          22..151
                     /region_name="CLECT"
                     /note="C-type lectin (CTL) or carbohydrate-recognition
                     domain (CRD); smart00034"
                     /db_xref="CDD:214480"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5FVR3.1)"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FVR3.1)"
     CDS             1..228
                     /gene="Cd302"
                     /gene_synonym="RGD1307606"
                     /coded_by="NM_001013916.1:237..923"
                     /db_xref="GeneID:295629"
                     /db_xref="RGD:1307606"
ORIGIN      
        1 mphaalsslv llslataifa dcpssiwvqf qgscytflqv tinveniedv rkqctdhgad
       61 lvsihneeen afildtlqkr wkgpddlllg mfydtddasf kwfdqsnmtf dkwadedged
      121 lvdtcgflya ktgewrkgnc emssvtgtlc ktaipydkky lsdnhilist lviastvtla
      181 vlgaviwfly rrsarsgfts fspapqspys dgcalvvsee deysvqld
//
LOCUS       NP_058995                512 aa            linear   ROD 28-APR-2025
DEFINITION  reduced folate transporter [Rattus norvegicus].
ACCESSION   NP_058995 XP_346601
VERSION     NP_058995.2
DBSOURCE    REFSEQ: accession NM_017299.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Zhang,S.S., Wu,Y.J., Pan,S., Wang,Q.H., Chen,W.G., Wang,Z.F.,
            Xu,J.Y., Zuo,J. and Yin,Q.
  TITLE     Xanthones from securidaca inappendiculata antagonizes the
            anti-rheumatic effect of methotrexate by inhibiting reduced folate
            carrier 1
  JOURNAL   Immunopharmacol Immunotoxicol 45 (1), 16-25 (2023)
   PUBMED   35850595
  REMARK    GeneRIF: Xanthones from securidaca inappendiculata antagonizes the
            anti-rheumatic effect of methotrexate by inhibiting reduced folate
            carrier 1.
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Radziejewska,A., Suliburska,J., Kolodziejski,P. and Chmurzynska,A.
  TITLE     Role of Slc19a1 and Tfr2 in liver transport of iron and folate: A
            rat model of folate/iron deficiency followed by supplementation
  JOURNAL   J Trace Elem Med Biol 62, 126568 (2020)
   PUBMED   32521439
  REMARK    GeneRIF: Role of Slc19a1 and Tfr2 in liver transport of iron and
            folate: A rat model of folate/iron deficiency followed by
            supplementation.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Luteijn,R.D., Zaver,S.A., Gowen,B.G., Wyman,S.K., Garelis,N.E.,
            Onia,L., McWhirter,S.M., Katibah,G.E., Corn,J.E., Woodward,J.J. and
            Raulet,D.H.
  TITLE     SLC19A1 transports immunoreactive cyclic dinucleotides
  JOURNAL   Nature 573 (7774), 434-438 (2019)
   PUBMED   31511694
  REMARK    Erratum:[Nature. 2020 Mar;579(7800):E12. doi:
            10.1038/s41586-020-2064-8. PMID: 32144410]
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Ritchie,C., Cordova,A.F., Hess,G.T., Bassik,M.C. and Li,L.
  TITLE     SLC19A1 Is an Importer of the Immunotransmitter cGAMP
  JOURNAL   Mol Cell 75 (2), 372-381 (2019)
   PUBMED   31126740
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Alam,C., Hoque,M.T., Finnell,R.H., Goldman,I.D. and Bendayan,R.
  TITLE     Regulation of Reduced Folate Carrier (RFC) by Vitamin D Receptor at
            the Blood-Brain Barrier
  JOURNAL   Mol Pharm 14 (11), 3848-3858 (2017)
   PUBMED   28885847
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Rajgopal,A., Sierra,E.E., Zhao,R. and Goldman,I.D.
  TITLE     Expression of the reduced folate carrier SLC19A1 in IEC-6 cells
            results in two distinct transport activities
  JOURNAL   Am J Physiol Cell Physiol 281 (5), C1579-C1586 (2001)
   PUBMED   11600421
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Chancy,C.D., Kekuda,R., Huang,W., Prasad,P.D., Kuhnel,J.M.,
            Sirotnak,F.M., Roon,P., Ganapathy,V. and Smith,S.B.
  TITLE     Expression and differential polarization of the reduced-folate
            transporter-1 and the folate receptor alpha in mammalian retinal
            pigment epithelium
  JOURNAL   J Biol Chem 275 (27), 20676-20684 (2000)
   PUBMED   10787414
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Honscha,W., Dotsch,K.U., Thomsen,N. and Petzinger,E.
  TITLE     Cloning and functional characterization of the bile acid-sensitive
            methotrexate carrier from rat liver cells
  JOURNAL   Hepatology 31 (6), 1296-1304 (2000)
   PUBMED   10827155
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Tse,A., Brigle,K., Taylor,S.M. and Moran,R.G.
  TITLE     Mutations in the reduced folate carrier gene which confer dominant
            resistance to 5,10-dideazatetrahydrofolate
  JOURNAL   J Biol Chem 273 (40), 25953-25960 (1998)
   PUBMED   9748272
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Chiao,J.H., Roy,K., Tolner,B., Yang,C.H. and Sirotnak,F.M.
  TITLE     RFC-1 gene expression regulates folate absorption in mouse small
            intestine
  JOURNAL   J Biol Chem 272 (17), 11165-11170 (1997)
   PUBMED   9111015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF099009.1 and BC085742.1.
            
            On Mar 31, 2009 this sequence version replaced NP_058995.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF099009.1, U38180.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN16676806 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..512
                     /product="reduced folate transporter"
                     /note="methotrexate carrier 1; folate transporter 1;
                     methotrexate carrier 6; methotrexate carrier 5;
                     methotrexate carrier 2; RFC-1; reduced folate carrier 1;
                     RFC1; solute carrier family 19 (folate transporter),
                     member 1; solute carrier family 19 (sodium/hydrogen
                     exchanger), member 1; plasma membrane folate antiporter
                     SLC19A1"
                     /calculated_mol_wt=57978
     Region          1..512
                     /region_name="rfc"
                     /note="RFC reduced folate carrier; TIGR00806"
                     /db_xref="CDD:129888"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P41440; propagated from
                     UniProtKB/Swiss-Prot (Q62866.2)"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62866.2)"
     Site            63..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            115..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            152..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            182..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            267..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            301..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            354..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            392..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Region          400..412
                     /region_name="Required for substrate-binding.
                     /evidence=ECO:0000250|UniProtKB:P41440"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            424..448
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41438; propagated from
                     UniProtKB/Swiss-Prot (Q62866.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41438; propagated from
                     UniProtKB/Swiss-Prot (Q62866.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41438; propagated from
                     UniProtKB/Swiss-Prot (Q62866.2)"
     Region          479..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62866.2)"
     CDS             1..512
                     /gene="Slc19a1"
                     /gene_synonym="MTX-1; MTX1"
                     /coded_by="NM_017299.2:249..1787"
                     /db_xref="GeneID:29723"
                     /db_xref="RGD:3695"
ORIGIN      
        1 mvptgqvaek qaceeprqdr elkswrwlvf ylcffgfmaq lrpgesfitp yllernftke
       61 qvtneiipml pyshlavlvp iflltdylry kpvlvlqcls fvcvwlllll gtsvvhmqlm
      121 evfysitmaa riayssyifs lvqpsryqrm asysraavll gvfissvlgq vlvtlggist
      181 ymlncislgf ilfslslslf lkrpkrslff nrsalvqgal pceldqmhpg pgrpeprkle
      241 rmlgtcrdsf lvrmlselvk nvrqpqlrlw clwwvfnsag yylityyvhv lwkitdsrln
      301 yngavdaast llsaitafta gfvnirwalw sklviasvia iqaglvfcmf qipdiwvcyv
      361 tfvlfrgayq flvpiatfqi asslskelca lvfgintfla talktsitlv vsdkrglglq
      421 vhqqfriyfm yfltlsiicl awagldglry yrrgrhqpla qaqalspled svqaislqdg
      481 dlrrpqpsap qllpedgsve dgradlrvea ka
//
LOCUS       NP_001019525             493 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing protein 14 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_001019525 XP_576302
VERSION     NP_001019525.1
DBSOURCE    REFSEQ: accession NM_001024354.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Wu,C., Yang,Y., Ou,J., Zhu,L., Zhao,W. and Cui,J.
  TITLE     LRRC14 attenuates Toll-like receptor-mediated NF-kappaB signaling
            through disruption of IKK complex
  JOURNAL   Exp Cell Res 347 (1), 65-73 (2016)
   PUBMED   27426725
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC092583.1.
            
            On May 27, 2005 this sequence version replaced XP_576302.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092583.1, SRR8487230.8487.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132265, SAMD00132267
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..493
                     /product="leucine-rich repeat-containing protein 14
                     isoform 2"
                     /note="leucine-rich repeat-containing protein 14"
                     /calculated_mol_wt=54784
     Region          111..146
                     /region_name="LRR 1, degenerate.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          194..218
                     /region_name="LRR 2, degenerate.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          219..246
                     /region_name="LRR 3, degenerate.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          <222..>427
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          247..282
                     /region_name="LRR 4, degenerate.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          283..307
                     /region_name="LRR 5.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          286..309
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          308..339
                     /region_name="LRR 6.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          311..337
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          338..361
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          340..360
                     /region_name="LRR 7.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          364..391
                     /region_name="LRR 8.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          367..394
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          392..416
                     /region_name="LRR 9.
                     /evidence=ECO:0000250|UniProtKB:Q3UWY1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569B5.1)"
     Region          395..406
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     CDS             1..493
                     /gene="Lrrc14"
                     /coded_by="NM_001024354.1:174..1655"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:500900"
                     /db_xref="RGD:1560202"
ORIGIN      
        1 mhtlvflstr qvlqcqpaac qalpllprel fpllfkvafm dkktavlrel vhtwpfplls
       61 fqqllqecah csrallqerl stesmqavil gltarihare aeagtqpvcr khtlrvldmt
      121 gllddgveqd pgtmsmwdct aavartciaq qqvgtakpgl spvpveirvd lrvnrasytf
      181 lrealqssvd sllrlccrdl raedlpmrnt vallqlldag clrridlrfn nlglrglsvi
      241 iphvarfqhl aslrlhyvhg dsrqpsvdge dnfryflaqm grficlrels igssllsgrl
      301 dqllstlqrp leslelafca llpedlrfla qsshaahlkk ldlsgndlsg nqltpfqgll
      361 qavaatllhl eltecqiada qllatlptlt rcaslrylgl ygnplsmagl kellrdsviq
      421 aelrtvvhpf pvdcyeglpw pppasvllea sineekfarv eaelhqllla sgrahvlwtt
      481 diygrlaady fnl
//
LOCUS       NP_001001516            1357 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 19 [Rattus norvegicus].
ACCESSION   NP_001001516 XP_341472 XP_341473
VERSION     NP_001001516.1
DBSOURCE    REFSEQ: accession NM_001001516.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1357)
  AUTHORS   Miao,R., Lu,Y., He,X., Liu,X., Chen,Z. and Wang,J.
  TITLE     Ubiquitin-specific protease 19 blunts pathological cardiac
            hypertrophy via inhibition of the TAK1-dependent pathway
  JOURNAL   J Cell Mol Med 24 (18), 10946-10957 (2020)
   PUBMED   32798288
  REMARK    GeneRIF: Ubiquitin-specific protease 19 blunts pathological cardiac
            hypertrophy via inhibition of the TAK1-dependent pathway.
REFERENCE   2  (residues 1 to 1357)
  AUTHORS   Zhang,X., Jiang,Y., Han,W., Liu,A., Xie,X., Han,C., Fan,C.,
            Wang,H., Zhang,H., Ding,S., Shan,Z. and Teng,W.
  TITLE     Effect of Prolonged Iodine Overdose on Type 2 Iodothyronine
            Deiodinase Ubiquitination-Related Enzymes in the Rat Pituitary
  JOURNAL   Biol Trace Elem Res 174 (2), 377-386 (2016)
   PUBMED   27156111
  REMARK    GeneRIF: High iodine intake had no discernible effects on USP20.
            Temporary increases in USP33 and USP19 mRNA levels were observed.
            The enzymes related to D2 ubiquitination change with prolonged high
            iodine intake. Increased D2 ubiquitination suppresses the activity
            of D2, causing a decrease in negative feedback of the
            hypothalamic-pituitary-thyroid axis.
REFERENCE   3  (residues 1 to 1357)
  AUTHORS   Wiles,B., Miao,M., Coyne,E., Larose,L., Cybulsky,A.V. and Wing,S.S.
  TITLE     USP19 deubiquitinating enzyme inhibits muscle cell differentiation
            by suppressing unfolded-protein response signaling
  JOURNAL   Mol Biol Cell 26 (5), 913-923 (2015)
   PUBMED   25568336
  REMARK    GeneRIF: Deubiquitination by USP19 does modulate muscle cell
            differentiation and that this function requires the ER-localized
            isoform and appears to act through regulation of the
            unfolded-protein response (UPR) signaling.
REFERENCE   4  (residues 1 to 1357)
  AUTHORS   Nakamura,N., Harada,K., Kato,M. and Hirose,S.
  TITLE     Ubiquitin-specific protease 19 regulates the stability of the E3
            ubiquitin ligase MARCH6
  JOURNAL   Exp Cell Res 328 (1), 207-216 (2014)
   PUBMED   25088257
REFERENCE   5  (residues 1 to 1357)
  AUTHORS   Lee,J.G., Kim,W., Gygi,S. and Ye,Y.
  TITLE     Characterization of the deubiquitinating activity of USP19 and its
            role in endoplasmic reticulum-associated degradation
  JOURNAL   J Biol Chem 289 (6), 3510-3517 (2014)
   PUBMED   24356957
REFERENCE   6  (residues 1 to 1357)
  AUTHORS   Ogawa,M., Yamaji,R., Higashimura,Y., Harada,N., Ashida,H.,
            Nakano,Y. and Inui,H.
  TITLE     17beta-estradiol represses myogenic differentiation by increasing
            ubiquitin-specific peptidase 19 through estrogen receptor alpha
  JOURNAL   J Biol Chem 286 (48), 41455-41465 (2011)
   PUBMED   21971047
REFERENCE   7  (residues 1 to 1357)
  AUTHORS   Sundaram,P., Pang,Z., Miao,M., Yu,L. and Wing,S.S.
  TITLE     USP19-deubiquitinating enzyme regulates levels of major
            myofibrillar proteins in L6 muscle cells
  JOURNAL   Am J Physiol Endocrinol Metab 297 (6), E1283-E1290 (2009)
   PUBMED   19773579
  REMARK    GeneRIF: USP19 modulates transcription of major myofibrillar
            proteins.
REFERENCE   8  (residues 1 to 1357)
  AUTHORS   Hassink,G.C., Zhao,B., Sompallae,R., Altun,M., Gastaldello,S.,
            Zinin,N.V., Masucci,M.G. and Lindsten,K.
  TITLE     The ER-resident ubiquitin-specific protease 19 participates in the
            UPR and rescues ERAD substrates
  JOURNAL   EMBO Rep 10 (7), 755-761 (2009)
   PUBMED   19465887
REFERENCE   9  (residues 1 to 1357)
  AUTHORS   Lu,Y., Adegoke,O.A., Nepveu,A., Nakayama,K.I., Bedard,N., Cheng,D.,
            Peng,J. and Wing,S.S.
  TITLE     USP19 deubiquitinating enzyme supports cell proliferation by
            stabilizing KPC1, a ubiquitin ligase for p27Kip1
  JOURNAL   Mol Cell Biol 29 (2), 547-558 (2009)
   PUBMED   19015242
  REMARK    GeneRIF: study reports that the USP19 deubiquitinating enzyme
            interacts with and stabilizes KPC1, thereby modulating p27(Kip1)
            levels and cell proliferation
            Erratum:[Mol Cell Biol. 2009 Jun;29(11):3241]
REFERENCE   10 (residues 1 to 1357)
  AUTHORS   Combaret,L., Adegoke,O.A., Bedard,N., Baracos,V., Attaix,D. and
            Wing,S.S.
  TITLE     USP19 is a ubiquitin-specific protease regulated in rat skeletal
            muscle during catabolic states
  JOURNAL   Am J Physiol Endocrinol Metab 288 (4), E693-E700 (2005)
   PUBMED   15562254
  REMARK    GeneRIF: USP19 is regulated in rat skeletal muscle during catabolic
            states.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY605065.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_341472.1, XP_341473.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY605065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132262, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1357
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..1357
                     /product="ubiquitin carboxyl-terminal hydrolase 19"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 19; ubiquitin
                     thiolesterase 19; ubiquitin thioesterase 19;
                     deubiquitinating enzyme 19; ubiquitin-specific-processing
                     protease 19"
                     /calculated_mol_wt=150172
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          58..140
                     /region_name="p23_like"
                     /note="Proteins containing this p23_like domain include
                     p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1.
                     Both are co-chaperones for the heat shock protein (Hsp)
                     90. p23 binds Hsp90 and participates in the folding of a
                     number of Hsp90 clients, including...; cd06463"
                     /db_xref="CDD:107220"
     Region          162..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJD6; propagated from
                     UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          275..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          327..423
                     /region_name="p23_CS_SGT1_like"
                     /note="p23_like domain similar to the C-terminal
                     CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of
                     Skp1). Sgt1 interacts with multiple protein complexes and
                     has the features of a cochaperone. Human (h) Sgt1
                     interacts with both Hsp70 and Hsp90, and has...; cd06466"
                     /db_xref="CDD:107223"
     Region          414..534
                     /region_name="USP19_linker"
                     /note="Linker region of USP19 deubiquitinase; pfam16602"
                     /db_xref="CDD:465191"
     Region          432..479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          <532..1254
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Region          962..981
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          1259..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Region          1292..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     Site            1331..1351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6J1Y9.1)"
     CDS             1..1357
                     /gene="Usp19"
                     /coded_by="NM_001001516.2:1..4074"
                     /db_xref="GeneID:361190"
                     /db_xref="RGD:1303276"
ORIGIN      
        1 msagtsatgp rrgppgleea tskkkqkdra nqeskdgdpr rvsmprkept kdellldwrq
       61 ssdkvvvklr vgtgpiclee vdaaftdtdc vvrlpdgrqw ggvffakiqs sctkvqtrkg
      121 gllqlalpkk vplltwpsll kkplgtqelv pglrcqengq elspialepg seprrakqea
      181 rnqkraqgrg evgsgaspga qagpsakrav hlcrgpegeg smdgpgpqgd apsflsdsat
      241 qveaeeqlhv ppvnpqtsll gseknlallt vektvsprsd svspvmirnr dpekddhfke
      301 emavgadpaa ladepesmvn lafvkndsye kgpdsvvvhv yvkesrrdts rvlfreqdft
      361 lifqtrdgnf lrlhpgcgph tifrwqvklr nliepeqctf cftasridic lrkrqsqrwg
      421 gleapatrvg gakvavptgp tpldstppgg gplpltgqee aravekekpk arsedsgldg
      481 vvartplehv tpkpephlas pkptcmvppm phspvsgdsv eedeeeekkv clpgftglvn
      541 lgntcfmnsv iqslsntrel rdffhdrsfe aeinynnplg tggrlaigfa vllralwkgt
      601 hqafqpsklk aivaskasqf tgyaqhdaqe fmaflldglh edlnriqnkp ytetvdsdgr
      661 pdevvaeeaw qrhkmrndsf ivdlfqgqyk sklvcpvcak vsitfdpfly lpvplpqkqk
      721 vlpiyyfare phskpikflv svskenssas evleslsqsv hvkpeslrla eviknrfhrv
      781 flpshsldav sptdvllcfe llspelaker vvvlevqqrp qvpsipiskc aacqrkqqse
      841 deklkrctrc yrvgycnqfc qkthwpdhkg lcrpenigyp flvsvpasrl tyarlaqlle
      901 gyarysvsvf qppfqpgrma lesqspgctt llstssleag dserepiqps elqlvtpvae
      961 gdtgahrmwp padrgpvpst sgissemlas gpmegcslla gervsrpeaa vpgyqhsres
     1021 vsahtpqffi ykidassreq rledkgdtpl elgddcslal vwrnnerlqe fvlvaskele
     1081 caedpgsage aaraghftld qclnlftrpe vlapeeawyc pqckqhreas kqlllwrlpn
     1141 vlivqlkrfs frsfiwrdki ndlvefpvrn ldlskfcigq keeqlpsydl yavinhyggm
     1201 igghytacar lpsdrssqrs dvgwrlfdds tvttvdesqv vtryayvlfy rrrnspverp
     1261 praahaehhp dlgpaaeaaa sqasriwqel eaeeemvpeg pgplgpwgpq dwvgppprgp
     1321 ttsdegclry fvlgtvaalv alvlnvfypl vsqsrwr
//
LOCUS       NP_071599                390 aa            linear   ROD 28-APR-2025
DEFINITION  calcium-binding and spermatid-specific protein 1 [Rattus
            norvegicus].
ACCESSION   NP_071599 XP_341197
VERSION     NP_071599.2
DBSOURCE    REFSEQ: accession NM_022263.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   St Laurent,C.D., St Laurent,K.E., Mathison,R.D. and Befus,A.D.
  TITLE     Calcium-binding protein, spermatid-specific 1 is expressed in human
            salivary glands and contains an anti-inflammatory motif
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 308 (7), R569-R575 (2015)
   PUBMED   25632019
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Calvel,P., Kervarrec,C., Lavigne,R., Vallet-Erdtmann,V.,
            Guerrois,M., Rolland,A.D., Chalmel,F., Jegou,B. and Pineau,C.
  TITLE     CLPH, a novel casein kinase 2-phosphorylated disordered protein, is
            specifically associated with postmeiotic germ cells in rat
            spermatogenesis
  JOURNAL   J Proteome Res 8 (6), 2953-2965 (2009)
   PUBMED   19271754
  REMARK    GeneRIF: Identified CLPH (for Casein-Like PHosphoprotein), a new
            testis-specific protein expressed exclusively in postmeiotic germ
            cells.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Kawashima,A., Osman,B.A., Takashima,M., Kikuchi,A., Kohchi,S.,
            Satoh,E., Tamba,M., Matsuda,M. and Okamura,N.
  TITLE     CABS1 is a novel calcium-binding protein specifically expressed in
            elongate spermatids of mice
  JOURNAL   Biol Reprod 80 (6), 1293-1304 (2009)
   PUBMED   19208547
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079062.1.
            
            On or before Jan 21, 2005 this sequence version replaced
            XP_341197.1, NP_071599.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079062.1, AF271155.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: PMID: 19271754
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p22"
     Protein         1..390
                     /product="calcium-binding and spermatid-specific protein
                     1"
                     /note="RSD-6; casein-like phosphoprotein; calcium-binding
                     protein, spermatid-specific 1"
                     /calculated_mol_wt=42125
     Region          1..390
                     /region_name="CABS1"
                     /note="Calcium-binding and spermatid-specific protein 1;
                     pfam15367"
                     /db_xref="CDD:464677"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX6.1)"
     Region          82..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX6.1)"
     Region          146..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK2.
                     /evidence=ECO:0000269|PubMed:19271754,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Region          330..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FX6.1)"
     CDS             1..390
                     /gene="Cabs1"
                     /gene_synonym="Clph; Rsd6"
                     /coded_by="NM_022263.2:30..1202"
                     /db_xref="GeneID:64029"
                     /db_xref="RGD:620592"
ORIGIN      
        1 maedgspkiy srpprdsskt pteadiffga dntipksett itsegdhits vndctadgdf
       61 sttvnkltpt keklkleedi easlksttlp ekeittptet tnskpkesit enfipvkign
      121 isspvgtvsl idfssnmake dillatidae dkevkpttel setqedssan dedtsvppde
      181 ntetdvssst ssdvpddgav qvtdsfspes dvppstekev ttipdnvaed kvtkidlivs
      241 edrpktvtkl sdseeekfit vfeltnsaek akdnpedplt deepadgvnt wvekdaanea
      301 eshavlltav esrydfvvta setnsvvvee phvdtknspe kdaaesvtnv teefpsvtsv
      361 veqsgnkedl stndsgifkl lkeepdelmm
//
LOCUS       NP_001274041             170 aa            linear   ROD 28-APR-2025
DEFINITION  vascular endothelial growth factor A isoform 10 precursor [Rattus
            norvegicus].
ACCESSION   NP_001274041
VERSION     NP_001274041.1
DBSOURCE    REFSEQ: accession NM_001287112.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Fu,W., Ye,Y. and Hu,F.
  TITLE     LncRNA XIST promotes neovascularization in diabetic retinopathy by
            regulating miR-101-3p/VEGFA
  JOURNAL   Arch Endocrinol Metab 68, e230097 (2024)
   PUBMED   38739522
  REMARK    GeneRIF: LncRNA XIST promotes neovascularization in diabetic
            retinopathy by regulating miR-101-3p/VEGFA.
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Li,Z., Xie,L., Zou,L., Xiao,S. and Tao,J.
  TITLE     Overexpression of RAD54L attenuates osteoarthritis by suppressing
            the HIF-1alpha/VEGF signaling pathway: Bioinformatics analysis and
            experimental validation
  JOURNAL   PLoS One 19 (4), e0298575 (2024)
   PUBMED   38593124
  REMARK    GeneRIF: Overexpression of RAD54L attenuates osteoarthritis by
            suppressing the HIF-1alpha/VEGF signaling pathway: Bioinformatics
            analysis and experimental validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Bastide,A., Karaa,Z., Bornes,S., Hieblot,C., Lacazette,E., Prats,H.
            and Touriol,C.
  TITLE     An upstream open reading frame within an IRES controls expression
            of a specific VEGF-A isoform
  JOURNAL   Nucleic Acids Res 36 (7), 2434-2445 (2008)
   PUBMED   18304943
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Meiron,M., Anunu,R., Scheinman,E.J., Hashmueli,S. and Levi,B.Z.
  TITLE     New isoforms of VEGF are translated from alternative initiation CUG
            codons located in its 5'UTR
  JOURNAL   Biochem Biophys Res Commun 282 (4), 1053-1060 (2001)
   PUBMED   11352659
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Terman,B.I., Dougher-Vermazen,M., Carrion,M.E., Dimitrov,D.,
            Armellino,D.C., Gospodarowicz,D. and Bohlen,P.
  TITLE     Identification of the KDR tyrosine kinase as a receptor for
            vascular endothelial cell growth factor
  JOURNAL   Biochem Biophys Res Commun 187 (3), 1579-1586 (1992)
   PUBMED   1417831
REFERENCE   9  (residues 1 to 170)
  AUTHORS   de Vries,C., Escobedo,J.A., Ueno,H., Houck,K., Ferrara,N. and
            Williams,L.T.
  TITLE     The fms-like tyrosine kinase, a receptor for vascular endothelial
            growth factor
  JOURNAL   Science 255 (5047), 989-991 (1992)
   PUBMED   1312256
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Breier,G., Albrecht,U., Sterrer,S. and Risau,W.
  TITLE     Expression of vascular endothelial growth factor during embryonic
            angiogenesis and endothelial cell differentiation
  JOURNAL   Development 114 (2), 521-532 (1992)
   PUBMED   1592003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO565920.1, BC168708.1,
            AF222779.1 and JAXUCZ010000009.1.
            
            Summary: This gene is a member of the PDGF/VEGF growth factor
            family. It encodes a heparin-binding protein, which exists as a
            disulfide-linked homodimer. This growth factor induces
            proliferation and migration of vascular endothelial cells, and is
            essential for both physiological and pathological angiogenesis.
            Disruption of this gene in mice resulted in abnormal embryonic
            blood vessel formation. This gene is upregulated in many known
            tumors and its expression is correlated with tumor stage and
            progression. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. There is also
            evidence for alternative translation initiation from upstream
            non-AUG (CUG) codons resulting in additional isoforms. A recent
            study showed that a C-terminally extended isoform is produced by
            use of an alternative in-frame translation termination codon via a
            stop codon readthrough mechanism, and that this isoform is
            antiangiogenic. Expression of some isoforms derived from the AUG
            start codon is regulated by a small upstream open reading frame,
            which is located within an internal ribosome entry site. [provided
            by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (6) lacks an in-frame, internal
            exon in the 3' coding region, compared to variant 1. This variant
            can initiate translation from non-AUG (CUG) site, and also from a
            downstream, in-frame AUG site. The isoform (10) represented in this
            RefSeq is derived from the AUG start codon and it is shorter at the
            N-terminus and lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR21887622.3313572.1,
                                           SRR21887620.1146399.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760400
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 18304943
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..170
                     /product="vascular endothelial growth factor A isoform 10
                     precursor"
                     /note="vascular permeability factor"
                     /calculated_mol_wt=16857
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3180
     mat_peptide     27..170
                     /product="vascular endothelial growth factor A isoform 10"
                     /calculated_mol_wt=16857
     Region          49..131
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(49..52,86,88..91,106..109)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(51,82,86,93,127,129)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(76,85)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P16612.2)"
     Region          131..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16612.2)"
     CDS             1..170
                     /gene="Vegfa"
                     /gene_synonym="Vegf; VEGF-A; VEGF111; VEGF164; VPF"
                     /coded_by="NM_001287112.1:1015..1527"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:83785"
                     /db_xref="RGD:619991"
ORIGIN      
        1 mnfllswvhw tlalllylhh akwsqaaptt egeqkahevv kfmdvyqrsy crpietlvdi
       61 fqeypdeiey ifkpscvplm rcagccndea lecvptsesn vtmqimrikp hqsqhigems
      121 flqhsrcecr pkkdrtkpek ksvrgkgkgq krkrkksrfk swsvcdkprr
//
LOCUS       NP_001258913             277 aa            linear   ROD 28-APR-2025
DEFINITION  caspase-6 [Rattus norvegicus].
ACCESSION   NP_001258913
VERSION     NP_001258913.1
DBSOURCE    REFSEQ: accession NM_001271984.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wang,C., Li,Q., Jia,Z., Zhang,H., Li,Y., Zhao,Q., Su,L., Yu,Y. and
            Xu,R.
  TITLE     Spinal caspase-6 contributes to remifentanil-induced hyperalgesia
            via regulating CCL21/CXCR3 pathway in rats
  JOURNAL   Neurosci Lett 721, 134802 (2020)
   PUBMED   32014515
  REMARK    GeneRIF: Spinal caspase-6 contributes to remifentanil-induced
            hyperalgesia via regulating CCL21/CXCR3 pathway in rats.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Nie,Z.Y., Yao,M., Yang,Z., Yang,L., Liu,X.J., Yu,J., Ma,Y.,
            Zhang,N., Zhang,X.Y., Liu,M.H., Jiang,L.L. and Luo,J.M.
  TITLE     De-regulated STAT5A/miR-202-5p/USP15/Caspase-6 regulatory axis
            suppresses CML cell apoptosis and contributes to Imatinib
            resistance
  JOURNAL   J Exp Clin Cancer Res 39 (1), 17 (2020)
   PUBMED   31952546
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Woo,V., Cheng,C., Duraikannu,A., Chandrasekhar,A., Purdy,K.,
            Martinez,J.A. and Zochodne,D.W.
  TITLE     Caspase-6 is a Dispensable Enabler of Adult Mammalian Axonal
            Degeneration
  JOURNAL   Neuroscience 371, 242-253 (2018)
   PUBMED   29229552
  REMARK    GeneRIF: To evaluate an axon autonomous role of Casp6, study
            examined axon integrity following transection ex vivo, and analyzed
            the serial morphological fragmentation of neurofilament expression
            as a structural index of axonal degeneration. Adding a specific
            Casp6 inhibitor to the preparation delayed neurofilament
            fragmentation.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Wei,Y., Zheng,D., Guo,X., Zhao,M., Gao,L. and Bai,L.
  TITLE     Transient Receptor Potential Channel, Vanilloid 5, Induces
            Chondrocyte Apoptosis in a Rat Osteoarthritis Model Through the
            Mediation of Ca2+ Influx
  JOURNAL   Cell Physiol Biochem 46 (2), 687-698 (2018)
   PUBMED   29621761
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Harrison,D.C., Davis,R.P., Bond,B.C., Campbell,C.A., James,M.F.,
            Parsons,A.A. and Philpott,K.L.
  TITLE     Caspase mRNA expression in a rat model of focal cerebral ischemia
  JOURNAL   Brain Res Mol Brain Res 89 (1-2), 133-146 (2001)
   PUBMED   11311984
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Guo,R.F., Huber-Lang,M., Wang,X., Sarma,V., Padgaonkar,V.A.,
            Craig,R.A., Riedemann,N.C., McClintock,S.D., Hlaing,T., Shi,M.M.
            and Ward,P.A.
  TITLE     Protective effects of anti-C5a in sepsis-induced thymocyte
            apoptosis
  JOURNAL   J Clin Invest 106 (10), 1271-1280 (2000)
   PUBMED   11086028
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Ferrer,I.
  TITLE     Role of caspases in ionizing radiation-induced apoptosis in the
            developing cerebellum
  JOURNAL   J Neurobiol 41 (4), 549-558 (1999)
   PUBMED   10590178
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Vakkala,M., Paakko,P. and Soini,Y.
  TITLE     Expression of caspases 3, 6 and 8 is increased in parallel with
            apoptosis and histological aggressiveness of the breast lesion
  JOURNAL   Br J Cancer 81 (4), 592-599 (1999)
   PUBMED   10574243
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Kaushal,G.P., Singh,A.B. and Shah,S.V.
  TITLE     Identification of gene family of caspases in rat kidney and altered
            expression in ischemia-reperfusion injury
  JOURNAL   Am J Physiol 274 (3), F587-F595 (1998)
   PUBMED   9530276
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM068086.1, DY310578.1 and BC078785.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY310578.1, SRR8487227.327647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132294
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q43"
     Protein         1..277
                     /product="caspase-6"
                     /EC_number="3.4.22.59"
                     /note="CASP-6; apoptotic protease Mch-2"
                     /calculated_mol_wt=31443
     Region          20..273
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; smart00115"
                     /db_xref="CDD:214521"
     Region          25..27
                     /region_name="Tri-arginine exosite.
                     /evidence=ECO:0000250|UniProtKB:P55212"
                     /note="propagated from UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(47,105,144,151,200..205,209..210)
                     /site_type="other"
                     /note="substrate pocket [chemical binding]"
                     /db_xref="CDD:237997"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08738; propagated from
                     UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(104,146)
                     /site_type="active"
                     /db_xref="CDD:237997"
     Region          108..125
                     /region_name="130's region.
                     /evidence=ECO:0000250|UniProtKB:P55212"
                     /note="propagated from UniProtKB/Swiss-Prot (O35397.2)"
     Site            order(152,185..186,193,196,199,222,230,236,256,261..262,
                     264,267..268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:237997"
     Site            order(153,184)
                     /site_type="active"
                     /note="proteolytic cleavage site [active]"
                     /db_xref="CDD:237997"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55212; propagated from
                     UniProtKB/Swiss-Prot (O35397.2)"
     CDS             1..277
                     /gene="Casp6"
                     /gene_synonym="Mch2"
                     /coded_by="NM_001271984.1:67..900"
                     /db_xref="GeneID:83584"
                     /db_xref="RGD:70967"
ORIGIN      
        1 mtetdgfyrs revldpaeqy kmdhkrrgta lifnherffw hlalperrgt nadrdnltrr
       61 fselgfevkc fndlraeell lkihevstss hvdadcflcv flshgegnhi yaydakieiq
      121 tltglfkgdk cqslvgkpki fiiqacrgsq hdvpvvpldv vdhqtdkldd nvtqvdaasv
      181 ytlpagadfl mcysvaegyy shretvngsw yiqdlcemla rhgsslefte lltlvnrkvs
      241 qrrvdfckdp gaigkkqvpc fasmltkklh fcpkpsk
//
LOCUS       NP_001020824             421 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat-containing protein 42 [Rattus norvegicus].
ACCESSION   NP_001020824 XP_216457
VERSION     NP_001020824.1
DBSOURCE    REFSEQ: accession NM_001025653.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098685.1.
            
            On Jul 22, 2005 this sequence version replaced XP_216457.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098685.1, SRR8487227.175420.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..421
                     /product="leucine-rich repeat-containing protein 42"
                     /calculated_mol_wt=47783
     Region          149..170
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Region          150..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <167..>273
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          174..195
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Region          175..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          202..222
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Region          203..234
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          234..255
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Region          235..259
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          259..280
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Region          374..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM95.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R2U7; propagated from
                     UniProtKB/Swiss-Prot (Q4KM95.1)"
     CDS             1..421
                     /gene="Lrrc42"
                     /gene_synonym="RGD1308919"
                     /coded_by="NM_001025653.1:187..1452"
                     /db_xref="GeneID:298309"
                     /db_xref="RGD:1308919"
ORIGIN      
        1 mayylnseah ldpgpiyvre ngqlhmvsla ldgvknslqk prpfrlfpkg fsvelcmnre
       61 ddtaqkektd hfiftytreg nlrysakslf slvlgfisdn vdhidsligf peqiaeklfs
      121 aaearqkfte pgaglralqk fteaygslvl cslclrnryl vvaekleeik sfreltrldl
      181 sccwlgdehe llehltneal ssvtqlhlkd nclsdagirk mtapvrvlkr glenltlldl
      241 scnpeitdag igylfsfrkl ncldisgtgl kdikavkdkl rthiglvhsk vplkefdhsn
      301 cktegwadqi vlqwervsve avrqrkdpep rkaaqyfyqk ralteasrkc plaethmnss
      361 gklqfyreka pdchepllsq eskkskkraf eeseqeqssp qsakqkcvcl avedwdllns
      421 y
//
LOCUS       NP_058704                333 aa            linear   ROD 28-APR-2025
DEFINITION  glyceraldehyde-3-phosphate dehydrogenase [Rattus norvegicus].
ACCESSION   NP_058704 XP_216453
VERSION     NP_058704.1
DBSOURCE    REFSEQ: accession NM_017008.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Huo,J., Dong,W., Xu,J., Ma,L. and You,C.
  TITLE     Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in
            autophagy activation following subarachnoid hemorrhage
  JOURNAL   Exp Neurol 371, 114577 (2024)
   PUBMED   37863305
  REMARK    GeneRIF: Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
            in autophagy activation following subarachnoid hemorrhage.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Khodabandeh,S., Hosseini,A., Khazali,H. and Azizi,V.
  TITLE     Interplay between polycystic ovary syndrome and hypothyroidism on
            serum testosterone, oxidative stress and StAR gene expression in
            female rats
  JOURNAL   Endocrinol Diabetes Metab 5 (5), e359 (2022)
   PUBMED   35871495
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Sugiyama,K., Miura,J., Shimizu,M., Takashima,A., Matsuda,Y.,
            Kayashima,H., Okamoto,M., Nagashima,T. and Araki,T.
  TITLE     Effects of advanced glycation end products on dental pulp
            calcification
  JOURNAL   Oral Dis 28 (3), 745-755 (2022)
   PUBMED   33539626
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Mikeladze,M.A., Dutysheva,E.A., Kartsev,V.G., Margulis,B.A.,
            Guzhova,I.V. and Lazarev,V.F.
  TITLE     Disruption of the Complex between GAPDH and Hsp70 Sensitizes C6
            Glioblastoma Cells to Hypoxic Stress
  JOURNAL   Int J Mol Sci 22 (4), 1520 (2021)
   PUBMED   33546324
  REMARK    GeneRIF: Disruption of the Complex between GAPDH and Hsp70
            Sensitizes C6 Glioblastoma Cells to Hypoxic Stress.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Jiang,T., Dai,S., Yi,Y., Liu,Y., Zhang,S., Luo,M., Wang,H. and
            Xu,D.
  TITLE     The combination of hprt and gapdh is the best compound reference
            genes in the fetal rat hippocampus
  JOURNAL   Dev Neurobiol 80 (7-8), 229-238 (2020)
   PUBMED   32875725
  REMARK    GeneRIF: The combination of hprt and gapdh is the best compound
            reference genes in the fetal rat hippocampus.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Brand,I.A. and Heinickel,A.
  TITLE     Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa
            Zn(2+)-binding protein (parathymosin)
  JOURNAL   J Biol Chem 266 (31), 20984-20989 (1991)
   PUBMED   1834654
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Ercolani,L., Florence,B., Denaro,M. and Alexander,M.
  TITLE     Isolation and complete sequence of a functional human
            glyceraldehyde-3-phosphate dehydrogenase gene
  JOURNAL   J Biol Chem 263 (30), 15335-15341 (1988)
   PUBMED   3170585
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Maehara,Y., Fujiyoshi,T., Takahashi,K., Yamamoto,M. and Endo,H.
  TITLE     1.5 kb mRNA abundantly expressed in rat tumors encodes a 37
            kilodalton protein in vitro
  JOURNAL   Biochem Biophys Res Commun 131 (2), 800-805 (1985)
   PUBMED   2413848
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tso,J.Y., Sun,X.H., Kao,T.H., Reece,K.S. and Wu,R.
  TITLE     Isolation and characterization of rat and human
            glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity
            and molecular evolution of the gene
  JOURNAL   Nucleic Acids Res 13 (7), 2485-2502 (1985)
   PUBMED   2987855
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Fort,P., Marty,L., Piechaczyk,M., el Sabrouty,S., Dani,C.,
            Jeanteur,P. and Blanchard,J.M.
  TITLE     Various rat adult tissues express only one major mRNA species from
            the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
  JOURNAL   Nucleic Acids Res 13 (5), 1431-1442 (1985)
   PUBMED   2987824
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC059110.1.
            
            On Jan 7, 2005 this sequence version replaced XP_216453.1.
            
            Summary: This gene encodes a member of the
            glyceraldehyde-3-phosphate dehydrogenase protein family. A similar
            protein in human and mouse has been identified as a moonlighting
            protein based on its ability to perform mechanistically distinct
            functions. The encoded protein was originally identified as a key
            glycolytic enzyme that converts D-glyceraldehyde 3-phosphate (G3P)
            into 3-phospho-D-glyceroyl phosphate. Subsequent studies in human
            and mouse have assigned a variety of additional functions to the
            protein including nitrosylation of nuclear proteins. Many
            pseudogenes similar to this locus are found throughout the rat
            genome. [provided by RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DY317204.1, CR754152.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: inferred from conservation
            RefSeq Select criteria          :: based on conservation,
                                               expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..333
                     /product="glyceraldehyde-3-phosphate dehydrogenase"
                     /EC_number="1.2.1.12"
                     /note="38 kDa BFA-dependent ADP-ribosylation substrate;
                     peptidyl-cysteine S-nitrosylase GAPDH"
                     /calculated_mol_wt=35697
     Region          1..146
                     /region_name="Interaction with WARS1.
                     /evidence=ECO:0000250|UniProtKB:P04406"
                     /note="propagated from UniProtKB/Swiss-Prot (P04797.3)"
     Region          <2..330
                     /region_name="PLN02272"
                     /note="glyceraldehyde-3-phosphate dehydrogenase"
                     /db_xref="CDD:177912"
     Site            3
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            64
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            154
                     /site_type="other"
                     /note="Not nitrosylated.
                     /evidence=ECO:0000269|PubMed:8626764; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            177
                     /site_type="other"
                     /note="Activates thiol group during catalysis.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            192
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            192
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            213
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            225
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            225
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Region          243..248
                     /region_name="[IL]-x-C-x-x-[DE] motif.
                     /evidence=ECO:0000250|UniProtKB:P04406"
                     /note="propagated from UniProtKB/Swiss-Prot (P04797.3)"
     Site            252
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            258
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            261
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     Site            332
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:P04406; propagated from
                     UniProtKB/Swiss-Prot (P04797.3)"
     CDS             1..333
                     /gene="Gapdh"
                     /gene_synonym="BARS-38; Gapd"
                     /coded_by="NM_017008.4:76..1077"
                     /db_xref="GeneID:24383"
                     /db_xref="RGD:2661"
ORIGIN      
        1 mvkvgvngfg rigrlvtraa fscdkvdiva indpfidlny mvymfqydst hgkfngtvka
       61 engklvingk pitifqerdp anikwgdaga eyvvestgvf ttmekagahl kggakrviis
      121 apsadapmfv mgvnhekydn slkivsnasc ttnclaplak vihdnfgive glmttvhait
      181 atqktvdgps gklwrdgrga aqniipastg aakavgkvip elngkltgma frvptpnvsv
      241 vdltcrlekp akyddikkvv kqaaegplkg ilgytedqvv scdfnsnshs stfdagagia
      301 lndnfvklis wydneygysn rvvdlmayma ske
//
LOCUS       NP_001233248              86 aa            linear   ROD 28-APR-2025
DEFINITION  centromere protein W [Rattus norvegicus].
ACCESSION   NP_001233248 XP_001070657 XP_002725503
VERSION     NP_001233248.1
DBSOURCE    REFSEQ: accession NM_001246319.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Prendergast,L., van Vuuren,C., Kaczmarczyk,A., Doering,V.,
            Hellwig,D., Quinn,N., Hoischen,C., Diekmann,S. and Sullivan,K.F.
  TITLE     Premitotic assembly of human CENPs -T and -W switches centromeric
            chromatin to a mitotic state
  JOURNAL   PLoS Biol 9 (6), e1001082 (2011)
   PUBMED   21695110
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Kim,H., Lee,M., Lee,S., Park,B., Koh,W., Lee,D.J., Lim,D.S. and
            Lee,S.
  TITLE     Cancer-upregulated gene 2 (CUG2), a new component of centromere
            complex, is required for kinetochore function
  JOURNAL   Mol Cells 27 (6), 697-701 (2009)
   PUBMED   19533040
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC129114.1.
            
            On or before Oct 11, 2011 this sequence version replaced
            XP_001070657.1, XP_002725503.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC129114.1, EV767419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p11"
     Protein         1..86
                     /product="centromere protein W"
                     /note="cancer-up-regulated gene 2 protein"
                     /calculated_mol_wt=9672
     Region          1..86
                     /region_name="CENP-W"
                     /note="CENP-W protein; pfam15510"
                     /db_xref="CDD:434767"
     CDS             1..86
                     /gene="Cenpw"
                     /gene_synonym="CENP-W"
                     /coded_by="NM_001246319.1:115..375"
                     /db_xref="GeneID:689399"
                     /db_xref="RGD:1593465"
ORIGIN      
        1 mvlsttvcrr irrkapcafl krtlkqkkpr lslekrcdll ihlncllfvq klaeesrtna
       61 cesksgvikk dhvqaaakvi lkksrg
//
LOCUS       NP_001032279             791 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin homology domain-containing family H member 3 precursor
            [Rattus norvegicus].
ACCESSION   NP_001032279 XP_340910
VERSION     NP_001032279.1
DBSOURCE    REFSEQ: accession NM_001037202.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC107561.1.
            
            On Nov 18, 2005 this sequence version replaced XP_340910.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC107561.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..791
                     /product="pleckstrin homology domain-containing family H
                     member 3 precursor"
                     /note="pleckstrin homology domain-containing family H
                     member 3; PH domain-containing family H member 3;
                     pleckstrin homology domain containing, family H (with
                     MyTH4 domain) member 3"
                     /calculated_mol_wt=83081
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3B7L1.1)"
                     /calculated_mol_wt=2107
     mat_peptide     19..791
                     /product="Pleckstrin homology domain-containing family H
                     member 3. /id=PRO_0000311110"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7L1.1)"
                     /calculated_mol_wt=83081
     Region          29..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7L1.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z736; propagated from
                     UniProtKB/Swiss-Prot (Q3B7L1.1)"
     Region          84..208
                     /region_name="PH3_MyoX-like"
                     /note="Myosin X-like Pleckstrin homology (PH) domain,
                     repeat 3; cd13297"
                     /db_xref="CDD:270109"
     Region          288..397
                     /region_name="MyTH4"
                     /note="MyTH4 domain; pfam00784"
                     /db_xref="CDD:459939"
     Region          401..497
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          511..>549
                     /region_name="FERM_M"
                     /note="FERM central domain; pfam00373"
                     /db_xref="CDD:459788"
     Region          549..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7L1.1)"
     Region          593..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7L1.1)"
     Site            636
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z736; propagated from
                     UniProtKB/Swiss-Prot (Q3B7L1.1)"
     Region          658..745
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          748..791
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B7L1.1)"
     CDS             1..791
                     /gene="Plekhh3"
                     /gene_synonym="RGD1304854"
                     /coded_by="NM_001037202.1:416..2791"
                     /db_xref="GeneID:360634"
                     /db_xref="RGD:1304854"
ORIGIN      
        1 mplpgglwwl lccrrgftll hrdygdgels gdgdededde tfelrspspa gggrgsldvt
       61 ltqptrngpi tdrlqsweet wslipdkglp eddpdvivkg wlyreprggg arpwllprra
      121 wfvltrdsld qfsssgkgar rlgslvltsl csvtgperrp ketglwsvtv sgrkhsirlc
      181 sprqaeaerw gvalrevias kapletptql llrdiqesgg dpeavaliyr rnpilrhtss
      241 alyapllplp yevsapgpgy aplreeavrl flalqalega rrpgplmqgv lqtcrdlpal
      301 qdelflqlak qtsgpagppg lpatqdpaal rywqlltcms ctfrpggavr ghllghlert
      361 eqalpdsela eyarfirkal grtrgrelvp slaeisalsr rqellctvhc pgagacpvsi
      421 dshttageva relvgrlgla rsrnafalye qrgaqerala ggtlvadvlt sltseevgle
      481 dspdsgwrlc lrlhgplhpe glspeghelp flfeqahall lrgrppppdd tlralaalrl
      541 qslhrdfspr gplplldrlm pppappreqp srparrppps aallagalws pglakrraer
      601 arrigtgrst estaqvgggg ggsttaavlg gwkrlrgmgq aeamaaylal aaqcpgfgaa
      661 rydvlelste pgggapqklc lglgakamsl srpgesepih svsyghvaac qligphtlal
      721 rvgdsqlllq spqveeimel vnaylanpsp erpcsssgpp sqdlsdtspp sqhqvlekpq
      781 gqsgclrqlq d
//
LOCUS       NP_001102679             617 aa            linear   ROD 28-APR-2025
DEFINITION  BPI fold-containing family B member 4 precursor [Rattus
            norvegicus].
ACCESSION   NP_001102679 XP_001063904 XP_575269
VERSION     NP_001102679.2
DBSOURCE    REFSEQ: accession NM_001109209.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Dear,T.N., Boehm,T., Keverne,E.B. and Rabbitts,T.H.
  TITLE     Novel genes for potential ligand-binding proteins in subregions of
            the olfactory mucosa
  JOURNAL   EMBO J 10 (10), 2813-2819 (1991)
   PUBMED   1915264
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Sep 9, 2010 this sequence version replaced
            XP_575269.3, XP_001063904.2, NP_001102679.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR22582416.1590438.1,
                                           SRR22582424.1709440.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..617
                     /product="BPI fold-containing family B member 4 precursor"
                     /note="long palate, lung and nasal epithelium
                     carcinoma-associated protein 4; ligand-binding protein
                     RY2G5; potential ligand-binding protein"
                     /calculated_mol_wt=63859
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1739
     mat_peptide     18..617
                     /product="BPI fold-containing family B member 4.
                     /id=PRO_0000089160"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05704.2)"
                     /calculated_mol_wt=63859
     Region          124..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05704.2)"
     Region          221..391
                     /region_name="BPI1"
                     /note="BPI/LBP/CETP N-terminal domain; smart00328"
                     /db_xref="CDD:214622"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05704.2)"
     Region          417..617
                     /region_name="BPI2"
                     /note="BPI/LBP/CETP C-terminal domain; smart00329"
                     /db_xref="CDD:128624"
     Site            order(425,430,433,437,440,499,532,534,543,579,583,587,613)
                     /site_type="active"
                     /note="apolar binding pocket [active]"
                     /db_xref="CDD:238164"
     CDS             1..617
                     /gene="Bpifb4"
                     /gene_synonym="Lplunc4; RY2G5"
                     /coded_by="NM_001109209.2:1..1854"
                     /db_xref="GeneID:499925"
                     /db_xref="RGD:1561174"
ORIGIN      
        1 mwtawcvaal svaavcgirq dtttvlrvtk dvlgdaisgt iqksdafrsa lrevpvgvgg
       61 vpyndfhvre pppkytngrq lggnykyghi eandntaqlg gkyrygeild sdgslrdlrh
      121 edyrpsdsay hrgpgryrsa adpssagrlh rrelrpgeip agvatgalgp ggllgtggil
      181 anegilagqg gllggggllg dggllggggv lgvlgeggil stvqgitglr iveltlprvs
      241 vrllpgvgvy lslytrvain gksligfldi avevnitakv rltmdrtgyp rlviercdtl
      301 lggikvkllr gllpnlvdnl vnrvlanvlp dllcpivdvv lglvndqlgl vdslvplgil
      361 gsvqytfssl plvtgeflel dlntlvgeag gdlidyplgr pamlprpqmp elppmgdntn
      421 sqlaisanfl ssvltmlqkq galdiditdg mfedlppltt stlgalipkv fqqypesrpl
      481 tiriqvpnpp tvtlqkdkal vkvfatsevv vsqpndvett iclidvdtdl lasfsvegdk
      541 lmidakldkt slnlrtsnvg nfdvfileml vekifdlafm pamnailgsg vplpkilnid
      601 fsnadidvle dllvlst
//
LOCUS       NP_149090               1711 aa            linear   ROD 28-APR-2025
DEFINITION  receptor-type tyrosine-protein phosphatase V precursor [Rattus
            norvegicus].
ACCESSION   NP_149090
VERSION     NP_149090.1
DBSOURCE    REFSEQ: accession NM_033099.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1711)
  AUTHORS   Flister,M.J., Hoffman,M.J., Reddy,P., Jacob,H.J. and Moreno,C.
  TITLE     Congenic mapping and sequence analysis of the Renin locus
  JOURNAL   Hypertension 61 (4), 850-856 (2013)
   PUBMED   23460292
REFERENCE   2  (residues 1 to 1711)
  AUTHORS   Lathrop,W., Jordan,J., Eustice,D. and Chen,D.
  TITLE     Rat osteotesticular phosphatase gene (Esp): genomic structure and
            chromosome location
  JOURNAL   Mamm Genome 10 (4), 366-370 (1999)
   PUBMED   10087294
REFERENCE   3  (residues 1 to 1711)
  AUTHORS   Mauro,L.J., Olmsted,E.A., Davis,A.R. and Dixon,J.E.
  TITLE     Parathyroid hormone regulates the expression of the receptor
            protein tyrosine phosphatase, OST-PTP, in rat osteoblast-like cells
  JOURNAL   Endocrinology 137 (3), 925-933 (1996)
   PUBMED   8603605
REFERENCE   4  (residues 1 to 1711)
  AUTHORS   Mauro,L.J., Olmsted,E.A., Skrobacz,B.M., Mourey,R.J., Davis,A.R.
            and Dixon,J.E.
  TITLE     Identification of a hormonally regulated protein tyrosine
            phosphatase associated with bone and testicular differentiation
  JOURNAL   J Biol Chem 269 (48), 30659-30667 (1994)
   PUBMED   7527035
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L36884.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L36884.1, SRR8487227.65596.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132263 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1711
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q13"
     Protein         1..1711
                     /product="receptor-type tyrosine-protein phosphatase V
                     precursor"
                     /EC_number="3.1.3.48"
                     /note="Osteotesticular phosphatase; receptor-type
                     tyrosine-protein phosphatase V; OST-PTP; ES cell
                     phosphatase; osteotesticular protein-tyrosine phosphatase;
                     embryonic stem cell protein-tyrosine phosphatase; R-PTP-V;
                     protein tyrosine phosphatase receptor type W"
                     /calculated_mol_wt=185343
     sig_peptide     1..17
                     /calculated_mol_wt=1969
     mat_peptide     18..1711
                     /product="receptor-type tyrosine-protein phosphatase V"
                     /EC_number="3.1.3.48"
                     /calculated_mol_wt=185343
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Region          49..110
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Region          <148..201
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            259
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Region          377..>749
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            570
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            649
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            737
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            851
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Region          950..1069
                     /region_name="PTP_tm"
                     /note="TM proximal of protein tyrosine phosphatase,
                     receptor type J; pfam18861"
                     /db_xref="CDD:465889"
     Site            970
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            982
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64612.1)"
     Site            1075..1095
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64612.1)"
     Region          1178..1407
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1477..1693
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..1711
                     /gene="Ptprv"
                     /gene_synonym="Esp"
                     /coded_by="NM_033099.1:205..5340"
                     /db_xref="GeneID:64576"
                     /db_xref="RGD:621123"
ORIGIN      
        1 mrplillaal lwlqgflaed dacsslegsp drqgggplls vnvsshgkst slflswvaae
       61 lggfdyalsl rsvnssgspe gqqlqahtne sgfefhglvp gsryqlkltv lrpcwqnvti
      121 tltartaptv vrglqlhsag sparleasws dapgdqdsyq lllyhlesqt lacnvsvspd
      181 tlsysfgdll pgtqyvlevi twagslhakt silqwtepvp pdhlalralg tsslqafwns
      241 segatsfhlm ltdllggtnt tavirqgvst htflhlspgt phelkicasa gphqiwgpsa
      301 tewtypsyps dlvltplrne lwaswkaglg ardgyvlkls gpmeststlg peecnavfpg
      361 plppghytlq lkvlagpyda wvegstwlae saalprevpg arlwldglea skqpgrrall
      421 ysddapgslg nisvpsgath vifcglvpga hyrvdiasst gdisqsisgy tsplppqsle
      481 visrsspsdl tiawgpapgq legykvtwhq dgsqrspgdl vdlgpdtlsl tlkslvpgsc
      541 ytvsawawag nldsdsqkih sctrpapptn lslgfahqpa alkaswyhpp ggrdafhlrl
      601 yrlrpltles ekvlpreaqn fswaqltagc efqvqlstlw gsersssana tgwtppsapt
      661 lvnvtsdapt qlqvswahvp ggrsryqvtl yqestrtats imgpkedgts flgltpgtky
      721 kveviswagp lytaaanvsa wtyplipnel lvsmqagsav vnlawpsgpl gqgachaqls
      781 daghlsweqp lklgqelfml rdltpghtis msvrcragpl qasthlvvls vepgpvedvl
      841 chpeatylal nwtmpagdvd vclvvverlv pgggthfvfq vntsgdalll pnlmpttsyr
      901 lsltvlgrns rwsravslvc stsaeawhpp elaeppqvel gtgmgvtvmr gmfgkddgqi
      961 qwygiiatin mtlaqpsrea inytwydhyy rgcesflall fpnpfypepw agprswtvpv
     1021 gtedcdntqe icngrlksgf qyrfsvvafs rlntpetila fsafsepras islaiipltv
     1081 mlgavvgsiv ivcavlcllr wrclkgprse kdgfskelmp ynlwrthrpi pihsfrqsye
     1141 aksahahqtf fqefeelkev gkdqprleae hpdniiknry phvlpydhsr vrltqlpgep
     1201 hsdyinanfi pgyshtqeii atqgplkktl edfwrlvweq qvhviimltv gmengrvlce
     1261 hywpanstpv thghitihll aeepedewtr refqlqhgte qkqrrvkqlq fttwpdhsvp
     1321 eapssllafv elvqeqvqat qgkgpilvhc sagvgrtgtf vallrllrql eeekvadvfn
     1381 tvyilrlhrp lmiqtlsqyi flhscllnki legppdssds gpisvmdfaq acakraanan
     1441 agflkeykll kqaikdgtgs llpppdynqn sivsrrhsqe qfalveecpe dsmleaslfp
     1501 ggpsgcdhvv ltgsagpkel wemvwehdah vlvslglpdt kekppdiwpv emqpivtdmv
     1561 tvhrvsesnt ttgwpstlfr vihgesgker qvqclqfpcs esgcelpant lltfldavgq
     1621 ccfrgkskkp gtllshsskn tnqlgtflam eqllqqagte rtvdvfnval kqsqacglmt
     1681 ptleqyiyly nclnsallng lpragkwpap c
//
LOCUS       NP_001019501             597 aa            linear   ROD 28-APR-2025
DEFINITION  uncharacterized protein C2orf81 homolog [Rattus norvegicus].
ACCESSION   NP_001019501 XP_575578
VERSION     NP_001019501.1
DBSOURCE    REFSEQ: accession NM_001024330.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC079424.1.
            
            On May 27, 2005 this sequence version replaced XP_575578.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079424.1, CK595569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..597
                     /product="uncharacterized protein C2orf81 homolog"
                     /note="hypothetical gene supported by BC079424"
                     /calculated_mol_wt=65761
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP4.1)"
     Region          6..570
                     /region_name="DUF4639"
                     /note="Domain of unknown function (DUF4639); pfam15479"
                     /db_xref="CDD:464739"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP4.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXP4.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXP4.1)"
     Region          302..335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP4.1)"
     Region          549..569
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXP4.1)"
     CDS             1..597
                     /gene="C4h2orf81"
                     /coded_by="NM_001024330.1:67..1860"
                     /db_xref="GeneID:500227"
                     /db_xref="RGD:1566019"
ORIGIN      
        1 mshegsrqar drgvtrskae karpptqpvp qvdivpgrln eaewiafmsl eegedivgdi
       61 ladlvtrvme cafkvyltqq cvpftisqar eamlqitewr flardegesa vaedptwged
      121 eeplacttda waqgsvpvlh apapvgveeh fhneepgnpd qflidsswlg resqeptqss
      181 epsaeprvnp rptpamevfe eaeprdalev phrqesiltv pskeslrptl evqtvhspql
      241 spklsqvvsl qtcertgssf gshlslqdly hcvpqpdaag drlnlknkgq lcrssigsad
      301 rsllsvptpd gpspflqpgg merrpshktp tmrldpsrlp rhwvrpvaev lipdlearpl
      361 eiyrvrprks qvgasasesq algsrthskl qvsiprfplk rcatfrssgp dptlnlaqss
      421 psfgsnlpfl spgfrflarn lvppdvasap spklwprakw psgwereaeq lgelwagrtr
      481 vppqgqepve dsvsedsgwp lavpqvleat sqvlwkpmvi senmklvpgv smwnrgtqel
      541 lnpaaiqeea eegtpqapeq qpiqtgvskp qvimkqlrne tpkawllptk pvphsgs
//
LOCUS       NP_001099287             724 aa            linear   ROD 28-APR-2025
DEFINITION  NAD(+) hydrolase SARM1 [Rattus norvegicus].
ACCESSION   NP_001099287 XP_001080875 XP_213404
VERSION     NP_001099287.1
DBSOURCE    REFSEQ: accession NM_001105817.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Guo,Y., Mehrabian,Z., Milbrandt,J., DiAntonio,A. and Bernstein,S.L.
  TITLE     Synergistic Protection of Retinal Ganglion Cells (RGCs) by SARM1
            Inactivation with CNTF in a Rodent Model of Nonarteritic Anterior
            Ischemic Optic Neuropathy
  JOURNAL   Cells 13 (3), 202 (2024)
   PUBMED   38334594
  REMARK    GeneRIF: Synergistic Protection of Retinal Ganglion Cells (RGCs) by
            SARM1 Inactivation with CNTF in a Rodent Model of Nonarteritic
            Anterior Ischemic Optic Neuropathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Sato-Yamada,Y., Strickland,A., Sasaki,Y., Bloom,J., DiAntonio,A.
            and Milbrandt,J.
  TITLE     A SARM1-mitochondrial feedback loop drives neuropathogenesis in a
            Charcot-Marie-Tooth disease type 2A rat model
  JOURNAL   J Clin Invest 132 (23), e161566 (2022)
   PUBMED   36287202
  REMARK    GeneRIF: A SARM1-mitochondrial feedback loop drives
            neuropathogenesis in a Charcot-Marie-Tooth disease type 2A rat
            model.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Xue,T., Sun,Q., Zhang,Y., Wu,X., Shen,H., Li,X., Wu,J., Li,H.,
            Wang,Z. and Chen,G.
  TITLE     Phosphorylation at S548 as a Functional Switch of Sterile Alpha and
            TIR Motif-Containing 1 in Cerebral Ischemia/Reperfusion Injury in
            Rats
  JOURNAL   Mol Neurobiol 58 (2), 453-469 (2021)
   PUBMED   32968873
  REMARK    GeneRIF: Phosphorylation at S548 as a Functional Switch of Sterile
            Alpha and TIR Motif-Containing 1 in Cerebral Ischemia/Reperfusion
            Injury in Rats.
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Cetinkaya-Fisgin,A., Luan,X., Reed,N., Jeong,Y.E., Oh,B.C. and
            Hoke,A.
  TITLE     Cisplatin induced neurotoxicity is mediated by Sarm1 and calpain
            activation
  JOURNAL   Sci Rep 10 (1), 21889 (2020)
   PUBMED   33318563
  REMARK    GeneRIF: Cisplatin induced neurotoxicity is mediated by Sarm1 and
            calpain activation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Wan,L., Essuman,K., Anderson,R.G., Sasaki,Y., Monteiro,F.,
            Chung,E.H., Osborne Nishimura,E., DiAntonio,A., Milbrandt,J.,
            Dangl,J.L. and Nishimura,M.T.
  TITLE     TIR domains of plant immune receptors are NAD+-cleaving enzymes
            that promote cell death
  JOURNAL   Science 365 (6455), 799-803 (2019)
   PUBMED   31439793
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Summers,D.W., Gibson,D.A., DiAntonio,A. and Milbrandt,J.
  TITLE     SARM1-specific motifs in the TIR domain enable NAD+ loss and
            regulate injury-induced SARM1 activation
  JOURNAL   Proc Natl Acad Sci U S A 113 (41), E6271-E6280 (2016)
   PUBMED   27671644
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Gerdts,J., Brace,E.J., Sasaki,Y., DiAntonio,A. and Milbrandt,J.
  TITLE     SARM1 activation triggers axon degeneration locally via NAD
            destruction
  JOURNAL   Science 348 (6233), 453-457 (2015)
   PUBMED   25908823
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Panneerselvam,P., Singh,L.P., Ho,B., Chen,J. and Ding,J.L.
  TITLE     Targeting of pro-apoptotic TLR adaptor SARM to mitochondria:
            definition of the critical region and residues in the signal
            sequence
  JOURNAL   Biochem J 442 (2), 263-271 (2012)
   PUBMED   22145856
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Chen,C.Y., Lin,C.W., Chang,C.Y., Jiang,S.T. and Hsueh,Y.P.
  TITLE     Sarm1, a negative regulator of innate immunity, interacts with
            syndecan-2 and regulates neuronal morphology
  JOURNAL   J Cell Biol 193 (4), 769-784 (2011)
   PUBMED   21555464
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Kim,Y., Zhou,P., Qian,L., Chuang,J.Z., Lee,J., Li,C., Iadecola,C.,
            Nathan,C. and Ding,A.
  TITLE     MyD88-5 links mitochondria, microtubules, and JNK3 in neurons and
            regulates neuronal survival
  JOURNAL   J Exp Med 204 (9), 2063-2074 (2007)
   PUBMED   17724133
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_213404.2, XP_001080875.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMD00132261, SAMD00132262
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q25"
     Protein         1..724
                     /product="NAD(+) hydrolase SARM1"
                     /EC_number="3.2.2.6"
                     /note="sterile alpha and TIR motif-containing protein 1;
                     NADase SARM1; NADP(+) hydrolase SARM1"
                     /calculated_mol_wt=76616
     transit_peptide 1..27
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q6SZW1; propagated from
                     UniProtKB/Swiss-Prot (D3ZUM2.1)"
                     /calculated_mol_wt=3091
     mat_peptide     28..724
                     /product="NAD(+) hydrolase SARM1. /id=PRO_0000452004"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
                     /calculated_mol_wt=76616
     Region          60..100
                     /region_name="ARM 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          88..399
                     /region_name="SARM1_N"
                     /note="N-terminal ARM-repeat domain of SARM1 (sterile
                     alpha and TIR motif containing 1); cd24153"
                     /db_xref="CDD:467946"
     Region          114..153
                     /region_name="ARM 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          155..193
                     /region_name="ARM 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          196..235
                     /region_name="ARM 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          237..280
                     /region_name="ARM 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          281..314
                     /region_name="ARM 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          315..354
                     /region_name="ARM 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          359..402
                     /region_name="ARM 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          409..477
                     /region_name="SAM_SARM1-like_repeat1"
                     /note="SAM domain ot SARM1-like proteins, repeat 1;
                     cd09501"
                     /db_xref="CDD:188900"
     Region          479..547
                     /region_name="SAM_SARM1-like_repeat2"
                     /note="SAM domain of SARM1-like, repeat 2; cd09502"
                     /db_xref="CDD:188901"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32968873; propagated from
                     UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PDS3; propagated from
                     UniProtKB/Swiss-Prot (D3ZUM2.1)"
     Region          561..702
                     /region_name="TIR"
                     /note="Toll - interleukin 1 - resistance; smart00255"
                     /db_xref="CDD:214587"
     Region          703..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZUM2.1)"
     CDS             1..724
                     /gene="Sarm1"
                     /coded_by="NM_001105817.1:128..2302"
                     /db_xref="GeneID:287545"
                     /db_xref="RGD:1310078"
ORIGIN      
        1 mvltllfsay klcrffimsg prpgadrltv pgpdrsggts pwwaaggrgs revspgvgte
       61 vqgalerslp elqqalselk qasaaqavga glaevfqlve eawllpavgr evaqglcdai
      121 rldggldlll rllqapelet rvqaarlleq ilvaenrdrv ariglgviln lskerepvel
      181 arsvagileh mfkhseetcq rlvaagglda vlywcrrtdp allrhcalal ancalhggqt
      241 vqrcmvekra aewlfplafs kedellrlha clavavlatn keverevehs gtlalveplv
      301 asldpgrfar clvdasdtsq grgpddlqsl vllldssrle aqcigafylc aeaaikslqg
      361 ktkvfsdiga iqslkrlvsy stngttstla kralrllgee vprrilpcva swkeaevqtw
      421 lqqigfsqyc enfrdqqvdg dlllrltdee lqtdlgmkss itrkrffrel telktfasya
      481 tcdrsnladw lgsldprfrq ytyglvscgl drsllhrvse qqlledcgir lgvhrtrils
      541 aaremlhspl pctggkpsgd tpdvfisyrr nsgsqlasll kvhlqlhgfs vfidveklea
      601 gkfedkliqs vmaarnfvlv lsagaldkcm qdheckdwvh keivtalscs knivpiidgf
      661 ewpepqalpe dmqavltfng ikwsheyqea tiekiirflq grpsqdssag sdtslegats
      721 mglp
//
LOCUS       NP_001015026             305 aa            linear   ROD 28-APR-2025
DEFINITION  tetraspanin-12 [Rattus norvegicus].
ACCESSION   NP_001015026 XP_342648
VERSION     NP_001015026.1
DBSOURCE    REFSEQ: accession NM_001015026.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Junge,H.J., Yang,S., Burton,J.B., Paes,K., Shu,X., French,D.M.,
            Costa,M., Rice,D.S. and Ye,W.
  TITLE     TSPAN12 regulates retinal vascular development by promoting Norrin-
            but not Wnt-induced FZD4/beta-catenin signaling
  JOURNAL   Cell 139 (2), 299-311 (2009)
   PUBMED   19837033
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC092623.1.
            
            On Apr 20, 2005 this sequence version replaced XP_342648.2.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC092623.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN12840108, SAMN16676810 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..305
                     /product="tetraspanin-12"
                     /note="tspan-12; transmembrane 4 superfamily member 12"
                     /calculated_mol_wt=35247
     Region          10..246
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569A2.1)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569A2.1)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569A2.1)"
     Region          116..218
                     /region_name="TM4SF12_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF12_like family.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03157"
                     /db_xref="CDD:239410"
     Site            order(117,122,126,128..129,132,149,152..153,156..157)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239410"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569A2.1)"
     CDS             1..305
                     /gene="Tspan12"
                     /gene_synonym="Tm4sf12"
                     /coded_by="NM_001015026.1:394..1311"
                     /db_xref="GeneID:362326"
                     /db_xref="RGD:1311102"
ORIGIN      
        1 maredsvkcl rcllyalnll fwlmsisvla vsawmrdyln nvltltaetr veeaviltyf
       61 pvvhpvmiav ccfliivgml gycgtvkrnl lllawyfgtl lvifcvelac gvwtyeqevm
      121 vpvqwsdmvt lkarmtnygl pryrwlthaw nyfqrefkcc gvvyftdwle mtemdwppds
      181 ccvrefpgcs kqahqedlsd lyqegcgkkm ysflrgtkql qvlrflgisi gvtqilamil
      241 titllwalyy drrepgtdqm lslkndasqh lschsvellk pslsrifeht smansfnthf
      301 emeel
//
LOCUS       NP_620260                312 aa            linear   ROD 28-APR-2025
DEFINITION  phospholipid phosphatase 3 [Rattus norvegicus].
ACCESSION   NP_620260
VERSION     NP_620260.2
DBSOURCE    REFSEQ: accession NM_138905.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Gutierrez-Martinez,E., Fernandez-Ulibarri,I., Lazaro-Dieguez,F.,
            Johannes,L., Pyne,S., Sarri,E. and Egea,G.
  TITLE     Lipid phosphate phosphatase 3 participates in transport carrier
            formation and protein trafficking in the early secretory pathway
  JOURNAL   J Cell Sci 126 (Pt 12), 2641-2655 (2013)
   PUBMED   23591818
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Lopez-Juarez,A., Morales-Lazaro,S., Sanchez-Sanchez,R., Sunkara,M.,
            Lomeli,H., Velasco,I., Morris,A.J. and Escalante-Alcalde,D.
  TITLE     Expression of LPP3 in Bergmann glia is required for proper
            cerebellar sphingosine-1-phosphate metabolism/signaling and
            development
  JOURNAL   Glia 59 (4), 577-589 (2011)
   PUBMED   21319224
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Humtsoe,J.O., Liu,M., Malik,A.B. and Wary,K.K.
  TITLE     Lipid phosphate phosphatase 3 stabilization of beta-catenin induces
            endothelial cell migration and formation of branching point
            structures
  JOURNAL   Mol Cell Biol 30 (7), 1593-1606 (2010)
   PUBMED   20123964
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Kai,M., Sakane,F., Jia,Y.J., Imai,S., Yasuda,S. and Kanoh,H.
  TITLE     Lipid phosphate phosphatases 1 and 3 are localized in distinct
            lipid rafts
  JOURNAL   J Biochem 140 (5), 677-686 (2006)
   PUBMED   17005594
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Humtsoe,J.O., Bowling,R.A. Jr., Feng,S. and Wary,K.K.
  TITLE     Murine lipid phosphate phosphohydrolase-3 acts as a cell-associated
            integrin ligand
  JOURNAL   Biochem Biophys Res Commun 335 (3), 906-919 (2005)
   PUBMED   16099422
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Humtsoe,J.O., Feng,S., Thakker,G.D., Yang,J., Hong,J. and Wary,K.K.
  TITLE     Regulation of cell-cell interactions by phosphatidic acid
            phosphatase 2b/VCIP
  JOURNAL   EMBO J 22 (7), 1539-1554 (2003)
   PUBMED   12660161
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Roberts,R., Sciorra,V.A. and Morris,A.J.
  TITLE     Human type 2 phosphatidic acid phosphohydrolases. Substrate
            specificity of the type 2a, 2b, and 2c enzymes and cell surface
            activity of the 2a isoform
  JOURNAL   J Biol Chem 273 (34), 22059-22067 (1998)
   PUBMED   9705349
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Kai,M., Wada,I., Imai,Si., Sakane,F. and Kanoh,H.
  TITLE     Cloning and characterization of two human isozymes of
            Mg2+-independent phosphatidic acid phosphatase
  JOURNAL   J Biol Chem 272 (39), 24572-24578 (1997)
   PUBMED   9305923
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Barila,D., Plateroti,M., Nobili,F., Muda,A.O., Xie,Y., Morimoto,T.
            and Perozzi,G.
  TITLE     The Dri 42 gene, whose expression is up-regulated during epithelial
            differentiation, encodes a novel endoplasmic reticulum resident
            transmembrane protein
  JOURNAL   J Biol Chem 271 (47), 29928-29936 (1996)
   PUBMED   8939937
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Barila,D., Murgia,C., Nobili,F., Gaetani,S. and Perozzi,G.
  TITLE     Subtractive hybridization cloning of novel genes differentially
            expressed during intestinal development
  JOURNAL   Eur J Biochem 223 (2), 701-709 (1994)
   PUBMED   8055940
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC072544.1.
            
            On Jun 13, 2004 this sequence version replaced NP_620260.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072544.1, Y07783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..312
                     /product="phospholipid phosphatase 3"
                     /EC_number="3.1.3.4"
                     /note="lipid phosphate phosphohydrolase 3; PAP2b; PAP-2b;
                     PAP2-beta; phosphatidic acid phosphatase 2b; phosphatidate
                     phosphohydrolase type 2b; phosphatidic acid phosphatase
                     type 2B; differentially expressed in rat intestine 42; ER
                     transmembrane protein Dri 42"
                     /calculated_mol_wt=35102
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O14495; propagated from
                     UniProtKB/Swiss-Prot (P97544.1)"
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Region          109..110
                     /region_name="Dityrosine basolateral targeting motif.
                     /evidence=ECO:0000250|UniProtKB:O14495"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Region          126..272
                     /region_name="PAP2_wunen"
                     /note="PAP2, wunen subfamily. Most likely a family of
                     membrane associated phosphatidic acid phosphatases. Wunen
                     is a drosophila protein expressed in the central nervous
                     system, which provides repellent activity towards
                     primordial germ cells (PGCs), controls the...; cd03384"
                     /db_xref="CDD:239479"
     Site            order(149,156,198..200,246,252,256)
                     /site_type="active"
                     /db_xref="CDD:239479"
     Region          149..157
                     /region_name="Phosphatase sequence motif I.
                     /evidence=ECO:0000250|UniProtKB:O34349"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97544.1)"
     Region          183..185
                     /region_name="Integrin-binding motif.
                     /evidence=ECO:0000250|UniProtKB:O14495"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Region          197..200
                     /region_name="Phosphatase sequence motif II.
                     /evidence=ECO:0000250|UniProtKB:O34349"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            227..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Region          245..256
                     /region_name="Phosphatase sequence motif III.
                     /evidence=ECO:0000250|UniProtKB:O34349"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Site            256
                     /site_type="other"
                     /note="Stabilizes the active site histidine for
                     nucleophilic attack.
                     /evidence=ECO:0000250|UniProtKB:O34349; propagated from
                     UniProtKB/Swiss-Prot (P97544.1)"
     Site            259..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     Region          276..312
                     /region_name="Mediates interaction with CTNND1.
                     /evidence=ECO:0000250|UniProtKB:O14495"
                     /note="propagated from UniProtKB/Swiss-Prot (P97544.1)"
     CDS             1..312
                     /gene="Plpp3"
                     /gene_synonym="Dri42; Ppap2b"
                     /coded_by="NM_138905.2:418..1356"
                     /db_xref="GeneID:192270"
                     /db_xref="RGD:620454"
ORIGIN      
        1 mqsykydkai vpesknggsp alnnnprkgg skrvllicld lfclfmaalp fliietstik
       61 pyrrgfycnd esikyplkvs etindavlca vgiviailai itgefyriyy lkeksrstiq
      121 npyvaalykq vgcflfgcai sqsftdiakv sigrlrphfl svcdpdfsqi ncsegyiqny
      181 rcrgedskvq earksffsgh asfsmftmly lvlylqarft wrgarllrpl lqftllmmaf
      241 ytglsrvsdy khhpsdvlag faqgalvacc ivffvsdlfk tkttlslpap airreilspv
      301 dimdrsnhhn mv
//
LOCUS       NP_742042                147 aa            linear   ROD 28-APR-2025
DEFINITION  protein phosphatase 1 regulatory subunit 14B [Rattus norvegicus].
ACCESSION   NP_742042 XP_001074638
VERSION     NP_742042.1
DBSOURCE    REFSEQ: accession NM_172045.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Tountas,N.A. and Brautigan,D.L.
  TITLE     Migration and retraction of endothelial and epithelial cells
            require PHI-1, a specific protein-phosphatase-1 inhibitor protein
  JOURNAL   J Cell Sci 117 (Pt 24), 5905-5912 (2004)
   PUBMED   15522888
  REMARK    GeneRIF: PHI-1 participates in regulatory events at the trailing
            edge of migrating cells and modulates retraction of endothelial and
            epithelial cells
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Liu,Q.R., Zhang,P.W., Lin,Z., Li,Q.F., Woods,A.S., Troncoso,J. and
            Uhl,G.R.
  TITLE     GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory
            protein, is activated by PKC and inactivated by PKA
  JOURNAL   Biochem J 377 (Pt 1), 171-181 (2004)
   PUBMED   12974676
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Deng,J.T., Sutherland,C., Brautigan,D.L., Eto,M. and Walsh,M.P.
  TITLE     Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and
            PHI-1, by integrin-linked kinase
  JOURNAL   Biochem J 367 (Pt 2), 517-524 (2002)
   PUBMED   12144526
  REMARK    GeneRIF: ILK may activate smooth-muscle contraction both directly,
            via phosphorylation of myosin, and indirectly, via phosphorylation
            and activation of CPI-17 and PHI-1, leading to inhibition of myosin
            light-chain phosphatase.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AY122323.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001074638.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY122323.1, AW918183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..147
                     /product="protein phosphatase 1 regulatory subunit 14B"
                     /note="phosphatase holoenzyme inhibitor 1; ubiquitous
                     PKC-potentiated PP1 inhibitor; protein phosphatase 1,
                     regulatory (inhibitor) 5 subunit 14B"
                     /calculated_mol_wt=15826
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K3F3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96C90; propagated from
                     UniProtKB/Swiss-Prot (Q8K3F3.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C90; propagated from
                     UniProtKB/Swiss-Prot (Q8K3F3.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q96C90; propagated from
                     UniProtKB/Swiss-Prot (Q8K3F3.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96C90; propagated from
                     UniProtKB/Swiss-Prot (Q8K3F3.1)"
     Region          51..147
                     /region_name="PP1_inhibitor"
                     /note="PKC-activated protein phosphatase-1 inhibitor;
                     pfam05361"
                     /db_xref="CDD:461630"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62084; propagated from
                     UniProtKB/Swiss-Prot (Q8K3F3.1)"
     CDS             1..147
                     /gene="Ppp1r14b"
                     /gene_synonym="PHI-1"
                     /coded_by="NM_172045.1:9..452"
                     /db_xref="GeneID:259225"
                     /db_xref="RGD:628702"
ORIGIN      
        1 madsgpagga alaapapgpg sgstgprvyf qsppgaageg pggadddgpv rrqgkvtvky
       61 drkelrkrln leewileqlt rlydcqeeei peleidvdel ldmesddtra arvkellvdc
      121 ykpteafisg lldkirgmqk lstpqkk
//
LOCUS       NP_443215                618 aa            linear   ROD 28-APR-2025
DEFINITION  sodium/iodide cotransporter [Rattus norvegicus].
ACCESSION   NP_443215
VERSION     NP_443215.2
DBSOURCE    REFSEQ: accession NM_052983.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Ravera,S., Nicola,J.P., Salazar-De Simone,G., Sigworth,F.J.,
            Karakas,E., Amzel,L.M., Bianchet,M.A. and Carrasco,N.
  TITLE     Structural insights into the mechanism of the sodium/iodide
            symporter
  JOURNAL   Nature 612 (7941), 795-801 (2022)
   PUBMED   36517601
  REMARK    GeneRIF: Structural insights into the mechanism of the
            sodium/iodide symporter.
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Di Giusto,P., Martin,M., Funes Chaban,M., Sampieri,L., Nicola,J.P.
            and Alvarez,C.
  TITLE     Transcription Factor CREB3L1 Regulates the Expression of the
            Sodium/Iodide Symporter (NIS) in Rat Thyroid Follicular Cells
  JOURNAL   Cells 11 (8), 1314 (2022)
   PUBMED   35455992
  REMARK    GeneRIF: Transcription Factor CREB3L1 Regulates the Expression of
            the Sodium/Iodide Symporter (NIS) in Rat Thyroid Follicular Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Concilio,S.C., Zhekova,H.R., Noskov,S.Y. and Russell,S.J.
  TITLE     Inter-species variation in monovalent anion substrate selectivity
            and inhibitor sensitivity in the sodium iodide symporter (NIS)
  JOURNAL   PLoS One 15 (2), e0229085 (2020)
   PUBMED   32084174
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Faria,M., Domingues,R., Paixao,F., Bugalho,M.J., Matos,P. and
            Silva,A.L.
  TITLE     TNFalpha-mediated activation of NF-kappaB downregulates
            sodium-iodide symporter expression in thyroid cells
  JOURNAL   PLoS One 15 (2), e0228794 (2020)
   PUBMED   32049985
  REMARK    GeneRIF: TNFalpha-mediated activation of NF-kappaB downregulates
            sodium-iodide symporter expression in thyroid cells
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Matos,L.P.L., Penha,R.C.C., Cardoso-Weide,L.C., Freitas,M.L.,
            Silva,D.L.S.G. and Ferreira,A.C.F.
  TITLE     Regulation of thyroid sodium-iodide symporter in different stages
            of goiter: Possible involvement of reactive oxygen species
  JOURNAL   Clin Exp Pharmacol Physiol 45 (4), 326-334 (2018)
   PUBMED   29112772
  REMARK    GeneRIF: relationship between the size of the goiter and NIS
            regulation
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Perron,B., Rodriguez,A.M., Leblanc,G. and Pourcher,T.
  TITLE     Cloning of the mouse sodium iodide symporter and its expression in
            the mammary gland and other tissues
  JOURNAL   J Endocrinol 170 (1), 185-196 (2001)
   PUBMED   11431151
REFERENCE   7  (residues 1 to 618)
  AUTHORS   Ohno,M., Zannini,M., Levy,O., Carrasco,N. and di Lauro,R.
  TITLE     The paired-domain transcription factor Pax8 binds to the upstream
            enhancer of the rat sodium/iodide symporter gene and participates
            in both thyroid-specific and cyclic-AMP-dependent transcription
  JOURNAL   Mol Cell Biol 19 (3), 2051-2060 (1999)
   PUBMED   10022892
REFERENCE   8  (residues 1 to 618)
  AUTHORS   Eskandari,S., Loo,D.D., Dai,G., Levy,O., Wright,E.M. and
            Carrasco,N.
  TITLE     Thyroid Na+/I- symporter. Mechanism, stoichiometry, and specificity
  JOURNAL   J Biol Chem 272 (43), 27230-27238 (1997)
   PUBMED   9341168
REFERENCE   9  (residues 1 to 618)
  AUTHORS   Fujiwara,H., Tatsumi,K., Miki,K., Harada,T., Miyai,K., Takai,S. and
            Amino,N.
  TITLE     Congenital hypothyroidism caused by a mutation in the Na+/I-
            symporter
  JOURNAL   Nat Genet 16 (2), 124-125 (1997)
   PUBMED   9171822
  REMARK    Erratum:[Nat Genet. 1997 Sep;17(1):122. doi: 10.1038/ng0997-122a.
            PMID: 9288112]
REFERENCE   10 (residues 1 to 618)
  AUTHORS   Dai,G., Levy,O. and Carrasco,N.
  TITLE     Cloning and characterization of the thyroid iodide transporter
  JOURNAL   Nature 379 (6564), 458-460 (1996)
   PUBMED   8559252
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U60282.1, JAXUCZ010000016.1 and BF392663.1.
            
            On Oct 11, 2007 this sequence version replaced NP_443215.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KP213324.1, SRR26643295.52320.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16p14"
     Protein         1..618
                     /product="sodium/iodide cotransporter"
                     /note="Na+/I- symporter; Na(+)/I(-) cotransporter;
                     Na(+)/I(-) symporter; solute carrier family 5 (sodium
                     iodide symporter), member 5; solute carrier family 5
                     (sodium/iodide cotransporter), member 5; sodium/iodide
                     symporter"
                     /calculated_mol_wt=65098
     Region          15..549
                     /region_name="SLC5sbd_NIS"
                     /note="Na(+)/iodide cotransporter NIS and related
                     proteins; solute-binding domain; cd11503"
                     /db_xref="CDD:271393"
     Site            15..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            57..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            order(65,68,350,353..354)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:271393"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            131..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            164..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            190..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            244..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            279..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            336..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            387..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            412..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            442..465
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63008.1)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q63008.1)"
     Site            521..545
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     Region          587..618
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63008.1)"
     CDS             1..618
                     /gene="Slc5a5"
                     /gene_synonym="Nis"
                     /coded_by="NM_052983.2:85..1941"
                     /db_xref="GeneID:114613"
                     /db_xref="RGD:69267"
ORIGIN      
        1 megaeagara tfgawdygvf atmllvstgi glwvglargg qrsaddfftg grqlaavpvg
       61 lslaasfmsa vqvlgvpaea aryglkflwm cagqllnsll taflflpify rlgltstyqy
      121 lelrfsravr lcgtlqylva tmlytgiviy apalilnqvt gldiwaslls tgiictlytt
      181 vggmkavvwt dvfqvvvmlv gfwvilargv illggprnml slaqnhsrin lmdfdpdprs
      241 rytfwtfivg gtlvwlsmyg vnqaqvqryv achtegkakl allvnqlglf livasaaccg
      301 ivmfvyykdc dplltgrisa pdqympllvl difedlpgvp glflacaysg tlstastsin
      361 amaavtvedl ikprmpglap rklvfiskgl sfiygsaclt vaalssllgg gvlqgsftvm
      421 gvisgpllga ftlgmllpac ntpgvlsgla aglavslwva vgatlyppge qtmgvlptsa
      481 agctndsvll gppgatnasn gipssgmdtg rpaladtfya isylyygalg tlttmlcgal
      541 isyltgptkr sslgpgllww dlarqtasva pkedtatlee slvkgpedip avtkkppglk
      601 pgaethplyl ghdvetnl
//
LOCUS       NP_001030328             559 aa            linear   ROD 28-APR-2025
DEFINITION  neutral amino acid transporter 9 [Rattus norvegicus].
ACCESSION   NP_001030328 XP_226760
VERSION     NP_001030328.1
DBSOURCE    REFSEQ: accession NM_001035251.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Jung,J.W., Macalino,S.J.Y., Cui,M., Kim,J.E., Kim,H.J., Song,D.G.,
            Nam,S.H., Kim,S., Choi,S. and Lee,J.W.
  TITLE     Transmembrane 4 L Six Family Member 5 Senses Arginine for mTORC1
            Signaling
  JOURNAL   Cell Metab 29 (6), 1306-1319 (2019)
   PUBMED   30956113
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Wyant,G.A., Abu-Remaileh,M., Wolfson,R.L., Chen,W.W., Freinkman,E.,
            Danai,L.V., Vander Heiden,M.G. and Sabatini,D.M.
  TITLE     mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino
            Acids from Lysosomes and Use Protein as a Nutrient
  JOURNAL   Cell 171 (3), 642-654 (2017)
   PUBMED   29053970
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Wang,S., Tsun,Z.Y., Wolfson,R.L., Shen,K., Wyant,G.A.,
            Plovanich,M.E., Yuan,E.D., Jones,T.D., Chantranupong,L., Comb,W.,
            Wang,T., Bar-Peled,L., Zoncu,R., Straub,C., Kim,C., Park,J.,
            Sabatini,B.L. and Sabatini,D.M.
  TITLE     Metabolism. Lysosomal amino acid transporter SLC38A9 signals
            arginine sufficiency to mTORC1
  JOURNAL   Science 347 (6218), 188-194 (2015)
   PUBMED   25567906
REFERENCE   5  (residues 1 to 559)
  AUTHORS   denDekker,A.D., Xu,X., Vaughn,M.D., Puckett,A.H., Gardner,L.L.,
            Lambring,C.J., Deschenes,L. and Samuelson,D.J.
  TITLE     Rat Mcs1b is concordant to the genome-wide association-identified
            breast cancer risk locus at human 5q11.2 and MIER3 is a candidate
            cancer susceptibility gene
  JOURNAL   Cancer Res 72 (22), 6002-6012 (2012)
   PUBMED   22993404
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105869.1.
            
            On Nov 1, 2005 this sequence version replaced XP_226760.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105869.1, JQ013729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132296, SAMD00132297
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q14"
     Protein         1..559
                     /product="neutral amino acid transporter 9"
                     /note="putative sodium-coupled neutral amino acid
                     transporter 9"
                     /calculated_mol_wt=63287
     Region          114..555
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Region          128..133
                     /region_name="Important for arginine binding and amino
                     acid transport. /evidence=ECO:0000250|UniProtKB:Q08BA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            198..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            282..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            308..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            393..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            436..456
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Region          442..452
                     /region_name="CARC motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NBW4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Region          455..461
                     /region_name="CRAC motif.
                     /evidence=ECO:0000250|UniProtKB:Q8NBW4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            506..526
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     Site            539..559
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q3.1)"
     CDS             1..559
                     /gene="Slc38a9"
                     /gene_synonym="RGD1311881"
                     /coded_by="NM_001035251.1:30..1709"
                     /db_xref="GeneID:310091"
                     /db_xref="RGD:1311881"
ORIGIN      
        1 manvdsdsrh lisevehevn pgpmniqfds sdlrskrpfy ieptnivnvn dviqkvsdha
       61 aamnkrihyy srlttpadka liapdhvvpa peecyvyspl gsayklksyt egyrkntslv
      121 tifmiwntmm gtsilsipwg ikqagfttgm cvivlmgllt lyccyrvvks rsmivtsdtt
      181 tweypdvckh yfgsfgqwss llfslvslig amivywvlms nflfntgkfi fnfihhindt
      241 dtvlstnnss pvicpsagsg hpdnssmify nsdtevrlfe rwwdksktvp fyliglllpl
      301 lnfkspsffs kfnilgtvsv lylifivtlk airlgfhlef hwfapteffv peiraqfpql
      361 tgvltlaffi hnciitllkn nknqennvrd lciaymlvtl tylyigvlvf asfpspplpk
      421 dcieqnfldn fpssdtlsfi aricllfqmm tvypllgyla rvqllghifg diypsifhvl
      481 ilnliivgag vtmacfypni ggiirysgaa cglafvfiyp sliyilsqhq eerltwpklv
      541 fhiiiiilgl anliaqffm
//
LOCUS       NP_434695                235 aa            linear   ROD 28-APR-2025
DEFINITION  BPI fold-containing family A member 2 precursor [Rattus
            norvegicus].
ACCESSION   NP_434695
VERSION     NP_434695.1
DBSOURCE    REFSEQ: accession NM_052808.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Abdolhosseini,M., Sotsky,J.B., Shelar,A.P., Joyce,P.B. and
            Gorr,S.U.
  TITLE     Human parotid secretory protein is a lipopolysaccharide-binding
            protein: identification of an anti-inflammatory peptide domain
  JOURNAL   Mol Cell Biochem 359 (1-2), 1-8 (2012)
   PUBMED   21833535
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Bingle,C.D., Seal,R.L. and Craven,C.J.
  TITLE     Systematic nomenclature for the PLUNC/PSP/BSP30/SMGB proteins as a
            subfamily of the BPI fold-containing superfamily
  JOURNAL   Biochem Soc Trans 39 (4), 977-983 (2011)
   PUBMED   21787333
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Ekstrom,J., Murakami,M., Inzitari,R., Khosravani,N., Fanali,C.,
            Cabras,T., Fujita-Yoshigaki,J., Sugiya,H., Messana,I. and
            Castagnola,M.
  TITLE     RP-HPLC-ESI-MS characterization of novel peptide fragments related
            to rat parotid secretory protein in parasympathetic induced saliva
  JOURNAL   J Sep Sci 32 (17), 2944-2952 (2009)
   PUBMED   19642100
  REMARK    GeneRIF: Results suggest that at least two pathways--granular and
            vesicular--are responsible for the generation of the two peptides,
            PSPFr-A and PSPFr-B, from rat parotid secretory protein.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Bingle,L., Barnes,F.A., Lunn,H., Musa,M., Webster,S., Douglas,C.W.,
            Cross,S.S., High,A.S. and Bingle,C.D.
  TITLE     Characterisation and expression of SPLUNC2, the human orthologue of
            rodent parotid secretory protein
  JOURNAL   Histochem Cell Biol 132 (3), 339-349 (2009)
   PUBMED   19499239
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Kwitek,A.E., Gullings-Handley,J., Yu,J., Carlos,D.C., Orlebeke,K.,
            Nie,J., Eckert,J., Lemke,A., Andrae,J.W., Bromberg,S., Pasko,D.,
            Chen,D., Scheetz,T.E., Casavant,T.L., Soares,M.B., Sheffield,V.C.,
            Tonellato,P.J. and Jacob,H.J.
  TITLE     High-density rat radiation hybrid maps containing over 24,000
            SSLPs, genes, and ESTs provide a direct link to the rat genome
            sequence
  JOURNAL   Genome Res 14 (4), 750-757 (2004)
   PUBMED   15060019
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Cowley,D.J., Chu,M. and Gorr,S.U.
  TITLE     Sorting of an exocrine secretory protein to the regulated secretory
            pathway in endocrine cells
  JOURNAL   Biochem Biophys Res Commun 299 (1), 98-101 (2002)
   PUBMED   12435394
  REMARK    GeneRIF: PSP co-fractionates with chromogranin A but not with
            secreted alkaline phosphatase; its sorting is not cell-type
            specific but the precise mechanism of its sorting is unknown
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Mirels,L., Miranda,A.J. and Ball,W.D.
  TITLE     Characterization of the rat salivary-gland B1-immunoreactive
            proteins
  JOURNAL   Biochem J 330 (Pt 1) (Pt 1), 437-444 (1998)
   PUBMED   9461541
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Mirels,L. and Ball,W.D.
  TITLE     Neonatal rat submandibular gland protein SMG-A and parotid
            secretory protein are alternatively regulated members of a salivary
            protein multigene family
  JOURNAL   J Biol Chem 267 (4), 2679-2687 (1992)
   PUBMED   1370829
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M83209.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M83209.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680423 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     Protein         1..235
                     /product="BPI fold-containing family A member 2 precursor"
                     /note="neonatal submandibular gland protein; short palate,
                     lung and nasal epithelium carcinoma-associated protein 2;
                     BPI fold containing family A, member 2E; parotid secretory
                     protein"
                     /calculated_mol_wt=22480
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2068
     mat_peptide     21..235
                     /product="BPI fold-containing family A member 2"
                     /name="secreted form"
                     /calculated_mol_wt=22480
     Region          45..214
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     CDS             1..235
                     /gene="Bpifa2"
                     /gene_synonym="Bpifa2e; Psp"
                     /coded_by="NM_052808.1:47..754"
                     /db_xref="GeneID:50585"
                     /db_xref="RGD:3431"
ORIGIN      
        1 mfqlgslvvl cglligtses llgdvanavn nldilnspse avaqnlnldv gslqqattwp
       61 sakdsiletl nkvelgnsng ftplnglllr vnkfrvldlq aglssngkdi dlklplvfei
      121 sfslpvigpt ldvavsldll nsvsvqtnaq tglpgvtlgk csgntdkisi sllgrrlpfv
      181 nrildgvsgl ltgavsillq nilcpvlqyl lstmsgsaiq gllsnvltgq lavpl
//
LOCUS       NP_001009653             715 aa            linear   ROD 28-APR-2025
DEFINITION  methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
            [Rattus norvegicus].
ACCESSION   NP_001009653 XP_215554
VERSION     NP_001009653.1
DBSOURCE    REFSEQ: accession NM_001009653.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Chu,C.H. and Cheng,D.
  TITLE     Expression, purification, characterization of human
            3-methylcrotonyl-CoA carboxylase (MCCC)
  JOURNAL   Protein Expr Purif 53 (2), 421-427 (2007)
   PUBMED   17360195
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Stadler,S.C., Polanetz,R., Meier,S., Mayerhofer,P.U.,
            Herrmann,J.M., Anslinger,K., Roscher,A.A., Roschinger,W. and
            Holzinger,A.
  TITLE     Mitochondrial targeting signals and mature peptides of
            3-methylcrotonyl-CoA carboxylase
  JOURNAL   Biochem Biophys Res Commun 334 (3), 939-946 (2005)
   PUBMED   16023992
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC088473.1.
            
            On Jan 13, 2005 this sequence version replaced XP_215554.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC088473.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q25"
     Protein         1..715
                     /product="methylcrotonoyl-CoA carboxylase subunit alpha,
                     mitochondrial"
                     /EC_number="6.4.1.4"
                     /note="methylcrotonoyl-Coenzyme A carboxylase 1 (alpha);
                     MCCase subunit alpha; 3-methylcrotonyl-CoA carboxylase 1;
                     3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
                     3-methylcrotonyl-CoA carboxylase biotin-containing
                     subunit; methylcrotonoyl-CoA carboxylase 1 (alpha)"
                     /calculated_mol_wt=74909
     transit_peptide 1..38
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q96RQ3; propagated from
                     UniProtKB/Swiss-Prot (Q5I0C3.1)"
                     /calculated_mol_wt=4439
     mat_peptide     39..715
                     /product="Methylcrotonoyl-CoA carboxylase subunit alpha,
                     mitochondrial. /id=PRO_0000365095"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5I0C3.1)"
                     /calculated_mol_wt=74909
     Region          45..494
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MR8; propagated from
                     UniProtKB/Swiss-Prot (Q5I0C3.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MR8; propagated from
                     UniProtKB/Swiss-Prot (Q5I0C3.1)"
     Site            490
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MR8; propagated from
                     UniProtKB/Swiss-Prot (Q5I0C3.1)"
     Site            577
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99MR8; propagated from
                     UniProtKB/Swiss-Prot (Q5I0C3.1)"
     Region          647..710
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(667,676..678,685)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            677
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..715
                     /gene="Mccc1"
                     /coded_by="NM_001009653.1:19..2166"
                     /db_xref="GeneID:294972"
                     /db_xref="RGD:1310615"
ORIGIN      
        1 maaaallaav drnqlrrvpi lllqprewpw khrtvkygtt pggsitkvli anrgeiacrv
       61 irtarkmgvq svavyseadr nsmhvdmade aysigpapsq qsylamekii qvakssaaqa
      121 ihpgygflse nmefaefckq egiifigpps tairdmgiks tsksimaaag vpvvegyhgn
      181 dqsdeclkeh agkigypvmi kairggggkg mriirsekef qeqlesarre akksfnddam
      241 liekfvdtpr hvevqvfgdh hgnavylfer dcsvqrrhqk iieeapapgi dpevrrrlge
      301 aavraakavn yvgagtvefi mdskhnfyfm emntrlqveh pvtemitgtd lvewqlriaa
      361 gekiplsqee iplqghafea riyaedpdnn fmpgagplvh lstpppdmst rietgvrqgd
      421 evsvhydpmi aklvvwasdr qsalsklrys lhqynivglr tnvdfllrls ghsefeagnv
      481 htdfipqhhk dllpthstia kesvcqaalg lilkekemts afklhtqdqf spfsfssgrr
      541 lnisytrnmt lrsgkndiii avtynrdgsy dmqienklfr vlgdlsnedg ytylkssvng
      601 vaskskfill dntiylfsme gsievgipvp kylspvsaeg tqggtiapmt gtiekvfvka
      661 gdrvkagdal mvmiamkmeh tikapkdgri kkvffsegaq anrhaplvef eeeev
//
LOCUS       NP_075247                887 aa            linear   ROD 28-APR-2025
DEFINITION  phosphatidylinositol 3-kinase catalytic subunit type 3 [Rattus
            norvegicus].
ACCESSION   NP_075247
VERSION     NP_075247.1
DBSOURCE    REFSEQ: accession NM_022958.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Li,H., Song,F., Duan,L.R., Sheng,J.J., Xie,Y.H., Yang,Q., Chen,Y.,
            Dong,Q.Q., Zhang,B.L. and Wang,S.W.
  TITLE     Paeonol and danshensu combination attenuates apoptosis in
            myocardial infarcted rats by inhibiting oxidative stress: Roles of
            Nrf2/HO-1 and PI3K/Akt pathway
  JOURNAL   Sci Rep 6, 23693 (2016)
   PUBMED   27021411
  REMARK    GeneRIF: Data show that the cardioprotective effect of paeonol and
            danshensu combination is, at least partly, via activation of
            Nrf2/HO-1 signaling and involvement of the PI3K/Akt cell survival
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Vicinanza,M., Korolchuk,V.I., Ashkenazi,A., Puri,C., Menzies,F.M.,
            Clarke,J.H. and Rubinsztein,D.C.
  TITLE     PI(5)P regulates autophagosome biogenesis
  JOURNAL   Mol Cell 57 (2), 219-234 (2015)
   PUBMED   25578879
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Dowdle,W.E., Nyfeler,B., Nagel,J., Elling,R.A., Liu,S.,
            Triantafellow,E., Menon,S., Wang,Z., Honda,A., Pardee,G.,
            Cantwell,J., Luu,C., Cornella-Taracido,I., Harrington,E.,
            Fekkes,P., Lei,H., Fang,Q., Digan,M.E., Burdick,D., Powers,A.F.,
            Helliwell,S.B., D'Aquin,S., Bastien,J., Wang,H., Wiederschain,D.,
            Kuerth,J., Bergman,P., Schwalb,D., Thomas,J., Ugwonali,S.,
            Harbinski,F., Tallarico,J., Wilson,C.J., Myer,V.E., Porter,J.A.,
            Bussiere,D.E., Finan,P.M., Labow,M.A., Mao,X., Hamann,L.G.,
            Manning,B.D., Valdez,R.A., Nicholson,T., Schirle,M., Knapp,M.S.,
            Keaney,E.P. and Murphy,L.O.
  TITLE     Selective VPS34 inhibitor blocks autophagy and uncovers a role for
            NCOA4 in ferritin degradation and iron homeostasis in vivo
  JOURNAL   Nat Cell Biol 16 (11), 1069-1079 (2014)
   PUBMED   25327288
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Zhu,W., Swaminathan,G. and Plowey,E.D.
  TITLE     GA binding protein augments autophagy via transcriptional
            activation of BECN1-PIK3C3 complex genes
  JOURNAL   Autophagy 10 (9), 1622-1636 (2014)
   PUBMED   25046113
  REMARK    GeneRIF: reveal a novel function of GABP in the regulation of
            autophagy via transcriptional activation of the BECN1-PIK3C3
            complex
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Devereaux,K., Dall'Armi,C., Alcazar-Roman,A., Ogasawara,Y.,
            Zhou,X., Wang,F., Yamamoto,A., De Camilli,P. and Di Paolo,G.
  TITLE     Regulation of mammalian autophagy by class II and III PI 3-kinases
            through PI3P synthesis
  JOURNAL   PLoS One 8 (10), e76405 (2013)
   PUBMED   24098492
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Irani,C., Goncharova,E.A., Hunter,D.S., Walker,C.L.,
            Panettieri,R.A. and Krymskaya,V.P.
  TITLE     Phosphatidylinositol 3-kinase but not tuberin is required for
            PDGF-induced cell migration
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 282 (4), L854-L862 (2002)
   PUBMED   11880313
  REMARK    GeneRIF: Phosphatidylinositol 3-kinase but not tuberin is required
            for PDGF-induced cell migration.
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Tu,V.C., Bahl,J.J. and Chen,Q.M.
  TITLE     Signals of oxidant-induced cardiomyocyte hypertrophy: key
            activation of p70 S6 kinase-1 and phosphoinositide 3-kinase
  JOURNAL   J Pharmacol Exp Ther 300 (3), 1101-1110 (2002)
   PUBMED   11861821
  REMARK    GeneRIF: oxidative stress induces activation of PI3K, which leads
            to p70S6K1 activation and enlargement of cell size
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Campos-Toimil,M., Bagrij,T., Edwardson,J.M. and Thomas,P.
  TITLE     Two modes of secretion in pancreatic acinar cells: involvement of
            phosphatidylinositol 3-kinase and regulation by capacitative Ca(2+)
            entry
  JOURNAL   Curr Biol 12 (3), 211-215 (2002)
   PUBMED   11839273
  REMARK    GeneRIF: secretion in pancreatic acinar cells: involvement of
            phosphatidylinositol 3-kinase
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Carbott,D.E., Duan,L. and Davis,M.A.
  TITLE     Phosphoinositol 3 kinase inhibitor, LY294002 increases bcl-2
            protein and inhibits okadaic acid-induced apoptosis in Bcl-2
            expressing renal epithelial cells
  JOURNAL   Apoptosis 7 (1), 69-76 (2002)
   PUBMED   11773707
  REMARK    GeneRIF: Phosphoinositol 3 kinase inhibitor, LY294002 increases
            bcl-2 protein and inhibits okadaic acid-induced apoptosis in Bcl-2
            expressing renal epithelial cells.
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Row,P.E., Reaves,B.J., Domin,J., Luzio,J.P. and Davidson,H.W.
  TITLE     Overexpression of a rat kinase-deficient phosphoinositide 3-kinase,
            Vps34p, inhibits cathepsin D maturation
  JOURNAL   Biochem J 353 (Pt 3), 655-661 (2001)
   PUBMED   11171063
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061981.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061981.1, AJ006710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132266
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p12"
     Protein         1..887
                     /product="phosphatidylinositol 3-kinase catalytic subunit
                     type 3"
                     /EC_number="2.7.1.137"
                     /note="PI3K type 3; phosphoinositide-3-kinase, class 3;
                     PI3-kinase type 3; ptdIns-3-kinase type 3; catalytic
                     phosphatidylinositol 3-kinase 3; PI-3K Vps34p"
                     /calculated_mol_wt=101404
     Region          26..186
                     /region_name="C2_PI3K_class_III"
                     /note="C2 domain present in class III phosphatidylinositol
                     3-kinases (PI3Ks); cd08397"
                     /db_xref="CDD:176042"
     Region          149..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88763.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q6PF93; propagated from
                     UniProtKB/Swiss-Prot (O88763.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q6PF93; propagated from
                     UniProtKB/Swiss-Prot (O88763.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (O88763.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NEB9; propagated from
                     UniProtKB/Swiss-Prot (O88763.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8NEB9; propagated from
                     UniProtKB/Swiss-Prot (O88763.1)"
     Region          283..503
                     /region_name="PI3Ka_III"
                     /note="Phosphoinositide 3-kinase (PI3K) class III,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, PI3Ks class III...; cd00870"
                     /db_xref="CDD:238442"
     Region          416..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88763.1)"
     Region          539..883
                     /region_name="PI3Kc_III"
                     /note="Catalytic domain of Class III Phosphoinositide
                     3-kinase; cd00896"
                     /db_xref="CDD:270628"
     Region          611..617
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O88763.1)"
     Site            order(612,614..616,618,634,636,639,670,682..685,689,692,
                     748,750,760..761)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270628"
     Region          740..748
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O88763.1)"
     Site            740..748
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270628"
     Region          759..780
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O88763.1)"
     Site            761..780
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270628"
     CDS             1..887
                     /gene="Pik3c3"
                     /coded_by="NM_022958.2:25..2688"
                     /db_xref="GeneID:65052"
                     /db_xref="RGD:620899"
ORIGIN      
        1 mgeaekfhyi yscdldinvq lkigslegkr eqksykavle dpmlkfsgly qetcsdlyvt
       61 cqvfaegkpl alpvrtsykp fstrwnwnew lklpvkypdl prnaqvalti wdvygpgrav
      121 pvggttvslf gkygmfrqgm hdlkvwpnve adgseptrtp grtsstlsed qmsrlakltk
      181 ahrqghmvkv dwldrltfre ieminesekr ssnfmylmve frcvkcddke ygivyyekdg
      241 desspiltsf elvkvpdpqm smenlveskh hklarslrsg psdhdlkpna ttrdqlniiv
      301 sypptkqlty eeqdlvwkfr yyltnqekal tkflkcvnwd lpqeakqale llgkwkpmdv
      361 edslellssh ytnptvrrya varlrqadde dllmyllqlv qalkyenfdd ikngleptkk
      421 dsqasvsesl sssgvssadi dssqiitnpl ppvaspppas kskevsdgen leqdlctfli
      481 sracknstla nylywyvive cedqdtqqrd pkthemylnv mrrfsqallk gdksvrvmrs
      541 llaaqqtfvd rlvhlmkavq resgnrkkkn erlqallgdn ekmnlsdvel iplplepqvk
      601 irgiipetat lfksalmpaq lffktedggk ypvifkhgdd lrqdqlilqi islmdkllrk
      661 enldlkltpy kvlatstkhg fmqfiqsvpv aevldtegsi qnffrkyaps etgpngisae
      721 vmdtyvksca gycvityilg vgdrhldnll ltktgklfhi dfgyilgrdp kplpppmkln
      781 kemvegmggt qseqyqefrk qcytaflhlr rysnlilnlf slmvdanipd ialepdktvk
      841 kvqdkfrldl sdeeavhymq slidesvhal faavveqihk faqywrk
//
LOCUS       NP_620431                262 aa            linear   ROD 28-APR-2025
DEFINITION  WW domain-binding protein 2 [Rattus norvegicus].
ACCESSION   NP_620431
VERSION     NP_620431.1
DBSOURCE    REFSEQ: accession NM_138975.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Buffa,L., Saeed,A.M. and Nawaz,Z.
  TITLE     Molecular mechanism of WW-domain binding protein-2 coactivation
            function in estrogen receptor signaling
  JOURNAL   IUBMB Life 65 (1), 76-84 (2013)
   PUBMED   23233354
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Lim,S.K., Orhant-Prioux,M., Toy,W., Tan,K.Y. and Lim,Y.P.
  TITLE     Tyrosine phosphorylation of transcriptional coactivator WW-domain
            binding protein 2 regulates estrogen receptor alpha function in
            breast cancer via the Wnt pathway
  JOURNAL   FASEB J 25 (9), 3004-3018 (2011)
   PUBMED   21642474
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Dhananjayan,S.C., Ramamoorthy,S., Khan,O.Y., Ismail,A., Sun,J.,
            Slingerland,J., O'Malley,B.W. and Nawaz,Z.
  TITLE     WW domain binding protein-2, an E6-associated protein interacting
            protein, acts as a coactivator of estrogen and progesterone
            receptors
  JOURNAL   Mol Endocrinol 20 (10), 2343-2354 (2006)
   PUBMED   16772533
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Nitsch,R., Di Palma,T., Mascia,A. and Zannini,M.
  TITLE     WBP-2, a WW domain binding protein, interacts with the
            thyroid-specific transcription factor Pax8
  JOURNAL   Biochem J 377 (Pt 3), 553-560 (2004)
   PUBMED   14531730
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Chen,H.I., Einbond,A., Kwak,S.J., Linn,H., Koepf,E., Peterson,S.,
            Kelly,J.W. and Sudol,M.
  TITLE     Characterization of the WW domain of human yes-associated protein
            and its polyproline-containing ligands
  JOURNAL   J Biol Chem 272 (27), 17070-17077 (1997)
   PUBMED   9202023
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF499026.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF499026.1, EV776174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.1"
     Protein         1..262
                     /product="WW domain-binding protein 2"
                     /note="WBP-2"
                     /calculated_mol_wt=28000
     Region          30..131
                     /region_name="PH-GRAM_WBP2"
                     /note="WW binding protein 2 (WB2) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13214"
                     /db_xref="CDD:275401"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q969T9; propagated from
                     UniProtKB/Swiss-Prot (Q8R478.1)"
     Region          196..200
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R478.1)"
     Region          197..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R478.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q969T9; propagated from
                     UniProtKB/Swiss-Prot (Q8R478.1)"
     Region          249..253
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R478.1)"
     CDS             1..262
                     /gene="Wbp2"
                     /coded_by="NM_138975.1:1..789"
                     /db_xref="GeneID:192645"
                     /db_xref="RGD:620032"
ORIGIN      
        1 malnknhseg ggvivnntes ilmsydhvel tfndmknvpe afkgtkkgtv yltpyrvifl
       61 skgkdamrsf mmpfylmkdc evkqpvfgan fikgtvkaea gggwegsasy kltftaggai
      121 efgqqmlqva sqasrgevpn gaygypymps gayvfpppva ngmypcppgy pypppppefy
      181 pgppmmdgam gyvqpppppy pgpmeppvvs gpsapptpaa eakaaeaaas ayynpgnphn
      241 vymptsqppp ppyyppedkk tq
//
LOCUS       NP_067718                896 aa            linear   ROD 28-APR-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_067718
VERSION     NP_067718.1
DBSOURCE    REFSEQ: accession NM_021686.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Zieger,H.L., Kunde,S.A., Rademacher,N., Schmerl,B. and
            Shoichet,S.A.
  TITLE     Disease-associated synaptic scaffold protein CNK2 modulates PSD
            size and influences localisation of the regulatory kinase TNIK
  JOURNAL   Sci Rep 10 (1), 5709 (2020)
   PUBMED   32235845
  REMARK    GeneRIF: Disease-associated synaptic scaffold protein CNK2
            modulates PSD size and influences localisation of the regulatory
            kinase TNIK.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Lim,J., Ritt,D.A., Zhou,M. and Morrison,D.K.
  TITLE     The CNK2 scaffold interacts with vilse and modulates Rac cycling
            during spine morphogenesis in hippocampal neurons
  JOURNAL   Curr Biol 24 (7), 786-792 (2014)
   PUBMED   24656827
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
REFERENCE   6  (residues 1 to 896)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
REFERENCE   7  (residues 1 to 896)
  AUTHORS   Iida,J., Nishimura,W., Yao,I. and Hata,Y.
  TITLE     Synaptic localization of membrane-associated guanylate
            kinase-interacting protein mediated by the pleckstrin homology
            domain
  JOURNAL   Eur J Neurosci 15 (9), 1493-1498 (2002)
   PUBMED   12028359
  REMARK    GeneRIF: MAGUIN-1 and -2 are recruited to synapses by the
            pleckstrin homology domain and that MAGUIN-1 subsequently interacts
            with PSD-95 at synapses.
REFERENCE   8  (residues 1 to 896)
  AUTHORS   Yao,I., Hata,Y., Ide,N., Hirao,K., Deguchi,M., Nishioka,H.,
            Mizoguchi,A. and Takai,Y.
  TITLE     MAGUIN, a novel neuronal membrane-associated guanylate
            kinase-interacting protein
  JOURNAL   J Biol Chem 274 (17), 11889-11896 (1999)
   PUBMED   10207009
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF102854.1 and JAXUCZ010000021.1.
            
            Transcript Variant: This variant (2) has an alternate 3' sequence,
            as compared to variant 1. The resulting isoform (2) has a shorter
            C-terminus, as compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF102854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760433
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq21"
     Protein         1..896
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 2"
                     /note="maguin-1; maguin-2; CNK2; CNK homolog protein 2;
                     connector enhancer of KSR 2; membrane-associated guanylate
                     kinase-interacting protein"
                     /calculated_mol_wt=101532
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          324..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          339..>487
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          480..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Region          559..672
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     Region          682..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9Z1T4.1)"
     CDS             1..896
                     /gene="Cnksr2"
                     /coded_by="NM_021686.3:174..2864"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:59322"
                     /db_xref="RGD:708454"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv vgwqlknlvn alredpsgvi ltlkkrpqsm
      301 ltsapallkn mrwkplalqp liprsptssv atpsstistp tkrdssalqd lyippppaep
      361 yiprdekgnl pcedlrghmv gkpvhkgses pnsfldqeyr krfniveedt vlycyeyekg
      421 rsssqgrres tptygklrpi smpveynwvg dyedpnkmkr dsrrensllr ymsnekiaqe
      481 eymfqrnskk dtgkkskkkg dkstspthys llpslqmdal rqdimgtpvp ettlyhtfqq
      541 sslqhkskkk nkgaiagksk rrisckdlgr gdcegwlwkk kdaksyfsqk wkkywfvlkd
      601 aslywyinee dekaegfisl pefkidrase crkkyafkac hpkiksfyfa aehlddmnrw
      661 lnrinmltag yaererikqe qdywsesdke eadtpstpkq dsppppydty prppsmscas
      721 pyveakhsrl sstetsqsqs sheefrqevt gssavspirk tasqrrswqd lietpltssg
      781 lhylqtlple dsvfsdsaai spehrrqstl ptqkchlqdh ygpyplaese rmqvlngngg
      841 kprsftlprd sgfnhcclna pvsacdpqdd iqppeveeee eeeeeeaage nigeks
//
LOCUS       NP_446429                827 aa            linear   ROD 28-APR-2025
DEFINITION  cadherin-17 precursor [Rattus norvegicus].
ACCESSION   NP_446429
VERSION     NP_446429.1
DBSOURCE    REFSEQ: accession NM_053977.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Bartolome,R.A., Pelaez-Garcia,A., Gomez,I., Torres,S.,
            Fernandez-Acenero,M.J., Escudero-Paniagua,B., Imbaud,J.I. and
            Casal,J.I.
  TITLE     An RGD motif present in cadherin 17 induces integrin activation and
            tumor growth
  JOURNAL   J Biol Chem 289 (50), 34801-34814 (2014)
   PUBMED   25336636
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Ohnishi,K., Melchers,F. and Shimizu,T.
  TITLE     Lymphocyte-expressed BILL-cadherin/cadherin-17 contributes to the
            development of B cells at two stages
  JOURNAL   Eur J Immunol 35 (3), 957-963 (2005)
   PUBMED   15688343
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Takamura,M., Ichida,T., Matsuda,Y., Kobayashi,M., Yamagiwa,S.,
            Genda,T., Shioji,K., Hashimoto,S., Nomoto,M., Hatakeyama,K.,
            Ajioka,Y., Sakamoto,M., Hirohashi,S. and Aoyagi,Y.
  TITLE     Reduced expression of liver-intestine cadherin is associated with
            progression and lymph node metastasis of human colorectal carcinoma
  JOURNAL   Cancer Lett 212 (2), 253-259 (2004)
   PUBMED   15279905
REFERENCE   4  (residues 1 to 827)
  AUTHORS   Wendeler,M.W., Praus,M., Jung,R., Hecking,M., Metzig,C. and
            Gessner,R.
  TITLE     Ksp-cadherin is a functional cell-cell adhesion molecule related to
            LI-cadherin
  JOURNAL   Exp Cell Res 294 (2), 345-355 (2004)
   PUBMED   15023525
REFERENCE   5  (residues 1 to 827)
  AUTHORS   Ohnishi,K., Shimizu,T., Karasuyama,H. and Melchers,F.
  TITLE     The identification of a nonclassical cadherin expressed during B
            cell development and its interaction with surrogate light chain
  JOURNAL   J Biol Chem 275 (40), 31134-31144 (2000)
   PUBMED   10906147
REFERENCE   6  (residues 1 to 827)
  AUTHORS   Erickson,R.H., Gum,J.R. Jr., Lindstrom,M.M., McKean,D. and Kim,Y.S.
  TITLE     Regional expression and dietary regulation of rat small intestinal
            peptide and amino acid transporter mRNAs
  JOURNAL   Biochem Biophys Res Commun 216 (1), 249-257 (1995)
   PUBMED   7488096
REFERENCE   7  (residues 1 to 827)
  AUTHORS   Berndorff,D., Gessner,R., Kreft,B., Schnoy,N., Lajous-Petter,A.M.,
            Loch,N., Reutter,W., Hortsch,M. and Tauber,R.
  TITLE     Liver-intestine cadherin: molecular cloning and characterization of
            a novel Ca(2+)-dependent cell adhesion molecule expressed in liver
            and intestine
  JOURNAL   J Cell Biol 125 (6), 1353-1369 (1994)
   PUBMED   8207063
REFERENCE   8  (residues 1 to 827)
  AUTHORS   Dantzig,A.H., Hoskins,J.A., Tabas,L.B., Bright,S., Shepard,R.L.,
            Jenkins,I.L., Duckworth,D.C., Sportsman,J.R., Mackensen,D.,
            Rosteck,P.R. Jr. et al.
  TITLE     Association of intestinal peptide transport with a protein related
            to the cadherin superfamily
  JOURNAL   Science 264 (5157), 430-433 (1994)
   PUBMED   8153632
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X78997.1 and JAXUCZ010000005.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643288.21495.1,
                                           SRR26643286.15827.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q13"
     Protein         1..827
                     /product="cadherin-17 precursor"
                     /note="LI-cadherin; liver-intestine cadherin"
                     /calculated_mol_wt=89566
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2315
     mat_peptide     22..827
                     /product="Cadherin-17. /id=PRO_0000003814"
                     /note="propagated from UniProtKB/Swiss-Prot (P55281.1)"
                     /calculated_mol_wt=89566
     Region          32..121
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(39..40,84,86,117,119..120)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          130..233
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Region          244..335
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(248..249,298,300,331,333..334)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Region          345..443
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(350..351,410,412,440,442..443)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Region          457..561
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(460..461,519,521,558,560..561)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Region          569..662
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            573
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Site            order(576..577,625,627,658,660..661)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55281.1)"
     Site            787..807
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55281.1)"
     CDS             1..827
                     /gene="Cdh17"
                     /coded_by="NM_053977.2:106..2589"
                     /db_xref="GeneID:117048"
                     /db_xref="RGD:619748"
ORIGIN      
        1 mvsaqlhflc lltlyltgay gqegkfsgpl kpmtfsifeg qepsqiifqf kanppavtfe
       61 ltgetdgifk iekdgllyht rvldretrav hhlqlaalds qgaivdgpvp iiievkdind
      121 nrptflqtky egsvrqnsrp gkpfmyvnat dlddpatpng qlfyqiviql pkinnvmyfq
      181 idnktgaisl tpegsqvldp iknpyynlvv svkdmggqne nsfsdttsvd itvreniwka
      241 pepveirenl tdphpikitq vqwndpgahy slinkeklpq fpfsidqegn iyvtqpldre
      301 ekdshvffat akdengkpla ypleirvkvi dindnpptcl sqvtvfevqe nevlgssigi
      361 faahdmdean ninsilkyrl vdqtpkvpsd elflideygg kvqlgkrslk kqdspqynlt
      421 vevsdidfkt lcslqvnvid indqipifer sdygsktlse dtaigstili iqatdddepf
      481 tgsskilyki vqgdtegrle vvtdpmtntg yvkirkpldf etepvtsivf kaenpeplvn
      541 gieynassfa sfeltvtdvn evpvfpqqif qanvsedtai gtkvgtvtar dpegltvsys
      601 lkdnkrgwlk idsvtgdifs tapldretes vyrvqvvate vggsslssta yfhlvlmdvn
      661 dnpprlakdy tglffchpls apgslifeat dddqqsvrrp kftfalgres lqsdwevski
      721 ngtharlstk htrfeeqvyd ipilindggq ppmegivsls vtfcqcvdgs cfrpagnqvg
      781 iptvgmavgi llttflvigi ilavvfirmr kdkvedpqsp enkplrs
//
LOCUS       NP_036891                843 aa            linear   ROD 28-APR-2025
DEFINITION  proto-oncogene vav [Rattus norvegicus].
ACCESSION   NP_036891
VERSION     NP_036891.2
DBSOURCE    REFSEQ: accession NM_012759.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Wang,Q., Gong,L., Mao,S., Yao,C., Liu,M., Wang,Y., Yang,J., Yu,B.,
            Chen,G. and Gu,X.
  TITLE     Klf2-Vav1-Rac1 axis promotes axon regeneration after peripheral
            nerve injury
  JOURNAL   Exp Neurol 343, 113788 (2021)
   PUBMED   34147481
  REMARK    GeneRIF: Klf2-Vav1-Rac1 axis promotes axon regeneration after
            peripheral nerve injury.
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Pedros,C., Gaud,G., Bernard,I., Kassem,S., Chabod,M., Lagrange,D.,
            Andreoletti,O., Dejean,A.S., Lesourne,R., Fournie,G.J. and
            Saoudi,A.
  TITLE     An Epistatic Interaction between Themis1 and Vav1 Modulates
            Regulatory T Cell Function and Inflammatory Bowel Disease
            Development
  JOURNAL   J Immunol 195 (4), 1608-1616 (2015)
   PUBMED   26163585
  REMARK    GeneRIF: these results highlight the importance of the signaling
            pathway involving epistasis between Themis1 and Vav1 in the control
            of Treg suppressive function and susceptibility to IBD development.
REFERENCE   3  (residues 1 to 843)
  AUTHORS   Liang,Y., Cucchetti,M., Roncagalli,R., Yokosuka,T., Malzac,A.,
            Bertosio,E., Imbert,J., Nijman,I.J., Suchanek,M., Saito,T.,
            Wulfing,C., Malissen,B. and Malissen,M.
  TITLE     The lymphoid lineage-specific actin-uncapping protein Rltpr is
            essential for costimulation via CD28 and the development of
            regulatory T cells
  JOURNAL   Nat Immunol 14 (8), 858-866 (2013)
   PUBMED   23793062
REFERENCE   4  (residues 1 to 843)
  AUTHORS   Valderrama,F., Thevapala,S. and Ridley,A.J.
  TITLE     Radixin regulates cell migration and cell-cell adhesion through
            Rac1
  JOURNAL   J Cell Sci 125 (Pt 14), 3310-3319 (2012)
   PUBMED   22467863
REFERENCE   5  (residues 1 to 843)
  AUTHORS   Lawson,C.D., Donald,S., Anderson,K.E., Patton,D.T. and Welch,H.C.
  TITLE     P-Rex1 and Vav1 cooperate in the regulation of
            formyl-methionyl-leucyl-phenylalanine-dependent neutrophil
            responses
  JOURNAL   J Immunol 186 (3), 1467-1476 (2011)
   PUBMED   21178006
REFERENCE   6  (residues 1 to 843)
  AUTHORS   Song,J.S., Haleem-Smith,H., Arudchandran,R., Gomez,J., Scott,P.M.,
            Mill,J.F., Tan,T.H. and Rivera,J.
  TITLE     Tyrosine phosphorylation of Vav stimulates IL-6 production in mast
            cells by a Rac/c-Jun N-terminal kinase-dependent pathway
  JOURNAL   J Immunol 163 (2), 802-810 (1999)
   PUBMED   10395673
REFERENCE   7  (residues 1 to 843)
  AUTHORS   Bieg,S.
  TITLE     Differential expression of p95vav in primary lymphoid tissue of BB
            rats congenic for the lymphopenia gene
  JOURNAL   Autoimmunity 30 (1), 37-42 (1999)
   PUBMED   10433093
REFERENCE   8  (residues 1 to 843)
  AUTHORS   Crespo,P., Schuebel,K.E., Ostrom,A.A., Gutkind,J.S. and
            Bustelo,X.R.
  TITLE     Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by
            the vav proto-oncogene product
  JOURNAL   Nature 385 (6612), 169-172 (1997)
   PUBMED   8990121
REFERENCE   9  (residues 1 to 843)
  AUTHORS   Margolis,B., Hu,P., Katzav,S., Li,W., Oliver,J.M., Ullrich,A.,
            Weiss,A. and Schlessinger,J.
  TITLE     Tyrosine phosphorylation of vav proto-oncogene product containing
            SH2 domain and transcription factor motifs
  JOURNAL   Nature 356 (6364), 71-74 (1992)
   PUBMED   1531699
REFERENCE   10 (residues 1 to 843)
  AUTHORS   Hernandez,L., Petropoulos,C.J., Hughes,S.H. and Lijinsky,W.
  TITLE     DNA methylation and oncogene expression in methapyrilene-induced
            rat liver tumors and in treated hepatocytes in culture
  JOURNAL   Mol Carcinog 4 (3), 203-209 (1991)
   PUBMED   2064726
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC091160.1.
            
            On Dec 11, 2007 this sequence version replaced NP_036891.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091160.1, U39476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q11"
     Protein         1..843
                     /product="proto-oncogene vav"
                     /note="p95; vav 1 oncogene; vav 1 guanine nucleotide
                     exchange factor"
                     /calculated_mol_wt=97840
     Region          2..121
                     /region_name="CH_VAV1"
                     /note="calponin homology (CH) domain found in VAV1
                     protein; cd21262"
                     /db_xref="CDD:409111"
     Site            order(3,7,70,72..73,76..77,79,90..98,104,106..107,
                     109..110,113..114,117)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409111"
     Region          195..371
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(201,205,295,323..324,327..328,330..331,334..335,
                     338..339,342,367,371)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          385..508
                     /region_name="PH_Vav"
                     /note="Vav pleckstrin homology (PH) domain; cd01223"
                     /db_xref="CDD:269930"
     Region          510..566
                     /region_name="C1_VAV1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in VAV1 protein; cd20867"
                     /db_xref="CDD:410417"
     Region          594..656
                     /region_name="SH3_VAV1_1"
                     /note="First Src homology 3 domain of VAV1 protein;
                     cd11979"
                     /db_xref="CDD:212912"
     Site            order(599,601,604,614,633..634,649,651..652)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212912"
     Region          663..765
                     /region_name="SH2_Vav1"
                     /note="Src homology 2 (SH2) domain found in the Vav1
                     proteins; cd10405"
                     /db_xref="CDD:198268"
     Site            order(676,694,715,717)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198268"
     Site            order(716,743)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198268"
     Region          784..837
                     /region_name="SH3_VAV1_2"
                     /note="C-terminal (or second) Src homology 3 domain of
                     VAV1 protein; cd11976"
                     /db_xref="CDD:212909"
     Site            order(789,791,794,798,817..818,831,833..834)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212909"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P15498; propagated from
                     UniProtKB/Swiss-Prot (P54100.1)"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P27870; propagated from
                     UniProtKB/Swiss-Prot (P54100.1)"
     CDS             1..843
                     /gene="Vav1"
                     /gene_synonym="Vav"
                     /coded_by="NM_012759.2:58..2589"
                     /db_xref="GeneID:25156"
                     /db_xref="RGD:3951"
ORIGIN      
        1 melwrqcthw liqcrvlpps hrvtwegaqv celaqalrdg vllcqllnnl lphainlrev
       61 nlwpqmsqfl clknirtfls tccekfglkr selfeafdlf dvqdfgkviy tlsalswtpi
      121 aqnkgimpfp tedsalgded iysglsdqid dtaeededly dcveneeaeg deiyedlmrs
      181 esvptppkmt eydkrccclr eiqqteekyt dtlgsiqqhf mkplqrflkp qdmetifvni
      241 eellsvhthf lkelkdalsg pgatmlyqvf ikykerflvy grycsqvesa skhldqvata
      301 redvqmklee csqranngrf tlrdllmvpm qrvlkyhlll qelvkhtqdt tekenlrlal
      361 damrdlaqcv nevkrdnetl rqitnfqlsi enldqslany grpkidgelk itsverrskt
      421 dryaflldka llickrrgds ydlkasvnlh sfqvrddssg erdnkkwshm flliedqgaq
      481 gyelffktre lkkkwmeqfe maisniypen atanghdfqm fsfeettsck acqmllrgtf
      541 yqgyrcyrcr apahkeclgr vppcgrqdfs gtmkkdklhr raqdkkrnel glpkmevcqe
      601 yygippppga fgpflrlnpg diveltkaea ehnwwegrnt atnevgwfpc nrvrpyvhgp
      661 pqdlsvhlwy agpmeragae giltnrsdgt ylvrqrvkdt aefaisikyn vevkhikimt
      721 seglyritek kafrglpelv efyqqnslkd cfksldttlq fpykeperra inkppvgstk
      781 yfgtakaryd fcardrsels lkegdiikil nkkgqqgwwr geiygrigwf psnyveedys
      841 eyc
//
LOCUS       NP_446246               2126 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein kinase WNK1 isoform 3 [Rattus norvegicus].
ACCESSION   NP_446246
VERSION     NP_446246.2
DBSOURCE    REFSEQ: accession NM_053794.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2126)
  AUTHORS   Boyd-Shiwarski,C.R., Shiwarski,D.J., Griffiths,S.E., Beacham,R.T.,
            Norrell,L., Morrison,D.E., Wang,J., Mann,J., Tennant,W.,
            Anderson,E.N., Franks,J., Calderon,M., Connolly,K.A., Cheema,M.U.,
            Weaver,C.J., Nkashama,L.J., Weckerly,C.C., Querry,K.E.,
            Pandey,U.B., Donnelly,C.J., Sun,D., Rodan,A.R. and Subramanya,A.R.
  TITLE     WNK kinases sense molecular crowding and rescue cell volume via
            phase separation
  JOURNAL   Cell 185 (24), 4488-4506 (2022)
   PUBMED   36318922
REFERENCE   2  (residues 1 to 2126)
  AUTHORS   Akella,R., Humphreys,J.M., Sekulski,K., He,H., Durbacz,M.,
            Chakravarthy,S., Liwocha,J., Mohammed,Z.J., Brautigam,C.A. and
            Goldsmith,E.J.
  TITLE     Osmosensing by WNK Kinases
  JOURNAL   Mol Biol Cell 32 (18), 1614-1623 (2021)
   PUBMED   33689398
  REMARK    GeneRIF: Osmosensing by WNK Kinases.
REFERENCE   3  (residues 1 to 2126)
  AUTHORS   Akella,R., Drozdz,M.A., Humphreys,J.M., Jiou,J., Durbacz,M.Z.,
            Mohammed,Z.J., He,H., Liwocha,J., Sekulski,K. and Goldsmith,E.J.
  TITLE     A Phosphorylated Intermediate in the Activation of WNK Kinases
  JOURNAL   Biochemistry 59 (18), 1747-1755 (2020)
   PUBMED   32314908
  REMARK    GeneRIF: A Phosphorylated Intermediate in the Activation of WNK
            Kinases.
REFERENCE   4  (residues 1 to 2126)
  AUTHORS   Kim,Y., Jun,I., Shin,D.H., Yoon,J.G., Piao,H., Jung,J., Park,H.W.,
            Cheng,M.H., Bahar,I., Whitcomb,D.C. and Lee,M.G.
  TITLE     Regulation of CFTR Bicarbonate Channel Activity by WNK1:
            Implications for Pancreatitis and CFTR-Related Disorders
  JOURNAL   Cell Mol Gastroenterol Hepatol 9 (1), 79-103 (2020)
   PUBMED   31561038
  REMARK    GeneRIF: Regulation of CFTR Bicarbonate Channel Activity by WNK1:
            Implications for Pancreatitis and CFTR-Related Disorders.
REFERENCE   5  (residues 1 to 2126)
  AUTHORS   Gao,J.L., Peng,K., Shen,M.W., Hou,Y.H., Qian,X.B., Meng,X.W.,
            Ji,F.H., Wang,L.N. and Yang,J.P.
  TITLE     Suppression of WNK1-SPAK/OSR1 Attenuates Bone Cancer Pain by
            Regulating NKCC1 and KCC2
  JOURNAL   J Pain 20 (12), 1416-1428 (2019)
   PUBMED   31085334
  REMARK    GeneRIF: Suppression of WNK1-SPAK/OSR1 Attenuates Bone Cancer Pain
            by Regulating NKCC1 and KCC2.
REFERENCE   6  (residues 1 to 2126)
  AUTHORS   Yang,C.L., Angell,J., Mitchell,R. and Ellison,D.H.
  TITLE     WNK kinases regulate thiazide-sensitive Na-Cl cotransport
  JOURNAL   J Clin Invest 111 (7), 1039-1045 (2003)
   PUBMED   12671053
  REMARK    GeneRIF: WNK1 has a role in the sodium regulatory pathway of the
            distal
REFERENCE   7  (residues 1 to 2126)
  AUTHORS   Xu,B.E., Min,X., Stippec,S., Lee,B.H., Goldsmith,E.J. and Cobb,M.H.
  TITLE     Regulation of WNK1 by an autoinhibitory domain and
            autophosphorylation
  JOURNAL   J Biol Chem 277 (50), 48456-48462 (2002)
   PUBMED   12374799
REFERENCE   8  (residues 1 to 2126)
  AUTHORS   Wilson,F.H., Disse-Nicodeme,S., Choate,K.A., Ishikawa,K.,
            Nelson-Williams,C., Desitter,I., Gunel,M., Milford,D.V.,
            Lipkin,G.W., Achard,J.M., Feely,M.P., Dussol,B., Berland,Y.,
            Unwin,R.J., Mayan,H., Simon,D.B., Farfel,Z., Jeunemaitre,X. and
            Lifton,R.P.
  TITLE     Human hypertension caused by mutations in WNK kinases
  JOURNAL   Science 293 (5532), 1107-1112 (2001)
   PUBMED   11498583
REFERENCE   9  (residues 1 to 2126)
  AUTHORS   Xu,B., English,J.M., Wilsbacher,J.L., Stippec,S., Goldsmith,E.J.
            and Cobb,M.H.
  TITLE     WNK1, a novel mammalian serine/threonine protein kinase lacking the
            catalytic lysine in subdomain II
  JOURNAL   J Biol Chem 275 (22), 16795-16801 (2000)
   PUBMED   10828064
REFERENCE   10 (residues 1 to 2126)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF227741.1 and JAXUCZ010000004.1.
            
            On Nov 20, 2010 this sequence version replaced NP_446246.1.
            
            Transcript Variant: This variant (3) has multiple differences in
            the coding region but maintains the reading frame compared to
            variant 1. The resulting protein (isoform 3) is shorter but has the
            same N- and C-termini compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF227741.1, SRR26360194.2246776.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2126
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..2126
                     /product="serine/threonine-protein kinase WNK1 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="protein kinase with no lysine 1"
                     /calculated_mol_wt=224982
     Region          1..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16081417; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          93..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          195..483
                     /region_name="STKc_WNK1"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 1; cd14030"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,310,349,
                     351,353..354,356,368,371,385..388)
                     /site_type="active"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,349,351,
                     353..354,356,368)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270932"
     Site            order(231,308,310,349,351,353,371,385..388)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270932"
     Site            367..388
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270932"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12374799; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12374799,
                     ECO:0000269|PubMed:22544747; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          488..555
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000269|PubMed:12374799"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          500..563
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          573..865
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          629..639
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1003..1006
                     /region_name="RFXV motif 1.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          <1320..1608
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1474..1507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1557..1595
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1604..1607
                     /region_name="RFXV motif 2.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1610..1695
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1690..1693
                     /region_name="RFXV motif 3.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1702..1705
                     /region_name="RFXV motif 4.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1709..1783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1755
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1856..1940
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            1865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1952..1990
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          1985..2005
                     /region_name="Amphipathic alpha-helix.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            2014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83741; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            2030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83741; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Region          2076..2097
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            2114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     Site            2116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H4A3; propagated from
                     UniProtKB/Swiss-Prot (Q9JIH7.2)"
     CDS             1..2126
                     /gene="Wnk1"
                     /gene_synonym="Hsn2; Prkwnk1"
                     /coded_by="NM_053794.2:166..6546"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:116477"
                     /db_xref="RGD:621141"
ORIGIN      
        1 msdgtaekqs gtpgflsppa pvpkngsssd ssvgeklgaa vadsgigrte eyrrrrhtmd
       61 kdsrgaaatt tptehrffrr svicdsnata lelpglplsi pqpsvpavvp qsappephre
      121 etltatvasq vsqqpsaaas pgeqavvgsa tatvpsstsk drpvsqpslv gskeepppsr
      181 sgsgsggasa kepqeernqq qddieeletk avgmsndgrf lkfdieigrg sfktvykgld
      241 tettvevawc elqdrkltks erqrfkeeae mlkglqhpni vrfydswest vkgkkcivlv
      301 telmtsgtlk tylkrfkvmk ikvlrswcrq ilkglqflht rtppiihrdl kcdnifitgp
      361 tgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd esvdvyafgm cmlematsey
      421 pysecqnaaq iyrrvtsgvk pasfdkvaip evkeiiegci rqnkderysi kdllnhaffq
      481 eetgvrvela eeddgekiai klwlriedik klkgkykdne aiefsfdler dvpedvaqem
      541 vesgyvcegd hktmakaikd rvslikrkre qrqlvreeqe krkqeessfk qqneqqasvs
      601 qagiqplsva stgiptaptt sasvstqvep eepeadqhqq lqyqqpsisv lsdgtvdsgq
      661 gssvftesrv ssqqtvsygs qheqahsigt apghtvssiq aqsqphgvyp pssmaqgqnq
      721 gqpssslagv lssqpvqhpq qqgiqptvpp qqavqyslpq aasssegtvq pvsqpqvsag
      781 tqsstqgvsq aappeqtpit qsqptqpvpl vssvdsahsd vasgmsdgne napsssgrhe
      841 grttkrhyrk svrsrsrhek tsrpklriln vsnkgdrvve cqlethnrkm vtfkfdldgd
      901 npeeiatimv nndfilaier esfvaqvrei iekademlse dvsvepegdq gleslqgkdd
      961 ygfpgsqkle gefkqpiavs smpqqigvpt ssltqvvhsa grrfivspvp esrlreskif
     1021 tseipdpvaa stsqgpgmnl shsasslslq qafselkhgq mtegpntapp nfnhpgptfs
     1081 pfltsiagvq tvaastpsvs vpitssplnd istsvmqseg alptdkgigg vttstgvvas
     1141 gglttlsvse tptlssavss stapavvtvs ttsqpvqast sgsiasstgs fpsgtfsttt
     1201 gttvssvavp nakpptvllq qvagntagva ivtsvstttp fpamasqpsl plgsstsapt
     1261 laetvvvsah sldkashsst aglglsfcap ssssssgtav sssvsqpgiv hplvissaia
     1321 stpvlpqpav ptstpllpqv pnipplvqpv anvpavqqtl ihsqpqpall pnqphthcpe
     1381 mdadtqskap giddiktlee klrslfsehs ssgtqhasvs letplvvetv tpgipttava
     1441 psklmtstts tclpptnlpl gtagmpvmpv gtpgqvstpg thasapasta tgakpgttpp
     1501 kpsltktvvp pvgtelsagt vpceqlppfp gpsliqtqqp ledldaqlrr tlspetipvt
     1561 pavgplstms stavteagsq pqkdgtevhv tasssgagvv kmgrfqvsvt mddaqkerkn
     1621 rsedtksvhf esstsessvl sssspestlv kpepngitvs gisldvpdst hrtptpeaks
     1681 etgqptkvgr fqvtttankv grfsvsrted kvtelkkegp vtspfrdseq tvipaaipkk
     1741 ekpelaepsh lngpssdlea aflsrggedg sgsphspphl cskslpiqtl sqslsnsfns
     1801 symssdnesd iededlrlel rrlrekhlke iqdlqsrqkh eieslytklg kvppaviipp
     1861 aaplsgrrrr ptkskgskss rssslgnksp qlsgnlsgqs gtsvlnpqqt lhppgntpet
     1921 ghnqllqplk pspssdnlys aftsdgaisv pslsapgqgt sstntvggtv ssqaaqaqpp
     1981 amtssrkgtf tddlhklvdn wardamnlsg rrgskghmny egpgmarkfs apgqlcismt
     2041 snmggstpis aasatslghf tksmcppqqy gfpaapfgtq wsgtggpapq plgqfqpvgt
     2101 tslqnfnisn lqksisnppg snlrtt
//
LOCUS       NP_001007623             349 aa            linear   ROD 28-APR-2025
DEFINITION  PDZ and LIM domain protein 2 [Rattus norvegicus].
ACCESSION   NP_001007623 XP_214229
VERSION     NP_001007623.1
DBSOURCE    REFSEQ: accession NM_001007622.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Torrado,M., Senatorov,V.V., Trivedi,R., Fariss,R.N. and
            Tomarev,S.I.
  TITLE     Pdlim2, a novel PDZ-LIM domain protein, interacts with
            alpha-actinins and filamin A
  JOURNAL   Invest Ophthalmol Vis Sci 45 (11), 3955-3963 (2004)
   PUBMED   15505042
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079091.1.
            
            On Nov 29, 2004 this sequence version replaced XP_214229.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079091.1, AY531526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p11"
     Protein         1..349
                     /product="PDZ and LIM domain protein 2"
                     /note="alpha-actinins and filamin-interacting protein"
                     /calculated_mol_wt=37449
     Region          4..82
                     /region_name="PDZ_PDLIM-like"
                     /note="PDZ domain of PDZ-LIM family proteins, and related
                     domains; cd06753"
                     /db_xref="CDD:467235"
     Site            order(12..18,30,33,62,66,69..70)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467235"
     Region          72..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Region          108..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96JY6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96JY6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96JY6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96JY6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Region          168..212
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Region          <198..252
                     /region_name="DUF4749"
                     /note="Domain of unknown function (DUF4749); pfam15936"
                     /db_xref="CDD:464948"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1G6; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Region          250..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AYD6.1)"
     Region          283..335
                     /region_name="LIM_Mystique"
                     /note="The LIM domain of Mystique, a subfamily of ALP LIM
                     domain proteins; cd09449"
                     /db_xref="CDD:188833"
     Site            order(283,286,304,307,310,313,331,334)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188833"
     CDS             1..349
                     /gene="Pdlim2"
                     /coded_by="NM_001007622.1:120..1169"
                     /db_xref="GeneID:290354"
                     /db_xref="RGD:1359203"
ORIGIN      
        1 maltvnvvgp apwgfrisgg rdfhtpiivt kvtergkaea adlrpgdiiv aingesaesm
       61 lhaeaqskir qsasplrlql drsqtaspgq ingegsldml atrfqgslrt hhnsqssqrs
      121 acfspaslsp rpdspfstpp ptspialsge nvigcsfqsl thspglaath hltypgqpts
      181 qqaghsspsd stvrvllhsp grpssprlss ldleedsevf kmlqenrqgr aaprqsssfr
      241 llqealeaee rggtpafvps slspkaslpt sralatppkl htcekcsvni snqavriqeg
      301 ryrhpgcytc adcglnlkmr ghfwvgnely cekharqrys mpgtlssqa
//
LOCUS       NP_001013058             593 aa            linear   ROD 28-APR-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 9 [Rattus
            norvegicus].
ACCESSION   NP_001013058 XP_236280
VERSION     NP_001013058.1
DBSOURCE    REFSEQ: accession NM_001013040.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Zhang,D., Marlin,M.C., Liang,Z., Ahmad,M., Ashpole,N.M.,
            Sonntag,W.E., Zhao,Z.J. and Li,G.
  TITLE     The Protein Tyrosine Phosphatase MEG2 Regulates the Transport and
            Signal Transduction of Tropomyosin Receptor Kinase A
  JOURNAL   J Biol Chem 291 (46), 23895-23905 (2016)
   PUBMED   27655914
  REMARK    GeneRIF: As a result, overexpression of PTP-MEG2 down-regulates
            NGF/TrkA signaling and blocks neurite outgrowth and differentiation
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Barr,A.J., Ugochukwu,E., Lee,W.H., King,O.N., Filippakopoulos,P.,
            Alfano,I., Savitsky,P., Burgess-Brown,N.A., Muller,S. and Knapp,S.
  TITLE     Large-scale structural analysis of the classical human protein
            tyrosine phosphatome
  JOURNAL   Cell 136 (2), 352-363 (2009)
   PUBMED   19167335
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Wang,X., Huynh,H., Gjorloff-Wingren,A., Monosov,E., Stridsberg,M.,
            Fukuda,M. and Mustelin,T.
  TITLE     Enlargement of secretory vesicles by protein tyrosine phosphatase
            PTP-MEG2 in rat basophilic leukemia mast cells and Jurkat T cells
  JOURNAL   J Immunol 168 (9), 4612-4619 (2002)
   PUBMED   11971009
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082041.1.
            
            On Apr 20, 2005 this sequence version replaced XP_236280.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..593
                     /product="tyrosine-protein phosphatase non-receptor type
                     9"
                     /EC_number="3.1.3.48"
                     /calculated_mol_wt=67831
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q641Z2.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P43378; propagated from
                     UniProtKB/Swiss-Prot (Q641Z2.1)"
     Region          20..66
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          90..238
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     Region          299..569
                     /region_name="PTPc-N9"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 9; cd14543"
                     /db_xref="CDD:350391"
     CDS             1..593
                     /gene="Ptpn9"
                     /gene_synonym="Meg2"
                     /coded_by="NM_001013040.1:23..1804"
                     /db_xref="GeneID:266611"
                     /db_xref="RGD:628726"
ORIGIN      
        1 mepataprpd mapeltpeee qatkqfleei nkwtvqynvs plswnvavkf lmarkfdvlr
       61 avelfhcyre trrkegivkl kpheeplrse ilsgkftiln vrdptgasia lftarlhhph
      121 ksvqhvvlqa lfylldravd sfetqrnglv fiydmcgsny anfeldlgkk vlnllkgafp
      181 arlkkvlivg apiwfrvpys iislllkdkv reriqilkts evtqhlprec lpenlggyik
      241 idlatwnfqf lpqvnghpdp fdeiilfslp paldwdsvhv pgphamtiqe lvdyvntrqk
      301 qgiyeeyedi rrenpvgtfh csmspgnlek nrygdvpcld qtrvkltkrs ghtqtdyina
      361 sfmdgykqkn ayigtqgple ntyrdfwlmv weqkvlvivm ttrfeeggrr kcgqywplek
      421 dsriqfgflt vtnlgvenmn hykkttleih nteerqkrqv thfqflswpd ygvpssaasl
      481 idflrvvrsq qsmavgslga rskgqcpepp ivvhcsagig rtgtfcsldi claqleelgt
      541 lnvfqtvsrm rtqrafsiqt peqyyfcyka ilefaeregm vpsghsllam dgq
//
LOCUS       NP_001258130             194 aa            linear   ROD 28-APR-2025
DEFINITION  four and a half LIM domains protein 1 isoform 4 [Rattus
            norvegicus].
ACCESSION   NP_001258130
VERSION     NP_001258130.1
DBSOURCE    REFSEQ: accession NM_001271201.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Li,Y., Pu,G., Chen,C. and Yang,L.
  TITLE     Inhibition of FHL1 inhibits cigarette smoke extract-induced
            proliferation in pulmonary arterial smooth muscle cells
  JOURNAL   Mol Med Rep 12 (3), 3801-3808 (2015)
   PUBMED   25975448
  REMARK    GeneRIF: FHL1 may be involved in excessive cell proliferation and
            may represent a potential therapeutic target for pulmonary
            hypertension.
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Wang,L., Miao,J., Li,L., Wu,D., Zhang,Y., Peng,Z., Zhang,L.,
            Yuan,Z. and Sun,K.
  TITLE     Identification of an FHL1 protein complex containing gamma-actin
            and non-muscle myosin IIB by analysis of protein-protein
            interactions
  JOURNAL   PLoS One 8 (11), e79551 (2013)
   PUBMED   24265776
  REMARK    GeneRIF: FHL1 exists as part of a complex, which binds gamma-actin
            and non-muscle myosin IIB
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Yue,J., Guan,J., Wang,X., Zhang,L., Yang,Z., Ao,Q., Deng,Y., Zhu,P.
            and Wang,G.
  TITLE     MicroRNA-206 is involved in hypoxia-induced pulmonary hypertension
            through targeting of the HIF-1alpha/Fhl-1 pathway
  JOURNAL   Lab Invest 93 (7), 748-759 (2013)
   PUBMED   23628900
  REMARK    GeneRIF: Hypoxia-induced downregulation of miR-206 promotes
            pulmonary hypertension by targeting the HIF-1alpha/Fhl-1 pathway in
            pulmonary artery smooth muscle cells.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Niu,C., Liang,C., Guo,J., Cheng,L., Zhang,H., Qin,X., Zhang,Q.,
            Ding,L., Yuan,B., Xu,X., Li,J., Lin,J. and Ye,Q.
  TITLE     Downregulation and growth inhibitory role of FHL1 in lung cancer
  JOURNAL   Int J Cancer 130 (11), 2549-2556 (2012)
   PUBMED   21702045
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Wang,L.L., Qiu,G.R., Fu,W.N., Yuan,Z.W. and Sun,K.L.
  TITLE     Transcriptional regulation of Fhl1 by estradiol in rat
            myoblastocytes
  JOURNAL   Steroids 75 (4-5), 368-372 (2010)
   PUBMED   20149813
  REMARK    GeneRIF: These data indicate that estradiol down-regulates Fhl1
            expression through its binding to the ERbeta.
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Chen,C.N., Ferrington,D.A. and Thompson,L.V.
  TITLE     Carbonic anhydrase III and four-and-a-half LIM protein 1 are
            preferentially oxidized with muscle unloading
  JOURNAL   J Appl Physiol (1985) 105 (5), 1554-1561 (2008)
   PUBMED   18756007
  REMARK    GeneRIF: Carbonic anhydrase III and four-and-a-half LIM protein 1
            are preferentially oxidized with muscle unloading.
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Yang,Z., Browning,C.F., Hallaq,H., Yermalitskaya,L., Esker,J.,
            Hall,M.R., Link,A.J., Ham,A.J., McGrath,M.J., Mitchell,C.A. and
            Murray,K.T.
  TITLE     Four and a half LIM protein 1: a partner for KCNA5 in human atrium
  JOURNAL   Cardiovasc Res 78 (3), 449-457 (2008)
   PUBMED   18281375
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Kang,M.A., Jeoung,N.H., Kim,J.Y., Lee,J.E., Jung,U.J., Choi,M.S.,
            Lee,W.H., Kwon,O.S., Lee,H. and Park,Y.B.
  TITLE     Up-regulation of skeletal muscle LIM protein 1 gene by
            25-hydroxycholesterol may mediate morphological changes of rat
            aortic smooth muscle cells
  JOURNAL   Life Sci 80 (5), 460-467 (2007)
   PUBMED   17161435
  REMARK    GeneRIF: Over-production of SLIM1 in the cells resulted in a change
            in the cell-shape into a spindle-like form.
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Lim,D.S., Roberts,R. and Marian,A.J.
  TITLE     Expression profiling of cardiac genes in human hypertrophic
            cardiomyopathy: insight into the pathogenesis of phenotypes
  JOURNAL   J Am Coll Cardiol 38 (4), 1175-1180 (2001)
   PUBMED   11583900
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM042472.1, BC061782.1 and CK840296.1.
            
            Transcript Variant: This variant (5) contains an alternate exon at
            the 5' end and lacks an exon in the 3' coding region compared to
            variant 1, which results in an isoform (4) with a shorter
            N-terminus and a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FM042472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..194
                     /product="four and a half LIM domains protein 1 isoform 4"
                     /note="four and a half LIM domains protein 1; skeletal
                     muscle LIM-protein 1; FHL-1"
                     /calculated_mol_wt=21895
     Region          <5..33
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cl02475"
                     /db_xref="CDD:413332"
     Region          40..93
                     /region_name="LIM1_FHL1"
                     /note="The first LIM domain of Four and a half LIM domains
                     protein 1; cd09344"
                     /db_xref="CDD:188730"
     Site            order(40,43,62,65,68,71,89,92)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188730"
     Region          101..158
                     /region_name="LIM2_FHL1"
                     /note="The second LIM domain of Four and a half LIM
                     domains protein 1 (FHL1); cd09424"
                     /db_xref="CDD:188808"
     Site            order(101,104,123,126,129,132,150,153)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188808"
     CDS             1..194
                     /gene="Fhl1"
                     /gene_synonym="SLIM1"
                     /coded_by="NM_001271201.1:65..649"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:25177"
                     /db_xref="RGD:2615"
ORIGIN      
        1 msekfdchyc rdplqgkkyv qkdgrhcclk cfdkfcantc vecrkpisad akevhyknry
       61 whdtcfrcak clhplasetf vskdgkilcn kcatredspr ckgcfkaiva gdqnveykgt
      121 iwhkdcftcs nckqvigtgs ffpkgedfyc vtchetkfak hcvkcnkglv kapvwwpmkd
      181 npgtttasta knap
//
LOCUS       NP_058856                249 aa            linear   ROD 28-APR-2025
DEFINITION  small ribosomal subunit protein eS6 [Rattus norvegicus].
ACCESSION   NP_058856
VERSION     NP_058856.1
DBSOURCE    REFSEQ: accession NM_017160.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Yang,H., Wen,Y., Zhang,M., Liu,Q., Zhang,H., Zhang,J., Lu,L.,
            Ye,T., Bai,X., Xiao,G. and Wang,M.
  TITLE     MTORC1 coordinates the autophagy and apoptosis signaling in
            articular chondrocytes in osteoarthritic temporomandibular joint
  JOURNAL   Autophagy 16 (2), 271-288 (2020)
   PUBMED   31007149
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Mao,B., Li,L., Yan,M., Wong,C.K.C., Silvestrini,B., Li,C., Ge,R.,
            Lian,Q. and Cheng,C.Y.
  TITLE     F5-Peptide and mTORC1/rpS6 Effectively Enhance BTB Transport
            Function in the Testis-Lesson From the Adjudin Model
  JOURNAL   Endocrinology 160 (8), 1832-1853 (2019)
   PUBMED   31157869
  REMARK    GeneRIF: a specific deletion of mTOR in Sertoli cells was found to
            cause an upregulation of p-rpS6-S240/S244 (i.e., an activation of
            rpS6), but not total rpS6, and was associated with BTB disruption,
            epithelial damage, loss of cell polarity, and infertility.
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Yan,M., Li,L., Mao,B., Li,H., Li,S.Y.T., Mruk,D., Silvestrini,B.,
            Lian,Q., Ge,R. and Cheng,C.Y.
  TITLE     mTORC1/rpS6 signaling complex modifies BTB transport function: an
            in vivo study using the adjudin model
  JOURNAL   Am J Physiol Endocrinol Metab 317 (1), E121-E138 (2019)
   PUBMED   31112404
  REMARK    GeneRIF: Overexpression of this rpS6 was capable of inducing
            blood-testis barrier remodeling, making the barrier 'leaky.'
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Younts,T.J., Monday,H.R., Dudok,B., Klein,M.E., Jordan,B.A.,
            Katona,I. and Castillo,P.E.
  TITLE     Presynaptic Protein Synthesis Is Required for Long-Term Plasticity
            of GABA Release
  JOURNAL   Neuron 92 (2), 479-492 (2016)
   PUBMED   27764673
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Pirbhoy,P.S., Farris,S. and Steward,O.
  TITLE     Synaptic activation of ribosomal protein S6 phosphorylation occurs
            locally in activated dendritic domains
  JOURNAL   Learn Mem 23 (6), 255-269 (2016)
   PUBMED   27194793
  REMARK    GeneRIF: Synaptic activation of ribosomal protein S6
            phosphorylation occurs locally in activated dendritic domains.
            results constrain hypotheses about the possible role of rpS6
            phosphorylation in regulating postsynaptic protein synthesis during
            induction of synaptic plasticity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Macfarlane,D.E. and Gailani,D.
  TITLE     Identification of phosphoprotein NP33 as a nucleus-associated
            ribosomal S6 protein and its phosphorylation in hematopoietic cells
  JOURNAL   Cancer Res 50 (10), 2895-2900 (1990)
   PUBMED   2334893
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Franco,R. and Rosenfeld,M.G.
  TITLE     Hormonally inducible phosphorylation of a nuclear pool of ribosomal
            protein S6
  JOURNAL   J Biol Chem 265 (8), 4321-4325 (1990)
   PUBMED   2106518
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Chan,Y.L. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein S6
  JOURNAL   J Biol Chem 263 (6), 2891-2896 (1988)
   PUBMED   3277962
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Gressner,A.M.
  TITLE     Two-dimensional electrophoretic analysis of ribosomal proteins from
            chronically injured liver
  JOURNAL   J Clin Chem Clin Biochem 17 (8), 541-545 (1979)
   PUBMED   501300
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Collatz,E., Wool,I.G., Lin,A. and Stoffler,G.
  TITLE     The isolation of eukaryotic ribosomal proteins. The purification
            and characterization of the 40 S ribosomal subunit proteins S2, S3,
            S4, S5, S6, S7, S8, S9, S13, S23/S24, S27, and S28
  JOURNAL   J Biol Chem 251 (15), 4666-4672 (1976)
   PUBMED   947902
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M29358.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M29358.1, CD372948.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..249
                     /product="small ribosomal subunit protein eS6"
                     /note="40S ribosomal protein S6; 40S ribosomal protein
                     S6-like"
                     /calculated_mol_wt=28550
     Region          1..215
                     /region_name="Ribosomal_S6e"
                     /note="Ribosomal protein S6e; cl00931"
                     /db_xref="CDD:469996"
     Site            137
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyarginine.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            211
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Region          217..249
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62755.1)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1, RPS6KA3, DAPK1 and PASK.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62753; propagated from
                     UniProtKB/Swiss-Prot (P62755.1)"
     CDS             1..249
                     /gene="Rps6"
                     /coded_by="NM_017160.1:16..765"
                     /db_xref="GeneID:29304"
                     /db_xref="RGD:3602"
ORIGIN      
        1 mklnisfpat gcqklievdd erklrtfyek rmatevaada lgeewkgyvv risggndkqg
       61 fpmkqgvlth grvrlllskg hscyrprrtg erkrksvrgc ivdanlsvln lvivkkgekd
      121 ipgltdttvp rrlgpkrasr irklfnlske ddvrqyvvrk plnkegkkpr tkapkiqrlv
      181 tprvlqhkrr rialkkqrtk knkeeaaeya kllakrmkea kekrqeqiak rrrlsslras
      241 tsksessqk
//
LOCUS       NP_620194                406 aa            linear   ROD 28-APR-2025
DEFINITION  vacuole membrane protein 1 [Rattus norvegicus].
ACCESSION   NP_620194
VERSION     NP_620194.1
DBSOURCE    REFSEQ: accession NM_138839.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Shoemaker,C.J., Huang,T.Q., Weir,N.R., Polyakov,N.J., Schultz,S.W.
            and Denic,V.
  TITLE     CRISPR screening using an expanded toolkit of autophagy reporters
            identifies TMEM41B as a novel autophagy factor
  JOURNAL   PLoS Biol 17 (4), e2007044 (2019)
   PUBMED   30933966
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Morita,K., Hama,Y., Izume,T., Tamura,N., Ueno,T., Yamashita,Y.,
            Sakamaki,Y., Mimura,K., Morishita,H., Shihoya,W., Nureki,O.,
            Mano,H. and Mizushima,N.
  TITLE     Genome-wide CRISPR screen identifies TMEM41B as a gene required for
            autophagosome formation
  JOURNAL   J Cell Biol 217 (11), 3817-3828 (2018)
   PUBMED   30093494
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Molejon,M.I., Ropolo,A., Re,A.L., Boggio,V. and Vaccaro,M.I.
  TITLE     The VMP1-Beclin 1 interaction regulates autophagy induction
  JOURNAL   Sci Rep 3, 1055 (2013)
   PUBMED   23316280
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Grasso,D., Ropolo,A., Lo Re,A., Boggio,V., Molejon,M.I.,
            Iovanna,J.L., Gonzalez,C.D., Urrutia,R. and Vaccaro,M.I.
  TITLE     Zymophagy, a novel selective autophagy pathway mediated by
            VMP1-USP9x-p62, prevents pancreatic cell death
  JOURNAL   J Biol Chem 286 (10), 8308-8324 (2011)
   PUBMED   21173155
  REMARK    GeneRIF: Zymophagy, a novel selective autophagy pathway mediated by
            VMP1-USP9x-p62, prevents pancreatic cell death.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Itakura,E. and Mizushima,N.
  TITLE     p62 Targeting to the autophagosome formation site requires
            self-oligomerization but not LC3 binding
  JOURNAL   J Cell Biol 192 (1), 17-27 (2011)
   PUBMED   21220506
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Hu,S.J., Ren,G., Liu,J.L., Zhao,Z.A., Yu,Y.S., Su,R.W., Ma,X.H.,
            Ni,H., Lei,W. and Yang,Z.M.
  TITLE     MicroRNA expression and regulation in mouse uterus during embryo
            implantation
  JOURNAL   J Biol Chem 283 (34), 23473-23484 (2008)
   PUBMED   18556655
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Sauermann,M., Sahin,O., Sultmann,H., Hahne,F., Blaszkiewicz,S.,
            Majety,M., Zatloukal,K., Fuzesi,L., Poustka,A., Wiemann,S. and
            Arlt,D.
  TITLE     Reduced expression of vacuole membrane protein 1 affects the
            invasion capacity of tumor cells
  JOURNAL   Oncogene 27 (9), 1320-1326 (2008)
   PUBMED   17724469
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Ropolo,A., Grasso,D., Pardo,R., Sacchetti,M.L., Archange,C., Lo
            Re,A., Seux,M., Nowak,J., Gonzalez,C.D., Iovanna,J.L. and
            Vaccaro,M.I.
  TITLE     The pancreatitis-induced vacuole membrane protein 1 triggers
            autophagy in mammalian cells
  JOURNAL   J Biol Chem 282 (51), 37124-37133 (2007)
   PUBMED   17940279
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Vaccaro,M.I., Grasso,D., Ropolo,A., Iovanna,J.L. and Cerquetti,M.C.
  TITLE     VMP1 expression correlates with acinar cell cytoplasmic
            vacuolization in arginine-induced acute pancreatitis
  JOURNAL   Pancreatology 3 (1), 69-74 (2003)
   PUBMED   12649568
  REMARK    GeneRIF: VMP1 expression may be involved in the cytoplasmic
            vacuolization of acinar cells during the early stage of acute
            pancreatitis.
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Dusetti,N.J., Jiang,Y., Vaccaro,M.I., Tomasini,R., Azizi Samir,A.,
            Calvo,E.L., Ropolo,A., Fiedler,F., Mallo,G.V., Dagorn,J.C. and
            Iovanna,J.L.
  TITLE     Cloning and expression of the rat vacuole membrane protein 1
            (VMP1), a new gene activated in pancreas with acute pancreatitis,
            which promotes vacuole formation
  JOURNAL   Biochem Biophys Res Commun 290 (2), 641-649 (2002)
   PUBMED   11785947
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC061721.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC061721.1, AF411216.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q26"
     Protein         1..406
                     /product="vacuole membrane protein 1"
                     /note="transmembrane protein 49"
                     /calculated_mol_wt=45770
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q96GC9; propagated from
                     UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Region          173..316
                     /region_name="VTT domain.
                     /evidence=ECO:0000250|UniProtKB:Q96GC9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Region          <247..298
                     /region_name="SNARE_assoc"
                     /note="SNARE associated Golgi protein; cl00429"
                     /db_xref="CDD:469768"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            274..294
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            306..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     Region          378..406
                     /region_name="Required for interaction with BECN1.
                     /evidence=ECO:0000269|PubMed:17940279"
                     /note="propagated from UniProtKB/Swiss-Prot (Q91ZQ0.1)"
     CDS             1..406
                     /gene="Vmp1"
                     /gene_synonym="Tmem49"
                     /coded_by="NM_138839.2:111..1331"
                     /db_xref="GeneID:192129"
                     /db_xref="RGD:70367"
ORIGIN      
        1 maengtncdq rrgamskeqh ngsftdpssv nekkrrdree rqnivlwrqp litlqyfsle
       61 tlvvlkewts klwhrqsmvv sfflllaalv atyyvegahq qyvqriekqf llyaywiglg
      121 ilssvglgtg lhtfllylgp hiasvtlaay ecnsvnfpep pypdqiicpd eegtegaisl
      181 wsiiskvrie acmwgigtai gelppyfmar aarlsgaepd deeyqefeem lehaetaqdf
      241 asraklavqk lvqkvgffgi lacasipnpl fdlagitcgh flvpfwtffg atligkaiik
      301 mhiqkifviv tfskhiveqm vafigavpgi gpslqkpfqe yleaqrqklh hrseagtaqg
      361 enwlswtfek lvvamvcyfi lsiinsmaqs yakriqqrln seektk
//
LOCUS       NP_001019944             416 aa            linear   ROD 28-APR-2025
DEFINITION  transcription factor IIIB 50 kDa subunit [Rattus norvegicus].
ACCESSION   NP_001019944 XP_224944
VERSION     NP_001019944.1
DBSOURCE    REFSEQ: accession NM_001024773.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Gouge,J., Satia,K., Guthertz,N., Widya,M., Thompson,A.J.,
            Cousin,P., Dergai,O., Hernandez,N. and Vannini,A.
  TITLE     Redox Signaling by the RNA Polymerase III TFIIB-Related Factor Brf2
  JOURNAL   Cell 163 (6), 1375-1387 (2015)
   PUBMED   26638071
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Vannini,A.
  TITLE     A structural perspective on RNA polymerase I and RNA polymerase III
            transcription machineries
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 258-264 (2013)
   PUBMED   23031840
  REMARK    Review article
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Dumay-Odelot,H., Durrieu-Gaillard,S., Da Silva,D., Roeder,R.G. and
            Teichmann,M.
  TITLE     Cell growth- and differentiation-dependent regulation of RNA
            polymerase III transcription
  JOURNAL   Cell Cycle 9 (18), 3687-3699 (2010)
   PUBMED   20890107
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC097435.1.
            
            On Jun 10, 2005 this sequence version replaced XP_224944.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC097435.1, EV779708.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.3"
     Protein         1..416
                     /product="transcription factor IIIB 50 kDa subunit"
                     /note="BRF-2; B-related factor 2; BRF2, subunit of RNA
                     polymerase III transcription initiation factor, BRF1-like;
                     BRF2, RNA polymerase III transcription initiation factor
                     50 subunit; BRF2, RNA polymerase III transcription
                     initiation factor subunit"
                     /calculated_mol_wt=46465
     Region          1..233
                     /region_name="tfb"
                     /note="transcription initiation factor IIB; Reviewed;
                     PRK00423"
                     /db_xref="CDD:234758"
     Region          66..162
                     /region_name="CYCLIN_BRF2"
                     /note="cyclin box found in B-related factor 2 (BRF-2) and
                     similar proteins; cd20555"
                     /db_xref="CDD:410258"
     Site            order(66,68,105,107..111,113..114,127,134..135,147,150,
                     153..154,158)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410258"
     Region          72..157
                     /region_name="Repetitive region"
                     /note="1; propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Region          108..114
                     /region_name="Interaction with target DNA.
                     /evidence=ECO:0000250|UniProtKB:Q9HAW0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Region          173..249
                     /region_name="Repetitive region"
                     /note="2; propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Region          317..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9HAW0; propagated from
                     UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Region          354..360
                     /region_name="Required for the formation of a ternary
                     complex with DNA and TBP, not required for interaction
                     with TBP in the absence of DNA.
                     /evidence=ECO:0000250|UniProtKB:Q9HAW0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     Region          362..416
                     /region_name="Required for interaction with TBP and
                     formation of a ternary complex with DNA and TBP.
                     /evidence=ECO:0000250|UniProtKB:Q9HAW0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V8D6.1)"
     CDS             1..416
                     /gene="Brf2"
                     /coded_by="NM_001024773.1:69..1319"
                     /db_xref="GeneID:306542"
                     /db_xref="RGD:1308817"
ORIGIN      
        1 mpngsrcpdc gsselvedsh ysqsqlvcsd cgcvvtegvl tttfsdegnl revtysrstg
       61 eneqvsrsqq rdlrrvrdlc rilklpltfe etavsyyqka yqlsgiraar lqkkevvvgc
      121 cvlitcrqhn wpltmgaict llyadldvfs stymqivkll gldvpslcla dlvksycssf
      181 klfqaspsmp akyvedkdkm lsrtlllvel anetwlvtgr hplpiitaat flawqslrps
      241 drltcslarf cklanvdlpy paasrlqell avllqmasql awlqvlrldk rsvvkhigdl
      301 lqhrhmlvrm afqdgtaeve tkqqqpqgrg qqeevgdstf dlpkrkrpas palllppcml
      361 kppkrthtmp pdsvvtgded isdseieqyl rtpqevrdfe raqaasraam svpnpp
//
LOCUS       NP_001258165             200 aa            linear   ROD 28-APR-2025
DEFINITION  sperm acrosome developmental regulator [Rattus norvegicus].
ACCESSION   NP_001258165 XP_002727991
VERSION     NP_001258165.1
DBSOURCE    REFSEQ: accession NM_001271236.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1.
            
            On Sep 9, 2012 this sequence version replaced XP_002727991.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079190.1, SRR26360181.2367821.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..200
                     /product="sperm acrosome developmental regulator"
                     /note="Uncharacterized protein C7orf61 homolog"
                     /calculated_mol_wt=23355
     Region          18..200
                     /region_name="DUF4703"
                     /note="Domain of unknown function (DUF4703); pfam15775"
                     /db_xref="CDD:406259"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AY52.1)"
     Region          167..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AY52.1)"
     CDS             1..200
                     /gene="Spacdr"
                     /gene_synonym="C12H7orf61"
                     /coded_by="NM_001271236.1:213..815"
                     /db_xref="GeneID:100362783"
                     /db_xref="RGD:11442159"
ORIGIN      
        1 mrflrwirqi wrkvpnwvlf wkhlakpgls dqrekhllkg pektskdfdt vklanaqked
       61 mvsdldvcpg vlrsvkersp lhdresrssr dsrslmtvvn svstfmfsvl qsgwrlcrwk
      121 ssmstgkvss htrtgsalgt peaemlrevy lvlwvirkql relarrqerr rrrrmrshas
      181 htsrhsesvq glkhdarspl
//
LOCUS       NP_062019               3933 aa            linear   ROD 28-APR-2025
DEFINITION  protein bassoon [Rattus norvegicus].
ACCESSION   NP_062019 XP_346836
VERSION     NP_062019.2
DBSOURCE    REFSEQ: accession NM_019146.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 3933)
  AUTHORS   Terry-Lorenzo,R.T., Torres,V.I., Wagh,D., Galaz,J., Swanson,S.K.,
            Florens,L., Washburn,M.P., Waites,C.L., Gundelfinger,E.D.,
            Reimer,R.J. and Garner,C.C.
  TITLE     Trio, a Rho Family GEF, Interacts with the Presynaptic Active Zone
            Proteins Piccolo and Bassoon
  JOURNAL   PLoS One 11 (12), e0167535 (2016)
   PUBMED   27907191
  REMARK    GeneRIF: The findings provide a mechanism for the presynaptic
            targeting of Trio and support a model in which Piccolo and Bassoon
            play a role in regulating neurotransmission through interactions
            with proteins, including Trio, that modulate the dynamic assembly
            of F-actin during cycles of synaptic vesicle exo- and endocytosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 3933)
  AUTHORS   Gundelfinger,E.D., Reissner,C. and Garner,C.C.
  TITLE     Role of Bassoon and Piccolo in Assembly and Molecular Organization
            of the Active Zone
  JOURNAL   Front Synaptic Neurosci 7, 19 (2016)
   PUBMED   26793095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3933)
  AUTHORS   Korber,C., Horstmann,H., Venkataramani,V., Herrmannsdorfer,F.,
            Kremer,T., Kaiser,M., Schwenger,D.B., Ahmed,S., Dean,C.,
            Dresbach,T. and Kuner,T.
  TITLE     Modulation of Presynaptic Release Probability by the
            Vertebrate-Specific Protein Mover
  JOURNAL   Neuron 87 (3), 521-533 (2015)
   PUBMED   26212709
REFERENCE   4  (residues 1 to 3933)
  AUTHORS   Ivanova,D., Dirks,A., Montenegro-Venegas,C., Schone,C.,
            Altrock,W.D., Marini,C., Frischknecht,R., Schanze,D., Zenker,M.,
            Gundelfinger,E.D. and Fejtova,A.
  TITLE     Synaptic activity controls localization and function of CtBP1 via
            binding to Bassoon and Piccolo
  JOURNAL   EMBO J 34 (8), 1056-1077 (2015)
   PUBMED   25652077
  REMARK    GeneRIF: CtBP1 is targeted and/or anchored to presynapses by direct
            interaction with the active zone scaffolding proteins Bassoon and
            piccolo.
REFERENCE   5  (residues 1 to 3933)
  AUTHORS   Dresbach,T., Torres,V., Wittenmayer,N., Altrock,W.D., Zamorano,P.,
            Zuschratter,W., Nawrotzki,R., Ziv,N.E., Garner,C.C. and
            Gundelfinger,E.D.
  TITLE     Assembly of active zone precursor vesicles: obligatory trafficking
            of presynaptic cytomatrix proteins Bassoon and Piccolo via a
            trans-Golgi compartment
  JOURNAL   J Biol Chem 281 (9), 6038-6047 (2006)
   PUBMED   16373352
  REMARK    GeneRIF: Results suggest that a primordial cytomatrix assembles in
            a trans-Golgi compartment, and that transport via Golgi-derived
            vesicles is essential for delivery of cytomatrix proteins such as
            bassoon and piccolo to the synapse.
REFERENCE   6  (residues 1 to 3933)
  AUTHORS   Dick,O., Hack,I., Altrock,W.D., Garner,C.C., Gundelfinger,E.D. and
            Brandstatter,J.H.
  TITLE     Localization of the presynaptic cytomatrix protein Piccolo at
            ribbon and conventional synapses in the rat retina: comparison with
            Bassoon
  JOURNAL   J Comp Neurol 439 (2), 224-234 (2001)
   PUBMED   11596050
REFERENCE   7  (residues 1 to 3933)
  AUTHORS   Kneussel,M., Haverkamp,S., Fuhrmann,J.C., Wang,H., Wassle,H.,
            Olsen,R.W. and Betz,H.
  TITLE     The gamma-aminobutyric acid type A receptor (GABAAR)-associated
            protein GABARAP interacts with gephyrin but is not involved in
            receptor anchoring at the synapse
  JOURNAL   Proc Natl Acad Sci U S A 97 (15), 8594-8599 (2000)
   PUBMED   10900017
REFERENCE   8  (residues 1 to 3933)
  AUTHORS   Brandstatter,J.H., Fletcher,E.L., Garner,C.C., Gundelfinger,E.D.
            and Wassle,H.
  TITLE     Differential expression of the presynaptic cytomatrix protein
            bassoon among ribbon synapses in the mammalian retina
  JOURNAL   Eur J Neurosci 11 (10), 3683-3693 (1999)
   PUBMED   10564375
REFERENCE   9  (residues 1 to 3933)
  AUTHORS   Richter,K., Langnaese,K., Kreutz,M.R., Olias,G., Zhai,R.,
            Scheich,H., Garner,C.C. and Gundelfinger,E.D.
  TITLE     Presynaptic cytomatrix protein bassoon is localized at both
            excitatory and inhibitory synapses of rat brain
  JOURNAL   J Comp Neurol 408 (3), 437-448 (1999)
   PUBMED   10340516
REFERENCE   10 (residues 1 to 3933)
  AUTHORS   tom Dieck,S., Sanmarti-Vila,L., Langnaese,K., Richter,K.,
            Kindler,S., Soyke,A., Wex,H., Smalla,K.H., Kampf,U., Franzer,J.T.,
            Stumm,M., Garner,C.C. and Gundelfinger,E.D.
  TITLE     Bassoon, a novel zinc-finger CAG/glutamine-repeat protein
            selectively localized at the active zone of presynaptic nerve
            terminals
  JOURNAL   J Cell Biol 142 (2), 499-509 (1998)
   PUBMED   9679147
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On Oct 27, 2007 this sequence version replaced NP_062019.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA5760383, SAMEA5760389
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate          :: PMID: 9679147, 16373352
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3933
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..3933
                     /product="protein bassoon"
                     /note="zinc finger protein 231; neuronal double zinc
                     finger protein"
                     /calculated_mol_wt=417896
     Region          1..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          62..70
                     /region_name="4 X 2 AA tandem repeats of P-G"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            145
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          162..225
                     /region_name="FYVE1_BSN"
                     /note="FYVE-related domain 1 found in protein bassoon;
                     cd15773"
                     /db_xref="CDD:277312"
     Region          <193..>346
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          228..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          <246..676
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          361..456
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          459..523
                     /region_name="FYVE_like_SF"
                     /note="FYVE domain like superfamily; cl28890"
                     /db_xref="CDD:333710"
     Site            order(478..483,488,507)
                     /site_type="other"
                     /note="phosphatidylinositol 3-phosphate binding site
                     [chemical binding]"
                     /db_xref="CDD:277249"
     Region          523..921
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          568..588
                     /region_name="3 X 7 AA tandem repeats of K-A-S-P-Q-A-[AK]"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            863
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1098
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          1293..1540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          <1333..1651
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1338
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:15340146; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1379
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          1560..1610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            1779
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1783
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1793
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88737;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            1805
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          1913..1963
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            1921
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            1977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2038
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2068
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2242
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2252
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2258
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          2279..2304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            2306
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          2317..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          <2350..>2420
                     /region_name="DUF4659"
                     /note="Domain of unknown function (DUF4659); pfam15558"
                     /db_xref="CDD:464768"
     Region          2460..2485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            2509
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          2512..2647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            2563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2580
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2607
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2684
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          2714..3262
                     /region_name="Interaction with DAO.
                     /evidence=ECO:0000269|PubMed:21700703"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            2795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          2838..2858
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            2844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2850
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            2929
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          2933..2995
                     /region_name="Sufficient for binding to ERC2"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            3006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          3038..>3396
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          3054..3147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          3161..3398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Site            3285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Site            3367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          3413..3545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O88778.3)"
     Region          <3476..3889
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            3487
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     Region          <3731..3915
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            3817
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88737; propagated from
                     UniProtKB/Swiss-Prot (O88778.3)"
     CDS             1..3933
                     /gene="Bsn"
                     /gene_synonym="Znf231"
                     /coded_by="NM_019146.2:102..11903"
                     /db_xref="GeneID:29138"
                     /db_xref="RGD:2223"
ORIGIN      
        1 mgneaslegg agegplppgg sglgpgpgag kppsalaggg qlpvagaara agpptpglgl
       61 vpgpgpgpgp gsvsrrldpk eplgsqrats ptpkqasata pgrespretr aqglsgqeae
      121 gprrtlqvds rtqrsgrsps vspdrgstpt spysvpqiap lpsstlcpic ktsdltstss
      181 qpnfntctqc hnkvcnqcgf npnphltqvk ewlclncqmq ralgmdmtta prsksqqqlh
      241 spalspahsp akqplgkpeq ersrspgatq sgprqaeaar atsvpgptqa tappevgrvs
      301 pqpplstkps taeprppage aqgksattvp sglgaaeqtq egltgklfgl gaslltqast
      361 lmsvqpeadt qgqpspskgp pkivfsdask eagprppgsg pgpgptpgak tepgprtgpg
      421 sgpgalaktg gtpspkhgra dhqaaskaaa kpktmpkera acplcqaeln vgsrgpanyn
      481 tctacklrvc tlcgfnptph lvektewlcl ncqtkrlleg slgepaplpl ptpqqppagv
      541 pqraagaspl kqkgpqgpgq psgslppkas pqaakaspqa akaspqakpl rasepsktss
      601 sapekktgip vkaepvpkpp petavppgtp kaksgvkrtd patpvvkpvp eapksgeaee
      661 pvpkpysqdl srspqslsdt gyssdgvsss qseitgvvqq eveqldsagv tgprppspse
      721 lhkvgssmrp sleaqavaps gewskppsgs avedqkrrph slsimpeafd sdeelgdile
      781 eddslawgrq reqqdtaess ddfgsqlrhd yvedsseggl splppqppar admtdeefmr
      841 rqilemsaee dnleeddtav sgrglakhga qkasarprpe ssqesvalpk rrlphnattg
      901 yeellseegp aeptdgalqg glrrfktiel nstgsyghel dlgqgsdpnl drepelemes
      961 ltgspedrsr gehsstlpas tpsytsgtsp tslssleeds dsspsrrqrl eeakqqrkar
     1021 hrshgpllpt iedsseeeel reeeellreq ekmreveqqr irstarktrr dkeelraqrr
     1081 rersktppsn lspiedaspt eelrqaaeme elhrsscsey spspsldsea etldggptrl
     1141 yksgseynlp afmslcspte tpsgssttps sgrplksaee ayedmmrkae llqrqqgqaa
     1201 gargphggps qptgprsqgs feyqdtqdhd yggrasqpaa dgtpaglgat vyeeilqtsq
     1261 siarmrqass rdlaftedkk kekqflnaes aymdpmkqng gpltpgtspt qlaapvsfpt
     1321 stssdssggr vipdvrvtqh fakepqeplk lhsspaspsl askevgmtfs qgpgtpatta
     1381 mapcpaslpr gymtpagper spstsstihs ygqppttany gsqteelpha psgpagsgra
     1441 srekplsggd gevgppqpsr gysyftgssp plspstpses ptfspsklgp rataefstqt
     1501 psltpssdip rspgtpspmv aqgtqtphrp stprlvwqqs sqeapvmvit lasdassqtr
     1561 mvhasastsp lcsptdsqpa shsysqttpp sasqmpsepa gppgfpraps agvdgplaly
     1621 gwgalpaeni slcrissvpg tsrvepgprp pgtavvdlrt avkptpiilt dqgmdltsla
     1681 vearkyglal dpvpgrqsta vqplvinlna qeqthtflat attvsitmas svlmaqqkqp
     1741 vvygdpfqsr ldfgqgsgsp vclaqvkqve qavqtapyrg gprgrpreak farynlpnqv
     1801 tplarrdili tqmgtaqsvs lkpgpvpepg aephratpae lrahalpgtr kphtvvvqmg
     1861 egaagtvttl lpeepagald ltgmrpesrl accdmaykfp fgssctgtfh papsapdksv
     1921 tdaalpgqss gpfysprdpe ppepltfraq gvvgpgphee qrpypqglpg rlyssmsdtn
     1981 laeaglnyha qrigqlfqgp grdsavdlss lkhsyslgfa dgrylgqglq ygsftdlrhp
     2041 tdllshplpm rryssvsniy sdhrygprgd avgfqeasla qysattarei srmcaalnsm
     2101 dqyggrhggg sggpdlvpyq pqhgpglnap qglaslrsgl lgnptypegq pspgnlaqyg
     2161 paasqgtavr qllpstatvr aadgmiysti ntpiaatlpi ttqpasvlrp mvrggmyrpy
     2221 gsggvtavpl tsltrvpmia prvplgpagl yrypapsrfp iastippaeg pvylgkpaaa
     2281 kasgaggppr pelpaggare eplsttappa vikeapvaqa papppgqkpa gdaaagsgsg
     2341 vlgrpvmeke easqedrqrk qqeqllqler erveleklrq lrlqeelere rvelqrhree
     2401 eqllvqrelq elqtikhhvl qqqqeerqaq falqreqlaq qrlqleqiqq lqqqlqqqle
     2461 eqkqrqkapf patceapsrg pppaatelaq ngqywpplth tafiavagte gpgqarepvl
     2521 hrglpssasd mslqteeqwe agrsgikkrh smprlrdace pesgpdpstv rriadssvqt
     2581 ddeegegryl ltrrrrtrrs adcsvqtdde dnaeweqpvr rrrsrlsrhs dsgsdskhea
     2641 sasssaaaaa aramssvgiq tisdcsvqte peqlprvspa ihitaatdpk veivryisap
     2701 ektgrgesla cqtepdgqaq gvagpqligp taispylpgi qivtpgalgr fekkkpdple
     2761 igyqahlppe slsqlvsrqp pkspqvlysp vsplsphrll dtsfasserl nkahvspqkq
     2821 fiadstlrqq tlprpmktlq rslsdpkpls ptaeesaker fslyqhqggl gsqvsalppn
     2881 glvrkvkrtl pspppeeahl plagqvpsql yaasllqrgl agpttvpatk asllreldrd
     2941 lrlvehestk lrkkqaelde eekeidaklk ylelgitqrk eslakdrvgr dypplrglge
     3001 hrdylsdsel nqlrlqgctt pagqyvdypa saavpatpsg ptafqqprfp paatqytags
     3061 sgptqngfla hqaptytgps typaptyppg tsypaepglp sqpafhptgh yaaptpmptt
     3121 qsapfpvqad shaahqkprq tsladleqkv ptnyevissp avtvsstpse tgysgpavss
     3181 syehgkapeh prggdrssvs qspaptypsd shytsleqnv prnyvmiddi seltkdstpt
     3241 asdsqrpepl gpggvsgrpg kdpgepavle gptlpccygr geeeseedsy dprgksghhr
     3301 smesngrpas thyysdsdyr hgaradkygp gpmgpkhpsk nlapaaissk rskhrkqgme
     3361 qkiskfspie eakdvesdla syppptvsss ltsrsrkfqd eityglkknv yeqqryygvs
     3421 srdtaeeddr myggssrsrv asaysgekls shdfssrskg yereretaer lqkagpkpss
     3481 lsmahgrarp pmrsqaseee spvsplgrpr paggalppgd tcpqfcsshs mpdvqehvkd
     3541 gprahaykre egyilddshc vvsdseayhl gqeetdwfdk prdarsdrfr hhgghtvsss
     3601 qkrgparhsy hdydeppeeg lwphdeggpg rhtsakehrh hgdhgrhsgr hageepgrra
     3661 arphardmgr hetrphpqas papamqkkgq pgypssadys qpsrapsayh hasdskkgsr
     3721 qahsgptvlq pkpeaqaqpq mqgrqavpgp qqsqppssrq tpsgtasrqp qtqqqqqqqq
     3781 qqqqqqqqqq qqglgqqapq qapsqarlqq qsqpttrsta paashpagkp qpgpttapgp
     3841 qpaglpraeq agsskpaaka pqqgrapqaq sapgpagakt garpggtpga pagqpaaege
     3901 svfskilpgg aaeqagklte avsafgkkfs sfw
//
LOCUS       NP_067594                153 aa            linear   ROD 28-APR-2025
DEFINITION  prostaglandin E synthase [Rattus norvegicus].
ACCESSION   NP_067594
VERSION     NP_067594.1
DBSOURCE    REFSEQ: accession NM_021583.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Lin,M.H., Lee,Y.C., Liao,J.B., Chou,C.Y. and Yang,Y.F.
  TITLE     PTGES is involved in myofibroblast differentiation via
            HIF-1alpha-dependent glycolysis pathway
  JOURNAL   J Cell Mol Med 28 (20), e70157 (2024)
   PUBMED   39417702
  REMARK    GeneRIF: PTGES is involved in myofibroblast differentiation via
            HIF-1alpha-dependent glycolysis pathway.
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Lin,Y.M., Fu,Y., Hegde,S., Tang,Y., Radhakrishnan,R. and Shi,X.Z.
  TITLE     Microsomal Prostaglandin E Synthase-1 Plays a Critical Role in
            Long-term Motility Dysfunction after Bowel Obstruction
  JOURNAL   Sci Rep 8 (1), 8831 (2018)
   PUBMED   29891860
  REMARK    GeneRIF: In conclusion, microsomal PGES-1 plays a critical role in
            the continuous suppression of motor function in the post-bowel
            obstruction state.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Gao,C., Fu,Y., Li,Y., Zhang,X., Zhang,L., Yu,F., Xu,S.S., Xu,Q.,
            Zhu,Y., Guan,Y., Wang,X. and Kong,W.
  TITLE     Microsomal Prostaglandin E Synthase-1-Derived PGE2 Inhibits
            Vascular Smooth Muscle Cell Calcification
  JOURNAL   Arterioscler Thromb Vasc Biol 36 (1), 108-121 (2016)
   PUBMED   26543101
  REMARK    GeneRIF: Suggest pivotal role of COX-2-mPGES-1-PGE2 axis in
            vascular calcification. Inhibition of COX-2 or mPGES-1 may increase
            the risk of calcification and subsequent adverse cardiovascular
            events during chronic renal failure.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Waclawik,A., Rivero-Muller,A., Rahman,N.A. and Ziecik,A.J.
  TITLE     Functional consequences of knocking down porcine prostaglandin
            synthases in SK-6 swine kidney cell line
  JOURNAL   Reprod Biol 15 (1), 42-47 (2015)
   PUBMED   25726376
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Bylund,J., Annas,A., Hellgren,D., Bjurstrom,S., Andersson,H. and
            Svanhagen,A.
  TITLE     Amide hydrolysis of a novel chemical series of microsomal
            prostaglandin E synthase-1 inhibitors induces kidney toxicity in
            the rat
  JOURNAL   Drug Metab Dispos 41 (3), 634-641 (2013)
   PUBMED   23284082
  REMARK    GeneRIF: Using metabolic profiling and exploratory rat toxicity
            studies, a new and active mPGES-1 inhibitor with improved margins
            to chemically induced kidney toxicity in rats has been identified.
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Lazarus,M., Kubata,B.K., Eguchi,N., Fujitani,Y., Urade,Y. and
            Hayaishi,O.
  TITLE     Biochemical characterization of mouse microsomal prostaglandin E
            synthase-1 and its colocalization with cyclooxygenase-2 in
            peritoneal macrophages
  JOURNAL   Arch Biochem Biophys 397 (2), 336-341 (2002)
   PUBMED   11795891
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Jabbour,H.N., Milne,S.A., Williams,A.R., Anderson,R.A. and
            Boddy,S.C.
  TITLE     Expression of COX-2 and PGE synthase and synthesis of PGE(2)in
            endometrial adenocarcinoma: a possible autocrine/paracrine
            regulation of neoplastic cell function via EP2/EP4 receptors
  JOURNAL   Br J Cancer 85 (7), 1023-1031 (2001)
   PUBMED   11592775
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Mancini,J.A., Blood,K., Guay,J., Gordon,R., Claveau,D., Chan,C.C.
            and Riendeau,D.
  TITLE     Cloning, expression, and up-regulation of inducible rat
            prostaglandin e synthase during lipopolysaccharide-induced pyresis
            and adjuvant-induced arthritis
  JOURNAL   J Biol Chem 276 (6), 4469-4475 (2001)
   PUBMED   11067848
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Murakami,M., Naraba,H., Tanioka,T., Semmyo,N., Nakatani,Y.,
            Kojima,F., Ikeda,T., Fueki,M., Ueno,A., Oh,S. and Kudo,I.
  TITLE     Regulation of prostaglandin E2 biosynthesis by inducible
            membrane-associated prostaglandin E2 synthase that acts in concert
            with cyclooxygenase-2
  JOURNAL   J Biol Chem 275 (42), 32783-32792 (2000)
   PUBMED   10869354
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Satoh,K., Nagano,Y., Shimomura,C., Suzuki,N., Saeki,Y. and
            Yokota,H.
  TITLE     Expression of prostaglandin E synthase mRNA is induced in
            beta-amyloid treated rat astrocytes
  JOURNAL   Neurosci Lett 283 (3), 221-223 (2000)
   PUBMED   10754227
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB048730.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB048730.1, BC105858.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p12"
     Protein         1..153
                     /product="prostaglandin E synthase"
                     /EC_number="2.5.1.18"
                     /EC_number="5.3.99.3"
                     /note="glutathione peroxidase PTGES; glutathione
                     transferase PTGES; inducible prostaglandin E synthase;
                     microsomal prostaglandin E synthase 1"
                     /calculated_mol_wt=17141
     Site            14..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHF3.1)"
     Region          17..147
                     /region_name="MAPEG"
                     /note="MAPEG family; pfam01124"
                     /db_xref="CDD:460074"
     Site            50
                     /site_type="other"
                     /note="Essential for protaglandin-E synthase activity.
                     /evidence=ECO:0000250|UniProtKB:O14684; propagated from
                     UniProtKB/Swiss-Prot (Q9JHF3.1)"
     Site            62..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHF3.1)"
     Site            99..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHF3.1)"
     Site            125..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JHF3.1)"
     Site            127
                     /site_type="other"
                     /note="Essential for protaglandin-E synthase activity.
                     /evidence=ECO:0000250|UniProtKB:O14684; propagated from
                     UniProtKB/Swiss-Prot (Q9JHF3.1)"
     CDS             1..153
                     /gene="Ptges"
                     /gene_synonym="mPGES-1; Pges"
                     /coded_by="NM_021583.3:41..502"
                     /db_xref="GeneID:59103"
                     /db_xref="RGD:62076"
ORIGIN      
        1 mtslglvmen sqvlpafllc stllvikmya vavitgqvrl rkkafanped alkrgglqyc
       61 rsdpdvercl rahrndmeti ypflflgfvy sflgpnplia wihflvvltg rvvhtvaylg
      121 kmnprirsga yvlaqfacfs malqilweva hhl
//
LOCUS       NP_997709                186 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich protein 3 [Rattus norvegicus].
ACCESSION   NP_997709 XP_347002
VERSION     NP_997709.1
DBSOURCE    REFSEQ: accession NM_212544.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Hurt,P., Walter,L., Sudbrak,R., Klages,S., Muller,I., Shiina,T.,
            Inoko,H., Lehrach,H., Gunther,E., Reinhardt,R. and Himmelbauer,H.
  TITLE     The genomic sequence and comparative analysis of the rat major
            histocompatibility complex
  JOURNAL   Genome Res 14 (4), 631-639 (2004)
   PUBMED   15060004
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126073.1.
            
            On Aug 30, 2004 this sequence version replaced XP_347002.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC126073.1, EV767777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20p12"
     Protein         1..186
                     /product="proline-rich protein 3"
                     /note="MHC class I region proline-rich protein CAT56;
                     proline-rich polypeptide 3"
                     /calculated_mol_wt=20520
     Region          1..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MG07.1)"
     Region          155..179
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     CDS             1..186
                     /gene="Prr3"
                     /gene_synonym="Cat56"
                     /coded_by="NM_212544.2:40..600"
                     /db_xref="GeneID:361788"
                     /db_xref="RGD:1303270"
ORIGIN      
        1 mpkrkkqnqp qppqhlalse rdepgdeede rpmgppsllg pppmangkpg dpksvfhrgp
       61 pgsrgpmipp llslpppprg rghirgglgp rsspygrgww gvnteppfpg pghggpsrei
      121 fyqeprnprr lkswslvknt yppkdsppmm edksdrpvcr hfskkghcry edhcafyhpg
      181 vngppl
//
LOCUS       NP_112348                675 aa            linear   ROD 28-APR-2025
DEFINITION  vitamin K-dependent protein S precursor [Rattus norvegicus].
ACCESSION   NP_112348 XP_343651
VERSION     NP_112348.2
DBSOURCE    REFSEQ: accession NM_031086.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Ginisty,A., Oliver,L., Arnault,P., Vallette,F., Benzakour,O. and
            Coronas,V.
  TITLE     The vitamin K-dependent factor, protein S, regulates brain neural
            stem cell migration and phagocytic activities towards glioma cells
  JOURNAL   Eur J Pharmacol 855, 30-39 (2019)
   PUBMED   31028740
  REMARK    GeneRIF: vitamin K-dependent factor, protein S, regulates brain
            neural stem cell migration and phagocytic activities towards glioma
            cells
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Zhong,F., Chen,H., Xie,Y., Azeloglu,E.U., Wei,C., Zhang,W., Li,Z.,
            Chuang,P.Y., Jim,B., Li,H., Elmastour,F., Riyad,J.M., Weber,T.,
            Chen,H., Wang,Y., Zhang,A., Jia,W., Lee,K. and He,J.C.
  TITLE     Protein S Protects against Podocyte Injury in Diabetic Nephropathy
  JOURNAL   J Am Soc Nephrol 29 (5), 1397-1410 (2018)
   PUBMED   29511111
  REMARK    GeneRIF: Our results support a protective role of PS against
            glomerular injury in DN progression.
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Alhenc-Gelas,M., Plu-Bureau,G., Horellou,M.H., Rauch,A. and
            Suchon,P.
  CONSRTM   GEHT genetic thrombophilia group
  TITLE     PROS1 genotype phenotype relationships in a large cohort of adults
            with suspicion of inherited quantitative protein S deficiency
  JOURNAL   Thromb Haemost 115 (3), 570-579 (2016)
   PUBMED   26466767
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Abonnenc,M., Nabeebaccus,A.A., Mayr,U., Barallobre-Barreiro,J.,
            Dong,X., Cuello,F., Sur,S., Drozdov,I., Langley,S.R., Lu,R.,
            Stathopoulou,K., Didangelos,A., Yin,X., Zimmermann,W.H., Shah,A.M.,
            Zampetaki,A. and Mayr,M.
  TITLE     Extracellular matrix secretion by cardiac fibroblasts: role of
            microRNA-29b and microRNA-30c
  JOURNAL   Circ Res 113 (10), 1138-1147 (2013)
   PUBMED   24006456
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Bouwens,E.A., Stavenuiter,F. and Mosnier,L.O.
  TITLE     Mechanisms of anticoagulant and cytoprotective actions of the
            protein C pathway
  JOURNAL   J Thromb Haemost 11 Suppl 1 (0 1), 242-253 (2013)
   PUBMED   23809128
  REMARK    Review article
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Duchemin,J., Gandrille,S., Borgel,D., Feurgard,P., Alhenc-Gelas,M.,
            Matheron,C., Dreyfus,M., Dupuy,E., Juhan-Vague,I. and Aiach,M.
  TITLE     The Ser 460 to Pro substitution of the protein S alpha (PROS1) gene
            is a frequent mutation associated with free protein S (type IIa)
            deficiency
  JOURNAL   Blood 86 (9), 3436-3443 (1995)
   PUBMED   7579448
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Jamison,C.S., McDowell,S.A., Marlar,R.A. and Degen,S.J.
  TITLE     Developmental expression of protein C and protein S in the rat
  JOURNAL   Thromb Res 78 (5), 407-419 (1995)
   PUBMED   7660357
REFERENCE   8  (residues 1 to 675)
  AUTHORS   Yasuda,F., Hayashi,T., Tanitame,K., Nishioka,J. and Suzuki,K.
  TITLE     Molecular cloning and functional characterization of rat plasma
            protein S
  JOURNAL   J Biochem 117 (2), 374-383 (1995)
   PUBMED   7608128
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Smith,G.L. and Steele,D.S.
  TITLE     Inorganic phosphate decreases the Ca2+ content of the sarcoplasmic
            reticulum in saponin-treated rat cardiac trabeculae
  JOURNAL   J Physiol 458, 457-473 (1992)
   PUBMED   1302274
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Thur,C. and Biedermann,M.
  TITLE     [Post-traumatic impingement syndrome caused by a displaced
            tuberculum majus fragment]
  JOURNAL   Z Unfallchir Versicherungsmed 85 (4), 189-201 (1992)
   PUBMED   1299299
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB790907.1, DY571157.1, CB580854.1, CV105055.1, CK366505.1,
            DV727991.1 and BC091117.1.
            
            On Apr 19, 2007 this sequence version replaced NP_112348.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132291,
                              SAMD00132292 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11p12"
     Protein         1..675
                     /product="vitamin K-dependent protein S precursor"
                     /note="vitamin K-dependent protein S; protein S (alpha)"
                     /calculated_mol_wt=71944
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2686
     Region          23..85
                     /region_name="GLA"
                     /note="Domain containing Gla (gamma-carboxyglutamate)
                     residues; smart00069"
                     /db_xref="CDD:214503"
     mat_peptide     42..675
                     /product="Vitamin K-dependent protein S.
                     /id=PRO_0000022128"
                     /note="propagated from UniProtKB/Swiss-Prot (P53813.1)"
                     /calculated_mol_wt=69875
     Site            47
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            48
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            55
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            57
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            60
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            61
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            66
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            67
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            70
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            73
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Site            77
                     /site_type="gamma-carboxyglutamic-acid"
                     /note="4-carboxyglutamate.
                     /evidence=ECO:0000250|UniProtKB:P07224,
                     ECO:0000255|PROSITE-ProRule:PRU00463; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Region          88..116
                     /region_name="Thrombin-sensitive"
                     /note="propagated from UniProtKB/Swiss-Prot (P53813.1)"
     Region          119..155
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            136
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyaspartate. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P53813.1)"
     Region          168..199
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          201..233
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(201,204,219)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          226..246
                     /region_name="cEGF"
                     /note="Complement Clr-like EGF-like; pfam12662"
                     /db_xref="CDD:463661"
     Region          247..282
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          329..459
                     /region_name="Laminin_G_1"
                     /note="Laminin G domain; pfam00054"
                     /db_xref="CDD:395008"
     Site            499
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     Region          509..646
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            509
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P53813.1)"
     CDS             1..675
                     /gene="Pros1"
                     /gene_synonym="Pros"
                     /coded_by="NM_031086.2:85..2112"
                     /db_xref="GeneID:81750"
                     /db_xref="RGD:620971"
ORIGIN      
        1 mrvlsvrfrv llaclalvlp vsetnflske rasqvlvrkr rantlleetk kgnlerecie
       61 elcnkeeare vfennpetdy fypkylgclg afrvgafsaa rqsanaypdl rscvnaipdq
      121 cdpmpcnedg ylsckdgqga ftcickpgwq gdkcqfdine ckdpsningg csqtcdntpg
      181 syhcsckigf amltnkkdck dvdecslkps vcgtavckni pgdfececpn gyrydpssks
      241 ckdvdecsen tcaqlcvnyp ggyscycdgk kgfklaqdqr scegipvcls ldldknyell
      301 ylaeqfagvv lylkfrlpdi trfsaefdfr tydsegiily aesldhsnwl lialregkie
      361 vqfknefstq ittggnvinn giwnmvsvee lddsvsikia keavmninkl gslfkptdgf
      421 ldtkiyfagl prkvesalik pinprldgci rgwnlmkqga lgakeivegk qnkhcfltve
      481 kgsyypgsgi aqfsidynnv tnaegwqinv tlnirpstgt gvmlalvsgd tvpfalslvd
      541 sgsgtsqdil vfvensvaah leaitlcseq psqlkcninr nglelwtpvr kdviyskdlq
      601 rqlaildktm kgtvatylgg vpdisfsatp vnafysgcme vningvqldl deaiskhndi
      661 rahscpsvrk iqknf
//
LOCUS       NP_001127832            1933 aa            linear   ROD 28-APR-2025
DEFINITION  WD repeat-containing protein 81 [Rattus norvegicus].
ACCESSION   NP_001127832 XP_001080687 XP_220710
VERSION     NP_001127832.1
DBSOURCE    REFSEQ: accession NM_001134360.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1933)
  AUTHORS   Liu,X., Li,Y., Wang,X., Xing,R., Liu,K., Gan,Q., Tang,C., Gao,Z.,
            Jian,Y., Luo,S., Guo,W. and Yang,C.
  TITLE     The BEACH-containing protein WDR81 coordinates p62 and LC3C to
            promote aggrephagy
  JOURNAL   J Cell Biol 216 (5), 1301-1320 (2017)
   PUBMED   28404643
REFERENCE   2  (residues 1 to 1933)
  AUTHORS   Rapiteanu,R., Davis,L.J., Williamson,J.C., Timms,R.T., Paul
            Luzio,J. and Lehner,P.J.
  TITLE     A Genetic Screen Identifies a Critical Role for the WDR81-WDR91
            Complex in the Trafficking and Degradation of Tetherin
  JOURNAL   Traffic 17 (8), 940-958 (2016)
   PUBMED   27126989
REFERENCE   3  (residues 1 to 1933)
  AUTHORS   Liu,K., Jian,Y., Sun,X., Yang,C., Gao,Z., Zhang,Z., Liu,X., Li,Y.,
            Xu,J., Jing,Y., Mitani,S., He,S. and Yang,C.
  TITLE     Negative regulation of phosphatidylinositol 3-phosphate levels in
            early-to-late endosome conversion
  JOURNAL   J Cell Biol 212 (2), 181-198 (2016)
   PUBMED   26783301
  REMARK    Erratum:[J Cell Biol. 2016 Mar 14;212(6):739. doi:
            10.1083/jcb.20150608103012016c. PMID: 26975852]
REFERENCE   4  (residues 1 to 1933)
  AUTHORS   Traka,M., Millen,K.J., Collins,D., Elbaz,B., Kidd,G.J., Gomez,C.M.
            and Popko,B.
  TITLE     WDR81 is necessary for purkinje and photoreceptor cell survival
  JOURNAL   J Neurosci 33 (16), 6834-6844 (2013)
   PUBMED   23595742
REFERENCE   5  (residues 1 to 1933)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   6  (residues 1 to 1933)
  AUTHORS   Florea,L., Di Francesco,V., Miller,J., Turner,R., Yao,A.,
            Harris,M., Walenz,B., Mobarry,C., Merkulov,G.V., Charlab,R.,
            Dew,I., Deng,Z., Istrail,S., Li,P. and Sutton,G.
  TITLE     Gene and alternative splicing annotation with AIR
  JOURNAL   Genome Res 15 (1), 54-66 (2005)
   PUBMED   15632090
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Aug 26, 2008 this sequence version replaced
            XP_001080687.1, XP_220710.4.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760494
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1933
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..1933
                     /product="WD repeat-containing protein 81"
                     /calculated_mol_wt=212130
     Region          1..643
                     /region_name="Necessary and sufficient for the interaction
                     with SQSTM1. /evidence=ECO:0000250|UniProtKB:Q562E7"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          305..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          347..587
                     /region_name="Beach"
                     /note="BEACH (Beige and Chediak-Higashi) domains,
                     implicated in membrane trafficking, are present in a
                     family of proteins conserved throughout eukaryotes. This
                     group contains human lysosomal trafficking regulator
                     (LYST), LPS-responsive and beige-like anchor...; cd06071"
                     /db_xref="CDD:100117"
     Region          663..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1038..1057
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1090..1209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1517..1544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1565..1590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          <1632..1931
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          1638..1677
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1644..1687
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1684..1724
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1692..1726
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1735..1771
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1776..1815
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1781..1814
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1818..1856
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     Region          1823..1856
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1863..1885
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1903..1933
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (D4A929.1)"
     CDS             1..1933
                     /gene="Wdr81"
                     /gene_synonym="RGD1311334"
                     /coded_by="NM_001134360.1:211..6012"
                     /db_xref="GeneID:303312"
                     /db_xref="RGD:1311334"
ORIGIN      
        1 maqgsrrrkv vltagaegcs sssgpdmeel lrcaerdlni darqlalapg gthvvalvst
       61 rwlaslrerr lgpcpraegl geaevrtllq rsvqrlpqgw trvevhglrk rrlsyplsrv
      121 lpfeegscsp etltrfmqev aaqnyrnlwr hayhtygqpy shstapsaip aldsirqalq
      181 rvygctflpv gesmqclsnv rdgpsrgssa cpsllraeal lespemlyvv hpyvqfslhd
      241 vvtfspaklt nsqakvlfil frvlramdac hrqglacgal slhhiavdek lcselrldls
      301 ayempseden qevseekdrt gvksekdgeg rpgcptcqke lrglvldwvh grvsnfyylm
      361 qlnrlagrrq gdpnyhpvlp wvvdfttpyg rfrdlrkskf rlnkgdkqld ftyemtrqaf
      421 vaggagsgep lhvphhisdv lsdityyvyk arrtprsvlc ghvraqweph eypatmermq
      481 twtpdecipe fytdpsifcs ihpdmpdldv pawcssnqef vtahralles wevsqdlhhw
      541 idltfgyklq gkeavkeknv clhlvdahth ltsygvvqlf dqphpqrlag apalapeppl
      601 iprllvqpiq eatgqedisg qlingagrhv vevtpcesgw trerptaged dleqateald
      661 sisipgkagd qpgssssqas pgllpfsaps gsrpgrrska tgldsgegde gkivlpegfs
      721 piqaleelek vgnflarglg sqleepekpq aqppvylqsl fhrdmqvlgv llaemvfatr
      781 vrilqpdapl wvrfeavrgl ctrhskdipv slqpvldtll qlsgpksplv vkkgkldplf
      841 eyrpvsqglp ppspaqllsp fssvvpfpty fpalhkfill yqarrvedev qgrelvfalw
      901 qqlgavlnei tpegleillp fvlslmseeh tavytawylf epvakalgpk ntikyllkpl
      961 igayenpcrl hgrfylytdc fvaqlvvrlg lqaflihllp hvlqvlagve asqeegkglv
     1021 gttedeenel pvpgpgscaf geeiqmggqp aassglglpd yrsgvsfhdq adlpdtedfq
     1081 aglyvaespq pqeaeavslg qlsdksstse asqgeerggd dggapvdkns vksgdssqdl
     1141 kqsegseeee eeeegcvvle eeeqdevtgt seltlsdtil smetvvapgd grdreeeeep
     1201 lpeqtegkeq killdtackm vrwlsaklgp tvasrhvarn llrlltscyv gptrqqftvs
     1261 cddspplnag niyqkrpvlg divsgpvlsc llhiahlyge pvltyqylpy isylvapgsn
     1321 sspsrlnsrk eagllaavtl tqkiivylsd ttlmdilpri shevllpvls fltsfvtgfp
     1381 sgaqartvlc vktisliali clrigqemvq qhlsepvatf fqvfshlhel rqqdlqldlk
     1441 gctegqlpea tfsdgqrrpv dptlleelqk vftlemayti yvpfscllgd iirkiipnhe
     1501 lvgelaglyl esmspsslrn pasmepvtps agpewnpqsg sclqddghsg tfgsvlvgnr
     1561 iqipdsqpqs sgplgsisgv gsgglssrne dnalkrelpr sahglsgnwl aywqyeigvs
     1621 qqdahfhfhq irlqsfpght gavkcvaals sedfflsgsk drtvrlwply nygdgtseta
     1681 prliyaqhrk svfyvgqlea pqyvvscdga vhvwdpftgk tlrtvdpsds rvpltavavm
     1741 paphtsitma ssdstlrfvd crkpglqhef rlggglnpgl vrslavspsg rsvvagfssg
     1801 fmvlldtrtg lvlrgwpahe gdilqikave gsvivssssd hsltvwkele qkpthhyksa
     1861 sdpihtfdly gsevvtgtva nkigvcslle ppsqattkls senfrgtlts lallptkrhl
     1921 llgsdngiir lla
//
LOCUS       NP_001020139             461 aa            linear   ROD 28-APR-2025
DEFINITION  lysosomal proton-coupled steroid conjugate and bile acid symporter
            SLC46A3 precursor [Rattus norvegicus].
ACCESSION   NP_001020139 XP_237862
VERSION     NP_001020139.1
DBSOURCE    REFSEQ: accession NM_001024968.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Kim,J.H., Matsubara,T., Lee,J., Fenollar-Ferrer,C., Han,K., Kim,D.,
            Jia,S., Chang,C.J., Yang,H., Nagano,T., Krausz,K.W., Yim,S.H. and
            Gonzalez,F.J.
  TITLE     Lysosomal SLC46A3 modulates hepatic cytosolic copper homeostasis
  JOURNAL   Nat Commun 12 (1), 290 (2021)
   PUBMED   33436590
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091179.1.
            
            On Jun 25, 2005 this sequence version replaced XP_237862.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132294, SAMD00132297
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..461
                     /product="lysosomal proton-coupled steroid conjugate and
                     bile acid symporter SLC46A3 precursor"
                     /note="lysosomal proton-coupled steroid conjugate and bile
                     acid symporter SLC46A3"
                     /calculated_mol_wt=48775
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK75.1)"
                     /calculated_mol_wt=2769
     Region          3..437
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(13..14,17..18,21,88,142..143,145..147,150,173,
                     176..177,180,267,270..271,274..276,279,308,312,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
     mat_peptide     26..461
                     /product="Lysosomal proton-coupled steroid conjugate and
                     bile acid symporter SLC46A3. /id=PRO_0000307256"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
                     /calculated_mol_wt=48775
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            71..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            198..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            325..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            348..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            382..402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     Region          446..449
                     /region_name="Tyrosine-based lysosomal-sorting motif.
                     /evidence=ECO:0000250|UniProtKB:Q7Z3Q1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BK75.1)"
     CDS             1..461
                     /gene="Slc46a3"
                     /gene_synonym="RGD1307594"
                     /coded_by="NM_001024968.1:347..1732"
                     /db_xref="GeneID:288454"
                     /db_xref="RGD:1307594"
ORIGIN      
        1 mkisfiepai llyafamtlt ipltaqyvyr riweetgnyt ftsssnvsec eqnkssstfa
       61 fqeevqkkas lfslqveisg lipglvstfm llsssdnhgr klpmvlsslg slgtnlwlca
      121 msyfdlplql lvastfigal fgnyttfwga cfayivdqek eykhriiria vldfmlgvvt
      181 gltglssgyf irelgfawsy fiiavvvlvn layilfflsd pikesssqiv tmscseslkd
      241 lfyrtymlfk ngsckrrsll clliftlvvy ffvvfgitpv ftlyelgppl cwnevyigyg
      301 salgslsfls sflgiwlfsy clkdihiayv gifttmvgmm ltaftrttlm mflvrisfff
      361 timplsilrs mlskvvhste qgvlfaciaf letlggvtst sayngiysat vawypgfvfl
      421 lsagllvlpa vslcmvkcig weegsytlli hdepsehtsd s
//
LOCUS       NP_001012082             326 aa            linear   ROD 28-APR-2025
DEFINITION  UDP-N-acetylglucosamine transporter [Rattus norvegicus].
ACCESSION   NP_001012082 XP_227620
VERSION     NP_001012082.1
DBSOURCE    REFSEQ: accession NM_001012082.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Maszczak-Seneczko,D., Sosicka,P., Majkowski,M., Olczak,T. and
            Olczak,M.
  TITLE     UDP-N-acetylglucosamine transporter and UDP-galactose transporter
            form heterologous complexes in the Golgi membrane
  JOURNAL   FEBS Lett 586 (23), 4082-4087 (2012)
   PUBMED   23089177
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Maszczak-Seneczko,D., Olczak,T. and Olczak,M.
  TITLE     Subcellular localization of UDP-GlcNAc, UDP-Gal and SLC35B4
            transporters
  JOURNAL   Acta Biochim Pol 58 (3), 413-419 (2011)
   PUBMED   21918738
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079371.1.
            
            On Feb 11, 2005 this sequence version replaced XP_227620.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079371.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..326
                     /product="UDP-N-acetylglucosamine transporter"
                     /note="golgi UDP-GlcNAc transporter; solute carrier family
                     35 (UDP-N-acetylglucosamine (UDP-GlcNAc) transporter),
                     member A3"
                     /calculated_mol_wt=35948
     Region          1..314
                     /region_name="Nuc_sug_transp"
                     /note="Nucleotide-sugar transporter; pfam04142"
                     /db_xref="CDD:398009"
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            243..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXR5.1)"
     CDS             1..326
                     /gene="Slc35a3"
                     /coded_by="NM_001012082.1:144..1124"
                     /db_xref="GeneID:310808"
                     /db_xref="RGD:1308615"
ORIGIN      
        1 msanlkylsl gilvfqttsl vltmrysrtl keegprylss tavvvaeflk imaciflvyk
       61 dskcsvrtln rvlhdeilnk pmetlklaip sgiytlqnnl lyvalsnlda atyqvtyqlk
      121 ilttalfsvs mlgkklgmyq wlslvilmag vafvqwpsds qelnskdlst gsqfvglmav
      181 liacfssgfa gvyfekilke tkqsvwirni qlgffgsifg lmgvyvydge lvskngffqg
      241 ynqltwivvv lqalgglvia avikyadnil kgfatslsii lstiisyfwl qdfvptsvff
      301 lgailviaat flygydpkpa gnptka
//
LOCUS       NP_001070699             522 aa            linear   ROD 28-APR-2025
DEFINITION  tetratricopeptide repeat protein 39C isoform 1 [Rattus norvegicus].
ACCESSION   NP_001070699 XP_001072783
VERSION     NP_001070699.1
DBSOURCE    REFSEQ: accession NM_001077231.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105623.1.
            
            On Oct 16, 2006 this sequence version replaced XP_001072783.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105623.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18p13"
     Protein         1..522
                     /product="tetratricopeptide repeat protein 39C isoform 1"
                     /note="tetratricopeptide repeat protein 39C; TPR repeat
                     protein 39C"
                     /calculated_mol_wt=58847
     Region          1..437
                     /region_name="Iml2-TPR_39"
                     /note="Iml2/Tetratricopeptide repeat protein 39;
                     pfam10300"
                     /db_xref="CDD:463047"
     Region          254..287
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VGK2.1)"
     Region          292..325
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VGK2.1)"
     Region          424..457
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VGK2.1)"
     CDS             1..522
                     /gene="Ttc39c"
                     /coded_by="NM_001077231.1:104..1672"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:686179"
                     /db_xref="RGD:1585423"
ORIGIN      
        1 msfgasfvsf lnammtfeee kmqlacddlk tteklcesee agvietiknk ikknvdarks
       61 tpsmvdrlqr qiiiadcqvy lavlsfvkqe lsayikggwi lrkawkiynk cyvdinalqe
      121 lhqktlteep lssdaandnh ivaegvteea lsrlkgavsf gyglfhlcis mvppnllkii
      181 nllgfpgdrl qglssltyas eskdmkapla tlallwyhtv vrpffaldgs dnkggldeak
      241 aillrkesay pnsslfmffk griqrlecqi nsaltsfhta lelavdqrei qhvclyeigw
      301 csmielnfkd afdsferlkn esrwsqcyya yltavcqgat gdvdgaqlif kevqklfkrk
      361 nnqieqfsvk kaerfrkqtp tralcvlasi evlylwkalp ncslpnlqrm sqachevdds
      421 svvglkhlll gaihkclgns qdavqffqra akdescrqnn syvqpyacye lgcllldrae
      481 tvargrtlll qakedfsgyd fenrlhvrvh aalaslrelv pq
//
LOCUS       NP_001095853            1450 aa            linear   ROD 28-APR-2025
DEFINITION  sister chromatid cohesion protein PDS5 homolog B isoform 1 [Rattus
            norvegicus].
ACCESSION   NP_001095853 XP_001070651
VERSION     NP_001095853.1
DBSOURCE    REFSEQ: accession NM_001102383.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1450)
  AUTHORS   Zhang,B., Chang,J., Fu,M., Huang,J., Kashyap,R., Salavaggione,E.,
            Jain,S., Kulkarni,S., Deardorff,M.A., Uzielli,M.L., Dorsett,D.,
            Beebe,D.C., Jay,P.Y., Heuckeroth,R.O., Krantz,I. and Milbrandt,J.
  TITLE     Dosage effects of cohesin regulatory factor PDS5 on mammalian
            development: implications for cohesinopathies
  JOURNAL   PLoS One 4 (5), e5232 (2009)
   PUBMED   19412548
  REMARK    Erratum:[PLoS One. 2009;4(5). doi:
            10.1371/annotation/ea5b7eb5-5087-448a-8325-c8efff1f54d9.
            Shashikant, Kulkarni [corrected to Kulkarni, Shashikant]]
REFERENCE   2  (residues 1 to 1450)
  AUTHORS   Watrin,E., Schleiffer,A., Tanaka,K., Eisenhaber,F., Nasmyth,K. and
            Peters,J.M.
  TITLE     Human Scc4 is required for cohesin binding to chromatin,
            sister-chromatid cohesion, and mitotic progression
  JOURNAL   Curr Biol 16 (9), 863-874 (2006)
   PUBMED   16682347
REFERENCE   3  (residues 1 to 1450)
  AUTHORS   Losada,A., Yokochi,T. and Hirano,T.
  TITLE     Functional contribution of Pds5 to cohesin-mediated cohesion in
            human cells and Xenopus egg extracts
  JOURNAL   J Cell Sci 118 (Pt 10), 2133-2141 (2005)
   PUBMED   15855230
REFERENCE   4  (residues 1 to 1450)
  AUTHORS   Geck,P., Maffini,M.V., Szelei,J., Sonnenschein,C. and Soto,A.M.
  TITLE     Androgen-induced proliferative quiescence in prostate cancer cells:
            the role of AS3 as its mediator
  JOURNAL   Proc Natl Acad Sci U S A 97 (18), 10185-10190 (2000)
   PUBMED   10963680
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000012.1 and CK357543.1.
            
            On Aug 21, 2007 this sequence version replaced XP_001070651.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA5760383, SAMEA5760386
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p12"
     Protein         1..1450
                     /product="sister chromatid cohesion protein PDS5 homolog B
                     isoform 1"
                     /note="androgen-induced prostate proliferative shutoff
                     associated protein; sister chromatid cohesion protein PDS5
                     homolog B; androgen-induced shutoff 3; androgen-induced
                     prostate proliferative shutoff-associated protein AS3;
                     PDS5, regulator of cohesion maintenance, homolog B"
                     /calculated_mol_wt=164388
     Region          29..1099
                     /region_name="PDS5"
                     /note="Sister chromatid cohesion protein PDS5 protein;
                     pfam20168"
                     /db_xref="CDD:466319"
     Region          240..261
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(253..254,257,260..261,290..291,294,297..298,303,
                     331..332,335,338,368..369,372,375..376,406..407)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          273..303
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          313..339
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          350..376
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          383..419
                     /region_name="HEAT. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1136
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Region          <1186..1411
                     /region_name="DUF4045"
                     /note="Domain of unknown function (DUF4045); pfam13254"
                     /db_xref="CDD:433066"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4VA53; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1369
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4VA53; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1372
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NTI5; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4VA53; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     Site            1422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4VA53; propagated from
                     UniProtKB/Swiss-Prot (Q6TRW4.2)"
     CDS             1..1450
                     /gene="Pds5b"
                     /gene_synonym="Aprin; AS3; CG008"
                     /coded_by="NM_001102383.2:10..4362"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:304218"
                     /db_xref="RGD:1310838"
ORIGIN      
        1 mahsktrtnd gkityppgvk eisdkiskee mvrrlkmvvk tfmdmdqdse eekelylnla
       61 lhlasdfflk hpdkdvrllv accladifri yapeapytsp dklkdifmfi trqlkgledt
      121 kspqfnryfy lleniawvks ynicfeleds neiftqlyrt lfsvinnghn qkvhmhmvdl
      181 mssiicegdt vsqelldtvl vnlvpahknl nkqaydlaka llkrtaqaie pyitnffnqv
      241 lmlgktsisd lsehvfdlil elynidshll lsvlpqlefk lksndneerl qvvkllakmf
      301 gakdselasq nkplwqcylg rfndihvpir lecvkfashc lmnhpdlakd lteylkvrsh
      361 dpeeairhdv ivsivtaakk dillvndhll nfvrertldk rwrvrkeamm glaqiykkya
      421 lqsaagkdaa kqicwvkdkl lhiyyqnsid drllverifa qymvphnlet termkclyyl
      481 yatldlnavk alnemwkcqn llrhqvkdll dlikqpktda svkaifskvm vitrnlpdpg
      541 kaqdfmkkft qvleddekir kqlealvspt csckqaegcv reitkklgnp kqptnpflem
      601 ikflleriap vhidtesisa likqvnksid gtaddedegv ptdqairagl ellkvlsfth
      661 pisfhsaetf esllaclkmd dekvaeaalq ifkntgskie edfphirsal lpvlhhkskk
      721 gpprqakyai hcihaifssk etqfaqifep lhksldpsnl ehlitplvti ghiallapdq
      781 faaplkslva tfivkdllmn drlpgkkttk lwvpdeevsp etmvkiqaik mmvrwllgmk
      841 nnhsksgtst lrllttilhs dgdlteqgki skpdmsrlrl aagsaivkla qepcyheiit
      901 leqyqlcala indecyqvrq vfaqklhkgl srlrlpleym aicalcakdp vkerraharq
      961 clvknitvrr eylkqhaavs ekllsllpey vvpytihlla hdpdyvkvqd ieqlkdvkec
     1021 lwfvleilma knennshafi rkmvenikqt kdaqgpddtk mneklytvcd vamniimsks
     1081 ttyslespkd pvlparfftq pdknfsntkn ylppemksff tpgkpktanv lgavnkplss
     1141 agkqsqtkss rmetvsnass ssnpsspgri kgrqaslqss pkfktedscs pvddplpgst
     1201 rgkcdqsaly qselekprsr kkasvtdpee klgmddlskl vqeqkpkgsq rgrkrghaas
     1261 eseeqqwpee krhkeellgn edeqnsppkk gkrgrppkpl ggtskeepvv ktskkgnkkk
     1321 pappvvdede eeerqmgnte qkskskqqrt skraqqraes petsavestq stpqkgrgrp
     1381 sktpspsqpk knirvgrskq vatkendsse emdvlqassp vsddttqega eeedisagnv
     1441 rrrsskrerr
//
LOCUS       NP_113748                329 aa            linear   ROD 28-APR-2025
DEFINITION  cathepsin K precursor [Rattus norvegicus].
ACCESSION   NP_113748
VERSION     NP_113748.1
DBSOURCE    REFSEQ: accession NM_031560.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Brito,V.G.B., Patrocinio,M.S., de Sousa,M.C.L., Barreto,A.E.A.,
            Frasnelli,S.C.T., Lara,V.S., Santos,C.F. and Oliveira,S.H.P.
  TITLE     Telmisartan Prevents Alveolar Bone Loss by Decreasing the
            Expression of Osteoclasts Markers in Hypertensive Rats With
            Periodontal Disease
  JOURNAL   Front Pharmacol 11, 579926 (2020)
   PUBMED   33364953
  REMARK    Erratum:[Front Pharmacol. 2021 Feb 19;11:635927. doi:
            10.3389/fphar.2020.635927. PMID: 33679393]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Danyukova,T., Ariunbat,K., Thelen,M., Brocke-Ahmadinejad,N.,
            Mole,S.E. and Storch,S.
  TITLE     Loss of CLN7 results in depletion of soluble lysosomal proteins and
            impaired mTOR reactivation
  JOURNAL   Hum Mol Genet 27 (10), 1711-1722 (2018)
   PUBMED   29514215
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Liu,N., Zhang,T., Cao,B.R., Luan,F.Y., Liu,R.X., Yin,H.R. and
            Wang,W.B.
  TITLE     Icariin possesses chondroprotective efficacy in a rat model of
            dexamethasone-induced cartilage injury through the activation of
            miR-206 targeting of cathepsin K
  JOURNAL   Int J Mol Med 41 (2), 1039-1047 (2018)
   PUBMED   29207029
  REMARK    GeneRIF: the present study identified icariin as a novel
            therapeutic agent in DXM-induced cartilage injury in rats, and
            revealed that the activation of miR-206 targeting of cathepsin K
            may be responsible for the chondroprotective efficacy of icariin
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Seto,S.P., Parks,A.N., Qiu,Y., Soslowsky,L.J., Karas,S., Platt,M.O.
            and Temenoff,J.S.
  TITLE     Cathepsins in Rotator Cuff Tendinopathy: Identification in Human
            Chronic Tears and Temporal Induction in a Rat Model
  JOURNAL   Ann Biomed Eng 43 (9), 2036-2046 (2015)
   PUBMED   25558848
  REMARK    GeneRIF: Cathepsins in Rotator Cuff Tendinopathy: Identification in
            Human Chronic Tears and Temporal Induction in a Rat Model.
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Ivatt,R.M., Sanchez-Martinez,A., Godena,V.K., Brown,S., Ziviani,E.
            and Whitworth,A.J.
  TITLE     Genome-wide RNAi screen identifies the Parkinson disease GWAS risk
            locus SREBF1 as a regulator of mitophagy
  JOURNAL   Proc Natl Acad Sci U S A 111 (23), 8494-8499 (2014)
   PUBMED   24912190
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Anway,M.D., Wright,W.W., Zirkin,B.R., Korah,N., Mort,J.S. and
            Hermo,L.
  TITLE     Expression and localization of cathepsin k in adult rat sertoli
            cells
  JOURNAL   Biol Reprod 70 (3), 562-569 (2004)
   PUBMED   14585819
  REMARK    GeneRIF: cathepsin K, in both its secreted and lysosomal forms, may
            play a role in the degradation of Sertoli cell residual bodies
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Friedrichs,B., Tepel,C., Reinheckel,T., Deussing,J., von Figura,K.,
            Herzog,V., Peters,C., Saftig,P. and Brix,K.
  TITLE     Thyroid functions of mouse cathepsins B, K, and L
  JOURNAL   J Clin Invest 111 (11), 1733-1745 (2003)
   PUBMED   12782676
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Tepel,C., Bromme,D., Herzog,V. and Brix,K.
  TITLE     Cathepsin K in thyroid epithelial cells: sequence, localization and
            possible function in extracellular proteolysis of thyroglobulin
  JOURNAL   J Cell Sci 113 Pt 24, 4487-4498 (2000)
   PUBMED   11082042
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Xia,L., Kilb,J., Wex,H., Li,Z., Lipyansky,A., Breuil,V., Stein,L.,
            Palmer,J.T., Dempster,D.W. and Bromme,D.
  TITLE     Localization of rat cathepsin K in osteoclasts and resorption pits:
            inhibition of bone resorption and cathepsin K-activity by peptidyl
            vinyl sulfones
  JOURNAL   Biol Chem 380 (6), 679-687 (1999)
   PUBMED   10430032
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Lazner,F., Gowen,M., Pavasovic,D. and Kola,I.
  TITLE     Osteopetrosis and osteoporosis: two sides of the same coin
  JOURNAL   Hum Mol Genet 8 (10), 1839-1846 (1999)
   PUBMED   10469835
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078793.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078793.1, FQ222438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..329
                     /product="cathepsin K precursor"
                     /EC_number="3.4.22.38"
                     /calculated_mol_wt=35012
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1797
     Region          26..85
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35186.1)"
     mat_peptide     115..329
                     /product="Cathepsin K. /id=PRO_0000026308"
                     /note="propagated from UniProtKB/Swiss-Prot (O35186.1)"
                     /calculated_mol_wt=23487
     Region          115..327
                     /region_name="Peptidase_C1"
                     /note="Papain family cysteine protease; pfam00112"
                     /db_xref="CDD:425470"
     Site            order(133,139,276,296)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            order(181..182,248,274,277,323)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35186.1)"
     CDS             1..329
                     /gene="Ctsk"
                     /coded_by="NM_031560.2:74..1063"
                     /db_xref="GeneID:29175"
                     /db_xref="RGD:61810"
ORIGIN      
        1 mwvfkflllp vvsfalspee tldtqwelwk kthgkqynsk vdeisrrliw eknlkkisvh
       61 nleaslgaht yelamnhlgd mtseevvqkm tglrvppsrs fsndtlytpe wegrvpdsid
      121 yrkkgyvtpv knqgqcgscw afssagaleg qlkkktgkll alspqnlvdc vsenygcggg
      181 ymttafqyvq qnggidseda ypyvgqdesc mynatakaak crgyreipvg nekalkrava
      241 rvgpvsvsid asltsfqfys rgvyydencd rdnvnhavlv vgygtqkgnk ywiiknswge
      301 swgnkgyvll arnknnacgi tnlasfpkm
//
LOCUS       NP_663702                210 aa            linear   ROD 28-APR-2025
DEFINITION  four and a half LIM domains protein 1 isoform 2 [Rattus
            norvegicus].
ACCESSION   NP_663702
VERSION     NP_663702.1
DBSOURCE    REFSEQ: accession NM_145669.3
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Li,Y., Pu,G., Chen,C. and Yang,L.
  TITLE     Inhibition of FHL1 inhibits cigarette smoke extract-induced
            proliferation in pulmonary arterial smooth muscle cells
  JOURNAL   Mol Med Rep 12 (3), 3801-3808 (2015)
   PUBMED   25975448
  REMARK    GeneRIF: FHL1 may be involved in excessive cell proliferation and
            may represent a potential therapeutic target for pulmonary
            hypertension.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Wang,L., Miao,J., Li,L., Wu,D., Zhang,Y., Peng,Z., Zhang,L.,
            Yuan,Z. and Sun,K.
  TITLE     Identification of an FHL1 protein complex containing gamma-actin
            and non-muscle myosin IIB by analysis of protein-protein
            interactions
  JOURNAL   PLoS One 8 (11), e79551 (2013)
   PUBMED   24265776
  REMARK    GeneRIF: FHL1 exists as part of a complex, which binds gamma-actin
            and non-muscle myosin IIB
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Yue,J., Guan,J., Wang,X., Zhang,L., Yang,Z., Ao,Q., Deng,Y., Zhu,P.
            and Wang,G.
  TITLE     MicroRNA-206 is involved in hypoxia-induced pulmonary hypertension
            through targeting of the HIF-1alpha/Fhl-1 pathway
  JOURNAL   Lab Invest 93 (7), 748-759 (2013)
   PUBMED   23628900
  REMARK    GeneRIF: Hypoxia-induced downregulation of miR-206 promotes
            pulmonary hypertension by targeting the HIF-1alpha/Fhl-1 pathway in
            pulmonary artery smooth muscle cells.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Niu,C., Liang,C., Guo,J., Cheng,L., Zhang,H., Qin,X., Zhang,Q.,
            Ding,L., Yuan,B., Xu,X., Li,J., Lin,J. and Ye,Q.
  TITLE     Downregulation and growth inhibitory role of FHL1 in lung cancer
  JOURNAL   Int J Cancer 130 (11), 2549-2556 (2012)
   PUBMED   21702045
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Wang,L.L., Qiu,G.R., Fu,W.N., Yuan,Z.W. and Sun,K.L.
  TITLE     Transcriptional regulation of Fhl1 by estradiol in rat
            myoblastocytes
  JOURNAL   Steroids 75 (4-5), 368-372 (2010)
   PUBMED   20149813
  REMARK    GeneRIF: These data indicate that estradiol down-regulates Fhl1
            expression through its binding to the ERbeta.
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Chen,C.N., Ferrington,D.A. and Thompson,L.V.
  TITLE     Carbonic anhydrase III and four-and-a-half LIM protein 1 are
            preferentially oxidized with muscle unloading
  JOURNAL   J Appl Physiol (1985) 105 (5), 1554-1561 (2008)
   PUBMED   18756007
  REMARK    GeneRIF: Carbonic anhydrase III and four-and-a-half LIM protein 1
            are preferentially oxidized with muscle unloading.
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Yang,Z., Browning,C.F., Hallaq,H., Yermalitskaya,L., Esker,J.,
            Hall,M.R., Link,A.J., Ham,A.J., McGrath,M.J., Mitchell,C.A. and
            Murray,K.T.
  TITLE     Four and a half LIM protein 1: a partner for KCNA5 in human atrium
  JOURNAL   Cardiovasc Res 78 (3), 449-457 (2008)
   PUBMED   18281375
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Kang,M.A., Jeoung,N.H., Kim,J.Y., Lee,J.E., Jung,U.J., Choi,M.S.,
            Lee,W.H., Kwon,O.S., Lee,H. and Park,Y.B.
  TITLE     Up-regulation of skeletal muscle LIM protein 1 gene by
            25-hydroxycholesterol may mediate morphological changes of rat
            aortic smooth muscle cells
  JOURNAL   Life Sci 80 (5), 460-467 (2007)
   PUBMED   17161435
  REMARK    GeneRIF: Over-production of SLIM1 in the cells resulted in a change
            in the cell-shape into a spindle-like form.
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Lim,D.S., Roberts,R. and Marian,A.J.
  TITLE     Expression profiling of cardiac genes in human hypertrophic
            cardiomyopathy: insight into the pathogenesis of phenotypes
  JOURNAL   J Am Coll Cardiol 38 (4), 1175-1180 (2001)
   PUBMED   11583900
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FQ119120.1, AY115564.1, BC061782.1 and CK840296.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 3' coding
            region compared to variant 1, which results in a frame-shift and a
            shorter isoform (2) with a distinct C-terminus compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY115564.1, FN803478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..210
                     /product="four and a half LIM domains protein 1 isoform 2"
                     /note="four and a half LIM domains protein 1; skeletal
                     muscle LIM-protein 1; FHL-1"
                     /calculated_mol_wt=23570
     Region          <21..49
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cl02475"
                     /db_xref="CDD:413332"
     Region          56..109
                     /region_name="LIM1_FHL1"
                     /note="The first LIM domain of Four and a half LIM domains
                     protein 1; cd09344"
                     /db_xref="CDD:188730"
     Site            order(56,59,78,81,84,87,105,108)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188730"
     Region          117..174
                     /region_name="LIM2_FHL1"
                     /note="The second LIM domain of Four and a half LIM
                     domains protein 1 (FHL1); cd09424"
                     /db_xref="CDD:188808"
     Site            order(117,120,139,142,145,148,166,169)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188808"
     CDS             1..210
                     /gene="Fhl1"
                     /gene_synonym="SLIM1"
                     /coded_by="NM_145669.3:84..716"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25177"
                     /db_xref="RGD:2615"
ORIGIN      
        1 masqrhsgps sykvgtmsek fdchycrdpl qgkkyvqkdg rhcclkcfdk fcantcvecr
       61 kpisadakev hyknrywhdt cfrcakclhp lasetfvskd gkilcnkcat redsprckgc
      121 fkaivagdqn veykgtiwhk dcftcsnckq vigtgsffpk gedfycvtch etkfakhcvk
      181 cnkglvkapv wwpmkdnpgt ttastaknap
//
LOCUS       NP_446400                172 aa            linear   ROD 28-APR-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB7 [Rattus norvegicus].
ACCESSION   NP_446400
VERSION     NP_446400.1
DBSOURCE    REFSEQ: accession NM_053948.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Knutson,B.A. and Hahn,S.
  TITLE     TFIIB-related factors in RNA polymerase I transcription
  JOURNAL   Biochim Biophys Acta 1829 (3-4), 265-273 (2013)
   PUBMED   22960599
  REMARK    Review article
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Khalyfa,A., Chlon,T., Qiang,H., Agarwal,N. and Cooper,N.G.
  TITLE     Microarray reveals complement components are regulated in the
            serum-deprived rat retinal ganglion cell line
  JOURNAL   Mol Vis 13, 293-308 (2007)
   PUBMED   17356516
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Kershnar,E., Wu,S.Y. and Chiang,C.M.
  TITLE     Immunoaffinity purification and functional characterization of
            human transcription factor IIH and RNA polymerase II from clonal
            cell lines that conditionally express epitope-tagged subunits of
            the multiprotein complexes
  JOURNAL   J Biol Chem 273 (51), 34444-34453 (1998)
   PUBMED   9852112
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Z71925.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z71925.1, FQ224086.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..172
                     /product="DNA-directed RNA polymerase II subunit RPB7"
                     /EC_number="2.7.7.6"
                     /note="RNA polymerase II subunit B7; DNA-directed RNA
                     polymerase II subunit G; polymerase (RNA) II (DNA
                     directed) polypeptide G; polymerase (RNA) II subunit G"
                     /calculated_mol_wt=19163
     Region          1..169
                     /region_name="PTZ00162"
                     /note="DNA-directed RNA polymerase II subunit 7;
                     Provisional"
                     /db_xref="CDD:240298"
     CDS             1..172
                     /gene="Polr2g"
                     /gene_synonym="Rpb7"
                     /coded_by="NM_053948.4:75..593"
                     /db_xref="GeneID:117017"
                     /db_xref="RGD:621284"
ORIGIN      
        1 mfyhislehe illhpryfgp nllntvkqkl ftevegtctg kygfviavtt idnigagviq
       61 pgrgfvlypv kykaivfrpf kgevvdavvt qvnkvglfte igpmscfisr hsipsemefd
      121 pnsnppcykt mdediviqqd deirlkivgt rvdkndifai gslmddylgl vs
//
LOCUS       NP_001013899             585 aa            linear   ROD 28-APR-2025
DEFINITION  clathrin heavy chain linker domain-containing protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001013899 XP_223711
VERSION     NP_001013899.1
DBSOURCE    REFSEQ: accession NM_001013877.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083604.1.
            
            On Apr 20, 2005 this sequence version replaced XP_223711.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083604.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..585
                     /product="clathrin heavy chain linker domain-containing
                     protein 1"
                     /note="uncharacterized protein C2orf63 homolog"
                     /calculated_mol_wt=67412
     Region          28..141
                     /region_name="TSNAXIP1_N"
                     /note="Translin-associated factor X-interacting
                     N-terminus; pfam15739"
                     /db_xref="CDD:464835"
     Region          297..351
                     /region_name="Clathrin_H_link"
                     /note="Clathrin-H-link; pfam13838"
                     /db_xref="CDD:463995"
     CDS             1..585
                     /gene="Clhc1"
                     /gene_synonym="RGD1307937"
                     /coded_by="NM_001013877.1:202..1959"
                     /db_xref="GeneID:289865"
                     /db_xref="RGD:1307937"
ORIGIN      
        1 mptqevkkha vlppiisrnd keflesmqry iitetkrvgc neegppdeyy tiyrnvfdkv
       61 idyvnayksv ltsikkeyda fietvkkgrr nafylhgklk vlaaeptalv yhqrrtiqle
      121 akmriidnns kaiqlqidqm kqlrmeyent evklcasskq lwkpipgmtl qdsvnldaln
      181 nhkqnledkc rklkqdmstm yvsaqkkadl deemivllkr rdiaenlnkd lrfrhqrlqv
      241 ishtlnswmk qnmripfkdv leriqqtkai yghakvvdel feddpnktke aivmlyyier
      301 fhelislgey ekaacfaans pkrilqnagt mnkfkaigkv rgkplplllf feaifntsqa
      361 fkrainvdlt legikcglse erldlvthwv tqakltfsek vgdaicayge qhpyhkskcl
      421 alaqivynec glhkkailcl crqgqfheam ehiqqskdin tddliqlita cpqidlirgl
      481 teerngkppf lsfgltvlhl fsvdmkkigm kllqevskae kdviehlvms dlfcsiekwq
      541 elaniclqng fknlsndims ilrsqagvse iseddttnvm ehvfw
//
LOCUS       NP_001012223             507 aa            linear   ROD 28-APR-2025
DEFINITION  bridging integrator 2 [Rattus norvegicus].
ACCESSION   NP_001012223 XP_345875
VERSION     NP_001012223.1
DBSOURCE    REFSEQ: accession NM_001012223.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Sanchez-Barrena,M.J., Vallis,Y., Clatworthy,M.R., Doherty,G.J.,
            Veprintsev,D.B., Evans,P.R. and McMahon,H.T.
  TITLE     Bin2 is a membrane sculpting N-BAR protein that influences
            leucocyte podosomes, motility and phagocytosis
  JOURNAL   PLoS One 7 (12), e52401 (2012)
   PUBMED   23285027
  REMARK    Erratum:[PLoS One. 2013;8(8).
            doi:10.1371/annotation/3bdc487b-5e25-4cd7-a354-b2952eec943d]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079406.1.
            
            On Feb 11, 2005 this sequence version replaced XP_345875.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q36"
     Protein         1..507
                     /product="bridging integrator 2"
                     /calculated_mol_wt=54987
     Region          30..240
                     /region_name="BAR_Bin2"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Bridging
                     integrator 2; cd07612"
                     /db_xref="CDD:153296"
     Site            order(49,52..53,57,60,63..64,67,77..78,80..81,84..85,
                     87..88,91,99,196,199..200,202,207..208,210..211,214..215,
                     217..218,221..222,224..225,229,232)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153296"
     Site            order(72,79,138,141,144..145,169)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153296"
     Region          271..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBW5; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBW5; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UBW5; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3Z6Q9; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3Z6Q9; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3Z6Q9; propagated from
                     UniProtKB/Swiss-Prot (Q68FR2.1)"
     CDS             1..507
                     /gene="Bin2"
                     /coded_by="NM_001012223.1:43..1566"
                     /db_xref="GeneID:366988"
                     /db_xref="RGD:1306789"
ORIGIN      
        1 maegkaggaa glfakqmqkk fsraqekvlq klgktvetkd erfeqsasnf yqqqaeghrl
       61 ykdlknflsa vkvmresskr vsetlqeiyn sdwdghedlk aivgnndllw edyeekladq
      121 alrtmenyvs qfsevkeria krgrklvdyd sarhhleavq nakkkdeakm akaeedfska
      181 qvvfedlnqe lleelpvlyn srigcyvtvf qnisnlrdvf yremsklnhs lyevmsklek
      241 qhsnkvfvvk glssssrrsl visppvqtct afspvspvts ptspnalsvt sesesvsata
      301 eeltseavge dsceseeslk deeadedqse tssseeeede dededeeesl aacngptptp
      361 aptpapaspa aevksqeeaa pcsptsslgr gqtgkehspp gevvlraras segaeqskrt
      421 asvqrtsapp srppppkasg gglssppgsa easkachpra ssdassdpep petgekegtg
      481 ssgpkephas stksatqvvs ndentel
//
LOCUS       NP_001099867            1047 aa            linear   ROD 28-APR-2025
DEFINITION  [F-actin]-monooxygenase MICAL1 [Rattus norvegicus].
ACCESSION   NP_001099867 XP_001069650 XP_215424
VERSION     NP_001099867.1
DBSOURCE    REFSEQ: accession NM_001106397.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Fremont,S., Hammich,H., Bai,J., Wioland,H., Klinkert,K.,
            Rocancourt,M., Kikuti,C., Stroebel,D., Romet-Lemonne,G.,
            Pylypenko,O., Houdusse,A. and Echard,A.
  TITLE     Oxidation of F-actin controls the terminal steps of cytokinesis
  JOURNAL   Nat Commun 8, 14528 (2017)
   PUBMED   28230050
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Alqassim,S.S., Urquiza,M., Borgnia,E., Nagib,M., Amzel,L.M. and
            Bianchet,M.A.
  TITLE     Modulation of MICAL Monooxygenase Activity by its Calponin Homology
            Domain: Structural and Mechanistic Insights
  JOURNAL   Sci Rep 6, 22176 (2016)
   PUBMED   26935886
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Vitali,T., Maffioli,E., Tedeschi,G. and Vanoni,M.A.
  TITLE     Properties and catalytic activities of MICAL1, the flavoenzyme
            involved in cytoskeleton dynamics, and modulation by its CH, LIM
            and C-terminal domains
  JOURNAL   Arch Biochem Biophys 593, 24-37 (2016)
   PUBMED   26845023
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Van Battum,E.Y., Gunput,R.A., Lemstra,S., Groen,E.J., Yu,K.L.,
            Adolfs,Y., Zhou,Y., Hoogenraad,C.C., Yoshida,Y., Schachner,M.,
            Akhmanova,A. and Pasterkamp,R.J.
  TITLE     The intracellular redox protein MICAL-1 regulates the development
            of hippocampal mossy fibre connections
  JOURNAL   Nat Commun 5, 4317 (2014)
   PUBMED   25007825
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Lundquist,M.R., Storaska,A.J., Liu,T.C., Larsen,S.D., Evans,T.,
            Neubig,R.R. and Jaffrey,S.R.
  TITLE     Redox modification of nuclear actin by MICAL-2 regulates SRF
            signaling
  JOURNAL   Cell 156 (3), 563-576 (2014)
   PUBMED   24440334
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Yamamura,R., Nishimura,N., Nakatsuji,H., Arase,S. and Sasaki,T.
  TITLE     The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates
            the assembly of tight junctions and adherens junctions
  JOURNAL   Mol Biol Cell 19 (3), 971-983 (2008)
   PUBMED   18094055
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Pasterkamp,R.J., Dai,H.N., Terman,J.R., Wahlin,K.J., Kim,B.,
            Bregman,B.S., Popovich,P.G. and Kolodkin,A.L.
  TITLE     MICAL flavoprotein monooxygenases: expression during neural
            development and following spinal cord injuries in the rat
  JOURNAL   Mol Cell Neurosci 31 (1), 52-69 (2006)
   PUBMED   16230022
  REMARK    GeneRIF: Tesults implicate MICALs in neuronal regeneration and
            support the possibility to attenuate axon repulsion in the injured
            spinal cord.
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Nadella,M., Bianchet,M.A., Gabelli,S.B., Barrila,J. and Amzel,L.M.
  TITLE     Structure and activity of the axon guidance protein MICAL
  JOURNAL   Proc Natl Acad Sci U S A 102 (46), 16830-16835 (2005)
   PUBMED   16275926
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   Fischer,J., Weide,T. and Barnekow,A.
  TITLE     The MICAL proteins and rab1: a possible link to the cytoskeleton?
  JOURNAL   Biochem Biophys Res Commun 328 (2), 415-423 (2005)
   PUBMED   15694364
  REMARK    GeneRIF: Using the microtubule depolymerizing drug nocodazole we
            detected a link between MICAL-1 and -3, and the microtubule
            cytoskeleton.
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Suzuki,T., Nakamoto,T., Ogawa,S., Seo,S., Matsumura,T.,
            Tachibana,K., Morimoto,C. and Hirai,H.
  TITLE     MICAL, a novel CasL interacting molecule, associates with vimentin
  JOURNAL   J Biol Chem 277 (17), 14933-14941 (2002)
   PUBMED   11827972
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH474025.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001069650.1, XP_215424.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..1047
                     /product="[F-actin]-monooxygenase MICAL1"
                     /EC_number="1.6.3.1"
                     /EC_number="1.14.13.225"
                     /note="NEDD9 interacting protein with calponin homology
                     and LIM domains; molecule interacting with CasL protein 1;
                     protein-methionine sulfoxide oxidase MICAL1;
                     F-actin-monooxygenase MICAL1; microtubule associated
                     monoxygenase, calponin and LIM domain containing 1;
                     [F-actin]-methionine sulfoxide oxidase MICAL1"
                     /calculated_mol_wt=116541
     Region          1..489
                     /region_name="Monooxygenase domain.
                     /evidence=ECO:0000250|UniProtKB:Q8VDP3"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          83..>220
                     /region_name="UbiH"
                     /note="2-polyprenyl-6-methoxyphenol hydroxylase and
                     related FAD-dependent oxidoreductases [Coenzyme transport
                     and metabolism, Energy production and conversion];
                     COG0654"
                     /db_xref="CDD:440419"
     Region          85..>122
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          506..611
                     /region_name="CH_MICAL1"
                     /note="calponin homology (CH) domain found in molecule
                     interacting with CasL protein 1; cd21196"
                     /db_xref="CDD:409045"
     Site            order(510,513,563,565..566,569..570,572,581..589,595,
                     597..598,600..601,604..605,608)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409045"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8TDZ2; propagated from
                     UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          644..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          681..734
                     /region_name="LIM_Mical_like"
                     /note="The LIM domain of Mical (molecule interacting with
                     CasL) like family; cd09358"
                     /db_xref="CDD:188744"
     Site            order(681,684,702,705,708,711,731,734)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188744"
     Region          739..787
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDP3; propagated from
                     UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDP3; propagated from
                     UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Site            816
                     /site_type="other"
                     /note="Important for interaction with ARHGAP26 AND
                     ARHGAP10. /evidence=ECO:0000250|UniProtKB:Q8TDZ2;
                     propagated from UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          849..872
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZBP4.1)"
     Region          921..1045
                     /region_name="bMERB_dom"
                     /note="Bivalent Mical/EHBP Rab binding domain; pfam12130"
                     /db_xref="CDD:463467"
     CDS             1..1047
                     /gene="Mical1"
                     /gene_synonym="MICAL-1; Nical"
                     /coded_by="NM_001106397.1:252..3395"
                     /db_xref="GeneID:294520"
                     /db_xref="RGD:1309386"
ORIGIN      
        1 masptstnpa hdhfetfvqa qlcqdvlssf qglcralgve sggglpqyhk ikaqlnywsa
       61 kslwakldkr asqpayqqgq actntkclvv gagpcglraa velallgarv vlvekrtkfs
      121 rhnvlhlwpf tihdlralga kkfygrfctg tldhisirql qllllkvall lgveihwgft
      181 ftglqpppkk gsgwrariqp sppaqlasye fdvlisaggg kfvpegftir emrgklaigi
      241 tanfvngrtv eetqvpeisg variynqkff qsllkatgid lenivyykdd thyfvmtakk
      301 qcllrlgvlr qdlpetdqll gkanvvpeal qqfaraaadf atqgklgkle faqdargrpd
      361 vaafdftsmm rsessariqe khgarlllgl vgdclvepfw plgtgvargf laafdaawmv
      421 krwaegtgpl ellaeresly qllsqtspen mhrnvaqygl dpatrypnln lravtpnqvq
      481 dlydimdkeh arkksdetda rktttgsagt eellhwcqeq tagfpgvsvt dfssswadgr
      541 alcalvhrlq pgllepselq gmsaleataw alrvaeyelg iipvlsaqav vagsdplgli
      601 aylshfhsaf kntphssglv sqphgtpsai lflgklqrsl qrtrtkveee tpcteeppvs
      661 epsvppalps eheeagaedv celcgkrlyi lerfcvdghf fhrgcfccrt ceatlrpggy
      721 gqypgdgyfy clqhlpqedq keadnngspe nqelptpgds ttqsgpsspv ppvteaspvp
      781 spsqparrli rlssverlrl sslniipdsg vepppkpprs cldlaqeslk ssfmgwgvlr
      841 apqvpeaiek geeeeeeeee eeeeeeelpp plaleveqsl ltlaknsgdm tkyptwrrtl
      901 mrrakeeemk rfckaqaiqr rlneieaamr eletegmkle valrkesssp ekqkklwleq
      961 llqliqkkns lvteeaelmi tvqeldleek qrqldhefrg inreetlktq adrlsedrvl
     1021 rklldvvnqr daliqfqeer rlrempv
//
LOCUS       NP_001230463             175 aa            linear   ROD 28-APR-2025
DEFINITION  UPF0696 protein C11orf68 homolog isoform 2 [Rattus norvegicus].
ACCESSION   NP_001230463
VERSION     NP_001230463.1
DBSOURCE    REFSEQ: accession NM_001243534.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Bitto,E., Bingman,C.A., Robinson,H., Allard,S.T., Wesenberg,G.E.
            and Phillips,G.N. Jr.
  TITLE     The structure at 2.5 A resolution of human basophilic
            leukemia-expressed protein BLES03
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 61 (Pt 9), 812-817
            (2005)
   PUBMED   16511166
  REMARK    GeneRIF: Structural characterization of the human ortholog.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region, which results in a frameshift, compared to
            variant 1. The encoded isoform (2) is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093387.1, FN802574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..175
                     /product="UPF0696 protein C11orf68 homolog isoform 2"
                     /note="basophilic leukemia-expressed protein Bles03;
                     UPF0696 protein C11orf68 homolog"
                     /calculated_mol_wt=18912
     CDS             1..175
                     /gene="Bles03"
                     /coded_by="NM_001243534.1:110..637"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:266609"
                     /db_xref="RGD:628612"
ORIGIN      
        1 maaaaaavag agrgggggad pgqersrars wvgaersegr sslttgwnqm kswkrrtlqv
       61 vvrmasllst wlqrpwqltw tpgwylmpvl hlpqswmpgw psthhlklla mgtqvhptln
      121 lwaglqpmgr vtppiqgmyk gcrqpgrlcr pvgdpshqvp caswpsptmc spasg
//
LOCUS       NP_001101073             300 aa            linear   ROD 28-APR-2025
DEFINITION  F-box/LRR-repeat protein 15 [Rattus norvegicus].
ACCESSION   NP_001101073 XP_001066947 XP_347195
VERSION     NP_001101073.1
DBSOURCE    REFSEQ: accession NM_001107603.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cui,Y., He,S., Xing,C., Lu,K., Wang,J., Xing,G., Meng,A., Jia,S.,
            He,F. and Zhang,L.
  TITLE     SCFFBXL(1) regulates BMP signalling by directing the degradation of
            HECT-type ubiquitin ligase Smurf1
  JOURNAL   EMBO J 30 (13), 2675-2689 (2011)
   PUBMED   21572392
  REMARK    GeneRIF: FBXL15 is a key regulator of BMP signalling during
            embryonic development and adult bone formation.
            Erratum:[EMBO J. 2011;30(13):2748]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473986.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_347195.1, XP_001066947.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ235302.1, SRR8487227.72574.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q54"
     Protein         1..300
                     /product="F-box/LRR-repeat protein 15"
                     /note="F-box only protein 37"
                     /calculated_mol_wt=33049
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H469; propagated from
                     UniProtKB/Swiss-Prot (D4ABB4.1)"
     Region          19..62
                     /region_name="F-box_FBXL15"
                     /note="F-box domain found in F-box/LRR-repeat protein 15
                     (FBXL15) and similar proteins; cd22126"
                     /db_xref="CDD:438898"
     Site            order(22,28,31..32,35..36,40,42..43,47..49,51)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438898"
     Region          62..88
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <71..146
                     /region_name="FBXL3_LRR-like"
                     /note="Leucine-rich repeat domain of FBXL3 and related
                     proteins; cl45928"
                     /db_xref="CDD:480268"
     Region          89..115
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          113..269
                     /region_name="Interaction with SMURF1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (D4ABB4.1)"
     Region          116..141
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <139..>268
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          142..167
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          168..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          195..220
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          221..245
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..300
                     /gene="Fbxl15"
                     /gene_synonym="RGD1306444"
                     /coded_by="NM_001107603.1:292..1194"
                     /db_xref="GeneID:309453"
                     /db_xref="RGD:1306444"
ORIGIN      
        1 meppmeqsgg eqepgavrll dlpwedvllp hvlnwvplrq llrlqrvsra fralvqlhla
       61 rlrrfdaaqv gpqipraalv rllrdaeglq elalapchew lldedlvpvl arnpqlrsva
      121 lagcgqlsrr algalaegcp rlqrislahc dwvdglalrg ladrcpalee ldltacrqlk
      181 deaivylaqr rgaglrslsl avnanvgdta vqelarncpq lehldltgcl rvgsdgvrtl
      241 aeycpalrsl rvrhchhvae pslsrlrkrg vdidvepplh qalvllqdma gfapfvnlqv
//
LOCUS       NP_001012187             586 aa            linear   ROD 28-APR-2025
DEFINITION  kelch-like protein 7 [Rattus norvegicus].
ACCESSION   NP_001012187 XP_342617
VERSION     NP_001012187.1
DBSOURCE    REFSEQ: accession NM_001012187.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Angius,A., Uva,P., Buers,I., Oppo,M., Puddu,A., Onano,S.,
            Persico,I., Loi,A., Marcia,L., Hohne,W., Cuccuru,G., Fotia,G.,
            Deiana,M., Marongiu,M., Atalay,H.T., Inan,S., El Assy,O.,
            Smit,L.M., Okur,I., Boduroglu,K., Utine,G.E., Kilic,E., Zampino,G.,
            Crisponi,G., Crisponi,L. and Rutsch,F.
  TITLE     Bi-allelic Mutations in KLHL7 Cause a Crisponi/CISS1-like Phenotype
            Associated with Early-Onset Retinitis Pigmentosa
  JOURNAL   Am J Hum Genet 99 (1), 236-245 (2016)
   PUBMED   27392078
  REMARK    Erratum:[Am J Hum Genet. 2018 Apr 5;102(4):713. doi:
            10.1016/j.ajhg.2018.03.020. PMID: 29625027]
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Kigoshi,Y., Tsuruta,F. and Chiba,T.
  TITLE     Ubiquitin ligase activity of Cul3-KLHL7 protein is attenuated by
            autosomal dominant retinitis pigmentosa causative mutation
  JOURNAL   J Biol Chem 286 (38), 33613-33621 (2011)
   PUBMED   21828050
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083903.1.
            
            On Feb 11, 2005 this sequence version replaced XP_342617.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083903.1, SRR8487230.131692.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q11"
     Protein         1..586
                     /product="kelch-like protein 7"
                     /note="kelch-like 7"
                     /calculated_mol_wt=65839
     Region          23..148
                     /region_name="BTB_POZ_KLHL7"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 7 (KLHL7); cd18237"
                     /db_xref="CDD:349546"
     Region          37..577
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          140..237
                     /region_name="BACK_KLHL7"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 7 (KLHL7); cd18447"
                     /db_xref="CDD:350522"
     Region          294..336
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     Region          337..382
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     Region          371..416
                     /region_name="Kelch_1"
                     /note="Kelch motif; pfam01344"
                     /db_xref="CDD:396078"
     Region          372..416
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          383..430
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     Region          420..468
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          431..481
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     Region          471..515
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          483..528
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     Region          530..575
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XHZ6.1)"
     CDS             1..586
                     /gene="Klhl7"
                     /coded_by="NM_001012187.1:26..1786"
                     /db_xref="GeneID:362303"
                     /db_xref="RGD:1305564"
ORIGIN      
        1 matsgvekss kkktekklaa reeakllagf mgvmnnmrkq rtlcdvilmv qerkipahrv
       61 vlaaashffn lmfttnmles ksfevelkda epdiieqlve faytarisvn snnvqsllda
      121 anqyqiepvk kmcvdflkeq vdasnclgis vlaecldcpe lkstaddfih qhftevyktd
      181 eflqldvkrv thllsqdtlt vraedqvyda avrwlkydep nrqpfmvdil akvrfplisk
      241 nflsktvqae pliqdnpecl kmvisgmryh llspedreel aggtrprrkk hdyrialfgg
      301 sqpqscryfn pkdyswtdir cpfekrrdaa cvfwdnvvyi lggsqlfpik rmdcynvvkd
      361 swysklgppt prdslaacaa egkiytsggs evgnsalylf ecydtrtesw htkpsmltqr
      421 cshgmveang liyvcggslg nnvsgrvlss cevydpatet wtelcsmiep rknhglvfvk
      481 dkifavggqn glggldnvey ydiklnewkm vspmpwrgvt vkcaavgsvi yvlagfqgvg
      541 rlghileynt etdkwvansk vrafpvtscl icvvdtcgan eetlet
//
LOCUS       NP_001028837             883 aa            linear   ROD 28-APR-2025
DEFINITION  brevican core protein isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_001028837 XP_579358
VERSION     NP_001028837.1
DBSOURCE    REFSEQ: accession NM_001033665.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Wohl,S.G., Jorstad,N.L., Levine,E.M. and Reh,T.A.
  TITLE     Muller glial microRNAs are required for the maintenance of glial
            homeostasis and retinal architecture
  JOURNAL   Nat Commun 8 (1), 1603 (2017)
   PUBMED   29150673
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Favuzzi,E., Marques-Smith,A., Deogracias,R., Winterflood,C.M.,
            Sanchez-Aguilera,A., Mantoan,L., Maeso,P., Fernandes,C., Ewers,H.
            and Rico,B.
  TITLE     Activity-Dependent Gating of Parvalbumin Interneuron Function by
            the Perineuronal Net Protein Brevican
  JOURNAL   Neuron 95 (3), 639-655 (2017)
   PUBMED   28712654
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Dwyer,C.A., Bi,W.L., Viapiano,M.S. and Matthews,R.T.
  TITLE     Brevican knockdown reduces late-stage glioma tumor aggressiveness
  JOURNAL   J Neurooncol 120 (1), 63-72 (2014)
   PUBMED   25052349
  REMARK    GeneRIF: High Brevican expression is associated with glioma tumor
            aggressiveness.
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Lu,R., Wu,C., Guo,L., Liu,Y., Mo,W., Wang,H., Ding,J., Wong,E.T.
            and Yu,M.
  TITLE     The role of brevican in glioma: promoting tumor cell motility in
            vitro and in vivo
  JOURNAL   BMC Cancer 12, 607 (2012)
   PUBMED   23253190
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Morales,D.M., Townsend,R.R., Malone,J.P., Ewersmann,C.A.,
            Macy,E.M., Inder,T.E. and Limbrick,D.D. Jr.
  TITLE     Alterations in protein regulators of neurodevelopment in the
            cerebrospinal fluid of infants with posthemorrhagic hydrocephalus
            of prematurity
  JOURNAL   Mol Cell Proteomics 11 (6), M111.011973 (2012)
   PUBMED   22186713
REFERENCE   6  (residues 1 to 883)
  AUTHORS   Aspberg,A., Miura,R., Bourdoulous,S., Shimonaka,M., Heinegard,D.,
            Schachner,M., Ruoslahti,E. and Yamaguchi,Y.
  TITLE     The C-type lectin domains of lecticans, a family of aggregating
            chondroitin sulfate proteoglycans, bind tenascin-R by
            protein-protein interactions independent of carbohydrate moiety
  JOURNAL   Proc Natl Acad Sci U S A 94 (19), 10116-10121 (1997)
   PUBMED   9294172
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Yamada,H., Watanabe,K., Shimonaka,M., Yamasaki,M. and Yamaguchi,Y.
  TITLE     cDNA cloning and the identification of an aggrecanase-like cleavage
            site in rat brevican
  JOURNAL   Biochem Biophys Res Commun 216 (3), 957-963 (1995)
   PUBMED   7488217
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Seidenbecher,C.I., Richter,K., Rauch,U., Fassler,R., Garner,C.C.
            and Gundelfinger,E.D.
  TITLE     Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs
            as secreted and cell surface glycosylphosphatidylinositol-anchored
            isoforms
  JOURNAL   J Biol Chem 270 (45), 27206-27212 (1995)
   PUBMED   7592978
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Jaworski,D.M., Kelly,G.M. and Hockfield,S.
  TITLE     The CNS-specific hyaluronan-binding protein BEHAB is expressed in
            ventricular zones coincident with gliogenesis
  JOURNAL   J Neurosci 15 (2), 1352-1362 (1995)
   PUBMED   7869103
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Jaworski,D.M., Kelly,G.M. and Hockfield,S.
  TITLE     BEHAB, a new member of the proteoglycan tandem repeat family of
            hyaluronan-binding proteins that is restricted to the brain
  JOURNAL   J Cell Biol 125 (2), 495-509 (1994)
   PUBMED   7512973
  REMARK    Erratum:[J Cell Biol 1997 Apr 21;137(2):521]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z28366.1, CB577797.1, U37142.1, CB784255.1 and CB810773.1.
            
            On Sep 22, 2005 this sequence version replaced XP_579358.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U37142.1, X79881.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..883
                     /product="brevican core protein isoform 1 precursor"
                     /note="brevican (brain specific proteoglycan in the
                     aggrecan family); brevican core protein; brain-enriched
                     hyaluronan-binding protein; brevican core protein-like"
                     /calculated_mol_wt=93816
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2204
     mat_peptide     23..883
                     /product="Brevican core protein. /id=PRO_0000017513"
                     /note="propagated from UniProtKB/Swiss-Prot (P55068.2)"
                     /calculated_mol_wt=93816
     Region          40..158
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          52..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          75..79
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          119..123
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55068.2)"
     Region          133..138
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..154
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          156..250
                     /region_name="Link_domain_CSPGs_modules_1_3"
                     /note="this extracellular link domain is found in the
                     first and third link modules of the chondroitin sulfate
                     proteoglycan core protein (CSPG) aggrecan. In addition, it
                     is found in the first link module of three other CSPGs:
                     versican, neurocan, and brevican; cd03517"
                     /db_xref="CDD:239594"
     Site            166..167
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239594"
     Region          257..352
                     /region_name="Link_domain_CSPGs_modules_2_4"
                     /note="this link domain is found in the second and fourth
                     link modules of the chondroitin sulfate proteoglycan core
                     protein (CSPG) aggrecan and, in the second link module of
                     three other CSPGs: versican, neurocan, and brevican. The
                     link domain is a hyaluronan...; cd03520"
                     /db_xref="CDD:239597"
     Site            264..265
                     /site_type="other"
                     /note="putative hyaluronan binding site [chemical
                     binding]"
                     /db_xref="CDD:239597"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55068.2)"
     Region          356..>630
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          389..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55068.2)"
     Site            413
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000250|UniProtKB:Q96GW7; propagated from
                     UniProtKB/Swiss-Prot (P55068.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P55068.2)"
     Region          485..>615
                     /region_name="Treacle"
                     /note="Treacher Collins syndrome protein Treacle;
                     pfam03546"
                     /db_xref="CDD:460967"
     Region          626..655
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          664..787
                     /region_name="CLECT"
                     /note="C-type lectin (CTL)/C-type lectin-like (CTLD)
                     domain; cl02432"
                     /db_xref="CDD:470576"
     Site            order(758,762,764,770,772..775,778..780)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153057"
     Region          791..848
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(801,821)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          859..883
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55068.2)"
     CDS             1..883
                     /gene="Bcan"
                     /gene_synonym="ALPBRE; BEHAB"
                     /coded_by="NM_001033665.1:256..2907"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:25393"
                     /db_xref="RGD:2194"
ORIGIN      
        1 miplllslla alvltqapaa laddlkedss edrafrvrig aaqlrgvlgg alaipchvhh
       61 lrpppsrraa pgfprvkwtf lsgdrevevl varglrvkvn eayrfrvalp aypasltdvs
      121 lvlselrpnd sgvyrcevqh giddssdave vkvkgvvfly regsaryafs fagaqeacar
      181 igariatpeq lyaaylggye qcdagwlsdq tvrypiqnpr eacygdmdgy pgvrnygvvg
      241 pddlydvycy aedlngelfl gappgkltwe eardyclerg aqiastgqly aawnggldrc
      301 spgwladgsv rypiitpsqr cggglpgvkt lflfpnqtgf pskqnrfnvy cfrdsahpsa
      361 fseasspasd gleaivtvte kleelqlpqe avesesrgai ysipitedgg ggsstpedpa
      421 eaprtplese tqsvapptgs seeegealee eerfkdtetp keekeqenlw vwptelsspl
      481 ptgletehsl sqvsppaqav lqlgaspspr pprvhgppae tlqppregsl tstpdgarev
      541 agetgspels gvpreseeag sssledgpsl lpatwapvgt reletpseek sgrtvltgts
      601 vqaqpvlptd sasrggvava pssgdcipsp chnggtclee kegfrclclp gyggdlcdvg
      661 lhfcspgwea fqgacykhfs trrsweeaes qcralgahlt sictpeeqdf vndryreyqw
      721 iglndrtieg dflwsdgapl lyenwnpgqp dsyflsgenc vvmvwhdqgq wsdvpcnyhl
      781 sytckmglvs cgpppqlpla qifgrprlry avdtvlryrc rdglaqrnlp lircqenglw
      841 eapqiscvpr rparalrsmt apegprgqlp rqrkalltpp ssl
//
LOCUS       NP_001101951             218 aa            linear   ROD 28-APR-2025
DEFINITION  ras-related protein R-Ras [Rattus norvegicus].
ACCESSION   NP_001101951 XP_001080661 XP_341852
VERSION     NP_001101951.1
DBSOURCE    REFSEQ: accession NM_001108481.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Flex,E., Jaiswal,M., Pantaleoni,F., Martinelli,S., Strullu,M.,
            Fansa,E.K., Caye,A., De Luca,A., Lepri,F., Dvorsky,R., Pannone,L.,
            Paolacci,S., Zhang,S.C., Fodale,V., Bocchinfuso,G., Rossi,C.,
            Burkitt-Wright,E.M., Farrotti,A., Stellacci,E., Cecchetti,S.,
            Ferese,R., Bottero,L., Castro,S., Fenneteau,O., Brethon,B.,
            Sanchez,M., Roberts,A.E., Yntema,H.G., Van Der Burgt,I., Cianci,P.,
            Bondeson,M.L., Cristina Digilio,M., Zampino,G., Kerr,B., Aoki,Y.,
            Loh,M.L., Palleschi,A., Di Schiavi,E., Care,A., Selicorni,A.,
            Dallapiccola,B., Cirstea,I.C., Stella,L., Zenker,M., Gelb,B.D.,
            Cave,H., Ahmadian,M.R. and Tartaglia,M.
  TITLE     Activating mutations in RRAS underlie a phenotype within the
            RASopathy spectrum and contribute to leukaemogenesis
  JOURNAL   Hum Mol Genet 23 (16), 4315-4327 (2014)
   PUBMED   24705357
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Ahmed,S.M., Theriault,B.L., Uppalapati,M., Chiu,C.W., Gallie,B.L.,
            Sidhu,S.S. and Angers,S.
  TITLE     KIF14 negatively regulates Rap1a-Radil signaling during breast
            cancer progression
  JOURNAL   J Cell Biol 199 (6), 951-967 (2012)
   PUBMED   23209302
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Sandri,C., Caccavari,F., Valdembri,D., Camillo,C., Veltel,S.,
            Santambrogio,M., Lanzetti,L., Bussolino,F., Ivaska,J. and Serini,G.
  TITLE     The R-Ras/RIN2/Rab5 complex controls endothelial cell adhesion and
            morphogenesis via active integrin endocytosis and Rac signaling
  JOURNAL   Cell Res 22 (10), 1479-1501 (2012)
   PUBMED   22825554
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Wilson,L.S., Baillie,G.S., Pritchard,L.M., Umana,B., Terrin,A.,
            Zaccolo,M., Houslay,M.D. and Maurice,D.H.
  TITLE     A phosphodiesterase 3B-based signaling complex integrates exchange
            protein activated by cAMP 1 and phosphatidylinositol 3-kinase
            signals in human arterial endothelial cells
  JOURNAL   J Biol Chem 286 (18), 16285-16296 (2011)
   PUBMED   21393242
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Willard,F.S., Willard,M.D., Kimple,A.J., Soundararajan,M.,
            Oestreich,E.A., Li,X., Sowa,N.A., Kimple,R.J., Doyle,D.A.,
            Der,C.J., Zylka,M.J., Snider,W.D. and Siderovski,D.P.
  TITLE     Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
            effector
  JOURNAL   PLoS One 4 (3), e4884 (2009)
   PUBMED   19319189
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Carta,C., Pantaleoni,F., Bocchinfuso,G., Stella,L., Vasta,I.,
            Sarkozy,A., Digilio,C., Palleschi,A., Pizzuti,A., Grammatico,P.,
            Zampino,G., Dallapiccola,B., Gelb,B.D. and Tartaglia,M.
  TITLE     Germline missense mutations affecting KRAS Isoform B are associated
            with a severe Noonan syndrome phenotype
  JOURNAL   Am J Hum Genet 79 (1), 129-135 (2006)
   PUBMED   16773572
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Oinuma,I., Ishikawa,Y., Katoh,H. and Negishi,M.
  TITLE     The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein
            for R-Ras
  JOURNAL   Science 305 (5685), 862-865 (2004)
   PUBMED   15297673
  REMARK    GeneRIF: Plexin-B1 mediates Sema4D-induced repulsive axon guidance
            signaling by acting as a GTPase activating protein for R-Ras
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Huang,Y., Rangwala,F., Fulkerson,P.C., Ling,B., Reed,E., Cox,A.D.,
            Kamholz,J. and Ratner,N.
  TITLE     Role of TC21/R-Ras2 in enhanced migration of
            neurofibromin-deficient Schwann cells
  JOURNAL   Oncogene 23 (2), 368-378 (2004)
   PUBMED   14724565
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473979.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_341852.1, XP_001080661.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ211166.1, BG662693.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..218
                     /product="ras-related protein R-Ras"
                     /EC_number="3.6.5.2"
                     /note="Harvey rat sarcoma oncogene, subgroup R;
                     Ras-related protein R-RAS (P23); Harvey rat sarcoma virus
                     oncogene, subgroup R; related RAS viral (r-ras) oncogene
                     homolog; RAS-related viral oncoprotein"
                     /calculated_mol_wt=23778
     mat_peptide     1..215
                     /product="Ras-related protein R-Ras. /id=PRO_0000408475"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8L7.1)"
                     /calculated_mol_wt=23584
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8L7.1)"
     Region          28..191
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            36..43
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            order(38..44,86,142..143,145,172..174)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206648"
     Region          58..66
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3Z8L7.1)"
     Site            61
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            64..66
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            83..86
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(85..86,102..103)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     Site            142..145
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            172..174
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     Site            215
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (D3Z8L7.1)"
     CDS             1..218
                     /gene="Rras"
                     /gene_synonym="p23"
                     /coded_by="NM_001108481.1:12..668"
                     /db_xref="GeneID:361568"
                     /db_xref="RGD:1311443"
ORIGIN      
        1 mssgaasgtg rgrprgggpg prdpppgeth klvvvggggv gksaltiqfi qsyfvsdydp
       61 tiedsytkic tvdgiparld ildtagqeef gamreqymra gngfllvfai ndrqsfievs
      121 klftqilrvk drddfpivlv gnkadletqr qvlrseassf sashhmtyfe asaklrlnvd
      181 eafeqlvrtv rkyqeqelpp sppsaprkkd grcpcvll
//
LOCUS       NP_001009659             474 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain-containing protein 174 [Rattus norvegicus].
ACCESSION   NP_001009659 XP_216221
VERSION     NP_001009659.2
DBSOURCE    REFSEQ: accession NM_001009659.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Volodarsky,M., Lichtig,H., Leibson,T., Sadaka,Y., Kadir,R.,
            Perez,Y., Liani-Leibson,K., Gradstein,L., Shaco-Levy,R., Shorer,Z.,
            Frank,D. and Birk,O.S.
  TITLE     CDC174, a novel component of the exon junction complex whose
            mutation underlies a syndrome of hypotonia and psychomotor
            developmental delay
  JOURNAL   Hum Mol Genet 24 (22), 6485-6491 (2015)
   PUBMED   26358778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC087050.1, CA334689.1 and BE106912.1.
            
            On Oct 1, 2011 this sequence version replaced NP_001009659.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..474
                     /product="coiled-coil domain-containing protein 174"
                     /note="uncharacterized protein C3orf19 homolog"
                     /calculated_mol_wt=54348
     Region          <4..340
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          39..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS7.2)"
     Region          129..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS7.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PII3; propagated from
                     UniProtKB/Swiss-Prot (Q5PQS7.2)"
     Region          238..311
                     /region_name="DUF4078"
                     /note="Domain of unknown function (DUF4078); pfam13300"
                     /db_xref="CDD:463837"
     Region          309..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS7.2)"
     Region          389..461
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PQS7.2)"
     CDS             1..474
                     /gene="Ccdc174"
                     /gene_synonym="RGD1305225"
                     /coded_by="NM_001009659.2:73..1497"
                     /db_xref="GeneID:297458"
                     /db_xref="RGD:1305225"
ORIGIN      
        1 mdrkkkpldv tasslvdlka elfrkqeefk qekllkdsgv fgkpktsnkk psiwskqnag
       61 vssraekdae qkleeqktld ksrekleeka klyekmtkgd fldeevedmy lvdftqkiid
      121 krkemevlga trdsrikeer daavaaandd ddeeefsekd ipppqdpsee wvdyvdslgr
      181 srrcmrkdlp sllemdknlq grlfvspane ktllsedmrk elqrqqweee erealkkpmg
      241 pihyediren earqlgvgyf afardkelrn kqmktlemlr eqttdqrikr enikekrkai
      301 learlaklrq kkmkkskedg teeesradgv vtepsepksv papppvaqss kveviiqerk
      361 dskpgvphir ewdrgkdfsf gfwskkqsel raerdpefap psnyfvgqkr tgslssqpws
      421 rpgaapsdlg hssgqsqeps sshtstpase sspqaptvtf qtlddmisyy kqvt
//
LOCUS       NP_001100893             717 aa            linear   ROD 28-APR-2025
DEFINITION  epithelial splicing regulatory protein 2 [Rattus norvegicus].
ACCESSION   NP_001100893 XP_001074518 XP_226421
VERSION     NP_001100893.1
DBSOURCE    REFSEQ: accession NM_001107423.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Bebee,T.W., Park,J.W., Sheridan,K.I., Warzecha,C.C., Cieply,B.W.,
            Rohacek,A.M., Xing,Y. and Carstens,R.P.
  TITLE     The splicing regulators Esrp1 and Esrp2 direct an epithelial
            splicing program essential for mammalian development
  JOURNAL   Elife 4, e08954 (2015)
   PUBMED   26371508
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473972.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_226421.4, XP_001074518.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760494
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..717
                     /product="epithelial splicing regulatory protein 2"
                     /note="RNA-binding protein 35B; RNA-binding motif protein
                     35B; RNA binding motif protein 35b"
                     /calculated_mol_wt=77197
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RYJ8.1)"
     Region          <82..214
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K0G8; propagated from
                     UniProtKB/Swiss-Prot (B2RYJ8.1)"
     Region          238..330
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          332..438
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          464..544
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Region          <555..678
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (B2RYJ8.1)"
     Region          664..>693
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..717
                     /gene="Esrp2"
                     /gene_synonym="Rbm35b; RGD1310855"
                     /coded_by="NM_001107423.1:232..2385"
                     /db_xref="GeneID:307810"
                     /db_xref="RGD:1310855"
ORIGIN      
        1 mtpppppppp pgpdpavdss tdpcpepqsl vvlfgataga lgpdlgsdet dlillvwqvv
       61 eprsrqvgtl hkslvraeaa alspqcreas glsadslara esldkvlqqf sqlvsgdval
      121 lgggpyvlct dgqqllrqvl hpeasrknlv lpdtffsfyd lrrefhvqhp stcsardltv
      181 gtmaqdlgle tdateddfgv wevktmvavi lhllegpngh lfskpevvkq kyetgpcska
      241 dvvdnetvvr arglpwqssd qdvarffkgl niarggvalc lnaqgrrnge alirfedseq
      301 rdlalqrhkh hmgvryievy katgeefvki aggtslevar flsredqvil rlrglpfsag
      361 padvldflgp ecpvtggvdg llfvrhpdgr ptgdafalfa ceelaqaalr rhkgmlgkry
      421 ielfrstaae vqqvlnryaa spllptltap llpipfplag gtgrdcvrlr glpytatied
      481 ilsflgeaaa dirphgvhmv lnqqgrpsgd afiqmmsver alaaaqrchk kvmkeryvev
      541 vpcsteemsr vlmggslsrs glspppcklp clspptyatf qaspalipte ttalypssal
      601 lpaarvpaaa tplayypgpa tqlymnytay ypsppvsptt vgylttppta lastptsmls
      661 qpgalvrmqg vpytagmkdl lsvfqayqla pddyatlvpv gdpprtvlqa pkewvcl
//
LOCUS       NP_058788                880 aa            linear   ROD 28-APR-2025
DEFINITION  tyrosine-protein kinase receptor TYRO3 precursor [Rattus
            norvegicus].
ACCESSION   NP_058788
VERSION     NP_058788.1
DBSOURCE    REFSEQ: accession NM_017092.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Powell,N.A., Kohrt,J.T., Filipski,K.J., Kaufman,M., Sheehan,D.,
            Edmunds,J.E., Delaney,A., Wang,Y., Bourbonais,F., Lee,D.Y.,
            Schwende,F., Sun,F., McConnell,P., Catana,C., Chen,H., Ohren,J. and
            Perrin,L.A.
  TITLE     Novel and selective spiroindoline-based inhibitors of Sky kinase
  JOURNAL   Bioorg Med Chem Lett 22 (1), 190-193 (2012)
   PUBMED   22119469
  REMARK    GeneRIF: analysis of novel and selective spiroindoline-based
            inhibitors of Sky kinase
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Brown,J.E., Krodel,M., Pazos,M., Lai,C. and Prieto,A.L.
  TITLE     Cross-phosphorylation, signaling and proliferative functions of the
            Tyro3 and Axl receptors in Rat2 cells
  JOURNAL   PLoS One 7 (5), e36800 (2012)
   PUBMED   22606290
  REMARK    GeneRIF: Overexpression of Tyro3 in the Rat2 cell line that
            expresses Axl, but not Mer or Tyro3, resulted in a 5 fold increase
            in cell proliferation.
REFERENCE   3  (residues 1 to 880)
  AUTHORS   Wang,Q., Lu,Q.J., Xiao,B., Zheng,Y. and Wang,X.M.
  TITLE     Expressions of Axl and Tyro-3 receptors are under regulation of
            nerve growth factor and are involved in differentiation of PC12
            cells
  JOURNAL   Neurosci Bull 27 (1), 15-22 (2011)
   PUBMED   21270900
  REMARK    GeneRIF: nerve growth factor affected intracellular localization of
            full-length Axl-eGFP and Tyro-3-eCFP in PC12 cells
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Zhong,Z., Wang,Y., Guo,H., Sagare,A., Fernandez,J.A., Bell,R.D.,
            Barrett,T.M., Griffin,J.H., Freeman,R.S. and Zlokovic,B.V.
  TITLE     Protein S protects neurons from excitotoxic injury by activating
            the TAM receptor Tyro3-phosphatidylinositol 3-kinase-Akt pathway
            through its sex hormone-binding globulin-like region
  JOURNAL   J Neurosci 30 (46), 15521-15534 (2010)
   PUBMED   21084607
  REMARK    Erratum:[J Neurosci. 2024 Apr 10;44(15):e0435242024. doi:
            10.1523/JNEUROSCI.0435-24.2024. PMID: 38561230]
REFERENCE   5  (residues 1 to 880)
  AUTHORS   Cosemans,J.M., Van Kruchten,R., Olieslagers,S., Schurgers,L.J.,
            Verheyen,F.K., Munnix,I.C., Waltenberger,J., Angelillo-Scherrer,A.,
            Hoylaerts,M.F., Carmeliet,P. and Heemskerk,J.W.
  TITLE     Potentiating role of Gas6 and Tyro3, Axl and Mer (TAM) receptors in
            human and murine platelet activation and thrombus stabilization
  JOURNAL   J Thromb Haemost 8 (8), 1797-1808 (2010)
   PUBMED   20546121
REFERENCE   6  (residues 1 to 880)
  AUTHORS   Broberger,C., Johansen,J., Schalling,M. and Hokfelt,T.
  TITLE     Hypothalamic neurohistochemistry of the murine anorexia (anx/anx)
            mutation: altered processing of neuropeptide Y in the arcuate
            nucleus
  JOURNAL   J Comp Neurol 387 (1), 124-135 (1997)
   PUBMED   9331176
REFERENCE   7  (residues 1 to 880)
  AUTHORS   Kajii,Y., Ninomiya,D., Kato,M., Mizuguchi,M., Saji,M.,
            Katsumoto,T., Ohno,K., Takashima,S. and Onodera,K.
  TITLE     A tyrosine kinase-like molecule is localized in the nuclear
            membrane of neurons: hippocampal behavior under stress
  JOURNAL   Biol Cell 88 (1-2), 45-54 (1996)
   PUBMED   9175267
REFERENCE   8  (residues 1 to 880)
  AUTHORS   Ohashi,K., Honda,S., Ichinomiya,N., Nakamura,T. and Mizuno,K.
  TITLE     Molecular cloning and in situ localization in the brain of rat sky
            receptor tyrosine kinase
  JOURNAL   J Biochem 117 (6), 1267-1275 (1995)
   PUBMED   7490270
REFERENCE   9  (residues 1 to 880)
  AUTHORS   Toshima,J., Ohashi,K., Iwashita,S. and Mizuno,K.
  TITLE     Autophosphorylation activity and association with Src family kinase
            of Sky receptor tyrosine kinase
  JOURNAL   Biochem Biophys Res Commun 209 (2), 656-663 (1995)
   PUBMED   7537495
REFERENCE   10 (residues 1 to 880)
  AUTHORS   Mark,M.R., Scadden,D.T., Wang,Z., Gu,Q., Goddard,A. and
            Godowski,P.J.
  TITLE     rse, a novel receptor-type tyrosine kinase with homology to
            Axl/Ufo, is expressed at high levels in the brain
  JOURNAL   J Biol Chem 269 (14), 10720-10728 (1994)
   PUBMED   7511603
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D37880.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D37880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132272
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..880
                     /product="tyrosine-protein kinase receptor TYRO3
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="tyrosine-protein kinase receptor TYRO3;
                     tyrosine-protein kinase SKY; TYRO3 protein tyrosine kinase
                     3; Bruton agammaglobulinemia tyrosine kinase"
                     /calculated_mol_wt=92807
     sig_peptide     1..31
                     /calculated_mol_wt=3131
     mat_peptide     32..880
                     /product="tyrosine-protein kinase receptor TYRO3"
                     /note="receptor tyrosine kinase"
                     /calculated_mol_wt=92807
     Region          40..126
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409553"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409553"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          90..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409553"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409553"
     Region          118..121
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409553"
     Region          130..209
                     /region_name="IgI_2_Axl_Tyro3_like"
                     /note="Second immunoglobulin (Ig)-like domain of Axl/Tyro3
                     family receptor tyrosine kinases (RTKs); member of the
                     I-set of Ig superfamily (IgSF) domains; cd05749"
                     /db_xref="CDD:409407"
     Region          130..133
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409407"
     Region          136..140
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409407"
     Region          144..153
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409407"
     Region          158..165
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409407"
     Region          167..170
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409407"
     Region          174..185
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409407"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          188..197
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409407"
     Site            196..201
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409407"
     Site            order(199..201,203)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409407"
     Region          201..209
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409407"
     Region          215..307
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(215,280,295)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            230
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            order(296..297,299..300)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          315..396
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            370
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            order(392..393,395..396)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            420..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55146.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06418; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          498..781
                     /region_name="PTKc_Tyro3"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tyro3; cd05074"
                     /db_xref="CDD:270659"
     Site            order(514..518,522,538,540,571,594..596,600,645,649..650,
                     652,663,681..685,694,728)
                     /site_type="active"
                     /db_xref="CDD:270659"
     Site            order(514..515,522,538,571,594..596,600,645,649..650,652,
                     663)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270659"
     Site            order(645,649,681..685,694,728)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270659"
     Site            662..687
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270659"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          804..827
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55146.1)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q06418; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     Region          842..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55146.1)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P55146.1)"
     CDS             1..880
                     /gene="Tyro3"
                     /gene_synonym="Brt"
                     /coded_by="NM_017092.1:26..2668"
                     /db_xref="GeneID:25232"
                     /db_xref="RGD:3923"
ORIGIN      
        1 malrrsmgrp glrplllagl aslllpgsaa aglklmgapv kmtvsqgqpv klncsvegmd
       61 dpdihwmkdg avvqnasqvs isiseqnwig llslksaers daglywcqvk dgeetkisqs
      121 vwltvegvpf ftvepkdlav ppnvpfqlsc eavgppepvt ifwwrgptkv ggpasspsvl
      181 nvtgvtqrte fsceahnikg latsrpaiir lqappaapfn itvttisssn asvawvpgad
      241 glallhsctv qvahapgewe alavvvpvpp ftcllrnlap atnyslrvrc analgpspyg
      301 dwvpfqtkgl aparapqnfh airtdsglil eweevipedp gegplgpykl swvqengtqd
      361 elmvegttan ltdwdpqkdl vlrvcasnai gdgpwsqplv vsshdhagrq gpphsrtswv
      421 pvvlgvltal itaaalalil lrkrrketrf gqafdsvmar gepavhfraa rsfnrerper
      481 ieatldslgi sdelkekled vlipeqqftl grmlgkgefg svreaqlkqe dgsfvkvavk
      541 mlkadiiass dieeflreaa cmkefdhphv aklvgvslrs rakgrlpipm vilpfmkhgd
      601 lhafllasri genpfnlplq tlvrfmvdia cgmeylssrn fihrdlaarn cmlaedmtvc
      661 vadfglsrki ysgdyyrqgc asklpvkwla lesladnlyt vhsdvwafgv tmweimtrgq
      721 tpyagienae iynylisgnr lkqppecmee vydlmyqcws adpkqrpsft clrmelenil
      781 ghlsvlstsq dplyiniera gqpaengspe lpcgeqssse agdgsgmgai ggipsdcryi
      841 fspgglaesp gqleqqpesp lnenqrllll qqgllphssc
//
LOCUS       NP_001020941             339 aa            linear   ROD 28-APR-2025
DEFINITION  centrosomal protein of 41 kDa isoform 1 [Rattus norvegicus].
ACCESSION   NP_001020941 XP_575421
VERSION     NP_001020941.1
DBSOURCE    REFSEQ: accession NM_001025770.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Ishikawa,H., Thompson,J., Yates,J.R. 3rd and Marshall,W.F.
  TITLE     Proteomic analysis of mammalian primary cilia
  JOURNAL   Curr Biol 22 (5), 414-419 (2012)
   PUBMED   22326026
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Lee,J.E., Silhavy,J.L., Zaki,M.S., Schroth,J., Bielas,S.L.,
            Marsh,S.E., Olvera,J., Brancati,F., Iannicelli,M., Ikegami,K.,
            Schlossman,A.M., Merriman,B., Attie-Bitach,T., Logan,C.V.,
            Glass,I.A., Cluckey,A., Louie,C.M., Lee,J.H., Raynes,H.R.,
            Rapin,I., Castroviejo,I.P., Setou,M., Barbot,C., Boltshauser,E.,
            Nelson,S.F., Hildebrandt,F., Johnson,C.A., Doherty,D.A.,
            Valente,E.M. and Gleeson,J.G.
  TITLE     CEP41 is mutated in Joubert syndrome and is required for tubulin
            glutamylation at the cilium
  JOURNAL   Nat Genet 44 (2), 193-199 (2012)
   PUBMED   22246503
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC098832.1.
            
            On Jul 22, 2005 this sequence version replaced XP_575421.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098832.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q22"
     Protein         1..339
                     /product="centrosomal protein of 41 kDa isoform 1"
                     /note="centrosomal protein of 41 kDa; testis specific gene
                     A14; testis specific, 14; testis-specific gene A14
                     protein; centrosomal protein 41kDa"
                     /calculated_mol_wt=36861
     Region          56..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99NF3; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     Region          136..221
                     /region_name="Rhodanese"
                     /note="Rhodanese-like domain; pfam00581"
                     /db_xref="CDD:425764"
     Site            192
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          283..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4KM37.1)"
     Site            309
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q99NF3; propagated from
                     UniProtKB/Swiss-Prot (Q4KM37.1)"
     CDS             1..339
                     /gene="Cep41"
                     /gene_synonym="Tsga14"
                     /coded_by="NM_001025770.2:65..1084"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:500069"
                     /db_xref="RGD:1562034"
ORIGIN      
        1 msdspidgsp qpepdyrykk delfkrikvt tfaqlviqva slsdqtlevt aeeiqrleds
       61 dsatseadtd iaaktngkgs peeqspspvq finstgagda srstlqsvis gvgeldvdkg
      121 lvkkeepsgk dkpypdcpfl lldvrdrdsy qqchivgays ypiatlsrtm npysndiley
      181 knahgkiiil yddderlasq aattmcergf enlfmlsggl kvlaqkfpeg lvtgslpasc
      241 qqalpfgsvr krpgpkmpal paenkwrftp edlkkiecyl eadqgpannp srlnqnnsag
      301 rdlkvpagrg gqnlptgcpt shsnsrtlns ghlqgkpwk
//
LOCUS       NP_077348                627 aa            linear   ROD 28-APR-2025
DEFINITION  sodium- and chloride-dependent GABA transporter 3 [Rattus
            norvegicus].
ACCESSION   NP_077348
VERSION     NP_077348.1
DBSOURCE    REFSEQ: accession NM_024372.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Augier,E., Barbier,E., Dulman,R.S., Licheri,V., Augier,G., Domi,E.,
            Barchiesi,R., Farris,S., Natt,D., Mayfield,R.D., Adermark,L. and
            Heilig,M.
  TITLE     A molecular mechanism for choosing alcohol over an alternative
            reward
  JOURNAL   Science 360 (6395), 1321-1326 (2018)
   PUBMED   29930131
  REMARK    GeneRIF: Expression of the gamma-aminobutyric acid (GABA)
            transporter GAT-3 was selectively decreased within the amygdala of
            alcohol-choosing rats, whereas a knockdown of this transcript
            reversed choice preference of rats that originally chose a sweet
            solution over alcohol.
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Chazalon,M., Paredes-Rodriguez,E., Morin,S., Martinez,A.,
            Cristovao-Ferreira,S., Vaz,S., Sebastiao,A., Panatier,A.,
            Boue-Grabot,E., Miguelez,C. and Baufreton,J.
  TITLE     GAT-3 Dysfunction Generates Tonic Inhibition in External Globus
            Pallidus Neurons in Parkinsonian Rodents
  JOURNAL   Cell Rep 23 (6), 1678-1690 (2018)
   PUBMED   29742425
  REMARK    GeneRIF: glial GAT-3 transporters are downregulated while neuronal
            GAT-1 function remains normal in dopamine-depleted rodents.
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Boddum,K., Jensen,T.P., Magloire,V., Kristiansen,U., Rusakov,D.A.,
            Pavlov,I. and Walker,M.C.
  TITLE     Astrocytic GABA transporter activity modulates excitatory
            neurotransmission
  JOURNAL   Nat Commun 7, 13572 (2016)
   PUBMED   27886179
  REMARK    GeneRIF: Increases in GAT-3 activity result in astrocytic Na+
            accumulation and a consequent increase in astrocytic Ca2+ through
            Na+/Ca2+ exchange, leading to the astrocytic release of
            ATP/adenosine.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Melone,M., Ciappelloni,S. and Conti,F.
  TITLE     Plasma membrane transporters GAT-1 and GAT-3 contribute to
            heterogeneity of GABAergic synapses in neocortex
  JOURNAL   Front Neuroanat 8, 72 (2014)
   PUBMED   25120439
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Weingarten,J., Lassek,M., Mueller,B.F., Rohmer,M., Lunger,I.,
            Baeumlisberger,D., Dudek,S., Gogesch,P., Karas,M. and Volknandt,W.
  TITLE     The proteome of the presynaptic active zone from mouse brain
  JOURNAL   Mol Cell Neurosci 59, 106-118 (2014)
   PUBMED   24534009
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Fletcher,E.L., Clark,M.J. and Furness,J.B.
  TITLE     Neuronal and glial localization of GABA transporter
            immunoreactivity in the myenteric plexus
  JOURNAL   Cell Tissue Res 308 (3), 339-346 (2002)
   PUBMED   12107427
  REMARK    GeneRIF: a small proportion of inhibitory motor neurons and at
            least some putative intrinsic primary afferent neurons within the
            rat gastrointestinal tract express GAT3.
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Ribak,C.E., Tong,W.M. and Brecha,N.C.
  TITLE     GABA plasma membrane transporters, GAT-1 and GAT-3, display
            different distributions in the rat hippocampus
  JOURNAL   J Comp Neurol 367 (4), 595-606 (1996)
   PUBMED   8731228
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Liu,Q.R., Lopez-Corcuera,B., Mandiyan,S., Nelson,H. and Nelson,N.
  TITLE     Molecular characterization of four pharmacologically distinct
            gamma-aminobutyric acid transporters in mouse brain [corrected]
  JOURNAL   J Biol Chem 268 (3), 2106-2112 (1993)
   PUBMED   8420981
  REMARK    Erratum:[J Biol Chem 1993 Apr 25;268(12):9156]
REFERENCE   9  (residues 1 to 627)
  AUTHORS   Borden,L.A., Smith,K.E., Hartig,P.R., Branchek,T.A. and
            Weinshank,R.L.
  TITLE     Molecular heterogeneity of the gamma-aminobutyric acid (GABA)
            transport system. Cloning of two novel high affinity GABA
            transporters from rat brain
  JOURNAL   J Biol Chem 267 (29), 21098-21104 (1992)
   PUBMED   1400419
REFERENCE   10 (residues 1 to 627)
  AUTHORS   Clark,J.A., Deutch,A.Y., Gallipoli,P.Z. and Amara,S.G.
  TITLE     Functional expression and CNS distribution of a
            beta-alanine-sensitive neuronal GABA transporter
  JOURNAL   Neuron 9 (2), 337-348 (1992)
   PUBMED   1497897
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M95763.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M95763.1, M95738.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760393, SAMEA5760396
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..627
                     /product="sodium- and chloride-dependent GABA transporter
                     3"
                     /note="GAT-3; solute carrier family 6 (neurotransmitter
                     transporter), member 11; GABA transporter GAT-3; solute
                     carrier family 6 (neurotransmitter transporter, GABA),
                     member 11"
                     /calculated_mol_wt=69816
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P31647.1)"
     Region          44..585
                     /region_name="SLC6sbd_GAT3"
                     /note="Na(+)- and Cl(-)-dependent GABA transporter 3;
                     solute-binding domain; cd11508"
                     /db_xref="CDD:212077"
     Site            54..74
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            order(60,63,401,404..405)
                     /site_type="other"
                     /note="Na binding site 2 [ion binding]"
                     /db_xref="CDD:212077"
     Site            order(61..62,64..67,142,303..304,309,311,405,408..409)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:212077"
     Site            order(62,67,304,336)
                     /site_type="other"
                     /note="Na binding site 1 [ion binding]"
                     /db_xref="CDD:212077"
     Site            order(69..70,141,145,148,370,374)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:212077"
     Site            82..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31647.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31647.1)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31647.1)"
     Site            221..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            248..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            301..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            330..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            384..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            433..451
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            468..488
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            509..528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     Site            548..566
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31647.1)"
     CDS             1..627
                     /gene="Slc6a11"
                     /gene_synonym="Gabt4; Gat3"
                     /coded_by="NM_024372.2:13..1896"
                     /db_xref="GeneID:79213"
                     /db_xref="RGD:628737"
ORIGIN      
        1 mtaeqalplg ngkaaeearg sealgggggg aagtreardk avherghwnn kvefvlsvag
       61 eiiglgnvwr fpylcykngg gaflipyvvf ficcgipvff letalgqfts eggitcwrrv
      121 cplfegigya tqvieahlnv yyiiilawai fylsncftte lpwatcghew ntekcvefqk
      181 lnfsnyshvs lqnatspvme fwerrvlais dgiehignlr welalcllaa wticyfciwk
      241 gtkstgkvvy vtatfpyiml lillirgvtl pgasegikfy lypdlsrlsd pqvwvdagtq
      301 iffsyaiclg cltalgsynn ynnncyrdci mlcclnsgts fvagfaifsv lgfmayeqgv
      361 piaevaesgp glafiaypka vtmmplsplw atlffmmlif lgldsqfvcv eslvtavvdm
      421 ypkvfrrgyr rellilalsi vsyflglvml teggmyifql fdsyaasgmc llfvaifecv
      481 cigwvygsnr fydniedmig yrplslikwc wkvvtpgica gififflvky kplkynnvyt
      541 ypawgygigw lmalssmlci plwifiklwk tegtlpeklq kltvpsadlk mrgklgaspr
      601 mvtvndceak vkgdgtisai tekethf
//
LOCUS       NP_001004090             268 aa            linear   ROD 28-APR-2025
DEFINITION  tetraspanin-5 [Rattus norvegicus].
ACCESSION   NP_001004090 XP_342351
VERSION     NP_001004090.2
DBSOURCE    REFSEQ: accession NM_001004090.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Moretto,E., Miozzo,F., Longatti,A., Bonnet,C., Coussen,F.,
            Jaudon,F., Cingolani,L.A. and Passafaro,M.
  TITLE     The tetraspanin TSPAN5 regulates AMPAR exocytosis by interacting
            with the AP4 complex
  JOURNAL   Elife 12, e76425 (2023)
   PUBMED   36795458
  REMARK    GeneRIF: The tetraspanin TSPAN5 regulates AMPAR exocytosis by
            interacting with the AP4 complex.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Haining,E.J., Yang,J., Bailey,R.L., Khan,K., Collier,R., Tsai,S.,
            Watson,S.P., Frampton,J., Garcia,P. and Tomlinson,M.G.
  TITLE     The TspanC8 subgroup of tetraspanins interacts with A disintegrin
            and metalloprotease 10 (ADAM10) and regulates its maturation and
            cell surface expression
  JOURNAL   J Biol Chem 287 (47), 39753-39765 (2012)
   PUBMED   23035126
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Dornier,E., Coumailleau,F., Ottavi,J.F., Moretti,J., Boucheix,C.,
            Mauduit,P., Schweisguth,F. and Rubinstein,E.
  TITLE     TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and
            promote Notch activation in flies and mammals
  JOURNAL   J Cell Biol 199 (3), 481-496 (2012)
   PUBMED   23091066
  REMARK    Erratum:[J Cell Biol. 2016 May 23;213(4):495-6. doi:
            10.1083/jcb.20120113304262016c. PMID: 27185832]
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hemler,M.E.
  TITLE     Specific tetraspanin functions
  JOURNAL   J Cell Biol 155 (7), 1103-1107 (2001)
   PUBMED   11756464
  REMARK    Review article
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100135.1.
            
            On Aug 21, 2005 this sequence version replaced NP_001004090.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100135.1, AF540877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..268
                     /product="tetraspanin-5"
                     /note="tetraspan 5; transmembrane 4 superfamily member 9"
                     /calculated_mol_wt=30206
     Region          15..258
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68VK5.2)"
     Region          113..233
                     /region_name="TM4SF9_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF9_like subfamily.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03159"
                     /db_xref="CDD:239412"
     Site            order(114,119,123,125..126,129,143,146..147,150..151)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239412"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q68VK5.2)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68VK5.2)"
     CDS             1..268
                     /gene="Tspan5"
                     /gene_synonym="Tm4sf9; Tspan-5"
                     /coded_by="NM_001004090.2:6..812"
                     /db_xref="GeneID:362048"
                     /db_xref="RGD:1303176"
ORIGIN      
        1 msgkhykgpe vsccikyfif gfnvifwflg itflgiglwa wnekgvlsni ssitdlggfd
       61 pvwlflvvgg vmfilgfagc igalrentfl lkffsvflgi iffleltagv lafvfkdwik
      121 dqlyffinnn irayrddidl qnlidftqey wqccgafgad dwnlniyfnc tdsnasrerc
      181 gvpfscctkd paedvintqc gydarqkpev dqqiviytkg cvpqfekwlq dnltivagif
      241 igiallqifg iclaqnlvsd ieavrasw
//
LOCUS       NP_001020921             350 aa            linear   ROD 28-APR-2025
DEFINITION  pleckstrin [Rattus norvegicus].
ACCESSION   NP_001020921 XP_344268
VERSION     NP_001020921.1
DBSOURCE    REFSEQ: accession NM_001025750.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Frobel,J., Cadeddu,R.P., Hartwig,S., Bruns,I., Wilk,C.M.,
            Kundgen,A., Fischer,J.C., Schroeder,T., Steidl,U.G., Germing,U.,
            Lehr,S., Haas,R. and Czibere,A.
  TITLE     Platelet proteome analysis reveals integrin-dependent aggregation
            defects in patients with myelodysplastic syndromes
  JOURNAL   Mol Cell Proteomics 12 (5), 1272-1280 (2013)
   PUBMED   23382103
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Lian,L., Wang,Y., Flick,M., Choi,J., Scott,E.W., Degen,J.,
            Lemmon,M.A. and Abrams,C.S.
  TITLE     Loss of pleckstrin defines a novel pathway for PKC-mediated
            exocytosis
  JOURNAL   Blood 113 (15), 3577-3584 (2009)
   PUBMED   19190246
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Edlich,C., Stier,G., Simon,B., Sattler,M. and Muhle-Goll,C.
  TITLE     Structure and phosphatidylinositol-(3,4)-bisphosphate binding of
            the C-terminal PH domain of human pleckstrin
  JOURNAL   Structure 13 (2), 277-286 (2005)
   PUBMED   15698571
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Roll,R.L., Bauman,E.M., Bennett,J.S. and Abrams,C.S.
  TITLE     Phosphorylated pleckstrin induces cell spreading via an
            integrin-dependent pathway
  JOURNAL   J Cell Biol 150 (6), 1461-1466 (2000)
   PUBMED   10995449
REFERENCE   6  (residues 1 to 350)
  AUTHORS   McDermott,A.M. and Haslam,R.J.
  TITLE     Chemical cross-linking of pleckstrin in human platelets: evidence
            for oligomerization of the protein and its dissociation by protein
            kinase C
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 119-124 (1996)
   PUBMED   8694752
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Craig,K.L. and Harley,C.B.
  TITLE     Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by
            protein kinase C
  JOURNAL   Biochem J 314 (Pt 3) (Pt 3), 937-942 (1996)
   PUBMED   8615792
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Abrams,C.S., Zhao,W., Belmonte,E. and Brass,L.F.
  TITLE     Protein kinase C regulates pleckstrin by phosphorylation of sites
            adjacent to the N-terminal pleckstrin homology domain
  JOURNAL   J Biol Chem 270 (40), 23317-23321 (1995)
   PUBMED   7559487
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Abrams,C.S., Wu,H., Zhao,W., Belmonte,E., White,D. and Brass,L.F.
  TITLE     Pleckstrin inhibits phosphoinositide hydrolysis initiated by
            G-protein-coupled and growth factor receptors. A role for
            pleckstrin's PH domains
  JOURNAL   J Biol Chem 270 (24), 14485-14492 (1995)
   PUBMED   7782310
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Tyers,M., Haslam,R.J., Rachubinski,R.A. and Harley,C.B.
  TITLE     Molecular analysis of pleckstrin: the major protein kinase C
            substrate of platelets
  JOURNAL   J Cell Biochem 40 (2), 133-145 (1989)
   PUBMED   2768345
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098846.1.
            
            On Jul 22, 2005 this sequence version replaced XP_344268.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098846.1, FQ225547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680436, SAMN09767679
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q22"
     Protein         1..350
                     /product="pleckstrin"
                     /calculated_mol_wt=39865
     Region          3..110
                     /region_name="PH1_Pleckstrin_2"
                     /note="Pleckstrin 2 Pleckstrin homology (PH) domain,
                     repeat 1; cd13301"
                     /db_xref="CDD:270113"
     Site            64
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P08567; propagated from
                     UniProtKB/Swiss-Prot (Q4KM33.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08567; propagated from
                     UniProtKB/Swiss-Prot (Q4KM33.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q4KM33.1)"
     Region          125..223
                     /region_name="DEP_PLEK1"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in pleckstrin 1-like proteins. Pleckstrin 1 plays a
                     role in cell spreading and reorganization of actin
                     cytoskeleton in platelets and leukocytes. Its activity is
                     highly regulated by phosphorylation; cd04445"
                     /db_xref="CDD:239892"
     Region          239..346
                     /region_name="PH2_Pleckstrin_2"
                     /note="Pleckstrin 2 Pleckstrin homology (PH) domain,
                     repeat 2; cd13302"
                     /db_xref="CDD:270114"
     Site            order(252,254..257,277,287,325)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270114"
     Site            order(272,274,276,286,289,291,293..294,320)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270114"
     CDS             1..350
                     /gene="Plek"
                     /coded_by="NM_001025750.1:210..1262"
                     /db_xref="GeneID:364206"
                     /db_xref="RGD:1308269"
ORIGIN      
        1 mepkriregy lvkkgsvfnt wkpmwvvlle dgiefykkks dnnpkgmipl kgstltspcq
       61 dfgkrmfvlk itttkqqdhf fqaayleerd awvrdikkai kcieggqkfa rkstrrsirl
      121 petidlgaly lsmkdpekgi kelnlekdkk vfnhcftgsg vidwlvsnkl vrnrqeglmi
      181 sasllsegyl qpasdlskna adgiaenpfl dnpdafyyfp dsgffceens sdddiilkee
      241 frgiiikqgc llkqghrrkn wkvrkfilre dpaylhyydp aggedplgai hlrgcvvtsv
      301 esnpdgkksd eenlfeiita devhyymqaa takertewik aiqvasrtgk
//
LOCUS       NP_001099914             114 aa            linear   ROD 28-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit KCP2 [Rattus norvegicus].
ACCESSION   NP_001099914 XP_001072393 XP_215616
VERSION     NP_001099914.1
DBSOURCE    REFSEQ: accession NM_001106444.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Roboti,P. and High,S.
  TITLE     The oligosaccharyltransferase subunits OST48, DAD1 and KCP2
            function as ubiquitous and selective modulators of mammalian
            N-glycosylation
  JOURNAL   J Cell Sci 125 (Pt 14), 3474-3484 (2012)
   PUBMED   22467853
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Shibatani,T., David,L.L., McCormack,A.L., Frueh,K. and Skach,W.R.
  TITLE     Proteomic analysis of mammalian oligosaccharyltransferase reveals
            multiple subcomplexes that contain Sec61, TRAP, and two potential
            new subunits
  JOURNAL   Biochemistry 44 (16), 5982-5992 (2005)
   PUBMED   15835887
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473976.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001072393.1, XP_215616.4.
            
            ##Evidence-Data-START##
            CDS exon combination :: CB611707.1, CB313424.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMD00132303, SAMEA5760476 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..114
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit KCP2"
                     /note="KCP-2; oligosaccharyl transferase subunit KCP2"
                     /calculated_mol_wt=12399
     Region          1..109
                     /region_name="Keratin_assoc"
                     /note="Keratinocyte-associated protein 2; pfam09775"
                     /db_xref="CDD:401649"
     CDS             1..114
                     /gene="Krtcap2"
                     /coded_by="NM_001106444.1:579..923"
                     /db_xref="GeneID:295243"
                     /db_xref="RGD:1308413"
ORIGIN      
        1 mqiysrqlas tewltiqggl lgsglfvfsl tafnnlenlv fgkgfqakif peillcllla
       61 lfasglihrv cvttcfifsm vglyyinkis stlyqatapa ltpakvtgks kkrn
//
LOCUS       NP_001004271             530 aa            linear   ROD 28-APR-2025
DEFINITION  UDP-glucuronosyltransferase 2B15 precursor [Rattus norvegicus].
ACCESSION   NP_001004271 NP_114186 XP_346460
VERSION     NP_001004271.1
DBSOURCE    REFSEQ: accession NM_001004271.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Dam,P.T.M., Jang,Y.J., Park,J.I., Choi,B.C., Song,S.J. and
            Chun,S.Y.
  TITLE     Regulation of uridine diphosphate-glucuronosyltransferase 2B15
            expression during ovulation in the rat
  JOURNAL   Endocr J 64 (6), 605-612 (2017)
   PUBMED   28442641
  REMARK    GeneRIF: Data suggest that gonadotropins transiently stimulate
            Ugt2b15 expression and activity in granulosa cells of pre-ovulatory
            follicles as they undergo ovulation; Ugt2b15 mRNA levels appear to
            be regulated by signal transduction involving progesterone
            receptors and vitamin D receptors.
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Xu,L., Krenitsky,D.M., Seacat,A.M., Butenhoff,J.L., Tephly,T.R. and
            Anders,M.W.
  TITLE     N-glucuronidation of perfluorooctanesulfonamide by human, rat, dog,
            and monkey liver microsomes and by expressed rat and human
            UDP-glucuronosyltransferases
  JOURNAL   Drug Metab Dispos 34 (8), 1406-1410 (2006)
   PUBMED   16720684
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Green,M.D., Clarke,D.J., Oturu,E.M., Styczynski,P.B., Jackson,M.R.,
            Burchell,B. and Tephly,T.R.
  TITLE     Cloning and expression of a rat liver phenobarbital-inducible
            UDP-glucuronosyltransferase (2B12) with specificity for
            monoterpenoid alcohols
  JOURNAL   Arch Biochem Biophys 322 (2), 460-468 (1995)
   PUBMED   7574722
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Styczynski,P., Green,M., Puig,J., Coffman,B. and Tephly,T.
  TITLE     Purification and properties of a rat liver phenobarbital-inducible
            4-hydroxybiphenyl UDP-glucuronosyltransferase
  JOURNAL   Mol Pharmacol 40 (1), 80-84 (1991)
   PUBMED   1906977
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078782.1.
            
            On or before Oct 20, 2005 this sequence version replaced
            NP_114186.1, XP_346460.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078782.1, U06273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14p21"
     Protein         1..530
                     /product="UDP-glucuronosyltransferase 2B15 precursor"
                     /EC_number="2.4.1.17"
                     /note="UDP-glucuronosyltransferase 2B4;
                     UDP-glucuronosyltransferase 2B15; UDPGT 2B4;
                     UDP-glucuronosyltransferase 2B12; UDPGT 2B12; UDPGT 2B15;
                     UDPGT 2B36; UDP glucuronosyltransferase 2 family,
                     polypeptide B36; UDP-glucuronosyltransferase 2B36; UDP
                     glycosyltransferase 2 family, polypeptide B4; UDP
                     glucuronosyltransferase 2 family, polypeptide B15"
                     /calculated_mol_wt=58488
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2557
     mat_peptide     24..530
                     /product="UDP-glucuronosyltransferase 2B15.
                     /id=PRO_0000036036"
                     /note="propagated from UniProtKB/Swiss-Prot (P36511.1)"
                     /calculated_mol_wt=58488
     Region          24..527
                     /region_name="UDPGT"
                     /note="UDP-glucoronosyl and UDP-glucosyl transferase;
                     pfam00201"
                     /db_xref="CDD:278624"
     Site            order(34..35,37,199,202..203,221,253,312,375,377,379..380,
                     383)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(34,312,375,377,379..380)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            35
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            order(49,147,458..459,462)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:340817"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P36511.1)"
     Site            494..510
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36511.1)"
     CDS             1..530
                     /gene="Ugt2b35"
                     /gene_synonym="Ugt2b12; Ugt2b15; Ugt2b36; Ugt2b4"
                     /coded_by="NM_001004271.1:22..1614"
                     /db_xref="GeneID:83808"
                     /db_xref="RGD:620895"
ORIGIN      
        1 mpgkwisall llqisfcfks gncgkvlvwp meyshwmnik iileelvqkg hevtvlrpsa
       61 svfldpkets dlkfvtfpts fsshdlenff trfvnvwtye lprdtclsyf lylqdtidey
      121 sdycltvcke avsnkqfmtk lqeskfdvvf sdaigpcgel iaellqipfl yslrfspgyt
      181 iekyiggvlf ppsyvpmifs glagqmtfie rvhnmicmly fdfwfqtfre kkwdpfyskt
      241 lgrpttlaei mgkaemwlir sywdlefphp ispnvdyigg lhckpakplp kdiedfvqss
      301 gehgvvvfsl gsmvrnmtee kaniiawala qipqkvlwrf dgkkpptlgp ntrlykwlpq
      361 ndllghpktk afvthggang iyeaihhgip migiplfgeq hdniahmvak gaavevnfrt
      421 msksdmlnal eevinnpfyk knamwlstih hdqptkpldr avfwiefvmr hkgakhlrsl
      481 ghnlpwyqyh sldvigfllt cvavtvvlal kcflfvyrff vkkekktkne
//
LOCUS       NP_001020075             436 aa            linear   ROD 28-APR-2025
DEFINITION  coiled-coil domain-containing protein 71 [Rattus norvegicus].
ACCESSION   NP_001020075 XP_573961
VERSION     NP_001020075.1
DBSOURCE    REFSEQ: accession NM_001024904.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Wu,T., Zhang,Z., Yuan,Z., Lo,L.J., Chen,J., Wang,Y. and Peng,J.
  TITLE     Distinctive genes determine different intramuscular fat and muscle
            fiber ratios of the longissimus dorsi muscles in Jinhua and
            landrace pigs
  JOURNAL   PLoS One 8 (1), e53181 (2013)
   PUBMED   23301040
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC098020.1.
            
            On Jun 17, 2005 this sequence version replaced XP_573961.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098020.1, FQ098142.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..436
                     /product="coiled-coil domain-containing protein 71"
                     /calculated_mol_wt=46331
     Region          8..433
                     /region_name="CCDC71L"
                     /note="Coiled-coil domain-containing protein 71L;
                     pfam15374"
                     /db_xref="CDD:464682"
     Region          95..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7C4.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8IV32; propagated from
                     UniProtKB/Swiss-Prot (Q4V7C4.1)"
     Region          210..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7C4.1)"
     Region          314..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V7C4.1)"
     CDS             1..436
                     /gene="Ccdc71"
                     /coded_by="NM_001024904.1:98..1408"
                     /db_xref="GeneID:498678"
                     /db_xref="RGD:1566341"
ORIGIN      
        1 msmvvqhvee kavhswsris tagkkaleea llvfnpmsqd lsateaqlva flqglrddgf
       61 qptilrsgdv ygyssctasp psqtklqart inppatslpa rapqtaksvp tgqttllpvp
      121 lsgrlakgst palakhtttn lllsslkqsn asntsgttvg fpahlypgvy pamqlsvvle
      181 alvplktpcl dvkhraqslq lslaksslkl rkgsgnpqsk aprritskgl kyltskgpga
      241 glrrgagtqs ngarmkgrst lgtktvrgka prtltkavca rasvapaktk tvrvrakvkq
      301 akpkaakaka kaaalrgkak dkavqakaka artkhkkrpk gyvqtrtgrt slknssetvg
      361 qkrkkaeetk glppkkrarc vprskarlgt gtakpqksqt ikvdrkcsdd evrqcaqqil
      421 rvnlspvvll qpllpv
//
LOCUS       NP_001257534             901 aa            linear   ROD 28-APR-2025
DEFINITION  glutamate receptor ionotropic, NMDA 1 isoform 2a precursor [Rattus
            norvegicus].
ACCESSION   NP_001257534
VERSION     NP_001257534.1
DBSOURCE    REFSEQ: accession NM_001270605.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Chou,T.H., Epstein,M., Fritzemeier,R.G., Akins,N.S., Paladugu,S.,
            Ullman,E.Z., Liotta,D.C., Traynelis,S.F. and Furukawa,H.
  TITLE     Molecular mechanism of ligand gating and opening of NMDA receptor
  JOURNAL   Nature 632 (8023), 209-217 (2024)
   PUBMED   39085540
  REMARK    GeneRIF: Molecular mechanism of ligand gating and opening of NMDA
            receptor.
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Prados-Pardo,A., Martin-Gonzalez,E., Mora,S., Martin,C.,
            Olmedo-Cordoba,M., Perez-Fernandez,C., Sanchez-Santed,F. and
            Moreno-Montoya,M.
  TITLE     Reduced Expression of the Htr2a, Grin1, and Bdnf Genes and
            Cognitive Inflexibility in a Model of High Compulsive Rats
  JOURNAL   Mol Neurobiol 60 (12), 6975-6991 (2023)
   PUBMED   37523044
  REMARK    GeneRIF: Reduced Expression of the Htr2a, Grin1, and Bdnf Genes and
            Cognitive Inflexibility in a Model of High Compulsive Rats.
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Zhang,J., Zhang,M., Wang,Q., Wen,H., Liu,Z., Wang,F., Wang,Y.,
            Yao,F., Song,N., Kou,Z., Li,Y., Guo,F. and Zhu,S.
  TITLE     Distinct structure and gating mechanism in diverse NMDA receptors
            with GluN2C and GluN2D subunits
  JOURNAL   Nat Struct Mol Biol 30 (5), 629-639 (2023)
   PUBMED   36959261
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Jyothi,A.K., Thotakura,B., Priyadarshini,S.C., Patil,S.,
            Poojari,M.S. and Subramanian,M.
  TITLE     Paternal stress alters synaptic density and expression of GAP-43,
            GRIN1, M1 and SYP genes in the hippocampus and cortex of offspring
            of stress-induced male rats
  JOURNAL   Morphologie 107 (356), 67-79 (2023)
   PUBMED   35715368
  REMARK    GeneRIF: Paternal stress alters synaptic density and expression of
            GAP-43, GRIN1, M1 and SYP genes in the hippocampus and cortex of
            offspring of stress-induced male rats.
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Kolcheva,M., Ladislav,M., Netolicky,J., Kortus,S., Rehakova,K.,
            Krausova,B.H., Hemelikova,K., Misiachna,A., Kadkova,A., Klima,M.,
            Chalupska,D. and Horak,M.
  TITLE     The pathogenic N650K variant in the GluN1 subunit regulates the
            trafficking, conductance, and pharmacological properties of NMDA
            receptors
  JOURNAL   Neuropharmacology 222, 109297 (2023)
   PUBMED   36341805
  REMARK    GeneRIF: The pathogenic N650K variant in the GluN1 subunit
            regulates the trafficking, conductance, and pharmacological
            properties of NMDA receptors.
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Ikeda,K., Nagasawa,M., Mori,H., Araki,K., Sakimura,K., Watanabe,M.,
            Inoue,Y. and Mishina,M.
  TITLE     Cloning and expression of the epsilon 4 subunit of the NMDA
            receptor channel
  JOURNAL   FEBS Lett 313 (1), 34-38 (1992)
   PUBMED   1385220
REFERENCE   7  (residues 1 to 901)
  AUTHORS   Kutsuwada,T., Kashiwabuchi,N., Mori,H., Sakimura,K., Kushiya,E.,
            Araki,K., Meguro,H., Masaki,H., Kumanishi,T., Arakawa,M. et al.
  TITLE     Molecular diversity of the NMDA receptor channel
  JOURNAL   Nature 358 (6381), 36-41 (1992)
   PUBMED   1377365
REFERENCE   8  (residues 1 to 901)
  AUTHORS   Sugihara,H., Moriyoshi,K., Ishii,T., Masu,M. and Nakanishi,S.
  TITLE     Structures and properties of seven isoforms of the NMDA receptor
            generated by alternative splicing
  JOURNAL   Biochem Biophys Res Commun 185 (3), 826-832 (1992)
   PUBMED   1352681
REFERENCE   9  (residues 1 to 901)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
REFERENCE   10 (residues 1 to 901)
  AUTHORS   Meguro,H., Mori,H., Araki,K., Kushiya,E., Kutsuwada,T.,
            Yamazaki,M., Kumanishi,T., Arakawa,M., Sakimura,K. and Mishina,M.
  TITLE     Functional characterization of a heteromeric NMDA receptor channel
            expressed from cloned cDNAs
  JOURNAL   Nature 357 (6373), 70-74 (1992)
   PUBMED   1374164
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FM039130.1, U08262.1 and JAXUCZ010000003.1.
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (2a) has the
            same N- and C-termini but is shorter compared to isoform 1b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U08262.1, SRR26643298.14330.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..901
                     /product="glutamate receptor ionotropic, NMDA 1 isoform 2a
                     precursor"
                     /note="glutamate [NMDA] receptor subunit zeta-1;
                     neurotransmitter receptor; NMDA R1 receptor C1 cassette;
                     N-methyl-D-aspartate glutamate receptor; NMD-R1;
                     N-methyl-D-aspartate receptor subunit NR1; glutamate
                     receptor ionotropic, NMDA 1; glutamate receptor,
                     ionotropic, N-methyl D-aspartate 1"
                     /calculated_mol_wt=99752
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1612
     Region          25..383
                     /region_name="PBP1_iGluR_NMDA_NR1"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR1, an essential
                     channel-forming subunit of the NMDA receptor; cd06379"
                     /db_xref="CDD:380602"
     Site            order(69..72,76,79,113,319,323,342)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Site            order(69..73,75..76,79..80,113..114,131,135,308..310,
                     319..320,322..323)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Region          395..799
                     /region_name="PBP2_iGluR_NMDA_Nr1"
                     /note="The ligand-binding domain of the NR1 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13719"
                     /db_xref="CDD:270437"
     Site            order(516..519,521,523..525,668,687..688,692,732,753..755,
                     758,764,780..783,786)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270437"
     Site            order(516..518,523,687..689,731..732)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270437"
     Region          835..863
                     /region_name="CaM_bdg_C0"
                     /note="Calmodulin-binding domain C0 of NMDA receptor NR1
                     subunit; pfam10562"
                     /db_xref="CDD:402271"
     CDS             1..901
                     /gene="Grin1"
                     /gene_synonym="GluN1; NMDAR1; NR1"
                     /coded_by="NM_001270605.1:325..3030"
                     /note="isoform 2a precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:24408"
                     /db_xref="RGD:2736"
ORIGIN      
        1 mstmhlltfa llfscsfara acdpkivnig avlstrkheq mfreavnqan krhgswkiql
       61 natsvthkpn aiqmalsvce dlissqvyai lvshpptpnd hftptpvsyt agfyripvlg
      121 lttrmsiysd ksihlsflrt vppyshqssv wfemmrvynw nhiillvsdd hegraaqkrl
      181 etlleeresk aekvlqfdpg tknvtallme arelearvii lsaseddaat vyraaamlnm
      241 tgsgyvwlvg ereisgnalr yapdgiiglq lingknesah isdavgvvaq avhelleken
      301 itdpprgcvg ntniwktgpl fkrvlmssky adgvtgrvef nedgdrkfan ysimnlqnrk
      361 lvqvgiyngt hvipndrkii wpggetekpr gyqmstrlki vtihqepfvy vkptmsdgtc
      421 keeftvngdp vkkvictgpn dtspgsprht vpqccygfci dlliklartm nftyevhlva
      481 dgkfgtqerv nnsnkkewng mmgellsgqa dmivapltin neraqyiefs kpfkyqglti
      541 lvkkeiprst ldsfmqpfqs tlwllvglsv hvvavmlyll drfspfgrfk vnseeeeeda
      601 ltlssamwfs wgvllnsgig egaprsfsar ilgmvwagfa miivasytan laaflvldrp
      661 eeritgindp rlrnpsdkfi yatvkqssvd iyfrrqvels tmyrhmekhn yesaaeaiqa
      721 vrdnklhafi wdsavlefea sqkcdlvttg elffrsgfgi gmrkdspwkq nvslsilksh
      781 engfmedldk twvryqecds rsnapatltf enmagvfmlv aggivagifl ifieiaykrh
      841 kdarrkqmql afaavnvwrk nlqstgggrg alqnqkdtvl prraiereeg qlqlcsrhre
      901 s
//
LOCUS       NP_112612               1905 aa            linear   ROD 28-APR-2025
DEFINITION  low-density lipoprotein receptor-related protein 4 precursor
            [Rattus norvegicus].
ACCESSION   NP_112612 XP_342465
VERSION     NP_112612.2
DBSOURCE    REFSEQ: accession NM_031322.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1905)
  AUTHORS   Wang,J., Qiu,X., Xu,T., Sheng,Z. and Yao,L.
  TITLE     Sclerostin/Receptor Related Protein 4 and Ginkgo Biloba Extract
            Alleviates beta-Glycerophosphate-Induced Vascular Smooth Muscle
            Cell Calcification By Inhibiting Wnt/beta-Catenin Pathway
  JOURNAL   Blood Purif 47 Suppl 1 (Suppl 1), 17-23 (2019)
   PUBMED   30699436
  REMARK    GeneRIF: beta-GP induced VSMC calcification by activating the
            Wnt/beta-catenin signaling pathway. Sclerostin and Lrp4 were
            involved in beta-GP-induced VSMC calcification and play an
            important role. GBE could alleviate VSMC calcification induced by
            beta-GP through inhibiting the Wnt/beta-catenin signaling pathway.
REFERENCE   2  (residues 1 to 1905)
  AUTHORS   Hoshi,T., Tezuka,T., Yokoyama,K., Iemura,S., Natsume,T. and
            Yamanashi,Y.
  TITLE     Mesdc2 plays a key role in cell-surface expression of Lrp4 and
            postsynaptic specialization in myotubes
  JOURNAL   FEBS Lett 587 (23), 3749-3754 (2013)
   PUBMED   24140340
REFERENCE   3  (residues 1 to 1905)
  AUTHORS   Witzemann,V., Chevessier,F., Pacifici,P.G. and Yampolsky,P.
  TITLE     The neuromuscular junction: selective remodeling of synaptic
            regulators at the nerve/muscle interface
  JOURNAL   Mech Dev 130 (6-8), 402-411 (2013)
   PUBMED   23032192
  REMARK    Review article
REFERENCE   4  (residues 1 to 1905)
  AUTHORS   Yumoto,N., Kim,N. and Burden,S.J.
  TITLE     Lrp4 is a retrograde signal for presynaptic differentiation at
            neuromuscular synapses
  JOURNAL   Nature 489 (7416), 438-442 (2012)
   PUBMED   22854782
REFERENCE   5  (residues 1 to 1905)
  AUTHORS   Zong,Y., Zhang,B., Gu,S., Lee,K., Zhou,J., Yao,G., Figueiredo,D.,
            Perry,K., Mei,L. and Jin,R.
  TITLE     Structural basis of agrin-LRP4-MuSK signaling
  JOURNAL   Genes Dev 26 (3), 247-258 (2012)
   PUBMED   22302937
  REMARK    GeneRIF: present the first crystal structure of an agrin-LRP4
            complex which is essential for neuronal agrin-induced acetylcholine
            receptor (AChR) clustering
REFERENCE   6  (residues 1 to 1905)
  AUTHORS   Simon-Chazottes,D., Tutois,S., Kuehn,M., Evans,M., Bourgade,F.,
            Cook,S., Davisson,M.T. and Guenet,J.L.
  TITLE     Mutations in the gene encoding the low-density lipoprotein receptor
            LRP4 cause abnormal limb development in the mouse
  JOURNAL   Genomics 87 (5), 673-677 (2006)
   PUBMED   16517118
REFERENCE   7  (residues 1 to 1905)
  AUTHORS   Li,Y., Chen,J., Lu,W., McCormick,L.M., Wang,J. and Bu,G.
  TITLE     Mesd binds to mature LDL-receptor-related protein-6 and antagonizes
            ligand binding
  JOURNAL   J Cell Sci 118 (Pt 22), 5305-5314 (2005)
   PUBMED   16263759
REFERENCE   8  (residues 1 to 1905)
  AUTHORS   Johnson,E.B., Hammer,R.E. and Herz,J.
  TITLE     Abnormal development of the apical ectodermal ridge and
            polysyndactyly in Megf7-deficient mice
  JOURNAL   Hum Mol Genet 14 (22), 3523-3538 (2005)
   PUBMED   16207730
REFERENCE   9  (residues 1 to 1905)
  AUTHORS   Tomita,Y., Kim,D.H., Magoori,K., Fujino,T. and Yamamoto,T.T.
  TITLE     A novel low-density lipoprotein receptor-related protein with type
            II membrane protein-like structure is abundant in heart
  JOURNAL   J Biochem 124 (4), 784-789 (1998)
   PUBMED   9756624
REFERENCE   10 (residues 1 to 1905)
  AUTHORS   Nakayama,M., Nakajima,D., Nagase,T., Nomura,N., Seki,N. and
            Ohara,O.
  TITLE     Identification of high-molecular-weight proteins with multiple
            EGF-like motifs by motif-trap screening
  JOURNAL   Genomics 51 (1), 27-34 (1998)
   PUBMED   9693030
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB073317.3.
            
            On Apr 9, 2011 this sequence version replaced NP_112612.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB073317.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760384
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1905
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..1905
                     /product="low-density lipoprotein receptor-related protein
                     4 precursor"
                     /note="low-density lipoprotein receptor-related protein 4;
                     multiple epidermal growth factor-like domains 7; LRP-4"
                     /calculated_mol_wt=209755
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2197
     mat_peptide     21..1905
                     /product="Low-density lipoprotein receptor-related protein
                     4. /id=PRO_0000017327"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
                     /calculated_mol_wt=209755
     Region          27..66
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(32,45,56..57)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(49,52,56,62..63)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            59..63
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          70..105
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(76,84,95..96)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(88,91,95,101..102)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            98..102
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          110..142
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(115,123,134..135)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(127,130,134,140..141)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            137..141
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          148..182
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(153,161,172..173)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(165,168,172,178..179)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            175..179
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          231..265
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(236,244,255..256)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(248,251,255,261..262)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            258..262
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          270..304
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(275,283,294..295)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(287,290,294,300..301)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            297..301
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          311..343
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(317,325,336..337)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(329,332,336,342..343)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            339..343
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          358..393
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          395..434
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(395,398,411)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          460..502
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          480..522
                     /region_name="LDL-receptor class B 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Site            498
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          505..545
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          523..565
                     /region_name="LDL-receptor class B 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          566..609
                     /region_name="LDL-receptor class B 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          566..607
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          590..632
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          610..652
                     /region_name="LDL-receptor class B 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          633..673
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          653..693
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          702..>729
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            719
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          749..982
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          785..827
                     /region_name="LDL-receptor class B 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          808..850
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          828..870
                     /region_name="LDL-receptor class B 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          871..914
                     /region_name="LDL-receptor class B 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          871..912
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          895..937
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            901
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          915..956
                     /region_name="LDL-receptor class B 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          957..998
                     /region_name="LDL-receptor class B 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1006..1043
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            1077
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          <1085..1277
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          1085..1123
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1093..1135
                     /region_name="LDL-receptor class B 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1128..1161
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1136..1178
                     /region_name="LDL-receptor class B 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1166..1203
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1179..1222
                     /region_name="LDL-receptor class B 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1179..1219
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          1212..1244
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1223..1263
                     /region_name="LDL-receptor class B 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1253..1277
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271320"
     Region          1264..1306
                     /region_name="LDL-receptor class B 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1313..1348
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1332..1583
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
     Region          1397..1439
                     /region_name="LDL-receptor class B 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Site            1415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1440..1482
                     /region_name="LDL-receptor class B 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Site            1467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1483..1526
                     /region_name="LDL-receptor class B 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1483..1524
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          1527..1568
                     /region_name="LDL-receptor class B 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1569..1610
                     /region_name="LDL-receptor class B 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1617..>1641
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1659..1696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Site            1724..1746
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     Region          1853..1905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QYP1.2)"
     CDS             1..1905
                     /gene="Lrp4"
                     /gene_synonym="Megf7"
                     /coded_by="NM_031322.3:14..5731"
                     /db_xref="GeneID:83469"
                     /db_xref="RGD:619731"
ORIGIN      
        1 mrrwwgalll gallcahgta snlecacgrs hftcavsalg ectcipaqwq cdgdndcgdh
       61 sdedgctlpt cspldfhcdn gkcirrswvc dgdndcedds deqdcpprec eedefpcqng
      121 ycirslwhcd gdndcgdnsd eqcdmrkcsd kefrcsdgsc iaehwycdgd tdckdgsdee
      181 scpsavpspp cnleefqcay grrildiyhc dgdddcgdws desdcsshqp crsgefmcds
      241 glcvnagwrc dgdadcddqs derncttsmc taeqfrcrsg rcvrlswrcd geddcadnsd
      301 eencentgsp qcasdqflcw ngrcigqrkl cngvndcgdn sdespqqncr prtgeencnv
      361 nnggcaqkcq mirgavqctc htgyrltedg rtcqdvneca eegycsqgct nsegafqcwc
      421 eagyelrpdr rsckalgpep vllfanridi rqvlphrsey tlllnnlena ialdfhhrre
      481 lvfwsdvtld rilranlngs nveevvstgl espgglavdw vhdklywtds gtsrievanl
      541 dgahrkvllw qslekpraia lhpmegtiyw tdwgntprie assmdgsgrr iiadthlfwp
      601 ngltidyagr rmywvdakhh vieranldgs hrkavisqgl phpfaitvfe dslywtdwht
      661 ksinsankft gknqeiirnk lhfpmdihtl hpqrqpagkn rcgdnnggct hlclpsgqny
      721 tcacptgfrk inshacaqsl dkfllfarrm dirrisfdte dlsddvipla dvrsavaldw
      781 dsrddhvywt dvstdtisra kwdgtgqkvv vdtslespag laidwvtnkl ywtdagtdri
      841 evantdgsmr tvliwenldr prdivvepmg gymywtdwga spkieragmd asnrqviiss
      901 nltwpnglai dygsqrlywa dagmktiefa gldgskrkvl igsqlphpfg ltlygqriyw
      961 tdwqtksiqs adrltgldre tlqenlenlm dihvfhrqrp pvttpcaven ggcshlclrs
     1021 pspsgfsctc ptginllldg ktcspgmnsf lifarridvr mvsldipyfa dvvvpinmtm
     1081 kntiaigvdp legkvywsds tlhrisrasl dgsqhediit tglqttdgla vdaigrkvyw
     1141 tdtgtnriev gnldgsmrkv lvwqnldspr aivlyhemgf mywtdwgena klersgmdgs
     1201 drtvlinnnl gwpngltvdk tssqllwada hterievadl nganrhtlvs pvqhpygltl
     1261 ldsyiywtdw qtrsihradk stgsnvilvr snlpglmdiq avdraqplgf nkcgsrnggc
     1321 shlclprpsg fscacptgiq lkgdgktcdp spetyllfss rgsirrisld tddhtdvhvp
     1381 vpglnnvisl dydsvdgkvy ytdvfldvir radlngsnme tvighglktt dglavdwvar
     1441 nlywtdtgrn tieasrldgs crkvlinnsl depraiavfp rkgylfwtdw ghiakieran
     1501 ldgserkvli nadlgwpngl tldydtrriy wvdahldrie sadlngklrq vlvshvshpf
     1561 altqqdrwiy wtdwqtksiq rvdkysgrnk etvlanvegl mdiivvspqr qtgtnacgvn
     1621 nggcshlcfa rasdfvcacp depdshpcsl vpglmppapr atslnekspv lpntlpttlh
     1681 ssttrtrtsp egaegrcser daqlglcahs neavpaapge glhvsyavgg llsvllillv
     1741 taalmlyrhr kskftdpgmg nltysnpsyr tstqevkiea apkpamynql cykkeggpdh
     1801 sytkekikiv egihllaghd aewgdlkqlr ssrggllrdh vcmktdtvsi qassgslddt
     1861 eteqllqeeq secssvhtat tperrgslpd tgwkherkls sesqv
//
LOCUS       NP_001104568             491 aa            linear   ROD 28-APR-2025
DEFINITION  tyrosine-protein kinase Lyn isoform B [Rattus norvegicus].
ACCESSION   NP_001104568
VERSION     NP_001104568.1
DBSOURCE    REFSEQ: accession NM_001111098.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Luo,L., Bokil,N.J., Wall,A.A., Kapetanovic,R., Lansdaal,N.M.,
            Marceline,F., Burgess,B.J., Tong,S.J., Guo,Z., Alexandrov,K.,
            Ross,I.L., Hibbs,M.L., Stow,J.L. and Sweet,M.J.
  TITLE     SCIMP is a transmembrane non-TIR TLR adaptor that promotes
            proinflammatory cytokine production from macrophages
  JOURNAL   Nat Commun 8, 14133 (2017)
   PUBMED   28098138
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Kassas,A., Moura,I.C., Yamashita,Y., Scheffel,J.,
            Guerin-Marchand,C., Blank,U., Sims,P.J., Wiedmer,T., Monteiro,R.C.,
            Rivera,J., Charles,N. and Benhamou,M.
  TITLE     Regulation of the tyrosine phosphorylation of Phospholipid
            Scramblase 1 in mast cells that are stimulated through the
            high-affinity IgE receptor
  JOURNAL   PLoS One 9 (10), e109800 (2014)
   PUBMED   25289695
  REMARK    GeneRIF: This study reveals a complex regulation for PLSCR1
            tyrosine phosphorylation in FcepsilonRI-activated mast cells, and
            that PLSCR1 sits at a crossroads between Lyn and Fyn pathways.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Lai,W.B., Wang,B.J., Hu,M.K., Hsu,W.M., Her,G.M. and Liao,Y.F.
  TITLE     Ligand-dependent activation of EphA4 signaling regulates the
            proteolysis of amyloid precursor protein through a Lyn-mediated
            pathway
  JOURNAL   Mol Neurobiol 49 (2), 1055-1068 (2014)
   PUBMED   24217950
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Zhu,Z., Li,R., Li,H., Zhou,T. and Davis,R.S.
  TITLE     FCRL5 exerts binary and compartment-specific influence on
            innate-like B-cell receptor signaling
  JOURNAL   Proc Natl Acad Sci U S A 110 (14), E1282-E1290 (2013)
   PUBMED   23509253
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Obata,Y., Fukumoto,Y., Nakayama,Y., Kuga,T., Dohmae,N. and
            Yamaguchi,N.
  TITLE     The Lyn kinase C-lobe mediates Golgi export of Lyn through
            conformation-dependent ACSL3 association
  JOURNAL   J Cell Sci 123 (Pt 15), 2649-2662 (2010)
   PUBMED   20605918
  REMARK    Erratum:[J Cell Sci. 2010 Aug 1;123(Pt 15):2681]
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Katagiri,T., Ogimoto,M., Hasegawa,K., Mizuno,K. and Yakura,H.
  TITLE     Selective regulation of Lyn tyrosine kinase by CD45 in immature B
            cells
  JOURNAL   J Biol Chem 270 (47), 27987-27990 (1995)
   PUBMED   7499277
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Pribluda,V.S., Pribluda,C. and Metzger,H.
  TITLE     Transphosphorylation as the mechanism by which the high-affinity
            receptor for IgE is phosphorylated upon aggregation
  JOURNAL   Proc Natl Acad Sci U S A 91 (23), 11246-11250 (1994)
   PUBMED   7526393
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Yamanashi,Y., Okada,M., Semba,T., Yamori,T., Umemori,H.,
            Tsunasawa,S., Toyoshima,K., Kitamura,D., Watanabe,T. and
            Yamamoto,T.
  TITLE     Identification of HS1 protein as a major substrate of
            protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 90 (8), 3631-3635 (1993)
   PUBMED   7682714
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Alai,M., Mui,A.L., Cutler,R.L., Bustelo,X.R., Barbacid,M. and
            Krystal,G.
  TITLE     Steel factor stimulates the tyrosine phosphorylation of the
            proto-oncogene product, p95vav, in human hemopoietic cells
  JOURNAL   J Biol Chem 267 (25), 18021-18025 (1992)
   PUBMED   1381360
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Tsukita,S., Oishi,K., Akiyama,T., Yamanashi,Y., Yamamoto,T. and
            Tsukita,S.
  TITLE     Specific proto-oncogenic tyrosine kinases of src family are
            enriched in cell-to-cell adherens junctions where the level of
            tyrosine phosphorylation is elevated
  JOURNAL   J Cell Biol 113 (4), 867-879 (1991)
   PUBMED   1709169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF000301.1 and JAXUCZ010000005.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' coding region, compared to variant 1, resulting in a
            shorter protein (isoform B).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF000301.1, AF000302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q12"
     Protein         1..491
                     /product="tyrosine-protein kinase Lyn isoform B"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase Lyn; lyn protein
                     non-receptor kinase; Yamaguchi sarcoma viral (v-yes-1)
                     oncogene homolog; v-yes-1 Yamaguchi sarcoma viral related
                     oncogene homolog"
                     /calculated_mol_wt=56002
     Region          46..101
                     /region_name="SH3_Lyn"
                     /note="Src homology 3 domain of Lyn Protein Tyrosine
                     Kinase; cd12004"
                     /db_xref="CDD:212937"
     Site            order(51,53,56..57,60,76..78,91,93,95..96)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212937"
     Region          104..204
                     /region_name="SH2_Src_Lyn"
                     /note="Src homology 2 (SH2) domain found in Lyn; cd10364"
                     /db_xref="CDD:198227"
     Site            order(115,135,137..140,145,161,163,196)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198227"
     Site            order(115,135,161,163)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198227"
     Site            order(162,190)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198227"
     Region          218..489
                     /region_name="PTKc_Lyn"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Lyn; cd05072"
                     /db_xref="CDD:270657"
     Site            order(232,234..236,240,252,254,298..301,305,346,350..351,
                     353,364,381..385,394,428)
                     /site_type="active"
                     /db_xref="CDD:270657"
     Site            order(232,240,252,254,298..301,304..305,308,350,353,364)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270657"
     Site            order(246,248,280,283,285,299,325,329,357,477)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270657"
     Site            order(335,338..339,402,464..466,468,470..471,474,478,
                     481..482,486)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270657"
     Site            order(346,350,381..385,394,428)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270657"
     Site            363..387
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270657"
     CDS             1..491
                     /gene="Lyn"
                     /gene_synonym="p53Lyn; p56Lyn"
                     /coded_by="NM_001111098.1:231..1706"
                     /note="isoform B is encoded by transcript variant 2"
                     /db_xref="GeneID:81515"
                     /db_xref="RGD:621017"
ORIGIN      
        1 mgcikskrkd nlnddgvdmk tqpvpesqll pgqrfqakdp eeqgdivval ypydgihpdd
       61 lsfkkgekmk vleehgewwk akslsskreg fipsnyvakv ntleteewff kditrkdaer
      121 qllapgnsag afliresetl kgsfslsvrd ydpmhgdvik hykirsldng gyyispritf
      181 pcisdmikhy qkqsdglcrr lekacispkp qkpwdkdawe ipresiklvk klgagqfgev
      241 wmgyynnstk vavktlkpgt msaqafleea nlmktlqhdk lvrlyavvtk eepiyiitef
      301 makgslldfl ksdegskvll pklidfsaqi aegmayierk nyihrdlraa nvlvseslmc
      361 kiadfglarv iedneytare gakfpikwta peainfgcft iksdvwsfgi llyeivtygk
      421 ipypgrtnad vmtalsqgyr mprmencpde lydimkmcwk esaeerptfd ylqsvlddfy
      481 tategqyqqq p
//
LOCUS       NP_001013889             876 aa            linear   ROD 28-APR-2025
DEFINITION  radial spoke head 10 homolog B [Rattus norvegicus].
ACCESSION   NP_001013889 XP_213713
VERSION     NP_001013889.1
DBSOURCE    REFSEQ: accession NM_001013867.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081935.1.
            
            On Apr 20, 2005 this sequence version replaced XP_213713.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081935.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12p11"
     Protein         1..876
                     /product="radial spoke head 10 homolog B"
                     /calculated_mol_wt=101456
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          <86..336
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          86..108
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          109..131
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          132..154
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          155..177
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          179..201
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          204..226
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          227..249
                     /region_name="MORN 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          251..273
                     /region_name="MORN 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          284..306
                     /region_name="MORN 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          307..329
                     /region_name="MORN 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          360..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     Region          841..876
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HB5.1)"
     CDS             1..876
                     /gene="Rsph10b"
                     /gene_synonym="RGD1311893"
                     /coded_by="NM_001013867.1:159..2789"
                     /db_xref="GeneID:288478"
                     /db_xref="RGD:1311893"
ORIGIN      
        1 mvkekkkadk kgdksarsps sisdnpeaak qeisaskqev apsavipvle tplkqtpkrd
       61 sehtyqsede tqyeepiltk livesyegek vrglyegegf avfqggntyh gmfseglmhg
      121 qgtyiwadgl kyegdfvkni pmnhgvytwp dgstyegevv ngmrngfgmf kcgtqpvsyi
      181 ghwchgkrhg kgsiyynqeg tswyegdwvy nikkgwgirc yksgniyegq wennmrhgeg
      241 rmrwlttnee ytghwekgiq ngfgthtwfl kripnsqypl rneyigafvn gfrhgqgkfy
      301 yasgamyege wvsnkkqgrg ritfkngrvy eglfsndhia qffeaemdys ysldrrsdis
      361 qrsrqargss vsadrepetl rkldgsesrs vlgssieldl nllldmypee sqeeekkqve
      421 yavlrnitel rriycfysgl gcdhsldntf lmtklhfwrf lkdcrfhhhn itladmdrvl
      481 svyngipiee ihspfrtill rtflnyllql ayyihhkefq nrspslflcf tklmaenihp
      541 hacqvkghlf neqqrtlysm nyidkcweiy taycrpneap pyeltmkmry flwmlkdfrm
      601 inkeltatkf mrviaednpf vydgmdsnfe lelvfleffe allcfslccm fdqmtrsylk
      661 apyddvttnr ygstqtvlnq sihrspsgat shdsevhfss tkssldkigv lpdgkirqse
      721 pklkkslsed kvskmnlkaq grglvfmsph gekyekskde qkeklnmwvn nlyvffvsvl
      781 fsaykheeal kekveenrlq eavlaqqkqi eneelearln ilreeearrq dfelditvlk
      841 eppevpavqp ltpsppkedl vsmqtskasp gkkkkk
//
LOCUS       NP_001014291             738 aa            linear   ROD 28-APR-2025
DEFINITION  leucine-rich repeat flightless-interacting protein 1 isoform 2
            [Rattus norvegicus].
ACCESSION   NP_001014291 XP_346075
VERSION     NP_001014291.1
DBSOURCE    REFSEQ: accession NM_001014269.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Labbe,P., Faure,E., Lecointe,S., Le Scouarnec,S., Kyndt,F.,
            Marrec,M., Le Tourneau,T., Offmann,B., Duplaa,C., Zaffran,S.,
            Schott,J.J. and Merot,J.
  TITLE     The alternatively spliced LRRFIP1 Isoform-1 is a key regulator of
            the Wnt/beta-catenin transcription pathway
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1864 (7), 1142-1152 (2017)
   PUBMED   28322931
  REMARK    GeneRIF: LRRFIP1-Iso1 is a muscle and cardiomyocyte specific Wnt
            transcription co-factor.
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Rotival,M., Ko,J.H., Srivastava,P.K., Kerloc'h,A., Montoya,A.,
            Mauro,C., Faull,P., Cutillas,P.R., Petretto,E. and Behmoaras,J.
  TITLE     Integrating phosphoproteome and transcriptome reveals new
            determinants of macrophage multinucleation
  JOURNAL   Mol Cell Proteomics 14 (3), 484-498 (2015)
   PUBMED   25532521
  REMARK    GeneRIF: Results identify LRRFIP1, SMARCA4, and DNMT1 as novel
            regulators of macrophage multinucleation.
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Gubern,C., Camos,S., Hurtado,O., Rodriguez,R., Romera,V.G.,
            Sobrado,M., Canadas,R., Moro,M.A., Lizasoain,I., Serena,J.,
            Mallolas,J. and Castellanos,M.
  TITLE     Characterization of Gcf2/Lrrfip1 in experimental cerebral ischemia
            and its role as a modulator of Akt, mTOR and beta-catenin signaling
            pathways
  JOURNAL   Neuroscience 268, 48-65 (2014)
   PUBMED   24637094
  REMARK    GeneRIF: First report to identify the different transcriptional
            variants of Lrrfip1 in the brain and to characterize their
            differential expression patterns and the subcellular location of
            the main isoform rLrrfip1 in ischemic conditions
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Choe,N., Kwon,J.S., Kim,J.R., Eom,G.H., Kim,Y., Nam,K.I., Ahn,Y.,
            Kee,H.J. and Kook,H.
  TITLE     The microRNA miR-132 targets Lrrfip1 to block vascular smooth
            muscle cell proliferation and neointimal hyperplasia
  JOURNAL   Atherosclerosis 229 (2), 348-355 (2013)
   PUBMED   23880186
  REMARK    GeneRIF: Our results suggest that miR-132 is a novel regulator of
            vascular smooth muscle cells proliferation that represses
            neointimal formation by inhibiting LRRFIP1 expression.
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Nguyen,J.B. and Modis,Y.
  TITLE     Crystal structure of the dimeric coiled-coil domain of the
            cytosolic nucleic acid sensor LRRFIP1
  JOURNAL   J Struct Biol 181 (1), 82-88 (2013)
   PUBMED   23099021
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Dai,P., Jeong,S.Y., Yu,Y., Leng,T., Wu,W., Xie,L. and Chen,X.
  TITLE     Modulation of TLR signaling by multiple MyD88-interacting partners
            including leucine-rich repeat Fli-I-interacting proteins
  JOURNAL   J Immunol 182 (6), 3450-3460 (2009)
   PUBMED   19265123
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Rikiyama,T., Curtis,J., Oikawa,M., Zimonjic,D.B., Popescu,N.,
            Murphy,B.A., Wilson,M.A. and Johnson,A.C.
  TITLE     GCF2: expression and molecular analysis of repression
  JOURNAL   Biochim Biophys Acta 1629 (1-3), 15-25 (2003)
   PUBMED   14522076
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Khachigian,L.M., Santiago,F.S., Rafty,L.A., Chan,O.L.,
            Delbridge,G.J., Bobik,A., Collins,T. and Johnson,A.C.
  TITLE     GC factor 2 represses platelet-derived growth factor A-chain gene
            transcription and is itself induced by arterial injury
  JOURNAL   Circ Res 84 (11), 1258-1267 (1999)
   PUBMED   10364563
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081883.1.
            
            On Apr 20, 2005 this sequence version replaced XP_346075.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081883.1, SRR8487230.132079.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132291, SAMD00132303
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q36"
     Protein         1..738
                     /product="leucine-rich repeat flightless-interacting
                     protein 1 isoform 2"
                     /note="leucine-rich repeat flightless-interacting protein
                     1; LRR FLII-interacting protein 1; leucine rich repeat (in
                     FLII) interacting protein 1"
                     /calculated_mol_wt=79888
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Region          40..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HF9.1)"
     Region          42..298
                     /region_name="LRRFIP"
                     /note="LRRFIP family; pfam09738"
                     /db_xref="CDD:462869"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UZ39; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Region          253..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UZ39; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UZ39; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Region          479..580
                     /region_name="DNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q32MZ4; propagated from
                     UniProtKB/Swiss-Prot (Q66HF9.1)"
     CDS             1..738
                     /gene="Lrrfip1"
                     /coded_by="NM_001014269.1:165..2381"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:367314"
                     /db_xref="RGD:1359548"
ORIGIN      
        1 mtspegaqnk eidclspeaq rlaearlaak raaraearei rmkelerqqk eveerpdkdf
       61 aekgsrnmps lsaatlaslg gtssrrgsgd tsismdteas ireikdslae veekykkamv
      121 snaqldnekt nfmyqvdtlk dmlleleeql aesqrqyeek nkeferekha hsilqfqfae
      181 vkealrqree mlekhgiiln seiatngets dtvndvgyqa ptkitkeeln alkaagegtl
      241 gkakevevkk eivekvgqre tlqdseqeqp klntgkdcvd rgvlhpgeka enqrpvedsa
      301 lspgplagak ceqevqsqdq entsilkspe qieshevtnk sdsrdsnspe psscrgglds
      361 evsgptalgi knqsensmds qgkenqedlg kgsfeprpdh vlgqtpeidk vsctdsrgtg
      421 gnhledvvqa gdtivedqvg tmasaeqsks menhigrsln dglgqssere laheaaelee
      481 altqssqagg entvteaeda avrdekplqa dvqatpaapt vqsghqdttg pgstdtkhts
      541 phakernkak seqqaealds pqkktknkkk knkkkkaaap metckdanee sscqdpdvgd
      601 geeeervqat dkkwaaetpe lkedpqsrps gkqndaeeds gpaegptdvl dqnslqcadg
      661 dispvgrkgp qrdasqigge eglvpsqhpg qadekgiegh svdnsdlsge lggfnsesge
      721 qareevgnsk skedctms
//
LOCUS       NP_001012117             664 aa            linear   ROD 28-APR-2025
DEFINITION  F-box only protein 43 [Rattus norvegicus].
ACCESSION   NP_001012117 XP_235375
VERSION     NP_001012117.2
DBSOURCE    REFSEQ: accession NM_001012117.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Suzuki,T., Suzuki,E., Yoshida,N., Kubo,A., Li,H., Okuda,E.,
            Amanai,M. and Perry,A.C.
  TITLE     Mouse Emi2 as a distinctive regulatory hub in second meiotic
            metaphase
  JOURNAL   Development 137 (19), 3281-3291 (2010)
   PUBMED   20724447
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Perrard,M.H., Chassaing,E., Montillet,G., Sabido,O. and Durand,P.
  TITLE     Cytostatic factor proteins are present in male meiotic cells and
            beta-nerve growth factor increases mos levels in rat late
            spermatocytes
  JOURNAL   PLoS One 4 (10), e7237 (2009)
   PUBMED   19802389
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Madgwick,S., Hansen,D.V., Levasseur,M., Jackson,P.K. and Jones,K.T.
  TITLE     Mouse Emi2 is required to enter meiosis II by reestablishing cyclin
            B1 during interkinesis
  JOURNAL   J Cell Biol 174 (6), 791-801 (2006)
   PUBMED   16966421
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Shoji,S., Yoshida,N., Amanai,M., Ohgishi,M., Fukui,T., Fujimoto,S.,
            Nakano,Y., Kajikawa,E. and Perry,A.C.
  TITLE     Mammalian Emi2 mediates cytostatic arrest and transduces the signal
            for meiotic exit via Cdc20
  JOURNAL   EMBO J 25 (4), 834-845 (2006)
   PUBMED   16456547
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC082107.1.
            
            On Oct 23, 2008 this sequence version replaced NP_001012117.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC082107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760434
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q22"
     Protein         1..664
                     /product="F-box only protein 43"
                     /note="endogenous meiotic inhibitor 2"
                     /calculated_mol_wt=73098
     Region          1..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H04.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q4G163; propagated from
                     UniProtKB/Swiss-Prot (Q66H04.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4G163; propagated from
                     UniProtKB/Swiss-Prot (Q66H04.2)"
     Region          315..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H04.2)"
     Region          454..502
                     /region_name="F-box_FBXO43"
                     /note="F-box domain found in F-box only protein 43
                     (FBXO43) and similar proteins; cd22171"
                     /db_xref="CDD:438942"
     Site            order(456,464,467..468,471..472,476,478..479,483..485,487)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438942"
     Region          590..640
                     /region_name="BRcat_RBR_FBXO43"
                     /note="BRcat domain found in F-box only protein 43
                     (FBXO43); cd20365"
                     /db_xref="CDD:439026"
     Region          637..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66H04.2)"
     CDS             1..664
                     /gene="Fbxo43"
                     /coded_by="NM_001012117.1:287..2281"
                     /db_xref="GeneID:315034"
                     /db_xref="RGD:1310225"
ORIGIN      
        1 mpqkhsashr agsnmgssav tvrcpslpdf gptssfkhrg phelsetcsf skkekdpmlt
       61 cehletprlg fpnpavspsp rkksvslrke keespelcet pklrrkkctl rrrldltltl
      121 lkgdsdsqss slesnishsl slekrlrdst sgfpkednfs plvtstvkte daisssqnsr
      181 lhfsqhktst iddskddcgl feveclspie gndfkdsvth fsdsglsasd entcpellgs
      241 sgsqttygad vttsvtpvss liakikfhgs qtlassaevr dslstpedsg fcslswdkse
      301 dflsdqegsf qelqkhrgtp tvgdlvrqpk hpgrlrrlpt lqeqgsqset ddemqvahps
      361 agvrvgtasg vlesqqgsee ksgdltlsfk dlsntpalql vcelfmkskr krfeqaddqe
      421 fseereegki arlqhvlagl igkkmgierl diltelqyrn lkhilamvld sltaeslysa
      481 wnvsrnwrgi vaqdkranrr rklfiaqlka kaqgaavlrv qdaatrlrll srlalrsvqa
      541 qaqapngqne qapaqspwge vltpvasssl thlrskqeqy lkvartlftd ealkpcprcq
      601 spakyqphkk rglcsrlacg fdfcvlclca yhgsedcrrg sakgrgsrdv lpgsaqskrn
      661 lkrl
//
LOCUS       NP_001263399             344 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich transmembrane protein 2 [Rattus norvegicus].
ACCESSION   NP_001263399 XP_001078254 XP_341932
VERSION     NP_001263399.1
DBSOURCE    REFSEQ: accession NM_001276470.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Mo,J., Wang,B., Zhu,X., Wu,X. and Liu,Y.
  TITLE     PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by
            influencing synaptic function in the primary motor cortex of rats
  JOURNAL   Neurobiol Dis 121, 274-285 (2019)
   PUBMED   30347267
  REMARK    GeneRIF: Study shows that proline-rich transmembrane protein 2
            (PRRT2) deficiency induces paroxysmal kinesigenic dyskinesia by
            influencing synaptic function in the primary motor cortex of rats.
            Results provide new insights into the function of PRRT2 in synaptic
            transmission and movement control.
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Tan,G.H., Liu,Y.Y., Wang,L., Li,K., Zhang,Z.Q., Li,H.F., Yang,Z.F.,
            Li,Y., Li,D., Wu,M.Y., Yu,C.L., Long,J.J., Chen,R.C., Li,L.X.,
            Yin,L.P., Liu,J.W., Cheng,X.W., Shen,Q., Shu,Y.S., Sakimura,K.,
            Liao,L.J., Wu,Z.Y. and Xiong,Z.Q.
  TITLE     PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by
            regulating synaptic transmission in cerebellum
  JOURNAL   Cell Res 28 (1), 90-110 (2018)
   PUBMED   29056747
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Liu,Y.T., Nian,F.S., Chou,W.J., Tai,C.Y., Kwan,S.Y., Chen,C.,
            Kuo,P.W., Lin,P.H., Chen,C.Y., Huang,C.W., Lee,Y.C., Soong,B.W. and
            Tsai,J.W.
  TITLE     PRRT2 mutations lead to neuronal dysfunction and neurodevelopmental
            defects
  JOURNAL   Oncotarget 7 (26), 39184-39196 (2016)
   PUBMED   27172900
  REMARK    GeneRIF: PRRT2 mutations have roles in neuronal dysfunction and
            neurodevelopmental defects
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Valente,P., Castroflorio,E., Rossi,P., Fadda,M., Sterlini,B.,
            Cervigni,R.I., Prestigio,C., Giovedi,S., Onofri,F., Mura,E.,
            Guarnieri,F.C., Marte,A., Orlando,M., Zara,F., Fassio,A.,
            Valtorta,F., Baldelli,P., Corradi,A. and Benfenati,F.
  TITLE     PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter
            Release Machinery
  JOURNAL   Cell Rep 15 (1), 117-131 (2016)
   PUBMED   27052163
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Rossi,P., Sterlini,B., Castroflorio,E., Marte,A., Onofri,F.,
            Valtorta,F., Maragliano,L., Corradi,A. and Benfenati,F.
  TITLE     A Novel Topology of Proline-rich Transmembrane Protein 2 (PRRT2):
            HINTS FOR AN INTRACELLULAR FUNCTION AT THE SYNAPSE
  JOURNAL   J Biol Chem 291 (12), 6111-6123 (2016)
   PUBMED   26797119
  REMARK    Erratum:[J Biol Chem. 2018 Mar 23;293(12):4581. doi:
            10.1074/jbc.AAC118.002651. PMID: 29572331]
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Schwenk,J., Harmel,N., Brechet,A., Zolles,G., Berkefeld,H.,
            Muller,C.S., Bildl,W., Baehrens,D., Huber,B., Kulik,A., Klocker,N.,
            Schulte,U. and Fakler,B.
  TITLE     High-resolution proteomics unravel architecture and molecular
            diversity of native AMPA receptor complexes
  JOURNAL   Neuron 74 (4), 621-633 (2012)
   PUBMED   22632720
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Chen,W.J., Lin,Y., Xiong,Z.Q., Wei,W., Ni,W., Tan,G.H., Guo,S.L.,
            He,J., Chen,Y.F., Zhang,Q.J., Li,H.F., Lin,Y., Murong,S.X., Xu,J.,
            Wang,N. and Wu,Z.Y.
  TITLE     Exome sequencing identifies truncating mutations in PRRT2 that
            cause paroxysmal kinesigenic dyskinesia
  JOURNAL   Nat Genet 43 (12), 1252-1255 (2011)
   PUBMED   22101681
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On or before Feb 17, 2013 this sequence version replaced
            XP_341932.4, XP_001078254.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213699.1, SRR26643298.5344.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760393 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q37"
     Protein         1..344
                     /product="proline-rich transmembrane protein 2"
                     /note="Dispanin subfamily B member 3"
                     /calculated_mol_wt=35690
     Region          1..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PUL5; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Region          <64..>186
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Region          233..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            244
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9PUL5; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PUL5; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9PUL5; propagated from
                     UniProtKB/Swiss-Prot (D3ZFB6.1)"
     Region          268..334
                     /region_name="CD225"
                     /note="Interferon-induced transmembrane protein;
                     pfam04505"
                     /db_xref="CDD:461336"
     Site            322..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (D3ZFB6.1)"
     CDS             1..344
                     /gene="Prrt2"
                     /gene_synonym="DSPB3; RGD1564195"
                     /coded_by="NM_001276470.1:201..1235"
                     /db_xref="GeneID:361651"
                     /db_xref="RGD:1564195"
ORIGIN      
        1 maasssevse mkgvedssnt hsegprhsee gmgpvqvvae nldqpealqs gpdttaapvd
       61 sgpkaelape ttetpvetpe tvqatdlsvn pgedsktcps pkeacqepas rpevnreata
      121 eqgaeqqsaa ppeptseqal qlntqsdpqp tsqpppkppl qaepptqenp ttevltestg
      181 ekqengavvp lqagdgeegp apqphsppst ktppangapp rvlqklveed rigrahgghp
      241 gsprgslsrh pssqlagpgv eggegtqkpr dyiilailsc fcpmwpvniv afayavmsrn
      301 slqqgdvdga qrlgrvakll sivalvggvl iiiascvinl gvyk
//
LOCUS       NP_001099561             387 aa            linear   ROD 28-APR-2025
DEFINITION  small ribosomal subunit protein mS31 [Rattus norvegicus].
ACCESSION   NP_001099561 XP_001073425 XP_214383
VERSION     NP_001099561.1
DBSOURCE    REFSEQ: accession NM_001106091.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Arden,S.D., Roep,B.O., Neophytou,P.I., Usac,E.F., Duinkerken,G., de
            Vries,R.R. and Hutton,J.C.
  TITLE     Imogen 38: a novel 38-kD islet mitochondrial autoantigen recognized
            by T cells from a newly diagnosed type 1 diabetic patient
  JOURNAL   J Clin Invest 97 (2), 551-561 (1996)
   PUBMED   8567980
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473970.2.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_214383.4, XP_001073425.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC158691.1, SRR8487231.45588.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.5"
     Protein         1..387
                     /product="small ribosomal subunit protein mS31"
                     /note="28S ribosomal protein S31, mitochondrial"
                     /calculated_mol_wt=37959
     transit_peptide 1..56
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (B0BN56.1)"
                     /calculated_mol_wt=6021
     mat_peptide     57..387
                     /product="Small ribosomal subunit protein mS31.
                     /id=PRO_0000383148"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN56.1)"
                     /calculated_mol_wt=37959
     Region          59..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN56.1)"
     Region          87..379
                     /region_name="MRP-S31"
                     /note="Mitochondrial 28S ribosomal protein S31; pfam15433"
                     /db_xref="CDD:464714"
     Region          203..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B0BN56.1)"
     CDS             1..387
                     /gene="Mrps31"
                     /gene_synonym="MRP-S31; S31mt"
                     /coded_by="NM_001106091.1:48..1211"
                     /db_xref="GeneID:290850"
                     /db_xref="RGD:1307668"
ORIGIN      
        1 mlhripafir prpfsglpls cgnrevsvaa svlpaagsga vrtentiqrh fctsrsicsk
       61 kddqsvpane tsqkaaesqg egketlkknl ldvikdmkvq lntanvkttk prgrqppahl
      121 etavgrlqka lgepprkrne flspelvaaa savadslpfd kqttksellk qlqqheeesr
      181 aqtdrqkrrv sftqiisnmk iakspsmrvs srpqhqiqfd eevdsslsqe kpadfrrrkc
      241 lfkgkrlsif dvkafddeap epeaapslwe iefakqlatv seqpfgngfe emiqwtkegk
      301 lwefpvnnea gldddgsefh ehiflekhle dfpkqgpirl fmelvtcgls knpylsvrqk
      361 vehiewfrny fnekrdilke nnihlts
//
LOCUS       NP_775169               2204 aa            linear   ROD 28-APR-2025
DEFINITION  protein unc-13 homolog C [Rattus norvegicus].
ACCESSION   NP_775169 XP_003750583
VERSION     NP_775169.4
DBSOURCE    REFSEQ: accession NM_173146.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 2204)
  AUTHORS   Kawabe,H., Mitkovski,M., Kaeser,P.S., Hirrlinger,J., Opazo,F.,
            Nestvogel,D., Kalla,S., Fejtova,A., Verrier,S.E., Bungers,S.R.,
            Cooper,B.H., Varoqueaux,F., Wang,Y., Nehring,R.B.,
            Gundelfinger,E.D., Rosenmund,C., Rizzoli,S.O., Sudhof,T.C.,
            Rhee,J.S. and Brose,N.
  TITLE     ELKS1 localizes the synaptic vesicle priming protein bMunc13-2 to a
            specific subset of active zones
  JOURNAL   J Cell Biol 216 (4), 1143-1161 (2017)
   PUBMED   28264913
  REMARK    Erratum:[J Cell Biol. 2017 Apr 3;216(4):1205. doi:
            10.1083/jcb.20160608603092017c. PMID: 28289090]
REFERENCE   2  (residues 1 to 2204)
  AUTHORS   Chen,Z., Cooper,B., Kalla,S., Varoqueaux,F. and Young,S.M. Jr.
  TITLE     The Munc13 proteins differentially regulate readily releasable pool
            dynamics and calcium-dependent recovery at a central synapse
  JOURNAL   J Neurosci 33 (19), 8336-8351 (2013)
   PUBMED   23658173
REFERENCE   3  (residues 1 to 2204)
  AUTHORS   Lipstein,N., Schaks,S., Dimova,K., Kalkhof,S., Ihling,C.,
            Kolbel,K., Ashery,U., Rhee,J., Brose,N., Sinz,A. and Jahn,O.
  TITLE     Nonconserved Ca(2+)/calmodulin binding sites in Munc13s
            differentially control synaptic short-term plasticity
  JOURNAL   Mol Cell Biol 32 (22), 4628-4641 (2012)
   PUBMED   22966208
REFERENCE   4  (residues 1 to 2204)
  AUTHORS   Augustin,I., Korte,S., Rickmann,M., Kretzschmar,H.A., Sudhof,T.C.,
            Herms,J.W. and Brose,N.
  TITLE     The cerebellum-specific Munc13 isoform Munc13-3 regulates
            cerebellar synaptic transmission and motor learning in mice
  JOURNAL   J Neurosci 21 (1), 10-17 (2001)
   PUBMED   11150314
REFERENCE   5  (residues 1 to 2204)
  AUTHORS   Augustin,I., Betz,A., Herrmann,C., Jo,T. and Brose,N.
  TITLE     Differential expression of two novel Munc13 proteins in rat brain
  JOURNAL   Biochem J 337 (Pt 3) (Pt 3), 363-371 (1999)
   PUBMED   9895278
REFERENCE   6  (residues 1 to 2204)
  AUTHORS   Brose,N., Hofmann,K., Hata,Y. and Sudhof,T.C.
  TITLE     Mammalian homologues of Caenorhabditis elegans unc-13 gene define
            novel family of C2-domain proteins
  JOURNAL   J Biol Chem 270 (42), 25273-25280 (1995)
   PUBMED   7559667
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U75361.1.
            
            On Nov 22, 2013 this sequence version replaced NP_775169.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U75361.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132266,
                                           SAMD00132272 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2204
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..2204
                     /product="protein unc-13 homolog C"
                     /note="Munc13-3; protein unc-13 homolog C-like"
                     /calculated_mol_wt=249006
     Region          28..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62770.3)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62770.3)"
     Region          128..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62770.3)"
     Region          419..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62770.3)"
     Region          <446..768
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62770.3)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62770.3)"
     Region          587..635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62770.3)"
     Region          647..770
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62770.3)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62770.3)"
     Site            1017
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K0T7; propagated from
                     UniProtKB/Swiss-Prot (Q62770.3)"
     Region          1069..1150
                     /region_name="C1_Munc13-2-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in Munc13-2, Munc13-3 and similar proteins; cd20859"
                     /db_xref="CDD:410409"
     Site            order(1093..1099,1107..1111,1114)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410409"
     Region          1210..1336
                     /region_name="C2B_Munc13"
                     /note="C2 domain second repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd04027"
                     /db_xref="CDD:175993"
     Site            order(1226,1232,1278,1280,1297)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175993"
     Region          1530..2018
                     /region_name="MUN"
                     /note="MUN domain; pfam06292"
                     /db_xref="CDD:461870"
     Region          2052..2171
                     /region_name="C2C_Munc13"
                     /note="C2 domain third repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08395"
                     /db_xref="CDD:176041"
     CDS             1..2204
                     /gene="Unc13c"
                     /gene_synonym="Unc13h3"
                     /coded_by="NM_173146.2:54..6668"
                     /db_xref="GeneID:286931"
                     /db_xref="RGD:628592"
ORIGIN      
        1 mvaslfksli layihklckg mftkklgntt kkkenrqqnk dqdfptaght kppklsnalk
       61 stvkkiakcs strnfsvede eghkdfslsp tfsyrvaian glqtavtnsd edllqelssi
      121 essysesfne lrsstenqvq sthtmpvrrn rksssslaps egssdgertl htlklgalrk
      181 lrkwkksqec vssdselstv kktwgirsks ldrtarnpkt nvlepgfsss gcisqthdvm
      241 emifkelqgi sqietelsel rghvnalkys ideisssvev vqseieqlrt gfvqarretr
      301 dihdyikhlg hmgskvslrf lnvpeerhey vesvvyqilv dkmgfsdvpn aikiefaqri
      361 gqqrdcpnak prpilvyfet pqqrdsvlkk syklkgtgia istdiltydi rerkekgvlp
      421 ssqtyesmdm klstpepkak knawlspnds drelesdlsr ssyadspakg sssksssksh
      481 sarsknkaan srtsqksdyn krpskppase kptphyveat plwhsqsdff tpklsrsesd
      541 fsklcqsyse dfsesqffcr tngssllsss drelwqrkqe gmtalyhspq dqgldgnipt
      601 vpgqgeient etvdsgmsns vvcasgdrsn ysgsqlslhe dlspwkewnq aghgtdglds
      661 stqepfdydt nslsdqqldm sskdlddlgk chsdlqddse sydltqddns spcpgldnep
      721 qgqwvgqyds yqktnsndly pnqshpsmmy rsqselqsdd seaaqpkswh srlsidlsdk
      781 tfkfpkfgst lqraksalev vwnkstqsls gcedsgsslm grfrtlsqst anessttlds
      841 diytepyyyk aeeeedycep vadsetdyve vmeqvlakle nrtsvtevde hikeydhpsy
      901 etpyetpqde gydgqaddii segeletlne pavemelved esqnlpvepp evmkpkrirp
      961 sfkeaalray kkqmaeleek ilagdsssvd ekarivsgnd ldaskfsalq vfggagrgly
     1021 gidsmpdlrr kktlpivrdv amtlaarksg lslamvirts lnneelkmhv frktlqaliy
     1081 pissttphnf evwtattpty cyecegllwg iarqgmkcle cgvkchekcq dllnadclqr
     1141 aaeksskhga edktqtiita mkermkirer nrpevfeviq emfqiskedf vqytkaakqs
     1201 vldgtskwsa kititvvsaq glqakdktgs sdpyvtvqvg knkrrtktif gnlnpvwdek
     1261 fyfechnstd rikvrvwded ddiksrvkqh fkkesddflg qtivevrtls gemdvwynle
     1321 krtdksavsg airlkinvei kgeekvapyh iqytclhenl fhyltevksn gsvkipevkg
     1381 deawkvffdd asqeivdefa mrygvesiyq amthfsclss kymcpgvpav msallanina
     1441 fyahttvstn vqvsasdrfa atnfgrekfi klldqlhnsl ridlskyren fpasnserlq
     1501 dlkstvdllt sitffrmkvl elqsppkasa vvkdcvracl dstykyifdn chelysqlid
     1561 pskkqdvpre eqgpttknld fwpqlitlmv tiidedktay tpvlnqfpqe lnmgkisaei
     1621 mwslfaldmk yaleehekqr lckstdymnl hfkvkwfyne yvrelpafkd avpeyslwfe
     1681 pfvmqwlden edvsmeflhg algrdkkdgf qqtsdhalfs csvvdvfaql nqsfeiikkl
     1741 ecpnpealsh lmrrfaktin kvlvqyaaiv ssdfssycdk etvpcilmnn iqqlrvqlek
     1801 mfesmggkel dpeastilke lqiklngvld alsvtygesf qlvieecikq mgaelnqmra
     1861 ngnsaanknn aamdaeivlr plmdfldkil slsakicekt vlkrvlkelw klvlnkiekq
     1921 ivlppltdqt gpqmifiaak elgqlsklke hmirddakgl tprqcaimev vlatikqyfh
     1981 aggnglkknf lekspdlhsl ryalslytqt tdalikkfie tqgsqsrssk davgqisvhv
     2041 dvtttpgtge hkvtvkviai ndlnwqtttm frpfvevcml gpslgdkkrk qgtktksntw
     2101 spkynetfqf ilgnenrpga yelhlsvkdy cfaredriig mtviqlqnia ekgsygawyp
     2161 llknlsmdet gltilrilsq rtsddvakef vrlksetrsi desa
//
LOCUS       NP_598275                302 aa            linear   ROD 28-APR-2025
DEFINITION  rab effector Noc2 [Rattus norvegicus].
ACCESSION   NP_598275
VERSION     NP_598275.1
DBSOURCE    REFSEQ: accession NM_133591.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Koumanov,F., Pereira,V.J., Richardson,J.D., Sargent,S.L.,
            Fazakerley,D.J. and Holman,G.D.
  TITLE     Insulin regulates Rab3-Noc2 complex dissociation to promote GLUT4
            translocation in rat adipocytes
  JOURNAL   Diabetologia 58 (8), 1877-1886 (2015)
   PUBMED   26024738
  REMARK    GeneRIF: discovery of the involvement of Rab3 and Noc2 in an
            insulin-regulated step in GLUT4 translocation suggests that the
            control of this translocation process is unexpectedly similar to
            regulated secretion and particularly pancreatic insulin-vesicle
            release.
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Handley,M.T. and Burgoyne,R.D.
  TITLE     The Rab27 effector Rabphilin, unlike Granuphilin and Noc2, rapidly
            exchanges between secretory granules and cytosol in PC12 cells
  JOURNAL   Biochem Biophys Res Commun 373 (2), 275-281 (2008)
   PUBMED   18573236
  REMARK    GeneRIF: Three Rab3/27 effectors, Granuphilin, Noc2, and Rabphilin,
            in PC12 cells using fluorescence recovery after photobleaching of
            EGFP-tagged proteins.
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Imai,A., Yoshie,S., Nashida,T., Shimomura,H. and Fukuda,M.
  TITLE     Functional involvement of Noc2, a Rab27 effector, in rat parotid
            acinar cells
  JOURNAL   Arch Biochem Biophys 455 (2), 127-135 (2006)
   PUBMED   17067543
  REMARK    GeneRIF: Our results suggest that the Noc2/Rab27 complex is an
            important constituent of the early stages of IPR-stimulated amylase
            release.
            Erratum:[Arch Biochem Biophys. 2007 Sep 1;465(1):301]
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Matsumoto,M., Miki,T., Shibasaki,T., Kawaguchi,M., Shinozaki,H.,
            Nio,J., Saraya,A., Koseki,H., Miyazaki,M., Iwanaga,T. and Seino,S.
  TITLE     Noc2 is essential in normal regulation of exocytosis in endocrine
            and exocrine cells
  JOURNAL   Proc Natl Acad Sci U S A 101 (22), 8313-8318 (2004)
   PUBMED   15159548
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Fukuda,M., Kanno,E. and Yamamoto,A.
  TITLE     Rabphilin and Noc2 are recruited to dense-core vesicles through
            specific interaction with Rab27A in PC12 cells
  JOURNAL   J Biol Chem 279 (13), 13065-13075 (2004)
   PUBMED   14722103
  REMARK    GeneRIF: Rabphilin and Noc2 are recruited to dense-core vesicles
            through specific interaction with Rab27A in rat cells
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Cheviet,S., Coppola,T., Haynes,L.P., Burgoyne,R.D. and Regazzi,R.
  TITLE     The Rab-binding protein Noc2 is associated with insulin-containing
            secretory granules and is essential for pancreatic beta-cell
            exocytosis
  JOURNAL   Mol Endocrinol 18 (1), 117-126 (2004)
   PUBMED   14593078
  REMARK    GeneRIF: Noc2 is a potential partner of Munc13, a component of the
            machinery that controls vesicle priming and insulin exocytosis
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Leenders,A.G., Lopes da Silva,F.H., Ghijsen,W.E. and Verhage,M.
  TITLE     Rab3a is involved in transport of synaptic vesicles to the active
            zone in mouse brain nerve terminals
  JOURNAL   Mol Biol Cell 12 (10), 3095-3102 (2001)
   PUBMED   11598194
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Haynes,L.P., Evans,G.J., Morgan,A. and Burgoyne,R.D.
  TITLE     A direct inhibitory role for the Rab3-specific effector, Noc2, in
            Ca2+-regulated exocytosis in neuroendocrine cells
  JOURNAL   J Biol Chem 276 (13), 9726-9732 (2001)
   PUBMED   11134008
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Kotake,K., Ozaki,N., Mizuta,M., Sekiya,S., Inagaki,N. and Seino,S.
  TITLE     Noc2, a putative zinc finger protein involved in exocytosis in
            endocrine cells
  JOURNAL   J Biol Chem 272 (47), 29407-29410 (1997)
   PUBMED   9367993
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091126.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091126.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..302
                     /product="rab effector Noc2"
                     /note="no C2 domains protein; rabphilin-3A-like protein"
                     /calculated_mol_wt=33302
     Region          45..159
                     /region_name="FYVE_2"
                     /note="FYVE-type zinc finger; pfam02318"
                     /db_xref="CDD:426716"
     Region          174..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54880.1)"
     Region          206..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O54880.1)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q768S4; propagated from
                     UniProtKB/Swiss-Prot (O54880.1)"
     CDS             1..302
                     /gene="Rph3al"
                     /gene_synonym="Noc2"
                     /coded_by="NM_133591.2:116..1024"
                     /db_xref="GeneID:171123"
                     /db_xref="RGD:620342"
ORIGIN      
        1 madtifssgn dqwvcpndrq lalraklqtg wsvhtyqtek qrrtqclspg evevilqviq
       61 raerldileq qrigrlverl etmqknvmgn gvsqcllcge mlgflgsssv fckdcrkkvc
      121 tkcgieaspg qkrplwlcki cseqrevwkr sgawfykglp kyilplktpg raddphfrpl
      181 pveptepqpq saevsrvytw argrvvssds dsdsdlssss ledrpmpsgi kgtkydkprg
      241 dsggsmespr mgparppshl sgsqsslgse tgagatdpqg gtlprpeprv sgkrhtwatt
      301 hy
//
LOCUS       NP_058931                334 aa            linear   ROD 28-APR-2025
DEFINITION  3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
            [Rattus norvegicus].
ACCESSION   NP_058931
VERSION     NP_058931.1
DBSOURCE    REFSEQ: accession NM_017235.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Matsuoka,H., Uchino,Y., Choshi,M., Nakamura,T. and Michihara,A.
  TITLE     Stroke-prone spontaneously hypertensive rats have reduced
            hydroxysteroid 17-beta dehydrogenase 7 levels for low cholesterol
            biosynthesis
  JOURNAL   Clin Exp Pharmacol Physiol 47 (2), 255-262 (2020)
   PUBMED   31587341
  REMARK    GeneRIF: Stroke-prone spontaneously hypertensive rats have reduced
            hydroxysteroid 17-beta dehydrogenase 7 levels for low cholesterol
            biosynthesis.
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Pascual-Mathey,L.I., Rojas-Duran,F., Aranda-Abreu,G.E., Manzo,J.,
            Herrera-Covarrubias,D., Munoz-Zavaleta,D.A., Garcia,L.I. and
            Hernandez,M.E.
  TITLE     Effect of hyperprolactinemia on PRL-receptor expression and
            activation of Stat and Mapk cell signaling in the prostate of
            long-term sexually-active rats
  JOURNAL   Physiol Behav 157, 170-177 (2016)
   PUBMED   26873413
  REMARK    GeneRIF: This study showed that Effect of hyperprolactinemia on
            PRL-receptor expression in the prostate of long-term
            sexually-active rats.
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Salilew-Wondim,D., Wang,Q., Tesfaye,D., Schellander,K., Hoelker,M.,
            Hossain,M.M. and Tsang,B.K.
  TITLE     Polycystic ovarian syndrome is accompanied by repression of gene
            signatures associated with biosynthesis and metabolism of steroids,
            cholesterol and lipids
  JOURNAL   J Ovarian Res 8, 24 (2015)
   PUBMED   25887459
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Stottmann,R.W., Moran,J.L., Turbe-Doan,A., Driver,E., Kelley,M. and
            Beier,D.R.
  TITLE     Focusing forward genetics: a tripartite ENU screen for
            neurodevelopmental mutations in the mouse
  JOURNAL   Genetics 188 (3), 615-624 (2011)
   PUBMED   21515572
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Marijanovic,Z., Laubner,D., Moller,G., Gege,C., Husen,B.,
            Adamski,J. and Breitling,R.
  TITLE     Closing the gap: identification of human 3-ketosteroid reductase,
            the last unknown enzyme of mammalian cholesterol biosynthesis
  JOURNAL   Mol Endocrinol 17 (9), 1715-1725 (2003)
   PUBMED   12829805
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Nokelainen,P., Peltoketo,H., Vihko,R. and Vihko,P.
  TITLE     Expression cloning of a novel estrogenic mouse 17
            beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase
            (m17HSD7), previously described as a prolactin receptor-associated
            protein (PRAP) in rat
  JOURNAL   Mol Endocrinol 12 (7), 1048-1059 (1998)
   PUBMED   9658408
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Duan,W.R., Parmer,T.G., Albarracin,C.T., Zhong,L. and Gibori,G.
  TITLE     PRAP, a prolactin receptor associated protein: its gene expression
            and regulation in the corpus luteum
  JOURNAL   Endocrinology 138 (8), 3216-3221 (1997)
   PUBMED   9231770
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Duan,W.R., Linzer,D.I. and Gibori,G.
  TITLE     Cloning and characterization of an ovarian-specific protein that
            associates with the short form of the prolactin receptor
  JOURNAL   J Biol Chem 271 (26), 15602-15607 (1996)
   PUBMED   8663045
REFERENCE   10 (residues 1 to 334)
  AUTHORS   McLean,M.P., Nelson,S., Parmer,T., Khan,I., Steinschneider,A.,
            Puryear,T. and Gibori,G.
  TITLE     Identification and characterization of an abundant phosphoprotein
            specific to the large luteal cell
  JOURNAL   Endocrinology 126 (4), 1796-1805 (1990)
   PUBMED   2318142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000013.1, FM073997.1 and FN803430.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U44803.1, SRR26643288.49894.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="13"
                     /map="13q24"
     Protein         1..334
                     /product="3-keto-steroid reductase/17-beta-hydroxysteroid
                     dehydrogenase 7"
                     /EC_number="1.1.1.62"
                     /EC_number="1.1.1.270"
                     /EC_number="1.1.1.210"
                     /note="3-keto-steroid reductase; prolactin
                     receptor-associated protein; PRAP; 17-beta-HSD 7; PRL
                     receptor-associated protein; estradiol
                     17-beta-dehydrogenase 7; 17-beta-hydroxysteroid
                     dehydrogenase 7; hydroxysteroid dehydrogenase 17 beta,
                     type 7; dihydrotestosterone oxidoreductase"
                     /calculated_mol_wt=37241
     Region          2..280
                     /region_name="3KS_SDR_c"
                     /note="3-keto steroid reductase, classical (c) SDRs;
                     cd08941"
                     /db_xref="CDD:187645"
     Site            order(9,11..14,35..37,50..52,90..92,141,169..171,193,197,
                     223..226,228..229)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187645"
     Site            37
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62904.1)"
     Site            order(142,171,193,197)
                     /site_type="active"
                     /db_xref="CDD:187645"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62904.1)"
     Site            229
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q62904.1)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62904.1)"
     CDS             1..334
                     /gene="Hsd17b7"
                     /coded_by="NM_017235.3:70..1074"
                     /db_xref="GeneID:29540"
                     /db_xref="RGD:2837"
ORIGIN      
        1 mrkvvlitga ssgiglalcg rllaedddlh lclacrnlsk agavrdalla shpsaevsiv
       61 qmdvsnlqsv vrgaeevkrr fqrldylyln agimpnpqln lkaffcgifs rnvihmfsta
      121 eglltqndki tadgfqevfe tnlfghfili relepllchs dnpsqliwts srnakksnfs
      181 lediqhakgq epyssskyat dllnvalnrn fnqkglyssv tcpgvvmtnl tygilppfvw
      241 tlllpviwll rffahaftvt pyngaealvw lfhqkpesln pltkylsgtt glgtnyvkgq
      301 kmdvdedtae kfyktllele kqvritiqks dhhs
//
LOCUS       NP_001102732             402 aa            linear   ROD 28-APR-2025
DEFINITION  ciliary microtubule-associated protein 2 [Rattus norvegicus].
ACCESSION   NP_001102732 XP_001065325 XP_575877
VERSION     NP_001102732.1
DBSOURCE    REFSEQ: accession NM_001109262.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Bonaldo,M.F., Lennon,G. and Soares,M.B.
  TITLE     Normalization and subtraction: two approaches to facilitate gene
            discovery
  JOURNAL   Genome Res 6 (9), 791-806 (1996)
   PUBMED   8889548
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC160900.1, CN542282.1 and BQ209190.1.
            
            On or before Oct 4, 2007 this sequence version replaced
            XP_001065325.1, XP_575877.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC160900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..402
                     /product="ciliary microtubule-associated protein 2"
                     /note="uncharacterized protein C1orf177 homolog;
                     lymphocyte expansion molecule"
                     /calculated_mol_wt=45704
     CDS             1..402
                     /gene="Cimap2"
                     /gene_synonym="Lexm; RGD1559493"
                     /coded_by="NM_001109262.2:45..1253"
                     /db_xref="GeneID:500516"
                     /db_xref="RGD:1559493"
ORIGIN      
        1 mstirkwfkg apfgvqshrf dvsavhpnqk kfstfteapy srhhsvelsh igpgtynske
       61 tcfskkfleq klgagwaraq easrltqlph fhfqaikker eqqankrgpg synikdflte
      121 lqkkpqskrg llssgetrfr glignyypgp gnygekgnpy tqleknswnr shsdglmcrl
      181 sskppplshq gsglgpgtyt iksdietfve kstgtrgpyd ifsgersspv pyghysvqkk
      241 kpreltsfks fvdelnaphk kkqggfskyp rdpkhpteri ywttlsqcpk dvnvagpgsw
      301 lpheteqkhv nrppfllask rsglkacqml lgtwnpvgvg rylnttlmek idrrqryrsl
      361 fmsepkrylh dlnrdkllqe ritpftkgkc rptvdynsdp tp
//
LOCUS       NP_001034107             443 aa            linear   ROD 28-APR-2025
DEFINITION  F-box only protein 39 [Rattus norvegicus].
ACCESSION   NP_001034107 XP_001080142 XP_220647
VERSION     NP_001034107.1
DBSOURCE    REFSEQ: accession NM_001039018.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Gaudet,P., Livstone,M.S., Lewis,S.E. and Thomas,P.D.
  TITLE     Phylogenetic-based propagation of functional annotations within the
            Gene Ontology consortium
  JOURNAL   Brief Bioinform 12 (5), 449-462 (2011)
   PUBMED   21873635
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC100079.1.
            
            On or before Jun 26, 2006 this sequence version replaced
            XP_220647.4, XP_001080142.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132298, SAMD00132306
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..443
                     /product="F-box only protein 39"
                     /calculated_mol_wt=52373
     Region          16..59
                     /region_name="F-box_FBXO39"
                     /note="F-box domain found in F-box only protein 39
                     (FBXO39) and similar proteins; cd22108"
                     /db_xref="CDD:438880"
     Site            order(19,23,26..27,30..31,35,37..38,42..44,46)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438880"
     CDS             1..443
                     /gene="Fbxo39"
                     /coded_by="NM_001039018.1:74..1405"
                     /db_xref="GeneID:303287"
                     /db_xref="RGD:1311464"
ORIGIN      
        1 mdedsevtqp qdqscwatlp dvclrrvfww lgdrdrsraa lvcrkwnqim ysadlwryrt
       61 itfsgrpsrv hasefesalw yvkkfgryle hleikflnpy navltkkfqv tmrgllsclg
      121 ksnnrlrsls iqhleldrlv wrnsirgsli kslsfflkkm gkhldhlslk garltveqgc
      181 hilnslsymr nenvaselni edffshhlav ygssqfnkam atfhnltflt lnyncisdel
      241 letlsennag tlrtmnikch vhdphgqvvw gmswaklarq asnlkvnfff ervmkyerla
      301 rillqeipvr sislrscyfs dpdwsmrptl tdllptfrnt lqkltfefnn nhesldeqlh
      361 llilacrklf yfkiwafldv kfverilksq eegqcslrtl kvriytnrye tneedrtlre
      421 iyrkyrklid selnyfviay pmm
//
LOCUS       NP_001274043             104 aa            linear   ROD 28-APR-2025
DEFINITION  vascular endothelial growth factor A isoform 12 [Rattus
            norvegicus].
ACCESSION   NP_001274043
VERSION     NP_001274043.1
DBSOURCE    REFSEQ: accession NM_001287114.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Kadekawa,K., Nishijima,S., Noguchi,K., Matsumoto,S. and Sugaya,K.
  TITLE     Elucidation of the pathophysiology of interstitial cystitis/bladder
            pain syndrome via experimental autoimmune cystitis rat model
  JOURNAL   Am J Physiol Regul Integr Comp Physiol 327 (2), R250-R260 (2024)
   PUBMED   38842512
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Fu,W., Ye,Y. and Hu,F.
  TITLE     LncRNA XIST promotes neovascularization in diabetic retinopathy by
            regulating miR-101-3p/VEGFA
  JOURNAL   Arch Endocrinol Metab 68, e230097 (2024)
   PUBMED   38739522
  REMARK    GeneRIF: LncRNA XIST promotes neovascularization in diabetic
            retinopathy by regulating miR-101-3p/VEGFA.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Feng,C., Tian,Q., Tang,X., Yu,J., Li,H., Geng,C. and Xu,L.
  TITLE     microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate traumatic
            brain injury
  JOURNAL   Exp Neurol 375, 114721 (2024)
   PUBMED   38342180
  REMARK    GeneRIF: microRNA-9a-5p disrupts the ELAVL1/VEGF axis to alleviate
            traumatic brain injury.
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Li,Z., Xie,L., Zou,L., Xiao,S. and Tao,J.
  TITLE     Overexpression of RAD54L attenuates osteoarthritis by suppressing
            the HIF-1alpha/VEGF signaling pathway: Bioinformatics analysis and
            experimental validation
  JOURNAL   PLoS One 19 (4), e0298575 (2024)
   PUBMED   38593124
  REMARK    GeneRIF: Overexpression of RAD54L attenuates osteoarthritis by
            suppressing the HIF-1alpha/VEGF signaling pathway: Bioinformatics
            analysis and experimental validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Bastide,A., Karaa,Z., Bornes,S., Hieblot,C., Lacazette,E., Prats,H.
            and Touriol,C.
  TITLE     An upstream open reading frame within an IRES controls expression
            of a specific VEGF-A isoform
  JOURNAL   Nucleic Acids Res 36 (7), 2434-2445 (2008)
   PUBMED   18304943
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Meiron,M., Anunu,R., Scheinman,E.J., Hashmueli,S. and Levi,B.Z.
  TITLE     New isoforms of VEGF are translated from alternative initiation CUG
            codons located in its 5'UTR
  JOURNAL   Biochem Biophys Res Commun 282 (4), 1053-1060 (2001)
   PUBMED   11352659
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Terman,B.I., Dougher-Vermazen,M., Carrion,M.E., Dimitrov,D.,
            Armellino,D.C., Gospodarowicz,D. and Bohlen,P.
  TITLE     Identification of the KDR tyrosine kinase as a receptor for
            vascular endothelial cell growth factor
  JOURNAL   Biochem Biophys Res Commun 187 (3), 1579-1586 (1992)
   PUBMED   1417831
REFERENCE   9  (residues 1 to 104)
  AUTHORS   de Vries,C., Escobedo,J.A., Ueno,H., Houck,K., Ferrara,N. and
            Williams,L.T.
  TITLE     The fms-like tyrosine kinase, a receptor for vascular endothelial
            growth factor
  JOURNAL   Science 255 (5047), 989-991 (1992)
   PUBMED   1312256
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Breier,G., Albrecht,U., Sterrer,S. and Risau,W.
  TITLE     Expression of vascular endothelial growth factor during embryonic
            angiogenesis and endothelial cell differentiation
  JOURNAL   Development 114 (2), 521-532 (1992)
   PUBMED   1592003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CO565920.1, BC168708.1,
            AY378102.1, AF215726.1 and JAXUCZ010000009.1.
            
            Summary: This gene is a member of the PDGF/VEGF growth factor
            family. It encodes a heparin-binding protein, which exists as a
            disulfide-linked homodimer. This growth factor induces
            proliferation and migration of vascular endothelial cells, and is
            essential for both physiological and pathological angiogenesis.
            Disruption of this gene in mice resulted in abnormal embryonic
            blood vessel formation. This gene is upregulated in many known
            tumors and its expression is correlated with tumor stage and
            progression. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. There is also
            evidence for alternative translation initiation from upstream
            non-AUG (CUG) codons resulting in additional isoforms. A recent
            study showed that a C-terminally extended isoform is produced by
            use of an alternative in-frame translation termination codon via a
            stop codon readthrough mechanism, and that this isoform is
            antiangiogenic. Expression of some isoforms derived from the AUG
            start codon is regulated by a small upstream open reading frame,
            which is located within an internal ribosome entry site. [provided
            by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (8) lacks an internal exon in the
            5' region, which results in translation initiation at a downstream
            AUG site, and two consecutive in-frame exons in the 3' coding
            region, compared to variant 1. The resulting isoform (12) is
            shorter at the N-terminus and lacks an internal segment, compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY033503.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN06680413, SAMN09345330
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q12"
     Protein         1..104
                     /product="vascular endothelial growth factor A isoform 12"
                     /note="vascular permeability factor"
                     /calculated_mol_wt=12143
     Region          7..89
                     /region_name="PDGF"
                     /note="Platelet-derived and vascular endothelial growth
                     factors (PDGF, VEGF) family; smart00141"
                     /db_xref="CDD:197537"
     Site            order(7..10,44,46..49,64..67)
                     /site_type="active"
                     /note="receptor binding interface [active]"
                     /db_xref="CDD:238079"
     Site            order(9,40,44,51,85,87)
                     /site_type="other"
                     /note="cysteine knot motif"
                     /db_xref="CDD:238079"
     Site            order(34,43)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238079"
     CDS             1..104
                     /gene="Vegfa"
                     /gene_synonym="Vegf; VEGF-A; VEGF111; VEGF164; VPF"
                     /coded_by="NM_001287114.1:1092..1406"
                     /note="isoform 12 is encoded by transcript variant 8"
                     /db_xref="GeneID:83785"
                     /db_xref="RGD:619991"
ORIGIN      
        1 mdvyqrsycr pietlvdifq eypdeieyif kpscvplmrc agccndeale cvptsesnvt
       61 mqimrikphq sqhigemsfl qhsrcecrpk kdrtkpekcd kprr
//
LOCUS       NP_001099263             711 aa            linear   ROD 28-APR-2025
DEFINITION  hydroperoxide isomerase ALOXE3 [Rattus norvegicus].
ACCESSION   NP_001099263 XP_001078483 XP_213336
VERSION     NP_001099263.1
DBSOURCE    REFSEQ: accession NM_001105793.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Gregus,A.M., Dumlao,D.S., Wei,S.C., Norris,P.C., Catella,L.C.,
            Meyerstein,F.G., Buczynski,M.W., Steinauer,J.J., Fitzsimmons,B.L.,
            Yaksh,T.L. and Dennis,E.A.
  TITLE     Systematic analysis of rat 12/15-lipoxygenase enzymes reveals
            critical role for spinal eLOX3 hepoxilin synthase activity in
            inflammatory hyperalgesia
  JOURNAL   FASEB J 27 (5), 1939-1949 (2013)
   PUBMED   23382512
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Krieg,P., Rosenberger,S., de Juanes,S., Latzko,S., Hou,J., Dick,A.,
            Kloz,U., van der Hoeven,F., Hausser,I., Esposito,I., Rauh,M. and
            Schneider,H.
  TITLE     Aloxe3 knockout mice reveal a function of epidermal lipoxygenase-3
            as hepoxilin synthase and its pivotal role in barrier formation
  JOURNAL   J Invest Dermatol 133 (1), 172-180 (2013)
   PUBMED   22832496
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Yan,L., Zhai,Q., Wei,J., Li,S., Wang,B., Huang,T., Du,M., Sun,J.,
            Kang,L., Li,C.B. and Li,C.
  TITLE     Role of tomato lipoxygenase D in wound-induced jasmonate
            biosynthesis and plant immunity to insect herbivores
  JOURNAL   PLoS Genet 9 (12), e1003964 (2013)
   PUBMED   24348260
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Zheng,Y., Yin,H., Boeglin,W.E., Elias,P.M., Crumrine,D., Beier,D.R.
            and Brash,A.R.
  TITLE     Lipoxygenases mediate the effect of essential fatty acid in skin
            barrier formation: a proposed role in releasing
            omega-hydroxyceramide for construction of the corneocyte lipid
            envelope
  JOURNAL   J Biol Chem 286 (27), 24046-24056 (2011)
   PUBMED   21558561
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Zheng,Y. and Brash,A.R.
  TITLE     On the role of molecular oxygen in lipoxygenase activation:
            comparison and contrast of epidermal lipoxygenase-3 with soybean
            lipoxygenase-1
  JOURNAL   J Biol Chem 285 (51), 39876-39887 (2010)
   PUBMED   20923767
REFERENCE   6  (residues 1 to 711)
  AUTHORS   Zheng,Y. and Brash,A.R.
  TITLE     Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical
            and atypical features of its catalytic activity with natural and
            synthetic polyunsaturated fatty acids
  JOURNAL   J Biol Chem 285 (51), 39866-39875 (2010)
   PUBMED   20921226
REFERENCE   7  (residues 1 to 711)
  AUTHORS   Hallenborg,P., Jorgensen,C., Petersen,R.K., Feddersen,S.,
            Araujo,P., Markt,P., Langer,T., Furstenberger,G., Krieg,P.,
            Koppen,A., Kalkhoven,E., Madsen,L. and Kristiansen,K.
  TITLE     Epidermis-type lipoxygenase 3 regulates adipocyte differentiation
            and peroxisome proliferator-activated receptor gamma activity
  JOURNAL   Mol Cell Biol 30 (16), 4077-4091 (2010)
   PUBMED   20530198
REFERENCE   8  (residues 1 to 711)
  AUTHORS   Yu,Z., Schneider,C., Boeglin,W.E. and Brash,A.R.
  TITLE     Human and mouse eLOX3 have distinct substrate specificities:
            implications for their linkage with lipoxygenases in skin
  JOURNAL   Arch Biochem Biophys 455 (2), 188-196 (2006)
   PUBMED   17045234
REFERENCE   9  (residues 1 to 711)
  AUTHORS   Yu,Z., Schneider,C., Boeglin,W.E., Marnett,L.J. and Brash,A.R.
  TITLE     The lipoxygenase gene ALOXE3 implicated in skin differentiation
            encodes a hydroperoxide isomerase
  JOURNAL   Proc Natl Acad Sci U S A 100 (16), 9162-9167 (2003)
   PUBMED   12881489
REFERENCE   10 (residues 1 to 711)
  AUTHORS   Jobard,F., Lefevre,C., Karaduman,A., Blanchet-Bardon,C., Emre,S.,
            Weissenbach,J., Ozguc,M., Lathrop,M., Prud'homme,J.F. and
            Fischer,J.
  TITLE     Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are
            mutated in non-bullous congenital ichthyosiform erythroderma (NCIE)
            linked to chromosome 17p13.1
  JOURNAL   Hum Mol Genet 11 (1), 107-113 (2002)
   PUBMED   11773004
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CH473948.1.
            
            On or before Oct 3, 2007 this sequence version replaced
            XP_213336.4, XP_001078483.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132268,
                              SAMD00132273 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..711
                     /product="hydroperoxide isomerase ALOXE3"
                     /EC_number="5.4.4.7"
                     /EC_number="4.2.1.152"
                     /note="epidermis-type lipoxygenase 3; epidermal LOX-3;
                     hydroperoxy icosatetraenoate dehydratase; hydroperoxy
                     dehydratase ALOXE3; hydroperoxy icosatetraenoate
                     isomerase; arachidonate lipoxygenase 3"
                     /calculated_mol_wt=80309
     Region          2..116
                     /region_name="PLAT_LOX"
                     /note="PLAT domain of 12/15-lipoxygenase. As a unique
                     subfamily of the mammalian lipoxygenases, they catalyze
                     enzymatic lipid peroxidation in complex biological
                     structures via direct dioxygenation of phospholipids and
                     cholesterol esters of biomembranes and...; cd01753"
                     /db_xref="CDD:238851"
     Region          <268..690
                     /region_name="Lipoxygenase"
                     /note="pfam00305"
                     /db_xref="CDD:459754"
     CDS             1..711
                     /gene="Aloxe3"
                     /gene_synonym="e-LOX-3; eLOX-3"
                     /coded_by="NM_001105793.1:27..2162"
                     /db_xref="GeneID:287424"
                     /db_xref="RGD:1306252"
ORIGIN      
        1 mavyrlcvtt gsylkagtld niyatlvgtc gespkqkldr vgrdfatgsv qkykvrcase
       61 lgeilllrlh kerfaffckd pwycsricvt tpdgsvvhfp cyqwidgyct velrpgtart
      121 icqdalplll dhrkrelqar qecyrwkiya pgfprmvdvs sfeemesdkk faltktapca
      181 dqddnsgnry lpgfpmkvdi psllhmepni rysatktasl ifnalpaslg mkirglldrk
      241 gswkrlddir nifwchktft seyvtehwce dsffgyqyln gvnpimlhcl sslpsklpvt
      301 ndmvapllgp gtclqteler ghifladywi laeapvhcln grqqyvtapl cllwlnpqgv
      361 llplaiqlsq ipgpespifl ptdceldwll aktwvrnsef lvhennthfl cthllceafs
      421 matlrqlplc hpvyklllph trytlqvnti aratllnpdg lvdkvtsigr rgliylmstg
      481 lahftytdfc lpdslrargv ltipnyhyrd dglkiwaaie rfvseivsyy ypndacvqqd
      541 selqawvgei faqaflgres sgfpsrlctp gelvkyltai ifncsaqhaa vnsgqhdfga
      601 wmpnapssmr qpppqtkgnt tmesyletlp evnttcsnll lfwlvsqepk dqrplgtypd
      661 ehfteeaprq siaafqkcla qiskdirarn eslalpyayl dppliensvs i
//
LOCUS       NP_446157               1862 aa            linear   ROD 28-APR-2025
DEFINITION  transient receptor potential cation channel subfamily M member 7
            [Rattus norvegicus].
ACCESSION   NP_446157 XP_001056331 XP_002726218
VERSION     NP_446157.2
DBSOURCE    REFSEQ: accession NM_053705.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1862)
  AUTHORS   Kim,I.Y., Park,C.S., Seo,K.J., Lee,J.Y. and Yune,T.Y.
  TITLE     TRPM7 Mediates Neuropathic Pain by Activating mTOR Signaling in
            Astrocytes after Spinal Cord Injury in Rats
  JOURNAL   Mol Neurobiol 61 (8), 5265-5281 (2024)
   PUBMED   38180616
  REMARK    GeneRIF: TRPM7 Mediates Neuropathic Pain by Activating mTOR
            Signaling in Astrocytes after Spinal Cord Injury in Rats.
REFERENCE   2  (residues 1 to 1862)
  AUTHORS   Lin,Y., Chen,Y., Hu,W., Liu,X., Hao,W., Xing,J., Ding,J., Xu,Y.,
            Yao,F., Zhao,Y., Wang,K., Li,S., Yu,Q., Hu,W. and Zhou,R.
  TITLE     TRPM7 facilitates fibroblast-like synoviocyte proliferation,
            metastasis and inflammation through increasing IL-6 stability via
            the PKCalpha-HuR axis in rheumatoid arthritis
  JOURNAL   Int Immunopharmacol 132, 111933 (2024)
   PUBMED   38581988
  REMARK    GeneRIF: TRPM7 facilitates fibroblast-like synoviocyte
            proliferation, metastasis and inflammation through increasing IL-6
            stability via the PKCalpha-HuR axis in rheumatoid arthritis.
REFERENCE   3  (residues 1 to 1862)
  AUTHORS   Park,C.S., Lee,J.Y., Seo,K.J., Kim,I.Y., Ju,B.G. and Yune,T.Y.
  TITLE     TRPM7 Mediates BSCB Disruption After Spinal Cord Injury by
            Regulating the mTOR/JMJD3 Axis in Rats
  JOURNAL   Mol Neurobiol 61 (2), 662-677 (2024)
   PUBMED   37653221
  REMARK    GeneRIF: TRPM7 Mediates BSCB Disruption After Spinal Cord Injury by
            Regulating the mTOR/JMJD3 Axis in Rats.
REFERENCE   4  (residues 1 to 1862)
  AUTHORS   Shin,M., Matsushima,A., Kajiya,H., Okamoto,F., Ogata,K., Oka,K.,
            Ohshima,H., Bartlett,J.D. and Okabe,K.
  TITLE     Conditional knockout of transient receptor potential melastatin 7
            in the enamel epithelium: Effects on enamel formation
  JOURNAL   Eur J Oral Sci 131 (2), e12920 (2023)
   PUBMED   36794562
  REMARK    GeneRIF: Conditional knockout of transient receptor potential
            melastatin 7 in the enamel epithelium: Effects on enamel formation.
REFERENCE   5  (residues 1 to 1862)
  AUTHORS   Jimenez-Dinamarca,I., Prado,Y., Tapia,P., Gatica,S., Alt,C.,
            Lin,C.P., Reyes-Martinez,C., Feijoo,C.G., Aravena,C.,
            Gonzalez-Canacer,A., Correa,S., Varela,D., Cabello-Verrugio,C. and
            Simon,F.
  TITLE     Disseminated intravascular coagulation phenotype is regulated by
            the TRPM7 channel during sepsis
  JOURNAL   Biol Res 56 (1), 8 (2023)
   PUBMED   36869357
  REMARK    GeneRIF: Disseminated intravascular coagulation phenotype is
            regulated by the TRPM7 channel during sepsis.
            Erratum:[Biol Res. 2023 May 11;56(1):24. doi:
            10.1186/s40659-023-00433-6. PMID: 37165417]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1862)
  AUTHORS   Hermosura,M.C., Nayakanti,H., Dorovkov,M.V., Calderon,F.R.,
            Ryazanov,A.G., Haymer,D.S. and Garruto,R.M.
  TITLE     A TRPM7 variant shows altered sensitivity to magnesium that may
            contribute to the pathogenesis of two Guamanian neurodegenerative
            disorders
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11510-11515 (2005)
   PUBMED   16051700
REFERENCE   7  (residues 1 to 1862)
  AUTHORS   He,Y., Yao,G., Savoia,C. and Touyz,R.M.
  TITLE     Transient receptor potential melastatin 7 ion channels regulate
            magnesium homeostasis in vascular smooth muscle cells: role of
            angiotensin II
  JOURNAL   Circ Res 96 (2), 207-215 (2005)
   PUBMED   15591230
  REMARK    GeneRIF: TRPM7 is a functionally important regulator of Mg2+
            homeostasis and growth in vascular smooth muscle cells.
REFERENCE   8  (residues 1 to 1862)
  AUTHORS   Jiang,X., Newell,E.W. and Schlichter,L.C.
  TITLE     Regulation of a TRPM7-like current in rat brain microglia
  JOURNAL   J Biol Chem 278 (44), 42867-42876 (2003)
   PUBMED   12904301
  REMARK    GeneRIF: TRPM7 currents were identified in the rat brain microglia
REFERENCE   9  (residues 1 to 1862)
  AUTHORS   Runnels,L.W., Yue,L. and Clapham,D.E.
  TITLE     The TRPM7 channel is inactivated by PIP(2) hydrolysis
  JOURNAL   Nat Cell Biol 4 (5), 329-336 (2002)
   PUBMED   11941371
  REMARK    GeneRIF: Data show that receptor-mediated activation of
            phospholipase C results in the hydrolysis of localized PIP(2),
            leading to inactivation of the TRPM7 channel.
REFERENCE   10 (residues 1 to 1862)
  AUTHORS   Runnels,L.W., Yue,L. and Clapham,D.E.
  TITLE     TRP-PLIK, a bifunctional protein with kinase and ion channel
            activities
  JOURNAL   Science 291 (5506), 1043-1047 (2001)
   PUBMED   11161216
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Sep 7, 2012 this sequence version replaced
            XP_001056331.2, XP_002726218.1, NP_446157.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360176.660399.1,
                                           SRR26643295.15233.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1862
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..1862
                     /product="transient receptor potential cation channel
                     subfamily M member 7"
                     /EC_number="2.7.11.1"
                     /note="long transient receptor potential channel 7;
                     transient receptor potential-phospholipase C-interacting
                     kinase"
                     /calculated_mol_wt=212292
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          106..371
                     /region_name="LSDAT_euk"
                     /note="SLOG in TRPM; pfam18139"
                     /db_xref="CDD:465665"
     Region          544..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          <722..1172
                     /region_name="TRPV"
                     /note="Transient Receptor Potential channel, Vanilloid
                     subfamily (TRPV); cl40437"
                     /db_xref="CDD:454755"
     Site            851..876
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            883..904
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            924..943
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            957..980
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1000..1023
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1070..1098
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          1194..1249
                     /region_name="TRPM_tetra"
                     /note="tetramerization domain of TRPM; pfam16519"
                     /db_xref="CDD:465156"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1265
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          1380..1418
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1404
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1466
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          1485..1511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1534
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          1577..1815
                     /region_name="Alpha_kinase_ChaK1_TRMP7"
                     /note="Alpha-kinase domain of channel kinase 1, also
                     called transient receptor potential cation channel
                     subfamily M member 7; cd16971"
                     /db_xref="CDD:341221"
     Site            1580
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            order(1616..1621,1623,1643,1645,1700,1717..1720,1764,1766,
                     1774)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:341221"
     Site            1657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1682
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1827
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Region          1840..1862
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1848
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q923J1; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     Site            1857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96QT4; propagated from
                     UniProtKB/Swiss-Prot (Q925B3.3)"
     CDS             1..1862
                     /gene="Trpm7"
                     /gene_synonym="Chak; LTrpC-7; Ltrpc7; Trp-plik"
                     /coded_by="NM_053705.2:252..5840"
                     /db_xref="GeneID:679906"
                     /db_xref="RGD:620053"
ORIGIN      
        1 msqkswiest ltkrecvyii psskdphrcl pgcqicqqlv rcfcgrlvkq hacftaslat
       61 kysdvklgeh fnqaieewsv ekhteqsptd aygvinfqgg shsyrakyvr lsydtkpeii
      121 lqlllkewqm elpklvisvh ggmqkfelhp rikqllgkgl ikaavttgaw iltggvntgv
      181 akhvgdalke hasrssrkic tigiapwgvi enrndlvgrd vvapyqtlln plsklnvlnn
      241 lhshfilvdd gtvgkygaev rlrrelekti nqqriharig qgvpvvalif eggpnviltv
      301 leylqesppv pvvvcegtgr aadllayihk qteeggnlpd aaepdiisti kktfnfgqse
      361 avhlfqtmme cmkkkelitv fhigsedhqd idvailtall kgtnasafdq liltlawdrv
      421 diaknhvfvy gqqwlvgsle qamldalvmd rvsfvkllie ngvsmhkflt iprleelynt
      481 kqgptnpmlf hlirdvkqgn lppgykitli diglvieylm ggtyrctytr krfrliynsl
      541 ggnnrrsgrn assstpqlrk shetfgnrad kkekmrhnhf iktaqpyrpk mdasmeegkk
      601 krtkdeivdi ddpetkrfpy plnelliwac lmkrqvmarf lwqhgeesma kalvackiyr
      661 smayeakqsd lvddtseelk qysndfgqla velleqsfrq detmamkllt yelknwsnst
      721 clklavssrl rpfvahtctq mllsdmwmgr lnmrknswyk vilsilvppa ilmleyktka
      781 emshipqsqd ahqmtmedse nnfhniteei pmevfkevki ldssegknem eihikskklp
      841 itrkfyafyh apivkfwfnt laylgflmly tfvvlvqmeq lpsvqewivi ayiftyaiek
      901 irevfmseag kisqkikvwf sdyfnvsdti aiisffvgfg lrfgakwnyi naydnhvfva
      961 grliyclnii fwyvrlldfl avnqqagpyv mmigkmvanm fyivvimalv llsfgvprka
     1021 ilypheepsw slakdivfhp ywmifgevya yeidvcands alpticgpgt wltpflqavy
     1081 lfvqyiimvn lliaffnnvy lqvkaisniv wkyqryhfim ayhekpvlpp pliilshivs
     1141 lfccickrrk kdktsdgpkl flteedqkkl hdfeeqcvem yfdekddkfn sgseerirvt
     1201 ferveqmsiq ikevgdrvny ikrslqslds qighlqdlsa ltvdtlktlt aqkaseaskv
     1261 hneitrelsi skhlaqnlid dvpvrpmwkk psvvntlsss lpqgdresnn pflcnifmkd
     1321 ekdpqynlfg qdlpvipqrk efnipeagss cgalfpsavs ppelrqrrhg vemlkifnkn
     1381 qklgsspnss phmsspptkf svstpsqpsc kshlesttkd pepifykaae gdniefgafv
     1441 ghrdsmdlqr fketsnkire llsndtpent lkhvgaagyn echktptslh seqescsrra
     1501 stedspdvds raallpdwlr drptnremps eggtlnglas pfkpvldtny yysavernnl
     1561 mrlsqsipfv pvpprgepvt vyrleessps ilnnsmssws qlglcakief lskeemgggl
     1621 rravkvlctw sehdvlrsgh lyiiksflpe vintwssiyk edtvlhlclr eiqqqraaqk
     1681 ltfafnqmkp ksipysprfl evfllychsa gqwfaveecm tgefrkynnn ngdeiiptnt
     1741 leeimlafsh wtyeytrgel lvldlqgvge nltdpsvika eekrscdmvf gpanlgedai
     1801 knfrakhhcn sccrklklpd lkrndytpdk iifpqdessd lnlqagnstk eseatnsvrl
     1861 ml
//
LOCUS       NP_072119                339 aa            linear   ROD 28-APR-2025
DEFINITION  cathepsin B preproprotein [Rattus norvegicus].
ACCESSION   NP_072119 XP_346478
VERSION     NP_072119.2
DBSOURCE    REFSEQ: accession NM_022597.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Zhou,Y., Dong,W., Wang,L., Ren,S., Wei,W. and Wu,G.
  TITLE     Cystatin C Attenuates Perihematomal Secondary Brain Injury by
            Inhibiting the Cathepsin B/NLRP3 Signaling Pathway in a Rat Model
            of Intracerebral Hemorrhage
  JOURNAL   Mol Neurobiol 61 (11), 9646-9662 (2024)
   PUBMED   38676809
  REMARK    GeneRIF: Cystatin C Attenuates Perihematomal Secondary Brain Injury
            by Inhibiting the Cathepsin B/NLRP3 Signaling Pathway in a Rat
            Model of Intracerebral Hemorrhage.
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Hassan,D.M., El-Kamel,A.H., Allam,E.A., Bakr,B.A. and Ashour,A.A.
  TITLE     Chitosan-coated nanostructured lipid carriers for effective brain
            delivery of Tanshinone IIA in Parkinson's disease: interplay
            between nuclear factor-kappa beta and cathepsin B
  JOURNAL   Drug Deliv Transl Res 14 (2), 400-417 (2024)
   PUBMED   37598133
  REMARK    GeneRIF: Chitosan-coated nanostructured lipid carriers for
            effective brain delivery of Tanshinone IIA in Parkinson's disease:
            interplay between nuclear factor-kappa beta and cathepsin B.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Katsumata-Kato,O., Yokoyama,M. and Fujita-Yoshigaki,J.
  TITLE     The secretory ability of newly formed secretory granules is
            regulated by pro-cathepsin B and amylase in parotid glands
  JOURNAL   Biochem Biophys Res Commun 666, 45-51 (2023)
   PUBMED   37178504
  REMARK    GeneRIF: The secretory ability of newly formed secretory granules
            is regulated by pro-cathepsin B and amylase in parotid glands.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Liu,C., Cai,Z., Hu,T., Yao,Q. and Zhang,L.
  TITLE     Cathepsin B aggravated doxorubicin-induced myocardial injury via
            NF-kappaB signalling
  JOURNAL   Mol Med Rep 22 (6), 4848-4856 (2020)
   PUBMED   33173960
  REMARK    GeneRIF: Cathepsin B aggravated doxorubicininduced myocardial
            injury via NFkappaB signalling.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Boutte,A.M., Hook,V., Thangavelu,B., Sarkis,G.A., Abbatiello,B.N.,
            Hook,G., Jacobsen,J.S., Robertson,C.S., Gilsdorf,J., Yang,Z.,
            Wang,K.K.W. and Shear,D.A.
  TITLE     Penetrating Traumatic Brain Injury Triggers Dysregulation of
            Cathepsin B Protein Levels Independent of Cysteine Protease
            Activity in Brain and Cerebral Spinal Fluid
  JOURNAL   J Neurotrauma 37 (13), 1574-1586 (2020)
   PUBMED   31973644
  REMARK    GeneRIF: Penetrating Traumatic Brain Injury Triggers Dysregulation
            of Cathepsin B Protein Levels Independent of Cysteine Protease
            Activity in Brain and Cerebral Spinal Fluid.
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Rowan,A.D., Mason,P., Mach,L. and Mort,J.S.
  TITLE     Rat procathepsin B. Proteolytic processing to the mature form in
            vitro
  JOURNAL   J Biol Chem 267 (22), 15993-15999 (1992)
   PUBMED   1639824
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Cataldo,A.M., Paskevich,P.A., Kominami,E. and Nixon,R.A.
  TITLE     Lysosomal hydrolases of different classes are abnormally
            distributed in brains of patients with Alzheimer disease
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 10998-11002 (1991)
   PUBMED   1837142
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Mar 15;89(6):2509]
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Tagawa,K., Kunishita,T., Maruyama,K., Yoshikawa,K., Kominami,E.,
            Tsuchiya,T., Suzuki,K., Tabira,T., Sugita,H. and Ishiura,S.
  TITLE     Alzheimer's disease amyloid beta-clipping enzyme (APP secretase):
            identification, purification, and characterization of the enzyme
  JOURNAL   Biochem Biophys Res Commun 177 (1), 377-387 (1991)
   PUBMED   1645961
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Ishii,Y., Hashizume,Y., Watanabe,T., Waguri,S., Sato,N.,
            Yamamoto,M., Hasegawa,S., Kominami,E. and Uchiyama,Y.
  TITLE     Cysteine proteinases in bronchoalveolar epithelial cells and lavage
            fluid of rat lung
  JOURNAL   J Histochem Cytochem 39 (4), 461-468 (1991)
   PUBMED   2005374
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Cataldo,A.M., Thayer,C.Y., Bird,E.D., Wheelock,T.R. and Nixon,R.A.
  TITLE     Lysosomal proteinase antigens are prominently localized within
            senile plaques of Alzheimer's disease: evidence for a neuronal
            origin
  JOURNAL   Brain Res 513 (2), 181-192 (1990)
   PUBMED   2350688
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB697852.1 and BC072490.1.
            
            On Dec 1, 2005 this sequence version replaced NP_072119.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072490.1, X82396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15p12"
     Protein         1..339
                     /product="cathepsin B preproprotein"
                     /EC_number="3.4.22.1"
                     /note="RSG-2; cathepsin B1"
                     /calculated_mol_wt=35657
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1905
     Region          26..65
                     /region_name="Propeptide_C1"
                     /note="Peptidase family C1 propeptide; pfam08127"
                     /db_xref="CDD:462365"
     mat_peptide     80..333
                     /product="Cathepsin B. /id=PRO_0000026154"
                     /note="propagated from UniProtKB/Swiss-Prot (P00787.2)"
                     /calculated_mol_wt=27753
     Region          81..328
                     /region_name="Peptidase_C1A_CathepsinB"
                     /note="Cathepsin B group; composed of cathepsin B and
                     similar proteins, including tubulointerstitial nephritis
                     antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like
                     cysteine peptidase which is expressed in all tissues and
                     functions primarily as an...; cd02620"
                     /db_xref="CDD:239111"
     Site            order(102,108,278,298)
                     /site_type="active"
                     /db_xref="CDD:239111"
     Site            order(154..155,252,276,279,324)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239111"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:6574504; propagated from
                     UniProtKB/Swiss-Prot (P00787.2)"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10605; propagated from
                     UniProtKB/Swiss-Prot (P00787.2)"
     CDS             1..339
                     /gene="Ctsb"
                     /coded_by="NM_022597.2:133..1152"
                     /db_xref="GeneID:64529"
                     /db_xref="RGD:621509"
ORIGIN      
        1 mwwsliplsc llaltsahdk psfhplsddm inyinkqntt wqagrnfynv disylkklcg
       61 tvlggpklpe rvgfsedinl pesfdareqw sncptiaqir dqgscgscwa fgaveamsdr
      121 icihtngrvn vevsaedllt ccgiqcgdgc nggypsgawn fwtrkglvsg gvynshigcl
      181 pytippcehh vngsrppctg egdtpkcnkm ceagystsyk edkhygytsy svsdsekeim
      241 aeiykngpve gaftvfsdfl tyksgvykhe agdvmgghai rilgwgieng vpywlvansw
      301 nvdwgdngff kilrgenhcg ieseivagip rtqqywgrf
//
LOCUS       NP_434684                550 aa            linear   ROD 28-APR-2025
DEFINITION  fibrinogen alpha chain isoform 2 precursor [Rattus norvegicus].
ACCESSION   NP_434684
VERSION     NP_434684.1
DBSOURCE    REFSEQ: accession NM_052797.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Wang,J., Zhang,Y., Liu,Y.M., Yang,X.C., Chen,Y.Y., Wu,G.J.,
            He,X.H., Duan,L., Dong,Y. and Ma,R.F.
  TITLE     Uncovering the protective mechanism of Huoxue Anxin Recipe against
            coronary heart disease by network analysis and experimental
            validation
  JOURNAL   Biomed Pharmacother 121, 109655 (2020)
   PUBMED   31734577
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Xu,S., Zhao,J., Liu,J. and Gou,W.
  TITLE     Fibrinopeptide A Induces Expression of C-Reactive Protein via the
            ROS-ERK1/2/ P38-NF-kappaB Signal Pathway in Vascular Smooth Muscle
            Cells
  JOURNAL   Cell Physiol Biochem 47 (1), 266-278 (2018)
   PUBMED   29768263
  REMARK    GeneRIF: Fibrinopeptide A induces CRP expression in Vascular Smooth
            Muscle Cells via Reactive Oxygen Species-ERK1/2/p38-NF-kappaB
            signal pathway.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Huang,Z., Song,Y., Pang,Z., Li,M., Guliya,Y., Shen,Y., Qian,J. and
            Ge,J.
  TITLE     Fibrin-targeting delivery: a novel platform for cardiac
            regenerative medicine
  JOURNAL   J Cell Mol Med 20 (12), 2410-2413 (2016)
   PUBMED   27469290
  REMARK    GeneRIF: Studies suggest fibrin as a homing target molecule in
            regenerative medicine and the fibrin-targeting therapy may be a
            generalizable platform technology for tissue injury.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Longstaff,C. and Kolev,K.
  TITLE     Basic mechanisms and regulation of fibrinolysis
  JOURNAL   J Thromb Haemost 13 Suppl 1, S98-S105 (2015)
   PUBMED   26149056
  REMARK    Review article
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Bai,J., He,A., Huang,C., Yang,J., Zhang,W., Wang,J., Yang,Y.,
            Zhang,P., Zhang,Y. and Zhou,F.
  TITLE     Serum peptidome based biomarkers searching for monitoring minimal
            residual disease in adult acute lymphocytic leukemia
  JOURNAL   Proteome Sci 12 (1), 49 (2014)
   PUBMED   25317080
  REMARK    Erratum:[Proteome Sci. 2020 Oct 24;18:9. doi:
            10.1186/s12953-020-00166-4. PMID: 33110398]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Nicholson,N.S., Panzer-Knodle,S.G., Salyers,A.K., Taite,B.B.,
            King,L.W., Miyano,M., Gorczynski,R.J., Williams,M.H., Zupec,M.E.,
            Tjoeng,F.S. et al.
  TITLE     Antiplatelet and antithrombotic effects of platelet glycoprotein
            IIb/IIIa (GPIIb/IIIa) inhibition by arginine-glycine-aspartic
            acid-serine (RGDS) and arginine-glycine-aspartic acid (RGD) (O-me)Y
            (SC-46749)
  JOURNAL   J Pharmacol Exp Ther 256 (3), 876-882 (1991)
   PUBMED   2005585
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Evans,E., Courtois,G.M., Kilian,P.L., Fuller,G.M. and Crabtree,G.R.
  TITLE     Induction of fibrinogen and a subset of acute phase response genes
            involves a novel monokine which is mimicked by phorbol esters
  JOURNAL   J Biol Chem 262 (22), 10850-10854 (1987)
   PUBMED   2440878
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Sobczak,J., Lotti,A.M., Taroux,P. and Duguet,M.
  TITLE     Molecular cloning of mRNA sequences transiently induced during rat
            liver regeneration
  JOURNAL   Exp Cell Res 169 (1), 47-56 (1987)
   PUBMED   3817019
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Procyk,R., Devlin,T.M. and Ch'ih,J.J.
  TITLE     Cycloheximide as a probe of fibrinogen synthesis
  JOURNAL   Biochem J 178 (2), 501-504 (1979)
   PUBMED   444225
REFERENCE   10 (residues 1 to 550)
  AUTHORS   John,D.W. and Miller,L.L.
  TITLE     Effect of whole x-irradiation of rats on net synthesis of albumin,
            fibrinogen, alpha-1-acid glycoprotein, and alpha-2-globulin (acute
            phase globulin) by the isolated, perfused rat liver
  JOURNAL   J Biol Chem 243 (2), 268-273 (1968)
   PUBMED   4170424
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127465.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127465.1, EX491745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..550
                     /product="fibrinogen alpha chain isoform 2 precursor"
                     /note="fibrinogen, alpha polypeptide; fibrinogen, A alpha
                     polypeptide"
                     /calculated_mol_wt=58446
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2078
     Site            36..37
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin, to release fibrinopeptide A;
                     propagated from UniProtKB/Swiss-Prot (P06399.3)"
     Region          50..189
                     /region_name="Fib_alpha"
                     /note="Fibrinogen alpha/beta chain family; pfam08702"
                     /db_xref="CDD:462570"
     Site            101..102
                     /site_type="cleavage"
                     /note="Cleavage, by plasmin, to break down fibrin clots.
                     /evidence=ECO:0000250|UniProtKB:P02671; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Site            122..123
                     /site_type="cleavage"
                     /note="Cleavage, by hementin, to prevent blood
                     coagulation. /evidence=ECO:0000250|UniProtKB:P02671;
                     propagated from UniProtKB/Swiss-Prot (P06399.3)"
     Site            124..125
                     /site_type="cleavage"
                     /note="Cleavage, by plasmin, to break down fibrin clots.
                     /evidence=ECO:0000250|UniProtKB:P02671; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Region          264..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06399.3)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Region          388..453
                     /region_name="Fibrinogen_aC"
                     /note="Fibrinogen alpha C domain; pfam12160"
                     /db_xref="CDD:432370"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Site            499
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline, by P4HA1.
                     /evidence=ECO:0000250|UniProtKB:P02671; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     Region          522..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06399.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P06399.3)"
     CDS             1..550
                     /gene="Fga"
                     /gene_synonym="Ac1873; Fba5e"
                     /coded_by="NM_052797.1:41..1693"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:361969"
                     /db_xref="RGD:2603"
ORIGIN      
        1 mlslrvacli lslastvwta dtgttsefie aggdirgpri verqpsqcke tdwpfcsded
       61 wnhkcpsgcr mkglideanq dftnrinklk nslfdfqknn kdsnsltrni meylrgdfan
      121 annfdntfgq vsedlrrrie ilkrkvieka qqiqvlqkdv rdqlidmkrl evdidikirs
      181 ckgscsrsvs reinlkdyeg qqkqleqvia kellpakdrq ylpaikmspv pdlvpgsfks
      241 qlqegppewk altemrqmrm elerpgkdga srgdlpgdsr gdsatrgpgs kienpmtpgh
      301 ggsgywrpgs sgsgsdgnwg sgttgsddtg twgagssrps sgsgnlkpsn pdwgefsefg
      361 gssspatrke yhtgklvtsk gdkelligne kvtstgtstt rrscsktitk tvlgndghre
      421 vvkevvtsdd gsdcgdgmdl glthsfsgrl delsrmhpel gsfydsrfgs ltsnfkefgs
      481 ktsdsdiftd ienpsshvpe fssssktstv rkqvtksykm adeaaseahq egdtrttkrg
      541 rartmrgiha
//
LOCUS       NP_445778                591 aa            linear   ROD 28-APR-2025
DEFINITION  PDZ and LIM domain protein 5 [Rattus norvegicus].
ACCESSION   NP_445778 XP_346645
VERSION     NP_445778.1
DBSOURCE    REFSEQ: accession NM_053326.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Ito,J., Iijima,M., Yoshimoto,N., Niimi,T., Kuroda,S. and
            Maturana,A.D.
  TITLE     RBM20 and RBM24 cooperatively promote the expression of short enh
            splice variants
  JOURNAL   FEBS Lett 590 (14), 2262-2274 (2016)
   PUBMED   27289039
  REMARK    GeneRIF: results suggest that, in healthy conditions, RBM20 and
            RBM24 cooperate to promote the expression of short ENH isoforms.
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Ito,J., Iijima,M., Yoshimoto,N., Niimi,T., Kuroda,S. and
            Maturana,A.D.
  TITLE     Scaffold protein enigma homolog activates CREB whereas a short
            splice variant prevents CREB activation in cardiomyocytes
  JOURNAL   Cell Signal 27 (12), 2425-2433 (2015)
   PUBMED   26365342
  REMARK    GeneRIF: ENH1 plays an essential role in CREB's activation and
            dependent transcription in cardiomyocytes.
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Ren,B., Li,X., Zhang,J., Fan,J., Duan,J. and Chen,Y.
  TITLE     PDLIM5 mediates PKCepsilon translocation in PMA-induced growth cone
            collapse
  JOURNAL   Cell Signal 27 (3), 424-435 (2015)
   PUBMED   25524223
  REMARK    GeneRIF: PDLIM5 acts as a scaffold protein by mediated PKCepsilon
            translocated to the membrane in PMA-induced growth cone collapse.
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Bang,C., Batkai,S., Dangwal,S., Gupta,S.K., Foinquinos,A.,
            Holzmann,A., Just,A., Remke,J., Zimmer,K., Zeug,A., Ponimaskin,E.,
            Schmiedl,A., Yin,X., Mayr,M., Halder,R., Fischer,A., Engelhardt,S.,
            Wei,Y., Schober,A., Fiedler,J. and Thum,T.
  TITLE     Cardiac fibroblast-derived microRNA passenger strand-enriched
            exosomes mediate cardiomyocyte hypertrophy
  JOURNAL   J Clin Invest 124 (5), 2136-2146 (2014)
   PUBMED   24743145
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Lasorella,A. and Iavarone,A.
  TITLE     The protein ENH is a cytoplasmic sequestration factor for Id2 in
            normal and tumor cells from the nervous system
  JOURNAL   Proc Natl Acad Sci U S A 103 (13), 4976-4981 (2006)
   PUBMED   16549780
  REMARK    GeneRIF: ENH is a restraining factor of the oncogenic activity of
            inhibitor of DNA binding 2 proteins in neural tumors
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Moser,K. and White,F.M.
  TITLE     Phosphoproteomic analysis of rat liver by high capacity IMAC and
            LC-MS/MS
  JOURNAL   J Proteome Res 5 (1), 98-104 (2006)
   PUBMED   16396499
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Maeno-Hikichi,Y., Chang,S., Matsumura,K., Lai,M., Lin,H.,
            Nakagawa,N., Kuroda,S. and Zhang,J.F.
  TITLE     A PKC epsilon-ENH-channel complex specifically modulates N-type
            Ca2+ channels
  JOURNAL   Nat Neurosci 6 (5), 468-475 (2003)
   PUBMED   12665800
  REMARK    GeneRIF: ENH protein, by interacting specifically with both protein
            kinase C (PKC)epsilon and the N-type Ca2+ channel, targets a
            specific PKC to its substrate to form a functional signaling
            complex.
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Nakagawa,N., Hoshijima,M., Oyasu,M., Saito,N., Tanizawa,K. and
            Kuroda,S.
  TITLE     ENH, containing PDZ and LIM domains, heart/skeletal muscle-specific
            protein, associates with cytoskeletal proteins through the PDZ
            domain
  JOURNAL   Biochem Biophys Res Commun 272 (2), 505-512 (2000)
   PUBMED   10833443
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Kuroda,S., Tokunaga,C., Kiyohara,Y., Higuchi,O., Konishi,H.,
            Mizuno,K., Gill,G.N. and Kikkawa,U.
  TITLE     Protein-protein interaction of zinc finger LIM domains with protein
            kinase C
  JOURNAL   J Biol Chem 271 (49), 31029-31032 (1996)
   PUBMED   8940095
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U48247.1.
            
            On Dec 17, 2003 this sequence version replaced XP_346645.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U48247.1, SRR8487231.98255.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q44"
     Protein         1..591
                     /product="PDZ and LIM domain protein 5"
                     /note="enigma-like PDZ and LIM domains protein; enigma
                     homolog"
                     /calculated_mol_wt=63071
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          5..83
                     /region_name="PDZ_PDLIM-like"
                     /note="PDZ domain of PDZ-LIM family proteins, and related
                     domains; cd06753"
                     /db_xref="CDD:467235"
     Site            order(13..19,31,34,63,67,70..71)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467235"
     Region          <36..>142
                     /region_name="PLN00049"
                     /note="carboxyl-terminal processing protease; Provisional"
                     /db_xref="CDD:177681"
     Region          84..>414
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            89
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8CI51; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          125..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62920.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          214..305
                     /region_name="DUF4749"
                     /note="Domain of unknown function (DUF4749); pfam15936"
                     /db_xref="CDD:464948"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          255..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62920.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            346
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CI51; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          348..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62920.2)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96HC4; propagated from
                     UniProtKB/Swiss-Prot (Q62920.2)"
     Region          415..466
                     /region_name="LIM1_ENH"
                     /note="The first LIM domain of the Enigma Homolog (ENH)
                     family; cd09453"
                     /db_xref="CDD:188837"
     Site            order(415,418,435,438,441,444,462,465)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188837"
     Region          474..525
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cl02475"
                     /db_xref="CDD:413332"
     Site            order(474,477,494,497,500,503,521,524)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     Region          533..587
                     /region_name="LIM"
                     /note="LIM is a small protein-protein interaction domain,
                     containing two zinc fingers; cl02475"
                     /db_xref="CDD:413332"
     Site            order(533,536,555,558,561,564,582,585)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259829"
     CDS             1..591
                     /gene="Pdlim5"
                     /gene_synonym="Enh; Enh1"
                     /coded_by="NM_053326.1:59..1834"
                     /db_xref="GeneID:64353"
                     /db_xref="RGD:621076"
ORIGIN      
        1 msnynvslvg papwgfrlqg gkdfnmplti sslkdggkas qahvrigdvv lsidgisaqg
       61 mthleaqnki kactgslnmt lqrasaaaks epvavqkgep kevvkpvpit spavskvtst
      121 tnmaynkvpr pfgsvsspkv tsipspssaf tpahaatssh aspppvaavt ppplsasglh
      181 asanpsaaqc ssppntgkpa vhvprqptvt svcsesaqel aegqrrgsqg dikqqngppr
      241 khiverntef yhipthsdas kkrliedted wrprtgttqs rsfrilaqit gtehlkesen
      301 dnakkanstp epsqqsaspl saaeslespg snrpvvaglr saaafkpvgs tsvkspswqr
      361 pnqaapstgr isnsasssgt gapmkpavgp pqpsdqdtlv qraehipagk rtpmcahcnq
      421 airgpflval gkswhpeefn cahckntmay igfveekgal ycelcyekff apecgrcqrk
      481 ilgevinalk qtwhvscfvc vacgkpirnn vfhledgepy cetdyyalfg ticrgcefpi
      541 eagdmfleal gstwhdtcfv csvccesleg qtffskkdkp lckkhahsvn f
//
LOCUS       NP_112622                536 aa            linear   ROD 28-APR-2025
DEFINITION  organic anion transporter 3 [Rattus norvegicus].
ACCESSION   NP_112622
VERSION     NP_112622.1
DBSOURCE    REFSEQ: accession NM_031332.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Taniguchi,T., Omura,K., Motoki,K., Sakai,M., Chikamatsu,N.,
            Ashizawa,N., Takada,T. and Iwanaga,T.
  TITLE     Hypouricemic agents reduce indoxyl sulfate excretion by inhibiting
            the renal transporters OAT1/3 and ABCG2
  JOURNAL   Sci Rep 11 (1), 7232 (2021)
   PUBMED   33790363
  REMARK    GeneRIF: Hypouricemic agents reduce indoxyl sulfate excretion by
            inhibiting the renal transporters OAT1/3 and ABCG2.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Pengrattanachot,N., Cherngwelling,R., Jaikumkao,K.,
            Pongchaidecha,A., Thongnak,L., Swe,M.T., Chatsudthipong,V. and
            Lungkaphin,A.
  TITLE     Atorvastatin attenuates obese-induced kidney injury and impaired
            renal organic anion transporter 3 function through inhibition of
            oxidative stress and inflammation
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (6), 165741 (2020)
   PUBMED   32101757
  REMARK    GeneRIF: Atorvastatin attenuates obese-induced kidney injury and
            impaired renal organic anion transporter 3 function through
            inhibition of oxidative stress and inflammation.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Bush,K.T., Singh,P. and Nigam,S.K.
  TITLE     Gut-derived uremic toxin handling in vivo requires OAT-mediated
            tubular secretion in chronic kidney disease
  JOURNAL   JCI Insight 5 (7), 133817 (2020)
   PUBMED   32271169
  REMARK    GeneRIF: Gut-derived uremic toxin handling in vivo requires
            OAT-mediated tubular secretion in chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Wanchai,K., Yasom,S., Tunapong,W., Chunchai,T.,
            Eaimworawuthikul,S., Thiennimitr,P., Chaiyasut,C.,
            Pongchaidecha,A., Chatsudthipong,V., Chattipakorn,S.,
            Chattipakorn,N. and Lungkaphin,A.
  TITLE     Probiotic Lactobacillus paracasei HII01 protects rats against
            obese-insulin resistance-induced kidney injury and impaired renal
            organic anion transporter 3 function
  JOURNAL   Clin Sci (Lond) 132 (14), 1545-1563 (2018)
   PUBMED   29980603
  REMARK    GeneRIF: Data suggest that a remote sensing and signaling system
            between gut and kidney by which probiotic might facilitate renal
            handling of gut microbiota products through the improvement of
            organic anion transporter 3 (Oat3) function.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Zhang,Z., Tachikawa,M., Uchida,Y. and Terasaki,T.
  TITLE     Drug Clearance from Cerebrospinal Fluid Mediated by Organic Anion
            Transporters 1 (Slc22a6) and 3 (Slc22a8) at Arachnoid Membrane of
            Rats
  JOURNAL   Mol Pharm 15 (3), 911-922 (2018)
   PUBMED   29436232
  REMARK    GeneRIF: Study results indicate that Oat1 and Oat3 at the
            blood-arachnoid barrier provide a distinct clearance pathway of
            organic anion drugs from cerebrospinal fluid independently of
            choroid plexus.
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Feng,B., Shu,Y. and Giacomini,K.M.
  TITLE     Role of aromatic transmembrane residues of the organic anion
            transporter, rOAT3, in substrate recognition
  JOURNAL   Biochemistry 41 (28), 8941-8947 (2002)
   PUBMED   12102636
  REMARK    GeneRIF: Role of aromatic transmembrane residues in substrate
            recognition
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Nagata,Y., Kusuhara,H., Endou,H. and Sugiyama,Y.
  TITLE     Expression and functional characterization of rat organic anion
            transporter 3 (rOat3) in the choroid plexus
  JOURNAL   Mol Pharmacol 61 (5), 982-988 (2002)
   PUBMED   11961115
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Hasegawa,M., Kusuhara,H., Sugiyama,D., Ito,K., Ueda,S., Endou,H.
            and Sugiyama,Y.
  TITLE     Functional involvement of rat organic anion transporter 3 (rOat3;
            Slc22a8) in the renal uptake of organic anions
  JOURNAL   J Pharmacol Exp Ther 300 (3), 746-753 (2002)
   PUBMED   11861777
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Kobayashi,Y., Hirokawa,N., Ohshiro,N., Sekine,T., Sasaki,T.,
            Tokuyama,S., Endou,H. and Yamamoto,T.
  TITLE     Differential gene expression of organic anion transporters in male
            and female rats
  JOURNAL   Biochem Biophys Res Commun 290 (1), 482-487 (2002)
   PUBMED   11779196
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Kusuhara,H., Sekine,T., Utsunomiya-Tate,N., Tsuda,M., Kojima,R.,
            Cha,S.H., Sugiyama,Y., Kanai,Y. and Endou,H.
  TITLE     Molecular cloning and characterization of a new multispecific
            organic anion transporter from rat brain
  JOURNAL   J Biol Chem 274 (19), 13675-13680 (1999)
   PUBMED   10224140
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB017446.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB017446.1, FQ209755.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5756307, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..536
                     /product="organic anion transporter 3"
                     /note="rOat3; solute carrier family 22 (organic anion
                     transporter), member 8; organic anion/dicarboxylate
                     exchanger"
                     /calculated_mol_wt=59056
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Region          11..503
                     /region_name="2A0119"
                     /note="cation transport protein; TIGR00898"
                     /db_xref="CDD:273328"
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            328..348
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            412..432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Site            472..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     Region          515..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R1U7.1)"
     CDS             1..536
                     /gene="Slc22a8"
                     /gene_synonym="Oat3; OCT3; Roct"
                     /coded_by="NM_031332.1:124..1734"
                     /db_xref="GeneID:83500"
                     /db_xref="RGD:632286"
ORIGIN      
        1 mtfseildrv gsmgpfqylh vtllalpvlg ianhnllqif tattpvhhcr pppnasigpw
       61 vlpldpngkp ekclrfvhlp naslpndtqr atepcldgwi ynstrdtivi ewdlvcssnk
      121 lkemaqsifm agilvggpvi gelsdrfgrk piltwsylml aasgsgaafs pslpvymifr
      181 flcgcsisgi slstvilnve wvptsmrais stsigycyti gqfilsglay aipqwrwlql
      241 tssapffifs llswwvpesi rwlvlsgkys kalktlqrva tfngkkeegk kltieelkfn
      301 lqkditsakv kyglsdlfrv silrrvtfcl slawfstgfa yyslamgvee fgvniyilqi
      361 ifggvdipak fitilslsyl grritqsfll llaggailal ifvpsemqll rtalavfgkg
      421 clsgsfsclf lytselyptv lrqtgmgisn vwarvgsmia plvkitgelq pfipnvifgt
      481 tallggsaaf flletlnrpl petiediqnw hkqvqktkqe seaekasqii plktgg
//
LOCUS       NP_001005556             507 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial antiviral-signaling protein [Rattus norvegicus].
ACCESSION   NP_001005556 XP_230537
VERSION     NP_001005556.1
DBSOURCE    REFSEQ: accession NM_001005556.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Song,N., Qi,Q., Cao,R., Qin,B., Wang,B., Wang,Y., Zhao,L., Li,W.,
            Du,X., Liu,F., Yan,Y., Yi,W., Jiang,H., Li,T., Zhou,T., Li,H.Y.,
            Xia,Q., Zhang,X.M., Zhong,W., Li,A.L. and Duan,X.
  TITLE     MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity
            against Lethal RNA Viruses
  JOURNAL   Cell Rep 28 (9), 2386-2396 (2019)
   PUBMED   31461653
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Ding,S., Zhu,S., Ren,L., Feng,N., Song,Y., Ge,X., Li,B.,
            Flavell,R.A. and Greenberg,H.B.
  TITLE     Rotavirus VP3 targets MAVS for degradation to inhibit type III
            interferon expression in intestinal epithelial cells
  JOURNAL   Elife 7, e39494 (2018)
   PUBMED   30460894
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Da Costa,A., Garza,E., Graham,J.B., Swarts,J.L., Soerens,A.G.,
            Gale,M. and Lund,J.M.
  TITLE     Extrinsic MAVS signaling is critical for Treg maintenance of Foxp3
            expression following acute flavivirus infection
  JOURNAL   Sci Rep 7, 40720 (2017)
   PUBMED   28094802
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Kandasamy,M., Suryawanshi,A., Tundup,S., Perez,J.T., Schmolke,M.,
            Manicassamy,S. and Manicassamy,B.
  TITLE     RIG-I Signaling Is Critical for Efficient Polyfunctional T Cell
            Responses during Influenza Virus Infection
  JOURNAL   PLoS Pathog 12 (7), e1005754 (2016)
   PUBMED   27438481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Gupta,S., Termini,J.M., Issac,B., Guirado,E. and Stone,G.W.
  TITLE     Constitutively Active MAVS Inhibits HIV-1 Replication via Type I
            Interferon Secretion and Induction of HIV-1 Restriction Factors
  JOURNAL   PLoS One 11 (2), e0148929 (2016)
   PUBMED   26849062
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Wang,D., Fang,L., Li,T., Luo,R., Xie,L., Jiang,Y., Chen,H. and
            Xiao,S.
  TITLE     Molecular cloning and functional characterization of porcine
            IFN-beta promoter stimulator 1 (IPS-1)
  JOURNAL   Vet Immunol Immunopathol 125 (3-4), 344-353 (2008)
   PUBMED   18586328
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Hoffert,J.D., Pisitkun,T., Wang,G., Shen,R.F. and Knepper,M.A.
  TITLE     Quantitative phosphoproteomics of vasopressin-sensitive renal
            cells: regulation of aquaporin-2 phosphorylation at two sites
  JOURNAL   Proc Natl Acad Sci U S A 103 (18), 7159-7164 (2006)
   PUBMED   16641100
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Kawai,T., Takahashi,K., Sato,S., Coban,C., Kumar,H., Kato,H.,
            Ishii,K.J., Takeuchi,O. and Akira,S.
  TITLE     IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
            interferon induction
  JOURNAL   Nat Immunol 6 (10), 981-988 (2005)
   PUBMED   16127453
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Xu,L.G., Wang,Y.Y., Han,K.J., Li,L.Y., Zhai,Z. and Shu,H.B.
  TITLE     VISA is an adapter protein required for virus-triggered IFN-beta
            signaling
  JOURNAL   Mol Cell 19 (6), 727-740 (2005)
   PUBMED   16153868
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC081869.1.
            
            On Oct 8, 2004 this sequence version replaced XP_230537.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC081869.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..507
                     /product="mitochondrial antiviral-signaling protein"
                     /note="IPS-1; virus-induced-signaling adapter; interferon
                     beta promoter stimulator protein 1; virus-induced
                     signaling adaptor"
                     /calculated_mol_wt=53674
     Region          3..93
                     /region_name="CARD_IPS1"
                     /note="Caspase activation and recruitment domain (CARD)
                     found in IPS-1; cd08811"
                     /db_xref="CDD:260073"
     Region          10..77
                     /region_name="Required for interaction with NLRX1.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          <65..468
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          123..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          143..147
                     /region_name="Interaction with TRAF2.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          153..158
                     /region_name="Interaction with TRAF6.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCF0; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            234
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCF0; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          250..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          340..507
                     /region_name="Interaction with DHX33.
                     /evidence=ECO:0000250|UniProtKB:Q8VCF0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          350..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCF0; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            408..409
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          419..422
                     /region_name="pLxIS motif.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434; propagated from
                     UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          423..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Region          435..440
                     /region_name="Interaction with TRAF6.
                     /evidence=ECO:0000250|UniProtKB:Q7Z434"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     Site            483..500
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q66HG9.1)"
     CDS             1..507
                     /gene="Mavs"
                     /gene_synonym="Visa"
                     /coded_by="NM_001005556.1:290..1813"
                     /db_xref="GeneID:311430"
                     /db_xref="RGD:1359371"
ORIGIN      
        1 mtfaeektyk yirynhskfc cvdvleilpy lsclttsdqd rlrasykqlg nqgtlwelfn
       61 tlqrrpgwve vfiralrice lpglaeqvtr vyqsylppga slhsldplqs pripttvsep
      121 safaaghtip dsgfqdkpgy pkpvqdtqpp kspvenseep pqanfgaipr msgdslissp
      181 nppalspqps rehpeqepel ggpstanvds vpiatygpvs ptvsfqplpr iaprtnlspg
      241 vtvsalsakt tlsssstgsa fakgagdqak aatcvstkeg vptnsvttss vpsikpvpvn
      301 tmssklpist kstaatpstv ptniapsklp insvytgivp skvtasvaka sastmppern
      361 nkqaketlea patvvttgss ltrpdissrs lhsgpelskp gvlvsqvdne pfsacsmdla
      421 ispstslgse pnhgpeeney ssfriqvdks psvdllgspe platqqspee eepcassvsw
      481 akwlgatsal laaflavmly rsrhlaq
//
LOCUS       NP_001013449             139 aa            linear   ROD 28-APR-2025
DEFINITION  mitochondrial intermembrane space import and assembly protein 40
            [Rattus norvegicus].
ACCESSION   NP_001013449 XP_232200
VERSION     NP_001013449.1
DBSOURCE    REFSEQ: accession NM_001013431.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Wang,Y., Zeng,Z., Zeng,Z., Chu,G. and Shan,X.
  TITLE     Elevated CHCHD4 orchestrates mitochondrial oxidative
            phosphorylation to disturb hypoxic pulmonary hypertension
  JOURNAL   J Transl Med 21 (1), 464 (2023)
   PUBMED   37438854
  REMARK    GeneRIF: Elevated CHCHD4 orchestrates mitochondrial oxidative
            phosphorylation to disturb hypoxic pulmonary hypertension.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Petrungaro,C., Zimmermann,K.M., Kuttner,V., Fischer,M., Dengjel,J.,
            Bogeski,I. and Riemer,J.
  TITLE     The Ca(2+)-Dependent Release of the Mia40-Induced MICU1-MICU2 Dimer
            from MCU Regulates Mitochondrial Ca(2+) Uptake
  JOURNAL   Cell Metab 22 (4), 721-733 (2015)
   PUBMED   26387864
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Mordas,A. and Tokatlidis,K.
  TITLE     The MIA pathway: a key regulator of mitochondrial oxidative protein
            folding and biogenesis
  JOURNAL   Acc Chem Res 48 (8), 2191-2199 (2015)
   PUBMED   26214018
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Hangen,E., Feraud,O., Lachkar,S., Mou,H., Doti,N., Fimia,G.M.,
            Lam,N.V., Zhu,C., Godin,I., Muller,K., Chatzi,A., Nuebel,E.,
            Ciccosanti,F., Flamant,S., Benit,P., Perfettini,J.L., Sauvat,A.,
            Bennaceur-Griscelli,A., Ser-Le Roux,K., Gonin,P., Tokatlidis,K.,
            Rustin,P., Piacentini,M., Ruvo,M., Blomgren,K., Kroemer,G. and
            Modjtahedi,N.
  TITLE     Interaction between AIF and CHCHD4 Regulates Respiratory Chain
            Biogenesis
  JOURNAL   Mol Cell 58 (6), 1001-1014 (2015)
   PUBMED   26004228
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Zhuang,J., Wang,P.Y., Huang,X., Chen,X., Kang,J.G. and Hwang,P.M.
  TITLE     Mitochondrial disulfide relay mediates translocation of p53 and
            partitions its subcellular activity
  JOURNAL   Proc Natl Acad Sci U S A 110 (43), 17356-17361 (2013)
   PUBMED   24101517
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Fischer,M., Horn,S., Belkacemi,A., Kojer,K., Petrungaro,C.,
            Habich,M., Ali,M., Kuttner,V., Bien,M., Kauff,F., Dengjel,J.,
            Herrmann,J.M. and Riemer,J.
  TITLE     Protein import and oxidative folding in the mitochondrial
            intermembrane space of intact mammalian cells
  JOURNAL   Mol Biol Cell 24 (14), 2160-2170 (2013)
   PUBMED   23676665
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Banci,L., Bertini,I., Cefaro,C., Cenacchi,L., Ciofi-Baffoni,S.,
            Felli,I.C., Gallo,A., Gonnelli,L., Luchinat,E., Sideris,D. and
            Tokatlidis,K.
  TITLE     Molecular chaperone function of Mia40 triggers consecutive induced
            folding steps of the substrate in mitochondrial protein import
  JOURNAL   Proc Natl Acad Sci U S A 107 (47), 20190-20195 (2010)
   PUBMED   21059946
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Tarantino,C., Paolella,G., Cozzuto,L., Minopoli,G., Pastore,L.,
            Parisi,S. and Russo,T.
  TITLE     miRNA 34a, 100, and 137 modulate differentiation of mouse embryonic
            stem cells
  JOURNAL   FASEB J 24 (9), 3255-3263 (2010)
   PUBMED   20439489
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Banci,L., Bertini,I., Cefaro,C., Ciofi-Baffoni,S., Gallo,A.,
            Martinelli,M., Sideris,D.P., Katrakili,N. and Tokatlidis,K.
  TITLE     MIA40 is an oxidoreductase that catalyzes oxidative protein folding
            in mitochondria
  JOURNAL   Nat Struct Mol Biol 16 (2), 198-206 (2009)
   PUBMED   19182799
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Hofmann,S., Rothbauer,U., Muhlenbein,N., Baiker,K., Hell,K. and
            Bauer,M.F.
  TITLE     Functional and mutational characterization of human MIA40 acting
            during import into the mitochondrial intermembrane space
  JOURNAL   J Mol Biol 353 (3), 517-528 (2005)
   PUBMED   16185709
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC091407.1.
            
            On Apr 20, 2005 this sequence version replaced XP_232200.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091407.1, FQ229282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q34"
     Protein         1..139
                     /product="mitochondrial intermembrane space import and
                     assembly protein 40"
                     /note="coiled-coil-helix-coiled-coil-helix
                     domain-containing protein 4"
                     /calculated_mol_wt=15336
     Region          64..100
                     /region_name="CHCH"
                     /note="CHCH domain; pfam06747"
                     /db_xref="CDD:429096"
     Region          64..74
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJN5.1)"
     Region          87..97
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJN5.1)"
     Region          104..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5BJN5.1)"
     CDS             1..139
                     /gene="Chchd4"
                     /coded_by="NM_001013431.1:175..594"
                     /db_xref="GeneID:312559"
                     /db_xref="RGD:1310746"
ORIGIN      
        1 msycrqegkd riifvtkedh etpssaelva ddpndpyeeh glilpngdin wncpclggma
       61 sgpcgeqfks afscfhyste dikgsdcidq framqecmqk ypdlypqdee eeeeakpvep
      121 veetadtkas aakeqgass
//
LOCUS       NP_001017506             447 aa            linear   ROD 28-APR-2025
DEFINITION  protein chibby homolog 2 [Rattus norvegicus].
ACCESSION   NP_001017506 XP_573846
VERSION     NP_001017506.1
DBSOURCE    REFSEQ: accession NM_001017506.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Feige,E., Chen,A. and Motro,B.
  TITLE     Nurit, a novel leucine-zipper protein, expressed uniquely in the
            spermatid flower-like structure
  JOURNAL   Mech Dev 117 (1-2), 369-377 (2002)
   PUBMED   12204287
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079300.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573846.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079300.1, CV116182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q11"
     Protein         1..447
                     /product="protein chibby homolog 2"
                     /note="spermatid-associated protein; spermatid associated"
                     /calculated_mol_wt=51878
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Region          76..191
                     /region_name="Cby_like"
                     /note="Chibby, a nuclear inhibitor of Wnt/beta-catenin
                     mediated transcription, and similar proteins; cd07429"
                     /db_xref="CDD:143631"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Region          208..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Region          266..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV6.1)"
     Region          <362..>421
                     /region_name="MreC"
                     /note="rod shape-determining protein MreC; cl46468"
                     /db_xref="CDD:480808"
     CDS             1..447
                     /gene="Cby2"
                     /gene_synonym="Spert"
                     /coded_by="NM_001017506.1:55..1398"
                     /db_xref="GeneID:498572"
                     /db_xref="RGD:1561044"
ORIGIN      
        1 msplecsecf gdqlmhrtyt whltlhsrpn ftrkreirse sleipinvil pqrgtepflr
       61 lhnlyttprc srqaampris rrvasqhsyp lnrfssmpfd pmerptsqad leldynpprv
      121 qlsdemfvfq dgrwvnescr lqspyfspss sfhhklhhkr makeyllqee nkslrdenra
      181 lrdenkalrk enkilqvfwe ehkvtlghee sqtsspllhk dttsqevvkk dnatlpaqrs
      241 kentlqfire enralqqlle qrqaywaqae esatsaeegk ptsspkeeph nsgllpdqst
      301 shsshfeepk aspttqedsk tlralremvt nlsgpsgeee gkagpnltds aqplqllrem
      361 nqalqalree nrllqeenra lhamreehrv fqeenkalwe nnklklqqrl vidtvtevta
      421 rmemlieely afmpaknnkd pkkpsrv
//
LOCUS       NP_742062                295 aa            linear   ROD 28-APR-2025
DEFINITION  proline-rich proteoglycan 2 precursor [Rattus norvegicus].
ACCESSION   NP_742062
VERSION     NP_742062.1
DBSOURCE    REFSEQ: accession NM_172065.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Castle,A.M. and Castle,J.D.
  TITLE     Novel secretory proline-rich proteoglycans from rat parotid.
            Cloning and characterization by expression in AtT-20 cells
  JOURNAL   J Biol Chem 268 (27), 20490-20496 (1993)
   PUBMED   8376404
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Clements,S., Mehansho,H. and Carlson,D.M.
  TITLE     Novel multigene families encoding highly repetitive peptide
            sequences. Sequence analyses of rat and mouse proline-rich protein
            cDNAs
  JOURNAL   J Biol Chem 260 (25), 13471-13477 (1985)
   PUBMED   3840480
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L17318.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L17318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="4"
                     /map="4q42"
     Protein         1..295
                     /product="proline-rich proteoglycan 2 precursor"
                     /note="acidic proline-rich protein PRP18; proline-rich
                     proteoglycan 2; proline-rich protein BstNI subfamily 1"
                     /calculated_mol_wt=28430
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1614
     Region          16..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10165.2)"
     mat_peptide     17..295
                     /product="Proline-rich proteoglycan 2. /id=PRO_0000022132"
                     /note="propagated from UniProtKB/Swiss-Prot (P10165.2)"
                     /calculated_mol_wt=28430
     CDS             1..295
                     /gene="Prpmp5"
                     /gene_synonym="Prb1; Prpg2"
                     /coded_by="NM_172065.2:21..908"
                     /db_xref="GeneID:257651"
                     /db_xref="RGD:628797"
ORIGIN      
        1 mlvvlltaal lvlssaqgvd eevvyedssq qleleqqsqg hgqhhpkppp gglpprppas
       61 dengdgddnd dgdddgsgdd vnrperppqh ggnhhhphhp ppaagpqrpp qpgspqgppp
      121 pggpqqrppq gpppqggpqr ppqpgspqgp pppggpqqrp pqgpppqggp qrppqpgspq
      181 gppppggpqq rapqgpppqg gpqrppqpgs pqgppppggp qqrppqgppp qggpqrppqp
      241 gspqgppppg gpqqrppqgp ppqggpqrpp qpgnpqgppq qggqqqssfl wsfsa
//
LOCUS       NP_001007691             742 aa            linear   ROD 28-APR-2025
DEFINITION  F-box only protein 30 [Rattus norvegicus].
ACCESSION   NP_001007691 XP_218085
VERSION     NP_001007691.1
DBSOURCE    REFSEQ: accession NM_001007690.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083823.1.
            
            On Nov 29, 2004 this sequence version replaced XP_218085.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083823.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132266, SAMD00132280
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..742
                     /product="F-box only protein 30"
                     /calculated_mol_wt=81881
     Region          8..99
                     /region_name="zf-TRAF_2"
                     /note="TRAF-like zinc-finger; pfam15965"
                     /db_xref="CDD:464957"
     Region          214..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI67.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5XI67.1)"
     Region          608..721
                     /region_name="F-box_4"
                     /note="pfam15966"
                     /db_xref="CDD:464958"
     CDS             1..742
                     /gene="Fbxo30"
                     /coded_by="NM_001007690.1:172..2400"
                     /db_xref="GeneID:308283"
                     /db_xref="RGD:1359367"
ORIGIN      
        1 meeevqqhsh cvncvsrrcm trpepgvscd ligcplvcga vfhsckadeh rllcpfervp
       61 clnsnfgcpf tlarnkvaeh lemcpasvvc ctmewnrwpv sysdrksyes lsrdadevsq
      121 ldmalalqdq rmlleslkva tmmskatgki skpreqisvn ssvqevpran glvsadeesy
      181 galyeatvet trslaaaldi lnsatrdigm lntslqgttn emdeesnres sqdrnakdqd
      241 hldegeigav ggidytgtsq naqaeqngss dllcnlntss ydtsalcngf plekmctqvk
      301 dqdqnfhgds tesnitngdc veadgtsepp ssllvaeqlk egsalpdsty qhilmpdedd
      361 dedlcwkkdl gdskdvngsp lshatsfkfl snswyipked kavdtsdlev aedpmglqgi
      421 dlitaallfc lgdspggrgi sdsrmvdvyh vdfgtqtfsl psailatntm vgeiasasac
      481 dhanpqlsnp spfqtlgldl vlecvaryqp kqrsmftfvc gqlfrrkefs shfknvhgdi
      541 haglngwmeq rcplayygct ysqrrfcpst qgakiihdrh lrsfgvqpcv staleepsrn
      601 cvlglrsdhl sslpfevlqh iagfldgfsl cqlacvsrlm rdicgsllqs rgmvilqwgk
      661 kkypegnssw qikekvwrfs tafcsvndwk fadilsmadh lkkcsynvie kreeaiplpc
      721 mcvtreltke grslrsvlkp vl
//
LOCUS       NP_001012142             423 aa            linear   ROD 28-APR-2025
DEFINITION  secernin-2 [Rattus norvegicus].
ACCESSION   NP_001012142 XP_340889
VERSION     NP_001012142.1
DBSOURCE    REFSEQ: accession NM_001012142.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC078939.1.
            
            On Feb 11, 2005 this sequence version replaced XP_340889.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..423
                     /product="secernin-2"
                     /calculated_mol_wt=46371
     Region          21..>231
                     /region_name="PepD"
                     /note="Dipeptidase [Amino acid transport and metabolism];
                     cl41909"
                     /db_xref="CDD:477862"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q96FV2; propagated from
                     UniProtKB/Swiss-Prot (Q6AYR8.1)"
     CDS             1..423
                     /gene="Scrn2"
                     /coded_by="NM_001012142.1:51..1322"
                     /db_xref="GeneID:360612"
                     /db_xref="RGD:1307741"
ORIGIN      
        1 massspdapc scdcfvsvpp asaipavifa knsdrprdev qevvfipagt htpgsrlqct
       61 yieveqvwkt havilsrpsw lwgaemgane lgvcigneav wtkepvgege allgmdllrl
      121 alersstaqa avhviaglld rygqggscre dpepfcyhnt flladrteaw vletagrlwa
      181 aqriqggarn isnqlsigtd isaehpelrs hakaqgwwsg qgvfdfaevf sltqqpvrme
      241 aakarfragc emlqrqqgsi taevmmdilr nkesgicmds ggfrttasmv svlpqdptkp
      301 cvhfltatpd psrsvfkpfi fevgvsqppq vlsptfgaqd pvrilprfqt qvdrrhslyr
      361 ghqaalglmd eqeqaqlrqe qqsleqegle alrglltgeq tpapqelgsl fqafverehq
      421 vya
//
LOCUS       NP_058786                690 aa            linear   ROD 28-APR-2025
DEFINITION  guanylate cyclase soluble subunit alpha-1 [Rattus norvegicus].
ACCESSION   NP_058786 XP_346629
VERSION     NP_058786.2
DBSOURCE    REFSEQ: accession NM_017090.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Galley,J.C., Miller,M.P., Sanker,S., Liu,M., Sharina,I., Martin,E.,
            Gomez,D. and Straub,A.C.
  TITLE     FoxO4 controls sGCbeta transcription in vascular smooth muscle
  JOURNAL   Am J Physiol Heart Circ Physiol 322 (3), H417-H426 (2022)
   PUBMED   35089807
  REMARK    GeneRIF: FoxO4 controls sGCbeta transcription in vascular smooth
            muscle.
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Dai,Y., Sweeny,E.A., Schlanger,S., Ghosh,A. and Stuehr,D.J.
  TITLE     GAPDH delivers heme to soluble guanylyl cyclase
  JOURNAL   J Biol Chem 295 (24), 8145-8154 (2020)
   PUBMED   32358060
  REMARK    GeneRIF: GAPDH delivers heme to soluble guanylyl cyclase.
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Du,L. and Roberts,J.D. Jr.
  TITLE     Transforming growth factor-beta downregulates sGC subunit
            expression in pulmonary artery smooth muscle cells via MEK and ERK
            signaling
  JOURNAL   Am J Physiol Lung Cell Mol Physiol 316 (1), L20-L34 (2019)
   PUBMED   30260287
  REMARK    GeneRIF: These studies identify MEK/ERK signaling as an important
            pathway by which TGFbeta regulates sGC expression in pulmonary
            artery smooth muscle cell.
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Wang,Q., Mergia,E., Koesling,D. and Mittmann,T.
  TITLE     Nitric oxide/cGMP signaling via guanylyl cyclase isoform 1
            modulates glutamate and GABA release in somatosensory cortex of
            mice
  JOURNAL   Neuroscience 360, 180-189 (2017)
   PUBMED   28782641
REFERENCE   5  (residues 1 to 690)
  AUTHORS   Sanguesa,G., Shaligram,S., Akther,F., Roglans,N., Laguna,J.C.,
            Rahimian,R. and Alegret,M.
  TITLE     Type of supplemented simple sugar, not merely calorie intake,
            determines adverse effects on metabolism and aortic function in
            female rats
  JOURNAL   Am J Physiol Heart Circ Physiol 312 (2), H289-H304 (2017)
   PUBMED   27923787
REFERENCE   6  (residues 1 to 690)
  AUTHORS   Baltrons,M.A., Pedraza,C.E., Heneka,M.T. and Garcia,A.
  TITLE     Beta-amyloid peptides decrease soluble guanylyl cyclase expression
            in astroglial cells
  JOURNAL   Neurobiol Dis 10 (2), 139-149 (2002)
   PUBMED   12127152
  REMARK    GeneRIF: treatment of rat brain astrocytes with betaA decreases
            their capacity to accumulate cyclic GMP (cGMP) in response to NO as
            a result of a decreased expression of soluble guanylyl cyclase
            alpha-1 and beta-1 subunits at the protein and mRNA levels.
REFERENCE   7  (residues 1 to 690)
  AUTHORS   Tao,Y.X. and Johns,R.A.
  TITLE     Activation and up-regulation of spinal cord nitric oxide receptor,
            soluble guanylate cyclase, after formalin injection into the rat
            hind paw
  JOURNAL   Neuroscience 112 (2), 439-446 (2002)
   PUBMED   12044461
  REMARK    GeneRIF: peripheral inflammation activates and later up-regulates
            soluble guanylate cyclase expression in the spinal cord
REFERENCE   8  (residues 1 to 690)
  AUTHORS   Azam,M., Gupta,G., Chen,W., Wellington,S., Warburton,D. and
            Danziger,R.S.
  TITLE     Genetic mapping of soluble guanylyl cyclase genes: implications for
            linkage to blood pressure in the Dahl rat
  JOURNAL   Hypertension 32 (1), 149-154 (1998)
   PUBMED   9674652
REFERENCE   9  (residues 1 to 690)
  AUTHORS   Smigrodzki,R. and Levitt,P.
  TITLE     The alpha 1 subunit of soluble guanylyl cyclase is expressed
            prenatally in the rat brain
  JOURNAL   Brain Res Dev Brain Res 97 (2), 226-234 (1996)
   PUBMED   8997507
REFERENCE   10 (residues 1 to 690)
  AUTHORS   Nakane,M., Arai,K., Saheki,S., Kuno,T., Buechler,W. and Murad,F.
  TITLE     Molecular cloning and expression of cDNAs coding for soluble
            guanylate cyclase from rat lung
  JOURNAL   J Biol Chem 265 (28), 16841-16845 (1990)
   PUBMED   1698769
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085746.1.
            
            On Jun 10, 2007 this sequence version replaced NP_058786.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085746.1, U60835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMN16676788
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..690
                     /product="guanylate cyclase soluble subunit alpha-1"
                     /EC_number="4.6.1.2"
                     /note="guanylate cyclase soluble subunit alpha-3;
                     guanylate cyclase 1 soluble subunit alpha 3; Guanylate
                     cyclase, soluble, alpha 1 (GTP pyrophosphate - lyase);
                     GCS-alpha-1; GCS-alpha-3; guanylate cyclase 1, soluble,
                     alpha 3; soluble guanylate cyclase large subunit"
                     /calculated_mol_wt=77408
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ERL9; propagated from
                     UniProtKB/Swiss-Prot (P19686.1)"
     Region          276..465
                     /region_name="HNOBA"
                     /note="Heme NO binding associated; pfam07701"
                     /db_xref="CDD:462234"
     Region          471..642
                     /region_name="Guanylate_cyc"
                     /note="Adenylate and Guanylate cyclase catalytic domain;
                     pfam00211"
                     /db_xref="CDD:425528"
     Site            order(483,485..490,525,527..529,532,594..596,600..601,
                     604..605)
                     /site_type="active"
                     /note="nucleotidyl binding site [active]"
                     /db_xref="CDD:143636"
     Site            order(485,529)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143636"
     Site            order(490,502,505..506,509,513,525..526,582,585,595..598,
                     601)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143636"
     CDS             1..690
                     /gene="Gucy1a1"
                     /gene_synonym="Gucy1a3; SGC"
                     /coded_by="NM_017090.2:138..2210"
                     /db_xref="GeneID:497757"
                     /db_xref="RGD:68436"
ORIGIN      
        1 mfcrkfkdlk itgecpfsll apgqvptepi eevagvsesc qatlptcqef aenaegshpq
       61 rktsrnrvyl htlaesigkl ifpeferlnl alqrtlakhk ikenrnssek edleriiaee
      121 aiaagvpvea lkdslgeelf kicyeedehi lgvvggtlkd flnsfstllk qsshcqeaer
      181 rgrledasil cldkdqdfln vyyffpkrtt alllpgiika aarilyeshv evslmppcfr
      241 sectefvnqp yllysvhvks tkpslspgkp qsslviptsl fcktfpfhfm ldrdlailql
      301 gngirrlvnk rdfqgkpnfe effeiltpki nqtfsgimtm lnmqfvirvr rwdnlvkkss
      361 rvmdlkgqmi yivessailf lgspcvdrle dftgrglyls dipihnalrd vvligeqara
      421 qdglkkrlgk lkatlehahq aleeekkktv dllcsifpse vaqqlwqgqi vqakkfnevt
      481 mlfsdivgft aicsqcsplq vitmlnalyt rfdqqcgeld vykvetigda ycvagglhre
      541 sdthavqial malkmmelsn evmsphgepi kmriglhsgs vfagvvgvkm pryclfgnnv
      601 tlankfescs vprkinvspt tyrllkdcpg fvftprsree lppnfpsdip gichfldayq
      661 hqgpnskpwf qqkdaedgna nflgkasgvd
//
LOCUS       NP_434687                232 aa            linear   ROD 28-APR-2025
DEFINITION  thymidine kinase, cytosolic [Rattus norvegicus].
ACCESSION   NP_434687 XP_001081763
VERSION     NP_434687.1
DBSOURCE    REFSEQ: accession NM_052800.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Mutahir,Z., Clausen,A.R., Andersson,K.M., Wisen,S.M.,
            Munch-Petersen,B. and Piskur,J.
  TITLE     Thymidine kinase 1 regulatory fine-tuning through tetramer
            formation
  JOURNAL   FEBS J 280 (6), 1531-1541 (2013)
   PUBMED   23351158
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Skovgaard,T., Uhlin,U. and Munch-Petersen,B.
  TITLE     Comparative active-site mutation study of human and Caenorhabditis
            elegans thymidine kinase 1
  JOURNAL   FEBS J 279 (10), 1777-1787 (2012)
   PUBMED   22385435
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wang,L. and Eriksson,S.
  TITLE     Tissue specific distribution of pyrimidine deoxynucleoside salvage
            enzymes shed light on the mechanism of mitochondrial DNA depletion
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 29 (4-6), 400-403 (2010)
   PUBMED   20544526
  REMARK    GeneRIF: A cytosolic form of TK2 was identified in all tested
            tissues in addition to mitochondrial TK2. TK1 was detected in liver
            and spleen cytosolic extracts while dCK was found in liver, spleen
            and lung cytosolic extracts.
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Mirzaee,S., Eriksson,S. and Albertioni,F.
  TITLE     Differences in cytosolic and mitochondrial 5'-nucleotidase and
            deoxynucleoside kinase activities in Sprague-Dawley rat and CD-1
            mouse tissues: implication for the toxicity of nucleoside analogs
            in animal models
  JOURNAL   Toxicology 267 (1-3), 159-164 (2010)
   PUBMED   19913594
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Arcot,S.S., Traina-Dorge,V.L. and Deininger,P.L.
  TITLE     The rat thymidine kinase gene 5' region: evolution of a promoter
  JOURNAL   DNA Seq 2 (2), 129-131 (1991)
   PUBMED   1777676
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Murphy,A.J. and Efstratiadis,A.
  TITLE     Cloning vectors for expression of cDNA libraries in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8277-8281 (1987)
   PUBMED   3479791
REFERENCE   8  (residues 1 to 232)
  AUTHORS   Sakai,K., Murata,N. and Yamane,Y.
  TITLE     Effect of copper and cadmium pretreatments on DNA synthesis and
            thymidine kinase activity in the liver of
            dimethylnitrosamine-treated and partially hepatectomized rats
  JOURNAL   Gan 74 (5), 663-670 (1983)
   PUBMED   6642140
REFERENCE   9  (residues 1 to 232)
  AUTHORS   Kozak,C.A. and Ruddle,F.H.
  TITLE     Assignment of the genes for thymidine kinase and galactokinase to
            Mus musculus chromosome 11 and the preferential segregation of this
            chromosome in Chinese hamster/mouse somatic cell hybrids
  JOURNAL   Somatic Cell Genet 3 (2), 121-133 (1977)
   PUBMED   204065
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Herzfeld,A., Rosenoer,V.M. and Raper,S.M.
  TITLE     Glutamate dehydrogenase, alanine aminotransferase, thymidine
            kinase, and arginase in fetal and adult human and rat liver
  JOURNAL   Pediatr Res 10 (12), 960-964 (1976)
   PUBMED   995499
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CK471539.1, M22642.1, CV072953.1, EV770793.1, AW919734.1,
            BF547747.1 and BP495650.1.
            
            On Oct 13, 2007 this sequence version replaced XP_001081763.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ229684.1, EV773050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760476, SAMEA5760494
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q32.2"
     Protein         1..232
                     /product="thymidine kinase, cytosolic"
                     /EC_number="2.7.1.21"
                     /note="thymidine kinase 1, soluble"
                     /calculated_mol_wt=25592
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P04183; propagated from
                     UniProtKB/Swiss-Prot (P27158.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04183; propagated from
                     UniProtKB/Swiss-Prot (P27158.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04183; propagated from
                     UniProtKB/Swiss-Prot (P27158.1)"
     Region          18..197
                     /region_name="TK"
                     /note="Thymidine kinase; cl23762"
                     /db_xref="CDD:451530"
     CDS             1..232
                     /gene="Tk1"
                     /gene_synonym="Tk"
                     /coded_by="NM_052800.1:63..761"
                     /db_xref="GeneID:24834"
                     /db_xref="RGD:621014"
ORIGIN      
        1 msyinlptvl pispsktrgq iqvilgpmfs gkstelmrrv rrfqiaqykc lvikyakdtr
       61 ysnsfsthdr ntmdalpacm lkdvaqealg vavigidegq ffpdivdfce tmantgktvi
      121 vaaldgtfqr kafgsilnlv plaesvvklt avcmecfrea sytkrlglek eveviggadk
      181 yhsvcrlcyf kkssaqtadn kenysvlgqp ieipavrklf apqqilqcns an
//
LOCUS       NP_787040                530 aa            linear   ROD 28-APR-2025
DEFINITION  UDP-glucuronosyltransferase 1A8 precursor [Rattus norvegicus].
ACCESSION   NP_787040 XP_217473 XP_347377
VERSION     NP_787040.2
DBSOURCE    REFSEQ: accession NM_175846.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Bellemare,J., Rouleau,M., Girard,H., Harvey,M. and Guillemette,C.
  TITLE     Alternatively spliced products of the UGT1A gene interact with the
            enzymatically active proteins to inhibit glucuronosyltransferase
            activity in vitro
  JOURNAL   Drug Metab Dispos 38 (10), 1785-1789 (2010)
   PUBMED   20610558
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Rowbotham,S.E., Illingworth,N.A., Daly,A.K., Veal,G.J. and
            Boddy,A.V.
  TITLE     Role of UDP-glucuronosyltransferase isoforms in 13-cis retinoic
            acid metabolism in humans
  JOURNAL   Drug Metab Dispos 38 (7), 1211-1217 (2010)
   PUBMED   20308471
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Brand,W., Boersma,M.G., Bik,H., Hoek-van den Hil,E.F., Vervoort,J.,
            Barron,D., Meinl,W., Glatt,H., Williamson,G., van Bladeren,P.J. and
            Rietjens,I.M.
  TITLE     Phase II metabolism of hesperetin by individual
            UDP-glucuronosyltransferases and sulfotransferases and rat and
            human tissue samples
  JOURNAL   Drug Metab Dispos 38 (4), 617-625 (2010)
   PUBMED   20056724
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Bellemare,J., Rouleau,M., Harvey,M. and Guillemette,C.
  TITLE     Modulation of the human glucuronosyltransferase UGT1A pathway by
            splice isoform polypeptides is mediated through protein-protein
            interactions
  JOURNAL   J Biol Chem 285 (6), 3600-3607 (2010)
   PUBMED   19996319
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Joseph,T.B., Wang,S.W., Liu,X., Kulkarni,K.H., Wang,J., Xu,H. and
            Hu,M.
  TITLE     Disposition of flavonoids via enteric recycling: enzyme stability
            affects characterization of prunetin glucuronidation across
            species, organs, and UGT isoforms
  JOURNAL   Mol Pharm 4 (6), 883-894 (2007)
   PUBMED   18052087
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Zhang,T., Haws,P. and Wu,Q.
  TITLE     Multiple variable first exons: a mechanism for cell- and
            tissue-specific gene regulation
  JOURNAL   Genome Res 14 (1), 79-89 (2004)
   PUBMED   14672974
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Kessler,F.K., Kessler,M.R., Auyeung,D.J. and Ritter,J.K.
  TITLE     Glucuronidation of acetaminophen catalyzed by multiple rat phenol
            UDP-glucuronosyltransferases
  JOURNAL   Drug Metab Dispos 30 (3), 324-330 (2002)
   PUBMED   11854153
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Leung,Y.K. and Ho,J.W.
  TITLE     Induction of UDP-glucuronosyltransferase 1A8 mRNA by
            3-methylcholanthene in rat hepatoma cells
  JOURNAL   Biochem Pharmacol 63 (4), 767-775 (2002)
   PUBMED   11992647
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Emi,Y., Ikushiro,S. and Iyanagi,T.
  TITLE     Drug-responsive and tissue-specific alternative expression of
            multiple first exons in rat UDP-glucuronosyltransferase family 1
            (UGT1) gene complex
  JOURNAL   J Biochem 117 (2), 392-399 (1995)
   PUBMED   7608130
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Sato,H., Koiwai,O., Tanabe,K. and Kashiwamata,S.
  TITLE     Isolation and sequencing of rat liver bilirubin
            UDP-glucuronosyltransferase cDNA: possible alternate splicing of a
            common primary transcript
  JOURNAL   Biochem Biophys Res Commun 169 (1), 260-264 (1990)
   PUBMED   2112380
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY435135.1 and AC120922.4.
            
            On Mar 9, 2006 this sequence version replaced NP_787040.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY435135.1, AF461735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMEA5760383
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..530
                     /product="UDP-glucuronosyltransferase 1A8 precursor"
                     /EC_number="2.4.1.17"
                     /note="UDP-glucuronosyltransferase 1-8; A3; UDPGT; UGT1*8;
                     UGT1.8; UGT1-08; UDP-glucuronosyltransferase 1A8; UDP
                     glycosyltransferase 1 family, polypeptide A8"
                     /calculated_mol_wt=57586
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2481
     mat_peptide     26..530
                     /product="UDP-glucuronosyltransferase 1A8.
                     /id=PRO_0000036022"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64634.1)"
                     /calculated_mol_wt=57586
     Region          26..521
                     /region_name="UDPGT"
                     /note="UDP-glucoronosyl and UDP-glucosyl transferase;
                     pfam00201"
                     /db_xref="CDD:278624"
     Site            order(36..37,39,199,202..203,207,240,306,369,371,373..374,
                     377)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(36,306,369,371,373..374)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            37
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64634.1)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64634.1)"
     Site            430
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64634.1)"
     Site            488..504
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64634.1)"
     CDS             1..530
                     /gene="Ugt1a8"
                     /gene_synonym="UDPGT 1-8; Ugt1; Ugt1a9"
                     /coded_by="NM_175846.2:1..1593"
                     /db_xref="GeneID:301595"
                     /db_xref="RGD:708474"
ORIGIN      
        1 mapsgcppsl plcvclflas gfaqagrllv vpmdgshwft mqmiveklsh rghevvvvip
       61 evswhmgksl nftvktysvs ytledlnyhf kffahnqwkt qevgmfsllk hsgkgffell
      121 fshcrslfkd kklveylkqs sfdavfldpf dvcglilaky fslpsvvfsg gifchyldeg
      181 aqcpsppsyv prilskftdt mtfkervwnh lsymkerafc pyffktavei asevlqtpvt
      241 mrdlfspvsi wmfrtdfvle fprpvmpnmv yigginchqg kplskefeay vnasgehgiv
      301 vfslgsmvse ipekkameia ealgripqtv lwrytgtrps nlakntilvk wlpqndllgh
      361 pkarafiths gshgiyegic ngvpmvmmpl fgdqmdnakr metrgagvtl nvlemtaddl
      421 enalktvinn ksykenimrl sslhkdrpie pldlavfwve yvmrhkgaph lrpaahdltw
      481 yqyhsldvig fllaivltvv fivykscayg crkcfggkgr vkkshkskth
//
LOCUS       NP_113886                631 aa            linear   ROD 28-APR-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit 2 precursor [Rattus norvegicus].
ACCESSION   NP_113886
VERSION     NP_113886.1
DBSOURCE    REFSEQ: accession NM_031698.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Honma,K., Iwao-Koizumi,K., Takeshita,F., Yamamoto,Y., Yoshida,T.,
            Nishio,K., Nagahara,S., Kato,K. and Ochiya,T.
  TITLE     RPN2 gene confers docetaxel resistance in breast cancer
  JOURNAL   Nat Med 14 (9), 939-948 (2008)
   PUBMED   18724378
  REMARK    Erratum:[Nat Med. 2008 Oct;14(10):1128]
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Limaye,A.M., Asangani,I., Bora,N. and Kondaiah,P.
  TITLE     Novel flutamide regulated genes in the rat ventral prostate:
            differential modulation of their expression by castration and
            flutamide treatments
  JOURNAL   Asian J Androl 9 (6), 801-808 (2007)
   PUBMED   17968466
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Farah,C.A., Liazoghli,D., Perreault,S., Desjardins,M., Guimont,A.,
            Anton,A., Lauzon,M., Kreibich,G., Paiement,J. and Leclerc,N.
  TITLE     Interaction of microtubule-associated protein-2 and p63: a new link
            between microtubules and rough endoplasmic reticulum membranes in
            neurons
  JOURNAL   J Biol Chem 280 (10), 9439-9449 (2005)
   PUBMED   15623521
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Kumar,V., Heinemann,F.S. and Ozols,J.
  TITLE     Interleukin-2 induces N-glycosylation in T-cells: characterization
            of human lymphocyte oligosaccharyltransferase
  JOURNAL   Biochem Biophys Res Commun 247 (2), 524-529 (1998)
   PUBMED   9642163
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Schweizer,A., Rohrer,J., Slot,J.W., Geuze,H.J. and Kornfeld,S.
  TITLE     Reassessment of the subcellular localization of p63
  JOURNAL   J Cell Sci 108 (Pt 6), 2477-2485 (1995)
   PUBMED   7673362
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Pirozzi,G., Zhou,Z.M., D'Eustachio,P., Sabatini,D.D. and
            Kreibich,G.
  TITLE     Rat ribophorin II: molecular cloning and chromosomal localization
            of a highly conserved transmembrane glycoprotein of the rough
            endoplasmic reticulum
  JOURNAL   Biochem Biophys Res Commun 176 (3), 1482-1486 (1991)
   PUBMED   1710116
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Dunn,W.A. Jr.
  TITLE     Studies on the mechanisms of autophagy: formation of the autophagic
            vacuole
  JOURNAL   J Cell Biol 110 (6), 1923-1933 (1990)
   PUBMED   2351689
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Kreibich,G., Freienstein,C.M., Pereyra,B.N., Ulrich,B.L. and
            Sabatini,D.D.
  TITLE     Proteins of rough microsomal membranes related to ribosome binding.
            II. Cross-linking of bound ribosomes to specific membrane proteins
            exposed at the binding sites
  JOURNAL   J Cell Biol 77 (2), 488-506 (1978)
   PUBMED   418074
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X55298.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X55298.1, BC060556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q42"
     Protein         1..631
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 2 precursor"
                     /EC_number="2.4.99.18"
                     /note="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 2; RPN-II; ribophorin-2;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase 63 kDa subunit"
                     /calculated_mol_wt=66932
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2148
     Region          9..624
                     /region_name="Ribophorin_II"
                     /note="Oligosaccharyltransferase subunit Ribophorin II;
                     pfam05817"
                     /db_xref="CDD:461749"
     mat_peptide     23..631
                     /product="Dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit 2. /id=PRO_0000022245"
                     /note="propagated from UniProtKB/Swiss-Prot (P25235.2)"
                     /calculated_mol_wt=66932
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P25235.2)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25235.2)"
     Site            572..592
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25235.2)"
     Site            597..617
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25235.2)"
     CDS             1..631
                     /gene="Rpn2"
                     /coded_by="NM_031698.1:10..1905"
                     /db_xref="GeneID:64701"
                     /db_xref="RGD:62075"
ORIGIN      
        1 mappgssavf llaltitast qaltpthylt khdverlkas ldrpftsles afysivglns
       61 lgaqvpdvkk acafiksnld psnvdslfya aqssqvlsgc eisvsnetrd lllaavseds
      121 svaqiyhava alsgfglpla shealgalta rlskeetvla tvqalhtash lsqqadlrni
      181 veeiedlvar ldelggvylq feegleltal fvaatyklmd hvgtepsike dqviqlmnti
      241 fskknfesls eafsvasaaa alsqnryhvp vvvvpegsas dtqeqailrl qvssvlshal
      301 aqaavkleha ksvasratvl qkmpfslvgd vfelnfknvk lpsgyydfsv rvegdnryia
      361 ntvelrvkis tevgitnadl stvdkdqsip pkttrvtypa kakgtfiads hqnfalffql
      421 vdvntgaelt phqtfvrlhn qktgqevvfv aepdnknvhk feldtserki efdsasgtyt
      481 lyliigdatl knpilwnvad vvikfpeeea pstvlsqnlf tpkqeiqhlf repekrpptv
      541 vsntftalil spllllfalw iriganvsnf tfapttiifh lghaamlglm yvywtqlnmf
      601 qtlkylavlg tvtflagnrm laqqavkrta h
//
LOCUS       NP_001008771             342 aa            linear   ROD 28-APR-2025
DEFINITION  methylosome protein WDR77 [Rattus norvegicus].
ACCESSION   NP_001008771 XP_227562
VERSION     NP_001008771.2
DBSOURCE    REFSEQ: accession NM_001008771.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Takai,H., Masuda,K., Sato,T., Sakaguchi,Y., Suzuki,T., Suzuki,T.,
            Koyama-Nasu,R., Nasu-Nishimura,Y., Katou,Y., Ogawa,H.,
            Morishita,Y., Kozuka-Hata,H., Oyama,M., Todo,T., Ino,Y., Mukasa,A.,
            Saito,N., Toyoshima,C., Shirahige,K. and Akiyama,T.
  TITLE     5-Hydroxymethylcytosine plays a critical role in
            glioblastomagenesis by recruiting the CHTOP-methylosome complex
  JOURNAL   Cell Rep 9 (1), 48-60 (2014)
   PUBMED   25284789
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Guderian,G., Peter,C., Wiesner,J., Sickmann,A., Schulze-Osthoff,K.,
            Fischer,U. and Grimmler,M.
  TITLE     RioK1, a new interactor of protein arginine methyltransferase 5
            (PRMT5), competes with pICln for binding and modulates PRMT5
            complex composition and substrate specificity
  JOURNAL   J Biol Chem 286 (3), 1976-1986 (2011)
   PUBMED   21081503
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Vascotto,C., Fantini,D., Romanello,M., Cesaratto,L., Deganuto,M.,
            Leonardi,A., Radicella,J.P., Kelley,M.R., D'Ambrosio,C.,
            Scaloni,A., Quadrifoglio,F. and Tell,G.
  TITLE     APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
            the rRNA quality control process
  JOURNAL   Mol Cell Biol 29 (7), 1834-1854 (2009)
   PUBMED   19188445
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Chari,A., Golas,M.M., Klingenhager,M., Neuenkirchen,N., Sander,B.,
            Englbrecht,C., Sickmann,A., Stark,H. and Fischer,U.
  TITLE     An assembly chaperone collaborates with the SMN complex to generate
            spliceosomal SnRNPs
  JOURNAL   Cell 135 (3), 497-509 (2008)
   PUBMED   18984161
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Peng,Y., Chen,F., Melamed,J., Chiriboga,L., Wei,J., Kong,X.,
            McLeod,M., Li,Y., Li,C.X., Feng,A., Garabedian,M.J., Wang,Z.,
            Roeder,R.G. and Lee,P.
  TITLE     Distinct nuclear and cytoplasmic functions of androgen receptor
            cofactor p44 and association with androgen-independent prostate
            cancer
  JOURNAL   Proc Natl Acad Sci U S A 105 (13), 5236-5241 (2008)
   PUBMED   18356297
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Zhou,L., Wu,H., Lee,P. and Wang,Z.
  TITLE     Roles of the androgen receptor cofactor p44 in the growth of
            prostate epithelial cells
  JOURNAL   J Mol Endocrinol 37 (2), 283-300 (2006)
   PUBMED   17032745
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Hosohata,K., Li,P., Hosohata,Y., Qin,J., Roeder,R.G. and Wang,Z.
  TITLE     Purification and identification of a novel complex which is
            involved in androgen receptor-dependent transcription
  JOURNAL   Mol Cell Biol 23 (19), 7019-7029 (2003)
   PUBMED   12972618
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB581439.1, BC097367.1 and CK842118.1.
            
            On Oct 8, 2005 this sequence version replaced NP_001008771.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ213175.1, FQ226328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..342
                     /product="methylosome protein WDR77"
                     /note="methylosome protein 50; WD repeat-containing
                     protein 77; methylosome protein 50-like"
                     /calculated_mol_wt=36945
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.2;
                     propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          22..75
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          78..116
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          80..319
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          123..162
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          129..165
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..205
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          170..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..250
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          216..250
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          253..293
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          257..292
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          295..330
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4QR85.1)"
     Region          300..333
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..342
                     /gene="Wdr77"
                     /gene_synonym="Ac2-269; MEP-50; RGD1310479"
                     /coded_by="NM_001008771.3:97..1125"
                     /db_xref="GeneID:310769"
                     /db_xref="RGD:1310479"
ORIGIN      
        1 mrkesppplv ppaarewnlp pnapacmerq leaaryrsdg slllgassls grcwagslwf
       61 fkdpsaapne gfcsagvqte agvadltwvg dkgilvasds gavelwelde netlivskfc
      121 kyehddivst vtvlssgtqa vsgskdfcik iwdlaqqmsl nsyrahagqv tcvaasphre
      181 tvflscseds rillwdtrcp kpasqmgcna sgylptslaw hpqqseifvf gdengsvslv
      241 dtknasctls savhsqcvtr lvfsphsvpf laslsedcsl avldssfsev frsrahrdfv
      301 rdatwsplnh sllttvgwdh qvihhvvple plpapgpdsv ve
//
LOCUS       NP_001004241             469 aa            linear   ROD 28-APR-2025
DEFINITION  sorting and assembly machinery component 50 homolog [Rattus
            norvegicus].
ACCESSION   NP_001004241 XP_217005
VERSION     NP_001004241.1
DBSOURCE    REFSEQ: accession NM_001004241.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Edelman,D., Kalia,H., Delio,M., Alani,M., Krishnamurthy,K., Abd,M.,
            Auton,A., Wang,T., Wolkoff,A.W. and Morrow,B.E.
  TITLE     Genetic analysis of nonalcoholic fatty liver disease within a
            Caribbean-Hispanic population
  JOURNAL   Mol Genet Genomic Med 3 (6), 558-569 (2015)
   PUBMED   26740948
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Ott,C., Dorsch,E., Fraunholz,M., Straub,S. and Kozjak-Pavlovic,V.
  TITLE     Detailed analysis of the human mitochondrial contact site complex
            indicate a hierarchy of subunits
  JOURNAL   PLoS One 10 (3), e0120213 (2015)
   PUBMED   25781180
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Hohr,A.I., Straub,S.P., Warscheid,B., Becker,T. and Wiedemann,N.
  TITLE     Assembly of beta-barrel proteins in the mitochondrial outer
            membrane
  JOURNAL   Biochim Biophys Acta 1853 (1), 74-88 (2015)
   PUBMED   25305573
  REMARK    Review article
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Ott,C., Ross,K., Straub,S., Thiede,B., Gotz,M., Goosmann,C.,
            Krischke,M., Mueller,M.J., Krohne,G., Rudel,T. and
            Kozjak-Pavlovic,V.
  TITLE     Sam50 functions in mitochondrial intermembrane space bridging and
            biogenesis of respiratory complexes
  JOURNAL   Mol Cell Biol 32 (6), 1173-1188 (2012)
   PUBMED   22252321
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Zhao,X., Leon,I.R., Bak,S., Mogensen,M., Wrzesinski,K., Hojlund,K.
            and Jensen,O.N.
  TITLE     Phosphoproteome analysis of functional mitochondria isolated from
            resting human muscle reveals extensive phosphorylation of inner
            membrane protein complexes and enzymes
  JOURNAL   Mol Cell Proteomics 10 (1), M110.000299 (2011)
   PUBMED   20833797
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Humphries,A.D., Streimann,I.C., Stojanovski,D., Johnston,A.J.,
            Yano,M., Hoogenraad,N.J. and Ryan,M.T.
  TITLE     Dissection of the mitochondrial import and assembly pathway for
            human Tom40
  JOURNAL   J Biol Chem 280 (12), 11535-11543 (2005)
   PUBMED   15644312
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Da Cruz,S., Xenarios,I., Langridge,J., Vilbois,F., Parone,P.A. and
            Martinou,J.C.
  TITLE     Proteomic analysis of the mouse liver mitochondrial inner membrane
  JOURNAL   J Biol Chem 278 (42), 41566-41571 (2003)
   PUBMED   12865426
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC079302.1.
            
            On Sep 10, 2004 this sequence version replaced XP_217005.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC079302.1, SRR8487227.88076.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..469
                     /product="sorting and assembly machinery component 50
                     homolog"
                     /note="sorting and assembly machinery component 50 homolog
                     A"
                     /calculated_mol_wt=51829
     Region          46..124
                     /region_name="POTRA"
                     /note="Surface antigen variable number repeat; pfam07244"
                     /db_xref="CDD:462121"
     Region          151..463
                     /region_name="Omp85"
                     /note="Omp85 superfamily domain; pfam01103"
                     /db_xref="CDD:460065"
     Site            255
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y512; propagated from
                     UniProtKB/Swiss-Prot (Q6AXV4.1)"
     CDS             1..469
                     /gene="Samm50"
                     /coded_by="NM_001004241.1:63..1472"
                     /db_xref="GeneID:300111"
                     /db_xref="RGD:1303219"
ORIGIN      
        1 mgtvharsle plpssgtdfg algeeaefve vepeakqeil enkdvvvqhv hfdglertkd
       61 diiiceigev fkaknlievm rrshearekl lrlgifrqvd vlidtchged alpngldvtf
      121 evtelrrltg syntmvgnne gsmvlglklp nllgraekvt fqfsygtket syglsffkpq
      181 pgnfeknfsv nlykvtgqfp wsslretdrg vsaeysfplc ktshtvkweg vwrelgclar
      241 tasfavrkes ghslksslsh amvidsrnss ilprrgallk vnqelagytg gdvsfikedf
      301 elqlnkplvl dsvfstslwg gmlvpigdkl ssiadrfylg gptsvrgfsm hsigpqsegd
      361 ylggeaywag glhlytplpf rpgqggfgel frthfflnag nlcnlnygeg prahirklae
      421 cirwsygagi vlrlgniarl elnycipmgv qrgdricdgv qfgagirfl
//
LOCUS       NP_001005901             953 aa            linear   ROD 28-APR-2025
DEFINITION  E3 ubiquitin-protein ligase MIB2 [Rattus norvegicus].
ACCESSION   NP_001005901 XP_001052967 XP_001052968 XP_002726712 XP_002729626
VERSION     NP_001005901.2
DBSOURCE    REFSEQ: accession NM_001005901.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Zemoura,K., Trumpler,C. and Benke,D.
  TITLE     Lys-63-linked Ubiquitination of gamma-Aminobutyric Acid (GABA),
            Type B1, at Multiple Sites by the E3 Ligase Mind Bomb-2 Targets
            GABAB Receptors to Lysosomal Degradation
  JOURNAL   J Biol Chem 291 (41), 21682-21693 (2016)
   PUBMED   27573246
  REMARK    GeneRIF: sustained activation of glutamate receptors, a condition
            occurring in brain ischemia that down-regulates GABAB receptors,
            considerably increased the expression of MIB2 and Lys-63-linked
            ubiquitination of GABAB receptors. Interfering with Lys-63-linked
            ubiquitination by overexpressing ubiquitin mutants or GABAB1
            mutants deficient in Lys-63-linked ubiquitination prevented
            glutamate-induced down-regulation of the receptors.
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Jurd,R., Thornton,C., Wang,J., Luong,K., Phamluong,K., Kharazia,V.,
            Gibb,S.L. and Ron,D.
  TITLE     Mind bomb-2 is an E3 ligase that ubiquitinates the
            N-methyl-D-aspartate receptor NR2B subunit in a
            phosphorylation-dependent manner
  JOURNAL   J Biol Chem 283 (1), 301-310 (2008)
   PUBMED   17962190
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Koo,B.K., Yoon,K.J., Yoo,K.W., Lim,H.S., Song,R., So,J.H., Kim,C.H.
            and Kong,Y.Y.
  TITLE     Mind bomb-2 is an E3 ligase for Notch ligand
  JOURNAL   J Biol Chem 280 (23), 22335-22342 (2005)
   PUBMED   15824097
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On or before Sep 1, 2012 this sequence version replaced
            XP_002726712.2, XP_001052968.2, XP_002729626.2, XP_001052967.2,
            NP_001005901.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.30683.1,
                                           SRR26643288.25153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..953
                     /product="E3 ubiquitin-protein ligase MIB2"
                     /EC_number="2.3.2.27"
                     /note="RBSC-skeletrophin/dystrophin-like polypeptide; mind
                     bomb homolog 2; mindbomb E3 ubiquitin protein ligase 2;
                     RING-type E3 ubiquitin transferase MIB2"
                     /calculated_mol_wt=103733
     Region          12..78
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          89..133
                     /region_name="ZZ_Mind_bomb"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     Drosophila Mind bomb (D-mib) and related proteins. The ZZ
                     motif coordinates two zinc ions and most likely
                     participates in ligand binding or molecular scaffolding.
                     Mind bomb is an E3 ubiqitin ligase that has...; cd02339"
                     /db_xref="CDD:239079"
     Site            order(91,94,106,109,115,118,124,128)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239079"
     Site            order(91,94,115,118)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239079"
     Site            order(92,103,105,111,113)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239079"
     Site            order(104,119,130,133)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239079"
     Site            order(106,109,124,128)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239079"
     Region          160..224
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          257..318
                     /region_name="SH3_15"
                     /note="Mind bomb SH3 repeat domain; pfam18346"
                     /db_xref="CDD:465720"
     Region          324..388
                     /region_name="SH3_15"
                     /note="Mind bomb SH3 repeat domain; pfam18346"
                     /db_xref="CDD:465720"
     Region          395..664
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          460..489
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          461..491
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(462,466..467,470..472,474..475,479,482,491,493,495,
                     499..500,503..505,507..508,512,515,524,526,528,532..533,
                     536..538,540..541,545,548,557)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          493..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          493..522
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          526..557
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..555
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          559..593
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          559..591
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          595..624
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          596..627
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(597,601..602,605..607,609..610,615,618,627,629,631,
                     635..636,639..641,643..644,648,651,661,663,665,669..670,
                     673..675,677..678,682,685,694)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          629..661
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          629..659
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          634..710
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          663..694
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          663..692
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          696..724
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          765..794
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68LP1.2)"
     Region          828..865
                     /region_name="RING-HC_MIB2_rpt1"
                     /note="first RING finger, HC subclass, found in mind bomb
                     2 (MIB2) and similar proteins; cd16726"
                     /db_xref="CDD:438386"
     Region          903..953
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(909,912,923,925,928,931,938,941)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438111"
     CDS             1..953
                     /gene="Mib2"
                     /coded_by="NM_001005901.2:864..3725"
                     /db_xref="GeneID:474147"
                     /db_xref="RGD:1359469"
ORIGIN      
        1 mdldphagvq vgmrvvrgmd wkwgqqdgge ggvgtvvelg rhgspstpdr tvvvqwdqgt
       61 rtnyragyqg ahdlllydna qigirhpnii cdcckkhglr gmrwkcrvcf dydlctqcym
      121 hnkhdlthaf eryetshsrp vtlsprqglp riplrgifqg akvvrgpdwe wgsqdggegk
      181 tgrvvdirgw dvetgrsvas vtwadgttnv yrvghkgkvd lkcvgeaagg fyykehlpkl
      241 gkpaelqrrv sadgqpfqrg dkvkclldtd vlrdmqeghg gwnprmaemg tvhritdrgd
      301 vrvqfnhetr wtfhpgaltk hnsfwvgdvv rviddldtvk rlqaghgewt ddmapalgrv
      361 gkvvkvfgdg nlrvavggqr wtfspaclva crpeedanlg vaerarenks slsvaldklr
      421 tqksdpehpg rlvveaalgn varaldllrr hpeqvdtknq grtalqvaay lgqvelvrll
      481 lqarasvdll deegntalhy tamgnqpeat rlllsagcgv daqngtrsta lhvavqrgfl
      541 evvkilcehg cdvnlpdaha dtplhsaisa gagassivev ltevpgidvt atnsqgftll
      601 hhaslkghvl avrkilarar qlvdakkedg ftalhlaaln nhrevaqvli regrcdvnvr
      661 nrklqsplhl avqqahlglv pllvdagcnv ntedeegdta lhvalqrhql lplvadragg
      721 dpgplqllsr lqasglpgst eltvgaavac flalegadvs yanhrgrspl dlategrvlk
      781 alqgcaqrfr erqagggggv ppgprhvlst pntvtnlhvs gtagpeaaec lvcselallv
      841 lfspcqhrtv ceecarrmkk circqviisk klrpdgsevv naiqvpgppr qlveelqsry
      901 rqmeeritcp icidshirlv fqcghgacap cgaalnacpi crqpirdriq ifv
//
LOCUS       NP_068615                273 aa            linear   ROD 28-APR-2025
DEFINITION  kit ligand isoform 1 precursor [Rattus norvegicus].
ACCESSION   NP_068615
VERSION     NP_068615.1
DBSOURCE    REFSEQ: accession NM_021843.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Zheng,H., Liu,Y.J., Chen,Z.C. and Fan,G.Q.
  TITLE     miR-222 regulates cell growth, apoptosis, and autophagy of
            interstitial cells of Cajal isolated from slow transit constipation
            rats by targeting c-kit
  JOURNAL   Indian J Gastroenterol 40 (2), 198-208 (2021)
   PUBMED   33792838
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Sudo,H.
  TITLE     Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation
            under a Tau Deficiency in Mammary Epithelial Cells
  JOURNAL   Int J Mol Sci 19 (9), 2488 (2018)
   PUBMED   30142893
  REMARK    GeneRIF: The data suggest that microtubule acetylation upregulates
            KL1 and induces more aneuploidy if tau is deficient.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Zhang,W., Wu,T., Zhang,C., Luo,L., Xie,M. and Huang,H.
  TITLE     Cadmium exposure in newborn rats ovary induces developmental
            disorders of primordial follicles and the differential expression
            of SCF/c-kit gene
  JOURNAL   Toxicol Lett 280, 20-28 (2017)
   PUBMED   28801138
  REMARK    GeneRIF: It was concluded that the exposure of cadimium on newborn
            rats ovaries could inhibit follicle development. SCF/c-kit system
            might mediate follicle development damage caused by cadmium, which
            is associated with DNA hypomethylation of SCF/c-kit promoter region
            may be worthy of further study.
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Qin,Q., Liu,J., Ma,Y., Wang,Y., Zhang,F., Gao,S. and Dong,L.
  TITLE     Aberrant expressions of stem cell factor/c-KIT in rat testis with
            varicocele
  JOURNAL   J Formos Med Assoc 116 (7), 542-548 (2017)
   PUBMED   27707610
  REMARK    GeneRIF: the SCF/c-KIT system is aberrantly expressed in
            varicocele(VC) testis, which could be involved in male infertility
            caused by VC.
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Lee,J.H., Lee,M., Ahn,C., Kang,H.Y., Tran,D.N. and Jeung,E.B.
  TITLE     Parabens Accelerate Ovarian Dysfunction in a 4-Vinylcyclohexene
            Diepoxide-Induced Ovarian Failure Model
  JOURNAL   Int J Environ Res Public Health 14 (2), 161 (2017)
   PUBMED   28208728
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ploemacher,R.E., van Soest,P.L., Boudewijn,A. and Neben,S.
  TITLE     Interleukin-12 enhances interleukin-3 dependent multilineage
            hematopoietic colony formation stimulated by interleukin-11 or
            steel factor
  JOURNAL   Leukemia 7 (9), 1374-1380 (1993)
   PUBMED   7690439
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Tsuji,K., Lyman,S.D., Sudo,T., Clark,S.C. and Ogawa,M.
  TITLE     Enhancement of murine hematopoiesis by synergistic interactions
            between steel factor (ligand for c-kit), interleukin-11, and other
            early acting factors in culture
  JOURNAL   Blood 79 (11), 2855-2860 (1992)
   PUBMED   1375116
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Lu,H.S., Clogston,C.L., Wypych,J., Fausset,P.R., Lauren,S.,
            Mendiaz,E.A., Zsebo,K.M. and Langley,K.E.
  TITLE     Amino acid sequence and post-translational modification of stem
            cell factor isolated from buffalo rat liver cell-conditioned medium
  JOURNAL   J Biol Chem 266 (13), 8102-8107 (1991)
   PUBMED   1708771
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Martin,F.H., Suggs,S.V., Langley,K.E., Lu,H.S., Ting,J.,
            Okino,K.H., Morris,C.F., McNiece,I.K., Jacobsen,F.W., Mendiaz,E.A.
            et al.
  TITLE     Primary structure and functional expression of rat and human stem
            cell factor DNAs
  JOURNAL   Cell 63 (1), 203-211 (1990)
   PUBMED   2208279
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Zsebo,K.M., Wypych,J., McNiece,I.K., Lu,H.S., Smith,K.A.,
            Karkare,S.B., Sachdev,R.K., Yuschenkoff,V.N., Birkett,N.C.,
            Williams,L.R. et al.
  TITLE     Identification, purification, and biological characterization of
            hematopoietic stem cell factor from buffalo rat liver--conditioned
            medium
  JOURNAL   Cell 63 (1), 195-201 (1990)
   PUBMED   2208278
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000007.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and it encodes the longer protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.28270.1,
                                           SRR26643288.29727.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..273
                     /product="kit ligand isoform 1 precursor"
                     /EC_number="3.2.1.31"
                     /note="mast cell growth factor; C-kit ligand;
                     hematopoietic growth factor KL; stem cell factor KL-1;
                     steel factor/kit ligand"
                     /calculated_mol_wt=27721
     Region          1..273
                     /region_name="SCF"
                     /note="Stem cell factor; pfam02404"
                     /db_xref="CDD:396808"
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3010
     mat_peptide     26..273
                     /product="Kit ligand. /id=PRO_0000031917"
                     /note="propagated from UniProtKB/Swiss-Prot (P21581.2)"
                     /calculated_mol_wt=27721
     Site            26
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial.
                     /evidence=ECO:0000269|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            97
                     /site_type="other"
                     /note="Not glycosylated.
                     /evidence=ECO:0000269|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            167
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000305|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            168
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            180
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:1708771; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Region          190..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21581.2)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21581.2)"
     Site            215..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21581.2)"
     CDS             1..273
                     /gene="Kitlg"
                     /gene_synonym="Kitl; Mgf; SCF"
                     /coded_by="NM_021843.4:175..996"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:60427"
                     /db_xref="RGD:3086"
ORIGIN      
        1 mkktqtwiit ciylqlllfn plvktqeicr npvtdnvkdi tklvanlpnd ymitlnyvag
       61 mdvlpshcwl rdmvthlsvs lttlldkfsn iseglsnysi idklgkivdd lvacmeenap
      121 knvkeslkkp etrnftpeef fsifnrsida fkdfmvasdt sdcvlsstlg pekdsrvsvt
      181 kpfmlppvaa sslrndssss nrkaaksped pglqwtamal palislvigf afgalywkkk
      241 qssltraven iqineednei smlqqkeref qev
//
LOCUS       NP_001093971             825 aa            linear   ROD 28-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 16 [Rattus norvegicus].
ACCESSION   NP_001093971 XP_001066902 XP_213676
VERSION     NP_001093971.1
DBSOURCE    REFSEQ: accession NM_001100501.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Belle,J.I. and Nijnik,A.
  TITLE     H2A-DUBbing the mammalian epigenome: expanding frontiers for
            histone H2A deubiquitinating enzymes in cell biology and physiology
  JOURNAL   Int J Biochem Cell Biol 50, 161-174 (2014)
   PUBMED   24647359
  REMARK    Review article
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Panier,S. and Durocher,D.
  TITLE     Push back to respond better: regulatory inhibition of the DNA
            double-strand break response
  JOURNAL   Nat Rev Mol Cell Biol 14 (10), 661-672 (2013)
   PUBMED   24002223
  REMARK    Review article
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Frangini,A., Sjoberg,M., Roman-Trufero,M., Dharmalingam,G.,
            Haberle,V., Bartke,T., Lenhard,B., Malumbres,M., Vidal,M. and
            Dillon,N.
  TITLE     The aurora B kinase and the polycomb protein ring1B combine to
            regulate active promoters in quiescent lymphocytes
  JOURNAL   Mol Cell 51 (5), 647-661 (2013)
   PUBMED   24034696
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Shanbhag,N.M., Rafalska-Metcalf,I.U., Balane-Bolivar,C.,
            Janicki,S.M. and Greenberg,R.A.
  TITLE     ATM-dependent chromatin changes silence transcription in cis to DNA
            double-strand breaks
  JOURNAL   Cell 141 (6), 970-981 (2010)
   PUBMED   20550933
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Joo,H.Y., Zhai,L., Yang,C., Nie,S., Erdjument-Bromage,H.,
            Tempst,P., Chang,C. and Wang,H.
  TITLE     Regulation of cell cycle progression and gene expression by H2A
            deubiquitination
  JOURNAL   Nature 449 (7165), 1068-1072 (2007)
   PUBMED   17914355
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Pai,M.T., Tzeng,S.R., Kovacs,J.J., Keaton,M.A., Li,S.S., Yao,T.P.
            and Zhou,P.
  TITLE     Solution structure of the Ubp-M BUZ domain, a highly specific
            protein module that recognizes the C-terminal tail of free
            ubiquitin
  JOURNAL   J Mol Biol 370 (2), 290-302 (2007)
   PUBMED   17512543
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ205918.1, BC112386.1, CV112036.1, BC087705.1 and BI282215.1.
            
            On or before Oct 25, 2008 this sequence version replaced
            XP_213676.3, XP_001066902.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132261,
                              SAMD00132262 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="11"
                     /map="11q11"
     Protein         1..825
                     /product="ubiquitin carboxyl-terminal hydrolase 16"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin thiolesterase 16; ubiquitin specific
                     protease 16; ubiquitin thioesterase 16; deubiquitinating
                     enzyme 16; ubiquitin-specific-processing protease 16"
                     /calculated_mol_wt=93560
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ09.2)"
     Region          48..122
                     /region_name="zf-UBP"
                     /note="Zn-finger in ubiquitin-hydrolases and other
                     protein; pfam02148"
                     /db_xref="CDD:460464"
     Region          <161..823
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y5T5; propagated from
                     UniProtKB/Swiss-Prot (Q2KJ09.2)"
     Region          195..>400
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     Region          391..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ09.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q2KJ09.2)"
     Region          525..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KJ09.2)"
     Region          <624..822
                     /region_name="Peptidase_C19K"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02667"
                     /db_xref="CDD:239132"
     CDS             1..825
                     /gene="Usp16"
                     /coded_by="NM_001100501.1:144..2621"
                     /db_xref="GeneID:288306"
                     /db_xref="RGD:1307192"
ORIGIN      
        1 mgkkrtkgks vpekassest epmcrhlrkg leqgnlkkal vnvewnicqd cktdnkvkdk
       61 seeeaedpsv wlclkcghqg cgrdsqeqha lkhyttprse phylvlsldn wsvwcykcde
      121 eikycssnrl gqvvdyvrkq agritskpek nnghielenk klekeskneq ereksesmak
      181 enipldsasq itvkglsnlg ntcffnavmq nlsqtpvlre llkevkmsgt ivkieppdla
      241 lteplevnle ppgpltlams qflnemqenk krivtpkelf sqvckkatrf kgyqqqdsqe
      301 llrylldgmr aeehqrvskg ilkafgnste kldeevknkv kdyekkkaip sfvdrifgge
      361 ltstimcddc rtvslvhesf ldlslpvldd qsgkknindk nvkktmeeed kdseeekdds
      421 ymktrsdvps gtskhtqkka kkqakkqakn qrrqqkiqer flhfneictt nytedndhea
      481 etalpgegev dtefnrgsqe eltqtelcan qkdvngqeem iesaaderkc pehpevksvs
      541 tesdlgslts apecprdlng afleertsge lditnglknl tlnaavdpde isieilndsh
      601 spalkvyevm nedpetafct lanreafstd ecsiqhclyq ftrneklqda nkllcevctr
      661 rqcngpkani kgerkhvytn akkqmlvsla ppvltlhlkr fqqagfnlrk vnkhikfpei
      721 ldlapfctlk cknvaeestr vlyslygvve hsgtmrsghy tayakertas chlsnlvlhg
      781 dipqdcemes tkgqwfhisd thvqavpitk vlnsqayllf yeril
//
LOCUS       NP_958827                531 aa            linear   ROD 28-APR-2025
DEFINITION  UDP-glucuronosyltransferase 1A3 precursor [Rattus norvegicus].
ACCESSION   NP_958827
VERSION     NP_958827.1
DBSOURCE    REFSEQ: accession NM_201424.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Tian,H., Ou,J., Strom,S.C. and Venkataramanan,R.
  TITLE     Activity and expression of various isoforms of uridine diphosphate
            glucuronosyltransferase are differentially regulated during hepatic
            regeneration in rats
  JOURNAL   Pharm Res 22 (12), 2007-2015 (2005)
   PUBMED   16222444
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Mackenzie,P.I., Bock,K.W., Burchell,B., Guillemette,C.,
            Ikushiro,S., Iyanagi,T., Miners,J.O., Owens,I.S. and Nebert,D.W.
  TITLE     Nomenclature update for the mammalian UDP glycosyltransferase (UGT)
            gene superfamily
  JOURNAL   Pharmacogenet Genomics 15 (10), 677-685 (2005)
   PUBMED   16141793
  REMARK    Review article
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Zhang,T., Haws,P. and Wu,Q.
  TITLE     Multiple variable first exons: a mechanism for cell- and
            tissue-specific gene regulation
  JOURNAL   Genome Res 14 (1), 79-89 (2004)
   PUBMED   14672974
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Emi,Y., Ikushiro,S. and Iyanagi,T.
  TITLE     Drug-responsive and tissue-specific alternative expression of
            multiple first exons in rat UDP-glucuronosyltransferase family 1
            (UGT1) gene complex
  JOURNAL   J Biochem 117 (2), 392-399 (1995)
   PUBMED   7608130
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Sato,H., Koiwai,O., Tanabe,K. and Kashiwamata,S.
  TITLE     Isolation and sequencing of rat liver bilirubin
            UDP-glucuronosyltransferase cDNA: possible alternate splicing of a
            common primary transcript
  JOURNAL   Biochem Biophys Res Commun 169 (1), 260-264 (1990)
   PUBMED   2112380
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY435131.1 and AC120922.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY435131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q35"
     Protein         1..531
                     /product="UDP-glucuronosyltransferase 1A3 precursor"
                     /EC_number="2.4.1.17"
                     /note="UDP-glucuronosyltransferase 1-3; B3; UDPGT; UGT1*3;
                     UGT1.3; UGT1-03; UDP glycosyltransferase 1 family
                     polypeptide A4; UDP-glucuronosyltransferase 1A3"
                     /calculated_mol_wt=57571
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2672
     mat_peptide     26..531
                     /product="UDP-glucuronosyltransferase 1A3.
                     /id=PRO_0000036014"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64637.1)"
                     /calculated_mol_wt=57571
     Region          26..522
                     /region_name="UDPGT"
                     /note="UDP-glucoronosyl and UDP-glucosyl transferase;
                     pfam00201"
                     /db_xref="CDD:278624"
     Site            order(36..37,39,200,203..204,208,249,307,370,372,374..375,
                     378)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(36,307,370,372,374..375)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            37
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64637.1)"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64637.1)"
     Site            293
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64637.1)"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q64637.1)"
     Site            489..505
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q64637.1)"
     CDS             1..531
                     /gene="Ugt1a3"
                     /gene_synonym="UDPGT 1-3; Ugt1; Ugt1a4"
                     /coded_by="NM_201424.2:1..1596"
                     /db_xref="GeneID:396551"
                     /db_xref="RGD:1549728"
ORIGIN      
        1 mgiqgflqkl sglllllcal pwaeggkvlv fpmegshwls mrdvvrelha rghqavvlap
       61 evtvhikeed fftlqtypvp ytkeeyrhhl lghlqnffet efslklvlqr maavnnvstf
      121 yvrscrgllh ntaliqslns ssfdvvltdp ffpcgavlam ylrvpavffl qsmlcelefe
      181 atnspnpssy iprlltlnsd hmsfldrvkn mlypvpwmyl chvnygslar lasdllqrev
      241 svveilrhas vwllrkdfvf yyprpfmpnm vfiggincan rkplsqefea yvnasgehgi
      301 vvfslgsmvs eipekkamei aealgripqt vlwrytgtrp snlakntilv kwlpqndllg
      361 hpkarafith sgshgiyegi cngvpmvmmp lfgdqmdnak rmetrgagvt lnvlemtadd
      421 lenalktvin nksykenimr lsslhkdrpi epldlavfwv eyvmrhkgap hlrpaahdlt
      481 wyqyhsldvi gfllaivltv vfivykscay gcrkcfggkg rvkkshkskt h
//
LOCUS       NP_112328                393 aa            linear   ROD 28-APR-2025
DEFINITION  fasciculation and elongation protein zeta-1 [Rattus norvegicus].
ACCESSION   NP_112328
VERSION     NP_112328.1
DBSOURCE    REFSEQ: accession NM_031066.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Chua,J.Y., Ng,S.J., Yagensky,O., Wanker,E.E. and Chua,J.J.E.
  TITLE     FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon and
            Dendrite Development
  JOURNAL   eNeuro 8 (2) (2021)
   PUBMED   33771901
  REMARK    GeneRIF: FEZ1 Forms Complexes with CRMP1 and DCC to Regulate Axon
            and Dendrite Development.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Gunaseelan,S., Wang,Z., Tong,V.K.J., Ming,S.W.S., Razar,R.B.B.A.,
            Srimasorn,S., Ong,W.Y., Lim,K.L. and Chua,J.J.E.
  TITLE     Loss of FEZ1, a gene deleted in Jacobsen syndrome, causes
            locomotion defects and early mortality by impairing motor neuron
            development
  JOURNAL   Hum Mol Genet 30 (1), 5-20 (2021)
   PUBMED   33395696
  REMARK    GeneRIF: Loss of FEZ1, a gene deleted in Jacobsen syndrome, causes
            locomotion defects and early mortality by impairing motor neuron
            development.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Zhang,Y., Shi,Q., Li,X. and Xia,C.
  TITLE     Fasciculation and Elongation Protein Zeta-1 Expression in Reactive
            Astrocytes in a Rat Model of Frontal Lobe Injury
  JOURNAL   J Neuropathol Exp Neurol 79 (2), 194-208 (2020)
   PUBMED   31774489
  REMARK    GeneRIF: Results indicate that astrocytic FEZ1 and
            glutamate-glutamine cycle dysfunction may be involved in the
            pathogenesis of depression after frontal lobe injury.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Butkevich,E., Hartig,W., Nikolov,M., Erck,C., Grosche,J.,
            Urlaub,H., Schmidt,C.F., Klopfenstein,D.R. and Chua,J.J.
  TITLE     Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases
            regulates its function in presynaptic protein trafficking
  JOURNAL   Sci Rep 6, 26965 (2016)
   PUBMED   27247180
  REMARK    GeneRIF: Phosphorylation of FEZ1 by MARK regulates its function in
            presynaptic protein trafficking.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Lin,M.Y. and Sheng,Z.H.
  TITLE     Regulation of mitochondrial transport in neurons
  JOURNAL   Exp Cell Res 334 (1), 35-44 (2015)
   PUBMED   25612908
  REMARK    Review article
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Lee,S., Walker,C.L., Karten,B., Kuny,S.L., Tennese,A.A.,
            O'Neill,M.A. and Wevrick,R.
  TITLE     Essential role for the Prader-Willi syndrome protein necdin in
            axonal outgrowth
  JOURNAL   Hum Mol Genet 14 (5), 627-637 (2005)
   PUBMED   15649943
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Okumura,F., Hatakeyama,S., Matsumoto,M., Kamura,T. and
            Nakayama,K.I.
  TITLE     Functional regulation of FEZ1 by the U-box-type ubiquitin ligase
            E4B contributes to neuritogenesis
  JOURNAL   J Biol Chem 279 (51), 53533-53543 (2004)
   PUBMED   15466860
  REMARK    GeneRIF: E4B serves as a ubiquitin ligase for FEZ1 and thereby
            regulates its function but not its degradation
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Honda,A., Miyoshi,K., Baba,K., Taniguchi,M., Koyama,Y., Kuroda,S.,
            Katayama,T. and Tohyama,M.
  TITLE     Expression of fasciculation and elongation protein zeta-1 (FEZ1) in
            the developing rat brain
  JOURNAL   Brain Res Mol Brain Res 122 (1), 89-92 (2004)
   PUBMED   14992819
  REMARK    GeneRIF: FEZ1 showed high levels of expression, especially in
            developing hippocampal neurons.
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Miyoshi,K., Honda,A., Baba,K., Taniguchi,M., Oono,K., Fujita,T.,
            Kuroda,S., Katayama,T. and Tohyama,M.
  TITLE     Disrupted-In-Schizophrenia 1, a candidate gene for schizophrenia,
            participates in neurite outgrowth
  JOURNAL   Mol Psychiatry 8 (7), 685-694 (2003)
   PUBMED   12874605
  REMARK    GeneRIF: DISC1 participates in neurite outgrowth through its
            interaction with FEZ1.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Kuroda,S., Nakagawa,N., Tokunaga,C., Tatematsu,K. and Tanizawa,K.
  TITLE     Mammalian homologue of the Caenorhabditis elegans UNC-76 protein
            involved in axonal outgrowth is a protein kinase C zeta-interacting
            protein
  JOURNAL   J Cell Biol 144 (3), 403-411 (1999)
   PUBMED   9971736
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U63740.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U63740.1, BC087740.1 [ECO:0000332]
            RNAseq introns              :: single sample supp
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